# HG changeset patch # User proteore # Date 1549633564 18000 # Node ID 1e856941a888164153c52fc55df01b3575206669 planemo upload commit 8de59a5dbf9206fa3d9f7a1c07e79ccb792b3e3f-dirty diff -r 000000000000 -r 1e856941a888 README.rst --- /dev/null Thu Jan 01 00:00:00 1970 +0000 +++ b/README.rst Fri Feb 08 08:46:04 2019 -0500 @@ -0,0 +1,28 @@ +Wrapper for Protein Features tool +================================= + +**Authors** + +David Christiany, Lisa Peru, T.P. Lien Nguyen, Florence Combes, Yves Vandenbrouck CEA, INSERM, CNRS, Grenoble-Alpes University, BIG Institute, FR + +Sandra Dérozier, Olivier Rué, Christophe Caron, Valentin Loux INRA, Paris-Saclay University, MAIAGE Unit, Migale Bioinformatics platform + +This work has been partially funded through the French National Agency for Research (ANR) IFB project. + +Contact support@proteore.org for any questions or concerns about the Galaxy implementation of this tool. + +--------------------------------- + +This tool add annotation (protein features) from UniProt database (knowledge base on mouse proteins) to your protein IDs list. + +**Input** + +Input can be a file containing multiple fields but with **at least one column of Uniprot accession number**. If your input file contains other type of IDs, please use the ID_Converter tool. + +**Databases** + +Annotations have been retrieved from the UniProt API. + +**Outputs** + +The output is a tabular file. The initial columns are kept and columns are be added according to which annotation you have selected. \ No newline at end of file diff -r 000000000000 -r 1e856941a888 add_protein_features_mouse.R --- /dev/null Thu Jan 01 00:00:00 1970 +0000 +++ b/add_protein_features_mouse.R Fri Feb 08 08:46:04 2019 -0500 @@ -0,0 +1,186 @@ +# Read file and return file content as data.frame +order_columns <- function (df,ncol,file){ + if (ncol==1){ #already at the right position + return (df) + } else { + df = df[,c(2:ncol,1,(ncol+1):dim.data.frame(df)[2])] + } + return (df) +} + +get_list_from_cp <-function(list){ + list = strsplit(list, "[ \t\n]+")[[1]] + list = gsub("NA","",list) + list = list[list != ""] #remove empty entry + list = gsub("-.+", "", list) #Remove isoform accession number (e.g. "-2") + return(list) +} + +check_ids <- function(vector,type) { + uniprot_pattern = "^([OPQ][0-9][A-Z0-9]{3}[0-9]|[A-NR-Z][0-9]([A-Z][A-Z0-9]{2}[0-9]){1,2})$" + entrez_id = "^([0-9]+|[A-Z]{1,2}_[0-9]+|[A-Z]{1,2}_[A-Z]{1,4}[0-9]+)$" + if (type == "entrez") + return(grepl(entrez_id,vector)) + else if (type == "uniprot") { + return(grepl(uniprot_pattern,vector)) + } +} + +get_args <- function(){ + + ## Collect arguments + args <- commandArgs(TRUE) + + ## Default setting when no arguments passed + if(length(args) < 1) { + args <- c("--help") + } + + ## Help section + if("--help" %in% args) { + cat("Selection and Annotation HPA + Arguments: + --inputtype: type of input (list of id or filename) + --input: input + --uniprot_file: path to uniprot reference file + --column: the column number which you would like to apply... + --header: true/false if your file contains a header + --pc_features: IsoPoint,SeqLength,MW + --output: text output filename \n") + + q(save="no") + } + + parseArgs <- function(x) strsplit(sub("^--", "", x), "=") + argsDF <- as.data.frame(do.call("rbind", parseArgs(args))) + args <- as.list(as.character(argsDF$V2)) + names(args) <- argsDF$V1 + + return(args) +} + +str2bool <- function(x){ + if (any(is.element(c("t","true"),tolower(x)))){ + return (TRUE) + }else if (any(is.element(c("f","false"),tolower(x)))){ + return (FALSE) + }else{ + return(NULL) + } +} + +#take data frame, return data frame +split_ids_per_line <- function(line,ncol){ + + #print (line) + header = colnames(line) + line[ncol] = gsub("[[:blank:]]|\u00A0","",line[ncol]) + + if (length(unlist(strsplit(as.character(line[ncol]),";")))>1) { + if (length(line)==1 ) { + lines = as.data.frame(unlist(strsplit(as.character(line[ncol]),";")),stringsAsFactors = F) + } else { + if (ncol==1) { #first column + lines = suppressWarnings(cbind(unlist(strsplit(as.character(line[ncol]),";")), line[2:length(line)])) + } else if (ncol==length(line)) { #last column + lines = suppressWarnings(cbind(line[1:ncol-1],unlist(strsplit(as.character(line[ncol]),";")))) + } else { + lines = suppressWarnings(cbind(line[1:ncol-1], unlist(strsplit(as.character(line[ncol]),";"),use.names = F), line[(ncol+1):length(line)])) + } + } + colnames(lines)=header + return(lines) + } else { + return(line) + } +} + +#create new lines if there's more than one id per cell in the columns in order to have only one id per line +one_id_one_line <-function(tab,ncol){ + + if (ncol(tab)>1){ + + tab[,ncol] = sapply(tab[,ncol],function(x) gsub("[[:blank:]]","",x)) + header=colnames(tab) + res=as.data.frame(matrix(ncol=ncol(tab),nrow=0)) + for (i in 1:nrow(tab) ) { + lines = split_ids_per_line(tab[i,],ncol) + res = rbind(res,lines) + } + }else { + res = unlist(sapply(tab[,1],function(x) strsplit(x,";")),use.names = F) + res = data.frame(res[which(!is.na(res[res!=""]))],stringsAsFactors = F) + colnames(res)=colnames(tab) + } + return(res) +} + +# Get information from neXtProt +get_uniprot_info <- function(ids,pc_features,uniprot_file){ + + cols = c("Entry",pc_features) + cols=cols[cols!="None"] + info = uniprot_file[match(ids,uniprot_file$Entry),cols] + colnames(info)[1]="UniProt-AC" + + return(info) +} + +main <- function() { + + args <- get_args() + + #save(args,file="/home/dchristiany/proteore_project/ProteoRE/tools/add_protein_features_mouse/args.rda") + #load("/home/dchristiany/proteore_project/ProteoRE/tools/add_protein_features_mouse/args.rda") + + #setting variables + inputtype = args$inputtype + if (inputtype == "copy_paste") { + ids = get_list_from_cp(args$input) + + #Check for UniProt-AC ids + if (all(!check_ids(ids,'uniprot'))){ + stop ("No UniProt-AC found in ids.") + } else if (any(!check_ids(ids,'uniprot'))) { + print ('Some ids in ids are not uniprot-AC:') + print (ids[which(!check_ids(ids,'uniprot'))]) + } + file = data.frame(ids,stringsAsFactors = F) + ncol=1 + + } else if (inputtype == "file") { + filename = args$input + ncol = args$column + # Check ncol + if (! as.numeric(gsub("c", "", ncol)) %% 1 == 0) { + stop("Please enter an integer for level") + } else { + ncol = as.numeric(gsub("c", "", ncol)) + } + + header = str2bool(args$header) + file = read.table(filename, header = header , sep = "\t", fill = TRUE, stringsAsFactors = FALSE, quote="", check.names = F, comment.char = "") # Get file content + if (any(grep(";",file[,ncol]))) {file = one_id_one_line(file,ncol)} + ids=file[,ncol] + } + + # Read reference file + uniprot_file <- read.table(args$uniprot_file, header = TRUE , sep = "\t", fill = TRUE,stringsAsFactors = FALSE, quote="", check.names = F, comment.char = "") + + # Parse arguments + pc_features = gsub("__ob__","[",gsub("__cb__","]",strsplit(args$pc_features, ",")[[1]])) + output = args$output + + #output file + res <- get_uniprot_info(ids,pc_features,uniprot_file) + res = res[!duplicated(res$`UniProt-AC`),] + output_content = merge(file, res,by.x=ncol,by.y="UniProt-AC",incomparables = NA,all.x=T) + output_content = order_columns(output_content,ncol,file) + output_content <- as.data.frame(apply(output_content, c(1,2), function(x) gsub("^$|^ $", NA, x))) #convert "" et " " to NA + write.table(output_content, output, row.names = FALSE, sep = "\t", quote = FALSE) + +} + +if(!interactive()) { + main() +} diff -r 000000000000 -r 1e856941a888 add_protein_features_mouse.xml --- /dev/null Thu Jan 01 00:00:00 1970 +0000 +++ b/add_protein_features_mouse.xml Fri Feb 08 08:46:04 2019 -0500 @@ -0,0 +1,150 @@ + +[UniProt] + + + R + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + inputtype=="file" + + + + + + + + + + + + + + + + + + + +`_. + + +----- + +**Output** + +Output is a tabular file containing both original columns and new columns including the annotation requested. +Please, note that a "NA" is returned when there is no information available from UniProt. + +----- + +**Data source (release date)** + +Annotations have been retrieved from UniProt.org (02/2019). + +----- + +.. class:: infomark + +**Authors** + +David Christiany, Lisa Peru, T.P. Lien Nguyen, Florence Combes, Yves Vandenbrouck CEA, INSERM, CNRS, Grenoble-Alpes University, BIG Institute, FR + +Sandra Dérozier, Olivier Rué, Christophe Caron, Valentin Loux INRA, Paris-Saclay University, MAIAGE Unit, Migale Bioinformatics platform, FR + +This work has been partially funded through the French National Agency for Research (ANR) IFB project. + +Contact support@proteore.org for any questions or concerns about the Galaxy implementation of this tool. + + ]]> + + + + diff -r 000000000000 -r 1e856941a888 test-data/Wilson-foie-souris-up.txt --- /dev/null Thu Jan 01 00:00:00 1970 +0000 +++ b/test-data/Wilson-foie-souris-up.txt Fri Feb 08 08:46:04 2019 -0500 @@ -0,0 +1,231 @@ +Q3TIA9 +Q9D566 +Q8VC49 +P02802 +Q9D2Y4 +P02798 +Q5HZH8 +Q3V0K9 +Q8VC73 +Q3TW96 +Q91YR9 +Q54AC6 +Q3V3U0 +P01592 +Q3TT92 +Q9D020 +Q62266 +P63166 +Q99M71 +Q9R0Y5 +Q8CD23 +Q99LB4 +B7FAV1 +A2AQU8 +Q6PDL0 +D3Z1Z8 +A0A0R4J0G0 +Q3U054 +Q80X95 +Q3U6P5 +D3YZ06 +Q8CGA1 +Q925B0 +P70460 +Q3TAY9 +Q9DBG9 +A0A0R4J0W6 +E9Q1Y3 +Q3TU94 +A0A087WRY3 +Q9Z2G9 +Q8K403 +Q9CQF3 +Q3U3E7 +Q8BG07 +P19639 +Q3TKP3 +Q9D1K2 +A2AFI4 +Q58EU7 +Q62159 +A2ASX2 +Q3TWK8 +Q543F3 +A0A1B0GT81 +Q569Z6 +Q684Q6 +Q4KML7 +E9Q616 +V9GX26 +E9PY03 +Q3TRG2 +Q07797 +A2AUK7 +B1B1A8 +Q9DBR7 +A0A0R4J1E8 +A6H6H4 +Q3UDY1 +Q3UKD6 +Q3TDI7 +A0A0R4J2B2 +Q3THE2 +A0A087WNV1 +Q6P8Q0 +Q9D964 +Q542Y0 +Q3UR53 +A2RST1 +Q99JG3 +D3YVS7 +Q4KMM5 +Q8VC73 +P35459 +Q9DBS1 +Q8R3G9 +F6XJA1 +Q99JW5 +Q148B1 +Q8VI94 +Q8R480 +Q920X5 +P15392 +Q543B6 +Q61024 +Q4KML7 +G5E924 +Q8VC49 +Q9D1M7 +Q9EQ79 +Q80V26 +Q91YL3 +Q52KR6 +E9QNN1 +Q3UQA7 +Q3TEP0 +Q3U3W2 +D3Z637 +B0G0Y1 +Q9CYL5 +Q60749 +P61327 +Q58DZ5 +Q8VCB1 +Q3TKP3 +Q3THA6 +Q3TFP0 +G5E866 +P57784 +B1AZI6 +Q4FJR9 +Q9WU81 +Q99MR6 +Q3U3F6 +Q8VDU3 +Q9CR32 +Q8BTU4 +H7BX95 +Q3TD86 +Q9D566 +Q8BXC0 +Q9D816 +Q80UW7 +Q4FK54 +Q00PI9 +Q8BHC4 +Q3THE2 +G8JL74 +Q99K86 +D3Z132 +Q58EU7 +Q3U263 +Q61753 +O08583 +B2RXT3 +A0A0N4SVP8 +Q569X3 +E9QN37 +Q499F3 +A0A0R4J0T5 +Q7TMX4 +Q3V1Z5 +P62627 +Q9CXX7 +Q53YX2 +Q9D8S5 +Q3TCL2 +A0A087WNV1 +O08692 +Q14AF6 +B1AVZ0 +Q8BUM1 +F6VQH5 +Q9D6G1 +A0PJK7 +Q3U6P5 +F8WJG3 +Q8K4Z5 +O88512 +Q3TDU5 +K3W4R2 +P11928 +Q9ER41 +O08532 +Q4FJM5 +Q69ZD1 +Q3UNZ1 +Z4YK56 +Q5BL18 +Q8VHM5 +Q3UKR1 +Q542D6 +E9Q616 +A2AFI9 +Q9CX86 +Q8VCN3 +Q58E59 +A0A0N4SVU8 +O88569 +Q9DBX3 +Q0VG47 +Q91VM5 +L7N451 +Q3V1S6 +Q99KP6 +Q69ZN7 +Q31094 +Q99M71 +Q3TFC0 +Q6P1F5 +Q542I8 +Q8VDP4 +Q62192 +Q9DB34 +E9Q5D6 +Q3U741 +G3X920 +Q4FJQ6 +Q9D4V7 +Q99LS5 +Q9BCZ4 +Q99PV0 +Q3TXV7 +Q3UKJ6 +Q8C0M2 +Q9DD06 +A0A0R4J0W6 +Q5U5I3 +Z4YLT8 +Q7TPX2 +Q91YR9 +Q8BVK3 +Q3UHJ0 +Q6PE01 +Q3TWW8 +F6ZV59 +Q8CHW4 +Q80X54 +G5E8V9 +Q8VIJ6 +P16045 diff -r 000000000000 -r 1e856941a888 test-data/results_wilson-foie-souris-up.tsv --- /dev/null Thu Jan 01 00:00:00 1970 +0000 +++ b/test-data/results_wilson-foie-souris-up.tsv Fri Feb 08 08:46:04 2019 -0500 @@ -0,0 +1,231 @@ +Q3TIA9 Entry name Protein names Length Mass Features Intramembrane Transmembrane Topological domain Pathway Function [CC] Post-translational modification Subcellular location [CC] Subunit structure [CC] Domain [CC] Tissue specificity Involvement in disease +A0A087WNV1 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +A0A087WNV1 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +A0A087WRY3 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +A0A0N4SVP8 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +A0A0N4SVU8 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +A0A0R4J0G0 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +A0A0R4J0T5 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +A0A0R4J0W6 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +A0A0R4J0W6 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +A0A0R4J1E8 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +A0A0R4J2B2 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +A0A1B0GT81 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +A0PJK7 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +A2AFI4 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +A2AFI9 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +A2AQU8 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +A2ASX2 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +A2AUK7 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +A2RST1 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +A6H6H4 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +B0G0Y1 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +B1AVZ0 UPP_MOUSE Uracil phosphoribosyltransferase homolog 310 34,278 Binding site (5); Chain (1); Modified residue (1); Nucleotide binding (1); Region (2) NA NA NA NA NA NA SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. NA NA NA NA +B1AZI6 THOC2_MOUSE THO complex subunit 2 (Tho2) 1594 182,773 Chain (1); Coiled coil (2); Modified residue (8); Motif (1) NA NA NA NA FUNCTION: Required for efficient export of polyadenylated RNA and spliced mRNA. Acts as component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and which specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NFX1 pathway. Plays a role for proper neuronal development. {ECO:0000250|UniProtKB:Q8NI27}. NA SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Nucleus speckle {ECO:0000250}. SUBUNIT: Component of the THO complex, which is composed of THOC1, THOC2, THOC3, THOC5, THOC6 and THOC7; together with at least ALYREF/THOC4, DDX39B, SARNP/CIP29 and CHTOP, THO forms the transcription/export (TREX) complex which seems to have a dynamic structure involving ATP-dependent remodeling. Interacts with THOC1, POLDIP3 and ZC3H11A (By similarity). {ECO:0000250}. NA TISSUE SPECIFICITY: Expressed in the hippocampus and the cortical neurons. {ECO:0000269|PubMed:26166480}. NA +B1B1A8 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +B2RXT3 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +B7FAV1 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +D3YVS7 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +D3YZ06 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +D3Z132 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +D3Z1Z8 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +D3Z637 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +E9PY03 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +E9Q1Y3 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +E9Q5D6 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +E9Q616 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +E9Q616 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +E9QN37 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +E9QNN1 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +F6VQH5 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +F6XJA1 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +F6ZV59 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +F8WJG3 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +G3X920 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +G5E866 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +G5E8V9 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +G5E924 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +G8JL74 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +H7BX95 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +K3W4R2 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +L7N451 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +O08532 CA2D1_MOUSE Voltage-dependent calcium channel subunit alpha-2/delta-1 (Voltage-gated calcium channel subunit alpha-2/delta-1) [Cleaved into: Voltage-dependent calcium channel subunit alpha-2-1; Voltage-dependent calcium channel subunit delta-1] 1103 124,630 Alternative sequence (3); Chain (3); Disulfide bond (1); Domain (2); Glycosylation (8); Metal binding (3); Modified residue (1); Motif (1); Signal peptide (1); Topological domain (2); Transmembrane (1) NA TRANSMEM 1074 1094 Helical. {ECO:0000255}. TOPO_DOM 25 1073 Extracellular. {ECO:0000255}.; TOPO_DOM 1095 1103 Cytoplasmic. {ECO:0000255}. NA FUNCTION: The alpha-2/delta subunit of voltage-dependent calcium channels regulates calcium current density and activation/inactivation kinetics of the calcium channel. Plays an important role in excitation-contraction coupling (By similarity). {ECO:0000250}. PTM: Proteolytically processed into subunits alpha-2-1 and delta-1 that are disulfide-linked. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Dimer formed of alpha-2-1 and delta-1 chains; disulfide-linked. Voltage-dependent calcium channels are multisubunit complexes, consisting of alpha-1 (CACNA1), alpha-2 (CACNA2D), beta (CACNB) and delta (CACNA2D) subunits in a 1:1:1:1 ratio (By similarity). {ECO:0000250}. DOMAIN: The MIDAS-like motif in the VWFA domain binds divalent metal cations and is required to promote trafficking of the alpha-1 (CACNA1) subunit to the plasma membrane by an integrin-like switch. {ECO:0000250}. TISSUE SPECIFICITY: Isoform 2A is expressed in skeletal muscle and aorta. Isoform 2B is expressed in brain. Isoform 2C is expressed in heart. Isoform 2D is expressed in heart and smooth muscle. Isoform 2E is expressed in smooth muscle. All five isoforms are expressed in the cardiovascular system. NA +O08583 THOC4_MOUSE THO complex subunit 4 (Tho4) (Ally of AML-1 and LEF-1) (Aly/REF export factor) (REF1-I) (RNA and export factor-binding protein 1) (Transcriptional coactivator Aly/REF) 255 26,940 Alternative sequence (1); Beta strand (4); Chain (1); Compositional bias (1); Domain (1); Helix (2); Initiator methionine (1); Modified residue (20); Region (1) NA NA NA NA FUNCTION: Export adapter involved in nuclear export of spliced and unspliced mRNA. Binds mRNA which is thought to be transferred to the NXF1-NXT1 heterodimer for export (TAP/NFX1 pathway). Component of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm. TREX recruitment occurs via an interaction between ALYREF/THOC4 and the cap-binding protein NCBP1. Required for TREX complex assembly and for linking DDX39B to the cap-binding complex (CBC). In conjunction with THOC5 functions in NXF1-NXT1 mediated nuclear export of HSP70 mRNA; both proteins enhance the RNA binding activity of NXF1 and are required for NXF1 localization to the nuclear rim. Involved in the nuclear export of intronless mRNA; proposed to be recruited to intronless mRNA by ATP-bound DDX39B. Involved in transcription elongation and genome stability.; FUNCTION: Acts as chaperone and promotes the dimerization of transcription factors containing basic leucine zipper (bZIP) domains and thereby promotes transcriptional activation. PTM: Arg-50 and Arg-203 are dimethylated, probably to asymmetric dimethylarginine. Arginine methylation reduces RNA binding (By similarity). {ECO:0000250}.; PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9119228}. Nucleus speckle {ECO:0000250|UniProtKB:Q86V81}. Cytoplasm {ECO:0000269|PubMed:9119228}. Note=Colocalizes with the core EJC, ALYREF/THOC4, NXF1 and DDX39B in the nucleus and nuclear speckles. Localizes to regions surrounding nuclear speckles known as perispeckles in which TREX complex assembly seems to occur. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. {ECO:0000250|UniProtKB:Q86V81}. SUBUNIT: Homomultimer (By similarity). Is part of several complexes involved in mRNA processing and export (By similarity). Component of the transcription/export (TREX) complex at least composed of ALYREF/THOC4, DDX39B, SARNP/CIP29, CHTOP and the THO subcomplex; TREX seems to have a dynamic structure involving ATP-dependent remodeling; in the complex interacts (via C-terminus) directly with DDX39B and interacts directly with THOC1 and THOC2 (By similarity). Found in mRNA splicing-dependent exon junction complexes (EJC) (By similarity). Identified in the spliceosome C complex (By similarity). Found in a mRNP complex with UPF3A and UPF3B (By similarity). Interacts with RBM8A, NCBP1, THOC5, LEF1, RUNX1, EIF4A3, RNPS1, SRRM1, IWS1 and EXOSC1 (By similarity). Interacts with RBM15B. Interacts with NXF1; the interaction is direct (PubMed:10786854). {ECO:0000250|UniProtKB:Q86V81, ECO:0000269|PubMed:10786854}. NA TISSUE SPECIFICITY: Highly expressed in heart, brain, spleen, lung, liver, skeletal muscle, kidney and testis. {ECO:0000269|PubMed:9119228}. NA +O08692 NGP_MOUSE Neutrophilic granule protein (NGP) (Cystatin-like protein) (Myeloid bactenecin protein) (Myeloid secondary granule protein) 167 19,332 Chain (1); Sequence conflict (1); Signal peptide (1) NA NA NA NA FUNCTION: Acts as an inhibitor of cathepsin B (CTSB) activity. Plays a role as a negative regulator of tumor vascular development, cell invasion and metastasis. {ECO:0000269|PubMed:21518852}. NA SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21518852}. Cytoplasmic granule {ECO:0000269|PubMed:8749713}. Note=Localizes in cytoplasmic granules of neutrophilic precursors (PubMed:8749713). {ECO:0000269|PubMed:21518852, ECO:0000269|PubMed:8749713}. SUBUNIT: Monomer. Homodimer; disulfide-linked. {ECO:0000269|PubMed:21518852}. NA TISSUE SPECIFICITY: Expressed in myeloid bone marrow cells. Expressed in neutrophilic precursors (at protein level) (PubMed:8749713). Expressed in myeloid bone marrow cells (PubMed:21518852). {ECO:0000269|PubMed:21518852, ECO:0000269|PubMed:8749713}. NA +O88512 AP1G2_MOUSE AP-1 complex subunit gamma-like 2 (Gamma2-adaptin) (G2ad) 791 87,863 Chain (1); Domain (1); Sequence conflict (1) NA NA NA NA FUNCTION: May function in protein sorting in late endosomes or multivesucular bodies (MVBs). Involved in MVB-assisted maturation of hepatitis B virus (HBV). {ECO:0000250|UniProtKB:O75843}. NA SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:O75843}; Peripheral membrane protein {ECO:0000250|UniProtKB:O75843}; Cytoplasmic side {ECO:0000250|UniProtKB:O75843}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:O75843}; Peripheral membrane protein {ECO:0000250|UniProtKB:O75843}. Endosome membrane {ECO:0000250|UniProtKB:O75843}; Peripheral membrane protein {ECO:0000250|UniProtKB:O75843}. Note=Mainly localized to perinuclear vesicular structures. Colocalizes with HBV major surface antigen L and HBV core protein C in CD63-containing compartments. Colocalizes with HBV major surface antigen L to cis-Golgi-like structures. {ECO:0000250|UniProtKB:O75843}. SUBUNIT: Probably interacts with AP1S1/Sigma1A-adaptin AP1S2/Sigma1B-adaptin. Probably does not interact with APB1. Interacts with HBV major surface antigen L. Interacts with HBV core protein C in a ubiquitin-dependent manner. Binds ubiquitin. {ECO:0000250|UniProtKB:O75843}. NA TISSUE SPECIFICITY: Widely expressed. NA +O88569 ROA2_MOUSE Heterogeneous nuclear ribonucleoproteins A2/B1 (hnRNP A2/B1) 353 37,403 Alternative sequence (2); Chain (1); Compositional bias (1); Cross-link (9); Domain (2); Modified residue (36); Motif (1); Region (2); Sequence conflict (3) NA NA NA NA FUNCTION: Heterogeneous nuclear ribonucleoprotein (hnRNP) that associates with nascent pre-mRNAs, packaging them into hnRNP particles. The hnRNP particle arrangement on nascent hnRNA is non-random and sequence-dependent and serves to condense and stabilize the transcripts and minimize tangling and knotting. Packaging plays a role in various processes such as transcription, pre-mRNA processing, RNA nuclear export, subcellular location, mRNA translation and stability of mature mRNAs. Forms hnRNP particles with at least 20 other different hnRNP and heterogeneous nuclear RNA in the nucleus. Involved in transport of specific mRNAs to the cytoplasm in oligodendrocytes and neurons: acts by specifically recognizing and binding the A2RE (21 nucleotide hnRNP A2 response element) or the A2RE11 (derivative 11 nucleotide oligonucleotide) sequence motifs present on some mRNAs, and promotes their transport to the cytoplasm (By similarity). Specifically binds single-stranded telomeric DNA sequences, protecting telomeric DNA repeat against endonuclease digestion (By similarity). Also binds other RNA molecules, such as primary miRNA (pri-miRNAs): acts as a nuclear 'reader' of the N6-methyladenosine (m6A) mark by specifically recognizing and binding a subset of nuclear m6A-containing pri-miRNAs. Binding to m6A-containing pri-miRNAs promotes pri-miRNA processing by enhancing binding of DGCR8 to pri-miRNA transcripts. Involved in miRNA sorting into exosomes following sumoylation, possibly by binding (m6A)-containing pre-miRNAs. Acts as a regulator of efficiency of mRNA splicing, possibly by binding to m6A-containing pre-mRNAs (By similarity). {ECO:0000250|UniProtKB:A7VJC2, ECO:0000250|UniProtKB:P22626}. PTM: Sumoylated in exosomes, promoting miRNAs-binding. {ECO:0000250|UniProtKB:P22626}.; PTM: Asymmetric dimethylation at Arg-266 constitutes the major methylation site (By similarity). According to a report, methylation affects subcellular location and promotes nuclear localization (By similarity). According to another report, methylation at Arg-266 does not influence nucleocytoplasmic shuttling (By similarity). {ECO:0000250|UniProtKB:A7VJC2, ECO:0000250|UniProtKB:P22626}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P22626}. Cytoplasmic granule {ECO:0000250|UniProtKB:P22626}. Secreted, exosome {ECO:0000250|UniProtKB:P22626}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Component of ribonucleosomes. Not found in the nucleolus. Found in exosomes follwong sumoylation. {ECO:0000250|UniProtKB:P22626}. SUBUNIT: Identified in the spliceosome C complex. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with IGF2BP1. Interacts with C9orf72. Interacts with DGCR8. Interacts with TARDBP. Interacts with CKAP5. {ECO:0000250|UniProtKB:P22626}. DOMAIN: The low complexity (LC) region is intrinsically disordered. When incubated at high concentration, it is able to polymerize into labile, amyloid-like fibers and form cross-beta polymerization structures, probably driving the formation of hydrogels. In contrast to irreversible, pathogenic amyloids, the fibers polymerized from LC regions disassemble upon dilution. A number of evidences suggest that formation of cross-beta structures by LC regions mediate the formation of RNA granules, liquid-like droplets, and hydrogels. {ECO:0000250|UniProtKB:P22626}. NA NA +P01592 IGJ_MOUSE Immunoglobulin J chain 159 18,014 Chain (1); Disulfide bond (5); Glycosylation (1); Sequence conflict (4); Signal peptide (1) NA NA NA NA FUNCTION: Serves to link two monomer units of either IgM or IgA. In the case of IgM, the J chain-joined dimer is a nucleating unit for the IgM pentamer, and in the case of IgA it induces larger polymers. It also help to bind these immunoglobulins to secretory component. {ECO:0000269|PubMed:1517233}. NA SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1517233}. NA NA NA NA +P02798 MT2_MOUSE Metallothionein-2 (MT-2) (Metallothionein-II) (MT-II) 61 6,115 Chain (1); Metal binding (20); Modified residue (2); Region (2); Sequence conflict (1) NA NA NA NA FUNCTION: Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids. NA NA NA DOMAIN: Class I metallothioneins contain 2 metal-binding domains: four divalent ions are chelated within cluster A of the alpha domain and are coordinated via cysteinyl thiolate bridges to 11 cysteine ligands. Cluster B, the corresponding region within the beta domain, can ligate three divalent ions to 9 cysteines. NA NA +P02802 MT1_MOUSE Metallothionein-1 (MT-1) (Metallothionein-I) (MT-I) 61 6,018 Beta strand (5); Chain (1); Metal binding (20); Modified residue (1); Region (2); Sequence conflict (2) NA NA NA NA FUNCTION: Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids. NA NA NA DOMAIN: Class I metallothioneins contain 2 metal-binding domains: four divalent ions are chelated within cluster A of the alpha domain and are coordinated via cysteinyl thiolate bridges to 11 cysteine ligands. Cluster B, the corresponding region within the beta domain, can ligate three divalent ions to 9 cysteines. NA NA +P11928 OAS1A_MOUSE 2'-5'-oligoadenylate synthase 1A ((2-5')oligo(A) synthase 1A) (2-5A synthase 1A) (EC 2.7.7.84) (p42 OAS) 367 42,429 Binding site (4); Chain (1); Metal binding (3); Region (2); Sequence conflict (8) NA NA NA NA FUNCTION: Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response. In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation. Synthesizes higher oligomers of 2'-5'-oligoadenylates (2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L (RNase L) leading to its dimerization and subsequent activation. Activation of RNase L leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication. Can mediate the antiviral effect via the classical RNase L-dependent pathway or an alternative antiviral pathway independent of RNase L. {ECO:0000269|PubMed:12396720}. NA SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15899864}. Mitochondrion {ECO:0000250|UniProtKB:P00973}. Nucleus {ECO:0000250|UniProtKB:P00973}. Microsome {ECO:0000250|UniProtKB:P00973}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P00973}. Note=Associated with different subcellular fractions such as mitochondrial, nuclear, and rough/smooth microsomal fractions. {ECO:0000250|UniProtKB:P00973}. SUBUNIT: Monomer (By similarity). Homotetramer (By similarity). Interacts with OAS1D; the interaction inhibits OAS1A catalytic activity (PubMed:15899864). {ECO:0000250|UniProtKB:P00973, ECO:0000269|PubMed:15899864}. NA TISSUE SPECIFICITY: Expressed in oocytes and granulosa cells of ovary, in intestine, stomach, spleen and uterus (at protein level) (PubMed:15899864). Expressed at high levels in the digestive tract and lymphoid organs (PubMed:12396720). Expressed in ovary and spleen (PubMed:27663720). {ECO:0000269|PubMed:12396720, ECO:0000269|PubMed:15899864, ECO:0000269|PubMed:27663720}. NA +P15392 CP2A4_MOUSE Cytochrome P450 2A4 (EC 1.14.14.1) (CYPIIA4) (Cytochrome P450-15-alpha) (Cytochrome P450-IIA3.1) (Testosterone 15-alpha-hydroxylase) 494 56,782 Chain (1); Metal binding (1); Modified residue (2); Sequence conflict (16) NA NA NA NA FUNCTION: Highly active in the 15-alpha-hydroxylation of testosterone. Also active in the 15-alpha-hydroxylation of progesterone and androstenedione. Little or no activity on corticosterone, pregnenolone, dehydroepiandrosterone, estradiol or estriol. NA SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. NA NA TISSUE SPECIFICITY: Kidney and lung. Expressed in liver, with a strong circadian rhythmicity. Circadian expression is regulated by DBP. {ECO:0000269|PubMed:10490589}. NA +P16045 LEG1_MOUSE Galectin-1 (Gal-1) (14 kDa lectin) (Beta-galactoside-binding lectin L-14-I) (Galaptin) (Lactose-binding lectin 1) (Lectin galactoside-binding soluble 1) (S-Lac lectin 1) 135 14,866 Beta strand (11); Binding site (2); Chain (1); Domain (1); Frameshift (2); Initiator methionine (1); Modified residue (8); Region (2); Sequence conflict (3) NA NA NA NA FUNCTION: Lectin that binds beta-galactoside and a wide array of complex carbohydrates. Plays a role in regulating apoptosis, cell proliferation and cell differentiation. Inhibits CD45 protein phosphatase activity and therefore the dephosphorylation of Lyn kinase. Strong inducer of T-cell apoptosis. {ECO:0000250|UniProtKB:P09382, ECO:0000269|PubMed:1986871}. NA SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P09382}. SUBUNIT: Homodimer. Binds LGALS3BP. Interacts with CD2, CD3, CD4, CD6, CD7, CD43, ALCAM and CD45. Interacts with laminin (via poly-N-acetyllactosamine). Interacts with SUSD2. {ECO:0000250|UniProtKB:P09382}. NA NA NA +P19639 GSTM3_MOUSE Glutathione S-transferase Mu 3 (EC 2.5.1.18) (GST class-mu 3) (Glutathione S-transferase GT9.3) 218 25,702 Chain (1); Cross-link (2); Domain (2); Erroneous initiation (1); Initiator methionine (1); Region (4) NA NA NA NA FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. NA SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Homodimer. NA NA NA +P35459 LY6D_MOUSE Lymphocyte antigen 6D (Ly-6D) (Thymocyte B-cell antigen) (ThB) 127 13,396 Chain (1); Disulfide bond (5); Domain (1); Erroneous initiation (1); Lipidation (1); Propeptide (1); Signal peptide (1) NA NA NA NA FUNCTION: May act as a specification marker at earliest stage specification of lymphocytes between B- and T-cell development. Marks the earliest stage of B-cell specification. {ECO:0000269|PubMed:19833765}. NA SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. NA NA TISSUE SPECIFICITY: Lymphoid cells lacking Ly6d, called ALP (all-lymphoid progenitor), retain full lymphoid potential and early thymic seeding activity, whereas cells containing Ly6d, called BLP (B-cell-biased lymphoid progenitor), up-regulate the B-cell specifying factors Ebf1 and Pax5 and behave essentially as B-cell progenitors (at protein level). Thymocytes and B-cells. {ECO:0000269|PubMed:19833765}. NA +P57784 RU2A_MOUSE U2 small nuclear ribonucleoprotein A' (U2 snRNP A') 255 28,357 Chain (1); Cross-link (2); Domain (1); Modified residue (5); Repeat (4); Sequence conflict (2) NA NA NA NA FUNCTION: Involved in pre-mRNA splicing as component of the spliceosome. Associated with sn-RNP U2, where it contributes to the binding of stem loop IV of U2 snRNA. {ECO:0000250|UniProtKB:P09661}. NA SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P09661}. SUBUNIT: Identified in the spliceosome B complex. Identified in the spliceosome C complex. Found in a pre-mRNA splicing complex with SFRS4, SFRS5, SNRNP70, SNRPA1, SRRM1 and SRRM2. Found in a pre-mRNA exonic splicing enhancer (ESE) complex with SNRNP70, SNRPA1, SRRM1 and TRA2B. Contributes to the binding of stem loop IV of U2 snRNA with SNRPB2. {ECO:0000250|UniProtKB:P09661}. NA NA NA +P61327 MGN_MOUSE Protein mago nashi homolog 146 17,164 Chain (1); Modified residue (1) NA NA NA NA FUNCTION: Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). The MAGOH-RBM8A heterodimer inhibits the ATPase activity of EIF4A3, thereby trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The MAGOH-RBM8A heterodimer interacts with the EJC key regulator PYM1 leading to EJC disassembly in the cytoplasm and translation enhancement of EJC-bearing spliced mRNAs by recruiting them to the ribosomal 48S preinitiation complex. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms; the function is different from the established EJC assembly (By similarity). {ECO:0000250}. NA SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus speckle {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Detected in granule-like structures in the dendroplasm. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. Colocalizes with the core EJC, ALYREF/THOC4, NXF1 and UAP56 in the nucleus and nuclear speckles (By similarity). {ECO:0000250}. SUBUNIT: Heterodimer with RBM8A. Part of the mRNA splicing-dependent exon junction complex (EJC) complex; the core complex contains CASC3, EIF4A3, MAGOH and RBM8A. Interacts with PYM1; the interaction is direct and dissociates the EJC from spliced mRNAs. Identified in the spliceosome C complex (By similarity). {ECO:0000250}. NA NA NA +P62627 DLRB1_MOUSE Dynein light chain roadblock-type 1 (Dynein light chain 2A, cytoplasmic) 96 10,990 Beta strand (5); Chain (1); Helix (2); Initiator methionine (1); Modified residue (1); Sequence conflict (1); Turn (1) NA NA NA NA FUNCTION: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. NA SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SUBUNIT: Homodimer. The cytoplasmic dynein 1 complex consists of two catalytic heavy chains (HCs) and a number of non-catalytic subunits presented by intermediate chains (ICs), light intermediate chains (LICs) and light chains (LCs); the composition seems to vary in respect to the IC, LIC and LC composition. The heavy chain homodimer serves as a scaffold for the probable homodimeric assembly of the respective non-catalytic subunits. The ICs and LICs bind directly to the HC dimer and the LCs assemble on the IC dimer. Interacts with DYNC1I1 and DYNC1I2. Self-associates. Interacts with DYNLRB2. Interacts with RAB6A; the interaction is direct. Interacts with RAB6B (GDP-bound) (By similarity). {ECO:0000250}. NA NA NA +P63166 SUMO1_MOUSE Small ubiquitin-related modifier 1 (SUMO-1) (SMT3 homolog 3) (Ubiquitin-homology domain protein PIC1) (Ubiquitin-like protein SMT3C) (Smt3C) 101 11,557 Chain (1); Cross-link (11); Domain (1); Initiator methionine (1); Modified residue (4); Propeptide (1); Site (1) NA NA NA NA FUNCTION: Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Covalently attached to the voltage-gated potassium channel KCNB1; this modulates the gating characteristics of KCNB1. Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development. Covalently attached to ZFHX3 (By similarity). {ECO:0000250|UniProtKB:P63165, ECO:0000269|PubMed:16990542}. PTM: Cleavage of precursor form by SENP1 or SENP2 is necessary for function. {ECO:0000250}.; PTM: Polymeric SUMO1 chains undergo polyubiquitination by RNF4. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus membrane. Nucleus speckle. Cytoplasm. Nucleus, PML body {ECO:0000250}. Cell membrane {ECO:0000250|UniProtKB:P63165}. Nucleus {ECO:0000250|UniProtKB:P63165}. Note=Recruited by BCL11A into the nuclear body. In the presence of ZFHX3, sequesterd to nuclear body (NB)-like dots in the nucleus some of which overlap or closely associate with PML body (By similarity). {ECO:0000250|UniProtKB:P63165, ECO:0000269|PubMed:18681895}. SUBUNIT: Interacts with USP25 (via ts SIM domain) the interaction weakly sumoylates USP25. Covalently attached to KCNB1; UBE2I increases cross-linking with KCNB1 and PIAS1 decreases cross-links with KCNB1 (By similarity). Interacts with SAE2, UBE2I, RANBP2, PIAS1 and PIAS2. Interacts with PRKN. Covalently attached to a number of proteins such as IKFZ1, PML, RANGAP1, HIPK2, SP100, p53, p73-alpha, MDM2, JUN, DNMT3B and TDG. Also interacts with HIF1A, HIPK2, HIPK3, CHD3, EXOSC9, RAD51 and RAD52. Interacts with SIMC1, CASP8AP2, RNF111 AND SOBP (via SIM domains). Interacts with BHLHE40/DEC1. Interacts with RWDD3. Interacts with UBE2I/UBC9 and this interaction is enhanced in the presence of RWDD3. Interacts with MTA1 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P63165}. NA TISSUE SPECIFICITY: Ubiquitous. NA +P70460 VASP_MOUSE Vasodilator-stimulated phosphoprotein (VASP) 375 39,667 Chain (1); Coiled coil (1); Compositional bias (2); Domain (1); Erroneous gene model prediction (1); Initiator methionine (1); Modified residue (12); Motif (1); Mutagenesis (4); Natural variant (1); Region (5); Repeat (2); Sequence conflict (3) NA NA NA NA FUNCTION: Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance, lamellipodial and filopodial dynamics, platelet activation and cell migration. VASP promotes actin filament elongation. It protects the barbed end of growing actin filaments against capping and increases the rate of actin polymerization in the presence of capping protein. VASP stimulates actin filament elongation by promoting the transfer of profilin-bound actin monomers onto the barbed end of growing actin filaments. Plays a role in actin-based mobility of Listeria monocytogenes in host cells. Regulates actin dynamics in platelets and plays an important role in regulating platelet aggregation (By similarity). {ECO:0000250, ECO:0000269|PubMed:10660044}. PTM: Major substrate for cAMP-dependent (PKA) and cGMP-dependent protein kinase (PKG) in platelets. The preferred site for PKA is Ser-153, the preferred site for PKG, Ser-235. In ADP-activated platelets, phosphorylation by PKA or PKG/PRKG1 on Ser-153 leads to fibrinogen receptor inhibition. Phosphorylation on Thr-274 requires prior phosphorylation on Ser-153 and Ser-235. In response to phorbol ester (PMA) stimulation, phosphorylated by PKC/PRKCA. In response to thrombin, phosphorylated by both PKC and ROCK1. Phosphorylation at Thr-274 by AMPK does not require prior phosphorylation at Ser-153 or Ser-235. Phosphorylation at Ser-153 by PKA is required for localization to the tight junctions in epithelial cells. Phosphorylation modulates F-actin binding, actin filament elongation and platelet activation. Phosphorylation at Ser-318 by AMPK also alters actin filament binding. Carbon monoxide (CO) promotes phosphorylation at Ser-153, while nitric oxide (NO) promotes phosphorylation at Ser-153, but also at Ser-235. {ECO:0000269|PubMed:10085070, ECO:0000269|PubMed:10882740, ECO:0000269|PubMed:12372613, ECO:0000269|PubMed:21945940}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10660044}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10660044}. Cell junction, focal adhesion {ECO:0000269|PubMed:10660044}. Cell junction, tight junction {ECO:0000250}. Cell projection, lamellipodium membrane {ECO:0000269|PubMed:10660044}. Cell projection, filopodium membrane {ECO:0000269|PubMed:10660044}. Note=Targeted to stress fibers and focal adhesions through interaction with a number of proteins including MRL family members. Localizes to the plasma membrane in protruding lamellipodia and filopodial tips. Stimulation by thrombin or PMA, also translocates VASP to focal adhesions. Localized along the sides of actin filaments throughout the peripheral cytoplasm under basal conditions (By similarity). In pre-apoptotic cells, colocalizes with MEFV in large specks (pyroptosomes) (By similarity). {ECO:0000250}. SUBUNIT: Homotetramer (By similarity). Interacts with PFN1, PFN2, LPP, ACTN1 and ACTG1. Interacts, via the EVH1 domain, with the Pro-rich regions of ZYX. This interaction is important for targeting to focal adhesions and the formation of actin-rich structures at the apical surface of cells. Interacts, via the EVH1 domain, with the Pro-rich domain of Listeria monocytogenes actA. Interacts with APBB1IP. Interacts, via the Pro-rich domain, with the C-terminal SH3 domain of DNMBP. Interacts weakly with MEFV (By similarity). {ECO:0000250}. DOMAIN: The EVH2 domain is comprised of 3 regions. Block A is a thymosin-like domain required for G-actin binding. The KLKR motif within this block is essential for the G-actin binding and for actin polymerization. Block B is required for F-actin binding and subcellular location, and Block C for tetramerization.; DOMAIN: The WH1 domain mediates interaction with XIRP1. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in thymus and spleen. Lower levels in lung, ovary, placenta and fat. {ECO:0000269|PubMed:10069337}. NA +Q00PI9 HNRL2_MOUSE Heterogeneous nuclear ribonucleoprotein U-like protein 2 (MLF1-associated nuclear protein) 745 84,940 Chain (1); Compositional bias (2); Domain (2); Modified residue (11); Sequence conflict (1) NA NA NA NA NA NA SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17008314}. SUBUNIT: Binds to MLF1 and retains it in the nucleus. {ECO:0000269|PubMed:17008314}. NA NA NA +Q07797 LG3BP_MOUSE Galectin-3-binding protein (Cyp-C-associated protein) (CyCAP) (Lectin galactoside-binding soluble 3-binding protein) (Protein MAMA) 577 64,491 Chain (1); Disulfide bond (3); Domain (3); Glycosylation (6); Sequence conflict (7); Signal peptide (1) NA NA NA NA FUNCTION: Promotes integrin-mediated cell adhesion. May stimulate host defense against viruses and tumor cells (By similarity). {ECO:0000250|UniProtKB:Q08380}. PTM: N-glycosylated. {ECO:0000269|PubMed:8341703}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q08380}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:8119883}. SUBUNIT: Homodimers and homomultimers. The multimers form ring-like structures with a diameter of 30-40 nm. Binds LGALS1 and LGALS3. Binds ITGB1, COL4A1, COL5A1, COL6A1, FN1 and NID (By similarity). Interacts with PPIC (in vitro). The unglycosylated form interacts with PDE4DIP isoform 2/MMG8/SMYLE; this interaction may connect a pericentrosomal complex to the gamma-tubulin ring complex (gamma-TuRC) to promote microtubule assembly and acetylation (By similarity). {ECO:0000250|UniProtKB:Q08380, ECO:0000269|PubMed:8341703}. NA TISSUE SPECIFICITY: Detected in embryo, liver, spleen, kidney, lung, heart, intestine, thymus and lymph node. {ECO:0000269|PubMed:8119883, ECO:0000269|PubMed:8341703}. NA +Q0VG47 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q148B1 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q14AF6 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q31094 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q3TAY9 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q3TCL2 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q3TD86 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q3TDI7 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q3TDU5 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q3TEP0 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q3TFC0 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q3TFP0 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q3THA6 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q3THE2 ML12B_MOUSE Myosin regulatory light chain 12B (Myosin regulatory light chain 2-B, smooth muscle isoform) (Myosin regulatory light chain 20 kDa) (MLC20) (Myosin regulatory light chain MRLC2) 172 19,779 Calcium binding (1); Chain (1); Domain (3); Frameshift (1); Modified residue (2); Sequence conflict (3) NA NA NA NA FUNCTION: Myosin regulatory subunit that plays an important role in regulation of both smooth muscle and nonmuscle cell contractile activity via its phosphorylation. Phosphorylation triggers actin polymerization in vascular smooth muscle. Implicated in cytokinesis, receptor capping, and cell locomotion. {ECO:0000250|UniProtKB:O14950}. PTM: Phosphorylation increases the actin-activated myosin ATPase activity and thereby regulates the contractile activity. It is required to generate the driving force in the migration of the cells but not necessary for localization of myosin-2 at the leading edge. Phosphorylation is reduced following epigallocatechin-3-O-gallate treatment. {ECO:0000250|UniProtKB:O14950}. NA SUBUNIT: Myosin is a hexamer of 2 heavy chains and 4 light chains: interacts with myosin heavy chain MYO19. {ECO:0000269|PubMed:24825904}. NA NA NA +Q3THE2 ML12B_MOUSE Myosin regulatory light chain 12B (Myosin regulatory light chain 2-B, smooth muscle isoform) (Myosin regulatory light chain 20 kDa) (MLC20) (Myosin regulatory light chain MRLC2) 172 19,779 Calcium binding (1); Chain (1); Domain (3); Frameshift (1); Modified residue (2); Sequence conflict (3) NA NA NA NA FUNCTION: Myosin regulatory subunit that plays an important role in regulation of both smooth muscle and nonmuscle cell contractile activity via its phosphorylation. Phosphorylation triggers actin polymerization in vascular smooth muscle. Implicated in cytokinesis, receptor capping, and cell locomotion. {ECO:0000250|UniProtKB:O14950}. PTM: Phosphorylation increases the actin-activated myosin ATPase activity and thereby regulates the contractile activity. It is required to generate the driving force in the migration of the cells but not necessary for localization of myosin-2 at the leading edge. Phosphorylation is reduced following epigallocatechin-3-O-gallate treatment. {ECO:0000250|UniProtKB:O14950}. NA SUBUNIT: Myosin is a hexamer of 2 heavy chains and 4 light chains: interacts with myosin heavy chain MYO19. {ECO:0000269|PubMed:24825904}. NA NA NA +Q3TKP3 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q3TKP3 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q3TRG2 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q3TT92 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q3TU94 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q3TW96 UAP1L_MOUSE UDP-N-acetylhexosamine pyrophosphorylase-like protein 1 (EC 2.7.7.-) 507 56,614 Alternative sequence (1); Binding site (7); Chain (1); Erroneous initiation (1); Motif (2); Region (1); Sequence caution (1) NA NA NA NA NA NA NA NA NA NA NA +Q3TWK8 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q3TWW8 SRSF6_MOUSE Serine/arginine-rich splicing factor 6 (Pre-mRNA-splicing factor SRP55) (Splicing factor, arginine/serine-rich 6) 339 39,025 Chain (1); Compositional bias (2); Cross-link (1); Domain (2); Modified residue (9); Sequence conflict (4) NA NA NA NA FUNCTION: Plays a role in constitutive splicing and modulates the selection of alternative splice sites. Plays a role in the alternative splicing of MAPT/Tau exon 10. Binds to alternative exons of TNC pre-mRNA and promotes the expression of alternatively spliced TNC. Plays a role in wound healing and in the regulation of keratinocyte differentiation and proliferation via its role in alternative splicing (By similarity). {ECO:0000250}. PTM: Extensively phosphorylated on serine residues in the RS domain. Phosphorylated by DYRK1A, probably in the RS domain. Phosphorylation by DYRK1A modulates alternative splice site selection and inhibits the expression of MAPT/Tau exon 10 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12549914}. Nucleus speckle {ECO:0000250|UniProtKB:Q13247}. SUBUNIT: Binds SREK1/SFRS12. Interacts with DYRK1A (By similarity). {ECO:0000250}. NA NA NA +Q3TXV7 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q3U054 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q3U263 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q3U3E7 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q3U3F6 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q3U3W2 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q3U6P5 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q3U6P5 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q3U741 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q3UDY1 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q3UHJ0 AAK1_MOUSE AP2-associated protein kinase 1 (EC 2.7.11.1) (Adaptor-associated kinase 1) 959 103,346 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Compositional bias (3); Domain (1); Modified residue (20); Nucleotide binding (1); Sequence conflict (3) NA NA NA NA FUNCTION: Regulates clathrin-mediated endocytosis by phosphorylating the AP2M1/mu2 subunit of the adaptor protein complex 2 (AP-2) which ensures high affinity binding of AP-2 to cargo membrane proteins during the initial stages of endocytosis. Isoform 1 and isoform 2 display similar levels of kinase activity towards AP2M1. Regulates phosphorylation of other AP-2 subunits as well as AP-2 localization and AP-2-mediated internalization of ligand complexes. Phosphorylates NUMB and regulates its cellular localization, promoting NUMB localization to endosomes. Binds to and stabilizes the activated form of NOTCH1, increases its localization in endosomes and regulates its transcriptional activity (By similarity). {ECO:0000250}. PTM: Autophosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Membrane, clathrin-coated pit {ECO:0000250}. Note=Active when found in clathrin-coated pits at the plasma membrane. In neuronal cells, enriched at presynaptic terminals. In non-neuronal cells, enriched at leading edge of migrating cells (By similarity). {ECO:0000250}. SUBUNIT: Interacts with alpha-adaptin, AP-2, clathrin, NUMB and EPS15 isoform 2 (By similarity). Interacts with membrane-bound activated NOTCH1 but not with the inactive full-length form of NOTCH1. Preferentially interacts with monoubiquitinated activated NOTCH1 compared to the non-ubiquitinated form. {ECO:0000250, ECO:0000269|PubMed:21464124}. NA NA NA +Q3UKD6 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q3UKJ6 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q3UKR1 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q3UNZ1 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q3UQA7 SELH_MOUSE Selenoprotein H (SelH) 116 12,974 Chain (1); Cross-link (1); Modified residue (1); Non-standard residue (1) NA NA NA NA FUNCTION: May be involved in a redox-related process. {ECO:0000305}. NA NA NA NA NA NA +Q3UR53 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q3V0K9 PLSI_MOUSE Plastin-1 630 70,408 Calcium binding (2); Chain (1); Domain (6); Modified residue (1); Region (2) NA NA NA NA FUNCTION: Actin-bundling protein in the absence of calcium. {ECO:0000250}. PTM: Phosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. NA NA NA +Q3V1S6 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q3V1Z5 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q3V3U0 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q499F3 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q4FJM5 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q4FJQ6 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q4FJR9 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q4FK54 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q4KML7 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q4KML7 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q4KMM5 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q52KR6 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q53YX2 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q542D6 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q542I8 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q542Y0 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q543B6 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q543F3 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q54AC6 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q569X3 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q569Z6 TR150_MOUSE Thyroid hormone receptor-associated protein 3 (Thyroid hormone receptor-associated protein complex 150 kDa component) (Trap150) 951 108,178 Chain (1); Compositional bias (2); Cross-link (36); Initiator methionine (1); Modified residue (49); Nucleotide binding (1); Region (2) NA NA NA NA FUNCTION: Involved in pre-mRNA splicing. Remains associated with spliced mRNA after splicing which probably involves interactions with the exon junction complex (EJC). Can trigger mRNA decay which seems to be independent of nonsense-mediated decay involving premature stop codons (PTC) recognition. May be involved in nuclear mRNA decay. Involved in regulation of signal-induced alternative splicing. During splicing of PTPRC/CD45 is proposed to sequester phosphorylated SFPQ from PTPRC/CD45 pre-mRNA in resting T-cells. Involved in cyclin-D1/CCND1 mRNA stability probably by acting as component of the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. Involved in response to DNA damage. Is excluced from DNA damage sites in a manner that parallels transcription inhibition; the function may involve the SNARP complex. Initially thought to play a role in transcriptional coactivation through its association with the TRAP complex; however, it is not regarded as a stable Mediator complex subunit. Cooperatively with HELZ2, enhances the transcriptional activation mediated by PPARG, maybe through the stabilization of the PPARG binding to DNA in presence of ligand. May play a role in the terminal stage of adipocyte differentiation. Plays a role in the positive regulation of the circadian clock. Acts as a coactivator of the CLOCK-ARNTL/BMAL1 heterodimer and promotes its transcriptional activator activity and binding to circadian target genes (PubMed:24043798). {ECO:0000269|PubMed:23525231, ECO:0000269|PubMed:24043798}. NA SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23525231}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9Y2W1}. Nucleus speckle {ECO:0000250|UniProtKB:Q9Y2W1}. SUBUNIT: Associated with the large multiprotein complex TRAP (Mediator complex-like). Interacts with SFPQ; the interaction is dependent on SFPQ phosphorylation at 'Thr-687' and inhibits binding of SFPQ to an ESS1 exonic splicing silencer element-containing RNA. Interacts with NXF1. Component of the SNARP complex which consists at least of SNIP1, SNW1, THRAP3, BCLAF1 and PNN. Associated with spliced mRNP complexes. Interacts with HELZ2 and PPARG. Interacts with CLOCK and ARNTL/BMAL1 (By similarity). Component of a MACOM-like complex, named WTAP complex, composed of WTAP, ZC3H13, CBLL1, KIAA1429, RBM15, BCLAF1 and THRAP3 (By similarity). {ECO:0000250|UniProtKB:Q9Y2W1}. NA NA NA +Q58DZ5 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q58E59 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q58EU7 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q58EU7 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q5BL18 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q5HZH8 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q5U5I3 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q60749 KHDR1_MOUSE KH domain-containing, RNA-binding, signal transduction-associated protein 1 (GAP-associated tyrosine phosphoprotein p62) (Src-associated in mitosis 68 kDa protein) (Sam68) (p21 Ras GTPase-activating protein-associated p62) (p68) 443 48,371 Chain (1); Compositional bias (7); Cross-link (5); Domain (1); Modified residue (44); Mutagenesis (4); Region (3); Sequence conflict (6) NA NA NA NA FUNCTION: Recruited and tyrosine phosphorylated by several receptor systems, for example the T-cell, leptin and insulin receptors. Once phosphorylated, functions as an adapter protein in signal transduction cascades by binding to SH2 and SH3 domain-containing proteins. Role in G2-M progression in the cell cycle. Represses CBP-dependent transcriptional activation apparently by competing with other nuclear factors for binding to CBP. Also acts as a putative regulator of mRNA stability and/or translation rates and mediates mRNA nuclear export. Positively regulates the association of constitutive transport element (CTE)-containing mRNA with large polyribosomes and translation initiation. May not be involved in the nucleocytoplasmic export of unspliced (CTE)-containing RNA species. RNA-binding protein that plays a role in the regulation of alternative splicing and influences mRNA splice site selection and exon inclusion. Binds to RNA containing 5'-[AU]UAA-3' as a bipartite motif spaced by more than 15 nucleotides. Binds poly(A). In cooperation with HNRNPA1 modulates alternative splicing of BCL2L1 by promoting splicing toward isoform Bcl-X(S), and of SMN1 (By similarity). Can regulate CD44 alternative splicing in a Ras pathway-dependent manner. Can regulate alternative splicing of NRXN1 and NRXN3 in the laminin G-like domain 6 containing the evolutionary conserved neurexin alternative spliced segment 4 (AS4) involved in neurexin selective targeting to postsynaptic partners. In a neuronal activity-dependent manner cooperates synergistically with KHDRBS2/SLIM-1 in regulation of NRXN1 exon skipping at AS4. The cooperation with KHDRBS2/SLIM-1 is antagonistic for regulation of NXRN3 alternative splicing at AS4 (PubMed:12478298, PubMed:22196734, PubMed:24469635). {ECO:0000250|UniProtKB:O75525, ECO:0000269|PubMed:12478298, ECO:0000269|PubMed:12496368, ECO:0000269|PubMed:22196734, ECO:0000269|PubMed:24469635, ECO:0000269|PubMed:7512695, ECO:0000269|PubMed:9315629}. PTM: Tyrosine phosphorylated by several non-receptor tyrosine kinases including LCK, FYN and JAK3. Also tyrosine phosphorylated by the non-receptor tyrosine kinase SRMS in an EGF-dependent manner (By similarity). Phosphorylation by PTK6 negatively regulates its RNA binding ability. Phosphorylation by PTK6 at Tyr-440 dictates the nuclear localization of KHDRBS1. Phosphorylation by MAPK1 at Ser-58, Thr-71 and Thr-84 regulates CD44 alternative splicing by promoting CD44 exon v5 inclusion. {ECO:0000250|UniProtKB:Q07666, ECO:0000269|PubMed:12478298, ECO:0000269|PubMed:7512695}.; PTM: Acetylated. Positively correlates with ability to bind RNA (By similarity). {ECO:0000250|UniProtKB:Q07666}.; PTM: Arginine methylation is required for nuclear localization. Inhibits interaction with Src-like SH3 domains, but not interaction with WW domains of WBP4/FBP21 AND FNBP4/FBP30 (By similarity). {ECO:0000250|UniProtKB:Q07666}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12496368}. Cytoplasm {ECO:0000250|UniProtKB:Q07666}. Membrane {ECO:0000269|PubMed:12496368}. Note=Predominantly located in the nucleus but also located partially in the cytoplasm. {ECO:0000250|UniProtKB:Q07666}. SUBUNIT: Self-associates to form homooligomers when bound to RNA, oligomerization appears to be limited when binding to proteins (PubMed:9315629). Interacts with KHDRBS3/SLIM-2 and KHDRBS2/SLIM-1; heterooligomer formation of KHDRBS family proteins may modulate RNA substrate specificity (PubMed:10077576, PubMed:24469635). Interacts with RASA1, FYN, GRB2, PLCG1, SRC, RBMY1A1, CBP, PRMT1 (PubMed:7799925, PubMed:7512695, PubMed:10077576, PubMed:10823932, PubMed:12496368, PubMed:12529443). Interacts with PTK6 (via SH3 and SH2 domains). Forms a complex with ILF2, ILF3, YLPM1, RBMX, NCOA5 and PPP1CA. Binds WBP4/FBP21 (via WW domains), FNBP4/FBP30 (via WW domains). Interacts (via Arg/Gly-rich-flanked Pro-rich regions) with FYN (via the SH3 domain). Interacts with APC, HNRNPA1 (By similarity). Interacts with the non-receptor tyrosine kinase SRMS; the interaction leads to phosphorylation of KHDRBS1 (By similarity). Interacts with ZBTB7A; negatively regulates KHDRBS1 splicing activity toward BCL2L1 (By similarity). {ECO:0000250|UniProtKB:Q07666, ECO:0000250|UniProtKB:Q91V33, ECO:0000269|PubMed:10077576, ECO:0000269|PubMed:12496368, ECO:0000269|PubMed:12529443, ECO:0000269|PubMed:24469635, ECO:0000269|PubMed:7512695, ECO:0000269|PubMed:7799925, ECO:0000269|PubMed:9315629}. DOMAIN: The KH domain is required for binding to RNA. {ECO:0000269|PubMed:9315629}.; DOMAIN: The Pro-rich domains are flanked by Arg/Gly-rich motifs which can be asymmetric dimethylated on arginine residues to give the DMA/Gly-rich regions. Selective methylation on these motifs can modulate protein-protein interactions (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: In adult cerebellum expressed in most neuronal cell populations, specifically in cerebellar granule cells of the internal granular layer, ROR(alpha)-positive Purkinje cells, internal granular layer and molecuar layer interneurons (at protein level). {ECO:0000269|PubMed:22196734}. NA +Q61024 ASNS_MOUSE Asparagine synthetase [glutamine-hydrolyzing] (EC 6.3.5.4) (Glutamine-dependent asparagine synthetase) 561 64,283 Active site (1); Binding site (3); Chain (1); Domain (2); Initiator methionine (1); Modified residue (3); Nucleotide binding (1); Region (2); Sequence conflict (1); Site (1) NA NA NA Amino-acid biosynthesis; L-asparagine biosynthesis; L-asparagine from L-aspartate (L-Gln route): step 1/1. NA NA NA NA NA NA NA +Q61753 SERA_MOUSE D-3-phosphoglycerate dehydrogenase (3-PGDH) (EC 1.1.1.95) (A10) 533 56,586 Active site (3); Binding site (4); Chain (1); Cross-link (2); Initiator methionine (1); Modified residue (5); Nucleotide binding (3); Sequence conflict (6) NA NA NA Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 1/3. FUNCTION: Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L-serine biosynthesis pathway. Does not catalyze the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate and the reversible oxidation of (S)-malate to oxaloacetate. {ECO:0000250|UniProtKB:O08651}. NA NA SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:O08651}. NA NA NA +Q62159 RHOC_MOUSE Rho-related GTP-binding protein RhoC (Silica-induced gene 61 protein) (SIG-61) 193 22,006 Chain (1); Lipidation (1); Modified residue (1); Motif (1); Nucleotide binding (3); Propeptide (1); Sequence conflict (1) NA NA NA NA FUNCTION: Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Serves as a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Regulates apical junction formation in bronchial epithelial cells. {ECO:0000269|PubMed:20974804}. NA SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cleavage furrow {ECO:0000250}. Note=Translocates to the equatorial region before furrow formation in a ECT2-dependent manner. {ECO:0000250}. SUBUNIT: Interacts with RTKN (PubMed:8662891). Interacts with AKAP13. Interacts with DIAPH1 (By similarity). Interacts with PKN2 (PubMed:20974804). Interacts with ROCK1 and ROCK2. Interacts with ARHGDIA. Interacts with RIPOR1 (By similarity). {ECO:0000250|UniProtKB:P08134, ECO:0000269|PubMed:20974804, ECO:0000269|PubMed:8662891}. NA NA NA +Q62192 CD180_MOUSE CD180 antigen (Lymphocyte antigen 78) (Ly-78) (Radioprotective 105 kDa protein) (CD antigen CD180) 661 74,302 Beta strand (29); Chain (1); Domain (2); Glycosylation (10); Helix (17); Repeat (19); Sequence conflict (5); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (13) NA TRANSMEM 627 650 Helical. {ECO:0000255}. TOPO_DOM 21 626 Extracellular.; TOPO_DOM 651 661 Cytoplasmic. NA FUNCTION: May cooperate with MD-1 and TLR4 to mediate the innate immune response to bacterial lipopolysaccharide (LPS) in B-cells. Leads to NF-kappa-B activation. Also involved in the life/death decision of B-cells. {ECO:0000269|PubMed:10880523}. NA SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SUBUNIT: M-shaped tetramer of two CD180-LY86 heterodimers. {ECO:0000269|PubMed:21959264}. NA TISSUE SPECIFICITY: B-lymphocytes and spleen. Not detected in thymus, kidney, muscle, heart, brain or liver. NA +Q62266 SPR1A_MOUSE Cornifin-A (Small proline-rich protein 1A) (SPR1 A) (SPR1A) 144 15,765 Chain (1); Region (1); Repeat (13) NA NA NA NA FUNCTION: Cross-linked envelope protein of keratinocytes. It is a keratinocyte protein that first appears in the cell cytosol, but ultimately becomes cross-linked to membrane proteins by transglutaminase. All that results in the formation of an insoluble envelope beneath the plasma membrane. May participate widely in the construction of cell envelopes in cornifying epithelia characterized by either increased thickness or a requirement for extreme flexibility. NA SUBCELLULAR LOCATION: Cytoplasm. NA NA TISSUE SPECIFICITY: Expressed in fetal periderm, hair follicles and in the thickened epidermis of the lip and footpad. Also present in the epithelia of various tissues such as the penis, vagina, forestomach, tongue and esophagus. {ECO:0000269|PubMed:8601731}. NA +Q684Q6 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q69ZD1 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q69ZN7 MYOF_MOUSE Myoferlin (Fer-1-like protein 3) 2048 233,324 Alternative sequence (6); Chain (1); Compositional bias (5); Domain (5); Erroneous initiation (1); Frameshift (1); Modified residue (5); Mutagenesis (1); Region (1); Sequence conflict (2); Topological domain (2); Transmembrane (1) NA TRANSMEM 2013 2033 Helical. {ECO:0000255}. TOPO_DOM 1 2012 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 2034 2048 Extracellular. {ECO:0000255}. NA FUNCTION: Calcium/phospholipid-binding protein that plays a role in the plasmalemma repair mechanism of endothelial cells that permits rapid resealing of membranes disrupted by mechanical stress. Involved in endocytic recycling. Implicated in VEGF signal transduction by regulating the levels of the receptor KDR. {ECO:0000269|PubMed:16280346, ECO:0000269|PubMed:17702744, ECO:0000269|PubMed:18502764}. NA SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Found at nuclear and plasma membranes. Enriched in undifferentiated myoblasts near the plasma membrane in puncate structures (By similarity). Concentrated at the membrane sites of both myoblast-myoblast and myoblast-myotube fusions. Detected at the plasmalemma in endothelial cells lining intact blood vessels. {ECO:0000250, ECO:0000269|PubMed:16280346, ECO:0000269|PubMed:17702744}. SUBUNIT: Interacts with EHD1 (PubMed:21177873). Interacts with EHD2; the interaction is direct (PubMed:21177873). Interacts with DNM2 and KDR (PubMed:21177873). Interacts with RIPOR2 (By similarity). {ECO:0000250|UniProtKB:Q9NZM1, ECO:0000269|PubMed:17702744, ECO:0000269|PubMed:21177873}. DOMAIN: The C2 1 domain associates with lipid membranes in a calcium-dependent manner. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in myoblasts (at protein level). Expressed in endothelial cells. {ECO:0000269|PubMed:16280346, ECO:0000269|PubMed:17702744}. NA +Q6P1F5 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q6P8Q0 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q6PDL0 DC1L2_MOUSE Cytoplasmic dynein 1 light intermediate chain 2 (Dynein light intermediate chain 2, cytosolic) 492 54,218 Chain (1); Modified residue (7); Nucleotide binding (1); Sequence conflict (1) NA NA NA NA FUNCTION: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in binding dynein to membranous organelles or chromosomes (By similarity). {ECO:0000250}. NA SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. SUBUNIT: Homodimer (By similarity). The cytoplasmic dynein 1 complex consists of two catalytic heavy chains (HCs) and a number of non-catalytic subunits presented by intermediate chains (ICs), light intermediate chains (LICs) and light chains (LCs); the composition seems to vary in respect to the IC, LIC and LC composition. The heavy chain homodimer serves as a scaffold for the probable homodimeric assembly of the respective non-catalytic subunits. The ICs and LICs bind directly to the HC dimer and the LCs assemble on the IC dimer. Self-associates. Interacts with DYNC1H1; DYNC1LI1 and DYNC1LI2 bind mutually exclusive to DYNC1H1 (By similarity). {ECO:0000250}. NA NA NA +Q6PE01 SNR40_MOUSE U5 small nuclear ribonucleoprotein 40 kDa protein (U5 snRNP 40 kDa protein) (WD repeat-containing protein 57) 358 39,276 Chain (1); Cross-link (2); Frameshift (1); Modified residue (1); Repeat (7); Sequence conflict (2) NA NA NA NA FUNCTION: Component of the U5 small nuclear ribonucleoprotein (snRNP) complex. The U5 snRNP is part of the spliceosome, a multiprotein complex that catalyzes the removal of introns from pre-messenger RNAs (By similarity). {ECO:0000250}. NA SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Identified in the spliceosome C complex. Associated with the spliceosome complex. Part of the U5 snRNP complex. Interacts with PRPF8. Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, WDR57, SNRNP40, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39 (By similarity). {ECO:0000250}. NA NA NA +Q7TMX4 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q7TPX2 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q80UW7 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q80V26 IMPA3_MOUSE Inositol monophosphatase 3 (IMP 3) (IMPase 3) (EC 3.1.3.25) (EC 3.1.3.7) (Golgi 3-prime phosphoadenosine 5-prime phosphate 3-prime phosphatase) (Golgi-resident PAP phosphatase) (gPAPP) (Inositol monophosphatase domain-containing protein 1) (Inositol-1(or 4)-monophosphatase 3) (Myo-inositol monophosphatase A3) 356 38,616 Binding site (2); Chain (1); Glycosylation (1); Metal binding (6); Modified residue (1); Region (1); Topological domain (2); Transmembrane (1) NA TRANSMEM 13 33 Helical. {ECO:0000255}. TOPO_DOM 1 12 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 34 356 Lumenal. {ECO:0000255}. Polyol metabolism; myo-inositol biosynthesis; myo-inositol from D-glucose 6-phosphate: step 2/2. FUNCTION: May play a role in the formation of skeletal elements derived through endochondral ossification, possibly by clearing adenosine 3',5'-bisphosphate produced by Golgi sulfotransferases during glycosaminoglycan sulfation. {ECO:0000269|PubMed:18695242}. PTM: Contains N-linked glycan resistant to endoglycosydase H. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:18695242}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. NA NA NA NA +Q80X54 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q80X95 RRAGA_MOUSE Ras-related GTP-binding protein A (Rag A) (RagA) 313 36,566 Chain (1); Cross-link (4); Erroneous initiation (1); Frameshift (1); Modified residue (1); Nucleotide binding (3) NA NA NA NA FUNCTION: Guanine nucleotide-binding protein that plays a crucial role in the cellular response to amino acid availability through regulation of the mTORC1 signaling cascade. Forms heterodimeric Rag complexes with RRAGC or RRAGD and cycles between an inactive GDP-bound and an active GTP-bound form. In its active form participates in the relocalization of mTORC1 to the lysosomes and its subsequent activation by the GTPase RHEB. Involved in the RCC1/Ran-GTPase pathway. May play a direct role in a TNF-alpha signaling pathway leading to induction of cell death. {ECO:0000250|UniProtKB:Q7L523}. PTM: Ubiquitinated. 'Lys-68'-linked polyubiquitination of the GDP-bound inactive form of RRAGA at Lys-142, Lys-220, Lys-230 and Lys-244 by RNF152 is increased in response to amino acid starvation. Polyubiquitination promotes interaction with the GATOR1 complex. This does not affect RRAGA degradation. {ECO:0000250|UniProtKB:Q7L523}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Lysosome {ECO:0000250}. Note=Predominantly cytoplasmic. May shuttle between the cytoplasm and nucleus, depending on the bound nucleotide state (By similarity). {ECO:0000250}. SUBUNIT: Can occur as a homodimer or as a heterodimer with RRAGC or RRAGD in a sequence-independent manner; heterodimerization stabilizes proteins of the heterodimer. In complex with RRAGC, but not with RRAGB, interacts with RPTOR. The GTP-bound form of RRAGA interacts with NOL8. Interacts with SH3BP4; the interaction with this negative regulator is most probably direct, preferentially occurs with the inactive GDP-bound form of RRAGA and is negatively regulated by amino acids. The Rag heterodimer interacts with SLC38A9; the probable amino acid sensor. Interacts (inactive GDP-bound form) with RNF152; stimulated by amino acid starvation. Interacts (polyubiquitinated) with the GATOR1 complex; inactivates RRAGA. Interacts (polyubiquitinated) with TSC2 (By similarity). Interacts with SESN1, SESN2 AND SESN3 (PubMed:25259925). {ECO:0000250|UniProtKB:Q7L523, ECO:0000269|PubMed:25259925}. NA NA NA +Q8BG07 PLD4_MOUSE Phospholipase D4 (PLD 4) (EC 3.1.4.4) (Choline phosphatase 4) (Phosphatidylcholine-hydrolyzing phospholipase D4) 503 56,154 Active site (6); Alternative sequence (1); Chain (1); Domain (2); Frameshift (1); Sequence conflict (7); Transmembrane (1) NA TRANSMEM 37 57 Helical. {ECO:0000255}. NA NA NA NA SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. NA NA NA NA +Q8BHC4 DCAKD_MOUSE Dephospho-CoA kinase domain-containing protein 231 26,476 Chain (1); Domain (1); Nucleotide binding (1) NA NA NA NA NA NA NA NA NA NA NA +Q8BTU4 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q8BUM1 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q8BVK3 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q8BXC0 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q8C0M2 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q8CD23 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q8CGA1 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q8CHW4 EI2BE_MOUSE Translation initiation factor eIF-2B subunit epsilon (eIF-2B GDP-GTP exchange factor subunit epsilon) 717 80,086 Chain (1); Cross-link (5); Domain (1); Modified residue (11); Sequence conflict (1) NA NA NA NA FUNCTION: Catalyzes the exchange of eukaryotic initiation factor 2-bound GDP for GTP. {ECO:0000250}. PTM: Phosphorylated at Ser-540 by DYRK2; this is required for subsequent phosphorylation by GSK3B. Phosphorylated on serine and threonine residues by GSK3B; phosphorylation inhibits its function (By similarity). {ECO:0000250}.; PTM: Polyubiquitinated, probably by NEDD4. {ECO:0000250}. NA SUBUNIT: Complex of five different subunits; alpha, beta, gamma, delta and epsilon. Interacts with RGS2 (By similarity). {ECO:0000250}. NA NA NA +Q8K403 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q8K4Z5 SF3A1_MOUSE Splicing factor 3A subunit 1 (SF3a120) 791 88,545 Beta strand (6); Chain (1); Compositional bias (6); Cross-link (6); Domain (1); Helix (4); Modified residue (9); Repeat (2); Sequence conflict (3); Site (1); Turn (1) NA NA NA NA FUNCTION: Subunit of the splicing factor SF3A required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA. May also be involved in the assembly of the 'E' complex (By similarity). {ECO:0000250}. NA SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Identified in the spliceosome C complex (By similarity). Component of splicing factor SF3A which is composed of three subunits; SF3A3/SAP61, SF3A2/SAP62, SF3A1/SAP114. SF3A associates with the splicing factor SF3B and a 12S RNA unit to form the U2 small nuclear ribonucleoproteins complex (U2 snRNP). Interacts with SF3A3 (By similarity). {ECO:0000250}. DOMAIN: SURP motif 2 mediates direct binding to SF3A3. {ECO:0000250}. NA NA +Q8R3G9 TSN8_MOUSE Tetraspanin-8 (Tspan-8) 235 25,582 Chain (1); Glycosylation (1); Topological domain (5); Transmembrane (4) NA TRANSMEM 13 33 Helical. {ECO:0000255}.; TRANSMEM 53 73 Helical. {ECO:0000255}.; TRANSMEM 85 105 Helical. {ECO:0000255}.; TRANSMEM 204 224 Helical. {ECO:0000255}. TOPO_DOM 1 12 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 34 52 Extracellular. {ECO:0000255}.; TOPO_DOM 74 84 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 106 203 Extracellular. {ECO:0000255}.; TOPO_DOM 225 235 Cytoplasmic. {ECO:0000255}. NA NA NA SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. NA NA NA NA +Q8R480 NUP85_MOUSE Nuclear pore complex protein Nup85 (85 kDa nucleoporin) (FROUNT) (Nucleoporin Nup85) (Pericentrin-1) 656 74,776 Chain (1); Erroneous gene model prediction (2); Modified residue (2); Sequence conflict (1) NA NA NA NA FUNCTION: Essential component of the nuclear pore complex (NPC) that seems to be required for NPC assembly and maintenance. As part of the NPC Nup107-160 subcomplex plays a role in RNA export and in tethering NUP96/Nup98 and NUP153 to the nucleus. The Nup107-160 complex seems to be required for spindle assembly during mitosis. NUP85 is required for membrane clustering of CCL2-activated CCR2. Seems to be involved in CCR2-mediated chemotaxis of monocytes and may link activated CCR2 to the phosphatidyl-inositol 3-kinase-Rac-lammellipodium protrusion cascade. {ECO:0000250|UniProtKB:Q9BW27}. NA SUBCELLULAR LOCATION: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q9BW27}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q9BW27}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9BW27}. Cytoplasm {ECO:0000250|UniProtKB:Q9BW27}. Nucleus membrane {ECO:0000250|UniProtKB:Q9BW27}. Note=During mitosis, localizes to the kinetochores and spindle poles. Upon CCl2 stimulation translocates from the cytoplasm to the membrane and colocalizes with CCR2 at the front of migrating cells. {ECO:0000250|UniProtKB:Q9BW27}. SUBUNIT: Component of the nuclear pore complex (NPC). Component of the NPC Nup107-160 subcomplex, consisting of at least NUP107, NUP98/Nup96, NUP160, NUP133, NUP85, NUP37, NUP43 and SEC13. Interacts with NUP160, NUP133 and SEC13 (PubMed:12718872). Interacts with NUP37, NUP107 and NUP43. Interacts with CCR2. {ECO:0000250|UniProtKB:Q9BW27, ECO:0000269|PubMed:12718872}. NA NA NA +Q8VC49 IF27B_MOUSE Interferon alpha-inducible protein 27-like protein 2B (Interferon-stimulated gene 12 protein B2) (ISG12(b2)) 283 27,772 Chain (1); Transit peptide (1); Transmembrane (3) NA TRANSMEM 130 150 Helical. {ECO:0000255}.; TRANSMEM 176 196 Helical. {ECO:0000255}.; TRANSMEM 202 222 Helical. {ECO:0000255}. NA NA FUNCTION: Functions in the intrinsic apoptotic signaling pathway and may have an interferon-induced antiviral activity. {ECO:0000269|PubMed:21151029}. NA SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:21151029}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Homooligomer (PubMed:21151029). Interacts with BAK1 (PubMed:21151029). Interacts with BAX (PubMed:21151029). Interacts with adenine nucleotide translocase (PubMed:21151029). {ECO:0000269|PubMed:21151029}. NA NA NA +Q8VC49 IF27B_MOUSE Interferon alpha-inducible protein 27-like protein 2B (Interferon-stimulated gene 12 protein B2) (ISG12(b2)) 283 27,772 Chain (1); Transit peptide (1); Transmembrane (3) NA TRANSMEM 130 150 Helical. {ECO:0000255}.; TRANSMEM 176 196 Helical. {ECO:0000255}.; TRANSMEM 202 222 Helical. {ECO:0000255}. NA NA FUNCTION: Functions in the intrinsic apoptotic signaling pathway and may have an interferon-induced antiviral activity. {ECO:0000269|PubMed:21151029}. NA SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:21151029}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Homooligomer (PubMed:21151029). Interacts with BAK1 (PubMed:21151029). Interacts with BAX (PubMed:21151029). Interacts with adenine nucleotide translocase (PubMed:21151029). {ECO:0000269|PubMed:21151029}. NA NA NA +Q8VC73 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q8VC73 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q8VCB1 NDC1_MOUSE Nucleoporin NDC1 (Transmembrane protein 48) 673 75,409 Chain (1); Modified residue (8); Topological domain (7); Transmembrane (6) NA TRANSMEM 26 46 Helical; Name=1. {ECO:0000255}.; TRANSMEM 72 92 Helical; Name=2. {ECO:0000255}.; TRANSMEM 116 136 Helical; Name=3. {ECO:0000255}.; TRANSMEM 167 187 Helical; Name=4. {ECO:0000255}.; TRANSMEM 227 247 Helical; Name=5. {ECO:0000255}.; TRANSMEM 262 282 Helical; Name=6. {ECO:0000255}. TOPO_DOM 1 25 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 47 71 Perinuclear space. {ECO:0000255}.; TOPO_DOM 93 115 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 137 166 Perinuclear space. {ECO:0000255}.; TOPO_DOM 188 226 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 248 261 Perinuclear space. {ECO:0000255}.; TOPO_DOM 283 673 Cytoplasmic. {ECO:0000255}. NA FUNCTION: Component of the nuclear pore complex (NPC), which plays a key role in de novo assembly and insertion of NPC in the nuclear envelope. Required for NPC and nuclear envelope assembly, possibly by forming a link between the nuclear envelope membrane and soluble nucleoporins, thereby anchoring the NPC in the membrane (By similarity). {ECO:0000250}. PTM: Phosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nuclear pore complex {ECO:0000250}. Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Central core structure of the nuclear pore complex. {ECO:0000250}. SUBUNIT: Interacts with the NUP35/NUP53. {ECO:0000250|UniProtKB:Q6AXN4}. NA NA NA +Q8VCN3 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q8VDP4 CCAR2_MOUSE Cell cycle and apoptosis regulator protein 2 (Cell division cycle and apoptosis regulator protein 2) 922 103,002 Chain (1); Coiled coil (2); Cross-link (2); Erroneous initiation (2); Modified residue (17); Region (2); Sequence conflict (3) NA NA NA NA FUNCTION: Core component of the DBIRD complex, a multiprotein complex that acts at the interface between core mRNP particles and RNA polymerase II (RNAPII) and integrates transcript elongation with the regulation of alternative splicing: the DBIRD complex affects local transcript elongation rates and alternative splicing of a large set of exons embedded in (A + T)-rich DNA regions. Inhibits SIRT1 deacetylase activity leading to increasing levels of p53/TP53 acetylation and p53-mediated apoptosis (By similarity). As part of a histone H3-specific methyltransferase complex may mediate ligand-dependent transcriptional activation by nuclear hormone receptors (By similarity). Inhibits SUV39H1 methyltransferase activity. Plays a critical role in maintaining genomic stability and cellular integrity following UV-induced genotoxic stress (By similarity) Regulates the circadian expression of the core clock components NR1D1 and ARNTL/BMAL1. Enhances the transcriptional repressor activity of NR1D1 through stabilization of NR1D1 protein levels by preventing its ubiquitination and subsequent degradation. Acts as a regulator of PCK1 expression and gluconeogenesis by a mechanism that involves, at least in part, both NR1D1 and SIRT1 (PubMed:24415752). Negatively regulates the deacetylase activity of HDAC3 and can alter its subcellular localization (PubMed:21030595). Plays an important role in tumor suppression through p53/TP53 regulation; stabilizes p53/TP53 by affecting its interaction with ubiquitin ligase MDM2 (PubMed:25732823). Represses the ligand-dependent transcriptional activation function of ESR2. Positively regulates the beta-catenin pathway (canonical Wnt signaling pathway) and is required for MCC-mediated repression of the beta-catenin pathway. Represses ligand-dependent transcriptional activation function of NR1H2 and NR1H3 and inhibits the interaction of SIRT1 with NR1H3. Represses the transcriptional activator activity of BRCA1. Inhibits SIRT1 in a CHEK2 and PSEM3-dependent manner and inhibits the activity of CHEK2 in vitro (By similarity). {ECO:0000250|UniProtKB:Q8N163, ECO:0000269|PubMed:23398316}. PTM: Acetylation at Lys-112 and Lys-215 by KAT8 prevents inhibitory binding to SIRT1 and increases its deacetylase activity. {ECO:0000250|UniProtKB:Q8N163}.; PTM: Genotoxic stress induces its sumoylation and sumoylation promotes the SIRT1-CCAR2 interaction which in turn inhibits SIRT1-mediated deacetylation of p53/TP53. Sumoylation leads to transcriptional activation of p53/TP53 by sequestering SIRT1 from p53/TP53. Desumoylated by SENP1. {ECO:0000250|UniProtKB:Q8N163}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8N163}. Cytoplasm {ECO:0000250|UniProtKB:Q8N163}. Note=Recruited to chromatin, post-UV irradiation. Sequestered to the cytoplasm in the presence of MCC. Translocated to the cytoplasm during UV-induced apoptosis. {ECO:0000250|UniProtKB:Q8N163}. SUBUNIT: Component of the DBIRD complex. Interacts with ZNF326/ZIRD; the interaction is direct. Interacts (via N-terminus) with SIRT1, which inhibits the deacetylation of substrates. Interacts (via N-terminus) with SUV39H1; this interaction abolishes the interaction with SIRT1. Part of a complex composed at least of ASCL2, EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; this complex may have a histone H3-specific methyltransferase activity. Interacts with NR1D1. Interacts (via N-terminus) with ESR1 and ESR2. Interacts (via N-terminus) with HDAC3 (via C-terminus). Interacts with HDAC1 and MED2F. Interacts with MCC. Interacts (via N-terminus) with NR1H2 and NR1H3 in a ligand-independent manner. Interacts with CSNK2A1. Interacts (via N-terminus) with p53/TP53. Interacts (via N-terminus) with BRCA1 (via the BRCT domains). Interacts (via N-terminus) with CHEK2 (via protein kinase domain). Interacts with PSEM3. Interacts (via N-terminus) with PSIA3 and SENP1. The sumoylated form shows a preferential interaction with SIRT1 as compared to its unmodified form (By similarity). {ECO:0000250|UniProtKB:Q8N163, ECO:0000269|PubMed:19218236, ECO:0000269|PubMed:21030595, ECO:0000269|PubMed:23398316, ECO:0000269|PubMed:24415752, ECO:0000269|PubMed:25732823}. NA NA NA +Q8VDU3 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q8VHM5 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q8VI94 OASL1_MOUSE 2'-5'-oligoadenylate synthase-like protein 1 (2',5'-oligoadenylate synthetase-like 9) 511 59,088 Chain (1); Domain (2); Frameshift (1); Sequence conflict (19) NA NA NA NA FUNCTION: Does not have 2'-5'-OAS activity, but can bind double-stranded RNA. Displays antiviral activity via an alternative antiviral pathway independent of RNase L. {ECO:0000269|PubMed:12396720, ECO:0000269|PubMed:12799444}. NA SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Cytoplasm {ECO:0000250}. SUBUNIT: Specifically interacts with the ligand binding domain of the thyroid receptor (TR). TRIP14 does not require the presence of thyroid hormone for its interaction. Binds MBD1 (By similarity). {ECO:0000250}. NA NA NA +Q8VIJ6 SFPQ_MOUSE Splicing factor, proline- and glutamine-rich (DNA-binding p52/p100 complex, 100 kDa subunit) (Polypyrimidine tract-binding protein-associated-splicing factor) (PSF) (PTB-associated-splicing factor) 699 75,442 Chain (1); Coiled coil (1); Compositional bias (11); Cross-link (3); Domain (2); Modified residue (32); Region (1); Repeat (3); Sequence conflict (2) NA NA NA NA FUNCTION: DNA- and RNA binding protein, involved in several nuclear processes. Essential pre-mRNA splicing factor required early in spliceosome formation and for splicing catalytic step II, probably as a heteromer with NONO. Binds to pre-mRNA in spliceosome C complex, and specifically binds to intronic polypyrimidine tracts. Involved in regulation of signal-induced alternative splicing. During splicing of PTPRC/CD45, a phosphorylated form is sequestered by THRAP3 from the pre-mRNA in resting T-cells; T-cell activation and subsequent reduced phosphorylation is proposed to lead to release from THRAP3 allowing binding to pre-mRNA splicing regulatotry elements which represses exon inclusion. Interacts with U5 snRNA, probably by binding to a purine-rich sequence located on the 3' side of U5 snRNA stem 1b. May be involved in a pre-mRNA coupled splicing and polyadenylation process as component of a snRNP-free complex with SNRPA/U1A. The SFPQ-NONO heteromer associated with MATR3 may play a role in nuclear retention of defective RNAs. SFPQ may be involved in homologous DNA pairing; in vitro, promotes the invasion of ssDNA between a duplex DNA and produces a D-loop formation. The SFPQ-NONO heteromer may be involved in DNA unwinding by modulating the function of topoisomerase I/TOP1; in vitro, stimulates dissociation of TOP1 from DNA after cleavage and enhances its jumping between separate DNA helices. The SFPQ-NONO heteromer binds DNA. The SFPQ-NONO heteromer may be involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination and may stabilize paired DNA ends; in vitro, the complex strongly stimulates DNA end joining, binds directly to the DNA substrates and cooperates with the Ku70/G22P1-Ku80/XRCC5 (Ku) dimer to establish a functional preligation complex. SFPQ is involved in transcriptional regulation. Functions as transcriptional activator (By similarity). Transcriptional repression is mediated by an interaction of SFPQ with SIN3A and subsequent recruitment of histone deacetylases (HDACs). The SFPQ-NONO-NR5A1 complex binds to the CYP17 promoter and regulates basal and cAMP-dependent transcriptional activity. SFPQ isoform Long binds to the DNA binding domains (DBD) of nuclear hormone receptors, like RXRA and probably THRA, and acts as transcriptional corepressor in absence of hormone ligands. Binds the DNA sequence 5'-CTGAGTC-3' in the insulin-like growth factor response element (IGFRE) and inhibits IGF-I-stimulated transcriptional activity (By similarity). Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex through histone deacetylation (PubMed:21680841, PubMed:22966205). Required for the assembly of nuclear speckles (By similarity). Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway (By similarity). {ECO:0000250|UniProtKB:P23246, ECO:0000269|PubMed:21680841, ECO:0000269|PubMed:22966205}. PTM: Phosphorylated on multiple serine and threonine residues during apoptosis (By similarity). Phosphorylation of C-terminal tyrosines promotes its cytoplasmic localization, impaired its binding to polypyrimidine RNA and led to cell cycle arrest (By similarity). In resting T-cells is phosphorylated at Thr-679 by GSK3B which is proposed to promote association with THRAP and to prevent binding to PTPRC/CD45 pre-mRNA; T-cell activation leads to reduced phosphorylation at Thr-679. {ECO:0000250|UniProtKB:P23246}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:P23246}. Nucleus matrix {ECO:0000269|PubMed:21680841}. Cytoplasm {ECO:0000250|UniProtKB:P23246}. Note=Predominantly in nuclear matrix. {ECO:0000250|UniProtKB:P23246}. SUBUNIT: Heterodimer with NONO. Monomer and component of the SFPQ-NONO complex, which is probably a heterotetramer of two 52 kDa (NONO) and two 100 kDa (SFPQ) subunits. The coiled coil domain mediates interaction with NONO, and can also mediate formation of long, linear homooligomers (in vitro). SFPQ is a component of spliceosome and U5.4/6 snRNP complexes. Interacts with SNRPA/U1A. Component of a snRNP-free complex with SNRPA/U1A. Part of complex consisting of SFPQ, NONO and MATR3. Interacts with polypyrimidine tract-binding protein 1/PTB. Part of a complex consisting of SFPQ, NONO and NR5A1. Interacts with RXRA, probably THRA, and SIN3A. Interacts with TOP1. Part of a complex consisting of SFPQ, NONO and TOP1. Interacts with SNRNP70 in apoptotic cells. Interacts with PSPC1 (PubMed:15140795). Interacts with RNF43 (By similarity). Interacts with PITX3 and NR4A2/NURR1 (PubMed:19144721). Interacts with PTK6. Interacts with THRAP3; the interaction is dependent on SFPQ phosphorylation at 'Thr-687' and inhibits binding of SFPQ to a ESS1 exonic splicing silencer element-containing RNA (By similarity). The large PER complex involved in the histone deacetylation is composed of at least HDAC1, PER2, SFPQ and SIN3A (PubMed:21680841). Interacts with PER1 and PER2 (PubMed:22966205). Part of the HDP-RNP complex composed of at least HEXIM1, PRKDC, XRCC5, XRCC6, paraspeckle proteins (SFPQ, NONO, PSPC1, RBM14, and MATR3) and NEAT1 RNA (By similarity). Interacts with PQBP1. Component of a multiprotein complex with NONO and WASL (By similarity). {ECO:0000250|UniProtKB:P23246, ECO:0000269|PubMed:15140795, ECO:0000269|PubMed:19144721, ECO:0000269|PubMed:21680841, ECO:0000269|PubMed:22966205}. DOMAIN: The coiled coil domain mediates interaction with NONO, and can also mediate formation of long, linear homooligomers (in vitro). The coiled coil domain is required for optimal DNA binding, and optimal transcription activation. {ECO:0000250|UniProtKB:P23246}. NA NA +Q91VM5 RMXL1_MOUSE RNA binding motif protein, X-linked-like-1 (Heterogeneous nuclear ribonucleoprotein G-like 1) (RNA binding motif protein, X chromosome retrogene) 388 42,162 Chain (1); Cross-link (1); Domain (1); Modified residue (1); Sequence conflict (5) NA NA NA NA FUNCTION: RNA-binding protein which may be involved in pre-mRNA splicing. {ECO:0000250}. NA SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. NA NA NA NA +Q91YL3 UCKL1_MOUSE Uridine-cytidine kinase-like 1 (EC 2.7.1.48) 548 60,842 Chain (1); Modified residue (3); Nucleotide binding (1) NA NA NA Pyrimidine metabolism; UMP biosynthesis via salvage pathway; UMP from uridine: step 1/1. FUNCTION: May contribute to UTP accumulation needed for blast transformation and proliferation. {ECO:0000250}. PTM: Ubiquitinated by RNF19B; which induces proteasomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Interacts with RNF19B. {ECO:0000250}. NA NA NA +Q91YR9 PTGR1_MOUSE Prostaglandin reductase 1 (PRG-1) (EC 1.3.1.-) (15-oxoprostaglandin 13-reductase) (EC 1.3.1.48) (NADP-dependent leukotriene B4 12-hydroxydehydrogenase) (EC 1.3.1.74) 329 35,560 Binding site (4); Chain (1); Modified residue (2); Nucleotide binding (3); Sequence conflict (2) NA NA NA NA FUNCTION: Functions as 15-oxo-prostaglandin 13-reductase and acts on 15-oxo-PGE1, 15-oxo-PGE2 and 15-oxo-PGE2-alpha. Has no activity towards PGE1, PGE2 and PGE2-alpha. Catalyzes the conversion of leukotriene B4 into its biologically less active metabolite, 12-oxo-leukotriene B4. This is an initial and key step of metabolic inactivation of leukotriene B4 (By similarity). {ECO:0000250}. NA SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Monomer or homodimer. {ECO:0000250}. NA NA NA +Q91YR9 PTGR1_MOUSE Prostaglandin reductase 1 (PRG-1) (EC 1.3.1.-) (15-oxoprostaglandin 13-reductase) (EC 1.3.1.48) (NADP-dependent leukotriene B4 12-hydroxydehydrogenase) (EC 1.3.1.74) 329 35,560 Binding site (4); Chain (1); Modified residue (2); Nucleotide binding (3); Sequence conflict (2) NA NA NA NA FUNCTION: Functions as 15-oxo-prostaglandin 13-reductase and acts on 15-oxo-PGE1, 15-oxo-PGE2 and 15-oxo-PGE2-alpha. Has no activity towards PGE1, PGE2 and PGE2-alpha. Catalyzes the conversion of leukotriene B4 into its biologically less active metabolite, 12-oxo-leukotriene B4. This is an initial and key step of metabolic inactivation of leukotriene B4 (By similarity). {ECO:0000250}. NA SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Monomer or homodimer. {ECO:0000250}. NA NA NA +Q920X5 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q925B0 PAWR_MOUSE PRKC apoptosis WT1 regulator protein (Prostate apoptosis response 4 protein) (Par-4) 333 35,908 Alternative sequence (1); Chain (1); Coiled coil (1); Modified residue (2); Motif (2); Region (2) NA NA NA NA FUNCTION: Pro-apoptopic protein capable of selectively inducing apoptosis in cancer cells, sensitizing the cells to diverse apoptotic stimuli and causing regression of tumors in animal models. Induces apoptosis in certain cancer cells by activation of the Fas prodeath pathway and coparallel inhibition of NF-kappa-B transcriptional activity. Inhibits the transcriptional activation and augments the transcriptional repression mediated by WT1. Down-regulates the anti-apoptotic protein BCL2 via its interaction with WT1. Seems also to be a transcriptional repressor by itself. May be directly involved in regulating the amyloid precursor protein (APP) cleavage activity of BACE1 (By similarity). {ECO:0000250, ECO:0000269|PubMed:15606896}. PTM: Preferentially phosphorylated at the Thr-156 by PKC in cancer cells. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Mainly cytoplasmic in absence of apoptosis signal and in normal cells. Nuclear in most cancer cell lines. Nuclear entry seems to be essential but not sufficient for apoptosis. Nuclear localization includes nucleoplasm and PML nuclear bodies (By similarity). {ECO:0000250}. SUBUNIT: Homooligomer. Interacts (via the C-terminal region) with WT1. Interacts with THAP1. Interacts with AATF. Interacts with BACE1. Interacts with SPSB1 (via B30.2/SPRY domain); this interaction is direct and occurs in association with the Elongin BC complex (PubMed:16369487, PubMed:20561531). Interacts with SPSB2 (via B30.2/SPRY domain); this interaction occurs in association with the Elongin BC complex (PubMed:16369487, PubMed:20561531). Interacts with SPSB4 (via B30.2/SPRY domain); this interaction occurs in association with the Elongin BC complex (PubMed:16369487, PubMed:20561531). Component of a ternary complex composed of SQSTM1 and PRKCZ (By similarity). Interacts with actin (By similarity). {ECO:0000250|UniProtKB:Q62627, ECO:0000250|UniProtKB:Q96IZ0}. DOMAIN: The leucine-zipper domain is not essential for apoptosis, but is required for sensitization of cells to exogenous apoptotic insults and for interaction with its partners. {ECO:0000250}.; DOMAIN: The SAC domain is a death-inducing domain selective for apoptosis induction in cancer cells. This domain is essential for nuclear entry, Fas activation, inhibition of NF-kappa-B activity and induction of apoptosis in cancer cells (By similarity). {ECO:0000250}.; DOMAIN: The B30.2/SPRY domain-binding motif mediates recognition by proteins containing a B30.2/SPRY domain. {ECO:0000250|UniProtKB:Q96IZ0}. NA NA +Q99JG3 ANX13_MOUSE Annexin A13 (Annexin XIII) (Annexin-13) 317 35,922 Chain (1); Initiator methionine (1); Lipidation (1); Repeat (4) NA NA NA NA NA NA SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Note=Associated with the plasma membrane of undifferentiated, proliferating crypt epithelial cells as well as differentiated villus enterocytes. {ECO:0000250}. NA DOMAIN: A pair of annexin repeats may form one binding site for calcium and phospholipid. NA NA +Q99JW5 EPCAM_MOUSE Epithelial cell adhesion molecule (Ep-CAM) (Epithelial glycoprotein 314) (EGP314) (mEGP314) (Protein 289A) (Tumor-associated calcium signal transducer 1) (CD antigen CD326) 315 35,019 Chain (1); Disulfide bond (6); Domain (1); Glycosylation (2); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) NA TRANSMEM 267 289 Helical. {ECO:0000255}. TOPO_DOM 24 266 Extracellular. {ECO:0000255}.; TOPO_DOM 290 315 Cytoplasmic. {ECO:0000255}. NA FUNCTION: May act as a physical homophilic interaction molecule between intestinal epithelial cells (IECs) and intraepithelial lymphocytes (IELs) at the mucosal epithelium for providing immunological barrier as a first line of defense against mucosal infection. Plays a role in embryonic stem cells proliferation and differentiation. Up-regulates the expression of FABP5, MYC and cyclins A and E (By similarity). {ECO:0000250}. PTM: Glycosylation at Asn-198 is crucial for protein stability. {ECO:0000250}. SUBCELLULAR LOCATION: Lateral cell membrane {ECO:0000250|UniProtKB:P16422}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P16422}. Cell junction, tight junction {ECO:0000250|UniProtKB:P16422}. Note=Colocalizes with CLDN7 at the lateral cell membrane and tight junction. {ECO:0000250|UniProtKB:P16422}. SUBUNIT: Monomer. Interacts with phosphorylated CLDN7 (By similarity). {ECO:0000250}. NA NA NA +Q99K86 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q99KP6 PRP19_MOUSE Pre-mRNA-processing factor 19 (EC 2.3.2.27) (Nuclear matrix protein 200) (PRP19/PSO4 homolog) (RING-type E3 ubiquitin transferase PRP19) (Senescence evasion factor) 504 55,239 Alternative sequence (2); Chain (1); Domain (1); Initiator methionine (1); Modified residue (5); Region (1); Repeat (7) NA NA NA Protein modification; protein ubiquitination. FUNCTION: Isoform 1: Ubiquitin-protein ligase which is a core component of several complexes mainly involved in pre-mRNA splicing and DNA repair. Core component of the PRP19C/Prp19 complex/NTC/Nineteen complex which is part of the spliceosome and participates in its assembly, its remodeling and is required for its activity. During assembly of the spliceosome, mediates 'Lys-63'-linked polyubiquitination of the U4 spliceosomal protein PRPF3. Ubiquitination of PRPF3 allows its recognition by the U5 component PRPF8 and stabilizes the U4/U5/U6 tri-snRNP spliceosomal complex. Recruited to RNA polymerase II C-terminal domain (CTD) and the pre-mRNA, it may also couple the transcriptional and spliceosomal machineries. The XAB2 complex, which contains PRPF19, is also involved in pre-mRNA splicing, transcription and transcription-coupled repair. Beside its role in pre-mRNA splicing PRPF19, as part of the PRP19-CDC5L complex, plays a role in the DNA damage response/DDR. It is recruited to the sites of DNA damage by the RPA complex where PRPF19 directly ubiquitinates RPA1 and RPA2. 'Lys-63'-linked polyubiquitination of the RPA complex allows the recruitment of the ATR-ATRIP complex and the activation of ATR, a master regulator of the DNA damage response. May also play a role in DNA double-strand break (DSB) repair by recruiting the repair factor SETMAR to altered DNA. As part of the PSO4 complex may also be involved in the DNA interstrand cross-links/ICLs repair process. In addition, may also mediate 'Lys-48'-linked polyubiquitination of substrates and play a role in proteasomal degradation (PubMed:17349974). May play a role in the biogenesis of lipid droplets (PubMed:17118936). May play a role in neural differentiation possibly through its function as part of the spliceosome (By similarity). {ECO:0000250|UniProtKB:Q9JMJ4, ECO:0000250|UniProtKB:Q9UMS4, ECO:0000269|PubMed:17118936, ECO:0000269|PubMed:17349974}.; FUNCTION: Isoform 2: Forced expression leads to suppression of neuronal differentiation, and on the contrary to stimulation of astroglial cell differentiation in retinoic acid-primed P19 cells (PubMed:16352598). {ECO:0000269|PubMed:16352598}. NA SUBCELLULAR LOCATION: Isoform 1: Nucleus {ECO:0000269|PubMed:16352598}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9UMS4}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9UMS4}. Cytoplasm {ECO:0000250|UniProtKB:Q9UMS4}. Lipid droplet {ECO:0000269|PubMed:17118936}. Note=Nucleoplasmic in interphase cells. Irregularly distributed in anaphase cells. In prophase cells, uniformly distributed, but not associated with condensing chromosomes. Found in extrachromosomal regions in metaphase cells. Mainly localized to the mitotic spindle apparatus when chromosomes segregate during anaphase. When nuclei reform during late telophase, uniformly distributed in daughter cells and displays no preferred association with decondensing chromatin. Recruited on damaged DNA at sites of double-strand break (By similarity). {ECO:0000250|UniProtKB:Q9UMS4}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm {ECO:0000269|PubMed:16352598}. Nucleus {ECO:0000269|PubMed:16352598}. SUBUNIT: Homotetramer. Component of the Prp19 complex/PRP19C/Nineteen complex/NTC and related complexes described as PRP19-CDC5L splicing complex and PSO4 complex. A homotetramer of PRPF19, CDC5L, PLRG1 and BCAS2 constitute the core of those complexes. The interaction with CDC5L, PLRG1 and BCAS2 is direct within this core complex. At least three less stably associated proteins CTNNBL1, CWC15 and HSPA8 are found in the Prp19 complex. The Prp19 complex associates with the spliceosome during its assembly and remodeling recruiting additional proteins. Component of the XAB2 complex, a multimeric protein complex composed of XAB2, PRPF19, AQR, ZNF830, ISY1, and PPIE. Interacts with CWC22 and EIF4A3 in an RNA-independent manner. Interacts with RPA1 and RPA2; the PRP19-CDC5L complex is recruited to the sites of DNA repair where it interacts with the replication protein A complex (RPA). Interacts with SETMAR; required for SETMAR recruitment to site of DNA damage. Interacts with U2AF2; the interaction is direct and recruits the Prp19 complex to RNA polymerase II C-terminal domain (CTD) and the pre-mRNA. Interacts with PRPF3. Interacts with APEX1, DNTT and PSMB4. Interacts with KNSTRN (By similarity). Interacts with PSMC5 (PubMed:17349974). Isoform 2 (via N-terminus) interacts with PPIA. Isoform 2 does not interact with CDC5L (PubMed:16352598). Interacts with KHDC4 (By similarity). {ECO:0000250|UniProtKB:Q9UMS4, ECO:0000269|PubMed:16352598, ECO:0000269|PubMed:17349974}. DOMAIN: The 7 WD repeats are necessary and sufficient to support interaction with the RPA complex. {ECO:0000250|UniProtKB:Q9UMS4}. TISSUE SPECIFICITY: Expressed in white and brown adipose tissues, brain and to a lower extent in liver, kidney, muscle, lung and spleen (at protein level). {ECO:0000269|PubMed:17118936}. NA +Q99LB4 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q99LS5 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q99M71 EPDR1_MOUSE Mammalian ependymin-related protein 1 (MERP-1) 224 25,485 Alternative sequence (1); Chain (1); Glycosylation (2); Sequence conflict (2); Signal peptide (1) NA NA NA NA NA NA SUBCELLULAR LOCATION: Secreted. NA NA NA NA +Q99M71 EPDR1_MOUSE Mammalian ependymin-related protein 1 (MERP-1) 224 25,485 Alternative sequence (1); Chain (1); Glycosylation (2); Sequence conflict (2); Signal peptide (1) NA NA NA NA NA NA SUBCELLULAR LOCATION: Secreted. NA NA NA NA +Q99MR6 SRRT_MOUSE Serrate RNA effector molecule homolog (Arsenite-resistance protein 2) 875 100,452 Alternative sequence (2); Chain (1); Compositional bias (3); Cross-link (1); Erroneous initiation (2); Initiator methionine (1); Modified residue (15); Sequence conflict (1) NA NA NA NA FUNCTION: Acts as a mediator between the cap-binding complex (CBC) and the primary microRNAs (miRNAs) processing machinery during cell proliferation. Contributes to the stability and delivery of capped primary miRNA transcripts to the primary miRNA processing complex containing DGCR8 and DROSHA, thereby playing a role in RNA-mediated gene silencing (RNAi) by miRNAs. Binds capped RNAs (m7GpppG-capped RNA); however interaction is probably mediated via its interaction with NCBP1/CBP80 component of the CBC complex. Involved in cell cycle progression at S phase. Does not directly confer arsenite resistance but rather modulates arsenic sensitivity. Independently of its activity on miRNAs, necessary and sufficient to promote neural stem cell self-renewal. Does so by directly binding SOX2 promoter and positively regulating its transcription. {ECO:0000269|PubMed:19632182, ECO:0000269|PubMed:22198669}. NA SUBCELLULAR LOCATION: Nucleus, nucleoplasm. Cytoplasm. Note=Predominantly nuclear. Shuttles between the nucleus and the cytoplasm in a CRM1-dependent way. SUBUNIT: Interacts with CASP8AP2 and ERBB4 (By similarity). Interacts with NCBP1/CBP80 and DROSHA (PubMed:19632182). Interacts with LUZP4 (By similarity). Interacts with NCBP2/CBP20 and NCBP3 (By similarity). {ECO:0000250|UniProtKB:Q9BXP5, ECO:0000269|PubMed:19632182}. NA TISSUE SPECIFICITY: Widely expressed, with a preference for proliferating cells. Highly expressed in hematopoietic tissues and reduced or absent expression in parenchymal organs like liver and kidney. In the brain, expressed in the subventricular zone by niche astrocytes, ependymal cells and neural stem cells. In this cerebral context, expressed in slowly dividing cells. {ECO:0000269|PubMed:18086880, ECO:0000269|PubMed:19632182, ECO:0000269|PubMed:22198669}. NA +Q99PV0 PRP8_MOUSE Pre-mRNA-processing-splicing factor 8 (Splicing factor Prp8) 2335 273,616 Chain (1); Domain (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (5); Region (7); Sequence conflict (2) NA NA NA NA FUNCTION: Functions as a scaffold that mediates the ordered assembly of spliceosomal proteins and snRNAs. Required for the assembly of the U4/U6-U5 tri-snRNP complex. Functions as scaffold that positions spliceosomal U2, U5 and U6 snRNAs at splice sites on pre-mRNA substrates, so that splicing can occur. Interacts with both the 5' and the 3' splice site. {ECO:0000250|UniProtKB:Q6P2Q9}. NA SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:15169873}. SUBUNIT: Part of the U5 snRNP complex. Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39. Component of the U5.U4atac/U6atac snRNP complexes in U12-dependent spliceosomes. Found in a mRNA splicing-dependent exon junction complex (EJC) with SRRM1. Interacts with U5 snRNP proteins SNRP116 and SNRNP40. Interacts with EFTUD2 and SNRNP200. Interacts (via the MPN (JAB/Mov34) domain) with PRPF3 ('Lys-63'-linked polyubiquitinated); may stabilize the U4/U6-U5 tri-snRNP complex. Interacts (via RNase H homology domain) with AAR2. {ECO:0000250|UniProtKB:Q6P2Q9}. DOMAIN: The MPN (JAB/Mov34) domain has structural similarity with deubiquitinating enzymes, but lacks the residues that would bind the catalytic metal ion. {ECO:0000250}.; DOMAIN: Contains a region with structural similarity to reverse transcripase, presenting the classical thumb, fingers and palm architecture, but lacks enzyme activity, since the essential metal-binding residues are not conserved. {ECO:0000250}.; DOMAIN: Contains a region with structural similarity to type-2 restriction endonucleases, but the residues that would bind catalytic metal ions in endonucleases are instead involved in hydrogen bonds that stabilize the protein structure. {ECO:0000250}.; DOMAIN: Contains a region with structural similarity to RNase H, but lacks RNase H activity. {ECO:0000250}. TISSUE SPECIFICITY: Strongly expressed in testis (preferentially in the outer cell layer), and moderately in ovary (preferentially in granulosa cells). {ECO:0000269|PubMed:11275560}. NA +Q9BCZ4 SELS_MOUSE Selenoprotein S (SelS) (Minor histocompatibility antigen H47) 190 21,509 Chain (1); Erroneous termination (3); Natural variant (1); Non-standard residue (1); Region (1); Sequence conflict (1); Transmembrane (1) NA TRANSMEM 28 48 Helical. {ECO:0000255}. NA NA FUNCTION: Involved in the degradation process of misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Probably acts by serving as a linker between DERL1, which mediates the retrotranslocation of misfolded proteins into the cytosol, and the ATPase complex VCP, which mediates the translocation and ubiquitination (By similarity). {ECO:0000250}. NA SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with DERL1 and (via VIM motif) with VCP, suggesting that it forms a membrane complex with DERL1 that serves as a receptor for VCP. Also interacts with DERL2, DERL3 and SELENOK. The SELENOK-SELENOS complex interacts with VCP (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9BQE4}. NA NA NA +Q9CQF3 CPSF5_MOUSE Cleavage and polyadenylation specificity factor subunit 5 (Nucleoside diphosphate-linked moiety X motif 21) (Nudix motif 21) (Nudix hydrolase 21) 227 26,240 Chain (1); Domain (1); Initiator methionine (1); Modified residue (6); Motif (1); Region (3); Sequence conflict (1); Site (2) NA NA NA NA FUNCTION: Component of the cleavage factor Im (CFIm) complex that functions as an activator of the pre-mRNA 3'-end cleavage and polyadenylation processing required for the maturation of pre-mRNA into functional mRNAs. CFIm contributes to the recruitment of multiprotein complexes on specific sequences on the pre-mRNA 3'-end, so called cleavage and polyadenylation signals (pA signals). Most pre-mRNAs contain multiple pA signals, resulting in alternative cleavage and polyadenylation (APA) producing mRNAs with variable 3'-end formation. The CFIm complex acts as a key regulator of cleavage and polyadenylation site choice during APA through its binding to 5'-UGUA-3' elements localized in the 3'-untranslated region (UTR) for a huge number of pre-mRNAs. NUDT21/CPSF5 activates indirectly the mRNA 3'-processing machinery by recruiting CPSF6 and/or CPSF7. Binds to 5'-UGUA-3' elements localized upstream of pA signals that act as enhancers of pre-mRNA 3'-end processing. The homodimer mediates simultaneous sequence-specific recognition of two 5'-UGUA-3' elements within the pre-mRNA (By similarity). Plays a role in somatic cell fate transitions and pluripotency by regulating widespread changes in gene expression through an APA-dependent function(PubMed:29249356). Binds to chromatin (PubMed:18032416). Binds to, but does not hydrolyze mono- and di-adenosine nucleotides (By similarity). {ECO:0000250|UniProtKB:O43809, ECO:0000269|PubMed:18032416, ECO:0000269|PubMed:29249356}. PTM: Acetylated mainly by p300/CBP, recruited to the complex by CPSF6. Acetylation decreases interaction with PAPAO. Deacetylated by the class I/II HDACs, HDAC1, HDAC3 and HDAC10, and by the class III HDACs, SIRT1 AND SIRT2. {ECO:0000250|UniProtKB:O43809}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18032416}. Cytoplasm {ECO:0000250|UniProtKB:O43809}. Note=Shuttles between the nucleus and the cytoplasm in a transcription- and XPO1/CRM1-independent manner, most probably in complex with the cleavage factor Im complex (CFIm). In punctate subnuclear structures localized adjacent to nuclear speckles, called paraspeckles. {ECO:0000250|UniProtKB:O43809}. SUBUNIT: Homodimer (via N- and C-terminus); binds RNA as homodimer. Component of the cleavage factor Im (CFIm) complex which is an heterotetramer composed of two subunits of NUDT21/CPSF5 and two subunits of CPSF6 or CPSF7 or an heterodimer of CPSF6 and CPSF7. The cleavage factor Im (CFIm) complex associates with the CPSF and CSTF complexes to promote the assembly of the core mRNA 3'-processing machinery. Interacts with CPSF6 (via the RRM domain); this interaction is direct and enhances binding to RNA. Interacts with CPSF7. Interacts with FIP1L1; this interaction occurs in a RNA sequence-specific manner. Interacts with PABPN1 (By similarity). Interacts (via N-terminus) with PAPOLA (via C-terminus); this interaction is direct and diminished by acetylation (PubMed:11716503). Interacts with SNRNP70 (By similarity). Interacts with VIRMA (By similarity). {ECO:0000250|UniProtKB:O43809, ECO:0000269|PubMed:11716503}. NA TISSUE SPECIFICITY: Expressed in testis (PubMed:18032416). Expressed in male germ cells (at protein level) (PubMed:18032416). {ECO:0000269|PubMed:18032416}. NA +Q9CR32 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q9CX86 ROA0_MOUSE Heterogeneous nuclear ribonucleoprotein A0 (hnRNP A0) 305 30,530 Chain (1); Compositional bias (1); Cross-link (9); Domain (2); Modified residue (9) NA NA NA NA FUNCTION: mRNA-binding component of ribonucleosomes. Specifically binds AU-rich element (ARE)-containing mRNAs. Involved in post-transcriptional regulation of cytokines mRNAs. {ECO:0000269|PubMed:12456657}. PTM: Phosphorylated at Ser-84 by MAPKAPK2 in response to LPS treatment, promoting stabilization of GADD45A mRNA. {ECO:0000269|PubMed:12456657}.; PTM: Arg-293 is dimethylated, probably to asymmetric dimethylarginine. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Component of ribonucleosomes. {ECO:0000250}. NA NA NA NA +Q9CXX7 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q9CYL5 GAPR1_MOUSE Golgi-associated plant pathogenesis-related protein 1 (GAPR-1) (Golgi-associated PR-1 protein) (Glioma pathogenesis-related protein 2) (GliPR 2) 154 17,090 Chain (1); Coiled coil (1); Domain (1); Initiator methionine (1); Lipidation (1); Region (1); Sequence conflict (2) NA NA NA NA NA NA SUBCELLULAR LOCATION: Golgi apparatus membrane; Lipid-anchor. Note=Binds lipid-enriched microdomains of Golgi membranes not only by ionic interactions but also through the myristate. {ECO:0000250|UniProtKB:Q9H4G4}. SUBUNIT: Homodimer. Interacts with CAV1 (By similarity). {ECO:0000250}. NA NA NA +Q9D020 5NT3A_MOUSE Cytosolic 5'-nucleotidase 3A (EC 3.1.3.5) (7-methylguanosine phosphate-specific 5'-nucleotidase) (7-methylguanosine nucleotidase) (EC 3.1.3.91) (Cytosolic 5'-nucleotidase 3) (Cytosolic 5'-nucleotidase III) (cN-III) (Lupin) (Pyrimidine 5'-nucleotidase 1) (P5'N-1) (P5N-1) (PN-I) 331 37,252 Active site (2); Alternative sequence (1); Beta strand (11); Binding site (4); Chain (1); Helix (15); Metal binding (3); Modified residue (1); Region (1); Sequence conflict (2); Turn (3) NA NA NA NA FUNCTION: Nucleotidase which shows specific activity towards cytidine monophosphate (CMP) and 7-methylguanosine monophosphate (m(7)GMP). CMP seems to be the preferred substrate. {ECO:0000250|UniProtKB:Q9H0P0}. NA SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. SUBUNIT: Monomer. NA TISSUE SPECIFICITY: Isoform 2 is highly expressed in the brain, heart, spleen, kidney and blood. Isoform 2 is expressed (at protein level) in the spleen, skeletal muscle and gastrointestinal epithelia. NA +Q9D1K2 VATF_MOUSE V-type proton ATPase subunit F (V-ATPase subunit F) (V-ATPase 14 kDa subunit) (Vacuolar proton pump subunit F) 119 13,370 Chain (1); Sequence conflict (1) NA NA NA NA FUNCTION: Subunit of the peripheral V1 complex of vacuolar ATPase essential for assembly or catalytic function. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. NA NA SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'' and d). NA NA NA +Q9D1M7 FKB11_MOUSE Peptidyl-prolyl cis-trans isomerase FKBP11 (PPIase FKBP11) (EC 5.2.1.8) (19 kDa FK506-binding protein) (19 kDa FKBP) (FKBP-19) (FK506-binding protein 11) (FKBP-11) (Rotamase) 201 22,137 Chain (1); Domain (1); Sequence conflict (2); Signal peptide (1); Transmembrane (1) NA TRANSMEM 156 176 Helical. {ECO:0000255}. NA NA FUNCTION: PPIases accelerate the folding of proteins during protein synthesis. NA SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. SUBUNIT: Interacts with IFITM5. {ECO:0000269|PubMed:20838829}. NA NA NA +Q9D2Y4 MLKL_MOUSE Mixed lineage kinase domain-like protein 472 54,317 Alternative sequence (1); Beta strand (11); Binding site (1); Chain (1); Coiled coil (2); Domain (1); Helix (19); Modified residue (5); Mutagenesis (8); Nucleotide binding (1); Region (1); Turn (2) NA NA NA NA FUNCTION: Pseudokinase that plays a key role in TNF-induced necroptosis, a programmed cell death process. Activated following phosphorylation by RIPK3, leading to homotrimerization, localization to the plasma membrane and execution of programmed necrosis characterized by calcium influx and plasma membrane damage. Does not have protein kinase activity (PubMed:23835476, PubMed:24012422, PubMed:24019532). Binds to highly phosphorylated inositol phosphates such as inositolhexakisphosphate (InsP6) which is essential for its necroptotic function (By similarity). {ECO:0000250|UniProtKB:Q8NB16, ECO:0000269|PubMed:23835476, ECO:0000269|PubMed:24012422, ECO:0000269|PubMed:24019532}. PTM: Phosphorylation by RIPK3 induces a conformational switch that is required for necroptosis. It also induces homotrimerization and localization to the plasma membrane. {ECO:0000269|PubMed:24012422, ECO:0000269|PubMed:24095729}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8NB16}. Cell membrane {ECO:0000250|UniProtKB:Q8NB16}. Note=Localizes to the cytoplasm and translocates to the plasma membrane on necroptosis induction. {ECO:0000250|UniProtKB:Q8NB16}. SUBUNIT: Homooligomer (By similarity). Homotrimer; forms homotrimers on necroptosis induction. Upon TNF-induced necrosis, forms in complex with PGAM5, RIPK1 and RIPK3. Within this complex, may play a role in the proper targeting of RIPK1/RIPK3 to its downstream effector PGAM5 (By similarity). Interacts with RIPK3; the interaction is direct. {ECO:0000250|UniProtKB:Q8NB16, ECO:0000269|PubMed:22265413, ECO:0000269|PubMed:23612963, ECO:0000269|PubMed:24012422, ECO:0000269|PubMed:24095729}. DOMAIN: The coiled coil region 2 is responsible for homotrimerization. {ECO:0000250}.; DOMAIN: The protein kinase domain is catalytically inactive but contains an unusual pseudoactive site with an interaction between Lys-219 and Gln-343 residues. Upon phosphorylation by RIPK3, undergoes an active conformation (PubMed:24012422, PubMed:24095729). {ECO:0000269|PubMed:24012422, ECO:0000269|PubMed:24095729}. TISSUE SPECIFICITY: Highly expressed in thymus, colon, intestine, liver, spleen and lung. Expressed at much lower level in skeletal muscle, heart and kidney. Not detected in brain. {ECO:0000269|PubMed:23835476}. NA +Q9D4V7 RABL3_MOUSE Rab-like protein 3 236 26,298 Alternative sequence (1); Chain (1); Nucleotide binding (3); Region (1); Sequence conflict (1) NA NA NA NA NA NA NA NA NA NA NA +Q9D566 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q9D566 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q9D6G1 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q9D816 CP255_MOUSE Cytochrome P450 2C55 (EC 1.14.14.1) (CYPIIC55) 490 56,096 Chain (1); Metal binding (1) NA NA NA NA FUNCTION: Metabolizes arachidonic acid mainly to 19-hydroxyeicosatetraenoic acid (HETE). {ECO:0000269|PubMed:15102943}. NA SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. NA NA TISSUE SPECIFICITY: Highest level in colon. Low levels in liver and small intestine. {ECO:0000269|PubMed:15102943}. NA +Q9D8S5 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q9D964 GATM_MOUSE Glycine amidinotransferase, mitochondrial (EC 2.1.4.1) (L-arginine:glycine amidinotransferase) (Transamidinase) 423 48,297 Active site (3); Chain (1); Modified residue (3); Sequence conflict (2); Transit peptide (1) NA NA NA Amine and polyamine biosynthesis; creatine biosynthesis; creatine from L-arginine and glycine: step 1/2. FUNCTION: Catalyzes the biosynthesis of guanidinoacetate, the immediate precursor of creatine. Creatine plays a vital role in energy metabolism in muscle tissues. May play a role in embryonic and central nervous system development. {ECO:0000269|PubMed:12671064}. NA SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. NA TISSUE SPECIFICITY: Expressed in kidney, brain, gonads, uterus, and embryonic head, chest and abdomen. Maternally expressed in the placenta and yolk sac of embryos. {ECO:0000269|PubMed:12671064}. NA +Q9DB34 CHM2A_MOUSE Charged multivesicular body protein 2a (Chromatin-modifying protein 2a) (CHMP2a) (Vacuolar protein sorting-associated protein 2) (mVps2) 222 25,134 Chain (1); Coiled coil (2); Modified residue (6); Motif (1); Region (2) NA NA NA NA FUNCTION: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis. Together with SPAST, the ESCRT-III complex promotes nuclear envelope sealing and mitotic spindle disassembly during late anaphase. ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. {ECO:0000250|UniProtKB:O43633}. PTM: ISGylated in a CHMP5-dependent manner. Isgylation weakens and inhibits its interactions with VPS4A and VTA1 respectively (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:15173323}. Note=Localizes to the midbody of dividing cells. Localized in two distinct rings on either side of the Fleming body. SUBUNIT: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III). ESCRT-III components are thought to multimerize to form a flat lattice on the perimeter membrane of the endosome. Several assembly forms of ESCRT-III may exist that interact and act sequentially. In vitro, heteromerizes with CHMP3 (but not CHMP4) to form helical tubular structures that expose membrane-interacting sites on the outside whereas VPS4B can associate on the inside of the tubule. Interacts with CHMP1B, CHMP2B, CHMP3, CHMP4A, CHMP4B, CHMP4C and CHMP5. Interacts with VPS4A; the interaction is direct. Interacts with VPS4B; the interaction is direct. Interacts with MITD1. Interacts with VTA1; the interaction probably involves the open conformation of CHMP2A (By similarity). {ECO:0000250}. DOMAIN: The acidic C-terminus and the basic N-termminus are thought to render the protein in a closed, soluble and inactive conformation through an autoinhibitory intramolecular interaction. The open and active conformation, which enables membrane binding and oligomerization, is achieved by interaction with other cellular binding partners, probably including other ESCRT components. TISSUE SPECIFICITY: Widely expressed. Highly expressed in brain, heart, liver and kidney. {ECO:0000269|PubMed:15173323}. NA +Q9DBG9 TX1B3_MOUSE Tax1-binding protein 3 (Tax interaction protein 1) (TIP-1) 124 13,723 Beta strand (8); Chain (1); Domain (1); Helix (5); Initiator methionine (1); Modified residue (2) NA NA NA NA FUNCTION: May regulate a number of protein-protein interactions by competing for PDZ domain binding sites. Binds CTNNB1 and may thereby act as an inhibitor of the Wnt signaling pathway. Competes with LIN7A for KCNJ4 binding, and thereby promotes KCNJ4 internalization. May play a role in the Rho signaling pathway (By similarity). {ECO:0000250, ECO:0000269|PubMed:12874278}. NA SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12874278}. Nucleus {ECO:0000269|PubMed:12874278}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Recruited to the cell membrane by interaction with membrane proteins. {ECO:0000250}. SUBUNIT: Interacts (via its PDZ domain) with GLS2. Interacts (via its PDZ domain) with RTKN (via the C-terminal region); this interaction facilitates Rho-mediated activation of the FOS serum response element (SRE). Interacts (via PDZ domain) with ARHGEF16. Interacts (via PDZ domain) with KCNJ4 (via C-terminus). Competes with LIN7A for KCNJ4 binding (By similarity). Interacts (via its PDZ domain) with CTNNB1; this interaction inhibits the transcriptional activity of CTNNB1. Interacts with ADGRB2 (By similarity). {ECO:0000250|UniProtKB:O14907, ECO:0000269|PubMed:12874278, ECO:0000269|PubMed:18835279}. NA NA NA +Q9DBR7 MYPT1_MOUSE Protein phosphatase 1 regulatory subunit 12A (Myosin phosphatase-targeting subunit 1) (Myosin phosphatase target subunit 1) 1029 114,996 Alternative sequence (1); Chain (1); Compositional bias (2); Modified residue (27); Motif (1); Region (1); Repeat (6) NA NA NA NA FUNCTION: Key regulator of protein phosphatase 1C (PPP1C). Mediates binding to myosin. As part of the PPP1C complex, involved in dephosphorylation of PLK1. Capable of inhibiting HIF1AN-dependent suppression of HIF1A activity (By similarity). {ECO:0000250|UniProtKB:O14974, ECO:0000250|UniProtKB:Q10728}. PTM: Phosphorylated by CIT (Rho-associated kinase) (By similarity). Phosphorylated cooperatively by ROCK1 and CDC42BP on Thr-694 (By similarity). Phosphorylated on upon DNA damage, probably by ATM or ATR. In vitro, phosphorylation of Ser-693 by PKA and PKG appears to prevent phosphorylation of the inhibitory site Thr-694, probably mediated by PRKG1. Phosphorylation at Ser-445, Ser-472 and Ser-909 by NUAK1 promotes interaction with 14-3-3, leading to inhibit interaction with myosin light chain MLC2, preventing dephosphorylation of MLC2. May be phosphorylated at Thr-694 by DMPK; may inhibit the myosin phosphatase activity (By similarity). Phosphorylated at Ser-473 by CDK1 during mitosis, creating docking sites for the POLO box domains of PLK1. Subsequently, PLK1 binds and phosphorylates PPP1R12A (By similarity). {ECO:0000250|UniProtKB:O14974}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O14974}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:O14974}. Note=Also along actomyosin filaments. {ECO:0000250|UniProtKB:O14974}. SUBUNIT: PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or PPP1CC, and one or several targeting or regulatory subunits. PPP1R12A mediates binding to myosin. Interacts with ARHA and CIT (By similarity). Binds PPP1R12B, ROCK1 and IL16. Interacts directly with PRKG1. Non-covalent dimer of 2 dimers; PRKG1-PRKG1 and PPP1R12A-PPP1R12A. Interacts with SMTNL1 (By similarity). Interacts with PPP1CB; the interaction is direct. Interacts (when phosphorylated at Ser-445, Ser-472 and Ser-910) with 14-3-3. Interacts with ROCK1 and ROCK2. Interacts with isoform 1 and isoform 2 of ZIPK/DAPK3. Interacts with RAF1. Interacts with HIF1AN (By similarity). Interacts with NCKAP1L (By similarity). {ECO:0000250|UniProtKB:O14974}. DOMAIN: Heterotetramerization is mediated by the interaction between a coiled-coil of PRKG1 and the leucine/isoleucine zipper of PPP1R12A/MBS, the myosin-binding subunit of the myosin phosphatase. {ECO:0000250}.; DOMAIN: The KVKF motif mediates interaction with PPP1CB. {ECO:0000250|UniProtKB:O14974}. TISSUE SPECIFICITY: Expressed in striated and vascular smooth muscle, specificcally in type 2a fibers (at protein level). Expression levels are 20-30% higher in developed males than females (at protein level). {ECO:0000269|PubMed:20634291}. NA +Q9DBS1 TMM43_MOUSE Transmembrane protein 43 (Protein LUMA) 400 44,783 Chain (1); Initiator methionine (1); Modified residue (1); Topological domain (5); Transmembrane (4) NA TRANSMEM 32 52 Helical. {ECO:0000255}.; TRANSMEM 314 334 Helical. {ECO:0000255}.; TRANSMEM 346 366 Helical. {ECO:0000255}.; TRANSMEM 369 389 Helical. {ECO:0000255}. TOPO_DOM 2 31 Nuclear. {ECO:0000255}.; TOPO_DOM 53 313 Perinuclear space. {ECO:0000255}.; TOPO_DOM 335 345 Nuclear. {ECO:0000255}.; TOPO_DOM 367 368 Perinuclear space. {ECO:0000255}.; TOPO_DOM 390 400 Nuclear. {ECO:0000255}. NA FUNCTION: May have an important role in maintaining nuclear envelope structure by organizing protein complexes at the inner nuclear membrane. Required for retaining emerin at the inner nuclear membrane. {ECO:0000269|PubMed:18230648}. NA SUBCELLULAR LOCATION: Endoplasmic reticulum. Nucleus inner membrane; Multi-pass membrane protein. Note=Retained in the inner nuclear membrane through interaction with EMD and A- and B-lamins. The N- and C-termini are oriented towards the nucleoplasm. The majority of the hydrophilic domain resides in the endoplasmic reticulum lumen. SUBUNIT: Can form oligomers through the transmembrane domains. Interacts with EMD; the interaction retains EMD at the inner nuclear membrane. Interacts with LMNA and LMNB2. Interacts with SUN2 (By similarity). {ECO:0000250}. NA NA NA +Q9DBX3 SUSD2_MOUSE Sushi domain-containing protein 2 820 90,641 Alternative sequence (2); Chain (1); Disulfide bond (9); Domain (4); Frameshift (1); Glycosylation (3); Helix (2); Sequence conflict (6); Signal peptide (1); Topological domain (2); Transmembrane (1) NA TRANSMEM 783 803 Helical. {ECO:0000255}. TOPO_DOM 23 782 Extracellular. {ECO:0000255}.; TOPO_DOM 804 820 Cytoplasmic. {ECO:0000255}. NA FUNCTION: May be a cytokine receptor for C10ORF99. May be a tumor suppressor; together with C10ORF99 has a growth inhibitory effect on colon cancer cells which includes G1 cell cycle arrest (By similarity). May play a role in breast tumorigenesis (PubMed:23131994). {ECO:0000250|UniProtKB:Q9UGT4, ECO:0000269|PubMed:23131994}. NA SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9UGT4}; Single-pass type I membrane protein {ECO:0000305}. NA NA NA NA +Q9DD06 RARR2_MOUSE Retinoic acid receptor responder protein 2 (Chemerin) 162 18,350 Chain (1); Disulfide bond (3); Natural variant (1); Propeptide (1); Signal peptide (1) NA NA NA NA FUNCTION: Adipocyte-secreted protein (adipokine) that regulates adipogenesis, metabolism and inflammation through activation of the chemokine-like receptor 1 (CMKLR1). Its other ligands include G protein-coupled receptor 1 (GPR1) and chemokine receptor-like 2 (CCRL2). Positively regulates adipocyte differentiation, modulates the expression of adipocyte genes involved in lipid and glucose metabolism and might play a role in angiogenesis, a process essential for the expansion of white adipose tissue. Also acts as a proinflammatory adipokine, causing an increase in secretion of proinflammatory and prodiabetic adipokines, which further impair adipose tissue metabolic function and have negative systemic effects including impaired insulin sensitivity, altered glucose and lipid metabolism, and a decrease in vascular function in other tissues. Can have both pro- and anti-inflammatory properties depending on the modality of enzymatic cleavage by different classes of proteases. Acts as a chemotactic factor for leukocyte populations expressing CMKLR1, particularly immature plasmacytoid dendritic cells, but also immature myeloid DCs, macrophages and natural killer cells. Exerts an anti-inflammatory role by preventing TNF/TNFA-induced VCAM1 expression and monocytes adhesion in vascular endothelial cells. The effect is mediated via inhibiting activation of NF-kappa-B and CRK/p38 through stimulation of AKT1/NOS3 signaling and nitric oxide production. Exhibits an antimicrobial function in the skin. {ECO:0000269|PubMed:17635925, ECO:0000269|PubMed:18242188}. PTM: Secreted in an inactive precursor form, prochemerin, which is proteolytically processed by a variety of extracellular proteases to generate forms with differing levels of bioactivity. For example, the removal of six amino acids results in chemerin-156, which exhibits the highest activity, while removal of seven amino acids results in chemerin-155 which has slightly less activity. Some proteases are able to cleave at more than one site and chemerin forms may be sequentially processed by different enzymes to modulate activity levels. The coordinated expression and activity of chemerin-modifying enzymes is essential for regulating its bioactivation, inactivation and, consequently, biological function. Cathepsin G cleaves seven C-terminal amino acids from prochemerin (chemerin-155), elastase is able to cleave six (chemerin-156), eight (chemerin-154) or eleven (chemerin-151), plasmin cleaves five amino acids (chemerin-157), and tryptase cleaves five (chemerin-157) or eight (chemerin-154). Multiple cleavages might be required to fully activate chemerin, with an initial tryptase cleavage resulting in chemerin with low activity (chemerin-157), and a second cleavage by carboxypeptidase N or B producing highly active chemerin (chemerin-156) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17635925, ECO:0000269|PubMed:18242188}. NA NA TISSUE SPECIFICITY: Expressed in the differentiated adipocytes (at protein level). Abundantly expressed in the liver, adipose tissue including visceral, epididymal, and brown adipose tissue. {ECO:0000269|PubMed:17635925, ECO:0000269|PubMed:17767914, ECO:0000269|PubMed:18242188}. NA +Q9EQ79 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Q9ER41 TOR1B_MOUSE Torsin-1B (Torsin ATPase-1B) (EC 3.6.4.-) (Torsin family 1 member B) 336 37,818 Chain (1); Glycosylation (2); Nucleotide binding (1); Sequence conflict (2); Signal peptide (1) NA NA NA NA FUNCTION: May serve as a molecular chaperone assisting in the proper folding of secreted and/or membrane proteins. Plays a role in non-neural cells nuclear envelope and endoplasmic reticulum integrity. May have a redundant function with TOR1A in non-neural tissues. {ECO:0000269|PubMed:20457914}. PTM: N-glycosylated. {ECO:0000269|PubMed:20015956}. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Nucleus membrane. SUBUNIT: Homohexamer. Interacts with TOR1A; the interaction may be specific of neural tissues. Interacts with TOR1AIP1; TOR1AIP1 is required for TOR1B location on the nuclear membrane. Interacts (ATP-bound) with TOR1AIP2; important for endoplasmic reticulum integrity. {ECO:0000269|PubMed:20457914}. NA TISSUE SPECIFICITY: Highly expressed in liver and muscle; lower expression levels are observed in brain (at protein level). {ECO:0000269|PubMed:20015956}. NA +Q9R0Y5 KAD1_MOUSE Adenylate kinase isoenzyme 1 (AK 1) (EC 2.7.4.3) (EC 2.7.4.6) (ATP-AMP transphosphorylase 1) (ATP:AMP phosphotransferase) (Adenylate monophosphate kinase) (Myokinase) 194 21,540 Alternative sequence (1); Binding site (7); Chain (1); Erroneous gene model prediction (1); Modified residue (2); Nucleotide binding (3); Region (2) NA NA NA NA FUNCTION: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Also possesses broad nucleoside diphosphate kinase activity. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism (By similarity). May provide a mechanism to buffer the adenylate energy charge for sperm motility. {ECO:0000250, ECO:0000269|PubMed:16790685}. NA SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03171}. SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03171}. DOMAIN: Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis. {ECO:0000255|HAMAP-Rule:MF_03171}. NA NA +Q9WU81 G6PT3_MOUSE Glucose-6-phosphate exchanger SLC37A2 (Solute carrier family 37 member 2) (cAMP-inducible protein 2) 501 55,073 Alternative sequence (1); Chain (1); Frameshift (1); Glycosylation (3); Sequence conflict (2); Transmembrane (12) NA TRANSMEM 19 39 Helical. {ECO:0000255}.; TRANSMEM 88 108 Helical. {ECO:0000255}.; TRANSMEM 118 140 Helical. {ECO:0000255}.; TRANSMEM 142 164 Helical. {ECO:0000255}.; TRANSMEM 179 199 Helical. {ECO:0000255}.; TRANSMEM 210 230 Helical. {ECO:0000255}.; TRANSMEM 303 323 Helical. {ECO:0000255}.; TRANSMEM 334 354 Helical. {ECO:0000255}.; TRANSMEM 362 382 Helical. {ECO:0000255}.; TRANSMEM 391 411 Helical. {ECO:0000255}.; TRANSMEM 434 454 Helical. {ECO:0000255}.; TRANSMEM 462 482 Helical. {ECO:0000255}. NA NA FUNCTION: Inorganic phosphate and glucose-6-phosphate antiporter. May transport cytoplasmic glucose-6-phosphate into the lumen of the endoplasmic reticulum and translocate inorganic phosphate into the opposite direction. Independent of a lumenal glucose-6-phosphatase. May not play a role in homeostatic regulation of blood glucose levels. {ECO:0000250|UniProtKB:Q8TED4}. NA SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8TED4}; Multi-pass membrane protein {ECO:0000255}. NA NA TISSUE SPECIFICITY: Highly expressed in bone marrow derived macrophages, and weakly in spleen. {ECO:0000269|PubMed:11004510}. NA +Q9Z2G9 HTAI2_MOUSE Oxidoreductase HTATIP2 (EC 1.1.1.-) 242 26,870 Active site (2); Alternative sequence (2); Beta strand (9); Binding site (1); Chain (1); Helix (9); Initiator methionine (1); Modified residue (1); Nucleotide binding (1); Sequence conflict (7) NA NA NA NA FUNCTION: Oxidoreductase required for tumor suppression. NAPDH-bound form inhibits nuclear import by competing with nuclear import substrates for binding to a subset of nuclear transport receptors. May act as a redox sensor linked to transcription through regulation of nuclear import. {ECO:0000269|PubMed:14695192}. NA SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus envelope {ECO:0000250}. SUBUNIT: Monomer. Binds nuclear transport receptors XPO4, IPO5/RANBP5, IPO7, IPO9 and KPNB1 as well as GCN1L1/GCN1 and LRPPRC probably through their HEAT repeats. Binds NCOA5/CIA (By similarity). {ECO:0000250}. NA NA NA +V9GX26 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Z4YK56 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA +Z4YLT8 NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA NA diff -r 000000000000 -r 1e856941a888 tool-data/uniprot_features_mouse.tsv --- /dev/null Thu Jan 01 00:00:00 1970 +0000 +++ b/tool-data/uniprot_features_mouse.tsv Fri Feb 08 08:46:04 2019 -0500 @@ -0,0 +1,17007 @@ +Entry Entry name Protein names Length Mass Features Intramembrane Transmembrane Topological domain Pathway Function [CC] Post-translational modification Subcellular location [CC] Subunit structure [CC] Domain [CC] Tissue specificity Involvement in disease +Q8K4K6 PANK1_MOUSE Pantothenate kinase 1 (mPank) (mPank1) (EC 2.7.1.33) (Pantothenic acid kinase 1) 548 60,091 Alternative sequence (2); Binding site (3); Chain (1); Modified residue (2) Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5. FUNCTION: Plays a role in the physiological regulation of the intracellular CoA concentration. SUBUNIT: Homodimer. {ECO:0000250}. DOMAIN: The N-terminal extension, present in isoform 1 may be the regulatory domain. TISSUE SPECIFICITY: Expressed in liver and kidney. Isoform 1 is highly expressed in heart and skeletal muscle, whereas isoform 2 is expressed exclusively in testis. +Q60967 PAPS1_MOUSE Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1 (PAPS synthase 1) (PAPSS 1) (Sulfurylase kinase 1) (SK 1) (SK1) [Includes: Sulfate adenylyltransferase (EC 2.7.7.4) (ATP-sulfurylase) (Sulfate adenylate transferase) (SAT); Adenylyl-sulfate kinase (EC 2.7.1.25) (3'-phosphoadenosine-5'-phosphosulfate synthase) (APS kinase) (Adenosine-5'-phosphosulfate 3'-phosphotransferase) (Adenylylsulfate 3'-phosphotransferase)] 624 70,794 Binding site (5); Chain (1); Modified residue (2); Nucleotide binding (3); Region (6) Sulfur metabolism; sulfate assimilation. FUNCTION: Bifunctional enzyme with both ATP sulfurylase and APS kinase activity, which mediates two steps in the sulfate activation pathway. The first step is the transfer of a sulfate group to ATP to yield adenosine 5'-phosphosulfate (APS), and the second step is the transfer of a phosphate group from ATP to APS yielding 3'-phosphoadenylylsulfate (PAPS: activated sulfate donor used by sulfotransferase). In mammals, PAPS is the sole source of sulfate; APS appears to be only an intermediate in the sulfate-activation pathway (PubMed:7493984). Required for normal biosynthesis of sulfated L-selectin ligands in endothelial cells (By similarity). {ECO:0000250|UniProtKB:O43252, ECO:0000269|PubMed:7493984}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O43252}. TISSUE SPECIFICITY: Expressed in the neonatal brain and in cartilage. {ECO:0000269|PubMed:7493984}. +Q9DCU0 PAQR5_MOUSE Membrane progestin receptor gamma (mPR gamma) (Membrane progesterone P4 receptor gamma) (Membrane progesterone receptor gamma) (Progesterone and adipoQ receptor family member 5) (Progestin and adipoQ receptor family member 5) (Progestin and adipoQ receptor family member V) 330 38,151 Chain (1); Erroneous initiation (1); Sequence caution (1); Topological domain (8); Transmembrane (7) TRANSMEM 52 72 Helical; Name=1. {ECO:0000255}.; TRANSMEM 82 101 Helical; Name=2. {ECO:0000255}.; TRANSMEM 114 134 Helical; Name=3. {ECO:0000255}.; TRANSMEM 142 162 Helical; Name=4. {ECO:0000255}.; TRANSMEM 187 207 Helical; Name=5. {ECO:0000255}.; TRANSMEM 254 274 Helical; Name=6. {ECO:0000255}.; TRANSMEM 295 315 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 51 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 73 81 Extracellular. {ECO:0000255}.; TOPO_DOM 102 113 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 135 141 Extracellular. {ECO:0000255}.; TOPO_DOM 163 186 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 208 253 Extracellular. {ECO:0000255}.; TOPO_DOM 275 294 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 316 330 Extracellular. {ECO:0000255}. FUNCTION: Plasma membrane progesterone (P4) receptor coupled to G proteins. Seems to act through a G(i) mediated pathway. May be involved in oocyte maturation. {ECO:0000250|UniProtKB:Q9NXK6}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9NXK6}; Multi-pass membrane protein {ECO:0000255}. +P09084 PAX1_MOUSE Paired box protein Pax-1 446 46,263 Chain (1); Domain (1); Erroneous gene model prediction (1); Erroneous initiation (1); Natural variant (1); Sequence conflict (4) FUNCTION: This protein is a transcriptional activator. It may play a role in the formation of segmented structures of the embryo. May play an important role in the normal development of the vertebral column. SUBCELLULAR LOCATION: Nucleus. DISEASE: Note=Undulated (un) homozygous mice exhibits vertebral malformations along the entire rostro-caudal axis. This is due to a single mutation in the paired box region. {ECO:0000269|PubMed:3180219}. +O88554 PARP2_MOUSE Poly [ADP-ribose] polymerase 2 (PARP-2) (mPARP-2) (EC 2.4.2.30) (ADP-ribosyltransferase diphtheria toxin-like 2) (ARTD2) (DNA ADP-ribosyltransferase PARP2) (EC 2.4.2.-) (NAD(+) ADP-ribosyltransferase 2) (ADPRT-2) (Poly[ADP-ribose] synthase 2) (pADPRT-2) (Protein poly-ADP-ribosyltransferase PARP2) (EC 2.4.2.-) 559 63,397 Beta strand (16); Chain (1); DNA binding (1); Domain (2); Erroneous initiation (1); Helix (17); Modified residue (5); Motif (2); Mutagenesis (2); Sequence conflict (3); Turn (1) FUNCTION: Poly-ADP-ribosyltransferase that mediates poly-ADP-ribosylation of proteins and plays a key role in DNA repair (PubMed:10364231). Mainly mediates glutamate and aspartate ADP-ribosylation of target proteins: the ADP-D-ribosyl group of NAD(+) is transferred to the acceptor carboxyl group of glutamate and aspartate residues and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units (By similarity). ADP-ribosylation follows DNA damage and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks (PubMed:10364231). Also mediates serine ADP-ribosylation of target proteins following interaction with HPF1; HPF1 conferring serine specificity (By similarity). In addition to proteins, also able to ADP-ribosylate DNA: preferentially acts on 5'-terminal phosphates at DNA strand breaks termini in nicked duplex (By similarity). {ECO:0000250|UniProtKB:Q9UGN5, ECO:0000269|PubMed:10364231}. PTM: Poly-ADP-ribosylated by PARP1. {ECO:0000269|PubMed:11948190}.; PTM: Acetylation reduces DNA binding and enzymatic activity. {ECO:0000269|PubMed:18436469}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10364231}. SUBUNIT: Component of a base excision repair (BER) complex, containing at least XRCC1, PARP1, POLB and LRIG3 (PubMed:11948190). Homo- and heterodimer with PARP1 (By similarity). Interacts weakly (via the PARP catalytic domain) with HPF1 (By similarity). {ECO:0000250|UniProtKB:Q9UGN5, ECO:0000269|PubMed:11948190}. TISSUE SPECIFICITY: Widely expressed; the highest levels were in testis followed by ovary. Expression is correlated with proliferation, with higher levels occurring during early fetal development and organogenesis and in the highly proliferative cell compartments of adult. +Q3UD82 PARP8_MOUSE Protein mono-ADP-ribosyltransferase PARP8 (EC 2.4.2.-) (ADP-ribosyltransferase diphtheria toxin-like 16) (ARTD16) (Poly [ADP-ribose] polymerase 8) (PARP-8) 852 95,560 Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (2); Modified residue (4); Sequence conflict (4) FUNCTION: Mono-ADP-ribosyltransferase that mediates mono-ADP-ribosylation of target proteins. {ECO:0000250|UniProtKB:Q8N3A8}. PTM: Auto-mono-ADP-ribosylated. {ECO:0000250|UniProtKB:Q8N3A8}. +O88634 PAR4_MOUSE Proteinase-activated receptor 4 (PAR-4) (Coagulation factor II receptor-like 3) (Thrombin receptor-like 3) 396 42,786 Chain (1); Compositional bias (1); Disulfide bond (1); Glycosylation (1); Propeptide (1); Sequence conflict (4); Signal peptide (1); Site (1); Topological domain (8); Transmembrane (7); Turn (1) TRANSMEM 95 115 Helical; Name=1. {ECO:0000255}.; TRANSMEM 121 141 Helical; Name=2. {ECO:0000255}.; TRANSMEM 163 183 Helical; Name=3. {ECO:0000255}.; TRANSMEM 204 224 Helical; Name=4. {ECO:0000255}.; TRANSMEM 256 276 Helical; Name=5. {ECO:0000255}.; TRANSMEM 296 316 Helical; Name=6. {ECO:0000255}.; TRANSMEM 332 355 Helical; Name=7. {ECO:0000255}. TOPO_DOM 60 94 Extracellular. {ECO:0000255}.; TOPO_DOM 116 120 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 142 162 Extracellular. {ECO:0000255}.; TOPO_DOM 184 203 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 225 255 Extracellular. {ECO:0000255}.; TOPO_DOM 277 295 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 317 331 Extracellular. {ECO:0000255}.; TOPO_DOM 356 396 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for activated thrombin or trypsin coupled to G proteins that stimulate phosphoinositide hydrolysis. May play a role in platelets activation. PTM: A proteolytic cleavage generates a new N-terminus that functions as a tethered ligand. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Highly expressed in the spleen. Slight expression in the heart, lung, skeletal muscle and kidney. No detectable expression in brain, liver or testis. Also detected in platelets. +Q5XJY4 PARL_MOUSE Presenilins-associated rhomboid-like protein, mitochondrial (EC 3.4.21.105) (Mitochondrial intramembrane-cleaving protease PARL) [Cleaved into: P-beta (Pbeta)] 377 41,964 Active site (2); Chain (1); Modified residue (2); Peptide (1); Topological domain (8); Transit peptide (1); Transmembrane (7) TRANSMEM 100 119 Helical. {ECO:0000255}.; TRANSMEM 166 185 Helical. {ECO:0000255}.; TRANSMEM 206 228 Helical. {ECO:0000255}.; TRANSMEM 243 260 Helical. {ECO:0000255}.; TRANSMEM 271 287 Helical. {ECO:0000255}.; TRANSMEM 294 316 Helical. {ECO:0000255}.; TRANSMEM 331 352 Helical. {ECO:0000255}. TOPO_DOM 51 99 Mitochondrial matrix. {ECO:0000255}.; TOPO_DOM 120 165 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 186 205 Mitochondrial matrix. {ECO:0000255}.; TOPO_DOM 229 242 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 261 270 Mitochondrial matrix. {ECO:0000255}.; TOPO_DOM 288 293 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 317 330 Mitochondrial matrix. {ECO:0000255}.; TOPO_DOM 353 377 Mitochondrial intermembrane. {ECO:0000255}. FUNCTION: Required for the control of apoptosis during postnatal growth. Essential for proteolytic processing of an antiapoptotic form of OPA1 which prevents the release of mitochondrial cytochrome c in response to intrinsic apoptoptic signals (By similarity). {ECO:0000250, ECO:0000269|PubMed:16839884}. PTM: P-beta is proteolytically processed (beta-cleavage) in a PARL-dependent manner. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:16839884}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9H300}.; SUBCELLULAR LOCATION: P-beta: Nucleus {ECO:0000250|UniProtKB:Q9H300}. Note=Translocated into the nucleus by an unknown mechanism (By similarity). {ECO:0000250|UniProtKB:Q9H300}. SUBUNIT: Interacts with PSEN1 and PSEN2 (By similarity). Binds OPA1. {ECO:0000250, ECO:0000269|PubMed:16839884}. +O35317 PBX3_MOUSE Pre-B-cell leukemia transcription factor 3 (Homeobox protein PBX3) 434 47,204 Alternative sequence (2); Chain (1); Compositional bias (1); DNA binding (1) FUNCTION: Transcriptional activator that binds the sequence 5'-ATCAATCAA-3'. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. SUBUNIT: Interacts with PBXIP1. {ECO:0000250}. +Q9DCG6 PBLD1_MOUSE Phenazine biosynthesis-like domain-containing protein 1 (EC 5.1.-.-) 288 32,048 Active site (1); Chain (1); Sequence conflict (1) +Q9CXN7 PBLD2_MOUSE Phenazine biosynthesis-like domain-containing protein 2 (EC 5.1.-.-) 288 31,983 Active site (1); Chain (1); Sequence conflict (1) +Q91XZ2 PCDB8_MOUSE Protocadherin beta-8 (PCDH-beta-8) 779 84,766 Beta strand (33); Chain (1); Disulfide bond (1); Domain (6); Glycosylation (6); Helix (6); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (8) TRANSMEM 691 711 Helical. {ECO:0000255}. TOPO_DOM 29 690 Extracellular. {ECO:0000305|PubMed:27161523}.; TOPO_DOM 712 779 Cytoplasmic. {ECO:0000305|PubMed:27161523}. FUNCTION: Calcium-dependent cell-adhesion protein involved in cells self-recognition and non-self discrimination (Probable). Thereby, it is involved in the establishment and maintenance of specific neuronal connections in the brain (PubMed:27161523). {ECO:0000305|PubMed:27161523}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:27161523}; Single-pass type I membrane protein {ECO:0000305|PubMed:27161523}. SUBUNIT: Forms homodimers in trans (molecules expressed by two different cells) (PubMed:27161523). Forms promiscuous heterodimers in cis (at the plasma membrane of the same cell) with other protocadherins (PubMed:27161523). {ECO:0000269|PubMed:27161523}. DOMAIN: Cadherin 1 to cadherin 4 domains mediate homophilic trans-interaction, the interaction with an identical protocadherin expressed by a neighboring cell (PubMed:27161523). This is a head-to-tail interaction, the cadherin 1 domain interacting with the cadherin 4 domain and the cadherin 2 domain interacting the cadherin 3 domain of the other protocadherin (PubMed:27161523). The cadherin 6 domain mediates promiscuous interactions with protocadherins on the same cell membrane (PubMed:27161523). Each cadherin domain binds three calcium ions (PubMed:27161523). {ECO:0000269|PubMed:27161523, ECO:0000312|PDB:5DZY}. +Q6PB90 PCDBE_MOUSE Protocadherin beta-14 (PCDH-beta-14) 796 87,022 Beta strand (9); Chain (1); Disulfide bond (1); Domain (6); Glycosylation (4); Helix (1); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (3) TRANSMEM 691 711 Helical. {ECO:0000255}. TOPO_DOM 30 690 Extracellular. {ECO:0000255}.; TOPO_DOM 712 796 Cytoplasmic. {ECO:0000255}. FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q8BTQ0 PCGF3_MOUSE Polycomb group RING finger protein 3 (RING finger protein 3A) 241 28,046 Alternative sequence (2); Chain (1); Zinc finger (1) FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility (PubMed:28596365). Within the PRC1-like complex, regulates RNF2 ubiquitin ligase activity (By similarity). Plays a redundant role with PCGF5 as part of a PRC1-like complex that mediates monoubiquitination of histone H2A 'Lys-119' on the X chromosome and is required for normal silencing of one copy of the X chromosome in XX females (PubMed:28596365). {ECO:0000250|UniProtKB:Q3KNV8, ECO:0000269|PubMed:28596365}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28596365}. Nucleus, nucleoplasm {ECO:0000269|PubMed:28596365}. Note=Recruited by the non-coding RNA Xist to specific nuclear foci that probably correspond to the inactivated X chromosome. {ECO:0000269|PubMed:28596365}. SUBUNIT: Component of a PRC1-like complex that contains PCGF3, RNF2 and RYBP (PubMed:28596365). Interacts with RNF2 (PubMed:28596365). Interacts with CBX6, CBX7 and CBX8 (By similarity). {ECO:0000250|UniProtKB:Q3KNV8, ECO:0000269|PubMed:28596365}. +Q6P8I4 PCNP_MOUSE PEST proteolytic signal-containing nuclear protein (PCNP) (PEST-containing nuclear protein) 178 18,963 Chain (1); Initiator methionine (1); Modified residue (10) FUNCTION: May be involved in cell cycle regulation. {ECO:0000250}. PTM: Ubiquitinated; mediated by UHRF2 and leading to its subsequent proteasomal degradation. {ECO:0000250}.; PTM: N-terminally acetylated in a HYPK-dependent manner by the NatA acetyltransferase complex which is composed of NAA10 and NAA15. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with UHRF2/NIRF. {ECO:0000250}. +P63054 PCP4_MOUSE Calmodulin regulator protein PCP4 (Brain-specific antigen PCP-4) (Brain-specific polypeptide PEP-19) (Purkinje cell protein 4) 62 6,807 Chain (1); Domain (1); Region (1); Sequence conflict (1) FUNCTION: Functions as a modulator of calcium-binding by calmodulin. Thereby, regulates calmodulin activity and the different processes it controls. For instance, may play a role in neuronal differentiation through activation of calmodulin-dependent kinase signaling pathways. {ECO:0000250|UniProtKB:P48539}. SUBUNIT: Binds to both calcium-free and calcium-bound calmodulin. The affinity for the calcium-bound form is 50-fold greater. {ECO:0000250|UniProtKB:P48539}. DOMAIN: Mostly intrinsically disordered, with residual structure localized to the IQ domain which mediates the interaction with calmodulin. {ECO:0000250|UniProtKB:P48539}. +Q9QXV0 PCSK1_MOUSE ProSAAS (IA-4) (Proprotein convertase subtilisin/kexin type 1 inhibitor) (Proprotein convertase 1 inhibitor) (pro-SAAS) [Cleaved into: KEP; Big SAAS (b-SAAS); Little SAAS (l-SAAS); Big PEN-LEN (b-PEN-LEN) (SAAS CT(1-49)); PEN; PEN-20; PEN-19; Little LEN (l-LEN); Big LEN (b-LEN) (SAAS CT(25-40))] 258 27,270 Chain (1); Motif (1); Mutagenesis (1); Peptide (9); Region (2); Sequence conflict (1); Signal peptide (1) FUNCTION: May function in the control of the neuroendocrine secretory pathway. Proposed be a specific endogenous inhibitor of PCSK1. ProSAAS and Big PEN-LEN, both containing the C-terminal inhibitory domain, but not the processed peptides reduce PCSK1 activity in the endoplasmic reticulum and Golgi. It reduces the activity of the 87 kDa form but not the autocatalytically derived 66 kDa form of PCSK1. Subsequent processing of proSAAS may eliminate the inhibition. Slows down convertase-mediated processing of proopiomelanocortin and proenkephalin. May control the intracellular timing of PCSK1 rather than its total level of activity. The function of the processed secreted peptides is not known. {ECO:0000269|PubMed:10632593, ECO:0000269|PubMed:11719503, ECO:0000269|PubMed:11742530}. PTM: Proteolytically cleaved in the Golgi. Little SAAS, PEN, PEN-20 and Big LEN are the major processed peptides in proSAAS-overexpressing AtT-20 pituitary corticotropic cell line. {ECO:0000269|PubMed:10632593, ECO:0000269|PubMed:11094058, ECO:0000269|PubMed:11259501, ECO:0000269|PubMed:11719503, ECO:0000269|PubMed:11742530}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10632593, ECO:0000269|PubMed:11742530}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:11742530}. SUBUNIT: Interacts via the C-terminal inhibitory domain with PCSK1 66 kDa form. {ECO:0000250}. DOMAIN: ProSAAS(1-180) increases secretion of enzymatically inactive PCSK1.; DOMAIN: The C-terminal inhibitory domain is involved in inhibition of PCSK1. It corresponds to the probable processing intermediate Big PEN-LEN, binds to PCSK1 in vitro and contains the hexapeptide L-L-R-V-K-R, which, as a synthetic peptide, is sufficient for PCSK1 inhibition. TISSUE SPECIFICITY: Expressed in brain (mostly hypothalamus and pituitary) and gut. Expressed in trigeminal ganglia and neuroendocrine cell lines. PEN is expressed in pancreas, spinal cord and brain (most abundant in striatum, hippocampus, pons and medulla, and cortex) (at protein level). {ECO:0000269|PubMed:10632593, ECO:0000269|PubMed:11259501, ECO:0000269|PubMed:16631141, ECO:0000269|PubMed:9630436}. +Q04592 PCSK5_MOUSE Proprotein convertase subtilisin/kexin type 5 (EC 3.4.21.-) (Proprotein convertase 5) (PC5) (Proprotein convertase 6) (PC6) (Subtilisin-like proprotein convertase 6) (SPC6) (Subtilisin/kexin-like protease PC5) 1877 209,257 Active site (3); Alternative sequence (2); Chain (1); Domain (2); Glycosylation (13); Motif (1); Propeptide (1); Region (3); Repeat (22); Sequence conflict (6); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 1769 1789 Helical. {ECO:0000255}. TOPO_DOM 117 1768 Extracellular. {ECO:0000255}.; TOPO_DOM 1790 1877 Cytoplasmic. {ECO:0000255}. FUNCTION: Serine endoprotease that processes various proproteins by cleavage at paired basic amino acids, recognizing the RXXX[KR]R consensus motif. Likely functions in the constitutive and regulated secretory pathways. Plays an essential role in pregnancy establishment by proteolytic activation of a number of important factors such as BMP2, CALD1 and alpha-integrins. May be responsible for the maturation of gastrointestinal peptides. May be involved in the cellular proliferation of adrenal cortex via the activation of growth factors. {ECO:0000250}. SUBCELLULAR LOCATION: Isoform PC5A: Secreted. Note=Secreted through the regulated secretory pathway.; SUBCELLULAR LOCATION: Isoform PC5B: Endomembrane system; Single-pass type I membrane protein. Note=Type I membrane protein localized to a paranuclear post-Golgi network compartment in communication with early endosomes. DOMAIN: The propeptide domain acts as an intramolecular chaperone assisting the folding of the zymogen within the endoplasmic reticulum.; DOMAIN: AC 1 and AC 2 (clusters of acidic amino acids) contain sorting information. AC 1 directs TGN localization and interacts with the TGN sorting protein PACS-1. TISSUE SPECIFICITY: PC5A is expressed in most tissues but is most abundant in the intestine and adrenals. PC5B is expressed in the intestine, adrenals and lung but not in the brain. +Q9D5U0 PCT2B_MOUSE Lysophosphatidylcholine acyltransferase 2B (EC 2.3.1.-) (Acyltransferase-like 1-B) 516 58,381 Calcium binding (2); Chain (1); Domain (2); Glycosylation (1); Motif (1); Transmembrane (3) TRANSMEM 44 64 Helical. {ECO:0000255}.; TRANSMEM 68 88 Helical. {ECO:0000255}.; TRANSMEM 102 122 Helical. {ECO:0000255}. Lipid metabolism; phospholipid metabolism. FUNCTION: Probable acetyltransferase. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. DOMAIN: The HXXXXD motif is essential for acyltransferase activity. {ECO:0000250}. +Q9QYC1 PCX1_MOUSE Pecanex-like protein 1 (Pecanex homolog protein 1) 2344 258,147 Alternative sequence (1); Chain (1); Compositional bias (3); Erroneous initiation (1); Glycosylation (9); Sequence conflict (7); Transmembrane (10) TRANSMEM 33 53 Helical. {ECO:0000255}.; TRANSMEM 57 77 Helical. {ECO:0000255}.; TRANSMEM 1010 1030 Helical. {ECO:0000255}.; TRANSMEM 1035 1055 Helical. {ECO:0000255}.; TRANSMEM 1069 1089 Helical. {ECO:0000255}.; TRANSMEM 1119 1139 Helical. {ECO:0000255}.; TRANSMEM 1163 1183 Helical. {ECO:0000255}.; TRANSMEM 1196 1216 Helical. {ECO:0000255}.; TRANSMEM 1269 1289 Helical. {ECO:0000255}.; TRANSMEM 1297 1317 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +P70263 PD2R_MOUSE Prostaglandin D2 receptor (PGD receptor) (PGD2 receptor) (Prostanoid DP receptor) 357 40,005 Chain (1); Disulfide bond (1); Glycosylation (2); Sequence conflict (1); Topological domain (8); Transmembrane (7) TRANSMEM 21 41 Helical; Name=1. {ECO:0000255}.; TRANSMEM 59 79 Helical; Name=2. {ECO:0000255}.; TRANSMEM 107 127 Helical; Name=3. {ECO:0000255}.; TRANSMEM 150 170 Helical; Name=4. {ECO:0000255}.; TRANSMEM 195 215 Helical; Name=5. {ECO:0000255}.; TRANSMEM 262 282 Helical; Name=6. {ECO:0000255}.; TRANSMEM 307 327 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 20 Extracellular. {ECO:0000255}.; TOPO_DOM 42 58 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 80 106 Extracellular. {ECO:0000255}.; TOPO_DOM 128 149 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 171 194 Extracellular. {ECO:0000255}.; TOPO_DOM 216 261 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 283 306 Extracellular. {ECO:0000255}.; TOPO_DOM 328 357 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for prostaglandin D2 (PGD2). The activity of this receptor is mainly mediated by G(s) proteins that stimulate adenylate cyclase, resulting in an elevation of intracellular cAMP. A mobilization of calcium is also observed, but without formation of inositol 1,4,5-trisphosphate (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Most abundantly expressed in the ileum, followed by lung, stomach and uterus. +Q02242 PDCD1_MOUSE Programmed cell death protein 1 (Protein PD-1) (mPD-1) (CD antigen CD279) 288 31,842 Beta strand (12); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (4); Helix (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 170 190 Helical. {ECO:0000255}. TOPO_DOM 21 169 Extracellular. {ECO:0000255}.; TOPO_DOM 191 288 Cytoplasmic. {ECO:0000255}. FUNCTION: Inhibitory cell surface receptor involved in the regulation of T-cell function during immunity and tolerance. Upon ligand binding, inhibits T-cell effector functions in an antigen-specific manner. Possible cell death inducer, in association with other factors (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Monomer. {ECO:0000269|PubMed:15030777, ECO:0000269|PubMed:18287011, ECO:0000269|PubMed:18641123}. TISSUE SPECIFICITY: Thymus. +P46718 PDCD2_MOUSE Programmed cell death protein 2 (Zinc finger protein Rp-8) 343 38,342 Chain (1); Sequence conflict (2); Zinc finger (1) FUNCTION: May be a DNA-binding protein with a regulatory function. May play an important role in cell death and/or in regulation of cell proliferation. PTM: Ubiquitinated by PRKN, promoting proteasomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +P46664 PURA2_MOUSE Adenylosuccinate synthetase isozyme 2 (AMPSase 2) (AdSS 2) (EC 6.3.4.4) (Adenylosuccinate synthetase, acidic isozyme) (Adenylosuccinate synthetase, liver isozyme) (L-type adenylosuccinate synthetase) (IMP--aspartate ligase 2) 456 50,021 Active site (2); Binding site (7); Chain (1); Metal binding (2); Nucleotide binding (4); Region (3); Sequence conflict (2) Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. FUNCTION: Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000269|PubMed:12482871}. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03127}. +P27664 PDE6A_MOUSE Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha (GMP-PDE alpha) (EC 3.1.4.35) 859 99,530 Active site (1); Chain (1); Domain (3); Initiator methionine (1); Lipidation (1); Metal binding (5); Modified residue (2); Propeptide (1); Sequence conflict (5) FUNCTION: This protein participates in processes of transmission and amplification of the visual signal. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. SUBUNIT: Oligomer composed of two catalytic chains (alpha and beta), an inhibitory chain (gamma) and the delta chain. +P23440 PDE6B_MOUSE Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit beta (GMP-PDE beta) (EC 3.1.4.35) 856 98,535 Active site (1); Alternative sequence (1); Chain (1); Domain (3); Initiator methionine (1); Lipidation (1); Metal binding (5); Modified residue (1); Propeptide (1); Sequence conflict (7) FUNCTION: This protein participates in processes of transmission and amplification of the visual signal. Necessary for the formation of a functional phosphodiesterase holoenzyme. SUBCELLULAR LOCATION: Membrane; Lipid-anchor. SUBUNIT: Oligomer composed of two catalytic chains (alpha and beta), an inhibitory chain (gamma) and the delta chain. DISEASE: Note=Defects in Pde6b are the cause of retinal degeneration. {ECO:0000269|PubMed:1977087}. +Q925I7 PDGFD_MOUSE Platelet-derived growth factor D (PDGF-D) (Spinal cord-derived growth factor B) (SCDGF-B) [Cleaved into: Platelet-derived growth factor D, latent form (PDGFD latent form); Platelet-derived growth factor D, receptor-binding form (PDGFD receptor-binding form)] 370 42,809 Alternative sequence (3); Chain (2); Disulfide bond (4); Domain (1); Glycosylation (1); Sequence conflict (1); Signal peptide (1); Site (2) FUNCTION: Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen for cells of mesenchymal origin. Plays an important role in wound healing (By similarity). Has oncogenic potential and can induce tumor formation. Induces macrophage recruitment, increased interstitial pressure, and blood vessel maturation during angiogenesis. Can initiate events that lead to a mesangial proliferative glomerulonephritis, including influx of monocytes and macrophages and production of extracellular matrix. {ECO:0000250, ECO:0000269|PubMed:11980634, ECO:0000269|PubMed:14747375, ECO:0000269|PubMed:15271796}. PTM: Activated by proteolytic cleavage. Proteolytic removal of the N-terminal CUB domain releasing the core domain is necessary for unmasking the receptor-binding epitopes of the core domain. Cleavage after Arg-247 or Arg-249 by urokinase plasminogen activator gives rise to the active form (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Released by platelets upon wounding. {ECO:0000250}. SUBUNIT: Homodimer; disulfide-linked. Interacts with PDGFRB homodimers, and with heterodimers formed by PDGFRA and PDGFRB (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed at high levels in developing heart, lung, kidney and some muscle derivatives. Moderately expressed in liver, brain and testis. In the kidney, localized to glomerular mesangial cells and vascular smooth muscle cells. Up-regulated in areas of renal fibrosis. In mice with unilateral ureteral obstruction, expressed in interstitial cells at day 4, with an increased to maximal expression at day 14. {ECO:0000269|PubMed:11331881, ECO:0000269|PubMed:12890490, ECO:0000269|PubMed:14514732, ECO:0000269|PubMed:14747375}. +O55057 PDE6D_MOUSE Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta (GMP-PDE delta) 150 17,348 Beta strand (9); Chain (1); Helix (3); Region (1); Turn (2) FUNCTION: Promotes the release of prenylated target proteins from cellular membranes (PubMed:22179043). Modulates the activity of prenylated or palmitoylated Ras family members by regulating their subcellular location (PubMed:22179043). Required for normal ciliary targeting of farnesylated target proteins, such as INPP5E (By similarity). Modulates the subcellular location of target proteins by acting as a GTP specific dissociation inhibitor (GDI) (PubMed:22179043). Increases the affinity of ARL3 for GTP by several orders of magnitude. Stabilizes ARL3-GTP by decreasing the nucleotide dissociation rate. {ECO:0000250|UniProtKB:O43924, ECO:0000250|UniProtKB:Q95142, ECO:0000269|PubMed:10518933, ECO:0000269|PubMed:15979089, ECO:0000269|PubMed:22179043}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:22179043}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:O43924}; Peripheral membrane protein {ECO:0000250|UniProtKB:O43924}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:O43924}. SUBUNIT: Interacts with the prenylated catalytic subunits of PDE6, an oligomer composed of two catalytic chains (PDE6A and PDE6B) and two inhibitory chains (gamma); has no effect on enzyme activity but promotes the release of the prenylated enzyme from cell membrane (By similarity). Interacts with prenylated GRK1 and GRK7 (By similarity). Interacts with prenylated INPP5E (By similarity). Interacts with prenylated Ras family members, including HRAS, KRAS, NRAS, RAP2A, RAP2C and RHEB (PubMed:22179043). Interacts with RAB13 (prenylated form); dissociates RAB13 from membranes (By similarity). Interacts with RPGR (PubMed:9990021). Interacts with ARL2 (PubMed:15979089). Interacts with ARL3; the interaction occurs specifically with the GTP-bound form of ARL3 (PubMed:15979089). Interaction with ARL2 and ARL3 promotes release of farnesylated cargo proteins (By similarity). {ECO:0000250|UniProtKB:O43924, ECO:0000250|UniProtKB:Q95142, ECO:0000269|PubMed:10518933, ECO:0000269|PubMed:15979089, ECO:0000269|PubMed:22179043, ECO:0000269|PubMed:9990021}. +P20033 PDGFA_MOUSE Platelet-derived growth factor subunit A (PDGF subunit A) (PDGF-1) (Platelet-derived growth factor A chain) (Platelet-derived growth factor alpha polypeptide) 211 24,102 Alternative sequence (2); Chain (1); Disulfide bond (5); Glycosylation (1); Propeptide (1); Region (1); Sequence conflict (3); Signal peptide (1) FUNCTION: Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen for cells of mesenchymal origin. Required for normal lung alveolar septum formation during embryogenesis, normal development of the gastrointestinal tract, normal development of Leydig cells and spermatogenesis. Required for normal oligodendrocyte development and normal myelination in the spinal cord and cerebellum. Plays an important role in wound healing. Signaling is modulated by the formation of heterodimers with PDGFB. {ECO:0000269|PubMed:10831606, ECO:0000269|PubMed:10903171, ECO:0000269|PubMed:11803579, ECO:0000269|PubMed:19030102, ECO:0000269|PubMed:8681381, ECO:0000269|PubMed:9374392, ECO:0000269|PubMed:9876175}. SUBCELLULAR LOCATION: Secreted. Note=Released by platelets upon wounding. SUBUNIT: Homodimer; antiparallel disulfide-linked dimer. Heterodimer with PDGFB; antiparallel disulfide-linked dimer. The PDGFA homodimer interacts with PDGFRA homodimers, and with heterodimers formed by PDGFRA and PDGFRB. The heterodimer composed of PDGFA and PDGFB interacts with PDGFRA homodimers, and with heterodimers formed by PDGFRA and PDGFRB. Interacts with CSPG4 (By similarity). {ECO:0000250}. DOMAIN: The long form contains a basic insert which acts as a cell retention signal. TISSUE SPECIFICITY: Expression primarily localized in papillary regions with presumable expression in tubular cells comprising the loop of Henle. In the renal cortex, a widespread expression seen in the vascular smooth muscle cells and is barely detectable in interstitial cells. {ECO:0000269|PubMed:14514732}. +P27773 PDIA3_MOUSE Protein disulfide-isomerase A3 (EC 5.3.4.1) (58 kDa glucose-regulated protein) (58 kDa microsomal protein) (p58) (Disulfide isomerase ER-60) (Endoplasmic reticulum resident protein 57) (ER protein 57) (ERp57) (Endoplasmic reticulum resident protein 60) (ER protein 60) (ERp60) 505 56,678 Active site (4); Chain (1); Disulfide bond (4); Domain (2); Modified residue (8); Motif (1); Sequence conflict (8); Signal peptide (1); Site (6) PTM: Phosphorylated. {ECO:0000269|Ref.7}. SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:P30101}. Endoplasmic reticulum lumen {ECO:0000250}. Melanosome {ECO:0000250|UniProtKB:P30101}. SUBUNIT: Subunit of the TAP complex, also known as the peptide loading complex (PLC). Can form disulfide-linked heterodimers with TAPBP. Interacts with ERP27 and CANX (By similarity). Interacts with MZB1 in a calcium-dependent manner. Interacts with SERPINA2 and with the S and Z variants of SERPINA1 (By similarity). Interacts with ATP2A2 (PubMed:23395171). {ECO:0000250|UniProtKB:P30101, ECO:0000269|PubMed:23395171}. TISSUE SPECIFICITY: In caput and cauda epididymal spermatozoa, detected in the acrosome and principal piece (at protein level). {ECO:0000269|PubMed:20400973}. +Q8QZR7 PDK1L_MOUSE Serine/threonine-protein kinase PDIK1L (EC 2.7.11.1) (PDLIM1-interacting kinase 1-like) 341 38,550 Active site (1); Binding site (1); Chain (1); Domain (1); Nucleotide binding (1); Sequence conflict (2) SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +Q8BFP9 PDK1_MOUSE [Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 1, mitochondrial (EC 2.7.11.2) (Pyruvate dehydrogenase kinase isoform 1) (PDH kinase 1) 434 48,995 Binding site (1); Chain (1); Domain (1); Modified residue (4); Nucleotide binding (3); Sequence conflict (1); Transit peptide (1) FUNCTION: Kinase that plays a key role in regulation of glucose and fatty acid metabolism and homeostasis via phosphorylation of the pyruvate dehydrogenase subunits PDHA1 and PDHA2. This inhibits pyruvate dehydrogenase activity, and thereby regulates metabolite flux through the tricarboxylic acid cycle, down-regulates aerobic respiration and inhibits the formation of acetyl-coenzyme A from pyruvate. Plays an important role in cellular responses to hypoxia and is important for cell proliferation under hypoxia. Protects cells against apoptosis in response to hypoxia and oxidative stress (By similarity). {ECO:0000250, ECO:0000269|PubMed:16517406}. PTM: Phosphorylated by constitutively activated ABL1, FGFR1, FLT3 and JAK2 (in vitro), and this may also occur in cancer cells that express constitutively activated ABL1, FGFR1, FLT3 and JAK2. Phosphorylation at Tyr-241 and Tyr-242 strongly increases kinase activity, while phosphorylation at Tyr-136 has a lesser effect (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. SUBUNIT: Homodimer, and heterodimer with PDK2. Interacts with the pyruvate dehydrogenase complex subunit DLAT, and is part of the multimeric pyruvate dehydrogenase complex that contains multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3) (By similarity). {ECO:0000250}. +Q9Z2A0 PDPK1_MOUSE 3-phosphoinositide-dependent protein kinase 1 (mPDK1) (EC 2.7.11.1) 559 63,759 Active site (1); Binding site (4); Chain (1); Compositional bias (1); Domain (2); Modified residue (15); Nucleotide binding (2); Region (1); Sequence conflict (4) FUNCTION: Serine/threonine kinase which acts as a master kinase, phosphorylating and activating a subgroup of the AGC family of protein kinases. Its targets include: protein kinase B (PKB/AKT1, PKB/AKT2, PKB/AKT3), p70 ribosomal protein S6 kinase (RPS6KB1), p90 ribosomal protein S6 kinase (RPS6KA1, RPS6KA2 and RPS6KA3), cyclic AMP-dependent protein kinase (PRKACA), protein kinase C (PRKCD and PRKCZ), serum and glucocorticoid-inducible kinase (SGK1, SGK2 and SGK3), p21-activated kinase-1 (PAK1), protein kinase PKN (PKN1 and PKN2). Plays a central role in the transduction of signals from insulin by providing the activating phosphorylation to PKB/AKT1, thus propagating the signal to downstream targets controlling cell proliferation and survival, as well as glucose and amino acid uptake and storage. Negatively regulates the TGF-beta-induced signaling by: modulating the association of SMAD3 and SMAD7 with TGF-beta receptor, phosphorylating SMAD2, SMAD3, SMAD4 and SMAD7, preventing the nuclear translocation of SMAD3 and SMAD4 and the translocation of SMAD7 from the nucleus to the cytoplasm in response to TGF-beta. Activates PPARG transcriptional activity and promotes adipocyte differentiation. Activates the NF-kappa-B pathway via phosphorylation of IKKB. The tyrosine phosphorylated form is crucial for the regulation of focal adhesions by angiotensin II. Controls proliferation, survival, and growth of developing pancreatic cells. Participates in the regulation of Ca(2+) entry and Ca(2+)-activated K(+) channels of mast cells. Essential for the motility of vascular endothelial cells (ECs) and is involved in the regulation of their chemotaxis. Plays a critical role in cardiac homeostasis by serving as a dual effector for cell survival and beta-adrenergic response. Plays an important role during thymocyte development by regulating the expression of key nutrient receptors on the surface of pre-T cells and mediating Notch-induced cell growth and proliferative responses. Provides negative feedback inhibition to toll-like receptor-mediated NF-kappa-B activation in macrophages. {ECO:0000269|PubMed:10792047, ECO:0000269|PubMed:16150867, ECO:0000269|PubMed:17371830, ECO:0000269|PubMed:17599070, ECO:0000269|PubMed:19429709, ECO:0000269|PubMed:19635472, ECO:0000269|PubMed:20584979, ECO:0000269|PubMed:21063107}. PTM: Phosphorylation on Ser-244 in the activation loop is required for full activity. PDPK1 itself can autophosphorylate Ser-244, leading to its own activation. Autophosphorylation is inhibited by the apoptotic C-terminus cleavage product of PKN2 (By similarity). Tyr-9 phosphorylation is critical for stabilization of both PDPK1 and the PDPK1/SRC complex via HSP90-mediated protection of PDPK1 degradation. Angiotensin II stimulates the tyrosine phosphorylation of PDPK1 in vascular smooth muscle in a calcium- and SRC-dependent manner. Phosphorylated on Tyr-9, Tyr-376 and Tyr-379 by INSR in response to insulin. Palmitate negatively regulates autophosphorylation at Ser-244 and palmitate-induced phosphorylation at Ser-532 and Ser-504 by PKC/PRKCQ negatively regulates its ability to phosphorylate PKB/AKT1. Phosphorylation at Thr-357 by MELK partially inhibits kinase activity, the inhibition is cooperatively enhanced by phosphorylation at Ser-397 and Ser-401 by MAP3K5 (By similarity). {ECO:0000250}.; PTM: Monoubiquitinated in the kinase domain, deubiquitinated by USP4. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17371830}. Nucleus {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:17371830}; Peripheral membrane protein {ECO:0000269|PubMed:17371830}. Cell junction, focal adhesion {ECO:0000250}. Note=Tyrosine phosphorylation seems to occur only at the cell membrane. Translocates to the cell membrane following insulin stimulation by a mechanism that involves binding to GRB14 and INSR. SRC and HSP90 promote its localization to the cell membrane. Its nuclear localization is dependent on its association with PTPN6 and its phosphorylation at Ser-396. Restricted to the nucleus in neuronal cells while in non-neuronal cells it is found in the cytoplasm. The Ser-244 phosphorylated form is distributed along the perinuclear region in neuronal cells while in non-neuronal cells it is found in both the nucleus and the cytoplasm. IGF1 transiently increases phosphorylation at Ser-241 of neuronal PDPK1, resulting in its translocation to other cellular compartments. The tyrosine-phosphorylated form colocalizes with PTK2B in focal adhesions after angiotensin II stimulation (By similarity). {ECO:0000250}. SUBUNIT: Homodimer in its autoinhibited state. Active as monomer. Interacts with NPRL2, PAK1, PTK2B, GRB14, STRAP and IKKB. The Tyr-9 phosphorylated form interacts with SRC, RASA1 and CRK (via their SH2 domains). Interacts with SGK3 in a phosphorylation-dependent manner. The tyrosine-phosphorylated form interacts with PTPN6. The Ser-244 phosphorylated form interacts with YWHAH and YWHAQ. Binds INSR in response to insulin. Interacts (via PH domain) with SMAD3, SMAD4 and SMAD7. Interacts with PKN2; the interaction stimulates PDPK1 autophosphorylation, its PI(3,4,5)P3-dependent kinase activity toward 'Ser-473' of AKT1 but also activates its kinase activity toward PRKCD and PRKCZ (By similarity). Interacts with PKN1 (via C-terminus) and PPARG. {ECO:0000250, ECO:0000269|PubMed:10792047, ECO:0000269|PubMed:16150867}. DOMAIN: The PH domain plays a pivotal role in the localization and nuclear import of PDPK1 and is also essential for its homodimerization. {ECO:0000250}.; DOMAIN: The PIF-pocket is a small lobe in the catalytic domain required by the enzyme for the binding to the hydrophobic motif of its substrates. It is an allosteric regulatory site that can accommodate small compounds acting as allosteric inhibitors. {ECO:0000250|UniProtKB:O15530}. TISSUE SPECIFICITY: Highly expressed in heart, brain, liver and testis, also expressed in embryonic cells. +Q3UV70 PDP1_MOUSE [Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrial (PDP 1) (EC 3.1.3.43) (Protein phosphatase 2C) (Pyruvate dehydrogenase phosphatase catalytic subunit 1) (PDPC 1) 538 61,180 Chain (1); Domain (1); Metal binding (5); Modified residue (1); Transit peptide (1) FUNCTION: Catalyzes the dephosphorylation and concomitant reactivation of the alpha subunit of the E1 component of the pyruvate dehydrogenase complex. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. SUBUNIT: Heterodimer of a catalytic (PDP1) and a regulatory (PDPR) subunit. {ECO:0000250}. +Q99K01 PDXD1_MOUSE Pyridoxal-dependent decarboxylase domain-containing protein 1 (EC 4.1.1.-) 787 87,335 Alternative sequence (5); Chain (1); Erroneous initiation (1); Modified residue (8); Sequence conflict (6) +Q8C5P5 NT5D1_MOUSE 5'-nucleotidase domain-containing protein 1 (EC 3.1.3.-) (Cytosolic 5'-nucleotidase II-like protein 1) 467 53,094 Active site (2); Alternative sequence (3); Chain (1); Metal binding (3); Modified residue (1); Sequence conflict (13) +Q5PT53 NTCP7_MOUSE Sodium/bile acid cotransporter 7 (Na(+)/bile acid cotransporter 7) (Solute carrier family 10 member 7) 340 37,256 Alternative sequence (2); Chain (1); Erroneous termination (1); Sequence conflict (1); Topological domain (11); Transmembrane (10) TRANSMEM 11 31 Helical. {ECO:0000255}.; TRANSMEM 38 58 Helical. {ECO:0000255}.; TRANSMEM 72 92 Helical. {ECO:0000255}.; TRANSMEM 117 137 Helical. {ECO:0000255}.; TRANSMEM 139 159 Helical. {ECO:0000255}.; TRANSMEM 164 184 Helical. {ECO:0000255}.; TRANSMEM 202 222 Helical. {ECO:0000255}.; TRANSMEM 235 255 Helical. {ECO:0000255}.; TRANSMEM 271 291 Helical. {ECO:0000255}.; TRANSMEM 299 319 Helical. {ECO:0000255}. TOPO_DOM 1 10 Cytoplasmic. {ECO:0000250|UniProtKB:Q0GE19}.; TOPO_DOM 32 37 Extracellular. {ECO:0000250|UniProtKB:Q0GE19}.; TOPO_DOM 59 71 Cytoplasmic. {ECO:0000250|UniProtKB:Q0GE19}.; TOPO_DOM 93 116 Extracellular. {ECO:0000250|UniProtKB:Q0GE19}.; TOPO_DOM 138 138 Cytoplasmic. {ECO:0000250|UniProtKB:Q0GE19}.; TOPO_DOM 160 163 Extracellular. {ECO:0000250|UniProtKB:Q0GE19}.; TOPO_DOM 185 201 Cytoplasmic. {ECO:0000250|UniProtKB:Q0GE19}.; TOPO_DOM 223 234 Extracellular. {ECO:0000250|UniProtKB:Q0GE19, ECO:0000305}.; TOPO_DOM 256 270 Cytoplasmic. {ECO:0000250|UniProtKB:Q0GE19}.; TOPO_DOM 292 298 Extracellular. {ECO:0000250|UniProtKB:Q0GE19}.; TOPO_DOM 320 340 Cytoplasmic. {ECO:0000250|UniProtKB:Q0GE19}. FUNCTION: Does not show transport activity towards bile acids or steroid sulfates (including taurocholate, cholate, chenodeoxycholate, estrone-3-sulfate, dehydroepiandrosterone sulfate (DHEAS) and pregnenolone sulfate). {ECO:0000250|UniProtKB:Q0GE19}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q0GE19}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q0GE19}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q0GE19}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q0GE19}. TISSUE SPECIFICITY: Expressed in heart, brain, colon, lung, liver, adrenal gland, stomach and ovary. Also expressed weakly in small intestine. {ECO:0000269|PubMed:17628207}. +Q8R480 NUP85_MOUSE Nuclear pore complex protein Nup85 (85 kDa nucleoporin) (FROUNT) (Nucleoporin Nup85) (Pericentrin-1) 656 74,776 Chain (1); Erroneous gene model prediction (2); Modified residue (2); Sequence conflict (1) FUNCTION: Essential component of the nuclear pore complex (NPC) that seems to be required for NPC assembly and maintenance. As part of the NPC Nup107-160 subcomplex plays a role in RNA export and in tethering NUP96/Nup98 and NUP153 to the nucleus. The Nup107-160 complex seems to be required for spindle assembly during mitosis. NUP85 is required for membrane clustering of CCL2-activated CCR2. Seems to be involved in CCR2-mediated chemotaxis of monocytes and may link activated CCR2 to the phosphatidyl-inositol 3-kinase-Rac-lammellipodium protrusion cascade. {ECO:0000250|UniProtKB:Q9BW27}. SUBCELLULAR LOCATION: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q9BW27}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q9BW27}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9BW27}. Cytoplasm {ECO:0000250|UniProtKB:Q9BW27}. Nucleus membrane {ECO:0000250|UniProtKB:Q9BW27}. Note=During mitosis, localizes to the kinetochores and spindle poles. Upon CCl2 stimulation translocates from the cytoplasm to the membrane and colocalizes with CCR2 at the front of migrating cells. {ECO:0000250|UniProtKB:Q9BW27}. SUBUNIT: Component of the nuclear pore complex (NPC). Component of the NPC Nup107-160 subcomplex, consisting of at least NUP107, NUP98/Nup96, NUP160, NUP133, NUP85, NUP37, NUP43 and SEC13. Interacts with NUP160, NUP133 and SEC13 (PubMed:12718872). Interacts with NUP37, NUP107 and NUP43. Interacts with CCR2. {ECO:0000250|UniProtKB:Q9BW27, ECO:0000269|PubMed:12718872}. +P50136 ODBA_MOUSE 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial (EC 1.2.4.4) (Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain) (BCKDE1A) (BCKDH E1-alpha) 442 50,371 Chain (1); Metal binding (3); Modified residue (7); Region (1); Transit peptide (1) FUNCTION: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). SUBCELLULAR LOCATION: Mitochondrion matrix. SUBUNIT: Heterotetramer of alpha and beta chains. {ECO:0000250}. +Q9D611 OCSTP_MOUSE Osteoclast stimulatory transmembrane protein (OC-STAMP) 498 54,574 Chain (1); Compositional bias (1); Frameshift (1); Topological domain (7); Transmembrane (6) TRANSMEM 52 72 Helical. {ECO:0000255}.; TRANSMEM 82 102 Helical. {ECO:0000255}.; TRANSMEM 122 142 Helical. {ECO:0000255}.; TRANSMEM 227 247 Helical. {ECO:0000255}.; TRANSMEM 304 324 Helical. {ECO:0000255}.; TRANSMEM 402 422 Helical. {ECO:0000255}. TOPO_DOM 1 51 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 73 81 Extracellular. {ECO:0000255}.; TOPO_DOM 103 121 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 143 226 Extracellular. {ECO:0000255}.; TOPO_DOM 248 303 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 325 401 Extracellular. {ECO:0000255}.; TOPO_DOM 423 498 Cytoplasmic. {ECO:0000255}. FUNCTION: Probable cell surface receptor that plays a role in cellular fusion and cell differentiation. Cooperates with DCSTAMP in modulating cell-cell fusion in both osteoclasts and foreign body giant cells (FBGCs). Involved in osteoclast bone resorption. Promotes osteoclast differentiation and may play a role in the multinucleated osteoclast maturation. {ECO:0000269|PubMed:18064667, ECO:0000269|PubMed:20882308, ECO:0000269|PubMed:22337159}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in osteoclast (at protein level). Ubiquitous. Highly expressed in multi-nuclear osteoclast cells compared to mono-nuclear macrophages. Expressed in foreign body giant cells (FBGCs). {ECO:0000269|PubMed:18064667, ECO:0000269|PubMed:20882308, ECO:0000269|PubMed:22337159}. +Q60597 ODO1_MOUSE 2-oxoglutarate dehydrogenase, mitochondrial (EC 1.2.4.2) (2-oxoglutarate dehydrogenase complex component E1) (OGDC-E1) (Alpha-ketoglutarate dehydrogenase) 1023 116,449 Alternative sequence (3); Calcium binding (1); Chain (1); Cross-link (1); Erroneous initiation (2); Metal binding (1); Modified residue (5); Region (1); Sequence conflict (4); Transit peptide (1) FUNCTION: 2-oxoglutarate dehydrogenase (E1) component of the 2-oxoglutarate dehydrogenase complex, which mediates the decarboxylation of alpha-ketoglutarate. The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). The 2-oxoglutarate dehydrogenase complex is mainly active in the mitochondrion. A fraction of the 2-oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation of histones: associates with KAT2A on chromatin and provides succinyl-CoA to histone succinyltransferase KAT2A. {ECO:0000250|UniProtKB:Q02218}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:Q02218}. Nucleus {ECO:0000250|UniProtKB:Q02218}. Note=Mainly localizes in the mitochondrion. A small fraction localizes to the nucleus, where the 2-oxoglutarate dehydrogenase complex is required for histone succinylation. {ECO:0000250|UniProtKB:Q02218}. SUBUNIT: The 2-oxoglutarate dehydrogenase complex is composed of OGDH (2-oxoglutarate dehydrogenase; E1), DLST (dihydrolipoamide succinyltransferase; E2) and DLD (dihydrolipoamide dehydrogenase; E3). It contains multiple copies of the three enzymatic components (E1, E2 and E3). In the nucleus, the 2-oxoglutarate dehydrogenase complex associates with KAT2A. {ECO:0000250|UniProtKB:Q02218}. +A2A8Z1 OSBL9_MOUSE Oxysterol-binding protein-related protein 9 (ORP-9) (OSBP-related protein 9) 736 83,109 Alternative sequence (2); Chain (1); Domain (1); Initiator methionine (1); Modified residue (7) SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250}. Note=Localizes at the Golgi-late endosome interface. {ECO:0000250}. SUBUNIT: Heterodimer with OSBPL11. Interacts with OSBPL10. {ECO:0000250|UniProtKB:Q96SU4}. +Q5QNQ6 OSBP2_MOUSE Oxysterol-binding protein 2 908 101,353 Chain (1); Domain (1); Modified residue (1) FUNCTION: Binds 7-ketocholesterol. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. +Q91XL9 OSBL1_MOUSE Oxysterol-binding protein-related protein 1 (ORP-1) (OSBP-related protein 1) 950 107,795 Alternative sequence (2); Beta strand (1); Chain (1); Coiled coil (2); Domain (1); Helix (8); Modified residue (1); Region (1); Repeat (3); Sequence conflict (8) FUNCTION: Binds phospholipids; exhibits strong binding to phosphatidic acid and weak binding to phosphatidylinositol 3-phosphate. Stabilizes GTP-bound RAB7A on late endosomes/lysosomes and alters functional properties of late endocytic compartments via its interaction with RAB7A. Binds 25-hydroxycholesterol and cholesterol. {ECO:0000250|UniProtKB:Q9BXW6}. SUBCELLULAR LOCATION: Late endosome {ECO:0000250}. Note=Co-localizes with RAB7A, RAB9A and LAMP1 in late endosomes. {ECO:0000250}. SUBUNIT: Interacts with VAPA (By similarity). Interacts with the GTP-bound form of RAB7A (By similarity). Interacts with OAS1B. {ECO:0000250, ECO:0000269|PubMed:22623793}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12215260}. +Q9DBS9 OSBL3_MOUSE Oxysterol-binding protein-related protein 3 (ORP-3) (OSBP-related protein 3) 855 96,966 Chain (1); Domain (1); Modified residue (12); Motif (2); Sequence conflict (1) FUNCTION: Phosphoinositide-binding protein which associates with both cell and endoplasmic reticulum (ER) membranes. Can bind to the ER membrane protein VAPA and recruit VAPA to plasma membrane sites, thus linking these intracellular compartments. The ORP3-VAPA complex stimulates RRAS signaling which in turn attenuates integrin beta-1 (ITGB1) activation at the cell surface. With VAPA, may regulate ER morphology. Has a role in regulation of the actin cytoskeleton, cell polarity and cell adhesion. Binds to phosphoinositides with preference for PI(3,4)P2 and PI(3,4,5)P3. Also binds 25-hydroxycholesterol and cholesterol. {ECO:0000250|UniProtKB:Q9H4L5}. PTM: Phosphorylation is enhanced in vitro by phorbol-12-myristate-13-acetate (PMA), forskolin and calcium ionophore A23187. Phosphorylation seems to be stimulated in conditions of low cell-cell (or cell-matrix) adhesion. {ECO:0000250|UniProtKB:Q9H4L5}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9H4L5}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9H4L5}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9H4L5}. Cell membrane {ECO:0000250|UniProtKB:Q9H4L5}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9H4L5}. Cell projection, filopodium tip {ECO:0000250|UniProtKB:Q9H4L5}. Nucleus membrane {ECO:0000250|UniProtKB:Q9H4L5}; Peripheral membrane protein {ECO:0000305}. SUBUNIT: Homodimer. Interacts with RRAS. Interacts (phosphorylated form) with VAPA. {ECO:0000250|UniProtKB:Q9H4L5}. DOMAIN: The FFAT 2 motif is required for interaction with VAPA and regulation of the endoplasmic reticulum targeting of ORP3. The FFAT 1 motif may contribute to VAPA binding. {ECO:0000250|UniProtKB:Q9H4L5}.; DOMAIN: The PH domain binds phosphoinositides, with a preference for PI(3,4)P2 and PI(3,4,5)P3. The PH domain mediates targeting to the plasma membrane. {ECO:0000250|UniProtKB:Q9H4L5}. TISSUE SPECIFICITY: Expressed in spinal ganglia. Expressed in a subset of small lymphocytes (at protein level). {ECO:0000269|PubMed:14593528}. +Q64512 PTN13_MOUSE Tyrosine-protein phosphatase non-receptor type 13 (EC 3.1.3.48) (PTP36) (Protein tyrosine phosphatase DPZPTP) (Protein tyrosine phosphatase PTP-BL) (Protein-tyrosine phosphatase RIP) 2453 270,334 Active site (1); Beta strand (7); Binding site (2); Chain (1); Coiled coil (1); Compositional bias (1); Domain (8); Helix (2); Modified residue (13); Region (1); Sequence conflict (16) FUNCTION: Tyrosine phosphatase which regulates negatively FAS-induced apoptosis and NGFR-mediated pro-apoptotic signaling. May regulate phosphoinositide 3-kinase (PI3K) signaling through dephosphorylation of PIK3R2. {ECO:0000250|UniProtKB:Q12923}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q12923}. Nucleus {ECO:0000250|UniProtKB:Q12923}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q12923}. Note=Colocalizes with PKN2 in lamellipodia-like structure, regions of large actin turnover. {ECO:0000250|UniProtKB:Q12923}. SUBUNIT: Interacts (via the first PDZ domain) with PLEKHA1 and PLEKHA2. Interacts (via the second PDZ domain) with TNFRSF6 (Fas receptor) (via C-terminus) (By similarity). Interacts (via the second PDZ domain) with TRIP6 (via the third LIM domain and C-terminus) (PubMed:10826496). Interacts (via the third PDZ domain) with NGFR (via C-terminal SVP motif) and PKN2 (via C-terminus) (By similarity). Interacts (via the second or fourth PDZ domains) with PDLIM4 (via C-terminus only or via combined C-terminus and LIM domain, but not LIM domain only) (PubMed:9487134, PubMed:15663004). Found in a complex with PDLIM4 and TRIP6 (PubMed:10826496). Interacts with PDLIM4; this interaction results in dephosphorylation of SRC 'Tyr-419' by this protein leading to its inactivation (By similarity). Interacts with BRD7 (PubMed:10526152). Interacts with RAPGEF6. Interacts with ARHGAP29. Interacts with PIK3R2; dephosphorylates PIK3R2. Interacts with FBXL2 (By similarity). Interacts (via the FERM domain) with ENTR1 (PubMed:23108400). Found in a complex with ENTR1, PTPN13 and GIT1 (PubMed:23108400). {ECO:0000250|UniProtKB:Q12923, ECO:0000269|PubMed:10526152, ECO:0000269|PubMed:10826496, ECO:0000269|PubMed:15663004, ECO:0000269|PubMed:23108400, ECO:0000269|PubMed:9487134}. TISSUE SPECIFICITY: Expressed predominantly in kidney and, to a lesser extent, in lung, heart, brain and testis. +B9EJ86 OSBL8_MOUSE Oxysterol-binding protein-related protein 8 (ORP-8) (OSBP-related protein 8) 889 101,269 Binding site (5); Chain (1); Domain (1); Erroneous gene model prediction (1); Modified residue (11); Region (4); Transmembrane (1) TRANSMEM 871 888 Helical. {ECO:0000255}. FUNCTION: Lipid transporter involved in lipid countertransport between the endoplasmic reticulum and the plasma membrane: specifically exchanges phosphatidylserine with phosphatidylinositol 4-phosphate (PI4P), delivering phosphatidylserine to the plasma membrane in exchange for PI4P, which is degraded by the SAC1/SACM1L phosphatase in the endoplasmic reticulum. Binds phosphatidylserine and PI4P in a mutually exclusive manner. Binds oxysterol, 25-hydroxycholesterol and cholesterol. {ECO:0000250|UniProtKB:Q9BZF1}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9BZF1}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9BZF1}. Nucleus membrane {ECO:0000250|UniProtKB:Q9BZF1}. Note=The presence of the N-terminus extension contains an overall negative charge that may explain the weak localization to the cortical endoplasmic reticulum. {ECO:0000250|UniProtKB:Q9BZF1}. SUBUNIT: Interacts with SPAG5. Interacts with NUP62. {ECO:0000250|UniProtKB:Q9BZF1}. TISSUE SPECIFICITY: Widely expressed. Most abundant in liver, spleen, kidney, brain and adipose tissue. {ECO:0000269|PubMed:17991739}. +P35821 PTN1_MOUSE Tyrosine-protein phosphatase non-receptor type 1 (EC 3.1.3.48) (Protein-tyrosine phosphatase 1B) (PTP-1B) (Protein-tyrosine phosphatase HA2) (PTP-HA2) 432 49,593 Active site (1); Binding site (2); Chain (1); Domain (1); Modified residue (12); Region (1); Sequence conflict (3) FUNCTION: Tyrosine-protein phosphatase which acts as a regulator of endoplasmic reticulum unfolded protein response. Mediates dephosphorylation of EIF2AK3/PERK; inactivating the protein kinase activity of EIF2AK3/PERK. May play an important role in CKII- and p60c-src-induced signal transduction cascades. May regulate the EFNA5-EPHA3 signaling pathway which modulates cell reorganization and cell-cell repulsion. May also regulate the hepatocyte growth factor receptor signaling pathway through dephosphorylation of MET (By similarity). {ECO:0000250}. PTM: Ser-50 is the major site of phosphorylation as compared to Ser-242 and Ser-243. Activated by phosphorylation at Ser-50 (By similarity). {ECO:0000250}.; PTM: S-nitrosylation of Cys-215 inactivates the enzyme activity. {ECO:0000250}.; PTM: Sulfhydration at Cys-215 following endoplasmic reticulum stress inactivates the enzyme activity, promoting EIF2AK3/PERK activity. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Interacts with EPHA3 at the cell membrane. {ECO:0000250}. SUBUNIT: Interacts with EPHA3 (phosphorylated); dephosphorylates EPHA3 and may regulate its trafficking and function. Interacts with MET. {ECO:0000250}. TISSUE SPECIFICITY: Most abundant in testis. Also found in kidney, spleen, muscle, liver, heart and brain. +O55082 PTN20_MOUSE Tyrosine-protein phosphatase non-receptor type 20 (EC 3.1.3.48) (Testis-specific tyrosine phosphatase) 426 49,119 Active site (1); Alternative sequence (2); Binding site (2); Chain (1); Domain (1); Modified residue (2); Region (1) FUNCTION: Tyrosine-protein phosphatase targeted to sites of actin polymerization in response of varied extracellular stimuli. Has tyrosine phosphatase activity towards various tyrosyl phosphorylated substrates. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Note=Colocalizes with the microtubule-organizing center and intracellular membrane compartments. {ECO:0000250}. TISSUE SPECIFICITY: Testis-specific. Specifically expressed in testicular germ cells that undergo meiosis (at protein level). {ECO:0000269|PubMed:9407093}. +Q6PB44 PTN23_MOUSE Tyrosine-protein phosphatase non-receptor type 23 (EC 3.1.3.48) 1692 185,216 Active site (1); Alternative sequence (1); Chain (1); Coiled coil (1); Compositional bias (2); Domain (2); Erroneous initiation (1); Modified residue (6); Region (2); Repeat (23); Sequence conflict (1) FUNCTION: Plays a role in sorting of endocytic ubiquitinated cargos into multivesicular bodies (MVBs) via its interaction with the ESCRT-I complex (endosomal sorting complex required for transport I), and possibly also other ESCRT complexes. May act as a negative regulator of Ras-mediated mitogenic activity. Plays a role in ciliogenesis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Endosome {ECO:0000250}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250}. SUBUNIT: Interacts with GRAP2 and GRB2. Interacts with UBAP1 and CHMP4B (By similarity). {ECO:0000250}. +Q9WU22 PTN4_MOUSE Tyrosine-protein phosphatase non-receptor type 4 (EC 3.1.3.48) (Testis-enriched protein tyrosine phosphatase) 926 105,832 Active site (1); Binding site (2); Chain (1); Domain (3); Modified residue (1); Region (1); Sequence conflict (5) FUNCTION: May act at junctions between the membrane and the cytoskeleton. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in testis. Specifically expressed in spermatocytes and spermatids within seminiferous tubules (at protein level). {ECO:0000269|PubMed:11054567}. +Q8R000 OSTA_MOUSE Organic solute transporter subunit alpha (OST-alpha) (Solute carrier family 51 subunit alpha) 340 37,759 Chain (1); Compositional bias (1); Glycosylation (1); Modified residue (1); Topological domain (8); Transmembrane (7) TRANSMEM 49 69 Helical. {ECO:0000255}.; TRANSMEM 88 108 Helical. {ECO:0000255}.; TRANSMEM 115 135 Helical. {ECO:0000255}.; TRANSMEM 182 202 Helical. {ECO:0000255}.; TRANSMEM 220 240 Helical. {ECO:0000255}.; TRANSMEM 256 276 Helical. {ECO:0000255}.; TRANSMEM 298 317 Helical. {ECO:0000255}. TOPO_DOM 1 48 Extracellular. {ECO:0000255}.; TOPO_DOM 70 87 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 109 114 Extracellular. {ECO:0000255}.; TOPO_DOM 136 181 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 203 219 Extracellular. {ECO:0000255}.; TOPO_DOM 241 255 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 277 297 Extracellular. {ECO:0000255}.; TOPO_DOM 318 340 Cytoplasmic. {ECO:0000255}. FUNCTION: Essential component of the Ost-alpha/Ost-beta complex, a heterodimer that acts as the intestinal basolateral transporter responsible for bile acid export from enterocytes into portal blood. Efficiently transports the major species of bile acids. {ECO:0000269|PubMed:15563450, ECO:0000269|PubMed:16317684, ECO:0000269|PubMed:18292224, ECO:0000269|PubMed:22535958}. PTM: N-glycosylated. {ECO:0000305|PubMed:15563450}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. Note=Mainly restricted to the lateral and basal membranes of ileal enterocytes. Transported from the endoplasmic reticulum to the plasma membrane upon interacting with SLC51B. SUBUNIT: Interacts with SLC51B. The Ost-alpha/Ost-beta complex is a heterodimer composed of alpha (SLC51A) and beta (SLC51B) subunit. {ECO:0000269|PubMed:17650074}. TISSUE SPECIFICITY: Present at high levels in ileum. In ileum, it is restricted to the apical domain on the mature villus enterocytes with little detectable expression in the goblet cells or crypt enterocytes (at protein level). Expressed in kidney but not in heart, brain, liver, spleen, embryo, lung, thymus, ovary nor testis. {ECO:0000269|PubMed:15563450, ECO:0000269|PubMed:16317684}. +P54830 PTN5_MOUSE Tyrosine-protein phosphatase non-receptor type 5 (EC 3.1.3.48) (Neural-specific protein-tyrosine phosphatase) (Striatum-enriched protein-tyrosine phosphatase) (STEP) 541 60,815 Active site (1); Alternative sequence (3); Beta strand (9); Binding site (2); Chain (1); Domain (1); Helix (15); Modified residue (3); Region (1); Sequence conflict (1); Transmembrane (2); Turn (3) TRANSMEM 64 84 Helical. {ECO:0000255}.; TRANSMEM 122 142 Helical. {ECO:0000255}. FUNCTION: May regulate the activity of several effector molecules involved in synaptic plasticity and neuronal cell survival, including MAPKs, Src family kinases and NMDA receptors. {ECO:0000250}. PTM: Phosphorylation at Ser-221 by PKA deactivates PTPN5. Phosphorylation at Thr-231 and Ser-244 by MAPKs stabilizes the phosphatase, dephosphorylation of these sites results in ubiquitin-mediated degradation of the active phosphatase (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Isoform STEP61: Endoplasmic reticulum membrane; Multi-pass membrane protein.; SUBCELLULAR LOCATION: Isoform STEP46: Cytoplasm. TISSUE SPECIFICITY: STEP20 is expressed only in the CNS. +O54734 OST48_MOUSE Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit (DDOST 48 kDa subunit) (Oligosaccharyl transferase 48 kDa subunit) 441 49,028 Chain (1); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 413 432 Helical. {ECO:0000255}. TOPO_DOM 29 412 Lumenal. {ECO:0000255}.; TOPO_DOM 433 441 Cytoplasmic. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity (By similarity). Required for the assembly of both SST3A- and SS3B-containing OST complexes (By similarity). {ECO:0000250|UniProtKB:P39656, ECO:0000250|UniProtKB:Q05052}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q29381}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q29381}. SUBUNIT: Component of the oligosaccharyltransferase (OST) complex. OST exists in two different complex forms which contain common core subunits RPN1, RPN2, OST48, OST4, DAD1 and TMEM258, either STT3A or STT3B as catalytic subunits, and form-specific accessory subunits. STT3A complex assembly occurs through the formation of 3 subcomplexes. Subcomplex 1 contains RPN1 and TMEM258, subcomplex 2 contains the STT3A-specific subunits STT3A, DC2/OSTC, and KCP2 as well as the core subunit OST4, and subcomplex 3 contains RPN2, DAD1, and OST48. The STT3A complex can form stable complexes with the Sec61 complex or with both the Sec61 and TRAP complexes. {ECO:0000250|UniProtKB:Q05052}. +Q66GT5 PTPM1_MOUSE Phosphatidylglycerophosphatase and protein-tyrosine phosphatase 1 (EC 3.1.3.27) (PTEN-like phosphatase) (Phosphoinositide lipid phosphatase) (Protein-tyrosine phosphatase mitochondrial 1) (EC 3.1.3.16) (EC 3.1.3.48) 193 21,943 Active site (1); Beta strand (5); Chain (1); Domain (1); Erroneous initiation (2); Frameshift (1); Helix (7); Modified residue (1); Mutagenesis (6); Transit peptide (1); Turn (2) Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 2/2. FUNCTION: Lipid phosphatase which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG) (PubMed:21641550, PubMed:21730175). PGP is an essential intermediate in the biosynthetic pathway of cardiolipin, a mitochondrial-specific phospholipid regulating the membrane integrity and activities of the organelle (PubMed:21641550). Has also been shown to display phosphatase activity toward phosphoprotein substrates, specifically mediates dephosphorylation of mitochondrial proteins, thereby playing an essential role in ATP production (By similarity). Has probably a preference for proteins phosphorylated on Ser and/or Thr residues compared to proteins phosphorylated on Tyr residues (By similarity). Probably involved in regulation of insulin secretion in pancreatic beta cells (By similarity). May prevent intrinsic apoptosis, probably by regulating mitochondrial membrane integrity (By similarity). {ECO:0000250|UniProtKB:P0C089, ECO:0000250|UniProtKB:Q8WUK0, ECO:0000269|PubMed:16039589, ECO:0000269|PubMed:21641550}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:16039589}; Peripheral membrane protein {ECO:0000250|UniProtKB:P0C089}; Matrix side {ECO:0000250|UniProtKB:P0C089}. SUBUNIT: Interacts with STYXL1; the interaction inhibits PTPMT1 catalytic activity. {ECO:0000250|UniProtKB:Q8WUK0}. TISSUE SPECIFICITY: Predominantly expressed in testis. Expressed at lower level in heart, brain, spleen, lung, liver, skeletal muscle, kidney, bone marrow, eye, lymph node, smooth muscle, prostate, thymus, stomach and uterus. {ECO:0000269|PubMed:15247229}. +P80560 PTPR2_MOUSE Receptor-type tyrosine-protein phosphatase N2 (R-PTP-N2) (EC 3.1.3.-) (EC 3.1.3.48) (PTP IA-2beta) (Phogrin) (Protein tyrosine phosphatase-NP) (PTP-NP) [Cleaved into: IA-2beta71; IA-2beta64; IA-2beta60] 1001 111,497 Active site (1); Binding site (2); Chain (4); Domain (1); Glycosylation (1); Modified residue (8); Motif (2); Mutagenesis (2); Region (2); Sequence conflict (10); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 601 621 Helical. {ECO:0000255}. TOPO_DOM 28 600 Extracellular. {ECO:0000255}.; TOPO_DOM 622 1001 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a role in vesicle-mediated secretory processes (PubMed:21732083). Required for normal accumulation of secretory vesicles in hippocampus, pituitary and pancreatic islets. Required for the accumulation of normal levels of insulin-containing vesicles and preventing their degradation (PubMed:21732083). Plays a role in insulin secretion in response to glucose stimuli (PubMed:15220191, PubMed:16418280, PubMed:21732083). Required for normal accumulation of the neurotransmitters norepinephrine, dopamine and serotonin in the brain. In females, but not in males, required for normal accumulation and secretion of pituitary hormones, such as luteinizing hormone (LH) and follicle-stimulating hormone (FSH) (PubMed:16269463). Required to maintain normal levels of renin expression and renin release (PubMed:19019914). May regulate catalytic active protein-tyrosine phosphatases such as PTPRA through dimerization (PubMed:12364328). Has phosphatidylinositol phosphatase activity; the PIPase activity is involved in its ability to regulate insulin secretion. Can dephosphorylate phosphatidylinositol 4,5-biphosphate (PI(4,5)P2), phosphatidylinositol 5-phosphate and phosphatidylinositol 3-phosphate (By similarity). Regulates PI(4,5)P2 level in the plasma membrane and localization of cofilin at the plasma membrane and thus is indirectly involved in regulation of actin dynamics related to cell migration and metastasis; upon hydrolyzation of PI(4,5)P2 cofilin is released from the plasma membrane and acts in the cytoplasm in severing F-actin filaments (By similarity). {ECO:0000250|UniProtKB:Q63475, ECO:0000250|UniProtKB:Q92932, ECO:0000269|PubMed:12364328, ECO:0000269|PubMed:15220191, ECO:0000269|PubMed:16269463, ECO:0000269|PubMed:16418280, ECO:0000269|PubMed:19019914, ECO:0000269|PubMed:21732083}. PTM: Subject to proteolytic cleavage at multiple sites during maturation of secretory granules. In the brain at least IA-2beta71, IA-2beta64 and IA-2beta60 have been detected, in the pancreas and a pancreatic beta cell line only IA-2beta60 has been detected. {ECO:0000269|PubMed:17611635, ECO:0000269|PubMed:8637868}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000269|PubMed:19361477}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:19361477}; Single-pass type I membrane protein {ECO:0000305}. Note=Predominantly found on dense-core secretory granules. Sorting to secretory granules in part is dependent of the N-terminal pro domain of the precursor and its interaction with CPE. Transiently found at the cell membrane, when secretory vesicles fuse with the cell membrane to release their cargo. Is then endocytosed and recycled to secretory vesicles involving clathrin-dependent AP2-mediated endocytosis. Recycled via STX6- but not TTTGN1/TGN38-containing compartments. {ECO:0000250|UniProtKB:Q63475, ECO:0000269|PubMed:15485654, ECO:0000269|PubMed:21210912, ECO:0000305}.; SUBCELLULAR LOCATION: IA-2beta60: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000305}. SUBUNIT: Self-associates. Interacts (via cytoplasmic domain) with PTPRN (via cytoplasmic domain) (PubMed:12364328). Interacts (precursor form) with CPE (PubMed:21210912). Interacts with HAP1 isoform A (PubMed:21544547). Interacts with AP2A1 or AP2A2 and AP1G1; indicative for an association with adaptor protein complex 2 (AP-2) and adaptor protein complex 1 (AP-1) (PubMed:16262730). Interacts with AP2M1; indicative for an association with adaptor protein complex 2 (AP-2). Interacts with MYO5A (By similarity). {ECO:0000250|UniProtKB:Q63475, ECO:0000269|PubMed:12364328, ECO:0000269|PubMed:16262730, ECO:0000269|PubMed:21210912}. DOMAIN: The tyrosine-based internalization signal is proposed to function in clathrin-mediated endocytosis and recycling. {ECO:0000250|UniProtKB:Q63475}.; DOMAIN: The leucine-based sorting signal is proposed to function in trafficking at the plasma membrane. {ECO:0000305|PubMed:16262730}. TISSUE SPECIFICITY: Detected in brain (PubMed:15220191, PubMed:19361477). Detected in pancreas islets (at protein level) (PubMed:8681804). Detected in pancreas and brain (PubMed:8681804, PubMed:8637868). {ECO:0000269|PubMed:15220191, ECO:0000269|PubMed:19361477, ECO:0000269|PubMed:8637868, ECO:0000269|PubMed:8681804}. +P49446 PTPRE_MOUSE Receptor-type tyrosine-protein phosphatase epsilon (Protein-tyrosine phosphatase epsilon) (R-PTP-epsilon) (EC 3.1.3.48) 699 80,688 Active site (2); Alternative sequence (2); Binding site (2); Chain (1); Domain (2); Glycosylation (2); Modified residue (1); Region (1); Sequence conflict (8); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 46 68 Helical. {ECO:0000255}. TOPO_DOM 20 45 Extracellular. {ECO:0000255}.; TOPO_DOM 69 699 Cytoplasmic. {ECO:0000255}. FUNCTION: Isoform 1 acts as a negative regulator of insulin receptor (IR) signaling and is involved in insulin-induced glucose metabolism mainly through direct dephosphorylation and inactivation of IR in hepatocytes and liver (By similarity). Plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells. May play a role in osteoclast formation and function. {ECO:0000250, ECO:0000269|PubMed:19508371, ECO:0000269|PubMed:8610169}.; FUNCTION: Isoform 2 acts as a negative regulator of insulin receptor (IR) signaling in skeletal muscle. Regulates insulin-induced tyrosine phosphorylation of insulin receptor (IR) and insulin receptor substrate 1 (IRS-1), phosphorylation of protein kinase B and glycogen synthase kinase-3 and insulin induced stimulation of glucose uptake.; FUNCTION: Isoform 1 and isoform 2 act as a negative regulator of FceRI-mediated signal transduction leading to cytokine production and degranulation, most likely by acting at the level of SYK to affect downstream events such as phosphorylation of SLP76 and LAT and mobilization of Ca(2+). PTM: A catalytically active cytoplasmic form (p65) is produced by proteolytic cleavage of either isoform 1, isoform 2 or isoform 3. {ECO:0000269|PubMed:10980613}.; PTM: Isoform 1 and isoform 2 are phosphorylated on tyrosine residues by tyrosine kinase Neu. {ECO:0000250}.; PTM: Isoform 1 is glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Note=Predominantly cytoplasmic. A small fraction is also associated with nucleus and membrane. Insulin can induce translocation to the membrane.; SUBCELLULAR LOCATION: Isoform 3: Cytoplasm. SUBUNIT: Monomer (By similarity). Isoform 2: Homodimer. Can form oligomers. Dimerization is increased by oxidative stress and decreased by EGFR. Isoform 2 interacts with GRB2 (By similarity). {ECO:0000250}. DOMAIN: The tyrosine-protein phosphatase 2 domain (D2) mediates dimerization. The extreme N- and C- termini of the D2 domain act to inhibit dimerization and removal of these sequences increases dimerization and inhibits enzyme activity. {ECO:0000269|PubMed:12861030}. TISSUE SPECIFICITY: Isoform 2 is expressed in the spleen and thymus (at protein level). Detected in fibroblasts, myeloid cells, macrophages, and T-cells but not in B-cell lines. Isoform 1 and isoform 2 are expressed predominantly in the brain, testes, and lungs, with lower levels present in lymph nodes, thymus, spleen, heart and mammary glands. Isoform 1 is expressed in osteoclasts and not in osteoblasts and its expression is related to osteoclast differentiation. It is also expressed in the erythrocytes. Isoform 2 is strongly expressed in skeletal muscle and L6 skeletal muscle cell line. {ECO:0000269|PubMed:18006633, ECO:0000269|PubMed:18924107, ECO:0000269|PubMed:1932742, ECO:0000269|PubMed:8610169, ECO:0000269|PubMed:8618876}. +Q05909 PTPRG_MOUSE Receptor-type tyrosine-protein phosphatase gamma (Protein-tyrosine phosphatase gamma) (R-PTP-gamma) (EC 3.1.3.48) 1442 161,243 Active site (1); Beta strand (15); Binding site (2); Chain (1); Disulfide bond (1); Domain (4); Glycosylation (6); Helix (9); Modified residue (1); Region (1); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 734 759 Helical. {ECO:0000255}. TOPO_DOM 20 733 Extracellular. {ECO:0000255}.; TOPO_DOM 760 1442 Cytoplasmic. {ECO:0000255}. FUNCTION: Possesses tyrosine phosphatase activity. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Monomer; active form. Homodimer; inactive form (By similarity). Interacts with CNTN3, CNTN4, CNTN5 and CNTN6. {ECO:0000250, ECO:0000269|PubMed:20133774}. TISSUE SPECIFICITY: Detected in brain, lung, kidney, heart, liver, skeletal muscle, spleen and testes. It is developmentally regulated in the brain. +Q60673 PTPRN_MOUSE Receptor-type tyrosine-protein phosphatase-like N (R-PTP-N) (PTP IA-2) [Cleaved into: ICA512-N-terminal fragment (ICA512-NTF); ICA512-transmembrane fragment (ICA512-TMF); ICA512-cleaved cytosolic fragment (ICA512-CCF)] 979 106,083 Chain (4); Cross-link (1); Disulfide bond (3); Domain (1); Erroneous initiation (1); Glycosylation (2); Modified residue (2); Mutagenesis (2); Region (3); Sequence conflict (5); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 576 600 Helical. {ECO:0000255}. TOPO_DOM 38 575 Lumenal. {ECO:0000255}.; TOPO_DOM 601 979 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a role in vesicle-mediated secretory processes (PubMed:21732083). Required for normal accumulation of secretory vesicles in hippocampus, pituitary and pancreatic islets. Required for the accumulation of normal levels of insulin-containing vesicles and preventing their degradation (PubMed:15939893, PubMed:21732083). Plays a role in insulin secretion in response to glucose stimuli (PubMed:12031972, PubMed:21732083). Required for normal accumulation of the neurotransmitters norepinephrine, dopamine and serotonin in the brain (PubMed:16269463). In females, but not in males, required for normal accumulation and secretion of pituitary hormones, such as luteinizing hormone (LH) and follicle-stimulating hormone (FSH) (PubMed:16269463). Seems to lack intrinsic enzyme activity (PubMed:7980563, PubMed:8878556). Required to maintain normal levels of renin expression and renin release (PubMed:19019914). May regulate catalytic active protein-tyrosine phosphatases such as PTPRA through dimerization (PubMed:12364328). {ECO:0000250|UniProtKB:Q16849, ECO:0000269|PubMed:12031972, ECO:0000269|PubMed:12364328, ECO:0000269|PubMed:15939893, ECO:0000269|PubMed:19019914, ECO:0000269|PubMed:7980563, ECO:0000269|PubMed:8878556}.; FUNCTION: ICA512-transmembrane fragment: ICA512-TMF regulates dynamics and exocytosis of insulin secretory granules (SGs); binding of ICA512-TMF to SNTB2/beta-2-syntrophin is proposed to restrain SGs mobility and exocytosis by tethering them to the actin cytoskeleton depending on UTRN; the function is inhibited by cytoplasmic ICA512-CFF dimerizing with ICA512-TMF and displacing SNTB2 (By similarity). {ECO:0000250|UniProtKB:Q16849}.; FUNCTION: ICA512-cleaved cytosolic fragment: ICA512-CCF translocated to the nucleus promotes expression of insulin and other granule-related genes; the function implicates binding to and regulating activity of STAT5B probably by preventing its dephosphorylation and potentially by inducing its sumoylation by recruiting PIAS4 (By similarity). Enhances pancreatic beta-cell proliferation by converging with signaling by STAT5B and STAT3 (PubMed:18178618). ICA512-CCF located in the cytoplasm regulates dynamics and exocytosis of insulin secretory granules (SGs) by dimerizing with ICA512-TMF and displacing SNTB2 thus enhancing SGs mobility and exocytosis (By similarity). {ECO:0000250|UniProtKB:Q16849, ECO:0000269|PubMed:18178618}. PTM: Subject to proteolytic cleavage at multiple sites. Subject to cleavage on a pair of basic residues. On exocytosis of secretory granules in pancreatic beta-cells ICA512-TMF is transiently inserted in the plasma-membrane and cleaved by mu-type calpain CPN1 to yield ICA512-CCF. {ECO:0000250|UniProtKB:P56722, ECO:0000250|UniProtKB:Q16849, ECO:0000250|UniProtKB:Q63259}.; PTM: O-glycosylated. {ECO:0000250|UniProtKB:Q16849}.; PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q16849}.; PTM: Sumoylated at two sites including Lys-754. Sumoylation decreases interaction with STAT5. {ECO:0000250|UniProtKB:Q16849}. SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q63259}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q63259}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000269|PubMed:19361477}; Single-pass type I membrane protein {ECO:0000305}. Perikaryon {ECO:0000250|UniProtKB:Q63259}. Cell projection, axon {ECO:0000250|UniProtKB:Q63259}. Cell junction, synapse {ECO:0000250|UniProtKB:Q63259}. Cell membrane {ECO:0000250|UniProtKB:Q63259}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q63259}. Endosome {ECO:0000250|UniProtKB:Q63259}. Note=Detected on neuronal secretory vesicles, but not on synaptic vesicles. Colocalizes with insulin-containing secretory granules. Primarily detected on secretory vesicle membranes. Transiently found at the cell membrane, when secretory vesicles fuse with the cell membrane to release their cargo. Is then endocytosed and recycled to secretory vesicles via the Golgi apparatus membranes. {ECO:0000250|UniProtKB:Q63259}.; SUBCELLULAR LOCATION: ICA512-transmembrane fragment: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:Q63259}.; SUBCELLULAR LOCATION: ICA512-cleaved cytosolic fragment: Nucleus {ECO:0000250|UniProtKB:Q16849}. SUBUNIT: Homodimer; shown for the unprocessed protein (proICA512) in the endoplasmic reticulum and resolved during protein maturation as ICA512-TMF seems to be predominantly monomeric in secretory granules; however, ICA512-CCF interacts with ICA512-TMF disrupting the ICA512-TMF:SNTB2 complex. The isolated lumenal RESP18 homology domain has been shown to form disulfide-linked homooligomers. Interacts (via cytoplasmic domain) with phosphorylated SNTB2; this protects PTPRN against cleavage by CAPN1 to produce ICA512-CCF. Dephosphorylation of SNTB2 upon insulin stimulation disrupts the interaction and results in PTPRN cleavage. Interacts with SNX19. ICA512-CCF interacts with PIAS4; in the nucleus. Interacts with STAT5B (phosphorylated); down-regulated by ICA512-CCF sumoylation; ICA512-CCF prevents STAT5B dephosphorylation; ICA512-CCF mediates interaction of STAT5B with PIAS4. Interacts (via RESP18 homology domain) with insulin and proinsulin (By similarity). Interacts with PTPRN2, PTPRA and PTPRE (PubMed:12364328). {ECO:0000250|UniProtKB:Q16849, ECO:0000269|PubMed:12364328}. DOMAIN: The RESP18 homology domain is sufficient for targeting proICA512 to secretory granules. {ECO:0000250|UniProtKB:Q16849}. TISSUE SPECIFICITY: Detected in pituitary (PubMed:16269463). Detected in brain (at protein level) (PubMed:12031972, PubMed:16269463, PubMed:19361477). Detected in brain (PubMed:7980563, PubMed:12031972). Weakly expressed in the colon, intestine, stomach and pancreas (PubMed:7980563). {ECO:0000269|PubMed:12031972, ECO:0000269|PubMed:16269463, ECO:0000269|PubMed:19361477, ECO:0000269|PubMed:7980563}. +Q9ESF1 OTOF_MOUSE Otoferlin (Fer-1-like protein 2) 1997 227,033 Alternative sequence (3); Chain (1); Coiled coil (1); Compositional bias (3); Domain (4); Sequence conflict (3); Topological domain (2); Transmembrane (1) TRANSMEM 1964 1984 Helical. {ECO:0000255}. TOPO_DOM 1 1963 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1985 1997 Extracellular. {ECO:0000255}. FUNCTION: Key calcium ion sensor involved in the Ca(2+)-triggered synaptic vesicle-plasma membrane fusion and in the control of neurotransmitter release at these output synapses. Interacts in a calcium-dependent manner to the presynaptic SNARE proteins at ribbon synapses of cochlear inner hair cells (IHCs) to trigger exocytosis of neurotransmitter. Also essential to synaptic exocytosis in immature outer hair cells (OHCs). May also play a role within the recycling of endosomes. {ECO:0000269|PubMed:17055430, ECO:0000269|PubMed:18287496, ECO:0000269|PubMed:18772196}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Single-pass type II membrane protein. Basolateral cell membrane; Single-pass type II membrane protein. Endoplasmic reticulum membrane; Single-pass type II membrane protein. Cell membrane; Single-pass type II membrane protein. Note=Detected at basolateral cell membrane with synaptic vesicles surrounding the ribbon and at the presynaptic plasma membrane in the inner hair cells (IHCs) at postnatal day 30 (P30). Colocalizes with GPR25 and RAB8B in inner hair cells. SUBUNIT: Interacts with SNAP25; the interaction is direct. Interacts with STX1; the interaction is direct. Interacts with RAB8B. {ECO:0000269|PubMed:17055430, ECO:0000269|PubMed:18772196}. DOMAIN: The N-terminal first 124 residues can be classified as C2 domain, based on their 3D-structure. They are not sufficient for calcium ion or phospholipid binding (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Isoform 1 is expressed in cochlea and brain. Expressed in the cochlear and vestibular hair cells. Expressed in both inner and outer hair cells (IHCs and OHCs) and cochlear ganglions neurons at postnatal day 2 (P2) and 6 (P6). Expressed only in IHCs at postnatal day 60 (P60) (at protein level). Strongly expressed in brain and inner ear. In the inner ear, it is mainly expressed in the cochlear IHC and vestibular type I sensory hair cells. Weakly expressed in eye, heart, skeletal muscle, liver, kidney, lung and testis. {ECO:0000269|PubMed:10192385, ECO:0000269|PubMed:17055430, ECO:0000269|PubMed:17229086, ECO:0000269|PubMed:18772196}. +P0C5E4 PTPRQ_MOUSE Phosphatidylinositol phosphatase PTPRQ (EC 3.1.3.-) (Receptor-type tyrosine-protein phosphatase Q) (PTP-RQ) (R-PTP-Q) (EC 3.1.3.48) 2300 256,785 Active site (1); Chain (1); Domain (18); Glycosylation (16); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1907 1927 Helical. {ECO:0000255}. TOPO_DOM 18 1906 Extracellular. {ECO:0000255}.; TOPO_DOM 1928 2300 Cytoplasmic. {ECO:0000255}. FUNCTION: Phosphatidylinositol phosphatase required for auditory function. May act by regulating the level of phosphatidylinositol 4,5-bisphosphate (PIP2) level in the basal region of hair bundles. Can dephosphorylate a broad range of phosphatidylinositol phosphates, including phosphatidylinositol 3,4,5-trisphosphate and most phosphatidylinositol monophosphates and diphosphates. Phosphate can be hydrolyzed from the D3 and D5 positions in the inositol ring. Has low tyrosine-protein phosphatase activity; however, the relevance of such activity in vivo is unclear. Plays an important role in adipogenesis of mesenchymal stem cells (MSCs). Regulates the phosphorylation state of AKT1 by suppressing the phosphatidylinositol 3,4,5-trisphosphate (PIP3) level in MSCs and preadipocyte cells (By similarity). {ECO:0000250, ECO:0000269|PubMed:14534255}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. TISSUE SPECIFICITY: In the inner ear of the early postnatal mouse, it is present in hair bundles in the cochlea and in the vestibule. Restricted to the hair bundles and not detected in any other cell type within the inner ear. Restricted to the basal region of the hair bundle (at protein level). {ECO:0000269|PubMed:14534255}. +Q80SX5 OTOP2_MOUSE Proton channel OTOP2 (Otopetrin-2) 563 62,582 Chain (1); Sequence conflict (1); Transmembrane (12) TRANSMEM 30 50 Helical. {ECO:0000255}.; TRANSMEM 62 82 Helical. {ECO:0000255}.; TRANSMEM 100 120 Helical. {ECO:0000255}.; TRANSMEM 137 157 Helical. {ECO:0000255}.; TRANSMEM 173 193 Helical. {ECO:0000255}.; TRANSMEM 242 262 Helical. {ECO:0000255}.; TRANSMEM 290 310 Helical. {ECO:0000255}.; TRANSMEM 325 345 Helical. {ECO:0000255}.; TRANSMEM 373 393 Helical. {ECO:0000255}.; TRANSMEM 403 423 Helical. {ECO:0000255}.; TRANSMEM 496 516 Helical. {ECO:0000255}.; TRANSMEM 528 548 Helical. {ECO:0000255}. FUNCTION: Proton-selective channel that specifically transports protons into cells. Proton-selective channel activity is probably required in cell types that use changes in intracellular pH for cell signaling or to regulate biochemical or developmental processes. {ECO:0000269|PubMed:29371428}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q80VM9}; Multi-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Expressed at higher level in stomach, testis and olfactory bulb. {ECO:0000269|PubMed:29371428}. +Q8R448 OTOSP_MOUSE Otospiralin (Organ of Corti 10 kDa protein) 89 10,185 Chain (1); Signal peptide (1) FUNCTION: May be essential for the survival of the neurosensory epithelium of the inner ear. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Ear specific. +P80206 OTX2_MOUSE Homeobox protein OTX2 (Orthodenticle homolog 2) 289 31,622 Chain (1); DNA binding (1); Helix (4); Mutagenesis (1) FUNCTION: Transcription factor probably involved in the development of the brain and the sense organs. Can bind to the bicoid/BCD target sequence (BTS): 5'-TCTAATCCC-3'. {ECO:0000250|UniProtKB:P32243}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P32243}. TISSUE SPECIFICITY: Brain: restricted regions of the developing rostral brain including the presumptive cerebral cortex and olfactory bulbs; expressed in the developing olfactory, auricolar and ocular systems, including the covering of the optic nerve. +B9EKR1 PTPRZ_MOUSE Receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta) (EC 3.1.3.48) 2312 254,405 Active site (1); Binding site (2); Chain (1); Compositional bias (3); Disulfide bond (2); Domain (4); Glycosylation (9); Modified residue (7); Region (1); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 1638 1658 Helical. {ECO:0000255}. TOPO_DOM 25 1637 Extracellular. {ECO:0000255}.; TOPO_DOM 1659 2312 Cytoplasmic. {ECO:0000255}. FUNCTION: Protein tyrosine phosphatase that negatively regulates oligodendrocyte precursor proliferation in the embryonic spinal cord. Required for normal differentiation of the precursor cells into mature, fully myelinating oligodendrocytes. May play a role in protecting oligondendrocytes against apoptosis. May play a role in the establishment of contextual memory, probably via the dephosphorylation of proteins that are part of important signaling cascades. {ECO:0000269|PubMed:12355066, ECO:0000269|PubMed:16513268, ECO:0000269|PubMed:21969550}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21969550}; Single-pass type I membrane protein {ECO:0000269|PubMed:21969550}. Secreted {ECO:0000269|PubMed:21969550}. Note=A secreted form is apparently generated by shedding of the extracellular domain. SUBUNIT: The carbonic-anhydrase like domain interacts with CNTN1 (contactin) (PubMed:20133774, PubMed:21969550). Interaction with PTN promotes formation of homooligomers; oligomerization impairs phosphatase activity (By similarity). {ECO:0000250|UniProtKB:Q62656, ECO:0000269|PubMed:20133774, ECO:0000269|PubMed:21969550}. TISSUE SPECIFICITY: Detected in neurons and astrocytes in the central nervous system (CNS). Detected in the hippocampus and in brain cortex. {ECO:0000269|PubMed:11003666, ECO:0000269|PubMed:9655611}. +Q3UU35 OVOS_MOUSE Ovostatin homolog 1456 162,340 Chain (1); Glycosylation (3); Sequence conflict (2); Signal peptide (1) FUNCTION: Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Homotetramer. {ECO:0000250}. +Q9R1Z7 PTPS_MOUSE 6-pyruvoyl tetrahydrobiopterin synthase (PTP synthase) (PTPS) (EC 4.2.3.12) 144 16,188 Active site (3); Chain (1); Metal binding (3); Modified residue (3); Sequence conflict (1) Cofactor biosynthesis; tetrahydrobiopterin biosynthesis; tetrahydrobiopterin from 7,8-dihydroneopterin triphosphate: step 1/3. FUNCTION: Involved in the biosynthesis of tetrahydrobiopterin, an essential cofactor of aromatic amino acid hydroxylases. Catalyzes the transformation of 7,8-dihydroneopterin triphosphate into 6-pyruvoyl tetrahydropterin. PTM: Phosphorylation of Ser-18 is required for maximal enzyme activity. {ECO:0000250}. SUBUNIT: Homohexamer formed of two homotrimers in a head to head fashion. {ECO:0000250}. +Q7M761 OVCH2_MOUSE Ovochymase-2 (EC 3.4.21.-) (Oviductin) 609 67,611 Active site (3); Alternative sequence (1); Chain (1); Disulfide bond (8); Domain (3); Glycosylation (5); Metal binding (1); Propeptide (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +Q8CE23 OX26_MOUSE Orexigenic neuropeptide QRFP (P518) [Cleaved into: QRF-amide (Neuropeptide RF-amide) (Pyroglutamylated arginine-phenylalanine-amide peptide)] 124 13,485 Modified residue (1); Peptide (1); Propeptide (1); Signal peptide (1) FUNCTION: Stimulates feeding and grooming behavior, metabolic rate and locomotor activity and increases blood pressure. May have orexigenic activity. May promote aldosterone secretion by the adrenal gland. {ECO:0000269|PubMed:16648250}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Ligand for the G-protein coupled receptor QRFPR/GPR103. TISSUE SPECIFICITY: Expressed in the brain with highest levels in the periventricular hypothalamic nucleus and lateral hypothalamic areas. Expressed at moderate levels in the adrenal gland, eye, heart, intestine, liver, lung, kidney, mesenteric lymph node, ovary, placenta, Peyer patches, skin, spleen, stomach, testis, thymus and uterus. {ECO:0000269|PubMed:12714592, ECO:0000269|PubMed:16648250}. +B1AZ99 OTUD3_MOUSE OTU domain-containing protein 3 (EC 3.4.19.12) 396 44,576 Active site (3); Chain (1); Domain (2); Region (3) FUNCTION: Deubiquitinating enzyme that hydrolyzes 'Lys-6'- and 'Lys-11'-linked polyubiquitin. Also hydrolyzes heterotypic (mixed and branched) and homotypic chains (By similarity). {ECO:0000250}. DOMAIN: The UBA-like domain has no influence on ubiquitin hydrolysis. {ECO:0000250}.; DOMAIN: Specificity is given by the S1' ubiquitin-binding site within the OTU domain composed of the Cys-, His- and Variable-loops. {ECO:0000250}. +Q3U2S4 OTUD5_MOUSE OTU domain-containing protein 5 (EC 3.4.19.12) (Deubiquitinating enzyme A) (DUBA) 566 60,306 Active site (3); Alternative sequence (1); Chain (1); Compositional bias (2); Domain (1); Modified residue (6); Region (3); Sequence conflict (6) FUNCTION: Deubiquitinating enzyme that functions as negative regulator of the innate immune system. Acts via TRAF3 deubiquitination and subsequent suppression of type I interferon (IFN) production. Has peptidase activity towards 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. Can also cleave 'Lys-11'-linked ubiquitin chains (in vitro) (By similarity). {ECO:0000250}. PTM: Phosphorylation at Ser-177 is required for deubiquitinating activity. {ECO:0000250}. SUBUNIT: Interacts with TRAF3. {ECO:0000250}. +D3YYM0 OVOL3_MOUSE Putative transcription factor ovo-like protein 3 189 21,273 Chain (1); Zinc finger (3) FUNCTION: May act as a transcription regulator. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q9CR10 OXLD1_MOUSE Oxidoreductase-like domain-containing protein 1 201 22,178 Chain (1); Domain (1) +P97926 OXYR_MOUSE Oxytocin receptor (OT-R) 388 42,805 Chain (1); Compositional bias (2); Disulfide bond (1); Glycosylation (2); Modified residue (2); Sequence conflict (1); Topological domain (8); Transmembrane (7) TRANSMEM 39 63 Helical; Name=1. {ECO:0000255}.; TRANSMEM 75 97 Helical; Name=2. {ECO:0000255}.; TRANSMEM 114 135 Helical; Name=3. {ECO:0000255}.; TRANSMEM 155 175 Helical; Name=4. {ECO:0000255}.; TRANSMEM 203 225 Helical; Name=5. {ECO:0000255}.; TRANSMEM 275 293 Helical; Name=6. {ECO:0000255}.; TRANSMEM 309 331 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 38 Extracellular. {ECO:0000255}.; TOPO_DOM 64 74 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 98 113 Extracellular. {ECO:0000255}.; TOPO_DOM 136 154 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 176 202 Extracellular. {ECO:0000255}.; TOPO_DOM 226 274 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 294 308 Extracellular. {ECO:0000255}.; TOPO_DOM 332 388 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for oxytocin. The activity of this receptor is mediated by G proteins which activate a phosphatidylinositol-calcium second messenger system. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q99LH2 PTSS1_MOUSE Phosphatidylserine synthase 1 (PSS-1) (PtdSer synthase 1) (EC 2.7.8.29) (Serine-exchange enzyme I) 473 55,604 Chain (1); Initiator methionine (1); Modified residue (5); Sequence conflict (8); Topological domain (10); Transmembrane (9) TRANSMEM 36 56 Helical. {ECO:0000255}.; TRANSMEM 73 93 Helical. {ECO:0000255}.; TRANSMEM 103 123 Helical. {ECO:0000255}.; TRANSMEM 187 207 Helical. {ECO:0000255}.; TRANSMEM 217 237 Helical. {ECO:0000255}.; TRANSMEM 287 307 Helical. {ECO:0000255}.; TRANSMEM 320 342 Helical. {ECO:0000255}.; TRANSMEM 356 376 Helical. {ECO:0000255}.; TRANSMEM 384 404 Helical. {ECO:0000255}. TOPO_DOM 2 35 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 57 72 Lumenal. {ECO:0000255}.; TOPO_DOM 94 102 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 124 186 Lumenal. {ECO:0000255}.; TOPO_DOM 208 216 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 238 286 Lumenal. {ECO:0000255}.; TOPO_DOM 308 319 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 343 355 Lumenal. {ECO:0000255}.; TOPO_DOM 377 383 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 405 473 Lumenal. {ECO:0000255}. Phospholipid metabolism; phosphatidylserine biosynthesis. FUNCTION: Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine (PE) or phosphatidylcholine (PC) is replaced by L-serine. In membranes, PTDSS1 catalyzes mainly the conversion of phosphatidylcholine. Also converts, in vitro and to a lesser extent, phosphatidylethanolamine. {ECO:0000269|PubMed:10432300, ECO:0000269|PubMed:9516423}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10938271}; Multi-pass membrane protein {ECO:0000269|PubMed:10938271}. Note=Highly enriched in the mitochondria-associated membrane (MAM). TISSUE SPECIFICITY: Expressed in kidney, testis, lung, skeletal muscle, liver brain, heart and spleen with highest expression in testis, liver, heart and brain. {ECO:0000269|PubMed:10432300}. +A3KG59 P20D2_MOUSE Peptidase M20 domain-containing protein 2 (Aminoacylase-1-like protein 2) 431 46,482 Alternative sequence (2); Chain (1); Sequence conflict (1) +Q9Z1X2 PTSS2_MOUSE Phosphatidylserine synthase 2 (PSS-2) (PtdSer synthase 2) (EC 2.7.8.29) (Serine-exchange enzyme II) 473 55,021 Alternative sequence (2); Chain (1); Glycosylation (1); Modified residue (3); Sequence conflict (3); Topological domain (8); Transmembrane (7) TRANSMEM 41 61 Helical. {ECO:0000255}.; TRANSMEM 75 95 Helical. {ECO:0000255}.; TRANSMEM 105 125 Helical. {ECO:0000255}.; TRANSMEM 292 312 Helical. {ECO:0000255}.; TRANSMEM 314 334 Helical. {ECO:0000255}.; TRANSMEM 355 375 Helical. {ECO:0000255}.; TRANSMEM 382 402 Helical. {ECO:0000255}. TOPO_DOM 1 40 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 62 74 Lumenal. {ECO:0000255}.; TOPO_DOM 96 104 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 126 291 Lumenal. {ECO:0000255}.; TOPO_DOM 313 313 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 335 354 Lumenal. {ECO:0000255}.; TOPO_DOM 376 381 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 403 473 Lumenal. {ECO:0000255}. Phospholipid metabolism; phosphatidylserine biosynthesis. FUNCTION: Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine (PE) or phosphatidylcholine (PC) is replaced by L-serine. PTDSS2 is specific for phosphatatidylethanolamine and does not act on phosphatidylcholine. {ECO:0000269|PubMed:10432300}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10938271}; Multi-pass membrane protein {ECO:0000269|PubMed:10938271}. Note=Highly enriched in the mitochondria-associated membrane (MAM). TISSUE SPECIFICITY: Highly expressed in testis. Detected at lower levels in kidney and heart. {ECO:0000269|PubMed:10432300, ECO:0000269|PubMed:12361952}. +Q9CQJ7 PTTG1_MOUSE Securin (Pituitary tumor-transforming gene 1 protein) 199 21,725 Alternative sequence (2); Chain (1); Initiator methionine (1); Modified residue (2); Motif (4); Mutagenesis (1); Sequence conflict (7) FUNCTION: Regulatory protein, which plays a central role in chromosome stability, in the p53/TP53 pathway, and DNA repair. Probably acts by blocking the action of key proteins. During the mitosis, it blocks Separase/ESPL1 function, preventing the proteolysis of the cohesin complex and the subsequent segregation of the chromosomes. At the onset of anaphase, it is ubiquitinated, conducting to its destruction and to the liberation of ESPL1. Its function is however not limited to a blocking activity, since it is required to activate ESPL1. Negatively regulates the transcriptional activity and related apoptosis activity of p53/TP53. The negative regulation of p53/TP53 may explain the strong transforming capability of the protein when it is overexpressed. May also play a role in DNA repair via its interaction with Ku, possibly by connecting DNA damage-response pathways with sister chromatid separation (By similarity). {ECO:0000250}. PTM: Phosphorylated at Ser-162 by CDC2 during mitosis. {ECO:0000250}.; PTM: Phosphorylated in vitro by ds-DNA kinase. {ECO:0000250}.; PTM: Ubiquitinated through 'Lys-11' linkage of ubiquitin moieties by the anaphase promoting complex (APC) at the onset of anaphase, conducting to its degradation. 'Lys-11'-linked ubiquitination is mediated by the E2 ligase UBE2C/UBCH10 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Interacts with RPS10 and DNAJA1. Interacts with the caspase-like ESPL1, and prevents its protease activity probably by covering its active site. Interacts with p53/TP53 and blocks its activity probably by blocking its binding to DNA. Interacts with the Ku 70 kDa subunit of ds-DNA kinase. Interacts with PTTG1IP (By similarity). {ECO:0000250}. DOMAIN: The N-terminal destruction box (D-box) acts as a recognition signal for degradation via the ubiquitin-proteasome pathway. {ECO:0000250}.; DOMAIN: The TEK-boxes are required for 'Lys-11'-linked ubiquitination and facilitate the transfer of the first ubiquitin and ubiquitin chain nucleation. TEK-boxes may direct a catalytically competent orientation of the UBE2C/UBCH10-ubiquitin thioester with the acceptor lysine residue (By similarity). {ECO:0000250}. +Q9Z176 P2R3D_MOUSE Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit delta (PP2A B''-PR59) (PP2A PR59) (Protein phosphatase 2A, 59 kDa regulatory subunit B) (Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit alpha) 491 55,706 Calcium binding (1); Chain (1); Compositional bias (1); Domain (1) FUNCTION: The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment. Interacts with retinoblastoma-related protein p107 (in vivo). May target PP2A core dimer to p107 resulting in dephosphorylation of p107. SUBUNIT: PP2A consists of a common heterodimeric core enzyme, composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant regulatory subunit (PR65 or subunit A), that associates with a variety of regulatory subunits. Proteins that associate with the core dimer include three families of regulatory subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa variable regulatory subunit, viral proteins, and cell signaling molecules. TISSUE SPECIFICITY: Expressed in testis, kidney, liver, lung, spleen, brain and heart. +Q8K3P1 P2RX2_MOUSE P2X purinoceptor 2 (P2X2) (ATP receptor) (Purinergic receptor) 485 53,937 Alternative sequence (4); Chain (1); Disulfide bond (6); Glycosylation (3); Region (1); Sequence conflict (1); Topological domain (3); Transmembrane (2) TRANSMEM 44 64 Helical; Name=1. {ECO:0000255}.; TRANSMEM 340 360 Helical; Name=2. {ECO:0000255}. TOPO_DOM 1 43 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 65 339 Extracellular. {ECO:0000255}.; TOPO_DOM 361 485 Cytoplasmic. {ECO:0000255}. FUNCTION: Ion channel gated by extracellular ATP involved in a variety of cellular responses, such as excitatory postsynaptic responses in sensory neurons, neuromuscular junctions (NMJ) formation, hearing, perception of taste and peristalsis. In the inner ear, regulates sound transduction and auditory neurotransmission, outer hair cell electromotility, inner ear gap junctions, and K(+) recycling. Mediates synaptic transmission between neurons and from neurons to smooth muscle. {ECO:0000269|PubMed:12917379, ECO:0000269|PubMed:12937291, ECO:0000269|PubMed:15961431, ECO:0000269|PubMed:16322458, ECO:0000269|PubMed:17706883, ECO:0000269|PubMed:23345450}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17706883}; Multi-pass membrane protein {ECO:0000269|PubMed:17706883}. SUBUNIT: Homotrimer and heterotrimer; functional P2XRs are organized as homomeric and heteromeric trimers. {ECO:0000250}. +Q61194 P3C2A_MOUSE Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha (PI3K-C2-alpha) (PtdIns-3-kinase C2 subunit alpha) (EC 2.7.1.154) (Cpk-m) (Phosphoinositide 3-kinase-C2-alpha) (p170) 1686 190,758 Alternative sequence (1); Beta strand (9); Chain (1); Domain (6); Erroneous initiation (1); Helix (2); Initiator methionine (1); Modified residue (8); Motif (1); Region (2); Sequence conflict (7) FUNCTION: Generates phosphatidylinositol 3-phosphate (PtdIns3P) and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) that act as second messengers. Has a role in several intracellular trafficking events. Functions in insulin signaling and secretion. Required for translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane and glucose uptake in response to insulin-mediated RHOQ activation. Regulates insulin secretion through two different mechanisms: involved in glucose-induced insulin secretion downstream of insulin receptor in a pathway that involves AKT1 activation and TBC1D4/AS160 phosphorylation, and participates in the late step of insulin granule exocytosis probably in insulin granule fusion. Synthesizes PtdIns3P in response to insulin signaling. Functions in clathrin-coated endocytic vesicle formation and distribution. Regulates dynamin-independent endocytosis, probably by recruiting EEA1 to internalizing vesicles. In neurosecretory cells synthesizes PtdIns3P on large dense core vesicles. Participates in calcium induced contraction of vascular smooth muscle by regulating myosin light chain (MLC) phosphorylation through a mechanism involving Rho kinase-dependent phosphorylation of the MLCP-regulatory subunit MYPT1. May play a role in the EGF signaling cascade. May be involved in mitosis and UV-induced damage response. Required for maintenance of normal renal structure and function by supporting normal podocyte function. {ECO:0000269|PubMed:20061534, ECO:0000269|PubMed:20974805, ECO:0000269|PubMed:8663140}. PTM: Phosphorylated on Ser-261 during mitosis and upon UV irradiation; which does not change enzymatic activity but leads to proteasomal degradation (By similarity). Phosphorylated upon insulin stimulation; which may lead to enzyme activation. {ECO:0000250, ECO:0000269|PubMed:10329640}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O00443}. Golgi apparatus {ECO:0000250|UniProtKB:O00443}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:O00443}. Nucleus {ECO:0000250|UniProtKB:O00443}. Cytoplasm {ECO:0000250|UniProtKB:O00443}. Note=Inserts preferentially into membranes containing PtdIns(4,5)P2. Associated with RNA-containing structures. {ECO:0000250|UniProtKB:O00443}. SUBUNIT: Interacts with ERBB2 and EGFR (By similarity). Interacts with clathrin trimers (By similarity). Interacts with SBF2/MTMR13 (PubMed:22648168). {ECO:0000250|UniProtKB:O00443, ECO:0000269|PubMed:22648168}. TISSUE SPECIFICITY: Expressed in brain (at protein level) (PubMed:22648168). Detected in podocytes (PubMed:20974805). {ECO:0000269|PubMed:20974805, ECO:0000269|PubMed:22648168}. +Q9DBN4 P33MX_MOUSE Putative monooxygenase p33MONOX (EC 1.-.-.-) 303 32,715 Alternative sequence (4); Chain (1); Erroneous initiation (1); Frameshift (1); Modified residue (3); Motif (1); Sequence conflict (4) FUNCTION: Potential NADPH-dependent oxidoreductase. May be involved in the regulation of neuronal survival, differentiation and axonal outgrowth (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21153684}. SUBUNIT: Interacts with NELFB, NOL12 and PRNP. {ECO:0000250|UniProtKB:Q96A73}. TISSUE SPECIFICITY: Expressed in neuronal pyramidal cells of the hippocampus and in the neurons of the cortex. {ECO:0000269|PubMed:21153684}. +Q9JJS7 P2RY4_MOUSE P2Y purinoceptor 4 (P2Y4) 361 41,034 Chain (1); Disulfide bond (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 31 58 Helical; Name=1. {ECO:0000255}.; TRANSMEM 69 91 Helical; Name=2. {ECO:0000255}.; TRANSMEM 109 127 Helical; Name=3. {ECO:0000255}.; TRANSMEM 150 170 Helical; Name=4. {ECO:0000255}.; TRANSMEM 193 218 Helical; Name=5. {ECO:0000255}.; TRANSMEM 243 265 Helical; Name=6. {ECO:0000255}.; TRANSMEM 284 305 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 30 Extracellular. {ECO:0000255}.; TOPO_DOM 59 68 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 92 108 Extracellular. {ECO:0000255}.; TOPO_DOM 128 149 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 171 192 Extracellular. {ECO:0000255}.; TOPO_DOM 219 242 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 266 283 Extracellular. {ECO:0000255}.; TOPO_DOM 306 361 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for ATP and UTP coupled to G-proteins that activate a phosphatidylinositol-calcium second messenger system. PTM: Phosphorylation of Ser-329 and Ser-330 is a key step in agonist-dependent desensitization and loss of surface P2RY4. This phosphorylation does not involve PKC, nor other calcium-activated kinases (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed in the liver, intestine, stomach, bladder and lung. +Q7TMJ8 P3IP1_MOUSE Phosphoinositide-3-kinase-interacting protein 1 (Calcineurin-regulated kringle domain-containing protein) (Kringle domain-containing protein HGFL) 264 28,567 Alternative sequence (2); Chain (1); Disulfide bond (3); Domain (1); Erroneous gene model prediction (3); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 171 191 Helical. {ECO:0000255}. TOPO_DOM 22 170 Extracellular. {ECO:0000255}.; TOPO_DOM 192 264 Cytoplasmic. {ECO:0000255}. FUNCTION: Negative regulator of hepatic phosphatidylinositol 3-kinase (PI3K) activity. {ECO:0000269|PubMed:18632611}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. +P21129 P3_MOUSE P3 protein (Solute carrier family 10 member 3) 473 50,255 Chain (1); Transmembrane (9) TRANSMEM 25 45 Helical. {ECO:0000255}.; TRANSMEM 221 241 Helical. {ECO:0000255}.; TRANSMEM 249 269 Helical. {ECO:0000255}.; TRANSMEM 277 297 Helical. {ECO:0000255}.; TRANSMEM 316 336 Helical. {ECO:0000255}.; TRANSMEM 356 376 Helical. {ECO:0000255}.; TRANSMEM 381 401 Helical. {ECO:0000255}.; TRANSMEM 413 433 Helical. {ECO:0000255}.; TRANSMEM 446 466 Helical. {ECO:0000255}. FUNCTION: The ubiquitous expression and the conservation of the sequence in distant animal species suggest that the gene codes for a protein with housekeeping functions. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q2TBE6 P4K2A_MOUSE Phosphatidylinositol 4-kinase type 2-alpha (EC 2.7.1.67) (Phosphatidylinositol 4-kinase type II-alpha) 479 54,258 Binding site (2); Chain (1); Compositional bias (1); Domain (1); Lipidation (4); Modified residue (7); Nucleotide binding (2); Region (4) FUNCTION: Membrane-bound phosphatidylinositol-4 kinase (PI4-kinase) that catalyzes the phosphorylation of phosphatidylinositol (PI) to phosphatidylinositol 4-phosphate (PI4P), a lipid that plays important roles in endocytosis, Golgi function, protein sorting and membrane trafficking and is required for prolonged survival of neurons. Besides, phosphorylation of phosphatidylinositol (PI) to phosphatidylinositol 4-phosphate (PI4P) is the first committed step in the generation of phosphatidylinositol 4,5-bisphosphate (PIP2), a precursor of the second messenger inositol 1,4,5-trisphosphate (InsP3). {ECO:0000269|PubMed:19581584, ECO:0000305}. PTM: Palmitoylated by ZDHHC3 and ZDHHC7 in the CCPCC motif. Palmitoylation is cholesterol-dependent, and required for TGN localization (By similarity). {ECO:0000250|UniProtKB:Q9BTU6}.; PTM: Ubiquitinated by ITCH; this does not lead to proteasomal degradation. {ECO:0000269|PubMed:23146885}. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q9BTU6}; Lipid-anchor {ECO:0000250|UniProtKB:Q9BTU6}. Membrane raft {ECO:0000250|UniProtKB:Q9BTU6}. Endosome {ECO:0000250|UniProtKB:Q99M64}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q99M64}. Cell projection, dendrite {ECO:0000269|PubMed:21998198}. Cell junction, synapse, presynaptic cell membrane {ECO:0000269|PubMed:21998198}. Cell junction, synapse, synaptosome {ECO:0000269|PubMed:21998198}. Mitochondrion {ECO:0000269|PubMed:21998198}. Membrane {ECO:0000269|PubMed:19581584}. Cell membrane {ECO:0000250|UniProtKB:Q9BTU6}. Note=Found in subdomains of the plasma membrane termed non-caveolar membrane rafts. Enriched in neurite tips and neuron projections in a BLOC-1- and AP-3-complexes-dependent manner (PubMed:21998198). Localized in neuronal cell body. Transported from neuronal cell body to neuron projections in a BLOC-1- and AP-3-complexes-dependent manner (PubMed:21998198). {ECO:0000269|PubMed:21998198}. SUBUNIT: Associates with the BLOC-1 and the AP-3 complexes; the BLOC-1 complex is required for optimal binding of PI4K2A to the AP-3 complex (PubMed:21998198). Interacts with BLOC1S5 and DTNBP1 (By similarity). Interacts with ITCH (PubMed:23146885). Interacts with FOS; this interaction may enhance phosphatidylinositol phosphorylation activity (PubMed:22105363). {ECO:0000250, ECO:0000269|PubMed:21998198, ECO:0000269|PubMed:22105363, ECO:0000269|PubMed:23146885}. TISSUE SPECIFICITY: Detected in brain (at protein level). {ECO:0000269|PubMed:19581584}. +Q8CBQ5 P4K2B_MOUSE Phosphatidylinositol 4-kinase type 2-beta (EC 2.7.1.67) (Phosphatidylinositol 4-kinase type II-beta) 469 53,478 Alternative sequence (1); Binding site (2); Chain (1); Domain (1); Modified residue (1); Nucleotide binding (2); Region (4); Sequence conflict (8) FUNCTION: Together with PI4K2A and the type III PI4Ks (PIK4CA and PIK4CB) it contributes to the overall PI4-kinase activity of the cell. This contribution may be especially significant in plasma membrane, endosomal and Golgi compartments. The phosphorylation of phosphatidylinositol (PI) to PI4P is the first committed step in the generation of phosphatidylinositol 4,5-bisphosphate (PIP2), a precursor of the second messenger inositol 1,4,5-trisphosphate (InsP3). Contributes to the production of InsP3 in stimulated cells and is likely to be involved in the regulation of vesicular trafficking (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}. Note=Mostly cytoplasmic but also found associated with the plasma membrane, the Golgi and endosomes. Compared to PI4K2A, a larger fraction of PI4K2B is cytosolic due to a smaller extent of palmitoylation. Translocates to membranes where it is recruited by PDGF stimulation by a Rac-GTP-dependent mechanism (By similarity). {ECO:0000250}. +Q60716 P4HA2_MOUSE Prolyl 4-hydroxylase subunit alpha-2 (4-PH alpha-2) (EC 1.14.11.2) (Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-2) 537 61,002 Alternative sequence (1); Binding site (1); Chain (1); Domain (1); Glycosylation (2); Metal binding (3); Modified residue (1); Repeat (1); Signal peptide (1) FUNCTION: Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. SUBUNIT: Heterotetramer of two alpha-2 chains and two beta chains (the beta chain is the multi-functional PDI). TISSUE SPECIFICITY: Expressed in a variety of tissues. +Q80U78 PUM1_MOUSE Pumilio homolog 1 1189 126,619 Alternative sequence (4); Chain (1); Compositional bias (3); Domain (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (18); Region (9); Repeat (8); Sequence conflict (4) FUNCTION: Sequence-specific RNA-binding protein that acts as a post-transcriptional repressor by binding the 3'-UTR of mRNA targets. Binds to an RNA consensus sequence, the Pumilio Response Element (PRE), 5'-UGUANAUA-3', that is related to the Nanos Response Element (NRE). Mediates post-transcriptional repression of transcripts via different mechanisms: acts via direct recruitment of the CCR4-POP2-NOT deadenylase leading to translational inhibition and mRNA degradation. Also mediates deadenylation-independent repression by promoting accessibility of miRNAs. Following growth factor stimulation, phosphorylated and binds to the 3'-UTR of CDKN1B/p27 mRNA, inducing a local conformational change that exposes miRNA-binding sites, promoting association of miR-221 and miR-222, efficient suppression of CDKN1B/p27 expression, and rapid entry to the cell cycle (By similarity). Acts as a post-transcriptional repressor of E2F3 mRNAs by binding to its 3'-UTR and facilitating miRNA regulation (By similarity). Represses a program of genes necessary to maintain genomic stability such as key mitotic, DNA repair and DNA replication factors. Its ability to repress those target mRNAs is regulated by the lncRNA NORAD (non-coding RNA activated by DNA damage) which, due to its high abundance and multitude of PUMILIO binding sites, is able to sequester a significant fraction of PUM1 and PUM2 in the cytoplasm (By similarity). Involved in neuronal functions by regulating ATXN1 mRNA levels: acts by binding to the 3'-UTR of ATXN1 transcripts, leading to their down-regulation independently of the miRNA machinery (PubMed:25768905). In testis, acts as a post-transcriptional regulator of spermatogenesis by binding to the 3'-UTR of mRNAs coding for regulators of p53/TP53 (PubMed:22342750). Involved in embryonic stem cell renewal by facilitating the exit from the ground state: acts by targeting mRNAs coding for naive pluripotency transcription factors and accelerates their down-regulation at the onset of differentiation (PubMed:24412312). Binds specifically to miRNA MIR199A precursor, with PUM2, regulates miRNA MIR199A expression at a postranscriptional level (By similarity). {ECO:0000250|UniProtKB:Q14671, ECO:0000269|PubMed:22342750, ECO:0000269|PubMed:24412312, ECO:0000269|PubMed:25768905}. PTM: Phosphorylation at Ser-715 promotes RNA-binding activity. Following growth factor stimulation phosphorylated at Ser-715, promoting binding to the 3'-UTR of CDKN1B/p27 mRNA. {ECO:0000250|UniProtKB:Q14671}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22342750}. Cytoplasm, P-body {ECO:0000250|UniProtKB:Q14671}. Cytoplasmic granule {ECO:0000250|UniProtKB:Q14671}. SUBUNIT: Recruits the CCR4-POP2-NOT deadenylase leading to translational inhibition and mRNA degradation (By similarity). Interacts with TRIM71 (via NHL repeats) in an RNA-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q14671}. DOMAIN: The pumilio repeats mediate the association with RNA by packing together to form a right-handed superhelix that approximates a half donut. RNA-binding occurs on the concave side of the surface. PUM1 is composed of 8 pumilio repeats of 36 residues; each repeat binds a single nucleotide in its RNA target. Residues at positions 12 and 16 of the pumilio repeat bind each RNA base via hydrogen bonding or van der Waals contacts with the Watson-Crick edge, while the amino acid at position 13 makes a stacking interaction. The recognition of RNA by pumilio repeats is base specific: cysteine and glutamine at position 12 and 16, respectively, bind adenine; asparagine and glutamine bind uracil; and serine and glutamate bind guanine. {ECO:0000250|UniProtKB:Q14671}. TISSUE SPECIFICITY: Widely expressed. Expressed in brain, heart, kidney, liver, lung, skin, intestine, spleen, testis and thymus. Weakly or not expressed in muscles and stomach. Expressed at various stages of myeloid and lymphoid cell development (PubMed:12667987). Highly expressed in testis (PubMed:22342750). Expressed in all major brain regions (at protein level) (PubMed:25768905). {ECO:0000269|PubMed:12667987, ECO:0000269|PubMed:22342750, ECO:0000269|PubMed:25768905}. +Q64143 P55G_MOUSE Phosphatidylinositol 3-kinase regulatory subunit gamma (PI3-kinase regulatory subunit gamma) (PI3K regulatory subunit gamma) (PtdIns-3-kinase regulatory subunit gamma) (Phosphatidylinositol 3-kinase 55 kDa regulatory subunit gamma) (PI3-kinase subunit p55-gamma) (PtdIns-3-kinase regulatory subunit p55-gamma) (p55PIK) 461 54,474 Chain (1); Domain (2); Modified residue (1) FUNCTION: Binds to activated (phosphorylated) protein-tyrosine kinases through its SH2 domain and regulates their kinase activity. During insulin stimulation, it also binds to IRS-1. SUBUNIT: Heterodimer of a regulatory subunit PIK3R3 and a p110 catalytic subunit (PIK3CA, PIK3CB or PIK3CD). Interacts with AXL (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highest levels in brain and testis. Lower levels in adipose tissue, kidney, heart, lung and skeletal muscle. Barely detectable in liver and spleen. +Q8CHY6 P66A_MOUSE Transcriptional repressor p66 alpha (GATA zinc finger domain-containing protein 2A) 629 67,334 Chain (1); Coiled coil (1); Compositional bias (1); Cross-link (9); Erroneous initiation (3); Modified residue (22); Region (2); Sequence conflict (1); Zinc finger (1) FUNCTION: Transcriptional repressor (By similarity). Enhances MBD2-mediated repression. Efficient repression requires the presence of GATAD2B (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}. Note=Speckled nuclear localization requires both CR1 and CR2 regions. {ECO:0000250}. SUBUNIT: Binds MBD2 and MBD3. Interaction with MBD2 is required for the enhancement of MBD2-mediated repression and for targeting to the chromatin (By similarity). Component of the MeCP1 histone deacetylase complex (By similarity). Interacts with histone tails, including that of histones H2A, H2B, H3 and H4. This interaction is reduced by histone acetylation (By similarity). {ECO:0000250}. +Q922W5 P5CR1_MOUSE Pyrroline-5-carboxylate reductase 1, mitochondrial (P5C reductase 1) (P5CR 1) (EC 1.5.1.2) 309 32,373 Binding site (2); Chain (1); Initiator methionine (1); Modified residue (3); Nucleotide binding (3) Amino-acid biosynthesis; L-proline biosynthesis; L-proline from L-glutamate 5-semialdehyde: step 1/1. FUNCTION: Housekeeping enzyme that catalyzes the last step in proline biosynthesis. Can utilize both NAD and NADP, but has higher affinity for NAD. Involved in the cellular response to oxidative stress. {ECO:0000250|UniProtKB:P32322}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P32322}. SUBUNIT: Homodecamer; composed of 5 homodimers. Interacts with LTO1. {ECO:0000250|UniProtKB:P32322}. TISSUE SPECIFICITY: Highly expressed in osteoblasts and skin. {ECO:0000269|PubMed:19648921}. +Q922Q4 P5CR2_MOUSE Pyrroline-5-carboxylate reductase 2 (P5C reductase 2) (P5CR 2) (EC 1.5.1.2) 320 33,659 Binding site (2); Chain (1); Initiator methionine (1); Modified residue (2); Nucleotide binding (3) Amino-acid biosynthesis; L-proline biosynthesis; L-proline from L-glutamate 5-semialdehyde: step 1/1. FUNCTION: Housekeeping enzyme that catalyzes the last step in proline biosynthesis. In some cell types, such as erythrocytes, its primary function may be the generation of NADP(+). Can utilize both NAD and NADP. Has higher affinity for NADP, but higher catalytic efficiency with NADH (By similarity). Involved in cellular response to oxidative stress (By similarity). {ECO:0000250|UniProtKB:Q96C36}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96C36}. Mitochondrion {ECO:0000250|UniProtKB:Q96C36}. SUBUNIT: Homodecamer; composed of 5 homodimers. Interacts with LTO1. {ECO:0000250|UniProtKB:Q96C36}. +O08908 P85B_MOUSE Phosphatidylinositol 3-kinase regulatory subunit beta (PI3-kinase regulatory subunit beta) (PI3K regulatory subunit beta) (PtdIns-3-kinase regulatory subunit beta) (Phosphatidylinositol 3-kinase 85 kDa regulatory subunit beta) (PI3-kinase subunit p85-beta) (PtdIns-3-kinase regulatory subunit p85-beta) 722 81,266 Beta strand (5); Chain (1); Domain (4); Helix (7); Modified residue (3); Sequence conflict (2); Turn (4) FUNCTION: Regulatory subunit of phosphoinositide-3-kinase (PI3K), a kinase that phosphorylates PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Binds to activated (phosphorylated) protein-tyrosine kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane. Indirectly regulates autophagy (By similarity). Promotes nuclear translocation of XBP1 isoform 2 in a ER stress- and/or insulin-dependent manner during metabolic overloading in the liver and hence plays a role in glucose tolerance improvement (PubMed:20348926). {ECO:0000250|UniProtKB:O00459, ECO:0000269|PubMed:20348926}. PTM: Phosphorylated in response to signaling from activated receptor-type protein kinases. Dephosphorylated by PTPRJ. Dephosphorylated at Tyr-649 by PTPN13. Phosphorylation of Tyr-649 impairs while its dephosphorylation promotes interaction with FBXL2 and SCF(FBXL2)-mediated polyubiquitination. {ECO:0000250|UniProtKB:O00459}.; PTM: Ubiquitinated. Polyubiquitination by the SCF(FBXL2) complex probably promotes proteasomal degradation of PIK3R2. {ECO:0000250|UniProtKB:O00459}. SUBUNIT: Heterodimer of a regulatory subunit PIK3R2 and a p110 catalytic subunit (PIK3CA, PIK3CB or PIK3CD). Interacts with AXL. Interacts with FLT1 (tyrosine-phosphorylated) and FLT4 (tyrosine-phosphorylated) (By similarity). Interacts with FBXL2; PIK3R2 is a substrate of the SCF(FBXL2) complex. Interacts with PTPN13; dephosphorylates PIK3R2 (By similarity). Interacts with NYAP1, NYAP2 and MYO16 (PubMed:21946561). Interacts with XBP1 isoform 2; the interaction is direct and induces translocation of XBP1 isoform 2 into the nucleus in a ER stress- and/or insulin-dependent but PI3K-independent manner (PubMed:20348926). Interacts with PIK3R1; the interaction is dissociated in an insulin-dependent manner (PubMed:20348926). {ECO:0000250|UniProtKB:O00459, ECO:0000269|PubMed:20348926, ECO:0000269|PubMed:21946561}. DOMAIN: The SH2 2 domain is required for interaction with FBXL2 and PTPN13. {ECO:0000250|UniProtKB:O00459}. +Q02819 NUCB1_MOUSE Nucleobindin-1 (CALNUC) 459 53,409 Calcium binding (2); Chain (1); Coiled coil (2); DNA binding (1); Domain (2); Modified residue (4); Region (1); Sequence conflict (4); Signal peptide (1) FUNCTION: Major calcium-binding protein of the Golgi. May have a role in calcium homeostasis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane {ECO:0000250|UniProtKB:Q63083}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q63083}; Lumenal side {ECO:0000250|UniProtKB:Q63083}. Cytoplasm {ECO:0000250|UniProtKB:Q63083}. Secreted {ECO:0000250|UniProtKB:Q63083}. Note=A small fraction of the protein may be cytoplasmic. In bone at least part of it is found in the extracellular matrix and in the culture medium of calvaria explants (By similarity). In lupus prone, but not in normal mice, at least part of it is in the serum where it induces the formation of autoantibodies including anti-DNA antibodies. {ECO:0000250|UniProtKB:Q63083, ECO:0000305}. SUBUNIT: Interacts with GNAI2 and GNAI3. {ECO:0000250}. DOMAIN: The EF-hand domains are unfolded in the absence of Ca(2+) and fold upon Ca(2+) addition. {ECO:0000250}. TISSUE SPECIFICITY: Lymphoid cells as well as other somatic cells, such as liver and kidney cells. +Q8R3U1 PA216_MOUSE HRAS-like suppressor 3 (HRSL3) (EC 3.1.1.32) (EC 3.1.1.4) (Adipose-specific phospholipase A2) (AdPLA) (Group XVI phospholipase A2) (H-rev 107 protein homolog) 162 17,872 Active site (3); Alternative sequence (1); Chain (1); Mutagenesis (4); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 133 155 Helical. {ECO:0000255}. TOPO_DOM 1 132 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 156 162 Lumenal. {ECO:0000255}. FUNCTION: Lipid-modifying enzyme that acts as major regulator of adipocyte lipolysis by catalyzing the release of fatty acids from phospholipids in adipose tissue (PubMed:18614531, PubMed:19047760, PubMed:19136964). Shows phospholipase A1 and A2 activity, catalyzing the calcium-independent hydrolysis of acyl groups in various phosphatidylcholines (PC) and phosphatidylethanolamine (PE) (PubMed:18614531, PubMed:19047760, PubMed:22134920). For most substrates, phospholipase A1 activity is much higher than phospholipase A2 activity (PubMed:18614531, PubMed:19047760). Phospholipase activity causes decreased intracellular levels of ether-type lipids, affecting peroxisome metabolism (PubMed:22134920). May also have acyltransferase activity: catalyzes both N-acylation of phosphatidylethanolamine to form N-acyl-phosphatidylethanolamine and O-acylation of lyso-phosphatidylcholines to form phosphatidylcholines (By similarity). The relevance of acyltransferase activity in vivo is however unclear and would require additional evidences (By similarity). Also has weak lysophospholipase activity (PubMed:18614531). {ECO:0000250|UniProtKB:P53816, ECO:0000269|PubMed:18614531, ECO:0000269|PubMed:19047760, ECO:0000269|PubMed:19136964, ECO:0000269|PubMed:22134920}.; FUNCTION: (Microbial infection) Acts as a host factor for picornaviruses: required during early infection to promote viral genome release into the cytoplasm (PubMed:28077878). {ECO:0000269|PubMed:28077878}. SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P53816}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:18614531}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:18614531}. Peroxisome membrane {ECO:0000269|PubMed:22134920}. SUBUNIT: Interacts with PPP2R1A; this interaction might decrease PP2A activity. {ECO:0000250|UniProtKB:P53816}. TISSUE SPECIFICITY: Ubiquitously expressed in normal tissues but down-regulated in primary carcinomas or in many cell lines derived from tumors (PubMed:12055182). Highly expressed in white adipose tissue and in adipocytes (PubMed:18614531, PubMed:19136964). Expressed at lower levels in brown adipose tissue (PubMed:18614531, PubMed:19136964). {ECO:0000269|PubMed:12055182, ECO:0000269|PubMed:18614531, ECO:0000269|PubMed:19136964}. +P97391 PA2G5_MOUSE Calcium-dependent phospholipase A2 (EC 3.1.1.4) (Group V phospholipase A2) (PLA2-10) (Phosphatidylcholine 2-acylhydrolase 5) 137 15,859 Active site (2); Chain (1); Disulfide bond (6); Metal binding (4); Sequence conflict (1); Signal peptide (1) FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. This isozyme hydrolyzes L-alpha-palmitoyl-2-oleoyl phosphatidylcholine more efficiently than L-alpha-1-palmitoyl-2-arachidonyl phosphatidylcholine, L-alpha-1-palmitoyl-2-arachidonyl phosphatidylethanolamine or L-alpha-1-stearoyl-2-arachidonyl phosphatidylinositol (By similarity). {ECO:0000250}. PTM: This enzyme lacks one of the seven disulfide bonds found in similar PA2 proteins. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10531350}. Membrane {ECO:0000269|PubMed:10531350}. Note=Also associated with various membranous organelles including the Golgi apparatus, nuclear envelope, and plasma membrane. +Q9QUL3 PA2GE_MOUSE Group IIE secretory phospholipase A2 (GIIE sPLA2) (sPLA2-IIE) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase 2E) 142 15,943 Active site (2); Chain (1); Disulfide bond (7); Metal binding (4); Signal peptide (1) FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Highly expressed in uterus, and at lower levels in various other tissues. +Q9QZT4 PA2GF_MOUSE Group IIF secretory phospholipase A2 (GIIF sPLA2) (sPLA2-IIF) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase 2F) 168 18,880 Active site (2); Alternative sequence (1); Chain (1); Disulfide bond (7); Glycosylation (3); Metal binding (4); Mutagenesis (2); Region (1); Signal peptide (1) FUNCTION: May play a role in lipid mediator production in inflammatory conditions, by providing arachidonic acid to downstream cyclooxygenases and lipoxygenases. Phospholipase A2, which catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides (PubMed:10531313). Hydrolyzes phosphatidylethanolamine more efficiently than phosphatidylcholine, with only a modest preference for arachidonic acid versus linoelic acid at the sn-2 position. Comparable activity toward 1-palmitoyl-2-oleoyl-phosphatidylserine vesicles to that toward 1-palmitoyl-2-oleoyl-phosphatidylglycerol (PubMed:11877435). Prefers phosphatidylglycerol compared to phosphatidylcholine (PubMed:10531313). {ECO:0000269|PubMed:10531313, ECO:0000269|PubMed:11877435}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11877435}. Cell membrane; Peripheral membrane protein {ECO:0000269|PubMed:11877435}. TISSUE SPECIFICITY: Strongly expressed in testis. {ECO:0000269|PubMed:10531313}. +Q3V3Q7 PACS2_MOUSE Phosphofurin acidic cluster sorting protein 2 (PACS-2) (PACS1-like protein) 862 94,932 Chain (1); Compositional bias (2); Modified residue (5); Sequence conflict (3) FUNCTION: Multifunctional sorting protein that controls the endoplasmic reticulum (ER)-mitochondria communication, including the apposition of mitochondria with the ER and ER homeostasis. In addition, in response to apoptotic inducer, translocates BIB to mitochondria, which initiates a sequence of events including the formation of mitochondrial truncated BID, the release of cytochrome c, the activation of caspase-3 thereby causing cell death. May also involved in ion channel trafficking, directing acidic cluster-containing ion channels to distinct subcellular compartments (By similarity). {ECO:0000250|UniProtKB:Q86VP3}. SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:Q86VP3}. Mitochondrion {ECO:0000250|UniProtKB:Q86VP3}. SUBUNIT: Interacts with BID and PKD2. Interacts with SIRT1. Interacts with HDAC1. Interacts with TRPV1. {ECO:0000250|UniProtKB:Q86VP3}. +Q8K2T8 PAF1_MOUSE RNA polymerase II-associated factor 1 homolog 535 60,518 Chain (1); Coiled coil (1); Compositional bias (2); Cross-link (2); Modified residue (2); Sequence conflict (3) FUNCTION: Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and is involved in transcriptional elongation, acting both indepentently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1. PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B ubiquitination is proposed to be coupled to transcription. PAF1C is involved in mRNA 3' end formation probably through association with cleavage and poly(A) factors. Connects PAF1C with the RNF20/40 E3 ubiquitin-protein ligase complex. Involved in polyadenylation of mRNA precursors (By similarity). {ECO:0000250, ECO:0000269|PubMed:19345177}. SUBCELLULAR LOCATION: Nucleus. Note=Punctuate distribution throughout the nucleus except in nucleoli and the perinuclear chromatin. {ECO:0000250}. SUBUNIT: Component of the PAF1 complex, which consists of CDC73, PAF1, LEO1, CTR9, RTF1 and WDR61. The PAF1 complex interacts with PHF5A (PubMed:27749823). Interacts with POLR2A, TCEA1, TTC37, KMT2A/MLL1, SUPT5H, RNF20 and RNF40. Interacts with UBE2E1 (By similarity). {ECO:0000250|UniProtKB:Q8N7H5, ECO:0000269|PubMed:27749823}. +Q8VEB4 PAG15_MOUSE Group XV phospholipase A2 (EC 2.3.1.-) (1-O-acylceramide synthase) (ACS) (LCAT-like lysophospholipase) (LLPL) (Lysophospholipase 3) (Lysosomal phospholipase A2) (LPLA2) 412 47,307 Active site (3); Binding site (2); Chain (1); Disulfide bond (1); Glycosylation (4); Mutagenesis (5); Sequence conflict (1); Signal peptide (1) FUNCTION: Has transacylase and calcium-independent phospholipase A2 activity. Catalyzes the formation of 1-O-acyl-N-acetylsphingosine and the concomitant release of a lyso-phospholipid (PubMed:11790796, PubMed:16106046, PubMed:16880524, PubMed:19017977, PubMed:20410020). Has high activity with 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) and 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC), catalyzing the transfer of oleic acid to N-acetyl-sphingosine (PubMed:16880524). Required for normal phospholipid degradation in alveolar and peritoneal macrophages and in spleen (PubMed:16880524, PubMed:19017977). {ECO:0000269|PubMed:11790796, ECO:0000269|PubMed:16106046, ECO:0000269|PubMed:16880524, ECO:0000269|PubMed:19017977, ECO:0000269|PubMed:20410020}. PTM: N-glycosylated (PubMed:11790796). N-glycosylation is important for maturation of the enzyme and normal subcellular location (By similarity). {ECO:0000250|UniProtKB:Q8NCC3, ECO:0000269|PubMed:11790796}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19017977, ECO:0000269|PubMed:20410020}. Lysosome {ECO:0000269|PubMed:19017977}. Membrane {ECO:0000250|UniProtKB:Q8NCC3}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8NCC3}. TISSUE SPECIFICITY: Detected in blood plasma (PubMed:20410020). Detected in alveolar macrophages (at protein level) (PubMed:16106046, PubMed:16880524, PubMed:19017977). Detected in heart, liver, spleen, kidney, thymus, brain and lung (PubMed:16880524). {ECO:0000269|PubMed:16106046, ECO:0000269|PubMed:16880524, ECO:0000269|PubMed:19017977, ECO:0000269|PubMed:20410020}. +Q8BGF7 PAN2_MOUSE PAN2-PAN3 deadenylation complex catalytic subunit Pan2 (EC 3.1.13.4) (Inactive ubiquitin carboxyl-terminal hydrolase 52) (PAB1P-dependent poly(A)-specific ribonuclease) (Poly(A)-nuclease deadenylation complex subunit 2) (PAN deadenylation complex subunit 2) 1200 135,253 Alternative sequence (3); Chain (1); Domain (2); Erroneous initiation (1); Metal binding (4); Modified residue (2); Region (1); Repeat (4); Sequence conflict (1) FUNCTION: Catalytic subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in general and miRNA-mediated mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein (PABP). PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by XRN1 (PubMed:16284618). Also acts as an important regulator of the HIF1A-mediated hypoxic response. Required for HIF1A mRNA stability independent of poly(A) tail length regulation (By similarity). {ECO:0000255|HAMAP-Rule:MF_03182, ECO:0000269|PubMed:16284618}. SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000255|HAMAP-Rule:MF_03182, ECO:0000269|PubMed:18625844}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03182}. Note=Shuttles between nucleus and cytoplasm. {ECO:0000255|HAMAP-Rule:MF_03182}. SUBUNIT: Forms a heterotrimer with an asymmetric homodimer of the regulatory subunit PAN3 to form the poly(A)-nuclease (PAN) deadenylation complex (By similarity). Interacts with ZFP36 (PubMed:21078877). {ECO:0000255|HAMAP-Rule:MF_03182, ECO:0000269|PubMed:21078877}. DOMAIN: Contains a pseudo-UCH domain. This ubiquitin C-terminal hydrolase (UCH)-like or ubiquitin specific protease (USP)-like domain is predicted to be catalytically inactive because it lacks the active site catalytic triad characteristic of thiol proteases, with residues at the equivalent structural positions that are incompatible with catalysis, and it cannot bind ubiquitin. It functions as a structural scaffold for intra- and intermolecular interactions in the complex. {ECO:0000255|HAMAP-Rule:MF_03182}.; DOMAIN: The linker, or PAN3 interaction domain (PID), between the WD40 repeats and the pseudo-UCH domain mediates interaction with PAN3. {ECO:0000255|HAMAP-Rule:MF_03182}. +Q6TCG8 PAQR3_MOUSE Progestin and adipoQ receptor family member 3 (Progestin and adipoQ receptor family member III) (Raf kinase trapping to Golgi) (RKTG) 311 36,212 Chain (1); Region (2); Topological domain (8); Transmembrane (7) TRANSMEM 71 91 Helical. {ECO:0000255}.; TRANSMEM 105 125 Helical. {ECO:0000255}.; TRANSMEM 146 166 Helical. {ECO:0000255}.; TRANSMEM 173 193 Helical. {ECO:0000255}.; TRANSMEM 204 224 Helical. {ECO:0000255}.; TRANSMEM 236 256 Helical. {ECO:0000255}.; TRANSMEM 276 296 Helical. {ECO:0000255}. TOPO_DOM 1 70 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 92 104 Lumenal. {ECO:0000255}.; TOPO_DOM 126 145 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 167 172 Lumenal. {ECO:0000255}.; TOPO_DOM 194 203 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 225 235 Lumenal. {ECO:0000255}.; TOPO_DOM 257 275 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 297 311 Lumenal. {ECO:0000255}. FUNCTION: Functions as a spatial regulator of RAF1 kinase by sequestrating it to the Golgi. {ECO:0000269|PubMed:17724343}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:17724343}; Multi-pass membrane protein {ECO:0000269|PubMed:17724343}. +Q9CQY7 PAQRB_MOUSE Monocyte to macrophage differentiation factor (Progestin and adipoQ receptor family member 11) (Progestin and adipoQ receptor family member XI) 238 27,677 Chain (1); Erroneous gene model prediction (1); Topological domain (8); Transmembrane (7) TRANSMEM 29 49 Helical. {ECO:0000255}.; TRANSMEM 62 82 Helical. {ECO:0000255}.; TRANSMEM 102 122 Helical. {ECO:0000255}.; TRANSMEM 124 144 Helical. {ECO:0000255}.; TRANSMEM 152 172 Helical. {ECO:0000255}.; TRANSMEM 175 195 Helical. {ECO:0000255}.; TRANSMEM 199 219 Helical. {ECO:0000255}. TOPO_DOM 1 28 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 50 61 Lumenal. {ECO:0000255}.; TOPO_DOM 83 101 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 123 123 Lumenal. {ECO:0000255}.; TOPO_DOM 145 151 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 173 174 Lumenal. {ECO:0000255}.; TOPO_DOM 196 198 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 220 238 Lumenal. {ECO:0000255}. FUNCTION: Involved in the dynamics of lysosomal membranes associated with microglial activation following brain lesion. {ECO:0000250}. SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Lysosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +P55086 PAR2_MOUSE Proteinase-activated receptor 2 (PAR-2) (Coagulation factor II receptor-like 1) (G-protein coupled receptor 11) (Thrombin receptor-like 1) 399 44,752 Chain (1); Compositional bias (1); Disulfide bond (1); Glycosylation (2); Lipidation (1); Propeptide (1); Signal peptide (1); Site (1); Topological domain (8); Transmembrane (7) TRANSMEM 74 103 Helical; Name=1. {ECO:0000250|UniProtKB:P55085}.; TRANSMEM 111 139 Helical; Name=2. {ECO:0000250|UniProtKB:P55085}.; TRANSMEM 152 179 Helical; Name=3. {ECO:0000250|UniProtKB:P55085}.; TRANSMEM 186 213 Helical; Name=4. {ECO:0000250|UniProtKB:P55085}.; TRANSMEM 238 271 Helical; Name=5. {ECO:0000250|UniProtKB:P55085}.; TRANSMEM 280 319 Helical; Name=6. {ECO:0000250|UniProtKB:P55085}.; TRANSMEM 326 349 Helical; Name=7. {ECO:0000250|UniProtKB:P55085}. TOPO_DOM 39 73 Extracellular. {ECO:0000250|UniProtKB:P55085}.; TOPO_DOM 104 110 Cytoplasmic. {ECO:0000250|UniProtKB:P55085}.; TOPO_DOM 140 151 Extracellular. {ECO:0000250|UniProtKB:P55085}.; TOPO_DOM 180 185 Cytoplasmic. {ECO:0000250|UniProtKB:P55085}.; TOPO_DOM 214 237 Extracellular. {ECO:0000250|UniProtKB:P55085}.; TOPO_DOM 272 279 Cytoplasmic. {ECO:0000250|UniProtKB:P55085}.; TOPO_DOM 320 325 Extracellular. {ECO:0000250|UniProtKB:P55085}.; TOPO_DOM 350 399 Cytoplasmic. {ECO:0000250|UniProtKB:P55085}. FUNCTION: Receptor for trypsin and trypsin-like enzymes coupled to G proteins. Its function is mediated through the activation of several signaling pathways including phospholipase C (PLC), intracellular calcium, mitogen-activated protein kinase (MAPK), I-kappaB kinase/NF-kappaB and Rho. Can also be transactivated by cleaved F2r/Par1. Involved in modulation of inflammatory responses and regulation of innate and adaptive immunity, and acts as a sensor for proteolytic enzymes generated during infection. Generally is promoting inflammation. Can signal synergistically with Tlr4 and probably Tlr2 in inflammatory responses and modulates Tlr3 signaling. Has a protective role in establishing the endothelial barrier; the activity involves coagulation factor X. Regulates endothelial cell barrier integrity during neutrophil extravasation, probably following proteolytic cleavage by PRTN3 (By similarity). Proposed to have a bronchoprotective role in airway epithelium, but also shown to compromise the airway epithelial barrier by interrupting E-cadherin adhesion. Involved in the regulation of vascular tone; activation results in hypotension presumably mediated by vasodilation. Associates with a subset of G proteins alpha subunits such as GNAQ, GNA11, GNA14, GNA12 and GNA13, but probably not with G(o) alpha, G(i) subunit alpha-1 and G(i) subunit alpha-2. Believed to be a class B receptor which internalizes as a complex with arrestin and traffic with it to endosomal vesicles, presumably as desensitized receptor, for extended periods of time. Mediates inhibition of TNF-alpha stimulated JNK phosphorylation via coupling to GNAQ and GNA11; the function involves dissociation of Ripk1 and Tradd from Tnfr1. Mediates phosphorylation of nuclear factor NF-kappa-B RELA subunit at 'Ser-536'; the function involves Ikbkb and is predominantly independent of G proteins. Involved in cellular migration. Involved in cytoskeletal rearrangement and chemotaxis through beta-arrestin-promoted scaffolds; the function is independent of GNAQ and GNA11 and involves promotion of cofilin dephosphorylation and actin filament severing. Induces redistribution of Cops5 from the plasma membrane to the cytosol and activation of the JNK cascade is mediated by Cops5. Involved in the recruitment of leukocytes to the sites of inflammation and is the major PAR receptor capable of modulating eosinophil function such as proinflammatory cytokine secretion, superoxide production and degranulation. During inflammation promotes dendritic cell maturation, trafficking to the lymph nodes and subsequent T-cell activation. Involved in antimicrobial response of innate immnune cells; activation enhances phagocytosis of Gram-positive and killing of Gram-negative bacteria. Acts synergistically with interferon-gamma in enhancing antiviral responses (By similarity). {ECO:0000250|UniProtKB:P55085, ECO:0000269|PubMed:11086091, ECO:0000269|PubMed:12821670, ECO:0000269|PubMed:19845798, ECO:0000269|PubMed:20215560, ECO:0000269|PubMed:9918574}. PTM: A proteolytic cleavage generates a new N-terminus that functions as a tethered ligand. Activating serine proteases include trypsin, mast cell tryptase, coagulation factors VII and Xa, myeloblastin/PRTN3 and membrane-type serine protease 1/ST14. Proposed subsequent cleaveage by serine proteases is leading to receptor deactivation and include neutrophil elastase and cathepsin G. At least in part, implicated proteases are also shown to activate the receptor; the glycosylation status of the receptor is thought to contribute to the difference. {ECO:0000250|UniProtKB:P55085}.; PTM: N-glycosylated and sialylated. {ECO:0000250|UniProtKB:P55085}.; PTM: Multiple phosphorylated on serine and threonine residues in the cytoplasmic region upon receptor activation; required for receptor desensitization and recruitment of beta-arrestin.; PTM: Monoubiquitinated by Cbl at the plasma membrane and in early endosomes; not required for receptor endocytosis but for translocation to late endosomes or lysosomes. Deubiquitination involves Stambp and Usp8; required for lysosomal trafficking and receptor degradation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein. SUBUNIT: Interacts with TLR4, COPS5 and TMED2 (By similarity). Interacts with GNAQ, GNA11, GNA12, GNA13 and GNA14. {ECO:0000250, ECO:0000269|PubMed:20215560}. +P47242 PAX9_MOUSE Paired box protein Pax-9 342 36,389 Chain (1); Domain (1); Region (1) FUNCTION: Transcription factor required for normal development of thymus, parathyroid glands, ultimobranchial bodies, teeth, skeletal elements of skull and larynx as well as distal limbs. {ECO:0000269|PubMed:9732271}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with KDM5B. {ECO:0000250}. TISSUE SPECIFICITY: In the embryo, expressed in pharyngeal pouches and derivatives, developing vertebral column, tail, head and limbs. +Q99NE9 PBX4_MOUSE Pre-B-cell leukemia transcription factor 4 (Homeobox protein PBX4) 378 41,961 Alternative sequence (2); Chain (1); DNA binding (1) SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. TISSUE SPECIFICITY: Almost exclusively expressed in testis. {ECO:0000269|PubMed:11335119}. +P57722 PCBP3_MOUSE Poly(rC)-binding protein 3 (Alpha-CP3) 371 39,294 Alternative sequence (1); Chain (1); Domain (3); Erroneous initiation (1); Sequence conflict (2) FUNCTION: Single-stranded nucleic acid binding protein that binds preferentially to oligo dC. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed, with highest levels in testis and fat tissues and lowest in heart. {ECO:0000269|PubMed:10936052}. +O55134 PCD12_MOUSE Protocadherin-12 (Vascular cadherin-2) (Vascular endothelial cadherin-2) (VE-cad-2) (VE-cadherin-2) [Cleaved into: Protocadherin-12, secreted form] 1180 128,673 Chain (2); Domain (6); Glycosylation (5); Modified residue (2); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 717 737 Helical. {ECO:0000255}. TOPO_DOM 18 716 Extracellular. {ECO:0000255}.; TOPO_DOM 738 1180 Cytoplasmic. {ECO:0000255}. FUNCTION: Cellular adhesion molecule that may play an important role in cell-cell interactions at interendothelial junctions (PubMed:9651350). Acts as a regulator of cell migration, probably via increasing cell-cell adhesion (By similarity). Promotes homotypic calcium-dependent aggregation and adhesion and clusters at intercellular junctions (PubMed:9651350). Unable to bind to catenins, weakly associates with the cytoskeleton (PubMed:9651350). {ECO:0000250|UniProtKB:Q9NPG4, ECO:0000269|PubMed:9651350}. PTM: N-glycosylated. {ECO:0000269|PubMed:15541725}.; PTM: Protocadherin-12: Cleaved by ADAM10 close to the transmembrane domain to release the Protocadherin-12, secreted form in the serum. Cleavage results in reduced cellular adhesion in a cell migration assay. {ECO:0000250|UniProtKB:Q9NPG4}. SUBCELLULAR LOCATION: Protocadherin-12: Cell membrane {ECO:0000250|UniProtKB:Q9NPG4}; Single-pass type I membrane protein {ECO:0000255}. Cell junction {ECO:0000269|PubMed:9651350}.; SUBCELLULAR LOCATION: Protocadherin-12, secreted form: Secreted {ECO:0000250|UniProtKB:Q9NPG4}. Note=The secreted form is produced following cleavage by ADAM10. {ECO:0000250|UniProtKB:Q9NPG4}. TISSUE SPECIFICITY: Expressed in endothelial cells: localizes in vasculogenic rather than angiogenic endothelium (PubMed:9651350, PubMed:15541725). Strongly expressed in a subset of invasive cells of the placenta, named glycogen-rich trophoblasts cells (at protein level) (PubMed:15541725). glycogen-rich trophoblasts cells originate from the from the ectoplacental cone where they rapidly form tight islets (at protein level) (PubMed:16269175). In adult mice, present at high level in mesangial cells of kidney glomeruli, while expression was not detected in other types of perivascular cells (PubMed:15541725). {ECO:0000269|PubMed:15541725, ECO:0000269|PubMed:16269175, ECO:0000269|PubMed:9651350}. +Q6PAC4 PCARE_MOUSE Photoreceptor cilium actin regulator 1279 139,298 Chain (1); Erroneous initiation (2); Initiator methionine (1); Lipidation (2); Sequence conflict (1) FUNCTION: Plays an essential role for normal photoreceptor cell maintenance and vision. {ECO:0000269|PubMed:25616964}. SUBCELLULAR LOCATION: Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:25616964}. Photoreceptor inner segment {ECO:0000269|PubMed:25616964}. TISSUE SPECIFICITY: Specifically expressed in retina. {ECO:0000269|PubMed:25616964}. +Q99PJ1 PCD15_MOUSE Protocadherin-15 1943 214,738 Alternative sequence (35); Beta strand (101); Chain (1); Compositional bias (3); Disulfide bond (1); Domain (11); Erroneous initiation (1); Glycosylation (13); Helix (24); Mutagenesis (2); Sequence conflict (48); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (24) TRANSMEM 1382 1402 Helical. {ECO:0000255}. TOPO_DOM 27 1381 Extracellular. {ECO:0000255}.; TOPO_DOM 1403 1943 Cytoplasmic. {ECO:0000255}. FUNCTION: Calcium-dependent cell-adhesion protein. Required for inner ear neuroepithelial cell elaboration and cochlear function. Probably involved in the maintenance of normal retinal function. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21436032, ECO:0000269|PubMed:23217710}; Single-pass membrane protein {ECO:0000269|PubMed:21436032, ECO:0000269|PubMed:23217710}. Note=Efficient localization to the plasma membrane requires the presence of LHFPL5.; SUBCELLULAR LOCATION: Isoform 1: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 2: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 3: Secreted {ECO:0000305}.; SUBCELLULAR LOCATION: Isoform 4: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 5: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 6: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 7: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 8: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 9: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 10: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 11: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 12: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 13: Secreted {ECO:0000305}.; SUBCELLULAR LOCATION: Isoform 14: Secreted {ECO:0000305}.; SUBCELLULAR LOCATION: Isoform 15: Secreted {ECO:0000305}.; SUBCELLULAR LOCATION: Isoform 16: Secreted {ECO:0000305}.; SUBCELLULAR LOCATION: Isoform 17: Secreted {ECO:0000305}.; SUBCELLULAR LOCATION: Isoform 18: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 19: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 21: Secreted {ECO:0000305}.; SUBCELLULAR LOCATION: Isoform 22: Secreted {ECO:0000305}.; SUBCELLULAR LOCATION: Isoform 23: Secreted {ECO:0000305}. SUBUNIT: Antiparallel heterodimer with CDH23 (PubMed:23135401, PubMed:17805295). Found in a complex with TMIE and LHFPL5 (PubMed:25467981). Interacts with LHFPL5/TMHS; this interaction is required for efficient localization to hair bundles (PubMed:23217710). Interacts with MYO7A (PubMed:16481439). Interacts with USH1G; this interaction may recruit USH1G to the plasma membrane (PubMed:21436032). Interacts with TOMT (PubMed:28504928). Isoforms CD1 and CD3 interact with TMC1 (via N-terminus) and TMC2 (via N-terminus) (PubMed:25114259). {ECO:0000269|PubMed:16481439, ECO:0000269|PubMed:17805295, ECO:0000269|PubMed:21436032, ECO:0000269|PubMed:23135401, ECO:0000269|PubMed:23217710, ECO:0000269|PubMed:25114259, ECO:0000269|PubMed:25467981, ECO:0000269|PubMed:28504928}. DOMAIN: Cadherin repeats 1 and 2 mediate calcium-dependent heterophilic interaction with CDH23. {ECO:0000269|PubMed:23135401}.; DOMAIN: Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain. {ECO:0000269|PubMed:23135401}. TISSUE SPECIFICITY: Expressed in brain and sensory epithelium of the developing inner ear. Expressed in the retina, in the photoreceptor inner segments, the outer plexiform layer, the inner nuclei layer and the ganglion cell layer and, more diffusely in the inner plexiform layer (at protein level). Not detected in the retinal pigment epithelium (at protein level). Expressed in the spleen, dorsal root ganglion, dorsal aspect of neural tube, floor plate and ependymal cells adjacent to the neural canal. {ECO:0000269|PubMed:11429292, ECO:0000269|PubMed:16481439, ECO:0000269|PubMed:16799054, ECO:0000269|PubMed:17805295}. DISEASE: Note=Defects in Pcdh15 are the cause of the Ames waltzer (av) phenotype. It is characterized by deafness and a balance disorder, associated with the degeneration of inner ear neuroepithelia. +Q3TFD2 PCAT1_MOUSE Lysophosphatidylcholine acyltransferase 1 (LPC acyltransferase 1) (LPCAT-1) (LysoPC acyltransferase 1) (mLPCAT1) (EC 2.3.1.23) (1-acylglycerophosphocholine O-acyltransferase) (1-alkylglycerophosphocholine O-acetyltransferase) (EC 2.3.1.67) (Acetyl-CoA:lyso-platelet-activating factor acetyltransferase) (Acetyl-CoA:lyso-PAF acetyltransferase) (Lyso-PAF acetyltransferase) (LysoPAFAT) (Acyltransferase-like 2) 534 59,744 Alternative sequence (2); Calcium binding (1); Chain (1); Domain (2); Erroneous initiation (3); Motif (2); Mutagenesis (25); Sequence conflict (7); Topological domain (2); Transmembrane (1) TRANSMEM 58 78 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 57 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 79 534 Lumenal. {ECO:0000255}. Lipid metabolism; phospholipid metabolism. FUNCTION: Possesses both acyltransferase and acetyltransferase activities (PubMed:16704971). Activity is calcium-independent (PubMed:18285344). Mediates the conversion of 1-acyl-sn-glycero-3-phosphocholine (LPC) into phosphatidylcholine (PC) (PubMed:16704971, PubMed:18156367). Displays a clear preference for saturated fatty acyl-CoAs, and 1-myristoyl or 1-palmitoyl LPC as acyl donors and acceptors, respectively (PubMed:16704971, PubMed:18285344). May synthesize phosphatidylcholine in pulmonary surfactant, thereby playing a pivotal role in respiratory physiology (PubMed:16704971). Involved in the regulation of lipid droplet number and size (By similarity). {ECO:0000250|UniProtKB:Q1HAQ0, ECO:0000250|UniProtKB:Q8NF37, ECO:0000269|PubMed:16704971, ECO:0000269|PubMed:18156367, ECO:0000269|PubMed:18285344}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16704971}; Single-pass type II membrane protein {ECO:0000269|PubMed:18156367}. Golgi apparatus membrane {ECO:0000269|PubMed:16704971}; Single-pass type II membrane protein {ECO:0000269|PubMed:18156367}. Lipid droplet {ECO:0000250|UniProtKB:Q8NF37}. Note=May adopt a monotopic topology when embedded in the lipid monolayer of the lipid droplet, with both termini exposed to the cytoplasm. {ECO:0000250|UniProtKB:Q8NF37}. DOMAIN: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphocholine. {ECO:0000250}.; DOMAIN: The di-lysine motif confers endoplasmic reticulum localization for type I membrane proteins. {ECO:0000250}. TISSUE SPECIFICITY: Predominantly expressed in lung where it is enriched in alveolar type II cells. Expressed at lower levels in spleen and brain. Also detected in erythroleukemic cells and reticulocytes. Weakly or not expressed in other tissues. {ECO:0000269|PubMed:16704971, ECO:0000269|PubMed:16864775, ECO:0000269|PubMed:18156367}. +P41778 PBX1_MOUSE Pre-B-cell leukemia transcription factor 1 (Homeobox protein PBX1) 430 46,626 Alternative sequence (2); Beta strand (1); Chain (1); Compositional bias (1); DNA binding (1); Helix (4); Turn (3) FUNCTION: Plays a role in the cAMP-dependent regulation of CYP17 gene expression via its cAMP-regulatory sequence (CRS1) 5'-ATCAATCAA-3'. Acts as a transcriptional activator of PF4 in complex with MEIS1. May have a role in steroidogenesis and, subsequently, sexual development and differentiation. Isoform PBX1b as part of a PDX1:PBX1b:MEIS2b complex in pancreatic acinar cells is involved in the transcriptional activation of the ELA1 enhancer; the complex binds to the enhancer B element and cooperates with the transcription factor 1 complex (PTF1) bound to the enhancer A element. Probably in complex with MEIS2, is involved in transcriptional regulation by KLF4. Acts as a transcriptional activator of NKX2-5 and a transcriptional repressor of CDKN2B. Together with NKX2-5, it is required for spleen development through a mechanism that involves CDKN2B repression. {ECO:0000269|PubMed:22560297}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P40424}. SUBUNIT: Forms a heterodimer with MEIS1 which binds DNA including a cAMP-responsive sequence in CYP17. Also forms heterotrimers with MEIS1 and a number of HOX proteins including HOXA9, HOXD4, HOXD9 and HOXD10. Interacts with PBXIP1 and TLX1. Isoform PBX1a interacts with MEIS2 isoform Meis2D, SP1, SP3 and KLF4. Isoform PBX1b is part of a PDX1:PBX1b:MEIS2b complex; PBX1b recruits Meis2B to the complex. Interacts with FOXC1 (By similarity). {ECO:0000250|UniProtKB:P40424, ECO:0000269|PubMed:10082572, ECO:0000269|PubMed:10523646, ECO:0000269|PubMed:11279116, ECO:0000269|PubMed:12409300, ECO:0000269|PubMed:9315626, ECO:0000269|PubMed:9525891, ECO:0000269|PubMed:9710595}. TISSUE SPECIFICITY: Widely distributed in steroidogenic and non-steroidogenic cells. +Q8BYI6 PCAT2_MOUSE Lysophosphatidylcholine acyltransferase 2 (LPC acyltransferase 2) (LPCAT-2) (LysoPC acyltransferase 2) (EC 2.3.1.23) (1-acylglycerol-3-phosphate O-acyltransferase 11) (1-AGP acyltransferase 11) (1-AGPAT 11) (EC 2.3.1.51) (1-acylglycerophosphocholine O-acyltransferase) (1-alkylglycerophosphocholine O-acetyltransferase) (EC 2.3.1.67) (Acetyl-CoA:lyso-platelet-activating factor acetyltransferase) (Acetyl-CoA:lyso-PAF acetyltransferase) (Lyso-PAF acetyltransferase) (LysoPAFAT) (Acyltransferase-like 1) 544 60,254 Alternative sequence (3); Calcium binding (2); Chain (1); Domain (2); Motif (2); Topological domain (2); Transmembrane (1) TRANSMEM 59 79 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 58 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 80 544 Lumenal. {ECO:0000255}. Lipid metabolism; phospholipid metabolism. FUNCTION: Possesses both acyltransferase and acetyltransferase activities (PubMed:17182612, PubMed:18156367). Activity is calcium-dependent (PubMed:17182612). Involved in platelet-activating factor (PAF) biosynthesis by catalyzing the conversion of the PAF precursor, 1-O-alkyl-sn-glycero-3-phosphocholine (lyso-PAF) into 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine (PAF) (PubMed:17182612). Also converts lyso-PAF to 1-O-alkyl-2-acyl-sn-glycero-3-phosphocholine (PC), a major component of cell membranes and a PAF precursor (PubMed:17182612, PubMed:18156367). Under resting conditions, acyltransferase activity is preferred (PubMed:17182612). Upon acute inflammatory stimulus, acetyltransferase activity is enhanced and PAF synthesis increases (PubMed:17182612). Also catalyzes the conversion of 1-acyl-sn-glycero-3-phosphocholine to 1,2-diacyl-sn-glycero-3-phosphocholine. Involved in the regulation of lipid droplet number and size (By similarity). {ECO:0000250|UniProtKB:Q8NF37, ECO:0000269|PubMed:17182612, ECO:0000269|PubMed:18156367}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:17182612}; Single-pass type II membrane protein {ECO:0000269|PubMed:18156367}. Golgi apparatus membrane {ECO:0000269|PubMed:17182612}; Single-pass type II membrane protein {ECO:0000269|PubMed:18156367}. Lipid droplet {ECO:0000250|UniProtKB:Q8NF37}. DOMAIN: The HXXXXD motif is essential for acyltransferase activity. {ECO:0000250}. TISSUE SPECIFICITY: Highest expression is found in resident macrophages and casein-induced neutrophils followed by skin, colon, spleen and thioglycollate-induced macrophages. Detected in erythroleukemic cells but not in reticulocytes. {ECO:0000269|PubMed:17182612, ECO:0000269|PubMed:18156367}. +O35984 PBX2_MOUSE Pre-B-cell leukemia transcription factor 2 (Homeobox protein PBX2) 430 45,809 Chain (1); Compositional bias (2); DNA binding (1); Modified residue (5) FUNCTION: Transcriptional activator that binds the sequence 5'-ATCAATCAA-3'. Activates transcription of PF4 in complex with MEIS1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Forms heterodimers with MEIS1 and heterotrimers with MEIS1 and HOXA9. Interacts with PBXIP1 (By similarity). {ECO:0000250}. +A9Q751 PCDP1_MOUSE Cilia- and flagella-associated protein 221 (Primary ciliary dyskinesia protein 1) 836 96,956 Chain (1); Region (1) FUNCTION: May play a role in cilium morphogenesis. {ECO:0000305|PubMed:18039845}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:18039845}. Cytoplasm {ECO:0000269|PubMed:18039845}. SUBUNIT: Interacts with calmodulin; calcium-dependent. {ECO:0000269|PubMed:20421426}. TISSUE SPECIFICITY: Expressed in testis, specifically in developing spermatocytes and spermatids but not in immature spermatogonia. Expressed in the ciliated respiratory epithelial cells lining the sinuses, trachea and bronchi (at protein level). {ECO:0000269|PubMed:15613475, ECO:0000269|PubMed:18039845}. +Q91Y11 PCDA9_MOUSE Protocadherin alpha-9 (PCDH-alpha-9) 979 106,763 Chain (1); Compositional bias (1); Domain (6); Glycosylation (3); Region (1); Repeat (5); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 727 747 Helical. {ECO:0000255}. TOPO_DOM 60 726 Extracellular. {ECO:0000305}.; TOPO_DOM 748 979 Cytoplasmic. {ECO:0000305}. FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain. {ECO:0000303|PubMed:11230163}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000303|PubMed:11230163}; Single-pass type I membrane protein {ECO:0000303|PubMed:11230163}. +Q3UK78 PCGF5_MOUSE Polycomb group RING finger protein 5 (RING finger protein 159) 256 29,657 Alternative sequence (1); Chain (1); Frameshift (1); Zinc finger (1) FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility (PubMed:27136092, PubMed:28596365). Within the PRC1-like complex, regulates RNF2 ubiquitin ligase activity (By similarity). Plays a redundant role with PCGF3 as part of a PRC1-like complex that mediates monoubiquitination of histone H2A 'Lys-119' on the X chromosome and is required for normal silencing of one copy of the X chromosome in XX females (PubMed:28596365). {ECO:0000250|UniProtKB:Q86SE9, ECO:0000269|PubMed:27136092, ECO:0000269|PubMed:28596365}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28596365}. Nucleus, nucleoplasm {ECO:0000269|PubMed:28596365}. Note=Recruited by the non-coding RNA Xist to specific nuclear foci that probably correspond to the inactivated X chromosome. {ECO:0000269|PubMed:28596365}. SUBUNIT: Component of a PRC1-like complex that contains PCGF5, RNF2 and UBE2D3 (PubMed:28596365). Interacts with RNF2; the interaction is direct (PubMed:27136092, PubMed:28596365). Interacts with CBX6, CBX7 and CBX8. Interacts with AUTS2; the interaction is direct. Identified in a complex that contains AUTS2, PCGF5, CSNK2B and RNF2 (By similarity). {ECO:0000250|UniProtKB:Q86SE9, ECO:0000269|PubMed:27136092, ECO:0000269|PubMed:28596365}. TISSUE SPECIFICITY: Detected in hematopoietic stem cells and multipotent progenitor cells. {ECO:0000269|PubMed:27136092}. +P29121 PCSK4_MOUSE Proprotein convertase subtilisin/kexin type 4 (EC 3.4.21.-) (KEX2-like endoprotease 3) (Neuroendocrine convertase 3) (NEC 3) (Prohormone convertase 3) 655 73,214 Active site (3); Alternative sequence (7); Chain (1); Domain (2); Glycosylation (1); Propeptide (1); Sequence conflict (2); Signal peptide (1) FUNCTION: Proprotein convertase involved in the processing of hormone and other protein precursors at sites comprised of pairs of basic amino acid residues. In males, important for ADAM2 processing as well as other acrosomal proteins with roles in fertilization and critical for normal fertilization events such as sperm capacitation, acrosome reaction and binding of sperm to zona pellucida (PubMed:9192653, PubMed:16371590, PubMed:19342015, PubMed:21302280). Plays also a role in female fertility, involved in the regulation of trophoblast migration and placental development, may be through the proteolytical processing and activation of proteins such as IGF2 (By similarity). May also participate in folliculogenesis in the ovaries (PubMed:11164898). {ECO:0000250|UniProtKB:Q6UW60, ECO:0000269|PubMed:11164898, ECO:0000269|PubMed:16371590, ECO:0000269|PubMed:19342015, ECO:0000269|PubMed:21302280, ECO:0000269|PubMed:9192653}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q6UW60}.; PTM: Synthesized in the endoplasmic reticulum as a zymogen, is matured by autocatalytic cleavage between the prodomain and the catalytic domain. {ECO:0000250|UniProtKB:Q6UW60}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome membrane {ECO:0000269|PubMed:16371590, ECO:0000269|PubMed:21080038, ECO:0000269|PubMed:21302280}. SUBUNIT: The proPCSK4 form interacts with HSPA5; the interaction takes place at the endoplasmic reticulum. {ECO:0000250|UniProtKB:Q6UW60}. TISSUE SPECIFICITY: Expressed abundantly in the testis since postnatal Day 16 (PubMed:1372895, PubMed:16371590, PubMed:21302280). In testis, strongly detected in round and elongated spermatids as well as spermatocytes. Also observed in residual bodies engulfed by Sertoli cells at spermatogenic stages VIII and IX (PubMed:16371590). In ovaries, expressed in macrophage-like cells of the ovarian theca, interstitium and corpora lutea (PubMed:11164898). {ECO:0000269|PubMed:11164898, ECO:0000269|PubMed:1372895, ECO:0000269|PubMed:16371590, ECO:0000269|PubMed:21302280}. +P49586 PCY1A_MOUSE Choline-phosphate cytidylyltransferase A (EC 2.7.7.15) (CCT-alpha) (CTP:phosphocholine cytidylyltransferase A) (CCT A) (CT A) (Phosphorylcholine transferase A) 367 41,667 Binding site (4); Chain (1); Modified residue (21); Nucleotide binding (3); Region (3); Repeat (3); Sequence conflict (1) Phospholipid metabolism; phosphatidylcholine biosynthesis; phosphatidylcholine from phosphocholine: step 1/2. FUNCTION: Controls phosphatidylcholine synthesis. PTM: The serine residues of the C-terminus are phosphorylated. The inactive soluble form is stabilized by phosphorylation, the active membrane bound form is promoted by anionic lipids or diacylglycerol, and is stabilized by dephosphorylation (By similarity). {ECO:0000250}.; PTM: Monoubiquitinated by the SCF(FBXL2) complex, leading to proteasomal degradation. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=It can interconvert between an inactive cytosolic form and an active membrane-bound form. {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P19836}. +Q9Z2J6 PD2R2_MOUSE Prostaglandin D2 receptor 2 (Chemoattractant receptor-homologous molecule expressed on Th2 cells) (G-protein coupled receptor 44) (CD antigen CD294, Gpr44) 382 42,950 Chain (1); Disulfide bond (1); Glycosylation (3); Modified residue (2); Motif (1); Topological domain (8); Transmembrane (7) TRANSMEM 33 55 Helical; Name=1. {ECO:0000255}.; TRANSMEM 67 88 Helical; Name=2. {ECO:0000255}.; TRANSMEM 106 126 Helical; Name=3. {ECO:0000255}.; TRANSMEM 146 167 Helical; Name=4. {ECO:0000255}.; TRANSMEM 210 230 Helical; Name=5. {ECO:0000255}.; TRANSMEM 247 268 Helical; Name=6. {ECO:0000255}.; TRANSMEM 288 307 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 32 Extracellular. {ECO:0000255}.; TOPO_DOM 56 66 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 89 105 Extracellular. {ECO:0000255}.; TOPO_DOM 127 145 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 168 209 Extracellular. {ECO:0000255}.; TOPO_DOM 231 246 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 269 287 Extracellular. {ECO:0000255}.; TOPO_DOM 308 357 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for prostaglandin D2 (PGD2). Coupled to the G(i)-protein. Receptor activation may result in pertussis toxin-sensitive decreases in cAMP levels and Ca(2+) mobilization. PI3K signaling is also implicated in mediating PTGDR2 effects. PGD2 induced receptor internalization. CRTH2 internalization can be regulated by diverse kinases such as, PKC, PKA, GRK2, GPRK5/GRK5 and GRK6. Receptor activation is responsible, at least in part, in immune regulation and allergic/inflammation responses (By similarity). {ECO:0000250, ECO:0000269|PubMed:12878180, ECO:0000269|PubMed:16888024}. PTM: Phosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Internalized receptors colocalized with RAB11A. {ECO:0000250}. DOMAIN: The 329-DSEL-332 motif is involved in the recycling of PTGDR2 to the cell surface after agonist-induced internalization. This motif seems to be required for GRK2 and GPRK5/GRK5 to promote agonist-induced internalization (By similarity). Thr-346 is a major site for PKC-induced internalization of the receptor (By similarity). {ECO:0000250}. +Q9WU78 PDC6I_MOUSE Programmed cell death 6-interacting protein (ALG-2-interacting protein 1) (ALG-2-interacting protein X) (E2F1-inducible protein) (Eig2) 869 96,024 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (1); Initiator methionine (1); Modified residue (7); Region (5); Sequence conflict (8) FUNCTION: Multifunctional protein involved in endocytosis, multivesicular body biogenesis, membrane repair, cytokinesis, apoptosis and maintenance of tight junction integrity. Class E VPS protein involved in concentration and sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome. Binds to the phospholipid lysobisphosphatidic acid (LBPA) which is abundant in MVBs internal membranes. The MVB pathway requires the sequential function of ESCRT-O, -I,-II and -III complexes. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis. Adapter for a subset of ESCRT-III proteins, such as CHMP4, to function at distinct membranes. Required for completion of cytokinesis. May play a role in the regulation of both apoptosis and cell proliferation. Regulates exosome biogenesis in concert with SDC1/4 and SDCBP (By similarity). By interacting with F-actin, PARD3 and TJP1 secures the proper assembly and positioning of actomyosin-tight junction complex at the apical sides of adjacent epithelial cells that defines a spatial membrane domain essential for the maintenance of epithelial cell polarity and barrier (PubMed:27336173). {ECO:0000250|UniProtKB:Q8WUM4, ECO:0000269|PubMed:27336173}. PTM: May be phosphorylated on tyrosine residues by activated PDGFRB. {ECO:0000250|UniProtKB:Q8WUM4}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9QZA2}. Melanosome {ECO:0000250|UniProtKB:Q8WUM4}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q8WUM4}. Secreted, exosome {ECO:0000269|PubMed:23523921}. Cell junction, tight junction {ECO:0000269|PubMed:27336173}. Midbody, Midbody ring {ECO:0000250|UniProtKB:Q8WUM4}. Note=Colocalized with CEP55 in the midbody during cytokinesis and at centrosomes in non-dividing cells (By similarity). Component of the actomyosin-tight junction complex (PubMed:27336173). {ECO:0000250|UniProtKB:Q8WUM4, ECO:0000269|PubMed:27336173}. SUBUNIT: Self-associates (By similarity). Interacts with SH3KBP1 (By similarity). Interacts with PDCD6 in a calcium-dependent manner (By similarity). Interacts with TSG101 in a calcium-dependent manner; PDCD6IP homooligomerization may be required for TSG101-binding (By similarity). Interacts with SGSM3 (By similarity). Directly interacts with CHMP4A, CHMP4B and CHMP4C (By similarity). Directly interacts with CEP55 in a 1:2 stoechiometry; this interaction is required for PDCD6IP targeting to the midbody (By similarity). May interact with PDGFRB (By similarity). Interacts with SH3GL1 and SH3GL2/endophilin-1 (By similarity). Forms a complex with SDCBP and SDC2 (PubMed:22660413). Found in a complex with F-actin, TJP1/ZO-1 and PARD3 (PubMed:27336173). Interacts with CD2AP (By similarity). Interacts with ARRDC1 (By similarity). {ECO:0000250|UniProtKB:Q8WUM4, ECO:0000250|UniProtKB:Q9QZA2, ECO:0000269|PubMed:22660413, ECO:0000269|PubMed:27336173}. TISSUE SPECIFICITY: Ubiquitously expressed (PubMed:27336173). High expression in choroid plexus and low expression in cerebral cortex (at protein level) (PubMed:27336173). {ECO:0000269|PubMed:27336173}. +P0C1Q2 PDE11_MOUSE Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11A (EC 3.1.4.35) (EC 3.1.4.53) (cAMP and cGMP phosphodiesterase 11A) 933 104,563 Active site (1); Binding site (1); Chain (1); Domain (3); Metal binding (5); Modified residue (3) FUNCTION: Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides cAMP and cGMP. Catalyzes the hydrolysis of both cAMP and cGMP to 5'-AMP and 5'-GMP, respectively (By similarity). {ECO:0000250, ECO:0000269|PubMed:15800654}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. DOMAIN: The tandem GAF domains bind cGMP, and regulate enzyme activity. The binding of cGMP stimulates enzyme activity (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in testis and developing spermatoza. {ECO:0000269|PubMed:15800654}. +Q3TIU4 PDE12_MOUSE 2',5'-phosphodiesterase 12 (2'-PDE) (2-PDE) (EC 3.1.4.-) (Mitochondrial deadenylase) (EC 3.1.13.4) 608 67,514 Active site (3); Chain (1); Erroneous initiation (1); Metal binding (4); Modified residue (1); Sequence conflict (10); Transit peptide (1) FUNCTION: Enzyme that cleaves 2',5'-phosphodiester bond linking adenosines of the 5'-triphosphorylated oligoadenylates, triphosphorylated oligoadenylates referred as 2-5A modulates the 2-5A system. This enzyme degraded triphosphorylated 2-5A to produce AMP and ATP. Also cleaves 3',5'-phosphodiester bond of oligoadenylates. Plays a role as a negative regulator of the 2-5A system that is one of the major pathways for antiviral and antitumor functions induced by interferon (IFNs) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. +Q61481 PDE1A_MOUSE Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1A (Cam-PDE 1A) (EC 3.1.4.17) (61 kDa Cam-PDE) 565 64,529 Active site (1); Alternative sequence (1); Chain (1); Domain (1); Metal binding (5); Region (1); Sequence conflict (2) FUNCTION: Cyclic nucleotide phosphodiesterase with a dual-specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. Has a higher affinity for cGMP than for cAMP (By similarity). {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +Q64338 PDE1C_MOUSE Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1C (Cam-PDE 1C) (3',5'-cyclic-AMP phosphodiesterase) (EC 3.1.4.-) (3',5'-cyclic-GMP phosphodiesterase) (EC 3.1.4.35) 706 80,290 Active site (1); Alternative sequence (4); Chain (1); Domain (1); Metal binding (5); Modified residue (1) FUNCTION: Calmodulin-dependent cyclic nucleotide phosphodiesterase with a dual-specificity for cAMP and cGMP, which are key regulators of many important physiological processes (PubMed:8810348). Exhibits high affinity for both cAMP and cGMP (By similarity). Modulates the amplitude and duration of the cAMP signal in sensory cilia in response to odorant stimulation, hence contributing to the generation of action potentials. Regulates smooth muscle cell proliferation. Regulates the stability of growth factor receptors, including PDGFRB (Probable). {ECO:0000250|UniProtKB:Q14123, ECO:0000269|PubMed:8810348, ECO:0000305|PubMed:29860631}. SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:29860631}. Note=Colocalizes with LAMP1. {ECO:0000269|PubMed:29860631}. SUBUNIT: Homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Isoform 1 is highly expressed in testis and at moderate levels in heart (PubMed:8810348). Isoform 2 is expressed at a moderate level in brain, the cerebellum, testis, heart and olfactory epithelium (PubMed:8810348). Isoform 3 highly expressed in olfactory epithelium and at very low levels, if any, in other tissues (PubMed:8810348). In the cochlea, expressed in the inner and outer hair cells (at protein level) (PubMed:29860631). In the brain, highly expressed in the neurons of the granule layer of the cerebellum, some Purkinje cells, the central amygdaloid nucleus, and the interpolar spinal trigem nucleus and, at moderate levels, in the glomerular and external plexiform layer of the olfactory bulb as well as in parts of the caudate-putamen and olfactory tubercle (PubMed:8810348). {ECO:0000269|PubMed:29860631, ECO:0000269|PubMed:8810348}. +Q8BVF2 PDCL3_MOUSE Phosducin-like protein 3 (Viral IAP-associated factor 1) (VIAF-1) 240 27,581 Chain (1); Compositional bias (1); Modified residue (4); Region (1); Sequence conflict (2) FUNCTION: Acts as a chaperone for the angiogenic VEGF receptor KDR/VEGFR2, controlling its abundance and inhibiting its ubiquitination and degradation. Modulates the activation of caspases during apoptosis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Interacts (via thioredoxin fold region) with KDR/VEGFR2 (via juxtamembrane domain). {ECO:0000250}. +P28650 PURA1_MOUSE Adenylosuccinate synthetase isozyme 1 (AMPSase 1) (AdSS 1) (EC 6.3.4.4) (Adenylosuccinate synthetase, basic isozyme) (Adenylosuccinate synthetase, muscle isozyme) (M-type adenylosuccinate synthetase) (IMP--aspartate ligase 1) 457 50,254 Active site (2); Alternative sequence (1); Beta strand (19); Binding site (7); Chain (1); Helix (20); Metal binding (2); Nucleotide binding (4); Region (3); Turn (5) Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. FUNCTION: Component of the purine nucleotide cycle (PNC), which interconverts IMP and AMP to regulate the nucleotide levels in various tissues, and which contributes to glycolysis and ammoniagenesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000269|PubMed:12482871}. SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein. Note=Partially associated with particulate fractions. SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03126, ECO:0000269|PubMed:12004071}. TISSUE SPECIFICITY: High levels in muscle. +Q9Z0X4 PDE3A_MOUSE cGMP-inhibited 3',5'-cyclic phosphodiesterase A (EC 3.1.4.17) (Cyclic GMP-inhibited phosphodiesterase A) (CGI-PDE A) 1141 124,513 Active site (1); Chain (1); Cross-link (1); Domain (1); Metal binding (5); Modified residue (7); Transmembrane (6) TRANSMEM 62 82 Helical. {ECO:0000255}.; TRANSMEM 127 147 Helical. {ECO:0000255}.; TRANSMEM 157 177 Helical. {ECO:0000255}.; TRANSMEM 182 202 Helical. {ECO:0000255}.; TRANSMEM 207 227 Helical. {ECO:0000255}.; TRANSMEM 229 249 Helical. {ECO:0000255}. FUNCTION: Cyclic nucleotide phosphodiesterase with a dual-specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. Involved in oocyte maturation. {ECO:0000269|PubMed:11420239}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +O88502 PDE8A_MOUSE High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8A (MmPDE8) (EC 3.1.4.53) 823 93,171 Active site (1); Chain (1); Domain (3); Metal binding (5); Modified residue (4) Purine metabolism; 3',5'-cyclic AMP degradation; AMP from 3',5'-cyclic AMP: step 1/1. FUNCTION: Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. May be involved in maintaining basal levels of the cyclic nucleotide and/or in the cAMP regulation of germ cell development. Binding to RAF1 reduces RAF1 'Ser-259' inhibitory-phosphorylation and stimulates RAF1-dependent EGF-activated ERK-signaling. Protects against cell death induced by hydrogen peroxide and staurosporine. {ECO:0000250|UniProtKB:O60658}. PTM: Phosphorylated at Ser-355 by PKA under elevated cAMP conditions, this enhances catalytic activity. {ECO:0000250}. SUBUNIT: Interacts with RAF1. The interaction promotes RAF1 activity. {ECO:0000250|UniProtKB:O60658}. DOMAIN: Composed of a C-terminal catalytic domain containing two putative divalent metal sites and an N-terminal regulatory domain. TISSUE SPECIFICITY: Highest levels in testis > eye > liver > skeletal muscle > heart > 7-day embryo > kidney > ovary > brain. In the testis, expressed specifically in the seminiferous epithelium in a spatial and temporal manner. +Q5NCR9 NSRP1_MOUSE Nuclear speckle splicing regulatory protein 1 (Coiled-coil domain-containing protein 55) (Nuclear speckle-related protein 70) (NSrp70) 542 63,799 Chain (1); Coiled coil (2); Compositional bias (1); Cross-link (3); Modified residue (7); Region (1) FUNCTION: RNA-binding protein that mediates pre-mRNA alternative splicing regulation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus speckle {ECO:0000250}. Note=Colocalizes with splicing factors SRSF1 and SRSF2 in speckles. {ECO:0000250}. SUBUNIT: Interacts (via C-terminus) with SRSF1. Interacts (via C-terminus) with SRSF2 (By similarity). {ECO:0000250}. +Q99NF2 NSMF_MOUSE NMDA receptor synaptonuclear signaling and neuronal migration factor (Juxtasynaptic attractor of caldendrin on dendritic boutons protein) (Jacob protein) (Nasal embryonic luteinizing hormone-releasing hormone factor) (Nasal embryonic LHRH factor) 532 60,293 Alternative sequence (6); Chain (1); Initiator methionine (1); Lipidation (1); Modified residue (3); Motif (1); Region (1); Sequence conflict (1) FUNCTION: Couples NMDA-sensitive glutamate receptor signaling to the nucleus and triggers long-lasting changes in the cytoarchitecture of dendrites and spine synapse processes. Part of the cAMP response element-binding protein (CREB) shut-off signaling pathway. Stimulates outgrowth of olfactory axons and migration of gonadotropin-releasing hormone (GnRH) and luteinizing-hormone-releasing hormone (LHRH) neuronal cells. {ECO:0000269|PubMed:10898796}. PTM: Proteolytically processed after NMDA receptor activation. Cleaved in a calcium-dependent and calpain-sensitive manner. Calpain cleavage is essential for the translocation process from dendrites to the nucleus (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Nucleus envelope {ECO:0000250}. Nucleus membrane {ECO:0000250}. Nucleus matrix {ECO:0000250}. Cytoplasm. Cytoplasm, cell cortex {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell membrane; Peripheral membrane protein. Cell projection, dendrite {ECO:0000250}. Cell junction, synapse {ECO:0000250}. Cell junction, synapse, synaptosome {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250}. Membrane {ECO:0000250}. Note=Found on the outside of the luteinizing-hormone-releasing hormone (LHRH) cell membrane and axons projecting from the olfactory pit and epithelium. Associates with transcriptionally active chromatin regions. Detected at the nuclear membranes of CA1 neurons. Cortical cytoskeleton. Localized in proximal apical dendrites. Colocalizes with CABP1 in dendrites and dendritic spines. Myristoylation is a prerequisite for extranuclear localization. Translocates from dendrites to the nucleus during NMDA receptor-dependent long-term potentiation (LTP) induction of synaptic transmission at Schaffer collateral/CA1 synapses of hippocampal primary neurons and in a importin-dependent manner (By similarity). {ECO:0000250}. SUBUNIT: Interacts with KPNA1; the interaction occurs in a calcium-independent manner after synaptic NMDA receptor stimulation and is required for nuclear import of NSMF but is competed by CABP1. Interacts (via the central NLS-containing motif region) with CABP1 (via EF-hands 1 and 2); the interaction occurs in a calcium-dependent manner after synaptic NMDA receptor stimulation and prevents the nuclear import of NSMF. Cannot be competed by calmodulin (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Preferentially expressed in immature migratory, in comparison to postmigrating, gonadotropin-releasing hormone (GnRH) neuronal cell lines (at protein level). Expressed in adult brain and liver. In the brain, expressed in the primary pituitary gland, cortex, hippocampus, olfactory bulb and thalamus. {ECO:0000269|PubMed:10898796, ECO:0000269|PubMed:15018815, ECO:0000269|PubMed:20025934}. +Q9CWD8 NUBPL_MOUSE Iron-sulfur protein NUBPL (Nucleotide-binding protein-like) 319 34,139 Chain (1); Nucleotide binding (1); Sequence conflict (1); Transit peptide (1) FUNCTION: Required for the assembly of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I). May deliver of one or more Fe-S clusters to complex I subunits (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. +Q9R061 NUBP2_MOUSE Cytosolic Fe-S cluster assembly factor NUBP2 (Nucleotide-binding protein 2) (NBP 2) 275 29,518 Chain (1); Metal binding (2); Modified residue (1); Nucleotide binding (1) FUNCTION: Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. The NUBP1-NUBP2 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins. Negatively regulates cilium formation and structure (PubMed:23807208). {ECO:0000255|HAMAP-Rule:MF_03039, ECO:0000269|PubMed:23807208}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03039, ECO:0000269|PubMed:16638812}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03039, ECO:0000269|PubMed:16638812}. Cytoplasm {ECO:0000269|PubMed:23807208}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:23807208}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:23807208}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000269|PubMed:23807208}. Note=Enriched at the centrosomes during mitosis (By similarity). Enriched in centrioles of microtubule asters during prophase, prometaphase and telophase stages of mitosis (PubMed:23807208). Localized at centrioles and in the nucleus at interphase (PubMed:23807208). Colocalizes with nubp-1 at prometaphase (PubMed:23807208). {ECO:0000255|HAMAP-Rule:MF_03039, ECO:0000269|PubMed:23807208}. SUBUNIT: Heterotetramer of 2 NUBP1 and 2 NUBP2 chains (By similarity). Interacts with KIFC1 (PubMed:16638812). Interacts with NUBP1 (PubMed:16638812, PubMed:23807208). {ECO:0000255|HAMAP-Rule:MF_03039, ECO:0000269|PubMed:16638812, ECO:0000269|PubMed:23807208}. TISSUE SPECIFICITY: Widely expressed. +O35685 NUDC_MOUSE Nuclear migration protein nudC (Nuclear distribution protein C homolog) (Silica-induced gene 92 protein) (SIG-92) 332 38,358 Beta strand (9); Chain (1); Coiled coil (1); Domain (1); Modified residue (10); Motif (1); Turn (2) FUNCTION: Plays a role in neurogenesis and neuronal migration. Necessary for correct formation of mitotic spindles and chromosome separation during mitosis (By similarity). {ECO:0000250, ECO:0000269|PubMed:11734602}. PTM: Reversibly phosphorylated on serine residues during the M phase of the cell cycle. Phosphorylation on Ser-275 and Ser-327 is necessary for correct formation of mitotic spindles and chromosome separation during mitosis. Phosphorylated by PLK and other kinases (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Nucleus {ECO:0000250}. Note=A small proportion is nuclear, in a punctate pattern (By similarity). In a filamentous pattern adjacent to the nucleus of migrating cerebellar granule cells. Colocalizes with tubulin and dynein and with the microtubule organizing center. Distributed throughout the cytoplasm of non-migrating cells (By similarity). {ECO:0000250}. SUBUNIT: Interacts with PLK1 (By similarity). Interacts with PAFAH1B1 (PubMed:9601647). Part of a complex containing PLK1, NUDC, dynein and dynactin (PubMed:11734602). Interacts with DCDC1 (By similarity). {ECO:0000250|UniProtKB:Q9Y266, ECO:0000269|PubMed:11734602, ECO:0000269|PubMed:9601647}. TISSUE SPECIFICITY: Detected in fetal and adult brain, in particular in the ventricular zone of the embryonic forebrain and in the embryonic cortical plate. Highly expressed in brain cortex from new born and adult mice. Detected in the choroid plexus and in ependymal cells in embryonic brain. {ECO:0000269|PubMed:11734602, ECO:0000269|PubMed:9601647}. +Q9JI46 NUDT3_MOUSE Diphosphoinositol polyphosphate phosphohydrolase 1 (DIPP-1) (muDIPP1) (EC 3.6.1.52) (Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 1) (EC 3.6.1.-) (Nucleoside diphosphate-linked moiety X motif 3) (Nudix motif 3) 168 19,030 Active site (1); Binding site (3); Chain (1); Domain (1); Metal binding (4); Modified residue (1); Motif (1); Mutagenesis (1); Region (3); Sequence caution (1) FUNCTION: Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate) and [PP]2-InsP4 (bisdiphosphoinositol tetrakisphosphate), suggesting that it may play a role in signal transduction. InsP6 (inositol hexakisphophate) is not a substrate. Also able to catalyze the hydrolysis of dinucleoside oligophosphates, with Ap6A and Ap5A being the preferred substrates. The major reaction products are ADP and p4a from Ap6A and ADP and ATP from Ap5A. Also able to hydrolyze 5-phosphoribose 1-diphosphate (By similarity). Acts as a negative regulator of the ERK1/2 pathway. {ECO:0000250|UniProtKB:O95989}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q566C7}. TISSUE SPECIFICITY: Present in heart, lung, liver and spleen (at protein level). Widely expressed. {ECO:0000269|PubMed:15212765}. +Q8BG93 NUD15_MOUSE Nucleotide triphosphate diphosphatase NUDT15 (EC 3.6.1.9) (MutT homolog 2) (mMTH2) (Nucleoside diphosphate-linked moiety X motif 15) (Nudix motif 15) (Nucleoside diphosphate-linked to another moiety X hydrolase 15) (Nudix hydrolase 15) 170 19,576 Chain (1); Domain (1); Metal binding (2); Motif (1); Region (1) FUNCTION: May catalyze the hydrolysis of nucleoside triphosphates including dGTP, dTTP, dCTP, their oxidized forms like 8-oxo-dGTP and the prodrug thiopurine derivatives 6-thio-dGTP and 6-thio-GTP (PubMed:12767940). Could also catalyze the hydrolysis of some nucleoside diphosphate derivatives (By similarity). Hydrolyzes oxidized nucleosides triphosphates like 8-oxo-dGTP in vitro, but the specificity and efficiency towards these substrates are low. Therefore, the potential in vivo sanitizing role of this enzyme, that would consist in removing oxidatively damaged forms of nucleosides to prevent their incorporation into DNA, is unclear (PubMed:12767940). Through the hydrolysis of thioguanosine triphosphates may participate in the catabolism of thiopurine drugs (By similarity). May also have a role in DNA synthesis and cell cycle progression by stabilizing PCNA (By similarity). {ECO:0000250|UniProtKB:Q9NV35, ECO:0000269|PubMed:12767940}. SUBUNIT: Homodimer. Interacts with PCNA; interaction is disrupted in response to UV irradiation. {ECO:0000250|UniProtKB:Q9NV35}. +Q9JKX6 NUDT5_MOUSE ADP-sugar pyrophosphatase (EC 3.6.1.13) (8-oxo-dGDP phosphatase) (EC 3.6.1.58) (Nuclear ATP-synthesis protein NUDIX5) (EC 2.7.7.96) (Nucleoside diphosphate-linked moiety X motif 5) (Nudix motif 5) 218 23,984 Binding site (4); Chain (1); Cross-link (1); Domain (1); Metal binding (6); Modified residue (5); Motif (1); Region (1); Sequence conflict (1) FUNCTION: Enzyme that can either act as an ADP-sugar pyrophosphatase in absence of diphosphate or catalyze the synthesis of ATP in presence of diphosphate (By similarity). In absence of diphosphate, hydrolyzes with similar activities various modified nucleoside diphosphates such as ADP-ribose, ADP-mannose, ADP-glucose, 8-oxo-GDP and 8-oxo-dGDP (PubMed:10722730). Can also hydrolyze other nucleotide sugars with low activity (PubMed:10722730). In presence of diphosphate, mediates the synthesis of ATP in the nucleus by catalyzing the conversion of ADP-ribose to ATP and ribose 5-phosphate (By similarity). Nuclear ATP synthesis takes place when dephosphorylated at Thr-44 (By similarity). Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming (By similarity). Does not play a role in U8 snoRNA decapping activity (PubMed:21070968). Binds U8 snoRNA (PubMed:21070968). {ECO:0000250|UniProtKB:Q9UKK9, ECO:0000269|PubMed:10722730, ECO:0000269|PubMed:21070968}. PTM: Phosphorylation at Thr-44 is required for homodimer stability; dephosphorylation results in destabilization of the homodimer. Dephosphorylation at Thr-44 promotes the ATP-synthesis activity. {ECO:0000250|UniProtKB:Q9UKK9}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UKK9}. SUBUNIT: Homodimer. Interacts with PARG. {ECO:0000250|UniProtKB:Q9UKK9}. TISSUE SPECIFICITY: Widely expressed. Most abundant in liver. {ECO:0000269|PubMed:10722730}. +O08600 NUCG_MOUSE Endonuclease G, mitochondrial (Endo G) (EC 3.1.30.-) 294 32,191 Active site (1); Chain (1); Erroneous initiation (1); Metal binding (1); Transit peptide (1) FUNCTION: Cleaves DNA at double-stranded (DG)n.(DC)n and at single-stranded (DC)n tracts. In addition to deoxyribonuclease activities, also has ribonuclease (RNase) and RNase H activities. Capable of generating the RNA primers required by DNA polymerase gamma to initiate replication of mitochondrial DNA (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion. SUBUNIT: Homodimer. {ECO:0000250}. +E9Q7G0 NUMA1_MOUSE Nuclear mitotic apparatus protein 1 (Nuclear mitotic apparatus protein) (NuMA protein) 2094 235,630 Chain (1); Coiled coil (1); Cross-link (4); Glycosylation (1); Modified residue (48); Motif (2); Region (7); Sequence conflict (1) FUNCTION: Microtubule (MT)-binding protein that plays a role in the formation and maintenance of the spindle poles and the alignement and the segregation of chromosomes during mitotic cell division (PubMed:19255246, PubMed:24109598, PubMed:26765568). Functions to tether the minus ends of MTs at the spindle poles, which is critical for the establishment and maintenance of the spindle poles (PubMed:26765568). Plays a role in the establishment of the mitotic spindle orientation during metaphase and elongation during anaphase in a dynein-dynactin-dependent manner (PubMed:26765568). In metaphase, part of a ternary complex composed of GPSM2 and G(i) alpha proteins, that regulates the recruitment and anchorage of the dynein-dynactin complex in the mitotic cell cortex regions situated above the two spindle poles, and hence regulates the correct oritentation of the mitotic spindle (PubMed:24109598, PubMed:26765568). During anaphase, mediates the recruitment and accumulation of the dynein-dynactin complex at the cell membrane of the polar cortical region through direct association with phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), and hence participates in the regulation of the spindle elongation and chromosome segregation. Binds also to other polyanionic phosphoinositides, such as phosphatidylinositol 3-phosphate (PIP), lysophosphatidic acid (LPA) and phosphatidylinositol triphosphate (PIP3), in vitro (By similarity). Also required for proper orientation of the mitotic spindle during asymmetric cell divisions (PubMed:26765568). Plays a role in mitotic MT aster assembly. Involved in anastral spindle assembly. Positively regulates TNKS protein localization to spindle poles in mitosis. Highly abundant component of the nuclear matrix where it may serve a non-mitotic structural role, occupies the majority of the nuclear volume (By similarity). Required for epidermal differentiation and hair follicle morphogenesis (PubMed:26765568). {ECO:0000250|UniProtKB:Q14980, ECO:0000269|PubMed:19255246, ECO:0000269|PubMed:24109598, ECO:0000269|PubMed:26765568}. PTM: Phosphorylation and dephosphorylation on Thr-2037 regulates the extent of cortical NUMA1 and the dynein-dynactin complex localization during mitotic metaphase and anaphase. In metaphase, phosphorylation on Thr-2037 occurs in a kinase CDK1-dependent manner; this phosphorylation maintains low levels of cortical dynein-dynactin complex at metaphase, and hence proper spindle positioning. In anaphase, dephosphorylated on Thr-2037 by phosphatase PPP2CA; this dephosphorylation stimulates its membrane association and with the dynein-dynactin complex its enrichment at the cell cortex, and hence robust spindle elongation. Probably also phosphorylated on Thr-1997 and Ser-2069 by CDK1; these phosphorylations may regulate its cell cortex recruitment during metaphase and anaphase. Phosphorylated on Ser-1751, Ser-1754, Ser-1771 and Ser-1816 by PLK1; these phosphorylations induce cortical dynein-dynactin complex dissociation from the NUMA1-GPSM2 complex and negatively regulates cortical dynein-dynactin complex localization. {ECO:0000250|UniProtKB:Q14980}.; PTM: ADP-ribosylated by TNKS at the onset of mitosis; ADP-ribosylation is not required for its localization to spindle poles. {ECO:0000250|UniProtKB:Q14980}.; PTM: O-glycosylated during cytokinesis at sites identical or close to phosphorylation sites, this interferes with the phosphorylation status. {ECO:0000250|UniProtKB:Q14980}.; PTM: Ubiquitinated with 'Lys-63'-linked polyubiquitin chains. Deubiquitination by the BRISC complex is important for the incorporation of NUMA1 into mitotic spindle poles and normal spindle pole function, probably by modulating interactions between NUMA1, dynein-dynactin complex and importin-beta. {ECO:0000250|UniProtKB:Q14980}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19255246}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q14980}. Nucleus matrix {ECO:0000250|UniProtKB:Q14980}. Chromosome {ECO:0000250|UniProtKB:Q14980}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:26765568}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q14980}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:19255246, ECO:0000269|PubMed:24109598, ECO:0000269|PubMed:26765568}. Cytoplasm, cell cortex {ECO:0000269|PubMed:24109598, ECO:0000269|PubMed:26765568, ECO:0000269|PubMed:26766442}. Cell membrane {ECO:0000250|UniProtKB:Q14980}; Lipid-anchor {ECO:0000250|UniProtKB:Q14980}; Cytoplasmic side {ECO:0000250|UniProtKB:Q14980}. Lateral cell membrane {ECO:0000269|PubMed:26766442}. Note=Mitotic cell cycle-dependent shuttling protein that relocalizes from the interphase nucleus to the spindle poles and cell cortex (PubMed:19255246, PubMed:24109598, PubMed:26765568). In interphase, resides in the nuclear matrix (PubMed:19255246). In prophase, restricted to the interchromatin or condensed chromosome space. In prometaphase, after nuclear envelope disassembly, forms aggregates both in the spindle midzone and at duplicated centrosomes and astral microtubules (MTs) of the bipolar spindle apparatus. Translocates from the spindle midzone towards the spindle poles along spindle fibers in a MT- and dynein-dynactin-dependent manner until the anaphase onset (By similarity). In metaphase, recruited to the polar cortical region in a GPSM2- and GNAI1-dependent manner (PubMed:24109598). Excluded from the metaphase equatorial cortical region in a RanGTP-dependent manner. Phosphorylation on Thr-2037 by CDK1 results in its localization at spindle poles in metaphase, but not at the cell cortex (By similarity). In anaphase, recruited and anchored at the cell membrane of the polar cortical region in a EPB41-, EPB41L2-, phosphatidylinositol-dependent and GPSM2- and G(i) alpha proteins-independent manner (PubMed:24109598). Excluded from the anaphase equatorial region of the cell cortex in a RACGAP1- and KIF23-dependent and RanGTP-independent manner. Associated with astral MTs emanating from the spindle poles during anaphase. Nonphosphorylated Thr-2037 localizes at the cell cortex, weakly during metaphase and more prominently during anaphase in a phosphatase PPP2CA-dependent manner. As mitosis progresses it reassociates with telophase chromosomes very early during nuclear reformation, before substantial accumulation of lamins on chromosomal surfaces is evident. Localizes to the tips of cortical MTs in prometaphase (By similarity). Localizes along MTs and specifically to both MT plus and minus ends (PubMed:26765568). Accumulates also at MT tips near the cell periphery. Colocalizes with GPSM2 at mitotic spindle poles during mitosis. Colocalizes with SPAG5 at mitotic spindle at prometaphase and at mitotic spindle poles at metaphase and anaphase. Colocalizes with ABRO1 at mitotic spindle poles. Colocalized with TNKS from prophase through to anaphase in mitosis. Colocalizes with tubulin alpha. CCSAP is essential for its centrosomal localization (By similarity). In horizontally retinal progenitor dividing cells, localized to the lateral cortical region (PubMed:26766442). {ECO:0000250|UniProtKB:Q14980, ECO:0000269|PubMed:19255246, ECO:0000269|PubMed:24109598, ECO:0000269|PubMed:26765568, ECO:0000269|PubMed:26766442}. SUBUNIT: Homodimer. Also forms multiarm oligomers by association of C-terminal tail domains, oligomers may further assemble to form a hexagonal nuclear lattice-like network. Associates with the dynein-dynactin complex; this association promotes the transport and accumulation of NUMA1 at the mitotic spindle poles that is inhibited by the BRISC complex in a PLK1-dependent manner. Part of a spindle orientation complex at least composed of GNAI1, GPSM2 and NUMA1 (By similarity). Interacts (via C-terminus) with microtubules (MTs); this interaction is direct and promotes both MT bundle formation and stability in a dynein-dynactin complex- and CDK1-independent manner. Interacts with EPB41 and EPB41L2; these interactions are negatively regulated by CDK1 during metaphase and are important for anaphase-specific localization of NUMA1 in symmetrically dividing cells. Interacts (via C-terminus) with GPSM2 (via TPR repeats); this interaction is direct, prevented by competitive binding of INSC, is inhibited in a PLK1-dependent manner, blocks the association of NUMA1 with MTs and inhibits NUMA1-induced MT bundle formation, prevents the association of NUMA1 with SPAG5, induces mitotic spindle pole localization of GPSM2, both metaphase cell cortex localization of NUMA1 and mitotic spindle organization. Does not interact with GPSM2 during anaphase. Interacts (via C-terminus) with the nuclear importin alpha/importin beta receptor; this interaction is inhibited by RanGTP. Interacts (via C-terminus) with KPNB1; this interaction is inhibited by RanGTP and the BRISC complex. Interacts with ABRAXAS2 and the BRISC complex; these interactions regulate mitotic spindle assembly. Interacts (via N-terminal end of the coiled-coil domain) with RAE1; this interaction promotes mitotic spindle formation. Interacts (via C-terminus) with SPAG5 (via C-terminus); this interaction promotes the recruitment of SPAG5 to the MTs at spindle poles in a dynein-dynactin-dependent manner and regulates mitotic spindle organization and proper chromosome alignment during mitosis. Interacts with TNKS; this interaction occurs at the onset of mitosis. Interacts with TNKS2. Interacts with tubulin. {ECO:0000250|UniProtKB:Q14980}. DOMAIN: The C-terminal tubulin-binding domain mediates direct binding to microtubules, independently of dynein-dynactin complex, and induces their bundling and stabilization. The 4.1-binding domain is necessary for its cortical stability and spindle orientation. {ECO:0000250|UniProtKB:Q14980}. TISSUE SPECIFICITY: Expressed in testis, speen, liver, lung, spinal cord and brain. Expressed in Purkinje neurons (at protein level) (PubMed:19255246). {ECO:0000269|PubMed:19255246}. +Q99P69 NUF2_MOUSE Kinetochore protein Nuf2 (Cell division cycle-associated protein 1) 463 54,594 Alternative sequence (2); Chain (1); Coiled coil (2); Frameshift (1); Modified residue (2); Region (2); Sequence conflict (7) FUNCTION: Acts as a component of the essential kinetochore-associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity. Required for kinetochore integrity and the organization of stable microtubule binding sites in the outer plate of the kinetochore. The NDC80 complex synergistically enhances the affinity of the SKA1 complex for microtubules and may allow the NDC80 complex to track depolymerizing microtubules. {ECO:0000250|UniProtKB:Q9BZD4}. PTM: Can be phosphorylated by AURKA and AURKB. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Note=Localizes to kinetochores from late prophase to anaphase. Localizes specifically to the outer plate of the kinetochore (By similarity). {ECO:0000250}. SUBUNIT: Component of the NDC80 complex, which consists of NDC80/HEC1, CDCA1, SPBC24 and SPBC25. The NDC80 complex is formed by two subcomplexes composed of NDC80/HEC1-CDCA1 and SPBC24-SPBC25. Each subcomplex is formed by parallel interactions through the coiled-coil domains of individual subunits. Formation of a tetrameric complex is mediated by interactions between the C-terminal regions of both subunits of the NDC80/HEC1-CDCA1 subcomplex and the N-terminal regions of both subunits of the SPBC24-SPBC25 complex. The tetrameric NDC80 complex has an elongated rod-like structure with globular domains at either end. May interact with AURKB/Aurora-B (By similarity). {ECO:0000250}. +P49722 PSA2_MOUSE Proteasome subunit alpha type-2 (EC 3.4.25.1) (Macropain subunit C3) (Multicatalytic endopeptidase complex subunit C3) (Proteasome component C3) 234 25,927 Beta strand (12); Chain (1); Helix (7); Initiator methionine (1); Modified residue (10); Sequence conflict (1); Turn (2) FUNCTION: Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). {ECO:0000269|PubMed:16581775, ECO:0000269|PubMed:22341445}. PTM: Phosphorylated on tyrosine residues; which may be important for nuclear import. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22078707}. Nucleus {ECO:0000269|PubMed:22078707}. Note=Colocalizes with TRIM5 in cytoplasmic bodies. SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is a barrel-shaped complex made of 28 subunits that are arranged in four stacked rings. The two outer rings are each formed by seven alpha subunits, and the two inner rings are formed by seven beta subunits. The proteolytic activity is exerted by three beta-subunits PSMB5, PSMB6 and PSMB7. {ECO:0000269|PubMed:16857966, ECO:0000269|PubMed:22341445}. TISSUE SPECIFICITY: Detected in liver (at protein level). {ECO:0000269|PubMed:22341445}. +Q6P3A8 ODBB_MOUSE 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial (EC 1.2.4.4) (Branched-chain alpha-keto acid dehydrogenase E1 component beta chain) (BCKDE1B) (BCKDH E1-beta) 390 42,880 Alternative sequence (1); Chain (1); Modified residue (2); Transit peptide (1) FUNCTION: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). SUBCELLULAR LOCATION: Mitochondrion matrix. SUBUNIT: Heterotetramer of 2 alpha and 2 beta chains. {ECO:0000250}. +Q920N1 ODF3A_MOUSE Outer dense fiber protein 3 (Outer dense fiber of sperm tails protein 3) (Sperm tail protein SHIPPO 1) 254 27,650 Chain (1); Repeat (2); Sequence conflict (1) FUNCTION: Outer dense fibers are filamentous structures located on the outside of the axoneme in the midpiece and principal piece of the mammalian sperm tail. May help to maintain the passive elastic structures and elastic recoil of the sperm tail. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11870087}. Note=Expressed in the cytoplasmic lobe of spermatids. TISSUE SPECIFICITY: Testis-specific (at protein level). Expression restricted to the germ cell fraction, absent in somatic cell fractions such as Sertoli and Leydig cells. Expression detected in the third week postpartum (23 days) after haploid germ cells developed, expression increased with age. Expressed in the tails of elongated spermatids sticking out toward the tubular lumen, and in cytoplasmic droplets still attached to the spermatid tail membrane. Expressed in the tails of mature sperm, from the connecting piece proximal to the head, along the middle and principal pieces, down to the distal end piece. {ECO:0000269|PubMed:11870087, ECO:0000269|PubMed:16141072}. +Q9D0J8 PTMS_MOUSE Parathymosin 101 11,430 Chain (1); Compositional bias (1); Initiator methionine (1); Modified residue (8) FUNCTION: Parathymosin may mediate immune function by blocking the effect of prothymosin alpha which confers resistance to certain opportunistic infections. {ECO:0000250}. +Q3B7Z2 OSBP1_MOUSE Oxysterol-binding protein 1 805 88,797 Alternative sequence (2); Binding site (1); Chain (1); Coiled coil (2); Domain (1); Initiator methionine (1); Modified residue (15); Motif (1); Region (4); Sequence caution (2) FUNCTION: Lipid transporter involved in lipid countertransport between the Golgi complex and membranes of the endoplasmic reticulum: specifically exchanges sterol with phosphatidylinositol 4-phosphate (PI4P), delivering sterol to the Golgi in exchange for PI4P, which is degraded by the SAC1/SACM1L phosphatase in the endoplasmic reticulum. Binds cholesterol and a range of oxysterols including 25-hydroxycholesterol. Cholesterol binding promotes the formation of a complex with PP2A and a tyrosine phosphatase which dephosphorylates ERK1/2, whereas 25-hydroxycholesterol causes its disassembly. Regulates cholesterol efflux by decreasing ABCA1 stability. {ECO:0000250|UniProtKB:P22059}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P22059}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P22059}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P22059}; Peripheral membrane protein {ECO:0000250|UniProtKB:P22059}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P22059}; Peripheral membrane protein {ECO:0000250|UniProtKB:P22059}. Note=Predominantly cytosolic. {ECO:0000250|UniProtKB:P22059}. SUBUNIT: Homodimer or homotrimer. Interacts (via FFAT motif) with VAPA. Interacts (via C-terminus) with RELCH (via the third HEAT repeat) (PubMed:29514919). Found in a complex composed of RELCH, OSBP1 and RAB11A (PubMed:29514919). {ECO:0000250|UniProtKB:P22059, ECO:0000269|PubMed:29514919}. DOMAIN: The FFAT motif is required for interaction with VATA and proper localization of the protein. {ECO:0000250|UniProtKB:P22059}.; DOMAIN: The PH and the Ala/Gly-rich domains control cholesterol binding without affecting 25-hydroxycholesterol binding. {ECO:0000250|UniProtKB:P16258}.; DOMAIN: The second coiled-coil domain is required for interaction with the tyrosine phosphatase. {ECO:0000250|UniProtKB:P16258}. +S4R1M9 OSB10_MOUSE Oxysterol-binding protein-related protein 10 (ORP-10) (OSBP-related protein 10) 766 83,856 Binding site (5); Chain (1); Domain (1); Modified residue (10); Region (4) FUNCTION: Probable lipid transporter involved in lipid countertransport between the endoplasmic reticulum and the plasma membrane. Its ability to bind phosphatidylserine, suggests that it specifically exchanges phosphatidylserine with phosphatidylinositol 4-phosphate (PI4P), delivering phosphatidylserine to the plasma membrane in exchange for PI4P. Plays a role in negative regulation of lipid biosynthesis. Negatively regulates APOB secretion from hepatocytes. Binds cholesterol and acidic phospholipids. Also binds 25-hydroxycholesterol. Binds phosphatidylserine. {ECO:0000250|UniProtKB:Q9BXB5}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9BXB5}. Note=Associates with microtubules. {ECO:0000250|UniProtKB:Q9BXB5}. SUBUNIT: Interacts with OSBPL9. Interacts with DIAPH1. {ECO:0000250|UniProtKB:Q9BXB5}. DOMAIN: The C-terminal region binds cholesterol, 25-hydroxysterol and acidic phospholipids and is required for localization to microtubules. {ECO:0000250|UniProtKB:Q9BXB5}.; DOMAIN: The PH domain selectively interacts with phosphatidylinositol-4-phosphate. {ECO:0000250|UniProtKB:Q9BXB5}. +P35831 PTN12_MOUSE Tyrosine-protein phosphatase non-receptor type 12 (EC 3.1.3.48) (MPTP-PEST) (Protein-tyrosine phosphatase P19) (P19-PTP) 775 86,526 Active site (1); Binding site (2); Chain (1); Domain (1); Modified residue (18); Region (2); Sequence conflict (9) FUNCTION: Dephosphorylates a range of proteins, and thereby regulates cellular signaling cascades (PubMed:17070019). Dephosphorylates cellular tyrosine kinases, such as ERBB2 and PTK2B/PYK2, and thereby regulates signaling via ERBB2 and PTK2B/PYK2. Selectively dephosphorylates ERBB2 phosphorylated at 'Tyr-1112', 'Tyr-1196', and/or 'Tyr-1248' (By similarity). {ECO:0000250|UniProtKB:Q05209, ECO:0000269|PubMed:17070019}. PTM: Phosphorylated by STK24/MST3 and this results in inhibition of its activity. {ECO:0000250|UniProtKB:Q05209}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12674328, ECO:0000269|PubMed:7772023}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q05209}. Cell projection, podosome {ECO:0000269|PubMed:12674328}. Note=Partial translocation to focal adhesion sites might be mediated by interaction with SORBS2. {ECO:0000250|UniProtKB:Q05209}. SUBUNIT: Interacts with PSTPIP1 and TGFB1I1 (PubMed:10092676, PubMed:11711533). Interacts with PTK2B/PYK2 (PubMed:12674328). Interacts with LPXN (PubMed:12674328, PubMed:15786712). Interacts with SORBS2; this interaction greatly enhances WASF1 dephosphorylation and might mediate partial translocation to focal adhesion sites (By similarity). {ECO:0000250|UniProtKB:Q05209, ECO:0000269|PubMed:10092676, ECO:0000269|PubMed:11711533, ECO:0000269|PubMed:12674328, ECO:0000269|PubMed:15786712}. +Q9ER64 OSBL5_MOUSE Oxysterol-binding protein-related protein 5 (ORP-5) (OSBP-related protein 5) (Oxysterol-binding protein homolog 1) 874 98,922 Binding site (5); Chain (1); Coiled coil (1); Domain (1); Erroneous initiation (2); Modified residue (3); Region (4); Sequence conflict (2); Transmembrane (1) TRANSMEM 855 873 Helical. {ECO:0000255}. FUNCTION: Lipid transporter involved in lipid countertransport between the endoplasmic reticulum and the plasma membrane: specifically exchanges phosphatidylserine with phosphatidylinositol 4-phosphate (PI4P), delivering phosphatidylserine to the plasma membrane in exchange for PI4P, which is degraded by the SAC1/SACM1L phosphatase in the endoplasmic reticulum. Binds phosphatidylserine and PI4P in a mutually exclusive manner. May cooperate with NPC1 to mediate the exit of cholesterol from endosomes/lysosomes. Binds 25-hydroxycholesterol and cholesterol. {ECO:0000250|UniProtKB:Q9H0X9}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9H0X9}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9H0X9}. Note=Localizes to endoplasmic reticulum-plasma membrane contact sites (EPCS). Localizes to the cortical endoplasmic reticulum at the EPCS. {ECO:0000250|UniProtKB:Q9H0X9}. +Q6PEB4 OSGP2_MOUSE Probable tRNA N6-adenosine threonylcarbamoyltransferase, mitochondrial (EC 2.3.1.234) (N6-L-threonylcarbamoyladenine synthase) (t(6)A synthase) (O-sialoglycoprotein endopeptidase-like protein 1) (t(6)A37 threonylcarbamoyladenosine biosynthesis protein Osgepl1) (tRNA threonylcarbamoyladenosine biosynthesis protein Osgepl1) 414 44,928 Alternative sequence (2); Binding site (4); Chain (1); Metal binding (3); Modified residue (1); Region (2); Sequence conflict (5); Transit peptide (1) FUNCTION: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in mitochondrial tRNAs that read codons beginning with adenine. Probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Involved in mitochondrial genome maintenance. {ECO:0000255|HAMAP-Rule:MF_03179}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03179}. SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03179}. +O70458 OSMR_MOUSE Oncostatin-M-specific receptor subunit beta (Interleukin-31 receptor subunit beta) (IL-31 receptor subunit beta) (IL-31R subunit beta) (IL-31R-beta) (IL-31RB) 971 110,229 Alternative sequence (1); Chain (1); Disulfide bond (1); Domain (4); Glycosylation (14); Motif (2); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 738 758 Helical. {ECO:0000255}. TOPO_DOM 24 737 Extracellular. {ECO:0000255}.; TOPO_DOM 759 971 Cytoplasmic. {ECO:0000255}. FUNCTION: Associates with IL31RA to form the IL31 receptor (PubMed:9920829). Binds IL31 to activate STAT3 and possibly STAT1 and STAT5 (By similarity). Capable of transducing OSM-specific signaling events (By similarity). {ECO:0000250|UniProtKB:Q99650, ECO:0000269|PubMed:9920829}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Heterodimer composed of OSMR and IL6ST (type II OSM receptor). Heterodimer with IL31RA to form the IL31 receptor. {ECO:0000269|PubMed:9584176, ECO:0000269|PubMed:9920829}. DOMAIN: The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding. {ECO:0000250}.; DOMAIN: The box 1 motif is required for JAK interaction and/or activation. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed (PubMed:9584176). Expressed at highest levels in the lung, heart, thymus and spleen (PubMed:9920829). Expressed in dorsal root ganglia (PubMed:25381841). {ECO:0000269|PubMed:25381841, ECO:0000269|PubMed:9584176, ECO:0000269|PubMed:9920829}. +P29352 PTN22_MOUSE Tyrosine-protein phosphatase non-receptor type 22 (EC 3.1.3.48) (Hematopoietic cell protein-tyrosine phosphatase 70Z-PEP) (PEST-domain phosphatase) (PEP) 802 89,714 Active site (1); Binding site (2); Chain (1); Domain (1); Helix (1); Modified residue (5); Region (2); Sequence conflict (2) FUNCTION: Acts as negative regulator of T-cell receptor (TCR) signaling by direct dephosphorylation of the Src family kinases LCK and FYN, ITAMs of the TCRz/CD3 complex, as well as ZAP70, VAV, VCP and other key signaling molecules (By similarity). Associates with and probably dephosphorylates CBL (By similarity). Dephosphorylates LCK at its activating 'Tyr-394' residue (By similarity). Dephosphorylates ZAP70 at its activating 'Tyr-492' residue (By similarity). Dephosphorylates the immune system activator SKAP2 (By similarity). Positively regulates toll-like receptor (TLR)-induced type 1 interferon production (PubMed:23871208). Promotes host antiviral responses mediated by type 1 interferon (PubMed:23871208). Regulates NOD2-induced pro-inflammatory cytokine secretion and autophagy (PubMed:23991106). {ECO:0000250|UniProtKB:Q9Y2R2, ECO:0000269|PubMed:23871208, ECO:0000269|PubMed:23991106}. PTM: Phosphorylation on Ser-35 by PKC/PRKCD abrogates its ability to dephosphorylate and inactivate the SRC family kinases. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8890164}. SUBUNIT: Interacts with CBL (By similarity). Interacts with CSK (PubMed:8890164, PubMed:11685249). Interacts with LPXN (PubMed:15786712). Interacts with TRAF3 (via MATH domain); the interaction promotes TRAF3 polyubiquitination (PubMed:23871208). {ECO:0000250|UniProtKB:Q9Y2R2, ECO:0000269|PubMed:11685249, ECO:0000269|PubMed:15786712, ECO:0000269|PubMed:23871208, ECO:0000269|PubMed:8890164}. TISSUE SPECIFICITY: Spleen, thymus, lymph node and bone marrow. +Q91ZD1 OSR2_MOUSE Protein odd-skipped-related 2 312 35,454 Alternative sequence (1); Beta strand (3); Chain (1); Helix (4); Sequence conflict (1); Zinc finger (5) SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q99LX8 OST4_MOUSE Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 4 37 4,193 Chain (1); Topological domain (2); Transmembrane (1) TRANSMEM 5 25 Helical. {ECO:0000255}. TOPO_DOM 1 4 Lumenal. {ECO:0000255}.; TOPO_DOM 26 37 Cytoplasmic. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. Specifically involved in maintaining stability of STT3A-containing OST complexes. {ECO:0000250|UniProtKB:P0C6T2}. SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:P0C6T2}. Endoplasmic reticulum membrane; Single-pass type III membrane protein {ECO:0000305}. SUBUNIT: Component of the oligosaccharyltransferase (OST) complex. OST exists in two different complex forms which contain common core subunits RPN1, RPN2, OST48, OST4, DAD1 and TMEM258, either STT3A or STT3B as catalytic subunits, and form-specific accessory subunits (By similarity). STT3A complex assembly occurs through the formation of 3 subcomplexes. Subcomplex 1 contains RPN1 and TMEM258, subcomplex 2 contains the STT3A-specific subunits STT3A, DC2/OSTC, and KCP2 as well as the core subunit OST4, and subcomplex 3 contains RPN2, DAD1, and OST48. The STT3A complex can form stable complexes with the Sec61 complex or with both the Sec61 and TRAP complexes (By similarity). {ECO:0000250|UniProtKB:P0C6T2, ECO:0000250|UniProtKB:P0CU66}. +Q80WK2 OSTB_MOUSE Organic solute transporter subunit beta (OST-beta) (Solute carrier family 51 subunit beta) 128 14,684 Chain (1); Erroneous termination (1); Modified residue (1); Mutagenesis (5); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 31 53 Helical. {ECO:0000255}. TOPO_DOM 1 30 Extracellular. {ECO:0000255}.; TOPO_DOM 54 128 Cytoplasmic. {ECO:0000255}. FUNCTION: Essential component of the Ost-alpha/Ost-beta complex, a heterodimer that acts as the intestinal basolateral transporter responsible for bile acid export from enterocytes into portal blood. Efficiently transports the major species of bile acids. Modulates SLC51A glycosylation, membrane trafficking and stability activities. {ECO:0000269|PubMed:15563450, ECO:0000269|PubMed:22535958}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15563450, ECO:0000269|PubMed:17650074, ECO:0000269|PubMed:22535958}; Single-pass membrane protein {ECO:0000269|PubMed:15563450, ECO:0000269|PubMed:17650074, ECO:0000269|PubMed:22535958}. Note=Mainly restricted to the lateral and basal membranes of ileal enterocytes. SUBUNIT: Interacts with SLC51A. The Ost-alpha/Ost-beta complex is a heterodimer composed of alpha (SLC51A) and beta (SLC51B) subunit; induces the transport of SLC51A from the reticulum endoplasmic to the plasma membrane. {ECO:0000269|PubMed:17650074}. DOMAIN: The transmembrane domain (TM) is the major site of interaction with SLC51A. The extracellular-membrane interface is absolutely required for transport activity. The intracellular-membrane interface is necessary for establishing the correct membrane orientation that is essential for the heterodimer Ost-alpha/Ost-beta complex formation and transport activity at the cell membrane surface. TISSUE SPECIFICITY: Present at high level in ileum. In ileum, it is restricted to the apical domain on the mature villus enterocytes with little detectable expression in the goblet cells or crypt enterocytes (at protein level). Expressed in kidney but not in heart, brain, liver, spleen, embryo, lung, thymus, ovary nor testis. {ECO:0000269|PubMed:15563450}. +Q8BUM3 PTN7_MOUSE Tyrosine-protein phosphatase non-receptor type 7 (EC 3.1.3.48) (Hematopoietic protein-tyrosine phosphatase) (HEPTP) 359 40,351 Active site (1); Binding site (2); Chain (1); Domain (1); Modified residue (5); Region (2) FUNCTION: May play a role in the regulation of T and B-lymphocyte development and signal transduction. {ECO:0000250}. PTM: Oxidized at active site cysteine. Treatment with pervanadate (vanadate and H(2)O(2)) or with antigen enhanced oxidation of active site cysteine. {ECO:0000269|PubMed:20157115}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20157115}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:20157115}. Note=Oxidized form is preferentially associated with actin cytoskeleton. TISSUE SPECIFICITY: Expressed in bone marrow-derived mast cells. {ECO:0000269|PubMed:20157115}. +O35239 PTN9_MOUSE Tyrosine-protein phosphatase non-receptor type 9 (EC 3.1.3.48) (Protein-tyrosine phosphatase MEG2) (PTPase MEG2) 593 67,970 Active site (1); Chain (1); Domain (2); Modified residue (1); Sequence conflict (13) FUNCTION: Protein-tyrosine phosphatase that could participate in the transfer of hydrophobic ligands or in functions of the Golgi apparatus. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. +P63089 PTN_MOUSE Pleiotrophin (PTN) (Heparin-binding brain mitogen) (HBBM) (Heparin-binding growth factor 8) (HBGF-8) (Heparin-binding growth-associated molecule) (HB-GAM) (Heparin-binding neutrophic factor) (HBNF) (Osteoblast-specific factor 1) (OSF-1) 168 18,869 Chain (1); Disulfide bond (5); Region (3); Signal peptide (1) FUNCTION: Secreted growth factor that induces neurite outgrowth and which is mitogenic for fibroblasts, epithelial, and endothelial cells. Binds anaplastic lymphoma kinase (ALK) which induces MAPK pathway activation, an important step in the anti-apoptotic signaling of PTN and regulation of cell proliferation. Binds to cell-surface target proteins via their chondroitin sulfate groups. Down-regulates PTPRZ1 activity. {ECO:0000250|UniProtKB:P21246}. PTM: Phosphorylated by NEK6. {ECO:0000250|UniProtKB:P21246}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P21246}. SUBUNIT: Interacts with ALK and NEK6. Interacts with PTPRZ1 (probably via chondroitin sulfate groups). {ECO:0000250|UniProtKB:P21246}. TISSUE SPECIFICITY: Osteoblast and brain. {ECO:0000269|PubMed:1701634, ECO:0000269|PubMed:1768439}. +Q62422 OSTF1_MOUSE Osteoclast-stimulating factor 1 (SH3 domain protein 3) 215 23,783 Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (4); Repeat (3) FUNCTION: Induces bone resorption, acting probably through a signaling cascade which results in the secretion of factor(s) enhancing osteoclast formation and activity. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. SUBUNIT: Interacts with C-SRC and SMN1. Interacts with FASLG (By similarity). {ECO:0000250}. DOMAIN: The SH3 domain mediates interaction with SMN1. {ECO:0000250}. +Q8BGT0 OSTM1_MOUSE Osteopetrosis-associated transmembrane protein 1 (Chloride channel 7 beta subunit) (Grey-lethal protein) 338 38,000 Chain (1); Glycosylation (10); Modified residue (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 289 309 Helical. {ECO:0000255}. TOPO_DOM 35 288 Lumenal. {ECO:0000255}.; TOPO_DOM 310 338 Cytoplasmic. {ECO:0000255}. FUNCTION: Required for osteoclast and melanocyte maturation and function. {ECO:0000269|PubMed:12627228, ECO:0000269|PubMed:16525474}. PTM: Undergoes proteolytic cleavage in the luminal domain, the cleaved fragments might be linked by disulfide bonds with the remnant of the protein. {ECO:0000269|PubMed:16525474}.; PTM: Highly N-glycosylated. {ECO:0000269|PubMed:16525474}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:12627228, ECO:0000269|PubMed:16525474}; Single-pass type I membrane protein {ECO:0000269|PubMed:12627228, ECO:0000269|PubMed:16525474}. Note=Requires CLCN7 to travel to lysosomes. SUBUNIT: Chloride channel 7 are heteromers of alpha (CLCN7) and beta (OSTM1) subunits. {ECO:0000269|PubMed:16525474}. TISSUE SPECIFICITY: Expressed primarily in osteoclasts and melanocytes as well as brain, kidney and spleen. Found at lower levels in the thymus, testis, heart and liver. {ECO:0000269|PubMed:12627228}. DISEASE: Note=Defects in Ostm1 are the cause of the spontaneous gray-lethal (gl) mutant, which is responsible for a coat color defect and for the development of the most severe autosomal recessive form of osteopetrosis. Osteopetrosis is a rare genetic disease characterized by abnormally dense bone, due to defective resorption of immature bone. The disorder occurs in two forms: a severe autosomal recessive form occurring in utero, infancy, or childhood, and a benign autosomal dominant form occurring in adolescence or adulthood. {ECO:0000269|PubMed:12627228}. +P61364 OSTN_MOUSE Osteocrin (Musclin) [Cleaved into: Processed Osteocrin] 130 14,438 Chain (1); Modified residue (1); Mutagenesis (2); Peptide (1); Signal peptide (1) FUNCTION: Hormone that acts as a ligand for natriuretic peptide receptor NPR3/NPR-C and promotes bone growth and physical endurance in muscle. Acts as a regulator of osteoblast differentiation and bone growth by binding to natriuretic peptide receptor NPR3/NPR-C, thereby preventing binding between NPR3/NPR-C and natriuretic peptides, leading to increase cGMP production (PubMed:14523025, PubMed:17951249). Required to enhance physical endurance: induced following physical exercise in muscle and promotes cGMP production, probably by interacting with NPR3/NPR-C (PubMed:26668395). May act as an autocrine and paracrine factor linked to glucose metabolism in skeletal muscle (PubMed:15044443). {ECO:0000269|PubMed:14523025, ECO:0000269|PubMed:15044443, ECO:0000269|PubMed:17951249, ECO:0000269|PubMed:26668395}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14523025, ECO:0000269|PubMed:15044443, ECO:0000269|PubMed:26668395}. SUBUNIT: Interacts with NPR3. {ECO:0000269|PubMed:17951249}. TISSUE SPECIFICITY: Expressed in skeletal muscle and to a much lesser extent in bone, brown adipose tissue, spleen and testis (PubMed:14523025, PubMed:15044443, PubMed:26668395). Not expressed in neurons (PubMed:27830782). {ECO:0000269|PubMed:14523025, ECO:0000269|PubMed:15044443, ECO:0000269|PubMed:26668395, ECO:0000269|PubMed:27830782}. +P10923 OSTP_MOUSE Osteopontin (2AR) (Bone sialoprotein 1) (Calcium oxalate crystal growth inhibitor protein) (Early T-lymphocyte activation 1 protein) (Minopontin) (Secreted phosphoprotein 1) (SPP-1) 294 32,459 Chain (1); Erroneous initiation (1); Glycosylation (3); Modified residue (36); Motif (1); Sequence conflict (12); Signal peptide (1) FUNCTION: Binds tightly to hydroxyapatite. Appears to form an integral part of the mineralized matrix. Probably important to cell-matrix interaction.; FUNCTION: Acts as a cytokine involved in enhancing production of interferon-gamma and interleukin-12 and reducing production of interleukin-10 and is essential in the pathway that leads to type I immunity. PTM: Extensively phosphorylated by FAM20C in the extracellular medium at multiple sites within the S-x-E/pS motif. {ECO:0000250|UniProtKB:P10451}.; PTM: O-glycosylated. {ECO:0000250|UniProtKB:P10451}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Ligand for integrin alpha-V/beta-3. +P54615 OSTR_MOUSE Osteocalcin-related protein (Gamma-carboxyglutamic acid-containing protein 3) (Nephrocalcin) (OC-X) 95 10,459 Chain (1); Disulfide bond (1); Domain (1); Metal binding (5); Modified residue (2); Propeptide (1); Sequence conflict (6); Signal peptide (1) FUNCTION: Binds strongly to apatite and calcium. {ECO:0000250|UniProtKB:P02820}. PTM: Gamma-carboxyglutamic acid residues are formed by vitamin K dependent carboxylation. These residues are essential for the binding of calcium. {ECO:0000250|UniProtKB:P02820}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Expressed in kidney and lung, but not in bone. {ECO:0000269|PubMed:8288580}. +B2RU80 PTPRB_MOUSE Receptor-type tyrosine-protein phosphatase beta (Protein-tyrosine phosphatase beta) (R-PTP-beta) (EC 3.1.3.48) (Vascular endothelial protein tyrosine phosphatase) (VE-PTP) 1998 224,495 Active site (1); Binding site (2); Chain (1); Domain (18); Glycosylation (23); Modified residue (1); Mutagenesis (2); Region (1); Sequence conflict (8); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1623 1643 Helical. {ECO:0000255}. TOPO_DOM 23 1622 Extracellular. {ECO:0000255}.; TOPO_DOM 1644 1997 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays an important role in blood vessel remodeling and angiogenesis. Not necessary for the initial formation of blood vessels, but is essential for their maintenance and remodeling. Can induce dephosphorylation of TEK/TIE2, CDH5/VE-cadherin and KDR/VEGFR-2. Regulates angiopoietin-TIE2 signaling in endothelial cells. Acts as a negative regulator of TIE2, and controls TIE2 driven endothelial cell proliferation, which in turn affects blood vessel remodeling during embryonic development and determines blood vessel size during perinatal growth. Essential for the maintenance of endothelial cell contact integrity and for the adhesive function of VE-cadherin in endothelial cells and this requires the presence of plakoglobin. {ECO:0000269|PubMed:10557082, ECO:0000269|PubMed:12234928, ECO:0000269|PubMed:16514057, ECO:0000269|PubMed:17360632, ECO:0000269|PubMed:19015309, ECO:0000269|PubMed:19451274}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Monomer (By similarity). Interacts with TEK (PubMed:10557082, PubMed:19451274). Interacts via fibronectin type-III 17 domain with CDH5 (PubMed:19015309). Detected in a complex with CNTN1 and NRCAM (PubMed:11564762). Interacts (phosphorylated form) with FYN and GRB2 (PubMed:20398064). {ECO:0000250|UniProtKB:P23467, ECO:0000269|PubMed:10557082, ECO:0000269|PubMed:11564762, ECO:0000269|PubMed:12234928, ECO:0000269|PubMed:19015309, ECO:0000269|PubMed:19451274, ECO:0000269|PubMed:20398064}. TISSUE SPECIFICITY: Expression is very high in the vasculature of lung, spleen, and kidney, as well as in the heart valves, and is also present in the endothelium of arterioles and venules. Also expressed in tumor vasculature. {ECO:0000269|PubMed:10557082, ECO:0000269|PubMed:16514057, ECO:0000269|PubMed:17360632}. +P11725 OTC_MOUSE Ornithine carbamoyltransferase, mitochondrial (EC 2.1.3.3) (Ornithine transcarbamylase) (OTCase) 354 39,765 Active site (1); Binding site (6); Chain (1); Modified residue (21); Natural variant (1); Region (3); Sequence conflict (1); Transit peptide (1) Nitrogen metabolism; urea cycle; L-citrulline from L-ornithine and carbamoyl phosphate: step 1/1. PTM: Acetylation at Lys-88 negatively regulates ornithine carbamoyltransferase activity in response to nutrient signals. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion matrix. SUBUNIT: Homotrimer. DISEASE: Note=Defects in Otc are the cause of the Sparse fur (spf) phenotype. Spf mouse have an OTCase with an overall decrease in activity, and altered substrate affinity. {ECO:0000269|PubMed:3603027}. +A2A8L5 PTPRF_MOUSE Receptor-type tyrosine-protein phosphatase F (EC 3.1.3.48) (Leukocyte common antigen related) (LAR) 1898 211,489 Active site (2); Beta strand (19); Binding site (2); Chain (1); Disulfide bond (3); Domain (13); Glycosylation (7); Helix (3); Modified residue (1); Region (2); Sequence conflict (7); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 1255 1275 Helical. {ECO:0000255}. TOPO_DOM 30 1254 Extracellular. {ECO:0000255}.; TOPO_DOM 1276 1898 Cytoplasmic. {ECO:0000255}. FUNCTION: Possible cell adhesion receptor. It possesses an intrinsic protein tyrosine phosphatase activity (PTPase) and dephosphorylates EPHA2 regulating its activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. SUBUNIT: Interacts with GRIP1. Interacts with PPFIA1, PPFIA2 and PPFIA3. Interacts with PTPRF. {ECO:0000250}. DOMAIN: The first PTPase domain has enzymatic activity, while the second one seems to affect the substrate specificity of the first one. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the cell of the T lineage but not in cells of any other hemopoietic lineage. {ECO:0000269|PubMed:11241288}. +P35822 PTPRK_MOUSE Receptor-type tyrosine-protein phosphatase kappa (Protein-tyrosine phosphatase kappa) (R-PTP-kappa) (EC 3.1.3.48) 1457 164,186 Active site (2); Binding site (2); Chain (1); Disulfide bond (1); Domain (8); Glycosylation (12); Modified residue (1); Region (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 753 774 Helical. {ECO:0000255}. TOPO_DOM 26 752 Extracellular. {ECO:0000255}.; TOPO_DOM 775 1457 Cytoplasmic. {ECO:0000255}. FUNCTION: Regulation of processes involving cell contact and adhesion such as growth control, tumor invasion, and metastasis. Negative regulator of EGFR signaling pathway. Forms complexes with beta-catenin and gamma-catenin/plakoglobin. Beta-catenin may be a substrate for the catalytic activity of PTPRK/PTP-kappa. PTM: This protein undergoes proteolytic processing. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. TISSUE SPECIFICITY: High levels in liver and kidney. Lower levels in lung, brain and heart. Not seen in spleen and testis. +P28828 PTPRM_MOUSE Receptor-type tyrosine-protein phosphatase mu (Protein-tyrosine phosphatase mu) (R-PTP-mu) (EC 3.1.3.48) 1452 163,653 Active site (2); Binding site (2); Chain (1); Disulfide bond (3); Domain (8); Glycosylation (12); Modified residue (1); Region (1); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 743 764 Helical. {ECO:0000255}. TOPO_DOM 21 742 Extracellular. {ECO:0000255}.; TOPO_DOM 765 1452 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in cell-cell adhesion through homophilic interactions. May play a key role in signal transduction and growth control. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. TISSUE SPECIFICITY: Most abundant in lung, less in brain and heart. +F7A4A7 OTOGL_MOUSE Otogelin-like protein 2325 260,929 Alternative sequence (1); Chain (1); Compositional bias (1); Disulfide bond (5); Domain (7); Glycosylation (7); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +O55225 OTOG_MOUSE Otogelin 2910 313,521 Alternative sequence (2); Chain (1); Compositional bias (2); Disulfide bond (7); Domain (7); Glycosylation (3); Sequence conflict (9); Signal peptide (1) FUNCTION: Glycoprotein specific to acellular membranes of the inner ear. May be required for the anchoring of the otoconial membranes and cupulae to the underlying neuroepithelia in the vestibule. May be involved in the organization and/or stabilization of the fibrillar network that compose the tectorial membrane in the cochlea. May play a role in mechanotransduction processes. {ECO:0000269|PubMed:10655058}. PTM: N-glycosylated. Not O-glycosylated. {ECO:0000269|PubMed:9405633}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:11506947, ECO:0000269|PubMed:9405633}; Peripheral membrane protein {ECO:0000269|PubMed:11506947, ECO:0000269|PubMed:9405633}; Extracellular side {ECO:0000269|PubMed:11506947, ECO:0000269|PubMed:9405633}. Secreted, extracellular space {ECO:0000269|PubMed:9405633}. Note=Found in fiber-like structures during the maturation process of the tectorial membrane (PubMed:9405633). TISSUE SPECIFICITY: Expressed specifically in neuroepithelial supporting cells of the inner ear. Expressed in the cochlea between postnatal day P0 and P6 in pseudostratified cells of the greater epithelial ridge, in supporting cells of the neuroepithelium comprising Deiter's, Hensen's, pillar and Claudius cells, in epithelial cells of the Reissner's membrane, in a small set of cells comprising the spiral prominence. Expressed in the cochlea at P15 in interdental cells located underneath the limbal part of the tectorial membrane. Expressed in the vestibular apparatus at P0 in supporting cells of the saccular, utricular maculae and cristae ampullares, in the epithelial cells of the roof of the saccule but not in the roof of the utricle and cristae ampullares (at protein level). Expressed in the cochlea and vestibular organ of the inner ear. {ECO:0000269|PubMed:11506947, ECO:0000269|PubMed:9405633}. +Q80VM9 OTOP1_MOUSE Proton channel OTOP1 (Otopetrin-1) 600 65,755 Alternative sequence (2); Chain (1); Mutagenesis (2); Sequence conflict (3); Transmembrane (12) TRANSMEM 65 85 Helical. {ECO:0000255}.; TRANSMEM 90 110 Helical. {ECO:0000255}.; TRANSMEM 135 155 Helical. {ECO:0000255}.; TRANSMEM 166 186 Helical. {ECO:0000255}.; TRANSMEM 199 219 Helical. {ECO:0000255}.; TRANSMEM 267 287 Helical. {ECO:0000255}.; TRANSMEM 309 329 Helical. {ECO:0000255}.; TRANSMEM 345 365 Helical. {ECO:0000255}.; TRANSMEM 391 411 Helical. {ECO:0000255}.; TRANSMEM 422 442 Helical. {ECO:0000255}.; TRANSMEM 533 553 Helical. {ECO:0000255}.; TRANSMEM 564 584 Helical. {ECO:0000255}. FUNCTION: Proton-selective channel that specifically transports protons into cells (PubMed:29371428). Proton channel activity is only weakly-sensitive to voltage (PubMed:29371428). Proton-selective channel activity is probably required in cell types that use changes in intracellular pH for cell signaling or to regulate biochemical or developmental processes (PubMed:29371428). In the vestibular system of the inner ear, required for the formation and function of otoconia, which are calcium carbonate crystals that sense gravity and acceleration (PubMed:12651873). Probably acts by maintaining the pH appropriate for formation of otoconia (PubMed:29371428). Regulates purinergic control of intracellular calcium in vestibular supporting cells (PubMed:17606897, PubMed:20554841). May be involved in sour taste perception in sour taste cells by mediating entry of protons within the cytosol (PubMed:29371428). Also involved in energy metabolism, by reducing adipose tissue inflammation and protecting from obesity-induced metabolic dysfunction (PubMed:24379350). {ECO:0000269|PubMed:12651873, ECO:0000269|PubMed:17606897, ECO:0000269|PubMed:20554841, ECO:0000269|PubMed:24379350, ECO:0000269|PubMed:29371428}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:29371428}; Multi-pass membrane protein {ECO:0000255}. Note=Detected in the gelatinous membrane overlying the inner ear macular epithelium. {ECO:0000269|PubMed:12651873, ECO:0000269|PubMed:21236346}. TISSUE SPECIFICITY: Detected in embryonic inner ear macular epithelia (PubMed:12651873). Expressed in thymus, heart, kidney, skin, vestibular system of the inner ear, sour taste cells, brown adipose tissue, heart, uterus, dorsal root ganglion, adrenal gland, lactating mammary gland and stimulated mast cells (PubMed:12651873, PubMed:29371428). Specifically expressed in sour taste cells and not other types of taste cells (PubMed:29371428). {ECO:0000269|PubMed:12651873, ECO:0000269|PubMed:29371428}. +Q9JIE3 OTOR_MOUSE Otoraplin (Melanoma inhibitory activity-like protein) 128 14,328 Chain (1); Disulfide bond (2); Domain (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Highly expressed in cochlea. +O09113 OTP_MOUSE Homeobox protein orthopedia 325 34,159 Chain (1); Compositional bias (2); DNA binding (1); Motif (1) FUNCTION: Involved in the specification of hypothalamic neuroendocrine cells. Specifically required for the specification of diencephalic dopaminergic neurons of the A11 group. {ECO:0000269|PubMed:10557207, ECO:0000269|PubMed:11071765, ECO:0000269|PubMed:17481897, ECO:0000269|PubMed:7913821}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-ProRule:PRU00138}. TISSUE SPECIFICITY: Restricted regions of the developing forebrain, hindbrain, and spinal cord. {ECO:0000269|PubMed:7913821}. +Q8CB27 OTU1_MOUSE Ubiquitin thioesterase OTU1 (EC 3.4.19.12) 343 37,485 Active site (4); Beta strand (4); Binding site (1); Chain (1); Domain (1); Erroneous termination (1); Frameshift (1); Helix (1); Region (5); Turn (2); Zinc finger (1) FUNCTION: Hydrolase that can remove conjugated ubiquitin from proteins and participates in endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins. May act by triming the ubiquitin chain on the associated substrate to facilitate their threading through the VCP/p97 pore. Ubiquitin moieties on substrates may present a steric impediment to the threading process when the substrate is transferred to the VCP pore and threaded through VCP's axial channel. Mediates deubiquitination of 'Lys-27'-, 'Lys-29'- and 'Lys-33'-linked polyubiquitin chains. Also able to hydrolyze 'Lys-11'-linked ubiquitin chains. Cleaves both polyubiquitin and di-ubiquitin. May play a role in macroautophagy, regulating for instance the clearance of damaged lysosomes. May recruit PLAA, UBXN6 and VCP to damaged lysosome membranes decorated with K48-linked ubiquitin chains and remove these chains allowing autophagosome formation. {ECO:0000250|UniProtKB:Q5VVQ6}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q5VVQ6}. Note=Recruited to damaged lysosomes decorated with K48-linked ubiquitin chains. {ECO:0000250|UniProtKB:Q5VVQ6}. SUBUNIT: Interacts with VCP; the interaction is direct. Interacts with FAF2/UBXD8. Interacts with DERL1; however interaction is dependent on the UBAX-like region, suggesting that it may be indirect. Interacts with PLAA, UBXN6 and VCP; may form a complex involved in macroautophagy. {ECO:0000250|UniProtKB:Q5VVQ6}. DOMAIN: The UBAX-like region mediates the interaction with VCP. {ECO:0000250|UniProtKB:Q5VVQ6}.; DOMAIN: The C2H2-type zinc finger mediates specificity for 'Lys-27'-, 'Lys-29'- and 'Lys-33'-linked polyubiquitin chains but not for 'Lys-11'-linked ubiquitin chains. Selectivity for 'Lys-11'-linked ubiquitin chains is provided by recognition of the sequence surrounding 'Lys-11' in ubiquitin. The S2 site region provides specificity for longer 'Lys-11'-linked ubiquitin chains. {ECO:0000250|UniProtKB:Q5VVQ6}. +P70289 PTPRV_MOUSE Receptor-type tyrosine-protein phosphatase V (R-PTP-V) (EC 3.1.3.48) (Embryonic stem cell protein-tyrosine phosphatase) (ES cell phosphatase) 1705 186,796 Active site (1); Binding site (2); Chain (1); Domain (12); Glycosylation (19); Region (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1078 1100 Helical. {ECO:0000255}. TOPO_DOM 19 1077 Extracellular. {ECO:0000255}.; TOPO_DOM 1101 1705 Cytoplasmic. {ECO:0000255}. FUNCTION: May play a role in the maintenance of pluripotency. Down-regulated during differentiation. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. +Q62010 OVGP1_MOUSE Oviduct-specific glycoprotein (Estrogen-dependent oviduct protein) (Oviductal glycoprotein) (Oviductin) 721 78,808 Chain (1); Glycosylation (3); Region (1); Repeat (21); Signal peptide (1) FUNCTION: Binds to oocyte zona pellucida in vivo. May play a role in the fertilization process and/or early embryonic development. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle. Note=Secretory granules. TISSUE SPECIFICITY: Epithelial cells of the oviduct. +Q9CUB6 OTUD1_MOUSE OTU domain-containing protein 1 (EC 3.4.19.12) 454 48,823 Active site (3); Chain (1); Compositional bias (1); Domain (2); Frameshift (1); Region (3) FUNCTION: Deubiquitinating enzyme that specifically hydrolyzes 'Lys-63'-linked polyubiquitin to monoubiquitin. {ECO:0000250}. DOMAIN: The UIM repeat increases the specificity and efficiency of the enzyme toward 'Lys-63'-linked polyubiquitin. {ECO:0000250}.; DOMAIN: Specificity is not given by the S1' ubiquitin-binding site within the OTU domain (composed of the Cys-, His- and Variable-loops). {ECO:0000250}. +B2RRE7 OTUD4_MOUSE OTU domain-containing protein 4 (EC 3.4.19.12) 1107 123,055 Active site (3); Chain (1); Domain (1); Modified residue (20); Mutagenesis (1); Region (3); Sequence conflict (1) FUNCTION: Deubiquitinase which hydrolyzes the isopeptide bond between the ubiquitin C-terminus and the lysine epsilon-amino group of the target protein. May negatively regulate inflammatory and pathogen recognition signaling in innate immune response. Upon phosphorylation at Ser-202 and Ser-204 residues, via IL-1 receptor and Toll-like receptor signaling pathway, specifically deubiquitinates 'Lys-63'-polyubiquitinated MYD88 adapter protein triggering down-regulation of NF-kappa-B-dependent transcription of inflammatory mediators (PubMed:29395066). Independently of the catalytic activity, acts as a scaffold for alternative deubiquitinases to assemble specific deubiquitinase-substrate complexes. Associates with USP7 and USP9X deubiquitinases to stabilize alkylation repair enzyme ALKBH3, thereby promoting the repair of alkylated DNA lesions (By similarity). {ECO:0000250|UniProtKB:Q01804, ECO:0000269|PubMed:29395066}. PTM: Phosphorylation at Ser-202 and Ser-204 activates 'Lys-63'-specific deubiquitinase activity. Induced upon stimulation with IL1B. {ECO:0000305|PubMed:29395066}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q01804}. Nucleus {ECO:0000250|UniProtKB:Q01804}. Note=Primarily cytoplasmic. {ECO:0000250|UniProtKB:Q01804}. SUBUNIT: Interacts with MYD88; the interaction is direct (PubMed:29395066). Interacts with ALKBH3; the interaction is direct. Interacts with USP7; the interaction is direct. Interacts with USP9X; the interaction is direct (By similarity). {ECO:0000250|UniProtKB:Q01804, ECO:0000269|PubMed:29395066}. +Q3TVP5 OTULL_MOUSE Inactive ubiquitin thioesterase OTULINL 353 41,576 Alternative sequence (1); Chain (1); Domain (1); Sequence conflict (2) +Q3UCV8 OTUL_MOUSE Ubiquitin thioesterase otulin (EC 3.4.19.12) (Deubiquitinating enzyme otulin) (OTU domain-containing deubiquitinase with linear linkage specificity) (Ubiquitin thioesterase Gumby) 352 40,320 Active site (3); Binding site (1); Chain (1); Coiled coil (1); Domain (1); Erroneous initiation (2); Modified residue (1); Motif (2); Mutagenesis (4); Region (5) FUNCTION: Deubiquitinase that specifically removes linear ('Met-1'-linked) polyubiquitin chains to substrates and acts as a regulator of angiogenesis and innate immune response (PubMed:23708998, PubMed:27523608, PubMed:29950720). Required during angiogenesis, craniofacial and neuronal development by regulating the canonical Wnt signaling together with the LUBAC complex (PubMed:23708998). Acts as a negative regulator of NF-kappa-B by regulating the activity of the LUBAC complex (By similarity). OTULIN function is mainly restricted to homeostasis of the LUBAC complex: acts by removing 'Met-1'-linked autoubiquitination of the LUBAC complex, thereby preventing inactivation of the LUBAC complex (PubMed:29950720). Acts as a key negative regulator of inflammation by restricting spontaneous inflammation and maintaining immune homeostasis (PubMed:27523608, PubMed:29950720). In myeloid cell, required to prevent unwarranted secretion of cytokines leading to inflammation and autoimmunity by restricting linear polyubiquitin formation (PubMed:27523608). Plays a role in innate immune response by restricting linear polyubiquitin formation on LUBAC complex in response to NOD2 stimulation, probably to limit NOD2-dependent proinflammatory signaling (By similarity). {ECO:0000250|UniProtKB:Q96BN8, ECO:0000269|PubMed:23708998, ECO:0000269|PubMed:27523608, ECO:0000269|PubMed:29950720}. PTM: Ubiquitinated. {ECO:0000250|UniProtKB:Q96BN8}.; PTM: Acetylated. {ECO:0000250|UniProtKB:Q96BN8}.; PTM: Phosphorylated. Phosphorylation at Tyr-56 prevents interaction with RNF31; dephosphorylation promotes interaction with RNF31 and the LUBAC complex. {ECO:0000250|UniProtKB:Q96BN8}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23708998}. SUBUNIT: Interacts (via the PUB domain) with RNF31 (via the PIM motif); the interaction is direct (PubMed:23708998). Interacts with DVL2 (PubMed:23708998). {ECO:0000269|PubMed:23708998}. DOMAIN: The specificity for linear polyubiquitin is given by the 'Glu-16' residue in ubiquitin chain. {ECO:0000250|UniProtKB:Q96BN8}.; DOMAIN: The PIM (PUB-interaction motif) motif mediates interaction with the PUB domain of RNF31. Does not interact with other PUB domain-containing proteins. Phosphorylation at Tyr-56 prevents interaction with RNF31. {ECO:0000250|UniProtKB:Q96BN8}. +O09046 OXLA_MOUSE L-amino-acid oxidase (LAAO) (LAO) (EC 1.4.3.2) (Interleukin-4-induced protein 1) (IL4-induced protein 1) (Protein Fig-1) (mFIG1) 630 70,191 Alternative sequence (1); Binding site (6); Chain (1); Disulfide bond (1); Erroneous initiation (1); Glycosylation (3); Nucleotide binding (2); Sequence conflict (19); Signal peptide (1) FUNCTION: Lysosomal L-amino-acid oxidase with highest specific activity with phenylalanine. May play a role in lysosomal antigen processing and presentation. {ECO:0000269|PubMed:15383589}. SUBCELLULAR LOCATION: Isoform 1: Lysosome.; SUBCELLULAR LOCATION: Isoform 2: Lysosome. TISSUE SPECIFICITY: Isoform 1 primarily found in immune tissues, mostly in B-lymphocytes. Isoform 2 restricted to the testis, predominantly in Sertoli cells at the periphery of the ducts, and the brain, including Purkinje cells, hippocampus and mitral cells in the olfactory bulb. No isoform 2 expression in fetal tissues. {ECO:0000269|PubMed:16029492}. +Q6IYF8 OXGR1_MOUSE 2-oxoglutarate receptor 1 (Alpha-ketoglutarate receptor 1) (G-protein coupled receptor 99) 337 38,230 Chain (1); Disulfide bond (1); Frameshift (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 39 59 Helical; Name=1. {ECO:0000255}.; TRANSMEM 70 90 Helical; Name=2. {ECO:0000255}.; TRANSMEM 117 137 Helical; Name=3. {ECO:0000255}.; TRANSMEM 152 172 Helical; Name=4. {ECO:0000255}.; TRANSMEM 201 221 Helical; Name=5. {ECO:0000255}.; TRANSMEM 243 263 Helical; Name=6. {ECO:0000255}.; TRANSMEM 285 305 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 38 Extracellular. {ECO:0000255}.; TOPO_DOM 60 69 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 91 116 Extracellular. {ECO:0000255}.; TOPO_DOM 138 151 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 173 200 Extracellular. {ECO:0000255}.; TOPO_DOM 222 242 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 264 284 Extracellular. {ECO:0000255}.; TOPO_DOM 306 337 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for alpha-ketoglutarate. Seems to act exclusively through a G(q)-mediated pathway. {ECO:0000269|PubMed:15141213}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Predominantly expressed in the kidney with limited expression in the testis and the smooth muscle. {ECO:0000269|PubMed:15141213}. +Q6P9R2 OXSR1_MOUSE Serine/threonine-protein kinase OSR1 (EC 2.7.11.1) (Oxidative stress-responsive 1 protein) 527 58,214 Active site (1); Binding site (1); Chain (1); Domain (1); Erroneous initiation (2); Initiator methionine (1); Modified residue (8); Nucleotide binding (1); Sequence conflict (1) FUNCTION: Phosphorylates RELL1, RELL2, RELT and PAK1. Phosphorylates PLSCR1 in the presence of RELT. {ECO:0000250|UniProtKB:O95747}. PTM: Autophosphorylated. {ECO:0000250|UniProtKB:O95747}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O95747}. SUBUNIT: Interacts with PAK1 (By similarity). Interacts with chloride channel proteins SLC12A6 isoform 2, SLC12A1 and SLC12A2 but not with SLC12A4 and SLC12A7, possibly establishing sensor/signaling modules that initiate the cellular response to environmental stress (PubMed:12386165). Interacts with RELL1, RELL2 and RELT (By similarity). Interacts with PLSCR1 in the presence of RELT (By similarity). {ECO:0000250|UniProtKB:O95747, ECO:0000269|PubMed:12386165}. TISSUE SPECIFICITY: Ubiquitously expressed in all tissues examined, except thymus. {ECO:0000269|PubMed:14707132}. +D3Z4S3 PTRD1_MOUSE Putative peptidyl-tRNA hydrolase PTRHD1 (EC 3.1.1.29) (Peptidyl-tRNA hydrolase domain-containing protein 1) 140 16,037 Chain (1) +Q5SW25 P12L2_MOUSE POM121-like protein 2 972 103,220 Chain (1); Compositional bias (1) +Q8CCJ9 P20L1_MOUSE PHD finger protein 20-like protein 1 1013 113,860 Alternative sequence (11); Chain (1); Compositional bias (1); Cross-link (3); Domain (2); Erroneous initiation (2); Modified residue (3); Sequence conflict (1); Zinc finger (1) +Q9CWP9 P23A3_MOUSE Proline-rich protein 23A3 254 27,565 Chain (1); Compositional bias (1) +Q3UHB1 NT5D3_MOUSE 5'-nucleotidase domain-containing protein 3 (EC 3.1.3.-) (GRP94-neighboring nucleotidase) 546 63,170 Active site (2); Chain (1); Metal binding (3); Region (1); Sequence conflict (2) +Q80WB5 NTAQ1_MOUSE Protein N-terminal glutamine amidohydrolase (EC 3.5.1.122) (Protein NH2-terminal glutamine deamidase) (N-terminal Gln amidase) (Nt(Q)-amidase) (WDYHV motif-containing protein 1) 209 24,337 Active site (3); Chain (1); Mutagenesis (8) FUNCTION: Mediates the side-chain deamidation of N-terminal glutamine residues to glutamate, an important step in N-end rule pathway of protein degradation. Conversion of the resulting N-terminal glutamine to glutamate renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. Does not act on substrates with internal or C-terminal glutamine and does not act on non-glutamine residues in any position. Does not deaminate acetylated N-terminal glutamine. With the exception of proline, all tested second-position residues on substrate peptides do not greatly influence the activity. In contrast, a proline at position 2, virtually abolishes deamidation of N-terminal glutamine. {ECO:0000269|PubMed:19560421}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:19560421}. Nucleus {ECO:0000269|PubMed:19560421}. SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q96HA8}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:19560421}. +Q9R060 NUBP1_MOUSE Cytosolic Fe-S cluster assembly factor NUBP1 (Nucleotide-binding protein 1) (NBP 1) 320 34,085 Chain (1); Metal binding (6); Modified residue (2); Nucleotide binding (1); Sequence conflict (4) FUNCTION: Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. The NUBP1-NUBP2 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins (By similarity). Implicated in the regulation of centrosome duplication (PubMed:16638812, PubMed:23807208). Negatively regulates cilium formation and structure (PubMed:23807208). {ECO:0000255|HAMAP-Rule:MF_03038, ECO:0000269|PubMed:16638812, ECO:0000269|PubMed:23807208}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03038, ECO:0000269|PubMed:23807208}. Nucleus {ECO:0000269|PubMed:23807208}. Cell projection {ECO:0000269|PubMed:23807208}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:23807208}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:23807208}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000269|PubMed:23807208}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:23807208}. Note=Enriched in centrioles of microtubule asters during prophase, prometaphase and telophase stages of mitosis. Localized at centrioles and in the nucleus at interphase. Colocalizes with NUBP2 at prometaphase. Specifically localizes to the axenome of motile cilia as opposed to primary non-motile cilia. Localization is independent of NUBP2 and KIFC1. {ECO:0000269|PubMed:23807208}. SUBUNIT: Heterotetramer of 2 NUBP1 and 2 NUBP2 chains (PubMed:16638812). Interacts with KIFC1 (PubMed:16638812). Interacts with NUBP2 (PubMed:16638812). Interacts with the BBS/CCT complex subunit CCT1 (PubMed:23807208). {ECO:0000255|HAMAP-Rule:MF_03038, ECO:0000269|PubMed:16638812, ECO:0000269|PubMed:23807208}. TISSUE SPECIFICITY: Expressed in trachea epithelial cells, and kidney inner medullary collecting duct cells. {ECO:0000269|PubMed:23807208}. +P03921 NU5M_MOUSE NADH-ubiquinone oxidoreductase chain 5 (EC 7.1.1.2) (NADH dehydrogenase subunit 5) 607 68,475 Beta strand (9); Chain (1); Helix (37); Sequence conflict (2); Transmembrane (16); Turn (6) TRANSMEM 3 23 Helical. {ECO:0000255}.; TRANSMEM 35 55 Helical. {ECO:0000255}.; TRANSMEM 84 104 Helical. {ECO:0000255}.; TRANSMEM 117 137 Helical. {ECO:0000255}.; TRANSMEM 140 160 Helical. {ECO:0000255}.; TRANSMEM 171 191 Helical. {ECO:0000255}.; TRANSMEM 210 230 Helical. {ECO:0000255}.; TRANSMEM 241 261 Helical. {ECO:0000255}.; TRANSMEM 272 292 Helical. {ECO:0000255}.; TRANSMEM 301 320 Helical. {ECO:0000255}.; TRANSMEM 324 344 Helical. {ECO:0000255}.; TRANSMEM 365 385 Helical. {ECO:0000255}.; TRANSMEM 405 427 Helical. {ECO:0000255}.; TRANSMEM 457 477 Helical. {ECO:0000255}.; TRANSMEM 482 502 Helical. {ECO:0000255}.; TRANSMEM 586 606 Helical. {ECO:0000255}. FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q641K5 NUAK1_MOUSE NUAK family SNF1-like kinase 1 (EC 2.7.11.1) (AMPK-related protein kinase 5) (Omphalocele kinase 1) 658 73,661 Active site (1); Binding site (1); Chain (1); Domain (1); Modified residue (5); Motif (1); Nucleotide binding (1) FUNCTION: Serine/threonine-protein kinase involved in various processes such as cell adhesion, regulation of cell ploidy and senescence, cell proliferation and tumor progression. Phosphorylates ATM, CASP6, LATS1, PPP1R12A and p53/TP53. Acts as a regulator of cellular senescence and cellular ploidy by mediating phosphorylation of 'Ser-464' of LATS1, thereby controlling its stability. Controls cell adhesion by regulating activity of the myosin protein phosphatase 1 (PP1) complex. Acts by mediating phosphorylation of PPP1R12A subunit of myosin PP1: phosphorylated PPP1R12A then interacts with 14-3-3, leading to reduced dephosphorylation of myosin MLC2 by myosin PP1. May be involved in DNA damage response: phosphorylates p53/TP53 at 'Ser-15' and 'Ser-392' and is recruited to the CDKN1A/WAF1 promoter to participate to transcription activation by p53/TP53. May also act as a tumor malignancy-associated factor by promoting tumor invasion and metastasis under regulation and phosphorylation by AKT1. Suppresses Fas-induced apoptosis by mediating phosphorylation of CASP6, thereby suppressing the activation of the caspase and the subsequent cleavage of CFLAR. Regulates UV radiation-induced DNA damage response mediated by CDKN1A. In association with STK11, phosphorylates CDKN1A in response to UV radiation and contributes to its degradation which is necessary for optimal DNA repair. {ECO:0000250|UniProtKB:O60285}. PTM: Phosphorylated at Thr-212 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. Not dephosphorylated by the myosin PP1 complex when regulating its activity, due to the presence of PPP1R12A, which prevents myosin PP1 from dephosphorylating NUAK1. Phosphorylated by STK38L upon stimulation with IGF1 (By similarity). {ECO:0000250}.; PTM: Ubiquitinated with 'Lys-29'- and 'Lys-33'-linked polyubiquitins which appear to impede LKB1-mediated phosphorylation. Deubiquitinated by USP9X (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. SUBUNIT: Interact (via GILK motif) with PPP1CB; the interaction is direct and bridges NUAK1 and PPP1R12A. Interacts with CDKN1A. {ECO:0000250|UniProtKB:O60285}. DOMAIN: The GILK motif mediates interaction with PPP1CB. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the developing central nervous system, in epidermis, and some other tissues. {ECO:0000269|PubMed:16715502}. +Q8BZN4 NUAK2_MOUSE NUAK family SNF1-like kinase 2 (EC 2.7.11.1) (Omphalocele kinase 2) 639 70,675 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Domain (1); Modified residue (6); Nucleotide binding (1); Sequence conflict (2) FUNCTION: Stress-activated kinase involved in tolerance to glucose starvation. Induces cell-cell detachment by increasing F-actin conversion to G-actin. Expression is induced by CD95 or TNF-alpha, via NF-kappa-B. Protects cells from CD95-mediated apoptosis and is required for the increased motility and invasiveness of CD95-activated tumor cells. Able to phosphorylate 'Ser-464' of LATS1 (By similarity). {ECO:0000250}. PTM: Phosphorylated at Thr-220 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. Autophosphorylated in vitro (By similarity). {ECO:0000250}. +P03925 NU6M_MOUSE NADH-ubiquinone oxidoreductase chain 6 (EC 7.1.1.2) (NADH dehydrogenase subunit 6) 172 18,626 Beta strand (2); Chain (1); Helix (8); Transmembrane (4); Turn (3) TRANSMEM 1 21 Helical. {ECO:0000255}.; TRANSMEM 38 58 Helical. {ECO:0000255}.; TRANSMEM 86 106 Helical. {ECO:0000255}.; TRANSMEM 147 167 Helical. {ECO:0000255}. FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8R1N4 NUDC3_MOUSE NudC domain-containing protein 3 363 40,890 Alternative sequence (4); Chain (1); Domain (1); Erroneous initiation (1); Modified residue (2) +Q8JZU0 NUD13_MOUSE Nucleoside diphosphate-linked moiety X motif 13 (Nudix motif 13) (EC 3.-.-.-) 352 39,137 Chain (1); Domain (1); Erroneous initiation (2); Motif (1) +Q8R2U6 NUDT4_MOUSE Diphosphoinositol polyphosphate phosphohydrolase 2 (DIPP-2) (EC 3.6.1.52) (Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 2) (EC 3.6.1.-) (Nucleoside diphosphate-linked moiety X motif 4) (Nudix motif 4) 179 20,156 Active site (1); Beta strand (7); Binding site (3); Chain (1); Domain (1); Helix (4); Metal binding (4); Motif (1); Region (3); Sequence conflict (2); Turn (2) FUNCTION: Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate), PP-InsP4 and [PP]2-InsP4 (bisdiphosphoinositol tetrakisphosphate), suggesting that it may play a role in signal transduction. Also able to catalyze the hydrolysis of dinucleoside oligophosphate Ap6A, but not Ap5A. The major reaction products are ADP and p4a from Ap6A. Also able to hydrolyze 5-phosphoribose 1-diphosphate (By similarity). Does not play a role in U8 snoRNA decapping activity. Binds U8 snoRNA. {ECO:0000250|UniProtKB:Q9NZJ9}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NZJ9}. +Q80XU3 NUCKS_MOUSE Nuclear ubiquitous casein and cyclin-dependent kinase substrate 1 (JC7) 234 26,313 Chain (1); Compositional bias (2); Modified residue (21); Sequence conflict (8) PTM: Phosphorylated by CDK1 and casein kinase. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +Q8BVU5 NUDT9_MOUSE ADP-ribose pyrophosphatase, mitochondrial (EC 3.6.1.13) (ADP-ribose diphosphatase) (ADP-ribose phosphohydrolase) (Adenosine diphosphoribose pyrophosphatase) (ADPR-PPase) (Nucleoside diphosphate-linked moiety X motif 9) (Nudix motif 9) 350 38,604 Chain (1); Domain (1); Modified residue (1); Motif (1); Sequence conflict (1); Transit peptide (1) FUNCTION: Hydrolyzes ADP-ribose (ADPR) to AMP and ribose 5'-phosphate. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. SUBUNIT: Monomer. Interacts with GLOD4. {ECO:0000250}. +P09405 NUCL_MOUSE Nucleolin (Protein C23) 707 76,723 Chain (1); Compositional bias (4); Cross-link (11); Domain (4); Initiator methionine (1); Modified residue (59); Region (1); Repeat (8); Sequence conflict (3) FUNCTION: Nucleolin is the major nucleolar protein of growing eukaryotic cells. It is found associated with intranucleolar chromatin and pre-ribosomal particles. It induces chromatin decondensation by binding to histone H1. It is thought to play a role in pre-rRNA transcription and ribosome assembly. May play a role in the process of transcriptional elongation. Binds RNA oligonucleotides with 5'-UUAGGG-3' repeats more tightly than the telomeric single-stranded DNA 5'-TTAGGG-3' repeats (By similarity). {ECO:0000250, ECO:0000269|PubMed:8065340}. PTM: Some glutamate residues are glycylated by TTLL8. This modification occurs exclusively on glutamate residues and results in a glycine chain on the gamma-carboxyl group.; PTM: Symmetrically methylated by PRMT5. {ECO:0000250|UniProtKB:P19338}. SUBCELLULAR LOCATION: Nucleus, nucleolus. Cytoplasm {ECO:0000250}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. {ECO:0000250}. SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs (By similarity). Component of the SWAP complex that consists of NPM1, NCL/nucleolin, PARP1 and SWAP70 (PubMed:9642267). Component of a complex which is at least composed of HTATSF1/Tat-SF1, the P-TEFb complex components CDK9 and CCNT1, RNA polymerase II, SUPT5H, and NCL/nucleolin (By similarity). Interacts with AICDA (PubMed:21518874). Interacts with APTX (By similarity). Interacts with C1QBP (By similarity). Interacts with ERBB4 (By similarity). Interacts (via C-terminus) with FMR1 isoform 6 (via N-terminus) (By similarity). Interacts with GZF1; this interaction is important for nucleolar localization of GZF1 (By similarity). Interacts with NSUN2 (By similarity). Interacts with NVL (PubMed:21474449). Interacts (via N-terminus domain) with SETX (By similarity). Interacts (via RRM1 and C-terminal RRM4/Arg/Gly-rich domains) with TERT; the interaction is important for nucleolar localization of TERT (By similarity). Interacts with WDR46 (By similarity). Interacts with ZFP36 (By similarity). Interacts with LRRC34 (PubMed:24991885). Interacts with RRP1B (By similarity). Interacts with HNRNPU; this interaction occurs during mitosis (By similarity). Interacts with RIOK1; RIOK1 recruits NCL to PRMT5 for symmetrically methylation (By similarity). Interacts with ZBTB7B (PubMed:28784777). {ECO:0000250|UniProtKB:P19338, ECO:0000269|PubMed:21474449, ECO:0000269|PubMed:21518874, ECO:0000269|PubMed:24991885, ECO:0000269|PubMed:28784777, ECO:0000269|PubMed:9642267}. TISSUE SPECIFICITY: Expressed in B-cells that have been induced to switch to various Ig isotypes. {ECO:0000269|PubMed:9642267}. +Q3U2V3 NUD18_MOUSE 8-oxo-dGDP phosphatase NUDT18 (EC 3.6.1.58) (2-hydroxy-dADP phosphatase) (7,8-dihydro-8-oxoguanine phosphatase) (MutT homolog 3) (Nucleoside diphosphate-linked moiety X motif 18) (Nudix motif 18) 323 35,694 Alternative sequence (2); Chain (1); Domain (1); Metal binding (2); Motif (1) FUNCTION: Mediates the hydrolyzis of oxidized nucleoside diphosphate derivatives. Hydrolyzes 8-oxo-7,8-dihydroguanine (8-oxo-Gua)-containing deoxyribo- and ribonucleoside diphosphates to the monophosphates. Hydrolyzes 8-oxo-dGDP and 8-oxo-GDP with the same efficiencies. Hydrolyzes also 8-OH-dADP and 2-OH-dADP. Exhibited no or minimal hydrolyzis activity against 8-oxo-dGTP, 8-oxo-GTP, dGTP, GTP, dGDP and GDP. Probably removes oxidized guanine nucleotides from both the DNA and RNA precursor pools (By similarity). {ECO:0000250}. +P11930 NUD19_MOUSE Nucleoside diphosphate-linked moiety X motif 19 (Nudix motif 19) (EC 3.6.1.-) (Androgen-regulated protein RP2) (Testosterone-regulated RP2 protein) (RP2p) 357 40,320 Chain (1); Domain (1); Metal binding (2); Modified residue (1); Motif (2); Sequence conflict (2) FUNCTION: Acyl-CoA diphosphatase that mediates the hydrolysis of a wide range of CoA esters, including choloyl-CoA and branched-chain fatty-acyl-CoA esters. At low substrate concentrations medium and long-chain fatty-acyl-CoA esters are the primary substrates. {ECO:0000269|PubMed:16185196}. SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:16185196}. +O70435 PSA3_MOUSE Proteasome subunit alpha type-3 (EC 3.4.25.1) (Macropain subunit C8) (Multicatalytic endopeptidase complex subunit C8) (Proteasome component C8) (Proteasome subunit K) 255 28,405 Beta strand (10); Chain (1); Helix (6); Initiator methionine (1); Modified residue (6); Turn (4) FUNCTION: Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). Binds to the C-terminus of CDKN1A and thereby mediates its degradation. Negatively regulates the membrane trafficking of the cell-surface thromboxane A2 receptor (TBXA2R) isoform 2. {ECO:0000269|PubMed:16581775, ECO:0000269|PubMed:22341445}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P25788}. Nucleus {ECO:0000250|UniProtKB:P25788}. SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is a barrel-shaped complex made of 28 subunits that are arranged in four stacked rings. The two outer rings are each formed by seven alpha subunits, and the two inner rings are formed by seven beta subunits. The proteolytic activity is exerted by three beta-subunits PSMB5, PSMB6 and PSMB7 (PubMed:16857966, PubMed:22341445). Interacts with AURKB. Interacts with CDKN1A. Interacts with MDM2 and RB1. Interacts with the C-terminus of TBXA2R isoform 2. Interacts with DNAJB2. {ECO:0000250|UniProtKB:P25788, ECO:0000269|PubMed:16857966, ECO:0000269|PubMed:22341445}. TISSUE SPECIFICITY: Detected in liver (at protein level). {ECO:0000269|PubMed:22341445}. +Q8R4R6 NUP35_MOUSE Nucleoporin NUP35 (35 kDa nucleoporin) (Mitotic phosphoprotein 44) (MP-44) (Nuclear pore complex protein Nup53) (Nucleoporin NUP53) 325 34,786 Beta strand (4); Chain (1); Domain (1); Helix (5); Modified residue (20); Sequence conflict (1); Turn (2) FUNCTION: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. May play a role in the association of MAD1 with the NPC (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q8NFH5}. Nucleus membrane {ECO:0000250|UniProtKB:Q8NFH5}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8NFH5}. Note=Tightly associated with the nuclear membrane and lamina. {ECO:0000250|UniProtKB:Q8NFH5}. SUBUNIT: Interacts with TMEM48/NDC1. Forms a complex with NUP93, NUP155, NUP205 and lamin B; The interaction with NUP93 is direct. {ECO:0000250}. +Q8BJ71 NUP93_MOUSE Nuclear pore complex protein Nup93 (93 kDa nucleoporin) (CBP-interacting protein 4) (Nucleoporin Nup93) 819 93,281 Alternative sequence (1); Chain (1); Frameshift (1); Modified residue (8); Sequence conflict (4) FUNCTION: Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. May anchor nucleoporins, but not NUP153 and TPR, to the NPC (By similarity). During renal development, regulates podocyte migration and proliferation through SMAD4 signaling (By similarity) (PubMed:26878725). {ECO:0000250|UniProtKB:Q8N1F7, ECO:0000269|PubMed:26878725}. SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250|UniProtKB:Q66HC5}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q66HC5}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q8N1F7}. Nucleus envelope {ECO:0000269|PubMed:26878725}. Note=Localizes at the nuclear basket and at or near the nuclear entry to the gated channel of the pore. {ECO:0000250}. SUBUNIT: Part of the nuclear pore complex (NPC). Component of the p62 complex, a complex composed of NUP62 and NUP54. Forms a complex with NUP35, NUP155, NUP205 and lamin B; the interaction with NUP35 is direct. Does not interact with TPR. Interacts with SMAD4 and IPO7; translocates SMAD4 to the nucleus through the NPC upon BMP7 stimulation resulting in activation of SMAD4 signaling. {ECO:0000250|UniProtKB:Q8N1F7}. +Q6PFD9 NUP98_MOUSE Nuclear pore complex protein Nup98-Nup96 (EC 3.4.21.-) [Cleaved into: Nuclear pore complex protein Nup98 (98 kDa nucleoporin) (Nucleoporin Nup98) (Nup98); Nuclear pore complex protein Nup96 (96 kDa nucleoporin) (Nucleoporin Nup96) (Nup96)] 1816 197,241 Active site (1); Beta strand (9); Chain (2); Compositional bias (2); Cross-link (3); Domain (1); Helix (4); Modified residue (22); Mutagenesis (1); Region (3); Sequence caution (3); Site (1); Turn (4) FUNCTION: Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. NUP98 and NUP96 are involved in the bidirectional transport across the NPC. May anchor NUP153 and TPR to the NPC. In cooperation with DHX9, plays a role in transcription and alternative splicing activation of a subset of genes. Involved in the localization of DHX9 in discrete intranuclear foci (GLFG-body). {ECO:0000250|UniProtKB:P52948}. PTM: Autoproteolytically cleaved to yield Nup98 and Nup96 or Nup98 only, respectively. Cleaved Nup98 is necessary for the targeting of Nup98 to the nuclear pore and the interaction with Nup96. {ECO:0000250|UniProtKB:P52948}. SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250|UniProtKB:P52948}; Peripheral membrane protein {ECO:0000250|UniProtKB:P52948}; Nucleoplasmic side {ECO:0000250|UniProtKB:P52948}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P52948}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P52948}. Note=Localized to the nucleoplasmic side of the nuclear pore complex (NPC), at or near the nucleoplasmic basket. Dissociates from the dissasembled NPC structure early during prophase of mitosis. Colocalized with NUP153 and TPR to the nuclear basket of NPC. Colocalized with DHX9 in diffuse and discrete intranuclear foci (GLFG-body). Remains localized to the nuclear membrane after poliovirus (PV) infection. {ECO:0000250|UniProtKB:P52948}. SUBUNIT: Part of the nuclear pore complex (NPC). Interacts directly with NUP96. Part of the Nup160 subcomplex in the nuclear pore which is composed of NUP160, NUP133, NUP107 and NUP96; this complex plays a role in RNA export and in tethering NUP98 and NUP153 to the nucleus. Interacts with RAE1. Does not interact with TPR (By similarity). Interacts directly with NUP88 and NUP214, subunits of the cytoplasmic filaments of the NPC (PubMed:22480613). Interacts (via N-terminus) with DHX9 (via DRBM, OB-fold and RGG domains); this interaction occurs in a RNA-dependent manner and stimulates DHX9-mediated ATPase activity (By similarity). {ECO:0000250|UniProtKB:P52948, ECO:0000269|PubMed:22480613}. DOMAIN: Contains G-L-F-G repeats. The FG repeat domains have a direct role in the transport (By similarity). {ECO:0000250}. +Q8BML2 OACYL_MOUSE O-acyltransferase like protein (Protein oacyl) 685 76,543 Alternative sequence (1); Chain (1); Sequence conflict (5); Signal peptide (1); Transmembrane (11) TRANSMEM 167 187 Helical. {ECO:0000255}.; TRANSMEM 281 301 Helical. {ECO:0000255}.; TRANSMEM 325 345 Helical. {ECO:0000255}.; TRANSMEM 378 398 Helical. {ECO:0000255}.; TRANSMEM 429 449 Helical. {ECO:0000255}.; TRANSMEM 456 476 Helical. {ECO:0000255}.; TRANSMEM 511 531 Helical. {ECO:0000255}.; TRANSMEM 538 558 Helical. {ECO:0000255}.; TRANSMEM 579 599 Helical. {ECO:0000255}.; TRANSMEM 607 627 Helical. {ECO:0000255}.; TRANSMEM 646 666 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. +A3KGV1 ODFP2_MOUSE Outer dense fiber protein 2 (84 kDa outer dense fiber protein) (Cenexin) (Outer dense fiber of sperm tails protein 2) 830 95,541 Alternative sequence (6); Chain (1); Coiled coil (3); Cross-link (1); Modified residue (13); Sequence conflict (1) FUNCTION: Seems to be a major component of sperm tail outer dense fibers (ODF). ODFs are filamentous structures located on the outside of the axoneme in the midpiece and principal piece of the mammalian sperm tail and may help to maintain the passive elastic structures and elastic recoil of the sperm tail. May have a modulating influence on sperm motility. Functions as a general scaffold protein that is specifically localized at the distal/subdistal appendages of mother centrioles. Component of the centrosome matrix required for the localization of PLK1 and NIN to the centrosomes. Required for the formation and/or maintenance of normal CETN1 assembly (By similarity). {ECO:0000250, ECO:0000269|PubMed:15852003}. PTM: Tyrosine phosphorylated (By similarity). Phosphorylated on Ser-95 by TSSK4 (PubMed:26961893). {ECO:0000250|UniProtKB:Q2MJU7, ECO:0000269|PubMed:26961893}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:15852003, ECO:0000269|PubMed:23386061}. Cell projection, cilium {ECO:0000269|PubMed:15852003}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:15852003}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:15852003}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:27682589}. Note=Localized at the microtubule organizing centers in interphase and spindle poles in mitosis. Localized at the distal/subdistal appendages of mother centrioles. {ECO:0000269|PubMed:15852003}. SUBUNIT: Self-associates. Associates with microtubules and forms a fibrillar structure partially linked to the microtubule network. Interacts via its C-terminus with PLK1 (By similarity). Interacts with ODF1 (PubMed:9045620). Interacts with MARK4; the interaction is required for localization of ODF2 to centrioles (By similarity). Interacts with TSSK4 (PubMed:25361759, PubMed:26961893). {ECO:0000250|UniProtKB:Q5BJF6, ECO:0000269|PubMed:25361759, ECO:0000269|PubMed:26961893, ECO:0000269|PubMed:9045620}. TISSUE SPECIFICITY: Testis-specific (at protein level) (PubMed:9045620, PubMed:27682589). Expressed in spermatids at tubular stage V of the spermatogenic cycle (PubMed:9740324). Highly expressed in the cytoplasm of elongating spermatids (tubular stages X/XI) (PubMed:9740324). In step 14/15 spermatids of tubular stage III/IV low expression detected (PubMed:9740324). No expression detected in other testicular cells as well as the early round of spermatids (PubMed:9740324). {ECO:0000269|PubMed:27682589, ECO:0000269|PubMed:9045620, ECO:0000269|PubMed:9740324}. +Q5M8M2 ODF3B_MOUSE Outer dense fiber protein 3B (Outer dense fiber protein 3-like protein 3) 238 25,923 Chain (1); Repeat (1) +P53395 ODB2_MOUSE Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial (EC 2.3.1.168) (Branched-chain alpha-keto acid dehydrogenase complex component E2) (BCKAD-E2) (BCKADE2) (Dihydrolipoamide acetyltransferase component of branched-chain alpha-keto acid dehydrogenase complex) (Dihydrolipoamide branched chain transacylase) (Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase) 482 53,247 Active site (2); Chain (1); Domain (2); Modified residue (16); Sequence conflict (1); Transit peptide (1) FUNCTION: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). Within this complex, the catalytic function of this enzyme is to accept, and to transfer to coenzyme A, acyl groups that are generated by the branched-chain alpha-keto acid decarboxylase component. SUBCELLULAR LOCATION: Mitochondrion matrix. SUBUNIT: Forms a 24-polypeptide structural core with octahedral symmetry. +Q60862 ORC2_MOUSE Origin recognition complex subunit 2 576 65,893 Chain (1); Modified residue (3); Repeat (1) FUNCTION: Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. The specific DNA sequences that define origins of replication have not been identified yet. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication (By similarity). Binds histone H3 and H4 trimethylation marks H3K9me3, H3K20me3 and H4K27me3. Stabilizes LRWD1, by protecting it from ubiquitin-mediated proteasomal degradation. Also stabilizes ORC3 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Component of ORC, a complex composed of at least 6 subunits: ORC1, ORC2, ORC3, ORC4, ORC5 and ORC6. ORC is regulated in a cell-cycle dependent manner. It is sequentially assembled at the exit from anaphase of mitosis and disassembled as cells enter S phase (By similarity). Interacts with DBF4 (PubMed:12614612). Interacts with MCM10. Interacts with LRWD1 throughout the cell cycle; this interaction, wich occurs only with non-ubiquitinated form of LRWD1, prevents LRWD1 ubiquitination and hence stabilizes the protein. Interacts with POLQ (By similarity). {ECO:0000250|UniProtKB:Q13416, ECO:0000269|PubMed:12614612}. +Q8C2E4 PTCD1_MOUSE Pentatricopeptide repeat-containing protein 1, mitochondrial 695 77,594 Chain (1); Compositional bias (1); Repeat (10); Sequence conflict (10) FUNCTION: Mitochondrial protein implicated in negative regulation of leucine tRNA levels, as well as negative regulation of mitochondria-encoded proteins and COX activity. Affects also the 3'-processing of mitochondrial tRNAs. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Mitochondrion matrix {ECO:0000250}. SUBUNIT: Associates with mitochondrial leucine tRNAs. Interacts with ELAC2. {ECO:0000250}. +P0C6B2 PTCRA_MOUSE Pre T-cell antigen receptor alpha (pT-alpha) (pTa) (gp33) (pT-alpha-TCR) 199 21,491 Alternative sequence (1); Chain (1); Compositional bias (1); Disulfide bond (2); Erroneous initiation (3); Glycosylation (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 147 167 Helical. {ECO:0000255}. TOPO_DOM 17 146 Extracellular. {ECO:0000255}.; TOPO_DOM 168 199 Cytoplasmic. {ECO:0000255}. FUNCTION: The pre-T-cell receptor complex (composed of PTCRA, TCRB and the CD3 complex) regulates early T-cell development. Isoform 1 acts to retain most TCRB intracellularly, while isoform 2 permits higher levels of cell surface TCRB expression and facilitates signaling from the CD3-TCRB complex. {ECO:0000269|PubMed:9647201}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Interacts with RHBDD1 (By similarity). Heterodimer with TCRB; disulfide linked. This heterodimer assembles with CD3 proteins into a signaling-competent pre-T-cell receptor complex. {ECO:0000250, ECO:0000269|PubMed:7973703}. TISSUE SPECIFICITY: Isoform 1 is expressed at higher levels than isoform 2 in the thymus while only isoform 2 is expressed in polyclonal beta-only cells. Isoform 1 shows a predominant expression in immature thymocytes. {ECO:0000269|PubMed:7973703, ECO:0000269|PubMed:9647201}. +O88708 ORC4_MOUSE Origin recognition complex subunit 4 433 49,982 Chain (1); Modified residue (1); Nucleotide binding (1); Sequence conflict (1) FUNCTION: Binds histone H3 and H4 trimethylation marks H3K9me3, H3K27me3 and H4K20me3 (By similarity). Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. The specific DNA sequences that define origins of replication have not been identified yet. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Component of ORC, a complex composed of at least 6 subunits: ORC1, ORC2, ORC3, ORC4, ORC5 and ORC6. ORC is regulated in a cell-cycle dependent manner. It is sequentially assembled at the exit from anaphase of mitosis and disassembled as cells enter S phase (By similarity). Interacts with DBF4 (PubMed:12614612). Interacts with POLQ (By similarity). {ECO:0000250|UniProtKB:O43929, ECO:0000269|PubMed:12614612}. +Q9WUV0 ORC5_MOUSE Origin recognition complex subunit 5 435 50,217 Chain (1); Nucleotide binding (1) FUNCTION: Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. The specific DNA sequences that define origins of replication have not been identified yet. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Component of ORC, a complex composed of at least 6 subunits: ORC1, ORC2, ORC3, ORC4, ORC5 and ORC6. ORC is regulated in a cell-cycle dependent manner. It is sequentially assembled at the exit from anaphase of mitosis and disassembled as cells enter S phase (By similarity). {ECO:0000250}. +O08586 PTEN_MOUSE Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN (EC 3.1.3.16) (EC 3.1.3.48) (EC 3.1.3.67) (Mutated in multiple advanced cancers 1) (Phosphatase and tensin homolog) 403 47,152 Active site (1); Chain (1); Cross-link (2); Domain (2); Initiator methionine (1); Modified residue (10); Region (2); Sequence conflict (1) FUNCTION: In motile cells, suppresses the formation of lateral pseudopods and thereby promotes cell polarization and directed movement (By similarity). Tumor suppressor. Acts as a dual-specificity protein phosphatase, dephosphorylating tyrosine-, serine- and threonine-phosphorylated proteins. Also acts as a lipid phosphatase, removing the phosphate in the D3 position of the inositol ring from phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 3,4-diphosphate, phosphatidylinositol 3-phosphate and inositol 1,3,4,5-tetrakisphosphate with order of substrate preference in vitro PtdIns(3,4,5)P3 > PtdIns(3,4)P2 > PtdIns3P > Ins(1,3,4,5)P4. The lipid phosphatase activity is critical for its tumor suppressor function. Antagonizes the PI3K-AKT/PKB signaling pathway by dephosphorylating phosphoinositides and thereby modulating cell cycle progression and cell survival. The unphosphorylated form cooperates with AIP1 to suppress AKT1 activation. Dephosphorylates tyrosine-phosphorylated focal adhesion kinase and inhibits cell migration and integrin-mediated cell spreading and focal adhesion formation. Plays a role as a key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation. May be a negative regulator of insulin signaling and glucose metabolism in adipose tissue. The nuclear monoubiquitinated form possesses greater apoptotic potential, whereas the cytoplasmic nonubiquitinated form induces less tumor suppressive ability. {ECO:0000250, ECO:0000269|PubMed:10339565, ECO:0000269|PubMed:19778506}. PTM: Constitutively phosphorylated by CK2 under normal conditions. Phosphorylation results in an inhibited activity towards PIP3. Phosphorylation can both inhibit or promote PDZ-binding. Phosphorylation at Tyr-336 by FRK/PTK5 protects this protein from ubiquitin-mediated degradation probably by inhibiting its binding to NEDD4 (By similarity). Phosphorylation by PLK3 promotes its stability and prevents its degradation by the proteasome. Phosphorylation by ROCK1 is essential for its stability and activity. {ECO:0000250, ECO:0000269|PubMed:19473982, ECO:0000269|PubMed:20008297, ECO:0000269|PubMed:20940307}.; PTM: Monoubiquitinated; monoubiquitination is increased in presence of retinoic acid. Deubiquitinated by USP7; leading to its nuclear exclusion. Monoubiquitination of one of either Lys-13 and Lys-289 amino acid is sufficient to modulate PTEN compartmentalization (By similarity). Ubiquitinated by XIAP/BIRC4. {ECO:0000250, ECO:0000269|PubMed:19473982}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19473982, ECO:0000269|PubMed:25801959}. Nucleus {ECO:0000269|PubMed:19473982, ECO:0000269|PubMed:25801959}. Nucleus, PML body {ECO:0000250|UniProtKB:P60484}. Note=Monoubiquitinated form is nuclear (By similarity). Nonubiquitinated form is cytoplasmic (By similarity). Colocalized with PML and USP7 in PML nuclear bodies (By similarity). XIAP/BIRC4 promotes its nuclear localization (PubMed:19473982). {ECO:0000250|UniProtKB:P60484, ECO:0000269|PubMed:19473982}. SUBUNIT: Monomer. The unphosphorylated form interacts with the second PDZ domain of AIP1 (By similarity). Interacts with MAGI2, MAGI3, MAST1 and MAST3, but neither with MAST4 nor with DLG5; interaction with MAGI2 increases protein stability (By similarity). Interacts with NEDD4 (By similarity). Interacts with NDFIP1 and NDFIP2; in the presence of NEDD4 or ITCH, this interaction promotes PTEN ubiquitination (By similarity). Interacts (via C2 domain) with FRK (By similarity). Interacts with USP7; the interaction is direct (By similarity). Interacts with ROCK1 (PubMed:20008297). Interacts with XIAP/BIRC4 (PubMed:19473982). Interacts with STK11; the interaction phosphorylates PTEN (By similarity). Interacts with PPP1R16B (By similarity). Interacts with NOP53; regulates PTEN phosphorylation and increases its stability (By similarity). {ECO:0000250|UniProtKB:P60484, ECO:0000269|PubMed:19473982, ECO:0000269|PubMed:20008297}. +Q60866 PTER_MOUSE Phosphotriesterase-related protein (EC 3.1.-.-) (Parathion hydrolase-related protein) 349 39,218 Alternative sequence (2); Chain (1); Metal binding (7); Sequence conflict (1) TISSUE SPECIFICITY: Expressed in kidney and liver. +Q9QX98 PTF1A_MOUSE Pancreas transcription factor 1 subunit alpha (Pancreas-specific transcription factor 1a) (bHLH transcription factor p48) (p48 DNA-binding subunit of transcription factor PTF1) (PTF1-p48) 324 35,185 Chain (1); Domain (1); Sequence conflict (3) FUNCTION: Transcription factor implicated in the cell fate determination in various organs. Binds to the E-box consensus sequence 5'-CANNTG-3'. Plays a role in early and late pancreas development and differentiation. Important for determining whether cells allocated to the pancreatic buds continue towards pancreatic organogenesis or revert back to duodenal fates. May be involved in the maintenance of exocrine pancreas-specific gene expression including ELA1 and amylase. Required for the formation of pancreatic acinar and ductal cells. Plays an important role in cerebellar development. Directly regulated by FOXN4 and RORC during retinal development, FOXN4-PTF1A pathway plays a central role in directing the differentiation of retinal progenitors towards horizontal and amacrine fates. {ECO:0000269|PubMed:11562365, ECO:0000269|PubMed:12185368, ECO:0000269|PubMed:15543146, ECO:0000269|PubMed:17075007, ECO:0000269|PubMed:9851981}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=In the cytoplasm loses its ability to form the PTF1 complex. SUBUNIT: Component of the pancreas transcription factor 1 complex (PTF1) which is composed of TCF3/p75, TCF12/p64 and PTF1A/p48. TCF3 is responsible for the nuclear import of the p48/p64 complex. Interacts with TCF3 and RBPSUH/RBP-Jkappa. {ECO:0000269|PubMed:11318877, ECO:0000269|PubMed:11562365}. TISSUE SPECIFICITY: Expressed in precursors of pancreatic islets, acini and ducts. {ECO:0000269|PubMed:9851981}. +Q8CI95 OSB11_MOUSE Oxysterol-binding protein-related protein 11 (ORP-11) (OSBP-related protein 11) 751 83,629 Chain (1); Domain (1); Erroneous initiation (1); Modified residue (9) FUNCTION: Plays a role in regulating ADIPOQ and FABP4 levels in differentiating adipocytes and is also involved in regulation of adipocyte triglyceride storage. Weakly binds 25-hydroxycholesterol. {ECO:0000250|UniProtKB:Q9BXB4}. SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250}. Note=Localizes at the Golgi-late endosome interface. {ECO:0000250}. SUBUNIT: Heterodimer with OSBPL9. {ECO:0000250}. DOMAIN: The PH domain binds phosphoinositides. {ECO:0000250}. +P35235 PTN11_MOUSE Tyrosine-protein phosphatase non-receptor type 11 (EC 3.1.3.48) (Protein-tyrosine phosphatase SYP) (SH-PTP2) (SHP-2) (Shp2) 597 68,460 Active site (1); Alternative sequence (1); Beta strand (6); Binding site (2); Chain (1); Domain (3); Helix (3); Initiator methionine (1); Modified residue (5); Region (1); Sequence conflict (1); Turn (1) FUNCTION: Acts downstream of various receptor and cytoplasmic protein tyrosine kinases to participate in the signal transduction from the cell surface to the nucleus. Positively regulates MAPK signal transduction pathway. Dephosphorylates GAB1, ARHGAP35 and EGFR. Dephosphorylates ROCK2 at 'Tyr-722' resulting in stimulatation of its RhoA binding activity. Dephosphorylates CDC73. {ECO:0000250|UniProtKB:Q06124, ECO:0000269|PubMed:14967142}. PTM: Phosphorylated on Tyr-546 and Tyr-584 upon receptor protein tyrosine kinase activation; which creates a binding site for GRB2 and other SH2-containing proteins. Phosphorylated upon activation of the receptor-type kinase FLT3. Phosphorylated by activated PDGFRB (By similarity). Phosphorylated upon activation of the receptor-type kinase PDGFRA. {ECO:0000250, ECO:0000269|PubMed:10080542, ECO:0000269|PubMed:16885344, ECO:0000269|PubMed:8943348}. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Interacts with CD84 and with phosphorylated SIT1 and MZPL1. Interacts with FCRL4, FCRL6 and ANKHD1. Interacts with GAREM1 (tyrosine phosphorylated); the interaction increases MAPK/ERK activity and does not affect the GRB2/SOS complex formation (By similarity). Interacts with PTPNS1 and BCAR3. Interacts with phosphorylated LIME1. Interacts with SHB and INPP5D/SHIP1. Interacts with KIR2DL1; the interaction is enhanced by ARRB2 (By similarity). Interacts with GAB2. Interacts with TERT; the interaction retains TERT in the nucleus. Interacts with PECAM1 and FER. Interacts with EPHA2 (activated); participates in PTK2/FAK1 dephosphorylation in EPHA2 downstream signaling (By similarity). Interacts with MILR1 (tyrosine phosphorylated). Interacts with FLT1 (tyrosine-phosphorylated), FLT3 (tyrosine-phosphorylated), FLT4 (tyrosine-phosphorylated), KIT and GRB2. Interacts with ROS1; mediates PTPN11 phosphorylation. Interacts with PDGFRA (tyrosine phosphorylated). Interacts with PDGFRB (tyrosine phosphorylated); this interaction increases the PTPN11 phosphatase activity. Interacts (via SH2 domain) with TEK/TIE2 (tyrosine phosphorylated). Interacts with CEACAM1 (via cytoplasmic domain); this interaction depends on the monomer/dimer equilibrium and is phosphorylation-dependent (PubMed:19948503, PubMed:9867848). Interacts with MPIG6B (via ITIM motif) (PubMed:23112346). Interacts with SIGLEC10 (PubMed:23374343). {ECO:0000250|UniProtKB:P41499, ECO:0000250|UniProtKB:Q06124, ECO:0000269|PubMed:10068651, ECO:0000269|PubMed:10080542, ECO:0000269|PubMed:10521483, ECO:0000269|PubMed:10896938, ECO:0000269|PubMed:12181353, ECO:0000269|PubMed:14610044, ECO:0000269|PubMed:16684964, ECO:0000269|PubMed:16885344, ECO:0000269|PubMed:19948503, ECO:0000269|PubMed:20526344, ECO:0000269|PubMed:23112346, ECO:0000269|PubMed:23374343, ECO:0000269|PubMed:7521735, ECO:0000269|PubMed:8943348, ECO:0000269|PubMed:9062191, ECO:0000269|PubMed:9110989, ECO:0000269|PubMed:9393882, ECO:0000269|PubMed:9528781, ECO:0000269|PubMed:9722576, ECO:0000269|PubMed:9867848}. DOMAIN: The SH2 domains repress phosphatase activity. Binding of these domains to phosphotyrosine-containing proteins relieves this auto-inhibition, possibly by inducing a conformational change in the enzyme. TISSUE SPECIFICITY: Highly expressed in brain, heart and kidney. {ECO:0000269|PubMed:7681217}. +Q8BX94 OSBL2_MOUSE Oxysterol-binding protein-related protein 2 (ORP-2) (OSBP-related protein 2) 484 55,384 Chain (1); Modified residue (2); Sequence conflict (1) FUNCTION: Binds phospholipids; exhibits strong binding to phosphatidic acid and weak binding to phosphatidylinositol 3-phosphate. Binds 25-hydroxycholesterol. {ECO:0000250|UniProtKB:Q9H1P3}. SUBUNIT: Interacts with DIAPH1. {ECO:0000250|UniProtKB:Q9H1P3}. +A2ARM1 PATL2_MOUSE Protein PAT1 homolog 2 (PAT1-like protein 2) (Protein PAT1 homolog a) (Pat1a) 529 59,639 Chain (1); Frameshift (1); Sequence conflict (7) FUNCTION: RNA-binding protein that acts as a translational repressor. {ECO:0000250|UniProtKB:Q4V7K4}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20826699}. Nucleus {ECO:0000269|PubMed:20826699}. SUBUNIT: Interacts with LSM1. {ECO:0000250|UniProtKB:C9JE40}. +Q925B0 PAWR_MOUSE PRKC apoptosis WT1 regulator protein (Prostate apoptosis response 4 protein) (Par-4) 333 35,908 Alternative sequence (1); Chain (1); Coiled coil (1); Modified residue (2); Motif (2); Region (2) FUNCTION: Pro-apoptopic protein capable of selectively inducing apoptosis in cancer cells, sensitizing the cells to diverse apoptotic stimuli and causing regression of tumors in animal models. Induces apoptosis in certain cancer cells by activation of the Fas prodeath pathway and coparallel inhibition of NF-kappa-B transcriptional activity. Inhibits the transcriptional activation and augments the transcriptional repression mediated by WT1. Down-regulates the anti-apoptotic protein BCL2 via its interaction with WT1. Seems also to be a transcriptional repressor by itself. May be directly involved in regulating the amyloid precursor protein (APP) cleavage activity of BACE1 (By similarity). {ECO:0000250, ECO:0000269|PubMed:15606896}. PTM: Preferentially phosphorylated at the Thr-156 by PKC in cancer cells. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Mainly cytoplasmic in absence of apoptosis signal and in normal cells. Nuclear in most cancer cell lines. Nuclear entry seems to be essential but not sufficient for apoptosis. Nuclear localization includes nucleoplasm and PML nuclear bodies (By similarity). {ECO:0000250}. SUBUNIT: Homooligomer. Interacts (via the C-terminal region) with WT1. Interacts with THAP1. Interacts with AATF. Interacts with BACE1. Interacts with SPSB1 (via B30.2/SPRY domain); this interaction is direct and occurs in association with the Elongin BC complex (PubMed:16369487, PubMed:20561531). Interacts with SPSB2 (via B30.2/SPRY domain); this interaction occurs in association with the Elongin BC complex (PubMed:16369487, PubMed:20561531). Interacts with SPSB4 (via B30.2/SPRY domain); this interaction occurs in association with the Elongin BC complex (PubMed:16369487, PubMed:20561531). Component of a ternary complex composed of SQSTM1 and PRKCZ (By similarity). Interacts with actin (By similarity). {ECO:0000250|UniProtKB:Q62627, ECO:0000250|UniProtKB:Q96IZ0}. DOMAIN: The leucine-zipper domain is not essential for apoptosis, but is required for sensitization of cells to exogenous apoptotic insults and for interaction with its partners. {ECO:0000250}.; DOMAIN: The SAC domain is a death-inducing domain selective for apoptosis induction in cancer cells. This domain is essential for nuclear entry, Fas activation, inhibition of NF-kappa-B activity and induction of apoptosis in cancer cells (By similarity). {ECO:0000250}.; DOMAIN: The B30.2/SPRY domain-binding motif mediates recognition by proteins containing a B30.2/SPRY domain. {ECO:0000250|UniProtKB:Q96IZ0}. +Q8BSQ9 PB1_MOUSE Protein polybromo-1 (BRG1-associated factor 180) (BAF180) 1634 187,188 Alternative sequence (1); Beta strand (2); Chain (1); Compositional bias (2); Cross-link (19); DNA binding (1); Domain (8); Erroneous initiation (1); Helix (6); Modified residue (20); Sequence caution (2); Sequence conflict (2); Turn (1) FUNCTION: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Required for the stability of the SWI/SNF chromatin remodeling complex SWI/SNF-B (PBAF). Acts as a negative regulator of cell proliferation. {ECO:0000250|UniProtKB:Q86U86, ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}. SUBUNIT: Component of the SWI/SNF-B (PBAF) chromatin remodeling complex, at least composed of SMARCA4/BRG1, SMARCB1/BAF47/SNF5, ACTL6A/BAF53A or ACTL6B/BAF53B, SMARCE1/BAF57, SMARCD1/BAF60A, SMARCD2/BAF60B, perhaps SMARCD3/BAF60C, SMARCC1/BAF155, SMARCC2/BAF170, PBRM1/BAF180, ARID2/BAF200 and actin. Interacts with PHF10/BAF45A (By similarity). Interacts with acetylated 'Lys-14' of histone H3 (H3K14ac), and may also interact with other acetylated or methylated Lys residues on histone H3 (By similarity). {ECO:0000250|UniProtKB:Q86U86, ECO:0000269|PubMed:17640523, ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}. +P47239 PAX7_MOUSE Paired box protein Pax-7 503 54,939 Chain (1); DNA binding (1); Domain (1); Motif (1); Region (1); Sequence conflict (4) FUNCTION: Transcription factor playing a role in myogenesis through regulation of muscle precursor cells proliferation. {ECO:0000269|PubMed:22862948}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22862948}. SUBUNIT: Can bind to DNA as a heterodimer with PAX3. Interacts with DAXX (By similarity). Interacts with PAXBP1; the interaction links PAX7 to a WDR5-containing histone methyltransferase complex (PubMed:22862948). {ECO:0000250|UniProtKB:P23759, ECO:0000269|PubMed:22862948}. +Q00288 PAX8_MOUSE Paired box protein Pax-8 457 48,793 Chain (1); Compositional bias (1); Domain (1); Modified residue (1); Sequence conflict (1) FUNCTION: Thought to encode a transcription factor. It may have a role in kidney cell differentiation. May play a regulatory role in mammalian development. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with WWTR1. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the developing excretory system and the thyroid gland. +P54822 PUR8_MOUSE Adenylosuccinate lyase (ASL) (EC 4.3.2.2) (Adenylosuccinase) (ASase) 484 54,866 Active site (2); Binding site (5); Chain (1); Cross-link (1); Initiator methionine (1); Modified residue (3); Region (3); Sequence conflict (2) Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 2/2. Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 2/2. FUNCTION: Catalyzes two non-sequential steps in de novo AMP synthesis: converts (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate (SAICAR) to fumarate plus 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide, and thereby also contributes to de novo IMP synthesis, and converts succinyladenosine monophosphate (SAMP) to AMP and fumarate. {ECO:0000250|UniProtKB:P30566}. SUBUNIT: Homotetramer. Residues from neighboring subunits contribute catalytic and substrate-binding residues to each active site. {ECO:0000250|UniProtKB:P30566}. +P57724 PCBP4_MOUSE Poly(rC)-binding protein 4 (Alpha-CP4) 403 41,399 Chain (1); Domain (3); Sequence conflict (1) FUNCTION: Single-stranded nucleic acid binding protein that binds preferentially to oligo dC. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed, with highest levels in testis and lowest in heart. {ECO:0000269|PubMed:10936052}. +Q8BIZ0 PCD20_MOUSE Protocadherin-20 952 104,737 Chain (1); Domain (6); Erroneous initiation (1); Glycosylation (8); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 892 912 Helical. {ECO:0000255}. TOPO_DOM 61 891 Extracellular. {ECO:0000255}.; TOPO_DOM 913 952 Cytoplasmic. {ECO:0000255}. FUNCTION: Potential calcium-dependent cell-adhesion protein. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. +Q91XY4 PCDG4_MOUSE Protocadherin gamma-A4 (PCDH-gamma-A4) 930 100,358 Beta strand (35); Chain (1); Domain (6); Glycosylation (2); Helix (5); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (5) TRANSMEM 692 712 Helical. {ECO:0000255}. TOPO_DOM 28 691 Extracellular. {ECO:0000255}.; TOPO_DOM 713 930 Cytoplasmic. {ECO:0000255}. FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain (By similarity). {ECO:0000250|UniProtKB:Q9Y5H4}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O88689}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:O88689}. +P23798 PCGF2_MOUSE Polycomb group RING finger protein 2 (DNA-binding protein Mel-18) (Melanoma nuclear protein 18) (RING finger protein 110) (Zinc finger protein 144) (Zfp-144) 342 37,723 Chain (1); Compositional bias (1); Cross-link (2); Modified residue (2); Motif (1); Zinc finger (1) FUNCTION: Transcriptional repressor (PubMed:8521824). Binds specifically to the DNA sequence 5'-GACTNGACT-3' (PubMed:8521824). Has tumor suppressor activity (PubMed:8521824). May play a role in control of cell proliferation and/or neural cell development (Probable). Regulates proliferation of early T progenitor cells by maintaining expression of HES1(PubMed:15728456). Also plays a role in antero-posterior specification of the axial skeleton and negative regulation of the self-renewal activity of hematopoietic stem cells (PubMed:8625838, PubMed:15183898). Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. Within the PRC1-like complex, regulates RNF2 ubiquitin ligase activity (By similarity). {ECO:0000250|UniProtKB:P35227, ECO:0000269|PubMed:11750047, ECO:0000269|PubMed:15183898, ECO:0000269|PubMed:15728456, ECO:0000269|PubMed:8521824, ECO:0000269|PubMed:8625838, ECO:0000305}. PTM: Phosphorylated. Homodimer formation is regulated by phosphorylation with only unphosphorylated proteins forming homodimers. {ECO:0000269|PubMed:12480532}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:2246278}. SUBUNIT: Exists as both a monomer and homodimer (PubMed:12480532). Component of a PRC1-like complex. Interacts with CBX8, RING1 AND RNF2 (By similarity). Interacts with CBX7 (PubMed:22226355). Interacts with PHC2 (PubMed:16024804). {ECO:0000250|UniProtKB:P35227, ECO:0000269|PubMed:12480532, ECO:0000269|PubMed:22226355}. TISSUE SPECIFICITY: Expressed in embryonic stem cells (PubMed:22226355). Expressed in a variety of tumor cells and in neural tissues (PubMed:2246278). {ECO:0000269|PubMed:22226355, ECO:0000269|PubMed:2246278}. DISEASE: Note=Probably related to tumorigenesis since it is expressed strongly in most tumor cell lines. +Q3UBG2 PCLI1_MOUSE PTB-containing, cubilin and LRP1-interacting protein (P-CLI1) (Phosphotyrosine interaction domain-containing protein 1) 217 24,784 Alternative sequence (1); Chain (1); Domain (1); Erroneous initiation (4); Modified residue (3); Sequence conflict (1) FUNCTION: Increases proliferation of preadipocytes without affecting adipocytic differentiation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Found in a complex with PID1/PCLI1, LRP1 and CUBNI. Interacts with LRP1 and CUBN. {ECO:0000250}. +Q8R4W6 PCOC2_MOUSE Procollagen C-endopeptidase enhancer 2 (Procollagen COOH-terminal proteinase enhancer 2) (PCPE-2) (Procollagen C-proteinase enhancer 2) 414 45,408 Chain (1); Compositional bias (1); Disulfide bond (7); Domain (3); Glycosylation (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Binds to the C-terminal propeptide of types I and II procollagens and may enhance the cleavage of that propeptide by BMP1. {ECO:0000250}. PTM: O-glycosylated; contains sialic acid. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. SUBUNIT: Interacts with heparin with high affinity, and type I or II collagen. {ECO:0000250}. +Q61139 PCSK7_MOUSE Proprotein convertase subtilisin/kexin type 7 (EC 3.4.21.-) (Prohormone convertase 7) (Proprotein convertase 7) (PC7) (Subtilisin-like proprotein convertase 7) (SPC7) (Subtilisin/kexin-like protease PC7) 770 84,358 Active site (3); Chain (1); Domain (2); Glycosylation (4); Propeptide (1); Sequence conflict (1); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 667 687 Helical. {ECO:0000255}. TOPO_DOM 141 666 Extracellular. {ECO:0000255}.; TOPO_DOM 688 770 Cytoplasmic. {ECO:0000255}. FUNCTION: Serine endoprotease that processes various proproteins by cleavage at paired basic amino acids, recognizing the RXXX[KR]R consensus motif. Likely functions in the constitutive secretory pathway. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Seems to be localized intracellularly to the trans Golgi network. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. Expressed in brain, lung, muscle, heart, liver, kidney, spleen and thymus. +Q80W65 PCSK9_MOUSE Proprotein convertase subtilisin/kexin type 9 (EC 3.4.21.-) (Neural apoptosis-regulated convertase 1) (NARC-1) (Proprotein convertase 9) (PC9) (Subtilisin/kexin-like protease PC9) 694 74,823 Active site (3); Chain (1); Disulfide bond (11); Domain (1); Erroneous initiation (3); Glycosylation (1); Modified residue (3); Motif (1); Propeptide (1); Region (1); Sequence conflict (8); Signal peptide (1); Site (2) FUNCTION: Crucial player in the regulation of plasma cholesterol homeostasis. Binds to low-density lipid receptor family members: low density lipoprotein receptor (LDLR), very low density lipoprotein receptor (VLDLR), apolipoprotein E receptor (LRP1/APOER) and apolipoprotein receptor 2 (LRP8/APOER2), and promotes their degradation in intracellular acidic compartments. Acts via a non-proteolytic mechanism to enhance the degradation of the hepatic LDLR through a clathrin LDLRAP1/ARH-mediated pathway. May prevent the recycling of LDLR from endosomes to the cell surface or direct it to lysosomes for degradation. Can induce ubiquitination of LDLR leading to its subsequent degradation. Inhibits intracellular degradation of APOB via the autophagosome/lysosome pathway in a LDLR-independent manner. Involved in the disposal of non-acetylated intermediates of BACE1 in the early secretory pathway. Inhibits epithelial Na(+) channel (ENaC)-mediated Na(+) absorption by reducing ENaC surface expression primarily by increasing its proteasomal degradation. Regulates neuronal apoptosis via modulation of LRP8/APOER2 levels and related anti-apoptotic signaling pathways. {ECO:0000269|PubMed:22481440, ECO:0000269|PubMed:22580899}. PTM: Cleavage by furin and PCSK5 generates a truncated inactive protein that is unable to induce LDLR degradation. {ECO:0000250}.; PTM: Undergoes autocatalytic cleavage in the endoplasmic reticulum to release the propeptide from the N-terminus and the cleavage of the propeptide is strictly required for its maturation and activation. The cleaved propeptide however remains associated with the catalytic domain through non-covalent interactions, preventing potential substrates from accessing its active site. As a result, it is secreted from cells as a propeptide-containing, enzymatically inactive protein (By similarity). {ECO:0000250}.; PTM: Phosphorylation protects the propeptide against proteolysis. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Secreted. Endosome {ECO:0000250}. Lysosome {ECO:0000250}. Cell surface {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Golgi apparatus {ECO:0000250}. Note=Autocatalytic cleavage is required to transport it from the endoplasmic reticulum to the Golgi apparatus and for the secretion of the mature protein. Localizes to the endoplasmic reticulum in the absence of LDLR and co-localizes to the cell surface and to the endosomes/lysosomes in the presence of LDLR. The sorting to the cell surface and endosomes is required in order to fully promote LDLR degradation (By similarity). {ECO:0000250}. SUBUNIT: Monomer. Can self-associate to form dimers and higher multimers which may have increased LDLR degrading activity. The precursor protein but not the mature protein may form multimers. Interacts with APOB, VLDLR, LRP8/APOER2 and BACE1. The full-length immature form (pro-PCSK9) interacts with SCNN1A, SCNN1B and SCNN1G. The pro-PCSK9 form (via C-terminal domain) interacts with LDLR. Interacts (via the C-terminal domain) with ANXA2 (via repeat Annexin 1); the interaction inhibits the degradation of LDLR. {ECO:0000250|UniProtKB:Q8NBP7}. DOMAIN: The C-terminal domain (CRD) is essential for the LDLR-binding and degrading activities. {ECO:0000250}.; DOMAIN: The catalytic domain is responsible for mediating its self-association. {ECO:0000250}. TISSUE SPECIFICITY: Hepatocytes, kidney mesenchymal cells, intestinal ileum, colon epithelia and embryonic brain telencephalon neurons. +Q5DU28 PCX2_MOUSE Pecanex-like protein 2 (Pecanex homolog protein 2) 2122 234,128 Alternative sequence (5); Chain (1); Compositional bias (1); Glycosylation (6); Transmembrane (15) TRANSMEM 36 53 Helical. {ECO:0000255}.; TRANSMEM 60 82 Helical. {ECO:0000255}.; TRANSMEM 825 845 Helical. {ECO:0000255}.; TRANSMEM 849 869 Helical. {ECO:0000255}.; TRANSMEM 882 902 Helical. {ECO:0000255}.; TRANSMEM 933 953 Helical. {ECO:0000255}.; TRANSMEM 976 998 Helical. {ECO:0000255}.; TRANSMEM 1010 1030 Helical. {ECO:0000255}.; TRANSMEM 1080 1100 Helical. {ECO:0000255}.; TRANSMEM 1105 1125 Helical. {ECO:0000255}.; TRANSMEM 1174 1194 Helical. {ECO:0000255}.; TRANSMEM 1218 1238 Helical. {ECO:0000255}.; TRANSMEM 1245 1265 Helical. {ECO:0000255}.; TRANSMEM 1270 1290 Helical. {ECO:0000255}.; TRANSMEM 1305 1325 Helical. {ECO:0000255}. FUNCTION: May play a role in tumorigenesis. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8VI59 PCX3_MOUSE Pecanex-like protein 3 (Pecanex homolog protein 3) 2028 221,573 Alternative sequence (1); Chain (1); Compositional bias (5); Glycosylation (3); Modified residue (11); Transmembrane (13) TRANSMEM 33 53 Helical. {ECO:0000255}.; TRANSMEM 54 74 Helical. {ECO:0000255}.; TRANSMEM 793 815 Helical. {ECO:0000255}.; TRANSMEM 819 836 Helical. {ECO:0000255}.; TRANSMEM 852 872 Helical. {ECO:0000255}.; TRANSMEM 880 900 Helical. {ECO:0000255}.; TRANSMEM 903 923 Helical. {ECO:0000255}.; TRANSMEM 946 968 Helical. {ECO:0000255}.; TRANSMEM 980 1000 Helical. {ECO:0000255}.; TRANSMEM 1053 1073 Helical. {ECO:0000255}.; TRANSMEM 1078 1098 Helical. {ECO:0000255}.; TRANSMEM 1244 1264 Helical. {ECO:0000255}.; TRANSMEM 1280 1300 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9CQF9 PCYOX_MOUSE Prenylcysteine oxidase (EC 1.8.3.5) 505 56,495 Chain (1); Glycosylation (3); Sequence conflict (1); Signal peptide (1) FUNCTION: Involved in the degradation of prenylated proteins. Cleaves the thioether bond of prenyl-L-cysteines, such as farnesylcysteine and geranylgeranylcysteine (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Lysosome {ECO:0000250}. +Q3UVY5 PCX4_MOUSE Pecanex-like protein 4 (Pecanex homolog protein 4) 1174 131,243 Alternative sequence (1); Chain (1); Erroneous initiation (3); Glycosylation (3); Sequence conflict (6); Transmembrane (14) TRANSMEM 40 60 Helical. {ECO:0000255}.; TRANSMEM 72 92 Helical. {ECO:0000255}.; TRANSMEM 140 160 Helical. {ECO:0000255}.; TRANSMEM 173 193 Helical. {ECO:0000255}.; TRANSMEM 217 237 Helical. {ECO:0000255}.; TRANSMEM 244 264 Helical. {ECO:0000255}.; TRANSMEM 284 304 Helical. {ECO:0000255}.; TRANSMEM 307 327 Helical. {ECO:0000255}.; TRANSMEM 366 386 Helical. {ECO:0000255}.; TRANSMEM 394 414 Helical. {ECO:0000255}.; TRANSMEM 451 471 Helical. {ECO:0000255}.; TRANSMEM 543 563 Helical. {ECO:0000255}.; TRANSMEM 580 600 Helical. {ECO:0000255}.; TRANSMEM 643 663 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8C7K6 PCYXL_MOUSE Prenylcysteine oxidase-like (EC 1.8.3.-) 495 54,875 Chain (1); Glycosylation (2); Signal peptide (1) FUNCTION: Probable oxidoreductase. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +Q8VE70 PDC10_MOUSE Programmed cell death protein 10 (TF-1 cell apoptosis-related protein 15) 212 24,716 Chain (1); Cross-link (1); Modified residue (1); Sequence conflict (3) FUNCTION: Promotes cell proliferation. Modulates apoptotic pathways. Increases mitogen-activated protein kinase activity and STK26 activity. Important for cell migration, and for normal structure and assembly of the Golgi complex (By similarity). Important for KDR/VEGFR2 signaling. Increases the stability of KDR/VEGFR2 and prevents its breakdown. Required for normal cardiovascular development. Required for normal angiogenesis, vasculogenesis and hematopoiesis during embryonic development (By similarity). {ECO:0000250|UniProtKB:Q9BUL8, ECO:0000269|PubMed:20371769}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:20371769}; Peripheral membrane protein {ECO:0000269|PubMed:20371769}; Cytoplasmic side {ECO:0000269|PubMed:20371769}. Note=Partially colocalizes with endogenous PXN at the leading edges of migrating cells. {ECO:0000250}. SUBUNIT: Homodimer. Interacts (via C-terminus) with CCM2. Interacts (via C-terminus) with PXN. Interacts (via N-terminus) with STK25. Interacts (via N-terminus) with STK26. Interacts (via N-terminus) with STK24. Interacts with GOLGA2. Identified in a complex with KRIT1 and CCM2. Interacts with KDR/VEGFR2 (By similarity). Interaction with KDR/VEGFR2 is enhanced by stimulation with VEGFA (PubMed:20371769). Interacts with RIPOR1 (via C-terminus); this interaction is required for the association of RIPOR1 with either STK24 and STK26 kinases and occurs in a Rho-independent manner (By similarity). {ECO:0000250|UniProtKB:Q9BUL8, ECO:0000269|PubMed:20371769}. +Q8C5N5 PDD2L_MOUSE Programmed cell death protein 2-like 364 39,955 Chain (1); Compositional bias (1); Initiator methionine (1); Modified residue (1); Sequence conflict (2) FUNCTION: Over-expression suppresses AP1, CREB, NFAT, and NF-kB transcriptional activation, and delays cell cycle progression at S phase. {ECO:0000250}. +Q01065 PDE1B_MOUSE Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B (Cam-PDE 1B) (EC 3.1.4.17) (63 kDa Cam-PDE) 535 61,226 Active site (1); Chain (1); Domain (1); Metal binding (5); Modified residue (4); Region (1); Sequence conflict (2) FUNCTION: Cyclic nucleotide phosphodiesterase with a dual-specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. Has a preference for cGMP as a substrate (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Homodimer. {ECO:0000250}. +Q9WTY1 PDCD7_MOUSE Programmed cell death protein 7 (ES18) 482 54,357 Chain (1); Coiled coil (1); Compositional bias (2) FUNCTION: Promotes apoptosis when overexpressed. {ECO:0000269|PubMed:10087507}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Interacts with RBM40. Component of the U11/U12 snRNPs that are part of the U12-type spliceosome (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in testis, thymus and lymph nodes. Detected at low levels in embryonic stem cells. +Q78Y63 PDCL2_MOUSE Phosducin-like protein 2 (MgcPhLP) (Phosducin-like protein similar 1) 240 27,770 Alternative sequence (1); Beta strand (5); Chain (1); Helix (3); Region (1); Sequence conflict (2); Turn (2) FUNCTION: May play a role in germ cell maturation. {ECO:0000269|PubMed:12424248}. SUBUNIT: Forms a complex with 14-3-3 protein(s). TISSUE SPECIFICITY: Predominantly, if not exclusively, expressed in male and female germ cells. In the male germ cells, expressed from the meiotic to the late haploid stages of spermatogenesis and in the mature spermatozoa of epididymal sperm (at protein level). Also detected in fertilized eggs (at protein level). {ECO:0000269|PubMed:12424248}. +Q922S4 PDE2A_MOUSE cGMP-dependent 3',5'-cyclic phosphodiesterase (EC 3.1.4.17) (Cyclic GMP-stimulated phosphodiesterase) (CGS-PDE) (cGSPDE) 939 105,619 Active site (1); Alternative sequence (3); Beta strand (12); Binding site (5); Chain (1); Domain (3); Frameshift (1); Helix (10); Initiator methionine (1); Lipidation (3); Metal binding (5); Modified residue (1); Region (1); Sequence conflict (1); Turn (3) FUNCTION: Cyclic nucleotide phosphodiesterase with a dual-specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. {ECO:0000250}.; FUNCTION: Isoform PDE2A2: Regulates mitochondrial cAMP levels and respiration (PubMed:21724846). Involved in the regulation of mitochondria morphology/dynamics and apoptotic cell death via local modulation of cAMP/PKA signaling in the mitochondrion, including the monitoring of local cAMP levels at the outer mitochondrial membrane and of PKA-dependent phosphorylation of DNM1L (PubMed:28463107). {ECO:0000269|PubMed:21724846, ECO:0000269|PubMed:28463107}. SUBCELLULAR LOCATION: Isoform PDE2A1: Cytoplasm {ECO:0000250|UniProtKB:O00408}.; SUBCELLULAR LOCATION: Isoform PDE2A2: Mitochondrion matrix {ECO:0000269|PubMed:21724846}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:O00408}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:O00408}.; SUBCELLULAR LOCATION: Isoform PDE2A3: Cell membrane {ECO:0000250|UniProtKB:O00408}; Lipid-anchor {ECO:0000250|UniProtKB:O00408}. SUBUNIT: Homodimer. {ECO:0000269|PubMed:12271124}. DOMAIN: GAF 1 functions as a dimerization domain, whereas GAF 2 binds cGMP, which causes activation of the catalytic activity of the enzyme. {ECO:0000269|PubMed:12271124}. TISSUE SPECIFICITY: Isoform PDE2A2: Expressed in brain and liver (at protein level). {ECO:0000269|PubMed:21724846}. +Q01063 PDE4D_MOUSE cAMP-specific 3',5'-cyclic phosphodiesterase 4D (EC 3.1.4.53) (DPDE3) 747 84,563 Active site (1); Alternative sequence (4); Binding site (1); Chain (1); Cross-link (1); Domain (1); Metal binding (5); Modified residue (4); Nucleotide binding (1); Sequence conflict (1); Site (1) Purine metabolism; 3',5'-cyclic AMP degradation; AMP from 3',5'-cyclic AMP: step 1/1. FUNCTION: Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. {ECO:0000250}. PTM: Sumoylation of long isoforms by PIAS4 augments their activation by PKA phosphorylation and represses their inhibition by ERK phosphorylation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Membrane. Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Apical cell membrane {ECO:0000250}. Note=Colocalized with SHANK2 to the apical membrane of colonic crypt cells (By similarity). Found in the soluble fraction, associated with membranes, and associated with the cytoskeleton and the centrosome. {ECO:0000250}. SUBUNIT: Homodimer for the long isoforms. Isoforms with truncated N-termini are monomeric. Binds ARRB2. Interacts with PDE4DIP (By similarity). Identified in a complex composed of RYR1, PDE4D, PKA, FKBP1A and protein phosphatase 1 (PP1). Interacts (via N-terminal region) with SHANK2 (via proline-rich region); the interaction is increased in a PKA-dependent manner. {ECO:0000250, ECO:0000269|PubMed:17244609, ECO:0000269|PubMed:18268335}. TISSUE SPECIFICITY: Expressed in brain (at protein level). Isoform 7 is detected in heart, brain, lung, kidney and testis. {ECO:0000269|PubMed:12834813, ECO:0000269|PubMed:17244609}. +P70453 PDE7A_MOUSE High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A (EC 3.1.4.53) (P2A) 456 52,486 Active site (1); Alternative sequence (1); Chain (1); Domain (1); Metal binding (5); Sequence conflict (1) Purine metabolism; 3',5'-cyclic AMP degradation; AMP from 3',5'-cyclic AMP: step 1/1. FUNCTION: Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. May have a role in muscle signal transduction (By similarity). {ECO:0000250}. SUBUNIT: Interacts with CBFA2T3. {ECO:0000250}. DOMAIN: Composed of a C-terminal catalytic domain containing two putative divalent metal sites and an N-terminal regulatory domain. TISSUE SPECIFICITY: Widely expressed with highest levels in the skeletal muscle. +Q9QXQ1 PDE7B_MOUSE cAMP-specific 3',5'-cyclic phosphodiesterase 7B (EC 3.1.4.53) 446 51,337 Active site (1); Chain (1); Domain (1); Metal binding (5); Modified residue (2) Purine metabolism; 3',5'-cyclic AMP degradation; AMP from 3',5'-cyclic AMP: step 1/1. FUNCTION: Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. May be involved in the control of cAMP-mediated neural activity and cAMP metabolism in the brain. DOMAIN: Composed of a C-terminal catalytic domain containing two putative divalent metal sites and an N-terminal regulatory domain. TISSUE SPECIFICITY: Highly expressed in brain. +Q922R8 PDIA6_MOUSE Protein disulfide-isomerase A6 (EC 5.3.4.1) (Thioredoxin domain-containing protein 7) 440 48,100 Beta strand (4); Chain (1); Compositional bias (1); Disulfide bond (2); Domain (2); Erroneous initiation (2); Helix (5); Modified residue (4); Motif (1); Sequence conflict (1); Signal peptide (1); Turn (4) FUNCTION: May function as a chaperone that inhibits aggregation of misfolded proteins (PubMed:24508390). Negatively regulates the unfolded protein response (UPR) through binding to UPR sensors such as ERN1, which in turn inactivates ERN1 signaling (By similarity). May also regulate the UPR via the EIF2AK3 UPR sensor (By similarity). Plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin (By similarity). {ECO:0000250|UniProtKB:Q15084, ECO:0000269|PubMed:24508390}. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:Q15084}. Cell membrane {ECO:0000250|UniProtKB:Q15084}. Melanosome {ECO:0000250|UniProtKB:Q15084}. SUBUNIT: Part of a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX. Interacts with MICA on the surface of tumor cells, leading to MICA disulfide bond reduction which is required for its release from tumor cells. Interacts with ITGB3 following platelet stimulation. Interacts with ERN1; the interaction is direct. Interacts with EIF2AK3. {ECO:0000250|UniProtKB:Q15084}. +Q91VA6 PDIP2_MOUSE Polymerase delta-interacting protein 2 368 41,870 Chain (1); Domain (1); Modified residue (1) SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Interacts with PCNA and POLD2. {ECO:0000250}. +D3Z6P0 PDIA2_MOUSE Protein disulfide-isomerase A2 (EC 5.3.4.1) (PDIp) 527 58,316 Active site (4); Alternative sequence (1); Chain (1); Disulfide bond (2); Domain (2); Glycosylation (3); Motif (1); Signal peptide (1); Site (5) FUNCTION: Acts as an intracellular estrogen-binding protein. May be involved in modulating cellular levels and biological functions of estrogens in the pancreas. May act as a chaperone that inhibits aggregation of misfolded proteins (By similarity). {ECO:0000250|UniProtKB:Q13087}. PTM: Glycosylated. {ECO:0000269|PubMed:9115635}. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:Q13087, ECO:0000255|PROSITE-ProRule:PRU10138}. SUBUNIT: Part of a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in pancreas. {ECO:0000269|PubMed:9115635}. +P31240 PDGFB_MOUSE Platelet-derived growth factor subunit B (PDGF subunit B) (PDGF-2) (Platelet-derived growth factor B chain) (Platelet-derived growth factor beta polypeptide) (Proto-oncogene c-Sis) 241 27,382 Chain (1); Disulfide bond (5); Glycosylation (1); Propeptide (2); Sequence conflict (2); Signal peptide (1); Site (2) FUNCTION: Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen for cells of mesenchymal origin. Required for normal proliferation and recruitment of pericytes and vascular smooth muscle cells in the central nervous system, skin, lung, heart and placenta. Required for normal blood vessel development, and for normal development of kidney glomeruli. Plays an important role in wound healing. Signaling is modulated by the formation of heterodimers with PDGFA. {ECO:0000269|PubMed:10734101, ECO:0000269|PubMed:14561699, ECO:0000269|PubMed:19030102, ECO:0000269|PubMed:7958863}. SUBCELLULAR LOCATION: Secreted. Note=Released by platelets upon wounding. {ECO:0000250}. SUBUNIT: Homodimer; antiparallel disulfide-linked dimer. Heterodimer with PDGFA; antiparallel disulfide-linked dimer. The PDGFB homodimer interacts with PDGFRA and PDGFRB homodimers, and with heterodimers formed by PDGFRA and PDGFRB. The heterodimer composed of PDGFA and PDGFB interacts with PDGFRB homodimers, and with heterodimers formed by PDGFRA and PDGFRB. Interacts with XLKD1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Localized to vascular smooth muscle cells. Also weakly expressed by cortical interstitial cells but absent in tubules. Up-regulated in areas of renal fibrosis. In mice with unilateral ureteral obstruction, an increased expression in interstitial cells and in some tubules observed after day 4. {ECO:0000269|PubMed:14514732}. +Q8R1G6 PDLI2_MOUSE PDZ and LIM domain protein 2 (PDZ-LIM protein mystique) 349 37,703 Beta strand (6); Chain (1); Domain (2); Helix (2); Modified residue (15); Turn (1) FUNCTION: Probable adapter protein located at the actin cytoskeleton that promotes cell attachment. Necessary for the migratory capacity of epithelial cells. Overexpression enhances cell adhesion to collagen and fibronectin and suppresses anchorage independent growth. May contribute to tumor cell migratory capacity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Note=Localizes at the cytoskeleton. Colocalizes with beta-1 integrin (ITGB1) and alpha-actinin but not with paxillin (PXN) (By similarity). {ECO:0000250}. SUBUNIT: Interacts with alpha-actinins ACTN1 and ACTN4, FLNA and MYH9. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in lung. Expressed at intermediate level in kidney, testis and spleen. Weakly expressed in heart and brain. {ECO:0000269|PubMed:15659642}. +O70571 PDK4_MOUSE [Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 4, mitochondrial (EC 2.7.11.2) (Pyruvate dehydrogenase kinase isoform 4) 412 46,596 Binding site (1); Chain (1); Domain (1); Nucleotide binding (3); Site (3); Transit peptide (1) FUNCTION: Kinase that plays a key role in regulation of glucose and fatty acid metabolism and homeostasis via phosphorylation of the pyruvate dehydrogenase subunits PDHA1 and PDHA2. This inhibits pyruvate dehydrogenase activity, and thereby regulates metabolite flux through the tricarboxylic acid cycle, down-regulates aerobic respiration and inhibits the formation of acetyl-coenzyme A from pyruvate. Inhibition of pyruvate dehydrogenase decreases glucose utilization and increases fat metabolism in response to prolonged fasting and starvation. Plays an important role in maintaining normal blood glucose levels under starvation, and is involved in the insulin signaling cascade. Via its regulation of pyruvate dehydrogenase activity, plays an important role in maintaining normal blood pH and in preventing the accumulation of ketone bodies under starvation. In the fed state, mediates cellular responses to glucose levels and to a high-fat diet. Regulates both fatty acid oxidation and de novo fatty acid biosynthesis. Plays a role in the generation of reactive oxygen species. Protects detached epithelial cells against anoikis. Plays a role in cell proliferation via its role in regulating carbohydrate and fatty acid metabolism. {ECO:0000269|PubMed:16606348, ECO:0000269|PubMed:18083902, ECO:0000269|PubMed:18430968, ECO:0000269|PubMed:19627255, ECO:0000269|PubMed:21321124, ECO:0000269|PubMed:22360721}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. SUBUNIT: Homodimer. Interacts with the pyruvate dehydrogenase complex subunit DLAT, and is part of the multimeric pyruvate dehydrogenase complex that contains multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3) (By similarity). {ECO:0000250}. +Q62053 PE2R2_MOUSE Prostaglandin E2 receptor EP2 subtype (PGE receptor EP2 subtype) (PGE2 receptor EP2 subtype) (Prostanoid EP2 receptor) 362 40,479 Chain (1); Disulfide bond (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 25 48 Helical; Name=1. {ECO:0000255}.; TRANSMEM 67 92 Helical; Name=2. {ECO:0000255}.; TRANSMEM 113 133 Helical; Name=3. {ECO:0000255}.; TRANSMEM 153 177 Helical; Name=4. {ECO:0000255}.; TRANSMEM 200 224 Helical; Name=5. {ECO:0000255}.; TRANSMEM 263 286 Helical; Name=6. {ECO:0000255}.; TRANSMEM 300 323 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 24 Extracellular. {ECO:0000255}.; TOPO_DOM 49 66 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 93 112 Extracellular. {ECO:0000255}.; TOPO_DOM 134 152 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 178 199 Extracellular. {ECO:0000255}.; TOPO_DOM 225 262 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 287 299 Extracellular. {ECO:0000255}.; TOPO_DOM 324 362 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for prostaglandin E2 (PGE2). The activity of this receptor is mediated by G(s) proteins that stimulate adenylate cyclase. The subsequent raise in intracellular cAMP is responsible for the relaxing effect of this receptor on smooth muscle. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q8VIK5 PEAR1_MOUSE Platelet endothelial aggregation receptor 1 (mPEAR1) (Jagged and Delta protein) (Protein Jedi) (Multiple epidermal growth factor-like domains protein 12) (Multiple EGF-like domains protein 12) 1034 110,580 Alternative sequence (4); Chain (1); Compositional bias (1); Disulfide bond (29); Domain (10); Erroneous initiation (1); Glycosylation (3); Modified residue (3); Sequence conflict (10); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 755 775 Helical. {ECO:0000255}. TOPO_DOM 19 754 Extracellular. {ECO:0000255}.; TOPO_DOM 776 1034 Cytoplasmic. {ECO:0000255}. FUNCTION: When overexpressed, reduces the number of both early and late non-adherent myeloid progenitor cells. {ECO:0000269|PubMed:17226770}. PTM: Phosphorylated on tyrosine residues by SRC. Tyrosine phosphorylation is detected upon platelet aggregation stimulated by collagen, TRAP and thrombin and platelet-platelet contacts but not after platelet activation. Tyrosine phosphorylation enhanced its association with SHC1 and SHC2 (By similarity). Phosphorylated in the intracellular domain on tyrosine residues. {ECO:0000250, ECO:0000269|PubMed:17226770}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=Detected on the cell surface in resting platelets. {ECO:0000250}. SUBUNIT: Interacts with SHC2 upon its aggregation-induced tyrosine phosphorylation. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in thymocytes, bone marrow stromal and osteogenic cells (at protein level). Strongly expressed in kidney and heart. Moderately expressed in lung, spleen, thymus, liver, brain, testis, skin and stomach. Expressed in hematopoietic stem progenitor cells. {ECO:0000269|PubMed:17226770}. +Q8C669 PELI1_MOUSE E3 ubiquitin-protein ligase pellino homolog 1 (Pellino-1) (EC 2.3.2.27) (RING-type E3 ubiquitin transferase pellino homolog 1) 418 46,259 Chain (1); Domain (1); Erroneous initiation (1); Region (1); Sequence conflict (1) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins (By similarity). Involved in the TLR and IL-1 signaling pathways via interaction with the complex containing IRAK kinases and TRAF6. Mediates 'Lys-63'-linked polyubiquitination of IRAK1 allowing subsequent NF-kappa-B activation (PubMed:16951688). Mediates 'Lys-48'-linked polyubiquitination of RIPK3 leading to its subsequent proteasome-dependent degradation; preferentially recognizes and mediates the degradation of the 'Thr-182' phosphorylated form of RIPK3 (PubMed:29883609). Negatively regulates necroptosis by reducing RIPK3 expression (PubMed:29883609). Mediates 'Lys-63'-linked ubiquitination of RIPK1 (By similarity). {ECO:0000250|UniProtKB:Q96FA3, ECO:0000269|PubMed:16951688, ECO:0000269|PubMed:29883609}. PTM: Phosphorylated by IRAK1 and IRAK4 enhancing its E3 ligase activity. {ECO:0000250}.; PTM: Sumoylated. {ECO:0000250}. SUBUNIT: Interacts with MAP3K7 (By similarity). Upon IL1B treatment, forms a complex with TRAF6, IRAK1, IRAK4 and MYD88; this complex recruits MAP3K7/TAK1, TAB1 and TAB2 to mediate NF-kappa-B activation. Direct binding of SMAD6 to PELI1 prevents the complex formation and hence negatively regulates IL1R-TLR signaling and eventually NF-kappa-B-mediated gene expression (PubMed:16951688). Interacts (via atypical FHA domain) with RIPK3 (PubMed:29883609). Binds preferentially to the 'Thr-182' phosphorylated form of RIPK3 (By similarity). Interacts with RIPK1 (PubMed:29883609). {ECO:0000250|UniProtKB:Q96FA3, ECO:0000269|PubMed:16951688, ECO:0000269|PubMed:29883609}. +Q7TN75 PEG10_MOUSE Retrotransposon-derived protein PEG10 (Embryonal carcinoma differentiation regulated protein) (Mammalian retrotransposon-derived protein 2) (Myelin expression factor 3) (MyEF-3) (Myelin expression factor 3-like protein 1) (MEF3-like protein 1) (Paternally expressed gene 10 protein) (Retrotransposon gag domain-containing protein 3) (Retrotransposon-derived gag-like polyprotein) (Ty3/Gypsy-like protein) 958 109,849 Alternative sequence (2); Chain (1); Compositional bias (4); Modified residue (4); Region (1); Sequence conflict (3); Zinc finger (1) FUNCTION: May have a role in cell growth promotion, apoptotic resistance and hepatoma formation. Inhibits the TGF-beta signaling by interacting with the TGF-beta receptor ALK1. When overexpressed, induces the formation of cellular extension, such as filipodia in association with ALK1 (By similarity). Involved at the immediate early stage of adipocyte differentiation. May bind to the 5'-GCCTGTCTTT-3' DNA sequence of the MB1 domain in the myelin basic protein (MBP) promoter. {ECO:0000250, ECO:0000269|PubMed:17707377}. PTM: Isoform 1 undergoes proteolytic cleavage. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Detected predominantly in the cytoplasm of breast and prostate carcinomas, in hepatocellular carcinoma (HCC) and B-cell chronic lymphocytic leukemia (B-CLL) cells. Colocalized with ALK1 (By similarity). {ECO:0000250}. SUBUNIT: Interacts with ALK1, SIAH1 and SIAH2. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain and testis. Expressed during the early process of adipocyte differentiation. Expressed weakly in mammary gland but strongly in breast carcinomas of a c-MCY-driven transgenic model. {ECO:0000269|PubMed:11574691, ECO:0000269|PubMed:16423995, ECO:0000269|PubMed:17707377}. +P22005 PENK_MOUSE Proenkephalin-A [Cleaved into: Synenkephalin; Met-enkephalin (Opioid growth factor) (OGF); PENK(114-133); PENK(143-184); Met-enkephalin-Arg-Ser-Leu; Leu-enkephalin; PENK(238-259); Met-enkephalin-Arg-Phe] 268 31,004 Disulfide bond (3); Modified residue (1); Peptide (11); Propeptide (2); Sequence conflict (2); Signal peptide (1) FUNCTION: Met- and Leu-enkephalins compete with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress. PENK(114-133) and PENK(238-259) increase glutamate release in the striatum. PENK(114-133) decreases GABA concentration in the striatum. PTM: The N-terminal domain contains 6 conserved cysteines thought to be involved in disulfide bonding and/or processing. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Spermatogenic and somatic cells. +E9PYK3 PARP4_MOUSE Protein mono-ADP-ribosyltransferase PARP4 (EC 2.4.2.-) (ADP-ribosyltransferase diphtheria toxin-like 4) (ARTD4) (Poly [ADP-ribose] polymerase 4) (PARP-4) (Vault poly(ADP-ribose) polymerase) (VPARP) (mVparp) 1969 216,133 Chain (1); Domain (6); Erroneous initiation (1); Modified residue (1); Motif (2); Region (1); Sequence conflict (5) FUNCTION: Mono-ADP-ribosyltransferase that mediates mono-ADP-ribosylation of target proteins. {ECO:0000250|UniProtKB:Q9UKK3}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8K3Y6}. Nucleus {ECO:0000250|UniProtKB:Q8K3Y6}. Note=Localizes in the cytoplasm at steady state, but shuttles between nucleus and cytoplasm in a XPO1-dependent manner. {ECO:0000250|UniProtKB:Q8K3Y6}. SUBUNIT: Component of the vault ribonucleoprotein particle, at least composed of MVP, PARP4 and one or more vault RNAs (vRNAs). Interacts with TEP1. {ECO:0000250|UniProtKB:Q9UKK3}. +P32115 PAX4_MOUSE Paired box protein Pax-4 349 38,008 Alternative sequence (2); Chain (1); DNA binding (1); Domain (1); Mutagenesis (1); Region (1); Sequence conflict (2) FUNCTION: Plays an important role in the differentiation and development of pancreatic islet beta cells. Transcriptional repressor that competes with PAX6 in binding to a common element in the glucagon, insulin and somatostatin promoters. SUBCELLULAR LOCATION: Nucleus. TISSUE SPECIFICITY: Expressed in early pancreas. Later restricted to beta cells. Undetectable in adult islets. +P58501 PAXB1_MOUSE PAX3- and PAX7-binding protein 1 (PAX3/7BP) (GC-rich sequence DNA-binding factor 1) 919 104,836 Alternative sequence (2); Chain (1); Cross-link (2); Erroneous initiation (1); Erroneous translation (4); Modified residue (8); Region (1); Sequence conflict (6) FUNCTION: Adapter protein linking the transcription factors PAX3 and PAX7 to the histone methylation machinery and involved in myogenesis. Associates with a histone methyltransferase complex that specifically mediates dimethylation and trimethylation of 'Lys-4' of histone H3. Mediates the recruitment of that complex to the transcription factors PAX3 and PAX7 on chromatin to regulate the expression of genes involved in muscle progenitor cells proliferation including ID3 and CDC20. {ECO:0000269|PubMed:22862948}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22862948}. SUBUNIT: Interacts with PAX3 and PAX7. Interacts with WDR5; associates with a histone methyltransferase (HMT) complex composed at least of RBBP5, ASH2L, SET1, SET2 and KMT2A/MLL1, KMT2D/MLL2, KMT2C/MLL3 and KMT2B/MLL4 through direct interaction with WDR5. {ECO:0000269|PubMed:22862948}. TISSUE SPECIFICITY: Ubiquitously expressed in all tissues tested including skeletal muscle. Expressed in primary myoblasts. {ECO:0000269|PubMed:22862948}. +Q6W8Q3 PC4L1_MOUSE Purkinje cell protein 4-like protein 1 (PCP4-like protein 1) 68 7,502 Chain (1); Domain (1); Erroneous initiation (2); Modified residue (1) TISSUE SPECIFICITY: Expressed in laminar and nuclear structures of the CNS. {ECO:0000269|PubMed:15053978}. +Q61990 PCBP2_MOUSE Poly(rC)-binding protein 2 (Alpha-CP2) (CTBP) (CBP) (Putative heterogeneous nuclear ribonucleoprotein X) (hnRNP X) 362 38,222 Alternative sequence (2); Chain (1); Cross-link (3); Domain (3); Modified residue (5) FUNCTION: Single-stranded nucleic acid binding protein that binds preferentially to oligo dC. Major cellular poly(rC)-binding protein. Binds also poly(rU). Negatively regulates cellular antiviral responses mediated by MAVS signaling. It acts as an adapter between MAVS and the E3 ubiquitin ligase ITCH, therefore triggering MAVS ubiquitinationa and degradation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. SUBUNIT: Identified in a mRNP complex, at least composed of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1. Interacts with IFIH1 and RNF135 (By similarity). Interacts with MAVS (via C-terminus) and ITCH (via WW domains) (By similarity). {ECO:0000250}. DOMAIN: The KH domains mediates poly(C) binding. {ECO:0000250}. +Q91XZ4 PCDB6_MOUSE Protocadherin beta-6 (PCDH-beta-6) 772 84,280 Beta strand (32); Chain (1); Disulfide bond (1); Domain (6); Glycosylation (5); Helix (6); Mutagenesis (10); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (7) TRANSMEM 691 711 Helical. {ECO:0000255}. TOPO_DOM 31 690 Extracellular. {ECO:0000305|PubMed:27161523}.; TOPO_DOM 712 772 Cytoplasmic. {ECO:0000305|PubMed:27161523}. FUNCTION: Calcium-dependent cell-adhesion protein involved in cells self-recognition and non-self discrimination (PubMed:27161523). Thereby, it is involved in the establishment and maintenance of specific neuronal connections in the brain (PubMed:27161523). {ECO:0000269|PubMed:27161523}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27161523}; Single-pass type I membrane protein {ECO:0000269|PubMed:27161523}. SUBUNIT: Forms homodimers in trans (molecules expressed by two different cells). Forms promiscuous heterodimers in cis (at the plasma membrane of the same cell) with other protocadherins. {ECO:0000269|PubMed:27161523}. DOMAIN: Cadherin 1 to cadherin 4 domains mediate homophilic trans-interaction, the interaction with an identical protocadherin expressed by a neighboring cell (PubMed:27161523). This is a head-to-tail interaction, the cadherin 1 domain interacting with the cadherin 4 domain and the cadherin 2 domain interacting the cadherin 3 domain of the other protocadherin (PubMed:27161523). The cadherin 6 domain mediates promiscuous interactions with protocadherins on the same cell membrane (PubMed:27161523). Each cadherin domain binds three calcium ions (PubMed:27161523). {ECO:0000269|PubMed:27161523, ECO:0000312|PDB:5DZX}. +E9PVD3 PCD16_MOUSE Protocadherin-16 (Protein Dchs1) (Protein dachsous homolog 1) 3291 346,384 Chain (1); Domain (27); Glycosylation (2); Modified residue (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 2934 2954 Helical. {ECO:0000255}. TOPO_DOM 36 2933 Extracellular. {ECO:0000255}.; TOPO_DOM 2955 3291 Cytoplasmic. {ECO:0000255}. FUNCTION: Calcium-dependent cell-adhesion protein. Mediates functions in neuroprogenitor cell proliferation and differentiation. In the heart, has a critical role for proper morphogenesis of the mitral valve, acting in the regulation of cell migration involved in valve formation (PubMed:26258302). {ECO:0000269|PubMed:24056717, ECO:0000269|PubMed:26258302}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=In the embryonic cortex, FAT4 and DCHS1 accumulated at the cell-cell boundaries located apical to the adherens junction. {ECO:0000269|PubMed:19506035}. SUBUNIT: Heterophilic interaction with FAT4; this interaction affects their respective protein levels. TISSUE SPECIFICITY: Expressed in the epicardium and atrioventricular sulcus (at protein level). {ECO:0000269|PubMed:26258302}. +Q91ZA3 PCCA_MOUSE Propionyl-CoA carboxylase alpha chain, mitochondrial (PCCase subunit alpha) (EC 6.4.1.3) (Propanoyl-CoA:carbon dioxide ligase subunit alpha) 724 79,922 Active site (1); Binding site (3); Chain (1); Domain (3); Modified residue (21); Sequence conflict (3); Transit peptide (1) Metabolic intermediate metabolism; propanoyl-CoA degradation; succinyl-CoA from propanoyl-CoA: step 1/3. PTM: Acetylated. {ECO:0000269|PubMed:23438705}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. SUBUNIT: Probably a dodecamer composed of six biotin-containing alpha subunits and six beta subunits (Probable). Interacts (via the biotin carboxylation domain) with SIRT4 (PubMed:23438705). Interacts with SIRT3 and SIRT5 (PubMed:23438705). {ECO:0000269|PubMed:23438705, ECO:0000305}. DISEASE: Note=Propionic acidemia due to recessively inherited deficiency of PCCase activity often causes life-threatening ketosis and acidosis. +Q91Y13 PCDA7_MOUSE Protocadherin alpha-7 (PCDH-alpha-7) 937 101,266 Chain (1); Compositional bias (1); Disulfide bond (1); Domain (6); Glycosylation (7); Mutagenesis (3); Region (1); Repeat (5); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 698 718 Helical. {ECO:0000255}. TOPO_DOM 30 697 Extracellular. {ECO:0000305|PubMed:27161523}.; TOPO_DOM 719 937 Cytoplasmic. {ECO:0000305|PubMed:27161523}. FUNCTION: Calcium-dependent cell-adhesion protein involved in cells self-recognition and non-self discrimination (PubMed:27161523). Thereby, it is involved in the establishment and maintenance of specific neuronal connections in the brain (PubMed:27161523). {ECO:0000269|PubMed:27161523}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27161523}; Single-pass type I membrane protein {ECO:0000269|PubMed:27161523}. SUBUNIT: Forms homodimers in trans (molecules expressed by two different cells) (PubMed:27161523). Forms promiscuous heterodimers in cis (at the plasma membrane of the same cell) with other protocadherins (PubMed:27161523). {ECO:0000269|PubMed:27161523}. DOMAIN: Cadherin 1 to cadherin 4 domains mediate homophilic trans-interaction, the interaction with an identical protocadherin expressed by a neighboring cell (PubMed:27161523). This is a head-to-tail interaction, the cadherin 1 domain interacting with the cadherin 4 domain and the cadherin 2 domain interacting the cadherin 3 domain of the other protocadherin (PubMed:27161523). The cadherin 6 domain mediates promiscuous interactions with protocadherins on the same cell membrane. Each cadherin domain binds three calcium ions (PubMed:27161523). {ECO:0000269|PubMed:27161523, ECO:0000312|PDB:5DZV}. +Q8BFV2 PCID2_MOUSE PCI domain-containing protein 2 (CSN12-like protein) 399 46,132 Chain (1); Domain (1); Initiator methionine (1); Modified residue (2); Sequence conflict (1) FUNCTION: Required for B-cell survival through the regulation of the expression of cell-cycle checkpoint MAD2L1 protein during B cell differentiation (PubMed:20870947). Component of the TREX-2 complex (transcription and export complex 2), composed of at least ENY2, GANP, PCID2, SEM1, and either centrin CETN2 or CETN3. The TREX-2 complex functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket). TREX-2 participates in mRNA export and accurate chromatin positioning in the nucleus by tethering genes to the nuclear periphery. Binds and stabilizes BRCA2 and is thus involved in the control of R-loop-associated DNA damage and transcription-associated genomic instability. R-loop accumulation does not increase in PCID2-depleted cells. {ECO:0000250|UniProtKB:Q5JVF3, ECO:0000269|PubMed:20870947}. SUBUNIT: Belongs to the TREX-2 complex (transcription and export complex 2), composed of at least ENY2, GANP, PCID2, SEM1, and either centrin CETN2 or CETN3. Interacts with BRCA2. {ECO:0000250|UniProtKB:Q5JVF3}. +Q9Z2V4 PCKGC_MOUSE Phosphoenolpyruvate carboxykinase, cytosolic [GTP] (PEPCK-C) (EC 4.1.1.32) 622 69,355 Active site (1); Binding site (4); Chain (1); Metal binding (3); Modified residue (9); Nucleotide binding (2); Region (2) Carbohydrate biosynthesis; gluconeogenesis. FUNCTION: Regulates cataplerosis and anaplerosis, the processes that control the levels of metabolic intermediates in the citric acid cycle. At low glucose levels, it catalyzes the cataplerotic conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle. At high glucose levels, it catalyzes the anaplerotic conversion of phosphoenolpyruvate to oxaloacetate. {ECO:0000269|PubMed:30193097}. PTM: Acetylated (PubMed:30193097). Lysine acetylation by p300/EP300 is increased on high glucose conditions and promotes ubiquitination by UBR5, acetylation is enhanced in the presence of BAG6. Deacetylated by SIRT2 (By similarity). Deacetylated by SIRT1 (PubMed:30193097). {ECO:0000250|UniProtKB:P35558, ECO:0000269|PubMed:30193097}.; PTM: Ubiquitination by UBR5 leads to proteasomal degradation. {ECO:0000250|UniProtKB:P35558}.; PTM: Phosphorylated in a GSK3B-mediated pathway; phosphorylation affects the efficiency of SIRT1-mediated deacetylation, and regulates PCK1 ubiquitination and degradation. {ECO:0000250|UniProtKB:P35558}. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P35558}. +P17918 PCNA_MOUSE Proliferating cell nuclear antigen (PCNA) (Cyclin) 261 28,785 Chain (1); Cross-link (3); DNA binding (1); Modified residue (5); Sequence conflict (2) FUNCTION: Auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand. Induces a robust stimulatory effect on the 3'-5' exonuclease and 3'-phosphodiesterase, but not apurinic-apyrimidinic (AP) endonuclease, APEX2 activities. Has to be loaded onto DNA in order to be able to stimulate APEX2. Plays a key role in DNA damage response (DDR) by being conveniently positioned at the replication fork to coordinate DNA replication with DNA repair and DNA damage tolerance pathways. Acts as a loading platform to recruit DDR proteins that allow completion of DNA replication after DNA damage and promote postreplication repair: Monoubiquitinated PCNA leads to recruitment of translesion (TLS) polymerases, while 'Lys-63'-linked polyubiquitination of PCNA is involved in error-free pathway and employs recombination mechanisms to synthesize across the lesion (By similarity). {ECO:0000250|UniProtKB:P12004}. PTM: Phosphorylated. Phosphorylation at Tyr-211 by EGFR stabilizes chromatin-associated PCNA (By similarity). {ECO:0000250|UniProtKB:P12004}.; PTM: Acetylated by CREBBP and p300/EP300; preferentially acetylated by CREBBP on Lys-80, Lys-13 and Lys-14 and on Lys-77 by p300/EP300 upon loading on chromatin in response to UV irradiation. Lysine acetylation disrupts association with chromatin, hence promoting PCNA ubiquitination and proteasomal degradation in response to UV damage in a CREBBP- and EP300-dependent manner. Acetylation disrupts interaction with NUDT15 and promotes degradation (By similarity). {ECO:0000250|UniProtKB:P12004}.; PTM: Ubiquitinated. Following DNA damage, can be either monoubiquitinated to stimulate direct bypass of DNA lesions by specialized DNA polymerases or polyubiquitinated to promote recombination-dependent DNA synthesis across DNA lesions by template switching mechanisms. Following induction of replication stress, monoubiquitinated by the UBE2B-RAD18 complex on Lys-164, leading to recruit translesion (TLS) polymerases, which are able to synthesize across DNA lesions in a potentially error-prone manner. An error-free pathway also exists and requires non-canonical polyubiquitination on Lys-164 through 'Lys-63' linkage of ubiquitin moieties by the E2 complex UBE2N-UBE2V2 and the E3 ligases, HLTF, RNF8 and SHPRH. This error-free pathway, also known as template switching, employs recombination mechanisms to synthesize across the lesion, using as a template the undamaged, newly synthesized strand of the sister chromatid. Monoubiquitination at Lys-164 also takes place in undamaged proliferating cells, and is mediated by the DCX(DTL) complex, leading to enhance PCNA-dependent translesion DNA synthesis. Sumoylated during S phase (By similarity). {ECO:0000250|UniProtKB:P12004}.; PTM: Methylated on glutamate residues by ARMT1. {ECO:0000250|UniProtKB:P12004}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24115439}. Note=Colocalizes with CREBBP, EP300 and POLD1 to sites of DNA damage (By similarity). Forms nuclear foci representing sites of ongoing DNA replication and vary in morphology and number during S phase. Together with APEX2, is redistributed in discrete nuclear foci in presence of oxidative DNA damaging agents. {ECO:0000250|UniProtKB:P12004}. SUBUNIT: Homotrimer. Interacts with p300/EP300; the interaction occurs on chromatin in UV-irradiated damaged cells. Interacts with CREBBP (via transactivation domain and C-terminus); the interaction occurs on chromatin in UV-irradiated damaged cells. Directly interacts with POLD1, POLD3 and POLD4 subunits of the DNA polymerase delta complex, POLD3 being the major interacting partner; the interaction with POLD3 is inhibited by CDKN1A/p21(CIP1). Forms a complex with activator 1 heteropentamer in the presence of ATP. Interacts with EXO1, POLH, POLK, DNMT1, ERCC5, FEN1, CDC6 and POLDIP2 (By similarity). Interacts with APEX2; this interaction is triggered by reactive oxygen species and increased by misincorporation of uracil in nuclear DNA (PubMed:12573260). Forms a ternary complex with DNTTIP2 and core histone (By similarity). Interacts with KCTD10 (By similarity). Interacts with PPP1R15A (PubMed:9371605). Directly interacts with BAZ1B. Interacts with HLTF and SHPRH. Interacts with NUDT15; this interaction is disrupted in response to UV irradiation and acetylation. Interacts with CDKN1A/p21(CIP1) and CDT1; interacts via their PIP-box which also recruits the DCX(DTL) complex. The interaction with CDKN1A inhibits POLD3 binding. Interacts with DDX11. Interacts with EGFR; positively regulates PCNA. Interacts with PARPBP. Interacts (when ubiquitinated) with SPRTN; leading to enhance RAD18-mediated PCNA ubiquitination. Interacts (when polyubiquitinated) with ZRANB3. Interacts with SMARCAD1. Interacts with CDKN1C. Interacts with PCLAF (via PIP-box) (By similarity). Interacts with RTEL1 (via PIP-box); the interaction is direct and essential for the suppression of telomere fragility (PubMed:24115439). Interacts with FAM111A (via PIP-box); the interaction is direct and required for PCNA loading on chromatin binding. Interacts with LIG1. Interacts with SETMAR. Interacts with ANKRD17. Interacts with FBXO18/FBH1 (via PIP-box); the interaction recruits the DCX(DTL) complex and promotes ubiquitination and degradation of FBXO18/FBH1. Interacts with POLN (By similarity). Interacts with SDE2 (via PIP-box); the interaction is direct and prevents ultraviolet light induced monoubiquitination (By similarity). Component of the replisome complex composed of at least DONSON, MCM2, MCM7, PCNA and TICRR; interaction at least with PCNA occurs during DNA replication (By similarity). Interacts with MAPK15; the interaction is chromatin binding dependent and prevents MDM2-mediated PCNA destruction by inhibiting the association of PCNA with MDM2. Interacts with PARP10 (via PIP-box) (By similarity). {ECO:0000250|UniProtKB:P04961, ECO:0000250|UniProtKB:P12004, ECO:0000269|PubMed:12573260, ECO:0000269|PubMed:24115439, ECO:0000269|PubMed:9371605}. +P48725 PCNT_MOUSE Pericentrin 2898 329,465 Alternative sequence (3); Chain (1); Coiled coil (11); Erroneous termination (1); Modified residue (10); Region (3); Sequence conflict (14) FUNCTION: Integral component of the filamentous matrix of the centrosome involved in the initial establishment of organized microtubule arrays in both mitosis and meiosis. Plays a role, together with DISC1, in the microtubule network formation. Is an integral component of the pericentriolar material (PCM). May play an important role in preventing premature centrosome splitting during interphase by inhibiting NEK2 kinase activity at the centrosome. {ECO:0000250|UniProtKB:O95613, ECO:0000269|PubMed:17626165}. PTM: Cleaved during mitotis which leads to removal of CDK5RAP2 from the centrosome and promotes centriole disengagement and subsequent centriole separation. The C-terminal fragment is rapidly degraded following cleavage. {ECO:0000250|UniProtKB:O95613}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:O95613}. Note=Centrosomal at all stages of the cell cycle. Remains associated with centrosomes following microtubule depolymerization. Colocalized with DISC1 at the centrosome. {ECO:0000250|UniProtKB:O95613}. SUBUNIT: Interacts with DISC1 and PCM1. Binds calmodulin. Interacts with CEP131 (By similarity). Interacts with CDK5RAP2; the interaction is leading to centrosomal localization of PCNT and CDK5RAP2 (PubMed:20471352). Interacts with CHD3 (PubMed:17626165). Interacts with CHD4; the interaction regulates centrosome integrity (PubMed:17626165). Interacts with NEK2 (By similarity). Interacts with CCDC13 (By similarity). Interacts with CEP68 (By similarity). Interacts with ATF5; the ATF5:PCNT:polyglutamylated tubulin (PGT) tripartite unites the mother centriole and the pericentriolar material (PCM) in the centrosome (By similarity). {ECO:0000250|UniProtKB:O95613, ECO:0000269|PubMed:17626165, ECO:0000269|PubMed:20471352}. DOMAIN: Composed of a coiled-coil central region flanked by non-helical N- and C-terminals. TISSUE SPECIFICITY: Expressed in heart and lung (at protein level). Expressed in kidney, thymus, liver, brain, muscle, testis, spleen, lung and heart. {ECO:0000269|PubMed:17084386}. +P12660 PCP2_MOUSE Purkinje cell protein 2 (Protein PCD-5) (Purkinje cell-specific protein L7) 120 13,054 Chain (1); Domain (2); Erroneous gene model prediction (1); Erroneous initiation (3); Frameshift (1); Modified residue (1) FUNCTION: May function as a cell-type specific modulator for G protein-mediated cell signaling. TISSUE SPECIFICITY: Cerebellum (Purkinje cells) and retinal bipolar neurons. +Q61398 PCOC1_MOUSE Procollagen C-endopeptidase enhancer 1 (P14) (Procollagen COOH-terminal proteinase enhancer 1) (PCPE-1) (Procollagen C-proteinase enhancer 1) (Type 1 procollagen C-proteinase enhancer protein) (Type I procollagen COOH-terminal proteinase enhancer) 468 50,168 Chain (1); Disulfide bond (6); Domain (3); Frameshift (1); Glycosylation (2); Modified residue (2); Sequence conflict (1); Signal peptide (1) FUNCTION: Binds to the C-terminal propeptide of type I procollagen and enhances procollagen C-proteinase activity. PTM: Processed from a 55 kDa form to 36 kDa and 34 kDa forms. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Expressed in interstitial connective tissues like tendons, calvaria, skin and at a lower level in heart and skeletal muscle. {ECO:0000269|PubMed:2256940}. +Q811Q9 PCY1B_MOUSE Choline-phosphate cytidylyltransferase B (EC 2.7.7.15) (CCT-beta) (CTP:phosphocholine cytidylyltransferase B) (CCT B) (CT B) (Phosphorylcholine transferase B) 369 41,900 Alternative sequence (2); Binding site (4); Chain (1); Erroneous initiation (1); Modified residue (14); Nucleotide binding (3); Sequence conflict (3) Phospholipid metabolism; phosphatidylcholine biosynthesis; phosphatidylcholine from phosphocholine: step 1/2. FUNCTION: Controls phosphatidylcholine synthesis. {ECO:0000269|PubMed:12842190, ECO:0000269|PubMed:15143167}. SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P19836}. TISSUE SPECIFICITY: Highly expressed in brain (at protein level). Expressed at lower levels in lung and gonads. {ECO:0000269|PubMed:12842190, ECO:0000269|PubMed:15143167}. +Q922E4 PCY2_MOUSE Ethanolamine-phosphate cytidylyltransferase (EC 2.7.7.14) (CTP:phosphoethanolamine cytidylyltransferase) (Phosphorylethanolamine transferase) 404 45,235 Binding site (1); Chain (1); Modified residue (3); Nucleotide binding (4); Sequence conflict (1) Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from ethanolamine: step 2/3. FUNCTION: Plays an important role in the biosynthesis of the phospholipid phosphatidylethanolamine. Catalyzes the formation of CDP-ethanolamine (By similarity). {ECO:0000250}. +Q9EP73 PD1L1_MOUSE Programmed cell death 1 ligand 1 (PD-L1) (PDCD1 ligand 1) (Programmed death ligand 1) (B7 homolog 1) (B7-H1) (CD antigen CD274) 290 32,780 Chain (1); Disulfide bond (2); Domain (2); Glycosylation (5); Mutagenesis (21); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 240 260 Helical. {ECO:0000255}. TOPO_DOM 19 239 Extracellular. {ECO:0000255}.; TOPO_DOM 261 290 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a critical role in induction and maintenance of immune tolerance to self. As a ligand for the inhibitory receptor PDCD1, modulates the activation threshold of T-cells and limits T-cell effector response (PubMed:11238124). The PDCD1-mediated inhibitory pathway is exploited by tumors to attenuate anti-tumor immunity and facilitate tumor survival (By similarity). May costimulate helper T-cell subsets through a yet unknown activating receptor (PubMed:11015443, PubMed:12719480). {ECO:0000250|UniProtKB:Q9NZQ7, ECO:0000269|PubMed:11015443, ECO:0000269|PubMed:11238124, ECO:0000269|PubMed:12719480}. PTM: Ubiquitinated; STUB1 likely mediates polyubiquitination of PD-L1/CD274 triggering its degradation. {ECO:0000250|UniProtKB:Q9NZQ7}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9NZQ7}; Single-pass type I membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:Q9NZQ7}; Single-pass type I membrane protein {ECO:0000255}. Recycling endosome membrane {ECO:0000250|UniProtKB:Q9NZQ7}; Single-pass type I membrane protein {ECO:0000255}. SUBUNIT: Interacts with PDCD1 (PubMed:11015443). Interacts with CMTM4 and CMTM6 (By similarity). {ECO:0000250|UniProtKB:Q9NZQ7, ECO:0000269|PubMed:11015443}. TISSUE SPECIFICITY: Highly expressed in the heart, thymus, skeletal muscle, and lung. Weakly expressed in the kidney, spleen, thyroid, and liver. Expressed on activated dendritic cells, B-cells and macrophages. Expressed in numerous tumor cells lines of lymphoid origin. {ECO:0000269|PubMed:11015443, ECO:0000269|PubMed:11224527, ECO:0000269|PubMed:11238124}. +Q9WUL5 PD1L2_MOUSE Programmed cell death 1 ligand 2 (PD-1 ligand 2) (PD-L2) (PDCD1 ligand 2) (Programmed death ligand 2) (Butyrophilin B7-DC) (B7-DC) (CD antigen CD273) 247 27,820 Beta strand (15); Chain (1); Disulfide bond (2); Domain (2); Glycosylation (4); Helix (3); Mutagenesis (17); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (3) TRANSMEM 222 242 Helical. {ECO:0000255}. TOPO_DOM 20 221 Extracellular. {ECO:0000255}.; TOPO_DOM 243 247 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in the costimulatory signal essential for T-cell proliferation and IFNG production in a PDCD1-independent manner. Interaction with PDCD1 inhibits T-cell proliferation by blocking cell cycle progression and cytokine production. {ECO:0000269|PubMed:11224527, ECO:0000269|PubMed:11283156, ECO:0000269|PubMed:12719480}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9BQ51}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9BQ51, ECO:0000305|PubMed:18641123}. SUBUNIT: Interacts with PDCD1. {ECO:0000269|PubMed:11283156, ECO:0000269|PubMed:18641123}. TISSUE SPECIFICITY: Expressed in immature and mature bone marrow-derived dendritic cells and splenic dendritic cells. Highly expressed in placenta, liver and weakly expressed in heart, spleen, lymph nodes and thymus. Also expressed in some tumor cell lines of lymphoid origin. {ECO:0000269|PubMed:11224527, ECO:0000269|PubMed:11283156}. +Q8CA95 PDE10_MOUSE cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A (EC 3.1.4.17) (EC 3.1.4.35) 790 89,408 Active site (1); Alternative sequence (4); Binding site (4); Chain (1); Domain (1); Metal binding (5); Mutagenesis (1); Region (2); Sequence conflict (1) Purine metabolism; 3',5'-cyclic AMP degradation; AMP from 3',5'-cyclic AMP: step 1/1. Purine metabolism; 3',5'-cyclic GMP degradation; GMP from 3',5'-cyclic GMP: step 1/1. FUNCTION: Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. Can hydrolyze both cAMP and cGMP, but has higher affinity for cAMP and is more efficient with cAMP as substrate. May play a critical role in regulating cAMP and cGMP levels in the striatum, a region of the brain that contributes to the control of movement and cognition. {ECO:0000269|PubMed:10359840, ECO:0000269|PubMed:27058446}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. DOMAIN: The tandem GAF domains bind cAMP, and regulate enzyme activity. The binding of cAMP stimulates enzyme activity (By similarity). {ECO:0000250}.; DOMAIN: Composed of a C-terminal catalytic domain containing two divalent metal sites and an N-terminal regulatory domain which contains one cyclic nucleotide-binding region. {ECO:0000250}. TISSUE SPECIFICITY: Detected in striatum (at protein level). Detected in testis and brain. {ECO:0000269|PubMed:10359840, ECO:0000269|PubMed:14751289}. +Q61823 PDCD4_MOUSE Programmed cell death protein 4 (Protein MA-3) (Topoisomerase-inhibitor suppressed protein) 469 51,702 Beta strand (2); Chain (1); Domain (2); Helix (18); Modified residue (12); Motif (3); Mutagenesis (3); Sequence conflict (5); Turn (2) FUNCTION: Inhibits translation initiation and cap-dependent translation. May excert its function by hindering the interaction between EIF4A1 and EIF4G. Inhibits the helicase activity of EIF4A. Modulates the activation of JUN kinase. Down-regulates the expression of MAP4K1, thus inhibiting events important in driving invasion, namely, MAPK85 activation and consequent JUN-dependent transcription. May play a role in apoptosis. Tumor suppressor. Inhibits tumor promoter-induced neoplastic transformation. Binds RNA. {ECO:0000269|PubMed:12482958, ECO:0000269|PubMed:12894233, ECO:0000269|PubMed:16024603, ECO:0000269|PubMed:17060447}. PTM: Polyubiquitinated, leading to its proteasomal degradation. Rapidly degraded in response to mitogens. Phosphorylation of the phosphodegron promotes interaction with BTRC and proteasomal degradation (By similarity). {ECO:0000250}.; PTM: Phosphorylated at Ser-67 by RPS6KB1 in response to mitogens; phosphorylation promotes proteasomal degradation of PDCD4. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12894233}. Cytoplasm {ECO:0000269|PubMed:12894233}. Note=Shuttles between the nucleus and cytoplasm (PubMed:12894233). Predominantly nuclear under normal growth conditions, and when phosphorylated at Ser-457 (By similarity). {ECO:0000250|UniProtKB:Q53EL6, ECO:0000269|PubMed:12894233}. SUBUNIT: Interacts (via MI domains) with EIF4A1 and EIF4A2 (via N-terminal domain). Heterotrimer with EIF4A1; one molecule of PDCD4 binds two molecules of EIF4A1. Interacts with EIF4G1. May form a complex with EIF4A1 and EIF4G1. The interaction between PDCD4 and EIF4A1 interferes with the interaction between EIF4A1 and EIF4G. When phosphorylated, interacts with BTRC and FBXW11 (By similarity). {ECO:0000250}. DOMAIN: Binds EIF4A1 via both MI domains. {ECO:0000269|PubMed:19153607}. TISSUE SPECIFICITY: Expressed ubiquitously. Highyly expressed in thymus and liver. Moderately expressed in brain, kidney and spleen; weakly in lung and heart. Expression is up- or down-regulated in response to apoptosis inducers. Regulated by many programmed cell death-inducing stimuli. {ECO:0000269|PubMed:8543179, ECO:0000269|PubMed:9714845}. DISEASE: Note=Decreases benign tumor development and malignant progression. {ECO:0000305|PubMed:16024603}. +P56812 PDCD5_MOUSE Programmed cell death protein 5 (TF-1 cell apoptosis-related protein 19) (Protein TFAR19) 126 14,275 Chain (1); Initiator methionine (1); Modified residue (4) FUNCTION: May function in the process of apoptosis. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9920759}. +P12815 PDCD6_MOUSE Programmed cell death protein 6 (ALG-257) (Apoptosis-linked gene 2 protein) (ALG-2) (PMP41) 191 21,867 Alternative sequence (1); Beta strand (5); Calcium binding (3); Chain (1); Domain (5); Erroneous initiation (1); Helix (8); Initiator methionine (1); Metal binding (14); Modified residue (1); Mutagenesis (1) FUNCTION: Calcium sensor that plays a key role in processes such as endoplasmic reticulum (ER)-Golgi vesicular transport, endosomal biogenesis or membrane repair (PubMed:10744743, PubMed:11525164, PubMed:27541325). Acts as an adapter that bridges unrelated proteins or stabilizes weak protein-protein complexes in response to calcium: calcium-binding triggers exposure of apolar surface, promoting interaction with different sets of proteins thanks to 3 different hydrophobic pockets, leading to translocation to membranes (PubMed:10744743, PubMed:11525164, PubMed:27541325). Involved in ER-Golgi transport by promoting the association between PDCD6IP and TSG101, thereby bridging together the ESCRT-III and ESCRT-I complexes (PubMed:10744743, PubMed:11525164, PubMed:27541325). Together with PEF1, acts as calcium-dependent adapter for the BCR(KLHL12) complex, a complex involved in ER-Golgi transport by regulating the size of COPII coats (By similarity). In response to cytosolic calcium increase, the heterodimer formed with PEF1 interacts with, and bridges together the BCR(KLHL12) complex and SEC31 (SEC31A or SEC31B), promoting monoubiquitination of SEC31 and subsequent collagen export, which is required for neural crest specification (By similarity). Involved in the regulation of the distribution and function of MCOLN1 in the endosomal pathway (By similarity). Promotes localization and polymerization of TFG at endoplasmic reticulum exit site (By similarity). Required for T-cell receptor-, Fas-, and glucocorticoid-induced apoptosis (PubMed:8560270). May mediate Ca(2+)-regulated signals along the death pathway: interaction with DAPK1 can accelerate apoptotic cell death by increasing caspase-3 activity (By similarity). Its role in apoptosis may however be indirect, as suggested by knockout experiments (PubMed:12024023). May inhibit KDR/VEGFR2-dependent angiogenesis; the function involves inhibition of VEGF-induced phosphorylation of the Akt signaling pathway (By similarity). {ECO:0000250|UniProtKB:O75340, ECO:0000269|PubMed:10744743, ECO:0000269|PubMed:11525164, ECO:0000269|PubMed:12024023, ECO:0000269|PubMed:27541325, ECO:0000305|PubMed:12024023}.; FUNCTION: Isoform 2: Has a lower Ca(2+) affinity than isoform 1 (PubMed:10744743). {ECO:0000269|PubMed:10744743}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O75340}; Peripheral membrane protein {ECO:0000250|UniProtKB:O75340}. Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250|UniProtKB:O75340}. Cytoplasm {ECO:0000250|UniProtKB:O75340}. Nucleus {ECO:0000250|UniProtKB:O75340}. Endosome {ECO:0000250|UniProtKB:O75340}. Note=Interaction with RBM22 induces relocalization from the cytoplasm to the nucleus. Translocated from the cytoplasm to the nucleus after heat shock cell treatment. Accumulates in cytoplasmic vesicle-like organelles after heat shock treatment, which may represent stress granules. In response to calcium increase, relocates from cytoplasm to COPII vesicle coat. Localizes to endoplasmic reticulum exit site (ERES). {ECO:0000250|UniProtKB:O75340}. SUBUNIT: Homodimer and heterodimer; heterodimerizes (via the EF-hand 5) with PEF1 (PubMed:10200558, PubMed:11525164, PubMed:27541325). Isoform 1 and isoform 2 self-associate; probably forming homodimers (By similarity). Interacts with CPNE4 (via VWFA domain) (PubMed:12522145). Interacts with PDCD6IP; the interaction is calcium-dependent (PubMed:10200558, PubMed:10744743, PubMed:11525164). Interacts with RBM22 (By similarity). Interacts with PLSCR4 (By similarity). Interacts with ANXA7 and TSG101 (By similarity). Interacts with DAPK1 (By similarity). Interacts with SEC31A; the interaction is calcium-dependent and promotes monoubiquitination of SEC31A (By similarity). Interacts with ANXA11 (via N-terminus); the interaction is calcium-dependent (By similarity). Interacts with PLSCR3 (via N-terminus); the interaction is calcium-dependent (By similarity). Interacts with MCOLN1; the interaction is calcium-dependent (By similarity). Interacts with KDR; the interaction is calcium-dependent (By similarity). Interacts with HEBP2; the interaction is calcium-dependent (By similarity). Interacts with TFG (By similarity). Isoform 1: Interacts with SHISA5, leading to stabilize it (PubMed:17889823). Isoform 2: Does not interact with SHISA5 (PubMed:17889823). Isoform 2: Does not interact with PDCD6IP, TSG101, ANXA7 and ANXA11 (PubMed:10744743). {ECO:0000250|UniProtKB:O75340, ECO:0000269|PubMed:10200558, ECO:0000269|PubMed:10744743, ECO:0000269|PubMed:11525164, ECO:0000269|PubMed:12522145, ECO:0000269|PubMed:17889823, ECO:0000269|PubMed:27541325}. DOMAIN: Interacts with different set of proteins thanks to 3 different hydrophobic pockets. Hydrophobic pockets 1 and 2, which mediate interaction with PDCD6IP, are largely formed by residues from EF-hand 3 (EF3) to 5 (EF5), as well as by Tyr-180 (EF5) of a dimerizing molecule (Pocket 1) and from EF-hand (EF2) to 4 (EF4) (Pocket 2). Hydrophobic pocket 3, which mediates interaction with SEC31A, is mainly formed by residues from EF-hand 1 (EF1) to 3 (EF3). {ECO:0000250|UniProtKB:O75340}.; DOMAIN: EF-hand 1 (EF1) and 3 (EF3) are the high-affinity calcium-binding sites, while EF-hand 5 (EF5) binds calcium with low-affinity (PubMed:11525164). A one-residue insertion in the EF5-binding loop prevents the glutamyl residue at the C-terminal end of the loop from serving as the canonical bidentate calcium ligand (PubMed:11525164). EF5 acts as a high-affinity magnesium-binding domain instead (PubMed:27541325). Magnesium, may affect dimerization (PubMed:27541325). EF5 may bind either calcium or magnesium depending on the context. {ECO:0000269|PubMed:11525164, ECO:0000269|PubMed:27541325, ECO:0000305}. +Q3UEI1 PDE4C_MOUSE cAMP-specific 3',5'-cyclic phosphodiesterase 4C (EC 3.1.4.53) 686 76,090 Active site (1); Alternative sequence (1); Binding site (3); Chain (1); Compositional bias (1); Domain (1); Metal binding (5); Modified residue (5); Nucleotide binding (1); Site (1) Purine metabolism; 3',5'-cyclic AMP degradation; AMP from 3',5'-cyclic AMP: step 1/1. FUNCTION: Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. {ECO:0000250}. SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000269|PubMed:21670265}. SUBUNIT: Part of a complex containing AKAP5, ADCY5, ADCY6 and PKD2. +Q61409 PDE3B_MOUSE cGMP-inhibited 3',5'-cyclic phosphodiesterase B (EC 3.1.4.17) (CGIPDE1) (Cyclic GMP-inhibited phosphodiesterase B) (CGI-PDE B) 1100 122,154 Active site (1); Chain (1); Coiled coil (1); Domain (1); Metal binding (5); Modified residue (4); Region (2); Sequence conflict (10); Transmembrane (6) TRANSMEM 69 89 Helical. {ECO:0000255}.; TRANSMEM 110 130 Helical. {ECO:0000255}.; TRANSMEM 140 160 Helical. {ECO:0000255}.; TRANSMEM 170 190 Helical. {ECO:0000255}.; TRANSMEM 198 218 Helical. {ECO:0000255}.; TRANSMEM 225 245 Helical. {ECO:0000255}. FUNCTION: Cyclic nucleotide phosphodiesterase with a dual-specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. May play a role in fat metabolism. Regulates cAMP binding of RAPGEF3. Through simultaneous binding to RAPGEF3 and PIK3R6 assembles a signaling complex in which the PI3K gamma complex is activated by RAPGEF3 and which is involved in angiogenesis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Interacts with PIK3CG. Interacts with RAPGEF3 and PIK3R6 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Abundant in adipose tissues. +Q8CG03 PDE5A_MOUSE cGMP-specific 3',5'-cyclic phosphodiesterase (EC 3.1.4.35) (cGMP-binding cGMP-specific phosphodiesterase) (CGB-PDE) 865 98,407 Active site (1); Beta strand (8); Binding site (1); Chain (1); Domain (3); Helix (4); Metal binding (5); Modified residue (1); Sequence conflict (1); Turn (5) Purine metabolism; 3',5'-cyclic GMP degradation; GMP from 3',5'-cyclic GMP: step 1/1. FUNCTION: Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. This phosphodiesterase catalyzes the specific hydrolysis of cGMP to 5'-GMP. Specifically regulates nitric-oxide-generated cGMP. {ECO:0000250|UniProtKB:O76074}. PTM: Phosphorylation is regulated by binding of cGMP to the two allosteric sites. Phosphorylation by PRKG1 leads to its activation. {ECO:0000250}. DOMAIN: Composed of a C-terminal catalytic domain containing two putative divalent metal sites and an N-terminal regulatory domain which contains two homologous allosteric cGMP-binding regions, A and B. +O89084 PDE4A_MOUSE cAMP-specific 3',5'-cyclic phosphodiesterase 4A (EC 3.1.4.53) 844 93,558 Active site (1); Alternative sequence (3); Binding site (3); Chain (1); Cross-link (1); Domain (1); Erroneous initiation (1); Metal binding (5); Modified residue (8); Nucleotide binding (1); Sequence conflict (2); Site (2) Purine metabolism; 3',5'-cyclic AMP degradation; AMP from 3',5'-cyclic AMP: step 1/1. FUNCTION: Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. {ECO:0000250}. PTM: Proteolytically cleaved by caspase-3. {ECO:0000250}.; PTM: Phosphorylation by MAPKAPK2 its activation through PKA phosphorylation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}. SUBUNIT: Interacts with LYN and ARRB2. {ECO:0000250}. +E9Q4S1 PDE8B_MOUSE High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8B (PDE8B) (EC 3.1.4.53) (Cell proliferation-inducing gene 22 protein) 865 96,739 Active site (1); Chain (1); Domain (2); Metal binding (5); Modified residue (3) Purine metabolism; 3',5'-cyclic AMP degradation; AMP from 3',5'-cyclic AMP: step 1/1. FUNCTION: Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. May be involved in specific signaling in the thyroid gland (By similarity). {ECO:0000250}. DOMAIN: Composed of a C-terminal catalytic domain containing two putative divalent metal sites and an N-terminal regulatory domain. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:18431404}. +O70628 PDE9A_MOUSE High affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A (EC 3.1.4.35) 534 61,636 Active site (1); Binding site (5); Chain (1); Domain (1); Metal binding (5); Modified residue (1); Nucleotide binding (2) Purine metabolism; 3',5'-cyclic GMP degradation; GMP from 3',5'-cyclic GMP: step 1/1. FUNCTION: Specifically hydrolyzes the second messenger cGMP, which is a key regulator of many important physiological processes (PubMed:9624145). Highly specific: compared to other members of the cyclic nucleotide phosphodiesterase family, has the highest affinity and selectivity for cGMP. Specifically regulates natriuretic-peptide-dependent cGMP signaling in heart, acting as a regulator of cardiac hypertrophy in myocytes and muscle. Does not regulate nitric oxide-dependent cGMP in heart (PubMed:25799991). Additional experiments are required to confirm whether its ability to hydrolyze natriuretic-peptide-dependent cGMP is specific to heart or is a general feature of the protein (Probable). In brain, involved in cognitive function, such as learning and long-term memory (PubMed:22328573, PubMed:24746365). {ECO:0000269|PubMed:22328573, ECO:0000269|PubMed:24746365, ECO:0000269|PubMed:25799991, ECO:0000269|PubMed:9624145, ECO:0000305}. SUBCELLULAR LOCATION: Cell projection, ruffle membrane {ECO:0000250|UniProtKB:O76083}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O76083}. Golgi apparatus {ECO:0000250|UniProtKB:O76083}. Endoplasmic reticulum {ECO:0000250|UniProtKB:O76083}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:O76083}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O76083}. TISSUE SPECIFICITY: Highly expressed in kidney. Lower levels in liver, lung and brain (PubMed:9624145). Widely expressed in brain, with highest expression in cerebellar Purkinje cells (PubMed:14501210). Present in heart (at protein level) (PubMed:25799991). {ECO:0000269|PubMed:14501210, ECO:0000269|PubMed:25799991, ECO:0000269|PubMed:9624145}. +Q8CI19 PDGFC_MOUSE Platelet-derived growth factor C (PDGF-C) (Fallotein) (Spinal cord-derived growth factor) (SCDGF) (VEGF-E) [Cleaved into: Platelet-derived growth factor C, latent form (PDGFC latent form); Platelet-derived growth factor C, receptor-binding form (PDGFC receptor-binding form)] 345 38,741 Chain (2); Disulfide bond (6); Domain (1); Glycosylation (2); Sequence conflict (5); Signal peptide (1); Site (3) FUNCTION: Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen and chemoattractant for cells of mesenchymal origin. Required for normal skeleton formation during embryonic development, especially for normal development of the craniofacial skeleton and for normal development of the palate. Required for normal skin morphogenesis during embryonic development. Plays an important role in wound healing, where it appears to be involved in three stages: inflammation, proliferation and remodeling. Plays an important role in angiogenesis and blood vessel development. Involved in fibrotic processes, in which transformation of interstitial fibroblasts into myofibroblasts plus collagen deposition occurs. The CUB domain has mitogenic activity in coronary artery smooth muscle cells, suggesting a role beyond the maintenance of the latency of the PDGF domain. In the nucleus, PDGFC seems to have additional function. {ECO:0000269|PubMed:10806482, ECO:0000269|PubMed:11297552, ECO:0000269|PubMed:12875986, ECO:0000269|PubMed:12972405, ECO:0000269|PubMed:15361870, ECO:0000269|PubMed:15372073, ECO:0000269|PubMed:15757957, ECO:0000269|PubMed:18184860}. PTM: Proteolytic removal of the N-terminal CUB domain releasing the core domain is necessary for unmasking the receptor-binding epitopes of the core domain. Cleavage after basic residues in the hinge region (region connecting the CUB and growth factor domains) gives rise to the receptor-binding form. Cleaved by PLAT and PLG (By similarity). {ECO:0000250}.; PTM: Sumoylated by SUMO1. {ECO:0000269|PubMed:16443219}.; PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:16443219}. Secreted {ECO:0000269|PubMed:15372073}. Nucleus {ECO:0000250|UniProtKB:Q9NRA1}. Cytoplasmic granule {ECO:0000250|UniProtKB:Q9NRA1}. Cell membrane {ECO:0000269|PubMed:16443219}. Note=Sumoylated form is predominant in the nucleus (PubMed:16443219). Stored in alpha granules in platelets (By similarity). {ECO:0000250|UniProtKB:Q9NRA1, ECO:0000269|PubMed:16443219}. SUBUNIT: Homodimer; disulfide-linked. Interacts with PDGFRA homodimers, and with heterodimers formed by PDGFRA and PDGFRB. Interacts (via CUB domain) with PLAT (via kringle domain) (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Mainly expressed in kidney, testis, liver, heart and brain (at protein level). Highly expressed in airway epithelium, interstitial cells and alveolar macrophages in the lung of mice overexpressing IL13. Expressed in the ovaries. {ECO:0000269|PubMed:11297552, ECO:0000269|PubMed:11744381, ECO:0000269|PubMed:16344272, ECO:0000269|PubMed:16951379, ECO:0000269|PubMed:18184860}. DISEASE: Note=Involved in the development of myocarditis and subsequent fibrosis in the experimental model of coxsackievirus B3-induced chronic myocarditis. {ECO:0000269|PubMed:15757957}. +P09103 PDIA1_MOUSE Protein disulfide-isomerase (PDI) (EC 5.3.4.1) (Cellular thyroid hormone-binding protein) (Endoplasmic reticulum resident protein 59) (ER protein 59) (ERp59) (Prolyl 4-hydroxylase subunit beta) (p55) 509 57,058 Active site (4); Chain (1); Disulfide bond (2); Domain (2); Modified residue (4); Motif (1); Sequence conflict (1); Signal peptide (1); Site (6) FUNCTION: This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP (By similarity). Receptor for LGALS9; the interaction retains P4HB at the cell surface of Th2 T helper cells, increasing disulfide reductase activity at the plasma membrane, altering the plasma membrane redox state and enhancing cell migration (PubMed:21670307). {ECO:0000250|UniProtKB:P07237, ECO:0000269|PubMed:21670307}. SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:P07237}. Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:P07237}. Melanosome {ECO:0000250|UniProtKB:P07237}. Cell membrane {ECO:0000269|PubMed:21670307}; Peripheral membrane protein {ECO:0000305}. Note=Highly abundant. In some cell types, seems to be also secreted or associated with the plasma membrane, where it undergoes constant shedding and replacement from intracellular sources. Localizes near CD4-enriched regions on lymphoid cell surfaces. Colocalizes with MTTP in the endoplasmic reticulum. {ECO:0000250|UniProtKB:P07237}. SUBUNIT: Heterodimer; heterodimerizes with the protein microsomal triglyceride transfer MTTP. Homodimer. Monomers and homotetramers may also occur. Also constitutes the structural subunit of prolyl 4-hydroxylase and of the microsomal triacylglycerol transfer protein MTTP in mammalian cells. Stabilizes both enzymes and retain them in the ER without contributing to the catalytic activity. Binds UBQLN1. Interacts with ERO1B (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P07237}. +Q9JK42 PDK2_MOUSE [Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 2, mitochondrial (EC 2.7.11.2) (Pyruvate dehydrogenase kinase isoform 2) (PDH kinase 2) 407 46,041 Binding site (1); Chain (1); Domain (1); Modified residue (3); Nucleotide binding (3); Sequence conflict (1); Transit peptide (1) FUNCTION: Kinase that plays a key role in the regulation of glucose and fatty acid metabolism and homeostasis via phosphorylation of the pyruvate dehydrogenase subunits PDHA1 and PDHA2. This inhibits pyruvate dehydrogenase activity, and thereby regulates metabolite flux through the tricarboxylic acid cycle, down-regulates aerobic respiration and inhibits the formation of acetyl-coenzyme A from pyruvate. Inhibition of pyruvate dehydrogenase decreases glucose utilization and increases fat metabolism. Mediates cellular responses to insulin. Plays an important role in maintaining normal blood glucose levels and in metabolic adaptation to nutrient availability. Via its regulation of pyruvate dehydrogenase activity, plays an important role in maintaining normal blood pH and in preventing the accumulation of ketone bodies under starvation. Plays a role in the regulation of cell proliferation and in resistance to apoptosis under oxidative stress. Plays a role in p53/TP53-mediated apoptosis. {ECO:0000269|PubMed:22360721}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:21190881}. SUBUNIT: Homodimer, and heterodimer with PDK1. Interacts with the pyruvate dehydrogenase complex subunit DLAT, and is part of the multimeric pyruvate dehydrogenase complex that contains multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3). {ECO:0000269|PubMed:21190881}. TISSUE SPECIFICITY: Detected in heart (at protein level). {ECO:0000269|PubMed:21190881}. +Q922H2 PDK3_MOUSE [Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 3, mitochondrial (EC 2.7.11.2) (Pyruvate dehydrogenase kinase isoform 3) 415 47,923 Binding site (1); Chain (1); Domain (1); Modified residue (1); Nucleotide binding (3); Sequence conflict (1); Transit peptide (1) FUNCTION: Inhibits pyruvate dehydrogenase activity by phosphorylation of the E1 subunit PDHA1, and thereby regulates glucose metabolism and aerobic respiration. Can also phosphorylate PDHA2. Decreases glucose utilization and increases fat metabolism in response to prolonged fasting, and as adaptation to a high-fat diet. Plays a role in glucose homeostasis and in maintaining normal blood glucose levels in function of nutrient levels and under starvation. Plays a role in the generation of reactive oxygen species (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. SUBUNIT: Homodimer. Interacts with the pyruvate dehydrogenase complex subunit DLAT, and is part of the multimeric pyruvate dehydrogenase complex that contains multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3) (By similarity). {ECO:0000250}. +O70400 PDLI1_MOUSE PDZ and LIM domain protein 1 (C-terminal LIM domain protein 1) (Elfin) (LIM domain protein CLP-36) 327 35,774 Chain (1); Domain (2); Initiator methionine (1); Metal binding (8); Modified residue (6); Sequence conflict (1) FUNCTION: Cytoskeletal protein that may act as an adapter that brings other proteins (like kinases) to the cytoskeleton (By similarity). Involved in assembly, disassembly and directioning of stress fibers in fibroblasts. Required for the localization of ACTN1 and PALLD to stress fibers. Required for cell migration and in maintaining cell polarity of fibroblasts (By similarity). {ECO:0000250|UniProtKB:O00151, ECO:0000250|UniProtKB:P52944}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11596114}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:O00151}. Note=Associates with the actin stress fibers (PubMed:11596114). SUBUNIT: Interacts with ACTN1, ACTN2 and ACTN4 (By similarity). Interacts with PDLIM4 (By similarity). {ECO:0000250|UniProtKB:O00151, ECO:0000250|UniProtKB:P52944}. TISSUE SPECIFICITY: Expressed in heart, lung, spleen, testis and skeletal muscle. {ECO:0000269|PubMed:11596114}. +Q62011 PDPN_MOUSE Podoplanin (Glycoprotein 38) (Gp38) (OTS-8) (PA2.26 antigen) (Transmembrane glycoprotein E11) (E11) 172 18,233 Chain (1); Glycosylation (19); Helix (1); Mutagenesis (5); Region (2); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 142 162 Helical. {ECO:0000255}. TOPO_DOM 23 141 Extracellular. {ECO:0000255}.; TOPO_DOM 163 172 Cytoplasmic. FUNCTION: Mediates effects on cell migration and adhesion through its different partners. During development plays a role in blood and lymphatic vessels separation by binding CLEC1B, triggering CLEC1B activation in platelets and leading to platelet activation and/or aggregation (PubMed:14522983, PubMed:15231832, PubMed:20110424, PubMed:17616532). Interaction with CD9, on the contrary, attenuates platelet aggregation and pulmonary metastasis induced by PDPN. Mediates effects on cell migration and adhesion through its different partners. Through MSN or EZR interaction promotes epithelial-mesenchymal transition (EMT) leading to ERZ phosphorylation and triggering RHOA activation leading to cell migration increase and invasiveness. Interaction with CD44 promotes directional cell migration in epithelial and tumor cells (By similarity). In lymph nodes (LNs), controls fibroblastic reticular cells (FRCs) adhesion to the extracellular matrix (ECM) and contraction of the actomyosin by maintaining ERM proteins (EZR; MSN and RDX) and MYL9 activation through association with unknown transmembrane proteins. Engagement of CLEC1B by PDPN promotes FRCs relaxation by blocking lateral membrane interactions leading to reduction of ERM proteins (EZR; MSN and RDX) and MYL9 activation (PubMed:25347465). Through binding with LGALS8 may participate to connection of the lymphatic endothelium to the surrounding extracellular matrix (By similarity). In keratinocytes, induces changes in cell morphology showing an elongated shape, numerous membrane protrusions, major reorganization of the actin cytoskeleton, increased motility and decreased cell adhesion (PubMed:10574709). Controls invadopodia stability and maturation leading to efficient degradation of the extracellular matrix (ECM) in tumor cells through modulation of RHOC activity in order to activate ROCK1/ROCK2 and LIMK1/LIMK2 and inactivation of CFL1 (By similarity). Required for normal lung cell proliferation and alveolus formation at birth (PubMed:12654292). Does not function as a water channel or as a regulator of aquaporin-type water channels (By similarity). Does not have any effect on folic acid or amino acid transport (PubMed:12032185). {ECO:0000250|UniProtKB:Q86YL7, ECO:0000269|PubMed:10574709, ECO:0000269|PubMed:12032185, ECO:0000269|PubMed:12654292, ECO:0000269|PubMed:14522983, ECO:0000269|PubMed:15231832, ECO:0000269|PubMed:17616532, ECO:0000269|PubMed:20110424, ECO:0000269|PubMed:25347465}. PTM: Extensively O-glycosylated. Contains sialic acid residues. O-glycosylation is necessary for platelet aggregation activity. Disialylated at Thr-52; sialic acid is critical for platelet-aggregating activity and for CLEC1B interaction (By similarity). {ECO:0000250|UniProtKB:Q86YL7, ECO:0000269|PubMed:10574709, ECO:0000269|PubMed:15231832}.; PTM: Phosphorylated by PKA; decreases cell migration. {ECO:0000269|PubMed:23530051}.; PTM: The N-terminus is blocked. {ECO:0000250|UniProtKB:Q64294}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10574709}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, lamellipodium membrane {ECO:0000269|PubMed:10574709}; Single-pass type I membrane protein {ECO:0000269|PubMed:10574709}. Cell projection, filopodium membrane {ECO:0000269|PubMed:10574709}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, microvillus membrane {ECO:0000269|PubMed:10574709}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, ruffle membrane {ECO:0000269|PubMed:10574709}; Single-pass type I membrane protein {ECO:0000255}. Membrane raft {ECO:0000250|UniProtKB:Q86YL7}. Apical cell membrane {ECO:0000250|UniProtKB:Q86YL7}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q86YL7}. Cell projection, invadopodium {ECO:0000250|UniProtKB:Q86YL7}. Note=Localized to actin-rich microvilli and plasma membrane projections such as filopodia, lamellipodia and ruffles (PubMed:10574709). Association to the lipid rafts is required for PDPN-induced epithelial to mesenchymal transition (EMT). Colocalizes with CD9 in tetraspanin microdomains. Localized at invadopodium adhesion rings in tumor cell. Association to the lipid rafts is essential for PDPN recruitment to invadopodia and ECM degradation (By similarity). {ECO:0000250|UniProtKB:Q86YL7, ECO:0000269|PubMed:10574709}. SUBUNIT: Homodimer. Interacts with CLEC1B; the interaction is independent of CLEC1B glycosylation and activates CLEC1B; the interaction is dependent of sialic acid on O-glycans (PubMed:17616532). Interacts with CD9; this interaction is homophilic and attenuates platelet aggregation and pulmonary metastasis induced by PDPN. Interacts with LGALS8; the interaction is glycosylation-dependent; may participate to connection of the lymphatic endothelium to the surrounding extracellular matrix. Interacts with HSPA9. Interacts (via extracellular domain) with CD44; this interaction is required for PDPN-mediated directional migration and regulation of lamellipodia extension/stabilization during cell spreading and migration. Interacts (via cytoplasmic domain) with MSN and EZR; activates RHOA and promotes epithelial-mesenchymal transition. Interacts with CCL21; relocalized PDPN to the basolateral membrane (By similarity). {ECO:0000250|UniProtKB:Q86YL7, ECO:0000269|PubMed:17616532}. DOMAIN: The cytoplasmic domain controls FRC elongation but is dispensable for contraction (PubMed:25347465). The cytoplasmic domain is essential for recruitment to invadopodia and ECM degradation (By similarity). {ECO:0000250|UniProtKB:Q86YL7, ECO:0000269|PubMed:25347465}. TISSUE SPECIFICITY: Detected at high levels in lung and brain, at lower levels in kidney, stomach, liver, spleen and esophagus, and not detected in skin and small intestine. Expressed in epithelial cells of choroid plexus, ependyma, glomerulus and alveolus, in mesothelial cells and in endothelia of lymphatic vessels. Also expressed in stromal cells of peripheral lymphoid tissue and thymic epithelial cells. Detected in carcinoma cell lines and cultured fibroblasts. Expressed at higher levels in colon carcinomas than in normal colon tissue. {ECO:0000269|PubMed:10574709, ECO:0000269|PubMed:12032185, ECO:0000269|PubMed:14522983}. +Q7TSQ8 PDPR_MOUSE Pyruvate dehydrogenase phosphatase regulatory subunit, mitochondrial (PDPr) 878 99,230 Chain (1); Erroneous initiation (1); Sequence conflict (1); Transit peptide (1) FUNCTION: Decreases the sensitivity of PDP1 to magnesium ions, and this inhibition is reversed by the polyamine spermine. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. SUBUNIT: Heterodimer of a catalytic (PDP1) and a regulatory (PDPR) subunit. {ECO:0000250}. +P59048 PDRG1_MOUSE p53 and DNA damage-regulated protein 1 133 15,382 Chain (1) FUNCTION: May play a role in chaperone-mediated protein folding. {ECO:0000305}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. +Q4VA53 PDS5B_MOUSE Sister chromatid cohesion protein PDS5 homolog B (Androgen-induced proliferation inhibitor) (Androgen-induced prostate proliferative shutoff-associated protein AS3) 1446 164,419 Alternative sequence (4); Chain (1); DNA binding (3); Modified residue (19); Repeat (1); Sequence conflict (3) FUNCTION: Regulator of sister chromatid cohesion in mitosis which may stabilize cohesin complex association with chromatin. May couple sister chromatid cohesion during mitosis to DNA replication. Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair. Plays a role in androgen-induced proliferative arrest in prostate cells (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6TRW4}. SUBUNIT: Interacts with the cohesin complex. Interacts with RAD21; the interaction is direct. Interacts with WAPL (via FGF motifs) or CDCA5 (via the FGF motif); the interaction is direct, cohesin-dependent and competitive (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in prostate. {ECO:0000269|Ref.1}. +P52946 PDX1_MOUSE Pancreas/duodenum homeobox protein 1 (Insulin promoter factor 1) (IPF-1) (Islet/duodenum homeobox 1) (IDX-1) (Somatostatin-transactivating factor 1) (STF-1) 284 30,999 Chain (1); Compositional bias (2); DNA binding (1); Modified residue (2); Motif (2); Mutagenesis (3); Region (1) FUNCTION: Activates insulin and somatostatin gene transcription. Key regulator of islet peptide hormone expression but also responsible for the development of the pancreas, most probably by determining maturation and differentiation of common pancreatic precursor cells in the developing gut. As part of a PDX1:PBX1b:MEIS2b complex in pancreatic acinar cells is involved in the transcriptional activation of the ELA1 enhancer; the complex binds to the enhancer B element and cooperates with the transcription factor 1 complex (PTF1) bound to the enhancer A element. Binds the DNA sequence 5'-CC[CT]TAATGGG-3'. {ECO:0000269|PubMed:11279116, ECO:0000269|PubMed:9710595}. PTM: Phosphorylated by the SAPK2 pathway at high intracellular glucose concentration. Phosphorylated by HIPK2 on Ser-269 upon glucose accumulation. This phosphorylation mediates subnuclear localization shifting. Phosphorylation by PASK may lead to translocation into the cytosol. {ECO:0000269|PubMed:17052199, ECO:0000269|PubMed:20637728}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:17052199}. Cytoplasm, cytosol {ECO:0000269|PubMed:17052199}. SUBUNIT: Interacts with the basic helix-loop-helix domains of TCF3(E47) and NEUROD1 and with HMG-I(Y). Interacts with the methyltransferase SETD7 (By similarity). Interacts with SPOP. Part of a PDX1:PBX1b:MEIS2b complex. {ECO:0000250, ECO:0000269|PubMed:11279116, ECO:0000269|PubMed:15121856, ECO:0000269|PubMed:9710595}. DOMAIN: The Antp-type hexapeptide mediates heterodimerization with PBX on a regulatory element of the somatostatin promoter. {ECO:0000250}.; DOMAIN: The homeodomain, which contains the nuclear localization signal, not only mediates DNA-binding, but also acts as a protein-protein interaction domain for TCF3(E47), NEUROD1 and HMG-I(Y). {ECO:0000250}. TISSUE SPECIFICITY: Duodenum and pancreas (Langerhans islet beta cells and small subsets of endocrine non-beta-cells, at low levels in acinar cells). +P30557 PE2R3_MOUSE Prostaglandin E2 receptor EP3 subtype (PGE receptor EP3 subtype) (PGE2 receptor EP3 subtype) (Prostanoid EP3 receptor) 365 40,077 Alternative sequence (2); Chain (1); Disulfide bond (1); Glycosylation (2); Topological domain (8); Transmembrane (7) TRANSMEM 31 55 Helical; Name=1. {ECO:0000255}.; TRANSMEM 69 89 Helical; Name=2. {ECO:0000255}.; TRANSMEM 109 130 Helical; Name=3. {ECO:0000255}.; TRANSMEM 152 173 Helical; Name=4. {ECO:0000255}.; TRANSMEM 204 229 Helical; Name=5. {ECO:0000255}.; TRANSMEM 260 283 Helical; Name=6. {ECO:0000255}.; TRANSMEM 304 325 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 30 Extracellular. {ECO:0000255}.; TOPO_DOM 56 68 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 90 108 Extracellular. {ECO:0000255}.; TOPO_DOM 131 151 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 174 203 Extracellular. {ECO:0000255}.; TOPO_DOM 230 259 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 284 303 Extracellular. {ECO:0000255}.; TOPO_DOM 326 365 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for prostaglandin E2 (PGE2) (PubMed:1372606, PubMed:8381413, PubMed:8223569). Required for normal development of fever in response to pyrinogens, including IL1B, prostaglandin E2 and bacterial lipopolysaccharide (LPS) (PubMed:9751056). Required for normal potentiation of platelet aggregation by prostaglandin E2, and thus plays a role in the regulation of blood coagulation (PubMed:11535576). Required for increased HCO3(-) secretion in the duodenum in response to mucosal acidification, and thereby contributes to the protection of the mucosa against acid-induced ulceration (PubMed:10535876). Not required for normal kidney function, normal urine volume and osmolality (PubMed:9843913). {ECO:0000269|PubMed:10535876, ECO:0000269|PubMed:11535576, ECO:0000269|PubMed:1372606, ECO:0000269|PubMed:8223569, ECO:0000269|PubMed:8381413, ECO:0000269|PubMed:9751056, ECO:0000269|PubMed:9843913}.; FUNCTION: Isoform Alpha: Receptor for prostaglandin E2 (PGE2); ligand binding activates a signaling cascade via G(i) proteins that leads to inhibition of adenylate cyclase (PubMed:1372606, PubMed:8381413). Shows high agonist-independent constitutive inhibition of adenylate cyclase (PubMed:8223569). {ECO:0000269|PubMed:1372606, ECO:0000269|PubMed:8223569, ECO:0000269|PubMed:8381413}.; FUNCTION: Isoform Beta: Receptor for prostaglandin E2 (PGE2); ligand binding activates a signaling cascade via G(i) proteins that leads to inhibition of adenylate cyclase. Requires much higher ligand concentrations than isoform Alpha for activation (PubMed:8381413). Does not display agonist-independent constitutive inhibition of adenylate cyclase (PubMed:8223569). {ECO:0000269|PubMed:8223569, ECO:0000269|PubMed:8381413}.; FUNCTION: Isoform Gamma: Receptor for prostaglandin E2 (PGE2); ligand binding can activate several distinct signaling cascades, resulting in activation or inhibition of adenylate cyclase. {ECO:0000269|PubMed:8223569}. PTM: Ligand binding is affected by cAMP-dependent phosphorylation in brain membranes. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1372606, ECO:0000269|PubMed:8223569, ECO:0000269|PubMed:8381413}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Interacts (via C-terminus) with MKLN1. {ECO:0000250|UniProtKB:P34980}. TISSUE SPECIFICITY: Detected in platelets (PubMed:11535576). Kidney, uterus, and mastocytoma cells, and in a lesser amount in brain, thymus, lung, heart, stomach and spleen (PubMed:1372606). {ECO:0000269|PubMed:11535576, ECO:0000269|PubMed:1372606}. +Q9CQH0 PDZ1I_MOUSE PDZK1-interacting protein 1 (17 kDa membrane-associated protein) 114 12,298 Chain (1); Modified residue (1); Transmembrane (1) TRANSMEM 30 50 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with PDZK1. {ECO:0000250}. +Q8BST6 PELI2_MOUSE E3 ubiquitin-protein ligase pellino homolog 2 (Pellino-2) (EC 2.3.2.27) (RING-type E3 ubiquitin transferase pellino homolog 2) 419 46,272 Alternative sequence (3); Chain (1); Domain (1); Sequence conflict (9) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins. Involved in the TLR and IL-1 signaling pathways via interaction with the complex containing IRAK kinases and TRAF6. Mediates IL1B-induced IRAK1 'Lys-63'-linked polyubiquitination and possibly 'Lys-48'-linked ubiquitination. May be important for LPS- and IL1B-induced MAP3K7-dependent, but not MAP3K3-dependent, NF-kappa-B activation. Can activate the MAP (mitogen activated protein) kinase pathway leading to activation of ELK1. {ECO:0000269|PubMed:12370331, ECO:0000269|PubMed:22669975}. PTM: Phosphorylated by IRAK1 and IRAK4 enhancing its E3 ligase activity. {ECO:0000250}. SUBUNIT: Interacts with TRAF6, IRAK4 and MAP3K7 (By similarity). Interacts with IRAK1. Interacts with BCL10; this interaction is impaired by SOCS3. {ECO:0000250, ECO:0000269|PubMed:12370331, ECO:0000269|PubMed:15213237}. DOMAIN: The atypical FHA domain contains a 'wing' insert and mediates binding to threonine-phosphorylated IRAK1. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed both in embryos and adult. Weakly or not expressed in spleen and thymus. {ECO:0000269|PubMed:12370331}. +P32240 PE2R4_MOUSE Prostaglandin E2 receptor EP4 subtype (PGE receptor EP4 subtype) (PGE2 receptor EP4 subtype) (Prostanoid EP4 receptor) 513 56,158 Chain (1); Compositional bias (1); Disulfide bond (1); Glycosylation (1); Modified residue (3); Topological domain (8); Transmembrane (7) TRANSMEM 45 68 Helical; Name=1. {ECO:0000255}.; TRANSMEM 81 104 Helical; Name=2. {ECO:0000255}.; TRANSMEM 122 140 Helical; Name=3. {ECO:0000255}.; TRANSMEM 161 185 Helical; Name=4. {ECO:0000255}.; TRANSMEM 210 236 Helical; Name=5. {ECO:0000255}.; TRANSMEM 296 323 Helical; Name=6. {ECO:0000255}.; TRANSMEM 341 360 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 44 Extracellular. {ECO:0000255}.; TOPO_DOM 69 80 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 105 121 Extracellular. {ECO:0000255}.; TOPO_DOM 141 160 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 186 209 Extracellular. {ECO:0000255}.; TOPO_DOM 237 295 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 324 340 Extracellular. {ECO:0000255}.; TOPO_DOM 361 513 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for prostaglandin E2 (PGE2). The activity of this receptor is mediated by G(s) proteins that stimulate adenylate cyclase. Has a relaxing effect on smooth muscle. May play an important role in regulating renal hemodynamics, intestinal epithelial transport, adrenal aldosterone secretion, and uterine function. PTM: Phosphorylation mediates agonist-mediated desensitization by promoting cytoplasmic retention. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBUNIT: Interacts with FEM1A. {ECO:0000250}. TISSUE SPECIFICITY: Abundant expression in ileum, thymus and mastocytoma P-815 cells. Also observed in lung, spleen, heart and uterus. +Q6ZPR5 NSMA3_MOUSE Sphingomyelin phosphodiesterase 4 (EC 3.1.4.12) (Neutral sphingomyelinase 3) (nSMase-3) (nSMase3) (Neutral sphingomyelinase III) 823 93,276 Alternative sequence (4); Chain (1); Erroneous initiation (1); Modified residue (4); Sequence conflict (6); Transmembrane (1) TRANSMEM 776 796 Helical. {ECO:0000255}. FUNCTION: Catalyzes the hydrolysis of membrane sphingomyelin to form phosphorylcholine and ceramide. May sensitize cells to DNA damage-induced apoptosis. {ECO:0000250|UniProtKB:Q9NXE4}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. Golgi apparatus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9NXE4}. +O08705 NTCP_MOUSE Sodium/bile acid cotransporter (Na(+)/bile acid cotransporter) (Na(+)/taurocholate transport protein) (Sodium/taurocholate cotransporting polypeptide) (Solute carrier family 10 member 1) 362 39,413 Chain (1); Glycosylation (5); Modified residue (1); Transmembrane (7) TRANSMEM 24 45 Helical. {ECO:0000255}.; TRANSMEM 60 80 Helical. {ECO:0000255}.; TRANSMEM 82 98 Helical. {ECO:0000255}.; TRANSMEM 158 178 Helical. {ECO:0000255}.; TRANSMEM 190 211 Helical. {ECO:0000255}.; TRANSMEM 228 244 Helical. {ECO:0000255}.; TRANSMEM 285 306 Helical. {ECO:0000255}. FUNCTION: The hepatic sodium/bile acid uptake system exhibits broad substrate specificity and transports various non-bile acid organic compounds as well. It is strictly dependent on the extracellular presence of sodium. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. +Q8VCE6 NT5M_MOUSE 5'(3')-deoxyribonucleotidase, mitochondrial (5',3'-nucleotidase, mitochondrial) (EC 3.1.3.-) (Deoxy-5'-nucleotidase 2) (dNT-2) 220 25,602 Active site (2); Binding site (8); Chain (1); Metal binding (3); Transit peptide (1) FUNCTION: Dephosphorylates specifically the 5' and 2'(3')-phosphates of uracil and thymine deoxyribonucleotides, and so protects mitochondrial DNA replication from excess dTTP. Has only marginal activity towards dIMP and dGMP. {ECO:0000269|PubMed:12234672}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000305}. +Q9DCN1 NUD12_MOUSE Peroxisomal NADH pyrophosphatase NUDT12 (EC 3.6.1.22) (Nucleoside diphosphate-linked moiety X motif 12) (Nudix motif 12) 462 51,511 Alternative sequence (2); Chain (1); Domain (1); Metal binding (2); Modified residue (3); Motif (2); Repeat (3); Sequence conflict (2) FUNCTION: Hydrolyzes NAD(P)H to NMNH and AMP (2',5'-ADP), and diadenosine diphosphate to AMP. Has also activity towards NAD(P)(+), ADP-ribose and diadenosine triphosphate. May act to regulate the concentration of peroxisomal nicotinamide nucleotide cofactors required for oxidative metabolism in this organelle (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}. +Q9R1P4 PSA1_MOUSE Proteasome subunit alpha type-1 (EC 3.4.25.1) (Macropain subunit C2) (Multicatalytic endopeptidase complex subunit C2) (Proteasome component C2) (Proteasome nu chain) 263 29,547 Beta strand (13); Chain (1); Cross-link (2); Glycosylation (1); Helix (8); Modified residue (3); Turn (4) FUNCTION: Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). {ECO:0000269|PubMed:12874245, ECO:0000269|PubMed:16581775, ECO:0000269|PubMed:19526544, ECO:0000269|PubMed:22341445}. PTM: C-terminal extension is partially cleaved off by limited proteolysis leading to a conversion of the proteasome from its latent into its active form. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P25786}. Nucleus {ECO:0000250|UniProtKB:P25786}. SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is a barrel-shaped complex made of 28 subunits that are arranged in four stacked rings. The two outer rings are each formed by seven alpha subunits, and the two inner rings are formed by seven beta subunits. The proteolytic activity is exerted by three beta-subunits PSMB5, PSMB6 and PSMB7 (PubMed:16857966). Interacts with NOTCH3 (By similarity). Interacts with ZFAND1 (By similarity). {ECO:0000250|UniProtKB:P25786, ECO:0000269|PubMed:16857966, ECO:0000269|PubMed:22341445}. TISSUE SPECIFICITY: Detected in liver (at protein level). {ECO:0000269|PubMed:22341445}. +Q9QZS3 NUMB_MOUSE Protein numb homolog (m-Nb) (m-Numb) 653 70,813 Alternative sequence (2); Beta strand (9); Chain (1); Domain (1); Helix (3); Modified residue (9); Sequence conflict (2); Turn (3) FUNCTION: Plays a role in the process of neurogenesis. Required throughout embryonic neurogenesis to maintain neural progenitor cells, also called radial glial cells (RGCs), by allowing their daughter cells to choose progenitor over neuronal cell fate. Not required for the proliferation of neural progenitor cells before the onset of neurogenesis. Also involved postnatally in the subventricular zone (SVZ) neurogenesis by regulating SVZ neuroblasts survival and ependymal wall integrity. May also mediate local repair of brain ventricular wall damage. {ECO:0000269|PubMed:10841580, ECO:0000269|PubMed:12410312, ECO:0000269|PubMed:15273690, ECO:0000269|PubMed:17174898}. PTM: Phosphorylated on Ser-276 and Ser-295 by CaMK1. {ECO:0000250}.; PTM: Ubiquitinated; mediated by SIAH1 and leading to its subsequent proteasomal degradation (By similarity) Isoform 1 and isoform 2 are ubiquitinated by LNX leading to their subsequent proteasomal degradation. {ECO:0000250, ECO:0000269|PubMed:11782429}. SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein. SUBUNIT: May interact with DUOXA1 (By similarity). Interacts with TFAP2B (By similarity). Interacts with CDH1, EPS15, LNX and NOTCH1. Interacts with RALBP1 in a complex also containing EPN1 and TFAP2A during interphase and mitosis. {ECO:0000250, ECO:0000269|PubMed:17174898, ECO:0000269|PubMed:9535908}. TISSUE SPECIFICITY: Expressed in subventricular zone (SVZ) neuroprogenitors and ependymal cells. {ECO:0000269|PubMed:17174898}. +Q9R1P0 PSA4_MOUSE Proteasome subunit alpha type-4 (EC 3.4.25.1) (Macropain subunit C9) (Multicatalytic endopeptidase complex subunit C9) (Proteasome component C9) (Proteasome subunit L) 261 29,471 Beta strand (12); Chain (1); Helix (7); Modified residue (5); Turn (3) FUNCTION: Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). {ECO:0000269|PubMed:16581775, ECO:0000269|PubMed:22341445}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22078707}. Nucleus {ECO:0000269|PubMed:22078707}. Note=Colocalizes with TRIM5 in the cytoplasmic bodies. {ECO:0000269|PubMed:22078707}. SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is a barrel-shaped complex made of 28 subunits that are arranged in four stacked rings. The two outer rings are each formed by seven alpha subunits, and the two inner rings are formed by seven beta subunits. The proteolytic activity is exerted by three beta-subunits PSMB5, PSMB6 and PSMB7 (PubMed:16857966, PubMed:22341445). {ECO:0000269|PubMed:16857966, ECO:0000269|PubMed:22341445}. TISSUE SPECIFICITY: Detected in liver (at protein level). {ECO:0000269|PubMed:22341445}. +Q9QUM9 PSA6_MOUSE Proteasome subunit alpha type-6 (EC 3.4.25.1) (Macropain iota chain) (Multicatalytic endopeptidase complex iota chain) (Proteasome iota chain) 246 27,372 Beta strand (10); Chain (1); Glycosylation (1); Helix (7); Modified residue (6); Sequence conflict (1); Turn (4) FUNCTION: Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). {ECO:0000269|PubMed:16581775, ECO:0000269|PubMed:22341445}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22078707}. Nucleus {ECO:0000269|PubMed:22078707}. Note=Colocalizes with TRIM5 in cytoplasmic bodies. {ECO:0000269|PubMed:22078707}. SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is a barrel-shaped complex made of 28 subunits that are arranged in four stacked rings. The two outer rings are each formed by seven alpha subunits, and the two inner rings are formed by seven beta subunits. The proteolytic activity is exerted by three beta-subunits PSMB5, PSMB6 and PSMB7 (PubMed:16857966, PubMed:22341445). Interacts with ALKBH4 (By similarity). {ECO:0000250|UniProtKB:P60900, ECO:0000269|PubMed:16857966, ECO:0000269|PubMed:22341445}. TISSUE SPECIFICITY: Detected in liver (at protein level). {ECO:0000269|PubMed:22341445}. +Q8R332 NUP58_MOUSE Nucleoporin p58/p45 (58 kDa nucleoporin) (Nucleoporin-like protein 1) 587 59,445 Alternative sequence (3); Chain (1); Coiled coil (2); Modified residue (1); Region (1); Repeat (14); Sequence conflict (5) FUNCTION: Component of the nuclear pore complex, a complex required for the trafficking across the nuclear membrane. {ECO:0000250|UniProtKB:P70581}. PTM: O-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P70581}. Nucleus membrane {ECO:0000250|UniProtKB:P70581}; Peripheral membrane protein {ECO:0000250|UniProtKB:P70581}; Cytoplasmic side {ECO:0000250|UniProtKB:P70581}. Nucleus membrane {ECO:0000250|UniProtKB:P70581}; Peripheral membrane protein {ECO:0000250|UniProtKB:P70581}; Nucleoplasmic side {ECO:0000250|UniProtKB:P70581}. Note=Biased towards cytoplasmic side. Central region of the nuclear pore complex, within the transporter. {ECO:0000250|UniProtKB:P70581}. SUBUNIT: Component of the p62 complex, a complex at least composed of NUP62, NUP54, and NUP58. Interacts with NUTF2. Interacts with SRP1-alpha and Importin p97 proteins when they are together, but not with SRP1-alpha protein alone (By similarity). {ECO:0000250|UniProtKB:P70581}. DOMAIN: Contains FG repeats. +Q9CWU9 NUP37_MOUSE Nucleoporin Nup37 (Nup107-160 subcomplex subunit Nup37) 326 36,732 Chain (1); Repeat (4); Sequence conflict (2) FUNCTION: Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex is required for the assembly of a functional NPC. The Nup107-160 subcomplex is also required for normal kinetochore microtubule attachment, mitotic progression and chromosome segregation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250}. SUBUNIT: Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex includes NUP160, NUP133, NUP107, NUP98, NUP85, NUP43, NUP37, SEH1 and SEC13 (By similarity). {ECO:0000250}. +P59235 NUP43_MOUSE Nucleoporin Nup43 (Nup107-160 subcomplex subunit Nup43) 380 41,990 Chain (1); Modified residue (1); Repeat (6); Sequence conflict (2) FUNCTION: Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex is required for the assembly of a functional NPC. The Nup107-160 subcomplex is also required for normal kinetochore microtubule attachment, mitotic progression and chromosome segregation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250}. SUBUNIT: Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex includes NUP160, NUP133, NUP107, NUP98, NUP85, NUP43, NUP37, SEH1 and SEC13 (By similarity). {ECO:0000250}. +Q8BTS4 NUP54_MOUSE Nuclear pore complex protein Nup54 (54 kDa nucleoporin) (Nucleoporin Nup54) 510 55,732 Chain (1); Compositional bias (4); Region (1); Repeat (8) FUNCTION: Component of the nuclear pore complex, a complex required for the trafficking across the nuclear membrane. {ECO:0000250|UniProtKB:P70582}. PTM: O-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P70582}. Nucleus membrane {ECO:0000250|UniProtKB:P70582}; Peripheral membrane protein {ECO:0000250|UniProtKB:P70582}; Cytoplasmic side {ECO:0000250|UniProtKB:P70582}. Nucleus membrane {ECO:0000250|UniProtKB:P70582}; Peripheral membrane protein {ECO:0000250|UniProtKB:P70582}; Nucleoplasmic side {ECO:0000250|UniProtKB:P70582}. Note=Biased towards cytoplasmic side. Central region of the nuclear pore complex, within the transporter. {ECO:0000250|UniProtKB:P70582}. SUBUNIT: Component of the p62 complex, a complex composed of NUP62, NUP54, and the isoform p58 and isoform p45 of NUP58. Interacts with NUTF2. {ECO:0000250|UniProtKB:P70582}. DOMAIN: Contains FG repeats. +Q8CEC0 NUP88_MOUSE Nuclear pore complex protein Nup88 (88 kDa nucleoporin) (Nucleoporin Nup88) 753 84,938 Alternative sequence (2); Chain (1); Coiled coil (1); Initiator methionine (1); Modified residue (8); Sequence conflict (4) FUNCTION: Essential component of nuclear pore complex. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nuclear pore complex {ECO:0000250}. SUBUNIT: Interacts with NUP214/CAN. {ECO:0000250}. +Q6NVF0 OCRL_MOUSE Inositol polyphosphate 5-phosphatase OCRL-1 (EC 3.1.3.36) 900 104,285 Alternative sequence (2); Chain (1); Domain (2); Motif (2); Region (2) FUNCTION: Converts phosphatidylinositol 4,5-bisphosphate to phosphatidylinositol 4-phosphate. Also converts inositol 1,4,5-trisphosphate to inositol 1,4-bisphosphate and inositol 1,3,4,5-tetrakisphosphate to inositol 1,3,4-trisphosphate. May function in lysosomal membrane trafficking by regulating the specific pool of phosphatidylinositol 4,5-bisphosphate that is associated with lysosomes. Involved in primary cilia assembly (By similarity). {ECO:0000250|UniProtKB:Q01968}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:D3ZGS3}. Early endosome membrane {ECO:0000250|UniProtKB:Q01968}. Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:Q01968}. Cell projection, cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:Q01968}. Cell projection, cilium {ECO:0000250|UniProtKB:Q01968}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:D3ZGS3}. Endosome {ECO:0000250|UniProtKB:Q01968}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:D3ZGS3}. Note=Also found on macropinosomes. {ECO:0000250|UniProtKB:Q01968}. SUBUNIT: Interacts with APPL1, PHETA1/SES1 and PHETA2/SES2; APPL1-binding and PHETA1-binding are mutually exclusive (By similarity). Interacts with clathrin heavy chain. Interacts with several Rab GTPases, at least RAB1B, RAB5A, RAB6A, RAB8A and RAB31; these interactions may play a dual role in targeting OCRL to the specific membranes and stimulating the phosphatase activitye (PubMed:25869668). Interaction with RAB8A modulates OCRL recruitment to cilia. Interacts with RAB31 (By similarity). Interacts with INPP5F (PubMed:25869668). {ECO:0000250|UniProtKB:Q01968, ECO:0000269|PubMed:25869668}. DOMAIN: The ASH (ASPM-SPD2-Hydin) and RhoGAP (Rho GTPase activating) domains form a single folding module. The ASH domain has an immunoglobulin-like fold, the Rho-GAP domain lacks the catalytic arginine and is catalytically inactive. The ASH-RhoGAP module regulates the majority of the protein-protein interactions currently described. The ASH domain mediates association with membrane-targeting Rab GTPases. The Rho-GAP domain interacts with the endocytic adapter APPL1, which is then displaced by PHETA1 and PHETA2 as endosomes mature (By similarity). {ECO:0000250}. +Q8VI88 ODFP4_MOUSE Outer dense fiber protein 4 (Outer dense fiber of sperm tails protein 4) (Testis-specific protein oppo 1) 290 33,177 Alternative sequence (2); Chain (1); Compositional bias (1); Modified residue (1); Sequence conflict (1); Transmembrane (4) TRANSMEM 44 64 Helical. {ECO:0000255}.; TRANSMEM 125 145 Helical. {ECO:0000255}.; TRANSMEM 164 184 Helical. {ECO:0000255}.; TRANSMEM 201 221 Helical. {ECO:0000255}. FUNCTION: Component of the outer dense fibers (ODF) of spermatozoa which could be involved in sperm tail structure, sperm movement and general organization of cellular cytoskeleton. {ECO:0000269|PubMed:12079992}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:12079992}. +A1E960 ODAM_MOUSE Odontogenic ameloblast-associated protein (Apin) 273 29,820 Chain (1); Compositional bias (1); Erroneous initiation (3); Glycosylation (9); Region (1); Signal peptide (1) FUNCTION: Tooth-associated epithelia protein that probably plays a role in odontogenesis, the complex process that results in the initiation and generation of the tooth. May be incorporated in the enamel matrix at the end of mineralization process. Involved in the induction of RHOA activity via interaction with ARHGEF and expression of downstream factors such as ROCK. Plays a role in attachment of the junctional epithelium to the tooth surface. {ECO:0000250|UniProtKB:A1E959}. PTM: O-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q3HS83}. Cytoplasm {ECO:0000250|UniProtKB:A1E959}. Nucleus {ECO:0000250|UniProtKB:A1E959}. SUBUNIT: Interacts (via C-terminus) with ARHGEF5. {ECO:0000250|UniProtKB:A1E959}. TISSUE SPECIFICITY: Highly expressed in tooth-associated epithelia. Predominantly expressed in mandible. {ECO:0000269|PubMed:17647262}. +Q8BP74 PSTK_MOUSE L-seryl-tRNA(Sec) kinase (EC 2.7.1.164) (O-phosphoseryl-tRNA(Sec) kinase) 359 40,763 Alternative sequence (1); Chain (1); Nucleotide binding (1) Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec) (archaeal/eukaryal route): step 1/2. FUNCTION: Specifically phosphorylates seryl-tRNA(Sec) to O-phosphoseryl-tRNA(Sec), an activated intermediate for selenocysteine biosynthesis. No activity with other tRNAs has been detected. +Q61038 PSYR_MOUSE Psychosine receptor (G-protein coupled receptor 65) (T-cell death-associated gene 8 protein) 337 39,388 Chain (1); Disulfide bond (1); Glycosylation (2); Sequence conflict (2); Topological domain (8); Transmembrane (7) TRANSMEM 18 38 Helical; Name=1. {ECO:0000255}.; TRANSMEM 53 73 Helical; Name=2. {ECO:0000255}.; TRANSMEM 92 112 Helical; Name=3. {ECO:0000255}.; TRANSMEM 132 152 Helical; Name=4. {ECO:0000255}.; TRANSMEM 183 203 Helical; Name=5. {ECO:0000255}.; TRANSMEM 230 250 Helical; Name=6. {ECO:0000255}.; TRANSMEM 274 294 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 17 Extracellular. {ECO:0000255}.; TOPO_DOM 39 52 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 74 91 Extracellular. {ECO:0000255}.; TOPO_DOM 113 131 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 153 182 Extracellular. {ECO:0000255}.; TOPO_DOM 204 229 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 251 273 Extracellular. {ECO:0000255}.; TOPO_DOM 295 337 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for the glycosphingolipid psychosine (PSY) and several related glycosphingolipids (By similarity). Plays a role in immune response by maintaining lysosome function and supporting phagocytosis-mediated intracellular bacteria clearance (PubMed:27287411). May have a role in activation-induced cell death or differentiation of T-cells (PubMed:8599842). {ECO:0000250|UniProtKB:Q8IYL9, ECO:0000269|PubMed:27287411, ECO:0000269|PubMed:8599842}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Detected in thymus and at low levels in spleen. +P0DJE0 PT100_MOUSE Protein PET100 homolog, mitochondrial 76 9,410 Chain (1); Transit peptide (1); Transmembrane (1) TRANSMEM 7 24 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Mitochondrion {ECO:0000269|PubMed:22356826}. Note=Localizes to a membrane-bound organelle. {ECO:0000250}. SUBUNIT: Interacts with COX7A2. {ECO:0000250}. +P0DJF2 PT117_MOUSE Protein PET117 homolog, mitochondrial 80 9,124 Chain (1); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}. +Q62035 PTAFR_MOUSE Platelet-activating factor receptor (PAF-R) (PAFr) 341 39,148 Chain (1); Disulfide bond (1); Glycosylation (2); Sequence conflict (1); Topological domain (8); Transmembrane (7) TRANSMEM 17 38 Helical; Name=1. {ECO:0000255}.; TRANSMEM 55 74 Helical; Name=2. {ECO:0000255}.; TRANSMEM 92 113 Helical; Name=3. {ECO:0000255}.; TRANSMEM 134 155 Helical; Name=4. {ECO:0000255}.; TRANSMEM 185 205 Helical; Name=5. {ECO:0000255}.; TRANSMEM 234 254 Helical; Name=6. {ECO:0000255}.; TRANSMEM 276 295 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 16 Extracellular. {ECO:0000255}.; TOPO_DOM 39 54 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 75 91 Extracellular. {ECO:0000255}.; TOPO_DOM 114 133 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 156 184 Extracellular. {ECO:0000255}.; TOPO_DOM 206 233 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 255 275 Extracellular. {ECO:0000255}.; TOPO_DOM 296 341 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for platelet activating factor, a chemotactic phospholipid mediator that possesses potent inflammatory, smooth-muscle contractile and hypotensive activity. Seems to mediate its action via a G protein that activates a phosphatidylinositol-calcium second messenger system. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBUNIT: Interacts with ARRB1. {ECO:0000250}. TISSUE SPECIFICITY: Found in a range of organs. Expressed most strongly in spleen, followed by skeletal muscle, lung and small intestine. Expressed at moderate levels in the heart. Expressed at relatively low levels in the brain, liver and kidney. {ECO:0000269|PubMed:8670084}. +O35599 OPSG_MOUSE Medium-wave-sensitive opsin 1 (Green cone photoreceptor pigment) (Green-sensitive opsin) (M opsin) (Medium wavelength-sensitive cone opsin) 359 40,218 Chain (1); Disulfide bond (1); Glycosylation (1); Modified residue (1); Topological domain (8); Transmembrane (7) TRANSMEM 48 72 Helical; Name=1. {ECO:0000255}.; TRANSMEM 85 110 Helical; Name=2. {ECO:0000255}.; TRANSMEM 125 144 Helical; Name=3. {ECO:0000255}.; TRANSMEM 164 187 Helical; Name=4. {ECO:0000255}.; TRANSMEM 214 241 Helical; Name=5. {ECO:0000255}.; TRANSMEM 264 287 Helical; Name=6. {ECO:0000255}.; TRANSMEM 296 320 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 47 Extracellular. {ECO:0000255}.; TOPO_DOM 73 84 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 111 124 Extracellular. {ECO:0000255}.; TOPO_DOM 145 163 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 188 213 Extracellular. {ECO:0000255}.; TOPO_DOM 242 263 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 288 295 Extracellular. {ECO:0000255}.; TOPO_DOM 321 359 Cytoplasmic. {ECO:0000255}. FUNCTION: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal. May increase spectral sensitivity in dim light. {ECO:0000269|PubMed:11055434}. PTM: Phosphorylated on some or all of the serine and threonine residues present in the C-terminal region. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SUBUNIT: Monomer. Homodimer. Homotetramer. {ECO:0000250|UniProtKB:P04001}. TISSUE SPECIFICITY: Expressed in cone photoreceptor cells. {ECO:0000269|PubMed:11055434}. +O35214 OPSX_MOUSE Visual pigment-like receptor peropsin 337 37,209 Chain (1); Disulfide bond (1); Glycosylation (2); Modified residue (1); Topological domain (8); Transmembrane (7) TRANSMEM 27 49 Helical; Name=1. {ECO:0000255}.; TRANSMEM 62 87 Helical; Name=2. {ECO:0000255}.; TRANSMEM 102 121 Helical; Name=3. {ECO:0000255}.; TRANSMEM 141 164 Helical; Name=4. {ECO:0000255}.; TRANSMEM 189 212 Helical; Name=5. {ECO:0000255}.; TRANSMEM 241 264 Helical; Name=6. {ECO:0000255}.; TRANSMEM 273 297 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 26 Extracellular.; TOPO_DOM 50 61 Cytoplasmic.; TOPO_DOM 88 101 Extracellular.; TOPO_DOM 122 140 Cytoplasmic.; TOPO_DOM 165 188 Extracellular.; TOPO_DOM 213 240 Cytoplasmic.; TOPO_DOM 265 272 Extracellular.; TOPO_DOM 298 337 Cytoplasmic. FUNCTION: May play a role in rpe physiology either by detecting light directly or by monitoring the concentration of retinoids or other photoreceptor-derived compounds. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Found only in the eye, where it is localized to the retinal pigment epithelium (RPE). In the RPE, it is localized to the microvilli that surround the photoreceptor outer segments. +P17225 PTBP1_MOUSE Polypyrimidine tract-binding protein 1 (PTB) (Heterogeneous nuclear ribonucleoprotein I) (hnRNP I) 527 56,478 Chain (1); Compositional bias (1); Cross-link (2); Domain (4); Modified residue (6) FUNCTION: Plays a role in pre-mRNA splicing and in the regulation of alternative splicing events. Activates exon skipping of its own pre-mRNA during muscle cell differentiation. Binds to the polypyrimidine tract of introns. May promote RNA looping when bound to two separate polypyrimidine tracts in the same pre-mRNA. May promote the binding of U2 snRNP to pre-mRNA. Cooperates with RAVER1 to modulate switching between mutually exclusive exons during maturation of the TPM1 pre-mRNA. Represses the splicing of MAPT/Tau exon 10. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Monomer. Part of a ternary complex containing KHSRP, PTBP1, PTBP2 and HNRPH1. Interacts with SFPQ (By similarity). Interacts with RAVER1. {ECO:0000250, ECO:0000269|PubMed:11724819}. DOMAIN: The C-terminal 195 amino acids of PTB are sufficient for specific RNA binding. TISSUE SPECIFICITY: Expressed in myoblast; expression gradually decreases during muscle cell differentiation (at protein level). {ECO:0000269|PubMed:21518792}. +Q91Z31 PTBP2_MOUSE Polypyrimidine tract-binding protein 2 (Brain-enriched polypyrimidine tract-binding protein) (Brain-enriched PTB) (Neural polypyrimidine tract-binding protein) (RRM-type RNA-binding protein brPTB) 531 57,489 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (4); Modified residue (4); Sequence conflict (1) FUNCTION: RNA-binding protein which binds to intronic polypyrimidine tracts and mediates negative regulation of exons splicing. May antagonize in a tissue-specific manner the ability of NOVA1 to activate exon selection. In addition to its function in pre-mRNA splicing, plays also a role in the regulation of translation. {ECO:0000269|PubMed:10829067, ECO:0000269|PubMed:11726525}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10829067}. SUBUNIT: Monomer. Identified in a mRNP complex, at least composed of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1. Part of a ternary complex containing KHSRP and HNRPH1 (By similarity). Interacts with NOVA1; the interaction is direct. Interacts with NOVA2; the interaction is direct. {ECO:0000250, ECO:0000269|PubMed:10829067}. TISSUE SPECIFICITY: Mainly expressed in brain, including cerebellum, brainstem, spinal cord, and hypothalamus. Also expressed in the peripheral nervous system and neural crest derivatives, including the dorsal root and trigeminal ganglia, the cochlear spiral and intestinal ganglion cells, and the adrenal medulla. Also detected to a lower extent in testis, heart, liver, lung, skeletal muscle and thymus (at protein level). {ECO:0000269|PubMed:10829067, ECO:0000269|PubMed:11231079}. +Q8BHD7 PTBP3_MOUSE Polypyrimidine tract-binding protein 3 (Regulator of differentiation 1) (Rod1) 523 56,701 Alternative sequence (1); Chain (1); Cross-link (2); Domain (4); Modified residue (4) FUNCTION: RNA-binding protein that mediates pre-mRNA alternative splicing regulation. Plays a role in the regulation of cell proliferation, differentiation and migration. Positive regulator of EPO-dependent erythropoiesis. Participates in cell differentiation regulation by repressing tissue-specific exons. Promotes Fas exon 6 skipping. Binds RNA, preferentially to both poly(G) and poly(U) (By similarity). {ECO:0000250}. SUBUNIT: Interacts with THBS4 (via the acidic amphipathic C-terminus). {ECO:0000250}. +Q61115 PTC1_MOUSE Protein patched homolog 1 (PTC) (PTC1) 1434 159,273 Chain (1); Cross-link (1); Domain (1); Glycosylation (6); Modified residue (2); Mutagenesis (1); Topological domain (13); Transmembrane (12) TRANSMEM 87 107 Helical. {ECO:0000255}.; TRANSMEM 423 443 Helical. {ECO:0000255}.; TRANSMEM 459 479 Helical. {ECO:0000255}.; TRANSMEM 488 508 Helical. {ECO:0000255}.; TRANSMEM 534 554 Helical. {ECO:0000255}.; TRANSMEM 564 584 Helical. {ECO:0000255}.; TRANSMEM 735 755 Helical. {ECO:0000255}.; TRANSMEM 1014 1034 Helical. {ECO:0000255}.; TRANSMEM 1040 1060 Helical. {ECO:0000255}.; TRANSMEM 1070 1090 Helical. {ECO:0000255}.; TRANSMEM 1108 1128 Helical. {ECO:0000255}.; TRANSMEM 1141 1161 Helical. {ECO:0000255}. TOPO_DOM 1 86 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 108 422 Extracellular. {ECO:0000255}.; TOPO_DOM 444 458 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 480 487 Extracellular. {ECO:0000255}.; TOPO_DOM 509 533 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 555 563 Extracellular. {ECO:0000255}.; TOPO_DOM 585 734 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 756 1013 Extracellular. {ECO:0000255}.; TOPO_DOM 1035 1039 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1061 1069 Extracellular. {ECO:0000255}.; TOPO_DOM 1091 1107 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1129 1140 Extracellular. {ECO:0000255}.; TOPO_DOM 1162 1434 Cytoplasmic. {ECO:0000255}. FUNCTION: Acts as a receptor for sonic hedgehog (SHH), indian hedgehog (IHH) and desert hedgehog (DHH). Associates with the smoothened protein (SMO) to transduce the hedgehog's proteins signal. Seems to have a tumor suppressor function, as inactivation of this protein is probably a necessary, if not sufficient step for tumorigenesis. {ECO:0000269|PubMed:21537345}. PTM: Glycosylation is necessary for SHH binding. {ECO:0000250}.; PTM: In the absence of Hh ligands, ubiquitination by ITCH at Lys-1413 promotes endocytosis and both proteasomal and lysosomal degradation. {ECO:0000269|PubMed:25092867}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24062445}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Interacts with SNX17 (By similarity). Interacts with IHH (PubMed:21537345). Interacts with G-protein coupled receptor GPR37L1 (PubMed:24062445). {ECO:0000250|UniProtKB:Q13635, ECO:0000269|PubMed:21537345, ECO:0000269|PubMed:24062445}. TISSUE SPECIFICITY: Detected in cerebellar Bergmann glia cells (at protein level) (PubMed:24062445). In the developing embryo, first detected within the ventral neural tube and later in the somites and limb buds (PubMed:8595881). Expression in the limb buds is restricted to the posterior ectoderm surrounding the zone of polarizing activity (PubMed:8595881). In the adult, expression is seen in brain, lung, liver, kidney and ocular tissues; lower levels in heart, skeletal muscle, and testis (PubMed:8595881). {ECO:0000269|PubMed:24062445, ECO:0000269|PubMed:8595881}. +O35125 LRC23_MOUSE Leucine-rich repeat-containing protein 23 (Leucine-rich protein B7) 340 39,292 Chain (1); Coiled coil (1); Domain (1); Repeat (6) +Q8CIM1 LRC45_MOUSE Leucine-rich repeat-containing protein 45 670 76,384 Chain (1); Coiled coil (1); Modified residue (1); Repeat (6); Sequence conflict (1) FUNCTION: Component of the proteinaceous fiber-like linker between two centrioles, required for centrosome cohesion. {ECO:0000250|UniProtKB:Q96CN5}. PTM: Phosphorylated by NEK2 during misosis, phosphorylation reduces centrosomal localization which subsequently leads to centrosome separation. {ECO:0000250|UniProtKB:Q96CN5}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q96CN5}. Note=Localizes to the proteinaceous linker between the proximal ends of the centrioles. {ECO:0000250|UniProtKB:Q96CN5}. SUBUNIT: Interacts with CROCC/rootletin and CEP250. {ECO:0000250|UniProtKB:Q96CN5}. +Q8CDD9 LRIF1_MOUSE Ligand-dependent nuclear receptor-interacting factor 1 755 82,998 Alternative sequence (2); Chain (1); Coiled coil (1); Cross-link (4); Modified residue (5); Motif (3); Sequence conflict (1) FUNCTION: Together with SMCHD1, involved in chromosome X inactivation in females by promoting the compaction of heterochromatin. Also able to repress the ligand-induced transcriptional activity of retinoic acid receptor alpha (RARA), possibly through direct recruitment of histone deacetylases. {ECO:0000250|UniProtKB:Q5T3J3}. SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:26391951}. Nucleus matrix {ECO:0000250|UniProtKB:Q5T3J3}. Note=Localizes to Barr body; recruited by SMCHD1. {ECO:0000250|UniProtKB:Q5T3J3}. SUBUNIT: Interacts with RARA (By similarity). Interacts with SMCHD1; leading to recruitment to inactivated chromosome X in females (PubMed:26391951). Interacts (via PxVxL motif) with HP1 (CBX1/HP1-beta, CBX3/HP1-gamma and CBX5/HP1-alpha) (By similarity). {ECO:0000250|UniProtKB:Q5T3J3, ECO:0000269|PubMed:26391951}. DOMAIN: The Pro-Xaa-Val-Xaa-Leu (PxVxL) motif mediates interaction with HP1 (CBX1/HP1-beta, CBX3/HP1-gamma and CBX5/HP1-alpha). {ECO:0000250|UniProtKB:Q5T3J3}. +Q9DAK8 LRC51_MOUSE Leucine-rich repeat-containing protein 51 (Protein LRTOMT1) 192 22,008 Alternative sequence (1); Chain (1); Domain (1); Repeat (3) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18953341}. TISSUE SPECIFICITY: Widely expressed in adult and embryonic tissues. Expressed in the developing choroid plexus from E12.5 and in the epithelium of the developing airway tract from E14.5. Also expressed in the postnatal inner ear. {ECO:0000269|PubMed:18953341}. +Q0P5X1 LRIQ1_MOUSE Leucine-rich repeat and IQ domain-containing protein 1 1673 191,812 Alternative sequence (2); Chain (1); Domain (3); Frameshift (1); Repeat (16); Sequence conflict (2) +Q3TYX2 LRN4L_MOUSE LRRN4 C-terminal-like protein 239 25,931 Chain (1); Domain (1); Glycosylation (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 195 215 Helical. {ECO:0000255}. TOPO_DOM 20 194 Extracellular. {ECO:0000255}.; TOPO_DOM 216 239 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +A2VDH3 LRC38_MOUSE Leucine-rich repeat-containing protein 38 (BK channel auxiliary gamma subunit LRRC38) 298 32,343 Chain (1); Disulfide bond (4); Domain (2); Erroneous initiation (1); Glycosylation (1); Repeat (5); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 252 272 Helical. {ECO:0000255}. TOPO_DOM 32 251 Extracellular. {ECO:0000255}.; TOPO_DOM 273 298 Cytoplasmic. {ECO:0000255}. FUNCTION: Auxiliary protein of the large-conductance, voltage and calcium-activated potassium channel (BK alpha). Modulates gating properties by producing a marked shift in the BK channel's voltage dependence of activation in the hyperpolarizing direction, and in the absence of calcium (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Interacts with KCNMA1. {ECO:0000250}. DOMAIN: The transmembrane domain is necessary for interaction with KCNMA1. {ECO:0000250}. +Q80XG9 LRRT4_MOUSE Leucine-rich repeat transmembrane neuronal protein 4 590 67,148 Alternative sequence (2); Chain (1); Domain (2); Erroneous initiation (1); Glycosylation (3); Repeat (10); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 425 445 Helical. {ECO:0000255}. TOPO_DOM 31 424 Extracellular. {ECO:0000255}.; TOPO_DOM 446 590 Cytoplasmic. {ECO:0000255}. FUNCTION: May play a role in the development and maintenance of the vertebrate nervous system. Exhibits strong synaptogenic activity, restricted to excitatory presynaptic differentiation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Peripherally associated with AMPAR complex. AMPAR complex consists of an inner core made of 4 pore-forming GluA/GRIA proteins (GRIA1, GRIA2, GRIA3 and GRIA4) and 4 major auxiliary subunits arranged in a twofold symmetry. One of the two pairs of distinct binding sites is occupied either by CNIH2, CNIH3 or CACNG2, CACNG3. The other harbors CACNG2, CACNG3, CACNG4, CACNG8 or GSG1L. This inner core of AMPAR complex is complemented by outer core constituents binding directly to the GluA/GRIA proteins at sites distinct from the interaction sites of the inner core constituents. Outer core constituents include at least PRRT1, PRRT2, CKAMP44/SHISA9, FRRS1L and NRN1. The proteins of the inner and outer core serve as a platform for other, more peripherally associated AMPAR constituents, including LRRTM4. Alone or in combination, these auxiliary subunits control the gating and pharmacology of the AMPAR complex and profoundly impact their biogenesis and protein processing. {ECO:0000269|PubMed:22632720}. TISSUE SPECIFICITY: Predominantly in the brain (at protein level). Also expressed in the cerebellum and other tissues. {ECO:0000269|PubMed:12676565, ECO:0000269|PubMed:22632720}. +Q99KG5 LSR_MOUSE Lipolysis-stimulated lipoprotein receptor (Lipolysis-stimulated receptor) (Liver-specific bHLH-Zip transcription factor) (Liver-specific gene on mouse chromosome 7 protein) 594 66,108 Alternative sequence (2); Chain (1); Compositional bias (1); Disulfide bond (1); Domain (1); Frameshift (1); Modified residue (16); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 207 227 Helical. {ECO:0000255}. TOPO_DOM 36 206 Extracellular. {ECO:0000255}.; TOPO_DOM 228 594 Cytoplasmic. {ECO:0000255}. FUNCTION: Probable role in the clearance of triglyceride-rich lipoprotein from blood. Binds chylomicrons, LDL and VLDL in presence of free fatty acids and allows their subsequent uptake in the cells (By similarity). {ECO:0000250, ECO:0000269|PubMed:15265030}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Homotrimer or homotetramer. {ECO:0000250}. TISSUE SPECIFICITY: Specifically expressed in liver and to a lower extent in kidney (at protein level). Also detected in brain, testis, ovaries, adrenal gland, intestine, muscle, and lung. {ECO:0000269|PubMed:15265030}. +Q8K4G1 LTBP4_MOUSE Latent-transforming growth factor beta-binding protein 4 (LTBP-4) 1666 178,642 Alternative sequence (3); Chain (1); Compositional bias (4); Disulfide bond (65); Domain (20); Glycosylation (5); Modified residue (1); Sequence conflict (4); Signal peptide (1) FUNCTION: Key regulator of transforming growth factor beta (TGFB1, TGFB2 and TGFB3) that controls TGF-beta activation by maintaining it in a latent state during storage in extracellular space. Associates specifically via disulfide bonds with the Latency-associated peptide (LAP), which is the regulatory chain of TGF-beta, and regulates integrin-dependent activation of TGF-beta. {ECO:0000250|UniProtKB:Q14766}. PTM: Contains hydroxylated asparagine residues. {ECO:0000250|UniProtKB:Q14766}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q8N2S1}. SUBUNIT: Forms part of the large latent transforming growth factor beta precursor complex; removal is essential for activation of complex. Interacts with LTBP1 and TGFB1. {ECO:0000250|UniProtKB:Q8N2S1}. +Q8K2P1 LUR1L_MOUSE Leucine rich adaptor protein 1-like 221 23,728 Chain (1); Compositional bias (1); Frameshift (1); Modified residue (1); Sequence conflict (2) +Q8VIK2 M17L2_MOUSE Mpv17-like protein 2 200 22,514 Chain (1); Sequence conflict (2); Transmembrane (3) TRANSMEM 24 40 Helical. {ECO:0000255}.; TRANSMEM 63 83 Helical. {ECO:0000255}.; TRANSMEM 102 122 Helical. {ECO:0000255}. FUNCTION: Required for the assembly and stability of the mitochondrial ribosome (By similarity). Is a positive regulator of mitochondrial protein synthesis (By similarity). {ECO:0000250|UniProtKB:Q567V2}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q567V2}. SUBUNIT: Interacts with the large mitochondrial ribosomal subunit. {ECO:0000250|UniProtKB:Q567V2}. +Q80WQ8 M18BP_MOUSE Mis18-binding protein 1 (Kinetochore-associated protein KNL-2 homolog) 998 113,956 Alternative sequence (3); Chain (1); Cross-link (7); Domain (2); Modified residue (14); Sequence conflict (2) FUNCTION: Required for recruitment of CENPA to centromeres and normal chromosome segregation during mitosis. {ECO:0000250|UniProtKB:Q6P0N0}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, centromere {ECO:0000250}. Note=Associated with centromeres in interphase cells, from late anaphase to the G1 phase. Not detected on centromeres during earlier phases of mitosis. Associated with chromatin (By similarity). {ECO:0000250}. SUBUNIT: Interacts with SP1 (Probable). Interacts with MIS18A. Identified in a complex containing MIS18A, OIP5/MIS18B, MIS18BP1, RBBP7 and RBBP4 (By similarity). Interacts (via N-terminus) with FLNA (via N-terminus). {ECO:0000250|UniProtKB:Q6P0N0, ECO:0000269|PubMed:21228480, ECO:0000305}. +Q9D925 LYZL4_MOUSE Lysozyme-like protein 4 (Lysozyme-4) 145 16,198 Active site (1); Chain (1); Disulfide bond (4); Erroneous initiation (1); Signal peptide (1) FUNCTION: May be involved in fertilization (PubMed:21444326). Has no detectable bacteriolytic in vitro (PubMed:21444326). Has no lysozyme activity in vitro (By similarity). {ECO:0000250|UniProtKB:D4ABW7, ECO:0000269|PubMed:21444326}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21444326}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:21444326}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:21444326}. Note=Found in the principal piece of sperm tail (PubMed:21444326). {ECO:0000269|PubMed:21444326}. SUBUNIT: Monomer. {ECO:0000305}. TISSUE SPECIFICITY: Expressed strongly in testis and in epididymis, and weakly in brain and lung (PubMed:21444326, PubMed:24013621). Detected in sperm (at protein level) (PubMed:21444326). {ECO:0000269|PubMed:21444326, ECO:0000269|PubMed:24013621}. +Q60935 NAR1_MOUSE GPI-linked NAD(P)(+)--arginine ADP-ribosyltransferase 1 (EC 2.4.2.31) (ADP-ribosyltransferase C2 and C3 toxin-like 1) (ARTC1) (Mono(ADP-ribosyl)transferase 1) (YAC-1) (CD antigen CD296) 325 35,898 Active site (1); Binding site (3); Chain (1); Disulfide bond (2); Glycosylation (2); Lipidation (1); Propeptide (1); Sequence conflict (3); Signal peptide (1) FUNCTION: Has ADP-ribosyltransferase activity toward GLP1R. {ECO:0000250}. SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane; Lipid-anchor, GPI-anchor. TISSUE SPECIFICITY: Abundantly expressed in cardiac and skeletal muscle. Low levels also found in lung. +Q80U28 MADD_MOUSE MAP kinase-activating death domain protein (Rab3 GDP/GTP exchange factor) 1577 175,180 Alternative sequence (17); Chain (1); Compositional bias (1); Domain (4); Erroneous initiation (1); Modified residue (18); Sequence conflict (20) FUNCTION: Plays a significant role in regulating cell proliferation, survival and death through alternative mRNA splicing. Converts GDP-bound inactive form of RAB3A, RAB3C and RAB3D to the GTP-bound active forms. Component of the TNFRSF1A signaling complex: MADD links TNFRSF1A with MAP kinase activation. Plays an important regulatory role in physiological cell death (TNF-alpha-induced, caspase-mediated apoptosis). {ECO:0000269|PubMed:14735464, ECO:0000269|PubMed:15007167}. SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q8WXG6}. Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with the death domain of TNFRSF1A through its own death domain. Interacts with PIDD1 (By similarity). {ECO:0000250}. +Q08AU7 MADL2_MOUSE Myeloid-associated differentiation marker-like protein 2 307 33,165 Alternative sequence (2); Chain (1); Domain (2); Erroneous initiation (3); Sequence conflict (1); Transmembrane (7) TRANSMEM 53 73 Helical. {ECO:0000255}.; TRANSMEM 90 110 Helical. {ECO:0000255}.; TRANSMEM 129 149 Helical. {ECO:0000255}.; TRANSMEM 163 183 Helical. {ECO:0000255}.; TRANSMEM 198 218 Helical. {ECO:0000255}.; TRANSMEM 232 252 Helical. {ECO:0000255}.; TRANSMEM 278 298 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q61083 M3K2_MOUSE Mitogen-activated protein kinase kinase kinase 2 (EC 2.7.11.25) (MAPK/ERK kinase kinase 2) (MEK kinase 2) (MEKK 2) 619 69,574 Active site (1); Binding site (1); Chain (1); Domain (2); Frameshift (1); Modified residue (9); Mutagenesis (9); Nucleotide binding (1) FUNCTION: Component of a protein kinase signal transduction cascade. Regulates the JNK and ERK5 pathways by phosphorylating and activating MAP2K5 and MAP2K7. Plays a role in caveolae kiss-and-run dynamics (By similarity). {ECO:0000250, ECO:0000269|PubMed:12659851}. PTM: Ubiquitination by XIAP/BIRC4 does not lead to proteasomal degradation. {ECO:0000250}.; PTM: Autophosphorylated. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Upon EGF stimulation, translocates into the nucleus. SUBUNIT: Self-associates (By similarity). Binds both upstream activators and downstream substrates in multimolecular complexes. Interacts (via the kinase catalytic domain) with STK38 (By similarity). Interacts with XIAP/BIRC4 (By similarity). {ECO:0000250}. +Q9DBV4 MXRA8_MOUSE Matrix remodeling-associated protein 8 (Adipocyte-specific protein 3) (Dual Ig domain-containing cell adhesion molecule) (DICAM) (Limitrin) 442 49,750 Chain (1); Disulfide bond (2); Domain (2); Glycosylation (2); Modified residue (1); Motif (2); Mutagenesis (2); Sequence conflict (11); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 341 361 Helical. {ECO:0000255}. TOPO_DOM 20 340 Extracellular. {ECO:0000255}.; TOPO_DOM 362 442 Cytoplasmic. {ECO:0000255}. FUNCTION: Transmembrane protein which can modulate activity of various signaling pathways, probably via binding to integrin ITGAV:ITGB3 (PubMed:18366072, PubMed:22492581, PubMed:29702220). Mediates heterophilic cell-cell interactions in vitro (PubMed:18366072). Inhibits osteoclastogenesis downstream of TNFSF11/RANKL and CSF1, where it may function by attenuating signaling via integrin ITGB3 and MAP kinase p38 (PubMed:22492581). Plays a role in cartilage formation where it promotes proliferation and maturation of growth plate chondrocytes (PubMed:29702220). Stimulates formation of primary cilia in chondrocytes (PubMed:29702220). Enhances expression of genes involved in the hedgehog signaling pathway in chondrocytes, including the hedgehog signaling molecule IHH; may also promote signaling via the PTHLH/PTHrP pathway (PubMed:29702220). Plays a role in angiogenesis where it suppresses migration of endothelial cells and also promotes their apoptosis (By similarity). Inhibits VEGF-induced activation of AKT and p38 MAP kinase in endothelial cells (By similarity). Also inhibits VTN (vitronectin)-mediated integrin ITGAV:ITGB3 signaling and activation of PTK2/FAK (By similarity). May play a role in the maturation and maintenance of the blood-brain barrier (PubMed:14603461). {ECO:0000250|UniProtKB:Q9BRK3, ECO:0000269|PubMed:14603461, ECO:0000269|PubMed:18366072, ECO:0000269|PubMed:22492581, ECO:0000269|PubMed:29702220}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14603461, ECO:0000269|PubMed:18366072, ECO:0000269|PubMed:22492581}; Single-pass type I membrane protein {ECO:0000255}. Cell junction, tight junction {ECO:0000269|PubMed:18366072}. Cytoplasm {ECO:0000269|PubMed:18366072, ECO:0000269|PubMed:29702220}. Cell projection, cilium membrane {ECO:0000269|PubMed:29702220}. Nucleus {ECO:0000269|PubMed:18366072}. Note=Primarily localizes to the cell membrane (PubMed:18366072). Detected in the cilium of primary chondrocytes (PubMed:29702220). Highly expressed at areas of cell-cell contact and may localize to tight junctions (PubMed:18366072). Also found in the nucleus where it is detected in the soluble (as opposed to chromatin-bound) fraction (PubMed:18366072). {ECO:0000269|PubMed:18366072, ECO:0000269|PubMed:29702220}. SUBUNIT: Homodimer in cis (PubMed:18366072). Does not appear to form trans-homodimers (PubMed:18366072). Interacts with ITGB3; the interaction inhibits ITGAV:ITGB3 heterodimer formation (PubMed:22492581). {ECO:0000269|PubMed:18366072, ECO:0000269|PubMed:22492581}. DOMAIN: RGD motif 2 (but not RGD motif 1) is involved in integrin ITGAV:ITGB3 binding. {ECO:0000269|PubMed:18366072}. TISSUE SPECIFICITY: Widely expressed (at protein level) (PubMed:18366072). Highly expressed in brain where it localizes to the glia limitans, which is formed by the endfeet of astrocytes surrounding capillaries, and beneath the pia mater (at protein level) (PubMed:14603461). In lung, detected in epithelial cells of the bronchus (at protein level). Expressed in intercalated disks in the heart (at protein level) (PubMed:18366072). Detected in pancreatic alpha-cells in the islet of Langerhans (at protein level) (PubMed:18366072). In kidney, found in the brush border of the proximal convoluted tubule (at protein level) (PubMed:18366072). Expressed in the epithelium of the small intestine (at protein level) (PubMed:18366072). Weakly expressed in liver (at protein level) (PubMed:18366072). Detected in myeloid cells (PubMed:22492581). {ECO:0000269|PubMed:14603461, ECO:0000269|PubMed:18366072, ECO:0000269|PubMed:22492581}. +P24526 MYP2_MOUSE Myelin P2 protein 132 14,935 Binding site (1); Chain (1); Initiator methionine (1); Modified residue (1); Region (1) FUNCTION: May play a role in lipid transport protein in Schwann cells. May bind cholesterol (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. DOMAIN: Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior. {ECO:0000250}. +Q9JK81 MYG1_MOUSE UPF0160 protein MYG1, mitochondrial (Protein Gamm1) 380 42,723 Chain (1); Modified residue (2); Transit peptide (1) SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19014353}. Mitochondrion {ECO:0000269|PubMed:19014353}. TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in testis. {ECO:0000269|PubMed:19014353}. +Q8C7U1 N4BP3_MOUSE NEDD4-binding protein 3 (N4BP3) 537 60,042 Chain (1); Coiled coil (1); Compositional bias (1); Modified residue (1); Sequence conflict (6) FUNCTION: Plays a role in axon and dendrite arborization during cranial nerve development. May also be important for neural crest migration and early development of other anterior structures including eye, brain and cranial cartilage. {ECO:0000250|UniProtKB:A0A1L8GXY6}. SUBCELLULAR LOCATION: Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q3LUD3}. Cell projection, axon {ECO:0000250|UniProtKB:Q3LUD3}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q3LUD3}. Note=In developing neurons, accumulates in early growth cones and at branching points of axons and dendrites. {ECO:0000250|UniProtKB:Q3LUD3}. SUBUNIT: Binds NEDD4. Interacts with 14-3-3 proteins. {ECO:0000250|UniProtKB:O15049}. +Q6SKR2 N6MT1_MOUSE Methyltransferase N6AMT1 (HemK methyltransferase family member 2) (Methylarsonite methyltransferase N6AMT1) (EC 2.1.1.-) (N(6)-adenine-specific DNA methyltransferase 1) (EC 2.1.1.72) (Protein N(5)-glutamine methyltransferase) (EC 2.1.1.-) 214 22,984 Alternative sequence (4); Binding site (2); Chain (1); Erroneous gene model prediction (2); Region (2); Sequence conflict (1) FUNCTION: Methyltransferase that can methylate both proteins and DNA, and to a lower extent, arsenic (PubMed:20606008, PubMed:26797129). Catalytic subunit of a heterodimer with TRMT112, which catalyzes N5-methylation of Glu residue of proteins with a Gly-Gln-Xaa-Xaa-Xaa-Arg motif (PubMed:26797129). Methylates ETF1 on 'Gln-185'; ETF1 needs to be complexed to ERF3 in its GTP-bound form to be efficiently methylated (PubMed:20606008, PubMed:26797129). Also acts as a N(6)-adenine-specific DNA methyltransferase by mediating methylation of DNA on the 6th position of adenine (N(6)-methyladenosine) (By similarity). N(6)-methyladenosine (m6A) DNA is significantly enriched in exonic regions and is associated with gene transcriptional activation (By similarity). May also play a role in the modulation of arsenic-induced toxicity by mediating the conversion of monomethylarsonous acid (3+) into the less toxic dimethylarsonic acid (By similarity). It however only plays a limited role in arsenic metabolism compared with AS3MT (By similarity). {ECO:0000250|UniProtKB:Q9Y5N5, ECO:0000269|PubMed:20606008, ECO:0000269|PubMed:26797129}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16684535, ECO:0000269|PubMed:19116772}. SUBUNIT: Heterodimer; heterodimerizes with TRMT112. {ECO:0000269|PubMed:26797129}. TISSUE SPECIFICITY: Highly expressed in undifferentiated embryonic stem cells (at protein level) (PubMed:19116772). Also expressed in testis and brain, weakly expressed in differentiated embryonic stem cells and kidney (PubMed:19116772). Not expressed in muscle, heart, placenta, pancreas, lung and stomach (PubMed:19116772). {ECO:0000269|PubMed:19116772}. +Q9JK37 MYOZ1_MOUSE Myozenin-1 (Calsarcin-2) (Filamin-, actinin- and telethonin-binding protein) (Protein FATZ) 296 31,457 Chain (1); Compositional bias (1); Modified residue (1); Sequence conflict (2) FUNCTION: Myozenins may serve as intracellular binding proteins involved in linking Z-disk proteins such as alpha-actinin, gamma-filamin, TCAP/telethonin, LDB3/ZASP and localizing calcineurin signaling to the sarcomere. Plays an important role in the modulation of calcineurin signaling. May play a role in myofibrillogenesis. {ECO:0000303|PubMed:10984498, ECO:0000303|PubMed:11114196, ECO:0000305}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cell projection, pseudopodium {ECO:0000250}. Note=Localized to the nucleus and pseudopodia of undifferentiated cells and detected throughout the myotubes of differentiated cells. Colocalizes with ACTN2, FLNC and MYOT at the Z-lines of skeletal muscle (By similarity). {ECO:0000250}. SUBUNIT: Interacts with ACTN2, ACTN3, FLNA, FLNB, FLNC, LDB3, PPP3CA and TCAP. Interacts via its C-terminal region with MYOT. {ECO:0000250|UniProtKB:Q9NP98, ECO:0000269|PubMed:11114196}. TISSUE SPECIFICITY: Expressed primarily in skeletal muscle and specifically enriched in the gastrocnemius, which is composed predominantly of fast-twitch muscle fibers. Detected at lower levels in heart. {ECO:0000269|PubMed:10984498, ECO:0000269|PubMed:11114196}. +Q8VE10 NAA40_MOUSE N-alpha-acetyltransferase 40 (EC 2.3.1.257) (N-acetyltransferase 11) (N-alpha-acetyltransferase D) (NatD) (Protein acetyltransferase 1) 237 27,229 Alternative sequence (3); Binding site (6); Chain (1); Domain (1); Frameshift (1); Initiator methionine (1); Lipidation (1); Region (3); Site (1) FUNCTION: N-alpha-acetyltransferase that specifically mediates the acetylation of the N-terminal residues of histones H4 and H2A (By similarity). In contrast to other N-alpha-acetyltransferase, has a very specific selectivity for histones H4 and H2A N-terminus and specifically recognizes the 'Ser-Gly-Arg-Gly sequence' (By similarity). Acts as a negative regulator of apoptosis (By similarity). May play a role in hepatic lipid metabolism (PubMed:22231784). {ECO:0000250|UniProtKB:Q86UY6, ECO:0000269|PubMed:22231784}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q86UY6}. Nucleus {ECO:0000250|UniProtKB:Q86UY6}. +Q3UX61 NAA11_MOUSE N-alpha-acetyltransferase 11 (EC 2.3.1.255) (N-terminal acetyltransferase complex ARD1 subunit homolog B) (NatA catalytic subunit Naa11) 218 24,671 Chain (1); Domain (1); Region (1); Sequence conflict (1) FUNCTION: Displays alpha (N-terminal) acetyltransferase activity. Proposed alternative catalytic subunit of the N-terminal acetyltransferase A (NatA) complex. {ECO:0000250|UniProtKB:Q9BSU3}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BSU3}. Nucleus {ECO:0000250|UniProtKB:Q9BSU3}. SUBUNIT: Component of the N-terminal acetyltransferase A (NatA) complex composed of NAA11 and NAA15. Interacts with HIF1A. {ECO:0000250|UniProtKB:Q9BSU3}. +Q80UM3 NAA15_MOUSE N-alpha-acetyltransferase 15, NatA auxiliary subunit (N-terminal acetyltransferase 1) (NMDA receptor-regulated protein 1) (Protein tubedown-1) 865 100,961 Chain (1); Compositional bias (1); Frameshift (1); Modified residue (8); Motif (1); Region (1); Repeat (9); Sequence caution (1); Sequence conflict (11) FUNCTION: Auxillary subunit of the N-terminal acetyltransferase A (NatA) complex which displays alpha (N-terminal) acetyltransferase activity. The NAT activity may be important for vascular, hematopoietic and neuronal growth and development. Required to control retinal neovascularization in adult ocular endothelial cells. In complex with XRCC6 and XRCC5 (Ku80), up-regulates transcription from the osteocalcin promoter. {ECO:0000269|PubMed:10842358, ECO:0000269|PubMed:12145306, ECO:0000269|PubMed:12888564, ECO:0000269|PubMed:15452080}. PTM: Acetylated. {ECO:0000269|PubMed:10842358}.; PTM: Cleaved by caspases during apoptosis. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Mainly cytoplasmic, nuclear in some cases. Present in the free cytosolic and cytoskeleton-bound polysomes, but not in the membrane-bound polysomes. {ECO:0000250}. SUBUNIT: Component of the N-terminal acetyltransferase A (NatA) complex composed of NAA10 or probably NAA11 and NAA15. Interacts with XRCC6, NAA50 and XRCC5. Associates with HYPK when in a complex with NAA10. {ECO:0000269|PubMed:12145306, ECO:0000269|PubMed:12888564}. TISSUE SPECIFICITY: Endothelial cells, osteoblasts and myeloid cells of the hematopoietic tissue. Present in adult ovary, bone marrow, brain, heart, kidney, testis and osteoblasts. {ECO:0000269|PubMed:11297529, ECO:0000269|PubMed:12145306, ECO:0000269|PubMed:12888564}. +Q8R4U1 MYPOP_MOUSE Myb-related transcription factor, partner of profilin (Myb-related protein p42POP) (Partner of profilin) 393 41,890 Alternative sequence (2); Chain (1); Compositional bias (2); Domain (1); Motif (3); Mutagenesis (4) FUNCTION: Transcriptional repressor; DNA-binding protein that specifically recognizes the core sequence 5'-YAAC[GT]G-3'. Dimerization with PFN1 reduces its DNA-binding capacity. {ECO:0000269|PubMed:15615774}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15615774}. SUBUNIT: Interacts with PFN1. Homodimer and heterodimer with PFN1. {ECO:0000269|PubMed:15615774}. DOMAIN: The proline-rich region is required for PFN1 interaction. TISSUE SPECIFICITY: Ubiquitous. Highly expressed in brain, liver and testis. Moderate expression in heart, lung and skeletal muscle. Low expression in spleen and kidney. {ECO:0000269|PubMed:15615774}. +P60202 MYPR_MOUSE Myelin proteolipid protein (PLP) (Lipophilin) 277 30,077 Alternative sequence (1); Chain (1); Disulfide bond (2); Initiator methionine (1); Lipidation (7); Modified residue (3); Natural variant (2); Sequence conflict (3); Topological domain (5); Transmembrane (4) TRANSMEM 10 36 Helical; Name=1. {ECO:0000305}.; TRANSMEM 64 88 Helical; Name=2. {ECO:0000305}.; TRANSMEM 152 177 Helical; Name=3. {ECO:0000305}.; TRANSMEM 234 260 Helical; Name=4. {ECO:0000305}. TOPO_DOM 2 9 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 37 63 Extracellular. {ECO:0000305}.; TOPO_DOM 89 151 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 178 233 Extracellular. {ECO:0000305}.; TOPO_DOM 261 277 Cytoplasmic. {ECO:0000305}. FUNCTION: This is the major myelin protein from the central nervous system. It plays an important role in the formation or maintenance of the multilamellar structure of myelin. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17634366}; Multi-pass membrane protein {ECO:0000269|PubMed:17634366}. Myelin membrane {ECO:0000269|PubMed:17634366}. Note=Colocalizes with SIRT2 in internodal regions, at paranodal axoglial junction and Schmidt-Lanterman incisures of myelin sheat. DISEASE: Note=Defects in Plp1 are the cause of the dysmyelinating diseases Jimpy and Rumpshaker (rsh). +Q9R0A0 PEX14_MOUSE Peroxisomal membrane protein PEX14 (PTS1 receptor-docking protein) (Peroxin-14) (Peroxisomal membrane anchor protein PEX14) 376 41,208 Chain (1); Initiator methionine (1); Modified residue (5) FUNCTION: Peroxisome membrane protein that is an essential component of the peroxisomal import machinery. Functions as a docking factor for the predominantly cytoplasmic PTS1 receptor (PEX5). Plays a key role for peroxisome movement through a direct interaction with tubulin. {ECO:0000250|UniProtKB:O75381}. SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000250|UniProtKB:O75381}; Peripheral membrane protein {ECO:0000250|UniProtKB:O75381}; Cytoplasmic side {ECO:0000250|UniProtKB:O75381}. SUBUNIT: Interacts with PEX5, PEX13 and PEX19. Interacts with tubulin. {ECO:0000250|UniProtKB:O75381}. +Q8VCI5 PEX19_MOUSE Peroxisomal biogenesis factor 19 (Peroxin-19) (Peroxisomal farnesylated protein) (PxF) 299 32,733 Alternative sequence (1); Chain (1); Initiator methionine (1); Lipidation (1); Modified residue (5); Propeptide (1); Region (2); Sequence conflict (5) FUNCTION: Necessary for early peroxisomal biogenesis. Acts both as a cytosolic chaperone and as an import receptor for peroxisomal membrane proteins (PMPs). Binds and stabilizes newly synthesized PMPs in the cytoplasm by interacting with their hydrophobic membrane-spanning domains, and targets them to the peroxisome membrane by binding to the integral membrane protein PEX3. Excludes CDKN2A from the nucleus and prevents its interaction with MDM2, which results in active degradation of TP53. {ECO:0000250|UniProtKB:P40855}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P40855}. Peroxisome membrane {ECO:0000250|UniProtKB:P40855}; Lipid-anchor {ECO:0000250|UniProtKB:P40855}; Cytoplasmic side {ECO:0000250|UniProtKB:P40855}. Note=Mainly cytoplasmic, some fraction membrane-associated to the outer surface of peroxisomes. {ECO:0000250|UniProtKB:P40855}. SUBUNIT: Interacts with a broad range of peroxisomal membrane proteins, including PEX3, PEX10, PEX11A, PEX11B, PEX12, PEX13, PEX14 and PEX16, PXMP2/PMP22, PXMP4/PMP24, SLC25A17/PMP34, ABCD1/ALDP, ABCD2/ALDRP, and ABCD3/PMP70. Also interacts with the tumor suppressor CDKN2A/p19ARF (By similarity). {ECO:0000250}. +Q91X91 NADC_MOUSE Nicotinate-nucleotide pyrophosphorylase [carboxylating] (EC 2.4.2.19) (Quinolinate phosphoribosyltransferase [decarboxylating]) (QAPRTase) (QPRTase) 299 31,530 Binding site (5); Chain (1); Modified residue (1); Region (3) Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-ribonucleotide from quinolinate: step 1/1. FUNCTION: Involved in the catabolism of quinolinic acid (QA). {ECO:0000250}. SUBUNIT: Hexamer formed by 3 homodimers. {ECO:0000250}. +Q9CZA6 NDE1_MOUSE Nuclear distribution protein nudE homolog 1 (NudE) (mNudE) 344 38,523 Alternative sequence (4); Chain (1); Coiled coil (1); Lipidation (1); Modified residue (8); Region (3) FUNCTION: Required for centrosome duplication and formation and function of the mitotic spindle. Essential for the development of the cerebral cortex. May regulate the production of neurons by controlling the orientation of the mitotic spindle during division of cortical neuronal progenitors of the proliferative ventricular zone of the brain. Orientation of the division plane perpendicular to the layers of the cortex gives rise to two proliferative neuronal progenitors whereas parallel orientation of the division plane yields one proliferative neuronal progenitor and a post-mitotic neuron. A premature shift towards a neuronal fate within the progenitor population may result in an overall reduction in the final number of neurons and an increase in the number of neurons in the deeper layers of the cortex. {ECO:0000269|PubMed:15473967}. PTM: Phosphorylated in mitosis (By similarity). Phosphorylation at Thr-246 is essential for the G2/M transition. {ECO:0000250, ECO:0000269|PubMed:21529751}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle. Chromosome, centromere, kinetochore. Cleavage furrow. Note=Localizes to the interphase and S phase centrosome. During mitosis, partially associated with the mitotic spindle. Concentrates at the plus ends of microtubules coincident with kinetochores in metaphase and anaphase in a CENPF-dependent manner. Also localizes to the cleavage furrow during cytokinesis. SUBUNIT: Interacts with dynactin and PCM1 (By similarity). Self-associates. Interacts with CENPF, LIS1, CNTRL, dynein, tubulin gamma, PAFAH1B1, PCNT, SLMAP and TCP1. Interacts with ZNF365 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in ovary. Also expressed in brain, heart, kidney, large intestine, liver, lung, small intestine and testis. {ECO:0000269|PubMed:11163258, ECO:0000269|PubMed:11163259}. +P52503 NDUS6_MOUSE NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial (Complex I-13kD-A) (CI-13kD-A) (NADH-ubiquinone oxidoreductase 13 kDa-A subunit) 116 13,020 Beta strand (7); Chain (1); Helix (2); Modified residue (2); Sequence conflict (4); Transit peptide (1); Turn (1) FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. {ECO:0000250|UniProtKB:O75380}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305|PubMed:22474353}; Peripheral membrane protein {ECO:0000305}; Matrix side {ECO:0000305}. SUBUNIT: Mammalian complex I is composed of 45 different subunits. This is a component of the iron-sulfur (IP) fragment of the enzyme. {ECO:0000269|PubMed:22474353}. +Q6R891 NEB2_MOUSE Neurabin-2 (Neurabin-II) (Protein phosphatase 1 regulatory subunit 9B) (Spinophilin) 817 89,520 Alternative sequence (2); Chain (1); Coiled coil (2); Compositional bias (1); Domain (1); Modified residue (11); Motif (1); Mutagenesis (1); Region (7) FUNCTION: Seems to act as a scaffold protein in multiple signaling pathways. Modulates excitatory synaptic transmission and dendritic spine morphology. Binds to actin filaments (F-actin) and shows cross-linking activity. Binds along the sides of the F-actin. May play an important role in linking the actin cytoskeleton to the plasma membrane at the synaptic junction. Believed to target protein phosphatase 1/PP1 to dendritic spines, which are rich in F-actin, and regulates its specificity toward ion channels and other substrates, such as AMPA-type and NMDA-type glutamate receptors. Plays a role in regulation of G-protein coupled receptor signaling, including dopamine D2 receptors and alpha-adrenergic receptors. May establish a signaling complex for dopaminergic neurotransmission through D2 receptors by linking receptors downstream signaling molecules and the actin cytoskeleton. Binds to ADRA1B and RGS2 and mediates regulation of ADRA1B signaling. May confer to Rac signaling specificity by binding to both, RacGEFs and Rac effector proteins. Probably regulates p70 S6 kinase activity by forming a complex with TIAM1. Required for hepatocyte growth factor (HGF)-induced cell migration (By similarity). {ECO:0000250}. PTM: Stimulation of D1 (but not D2) dopamine receptors induces Ser-94 phosphorylation. Dephosphorylation of Ser-94 is mediated mainly by PP1 and to a lesser extent by PP2A. Phosphorylation of spinophilin disrupts its association with F-actin, but does not affect its binding to PP1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Nucleus {ECO:0000250}. Cell projection, dendritic spine {ECO:0000250}. Cell junction, synapse. Cell junction, adherens junction {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Cell projection, filopodium {ECO:0000250}. Cell projection, ruffle membrane {ECO:0000250}. Note=Enriched at synapse and cadherin-based cell-cell adhesion sites. In neurons, both cytosolic and membrane-associated, and highly enriched in the postsynaptic density apposed to exitatory synapses. Colocalizes with PPP1R2 at actin-rich adherens junctions in epithelial cells and in dendritic spines. Accumulates in the lamellipodium, filopodium and ruffle membrane in response to hepatocyte growth factor (HGF) treatment (By similarity). {ECO:0000250}. SUBUNIT: Possibly exists as a homodimer, homotrimer or a homotetramer. Interacts with F-actin, PPP1CA, neurabin-1, TGN38 and D(2) dopamine receptor. Interacts with RGS1, RGS2, RGS4, RGS19 and ADRA1B, ADRA2A, ADRA2B, ADRA2C, CDKN2A, PPP1R2, RASGFR1 and TIAM1. Interacts (via C-terminus) with SPATA13 (via C-terminal tail) (By similarity). Interacts with DCLK2. Interacts with ADRA2B (By similarity). {ECO:0000250|UniProtKB:O35274, ECO:0000250|UniProtKB:Q96SB3, ECO:0000269|PubMed:16628014}. DOMAIN: The PP1 binding region is natively unstructured, upon PP1 binding, it acquires structure, blocks a substrate-binding site, and restricts PP1 phosphatase specificity to a subset of substrates. {ECO:0000250}. +Q9QXZ9 OPN4_MOUSE Melanopsin (Opsin-4) 521 57,231 Alternative sequence (1); Chain (1); Disulfide bond (1); Glycosylation (2); Modified residue (1); Topological domain (8); Transmembrane (7) TRANSMEM 72 92 Helical; Name=1. {ECO:0000255}.; TRANSMEM 107 127 Helical; Name=2. {ECO:0000255}.; TRANSMEM 144 164 Helical; Name=3. {ECO:0000255}.; TRANSMEM 188 208 Helical; Name=4. {ECO:0000255}.; TRANSMEM 238 258 Helical; Name=5. {ECO:0000255}.; TRANSMEM 294 314 Helical; Name=6. {ECO:0000255}.; TRANSMEM 330 350 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 71 Extracellular. {ECO:0000255}.; TOPO_DOM 93 106 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 128 143 Extracellular. {ECO:0000255}.; TOPO_DOM 165 187 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 209 237 Extracellular. {ECO:0000255}.; TOPO_DOM 259 293 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 315 329 Extracellular. {ECO:0000255}.; TOPO_DOM 351 521 Cytoplasmic. {ECO:0000255}. FUNCTION: Photoreceptor required for regulation of circadian rhythm. Contributes to pupillar reflex and other non-image forming responses to light. May be able to isomerize covalently bound all-trans retinal back to 11-cis retinal. {ECO:0000269|PubMed:10632589, ECO:0000269|PubMed:12808468, ECO:0000269|PubMed:19793992}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19793992}; Multi-pass membrane protein {ECO:0000269|PubMed:19793992}. Note=Found in soma, dendrites and proximal part of axons of certain retinal ganglion cells. {ECO:0000250}. TISSUE SPECIFICITY: Eye. Expression is restricted within the ganglion and amacrine cell layers of the retina. Isoform 2 is about 40 times more abundant than isoform 1 in the retina. Isoform 1 is observed with processes in the outer strata of inner plexiform layer (IPL) close to the inner nuclear layer (INL) or is found to be bistratified with processes located both in the inner (ON) or outer (OFF) layers of the IPL. A second population of isoform 1 is identified in processes which are confined to the inner layer of the IPL near to the ganglion cell layer (GCL). Isoform 2 is involved in processes localized to the outer IPL or is bistratified with processes in both the inner and outer layers of the IPL. Isoform 2 is absent in the processes confined only to the inner layer of the IPL. {ECO:0000269|PubMed:10632589, ECO:0000269|PubMed:19793992}. +P32300 OPRD_MOUSE Delta-type opioid receptor (D-OR-1) (DOR-1) (K56) (MSL-2) 372 40,561 Beta strand (3); Chain (1); Disulfide bond (1); Glycosylation (2); Helix (11); Lipidation (1); Topological domain (8); Transmembrane (7) TRANSMEM 48 75 Helical; Name=1.; TRANSMEM 86 110 Helical; Name=2.; TRANSMEM 123 144 Helical; Name=3.; TRANSMEM 164 186 Helical; Name=4.; TRANSMEM 207 238 Helical; Name=5.; TRANSMEM 262 284 Helical; Name=6.; TRANSMEM 300 321 Helical; Name=7. TOPO_DOM 1 47 Extracellular. {ECO:0000269|PubMed:22596164}.; TOPO_DOM 76 85 Cytoplasmic. {ECO:0000269|PubMed:22596164}.; TOPO_DOM 111 122 Extracellular. {ECO:0000269|PubMed:22596164}.; TOPO_DOM 145 163 Cytoplasmic. {ECO:0000269|PubMed:22596164}.; TOPO_DOM 187 206 Extracellular. {ECO:0000269|PubMed:22596164}.; TOPO_DOM 239 261 Cytoplasmic. {ECO:0000269|PubMed:22596164}.; TOPO_DOM 285 299 Extracellular. {ECO:0000269|PubMed:22596164}.; TOPO_DOM 322 372 Cytoplasmic. {ECO:0000269|PubMed:22596164}. FUNCTION: G-protein coupled receptor that functions as receptor for endogenous enkephalins and for a subset of other opioids. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling leads to the inhibition of adenylate cyclase activity. Inhibits neurotransmitter release by reducing calcium ion currents and increasing potassium ion conductance. Plays a role in the perception of pain and in opiate-mediated analgesia. Plays a role in developing analgesic tolerance to morphine. {ECO:0000269|PubMed:10677041, ECO:0000269|PubMed:1334555, ECO:0000269|PubMed:1335167}. PTM: Ubiquitinated. A basal ubiquitination seems not to be related to degradation. Ubiquitination is increased upon formation of OPRM1:OPRD1 oligomers leading to proteasomal degradation; the ubiquitination is diminished by RTP4. {ECO:0000269|PubMed:18836069}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10677041, ECO:0000269|PubMed:1334555, ECO:0000269|PubMed:1335167, ECO:0000269|PubMed:18836069, ECO:0000269|PubMed:22596164}; Multi-pass membrane protein {ECO:0000269|PubMed:10677041, ECO:0000269|PubMed:1334555, ECO:0000269|PubMed:1335167, ECO:0000269|PubMed:22596164}. SUBUNIT: May form homooligomers. Forms a heterodimer with OPRM1 (PubMed:18836069). Interacts with GPRASP1 (By similarity). Interacts with RTP4; the interaction promotes cell surface localization of the OPRD1-OPRM1 heterodimer (PubMed:18836069). {ECO:0000250|UniProtKB:P41143, ECO:0000269|PubMed:18836069}. TISSUE SPECIFICITY: Brain, with high concentrations in the basal ganglia and limbic regions. {ECO:0000269|PubMed:10677041, ECO:0000269|PubMed:1335167}. +P33534 OPRK_MOUSE Kappa-type opioid receptor (K-OR-1) (KOR-1) (MSL-1) 380 42,652 Chain (1); Disulfide bond (1); Glycosylation (2); Lipidation (1); Sequence conflict (2); Topological domain (8); Transmembrane (7) TRANSMEM 58 85 Helical; Name=1. {ECO:0000250}.; TRANSMEM 96 119 Helical; Name=2. {ECO:0000250}.; TRANSMEM 133 154 Helical; Name=3. {ECO:0000250}.; TRANSMEM 174 196 Helical; Name=4. {ECO:0000250}.; TRANSMEM 223 247 Helical; Name=5. {ECO:0000250}.; TRANSMEM 275 296 Helical; Name=6. {ECO:0000250}.; TRANSMEM 312 333 Helical; Name=7. {ECO:0000250}. TOPO_DOM 1 57 Extracellular. {ECO:0000250}.; TOPO_DOM 86 95 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 120 132 Extracellular. {ECO:0000250}.; TOPO_DOM 155 173 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 197 222 Extracellular. {ECO:0000250}.; TOPO_DOM 248 274 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 297 311 Extracellular. {ECO:0000250}.; TOPO_DOM 334 380 Cytoplasmic. {ECO:0000250}. FUNCTION: G-protein coupled opioid receptor that functions as receptor for endogenous alpha-neoendorphins and dynorphins, but has low affinity for beta-endorphins. Also functions as receptor for various synthetic opioids and for the psychoactive diterpene salvinorin A. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling leads to the inhibition of adenylate cyclase activity. Inhibits neurotransmitter release by reducing calcium ion currents and increasing potassium ion conductance. Plays a role in the perception of pain. Plays a role in mediating reduced physical activity upon treatment with synthetic opioids. Plays a role in the regulation of salivation in response to synthetic opioids. May play a role in arousal and regulation of autonomic and neuroendocrine functions. {ECO:0000269|PubMed:8393575, ECO:0000269|PubMed:9463367}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8393575, ECO:0000269|PubMed:9463367}; Multi-pass membrane protein {ECO:0000269|PubMed:8393575, ECO:0000269|PubMed:9463367}. SUBUNIT: Interacts with SLC9A3R1. Interacts with GABARAPL1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Detected in brain (at protein level). Brain (neocortex, hippocampus, amygdala, medial habenula, hypothalamus, locus ceruleus, and parabrachial nucleus). {ECO:0000269|PubMed:8393575, ECO:0000269|PubMed:9463367}. +P42866 OPRM_MOUSE Mu-type opioid receptor (M-OR-1) (MOR-1) 398 44,421 Alternative sequence (16); Beta strand (5); Chain (1); Disulfide bond (1); Glycosylation (4); Helix (11); Lipidation (1); Modified residue (5); Motif (1); Mutagenesis (2); Sequence conflict (1); Topological domain (8); Transmembrane (7); Turn (2) TRANSMEM 67 91 Helical; Name=1. {ECO:0000269|PubMed:22437502, ECO:0000269|PubMed:26245379}.; TRANSMEM 105 129 Helical; Name=2. {ECO:0000269|PubMed:22437502, ECO:0000269|PubMed:26245379}.; TRANSMEM 141 163 Helical; Name=3. {ECO:0000269|PubMed:22437502, ECO:0000269|PubMed:26245379}.; TRANSMEM 184 205 Helical; Name=4. {ECO:0000269|PubMed:22437502, ECO:0000269|PubMed:26245379}.; TRANSMEM 229 253 Helical; Name=5. {ECO:0000269|PubMed:22437502, ECO:0000269|PubMed:26245379}.; TRANSMEM 278 304 Helical; Name=6. {ECO:0000269|PubMed:22437502, ECO:0000269|PubMed:26245379}.; TRANSMEM 313 336 Helical; Name=7. {ECO:0000269|PubMed:22437502, ECO:0000269|PubMed:26245379}. TOPO_DOM 1 66 Extracellular. {ECO:0000269|PubMed:22437502, ECO:0000269|PubMed:26245379}.; TOPO_DOM 92 104 Cytoplasmic. {ECO:0000269|PubMed:22437502, ECO:0000269|PubMed:26245379}.; TOPO_DOM 130 140 Extracellular. {ECO:0000269|PubMed:22437502, ECO:0000269|PubMed:26245379}.; TOPO_DOM 164 183 Cytoplasmic. {ECO:0000269|PubMed:22437502, ECO:0000269|PubMed:26245379}.; TOPO_DOM 206 228 Extracellular. {ECO:0000269|PubMed:22437502, ECO:0000269|PubMed:26245379}.; TOPO_DOM 254 277 Cytoplasmic. {ECO:0000269|PubMed:22437502, ECO:0000269|PubMed:26245379}.; TOPO_DOM 305 312 Extracellular. {ECO:0000269|PubMed:22437502, ECO:0000269|PubMed:26245379}.; TOPO_DOM 337 398 Cytoplasmic. {ECO:0000269|PubMed:22437502, ECO:0000269|PubMed:26245379}. FUNCTION: Receptor for endogenous opioids such as beta-endorphin and endomorphin. Receptor for natural and synthetic opioids including morphine, heroin, DAMGO, fentanyl, etorphine, buprenorphin and methadone. Agonist binding to the receptor induces coupling to an inactive GDP-bound heterotrimeric G-protein complex and subsequent exchange of GDP for GTP in the G-protein alpha subunit leading to dissociation of the G-protein complex with the free GTP-bound G-protein alpha and the G-protein beta-gamma dimer activating downstream cellular effectors. The agonist- and cell type-specific activity is predominantly coupled to pertussis toxin-sensitive G(i) and G(o) G alpha proteins, GNAI1, GNAI2, GNAI3 and GNAO1 isoforms Alpha-1 and Alpha-2, and to a lesser extent to pertussis toxin-insensitive G alpha proteins GNAZ and GNA15. They mediate an array of downstream cellular responses, including inhibition of adenylate cyclase activity and both N-type and L-type calcium channels, activation of inward rectifying potassium channels, mitogen-activated protein kinase (MAPK), phospholipase C (PLC), phosphoinositide/protein kinase (PKC), phosphoinositide 3-kinase (PI3K) and regulation of NF-kappa-B. Also couples to adenylate cyclase stimulatory G alpha proteins. The selective temporal coupling to G-proteins and subsequent signaling can be regulated by RGSZ proteins, such as RGS9, RGS17 and RGS4. Phosphorylation by members of the GPRK subfamily of Ser/Thr protein kinases and association with beta-arrestins is involved in short-term receptor desensitization. Beta-arrestins associate with the GPRK-phosphorylated receptor and uncouple it from the G-protein thus terminating signal transduction. The phosphorylated receptor is internalized through endocytosis via clathrin-coated pits which involves beta-arrestins. The activation of the ERK pathway occurs either in a G-protein-dependent or a beta-arrestin-dependent manner and is regulated by agonist-specific receptor phosphorylation. Acts as a class A G-protein coupled receptor (GPCR) which dissociates from beta-arrestin at or near the plasma membrane and undergoes rapid recycling. Receptor down-regulation pathways are varying with the agonist and occur dependent or independent of G-protein coupling. Endogenous ligands induce rapid desensitization, endocytosis and recycling. Heterooligomerization with other GPCRs can modulate agonist binding, signaling and trafficking properties. Involved in neurogenesis. Isoform 9 is involved in morphine-induced scratching and seems to cross-activate GRPR in response to morphine. {ECO:0000269|PubMed:10842167, ECO:0000269|PubMed:16682964, ECO:0000269|PubMed:21422164, ECO:0000269|PubMed:22437502, ECO:0000269|PubMed:26245379, ECO:0000269|PubMed:7797593, ECO:0000269|PubMed:9037090}. PTM: Phosphorylated. Differentially phosphorylated in basal and agonist-induced conditions. Agonist-mediated phosphorylation modulates receptor internalization. Phosphorylated by GRK2 in a agonist-dependent manner. Phosphorylation at Tyr-166 requires receptor activation, is dependent on non-receptor protein tyrosine kinase Src and results in a decrease in agonist efficacy by reducing G-protein coupling efficiency. Phosphorylated on tyrosine residues; the phosphorylation is involved in agonist-induced G-protein-independent receptor down-regulation. Phosphorylation at Ser-375 is involved in G-protein-dependent but not beta-arrestin-dependent activation of the ERK pathway. {ECO:0000250|UniProtKB:P33535}.; PTM: Ubiquitinated. A basal ubiquitination seems not to be related to degradation. Ubiquitination is increased upon formation of OPRM1:OPRD1 oligomers leading to proteasomal degradation; the ubiquitination is diminished by RTP4. {ECO:0000269|PubMed:18836069}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12642578, ECO:0000269|PubMed:22437502, ECO:0000269|PubMed:7797593}; Multi-pass membrane protein {ECO:0000269|PubMed:12642578, ECO:0000269|PubMed:22437502, ECO:0000269|PubMed:26245379, ECO:0000269|PubMed:7797593}. Cell projection, axon {ECO:0000250|UniProtKB:P97266}. Perikaryon {ECO:0000250|UniProtKB:P97266}. Cell projection, dendrite {ECO:0000250|UniProtKB:P97266}. Endosome {ECO:0000250|UniProtKB:P97266}. Note=Is rapidly internalized after agonist binding. {ECO:0000250|UniProtKB:P97266}. SUBUNIT: Forms homooligomers and heterooligomers with other GPCRs, such as OPRD1, OPRK1, OPRL1, NPFFR2, ADRA2A, SSTR2, CNR1 and CCR5 (probably in dimeric forms) (PubMed:10842167, PubMed:12270145, PubMed:18836069, PubMed:21422164). Interacts with heterotrimeric G proteins; interaction with a heterotrimeric complex containing GNAI1, GNB1 and GNG2 stabilizes the active conformation of the receptor and increases its affinity for endomorphin-2, the synthetic opioid peptide DAMGO and for morphinan agonists (PubMed:26245379). Interacts with PPL; the interaction disrupts agonist-mediated G-protein activation. Interacts (via C-terminus) with DNAJB4 (via C-terminus). Interacts with calmodulin; the interaction inhibits the constitutive activity of OPRM1; it abolishes basal and attenuates agonist-stimulated G-protein coupling. Interacts with FLNA, PLD2, RANBP9 and WLS and GPM6A (By similarity). Interacts with RTP4 (PubMed:18836069). Interacts with SYP and GNAS (By similarity). Interacts with RGS9, RGS17, RGS20, RGS4, PPP1R9B and HINT1 (PubMed:15827571, PubMed:17725581, PubMed:18439408, PubMed:21153910). Isoform 9 interacts with GRPR (PubMed:22000021). {ECO:0000250|UniProtKB:P33535, ECO:0000250|UniProtKB:P35372, ECO:0000269|PubMed:10842167, ECO:0000269|PubMed:12270145, ECO:0000269|PubMed:15827571, ECO:0000269|PubMed:17725581, ECO:0000269|PubMed:18439408, ECO:0000269|PubMed:18836069, ECO:0000269|PubMed:21153910, ECO:0000269|PubMed:21422164, ECO:0000269|PubMed:22000021, ECO:0000269|PubMed:22437502, ECO:0000269|PubMed:26245379}. +P15409 OPSD_MOUSE Rhodopsin 348 39,070 Chain (1); Disulfide bond (1); Glycosylation (2); Lipidation (2); Metal binding (2); Modified residue (8); Motif (1); Region (1); Sequence conflict (2); Site (1); Topological domain (8); Transmembrane (7) TRANSMEM 37 61 Helical; Name=1. {ECO:0000250|UniProtKB:P02699}.; TRANSMEM 74 96 Helical; Name=2. {ECO:0000250|UniProtKB:P02699}.; TRANSMEM 111 133 Helical; Name=3. {ECO:0000250|UniProtKB:P02699}.; TRANSMEM 153 173 Helical; Name=4. {ECO:0000250|UniProtKB:P02699}.; TRANSMEM 203 224 Helical; Name=5. {ECO:0000250|UniProtKB:P02699}.; TRANSMEM 253 274 Helical; Name=6. {ECO:0000250|UniProtKB:P02699}.; TRANSMEM 287 308 Helical; Name=7. {ECO:0000250|UniProtKB:P02699}. TOPO_DOM 1 36 Extracellular. {ECO:0000305}.; TOPO_DOM 62 73 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 97 110 Extracellular. {ECO:0000305}.; TOPO_DOM 134 152 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 174 202 Extracellular. {ECO:0000305}.; TOPO_DOM 225 252 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 275 286 Extracellular. {ECO:0000305}.; TOPO_DOM 309 348 Cytoplasmic. {ECO:0000305}. FUNCTION: Photoreceptor required for image-forming vision at low light intensity. Required for photoreceptor cell viability after birth (PubMed:9020854). Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change that activates signaling via G-proteins. Subsequent receptor phosphorylation mediates displacement of the bound G-protein alpha subunit by the arrestin SAG and terminates signaling (PubMed:27353443). {ECO:0000269|PubMed:27353443, ECO:0000269|PubMed:9020854}. PTM: Phosphorylated on some or all of the serine and threonine residues present in the C-terminal region. {ECO:0000269|PubMed:11910029}.; PTM: Contains one covalently linked retinal chromophore. Upon light absorption, the covalently bound 11-cis-retinal is converted to all-trans-retinal. After hydrolysis of the Schiff base and release of the covalently bound all-trans-retinal, active rhodopsin is regenerated by binding of a fresh molecule of 11-cis-retinal. {ECO:0000250|UniProtKB:P02699}. SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P02699}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P02699}. Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:27353443}. Note=Synthesized in the inner segment (IS) of rod photoreceptor cells before vectorial transport to disk membranes in the rod outer segment (OS) photosensory cilia. {ECO:0000250|UniProtKB:P08100}. SUBUNIT: Homodimer. Interacts (phosphorylated form) with SAG. Interacts with GNAT1, Interacts with GNAT3. SAG and G-proteins compete for a common binding site. Interacts with GRK1 (By similarity). {ECO:0000250|UniProtKB:P02699, ECO:0000250|UniProtKB:P08100}. TISSUE SPECIFICITY: Rod-shaped photoreceptor cells in the retina (at protein level). {ECO:0000269|PubMed:27353443}. +Q8K3K8 OPTN_MOUSE Optineurin 584 67,018 Chain (1); Coiled coil (3); Helix (1); Modified residue (3); Motif (2); Mutagenesis (1); Region (3); Zinc finger (1) FUNCTION: Plays an important role in the maintenance of the Golgi complex, in membrane trafficking, in exocytosis, through its interaction with myosin VI and Rab8. Links myosin VI to the Golgi complex and plays an important role in Golgi ribbon formation. Plays a role in the activation of innate immune response during viral infection. Mechanistically, recruits TBK1 at the Golgi apparatus, promoting its trans-phosphorylation after RLR or TLR3 stimulation. In turn, activated TBK1 phosphorylates its downstream partner IRF3 to produce IFN-beta. Plays a neuroprotective role in the eye and optic nerve. May act by regulating membrane trafficking and cellular morphogenesis via a complex that contains Rab8 and hungtingtin (HD). Mediates the interaction of Rab8 with the probable GTPase-activating protein TBC1D17 during Rab8-mediated endocytic trafficking, such as of transferrin receptor (TFRC/TfR); regulates Rab8 recruitnment to tubules emanating from the endocytic recycling compartment. Autophagy receptor that interacts directly with both the cargo to become degraded and an autophagy modifier of the MAP1 LC3 family; targets ubiquitin-coated bacteria (xenophagy), such as cytoplasmic Salmonella enterica, and appears to function in the same pathway as SQSTM1 and CALCOCO2/NDP52. May constitute a cellular target for adenovirus E3 14.7, an inhibitor of TNF-alpha functions, thereby affecting cell death. {ECO:0000250|UniProtKB:Q96CV9, ECO:0000269|PubMed:26677802}. PTM: Phosphorylated by TBK1, leading to restrict bacterial proliferation in case of infection. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:15607428}. Golgi apparatus {ECO:0000250|UniProtKB:Q96CV9}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Cytoplasmic vesicle, autophagosome {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Recycling endosome {ECO:0000250}. Note=Found in the perinuclear region and associates with the Golgi apparatus. Colocalizes with MYO6 and RAB8 at the Golgi complex and in vesicular structures close to the plasma membrane. Localizes to LC3-positive cytoplasmic vesicles upon induction of autophagy (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q96CV9}. SUBUNIT: Interacts with HD, Rab8 (RAB8A and/or RAB8B) (active GTP-bound form), GTF3A, TRAF3, TBK1, MYO6 and TFRC. Binds to linear ubiquitin chains. Interacts with LC3 family members MAP1LC3A, MAP1LC3B, GABARAP, GABARAPL1 and GABARAPL2; OPTN phosphorylation increases the association (at least with MAP1LC3B). Self-associates. Interacts with RAB12; the interaction may be indirect. Interacts with TBK1; this interaction leads to the Golgi localization of TBK1 and its subsequent activation. {ECO:0000250|UniProtKB:Q96CV9, ECO:0000269|PubMed:20388642}. DOMAIN: Ubiquitin-binding motif (UBAN) is essential for its inhibitory function, subcellular localization and interaction with TBK1. {ECO:0000250}.; DOMAIN: The LIR (LC3-interacting region) motif mediates the interaction with ATG8 family proteins. {ECO:0000250}. TISSUE SPECIFICITY: In eye, it is expressed in anterior segment, retina, and optic nerve blood vessels (at protein level). Highly expressed in adult liver, heart and testis. {ECO:0000269|PubMed:15607428}. +Q920A0 OPT_MOUSE Opticin (Oculoglycan) 328 36,422 Chain (1); Compositional bias (2); Disulfide bond (1); Domain (1); Glycosylation (4); Modified residue (1); Repeat (6); Sequence conflict (3); Signal peptide (1) FUNCTION: Binds collagen fibrils. {ECO:0000250}. PTM: O-glycosylated. {ECO:0000305}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. TISSUE SPECIFICITY: Present in the presumptive ciliary body during development and in the nonpigmented ciliary epithelium of the adult eye. +Q61183 PAPOA_MOUSE Poly(A) polymerase alpha (PAP-alpha) (EC 2.7.7.19) (Polynucleotide adenylyltransferase) 739 82,309 Alternative sequence (6); Binding site (4); Chain (1); Cross-link (6); Metal binding (5); Modified residue (9); Motif (2); Mutagenesis (3); Nucleotide binding (3); Region (2); Sequence conflict (1); Site (5) FUNCTION: Polymerase that creates the 3'-poly(A) tail of mRNA's. Also required for the endoribonucleolytic cleavage reaction at some polyadenylation sites. May acquire specificity through interaction with a cleavage and polyadenylation specificity factor (CPSF) at its C-terminus. {ECO:0000250|UniProtKB:P51003, ECO:0000269|PubMed:18084034, ECO:0000269|PubMed:18281463}. PTM: Polysumoylated. Varying sumolyation depending on tissue- and cell-type. Highly sumoylated in bladder and NIH 3T3 cells. Sumoylation is required for nuclear localization and enhances PAP stability. Desumoylated by SENP1. Inhibits polymerase activity. {ECO:0000269|PubMed:18281463}.; PTM: Hyperphosphorylation on multiple CDK2 consensus and non-consensus sites in the C-terminal Ser/Thr-rich region represses PAP activity in late M-phase. Phosphorylation/dephosphorylation may regulate the interaction between PAP and CPSF (By similarity). {ECO:0000250}.; PTM: Acetylated in the C-terminus. Acetylation decreases interaction with NUDT21 and KPNB1, and inhibits nuclear localization through inhibiting binding to the importin alpha/beta complex (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Monomer. Found in a complex with CPSF1, FIP1L1 and PAPOLA. Interacts with AHCYL1 and FIP1L1; the interaction with AHCYL1 seems to increase interaction with FIP1L1 (PubMed:19224921). Interacts with NUDT21; the interaction is diminished by acetylation. Interacts with KPNB1; the interaction promotes PAP nuclear import and is inhibited by acetylation of PAP (By similarity). {ECO:0000250|UniProtKB:P25500, ECO:0000250|UniProtKB:P51003, ECO:0000269|PubMed:19224921}. TISSUE SPECIFICITY: Expressed in brain, thymus, lung, kidney, bladder, testis and spleen. {ECO:0000269|PubMed:18281463}. +Q61006 MUSK_MOUSE Muscle, skeletal receptor tyrosine-protein kinase (EC 2.7.10.1) (Muscle-specific tyrosine-protein kinase receptor) (MuSK) (Muscle-specific kinase receptor) 868 96,693 Active site (1); Alternative sequence (3); Binding site (1); Chain (1); Disulfide bond (9); Domain (5); Glycosylation (3); Modified residue (4); Mutagenesis (1); Nucleotide binding (1); Sequence conflict (20); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 495 515 Helical. {ECO:0000255}. TOPO_DOM 22 494 Extracellular. {ECO:0000255}.; TOPO_DOM 516 868 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor tyrosine kinase which plays a central role in the formation and the maintenance of the neuromuscular junction (NMJ), the synapse between the motor neuron and the skeletal muscle. Recruitment of AGRIN by LRP4 to the MUSK signaling complex induces phosphorylation and activation of MUSK, the kinase of the complex. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. May regulate AChR phosphorylation and clustering through activation of ABL1 and Src family kinases which in turn regulate MUSK. DVL1 and PAK1 that form a ternary complex with MUSK are also important for MUSK-dependent regulation of AChR clustering. May positively regulate Rho family GTPases through FNTA. Mediates the phosphorylation of FNTA which promotes prenylation, recruitment to membranes and activation of RAC1 a regulator of the actin cytoskeleton and of gene expression. Other effectors of the MUSK signaling include DNAJA3 which functions downstream of MUSK. May also play a role within the central nervous system by mediating cholinergic responses, synaptic plasticity and memory formation. {ECO:0000269|PubMed:11323662, ECO:0000269|PubMed:12756238, ECO:0000269|PubMed:14622576, ECO:0000269|PubMed:15340048, ECO:0000269|PubMed:8653786}. PTM: Ubiquitinated by PDZRN3. Ubiquitination promotes endocytosis and lysosomal degradation. {ECO:0000269|PubMed:17576800}.; PTM: Phosphorylated (PubMed:16818610). Phosphorylation is induced by AGRIN (PubMed:8653787, PubMed:18848351). Autophosphorylated. Autophosphorylation at Tyr-553 is required for interaction with DOK7 which in turn stimulates the phosphorylation and the activation of MUSK (PubMed:16794080, PubMed:20603078). {ECO:0000269|PubMed:16794080, ECO:0000269|PubMed:16818610, ECO:0000269|PubMed:18848351, ECO:0000269|PubMed:20603078, ECO:0000269|PubMed:8653787}.; PTM: Neddylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane {ECO:0000269|PubMed:19038220}; Single-pass type I membrane protein {ECO:0000269|PubMed:19038220}. Note=Localizes to the postsynaptic cell membrane of the neuromuscular junction. SUBUNIT: Monomer. Homodimer (Probable). Interacts with LRP4; the heterodimer forms an AGRIN receptor complex that binds AGRIN resulting in activation of MUSK. Forms a heterotetramer composed of 2 DOK7 and 2 MUSK molecules which facilitates MUSK trans-autophosphorylation on tyrosine residue and activation. Interacts (via cytoplasmic part) with DOK7 (via IRS-type PTB domain); requires MUSK phosphorylation. Interacts with DVL1 (via DEP domain); the interaction is direct and mediates the formation of a DVL1, MUSK and PAK1 ternary complex involved in AChR clustering. Interacts with PDZRN3; this interaction is enhanced by agrin. Interacts with FNTA; the interaction is direct and mediates AGRIN-induced phosphorylation and activation of FNTA. Interacts with CSNK2B; mediates regulation by CK2. Interacts (via the cytoplasmic domain) with DNAJA3. Interacts with NSF; may regulate MUSK endocytosis and activity. Interacts with CAV3; may regulate MUSK signaling. Interacts with RNF31. {ECO:0000269|PubMed:12165471, ECO:0000269|PubMed:14622576, ECO:0000269|PubMed:14678832, ECO:0000269|PubMed:16794080, ECO:0000269|PubMed:16818610, ECO:0000269|PubMed:17576800, ECO:0000269|PubMed:18272689, ECO:0000269|PubMed:18848351, ECO:0000269|PubMed:19038220, ECO:0000269|PubMed:19940021, ECO:0000269|PubMed:20603078, ECO:0000305}. TISSUE SPECIFICITY: Expressed preferentially in skeletal muscle. {ECO:0000269|PubMed:7624144}. +P16332 MUTA_MOUSE Methylmalonyl-CoA mutase, mitochondrial (MCM) (EC 5.4.99.2) (Methylmalonyl-CoA isomerase) 748 82,844 Binding site (4); Chain (1); Domain (1); Metal binding (1); Modified residue (7); Region (4); Sequence conflict (12); Transit peptide (1) FUNCTION: Involved in the degradation of several amino acids, odd-chain fatty acids and cholesterol via propionyl-CoA to the tricarboxylic acid cycle. {ECO:0000250|UniProtKB:P22033}. SUBCELLULAR LOCATION: Mitochondrion matrix. SUBUNIT: Homodimer. Interacts (the apoenzyme form) with MMAA; the interaction is GTP dependent. {ECO:0000250|UniProtKB:P22033}. +P10166 MYCL_MOUSE Protein L-Myc 368 40,848 Chain (1); Domain (1); Region (1) SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}. SUBUNIT: Efficient DNA binding requires dimerization with another bHLH protein. Binds DNA as a heterodimer with MAX. +P06876 MYB_MOUSE Transcriptional activator Myb (Proto-oncogene c-Myb) 636 71,422 Beta strand (4); Chain (1); Cross-link (1); DNA binding (3); Domain (3); Helix (13); Modified residue (4); Region (4); Sequence conflict (8) FUNCTION: Transcriptional activator; DNA-binding protein that specifically recognize the sequence 5'-YAAC[GT]G-3'. Plays an important role in the control of proliferation and differentiation of hematopoietic progenitor cells. PTM: Ubiquitinated; mediated by SIAH1 and leading to its subsequent proteasomal degradation. {ECO:0000250}.; PTM: Phosphorylated by NLK on multiple sites, which induces proteasomal degradation.; PTM: Phosphorylated by HIPK1. This phosphorylation reduces MYB transcription factor activity but not MYB protein levels (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Binds to HIPK1 (By similarity). Interacts with HIPK2, MAF, MYBBP1A and NLK. {ECO:0000250, ECO:0000269|PubMed:11792321, ECO:0000269|PubMed:15082531, ECO:0000269|PubMed:17823980, ECO:0000269|PubMed:9447996, ECO:0000269|PubMed:9566892}. DOMAIN: Comprised of 3 domains; an N-terminal DNA-binding domain, a centrally located transcriptional activation domain and a C-terminal domain involved in transcriptional repression.; DOMAIN: C-terminal truncated mutants display increased transactivation. +P48972 MYBB_MOUSE Myb-related protein B (B-Myb) (Myb-like protein 2) 704 79,103 Beta strand (1); Chain (1); Cross-link (16); DNA binding (3); Domain (3); Helix (3); Modified residue (9) FUNCTION: Transcription factor involved in the regulation of cell survival, proliferation, and differentiation. Transactivates the expression of the CLU gene (By similarity). {ECO:0000250}. PTM: Phosphorylated by cyclin A/CDK2 during S-phase. Phosphorylation at Thr-524 is probably involved in transcriptional activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Component of the DREAM complex (also named LINC complex) at least composed of E2F4, E2F5, LIN9, LIN37, LIN52, LIN54, MYBL1, MYBL2, RBL1, RBL2, RBBP4, TFDP1 and TFDP2. The complex exists in quiescent cells where it represses cell cycle-dependent genes. It dissociates in S phase when LIN9, LIN37, LIN52 and LIN54 form a subcomplex that binds to MYBL2 (By similarity). {ECO:0000250}. +Q8VIM5 MYCD_MOUSE Myocardin (Basic SAP coiled-coil transcription activator 2) (SRF cofactor protein) 935 101,400 Alternative sequence (3); Chain (1); Coiled coil (2); Compositional bias (2); Domain (1); Modified residue (12); Motif (1); Mutagenesis (10); Region (1); Repeat (3); Sequence conflict (2) FUNCTION: Smooth muscle cells (SM) and cardiac muscle cells-specific transcriptional factor which uses the canonical single or multiple CArG boxes DNA sequence. Acts as a cofactor of serum response factor (SRF) with the potential to modulate SRF-target genes. Plays a crucial role in cardiogenesis and differentiation of the smooth muscle cell lineage (myogenesis). Isoform 1 mediates the cardiac transcription factor MEF2C-dependent transcription. Isoform 1 and isoform 3 are more active than isoform 2 and isoform 4 in stimulating cardiac muscle promoters. {ECO:0000269|PubMed:11439182, ECO:0000269|PubMed:12640126, ECO:0000269|PubMed:12663482, ECO:0000269|PubMed:16818234, ECO:0000269|PubMed:20385216}. PTM: Phosphorylation regulates negatively transcriptional activity. {ECO:0000269|PubMed:16141410, ECO:0000269|PubMed:19776005}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:11439182, ECO:0000269|PubMed:15601857}. Note=Nuclear, with a punctate intranuclear pattern with exclusion from nuclei. SUBUNIT: Homodimer. Interacts with MLLT7/FOXO4 (By similarity). Interacts with SRF, its association does not depend on specific DNA sequences for ternary complex formation. Interacts (via C-terminal) with EP300 (via CREB-binding domain). Interacts with HDAC4 and HDAC5. Interacts with MEF2C. {ECO:0000250, ECO:0000269|PubMed:11439182, ECO:0000269|PubMed:12663482, ECO:0000269|PubMed:15601857, ECO:0000269|PubMed:16818234}. DOMAIN: The C-terminal region contains a general transcription activation domain. The N-terminal region, comprising a basic and a Gln-rich domain, confers transcriptional potency and specificity by mediating association with the MADS box of SRF. The basic domain may be required for nuclear localization. The SAP domain is important for transactivation and ternary complex formation. TISSUE SPECIFICITY: Expressed in heart, aorta, and in smooth muscle cell-containing tissues: stomach, bladder and uterus. Isoform 1 and isoform 3 are predominantly expressed in cardiac muscle whereas isoform 4 and isoform 5 are predominantly expressed in SMC-rich tissues. Isoform 3 is the most abundant isoform in the heart from embryo to adult. {ECO:0000269|PubMed:11439182, ECO:0000269|PubMed:12640126, ECO:0000269|PubMed:12663482, ECO:0000269|PubMed:14645532, ECO:0000269|PubMed:20385216}. +Q5SX40 MYH1_MOUSE Myosin-1 (Myosin heavy chain 1) (Myosin heavy chain 2x) (MyHC-2x) (Myosin heavy chain, skeletal muscle, adult 1) 1942 223,342 Chain (1); Coiled coil (1); Domain (3); Modified residue (40); Nucleotide binding (1); Region (2) FUNCTION: Muscle contraction. SUBCELLULAR LOCATION: Cytoplasm, myofibril. Note=Thick filaments of the myofibrils. SUBUNIT: Muscle myosin is a hexameric protein that consists of 2 heavy chain subunits (MHC), 2 alkali light chain subunits (MLC) and 2 regulatory light chain subunits (MLC-2). DOMAIN: The rodlike tail sequence is highly repetitive, showing cycles of a 28-residue repeat pattern composed of 4 heptapeptides, characteristic for alpha-helical coiled coils.; DOMAIN: Limited proteolysis of myosin heavy chain produces 1 light meromyosin (LMM) and 1 heavy meromyosin (HMM). HMM can be further cleaved into 2 globular subfragments (S1) and 1 rod-shaped subfragment (S2). {ECO:0000305}. +P01108 MYC_MOUSE Myc proto-oncogene protein (Proto-oncogene c-Myc) (Transcription factor p64) 439 48,971 Chain (1); Compositional bias (2); Cross-link (4); Domain (1); Erroneous initiation (1); Glycosylation (1); Modified residue (14); Mutagenesis (3); Region (1); Sequence conflict (3) FUNCTION: Transcription factor that binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3'. Activates the transcription of growth-related genes. Binds to the VEGFA promoter, promoting VEGFA production and subsequent sprouting angiogenesis. {ECO:0000250|UniProtKB:P01106}. PTM: Phosphorylated by PRKDC. Phosphorylated at Ser-62 by DYRK2; this primes the protein for subsequent phosphorylation by GSK3B at Thr-58. Phosphorylation at Thr-58 and Ser-62 by GSK3 is required for ubiquitination and degradation by the proteasome. Phosphorylation at Ser-62 by CDK2 prevents Ras-induced senescence (By similarity). Phosphorylation at Ser-329 by PIM2 leads to the stabilization of MYC. {ECO:0000250, ECO:0000269|PubMed:18438430}.; PTM: Ubiquitinated by the SCF(FBXW7) complex when phosphorylated at Thr-58 and Ser-62, leading to its degradation by the proteasome. Ubiquitination is counteracted by USP28 in the nucleoplasm and USP36 in the nucleolus, both interacting with of FBXW7, leading to its deubiquitination and preventing degradation. Also polyubiquitinated by the DCX(TRUSS) complex (By similarity). Ubiquitinated by TRIM6 in a phosphorylation-independent manner (PubMed:22328504). {ECO:0000250|UniProtKB:P01106, ECO:0000269|PubMed:22328504}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P01106}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P01106}. SUBUNIT: Efficient DNA binding requires dimerization with another bHLH protein. Binds DNA as a heterodimer with MAX (By similarity). Interacts with TAF1C and SPAG9. Interacts with PARP10. Interacts with KDM5A and KDM5B. Interacts (when phosphorylated at Thr-58 and Ser-62) with FBXW7. Interacts with PIM2 (PubMed:18438430). Interacts with RIOX1. The heterodimer MYC:MAX interacts with ABI1; the interaction may enhance MYC:MAX transcriptional activity (By similarity). Interacts with TRIM6 (PubMed:22328504). Interacts with NPM1; the binary complex is recruited to the promoter of MYC target genes and enhances their transcription (By similarity). Interacts with CIP2A; leading to the stabilization of MYC (By similarity). {ECO:0000250|UniProtKB:P01106, ECO:0000269|PubMed:12391307, ECO:0000269|PubMed:18438430, ECO:0000269|PubMed:22328504}. +Q3UR85 MYRF_MOUSE Myelin regulatory factor (EC 3.4.-.-) (Myelin gene regulatory factor) [Cleaved into: Myelin regulatory factor, N-terminal; Myelin regulatory factor, C-terminal] 1138 123,288 Alternative sequence (5); Beta strand (17); Chain (3); Coiled coil (1); Compositional bias (1); DNA binding (1); Domain (1); Glycosylation (3); Helix (1); Modified residue (1); Motif (2); Mutagenesis (10); Sequence conflict (1); Site (1); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 769 789 Helical. {ECO:0000255}. TOPO_DOM 1 768 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 790 1138 Lumenal. {ECO:0000255}. FUNCTION: Myelin regulatory factor: Constitutes a precursor of the transcription factor. Mediates the autocatalytic cleavage that releases the Myelin regulatory factor, N-terminal component that specifically activates transcription of central nervous system (CNS) myelin genes. {ECO:0000269|PubMed:23966833, ECO:0000269|PubMed:28623291}.; FUNCTION: Myelin regulatory factor, C-terminal: Membrane-bound part that has no transcription factor activity and remains attached to the endoplasmic reticulum membrane following cleavage. {ECO:0000269|PubMed:23966833}.; FUNCTION: Myelin regulatory factor, N-terminal: Transcription factor that specifically activates expression of myelin genes such as MBP, MOG, MAG, DUSP15 and PLP1 during oligodendrocyte (OL) maturation, thereby playing a central role in oligodendrocyte maturation and CNS myelination (PubMed:19596243, PubMed:22956843, PubMed:23966833, PubMed:24204311, PubMed:27532821). Specifically recognizes and binds DNA sequence 5'-CTGGYAC-3' in the regulatory regions of myelin-specific genes and directly activates their expression. Not only required during oligodendrocyte differentiation but is also required on an ongoing basis for the maintenance of expression of myelin genes and for the maintenance of a mature, viable oligodendrocyte phenotype (PubMed:19596243, PubMed:22956843, PubMed:23966833). {ECO:0000269|PubMed:19596243, ECO:0000269|PubMed:22956843, ECO:0000269|PubMed:23966833, ECO:0000269|PubMed:24204311, ECO:0000269|PubMed:27532821}. PTM: Myelin regulatory factor, C-terminal: Glycosylated. {ECO:0000250|UniProtKB:Q9Y2G1}.; PTM: Myelin regulatory factor: Follows autocatalytic cleavage via the peptidase S74 domain. Autoprocessing is apparently constitutive and is essential for transcriptional activity. {ECO:0000269|PubMed:23966833, ECO:0000269|PubMed:28623291}. SUBCELLULAR LOCATION: Myelin regulatory factor: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23966833}; Single-pass membrane protein.; SUBCELLULAR LOCATION: Myelin regulatory factor, N-terminal: Nucleus {ECO:0000269|PubMed:23966833, ECO:0000269|PubMed:28441531}. Cytoplasm {ECO:0000269|PubMed:23966833}. Note=Translocates from the cytoplasm to the nucleus upon autocatalytic cleavage. {ECO:0000269|PubMed:23966833}.; SUBCELLULAR LOCATION: Myelin regulatory factor, C-terminal: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23966833}; Single-pass membrane protein {ECO:0000269|PubMed:23966833}. SUBUNIT: Homotrimer. {ECO:0000269|PubMed:23966833, ECO:0000269|PubMed:28623291}. DOMAIN: Myelin regulatory factor, N-terminal: The nuclear localization signals mediate translocation to the nucleus. {ECO:0000269|PubMed:23966833}.; DOMAIN: Myelin regulatory factor: The peptidase S74 domain, also named Intramolecular Chaperone Auto-processed (ICA) domain or Intramolecuar Chaperone Domain (ICD), has protease activity and mediates autocatalytic processing of the protein to generate the Myelin regulatory factor, N-terminal active transcription factor and the Myelin regulatory factor, C-terminal components. {ECO:0000269|PubMed:23966833}. TISSUE SPECIFICITY: Specifically expressed by postmitotic oligodendrocytes in the CNS. Not detected in the peripheral nervous system (PNS). {ECO:0000269|PubMed:19596243}. +Q8VCR8 MYLK2_MOUSE Myosin light chain kinase 2, skeletal/cardiac muscle (MLCK2) (EC 2.7.11.18) 613 65,990 Active site (1); Binding site (1); Chain (1); Compositional bias (2); Domain (1); Modified residue (4); Nucleotide binding (1); Region (1) FUNCTION: Implicated in the level of global muscle contraction and cardiac function. Phosphorylates a specific serine in the N-terminus of a myosin light chain (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Colocalizes with phosphorylated myosin light chain (RLCP) at filaments of the myofibrils. {ECO:0000250}. SUBUNIT: May interact with centrin. {ECO:0000250}. +Q1EG27 MYO3B_MOUSE Myosin-IIIb (EC 2.7.11.1) 1305 148,099 Active site (1); Alternative sequence (2); Binding site (1); Chain (1); Domain (4); Helix (3); Nucleotide binding (1); Region (1); Sequence conflict (2) FUNCTION: Probable actin-based motor with a protein kinase activity (By similarity). Required for normal cochlear hair bundle development and hearing. Plays an important role in the early steps of cochlear hair bundle morphogenesis. Influences the number and lengths of stereocilia to be produced and limits the growth of microvilli within the forming auditory hair bundles thereby contributing to the architecture of the hair bundle, including its staircase pattern (PubMed:26754646). Involved in the elongation of actin in stereocilia tips by transporting the actin regulatory factor ESPN to the plus ends of actin filaments (PubMed:22264607). {ECO:0000250|UniProtKB:Q8WXR4, ECO:0000269|PubMed:22264607, ECO:0000269|PubMed:26754646}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell projection, stereocilium {ECO:0000269|PubMed:26754646}. SUBUNIT: Interacts (via C-terminus) with ESPN (PubMed:26785147, PubMed:26926603). Interacts (via C-terminus) with ESPNL (PubMed:26926603). {ECO:0000269|PubMed:26785147, ECO:0000269|PubMed:26926603}. TISSUE SPECIFICITY: Expressed in the cochlear hair cells (at protein level) (PubMed:26754646). Expressed in utricle hair bundles (at protein level) (PubMed:26926603). {ECO:0000269|PubMed:26754646, ECO:0000269|PubMed:26926603}. +Q8C170 MYO9A_MOUSE Unconventional myosin-IXa (Unconventional myosin-9a) 2542 292,119 Alternative sequence (1); Chain (1); Coiled coil (3); Compositional bias (1); Domain (8); Erroneous initiation (1); Modified residue (10); Nucleotide binding (1); Region (3); Sequence conflict (1); Transmembrane (1); Zinc finger (2) TRANSMEM 175 195 Helical. {ECO:0000255}. FUNCTION: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Regulates Rho by stimulating it's GTPase activity in neurons, has a role in the regulation of neuronal morphology and function. {ECO:0000250|UniProtKB:Q9Z1N3}. PTM: Phosphorylated by ALPK1 following monosodium urate monohydrate (MSU)-induced inflammation. {ECO:0000250|UniProtKB:B2RTY4}. SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9Z1N3}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9Z1N3}. Cytoplasm {ECO:0000250|UniProtKB:Q9Z1N3}. Note=Localized in the cytoplasm of cell bodies, dendrites and axons with occasional hints of an enrichment near the plasma membrane. {ECO:0000250|UniProtKB:Q9Z1N3}. TISSUE SPECIFICITY: Expressed in the eye, lung, liver, brain, heart, kidney, skeletal muscle and spleen. No detection was found in liver. {ECO:0000269|PubMed:10409426}. +Q8CES0 NAA30_MOUSE N-alpha-acetyltransferase 30 (EC 2.3.1.256) (N-acetyltransferase 12) (N-acetyltransferase MAK3 homolog) (NatC catalytic subunit) 364 39,433 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (1); Frameshift (1); Modified residue (6); Sequence conflict (1) FUNCTION: Catalytic subunit of the N-terminal acetyltransferase C (NatC) complex. Catalyzes acetylation of the N-terminal methionine residues of peptides beginning with Met-Leu-Ala and Met-Leu-Gly. Necessary for the lysosomal localization and function of ARL8B sugeesting that ARL8B is a NatC substrate. {ECO:0000250|UniProtKB:Q147X3}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q147X3}. Nucleus {ECO:0000250|UniProtKB:Q147X3}. SUBUNIT: Component of the N-terminal acetyltransferase C (NatC) complex, which is composed of NAA35, NAA38 and NAA30. {ECO:0000250|UniProtKB:Q147X3}. +Q9CQ65 MTAP_MOUSE S-methyl-5'-thioadenosine phosphorylase (EC 2.4.2.28) (5'-methylthioadenosine phosphorylase) (MTA phosphorylase) (MTAP) (MTAPase) 283 31,062 Binding site (3); Chain (1); Modified residue (1); Region (3); Site (2) Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (phosphorylase route): step 1/1. FUNCTION: Catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates. {ECO:0000255|HAMAP-Rule:MF_03155}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000255|HAMAP-Rule:MF_03155}. SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_03155}. +Q9D110 MTHFS_MOUSE 5-formyltetrahydrofolate cyclo-ligase (EC 6.3.3.2) (5,10-methenyl-tetrahydrofolate synthetase) (MTHFS) (Methenyl-THF synthetase) 203 23,202 Binding site (3); Chain (1); Initiator methionine (1); Metal binding (2); Modified residue (1); Nucleotide binding (2); Region (1) FUNCTION: Contributes to tetrahydrofolate metabolism. Helps regulate carbon flow through the folate-dependent one-carbon metabolic network that supplies carbon for the biosynthesis of purines, thymidine and amino acids. Catalyzes the irreversible conversion of 5-formyltetrahydrofolate (5-CHO-H(4)PteGlu) to yield 5,10-methenyltetrahydrofolate (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. +Q9WTJ6 MTL5_MOUSE Tesmin (Metallothionein-like 5, testis-specific) (Testis-specific metallothionein-like protein) 475 50,616 Alternative sequence (1); Chain (1); Domain (1); Erroneous initiation (1); Modified residue (2); Sequence conflict (2) FUNCTION: May have a role in spermatogenesis. {ECO:0000305}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11803038, ECO:0000269|PubMed:12606435}. Nucleus {ECO:0000269|PubMed:11803038, ECO:0000269|PubMed:12606435}. Note=Predominantly localized to the cytoplasm (PubMed:11803038, PubMed:12606435). Translocates from the cytoplasm to the nucleus in the G2/M transition upon treatment with cadmium, cobalt or zinc (PubMed:11803038, PubMed:12606435). {ECO:0000269|PubMed:11803038, ECO:0000269|PubMed:12606435}. TISSUE SPECIFICITY: Expressed in spermatocytes and adult heart. Also expressed in fetal brain, heart, kidney and ovary. {ECO:0000269|PubMed:10191092, ECO:0000269|PubMed:12606435, ECO:0000269|PubMed:14648882}. +Q8VED8 MTFR2_MOUSE Mitochondrial fission regulator 2 (DUF729 domain-containing protein 1) 361 40,748 Chain (1); Compositional bias (1); Modified residue (3); Sequence conflict (7) FUNCTION: May play a role in mitochondrial aerobic respiration essentially in the testis. Can also promote mitochondrial fission. {ECO:0000269|PubMed:20568109}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:20568109}. Note=Associated with membranes. TISSUE SPECIFICITY: Expressed predominantly in testis (at protein level). Expressed to a lower extent in spleen. {ECO:0000269|PubMed:20568109}. +Q8R2R6 MTG1_MOUSE Mitochondrial ribosome-associated GTPase 1 (GTP-binding protein 7) (Mitochondrial GTPase 1) 326 36,679 Binding site (1); Chain (1); Domain (1); Erroneous termination (1); Nucleotide binding (2); Sequence conflict (3); Transit peptide (1) FUNCTION: Plays a role in the regulation of the mitochondrial ribosome assembly and of translational activity (By similarity). Displays mitochondrial GTPase activity (By similarity). {ECO:0000250|UniProtKB:Q9BT17}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9BT17}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9BT17}; Matrix side {ECO:0000250|UniProtKB:Q9BT17}. SUBUNIT: Associates with the mitochondrial ribosome large subunit; the association occurs in a GTP-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q9BT17}. +Q9WVQ5 MTNB_MOUSE Methylthioribulose-1-phosphate dehydratase (MTRu-1-P dehydratase) (EC 4.2.1.109) (APAF1-interacting protein) (Monocyte/macrophage protein 19) 241 26,949 Active site (1); Binding site (1); Chain (1); Metal binding (3); Sequence conflict (1) Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 2/6. FUNCTION: Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P). Functions in the methionine salvage pathway, which plays a key role in cancer, apoptosis, microbial proliferation and inflammation. May inhibit the CASP1-related inflammatory response (pyroptosis), the CASP9-dependent apoptotic pathway and the cytochrome c-dependent and APAF1-mediated cell death. {ECO:0000255|HAMAP-Rule:MF_03116, ECO:0000269|PubMed:15262985, ECO:0000269|PubMed:17086211}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03116}. SUBUNIT: Homotetramer. Interacts with APAF1. May interact with CASP1. {ECO:0000255|HAMAP-Rule:MF_03116}. TISSUE SPECIFICITY: Expressed in skeletal muscle (at protein level). {ECO:0000269|PubMed:15262985}. +Q99JT9 MTND_MOUSE 1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase (EC 1.13.11.54) (Acireductone dioxygenase (Fe(2+)-requiring)) (ARD) (Fe-ARD) (Membrane-type 1 matrix metalloproteinase cytoplasmic tail-binding protein 1) (MTCBP-1) 179 21,524 Beta strand (9); Chain (1); Helix (5); Metal binding (4); Turn (1) Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 5/6. FUNCTION: Catalyzes the formation of formate and 2-keto-4-methylthiobutyrate (KMTB) from 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) (PubMed:26858196). Also down-regulates cell migration mediated by MMP14. {ECO:0000255|HAMAP-Rule:MF_03154, ECO:0000269|PubMed:26858196}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03154}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03154}. Cell membrane {ECO:0000255|HAMAP-Rule:MF_03154}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03154}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03154}. Note=Localizes to the plasma membrane when complexed to MMP14. {ECO:0000255|HAMAP-Rule:MF_03154}. SUBUNIT: Monomer. Interacts with MMP14. {ECO:0000255|HAMAP-Rule:MF_03154}. +P35377 OPRX_MOUSE Nociceptin receptor (K3 opiate receptor) (Kappa-type 3 opioid receptor) (KOR-3) (ORGC) (Orphanin FQ receptor) 367 40,491 Alternative sequence (9); Chain (1); Disulfide bond (1); Glycosylation (3); Lipidation (1); Sequence conflict (1); Site (2); Topological domain (8); Transmembrane (7) TRANSMEM 46 71 Helical; Name=1. {ECO:0000250}.; TRANSMEM 85 106 Helical; Name=2. {ECO:0000250}.; TRANSMEM 122 143 Helical; Name=3. {ECO:0000250}.; TRANSMEM 163 185 Helical; Name=4. {ECO:0000250}.; TRANSMEM 209 233 Helical; Name=5. {ECO:0000250}.; TRANSMEM 262 282 Helical; Name=6. {ECO:0000250}.; TRANSMEM 298 319 Helical; Name=7. {ECO:0000250}. TOPO_DOM 1 45 Extracellular. {ECO:0000250}.; TOPO_DOM 72 84 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 107 121 Extracellular. {ECO:0000250}.; TOPO_DOM 144 162 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 186 208 Extracellular. {ECO:0000250}.; TOPO_DOM 234 261 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 283 297 Extracellular. {ECO:0000250}.; TOPO_DOM 320 367 Cytoplasmic. {ECO:0000250}. FUNCTION: G-protein coupled opioid receptor that functions as receptor for the endogenous neuropeptide nociceptin. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Signaling via G proteins mediates inhibition of adenylate cyclase activity and calcium channel activity. Arrestins modulate signaling via G proteins and mediate the activation of alternative signaling pathways that lead to the activation of MAP kinases. Plays a role in modulating nociception and the perception of pain. Plays a role in the regulation of locomotor activity by the neuropeptide nociceptin. {ECO:0000269|PubMed:12217419, ECO:0000269|PubMed:12814369, ECO:0000269|PubMed:23652222, ECO:0000269|PubMed:7603458, ECO:0000269|PubMed:8794880}. PTM: Phosphorylation at Ser-360 requires GRK3. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cytoplasmic vesicle {ECO:0000250}. Note=Ligand binding leads to receptor internalization into cytoplasmic vesicles, decreasing the amount of available receptor at the cell surface. Internalization requires phosphorylation at Ser-360. Can recycle to the cell membrane (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: In the brain, isoform KOR3 and isoform KOR3C are most abundant in hypothalamus and periaqueductal gray. Isoform KOR3A is highly expressed in cortex, striatum and brainstem. Isoform KOR3D is highly expressed in cerebellum, hypothalamus and brainstem. Detected in spleen lymphocytes. {ECO:0000269|PubMed:7603458, ECO:0000269|PubMed:7797625, ECO:0000269|PubMed:9755860}. +Q9Z1N2 ORC1_MOUSE Origin recognition complex subunit 1 840 95,103 Beta strand (14); Binding site (5); Chain (1); Domain (1); Helix (3); Metal binding (2); Modified residue (6); Nucleotide binding (1); Region (1); Sequence conflict (2); Turn (1) FUNCTION: Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. The specific DNA sequences that define origins of replication have not been identified yet. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication (By similarity). {ECO:0000250}. PTM: Phosphorylated during mitosis. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of ORC, a complex composed of at least 6 subunits: ORC1, ORC2, ORC3, ORC4, ORC5 and ORC6. ORC is regulated in a cell-cycle dependent manner. It is sequentially assembled at the exit from anaphase of mitosis and disassembled as cells enter S phase (By similarity). Interacts with CDC6 and KAT7/HBO1 (By similarity). Interacts with LRWD1 predominantly during the G1 phase and with less affinity during mitosis, when phosphorylated (By similarity). {ECO:0000250}. DOMAIN: The BAH domain mediates binding to dimethylated histone H4 'Lys-20' (H4K20me2), which is enriched at replication origins. +Q9CQZ0 ORML2_MOUSE ORM1-like protein 2 153 17,390 Alternative sequence (1); Chain (1); Sequence conflict (1); Transmembrane (2) TRANSMEM 22 42 Helical. {ECO:0000255}.; TRANSMEM 43 63 Helical. {ECO:0000255}. FUNCTION: Negative regulator of sphingolipid synthesis. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q9CPZ6 ORML3_MOUSE ORM1-like protein 3 153 17,477 Chain (1); Sequence conflict (1); Transmembrane (3) TRANSMEM 22 42 Helical. {ECO:0000255}.; TRANSMEM 43 63 Helical. {ECO:0000255}.; TRANSMEM 95 117 Helical. {ECO:0000255}. FUNCTION: Negative regulator of sphingolipid synthesis. May indirectly regulate endoplasmic reticulum-mediated Ca(+2) signaling (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with SPTLC1. {ECO:0000250}. +Q8R2W9 PANK3_MOUSE Pantothenate kinase 3 (mPanK3) (EC 2.7.1.33) (Pantothenic acid kinase 3) 370 41,120 Binding site (3); Chain (1) Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5. FUNCTION: Plays a role in the physiological regulation of the intracellular CoA concentration. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. SUBUNIT: Homodimer. {ECO:0000250}. +Q68ED3 PAPD5_MOUSE Terminal nucleotidyltransferase 4A (Non-canonical poly(A) RNA polymerase PAPD5) (EC 2.7.7.19) (PAP-associated domain-containing protein 5) (Terminal guanylyltransferase) (EC 2.7.7.-) (Terminal nucleotidyltransferase 4B) (Terminal uridylyltransferase 3) (TUTase 3) (Topoisomerase-related function protein 4-2) (TRF4-2) 633 69,704 Chain (1); Compositional bias (3); Cross-link (4); Domain (1); Erroneous initiation (1); Metal binding (2); Modified residue (1); Motif (1); Sequence conflict (2) FUNCTION: Terminal nucleotidyltransferase that catalyzes preferentially the transfert of ATP and GTP on RNA 3' poly(A) tail creating a heterogeneous 3' poly(A) tail leading to mRNAs stabilization by protecting mRNAs from active deadenylation (By similarity). Also functions as a catalytic subunit of a TRAMP-like complex which has a poly(A) RNA polymerase activity and is involved in a post-transcriptional quality control mechanism. Polyadenylation with short oligo(A) tails is required for the degradative activity of the exosome on several of its nuclear RNA substrates. Doesn't need a cofactor for polyadenylation activity (in vitro). Plays a role in replication-dependent histone mRNA degradation, probably through terminal uridylation of mature histone mRNAs. May play a role in sister chromatid cohesion (By similarity). {ECO:0000250|UniProtKB:Q8NDF8}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8NDF8}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q8NDF8}. Cytoplasm {ECO:0000250|UniProtKB:Q8NDF8}. Note=Predominantly expressed in the cytoplasm. {ECO:0000250|UniProtKB:Q8NDF8}. SUBUNIT: Component of a nucleolar TRAMP-like complex, an ATP-dependent exosome regulatory complex consisting of a helicase (MTREX), an oligadenylate polymerase (TENT4B or TENT4A), and a substrate specific RNA-binding factor (ZCCHC7 or ZCCHC8). Several TRAMP-like complexes exist with specific compositions and are associated with nuclear, or nucleolar RNA exosomes. {ECO:0000250|UniProtKB:Q8NDF8}. +O88940 MUSC_MOUSE Musculin (Myogenic repressor) 201 21,538 Chain (1); Compositional bias (2); Domain (1); Motif (1); Mutagenesis (1) FUNCTION: Transcription repressor that blocks myogenesis and activation of E-box dependent muscle genes. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Efficient DNA binding requires dimerization with another bHLH protein. Binds DNA as a homodimer or a heterodimer. Forms a heterodimer with TCF3. +Q61909 MTG8_MOUSE Protein CBFA2T1 (Protein MTG8) 577 64,338 Chain (1); Compositional bias (4); Domain (1); Modified residue (2); Region (3); Zinc finger (1) FUNCTION: Transcriptional corepressor which facilitates transcriptional repression via its association with DNA-binding transcription factors and recruitment of other corepressors and histone-modifying enzymes. Can repress the expression of MMP7 in a ZBTB33-dependent manner. Can repress transactivation mediated by TCF12 (By similarity). Acts as a negative regulator of adipogenesis (PubMed:23527555). {ECO:0000250|UniProtKB:Q06455, ECO:0000269|PubMed:23527555}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00440}. Note=Colocalizes with ATN1 in discrete nuclear dots. {ECO:0000250}. SUBUNIT: Homotetramer (By similarity). Heterotetramer with CBFA2T2 and CBFA2T3 (By similarity). Interacts with TCF12, SIN3A, HDAC1, HDAC2, HDAC3, NCOR1 and NCOR2. Interacts with ATN1 (via its N-terminus); the interaction enhances the transcriptional repression (By similarity). {ECO:0000250|UniProtKB:Q06455}. DOMAIN: The TAFH domain mediates interaction with transcription regulators. {ECO:0000250|UniProtKB:Q06455}.; DOMAIN: Nervy homology region 2 (NHR2) mediates homo- and possibly heterotypic oligomerization by forming a four-helix bundle tetrameric structure. {ECO:0000250|UniProtKB:Q06455}. +Q60945 MTCP1_MOUSE Protein p13 MTCP-1 (p13MTCP1) (Mature T-cell proliferation-1 type B1) (MTCP-1 type B1) 107 12,645 Chain (1) FUNCTION: Enhances the phosphorylation and activation of AKT1 and AKT2. {ECO:0000250}. SUBUNIT: Interacts with AKT1 and AKT2 (via PH domain). Does not interact with AKT3 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Not found at a significant level in any tissue. +Q8BKY8 MTEF2_MOUSE Transcription termination factor 2, mitochondrial (Mitochondrial transcription termination factor 2) (mTERF2) (mTERF domain-containing protein 3, mitochondrial) 385 43,453 Chain (1); Transit peptide (1) FUNCTION: Binds mitochondrial DNA and plays a role in the regulation of transcription of mitochondrial mRNA and rRNA species. {ECO:0000250|UniProtKB:Q49AM1}. SUBCELLULAR LOCATION: Mitochondrion matrix, mitochondrion nucleoid {ECO:0000269|PubMed:19366608}. SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q49AM1}. +Q8BJS8 MTBP_MOUSE Mdm2-binding protein (mMTBP) 894 100,314 Alternative sequence (3); Chain (1); Modified residue (4); Region (1); Sequence conflict (6) FUNCTION: May play a role in MDM2-dependent p53/TP53 homeostasis in unstressed cells. Inhibits autoubiquitination of MDM2, thereby enhancing MDM2 stability. This promotes MDM2-mediated ubiquitination of p53/TP53 and its subsequent degradation. Inhibits cell migration in vitro and suppresses the invasive behavior of tumor cells. {ECO:0000269|PubMed:10906133, ECO:0000269|PubMed:15632057}. SUBUNIT: Interacts with MDM2. {ECO:0000269|PubMed:10906133}. TISSUE SPECIFICITY: Expressed in small intestine and spleen at low levels, in the ovary at intermediate levels and in the testis and thymus at high levels. {ECO:0000269|PubMed:10906133}. +Q80TA6 MTMRC_MOUSE Myotubularin-related protein 12 (Inactive phosphatidylinositol 3-phosphatase 12) 747 85,516 Alternative sequence (1); Chain (1); Domain (1); Erroneous initiation (2); Modified residue (2); Region (1) FUNCTION: Acts as an adapter for the myotubularin-related phosphatases (PubMed:23818870). Regulates phosphatase MTM1 protein stability and possibly its intracellular location (PubMed:23818870). By stabilizing MTM1 protein levels, required for skeletal muscle maintenance but not for myogenesis (PubMed:23818870). {ECO:0000269|PubMed:23818870}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9C0I1}. Sarcoplasmic reticulum {ECO:0000269|PubMed:23818870}. Cytoplasm, myofibril, sarcomere {ECO:0000269|PubMed:23818870}. Note=Localizes to punctate vesicles when associated with MTM1 (By similarity). Localizes to triads, a structure formed by a T tubule and two sarcoplasmic reticulum terminal cisterna (PubMed:23818870). In skeletal muscles, co-localizes with MTM1 in the sarcomere (PubMed:23818870). Partially localizes to the sarcoplasmic reticulum in skeletal muscles (PubMed:23818870). {ECO:0000250|UniProtKB:Q9C0I1, ECO:0000269|PubMed:23818870}. SUBUNIT: Forms a complex composed of MTMR12 and lipid phosphatase MTM1; in skeletal muscles, the interaction stabilizes both MTMR12 and MTM1 protein levels; the interaction may modulate MTM1 intracellular location (PubMed:23818870). Forms a complex composed of MTMR12 and lipid phosphatase MTMR2 (By similarity). {ECO:0000250|UniProtKB:Q9C0I1, ECO:0000269|PubMed:23818870}. TISSUE SPECIFICITY: Expressed in skeletal muscles (at protein level). {ECO:0000269|PubMed:23818870}. +Q8VEL2 MTMRE_MOUSE Myotubularin-related protein 14 (EC 3.1.3.-) (mJumpy) 648 72,443 Active site (1); Chain (1); Compositional bias (1); Erroneous initiation (1); Glycosylation (3); Modified residue (6) FUNCTION: Lipid phosphatase which efficiently dephosphorylates phosphatidylinositol 3-phosphate (PtdIns3P) and PtdIns(3,5)P2; inactive toward PtdIns4P, PtdIns(3,4)P2, PtdIns(4,5)P2 and PtdIns(3,4,5)P3. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Note=Found in reticular structures and plasma membrane ruffles. Concentrated near the nucleus (By similarity). {ECO:0000250}. +Q8VE11 MTMR6_MOUSE Myotubularin-related protein 6 (EC 3.1.3.-) 617 70,933 Active site (1); Binding site (1); Chain (1); Domain (1); Modified residue (4); Region (3) FUNCTION: Phosphatase that acts on lipids with a phosphoinositol headgroup. Acts as a negative regulator of KCNN4/KCa3.1 channel activity in CD4+ T-cells possibly by decreasing intracellular levels of phosphatidylinositol 3 phosphatase. Negatively regulates proliferation of reactivated CD4+ T-cells (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000250|UniProtKB:Q9Y217}. SUBUNIT: Interacts with ALKBH4, KCNN4, MTMR7, MTMR8 and MTMR9. {ECO:0000250}. +Q9Z2D0 MTMR9_MOUSE Myotubularin-related protein 9 545 62,908 Chain (1); Domain (1); Frameshift (1); Modified residue (1) FUNCTION: Probable pseudophosphatase. Contains a Gly residue instead of a conserved Cys residue in the dsPTPase catalytic loop which renders it catalytically inactive as a phosphatase (Potential). {ECO:0000305}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with MTMR6, MTMR7 and MTMR8. {ECO:0000250}. +Q7TPM9 MTMRA_MOUSE Myotubularin-related protein 10 (Inactive phosphatidylinositol 3-phosphatase 10) 771 88,197 Chain (1); Compositional bias (1); Domain (1); Modified residue (2); Sequence caution (1) +Q3V1L6 MTMRB_MOUSE Myotubularin-related protein 11 (Inactive phosphatidylinositol 3-phosphatase 11) 700 78,396 Chain (1); Domain (1); Erroneous initiation (1) +Q9CQT1 MTNA_MOUSE Methylthioribose-1-phosphate isomerase (M1Pi) (MTR-1-P isomerase) (EC 5.3.1.23) (S-methyl-5-thioribose-1-phosphate isomerase) (Translation initiation factor eIF-2B subunit alpha/beta/delta-like protein) 369 39,411 Active site (1); Chain (1); Modified residue (3); Sequence conflict (4); Site (1) Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 1/6. FUNCTION: Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P). {ECO:0000255|HAMAP-Rule:MF_03119}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03119}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03119}. +Q8BGX4 OFCC1_MOUSE Orofacial cleft 1 candidate gene 1 protein homolog (Orofacial clefting chromosomal breakpoint region candidate 1 protein homolog) 166 18,233 Chain (1) +P62774 MTPN_MOUSE Myotrophin (Granule cell differentiation protein) (Protein V-1) 118 12,861 Beta strand (2); Chain (1); Helix (9); Initiator methionine (1); Modified residue (5); Repeat (3); Sequence conflict (1); Turn (3) FUNCTION: Promotes dimerization of NF-kappa-B subunits and regulates NF-kappa-B transcription factor activity. Promotes growth of cardiomyocytes, but not cardiomyocyte proliferation. Promotes cardiac muscle hypertrophy (By similarity). Plays a role in the regulation of the growth of actin filaments. Inhibits the activity of the F-actin-capping protein complex formed by the CAPZA1 and CAPZB heterodimer. {ECO:0000250, ECO:0000269|PubMed:20538588}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. SUBUNIT: Interacts with RELA (By similarity). Interacts with the heterodimer formed by CAPZA1 and CAPZB. {ECO:0000250, ECO:0000269|PubMed:20538588}. +O08601 MTP_MOUSE Microsomal triglyceride transfer protein large subunit 894 99,099 Alternative sequence (1); Chain (1); Domain (1); Sequence conflict (8); Signal peptide (1) FUNCTION: Catalyzes the transport of triglyceride, cholesteryl ester, and phospholipid between phospholipid surfaces. Required for the secretion of plasma lipoproteins that contain apolipoprotein B. May be involved in regulating cholesteryl ester biosynthesis in cells that produce lipoproteins. Loads phospholipid into the C1D1 antigen-binding groove. Isoform 2 is critical for the development of natural killer T (NKT) cells. May have a role in the biogenesis of lipid droplets. {ECO:0000269|PubMed:17312007, ECO:0000269|PubMed:17635917, ECO:0000269|PubMed:18502767}. SUBCELLULAR LOCATION: Isoform 1: Endoplasmic reticulum. Note=Localized to the endoplasmic reticulum (PubMed:17312007). Colocalizes with P4HB/PDI in the endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:P55157, ECO:0000269|PubMed:17312007}.; SUBCELLULAR LOCATION: Isoform 2: Endoplasmic reticulum. Golgi apparatus. Note=Localized to the endoplasmic reticulum (PubMed:17312007). Localized to the Golgi apparatus (PubMed:17635917). {ECO:0000269|PubMed:17312007, ECO:0000269|PubMed:17635917}. SUBUNIT: Heterodimer; heterodimerizes with the protein disulfide isomerase (P4HB/PDI). Interacts with APOB. {ECO:0000250|UniProtKB:P55157}. TISSUE SPECIFICITY: Expressed in heart. Isoform 1 is mainly expressed in the intestine and the liver, and at lower levels in white and brown fat cells. Isoform 2 is ubiquitous, and is the major isoform in hematopoietic cells and adipocytes. {ECO:0000269|PubMed:17312007, ECO:0000269|PubMed:17635917, ECO:0000269|PubMed:9502759}. +O88495 MTR1L_MOUSE Melatonin-related receptor (G protein-coupled receptor 50) (H9) 591 65,130 Chain (1); Disulfide bond (1); Topological domain (8); Transmembrane (7) TRANSMEM 39 59 Helical; Name=1. {ECO:0000255}.; TRANSMEM 73 93 Helical; Name=2. {ECO:0000255}.; TRANSMEM 112 132 Helical; Name=3. {ECO:0000255}.; TRANSMEM 152 172 Helical; Name=4. {ECO:0000255}.; TRANSMEM 197 217 Helical; Name=5. {ECO:0000255}.; TRANSMEM 248 268 Helical; Name=6. {ECO:0000255}.; TRANSMEM 282 302 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 38 Extracellular. {ECO:0000255}.; TOPO_DOM 60 72 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 94 111 Extracellular. {ECO:0000255}.; TOPO_DOM 133 151 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 173 196 Extracellular. {ECO:0000255}.; TOPO_DOM 218 247 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 269 281 Extracellular. {ECO:0000255}.; TOPO_DOM 303 591 Cytoplasmic. {ECO:0000255}. FUNCTION: Does not bind melatonin. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBUNIT: Homodimer, and heterodimer with MTNR1A and MTNR1B. {ECO:0000250}. +Q8R1S4 MTSS1_MOUSE Metastasis suppressor protein 1 (Missing in metastasis protein) 759 82,408 Alternative sequence (3); Chain (1); Coiled coil (1); Compositional bias (2); Domain (2); Helix (9); Modified residue (9); Mutagenesis (2); Sequence conflict (2); Turn (1) FUNCTION: Inhibits the nucleation of actin filaments in vitro. {ECO:0000269|PubMed:12482861}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SUBUNIT: Binds to actin. DOMAIN: The WH2 motif at the C-terminus binds to actin monomers. {ECO:0000269|PubMed:12482861}. TISSUE SPECIFICITY: Strongly expressed in the developing neurons and skeletal and cardiac muscles in embryos. Strongly expressed also in liver, outer layers of the kidney, and in the Purkinje cells of the brain. {ECO:0000269|PubMed:12482861}. +Q9DAT5 MTU1_MOUSE Mitochondrial tRNA-specific 2-thiouridylase 1 (EC 2.8.1.14) 417 47,240 Active site (2); Binding site (2); Chain (1); Disulfide bond (1); Nucleotide binding (1); Region (3); Site (3) FUNCTION: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). Required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. ATP is required to activate the C2 atom of the wobble base. {ECO:0000250|UniProtKB:O75648}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14746906}. TISSUE SPECIFICITY: Widely expressed but most abundant in tissues with high metabolic rate including heart, liver and brain. Expression is low in spleen, testis, lung and skeletal muscle. Also expressed in inner ear. {ECO:0000269|PubMed:14746906}. +Q5HZI1 MTUS1_MOUSE Microtubule-associated tumor suppressor 1 homolog (AT2 receptor-binding protein) (Angiotensin-II type 2 receptor-interacting protein) (Coiled-coiled tumor suppressor gene 1 protein) (Mitochondrial tumor suppressor 1 homolog) 1210 134,379 Alternative sequence (5); Chain (1); Coiled coil (1); Erroneous initiation (3); Modified residue (13); Sequence conflict (28) FUNCTION: Cooperates with AGTR2 to inhibit ERK2 activation and cell proliferation. May be required for AGTR2 cell surface expression. Together with PTPN6, induces UBE2V2 expression upon angiotensin-II stimulation. {ECO:0000269|PubMed:15123706, ECO:0000269|PubMed:15539617, ECO:0000269|PubMed:17068200}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Golgi apparatus. Cell membrane. Nucleus. Note=In neurons, translocates into the nucleus after treatment with angiotensin-II. SUBUNIT: Homodimer. Interacts with AGTR2. Interacts with PTPN6. {ECO:0000269|PubMed:15123706, ECO:0000269|PubMed:15539617, ECO:0000269|PubMed:17068200}. TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in uterus and adrenal gland. {ECO:0000269|PubMed:15539617}. +Q91ZW2 OFUT1_MOUSE GDP-fucose protein O-fucosyltransferase 1 (EC 2.4.1.221) (Peptide-O-fucosyltransferase 1) (O-FucT-1) 393 44,688 Beta strand (18); Binding site (1); Chain (1); Disulfide bond (4); Glycosylation (2); Helix (20); Motif (1); Region (3); Sequence conflict (1); Signal peptide (1); Turn (4) Protein modification; protein glycosylation. FUNCTION: Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue found in the consensus sequence C2-X(4,5)-[S/T]-C3 of EGF domains, where C2 and C3 are the second and third conserved cysteines. Specifically uses GDP-fucose as donor substrate and proper disulfide pairing of the substrate EGF domains is required for fucose transfer. Plays a crucial role in NOTCH signaling. Initial fucosylation of NOTCH by POFUT1 generates a substrate for FRINGE/RFNG, an acetylglucosaminyltransferase that can then extend the fucosylation on the NOTCH EGF repeats. This extended fucosylation is required for optimal ligand binding and canonical NOTCH signaling induced by DLL1 or JAGGED1. Fucosylates AGRN and determines its ability to cluster acetylcholine receptors (AChRs). {ECO:0000269|PubMed:12697902, ECO:0000269|PubMed:18775496}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:P83337}. SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:Q6EV70}. +Q3UHD3 MTUS2_MOUSE Microtubule-associated tumor suppressor candidate 2 homolog (Cardiac zipper protein) (Microtubule plus-end tracking protein TIP150) (Tracking protein of 150 kDa) 1353 147,356 Alternative sequence (4); Chain (1); Coiled coil (1); Modified residue (2); Region (3); Sequence caution (1) FUNCTION: Binds microtubules. Together with MAPRE1 may target the microtubule depolymerase KIF2C to the plus-end of microtubules. May regulate the dynamics of microtubules at their growing distal tip (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Note=Associated with the microtubule network at the growing distal tip (the plus-end) of microtubules. {ECO:0000250}. SUBUNIT: Homodimer. Interacts with KIF2C and MAPRE1; the interaction is direct and probably targets MTUS2 and KIF2C to microtubules (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in heart from early embryonic development onwards. Later during embryonic development, expressed in brain and nervous system, in limb buds and in the epithelium lining the bronchia of the lung. Detected in adult brain, heart and eye, but not detected in other adult tissues examined. {ECO:0000269|PubMed:19806667}. +Q8VHI3 OFUT2_MOUSE GDP-fucose protein O-fucosyltransferase 2 (EC 2.4.1.221) (Peptide-O-fucosyltransferase 2) (O-FucT-2) 429 49,429 Binding site (1); Chain (1); Disulfide bond (2); Frameshift (1); Glycosylation (3); Mutagenesis (1); Region (3); Signal peptide (1); Site (1) Protein modification; protein glycosylation. FUNCTION: Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue in the consensus sequence C1-X(2,3)-S/T-C2-X(2)-G of thrombospondin type I repeats (TSRs) where C1 and C2 are the first and second cysteines of the repeat, respectively. O-fucosylates members of several protein families including the ADAMTS superfamily and the thrombosporin (TSP) and spondin families. Required for the proper secretion of ADAMTS family members such as ADAMSL1 and ADAMST13 (By similarity). O-fucosylation of TSRs is also required for restricting epithelial to mesenchymal transition (EMT), maintaining the correct patterning of mesoderm and localization of the definite endoderm. {ECO:0000250, ECO:0000269|PubMed:20637190}. SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250}. Golgi apparatus {ECO:0000250}. Note=Mainly located in the endoplasmic reticulum. {ECO:0000250}. +P47802 MTX1_MOUSE Metaxin-1 (Mitochondrial outer membrane import complex protein 1) 317 35,624 Chain (1); Cross-link (4); Transmembrane (1) TRANSMEM 272 292 Helical. {ECO:0000255}. FUNCTION: Involved in transport of proteins into the mitochondrion. Essential for embryonic development. {ECO:0000269|PubMed:9045676}. PTM: Ubiquitinated by PRKN during mitophagy, leading to its degradation and enhancement of mitophagy. Deubiquitinated by USP30. {ECO:0000250|UniProtKB:Q13505}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:9045676}. SUBUNIT: Interacts with MTX2/metaxin-2. Associates with the mitochondrial contact site and cristae organizing system (MICOS) complex, composed of at least MINOS1/MIC10, CHCHD3/MIC19, CHCHD6/MIC25, APOOL/MIC27, IMMT/MIC60, APOO/MIC23/MIC26 and QIL1/MIC13. This complex was also known under the names MINOS or MitOS complex. The MICOS complex associates with mitochondrial outer membrane proteins SAMM50, MTX1 and MTX2 (together described as components of the mitochondrial outer membrane sorting assembly machinery (SAM) complex) and DNAJC11, mitochondrial inner membrane protein TMEM11 and with HSPA9. The MICOS and SAM complexes together with DNAJC11 are part of a large protein complex spanning both membranes termed the mitochondrial intermembrane space bridging (MIB) complex (By similarity). {ECO:0000250|UniProtKB:Q13505, ECO:0000269|PubMed:10381257}. TISSUE SPECIFICITY: Ubiquitous. Higher levels are seen in the kidney as compared to other tissues. +O88441 MTX2_MOUSE Metaxin-2 (Mitochondrial outer membrane import complex protein 2) 263 29,758 Chain (1); Initiator methionine (1); Modified residue (1) FUNCTION: Involved in transport of proteins into the mitochondrion. {ECO:0000269|PubMed:10381257}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:10381257}. Mitochondrion {ECO:0000250|UniProtKB:O75431}. SUBUNIT: Interacts with MTX1/metaxin-1. Associates with the mitochondrial contact site and cristae organizing system (MICOS) complex, composed of at least MINOS1/MIC10, CHCHD3/MIC19, CHCHD6/MIC25, APOOL/MIC27, IMMT/MIC60, APOO/MIC23/MIC26 and QIL1/MIC13. This complex was also known under the names MINOS or MitOS complex. The MICOS complex associates with mitochondrial outer membrane proteins SAMM50, MTX1 and MTX2 (together described as components of the mitochondrial outer membrane sorting assembly machinery (SAM) complex) and DNAJC11, mitochondrial inner membrane protein TMEM11 and with HSPA9. The MICOS and SAM complexes together with DNAJC11 are part of a large protein complex spanning both membranes termed the mitochondrial intermembrane space bridging (MIB) complex (By similarity). {ECO:0000250|UniProtKB:O75431, ECO:0000269|PubMed:10381257}. +Q9EQQ9 OGA_MOUSE Protein O-GlcNAcase (OGA) (EC 3.2.1.169) (Beta-N-acetylhexosaminidase) (Beta-hexosaminidase) (Bifunctional protein NCOAT) (Meningioma-expressed antigen 5) (N-acetyl-beta-D-glucosaminidase) (N-acetyl-beta-glucosaminidase) 916 103,162 Active site (1); Alternative sequence (3); Binding site (6); Chain (1); Erroneous initiation (2); Modified residue (1); Mutagenesis (5); Region (1); Sequence caution (1); Sequence conflict (3); Site (1) FUNCTION: Cleaves GlcNAc but not GalNAc from O-glycosylated proteins. Can use p-nitrophenyl-beta-GlcNAc and 4-methylumbelliferone-GlcNAc as substrates but not p-nitrophenyl-beta-GalNAc or p-nitrophenyl-alpha-GlcNAc (in vitro) (PubMed:16517082). Does not bind acetyl-CoA and does not have histone acetyltransferase activity. {ECO:0000250|UniProtKB:O60502, ECO:0000269|PubMed:16517082}. PTM: Proteolytically cleaved by caspase-3 during apoptosis. The fragments interact with each other; cleavage does not decrease enzyme activity. {ECO:0000250|UniProtKB:O60502}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. SUBUNIT: Monomer (By similarity). Interacts with CLOCK. {ECO:0000250|UniProtKB:O60502, ECO:0000269|PubMed:23395175}. +Q3U0K8 OGFD1_MOUSE Prolyl 3-hydroxylase OGFOD1 (EC 1.14.11.-) (2-oxoglutarate and iron-dependent oxygenase domain-containing protein 1) (uS12 prolyl 3-hydroxylase) 545 62,734 Alternative sequence (2); Binding site (2); Chain (1); Domain (1); Erroneous initiation (1); Metal binding (3); Sequence conflict (5) FUNCTION: Prolyl 3-hydroxylase that catalyzes 3-hydroxylation of 'Pro-62' of small ribosomal subunit uS12 (RPS23), thereby regulating protein translation termination efficiency. Involved in stress granule formation. {ECO:0000250|UniProtKB:Q8N543}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8N543}. Nucleus {ECO:0000250|UniProtKB:Q8N543}. SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q8N543}. +P19467 MUC13_MOUSE Mucin-13 (MUC-13) (Cell surface antigen 114/A10) (Lymphocyte antigen 64) 573 58,701 Chain (1); Disulfide bond (9); Domain (4); Glycosylation (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 481 508 Helical. {ECO:0000255}. TOPO_DOM 18 480 Extracellular. {ECO:0000255}.; TOPO_DOM 509 573 Cytoplasmic. {ECO:0000255}. FUNCTION: Epithelial and hemopoietic transmembrane mucin that may play a role in cell signaling. {ECO:0000250}. PTM: Cleaved into two subunits, alpha and beta, probably between the first EGF domain and the SEA domain. Beta subunit contains the cytoplasmic tail and alpha subunit the extracellular tail. The homooligomerization into dimers is dependent on intrachain disulfide bonds (By similarity). {ECO:0000250}.; PTM: Highly N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Secreted {ECO:0000250}. Note=Also exists as a soluble form. {ECO:0000250}. SUBUNIT: Homodimer of beta subunits. {ECO:0000250}. +Q8VE52 OGRL1_MOUSE Opioid growth factor receptor-like protein 1 464 52,268 Chain (1); Erroneous initiation (1) +Q8R2Y2 MUC18_MOUSE Cell surface glycoprotein MUC18 (Gicerin) (Melanoma cell adhesion molecule) (Melanoma-associated antigen MUC18) (CD antigen CD146) 648 71,545 Alternative sequence (1); Chain (1); Disulfide bond (5); Domain (5); Glycosylation (2); Modified residue (2); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 564 584 Helical. {ECO:0000255}. TOPO_DOM 24 563 Extracellular. {ECO:0000255}.; TOPO_DOM 585 648 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a role in cell adhesion, and in cohesion of the endothelial monolayer at intercellular junctions in vascular tissue. Its expression may allow melanoma cells to interact with cellular elements of the vascular system, thereby enhancing hematogeneous tumor spread. Could be an adhesion molecule active in neural crest cells during embryonic development. Acts as surface receptor that triggers tyrosine phosphorylation of FYN and PTK2/FAK1, and a transient increase in the intracellular calcium concentration (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Detected in melanoma cell lines. {ECO:0000269|PubMed:11255016}. +Q8BUE7 MUC20_MOUSE Mucin-20 (MUC-20) 656 68,720 Chain (1); Compositional bias (1); Erroneous initiation (1); Glycosylation (2); Region (3); Repeat (5); Sequence conflict (12); Signal peptide (1) FUNCTION: May regulate MET signaling cascade. Seems to decrease hepatocyte growth factor (HGF)-induced transient MAPK activation. Blocks GRB2 recruitment to MET thus suppressing the GRB2-RAS pathway. Inhibits HGF-induced proliferation of MMP1 and MMP9 expression (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Apical cell membrane {ECO:0000250}. Basolateral cell membrane {ECO:0000250}. Cell projection, microvillus membrane {ECO:0000250}. SUBUNIT: Interacts with MET; oligomerization increases affinity for MET. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in kidney. Up-regulated in renal tissues during renal injury. {ECO:0000269|PubMed:14565953}. +Q9R0L9 MUC24_MOUSE Sialomucin core protein 24 (MUC-24) (Endolyn) (Multi-glycosylated core protein 24) (MGC-24) (MGC-24v) (CD antigen CD164) 197 21,059 Chain (1); Compositional bias (1); Glycosylation (9); Mutagenesis (2); Region (1); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 163 183 Helical. {ECO:0000255}. TOPO_DOM 24 162 Extracellular. {ECO:0000255}.; TOPO_DOM 184 197 Cytoplasmic. {ECO:0000255}. FUNCTION: Sialomucin that may play a key role in hematopoiesis. May be involved in cell adhesion (By similarity). Promotes myogenesis by enhancing CXCR4-dependent cell motility. Positively regulates myoblast migration and promotes myoblast fusion into myotubes. {ECO:0000250|UniProtKB:Q04900, ECO:0000269|PubMed:18227060}. PTM: Highly N- and O-glycosylated; contains sialic acid. {ECO:0000250}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q04900}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q04900}. Endosome membrane {ECO:0000250|UniProtKB:Q04900}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q04900}. Cell membrane {ECO:0000250|UniProtKB:Q04900}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q04900}. SUBUNIT: Interacts with CXCR4. {ECO:0000269|PubMed:18227060}. TISSUE SPECIFICITY: Expressed at high levels in the submaxillary gland and kidney, at moderate levels in the brain, heart, lung, liver, intestine, testis, muscle and bone marrow, and at low levels in the pancreas, spleen and thymus. In the ear, expressed in the inner and outer hair cells of the organ of Corti, cells of Kolliker's organ, cells in the lateral cochlear wall behind the spiral prominence and cells of the stria vascularis (PubMed:26197441). {ECO:0000269|PubMed:10491205, ECO:0000269|PubMed:11027692, ECO:0000269|PubMed:26197441}. +Q80Z19 MUC2_MOUSE Mucin-2 (MUC-2) (Colonic mucin) (MCM) (Secreted gel-forming mucin) (Fragments) 2680 293,436 Chain (1); Compositional bias (1); Disulfide bond (6); Domain (8); Erroneous initiation (1); Glycosylation (3); Modified residue (1); Non-adjacent residues (2); Sequence conflict (4); Signal peptide (1) FUNCTION: Coats the epithelia of the intestines, airways, and other mucus membrane-containing organs. Thought to provide a protective, lubricating barrier against particles and infectious agents at mucosal surfaces. Major constituent of both the inner and outer mucus layers of the colon and may play a role in excluding bacteria from the inner mucus layer. {ECO:0000250|UniProtKB:Q02817, ECO:0000269|PubMed:18806221, ECO:0000269|PubMed:19432394}. PTM: O-glycosylated. {ECO:0000269|PubMed:9886986}.; PTM: May undergo proteolytic cleavage in the outer mucus layer of the colon, contributing to the expanded volume and loose nature of this layer which allows for bacterial colonization in contrast to the inner mucus layer which is dense and devoid of bacteria. {ECO:0000269|PubMed:18806221}.; PTM: May undergo autocatalytic cleavage in vivo triggered by the low pH of the late secretory pathway. {ECO:0000250|UniProtKB:Q02817}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18806221, ECO:0000269|PubMed:19432394}. Note=In the intestine, secreted into the inner and outer mucus layers. SUBUNIT: Homotrimer; disulfide-linked. Dimerizes in the endoplasmic reticulum via its C-terminal region and polymerizes via its N-terminal region by disulfide-linked trimerization (By similarity). Interacts with FCGBP. Interacts with AGR2; disulfide-linked (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in goblet cells of the colon with lower levels in the small intestine and no expression in the stomach (at protein level). {ECO:0000269|PubMed:14984930, ECO:0000269|PubMed:9886986}. +Q80T03 MUC6_MOUSE Mucin-6 (MUC-6) (Gastric mucin-6) (Secreted gel-forming mucin-6) 2850 300,401 Chain (1); Compositional bias (1); Disulfide bond (6); Domain (6); Glycosylation (6); Region (1); Repeat (8); Sequence conflict (2); Signal peptide (1) FUNCTION: May provide a mechanism for modulation of the composition of the protective mucus layer related to acid secretion or the presence of bacteria and noxious agents in the lumen. Plays an important role in the cytoprotection of epithelial surfaces and are used as tumor markers in a variety of cancers. May play a role in epithelial organogenesis. PTM: O-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Multimer; disulfide-linked. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in stomach, duodenum and small intestine. {ECO:0000269|PubMed:12676567, ECO:0000269|PubMed:14984930}. +P28666 MUG2_MOUSE Murinoglobulin-2 (MuG2) 1451 162,382 Chain (1); Cross-link (1); Disulfide bond (10); Glycosylation (8); Region (1); Sequence conflict (3); Signal peptide (1) FUNCTION: A proteinase activates the inhibitor by specific proteolysis in the bait region, which, by an unknown mechanism leads to reaction at the cysteinyl-glutamyl internal thiol ester site and to a conformational change, whereby the proteinase is trapped and/or covalently bound to the inhibitor. While in the tetrameric proteinase inhibitors steric inhibition is sufficiently strong, monomeric forms need a covalent linkage between the activated glutamyl residue of the original thiol ester and a terminal amino group of a lysine or another nucleophilic group on the proteinase, for inhibition to be effective. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Monomer. TISSUE SPECIFICITY: Plasma. +Q8R4V5 OIT3_MOUSE Oncoprotein-induced transcript 3 protein (Liver-specific zona pellucida domain-containing protein) 546 60,316 Alternative sequence (1); Chain (1); Compositional bias (1); Disulfide bond (3); Domain (2); Glycosylation (3); Sequence conflict (5); Signal peptide (1) FUNCTION: May be involved in hepatocellular function and development. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000269|PubMed:15346761}. Note=Secreted into blood in a truncated form. TISSUE SPECIFICITY: Liver-specific. Expressed only in the hepatocytes. {ECO:0000269|PubMed:12939600, ECO:0000269|PubMed:15346761}. +Q60881 OL142_MOUSE Olfactory receptor 142 (Olfactory receptor 227-2) (Olfactory receptor 4C) 305 34,312 Chain (1); Disulfide bond (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 26 46 Helical; Name=1. {ECO:0000255}.; TRANSMEM 56 76 Helical; Name=2. {ECO:0000255}.; TRANSMEM 96 116 Helical; Name=3. {ECO:0000255}.; TRANSMEM 142 162 Helical; Name=4. {ECO:0000255}.; TRANSMEM 203 223 Helical; Name=5. {ECO:0000255}.; TRANSMEM 237 257 Helical; Name=6. {ECO:0000255}.; TRANSMEM 267 287 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 25 Extracellular. {ECO:0000255}.; TOPO_DOM 47 55 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 77 95 Extracellular. {ECO:0000255}.; TOPO_DOM 117 141 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 163 202 Extracellular. {ECO:0000255}.; TOPO_DOM 224 236 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 258 266 Extracellular. {ECO:0000255}.; TOPO_DOM 288 305 Cytoplasmic. {ECO:0000255}. FUNCTION: Odorant receptor. {ECO:0000305}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +P34985 OL143_MOUSE Olfactory receptor 143 (Odorant receptor K18) (Olfactory receptor 170-6) (Olfactory receptor 7A) 313 35,201 Chain (1); Disulfide bond (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 28 48 Helical; Name=1. {ECO:0000255}.; TRANSMEM 60 80 Helical; Name=2. {ECO:0000255}.; TRANSMEM 97 117 Helical; Name=3. {ECO:0000255}.; TRANSMEM 137 157 Helical; Name=4. {ECO:0000255}.; TRANSMEM 209 229 Helical; Name=5. {ECO:0000255}.; TRANSMEM 240 260 Helical; Name=6. {ECO:0000255}.; TRANSMEM 275 295 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 27 Extracellular. {ECO:0000255}.; TOPO_DOM 49 59 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 81 96 Extracellular. {ECO:0000255}.; TOPO_DOM 118 136 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 158 208 Extracellular. {ECO:0000255}.; TOPO_DOM 230 239 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 261 274 Extracellular. {ECO:0000255}.; TOPO_DOM 296 313 Cytoplasmic. {ECO:0000255}. FUNCTION: Odorant receptor. {ECO:0000305}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Olfactory epithelium. +Q60882 OL145_MOUSE Olfactory receptor 145 (Odorant receptor K21) (Olfactory receptor 161-6) (Olfactory receptor 7C) 310 34,451 Chain (1); Disulfide bond (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 28 48 Helical; Name=1. {ECO:0000255}.; TRANSMEM 56 76 Helical; Name=2. {ECO:0000255}.; TRANSMEM 99 119 Helical; Name=3. {ECO:0000255}.; TRANSMEM 141 161 Helical; Name=4. {ECO:0000255}.; TRANSMEM 196 216 Helical; Name=5. {ECO:0000255}.; TRANSMEM 239 259 Helical; Name=6. {ECO:0000255}.; TRANSMEM 271 291 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 27 Extracellular. {ECO:0000255}.; TOPO_DOM 49 55 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 77 98 Extracellular. {ECO:0000255}.; TOPO_DOM 120 140 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 162 195 Extracellular. {ECO:0000255}.; TOPO_DOM 217 238 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 260 270 Extracellular. {ECO:0000255}.; TOPO_DOM 292 310 Cytoplasmic. {ECO:0000255}. FUNCTION: Odorant receptor. {ECO:0000305}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q60884 OL146_MOUSE Olfactory receptor 146 (Odorant receptor M15) (Olfactory receptor 171-10) (Olfactory receptor 7D) 306 34,373 Chain (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 29 49 Helical; Name=1. {ECO:0000255}.; TRANSMEM 57 77 Helical; Name=2. {ECO:0000255}.; TRANSMEM 98 118 Helical; Name=3. {ECO:0000255}.; TRANSMEM 144 164 Helical; Name=4. {ECO:0000255}.; TRANSMEM 197 217 Helical; Name=5. {ECO:0000255}.; TRANSMEM 237 257 Helical; Name=6. {ECO:0000255}.; TRANSMEM 272 292 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 28 Extracellular. {ECO:0000255}.; TOPO_DOM 50 56 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 78 97 Extracellular. {ECO:0000255}.; TOPO_DOM 119 143 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 165 196 Extracellular. {ECO:0000255}.; TOPO_DOM 218 236 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 258 271 Extracellular. {ECO:0000255}.; TOPO_DOM 293 306 Cytoplasmic. {ECO:0000255}. FUNCTION: Odorant receptor. {ECO:0000305}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q60886 OL147_MOUSE Olfactory receptor 147 (Odorant receptor M3) (Olfactory receptor 164-1) (Olfactory receptor 7E) 317 35,358 Chain (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 33 53 Helical; Name=1. {ECO:0000255}.; TRANSMEM 60 80 Helical; Name=2. {ECO:0000255}.; TRANSMEM 98 118 Helical; Name=3. {ECO:0000255}.; TRANSMEM 137 157 Helical; Name=4. {ECO:0000255}.; TRANSMEM 200 220 Helical; Name=5. {ECO:0000255}.; TRANSMEM 243 263 Helical; Name=6. {ECO:0000255}.; TRANSMEM 275 294 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 32 Extracellular. {ECO:0000255}.; TOPO_DOM 54 59 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 81 97 Extracellular. {ECO:0000255}.; TOPO_DOM 119 136 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 158 199 Extracellular. {ECO:0000255}.; TOPO_DOM 221 242 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 264 274 Extracellular. {ECO:0000255}.; TOPO_DOM 295 317 Cytoplasmic. {ECO:0000255}. FUNCTION: Odorant receptor. {ECO:0000305}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q60887 OL148_MOUSE Olfactory receptor 148 (Odorant receptor M30) (Olfactory receptor 224-4) (Olfactory receptor 7F) 310 34,662 Chain (1); Disulfide bond (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 24 44 Helical; Name=1. {ECO:0000255}.; TRANSMEM 56 76 Helical; Name=2. {ECO:0000255}.; TRANSMEM 96 116 Helical; Name=3. {ECO:0000255}.; TRANSMEM 137 157 Helical; Name=4. {ECO:0000255}.; TRANSMEM 203 223 Helical; Name=5. {ECO:0000255}.; TRANSMEM 238 258 Helical; Name=6. {ECO:0000255}.; TRANSMEM 265 285 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 23 Extracellular. {ECO:0000255}.; TOPO_DOM 45 55 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 77 95 Extracellular. {ECO:0000255}.; TOPO_DOM 117 136 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 158 202 Extracellular. {ECO:0000255}.; TOPO_DOM 224 237 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 259 264 Extracellular. {ECO:0000255}.; TOPO_DOM 286 310 Cytoplasmic. {ECO:0000255}. FUNCTION: Odorant receptor. {ECO:0000305}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q8VEX5 OL186_MOUSE Olfactory receptor 186 (Olfactory receptor 183-9) 309 34,902 Chain (1); Disulfide bond (1); Glycosylation (2); Topological domain (8); Transmembrane (7) TRANSMEM 29 49 Helical; Name=1. {ECO:0000255}.; TRANSMEM 57 77 Helical; Name=2. {ECO:0000255}.; TRANSMEM 94 114 Helical; Name=3. {ECO:0000255}.; TRANSMEM 145 165 Helical; Name=4. {ECO:0000255}.; TRANSMEM 199 219 Helical; Name=5. {ECO:0000255}.; TRANSMEM 240 260 Helical; Name=6. {ECO:0000255}.; TRANSMEM 272 292 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 28 Extracellular. {ECO:0000255}.; TOPO_DOM 50 56 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 78 93 Extracellular. {ECO:0000255}.; TOPO_DOM 115 144 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 166 198 Extracellular. {ECO:0000255}.; TOPO_DOM 220 239 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 261 271 Extracellular. {ECO:0000255}.; TOPO_DOM 293 309 Cytoplasmic. {ECO:0000255}. FUNCTION: Potential odorant receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q8VF65 OL470_MOUSE Olfactory receptor 470 (Olfactory receptor 204-22) 314 34,840 Chain (1); Disulfide bond (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 29 49 Helical; Name=1. {ECO:0000255}.; TRANSMEM 58 78 Helical; Name=2. {ECO:0000255}.; TRANSMEM 103 123 Helical; Name=3. {ECO:0000255}.; TRANSMEM 137 157 Helical; Name=4. {ECO:0000255}.; TRANSMEM 200 220 Helical; Name=5. {ECO:0000255}.; TRANSMEM 241 261 Helical; Name=6. {ECO:0000255}.; TRANSMEM 275 295 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 28 Extracellular. {ECO:0000255}.; TOPO_DOM 50 57 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 79 102 Extracellular. {ECO:0000255}.; TOPO_DOM 124 136 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 158 199 Extracellular. {ECO:0000255}.; TOPO_DOM 221 240 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 262 274 Extracellular. {ECO:0000255}.; TOPO_DOM 296 314 Cytoplasmic. {ECO:0000255}. FUNCTION: Potential odorant receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +P53347 ONCM_MOUSE Oncostatin-M (OSM) 263 30,114 Chain (1); Disulfide bond (2); Glycosylation (3); Propeptide (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Growth regulator. Inhibits the proliferation of a number of tumor cell lines. It regulates cytokine production, including IL-6, G-CSF and GM-CSF from endothelial cells (By similarity). Uses only type II OSM receptor (heterodimers composed of OSMR and IL6ST). Involved in the maturation of fetal hepatocytes, thereby promoting liver development and regeneration (By similarity). {ECO:0000250}. PTM: Propeptide processing is not important for receptor binding activity but may be important growth-inhibitory activity. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. +P51879 ONCO_MOUSE Oncomodulin (OM) (Parvalbumin beta) 109 12,260 Calcium binding (2); Chain (1); Domain (2); Initiator methionine (1); Metal binding (9); Modified residue (1) FUNCTION: Has some calmodulin-like activity with respect to enzyme activation and growth regulation. Binds two calcium ions. TISSUE SPECIFICITY: Found in tumor tissues and not detected in normal tissues. +Q3UWY1 OOG3_MOUSE Oogenesin-3 500 57,407 Alternative sequence (1); Chain (1); Repeat (9) TISSUE SPECIFICITY: Expressed in ovary, specifically in oocytes. Detected in follicles with two layers of granulosa cells, and are present in early as well as large antral follicles. {ECO:0000269|PubMed:14675769}. +Q925U0 OOSP1_MOUSE Oocyte-secreted protein 1 (Initiate factor 3) 202 23,013 Alternative sequence (2); Chain (1); Sequence conflict (1); Signal peptide (1) FUNCTION: May be involved in cell differentiation. {ECO:0000269|PubMed:12237121}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Expressed in oocytes in primary through antral-stage follicles. Expressed in liver and ovary. {ECO:0000269|PubMed:11747200, ECO:0000269|PubMed:12237121}. +P58281 OPA1_MOUSE Dynamin-like 120 kDa protein, mitochondrial (EC 3.6.5.5) (Large GTP-binding protein) (LargeG) (Optic atrophy protein 1 homolog) [Cleaved into: Dynamin-like 120 kDa protein, form S1] 960 111,339 Alternative sequence (1); Chain (2); Coiled coil (2); Domain (1); Erroneous initiation (1); Modified residue (1); Nucleotide binding (3); Region (5); Sequence conflict (2); Site (1); Topological domain (2); Transit peptide (1); Transmembrane (1) TRANSMEM 97 113 Helical. {ECO:0000255}. TOPO_DOM 88 96 Mitochondrial matrix. {ECO:0000255}.; TOPO_DOM 114 960 Mitochondrial intermembrane. {ECO:0000255}. FUNCTION: Dynamin-related GTPase that is essential for normal mitochondrial morphology by regulating the equilibrium between mitochondrial fusion and mitochondrial fission (PubMed:11847212, PubMed:24616225, PubMed:26785494, PubMed:28746876). Coexpression of isoform 1 with shorter alternative products is required for optimal activity in promoting mitochondrial fusion (By similarity). Binds lipid membranes enriched in negatively charged phospholipids, such as cardiolipin, and promotes membrane tubulation. The intrinsic GTPase activity is low, and is strongly increased by interaction with lipid membranes (By similarity). Plays a role in remodeling cristae and the release of cytochrome c during apoptosis (PubMed:16839884, PubMed:16839885). Proteolytic processing in response to intrinsic apoptotic signals may lead to disassembly of OPA1 oligomers and release of the caspase activator cytochrome C (CYCS) into the mitochondrial intermembrane space (PubMed:16839884, PubMed:16839885). Plays a role in mitochondrial genome maintenance (By similarity). {ECO:0000250|UniProtKB:O60313, ECO:0000269|PubMed:11847212, ECO:0000269|PubMed:16839884, ECO:0000269|PubMed:16839885, ECO:0000269|PubMed:24616225, ECO:0000269|PubMed:26785494, ECO:0000269|PubMed:28746876}.; FUNCTION: Dynamin-like 120 kDa protein, form S1: Produced by cleavage at position S1 by OMA1 following stress conditions that induce loss of mitochondrial membrane potential, leading to negative regulation of mitochondrial fusion. {ECO:0000269|PubMed:20038678, ECO:0000269|PubMed:22433842}.; FUNCTION: Isoforms that contain the alternative exon 4b (present in isoform 2, but not in isoform 1) are required for mitochondrial genome maintenance, possibly by anchoring the mitochondrial nucleoids to the inner mitochondrial membrane. {ECO:0000250|UniProtKB:O60313}. PTM: PARL-dependent proteolytic processing releases an antiapoptotic soluble form not required for mitochondrial fusion. Cleaved by OMA1 at position S1 following stress conditions (PubMed:20038678, PubMed:22433842). {ECO:0000269|PubMed:20038678, ECO:0000269|PubMed:22433842}.; PTM: Cleavage at position S2 is mediated by YME1L (PubMed:24616225, PubMed:26785494). Cleavage may occur in the sequence motif Leu-Gln-Gln-Gln-Ile-Gln (LQQQIQ) (By similarity). This motif is present in isoform 2, but is absent in the displayed isoform 1. {ECO:0000250|UniProtKB:Q2TA68, ECO:0000269|PubMed:24616225, ECO:0000269|PubMed:26785494, ECO:0000305}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:16839884, ECO:0000269|PubMed:21081504, ECO:0000269|PubMed:28746876}; Single-pass membrane protein {ECO:0000255}. Mitochondrion {ECO:0000269|PubMed:11847212}. Mitochondrion membrane {ECO:0000250|UniProtKB:O60313}. Note=Detected at contact sites between endoplamic reticulum and mitochondrion membranes. {ECO:0000250|UniProtKB:O60313}. SUBUNIT: Oligomeric complex consisting of membrane-bound and soluble forms of OPA1 (PubMed:16839885). Interacts with CHCHD3 and IMMT; these interactions occur preferentially with soluble OPA1 forms (PubMed:21081504). Interacts with RCC1L; this interaction is direct (PubMed:28746876). Binds PARL (PubMed:16839884). Interacts with PRELID1 (By similarity). {ECO:0000250|UniProtKB:O60313, ECO:0000269|PubMed:16839884, ECO:0000269|PubMed:16839885, ECO:0000269|PubMed:21081504, ECO:0000269|PubMed:28746876}. TISSUE SPECIFICITY: Detected in brain (at protein level) (PubMed:11847212). Detected in brain, brain stem, heart, kidney, liver and skeletal muscle (PubMed:11847212). {ECO:0000269|PubMed:11847212}. +Q505D7 OPA3_MOUSE Optic atrophy 3 protein homolog 179 20,110 Chain (1); Coiled coil (1); Mutagenesis (1); Sequence conflict (1) FUNCTION: May play some role in mitochondrial processes. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. +Q7M750 OPALI_MOUSE Opalin (Oligodendrocytic myelin paranodal and inner loop protein) (Transmembrane protein 10) 143 15,833 Chain (1); Glycosylation (3); Mutagenesis (3); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 31 51 Helical. {ECO:0000255}. TOPO_DOM 1 30 Extracellular. {ECO:0000255}.; TOPO_DOM 52 143 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18439243, ECO:0000269|PubMed:18490449}; Single-pass type I membrane protein {ECO:0000269|PubMed:18439243, ECO:0000269|PubMed:18490449}. Note=In the CNS, enriched in the myelin paranodal and inner loop membranes, but not that of the PNS. TISSUE SPECIFICITY: Expressed specifically in oligodendrocytes of the brain. {ECO:0000269|PubMed:17442045, ECO:0000269|PubMed:18439243, ECO:0000269|PubMed:18490449}. +Q61200 NXPH1_MOUSE Neurexophilin-1 271 31,048 Chain (1); Glycosylation (6); Region (4); Sequence conflict (1); Signal peptide (1) FUNCTION: May be signaling molecules that resemble neuropeptides. Ligand for alpha-neurexins. PTM: May be proteolytically processed at the boundary between the N-terminal non-conserved and the central conserved domain in neuron-like cells. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Brain, only in a scattered subpopulation of neurons that probably represent inhibitory interneurons. +Q6PDG8 MON1A_MOUSE Vacuolar fusion protein MON1 homolog A 556 62,131 Alternative sequence (2); Chain (1); Modified residue (5); Natural variant (1) FUNCTION: Plays an important role in membrane trafficking through the secretory apparatus. Not involved in endocytic trafficking to lysosomes (PubMed:17632513). Acts in concert with CCZ1, as a guanine exchange factor (GEF) for RAB7, promotes the exchange of GDP to GTP, converting it from an inactive GDP-bound form into an active GTP-bound form (By similarity). {ECO:0000250|UniProtKB:Q86VX9, ECO:0000269|PubMed:17632513}. SUBUNIT: Interacts with CCZ1. Found in a complex with RMC1, CCZ1 MON1A and MON1B. {ECO:0000250|UniProtKB:Q86VX9}. TISSUE SPECIFICITY: Widely expressed (at protein level). {ECO:0000269|PubMed:17632513}. +Q6PFX7 NYAP1_MOUSE Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 1 833 87,668 Alternative sequence (2); Chain (1); Compositional bias (2); Frameshift (1); Mutagenesis (2); Region (1) FUNCTION: Activates PI3K and concomitantly recruits the WAVE1 complex to the close vicinity of PI3K and regulates neuronal morphogenesis. {ECO:0000269|PubMed:21946561}. PTM: Phosphorylated on tyrosine residues by FYN upon stimulation with CNTN5. Phosphorylation begins at E14, reaches a peak during perinatal days in brain, then gradually decreases. {ECO:0000269|PubMed:21946561}. SUBUNIT: Interacts with ACOT9, ARHGAP26 and PIK3R2. Interacts with components of the WAVE1 complex, CYFIP1 and NCKAP1; this interaction mediates PI3K-WAVE1 association and actin cytoskeleton remodeling. {ECO:0000269|PubMed:21946561}. TISSUE SPECIFICITY: Expressed predominantly in brain where it is present in the neurons, but not in astrocytes or oligodendrites. {ECO:0000269|PubMed:21946561}. +O70451 MOT2_MOUSE Monocarboxylate transporter 2 (MCT 2) (Solute carrier family 16 member 7) 484 52,604 Chain (1); Topological domain (13); Transmembrane (12) TRANSMEM 17 37 Helical. {ECO:0000255}.; TRANSMEM 61 81 Helical. {ECO:0000255}.; TRANSMEM 91 111 Helical. {ECO:0000255}.; TRANSMEM 117 137 Helical. {ECO:0000255}.; TRANSMEM 150 170 Helical. {ECO:0000255}.; TRANSMEM 175 195 Helical. {ECO:0000255}.; TRANSMEM 246 266 Helical. {ECO:0000255}.; TRANSMEM 282 302 Helical. {ECO:0000255}.; TRANSMEM 312 332 Helical. {ECO:0000255}.; TRANSMEM 338 358 Helical. {ECO:0000255}.; TRANSMEM 373 393 Helical. {ECO:0000255}.; TRANSMEM 406 426 Helical. {ECO:0000255}. TOPO_DOM 1 16 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 38 60 Extracellular. {ECO:0000255}.; TOPO_DOM 82 90 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 112 116 Extracellular. {ECO:0000255}.; TOPO_DOM 138 149 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 171 174 Extracellular. {ECO:0000255}.; TOPO_DOM 196 245 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 267 281 Extracellular. {ECO:0000255}.; TOPO_DOM 303 311 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 333 337 Extracellular. {ECO:0000255}.; TOPO_DOM 359 372 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 394 405 Extracellular. {ECO:0000255}.; TOPO_DOM 427 484 Cytoplasmic. {ECO:0000255}. FUNCTION: Proton-coupled monocarboxylate transporter. Catalyzes the rapid transport across the plasma membrane of many monocarboxylates such as lactate, pyruvate, branched-chain oxo acids derived from leucine, valine and isoleucine, and the ketone bodies acetoacetate, beta-hydroxybutyrate and acetate. Functions as high-affinity pyruvate transporter. {ECO:0000269|PubMed:21792931}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with GRID2IP. Interacts with BSG. {ECO:0000269|PubMed:17496809, ECO:0000269|PubMed:21792931}. TISSUE SPECIFICITY: Detected in testis and in spermatozoa (at protein level). {ECO:0000269|PubMed:21792931}. +Q8K1C7 MOT14_MOUSE Monocarboxylate transporter 14 (MCT 14) (Solute carrier family 16 member 14) 512 56,476 Chain (1); Erroneous initiation (2); Topological domain (2); Transmembrane (12) TRANSMEM 30 50 Helical. {ECO:0000255}.; TRANSMEM 76 96 Helical. {ECO:0000255}.; TRANSMEM 105 125 Helical. {ECO:0000255}.; TRANSMEM 129 149 Helical. {ECO:0000255}.; TRANSMEM 161 181 Helical. {ECO:0000255}.; TRANSMEM 193 211 Helical. {ECO:0000255}.; TRANSMEM 317 337 Helical. {ECO:0000255}.; TRANSMEM 355 375 Helical. {ECO:0000255}.; TRANSMEM 381 401 Helical. {ECO:0000255}.; TRANSMEM 410 430 Helical. {ECO:0000255}.; TRANSMEM 446 466 Helical. {ECO:0000255}.; TRANSMEM 476 496 Helical. {ECO:0000255}. TOPO_DOM 1 29 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 497 512 Cytoplasmic. {ECO:0000255}. FUNCTION: Proton-linked monocarboxylate transporter. May catalyze the transport of monocarboxylates across the plasma membrane. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q6P7F1 MPP4_MOUSE MAGUK p55 subfamily member 4 (Discs large homolog 6) (mDLG6) 635 72,001 Alternative sequence (4); Chain (1); Coiled coil (1); Domain (5); Erroneous initiation (4); Frameshift (2); Sequence caution (1); Sequence conflict (25) FUNCTION: May play a role in retinal photoreceptors development. {ECO:0000269|PubMed:12859944}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12859944, ECO:0000269|PubMed:15558731}. Note=Localized at photoreceptor synaptic terminals in retina. Localized in rod and cone photoreceptors at the plasma membrane and at membranes of intracellular vesicles around the subapical region (SAR) and adherens junction, and in the outer plexiform layer (OPL). SUBUNIT: May interact with GRIA2 (By similarity). Interacts with MPDZ. Forms a complex with CRB1 and MPP5. Interacts with FASLG (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Detected in the retina (at protein level). Highly enriched in the retina where it is mainly expressed by rod photoreceptors; detected in the inner segment of the photoreceptor layer and in the outer nuclear layer. Also detected at much lower levels in pineal gland, cerebellum, cortex, hippocampus, olfactory bulb, heart, liver and spleen. Expressed in the CA1-CA3 regions of pyramidal cell layers and in the granule cell layer of dentate gyrus in the hippocampus. In the cerebellum, expressed in Purkinje cells and throughout the granule cell layer. In the olfactory bulb, expressed in mitral cells. {ECO:0000269|PubMed:12127943, ECO:0000269|PubMed:12384283, ECO:0000269|PubMed:12859944, ECO:0000269|PubMed:15558731}. +P54276 MSH6_MOUSE DNA mismatch repair protein Msh6 (G/T mismatch-binding protein) (GTBP) (GTMBP) (MutS protein homolog 6) (MutS-alpha 160 kDa subunit) (p160) 1358 151,084 Chain (1); Compositional bias (1); Domain (1); Modified residue (23); Nucleotide binding (1); Sequence conflict (7) FUNCTION: Component of the post-replicative DNA mismatch repair system (MMR). Heterodimerizes with MSH2 to form MutS alpha, which binds to DNA mismatches thereby initiating DNA repair. When bound, MutS alpha bends the DNA helix and shields approximately 20 base pairs, and recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. After mismatch binding, forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. ATP binding and hydrolysis play a pivotal role in mismatch repair functions. The ATPase activity associated with MutS alpha regulates binding similar to a molecular switch: mismatched DNA provokes ADP-->ATP exchange, resulting in a discernible conformational transition that converts MutS alpha into a sliding clamp capable of hydrolysis-independent diffusion along the DNA backbone. This transition is crucial for mismatch repair. MutS alpha may also play a role in DNA homologous recombination repair. Recruited on chromatin in G1 and early S phase via its PWWP domain that specifically binds trimethylated 'Lys-36' of histone H3 (H3K36me3): early recruitment to chromatin to be replicated allowing a quick identification of mismatch repair to initiate the DNA mismatch repair reaction (By similarity). {ECO:0000250|UniProtKB:P52701}. PTM: Phosphorylated by PRKCZ, which may prevent MutS alpha degradation by the ubiquitin-proteasome pathway. {ECO:0000250|UniProtKB:P52701}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P52701}. Chromosome {ECO:0000250|UniProtKB:P52701}. Note=Associates with H3K36me3 via its PWWP domain. {ECO:0000250|UniProtKB:P52701}. SUBUNIT: Component of the DNA mismatch repair (MMR) complex composed at least of MSH2, MSH3, MSH6, PMS1 and MLH1. Heterodimer consisting of MSH2-MSH6 (MutS alpha). Forms a ternary complex with MutL alpha (MLH1-PMS1). Interacts with MCM9. Part of the BRCA1-associated genome surveillance complex (BASC), which contains BRCA1, MSH2, MSH6, MLH1, ATM, BLM, PMS2 and the RAD50-MRE11-NBS1 protein complex. This association could be a dynamic process changing throughout the cell cycle and within subnuclear domains. {ECO:0000250|UniProtKB:P52701}. DOMAIN: The PWWP domain specifically recognizes and binds trimethylated 'Lys-36' of histone H3 (H3K36me3). {ECO:0000250|UniProtKB:P52701}. +Q01727 MSHR_MOUSE Melanocyte-stimulating hormone receptor (MSH-R) (Melanocortin receptor 1) (MC1-R) 315 35,226 Chain (1); Glycosylation (2); Lipidation (1); Sequence conflict (2); Topological domain (8); Transmembrane (7) TRANSMEM 36 61 Helical; Name=1. {ECO:0000255}.; TRANSMEM 71 91 Helical; Name=2. {ECO:0000255}.; TRANSMEM 117 138 Helical; Name=3. {ECO:0000255}.; TRANSMEM 162 181 Helical; Name=4. {ECO:0000255}.; TRANSMEM 190 209 Helical; Name=5. {ECO:0000255}.; TRANSMEM 239 264 Helical; Name=6. {ECO:0000255}.; TRANSMEM 278 298 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 35 Extracellular. {ECO:0000255}.; TOPO_DOM 62 70 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 92 116 Extracellular. {ECO:0000255}.; TOPO_DOM 139 161 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 182 189 Extracellular. {ECO:0000255}.; TOPO_DOM 210 238 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 265 277 Extracellular. {ECO:0000255}.; TOPO_DOM 299 315 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for MSH (alpha, beta and gamma) and ACTH. The activity of this receptor is mediated by G proteins which activate adenylate cyclase. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBUNIT: Interacts with MGRN1, but does not undergo MGRN1-mediated ubiquitination; this interaction competes with GNAS-binding and thus inhibits agonist-induced cAMP production. {ECO:0000250}. TISSUE SPECIFICITY: Melanocytes and corticoadrenal tissue. +Q920Q6 MSI2H_MOUSE RNA-binding protein Musashi homolog 2 (Musashi-2) 346 36,939 Alternative sequence (3); Chain (1); Compositional bias (1); Domain (2); Modified residue (4) FUNCTION: RNA binding protein that regulates the expression of target mRNAs at the translation level. May play a role in the proliferation and maintenance of stem cells in the central nervous system. {ECO:0000269|PubMed:11588182, ECO:0000269|PubMed:12407178}. PTM: Phosphorylated. {ECO:0000269|PubMed:11588182}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11588182}. Note=Associated with polysomes. TISSUE SPECIFICITY: Ubiquitous. Expressed in proliferating neural precursor cells. {ECO:0000269|PubMed:11588182, ECO:0000269|PubMed:12923295}. +Q61468 MSLN_MOUSE Mesothelin (Pre-pro-megakaryocyte-potentiating factor) [Cleaved into: Megakaryocyte-potentiating factor (MPF); Mesothelin, cleaved form] 625 69,423 Chain (3); Disulfide bond (1); Glycosylation (4); Lipidation (1); Modified residue (1); Propeptide (1); Signal peptide (1) FUNCTION: Membrane-anchored forms may play a role in cellular adhesion. {ECO:0000269|PubMed:10733593, ECO:0000269|PubMed:14676194}.; FUNCTION: Megakaryocyte-potentiating factor (MPF) may potentiate megakaryocyte colony formation. {ECO:0000250}. PTM: Proteolytically cleaved by a furin-like convertase to generate megakaryocyte-potentiating factor (MPF), and the cleaved form of mesothelin. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. Golgi apparatus {ECO:0000250}.; SUBCELLULAR LOCATION: Megakaryocyte-potentiating factor: Secreted {ECO:0000250}. SUBUNIT: Interacts with MUC16. {ECO:0000269|PubMed:14676194}. TISSUE SPECIFICITY: Highly expressed in lung and heart. Expressed at low levels in spleen, liver, kidney and testis. Present in lung (at protein level). {ECO:0000269|PubMed:10733593}. +B1AWI6 MSMP_MOUSE Prostate-associated microseminoprotein (PC3-secreted microprotein homolog) 139 14,981 Chain (1); Disulfide bond (5); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +Q9CQL0 MT21A_MOUSE Protein N-lysine methyltransferase METTL21A (EC 2.1.1.-) (Methyltransferase-like protein 21A) 218 24,286 Binding site (4); Chain (1); Region (1); Sequence conflict (1) FUNCTION: Protein-lysine methyltransferase that selectively trimethylates residues in heat shock protein 70 (HSP70) family members. Contributes to the in vivo trimethylation of Lys residues in HSPA1 and HSPA8. In vitro methylates 'Lys-561' in HSPA1, 'Lys-564' in HSPA2, 'Lys-585' in HSPA5, 'Lys-563' in HSPA6 and 'Lys-561' in HSPA8 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with heat shock 70 family members; these proteins probably are methylation substrates. {ECO:0000250}. +Q8BLU2 MT21C_MOUSE Protein-lysine methyltransferase METTL21C (EC 2.1.1.-) (Methyltransferase-like protein 21C) 248 27,892 Binding site (3); Chain (1); Region (1) FUNCTION: Protein-lysine methyltransferase. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with members of the heat shock protein 70 families; these proteins may possibly be methylation substrates for the enzyme. {ECO:0000250}. +Q8C436 MT21D_MOUSE Protein-lysine methyltransferase METTL21D (EC 2.1.1.-) (Methyltransferase-like protein 21D) (VCP lysine methyltransferase) (VCP-KMT) (Valosin-containing protein lysine methyltransferase) 228 25,535 Alternative sequence (1); Binding site (4); Chain (1); Initiator methionine (1); Modified residue (1); Region (1) FUNCTION: Protein-lysine N-methyltransferase that specifically trimethylates 'Lys-315' of VCP/p97; this modification may decrease VCP ATPase activity. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with ALKBH6. Interacts with ASPSCR1 and UBXN6; interaction with ASPSCR1, but not with UBXN6, enhances VCP methylation. {ECO:0000250}. +P0C913 OCC1_MOUSE Overexpressed in colon carcinoma 1 protein homolog (OCC-1) 63 6,453 Chain (1) +Q8VCR9 OCEL1_MOUSE Occludin/ELL domain-containing protein 1 219 25,111 Chain (1); Sequence conflict (6) +P20357 MTAP2_MOUSE Microtubule-associated protein 2 (MAP-2) 1828 199,132 Chain (1); Modified residue (50); Region (2); Repeat (3); Sequence conflict (12) FUNCTION: The exact function of MAP2 is unknown but MAPs may stabilize the microtubules against depolymerization. They also seem to have a stiffening effect on microtubules. PTM: Phosphorylated at serine residues in K-X-G-S motifs by causing MAP/microtubule affinity-regulating kinase (MARK1 or MARK2), detachment from microtubules, and their disassembly (By similarity). The interaction with KNDC1 enhances MAP2 threonine phosphorylation (PubMed:17984326). {ECO:0000250|UniProtKB:P15146, ECO:0000269|PubMed:17984326}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. Cell projection, dendrite {ECO:0000269|PubMed:17984326}. SUBUNIT: Interacts with KNDC1 (via KIND2); the interaction enhances MAP2 phosphorylation and localizes KNDC1 to dendrites. {ECO:0000269|PubMed:17984326}. +O70374 MTG8R_MOUSE Protein CBFA2T2 (MTG8-like protein) (MTG8-related protein 1) 594 65,904 Alternative sequence (1); Chain (1); Coiled coil (1); Compositional bias (1); Cross-link (2); Domain (1); Helix (4); Modified residue (4); Mutagenesis (9); Region (3); Sequence conflict (3); Zinc finger (1) FUNCTION: Transcriptional corepressor which facilitates transcriptional repression via its association with DNA-binding transcription factors and recruitment of other corepressors and histone-modifying enzymes. Via association with PRDM14 is involved in regulation of embryonic stem cell (ESC) pluripotency. Involved in primordial germ cell (PCG) formation (PubMed:27281218). Stabilizes PRDM14 and OCT4 on chromatin in a homooligomerization-dependent mannerCan repress the expression of MMP7 in a ZBTB33-dependent manner (By similarity). Through heteromerization with CBFA2T3/MTG16 may be involved in regulation of the proliferation and the differentiation of erythroid progenitors by repressing the expression of TAL1 target genes (PubMed:19799863). Required for the maintenance of the secretory cell lineage in the small intestine (PubMed:16227606). Can inhibit Notch signaling probably by association with RBPJ and may be involved in GFI1-mediated Paneth cell differentiation (PubMed:25398765). {ECO:0000250|UniProtKB:O43439, ECO:0000269|PubMed:16227606, ECO:0000269|PubMed:25398765, ECO:0000269|PubMed:27281218}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00440}. SUBUNIT: Homooligomer. Homotetramerization is mediated by the NHR2 domain. Interacts with CBFA2T3/MTG16 (PubMed:19799863). Can interact with RUNX1T1/CBFA2T1. Heterotetramerization between members of the CBFA2T family is proposed (By similarity). Interacts with RBP, GFI1, TCF4, PRDM14 (PubMed:25398765, PubMed:18039847, PubMed:27281218). Interacts with TAL1 and CBFA2T3/MTG16; the heteromer with CBFA2T3/MTG16 may function in repression of TAL1 (PubMed:19799863). {ECO:0000250|UniProtKB:O43439, ECO:0000269|PubMed:18039847, ECO:0000269|PubMed:19799863, ECO:0000269|PubMed:25398765, ECO:0000269|PubMed:27281218}. DOMAIN: Nervy homology region 2 (NHR2) mediates homo- and possibly heterotypic oligomerization by forming a four-helix bundle tetrameric structure. {ECO:0000250|UniProtKB:Q06455}. TISSUE SPECIFICITY: Expressed in embryonic stem cells. {ECO:0000269|PubMed:26523391}. DISEASE: Note=Required for tumorigenesis in a AOM/DSS colitis-associated carcinoma model. May be involved in intestinal tumorigenesis. {ECO:0000269|PubMed:21303973}. +Q8BMF4 ODP2_MOUSE Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial (EC 2.3.1.12) (Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex) (Pyruvate dehydrogenase complex component E2) (PDC-E2) (PDCE2) 642 67,942 Active site (2); Chain (1); Domain (3); Modified residue (6); Region (2); Sequence conflict (5); Transit peptide (1) FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle. {ECO:0000250}. PTM: Delipoylated at Lys-131 and Lys-258 by SIRT4, delipoylation decreases the PHD complex activity. {ECO:0000250|UniProtKB:P10515}. SUBCELLULAR LOCATION: Mitochondrion matrix. SUBUNIT: Part of the multimeric pyruvate dehydrogenase complex that contains multiple copies of pyruvate dehydrogenase (subunits PDH1A and PDHB, E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3). These subunits are bound to an inner core composed of about 48 DLAT and 12 PDHX molecules. Interacts with PDK2 and PDK3. Interacts with SIRT4. Interacts with PDHB. {ECO:0000250|UniProtKB:P10515}. +Q9Z2C4 MTMR1_MOUSE Myotubularin-related protein 1 (Phosphatidylinositol-3,5-bisphosphate 3-phosphatase) (EC 3.1.3.95) (Phosphatidylinositol-3-phosphate phosphatase) (EC 3.1.3.64) 669 75,313 Active site (1); Binding site (1); Chain (1); Domain (2); Modified residue (3); Region (4) FUNCTION: Lipid phosphatase that has high specificity for phosphatidylinositol 3-phosphate and has no activity with phosphatidylinositol 4-phosphate, phosphatidylinositol (4,5)-bisphosphate and phosphatidylinositol (3,4,5)-trisphosphate (PubMed:12217958). Activity with phosphatidylinositol (3,5)-bisphosphate is controversial; it has been shown for the human ortholog (By similarity). In contrast, PubMed:12217958 find no activity with this substrate. {ECO:0000250|UniProtKB:Q13613, ECO:0000269|PubMed:12217958}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12217958}; Peripheral membrane protein {ECO:0000269|PubMed:12217958}; Cytoplasmic side {ECO:0000269|PubMed:12217958}. Cytoplasm {ECO:0000269|PubMed:12217958}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q13613}. DOMAIN: The C-terminal region is required for dimerization. {ECO:0000250|UniProtKB:Q13613}. TISSUE SPECIFICITY: Widely expressed. Detected in skeletal muscle, heart, lung, liver and brain. {ECO:0000269|PubMed:12217958}. +Q8BT35 MTLN_MOUSE Mitoregulin (Small integral membrane protein 37) 56 6,529 Chain (1); Initiator methionine (1); Topological domain (2); Transmembrane (1) TRANSMEM 10 27 Helical. {ECO:0000255}. TOPO_DOM 2 9 Mitochondrial matrix. {ECO:0000305|PubMed:29949756}.; TOPO_DOM 28 56 Mitochondrial intermembrane. {ECO:0000305|PubMed:29949756}. FUNCTION: Positively regulates mitochondrial complex assembly and/or stability (PubMed:29949756). Increases mitochondrial membrane potential and mitochondrial respiration rate while decreasing mitochondrial reactive oxygen species (By similarity). Also increases mitochondrial calcium retention capacity (PubMed:29949756). {ECO:0000250|UniProtKB:Q8NCU8, ECO:0000269|PubMed:29949756}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:29949756}; Single-pass membrane protein {ECO:0000305}. Note=Preferentially binds to cardiolipin relative to other common cell membrane lipids. {ECO:0000269|PubMed:29949756}. TISSUE SPECIFICITY: Enriched in heart, skeletal muscle and adipose tissue with lower levels detected in liver, pancreas and brain (at protein level). {ECO:0000269|PubMed:29949756}. +Q9CRB8 MTFP1_MOUSE Mitochondrial fission process protein 1 (Mitochondrial 18 kDa protein) (MTP18) 166 18,314 Chain (1); Modified residue (1); Sequence conflict (1); Transmembrane (3) TRANSMEM 34 54 Helical. {ECO:0000255}.; TRANSMEM 78 98 Helical. {ECO:0000255}.; TRANSMEM 129 149 Helical. {ECO:0000255}. FUNCTION: Involved in the mitochondrial division probably by regulating membrane fission. Loss-of-function leads to apoptosis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8K296 MTMR3_MOUSE Myotubularin-related protein 3 (EC 3.1.3.48) (Phosphatidylinositol-3,5-bisphosphate 3-phosphatase) (EC 3.1.3.95) (Phosphatidylinositol-3-phosphate phosphatase) (EC 3.1.3.64) 1196 133,840 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Coiled coil (1); Domain (1); Erroneous gene model prediction (1); Modified residue (7); Region (3); Sequence conflict (2); Zinc finger (1) FUNCTION: Phosphatase that acts on lipids with a phosphoinositol headgroup. Has phosphatase activity towards phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5-bisphosphate. May also dephosphorylate proteins phosphorylated on Ser, Thr, and Tyr residues (By similarity). {ECO:0000250|UniProtKB:Q13615}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13615}. Membrane {ECO:0000250|UniProtKB:Q13615}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q13615}. +Q91XS1 MTMR4_MOUSE Myotubularin-related protein 4 (EC 3.1.3.48) 1190 132,885 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Coiled coil (1); Domain (1); Modified residue (3); Region (3); Zinc finger (1) FUNCTION: Dephosphorylates proteins phosphorylated on Ser, Thr, and Tyr residues and low molecular weight phosphatase substrate para-nitrophenylphosphate. Phosphorylates phosphatidylinositol 3,4,5-trisphosphate (PIP3) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Localized to perinuclear region. {ECO:0000250}. +Q6ZPE2 MTMR5_MOUSE Myotubularin-related protein 5 (SET-binding factor 1) (Sbf1) 1867 208,693 Alternative sequence (1); Beta strand (9); Chain (1); Domain (6); Erroneous initiation (2); Helix (2); Modified residue (4); Sequence conflict (3); Turn (2) FUNCTION: Probable pseudophosphatase. Lacks several amino acids in the catalytic pocket which renders it catalytically inactive as a phosphatase. The pocket is however sufficiently preserved to bind phosphorylated substrates, and maybe protect them from phosphatases. Inhibits myoblast differentiation in vitro and induces oncogenic transformation in fibroblasts. Alternatively proposed to function as a guanine nucleotide exchange factor (GEF) activating RAB28. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with the SET domain of KMT2A/MLL1. Interacts with SUV39H1 (By similarity). {ECO:0000250}. +Q9WVP6 PAPOB_MOUSE Poly(A) polymerase beta (PAP-beta) (EC 2.7.7.19) (Polynucleotide adenylyltransferase beta) (Testis-specific poly(A) polymerase) 641 72,198 Binding site (4); Chain (1); Erroneous initiation (1); Metal binding (5); Nucleotide binding (3); Sequence conflict (1); Site (4) SUBCELLULAR LOCATION: Cytoplasm. Nucleus. SUBUNIT: Interacts with GSG1. {ECO:0000269|PubMed:18325338}. TISSUE SPECIFICITY: Testis specific. {ECO:0000269|PubMed:11150526}. +Q6PCL9 PAPOG_MOUSE Poly(A) polymerase gamma (PAP-gamma) (EC 2.7.7.19) (Polynucleotide adenylyltransferase gamma) (SRP RNA 3'-adenylating enzyme) (Signal recognition particle RNA-adenylating enzyme) (SRP RNA-adenylating enzyme) 739 82,957 Binding site (4); Chain (1); Metal binding (5); Modified residue (7); Nucleotide binding (3); Sequence conflict (1); Site (5) FUNCTION: Responsible for the post-transcriptional adenylation of the 3'-terminal of mRNA precursors and several small RNAs including signal recognition particle (SRP) RNA, nuclear 7SK RNA, U2 small nuclear RNA, and ribosomal 5S RNA. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BWT3}. +Q8CEE6 PASK_MOUSE PAS domain-containing serine/threonine-protein kinase (PAS-kinase) (PASKIN) (EC 2.7.11.1) 1383 151,250 Active site (1); Binding site (2); Chain (1); Domain (3); Modified residue (6); Nucleotide binding (2); Sequence conflict (7) FUNCTION: Serine/threonine-protein kinase involved in energy homeostasis and protein translation. Phosphorylates EEF1A1, GYS1, PDX1 and RPS6. Probably plays a role under changing environmental conditions (oxygen, glucose, nutrition), rather than under standard conditions. Acts as a sensor involved in energy homeostasis: regulates glycogen synthase synthesis by mediating phosphorylation of GYS1, leading to GYS1 inactivation. May be involved in glucose-stimulated insulin production in pancreas and regulation of glucagon secretion by glucose in alpha cells; however such data require additional evidences. May play a role in regulation of protein translation by phosphorylating EEF1A1, leading to increase translation efficiency. May also participate to respiratory regulation. {ECO:0000269|PubMed:15148392, ECO:0000269|PubMed:17878307, ECO:0000269|PubMed:18509100, ECO:0000269|PubMed:21181396}. PTM: Autophosphorylated on Thr-1221 and Thr-1225. Autophosphorylation is activated by phospholipids (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Localizes in the nucleus of testis germ cells and in the midpiece of sperm tails. {ECO:0000250}. DOMAIN: The protein kinase domain mediates binding to phosphatidylinositol. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed. Strongly up-regulated in postmeiotic germ cells during spermatogenesis. {ECO:0000269|PubMed:12972598}. +P03966 MYCN_MOUSE N-myc proto-oncogene protein 462 49,572 Chain (1); Compositional bias (1); Domain (1); Modified residue (2); Region (3); Sequence conflict (5) FUNCTION: Positively regulates the transcription of MYCNOS in neuroblastoma cells. {ECO:0000250|UniProtKB:P04198}. PTM: Phosphorylated by GSK3-beta which may promote its degradation. Phosphorylated by AURKA. {ECO:0000250|UniProtKB:P04198}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Efficient DNA binding requires dimerization with another bHLH protein. Binds DNA as a heterodimer with MAX. Interacts with KDM5A, KDM5B and HUWE1. Interacts with MYCNOS. Interacts with AURKA; interaction is phospho-independent and triggers AURKA activation; AURKA competes with FBXW7 for binding to unphosphorylated MYCN but not for binding to unphosphorylated MYCN. Interacts with FBXW7; FBXW7 competes with AURKA for binding to unphosphorylated MYCN but not for binding to phosphorylated MYCN. {ECO:0000250|UniProtKB:P04198}. +Q8BM54 MYLIP_MOUSE E3 ubiquitin-protein ligase MYLIP (EC 2.3.2.27) (Inducible degrader of the LDL-receptor) (Idol) (Myosin regulatory light chain-interacting protein) (MIR) (RING-type E3 ubiquitin transferase MYLIP) 445 49,849 Alternative sequence (1); Chain (1); Domain (1); Metal binding (3); Mutagenesis (1); Region (1); Sequence conflict (1); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of myosin regulatory light chain (MRLC), LDLR, VLDLR and LRP8. Activity depends on E2 enzymes of the UBE2D family. Proteasomal degradation of MRLC leads to inhibit neurite outgrowth in presence of NGF by counteracting the stabilization of MRLC by saposin-like protein (CNPY2/MSAP) and reducing CNPY2-stimulated neurite outgrowth. Acts as a sterol-dependent inhibitor of cellular cholesterol uptake by mediating ubiquitination and subsequent degradation of LDLR. {ECO:0000269|PubMed:19520913, ECO:0000269|PubMed:20427281}. PTM: Autoubiquitinated. {ECO:0000305|PubMed:19520913}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Cell membrane {ECO:0000250|UniProtKB:Q8WY64}; Peripheral membrane protein. SUBUNIT: Homodimer. Interacts with the E2 ubiquitin-conjugating enzyme, UBE2D1 (via RING-type zinc finger). Interacts with myosin regulatory light chain (MRLC) and TMEM4. {ECO:0000250|UniProtKB:Q8WY64}. DOMAIN: The RING domain mediates ubiquitination and the neurite outgrowth inhibitory activity. {ECO:0000250}.; DOMAIN: The FERM domain binds phospholipids and mediates lipoprotein receptors recognition at the plasma membrane through their cytoplasmic tails. {ECO:0000250}.; DOMAIN: The RING-type zinc finger mediates the interaction with UBE2D E2 enzymes. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in liver, spleen, intestine and adrenals. {ECO:0000269|PubMed:19520913}. +O70468 MYPC3_MOUSE Myosin-binding protein C, cardiac-type (Cardiac MyBP-C) (C-protein, cardiac muscle isoform) 1270 140,632 Beta strand (9); Chain (1); Compositional bias (1); Disulfide bond (1); Domain (10); Helix (2); Metal binding (4); Modified residue (12); Sequence conflict (10); Turn (2) FUNCTION: Thick filament-associated protein located in the crossbridge region of vertebrate striated muscle a bands. In vitro it binds MHC, F-actin and native thin filaments, and modifies the activity of actin-activated myosin ATPase. It may modulate muscle contraction or may play a more structural role. PTM: Substrate for phosphorylation by PKA and PKC. Reversible phosphorylation appears to modulate contraction (By similarity). {ECO:0000250}.; PTM: Polyubiquitinated. {ECO:0000250|UniProtKB:Q14896}. +Q497P3 NUPR2_MOUSE Nuclear protein 2 (Nuclear transcriptional regulator 1-like protein) (Nuclear transcriptional regulator protein 2) 102 11,767 Chain (1); Frameshift (1); Sequence conflict (1) FUNCTION: Acts as a transcriptional repressor by inhibiting gene expression at the NUPR1 promoter in a p53/TP53-dependent manner in cancer cells. Involved in the G1 cell cycle arrest, and in a decrease in cell viability and cell proliferation of pancreatic cancer cells. Plays a role as a negative regulator of the protumoral factor NUPR1. {ECO:0000250|UniProtKB:A6NF83}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:A6NF83}. +Q9ERH4 NUSAP_MOUSE Nucleolar and spindle-associated protein 1 (NuSAP) 427 48,573 Alternative sequence (1); Chain (1); Coiled coil (1); Modified residue (9); Motif (1); Region (1); Sequence conflict (6) FUNCTION: Microtubule-associated protein with the capacity to bundle and stabilize microtubules. May associate with chromosomes and promote the organization of mitotic spindle microtubules around them. {ECO:0000269|PubMed:12963707, ECO:0000269|PubMed:17276916}. PTM: Ubiquitinated. Ubiquitination by FZR1 may lead to proteasome-dependent degradation of this protein (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus. Cytoplasm, cytoskeleton, spindle. Chromosome. Note=Found in the cytoplasm and nucleolus during interphase and redistributes to the mitotic spindle in prometaphase. Localizes to the mitotic spindle and to the chromosomes during anaphase and telophase then disappears from around the chromosomes during cytokinesis. SUBUNIT: Interacts with DNA and microtubules. Microtubule bundling is inhibited by IPO7, KPNA2 and KPNB1 while association with DNA is also inhibited by IPO7 and KPNA2. DOMAIN: The KEN box is required for the FZR1-dependent degradation of this protein subsequent to ubiquitination. {ECO:0000250}. +Q8BTP3 MO2R5_MOUSE Cell surface glycoprotein CD200 receptor 5 (CD200 cell surface glycoprotein receptor-like 5) (CD200 receptor-like 5) (CD200 cell surface glycoprotein receptor-like e) (CD200RLe) (Cell surface glycoprotein OX2 receptor 5) 270 29,528 Chain (1); Disulfide bond (2); Domain (2); Glycosylation (3); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 242 262 Helical. {ECO:0000255}. TOPO_DOM 26 241 Extracellular. {ECO:0000255}.; TOPO_DOM 263 270 Cytoplasmic. {ECO:0000255}. FUNCTION: May not be a receptor for the CD200/OX2 cell surface glycoprotein. {ECO:0000269|PubMed:16081818}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +P60762 MO4L1_MOUSE Mortality factor 4-like protein 1 (MORF-related gene 15 protein) (Testis-expressed gene 189 protein) (Transcription factor-like protein MRG15) 362 41,493 Alternative sequence (1); Chain (1); Domain (1); Modified residue (1); Motif (1); Region (5) FUNCTION: Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. The NuA4 complex ATPase and helicase activities seem to be, at least in part, contributed by the association of RUVBL1 and RUVBL2 with EP400. NuA4 may also play a direct role in DNA repair when directly recruited to sites of DNA damage. Also component of the mSin3A complex which acts to repress transcription by deacetylation of nucleosomal histones. Required for homologous recombination repair (HRR) and resistance to mitomycin C (MMC). Involved in the localization of PALB2, BRCA2 and RAD51, but not BRCA1, to DNA-damage foci (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00972}. SUBUNIT: Component of the NuA4 histone acetyltransferase complex which contains the catalytic subunit KAT5/TIP60 and the subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6. The NuA4 complex interacts with MYC. MORF4L1 may also participate in the formation of NuA4 related complexes which lack the KAT5/TIP60 catalytic subunit, but which include the SWI/SNF related protein SRCAP. Component of the mSin3A histone deacetylase complex, which includes SIN3A, HDAC2, ARID4B, MORF4L1, RBBP4/RbAp48, and RBBP7/RbAp46. Interacts with RB1 and KAT8. May also interact with PHF12 and one or more as yet undefined members of the TLE (transducin-like enhancer of split) family of transcriptional repressors. Interacts with the N-terminus of MRFAP1 (By similarity). Found in a complex composed of MORF4L1, MRFAP1 and RB1. Interacts with the entire BRCA complex, which contains BRCA1, PALB2, BRCA2 and RAD51. Interacts with PALB2 (By similarity). Forms a complex with MSL1 and NUPR1 (By similarity). {ECO:0000250}. +Q8VC33 NXNL1_MOUSE Nucleoredoxin-like protein 1 (Rod-derived cone viability factor) (RdCVF) (Thioredoxin-like protein 6) 217 24,912 Chain (1); Domain (1) FUNCTION: May play a role in cone cell viability, slowing down cone degeneration, does not seem to play a role in degenerating rods. {ECO:0000269|PubMed:15220920}. SUBCELLULAR LOCATION: Nucleus outer membrane {ECO:0000269|PubMed:15220920}. TISSUE SPECIFICITY: Retina-specific. Expressed predominantly by photoreceptors, expression mainly restricted to the outer nuclear layer containing the rods and cones. +Q9D531 NXNL2_MOUSE Nucleoredoxin-like protein 2 (Rod-derived cone viability factor 2) (RdCVF2) 156 17,620 Alternative sequence (2); Chain (1); Domain (1) FUNCTION: May be involved in the maintenance of both the function and the viability of sensory neurons, including photoreceptors and olfactory neurons. In the retina, isoform 1 may be required for rod function and isoform 2 for cone viability and function. {ECO:0000269|PubMed:22343139}. TISSUE SPECIFICITY: Both isoforms are expressed in retina, in the photoreceptor layer, and throughout the olfactory sensory neuron layer of the nasal epithelium, in neurons. Also expressed at low levels in brain and testis. {ECO:0000269|PubMed:17764561, ECO:0000269|PubMed:22343139}. +Q9D3S5 NXRD1_MOUSE NADP-dependent oxidoreductase domain-containing protein 1 (EC 1.-.-.-) (Pyrroline-5-carboxylate reductase-like protein C14orf148 homolog) 366 41,666 Chain (1) FUNCTION: Probable oxidoreductase. {ECO:0000250}. +P00536 MOS_MOUSE Proto-oncogene serine/threonine-protein kinase mos (EC 2.7.11.1) (Oocyte maturation factor mos) (Proto-oncogene c-Mos) 390 42,875 Active site (1); Binding site (1); Chain (1); Domain (1); Nucleotide binding (1); Sequence conflict (6) TISSUE SPECIFICITY: Expressed specifically in testis during spermatogenesis. +Q91ZC1 MRGB3_MOUSE Mas-related G-protein coupled receptor member B3 312 35,510 Chain (1); Sequence conflict (1); Topological domain (8); Transmembrane (7) TRANSMEM 32 52 Helical; Name=1. {ECO:0000255}.; TRANSMEM 68 88 Helical; Name=2. {ECO:0000255}.; TRANSMEM 107 127 Helical; Name=3. {ECO:0000255}.; TRANSMEM 141 161 Helical; Name=4. {ECO:0000255}.; TRANSMEM 181 201 Helical; Name=5. {ECO:0000255}.; TRANSMEM 221 241 Helical; Name=6. {ECO:0000255}.; TRANSMEM 260 280 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 31 Extracellular. {ECO:0000255}.; TOPO_DOM 53 67 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 89 106 Extracellular. {ECO:0000255}.; TOPO_DOM 128 140 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 162 180 Extracellular. {ECO:0000255}.; TOPO_DOM 202 220 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 242 259 Extracellular. {ECO:0000255}.; TOPO_DOM 281 312 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan receptor. Probably involved in the function of nociceptive neurons. May regulate nociceptor function and/or development, including the sensation or modulation of pain (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q64449 MRC2_MOUSE C-type mannose receptor 2 (Lectin lambda) (Macrophage mannose receptor 2) (CD antigen CD280) 1479 167,074 Alternative sequence (2); Chain (1); Cross-link (1); Disulfide bond (15); Domain (10); Erroneous initiation (1); Frameshift (1); Glycosylation (5); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1414 1434 Helical. {ECO:0000255}. TOPO_DOM 31 1413 Extracellular. {ECO:0000255}.; TOPO_DOM 1435 1479 Cytoplasmic. {ECO:0000255}. FUNCTION: May play a role as endocytotic lectin receptor displaying calcium-dependent lectin activity. Internalizes glycosylated ligands from the extracellular space for release in an endosomal compartment via clathrin-mediated endocytosis. May be involved in plasminogen activation system controlling the extracellular level of PLAUR/PLAU, and thus may regulate protease activity at the cell surface. May contribute to cellular uptake, remodeling and degradation of extracellular collagen matrices. May participate in remodeling of extracellular matrix cooperating with the matrix metalloproteinases (MMPs). {ECO:0000269|PubMed:12668656, ECO:0000269|PubMed:14729061, ECO:0000269|PubMed:15967816}. PTM: Phosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Interacts directly with PLAUR/UPAR and PLAU/pro-UPA to form a tri-molecular complex. Interacts with collagen V and with C-terminal region of type I collagen/COL1A1 (By similarity). {ECO:0000250}. DOMAIN: C-type lectin domains 3 to 8 are not required for calcium-dependent binding of mannose, fucose and N-acetylglucosamine. C-type lectin domain 2 is responsible for sugar-binding in a calcium-dependent manner (By similarity). {ECO:0000250}.; DOMAIN: Fibronectin type-II domain mediates collagen-binding. {ECO:0000250}.; DOMAIN: Ricin B-type lectin domain contacts with the second C-type lectin domain. TISSUE SPECIFICITY: Highly expressed in heart, lung and kidney, but little or no expression in brain, thymus or adult liver. Expressed at highly endothelialized sites such as those in choroid plexus and kidney glomerulai as well as in chondrocytes in cartilaginous regions of the embryo. {ECO:0000269|PubMed:8702911}. +Q91ZB7 MRGRE_MOUSE Mas-related G-protein coupled receptor member E (Evolutionary breakpoint transcript 3 protein) 310 34,588 Chain (1); Glycosylation (2); Topological domain (8); Transmembrane (7) TRANSMEM 23 43 Helical; Name=1. {ECO:0000255}.; TRANSMEM 61 81 Helical; Name=2. {ECO:0000255}.; TRANSMEM 93 113 Helical; Name=3. {ECO:0000255}.; TRANSMEM 134 154 Helical; Name=4. {ECO:0000255}.; TRANSMEM 175 195 Helical; Name=5. {ECO:0000255}.; TRANSMEM 214 234 Helical; Name=6. {ECO:0000255}.; TRANSMEM 249 269 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 22 Extracellular. {ECO:0000255}.; TOPO_DOM 44 60 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 82 92 Extracellular. {ECO:0000255}.; TOPO_DOM 114 133 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 155 174 Extracellular. {ECO:0000255}.; TOPO_DOM 196 213 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 235 248 Extracellular. {ECO:0000255}.; TOPO_DOM 270 310 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan receptor. May regulate nociceptor function and/or development, including the sensation or modulation of pain. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q8CIP3 MRGX1_MOUSE Mas-related G-protein coupled receptor member X1 (Mas-related G-protein coupled receptor member C11) (Sensory neuron-specific G-protein coupled receptor 1) 322 36,810 Chain (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 31 51 Helical; Name=1. {ECO:0000255}.; TRANSMEM 60 80 Helical; Name=2. {ECO:0000255}.; TRANSMEM 101 121 Helical; Name=3. {ECO:0000255}.; TRANSMEM 143 163 Helical; Name=4. {ECO:0000255}.; TRANSMEM 180 200 Helical; Name=5. {ECO:0000255}.; TRANSMEM 224 244 Helical; Name=6. {ECO:0000255}.; TRANSMEM 258 278 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 30 Extracellular. {ECO:0000255}.; TOPO_DOM 52 59 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 81 100 Extracellular. {ECO:0000255}.; TOPO_DOM 122 142 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 164 179 Extracellular. {ECO:0000255}.; TOPO_DOM 201 223 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 245 257 Extracellular. {ECO:0000255}.; TOPO_DOM 279 322 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan receptor activated by neuropeptides terminating in Arg-Phe or Arg-Phe-amide. Mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. Its effect is mediated by G(q) and G(11) proteins. May regulate the function of nociceptive neurons by modulation of pain perception. {ECO:0000250|UniProtKB:Q96LB2, ECO:0000269|PubMed:12397184}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in a subset of IB4-positive small diameter nociceptive dorsal root neurons. {ECO:0000269|PubMed:12397184}. +Q7M6Y6 MRO2B_MOUSE Maestro heat-like repeat-containing protein family member 2B (HEAT repeat-containing protein 7B2) (Sperm PKA-interacting factor) (SPIF) 1581 180,480 Alternative sequence (2); Chain (1); Erroneous initiation (1); Repeat (16); Sequence conflict (2) FUNCTION: May play a role in the process of sperm capacitation (PubMed:27105888). {ECO:0000269|PubMed:27105888}. PTM: Constitutively phosphorylated on serine and threonine residues in acrosomal region of the sperm head, midpiece and flagellar regions of noncapacitated spermatozoa. Phosphorylation on tyrosine residues increases upon sperm capacitation within the acrosomal and tail regions in a protein kinase A (PKA)-dependent signaling pathway. {ECO:0000269|PubMed:27105888}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27105888}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:27105888}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:27105888}. Note=Colocalizes with PRKACA and TCP11 on the acrosome and tail regions in round spermatids and spermatozoa regardless of the capacitation status of the sperm. {ECO:0000269|PubMed:27105888}. SUBUNIT: Found in a complex at least composed of MROH2B isoform 2, PRKACA isoform 2 and TCP11 (PubMed:27105888). Interacts with PRKACA isoform 2 (PubMed:27105888). Interacts with TCP11 (PubMed:27105888). {ECO:0000269|PubMed:27105888}. TISSUE SPECIFICITY: Expressed strongly in round spermatids and fully mature spermatozoa. Expressed weakly in pachytene spermatocytes (at protein level). Isoform 2 is specifically expressed in the testis. Isoform 2 is expressed in pachytene spermatocytes and round spermatids. Isoform 3 is weakly expressed in testis. {ECO:0000269|PubMed:27105888}. +Q07243 MTF1_MOUSE Metal regulatory transcription factor 1 (MRE-binding transcription factor) (Transcription factor MTF-1) 675 72,603 Chain (1); Compositional bias (2); Initiator methionine (1); Modified residue (3); Motif (1); Sequence conflict (1); Zinc finger (6) FUNCTION: Activates the metallothionein I promoter. Binds to the metal responsive element (MRE). SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:11005378}. +Q02395 MTF2_MOUSE Metal-response element-binding transcription factor 2 (Metal regulatory transcription factor 2) (Metal-response element DNA-binding protein M96) (Polycomb-like protein 2) (mPCl2) (Zinc-regulated factor 1) (ZiRF1) 593 66,924 Alternative sequence (1); Beta strand (9); Chain (1); Compositional bias (2); Cross-link (2); Domain (1); Helix (2); Modified residue (2); Sequence caution (2); Sequence conflict (5); Turn (4); Zinc finger (2) FUNCTION: Polycomb group (PcG) that specifically binds histone H3 trimethylated at 'Lys-36' (H3K36me3) and recruits the PRC2 complex. Acts by binding to H3K36me3, a mark for transcriptional activation, and recruiting the PRC2 complex, leading to enhance PRC2 H3K27me3 methylation activity. Regulates the transcriptional networks during embryonic stem cell self-renewal and differentiation. Promotes recruitment of the PRC2 complex to the inactive X chromosome in differentiating XX ES cells and PRC2 recruitment to target genes in undifferentiated ES cells. Required to repress Hox genes by enhancing H3K27me3 methylation of the PRC2 complex. In some conditions may act as an inhibitor of PRC2 activity: able to activate the CDKN2A gene and promote cellular senescence by suppressing the catalytic activity of the PRC2 complex locally. Binds to the metal-regulating-element (MRE) of MT1A gene promoter. {ECO:0000269|PubMed:20144788, ECO:0000269|PubMed:21059868, ECO:0000269|PubMed:21367819, ECO:0000269|PubMed:9173905}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21367819}. SUBUNIT: Associated component of the PRC2 complex. DOMAIN: The Tudor domain recognizes and binds H3K36me3. {ECO:0000269|PubMed:23104054}. +P18155 MTDC_MOUSE Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial [Includes: NAD-dependent methylenetetrahydrofolate dehydrogenase (EC 1.5.1.15); Methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9)] 350 37,863 Binding site (1); Chain (1); Cross-link (1); Modified residue (1); Nucleotide binding (1); Region (3); Transit peptide (1) FUNCTION: Although its dehydrogenase activity is NAD-specific, it can also utilize NADP at a reduced efficiency. {ECO:0000250|UniProtKB:P13995}. SUBCELLULAR LOCATION: Mitochondrion. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P13995}. +Q8BH10 ORAI2_MOUSE Protein orai-2 (Transmembrane protein 142B) 250 28,199 Chain (1); Frameshift (1); Transmembrane (4) TRANSMEM 66 83 Helical. {ECO:0000255}.; TRANSMEM 94 114 Helical. {ECO:0000255}.; TRANSMEM 148 168 Helical. {ECO:0000255}.; TRANSMEM 192 212 Helical. {ECO:0000255}. FUNCTION: Ca(2+) release-activated Ca(2+)-like (CRAC-like) channel subunit which mediates Ca(2+) influx and increase in Ca(2+)-selective current by synergy with the Ca(2+) sensor, STIM1. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with CRACR2A/EFCAB4B. {ECO:0000250}. +Q6P8G8 ORAI3_MOUSE Protein orai-3 (Transmembrane protein 142C) 290 31,358 Chain (1); Modified residue (2); Transmembrane (4) TRANSMEM 63 82 Helical. {ECO:0000255}.; TRANSMEM 95 115 Helical. {ECO:0000255}.; TRANSMEM 157 177 Helical. {ECO:0000255}.; TRANSMEM 239 259 Helical. {ECO:0000255}. FUNCTION: Key regulator or component of store-operated Ca(2+) channel and transcription factor NFAT nuclear import. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with CRACR2A/EFCAB4B. {ECO:0000250}. +Q921I0 ORML1_MOUSE ORM1-like protein 1 153 17,355 Chain (1); Sequence conflict (1); Transmembrane (2) TRANSMEM 22 42 Helical. {ECO:0000255}.; TRANSMEM 101 121 Helical. {ECO:0000255}. FUNCTION: Negative regulator of sphingolipid synthesis. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q9WVD5 ORNT1_MOUSE Mitochondrial ornithine transporter 1 (Solute carrier family 25 member 15) 301 32,823 Chain (1); Repeat (3); Transmembrane (6) TRANSMEM 5 25 Helical; Name=1. {ECO:0000255}.; TRANSMEM 68 88 Helical; Name=2. {ECO:0000255}.; TRANSMEM 110 130 Helical; Name=3. {ECO:0000255}.; TRANSMEM 168 188 Helical; Name=4. {ECO:0000255}.; TRANSMEM 207 227 Helical; Name=5. {ECO:0000255}.; TRANSMEM 237 257 Helical; Name=6. {ECO:0000255}. FUNCTION: Ornithine-citrulline antiporter (PubMed:19287344). Connects the cytosolic and the intramitochondrial reactions of the urea cycle by exchanging cytosolic ornithine with matrix citrulline. The stoichiometry is close to 1:1 (By similarity). {ECO:0000250|UniProtKB:A0A0G2K309, ECO:0000269|PubMed:19287344}. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:A0A0G2K309}. TISSUE SPECIFICITY: Widely expressed, with highest levels in the liver, testis and kidney. In the brain, expressed at high levels in the hypothalamus. {ECO:0000269|PubMed:19287344}. +Q9D8S4 ORN_MOUSE Oligoribonuclease, mitochondrial (EC 3.1.-.-) (RNA exonuclease 2 homolog) (Small fragment nuclease) 237 26,739 Chain (1); Domain (1); Modified residue (3); Transit peptide (1) FUNCTION: 3'-to-5' exoribonuclease specific for small oligoribonucleotides. Active on small (primarily C18:2 > C18:1 > C18:0. Plays a central role in absorption of dietary fat in the small intestine by catalyzing the resynthesis of triacylglycerol in enterocytes. May play a role in diet-induced obesity. {ECO:0000269|PubMed:12576479, ECO:0000269|PubMed:12730219, ECO:0000269|PubMed:14966132}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14966132}; Multi-pass membrane protein {ECO:0000269|PubMed:14966132}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q3SYC2}. TISSUE SPECIFICITY: Mainly expressed in small intestine. Detected in the small intestine in a proximal-to-distal gradient that correlated with fat absorption pattern. Present not only in the villi, but also in the crypt regions of the small intestine, which suggests that expression occurs prior to the maturation of enterocytes. Not detectable in other sections of the digestive tract, including stomach, cecum, colon and rectum, or other tissues such as kidney, liver and adipocytes (at protein level). Also detected in kidney, adipose and stomach. Expressed at very low level in liver, skeletal muscle and spleen. Not expressed in brain, heart, lung, skin, testis and thymus. {ECO:0000269|PubMed:12576479, ECO:0000269|PubMed:12621063, ECO:0000269|PubMed:14966132}. +Q9Z223 MOC2B_MOUSE Molybdopterin synthase catalytic subunit (EC 2.8.1.12) (Molybdenum cofactor synthesis protein 2 large subunit) (Molybdenum cofactor synthesis protein 2B) (MOCS2B) 189 20,924 Alternative sequence (3); Binding site (1); Chain (1); Modified residue (1); Region (2); Sequence conflict (8) Cofactor biosynthesis; molybdopterin biosynthesis. FUNCTION: Catalytic subunit of the molybdopterin synthase complex, a complex that catalyzes the conversion of precursor Z into molybdopterin. Acts by mediating the incorporation of 2 sulfur atoms from thiocarboxylated MOCS2A into precursor Z to generate a dithiolene group. {ECO:0000255|HAMAP-Rule:MF_03052}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000255|HAMAP-Rule:MF_03052}. SUBUNIT: Heterotetramer; composed of 2 small (MOCS2A) and 2 large (MOCS2B) subunits. {ECO:0000255|HAMAP-Rule:MF_03052}. +P53986 MOT1_MOUSE Monocarboxylate transporter 1 (MCT 1) (Solute carrier family 16 member 1) 493 53,267 Chain (1); Modified residue (11); Topological domain (13); Transmembrane (12) TRANSMEM 16 36 Helical. {ECO:0000255}.; TRANSMEM 60 80 Helical. {ECO:0000255}.; TRANSMEM 87 107 Helical. {ECO:0000255}.; TRANSMEM 112 132 Helical. {ECO:0000255}.; TRANSMEM 144 164 Helical. {ECO:0000255}.; TRANSMEM 167 187 Helical. {ECO:0000255}.; TRANSMEM 256 276 Helical. {ECO:0000255}.; TRANSMEM 292 312 Helical. {ECO:0000255}.; TRANSMEM 322 342 Helical. {ECO:0000255}.; TRANSMEM 347 367 Helical. {ECO:0000255}.; TRANSMEM 383 403 Helical. {ECO:0000255}.; TRANSMEM 416 436 Helical. {ECO:0000255}. TOPO_DOM 1 15 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 37 59 Extracellular. {ECO:0000255}.; TOPO_DOM 81 86 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 108 111 Extracellular. {ECO:0000255}.; TOPO_DOM 133 143 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 165 166 Extracellular. {ECO:0000255}.; TOPO_DOM 188 255 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 277 291 Extracellular. {ECO:0000255}.; TOPO_DOM 313 321 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 343 346 Extracellular. {ECO:0000255}.; TOPO_DOM 368 382 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 404 415 Extracellular. {ECO:0000255}.; TOPO_DOM 437 493 Cytoplasmic. {ECO:0000255}. FUNCTION: Proton-coupled monocarboxylate transporter. Catalyzes the rapid transport across the plasma membrane of many monocarboxylates such as lactate, pyruvate, branched-chain oxo acids derived from leucine, valine and isoleucine, and the ketone bodies acetoacetate, beta-hydroxybutyrate and acetate. Depending on the tissue and on cicumstances, mediates the import or export of lactic acid and ketone bodies. Required for normal nutrient assimilation, increase of white adipose tissue and body weight gain when on a high-fat diet. Plays a role in cellular responses to a high-fat diet by modulating the cellular levels of lactate and pyruvate, small molecules that contribute to the regulation of central metabolic pathways and insulin secretion, with concomitant effects on plasma insulin levels and blood glucose homeostasis. {ECO:0000269|PubMed:22522610, ECO:0000269|PubMed:24367518}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21792931, ECO:0000269|PubMed:8603082}; Multi-pass membrane protein {ECO:0000269|PubMed:21792931, ECO:0000269|PubMed:8603082}. SUBUNIT: Interacts with BSG. Interacts with EMB. Interaction with either BSG or EMB is required for expression at the cell membrane. {ECO:0000269|PubMed:21792931}. TISSUE SPECIFICITY: Detected in liver, brain, spinal cord, spermatozoa, muscle, white adipose tissue and brown adipose tissue (at protein level). Widely expressed, except in pancreas, where expression is not detectable. {ECO:0000269|PubMed:21792931, ECO:0000269|PubMed:22522610, ECO:0000269|PubMed:24367518, ECO:0000269|PubMed:8603082, ECO:0000269|PubMed:9725820}. +Q6PGF2 MORN4_MOUSE MORN repeat-containing protein 4 146 16,206 Chain (1); Repeat (4) FUNCTION: Plays a role in promoting axonal degeneration following neuronal injury by toxic insult or trauma. {ECO:0000269|PubMed:22496551}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8NDC4}. Cell projection, filopodium tip {ECO:0000250|UniProtKB:Q8NDC4}. Cell projection, stereocilium {ECO:0000269|PubMed:26754646}. Note=Found in the cytoplasm in the absence of MYO3A and localizes at filopodial tips in the presence of MYO3A. {ECO:0000250|UniProtKB:Q8NDC4}. SUBUNIT: Interacts with MYO3A. {ECO:0000269|PubMed:26754646}. +Q9DAI9 MORN5_MOUSE MORN repeat-containing protein 5 170 20,078 Chain (1); Repeat (3) +Q60856 OAS1B_MOUSE Inactive 2'-5'-oligoadenylate synthase 1B ((2-5')oligo(A) synthase 1B) (2-5A synthase 1B) (2'-5'-oligoadenylate synthase-like protein 1) 376 43,620 Chain (1); Frameshift (2); Natural variant (32); Sequence conflict (3); Topological domain (2); Transmembrane (1) TRANSMEM 352 370 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 1 351 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 371 376 Extracellular. {ECO:0000255}. FUNCTION: Does not have 2'-5'-OAS activity, but can bind double-stranded RNA (PubMed:12396720, PubMed:27663720). The full-length protein displays antiviral activity against flaviviruses such as west Nile virus (WNV) via an alternative antiviral pathway independent of RNase L (PubMed:12080145, PubMed:16371364, PubMed:17904183, PubMed:27663720). The truncated form of the protein lacks antiviral activity (PubMed:12080145, PubMed:16371364, PubMed:17904183). {ECO:0000269|PubMed:12080145, ECO:0000269|PubMed:12396720, ECO:0000269|PubMed:16371364, ECO:0000269|PubMed:17904183, ECO:0000269|PubMed:27663720}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305|PubMed:22623793}; Single-pass type IV membrane protein {ECO:0000305|PubMed:22623793}. SUBUNIT: Interacts with OSBPL1A and ABCF3. {ECO:0000269|PubMed:22623793}. TISSUE SPECIFICITY: Highly expressed in lung, spleen and thymus (PubMed:12396720, PubMed:12186974). Also detected at lower levels in heart, kidney, liver, lung, skeletal muscle, testes, uterus and ovaries (PubMed:12396720, PubMed:12186974, PubMed:27663720). {ECO:0000269|PubMed:12186974, ECO:0000269|PubMed:12396720, ECO:0000269|PubMed:27663720}. +Q924S2 OAS1C_MOUSE Inactive 2'-5' oligoadenylate synthetase 1C (2',5'-oligoadenylate synthetase-like 5) 362 42,912 Chain (1) FUNCTION: Does not have 2'-5'-OAS activity, but can bind double-stranded RNA. {ECO:0000269|PubMed:11418248, ECO:0000269|PubMed:27663720}. TISSUE SPECIFICITY: Expressed at highest level in brain with lesser amounts in spleen, kidney, stomach, liver, intestine, ovary, skin and testis. Not detected in lung, thymus, heart and uterus. {ECO:0000269|PubMed:11418248, ECO:0000269|PubMed:27663720}. +E9Q9A9 OAS2_MOUSE 2'-5'-oligoadenylate synthase 2 ((2-5')oligo(A) synthase 2) (2-5A synthase 2) (EC 2.7.7.84) (2',5'-oligoadenylate synthetase-like 11) 742 85,051 Alternative sequence (1); Binding site (3); Chain (1); Initiator methionine (1); Lipidation (1); Metal binding (3); Modified residue (1); Mutagenesis (4); Natural variant (1); Region (2); Sequence conflict (2) FUNCTION: Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response (PubMed:12396720, PubMed:29117179). Activated by detection of double stranded RNA (dsRNA): polymerizes higher oligomers of 2'-5'-oligoadenylates (2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L (RNASEL) leading to its dimerization and subsequent activation (PubMed:29117179). Activation of RNASEL leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication (PubMed:21142819). Can mediate the antiviral effect via the classical RNASEL-dependent pathway or an alternative antiviral pathway independent of RNASEL (PubMed:21142819). In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation (PubMed:21142819). May act as a negative regulator of lactation, stopping lactation in virally infected mammary gland lobules, thereby preventing transmission of viruses to neonates (PubMed:29117179). Non-infected lobules would not be affected, allowing efficient pup feeding during infection (PubMed:29117179). {ECO:0000269|PubMed:12396720, ECO:0000269|PubMed:15865429, ECO:0000269|PubMed:29117179, ECO:0000303|PubMed:21142819}. PTM: Myristoylation is not essential for its activity. {ECO:0000250|UniProtKB:P29728}.; PTM: Glycosylated. Glycosylation is essential for its activity. {ECO:0000250|UniProtKB:P29728}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P29728}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P29728}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P29728}. TISSUE SPECIFICITY: Expressed in the uterus (PubMed:12396720). Expressed in mammary glands: expressed at low level before the establishment of lactation, then expression strongly increases, and subsequently decreases during early involution (PubMed:29117179). {ECO:0000269|PubMed:12396720, ECO:0000269|PubMed:29117179}. +Q8C160 MSLNL_MOUSE Mesothelin-like protein (Pre-pro-megakaryocyte-potentiating-factor-like) 685 74,710 Chain (1); Glycosylation (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 628 648 Helical. {ECO:0000255}. TOPO_DOM 33 627 Extracellular. {ECO:0000255}.; TOPO_DOM 649 685 Cytoplasmic. {ECO:0000255}. FUNCTION: May play a role in cellular adhesion. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q69ZF8 MSL2_MOUSE E3 ubiquitin-protein ligase MSL2 (EC 2.3.2.-) (E3 ubiquitin-protein transferase MSL2) (Male-specific lethal 2-like 1) (MSL2-like 1) (Male-specific lethal-2 homolog) (MSL-2) (Male-specific lethal-2 homolog 1) (RING finger protein 184) 577 62,538 Chain (1); Compositional bias (1); Cross-link (1); Erroneous initiation (1); Modified residue (1); Region (1); Zinc finger (1) FUNCTION: Component of histone acetyltransferase complex responsible for the majority of histone H4 acetylation at lysine 16 which is implicated in the formation of higher-order chromatin structure (By similarity). Acts as an E3 ubiquitin ligase that promotes monoubiquitination of histone H2B at 'Lys-35' (H2BK34Ub), but not that of H2A. This activity is greatly enhanced by heterodimerization with MSL1. H2B ubiquitination in turn stimulates histone H3 methylation at 'Lys-5' (H3K4me) and 'Lys-80' (H3K79me) and leads to gene activation, including that of HOXA9 and MEIS1 (By similarity). {ECO:0000250}. SUBUNIT: Component of a multisubunit histone acetyltransferase complex (MSL) at least composed of the KAT8/MOF/MYST1, MSL1/hampin, MSL2 and MSL3. Forms a MSL heterotetrameric core with MSL1. +Q9D6Y7 MSRA_MOUSE Mitochondrial peptide methionine sulfoxide reductase (EC 1.8.4.11) (Peptide-methionine (S)-S-oxide reductase) (Peptide Met(O) reductase) (Protein-methionine-S-oxide reductase) (PMSR) 233 25,988 Alternative sequence (3); Beta strand (7); Chain (1); Helix (7); Lipidation (1); Modified residue (4); Sequence conflict (3); Transit peptide (1); Turn (5) FUNCTION: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Isoform 1: Mitochondrion.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Nucleus. Membrane; Lipid-anchor. +Q9JLC3 MSRB1_MOUSE Methionine-R-sulfoxide reductase B1 (MsrB1) (EC 1.8.4.12) (EC 1.8.4.14) (Selenoprotein R) (SelR) (Selenoprotein X) (SelX) 116 12,788 Active site (1); Beta strand (8); Chain (1); Domain (1); Helix (1); Metal binding (4); Non-standard residue (1); Turn (4) FUNCTION: Methionine-sulfoxide reductase that specifically reduces methionine (R)-sulfoxide back to methionine. While in many cases, methionine oxidation is the result of random oxidation following oxidative stress, methionine oxidation is also a post-translational modification that takes place on specific residue. Acts as a regulator of actin assembly by reducing methionine (R)-sulfoxide mediated by MICALs (MICAL1, MICAL2 or MICAL3) on actin, thereby promoting filament repolymerization. Plays a role in innate immunity by reducing oxidized actin, leading to actin repolymerization in macrophages. {ECO:0000269|PubMed:14699060, ECO:0000269|PubMed:23911929}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14699060}. Nucleus {ECO:0000269|PubMed:14699060}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:23911929}. +Q9D3H2 OBP1A_MOUSE Odorant-binding protein 1a (Odorant-binding protein IA) 163 18,469 Chain (1); Disulfide bond (2); Signal peptide (1) FUNCTION: Binds the chemical odorant 2-isobutyl-3-methoxypyrazine. {ECO:0000269|PubMed:8529023}. PTM: The N-terminus may be blocked. {ECO:0000269|PubMed:8529023}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. SUBUNIT: May form a heterodimer with OBP1B. {ECO:0000305|PubMed:8529023}. TISSUE SPECIFICITY: Expressed in nasal mucosa (at protein level) (PubMed:8529023). Specifically detected in septal and lateral nasal glands (PubMed:9661663). {ECO:0000269|PubMed:8529023, ECO:0000269|PubMed:9661663}. +A2AEP0 OBP1B_MOUSE Odorant-binding protein 1b (Odorant-binding protein IB) 171 19,394 Chain (1); Disulfide bond (2); Signal peptide (1) FUNCTION: Binds the chemical odorant 2-isobutyl-3-methoxypyrazine. {ECO:0000269|PubMed:8529023}. PTM: The N-terminus may be blocked. {ECO:0000269|PubMed:8529023}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. SUBUNIT: May form a heterodimer with OBP1A. {ECO:0000305|PubMed:8529023}. TISSUE SPECIFICITY: Expressed in nasal mucosa (at protein level) (PubMed:8529023). Specifically detected in septal and lateral nasal glands (PubMed:9661663). {ECO:0000269|PubMed:8529023, ECO:0000269|PubMed:9661663}. +Q9D5Z5 MSS51_MOUSE Putative protein MSS51 homolog, mitochondrial (Zinc finger MYND domain-containing protein 17) 446 49,950 Chain (1); Zinc finger (1) +P13297 MSX1_MOUSE Homeobox protein MSX-1 (Homeobox protein Hox-7) (Hox-7.1) (Msh homeobox 1-like protein) 303 31,672 Chain (1); Cross-link (2); DNA binding (1); Erroneous initiation (2); Frameshift (1); Helix (3); Mutagenesis (6); Sequence conflict (1) FUNCTION: Acts as a transcriptional repressor. May play a role in limb-pattern formation. Acts in cranofacial development and specifically in odontogenesis. {ECO:0000269|PubMed:1677742, ECO:0000269|PubMed:7823952}. PTM: Sumoylated by PIAS1, desumoylated by SENP1. {ECO:0000269|PubMed:16678795}. SUBCELLULAR LOCATION: Nucleus. +D3YYU8 OBSL1_MOUSE Obscurin-like protein 1 1804 197,937 Alternative sequence (3); Chain (1); Disulfide bond (12); Domain (15); Modified residue (1); Region (2); Sequence conflict (2) FUNCTION: Core component of the 3M complex, a complex required to regulate microtubule dynamics and genome integrity. It is unclear how the 3M complex regulates microtubules, it could act by controlling the level of a microtubule stabilizer. Acts as a regulator of the Cul7-RING(FBXW8) ubiquitin-protein ligase, playing a critical role in the ubiquitin ligase pathway that regulates Golgi morphogenesis and dendrite patterning in brain. Required to localize CUL7 to the Golgi apparatus in neurons (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O75147}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O75147}. Golgi apparatus {ECO:0000250|UniProtKB:O75147}. Note=Colocalizes with CUL7 at the Golgi apparatus in neurons. {ECO:0000250|UniProtKB:O75147}. SUBUNIT: Component of the 3M complex, composed of core components CUL7, CCDC8 and OBSL1. Interacts with CCDC8. Interacts with CUL7; the interaction is direct. Interacts with FBXW8. Interacts (via N-terminal Ig-like domain) with TTN/titin (via C-terminal Ig-like domain); the interaction is direct (By similarity). {ECO:0000250}. +Q9Z0L3 OC90_MOUSE Otoconin-90 (Oc90) (Otoconin-95) (Oc95) 485 52,445 Alternative sequence (6); Chain (1); Disulfide bond (7); Glycosylation (4); Region (3); Sequence conflict (3); Signal peptide (1) FUNCTION: Major protein of the otoconia, a calcium carbonate structure in the saccule and utricle of the ear (PubMed:17300776). Together with OTOL1, acts as a scaffold for otoconia biomineralization: sequesters calcium and forms interconnecting fibrils between otoconia that are incorporated into the calcium crystal structure (PubMed:21655225, PubMed:24748133). Together with OTOL1, modulates calcite crystal morphology and growth kinetics (PubMed:24748133). It is unlikely that this protein has phospholipase A2 activity (PubMed:17300776). {ECO:0000269|PubMed:17300776, ECO:0000269|PubMed:21655225, ECO:0000269|PubMed:24748133}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P81869}. SUBUNIT: Interacts with OTOL1. {ECO:0000269|PubMed:17300776, ECO:0000269|PubMed:20856818, ECO:0000269|PubMed:21655225}. DOMAIN: Consists of 3 PA2-type domains. TISSUE SPECIFICITY: In the embryo, highly expressed in the developing otocyst with weak expression in the brain. Also expressed in nonsensory epithelia of both the vestibular and cochlear portions of the developing inner ear. Not expressed in adult or embryonic macular sensory epithelia. {ECO:0000269|PubMed:9892667}. +Q03358 MSX2_MOUSE Homeobox protein MSX-2 (Homeobox protein Hox-8-1) 267 28,915 Chain (1); DNA binding (1); Sequence conflict (4) FUNCTION: Acts as a transcriptional regulator in bone development. Represses the ALPL promoter activity and antagonizes the stimulatory effect of DLX5 on ALPL expression during osteoblast differentiation. Probable morphogenetic role. May play a role in limb-pattern formation. In osteoblasts, suppresses transcription driven by the osteocalcin FGF response element (OCFRE). Binds to the homeodomain-response element of the ALPL promoter. {ECO:0000269|PubMed:15383550, ECO:0000269|PubMed:1677742}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with MINT. Interacts with XRCC6 (Ku70) and XRCC5 (Ku80) (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in mesenchymal tissue in the developing spinal cord and limbs. +Q9D8W7 OCAD2_MOUSE OCIA domain-containing protein 2 154 16,926 Chain (1); Domain (1); Modified residue (1) SUBCELLULAR LOCATION: Endosome {ECO:0000305}. +Q8CDZ2 MT21E_MOUSE Protein-lysine methyltransferase METTL21E (EC 2.1.1.-) (Methyltransferase-like protein 21E) 244 28,067 Binding site (4); Chain (1); Region (1) FUNCTION: Protein-lysine methyltransferase. {ECO:0000250}. +Q9D2G2 ODO2_MOUSE Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial (EC 2.3.1.61) (2-oxoglutarate dehydrogenase complex component E2) (OGDC-E2) (Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex) (E2K) 454 48,995 Active site (2); Alternative sequence (2); Chain (1); Domain (1); Modified residue (8); Sequence conflict (1); Transit peptide (1) Amino-acid degradation; L-lysine degradation via saccharopine pathway; glutaryl-CoA from L-lysine: step 6/6. FUNCTION: Dihydrolipoamide succinyltransferase (E2) component of the 2-oxoglutarate dehydrogenase complex (By similarity). The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2) (By similarity). The 2-oxoglutarate dehydrogenase complex is mainly active in the mitochondrion. A fraction of the 2-oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation of histones: associates with KAT2A on chromatin and provides succinyl-CoA to histone succinyltransferase KAT2A (By similarity). {ECO:0000250|UniProtKB:P36957, ECO:0000250|UniProtKB:Q9N0F1}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:P36957}. Nucleus {ECO:0000250|UniProtKB:P36957}. Note=Mainly localizes in the mitochondrion. A small fraction localizes to the nucleus, where the 2-oxoglutarate dehydrogenase complex is required for histone succinylation. {ECO:0000250|UniProtKB:P36957}. SUBUNIT: The 2-oxoglutarate dehydrogenase complex is composed of OGDH (2-oxoglutarate dehydrogenase; E1), DLST (dihydrolipoamide succinyltransferase; E2) and DLD (dihydrolipoamide dehydrogenase; E3). It contains multiple copies of the three enzymatic components (E1, E2 and E3). In the nucleus, the 2-oxoglutarate dehydrogenase complex associates with KAT2A. {ECO:0000250|UniProtKB:P36957}. +Q791T5 MTCH1_MOUSE Mitochondrial carrier homolog 1 (Mitochondrial carrier-like protein 1) 389 41,565 Alternative sequence (1); Chain (1); Erroneous initiation (4); Modified residue (1); Repeat (2); Sequence conflict (2); Transmembrane (2) TRANSMEM 248 268 Helical. {ECO:0000255}.; TRANSMEM 315 335 Helical. {ECO:0000255}. FUNCTION: Potential mitochondrial transporter. May play a role in apoptosis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Interacts with PSEN1. {ECO:0000250}. +Q3UHU5 MTCL1_MOUSE Microtubule cross-linking factor 1 (Coiled-coil domain-containing protein 165) (PAR-1-interacting protein) (SOGA family member 2) 1945 213,862 Alternative sequence (2); Chain (1); Coiled coil (4); Compositional bias (3); Modified residue (32); Region (4) FUNCTION: Microtubule-associated factor involved in the late phase of epithelial polarization and microtubule dynamics regulation. Plays a role in the development and maintenance of non-centrosomal microtubule bundles at the lateral membrane in polarized epithelial cells. {ECO:0000269|PubMed:23902687}. SUBCELLULAR LOCATION: Isoform 1: Lateral cell membrane. Apical cell membrane. Cytoplasm, cytoskeleton, spindle pole. Midbody. Cytoplasm, cytoskeleton. Note=Colocalized with microtubules at the base of cilia. Gradually accumulates on the apicobasal microtubule bundles during epithelial cell polarization (By similarity). Colocalized with the apicobasal microtubule bundles running beneath the lateral membrane. Colocalized with microtubule bundles in the spindle pole in mitotic cells and in the midbodies at the end of cytokinesis. {ECO:0000250}. SUBUNIT: Homodimer. Isoform 1 interacts with MARK2; the interaction increases MARK2 microtubule-binding ability. Associates (via N- and C-terminus domains) with microtubule filaments. {ECO:0000269|PubMed:23902687}. +Q8CIQ6 MTR1B_MOUSE Melatonin receptor type 1B (Mel-1B-R) (Mel1b receptor) 364 40,261 Chain (1); Disulfide bond (1); Glycosylation (1); Sequence conflict (1); Topological domain (8); Transmembrane (7) TRANSMEM 43 63 Helical; Name=1. {ECO:0000255}.; TRANSMEM 77 97 Helical; Name=2. {ECO:0000255}.; TRANSMEM 116 136 Helical; Name=3. {ECO:0000255}.; TRANSMEM 156 176 Helical; Name=4. {ECO:0000255}.; TRANSMEM 201 221 Helical; Name=5. {ECO:0000255}.; TRANSMEM 254 274 Helical; Name=6. {ECO:0000255}.; TRANSMEM 288 308 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 42 Extracellular. {ECO:0000255}.; TOPO_DOM 64 76 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 98 115 Extracellular. {ECO:0000255}.; TOPO_DOM 137 155 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 177 200 Extracellular. {ECO:0000255}.; TOPO_DOM 222 253 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 275 287 Extracellular. {ECO:0000255}.; TOPO_DOM 309 364 Cytoplasmic. {ECO:0000255}. FUNCTION: High affinity receptor for melatonin. The activity of this receptor is mediated by pertussis toxin sensitive G proteins that inhibits adenylate cyclase activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q8C1A3 MTRR_MOUSE Methionine synthase reductase (MSR) (EC 1.16.1.8) 696 77,518 Binding site (3); Chain (1); Domain (2); Modified residue (2); Nucleotide binding (6); Region (1); Sequence conflict (13) FUNCTION: Involved in the reductive regeneration of cob(I)alamin (vitamin B12) cofactor required for the maintenance of methionine synthase in a functional state. Necessary for utilization of methylgroups from the folate cycle, thereby affecting transgenerational epigenetic inheritance. Folate pathway donates methyl groups necessary for cellular methylation and affects different pathways such as DNA methylation, possibly explaining the transgenerational epigenetic inheritance effects. {ECO:0000269|PubMed:24074862}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +Q8CGA4 MTURN_MOUSE Maturin (Maturin neural progenitor differentiation regulator protein homolog) 131 14,841 Chain (1); Compositional bias (1) FUNCTION: May be involved in early neuronal development. {ECO:0000250}. +Q9CQ04 OGFD2_MOUSE 2-oxoglutarate and iron-dependent oxygenase domain-containing protein 2 (EC 1.14.11.-) 349 39,270 Binding site (1); Chain (1); Domain (1); Erroneous initiation (1); Frameshift (1); Metal binding (3); Sequence conflict (3) +Q9D136 OGFD3_MOUSE 2-oxoglutarate and iron-dependent oxygenase domain-containing protein 3 (EC 1.14.11.-) 315 35,385 Active site (1); Binding site (1); Chain (1); Domain (1); Glycosylation (2); Metal binding (3); Topological domain (2); Transmembrane (1) TRANSMEM 42 62 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 41 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 63 315 Lumenal. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. +Q99PG2 OGFR_MOUSE Opioid growth factor receptor (OGFr) (Zeta-type opioid receptor) 633 70,679 Alternative sequence (2); Chain (1); Modified residue (9); Motif (1); Region (1); Repeat (14); Sequence conflict (2) FUNCTION: Receptor for opioid growth factor (OGF), also known as Met-enkephalin. Seems to be involved in growth regulation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=The OGF/OGFR complex is probably translocated to the nucleus. TISSUE SPECIFICITY: Expressed in all tissues examined, including brain, heart, lung, liver, kidney and skeletal muscle. +O08760 OGG1_MOUSE N-glycosylase/DNA lyase [Includes: 8-oxoguanine DNA glycosylase (EC 3.2.2.-); DNA-(apurinic or apyrimidinic site) lyase (AP lyase) (EC 4.2.99.18)] 345 38,883 Active site (1); Binding site (9); Chain (1); Sequence conflict (7) FUNCTION: DNA repair enzyme that incises DNA at 8-oxoG residues. Excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine (FAPY) from damaged DNA. Has a beta-lyase activity that nicks DNA 3' to the lesion. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}. Nucleus speckle {ECO:0000250}. Nucleus matrix {ECO:0000250}. Note=Together with APEX1 is recruited to nuclear speckles in UVA-irradiated cells. {ECO:0000250}. TISSUE SPECIFICITY: Highest expression in testis. +Q8BFQ3 OGR1_MOUSE Ovarian cancer G-protein coupled receptor 1 (G-protein coupled receptor 68) (Sphingosylphosphorylcholine receptor) 365 41,209 Chain (1); Disulfide bond (1); Erroneous initiation (5); Glycosylation (2); Topological domain (8); Transmembrane (7) TRANSMEM 22 46 Helical; Name=1. {ECO:0000255}.; TRANSMEM 59 80 Helical; Name=2. {ECO:0000255}.; TRANSMEM 96 117 Helical; Name=3. {ECO:0000255}.; TRANSMEM 137 158 Helical; Name=4. {ECO:0000255}.; TRANSMEM 184 205 Helical; Name=5. {ECO:0000255}.; TRANSMEM 229 249 Helical; Name=6. {ECO:0000255}.; TRANSMEM 264 284 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 21 Extracellular. {ECO:0000255}.; TOPO_DOM 47 58 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 81 95 Extracellular. {ECO:0000255}.; TOPO_DOM 118 136 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 159 183 Extracellular. {ECO:0000255}.; TOPO_DOM 206 228 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 250 263 Extracellular. {ECO:0000255}.; TOPO_DOM 285 365 Cytoplasmic. {ECO:0000255}. FUNCTION: Proton-sensing receptor involved in pH homeostasis. May represents an osteoblastic pH sensor regulating cell-mediated responses to acidosis in bone. Mediates its action by association with G proteins that stimulates inositol phosphate (IP) production or Ca(2+) mobilization. The receptor is almost silent at pH 7.8 but fully activated at pH 6.8. Function also as a metastasis suppressor gene in prostate cancer. {ECO:0000269|PubMed:17728215, ECO:0000269|PubMed:18847331}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed in the lung, testis, heart, brain, spleen, thymus, brown fat, small intestine, colon, peripheral blood leukocytes, macrophages, stomach, ovary and white fat but not in the liver, kidney, and skeletal muscle. Expression in the prostate is weak but detectable. {ECO:0000269|PubMed:19479052}. +Q8C6Z1 MUC15_MOUSE Mucin-15 (MUC-15) 331 36,383 Chain (1); Compositional bias (1); Frameshift (2); Glycosylation (12); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 234 254 Helical. {ECO:0000255}. TOPO_DOM 23 233 Extracellular. {ECO:0000255}.; TOPO_DOM 255 331 Cytoplasmic. {ECO:0000255}. PTM: Highly glycosylated (N- and O-linked carbohydrates). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q6PZE0 MUC19_MOUSE Mucin-19 (MUC-19) (Gel-forming secreted mucin-19) (Sublingual apomucin) 7524 693,499 Chain (1); Compositional bias (2); Disulfide bond (6); Domain (7); Region (1); Repeat (36); Sequence caution (1); Sequence conflict (8); Signal peptide (1) FUNCTION: May function in ocular mucus homeostasis. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Specifically expressed in sublingual salivary glands. Expressed by mucous cells of the submandibular gland and submucosal gland of the trachea. Expression is altered in sld (sublingual gland differentiation arrest) mutants. {ECO:0000269|PubMed:12847143, ECO:0000269|PubMed:12882755, ECO:0000269|PubMed:15340121}. +Q8CGY8 OGT1_MOUSE UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit (EC 2.4.1.255) (O-GlcNAc transferase subunit p110) (O-linked N-acetylglucosamine transferase 110 kDa subunit) (OGT) 1046 116,952 Active site (1); Alternative sequence (1); Binding site (3); Chain (1); Glycosylation (2); Initiator methionine (1); Modified residue (5); Motif (1); Mutagenesis (4); Nucleotide binding (3); Region (1); Repeat (13); Sequence conflict (2) Protein modification; protein glycosylation. FUNCTION: Catalyzes the transfer of a single N-acetylglucosamine from UDP-GlcNAc to a serine or threonine residue in cytoplasmic and nuclear proteins resulting in their modification with a beta-linked N-acetylglucosamine (O-GlcNAc) (PubMed:29465778). Glycosylates a large and diverse number of proteins including histone H2B, AKT1, EZH2, PFKL, KMT2E/MLL5, MAPT/TAU and HCFC1. Can regulate their cellular processes via cross-talk between glycosylation and phosphorylation or by affecting proteolytic processing. Probably by glycosylating KMT2E/MLL5, stabilizes KMT2E/MLL5 by preventing its ubiquitination (By similarity).Involved in insulin resistance in muscle and adipocyte cells via glycosylating insulin signaling components and inhibiting the 'Thr-308' phosphorylation of AKT1, enhancing IRS1 phosphorylation and attenuating insulin signaling (By similarity). Involved in glycolysis regulation by mediating glycosylation of 6-phosphofructokinase PFKL, inhibiting its activity. Component of a THAP1/THAP3-HCFC1-OGT complex that is required for the regulation of the transcriptional activity of RRM1. Plays a key role in chromatin structure by mediating O-GlcNAcylation of 'Ser-112' of histone H2B: recruited to CpG-rich transcription start sites of active genes via its interaction with TET proteins (TET1, TET2 or TET3). As part of the NSL complex indirectly involved in acetylation of nucleosomal histone H4 on several lysine residues. O-GlcNAcylation of 'Ser-75' of EZH2 increases its stability, and facilitating the formation of H3K27me3 by the PRC2/EED-EZH2 complex (By similarity). Regulates circadian oscillation of the clock genes and glucose homeostasis in the liver. Stabilizes clock proteins ARNTL/BMAL1 and CLOCK through O-glycosylation, which prevents their ubiquitination and subsequent degradation. Promotes the CLOCK-ARNTL/BMAL1-mediated transcription of genes in the negative loop of the circadian clock such as PER1/2 and CRY1/2 (PubMed:23337503, PubMed:23395176). O-glycosylates HCFC1 and regulates its proteolytic processing and transcriptional activity (By similarity). Regulates mitochondrial motility in neurons by mediating glycosylation of TRAK1 (By similarity). Glycosylates HOXA1 (PubMed:29465778). {ECO:0000250|UniProtKB:O15294, ECO:0000250|UniProtKB:P56558, ECO:0000269|PubMed:23337503, ECO:0000269|PubMed:23395176, ECO:0000269|PubMed:29465778}. PTM: Ubiquitinated, leading to its proteasomal degradation. {ECO:0000250}.; PTM: Phosphorylation on Ser-3 or Ser-4 by GSK3-beta positively regulates its activity. {ECO:0000269|PubMed:23395175}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O15294}. Nucleus {ECO:0000269|PubMed:29465778}. Cell membrane {ECO:0000250|UniProtKB:O15294}. Mitochondrion membrane {ECO:0000250|UniProtKB:P56558}. Cell projection {ECO:0000250|UniProtKB:P56558}. Note=Mostly in the nucleus. Retained in the nucleus via interaction with HCFC1. After insulin induction, translocated from the nucleus to the cell membrane via phophatidylinositide binding. Colocalizes with AKT1 at the plasma membrane (By similarity). TRAK1 recruits this protein to mitochondria. In the absence of TRAK1, localizes in cytosol and nucleus (By similarity). {ECO:0000250|UniProtKB:O15294, ECO:0000250|UniProtKB:P56558}. SUBUNIT: Heterotrimer; consists of one 78 kDa subunit and two 110 kDa subunits dimerized via TPR repeats 6 and 7. Component of a THAP1/THAP3-HCFC1-OGT complex. Component of the NSL complex at least composed of MOF/KAT8, KANSL1, KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT, WDR5 and HCFC1. Interacts directly with HCFC1; the interaction O-glycosylates HCFC1, regulates its proteolytic processing and transcriptional activity and, in turn, stabilizes OGT in the nucleus. Interacts (via TPRs 1-6) with SIN3A; the interaction mediates transcriptional repression in parallel with histone deacetylase (By similarity). Interacts (via TPR 5-6) with TET1, TET2 and TET3 (PubMed:23352454). Interacts (via TPR repeats 6 and 7) with ATXN10 (PubMed:16182253). Interacts with histone H2B (By similarity). Interacts with ARNTL/BMAL1 (PubMed:23337503). Found in a complex composed of at least SINHCAF, SIN3A, HDAC1, SAP30, RBBP4, OGT and TET1 (PubMed:28554894). Interacts with SINHCAF (PubMed:28554894). Component of a complex composed of KMT2E/MLL5, OGT and USP7; the complex stabilizes KMT2E/MLL5, preventing KMT2E/MLL5 ubiquitination and proteosomal-mediated degradation. Interacts (via TRP repeats) with KMT2E/MLL5 (via N-terminus). Interacts with USP7 (By similarity). Interacts with TRAK1; this interaction is not required for glycosylation of TRAK1 by this protein. Found in a complex with KIF5B, RHOT1, RHOT2 and TRAK1 (By similarity). Interacts (via TPR repeats domain) with HOXA1; the interaction takes place mainly in the nucleus (PubMed:29465778). {ECO:0000250|UniProtKB:O15294, ECO:0000250|UniProtKB:P56558, ECO:0000269|PubMed:16182253, ECO:0000269|PubMed:23337503, ECO:0000269|PubMed:23352454, ECO:0000269|PubMed:28554894, ECO:0000269|PubMed:29465778}. DOMAIN: The TPR repeat domain is required for substrate binding and oligomerization. {ECO:0000250|UniProtKB:O15294}. +P28665 MUG1_MOUSE Murinoglobulin-1 (MuG1) 1476 165,298 Chain (1); Cross-link (1); Disulfide bond (10); Glycosylation (11); Region (1); Sequence conflict (5); Signal peptide (1) FUNCTION: A proteinase activates the inhibitor by specific proteolysis in the bait region, which, by an unknown mechanism leads to reaction at the cysteinyl-glutamyl internal thiol ester site and to a conformational change, whereby the proteinase is trapped and/or covalently bound to the inhibitor. While in the tetrameric proteinase inhibitors steric inhibition is sufficiently strong, monomeric forms need a covalent linkage between the activated glutamyl residue of the original thiol ester and a terminal amino group of a lysine or another nucleophilic group on the proteinase, for inhibition to be effective. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Monomer. TISSUE SPECIFICITY: Plasma. +Q9QY00 OL154_MOUSE Olfactory receptor 154 (Olfactory receptor 175-1) 318 35,901 Chain (1); Disulfide bond (1); Glycosylation (1); Sequence conflict (14); Topological domain (8); Transmembrane (7) TRANSMEM 29 49 Helical; Name=1. {ECO:0000255}.; TRANSMEM 57 77 Helical; Name=2. {ECO:0000255}.; TRANSMEM 94 114 Helical; Name=3. {ECO:0000255}.; TRANSMEM 145 165 Helical; Name=4. {ECO:0000255}.; TRANSMEM 199 219 Helical; Name=5. {ECO:0000255}.; TRANSMEM 240 260 Helical; Name=6. {ECO:0000255}.; TRANSMEM 272 292 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 28 Extracellular. {ECO:0000255}.; TOPO_DOM 50 56 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 78 93 Extracellular. {ECO:0000255}.; TOPO_DOM 115 144 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 166 198 Extracellular. {ECO:0000255}.; TOPO_DOM 220 239 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 261 271 Extracellular. {ECO:0000255}.; TOPO_DOM 293 318 Cytoplasmic. {ECO:0000255}. FUNCTION: Potential odorant receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q7TS48 OL180_MOUSE Olfactory receptor Olfr180 317 36,239 Chain (1); Disulfide bond (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 29 49 Helical; Name=1. {ECO:0000255}.; TRANSMEM 57 77 Helical; Name=2. {ECO:0000255}.; TRANSMEM 94 114 Helical; Name=3. {ECO:0000255}.; TRANSMEM 145 165 Helical; Name=4. {ECO:0000255}.; TRANSMEM 199 219 Helical; Name=5. {ECO:0000255}.; TRANSMEM 240 259 Helical; Name=6. {ECO:0000255}.; TRANSMEM 269 289 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 28 Extracellular. {ECO:0000255}.; TOPO_DOM 50 56 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 78 93 Extracellular. {ECO:0000255}.; TOPO_DOM 115 144 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 166 198 Extracellular. {ECO:0000255}.; TOPO_DOM 220 239 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 260 268 Extracellular. {ECO:0000255}.; TOPO_DOM 290 317 Cytoplasmic. {ECO:0000255}. FUNCTION: Potential odorant receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q8VFB9 OL183_MOUSE Olfactory receptor 183 (Olfactory receptor 183-2) 309 35,329 Chain (1); Disulfide bond (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 29 49 Helical; Name=1. {ECO:0000255}.; TRANSMEM 57 77 Helical; Name=2. {ECO:0000255}.; TRANSMEM 94 114 Helical; Name=3. {ECO:0000255}.; TRANSMEM 145 165 Helical; Name=4. {ECO:0000255}.; TRANSMEM 199 219 Helical; Name=5. {ECO:0000255}.; TRANSMEM 240 260 Helical; Name=6. {ECO:0000255}.; TRANSMEM 272 292 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 28 Extracellular. {ECO:0000255}.; TOPO_DOM 50 56 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 78 93 Extracellular. {ECO:0000255}.; TOPO_DOM 115 144 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 166 198 Extracellular. {ECO:0000255}.; TOPO_DOM 220 239 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 261 271 Extracellular. {ECO:0000255}.; TOPO_DOM 293 309 Cytoplasmic. {ECO:0000255}. FUNCTION: Potential odorant receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q8VF66 OL469_MOUSE Olfactory receptor 469 (Olfactory receptor 204-21) 314 34,839 Chain (1); Disulfide bond (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 29 49 Helical; Name=1. {ECO:0000255}.; TRANSMEM 58 78 Helical; Name=2. {ECO:0000255}.; TRANSMEM 103 123 Helical; Name=3. {ECO:0000255}.; TRANSMEM 137 157 Helical; Name=4. {ECO:0000255}.; TRANSMEM 200 220 Helical; Name=5. {ECO:0000255}.; TRANSMEM 241 261 Helical; Name=6. {ECO:0000255}.; TRANSMEM 275 295 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 28 Extracellular. {ECO:0000255}.; TOPO_DOM 50 57 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 79 102 Extracellular. {ECO:0000255}.; TOPO_DOM 124 136 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 158 199 Extracellular. {ECO:0000255}.; TOPO_DOM 221 240 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 262 274 Extracellular. {ECO:0000255}.; TOPO_DOM 296 314 Cytoplasmic. {ECO:0000255}. FUNCTION: Potential odorant receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q8VFC9 OL474_MOUSE Olfactory receptor 474 (Olfactory receptor 204-20) 310 34,423 Chain (1); Disulfide bond (1); Glycosylation (3); Topological domain (8); Transmembrane (7) TRANSMEM 26 46 Helical; Name=1. {ECO:0000255}.; TRANSMEM 55 75 Helical; Name=2. {ECO:0000255}.; TRANSMEM 100 120 Helical; Name=3. {ECO:0000255}.; TRANSMEM 134 154 Helical; Name=4. {ECO:0000255}.; TRANSMEM 197 217 Helical; Name=5. {ECO:0000255}.; TRANSMEM 238 258 Helical; Name=6. {ECO:0000255}.; TRANSMEM 272 292 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 25 Extracellular. {ECO:0000255}.; TOPO_DOM 47 54 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 76 99 Extracellular. {ECO:0000255}.; TOPO_DOM 121 133 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 155 196 Extracellular. {ECO:0000255}.; TOPO_DOM 218 237 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 259 271 Extracellular. {ECO:0000255}.; TOPO_DOM 293 310 Cytoplasmic. {ECO:0000255}. FUNCTION: Potential odorant receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q8VGI6 OL477_MOUSE Olfactory receptor 477 (Olfactory receptor 204-1) 310 34,141 Chain (1); Disulfide bond (1); Glycosylation (3); Topological domain (8); Transmembrane (7) TRANSMEM 26 46 Helical; Name=1. {ECO:0000255}.; TRANSMEM 55 75 Helical; Name=2. {ECO:0000255}.; TRANSMEM 100 120 Helical; Name=3. {ECO:0000255}.; TRANSMEM 134 154 Helical; Name=4. {ECO:0000255}.; TRANSMEM 197 217 Helical; Name=5. {ECO:0000255}.; TRANSMEM 238 258 Helical; Name=6. {ECO:0000255}.; TRANSMEM 272 292 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 25 Extracellular. {ECO:0000255}.; TOPO_DOM 47 54 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 76 99 Extracellular. {ECO:0000255}.; TOPO_DOM 121 133 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 155 196 Extracellular. {ECO:0000255}.; TOPO_DOM 218 237 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 259 271 Extracellular. {ECO:0000255}.; TOPO_DOM 293 310 Cytoplasmic. {ECO:0000255}. FUNCTION: Potential odorant receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q8VEZ0 OL480_MOUSE Olfactory receptor 480 (Odorant receptor S25) (Olfactory receptor 204-32) 312 34,729 Chain (1); Disulfide bond (1); Erroneous initiation (1); Glycosylation (2); Topological domain (8); Transmembrane (7) TRANSMEM 26 46 Helical; Name=1. {ECO:0000255}.; TRANSMEM 55 75 Helical; Name=2. {ECO:0000255}.; TRANSMEM 100 120 Helical; Name=3. {ECO:0000255}.; TRANSMEM 134 154 Helical; Name=4. {ECO:0000255}.; TRANSMEM 197 217 Helical; Name=5. {ECO:0000255}.; TRANSMEM 238 258 Helical; Name=6. {ECO:0000255}.; TRANSMEM 272 292 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 25 Extracellular. {ECO:0000255}.; TOPO_DOM 47 54 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 76 99 Extracellular. {ECO:0000255}.; TOPO_DOM 121 133 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 155 196 Extracellular. {ECO:0000255}.; TOPO_DOM 218 237 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 259 271 Extracellular. {ECO:0000255}.; TOPO_DOM 293 312 Cytoplasmic. {ECO:0000255}. "FUNCTION: Probable odorant receptor, which recognizes only aliphatic alcohols, suggesting that it may convey a ""woody"" or ""sweet"" sour. {ECO:0000269|PubMed:11802173}." SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q8VG05 OL483_MOUSE Olfactory receptor 483 (Olfactory receptor 204-12) 315 34,774 Chain (1); Disulfide bond (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 29 49 Helical; Name=1. {ECO:0000255}.; TRANSMEM 58 78 Helical; Name=2. {ECO:0000255}.; TRANSMEM 103 123 Helical; Name=3. {ECO:0000255}.; TRANSMEM 137 157 Helical; Name=4. {ECO:0000255}.; TRANSMEM 201 221 Helical; Name=5. {ECO:0000255}.; TRANSMEM 242 262 Helical; Name=6. {ECO:0000255}.; TRANSMEM 276 296 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 28 Extracellular. {ECO:0000255}.; TOPO_DOM 50 57 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 79 102 Extracellular. {ECO:0000255}.; TOPO_DOM 124 136 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 158 200 Extracellular. {ECO:0000255}.; TOPO_DOM 222 241 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 263 275 Extracellular. {ECO:0000255}.; TOPO_DOM 297 315 Cytoplasmic. {ECO:0000255}. FUNCTION: Potential odorant receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q8VG02 OL488_MOUSE Olfactory receptor 488 (Olfactory receptor 204-15) 314 35,125 Chain (1); Disulfide bond (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 29 49 Helical; Name=1. {ECO:0000255}.; TRANSMEM 58 78 Helical; Name=2. {ECO:0000255}.; TRANSMEM 103 123 Helical; Name=3. {ECO:0000255}.; TRANSMEM 137 157 Helical; Name=4. {ECO:0000255}.; TRANSMEM 200 220 Helical; Name=5. {ECO:0000255}.; TRANSMEM 241 261 Helical; Name=6. {ECO:0000255}.; TRANSMEM 275 295 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 28 Extracellular. {ECO:0000255}.; TOPO_DOM 50 57 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 79 102 Extracellular. {ECO:0000255}.; TOPO_DOM 124 136 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 158 199 Extracellular. {ECO:0000255}.; TOPO_DOM 221 240 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 262 274 Extracellular. {ECO:0000255}.; TOPO_DOM 296 314 Cytoplasmic. {ECO:0000255}. FUNCTION: Potential odorant receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q8VFD1 OL492_MOUSE Olfactory receptor 492 (Olfactory receptor 204-18) 314 34,717 Chain (1); Disulfide bond (1); Glycosylation (2); Topological domain (8); Transmembrane (7) TRANSMEM 29 49 Helical; Name=1. {ECO:0000255}.; TRANSMEM 58 78 Helical; Name=2. {ECO:0000255}.; TRANSMEM 103 123 Helical; Name=3. {ECO:0000255}.; TRANSMEM 137 157 Helical; Name=4. {ECO:0000255}.; TRANSMEM 200 220 Helical; Name=5. {ECO:0000255}.; TRANSMEM 241 261 Helical; Name=6. {ECO:0000255}.; TRANSMEM 275 295 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 28 Extracellular. {ECO:0000255}.; TOPO_DOM 50 57 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 79 102 Extracellular. {ECO:0000255}.; TOPO_DOM 124 136 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 158 199 Extracellular. {ECO:0000255}.; TOPO_DOM 221 240 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 262 274 Extracellular. {ECO:0000255}.; TOPO_DOM 296 314 Cytoplasmic. {ECO:0000255}. FUNCTION: Potential odorant receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q8VG07 OL494_MOUSE Olfactory receptor 494 (Olfactory receptor 204-10) 314 34,658 Chain (1); Disulfide bond (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 29 49 Helical; Name=1. {ECO:0000255}.; TRANSMEM 58 78 Helical; Name=2. {ECO:0000255}.; TRANSMEM 103 123 Helical; Name=3. {ECO:0000255}.; TRANSMEM 137 157 Helical; Name=4. {ECO:0000255}.; TRANSMEM 200 220 Helical; Name=5. {ECO:0000255}.; TRANSMEM 241 261 Helical; Name=6. {ECO:0000255}.; TRANSMEM 275 295 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 28 Extracellular. {ECO:0000255}.; TOPO_DOM 50 57 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 79 102 Extracellular. {ECO:0000255}.; TOPO_DOM 124 136 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 158 199 Extracellular. {ECO:0000255}.; TOPO_DOM 221 240 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 262 274 Extracellular. {ECO:0000255}.; TOPO_DOM 296 314 Cytoplasmic. {ECO:0000255}. FUNCTION: Potential odorant receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q8VF12 OL495_MOUSE Olfactory receptor 495 (Olfactory receptor 204-37) 330 36,873 Chain (1); Disulfide bond (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 29 49 Helical; Name=1. {ECO:0000255}.; TRANSMEM 58 78 Helical; Name=2. {ECO:0000255}.; TRANSMEM 103 123 Helical; Name=3. {ECO:0000255}.; TRANSMEM 137 157 Helical; Name=4. {ECO:0000255}.; TRANSMEM 200 220 Helical; Name=5. {ECO:0000255}.; TRANSMEM 241 261 Helical; Name=6. {ECO:0000255}.; TRANSMEM 275 295 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 28 Extracellular. {ECO:0000255}.; TOPO_DOM 50 57 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 79 102 Extracellular. {ECO:0000255}.; TOPO_DOM 124 136 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 158 199 Extracellular. {ECO:0000255}.; TOPO_DOM 221 240 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 262 274 Extracellular. {ECO:0000255}.; TOPO_DOM 296 330 Cytoplasmic. {ECO:0000255}. FUNCTION: Potential odorant receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q8VEW2 OL498_MOUSE Olfactory receptor 498 (Olfactory receptor 204-36) 330 36,854 Chain (1); Disulfide bond (1); Glycosylation (1); Sequence conflict (1); Topological domain (8); Transmembrane (7) TRANSMEM 29 49 Helical; Name=1. {ECO:0000255}.; TRANSMEM 58 78 Helical; Name=2. {ECO:0000255}.; TRANSMEM 103 123 Helical; Name=3. {ECO:0000255}.; TRANSMEM 137 157 Helical; Name=4. {ECO:0000255}.; TRANSMEM 200 220 Helical; Name=5. {ECO:0000255}.; TRANSMEM 241 261 Helical; Name=6. {ECO:0000255}.; TRANSMEM 275 295 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 28 Extracellular. {ECO:0000255}.; TOPO_DOM 50 57 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 79 102 Extracellular. {ECO:0000255}.; TOPO_DOM 124 136 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 158 199 Extracellular. {ECO:0000255}.; TOPO_DOM 221 240 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 262 274 Extracellular. {ECO:0000255}.; TOPO_DOM 296 330 Cytoplasmic. {ECO:0000255}. FUNCTION: Potential odorant receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q8VG09 OL502_MOUSE Olfactory receptor 502 (Olfactory receptor 204-8) 314 34,550 Chain (1); Disulfide bond (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 29 49 Helical; Name=1. {ECO:0000255}.; TRANSMEM 58 78 Helical; Name=2. {ECO:0000255}.; TRANSMEM 103 123 Helical; Name=3. {ECO:0000255}.; TRANSMEM 137 157 Helical; Name=4. {ECO:0000255}.; TRANSMEM 200 220 Helical; Name=5. {ECO:0000255}.; TRANSMEM 241 261 Helical; Name=6. {ECO:0000255}.; TRANSMEM 275 295 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 28 Extracellular. {ECO:0000255}.; TOPO_DOM 50 57 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 79 102 Extracellular. {ECO:0000255}.; TOPO_DOM 124 136 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 158 199 Extracellular. {ECO:0000255}.; TOPO_DOM 221 240 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 262 274 Extracellular. {ECO:0000255}.; TOPO_DOM 296 314 Cytoplasmic. {ECO:0000255}. FUNCTION: Potential odorant receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q8VG13 OL507_MOUSE Olfactory receptor 507 (Olfactory receptor 204-7) 316 34,824 Chain (1); Disulfide bond (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 29 49 Helical; Name=1. {ECO:0000255}.; TRANSMEM 58 78 Helical; Name=2. {ECO:0000255}.; TRANSMEM 103 123 Helical; Name=3. {ECO:0000255}.; TRANSMEM 137 157 Helical; Name=4. {ECO:0000255}.; TRANSMEM 200 220 Helical; Name=5. {ECO:0000255}.; TRANSMEM 241 261 Helical; Name=6. {ECO:0000255}.; TRANSMEM 275 297 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 28 Extracellular. {ECO:0000255}.; TOPO_DOM 50 57 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 79 102 Extracellular. {ECO:0000255}.; TOPO_DOM 124 136 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 158 199 Extracellular. {ECO:0000255}.; TOPO_DOM 221 240 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 262 274 Extracellular. {ECO:0000255}.; TOPO_DOM 298 316 Cytoplasmic. {ECO:0000255}. FUNCTION: Potential odorant receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q8VEW6 OL510_MOUSE Olfactory receptor 510 (Olfactory receptor 204-34) 314 34,883 Chain (1); Disulfide bond (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 29 49 Helical; Name=1. {ECO:0000255}.; TRANSMEM 58 78 Helical; Name=2. {ECO:0000255}.; TRANSMEM 103 123 Helical; Name=3. {ECO:0000255}.; TRANSMEM 137 157 Helical; Name=4. {ECO:0000255}.; TRANSMEM 200 220 Helical; Name=5. {ECO:0000255}.; TRANSMEM 241 261 Helical; Name=6. {ECO:0000255}.; TRANSMEM 275 295 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 28 Extracellular. {ECO:0000255}.; TOPO_DOM 50 57 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 79 102 Extracellular. {ECO:0000255}.; TOPO_DOM 124 136 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 158 199 Extracellular. {ECO:0000255}.; TOPO_DOM 221 240 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 262 274 Extracellular. {ECO:0000255}.; TOPO_DOM 296 314 Cytoplasmic. {ECO:0000255}. FUNCTION: Potential odorant receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q6W049 OL688_MOUSE Olfactory receptor 688 321 35,690 Chain (1); Disulfide bond (1); Erroneous gene model prediction (1); Topological domain (8); Transmembrane (7) TRANSMEM 37 57 Helical; Name=1. {ECO:0000255}.; TRANSMEM 71 91 Helical; Name=2. {ECO:0000255}.; TRANSMEM 106 126 Helical; Name=3. {ECO:0000255}.; TRANSMEM 129 149 Helical; Name=4. {ECO:0000255}.; TRANSMEM 208 228 Helical; Name=5. {ECO:0000255}.; TRANSMEM 251 271 Helical; Name=6. {ECO:0000255}.; TRANSMEM 276 296 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 36 Extracellular. {ECO:0000255}.; TOPO_DOM 58 70 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 92 105 Extracellular. {ECO:0000255}.; TOPO_DOM 127 128 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 150 207 Extracellular. {ECO:0000255}.; TOPO_DOM 229 250 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 272 275 Extracellular. {ECO:0000255}.; TOPO_DOM 297 321 Cytoplasmic. {ECO:0000255}. FUNCTION: Odorant receptor. {ECO:0000303|PubMed:14611657, ECO:0000305}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8VEY3 OL958_MOUSE Olfactory receptor 958 (Olfactory receptor 224-9) 312 34,528 Chain (1); Disulfide bond (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 27 47 Helical; Name=1. {ECO:0000255}.; TRANSMEM 58 78 Helical; Name=2. {ECO:0000255}.; TRANSMEM 98 118 Helical; Name=3. {ECO:0000255}.; TRANSMEM 140 160 Helical; Name=4. {ECO:0000255}.; TRANSMEM 198 218 Helical; Name=5. {ECO:0000255}.; TRANSMEM 240 260 Helical; Name=6. {ECO:0000255}.; TRANSMEM 267 287 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 26 Extracellular. {ECO:0000255}.; TOPO_DOM 48 57 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 79 97 Extracellular. {ECO:0000255}.; TOPO_DOM 119 139 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 161 197 Extracellular. {ECO:0000255}.; TOPO_DOM 219 239 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 261 266 Extracellular. {ECO:0000255}.; TOPO_DOM 288 312 Cytoplasmic. {ECO:0000255}. FUNCTION: Potential odorant receptor. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q60883 OLF10_MOUSE Olfactory receptor 10 (Odorant receptor L45) 311 34,270 Chain (1); Disulfide bond (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 26 46 Helical; Name=1. {ECO:0000255}.; TRANSMEM 58 78 Helical; Name=2. {ECO:0000255}.; TRANSMEM 100 120 Helical; Name=3. {ECO:0000255}.; TRANSMEM 134 154 Helical; Name=4. {ECO:0000255}.; TRANSMEM 198 218 Helical; Name=5. {ECO:0000255}.; TRANSMEM 236 256 Helical; Name=6. {ECO:0000255}.; TRANSMEM 271 291 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 25 Extracellular. {ECO:0000255}.; TOPO_DOM 47 57 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 79 99 Extracellular. {ECO:0000255}.; TOPO_DOM 121 133 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 155 197 Extracellular. {ECO:0000255}.; TOPO_DOM 219 235 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 257 270 Extracellular. {ECO:0000255}.; TOPO_DOM 292 311 Cytoplasmic. {ECO:0000255}. FUNCTION: Odorant receptor. {ECO:0000305}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +P34984 OLF13_MOUSE Olfactory receptor 13 (Odorant receptor K7) (Olfactory receptor 261-6) 310 34,569 Chain (1); Disulfide bond (1); Glycosylation (2); Topological domain (8); Transmembrane (7) TRANSMEM 25 45 Helical; Name=1. {ECO:0000255}.; TRANSMEM 54 74 Helical; Name=2. {ECO:0000255}.; TRANSMEM 97 117 Helical; Name=3. {ECO:0000255}.; TRANSMEM 149 169 Helical; Name=4. {ECO:0000255}.; TRANSMEM 205 225 Helical; Name=5. {ECO:0000255}.; TRANSMEM 240 260 Helical; Name=6. {ECO:0000255}.; TRANSMEM 274 291 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 24 Extracellular. {ECO:0000255}.; TOPO_DOM 46 53 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 75 96 Extracellular. {ECO:0000255}.; TOPO_DOM 118 148 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 170 204 Extracellular. {ECO:0000255}.; TOPO_DOM 226 239 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 261 273 Extracellular. {ECO:0000255}.; TOPO_DOM 292 310 Cytoplasmic. {ECO:0000255}. FUNCTION: Odorant receptor. {ECO:0000305}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Olfactory epithelium. +Q0VAX9 OLF18_MOUSE Olfactory receptor 18 (Olfactory receptor 145-1) (Olfactory receptor TPCR34) 331 37,358 Chain (1); Disulfide bond (1); Glycosylation (1); Sequence conflict (1); Topological domain (8); Transmembrane (7) TRANSMEM 48 68 Helical; Name=1. {ECO:0000255}.; TRANSMEM 81 100 Helical; Name=2. {ECO:0000255}.; TRANSMEM 120 140 Helical; Name=3. {ECO:0000255}.; TRANSMEM 165 185 Helical; Name=4. {ECO:0000255}.; TRANSMEM 219 239 Helical; Name=5. {ECO:0000255}.; TRANSMEM 267 287 Helical; Name=6. {ECO:0000255}.; TRANSMEM 294 314 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 47 Extracellular. {ECO:0000255}.; TOPO_DOM 69 80 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 101 119 Extracellular. {ECO:0000255}.; TOPO_DOM 141 164 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 186 218 Extracellular. {ECO:0000255}.; TOPO_DOM 240 266 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 288 293 Extracellular. {ECO:0000255}.; TOPO_DOM 315 331 Cytoplasmic. {ECO:0000255}. FUNCTION: Odorant receptor. {ECO:0000305}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q9JHB2 OLF19_MOUSE Olfactory receptor 19 (Odorant receptor M12) (Olfactory receptor 140-1) 309 34,661 Chain (1); Disulfide bond (1); Glycosylation (1); Sequence conflict (3); Topological domain (8); Transmembrane (7) TRANSMEM 27 47 Helical; Name=1. {ECO:0000255}.; TRANSMEM 58 78 Helical; Name=2. {ECO:0000255}.; TRANSMEM 98 118 Helical; Name=3. {ECO:0000255}.; TRANSMEM 140 160 Helical; Name=4. {ECO:0000255}.; TRANSMEM 197 217 Helical; Name=5. {ECO:0000255}.; TRANSMEM 245 265 Helical; Name=6. {ECO:0000255}.; TRANSMEM 270 292 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 26 Extracellular. {ECO:0000255}.; TOPO_DOM 48 57 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 79 97 Extracellular. {ECO:0000255}.; TOPO_DOM 119 139 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 161 196 Extracellular. {ECO:0000255}.; TOPO_DOM 218 244 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 266 269 Extracellular. {ECO:0000255}.; TOPO_DOM 293 309 Cytoplasmic. {ECO:0000255}. FUNCTION: Odorant receptor. {ECO:0000305}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q8VGI1 OLF1_MOUSE Olfactory receptor 1 (Odorant receptor I54) (Olfactory receptor 135-13) 314 35,479 Chain (1); Disulfide bond (1); Glycosylation (3); Topological domain (8); Transmembrane (7) TRANSMEM 30 50 Helical; Name=1. {ECO:0000255}.; TRANSMEM 58 78 Helical; Name=2. {ECO:0000255}.; TRANSMEM 98 118 Helical; Name=3. {ECO:0000255}.; TRANSMEM 144 164 Helical; Name=4. {ECO:0000255}.; TRANSMEM 197 217 Helical; Name=5. {ECO:0000255}.; TRANSMEM 240 260 Helical; Name=6. {ECO:0000255}.; TRANSMEM 272 292 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 29 Extracellular. {ECO:0000255}.; TOPO_DOM 51 57 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 79 97 Extracellular. {ECO:0000255}.; TOPO_DOM 119 143 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 165 196 Extracellular. {ECO:0000255}.; TOPO_DOM 218 239 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 261 271 Extracellular. {ECO:0000255}.; TOPO_DOM 293 314 Cytoplasmic. {ECO:0000255}. FUNCTION: Odorant receptor. Activated by a lily-derived aldehyde as well as other odorants. May signal through an inositol 1,4,5-trisphosphate (IP3) second messenger system (By similarity). {ECO:0000250|UniProtKB:P70526}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Olfactory epithelium. {ECO:0000269|PubMed:8087849}. +Q8VFM9 OLF24_MOUSE Olfactory receptor 24 (Olfactory receptor 132-1) (Olfactory receptor TPCR51) 313 34,863 Chain (1); Disulfide bond (1); Glycosylation (2); Topological domain (8); Transmembrane (7) TRANSMEM 26 46 Helical; Name=1. {ECO:0000255}.; TRANSMEM 55 75 Helical; Name=2. {ECO:0000255}.; TRANSMEM 98 118 Helical; Name=3. {ECO:0000255}.; TRANSMEM 143 163 Helical; Name=4. {ECO:0000255}.; TRANSMEM 197 217 Helical; Name=5. {ECO:0000255}.; TRANSMEM 245 265 Helical; Name=6. {ECO:0000255}.; TRANSMEM 275 292 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 25 Extracellular. {ECO:0000255}.; TOPO_DOM 47 54 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 76 97 Extracellular. {ECO:0000255}.; TOPO_DOM 119 142 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 164 196 Extracellular. {ECO:0000255}.; TOPO_DOM 218 244 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 266 274 Extracellular. {ECO:0000255}.; TOPO_DOM 293 313 Cytoplasmic. {ECO:0000255}. FUNCTION: Odorant receptor. {ECO:0000305}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:9119360}. +Q9Z0E1 M1AP_MOUSE Meiosis 1 arrest protein (Meiosis 1-arresting protein) (Meiosis 1-associated protein) (Spermatogenesis-associated protein 37) 529 58,618 Chain (1); Modified residue (1); Sequence conflict (2) FUNCTION: Required for meiosis I progression during spermatogenesis. {ECO:0000269|PubMed:23269666}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23269666}. TISSUE SPECIFICITY: Expressed in germ cells of the testis. Expressed from spermatogonia to spermatids. Expressed at very low levels in lung, stomach, thymus. Not detected in Sertoli cells. {ECO:0000269|PubMed:16881047, ECO:0000269|PubMed:23269666, ECO:0000269|PubMed:9927484}. +P97412 LYST_MOUSE Lysosomal-trafficking regulator (Beige protein) (CHS1 homolog) 3788 425,287 Alternative sequence (2); Chain (1); Domain (2); Modified residue (10); Repeat (7) FUNCTION: May be required for sorting endosomal resident proteins into late multivesicular endosomes by a mechanism involving microtubules. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. SUBUNIT: Interacts with CENPJ, LIP8 and ZNF521. {ECO:0000250}. DISEASE: Note=Defects in Lyst are the cause of beige, an autosomal recessive disorder characterized by hypopigmentation, bleeding, immune cell dysfunction, abnormal intracellular transport to and from the lysosome, and giant inclusion bodies in a variety of cell types. +Q9CR62 M2OM_MOUSE Mitochondrial 2-oxoglutarate/malate carrier protein (OGCP) (Solute carrier family 25 member 11) 314 34,155 Chain (1); Initiator methionine (1); Modified residue (6); Repeat (3); Transmembrane (6) TRANSMEM 24 42 Helical; Name=1. {ECO:0000255}.; TRANSMEM 83 101 Helical; Name=2. {ECO:0000255}.; TRANSMEM 119 140 Helical; Name=3. {ECO:0000255}.; TRANSMEM 183 202 Helical; Name=4. {ECO:0000255}.; TRANSMEM 222 240 Helical; Name=5. {ECO:0000255}.; TRANSMEM 281 300 Helical; Name=6. {ECO:0000255}. FUNCTION: Catalyzes the transport of 2-oxoglutarate across the inner mitochondrial membrane in an electroneutral exchange for malate or other dicarboxylic acids, and plays an important role in several metabolic processes, including the malate-aspartate shuttle, the oxoglutarate/isocitrate shuttle, in gluconeogenesis from lactate, and in nitrogen metabolism (By similarity). Maintains mitochondrial fusion and fission events, and the organization and morphology of cristae (By similarity). Involved in the regulation of apoptosis (PubMed:21448454). {ECO:0000250|UniProtKB:P97700, ECO:0000250|UniProtKB:Q02978, ECO:0000269|PubMed:21448454}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P97700}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P97700}. +Q99N09 M4A6B_MOUSE Membrane-spanning 4-domains subfamily A member 6B 244 26,860 Chain (1); Sequence conflict (2); Topological domain (5); Transmembrane (4) TRANSMEM 47 67 Helical. {ECO:0000255}.; TRANSMEM 85 105 Helical. {ECO:0000255}.; TRANSMEM 122 142 Helical. {ECO:0000255}.; TRANSMEM 177 197 Helical. {ECO:0000255}. TOPO_DOM 1 46 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 68 84 Extracellular. {ECO:0000255}.; TOPO_DOM 106 121 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 143 176 Extracellular. {ECO:0000255}.; TOPO_DOM 198 244 Cytoplasmic. {ECO:0000255}. FUNCTION: May be involved in signal transduction as a component of a multimeric receptor complex. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed at high levels in thymus, spleen, and peripheral lymph nodes, with less abundant levels in non-lymphoid tissues. +P27046 MA2A1_MOUSE Alpha-mannosidase 2 (EC 3.2.1.114) (Golgi alpha-mannosidase II) (AMan II) (Man II) (Mannosidase alpha class 2A member 1) (Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase) 1150 131,631 Active site (1); Chain (1); Glycosylation (3); Metal binding (4); Modified residue (2); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 6 26 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 5 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 27 1150 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Catalyzes the first committed step in the biosynthesis of complex N-glycans. It controls conversion of high mannose to complex N-glycans; the final hydrolytic step in the N-glycan maturation pathway. {ECO:0000250|UniProtKB:P28494}. PTM: Glycosylated. {ECO:0000250|UniProtKB:P28494}. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein. SUBUNIT: Homodimer; disulfide-linked. TISSUE SPECIFICITY: All tissues, mostly in adrenal and thymus. +Q8BRK9 MA2A2_MOUSE Alpha-mannosidase 2x (EC 3.2.1.114) (Alpha-mannosidase IIx) (Man IIx) (Mannosidase alpha class 2A member 2) (Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase) 1152 130,649 Active site (1); Alternative sequence (2); Chain (1); Coiled coil (1); Glycosylation (2); Metal binding (4); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 6 26 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 5 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 27 796 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Catalyzes the first committed step in the biosynthesis of complex N-glycans. It controls conversion of high mannose to complex N-glycans; the final hydrolytic step in the N-glycan maturation pathway (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. SUBUNIT: Homodimer; disulfide-linked (By similarity). Interacts with MGAT4D. {ECO:0000250, ECO:0000269|PubMed:20805325}. +Q99JP0 M4K3_MOUSE Mitogen-activated protein kinase kinase kinase kinase 3 (EC 2.7.11.1) (Germinal center kinase-related protein kinase) (GLK) (MAPK/ERK kinase kinase kinase 3) (MEK kinase kinase 3) (MEKKK 3) 894 101,119 Active site (1); Binding site (1); Chain (1); Domain (2); Modified residue (3); Nucleotide binding (1); Sequence conflict (1) FUNCTION: May play a role in the response to environmental stress. Appears to act upstream of the JUN N-terminal pathway (By similarity). {ECO:0000250}. SUBUNIT: Interacts with SH3GL2. Interaction appears to regulate MAP4K3-mediated JNK activation (By similarity). {ECO:0000250|UniProtKB:Q924I2}. +A2AJI0 MA7D1_MOUSE MAP7 domain-containing protein 1 846 93,276 Alternative sequence (1); Chain (1); Coiled coil (3); Compositional bias (2); Cross-link (1); Erroneous initiation (2); Modified residue (25); Sequence caution (1); Sequence conflict (1) SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle {ECO:0000250}. +Q4VC33 MAEA_MOUSE E3 ubiquitin-protein transferase MAEA (EC 2.3.2.27) (Erythroblast macrophage protein) (Macrophage erythroblast attacher) 396 45,336 Alternative sequence (1); Chain (1); Domain (2); Erroneous initiation (1); Modified residue (1); Region (1); Sequence conflict (4); Site (1); Zinc finger (1) FUNCTION: Core component of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1. MAEA and RMND5A are both required for catalytic activity of the CTLH E3 ubiquitin-protein ligase complex. MAEA is required for normal cell proliferation. The CTLH E3 ubiquitin-protein ligase complex is not required for the degradation of enzymes involved in gluconeogenesis, such as FBP1 (By similarity). Plays a role in erythroblast enucleation during erythrocyte maturation and in the development of mature macrophages (PubMed:16707498). Mediates the attachment of erythroid cell to mature macrophages; this MAEA-mediated contact inhibits erythroid cell apoptosis (By similarity). Participates in erythroblastic island formation, which is the functional unit of definitive erythropoiesis (PubMed:16707498, PubMed:17071116). Associates with F-actin to regulate actin distribution in erythroblasts and macrophages (PubMed:16707498). May contribute to nuclear architecture and cells division events (By similarity). {ECO:0000250|UniProtKB:Q7L5Y9, ECO:0000269|PubMed:16707498, ECO:0000269|PubMed:17071116}. PTM: Autoubiquitinated as component of the CTLH E3 ubiquitin-protein ligase complex (in vitro). {ECO:0000250|UniProtKB:Q7L5Y9}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17071116}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q7L5Y9}. Nucleus matrix {ECO:0000269|PubMed:17071116}. Cell membrane {ECO:0000269|PubMed:17071116}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16707498, ECO:0000269|PubMed:17071116}. Note=Detected in a nuclear, speckled-like pattern (PubMed:17071116). Localized with condensed chromatin at prophase; Detected in nuclear spindle poles at metaphase and in the contractile ring during telophase and cytokinesis (By similarity). Present in cytoplasm, nuclear matrix and at the cell surface in macrophages; predominantly nuclear in immature macrophages and predominantly detected at the cell surface in mature macrophages (PubMed:17071116). Colocalizes with F-actin in macrophages (PubMed:16707498). {ECO:0000250|UniProtKB:Q7L5Y9, ECO:0000269|PubMed:16707498, ECO:0000269|PubMed:17071116}. SUBUNIT: Identified in the CTLH complex that contains GID4, RANBP9 and/or RANBP10, MKLN1, MAEA, RMND5A (or alternatively its paralog RMND5B), GID8, ARMC8, WDR26 and YPEL5. Within this complex, MAEA, RMND5A (or alternatively its paralog RMND5B), GID8, WDR26, and RANBP9 and/or RANBP10 form the catalytic core, while GID4, MKLN1, ARMC8 and YPEL5 have ancillary roles (By similarity). Interacts with F-actin (PubMed:16707498). {ECO:0000250|UniProtKB:Q7L5Y9, ECO:0000269|PubMed:16707498}. DOMAIN: The expected RING-type zinc finger domain is highly divergent and most of the expected Cys residues are not conserved. Still, the protein is required for CTLH complex E3 ubiquitin-protein transferase activity. In addition, the conserved Cys-314 in this highly divergent region is required for ubiquitination by the yeast GID complex, suggesting a direct role in catalyzing ubiquitination. {ECO:0000250|UniProtKB:Q7L5Y9}. TISSUE SPECIFICITY: Detected in embryonic fibroblasts (PubMed:16707498). Detected in macrophages (PubMed:17071116). Detected in heart. liver, spleen and kidney (at protein level) (PubMed:16510120). {ECO:0000269|PubMed:16510120, ECO:0000269|PubMed:16707498, ECO:0000269|PubMed:17071116}. +P0C6A2 MAMD1_MOUSE Mastermind-like domain-containing protein 1 803 87,598 Chain (1) FUNCTION: Transactivates the HES3 promoter independently of NOTCH proteins. HES3 is a non-canonical NOTCH target gene which lacks binding sites for RBPJ (By similarity). Required for testosterone production. {ECO:0000250, ECO:0000269|PubMed:18162467}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Punctate nuclear localization. {ECO:0000250}. +Q9D956 MALD3_MOUSE MARVEL domain-containing protein 3 376 42,146 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (1); Sequence conflict (1); Topological domain (5); Transmembrane (4) TRANSMEM 174 194 Helical. {ECO:0000255}.; TRANSMEM 248 268 Helical. {ECO:0000255}.; TRANSMEM 276 296 Helical. {ECO:0000255}.; TRANSMEM 336 356 Helical. {ECO:0000255}. TOPO_DOM 1 173 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 195 247 Extracellular. {ECO:0000255}.; TOPO_DOM 269 275 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 297 335 Extracellular. {ECO:0000255}.; TOPO_DOM 357 376 Cytoplasmic. {ECO:0000255}. FUNCTION: As a component of tight junctions, plays a role in paracellular ion conductivity. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cell junction, tight junction {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed with highest levels in small intestine, colon, stomach and lung. Liver expresses only isoform 2. {ECO:0000269|PubMed:20028514}. +Q6NXH2 MANEA_MOUSE Glycoprotein endo-alpha-1,2-mannosidase (Endo-alpha mannosidase) (Endomannosidase) (mEndo) (EC 3.2.1.130) 462 53,183 Chain (1); Region (1); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 10 30 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 9 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 31 462 Lumenal. {ECO:0000255}. PTM: Undergoes proteolytic cleavage in the C-terminal region. {ECO:0000250|UniProtKB:Q5GF25}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q5GF25}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q5GF25}. +O35701 MATN3_MOUSE Matrilin-3 481 51,845 Chain (1); Coiled coil (1); Disulfide bond (12); Domain (5); Glycosylation (1); Modified residue (2); Sequence conflict (1); Signal peptide (1) FUNCTION: Major component of the extracellular matrix of cartilage and may play a role in the formation of extracellular filamentous networks. {ECO:0000269|PubMed:10660556}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10660556}. SUBUNIT: Can form homooligomers (monomers, dimers, trimers and tetramers) and heterooligomers with matrilin-1. Interacts with COMP (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Strongly expressed in growing skeletal tissue such as epiphyseal growth plate or in bone undergoing growth and remodeling. In the bone, actively synthesized in osteoblasts and osteocytes. Expressed in cartilage of sternum, femur, vertebrae, trachea, articular and epiphyseal cartilage, cartilage of developing bones and bones. +Q8C181 MBNL2_MOUSE Muscleblind-like protein 2 373 40,156 Alternative sequence (3); Chain (1); Erroneous initiation (1); Sequence conflict (1); Zinc finger (4) FUNCTION: Mediates pre-mRNA alternative splicing regulation. Acts either as activator or repressor of splicing on specific pre-mRNA targets. Inhibits cardiac troponin-T (TNNT2) pre-mRNA exon inclusion but induces insulin receptor (IR) pre-mRNA exon inclusion in muscle. Antagonizes the alternative splicing activity pattern of CELF proteins. RNA-binding protein that binds to 5'ACACCC-3' core sequence, termed zipcode, within the 3'UTR of ITGA3. Binds to CUG triplet repeat expansion in myotonic dystrophy muscle cells by sequestering the target RNAs. Seems to regulate expression and localization of ITGA3 by transporting it from the nucleus to cytoplasm at adhesion plaques. May play a role in myotonic dystrophy pathophysiology (DM) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5VZF2}. Cytoplasm {ECO:0000250|UniProtKB:Q5VZF2}. Note=Greater concentration in the nucleus. Expressed in or near large cytoplasmic adhesion plaques. Location in the cytoplasm is microtubule-dependent. {ECO:0000250|UniProtKB:Q5VZF2}. SUBUNIT: Interacts with ITGA3. {ECO:0000250}. +Q8BH98 MBOA1_MOUSE Lysophospholipid acyltransferase 1 (LPLAT 1) (EC 2.3.1.-) (1-acylglycerophosphoethanolamine O-acyltransferase) (EC 2.3.1.n7) (1-acylglycerophosphoserine O-acyltransferase) (EC 2.3.1.n6) (Lysophosphatidylethanolamine acyltransferase) (LPEAT) (Lyso-PE acyltransferase) (Lysophosphatidylserine acyltransferase) (LPSAT) (Lyso-PS acyltransferase) (Membrane-bound O-acyltransferase domain-containing protein 1) (O-acyltransferase domain-containing protein 1) 492 56,160 Active site (2); Chain (1); Modified residue (1); Sequence conflict (3); Transmembrane (9) TRANSMEM 33 53 Helical. {ECO:0000255}.; TRANSMEM 69 89 Helical. {ECO:0000255}.; TRANSMEM 125 145 Helical. {ECO:0000255}.; TRANSMEM 179 199 Helical. {ECO:0000255}.; TRANSMEM 237 257 Helical. {ECO:0000255}.; TRANSMEM 296 316 Helical. {ECO:0000255}.; TRANSMEM 370 390 Helical. {ECO:0000255}.; TRANSMEM 423 443 Helical. {ECO:0000255}.; TRANSMEM 452 472 Helical. {ECO:0000255}. Lipid metabolism; phospholipid metabolism. FUNCTION: Acyltransferase which mediates the conversion of lysophosphatidylethanolamine (1-acyl-sn-glycero-3-phosphoethanolamine or LPE) into phosphatidylethanolamine (1,2-diacyl-sn-glycero-3-phosphoethanolamine or PE) (LPEAT activity). Catalyzes also the acylation of lysophosphatidylserine (1-acyl-2-hydroxy-sn-glycero-3-phospho-L-serine or LPS) into phosphatidylserine (1,2-diacyl-sn-glycero-3-phospho-L-serine or PS) (LPSAT activity). Prefers oleoyl-CoA as the acyl donor. Lysophospholipid acyltransferases (LPLATs) catalyze the reacylation step of the phospholipid remodeling pathway also known as the Lands cycle. {ECO:0000269|PubMed:18287005}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Endoplasmic reticulum {ECO:0000269|PubMed:18287005}. TISSUE SPECIFICITY: Highly expressed in stomach, epididymis, and colon. {ECO:0000269|PubMed:18287005}. +Q9D0L8 MCES_MOUSE mRNA cap guanine-N7 methyltransferase (EC 2.1.1.56) (RG7MT1) (mRNA (guanine-N(7)-)-methyltransferase) (mRNA cap methyltransferase) 465 53,291 Alternative sequence (2); Binding site (6); Chain (1); Domain (1); Erroneous initiation (1); Modified residue (5); Motif (1); Region (1); Sequence conflict (2); Site (6) FUNCTION: Catalytic subunit of the mRNA-capping methyltransferase RNMT:RAMAC complex that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs. Binds RNA containing 5'-terminal GpppC. {ECO:0000250|UniProtKB:O43148}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O43148}. SUBUNIT: Interacts with importin alpha, leading to stimulate both RNA-binding and methyltransferase activity. Interaction with importin alpha and beta is required for its nuclear localization, importin beta dissociating in response to RanGTP, allowing RNMT-importin alpha to bind RNA substrates. Interacts with elongating form of polymerase II and RNGTT. Interacts with RAMAC, this interaction significantly enhances RNA-binding and cap methyltransferase activity. {ECO:0000250|UniProtKB:O43148}. +Q0VBD2 MCM10_MOUSE Protein MCM10 homolog 885 98,406 Chain (1); Coiled coil (1); Cross-link (3); Modified residue (2); Region (5); Sequence conflict (3) FUNCTION: Acts as a replication initiation factor that brings together the MCM2-7 helicase and the DNA polymerase alpha/primase complex in order to initiate DNA replication. Additionally, plays a role in preventing DNA damage during replication. Key effector of the RBBP6 and ZBTB38-mediated regulation of DNA-replication and common fragile sites stability; acts as a direct target of transcriptional repression by ZBTB38 (By similarity). {ECO:0000250|UniProtKB:Q7L590}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q7L590}. Note=Colocalizes with ORC2 in nuclei foci. Associated with chromatin in S phase (By similarity). {ECO:0000250|UniProtKB:Q7L590}. SUBUNIT: Self-associates (By similarity). Interacts with ORC2. May interact with MCM2 and MCM6. Interacts with the DNA polymerase alpha subunit POLA1. Interacts with RECQL4; this interaction regulates RECQL4 unwinding activity. Interacts with WDHD1 (By similarity). {ECO:0000250|UniProtKB:Q5EAW4, ECO:0000250|UniProtKB:Q7L590}. DOMAIN: Each zinc finger-like domain binds a zinc ion and is involved in both ssDNA and dsDNA binding, as is the OB-fold domain. {ECO:0000250|UniProtKB:Q5EAW4}.; DOMAIN: The N-terminal domain mediates homodimerization. {ECO:0000250|UniProtKB:Q5EAW4}. +Q9D1I5 MCEE_MOUSE Methylmalonyl-CoA epimerase, mitochondrial (EC 5.1.99.1) (DL-methylmalonyl-CoA racemase) 178 19,017 Chain (1); Compositional bias (1); Domain (1); Metal binding (3); Modified residue (3); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}. +P97287 MCL1_MOUSE Induced myeloid leukemia cell differentiation protein Mcl-1 homolog (Bcl-2-related protein EAT/mcl1) 331 35,217 Alternative sequence (1); Beta strand (1); Chain (1); Compositional bias (1); Cross-link (3); Helix (9); Modified residue (4); Motif (3); Region (1); Site (2); Transmembrane (1); Turn (2) TRANSMEM 308 330 Helical. {ECO:0000255}. FUNCTION: Involved in the regulation of apoptosis versus cell survival, and in the maintenance of viability but not of proliferation. Mediates its effects by interactions with a number of other regulators of apoptosis. Isoform 2 has antiapoptotic activity. {ECO:0000269|PubMed:16543145, ECO:0000269|PubMed:19919825}. PTM: Cleaved by CASP3 during apoptosis, yielding a pro-apoptotic C-terminal fragment. {ECO:0000250}.; PTM: Rapidly degraded in the absence of phosphorylation in the PEST region. {ECO:0000250}.; PTM: Phosphorylated on Ser-140, by GSK3, in response to IL3/interleukin-3 withdrawal. Phosphorylation at Ser-140 induces ubiquitination and proteasomal degradation, abrogating the anti-apoptotic activity. Treatment with taxol or okadaic acid induces phosphorylation on additional sites. {ECO:0000269|PubMed:16543145}.; PTM: Ubiquitinated. Ubiquitination is induced by phosphorylation at Ser-140 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Mitochondrion. Nucleus, nucleoplasm {ECO:0000250}. Note=Cytoplasmic, associated with mitochondria. SUBUNIT: Interacts with HIF3A isoform 2 (via C-terminus domain) (PubMed:21546903). Interacts with BAD, BOK, BIK, BAX, BAK1, and TPT1. Interacts with BBC3, BMF and PMAIP1 (PubMed:15550399, PubMed:18589438). Interacts with BOP. Interacts with BCL2L11; this interaction may sequester BCL2L11 and prevent its pro-apoptotic activity (PubMed:16543145, PubMed:27013495, PubMed:15550399). {ECO:0000269|PubMed:15550399, ECO:0000269|PubMed:16543145, ECO:0000269|PubMed:18589438, ECO:0000269|PubMed:21546903, ECO:0000269|PubMed:27013495}. +Q8CHX6 MBTP2_MOUSE Membrane-bound transcription factor site-2 protease (EC 3.4.24.85) (Endopeptidase S2P) 515 56,960 Active site (1); Chain (1); Compositional bias (2); Glycosylation (1); Metal binding (2); Topological domain (6); Transmembrane (10) TRANSMEM 4 24 Helical. {ECO:0000255}.; TRANSMEM 75 95 Helical. {ECO:0000255}.; TRANSMEM 96 107 Helical. {ECO:0000255}.; TRANSMEM 141 165 Helical. {ECO:0000255}.; TRANSMEM 170 182 Helical. {ECO:0000255}.; TRANSMEM 183 205 Helical. {ECO:0000255}.; TRANSMEM 225 247 Helical. {ECO:0000255}.; TRANSMEM 443 460 Helical. {ECO:0000255}.; TRANSMEM 461 472 Helical. {ECO:0000255}.; TRANSMEM 489 509 Helical. {ECO:0000255}. TOPO_DOM 1 3 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 25 74 Lumenal. {ECO:0000250}.; TOPO_DOM 108 140 Lumenal. {ECO:0000250}.; TOPO_DOM 248 442 Lumenal. {ECO:0000250}.; TOPO_DOM 473 488 Lumenal. {ECO:0000255}.; TOPO_DOM 510 515 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in regulated intramembrane proteolysis (RIP) that is the cleavage of membrane-spanning regulatory proteins by proteases within the plane of the membrane. It cleaves sterol-regulatory element-binding proteins (SREBPs) within the first transmembrane segment, thereby releasing the N-terminal segment with a portion of the transmembrane segment attached. Mature N-terminal fragments shuttle to the nucleus and activate gene transcription. Involved in RIP-mediated regulation of bone formation. {ECO:0000250|UniProtKB:O43462}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm {ECO:0000250}. +Q8BH27 MEGF9_MOUSE Multiple epidermal growth factor-like domains protein 9 (Multiple EGF-like domains protein 9) (Epidermal growth factor-like protein 5) (EGF-like protein 5) 600 62,831 Chain (1); Disulfide bond (20); Domain (5); Glycosylation (12); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 513 533 Helical. {ECO:0000255}. TOPO_DOM 35 512 Extracellular. {ECO:0000255}.; TOPO_DOM 534 600 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q3UIK4 MET14_MOUSE N6-adenosine-methyltransferase non-catalytic subunit (Methyltransferase-like protein 14) 456 52,122 Alternative sequence (1); Binding site (5); Chain (1); Compositional bias (1); Erroneous initiation (1); Modified residue (1); Region (7); Sequence conflict (1) FUNCTION: The METTL3-METTL14 heterodimer forms a N6-methyltransferase complex that methylates adenosine residues at the N(6) position of some mRNAs and regulates the circadian clock, differentiation of embryonic stem cells and cortical neurogenesis (PubMed:24394384, PubMed:28965759). In the heterodimer formed with METTL3, METTL14 constitutes the RNA-binding scaffold that recognizes the substrate rather than the catalytic core (By similarity). N6-methyladenosine (m6A), which takes place at the 5'-[AG]GAC-3' consensus sites of some mRNAs, plays a role in mRNA stability and processing (By similarity). M6A acts as a key regulator of mRNA stability by promoting mRNA destabilization and degradation (PubMed:24394384). In embryonic stem cells (ESCs), m6A methylation of mRNAs encoding key naive pluripotency-promoting transcripts results in transcript destabilization (PubMed:24394384). M6A regulates spermatogonial differentiation and meiosis and is essential for male fertility and spermatogenesis (PubMed:28914256). M6A also regulates cortical neurogenesis: m6A methylation of transcripts related to transcription factors, neural stem cells, the cell cycle and neuronal differentiation during brain development promotes their destabilization and decay, promoting differentiation of radial glial cells (PubMed:28965759). {ECO:0000250|UniProtKB:Q9HCE5, ECO:0000269|PubMed:24394384, ECO:0000269|PubMed:28914256, ECO:0000269|PubMed:28965759}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24394384, ECO:0000269|PubMed:28914256, ECO:0000269|PubMed:29547716}. SUBUNIT: Heterodimer; heterodimerizes with METTL3 to form an antiparallel heterodimer that constitutes an active methyltransferase (By similarity). Component of the WMM complex, a N6-methyltransferase complex composed of a catalytic subcomplex, named MAC, and of an associated subcomplex, named MACOM (PubMed:29535189, PubMed:29547716). The MAC subcomplex is composed of METTL3 and METTL14 (PubMed:29535189, PubMed:29547716). The MACOM subcomplex is composed of WTAP, ZC3H13, CBLL1/HAKAI, VIRMA, and, in some cases of RBM15 (RBM15 or RBM15B) (PubMed:29535189, PubMed:29547716). {ECO:0000250|UniProtKB:Q9HCE5, ECO:0000269|PubMed:29535189, ECO:0000269|PubMed:29547716}. TISSUE SPECIFICITY: Expressed in testis (PubMed:28914256). Highly expressed in radial glial cells during embryonic cortical neurogenesis (PubMed:28965759). {ECO:0000269|PubMed:28914256, ECO:0000269|PubMed:28965759}. +Q8C0T7 MFSD9_MOUSE Major facilitator superfamily domain-containing protein 9 466 49,663 Chain (1); Transmembrane (9) TRANSMEM 35 55 Helical. {ECO:0000255}.; TRANSMEM 64 84 Helical. {ECO:0000255}.; TRANSMEM 105 125 Helical. {ECO:0000255}.; TRANSMEM 157 177 Helical. {ECO:0000255}.; TRANSMEM 187 207 Helical. {ECO:0000255}.; TRANSMEM 272 292 Helical. {ECO:0000255}.; TRANSMEM 315 335 Helical. {ECO:0000255}.; TRANSMEM 351 371 Helical. {ECO:0000255}.; TRANSMEM 428 448 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +P26187 MGMT_MOUSE Methylated-DNA--protein-cysteine methyltransferase (EC 2.1.1.63) (6-O-methylguanine-DNA methyltransferase) (MGMT) (O-6-methylguanine-DNA-alkyltransferase) 211 22,435 Active site (1); Binding site (6); Chain (1); Metal binding (4); Modified residue (2) FUNCTION: Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +P27106 MIS_MOUSE Muellerian-inhibiting factor (Anti-Muellerian hormone) (AMH) (Muellerian-inhibiting substance) (MIS) 555 59,778 Chain (1); Disulfide bond (4); Glycosylation (3); Propeptide (1); Signal peptide (1) FUNCTION: This glycoprotein, produced by the Sertoli cells of the testis, causes regression of the Muellerian duct. It is also able to inhibit the growth of tumors derived from tissues of Muellerian duct origin. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Homodimer; disulfide-linked. TISSUE SPECIFICITY: Sertoli cells of fetal testes, and testes just after birth, but absent in adult testes. In female, AMH is expressed after birth in the granulosa cells of the follicle. AMH expression is dependent on the degree of follicular maturation and not on the age of the ovary. +Q8VDV8 MITD1_MOUSE MIT domain-containing protein 1 249 28,847 Chain (1); Domain (1); Frameshift (1); Helix (3); Region (1); Sequence conflict (1) FUNCTION: Required for efficient abscission at the end of cytokinesis, together with components of the ESCRT-III complex. {ECO:0000250}. SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Midbody {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=During cytokinesis, recruited to the midbody via interaction with CHMP1A. Interacts with membranes enriched in phosphoinositides (By similarity). {ECO:0000250}. SUBUNIT: Homodimer. Interacts (via MIT domain) with CHMP1A, CHMP1B, CHMP2A and IST1 (By similarity). {ECO:0000250}. DOMAIN: The C-terminal domain interacts with lipid membranes containing acidic phosphoinositides and is required for location at the midbody. {ECO:0000250}.; DOMAIN: The MIT domain interacts with the MIT-interacting motifs of several components of the ESCRT-III complex. {ECO:0000250}. +Q8JZN7 MIRO2_MOUSE Mitochondrial Rho GTPase 2 (MIRO-2) (EC 3.6.5.-) (Ras homolog gene family member T2) 620 69,071 Calcium binding (2); Chain (1); Domain (4); Nucleotide binding (6); Topological domain (2); Transmembrane (1) TRANSMEM 595 617 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 1 594 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 618 620 Cytoplasmic. {ECO:0000255}. FUNCTION: Mitochondrial GTPase involved in mitochondrial trafficking. Probably involved in control of anterograde transport of mitochondria and their subcellular distribution (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Note=Colocalizes with MGARP and RHOT2 at the mitochondria. {ECO:0000250}. SUBUNIT: Interacts with the kinesin-binding proteins TRAK1/OIP106 and TRAK2/GRIF1, forming a link between mitochondria and the trafficking apparatus of the microtubules (By similarity). Interacts with ARMCX3 (PubMed:22569362). Found in a complex with KIF5B, OGT, RHOT1 and TRAK1 (By similarity). {ECO:0000250|UniProtKB:Q8IXI1, ECO:0000269|PubMed:22569362}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:15218247}. +Q9CY25 MIS12_MOUSE Protein MIS12 homolog 206 24,131 Chain (1); Coiled coil (1); Sequence conflict (1) FUNCTION: Part of the MIS12 complex which is required for normal chromosome alignment and segregation and for kinetochore formation during mitosis. Essential for proper kinetochore microtubule attachments. {ECO:0000250|UniProtKB:Q9H081}. SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q9H081}. Note=Associated with the kinetochore. {ECO:0000250|UniProtKB:Q9H081}. SUBUNIT: Component of the MIS12 complex composed of MIS12, DSN1, NSL1 and PMF1. Also interacts with KNL1, CBX3, CBX5, NDC80 and ZWINT. {ECO:0000250|UniProtKB:Q9H081}. +Q9WUI0 MIXL1_MOUSE Homeobox protein MIXL1 (Homeodomain protein MIX) (mMix) (MIX1 homeobox-like protein 1) (Mix.1 homeobox-like protein) 231 24,844 Chain (1); DNA binding (1) FUNCTION: Transcription factor that play a central role in proper axial mesendoderm morphogenesis and endoderm formation. Required for efficient differentiation of cells from the primitive streak stage to blood, by acting early in the recruitment and/or expansion of mesodermal progenitors to the hemangioblastic and hematopoietic lineages. Also involved in the morphogenesis of the heart and the gut during embryogenesis. Acts as a negative regulator of brachyury expression. {ECO:0000269|PubMed:12117810, ECO:0000269|PubMed:15673572, ECO:0000269|PubMed:16403910, ECO:0000269|PubMed:17060613, ECO:0000269|PubMed:17151016, ECO:0000269|PubMed:17446562}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:12619131}. TISSUE SPECIFICITY: Expressed in the primitive streak of the gastrulating embryo, and marks cells destined to form mesoderm and endoderm. Present in differentiating embryonic stem cells (at protein level). {ECO:0000269|PubMed:12619131, ECO:0000269|PubMed:16433620}. +Q9D7G9 MISS_MOUSE MAPK-interacting and spindle-stabilizing protein (Mitogen-activated protein kinase 1-interacting protein 1) 263 27,761 Chain (1); Compositional bias (1) FUNCTION: Involved in the maintenance of the spindle integrity during the cytostatic factor (CSF) arrest of oocytes. {ECO:0000269|PubMed:12011110}. PTM: Phosphorylated in vitro by MAPK1. {ECO:0000269|PubMed:12011110}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12011110}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:12011110}. Note=Colocalizes with the spindle at discrete sites during the second meiotic division. SUBUNIT: Interacts with MAPK1. {ECO:0000269|PubMed:12011110}. +O08911 MK12_MOUSE Mitogen-activated protein kinase 12 (MAP kinase 12) (MAPK 12) (EC 2.7.11.24) (Extracellular signal-regulated kinase 6) (ERK-6) (Mitogen-activated protein kinase p38 gamma) (MAP kinase p38 gamma) (Stress-activated protein kinase 3) 367 42,043 Active site (1); Binding site (1); Chain (1); Domain (1); Modified residue (2); Motif (1); Nucleotide binding (1) FUNCTION: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK12 is one of the four p38 MAPKs which play an important role in the cascades of cellular responses evoked by extracellular stimuli such as proinflammatory cytokines or physical stress leading to direct activation of transcription factors such as ELK1 and ATF2. Accordingly, p38 MAPKs phosphorylate a broad range of proteins and it has been estimated that they may have approximately 200 to 300 substrates each. Some of the targets are downstream kinases such as MAPKAPK2, which are activated through phosphorylation and further phosphorylate additional targets. Plays a role in myoblast differentiation and also in the down-regulation of cyclin D1 in response to hypoxia in adrenal cells suggesting MAPK12 may inhibit cell proliferation while promoting differentiation. Phosphorylates DLG1. Following osmotic shock, MAPK12 in the cell nucleus increases its association with nuclear DLG1, thereby causing dissociation of DLG1-SFPQ complexes. This function is independent of its catalytic activity and could affect mRNA processing and/or gene transcription to aid cell adaptation to osmolarity changes in the environment. Regulates UV-induced checkpoint signaling and repair of UV-induced DNA damage and G2 arrest after gamma-radiation exposure. MAPK12 is involved in the regulation of SLC2A1 expression and basal glucose uptake in L6 myotubes; and negatively regulates SLC2A4 expression and contraction-mediated glucose uptake in adult skeletal muscle. C-Jun (JUN) phosphorylation is stimulated by MAPK14 and inhibited by MAPK12, leading to a distinct AP-1 regulation. MAPK12 is required for the normal kinetochore localization of PLK1, prevents chromosomal instability and supports mitotic cell viability. MAPK12-signaling is also positively regulating the expansion of transient amplifying myogenic precursor cells during muscle growth and regeneration. {ECO:0000269|PubMed:20026657, ECO:0000269|PubMed:21170151, ECO:0000269|PubMed:21558321}. PTM: Dually phosphorylated on Thr-183 and Tyr-185 by MAP2K3/MKK3 and MAP2K6/MKK6, which activates the enzyme. {ECO:0000269|PubMed:20004242}.; PTM: Ubiquitinated. Ubiquitination leads to degradation by the proteasome pathway (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Mitochondrion {ECO:0000250}. Note=Mitochondrial when associated with SH3BP5. In skeletal muscle colocalizes with SNTA1 at the neuromuscular junction and throughout the sarcolemma. {ECO:0000250}. SUBUNIT: Monomer. Interacts with the PDZ domain of the syntrophin SNTA1 (By similarity). Interacts with SH3BP5, LIN7C, SCRIB and SYNJ2BP (By similarity). {ECO:0000250}. DOMAIN: The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases. TISSUE SPECIFICITY: Highly expressed in skeletal muscle. Also expressed in the heart, particularly in cardiac myocytes, lung, thymus and testes. {ECO:0000269|PubMed:11991731}. +Q63844 MK03_MOUSE Mitogen-activated protein kinase 3 (MAP kinase 3) (MAPK 3) (EC 2.7.11.24) (ERT2) (Extracellular signal-regulated kinase 1) (ERK-1) (Insulin-stimulated MAP2 kinase) (MAP kinase isoform p44) (p44-MAPK) (MNK1) (Microtubule-associated protein 2 kinase) (p44-ERK1) 380 43,066 Active site (1); Binding site (1); Chain (1); Domain (1); Initiator methionine (1); Modified residue (5); Motif (1); Nucleotide binding (1); Sequence conflict (2) FUNCTION: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK1/ERK2 and MAPK3/ERK1 are the 2 MAPKs which play an important role in the MAPK/ERK cascade. They participate also in a signaling cascade initiated by activated KIT and KITLG/SCF. Depending on the cellular context, the MAPK/ERK cascade mediates diverse biological functions such as cell growth, adhesion, survival and differentiation through the regulation of transcription, translation, cytoskeletal rearrangements. The MAPK/ERK cascade plays also a role in initiation and regulation of meiosis, mitosis, and postmitotic functions in differentiated cells by phosphorylating a number of transcription factors. About 160 substrates have already been discovered for ERKs. Many of these substrates are localized in the nucleus, and seem to participate in the regulation of transcription upon stimulation. However, other substrates are found in the cytosol as well as in other cellular organelles, and those are responsible for processes such as translation, mitosis and apoptosis. Moreover, the MAPK/ERK cascade is also involved in the regulation of the endosomal dynamics, including lysosome processing and endosome cycling through the perinuclear recycling compartment (PNRC); as well as in the fragmentation of the Golgi apparatus during mitosis. The substrates include transcription factors (such as ATF2, BCL6, ELK1, ERF, FOS, HSF4 or SPZ1), cytoskeletal elements (such as CANX, CTTN, GJA1, MAP2, MAPT, PXN, SORBS3 or STMN1), regulators of apoptosis (such as BAD, BTG2, CASP9, DAPK1, IER3, MCL1 or PPARG), regulators of translation (such as EIF4EBP1) and a variety of other signaling-related molecules (like ARHGEF2, FRS2 or GRB10). Protein kinases (such as RAF1, RPS6KA1/RSK1, RPS6KA3/RSK2, RPS6KA2/RSK3, RPS6KA6/RSK4, SYK, MKNK1/MNK1, MKNK2/MNK2, RPS6KA5/MSK1, RPS6KA4/MSK2, MAPKAPK3 or MAPKAPK5) and phosphatases (such as DUSP1, DUSP4, DUSP6 or DUSP16) are other substrates which enable the propagation the MAPK/ERK signal to additional cytosolic and nuclear targets, thereby extending the specificity of the cascade. {ECO:0000269|PubMed:11702783, ECO:0000269|PubMed:12134156}. PTM: Dually phosphorylated on Thr-203 and Tyr-205, which activates the enzyme. Ligand-activated ALK induces tyrosine phosphorylation (By similarity). Dephosphorylated by PTPRJ at Tyr-205 (By similarity). Autophosphorylated on threonine and tyrosine residues in vitro. Phosphorylated upon FLT3 and KIT signaling (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Membrane, caveola {ECO:0000250|UniProtKB:P21708}. Note=Autophosphorylation at Thr-207 promotes nuclear localization (By similarity). PEA15-binding redirects the biological outcome of MAPK3 kinase-signaling by sequestering MAPK3 into the cytoplasm. {ECO:0000250}. SUBUNIT: Binds both upstream activators and downstream substrates in multimolecular complexes. Found in a complex with at least BRAF, HRAS, MAP2K1/MEK1, MAPK3 and RGS14. Interacts with TPR. Interacts with ADAM15, ARRB2, CANX, DAPK1 (via death domain), HSF4, IER3, MAP2K1/MEK1, NISCH, and SGK1 (By similarity). Interacts with MORG1 (PubMed:15118098). Interacts with PEA15 (PubMed:11702783). Interacts with isoform 1 of MKNK2 and this binding prevents from dephosphorylation and inactivation (PubMed:16162500). Interacts with CDKN2AIP. Interacts with HSF1 (via D domain and preferentially with hyperphosphorylated form); this interaction occurs upon heat shock. Interacts with CAVIN4 (By similarity). {ECO:0000250|UniProtKB:P21708, ECO:0000250|UniProtKB:P27361, ECO:0000269|PubMed:11702783, ECO:0000269|PubMed:15118098, ECO:0000269|PubMed:16162500}. DOMAIN: The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases. +Q61532 MK06_MOUSE Mitogen-activated protein kinase 6 (MAP kinase 6) (MAPK 6) (EC 2.7.11.24) (Extracellular signal-regulated kinase 3) (ERK-3) 720 82,199 Active site (1); Binding site (1); Chain (1); Cross-link (1); Domain (1); Modified residue (5); Motif (2); Mutagenesis (4); Nucleotide binding (1); Sequence conflict (5) FUNCTION: Atypical MAPK protein. Phosphorylates microtubule-associated protein 2 (MAP2) and MAPKAPK5. The precise role of the complex formed with MAPKAPK5 is still unclear, but the complex follows a complex set of phosphorylation events: upon interaction with atypical MAPKAPK5, ERK3/MAPK6 is phosphorylated at Ser-189 and then mediates phosphorylation and activation of MAPKAPK5, which in turn phosphorylates ERK3/MAPK6. May promote entry in the cell cycle. {ECO:0000269|PubMed:15538386, ECO:0000269|PubMed:15577943}. PTM: Phosphorylated at Ser-189 by PAK1, PAK2 and PAK3 resulting in catalytic activation. Phosphorylated by MAPKAPK5 at other sites. {ECO:0000269|PubMed:18720373}.; PTM: Ubiquitination at Met-1 leads to degradation by the proteasome pathway. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Translocates to the cytoplasm following interaction with MAPKAPK5. SUBUNIT: Heterodimer with ERK4/MAPK4. Interacts with (via FRIEDE motif) MAPKAPK5. Interacts with UBE3A; this interaction may be indirect and mediated by HERC2, possibly via HERC2 interaction with NEURL4 (By similarity). {ECO:0000250}. DOMAIN: In contrast to classical MAPKs, the TXY motif within the activation loop is replaced by the SEG motif, whose phosphorylation activates the MAP kinases. {ECO:0000269|PubMed:19473979}. +Q80Y86 MK15_MOUSE Mitogen-activated protein kinase 15 (MAP kinase 15) (MAPK 15) (EC 2.7.11.24) (Extracellular signal-regulated kinase 7) (ERK-7) (Extracellular signal-regulated kinase 8) (ERK-8) 549 60,679 Active site (1); Binding site (1); Chain (1); Domain (1); Modified residue (3); Motif (1); Nucleotide binding (1); Region (3); Repeat (4) FUNCTION: Atypical MAPK protein that regulates several process such as autophagy, ciliogenesis, protein trafficking/secretion and genome integrity, in a kinase activity-dependent manner (By similarity) (PubMed:25823377). Controls both, basal and starvation-induced autophagy throught its interaction with GABARAP, MAP1LC3B and GABARAPL1 leading to autophagosome formation, SQSTM1 degradation and reduced MAP1LC3B inhibitory phosphorylation. Regulates primary cilium formation and the localization of ciliary proteins involved in cilium structure, transport, and signaling. Prevents the relocation of the sugar-adding enzymes from the Golgi to the endoplasmic reticulum, thereby restricting the production of sugar-coated proteins. Upon amino-acid starvation, mediates transitional endoplasmic reticulum site disassembly and inhibition of secretion. Binds to chromatin leading to MAPK15 activation and interaction with PCNA, that which protects genomic integrity by inhibiting MDM2-mediated degradation of PCNA. Regulates DA transporter (DAT) activity and protein expression via activation of RhoA. In response to H(2)O(2) treatment phosphorylates ELAVL1, thus preventing it from binding to the PDCD4 3'UTR and rendering the PDCD4 mRNA accessible to miR-21 and leading to its degradation and loss of protein expression (By similarity). Also functions in a kinase activity-independent manner as a negative regulator of growth (By similarity). Phosphorylates in vitro FOS and MBP (By similarity). During oocyte maturation, plays a key role in the microtubule organization and meiotic cell cycle progression in oocytes, fertilized eggs, and early embryos (PubMed:23351492). Interacts with ESRRA promoting its re-localization from the nucleus to the cytoplasm and then prevents its transcriptional activity (By similarity). {ECO:0000250|UniProtKB:Q8TD08, ECO:0000250|UniProtKB:Q9Z2A6, ECO:0000269|PubMed:23351492, ECO:0000269|PubMed:25823377}. PTM: Autophosphorylated on Thr-176 and Tyr-178; activates the enzyme. {ECO:0000250|UniProtKB:Q8TD08}.; PTM: Ubiquitinated. Ubiquitination may allow its tight kinase activity regulation and rapid turnover. May be ubiquitinated by a SCF E3 ligase (By similarity). {ECO:0000250|UniProtKB:Q9Z2A6}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q8TD08}. Cell junction, tight junction {ECO:0000250|UniProtKB:Q8TD08}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q8TD08}. Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:Q8TD08}. Golgi apparatus {ECO:0000250|UniProtKB:Q8TD08}. Nucleus {ECO:0000250|UniProtKB:Q8TD08}. Cytoplasm {ECO:0000250|UniProtKB:Q8TD08}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:23351492}. Note=Co-localizes to the cytoplasm only in presence of ESRRA. Translocates to the nucleus upon activation (By similarity). At prometaphase I, metaphase I (MI), anaphase I, telophase I, and metaphase II (MII) stages, is stably detected at the spindle (PubMed:23351492). {ECO:0000250|UniProtKB:Q8TD08, ECO:0000269|PubMed:23351492}. SUBUNIT: Interacts with TGFB1I1 (PubMed:16624805). Interacts with CSK/c-Src, ABL1 and RET. Interacts with GABARAP, MAP1LC3B and GABARAPL1; controls, in a kinase-dependent fashion, both basal and starvation-induced autophagy. Interacts with ESRRA; promotes re-localization of ESRRA to the cytoplasm through a XPO1-dependent mechanism then inhibits ESRRA transcriptional activity. Interacts with PCNA; the interaction is chromatin binding- and kinase activity-dependent and prevents MDM2-mediated PCNA destruction by inhibiting the association of PCNA with MDM2 (By similarity). Interacts with DVL2 (PubMed:25823377). Interacts with CLIC3; MAPK15 does not phosphorylates CLIC3 (By similarity). {ECO:0000250|UniProtKB:Q8TD08, ECO:0000250|UniProtKB:Q9Z2A6, ECO:0000269|PubMed:16624805, ECO:0000269|PubMed:25823377}. DOMAIN: The N-terminal region (1-20) is the minimal region necessary for ubiquitination and further proteasomal degradation. {ECO:0000250}.; DOMAIN: The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases. TISSUE SPECIFICITY: Expressed at all stages of oocyte meiotic maturation. {ECO:0000269|PubMed:23351492}. +Q9ERV1 MKRN2_MOUSE Probable E3 ubiquitin-protein ligase makorin-2 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase makorin-2) 416 46,597 Chain (1); Modified residue (1); Region (1); Sequence conflict (1); Zinc finger (5) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins. {ECO:0000250}. +Q5SW45 MKS1_MOUSE Meckel syndrome type 1 protein homolog 561 64,416 Chain (1); Domain (1); Sequence conflict (1) FUNCTION: Component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. Involved in centrosome migration to the apical cell surface during early ciliogenesis. Required for ciliary structure and function, including a role in regulating length and appropriate number through modulating centrosome duplication. Required for cell branching morphology. {ECO:0000269|PubMed:17185389, ECO:0000269|PubMed:19515853, ECO:0000269|PubMed:21725307, ECO:0000269|PubMed:22179047}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:21725307}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Note=Localizes at the transition zone, a region between the basal body and the ciliary axoneme. SUBUNIT: Part of the tectonic-like complex (also named B9 complex) (PubMed:22179047, PubMed:21725307). Interacts with TMEM107 (By similarity). Interacts with TCTN3, AHI1, TCTN1, TCTN2, CC2D2A (PubMed:21565611). Interacts with FLNA. Interacts with TMEM67 (By similarity). Interacts with B9D1 and B9D2 (PubMed:21763481, PubMed:21565611). {ECO:0000250|UniProtKB:Q9NXB0, ECO:0000269|PubMed:21565611, ECO:0000269|PubMed:21725307, ECO:0000269|PubMed:21763481, ECO:0000269|PubMed:22179047}. TISSUE SPECIFICITY: Widely expressed in embryo at E15.5, with a relatively strong expression in brain, liver, kidney and digits of the upper limbs. Highly expressed in bronchiolar epithelium. {ECO:0000269|PubMed:16415886}. +Q8BR76 MKS3_MOUSE Meckelin (Meckel syndrome type 3 protein homolog) (Transmembrane protein 67) 992 111,810 Alternative sequence (2); Chain (1); Erroneous initiation (2); Glycosylation (1); Signal peptide (1); Transmembrane (6) TRANSMEM 523 543 Helical. {ECO:0000255}.; TRANSMEM 567 587 Helical. {ECO:0000255}.; TRANSMEM 606 626 Helical. {ECO:0000255}.; TRANSMEM 686 706 Helical. {ECO:0000255}.; TRANSMEM 731 751 Helical. {ECO:0000255}.; TRANSMEM 936 956 Helical. {ECO:0000255}. FUNCTION: Part of the tectonic-like complex which is required for tissue-specific ciliogenesis and may regulate ciliary membrane composition. Involved in centrosome migration to the apical cell surface during early ciliogenesis. Required for ciliary structure and function, including a role in regulating length and appropriate number through modulating centrosome duplication. Required for cell branching morphology. Essential for endoplasmic reticulum-associated degradation (ERAD) of surfactant protein C (sftpc). {ECO:0000269|PubMed:17185389, ECO:0000269|PubMed:19515853, ECO:0000269|PubMed:21725307}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Endoplasmic reticulum membrane; Multi-pass membrane protein. Cytoplasm, cytoskeleton, cilium basal body. Note=Localizes at the transition zone, a region between the basal body and the ciliary axoneme. SUBUNIT: Interacts with DNAJB9, DNAJC10 and mutated SFTPC (By similarity). Interacts with SYNE2 during the early establishment of cell polarity (By similarity). Part of the tectonic-like complex (also named B9 complex) (PubMed:21725307). Interacts (via C-terminus) with FLNA (By similarity). {ECO:0000250|UniProtKB:Q5HYA8, ECO:0000269|PubMed:21725307}. DISEASE: Note=A spontaneous deletion of TMEM67 cause the bilateral polycystic kidneys (bpck) phenotype, a disease mimicking human Meckel-Gruber syndrome 3. Homozygous bpck/bpck mice typically manifest bilateral nephropathy with swollen abdomens resulting from grossly enlarged polycystic kidneys and die by 3 week of age. Some mice also develop hydrocephalus, usually detectable within a few days of birth (PubMed:19211713). Additionally, bpck/bpck mice exhibit retinal degeneration and tissue disorganization in the eye, and cochlear defects (PubMed:23393159). {ECO:0000269|PubMed:19211713, ECO:0000269|PubMed:23393159}. +Q8BIA3 MKX_MOUSE Homeobox protein Mohawk 353 39,401 Chain (1); DNA binding (1) FUNCTION: May act as a morphogenetic regulator of cell adhesion. Participates in the early events that lead to differentiation. {ECO:0000269|PubMed:16408284}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q3THE2 ML12B_MOUSE Myosin regulatory light chain 12B (Myosin regulatory light chain 2-B, smooth muscle isoform) (Myosin regulatory light chain 20 kDa) (MLC20) (Myosin regulatory light chain MRLC2) 172 19,779 Calcium binding (1); Chain (1); Domain (3); Frameshift (1); Modified residue (2); Sequence conflict (3) FUNCTION: Myosin regulatory subunit that plays an important role in regulation of both smooth muscle and nonmuscle cell contractile activity via its phosphorylation. Phosphorylation triggers actin polymerization in vascular smooth muscle. Implicated in cytokinesis, receptor capping, and cell locomotion. {ECO:0000250|UniProtKB:O14950}. PTM: Phosphorylation increases the actin-activated myosin ATPase activity and thereby regulates the contractile activity. It is required to generate the driving force in the migration of the cells but not necessary for localization of myosin-2 at the leading edge. Phosphorylation is reduced following epigallocatechin-3-O-gallate treatment. {ECO:0000250|UniProtKB:O14950}. SUBUNIT: Myosin is a hexamer of 2 heavy chains and 4 light chains: interacts with myosin heavy chain MYO19. {ECO:0000269|PubMed:24825904}. +Q8K099 LRIT1_MOUSE Leucine-rich repeat, immunoglobulin-like domain and transmembrane domain-containing protein 1 (Leucine-rich repeat-containing protein 21) (Photoreceptor-associated LRR superfamily protein) (Retina-specific protein PAL) 624 68,464 Chain (1); Disulfide bond (1); Domain (4); Erroneous initiation (1); Glycosylation (3); Repeat (6); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 528 548 Helical. {ECO:0000255}. TOPO_DOM 22 527 Lumenal. {ECO:0000255}.; TOPO_DOM 549 624 Cytoplasmic. {ECO:0000255}. FUNCTION: Possible role in phototransduction. {ECO:0000250|UniProtKB:Q9JMH2}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9JMH2}. +Q6PFC5 LRIT2_MOUSE Leucine-rich repeat, immunoglobulin-like domain and transmembrane domain-containing protein 2 (Leucine-rich repeat-containing protein 22) 549 61,360 Chain (1); Disulfide bond (1); Domain (4); Glycosylation (3); Repeat (4); Signal peptide (1); Transmembrane (1) TRANSMEM 463 483 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. +Q80TG9 LRFN2_MOUSE Leucine-rich repeat and fibronectin type-III domain-containing protein 2 788 84,963 Chain (1); Disulfide bond (1); Domain (4); Erroneous initiation (1); Glycosylation (4); Motif (1); Mutagenesis (1); Repeat (7); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 535 555 Helical. {ECO:0000255}. TOPO_DOM 21 534 Extracellular. {ECO:0000255}.; TOPO_DOM 556 788 Cytoplasmic. {ECO:0000255}. FUNCTION: Promotes neurite outgrowth in hippocampal neurons. Enhances the cell surface expression of 2 NMDA receptor subunits GRIN1 and GRIN2A (By similarity). May play a role in redistributing DLG4 to the cell periphery. {ECO:0000250, ECO:0000269|PubMed:16828986}. PTM: Glycosylated. {ECO:0000269|PubMed:16828986}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:16828986}; Single-pass type I membrane protein {ECO:0000269|PubMed:16828986}. Cell junction, synapse {ECO:0000269|PubMed:16828986}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000250}. SUBUNIT: Forms heteromeric complexes with LRFN1, LRFN3, LRFN4 and LRFN5. Can form homomeric complexes, but not across cell junctions (By similarity). Interacts with DLG4. Directly interacts with DLG1, DLG2 and DLG3 (By similarity). Directly interacts with 2 NMDA receptor subunits GRIN1 and GRIN2A (By similarity). {ECO:0000250}. DOMAIN: The PDZ-binding motif is required for cell surface expression, neurite outgrowth promotion and interaction with DLG1, DLG3 and DLG4. {ECO:0000250}. TISSUE SPECIFICITY: Predominantly expressed in the brain, with a weak, but broad expression in the cerebral cortex and diencephalic nuclei. Strongly expressed in both the pyramidal layer and the dentate gyrus of the hippocampus. Also detected in other parts of the central nervous system, including the olfactory bulb, pons, cerebellum, and medulla oblongata, as well as in the peripheral nervous system, such as the ganglia of cranial nerves and the dorsal root ganglion during gestation. {ECO:0000269|PubMed:16828986}. +A2AR95 LRAD3_MOUSE Low-density lipoprotein receptor class A domain-containing protein 3 345 37,467 Alternative sequence (2); Chain (1); Compositional bias (1); Disulfide bond (9); Domain (3); Erroneous initiation (1); Glycosylation (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 174 194 Helical. {ECO:0000255}. TOPO_DOM 18 173 Extracellular. {ECO:0000255}.; TOPO_DOM 195 345 Cytoplasmic. {ECO:0000255}. FUNCTION: May influence APP processing, resulting in a decrease in sAPP-alpha production and increased amyloidogenic P3 peptide production. {ECO:0000269|PubMed:21795536}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21795536}; Single-pass type I membrane protein {ECO:0000269|PubMed:21795536}. SUBUNIT: Interacts with APP precursor C-terminus. {ECO:0000269|PubMed:21795536}. TISSUE SPECIFICITY: Expressed in the cerebral cortex and hippocampus. {ECO:0000269|PubMed:21795536}. +Q9D9B4 LRMDA_MOUSE Leucine-rich melanocyte differentiation-associated protein 229 25,989 Chain (1); Domain (1); Repeat (3) FUNCTION: Required for melanocyte differentiation. {ECO:0000250|UniProtKB:Q9H2I8}. +Q14DL3 LRIQ3_MOUSE Leucine-rich repeat and IQ domain-containing protein 3 (Leucine-rich repeat-containing protein 44) 633 75,364 Alternative sequence (4); Chain (1); Coiled coil (1); Domain (2); Frameshift (1); Repeat (3); Sequence conflict (1) +Q9D1G5 LRC57_MOUSE Leucine-rich repeat-containing protein 57 239 26,760 Chain (1); Initiator methionine (1); Lipidation (1); Repeat (8); Sequence conflict (2) SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q8N9N7}; Lipid-anchor {ECO:0000250|UniProtKB:Q8N9N7}. +Q8BLK3 LSAMP_MOUSE Limbic system-associated membrane protein (LSAMP) 341 38,086 Chain (1); Disulfide bond (3); Domain (3); Glycosylation (7); Modified residue (1); Propeptide (1); Signal peptide (1) FUNCTION: Mediates selective neuronal growth and axon targeting. Contributes to the guidance of developing axons and remodeling of mature circuits in the limbic system. Essential for normal growth of the hyppocampal mossy fiber projection (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. +Q5S006 LRRK2_MOUSE Leucine-rich repeat serine/threonine-protein kinase 2 (EC 2.7.11.1) 2527 284,732 Active site (1); Binding site (1); Chain (1); Coiled coil (1); Compositional bias (3); Domain (2); Modified residue (1); Mutagenesis (1); Nucleotide binding (4); Repeat (19); Sequence conflict (5) FUNCTION: Positively regulates autophagy through a calcium-dependent activation of the CaMKK/AMPK signaling pathway. The process involves activation of nicotinic acid adenine dinucleotide phosphate (NAADP) receptors, increase in lysosomal pH, and calcium release from lysosomes. Together with RAB29, plays a role in the retrograde trafficking pathway for recycling proteins, such as mannose 6 phosphate receptor (M6PR), between lysosomes and the Golgi apparatus in a retromer-dependent manner. Regulates neuronal process morphology in the intact central nervous system (CNS). Phosphorylates PRDX3. Has GTPase activity (By similarity). Plays an important role in recruiting SEC16A to endoplasmic reticulum exit sites (ERES) and in regulating ER to Golgi vesicle-mediated transport and ERES organization (PubMed:25201882). {ECO:0000250|UniProtKB:Q5S007, ECO:0000269|PubMed:25201882}. PTM: Autophosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Perikaryon {ECO:0000250}. Cell projection, axon {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Golgi apparatus {ECO:0000269|PubMed:17120249}. Endoplasmic reticulum {ECO:0000269|PubMed:17120249, ECO:0000269|PubMed:25201882}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q5S007, ECO:0000269|PubMed:17120249}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q5S007}; Cytoplasmic side {ECO:0000250|UniProtKB:Q5S007}. Endosome {ECO:0000269|PubMed:17120249}. Lysosome {ECO:0000269|PubMed:17120249}. Mitochondrion outer membrane {ECO:0000269|PubMed:17120249}. Mitochondrion inner membrane {ECO:0000269|PubMed:17120249}. Mitochondrion matrix {ECO:0000269|PubMed:17120249}. Note=Localized in the cytoplasm and associated with cellular membrane structures. Colocalized with RAB29 along tubular structures emerging from Golgi apparatus. Localizes in intracytoplasmic punctate structures of neuronal perikarya and dendritic and axonal processes (By similarity). Predominantly associated with intracytoplasmic vesicular and membranous structures. Predominantly associated with the mitochondrial outer membrane of the mitochondria. Localizes to endoplasmic reticulum exit sites (ERES), also known as transitional endoplasmic reticulum (tER) (PubMed:25201882). {ECO:0000250|UniProtKB:Q5S007, ECO:0000269|PubMed:25201882}. SUBUNIT: Homodimer. Interacts with PRKN, PRDX3 and TPCN2 (By similarity). Interacts with VPS35 and RAB29 (PubMed:23395371). Interacts (via ROC domain) with SEC16A (PubMed:25201882). {ECO:0000250|UniProtKB:Q5S007, ECO:0000269|PubMed:23395371, ECO:0000269|PubMed:25201882}. DOMAIN: The seven-bladed WD repeat region is critical for synaptic vesicle trafficking and mediates interaction with multiple vesicle-associated presynaptic proteins. {ECO:0000250|UniProtKB:Q5S007}.; DOMAIN: The Roc domain mediates homodimerization and regulates kinase activity. {ECO:0000250|UniProtKB:Q5S007}. TISSUE SPECIFICITY: Expressed in the brain (at protein level). Detected throughout the adult brain. Expressed in deep cerebral cortex layers, superficial cingulate cortex layers, the piriform cortex, hippocampal formation, caudate putamen, substantia nigra, the basolateral and basomedial anterior amygdala nuclei, reticular thalamic nucleus and also in the cerebellar granular cell layer. Highly expressed in the striatum, cortex and olfactory tubercle. Little or no expression in the substantia nigra, where dopaminergic neurons preferentially degenerate in Parkinson disease. Expression is particularly high in brain dopaminoceptive areas. High and strikingly specific expression in striatum and parts of cortex and no signals in dopamine neurons. {ECO:0000269|PubMed:16487147, ECO:0000269|PubMed:16504409, ECO:0000269|PubMed:16532471, ECO:0000269|PubMed:17120249}. +Q8CDN9 LRRC9_MOUSE Leucine-rich repeat-containing protein 9 1456 167,302 Alternative sequence (2); Chain (1); Frameshift (2); Modified residue (1); Repeat (32); Sequence conflict (5) +Q8C0R9 LRRD1_MOUSE Leucine-rich repeat and death domain-containing protein 1 853 97,132 Chain (1); Domain (1); Repeat (26); Sequence conflict (3) +A2ARV4 LRP2_MOUSE Low-density lipoprotein receptor-related protein 2 (LRP-2) (Glycoprotein 330) (gp330) (Megalin) 4660 519,208 Chain (1); Disulfide bond (126); Domain (42); Glycosylation (43); Metal binding (12); Modified residue (6); Motif (7); Region (1); Repeat (36); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 4426 4446 Helical. {ECO:0000255}. TOPO_DOM 26 4425 Extracellular. {ECO:0000255}.; TOPO_DOM 4447 4660 Cytoplasmic. {ECO:0000255}. FUNCTION: Multiligand endocytic receptor. Acts together with CUBN to mediate endocytosis of high-density lipoproteins (PubMed:10766831). Mediates receptor-mediated uptake of polybasic drugs such as aprotinin, aminoglycosides and polymyxin B (By similarity). In the kidney, mediates the tubular uptake and clearance of leptin (PubMed:22841573). Also mediates transport of leptin across the blood-brain barrier through endocytosis at the choroid plexus epithelium (By similarity). Endocytosis of leptin in neuronal cells is required for hypothalamic leptin signaling and leptin-mediated regulation of feeding and body weight (PubMed:24825475). Mediates endocytosis and subsequent lysosomal degradation of CST3 in kidney proximal tubule cells (PubMed:17462596). Mediates renal uptake of 25-hydroxyvitamin D3 in complex with the vitamin D3 transporter GC/DBP (PubMed:10052453). Mediates renal uptake of metallothionein-bound heavy metals (By similarity). Together with CUBN, mediates renal reabsorption of myoglobin (By similarity). Mediates renal uptake and subsequent lysosomal degradation of APOM (By similarity). Plays a role in kidney selenium homeostasis by mediating renal endocytosis of selenoprotein SEPP1 (PubMed:18174160). Mediates renal uptake of the antiapoptotic protein BIRC5/survivin which may be important for functional integrity of the kidney (PubMed:23825075). Mediates renal uptake of matrix metalloproteinase MMP2 in complex with metalloproteinase inhibitor TIMP1 (PubMed:28659595). Mediates endocytosis of Sonic hedgehog protein N-product (ShhN), the active product of SHH (By similarity). Also mediates ShhN transcytosis (By similarity). In the embryonic neuroepithelium, mediates endocytic uptake and degradation of BMP4, is required for correct SHH localization in the ventral neural tube and plays a role in patterning of the ventral telencephalon (PubMed:15623804). Required at the onset of neurulation to sequester SHH on the apical surface of neuroepithelial cells of the rostral diencephalon ventral midline and to control PTCH1-dependent uptake and intracellular trafficking of SHH (PubMed:22340494). During neurulation, required in neuroepithelial cells for uptake of folate bound to the folate receptor FOLR1 which is necessary for neural tube closure (PubMed:24639464). In the adult brain, negatively regulates BMP signaling in the subependymal zone which enables neurogenesis to proceed (PubMed:20460439). In astrocytes, mediates endocytosis of ALB which is required for the synthesis of the neurotrophic factor oleic acid (By similarity). Involved in neurite branching (PubMed:20637285). During optic nerve development, required for SHH-mediated migration and proliferation of oligodendrocyte precursor cells (PubMed:22354480). Mediates endocytic uptake and clearance of SHH in the retinal margin which protects retinal progenitor cells from mitogenic stimuli and keeps them quiescent (PubMed:26439398). Plays a role in reproductive organ development by mediating uptake in reproductive tissues of androgen and estrogen bound to the sex hormone binding protein SHBG (PubMed:16143106). Mediates endocytosis of angiotensin-2 (By similarity). Also mediates endocytosis of angiotensin 1-7 (By similarity). Binds to the complex composed of beta-amyloid protein 40 and CLU/APOJ and mediates its endocytosis and lysosomal degradation (By similarity). Required for embryonic heart development (PubMed:26822476). Required for normal hearing, possibly through interaction with estrogen in the inner ear (PubMed:17846082). {ECO:0000250|UniProtKB:C0HL13, ECO:0000250|UniProtKB:P98158, ECO:0000250|UniProtKB:P98164, ECO:0000269|PubMed:10052453, ECO:0000269|PubMed:10766831, ECO:0000269|PubMed:15623804, ECO:0000269|PubMed:16143106, ECO:0000269|PubMed:16380466, ECO:0000269|PubMed:17462596, ECO:0000269|PubMed:17846082, ECO:0000269|PubMed:18174160, ECO:0000269|PubMed:20460439, ECO:0000269|PubMed:20637285, ECO:0000269|PubMed:22340494, ECO:0000269|PubMed:22354480, ECO:0000269|PubMed:22841573, ECO:0000269|PubMed:23825075, ECO:0000269|PubMed:24639464, ECO:0000269|PubMed:24825475, ECO:0000269|PubMed:26439398, ECO:0000269|PubMed:26822476, ECO:0000269|PubMed:28659595}. PTM: A fraction undergoes proteolytic cleavage of the extracellular domain at the cell membrane to generate a cytoplasmic tail fragment. This is internalized into the early endosome from where it trafficks in an LDLRAP1/ARH-dependent manner to the endocytic recycling compartment (ERC). In the ERC, it is further cleaved by gamma-secretase to release a fragment which translocates to the nucleus and mediates transcriptional repression. {ECO:0000250|UniProtKB:P98158}.; PTM: N-glycosylation is required for ligand binding. Contains core-fucosylated N-glycans in kidney proximal convoluted tubules (PCTs) and hybrid-type N-glycans in proximal straight tubules (PSTs). Interacts with ligands in a glycoform-dependent manner. Retinol-binding protein and the vitamin D carrier GC/DBP are endocytosed primarily by PCTs, albumin is endocytosed equally by PCTs and PSTs, and the aminoglycoside kanamycin is endocytosed primarily by PSTs. {ECO:0000269|PubMed:27773703}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:16143106, ECO:0000269|PubMed:20460439, ECO:0000269|PubMed:22340494, ECO:0000269|PubMed:22354480}; Single-pass type I membrane protein {ECO:0000255}. Endosome lumen {ECO:0000250|UniProtKB:P98158}. Membrane, coated pit {ECO:0000269|PubMed:22340494}. Cell projection, dendrite {ECO:0000269|PubMed:20637285}. Cell projection, axon {ECO:0000269|PubMed:20637285}. Note=Localizes to brush border membranes in the kidney. In the endolymphatic sac of the inner ear, located in the lumen of endosomes as a soluble form. {ECO:0000250|UniProtKB:P98158}. SUBUNIT: Binds plasminogen, extracellular matrix components, plasminogen activator-plasminogen activator inhibitor type I complex, apolipoprotein E-enriched beta-VLDL, lipoprotein lipase, lactoferrin, CLU/clusterin and calcium. Forms a multimeric complex together with LRPAP1 (By similarity). Interacts (via PxLPxI/L motif) with ANKRA2 (via ankyrin repeats) (By similarity). Interacts with LRP2BP. Interacts (via NPXY motif) with DAB2; the interaction is not affected by tyrosine phosphorylation of the NPXY motif (PubMed:11247302). Interacts with MB (By similarity). Interacts with BMP4 (PubMed:15623804). Interacts with the Sonic hedgehog protein N-product which is the active product of SHH (PubMed:11964399). Interacts with CST3 in a calcium-dependent manner (By similarity). Interacts with the vitamin-D binding protein GC/DBP (PubMed:10052453). Interacts with sex hormone-binding protein SHBG (By similarity). Interacts with angiotensin-2 (PubMed:15467006). Also interacts with angiotensin 1-7 (PubMed:16380466). Interacts with APOM (PubMed:16099815). Interacts with selenoprotein SEPP1 (PubMed:18174160). Interacts with LEP (By similarity). Interacts with ALB (By similarity). Interacts with the antiapoptotic protein BIRC5/survivin (By similarity). Interacts with matrix metalloproteinase MMP2 in complex with metalloproteinase inhibitor TIMP1 (By similarity). In neurons, forms a trimeric complex with APP and APPB1/FE65 (PubMed:20637285). Interacts with LDLRAP1/ARH; mediates trafficking of LRP2 to the endocytic recycling compartment (By similarity). Does not interact with beta-amyloid protein 40 alone but interacts with the complex composed of beta-amyloid protein 40 and CLU/APOJ (By similarity). {ECO:0000250|UniProtKB:C0HL13, ECO:0000250|UniProtKB:P98158, ECO:0000250|UniProtKB:P98164, ECO:0000269|PubMed:10052453, ECO:0000269|PubMed:11247302, ECO:0000269|PubMed:11964399, ECO:0000269|PubMed:15467006, ECO:0000269|PubMed:15623804, ECO:0000269|PubMed:16099815, ECO:0000269|PubMed:16380466, ECO:0000269|PubMed:18174160, ECO:0000269|PubMed:20637285}. DOMAIN: Two overlapping PxLPxI/L motifs mediate interaction with ankyrin repeats of ANKRA2. {ECO:0000250|UniProtKB:P98158}.; DOMAIN: The cytoplasmic domain is required for sorting to the apical cell membrane. {ECO:0000250|UniProtKB:P98158}. TISSUE SPECIFICITY: In the inner ear, strongly expressed in the marginal cells of the stria vascularis (at protein level) (PubMed:17846082). In the female reproductive tract, expressed on the luminal side of the uterine epithelium (at protein level) (PubMed:16143106). In the adult brain, expressed in ependymal cells of the lateral ventricles where expression is restricted to the ependyma that faces the stem cell niche (at protein level) (PubMed:20460439). Expressed in neurons throughout the brain including in the hippocampus, limbic cortices and cerebellum (at protein level) (PubMed:20637285). In the developing optic nerve, expressed exclusively in astrocytes at E14.5, E16.5 and E18.5 (at protein level) (PubMed:22354480). {ECO:0000269|PubMed:16143106, ECO:0000269|PubMed:17846082, ECO:0000269|PubMed:20460439, ECO:0000269|PubMed:20637285, ECO:0000269|PubMed:22354480}. +Q924X6 LRP8_MOUSE Low-density lipoprotein receptor-related protein 8 (LRP-8) (Apolipoprotein E receptor 2) 996 109,818 Alternative sequence (1); Chain (1); Disulfide bond (30); Domain (10); Glycosylation (4); Mutagenesis (3); Region (1); Repeat (5); Sequence conflict (9); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 859 881 Helical. {ECO:0000255}. TOPO_DOM 29 858 Extracellular. {ECO:0000255}.; TOPO_DOM 882 996 Cytoplasmic. {ECO:0000255}. FUNCTION: Cell surface receptor for Reelin (RELN) and apolipoprotein E (apoE)-containing ligands. LRP8 participates in transmitting the extracellular Reelin signal to intracellular signaling processes, by binding to DAB1 on its cytoplasmic tail. Reelin acts via both the VLDL receptor (VLDLR) and LRP8 to regulate DAB1 tyrosine phosphorylation and microtubule function in neurons. LRP8 has higher affinity for Reelin than VLDLR. LRP8 is thus a key component of the Reelin pathway which governs neuronal layering of the forebrain during embryonic brain development. Binds the endoplasmic reticulum resident receptor-associated protein (RAP). Binds dimers of beta 2-glycoprotein I and may be involved in the suppression of platelet aggregation in the vasculature. Highly expressed in the initial segment of the epididymis, where it affects the functional expression of clusterin and phospholipid hydroperoxide glutathione peroxidase (PHGPx), two proteins required for sperm maturation (PubMed:12695510). May also function as an endocytic receptor. Not required for endocytic uptake of SEPP1 in the kidney which is mediated by LRP2 (PubMed:18174160). Together with its ligand, apolipoprotein E (apoE), may indirectly play a role in the suppression of the innate immune response by controlling the survival of myeloid-derived suppressor cells (PubMed:29336888). {ECO:0000269|PubMed:12695510, ECO:0000269|PubMed:18174160, ECO:0000269|PubMed:29336888}. PTM: O-glycosylated. Some alternatively spliced isoforms lack the O-linked sugar domain. {ECO:0000269|PubMed:12871934}.; PTM: Undergoes sequential, furin and gamma-secretase dependent, proteolytic processing, resulting in the extracellular release of the entire ligand-binding domain as a soluble polypeptide and in the intracellular domain (ICD) release into the cytoplasm. The gamma-secretase-dependent proteolytical processing occurs after the bulk of the extracellular domain has been shed, in a furin-dependent manner, in alternatively spliced isoforms carrying the furin cleavage site. Hypoglycosylation (mainly hypo-O-glycosylation) leads to increased extracellular cleavage, which in turn results in accelerating release of the intracellular domain (ICD) by the gamma-secretase. The resulting receptor fragment is able to inhibit Reelin signaling and in particular the Reelin-induced DAB1 phosphorylation. {ECO:0000269|PubMed:12426372, ECO:0000269|PubMed:12871934}.; PTM: Tyrosine phosphorylated upon apoE binding. {ECO:0000250}.; PTM: Ubiquitinated by MYLIP leading to degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Secreted. Note=Isoforms that contain the exon coding for a furin-type cleavage site are proteolytically processed, leading to a secreted receptor fragment. SUBUNIT: Reelin associates with two or more receptor molecules. Interacts with DAB1 and JNK-interacting proteins. Interacts with SNX17. Interacts with PCSK9 (By similarity). {ECO:0000250}. DOMAIN: The cytoplasmic domain is involved in the binding of DAB1 and in the recruitment of JNK-interacting proteins. Isoforms, which lack part of the cytoplasmic domain, are unable to recruit members of the family of JNK interacting proteins (JIP) to the cytoplasmic tail. TISSUE SPECIFICITY: Expressed in neurons throughout the brain, with strong expression in pyramidal neurons of the hippocampus, granule cells of the dentate gyrus, cortical neurons and Purkinje cells of the cerebellum. Also expressed in the epithelium of the choroid plexus and of the blood vessels (apical expression), as well as in the epididymis. {ECO:0000269|PubMed:10827199}. +Q9CYI4 LUC7L_MOUSE Putative RNA-binding protein Luc7-like 1 371 43,934 Alternative sequence (1); Chain (1); Coiled coil (2); Compositional bias (1); Modified residue (2); Sequence conflict (3) FUNCTION: May bind to RNA via its Arg/Ser-rich domain. +O70582 LX12B_MOUSE Arachidonate 12-lipoxygenase, 12R-type (12R-LOX) (12R-lipoxygenase) (EC 1.13.11.-) (Epidermis-type lipoxygenase 12) (Epidermis-type lipoxygenase 2) (e-LOX 2) 701 80,578 Chain (1); Domain (2); Metal binding (5); Mutagenesis (6); Natural variant (3) Lipid metabolism; hydroperoxy eicosatetraenoic acid biosynthesis. Lipid metabolism; sphingolipid metabolism. FUNCTION: Non-heme iron-containing dioxygenase that catalyzes the stereo-specific peroxidation of free and esterified polyunsaturated fatty acids generating a spectrum of bioactive lipid mediators. Mainly converts arachidonic acid to (12R)-hydroperoxyeicosatetraenoic acid/(12R)-HPETE and minor stereoisomers. In the skin, acts upstream of ALOXE3 on the lineolate moiety of esterified omega-hydroxyacyl-sphingosine (EOS) ceramides to produce an epoxy-ketone derivative, a crucial step in the conjugation of omega-hydroxyceramide to membrane proteins. Therefore plays a crucial role in the synthesis of corneocytes lipid envelope and the establishment of the skin barrier to water loss. May also play a role in the regulation of the expression of airway mucins. {ECO:0000269|PubMed:16129665, ECO:0000269|PubMed:17403930, ECO:0000269|PubMed:17429434, ECO:0000269|PubMed:21558561}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00726}. TISSUE SPECIFICITY: Expressed in skin epidermis and other stratified epithelia including tongue and forestomach. Low levels of expression are found in trachea, brain and lung. Not expressed in intestine, liver, kidney, adipose tissue, muscle or hematopoietic cells. {ECO:0000269|PubMed:9518531}. +P55249 LX12E_MOUSE Arachidonate 12-lipoxygenase, epidermal-type (12-LOX) (EC 1.13.11.31) 662 75,456 Chain (1); Domain (2); Metal binding (4); Natural variant (3); Sequence conflict (1) Lipid metabolism; hydroperoxy eicosatetraenoic acid biosynthesis. FUNCTION: Non-heme iron-containing dioxygenase that probably catalyzes the stereo-specific peroxidation of free and esterified polyunsaturated fatty acids generating a spectrum of bioactive lipid mediators. May preferentially convert arachidonic acid to (12S)-hydroperoxyeicosatetraenoic acid/(12S)-HPETE. {ECO:0000269|PubMed:8798535, ECO:0000269|PubMed:9037187}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00726}. TISSUE SPECIFICITY: Expressed in epidermis. {ECO:0000269|PubMed:8798535}. +Q9D7V2 LYSM2_MOUSE LysM and putative peptidoglycan-binding domain-containing protein 2 215 23,694 Alternative sequence (1); Chain (1); Domain (1); Initiator methionine (1); Modified residue (5); Sequence conflict (7) +O09043 NAPSA_MOUSE Napsin-A (EC 3.4.23.-) (KDAP-1) (Kidney-derived aspartic protease-like protein) (KAP) 419 45,544 Active site (2); Chain (1); Disulfide bond (3); Domain (1); Glycosylation (4); Propeptide (1); Signal peptide (1) FUNCTION: May be involved in processing of pneumocyte surfactant precursors. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Expressed at the highest levels in the kidney, at a moderate level in the lung, and at low levels in the spleen and adipose tissue. {ECO:0000269|PubMed:9013890}. +P08905 LYZ2_MOUSE Lysozyme C-2 (EC 3.2.1.17) (1,4-beta-N-acetylmuramidase C) (Lysozyme C type M) 148 16,689 Active site (2); Beta strand (7); Chain (1); Disulfide bond (4); Erroneous initiation (3); Helix (8); Signal peptide (1); Turn (3) FUNCTION: Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Lyz2 is active against a range of Gram-positive and Gram-negative bacteria. More effective than Lyz1 in killing Gram-negative bacteria. Lyz1 and Lyz2 are equally effective in killing Gram-positive bacteria. {ECO:0000255|PROSITE-ProRule:PRU00680, ECO:0000269|PubMed:14977423}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Monomer. {ECO:0000269|PubMed:12613666}. TISSUE SPECIFICITY: Expressed weakly in myeloblasts, moderately in immature macrophages, and strongly in both mature macrophages and macrophage-rich tissues. +Q99N08 M4A6C_MOUSE Membrane-spanning 4-domains subfamily A member 6C 217 23,622 Alternative sequence (2); Chain (1); Sequence conflict (6); Topological domain (5); Transmembrane (4) TRANSMEM 47 67 Helical. {ECO:0000255}.; TRANSMEM 85 105 Helical. {ECO:0000255}.; TRANSMEM 122 142 Helical. {ECO:0000255}.; TRANSMEM 187 207 Helical. {ECO:0000255}. TOPO_DOM 1 46 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 68 84 Extracellular. {ECO:0000255}.; TOPO_DOM 106 121 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 143 186 Extracellular. {ECO:0000255}.; TOPO_DOM 208 217 Cytoplasmic. {ECO:0000255}. FUNCTION: May be involved in signal transduction as a component of a multimeric receptor complex. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed only by thymus, spleen, peripheral lymph node and bone marrow. +Q8BVN9 MAEL_MOUSE Protein maelstrom homolog 434 49,371 Chain (1); DNA binding (1) FUNCTION: Plays a central role during spermatogenesis by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons. Its association with piP-bodies suggests a participation in the secondary piRNAs metabolic process. Required for the localization of germ-cell factors to the meiotic nuage. {ECO:0000269|PubMed:18694567, ECO:0000269|PubMed:20011505}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18694567, ECO:0000269|PubMed:20011505}. Nucleus {ECO:0000269|PubMed:16787967, ECO:0000269|PubMed:18694567}. Note=Component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis. Recruited to perinuclear nuage during spermatogenesis. Specifically localizes to piP-bodies, a subset of the nuage which contains secondary piRNAs. PIWIL2 is required for its localization to piP-bodies. PubMed:16787967, reported an association with the nuclear XY body, however, PubMed:18694567 showed that it is not the case because the antibody used by PubMed:16787967 still stains the nuclear XY body in spermatocytes lacking Mael. Moreover other antibodies raized against the same epitope used in PubMed:16787967 do not recognize any epitopes on XY chromosomes but show a clear localization to the meiotic nuage. {ECO:0000269|PubMed:16787967, ECO:0000269|PubMed:18694567, ECO:0000269|PubMed:20011505}. SUBUNIT: Interacts with SMARCB1, SIN3B and DDX4. Interacts with piRNA-associated proteins TDRD1, PIWIL1 and PIWIL2. Interacts with Tex19.1 and, probably, Tex19.2 (PubMed:28254886). {ECO:0000269|PubMed:16787967, ECO:0000269|PubMed:28254886}. TISSUE SPECIFICITY: Testis-specific. Present in spermatocytes and round and early elongating spermatids. {ECO:0000269|PubMed:16787967, ECO:0000269|PubMed:18694567}. +Q9D0U6 MAF1_MOUSE Repressor of RNA polymerase III transcription MAF1 homolog 258 28,780 Chain (1); Cross-link (1); Modified residue (8); Sequence conflict (1) FUNCTION: Element of the mTORC1 signaling pathway that acts as a mediator of diverse signals and that represses RNA polymerase III transcription. Inhibits the de novo assembly of TFIIIB onto DNA (By similarity). {ECO:0000250}. PTM: Phosphorylated at Ser-60, Ser-68 and Ser-75; the major sites of phosphorylation. Nuclear accumulation correlates with a concomitant dephosphorylation. Phosphorylation may attenuate its RNA polymerase III-repressive function (By similarity). {ECO:0000250}.; PTM: Sumoylated with SUMO1 and SUMO2, mainly on Lys-35. Desumoylated by SENP1. SUMOylation promotes the ability of MAF1 to repress transcription and suppress colony formation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20543138}. Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with BRF2. {ECO:0000250}. +Q8VDG6 M3K21_MOUSE Mitogen-activated protein kinase kinase kinase 21 (EC 2.7.11.25) (Mitogen-activated protein kinase kinase kinase MLK4) (Mixed lineage kinase 4) 1002 110,112 Active site (1); Binding site (1); Chain (1); Compositional bias (1); Domain (2); Erroneous initiation (1); Frameshift (1); Modified residue (7); Nucleotide binding (1); Region (2); Sequence conflict (1) FUNCTION: Negative regulator of TLR4 signaling. Does not activate JNK1/MAPK8 pathway, p38/MAPK14, nor ERK2/MAPK1 pathways (By similarity). {ECO:0000250}. PTM: Autophosphorylation on serine and threonine residues within the activation loop plays a role in enzyme activation. {ECO:0000250|UniProtKB:P80192}. SUBUNIT: Homodimer. Interacts with TLR4. {ECO:0000250}. +Q922B1 MACD1_MOUSE ADP-ribose glycohydrolase MACROD1 (MACRO domain-containing protein 1) (O-acetyl-ADP-ribose deacetylase MACROD1) (EC 3.5.1.-) (Protein LRP16) ([Protein ADP-ribosylaspartate] hydrolase MACROD1) (EC 3.2.2.-) ([Protein ADP-ribosylglutamate] hydrolase MACROD1) (EC 3.2.2.-) 323 35,295 Binding site (1); Chain (1); Cross-link (1); Domain (1); Erroneous initiation (2); Modified residue (4); Region (4) FUNCTION: Removes ADP-ribose from asparatate and glutamate residues in proteins bearing a single ADP-ribose moiety. Inactive towards proteins bearing poly-ADP-ribose. Deacetylates O-acetyl-ADP ribose, a signaling molecule generated by the deacetylation of acetylated lysine residues in histones and other proteins. Plays a role in estrogen signaling. Binds to androgen receptor (AR) and amplifies the transactivation function of AR in response to androgen. May play an important role in carcinogenesis and/or progression of hormone-dependent cancers by feed-forward mechanism that activates ESR1 transactivation. Could be an ESR1 coactivator, providing a positive feedback regulatory loop for ESR1 signal transduction. Could be involved in invasive growth by down-regulating CDH1 in endometrial cancer cells. Enhances ESR1-mediated transcription activity. {ECO:0000250|UniProtKB:Q9BQ69}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BQ69}. Note=Recruited to DNA lesions, probably via mono-APD-ribosylated proteins. {ECO:0000250|UniProtKB:Q9BQ69}. SUBUNIT: Interacts with ESR1; Interacts in a manner that is estrogen independent but is enhanced by estrogen. Interacts (via macro domain) with AR. {ECO:0000250|UniProtKB:Q9BQ69}. +P20917 MAG_MOUSE Myelin-associated glycoprotein (Siglec-4a) 626 69,260 Alternative sequence (2); Beta strand (26); Binding site (1); Chain (1); Disulfide bond (7); Domain (5); Glycosylation (9); Helix (8); Lipidation (1); Modified residue (4); Mutagenesis (8); Region (4); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (2) TRANSMEM 517 536 Helical. {ECO:0000255}. TOPO_DOM 20 516 Extracellular. {ECO:0000255}.; TOPO_DOM 537 626 Cytoplasmic. {ECO:0000255}. FUNCTION: Adhesion molecule that mediates interactions between myelinating cells and neurons by binding to neuronal sialic acid-containing gangliosides and to the glycoproteins RTN4R and RTN4RL2 (PubMed:7533044, PubMed:12089450, PubMed:27922006). Not required for initial myelination, but seems to play a role in the maintenance of normal axon myelination (PubMed:7516497, PubMed:9262180, PubMed:9482781, PubMed:9482783, PubMed:9469574, PubMed:10625334). Protects motoneurons against apoptosis, also after injury; protection against apoptosis is probably mediated via interaction with neuronal RTN4R and RTN4RL2 (PubMed:26335717). Required to prevent degeneration of myelinated axons in adults; this probably depends on binding to gangliosides on the axon cell membrane (PubMed:15953602, PubMed:19158290). Negative regulator of neurite outgrowth that inhibits axon longitudinal growth (PubMed:19158290, PubMed:27922006, PubMed:12089450). Negative regulator of neurite outgrowth; in dorsal root ganglion neurons the inhibition is mediated primarily via binding to neuronal RTN4R or RTN4RL2 and to a lesser degree via binding to neuronal gangliosides (PubMed:17640868). In cerebellar granule cells the inhibition is mediated via binding to neuronal gangliosides (PubMed:17640868). In sensory neurons, inhibition of neurite extension depends only partially on RTN4R, RTN4RL2 and gangliosides (By similarity). Inhibits axon outgrowth by binding to RTN4R (PubMed:12089450). Preferentially binds to alpha-2,3-linked sialic acid (PubMed:7533044, PubMed:27922006). Binds ganglioside Gt1b (PubMed:27922006). {ECO:0000250|UniProtKB:P07722, ECO:0000269|PubMed:10625334, ECO:0000269|PubMed:12089450, ECO:0000269|PubMed:15953602, ECO:0000269|PubMed:17640868, ECO:0000269|PubMed:19158290, ECO:0000269|PubMed:26335717, ECO:0000269|PubMed:27922006, ECO:0000269|PubMed:7516497, ECO:0000269|PubMed:7533044, ECO:0000269|PubMed:9262180, ECO:0000269|PubMed:9469574, ECO:0000269|PubMed:9482781, ECO:0000269|PubMed:9482783}. PTM: N-glycosylated. {ECO:0000269|PubMed:1716323, ECO:0000269|PubMed:27922006}.; PTM: Phosphorylated on tyrosine residues. {ECO:0000250|UniProtKB:P07722}.; PTM: Ubiquitinated, leading to proteasomal degradation. {ECO:0000269|PubMed:24191038}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7533044, ECO:0000269|PubMed:9482783}; Single-pass type I membrane protein {ECO:0000269|PubMed:7533044, ECO:0000269|PubMed:9482783}. Membrane raft {ECO:0000250|UniProtKB:P07722}. SUBUNIT: Monomer and homodimer (PubMed:27922006). Interacts (via the first three N-terminal Ig-like domains) with RTN4R and RTN4RL2 (PubMed:12089450, PubMed:26335717). {ECO:0000269|PubMed:12089450, ECO:0000269|PubMed:26335717, ECO:0000269|PubMed:27922006}. DOMAIN: The C-terminal cytoplasmic region found only in isoform L-MAG is required for normal myelination in the central nervous system (CNS), but is apparently not required for normal myelination in the peripheral nervous system (PNS). {ECO:0000269|PubMed:9482783}.; DOMAIN: The extracellular domain is required to protect against axon degeneration (PubMed:19158290, PubMed:26335717). The first three Ig-like domains mediate interaction with RTN4R and RTN4RL2, but are not sufficient to inhibit neurite outgrowth (By similarity). The two C-terminal extracellular Ig-like C2-type domains are required for inhibition of axon longitudinal growth. Besides, the two C-terminal extracellular Ig-like C2-type domains are required for protection against apoptosis after nerve injury (PubMed:26335717). {ECO:0000250|UniProtKB:P07722, ECO:0000269|PubMed:19158290, ECO:0000269|PubMed:26335717}. TISSUE SPECIFICITY: Detected in the myelin tract in brain, especially in the corpus callosum and in peripheral nerve (PubMed:7516497, PubMed:9482783, PubMed:24191038). Expressed by myelinating glial cells in the central and peripheral nervous system (PubMed:10625334). Detected in oligodendrocyte processes before formation of compact myelin (PubMed:2474006, PubMed:10625334). Restricted to the periaxonal space after myelination (PubMed:10625334). Isoform S-MAG is the predominant isoform in CNS and PNS of the adult (at protein level) (PubMed:1716323). {ECO:0000269|PubMed:10625334, ECO:0000269|PubMed:1716323, ECO:0000269|PubMed:24191038, ECO:0000269|PubMed:2474006, ECO:0000269|PubMed:7516497, ECO:0000269|PubMed:9482783}. +Q8BQR7 MAGBI_MOUSE Melanoma-associated antigen B18 (MAGE-B18 antigen) 327 37,203 Chain (1); Domain (1) FUNCTION: May enhance ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex. {ECO:0000250|UniProtKB:Q96M61}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22332604}. SUBUNIT: Interacts with LNX1. {ECO:0000250|UniProtKB:Q96M61}. TISSUE SPECIFICITY: Expressed in testis, stomach, large intestine, small intestine, spleen, lymph node, bone marrow lymphocytes and blood T-lymphocytes. Not detected in brain, heart, lung, liver or kidney (at protein level). {ECO:0000269|PubMed:22332604}. +A2AEY4 MA7D3_MOUSE MAP7 domain-containing protein 3 876 98,230 Alternative sequence (1); Chain (1); Coiled coil (3); Erroneous gene model prediction (1); Erroneous initiation (3); Modified residue (2); Sequence conflict (1) FUNCTION: Promotes the assembly and stability of microtubules. {ECO:0000250|UniProtKB:Q8IWC1}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q8IWC1}. Note=Localizes to the microtubules throughout mitosis. {ECO:0000250|UniProtKB:Q8IWC1}. TISSUE SPECIFICITY: High expression in lung, skeletal muscle, brain, and kidney, with much weaker expression in spleen, small intestine, liver, and heart. {ECO:0000269|PubMed:22142902}. +A2AQW0 M3K15_MOUSE Mitogen-activated protein kinase kinase kinase 15 (EC 2.7.11.25) (MAPK/ERK kinase kinase 15) (MEK kinase 15) (MEKK 15) 1331 149,327 Active site (1); Binding site (1); Chain (1); Coiled coil (1); Compositional bias (3); Domain (1); Nucleotide binding (1) FUNCTION: May function in a signal transduction pathway that is activated by various cell stresses and leads to apoptosis. {ECO:0000250}. +Q9D8X0 MANBL_MOUSE Protein MANBAL 85 9,340 Chain (1); Sequence conflict (2); Transmembrane (1) TRANSMEM 24 44 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +O89029 MATN4_MOUSE Matrilin-4 (MAT-4) 624 68,918 Alternative sequence (1); Chain (1); Coiled coil (1); Disulfide bond (12); Domain (6); Glycosylation (2); Natural variant (2); Signal peptide (1) FUNCTION: Major component of the extracellular matrix of cartilage. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Interacts with COMP. {ECO:0000250}. TISSUE SPECIFICITY: Lung, brain, sternum, kidney and heart. +Q8VCF0 MAVS_MOUSE Mitochondrial antiviral-signaling protein (MAVS) (CARD adapter inducing interferon beta) (Cardif) (Interferon beta promoter stimulator protein 1) (IPS-1) (Virus-induced-signaling adapter) (VISA) 503 53,399 Chain (1); Domain (1); Modified residue (9); Region (5); Topological domain (2); Transmembrane (1) TRANSMEM 479 496 Helical. {ECO:0000255}. TOPO_DOM 1 478 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 497 503 Mitochondrial intermembrane. {ECO:0000305}. FUNCTION: Required for innate immune defense against viruses. Acts downstream of DHX33, DDX58/RIG-I and IFIH1/MDA5, which detect intracellular dsRNA produced during viral replication, to coordinate pathways leading to the activation of NF-kappa-B, IRF3 and IRF7, and to the subsequent induction of antiviral cytokines such as IFN-beta and RANTES (CCL5). Peroxisomal and mitochondrial MAVS act sequentially to create an antiviral cellular state. Upon viral infection, peroxisomal MAVS induces the rapid interferon-independent expression of defense factors that provide short-term protection, whereas mitochondrial MAVS activates an interferon-dependent signaling pathway with delayed kinetics, which amplifies and stabilizes the antiviral response. May activate the same pathways following detection of extracellular dsRNA by TLR3. May protect cells from apoptosis (By similarity). {ECO:0000250|UniProtKB:Q7Z434, ECO:0000269|PubMed:24037184}. PTM: Ubiquitinated. Undergoes 'Lys-48'-linked polyubiquitination catalyzed by ITCH; ITCH-dependent polyubiquitination is mediated by the interaction with PCBP2 and leads to MAVS/IPS1 proteasomal degradation. Ubiquitinated by RNF125, leading to its degradation by the proteasome. Undergoes 'Lys-48'-linked ubiquitination catalyzed by SMURF1. {ECO:0000250|UniProtKB:Q7Z434}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q7Z434}. Mitochondrion {ECO:0000250|UniProtKB:Q7Z434}. Peroxisome {ECO:0000250|UniProtKB:Q7Z434}. SUBUNIT: Self-associates and polymerizes (via CARD domains) to form 400 nM long three-stranded helical filaments on mitochondria, filament nucleation requires interaction with DDX58/RIG-I whose CARD domains act as a template for filament assembly (By similarity). Interacts with DDX58/RIG-I, IFIH1/MDA5, TRAF2, TRAF6 and C1QBP. May interact with IRF3, FADD, RIPK1, IKBKE, CHUK and IKBKB. Interacts with NLRX1. Interaction with NLRX1 requires the CARD domain. Interacts with PSMA7. Interacts with TRAFD1. Interacts (via C-terminus) with PCBP2 in a complex containing MAVS/IPS1, PCBP2 and ITCH. Interacts with CYLD. Interacts with SRC. Interacts with DHX58/LGP2 and IKBKE. Interacts with TMEM173/MITA. Interacts with IFIT3 (via N-terminus). Interacts with TBK1 only in the presence of IFIT3. Interacts with MUL1. Interacts with ANKRD17. Interacts with NDFIP1 (By similarity). Interacts with SMURF1; the interaction is mediated by NDFIP1 and leads to MAVS ubiquitination and degradation (PubMed:23087404). Interacts (via C-terminus) with GPATCH3; the interaction is markedly increased upon viral infection (By similarity). Directly interacts (via CARD domain) with ATG5 and ATG12, either as ATG5 and ATG12 monomers or as ATG12-ATG5 conjugates (By similarity). Interacts with DHX33 (via the helicase C-terminal domain) (PubMed:24037184). {ECO:0000250|UniProtKB:Q7Z434, ECO:0000269|PubMed:18849341, ECO:0000269|PubMed:23087404, ECO:0000269|PubMed:24037184}. DOMAIN: Both CARD and transmembrane domains are essential for antiviral function. The CARD domain is responsible for interaction with DDX58/RIG-I and IFIH1/MDA5 (By similarity). {ECO:0000250|UniProtKB:Q7Z434}.; DOMAIN: The transmembrane domain and residues 285-420 are essential for its interaction with DHX58/LGP2. {ECO:0000250|UniProtKB:Q7Z434}. +P28574 MAX_MOUSE Protein max (Myc-associated factor X) (Myc-binding novel HLH/LZ protein) (Protein myn) 160 18,245 Alternative sequence (1); Chain (1); Domain (1); Helix (2); Initiator methionine (1); Modified residue (7); Region (1); Sequence conflict (2) FUNCTION: Transcription regulator. Forms a sequence-specific DNA-binding protein complex with MYC or MAD which recognizes the core sequence 5'-CAC[GA]TG-3'. The MYC:MAX complex is a transcriptional activator, whereas the MAD:MAX complex is a repressor. CpG methylation of the recognition site greatly inhibits DNA binding, suggesting that DNA methylation may regulate the MYC:MAX complex in vivo. May repress transcription via the recruitment of a chromatin remodeling complex containing H3 'Lys-9' histone methyltransferase activity. Represses MYC transcriptional activity from E-box elements (By similarity). {ECO:0000250|UniProtKB:P61244}. PTM: Phosphorylated. {ECO:0000305}. SUBCELLULAR LOCATION: Nucleus. Cell projection, dendrite {ECO:0000250}. SUBUNIT: Efficient DNA binding requires dimerization with another bHLH protein. Binds DNA as a heterodimer with MYC or MAD. Part of the E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1, RING1, RNF2, MBLR, L3MBTL2 and YAF2. Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Interacts with SPAG9. The heterodimer MYC:MAX interacts with ABI1; the interaction may enhance MYC:MAX transcriptional activity. {ECO:0000269|PubMed:12391307, ECO:0000269|PubMed:9680483}. +P39039 MBL1_MOUSE Mannose-binding protein A (MBP-A) (Mannan-binding protein) (Ra-reactive factor polysaccharide-binding component p28B) (RaRF p28B) 239 25,396 Alternative sequence (1); Chain (1); Disulfide bond (2); Domain (2); Glycosylation (4); Metal binding (9); Modified residue (10); Region (1); Signal peptide (1) FUNCTION: Calcium-dependent lectin. Plays a role in the innate immune response by binding mannose, fucose and N-acetylglucosamine moieties on different microorganisms and mediating activation of the lectin complement pathway (By similarity). Binds to late apoptotic cells, as well as to apoptotic blebs and to necrotic cells, but not to early apoptotic cells, facilitating their uptake by macrophages (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P19999}. PTM: Hydroxylated on lysine and proline residues within the collagen-like domain. {ECO:0000250|UniProtKB:P19999}.; PTM: O-glycosylated. O-linked glycans on hydroxylysine residues consist of Glc-Gal disaccharides bound to the oxygen atom of post-translationally added hydroxyl groups. {ECO:0000250|UniProtKB:P19999}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1637828, ECO:0000269|PubMed:25419660}. SUBUNIT: Homotrimer (By similarity). Forms higher oligomeric complexes formed by the association of two, three or more homotrimers (PubMed:25419660). Oligomerization occurs in the endoplasmic reticulum (By similarity). Interacts with MASP1 and MASP2 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P19999, ECO:0000269|PubMed:25419660}. DOMAIN: The helical collagen-like domains from three protein chains assemble into a coiled coil and mediate trimerization. {ECO:0000250|UniProtKB:P19999}. TISSUE SPECIFICITY: Detected in liver and blood serum (at protein level) (PubMed:1637828, PubMed:25419660). Detected in liver (PubMed:1712818). {ECO:0000269|PubMed:1637828, ECO:0000269|PubMed:1712818, ECO:0000269|PubMed:25419660}. +P41317 MBL2_MOUSE Mannose-binding protein C (MBP-C) (Mannan-binding protein) (RA-reactive factor P28A subunit) (RARF/P28A) 244 25,957 Chain (1); Coiled coil (1); Disulfide bond (4); Domain (2); Glycosylation (1); Modified residue (5); Sequence conflict (2); Signal peptide (1) FUNCTION: Calcium-dependent lectin involved in innate immune defense. Binds mannose, fucose and N-acetylglucosamine on different microorganisms and activates the lectin complement pathway. Binds to late apoptotic cells, as well as to apoptotic blebs and to necrotic cells, but not to early apoptotic cells, facilitating their uptake by macrophages (By similarity). {ECO:0000250}. PTM: Hydroxylation on proline residues within the sequence motif, GXPG, is most likely to be 4-hydroxy as this fits the requirement for 4-hydroxylation in vertebrates. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Oligomeric complex of 3 or more homotrimers. Interacts with MASP1 and MASP2 (By similarity). Interacts with MEP1A and MEP1B and may inhibit their catalytic activity (By similarity). {ECO:0000250}. DOMAIN: The coiled-coil domain mediates trimerization. {ECO:0000250}. +Q8BWY4 MBLC1_MOUSE Metallo-beta-lactamase domain-containing protein 1 (EC 3.-.-.-) 260 26,923 Chain (1); Metal binding (6); Sequence conflict (1) +Q8BL86 MBLC2_MOUSE Metallo-beta-lactamase domain-containing protein 2 (EC 3.-.-.-) 279 31,205 Chain (1); Initiator methionine (1); Metal binding (8); Modified residue (1); Sequence conflict (2) +Q9Z2Z6 MCAT_MOUSE Mitochondrial carnitine/acylcarnitine carrier protein (Carnitine/acylcarnitine translocase) (CAC) (mCAC) (Solute carrier family 25 member 20) 301 33,027 Chain (1); Initiator methionine (1); Modified residue (5); Repeat (3); Topological domain (7); Transmembrane (6) TRANSMEM 13 31 Helical; Name=1. {ECO:0000255}.; TRANSMEM 74 93 Helical; Name=2. {ECO:0000255}.; TRANSMEM 113 131 Helical; Name=3. {ECO:0000255}.; TRANSMEM 171 190 Helical; Name=4. {ECO:0000255}.; TRANSMEM 212 230 Helical; Name=5. {ECO:0000255}.; TRANSMEM 268 287 Helical; Name=6. {ECO:0000255}. TOPO_DOM 2 12 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 32 73 Mitochondrial matrix. {ECO:0000255}.; TOPO_DOM 94 112 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 132 170 Mitochondrial matrix. {ECO:0000255}.; TOPO_DOM 191 211 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 231 267 Mitochondrial matrix. {ECO:0000255}.; TOPO_DOM 288 301 Cytoplasmic. {ECO:0000255}. FUNCTION: Mediates the transport of acylcarnitines of different length across the mitochondrial inner membrane from the cytosol to the mitochondrial matrix for their oxidation by the mitochondrial fatty acid-oxidation pathway. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed, with highest levels in the liver, intermediate levels in heart, testis and kidney and low levels in brain, including cortex, cerebellum, hippocampus and hypothalamus. {ECO:0000269|PubMed:19287344}. +Q1HFZ0 NSUN2_MOUSE tRNA (cytosine(34)-C(5))-methyltransferase (EC 2.1.1.203) (Myc-induced SUN domain-containing protein) (Misu) (NOL1/NOP2/Sun domain family member 2) 757 85,452 Active site (1); Alternative sequence (1); Binding site (3); Chain (1); Cross-link (7); Erroneous initiation (2); Modified residue (9); Region (1); Sequence conflict (7) FUNCTION: RNA methyltransferase that methylates tRNAs, and possibly RNA polymerase III transcripts. Methylates cytosine to 5-methylcytosine (m5C) at positions 34 and 48 of intron-containing tRNA(Leu)(CAA) precursors, and at positions 48, 49 and 50 of tRNA(Gly)(GCC) precursors (By similarity). May act downstream of Myc to regulate epidermal cell growth and proliferation. Required for proper spindle assembly and chromosome segregation, independently of its methyltransferase activity. {ECO:0000250, ECO:0000269|PubMed:16713953, ECO:0000269|PubMed:19596847}. PTM: Phosphorylated at Ser-139 by AURKB during mitosis, leading to abolish methyltransferase activity and the interaction with NPM1. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus. Cytoplasm, cytoskeleton, spindle. Note=Concentrated in the nucleolus during interphase and translocates to the spindle during mitosis as an RNA-protein complex that includes 18S ribosomal RNA. SUBUNIT: Interacts with NPM1 and NCL during interphase; interaction is disrupted following phosphorylation at Ser-139. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed at low level. Up-regulated in tumors. {ECO:0000269|PubMed:16713953}. +Q8K4F6 NSUN5_MOUSE Probable 28S rRNA (cytosine-C(5))-methyltransferase (EC 2.1.1.-) (NOL1/NOP2/Sun domain family member 5) (Williams-Beuren syndrome chromosomal region 20A protein homolog) 465 51,030 Active site (1); Binding site (3); Chain (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (2); Region (1); Sequence conflict (4) FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the C(5) position of a cytosine in 28S rRNA. {ECO:0000250}. +Q9WUI1 MK11_MOUSE Mitogen-activated protein kinase 11 (MAP kinase 11) (MAPK 11) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 beta) (MAP kinase p38 beta) (p38B) 364 41,397 Active site (1); Binding site (2); Chain (1); Domain (1); Modified residue (3); Motif (1); Nucleotide binding (1); Region (2); Sequence conflict (2) FUNCTION: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK11 is one of the four p38 MAPKs which play an important role in the cascades of cellular responses evoked by extracellular stimuli such as proinflammatory cytokines or physical stress leading to direct activation of transcription factors. Accordingly, p38 MAPKs phosphorylate a broad range of proteins and it has been estimated that they may have approximately 200 to 300 substrates each. MAPK11 functions are mostly redundant with those of MAPK14. Some of the targets are downstream kinases which are activated through phosphorylation and further phosphorylate additional targets. RPS6KA5/MSK1 and RPS6KA4/MSK2 can directly phosphorylate and activate transcription factors such as CREB1, ATF1, the NF-kappa-B isoform RELA/NFKB3, STAT1 and STAT3, but can also phosphorylate histone H3 and the nucleosomal protein HMGN1. RPS6KA5/MSK1 and RPS6KA4/MSK2 play important roles in the rapid induction of immediate-early genes in response to stress or mitogenic stimuli, either by inducing chromatin remodeling or by recruiting the transcription machinery. On the other hand, two other kinase targets, MAPKAPK2/MK2 and MAPKAPK3/MK3, participate in the control of gene expression mostly at the post-transcriptional level, by phosphorylating ZFP36 (tristetraprolin) and ELAVL1, and by regulating EEF2K, which is important for the elongation of mRNA during translation. MKNK1/MNK1 and MKNK2/MNK2, two other kinases activated by p38 MAPKs, regulate protein synthesis by phosphorylating the initiation factor EIF4E2. In the cytoplasm, the p38 MAPK pathway is an important regulator of protein turnover. For example, CFLAR is an inhibitor of TNF-induced apoptosis whose proteasome-mediated degradation is regulated by p38 MAPK phosphorylation. Ectodomain shedding of transmembrane proteins is regulated by p38 MAPKs as well. In response to inflammatory stimuli, p38 MAPKs phosphorylate the membrane-associated metalloprotease ADAM17. Such phosphorylation is required for ADAM17-mediated ectodomain shedding of TGF-alpha family ligands, which results in the activation of EGFR signaling and cell proliferation. Additional examples of p38 MAPK substrates are the FGFR1. FGFR1 can be translocated from the extracellular space into the cytosol and nucleus of target cells, and regulates processes such as rRNA synthesis and cell growth. FGFR1 translocation requires p38 MAPK activation. In the nucleus, many transcription factors are phosphorylated and activated by p38 MAPKs in response to different stimuli. Classical examples include ATF1, ATF2, ATF6, ELK1, PTPRH, DDIT3, TP53/p53 and MEF2C and MEF2A. The p38 MAPKs are emerging as important modulators of gene expression by regulating chromatin modifiers and remodelers. The promoters of several genes involved in the inflammatory response, such as IL6, IL8 and IL12B, display a p38 MAPK-dependent enrichment of histone H3 phosphorylation on 'Ser-10' (H3S10ph) in LPS-stimulated myeloid cells. This phosphorylation enhances the accessibility of the cryptic NF-kappa-B-binding sites marking promoters for increased NF-kappa-B recruitment. {ECO:0000269|PubMed:11909979}. PTM: Dually phosphorylated on Thr-180 and Tyr-182 by MAP2K3/MKK3, MAP2K4/MKK4 and MAP2K6/MKK6, which activates the enzyme. {ECO:0000269|PubMed:20004242}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Interacts with HDAC3 and DUSP16. {ECO:0000250}. DOMAIN: The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases. +P47811 MK14_MOUSE Mitogen-activated protein kinase 14 (MAP kinase 14) (MAPK 14) (EC 2.7.11.24) (CRK1) (Mitogen-activated protein kinase p38 alpha) (MAP kinase p38 alpha) 360 41,287 Active site (1); Alternative sequence (4); Beta strand (13); Binding site (9); Chain (1); Domain (1); Helix (21); Initiator methionine (1); Modified residue (10); Motif (1); Mutagenesis (2); Nucleotide binding (1); Region (1); Sequence conflict (13); Turn (3) FUNCTION: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK14 is one of the four p38 MAPKs which play an important role in the cascades of cellular responses evoked by extracellular stimuli such as proinflammatory cytokines or physical stress leading to direct activation of transcription factors. Accordingly, p38 MAPKs phosphorylate a broad range of proteins and it has been estimated that they may have approximately 200 to 300 substrates each. Some of the targets are downstream kinases which are activated through phosphorylation and further phosphorylate additional targets. RPS6KA5/MSK1 and RPS6KA4/MSK2 can directly phosphorylate and activate transcription factors such as CREB1, ATF1, the NF-kappa-B isoform RELA/NFKB3, STAT1 and STAT3, but can also phosphorylate histone H3 and the nucleosomal protein HMGN1. RPS6KA5/MSK1 and RPS6KA4/MSK2 play important roles in the rapid induction of immediate-early genes in response to stress or mitogenic stimuli, either by inducing chromatin remodeling or by recruiting the transcription machinery. On the other hand, two other kinase targets, MAPKAPK2/MK2 and MAPKAPK3/MK3, participate in the control of gene expression mostly at the post-transcriptional level, by phosphorylating ZFP36 (tristetraprolin) and ELAVL1, and by regulating EEF2K, which is important for the elongation of mRNA during translation. MKNK1/MNK1 and MKNK2/MNK2, two other kinases activated by p38 MAPKs, regulate protein synthesis by phosphorylating the initiation factor EIF4E2. MAPK14 interacts also with casein kinase II, leading to its activation through autophosphorylation and further phosphorylation of TP53/p53. In the cytoplasm, the p38 MAPK pathway is an important regulator of protein turnover. For example, CFLAR is an inhibitor of TNF-induced apoptosis whose proteasome-mediated degradation is regulated by p38 MAPK phosphorylation. In a similar way, MAPK14 phosphorylates the ubiquitin ligase SIAH2, regulating its activity towards EGLN3. MAPK14 may also inhibit the lysosomal degradation pathway of autophagy by interfering with the intracellular trafficking of the transmembrane protein ATG9. Another function of MAPK14 is to regulate the endocytosis of membrane receptors by different mechanisms that impinge on the small GTPase RAB5A. In addition, clathrin-mediated EGFR internalization induced by inflammatory cytokines and UV irradiation depends on MAPK14-mediated phosphorylation of EGFR itself as well as of RAB5A effectors. Ectodomain shedding of transmembrane proteins is regulated by p38 MAPKs as well. In response to inflammatory stimuli, p38 MAPKs phosphorylate the membrane-associated metalloprotease ADAM17. Such phosphorylation is required for ADAM17-mediated ectodomain shedding of TGF-alpha family ligands, which results in the activation of EGFR signaling and cell proliferation. Another p38 MAPK substrate is FGFR1. FGFR1 can be translocated from the extracellular space into the cytosol and nucleus of target cells, and regulates processes such as rRNA synthesis and cell growth. FGFR1 translocation requires p38 MAPK activation. In the nucleus, many transcription factors are phosphorylated and activated by p38 MAPKs in response to different stimuli. Classical examples include ATF1, ATF2, ATF6, ELK1, PTPRH, DDIT3, TP53/p53 and MEF2C and MEF2A. The p38 MAPKs are emerging as important modulators of gene expression by regulating chromatin modifiers and remodelers. The promoters of several genes involved in the inflammatory response, such as IL6, IL8 and IL12B, display a p38 MAPK-dependent enrichment of histone H3 phosphorylation on 'Ser-10' (H3S10ph) in LPS-stimulated myeloid cells. This phosphorylation enhances the accessibility of the cryptic NF-kappa-B-binding sites marking promoters for increased NF-kappa-B recruitment. Phosphorylates CDC25B and CDC25C which is required for binding to 14-3-3 proteins and leads to initiation of a G2 delay after ultraviolet radiation. Phosphorylates TIAR following DNA damage, releasing TIAR from GADD45A mRNA and preventing mRNA degradation. The p38 MAPKs may also have kinase-independent roles, which are thought to be due to the binding to targets in the absence of phosphorylation. Protein O-Glc-N-acylation catalyzed by the OGT is regulated by MAPK14, and, although OGT does not seem to be phosphorylated by MAPK14, their interaction increases upon MAPK14 activation induced by glucose deprivation. This interaction may regulate OGT activity by recruiting it to specific targets such as neurofilament H, stimulating its O-Glc-N-acylation. Required in mid-fetal development for the growth of embryo-derived blood vessels in the labyrinth layer of the placenta. Also plays an essential role in developmental and stress-induced erythropoiesis, through regulation of EPO gene expression. Phosphorylates S100A9 at 'Thr-113' (By similarity). {ECO:0000250|UniProtKB:Q16539, ECO:0000269|PubMed:10704466, ECO:0000269|PubMed:10943842, ECO:0000269|PubMed:11909979, ECO:0000269|PubMed:15735649}. PTM: Dually phosphorylated on Thr-180 and Tyr-182 by the MAP2Ks MAP2K3/MKK3, MAP2K4/MKK4 and MAP2K6/MKK6 in response to inflammatory cytokines, environmental stress or growth factors, which activates the enzyme. Dual phosphorylation can also be mediated by TAB1-mediated autophosphorylation. TCR engagement in T-cells also leads to Tyr-323 phosphorylation by ZAP70. Dephosphorylated and inactivated by DUPS1, DUSP10 and DUSP16. PPM1D also mediates dephosphorylation and inactivation of MAPK14 (By similarity). {ECO:0000250|UniProtKB:Q16539, ECO:0000269|PubMed:15735649, ECO:0000269|PubMed:18669639}.; PTM: Acetylated at Lys-53 and Lys-152 by KAT2B and EP300. Acetylation at Lys-53 increases the affinity for ATP and enhances kinase activity. Lys-53 and Lys-152 are deacetylated by HDAC3 (By similarity). {ECO:0000250|UniProtKB:Q16539}.; PTM: Ubiquitinated. Ubiquitination leads to degradation by the proteasome pathway (By similarity). {ECO:0000250|UniProtKB:Q16539}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10601328}. Nucleus {ECO:0000269|PubMed:10601328}. SUBUNIT: Component of a signaling complex containing at least AKAP13, PKN1, MAPK14, ZAK and MAP2K3. Within this complex, AKAP13 interacts directly with PKN1, which in turn recruits MAPK14, MAP2K3 and ZAK (By similarity). Binds to a kinase interaction motif within the protein tyrosine phosphatase, PTPRR (By similarity). This interaction retains MAPK14 in the cytoplasm and prevents nuclear accumulation (By similarity). Interacts with SPAG9 and GADD45A (By similarity). Interacts with CDC25B, CDC25C, DUSP1, DUSP10, DUSP16, NP60, SUPT20H and TAB1. Interacts with casein kinase II subunits CSNK2A1 and CSNK2B. Interacts with PPM1D. Interacts with CDK5RAP3; recruits PPM1D to MAPK14 and may regulate its dephosphorylation (By similarity). {ECO:0000250|UniProtKB:Q16539, ECO:0000269|PubMed:10601328, ECO:0000269|PubMed:10943842, ECO:0000269|PubMed:12391307, ECO:0000269|PubMed:15735649, ECO:0000269|PubMed:16751104, ECO:0000269|PubMed:22375048}. DOMAIN: The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases. TISSUE SPECIFICITY: Macrophages, monocytes, T- and B-lymphocytes. Isoform 2 is specifically expressed in kidney and liver. +Q9JI70 MKKS_MOUSE McKusick-Kaufman/Bardet-Biedl syndromes putative chaperonin (Protein Bbs6 homolog) 570 61,924 Chain (1); Nucleotide binding (1); Region (1); Sequence conflict (1) FUNCTION: Probable molecular chaperone that assists the folding of proteins upon ATP hydrolysis (By similarity). Plays a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia (PubMed:28753627). May play a role in protein processing in limb, cardiac and reproductive system development. May play a role in cytokinesis (By similarity). {ECO:0000250|UniProtKB:Q9NPJ1, ECO:0000269|PubMed:28753627}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9NPJ1}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9NPJ1}. Nucleus {ECO:0000250|UniProtKB:Q9NPJ1}. Note=The majority of the protein resides within the pericentriolar material (PCM), a proteinaceous tube surrounding centrioles. During interphase, the protein is confined to the lateral surfaces of the PCM but during mitosis it relocalizes throughout the PCM and is found at the intercellular bridge. The MKSS protein is highly mobile and rapidly shuttles between the cytosol and centrosome. {ECO:0000250|UniProtKB:Q9NPJ1}. SUBUNIT: Component of a complex composed at least of MKKS, BBS10, BBS12, TCP1, CCT2, CCT3, CCT4, CCT5 AND CCT8. Interacts with STUB1. Interacts with BBS2 (via coiled coil domain). Interacts with CCDC28B. Interacts with BBS12. Interacts with SMARCC1, a component of the SWI/SNF complexes; the interaction takes place predominantly in the cytoplasm and may modulate SMARCC1 location. {ECO:0000250|UniProtKB:Q9NPJ1}. TISSUE SPECIFICITY: Widely expressed in adult and fetal tissues. Expressed in the developing heart, brain retina, limb buds, as well as in the developing neural tube. Expressed in the embryo in the first and second branchial arches. Expressed in parafin embedded tissue sections of brain, kidney, retina, olfactory epithelium and the ependymal layer of ventricles. Detected only in restricted regions of these tissue sections, including the ciliated border of renal tubules, the connecting cilium and the inner and outer nuclear layers of retina, and the ciliated layer of olfactory epithelia. {ECO:0000269|PubMed:15731008}. +Q91VE6 MK67I_MOUSE MKI67 FHA domain-interacting nucleolar phosphoprotein (Nucleolar protein interacting with the FHA domain of pKI-67) (mNIFK) 317 36,265 Alternative sequence (1); Chain (1); Cross-link (5); Domain (1); Initiator methionine (1); Modified residue (11); Sequence conflict (1) PTM: Phosphorylated. {ECO:0000250}.; PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}. SUBCELLULAR LOCATION: Nucleus, nucleolus. Chromosome {ECO:0000250}. Note=Localizes to mitotic chromosomes in conjunction with MKI67. {ECO:0000250}. SUBUNIT: Binds to the FHA domain of MKI67; this interaction is enhanced in mitosis. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain, heart, hind limb muscles, intestine, liver, skin and spleen. {ECO:0000269|PubMed:12798774}. +Q9WTU6 MK09_MOUSE Mitogen-activated protein kinase 9 (MAP kinase 9) (MAPK 9) (EC 2.7.11.24) (Stress-activated protein kinase JNK2) (c-Jun N-terminal kinase 2) 423 48,189 Active site (1); Alternative sequence (2); Binding site (1); Chain (1); Domain (1); Modified residue (2); Motif (1); Nucleotide binding (1); Sequence conflict (3) FUNCTION: Serine/threonine-protein kinase involved in various processes such as cell proliferation, differentiation, migration, transformation and programmed cell death. Extracellular stimuli such as proinflammatory cytokines or physical stress stimulate the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. In this cascade, two dual specificity kinases MAP2K4/MKK4 and MAP2K7/MKK7 phosphorylate and activate MAPK9/JNK2. In turn, MAPK9/JNK2 phosphorylates a number of transcription factors, primarily components of AP-1 such as JUN and ATF2 and thus regulates AP-1 transcriptional activity. In response to oxidative or ribotoxic stresses, inhibits rRNA synthesis by phosphorylating and inactivating the RNA polymerase 1-specific transcription initiation factor RRN3. Promotes stressed cell apoptosis by phosphorylating key regulatory factors including TP53 and YAP1. In T-cells, MAPK8 and MAPK9 are required for polarized differentiation of T-helper cells into Th1 cells. Upon T-cell receptor (TCR) stimulation, is activated by CARMA1, BCL10, MAP2K7 and MAP3K7/TAK1 to regulate JUN protein levels. Plays an important role in the osmotic stress-induced epithelial tight-junctions disruption. When activated, promotes beta-catenin/CTNNB1 degradation and inhibits the canonical Wnt signaling pathway. Participates also in neurite growth in spiral ganglion neurons. Phosphorylates the CLOCK-ARNTL/BMAL1 heterodimer and plays a role in the regulation of the circadian clock (PubMed:22441692). Phosphorylates POU5F1, which results in the inhibition of POU5F1's transcriptional activity and enhances its proteosomal degradation (PubMed:29153991). {ECO:0000269|PubMed:10811224, ECO:0000269|PubMed:11562351, ECO:0000269|PubMed:16973441, ECO:0000269|PubMed:21554942, ECO:0000269|PubMed:22441692, ECO:0000269|PubMed:29153991, ECO:0000269|PubMed:9806643}. PTM: Dually phosphorylated on Thr-183 and Tyr-185 by MAP2K7 and MAP2K4, which activates the enzyme. Autophosphorylated in vitro. {ECO:0000250|UniProtKB:P45984}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P45984}. Nucleus {ECO:0000269|PubMed:29153991}. Note=Colocalizes with POU5F1 in the nucleus. {ECO:0000269|PubMed:29153991}. SUBUNIT: Interacts with MECOM (By similarity). Binds to at least four scaffolding proteins, MAPK8IP1/JIP-1, MAPK8IP2/JIP-2, MAPK8IP3/JIP-3/JSAP1 and SPAG9/MAPK8IP4/JIP-4. These proteins also bind other components of the JNK signaling pathway (PubMed:11562351). Interacts with NFATC4 (By similarity). Interacts with ATF7; the interaction does not phosphorylate ATF7 but acts as a docking site for ATF7-associated partners such as JUN (By similarity). Interacts with BCL10 (By similarity). Interacts with CTNNB1 and GSK3B (By similarity). Interacts with DCLK2 (PubMed:16628014). Interacts with MAPKBP1 (By similarity). Interacts with POU5F1; phosphorylates POU5F1 at 'Ser-347' (PubMed:29153991). Found in a complex with SH3RF1, RAC2, MAP3K7/TAK1, MAP2K7/MKK7, MAPK8IP1/JIP1 and MAPK8/JNK1 (PubMed:27084103). {ECO:0000250|UniProtKB:P45984, ECO:0000250|UniProtKB:P49186, ECO:0000269|PubMed:11562351, ECO:0000269|PubMed:16628014, ECO:0000269|PubMed:27084103, ECO:0000269|PubMed:29153991}. DOMAIN: The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases. TISSUE SPECIFICITY: All four isoforms are widely distributed in brain. Isoforms alpha-1 and alpha-2 are predominantly expressed in hippocampus, cerebral cortex, caudate-putamen, amygdala and the granule layer of the cerebellum. Alpha-1 is more abundant than alpha-2 in the periaqueductal region and the substantia nigra. {ECO:0000269|PubMed:10674476}. +Q61884 MNS1_MOUSE Meiosis-specific nuclear structural protein 1 491 60,236 Chain (1); Coiled coil (2); Compositional bias (1); Modified residue (1) FUNCTION: May play a role in the control of meiotic division and germ cell differentiation through regulation of pairing and recombination during meiosis. {ECO:0000269|PubMed:8032679}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8032679}. TISSUE SPECIFICITY: Testis and pachytene spermatocytes. Expressed at the pachytene stage during spermatogenesis. {ECO:0000269|PubMed:8032679}. +Q8BHP2 NUTM1_MOUSE NUT family member 1 (Nuclear protein in testis) 1126 120,687 Chain (1); Compositional bias (1); Modified residue (5) PTM: Methylated at Gln-1042 by N6AMT1. {ECO:0000250|UniProtKB:Q86Y26}.; PTM: Phosphorylation on Ser-1022, Ser-1025 or Ser-1027 is important for cytoplasmic export. {ECO:0000250|UniProtKB:Q86Y26}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q86Y26}. Nucleus {ECO:0000250|UniProtKB:Q86Y26}. Note=Shuttles between nucleus and cytoplasm. {ECO:0000250|UniProtKB:Q86Y26}. +Q3V0C3 NUTM2_MOUSE NUT family member 2 733 80,589 Chain (1) +Q9DBY8 NVL_MOUSE Nuclear valosin-containing protein-like (NVLp) (Nuclear VCP-like protein) 855 94,476 Beta strand (1); Chain (1); Cross-link (1); Helix (3); Modified residue (7); Motif (3); Nucleotide binding (2); Region (2); Sequence conflict (1); Turn (1) FUNCTION: Participates in the assembly of the telomerase holoenzyme and effecting of telomerase activity via its interaction with TERT. Involved in both early and late stages of the pre-rRNA processing pathways. Spatiotemporally regulates 60S ribosomal subunit biogenesis in the nucleolus. Catalyzes the release of specific assembly factors, such as WDR74, from pre-60S ribosomal particles through the ATPase activity. {ECO:0000250|UniProtKB:O15381}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:21474449}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:O15381}. Note=Associates with pre-ribosomal particles in the nucleus. {ECO:0000250|UniProtKB:O15381}. SUBUNIT: Interacts with NCL/nucleolin (PubMed:21474449). Interacts with TERT. Interacts MTREX in an ATP-dependent manner. Interacts with RPL5 in an ATP-dependent manner. Interacts with WDR74 (through WDR repeats); the interaction is independent of RNA or pre-60S ribosome particles (By similarity). {ECO:0000250|UniProtKB:O15381, ECO:0000269|PubMed:21474449}. +A6H603 NWD1_MOUSE NACHT domain- and WD repeat-containing protein 1 1563 173,270 Alternative sequence (5); Chain (1); Domain (1); Erroneous initiation (1); Frameshift (1); Nucleotide binding (1); Repeat (13); Sequence conflict (5) FUNCTION: May play a role in the control of androgen receptor (AR) protein steady-state levels. {ECO:0000250|UniProtKB:Q149M9}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q149M9}. SUBUNIT: May interact with HSP90AA1, HSP90AB1 and BAG2. {ECO:0000250|UniProtKB:Q149M9}. +Q6P5U7 NWD2_MOUSE NACHT and WD repeat domain-containing protein 2 (Leucine-rich repeat and WD repeat-containing protein KIAA1239) 1742 197,414 Chain (1); Domain (1); Erroneous initiation (1); Repeat (16); Sequence conflict (1) +Q9WVS4 MOK_MOUSE MAPK/MAK/MRK overlapping kinase (EC 2.7.11.22) (MOK protein kinase) (Serine/threonine kinase 30) 420 48,065 Active site (1); Alternative sequence (4); Binding site (1); Chain (1); Domain (1); Mutagenesis (2); Nucleotide binding (1) FUNCTION: Able to phosphorylate several exogenous substrates and to undergo autophosphorylation (PubMed:10421840). Negatively regulates cilium length in a cAMP and mTORC1 signaling-dependent manner (PubMed:25243405). {ECO:0000269|PubMed:10421840, ECO:0000269|PubMed:25243405}. PTM: Autophosphorylated. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10421840}. Cell projection, cilium {ECO:0000269|PubMed:25243405}. Nucleus {ECO:0000269|PubMed:25243405}. TISSUE SPECIFICITY: Highly expressed in testis, and less in kidney, brain and lung. +Q8C5T4 MORN3_MOUSE MORN repeat-containing protein 3 241 27,881 Alternative sequence (2); Chain (1); Repeat (7); Sequence conflict (2) +P83503 NYX_MOUSE Nyctalopin 476 52,431 Chain (1); Domain (2); Glycosylation (7); Repeat (11); Signal peptide (1) SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. TISSUE SPECIFICITY: Expressed abundantly in retina with lower levels in brain, lung, spleen and testis. Not detected in kidney, heart or liver. In the retina, highest expression found in the inner nuclear layer and ganglion cell layer. {ECO:0000269|PubMed:12506099, ECO:0000269|PubMed:12714669}. DISEASE: Note=Defects in Nyx are the cause of the nob (no b-wave) phenotype which is characterized by a decreased sensitivity to light and an absence of the rod b-wave in electroretinograms. An 85-bp deletion in exon 3 results in the loss of 288 residues from the C-terminus of the protein. {ECO:0000269|PubMed:12506099}. +P63030 MPC1_MOUSE Mitochondrial pyruvate carrier 1 (Brain protein 44-like protein) 109 12,455 Chain (1); Initiator methionine (1); Modified residue (2); Sequence conflict (1); Transmembrane (2) TRANSMEM 21 41 Helical. {ECO:0000255}.; TRANSMEM 53 71 Helical. {ECO:0000255}. FUNCTION: Mediates the uptake of pyruvate into mitochondria. {ECO:0000269|PubMed:22628554}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:22628554}; Multi-pass membrane protein {ECO:0000269|PubMed:22628554}. SUBUNIT: The functional 150 kDa pyruvate import complex is a heteromer of MPC1 and MPC2. {ECO:0000269|PubMed:22628554}. +Q8VFL9 O1086_MOUSE Olfactory receptor 1086 (Olfactory receptor 179-2) 310 34,661 Chain (1); Disulfide bond (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 24 44 Helical; Name=1. {ECO:0000255}.; TRANSMEM 53 73 Helical; Name=2. {ECO:0000255}.; TRANSMEM 98 118 Helical; Name=3. {ECO:0000255}.; TRANSMEM 132 152 Helical; Name=4. {ECO:0000255}.; TRANSMEM 195 215 Helical; Name=5. {ECO:0000255}.; TRANSMEM 236 256 Helical; Name=6. {ECO:0000255}.; TRANSMEM 270 290 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 23 Extracellular. {ECO:0000255}.; TOPO_DOM 45 52 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 74 97 Extracellular. {ECO:0000255}.; TOPO_DOM 119 131 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 153 194 Extracellular. {ECO:0000255}.; TOPO_DOM 216 235 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 257 269 Extracellular. {ECO:0000255}.; TOPO_DOM 291 310 Cytoplasmic. {ECO:0000255}. FUNCTION: Potential odorant receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q99MS3 MP17L_MOUSE Mpv17-like protein (M-LP) 194 22,180 Alternative sequence (3); Chain (1); Region (1); Topological domain (5); Transmembrane (4) TRANSMEM 15 34 Helical. {ECO:0000255}.; TRANSMEM 51 67 Helical. {ECO:0000255}.; TRANSMEM 92 110 Helical. {ECO:0000255}.; TRANSMEM 151 168 Helical. {ECO:0000255}. TOPO_DOM 1 14 Cytoplasmic. {ECO:0000269|PubMed:15541722}.; TOPO_DOM 35 50 Lumenal. {ECO:0000269|PubMed:15541722}.; TOPO_DOM 68 91 Cytoplasmic. {ECO:0000269|PubMed:15541722}.; TOPO_DOM 111 150 Lumenal. {ECO:0000269|PubMed:15541722}.; TOPO_DOM 169 194 Cytoplasmic. {ECO:0000269|PubMed:15541722}. FUNCTION: Isoform 1 and isoform 3 participate in reactive oxygen species metablism by up- or down-regulation of the genes of antioxidant enzymes. {ECO:0000269|PubMed:12471025, ECO:0000269|PubMed:15541722}. SUBCELLULAR LOCATION: Isoform 1: Peroxisome membrane {ECO:0000269|PubMed:12471025}; Multi-pass membrane protein.; SUBCELLULAR LOCATION: Isoform 3: Cytoplasm {ECO:0000269|PubMed:15541722}. TISSUE SPECIFICITY: Isoform 1 and isoform 3 are expressed in the kidney (at protein level). Isoform 1 is expressed in the kidney, spleen, heart, brain, lung and liver. Isoform 3 is expressed in the kidney. Isoform 1 and isoform 3 expression increase during development, reache their highest level in adulthood and decrease with aging. {ECO:0000269|PubMed:11327696, ECO:0000269|PubMed:12471025, ECO:0000269|PubMed:15541722}. +O09110 MP2K3_MOUSE Dual specificity mitogen-activated protein kinase kinase 3 (MAP kinase kinase 3) (MAPKK 3) (EC 2.7.12.2) (MAPK/ERK kinase 3) (MEK 3) 347 39,296 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Domain (1); Modified residue (4); Nucleotide binding (1); Sequence conflict (5) FUNCTION: Dual specificity kinase. Is activated by cytokines and environmental stress in vivo. Catalyzes the concomitant phosphorylation of a threonine and a tyrosine residue in the MAP kinase p38. Part of a signaling cascade that begins with the activation of the adrenergic receptor ADRA1B and leads to the activation of MAPK14. {ECO:0000250|UniProtKB:P46734}. PTM: Autophosphorylated. Phosphorylation on Ser-218 and Thr-222 by MAP kinase kinase kinases regulates positively the kinase activity. Phosphorylated by TAOK2. {ECO:0000250|UniProtKB:P46734}. SUBUNIT: Component of a signaling complex containing at least AKAP13, PKN1, MAPK14, ZAK and MAP2K3. Within this complex, AKAP13 interacts directly with PKN1, which in turn recruits MAPK14, MAP2K3 and ZAK. Binds to DYRK1B/MIRK and increases its kinase activity (By similarity). Part of a complex with MAP3K3, RAC1 and CCM2 (PubMed:14634666). Interacts with ARRB1 (By similarity). {ECO:0000250|UniProtKB:P46734, ECO:0000269|PubMed:14634666}. +Q9WV34 MPP2_MOUSE MAGUK p55 subfamily member 2 (Discs large homolog 2) (Protein MPP2) 552 61,555 Alternative sequence (1); Chain (1); Domain (5); Modified residue (3); Sequence conflict (1) FUNCTION: Postsynaptic MAGUK scaffold protein that links CADM1 cell adhesion molecules to core components of the postsynaptic density (By similarity). In CA1 pyramidal neurons, required for synaptic KCNN2-containing channel function and long-term potentiation expression (PubMed:26880549). Seems to negatively regulate SRC function in epithelial cells (By similarity). {ECO:0000250|UniProtKB:D3ZAA9, ECO:0000250|UniProtKB:Q14168, ECO:0000269|PubMed:26880549}. PTM: Phosphorylated by SRC. {ECO:0000250|UniProtKB:Q14168}. SUBCELLULAR LOCATION: Cell projection, dendrite {ECO:0000269|PubMed:26880549}. Cell projection, dendritic spine membrane {ECO:0000269|PubMed:26880549}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250|UniProtKB:D3ZAA9}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q14168}. Membrane {ECO:0000250|UniProtKB:Q14168}. Note=Prominently expressed in the post-synaptic densities of dendritic spines, is also detected in dendritic shafts. {ECO:0000269|PubMed:26880549}. SUBUNIT: Can homomultimerise. Interacts with CACNG2. Interacts (via the SH3-Guanylate kinase-like sub-module) with DLG4/PSD95 and DLGAP1/GKAP. Interacts (via the PDZ domain) with CADM1 (via C-terminus) (By similarity). Interacts with KCNN2/SK2 (via N-terminal domain) (PubMed:26880549). Interacts with SRC (By similarity). {ECO:0000250|UniProtKB:D3ZAA9, ECO:0000250|UniProtKB:Q14168, ECO:0000269|PubMed:26880549}. TISSUE SPECIFICITY: Expressed in pyramidal neurons of CA1 region of the hippocampus. {ECO:0000269|PubMed:26880549}. +Q9JLB0 MPP6_MOUSE MAGUK p55 subfamily member 6 (Dlgh4 protein) (P55T protein) (Protein associated with Lin-7 2) 553 62,631 Alternative sequence (1); Chain (1); Domain (5); Modified residue (1); Sequence conflict (1) SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein. SUBUNIT: Interacts with CADM1. Interacts with the LIN7 proteins. {ECO:0000269|PubMed:12826663}. +A6H5Y1 MPP9_MOUSE M-phase phosphoprotein 9 991 109,953 Chain (1); Coiled coil (2); Erroneous initiation (1); Modified residue (1) PTM: Phosphorylated in M (mitotic) phase. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Localizes to the distal and proximal end of centriole pairs in duplicated centrosomes. In ciliated cells, localizes to the distal and proximal end of daughter centriole and proximal of the mother centriole but not in the distal end of the mother centriole (By similarity). {ECO:0000250}. +Q8VFV4 O1440_MOUSE Olfactory receptor 1440 (Olfactory receptor 202-4) 315 34,943 Chain (1); Disulfide bond (1); Topological domain (9); Transmembrane (8) TRANSMEM 30 50 Helical; Name=1. {ECO:0000255}.; TRANSMEM 55 75 Helical; Name=2. {ECO:0000255}.; TRANSMEM 100 120 Helical; Name=3. {ECO:0000255}.; TRANSMEM 124 143 Helical; Name=4. {ECO:0000255}.; TRANSMEM 145 165 Helical; Name=5. {ECO:0000255}.; TRANSMEM 203 223 Helical; Name=6. {ECO:0000255}.; TRANSMEM 241 261 Helical; Name=7. {ECO:0000255}.; TRANSMEM 273 293 Helical; Name=8. {ECO:0000255}. TOPO_DOM 1 29 Extracellular. {ECO:0000255}.; TOPO_DOM 51 54 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 76 99 Extracellular. {ECO:0000255}.; TOPO_DOM 121 123 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 144 144 Extracellular. {ECO:0000255}.; TOPO_DOM 166 202 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 224 240 Extracellular. {ECO:0000255}.; TOPO_DOM 262 272 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 294 315 Extracellular. {ECO:0000255}. FUNCTION: Odorant receptor involved in the detection of muscone. {ECO:0000269|PubMed:24361078}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Localized in the dorsomedial and ventral region of the olfactory bulb. {ECO:0000269|PubMed:24361078}. +Q7TQQ0 O1509_MOUSE Olfactory receptor 1509 (Odorant receptor 244-3) (Odorant receptor 83) 308 34,986 Chain (1); Disulfide bond (1); Glycosylation (1); Metal binding (3); Mutagenesis (35); Sequence conflict (4); Topological domain (8); Transmembrane (7) TRANSMEM 25 45 Helical; Name=1. {ECO:0000255}.; TRANSMEM 58 78 Helical; Name=2. {ECO:0000255}.; TRANSMEM 98 118 Helical; Name=3. {ECO:0000255}.; TRANSMEM 144 164 Helical; Name=4. {ECO:0000255}.; TRANSMEM 205 225 Helical; Name=5. {ECO:0000255}.; TRANSMEM 237 257 Helical; Name=6. {ECO:0000255}.; TRANSMEM 269 289 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 24 Extracellular. {ECO:0000305}.; TOPO_DOM 46 57 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 79 97 Extracellular. {ECO:0000305}.; TOPO_DOM 119 143 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 165 204 Extracellular. {ECO:0000305}.; TOPO_DOM 226 236 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 258 268 Extracellular. {ECO:0000305}.; TOPO_DOM 290 308 Cytoplasmic. {ECO:0000305}. FUNCTION: Olfactory receptor that is activated by the binding of organosulfur odorants with thioether groups such as (methylthio)methanethiol (MTMT) and bis(methylthiomethyl) disulfide (PubMed:22328155, PubMed:25185561, PubMed:25901328, PubMed:29659735). Also binds odorants cis-cyclooctene and tert-butyl mercaptan (PubMed:27019154). The activity of this receptor is mediated by G proteins which activate adenylyl cyclase (Potential). {ECO:0000269|PubMed:22328155, ECO:0000269|PubMed:25185561, ECO:0000269|PubMed:25901328, ECO:0000269|PubMed:27019154, ECO:0000269|PubMed:29659735, ECO:0000305}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|RuleBase:RU363047, ECO:0000255|SAAS:SAAS00857205, ECO:0000269|PubMed:22328155, ECO:0000269|PubMed:27019154, ECO:0000269|PubMed:29659735, ECO:0000305|PubMed:25185561, ECO:0000305|PubMed:25901328}; Multi-pass membrane protein {ECO:0000255|RuleBase:RU363047, ECO:0000255|SAAS:SAAS00857205, ECO:0000269|PubMed:27019154}. TISSUE SPECIFICITY: Expressed in olfactory epithelium, specifically in the olfactory sensory neurons of the septal organ. {ECO:0000269|PubMed:10493742, ECO:0000269|PubMed:18214836, ECO:0000269|PubMed:22328155}. +Q61216 MRE11_MOUSE Double-strand break repair protein MRE11 (EC 3.1.-.-) (Double-strand break repair protein MRE11A) (MmMRE11A) (Meiotic recombination 11 homolog 1) (MRE11 homolog 1) (Meiotic recombination 11 homolog A) (MRE11 homolog A) 706 80,223 Active site (1); Alternative sequence (1); Chain (1); Cross-link (1); Initiator methionine (1); Modified residue (9) FUNCTION: Component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis. The complex possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by MRE11. RAD50 may be required to bind DNA ends and hold them in close proximity. This could facilitate searches for short or long regions of sequence homology in the recombining DNA templates, and may also stimulate the activity of DNA ligases and/or restrict the nuclease activity of MRE11 to prevent nucleolytic degradation past a given point. The complex may also be required for DNA damage signaling via activation of the ATM kinase. In telomeres the MRN complex may modulate t-loop formation. {ECO:0000250|UniProtKB:P49959}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P49959}. Chromosome, telomere {ECO:0000250|UniProtKB:P49959}. Chromosome {ECO:0000250|UniProtKB:P49959}. Note=Localizes to discrete nuclear foci after treatment with genotoxic agents. {ECO:0000250|UniProtKB:P49959}. SUBUNIT: Component of the MRN complex composed of two heterodimers RAD50/MRE11 associated with a single NBN. As part of the MRN complex, interacts with MCM9; the interaction recruits the complex to DNA repair sites. Component of the BASC complex, at least composed of BRCA1, MSH2, MSH6, MLH1, ATM, BLM, RAD50, MRE11 and NBN. Found in a complex with TERF2. Interacts with DCLRE1C/Artemis and DCLRE1B/Apollo. Interacts with ATF2. Interacts with EXD2. Interacts with MRNIP. Interacts with SAMHD1; leading to stimulate 3'-5' exonuclease activity. {ECO:0000250|UniProtKB:P49959}. +Q91ZC6 MRGA6_MOUSE Mas-related G-protein coupled receptor member A6 301 34,538 Chain (1); Sequence conflict (12); Topological domain (8); Transmembrane (7) TRANSMEM 16 36 Helical; Name=1. {ECO:0000255}.; TRANSMEM 43 63 Helical; Name=2. {ECO:0000255}.; TRANSMEM 78 98 Helical; Name=3. {ECO:0000255}.; TRANSMEM 129 149 Helical; Name=4. {ECO:0000255}.; TRANSMEM 164 184 Helical; Name=5. {ECO:0000255}.; TRANSMEM 204 224 Helical; Name=6. {ECO:0000255}.; TRANSMEM 241 261 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 15 Extracellular. {ECO:0000255}.; TOPO_DOM 37 42 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 64 77 Extracellular. {ECO:0000255}.; TOPO_DOM 99 128 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 150 163 Extracellular. {ECO:0000255}.; TOPO_DOM 185 203 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 225 240 Extracellular. {ECO:0000255}.; TOPO_DOM 262 301 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan receptor. May be a receptor for RFamide-family neuropeptides such as NPFF and NPAF, which are analgesic in vivo. May regulate nociceptor function and/or development, including the sensation or modulation of pain (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed in a subset of sensory neurons that includes nociceptors. Expressed in the subclass of non-peptidergic sensory neurons that are IB4(+) and VR1(-). {ECO:0000269|PubMed:11551509}. +Q3UG61 MRGB1_MOUSE Mas-related G-protein coupled receptor member B1 350 40,161 Chain (1); Compositional bias (1); Glycosylation (2); Sequence conflict (8); Topological domain (8); Transmembrane (7) TRANSMEM 47 67 Helical; Name=1. {ECO:0000255}.; TRANSMEM 88 108 Helical; Name=2. {ECO:0000255}.; TRANSMEM 116 136 Helical; Name=3. {ECO:0000255}.; TRANSMEM 156 176 Helical; Name=4. {ECO:0000255}.; TRANSMEM 201 221 Helical; Name=5. {ECO:0000255}.; TRANSMEM 236 256 Helical; Name=6. {ECO:0000255}.; TRANSMEM 276 296 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 46 Extracellular. {ECO:0000255}.; TOPO_DOM 68 87 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 109 115 Extracellular. {ECO:0000255}.; TOPO_DOM 137 155 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 177 200 Extracellular. {ECO:0000255}.; TOPO_DOM 222 235 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 257 275 Extracellular. {ECO:0000255}.; TOPO_DOM 297 350 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan receptor. Probably involved in the function of nociceptive neurons. May regulate nociceptor function and/or development, including the sensation or modulation of pain (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q3KNA1 MRGB2_MOUSE Mas-related G-protein coupled receptor member B2 338 38,832 Chain (1); Glycosylation (3); Sequence conflict (3); Topological domain (8); Transmembrane (7) TRANSMEM 41 61 Helical; Name=1. {ECO:0000255}.; TRANSMEM 90 110 Helical; Name=2. {ECO:0000255}.; TRANSMEM 112 132 Helical; Name=3. {ECO:0000255}.; TRANSMEM 158 178 Helical; Name=4. {ECO:0000255}.; TRANSMEM 192 212 Helical; Name=5. {ECO:0000255}.; TRANSMEM 232 252 Helical; Name=6. {ECO:0000255}.; TRANSMEM 269 289 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 40 Extracellular. {ECO:0000255}.; TOPO_DOM 62 89 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 111 111 Extracellular. {ECO:0000255}.; TOPO_DOM 133 157 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 179 191 Extracellular. {ECO:0000255}.; TOPO_DOM 213 231 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 253 268 Extracellular. {ECO:0000255}.; TOPO_DOM 290 338 Cytoplasmic. {ECO:0000255}. FUNCTION: Mast cell-specific receptor for basic secretagogues, i.e. cationic amphiphilic drugs, as well as endo- or exogenous peptides, consisting of a basic head group and a hydrophobic core. Recognizes and binds small molecules containing a cyclized tetrahydroisoquinoline (THIQ), such as non-steroidal neuromuscular blocking drugs (NMBDs), including tubocurarine and atracurium. In response to these compounds, mediates pseudo-allergic reactions characterized by histamine release, inflammation and airway contraction (PubMed:25517090). {ECO:0000269|PubMed:25517090}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Mast cell-specific. {ECO:0000269|PubMed:25517090}. +Q80UW5 MRCKG_MOUSE Serine/threonine-protein kinase MRCK gamma (EC 2.7.11.1) (CDC42-binding protein kinase gamma) (DMPK-like gamma) (Myotonic dystrophy kinase-related CDC42-binding kinase gamma) (MRCK gamma) (Myotonic dystrophy protein kinase-like gamma) (Myotonic dystrophy protein kinase-like alpha) 1551 172,147 Active site (1); Binding site (1); Chain (1); Coiled coil (2); Compositional bias (1); Domain (5); Modified residue (4); Nucleotide binding (1); Sequence conflict (1); Zinc finger (1) FUNCTION: May act as a downstream effector of CDC42 in cytoskeletal reorganization. Contributes to the actomyosin contractility required for cell invasion, through the regulation of MYPT1 and thus MLC2 phosphorylation (By similarity). {ECO:0000250|UniProtKB:Q5VT25}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Concentrates at the leading edge of cells. {ECO:0000250}. SUBUNIT: Homodimer and homotetramer via the coiled coil regions. Interacts tightly with GTP-bound but not GDP-bound CDC42 (By similarity). {ECO:0000250}. +Q8VI47 MRP2_MOUSE Canalicular multispecific organic anion transporter 1 (ATP-binding cassette sub-family C member 2) 1543 173,671 Chain (1); Domain (4); Glycosylation (4); Modified residue (6); Nucleotide binding (2); Sequence conflict (1); Topological domain (18); Transmembrane (17) TRANSMEM 27 47 Helical; Name=1. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 68 88 Helical; Name=2. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 93 113 Helical; Name=3. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 126 146 Helical; Name=4. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 165 185 Helical; Name=5. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 312 332 Helical; Name=6. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 359 379 Helical; Name=7. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 436 456 Helical; Name=8. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 460 480 Helical; Name=9. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 543 563 Helical; Name=10. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 586 606 Helical; Name=11. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 970 990 Helical; Name=12. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 1032 1052 Helical; Name=13. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 1096 1116 Helical; Name=14. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 1118 1138 Helical; Name=15. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 1210 1230 Helical; Name=16. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 1233 1253 Helical; Name=17. {ECO:0000255|PROSITE-ProRule:PRU00441}. TOPO_DOM 1 26 Extracellular. {ECO:0000250}.; TOPO_DOM 48 67 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 89 92 Extracellular. {ECO:0000250}.; TOPO_DOM 114 125 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 147 164 Extracellular. {ECO:0000250}.; TOPO_DOM 186 311 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 333 358 Extracellular. {ECO:0000250}.; TOPO_DOM 380 435 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 457 459 Extracellular. {ECO:0000250}.; TOPO_DOM 481 542 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 564 585 Extracellular. {ECO:0000250}.; TOPO_DOM 607 969 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 991 1031 Extracellular. {ECO:0000250}.; TOPO_DOM 1053 1095 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 1117 1117 Extracellular. {ECO:0000250}.; TOPO_DOM 1139 1209 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 1231 1232 Extracellular. {ECO:0000250}.; TOPO_DOM 1254 1543 Cytoplasmic. {ECO:0000250}. FUNCTION: Mediates hepatobiliary excretion of numerous organic anions. May function as a cellular cisplatin transporter (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. +O08608 OAZ2_MOUSE Ornithine decarboxylase antizyme 2 (AZ2) (ODC-Az 2) (Seizure-related protein 15) 189 21,025 Chain (1); Modified residue (1) FUNCTION: Ornithine decarboxylase (ODC) antizyme protein that negatively regulates ODC activity and intracellular polyamine biosynthesis and uptake in response to increased intracellular polyamine levels. Binds to ODC monomers, inhibiting the assembly of the functional ODC homodimers. Does not target the ODC monomers for degradation, which allows a protein synthesis-independent restoration of ODC activity (PubMed:16916800, PubMed:18508777, PubMed:24967154). Involved in the translocation of AZIN2 from ER-Golgi intermediate compartment (ERGIC) to the cytosol (PubMed:19449338). {ECO:0000269|PubMed:16916800, ECO:0000269|PubMed:18508777, ECO:0000269|PubMed:19449338, ECO:0000269|PubMed:24967154}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19725046}. SUBUNIT: Interacts with ODC1 and thereby sterically blocks ODC homodimerization (By similarity). Interacts with AZIN2; this interaction disrupts the interaction between the antizyme and ODC1 (PubMed:16916800). {ECO:0000250|UniProtKB:P54368, ECO:0000269|PubMed:16916800}. +Q9R109 OAZ3_MOUSE Ornithine decarboxylase antizyme 3 (AZ3) (ODC-Az 3) (OAZ-t) 243 28,228 Chain (1); Erroneous initiation (2); Frameshift (1); Modified residue (3); Sequence caution (2) FUNCTION: Ornithine decarboxylase (ODC) antizyme protein that negatively regulates ODC activity and intracellular polyamine biosynthesis and uptake in response to increased intracellular polyamine levels. Binds to ODC monomers, inhibiting the assembly of the functional ODC homodimers. Does not target the ODC monomers for degradation, which allows a protein synthesis-independent restoration of ODC activity (PubMed:16916800, PubMed:18508777, PubMed:18973822). Stabilizes AZIN2 by interfering with its ubiquitination (PubMed:18062773). Involved in the translocation of AZNI2 from ER-Golgi intermediate compartment (ERGIC) to the cytosol (PubMed:19449338). Probably plays a key role in spermatogenesis by regulating the intracellular concentration of polyamines in haploid germ cells (PubMed:24967154). {ECO:0000269|PubMed:16916800, ECO:0000269|PubMed:18062773, ECO:0000269|PubMed:18508777, ECO:0000269|PubMed:18973822, ECO:0000269|PubMed:19449338, ECO:0000269|PubMed:24967154}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15642376}. Cytoplasm {ECO:0000269|PubMed:15642376}. SUBUNIT: Interacts with ODC1 and thereby sterically blocks ODC homodimerization (By similarity). Interacts with AZIN2; this interaction disrupts the interaction between the antizyme and ODC1 (PubMed:16916800, PubMed:18062773, PubMed:18973822). Interacts with GGN (PubMed:15642376). {ECO:0000250|UniProtKB:P54368, ECO:0000269|PubMed:15642376, ECO:0000269|PubMed:16916800, ECO:0000269|PubMed:18062773, ECO:0000269|PubMed:18973822}. TISSUE SPECIFICITY: Testis specific. Expressed throughout the differentiation process from spermatids to spermatozoa in the inner part of the seminiferous tubules. {ECO:0000269|PubMed:18973822}. +Q8R4P9 MRP7_MOUSE Multidrug resistance-associated protein 7 (ATP-binding cassette sub-family C member 10) 1501 163,735 Alternative sequence (3); Chain (1); Domain (4); Modified residue (2); Nucleotide binding (2); Transmembrane (17) TRANSMEM 32 52 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 70 90 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 102 122 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 133 153 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 172 192 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 294 314 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 321 341 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 392 412 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 415 435 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 508 528 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 539 559 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 877 897 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 969 989 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 1033 1053 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 1056 1076 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 1158 1178 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 1187 1207 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}. FUNCTION: ATP-dependent transporter probably involved in cellular detoxification through lipophilic anion extrusion. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. TISSUE SPECIFICITY: Expressed in all tissues tested including liver, brain, heart, skeletal muscle, kidney and spleen. {ECO:0000269|PubMed:11943485}. +Q9CZJ6 MS18A_MOUSE Protein Mis18-alpha 204 22,949 Chain (1); Cross-link (1); Domain (1); Metal binding (4); Modified residue (4) FUNCTION: Required for recruitment of CENPA to centromeres and normal chromosome segregation during mitosis. {ECO:0000250|UniProtKB:Q9NYP9}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NYP9}. Chromosome {ECO:0000250|UniProtKB:Q9NYP9}. Chromosome, centromere {ECO:0000250|UniProtKB:Q9NYP9}. Note=Associated with centromeres in interphase cells, from late anaphase to the G1 phase. Not detected on centromeres during earlier phases of mitosis. Associated with chromatin. {ECO:0000250|UniProtKB:Q9NYP9}. SUBUNIT: Homodimer, and heterodimer with OIP5/MIS18B. Identified in a complex containing MIS18A, OIP5/MIS18B, MIS18BP1, RBBP7 and RBBP4. {ECO:0000250|UniProtKB:Q9NYP9}. +A2AQ14 MS18B_MOUSE Protein Mis18-beta (Opa-interacting protein 5 homolog) 241 26,861 Chain (1); Domain (1); Erroneous initiation (1); Metal binding (4); Modified residue (2); Sequence conflict (5) FUNCTION: Required for recruitment of CENPA to centromeres and normal chromosome segregation during mitosis. {ECO:0000250|UniProtKB:O43482}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O43482}. Chromosome {ECO:0000250|UniProtKB:O43482}. Chromosome, centromere {ECO:0000250|UniProtKB:O43482}. Note=Associated with centromeres in interphase cells, from late anaphase to the G1 phase. Not detected on centromeres during earlier phases of mitosis. Associated with chromatin. {ECO:0000250|UniProtKB:O43482}. SUBUNIT: Homodimer, and heterodimer with MIS18A. Identified in a complex containing MIS18A, OIP5/MIS18B, MIS18BP1, RBBP7 and RBBP4. {ECO:0000250|UniProtKB:O43482}. +Q8JZY4 MRPP3_MOUSE Mitochondrial ribonuclease P catalytic subunit (EC 3.1.26.5) (Mitochondrial ribonuclease P protein 3) (Mitochondrial RNase P protein 3) 584 66,857 Chain (1); Domain (1); Erroneous initiation (1); Metal binding (8); Sequence caution (1); Sequence conflict (1); Transit peptide (1) FUNCTION: Catalytic ribonuclease component of mitochondrial ribonuclease P, a complex composed of TRMT10C/MRPP1, HSD17B10/MRPP2 and MRPP3, which cleaves tRNA molecules in their 5'-ends. The presence of TRMT10C/MRPP1, HSD17B10/MRPP2 is required to catalyze tRNA molecules in their 5'-ends. {ECO:0000250|UniProtKB:O15091}. PTM: Degraded by LONP1 following mitochondrial unfolded protein response, probably leading to inhibit translation in mitochondrion. {ECO:0000250|UniProtKB:O15091}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:O15091}. SUBUNIT: Catalytic component of mitochondrial ribonuclease P, a complex composed of TRMT10C/MRPP1, HSD17B10/MRPP2 and MRPP31. {ECO:0000250|UniProtKB:O15091}. DOMAIN: Displays a distorted and non-productive active site that probably switches to a fully productive state only upon association with TRMT10C/MRPP1, HSD17B10/MRPP2 and pre-tRNA substrate. {ECO:0000250|UniProtKB:O15091}. +Q64693 OBF1_MOUSE POU domain class 2-associating factor 1 (B-cell-specific coactivator OBF-1) (BOB-1) (BOB1) (OCA-B) (OCT-binding factor 1) 256 27,692 Chain (1); Sequence conflict (2) FUNCTION: Transcriptional coactivator that specifically associates with either OCT1 or OCT2. It boosts the OCT1 mediated promoter activity and to a lesser extent, that of OCT2. It has no intrinsic DNA-binding activity. It recognizes the POU domains of OCT1 and OCT2. It is essential for the response of B-cells to antigens and required for the formation of germinal centers. PTM: Ubiquitinated; mediated by SIAH1 or SIAH2 and leading to its subsequent proteasomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. TISSUE SPECIFICITY: B-cell specific. +Q8BIL2 MSD1_MOUSE Myb/SANT-like DNA-binding domain-containing protein 1 278 32,153 Chain (1); Domain (1) +Q9JK54 MSGN1_MOUSE Mesogenin-1 (Paraxial mesoderm-specific mesogenin1) (pMesogenin1) (pMsgn1) 188 20,553 Chain (1); Domain (1) FUNCTION: Involved in specifying the paraxial, but not dorsal, mesoderm. May regulate the expression of T-box transcription factors required for mesoderm formation and differentiation. {ECO:0000269|PubMed:10837126, ECO:0000269|PubMed:11124811}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}. +P43247 MSH2_MOUSE DNA mismatch repair protein Msh2 (MutS protein homolog 2) 935 104,151 Chain (1); Initiator methionine (1); Modified residue (3); Nucleotide binding (1); Region (1); Sequence conflict (1) FUNCTION: Component of the post-replicative DNA mismatch repair system (MMR). Forms two different heterodimers: MutS alpha (MSH2-MSH6 heterodimer) and MutS beta (MSH2-MSH3 heterodimer) which binds to DNA mismatches thereby initiating DNA repair. When bound, heterodimers bend the DNA helix and shields approximately 20 base pairs. MutS alpha recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. MutS beta recognizes larger insertion-deletion loops up to 13 nucleotides long. After mismatch binding, MutS alpha or beta forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. Recruits DNA helicase MCM9 to chromatin which unwinds the mismatch containg DNA strand. ATP binding and hydrolysis play a pivotal role in mismatch repair functions. The ATPase activity associated with MutS alpha regulates binding similar to a molecular switch: mismatched DNA provokes ADP-->ATP exchange, resulting in a discernible conformational transition that converts MutS alpha into a sliding clamp capable of hydrolysis-independent diffusion along the DNA backbone. This transition is crucial for mismatch repair. MutS alpha may also play a role in DNA homologous recombination repair. In melanocytes may modulate both UV-B-induced cell cycle regulation and apoptosis. {ECO:0000250|UniProtKB:P43246}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P43246}. Chromosome {ECO:0000250|UniProtKB:P43246}. SUBUNIT: Component of the DNA mismatch repair (MMR) complex composed at least of MSH2, MSH3, MSH6, PMS1 and MLH1. Heterodimer consisting of MSH2-MSH6 (MutS alpha) or MSH2-MSH3 (MutS beta). Both heterodimers form a ternary complex with MutL alpha (MLH1-PMS1). Interacts with MCM9; the interaction recruits MCM9 to chromatin. Interacts with MCM8. Interacts with EXO1. Part of the BRCA1-associated genome surveillance complex (BASC), which contains BRCA1, MSH2, MSH6, MLH1, ATM, BLM, PMS2 and the RAD50-MRE11-NBS1 protein complex. This association could be a dynamic process changing throughout the cell cycle and within subnuclear domains. Interacts with ATR. Interacts with SLX4/BTBD12; this interaction is direct and links MutS beta to SLX4, a subunit of different structure-specific endonucleases. Interacts with SMARCAD1. {ECO:0000250|UniProtKB:P43246}. +Q78J03 MSRB2_MOUSE Methionine-R-sulfoxide reductase B2, mitochondrial (MsrB2) (EC 1.8.4.12) (EC 1.8.4.14) 175 19,157 Active site (1); Beta strand (8); Chain (1); Domain (1); Helix (6); Metal binding (4); Transit peptide (1); Turn (1) FUNCTION: Methionine-sulfoxide reductase that specifically reduces methionine (R)-sulfoxide back to methionine. While in many cases, methionine oxidation is the result of random oxidation following oxidative stress, methionine oxidation is also a post-translational modification that takes place on specific residue. Upon oxidative stress, may play a role in the preservation of mitochondrial integrity by decreasing the intracellular reactive oxygen species build-up through its scavenging role, hence contributing to cell survival and protein maintenance. {ECO:0000269|PubMed:14699060, ECO:0000269|PubMed:23911929}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14699060}. +P30204 MSRE_MOUSE Macrophage scavenger receptor types I and II (Macrophage acetylated LDL receptor I and II) (Scavenger receptor type A) (SR-A) (CD antigen CD204) 458 50,170 Alternative sequence (2); Chain (1); Coiled coil (1); Disulfide bond (3); Domain (2); Erroneous initiation (2); Glycosylation (6); Modified residue (2); Region (1); Sequence conflict (48); Topological domain (2); Transmembrane (1) TRANSMEM 56 78 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 55 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 79 458 Extracellular. {ECO:0000255}. FUNCTION: Membrane glycoproteins implicated in the pathologic deposition of cholesterol in arterial walls during atherogenesis. Two types of receptor subunits exist. These receptors mediate the endocytosis of a diverse group of macromolecules, including modified low density lipoproteins (LDL). {ECO:0000250|UniProtKB:P21757}. SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. SUBUNIT: Homotrimer (PubMed:8394868). Interacts with MYO18A (By similarity). {ECO:0000250|UniProtKB:P21757, ECO:0000269|PubMed:8394868}. +Q91X96 MSS4_MOUSE Guanine nucleotide exchange factor MSS4 (Rab-interacting factor) 123 13,915 Chain (1); Domain (1); Metal binding (4); Modified residue (1) FUNCTION: Guanine-nucleotide-releasing protein that acts on members of the SEC4/YPT1/RAB subfamily. Stimulates GDP release from both YPT1 and RAB3A, but is less active on these proteins than on the SEC4 protein. Might play a general role in vesicular transport (By similarity). {ECO:0000250}. SUBUNIT: Interacts with RAB8A. {ECO:0000250}. +O89013 OBRG_MOUSE Leptin receptor gene-related protein (Endospanin-1) (OB-R gene-related protein) (OB-RGRP) 131 14,316 Alternative sequence (1); Chain (1); Sequence conflict (3); Transmembrane (4) TRANSMEM 7 27 Helical. {ECO:0000255}.; TRANSMEM 32 52 Helical. {ECO:0000255}.; TRANSMEM 69 89 Helical. {ECO:0000255}.; TRANSMEM 100 120 Helical. {ECO:0000255}. FUNCTION: Negatively regulates leptin receptor (LEPR) cell surface expression, and thus decreases response to leptin. Negatively regulates growth hormone (GH) receptor cell surface expression in liver. May play a role in liver resistance to GH during periods of reduced nutrient availability. {ECO:0000269|PubMed:18042720, ECO:0000269|PubMed:19907080}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:18042720}; Multi-pass membrane protein {ECO:0000269|PubMed:18042720}. Endosome membrane {ECO:0000269|PubMed:18042720}. SUBUNIT: Interacts with LEPR. Interacts with RAB13 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely distributed in the brain, with elevated expression in the hypothalamic regions, including the paraventricular nucleus. In the placenta, present at high levels in the junctional zone situated towards the maternal aspect and throughout the labyrinth zone in close proximity to the developing fetus. {ECO:0000269|PubMed:10849209}. +A2AAJ9 OBSCN_MOUSE Obscurin (EC 2.7.11.1) (Obscurin-RhoGEF) (Obscurin-myosin light chain kinase) (Obscurin-MLCK) 8891 966,372 Active site (2); Alternative sequence (4); Binding site (2); Chain (1); Disulfide bond (46); Domain (64); Erroneous gene model prediction (3); Modified residue (15); Nucleotide binding (2); Sequence conflict (2) FUNCTION: Structural component of striated muscles which plays a role in myofibrillogenesis. Probably involved in the assembly of myosin into sarcomeric A bands in striated muscle (By similarity). Has serine/threonine protein kinase activity and phosphorylates N-cadherin CDH2 and sodium/potassium-transporting ATPase subunit ATP1B1 (PubMed:23392350). {ECO:0000250|UniProtKB:Q5VST9, ECO:0000269|PubMed:23392350}. PTM: Autophosphorylated by protein kinase domain 1 and 2. {ECO:0000269|PubMed:23392350}.; PTM: Two small isoforms, one probably containing protein kinase domain 2 and a partial protein kinase domain 1 and one containing only protein kinase domain 2, are glycosylated. {ECO:0000269|PubMed:23392350}. SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, M line {ECO:0000269|PubMed:23392350}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:23392350}. Cell membrane, sarcolemma {ECO:0000269|PubMed:23392350}. Nucleus {ECO:0000269|PubMed:23392350}. Secreted {ECO:0000269|PubMed:23392350}. Note=Colocalizes with CDH2 and ATP1B1 to the sarcolemma and to intercalating disks in cardiac muscles. Colocalizes with ATP1B1 to M line and Z line in cardiac muscles. One or both small isoforms, one probably containing protein kinase domain 2 and partial protein kinase domain 1 and one containing only protein kinase domain 2, localize to the extracellular side of the sarcolemma. {ECO:0000269|PubMed:23392350}. SUBUNIT: Interacts (via protein kinase domain 1) with CDH2 and (via protein kinase domain 1) with ATP1B1. {ECO:0000269|PubMed:23392350}. TISSUE SPECIFICITY: Expressed in skeletal muscles including flexor digitorum brevis (FDB), soleus and tibialis anterior muscles, and to a lesser extent in heart muscles (at protein level). {ECO:0000269|PubMed:23392350}. +Q9CRD0 OCAD1_MOUSE OCIA domain-containing protein 1 247 27,610 Alternative sequence (3); Chain (1); Domain (1); Frameshift (1); Modified residue (4); Sequence conflict (1) FUNCTION: Maintains stem cell potency (PubMed:23972987). Increases STAT3 phosphorylation and controls ERK phosphorylation (PubMed:23972987). May act as a scaffold, increasing STAT3 recruitment onto endosomes (PubMed:23972987). {ECO:0000269|PubMed:23972987}. SUBCELLULAR LOCATION: Endosome {ECO:0000269|PubMed:12889067, ECO:0000269|PubMed:23972987}. SUBUNIT: Interacts with STAT3. {ECO:0000269|PubMed:23972987}. DOMAIN: The OCIA domain is necessary and sufficient for endosomal localization (PubMed:23972987). {ECO:0000269|PubMed:23972987}. TISSUE SPECIFICITY: Expressed at high levels in the brain and at lower levels in the heart, ovary, testis and kidney. Expression is strongest in embryonic stem cells and in the blood vessels. {ECO:0000269|PubMed:12889067}. +P02802 MT1_MOUSE Metallothionein-1 (MT-1) (Metallothionein-I) (MT-I) 61 6,018 Beta strand (5); Chain (1); Metal binding (20); Modified residue (1); Region (2); Sequence conflict (2) FUNCTION: Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids. DOMAIN: Class I metallothioneins contain 2 metal-binding domains: four divalent ions are chelated within cluster A of the alpha domain and are coordinated via cysteinyl thiolate bridges to 11 cysteine ligands. Cluster B, the corresponding region within the beta domain, can ligate three divalent ions to 9 cysteines. +P02798 MT2_MOUSE Metallothionein-2 (MT-2) (Metallothionein-II) (MT-II) 61 6,115 Chain (1); Metal binding (20); Modified residue (2); Region (2); Sequence conflict (1) FUNCTION: Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids. DOMAIN: Class I metallothioneins contain 2 metal-binding domains: four divalent ions are chelated within cluster A of the alpha domain and are coordinated via cysteinyl thiolate bridges to 11 cysteine ligands. Cluster B, the corresponding region within the beta domain, can ligate three divalent ions to 9 cysteines. +Q61146 OCLN_MOUSE Occludin 521 59,000 Chain (1); Coiled coil (1); Compositional bias (2); Disulfide bond (1); Domain (1); Modified residue (15); Topological domain (5); Transmembrane (4) TRANSMEM 67 89 Helical. {ECO:0000255}.; TRANSMEM 134 158 Helical. {ECO:0000255}.; TRANSMEM 169 193 Helical. {ECO:0000255}.; TRANSMEM 242 263 Helical. {ECO:0000255}. TOPO_DOM 1 66 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 90 133 Extracellular. {ECO:0000255}.; TOPO_DOM 159 168 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 194 241 Extracellular. {ECO:0000255}.; TOPO_DOM 264 521 Cytoplasmic. {ECO:0000255}. FUNCTION: May play a role in the formation and regulation of the tight junction (TJ) paracellular permeability barrier. PTM: Dephosphorylated by PTPRJ (By similarity). May be phosphorylated by PKC during translocation to cell-cell contacts. {ECO:0000250, ECO:0000269|PubMed:11502742}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q16625}; Multi-pass membrane protein {ECO:0000255}. Cell junction, tight junction {ECO:0000250|UniProtKB:Q16625}. SUBUNIT: Interacts with TJP1/ZO1 and with VAPA. Interacts with CLDN1, CLDN6, CLDN9, CLDN11, CLDN12 and CLDN17. {ECO:0000250|UniProtKB:Q16625}. DOMAIN: The C-terminal is cytoplasmic and is important for interaction with ZO-1. Necessary for the tight junction localization. Involved in the regulation of the permeability barrier function of the tight junction (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Localized at tight junctions of both epithelial and endothelial cells. Highly expressed in the testis, kidney, lung, liver and brain. Not detected in skeletal muscle, spleen and heart. +P28184 MT3_MOUSE Metallothionein-3 (MT-3) (Growth inhibitory factor) (GIF) (Metallothionein-III) (MT-III) 68 7,009 Beta strand (1); Chain (1); Metal binding (20); Modified residue (2); Region (2); Turn (1) FUNCTION: Binds heavy metals. Contains three zinc and three copper atoms per polypeptide chain and only a negligible amount of cadmium. Inhibits survival and neurite formation of cortical neurons in vitro (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Brain. +Q8CHZ9 MTF1A_MOUSE Transcription termination factor 1a, mitochondrial (Mitochondrial transcription termination factor 1a) (mTERF1a) 379 43,815 Chain (1); Region (5); Sequence conflict (8); Site (3); Transit peptide (1) FUNCTION: Transcription termination factor. Binds to a 28 bp region within the tRNA(Leu(uur)) gene at a position immediately adjacent to and downstream of the 16S rRNA gene; this region comprises a tridecamer sequence critical for directing accurate termination. Binds DNA along the major grove and promotes DNA bending and partial unwinding. Promotes base flipping. Transcription termination activity appears to be polarized with highest specificity for transcripts initiated on the light strand. {ECO:0000269|PubMed:23562081}. PTM: Phosphoprotein with mostly four phosphate groups. While the DNA-binding activity is unaffected by the phosphorylation state, only the phosphorylated form of the protein is active for termination activity. Functioning seems to be regulated by phosphorylation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:15582606}. SUBUNIT: Monomer. {ECO:0000250}. DOMAIN: Contains nine structural repeats of about 35 residues, where each repeat contains three helices. The repeats form a left-handed superhelical assembly with a solenoid structure that wraps itself around DNA (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Predominantly expressed in heart and liver, with extremely low levels in other tissues (PubMed:15582606). Expressed strongly in the heart and at lower levels in brain, liver and kidney (PubMed:23562081). {ECO:0000269|PubMed:15582606, ECO:0000269|PubMed:23562081}. +Q60700 M3K12_MOUSE Mitogen-activated protein kinase kinase kinase 12 (EC 2.7.11.25) (Dual leucine zipper bearing kinase) (DLK) (Leucine-zipper protein kinase) (ZPK) (MAPK-upstream kinase) (MUK) (Mixed lineage kinase) 888 96,084 Active site (1); Binding site (1); Chain (1); Compositional bias (4); Domain (1); Modified residue (4); Mutagenesis (2); Nucleotide binding (1); Region (2); Sequence conflict (8) FUNCTION: Protein kinase which is part of a non-canonical MAPK signaling pathway (PubMed:7983011, PubMed:8663324, PubMed:28111074). Activated by APOE, enhances the AP-1-mediated transcription of APP, via a MAP kinase signal transduction pathway composed of MAP2K7 and MAPK1/ERK2 and MAPK3/ERK1 (PubMed:28111074). May be an activator of the JNK/SAPK pathway. {ECO:0000269|PubMed:28111074, ECO:0000269|PubMed:7983011, ECO:0000269|PubMed:8663324}. PTM: Autophosphorylated on Ser/Thr. Phosphorylated in cytosol under basal conditions and dephosphorylated when membrane-associated. {ECO:0000269|PubMed:7983011, ECO:0000269|PubMed:8663324}.; PTM: The activity of MAP3K12 can be regulated through its proteasomal degradation. APOE, through a receptor-mediated mechanism, activates MAP3K12 by preventing its proteasomal degradation. {ECO:0000250|UniProtKB:Q12852}. SUBCELLULAR LOCATION: Cytoplasm. Cell membrane {ECO:0000269|PubMed:8663324}. Note=Behaves essentially as an integral membrane protein. {ECO:0000269|PubMed:8663324}. SUBUNIT: Homodimer (PubMed:8663324). Interacts with MBIP (By similarity). {ECO:0000250|UniProtKB:Q12852, ECO:0000269|PubMed:8663324}. DOMAIN: Interacts with MBIP through the leucine-zipper motif. {ECO:0000250|UniProtKB:Q12852}. TISSUE SPECIFICITY: Within the nervous system, predominantly expressed in neurons and enriched in synaptic terminals (PubMed:8663324). Expressed in brain, kidney, lung, heart, testis, gastrointestinal tract, stomach, liver and pancreas (PubMed:8769565, PubMed:7983011). {ECO:0000269|PubMed:7983011, ECO:0000269|PubMed:8663324, ECO:0000269|PubMed:8769565}. +Q60948 MAD4_MOUSE Max dimerization protein 4 (Max dimerizer 4) (Max-associated protein 4) (Max-interacting transcriptional repressor MAD4) 209 23,590 Chain (1); Domain (1); Region (1) FUNCTION: Transcriptional repressor. Binds with MAX to form a sequence-specific DNA-binding protein complex which recognizes the core sequence 5'-CAC[GA]TG-3'. Antagonizes MYC transcriptional activity by competing for MAX and suppresses MYC dependent cell transformation. {ECO:0000269|PubMed:8521822}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Efficient DNA binding requires dimerization with another bHLH protein. Binds DNA as a heterodimer with MAX. Interacts with SIN3A AND SIN3B. Interacts with RNF17. {ECO:0000269|PubMed:10597267, ECO:0000269|PubMed:8521822}. +Q9QYH6 MAGD1_MOUSE Melanoma-associated antigen D1 (Dlxin-1) (MAGE-D1 antigen) (Neurotrophin receptor-interacting MAGE homolog) 775 85,670 Chain (1); Compositional bias (1); Domain (1); Region (1); Repeat (22); Sequence conflict (1) FUNCTION: Involved in the apoptotic response after nerve growth factor (NGF) binding in neuronal cells. Inhibits cell cycle progression, and facilitates NGFR-mediated apoptosis. May act as a regulator of the function of DLX family members. May enhance ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex. Plays a role in the circadian rhythm regulation. May act as RORA coregulator, modulating the expression of core clock genes such as ARNTL/BMAL1 and NFIL3, induced, or NR1D1, repressed. {ECO:0000269|PubMed:20300063}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20300063}. Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Expression shifts from the cytoplasm to the plasma membrane upon stimulation with NGF. {ECO:0000250}. SUBUNIT: Interacts with DLX5, DLX7 and MSX2 and forms homomultimers. Interacts with UNC5A. Interacts with TRIM28 and PJA1. Interacts with NGFR/p75NTR and RORA. {ECO:0000269|PubMed:20300063}. TISSUE SPECIFICITY: Ubiquitously expressed in many adult tissues, except for the spleen. Expressed in osteoblastic and chondrogenic cell lines and also during embryonic development. +O35099 M3K5_MOUSE Mitogen-activated protein kinase kinase kinase 5 (EC 2.7.11.25) (Apoptosis signal-regulating kinase 1) (ASK-1) (MAPK/ERK kinase kinase 5) (MEK kinase 5) (MEKK 5) 1380 154,512 Active site (1); Binding site (1); Chain (1); Coiled coil (1); Domain (1); Modified residue (9); Nucleotide binding (1); Sequence conflict (3) FUNCTION: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. Plays an important role in the cascades of cellular responses evoked by changes in the environment. Mediates signaling for determination of cell fate such as differentiation and survival. Plays a crucial role in the apoptosis signal transduction pathway through mitochondria-dependent caspase activation. MAP3K5/ASK1 is required for the innate immune response, which is essential for host defense against a wide range of pathogens. Mediates signal transduction of various stressors like oxidative stress as well as by receptor-mediated inflammatory signals, such as the tumor necrosis factor (TNF) or lipopolysaccharide (LPS). Once activated, acts as an upstream activator of the MKK/JNK signal transduction cascade and the p38 MAPK signal transduction cascade through the phosphorylation and activation of several MAP kinase kinases like MAP2K4/SEK1, MAP2K3/MKK3, MAP2K6/MKK6 and MAP2K7/MKK7. These MAP2Ks in turn activate p38 MAPKs and c-jun N-terminal kinases (JNKs). Both p38 MAPK and JNKs control the transcription factors activator protein-1 (AP-1). {ECO:0000269|PubMed:11266364, ECO:0000269|PubMed:14749717, ECO:0000269|PubMed:15864310, ECO:0000269|PubMed:16527894, ECO:0000269|PubMed:16648474}. PTM: Ser-90 and Ser-1040 are inactivating phosphorylation sites, the former of which is phosphorylated by AKT1 and AKT2 (By similarity). Phosphorylated at Ser-973 which induces association of MAP3K5/ASK1 with the 14-3-3 family proteins and suppresses MAP3K5/ASK1 activity (By similarity). Calcineurin (CN) dephosphorylates this site. Also dephosphorylated and activated by PGAM5 (By similarity). Phosphorylated at Thr-845 through autophosphorylation and by MAP3K6/ASK2 which leads to activation. Thr-845 is dephosphorylated by PPP5C. {ECO:0000250, ECO:0000269|PubMed:11920685, ECO:0000269|PubMed:16648474, ECO:0000269|PubMed:18948261, ECO:0000269|PubMed:22399290}.; PTM: Ubiquitinated. Tumor necrosis factor (TNF) induces TNFR2-dependent ubiquitination leading to proteasomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Note=Interaction with 14-3-3 proteins alters the distribution of MAP3K5/ASK1 and restricts it to the perinuclear endoplasmic reticulum region. {ECO:0000250}. SUBUNIT: Homodimer when inactive (By similarity). Binds both upstream activators and downstream substrates in multimolecular complexes. Part of a cytoplasmic complex made of HIPK1, DAB2IP and MAP3K5 in response to TNF (By similarity). This complex formation promotes MAP3K5-JNK activation and subsequent apoptosis (By similarity). Interacts with SOCS1 which recognizes phosphorylation of Tyr-725 and induces MAP3K5/ASK1 degradation in endothelial cells (By similarity). Interacts with the 14-3-3 family proteins such as YWHAB, YWHAE, YWHAQ, YWHAH, YWHAZ and SFN (By similarity). Interacts with ARRB2, BIRC2, DAB2IP, IGF1R, MAP3K6/ASK2, PIM1, PGAM5, PPP5C, SOCS1, STUB1, TRAF2 and TXN (By similarity). Interacts with ERN1 in a TRAF2-dependent manner (By similarity). Interacts with calcineurin subunit PPP3R1, PPM1L and TRAF6. Interacts (via N-terminus) with RAF1 and this interaction inhibits the proapoptotic function of MAP3K5. Interacts with DAB2IP (via N-terminus C2 domain); the interaction occurs in a TNF-alpha-dependent manner (By similarity).Interacts with DUSP13/DUSP13A; may positively regulate apoptosis (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in various adult mouse tissues including heart, brain, lung, liver and kidney. {ECO:0000269|PubMed:9367868}. +Q7TQE6 MACOI_MOUSE Macoilin (Brain-specific adapter protein C61) (Macoilin-1) (Transmembrane protein 57) 664 76,089 Chain (1); Glycosylation (4); Modified residue (4); Transmembrane (4) TRANSMEM 28 48 Helical. {ECO:0000255}.; TRANSMEM 75 95 Helical. {ECO:0000255}.; TRANSMEM 120 140 Helical. {ECO:0000255}.; TRANSMEM 154 174 Helical. {ECO:0000255}. FUNCTION: Plays a role in the regulation of neuronal activity. {ECO:0000250|UniProtKB:Q8N5G2}. SUBCELLULAR LOCATION: Rough endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P91193}; Multi-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:P91193}; Multi-pass membrane protein {ECO:0000255}. Note=Detected in the nucleus membrane of non-neuronal cells and in axonal outgrowths of neuronal cells (PubMed:15255972). {ECO:0000269|PubMed:15255972}. TISSUE SPECIFICITY: Strong expression in whole nervous system up to E12.5. Highly expressed in all neuronal differentiation fields from E14.5 to birth, with highest expression in the telencephalic cortical plate and mitral cells in the olfactory bulb, and lower expression in neuronal progenitor zones. Progressively decreased expression in fields of neuron precursor proliferation from E14.5 and virtually undetectable there by E17.5. No significant expression detected outside the nervous system. After birth, significant expression remains in the cerebellum, olfactory bulb and hippocampus. {ECO:0000269|PubMed:15255972}. +Q9NWG9 MAGH1_MOUSE Melanoma-associated antigen H1 (MAGE-H1 antigen) 218 24,325 Chain (1); Domain (1); Modified residue (1) +P33033 MC3R_MOUSE Melanocortin receptor 3 (MC3-R) 323 35,806 Chain (1); Glycosylation (3); Lipidation (1); Topological domain (8); Transmembrane (7) TRANSMEM 38 63 Helical; Name=1. {ECO:0000255}.; TRANSMEM 76 100 Helical; Name=2. {ECO:0000255}.; TRANSMEM 119 140 Helical; Name=3. {ECO:0000255}.; TRANSMEM 161 181 Helical; Name=4. {ECO:0000255}.; TRANSMEM 187 210 Helical; Name=5. {ECO:0000255}.; TRANSMEM 246 268 Helical; Name=6. {ECO:0000255}.; TRANSMEM 278 301 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 37 Extracellular. {ECO:0000255}.; TOPO_DOM 64 75 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 101 118 Extracellular. {ECO:0000255}.; TOPO_DOM 141 160 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 182 186 Extracellular. {ECO:0000255}.; TOPO_DOM 211 245 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 269 277 Extracellular. {ECO:0000255}.; TOPO_DOM 302 323 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for MSH (alpha, beta and gamma) and ACTH. This receptor is mediated by G proteins which activate adenylate cyclase. Required for expression of anticipatory patterns of activity and wakefulness during periods of limited nutrient availability and for the normal regulation of circadian clock activity in the brain (PubMed:19036988). {ECO:0000269|PubMed:19036988}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Brain. +Q8BH31 MFSD8_MOUSE Major facilitator superfamily domain-containing protein 8 519 57,569 Chain (1); Glycosylation (2); Motif (1); Sequence conflict (7); Topological domain (13); Transmembrane (12) TRANSMEM 42 62 Helical. {ECO:0000255}.; TRANSMEM 76 96 Helical. {ECO:0000255}.; TRANSMEM 107 127 Helical. {ECO:0000255}.; TRANSMEM 141 161 Helical. {ECO:0000255}.; TRANSMEM 175 195 Helical. {ECO:0000255}.; TRANSMEM 213 233 Helical. {ECO:0000255}.; TRANSMEM 268 288 Helical. {ECO:0000255}.; TRANSMEM 311 331 Helical. {ECO:0000255}.; TRANSMEM 339 359 Helical. {ECO:0000255}.; TRANSMEM 417 439 Helical. {ECO:0000255}.; TRANSMEM 453 473 Helical. {ECO:0000255}.; TRANSMEM 484 504 Helical. {ECO:0000255}. TOPO_DOM 1 41 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 63 75 Extracellular. {ECO:0000255}.; TOPO_DOM 97 106 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 128 140 Extracellular. {ECO:0000255}.; TOPO_DOM 162 174 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 196 212 Extracellular. {ECO:0000255}.; TOPO_DOM 234 267 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 289 310 Extracellular. {ECO:0000255}.; TOPO_DOM 332 338 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 360 416 Extracellular. {ECO:0000255}.; TOPO_DOM 440 452 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 474 483 Extracellular. {ECO:0000255}.; TOPO_DOM 505 519 Cytoplasmic. {ECO:0000255}. FUNCTION: May be a carrier that transport small solutes by using chemiosmotic ion gradients. {ECO:0000305}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Sorting to lysosomes involves tyrosine- and/or dileucine-based motifs. {ECO:0000250}. +Q8BMG8 MFTC_MOUSE Mitochondrial folate transporter/carrier (Solute carrier family 25 member 32) 316 35,049 Chain (1); Repeat (3); Transmembrane (6) TRANSMEM 26 46 Helical; Name=1. {ECO:0000255}.; TRANSMEM 89 106 Helical; Name=2. {ECO:0000255}.; TRANSMEM 123 143 Helical; Name=3. {ECO:0000255}.; TRANSMEM 185 203 Helical; Name=4. {ECO:0000255}.; TRANSMEM 227 243 Helical; Name=5. {ECO:0000255}.; TRANSMEM 281 300 Helical; Name=6. {ECO:0000255}. FUNCTION: Transports folate across the inner membranes of mitochondria. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q8CCT7 NSUN3_MOUSE tRNA (cytosine(34)-C(5))-methyltransferase, mitochondrial (EC 2.1.1.-) (NOL1/NOP2/Sun domain family member 3) 348 39,182 Active site (1); Alternative sequence (1); Binding site (3); Chain (1); Region (1) FUNCTION: Mitochondrial tRNA methyltransferase that mediates methylation of cytosine to 5-methylcytosine (m5C) at position 34 of mt-tRNA(Met). mt-tRNA(Met) methylation at cytosine(34) takes place at the wobble position of the anticodon and initiates the formation of 5-formylcytosine (f(5)c) at this position. mt-tRNA(Met) containing the f(5)c modification at the wobble position enables recognition of the AUA codon in addition to the AUG codon, expanding codon recognition in mitochondrial translation. {ECO:0000250|UniProtKB:Q9H649}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:Q9H649}. +P61971 NTF2_MOUSE Nuclear transport factor 2 (NTF-2) 127 14,478 Chain (1); Domain (1); Modified residue (1) FUNCTION: Mediates the import of GDP-bound RAN from the cytoplasm into the nucleus which is essential for the function of RAN in cargo receptor-mediated nucleocytoplasmic transport. Thereby, plays indirectly a more general role in cargo receptor-mediated nucleocytoplasmic transport. Interacts with GDP-bound RAN in the cytosol, recruits it to the nuclear pore complex via its interaction with nucleoporins and promotes its nuclear import. {ECO:0000250|UniProtKB:P61970}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P61970}. Nucleus outer membrane {ECO:0000250|UniProtKB:P61972}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P61972}. Nucleus inner membrane {ECO:0000250|UniProtKB:P61972}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P61970}. Note=At steady state it is essentially nucleoplasmic, enriched in nucleoplasmic foci. {ECO:0000250|UniProtKB:P61970}. SUBUNIT: Homodimer. Interacts with RAN (GDP-bound form); the interaction is direct and regulates RAN nuclear import. Interacts with the nucleoporins NUP54, NUP58 and NUP62 (via FG repeats); recruits NUTF2 to the nuclear pore complex a step required for NUTF2-mediated GDP-bound RAN nuclear import. Interacts with CAPG; mediates its nuclear import. {ECO:0000250|UniProtKB:P61970}. +P20181 NTF3_MOUSE Neurotrophin-3 (NT-3) (HDNF) (Nerve growth factor 2) (NGF-2) (Neurotrophic factor) 258 29,588 Chain (1); Disulfide bond (3); Glycosylation (1); Propeptide (1); Signal peptide (1) FUNCTION: Seems to promote the survival of visceral and proprioceptive sensory neurons. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Brain and peripheral tissues. +Q80VU4 NTF4_MOUSE Neurotrophin-4 (NT-4) (Neurotrophin-5) (NT-5) (Neutrophic factor 4) 209 22,346 Chain (1); Disulfide bond (3); Glycosylation (1); Propeptide (1); Signal peptide (1) FUNCTION: Could serve as a target-derived trophic factor for sensory and sympathetic neurons. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +O35980 NTH_MOUSE Endonuclease III-like protein 1 (EC 3.2.2.-) (EC 4.2.99.18) (Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase) (DNA glycosylase/AP lyase) 300 33,637 Active site (1); Chain (1); Domain (1); Frameshift (1); Metal binding (4); Site (1); Transit peptide (1) FUNCTION: Bifunctional DNA N-glycosylase with associated apurinic/apyrimidinic (AP) lyase function that catalyzes the first step in base excision repair (BER), the primary repair pathway for the repair of oxidative DNA damage. The DNA N-glycosylase activity releases the damaged DNA base from DNA by cleaving the N-glycosidic bond, leaving an AP site. The AP lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination. Primarily recognizes and repairs oxidative base damage of pyrimidines. {ECO:0000255|HAMAP-Rule:MF_03183, ECO:0000269|PubMed:9743625}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03183}. Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03183, ECO:0000269|PubMed:12531031}. SUBUNIT: Interacts with YBX1. {ECO:0000255|HAMAP-Rule:MF_03183}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9743625}. +Q8R2U4 NTM1A_MOUSE N-terminal Xaa-Pro-Lys N-methyltransferase 1 (EC 2.1.1.244) (Alpha N-terminal protein methyltransferase 1A) (Methyltransferase-like protein 11A) (X-Pro-Lys N-terminal protein methyltransferase 1A) (NTM1A) [Cleaved into: N-terminal Xaa-Pro-Lys N-methyltransferase 1, N-terminally processed] 223 25,420 Binding site (3); Chain (2); Initiator methionine (1); Modified residue (2); Region (2) FUNCTION: Distributive alpha-N-methyltransferase that methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Gly/Pro/Ser]-Pro-Lys when the initiator Met is cleaved. Specifically catalyzes mono-, di- or tri-methylation of the exposed alpha-amino group of the Ala, Gly or Ser residue in the [Ala/Gly/Ser]-Pro-Lys motif and mono- or di-methylation of Pro in the Pro-Pro-Lys motif (PubMed:20668449). Some of the substrates may be primed by METTL11B-mediated monomethylation. Catalyzes the trimethylation of the N-terminal Gly in CENPA (after removal of Met-1) (By similarity). Responsible for the N-terminal methylation of KLHL31, MYL2, MYL3, RB1, RCC1, RPL23A and SET. Required during mitosis for normal bipolar spindle formation and chromosome segregation via its action on RCC1 (PubMed:20668449). {ECO:0000250|UniProtKB:Q9BV86, ECO:0000269|PubMed:20668449}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BV86}. Note=Predominantly nuclear. {ECO:0000250|UniProtKB:Q9BV86}. +B2RXM4 NTM1B_MOUSE Alpha N-terminal protein methyltransferase 1B (EC 2.1.1.299) (Methyltransferase-like protein 11B) (X-Pro-Lys N-terminal protein methyltransferase 1B) (NTM1B) 283 32,313 Binding site (3); Chain (1); Region (1) FUNCTION: Alpha-N-methyltransferase that methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys when the initiator Met is cleaved. Specifically catalyzes monomethylation of exposed alpha-amino group of Ala or Ser residue in the [Ala/Ser]-Pro-Lys motif and Pro in the Pro-Pro-Lys motif. May activate NTMT1 by priming its substrates for trimethylation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +Q8R4G0 NTNG1_MOUSE Netrin-G1 (Laminet-1) 539 60,566 Alternative sequence (16); Chain (1); Disulfide bond (17); Domain (4); Erroneous initiation (1); Glycosylation (4); Lipidation (1); Propeptide (1); Region (3); Sequence conflict (8); Signal peptide (1) FUNCTION: Involved in controlling patterning and neuronal circuit formation at the laminar, cellular, subcellular and synaptic levels. Promotes neurite outgrowth of both axons and dendrites. {ECO:0000269|PubMed:11804778}. PTM: N-glycosylated. {ECO:0000269|PubMed:10964959}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10964959}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:10964959}; Extracellular side {ECO:0000269|PubMed:10964959}. DOMAIN: The laminin N-terminal domain mediates 1:1 binding to NGL ligand with sub-micromolar affinity. Three NGL-binding loops mediate discrimination for LRRC4C/NGL1 among other NGLs by binding specifically to its LRR repeats. This specificity drives the sorting of a mixed population of molecules into discrete cell surface subdomains (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expression is restricted primarily to neurons of the CNS, particularly in the dorsal thalamus, olfactory bulb and inferior colliculus. Isoform 1A and isoform 1D are the major products in adult brain. {ECO:0000269|PubMed:10964959, ECO:0000269|PubMed:11804778, ECO:0000269|PubMed:11906208}. +Q8R4F1 NTNG2_MOUSE Netrin-G2 (Laminet-2) 589 66,166 Alternative sequence (4); Chain (1); Disulfide bond (19); Domain (4); Glycosylation (5); Lipidation (1); Propeptide (1); Region (3); Sequence conflict (3); Signal peptide (1) FUNCTION: Involved in controlling patterning and neuronal circuit formation at the laminar, cellular, subcellular and synaptic levels. Promotes neurite outgrowth of both axons and dendrites. {ECO:0000269|PubMed:11804778}. PTM: N-glycosylated. {ECO:0000269|PubMed:11906208}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11804778}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:11804778}; Extracellular side {ECO:0000269|PubMed:11804778}. SUBUNIT: Interacts with LRRC4. {ECO:0000269|PubMed:16980967, ECO:0000269|PubMed:17973922}. DOMAIN: The laminin N-terminal domain mediates 1:1 binding to NGL ligand with sub-micromolar affinity. Three NGL-binding loops mediate discrimination for LRRC4/NGL2 among other NGLs by binding specifically to its LRR repeats. This specificity drives the sorting of a mixed population of molecules into discrete cell surface subdomains (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expression is restricted primarily to neurons of the CNS, particularly in the cerebral cortex, habenular nucleus and superior colliculus. Low levels in lung, kidney, heart and spleen. {ECO:0000269|PubMed:11804778, ECO:0000269|PubMed:11906208}. +Q9CQA9 NTPCR_MOUSE Cancer-related nucleoside-triphosphatase homolog (NTPase) (EC 3.6.1.15) (Nucleoside triphosphate phosphohydrolase) 190 20,667 Chain (1); Modified residue (1); Nucleotide binding (2) FUNCTION: Has nucleotide phosphatase activity towards ATP, GTP, CTP, TTP and UTP. Hydrolyzes nucleoside diphosphates with lower efficiency (By similarity). {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. +O88319 NTR1_MOUSE Neurotensin receptor type 1 (NT-R-1) (NTR1) 424 47,217 Chain (1); Disulfide bond (1); Glycosylation (4); Lipidation (2); Region (1); Topological domain (8); Transmembrane (7) TRANSMEM 68 88 Helical; Name=1. {ECO:0000250|UniProtKB:P20789}.; TRANSMEM 103 122 Helical; Name=2. {ECO:0000250|UniProtKB:P20789}.; TRANSMEM 143 164 Helical; Name=3. {ECO:0000250|UniProtKB:P20789}.; TRANSMEM 185 205 Helical; Name=4. {ECO:0000250|UniProtKB:P20789}.; TRANSMEM 235 259 Helical; Name=5. {ECO:0000250|UniProtKB:P20789}.; TRANSMEM 309 330 Helical; Name=6. {ECO:0000250|UniProtKB:P20789}.; TRANSMEM 349 369 Helical; Name=7. {ECO:0000250|UniProtKB:P20789}. TOPO_DOM 1 67 Extracellular. {ECO:0000250|UniProtKB:P20789}.; TOPO_DOM 89 102 Cytoplasmic. {ECO:0000250|UniProtKB:P20789}.; TOPO_DOM 123 142 Extracellular. {ECO:0000250|UniProtKB:P20789}.; TOPO_DOM 165 184 Cytoplasmic. {ECO:0000250|UniProtKB:P20789}.; TOPO_DOM 206 234 Extracellular. {ECO:0000250|UniProtKB:P20789}.; TOPO_DOM 260 308 Cytoplasmic. {ECO:0000250|UniProtKB:P20789}.; TOPO_DOM 331 348 Extracellular. {ECO:0000250|UniProtKB:P20789}.; TOPO_DOM 370 424 Cytoplasmic. {ECO:0000250|UniProtKB:P20789}. FUNCTION: G-protein coupled receptor for the tridecapeptide neurotensin (NTS). Signaling is effected via G proteins that activate a phosphatidylinositol-calcium second messenger system. Signaling leads to the activation of downstream MAP kinases and protects cells against apoptosis. {ECO:0000250|UniProtKB:P30989}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:P30989}.; PTM: Palmitoylated; this is required for normal localization at membrane rafts and normal GNA11-mediated activation of down-stream signaling cascades. The palmitoylation level increases in response to neurotensin treatment. {ECO:0000250|UniProtKB:P30989}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P30989}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P30989}. Membrane raft {ECO:0000250|UniProtKB:P30989}. Note=Palmitoylation is required for localization at CAV1-enriched membrane rafts. {ECO:0000250|UniProtKB:P30989}. SUBUNIT: Interacts (palmitoylated form) with GNA11. {ECO:0000250|UniProtKB:P30989}. DOMAIN: The ligand binding pocket consists mainly of extracellular loops ECL2 and ECL3, as well as transmembrane regions TM6 and TM7. {ECO:0000250|UniProtKB:P20789}. +P70310 NTR2_MOUSE Neurotensin receptor type 2 (NT-R-2) (NTR2) (Low-affinity levocabastine-sensitive neurotensin receptor) (NTRL) 416 46,376 Chain (1); Disulfide bond (1); Frameshift (1); Lipidation (1); Modified residue (1); Sequence conflict (3); Topological domain (8); Transmembrane (7) TRANSMEM 33 55 Helical; Name=1. {ECO:0000255}.; TRANSMEM 65 87 Helical; Name=2. {ECO:0000255}.; TRANSMEM 110 131 Helical; Name=3. {ECO:0000255}.; TRANSMEM 155 176 Helical; Name=4. {ECO:0000255}.; TRANSMEM 218 237 Helical; Name=5. {ECO:0000255}.; TRANSMEM 298 318 Helical; Name=6. {ECO:0000255}.; TRANSMEM 338 358 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 32 Extracellular. {ECO:0000255}.; TOPO_DOM 56 64 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 88 109 Extracellular. {ECO:0000255}.; TOPO_DOM 132 154 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 177 217 Extracellular. {ECO:0000255}.; TOPO_DOM 238 297 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 319 337 Extracellular. {ECO:0000255}.; TOPO_DOM 359 416 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for the tridecapeptide neurotensin. It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed maximally in the cerebellum, hyppocampus, piriform cortex and neocortex of adult brain. +Q99PJ0 NTRI_MOUSE Neurotrimin 344 37,984 Chain (1); Disulfide bond (3); Domain (3); Glycosylation (7); Lipidation (1); Propeptide (1); Sequence conflict (6); Signal peptide (1) FUNCTION: Neural cell adhesion molecule. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. +Q3UFB7 NTRK1_MOUSE High affinity nerve growth factor receptor (EC 2.7.10.1) (Neurotrophic tyrosine kinase receptor type 1) 799 87,738 Active site (1); Binding site (1); Chain (1); Disulfide bond (5); Domain (4); Erroneous initiation (1); Glycosylation (11); Modified residue (5); Nucleotide binding (1); Region (1); Repeat (2); Signal peptide (1); Site (2); Topological domain (2); Transmembrane (1) TRANSMEM 421 441 Helical. {ECO:0000255}. TOPO_DOM 34 420 Extracellular. {ECO:0000255}.; TOPO_DOM 442 799 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor tyrosine kinase involved in the development and the maturation of the central and peripheral nervous systems through regulation of proliferation, differentiation and survival of sympathetic and nervous neurons. High affinity receptor for NGF which is its primary ligand, it can also bind and be activated by NTF3/neurotrophin-3. However, NTF3 only supports axonal extension through NTRK1 but has no effect on neuron survival. Upon dimeric NGF ligand-binding, undergoes homodimerization, autophosphorylation and activation. Recruits, phosphorylates and/or activates several downstream effectors including SHC1, FRS2, SH2B1, SH2B2 and PLCG1 that regulate distinct overlapping signaling cascades driving cell survival and differentiation. Through SHC1 and FRS2 activates a GRB2-Ras-MAPK cascade that regulates cell differentiation and survival. Through PLCG1 controls NF-Kappa-B activation and the transcription of genes involved in cell survival. Through SHC1 and SH2B1 controls a Ras-PI3 kinase-AKT1 signaling cascade that is also regulating survival. In absence of ligand and activation, may promote cell death, making the survival of neurons dependent on trophic factors. {ECO:0000269|PubMed:21816277, ECO:0000269|PubMed:8145823, ECO:0000269|PubMed:8815902}. PTM: Ligand-mediated autophosphorylation. Interaction with SQSTM1 is phosphotyrosine-dependent. Autophosphorylation at Tyr-499 mediates interaction and phosphorylation of SHC1.; PTM: N-glycosylated. {ECO:0000250|UniProtKB:P04629}.; PTM: Ubiquitinated (PubMed:16113645). Undergoes polyubiquitination upon activation; regulated by NGFR. Ubiquitination by NEDD4L leads to degradation (By similarity). Ubiquitination regulates the internalization of the receptor (PubMed:16113645). {ECO:0000250|UniProtKB:P04629, ECO:0000269|PubMed:16113645}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P35739}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P35739}. Early endosome membrane {ECO:0000269|PubMed:21816277}; Single-pass type I membrane protein {ECO:0000269|PubMed:21816277}. Late endosome membrane {ECO:0000250|UniProtKB:P35739}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P35739}. Recycling endosome membrane {ECO:0000250|UniProtKB:P35739}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P35739}. Note=Internalized to endosomes upon binding of NGF or NTF3 and further transported to the cell body via a retrograde axonal transport. Localized at cell membrane and early endosomes before nerve growth factor (NGF) stimulation. Recruited to late endosomes after NGF stimulation. Colocalized with RAPGEF2 at late endosomes. {ECO:0000250|UniProtKB:P35739}. SUBUNIT: Exists in a dynamic equilibrium between monomeric (low affinity) and dimeric (high affinity) structures. Homodimerization is induced by binding of a NGF dimer (By similarity). Found in a complex, at least composed of KIDINS220, MAGI2, NTRK1 and RAPGEF2; the complex is mainly formed at late endosomes in a nerve growth factor (NGF)-dependent manner. Interacts with RAPGEF2; the interaction is strengthened after NGF stimulation. Interacts with SQSTM1; bridges NTRK1 to NGFR. Forms a ternary complex with NGFR and KIDINS220; this complex is affected by the expression levels of KIDINS220 and an increase in KIDINS220 expression leads to a decreased association of NGFR and NTRK1. Interacts (phosphorylated upon activation by NGF) with SHC1; mediates SHC1 phosphorylation and activation. Interacts (phosphorylated upon activation by NGF) with PLCG1; mediates PLCG1 phosphorylation and activation. Interacts (phosphorylated) with SH2B1 and SH2B2. Interacts with GRB2. Interacts with PIK3R1. Interacts with FRS2. Interacts with SORT1; may regulate NTRK1 anterograde axonal transport (By similarity). Interacts with SH2D1A; regulates NTRK1 (PubMed:16223723). Interacts with NRADD. Interacts with RAB7A. Interacts with PTPRS (By similarity). Interacts with USP36; USP36 does not deubiquitinate NTRK1 (By similarity). Interacts with GGA3 (By similarity). {ECO:0000250|UniProtKB:P04629, ECO:0000250|UniProtKB:P35739, ECO:0000269|PubMed:16223723}. DOMAIN: The transmembrane domain mediates interaction with KIDINS220. {ECO:0000250|UniProtKB:P35739}.; DOMAIN: The extracellular domain mediates interaction with NGFR. {ECO:0000250|UniProtKB:P35739}. +P15209 NTRK2_MOUSE BDNF/NT-3 growth factors receptor (EC 2.7.10.1) (GP145-TrkB/GP95-TrkB) (Trk-B) (Neurotrophic tyrosine kinase receptor type 2) (TrkB tyrosine kinase) 821 92,133 Active site (1); Alternative sequence (5); Binding site (1); Chain (1); Disulfide bond (6); Domain (5); Glycosylation (11); Modified residue (5); Mutagenesis (2); Nucleotide binding (1); Region (1); Repeat (2); Signal peptide (1); Site (3); Topological domain (2); Transmembrane (1) TRANSMEM 430 453 Helical. {ECO:0000255}. TOPO_DOM 32 429 Extracellular. {ECO:0000255}.; TOPO_DOM 454 821 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor tyrosine kinase involved in the development and the maturation of the central and the peripheral nervous systems through regulation of neuron survival, proliferation, migration, differentiation, and synapse formation and plasticity. Receptor for BDNF/brain-derived neurotrophic factor and NTF4/neurotrophin-4. Alternatively can also bind NTF3/neurotrophin-3 which is less efficient in activating the receptor but regulates neuron survival through NTRK2. Upon ligand-binding, undergoes homodimerization, autophosphorylation and activation. Recruits, phosphorylates and/or activates several downstream effectors including SHC1, FRS2, SH2B1, SH2B2 and PLCG1 that regulate distinct overlapping signaling cascades. Through SHC1, FRS2, SH2B1, SH2B2 activates the GRB2-Ras-MAPK cascade that regulates for instance neuronal differentiation including neurite outgrowth. Through the same effectors controls the Ras-PI3 kinase-AKT1 signaling cascade that mainly regulates growth and survival. Through PLCG1 and the downstream protein kinase C-regulated pathways controls synaptic plasticity. Thereby, plays a role in learning and memory by regulating both short term synaptic function and long-term potentiation. PLCG1 also leads to NF-Kappa-B activation and the transcription of genes involved in cell survival. Hence, it is able to suppress anoikis, the apoptosis resulting from loss of cell-matrix interactions. Isoform GP95-TRKB may also play a role in neutrophin-dependent calcium signaling in glial cells and mediate communication between neurons and glia. {ECO:0000269|PubMed:10571233, ECO:0000269|PubMed:12367511, ECO:0000269|PubMed:15329723, ECO:0000269|PubMed:15372074, ECO:0000269|PubMed:1645620, ECO:0000269|PubMed:16801538, ECO:0000269|PubMed:21414899, ECO:0000269|PubMed:8402890, ECO:0000269|PubMed:9728914}. PTM: Phosphorylated. Undergoes ligand-mediated autophosphorylation that is required for interaction with SHC1 and PLCG1 and other downstream effectors. Some isoforms are not phosphorylated (By similarity). {ECO:0000250}.; PTM: Ubiquitinated. Undergoes polyubiquitination upon activation; regulated by NGFR. Ubiquitination regulates the internalization of the receptor. {ECO:0000269|PubMed:16113645}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14581459}; Single-pass type I membrane protein {ECO:0000269|PubMed:14581459}. Endosome membrane {ECO:0000269|PubMed:14581459}; Single-pass type I membrane protein {ECO:0000269|PubMed:14581459}. Early endosome membrane {ECO:0000269|PubMed:21849472}. Cell projection, axon {ECO:0000250|UniProtKB:Q63604}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q63604}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q63604}. Note=Internalized to endosomes upon ligand-binding. {ECO:0000269|PubMed:21849472}. SUBUNIT: Exists in a dynamic equilibrium between monomeric (low affinity) and dimeric (high affinity) structures. Interacts (phosphorylated upon activation by BDNF) with SHC1; mediates SHC1 phosphorylation and activation. Interacts (phosphorylated upon activation by BDNF) with PLCG1 and/or PLCG2; mediates PLCG1 phosphorylation and activation. Interacts with SH2B1 and SH2B2. Interacts with NGFR; may regulate the ligand specificity of the receptor (By similarity). Interacts (phosphorylated upon ligand-binding) with SH2D1A; regulates NTRK2. Interacts with SQSTM1 and KIDINS220 (By similarity). Interacts (phosphorylated upon ligand-binding) with FRS2; activates the MAPK signaling pathway (By similarity). Interacts with APPL1 (PubMed:21849472). Interacts with MAPK8IP3/JIP3 and KLC1; interaction with KLC1 is mediated by MAPK8IP3/JIP3 (By similarity). {ECO:0000250|UniProtKB:P04629, ECO:0000250|UniProtKB:Q63604, ECO:0000269|PubMed:21849472}. TISSUE SPECIFICITY: Widely expressed in the central and peripheral nervous system. The different forms are differentially expressed in various cell types. Isoform GP95-TRKB is specifically expressed in glial cells. +Q6VNS1 NTRK3_MOUSE NT-3 growth factor receptor (EC 2.7.10.1) (GP145-TrkC) (Trk-C) (Neurotrophic tyrosine kinase receptor type 3) (TrkC tyrosine kinase) 825 92,760 Active site (1); Alternative sequence (4); Binding site (1); Chain (1); Disulfide bond (6); Domain (4); Glycosylation (14); Modified residue (5); Nucleotide binding (1); Repeat (2); Sequence conflict (1); Signal peptide (1); Site (2); Topological domain (2); Transmembrane (1) TRANSMEM 430 453 Helical. {ECO:0000255}. TOPO_DOM 32 429 Extracellular. {ECO:0000255}.; TOPO_DOM 454 825 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor tyrosine kinase involved in nervous system and probably heart development. Upon binding of its ligand NTF3/neurotrophin-3, NTRK3 autophosphorylates and activates different signaling pathways, including the phosphatidylinositol 3-kinase/AKT and the MAPK pathways, that control cell survival and differentiation. {ECO:0000250|UniProtKB:Q16288}. PTM: Ligand-mediated auto-phosphorylation. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Exists in a dynamic equilibrium between monomeric (low affinity) and dimeric (high affinity) structures (By similarity). Binds SH2B2. Interacts with SQSTM1 and KIDINS220 (By similarity). Interacts with PTPRS (PubMed:25385546).Interacts with MAPK8IP3/JIP3 (By similarity). {ECO:0000250|UniProtKB:P04629, ECO:0000250|UniProtKB:Q03351, ECO:0000269|PubMed:25385546}. TISSUE SPECIFICITY: Isoform 2 expression is restricted to specific areas in adult brain. Isoform 3 transcripts are readily detected early during embryogenesis and are expressed predominantly in adult brain and gonads. {ECO:0000269|PubMed:9802700}. +Q8BH74 NU107_MOUSE Nuclear pore complex protein Nup107 (107 kDa nucleoporin) (Nucleoporin Nup107) 926 106,717 Chain (1); Modified residue (14) FUNCTION: Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. Required for the assembly of peripheral proteins into the NPC. May anchor NUP62 to the NPC. {ECO:0000250|UniProtKB:P57740}. SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250|UniProtKB:P57740}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P57740}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:P57740}. Note=Located on both the cytoplasmic and nuclear sides of the NPC core structure. During mitosis, localizes to the kinetochores. Dissociates from the dissasembled NPC structure late during prophase of mitosis. {ECO:0000250|UniProtKB:P57740}. SUBUNIT: Part of the nuclear pore complex (NPC). Forms part of the Nup160 subcomplex in the nuclear pore which is composed of NUP160, NUP133, NUP107 and Nup96; this complex plays a role in RNA export and in tethering Nup98 and NUP153 to the nucleus. Does not interact with TPR (By similarity). Interacts with ZNF106 (PubMed:28072389). {ECO:0000250|UniProtKB:P57740, ECO:0000269|PubMed:28072389}. +Q8R0G9 NU133_MOUSE Nuclear pore complex protein Nup133 (133 kDa nucleoporin) (Nucleoporin Nup133) 1155 128,620 Chain (1); Modified residue (19); Sequence conflict (5) FUNCTION: Involved in poly(A)+ RNA transport. {ECO:0000250|UniProtKB:Q8WUM0}. SUBCELLULAR LOCATION: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q8WUM0}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q8WUM0}. Note=Located on both the cytoplasmic and nuclear sides of the nuclear pore. During mitosis, localizes to the kinetochores. {ECO:0000250|UniProtKB:Q8WUM0}. SUBUNIT: Forms part of the Nup160 subcomplex in the nuclear pore which is composed of NUP160, NUP133, NUP107 and Nup96. This complex plays a role in RNA export and in tethering Nup98 and NUP153 to the nucleus (By similarity). {ECO:0000250}. +Q99P88 NU155_MOUSE Nuclear pore complex protein Nup155 (155 kDa nucleoporin) (Nucleoporin Nup155) 1391 155,118 Chain (1); Compositional bias (1); Glycosylation (1); Modified residue (1) FUNCTION: Essential component of nuclear pore complex. Could be essessential for embryogenesis. Nucleoporins may be involved both in binding and translocating proteins during nucleocytoplasmic transport. {ECO:0000250|UniProtKB:P37199, ECO:0000269|PubMed:19070573}. PTM: Phosphorylated. Phosphorylation and dephosphorylation may be important for the function of NUP155 and may play a role in the reversible disassembly of the nuclear pore complex during mitosis (By similarity). {ECO:0000250}.; PTM: Disulfide-linked to NUP62. The inner channel of the NPC has a different redox environment from the cytoplasm and allows the formation of interchain disulfide bonds between some nucleoporins, the significant increase of these linkages upon oxidative stress reduces the permeability of the NPC. SUBCELLULAR LOCATION: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P37199}. Nucleus membrane {ECO:0000250|UniProtKB:P37199}; Peripheral membrane protein {ECO:0000250|UniProtKB:P37199}; Cytoplasmic side {ECO:0000250|UniProtKB:P37199}. Nucleus membrane {ECO:0000250|UniProtKB:P37199}; Peripheral membrane protein {ECO:0000250|UniProtKB:P37199}; Nucleoplasmic side {ECO:0000250|UniProtKB:P37199}. Note=In mitosis, assumes a diffuse cytoplasmic distribution probably as a monomer, before reversing back into a punctate nuclear surface localization at the end of mitosis. {ECO:0000250|UniProtKB:P37199}. SUBUNIT: Interacts with GLE1 and NUP35/NUP53. Able to form a heterotrimer with GLE1 and NUPL2 in vitro (By similarity). Forms a complex with NUP35, NUP93, NUP205 and lamin B (By similarity). {ECO:0000250|UniProtKB:O75694}. +Q9Z0W3 NU160_MOUSE Nuclear pore complex protein Nup160 (160 kDa nucleoporin) (Gene trap locus 1-13 protein) (GTL-13) (Nucleoporin Nup160) 1402 158,232 Alternative sequence (2); Chain (1); Modified residue (4); Sequence conflict (5) FUNCTION: Involved in poly(A)+ RNA transport. {ECO:0000269|PubMed:11684705}. SUBCELLULAR LOCATION: Nucleus, nuclear pore complex {ECO:0000269|PubMed:11564755, ECO:0000269|PubMed:11684705}. SUBUNIT: Forms part of the Nup160 subcomplex in the nuclear pore which is composed of NUP160, NUP133, NUP107 and Nup96. This complex plays a role in RNA export and in tethering Nup98 and NUP153 to the nucleus. {ECO:0000269|PubMed:11564755, ECO:0000269|PubMed:11684705}. +Q6ZQH8 NU188_MOUSE Nucleoporin NUP188 homolog 1759 196,696 Chain (1); Erroneous initiation (2); Initiator methionine (1); Modified residue (3); Sequence conflict (1) FUNCTION: May function as a component of the nuclear pore complex (NPC). SUBCELLULAR LOCATION: Nucleus, nuclear pore complex {ECO:0000305}. +P03888 NU1M_MOUSE NADH-ubiquinone oxidoreductase chain 1 (EC 7.1.1.2) (NADH dehydrogenase subunit 1) 318 36,059 Beta strand (7); Chain (1); Erroneous initiation (2); Helix (13); Transmembrane (8); Turn (8) TRANSMEM 2 22 Helical. {ECO:0000255}.; TRANSMEM 70 90 Helical. {ECO:0000255}.; TRANSMEM 100 120 Helical. {ECO:0000255}.; TRANSMEM 136 156 Helical. {ECO:0000255}.; TRANSMEM 171 191 Helical. {ECO:0000255}.; TRANSMEM 231 251 Helical. {ECO:0000255}.; TRANSMEM 253 273 Helical. {ECO:0000255}.; TRANSMEM 293 313 Helical. {ECO:0000255}. FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q80U93 NU214_MOUSE Nuclear pore complex protein Nup214 (214 kDa nucleoporin) (Nucleoporin Nup214) 2085 212,979 Chain (1); Coiled coil (1); Compositional bias (1); Cross-link (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (27); Region (6); Repeat (7); Sequence conflict (1) FUNCTION: May serve as a docking site in the receptor-mediated import of substrates across the nuclear pore complex. {ECO:0000250|UniProtKB:P35658}. PTM: Probably glycosylated as it reacts with wheat germ agglutinin (WGA). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P35658}. Note=Cytoplasmic side of the nuclear pore complex. {ECO:0000250|UniProtKB:P35658}. SUBUNIT: Homodimer. Interacts with ZFP36; this interaction increases upon lipopolysaccharide (LPS) stimulation. Interacts with DDX19. Interacts with NUP88. Interacts with XPO1. Interacts with XPO5. {ECO:0000250|UniProtKB:P35658}. DOMAIN: Contains FG repeats.; DOMAIN: The beta-propeller contains long interblade connector loops, and mediates interaction with DDX19B. {ECO:0000250}. +Q9D279 MISP_MOUSE Mitotic interactor and substrate of PLK1 (Mitotic spindle positioning protein) 648 72,281 Chain (1); Coiled coil (1); Modified residue (17) FUNCTION: Plays a role in mitotic spindle orientation and mitotic progression. Regulates the distribution of dynactin at the cell cortex in a PLK1-dependent manner, thus stabilizing cortical and astral microtubule attachments required for proper mitotic spindle positioning. May link microtubules to the actin cytoskeleton and focal adhesions. May be required for directed cell migration and centrosome orientation. May also be necessary for proper stacking of the Golgi apparatus (By similarity). {ECO:0000250}. PTM: Phosphorylated by CDK1 and PLK1. CDK1 is the priming kinase for PLK1 phosphorylation. Phosphorylation by PLK1 is required for proper spindle orientation at metaphase (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Note=Predominantly localizes to cortical actin structures during interphase and mitosis. Present in retraction fibers, which are formed at former adhesion sites during mitosis, and at spicular membrane protrusions in re-attaching cytokinetic cells. Partially colocalizes with cytoplasmic F-actin. Not detected at microtubules at interphase, nor at spindle during mitosis (By similarity). {ECO:0000250}. SUBUNIT: Associates with F-actin. Interacts with DCTN1; this interaction regulates DCTN1 distribution at the cell cortex. Interacts with PTK2/FAK and MAPRE1 (By similarity). {ECO:0000250}. +P63085 MK01_MOUSE Mitogen-activated protein kinase 1 (MAP kinase 1) (MAPK 1) (EC 2.7.11.24) (ERT1) (Extracellular signal-regulated kinase 2) (ERK-2) (MAP kinase isoform p42) (p42-MAPK) (Mitogen-activated protein kinase 2) (MAP kinase 2) (MAPK 2) 358 41,276 Active site (1); Binding site (7); Chain (1); Compositional bias (1); Domain (1); Initiator methionine (1); Modified residue (8); Motif (1); Nucleotide binding (1); Region (2) FUNCTION: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK1/ERK2 and MAPK3/ERK1 are the 2 MAPKs which play an important role in the MAPK/ERK cascade. They participate also in a signaling cascade initiated by activated KIT and KITLG/SCF. Depending on the cellular context, the MAPK/ERK cascade mediates diverse biological functions such as cell growth, adhesion, survival and differentiation through the regulation of transcription, translation, cytoskeletal rearrangements. The MAPK/ERK cascade plays also a role in initiation and regulation of meiosis, mitosis, and postmitotic functions in differentiated cells by phosphorylating a number of transcription factors. About 160 substrates have already been discovered for ERKs. Many of these substrates are localized in the nucleus, and seem to participate in the regulation of transcription upon stimulation. However, other substrates are found in the cytosol as well as in other cellular organelles, and those are responsible for processes such as translation, mitosis and apoptosis. Moreover, the MAPK/ERK cascade is also involved in the regulation of the endosomal dynamics, including lysosome processing and endosome cycling through the perinuclear recycling compartment (PNRC); as well as in the fragmentation of the Golgi apparatus during mitosis. The substrates include transcription factors (such as ATF2, BCL6, ELK1, ERF, FOS, HSF4 or SPZ1), cytoskeletal elements (such as CANX, CTTN, GJA1, MAP2, MAPT, PXN, SORBS3 or STMN1), regulators of apoptosis (such as BAD, BTG2, CASP9, DAPK1, IER3, MCL1 or PPARG), regulators of translation (such as EIF4EBP1) and a variety of other signaling-related molecules (like ARHGEF2, DCC, FRS2 or GRB10). Protein kinases (such as RAF1, RPS6KA1/RSK1, RPS6KA3/RSK2, RPS6KA2/RSK3, RPS6KA6/RSK4, SYK, MKNK1/MNK1, MKNK2/MNK2, RPS6KA5/MSK1, RPS6KA4/MSK2, MAPKAPK3 or MAPKAPK5) and phosphatases (such as DUSP1, DUSP4, DUSP6 or DUSP16) are other substrates which enable the propagation the MAPK/ERK signal to additional cytosolic and nuclear targets, thereby extending the specificity of the cascade. Mediates phosphorylation of TPR in respons to EGF stimulation. May play a role in the spindle assembly checkpoint. Phosphorylates PML and promotes its interaction with PIN1, leading to PML degradation. Phosphorylates CDK2AP2 (By similarity). {ECO:0000250|UniProtKB:P28482, ECO:0000250|UniProtKB:P63086, ECO:0000269|PubMed:10753946, ECO:0000269|PubMed:11702783, ECO:0000269|PubMed:12134156, ECO:0000303|PubMed:16393692, ECO:0000303|PubMed:19565474, ECO:0000303|PubMed:21779493}.; FUNCTION: Acts as a transcriptional repressor. Binds to a [GC]AAA[GC] consensus sequence. Repress the expression of interferon gamma-induced genes. Seems to bind to the promoter of CCL5, DMP1, IFIH1, IFITM1, IRF7, IRF9, LAMP3, OAS1, OAS2, OAS3 and STAT1. Transcriptional activity is independent of kinase activity. {ECO:0000250|UniProtKB:P28482}. PTM: Dually phosphorylated on Thr-183 and Tyr-185, which activates the enzyme. Ligand-activated ALK induces tyrosine phosphorylation (By similarity). Dephosphorylated by PTPRJ at Tyr-185 (By similarity). Phosphorylated upon FLT3 and KIT signaling (By similarity). Dephosphorylated by DUSP1 at Thr-183 and Tyr-185 (PubMed:8221888). {ECO:0000250, ECO:0000269|PubMed:8221888}.; PTM: ISGylated. {ECO:0000269|PubMed:22022510}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm. Membrane, caveola {ECO:0000250|UniProtKB:P63086}. Note=Associated with the spindle during prometaphase and metaphase (By similarity). PEA15-binding and phosphorylated DAPK1 promote its cytoplasmic retention. Phosphorylation at Ser-244 and Ser-246 as well as autophosphorylation at Thr-188 promote nuclear localization (By similarity). {ECO:0000250}. SUBUNIT: Binds both upstream activators and downstream substrates in multimolecular complexes. Interacts with ADAM15, ARHGEF2, ARRB2, DAPK1 (via death domain), HSF4, IER3, IPO7, DUSP6, NISCH, SGK1, and isoform 1 of NEK2. Interacts (via phosphorylated form) with TPR (via C-terminal region and phosphorylated form); the interaction requires dimerization of MAPK1/ERK2 and increases following EGF stimulation (By similarity). Interacts (phosphorylated form) with CAV2 ('Tyr-19'-phosphorylated form); the interaction, promoted by insulin, leads to nuclear location and MAPK1 activation. Interacts with DCC (By similarity). Interacts with MORG1 (PubMed:15118098). Interacts with PEA15 (PubMed:16162500). Interacts with MKNK2. MKNK2 isoform 1 binding prevents from dephosphorylation and inactivation (PubMed:11702783). The phosphorylated form interacts with PML. Interacts with STYX. Interacts with CDK2AP2. Interacts with CAVIN4 (By similarity). Interacts with DUSP7; the interaction enhances DUSP7 phosphatase activity (PubMed:27783954). {ECO:0000250|UniProtKB:P28482, ECO:0000250|UniProtKB:P63086, ECO:0000269|PubMed:11702783, ECO:0000269|PubMed:15118098, ECO:0000269|PubMed:16162500, ECO:0000269|PubMed:27783954}. DOMAIN: The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases. TISSUE SPECIFICITY: Widely expressed. +Q6P5G0 MK04_MOUSE Mitogen-activated protein kinase 4 (MAP kinase 4) (MAPK 4) (EC 2.7.11.24) (Extracellular signal-regulated kinase 4) (ERK-4) 583 65,574 Active site (1); Binding site (1); Chain (1); Domain (1); Modified residue (2); Motif (2); Mutagenesis (5); Nucleotide binding (1) FUNCTION: Atypical MAPK protein. Phosphorylates microtubule-associated protein 2 (MAP2) and MAPKAPK5. The precise role of the complex formed with MAPKAPK5 is still unclear, but the complex follows a complex set of phosphorylation events: upon interaction with atypical MAPKAPK5, ERK4/MAPK4 is phosphorylated at Ser-186 and then mediates phosphorylation and activation of MAPKAPK5, which in turn phosphorylates ERK4/MAPK4. May promote entry in the cell cycle. {ECO:0000269|PubMed:16973613}. PTM: Phosphorylated at Ser-186 by PAK1, PAK2 and PAK3 resulting in catalytic activation. Phosphorylated by MAPKAPK5 at other sites. {ECO:0000269|PubMed:18248330, ECO:0000269|PubMed:18720373}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16973613}. Nucleus {ECO:0000269|PubMed:16973613}. Note=Translocates to the cytoplasm following interaction with MAPKAPK5. SUBUNIT: Homodimer. Heterodimer with ERK3/MAPK6. Interacts with (via FRIEDE motif) MAPKAPK5. {ECO:0000269|PubMed:16973613, ECO:0000269|PubMed:18248330, ECO:0000269|PubMed:18720373, ECO:0000269|PubMed:19473979}. DOMAIN: The FRIEDE motif is required for docking MAPKAPK5. {ECO:0000269|PubMed:19473979}.; DOMAIN: In contrast to classical MAPKs, the TXY motif within the activation loop is replaced by the SEG motif, whose phosphorylation activates the MAP kinases. {ECO:0000269|PubMed:19473979}. +Q9WVS8 MK07_MOUSE Mitogen-activated protein kinase 7 (MAP kinase 7) (MAPK 7) (EC 2.7.11.24) (Big MAP kinase 1) (BMK-1) (Extracellular signal-regulated kinase 5) (ERK-5) 806 87,733 Active site (1); Alternative sequence (4); Binding site (1); Chain (1); Compositional bias (3); Domain (1); Initiator methionine (1); Modified residue (3); Motif (2); Nucleotide binding (1); Region (4); Sequence conflict (24) FUNCTION: Plays a role in various cellular processes such as proliferation, differentiation and cell survival. The upstream activator of MAPK7 is the MAPK kinase MAP2K5. Upon activation, it translocates to the nucleus and phosphorylates various downstream targets including MEF2C. EGF activates MAPK7 through a Ras-independent and MAP2K5-dependent pathway. May have a role in muscle cell differentiation. May be important for endothelial function and maintenance of blood vessel integrity. MAP2K5 and MAPK7 interact specifically with one another and not with MEK1/ERK1 or MEK2/ERK2 pathways. Phosphorylates SGK1 at Ser-78 and this is required for growth factor-induced cell cycle progression (By similarity). Involved in the regulation of p53/TP53 by disrupting the PML-MDM2 interaction (By similarity). {ECO:0000250, ECO:0000269|PubMed:11139578, ECO:0000269|PubMed:11278431, ECO:0000269|PubMed:11520859, ECO:0000269|PubMed:15085193, ECO:0000269|PubMed:15716121}. PTM: Dually phosphorylated on Thr-219 and Tyr-221, which activates the enzyme. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11139578}. Nucleus {ECO:0000269|PubMed:11139578}. Nucleus, PML body {ECO:0000250}. Note=Translocates to the nucleus upon activation. {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 1: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Isoform 1 is detected in cytoplasm and nucleus. {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 2: Nucleus {ECO:0000250}. Note=Isoform 2 is detected only in the nucleus. Translocates to the nucleus upon activation (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 3: Nucleus {ECO:0000250}. Note=Isoform 2 is detected only in the nucleus. Translocates to the nucleus upon activation (By similarity). {ECO:0000250}. SUBUNIT: Interacts with MAP2K5 (By similarity). Forms oligomers. Interacts with MEF2A, MEF2C and MEF2D; the interaction phosphorylates the MEF2s and enhances transcriptional activity of MEF2A, MEF2C but not MEF2D (By similarity). Interacts with SGK1 (By similarity). Interacts with PML (By similarity). Interacts (via N-terminal half) with HSP90AB1-CDC37 chaperone complex in resting cells; the interaction is MAP2K5-independent and prevents MAPK7 from ubiquitination and proteasomal degradation (PubMed:23428871). {ECO:0000250, ECO:0000269|PubMed:23428871}. DOMAIN: The second proline-rich region may interact with actin targeting the kinase to a specific location in the cell.; DOMAIN: The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases. TISSUE SPECIFICITY: Detected in testis, brain, kidney, lung and heart. Detected in total embryo (at protein level). {ECO:0000269|PubMed:11139578}. +O89050 MKLN1_MOUSE Muskelin 735 84,878 Beta strand (10); Chain (1); Domain (2); Helix (3); Initiator methionine (1); Modified residue (1); Mutagenesis (4); Region (1); Repeat (6) FUNCTION: Component of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1 (By similarity). Required for internalization of the GABA receptor GABRA1 from the cell membrane via endosomes and subsequent GABRA1 degradation (PubMed:21482357). Acts as a mediator of cell spreading and cytoskeletal responses to the extracellular matrix component THBS1 (PubMed:9724633, PubMed:18710924). {ECO:0000250|UniProtKB:Q9UL63, ECO:0000269|PubMed:18710924, ECO:0000269|PubMed:21482357, ECO:0000269|PubMed:9724633}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9724633}. Cytoplasm, cytosol {ECO:0000269|PubMed:18710924}. Nucleus, nucleoplasm {ECO:0000269|PubMed:18710924}. Cell projection, ruffle {ECO:0000269|PubMed:9724633}. Cytoplasm, cell cortex {ECO:0000269|PubMed:9724633}. Cell junction, synapse {ECO:0000269|PubMed:21482357}. Note=Colocalizes with GABRA1 at synapses and in post-synaptic regions (PubMed:21482357). Colocalizes with actin fibers in the cell cortex. {ECO:0000269|PubMed:21482357, ECO:0000269|PubMed:9724633}. SUBUNIT: Homodimer; may form higher oligomers (By similarity). Identified in the CTLH complex that contains GID4, RANBP9 and/or RANBP10, MKLN1, MAEA, RMND5A (or alternatively its paralog RMND5B), GID8, ARMC8, WDR26 and YPEL5. Within this complex, MAEA, RMND5A (or alternatively its paralog RMND5B), GID8, WDR26, and RANBP9 and/or RANBP10 form the catalytic core, while GID4, MKLN1, ARMC8 and YPEL5 have ancillary roles (By similarity). Interacts with RANBP9 (PubMed:18710924). Part of a complex consisting of RANBP9, MKLN1 and GID8 (By similarity). Interacts with GABRA1 (PubMed:21482357). Interacts with the C-terminal tail of PTGER3 (By similarity). {ECO:0000250|UniProtKB:Q99PV3, ECO:0000250|UniProtKB:Q9UL63, ECO:0000269|PubMed:18710924, ECO:0000269|PubMed:21482357}. DOMAIN: The LisH domain contains a nuclear targeting signal (PubMed:18710924). The LisH domain mediates head to tail dimerization (By similarity). {ECO:0000250|UniProtKB:Q99PV3, ECO:0000269|PubMed:18710924}. TISSUE SPECIFICITY: Detected in brain, especially in hippocampus and cerebellum (at protein level). {ECO:0000269|PubMed:21482357}. +Q91Z83 MYH7_MOUSE Myosin-7 (Myosin heavy chain 7) (Myosin heavy chain slow isoform) (MyHC-slow) (Myosin heavy chain, cardiac muscle beta isoform) (MyHC-beta) 1935 222,879 Chain (1); Coiled coil (1); Domain (3); Modified residue (9); Nucleotide binding (1); Region (2) FUNCTION: Myosins are actin-based motor molecules with ATPase activity essential for muscle contraction. Forms regular bipolar thick filaments that, together with actin thin filaments, constitute the fundamental contractile unit of skeletal and cardiac muscle. {ECO:0000250|UniProtKB:P12883}. SUBCELLULAR LOCATION: Cytoplasm, myofibril {ECO:0000250|UniProtKB:P02564}. Cytoplasm, myofibril, sarcomere {ECO:0000250|UniProtKB:P02564}. Note=Thick filaments of the myofibrils. {ECO:0000250|UniProtKB:P02564}. SUBUNIT: Muscle myosin is a hexameric protein that consists of 2 heavy chain subunits (MHC), 2 alkali light chain subunits (MLC) and 2 regulatory light chain subunits (MLC-2). Interacts with ECPAS. Interacts (via C-terminus) with LRRC39. {ECO:0000250|UniProtKB:P12883}. DOMAIN: Limited proteolysis of myosin heavy chain produces 1 light meromyosin (LMM) and 1 heavy meromyosin (HMM). HMM can be further cleaved into 2 globular subfragments (S1) and 1 rod-shaped subfragment (S2). {ECO:0000305}.; DOMAIN: The rodlike tail sequence is highly repetitive, showing cycles of a 28-residue repeat pattern composed of 4 heptapeptides, characteristic for alpha-helical coiled coils. Four skip residues (Skip1: Thr-1188, Skip2: Glu-1385, Skip3: Glu-1582 and Skip4: Gly-1807) introduce discontinuities in the coiled-coil heptad repeats. The first three skip residues are structurally comparable and induce a unique local relaxation of the coiled-coil superhelical pitch and the fourth skip residue lies within a highly flexible molecular hinge that is necessary for myosin incorporation in the bare zone of sarcomeres. {ECO:0000250|UniProtKB:P12883}. +Q62082 MYL10_MOUSE Myosin regulatory light chain 10 (Myosin light chain 2, lymphocyte-specific) (Precursor lymphocyte-specific regulatory light chain) 202 22,511 Alternative sequence (2); Calcium binding (1); Chain (1); Domain (3); Erroneous initiation (1); Erroneous translation (1) SUBUNIT: Myosin is a hexamer of 2 heavy chains and 4 light chains. TISSUE SPECIFICITY: Specifically expressed in precursor B- and T-lymphocytes. {ECO:0000269|PubMed:1628631}. +Q8CGK3 LONM_MOUSE Lon protease homolog, mitochondrial (EC 3.4.21.53) (Lon protease-like protein) (LONP) (Mitochondrial ATP-dependent protease Lon) (Serine protease 15) 949 105,843 Active site (2); Chain (1); Domain (2); Nucleotide binding (1); Sequence conflict (11); Transit peptide (1) FUNCTION: ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial promoters and RNA in a single-stranded, site-specific, and strand-specific manner. May regulate mitochondrial DNA replication and/or gene expression using site-specific, single-stranded DNA binding to target the degradation of regulatory proteins binding to adjacent sites in mitochondrial promoters. {ECO:0000255|HAMAP-Rule:MF_03120, ECO:0000269|PubMed:12657466}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-Rule:MF_03120, ECO:0000269|PubMed:12657466}. SUBUNIT: Homohexamer. Organized in a ring with a central cavity. The ATP-binding and proteolytic domains (AP-domain) form a hexameric chamber, while the N-terminal domain is arranged as a trimer of dimers. DNA and RNA binding is stimulated by substrate and inhibited by ATP binding. Interacts with TWNK and mitochondrial DNA polymerase subunit POLG. {ECO:0000255|HAMAP-Rule:MF_03120}. TISSUE SPECIFICITY: Detected in liver > heart > kidney > testis. {ECO:0000269|PubMed:12657466}. +P09542 MYL3_MOUSE Myosin light chain 3 (Myosin alkali light chain 1, ventricular/slow skeletal muscle isoform) (Myosin light chain 1, slow-twitch muscle B/ventricular isoform) (MLC1SB) 204 22,422 Chain (1); Domain (3); Initiator methionine (1); Modified residue (6) FUNCTION: Regulatory light chain of myosin. Does not bind calcium. PTM: N-terminus is methylated by METTL11A/NTM1. {ECO:0000269|PubMed:20668449}. SUBUNIT: Myosin is a hexamer of 2 heavy chains and 4 light chains. +P09541 MYL4_MOUSE Myosin light chain 4 (MLC1EMB) (Myosin light chain 1, atrial/fetal isoform) (MLC1A) 193 21,159 Chain (1); Domain (2); Initiator methionine (1); Modified residue (1) FUNCTION: Regulatory light chain of myosin. Does not bind calcium. {ECO:0000305}. SUBUNIT: Myosin is a hexamer of 2 heavy chains and 4 light chains. TISSUE SPECIFICITY: Expressed in atrial muscle and in fetal skeletal and ventricular muscle. +C8YR32 LOXH1_MOUSE Lipoxygenase homology domain-containing protein 1 2068 235,757 Chain (1); Domain (15); Natural variant (1) FUNCTION: Required for normal function of hair cells in the inner ear. {ECO:0000269|PubMed:19732867}. SUBCELLULAR LOCATION: Cell projection, stereocilium {ECO:0000269|PubMed:19732867}. TISSUE SPECIFICITY: Expressed in the inner ear, specifically in hair cells. Higher expression is detected in the cochlea. {ECO:0000269|PubMed:19732867}. +Q99PI4 LPIN3_MOUSE Phosphatidate phosphatase LPIN3 (EC 3.1.3.4) (Lipin-3) 848 94,316 Chain (1); Modified residue (4); Motif (3); Region (2); Sequence conflict (1) FUNCTION: Regulates fatty acid metabolism. Magnesium-dependent phosphatidate phosphatase enzyme which catalyzes the conversion of phosphatidic acid to diacylglycerol during triglyceride, phosphatidylcholine and phosphatidylethanolamine biosynthesis. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. DOMAIN: Contains 1 Asp-Xaa-Asp-Xaa-Thr (DXDXT) motif, a catalytic motif known to be essential for phosphatidate phosphatase activity. {ECO:0000250}.; DOMAIN: Contains one Leu-Xaa-Xaa-Ile-Leu (LXXIL) motif, a motif known to be a transcriptional binding motif. {ECO:0000250}. TISSUE SPECIFICITY: Significant expression in intestine and other regions of the gastrointestinal tract. {ECO:0000269|PubMed:17158099}. +Q924C6 LOXL4_MOUSE Lysyl oxidase homolog 4 (EC 1.4.3.-) (Lysyl oxidase-like protein 4) (Lysyl oxidase-related protein C) 757 84,779 Chain (1); Cross-link (1); Disulfide bond (17); Domain (4); Glycosylation (2); Metal binding (3); Modified residue (1); Region (1); Sequence conflict (5); Signal peptide (1) FUNCTION: May modulate the formation of a collagenous extracellular matrix. PTM: The lysine tyrosylquinone cross-link (LTQ) is generated by condensation of the epsilon-amino group of a lysine with a topaquinone produced by oxidation of tyrosine. {ECO:0000250|UniProtKB:P33072}. SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000305}. +Q9CQ07 LRC18_MOUSE Leucine-rich repeat-containing protein 18 (Testis-specific LRR protein) 262 29,520 Alternative sequence (1); Chain (1); Repeat (7); Sequence caution (1); Sequence conflict (2) FUNCTION: May be involved in the regulation of spermatogenesis and sperm maturation. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15707978}. TISSUE SPECIFICITY: Exclusively expressed in spermatocytes and roud spermatids within seminiferous tubules during spermatogenesis. {ECO:0000269|PubMed:15707978}. +Q8BJ48 NAGPA_MOUSE N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase (EC 3.1.4.45) (Mannose 6-phosphate-uncovering enzyme) (Phosphodiester alpha-GlcNAcase) 517 56,044 Chain (1); Disulfide bond (5); Domain (1); Glycosylation (5); Motif (2); Propeptide (1); Region (1); Sequence conflict (8); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 454 474 Helical. {ECO:0000255}. TOPO_DOM 50 453 Lumenal. {ECO:0000255}.; TOPO_DOM 475 517 Cytoplasmic. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Catalyzes the second step in the formation of the mannose 6-phosphate targeting signal on lysosomal enzyme oligosaccharides by removing GlcNAc residues from GlcNAc-alpha-P-mannose moieties, which are formed in the first step. Also hydrolyzes UDP-GlcNAc, a sugar donor for Golgi N-acetylglucosaminyltransferases. PTM: The precursor is cleaved and activated in the trans-Golgi network by a furin endopeptidase. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-pass type I membrane protein. Golgi apparatus, trans-Golgi network {ECO:0000250}. Note=Cis/medial Golgi. SUBUNIT: Homotetramer arranged as two disulfide-linked homodimers. Interacts with AP4M1. {ECO:0000250|UniProtKB:P68827, ECO:0000250|UniProtKB:Q9UK23}. DOMAIN: The tyrosine-based internalization signal may be essential for its retrieval from the plasma membrane to the TGN.; DOMAIN: The C-terminal NPFKD sequence is an attractive candidate for either an endocytosis signal acting at the plasma membrane or a retrieval signal acting at the TGN to return the enzyme to the cis/medial-Golgi. +Q9D1L9 LTOR5_MOUSE Ragulator complex protein LAMTOR5 (Late endosomal/lysosomal adaptor and MAPK and MTOR activator 5) 91 9,642 Chain (1); Modified residue (1) FUNCTION: As part of the Ragulator complex it is involved in amino acid sensing and activation of mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids. Activated by amino acids through a mechanism involving the lysosomal V-ATPase, the Ragulator functions as a guanine nucleotide exchange factor activating the small GTPases Rag. Activated Ragulator and Rag GTPases function as a scaffold recruiting mTORC1 to lysosomes where it is in turn activated. When complexed to BIRC5, interferes with apoptosome assembly, preventing recruitment of pro-caspase-9 to oligomerized APAF1, thereby selectively suppressing apoptosis initiated via the mitochondrial/cytochrome c pathway (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Lysosome {ECO:0000250}. SUBUNIT: Homodimer. Part of the Ragulator complex composed of LAMTOR1, LAMTOR2, LAMTOR3, LAMTOR4 and LAMTOR5. LAMTOR4 and LAMTOR5 form a heterodimer that interacts, through LAMTOR1, with a LAMTOR2, LAMTOR3 heterodimer. The Ragulator complex interacts with both the mTORC1 complex and heterodimers constituted of the Rag GTPases RRAGA, RRAGB, RRAGC and RRAGD; regulated by amino acid availability. The Ragulator complex interacts with SLC38A9; the probable amino acid sensor. Interacts with phosphorylated BIRC5; the resulting complex binds pro-caspase-9, as well as active caspase-9, but much less efficiently. Interacts with SUPV3L1. Interacts with hepatitis B virus (HBV) oncoprotein HBX C-terminus. {ECO:0000250|UniProtKB:O43504}. +Q99LE3 LYSM3_MOUSE LysM and putative peptidoglycan-binding domain-containing protein 3 305 34,258 Chain (1); Domain (1); Glycosylation (3); Modified residue (1); Topological domain (2); Transmembrane (1) TRANSMEM 217 237 Helical. {ECO:0000255}. TOPO_DOM 1 216 Extracellular. {ECO:0000255}.; TOPO_DOM 238 305 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +P17897 LYZ1_MOUSE Lysozyme C-1 (EC 3.2.1.17) (1,4-beta-N-acetylmuramidase C) (Lysozyme C type P) 148 16,794 Active site (2); Chain (1); Disulfide bond (4); Signal peptide (1) FUNCTION: Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Lyz1 is active against a range of Gram-positive and Gram-negative bacteria. Less effective than Lyz2 in killing Gram-negative bacteria. Lyz1 and Lyz2 are equally effective in killing Gram-positive bacteria. {ECO:0000255|PROSITE-ProRule:PRU00680, ECO:0000269|PubMed:14977423}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Monomer. TISSUE SPECIFICITY: Expressed strongly only in small intestine. +Q8K3C3 LZIC_MOUSE Protein LZIC (Leucine zipper and CTNNBIP1 domain-containing protein) (Leucine zipper and ICAT homologous domain-containing protein) 190 21,537 Chain (1); Coiled coil (1) SUBUNIT: Does not interact with CTNNB1. +Q9D0E3 LYSM1_MOUSE LysM and putative peptidoglycan-binding domain-containing protein 1 226 24,814 Chain (1); Domain (1); Modified residue (7) +P50538 MAD1_MOUSE Max dimerization protein 1 (Max dimerizer 1) (Protein MAD) 227 25,562 Chain (1); Domain (1); Motif (1); Sequence conflict (2) FUNCTION: Transcriptional repressor. MAD binds with MAX to form a sequence-specific DNA-binding protein complex which recognizes the core sequence 5'-CAC[GA]TG-3'. MAD thus antagonizes MYC transcriptional activity by competing for MAX. PTM: Ubiquitinated by BIRC2/c-IAP1, leading to its subsequent degradation by the proteasome. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Efficient DNA binding requires dimerization with another bHLH protein. Binds DNA as a heterodimer with MAX. Interacts with RNF17. {ECO:0000269|PubMed:10597267}. +P54843 MAF_MOUSE Transcription factor Maf (Proto-oncogene c-Maf) (V-maf musculoaponeurotic fibrosarcoma oncogene homolog) 370 38,435 Alternative sequence (2); Chain (1); Compositional bias (3); Cross-link (3); Domain (1); Mutagenesis (3); Region (3); Sequence conflict (5) FUNCTION: Acts as a transcriptional activator or repressor. When overexpressed, represses anti-oxidant response element (ARE)-mediated transcription. Involved either as an oncogene or as a tumor suppressor, depending on the cell context. Binds to the ARE sites of detoxifying enzyme gene promoters (By similarity). Involved in embryonic lens fiber cell development. Recruits the transcriptional coactivators CREBBP and/or EP300 to crystallin promoters leading to up-regulation of crystallin gene during lens fiber cell differentiation. Activates the expression of IL4 in T helper 2 (Th2) cells. Increases T-cell susceptibility to apoptosis by interacting with MYB and decreasing BCL2 expression. Together with PAX6, transactivates strongly the glucagon gene promoter through the G1 element. Activates transcription of the CD13 proximal promoter in endothelial cells. Represses transcription of the CD13 promoter in early stages of myelopoiesis by affecting the ETS1 and MYB cooperative interaction. Involved in the initial chondrocyte terminal differentiation and the disappearance of hypertrophic chondrocytes during endochondral bone development. Binds to the sequence 5'-[GT]G[GC]N[GT]NCTCAGNN-3' in the L7 promoter. Binds to the T-MARE (Maf response element) sites of lens-specific alpha- and beta-crystallin gene promoters. Binds element G1 on the glucagon promoter. Binds an AT-rich region adjacent to the TGC motif (atypical Maf response element) in the CD13 proximal promoter in endothelial cells. It may interact with additional basic-zipper proteins that determine a subtype of Maf-responsive element binding. {ECO:0000250, ECO:0000269|PubMed:10097114, ECO:0000269|PubMed:10383433, ECO:0000269|PubMed:10403649, ECO:0000269|PubMed:10603348, ECO:0000269|PubMed:11943779, ECO:0000269|PubMed:14512017, ECO:0000269|PubMed:17823980, ECO:0000269|PubMed:17897790, ECO:0000269|PubMed:17901057, ECO:0000269|PubMed:19143053, ECO:0000269|PubMed:9070273, ECO:0000269|PubMed:9566892}. PTM: Ubiquitinated, leading to its degradation by the proteasome. Ubiquitination is triggered by glucocorticoids (By similarity). {ECO:0000250}.; PTM: Phosphorylated by GSK3 and MAPK13 on serine and threonine residues (By similarity). The phosphorylation status can serve to either stimulate or inhibit transcription. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Homodimer or heterodimer with other bHLH-Zip transcription factors. Binds DNA as a homodimer or as a heterodimer. Heterotetramer of two MAF and two USF2. Interacts with PAX6; the interaction is direct. Interacts with MYB; interaction takes place weakly in normal T-cells and increases in T-cells following stimulation through the TCR engagement. Interacts with MYB; the ternary complex formed with MYB and the CD13 promoter is regulated in response to differentiating signals. Interacts with USF2; the interaction inhibits its DNA-binding activity on the L7 promoter. Interacts with CREBBP, EP300 and ETS1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in tubules of the renal cortex and hepatocytes. Expressed in the lens (at protein level). Expressed in pancreatic islets and endothelial cells. {ECO:0000269|PubMed:15249232, ECO:0000269|PubMed:17897790, ECO:0000269|PubMed:17901057}. +Q9CWV4 MAGBG_MOUSE Melanoma-associated antigen B16 (MAGE-B16 antigen) 363 40,893 Chain (1); Compositional bias (1); Domain (1); Sequence conflict (1) +P54841 MAFB_MOUSE Transcription factor MafB (Maf-B) (Kreisler) (Segmentation protein Kr) (Transcription factor Maf-1) (V-maf musculoaponeurotic fibrosarcoma oncogene homolog B) 323 35,809 Chain (1); Compositional bias (2); Cross-link (2); Domain (1); Helix (3); Mutagenesis (4); Region (2); Sequence conflict (1); Turn (1) FUNCTION: Acts as a transcriptional activator or repressor. Plays a pivotal role in regulating lineage-specific hematopoiesis by repressing ETS1-mediated transcription of erythroid-specific genes in myeloid cells. Required for monocytic, macrophage, osteoclast, podocyte and islet beta cell differentiation. Involved in renal tubule survival and F4/80 maturation. Activates the insulin and glucagon promoters. Together with PAX6, transactivates weakly the glucagon gene promoter through the G1 element. SUMO modification controls its transcriptional activity and ability to specify macrophage fate. Binds element G1 on the glucagon promoter. Involved either as an oncogene or as a tumor suppressor, depending on the cell context. {ECO:0000250|UniProtKB:Q9Y5Q3, ECO:0000269|PubMed:10790365, ECO:0000269|PubMed:16443760, ECO:0000269|PubMed:16847325, ECO:0000269|PubMed:17548468, ECO:0000269|PubMed:17901057, ECO:0000269|PubMed:18199433, ECO:0000269|PubMed:19143053, ECO:0000269|PubMed:19440205}. PTM: Sumoylated. Sumoylation on Lys-32 and Lys-297 stimulates its transcriptional repression activity and promotes macrophage differentiation from myeloid progenitors. {ECO:0000269|PubMed:17548468}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:15135046}. SUBUNIT: Homodimer or heterodimer with other bHLH-Zip transcription factors. Forms homodimers and heterodimers with FOS, FOSB and FOSL2, but not with JUN proteins (JUN, JUNB and JUND). Interacts with the intracellular cytoplasmic domain of LRP1 (LRPICD); the interaction results in a moderate reduction of MAFB transcriptional potential (By similarity). Binds DNA as a homodimer or a heterodimer. Interacts with PAX6; the interaction is direct. Interacts with ETS1 and LRP1. {ECO:0000250, ECO:0000269|PubMed:10790365, ECO:0000269|PubMed:15135046, ECO:0000269|PubMed:17901057}. DOMAIN: The leucine-zipper domain is involved in the interaction with LRPICD. TISSUE SPECIFICITY: Expressed in pancreatic alpha-cells (glucagon-positive cells), in podocytes of the kidney and macrophages (at protein level). Most abundant in kidney, gut, lung and brain. {ECO:0000269|PubMed:16443760, ECO:0000269|PubMed:16847325, ECO:0000269|PubMed:17901057}. +Q9WUL6 M3K14_MOUSE Mitogen-activated protein kinase kinase kinase 14 (EC 2.7.11.25) (NF-kappa-beta-inducing kinase) (Serine/threonine-protein kinase NIK) 942 103,080 Active site (1); Beta strand (13); Binding site (1); Chain (1); Domain (1); Helix (14); Modified residue (1); Mutagenesis (1); Nucleotide binding (1); Region (1); Turn (8) FUNCTION: Lymphotoxin beta-activated kinase which seems to be exclusively involved in the activation of NF-kappa-B and its transcriptional activity. Promotes proteolytic processing of NFKB2/P100, which leads to activation of NF-kappa-B via the non-canonical pathway. Could act in a receptor-selective manner. {ECO:0000269|PubMed:11239468}. PTM: Phosphorylation at Thr-561 is required to activates its kinase activity and 'Lys-63'-linked polyubiquitination. Phosphorylated by CHUK/IKKA leading to MAP3K14 destabilization (By similarity). Autophosphorylated. {ECO:0000250}.; PTM: Ubiquitinated. Undergoes both 'Lys-48'- and 'Lys-63'-linked polyubiquitination. 'Lys-48'-linked polyubiquitination leads to its degradation by the proteasome, while 'Lys-63'-linked polyubiquitination stabilizes and activates it (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Interacts with TRAF2, TRAF3, TRAF5, TRAF6, IKKA and NF-kappa-B2/P100. Interacts with PELI3. Interacts with NIBP; the interaction is direct. Interacts with ARRB1 and ARRB2. Interacts with GRB10. Interacts with ZFP91 (By similarity). {ECO:0000250}. +Q3UZP0 MALD2_MOUSE MARVEL domain-containing protein 2 (Tricellulin) 555 63,662 Chain (1); Coiled coil (1); Compositional bias (1); Domain (1); Erroneous initiation (1); Modified residue (5); Sequence conflict (1); Topological domain (5); Transmembrane (4) TRANSMEM 192 212 Helical. {ECO:0000255}.; TRANSMEM 252 272 Helical. {ECO:0000255}.; TRANSMEM 289 309 Helical. {ECO:0000255}.; TRANSMEM 339 359 Helical. {ECO:0000255}. TOPO_DOM 1 191 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 213 251 Extracellular. {ECO:0000255}.; TOPO_DOM 273 288 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 310 338 Extracellular. {ECO:0000255}.; TOPO_DOM 360 555 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a role in the formation of tricellular tight junctions and of epithelial barriers (PubMed:16365161). Required for normal hearing via its role in the separation of the endolymphatic and perilymphatic spaces of the organ of Corti in the inner ear, and for normal survival of hair cells in the organ of Corti (PubMed:26677943). {ECO:0000269|PubMed:16365161, ECO:0000269|PubMed:26677943}. PTM: Phosphorylated. {ECO:0000269|PubMed:16365161}.; PTM: Ubiquitinated by ITCH; but this ubiquitination does not lead to proteasomal degradation. {ECO:0000250|UniProtKB:Q8N4S9}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16365161, ECO:0000269|PubMed:17186462, ECO:0000269|PubMed:26677943}; Multi-pass membrane protein {ECO:0000305}. Cell junction, tight junction {ECO:0000269|PubMed:16365161, ECO:0000269|PubMed:17186462, ECO:0000269|PubMed:26677943}. Note=Found at tricellular contacts. {ECO:0000269|PubMed:16365161, ECO:0000269|PubMed:17186462, ECO:0000269|PubMed:26677943}. SUBUNIT: Interacts with TJP1. Interacts with the ubiquitin ligase ITCH. {ECO:0000250|UniProtKB:Q8N4S9}. TISSUE SPECIFICITY: Detected in small intestine, stomach and kidney, in epithelial cells (PubMed:16365161). Detected in pancreas, retina and lung, and in stria vascularis, utricle and the organ of Conti in the inner ear (at protein level) (PubMed:26677943, PubMed:17186462). Predominantly detected in small intestine, lung and kidney, with lower levels in liver, testis and brain (PubMed:16365161). {ECO:0000269|PubMed:16365161, ECO:0000269|PubMed:17186462, ECO:0000269|PubMed:26677943}. +Q6P5G3 MBTD1_MOUSE MBT domain-containing protein 1 631 70,669 Alternative sequence (2); Chain (1); Erroneous initiation (1); Modified residue (1); Repeat (4); Zinc finger (1) FUNCTION: Putative Polycomb group (PcG) protein. PcG proteins maintain the transcriptionally repressive state of genes, probably via a modification of chromatin, rendering it heritably changed in its expressibility. Specifically binds to monomethylated and dimethylated 'Lys-20' on histone H4 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Monomer. {ECO:0000250}. +Q9D8U6 MCEM1_MOUSE Mast cell-expressed membrane protein 1 183 20,649 Chain (1); Glycosylation (1); Topological domain (2); Transmembrane (1) TRANSMEM 71 91 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 70 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 92 183 Extracellular. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. +Q9D1M4 MCA3_MOUSE Eukaryotic translation elongation factor 1 epsilon-1 (Elongation factor p18) (Multisynthase complex auxiliary component p18) 174 19,859 Chain (1); Coiled coil (1); Domain (1); Initiator methionine (1); Modified residue (2); Region (3) FUNCTION: Positive modulator of ATM response to DNA damage. {ECO:0000269|PubMed:15680327}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15680327}. Nucleus {ECO:0000269|PubMed:15680327}. Note=Cytoplasmic under growth arrest conditions. Translocated into the nucleus when growth resumes at S phase and following DNA damage. SUBUNIT: Part of a multisubunit complex that groups tRNA ligases for Arg (RARS), Asp (DARS), Gln (QARS), Ile (IARS), Leu (LARS), Lys (KARS), Met (MARS) the bifunctional ligase for Glu and Pro (EPRS) and the auxiliary subunits AIMP1/p43, AIMP2/p38 and EEF1E1/p18 (PubMed:12060739). Can interact simultaneously with MARS and EPRS. Forms a linear complex that contains MARS, EEF1E1, EPRS and AIMP2 that is at the core of the multisubunit complex. Interacts with ATM and ATR. The interaction with ATM, which takes place independently of TP53, is induced by DNA damage that may occur during genotoxic stress or cell growth. The interaction with ATR is enhanced by UV irradiation (By similarity). {ECO:0000250|UniProtKB:O43324, ECO:0000269|PubMed:12060739}. +Q64096 MCF2L_MOUSE Guanine nucleotide exchange factor DBS (DBL's big sister) (MCF2-transforming sequence-like protein) 1149 129,113 Beta strand (9); Chain (1); Coiled coil (1); Compositional bias (1); Domain (4); Helix (17); Modified residue (10); Repeat (1); Sequence conflict (2); Turn (7) FUNCTION: Guanine nucleotide exchange factor that catalyzes guanine nucleotide exchange on RHOA and CDC42, and thereby contributes to the regulation of RHOA and CDC42 signaling pathways (PubMed:17000758, PubMed:11889037, PubMed:12006984). Seems to lack activity with RAC1. Becomes activated and highly tumorigenic by truncation of the N-terminus (By similarity). {ECO:0000250|UniProtKB:Q63406, ECO:0000269|PubMed:11889037, ECO:0000269|PubMed:12006984}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17000758}. Cell membrane {ECO:0000269|PubMed:17000758}; Peripheral membrane protein {ECO:0000269|PubMed:17000758}; Cytoplasmic side {ECO:0000269|PubMed:17000758}. SUBUNIT: Interacts with GTP-bound RAC1 (By similarity). Interacts with CDC42 (PubMed:11889037). Interacts with RHOA (PubMed:12006984). Interacts with CCPG1, which results in specific inhibition of its exchange activity toward RHOA, but does not affect its activity on CDC42 (PubMed:17000758). {ECO:0000250|UniProtKB:Q63406, ECO:0000269|PubMed:17000758}. DOMAIN: The DH domain is involved in interaction with CCPG1. {ECO:0000269|PubMed:17000758}.; DOMAIN: The CRAL-TRIO domain mediates interaction with various inositol phospholipids, such as phosphatidylinositol 3-phosphate (PI3P), phosphatidylinositol 4-phosphate (PI4P) and phosphatidylinositol 5-phosphate (PI5P). {ECO:0000250|UniProtKB:O15068}. TISSUE SPECIFICITY: Expressed at low levels in several hemopoietic cell lines and in thymus and spleen, and at higher levels in other tissues, particularly in brain. {ECO:0000269|PubMed:7862449}. +O55236 MCE1_MOUSE mRNA-capping enzyme (HCE) (MCE1) [Includes: Polynucleotide 5'-triphosphatase (TPase) (mRNA 5'-triphosphatase) (EC 3.1.3.33); mRNA guanylyltransferase (EC 2.7.7.50) (GTP--RNA guanylyltransferase) (GTase)] 597 68,684 Active site (2); Beta strand (19); Binding site (2); Chain (1); Compositional bias (1); Helix (20); Mutagenesis (20); Nucleotide binding (3); Region (3); Turn (5) FUNCTION: Bifunctional mRNA-capping enzyme exhibiting RNA 5'-triphosphatase activity in the N-terminal part and mRNA guanylyltransferase activity in the C-terminal part. Catalyzes the first two steps of cap formation: by removing the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end, and by transferring the gmp moiety of GTP to the 5'-diphosphate terminus. {ECO:0000269|PubMed:21683636, ECO:0000269|PubMed:9371772}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with SUPT5H and RNMT (By similarity). Interacts with POLR2A (via C-terminus); this enhances guanylyltransferase activity. Binds (via GTase domain) to the elongating phosphorylated form of RNA polymerase II; can form direct interactions with the phosphorylated POLR2A C-terminal domain and indirect interactions via bound RNA. {ECO:0000250, ECO:0000269|PubMed:21683636, ECO:0000269|PubMed:9371772, ECO:0000269|PubMed:9407024}. +Q8K3A9 MEPCE_MOUSE 7SK snRNA methylphosphate capping enzyme (MePCE) (EC 2.1.1.-) 666 72,050 Binding site (1); Chain (1); Compositional bias (1); Cross-link (1); Domain (1); Erroneous initiation (1); Frameshift (1); Modified residue (14); Region (3); Sequence conflict (3) FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that adds a methylphosphate cap at the 5'-end of 7SK snRNA, leading to stabilize it. {ECO:0000250|UniProtKB:Q7L2J0}. SUBUNIT: Component of the 7SK snRNP complex at least composed of P-TEFb (composed of CDK9 and CCNT1/cyclin-T1), HEXIM1, HEXIM2, MEPCE/BCDIN3, SART3 proteins and 7SK and U6 snRNAs. Interacts with METTL16. {ECO:0000250|UniProtKB:Q7L2J0}. +P97309 MESP1_MOUSE Mesoderm posterior protein 1 243 26,386 Chain (1); Domain (1); Motif (1); Sequence conflict (2) FUNCTION: Transcription factor. Plays a role in the epithelialization of somitic mesoderm and in the development of cardiac mesoderm. Defines the rostrocaudal patterning of the somites by participating in distinct Notch pathways. {ECO:0000269|PubMed:15677726, ECO:0000269|PubMed:17306789}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: No expression was detected in adult tissues except the testis. Expression in the testis was regulated developmentally; expressed 2 weeks after birth, and increases, reaching the full expression level in mature testes. {ECO:0000269|PubMed:8787751}. +O08574 MESP2_MOUSE Mesoderm posterior protein 2 370 39,789 Chain (1); Compositional bias (1); Domain (1); Mutagenesis (2); Region (1); Sequence conflict (3) FUNCTION: Transcription factor with important role in somitogenesis. Defines the rostrocaudal patterning of the somite by participating in distinct Notch pathways. Regulates also the FGF signaling pathway. Specifies the rostral half of the somites. Generates rostro-caudal polarity of somites by down-regulating in the presumptive rostral domain DLL1, a Notch ligand. Participates in the segment border formation by activating in the anterior presomitic mesoderm LFNG, a negative regulator of DLL1-Notch signaling. Acts as a strong suppressor of Notch activity. Together with MESP1 is involved in the epithelialization of somitic mesoderm and in the development of cardiac mesoderm. May play a role with Tcf15 in the differentiation of myotomal and sclerotomal cells by regulating Pax family genes. Controls also the expression of the protocadherin PCDH8/PAPC, EPHA4, RIPPLY2, NOTCH2, FGFR1, and CER1. Binds to the E-boxes within the EPH4A and RIPPLY2 enhancers. {ECO:0000269|PubMed:10887078, ECO:0000269|PubMed:10932180, ECO:0000269|PubMed:12591245, ECO:0000269|PubMed:12900443, ECO:0000269|PubMed:15677726, ECO:0000269|PubMed:15902259, ECO:0000269|PubMed:16728472, ECO:0000269|PubMed:17306789, ECO:0000269|PubMed:17477400, ECO:0000269|PubMed:9242490}. PTM: Degraded by the proteasome.; PTM: Phosphorylated. {ECO:0000269|PubMed:16996494}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:15902259, ECO:0000269|PubMed:16996494}. +Q91YR5 MET13_MOUSE Methyltransferase-like protein 13 (EC 2.1.1.-) 698 78,757 Alternative sequence (4); Chain (1); Erroneous initiation (1); Modified residue (2); Sequence conflict (1) SUBUNIT: Part of a tripartite complex containing GAB1, METTL13 and SPRY2. Interacts with GAB1. Interacts with SPRY2. {ECO:0000250|UniProtKB:Q8N6R0}. TISSUE SPECIFICITY: Expressed in the inner ear. Expression is detected in the cochlear duct, spiral limbus region, efferent and afferent nerves, and in spiral ganglion neurons. {ECO:0000269|PubMed:29408807}. +Q8BG51 MIRO1_MOUSE Mitochondrial Rho GTPase 1 (MIRO-1) (EC 3.6.5.-) (Ras homolog gene family member T1) 631 72,242 Alternative sequence (3); Calcium binding (2); Chain (1); Domain (4); Erroneous gene model prediction (1); Erroneous initiation (2); Nucleotide binding (6); Sequence conflict (5); Topological domain (2); Transmembrane (1) TRANSMEM 606 628 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 1 605 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 629 631 Cytoplasmic. {ECO:0000255}. FUNCTION: Mitochondrial GTPase involved in mitochondrial trafficking. Probably involved in control of anterograde transport of mitochondria and their subcellular distribution (By similarity). {ECO:0000250}. PTM: Ubiquitinated by PRKN during mitophagy, leading to its degradation and enhancement of mitophagy. Deubiquitinated by USP30 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Note=Colocalizes with MGARP and RHOT2 at the mitochondria. {ECO:0000250}. SUBUNIT: Interacts with the kinesin-binding proteins TRAK1/OIP106 and TRAK2/GRIF1, forming a link between mitochondria and the trafficking apparatus of the microtubules (By similarity). Interacts with ARMCX1 (PubMed:28009275). Found in a complex with KIF5B, OGT, RHOT2 and TRAK1 (By similarity). {ECO:0000250|UniProtKB:Q8IXI2, ECO:0000269|PubMed:28009275}. +Q08874 MITF_MOUSE Microphthalmia-associated transcription factor 526 58,605 Alternative sequence (8); Chain (1); Coiled coil (1); Cross-link (2); Domain (1); Helix (4); Modified residue (5); Mutagenesis (1); Natural variant (9); Region (3); Sequence conflict (7) FUNCTION: Transcription factor that regulates the expression of genes with essential roles in cell differentiation, proliferation and survival. Binds to M-boxes (5'-TCATGTG-3') and symmetrical DNA sequences (E-boxes) (5'-CACGTG-3') found in the promoters of target genes, such as BCL2 and tyrosinase (TYR) (PubMed:23207919). Plays an important role in melanocyte development by regulating the expression of tyrosinase (TYR) and tyrosinase-related protein 1 (TYRP1). Plays a critical role in the differentiation of various cell types, such as neural crest-derived melanocytes, mast cells, osteoclasts and optic cup-derived retinal pigment epithelium. {ECO:0000250|UniProtKB:O75030, ECO:0000269|PubMed:23207919}. PTM: Phosphorylation at Ser-405 significantly enhances the ability to bind the tyrosinase promoter. Phosphorylated at Ser-180 and Ser-516 following KIT signaling, trigerring a short live activation: Phosphorylation at Ser-180 and Ser-516 by MAPK and RPS6KA1, respectively, activate the transcription factor activity but also promote ubiquitination and subsequent degradation by the proteasome (By similarity). {ECO:0000250|UniProtKB:O75030}.; PTM: Ubiquitinated following phosphorylation at Ser-180, leading to subsequent degradation by the proteasome. Deubiquitinated by USP13, preventing its degradation (By similarity). {ECO:0000250|UniProtKB:O75030}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:8622664}. SUBUNIT: Homodimer or heterodimer; dimerization is mediated via the coiled coil region (PubMed:23207919). Efficient DNA binding requires dimerization with another bHLH protein (PubMed:23207919). Binds DNA in the form of homodimer or heterodimer with either TFE3, TFEB or TFEC (By similarity). Binds DNA as a homodimer (in vitro) (PubMed:23207919). Interacts with KARS (PubMed:14975237). Identified in a complex with HINT1 and CTNNB1 (By similarity). {ECO:0000250|UniProtKB:O75030, ECO:0000269|PubMed:14975237, ECO:0000269|PubMed:23207919}. DOMAIN: The leucine zipper region is part of a larger coiled coil. {ECO:0000305|PubMed:23207919}. TISSUE SPECIFICITY: In the adult, expressed at high levels in the heart, skin, skeletal muscle, intestine, stomach, kidney, ovary, lung, spleen and brain. In the embryo, expressed in developing eye, ear, skin and heart. Isoform M is expressed in melanocytes and also in the embryonic and adult heart while isoform A and isoform H are more widely expressed. {ECO:0000269|PubMed:8343963}. DISEASE: Note=Defects in Mitf are the cause of microphthalmia (mi), a condition characterized by loss of pigmentation; reduced eye size; failure of secondary bone resorption; reduced numbers of mast cells; early onset of deafness, and which gives rise to a number of different phenotypes. Among them, microphthalmia-eyeless white (mi-ew) has a normal appearance at the heterozygous state, but shows white coat; eyes almost absent and eyelids never open at homozygosity. Microphthalmia-black and white spot (mi-bws) is normal at heterozygosity, and presents white spots and black eyes at homozygous state. Microphthalmia-white (mi-wh) has reduced coat color and eye pigmentation; spots on toes, tail and belly; inner ear defects at heterozygosity, and at homozygosity shows white coat; eyes small and inner iris slightly pigmented; spinal ganglia, adrenal medulla and dermis smaller than normal, and inner ear defects. Microphthalmia-vitiligo (mi-vi) has normal phenotype at heterozygosity, but shows gradual depigmentation of coat, skin and eyes; and retinal degeneration at homozygosity. Microphthalmia-spotted (mi-sp) shows normal phenotype; at homozygosity, however, tyrosinase activity in skin is reduced. Microphthalmia-defective irism (mi-di) has reduced retinal pigmentation at heterozygosity and shows white coat; eyes of reduced sized and possible mild osteoporosis at homozygosity. Microphthalmia-cloudy eyed (mi-ce) has a normal appearance at the heterozygous state, but shows white coat; eyes of reduced size and unpigmented at homozygosity. Microphthalmia-red-eyed white (mi-rw) has a normal appearance at the homozygous state, but shows white coat with one or more pigmented spots around the head/and or tail; eyes are small and red at heterozygosity. Microphthalmia-black-eyed white (mi-bw) shows a white coat but normal sized eyes which reamin black at homozygosity. {ECO:0000269|PubMed:10400990, ECO:0000269|PubMed:7874168}. +Q61831 MK10_MOUSE Mitogen-activated protein kinase 10 (MAP kinase 10) (MAPK 10) (EC 2.7.11.24) (MAP kinase p49 3F12) (Stress-activated protein kinase JNK3) (c-Jun N-terminal kinase 3) 464 52,532 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Domain (1); Lipidation (2); Modified residue (2); Motif (1); Nucleotide binding (1); Sequence conflict (4) FUNCTION: Serine/threonine-protein kinase involved in various processes such as neuronal proliferation, differentiation, migration and programmed cell death. Extracellular stimuli such as proinflammatory cytokines or physical stress stimulate the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. In this cascade, two dual specificity kinases MAP2K4/MKK4 and MAP2K7/MKK7 phosphorylate and activate MAPK10/JNK3. In turn, MAPK10/JNK3 phosphorylates a number of transcription factors, primarily components of AP-1 such as JUN and ATF2 and thus regulates AP-1 transcriptional activity. Plays regulatory roles in the signaling pathways during neuronal apoptosis. Phosphorylates the neuronal microtubule regulator STMN2. Acts in the regulation of the amyloid-beta precursor protein/APP signaling during neuronal differentiation by phosphorylating APP. Participates also in neurite growth in spiral ganglion neurons. Phosphorylates the CLOCK-ARNTL/BMAL1 heterodimer and plays a role in the photic regulation of the circadian clock (PubMed:22441692). {ECO:0000269|PubMed:20418776, ECO:0000269|PubMed:21554942, ECO:0000269|PubMed:22441692, ECO:0000269|PubMed:9349820}. PTM: Dually phosphorylated on Thr-221 and Tyr-223 by MAP2K4 and MAP2K7, which activates the enzyme. MAP2K7 shows a strong preference for Thr-221 while MAP2K4 phosphorylates Tyr-223 preferentially. Weakly autophosphorylated on threonine and tyrosine residues in vitro (By similarity). {ECO:0000250}.; PTM: Palmitoylation regulates subcellular location and axonal development. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17724133}. Membrane {ECO:0000269|PubMed:17724133}; Lipid-anchor {ECO:0000269|PubMed:17724133}. Nucleus {ECO:0000269|PubMed:17724133}. Mitochondrion {ECO:0000269|PubMed:17724133}. Note=Palmitoylation regulates MAPK10 trafficking to cytoskeleton (By similarity). Recruited to the mitochondria in the presence of SARM1. {ECO:0000250}. SUBUNIT: Binds to at least four scaffolding proteins, MAPK8IP1/JIP1, MAPK8IP2/JIP2, MAPK8IP3/JIP3/JSAP1 and SPAG9/MAPK8IP4/JIP4. These proteins also bind other components of the JNK signaling pathway (By similarity). Interacts with HDAC9 and MAPKBP1. Interacts with ARRB2; the interaction enhances MAPK10 activation by MAP3K5 (By similarity). Interacts with SARM1. {ECO:0000250, ECO:0000250|UniProtKB:P49187, ECO:0000269|PubMed:10471813, ECO:0000269|PubMed:16611996, ECO:0000269|PubMed:17724133}. DOMAIN: The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases. TISSUE SPECIFICITY: Brain (at protein level). Expressed specifically in neurons of the hippocampus, cortex, cerebellum, brainstem, and spinal cord. Seems to be also found in testis, and very weakly in the heart. {ECO:0000269|PubMed:22441692}. +Q8BH93 MISSL_MOUSE MAPK-interacting and spindle-stabilizing protein-like (Mitogen-activated protein kinase 1-interacting protein 1-like) 242 23,885 Chain (1); Compositional bias (1); Initiator methionine (1); Modified residue (4); Sequence conflict (1) +Q9Z1B7 MK13_MOUSE Mitogen-activated protein kinase 13 (MAP kinase 13) (MAPK 13) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 delta) (MAP kinase p38 delta) (Stress-activated protein kinase 4) 366 42,072 Active site (1); Binding site (1); Chain (1); Domain (1); Modified residue (3); Motif (1); Nucleotide binding (1); Sequence conflict (1) FUNCTION: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK13 is one of the four p38 MAPKs which play an important role in the cascades of cellular responses evoked by extracellular stimuli such as proinflammatory cytokines or physical stress leading to direct activation of transcription factors such as ELK1 and ATF2. Accordingly, p38 MAPKs phosphorylate a broad range of proteins and it has been estimated that they may have approximately 200 to 300 substrates each. MAPK13 is one of the less studied p38 MAPK isoforms. Some of the targets are downstream kinases such as MAPKAPK2, which are activated through phosphorylation and further phosphorylate additional targets. Plays a role in the regulation of protein translation by phosphorylating and inactivating EEF2K. Involved in cytoskeletal remodeling through phosphorylation of MAPT and STMN1. Mediates UV irradiation induced up-regulation of the gene expression of CXCL14. Plays an important role in the regulation of epidermal keratinocyte differentiation, apoptosis and skin tumor development. Phosphorylates the transcriptional activator MYB in response to stress which leads to rapid MYB degradation via a proteasome-dependent pathway. MAPK13 also phosphorylates and down-regulates PRKD1 during regulation of insulin secretion in pancreatic beta cells. {ECO:0000269|PubMed:19135240, ECO:0000269|PubMed:21558321}. PTM: Dually phosphorylated on Thr-180 and Tyr-182 by MAP2K3/MKK3, MAP2K4/MKK4, MAP2K6/MKK6 and MAP2K7/MKK7, which activates the enzyme. Dephosphorylated by dual specificity phosphatase DUSP1 (By similarity). {ECO:0000250}. SUBUNIT: Interacts with MAPK8IP2. {ECO:0000269|PubMed:11378392}. DOMAIN: The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases. +P03893 NU2M_MOUSE NADH-ubiquinone oxidoreductase chain 2 (EC 7.1.1.2) (NADH dehydrogenase subunit 2) 345 38,752 Beta strand (5); Chain (1); Helix (23); Sequence conflict (3); Transmembrane (10); Turn (7) TRANSMEM 1 21 Helical. {ECO:0000255}.; TRANSMEM 25 45 Helical. {ECO:0000255}.; TRANSMEM 56 76 Helical. {ECO:0000255}.; TRANSMEM 92 114 Helical. {ECO:0000255}.; TRANSMEM 149 171 Helical. {ECO:0000255}.; TRANSMEM 178 198 Helical. {ECO:0000255}.; TRANSMEM 200 220 Helical. {ECO:0000255}.; TRANSMEM 241 261 Helical. {ECO:0000255}.; TRANSMEM 274 294 Helical. {ECO:0000255}.; TRANSMEM 324 344 Helical. {ECO:0000255}. FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. +Q91Y86 MK08_MOUSE Mitogen-activated protein kinase 8 (MAP kinase 8) (MAPK 8) (EC 2.7.11.24) (Stress-activated protein kinase JNK1) (c-Jun N-terminal kinase 1) 384 44,229 Active site (1); Binding site (1); Chain (1); Domain (1); Modified residue (4); Motif (1); Nucleotide binding (1) FUNCTION: Serine/threonine-protein kinase involved in various processes such as cell proliferation, differentiation, migration, transformation and programmed cell death. Extracellular stimuli such as proinflammatory cytokines or physical stress stimulate the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. In this cascade, two dual specificity kinases MAP2K4/MKK4 and MAP2K7/MKK7 phosphorylate and activate MAPK8/JNK1. In turn, MAPK8/JNK1 phosphorylates a number of transcription factors, primarily components of AP-1 such as JUN, JDP2 and ATF2 and thus regulates AP-1 transcriptional activity. Phosphorylates the replication licensing factor CDT1, inhibiting the interaction between CDT1 and the histone H4 acetylase HBO1 to replication origins. Loss of this interaction abrogates the acetylation required for replication initiation. Promotes stressed cell apoptosis by phosphorylating key regulatory factors including p53/TP53 and Yes-associates protein YAP1. In T-cells, MAPK8 and MAPK9 are required for polarized differentiation of T-helper cells into Th1 cells. Contributes to the survival of erythroid cells by phosphorylating the antagonist of cell death BAD upon EPO stimulation. Mediates starvation-induced BCL2 phosphorylation, BCL2 dissociation from BECN1, and thus activation of autophagy. Phosphorylates STMN2 and hence regulates microtubule dynamics, controlling neurite elongation in cortical neurons. In the developing brain, through its cytoplasmic activity on STMN2, negatively regulates the rate of exit from multipolar stage and of radial migration from the ventricular zone (By similarity). Phosphorylates several other substrates including heat shock factor protein 4 (HSF4), the deacetylase SIRT1, ELK1, or the E3 ligase ITCH. Phosphorylates the CLOCK-ARNTL/BMAL1 heterodimer and plays a role in the regulation of the circadian clock (PubMed:22441692). Phosphorylates the heat shock transcription factor HSF1, suppressing HSF1-induced transcriptional activity (By similarity). Phosphorylates POU5F1, which results in the inhibition of POU5F1's transcriptional activity and enhances its proteosomal degradation (PubMed:29153991). {ECO:0000250|UniProtKB:P45983, ECO:0000269|PubMed:10811224, ECO:0000269|PubMed:11602244, ECO:0000269|PubMed:19966288, ECO:0000269|PubMed:21297631, ECO:0000269|PubMed:22441692, ECO:0000269|PubMed:29153991, ECO:0000269|PubMed:9393873}. PTM: Phosphorylated by TAOK2 (By similarity). Dually phosphorylated on Thr-183 and Tyr-185 by MAP2K7 and MAP2K4, which activates the enzyme (PubMed:11562351). May be phosphorylated at Thr-183 and Tyr-185 by MAP3K1/MEKK1 (PubMed:17761173). {ECO:0000250|UniProtKB:P45983, ECO:0000269|PubMed:11562351, ECO:0000269|PubMed:17761173}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16618812}. Nucleus {ECO:0000269|PubMed:29153991}. Note=Colocalizes with POU5F1 in the nucleus. {ECO:0000269|PubMed:29153991}. SUBUNIT: Binds to at least four scaffolding proteins, MAPK8IP1/JIP-1, MAPK8IP2/JIP-2, MAPK8IP3/JIP-3/JSAP1 and SPAG9/MAPK8IP4/JIP-4 (PubMed:10523642, PubMed:12391307, PubMed:11562351). These proteins also bind other components of the JNK signaling pathway. Forms a complex with MAPK8IP1 and ARHGEF28 (PubMed:14499478). Interacts with TP53 and WWOX (By similarity). Interacts with JAMP (PubMed:16166642). Interacts with NFATC4 (By similarity). Interacts with MECOM; regulates JNK signaling (By similarity). Interacts with PIN1; this interaction mediates MAPK8 conformational changes leading to the binding of MAPK8 to its substrates (By similarity). Interacts with HSF1 (via D domain and preferentially with hyperphosphorylated form); this interaction occurs under both normal growth conditions and immediately upon heat shock (By similarity). Interacts (phosphorylated form) with NFE2; the interaction phosphorylates NFE2 in undifferentiated cells (PubMed:19966288). Interacts with GRIPAP1 (By similarity). Interacts with POU5F1; phosphorylates POU5F1 at 'Ser-347' (PubMed:29153991). Found in a complex with SH3RF1, RAC1, MAP3K11/MLK3, MAP2K7/MKK7 and MAPK8IP1/JIP1 (PubMed:23963642). Found in a complex with SH3RF1, RAC2, MAP3K7/TAK1, MAP2K7/MKK7, MAPK8IP1/JIP1 and MAPK9/JNK2 (PubMed:27084103). {ECO:0000250|UniProtKB:P45983, ECO:0000250|UniProtKB:P49185, ECO:0000269|PubMed:10523642, ECO:0000269|PubMed:11562351, ECO:0000269|PubMed:12391307, ECO:0000269|PubMed:14499478, ECO:0000269|PubMed:16166642, ECO:0000269|PubMed:19966288, ECO:0000269|PubMed:23963642, ECO:0000269|PubMed:27084103, ECO:0000269|PubMed:29153991}. DOMAIN: The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases. TISSUE SPECIFICITY: Brain (at protein level). {ECO:0000269|PubMed:22441692}. +Q8CDB0 MKNK2_MOUSE MAP kinase-interacting serine/threonine-protein kinase 2 (EC 2.7.11.1) (MAP kinase signal-integrating kinase 2) (MAPK signal-integrating kinase 2) (Mnk2) 459 51,633 Active site (1); Alternative sequence (1); Binding site (2); Chain (1); Domain (1); Erroneous initiation (1); Frameshift (2); Metal binding (3); Modified residue (8); Motif (2); Mutagenesis (6); Nucleotide binding (1); Region (1); Sequence conflict (3) FUNCTION: Serine/threonine-protein kinase that phosphorylates SFPQ/PSF, HNRNPA1 and EIF4E. May play a role in the response to environmental stress and cytokines. Appears to regulate translation by phosphorylating EIF4E, thus increasing the affinity of this protein for the 7-methylguanosine-containing mRNA cap. Required for mediating PP2A-inhibition-induced EIF4E phosphorylation. Triggers EIF4E shuttling from cytoplasm to nucleus. Enhances the formation of EIF4F complex in pachytene spermatocytes, thus promoting mRNA translation during spermatogenesis. Displays a high basal kinase activity. Acts as a mediator of the suppressive effects of IFNgamma on hematopoiesis. Negative regulator for signals that control generation of arsenic trioxide As(2)O(3)-dependent apoptosis and anti-leukemic responses. Involved in anti-apoptotic signaling in response to serum withdrawal. {ECO:0000269|PubMed:11154262, ECO:0000269|PubMed:17689282, ECO:0000269|PubMed:17903173, ECO:0000269|PubMed:20574055, ECO:0000269|PubMed:20823271, ECO:0000269|PubMed:20927323, ECO:0000269|PubMed:9155017}. PTM: Dual phosphorylation of Thr-244 and Thr-249 activates the kinase. Phosphorylation of Thr-379 activates the kinase. Phosphorylated upon arsenic trioxide As(2)O(3) treatment. Phosphorylated by MAPK1/ERK2, MAPK11 and MAPK14 (By similarity). Dephosphorylated by PP2A. {ECO:0000250, ECO:0000269|PubMed:11154262}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, PML body {ECO:0000250}. SUBUNIT: Interacts with ESR2 and EIF4E in the nucleus (By similarity). Monomer. Interacts with the C-terminal regions of EIF4G1 and EIF4G2; this interaction is promoted when MAPK pathways are repressed but repressed upon ERK proteins activation. Also binds to dephosphorylated MAPK3/ERK1 and MAPK1/ERK2. Interaction with phosphorylated MAPK3/ERK1 and MAPK1/ERK2 protects it from dephosphorylation and inactivation. {ECO:0000250, ECO:0000269|PubMed:11154262, ECO:0000269|PubMed:16162500, ECO:0000269|PubMed:20823271, ECO:0000269|PubMed:9155017}. TISSUE SPECIFICITY: Ubiquitously expressed in all tissues examined, with high levels in skeletal muscle and low levels in brain. {ECO:0000269|PubMed:9155017}. +Q9QXP6 MKRN1_MOUSE E3 ubiquitin-protein ligase makorin-1 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase makorin-1) 481 53,008 Alternative sequence (2); Chain (1); Region (1); Zinc finger (5) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins. These substrates include FILIP1, p53/TP53, CDKN1A and TERT. Keeps cells alive by suppressing p53/TP53 under normal conditions, but stimulates apoptosis by repressing CDKN1A under stress conditions. Acts as a negative regulator of telomerase (By similarity). Has negative and positive effects on RNA polymerase II-dependent transcription. {ECO:0000250, ECO:0000269|PubMed:16785614}. PTM: Auto-ubiquitinated; which leads to proteasomal degradation. {ECO:0000250}. SUBUNIT: Interacts with p53/TP53 and CDKN1A. Interacts with TERT, modulating telomere length homeostasis (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in embryo, in specific cell types of the central nervous system, in brain with the strongest levels of expression in the mantle layers and in testis. Moderate to low levels in somatic tissues. {ECO:0000269|PubMed:10843807, ECO:0000269|PubMed:12721631, ECO:0000269|PubMed:12971993}. +Q60764 MKRN3_MOUSE Probable E3 ubiquitin-protein ligase makorin-3 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase makorin-3) (Zinc finger protein 127) 544 59,434 Chain (1); Region (1); Sequence conflict (3); Zinc finger (4) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in testis, brain, heart and kidney. Ubiquitously detected at low levels throughout the entire embryo, but expression is highest in the ventricular layers of the brain. {ECO:0000269|PubMed:10196368, ECO:0000269|PubMed:12971993}. +P12025 MK_MOUSE Midkine (MK) (Retinoic acid-induced differentiation factor) 140 15,434 Chain (1); Disulfide bond (5); Signal peptide (1) FUNCTION: Developmentally regulated, secreted growth factor homologous to pleiotrophin (PTN), which has heparin binding activity. Binds anaplastic lymphoma kinase (ALK) which induces ALK activation and subsequent phosphorylation of the insulin receptor substrate (IRS1), followed by the activation of mitogen-activated protein kinase (MAPK) and PI3-kinase, and the induction of cell proliferation (By similarity). Involved in neointima formation after arterial injury, possibly by mediating leukocyte recruitment. Also involved in early fetal adrenal gland development. {ECO:0000250, ECO:0000269|PubMed:10683378}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. SUBUNIT: Homodimer. Interacts with ALK. {ECO:0000250}. +Q8BZT5 LRC19_MOUSE Leucine-rich repeat-containing protein 19 364 41,573 Chain (1); Domain (1); Glycosylation (11); Repeat (5); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 265 285 Helical. {ECO:0000255}. TOPO_DOM 21 264 Extracellular. {ECO:0000255}.; TOPO_DOM 286 364 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q8CI70 LRC20_MOUSE Leucine-rich repeat-containing protein 20 184 20,809 Chain (1); Modified residue (1); Repeat (6) +Q2WF71 LRFN1_MOUSE Leucine-rich repeat and fibronectin type III domain-containing protein 1 (Synaptic adhesion-like molecule 2) (Synaptic differentiation-enhancing molecule 1) 766 81,945 Alternative sequence (3); Beta strand (20); Chain (1); Disulfide bond (1); Domain (4); Frameshift (1); Glycosylation (2); Helix (7); Modified residue (1); Motif (1); Mutagenesis (1); Repeat (7); Sequence conflict (5); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (4) TRANSMEM 537 557 Helical. {ECO:0000255}. TOPO_DOM 32 536 Extracellular. {ECO:0000255}.; TOPO_DOM 558 766 Cytoplasmic. {ECO:0000255}. FUNCTION: Promotes neurite outgrowth in hippocampal neurons. Involved in the regulation and maintenance of excitatory synapses. Induces the clustering of excitatory postsynaptic proteins, including DLG4, DLGAP1, GRIA1 and GRIN1. {ECO:0000269|PubMed:16828986, ECO:0000269|PubMed:18585462}. PTM: Glycosylated. {ECO:0000269|PubMed:16828986}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cell junction, synapse {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250}. Note=Detected in excitatory, but not inhibitory, synaptic plasma membrane. {ECO:0000250}. SUBUNIT: Can form heteromeric complexes with LRFN2, LRFN3, LRFN4 and LRFN5. Forms homomeric complexes, but not across cell junctions. Interacts with DLG4. Interacts also with DLG1, DLG2, and DLG3 (By similarity). Interacts with 2 AMPA receptor subunits GRIA1 and GRIA2 and NMDA receptor subunit GRIN1. {ECO:0000250, ECO:0000269|PubMed:16828986, ECO:0000269|PubMed:18227064}. DOMAIN: The PDZ-binding motif is required for neurite outgrowth promotion. This motif is also involved in DLG1-, DLG3- and DLG4-binding (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Predominantly expressed in the brain, with a weak, but broad expression in the cerebral cortex and diencephalic nuclei. Also detected in other parts of the central nervous system, including the olfactory bulb, pons, cerebellum, and medulla oblongata, as well as in the peripheral nervous system, such as the ganglia of cranial nerves and the dorsal root ganglion during gestation. {ECO:0000269|PubMed:16828986}. +Q80WG5 LRC8A_MOUSE Volume-regulated anion channel subunit LRRC8A (Leucine-rich repeat-containing protein 8A) 810 94,120 Beta strand (17); Chain (1); Disulfide bond (3); Glycosylation (2); Helix (23); Modified residue (5); Mutagenesis (1); Repeat (17); Topological domain (5); Transmembrane (4) TRANSMEM 23 45 Helical. {ECO:0000305|PubMed:29769723}.; TRANSMEM 124 146 Helical. {ECO:0000305|PubMed:29769723}.; TRANSMEM 263 285 Helical. {ECO:0000305|PubMed:29769723}.; TRANSMEM 320 342 Helical. {ECO:0000305|PubMed:29769723}. TOPO_DOM 1 22 Cytoplasmic. {ECO:0000305|PubMed:29769723}.; TOPO_DOM 46 123 Extracellular. {ECO:0000305|PubMed:29769723}.; TOPO_DOM 147 262 Cytoplasmic. {ECO:0000305|PubMed:29769723}.; TOPO_DOM 286 319 Extracellular. {ECO:0000305|PubMed:29769723}.; TOPO_DOM 343 810 Cytoplasmic. {ECO:0000305|PubMed:29769723}. FUNCTION: Essential component of the volume-regulated anion channel (VRAC, also named VSOAC channel), an anion channel required to maintain a constant cell volume in response to extracellular or intracellular osmotic changes (PubMed:29769723). The VRAC channel conducts iodide better than chloride and can also conduct organic osmolytes like taurine (By similarity). Mediates efflux of amino acids, such as aspartate and glutamate, in response to osmotic stress (By similarity). Required for channel activity, together with at least one other family member (LRRC8B, LRRC8C, LRRC8D or LRRC8E); channel characteristics depend on the precise subunit composition. Can form functional channels by itself (in vitro) (By similarity). Involved in B-cell development: required for the pro-B cell to pre-B cell transition (PubMed:14660746, PubMed:24752297). Also required for T-cell development (PubMed:24752297). {ECO:0000250|UniProtKB:Q8IWT6, ECO:0000269|PubMed:14660746, ECO:0000269|PubMed:24752297, ECO:0000269|PubMed:29769723}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q8IWT6}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24782309, ECO:0000269|PubMed:29769723}; Multi-pass membrane protein {ECO:0000269|PubMed:29769723}. Note=The leucine-rich repeat (LRR) domain is on the cytoplasmic side of the cell membrane. {ECO:0000269|PubMed:29769723}. SUBUNIT: Hexamer (PubMed:29769723). Heterohexamer; oligomerizes with other LRRC8 proteins (LRRC8B, LRRC8C, LRRC8D and/or LRRC8E) to form a heterohexamer (PubMed:24782309, PubMed:29769723). Can form homohexamers in vitro, but these have lower conductance than heterohexamers (PubMed:29769723). Detected in a channel complex that contains LRRC8A, LRRC8C and LRRC8E (By similarity). In vivo, the subunit composition may depend primarily on expression levels, and heterooligomeric channels containing various proportions of the different LRRC8 proteins may coexist (Probable). {ECO:0000250|UniProtKB:Q8IWT6, ECO:0000269|PubMed:24782309, ECO:0000269|PubMed:29769723, ECO:0000305}. TISSUE SPECIFICITY: Ubiquitously expressed. High levels detected in the bone marrow; lower levels found in peripheral blood cells. {ECO:0000269|PubMed:14660746, ECO:0000269|PubMed:15094057, ECO:0000269|PubMed:24725410, ECO:0000269|PubMed:24752297}. +Q66JT1 LRC8E_MOUSE Volume-regulated anion channel subunit LRRC8E (Leucine-rich repeat-containing protein 8E) 795 90,501 Chain (1); Disulfide bond (1); Glycosylation (2); Repeat (10); Sequence conflict (4); Topological domain (5); Transmembrane (4) TRANSMEM 23 43 Helical. {ECO:0000255}.; TRANSMEM 117 137 Helical. {ECO:0000255}.; TRANSMEM 265 285 Helical. {ECO:0000255}.; TRANSMEM 313 333 Helical. {ECO:0000255}. TOPO_DOM 1 22 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 44 116 Extracellular. {ECO:0000255}.; TOPO_DOM 138 264 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 286 312 Extracellular. {ECO:0000255}.; TOPO_DOM 334 795 Cytoplasmic. {ECO:0000255}. FUNCTION: Non-essential component of the volume-regulated anion channel (VRAC, also named VSOAC channel), an anion channel required to maintain a constant cell volume in response to extracellular or intracellular osmotic changes. The VRAC channel conducts iodide better than chloride and can also conduct organic osmolytes like taurine. Mediates efflux of amino acids, such as aspartate, in response to osmotic stress. Channel activity requires LRRC8A plus at least one other family member (LRRC8B, LRRC8C, LRRC8D or LRRC8E); channel characteristics depend on the precise subunit composition. {ECO:0000250|UniProtKB:Q6NSJ5}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6NSJ5}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q6NSJ5}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q6NSJ5}. Note=In the absence of LRRC8A, resides primarily in a cytoplasmic compartment, probably the endoplasmic reticulum. Requires LRRC8A for expression at the cell membrane. {ECO:0000250|UniProtKB:Q6NSJ5}. SUBUNIT: Heterohexamer. Oligomerizes with other LRRC8 proteins (LRRC8A, LRRC8C, LRRC8D and/or LRRC8B) to form a heterohexamer. Detected in a channel complex that contains LRRC8A, LRRC8C and LRRC8E. In vivo, the subunit composition may depend primarily on expression levels, and heterooligomeric channels containing various proportions of the different LRRC8 proteins may coexist. {ECO:0000250|UniProtKB:Q6NSJ5}. +Q8K2F8 LS14A_MOUSE Protein LSM14 homolog A (Protein FAM61A) (RNA-associated protein 55A) (mRAP55A) 462 50,546 Chain (1); Domain (1); Initiator methionine (1); Modified residue (8); Motif (2) FUNCTION: Essential for formation of P-bodies, cytoplasmic structures that provide storage sites for non-translating mRNAs. {ECO:0000250|UniProtKB:Q8ND56}. SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000250|UniProtKB:Q8ND56}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q8ND56}. SUBUNIT: Component of a ribonucleoprotein (RNP) complex. {ECO:0000250}. DOMAIN: The LSM14 domain and the RGG repeats are required for accumulation in P-bodies, and the region containing the FDF motif is responsible for cytoplasmic retention. {ECO:0000250}. +Q8CF66 LTOR4_MOUSE Ragulator complex protein LAMTOR4 (Late endosomal/lysosomal adaptor and MAPK and MTOR activator 4) [Cleaved into: Ragulator complex protein LAMTOR4, N-terminally processed] 99 10,678 Chain (2); Erroneous initiation (3); Initiator methionine (1); Modified residue (2); Sequence conflict (1) FUNCTION: As part of the Ragulator complex it is involved in amino acid sensing and activation of mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids. Activated by amino acids through a mechanism involving the lysosomal V-ATPase, the Ragulator functions as a guanine nucleotide exchange factor activating the small GTPases Rag. Activated Ragulator and Rag GTPases function as a scaffold recruiting mTORC1 to lysosomes where it is in turn activated (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Lysosome {ECO:0000250}. SUBUNIT: Part of the Ragulator complex composed of LAMTOR1, LAMTOR2, LAMTOR3, LAMTOR4 and LAMTOR5. LAMTOR4 and LAMTOR5 form a heterodimer that interacts, through LAMTOR1, with a LAMTOR2, LAMTOR3 heterodimer. The Ragulator complex interacts with both the mTORC1 complex and heterodimers constituted of the Rag GTPases RRAGA, RRAGB, RRAGC and RRAGD; regulated by amino acid availability. The Ragulator complex interacts with SLC38A9; the probable amino acid sensor. {ECO:0000250|UniProtKB:Q0VGL1}. +Q8C525 M21D2_MOUSE Protein MB21D2 (Mab-21 domain-containing protein 2) 428 48,477 Chain (1); Modified residue (4); Sequence conflict (2) +Q91YU6 LZTS2_MOUSE Leucine zipper putative tumor suppressor 2 (Protein LAPSER1) 671 72,578 Chain (1); Coiled coil (1); Compositional bias (1); Erroneous initiation (1); Modified residue (3); Motif (1); Region (3); Sequence conflict (5) FUNCTION: Negative regulator of katanin-mediated microtubule severing and release from the centrosome. Required for central spindle formation and the completion of cytokinesis. May negatively regulate axonal outgrowth by preventing the formation of microtubule bundles that are necessary for transport within the elongating axon. Negative regulator of the Wnt signaling pathway. Represses beta-catenin-mediated transcriptional activation by promoting the nuclear exclusion of beta-catenin. {ECO:0000255|HAMAP-Rule:MF_03026}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03026}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03026, ECO:0000269|PubMed:18490357}. Note=Localized to the centrosome throughout the cell cycle. Localized to the midbody in cells undergoing cytokinesis. {ECO:0000255|HAMAP-Rule:MF_03026}. SUBUNIT: Interacts with KATNB1. Also interacts with CTNNB1, gamma-tubulin and KIF23. {ECO:0000255|HAMAP-Rule:MF_03026}. +Q9DBT9 M2GD_MOUSE Dimethylglycine dehydrogenase, mitochondrial (EC 1.5.8.4) (ME2GLYDH) 869 97,255 Binding site (4); Chain (1); Modified residue (22); Nucleotide binding (4); Region (2); Sequence conflict (1); Transit peptide (1) Amine and polyamine degradation; betaine degradation; sarcosine from betaine: step 2/2. FUNCTION: Catalyzes the demethylation of N,N-dimethylglycine to sarcosine. Also has activity with sarcosine in vitro. {ECO:0000250|UniProtKB:Q63342}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q63342}. +Q61826 MADCA_MOUSE Mucosal addressin cell adhesion molecule 1 (MAdCAM-1) (mMAdCAM-1) 405 43,652 Alternative sequence (1); Chain (1); Disulfide bond (4); Domain (3); Glycosylation (3); Region (1); Sequence conflict (5); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 365 385 Helical. {ECO:0000255}. TOPO_DOM 22 364 Extracellular. {ECO:0000255}.; TOPO_DOM 386 405 Cytoplasmic. {ECO:0000255}. FUNCTION: Cell adhesion leukocyte receptor expressed by mucosal venules, helps to direct lymphocyte traffic into mucosal tissues including the Peyer patches and the intestinal lamina propria. It can bind both the integrin alpha-4/beta-7 and L-selectin, regulating both the passage and retention of leukocytes. Both isoform 1 and isoform 2 can adhere to integrin alpha-4/beta-7. Isoform 2, lacking the mucin-like domain, may be specialized in supporting integrin alpha-4/beta-7-dependent adhesion strengthening, independent of L-selectin binding. {ECO:0000269|PubMed:3340147, ECO:0000269|PubMed:7488084}. PTM: O-glycosylated; contains syalic acid. The Ser/Thr-rich mucin-like domain may provide possible sites for O-glycosylation. {ECO:0000269|PubMed:7505053}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Homodimer. {ECO:0000305}. TISSUE SPECIFICITY: Highly expressed on high endothelial venules (HEV) of organized intestinal lymphoid tissues like the Peyer patches and mesenteric lymph nodes, and in the lamina propria of the intestine. Some expression found in the spleen, and low levels of expression in the peripheral lymph nodes and the lactating mammary gland. No expression was detected in the liver, kidneys, lungs or in normal brain. Expressed as well in brain endothelioma cells, and mucosal tissues which are in a chronic state of inflammation, such as inflammed pancreas. {ECO:0000269|PubMed:3340147, ECO:0000269|PubMed:7693764, ECO:0000269|PubMed:8502297}. DISEASE: Note=Absence of Madcam1 in the spleen has been found in aly/aly mice, but normal expression is found in intestinal venules. This aberrant expression is a secondary defect and not the direct cause of aly alymphoplasia, an autosomal recessive mutation which induces total aplasia of lymph nodes and Peyer patches. {ECO:0000269|PubMed:9316640}. +Q4KL35 MAGIX_MOUSE PDZ domain-containing protein MAGIX 324 34,771 Chain (1); Domain (1); Modified residue (1); Sequence conflict (1) +Q91W89 MA2C1_MOUSE Alpha-mannosidase 2C1 (EC 3.2.1.24) (Alpha-D-mannoside mannohydrolase) (Mannosidase alpha class 2C member 1) (Neutral/cytosolic alpha-mannosidase) 1039 115,688 Active site (1); Chain (1); Metal binding (4) FUNCTION: Cleaves alpha 1,2-, alpha 1,3-, and alpha 1,6-linked mannose residues from glycoproteins. Involved in the degradation of free oligosaccharides in the cytoplasm. {ECO:0000269|PubMed:16904268, ECO:0000269|PubMed:24550399}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16904268}. TISSUE SPECIFICITY: Expressed in kidney and liver (at protein level) (PubMed:24550399). Widely expressed, with highest levels in lung, ovary and testis (PubMed:16904268). Also detected at lower levels in heart, brain, liver, spleen, kidney and thymus (PubMed:16904268). {ECO:0000269|PubMed:16904268, ECO:0000269|PubMed:24550399}. +A2A9R3 MAGB4_MOUSE Melanoma-associated antigen B4 556 60,922 Chain (1); Domain (1); Modified residue (1); Region (1); Repeat (15); Sequence conflict (7) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10706124}. TISSUE SPECIFICITY: Expressed in testis (at protein level). {ECO:0000269|PubMed:10706124}. +Q9D8B4 NDUAB_MOUSE NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11 (Complex I-B14.7) (CI-B14.7) (NADH-ubiquinone oxidoreductase subunit B14.7) 141 14,982 Chain (1); Erroneous initiation (1); Transmembrane (2) TRANSMEM 21 43 Helical. {ECO:0000255}.; TRANSMEM 58 80 Helical. {ECO:0000255}. FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. {ECO:0000250|UniProtKB:Q86Y39}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q86Y39}; Multi-pass membrane protein {ECO:0000255}; Matrix side {ECO:0000250|UniProtKB:Q86Y39}. SUBUNIT: Complex I is composed of 45 different subunits. {ECO:0000250|UniProtKB:Q86Y39}. +Q7TMF3 NDUAC_MOUSE NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12 (Complex I-B17.2) (CI-B17.2) (CIB17.2) (NADH-ubiquinone oxidoreductase subunit B17.2) 145 17,086 Beta strand (5); Chain (1); Erroneous initiation (1); Helix (4); Modified residue (1); Turn (2) FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. {ECO:0000250|UniProtKB:Q9UI09}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9UI09}; Peripheral membrane protein {ECO:0000255}; Matrix side {ECO:0000250|UniProtKB:Q9UI09}. SUBUNIT: Complex I is composed of 45 different subunits. {ECO:0000250|UniProtKB:Q9UI09}. +A2APY7 NDUF5_MOUSE Arginine-hydroxylase NDUFAF5, mitochondrial (EC 1.-.-.-) (NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 5) (Putative methyltransferase NDUFAF5) (EC 2.1.1.-) 343 38,405 Alternative sequence (1); Chain (1); Erroneous initiation (1); Transit peptide (1) FUNCTION: Arginine hydroxylase involved in the assembly of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I, MT-ND1) at early stages. Acts by mediating hydroxylation of 'Arg-111' of NDUFS7. May also have methyltransferase activity. {ECO:0000250|UniProtKB:Q5TEU4}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q5TEU4}. Note=Peripherally localized on the matrix face of the mitochondrial inner membrane. {ECO:0000250|UniProtKB:Q5TEU4}. SUBUNIT: Interacts with NDUFAF8, leading to stabilize NDUFAF5. Interacts with NDUFS7. {ECO:0000250|UniProtKB:Q5TEU4}. +Q9QXZ0 MACF1_MOUSE Microtubule-actin cross-linking factor 1 (Actin cross-linking family 7) 7354 831,878 Alternative sequence (3); Calcium binding (2); Chain (1); Compositional bias (5); Domain (6); Erroneous gene model prediction (2); Erroneous initiation (1); Modified residue (26); Region (3); Repeat (49); Sequence conflict (34) FUNCTION: Isoform 2: F-actin-binding protein which plays a role in cross-linking actin to other cytoskeletal proteins and also binds to microtubules (PubMed:16815997, PubMed:18854161, PubMed:21295697). Plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex (By similarity). Acts as a positive regulator of Wnt receptor signaling pathway and is involved in the translocation of AXIN1 and its associated complex (composed of APC, CTNNB1 and GSK3B) from the cytoplasm to the cell membrane (PubMed:16815997). Has actin-regulated ATPase activity and is essential for controlling focal adhesions (FAs) assembly and dynamics (PubMed:18854161). Interaction with CAMSAP3 at the minus ends of non-centrosomal microtubules tethers microtubules minus-ends to actin filaments, regulating focal adhesion size and cell migration (By similarity). May play role in delivery of transport vesicles containing GPI-linked proteins from the trans-Golgi network through its interaction with GOLGA4 (By similarity). Plays a key role in wound healing and epidermal cell migration (PubMed:21295697). Required for efficient upward migration of bulge cells in response to wounding and this function is primarily rooted in its ability to coordinate microtubule dynamics and polarize hair follicle stem cells (PubMed:21295697). {ECO:0000250|UniProtKB:Q9UPN3, ECO:0000269|PubMed:16815997, ECO:0000269|PubMed:18854161, ECO:0000269|PubMed:21295697}. PTM: Phosphorylated on serine residues in the C-terminal tail by GSK3B. Phosphorylation inhibits microtubule-binding and this plays a critical role in bulge stem cell migration and skin wound repair. Wnt-signaling can repress phosphorylation. {ECO:0000269|PubMed:21295697}. SUBCELLULAR LOCATION: Isoform 2: Cytoplasm {ECO:0000269|PubMed:18854161, ECO:0000269|PubMed:21295697}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:18854161, ECO:0000269|PubMed:21295697}. Golgi apparatus {ECO:0000250|UniProtKB:Q9UPN3}. Cell membrane {ECO:0000250|UniProtKB:Q9UPN3}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q9UPN3}. Note=APC controls its localization to the cell membrane which is critical for its function in microtubule stabilization. Localizes to the tips of microtubules. Associated with the minus-end of microtubules via interaction with CAMSAP3. The phosphorylated form is found in the cytoplasm while the non-phosphorylated form associates with the microtubules. {ECO:0000250|UniProtKB:Q9UPN3}.; SUBCELLULAR LOCATION: Isoform 1: Cytoplasm {ECO:0000250|UniProtKB:Q9UPN3}. Golgi apparatus {ECO:0000250|UniProtKB:Q9UPN3}. SUBUNIT: Isoform 2: Interacts with AXIN1, LRP6 and GOLGA4 (By similarity). Isoform 2: Found in a complex composed of MACF1, APC, AXIN1, CTNNB1 and GSK3B (By similarity). Isoform 2: Interacts with MAPRE1, CLASP1 AND CLASP2 (PubMed:18854161). Isoform 2: Interacts with CAMSAP3. {ECO:0000250|UniProtKB:Q9UPN3, ECO:0000269|PubMed:18854161}. DOMAIN: The C-terminal tail is required for phosphorylation by GSK3B and for microtubule-binding. {ECO:0000269|PubMed:21295697}. TISSUE SPECIFICITY: Enriched in the hair follicle stem cells (at protein level). Isoform 1 and isoform 2 are ubiquitous expressed, with higher levels seen in lung, heart, thymus, spleen and brain. {ECO:0000269|PubMed:16076900, ECO:0000269|PubMed:16815997, ECO:0000269|PubMed:21295697}. +Q9WTR2 M3K6_MOUSE Mitogen-activated protein kinase kinase kinase 6 (EC 2.7.11.25) (Apoptosis signal-regulating kinase 2) 1291 143,055 Active site (1); Binding site (1); Chain (1); Coiled coil (2); Domain (1); Modified residue (3); Mutagenesis (1); Nucleotide binding (1); Sequence conflict (10) FUNCTION: Component of a protein kinase signal transduction cascade. Activates the JNK, but not ERK or p38 kinase pathways. {ECO:0000269|PubMed:17210579}. SUBUNIT: Binds both upstream activators and downstream substrates in multimolecular complexes. {ECO:0000269|PubMed:17210579}. +A2AMZ4 NDUF8_MOUSE NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 8 74 7,785 Chain (1); Disulfide bond (2); Domain (1); Motif (2) FUNCTION: Involved in the assembly of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I, MT-ND1). Required to stabilize NDUFAF5. {ECO:0000250|UniProtKB:A1L188}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:A1L188}. SUBUNIT: Interacts with NDUFAF5. {ECO:0000250|UniProtKB:A1L188}. +Q8K5B2 MCFD2_MOUSE Multiple coagulation factor deficiency protein 2 homolog (Neural stem cell-derived neuronal survival protein) 145 16,168 Calcium binding (2); Chain (1); Domain (2); Modified residue (1); Signal peptide (1) FUNCTION: The MCFD2-LMAN1 complex forms a specific cargo receptor for the ER-to-Golgi transport of selected proteins. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Golgi apparatus {ECO:0000250}. SUBUNIT: Interacts in a calcium-dependent manner with LMAN1. {ECO:0000250}. +Q3UL97 MCAF2_MOUSE Activating transcription factor 7-interacting protein 2 (MBD1-containing chromatin-associated factor 2) (Protein similar to MCAF2) 452 50,975 Alternative sequence (6); Chain (1); Domain (1); Modified residue (2); Sequence conflict (5) FUNCTION: Recruiter that couples transcriptional factors to general transcription apparatus and thereby modulates transcription regulation and chromatin formation. Can both act as an activator or a repressor depending on the context. Mediates MBD1-dependent transcriptional repression, probably by recruiting complexes containing SETDB1. The complex formed with MBD1 and SETDB1 represses transcription and probably couples DNA methylation and histone H3 'Lys-9' trimethylation (H3K9me3) activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with MBD1, SETDB1 and SP1. Probably forms a complex with SETDB1 and MBD1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:16850184}. +P56942 MCH_MOUSE Pro-MCH [Cleaved into: Neuropeptide-glycine-glutamic acid (NGE) (Neuropeptide G-E); Neuropeptide-glutamic acid-isoleucine (NEI) (Neuropeptide E-I); Melanin-concentrating hormone (MCH)] 165 18,516 Chain (1); Disulfide bond (1); Modified residue (1); Peptide (3); Sequence conflict (2); Signal peptide (1) FUNCTION: MCH may act as a neurotransmitter or neuromodulator in a broad array of neuronal functions directed toward the regulation of goal-directed behavior, such as food intake, and general arousal. {ECO:0000269|PubMed:8637571}. PTM: Pro-MCH is processed differentially in the brain and in peripheral organs producing two neuropeptides; NEI and MCH. A third peptide, NGE, may also be produced. Preferential processing in neurons by prohormone convertase 2 (PC2) generates NEI. MCH is generated in neurons of the lateral hypothalmic area by several prohormone convertases including PC1/3, PC2 and PC5/6. {ECO:0000269|PubMed:10037747}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. TISSUE SPECIFICITY: Predominantly expressed in hypothalamus. Also found in heart, intestine, spleen and testis (spermatogonia, early spermatocytes and Sertoli cells). In brain only mature MCH and NEI peptides are present. In peripheral tissues a large product, encompassing the NEI and MCH domains of the precursor, is found predominantly. {ECO:0000269|PubMed:8724342}. +Q3UZ45 MCIN_MOUSE Multicilin (Multiciliate differentiation and DNA synthesis-associated cell cycle protein) (McIdas protein) (Protein Idas) 379 41,148 Chain (1); Coiled coil (1); Region (3) FUNCTION: Transcription regulator specifically required for multiciliate cell differentiation. Acts in a multiprotein complex containing E2F4 and E2F5 that binds and activates genes required for centriole biogenesis. Required for the deuterosome-mediated acentriolar pathway. Plays a role in mitotic cell cycle progression by promoting cell cycle exit. Modulates GMNN activity by reducing its affinity for CDT1. {ECO:0000250|UniProtKB:D6RGH6, ECO:0000250|UniProtKB:Q08B36}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21543332}. Note=Excluded from the nucleolus. {ECO:0000250|UniProtKB:D6RGH6}. SUBUNIT: Heterodimer (via coiled-coil domain) with GMNN (via coiled-coil domain); targets GMNN to the nucleus. Can form homodimers (in vitro, via coiled-coil domain), but these are much less stable than the heterodimer formed with GMNN. {ECO:0000250|UniProtKB:D6RGH6}. +Q99J21 MCLN1_MOUSE Mucolipin-1 (Mucolipidin) (Transient receptor potential-mucolipin 1) (TRPML1) 580 65,506 Alternative sequence (1); Chain (1); Disulfide bond (2); Glycosylation (2); Intramembrane (1); Modified residue (3); Motif (3); Mutagenesis (1); Region (3); Topological domain (8); Transmembrane (6) INTRAMEM 457 477 Pore-forming. {ECO:0000269|PubMed:29019981}. TRANSMEM 66 86 Helical; Name=1. {ECO:0000269|PubMed:29019981}.; TRANSMEM 299 321 Helical; Name=2. {ECO:0000269|PubMed:29019981}.; TRANSMEM 351 371 Helical; Name=3. {ECO:0000269|PubMed:29019981}.; TRANSMEM 383 405 Helical; Name=4. {ECO:0000269|PubMed:29019981}.; TRANSMEM 428 448 Helical; Name=5. {ECO:0000269|PubMed:29019981}.; TRANSMEM 492 513 Helical; Name=6. {ECO:0000269|PubMed:29019981}. TOPO_DOM 1 65 Cytoplasmic. {ECO:0000269|PubMed:29019981}.; TOPO_DOM 87 298 Extracellular. {ECO:0000269|PubMed:29019981}.; TOPO_DOM 322 350 Cytoplasmic. {ECO:0000269|PubMed:29019981}.; TOPO_DOM 372 382 Extracellular. {ECO:0000269|PubMed:29019981}.; TOPO_DOM 406 427 Cytoplasmic. {ECO:0000269|PubMed:29019981}.; TOPO_DOM 449 456 Extracellular. {ECO:0000269|PubMed:29019981}.; TOPO_DOM 478 491 Extracellular. {ECO:0000269|PubMed:29019981}.; TOPO_DOM 514 580 Cytoplasmic. {ECO:0000269|PubMed:29019981}. FUNCTION: Nonselective cation channel probably playing a role in the regulation of membrane trafficking events and of metal homeostasis (PubMed:29019981). Proposed to play a major role in Ca(2+) release from late endosome and lysosome vesicles to the cytoplasm, which is important for many lysosome-dependent cellular events, including the fusion and trafficking of these organelles, exocytosis and autophagy. Required for efficient uptake of large particles in macrophages in which Ca(2+) release from the lysosomes triggers lysosomal exocytosis. May also play a role in phagosome-lysosome fusion (PubMed:23993788). Involved in lactosylceramide trafficking indicative for a role in the regulation of late endocytic membrane fusion/fission events. By mediating lysosomal Ca(2+) release is involved in regulation of mTORC1 signaling and in mTOR/TFEB-dependent lysosomal adaptation to environmental cues such as nutrient levels (PubMed:25733853). Seems to act as lysosomal active oxygen species (ROS) sensor involved in ROS-induced TFEB activation and autophagy (By similarity). Functions as a Fe(2+) permeable channel in late endosomes and lysosomes. Proposed to play a role in zinc homeostasis probably implicating its association with TMEM163 (By similarity). In adaptive immunity, TRPML2 and TRPML1 may play redundant roles in the function of the specialized lysosomes of B cells (PubMed:17050035). {ECO:0000250|UniProtKB:Q9GZU1, ECO:0000269|PubMed:17050035, ECO:0000269|PubMed:23993788, ECO:0000269|PubMed:25733853, ECO:0000269|PubMed:29019981}.; FUNCTION: May contribute to cellular lipase activity within the late endosomal pathway or at the cell surface which may be involved in processes of membrane reshaping and vesiculation, especially the growth of tubular structures. However, it is not known, whether it conveys the enzymatic activity directly, or merely facilitates the activity of an associated phospholipase. {ECO:0000250|UniProtKB:Q9GZU1}. PTM: Palmitoylated; involved in association with membranes. {ECO:0000250|UniProtKB:Q9GZU1}.; PTM: Phosphorylation by PKA inhibits channel activity. Dephosphorylation increases activity. {ECO:0000250|UniProtKB:Q9GZU1}.; PTM: Proteolytically cleaved probably involving multiple lysosomal proteases including cathepsin B; inhibits lysosomal channnel activity. {ECO:0000250|UniProtKB:Q9GZU1}. SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250|UniProtKB:Q9GZU1}; Multi-pass membrane protein {ECO:0000269|PubMed:29019981}. Lysosome membrane {ECO:0000250|UniProtKB:Q9GZU1}; Multi-pass membrane protein {ECO:0000269|PubMed:29019981}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q9GZU1}; Multi-pass membrane protein {ECO:0000269|PubMed:29019981}. Cell projection, phagocytic cup {ECO:0000269|PubMed:23993788}. Cytoplasmic vesicle, phagosome membrane {ECO:0000269|PubMed:23993788}; Multi-pass membrane protein {ECO:0000269|PubMed:29019981}. Cell membrane {ECO:0000250|UniProtKB:Q9GZU1}; Multi-pass membrane protein {ECO:0000269|PubMed:29019981}. Note=Delivery from the trans-Golgi to lysosomes seems to occur mainly in a direct intracellular manner without intermediate delivery to the plasma membrane (By similarity). Under normal conditions, restricted to intracellular compartments so that only a very minor proportion is present at the cell membrane (PubMed:29019981). {ECO:0000250|UniProtKB:Q9GZU1, ECO:0000269|PubMed:29019981}. SUBUNIT: Homotetramer (PubMed:29019981). Homooligomer. Can heterooligomerize with MCOLN2 or MCOLN3; heteromeric assemblies have different channel properties as compared to the respective homooligomers and may be tissue-specific. Interacts with PDCD6. Interacts with TMEM163. Interacts with LAPTM4B (By similarity). {ECO:0000250|UniProtKB:Q9GZU1, ECO:0000269|PubMed:29019981}. DOMAIN: The most N-terminal extracellular/lumenal domain (referred to as I-II linker or polycystin-mucolipin domain) contributes to a structure with a four-fold rotational symmetry in a tetrameric assembly; the structure contains a central highly electronegative pore with a 14 A diameter. The pore is critical for Ca(2+) and pH regulation. The protruding structure formed by the I-II linkers may contain all the interaction sites with lipids and proteins in the endolysosomal lumen. {ECO:0000250|UniProtKB:Q9GZU1}. TISSUE SPECIFICITY: Widely expressed, with the highest expression in brain, liver and kidney. {ECO:0000269|PubMed:11897010}. +P49717 MCM4_MOUSE DNA replication licensing factor MCM4 (EC 3.6.4.12) (CDC21 homolog) (P1-CDC21) 862 96,736 Chain (1); Cross-link (2); Domain (1); Initiator methionine (1); Modified residue (15); Motif (1); Nucleotide binding (1); Sequence conflict (2) FUNCTION: Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. {ECO:0000250|UniProtKB:P33991}. PTM: Sumoylated; SUMO2 modified in response to stress caused by inhibition of proteasome activity (in vitro). {ECO:0000269|PubMed:26524493}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the MCM2-7 complex. The complex forms a toroidal hexameric ring with the proposed subunit order MCM2-MCM6-MCM4-MCM7-MCM3-MCM5. Interacts with MCMBP. {ECO:0000250|UniProtKB:P33991}. +P49718 MCM5_MOUSE DNA replication licensing factor MCM5 (EC 3.6.4.12) (CDC46 homolog) (P1-CDC46) 733 82,343 Chain (1); Domain (1); Initiator methionine (1); Modified residue (5); Motif (1); Nucleotide binding (1) FUNCTION: Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P33992}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P33992}. SUBUNIT: Component of the MCM2-7 complex. The complex forms a toroidal hexameric ring with the proposed subunit order MCM2-MCM6-MCM4-MCM7-MCM3-MCM5. Interacts with MCMBP (By simililarity). Interacts with ANKRD17. {ECO:0000250|UniProtKB:P33992}. +Q2LKU9 NLR1A_MOUSE NACHT, LRR and PYD domains-containing protein 1a (Caspase recruitment domain-containing protein 7) (Death effector filament-forming ced-4-like apoptosis protein) (Nucleotide-binding domain and caspase recruitment domain) 1182 134,308 Alternative sequence (3); Chain (1); Domain (3); Mutagenesis (1); Natural variant (18); Nucleotide binding (1); Repeat (3); Sequence conflict (1); Site (1) FUNCTION: As a potential sensor component of the NLRP1 inflammasome, plays a crucial role in innate immunity and inflammation. In response to pathogens and other damage-associated signals, initiates the formation of the inflammasome polymeric complex, made of Nlrp1b, CASP1, and possibly PYCARD. Recruitment of proCASP1 to the inflammasome promotes its activation and CASP1-catalyzed IL1B and IL18 maturation and secretion in the extracellular milieu. Activation of NLRP1 inflammasome is also required for HMGB1 secretion. The active cytokines and HMGB1 stimulate inflammatory responses. Inflammasomes can also induce pyroptosis, an inflammatory form of programmed cell death (By similarity) (PubMed:23219391). When activated in the bone marrow, induces the pyroptosis of hematopoietic stem cells and progenitor cells of both myeloid and lymphoid lineages, hence allowing the removal of damaged cells, and the release of IL1B, which induces granulopoiesis (PubMed:23219391). Binds ATP (By similarity). {ECO:0000250|UniProtKB:Q2LKW6, ECO:0000250|UniProtKB:Q9C000, ECO:0000269|PubMed:23219391}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9C000}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9C000}. Inflammasome {ECO:0000250|UniProtKB:Q2LKW6}. SUBUNIT: Sensor component of NLRP1 inflammasomes. Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other damage-associated signals and play critical roles in innate immunity and inflammation. Classical inflammasomes consist of a signal sensor component, an adapter (ASC/PYCARD), which recruits an effector proinflammatory caspase (CASP1 and possibly CASP4/CASP11). CASP1 filament formation increases local enzyme concentration, resulting in trans-autocleavage and activation. Active CASP1 then processes IL1B and IL18 precursors, leading to the release of mature cytokines in the extracellular milieu and inflammatory response. In NLRP1 inflammasome, the role of PYCARD is not clear. Following activation, Nlrp1b may directly interact with CASP1 (through the CARD domain) to form a functional inflammasome. Hence PYCARD may not be necessary for NLRP1 and CASP1 interaction, but is required for speck formation and full inflammasome activity (By similarity) (PubMed:23219391). Homomer (By similarity). Interacts (via LRR repeats) with BCL2 and BCL2L1 (via the loop between motifs BH4 and BH3); these interactions reduce NLRP1 inflammasome-induced CASP1 activation and IL1B release, possibly by impairing NLRP1 interaction with PYCARD (By similarity). Interacts with NOD2; this interaction may lead to increased IL1B release (By similarity). Interacts with EIF2AK2/PKR; this interaction requires EIF2AK2 activity, is accompanied by EIF2AK2 autophosphorylation and promotes inflammasome assembly in response to dange-associated signals (By similarity). Interacts with MEFV; this interaction targets NLRP1 to degradation by autophagy, hence preventing excessive IL1B- and IL18-mediated inflammation (By similarity). {ECO:0000250|UniProtKB:Q2LKW6, ECO:0000250|UniProtKB:Q9C000, ECO:0000269|PubMed:23219391}. DOMAIN: The CARD domain might be involved in the interaction with PYCARD, CASP1 and CASP4/CASP11. {ECO:0000250|UniProtKB:Q9C000}.; DOMAIN: The leucine-rich repeat (LRR) domain may be involved in autoinhibition in the absence of activating signal, possibly through intramolecular interaction with the NACHT domain. {ECO:0000250|UniProtKB:Q2LKW6}.; DOMAIN: The FIIND (domain with function to find) region is involved in homomerization, but not in CASP1-binding. Autocatalytic cleavage in this region occurs constitutively, prior to activation signals, and is required for inflammasome activity (IL1B release), possibly by facilitating CASP1 binding. Both N- and C-terminal fragments remain associated. {ECO:0000250|UniProtKB:Q2LKW6}. TISSUE SPECIFICITY: Highly expressed in hematopoietic stem cells and progenitor cells of both myeloid and lymphoid origin (PubMed:23219391). The expression is highly strain-dependent. Not expressed in Balb/cJ animals, but widely expressed in C57BL/6J. Expressed in macrophages resistant to Bacillus anthracis lethal toxin, but not in toxin-sensitive macrophages, except in CAST/EiJ strain (PubMed:23506131). {ECO:0000269|PubMed:23219391, ECO:0000269|PubMed:23506131}. +Q66X03 NLR9A_MOUSE NACHT, LRR and PYD domains-containing protein 9A (NALP-theta) 949 109,680 Alternative sequence (2); Chain (1); Domain (2); Nucleotide binding (1); Repeat (5); Sequence conflict (2) FUNCTION: May be involved in inflammation. {ECO:0000305}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q66X22}. TISSUE SPECIFICITY: Oocyte specific. {ECO:0000269|PubMed:15317747}. +Q66X22 NLR9B_MOUSE NACHT, LRR and PYD domains-containing protein 9B (NALP-delta) 1003 114,802 Alternative sequence (3); Chain (1); Domain (2); Nucleotide binding (1); Repeat (7) FUNCTION: As the sensor component of the NLRP9 inflammasome, plays a crucial role in innate immunity and inflammation. In response to pathogens, including rotavirus, initiates the formation of the inflammasome polymeric complex, made of NLRP9, PYCARD and CASP1. Recruitment of proCASP1 to the inflammasome promotes its activation and CASP1-catalyzed IL1B and IL18 maturation and release in the extracellular milieu. The active cytokines stimulate inflammatory responses. Inflammasomes can also induce pyroptosis, an inflammatory form of programmed cell death. NLRP9 inflammasome activation may be initiated by DHX9 interaction with viral double-stranded RNA (dsRNA), preferentially to short dsRNA segments. {ECO:0000269|PubMed:28636595}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:26411641}. Inflammasome {ECO:0000250|UniProtKB:Q7RTR0}. SUBUNIT: Sensor component of NLRP9 inflammasomes. Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens, such as rotavirus, but not encephalomyocarditis virus (EMCV), and play critical roles in innate immunity and inflammation. The core of NLRP9 inflammasomes consists of a signal sensor component (NLRP9), an adapter (ASC/PYCARD), which recruits an effector proinflammatory caspase (CASP1). Within the complex, NLRP9 and PYCARD interact via their respective DAPIN/pyrin domains. This interaction initiates speck formation (nucleation) which greatly enhances further addition of soluble PYCARD molecules to the speck in a prion-like polymerization process. Clustered PYCARD nucleates the formation of CASP1 filaments through the interaction of their respective CARD domains, acting as a platform for CASP1 polymerization. CASP1 filament formation increases local enzyme concentration, resulting in trans-autocleavage and activation. Active CASP1 then processes IL1B and IL18 precursors, leading to the release of mature cytokines in the extracellular milieu and inflammatory response. Interacts with DHX9 upon rotavirus infection; this interaction may trigger inflammasome activation and inflammatory response. {ECO:0000250|UniProtKB:Q7RTR0}. TISSUE SPECIFICITY: Predominantly expressed in the intestine, including proximal and distal colon, cecum, ileum, jejunum and duodenum (at protein level) (PubMed:26411641, PubMed:28636595). In the ileum, expressed in epithelial cells (PubMed:28636595). Also expressed in oocytes at all follicular stages and in preimplantation embryos (at protein level) (PubMed:15317747, PubMed:26411641). Although expression decreases in preimplantation embryos, it is still detectable in blastocyts (PubMed:26411641). {ECO:0000269|PubMed:15317747, ECO:0000269|PubMed:26411641, ECO:0000269|PubMed:28636595}. +P32020 NLTP_MOUSE Non-specific lipid-transfer protein (NSL-TP) (EC 2.3.1.176) (Propanoyl-CoA C-acyltransferase) (SCP-chi) (SCPX) (Sterol carrier protein 2) (SCP-2) (Sterol carrier protein X) (SCP-X) 547 59,126 Alternative sequence (1); Chain (1); Domain (1); Modified residue (34); Motif (1); Sequence conflict (2) FUNCTION: Mediates in vitro the transfer of all common phospholipids, cholesterol and gangliosides between membranes. May play a role in regulating steroidogenesis. SUBCELLULAR LOCATION: Cytoplasm. Note=Cytoplasmic in the liver and also associated with mitochondria especially in steroidogenic tissues.; SUBCELLULAR LOCATION: Isoform SCP2: Mitochondrion.; SUBCELLULAR LOCATION: Isoform SCPx: Peroxisome. Note=Interaction with PEX5 is essential for peroxisomal import. {ECO:0000250}. SUBUNIT: Interacts with PEX5. {ECO:0000250}. TISSUE SPECIFICITY: Present at low levels in all tissues examined but expressed predominantly in the liver. +O54799 NMBR_MOUSE Neuromedin-B receptor (NMB-R) (Neuromedin-B-preferring bombesin receptor) 390 43,623 Chain (1); Disulfide bond (1); Glycosylation (3); Lipidation (1); Modified residue (1); Topological domain (8); Transmembrane (7) TRANSMEM 42 65 Helical; Name=1. {ECO:0000255}.; TRANSMEM 80 99 Helical; Name=2. {ECO:0000255}.; TRANSMEM 118 139 Helical; Name=3. {ECO:0000255}.; TRANSMEM 157 177 Helical; Name=4. {ECO:0000255}.; TRANSMEM 212 235 Helical; Name=5. {ECO:0000255}.; TRANSMEM 267 287 Helical; Name=6. {ECO:0000255}.; TRANSMEM 300 327 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 41 Extracellular. {ECO:0000255}.; TOPO_DOM 66 79 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 100 117 Extracellular. {ECO:0000255}.; TOPO_DOM 140 156 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 178 211 Extracellular. {ECO:0000255}.; TOPO_DOM 236 266 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 288 299 Extracellular. {ECO:0000255}.; TOPO_DOM 328 390 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for neuromedin-B. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q9CR53 NMB_MOUSE Neuromedin-B [Cleaved into: Neuromedin-B-32; Neuromedin-B] 121 13,571 Modified residue (1); Peptide (2); Propeptide (1); Signal peptide (1) FUNCTION: Stimulates smooth muscle contraction in a manner similar to that of bombesin. SUBCELLULAR LOCATION: Secreted. +Q91ZU9 NMD3B_MOUSE Glutamate receptor ionotropic, NMDA 3B (GluN3B) (N-methyl-D-aspartate receptor subunit NR3B) (NMDAR3B) (NR3B) (NMDA receptor 4) (Nr4) 1003 109,158 Chain (1); Coiled coil (1); Glycosylation (6); Region (1); Sequence conflict (4); Signal peptide (1); Topological domain (4); Transmembrane (3) TRANSMEM 565 585 Helical. {ECO:0000255}.; TRANSMEM 649 669 Helical. {ECO:0000255}.; TRANSMEM 827 847 Helical. {ECO:0000255}. TOPO_DOM 25 564 Extracellular. {ECO:0000255}.; TOPO_DOM 586 648 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 670 826 Extracellular. {ECO:0000255}.; TOPO_DOM 848 1003 Cytoplasmic. {ECO:0000255}. FUNCTION: NMDA receptor subtype of glutamate-gated ion channels with reduced single-channel conductance, low calcium permeability and low voltage-dependent sensitivity to magnesium. Mediated by glycine. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14602821}; Multi-pass membrane protein {ECO:0000269|PubMed:14602821}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000269|PubMed:14602821}. Note=Requires the presence of GRIN1 to be targeted at the plasma membrane. SUBUNIT: Forms heteromeric channel of a zeta subunit (GRIN1), a epsilon subunit (GRIN2A, GRIN2B, GRIN2C or GRIN2D) and a third subunit (GRIN3A or GRIN3B). Does not form functional homomeric channels. Found in a complex with GRIN1 and GRIN2A or GRIN2B. {ECO:0000269|PubMed:12008020, ECO:0000269|PubMed:14602821}. TISSUE SPECIFICITY: Expressed in the facial nucleus and the ambiguus nucleus of the brainstem, pons, medulla, spinal cord and cerebellum. {ECO:0000269|PubMed:11717388, ECO:0000269|PubMed:12008020, ECO:0000269|PubMed:14602821}. +Q99L48 NMD3_MOUSE 60S ribosomal export protein NMD3 503 57,611 Alternative sequence (2); Chain (1); Modified residue (5); Motif (2); Region (1) FUNCTION: Acts as an adapter for the XPO1/CRM1-mediated export of the 60S ribosomal subunit. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96D46}. Nucleus {ECO:0000250|UniProtKB:Q96D46}. Note=Shuttles between the nucleus/nucleolus and the cytoplasm in a XPO1/CRM1-dependent manner. {ECO:0000250|UniProtKB:Q96D46}. SUBUNIT: Found in a 60S ribosomal subunit export complex with RAN and XPO1. Interacts with XPO1. Associates with the 60S ribosomal subunit (By similarity). {ECO:0000250}. +P35436 NMDE1_MOUSE Glutamate receptor ionotropic, NMDA 2A (GluN2A) (Glutamate [NMDA] receptor subunit epsilon-1) (N-methyl D-aspartate receptor subtype 2A) (NMDAR2A) (NR2A) 1464 165,421 Binding site (1); Chain (1); Disulfide bond (4); Glycosylation (6); Intramembrane (1); Metal binding (4); Modified residue (8); Motif (1); Region (4); Signal peptide (1); Site (1); Topological domain (5); Transmembrane (3) INTRAMEM 601 620 Discontinuously helical. {ECO:0000250|UniProtKB:B7ZSK1}. TRANSMEM 556 576 Helical. {ECO:0000250|UniProtKB:B7ZSK1}.; TRANSMEM 626 645 Helical. {ECO:0000250|UniProtKB:B7ZSK1}.; TRANSMEM 817 837 Helical. {ECO:0000250|UniProtKB:B7ZSK1}. TOPO_DOM 23 555 Extracellular. {ECO:0000305}.; TOPO_DOM 577 600 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 621 625 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 646 816 Extracellular. {ECO:0000305}.; TOPO_DOM 838 1464 Cytoplasmic. {ECO:0000305}. FUNCTION: Component of NMDA receptor complexes that function as heterotetrameric, ligand-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium (PubMed:1374164). Channel activation requires binding of the neurotransmitter glutamate to the epsilon subunit, glycine binding to the zeta subunit, plus membrane depolarization to eliminate channel inhibition by Mg(2+). Sensitivity to glutamate and channel kinetics depend on the subunit composition; channels containing GRIN1 and GRIN2A have higher sensitivity to glutamate and faster kinetics than channels formed by GRIN1 and GRIN2B (By similarity). Contributes to the slow phase of excitatory postsynaptic current, long-term synaptic potentiation, and learning (PubMed:7816096, PubMed:8987814). {ECO:0000250|UniProtKB:Q00959, ECO:0000269|PubMed:1374164, ECO:0000269|PubMed:7816096, ECO:0000269|PubMed:8987814}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1374164}; Multi-pass membrane protein {ECO:0000305}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000250|UniProtKB:Q00959}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q00959}. SUBUNIT: Heterotetramer (By similarity). Forms heterotetrameric channels composed of two zeta subunits (GRIN1), and two epsilon subunits (GRIN2A, GRIN2B, GRIN2C or GRIN2D) (in vitro) (PubMed:1374164). Can also form heterotetrameric channels that contain at least one zeta subunit (GRIN1), at least one epsilon subunit, plus GRIN3A or GRIN3B (PubMed:12008020). In vivo, the subunit composition may depend on the expression levels of the different subunits. Found in a complex with GRIN1, GRIN3A and PPP2CB (By similarity). Found in a complex with GRIN1 and GRIN3B (PubMed:12008020). Interacts with AIP1 (By similarity). Interacts with HIP1 and NETO1 (PubMed:17329427, PubMed:19243221). Interacts with SNX27 (via PDZ domain); the interaction is required for recycling to the plasma membrane when endocytosed and prevent degradation in lysosomes (PubMed:23524343). Interacts with PDZ domains of PATJ and DLG4. Interacts with LRFN2 (By similarity). {ECO:0000250|UniProtKB:Q00959, ECO:0000269|PubMed:12008020, ECO:0000269|PubMed:1374164, ECO:0000269|PubMed:17329427, ECO:0000269|PubMed:19243221, ECO:0000269|PubMed:23524343}. DOMAIN: Contains an N-terminal domain, a ligand-binding domain and a transmembrane domain. Agonist binding to the extracellular ligand-binding domains triggers channel gating. {ECO:0000250|UniProtKB:Q00959}.; DOMAIN: A hydrophobic region that gives rise to the prediction of a transmembrane span does not cross the membrane, but is part of a discontinuously helical region that dips into the membrane and is probably part of the pore and of the selectivity filter. {ECO:0000250|UniProtKB:B7ZSK1}. TISSUE SPECIFICITY: Detected in forbrain (PubMed:7816096). Detected in cerebellum (at protein level) (PubMed:8987814). Detected in brain cortex, piriform cortex, hippocampus, caudate-putamen, dentate gyrus and granule cell layer (PubMed:1374164, PubMed:7816096). {ECO:0000269|PubMed:1374164, ECO:0000269|PubMed:7816096, ECO:0000269|PubMed:8987814}. +Q01097 NMDE2_MOUSE Glutamate receptor ionotropic, NMDA 2B (GluN2B) (Glutamate [NMDA] receptor subunit epsilon-2) (N-methyl D-aspartate receptor subtype 2B) (NMDAR2B) (NR2B) 1482 165,959 Binding site (3); Chain (1); Compositional bias (1); Disulfide bond (4); Glycosylation (7); Intramembrane (1); Metal binding (2); Modified residue (17); Motif (1); Region (3); Sequence conflict (1); Signal peptide (1); Site (1); Topological domain (5); Transmembrane (3) INTRAMEM 604 623 Discontinuously helical. {ECO:0000250|UniProtKB:Q00960}. TRANSMEM 558 576 Helical. {ECO:0000250|UniProtKB:Q00960}.; TRANSMEM 631 646 Helical. {ECO:0000250|UniProtKB:Q00960}.; TRANSMEM 818 837 Helical. {ECO:0000250|UniProtKB:Q00960}. TOPO_DOM 27 557 Extracellular. {ECO:0000250|UniProtKB:Q00960}.; TOPO_DOM 577 603 Cytoplasmic. {ECO:0000250|UniProtKB:Q00960}.; TOPO_DOM 624 630 Cytoplasmic. {ECO:0000250|UniProtKB:Q00960}.; TOPO_DOM 647 817 Extracellular. {ECO:0000250|UniProtKB:Q00960}.; TOPO_DOM 838 1482 Cytoplasmic. {ECO:0000250|UniProtKB:Q00960}. FUNCTION: Component of NMDA receptor complexes that function as heterotetrameric, ligand-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Channel activation requires binding of the neurotransmitter glutamate to the epsilon subunit, glycine binding to the zeta subunit, plus membrane depolarization to eliminate channel inhibition by Mg(2+) (PubMed:1377365, PubMed:26912815). Sensitivity to glutamate and channel kinetics depend on the subunit composition (PubMed:1377365). In concert with DAPK1 at extrasynaptic sites, acts as a central mediator for stroke damage. Its phosphorylation at Ser-1303 by DAPK1 enhances synaptic NMDA receptor channel activity inducing injurious Ca2+ influx through them, resulting in an irreversible neuronal death (PubMed:20141836). Contributes to neural pattern formation in the developing brain (PubMed:8789948). Plays a role in long-term depression (LTD) of hippocampus membrane currents and in synaptic plasticity (PubMed:8789948). {ECO:0000269|PubMed:1377365, ECO:0000269|PubMed:20141836, ECO:0000269|PubMed:26912815, ECO:0000269|PubMed:8789948}. PTM: Phosphorylated on tyrosine residues (PubMed:12451687). Phosphorylation at Ser-1303 by DAPK1 enhances synaptic NMDA receptor channel activity (PubMed:20141836). {ECO:0000269|PubMed:12451687, ECO:0000269|PubMed:20141836}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1377365, ECO:0000269|PubMed:26912815}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q00960}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000250|UniProtKB:Q00960}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q00960}. SUBUNIT: Heterotetramer. Forms heterotetrameric channels composed of two zeta subunits (GRIN1), and two epsilon subunits (GRIN2A, GRIN2B, GRIN2C or GRIN2D) (in vitro) (PubMed:1377365, PubMed:26912815). Can also form heterotetrameric channels that contain at least one zeta subunit (GRIN1), at least one epsilon subunit, plus GRIN3A or GRIN3B (PubMed:12008020, PubMed:14602821). In vivo, the subunit composition may depend on the expression levels of the different subunits (Probable). Found in a complex with GRIN1, GRIN3A and PPP2CB (By similarity). Found in a complex with GRIN1 and GRIN3B (PubMed:12008020, PubMed:14602821). Interacts with MAGI3 (By similarity). Interacts with HIP1 and NETO1 (PubMed:17329427, PubMed:19243221). Interacts with PDZ domains of PATJ, DLG3 and DLG4. Interacts with DAPK1 (PubMed:20141836). Found in a complex with GRIN1 and PRR7. Interacts with PRR7 (By similarity). Interacts with CAMK2A (By similarity). {ECO:0000250|UniProtKB:Q00960, ECO:0000250|UniProtKB:Q13224, ECO:0000269|PubMed:12008020, ECO:0000269|PubMed:1377365, ECO:0000269|PubMed:14602821, ECO:0000269|PubMed:17329427, ECO:0000269|PubMed:19243221, ECO:0000269|PubMed:20141836, ECO:0000269|PubMed:26912815}. DOMAIN: A hydrophobic region that gives rise to the prediction of a transmembrane span does not cross the membrane, but is part of a discontinuously helical region that dips into the membrane and is probably part of the pore and of the selectivity filter. {ECO:0000250|UniProtKB:Q00960}. TISSUE SPECIFICITY: Detected in brain (at protein level) (PubMed:8789948). Detected throughout the brain, and in brain stem trigeminal nucleus (PubMed:8789948). Detected in forebrain (PubMed:1377365). {ECO:0000269|PubMed:1377365, ECO:0000269|PubMed:8789948}. +Q01098 NMDE3_MOUSE Glutamate receptor ionotropic, NMDA 2C (GluN2C) (Glutamate [NMDA] receptor subunit epsilon-3) (N-methyl D-aspartate receptor subtype 2C) (NMDAR2C) (NR2C) 1239 135,420 Binding site (3); Chain (1); Disulfide bond (4); Glycosylation (4); Intramembrane (1); Modified residue (3); Motif (1); Region (3); Signal peptide (1); Site (1); Topological domain (5); Transmembrane (3) INTRAMEM 601 620 Discontinuously helical. {ECO:0000250|UniProtKB:Q00960}. TRANSMEM 555 573 Helical. {ECO:0000250|UniProtKB:Q00960}.; TRANSMEM 628 643 Helical. {ECO:0000250|UniProtKB:Q00960}.; TRANSMEM 815 834 Helical. {ECO:0000250|UniProtKB:Q00960}. TOPO_DOM 20 554 Extracellular. {ECO:0000250|UniProtKB:Q00960}.; TOPO_DOM 574 600 Cytoplasmic. {ECO:0000250|UniProtKB:Q00960}.; TOPO_DOM 621 627 Cytoplasmic. {ECO:0000250|UniProtKB:Q00960}.; TOPO_DOM 644 814 Extracellular. {ECO:0000250|UniProtKB:Q00960}.; TOPO_DOM 835 1239 Cytoplasmic. {ECO:0000250|UniProtKB:Q00960}. FUNCTION: Component of NMDA receptor complexes that function as heterotetrameric, ligand-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Channel activation requires binding of the neurotransmitter glutamate to the epsilon subunit, glycine binding to the zeta subunit, plus membrane depolarization to eliminate channel inhibition by Mg(2+) (PubMed:1377365). Sensitivity to glutamate and channel kinetics depend on the subunit composition (PubMed:1377365). Plays a role in regulating the balance between excitatory and inhibitory activity of pyramidal neurons in the prefrontal cortex (PubMed:27922130). Contributes to the slow phase of excitatory postsynaptic current, long-term synaptic potentiation, and learning (PubMed:8987814). {ECO:0000269|PubMed:1377365, ECO:0000269|PubMed:27922130, ECO:0000269|PubMed:8987814}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1377365}; Multi-pass membrane protein {ECO:0000305}. Cell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein. SUBUNIT: Heterotetramer. Forms heterotetrameric channels composed of two zeta subunits (GRIN1), and two epsilon subunits (GRIN2A, GRIN2B, GRIN2C or GRIN2D) (in vitro) (PubMed:1377365). Can also form heterotetrameric channels that contain at least one zeta subunit (GRIN1), at least one epsilon subunit, plus GRIN3A or GRIN3B (By similarity). In vivo, the subunit composition may depend on the expression levels of the different subunits (Probable). Interacts with PDZ domains of PATJ and DLG4 (By similarity). Interacts (via PDZ-binding motif) with SNX27 (via PDZ domain); the interaction is required for recycling to the plasma membrane when endocytosed and prevent degradation in lysosomes (By similarity). {ECO:0000250|UniProtKB:Q00961, ECO:0000250|UniProtKB:Q14957, ECO:0000269|PubMed:1377365, ECO:0000305}. DOMAIN: A hydrophobic region that gives rise to the prediction of a transmembrane span does not cross the membrane, but is part of a discontinuously helical region that dips into the membrane and is probably part of the pore and of the selectivity filter. {ECO:0000250|UniProtKB:Q00960}. TISSUE SPECIFICITY: Detected in cerebellum (at protein level) (PubMed:8987814). Detected in the granule cell layer of the cerebellum (PubMed:1377365). {ECO:0000269|PubMed:1377365, ECO:0000269|PubMed:8987814}. +Q03391 NMDE4_MOUSE Glutamate receptor ionotropic, NMDA 2D (GluN2D) (Glutamate [NMDA] receptor subunit epsilon-4) (N-methyl D-aspartate receptor subtype 2D) (NMDAR2D) (NR2D) 1323 142,963 Binding site (3); Chain (1); Compositional bias (4); Disulfide bond (4); Glycosylation (5); Intramembrane (1); Modified residue (2); Motif (1); Region (3); Sequence conflict (2); Signal peptide (1); Site (1); Topological domain (5); Transmembrane (3) INTRAMEM 628 647 Discontinuously helical. {ECO:0000250|UniProtKB:Q00960}. TRANSMEM 582 600 Helical. {ECO:0000250|UniProtKB:Q00960}.; TRANSMEM 655 670 Helical. {ECO:0000250|UniProtKB:Q00960}.; TRANSMEM 842 861 Helical. {ECO:0000250|UniProtKB:Q00960}. TOPO_DOM 28 581 Extracellular. {ECO:0000305}.; TOPO_DOM 601 627 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 648 654 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 671 841 Extracellular. {ECO:0000305}.; TOPO_DOM 862 1323 Cytoplasmic. {ECO:0000305}. FUNCTION: Component of NMDA receptor complexes that function as heterotetrameric, ligand-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Channel activation requires binding of the neurotransmitter glutamate to the epsilon subunit, glycine binding to the zeta subunit, plus membrane depolarization to eliminate channel inhibition by Mg(2+) (PubMed:1385220). Sensitivity to glutamate and channel kinetics depend on the subunit composition (Probable). {ECO:0000269|PubMed:1385220, ECO:0000305}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1385220}; Multi-pass membrane protein {ECO:0000305}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000305|PubMed:8774946}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Heterotetramer. Forms heterotetrameric channels composed of two zeta subunits (GRIN1), and two epsilon subunits (GRIN2A, GRIN2B, GRIN2C or GRIN2D) (in vitro) (PubMed:1385220). In vivo, the subunit composition may depend on the expression levels of the different subunits (Probable). Interacts with PDZ domains of PATJ and DLG4 (By similarity). {ECO:0000250|UniProtKB:Q62645, ECO:0000269|PubMed:1385220, ECO:0000305}. DOMAIN: A hydrophobic region that gives rise to the prediction of a transmembrane span does not cross the membrane, but is part of a discontinuously helical region that dips into the membrane and is probably part of the pore and of the selectivity filter. {ECO:0000250|UniProtKB:Q00960}. TISSUE SPECIFICITY: Detected in neonate brain synaptosomes (at protein level). {ECO:0000269|PubMed:8774946}. +P35438 NMDZ1_MOUSE Glutamate receptor ionotropic, NMDA 1 (GluN1) (Glutamate [NMDA] receptor subunit zeta-1) (N-methyl-D-aspartate receptor subunit NR1) (NMD-R1) 938 105,481 Alternative sequence (2); Binding site (3); Chain (1); Disulfide bond (4); Glycosylation (10); Intramembrane (1); Modified residue (4); Natural variant (1); Region (2); Signal peptide (1); Topological domain (5); Transmembrane (3) INTRAMEM 603 624 Discontinuously helical. {ECO:0000250|UniProtKB:A0A1L8F5J9}. TRANSMEM 560 580 Helical. {ECO:0000250|UniProtKB:P35439}.; TRANSMEM 631 647 Helical. {ECO:0000250|UniProtKB:P35439}.; TRANSMEM 813 833 Helical. {ECO:0000250|UniProtKB:P35439}. TOPO_DOM 19 559 Extracellular. {ECO:0000305}.; TOPO_DOM 581 602 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 625 630 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 648 812 Extracellular. {ECO:0000305}.; TOPO_DOM 834 938 Cytoplasmic. {ECO:0000305}. FUNCTION: Component of NMDA receptor complexes that function as heterotetrameric, ligand-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Channel activation requires binding of the neurotransmitter glutamate to the epsilon subunit, glycine binding to the zeta subunit, plus membrane depolarization to eliminate channel inhibition by Mg(2+) (PubMed:1532151, PubMed:8060614, PubMed:12008020). Sensitivity to glutamate and channel kinetics depend on the subunit composition (PubMed:12008020). {ECO:0000269|PubMed:12008020, ECO:0000269|PubMed:1532151, ECO:0000269|PubMed:8060614}. PTM: NMDA is probably regulated by C-terminal phosphorylation of an isoform of NR1 by PKC. Dephosphorylated on Ser-897 probably by protein phosphatase 2A (PPP2CB). Its phosphorylated state is influenced by the formation of the NMDAR-PPP2CB complex and the NMDAR channel activity (By similarity). {ECO:0000250|UniProtKB:P35439}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12008020, ECO:0000269|PubMed:1532151, ECO:0000269|PubMed:8060614}; Multi-pass membrane protein {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250}. Note=Enriched in postsynaptic plasma membrane and postsynaptic densities. {ECO:0000250}. SUBUNIT: Forms heteromeric channel of a zeta subunit (GRIN1), a epsilon subunit (GRIN2A, GRIN2B, GRIN2C or GRIN2D) and a third subunit (GRIN3A or GRIN3B) (PubMed:12008020, PubMed:14602821). Found in a complex with GRIN2A or GRIN2B and GRIN3B (PubMed:12008020, PubMed:14602821). Found in a complex with GRIN2A or GRIN2B, GRIN3A and PPP2CB (By similarity). Interacts with DLG4 and MPDZ (By similarity). Interacts with LRFN1 and LRFN2 (By similarity). Interacts with MYZAP (PubMed:18849881). Interacts with SNX27 (via PDZ domain); the interaction is required for recycling to the plasma membrane when endocytosed and prevent degradation in lysosomes (PubMed:23524343). Found in a complex with DLG4 and PRR7 (By similarity). Found in a complex with GRIN2B and PRR7 (By similarity). Interacts with PRR7; the interaction is reduced following NMDA receptor activity (By similarity). {ECO:0000250|UniProtKB:P35439, ECO:0000269|PubMed:12008020, ECO:0000269|PubMed:14602821, ECO:0000269|PubMed:18849881, ECO:0000269|PubMed:23524343}. DOMAIN: A hydrophobic region that gives rise to the prediction of a transmembrane span does not cross the membrane, but is part of a discontinuously helical region that dips into the membrane and is probably part of the pore and of the selectivity filter. {ECO:0000250|UniProtKB:A0A1L8F5J9}. TISSUE SPECIFICITY: Detected in brain (at protein level). Detected in brain. {ECO:0000269|PubMed:8060614}. +Q810Q5 NMES1_MOUSE Normal mucosa of esophagus-specific gene 1 protein 83 9,584 Chain (1) SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. TISSUE SPECIFICITY: Strongly expressed in vertebrae, brain, intestine and stomach. {ECO:0000269|PubMed:12209954}. +O35309 NMI_MOUSE N-myc-interactor (Nmi) (N-myc and STAT interactor) 314 35,236 Chain (1); Modified residue (1); Sequence conflict (4) FUNCTION: May be involved in augmenting coactivator protein recruitment to a group of sequence-specific transcription factors. Augments cytokine-mediated STAT transcription (By similarity). Enhances CBP/p300 coactivator protein recruitment to STAT1 and STAT5 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Interacts with MYCN and MYC, as well as with other transcription factors with a Zip, HLH or a HLH-Zip motif. Interacts with all STAT proteins except STAT2. {ECO:0000250}. +Q9EPA7 NMNA1_MOUSE Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1 (NMN/NaMN adenylyltransferase 1) (EC 2.7.7.1) (EC 2.7.7.18) (Nicotinamide mononucleotide adenylyltransferase 1) (NMN adenylyltransferase 1) (Nicotinate-nucleotide adenylyltransferase 1) (NaMN adenylyltransferase 1) 285 32,355 Binding site (2); Chain (1); Erroneous initiation (3); Modified residue (1); Motif (1); Mutagenesis (2); Nucleotide binding (3); Region (3) Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from nicotinamide D-ribonucleotide: step 1/1. Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1. FUNCTION: Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP (PubMed:15381699). Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate with the same efficiency (By similarity). Can use triazofurin monophosphate (TrMP) as substrate (By similarity). Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+) (By similarity). For the pyrophosphorolytic activity, prefers NAD(+) and NaAD as substrates and degrades NADH, nicotinic acid adenine dinucleotide phosphate (NHD) and nicotinamide guanine dinucleotide (NGD) less effectively (By similarity). Involved in the synthesis of ATP in the nucleus, together with PARP1, PARG and NUDT5 (By similarity). Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming (By similarity). Fails to cleave phosphorylated dinucleotides NADP(+), NADPH and NaADP(+) (By similarity). Protects against axonal degeneration following mechanical or toxic insults (PubMed:15310905, PubMed:16914673). Delays axonal degeneration after axotomy. Results in a >10-fold increase in intact neurites 72 hours after injury (PubMed:16914673). {ECO:0000250|UniProtKB:Q9HAN9, ECO:0000269|PubMed:15310905, ECO:0000269|PubMed:15381699, ECO:0000269|PubMed:16914673}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16914673}. SUBUNIT: Homohexamer. Interacts with ADPRT/PARP1. {ECO:0000250|UniProtKB:Q9HAN9}. +Q8BNJ3 NMNA2_MOUSE Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2 (NMN/NaMN adenylyltransferase 2) (EC 2.7.7.1) (EC 2.7.7.18) (Nicotinamide mononucleotide adenylyltransferase 2) (NMN adenylyltransferase 2) (Nicotinate-nucleotide adenylyltransferase 2) (NaMN adenylyltransferase 2) (Protein bloated bladder) (Blad) 307 34,505 Binding site (1); Chain (1); Frameshift (1); Lipidation (2); Mutagenesis (6); Nucleotide binding (3); Region (3) Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from nicotinamide D-ribonucleotide: step 1/1. Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1. FUNCTION: Nicotinamide/nicotinate-nucleotide adenylyltransferase that acts as an axon maintenance factor (PubMed:20126265, PubMed:23082226). Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP (By similarity). Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate but with a lower efficiency (By similarity). Cannot use triazofurin monophosphate (TrMP) as substrate (By similarity). Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+) (By similarity). For the pyrophosphorolytic activity prefers NAD(+), NADH and NaAD as substrates and degrades nicotinic acid adenine dinucleotide phosphate (NHD) less effectively (By similarity). Fails to cleave phosphorylated dinucleotides NADP(+), NADPH and NaADP(+) (By similarity). Axon survival factor required for the maintenance of healthy axons: acts by delaying Wallerian axon degeneration, an evolutionarily conserved process that drives the loss of damaged axons (PubMed:20126265, PubMed:23082226). {ECO:0000250|UniProtKB:Q9BZQ4, ECO:0000269|PubMed:20126265, ECO:0000269|PubMed:23082226}. PTM: Degraded in response to injured neurite (PubMed:20126265, PubMed:23665224, PubMed:23610559). Degradation is probably caused by ubiquitination by MYCBP2 (PubMed:23665224, PubMed:23610559). Ubiquitinated on threonine and/or serine residues by MYCBP2; consequences of threonine and/or serine ubiquitination are however unclear (By similarity). {ECO:0000250|UniProtKB:Q9BZQ4, ECO:0000269|PubMed:20126265, ECO:0000269|PubMed:23610559, ECO:0000269|PubMed:23665224}.; PTM: Palmitoylated; palmitoylation is required for membrane association. {ECO:0000269|PubMed:23610559}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:23610559}; Lipid-anchor {ECO:0000269|PubMed:23610559}. Cytoplasmic vesicle membrane; Lipid-anchor {ECO:0000269|PubMed:23610559}. Cytoplasm {ECO:0000250|UniProtKB:Q9BZQ4}. Cell projection, axon {ECO:0000269|PubMed:23610559}. Note=Delivered to axons with Golgi-derived cytoplasmic vesicles. {ECO:0000269|PubMed:23610559}. SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9BZQ4}. TISSUE SPECIFICITY: Expressed predominantly in the brain and nervous system. {ECO:0000269|PubMed:23082226}. +Q99JR6 NMNA3_MOUSE Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 3 (NMN/NaMN adenylyltransferase 3) (EC 2.7.7.1) (EC 2.7.7.18) (Nicotinamide-nucleotide adenylyltransferase 3) (NMN adenylyltransferase 3) (Nicotinate-nucleotide adenylyltransferase 3) (NaMN adenylyltransferase 3) 245 27,703 Binding site (3); Chain (1); Nucleotide binding (3); Region (3) Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from nicotinamide D-ribonucleotide: step 1/1. Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1. FUNCTION: Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate with the same efficiency. Can use triazofurin monophosphate (TrMP) as substrate. Can also use GTP and ITP as nucleotide donors. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). For the pyrophosphorolytic activity, can use NAD(+), NADH, NaAD, nicotinic acid adenine dinucleotide phosphate (NHD), nicotinamide guanine dinucleotide (NGD) as substrates. Fails to cleave phosphorylated dinucleotides NADP(+), NADPH and NaADP(+). Protects against axonal degeneration following injury. {ECO:0000269|PubMed:16914673}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16914673}. SUBUNIT: Homotetramer. {ECO:0000250}. +Q8K2T1 NMRL1_MOUSE NmrA-like family domain-containing protein 1 309 34,376 Alternative sequence (5); Binding site (2); Chain (1); Frameshift (1); Nucleotide binding (5); Region (1); Sequence conflict (1) FUNCTION: Redox sensor protein. Undergoes restructuring and subcellular redistribution in response to changes in intracellular NADPH/NADP(+) levels. At low NADPH concentrations the protein is found mainly as a monomer, and binds argininosuccinate synthase (ASS1), the enzyme involved in nitric oxide synthesis. Association with ASS1 impairs its activity and reduces the production of nitric oxide, which subsecuently prevents apoptosis. Under normal NADPH concentrations, the protein is found as a dimer and hides the binding site for ASS1. The homodimer binds one molecule of NADPH. Has higher affinity for NADPH than for NADP(+). Binding to NADPH is necessary to form a stable dimer (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region. Nucleus. Note=Under normal redox growth conditions localizes in the cytoplasm and perinuclear region. Nuclear localization is promoted by increased intracellular nitric oxide and reduced NADPH/NADP(+) ratios (By similarity). {ECO:0000250}. SUBUNIT: Homodimer. Interacts with ASS1. Interaction is enhanced by low NADPH/NADP(+) ratios, which results in inhibition of ASS1 activity (By similarity). {ECO:0000250}. +Q5H8A1 NMS_MOUSE Neuromedin-S 153 17,883 Modified residue (1); Peptide (1); Propeptide (4); Signal peptide (1) FUNCTION: Implicated in the regulation of circadian rhythms through autocrine and/or paracrine actions. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +O70310 NMT1_MOUSE Glycylpeptide N-tetradecanoyltransferase 1 (EC 2.3.1.97) (Myristoyl-CoA:protein N-myristoyltransferase 1) (NMT 1) (Type I N-myristoyltransferase) (Peptide N-myristoyltransferase 1) 496 56,888 Chain (1); Compositional bias (1); Modified residue (3); Region (3) FUNCTION: Adds a myristoyl group to the N-terminal glycine residue of certain cellular and viral proteins. Required for normal embryogenesis. {ECO:0000269|PubMed:15753093}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P30419}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P30419}. Membrane {ECO:0000250|UniProtKB:P30419}; Peripheral membrane protein {ECO:0000250|UniProtKB:P30419}. Note=Copurifies with ribosomes. {ECO:0000250|UniProtKB:P30419}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15753093}. +O70311 NMT2_MOUSE Glycylpeptide N-tetradecanoyltransferase 2 (EC 2.3.1.97) (Myristoyl-CoA:protein N-myristoyltransferase 2) (NMT 2) (Peptide N-myristoyltransferase 2) (Type II N-myristoyltransferase) 529 60,484 Chain (1); Compositional bias (1); Modified residue (1); Region (3) FUNCTION: Adds a myristoyl group to the N-terminal glycine residue of certain cellular and viral proteins. {ECO:0000250|UniProtKB:O60551}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O60551}. Membrane {ECO:0000250|UniProtKB:O60551}; Peripheral membrane protein {ECO:0000250|UniProtKB:O60551}. +O55040 NMUR1_MOUSE Neuromedin-U receptor 1 (NMU-R1) (G-protein coupled receptor 66) (G-protein coupled receptor FM-3) 428 47,934 Chain (1); Disulfide bond (1); Erroneous gene model prediction (1); Erroneous initiation (2); Glycosylation (2); Topological domain (8); Transmembrane (7) TRANSMEM 60 80 Helical; Name=1. {ECO:0000255}.; TRANSMEM 97 117 Helical; Name=2. {ECO:0000255}.; TRANSMEM 138 158 Helical; Name=3. {ECO:0000255}.; TRANSMEM 182 202 Helical; Name=4. {ECO:0000255}.; TRANSMEM 236 256 Helical; Name=5. {ECO:0000255}.; TRANSMEM 295 315 Helical; Name=6. {ECO:0000255}.; TRANSMEM 340 360 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 59 Extracellular. {ECO:0000255}.; TOPO_DOM 81 96 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 118 137 Extracellular. {ECO:0000255}.; TOPO_DOM 159 181 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 203 235 Extracellular. {ECO:0000255}.; TOPO_DOM 257 294 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 316 339 Extracellular. {ECO:0000255}.; TOPO_DOM 361 428 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for the neuromedin-U and neuromedin-S neuropeptides. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:9782091}. +A2ABV5 MED14_MOUSE Mediator of RNA polymerase II transcription subunit 14 (Cofactor required for Sp1 transcriptional activation subunit 2) (CRSP complex subunit 2) (Mediator complex subunit 14) (Thyroid hormone receptor-associated protein complex 170 kDa component) (Trap170) 1459 160,966 Alternative sequence (6); Chain (1); Compositional bias (2); Modified residue (7); Motif (2); Region (2); Sequence conflict (2) FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Component of the Mediator complex, which is composed of MED1, MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L, MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23, MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8 subunits form a distinct module termed the CDK8 module. Mediator containing the CDK8 module is less active than Mediator lacking this module in supporting transcriptional activation. Individual preparations of the Mediator complex lacking one or more distinct subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and TRAP. Interacts with AR, ESR1, SREBF1 and STAT2 (By similarity). Interacts with GATA1. {ECO:0000250, ECO:0000269|PubMed:17132730}. +Q61979 NNAT_MOUSE Neuronatin 81 9,211 Alternative sequence (1); Chain (1); Sequence caution (1) FUNCTION: May participate in the maintenance of segment identity in the hindbrain and pituitary development, and maturation or maintenance of the overall structure of the nervous system. TISSUE SPECIFICITY: Highest in brain and ovary. +O55239 NNMT_MOUSE Nicotinamide N-methyltransferase (EC 2.1.1.1) 264 29,598 Beta strand (12); Binding site (5); Chain (1); Helix (11); Region (3); Turn (3) FUNCTION: Catalyzes the N-methylation of nicotinamide and other pyridines to form pyridinium ions. This activity is important for biotransformation of many drugs and xenobiotic compounds. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Monomer. {ECO:0000250}. +Q9CZ42 NNRD_MOUSE ATP-dependent (S)-NAD(P)H-hydrate dehydratase (EC 4.2.1.93) (ATP-dependent NAD(P)HX dehydratase) (Carbohydrate kinase domain-containing protein) (NAD(P)HX dehydratase) 343 36,717 Alternative sequence (2); Binding site (2); Chain (1); Domain (1); Modified residue (3); Nucleotide binding (2); Region (1); Sequence conflict (1); Transit peptide (1) FUNCTION: Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ATP, which is converted to ADP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. {ECO:0000255|HAMAP-Rule:MF_03157, ECO:0000269|PubMed:21994945}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03157, ECO:0000269|PubMed:18614015}. +Q99K74 MED24_MOUSE Mediator of RNA polymerase II transcription subunit 24 (Mediator complex subunit 24) (Thyroid hormone receptor-associated protein 4) (Thyroid hormone receptor-associated protein complex 100 kDa component) (Trap100) (mTRAP100) 987 109,985 Alternative sequence (4); Chain (1); Modified residue (2); Motif (6); Sequence conflict (10) FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). Required for basal and activator-dependent transcription. {ECO:0000250, ECO:0000269|PubMed:10406464, ECO:0000269|PubMed:12093747}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Component of the Mediator complex, which is composed of MED1, MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L, MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23, MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8 subunits form a distinct module termed the CDK8 module. Mediator containing the CDK8 module is less active than Mediator lacking this module in supporting transcriptional activation. Individual preparations of the Mediator complex lacking one or more distinct subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and TRAP. Interacts with AR (By similarity). Interacts with MED1 and MED10. {ECO:0000250, ECO:0000269|PubMed:10406464, ECO:0000269|PubMed:12093747}. TISSUE SPECIFICITY: Expressed in the adrenal gland, brain, epididymis, heart, kidney, liver, ovary, pancreas, prostate, skeletal muscle, small intestine, spleen, stomach, testis and thymus. {ECO:0000269|PubMed:10406464, ECO:0000269|PubMed:12093747}. +Q9CQI9 MED30_MOUSE Mediator of RNA polymerase II transcription subunit 30 (Mediator complex subunit 30) (Thyroid hormone receptor-associated protein 6) (Thyroid hormone receptor-associated protein complex 25 kDa component) (Trap25) 178 20,358 Chain (1); Coiled coil (1); Initiator methionine (1); Modified residue (1) FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Component of the Mediator complex, which is composed of MED1, MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L, MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23, MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8 subunits form a distinct module termed the CDK8 module. Mediator containing the CDK8 module is less active than Mediator lacking this module in supporting transcriptional activation. Individual preparations of the Mediator complex lacking one or more distinct subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and TRAP (By similarity). {ECO:0000250}. +Q8K4Z3 NNRE_MOUSE NAD(P)H-hydrate epimerase (EC 5.1.99.6) (Apolipoprotein A-I-binding protein) (AI-BP) (NAD(P)HX epimerase) 282 30,973 Beta strand (9); Binding site (1); Chain (1); Domain (1); Helix (9); Metal binding (3); Modified residue (2); Region (2); Transit peptide (1); Turn (2) FUNCTION: Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX. {ECO:0000250|UniProtKB:Q8NCW5, ECO:0000255|HAMAP-Rule:MF_03159}. PTM: Undergoes physiological phosphorylation during sperm capacitation, downstream to PKA activation. {ECO:0000255|HAMAP-Rule:MF_03159, ECO:0000269|PubMed:18202122}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03159}. Secreted {ECO:0000255|HAMAP-Rule:MF_03159, ECO:0000269|PubMed:18202122, ECO:0000269|PubMed:18614015}. Note=In sperm, secretion gradually increases during capacitation. SUBUNIT: Interacts with APOA1 and APOA2 (By similarity). Homodimer. {ECO:0000250, ECO:0000269|PubMed:18202122}. TISSUE SPECIFICITY: Detected in testis and sperm (at protein level). Expressed at high levels in heart, liver, kidney, and testis. {ECO:0000269|PubMed:18202122}. +Q9CQA5 MED4_MOUSE Mediator of RNA polymerase II transcription subunit 4 (Mediator complex subunit 4) 270 29,781 Alternative sequence (2); Chain (1); Coiled coil (1); Compositional bias (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (2) FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the Mediator complex, which is composed of MED1, MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L, MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23, MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8 subunits form a distinct module termed the CDK8 module. Mediator containing the CDK8 module is less active than Mediator lacking this module in supporting transcriptional activation. Individual preparations of the Mediator complex lacking one or more distinct subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and TRAP (By similarity). {ECO:0000250}. +Q9QZV9 NXT1_MOUSE NTF2-related export protein 1 140 15,847 Chain (1); Domain (1); Initiator methionine (1); Modified residue (1); Sequence conflict (1) FUNCTION: Stimulator of protein export for NES-containing proteins. Also plays a role in the nuclear export of U1 snRNA, tRNA, and mRNA. The NXF1-NXT1 heterodimer is involved in the export of HSP70 mRNA in conjunction with ALYREF/THOC4 and THOC5 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Nucleus speckle {ECO:0000250}. Cytoplasm. Note=Shuttles between the nucleus and the cytoplasm. SUBUNIT: Heterodimer with NXF1. Forms a complex with RANGAP1, RANBP2/NUP358 and NXF1. Interacts (via NTF2 domain) with NXF1. Stabilizes the NTF2 domain of NXF1 by heterodimerization. The formation of NXF1-NXT1 heterodimers is required for the NXF1-mediated nuclear mRNA export. Preferentially binds Ran-GTP. Associates with NXF2, NXF3 and NXF5. Does not bind nucleoporins (NPC) directly, its association to NPC is mediated by NXF1. {ECO:0000250|UniProtKB:Q9UKK6}. +Q61885 MOG_MOUSE Myelin-oligodendrocyte glycoprotein 246 28,271 Beta strand (9); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (1); Helix (4); Sequence conflict (4); Signal peptide (1); Topological domain (3); Transmembrane (2); Turn (1) TRANSMEM 157 177 Helical. {ECO:0000255}.; TRANSMEM 210 230 Helical. {ECO:0000255}. TOPO_DOM 29 156 Extracellular. {ECO:0000255}.; TOPO_DOM 178 209 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 231 246 Extracellular. {ECO:0000255}. FUNCTION: Minor component of the myelin sheath. May be involved in completion and/or maintenance of the myelin sheath and in cell-cell communication. Mediates homophilic cell-cell adhesion. {ECO:0000269|PubMed:12960396}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SUBUNIT: Homodimer. {ECO:0000269|PubMed:12960396}. TISSUE SPECIFICITY: Found exclusively in the CNS, where it is localized on the surface of myelin and oligodendrocyte cytoplasmic membranes. Reduced expression levels are observed in jimpy and quacking dysmyelinating mutant mice. {ECO:0000269|PubMed:1373175}. +Q8VFK1 O1009_MOUSE Olfactory receptor 1009 (Olfactory receptor 175-3) 314 35,458 Chain (1); Disulfide bond (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 26 46 Helical; Name=1. {ECO:0000255}.; TRANSMEM 55 75 Helical; Name=2. {ECO:0000255}.; TRANSMEM 100 120 Helical; Name=3. {ECO:0000255}.; TRANSMEM 134 154 Helical; Name=4. {ECO:0000255}.; TRANSMEM 197 217 Helical; Name=5. {ECO:0000255}.; TRANSMEM 238 258 Helical; Name=6. {ECO:0000255}.; TRANSMEM 272 292 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 25 Extracellular. {ECO:0000255}.; TOPO_DOM 47 54 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 76 99 Extracellular. {ECO:0000255}.; TOPO_DOM 121 133 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 155 196 Extracellular. {ECO:0000255}.; TOPO_DOM 218 237 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 259 271 Extracellular. {ECO:0000255}.; TOPO_DOM 293 314 Cytoplasmic. {ECO:0000255}. FUNCTION: Potential odorant receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q8CE94 MOT13_MOUSE Monocarboxylate transporter 13 (MCT 13) (Solute carrier family 16 member 13) 428 44,862 Chain (1); Erroneous initiation (1); Sequence conflict (6); Topological domain (2); Transmembrane (12) TRANSMEM 11 31 Helical. {ECO:0000255}.; TRANSMEM 52 72 Helical. {ECO:0000255}.; TRANSMEM 81 101 Helical. {ECO:0000255}.; TRANSMEM 106 126 Helical. {ECO:0000255}.; TRANSMEM 139 159 Helical. {ECO:0000255}.; TRANSMEM 172 192 Helical. {ECO:0000255}.; TRANSMEM 221 241 Helical. {ECO:0000255}.; TRANSMEM 244 264 Helical. {ECO:0000255}.; TRANSMEM 283 303 Helical. {ECO:0000255}.; TRANSMEM 306 326 Helical. {ECO:0000255}.; TRANSMEM 338 358 Helical. {ECO:0000255}.; TRANSMEM 374 394 Helical. {ECO:0000255}. TOPO_DOM 1 10 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 395 428 Cytoplasmic. {ECO:0000255}. FUNCTION: Proton-linked monocarboxylate transporter. May catalyze the transport of monocarboxylates across the plasma membrane. {ECO:0000250|UniProtKB:Q7RTY0}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q7RTY0}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q7RTY0}. Cell membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. +Q63932 MP2K2_MOUSE Dual specificity mitogen-activated protein kinase kinase 2 (MAP kinase kinase 2) (MAPKK 2) (EC 2.7.12.2) (ERK activator kinase 2) (MAPK/ERK kinase 2) (MEK 2) 401 44,402 Active site (1); Binding site (1); Chain (1); Compositional bias (1); Domain (1); Modified residue (9); Mutagenesis (1); Nucleotide binding (1); Sequence conflict (1); Site (1) FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. Activates the ERK1 and ERK2 MAP kinases. {ECO:0000269|PubMed:19219045}. PTM: Phosphorylation on Ser/Thr by MAP kinase kinase kinases (RAF or MEKK1) regulates positively the kinase activity. Phosphorylated by MAP2K1/MEK1. Low levels of autophosphorylation have been observed. {ECO:0000269|PubMed:19219045}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane {ECO:0000269|PubMed:10409742}; Peripheral membrane protein {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. SUBUNIT: Interacts with MORG1 (PubMed:15118098). Interacts with SGK1 (By similarity). Interacts KSR1 (PubMed:10409742). {ECO:0000250|UniProtKB:P36507, ECO:0000269|PubMed:10409742, ECO:0000269|PubMed:15118098}. TISSUE SPECIFICITY: Expressed in adult intestine, kidney, liver, lung, pancreas, spleen, thymus, and at high levels in the neonatal brain. Lower expression is found in adult brain and heart. +Q8VES2 O1102_MOUSE Olfactory receptor 1102 (Olfactory receptor 179-4) 324 36,292 Chain (1); Disulfide bond (1); Glycosylation (3); Sequence conflict (3); Topological domain (8); Transmembrane (7) TRANSMEM 38 58 Helical; Name=1. {ECO:0000255}.; TRANSMEM 67 87 Helical; Name=2. {ECO:0000255}.; TRANSMEM 112 132 Helical; Name=3. {ECO:0000255}.; TRANSMEM 146 166 Helical; Name=4. {ECO:0000255}.; TRANSMEM 209 229 Helical; Name=5. {ECO:0000255}.; TRANSMEM 250 270 Helical; Name=6. {ECO:0000255}.; TRANSMEM 284 304 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 37 Extracellular. {ECO:0000255}.; TOPO_DOM 59 66 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 88 111 Extracellular. {ECO:0000255}.; TOPO_DOM 133 145 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 167 208 Extracellular. {ECO:0000255}.; TOPO_DOM 230 249 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 271 283 Extracellular. {ECO:0000255}.; TOPO_DOM 305 324 Cytoplasmic. {ECO:0000255}. FUNCTION: Potential odorant receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +B1AT66 MOT7_MOUSE Monocarboxylate transporter 7 (MCT 7) (Monocarboxylate transporter 6) (MCT 6) (Solute carrier family 16 member 6) 607 66,236 Alternative sequence (1); Chain (1); Modified residue (4); Sequence conflict (3); Topological domain (13); Transmembrane (12) TRANSMEM 106 126 Helical. {ECO:0000255}.; TRANSMEM 147 167 Helical. {ECO:0000255}.; TRANSMEM 176 196 Helical. {ECO:0000255}.; TRANSMEM 203 223 Helical. {ECO:0000255}.; TRANSMEM 234 254 Helical. {ECO:0000255}.; TRANSMEM 269 289 Helical. {ECO:0000255}.; TRANSMEM 384 404 Helical. {ECO:0000255}.; TRANSMEM 415 435 Helical. {ECO:0000255}.; TRANSMEM 443 463 Helical. {ECO:0000255}.; TRANSMEM 466 486 Helical. {ECO:0000255}.; TRANSMEM 508 528 Helical. {ECO:0000255}.; TRANSMEM 537 557 Helical. {ECO:0000255}. TOPO_DOM 1 105 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 127 146 Extracellular. {ECO:0000255}.; TOPO_DOM 168 175 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 197 202 Extracellular. {ECO:0000255}.; TOPO_DOM 224 233 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 255 268 Extracellular. {ECO:0000255}.; TOPO_DOM 290 383 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 405 414 Extracellular. {ECO:0000255}.; TOPO_DOM 436 442 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 464 465 Extracellular. {ECO:0000255}.; TOPO_DOM 487 507 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 529 536 Extracellular. {ECO:0000255}.; TOPO_DOM 558 607 Cytoplasmic. {ECO:0000255}. FUNCTION: Proton-linked monocarboxylate transporter. Catalyzes the rapid transport across the plasma membrane of many monocarboxylates such as lactate, pyruvate, branched-chain oxo acids derived from leucine, valine and isoleucine, and the ketone bodies acetoacetate, beta-hydroxybutyrate and acetate (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +O70324 MOT8_MOUSE Monocarboxylate transporter 8 (MCT 8) (Solute carrier family 16 member 2) (X-linked PEST-containing transporter) 545 60,025 Chain (1); Initiator methionine (1); Modified residue (2); Region (1); Repeat (2); Sequence conflict (2); Topological domain (13); Transmembrane (12) TRANSMEM 103 123 Helical. {ECO:0000255}.; TRANSMEM 150 170 Helical. {ECO:0000255}.; TRANSMEM 178 198 Helical. {ECO:0000255}.; TRANSMEM 207 227 Helical. {ECO:0000255}.; TRANSMEM 236 256 Helical. {ECO:0000255}.; TRANSMEM 265 285 Helical. {ECO:0000255}.; TRANSMEM 329 349 Helical. {ECO:0000255}.; TRANSMEM 363 383 Helical. {ECO:0000255}.; TRANSMEM 393 413 Helical. {ECO:0000255}.; TRANSMEM 416 436 Helical. {ECO:0000255}.; TRANSMEM 454 474 Helical. {ECO:0000255}.; TRANSMEM 484 504 Helical. {ECO:0000255}. TOPO_DOM 2 102 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 124 149 Extracellular. {ECO:0000255}.; TOPO_DOM 171 177 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 199 206 Extracellular. {ECO:0000255}.; TOPO_DOM 228 235 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 257 264 Extracellular. {ECO:0000255}.; TOPO_DOM 286 328 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 350 362 Extracellular. {ECO:0000255}.; TOPO_DOM 384 392 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 414 415 Extracellular. {ECO:0000255}.; TOPO_DOM 437 453 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 475 483 Extracellular. {ECO:0000255}.; TOPO_DOM 505 545 Cytoplasmic. {ECO:0000255}. FUNCTION: Very active and specific thyroid hormone transporter. Stimulates cellular uptake of thyroxine (T4), triiodothyronine (T3), reverse triiodothyronine (rT3) and diidothyronine. Does not transport Leu, Phe, Trp or Tyr. {ECO:0000250|UniProtKB:Q8K1P8}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8K1P8}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8K1P8}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P36021}. TISSUE SPECIFICITY: Highly expressed in liver and kidney. +Q91WW3 MRGA3_MOUSE Mas-related G-protein coupled receptor member A3 302 34,483 Chain (1); Glycosylation (3); Topological domain (8); Transmembrane (7) TRANSMEM 18 38 Helical; Name=1. {ECO:0000255}.; TRANSMEM 47 67 Helical; Name=2. {ECO:0000255}.; TRANSMEM 82 102 Helical; Name=3. {ECO:0000255}.; TRANSMEM 130 150 Helical; Name=4. {ECO:0000255}.; TRANSMEM 168 188 Helical; Name=5. {ECO:0000255}.; TRANSMEM 212 232 Helical; Name=6. {ECO:0000255}.; TRANSMEM 243 263 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 17 Extracellular. {ECO:0000255}.; TOPO_DOM 39 46 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 68 81 Extracellular. {ECO:0000255}.; TOPO_DOM 103 129 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 151 167 Extracellular. {ECO:0000255}.; TOPO_DOM 189 211 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 233 242 Extracellular. {ECO:0000255}.; TOPO_DOM 264 302 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan receptor. May be a receptor for RFamide-family neuropeptides such as NPFF and NPAF, which are analgesic in vivo. May regulate nociceptor function and/or development, including the sensation or modulation of pain (By similarity). Activated by the antimalarial drug chloroquine. Mediates chloroquine-induced itch, in a histamine-independent manner. {ECO:0000250, ECO:0000269|PubMed:20004959}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed exclusively in dorsal root ganglia and nodose ganglia. Expressed in a subset of sensory neurons that includes nociceptors. Expressed in the subclass of non-peptidergic sensory neurons that are IB4(+) and VR1(-). {ECO:0000269|PubMed:11551509, ECO:0000269|PubMed:20004959}. +Q91ZC4 MRGA8_MOUSE Mas-related G-protein coupled receptor member A8 305 35,004 Chain (1); Glycosylation (2); Topological domain (8); Transmembrane (7) TRANSMEM 18 38 Helical; Name=1. {ECO:0000255}.; TRANSMEM 47 67 Helical; Name=2. {ECO:0000255}.; TRANSMEM 86 106 Helical; Name=3. {ECO:0000255}.; TRANSMEM 130 150 Helical; Name=4. {ECO:0000255}.; TRANSMEM 173 193 Helical; Name=5. {ECO:0000255}.; TRANSMEM 208 228 Helical; Name=6. {ECO:0000255}.; TRANSMEM 244 264 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 17 Extracellular. {ECO:0000255}.; TOPO_DOM 39 46 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 68 85 Extracellular. {ECO:0000255}.; TOPO_DOM 107 129 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 151 172 Extracellular. {ECO:0000255}.; TOPO_DOM 194 207 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 229 243 Extracellular. {ECO:0000255}.; TOPO_DOM 265 305 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan receptor. May be a receptor for RFamide-family neuropeptides such as NPFF and NPAF, which are analgesic in vivo. May regulate nociceptor function and/or development, including the sensation or modulation of pain (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed in a subset of sensory neurons that includes nociceptors. Expressed in the subclass of non-peptidergic sensory neurons that are IB4(+) and VR1(-). +Q9CPY0 MRM2_MOUSE rRNA methyltransferase 2, mitochondrial (EC 2.1.1.-) (16S rRNA (uridine(1369)-2'-O)-methyltransferase) (16S rRNA [Um1369] 2'-O-methyltransferase) (Protein ftsJ homolog 2) 246 27,145 Active site (1); Binding site (2); Chain (1); Region (2); Transit peptide (1) FUNCTION: S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of 2'-O-methyluridine at position 1369 (Um1369) in the 16S mitochondrial large subunit ribosomal RNA (mtLSU rRNA), a universally conserved modification in the peptidyl transferase domain of the mtLSU rRNA. {ECO:0000250|UniProtKB:Q9UI43}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:24036117}. +O35379 MRP1_MOUSE Multidrug resistance-associated protein 1 (ATP-binding cassette sub-family C member 1) (Leukotriene C(4) transporter) (LTC4 transporter) 1528 171,185 Chain (1); Domain (4); Glycosylation (2); Modified residue (7); Nucleotide binding (2); Topological domain (18); Transmembrane (17) TRANSMEM 34 54 Helical; Name=1. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 75 95 Helical; Name=2. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 101 121 Helical; Name=3. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 134 154 Helical; Name=4. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 173 193 Helical; Name=5. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 318 338 Helical; Name=6. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 365 385 Helical; Name=7. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 442 462 Helical; Name=8. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 466 486 Helical; Name=9. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 549 569 Helical; Name=10. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 592 612 Helical; Name=11. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 964 984 Helical; Name=12. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 1023 1043 Helical; Name=13. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 1087 1107 Helical; Name=14. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 1109 1129 Helical; Name=15. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 1201 1221 Helical; Name=16. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 1224 1244 Helical; Name=17. {ECO:0000255|PROSITE-ProRule:PRU00441}. TOPO_DOM 1 33 Extracellular. {ECO:0000250}.; TOPO_DOM 55 74 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 96 100 Extracellular. {ECO:0000250}.; TOPO_DOM 122 133 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 155 172 Extracellular. {ECO:0000250}.; TOPO_DOM 194 317 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 339 364 Extracellular. {ECO:0000250}.; TOPO_DOM 386 441 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 463 465 Extracellular. {ECO:0000250}.; TOPO_DOM 487 548 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 570 591 Extracellular. {ECO:0000250}.; TOPO_DOM 613 963 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 985 1022 Extracellular. {ECO:0000250}.; TOPO_DOM 1044 1086 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 1108 1108 Extracellular. {ECO:0000250}.; TOPO_DOM 1130 1200 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 1222 1223 Extracellular. {ECO:0000250}.; TOPO_DOM 1245 1528 Cytoplasmic. {ECO:0000250}. FUNCTION: Mediates export of organic anions and drugs from the cytoplasm. Mediates ATP-dependent transport of glutathione and glutathione conjugates, leukotriene C4, estradiol-17-beta-o-glucuronide, methotrexate, antiviral drugs and other xenobiotics. Confers resistance to anticancer drugs. Hydrolyzes ATP with low efficiency. {ECO:0000269|PubMed:9281595}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. +Q6NVG5 MREG_MOUSE Melanoregulin (Dilute suppressor protein) (Whn-dependent transcript 2) 214 25,010 Chain (1); Compositional bias (1); Helix (7); Modified residue (1); Motif (1); Mutagenesis (8) FUNCTION: Probably functions as cargo-recognition protein that couples cytoplasmic vesicles to the transport machinery (PubMed:22940130, PubMed:22275436, PubMed:30174147). Plays a role in hair pigmentation, a process that involves shedding of melanosome-containing vesicles from melanocytes, followed by phagocytosis of the melanosome-containing vesicles by keratinocytes (PubMed:15550542, PubMed:3410303, PubMed:22753477). Functions on melanosomes as receptor for RILP and the complex formed by RILP and DCTN1, and thereby contributes to retrograde melanosome transport from the cell periphery to the center (PubMed:22940130, PubMed:22275436). Overexpression causes accumulation of late endosomes and/or lysosomes at the microtubule organising center (MTOC) at the center of the cell (PubMed:19240024, PubMed:30174147). Probably binds cholesterol and requires the presence of cholesterol in membranes to function in microtubule-mediated retrograde organelle transport (PubMed:30174147). Binds phosphatidylinositol 3-phosphate, phosphatidylinositol 4-phosphate, phosphatidylinositol 5-phosphate and phosphatidylinositol 3,5-bisphosphate, but not phosphatidylinositol 3,4-bisphosphate or phosphatidylinositol 4,5-bisphosphate (PubMed:19240024). Required for normal phagosome clearing and normal activation of lysosomal enzymes in lysosomes from retinal pigment epithelium cells (PubMed:19240024). Required for normal degradation of the lipofuscin component N-retinylidene-N-retinylethanolamine (A2E) in the eye (PubMed:19240024). May function in membrane fusion and regulate the biogenesis of disk membranes of photoreceptor rod cells (Probable). {ECO:0000269|PubMed:15550542, ECO:0000269|PubMed:19240024, ECO:0000269|PubMed:22275436, ECO:0000269|PubMed:22753477, ECO:0000269|PubMed:22940130, ECO:0000269|PubMed:30174147, ECO:0000269|PubMed:3410303, ECO:0000305|PubMed:17260955}. PTM: Palmitoylated. Palmitoylation is required to maintain the protein at the melanosome membrane. {ECO:0000269|PubMed:22940130}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:17260955}; Peripheral membrane protein {ECO:0000269|PubMed:17260955}. Melanosome membrane {ECO:0000269|PubMed:22275436, ECO:0000269|PubMed:22940130}; Lipid-anchor {ECO:0000269|PubMed:22940130}. Lysosome membrane {ECO:0000269|PubMed:22940130, ECO:0000269|PubMed:30174147}; Lipid-anchor {ECO:0000269|PubMed:22940130}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:19240024}. Note=Localizes to the inner segment and basal outer segment of rods in the retina. {ECO:0000269|PubMed:17260955}. SUBUNIT: Identified in a complex with RILP and DCTN1; interacts directly with RILP, but does not interact directly with DCTN1 (PubMed:22275436). Interacts with PRPH2 (PubMed:17260955). {ECO:0000269|PubMed:17260955, ECO:0000269|PubMed:22275436}. TISSUE SPECIFICITY: Detected in melanocytes (PubMed:15550542). Expressed in retina, in retinal pigment epithelium (at protein level) (PubMed:17260955, PubMed:19240024). Widely expressed with higher expression in skin, heart, liver, testis and thymus (PubMed:15550542). Detected in retina, in retinal pigment epithelium cells (PubMed:19240024). {ECO:0000269|PubMed:15550542, ECO:0000269|PubMed:17260955, ECO:0000269|PubMed:19240024}. +Q3UN70 MRFL_MOUSE Myelin regulatory factor-like protein 904 101,689 Chain (1); Coiled coil (1); DNA binding (1); Domain (1); Sequence conflict (1); Transmembrane (1) TRANSMEM 624 644 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +P54369 OAZ1_MOUSE Ornithine decarboxylase antizyme 1 (ODC-Az) 227 25,133 Chain (1); Sequence conflict (1) FUNCTION: Ornithine decarboxylase (ODC) antizyme protein that negatively regulates ODC activity and intracellular polyamine biosynthesis and uptake in response to increased intracellular polyamine levels. Binds to ODC monomers, inhibiting the assembly of the functional ODC homodimer, and targets the monomers for ubiquitin-independent proteolytic destruction by the 26S proteasome (PubMed:16916800, PubMed:18508777). Triggers ODC degradation by inducing the exposure of a cryptic proteasome-interacting surface of ODC (By similarity). Stabilizes AZIN2 by interfering with its ubiquitination (PubMed:18062773). Also inhibits cellular uptake of polyamines by inactivating the polyamine uptake transporter. SMAD1/OAZ1/PSMB4 complex mediates the degradation of the CREBBP/EP300 repressor SNIP1. Involved in the translocation of AZIN2 from ER-Golgi intermediate compartment (ERGIC) to the cytosol (PubMed:19449338). {ECO:0000250|UniProtKB:P54368, ECO:0000269|PubMed:16916800, ECO:0000269|PubMed:18062773, ECO:0000269|PubMed:18508777, ECO:0000269|PubMed:19449338}. SUBUNIT: Interacts with ODC1 and thereby sterically blocks ODC homodimerization (By similarity). Forms a ternary complex with PSMB4 and OAZ1 before PSMB4 is incorporated into the 20S proteasome (By similarity). Interacts with AZIN2; this interaction disrupts the interaction between the antizyme and ODC1 (PubMed:16916800, PubMed:18062773, PubMed:24967154). {ECO:0000250|UniProtKB:P54368, ECO:0000269|PubMed:16916800, ECO:0000269|PubMed:18062773, ECO:0000269|PubMed:24967154}. +Q9WVG9 MS3L1_MOUSE Male-specific lethal 3 homolog (Male-specific lethal-3 homolog 1) (Male-specific lethal-3 protein-like 1) (MSL3-like 1) 525 60,292 Alternative sequence (2); Chain (1); Domain (2); Modified residue (7); Region (1) FUNCTION: May be involved in chromatin remodeling and transcriptional regulation. May have a role in X inactivation. Component of the MSL complex which is responsible for the majority of histone H4 acetylation at 'Lys-16' which is implicated in the formation of higher-order chromatin structure. Specifically recognizes histone H4 monomethylated at 'Lys-20' (H4K20Me1) in a DNA-dependent manner and is proposed to be involved in chromosomal targeting of the MSL complex (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00972}. SUBUNIT: Component the MSL histone acetyltransferase complex at least composed of the MOF/MYST1, MSL1/hampin, MSL2 and MSL3. Interacts (via the MRG domain) with MSL1. {ECO:0000269|PubMed:21217699}. +Q8BU85 MSRB3_MOUSE Methionine-R-sulfoxide reductase B3, mitochondrial (MsrB3) (EC 1.8.4.12) (EC 1.8.4.14) 253 26,832 Active site (1); Chain (1); Domain (1); Erroneous initiation (3); Metal binding (4); Modified residue (2); Motif (1); Signal peptide (1) FUNCTION: Catalyzes the reduction of free and protein-bound methionine sulfoxide to methionine. {ECO:0000250|UniProtKB:Q8IXL7}. SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:15249228}. Note=Not detected in the mitochondrion. SUBUNIT: Monomer. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. Detected in the sensory epithelia of the organ of Corti and vestibular end organs as early as P2 up to adulthood (at protein level). In the organ of Corti, present in inner and outer hair cells and, to a lesser extent, in supporting cells (at protein level). In hair cells, distributed throughout the cell body. Barely detectable level in stereocilia. Also observed in spiral ganglion neurons, but not in the stria vascularis. In the vestibular end organs, found throughout the sensory epithelium, but more intense expression in hair cells than in supporting cells (at protein level). In vestibular hair cells, present within cell bodies and to a lesser extent in kinocilia. Barely detectable in stereocilia. {ECO:0000269|PubMed:21185009}. +Q8K1H9 OBP2A_MOUSE Odorant-binding protein 2a (Epididymal-specific lipocalin-13) 176 19,996 Chain (1); Disulfide bond (1); Glycosylation (2); Signal peptide (1) FUNCTION: May play a role in male fertility. May act as a retinoid carrier protein within the epididymis. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. TISSUE SPECIFICITY: Expressed in epididymis. {ECO:0000269|PubMed:15363845}. +Q2YDW2 MSTO1_MOUSE Protein misato homolog 1 556 61,230 Alternative sequence (1); Chain (1); Modified residue (1); Sequence conflict (9) FUNCTION: Involved in the regulation of mitochondrial distribution and morphology. Required for mitochondrial fusion and mitochondrial network formation. {ECO:0000250|UniProtKB:Q9BUK6}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q9BUK6}. Cytoplasm {ECO:0000250|UniProtKB:Q9BUK6}. +Q7TNB4 MSTRO_MOUSE Protein maestro (Male-specific transcription in the developing reproductive organs) 248 28,567 Chain (1); Repeat (1); Sequence conflict (2) SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12889070}. TISSUE SPECIFICITY: Prominent expression seen in testis, brain, liver and heart. Weakly expressed in the kidney. {ECO:0000269|PubMed:12889070}. +Q99JI1 MSTN1_MOUSE Musculoskeletal embryonic nuclear protein 1 82 8,941 Chain (1); Modified residue (2); Motif (1) FUNCTION: May be involved in the development and regeneration of the musculoskeletal system. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +P70354 MSX3_MOUSE Homeobox protein MSX-3 204 21,971 Chain (1); DNA binding (1); Erroneous initiation (1); Sequence conflict (1) FUNCTION: Acts as a potent transcriptional repressor of MSX1. {ECO:0000269|PubMed:11115394}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:11115394}. SUBUNIT: Interacts with CREBBP/CBP, NOTCH1/p300 and HDAC1. Appears to exist in two distinct complexes in the cell, one which includes CREBBP and NOTCH1 and the other which contains HDAC1. {ECO:0000269|PubMed:11115394}. TISSUE SPECIFICITY: Restricted to the dorsal embryonic central nervous system. +Q8BVN4 MTEF4_MOUSE Transcription termination factor 4, mitochondrial (Mitochondrial transcription termination factor 4) (mTERF domain-containing protein 2) 346 40,249 Chain (1); Erroneous initiation (2); Region (1); Repeat (5); Sequence conflict (2); Transit peptide (1) FUNCTION: Regulator of mitochondrial ribosome biogenesis and translation. Binds to mitochondrial ribosomal RNAs 16S, 12S and 7S (By similarity). Targets NSUN4 RNA methyltransferase to the mitochondrial large ribosomal subunit. {ECO:0000250, ECO:0000269|PubMed:21531335}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:21531335}. SUBUNIT: Heterodimer with NSUN4; this interaction may be required for NSUN4 recruitment to the mitochondrial large ribosomal subunit. {ECO:0000250}. DOMAIN: The MTERF repeats form a half-donut shaped, right-handed superhelix, where the concave side displays a positively charged path for nucleic acid interaction. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed, with highest levels in liver, followed by testis, kidney and brain. {ECO:0000269|PubMed:21531335}. +Q3URQ7 MTHSD_MOUSE Methenyltetrahydrofolate synthase domain-containing protein 372 40,789 Alternative sequence (3); Chain (1); Domain (1) +Q9Z2D1 MTMR2_MOUSE Myotubularin-related protein 2 (Phosphatidylinositol-3,5-bisphosphate 3-phosphatase) (EC 3.1.3.95) (Phosphatidylinositol-3-phosphate phosphatase) (EC 3.1.3.64) 643 73,232 Active site (1); Binding site (1); Chain (1); Coiled coil (1); Compositional bias (1); Domain (2); Erroneous initiation (1); Modified residue (3); Mutagenesis (2); Region (3) FUNCTION: Phosphatase that acts on lipids with a phosphoinositol headgroup. Has phosphatase activity towards phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5-bisphosphate. Binds phosphatidylinositol 4-phosphate, phosphatidylinositol 5-phosphate, phosphatidylinositol 3,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate. {ECO:0000269|PubMed:12045210}. PTM: Phosphorylation at Ser-58 decreases MTMR2 localization to endocytic vesicular structures. {ECO:0000250|UniProtKB:Q13614}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14530412}. Early endosome membrane {ECO:0000250|UniProtKB:Q13614}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q13614}. Note=Partly associated with membranes. {ECO:0000250|UniProtKB:Q13614}. SUBUNIT: Homooligomer and heterooligomer. Interacts with SBF1 and SBF2 (By similarity). {ECO:0000250|UniProtKB:Q13614}. TISSUE SPECIFICITY: Detected in fetal forebrain, dorsal root ganglia, trigeminal ganglia, kidney, adrenal gland and lung. Detected in adult dorsal root ganglia, neurons of the central nervous system, motor neurons, cell soma and neurites of sensory neurons, olfactory bulb, cerebellum and hippocampus. {ECO:0000269|PubMed:12045210}. +Q9Z2C5 MTM1_MOUSE Myotubularin (Phosphatidylinositol-3,5-bisphosphate 3-phosphatase) (EC 3.1.3.95) (Phosphatidylinositol-3-phosphate phosphatase) (EC 3.1.3.64) 603 69,559 Active site (1); Chain (1); Domain (2); Modified residue (4); Sequence conflict (1) FUNCTION: Lipid phosphatase which dephosphorylates phosphatidylinositol 3-monophosphate (PI3P) and phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2). Has also been shown to dephosphorylate phosphotyrosine- and phosphoserine-containing peptides. Negatively regulates EGFR degradation through regulation of EGFR trafficking from the late endosome to the lysosome. Plays a role in vacuolar formation and morphology (By similarity). Regulates desmin intermediate filament assembly and architecture. Plays a role in mitochondrial morphology and positioning (PubMed:21135508). Required for skeletal muscle maintenance but not for myogenesis (PubMed:12391329). In skeletal muscles, stabilizes MTMR12 protein levels (PubMed:23818870). {ECO:0000250|UniProtKB:Q13496, ECO:0000269|PubMed:12391329, ECO:0000269|PubMed:21135508, ECO:0000269|PubMed:23818870}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12118066}. Cell membrane {ECO:0000250|UniProtKB:Q13496}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q13496}. Cell projection, filopodium {ECO:0000269|PubMed:12118066}. Cell projection, ruffle {ECO:0000269|PubMed:12118066}. Late endosome {ECO:0000250|UniProtKB:Q13496}. Cytoplasm, myofibril, sarcomere {ECO:0000269|PubMed:23818870}. Note=Localizes as a dense cytoplasmic network. Also localizes to the plasma membrane, including plasma membrane extensions such as filopodia and ruffles. Predominantly located in the cytoplasm following interaction with MTMR12. Recruited to the late endosome following EGF stimulation (By similarity). In skeletal muscles, co-localizes with MTMR12 in the sarcomere (PubMed:23818870). {ECO:0000250|UniProtKB:Q13496, ECO:0000269|PubMed:23818870}. SUBUNIT: Forms a complex composed of MTMR12 and lipid phosphatase MTM1; in skeletal muscles, the interaction stabilizes both MTMR12 and MTM1 protein levels; the interaction may modulate MTM1 intracellular location (PubMed:23818870). Interacts with KMT2A/MLL1 (via SET domain) (By similarity). Interacts with DES in skeletal muscle but not in cardiac muscle (PubMed:21135508). Interacts with SPEG (By similarity). {ECO:0000250|UniProtKB:Q13496, ECO:0000269|PubMed:21135508, ECO:0000269|PubMed:23818870}. DOMAIN: The GRAM domain mediates binding to PI(3,5)P2 and, with lower affinity, to other phosphoinositides. {ECO:0000250|UniProtKB:Q13496}. TISSUE SPECIFICITY: Widely expressed with highest levels detected in heart and muscle and low levels in brain (at protein level) (PubMed:12118066). Expressed in skeletal muscles (at protein level) (PubMed:23818870). {ECO:0000269|PubMed:12118066, ECO:0000269|PubMed:23818870}. +O54972 MTG16_MOUSE Protein CBFA2T3 (Eight twenty one protein 2) (MTG8-related protein 2) (Protein ETO-2) 620 68,032 Alternative sequence (2); Chain (1); Coiled coil (1); Compositional bias (1); Domain (1); Frameshift (1); Modified residue (2); Region (6); Sequence conflict (2); Zinc finger (1) FUNCTION: Transcriptional corepressor which facilitates transcriptional repression via its association with DNA-binding transcription factors and recruitment of other corepressors and histone-modifying enzymes. Can repress the expression of MMP7 in a ZBTB33-dependent manner. Reduces the protein levels and stability of the transcriptinal regulator HIF1A; interacts with EGLN1 and promotes the HIF1A prolyl hydroxylation-dependent ubiquitination and proteasomal degradation pathway. Contributes to inhibition of glycolysis and stimulation of mitochondrial respiration by down-regulating the expression of glycolytic genes including PFKFB3, PFKFB4, PDK1, PFKP, LDHA and HK1 which are direct targets of HIF1A (By similarity). Regulates the proliferation and the differentiation of erythroid progenitors by repressing the expression of TAL1 target genes (PubMed:16407974). Plays a role in granulocyte differentiation (PubMed:15231665). {ECO:0000250|UniProtKB:O75081, ECO:0000269|PubMed:11533236, ECO:0000269|PubMed:15231665, ECO:0000269|PubMed:16407974}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:10022820}. Nucleus, nucleoplasm {ECO:0000269|PubMed:10022820}. Golgi apparatus membrane {ECO:0000250}. SUBUNIT: Heterodimer with RUNX1T1 and CBFA2T2. Interacts with ZNF652 and ERBB4. May interact with PRKAR2A, PDE7A and probably PDE4A. Interacts with PLXNA1, PLXNA3 and PRKAR1A (By similarity). Interacts with HDAC1, HDAC2, HDAC3, HDAC6, HDAC8, NCOR1 and NCOR2. Component of a TAL-1 complex composed at least of CBFA2T3, LDB1, TAL1 and TCF3. Interacts with ZBTB4, ZBTB38 and ZBTB33. Interacts with HIF1A and EGLN1 (By similarity). {ECO:0000250|UniProtKB:O75081, ECO:0000269|PubMed:11533236, ECO:0000269|PubMed:15231665, ECO:0000269|PubMed:16407974}. DOMAIN: Nervy homology region 2 (NHR2) mediates homo- and possibly heterotypic oligomerization by forming a four-helix bundle tetrameric structure. {ECO:0000250|UniProtKB:Q06455}. TISSUE SPECIFICITY: Widely expressed with higher expression in heart, brain, lung and spleen. Expressed in hematopoietic cells (at protein level). {ECO:0000269|PubMed:10022820, ECO:0000269|PubMed:15231665}. +Q9D2V8 MFS10_MOUSE Major facilitator superfamily domain-containing protein 10 (Tetracycline transporter-like protein) 456 49,369 Chain (1); Erroneous initiation (1); Glycosylation (1); Sequence conflict (3); Transmembrane (11) TRANSMEM 25 45 Helical. {ECO:0000255}.; TRANSMEM 87 107 Helical. {ECO:0000255}.; TRANSMEM 114 136 Helical. {ECO:0000255}.; TRANSMEM 179 199 Helical. {ECO:0000255}.; TRANSMEM 203 223 Helical. {ECO:0000255}.; TRANSMEM 278 298 Helical. {ECO:0000255}.; TRANSMEM 311 328 Helical. {ECO:0000255}.; TRANSMEM 345 365 Helical. {ECO:0000255}.; TRANSMEM 366 386 Helical. {ECO:0000255}.; TRANSMEM 403 423 Helical. {ECO:0000255}.; TRANSMEM 424 444 Helical. {ECO:0000255}. FUNCTION: Confers cellular resistance to apoptosis induced by the non-steroidal anti-inflammatory drugs indomethacin and diclofenac. May act as an efflux pump (By similarity). {ECO:0000250|UniProtKB:Q14728}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. +O08789 MNT_MOUSE Max-binding protein MNT (Myc antagonist MNT) (Protein ROX) 591 63,274 Chain (1); Domain (1); Initiator methionine (1); Modified residue (1); Region (1); Sequence conflict (8) FUNCTION: Binds DNA as a heterodimer with MAX and represses transcription. Binds to the canonical E box sequence 5'-CACGTG-3' and, with higher affinity, to 5'-CACGCG-3'. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Efficient DNA binding requires dimerization with another bHLH protein. Binds DNA as a homodimer or a heterodimer with MAX. +Q6XJV6 MO2R2_MOUSE Cell surface glycoprotein CD200 receptor 2 (CD200 cell surface glycoprotein receptor-like 2) (CD200 receptor-like 2) (CD200 cell surface glycoprotein receptor-like c) (CD200RLc) (Cell surface glycoprotein OX2 receptor 2) 249 27,408 Chain (1); Disulfide bond (2); Domain (2); Glycosylation (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 221 241 Helical. {ECO:0000255}. TOPO_DOM 25 220 Extracellular. {ECO:0000255}.; TOPO_DOM 242 249 Cytoplasmic. {ECO:0000255}. FUNCTION: According to PubMed:15187158 it is a receptor for the CD200 cell surface glycoprotein. According to PubMed:16081818 it is not a receptor for the CD200/OX2 cell surface glycoprotein. Involved in the recruitment or surface expression of the TYROBP receptor. {ECO:0000269|PubMed:15187158, ECO:0000269|PubMed:15471863, ECO:0000269|PubMed:16081818}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in bone marrow, spleen, brain, lung, testis and thymus. {ECO:0000269|PubMed:15187158, ECO:0000269|PubMed:15274657}. +Q8VE04 MOB3B_MOUSE MOB kinase activator 3B (Mob1 homolog 2b) (Mps one binder kinase activator-like 2B) 216 25,519 Chain (1); Metal binding (4) FUNCTION: Modulates LATS1 expression in the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. {ECO:0000250|UniProtKB:Q86TA1}. +P97346 NXN_MOUSE Nucleoredoxin (EC 1.8.1.8) (Protein Red-1) 435 48,344 Alternative sequence (2); Chain (1); Domain (1); Initiator methionine (1); Modified residue (1); Mutagenesis (2) FUNCTION: Functions as a redox-dependent negative regulator of the Wnt signaling pathway, possibly by preventing ubiquitination of DVL3 by the BCR(KLHL12) complex. May also function as a transcriptional regulator act as a regulator of protein phosphatase 2A (PP2A). {ECO:0000269|PubMed:10903915, ECO:0000269|PubMed:16604061, ECO:0000269|PubMed:16764867, ECO:0000269|PubMed:20970343}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:16604061}. Nucleus {ECO:0000269|PubMed:10903915, ECO:0000269|PubMed:9119370}. SUBUNIT: Associates with the phosphatase 2A holoenzyme. Interacts with PPP2CA; the interaction is direct. Interacts with DVL1 (via PDZ domain); the interaction is direct and regulated by oxidative stress. {ECO:0000269|PubMed:16604061, ECO:0000269|PubMed:16764867}. TISSUE SPECIFICITY: Widely expressed with higher expression in testis and skin. {ECO:0000269|PubMed:9119370}. +Q8C784 MOSMO_MOUSE Modulator of smoothened protein (Attenuator of hedgehog) 167 18,250 Alternative sequence (1); Chain (1); Erroneous initiation (1); Glycosylation (1); Transmembrane (4) TRANSMEM 7 29 Helical. {ECO:0000255}.; TRANSMEM 68 88 Helical. {ECO:0000255}.; TRANSMEM 101 121 Helical. {ECO:0000255}.; TRANSMEM 139 159 Helical. {ECO:0000255}. FUNCTION: Acts as a negative regulator of hedgehog signaling probably by promoting internalization and subsequent degradation of smoothened protein (SMO) present in the ciliary membrane (PubMed:29290584). Plays a role in sonic hedgehog (SHH)-induced spinal neural progenitor cells differentiation (PubMed:29290584). {ECO:0000269|PubMed:29290584}. SUBCELLULAR LOCATION: Cell projection, cilium membrane {ECO:0000269|PubMed:29290584}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:29290584}; Multi-pass membrane protein {ECO:0000255}. +Q8BMQ8 MON1B_MOUSE Vacuolar fusion protein MON1 homolog B 553 60,016 Chain (1); Modified residue (2) SUBUNIT: Interacts with CCNT2; downregulates CCNT2-mediated activation of viral promoters during herpes simplex virus 1/HHV-1 infection. Found in a complex with RMC1, CCZ1 MON1A and MON1B. {ECO:0000250|UniProtKB:Q7L1V2}. +Q3UNA4 NXT2_MOUSE NTF2-related export protein 2 142 16,257 Alternative sequence (2); Chain (1); Domain (1); Sequence conflict (1) FUNCTION: Regulator of protein export for NES-containing proteins. Also plays a role in mRNA nuclear export (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Shuttles between the nucleus and the cytoplasm. {ECO:0000250}. SUBUNIT: Associates with NXF1, NXF2, NXF3 and NXF5. {ECO:0000250}. +Q8VFK2 O1002_MOUSE Olfactory receptor 1002 (Olfactory receptor 175-2) 318 35,833 Chain (1); Disulfide bond (1); Glycosylation (1); Sequence conflict (1); Topological domain (8); Transmembrane (7) TRANSMEM 26 46 Helical; Name=1. {ECO:0000255}.; TRANSMEM 55 75 Helical; Name=2. {ECO:0000255}.; TRANSMEM 100 120 Helical; Name=3. {ECO:0000255}.; TRANSMEM 134 154 Helical; Name=4. {ECO:0000255}.; TRANSMEM 197 217 Helical; Name=5. {ECO:0000255}.; TRANSMEM 238 258 Helical; Name=6. {ECO:0000255}.; TRANSMEM 272 292 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 25 Extracellular. {ECO:0000255}.; TOPO_DOM 47 54 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 76 99 Extracellular. {ECO:0000255}.; TOPO_DOM 121 133 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 155 196 Extracellular. {ECO:0000255}.; TOPO_DOM 218 237 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 259 271 Extracellular. {ECO:0000255}.; TOPO_DOM 293 318 Cytoplasmic. {ECO:0000255}. FUNCTION: Potential odorant receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q8VFK7 O1020_MOUSE Olfactory receptor 1020 (Olfactory receptor 201-2) 317 35,284 Chain (1); Disulfide bond (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 33 53 Helical; Name=1. {ECO:0000255}.; TRANSMEM 62 82 Helical; Name=2. {ECO:0000255}.; TRANSMEM 107 127 Helical; Name=3. {ECO:0000255}.; TRANSMEM 141 161 Helical; Name=4. {ECO:0000255}.; TRANSMEM 204 224 Helical; Name=5. {ECO:0000255}.; TRANSMEM 245 265 Helical; Name=6. {ECO:0000255}.; TRANSMEM 279 299 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 32 Extracellular. {ECO:0000255}.; TOPO_DOM 54 61 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 83 106 Extracellular. {ECO:0000255}.; TOPO_DOM 128 140 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 162 203 Extracellular. {ECO:0000255}.; TOPO_DOM 225 244 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 266 278 Extracellular. {ECO:0000255}.; TOPO_DOM 300 317 Cytoplasmic. {ECO:0000255}. FUNCTION: Potential odorant receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q8VGS1 O1038_MOUSE Olfactory receptor 1038 (Olfactory receptor 185-3) 319 36,135 Chain (1); Disulfide bond (1); Glycosylation (2); Topological domain (8); Transmembrane (7) TRANSMEM 26 46 Helical; Name=1. {ECO:0000255}.; TRANSMEM 55 75 Helical; Name=2. {ECO:0000255}.; TRANSMEM 100 120 Helical; Name=3. {ECO:0000255}.; TRANSMEM 134 154 Helical; Name=4. {ECO:0000255}.; TRANSMEM 197 217 Helical; Name=5. {ECO:0000255}.; TRANSMEM 238 258 Helical; Name=6. {ECO:0000255}.; TRANSMEM 272 292 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 25 Extracellular. {ECO:0000255}.; TOPO_DOM 47 54 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 76 99 Extracellular. {ECO:0000255}.; TOPO_DOM 121 133 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 155 196 Extracellular. {ECO:0000255}.; TOPO_DOM 218 237 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 259 271 Extracellular. {ECO:0000255}.; TOPO_DOM 293 319 Cytoplasmic. {ECO:0000255}. FUNCTION: Potential odorant receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q8VGR9 O1044_MOUSE Olfactory receptor 1044 (Olfactory receptor 185-4) 314 35,612 Chain (1); Disulfide bond (1); Glycosylation (2); Topological domain (8); Transmembrane (7) TRANSMEM 26 46 Helical; Name=1. {ECO:0000255}.; TRANSMEM 55 75 Helical; Name=2. {ECO:0000255}.; TRANSMEM 100 120 Helical; Name=3. {ECO:0000255}.; TRANSMEM 134 154 Helical; Name=4. {ECO:0000255}.; TRANSMEM 197 217 Helical; Name=5. {ECO:0000255}.; TRANSMEM 238 258 Helical; Name=6. {ECO:0000255}.; TRANSMEM 272 292 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 25 Extracellular. {ECO:0000255}.; TOPO_DOM 47 54 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 76 99 Extracellular. {ECO:0000255}.; TOPO_DOM 121 133 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 155 196 Extracellular. {ECO:0000255}.; TOPO_DOM 218 237 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 259 271 Extracellular. {ECO:0000255}.; TOPO_DOM 293 314 Cytoplasmic. {ECO:0000255}. FUNCTION: Potential odorant receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q8VGR8 O1052_MOUSE Olfactory receptor 1052 (Olfactory receptor 172-1) 312 34,586 Chain (1); Disulfide bond (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 26 46 Helical; Name=1. {ECO:0000255}.; TRANSMEM 55 75 Helical; Name=2. {ECO:0000255}.; TRANSMEM 100 120 Helical; Name=3. {ECO:0000255}.; TRANSMEM 134 154 Helical; Name=4. {ECO:0000255}.; TRANSMEM 197 217 Helical; Name=5. {ECO:0000255}.; TRANSMEM 238 258 Helical; Name=6. {ECO:0000255}.; TRANSMEM 272 292 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 25 Extracellular. {ECO:0000255}.; TOPO_DOM 47 54 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 76 99 Extracellular. {ECO:0000255}.; TOPO_DOM 121 133 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 155 196 Extracellular. {ECO:0000255}.; TOPO_DOM 218 237 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 259 271 Extracellular. {ECO:0000255}.; TOPO_DOM 293 312 Cytoplasmic. {ECO:0000255}. FUNCTION: Potential odorant receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q9D1Q1 MPH6_MOUSE M-phase phosphoprotein 6 161 19,086 Chain (1); Compositional bias (1); Cross-link (5); Modified residue (1); Motif (1) FUNCTION: RNA-binding protein that associates with the RNA exosome complex. Involved in the 3'-processing of the 7S pre-RNA to the mature 5.8S rRNA and plays a role in recruiting the RNA exosome complex to pre-rRNA; this function may include C1D. {ECO:0000250|UniProtKB:Q99547}. PTM: Phosphorylated in M (mitotic) phase. {ECO:0000250|UniProtKB:Q99547}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q99547}. Cytoplasm {ECO:0000250|UniProtKB:Q99547}. Note=Cytoplasmic in M phase. {ECO:0000250|UniProtKB:Q99547}. SUBUNIT: Associates with the RNA exosome complex, probably mediated by EXOSC10. Interacts with ARHGAP18, EXOSC10 and MTREX. {ECO:0000250|UniProtKB:Q99547}. +Q924M7 MPI_MOUSE Mannose-6-phosphate isomerase (EC 5.3.1.8) (Phosphohexomutase) (Phosphomannose isomerase) (PMI) 423 46,575 Active site (1); Chain (1); Initiator methionine (1); Metal binding (4); Modified residue (3) Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 1/2. FUNCTION: Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12122025}. +Q8R0M8 MOT5_MOUSE Monocarboxylate transporter 5 (MCT 5) 500 55,678 Alternative sequence (2); Chain (1); Sequence conflict (1); Topological domain (13); Transmembrane (12) TRANSMEM 17 37 Helical. {ECO:0000255}.; TRANSMEM 59 79 Helical. {ECO:0000255}.; TRANSMEM 88 108 Helical. {ECO:0000255}.; TRANSMEM 110 129 Helical. {ECO:0000255}.; TRANSMEM 154 174 Helical. {ECO:0000255}.; TRANSMEM 176 195 Helical. {ECO:0000255}.; TRANSMEM 305 325 Helical. {ECO:0000255}.; TRANSMEM 343 363 Helical. {ECO:0000255}.; TRANSMEM 375 395 Helical. {ECO:0000255}.; TRANSMEM 397 416 Helical. {ECO:0000255}.; TRANSMEM 431 451 Helical. {ECO:0000255}.; TRANSMEM 464 484 Helical. {ECO:0000255}. TOPO_DOM 1 16 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 38 58 Extracellular. {ECO:0000255}.; TOPO_DOM 80 87 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 109 109 Extracellular. {ECO:0000255}.; TOPO_DOM 130 153 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 175 175 Extracellular. {ECO:0000255}.; TOPO_DOM 196 304 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 326 342 Extracellular. {ECO:0000255}.; TOPO_DOM 364 374 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 396 396 Extracellular. {ECO:0000255}.; TOPO_DOM 417 430 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 452 463 Extracellular. {ECO:0000255}.; TOPO_DOM 485 500 Cytoplasmic. {ECO:0000255}. FUNCTION: Proton-linked monocarboxylate transporter. Catalyzes the rapid transport across the plasma membrane of many monocarboxylates such as lactate, pyruvate, branched-chain oxo acids derived from leucine, valine and isoleucine, and the ketone bodies acetoacetate, beta-hydroxybutyrate and acetate (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +P70236 MP2K6_MOUSE Dual specificity mitogen-activated protein kinase kinase 6 (MAP kinase kinase 6) (MAPKK 6) (EC 2.7.12.2) (MAPK/ERK kinase 6) (MEK 6) (SAPKK3) 334 37,432 Active site (1); Binding site (1); Chain (1); Domain (1); Modified residue (2); Nucleotide binding (1); Region (2) FUNCTION: Dual specificity protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. With MAP3K3/MKK3, catalyzes the concomitant phosphorylation of a threonine and a tyrosine residue in the MAP kinases p38 MAPK11, MAPK12, MAPK13 and MAPK14 and plays an important role in the regulation of cellular responses to cytokines and all kinds of stresses. Especially, MAP2K3/MKK3 and MAP2K6/MKK6 are both essential for the activation of MAPK11 and MAPK13 induced by environmental stress, whereas MAP2K6/MKK6 is the major MAPK11 activator in response to TNF. MAP2K6/MKK6 also phosphorylates and activates PAK6. The p38 MAP kinase signal transduction pathway leads to direct activation of transcription factors. Nuclear targets of p38 MAP kinase include the transcription factors ATF2 and ELK1. Within the p38 MAPK signal transduction pathway, MAP3K6/MKK6 mediates phosphorylation of STAT4 through MAPK14 activation, and is therefore required for STAT4 activation and STAT4-regulated gene expression in response to IL-12 stimulation. The pathway is also crucial for IL-6-induced SOCS3 expression and down-regulation of IL-6-mediated gene induction; and for IFNG-dependent gene transcription. Has a role in osteoclast differentiation through NF-kappa-B transactivation by TNFSF11, and in endochondral ossification and since SOX9 is another likely downstream target of the p38 MAPK pathway. MAP2K6/MKK6 mediates apoptotic cell death in thymocytes. Acts also as a regulator for melanocytes dendricity, through the modulation of Rho family GTPases. {ECO:0000269|PubMed:12151339, ECO:0000269|PubMed:12824301, ECO:0000269|PubMed:12893778, ECO:0000269|PubMed:15644321, ECO:0000269|PubMed:16387856, ECO:0000269|PubMed:16498455, ECO:0000269|PubMed:20004242}. PTM: Weakly autophosphorylated. Phosphorylated at Ser-207 and Thr-211 by the majority of M3Ks, such as MAP3K5/ASK1, MAP3K1/MEKK1, MAP3K2/MEKK2, MAP3K3/MEKK3, MAP3K4/MEKK4, MAP3K7/TAK1, MAP3K11/MLK3 and MAP3K17/TAOK2. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Binds to microtubules. {ECO:0000250}. SUBUNIT: Dimer. Interacts (via its D domain) with its substrates MAPK11, MAPK12, MAPK13 and MAPK14. Interacts (via its DVD domain) with MAP3Ks activators like MAP3K5/ASK1, MAP3K1/MEKK1, MAP3K2/MEKK2, MAP3K3/MEKK3, MAP3K4/MEKK4, MAP3K7/TAK1, MAP3K11/MLK3 and MAP3K17/TAOK2. Interacts with DCTN1. Interacts with EIF2AK2/PKR. {ECO:0000250}. DOMAIN: The DVD domain (residues 311-334) contains a conserved docking site and is found in the mammalian MAP kinase kinases (MAP2Ks). The DVD sites bind to their specific upstream MAP kinase kinase kinases (MAP3Ks) and are essential for activation (By similarity). {ECO:0000250}.; DOMAIN: The D domain (residues 4-19) contains a conserved docking site and is required for the binding to MAPK substrates. {ECO:0000250}. +Q8CE90 MP2K7_MOUSE Dual specificity mitogen-activated protein kinase kinase 7 (MAP kinase kinase 7) (MAPKK 7) (EC 2.7.12.2) (JNK-activating kinase 2) (MAPK/ERK kinase 7) (MEK 7) (c-Jun N-terminal kinase kinase 2) (JNK kinase 2) (JNKK 2) 535 59,312 Active site (1); Alternative sequence (8); Binding site (1); Chain (1); Coiled coil (1); Domain (1); Initiator methionine (1); Modified residue (4); Nucleotide binding (1); Region (2); Sequence conflict (8); Site (2) FUNCTION: Dual specificity protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. Essential component of the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. With MAP2K4/MKK4, is the one of the only known kinase to directly activate the stress-activated protein kinase/c-Jun N-terminal kinases MAPK8/JNK1, MAPK9/JNK2 and MAPK10/JNK3. MAP2K4/MKK4 and MAP2K7/MKK7 both activate the JNKs by phosphorylation, but they differ in their preference for the phosphorylation site in the Thr-Pro-Tyr motif. MAP2K4/MKK4 shows preference for phosphorylation of the Tyr residue and MAP2K7/MKK7 for the Thr residue. The monophosphorylation of JNKs on the Thr residue is sufficient to increase JNK activity indicating that MAP2K7/MKK7 is important to trigger JNK activity, while the additional phosphorylation of the Tyr residue by MAP2K4/MKK4 ensures optimal JNK activation. Has a specific role in JNK signal transduction pathway activated by proinflammatory cytokines. The MKK/JNK signaling pathway is also involved in mitochondrial death signaling pathway, including the release cytochrome c, leading to apoptosis. Part of a non-canonical MAPK signaling pathway, composed of the upstream MAP3K12 kinase and downstream MAP kinases MAPK1/ERK2 and MAPK3/ERK1, that enhances the AP-1-mediated transcription of APP in response to APOE (PubMed:28111074). {ECO:0000269|PubMed:11390361, ECO:0000269|PubMed:12624093, ECO:0000269|PubMed:28111074, ECO:0000269|PubMed:9312105, ECO:0000269|PubMed:9384583, ECO:0000269|PubMed:9405446, ECO:0000269|PubMed:9535930, ECO:0000269|PubMed:9891090}. PTM: Activated by phosphorylation on Ser-287 and Thr-291 by MAP kinase kinase kinases (MAP3Ks). {ECO:0000269|PubMed:9891090}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9891090}. Cytoplasm {ECO:0000269|PubMed:9891090}. SUBUNIT: Interacts with RASSF7, the interaction promotes phosphorylation. Interacts with VRK2 (By similarity). Interacts (via its D domain) with its substrates MAPK8/JNK1, MAPK9/JNK2 and MAPK10/JNK3 (By similarity). Interacts (via its DVD domain) with MAP3Ks activators like MAP3K5/ASK1 and MAP3K1/MEKK1 (By similarity). Interacts with SH3RF1, MAPK8IP1/JIP1, MAPK8IP2/JIP2 and MAPK8IP3/JIP3 scaffold proteins. Found in a complex with SH3RF1, RAC1, MAP3K11/MLK3, MAPK8IP1/JIP1 and MAPK8/JNK1 (PubMed:23963642). Found in a complex with SH3RF1, RAC2, MAP3K7/TAK1, MAPK8IP1/JIP1, MAPK8/JNK1 and MAPK9/JNK2 (PubMed:27084103). {ECO:0000250|UniProtKB:O14733, ECO:0000269|PubMed:10629060, ECO:0000269|PubMed:23963642, ECO:0000269|PubMed:27084103, ECO:0000269|PubMed:9733513}. DOMAIN: The DVD domain (residues 393-413) contains a conserved docking site and is found in the mammalian MAP kinase kinases (MAP2Ks). The DVD sites bind to their specific upstream MAP kinase kinase kinases (MAP3Ks) and are essential for activation.; DOMAIN: The D domain (residues 37-73) contains a conserved docking site and is required for the binding to MAPK substrates. TISSUE SPECIFICITY: Expressed at high levels in brain, lung, liver, skeletal muscle, kidney, and testis and at lower levels in the heart and spleen. {ECO:0000269|PubMed:9312105, ECO:0000269|PubMed:9405446, ECO:0000269|PubMed:9535930}. +Q8VFX2 O1444_MOUSE Olfactory receptor 1444 (Olfactory receptor 202-4) 319 35,485 Chain (1); Disulfide bond (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 27 47 Helical; Name=1. {ECO:0000255}.; TRANSMEM 56 76 Helical; Name=2. {ECO:0000255}.; TRANSMEM 101 121 Helical; Name=3. {ECO:0000255}.; TRANSMEM 135 155 Helical; Name=4. {ECO:0000255}.; TRANSMEM 198 218 Helical; Name=5. {ECO:0000255}.; TRANSMEM 239 259 Helical; Name=6. {ECO:0000255}.; TRANSMEM 273 293 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 26 Extracellular. {ECO:0000255}.; TOPO_DOM 48 55 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 77 100 Extracellular. {ECO:0000255}.; TOPO_DOM 122 134 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 156 197 Extracellular. {ECO:0000255}.; TOPO_DOM 219 238 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 260 272 Extracellular. {ECO:0000255}.; TOPO_DOM 294 319 Cytoplasmic. {ECO:0000255}. FUNCTION: Potential odorant receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q810V0 MPP10_MOUSE U3 small nucleolar ribonucleoprotein protein MPP10 (M phase phosphoprotein 10) 681 78,735 Chain (1); Coiled coil (4); Compositional bias (2); Cross-link (6); Modified residue (11); Sequence conflict (4) FUNCTION: Component of the 60-80S U3 small nucleolar ribonucleoprotein (U3 snoRNP). Required for the early cleavages during pre-18S ribosomal RNA processing (By similarity). {ECO:0000250}. PTM: Phosphorylated in M (mitotic) phase. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:O00566}. Chromosome {ECO:0000250|UniProtKB:O00566}. Note=Fibrillar region of the nucleolus. After dissolution of the nucleolus in early M phase becomes associated with chromosomes through metaphase and anaphase. In telophase localized to small cellular prenucleolar bodies that not always contain fibrillarin. The reassociation with nucleolus is preceeded by the arrival of fibrillarin. {ECO:0000250|UniProtKB:O00566}. SUBUNIT: Component of a heterotrimeric complex containing IMP3, IMP4 and MPHOSPH10. Interacts with IMP3 and IMP4 (By similarity). {ECO:0000250}. +Q9R0Q9 MPU1_MOUSE Mannose-P-dolichol utilization defect 1 protein (Suppressor of Lec15 and Lec35 glycosylation mutation homolog) (SL15) 247 26,498 Chain (1); Domain (2); Initiator methionine (1); Modified residue (1); Sequence conflict (2); Transmembrane (7) TRANSMEM 37 57 Helical. {ECO:0000255}.; TRANSMEM 74 94 Helical. {ECO:0000255}.; TRANSMEM 100 120 Helical. {ECO:0000255}.; TRANSMEM 128 145 Helical. {ECO:0000255}.; TRANSMEM 151 171 Helical. {ECO:0000255}.; TRANSMEM 185 205 Helical. {ECO:0000255}.; TRANSMEM 213 233 Helical. {ECO:0000255}. FUNCTION: Required for normal utilization of mannose-dolichol phosphate (Dol-P-Man) in the synthesis of N-linked and O-linked oligosaccharides and GPI anchors. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +P19258 MPV17_MOUSE Protein Mpv17 (Mpv-17) 176 19,686 Chain (1); Transmembrane (4) TRANSMEM 18 38 Helical. {ECO:0000255}.; TRANSMEM 53 73 Helical. {ECO:0000255}.; TRANSMEM 94 114 Helical. {ECO:0000255}.; TRANSMEM 131 151 Helical. {ECO:0000255}. FUNCTION: Involved in mitochondria homeostasis. May be involved in the metabolism of reactive oxygen species and control of oxidative phosphorylation and mitochondrial DNA (mtDNA) maintenance (Probable). {ECO:0000305|PubMed:7957077}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: High levels in heart, kidney, and brain, intermediate levels in testis, and low levels in liver and spleen. +O70255 MPZL2_MOUSE Myelin protein zero-like protein 2 (Epithelial V-like antigen 1) 215 24,162 Chain (1); Disulfide bond (1); Domain (1); Glycosylation (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 155 175 Helical. {ECO:0000255}. TOPO_DOM 27 154 Extracellular. {ECO:0000255}.; TOPO_DOM 176 215 Cytoplasmic. {ECO:0000255}. FUNCTION: Mediates homophilic cell-cell adhesion. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in liver and gut, skin, and testis but not in thymocytes, lymphocytes, macrophage or dendritic cells or cell lines. +Q91ZG2 MPPD1_MOUSE Metallophosphoesterase domain-containing protein 1 (EC 3.1.-.-) 326 37,214 Chain (1); Sequence conflict (1) FUNCTION: May have metallophosphoesterase activity (in vitro). {ECO:0000250}. +P35487 ODPAT_MOUSE Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial (EC 1.2.4.1) (PDHE1-A type II) 391 43,413 Chain (1); Modified residue (2); Transit peptide (1) FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. SUBUNIT: Heterotetramer of two PDHA2 and two PDHB subunits. The heterotetramer interacts with DLAT, and is part of the multimeric pyruvate dehydrogenase complex that contains multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3). These subunits are bound to an inner core composed of about 48 DLAT and 12 PDHX molecules (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Testis. +P35486 ODPA_MOUSE Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial (EC 1.2.4.1) (PDHE1-A type I) 390 43,232 Chain (1); Modified residue (16); Mutagenesis (1); Transit peptide (1) FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle. {ECO:0000269|PubMed:11708858, ECO:0000269|PubMed:20841503}. PTM: Phosphorylation at Ser-232, Ser-293 and Ser-300 by PDK family kinases inactivates the enzyme; for this phosphorylation at a single site is sufficient. Phosphorylation at Ser-293 interferes with access to active site, and thereby inactivates the enzyme. Dephosphorylation at all three sites, i.e. at Ser-232, Ser-293 and Ser-300, is required for reactivation (By similarity). {ECO:0000250}.; PTM: Acetylation alters the phosphorylation pattern. Deacetylated by SIRT3. {ECO:0000269|PubMed:19341700, ECO:0000269|PubMed:23835326}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:19341700}. SUBUNIT: Heterotetramer of two PDHA1 and two PDHB subunits. The heterotetramer interacts with DLAT, and is part of the multimeric pyruvate dehydrogenase complex that contains multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3). These subunits are bound to an inner core composed of about 48 DLAT and 12 PDHX molecules (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: In all tissues, but in very low amount in testis. +Q8BKZ9 ODPX_MOUSE Pyruvate dehydrogenase protein X component, mitochondrial (Dihydrolipoamide dehydrogenase-binding protein of pyruvate dehydrogenase complex) (Lipoyl-containing pyruvate dehydrogenase complex component X) 501 53,999 Chain (1); Compositional bias (1); Domain (2); Modified residue (4); Transit peptide (1) FUNCTION: Required for anchoring dihydrolipoamide dehydrogenase (E3) to the dihydrolipoamide transacetylase (E2) core of the pyruvate dehydrogenase complexes of eukaryotes. This specific binding is essential for a functional PDH complex (By similarity). {ECO:0000250}. PTM: Delipoylated at Lys-97 by SIRT4, delipoylation decreases the PHD complex activity. {ECO:0000250|UniProtKB:O00330}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. SUBUNIT: Part of the inner core of the multimeric pyruvate dehydrogenase complex that is composed of about 48 DLAT and 12 PDHX molecules. This core binds multiple copies of pyruvate dehydrogenase (subunits PDH1A and PDHB, E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3). Interacts with SIRT4. Interacts with DLD. {ECO:0000250|UniProtKB:O00330}. +Q923Z3 MTO1_MOUSE Protein MTO1 homolog, mitochondrial 669 74,332 Chain (1); Modified residue (1); Nucleotide binding (1); Sequence conflict (1); Transit peptide (1) FUNCTION: Involved in the 5-carboxymethylaminomethyl modification (mnm(5)s(2)U34) of the wobble uridine base in mitochondrial tRNAs. {ECO:0000269|PubMed:14522080}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14522080}. TISSUE SPECIFICITY: Ubiquitously expressed in various tissues, but with markedly elevated expression in tissues of high metabolic rates. {ECO:0000269|PubMed:14522080}. +Q9WTK0 NUPR1_MOUSE Nuclear protein 1 (Nuclear transcriptional regulator protein 1) (Protein p8) 80 8,901 Chain (1); Motif (1); Sequence conflict (1) FUNCTION: Chromatin-binding protein that converts stress signals into a program of gene expression that empowers cells with resistance to the stress induced by a change in their microenvironment. Interacts with MSL1 and inhibits its activity on histone H4 'Lys-16' acetylation (H4K16ac) (By similarity). Binds the RELB promoter and activates its transcription, leading to the transactivation of IER3 (By similarity). NUPR1 overexpression leads to the activation of PI3K/AKT signaling pathway, CDKN1A/p21 phosphorylation and relocalization from the nucleus to the cytoplasm, leading to resistance to toxic agents, such as doxorubicin (By similarity). As a member of the NUPR1/RELB/IER3 survival pathway, may allow the development of pancreatic intraepithelial neoplasias. {ECO:0000250, ECO:0000269|PubMed:22565310}. PTM: Phosphorylated. Phosphorylation promotes DNA-binding activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Monomer. Directly interacts with MSL1 and binds MORF4L1, two components of histone acetyltransferase complex; the interaction with MORF4L1 may be mediated by MSL1. {ECO:0000250}. DOMAIN: May exhibit the features of HMG-I(Y) proteins. {ECO:0000250}. +Q8BMD7 MORC4_MOUSE MORC family CW-type zinc finger protein 4 (Zinc finger CW-type coiled-coil domain protein 2) 928 105,740 Alternative sequence (2); Chain (1); Coiled coil (1); Erroneous initiation (1); Erroneous termination (1); Sequence caution (1); Sequence conflict (8); Zinc finger (1) SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +Q69ZX6 MOR2A_MOUSE MORC family CW-type zinc finger protein 2A (Zinc finger CW-type coiled-coil domain protein 1) 1030 117,330 Chain (1); Coiled coil (4); Compositional bias (1); Erroneous initiation (1); Modified residue (6); Zinc finger (1) TISSUE SPECIFICITY: Expressed in the axons and Schwann cells of peripheral nerves. {ECO:0000269|PubMed:26497905}. +Q3V3F6 MPZL3_MOUSE Myelin protein zero-like protein 3 237 26,058 Alternative sequence (2); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (1); Natural variant (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 160 180 Helical. {ECO:0000255}. TOPO_DOM 33 159 Extracellular. {ECO:0000255}.; TOPO_DOM 181 237 Cytoplasmic. {ECO:0000255}. FUNCTION: Mediates homophilic cell-cell adhesion. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Present in all tissues tested, including the skin. Present in the keratinocytes and sebocytes in the skin (at protein level). {ECO:0000269|PubMed:17273165}. DISEASE: Note=Defects in Mpzl3 are the cause of rough coat (rc) phenotype, an autosomal-recessive mutation, arose spontaneously in C57BL/6J mice. Rc mice develop severe skin and hair abnormalities, including cyclic and progressive hair loss and sebaceous gland hypertrophy. +Q8QZR4 OAF_MOUSE Out at first protein homolog 282 31,524 Chain (1); Sequence conflict (1); Signal peptide (1) +Q91WW5 MRGA1_MOUSE Mas-related G-protein coupled receptor member A1 (RF-amide G-protein coupled receptor) 304 34,381 Chain (1); Glycosylation (1); Sequence conflict (8); Topological domain (8); Transmembrane (7) TRANSMEM 18 38 Helical; Name=1. {ECO:0000255}.; TRANSMEM 54 74 Helical; Name=2. {ECO:0000255}.; TRANSMEM 76 96 Helical; Name=3. {ECO:0000255}.; TRANSMEM 132 152 Helical; Name=4. {ECO:0000255}.; TRANSMEM 167 187 Helical; Name=5. {ECO:0000255}.; TRANSMEM 207 227 Helical; Name=6. {ECO:0000255}.; TRANSMEM 244 264 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 17 Extracellular. {ECO:0000255}.; TOPO_DOM 39 53 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 75 75 Extracellular. {ECO:0000255}.; TOPO_DOM 97 131 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 153 166 Extracellular. {ECO:0000255}.; TOPO_DOM 188 206 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 228 243 Extracellular. {ECO:0000255}.; TOPO_DOM 265 304 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan receptor activated by a subset of RFamide-family neuropeptides such as FLRF-amide and FMRF-amide. Mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. Its effect is mediated by G(q) and G(11) proteins. May regulate the function of nociceptive neurons by modulation of pain perception. {ECO:0000269|PubMed:12397184}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11551509}; Multi-pass membrane protein {ECO:0000269|PubMed:11551509}. TISSUE SPECIFICITY: Expressed in a subset of sensory neurons that includes nociceptors. Expressed in the subclass of non-peptidergic sensory neurons that are IB4(+) and VR1(-). {ECO:0000269|PubMed:11551509}. +P29758 OAT_MOUSE Ornithine aminotransferase, mitochondrial (EC 2.6.1.13) (Ornithine--oxo-acid aminotransferase) 439 48,355 Chain (1); Modified residue (13); Transit peptide (1) Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-ornithine: step 1/1. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:P04181}. SUBUNIT: Homohexamer. {ECO:0000250|UniProtKB:P04181}. +A2AVR2 MROH7_MOUSE Maestro heat-like repeat-containing protein family member 7 (HEAT repeat-containing protein 8) 1279 141,710 Chain (1); Compositional bias (1); Glycosylation (6); Modified residue (1); Repeat (4); Transmembrane (2) TRANSMEM 548 568 Helical. {ECO:0000255}.; TRANSMEM 722 742 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q5NCE8 MRS2_MOUSE Magnesium transporter MRS2 homolog, mitochondrial (MRS2-like protein) 434 49,299 Chain (1); Erroneous initiation (1); Topological domain (3); Transit peptide (1); Transmembrane (2) TRANSMEM 329 351 Helical. {ECO:0000255}.; TRANSMEM 364 381 Helical. {ECO:0000255}. TOPO_DOM 54 328 Mitochondrial matrix. {ECO:0000255}.; TOPO_DOM 352 363 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 382 434 Mitochondrial matrix. {ECO:0000255}. FUNCTION: Magnesium transporter that mediates the influx of magnesium into the mitochondrial matrix. Required for normal expression of the mitochondrial respiratory complex I subunits. {ECO:0000250|UniProtKB:Q9HD23}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9HD23}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9HD23}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:11401429}. +Q6NZR2 MSD2_MOUSE Myb/SANT-like DNA-binding domain-containing protein 2 559 61,361 Alternative sequence (1); Chain (1); Compositional bias (1); Cross-link (2); Domain (1); Modified residue (6) +Q9QUM7 MSH5_MOUSE MutS protein homolog 5 833 92,602 Chain (1); Mutagenesis (1); Nucleotide binding (1); Sequence conflict (2) FUNCTION: Involved in DNA mismatch repair and meiotic recombination processes. Facilitates crossovers between homologs during meiosis (By similarity). {ECO:0000250}. SUBUNIT: Heterooligomer of MSH4 and MSH5. Interacts with HJURP (By similarity). {ECO:0000250}. +Q61474 MSI1H_MOUSE RNA-binding protein Musashi homolog 1 (Musashi-1) 362 39,119 Alternative sequence (2); Beta strand (13); Chain (1); Compositional bias (1); Domain (2); Helix (5); Modified residue (2); Mutagenesis (3); Turn (3) FUNCTION: RNA binding protein that regulates the expression of target mRNAs at the translation level. Regulates expression of the NOTCH1 antagonist NUMB. Binds RNA containing the sequence 5'-GUUAGUUAGUUAGUU-3' and other sequences containing the pattern 5'-[GA]U(1-3)AGU-3'. May play a role in the proliferation and maintenance of stem cells in the central nervous system. {ECO:0000269|PubMed:11359897, ECO:0000269|PubMed:12407178}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. DOMAIN: The first RNA recognition motif binds more strongly to RNA compared to the second one. TISSUE SPECIFICITY: Detected in olfactory bulb, brain stem, small intestine, and at low levels in brain cortex, hippocampus and ovary. Detected in neural progenitor cells, including neural stem cells. {ECO:0000269|PubMed:8660864}. +Q6PDM1 MSL1_MOUSE Male-specific lethal 1 homolog (MSL-1) (Hampin) (Male-specific lethal 1-like 1) (MSL1-like 1) (Male-specific lethal-1 homolog 1) 616 67,320 Alternative sequence (6); Chain (1); Coiled coil (1); Compositional bias (2); Cross-link (3); Frameshift (1); Helix (1); Modified residue (7); Mutagenesis (7); Region (3); Sequence conflict (2) FUNCTION: Component of histone acetyltransferase complex responsible for the majority of histone H4 acetylation at 'Lys-17' which is implicated in the formation of higher-order chromatin. structure (By similarity). Greatly enhances MSL2 E3 ubiquitin ligase activity, promoting monoubiquitination of histone H2B at 'Lys-35' (H2BK34Ub). This modification in turn stimulates histone H3 methylation at 'Lys-5' (H3K4me) and 'Lys-80' (H3K79me) and leads to gene activation, including that of HOXA9 and MEIS1. In the MSL complex, acts as a scaffold to tether MSL3 and KAT8 together for enzymatic activity regulation. {ECO:0000250, ECO:0000269|PubMed:21217699}. PTM: Sumoylated with SUMO1. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16119455}. SUBUNIT: Component of a multisubunit histone acetyltransferase complex (MSL) at least composed of the KAT8/MOF/MYST1, MSL1/hampin, MSL2 and MSL3. Directly interacts with MSL2 via its coiled coil domain (By similarity). Directly interacts with NUPR1 (By similarity). Interacts with TP53BP1; this interaction may be required for MSL1 DNA repair activity, but not for histone acetyltransferase activity (By similarity). Forms a MSL heterotetrameric core with MSL2 (By similarity). Interacts with KAT8 and MSL3; both interactions are direct. {ECO:0000250, ECO:0000269|PubMed:21217699}. DOMAIN: The coiled coil is formed by helices from two subunits in the MSL1 homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in testis and several other tissues. {ECO:0000269|PubMed:16119455}. +O08540 MSMB_MOUSE Beta-microseminoprotein (Prostate secreted seminal plasma protein) (Prostate secretory protein of 94 amino acids) (PSP-94) (PSP94) 113 12,845 Chain (1); Disulfide bond (5); Signal peptide (1) SUBCELLULAR LOCATION: Secreted. Note=Sperm surface. {ECO:0000250}. SUBUNIT: Homodimer; Interacts with PI16. {ECO:0000250}. +Q9CRA4 MSMO1_MOUSE Methylsterol monooxygenase 1 (EC 1.14.18.9) (C-4 methylsterol oxidase) 293 34,772 Chain (1); Domain (1); Motif (3); Transmembrane (3) TRANSMEM 55 75 Helical. {ECO:0000255}.; TRANSMEM 100 120 Helical. {ECO:0000255}.; TRANSMEM 199 219 Helical. {ECO:0000255}. Steroid biosynthesis; zymosterol biosynthesis; zymosterol from lanosterol: step 3/6. FUNCTION: Catalyzes the first step in the removal of the two C-4 methyl groups of 4,4-dimethylzymosterol. {ECO:0000250|UniProtKB:P53045}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. DOMAIN: The histidine box domains may contain the active site and/or be involved in metal ion binding. +Q8VEL0 MSPD1_MOUSE Motile sperm domain-containing protein 1 213 24,074 Alternative sequence (1); Chain (1); Domain (1); Motif (1); Mutagenesis (1); Transmembrane (2) TRANSMEM 159 179 Helical. {ECO:0000255}.; TRANSMEM 191 211 Helical. {ECO:0000255}. FUNCTION: Plays a role in differentiation and/or proliferation of mesenchymal stem cells (PubMed:21792907, PubMed:26175344). Proposed to be involved in epithelial-to-mesenchymal transition (EMT) (PubMed:21792907). However, another study suggests that it is not required for EMT or stem cell self-renewal and acts during later stages of differentiation (PubMed:26175344). {ECO:0000269|PubMed:21792907, ECO:0000269|PubMed:26175344}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305|PubMed:21792907}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000305|PubMed:21792907}; Multi-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Widely expressed. Shows highest expression in ribs, and slightly lower levels of expression in heart, kidney, muscle, thymus, calvariae and lung. Also detected at low levels in spleen and liver. {ECO:0000269|PubMed:21792907}. +Q9CWP6 MSPD2_MOUSE Motile sperm domain-containing protein 2 518 59,855 Alternative sequence (6); Beta strand (12); Chain (1); Domain (2); Frameshift (1); Helix (1); Natural variant (1); Sequence conflict (1); Transmembrane (1); Turn (2) TRANSMEM 497 517 Helical. {ECO:0000255}. FUNCTION: Promotes migration of primary monocytes and neutrophils, in response to various chemokines. {ECO:0000250|UniProtKB:Q8NHP6}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8NHP6}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8NHP6}. +Q8BGG6 MSPD3_MOUSE Motile sperm domain-containing protein 3 235 25,433 Chain (1); Domain (1); Transmembrane (2) TRANSMEM 179 199 Helical. {ECO:0000255}.; TRANSMEM 213 233 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Detected in heart, kidney, liver, spleen and brain. {ECO:0000269|PubMed:15533722}. DISEASE: Note=Defects in Mospd3 are a cause of defects of the right heart ventricle and of high mortality in newborns. {ECO:0000269|PubMed:15533722}. +Q9D035 NKAI1_MOUSE Sodium/potassium-transporting ATPase subunit beta-1-interacting protein 1 (Na(+)/K(+)-transporting ATPase subunit beta-1-interacting protein 1) (Protein FAM77C) 207 23,551 Chain (1); Glycosylation (1); Transmembrane (4) TRANSMEM 2 22 Helical. {ECO:0000255}.; TRANSMEM 35 55 Helical. {ECO:0000255}.; TRANSMEM 62 82 Helical. {ECO:0000255}.; TRANSMEM 147 167 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Interacts with ATP1B1 C-terminus. {ECO:0000269|PubMed:17606467}. TISSUE SPECIFICITY: Detected in the brain only and specifically in neurons. Expressed in multiple regions such as cerebral cortex, thalamus, hippocampus, olfactory bulb and brainstem as well as in cerebellum with high expression in granular cell layer. {ECO:0000269|PubMed:17606467}. +Q3URJ8 NKAI3_MOUSE Sodium/potassium-transporting ATPase subunit beta-1-interacting protein 3 (Na(+)/K(+)-transporting ATPase subunit beta-1-interacting protein 3) (Protein FAM77D) 181 20,700 Alternative sequence (2); Chain (1); Sequence conflict (2); Transmembrane (4) TRANSMEM 2 22 Helical. {ECO:0000255}.; TRANSMEM 35 55 Helical. {ECO:0000255}.; TRANSMEM 62 82 Helical. {ECO:0000255}.; TRANSMEM 152 172 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Interacts with ATP1B1. {ECO:0000250}. TISSUE SPECIFICITY: Detected in the brain only and specifically in neurons. Expressed in multiple regions such as cerebral cortex, thalamus, hippocampus, olfactory bulb and brainstem as well as in cerebellum with low expression in granular cell layer. {ECO:0000269|PubMed:17606467}. +Q9CQS2 NOP10_MOUSE H/ACA ribonucleoprotein complex subunit 3 (Nucleolar protein 10) (Nucleolar protein family A member 3) (snoRNP protein NOP10) 64 7,706 Chain (1) "FUNCTION: Required for ribosome biogenesis and telomere maintenance. Part of the H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Each rRNA can contain up to 100 pseudouridine (""psi"") residues, which may serve to stabilize the conformation of rRNAs. May also be required for correct processing or intranuclear trafficking of TERC, the RNA component of the telomerase reverse transcriptase (TERT) holoenzyme (By similarity). {ECO:0000250}." SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Nucleus, Cajal body {ECO:0000250}. Note=Also localized to Cajal bodies (coiled bodies). {ECO:0000250}. SUBUNIT: Part of the H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which contains NHP2/NOLA2, GAR1/NOLA1, NOP10/NOLA3, and DKC1/NOLA4, which is presumed to be the catalytic subunit. The complex contains a stable core formed by binding of one or two NOP10-DKC1 heterodimers to NHP2; GAR1 subsequently binds to this core via DKC1. The complex binds a box H/ACA small nucleolar RNA (snoRNA), which may target the specific site of modification within the RNA substrate. During assembly, the complex contains NAF1 instead of GAR1/NOLA1. The complex also interacts with TERC, which contains a 3'-terminal domain related to the box H/ACA snoRNAs. Specific interactions with snoRNAs or TERC are mediated by GAR1 and NHP2. Associates with NOLC1/NOPP140. H/ACA snoRNPs interact with the SMN complex, consisting of SMN1 or SMN2, GEMIN2/SIP1, DDX20/GEMIN3, and GEMIN4. This is mediated by interaction between GAR1 and SMN1 or SMN2. The SMN complex may be required for correct assembly of the H/ACA snoRNP complex. Component of the telomerase holoenzyme complex composed of one molecule of TERT, one molecule of WRAP53/TCAB1, two molecules of H/ACA ribonucleoprotein complex subunits DKC1, NOP10, NHP2 and GAR1, and a telomerase RNA template component (TERC). The telomerase holoenzyme complex is associated with TEP1, SMG6/EST1A and POT1. {ECO:0000250|UniProtKB:Q9NPE3}. +Q9QZQ0 NPAS3_MOUSE Neuronal PAS domain-containing protein 3 (Neuronal PAS3) (Basic-helix-loop-helix-PAS protein MOP6) (Member of PAS protein 6) 925 100,458 Chain (1); Compositional bias (3); Domain (4); Region (1); Sequence conflict (3) FUNCTION: May play a broad role in neurogenesis. May control regulatory pathways relevant to schizophrenia and to psychotic illness. {ECO:0000269|PubMed:15347806}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:15347806}. SUBUNIT: Efficient DNA binding requires dimerization with another bHLH protein. Interacts with ARNT; forms a heterodimer that binds core DNA sequence 5'-[AG]CGTG-3' within the hypoxia response element (HRE) of target gene promoters (PubMed:27782878). {ECO:0000269|PubMed:27782878}. TISSUE SPECIFICITY: Detected exclusively in adult brain in inhibitory interneurons. +Q794H2 NP1L3_MOUSE Nucleosome assembly protein 1-like 3 (Brain-specific protein MB20) 544 61,377 Chain (1); Compositional bias (2) SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11161794}. Cytoplasm {ECO:0000269|PubMed:11161794}. TISSUE SPECIFICITY: Expressed in brain. {ECO:0000269|PubMed:11161794}. +Q8BFZ2 PLPR1_MOUSE Phospholipid phosphatase-related protein type 1 (Lipid phosphate phosphatase-related protein type 1) (Plasticity-related gene 3 protein) (PRG-3) 325 35,932 Alternative sequence (1); Chain (1); Erroneous initiation (1); Glycosylation (3); Modified residue (1); Sequence conflict (2); Transmembrane (6) TRANSMEM 13 33 Helical. {ECO:0000255}.; TRANSMEM 67 87 Helical. {ECO:0000255}.; TRANSMEM 127 147 Helical. {ECO:0000255}.; TRANSMEM 201 218 Helical. {ECO:0000255}.; TRANSMEM 230 247 Helical. {ECO:0000255}.; TRANSMEM 257 277 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q64322 NPDC1_MOUSE Neural proliferation differentiation and control protein 1 (NPDC-1) 332 35,720 Chain (1); Compositional bias (2); Modified residue (1); Sequence conflict (2); Signal peptide (1); Transmembrane (1) TRANSMEM 191 211 Helical. {ECO:0000255}. FUNCTION: Suppresses oncogenic transformation in neural and non-neural cells and down-regulates neural cell proliferation. Might be involved in transcriptional regulation. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in the brain and nervous system. Not detected in liver, heart, skeletal muscle, spleen, pancreas, pituitary and adrenal glands. Expression increases when cultured neural cells are growth-arrested and begin to differentiate. +P49681 NPBW1_MOUSE Neuropeptides B/W receptor type 1 (G-protein coupled receptor 7) 329 36,076 Chain (1); Disulfide bond (1); Glycosylation (3); Topological domain (8); Transmembrane (7) TRANSMEM 44 64 Helical; Name=1. {ECO:0000255}.; TRANSMEM 76 96 Helical; Name=2. {ECO:0000255}.; TRANSMEM 113 133 Helical; Name=3. {ECO:0000255}.; TRANSMEM 159 179 Helical; Name=4. {ECO:0000255}.; TRANSMEM 210 230 Helical; Name=5. {ECO:0000255}.; TRANSMEM 251 271 Helical; Name=6. {ECO:0000255}.; TRANSMEM 290 312 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 43 Extracellular. {ECO:0000255}.; TOPO_DOM 65 75 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 97 112 Extracellular. {ECO:0000255}.; TOPO_DOM 134 158 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 180 209 Extracellular. {ECO:0000255}.; TOPO_DOM 231 250 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 272 289 Extracellular. {ECO:0000255}.; TOPO_DOM 313 329 Cytoplasmic. {ECO:0000255}. FUNCTION: Interacts specifically with a number of opioid ligands. Receptor for neuropeptides B and W, which may be involved in neuroendocrine system regulation, food intake and the organization of other signals (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q8CIZ9 NOX1_MOUSE NADPH oxidase 1 (NOX-1) (EC 1.-.-.-) 591 68,193 Alternative sequence (2); Chain (1); Domain (2); Glycosylation (2); Metal binding (4); Nucleotide binding (1); Region (1); Topological domain (7); Transmembrane (6) TRANSMEM 37 59 Helical; Name=1. {ECO:0000255}.; TRANSMEM 73 97 Helical; Name=2. {ECO:0000255}.; TRANSMEM 131 151 Helical; Name=3. {ECO:0000255}.; TRANSMEM 196 216 Helical; Name=4. {ECO:0000255}.; TRANSMEM 235 255 Helical; Name=5. {ECO:0000255}.; TRANSMEM 424 444 Helical; Name=6. {ECO:0000255}. TOPO_DOM 1 36 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 60 72 Extracellular. {ECO:0000255}.; TOPO_DOM 98 130 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 152 195 Extracellular. {ECO:0000255}.; TOPO_DOM 217 234 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 256 423 Extracellular. {ECO:0000255}.; TOPO_DOM 445 591 Cytoplasmic. {ECO:0000255}. FUNCTION: Pyridine nucleotide-dependent oxidoreductase that generates superoxide and might conduct H(+) ions as part of its electron transport mechanism. {ECO:0000269|PubMed:16724959}. SUBCELLULAR LOCATION: Cell projection, invadopodium membrane {ECO:0000250|UniProtKB:Q9Y5S8}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9Y5S8}. Cell membrane {ECO:0000250|UniProtKB:Q9Y5S8}. SUBUNIT: NOX1, NOXA1, NOXO1, RAC1 and CYBA forms a functional multimeric complex supporting ROS production. Interacts with NOXA1 and NOXO1. {ECO:0000269|PubMed:12473664}. TISSUE SPECIFICITY: Isoform 2 expressed in colon and vascular smooth muscle cells (VSMC). {ECO:0000269|PubMed:16724959}. +Q672J9 NOX3_MOUSE NADPH oxidase 3 (EC 1.6.3.-) 568 64,495 Chain (1); Domain (2); Erroneous initiation (2); Glycosylation (1); Mutagenesis (2); Sequence conflict (1); Topological domain (7); Transmembrane (6) TRANSMEM 13 33 Helical. {ECO:0000255}.; TRANSMEM 50 70 Helical. {ECO:0000255}.; TRANSMEM 104 124 Helical. {ECO:0000255}.; TRANSMEM 168 188 Helical. {ECO:0000255}.; TRANSMEM 202 222 Helical. {ECO:0000255}.; TRANSMEM 396 416 Helical. {ECO:0000255}. TOPO_DOM 1 12 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 34 49 Extracellular. {ECO:0000255}.; TOPO_DOM 71 103 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 125 167 Extracellular. {ECO:0000255}.; TOPO_DOM 189 201 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 223 395 Extracellular. {ECO:0000255}.; TOPO_DOM 417 568 Cytoplasmic. {ECO:0000255}. FUNCTION: NADPH oxidase which constitutively produces superoxide upon formation of a complex with CYBA/p22phox. Plays a role in the biogenesis of otoconia/otolith, which are crystalline structures of the inner ear involved in the perception of gravity. {ECO:0000269|PubMed:15014044, ECO:0000269|PubMed:15326186}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Interacts with and stabilizes CYBA/p22phox. TISSUE SPECIFICITY: Specifically expressed in inner ear by the spiral glanglion neurons, the vestibular system and the sensory epithelial cell layer of the saccule. Weakly expressed in skull and brain. {ECO:0000269|PubMed:15326186}. +Q9JHI8 NOX4_MOUSE NADPH oxidase 4 (EC 1.6.3.-) (Kidney oxidase-1) (KOX-1) (Kidney superoxide-producing NADPH oxidase) (Renal NAD(P)H-oxidase) (Superoxide-generating NADPH oxidase 4) 578 66,519 Alternative sequence (5); Chain (1); Domain (2); Frameshift (1); Glycosylation (2); Region (1); Sequence conflict (1); Topological domain (7); Transmembrane (6) TRANSMEM 17 37 Helical. {ECO:0000255}.; TRANSMEM 63 83 Helical. {ECO:0000255}.; TRANSMEM 105 125 Helical. {ECO:0000255}.; TRANSMEM 155 175 Helical. {ECO:0000255}.; TRANSMEM 189 209 Helical. {ECO:0000255}.; TRANSMEM 425 445 Helical. {ECO:0000255}. TOPO_DOM 1 16 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 38 62 Extracellular. {ECO:0000255}.; TOPO_DOM 84 104 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 126 154 Extracellular. {ECO:0000255}.; TOPO_DOM 176 188 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 210 424 Extracellular. {ECO:0000255}.; TOPO_DOM 446 578 Cytoplasmic. {ECO:0000255}. FUNCTION: Constitutive NADPH oxidase which generates superoxide intracellularly upon formation of a complex with CYBA/p22phox. Regulates signaling cascades probably through phosphatases inhibition. May function as an oxygen sensor regulating the KCNK3/TASK-1 potassium channel and HIF1A activity. May regulate insulin signaling cascade. May play a role in apoptosis, bone resorption and lipolysaccharide-mediated activation of NFKB. {ECO:0000269|PubMed:10869423, ECO:0000269|PubMed:11098048}. PTM: N-glycosylation is required for the function. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell junction, focal adhesion {ECO:0000250}. Cell membrane {ECO:0000250}. Note=May localize to plasma membrane and focal adhesions. {ECO:0000250}. SUBUNIT: Interacts with, relocalizes and stabilizes CYBA/p22phox. Interacts with TLR4. Interacts with protein disulfide isomerase (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: EXpressed in brain, in all layers of the cerebellum, in pyramidal cells of the Ammon horn and in Purkinje cells (at protein level). Expressed in osteoclasts, leukocytes, kidney, liver and lung. {ECO:0000269|PubMed:10869423, ECO:0000269|PubMed:11098048, ECO:0000269|PubMed:15802177}. +Q9QY53 NPHP1_MOUSE Nephrocystin-1 687 77,035 Chain (1); Coiled coil (2); Compositional bias (2); Domain (1); Modified residue (2); Sequence conflict (9) FUNCTION: Together with BCAR1 it may play a role in the control of epithelial cell polarity. Involved in the organization of apical junctions in kidney cells, together with NPHP4 and RPGRIP1L/NPHP8. Does not seem to be strictly required for ciliogenesis. Seems to help to recruit PTK2B/PYK2 to cell matrix adhesions, thereby initiating phosphorylation of PTK2B/PYK2 and PTK2B/PYK2-dependent signaling. May play a role in the regulation of intraflagellar transport (IFT) during cilia assembly. Required for normal retina development. In connecting photoreceptor cilia influences the movement of some IFT proteins such as IFT88 and WDR19. Involved in spermatogenesis; required for the differentiation of early elongating spermatids into spermatozoa. {ECO:0000269|PubMed:18684731, ECO:0000269|PubMed:19208653, ECO:0000269|PubMed:21565611}. SUBCELLULAR LOCATION: Cell junction, adherens junction. Cell projection, cilium. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250}. Cell junction, tight junction. Note=Colocalizes with E-cadherin and BCAR1 at or near the cell-cell adherens junctions. Localized to respiratory cilia axoneme. Localized to the transition zone of respiratory cilia, photoreceptor-connecting cilia and renal monocilia. In cultured renal cells, it localizes diffusely in the cytoplasm but, as cells approach confluence, it accumulates to basolateral tight junctions (By similarity). {ECO:0000250}. SUBUNIT: Interacts with INVS and NPHP3 (By similarity). Interacts with Crk-associated substrate BCAR1, NPHP4, PTK2B/PYK2 and tensin. Interacts with AHI1 and TNK2 (By similarity). Interacts with NPHP4 in a complex containing NPHP1, NPHP4 and RPGRIP1L/NPHP8 (By similarity). Interacts with IQCB1; the interaction likely requires additional interactors (By similarity). Interacts (via SH3 domain) with PKD1. Interacts with KIF7 (By similarity). Interacts with ANKS3 (PubMed:25671767). {ECO:0000250, ECO:0000269|PubMed:25671767}. DOMAIN: The SH3 domain mediates the stable interaction with Cas and is involved in establishing tight junctions in epithelial cells. {ECO:0000269|PubMed:12006559}. TISSUE SPECIFICITY: Widespread expression, with highest levels in testis, in cell stages of the first meiotic division and thereafter. Weaker expression in skeletal muscle, kidney, thyroid, ovary, lung, prostate, thymus, uterus, heart and liver. Lowest levels in brain and spleen. +Q61937 NPM_MOUSE Nucleophosmin (NPM) (Nucleolar phosphoprotein B23) (Nucleolar protein NO38) (Numatrin) 292 32,560 Beta strand (8); Chain (1); Compositional bias (3); Cross-link (17); Helix (1); Modified residue (33); Motif (2); Region (3); Site (2); Turn (1) FUNCTION: Involved in diverse cellular processes such as ribosome biogenesis, centrosome duplication, protein chaperoning, histone assembly, cell proliferation, and regulation of tumor suppressors p53/TP53 and ARF. Binds ribosome presumably to drive ribosome nuclear export. Associated with nucleolar ribonucleoprotein structures and bind single-stranded nucleic acids. Acts as a chaperonin for the core histones H3, H2B and H4. Stimulates APEX1 endonuclease activity on apurinic/apyrimidinic (AP) double-stranded DNA but inhibits APEX1 endonuclease activity on AP single-stranded RNA. May exert a control of APEX1 endonuclease activity within nucleoli devoted to repair AP on rDNA and the removal of oxidized rRNA molecules. In concert with BRCA2, regulates centrosome duplication. Regulates centriole duplication: phosphorylation by PLK2 is able to trigger centriole replication. Negatively regulates the activation of EIF2AK2/PKR and suppresses apoptosis through inhibition of EIF2AK2/PKR autophosphorylation. Antagonizes the inhibitory effect of ATF5 on cell proliferation and relieves ATF5-induced G2/M blockade. In complex with MYC enhances the transcription of MYC target genes. {ECO:0000250|UniProtKB:P06748}. PTM: Acetylated at C-terminal lysine residues, thereby increasing affinity to histones. {ECO:0000250|UniProtKB:P06748}.; PTM: ADP-ribosylated. {ECO:0000250|UniProtKB:P06748}.; PTM: Phosphorylated at Ser-4 by PLK1 and PLK2. Phosphorylation at Ser-4 by PLK2 in S phase is required for centriole duplication and is sufficient to trigger centriole replication. Phosphorylation at Ser-4 by PLK1 takes place during mitosis. Phosphorylated by CDK2 at Ser-125 and Thr-198. Phosphorylation at Thr-198 may trigger initiation of centrosome duplication. Phosphorylated by CDK1 at Thr-198, Thr-217, Thr-232 and Thr-235 during cell mitosis. When these four sites are phosphorated, RNA-binding activity seem to be abolished. May be phosphorylated at Ser-70 by NEK2. The Thr-198 phosphorylated form has higher affinity for ROCK2 (By similarity). {ECO:0000250|UniProtKB:P06748}.; PTM: Sumoylated by ARF. {ECO:0000250|UniProtKB:P06748}.; PTM: Ubiquitinated. Ubiquitination leads to proteasomal degradation. Deubiquitinated by USP36. {ECO:0000250|UniProtKB:P06748}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:P06748}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P06748}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P06748}. Note=Generally nucleolar, but is translocated to the nucleoplasm in case of serum starvation or treatment with anticancer drugs. Colocalizes with the methylated form of RPS10 in the granular component (GC) region of the nucleolus. Colocalized with nucleolin and APEX1 in nucleoli. NEK2 is required for its localization to the centrosome during mitosis (By similarity). {ECO:0000250|UniProtKB:P06748}. SUBUNIT: Decamer formed by two pentameric rings associated in a head-to-head fashion. Disulfide-linked dimers under certain conditions. Interacts with NSUN2 and SENP3 (By similarity). The SWAP complex consists of NPM1, NCL, PARP1 and SWAP70. Interacts with the methylated form of RPS10. Interacts (via N-terminal domain) with APEX1; the interaction is RNA-dependent and decreases peroxide-damaged cells. Interacts with NEK2. Interacts with ROCK2 and BRCA2 (By similarity). Interacts with RPGR. Interacts with CENPW (By similarity). Interacts with EIF2AK2/PKR. Interacts with CEBPA (isoform 4) (By similarity). Interacts with DDX31; this interaction prevents interaction between NPM1 and HDM2 (By similarity). Interacts with MYC; competitive with NOP53. Interacts with NOP53; the interaction is direct and competitive with MYC (By similarity). Interacts with LRRC34 (PubMed:24991885). Interacts with RRP1B (By similarity). {ECO:0000250|UniProtKB:P06748, ECO:0000269|PubMed:12882984, ECO:0000269|PubMed:24991885, ECO:0000269|PubMed:9642267}. TISSUE SPECIFICITY: Expressed in B-cells that have been induced to switch to various Ig isotypes. {ECO:0000269|PubMed:9642267}. +Q9CPP0 NPM3_MOUSE Nucleoplasmin-3 175 19,023 Chain (1); Compositional bias (2); Initiator methionine (1); Modified residue (5) FUNCTION: May act as a chaperone. PTM: Phosphorylated. {ECO:0000305}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. +Q9CQE1 NPS3B_MOUSE Protein NipSnap homolog 3B (NipSnap3B) (NipSnap-related protein) (Protein NipSnap homolog 3A) (NipSnap3A) 247 28,308 Chain (1); Modified residue (4); Sequence conflict (3) SUBCELLULAR LOCATION: Cytoplasm, cytosol. Note=May be part of some vesicular structure distinct from lysosomal vesicles. {ECO:0000250}. +P97295 NPY2R_MOUSE Neuropeptide Y receptor type 2 (NPY2-R) (NPY-Y2 receptor) (Y2 receptor) 381 42,628 Chain (1); Disulfide bond (1); Erroneous initiation (1); Glycosylation (1); Lipidation (1); Topological domain (8); Transmembrane (7) TRANSMEM 52 72 Helical; Name=1. {ECO:0000255}.; TRANSMEM 87 107 Helical; Name=2. {ECO:0000255}.; TRANSMEM 125 145 Helical; Name=3. {ECO:0000255}.; TRANSMEM 166 186 Helical; Name=4. {ECO:0000255}.; TRANSMEM 217 237 Helical; Name=5. {ECO:0000255}.; TRANSMEM 269 289 Helical; Name=6. {ECO:0000255}.; TRANSMEM 305 325 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 51 Extracellular. {ECO:0000255}.; TOPO_DOM 73 86 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 108 124 Extracellular. {ECO:0000255}.; TOPO_DOM 146 165 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 187 216 Extracellular. {ECO:0000255}.; TOPO_DOM 238 268 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 290 304 Extracellular. {ECO:0000255}.; TOPO_DOM 326 381 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for neuropeptide Y and peptide YY. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q8BZP8 NPSR1_MOUSE Neuropeptide S receptor (G-protein coupled receptor 154) (G-protein coupled receptor PGR14) 371 42,439 Chain (1); Disulfide bond (1); Erroneous initiation (1); Glycosylation (2); Topological domain (8); Transmembrane (7) TRANSMEM 53 73 Helical; Name=1. {ECO:0000255}.; TRANSMEM 83 103 Helical; Name=2. {ECO:0000255}.; TRANSMEM 124 144 Helical; Name=3. {ECO:0000255}.; TRANSMEM 165 185 Helical; Name=4. {ECO:0000255}.; TRANSMEM 213 233 Helical; Name=5. {ECO:0000255}.; TRANSMEM 276 296 Helical; Name=6. {ECO:0000255}.; TRANSMEM 313 333 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 52 Extracellular. {ECO:0000255}.; TOPO_DOM 74 82 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 104 123 Extracellular. {ECO:0000255}.; TOPO_DOM 145 164 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 186 212 Extracellular. {ECO:0000255}.; TOPO_DOM 234 275 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 297 312 Extracellular. {ECO:0000255}.; TOPO_DOM 334 371 Cytoplasmic. {ECO:0000255}. FUNCTION: G-protein coupled receptor for neuropeptide S (NPS). Promotes mobilization of intracellular Ca(2+) stores. Inhibits cell growth in response to NPS binding. Involved in pathogenesis of asthma and other IgE-mediated diseases. {ECO:0000250|UniProtKB:Q6W5P4}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6W5P4}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q6W5P4}. +O70342 NPY5R_MOUSE Neuropeptide Y receptor type 5 (NPY5-R) (NPY-Y5 receptor) (NPYY5-R) (Y5 receptor) 466 52,785 Chain (1); Disulfide bond (1); Glycosylation (4); Lipidation (1); Sequence conflict (2); Topological domain (8); Transmembrane (7) TRANSMEM 64 84 Helical; Name=1. {ECO:0000255}.; TRANSMEM 99 119 Helical; Name=2. {ECO:0000255}.; TRANSMEM 139 159 Helical; Name=3. {ECO:0000255}.; TRANSMEM 178 198 Helical; Name=4. {ECO:0000255}.; TRANSMEM 230 250 Helical; Name=5. {ECO:0000255}.; TRANSMEM 390 410 Helical; Name=6. {ECO:0000255}.; TRANSMEM 428 448 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 63 Extracellular. {ECO:0000255}.; TOPO_DOM 85 98 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 120 138 Extracellular. {ECO:0000255}.; TOPO_DOM 160 177 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 199 229 Extracellular. {ECO:0000255}.; TOPO_DOM 251 389 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 411 427 Extracellular. {ECO:0000255}.; TOPO_DOM 449 466 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for neuropeptide Y and peptide YY. The activity of this receptor is mediated by G proteins that inhibit adenylate cyclase activity. Seems to be associated with food intake. Could be involved in feeding disorders (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q61233 PLSL_MOUSE Plastin-2 (65 kDa macrophage protein) (L-plastin) (Lymphocyte cytosolic protein 1) (LCP-1) (pp65) 627 70,149 Calcium binding (2); Chain (1); Domain (6); Initiator methionine (1); Modified residue (21); Region (2); Sequence conflict (7) FUNCTION: Actin-binding protein. Plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. Modulates the cell surface expression of IL2RA/CD25 and CD69. {ECO:0000250|UniProtKB:P13796}. PTM: Phosphorylated on a serine residue in response to costimulation through TCR/CD3 and CD2 or CD28. Serine phosphorylation promotes association with the actin cytoskeleton and targeting to peripheral cell projections (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:14756805}. Cell projection {ECO:0000250}. Cell junction {ECO:0000250}. Cell projection, ruffle membrane {ECO:0000269|PubMed:14756805}; Peripheral membrane protein {ECO:0000269|PubMed:14756805}; Cytoplasmic side {ECO:0000269|PubMed:14756805}. Note=Relocalizes to the immunological synapse between peripheral blood T-lymphocytes and antibody-presenting cells in response to costimulation through TCR/CD3 and CD2 or CD28. Relocalizes to actin-rich cell projections upon serine phosphorylation (By similarity). Associated with the actin cytoskeleton at membrane ruffles. {ECO:0000250|UniProtKB:P13796}. SUBUNIT: Monomer (By similarity). Interacts with AIF1 (PubMed:14756805). Interacts with actin (By similarity). {ECO:0000250|UniProtKB:P13796, ECO:0000269|PubMed:14756805}. +Q99K51 PLST_MOUSE Plastin-3 (T-plastin) 630 70,742 Calcium binding (2); Chain (1); Domain (6); Modified residue (5); Region (2); Sequence conflict (1) FUNCTION: Actin-bundling protein. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. +Q64249 NR6A1_MOUSE Nuclear receptor subfamily 6 group A member 1 (Germ cell nuclear factor) (GCNF) (mGCNF) (Retinoid receptor-related testis-specific receptor) (RTR) 495 55,976 Alternative sequence (4); Beta strand (1); Chain (1); DNA binding (1); Domain (1); Helix (4); Mutagenesis (3); Region (1); Turn (2); Zinc finger (2) FUNCTION: Orphan nuclear receptor. Binds to a response element containing the sequence 5'-TCAAGGTCA-3'. May be involved in the regulation of gene expression in germ cell development during gametogenesis. {ECO:0000269|PubMed:7854358}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Homodimer. Interacts with UIMC1. {ECO:0000269|PubMed:12080054, ECO:0000269|PubMed:7760852}. TISSUE SPECIFICITY: Expressed in the germ cells of both the adult testis and ovary, being most abundant in spermatids. {ECO:0000269|PubMed:7835709, ECO:0000269|PubMed:7854358}. +Q3TV70 NR2CA_MOUSE Nuclear receptor 2C2-associated protein (TR4 orphan receptor-associated 16 kDa protein) 140 15,857 Chain (1) FUNCTION: May act as a repressor of NR2C2-mediated transactivation by suppressing the binding between NR2C2/TR4 and the TR4-response element in target genes. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with NR2C2/TR4. {ECO:0000250}. +Q8C4W3 NRN1L_MOUSE Neuritin-like protein (Candidate plasticity gene 15-2 protein) 162 17,390 Alternative sequence (1); Chain (1); Lipidation (1); Propeptide (1); Signal peptide (1) SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}. +Q9R0G8 NRK_MOUSE Nik-related protein kinase (EC 2.7.11.1) (Nck-interacting kinase-like embryo specific kinase) (NESK) (NIK-like embryo-specific kinase) 1455 163,647 Active site (1); Binding site (1); Chain (1); Coiled coil (1); Compositional bias (3); Domain (2); Modified residue (2); Mutagenesis (1); Nucleotide binding (1); Sequence caution (1); Sequence conflict (5) FUNCTION: May phosphorylate cofilin-1 and induce actin polymerization through this process, during the late stages of embryogenesis. Involved in the TNF-alpha-induced signaling pathway. {ECO:0000269|PubMed:10801798, ECO:0000269|PubMed:12837278}. +E9Q7X7 NRX2A_MOUSE Neurexin-2 (Neurexin II-alpha) (Neurexin-2-alpha) 1710 184,885 Chain (1); Compositional bias (2); Disulfide bond (12); Domain (9); Glycosylation (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1635 1655 Helical. {ECO:0000255}. TOPO_DOM 29 1634 Extracellular. {ECO:0000305}.; TOPO_DOM 1656 1710 Cytoplasmic. {ECO:0000305}. FUNCTION: Neuronal cell surface protein that may be involved in cell recognition and cell adhesion. May mediate intracellular signaling. {ECO:0000250|UniProtKB:Q63374}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. SUBUNIT: The laminin G-like domain 1 binds to NXPH1. Interacts with PATJ (By similarity). Interacts with CBLN1, CBLN2 and, less avidly, with CBLN4 (PubMed:22220752, PubMed:21410790). Isoforms alpha 2C bind to alpha-dystroglycan (By similarity). Interacts (via Laminin G-like 1 domain) with IGSF21 (Ig-like 1 domain) in a trans-interaction manner (PubMed:28864826). {ECO:0000250|UniProtKB:Q63374, ECO:0000269|PubMed:21410790, ECO:0000269|PubMed:22220752, ECO:0000269|PubMed:28864826}. +P47759 NSG2_MOUSE Neuronal vesicle trafficking-associated protein 2 (Neuron-specific protein family member 2) (Protein 8.5) (Protein p19) 171 19,000 Chain (1); Topological domain (2); Transmembrane (1) TRANSMEM 72 92 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 71 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 93 171 Lumenal. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q3KR51}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q3KR51}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q3KR51}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q3KR51}. Endosome membrane {ECO:0000250|UniProtKB:Q3KR51}. Early endosome membrane {ECO:0000250|UniProtKB:Q3KR51}. Late endosome membrane {ECO:0000250|UniProtKB:Q3KR51}. Lysosome lumen {ECO:0000250|UniProtKB:Q3KR51}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:7829526}. Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:7829526}. Endosome, multivesicular body membrane {ECO:0000269|PubMed:7829526}. Note=Endocytosed from the cell surface, thus entered into early endosomes, trafficks to late endosomes and degradates in lysosomes (By similarity). Mainly Golgi stack, but also found in small vacuolar organelles and multivesicular bodies (PubMed:7829526). Found in both stationary and motile endosomes (PubMed:28874679). {ECO:0000250|UniProtKB:Q3KR51, ECO:0000269|PubMed:28874679, ECO:0000269|PubMed:7829526}. TISSUE SPECIFICITY: Specifically expressed in neural and neuroendocrine tissues. Pituitary and less in adrenal gland and testis. Expressed in the hippocampus throughout development. Remains enriched in layer V cortical neurons during development. At P0, broadly expressed in the neocortex. Is down-regulated overall at P8 and P14, but remains relatively enriched in layer V. At P0 is lower expressed in the cerebellum. Expression remains low throughout development, and is undetectable by adulthood (PubMed:28299779). {ECO:0000269|PubMed:28299779}. +Q8K305 NSL1_MOUSE Kinetochore-associated protein NSL1 homolog 281 31,739 Chain (1) FUNCTION: Part of the MIS12 complex which is required for normal chromosome alignment and segregation and kinetochore formation during mitosis. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96IY1}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q96IY1}. Note=Associated with the kinetochore. {ECO:0000250|UniProtKB:Q96IY1}. SUBUNIT: Component of the MIS12 complex composed of MIS12, DSN1, NSL1/DC8 and PMF1. Interacts with KNL1 (By similarity). {ECO:0000250}. +P70172 NTCP2_MOUSE Ileal sodium/bile acid cotransporter (Apical sodium-dependent bile acid transporter) (ASBT) (Ileal Na(+)/bile acid cotransporter) (Ileal sodium-dependent bile acid transporter) (IBAT) (ISBT) (Na(+)-dependent ileal bile acid transporter) (Sodium/taurocholate cotransporting polypeptide, ileal) (Solute carrier family 10 member 2) 348 38,134 Chain (1); Glycosylation (2); Modified residue (1); Natural variant (4); Topological domain (8); Transmembrane (7) TRANSMEM 29 49 Helical. {ECO:0000255}.; TRANSMEM 88 108 Helical. {ECO:0000255}.; TRANSMEM 127 147 Helical. {ECO:0000255}.; TRANSMEM 158 178 Helical. {ECO:0000255}.; TRANSMEM 196 216 Helical. {ECO:0000255}.; TRANSMEM 225 245 Helical. {ECO:0000255}.; TRANSMEM 285 305 Helical. {ECO:0000255}. TOPO_DOM 1 28 Extracellular. {ECO:0000255}.; TOPO_DOM 50 87 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 109 126 Extracellular. {ECO:0000255}.; TOPO_DOM 148 157 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 179 195 Extracellular. {ECO:0000255}.; TOPO_DOM 217 224 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 246 284 Extracellular. {ECO:0000255}.; TOPO_DOM 306 348 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a critical role in the sodium-dependent reabsorption of bile acids from the lumen of the small intestine. Plays a key role in cholesterol metabolism (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Monomer and homodimer. {ECO:0000250}. +P03899 NU3M_MOUSE NADH-ubiquinone oxidoreductase chain 3 (EC 7.1.1.2) (NADH dehydrogenase subunit 3) 115 13,219 Beta strand (2); Chain (1); Helix (4); Sequence conflict (3); Transmembrane (3); Turn (2) TRANSMEM 3 23 Helical. {ECO:0000255}.; TRANSMEM 55 75 Helical. {ECO:0000255}.; TRANSMEM 86 106 Helical. {ECO:0000255}. FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q9WV70 NOC2L_MOUSE Nucleolar complex protein 2 homolog (Protein NOC2 homolog) (NOC2-like protein) (Novel INHAT repressor) 747 85,424 Chain (1); Compositional bias (1); Modified residue (4); Sequence conflict (3) FUNCTION: Acts as an inhibitor of histone acetyltransferase activity; prevents acetylation of all core histones by the EP300/p300 histone acetyltransferase at p53/TP53-regulated target promoters in a histone deacetylases (HDAC)-independent manner. Acts as a transcription corepressor of p53/TP53- and TP63-mediated transactivation of the p21/CDKN1A promoter. Involved in the regulation of p53/TP53-dependent apoptosis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Note=Translocates from the nucleoli to the nucleoplasm in presence of several stressors like ultraviolet irradiation and actinomycin-D. Predominantly detected in the nucleoli in non-mitotic cells. Predominantly detected in nucleoplasma in cells undergoing mitosis (By similarity). {ECO:0000250}. SUBUNIT: Interacts with p53/TP53. Interacts (via the N- and C-terminus domains) with AURKB (via the middle kinase domain). Interacts with TP63 (via activation domain). Interacts with histone H3 (via N-terminus and non-acetylated form preferentially). Associates with core histones and nucleosomes (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:16322561}. +Q922K7 NOP2_MOUSE Probable 28S rRNA (cytosine-C(5))-methyltransferase (EC 2.1.1.-) (Nucleolar protein 1) (Nucleolar protein 2 homolog) (Proliferating-cell nucleolar antigen p120) (Proliferation-associated nucleolar protein p120) 793 86,752 Active site (1); Binding site (3); Chain (1); Cross-link (3); Modified residue (12); Region (1); Sequence conflict (3) FUNCTION: Involved in ribosomal large subunit assembly. S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the C(5) position of cytosine 4447 in 28S rRNA. May play a role in the regulation of the cell cycle and the increased nucleolar activity that is associated with the cell proliferation. {ECO:0000250|UniProtKB:P46087}. PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. SUBUNIT: Interacts with MCRS1. Interacts with WDR46. Interacts with RRP1B. {ECO:0000250|UniProtKB:P46087}. +Q3UHX0 NOL8_MOUSE Nucleolar protein 8 1147 128,635 Alternative sequence (1); Chain (1); Coiled coil (2); Compositional bias (1); Cross-link (3); Domain (1); Erroneous initiation (2); Modified residue (20); Sequence conflict (2) FUNCTION: Plays an essential role in the survival of diffuse-type gastric cancer cells. Acts as a nucleolar anchoring protein for DDX47. May be involved in regulation of gene expression at the post-transcriptional level or in ribosome biogenesis in cancer cells (By similarity). {ECO:0000250}. PTM: Phosphorylated. {ECO:0000250|UniProtKB:Q76FK4}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Note=Localizes in the nucleolar-organizing region during ribosome biogenesis. {ECO:0000250}. SUBUNIT: Interacts with the GTP form of RRAGA, RRAGC and RRAGD. Interacts with NIP7. Interacts with DDX18; the interaction is RNA-dependent. Interacts with DDX47; the interaction is RNA-dependent (By similarity). {ECO:0000250}. +Q8BHY2 NOC4L_MOUSE Nucleolar complex protein 4 homolog (NOC4 protein homolog) (NOC4-like protein) (Nucleolar complex-associated protein 4-like protein) 516 58,676 Chain (1); Sequence conflict (1); Transmembrane (3) TRANSMEM 296 316 Helical. {ECO:0000255}.; TRANSMEM 347 367 Helical. {ECO:0000255}.; TRANSMEM 375 395 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. +Q8BMC4 NOP9_MOUSE Nucleolar protein 9 (Pumilio domain-containing protein NOP9) 636 70,046 Chain (1); Compositional bias (1); Erroneous initiation (2); Frameshift (1); Modified residue (1); Repeat (6); Sequence conflict (7) +Q32LZ8 PLPL5_MOUSE Patatin-like phospholipase domain-containing protein 5 (EC 3.1.1.-) 432 48,480 Active site (2); Alternative sequence (1); Chain (1); Domain (1); Motif (3) FUNCTION: Lipid hydrolase. {ECO:0000250}. +A2AJ88 PLPL7_MOUSE Patatin-like phospholipase domain-containing protein 7 (EC 3.1.1.-) (Neuropathy target esterase-related esterase) (NRE) (NTE-related esterase) 1352 150,494 Active site (2); Alternative sequence (4); Chain (1); Domain (1); Erroneous initiation (6); Glycosylation (5); Modified residue (4); Motif (3); Nucleotide binding (3); Sequence caution (1); Sequence conflict (6); Transmembrane (1) TRANSMEM 37 57 Helical. {ECO:0000255}. FUNCTION: Serine hydrolase, whose specific chemical modification by certain organophosphorus (OP) compounds leads to distal axonopathy (By similarity). Isoform 1 and isoform 2 have equal enzyme activity. Isoform 3 has no enzyme activity. {ECO:0000250, ECO:0000269|PubMed:22326266}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Mitochondrion membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Lysosome membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Microsome membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=Found in the nuclear, mitochondrial, lysosomal, and microsomal fractions. {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 1: Endoplasmic reticulum membrane; Single-pass membrane protein.; SUBCELLULAR LOCATION: Isoform 2: Endoplasmic reticulum membrane; Single-pass membrane protein.; SUBCELLULAR LOCATION: Isoform 3: Endoplasmic reticulum membrane; Single-pass membrane protein. TISSUE SPECIFICITY: Isoform 1, isoform 2 and isoform 3 are expressed in white adipose tissue, cardiac muscle, skeletal muscle, and testis. {ECO:0000269|PubMed:22326266}. +Q99K48 NONO_MOUSE Non-POU domain-containing octamer-binding protein (NonO protein) 473 54,541 Alternative sequence (1); Beta strand (5); Chain (1); Coiled coil (1); Compositional bias (3); Cross-link (11); Domain (2); Erroneous termination (1); Frameshift (1); Helix (3); Modified residue (12); Region (1); Sequence conflict (9); Turn (1) FUNCTION: DNA- and RNA binding protein, involved in several nuclear processes. Binds the conventional octamer sequence in double-stranded DNA. Also binds single-stranded DNA and RNA at a site independent of the duplex site. Involved in pre-mRNA splicing, probably as a heterodimer with SFPQ. Interacts with U5 snRNA, probably by binding to a purine-rich sequence located on the 3' side of U5 snRNA stem 1b. Together with PSPC1, required for the formation of nuclear paraspeckles. The SFPQ-NONO heteromer associated with MATR3 may play a role in nuclear retention of defective RNAs. The SFPQ-NONO heteromer may be involved in DNA unwinding by modulating the function of topoisomerase I/TOP1. The SFPQ-NONO heteromer may be involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination and may stabilize paired DNA ends. In vitro, the complex strongly stimulates DNA end joining, binds directly to the DNA substrates and cooperates with the Ku70/G22P1-Ku80/XRCC5 (Ku) dimer to establish a functional preligation complex. NONO is involved in transcriptional regulation. The SFPQ-NONO-NR5A1 complex binds to the CYP17 promoter and regulates basal and cAMP-dependent transcriptional activity. NONO binds to an enhancer element in long terminal repeats of endogenous intracisternal A particles (IAPs) and activates transcription. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer. Important for the functional organization of GABAergic synapses. Plays a specific and important role in the regulation of synaptic RNAs and GPHN/gephyrin scaffold structure, through the regulation of GABRA2 transcript (PubMed:26571461).Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway. {ECO:0000250|UniProtKB:Q15233, ECO:0000269|PubMed:22966205, ECO:0000269|PubMed:26571461, ECO:0000269|PubMed:8355702, ECO:0000269|PubMed:9001221}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15860628, ECO:0000269|PubMed:26571461}. Nucleus, nucleolus {ECO:0000250}. Nucleus speckle {ECO:0000250}. Note=Detected in punctate subnuclear structures often located adjacent to splicing speckles, called paraspeckles. {ECO:0000250}. SUBUNIT: Monomer and component of the SFPQ-NONO complex, which is probably a heterotetramer of two 52 kDa (NONO) and two 100 kDa (SFPQ) subunits. NONO is a component of spliceosome and U5.4/6 snRNP complexes (By similarity). Interacts with CPNE4 (via VWFA domain) (PubMed:12522145). Forms heterodimers with PSPC1; this involves formation of a coiled coil domain by helices from both proteins (PubMed:15140795). Part of complex consisting of SFPQ, NONO and MATR3. Part of a complex consisting of SFPQ, NONO and NR5A1. Part of a complex consisting of SFPQ, NONO and TOP1. Interacts with SPI1 (PubMed:8626664). Interacts with RNF43 (By similarity). Interacts with PER1 and PER2 (PubMed:22966205). Part of the HDP-RNP complex composed of at least HEXIM1, PRKDC, XRCC5, XRCC6, paraspeckle proteins (SFPQ, NONO, PSPC1, RBM14, and MATR3) and NEAT1 RNA. Interacts (via second RRM domain) with WASL; the interaction is direct. Component of a multiprotein complex with WASL and SFPQ (By similarity). {ECO:0000250|UniProtKB:Q15233, ECO:0000269|PubMed:12522145, ECO:0000269|PubMed:15140795, ECO:0000269|PubMed:22966205, ECO:0000269|PubMed:8626664}. TISSUE SPECIFICITY: Expressed in liver and suprachiasmatic nuclei, hippocampus and neocortex (at protein level). Expression is strongest in neurons in CA1 and CA3 pyramidal regions and granule cells of the dentate gyrus. Detected in testis and kidney. {ECO:0000269|PubMed:15860628, ECO:0000269|PubMed:22966205, ECO:0000269|PubMed:26571461}. +Q9DAX2 PLPP2_MOUSE Phospholipid phosphatase 2 (EC 3.1.3.4) (Lipid phosphate phosphohydrolase 2) (PAP2-gamma) (PAP2-G) (Phosphatidate phosphohydrolase type 2c) (Phosphatidic acid phosphatase 2c) (PAP-2c) (PAP2c) 276 31,193 Alternative sequence (2); Chain (1); Glycosylation (2); Transmembrane (6) TRANSMEM 5 25 Helical. {ECO:0000255}.; TRANSMEM 52 72 Helical. {ECO:0000255}.; TRANSMEM 88 108 Helical. {ECO:0000255}.; TRANSMEM 162 182 Helical. {ECO:0000255}.; TRANSMEM 190 210 Helical. {ECO:0000255}.; TRANSMEM 219 239 Helical. {ECO:0000255}. FUNCTION: Catalyzes the conversion of phosphatidic acid (PA) to diacylglycerol (DG). In addition it hydrolyzes lysophosphatidic acid (LPA), ceramide-1-phosphate (C-1-P) and sphingosine-1-phosphate (S-1-P) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SUBUNIT: Homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Expressed at high levels in lung, liver and kidney; at low levels in heart and brain, and was not detected in skeletal muscle. +P97459 NPAS1_MOUSE Neuronal PAS domain-containing protein 1 (Neuronal PAS1) 594 63,737 Beta strand (14); Chain (1); Compositional bias (1); Domain (4); Helix (12); Mutagenesis (4); Turn (2) FUNCTION: May control regulatory pathways relevant to schizophrenia and to psychotic illness. May play a role in late central nervous system development by modulating EPO expression in response to cellular oxygen level. Forms a heterodimer that binds core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) leading to transcriptional repression on its target gene TH (PubMed:27782878). {ECO:0000269|PubMed:15347806, ECO:0000269|PubMed:15635607, ECO:0000269|PubMed:27782878}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Efficient DNA binding requires dimerization with another bHLH protein. Interacts with ARNT; forms a heterodimer that binds core DNA sequence 5'-[AG]CGTG-3' within the hypoxia response element (HRE) leading to a transcriptional repressor on its target gene TH. {ECO:0000269|PubMed:15635607, ECO:0000269|PubMed:27782878}. TISSUE SPECIFICITY: Expressed in brain in inhibitory interneurons. Also found in spinal cord. {ECO:0000269|PubMed:15347806}. +P97460 NPAS2_MOUSE Neuronal PAS domain-containing protein 2 (Neuronal PAS2) 816 90,916 Chain (1); Domain (4); Metal binding (2); Mutagenesis (2); Region (1) FUNCTION: Transcriptional activator which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, ARNTL/BMAL1, ARNTL2/BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and ARNTL/BMAL1 or ARNTL2/BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-ARNTL/BMAL1|ARNTL2/BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress ARNTL/BMAL1 transcription, respectively. The NPAS2-ARNTL/BMAL1 heterodimer positively regulates the expression of MAOA, F7 and LDHA and modulates the circadian rhythm of daytime contrast sensitivity by regulating the rhythmic expression of adenylate cyclase type 1 (ADCY1) in the retina. NPAS2 plays an important role in sleep homeostasis and in maintaining circadian behaviors in normal light/dark and feeding conditions and in the effective synchronization of feeding behavior with scheduled food availability. Regulates the gene transcription of key metabolic pathways in the liver and is involved in DNA damage response by regulating several cell cycle and DNA repair genes. {ECO:0000269|PubMed:12843397, ECO:0000269|PubMed:16628007, ECO:0000269|PubMed:16636276, ECO:0000269|PubMed:17417633, ECO:0000269|PubMed:18230344, ECO:0000269|PubMed:18316400, ECO:0000269|PubMed:18439826, ECO:0000269|PubMed:20026146, ECO:0000269|PubMed:24048828, ECO:0000269|PubMed:24067359}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:16628007}. SUBUNIT: Component of the circadian clock oscillator which includes the CRY proteins, CLOCK or NPAS2, ARNTL/BMAL1 or ARNTL2/BMAL2, CSNK1D and/or CSNK1E, TIMELESS and the PER proteins. Efficient DNA binding requires dimerization with another bHLH protein. Interacts with NCOA3, KAT2B and CREBBP (By similarity). Forms a heterodimer with ARNTL/BMAL1 and this heterodimerization is required for E-box-dependent transactivation. Interacts with EP300. {ECO:0000250|UniProtKB:Q99743, ECO:0000269|PubMed:14645221, ECO:0000269|PubMed:16628007}. TISSUE SPECIFICITY: Expressed in the retinal ganglion cells (at protein level). Expressed in the hypothalamic suprachiasmatic CC nuclei (SCN) of the brain. Also found in spinal cord, and to a lesser extent in colon, small intestine and uterus. {ECO:0000269|PubMed:17417633, ECO:0000269|PubMed:24048828, ECO:0000269|PubMed:9012850}. +P60487 PLPP_MOUSE Pyridoxal phosphate phosphatase (PLP phosphatase) (EC 3.1.3.3) (EC 3.1.3.74) (Chronophin) 292 31,512 Active site (2); Beta strand (13); Binding site (2); Chain (1); Helix (14); Metal binding (3); Mutagenesis (1); Region (1); Turn (3) FUNCTION: Protein serine phosphatase that dephosphorylates 'Ser-3' in cofilin and probably also dephosphorylates phospho-serine residues in DSTN. Regulates cofilin-dependent actin cytoskeleton reorganization. Required for normal progress through mitosis and normal cytokinesis. Does not dephosphorylate phospho-threonines in LIMK1. Does not dephosphorylate peptides containing phospho-tyrosine (By similarity). Pyridoxal phosphate (PLP) phosphatase, which also catalyzes the dephosphorylation of pyridoxine 5'-phosphate (PNP) and pyridoxamine 5'-phosphate (PMP), with order of substrate preference PLP > PNP > PMP (By similarity) (PubMed:24338473, PubMed:24338687). {ECO:0000250|UniProtKB:Q96GD0, ECO:0000269|PubMed:24338473, ECO:0000269|PubMed:24338687}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q96GD0}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q96GD0}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q96GD0}; Peripheral membrane protein {ECO:0000250, ECO:0000250|UniProtKB:Q96GD0}; Cytoplasmic side {ECO:0000250|UniProtKB:Q96GD0}. Cell projection, lamellipodium membrane {ECO:0000250|UniProtKB:Q96GD0}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q96GD0}; Cytoplasmic side {ECO:0000250|UniProtKB:Q96GD0}. Cell membrane {ECO:0000250|UniProtKB:Q96GD0}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q96GD0}; Cytoplasmic side {ECO:0000250|UniProtKB:Q96GD0}. Note=Colocalizes with the actin cytoskeleton in membrane ruffles and lamellipodia. Diffusely distributed throughout the cytosol during pro-metaphase and metaphase. Detected at the dynamic cell poles during telophase. Detected at the cleavage furrow and contractile ring during cytokinesis. Transiently detected at the plasma membrane in late stages of cytokinesis. Detected at the midbody. {ECO:0000250|UniProtKB:Q96GD0}. SUBUNIT: Homodimer. {ECO:0000269|PubMed:24338473, ECO:0000269|PubMed:24338687}. TISSUE SPECIFICITY: Ubiquitous. highly expressed in brain (at protein level). {ECO:0000269|PubMed:24338473}. +Q7TPB0 PLPR3_MOUSE Phospholipid phosphatase-related protein type 3 (EC 3.1.3.4) (Lipid phosphate phosphatase-related protein type 3) (Plasticity-related gene 2 protein) (PRG-2) 716 76,693 Alternative sequence (2); Chain (1); Compositional bias (3); Glycosylation (2); Modified residue (6); Sequence conflict (2); Transmembrane (6) TRANSMEM 18 38 Helical. {ECO:0000255}.; TRANSMEM 70 90 Helical. {ECO:0000255}.; TRANSMEM 131 151 Helical. {ECO:0000255}.; TRANSMEM 205 225 Helical. {ECO:0000255}.; TRANSMEM 231 251 Helical. {ECO:0000255}.; TRANSMEM 261 281 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9DCJ9 NPL_MOUSE N-acetylneuraminate lyase (NALase) (EC 4.1.3.3) (N-acetylneuraminate pyruvate-lyase) (N-acetylneuraminic acid aldolase) (Sialate lyase) (Sialate-pyruvate lyase) (Sialic acid aldolase) (Sialic acid lyase) 320 35,130 Active site (1); Chain (1); Modified residue (1); Region (1); Site (1) Amino-sugar metabolism; N-acetylneuraminate degradation. FUNCTION: Catalyzes the cleavage of N-acetylneuraminic acid (sialic acid) to form pyruvate and N-acetylmannosamine via a Schiff base intermediate. It prevents sialic acids from being recycled and returning to the cell surface. Involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway. {ECO:0000269|PubMed:22692205}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homotetramer. {ECO:0000250}. +Q61983 NPT1_MOUSE Sodium-dependent phosphate transport protein 1 (Na(+)/PI cotransporter 1) (Renal Na(+)-dependent phosphate cotransporter 1) (Renal sodium-dependent phosphate transport protein 1) (Renal sodium-phosphate transport protein 1) (Sodium/phosphate cotransporter 1) (Solute carrier family 17 member 1) 465 51,649 Chain (1); Glycosylation (3); Sequence conflict (3); Transmembrane (10) TRANSMEM 79 99 Helical. {ECO:0000255}.; TRANSMEM 117 137 Helical. {ECO:0000255}.; TRANSMEM 176 196 Helical. {ECO:0000255}.; TRANSMEM 199 219 Helical. {ECO:0000255}.; TRANSMEM 260 280 Helical. {ECO:0000255}.; TRANSMEM 304 324 Helical. {ECO:0000255}.; TRANSMEM 337 356 Helical. {ECO:0000255}.; TRANSMEM 363 383 Helical. {ECO:0000255}.; TRANSMEM 399 419 Helical. {ECO:0000255}.; TRANSMEM 429 449 Helical. {ECO:0000255}. FUNCTION: Important for the resorption of phosphate by the kidney. May be involved in actively transporting phosphate into cells via Na(+) cotransport in the renal brush border membrane. Plays a role in urate transport in the kidney. {ECO:0000250|UniProtKB:Q14916}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:Q14916}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Interacts with PDZK1. {ECO:0000269|PubMed:11099500}. TISSUE SPECIFICITY: Kidney. +Q9WUE4 NPRL2_MOUSE GATOR complex protein NPRL2 (Gene 21 protein) (G21 protein) (Nitrogen permease regulator 2-like protein) (NPR2-like protein) 380 43,644 Chain (1); Region (1) FUNCTION: As a component of the GATOR1 complex functions as an inhibitor of the amino acid-sensing branch of the TORC1 pathway. The GATOR1 complex strongly increases GTP hydrolysis by RRAGA and RRAGB within RRAGC-containing heterodimers, thereby deactivating RRAGs, releasing mTORC1 from lysosomal surface and inhibiting mTORC1 signaling. The GATOR1 complex is negatively regulated by GATOR2 the other GATOR subcomplex in this amino acid-sensing branch of the TORC1 pathway. {ECO:0000250|UniProtKB:Q8WTW4}.; FUNCTION: Suppresses Src-dependent tyrosine phosphorylation and activation of PDPK1 and its downstream signaling. Down-regulates PDPK1 kinase activity by interfering with tyrosine phosphorylation at 'Tyr-9', 'Tyr-373' and 'Tyr-376' residues. May act as a tumor suppressor. Suppresses cell growth and enhances sensitivity to various anticancer drugs. {ECO:0000250|UniProtKB:Q8WTW4}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q8WTW4}. Note=Localization to lysosomes is amino acid-independent. {ECO:0000250|UniProtKB:Q8WTW4}. SUBUNIT: Forms a heterodimer with NPRL3. Interacts with PDPK1 (By similarity). Within the GATOR complex, component of the GATOR1 subcomplex, made of DEPDC5, NPRL2 and NPRL3. GATOR1 mediates the strong interaction of the GATOR complex with RRAGA/RRAGC and RRAGB/RRAGC heterodimers (By similarity). {ECO:0000250}. +Q62443 NPTX1_MOUSE Neuronal pentraxin-1 (NP1) (Neuronal pentraxin I) (NP-I) 432 47,117 Chain (1); Disulfide bond (1); Domain (1); Glycosylation (2); Metal binding (7); Signal peptide (1) FUNCTION: May be involved in mediating uptake of synaptic material during synapse remodeling or in mediating the synaptic clustering of AMPA glutamate receptors at a subset of excitatory synapses. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle {ECO:0000305}. SUBUNIT: Homooligomer or heterooligomer (probably pentamer) with neuronal pentraxin receptor (NPTXR). {ECO:0000250}. +Q61041 NPY4R_MOUSE Neuropeptide Y receptor type 4 (NPY4-R) (NPYR-D) (Pancreatic polypeptide receptor 1) (PP1) 375 42,648 Chain (1); Disulfide bond (1); Glycosylation (4); Lipidation (1); Sequence conflict (2); Topological domain (8); Transmembrane (7) TRANSMEM 40 60 Helical; Name=1. {ECO:0000255}.; TRANSMEM 79 99 Helical; Name=2. {ECO:0000255}.; TRANSMEM 117 137 Helical; Name=3. {ECO:0000255}.; TRANSMEM 156 176 Helical; Name=4. {ECO:0000255}.; TRANSMEM 212 232 Helical; Name=5. {ECO:0000255}.; TRANSMEM 267 287 Helical; Name=6. {ECO:0000255}.; TRANSMEM 302 322 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 39 Extracellular. {ECO:0000255}.; TOPO_DOM 61 78 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 100 116 Extracellular. {ECO:0000255}.; TOPO_DOM 138 155 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 177 211 Extracellular. {ECO:0000255}.; TOPO_DOM 233 266 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 288 301 Extracellular. {ECO:0000255}.; TOPO_DOM 323 375 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for neuropeptide Y and peptide YY. The rank order of affinity of this receptor for pancreatic polypeptides is PP >> PYY >= NPY. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Heart, detected in small intestine. +P0C0P8 NPS_MOUSE Neuropeptide S 89 9,861 Peptide (1); Propeptide (1); Signal peptide (1) FUNCTION: May play an important anorexigenic role. Modulates arousal and anxiety as well as increases locomotor activity. Binds to its receptor NPSR1 with nanomolar affinity to increase intracellular calcium concentrations. {ECO:0000269|PubMed:16279934}. SUBCELLULAR LOCATION: Secreted. +Q61212 NPY6R_MOUSE Neuropeptide Y receptor type 6 (NPY6-R) (Pancreatic polypeptide receptor 2) (PP2) 371 42,714 Chain (1); Disulfide bond (1); Glycosylation (3); Lipidation (1); Topological domain (8); Transmembrane (7) TRANSMEM 32 52 Helical; Name=1. {ECO:0000255}.; TRANSMEM 83 103 Helical; Name=2. {ECO:0000255}.; TRANSMEM 112 132 Helical; Name=3. {ECO:0000255}.; TRANSMEM 151 171 Helical; Name=4. {ECO:0000255}.; TRANSMEM 207 227 Helical; Name=5. {ECO:0000255}.; TRANSMEM 264 284 Helical; Name=6. {ECO:0000255}.; TRANSMEM 298 318 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 31 Extracellular. {ECO:0000255}.; TOPO_DOM 53 82 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 104 111 Extracellular. {ECO:0000255}.; TOPO_DOM 133 150 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 172 206 Extracellular. {ECO:0000255}.; TOPO_DOM 228 263 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 285 297 Extracellular. {ECO:0000255}.; TOPO_DOM 319 371 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for neuropeptide Y and peptide YY. The rank order of affinity of this receptor for pancreatic polypeptides is NPY = PYY >= NPY (2-36) = [Leu-31, Pro-34] NPY > NPY (13-36) > PP. The activity of this receptor is mediated by G proteins that inhibits adenylate cyclase activity. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Kidney and discrete regions of the hypothalamus including the suprachiasmatic nucleus, anterior hypothalamus, bed nucleus stria terminalis, and the ventromedial nucleus. +Q9JI75 NQO2_MOUSE Ribosyldihydronicotinamide dehydrogenase [quinone] (EC 1.10.5.1) (NRH dehydrogenase [quinone] 2) (NRH:quinone oxidoreductase 2) (Quinone reductase 2) (QR2) 231 26,248 Binding site (4); Chain (1); Metal binding (3); Modified residue (1); Nucleotide binding (3); Region (1) FUNCTION: The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinones involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +P45448 NR5A2_MOUSE Nuclear receptor subfamily 5 group A member 2 (Liver receptor homolog 1) (LRH-1) 560 64,020 Beta strand (3); Binding site (2); Chain (1); Cross-link (1); DNA binding (1); Domain (1); Helix (12); Motif (1); Turn (1); Zinc finger (2) FUNCTION: Nuclear receptor that acts as a key metabolic sensor by regulating the expression of genes involved in bile acid synthesis, cholesterol homeostasis and triglyceride synthesis. Together with the oxysterol receptors NR1H3/LXR-alpha and NR1H2/LXR-beta, acts as an essential transcriptional regulator of lipid metabolism. Plays an anti-inflammatory role during the hepatic acute phase response by acting as a corepressor: inhibits the hepatic acute phase response by preventing dissociation of the N-Cor corepressor complex. Key regulator of cholesterol 7-alpha-hydroxylase gene (CYP7A) expression in liver. May also contribute to the regulation of pancreas-specific genes and play important roles in embryonic development. {ECO:0000250|UniProtKB:O00482}. PTM: Sumoylated by SUMO1 at Lys-289 during the hepatic acute phase response, leading to promote interaction with GPS2 and prevent N-Cor corepressor complex dissociation. {ECO:0000250|UniProtKB:O00482}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O00482}. SUBUNIT: Binds DNA as a monomer (By similarity). Interacts with GRIP1, NCOA2 and NR0B2 (PubMed:12820970, PubMed:15976031). Interacts (when sumoylated) with GPS2; interaction with GPS2 onto hepatic acute phase protein promoters prevents N-Cor corepressor complex dissociation (By similarity). {ECO:0000250|UniProtKB:O00482, ECO:0000269|PubMed:12820970, ECO:0000269|PubMed:15976031}. +Q3UV55 NR1D1_MOUSE Nuclear receptor subfamily 1 group D member 1 (Rev-erbA-alpha) (V-erbA-related protein 1) (EAR-1) 615 66,802 Binding site (2); Chain (1); Compositional bias (1); DNA binding (1); Domain (1); Modified residue (5); Mutagenesis (1); Region (2); Sequence conflict (5); Zinc finger (2) FUNCTION: Transcriptional repressor which coordinates circadian rhythm and metabolic pathways in a heme-dependent manner. Integral component of the complex transcription machinery that governs circadian rhythmicity and forms a critical negative limb of the circadian clock by directly repressing the expression of core clock components ARTNL/BMAL1, CLOCK and CRY1. Also regulates genes involved in metabolic functions, including lipid and bile acid metabolism, adipogenesis, gluconeogenesis and the macrophage inflammatory response. Acts as a receptor for heme which stimulates its interaction with the NCOR1/HDAC3 corepressor complex, enhancing transcriptional repression. Recognizes two classes of DNA response elements within the promoter of its target genes and can bind to DNA as either monomers or homodimers, depending on the nature of the response element. Binds as a monomer to a response element composed of the consensus half-site motif 5'-[A/G]GGTCA-3' preceded by an A/T-rich 5' sequence (RevRE), or as a homodimer to a direct repeat of the core motif spaced by two nucleotides (RevDR-2). Acts as a potent competitive repressor of ROR alpha (RORA) function and regulates the levels of its ligand heme by repressing the expression of PPARGC1A, a potent inducer of heme synthesis. Regulates lipid metabolism by repressing the expression of APOC3 and by influencing the activity of sterol response element binding proteins (SREBPs); represses INSIG2 which interferes with the proteolytic activation of SREBPs which in turn govern the rhythmic expression of enzymes with key functions in sterol and fatty acid synthesis. Regulates gluconeogenesis via repression of G6PC and PEPCK and adipocyte differentiation via repression of PPARG. Regulates glucagon release in pancreatic alpha-cells via the AMPK-NAMPT-SIRT1 pathway and the proliferation, glucose-induced insulin secretion and expression of key lipogenic genes in pancreatic-beta cells. Positively regulates bile acid synthesis by increasing hepatic expression of CYP7A1 via repression of NR0B2 and NFIL3 which are negative regulators of CYP7A1. Modulates skeletal muscle oxidative capacity by regulating mitochondrial biogenesis and autophagy; controls mitochondrial biogenesis and respiration by interfering with the STK11-PRKAA1/2-SIRT1-PPARGC1A signaling pathway. Represses the expression of SERPINE1/PAI1, an important modulator of cardiovascular disease and the expression of inflammatory cytokines and chemokines in macrophages. Represses gene expression at a distance in macrophages by inhibiting the transcription of enhancer-derived RNAs (eRNAs). Plays a role in the circadian regulation of body temperature and negatively regulates thermogenic transcriptional programs in brown adipose tissue (BAT); imposes a circadian oscillation in BAT activity, increasing body temperature when awake and depressing thermogenesis during sleep. In concert with NR2E3, regulates transcriptional networks critical for photoreceptor development and function. In addition to its activity as a repressor, can also act as a transcriptional activator. In the ovarian granulosa cells acts as a transcriptional activator of STAR which plays a role in steroid biosynthesis. In collaboration with SP1, activates GJA1 transcription in a heme-independent manner. {ECO:0000269|PubMed:18227153, ECO:0000269|PubMed:18454201, ECO:0000269|PubMed:18565334, ECO:0000269|PubMed:19710360, ECO:0000269|PubMed:19721697, ECO:0000269|PubMed:20159955, ECO:0000269|PubMed:21408158, ECO:0000269|PubMed:21874017, ECO:0000269|PubMed:22166979, ECO:0000269|PubMed:22184247, ECO:0000269|PubMed:22474260, ECO:0000269|PubMed:22549838, ECO:0000269|PubMed:23201262, ECO:0000269|PubMed:23728303, ECO:0000269|PubMed:23852339, ECO:0000269|PubMed:23936124, ECO:0000269|PubMed:24030830, ECO:0000269|PubMed:24162845}. PTM: Ubiquitinated, leading to its proteasomal degradation (By similarity). Ubiquitinated by SIAH2; leading to its proteasomal degradation (By similarity). {ECO:0000250|UniProtKB:P20393}.; PTM: Undergoes lysosome-mediated degradation in a time-dependent manner in the liver. {ECO:0000269|PubMed:29937374}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407, ECO:0000269|PubMed:21874017}. Cytoplasm {ECO:0000269|PubMed:21874017}. Cell projection, dendrite {ECO:0000269|PubMed:21874017}. Cell projection, dendritic spine {ECO:0000269|PubMed:21874017}. Note=Localizes to the cytoplasm, dendrites and dendritic spine in the presence of OPHN1. SUBUNIT: Binds DNA as a monomer or a homodimer (By similarity). Interacts with NR2E3 and ZNHIT1 (By similarity). Interacts with C1D (PubMed:9405624). Interacts with SP1 (PubMed:22549838). Interacts with OPHN1 (via C-terminus) (PubMed:21874017). Interacts with PER2; the interaction associates PER2 to ARNTL promoter region (PubMed:20159955, PubMed:22170608). Interacts with CRY1 (By similarity). Interacts with CCAR2 (PubMed:23398316). Interacts with SIAH2 (By similarity). {ECO:0000250|UniProtKB:P20393, ECO:0000269|PubMed:20159955, ECO:0000269|PubMed:21874017, ECO:0000269|PubMed:22170608, ECO:0000269|PubMed:22549838, ECO:0000269|PubMed:23398316, ECO:0000269|PubMed:9405624}. DOMAIN: Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain. TISSUE SPECIFICITY: Expressed during adipocyte differentiation (at protein level). Expressed in skeletal muscle, bladder, lumbar spinal cord, pancreatic islets and hypothalamus. Expressed in developing and adult retina. In the adult retina, predominantly expressed in the outer nuclear layer, where rod and cone cells reside, and also localized to the ganglion cell layer. {ECO:0000269|PubMed:18227153, ECO:0000269|PubMed:18454201, ECO:0000269|PubMed:21408158, ECO:0000269|PubMed:21874017, ECO:0000269|PubMed:22166979, ECO:0000269|PubMed:23531614, ECO:0000269|PubMed:24603368}. +O35627 NR1I3_MOUSE Nuclear receptor subfamily 1 group I member 3 (Constitutive androstane receptor) (CAR) (Orphan nuclear receptor MB67) 358 40,913 Alternative sequence (2); Beta strand (3); Chain (1); DNA binding (1); Domain (1); Helix (15); Modified residue (1); Mutagenesis (8); Sequence conflict (2); Site (6); Turn (3); Zinc finger (2) FUNCTION: Binds and transactivates the retinoic acid response elements that control expression of the retinoic acid receptor beta 2 and alcohol dehydrogenase 3 genes. Transactivates both the phenobarbital responsive element module of the human CYP2B6 gene and the CYP3A4 xenobiotic response element (By similarity). {ECO:0000250, ECO:0000269|PubMed:10462436}. PTM: Phosphorylated at Thr-48 by PKC, dephosphorylation of Thr-48 is required for nuclear translocation and activation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Recruited to the cytoplasm by DNAJC7. SUBUNIT: Heterodimer of NR1I3 and RXR. Interacts with PSMC4. Interacts with ECT2. Directly interacts with DNAJC7; this complex may also include HSP90. {ECO:0000269|PubMed:14573755, ECO:0000269|PubMed:15610733, ECO:0000269|PubMed:17904126, ECO:0000269|PubMed:8603043}. DOMAIN: Composed by a short N-terminal domain followed by the DNA binding, hinge, and ligand binding/dimerization domains. TISSUE SPECIFICITY: Predominantly expressed in liver. +Q505F1 NR2C1_MOUSE Nuclear receptor subfamily 2 group C member 1 (Orphan nuclear receptor TR2) (Testicular receptor 2) (mTR2) 590 65,476 Alternative sequence (2); Chain (1); Cross-link (3); DNA binding (1); Domain (1); Modified residue (6); Mutagenesis (15); Natural variant (6); Region (2); Sequence conflict (14); Zinc finger (2) FUNCTION: Orphan nuclear receptor. Binds the IR7 element in the promoter of its own gene in an autoregulatory negative feedback mechanism. Primarily repressor of a broad range of genes including ESR1 and RARB. Together with NR2C2, forms the core of the DRED (direct repeat erythroid-definitive) complex that represses embryonic and fetal globin transcription. Binds to hormone response elements (HREs) consisting of two 5'-AGGTCA-3' half site direct repeat consensus sequences (By similarity). Also activator of OCT4 gene expression. Plays a fundamental role in early embryogenesis and regulates embryonic stem cell proliferation and differentiation. Mediator of retinoic acid-regulated preadipocyte proliferation. {ECO:0000250, ECO:0000269|PubMed:11463856, ECO:0000269|PubMed:12093744, ECO:0000269|PubMed:16130175, ECO:0000269|PubMed:16317770, ECO:0000269|PubMed:17187077, ECO:0000269|PubMed:17389641, ECO:0000269|PubMed:17431400, ECO:0000269|PubMed:17974920, ECO:0000269|PubMed:19131575, ECO:0000269|PubMed:8530418, ECO:0000269|PubMed:8858600, ECO:0000269|PubMed:9071982, ECO:0000269|PubMed:9774688}. PTM: Sumoylation requires both PIAS1 and UBE2I. Sumoylation appears to dissociate NR2C1 from the PML nuclear bodies. Enhances the interaction with NRIP1 but inhibits interaction with KAT2B. In proliferating cells, stimulation by all-trans retinoic acid, activation of MAPK1-mediated phosphorylation and recruitment to PML bodies with subsequent sumoylation, suppresses OCT4 expression.; PTM: Phosphorylated on several serine and threonine residues. Phosphorylation on Thr-210, stimulated by all-trans retinoic acid (atRA) mediates PML location and sumoylation in proliferating cells which then modulates its association with effector molecules, KAT2B and NRIP1. Phosphorylation on Ser-568 by PKC is important for protein stability and function as activator of RARB. {ECO:0000269|PubMed:16130175, ECO:0000269|PubMed:18682553}. SUBCELLULAR LOCATION: Nucleus. Nucleus, PML body. Note=Recruited by HDAC3, after all-trans retinoic acid stimulated MAPK1-mediated Thr-210 phosphorylation, to PML bodies for subsequent sumoylation. SUBUNIT: Homodimer. Heterodimer; with NR2C2 which is required for chromatin remodeling and for binding to promoter regions such as globin DR1 repeats. Interacts with ESR1; the interaction prevents homodimerization of ESR1 and suppresses its transcriptional activity and cell growth (By similarity). Interacts with NRIP1 (via its LXXLL motifs); the interaction provides corepressor activity. Interacts with HDAC3 (via the DNA-binding domain); the interaction recruits phosphorylated NR2C1 to PML bodies for sumoylation. Interacts with HDAC4 (via the DNA-binding domain). Interacts with PIAS1; the interaction is required for sumoylation of NR2C1. Interacts with UBE2I; the interaction is required for sumoylation of NR2C1. Interacts with KAT2B; the interaction acts as a corepressor of gene expression. {ECO:0000250, ECO:0000269|PubMed:11463856, ECO:0000269|PubMed:16317770, ECO:0000269|PubMed:17187077, ECO:0000269|PubMed:18682553, ECO:0000269|PubMed:19204783, ECO:0000269|PubMed:9774688}. TISSUE SPECIFICITY: Isoform 1 is highly expressed in the adlumenal compartment of the seminiferous tubule of adult testes (at protein level) and in the eyes of newborn animals. Weakly expressed in other adult organs including the seminal vesicle, prostate, ovary, adrenal gland, heart, thymus, placenta and brain. Expressed during embryonic stages in developing eyes, brain and cartilage primordia (at protein level). Also expressed in the developing spinal motor neurons and in the sympathetic-, parasympathetic- and sensory ganglia of the embryonic PNS. Expressed in the developing neural epithelia of the inner ear, nasal cavity, tongue and retina. At day 16.5, expressed in various tissues including kidney and intestine. In contrast, isoform 2 is widely expressed at a low level throughout the adult testis. {ECO:0000269|PubMed:12052874, ECO:0000269|PubMed:8530418, ECO:0000269|PubMed:8595902, ECO:0000269|PubMed:8858600, ECO:0000269|PubMed:9071982, ECO:0000269|PubMed:9504722, ECO:0000269|PubMed:9694834}. +Q06219 NR4A2_MOUSE Nuclear receptor subfamily 4 group A member 2 (NUR-related factor 1) (Orphan nuclear receptor NURR1) 598 66,593 Alternative sequence (2); Chain (1); Compositional bias (3); DNA binding (1); Domain (1); Motif (4); Zinc finger (2) FUNCTION: Transcriptional regulator which is important for the differentiation and maintenance of meso-diencephalic dopaminergic (mdDA) neurons during development. It is crucial for expression of a set of genes such as SLC6A3, SLC18A2, TH and DRD2 which are essential for development of mdDA neurons. {ECO:0000269|PubMed:19144721}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus. Note=Mostly nuclear; oxidative stress promotes cytoplasmic localization. {ECO:0000250}. SUBUNIT: Interacts with SFPQ, NCOR2, SIN3A and HADC1. The interaction with NCOR2 increases in the absence of PITX3. Interacts with PER2. {ECO:0000269|PubMed:19144721, ECO:0000269|PubMed:20159955}. DOMAIN: the ligand-binding domain (LBD) contains no cavity as a result of the tight packing of side chains from several bulky hydrophobic residues in the region normally occupied by ligands. NR4A2 lacks a 'classical' binding site for coactivators (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Brain. +Q8BHG1 NRDC_MOUSE Nardilysin (EC 3.4.24.61) (N-arginine dibasic convertase) (NRD convertase) (NRD-C) (Nardilysin convertase) 1161 132,891 Active site (1); Chain (1); Compositional bias (5); Metal binding (3); Modified residue (3); Signal peptide (1) FUNCTION: Cleaves peptide substrates on the N-terminus of arginine residues in dibasic pairs. +Q80XC6 NRDE2_MOUSE Protein NRDE2 homolog 1172 133,467 Chain (1); Coiled coil (1); Compositional bias (2); Erroneous initiation (1); Erroneous termination (1); Frameshift (1); Initiator methionine (1); Modified residue (1); Repeat (5); Sequence conflict (3) +Q920Q8 NS1BP_MOUSE Influenza virus NS1A-binding protein homolog (NS1-BP) (NS1-binding protein homolog) (Kelch family protein Nd1-L) (ND1-L2) (Nd1-S) 642 71,581 Alternative sequence (4); Chain (1); Domain (2); Erroneous initiation (1); Modified residue (5); Repeat (6); Sequence conflict (8) FUNCTION: Involved in many cell functions, including pre-mRNA splicing, the aryl hydrocarbon receptor (AHR) pathway, F-actin organization and protein ubiquitination. Plays a role in the dynamic organization of the actin skeleton as a stabilizer of actin filaments by association with F-actin through Kelch repeats (PubMed:12213805, PubMed:16317045). Protects cells from cell death induced by actin destabilization (PubMed:16952015). Functions as modifier of the AHR/Aryl hydrocarbon receptor pathway increasing the concentration of AHR available to activate transcription (By similarity). In addition, functions as a negative regulator of BCR(KLHL20) E3 ubiquitin ligase complex to prevent ubiquitin-mediated proteolysis of PML and DAPK1, two tumor suppressors (By similarity). Inhibits pre-mRNA splicing (in vitro) (By similarity). {ECO:0000250|UniProtKB:Q9Y6Y0, ECO:0000269|PubMed:12213805, ECO:0000269|PubMed:16317045, ECO:0000269|PubMed:16952015}.; FUNCTION: Isoform 2: May play a role in cell cycle progression in the nucleus. {ECO:0000269|PubMed:15684717}. SUBCELLULAR LOCATION: Isoform 1: Cytoplasm. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12213805}. Note=Associated with actin filaments. {ECO:0000269|PubMed:12213805}.; SUBCELLULAR LOCATION: Isoform 2: Nucleus {ECO:0000269|PubMed:15684717}. Note=Not associated with actin filaments (PubMed:15684717). {ECO:0000269|PubMed:15684717}. SUBUNIT: Homodimer; through the BTB domain. Interacts with AHR/Aryl hydrocarbon receptor (By similarity). {ECO:0000250|UniProtKB:Q9Y6Y0}. DOMAIN: When the BTB domain is lacking, AHR signaling induction promoted by IVNS1ABP is massively increased; Thus, the BTB domain inhibits AHR signaling induced by IVNS1ABP. {ECO:0000250|UniProtKB:Q9Y6Y0}. TISSUE SPECIFICITY: Ubiquitous expression. In the heart, the highest expression is detected in the ventricles and the lowest in the atria. Expressed in dendrites and spines in neurons. {ECO:0000269|PubMed:12213805, ECO:0000269|PubMed:15684717, ECO:0000269|PubMed:16317045}. +Q9JJY3 NSMA2_MOUSE Sphingomyelin phosphodiesterase 3 (EC 3.1.4.12) (Neutral sphingomyelinase 2) (nSMase-2) (nSMase2) (Neutral sphingomyelinase II) 655 71,197 Active site (1); Chain (1); Intramembrane (2); Lipidation (5); Metal binding (1); Modified residue (2); Site (1); Topological domain (3) INTRAMEM 11 31 Helical. {ECO:0000255}.; INTRAMEM 65 85 Helical. {ECO:0000255}. TOPO_DOM 1 10 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 32 64 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 86 655 Cytoplasmic. {ECO:0000255}. Lipid metabolism; sphingolipid metabolism. FUNCTION: Catalyzes the hydrolysis of sphingomyelin to form ceramide and phosphocholine. Ceramide mediates numerous cellular functions, such as apoptosis and growth arrest, and is capable of regulating these 2 cellular events independently. Also hydrolyzes sphingosylphosphocholine. Regulates the cell cycle by acting as a growth suppressor in confluent cells. Acts as a regulator of postnatal development and participates in bone and dentin mineralization. Overexpression enhances cell death, suggesting that it may be involved in apoptosis control. {ECO:0000269|PubMed:15051724, ECO:0000269|PubMed:15764706, ECO:0000269|PubMed:15929065, ECO:0000269|PubMed:16025116}. PTM: Palmitoylated, palmitoylation-deficient proteins are targeted for lysosomal degradation. {ECO:0000269|PubMed:17272284}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:15764706}; Lipid-anchor {ECO:0000269|PubMed:15764706}. Cell membrane {ECO:0000269|PubMed:17272284}; Lipid-anchor {ECO:0000269|PubMed:17272284}. Note=May localize to detergent-resistant subdomains of Golgi membranes of hypothalamic neurosecretory neurons (PubMed:15764706). TISSUE SPECIFICITY: Predominantly expressed in brain (at protein level). {ECO:0000269|PubMed:10823942}. +Q3UEZ8 NTCP4_MOUSE Sodium/bile acid cotransporter 4 (Na(+)/bile acid cotransporter 4) (Solute carrier family 10 member 4) 437 46,642 Chain (1); Glycosylation (4); Sequence conflict (1); Site (1); Topological domain (8); Transmembrane (7) TRANSMEM 104 124 Helical. {ECO:0000255}.; TRANSMEM 141 161 Helical. {ECO:0000255}.; TRANSMEM 198 218 Helical. {ECO:0000255}.; TRANSMEM 234 254 Helical. {ECO:0000255}.; TRANSMEM 268 288 Helical. {ECO:0000255}.; TRANSMEM 292 312 Helical. {ECO:0000255}.; TRANSMEM 361 381 Helical. {ECO:0000255}. TOPO_DOM 1 103 Extracellular. {ECO:0000255}.; TOPO_DOM 125 140 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 162 197 Extracellular. {ECO:0000255}.; TOPO_DOM 219 233 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 255 267 Extracellular. {ECO:0000255}.; TOPO_DOM 289 291 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 313 360 Extracellular. {ECO:0000255}.; TOPO_DOM 382 437 Cytoplasmic. {ECO:0000255}. FUNCTION: Transporter for bile acids. {ECO:0000250}. PTM: Activated following N-terminal proteolytic cleavage by thrombin and/or proteases. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Highest expression in the brain and significantly above background levels in the eye, prostate, and whole embryo tissue preparations. {ECO:0000269|PubMed:18355966}. +Q5PT54 NTCP5_MOUSE Sodium/bile acid cotransporter 5 (Na(+)/bile acid cotransporter 5) (Solute carrier family 10 member 5) 434 48,123 Chain (1); Glycosylation (2); Signal peptide (1); Topological domain (10); Transmembrane (9) TRANSMEM 130 150 Helical. {ECO:0000255}.; TRANSMEM 173 193 Helical. {ECO:0000255}.; TRANSMEM 204 226 Helical. {ECO:0000255}.; TRANSMEM 233 255 Helical. {ECO:0000255}.; TRANSMEM 269 289 Helical. {ECO:0000255}.; TRANSMEM 307 327 Helical. {ECO:0000255}.; TRANSMEM 332 352 Helical. {ECO:0000255}.; TRANSMEM 366 386 Helical. {ECO:0000255}.; TRANSMEM 396 416 Helical. {ECO:0000255}. TOPO_DOM 19 129 Extracellular. {ECO:0000255}.; TOPO_DOM 151 172 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 194 203 Extracellular. {ECO:0000255}.; TOPO_DOM 227 232 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 256 268 Extracellular. {ECO:0000255}.; TOPO_DOM 290 306 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 328 331 Extracellular. {ECO:0000255}.; TOPO_DOM 353 365 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 387 395 Extracellular. {ECO:0000255}.; TOPO_DOM 417 434 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8C985 NRX3B_MOUSE Neurexin-3-beta (Neurexin III-beta) [Cleaved into: Neurexin-3-beta, soluble form; Neurexin-3-beta, C-terminal fragment (NRXN3-CTF)] 567 62,376 Chain (3); Compositional bias (2); Domain (1); Frameshift (1); Glycosylation (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 493 513 Helical. {ECO:0000255}. TOPO_DOM 36 492 Extracellular. {ECO:0000255}.; TOPO_DOM 514 567 Cytoplasmic. {ECO:0000255}. FUNCTION: Neuronal cell surface protein that may be involved in cell recognition and cell adhesion. May play a role in angiogenesis (By similarity). {ECO:0000250}. PTM: Proccessed by alpha-secretase leading to the formation of an extracellular soluble protein as well as a C-terminal membrane-embedded fragment (CTF). Proteolysis of these CTFs by gamma-secretase releases intracellular domains (ICDs) and extracellular peptides (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: The cytoplasmic C-terminal region binds to CASK (By similarity). Binds to neuroligins NLGN1, NLGN2 and NLGN3 (By similarity). Weakly interacts with CBLN1 and CBLN2. Very weak binding, if any, to CBLN4. {ECO:0000250, ECO:0000269|PubMed:21410790, ECO:0000269|PubMed:22220752}. +P54729 NUB1_MOUSE NEDD8 ultimate buster 1 (Negative regulator of ubiquitin-like proteins 1) (Protein BS4) 614 70,307 Beta strand (2); Chain (1); Coiled coil (2); Domain (3); Frameshift (1); Helix (3); Motif (1); Region (2); Turn (1) FUNCTION: Specific down-regulator of the NEDD8 conjugation system. Recruits NEDD8, UBD, and their conjugates to the proteasome for degradation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Predominantly nuclear. {ECO:0000250}. SUBUNIT: Directly interacts with NEDD8 and PSMD4/S5a, a member of the regulatory subunit of the 26S proteasome. Interacts with AIPL1. The interaction with UBD via UBA domains facilitates the linking of UBD-conjugated target protein to the proteasome complex and accelerates UBD degradation and that of its conjugates (By similarity). {ECO:0000250|UniProtKB:Q9Y5A7}. +P0C027 NUD10_MOUSE Diphosphoinositol polyphosphate phosphohydrolase 3-alpha (DIPP-3-alpha) (DIPP3-alpha) (EC 3.6.1.52) (Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 3-alpha) (Diadenosine hexaphosphate hydrolase (AMP-forming)) (EC 3.6.1.60) (Nucleoside diphosphate-linked moiety X motif 10) (Nudix motif 10) 164 18,593 Active site (1); Binding site (3); Chain (1); Domain (1); Metal binding (4); Motif (1); Region (3) FUNCTION: Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate), suggesting that it may play a role in signal transduction. Also able to catalyze the hydrolysis of dinucleoside oligophosphates, with Ap6A and Ap5A being the preferred substrates. The major reaction products are ADP and p4a from Ap6A and ADP and ATP from Ap5A. Also able to hydrolyze 5-phosphoribose 1-diphosphate; however, the relevance of such activity in vivo remains unclear. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8NFP7}. TISSUE SPECIFICITY: Mainly expressed in testis, liver kidney and, at lower level, in heart, brain, spleen, lung and skeletal muscle. {ECO:0000269|PubMed:12689335}. +O08919 NUMBL_MOUSE Numb-like protein 604 64,130 Chain (1); Compositional bias (1); Domain (1); Modified residue (5); Sequence conflict (3) FUNCTION: Plays a role in the process of neurogenesis. Required throughout embryonic neurogenesis to maintain neural progenitor cells, also called radial glial cells (RGCs), by allowing their daughter cells to choose progenitor over neuronal cell fate. Not required for the proliferation of neural progenitor cells before the onset of embryonic neurogenesis. Also required postnatally in the subventricular zone (SVZ) neurogenesis by regulating SVZ neuroblasts survival and ependymal wall integrity. Negative regulator of NF-kappa-B signaling pathway. The inhibition of NF-kappa-B activation is mediated at least in part, by preventing MAP3K7IP2 to interact with polyubiquitin chains of TRAF6 and RIPK1 and by stimulating the 'Lys-48'-linked polyubiquitination and degradation of TRAF6 in cortical neurons. {ECO:0000269|PubMed:12410312, ECO:0000269|PubMed:15273690, ECO:0000269|PubMed:17174898, ECO:0000269|PubMed:9169836}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9169836}. Note=Symmetrically distributed throughout the cytoplasm in non dividing neuroblasts of the CNS. SUBUNIT: Interacts (via PTB domain) with MAP3K7IP2 (via C-terminal). Interacts (via C-terminal) with TRAF6 (via TRAF domains) (By similarity). Associates with EPS15 and NOTCH1. {ECO:0000250}. DOMAIN: The PTB domain is necessary for the inhibition of MAP3K7IP2-mediated activation of NF-kappa-B. {ECO:0000250}. TISSUE SPECIFICITY: Preferentially expressed in the nervous system. In the developing neocortex, expressed in postmitotic neurons in the cortical plate but not in progenitors within the ventricular zone. {ECO:0000269|PubMed:9169836}. +P28660 NCKP1_MOUSE Nck-associated protein 1 (NAP 1) (Brain protein H19) (MH19) (Membrane-associated protein HEM-2) (p125Nap1) 1128 128,784 Alternative sequence (2); Chain (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (1); Sequence conflict (3); Transmembrane (1) TRANSMEM 995 1015 Helical. {ECO:0000255}. FUNCTION: Part of the WAVE complex that regulates lamellipodia formation. The WAVE complex regulates actin filament reorganization via its interaction with the Arp2/3 complex. Actin remodeling activity is regulated by RAC1. As component of the WAVE1 complex, required for BDNF-NTRK2 endocytic trafficking and signaling from early endosomes (PubMed:27605705). {ECO:0000269|PubMed:14765121, ECO:0000269|PubMed:27605705}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14765121}; Single-pass membrane protein {ECO:0000269|PubMed:14765121}; Cytoplasmic side {ECO:0000269|PubMed:14765121}. Cell projection, lamellipodium membrane {ECO:0000269|PubMed:14765121}; Single-pass membrane protein {ECO:0000269|PubMed:14765121}; Cytoplasmic side {ECO:0000269|PubMed:14765121}. Cytoplasm {ECO:0000269|PubMed:14765121}. Note=At the interface between the lamellipodial actin meshwork and the membrane. SUBUNIT: Associates preferentially with the first SH3 domain of NCK (By similarity). Component of the WAVE1 complex composed of ABI2, CYFIP1 or CYFIP2, BRK1, NCKAP1 and WASF1/WAVE1. Within the complex, a heterodimer containing NCKAP1 and CYFIP1 interacts with a heterotrimer formed by WAVE1, ABI2 and BRK1. Component of the WAVE2 complex composed of ABI1, CYFIP1/SRA1, NCKAP1/NAP1 and WASF2/WAVE2. CYFIP2 binds to activated RAC1 which causes the complex to dissociate, releasing activated WASF1. The complex can also be activated by NCK1. Interacts with NYAP1, NYAP2 and MYO16. {ECO:0000250|UniProtKB:Q9Y2A7, ECO:0000269|PubMed:21946561}. TISSUE SPECIFICITY: High expression in cerebral cortex, not in cerebellar cortex. +Q80Z24 NEGR1_MOUSE Neuronal growth regulator 1 (Kindred of IgLON) (Kilon) (Neurotractin) 348 37,900 Chain (1); Disulfide bond (3); Domain (3); Glycosylation (6); Lipidation (1); Modified residue (1); Propeptide (1); Signal peptide (1) FUNCTION: May be involved in cell-adhesion. May function as a trans-neural growth-promoting factor in regenerative axon sprouting in the mammalian brain. {ECO:0000269|PubMed:15946856}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain. {ECO:0000269|PubMed:15946856}. +O35130 NEP1_MOUSE Ribosomal RNA small subunit methyltransferase NEP1 (EC 2.1.1.-) (18S rRNA (pseudouridine(1248)-N1)-methyltransferase) (18S rRNA Psi1248 methyltransferase) (Nucleolar protein EMG1 homolog) (Protein C2f) (Ribosome biogenesis protein NEP1) 244 26,974 Binding site (3); Chain (1); Modified residue (2); Region (1); Site (5) FUNCTION: S-adenosyl-L-methionine-dependent pseudouridine N(1)-methyltransferase that methylates pseudouridine at position 1248 (Psi1248) in 18S rRNA. Involved the biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi) conserved in eukaryotic 18S rRNA. Is not able to methylate uridine at this position. Has also an essential role in 40S ribosomal subunit biogenesis independent on its methyltransferase activity, facilitating the incorporation of ribosomal protein S19 during the formation of pre-ribosomes. {ECO:0000250|UniProtKB:Q06287, ECO:0000250|UniProtKB:Q92979}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q92979}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q06287}. +O88522 NEMO_MOUSE NF-kappa-B essential modulator (NEMO) (IkB kinase-associated protein 1) (IKKAP1) (mFIP-3) (Inhibitor of nuclear factor kappa-B kinase subunit gamma) (I-kappa-B kinase subunit gamma) (IKK-gamma) (IKKG) (IkB kinase subunit gamma) (NF-kappa-B essential modifier) 412 47,972 Chain (1); Coiled coil (1); Cross-link (17); Disulfide bond (2); Helix (3); Modified residue (6); Mutagenesis (17); Region (8); Sequence conflict (1); Zinc finger (1) FUNCTION: Regulatory subunit of the IKK core complex which phosphorylates inhibitors of NF-kappa-B thus leading to the dissociation of the inhibitor/NF-kappa-B complex and ultimately the degradation of the inhibitor. Its binding to scaffolding polyubiquitin seems to play a role in IKK activation by multiple signaling receptor pathways. Also considered to be a mediator for TAX activation of NF-kappa-B. Could be implicated in NF-kappa-B-mediated protection from cytokine toxicity. Involved in TLR3- and IFIH1-mediated antiviral innate response; this function requires 'Lys-27'-linked polyubiquitination. {ECO:0000269|PubMed:9927690}. PTM: Phosphorylation at Ser-68 attenuates aminoterminal homodimerization. {ECO:0000250}.; PTM: Polyubiquitinated on Lys-278 through 'Lys-63'; the ubiquitination is mediated by NOD2 and RIPK2 and probably plays a role in signaling by facilitating interactions with ubiquitin domain-containing proteins and activates the NF-kappa-B pathway. Polyubiquitinated on Lys-392 through 'Lys-63'; the ubiquitination is mediated by BCL10, MALT1 and TRAF6 and probably plays a role in signaling by facilitating interactions with ubiquitin domain-containing proteins and activates the NF-kappa-B pathway. Monoubiquitinated on Lys-270 and Lys-302; promotes nuclear export. Polyubiquitinated through 'Lys-27' by TRIM23; involved in antiviral innate and inflammatory responses. Linear polyubiquitinated on Lys-111, Lys-143, Lys-226, Lys-246, Lys-270, Lys-278, Lys-285, Lys-295, Lys-302 and Lys-319; the head-to-tail polyubiquitination is mediated by the LUBAC complex and plays a key role in NF-kappa-B activation. Deubiquitinated by USP10 in a TANK-dependent and -independent manner, leading to the negative regulation of NF-kappa-B signaling upon DNA damage (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9Y6K9}.; PTM: Sumoylated on Lys-270 and Lys-302 with SUMO1; the modification results in phosphorylation of Ser-85 by ATM leading to a replacement of the sumoylation by mono-ubiquitination on these residues. {ECO:0000250}.; PTM: Neddylated by TRIM40, resulting in stabilization of NFKBIA and down-regulation of NF-kappa-B activity. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Homodimer; disulfide-linked. Component of the I-kappa-B-kinase (IKK) core complex consisting of CHUK, IKBKB and IKBKG; probably four alpha/CHUK-beta/IKBKB dimers are associated with four gamma/IKBKG subunits. The IKK core complex seems to associate with regulatory or adapter proteins to form a IKK-signalosome holo-complex. The IKK complex associates with TERF2IP/RAP1, leading to promote IKK-mediated phosphorylation of RELA/p65. Part of a complex composed of NCOA2, NCOA3, CHUK/IKKA, IKBKB, IKBKG and CREBBP. Interacts with COPS3, CYLD, NALP2, TRPC4AP and PIDD1. Interacts with ATM; the complex is exported from the nucleus. Interacts with TRAF6. Interacts with IKBKE. Interacts with TANK; the interaction is enhanced by TBK1 and IKBKE. Part of a ternary complex consisting of TANK, IKBKB and IKBKG. Interacts with ZFAND5. Interacts with RIPK2. Interacts with TNIP1 and TNFAIP3; TNIP1 facilitates the TNFAIP3-mediated de-ubiquitination of IKBKG. Interacts with TNFAIP3; the interaction is induced by TNF stimulation and by polyubiquitin. Interacts with NLRP10. Interacts with TANK; this interaction increases in response to DNA damage (By similarity). Interacts with USP10; this interaction increases in response to DNA damage (By similarity). Interacts with ZC3H12A; this interaction increases in response to DNA damage (By similarity). Interacts with TRIM29; this interaction induces IKBKG/NEMO ubiquitination and proteolytic degradation (By similarity). Interacts with TRIM13; this interaction leads to IKBKG/NEMO ubiquitination (By similarity). {ECO:0000250|UniProtKB:Q9Y6K9, ECO:0000269|PubMed:12133833, ECO:0000269|PubMed:16684768, ECO:0000269|PubMed:19303852, ECO:0000269|PubMed:20622870}. DOMAIN: The leucine-zipper domain and the CCHC NOA-type zinc-finger are essential for polyubiquitin binding and for the activation of IRF3. {ECO:0000250}. +Q8R007 NECT4_MOUSE Nectin-4 (Ig superfamily receptor LNIR) (Nectin cell adhesion molecule 4) (Poliovirus receptor-related protein 4) 508 55,657 Alternative sequence (1); Chain (1); Disulfide bond (3); Domain (3); Erroneous initiation (1); Glycosylation (1); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 348 368 Helical. {ECO:0000255}. TOPO_DOM 31 347 Extracellular. {ECO:0000255}.; TOPO_DOM 369 508 Cytoplasmic. {ECO:0000255}. FUNCTION: Seems to be involved in cell adhesion through trans-homophilic and -heterophilic interactions, the latter including specifically interactions with NECTIN1. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Cell junction, adherens junction {ECO:0000250|UniProtKB:Q96NY8}. SUBUNIT: Self-associates. Interacts via its Ig-like V-type domain with NECTIN1 Ig-like V-type domain. Interacts via its C-terminus with AFDN (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain, lung, testis and embryo. {ECO:0000269|PubMed:11544254}. +Q91YT0 NDUV1_MOUSE NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial (EC 1.6.99.3) (EC 7.1.1.2) (Complex I-51kD) (CI-51kD) (NADH-ubiquinone oxidoreductase 51 kDa subunit) 464 50,834 Beta strand (17); Chain (1); Helix (22); Metal binding (4); Modified residue (5); Nucleotide binding (2); Transit peptide (1); Turn (8) FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Matrix side {ECO:0000250}. SUBUNIT: Complex I is composed of 45 different subunits. This is a component of the flavoprotein-sulfur (FP) fragment of the enzyme (By similarity). {ECO:0000250}. +P70255 NFIC_MOUSE Nuclear factor 1 C-type (NF1-C) (Nuclear factor 1/C) (CCAAT-box-binding transcription factor) (CTF) (Nuclear factor I/C) (NF-I/C) (NFI-C) (TGGCA-binding protein) 439 48,768 Alternative sequence (5); Chain (1); DNA binding (1); Modified residue (14) FUNCTION: Recognizes and binds the palindromic sequence 5'-TTGGCNNNNNGCCAA-3' present in viral and cellular promoters and in the origin of replication of adenovirus type 2. These proteins are individually capable of activating transcription and replication. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Binds DNA as a homodimer. TISSUE SPECIFICITY: Highest levels in skeletal muscle. Lower levels in heart, liver, kidney, lung and brain. Very low levels in testis and spleen. +O08750 NFIL3_MOUSE Nuclear factor interleukin-3-regulated protein (E4 promoter-binding protein 4) (Embryo implantation-related NFIL3/E4BP4-like transcription factor) 462 50,943 Chain (1); Cross-link (18); Domain (1); Modified residue (2); Region (3); Sequence conflict (4) FUNCTION: Acts as a transcriptional regulator that recognizes and binds to the sequence 5'-[GA]TTA[CT]GTAA[CT]-3', a sequence present in many cellular and viral promoters. Represses transcription from promoters with activating transcription factor (ATF) sites (By similarity). Represses promoter activity in osteoblasts. Represses transcriptional activity of PER1. Represses transcriptional activity of PER2 via the B-site on the promoter. Activates transcription from the interleukin-3 promoter in T-cells (By similarity). Competes for the same consensus-binding site with PAR DNA-binding factors (DBP, HLF and TEF). Component of the circadian clock that acts as a negative regulator for the circadian expression of PER2 oscillation in the cell-autonomous core clock. Protects pro-B cells from programmed cell death. {ECO:0000250, ECO:0000269|PubMed:11316793, ECO:0000269|PubMed:15087429, ECO:0000269|PubMed:17182630, ECO:0000269|PubMed:9122243}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:11316793}. SUBUNIT: Homodimer (By similarity). Binds DNA as a dimer (By similarity). Interacts with DR1 (By similarity). Interacts with PER2 and CRY2. {ECO:0000250, ECO:0000269|PubMed:17274955}. TISSUE SPECIFICITY: Expressed in suprachiasmatic nucleus and liver (at protein level). Expressed in suprachiasmatic nucleus, hippocampus, gyrus dentatus, piriform cortex, internal granular layer of olfactory bulb, dorsomedial hypothalamic nucleus, pontine nuclei, granular layer of cerebellum, liver and calvariae osteoblasts. {ECO:0000269|PubMed:11316793, ECO:0000269|PubMed:12743120}. +Q6PIJ4 NFRKB_MOUSE Nuclear factor related to kappa-B-binding protein (DNA-binding protein R kappa-B) 1296 138,764 Chain (1); Compositional bias (5); Cross-link (4); Erroneous initiation (1); Modified residue (6); Region (1) FUNCTION: Binds to the DNA consensus sequence 5'-GGGGAATCTCC-3'. {ECO:0000250}.; FUNCTION: Putative regulatory component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. Modulates the deubiquitinase activity of UCHL5 in the INO80 complex (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the chromatin remodeling INO80 complex; specifically part of a complex module associated with the N-terminus of INO80. Interacts with UCHL5 (By similarity). {ECO:0000250}. DOMAIN: NFRKB seems to be mostly disordered. The wing-helix like domain doesn't bind DNA (By similarity). {ECO:0000250}. +Q923S6 NEUL1_MOUSE E3 ubiquitin-protein ligase NEURL1 (EC 2.3.2.27) (Neuralized-like protein 1A) (m-neu1) (m-neuralized 1) (Neuralized1) (RING-type E3 ubiquitin transferase NEURL1) 574 61,778 Alternative sequence (3); Chain (1); Domain (2); Initiator methionine (1); Lipidation (1); Sequence conflict (11); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: Plays a role in hippocampal-dependent synaptic plasticity, learning and memory. Involved in the formation of spines and functional synaptic contacts by modulating the translational activity of the cytoplasmic polyadenylation element-binding protein CPEB3. Promotes ubiquitination of CPEB3, and hence induces CPEB3-dependent mRNA translation activation of glutamate receptor GRIA1 and GRIA2. Can function as an E3 ubiquitin-protein ligase to activate monoubiquitination of JAG1 (in vitro), thereby regulating the Notch pathway. Acts as a tumor suppressor; inhibits malignant cell transformation of medulloblastoma (MB) cells by inhibiting the Notch signaling pathway. {ECO:0000269|PubMed:18077452, ECO:0000269|PubMed:22153079}. PTM: Myristoylation is a determinant of membrane targeting. {ECO:0000269|PubMed:18077452}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:22153079}; Peripheral membrane protein {ECO:0000269|PubMed:22153079}. Perikaryon {ECO:0000269|PubMed:22153079}. Cell projection, dendrite {ECO:0000269|PubMed:22153079}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000269|PubMed:22153079}. Note=Colocalized with JAG1 at the cell surface (By similarity). Localized in the cell bodies of the pyramidal neurons and distributed along their apical dendrites. Colocalized with PSD95 in postsynaptic sites. Colocalized with CPEB3 at apical dendrites of CA1 neurons. {ECO:0000250}. SUBUNIT: Interacts with CPEB3 (via N-terminal domain); the interaction increases CPEB3 ubiquitination. Interacts with DLL1 (PubMed:19723503). {ECO:0000269|PubMed:19723503, ECO:0000269|PubMed:22153079}. TISSUE SPECIFICITY: Expressed in CA1 pyramidal neurons (at protein level). Expressed throughout the adult forebrain, including the cerebral cortex, amygdala, striatum, and CA1 area of the hippocampus. Expressed in sensory neurons of the olfactory epithelium, the vomeronasal organ, mammary gland and skeletal muscle. {ECO:0000269|PubMed:11481456, ECO:0000269|PubMed:11585928, ECO:0000269|PubMed:22153079}. +Q9WTK5 NFKB2_MOUSE Nuclear factor NF-kappa-B p100 subunit (DNA-binding factor KBF2) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 2) [Cleaved into: Nuclear factor NF-kappa-B p52 subunit] 899 96,832 Beta strand (8); Chain (2); Compositional bias (1); Cross-link (1); Domain (2); Helix (3); Modified residue (9); Motif (1); Region (1); Repeat (7); Site (1); Turn (1) FUNCTION: NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. In a non-canonical activation pathway, the MAP3K14-activated CHUK/IKKA homodimer phosphorylates NFKB2/p100 associated with RelB, inducing its proteolytic processing to NFKB2/p52 and the formation of NF-kappa-B RelB-p52 complexes. The NF-kappa-B heterodimeric RelB-p52 complex is a transcriptional activator. The NF-kappa-B p52-p52 homodimer is a transcriptional repressor. NFKB2 appears to have dual functions such as cytoplasmic retention of attached NF-kappa-B proteins by p100 and generation of p52 by a cotranslational processing. The proteasome-mediated process ensures the production of both p52 and p100 and preserves their independent function. p52 binds to the kappa-B consensus sequence 5'-GGRNNYYCC-3', located in the enhancer region of genes involved in immune response and acute phase reactions. p52 and p100 are respectively the minor and major form; the processing of p100 being relatively poor. Isoform p49 is a subunit of the NF-kappa-B protein complex, which stimulates the HIV enhancer in synergy with p65 (By similarity). In concert with RELB, regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer. {ECO:0000250, ECO:0000269|PubMed:22894897}. PTM: While translation occurs, the particular unfolded structure after the GRR repeat promotes the generation of p52 making it an acceptable substrate for the proteasome. This process is known as cotranslational processing. The processed form is active and the unprocessed form acts as an inhibitor (I kappa B-like), being able to form cytosolic complexes with NF-kappa B, trapping it in the cytoplasm. Complete folding of the region downstream of the GRR repeat precludes processing (By similarity). {ECO:0000250}.; PTM: Subsequent to MAP3K14-dependent serine phosphorylation, p100 polyubiquitination occurs then triggering its proteasome-dependent processing. {ECO:0000250}.; PTM: Constitutive processing is tightly suppressed by its C-terminal processing inhibitory domain, named PID, which contains the death domain. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Nuclear, but also found in the cytoplasm in an inactive form complexed to an inhibitor (I-kappa-B). {ECO:0000250}. SUBUNIT: Component of the NF-kappa-B RelB-p52 complex. Homodimer; component of the NF-kappa-B p52-p52 complex. Component of the NF-kappa-B p65-p52 complex. Component of the NF-kappa-B p52-c-Rel complex. NFKB2/p52 interacts with NFKBIE. Component of a complex consisting of the NF-kappa-B p50-p50 homodimer and BCL3 (By similarity). Directly interacts with MEN1 (By similarity). {ECO:0000250}. DOMAIN: The C-terminus of p100 might be involved in cytoplasmic retention, inhibition of DNA-binding by p52 homodimers, and/or transcription activation. {ECO:0000250}.; DOMAIN: The glycine-rich region (GRR) appears to be a critical element in the generation of p52. TISSUE SPECIFICITY: Highly expressed in lymph nodes and thymus. {ECO:0000269|PubMed:10398801}. +Q91YP2 NEUL_MOUSE Neurolysin, mitochondrial (EC 3.4.24.16) (Microsomal endopeptidase) (MEP) (Mitochondrial oligopeptidase M) (Neurotensin endopeptidase) 704 80,429 Active site (1); Chain (1); Metal binding (3); Modified residue (1); Sequence conflict (2); Transit peptide (1) FUNCTION: Hydrolyzes oligopeptides such as neurotensin, bradykinin and dynorphin A. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion intermembrane space {ECO:0000250}. Cytoplasm {ECO:0000250}. +Q9DB96 NGDN_MOUSE Neuroguidin (EIF4E-binding protein) 315 35,659 Chain (1); Coiled coil (2); Erroneous initiation (1); Initiator methionine (1); Modified residue (6); Region (1); Sequence conflict (1) FUNCTION: Inhibits mRNA translation in a cytoplasmic polyadenylation element (CPE)-dependent manner. {ECO:0000269|PubMed:16705177}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16705177}. Nucleus, nucleolus {ECO:0000250}. Chromosome, centromere {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:16705177}. Cell projection, axon {ECO:0000269|PubMed:16705177}. Cell projection, dendrite {ECO:0000269|PubMed:16705177}. Cell projection, filopodium {ECO:0000269|PubMed:16705177}. Note=Translocated from nucleolus to nuclear foci in response to UV damage (By similarity). Detected in axons, dendrites and filopodia. Colocalized with EIF4E in neurites. {ECO:0000250}. SUBUNIT: Interacts with CPEB1 and EIF4E. {ECO:0000269|PubMed:16705177}. TISSUE SPECIFICITY: Expressed in testis, ovary, spleen, kidney, hippocampus and cerebellum (at protein level). Expressed in testis, ovary, spleen, kidney, brain. {ECO:0000269|PubMed:16705177}. +Q9JHW2 NIT2_MOUSE Omega-amidase NIT2 (EC 3.5.1.3) (Nitrilase homolog 2) 276 30,502 Active site (3); Beta strand (18); Chain (1); Domain (1); Helix (9); Modified residue (5); Turn (4) FUNCTION: Has a omega-amidase activity. The role of omega-amidase is to remove potentially toxic intermediates by converting 2-oxoglutaramate and 2-oxosuccinamate to biologically useful 2-oxoglutarate and oxaloacetate, respectively. {ECO:0000269|PubMed:19596042}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: May form dimer. {ECO:0000269|PubMed:19595734}. +Q2LKW6 NL1B1_MOUSE NACHT, LRR and PYD domains-containing protein 1b allele 1 1233 140,688 Chain (1); Domain (3); Mutagenesis (49); Nucleotide binding (1); Repeat (2); Site (2) FUNCTION: As the sensor component of the NLRP1 inflammasome, plays a crucial role in innate immunity and inflammation. In response to pathogens and other damage-associated signals, initiates the formation of the inflammasome polymeric complex, made of Nlrp1b, CASP1, and possibly PYCARD. Recruitment of proCASP1 to the inflammasome promotes its activation and CASP1-catalyzed IL1B and IL18 maturation and secretion in the extracellular milieu. Activation of NLRP1 inflammasome is also required for HMGB1 secretion. The active cytokines and HMGB1 stimulate inflammatory responses. Inflammasomes can also induce pyroptosis, an inflammatory form of programmed cell death (PubMed:19651869, PubMed:21170303, PubMed:22753929, PubMed:22536155, PubMed:23818853). Activated by cleavage by Bacillus anthracis lethal toxin (LT) endopeptidase component (PubMed:19124602, PubMed:19651869, PubMed:19949100, PubMed:22536155, PubMed:23818853,PubMed:24935976, PubMed:24492532). Activated by metabolic inhibitors, such as 2-deoxy-D-glucose and sodium azide, by nutrient deprivation and hypoxia, possibly due to a decrease in cytosolic ATP (PubMed:23230290, PubMed:24935976). Also activated by Toxoplasma gondii (PubMed:24218483). Not activated by muramyl dipeptide, nor by full-length bacterial peptidoglycan (PubMed:22753929). Primary mediator of macrophage susceptibility to LT. In response to Bacillus anthracis infection, macrophages and dendritic cells release IL1B and undergo pyroptosis, an inflammatory form of programmed cell death. This early inflammatory response to the toxin increases resistance to infection by B. anthracis spores (PubMed:16429160, PubMed:19949100, PubMed:21170303, PubMed:22753929, PubMed:23818853). Binds ATP (By similarity). {ECO:0000250|UniProtKB:Q9C000, ECO:0000269|PubMed:16429160, ECO:0000269|PubMed:19124602, ECO:0000269|PubMed:19651869, ECO:0000269|PubMed:19949100, ECO:0000269|PubMed:21170303, ECO:0000269|PubMed:22536155, ECO:0000269|PubMed:22753929, ECO:0000269|PubMed:23230290, ECO:0000269|PubMed:23818853, ECO:0000269|PubMed:24218483, ECO:0000269|PubMed:24492532, ECO:0000269|PubMed:24935976}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19124602}. Cytoplasm, cytosol {ECO:0000269|PubMed:19124602}. Inflammasome {ECO:0000269|PubMed:24492532}. Membrane {ECO:0000269|PubMed:19124602}. SUBUNIT: Sensor component of NLRP1 inflammasomes. Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other damage-associated signals and play critical roles in innate immunity and inflammation. Classical inflammasomes consist of a signal sensor component, an adapter (ASC/PYCARD), which recruits an effector proinflammatory caspase (CASP1 and possibly CASP4/CASP11). CASP1 filament formation increases local enzyme concentration, resulting in trans-autocleavage and activation. Active CASP1 then processes IL1B and IL18 precursors, leading to the release of mature cytokines in the extracellular milieu and inflammatory response. In NLRP1 inflammasome, the role of PYCARD is not clear. Following activation, Nlrp1b may directly interact with CASP1 (through the CARD domain) to form a functional inflammasome (PubMed:19124602, PubMed:19651869, PubMed:24492532). Hence PYCARD may not be necessary for NLRP1 and CASP1 interaction, but is required for speck formation and full inflammasome activity (PubMed:19651869, PubMed:24492532). Homomer (PubMed:19651869, PubMed:22536155). Interacts (via LRR repeats) with BCL2 and BCL2L1 (via the loop between motifs BH4 and BH3); these interactions reduce NLRP1 inflammasome-induced CASP1 activation and IL1B release, possibly by impairing NLRP1 interaction with PYCARD (By similarity). Interacts with NOD2; this interaction may increase IL1B release (By similarity). Interacts with EIF2AK2/PKR; this interaction requires EIF2AK2 activity, is accompanied by EIF2AK2 autophosphorylation and promotes inflammasome assembly in response to Bacillus anthracis lethal toxin (PubMed:22801494). Interacts with MEFV; this interaction targets NLRP1 to degradation by autophagy, hence preventing excessive IL1B- and IL18-mediated inflammation (By similarity). {ECO:0000250|UniProtKB:Q9C000, ECO:0000269|PubMed:19124602, ECO:0000269|PubMed:19651869, ECO:0000269|PubMed:22536155, ECO:0000269|PubMed:24492532}. DOMAIN: The CARD domain is involved in the interaction with PYCARD, CASP1 and CASP4/CASP11. {ECO:0000250|UniProtKB:Q9C000}.; DOMAIN: The leucine-rich repeat (LRR) domain may be involved in autoinhibition in the absence of activating signal, possibly through intramolecular interaction with the NACHT domain. {ECO:0000269|PubMed:19651869, ECO:0000269|PubMed:23818853, ECO:0000269|PubMed:24935976}.; DOMAIN: The FIIND (domain with function to find) region is involved in homomerization, but not in CASP1-binding (PubMed:22536155). Autocatalytic cleavage in this region occurs constitutively, prior to activation signals, and is required for inflammasome activity (IL1B release), possibly by facilitating CASP1 binding. Both N- and C-terminal fragments remain associated (PubMed:22536155, PubMed:23818853). {ECO:0000269|PubMed:22536155, ECO:0000269|PubMed:23818853}. TISSUE SPECIFICITY: Widely expressed, including in macrophages. {ECO:0000269|PubMed:16429160, ECO:0000269|PubMed:23506131}. +Q99PA5 NKG7_MOUSE Protein NKG7 (Natural killer cell protein 7) 165 17,958 Chain (1); Transmembrane (4) TRANSMEM 9 29 Helical. {ECO:0000255}.; TRANSMEM 61 81 Helical. {ECO:0000255}.; TRANSMEM 92 112 Helical. {ECO:0000255}.; TRANSMEM 133 153 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cytoplasmic granule membrane; Multi-pass membrane protein. Note=Cytoplasmic granules of cytolytic T-lymphocytes, NK cells, and neutrophils. {ECO:0000250}. +Q8VEJ4 NLE1_MOUSE Notchless protein homolog 1 485 53,134 Chain (1); Initiator methionine (1); Modified residue (2); Mutagenesis (2); Repeat (8); Sequence conflict (1) FUNCTION: Plays a role in regulating Notch activity (Probable). Plays a role in regulating the expression of CDKN1A and several members of the Wnt pathway, probably via its effects on Notch activity. Required during embryogenesis for inner mass cell survival. {ECO:0000269|PubMed:16611995, ECO:0000269|PubMed:23231322, ECO:0000305}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. TISSUE SPECIFICITY: Highest expression in heart, brain, lung, liver, skeletal muscle and testis with lower levels in spleen and kidney. {ECO:0000269|PubMed:16611995}. +G5E897 PLGT3_MOUSE Protein O-glucosyltransferase 3 (EC 2.4.1.-) (KDEL motif-containing protein 2) (Protein O-xylosyltransferase POGLUT3) (EC 2.4.2.26) 503 57,686 Chain (1); Glycosylation (2); Motif (1); Repeat (1); Signal peptide (1) Protein modification; protein glycosylation. FUNCTION: Protein glucosyltransferase that catalyzes the transfer of glucose from UDP-glucose to a serine residue within the consensus sequence peptide C-X-N-T-X-G-S-F-X-C. Can also catalyze the transfer of xylose from UDP-xylose but less efficiently. Specifically targets extracellular EGF repeats of proteins such as NOTCH1 and NOTCH3. May regulate the transport of NOTCH1 and NOTCH3 to the plasma membrane and thereby the Notch signaling pathway. {ECO:0000250|UniProtKB:Q7Z4H8}. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138}. +P42580 NKX12_MOUSE NK1 transcription factor-related protein 2 (Homeobox protein SAX-1) (NKX-1.1) 305 32,013 Chain (1); Compositional bias (3); DNA binding (1); Erroneous gene model prediction (1); Sequence caution (2); Sequence conflict (1) FUNCTION: May function in cell specification, particularly in the CNS. PTM: Phosphorylated by HIPK2 in vitro. {ECO:0000269|PubMed:9748262}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Interacts with HIPK1, HIPK2, and HIPK3. {ECO:0000269|PubMed:9748262}. TISSUE SPECIFICITY: Expression detected in adult brain, testis and spleen. In the testis, expressed in the germ cells of the seminiferous epithelium, in elongating spermatids and in spermatozoa. Expressed throughout the brain with highest levels in regions of the cerebral cortex, hippocampus, diencephalon, pons, medulla and cerebellum. In the embryo, expressed in the developing posterior central nervous system. First seen in the ectoderm lateral to the primitive streak, later it encompasses the neural plate. Starting at day 9.5 pc, expressed in distinct areas of spinal cord, hindbrain, midbrain and forebrain. {ECO:0000269|PubMed:10681422, ECO:0000269|PubMed:7669696}. +P50220 NKX21_MOUSE Homeobox protein Nkx-2.1 (Thyroid nuclear factor 1) (Thyroid transcription factor 1) (TTF-1) (Thyroid-specific enhancer-binding protein) (T/EBP) 372 38,570 Chain (1); Compositional bias (3); DNA binding (1); Modified residue (1) FUNCTION: Transcription factor that binds and activates the promoter of thyroid specific genes such as thyroglobulin, thyroperoxidase, and thyrotropin receptor. Crucial in the maintenance of the thyroid differentiation phenotype. May play a role in lung development and surfactant homeostasis. Forms a regulatory loop with GRHL2 that coordinates lung epithelial cell morphogenesis and differentiation (PubMed:22955271). Activates the transcription of GNRHR and plays a role in enhancing the circadian oscillation of its gene expression. Represses the transcription of the circadian transcriptional repressor NR1D1 (PubMed:22356123). {ECO:0000250|UniProtKB:P23441, ECO:0000269|PubMed:22356123, ECO:0000269|PubMed:22955271}. PTM: Phosphorylated on serine residues by STK3/MST2. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22955271}. SUBUNIT: Interacts with WWTR1. {ECO:0000250|UniProtKB:P43699}. TISSUE SPECIFICITY: Thyroid, lung and brain. +B0F2B4 NLGN4_MOUSE Neuroligin 4-like (Neuroligin-4) (NL-4) 945 97,348 Chain (1); Compositional bias (5); Disulfide bond (3); Sequence conflict (10); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 762 782 Helical. {ECO:0000255}. TOPO_DOM 19 761 Extracellular. {ECO:0000255}.; TOPO_DOM 783 945 Cytoplasmic. {ECO:0000255}. FUNCTION: Cell surface protein involved in cell-cell-interactions. Plays a role in the formation or maintenance of synaptic junctions via its interactions (via the extracellular domains) with neurexin family members. Plays a role in synaptic signal transmission. {ECO:0000269|PubMed:18434543, ECO:0000269|PubMed:21282647}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Cell junction, synapse, postsynaptic cell membrane. Note=Detected at glycinergic postsynapses in retina. Detected on dendritic spines on cultured neurons. SUBUNIT: Homodimer. Interacts with NRXN1. Interacts with GPHN and ARHGEF9. {ECO:0000269|PubMed:18434543, ECO:0000269|PubMed:21282647}. TISSUE SPECIFICITY: Detected in brain cortex, septum, hippocampus, striatum, olfactory bulb, retina, colliculi, brain stem, cerebellum, thymus and skeletal muscle. Detected at inhibitory synapses throughout the brain and spinal cord (at protein level). Detected in brain, spleen, lung, skeletal muscle and kidney. {ECO:0000269|PubMed:18227507, ECO:0000269|PubMed:18434543, ECO:0000269|PubMed:21282647}. +P43688 NKX26_MOUSE Homeobox protein Nkx-2.6 (Homeobox protein NK-2 homolog F) 289 31,597 Chain (1); DNA binding (1) FUNCTION: Acts as a transcriptional activator (By similarity). In conjunction with NKX2-5, may play a role in both pharyngeal and cardiac embryonic development (PubMed:10733590, PubMed:11390666). {ECO:0000250|UniProtKB:A6NCS4, ECO:0000269|PubMed:10733590, ECO:0000269|PubMed:11390666}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: Not detected in any neonate or adult tissues. {ECO:0000269|PubMed:10733590}. +Q6KCD5 NIPBL_MOUSE Nipped-B-like protein (Delangin homolog) (SCC2 homolog) 2798 315,450 Alternative sequence (6); Chain (1); Compositional bias (1); Modified residue (36); Motif (1); Repeat (5); Sequence conflict (1) FUNCTION: Plays an important role in the loading of the cohesin complex on to DNA (PubMed:29094699). Forms a heterodimeric complex (also known as cohesin loading complex) with MAU2/SCC4 which mediates the loading of the cohesin complex onto chromatin. Plays a role in cohesin loading at sites of DNA damage. Its recruitement to double-strand breaks (DSBs) sites occurs in a CBX3-, RNF8- and RNF168-dependent manner whereas its recruitement to UV irradiation-induced DNA damage sites occurs in a ATM-, ATR-, RNF8- and RNF168-dependent manner (By similarity). Along with ZNF609, promotes cortical neuron migration during brain development by regulating the transcription of crucial genes in this process. Preferentially binds promoters containing paused RNA polymerase II. Up-regulates the expression of SEMA3A, NRP1, PLXND1 and GABBR2 genes, among others (PubMed:28041881). {ECO:0000250|UniProtKB:Q6KC79, ECO:0000269|PubMed:28041881, ECO:0000269|PubMed:29094699}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23967866, ECO:0000269|PubMed:24287868, ECO:0000269|PubMed:28041881, ECO:0000269|PubMed:28914604}. Chromosome {ECO:0000269|PubMed:23967866, ECO:0000269|PubMed:24287868}. SUBUNIT: Heterodimerizes with MAU2/SCC4 to form the cohesin loading complex (By similarity). The NIPBL-MAU2 heterodimer interacts with the SMC1A-SMC3 heterodimer and with the cohesin complex composed of SMC1A, SMC3, RAD21 and STAG1. Interacts directly (via PxVxL motif) with CBX3 and CBX5 (By similarity). Interacts with ZNF609 (via N-terminus) (PubMed:28041881). Interacts with the multiprotein complex Integrator (PubMed:28041881). {ECO:0000250|UniProtKB:Q6KC79, ECO:0000269|PubMed:28041881}. DOMAIN: Contains one Pro-Xaa-Val-Xaa-Leu (PxVxL) motif, which is required for interaction with chromoshadow domains. This motif requires additional residues -7, -6, +4 and +5 of the central Val which contact the chromoshadow domain. {ECO:0000250|UniProtKB:Q6KC79}.; DOMAIN: The C-terminal region containing HEAT repeats and Pro-Xaa-Val-Xaa-Leu (PxVxL) motif are involved in the recruitment of NIPBL to sites of DNA damage. {ECO:0000250|UniProtKB:Q6KC79}. TISSUE SPECIFICITY: Spermatocytes and oocytes (at protein level). {ECO:0000269|PubMed:23967866, ECO:0000269|PubMed:24287868}. +Q60806 PLK3_MOUSE Serine/threonine-protein kinase PLK3 (EC 2.7.11.21) (Cytokine-inducible serine/threonine-protein kinase) (FGF-inducible kinase) (Polo-like kinase 3) (PLK-3) 631 70,012 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Domain (3); Nucleotide binding (1); Sequence conflict (1) FUNCTION: Serine/threonine-protein kinase involved in cell cycle regulation, response to stress and Golgi disassembly. Polo-like kinases act by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates ATF2, BCL2L1, CDC25A, CDC25C, CHEK2, HIF1A, JUN, p53/TP53, p73/TP73, PTEN, TOP2A and VRK1. Involved in cell cycle regulation: required for entry into S phase and cytokinesis. Phosphorylates BCL2L1, leading to regulate the G2 checkpoint and progression to cytokinesis during mitosis. Plays a key role in response to stress: rapidly activated upon stress stimulation, such as ionizing radiation, reactive oxygen species (ROS), hyperosmotic stress, UV irradiation and hypoxia. Involved in DNA damage response and G1/S transition checkpoint by phosphorylating CDC25A, p53/TP53 and p73/TP73. Phosphorylates p53/TP53 in response to reactive oxygen species (ROS), thereby promoting p53/TP53-mediated apoptosis. Phosphorylates CHEK2 in response to DNA damage, promoting the G2/M transition checkpoint. Phosphorylates the transcription factor p73/TP73 in response to DNA damage, leading to inhibit p73/TP73-mediated transcriptional activation and pro-apoptotic functions. Phosphorylates HIF1A and JUN is response to hypoxia. Phosphorylates ATF2 following hyperosmotic stress in corneal epithelium. Also involved in Golgi disassembly during the cell cycle: part of a MEK1/MAP2K1-dependent pathway that induces Golgi fragmentation during mitosis by mediating phosphorylation of VRK1. May participate in endomitotic cell cycle, a form of mitosis in which both karyokinesis and cytokinesis are interrupted and is a hallmark of megakaryocyte differentiation, via its interaction with CIB1. {ECO:0000269|PubMed:20940307, ECO:0000269|PubMed:21376736, ECO:0000269|PubMed:9677325}. PTM: Phosphorylated in an ATM-dependent manner following DNA damage (By similarity). Phosphorylated as cells enter mitosis and dephosphorylated as cells exit mitosis. {ECO:0000250, ECO:0000269|PubMed:9677325}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Golgi apparatus {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Note=Translocates to the nucleus upon cisplatin treatment. Localizes to the Golgi apparatus during interphase (By similarity). {ECO:0000250}. SUBUNIT: Interacts (via the POLO-box domain) with CIB1; leading to inhibit PLK3 kinase activity. Interacts with GOLGB1 (By similarity). {ECO:0000250}. DOMAIN: The POLO box domains act as phosphopeptide-binding module that recognize and bind serine-[phosphothreonine/phosphoserine]-(proline/X) motifs. PLK3 recognizes and binds docking proteins that are already phosphorylated on these motifs, and then phosphorylates them. The POLO box domains mediates localization to the centrosome (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in skin. +O55126 NIPS2_MOUSE Protein NipSnap homolog 2 (NipSnap2) (Glioblastoma-amplified sequence) 281 32,933 Chain (1) FUNCTION: May act as a positive regulator of L-type calcium channels. {ECO:0000269|PubMed:22627147}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:22627147}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:O75323}. SUBUNIT: Interacts with VDAC1. {ECO:0000250|UniProtKB:O75323}. +Q8VIH1 NOBOX_MOUSE Homeobox protein NOBOX (Homeodomain-containing protein OG-2) (Newborn ovary homeobox protein) (Oocyte-specific homeobox protein) 527 57,565 Chain (1); Compositional bias (1); DNA binding (1); Mutagenesis (3); Sequence conflict (1) FUNCTION: Transcription factor which plays an essential role in postnatal follicle development. Binds preferentially to the DNA sequences 5'-TAATTG-3', 5'-TAGTTG-3' and 5'-TAATTA-3'. Directly regulates the transcription of POU5F1 and GDF9 during early folliculogenesis. {ECO:0000269|PubMed:15326356, ECO:0000269|PubMed:16997917}. SUBCELLULAR LOCATION: Nucleus. TISSUE SPECIFICITY: Specifically expressed in ovaries and testes. In ovaries, expressed in oocytes from primordial through antral follicles but not in granulosa cells, theca cells and corpora lutea. {ECO:0000269|PubMed:11804785}. +Q9CPT5 NOP16_MOUSE Nucleolar protein 16 178 21,139 Chain (1); Cross-link (1); Modified residue (3); Natural variant (2); Sequence conflict (1) SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. +Q8BHB0 NOD1_MOUSE Nucleotide-binding oligomerization domain-containing protein 1 (Caspase recruitment domain-containing protein 4) 953 107,740 Chain (1); Domain (2); Natural variant (1); Nucleotide binding (1); Repeat (8) FUNCTION: Enhances caspase-9-mediated apoptosis. Induces NF-kappa-B activity via RIPK2 and IKK-gamma. Confers responsiveness to intracellular bacterial lipopolysaccharides (LPS). Forms an intracellular sensing system along with ARHGEF2 for the detection of microbial effectors during cell invasion by pathogens. Recruits NLRP10 to the cell membrane following bacterial infection (By similarity). {ECO:0000250}. PTM: Ubiquitinated. 'Lys-48'-linked polyubiquitination by RNF34 promotes proteasomal degradation and thereby negatively regulates NOD1 for instance in NF-kappa-B activition. {ECO:0000250|UniProtKB:Q9Y239}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Apical cell membrane {ECO:0000250}. Basolateral cell membrane {ECO:0000250}. Note=Detected in the cytoplasm and at the cell membrane. Following bacterial infection, localizes to bacterial entry sites in the cell membrane. Recruited to the basolateral and apical membranes in polarized epithelial cells (By similarity). {ECO:0000250}. SUBUNIT: Homodimer. Self-associates. Binds to caspase-9 and RIPK2 by CARD-CARD interaction. Interacts with ARHGEF2. Interacts with NLRP10 and recruits it to the cell membrane following invasive bacterial infection. Interacts with RNF34. {ECO:0000250|UniProtKB:Q9Y239}. +Q8R3N1 NOP14_MOUSE Nucleolar protein 14 (Nucleolar complex protein 14) 860 98,769 Chain (1); Modified residue (4); Sequence conflict (12) FUNCTION: Involved in nucleolar processing of pre-18S ribosomal RNA. Has a role in the nuclear export of 40S pre-ribosomal subunit to the cytoplasm (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. SUBUNIT: Component of the ribosomal small subunit (SSU) processome. {ECO:0000250}. +Q9Z2Y8 PLPHP_MOUSE Pyridoxal phosphate homeostasis protein (PLP homeostasis protein) (Proline synthase co-transcribed bacterial homolog protein) (Pyridoxal phosphate-binding protein) 274 30,049 Chain (1); Modified residue (6) FUNCTION: Pyridoxal 5'-phosphate (PLP)-binding protein, which may be involved in intracellular homeostatic regulation of pyridoxal 5'-phosphate (PLP), the active form of vitamin B6. {ECO:0000255|HAMAP-Rule:MF_03225}. +Q8BK35 NOP53_MOUSE Ribosome biogenesis protein NOP53 (Glioma tumor suppressor candidate region gene 2 protein) (PreS1-binding protein) 484 55,793 Chain (1); Initiator methionine (1); Modified residue (3); Region (4); Sequence conflict (2) FUNCTION: Nucleolar protein which is involved in the integration of the 5S RNP into the ribosomal large subunit during ribosome biogenesis. In ribosome biogenesis, may also play a role in rRNA transcription (By similarity). Also functions as a nucleolar sensor that regulates the activation of p53/TP53 in response to ribosome biogenesis perturbation, DNA damage and other stress conditions. DNA damage or perturbation of ribosome biogenesis disrupt the interaction between NOP53 and RPL11 allowing RPL11 transport to the nucleoplasm where it can inhibit MDM2 and allow p53/TP53 activation (PubMed:21804542). It may also positively regulate the function of p53/TP53 in cell cycle arrest and apoptosis through direct interaction, preventing its MDM2-dependent ubiquitin-mediated proteasomal degradation. Originally identified as a tumor suppressor, it may also play a role in cell proliferation and apoptosis by positively regulating the stability of PTEN, thereby antagonizing the PI3K-AKT/PKB signaling pathway. May also inhibit cell proliferation and increase apoptosis through its interaction with NF2. May negatively regulate NPM1 by regulating its nucleoplasmic localization, oligomerization and ubiquitin-mediated proteasomal degradation. Thereby, may prevent NPM1 interaction with MYC and negatively regulate transcription mediated by the MYC-NPM1 complex. May also regulate cellular aerobic respiration. In the cellular response to viral infection, may play a role in the attenuation of interferon-beta through the inhibition of DDX58/RIG-1 (By similarity). {ECO:0000250|UniProtKB:Q9NZM5, ECO:0000269|PubMed:21804542}. PTM: Ubiquitin-mediated proteasomal degradation is regulated by c-JUN. It is associated with relocalization to the nucleoplasm and decreased homooligomerization. {ECO:0000250|UniProtKB:Q9NZM5}.; PTM: Phosphorylated upon DNA damage probably by ATM and DNA-PK; may regulate NOP53 degradation. {ECO:0000250|UniProtKB:Q9NZM5}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:21804542}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9NZM5}. Note=In the nucleolus may be more specifically localized to the fibrillar center. Mainly nucleolar it relocalizes to the nucleoplasm under specific conditions including ribosomal stress enabling it to interact and regulate nucleoplasmic proteins like p53/TP53. Also detected in the cytosol. {ECO:0000250|UniProtKB:Q9NZM5}. SUBUNIT: Homooligomer. Interacts with PTEN; regulates PTEN phosphorylation and increases its stability (By similarity). Interacts with RPL11; retains RPL11 into the nucleolus (PubMed:21804542). Interacts with CDKN2A/isoform tumor suppressor ARF; the interaction is direct and promotes ARF nucleoplasmic relocalization and ubiquitin-mediated proteasomal degradation. Interacts with NPM1; the interaction is direct and competitive with MYC. Interacts with NF2 (via FERM domain); the interaction is direct. Interacts with p53/TP53 (via the oligomerization region); the interaction is direct and may prevent the MDM2-mediated proteasomal degradation of p53/TP53. Interacts with DDX58; may regulate DDX58 through USP15-mediated 'Lys-63'-linked deubiquitination. Interacts with UBTF (By similarity). {ECO:0000250|UniProtKB:Q9NZM5, ECO:0000269|PubMed:21804542}. +Q571H0 NPA1P_MOUSE Nucleolar pre-ribosomal-associated protein 1 (URB1 ribosome biogenesis 1 homolog) 2274 254,614 Alternative sequence (2); Chain (1); Modified residue (2); Sequence conflict (1) SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. +Q91WC7 NPAL2_MOUSE NIPA-like protein 2 383 42,091 Chain (1); Glycosylation (2); Sequence conflict (4); Transmembrane (9) TRANSMEM 46 66 Helical. {ECO:0000255}.; TRANSMEM 88 108 Helical. {ECO:0000255}.; TRANSMEM 115 135 Helical. {ECO:0000255}.; TRANSMEM 144 164 Helical. {ECO:0000255}.; TRANSMEM 177 197 Helical. {ECO:0000255}.; TRANSMEM 208 228 Helical. {ECO:0000255}.; TRANSMEM 243 263 Helical. {ECO:0000255}.; TRANSMEM 278 298 Helical. {ECO:0000255}.; TRANSMEM 306 326 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q0VBU9 PLPP4_MOUSE Phospholipid phosphatase 4 (EC 3.1.3.4) (Phosphatidic acid phosphatase type 2 domain-containing protein 1A) 271 30,444 Chain (1); Region (3); Transmembrane (6) TRANSMEM 4 24 Helical. {ECO:0000255}.; TRANSMEM 49 69 Helical. {ECO:0000255}.; TRANSMEM 84 104 Helical. {ECO:0000255}.; TRANSMEM 142 162 Helical. {ECO:0000255}.; TRANSMEM 179 199 Helical. {ECO:0000255}.; TRANSMEM 202 222 Helical. {ECO:0000255}. FUNCTION: Displays magnesium-independent phosphatidate phosphatase activity in vitro. Catalyzes the conversion of phosphatidic acid to diacylglycerol (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q5TIS6 NOTO_MOUSE Homeobox protein notochord 240 26,322 Chain (1); DNA binding (1); Natural variant (1) FUNCTION: Transcription factor that controls node morphogenesis (PubMed:15231714, PubMed:17884984, PubMed:18061569, PubMed:22357932). Acts downstream of both FOXA2 and Brachyury (T) during notochord development (PubMed:15231714). Is essential for cilia formation in the posterior notochord (PNC) and for left-right patterning; acts upstream of FOXJ1 and RFX3 in this process and is required for the expression of various components important for axonemal assembly and function (PubMed:17884984). Plays a role in regulating axial versus paraxial cell fate (PubMed:18061569). Activates the transcription of ciliary proteins C11orf97 homolog, FAM183B and SPACA9 in the embryonic ventral node (PubMed:27914912). {ECO:0000269|PubMed:15231714, ECO:0000269|PubMed:17884984, ECO:0000269|PubMed:18061569, ECO:0000269|PubMed:22357932, ECO:0000269|PubMed:27914912}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. DISEASE: Note=Defects in Noto are the cause of the truncate (tc) phenotype. Truncate (tc) is a recessive mutation that affects the development of the caudal notochord. Mice homozygous for tc are viable but viability is reduced, which is attributed at least in part to spinal injury in the sacral and lower lumbar region. {ECO:0000269|PubMed:15231714}. +Q8BGD7 NPAS4_MOUSE Neuronal PAS domain-containing protein 4 (Neuronal PAS4) (HLH-PAS transcription factor NXF) (Limbic-enhanced PAS protein) (LE-PAS) 802 87,286 Chain (1); Coiled coil (2); Domain (4); Frameshift (1); Region (2) FUNCTION: Transcription factor expressed in neurons of the brain that regulates the excitatory-inhibitory balance within neural circuits and is required for contextual memory in the hyppocampus (PubMed:18815592, PubMed:22194569, PubMed:23029555, PubMed:24201284, PubMed:24855953). Plays a key role in the structural and functional plasticity of neurons (PubMed:23172225). Acts as an early-response transcription factor in both excitatory and inhibitory neurons, where it induces distinct but overlapping sets of late-response genes in these two types of neurons, allowing the synapses that form on inhibitory and excitatory neurons to be modified by neuronal activity in a manner specific to their function within a circuit, thereby facilitating appropriate circuit responses to sensory experience (PubMed:24201284, PubMed:24855953). In excitatory neurons, activates transcription of BDNF, which in turn controls the number of GABA-releasing synapses that form on excitatory neurons, thereby promoting an increased number of inhibitory synapses on excitatory neurons (PubMed:18815592, PubMed:22194569, PubMed:24201284). In inhibitory neurons, regulates a distinct set of target genes that serve to increase excitatory input onto somatostatin neurons, probably resulting in enhanced feedback inhibition within cortical circuits (PubMed:24855953). The excitatory and inhibitory balance in neurons affects a number of processes, such as short-term and long-term memory, acquisition of experience, fear memory, response to stress and social behavior (PubMed:18815592, PubMed:22194569, PubMed:23029555, PubMed:24201284, PubMed:27238022). Acts as a regulator of dendritic spine development in olfactory bulb granule cells in a sensory-experience-dependent manner by regulating expression of MDM2 (PubMed:25088421). Efficient DNA binding requires dimerization with another bHLH protein, such as ARNT, ARNT2 or BMAL1 (PubMed:14701734, PubMed:15363889, PubMed:19284974). Can activate the CME (CNS midline enhancer) element (PubMed:14701734, PubMed:15363889). {ECO:0000269|PubMed:14701734, ECO:0000269|PubMed:15363889, ECO:0000269|PubMed:18815592, ECO:0000269|PubMed:22194569, ECO:0000269|PubMed:23029555, ECO:0000269|PubMed:23172225, ECO:0000269|PubMed:24201284, ECO:0000269|PubMed:24855953, ECO:0000269|PubMed:25088421, ECO:0000269|PubMed:27238022}. PTM: Ubiquitinated, leading to degradation by the proteosome. {ECO:0000269|PubMed:26663079}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:15363889, ECO:0000269|PubMed:24201284}. SUBUNIT: Efficient DNA binding requires dimerization with another bHLH protein (PubMed:14701734, PubMed:15363889, PubMed:19284974). Heterodimer; forms a heterodimer with ARNT, ARNT2 or BMAL1 (PubMed:14701734, PubMed:15363889, PubMed:19284974). {ECO:0000269|PubMed:14701734, ECO:0000269|PubMed:15363889, ECO:0000269|PubMed:19284974, ECO:0000269|PubMed:27782878}. TISSUE SPECIFICITY: Mainly expressed in brain (PubMed:14701734, PubMed:15363889). Expressed in the limbic system and olfactory bulb (PubMed:15363889, PubMed:25088421). Specifically expressed in CA1 and CA3 region of the hippocampus after contextual learning (at protein level) (PubMed:22194569, PubMed:23029555). Also expressed in pancreatic beta cells (PubMed:26663079). {ECO:0000269|PubMed:14701734, ECO:0000269|PubMed:15363889, ECO:0000269|PubMed:22194569, ECO:0000269|PubMed:23029555, ECO:0000269|PubMed:25088421, ECO:0000269|PubMed:26663079}. +Q78ZA7 NP1L4_MOUSE Nucleosome assembly protein 1-like 4 375 42,679 Chain (1); Compositional bias (3); Initiator methionine (1); Modified residue (12); Motif (1) FUNCTION: Acts as histone chaperone in nucleosome assembly (PubMed:28366643). In condensing spermatids, mediates the loading of the heterodimer composed of histones H2AFB1 and HIST1H2BA/TH2B onto the nucleosomes, thereby promoting the replacement of histones to protamine in male germ cells (PubMed:28366643). {ECO:0000269|PubMed:28366643}. PTM: Polyglutamylated and polyglycylated. These 2 modifications occur exclusively on glutamate residues and result in either polyglutamate or polyglycine chains on the gamma-carboxyl group. Both modifications can coexist on the same protein on adjacent residues, and lowering polyglycylation levels increases polyglutamylation, and reciprocally. Polyglutamylated by TTLL4. {ECO:0000269|PubMed:17499049}.; PTM: Phosphorylated at the G0/G1 boundary but it is not phosphorylated in S-phase. Phosphorylated protein remains in the cytoplasm in a complex with histones during the G0/G1 transition, whereas dephosphorylation triggers its transport into the nucleus at the G1/S-boundary. {ECO:0000250|UniProtKB:Q99733}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q99733}. Cytoplasm {ECO:0000250|UniProtKB:Q99733}. Note=Present in the cytoplasm and excluded from the nucleus during G0/G1 phase, then relocates to the nucleus by the time cells are in S phase. Phosphorylated form localizes in the cytoplasm during the G0/G1 transition, whereas dephosphorylation leads to relocalization into the nucleus at the G1/S-boundary. {ECO:0000250|UniProtKB:Q99733}. SUBUNIT: Interacts with core (H2A, H2B, H3, H4) and linker (H1) histones. {ECO:0000250|UniProtKB:Q99733}. +Q9JJF0 NP1L5_MOUSE Nucleosome assembly protein 1-like 5 156 17,024 Chain (1); Coiled coil (1); Compositional bias (1) SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q8K4P1 NPB_MOUSE Neuropeptide B (Preproprotein L7) (mPPL7) [Cleaved into: Neuropeptide B-29 (NPB29) (L7C)] 119 13,018 Peptide (1); Propeptide (1); Signal peptide (1) FUNCTION: Has an effect in food intake, on locomotor activity and has an analgesic effect, (in vivo pharmacological studies). May be involved in the regulation of neuroendocrine system, memory and learning (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Detected in brain; more specifically in paraventricular hypothalamic nucleus, hippocampus and several nuclei in midbrain and brainstem. {ECO:0000269|PubMed:12719537}. +Q922V4 PLRG1_MOUSE Pleiotropic regulator 1 513 56,938 Chain (1); Modified residue (4); Repeat (7); Sequence conflict (1) FUNCTION: Involved in pre-mRNA splicing as component of the spliceosome. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. {ECO:0000250|UniProtKB:O43660}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O43660}. Nucleus speckle {ECO:0000250|UniProtKB:O43660}. SUBUNIT: Identified in the spliceosome C complex. Component of the PRP19-CDC5L splicing complex composed of a core complex comprising a homotetramer of PRPF19, CDC5L, PLRG1 and BCAS2, and at least three less stably associated proteins CTNNBL1, CWC15 and HSPA8. Interacts (via its WD40 repeat domain) directly with CDC5L (via its C-terminal); the interaction is required for mRNA splicing but not for spliceosome assembly. Also interacts directly in the complex with BCAS2 and PRPF19. {ECO:0000250|UniProtKB:O43660}. +P70313 NOS3_MOUSE Nitric oxide synthase, endothelial (EC 1.14.13.39) (Constitutive NOS) (cNOS) (EC-NOS) (Endothelial NOS) (eNOS) (NOS type III) (NOSIII) 1202 132,916 Chain (1); Compositional bias (1); Domain (2); Initiator methionine (1); Lipidation (3); Metal binding (3); Modified residue (8); Nucleotide binding (5); Region (2); Sequence conflict (2) FUNCTION: Produces nitric oxide (NO) which is implicated in vascular smooth muscle relaxation through a cGMP-mediated signal transduction pathway. NO mediates vascular endothelial growth factor (VEGF)-induced angiogenesis in coronary vessels and promotes blood clotting through the activation of platelets. May play a significant role in normal and abnormal limb development. {ECO:0000269|PubMed:9843834}. PTM: Phosphorylation by AMPK at Ser-1176 in the presence of Ca(2+)-calmodulin (CaM) activates activity. In absence of Ca(2+)-calmodulin, AMPK also phosphorylates Thr-494, resulting in inhibition of activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane, caveola {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Golgi apparatus {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Specifically associates with actin cytoskeleton in the G2 phase of the cell cycle, which is favored by interaction with NOSIP and results in a reduced enzymatic activity. {ECO:0000250}. SUBUNIT: Homodimer. Interacts with NOSIP and NOSTRIN (By similarity). Interacts with HSP90AB1 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P29474}. +Q9D3P8 PLRKT_MOUSE Plasminogen receptor (KT) (Plg-R(KT)) 147 17,261 Chain (1); Mutagenesis (1); Topological domain (3); Transmembrane (2) TRANSMEM 53 73 Helical. {ECO:0000255}.; TRANSMEM 79 99 Helical. {ECO:0000255}. TOPO_DOM 1 52 Extracellular. {ECO:0000255}.; TOPO_DOM 74 78 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 100 147 Extracellular. {ECO:0000255}. FUNCTION: Receptor for plasminogen. Regulates urokinase plasminogen activator-dependent and stimulates tissue-type plasminogen activator-dependent cell surface plasminogen activation. Proposed to be part of a local catecholaminergic cell plasminogen activation system that regulates neuroendocrine prohormone processing. Involved in regulation of inflammatory response; regulates monocyte chemotactic migration and matrix metallproteinase activation, such as of MMP2 and MMP9. {ECO:0000269|PubMed:19897580, ECO:0000269|PubMed:21795689, ECO:0000269|PubMed:21940822}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19897580, ECO:0000269|PubMed:21795689}; Multi-pass membrane protein {ECO:0000269|PubMed:19897580, ECO:0000269|PubMed:21795689}. Note=Colocalizes on the cell surface with urokinase plasminogen activator surface receptor/Plaur. SUBUNIT: Interacts with PLAT. Interacts with PLAUR (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in monocytes; detected in differentiated monocytes but not in progenitor cells. Expressed in adrenal medulla and hippocampus. {ECO:0000269|PubMed:21795689}. +P33610 PRI2_MOUSE DNA primase large subunit (EC 2.7.7.-) (DNA primase 58 kDa subunit) (p58) 505 58,408 Chain (1); Metal binding (4); Modified residue (1); Sequence conflict (1) FUNCTION: DNA primase is the polymerase that synthesizes small RNA primers for the Okazaki fragments made during discontinuous DNA replication. SUBUNIT: Heterodimer of a small subunit and a large subunit. +Q8CBD1 NRIP1_MOUSE Nuclear receptor-interacting protein 1 (Nuclear factor RIP140) (Receptor-interacting protein 140) 1161 126,337 Chain (1); Cross-link (14); Modified residue (22); Motif (12); Mutagenesis (5); Region (8); Sequence conflict (15) FUNCTION: Modulates transcriptional repression by nuclear hormone receptors such as NR2C1, thyroid hormone receptor and retinoic acid receptor/RARA. Essential for cumulus expansion and follicle rupture during ovulation. Also controls the balance between fat accumulation and energy expenditure. Positive regulator of the circadian clock gene expression: stimulates transcription of ARNTL/BMAL1, CLOCK and CRY1 by acting as a coactivator for RORA and RORC. {ECO:0000269|PubMed:10531331, ECO:0000269|PubMed:11100122, ECO:0000269|PubMed:15130509, ECO:0000269|PubMed:15155905, ECO:0000269|PubMed:15919748, ECO:0000269|PubMed:21628546, ECO:0000269|PubMed:9774688}. PTM: Acetylation abolishes interaction with CTBP1. Phosphorylation enhances interaction with YWHAH (By similarity). Acetylation regulates its nuclear translocation and corepressive activity. {ECO:0000250|UniProtKB:P48552, ECO:0000269|PubMed:15846843, ECO:0000269|PubMed:15879431}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15879431}. SUBUNIT: Interacts with CTBP1, CTBP2, ERS1, HDAC1, HDAC2, HDAC5, HDAC6, NR2C2, NR3C1, NR3C2, YWHAH, JUN and FOS. Found in a complex with both NR3C1 and YWHAH (By similarity). Interacts with NR2C1 (sumoylated form and via the ligand-binding domain); the interaction results in promoting the repressor activity of NR2C1. Interacts with RARA and RXRB homodimers and RARA/RXRB heterodimers in the presence of ligand. Interacts with HDAC1 and HDAC3 via its N-terminal domain. Interacts with ZNF366 (By similarity). Interacts with RORA. {ECO:0000250|UniProtKB:P48552, ECO:0000269|PubMed:21628546}. DOMAIN: Contains at least 4 autonomous repression domains (RD1-4). {ECO:0000250}.; DOMAIN: Contains 9 Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs, which have different affinities for nuclear receptors.; DOMAIN: The Ligand-dependent nuclear receptor binding region is required for ligand-dependent interaction with RAAR and RXRB homo- and heterodimers, for the corepressor activity, and for the formation of an HDAC3 complex with RARA/RXRB. TISSUE SPECIFICITY: Expressed in the embryonic placenta. In the adult, expression is strong in the testis and brain. Also expressed at a high level in the white adipose tissue. Expressed constantly but at a weaker level in the adult heart, lung, stomach and kidney. Expressed moderately in the skeletal muscle. Expressed at a low level in the adult spleen, liver and brown adipose tissue. Expressed in the ovary at a high level in granulosa cells and at a lower level in the thecal and interstitial compartments. {ECO:0000269|PubMed:11100122, ECO:0000269|PubMed:15155905, ECO:0000269|PubMed:9774688}. +Q9JHR9 NRIP2_MOUSE Nuclear receptor-interacting protein 2 (Neuronal-interacting factor X 1) 270 29,284 Alternative sequence (1); Chain (1); Frameshift (1); Motif (1); Region (1); Sequence conflict (6) FUNCTION: Down-regulates transcriptional activation by nuclear receptors, such as NR1F2. {ECO:0000269|PubMed:10860982}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10860982}. SUBUNIT: Interacts with NR1F2, RARA and THRB in a ligand-dependent manner. {ECO:0000269|PubMed:10860982}. TISSUE SPECIFICITY: Expression is restricted to the central nervous system (neurons in the dentate gyrus of the hippocampus, the amygdala, thalamic and hypothalamic regions). {ECO:0000269|PubMed:10860982}. +Q9CS84 NRX1A_MOUSE Neurexin-1 (Neurexin I-alpha) (Neurexin-1-alpha) 1514 166,169 Alternative sequence (6); Beta strand (14); Chain (1); Compositional bias (3); Disulfide bond (11); Domain (9); Erroneous initiation (1); Glycosylation (4); Helix (2); Metal binding (10); Sequence caution (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1439 1459 Helical. {ECO:0000255}. TOPO_DOM 31 1438 Extracellular. {ECO:0000255}.; TOPO_DOM 1460 1514 Cytoplasmic. {ECO:0000255}. FUNCTION: Cell surface protein involved in cell-cell-interactions, exocytosis of secretory granules and regulation of signal transmission. Function is isoform-specific. Alpha-type isoforms have a long N-terminus with six laminin G-like domains and play an important role in synaptic signal transmission. Alpha-type isoforms play a role in the regulation of calcium channel activity and Ca(2+)-triggered neurotransmitter release at synapses and at neuromuscular junctions. They play an important role in Ca(2+)-triggered exocytosis of secretory granules in pituitary gland. They may effect their functions at synapses and in endocrine cells via their interactions with proteins from the exocytotic machinery. Likewise, alpha-type isoforms play a role in regulating the activity of postsynaptic NMDA receptors, a subtype of glutamate-gated ion channels. Both alpha-type and beta-type isoforms may play a role in the formation or maintenance of synaptic junctions via their interactions (via the extracellular domains) with neuroligin family members, CBLN1 or CBLN2. In vitro, triggers the de novo formation of presynaptic structures. May be involved in specification of excitatory synapses. Alpha-type isoforms were first identified as receptors for alpha-latrotoxin from spider venom. {ECO:0000269|PubMed:12827191, ECO:0000269|PubMed:14983056, ECO:0000269|PubMed:16406382, ECO:0000269|PubMed:17035546, ECO:0000269|PubMed:21410790, ECO:0000269|PubMed:9430716}. PTM: N-glycosylated. {ECO:0000250}.; PTM: O-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21410790}; Single-pass type I membrane protein {ECO:0000269|PubMed:21410790}. Cell junction, synapse {ECO:0000269|PubMed:21410790}. Note=Localized on the pre-synaptic membrane. {ECO:0000250}. SUBUNIT: The cytoplasmic C-terminal region binds to CASK, CASKIN1 and APBA1. Interacts (via laminin G-like domain 2) with NXPH1 and NXPH3 (By similarity). Alpha-type isoforms (neurexin-1-alpha) interact (via laminin G-like domain 2 and/or laminin G-like domain 6) with DAG1 (via alpha-dystroglycan chain). Alpha-type isoforms interact with alpha-latrotoxin from spider venom. Interacts with LRRTM1, LRRTM2, LRRTM3 and LRRTM4 (By similarity). Interacts (via laminin G-like domain 2 and/or laminin G-like domain 6) with NLGN1 forming a heterotetramer, where one NLGN1 dimer interacts with one NRXN1 dimer. Interacts (via laminin G-like domain 2 and/or laminin G-like domain 6) with NLGN1, NLGN2, NLGN3 and NLGN4L; these interactions are calcium-dependent. Interacts with SYT13 and SYTL1. Interacts with CBLN1, CBLN2 and, less avidly, with CBLN4. {ECO:0000250, ECO:0000269|PubMed:11171101, ECO:0000269|PubMed:11243866, ECO:0000269|PubMed:18334216, ECO:0000269|PubMed:18434543, ECO:0000269|PubMed:20624592, ECO:0000269|PubMed:21410790}. +Q9D720 NSE1_MOUSE Non-structural maintenance of chromosomes element 1 homolog (Non-SMC element 1 homolog) (EC 2.3.2.27) 266 30,708 Chain (1); Erroneous initiation (4); Region (1); Sequence conflict (1); Zinc finger (1) FUNCTION: RING-type zinc finger-containing E3 ubiquitin ligase that assembles with melanoma antigen protein (MAGE) to catalyze the direct transfer of ubiquitin from E2 ubiquitin-conjugating enzyme to a specific substrate. Within MAGE-RING ubiquitin ligase complex, MAGE stimulates and specifies ubiquitin ligase activity likely through recruitment and/or stabilization of the E2 ubiquitin-conjugating enzyme at the E3:substrate complex. Involved in maintenance of genome integrity, DNA damage response and DNA repair. NSMCE3/MAGEG1 and NSMCE1 ubiquitin ligase are components of SMC5-SMC6 complex and may positively regulate homologous recombination-mediated DNA repair. {ECO:0000250|UniProtKB:Q8WV22}. PTM: Ubiquitinated. {ECO:0000250|UniProtKB:Q8WV22}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8WV22}. Chromosome, telomere {ECO:0000250|UniProtKB:Q8WV22}. SUBUNIT: Component of the SMC5-SMC6 complex which consists at least of SMC5, SMC6, NSMCE2, NSMCE1, NSMCE4A or EID3 and NSMCE3. NSMCE1, NSMCE4A or EID3 and NSMCE3 probably form a subcomplex that bridges the head domains of the SMC5-SMC6 heterodimer. Interacts with NSMCE3. {ECO:0000250|UniProtKB:Q8WV22}. +Q6P2L6 NSD3_MOUSE Histone-lysine N-methyltransferase NSD3 (EC 2.1.1.43) (Nuclear SET domain-containing protein 3) (Wolf-Hirschhorn syndrome candidate 1-like protein 1 homolog) (WHSC1-like protein 1) 1439 161,002 Alternative sequence (8); Chain (1); Coiled coil (1); Cross-link (7); Domain (5); Modified residue (7); Sequence conflict (3); Zinc finger (4) FUNCTION: Histone methyltransferase. Preferentially methylates 'Lys-4' and 'Lys-27' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation, while 'Lys-27' is a mark for transcriptional repression (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}. SUBUNIT: Interacts with BRD4. {ECO:0000250}. +P46460 NSF_MOUSE Vesicle-fusing ATPase (EC 3.6.4.6) (N-ethylmaleimide-sensitive fusion protein) (NEM-sensitive fusion protein) (Suppressor of K(+) transport growth defect 2) (Protein SKD2) (Vesicular-fusion protein NSF) 744 82,613 Chain (1); Erroneous gene model prediction (2); Metal binding (1); Modified residue (4); Mutagenesis (2); Nucleotide binding (2); Sequence conflict (5) FUNCTION: Required for vesicle-mediated transport. Catalyzes the fusion of transport vesicles within the Golgi cisternae. Is also required for transport from the endoplasmic reticulum to the Golgi stack. Seems to function as a fusion protein required for the delivery of cargo proteins to all compartments of the Golgi stack GRIA2 leads to influence GRIA2 membrane cycling (By similarity). {ECO:0000250, ECO:0000269|PubMed:16461345}. PTM: Phosphorylation at Ser-569 interferes with homohexamerization. {ECO:0000269|PubMed:16461345}. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Homohexamer. Interacts with GABARAP and GABARAPL2. Interacts with GRIA2. Interacts with PLK2, leading to disrupt the interaction with GRIA2. Interacts with MUSK; may regulate MUSK endocytosis and activity (By similarity). Interacts with CDK16. {ECO:0000250, ECO:0000269|PubMed:16461345, ECO:0000269|PubMed:18272689}. +Q9CQ48 NUDC2_MOUSE NudC domain-containing protein 2 157 17,660 Beta strand (9); Chain (1); Domain (1); Helix (4); Initiator methionine (1); Modified residue (3); Sequence conflict (4) FUNCTION: May regulate the LIS1/dynein pathway by stabilizing LIS1 with Hsp90 chaperone. {ECO:0000250}. SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. Note=Associates with centrosomes in interphase and to spindle poles and kinetochores during mitosis. {ECO:0000250}. SUBUNIT: Interacts with LIS1. {ECO:0000250}. +P81117 NUCB2_MOUSE Nucleobindin-2 (DNA-binding protein NEFA) (Prepronesfatin) [Cleaved into: Nesfatin-1] 420 50,304 Calcium binding (2); Chain (2); Compositional bias (1); DNA binding (1); Domain (2); Modified residue (1); Region (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Calcium-binding protein. May have a role in calcium homeostasis. {ECO:0000269|PubMed:10915798}.; FUNCTION: Nesfatin-1: Anorexigenic peptide, seems to play an important role in hypothalamic pathways regulating food intake and energy homeostasis, acting in a leptin-independent manner. May also exert hypertensive roles and modulate blood pressure through directly acting on peripheral arterial resistance (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10915798}. Perikaryon {ECO:0000269|PubMed:10915798}. Endoplasmic reticulum {ECO:0000269|PubMed:10915798}. Golgi apparatus {ECO:0000250}. Nucleus envelope {ECO:0000269|PubMed:10915798}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Secreted {ECO:0000269|PubMed:10915798}. Note=In dendrites and perikarya of brain neurons. Abundant in the ER cisternae and nuclear envelope, but not detected in Golgi, mitochondria or nucleoplasm in neurons. In cell culture, cytoplasmic and secreted.; SUBCELLULAR LOCATION: Nesfatin-1: Secreted {ECO:0000250}. SUBUNIT: Binds to the postmitotic growth suppressor necdin; co-expression abolishes Nucb2 secretion. {ECO:0000269|PubMed:10915798}. TISSUE SPECIFICITY: Found in liver, heart, thymus, muscle, intestine, kidney, lung, spleen and throughout the brain, in cerebral cortex, hippocampus, hypothalamus and medulla oblongata. Nucb2 and necdin levels were higher in postmitotic neurons. {ECO:0000269|PubMed:10915798}. +Q925Q3 NCLX_MOUSE Mitochondrial sodium/calcium exchanger protein (Na(+)/K(+)/Ca(2+)-exchange protein 6) (Sodium/calcium exchanger protein, mitochondrial) (Sodium/potassium/calcium exchanger 6) (Solute carrier family 24 member 6) (Solute carrier family 8 member B1) 585 64,365 Alternative sequence (2); Chain (1); Glycosylation (1); Modified residue (1); Sequence conflict (6); Topological domain (14); Transit peptide (1); Transmembrane (13) TRANSMEM 96 116 Helical; Name=1. {ECO:0000255}.; TRANSMEM 141 161 Helical; Name=2. {ECO:0000255}.; TRANSMEM 169 189 Helical; Name=3. {ECO:0000255}.; TRANSMEM 206 226 Helical; Name=4. {ECO:0000255}.; TRANSMEM 230 250 Helical; Name=5. {ECO:0000255}.; TRANSMEM 326 346 Helical; Name=6. {ECO:0000255}.; TRANSMEM 361 381 Helical; Name=7. {ECO:0000255}.; TRANSMEM 384 404 Helical; Name=8. {ECO:0000255}.; TRANSMEM 417 437 Helical; Name=9. {ECO:0000255}.; TRANSMEM 446 466 Helical; Name=10. {ECO:0000255}.; TRANSMEM 492 512 Helical; Name=11. {ECO:0000255}.; TRANSMEM 526 546 Helical; Name=12. {ECO:0000255}.; TRANSMEM 560 580 Helical; Name=13. {ECO:0000255}. TOPO_DOM 27 95 Extracellular. {ECO:0000255}.; TOPO_DOM 117 140 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 162 168 Extracellular. {ECO:0000255}.; TOPO_DOM 190 205 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 227 229 Extracellular. {ECO:0000255}.; TOPO_DOM 251 325 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 347 360 Extracellular. {ECO:0000255}.; TOPO_DOM 382 383 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 405 416 Extracellular. {ECO:0000255}.; TOPO_DOM 438 445 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 467 491 Extracellular. {ECO:0000255}.; TOPO_DOM 513 525 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 547 559 Extracellular. {ECO:0000255}.; TOPO_DOM 581 585 Cytoplasmic. {ECO:0000255}. FUNCTION: Mitochondrial sodium/calcium antiporter that mediates sodium-dependent calcium efflux from mitochondrion, by mediating the exchange of 3 sodium ions per 1 calcium ion (PubMed:20018762, PubMed:28445457). Plays a central role in mitochondrial calcium homeostasis by mediating mitochondrial calcium extrusion: calcium efflux is essential for mitochondrial function and cell survival, notably in cardiomyocytes (PubMed:24067497, PubMed:28445457). Regulates rates of glucose-dependent insulin secretion in pancreatic beta-cells during the first phase of insulin secretion: acts by mediating efflux of calcium from mitochondrion, thereby affecting cytoplasmic calcium responses (By similarity). Required for store-operated Ca(2+) entry (SOCE) and Ca(2+) release-activated Ca(2+) (CRAC) channel regulation: sodium transport by SLC8B1 leads to promote calcium-shuttling that modulates mitochondrial redox status, thereby regulating SOCE activity (By similarity). Involved in B-lymphocyte chemotaxis (PubMed:27328625). Able to transport Ca(2+) in exchange of either Li(+) or Na(+), explaining how Li(+) catalyzes Ca(2+) exchange (By similarity). In contrast to other members of the family its function is independent of K(+) (By similarity). {ECO:0000250|UniProtKB:Q6J4K2, ECO:0000269|PubMed:20018762, ECO:0000269|PubMed:24067497, ECO:0000269|PubMed:27328625, ECO:0000269|PubMed:28445457}. PTM: Phosphorylation at Ser-258 by PKA prevents calcium overload. {ECO:0000250|UniProtKB:Q6J4K2}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:20018762, ECO:0000269|PubMed:24067497}; Multi-pass membrane protein {ECO:0000269|PubMed:20018762}. Note=Mainly localizes to mitochondrion inner membrane (PubMed:20018762).; SUBCELLULAR LOCATION: Isoform 2: Cell membrane {ECO:0000269|PubMed:14625281}; Multi-pass membrane protein {ECO:0000269|PubMed:14625281}. TISSUE SPECIFICITY: Ubiquitously expressed. Expressed in dental tissues. {ECO:0000269|PubMed:14625281, ECO:0000269|PubMed:22677781}. +Q8C567 NCTR1_MOUSE Natural cytotoxicity triggering receptor 1 (Activating receptor 1) (mAR-1) (Lymphocyte antigen 94) (Natural killer cell p46-related protein) (NK-p46) (NKp46) (mNKp46) (CD antigen CD335) 325 37,266 Chain (1); Disulfide bond (2); Domain (2); Glycosylation (3); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 256 273 Helical. {ECO:0000255}. TOPO_DOM 17 255 Extracellular. {ECO:0000255}.; TOPO_DOM 274 325 Cytoplasmic. {ECO:0000255}. FUNCTION: Cytotoxicity-activating receptor that may contribute to the increased efficiency of activated natural killer (NK) cells to mediate tumor cell lysis. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Interacts with CD3Z and FCER1G. {ECO:0000250}. TISSUE SPECIFICITY: Selectively expressed by NK cells. {ECO:0000269|PubMed:10092106}. +Q8K224 NAT10_MOUSE RNA cytidine acetyltransferase (EC 2.3.1.-) (18S rRNA cytosine acetyltransferase) (N-acetyltransferase 10) 1024 115,419 Binding site (2); Chain (1); Compositional bias (2); Domain (1); Modified residue (5); Nucleotide binding (1); Region (3); Sequence conflict (5) FUNCTION: RNA cytidine acetyltransferase with specificity toward both 18S rRNA and tRNAs. Catalyzes the formation of N(4)-acetylcytidine (ac4C) in 18S rRNA. Required for early nucleolar cleavages of precursor rRNA at sites A0, A1 and A2 during 18S rRNA synthesis. Catalyzes the formation of ac4C in serine and leucine tRNAs. Requires the tRNA-binding adapter protein THUMBD1 for full tRNA acetyltransferase activity but not for 18S rRNA acetylation (Probable). Can acetylate both histones and microtubules. Histone acetylation may regulate transcription and mitotic chromosome de-condensation. Activates telomerase activity by stimulating the transcription of TERT, and may also regulate telomerase function by affecting the balance of telomerase subunit assembly, disassembly, and localization. Acetylates alpha-tubulin, which may affect microtubule stability and cell division (By similarity). {ECO:0000250|UniProtKB:Q9H0A0, ECO:0000255|HAMAP-Rule:MF_03211}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000255|HAMAP-Rule:MF_03211}. SUBUNIT: Interacts with THUMBD1 (Probable). Interacts with SUN1 (via N-terminus). Also interacts with TERT (By similarity). {ECO:0000250|UniProtKB:Q9H0A0, ECO:0000255|HAMAP-Rule:MF_03211}. +Q9EPN1 NBEA_MOUSE Neurobeachin (Lysosomal-trafficking regulator 2) 2936 326,743 Alternative sequence (3); Chain (1); Domain (2); Modified residue (7); Repeat (5); Sequence conflict (12) FUNCTION: Binds to type II regulatory subunits of protein kinase A and anchors/targets them to the membrane. May anchor the kinase to cytoskeletal and/or organelle-associated proteins. May have a role in membrane trafficking. {ECO:0000269|PubMed:11102458, ECO:0000303|PubMed:11102458}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11102458}; Peripheral membrane protein {ECO:0000269|PubMed:11102458}. Endomembrane system {ECO:0000269|PubMed:11102458}; Peripheral membrane protein {ECO:0000269|PubMed:11102458}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000269|PubMed:11102458}; Peripheral membrane protein {ECO:0000269|PubMed:11102458}. Note=Associated with pleomorphic tubulovesicular endomembranes near the trans sides of Golgi stacks and throughout the cell bodies and cell processes. Concentrated at the postsynaptic plasma membrane of a subpopulation of synapses. SUBUNIT: Interacts with RII subunit of PKA. {ECO:0000269|PubMed:11102458}. DOMAIN: RII-alpha binding site, predicted to form an amphipathic helix, could participate in protein-protein interactions with a complementary surface on the R-subunit dimer. {ECO:0000303|PubMed:11102458}. TISSUE SPECIFICITY: Forebrain, brainstem and cerebellum. {ECO:0000269|PubMed:11102458}. +Q9DB73 NB5R1_MOUSE NADH-cytochrome b5 reductase 1 (b5R.1) (EC 1.6.2.2) (NAD(P)H:quinone oxidoreductase type 3 polypeptide A2) 305 34,135 Alternative sequence (2); Chain (1); Domain (1); Nucleotide binding (2); Transmembrane (1) TRANSMEM 8 28 Helical. {ECO:0000255}. FUNCTION: NADH-cytochrome b5 reductases are involved in desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q6GQX2 NCK5L_MOUSE Nck-associated protein 5-like (Centrosomal protein of 169 kDa) (Cep169) 1323 138,170 Chain (1); Coiled coil (2); Compositional bias (3); Modified residue (11); Motif (3); Region (2); Sequence conflict (2) FUNCTION: Regulates microtubule organization and stabilization. Promotes microtubule growth and bundling formation and stabilizes microtubules by increasing intense acetylation of microtubules. Both tubulin-binding and homodimer formation are required for NCKAP5L-mediated microtubule bundle formation. {ECO:0000250|UniProtKB:Q9HCH0}. PTM: CDK1/Cyclin B-dependent phosphorylation mediates its dissociation from centrosomes during mitosis. {ECO:0000250|UniProtKB:Q9HCH0}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9HCH0}. Note=Localizes to microtubule plus ends. Associates with centrosomes during interphase, but dissociates from these structures from the onset of mitosis. {ECO:0000250|UniProtKB:Q9HCH0}. SUBUNIT: Homodimer. Interacts with CDK5RAP2. Interacts with MAPRE1. Interacts with beta-tubulin. {ECO:0000250|UniProtKB:Q9HCH0}. +Q9CQJ2 PIHD1_MOUSE PIH1 domain-containing protein 1 (Nucleolar protein 17 homolog) 290 32,209 Beta strand (5); Chain (1); Helix (5); Modified residue (3); Mutagenesis (3); Sequence conflict (1); Site (3) FUNCTION: Involved in the assembly of C/D box small nucleolar ribonucleoprotein (snoRNP) particles. Recruits the SWI/SNF complex to the core promoter of rRNA genes and enhances pre-rRNA transcription. Mediates interaction of TELO2 with the R2TP complex which is necessary for the stability of MTOR and SMG1. Positively regulates the assembly and activity of the mTORC1 complex. {ECO:0000250|UniProtKB:Q9NWS0}. SUBUNIT: Component of the R2TP complex composed at least of PIHD1, RUVBL1, RUVBL2 and RPAP3. Interacts with phosphorylated TELO2 (PubMed:24794838). Mediates interaction of TELO2 with the R2TP complex. Interacts with phosphorylated ECD, EFTUD2/SNRP116, RPB1 and UBR5 and with RPB1 in a phosphorylation-independent manner. Interacts with the core C/D box snoRNP particle components NOP58 and FBL and with RUVBL1/TIP49. Interacts with RPAP3 and WDR92. Interacts with histone H4 and with SWI/SNF complex member SMARCB1/SNF5. Interacts with the mTORC1 complex member RPTOR (By similarity). {ECO:0000250|UniProtKB:Q9NWS0, ECO:0000269|PubMed:24794838}. DOMAIN: The N-terminal region is required for binding to phosphorylated substrates while the C-terminal region binds to the other R2TP complex components. {ECO:0000250|UniProtKB:Q9NWS0}. +Q9CZX5 PINX1_MOUSE PIN2/TERF1-interacting telomerase inhibitor 1 (67-11-3 protein) (LPTS1) (Liver-related putative tumor suppressor) (Pin2-interacting protein X1) (TRF1-interacting protein 1) 332 37,221 Chain (1); Domain (1); Modified residue (4); Motif (1); Region (1); Sequence conflict (2) FUNCTION: Microtubule-binding protein essential for faithful chromosome segregation. Mediates TRF1 and TERT accumulation in nucleolus and enhances TRF1 binding to telomeres. Inhibits telomerase activity. May inhibit cell proliferation and act as tumor suppressor (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Chromosome, telomere {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Note=Localizes in nucleoli, at telomere speckles and to the outer plate of kinetochores. Localization to the kinetochore is mediated by its central region and depends on NDC80 and CENPE (By similarity). {ECO:0000250}. SUBUNIT: Interacts with MCRS1, TERT, TERF1, NCL/nucleolin, and the telomerase RNA. {ECO:0000250}. DOMAIN: The TID (telomerase inhibiting domain) domain is sufficient to bind TERT and inhibits its activity. {ECO:0000250}.; DOMAIN: The TBM domain mediates interaction with TERF1. {ECO:0000250}. +Q2VWQ2 NELL1_MOUSE Protein kinase C-binding protein NELL1 (NEL-like protein 1) 810 89,415 Chain (1); Disulfide bond (18); Domain (9); Glycosylation (10); Signal peptide (1) FUNCTION: Plays a role in the control of cell growth and differentiation. Promotes osteoblast cell differentiation and terminal mineralization. {ECO:0000269|PubMed:16537572}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus envelope {ECO:0000250}. Secreted {ECO:0000250}. Note=Colocalizes with ATRAID on the nuclear envelope and the perinuclear region. {ECO:0000250}. SUBUNIT: Homotrimer. Binds to PKC beta-1. Interacts with ATRAID; the interaction promotes osteoblast cell differentiation and mineralization (By similarity). {ECO:0000250}. +Q6R2P8 NEIL2_MOUSE Endonuclease 8-like 2 (EC 3.2.2.-) (EC 4.2.99.18) (DNA glycosylase/AP lyase Neil2) (DNA-(apurinic or apyrimidinic site) lyase Neil2) (Endonuclease VIII-like 2) (Nei homolog 2) (NEH2) (Nei-like protein 2) 329 36,834 Active site (4); Binding site (1); Chain (1); Initiator methionine (1); Modified residue (3); Sequence conflict (3); Zinc finger (1) FUNCTION: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Has DNA glycosylase activity towards 5-hydroxyuracil and other oxidized derivatives of cytosine with a preference for mismatched double-stranded DNA (DNA bubbles). Has low or no DNA glycosylase activity towards thymine glycol, 2-hydroxyadenine, hypoxanthine and 8-oxoguanine. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Binds EP300. {ECO:0000250}. DOMAIN: The zinc-finger domain is important for DNA binding. +Q3UGM2 NEK10_MOUSE Serine/threonine-protein kinase Nek10 (EC 2.7.11.1) (Never in mitosis A-related kinase 10) (NimA-related protein kinase 10) 1111 126,058 Active site (1); Alternative sequence (2); Binding site (1); Chain (1); Coiled coil (1); Domain (1); Nucleotide binding (1) +Q8BG30 NELFA_MOUSE Negative elongation factor A (NELF-A) (Wolf-Hirschhorn syndrome candidate 2 homolog) (mWHSC2) 530 57,585 Chain (1); Domain (1); Erroneous initiation (1); Modified residue (5); Region (2); Sequence conflict (10) FUNCTION: Essential component of the NELF complex, a complex that negatively regulates the elongation of transcription by RNA polymerase II (By similarity). The NELF complex, which acts via an association with the DSIF complex and causes transcriptional pausing, is counteracted by the P-TEFb kinase complex (By similarity). {ECO:0000250|UniProtKB:Q9H3P2}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H3P2}. SUBUNIT: The NELF complex is composed of NELFA, NELFB, NELFCD and NELFE; NELFA and NELFCD form a stable subcomplex that binds to the N-terminus of NELFB (By similarity). In vitro, the NELFA:NELFCD subcomplex binds to ssDNA and ssRNA in a sequence- and structure-dependent manner (By similarity). Interacts with the RNA polymerase II complex when it is not phosphorylated by P-TEFb (By similarity). Interacts with NELFB (PubMed:26010750). {ECO:0000250|UniProtKB:Q9H3P2, ECO:0000269|PubMed:26010750}. DOMAIN: The HDAg-like domain is essential for transcriptional repression, and mediates the interaction with the RNA polymerase II complex. {ECO:0000250|UniProtKB:Q9H3P2}. TISSUE SPECIFICITY: Ubiquitous. Expressed in brain, heart, spleen, lung, liver, muscle, kidney and testis. Already expressed in 7 dpc embryos. {ECO:0000269|PubMed:10409432}. +Q8K045 PKN3_MOUSE Serine/threonine-protein kinase N3 (EC 2.7.11.13) (Protein kinase PKN-beta) (Protein-kinase C-related kinase 3) 878 97,881 Active site (1); Binding site (1); Chain (1); Compositional bias (1); Domain (5); Modified residue (4); Nucleotide binding (1) FUNCTION: Contributes to invasiveness in malignant prostate cancer. {ECO:0000269|PubMed:15282551}. PTM: Autophosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Nuclear and perinuclear Golgi region. {ECO:0000250}. DOMAIN: The C1 domain does not bind the diacylglycerol (DAG). +Q99KK2 NEUA_MOUSE N-acylneuraminate cytidylyltransferase (EC 2.7.7.43) (CMP-N-acetylneuraminic acid synthase) (CMP-NeuNAc synthase) 432 48,058 Active site (1); Alternative sequence (1); Beta strand (16); Binding site (6); Chain (1); Helix (18); Modified residue (3); Motif (3); Mutagenesis (8); Sequence conflict (2); Turn (3) Amino-sugar metabolism; N-acetylneuraminate metabolism. FUNCTION: Catalyzes the activation of N-acetylneuraminic acid (NeuNAc) to cytidine 5'-monophosphate N-acetylneuraminic acid (CMP-NeuNAc), a substrate required for the addition of sialic acid. Has some activity toward NeuNAc, N-glycolylneuraminic acid (Neu5Gc) or 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN). {ECO:0000269|PubMed:9689047}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11893746, ECO:0000269|PubMed:9689047}. SUBUNIT: Homotetramer; the active enzyme is formed by a dimer of dimers. {ECO:0000269|PubMed:14636592}. DOMAIN: The BC2 (basic cluster 2) motif is necessary and sufficient for the nuclear localization and contains the catalytic active site. The localization in the nucleus is however not required for the enzyme activity. TISSUE SPECIFICITY: Highly expressed in brain and heart, and at intermediate level muscle and liver. {ECO:0000269|PubMed:9689047}. +Q8R0W6 NFIP1_MOUSE NEDD4 family-interacting protein 1 (NEDD4 WW domain-binding protein 5) 221 24,914 Chain (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (1); Motif (3); Mutagenesis (2); Region (2); Topological domain (4); Transmembrane (3) TRANSMEM 117 137 Helical. {ECO:0000255}.; TRANSMEM 144 164 Helical. {ECO:0000255}.; TRANSMEM 173 193 Helical. {ECO:0000255}. TOPO_DOM 2 116 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 138 143 Extracellular. {ECO:0000255}.; TOPO_DOM 165 172 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 194 221 Extracellular. {ECO:0000255}. FUNCTION: Activates HECT domain-containing E3 ubiquitin-protein ligases, including NEDD4 and ITCH, and consequently modulates the stability of their targets. As a result, controls many cellular processes. Prevents chronic T-helper cell-mediated inflammation by activating ITCH and thus controlling JUNB degradation (PubMed:11748237, PubMed:17137798, PubMed:20962770). Promotes pancreatic beta cell death through degradation of JUNB and inhibition of the unfolded protein response, leading to reduction of insulin secretion (PubMed:26319551). Restricts the production of proinflammatory cytokines in effector Th17 T-cells by promoting ITCH-mediated ubiquitination and degradation of RORC (PubMed:28051111). Together with NDFIP2, limits the cytokine signaling and expansion of effector Th2 T-cells by promoting degradation of JAK1, probably by ITCH- and NEDD4L-mediated ubiquitination (PubMed:27088444). Regulates peripheral T-cell tolerance to self and foreign antigens, forcing the exit of naive CD4+ T-cells from the cell cycle before they become effector T-cells (PubMed:24520172, PubMed:28051111). Negatively regulates RLR-mediated antiviral response by promoting SMURF1-mediated ubiquitination and subsequent degradation of MAVS (By similarity). Negatively regulates KCNH2 potassium channel activity by decreasing its cell-surface expression and interfering with channel maturation through recruitment of NEDD4L to the Golgi apparatus where it mediates KCNH2 degradation (By similarity). In cortical neurons, mediates the ubiquitination of the divalent metal transporter SLC11A2/DMT1 by NEDD4L, leading to its down-regulation and protection of the cells from cobalt and iron toxicity (By similarity). Important for normal development of dendrites and dendritic spines in cortex (PubMed:23897647). Enhances the ubiquitination of BRAT1 mediated by: NEDD4, NEDD4L and ITCH and is required for the nuclear localization of ubiquitinated BRAT1 (PubMed:25631046). Enhances the ITCH-mediated ubiquitination of MAP3K7 by recruiting E2 ubiquitin-conjugating enzyme UBE2L3 to ITCH (PubMed:25632008). Modulates EGFR signaling through multiple pathways. In particular, may regulate the ratio of AKT1-to-MAPK8 signaling in response to EGF, acting on AKT1 probably through PTEN destabilization and on MAPK8 through ITCH-dependent MAP2K4 inactivation. As a result, may control cell growth rate (By similarity). Inhibits cell proliferation by promoting PTEN nuclear localization and changing its signaling specificity (PubMed:25801959). {ECO:0000250|UniProtKB:Q9BT67, ECO:0000269|PubMed:11748237, ECO:0000269|PubMed:17137798, ECO:0000269|PubMed:20962770, ECO:0000269|PubMed:23897647, ECO:0000269|PubMed:24520172, ECO:0000269|PubMed:25631046, ECO:0000269|PubMed:25632008, ECO:0000269|PubMed:25801959, ECO:0000269|PubMed:26319551, ECO:0000269|PubMed:27088444, ECO:0000269|PubMed:28051111}. PTM: Ubiquitinated by NEDD4; mono-, di- and polyubiquitinated forms are detected. Ubiquitination regulates its degradation. {ECO:0000269|PubMed:11748237}.; PTM: Undergoes transient tyrosine phosphorylation following EGF stimulation, most probably by catalyzed by SRC. Phosphorylation SRC is enhanced in the presence of NDFIP2 which may act as a scaffold to recruit SRC to NDFIP1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250|UniProtKB:Q9BT67}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9BT67}. Golgi apparatus membrane {ECO:0000269|PubMed:11748237, ECO:0000269|PubMed:16822981, ECO:0000269|PubMed:18819914}. Cell junction, synapse, synaptosome {ECO:0000269|PubMed:23897647}. Cell projection, dendrite {ECO:0000269|PubMed:23897647}. Secreted {ECO:0000250|UniProtKB:Q9BT67}. Note=Detected in exosomes and secreted via the exosomal pathway. {ECO:0000250|UniProtKB:Q9BT67}. SUBUNIT: Forms heterodimers with NDFIP2 (By similarity). Interacts with several E3 ubiquitin-protein ligases, including ITCH, NEDD4, NEDD4L and WWP2 (PubMed:11042109, PubMed:11748237, PubMed:17137798, PubMed:25632008). The interaction with NEDD4, NEDD4L and ITCH leads to relocalization of these proteins to exosomes and eventually to exosomal secretion (PubMed:11748237). Interacts with U2SURP (PubMed:11748237). Interacts with SLC11A2/DMT1 (By similarity). Interacts with PTEN (By similarity). May interact with phosphorylated EGFR (By similarity). Interacts with BRAT1 (By similarity). Interacts with KCNH2 (By similarity). Interacts with MAVS (By similarity). Part of a complex containing ITCH, NDFIP1 and MAP3K7 (PubMed:25632008). Interacts (via N-terminus) with UBE2L3; the interaction mediates recruitment of UBE2L3 to ITCH (PubMed:25632008). {ECO:0000250|UniProtKB:Q9BT67, ECO:0000269|PubMed:11042109, ECO:0000269|PubMed:11748237, ECO:0000269|PubMed:17137798, ECO:0000269|PubMed:25632008}. DOMAIN: The PPxY motifs are required for E3 ubiquitin-protein ligase binding and activation and for ubiquitination. {ECO:0000269|PubMed:11042109, ECO:0000269|PubMed:11748237}. TISSUE SPECIFICITY: Highly expressed in embryonic and early postnatal cortex (at protein level) (PubMed:23897647). Widely expressed (PubMed:11748237). Hardly detectable in resting T-cells; up-regulated in T-cells in response to activation (PubMed:17137798). {ECO:0000269|PubMed:11748237, ECO:0000269|PubMed:17137798, ECO:0000269|PubMed:23897647}. +Q9R1A3 NET3_MOUSE Netrin-3 (Netrin-2-like protein) 580 62,023 Chain (1); Disulfide bond (15); Domain (5); Glycosylation (2); Motif (1); Sequence conflict (4); Signal peptide (1) FUNCTION: Netrins control guidance of CNS commissural axons and peripheral motor axons. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:11231084}. TISSUE SPECIFICITY: Very low levels at E10.5 to E12.5 in dorsal root ganglia. High levels in motor neurons at E13.5, E14.5 and E15.5. At E11.5 also expressed in the developing limb buds. {ECO:0000269|PubMed:10381568, ECO:0000269|PubMed:11231084}. +Q8BJW5 NOL11_MOUSE Nucleolar protein 11 723 80,818 Alternative sequence (1); Chain (1); Modified residue (1); Sequence conflict (7) FUNCTION: Ribosome biogenesis factor. May be required for both optimal rDNA transcription and small subunit (SSU) pre-rRNA processing at sites A', A0, 1 and 2b (By similarity). {ECO:0000250|UniProtKB:Q9H8H0}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9H8H0}. SUBUNIT: Interacts with UTP4. Interacts with FBL/fibrillarin in a transcription-dependent manner. May associate with the proposed t-UTP subcomplex of the SSU processome containing at least UTP4, WDR43, HEATR1, UTP15, WDR75. {ECO:0000250|UniProtKB:Q9H8H0}. +Q8R5K4 NOL6_MOUSE Nucleolar protein 6 (Nucleolar RNA-associated protein) (Nrap) 1152 129,228 Alternative sequence (2); Chain (1); Coiled coil (1); Erroneous initiation (4); Modified residue (3); Sequence conflict (4) SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11895476}. Chromosome {ECO:0000269|PubMed:11895476}. Note=Localizes to condensed chromosomes in mitosis. SUBUNIT: Probably associated with rRNA. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:11895476}. +P97466 NOGG_MOUSE Noggin 232 25,770 Chain (1); Disulfide bond (4); Glycosylation (1); Signal peptide (1) FUNCTION: Essential for cartilage morphogenesis and joint formation. Inhibitor of bone morphogenetic proteins (BMP) signaling which is required for growth and patterning of the neural tube and somite (PubMed:9585504, PubMed:9603738). Inhibits chondrocyte differentiation through its interaction with GDF5 and, probably, GDF6 (By similarity). {ECO:0000250|UniProtKB:Q13253, ECO:0000269|PubMed:9585504, ECO:0000269|PubMed:9603738}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Homodimer. Interacts with GDF5; inhibits chondrocyte differentiation. {ECO:0000250|UniProtKB:Q13253}. TISSUE SPECIFICITY: Expressed in condensing cartilage and immature chondrocytes. {ECO:0000269|PubMed:9603738}. +Q6WKZ7 NOSTN_MOUSE Nostrin (Disabled homolog 2-interacting protein 2) (Dab2-interacting protein 2) (Nitric oxide synthase trafficker) (eNOS-trafficking inducer) 506 57,673 Chain (1); Coiled coil (2); Domain (3); Modified residue (2); Sequence conflict (1) FUNCTION: Multivalent adapter protein which may decrease NOS3 activity by inducing its translocation away from the plasma membrane. {ECO:0000250, ECO:0000269|PubMed:16171775}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8IVI9}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8IVI9}; Cytoplasmic side {ECO:0000250|UniProtKB:Q8IVI9}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q8IVI9}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q8IVI9}. Cytoplasm {ECO:0000269|PubMed:15596140}. Nucleus {ECO:0000269|PubMed:15596140}. Note=Enriched in selected actin structures. {ECO:0000250|UniProtKB:Q8IVI9}. SUBUNIT: Homotrimer. Interacts with NOS3, DNM2, WASL and CAV1 (By similarity). Interacts with DAB2. {ECO:0000250, ECO:0000269|PubMed:15596140}. DOMAIN: The SH3 domain mediates interaction with NOS3, DNM2 and WASL. {ECO:0000250}.; DOMAIN: The F-BAR domain is necessary for membrane targeting. {ECO:0000250}. +Q9Z0J4 NOS1_MOUSE Nitric oxide synthase, brain (EC 1.14.13.39) (Constitutive NOS) (NC-NOS) (NOS type I) (Neuronal NOS) (N-NOS) (nNOS) (Peptidyl-cysteine S-nitrosylase NOS1) (bNOS) 1429 160,472 Alternative sequence (5); Chain (1); Domain (3); Helix (1); Metal binding (1); Modified residue (4); Nucleotide binding (5); Region (4); Sequence conflict (1) FUNCTION: Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In the brain and peripheral nervous system, NO displays many properties of a neurotransmitter. Probably has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such SRR. Isoform NNOS Mu may be an effector enzyme for the dystrophin complex. {ECO:0000269|PubMed:17293453}. PTM: Ubiquitinated; mediated by STUB1/CHIP in the presence of Hsp70 and Hsp40 (in vitro). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane, sarcolemma; Peripheral membrane protein. Cell projection, dendritic spine {ECO:0000250}. Note=In skeletal muscle, it is localized beneath the sarcolemma of fast-twitch muscle fiber by associating with the dystrophin glycoprotein complex. In neurons, enriched in dendritic spines (By similarity). {ECO:0000250}. SUBUNIT: Homodimer. Forms a ternary complex with CAPON and SYN1. Interacts with ZDHHC23. Interacts with NOSIP; which may impair its synaptic location (By similarity). Interacts with DLG4; the interaction possibly being prevented by the association between NOS1 and CAPON. Interacts with HTR4. Forms a ternary complex with CAPON and RASD1. Interacts with VAC14 (By similarity). Interacts (via N-terminal domain) with DLG4 (via N-terminal tandem pair of PDZ domains) (By similarity). Interacts with SLC6A4. {ECO:0000250, ECO:0000269|PubMed:10623522, ECO:0000269|PubMed:11086993, ECO:0000269|PubMed:15466885, ECO:0000269|PubMed:17452640, ECO:0000269|Ref.11}. DOMAIN: The PDZ domain in the N-terminal part of the neuronal isoform participates in protein-protein interaction, and is responsible for targeting nNos to synaptic membranes in muscles. Mediates interaction with VAC14 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed in the nervous system: expressed in cerebrum, olfactory bulb, hippocampus, midbrain, cerebellum, pons, medulla oblongata, and spinal cord. Also found in skeletal muscle, where it is localized beneath the sarcolemma of fast twitch muscle fibers, and in spleen, heart, kidney, and liver. N-NOS-1 and N-NOS-2 are found in all parts of the nervous system. NNOS beta and gamma occur in a region-specific manner in the brain and NNOS beta expression is developmentally regulated. NNOS Mu is only found in mature skeletal and cardiac muscles. DISEASE: Note=In MDX mice (mouse model of dystrophinopathy) the dystrophin complex is disrupted and nNOS is displaced from sarcolemma and accumulates in the cytosol. +P28656 NP1L1_MOUSE Nucleosome assembly protein 1-like 1 (Brain protein DN38) (NAP-1-related protein) 391 45,345 Chain (1); Compositional bias (3); Initiator methionine (1); Lipidation (1); Modified residue (10); Motif (1); Mutagenesis (2); Propeptide (1); Sequence conflict (1) FUNCTION: Plays a key role in the regulation of embryonic neurogenesis (PubMed:29490266). Promotes the proliferation of neural progenitors and inhibits neuronal differentiation during cortical development (PubMed:29490266). Regulates neurogenesis via the modulation of RASSF10; regulates RASSF10 expression by promoting SETD1A-mediated H3K4 methylation at the RASSF10 promoter (PubMed:29490266). {ECO:0000269|PubMed:29490266}. PTM: Polyglycylated by TTLL10 on glutamate residues, resulting in polyglycine chains on the gamma-carboxyl group. Both polyglutamylation and polyglycylation modifications can coexist on the same protein on adjacent residues, and lowering polyglycylation levels increases polyglutamylation, and reciprocally. {ECO:0000269|PubMed:18331838}.; PTM: Polyglutamylated by TTLL4 on glutamate residues, resulting in polyglutamate chains on the gamma-carboxyl group. Both polyglutamylation and polyglycylation modifications can coexist on the same protein on adjacent residues, and lowering polyglycylation levels increases polyglutamylation, and reciprocally. {ECO:0000269|PubMed:17499049}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29490266}. Cytoplasm {ECO:0000269|PubMed:29490266}. Melanosome {ECO:0000250|UniProtKB:P55209}. SUBUNIT: Interacts with SETD1A. {ECO:0000269|PubMed:29490266}. DOMAIN: The acidic domains are probably involved in the interaction with histones. TISSUE SPECIFICITY: Highly expressed in the brain (at protein level) (PubMed:29490266). High expression in cerebral cortex, not in cerebellar cortex. {ECO:0000269|PubMed:29490266}. +Q9JKN6 NOVA1_MOUSE RNA-binding protein Nova-1 (Neuro-oncological ventral antigen 1) (Ventral neuron-specific protein 1) 507 51,756 Chain (1); Compositional bias (1); Domain (3); Modified residue (1); Motif (1) FUNCTION: Functions to regulate alternative splicing in neurons by binding pre-mRNA in a sequence-specific manner to activate exon inclusion. It binds specifically to the sequence UCAUY. Most likely acts to activate the inclusion of exon E3A in the glycine receptor alpha-2 chain and of exon E9 in gamma-aminobutyric-acid receptor gamma-2 subunit via a distal downstream UCAU-rich intronic splicing enhancer. {ECO:0000269|PubMed:10719891, ECO:0000269|PubMed:12808107, ECO:0000269|PubMed:15933722}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with PTBP2; the interaction is direct. {ECO:0000269|PubMed:10829067}. DISEASE: Note=Defects in Nova1 leads to neuronal death in spinal and brainstem neurons. {ECO:0000269|PubMed:10719891}. +Q9QZS7 NPHN_MOUSE Nephrin (Renal glomerulus-specific cell adhesion receptor) 1256 136,336 Alternative sequence (1); Chain (1); Disulfide bond (8); Domain (9); Glycosylation (7); Modified residue (5); Sequence conflict (21); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1079 1099 Helical. {ECO:0000255}. TOPO_DOM 36 1078 Extracellular. {ECO:0000255}.; TOPO_DOM 1100 1256 Cytoplasmic. {ECO:0000255}. FUNCTION: Seems to play a role in the development or function of the kidney glomerular filtration barrier. Regulates glomerular vascular permeability. May anchor the podocyte slit diaphragm to the actin cytoskeleton. Plays a role in skeletal muscle formation through regulation of myoblast fusion. {ECO:0000269|PubMed:11136707, ECO:0000269|PubMed:12039968, ECO:0000269|PubMed:19470472}. PTM: Phosphorylated at Tyr-1208 by FYN, leading to the recruitment and activation of phospholipase C-gamma-1/PLCG1. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Located at podocyte slit diaphragm between podocyte foot processes. {ECO:0000269|PubMed:10504499}. SUBUNIT: Interacts with NPHS2 and with CD2AP (via C-terminal domain). Interacts with MAGI1 (via PDZ 2 and 3 domains) forming a tripartite complex with IGSF5/JAM4. Forms a complex with ACTN4, CASK, IQGAP1, MAGI2, SPTAN1 and SPTBN1 (By similarity). Interacts with DDN; the interaction is direct. Self-associates (via the Ig-like domains). Also interacts (via the Ig-like domains) with KIRREL1 and KIRREL2; the interaction with KIRREL1 is dependent on KIRREL1 glycosylation. Interacts with KIRREL3 (PubMed:15843475, PubMed:18752272). {ECO:0000250|UniProtKB:Q9R044, ECO:0000269|PubMed:11733379, ECO:0000269|PubMed:11733557, ECO:0000269|PubMed:12424224, ECO:0000269|PubMed:12660326, ECO:0000269|PubMed:15843475, ECO:0000269|PubMed:17537921, ECO:0000269|PubMed:18752272, ECO:0000269|PubMed:19887377}. TISSUE SPECIFICITY: Expressed in kidney glomeruli. In the embryo, expressed in the mesonephric kidney at E11 with strong expression in cranial tubules with podocyte-like structures. Expression is observed in the podocytes of the developing kidney from E13. High expression is also detected in the developing cerebellum, hindbrain, spinal cord, retina and hypothalamus. Expressed in skeletal muscle during myoblast fusion such as in the adult following acute injury and in the embryo but not detected in uninjured adult skeletal muscle. Isoform 1 and isoform 2 are expressed in the newborn brain and developing cerebellum. Isoform 1 is the predominant isoform in adult kidney. {ECO:0000269|PubMed:10820162, ECO:0000269|PubMed:11136707, ECO:0000269|PubMed:12538735, ECO:0000269|PubMed:19470472, ECO:0000269|PubMed:19887377}. +Q7TNH6 NPHP3_MOUSE Nephrocystin-3 1325 150,289 Alternative sequence (2); Chain (1); Coiled coil (1); Erroneous initiation (1); Erroneous termination (1); Frameshift (1); Initiator methionine (1); Lipidation (1); Natural variant (1); Repeat (11); Sequence conflict (11) FUNCTION: Required for normal ciliary development and function. Inhibits disheveled-1-induced canonical Wnt-signaling activity and may also play a role in the control of non-canonical Wnt signaling that regulates planar cell polarity. Probably acts as a molecular switch between different Wnt signaling pathways. Required for proper convergent extension cell movements. {ECO:0000269|PubMed:18371931}. SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000250}. Note=Localization to cilium is mediated via interaction with UNC119 and UNC119B, which bind to the myristoyl moiety of the N-terminus. {ECO:0000250}. SUBUNIT: Interacts with NPHP1 and INVS/NPHP2. Interacts (when myristoylated) with UNC119 and UNC119B; interaction is required for localization to cilium (By similarity). Interacts with CEP164 (By similarity). Component of a complex containing at least ANKS6, INVS, NEK8 and NPHP3. ANKS6 may organize complex assembly by linking INVS and NPHP3 to NEK8 and INVS may target the complex to the proximal ciliary axoneme (By similarity). {ECO:0000250}. DISEASE: Note=Defects in Nphp3 may be the cause of polycystic kidney disease (pcy). Pcy is a recessive disorder causing chronic renal failure. The Pcy phenotype can be slowed by diet modification such as protein restriction, administration of soy-based proteins, administration of methylprednisolone or treatment with V2R antagonist. In contrast administration of bicarbonate/citrate has no effect. +P60670 NPL4_MOUSE Nuclear protein localization protein 4 homolog (Protein NPL4) 608 68,017 Alternative sequence (1); Beta strand (3); Chain (1); Domain (1); Erroneous initiation (1); Helix (2); Initiator methionine (1); Modified residue (2); Turn (2); Zinc finger (1) Protein degradation; proteasomal ubiquitin-dependent pathway. FUNCTION: The ternary complex containing UFD1, VCP and NPLOC4 binds ubiquitinated proteins and is necessary for the export of misfolded proteins from the ER to the cytoplasm, where they are degraded by the proteasome. The NPLOC4-UFD1-VCP complex regulates spindle disassembly at the end of mitosis and is necessary for the formation of a closed nuclear envelope (By similarity). Acts as a negative regulator of type I interferon production via the complex formed with VCP and UFD1, which binds to DDX58/RIG-I and recruits RNF125 to promote ubiquitination and degradation of DDX58/RIG-I (By similarity). {ECO:0000250|UniProtKB:Q8TAT6, ECO:0000250|UniProtKB:Q9ES54}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9ES54}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9ES54}. Nucleus {ECO:0000250|UniProtKB:Q9ES54}. Note=Associated with the endoplasmic reticulum and nuclear. {ECO:0000250|UniProtKB:Q9ES54}. SUBUNIT: Heterodimer with UFD1. The heterodimer binds ubiquitinated proteins. The heterodimer binds to VCP and inhibits Golgi membrane fusion (By similarity). Interacts with ZFAND2B; probably through VCP (PubMed:24160817). {ECO:0000250|UniProtKB:Q9ES54, ECO:0000269|PubMed:24160817}. DOMAIN: Binds ubiquitinated proteins via its RanBP2-type zinc finger. {ECO:0000250|UniProtKB:Q9ES54}. +Q91V88 NPNT_MOUSE Nephronectin (Preosteoblast EGF-like repeat protein with MAM domain) 561 61,490 Alternative sequence (2); Chain (1); Compositional bias (1); Disulfide bond (12); Domain (6); Motif (1); Mutagenesis (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Functional ligand of integrin alpha-8/beta-1 in kidney development. Regulates the expression of GDNF with integrin alpha-8/beta-1 which is essential for kidney development. May also play a role in the development and function of various tissues, regulating cell adhesion, spreading and survival through the binding of several integrins. {ECO:0000269|PubMed:11470831, ECO:0000269|PubMed:11546798, ECO:0000269|PubMed:17537792}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:11470831, ECO:0000269|PubMed:11546798}. Note=Trapped on the cell surface or in the extracellular matrix. SUBUNIT: Homodimer and homotrimer. DOMAIN: The MAM domain is required for localization at the cell surface. TISSUE SPECIFICITY: Expressed in kidney (at protein level). {ECO:0000269|PubMed:11470831}. +Q9ESQ8 NPVF_MOUSE Pro-FMRFamide-related neuropeptide VF (FMRFamide-related peptides) [Cleaved into: Neuropeptide NPSF; Neuropeptide RFRP-1; Neuropeptide NPVF (Neuropeptide RFRP-2)] 188 21,065 Alternative sequence (1); Modified residue (2); Peptide (3); Propeptide (3); Signal peptide (1) FUNCTION: Neuropeptide RFRP-1 acts as a potent negative regulator of gonadotropin synthesis and secretion. Neuropeptides NPSF and NPVF efficiently inhibit forskolin-induced production of cAMP. Neuropeptide NPVF blocks morphine-induced analgesia (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. +Q04573 NPY1R_MOUSE Neuropeptide Y receptor type 1 (NPY1-R) 382 44,015 Alternative sequence (2); Chain (1); Disulfide bond (1); Glycosylation (3); Lipidation (1); Modified residue (2); Topological domain (8); Transmembrane (7) TRANSMEM 34 54 Helical; Name=1. {ECO:0000255}.; TRANSMEM 76 96 Helical; Name=2. {ECO:0000255}.; TRANSMEM 116 136 Helical; Name=3. {ECO:0000255}.; TRANSMEM 154 174 Helical; Name=4. {ECO:0000255}.; TRANSMEM 211 231 Helical; Name=5. {ECO:0000255}.; TRANSMEM 260 280 Helical; Name=6. {ECO:0000255}.; TRANSMEM 299 319 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 33 Extracellular. {ECO:0000255}.; TOPO_DOM 55 75 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 97 115 Extracellular. {ECO:0000255}.; TOPO_DOM 137 153 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 175 210 Extracellular. {ECO:0000255}.; TOPO_DOM 232 259 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 281 298 Extracellular. {ECO:0000255}.; TOPO_DOM 320 382 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for neuropeptide Y and peptide YY. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: The alpha form is highly expressed in the brain, heart, kidney, spleen, skeletal muscle, and lung, whereas the beta receptor mRNA was not detected in these tissues. However, the beta form is expressed in mouse embryonic developmental stage (7 and 11 days), bone marrow cells and several hematopoietic cell lines. +P57774 NPY_MOUSE Pro-neuropeptide Y [Cleaved into: Neuropeptide Y (Neuropeptide tyrosine) (NPY); C-flanking peptide of NPY (CPON)] 97 10,874 Modified residue (2); Peptide (2); Sequence conflict (2); Signal peptide (1); Site (1) FUNCTION: NPY is implicated in the control of feeding and in secretion of gonadotrophin-release hormone. {ECO:0000250}. PTM: The neuropeptide Y form is cleaved at Pro-30 by the prolyl endopeptidase FAP (seprase) activity (in vitro). {ECO:0000250|UniProtKB:P01303}. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: One of the most abundant peptides in the nervous system. Also found in some chromaffin cells of the adrenal medulla. +O54915 NR1I2_MOUSE Nuclear receptor subfamily 1 group I member 2 (Orphan nuclear receptor PXR) (Pregnane X receptor) 431 49,567 Alternative sequence (1); Binding site (3); Chain (1); DNA binding (1); Domain (1); Motif (1); Region (1); Zinc finger (2) FUNCTION: Nuclear receptor that binds and is activated by a variety of endogenous and xenobiotic compounds. Transcription factor that activates the transcription of multiple genes involved in the metabolism and secretion of potentially harmful xenobiotics, endogenous compounds and drugs. Response to specific ligands is species-specific, due to differences in the ligand-binding domain. Binds to a response element in the promoters of the CYP3A4 and ABCB1/MDR1 genes (By similarity). Activated by naturally occurring steroids such as pregnenolone and progesterone, the cholesterol metabolite 5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol, synthetic glucocorticoids and antiglucocorticoids and 16-alpha-carbonitrile (PCN). {ECO:0000250, ECO:0000269|PubMed:12569201, ECO:0000269|PubMed:19297428}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}. SUBUNIT: Heterodimer with RXRA. Interacts with NCOA1 (By similarity). {ECO:0000250}. +Q8VC65 NRM_MOUSE Nurim (Nuclear envelope membrane protein) (Nuclear rim protein) 262 29,435 Chain (1); Compositional bias (2); Topological domain (7); Transmembrane (6) TRANSMEM 5 28 Helical. {ECO:0000255}.; TRANSMEM 59 80 Helical. {ECO:0000255}.; TRANSMEM 98 114 Helical. {ECO:0000255}.; TRANSMEM 134 164 Helical. {ECO:0000255}.; TRANSMEM 192 210 Helical. {ECO:0000255}.; TRANSMEM 217 234 Helical. {ECO:0000255}. TOPO_DOM 1 4 Nuclear. {ECO:0000255}.; TOPO_DOM 29 58 Perinuclear space. {ECO:0000255}.; TOPO_DOM 81 97 Nuclear. {ECO:0000255}.; TOPO_DOM 115 133 Perinuclear space. {ECO:0000255}.; TOPO_DOM 165 191 Nuclear. {ECO:0000255}.; TOPO_DOM 211 216 Perinuclear space. {ECO:0000255}.; TOPO_DOM 235 262 Nuclear. {ECO:0000255}. SUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q8CFV4 NRN1_MOUSE Neuritin (Candidate plasticity gene 15 protein) 142 15,353 Chain (1); Lipidation (1); Propeptide (1); Signal peptide (1) FUNCTION: Promotes neurite outgrowth and especially branching of neuritic processes in primary hippocampal and cortical cells. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}. Cell junction, synapse {ECO:0000305|PubMed:22632720}. SUBUNIT: Component of the outer core of AMPAR complex. AMPAR complex consists of an inner core made of 4 pore-forming GluA/GRIA proteins (GRIA1, GRIA2, GRIA3 and GRIA4) and 4 major auxiliary subunits arranged in a twofold symmetry. One of the two pairs of distinct binding sites is occupied either by CNIH2, CNIH3 or CACNG2, CACNG3. The other harbors CACNG2, CACNG3, CACNG4, CACNG8 or GSG1L. This inner core of AMPAR complex is complemented by outer core constituents binding directly to the GluA/GRIA proteins at sites distinct from the interaction sites of the inner core constituents. Outer core constituents include at least PRRT1, PRRT2, CKAMP44/SHISA9, FRRS1L and NRN1. The proteins of the inner and outer core serve as a platform for other, more peripherally associated AMPAR constituents. Alone or in combination, these auxiliary subunits control the gating and pharmacology of the AMPAR complex and profoundly impact their biogenesis and protein processing. {ECO:0000269|PubMed:22632720}. TISSUE SPECIFICITY: Expressed in the brain (at protein level). {ECO:0000269|PubMed:22632720}. +Q9D7C9 NRK2_MOUSE Nicotinamide riboside kinase 2 (NRK 2) (NmR-K 2) (EC 2.7.1.22) (Integrin beta-1-binding protein 3) (Muscle integrin-binding protein) (MIBP) (Nicotinic acid riboside kinase 2) (EC 2.7.1.173) (Ribosylnicotinamide kinase 2) (RNK 2) (Ribosylnicotinic acid kinase 2) 195 22,375 Active site (1); Binding site (2); Chain (1); Metal binding (2); Nucleotide binding (3); Region (3) Cofactor biosynthesis; NAD(+) biosynthesis. FUNCTION: Catalyzes the phosphorylation of nicotinamide riboside (NR) and nicotinic acid riboside (NaR) to form nicotinamide mononucleotide (NMN) and nicotinic acid mononucleotide (NaMN). Reduces laminin matrix deposition and cell adhesion to laminin, but not to fibronectin. Involved in the regulation of PXN at the protein level and of PXN tyrosine phosphorylation. May play a role in the regulation of terminal myogenesis (By similarity). {ECO:0000250, ECO:0000269|PubMed:10613898}. SUBUNIT: Monomer (By similarity). Interacts with ITGB1 alone or when associated with alpha-7, but not with alpha-5. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in skeletal muscle (at protein level). {ECO:0000269|PubMed:10613898}. +P70365 NCOA1_MOUSE Nuclear receptor coactivator 1 (NCoA-1) (EC 2.3.1.48) (Nuclear receptor coactivator protein 1) (mNRC-1) (Steroid receptor coactivator 1) (SRC-1) 1447 157,016 Alternative sequence (4); Beta strand (6); Chain (1); Compositional bias (2); Cross-link (3); Domain (2); Helix (4); Initiator methionine (1); Modified residue (16); Motif (7); Mutagenesis (2); Region (2); Sequence conflict (13); Turn (1) FUNCTION: Nuclear receptor coactivator that directly binds nuclear receptors and stimulates the transcriptional activities in a hormone-dependent fashion. Involved in the coactivation of different nuclear receptors, such as for steroids (PGR, GR and ER), retinoids (RXRs), thyroid hormone (TRs) and prostanoids (PPARs). Also involved in coactivation mediated by STAT3, STAT5A, STAT5B and STAT6 transcription factors. Displays histone acetyltransferase activity toward H3 and H4; the relevance of such activity remains however unclear. Plays a central role in creating multisubunit coactivator complexes that act via remodeling of chromatin, and possibly acts by participating in both chromatin remodeling and recruitment of general transcription factors. Required with NCOA2 to control energy balance between white and brown adipose tissues. Required for mediating steroid hormone response. Isoform 2 has a higher thyroid hormone-dependent transactivation activity than isoform 1 and isoform 3. {ECO:0000269|PubMed:12507421, ECO:0000269|PubMed:16148126, ECO:0000269|PubMed:8616895, ECO:0000269|PubMed:9506940}. PTM: Sumoylated; sumoylation increases its interaction with PGR and prolongs its retention in the nucleus. It does not prevent its ubiquitination and does not exert a clear effect on the stability of the protein (By similarity). {ECO:0000250}.; PTM: Ubiquitinated; leading to proteasome-mediated degradation. Ubiquitination and sumoylation take place at different sites (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:8855229}. SUBUNIT: Interacts with NCOA6 and NCOA2. Interacts with the FDL motif of STAT5A and STAT5B. Interacts with the LXXLL motif of STAT6. Interacts with STAT3 following IL-6 stimulation. Interacts with the basal transcription factor GTF2B. Interacts with COPS5, NR3C1, PCAF and TTLL5/STAMP. Interacts with the histone acetyltransferases EP300 and CREBBP, and the methyltransferase CARM1. Interacts with PSMB9. Interacts with UBE2L3; they functionally interact to regulate progesterone receptor transcriptional activity. Interacts with PRMT2 and DDX5. Interacts with ASXL1. Interacts with PRMT6. Interacts (via LXXLL 1, 2 and 3 motifs) with RORC (via AF-2 motif). Interacts in a ligand-dependent fashion with RXRA. Interacts with TRIP4. Interacts with NR4A3 (PubMed:12709428). Interacts with VDR (By similarity). {ECO:0000250|UniProtKB:Q15788, ECO:0000269|PubMed:10381882, ECO:0000269|PubMed:12709428, ECO:0000269|PubMed:14757047, ECO:0000269|PubMed:16148126, ECO:0000269|PubMed:8616895, ECO:0000269|PubMed:8855229}. DOMAIN: The C-terminal (1113-1447) part mediates the histone acetyltransferase (HAT) activity. {ECO:0000250}.; DOMAIN: Contains 7 Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs. LXXLL motifs 3, 4 and 5 are essential for the association with nuclear receptors. LXXLL motif 7, which is not present in isoform 2, increases the affinity for steroid receptors in vitro. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:8855229, ECO:0000269|PubMed:9192892}. +O35136 NCAM2_MOUSE Neural cell adhesion molecule 2 (N-CAM-2) (NCAM-2) (Neural cell adhesion molecule RB-8) (R4B12) 837 93,204 Alternative sequence (1); Chain (1); Disulfide bond (5); Domain (7); Glycosylation (8); Lipidation (1); Modified residue (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 698 718 Helical. {ECO:0000255}. TOPO_DOM 20 697 Extracellular. {ECO:0000255}.; TOPO_DOM 719 837 Cytoplasmic. {ECO:0000255}. FUNCTION: May play important roles in selective fasciculation and zone-to-zone projection of the primary olfactory axons. SUBCELLULAR LOCATION: Isoform Long: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Isoform Short: Cell membrane; Lipid-anchor, GPI-anchor. TISSUE SPECIFICITY: Expressed in subsets of both olfactory and vomeronasal neurons in a zone-specific manner. +O09000 NCOA3_MOUSE Nuclear receptor coactivator 3 (NCoA-3) (EC 2.3.1.48) (Amplified in breast cancer-1 protein homolog) (AIB-1) (CBP-interacting protein) (p/CIP) (pCIP) (Receptor-associated coactivator 3) (RAC-3) (Steroid receptor coactivator protein 3) (SRC-3) (Thyroid hormone receptor activator molecule 1) (ACTR) (TRAM-1) 1398 151,574 Chain (1); Compositional bias (2); Domain (2); Initiator methionine (1); Modified residue (18); Motif (3); Region (2) FUNCTION: Nuclear receptor coactivator that directly binds nuclear receptors and stimulates the transcriptional activities in a hormone-dependent fashion. Plays a central role in creating a multisubunit coactivator complex, probably via remodeling of chromatin. Involved in the coactivation of different nuclear receptors, such as for steroids (GR and ER), retinoids (RARs and RXRs), thyroid hormone (TRs), vitamin D3 (VDR) and prostanoids (PPARs). Displays histone acetyltransferase activity. Also involved in the coactivation of the NF-kappa-B pathway via its interaction with the NFKB1 subunit (By similarity). {ECO:0000250, ECO:0000269|PubMed:10823921}. PTM: Acetylated by CREBBP. Acetylation occurs in the RID domain, and disrupts the interaction with nuclear receptors and regulates its function (By similarity). {ECO:0000250}.; PTM: Methylated by CARM1. {ECO:0000269|PubMed:11701890}.; PTM: Phosphorylated by IKK complex. Regulated its function (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}. Note=Mainly cytoplasmic and weakly nuclear. Upon TNF activation and subsequent phosphorylation, it translocates from the cytoplasm to the nucleus (By similarity). {ECO:0000250}. SUBUNIT: Interacts with the histone acetyltransferase protein CREBBP. These two proteins are present in a complex containing NCOA2, IKKA, IKKB and IKBKG. Interacts with PCAF and NR3C1 (By similarity). Interacts with CARM1. Interacts with CASP8AP2. Interacts with ATAD2 and this interaction is enhanced by estradiol (By similarity). Interacts with PSMB9. Binds to CSNK1D (By similarity). Found in a complex containing NCOA3, AR and MAK. Interacts with DDX5. Interacts with NPAS2 (By similarity). Interacts with NR4A3 (via AF-1 domain) (PubMed:12709428). Interacts with ESRRB; mediates the interaction between ESRRB and RNA polymerase II complexes and allows NCOA3 corecruitment to ESRRB, KLF4, NANOG, and SOX2 enhancer regions to trigger ESRRB-dependent gene activation involved in self-renewal and pluripotency (PubMed:23019124). {ECO:0000250, ECO:0000269|PubMed:12709428, ECO:0000269|PubMed:23019124}. DOMAIN: Contains three Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs. Motifs 1 and 2 are essential for the association with nuclear receptors, and constitute the RID domain (Receptor-interacting domain) (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Not expressed in all steroid sensitive tissues. Highly expressed in the female reproductive system, in both oocyte and smooth muscle cells of the oviduct, but not expressed in the uterine endometrium. Highly expressed in mammary glands. Expressed moderately in smooth muscle cells of both blood vessels and intestines, and weakly expressed in hepatocytes. In brain, highly expressed in neurons of the hyppocampus, and in mitral cell and granule layers of the olfactory bulb. Expressed moderately in the internal layer of cerebellum. Not expressed in the spinal chord, cardiac muscle, skeletal muscle, thymus and pancreas. {ECO:0000269|PubMed:10823921}. +Q9D9W1 PIFO_MOUSE Protein pitchfork 207 23,434 Alternative sequence (1); Chain (1) FUNCTION: During primary cilia disassembly, involved in cilia disassembly. Required specifically to control cilia retraction as well as the liberation and duplication of the basal body/centrosome. May act by stimulating AURKA activity at the basal body in a cell cycle-dependent manner. {ECO:0000269|PubMed:20643351}. SUBCELLULAR LOCATION: Isoform 1: Golgi apparatus, Golgi stack. Golgi apparatus, trans-Golgi network.; SUBCELLULAR LOCATION: Isoform 2: Nucleus.; SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20643351}. Cytoplasmic vesicle {ECO:0000269|PubMed:20643351}. Note=Accumulates specifically at the basal body and ciliary necklace during the early steps of cilia assembly and disassembly, when structural, functional and regulatory proteins are delivered to cilia. At S phase, accumulates in vesicles and declines during mitosis. In node pit cells, found close to the ciliary membrane along the axoneme. In spermatocytes, localizes to particles along the stabilized microtubules of tails. SUBUNIT: Interacts with proteins involved in ciliary transport, including ARL13B, CETN1, KIF3A, RAB6A, RAB8A, TUBB1 and TUBG1. Interacts with AURKA. {ECO:0000269|PubMed:20643351}. TISSUE SPECIFICITY: Expressed in tissues rich in ciliated cells, such as lung, kidney, vas deferens and testis. Both isoforms 1 and 2 are expressed in testis. {ECO:0000269|PubMed:20643351}. +Q8C119 NDNF_MOUSE Protein NDNF (Epidermacan) (Neuron-derived neurotrophic factor) 568 65,027 Chain (1); Compositional bias (1); Domain (2); Frameshift (1); Glycosylation (2); Sequence conflict (2); Signal peptide (1) FUNCTION: Promotes neuron migration, growth and survival as well as neurite outgrowth (By similarity). Promotes matrix assembly and cell adhesiveness. Promotes endothelial cell survival, vessel formation and plays an important role in the process of revascularization through NOS3-dependent mechanisms (PubMed:24706764). {ECO:0000250|UniProtKB:Q8TB73, ECO:0000269|PubMed:18757743, ECO:0000269|PubMed:24706764}. PTM: O-glycosylated; contains heparan sulfate and chondroitin sulfate. {ECO:0000269|PubMed:20969804}.; PTM: N-glycosylated. {ECO:0000269|PubMed:20969804}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18757743}. SUBUNIT: Binds heparin and chondroitin sulfate. {ECO:0000269|PubMed:18757743}. TISSUE SPECIFICITY: Expressed in brain and spinal cord with no expression detected in heart, kidney or liver. Expressed by neurons but not by astrocytes. In the brain, detected in the cerebrum, cerebellum and olfactory bulbs. In the cerebral cortex, highly expressed in Cajal-Retzius cells. Also expressed in hippocampal neurons and in Purkinje and granule cells of the cerebellum (at protein level). {ECO:0000269|PubMed:20969804}. +Q8C2R7 PIGM_MOUSE GPI mannosyltransferase 1 (EC 2.4.1.-) (GPI mannosyltransferase I) (GPI-MT-I) (Phosphatidylinositol-glycan biosynthesis class M protein) (PIG-M) 423 49,789 Chain (1); Sequence conflict (3); Topological domain (9); Transmembrane (8) TRANSMEM 18 38 Helical. {ECO:0000255}.; TRANSMEM 90 110 Helical. {ECO:0000255}.; TRANSMEM 170 190 Helical. {ECO:0000255}.; TRANSMEM 225 245 Helical. {ECO:0000255}.; TRANSMEM 288 308 Helical. {ECO:0000255}.; TRANSMEM 330 350 Helical. {ECO:0000255}.; TRANSMEM 358 378 Helical. {ECO:0000255}.; TRANSMEM 385 405 Helical. {ECO:0000255}. TOPO_DOM 1 17 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 39 89 Lumenal. {ECO:0000255}.; TOPO_DOM 111 169 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 191 224 Lumenal. {ECO:0000255}.; TOPO_DOM 246 287 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 309 329 Lumenal. {ECO:0000255}.; TOPO_DOM 351 357 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 379 384 Lumenal. {ECO:0000255}.; TOPO_DOM 406 423 Cytoplasmic. {ECO:0000255}. Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis. FUNCTION: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN-acyl-PI during GPI precursor assembly (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q6PD26 PIGS_MOUSE GPI transamidase component PIG-S (Phosphatidylinositol-glycan biosynthesis class S protein) 555 61,711 Chain (1); Glycosylation (2); Topological domain (3); Transmembrane (2) TRANSMEM 19 39 Helical. {ECO:0000255}.; TRANSMEM 521 541 Helical. {ECO:0000255}. TOPO_DOM 1 18 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 40 520 Lumenal. {ECO:0000255}.; TOPO_DOM 542 555 Cytoplasmic. {ECO:0000255}. Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis. FUNCTION: Component of the GPI transamidase complex. Essential for transfer of GPI to proteins, particularly for formation of carbonyl intermediates (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Forms a complex with PIGK/GPI8, PIGT, PIGU and GAA1. {ECO:0000250}. +Q9CR61 NDUB7_MOUSE NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7 (Complex I-B18) (CI-B18) (NADH-ubiquinone oxidoreductase B18 subunit) 137 16,331 Beta strand (1); Chain (1); Disulfide bond (2); Domain (1); Helix (3); Initiator methionine (1); Lipidation (1); Modified residue (1); Motif (2); Turn (1) FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. {ECO:0000250|UniProtKB:P17568}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P17568}; Peripheral membrane protein {ECO:0000250|UniProtKB:P17568}. Mitochondrion intermembrane space {ECO:0000250|UniProtKB:P17568}. SUBUNIT: Complex I is composed of 45 different subunits. {ECO:0000250|UniProtKB:P17568}. DOMAIN: Contains two C-X9-C motifs that are predicted to form a helix-coil-helix structure, permitting the formation of intramolecular disulfide bonds. {ECO:0000250|UniProtKB:P17568}. +P0DN34 NDUB1_MOUSE NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1 (Complex I-MNLL) (CI-MNLL) (NADH-ubiquinone oxidoreductase MNLL subunit) 57 6,954 Beta strand (1); Chain (1); Helix (2); Transmembrane (1) TRANSMEM 10 26 Helical. {ECO:0000255}. FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. {ECO:0000250|UniProtKB:O75438}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:O75438}; Single-pass membrane protein {ECO:0000255}; Matrix side {ECO:0000250|UniProtKB:O75438}. SUBUNIT: Complex I is composed of 45 different subunits. {ECO:0000250|UniProtKB:O75438}. +Q61220 NELL2_MOUSE Protein kinase C-binding protein NELL2 (MEL91 protein) (NEL-like protein 2) 819 91,432 Chain (1); Disulfide bond (18); Domain (9); Glycosylation (7); Sequence conflict (9); Signal peptide (1) FUNCTION: Required for neuron survival through the modulation of MAPK pathways (By similarity). Involved in the regulation of hypothalamic GNRH secretion and the control of puberty (By similarity). {ECO:0000250|UniProtKB:Q62918}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q62918}. +Q9D1J1 NECP2_MOUSE Adaptin ear-binding coat-associated protein 2 (NECAP endocytosis-associated protein 2) (NECAP-2) 266 28,598 Chain (1); Modified residue (1); Motif (2) FUNCTION: Involved in endocytosis. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000269|PubMed:14555962}. Cell membrane {ECO:0000269|PubMed:14555962}. Note=Colocalizes with AP-2 at the plasma membrane. SUBUNIT: Interacts with AP1G1 and AP2A1 components of the adapter protein complexes AP-1 and AP-2. Interacts with the GAE domain proteins GGA1, GGA2 and GGA3. {ECO:0000269|PubMed:14665628}. DOMAIN: The WXXF motifs mediate binding of accessory proteins to the ear-domain of AP-1, GGAs and AP-2 through hydrophobic interactions. Selective binding to the GAE domains of AP-1 or to the alpha-ear domain of AP-2 is tuned by the acidic context surrounding the motif and the properties of the second residue of the motif itself (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver, lung, skeletal muscles and testis (at protein level). +P63239 NEC1_MOUSE Neuroendocrine convertase 1 (NEC 1) (EC 3.4.21.93) (Furin homolog) (PC3) (Prohormone convertase 1) (Propeptide-processing protease) (Proprotein convertase 1) (PC1) 753 84,174 Active site (3); Beta strand (7); Chain (1); Disulfide bond (3); Domain (2); Glycosylation (2); Helix (4); Propeptide (1); Sequence conflict (7); Signal peptide (1); Turn (2) FUNCTION: Involved in the processing of hormone and other protein precursors at sites comprised of pairs of basic amino acid residues. Substrates include POMC, renin, enkephalin, dynorphin, somatostatin, insulin and AGRP. {ECO:0000269|PubMed:16384863}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle. Note=Localized in the secretion granules. +Q91ZR4 NEK8_MOUSE Serine/threonine-protein kinase Nek8 (EC 2.7.11.1) (Never in mitosis A-related kinase 8) (NimA-related protein kinase 8) 698 75,265 Active site (1); Binding site (1); Chain (1); Domain (1); Modified residue (1); Mutagenesis (4); Natural variant (1); Nucleotide binding (1); Repeat (5); Sequence conflict (2) FUNCTION: Required for renal tubular integrity. May regulate local cytoskeletal structure in kidney tubule epithelial cells. May regulate ciliary biogenesis through targeting of proteins to the cilia. Plays a role in organogenesis and is involved in the regulation of the Hippo signaling pathway. {ECO:0000269|PubMed:18199800}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16267153}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16267153}. Cell projection, cilium {ECO:0000269|PubMed:16267153}. Note=Predominantly cytoplasmic. Localizes to the proximal region of the primary cilium and is not observed in dividing cells. SUBUNIT: Interacts with PKD2; may regulate PKD2 targeting to the cilium. Component of a complex containing at least ANKS6, INVS, NEK8 and NPHP3. ANKS6 may organize complex assembly by linking INVS and NPHP3 to NEK8 and INVS may target the complex to the proximal ciliary axoneme (By similarity). Interacts with ANKS3 (PubMed:25671767). {ECO:0000250, ECO:0000269|PubMed:25671767}. TISSUE SPECIFICITY: Kidney, liver, and testis. DISEASE: Note=Defects in Nek8 are the cause of autosomal recessive juvenile polycystic kidney disease (ARJPKD). +Q8C0Q4 NEK11_MOUSE Serine/threonine-protein kinase Nek11 (EC 2.7.11.1) (Never in mitosis A-related kinase 11) (NimA-related protein kinase 11) 628 71,648 Active site (1); Binding site (1); Chain (1); Coiled coil (1); Domain (1); Modified residue (1); Nucleotide binding (1); Sequence conflict (3) FUNCTION: Protein kinase which plays an important role in the G2/M checkpoint response to DNA damage. Controls degradation of CDC25A by directly phosphorylating it on residues whose phosphorylation is required for BTRC-mediated polyubiquitination and degradation. {ECO:0000250|UniProtKB:Q8NG66}. PTM: Phosphorylated by NEK2. Phosphorylation at Ser-274 is important for its activation. {ECO:0000250|UniProtKB:Q8NG66}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8NG66}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q8NG66}. Note=Nuclear during interphase but moves to the polar microtubules during prometaphase and metaphase. Accumulates in the nucleolus in G1/S-arrested cells. {ECO:0000250|UniProtKB:Q8NG66}. SUBUNIT: Interacts with NEK2. {ECO:0000250|UniProtKB:Q8NG66}. +Q60591 NFAC2_MOUSE Nuclear factor of activated T-cells, cytoplasmic 2 (NF-ATc2) (NFATc2) (NFAT pre-existing subunit) (NF-ATp) (T-cell transcription factor NFAT1) 927 100,020 Alternative sequence (2); Chain (1); DNA binding (1); Domain (1); Modified residue (32); Motif (1); Mutagenesis (10); Region (4); Repeat (3); Sequence caution (1); Sequence conflict (7) FUNCTION: Plays a role in the inducible expression of cytokine genes in T-cells, especially in the induction of the IL-2, IL-3, IL-4, TNF-alpha or GM-CSF. Promotes invasive migration through the activation of GPC6 expression and WNT5A signaling pathway. {ECO:0000250|UniProtKB:Q13469}. PTM: In resting cells, phosphorylated by NFATC-kinase on at least 18 sites in the 99-365 region. Upon cell stimulation, all these sites except Ser-245 are dephosphorylated by calcineurin. Dephosphorylation induces a conformational change that simultaneously exposes an NLS and masks an NES, which results in nuclear localization. Simultaneously, one site among Ser-53; Ser-54 and Ser-56 is phosphorylated; which is required for full transcriptional activity. {ECO:0000269|PubMed:11030334}.; PTM: Ubiquitinated in endothelial cells by RNF213 downstream of the non-canonical Wnt signaling pathway, leading to its degradation by the proteasome. {ECO:0000250|UniProtKB:Q13469}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11030334}. Nucleus {ECO:0000269|PubMed:11030334}. Note=Cytoplasmic for the phosphorylated form and nuclear after activation that is controlled by calcineurin-mediated dephosphorylation. Rapid nuclear exit of NFATC is thought to be one mechanism by which cells distinguish between sustained and transient calcium signals. The subcellular localization of NFATC plays a key role in the regulation of gene transcription. SUBUNIT: Member of the multicomponent NFATC transcription complex that consists of at least two components, a pre-existing cytoplasmic component NFATC2 and an inducible nuclear component NFATC1. Other members such as NFATC4, NFATC3 or members of the activating protein-1 family, MAF, GATA4 and Cbp/p300 can also bind the complex. The phosphorylated form specifically interacts with XPO1; which mediates nuclear export. NFATC proteins bind to DNA as monomers. Interacts with NFATC2IP. Interacts with FOXP3 (By similarity). Interacts with TBX21 ('Thr-302' phosphorylated form) (PubMed:23616576). Interacts with KAT2A (PubMed:28424240). Interacts with HOMER2 and HOMER3 (By similarity). Interacts with protein phosphatase PPP3CA/calcineurin A (By similarity). {ECO:0000250|UniProtKB:Q13469, ECO:0000269|PubMed:11030334, ECO:0000269|PubMed:23616576, ECO:0000269|PubMed:28424240, ECO:0000269|PubMed:8943202}. DOMAIN: Rel Similarity Domain (RSD) allows DNA-binding and cooperative interactions with AP1 factors. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in thymus, spleen, heart, testis, brain, placenta, muscle and pancreas. {ECO:0000269|PubMed:18675896}. +P97305 NFAC3_MOUSE Nuclear factor of activated T-cells, cytoplasmic 3 (NF-ATc3) (NFATc3) (NFATx) (T-cell transcription factor NFAT4) (NF-AT4) 1075 115,451 Alternative sequence (2); Chain (1); Compositional bias (1); DNA binding (1); Domain (1); Initiator methionine (1); Modified residue (4); Motif (3); Region (2); Repeat (3); Sequence conflict (14) FUNCTION: Acts as a regulator of transcriptional activation. Plays a role in the inducible expression of cytokine genes in T-cells, especially in the induction of the IL-2 (By similarity). {ECO:0000250}. PTM: Phosphorylated by NFATC-kinase; dephosphorylated by calcineurin. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Cytoplasmic for the phosphorylated form and nuclear after activation that is controlled by calcineurin-mediated dephosphorylation. Rapid nuclear exit of NFATC is thought to be one mechanism by which cells distinguish between sustained and transient calcium signals. The subcellular localization of NFATC plays a key role in the regulation of gene transcription. SUBUNIT: Member of the multicomponent NFATC transcription complex that consists of at least two components, a pre-existing cytoplasmic component NFATC2 and an inducible nuclear component NFATC1. Other members such as NFATC4, NFATC3 or members of the activating protein-1 family, MAF, GATA4 and Cbp/p300 can also bind the complex. NFATC proteins bind to DNA as monomers. DOMAIN: Rel Similarity Domain (RSD) allows DNA-binding and cooperative interactions with AP1 factors. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in thymus. Weakly expressed in muscle, spleen and kidney. Also expressed in lymph node. +Q9JMH7 NEUR3_MOUSE Sialidase-3 (EC 3.2.1.18) (Ganglioside sialidase) (Membrane sialidase) (N-acetyl-alpha-neuraminidase 3) 418 46,846 Active site (3); Binding site (7); Chain (1); Modified residue (1); Motif (1); Repeat (3) FUNCTION: Plays a role in modulating the ganglioside content of the lipid bilayer at the level of membrane-bound sialyl glycoconjugates. {ECO:0000269|PubMed:10713120}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Expressed in heart, brain and cerebral cortex. {ECO:0000269|PubMed:10713120}. +P25799 NFKB1_MOUSE Nuclear factor NF-kappa-B p105 subunit (DNA-binding factor KBF1) (EBP-1) (NF-kappa-B1 p84/NF-kappa-B1 p98) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1) [Cleaved into: Nuclear factor NF-kappa-B p50 subunit] 971 105,615 Alternative sequence (5); Beta strand (28); Chain (2); Compositional bias (1); Cross-link (1); Domain (2); Erroneous initiation (1); Helix (8); Lipidation (1); Modified residue (12); Motif (1); Region (3); Repeat (7); Sequence conflict (9); Site (1); Turn (4) FUNCTION: NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52 and the heterodimeric p65-p50 complex appears to be most abundant one. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. NF-kappa-B heterodimeric p65-p50 and RelB-p50 complexes are transcriptional activators. The NF-kappa-B p50-p50 homodimer is a transcriptional repressor, but can act as a transcriptional activator when associated with BCL3. NFKB1 appears to have dual functions such as cytoplasmic retention of attached NF-kappa-B proteins by p105 and generation of p50 by a cotranslational processing. The proteasome-mediated process ensures the production of both p50 and p105 and preserves their independent function, although processing of NFKB1/p105 also appears to occur post-translationally. p50 binds to the kappa-B consensus sequence 5'-GGRNNYYCC-3', located in the enhancer region of genes involved in immune response and acute phase reactions. Plays a role in the regulation of apoptosis. Isoform 5, isoform 6 and isoform 7 act as inhibitors of transactivation of p50 NF-kappa-B subunit, probably by sequestering it in the cytoplasm. Isoform 3 (p98) (but not p84 or p105) acts as a transactivator of NF-kappa-B-regulated gene expression. In a complex with MAP3K8, NFKB1/p105 represses MAP3K8-induced MAPK signaling; active MAP3K8 is released by proteasome-dependent degradation of NFKB1/p105. PTM: While translation occurs, the particular unfolded structure after the GRR repeat promotes the generation of p50 making it an acceptable substrate for the proteasome. This process is known as cotranslational processing. The processed form is active and the unprocessed form acts as an inhibitor (I kappa B-like), being able to form cytosolic complexes with NF-kappa B, trapping it in the cytoplasm. Complete folding of the region downstream of the GRR repeat precludes processing.; PTM: Phosphorylation at 'Ser-930' and 'Ser-935' are required for BTRC/BTRCP-mediated proteolysis. {ECO:0000250}.; PTM: Polyubiquitination seems to allow p105 processing.; PTM: S-nitrosylation of Cys-59 affects DNA binding. {ECO:0000250}.; PTM: The covalent modification of cysteine by 15-deoxy-Delta12,14-prostaglandin-J2 is autocatalytic and reversible. It may occur as an alternative to other cysteine modifications, such as S-nitrosylation and S-palmitoylation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Nuclear, but also found in the cytoplasm in an inactive form complexed to an inhibitor (I-kappa-B).; SUBCELLULAR LOCATION: Isoform 5: Cytoplasm.; SUBCELLULAR LOCATION: Isoform 6: Nucleus. Cytoplasm.; SUBCELLULAR LOCATION: Isoform 7: Nucleus. SUBUNIT: Component of the NF-kappa-B p65-p50 complex. Component of the NF-kappa-B p65-p50 complex. Homodimer; component of the NF-kappa-B p50-p50 complex. Component of the NF-kappa-B p105-p50 complex. Component of the NF-kappa-B p50-c-Rel complex. Component of a complex consisting of the NF-kappa-B p50-p50 homodimer and BCL3. Also interacts with MAP3K8. NF-kappa-B p50 subunit interacts with NCOA3 coactivator, which may coactivate NF-kappa-B dependent expression via its histone acetyltransferase activity. Interacts with DSIPI; this interaction prevents nuclear translocation and DNA-binding. Interacts with SPAG9 and UNC5CL. NFKB1/p105 interacts with CFLAR; the interaction inhibits p105 processing into p50. NFKB1/p105 forms a ternary complex with MAP3K8 and TNIP2. Interacts with GSK3B; the interaction prevents processing of p105 to p50. NFKB1/p50 interacts with NFKBIE (By similarity). NFKB1/p50 interacts with NFKBIZ. Nuclear factor NF-kappa-B p50 subunit interacts with NFKBID. Directly interacts with MEN1 (By similarity). Interacts with HIF1AN (By similarity). {ECO:0000250}. DOMAIN: The C-terminus of p105 might be involved in cytoplasmic retention, inhibition of DNA-binding, and transcription activation.; DOMAIN: Glycine-rich region (GRR) appears to be a critical element in the generation of p50. +Q9WV30 NFAT5_MOUSE Nuclear factor of activated T-cells 5 (NF-AT5) (Rel domain-containing transcription factor NFAT5) (T-cell transcription factor NFAT5) 1534 165,800 Alternative sequence (5); Chain (1); Compositional bias (5); Cross-link (3); DNA binding (1); Domain (1); Erroneous gene model prediction (1); Erroneous initiation (1); Erroneous translation (1); Modified residue (6); Sequence conflict (1) FUNCTION: Transcription factor involved in the transcriptional regulation of osmoprotective and inflammatory genes. Regulates hypertonicity-induced cellular accumulation of osmolytes. {ECO:0000269|PubMed:11934689, ECO:0000269|PubMed:14983020}. PTM: Phosphorylated at Thr-135 by CDK5 in response to osmotic stress; this phosphorylation mediates its rapid nuclear localization. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10377394, ECO:0000269|PubMed:11934689}. Cytoplasm {ECO:0000269|PubMed:11934689}. Note=Nuclear distribution increases under hypertonic conditions. SUBUNIT: Homodimer when bound to DNA, completely encircles its DNA target. Does not bind with Fos and Jun transcription factors. Interacts with CIDEC; this interaction is direct and retains NFAT5 in the cytoplasm (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Detected in white and brown adipose tissue, muscle, heart, liver and kidney. Expressed in lymphocytes (at protein level). {ECO:0000269|PubMed:14983020, ECO:0000269|PubMed:23233732}. +Q9QY23 PKP3_MOUSE Plakophilin-3 797 87,333 Alternative sequence (1); Chain (1); Modified residue (10); Repeat (8); Sequence conflict (3) FUNCTION: May play a role in junctional plaques. SUBCELLULAR LOCATION: Nucleus. Cell junction, desmosome. Note=Nuclear and associated with desmosomes. +P27612 PLAP_MOUSE Phospholipase A-2-activating protein (PLA2P) (PLAP) 794 87,221 Chain (1); Domain (2); Frameshift (1); Modified residue (2); Mutagenesis (1); Repeat (13); Sequence caution (1); Sequence conflict (6) FUNCTION: Plays a role in protein ubiquitination, sorting and degradation through its association with VCP (By similarity). Involved in ubiquitin-mediated membrane proteins trafficking to late endosomes in an ESCRT-dependent manner, and hence plays a role in synaptic vesicle recycling (PubMed:28413018). May play a role in macroautophagy, regulating for instance the clearance of damaged lysosomes (By similarity). Plays a role in cerebellar Purkinje cell development (PubMed:28413018). Positively regulates cytosolic and calcium-independent phospholipase A2 activities in a tumor necrosis factor alpha (TNF-alpha)- or lipopolysaccharide (LPS)-dependent manner, and hence prostaglandin E2 biosynthesis (PubMed:28007986). {ECO:0000250|UniProtKB:Q9Y263, ECO:0000269|PubMed:28007986, ECO:0000269|PubMed:28413018}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28413018}. Cytoplasm {ECO:0000269|PubMed:28413018}. Cell junction, synapse {ECO:0000269|PubMed:28413018}. Note=Recruited to damaged lysosomes decorated with K48-linked ubiquitin chains. {ECO:0000250|UniProtKB:Q9Y263}. SUBUNIT: Interacts with ubiquitin. Interacts with UBXN6, VCP and YOD1; may form a complex involved in macroautophagy. {ECO:0000250|UniProtKB:Q9Y263}. DOMAIN: The PUL domain is composed of 6 armadillo-like repeats and mediates the interaction with VCP C-terminus. {ECO:0000250|UniProtKB:Q9Y263}.; DOMAIN: The PFU domain mediates interaction with ubiquitin. {ECO:0000250|UniProtKB:Q9Y263}. TISSUE SPECIFICITY: Expressed in the brain, with highest levels in hippocampal neurons, cerebellar granular cell layer and Purkinje cells (PubMed:28413018). {ECO:0000269|PubMed:28413018}. +Q8R1F1 NIBL1_MOUSE Niban-like protein 1 (Protein FAM129B) 749 84,819 Chain (1); Domain (1); Erroneous initiation (1); Initiator methionine (1); Lipidation (1); Modified residue (11); Sequence conflict (10) FUNCTION: May play a role in apoptosis suppression. {ECO:0000250}. PTM: As apoptosis proceeds, degraded via an proteasome-independent pathway, probably by caspases. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:21148485}. Cell junction, adherens junction {ECO:0000250}. Membrane {ECO:0000250|UniProtKB:Q96TA1}; Lipid-anchor {ECO:0000250|UniProtKB:Q96TA1}. Note=In exponentially growing cells, exclusively cytoplasmic. Cell membrane localization is observed when cells reach confluency and during telophase (By similarity). Phosphorylation may play a role in relocalization to the membrane (By similarity). {ECO:0000250}. +Q9JHL1 NHRF2_MOUSE Na(+)/H(+) exchange regulatory cofactor NHE-RF2 (NHERF-2) (NHE3 kinase A regulatory protein E3KARP) (Octs2) (SRY-interacting protein 1) (SIP-1) (Sodium-hydrogen exchanger regulatory factor 2) (Solute carrier family 9 isoform A3 regulatory factor 2) (Tyrosine kinase activator protein 1) (TKA-1) 337 37,403 Alternative sequence (2); Chain (1); Domain (2); Modified residue (7); Sequence conflict (11) FUNCTION: Scaffold protein that connects plasma membrane proteins with members of the ezrin/moesin/radixin family and thereby helps to link them to the actin cytoskeleton and to regulate their surface expression. Necessary for cAMP-mediated phosphorylation and inhibition of SLC9A3. May also act as scaffold protein in the nucleus (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Nucleus {ECO:0000250}. Apical cell membrane {ECO:0000250}. Note=Localizes with EZR and PODXL at the apical cell membrane of glomerular epithelium cells and the sides of the food processes. Nuclear, in a punctate pattern (By similarity). {ECO:0000250}. SUBUNIT: Homodimer, and heterodimer with SLC9A3R1. Binds PDZK1. Interacts with SRY. Binds ADRB2, SLC9A3, P2RY1, P2YR2, RDX and LPAR2 (By similarity). Interacts with MCC (By similarity). Found in a complex with EZR, PODXL and SLC9A3R2 (By similarity). Interacts (via the PDZ domains) with PODXL (via the C-terminal PDZ-binding motif DTHL); interaction is detected in glomerular epithelium cells (By similarity). Interacts with SGK1 and KCNJ1/ROMK1 (By similarity). Interacts (via the PDZ domains) with SLC26A6 (By similarity). {ECO:0000250}. +Q3TTY0 PLB1_MOUSE Phospholipase B1, membrane-associated (Phospholipase B) (Phospholipase B/lipase) (PLB/LIP) [Includes: Phospholipase A2 (EC 3.1.1.4); Lysophospholipase (EC 3.1.1.5)] 1478 164,541 Active site (3); Alternative sequence (6); Binding site (2); Chain (1); Erroneous initiation (1); Glycosylation (6); Region (2); Repeat (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1423 1443 Helical. {ECO:0000255}. TOPO_DOM 24 1422 Extracellular. {ECO:0000255}.; TOPO_DOM 1444 1478 Cytoplasmic. {ECO:0000255}. FUNCTION: Membrane-associated phospholipase. Exhibits a calcium-independent broad substrate specificity including phospholipase A2/lysophospholipase activity. Preferential hydrolysis at the sn-2 position of diacylphospholipids and diacyglycerol, whereas it shows no positional specificity toward triacylglycerol. Exhibits also esterase activity toward p-nitrophenyl. May act on the brush border membrane to facilitate the absorption of digested lipids (By similarity). {ECO:0000250}. PTM: Undergoes proteolytic cleavage in the ileum. {ECO:0000250}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Present in the intestinal brush border membranes. {ECO:0000250}. DOMAIN: Repeat 2 contains the catalytic domain. {ECO:0000250}. +O70131 NINJ1_MOUSE Ninjurin-1 (Nerve injury-induced protein 1) 152 16,555 Chain (1); Modified residue (3); Topological domain (3); Transmembrane (2) TRANSMEM 80 100 Helical. {ECO:0000255}.; TRANSMEM 121 141 Helical. {ECO:0000255}. TOPO_DOM 1 79 Extracellular. {ECO:0000255}.; TOPO_DOM 101 120 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 142 152 Extracellular. {ECO:0000255}. FUNCTION: Homophilic cell adhesion molecule that promotes axonal growth. May play a role in nerve regeneration and in the formation and function of other tissues. Cell adhesion requires divalent cations (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. +Q9WV52 PLEK2_MOUSE Pleckstrin-2 353 40,018 Beta strand (8); Chain (1); Domain (3); Helix (3); Modified residue (2) FUNCTION: May help orchestrate cytoskeletal arrangement. Contribute to lamellipodia formation. Overexpression of pleckstrin 2 causes large lamellipodia and peripheral ruffle formation. SUBCELLULAR LOCATION: Cell projection, lamellipodium membrane; Peripheral membrane protein. Cytoplasm, cytoskeleton. TISSUE SPECIFICITY: Ubiquitous. Most abundant in the thymus, large bowel, small bowel, stomach, and prostate. +P30549 NK2R_MOUSE Substance-K receptor (SKR) (NK-2 receptor) (NK-2R) (Neurokinin A receptor) (Tachykinin receptor 2) 384 43,114 Chain (1); Disulfide bond (1); Glycosylation (1); Lipidation (1); Topological domain (8); Transmembrane (7) TRANSMEM 33 56 Helical; Name=1. {ECO:0000255}.; TRANSMEM 70 90 Helical; Name=2. {ECO:0000255}.; TRANSMEM 108 129 Helical; Name=3. {ECO:0000255}.; TRANSMEM 150 170 Helical; Name=4. {ECO:0000255}.; TRANSMEM 197 218 Helical; Name=5. {ECO:0000255}.; TRANSMEM 252 272 Helical; Name=6. {ECO:0000255}.; TRANSMEM 291 310 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 32 Extracellular. {ECO:0000255}.; TOPO_DOM 57 69 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 91 107 Extracellular. {ECO:0000255}.; TOPO_DOM 130 149 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 171 196 Extracellular. {ECO:0000255}.; TOPO_DOM 219 251 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 273 290 Extracellular. {ECO:0000255}.; TOPO_DOM 311 384 Cytoplasmic. {ECO:0000255}. FUNCTION: This is a receptor for the tachykinin neuropeptide substance K (neurokinin A). It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system. The rank order of affinity of this receptor to tachykinins is: substance K > neuromedin-K > substance P. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +O54709 NKG2D_MOUSE NKG2-D type II integral membrane protein (Killer cell lectin-like receptor subfamily K member 1) (NK cell receptor D) (NKG2-D-activating NK receptor) (CD antigen CD314) 232 26,710 Alternative sequence (1); Beta strand (9); Chain (1); Disulfide bond (4); Domain (1); Glycosylation (3); Helix (2); Topological domain (2); Transmembrane (1); Turn (4) TRANSMEM 67 89 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 66 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 90 232 Extracellular. {ECO:0000255}. FUNCTION: Function as an activating and costimulatory receptor involved in immunosurveillance upon binding to various cellular stress-inducible ligands displayed at the surface of autologous tumor cells and virus-infected cells. Provides both stimulatory and costimulatory innate immune responses on activated killer (NK) cells, leading to cytotoxic activity. Acts as a costimulatory receptor for T-cell receptor (TCR) in CD8(+) T-cell-mediated adaptive immune responses by amplifying T-cell activation. Stimulates perforin-mediated elimination of ligand-expressing tumor cells. Signaling involves calcium influx, culminating in the expression of TNF-alpha. Participates in NK cell-mediated bone marrow graft rejection. May play a regulatory role in differentiation and survival of NK cells. Binds to ligands belonging to various subfamilies of MHC class I-related glycoproteins including RAET1A, RAET1B, RAET1C, RAET1D, RAET1E, H60 and MULT1. {ECO:0000269|PubMed:10894171, ECO:0000269|PubMed:11248803, ECO:0000269|PubMed:11557981, ECO:0000269|PubMed:11567106, ECO:0000269|PubMed:12150888, ECO:0000269|PubMed:12370332, ECO:0000269|PubMed:12426564, ECO:0000269|PubMed:12426565, ECO:0000269|PubMed:15189740, ECO:0000269|PubMed:16086018, ECO:0000269|PubMed:18394936, ECO:0000269|PubMed:19631564, ECO:0000269|PubMed:21898152, ECO:0000269|PubMed:23298206}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12426565, ECO:0000269|PubMed:15294961}; Single-pass type II membrane protein {ECO:0000269|PubMed:12426565, ECO:0000269|PubMed:15294961}. Note=Colocalized with HCST and TYROBP on the cell surface. SUBUNIT: Homodimer; disulfide-linked. Heterohexamer composed of two subunits of KLRK1 and four subunits of HCST/DAP10 (By similarity). Isoform 1 (via transmembrane domain) interacts with HCST/DAP10; the interaction is required for KLRK1 cell surface expression on activated CD8(+) T-cells, but is dispensable on activated TYROBP-expressing NK cells. Isoform 2 (via transmembrane domain) interacts with HCST/DAP10 (via transmembrane domain); the interaction is required for KLRK1 NK cell surface expression and induces NK cell-mediated cytotoxicity. Isoform 2 (via transmembrane domain) interacts with TYROBP (via transmembrane domain); the interaction is required for KLRK1 NK cell surface expression and induce NK cell-mediated cytotoxicity and cytokine secretion. Isoform 1 does not interact with TYROBP. Interacts with CEACAM1; recruits PTPN6 that dephosphorylates VAV1 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P26718, ECO:0000269|PubMed:11825567, ECO:0000269|PubMed:12426564, ECO:0000269|PubMed:12426565, ECO:0000269|PubMed:15294961}. TISSUE SPECIFICITY: Expressed in natural killer (NK) cells, activated CD8(+) alpha-beta and gamma-delta T-cells and natural killer T (NKT) cells (at protein level). May be expressed on dendritic cell (DC). Isoform 1 is strongly expressed in natural killer (NK) cells. Isoform 2 is weakly expressed in natural killer (NK) cells. Isoform 1 and isoform 2 are expressed in stimulated, but not in unstimulated, CD8(+) T-cells and macrophages. {ECO:0000269|PubMed:11248803, ECO:0000269|PubMed:11567106, ECO:0000269|PubMed:12150888, ECO:0000269|PubMed:15048723}. DISEASE: Note=Involved in autoreactive CD8(+) T-cell-mediated development of autoimmune diabetes. {ECO:0000269|PubMed:15189740}. +Q8BG17 NOL12_MOUSE Nucleolar protein 12 (Nucleolar protein of 25 kDa) 217 25,356 Chain (1); Coiled coil (1); Sequence conflict (2) FUNCTION: May bind to 28S rRNA. In vitro binds single-stranded nucleic acids. {ECO:0000269|PubMed:16430885}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:16430885}. SUBUNIT: Interacts with KIAA1191. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain, lung, spleen, kidney and heart. {ECO:0000269|PubMed:16430885}. +Q6GQT9 NOMO1_MOUSE Nodal modulator 1 1214 133,420 Chain (1); Coiled coil (1); Erroneous initiation (3); Glycosylation (3); Modified residue (2); Sequence conflict (11); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1151 1167 Helical. {ECO:0000255}. TOPO_DOM 24 1150 Extracellular. {ECO:0000255}.; TOPO_DOM 1168 1214 Cytoplasmic. {ECO:0000255}. FUNCTION: May antagonize Nodal signaling. {ECO:0000250|UniProtKB:Q5JPE7}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}. +Q99LH1 NOG2_MOUSE Nucleolar GTP-binding protein 2 728 83,345 Chain (1); Domain (1); Modified residue (2); Nucleotide binding (2); Sequence conflict (4) FUNCTION: GTPase that associates with pre-60S ribosomal subunits in the nucleolus and is required for their nuclear export and maturation (By similarity). May promote cell proliferation possibly by increasing p53/TP53 protein levels, and consequently those of its downstream product CDKN1A/p21, and decreasing RPL23A protein levels (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q13823}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q13823}. SUBUNIT: Interacts with LYAR and RPL23A (By similarity). Interacts with the nuclear importin-beta receptor and, at a lower extent, with importin-alpha (By similarity). {ECO:0000250|UniProtKB:Q13823}. +Q9JJG9 NOA1_MOUSE Nitric oxide-associated protein 1 693 77,379 Chain (1); Domain (1); Modified residue (1); Mutagenesis (1); Sequence conflict (3) FUNCTION: Involved in regulation of mitochondrial protein translation and respiration. Plays a role in mitochondria-mediated cell death. May act as a scaffolding protein or stabilizer of respiratory chain supercomplexes. Binds GTP. {ECO:0000269|PubMed:18456285, ECO:0000269|PubMed:21118999}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:16380119, ECO:0000269|PubMed:18456285}; Peripheral membrane protein {ECO:0000269|PubMed:16380119, ECO:0000269|PubMed:18456285}; Matrix side {ECO:0000269|PubMed:16380119, ECO:0000269|PubMed:18456285}. SUBUNIT: Homodimer or multimer. Interacts with mitochondrial complex I, DAP3, MRPL12 and MRPS27. {ECO:0000269|PubMed:18456285}. TISSUE SPECIFICITY: Expressed in tissues associated with high mitochondria content including testes, heart, liver, brain and thymus. Also expressed in various bone cell lines. {ECO:0000269|PubMed:16380119}. +Q01705 NOTC1_MOUSE Neurogenic locus notch homolog protein 1 (Notch 1) (Motch A) (mT14) (p300) [Cleaved into: Notch 1 extracellular truncation (NEXT); Notch 1 intracellular domain (NICD)] 2531 270,835 Alternative sequence (5); Beta strand (8); Chain (3); Cross-link (1); Disulfide bond (115); Domain (36); Glycosylation (47); Helix (14); Metal binding (16); Modified residue (3); Mutagenesis (34); Region (4); Repeat (8); Sequence conflict (56); Signal peptide (1); Site (3); Topological domain (2); Transmembrane (1) TRANSMEM 1726 1746 Helical. {ECO:0000255}. TOPO_DOM 19 1725 Extracellular. {ECO:0000255}.; TOPO_DOM 1747 2531 Cytoplasmic. {ECO:0000255}. FUNCTION: Functions as a receptor for membrane-bound ligands Jagged-1 (JAG1), Jagged-2 (JAG2) and Delta-1 (DLL1) to regulate cell-fate determination. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. Affects the implementation of differentiation, proliferation and apoptotic programs. Involved in angiogenesis; negatively regulates endothelial cell proliferation and migration and angiogenic sprouting. Involved in the maturation of both CD4(+) and CD8(+) cells in the thymus. Important for follicular differentiation and possibly cell fate selection within the follicle. During cerebellar development, functions as a receptor for neuronal DNER and is involved in the differentiation of Bergmann glia. Represses neuronal and myogenic differentiation. May play an essential role in postimplantation development, probably in some aspect of cell specification and/or differentiation. May be involved in mesoderm development, somite formation and neurogenesis. May enhance HIF1A function by sequestering HIF1AN away from HIF1A. Required for the THBS4 function in regulating protective astrogenesis from the subventricular zone (SVZ) niche after injury. Involved in determination of left/right symmetry by modulating the balance between motile and immotile (sensory) cilia at the left-right organiser (LRO). {ECO:0000269|PubMed:15965470, ECO:0000269|PubMed:18299578, ECO:0000269|PubMed:23160044, ECO:0000269|PubMed:23615612}. PTM: Synthesized in the endoplasmic reticulum as an inactive form which is proteolytically cleaved by a furin-like convertase in the trans-Golgi network before it reaches the plasma membrane to yield an active, ligand-accessible form (PubMed:10882062, PubMed:10882063). Cleavage results in a C-terminal fragment N(TM) and a N-terminal fragment N(EC). Following ligand binding, it is cleaved by ADAM17 to yield a membrane-associated intermediate fragment called notch extracellular truncation (NEXT) (PubMed:10882062, PubMed:10882063). Following endocytosis, this fragment is then cleaved by presenilin dependent gamma-secretase to release a notch-derived peptide containing the intracellular domain (NICD) from the membrane (PubMed:10882062, PubMed:11518718, PubMed:11459941). {ECO:0000269|PubMed:10882062, ECO:0000269|PubMed:10882063, ECO:0000269|PubMed:11459941, ECO:0000269|PubMed:11518718}.; PTM: Phosphorylated.; PTM: O-linked glycosylation by GALNT11 is involved in determination of left/right symmetry: glycosylation promotes activation of NOTCH1, possibly by promoting cleavage by ADAM17, modulating the balance between motile and immotile (sensory) cilia at the left-right organiser (LRO) (By similarity). O-glycosylated on the EGF-like domains (PubMed:21757702). O-glucosylated at Ser-435 by KDELC1 and KDELC2 (PubMed:30127001). Contains both O-linked fucose and O-linked glucose in the EGF-like domains 11, 12 and 13, which are interacting with the residues on DLL4 (By similarity). O-glycosylation at Ser-1027 is only partial (PubMed:21757702). MFNG-, RFNG- and LFNG-mediated modification of O-fucose residues at specific EGF-like domains results in inhibition of its activation by JAG1 and enhancement of its activation by DLL1 via an increased binding to DLL1 (PubMed:28089369). {ECO:0000250|UniProtKB:P46531, ECO:0000250|UniProtKB:Q07008, ECO:0000269|PubMed:21757702, ECO:0000269|PubMed:28089369, ECO:0000269|PubMed:30127001}.; PTM: Ubiquitinated. Undergoes 'Lys-29'-linked polyubiquitination by ITCH; promotes the lysosomal degradation of non-activated internalized NOTCH1 (PubMed:18628966, PubMed:23886940). Monoubiquitination at Lys-1749 is required for activation by gamma-secretase cleavage, it promotes interaction with AAK1, which stabilizes it. Deubiquitination by EIF3F is necessary for nuclear import of activated Notch (PubMed:15240571). {ECO:0000269|PubMed:15240571, ECO:0000269|PubMed:18628966, ECO:0000269|PubMed:23886940}.; PTM: Hydroxylated at Asn-1945 and Asn-2012 by HIF1AN. Hydroxylation reduces affinity for HI1AN and may thus indirectly modulate negative regulation of NICD. {ECO:0000269|PubMed:17573339, ECO:0000269|PubMed:18299578}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10882062, ECO:0000269|PubMed:28498977}; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Notch 1 intracellular domain: Nucleus {ECO:0000269|PubMed:28498977}. Note=Following proteolytical processing NICD is translocated to the nucleus. Nuclear location may require MEGF10. {ECO:0000269|PubMed:28498977}. SUBUNIT: Heterodimer of a C-terminal fragment N(TM) and an N-terminal fragment N(EC) which are probably linked by disulfide bonds. Interacts with DNER, DTX1, DTX2 and RBPJ/RBPSUH. Also interacts with MAML1, MAML2 and MAML3 which act as transcriptional coactivators for NOTCH1. Notch 1 intracellular domain interacts with SNW1; the interaction involves multimerized NOTCH1 NICD and is implicated in a formation of an intermediate preactivation complex which associates with DNA-bound CBF-1/RBPJ. The activated membrane-bound form interacts with AAK1 which promotes NOTCH1 stabilization. Forms a trimeric complex with FBXW7 and SGK1. Interacts with HIF1AN. HIF1AN negatively regulates the function of notch intracellular domain (NICD), accelerating myogenic differentiation. Interacts (via NICD) with SNAI1 (via zinc fingers); the interaction induces SNAI1 degradation via MDM2-mediated ubiquitination and inhibits SNAI1-induced cell invasion. Interacts (via NICD) with MDM2A. Interacts (via NICD) with BCL6; the interaction decreases MAML1 recruitment by NOTCH1 NICD on target genes DNA and inhibits NOTCH1 transcractivation activity. Interacts with THBS4. Interacts (via the EGF-like repeat region) with CCN3 (via CTCK domain) (PubMed:12050162). Interacts (via EGF-like domains) with DLL4 (via N-terminal DSL and MNNL domains) (By similarity). Interacts with ZMIZ1. Interacts (via NICD domain) with MEGF10 (via the cytoplasmic domain) (PubMed:28498977). Interacts with DLL1 and JAG1 (PubMed:28089369). Interacts (via NICD domain) with PRAG1 (PubMed:25038227). Forms a complex with PRAG1, N1ICD and MAML1, in a MAML1-dependent manner (PubMed:25038227). {ECO:0000250|UniProtKB:Q07008, ECO:0000269|PubMed:11226752, ECO:0000269|PubMed:12050162, ECO:0000269|PubMed:15019995, ECO:0000269|PubMed:15965470, ECO:0000269|PubMed:17573339, ECO:0000269|PubMed:18299578, ECO:0000269|PubMed:21464124, ECO:0000269|PubMed:23160044, ECO:0000269|PubMed:23615612, ECO:0000269|PubMed:25038227, ECO:0000269|PubMed:28089369, ECO:0000269|PubMed:28498977}. TISSUE SPECIFICITY: Highly expressed in the brain, lung and thymus. Expressed at lower levels in the spleen, bone-marrow, spinal cord, eyes, mammary gland, liver, intestine, skeletal muscle, kidney and heart. In the hair follicle, highly expressed exclusively in the epithelial compartment. {ECO:0000269|PubMed:15965470}. +Q80W85 NPM2_MOUSE Nucleoplasmin-2 207 23,309 Chain (1); Compositional bias (2); Motif (1); Region (1); Sequence conflict (1); Site (2) FUNCTION: Core histones chaperone involved in chromatin reprogramming, specially during fertilization and early embryonic development. Probably involved in sperm DNA decondensation during fertilization. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12714744}. Note=Found in the oocyte nucleus before nuclear membrane breakdown, after which it is redistributed to the cytoplasm. SUBUNIT: Homopentamer, when bound to H2A-H2B dimers only. Homodecamer of two stacked pentamers, when bound to H2A-H2B dimers and H3-H4 tetramers simultaneously (By similarity). {ECO:0000250}. DOMAIN: The acidic tract A2 mediates histone binding. {ECO:0000250}. TISSUE SPECIFICITY: Ovary specific. {ECO:0000269|PubMed:12714744}. +Q60825 NPT2A_MOUSE Sodium-dependent phosphate transport protein 2A (Sodium-phosphate transport protein 2A) (Na(+)-dependent phosphate cotransporter 2A) (NaPi-7) (Sodium/phosphate cotransporter 2A) (Na(+)/Pi cotransporter 2A) (NaPi-2a) (Solute carrier family 34 member 1) 637 68,774 Chain (1); Disulfide bond (2); Erroneous initiation (1); Glycosylation (2); Modified residue (6); Sequence conflict (11); Topological domain (9); Transmembrane (8) TRANSMEM 104 125 Helical; Name=M1. {ECO:0000255}.; TRANSMEM 146 163 Helical; Name=M2. {ECO:0000255}.; TRANSMEM 166 185 Helical; Name=M3. {ECO:0000255}.; TRANSMEM 346 368 Helical; Name=M4. {ECO:0000255}.; TRANSMEM 411 434 Helical; Name=M5. {ECO:0000255}.; TRANSMEM 465 485 Helical; Name=M6. {ECO:0000255}.; TRANSMEM 512 532 Helical; Name=M7. {ECO:0000255}.; TRANSMEM 538 559 Helical; Name=M8. {ECO:0000255}. TOPO_DOM 1 103 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 126 145 Extracellular. {ECO:0000255}.; TOPO_DOM 164 165 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 186 345 Extracellular. {ECO:0000255}.; TOPO_DOM 369 410 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 435 464 Extracellular. {ECO:0000255}.; TOPO_DOM 486 511 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 533 537 Extracellular. {ECO:0000255}.; TOPO_DOM 560 637 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in actively transporting phosphate into cells via Na(+) cotransport in the renal brush border membrane. Probably mediates 70-80% of the apical influx. {ECO:0000250|UniProtKB:Q06495}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:Q06495}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Interacts via its C-terminal region with PDZK2 (PubMed:11950846). Interacts with SLC9A3R1 (By similarity). {ECO:0000250|UniProtKB:Q06495, ECO:0000269|PubMed:11950846}. TISSUE SPECIFICITY: Kidney. +Q5SZA1 NPT3_MOUSE Sodium-dependent phosphate transport protein 3 (Na(+)/PI cotransporter 3) (Sodium/phosphate cotransporter 3) (Solute carrier family 17 member 2) 478 51,965 Alternative sequence (1); Chain (1); Glycosylation (4); Transmembrane (10) TRANSMEM 98 118 Helical. {ECO:0000255}.; TRANSMEM 130 150 Helical. {ECO:0000255}.; TRANSMEM 183 203 Helical. {ECO:0000255}.; TRANSMEM 211 231 Helical. {ECO:0000255}.; TRANSMEM 273 293 Helical. {ECO:0000255}.; TRANSMEM 317 337 Helical. {ECO:0000255}.; TRANSMEM 341 361 Helical. {ECO:0000255}.; TRANSMEM 363 383 Helical. {ECO:0000255}.; TRANSMEM 405 425 Helical. {ECO:0000255}.; TRANSMEM 442 462 Helical. {ECO:0000255}. FUNCTION: Important for the resorption of phosphate by the kidney. May be involved in actively transporting phosphate into cells via Na(+) cotransport in the renal brush border membrane (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SUBUNIT: Interacts with PDZK1. {ECO:0000250}. +Q64669 NQO1_MOUSE NAD(P)H dehydrogenase [quinone] 1 (EC 1.6.5.2) (Azoreductase) (DT-diaphorase) (DTD) (Menadione reductase) (NAD(P)H:quinone oxidoreductase 1) (Phylloquinone reductase) (Quinone reductase 1) (QR1) 274 30,960 Beta strand (9); Binding site (4); Chain (1); Cross-link (1); Helix (13); Initiator methionine (1); Modified residue (2); Nucleotide binding (3); Region (1); Turn (6) FUNCTION: The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinons involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Homodimer. {ECO:0000269|PubMed:10706635}. +Q8BVG8 NAT14_MOUSE N-acetyltransferase 14 (EC 2.3.1.-) 206 21,778 Chain (1); Domain (1); Transmembrane (1) TRANSMEM 57 77 Helical. {ECO:0000255}. FUNCTION: Probable acetyltransferase that binds the 5'-GGACTACAG-3' sequence of coproporphyrinogen oxidase promoter. Able to activate transcription of a reporter construct in vitro (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. +O55033 NCK2_MOUSE Cytoplasmic protein NCK2 (Growth factor receptor-bound protein 4) (NCK adaptor protein 2) (Nck-2) (SH2/SH3 adaptor protein NCK-beta) 380 42,879 Chain (1); Domain (4); Initiator methionine (1); Modified residue (5) FUNCTION: Adapter protein which associates with tyrosine-phosphorylated growth factor receptors or their cellular substrates. Maintains low levels of EIF2S1 phosphorylation by promoting its dephosphorylation by PP1. Plays a role in ELK1-dependent transcriptional activation in response to activated Ras signaling (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. SUBUNIT: Interacts with DOCK1, LIMS1 and TGFB1I1. Part of a complex containing PPP1R15B, PP1 and NCK2. Interacts with FASLG. Interacts with AXL. Interacts with PAK1, PKN2 and SOS1. Interacts (via SH2 domain) with EGFR. Interacts (via SH2 domain) with DDR1 (By similarity). {ECO:0000250}. +Q9D0F1 NDC80_MOUSE Kinetochore protein NDC80 homolog (Kinetochore protein Hec1) (Kinetochore-associated protein 2) 642 73,962 Chain (1); Coiled coil (2); Modified residue (4); Region (7); Sequence conflict (2) FUNCTION: Acts as a component of the essential kinetochore-associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity. Required for kinetochore integrity and the organization of stable microtubule binding sites in the outer plate of the kinetochore. The NDC80 complex synergistically enhances the affinity of the SKA1 complex for microtubules and may allow the NDC80 complex to track depolymerizing microtubules. Plays a role in chromosome congression and is essential for the end-on attachment of the kinetochores to spindle microtubules. {ECO:0000250|UniProtKB:O14777}. PTM: Phosphorylation begins in S phase of the cell cycle and peaks in mitosis. Phosphorylated by NEK2. May also be phosphorylated by AURKA and AURKB (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Note=Localizes to kinetochores from late prophase to anaphase. Localizes specifically to the outer plate of the kinetochore (By similarity). {ECO:0000250}. SUBUNIT: Component of the NDC80 complex, which consists of NDC80/HEC1, CDCA1, SPBC24 and SPBC25. The NDC80 complex is formed by two subcomplexes composed of NDC80/HEC1-CDCA1 and SPBC24-SPBC25. Each subcomplex is formed by parallel interactions through the coiled-coil domains of individual subunits. Formation of a tetrameric complex is mediated by interactions between the C-terminal regions of both subunits of the NDC80/HEC1-CDCA1 subcomplex and the N-terminal regions of both subunits of the SPBC24-SPBC25 complex. The tetrameric NDC80 complex has an elongated rod-like structure with globular domains at either end. Interacts with NEK2 and ZWINT specifically during mitosis. Interacts with CENPH and MIS12. May interact with AURKB, PSMC2, PSMC5 and SMC1A. May interact with RB1 during G2 phase and mitosis. Interacts with CKAP5 (By similarity). Interacts with CDT1; leading to kinetochore localization of CDT1 (By similarity). {ECO:0000250|UniProtKB:O14777}. TISSUE SPECIFICITY: Expressed in spleen, testis and thymus. {ECO:0000269|PubMed:9315664}. +Q8BLF1 NCEH1_MOUSE Neutral cholesterol ester hydrolase 1 (NCEH) (EC 3.1.1.-) (Arylacetamide deacetylase-like 1) (Chlorpyrifos oxon-binding protein) (CPO-BP) 408 45,740 Active site (3); Chain (1); Erroneous initiation (1); Glycosylation (3); Motif (1); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 5 25 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 4 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 26 408 Lumenal. {ECO:0000255}. FUNCTION: Hydrolyzes 2-acetyl monoalkylglycerol ether, the penultimate precursor of the pathway for de novo synthesis of platelet-activating factor. May be responsible for cholesterol ester hydrolysis in macrophages. Also involved in organ detoxification by hydrolyzing exogenous organophosphorus compounds. {ECO:0000269|PubMed:15840715, ECO:0000269|PubMed:16978018, ECO:0000269|PubMed:18164358, ECO:0000269|PubMed:18782767}. PTM: N-glycosylated. {ECO:0000269|PubMed:12740587}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Microsome {ECO:0000269|PubMed:18782767}. TISSUE SPECIFICITY: Present in brain, heart, kidney, lung, spinal cord and testis but not liver (at protein level). Expressed in peritoneal macrophages and kidney. {ECO:0000269|PubMed:16978018, ECO:0000269|PubMed:18782767}. +Q9ET66 PI16_MOUSE Peptidase inhibitor 16 (PI-16) (Cysteine-rich protease inhibitor) (CD antigen CD364) 498 53,650 Alternative sequence (1); Chain (1); Domain (1); Erroneous gene model prediction (2); Erroneous initiation (4); Glycosylation (2); Sequence conflict (1); Signal peptide (1) FUNCTION: May inhibit cardiomyocyte growth. {ECO:0000269|PubMed:17909105}. PTM: N-glycosylated. {ECO:0000269|PubMed:17909105}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17909105}. SUBUNIT: Interacts with PSP94/MSMB. {ECO:0000250|UniProtKB:Q6UXB8}. TISSUE SPECIFICITY: Expressed strongly in aorta and skin, and weakly in adipose tissue (at protein level). In heart, found in the extracellular space surrounding cardiomyocytes (at protein level). {ECO:0000269|PubMed:17909105}. +Q9CR95 NECP1_MOUSE Adaptin ear-binding coat-associated protein 1 (NECAP endocytosis-associated protein 1) (NECAP-1) 275 29,639 Beta strand (9); Chain (1); Helix (2); Modified residue (1); Motif (2); Mutagenesis (8); Turn (1) FUNCTION: Involved in endocytosis. {ECO:0000250, ECO:0000269|PubMed:14555962}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000269|PubMed:14555962}. Cell membrane {ECO:0000269|PubMed:14555962}. Note=Colocalizes with AP-2 at the plasma membrane. SUBUNIT: Interacts with AP1G1 and AP2A1 components of the adapter protein complexes AP-1 and AP-2. Interacts with the GAE domain proteins GGA1, GGA2 and GGA3. {ECO:0000269|PubMed:14555962, ECO:0000269|PubMed:14665628, ECO:0000269|PubMed:15359277}. DOMAIN: The WXXF motifs mediate binding of accessory proteins to the ear-domain of AP-1, GGAs and AP-2 through hydrophobic interactions. Selective binding to the GAE domains of AP-1 or to the alpha-ear domain of AP-2 is tuned by the acidic context surrounding the motif and the properties of the second residue of the motif itself. The WXXF motif 1, which is preceded by an acidic residue and has a glycine in second position mediates specific interaction with AP-1. The WXXF motif 2, which is followed by the C-terminal carboxyl group negative charge, allows specific interaction with AP-2. TISSUE SPECIFICITY: Expressed primarily in brain (at protein level). {ECO:0000269|PubMed:14555962}. +P53811 PIPNB_MOUSE Phosphatidylinositol transfer protein beta isoform (PI-TP-beta) (PtdIns transfer protein beta) (PtdInsTP beta) 271 31,487 Chain (1); Modified residue (2); Mutagenesis (2) FUNCTION: Catalyzes the transfer of PtdIns and phosphatidylcholine between membranes. PTM: Constitutive phosphorylation of Ser-262 has no effect on phospholipid transfer activity but is required for Golgi targeting. {ECO:0000269|PubMed:11953429}. SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus. +Q9ES70 NEK6_MOUSE Serine/threonine-protein kinase Nek6 (EC 2.7.11.1) (Never in mitosis A-related kinase 6) (NimA-related protein kinase 6) 313 35,742 Active site (1); Binding site (1); Chain (1); Domain (1); Modified residue (4); Nucleotide binding (1); Region (2); Sequence conflict (3); Site (1) FUNCTION: Protein kinase which plays an important role in mitotic cell cycle progression. Required for chromosome segregation at metaphase-anaphase transition, robust mitotic spindle formation and cytokinesis. Phosphorylates ATF4, CIR1, PTN, RAD26L, RBBP6, RPS7, TRIP4, RPS6KB1 and histones H1 and H3. Phosphorylates KIF11 to promote mitotic spindle formation. Involved in G2/M phase cell cycle arrest induced by DNA damage. Inhibition of activity results in apoptosis. May contribute to tumorigenesis by suppressing p53/TP53-induced cancer cell senescence (By similarity). Phosphorylates STAT3. {ECO:0000250, ECO:0000269|PubMed:20595392}. PTM: Autophosphorylated. Phosphorylation at Ser-206 is required for its activation. Phosphorylated upon IR or UV-induced DNA damage. Phosphorylated by CHEK1 and CHEK2. Interaction with APBB1 down-regulates phosphorylation at Thr-210 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Nucleus speckle {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. Note=Co- localizes with APBB1 at the nuclear speckles. Colocalizes with PIN1 in the nucleus. Colocalizes with ATF4, CIR1, ARHGAP33, ANKRA2, CDC42, NEK9, RAD26L, RBBP6, RPS7, TRIP4, RELB and PHF1 in the centrosome. Localizes to spindle microtubules in metaphase and anaphase and to the midbody during cytokinesis (By similarity). {ECO:0000250}. SUBUNIT: Interacts with NEK9, predominantly in mitosis. Interacts with KIF11 (via C-terminus). Interacts with APBB1 (via WW domain). Interacts with ANKRA2, ATF4, ARHGAP33, CDC42, CIR1, PRAM1, PTN, PRDX3, PIN1, RAD26L, RBBP6, RPS7, RPS6KB1 and TRIP4 (By similarity). Interacts with STAT3. {ECO:0000250, ECO:0000269|PubMed:20595392}. DOMAIN: Displays an autoinhibited conformation: Tyr-108 side chain points into the active site, interacts with the activation loop, and blocks the alphaC helix. The autoinhibitory conformation is released upon binding with NEK9 (By similarity). {ECO:0000250}. +Q8BWW9 PKN2_MOUSE Serine/threonine-protein kinase N2 (EC 2.7.11.13) (PKN gamma) (Protein kinase C-like 2) (Protein-kinase C-related kinase 2) 983 111,607 Active site (1); Alternative sequence (3); Binding site (1); Chain (1); Domain (6); Modified residue (15); Mutagenesis (4); Nucleotide binding (1); Region (3); Sequence conflict (5); Site (2) FUNCTION: PKC-related serine/threonine-protein kinase and Rho/Rac effector protein that participates in specific signal transduction responses in the cell. Plays a role in the regulation of cell cycle progression, actin cytoskeleton assembly, cell migration, cell adhesion, tumor cell invasion and transcription activation signaling processes. Phosphorylates CTTN in hyaluronan-induced astrocytes and hence decreases CTTN ability to associate with filamentous actin. Phosphorylates HDAC5, therefore lead to impair HDAC5 import. Direct RhoA target required for the regulation of the maturation of primordial junctions into apical junction formation in bronchial epithelial cells. Required for G2/M phases of the cell cycle progression and abscission during cytokinesis in a ECT2-dependent manner. Stimulates FYN kinase activity that is required for establishment of skin cell-cell adhesion during keratinocytes differentiation. Regulates epithelial bladder cells speed and direction of movement during cell migration and tumor cell invasion. Inhibits Akt pro-survival-induced kinase activity. Mediates Rho protein-induced transcriptional activation via the c-fos serum response factor (SRF). Involved in the negative regulation of ciliogenesis (By similarity). {ECO:0000250|UniProtKB:Q16513, ECO:0000269|PubMed:17403031, ECO:0000269|PubMed:20974804, ECO:0000269|PubMed:8910519}. PTM: Phosphorylated during mitosis (By similarity). Autophosphorylated. Phosphorylated. Phosphorylated by CDK10 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q16513}.; PTM: Activated by limited proteolysis with trypsin. Proteolytically cleaved by caspase-3 during the induction of apoptotic cell death. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9121475}. Nucleus {ECO:0000250|UniProtKB:Q16513}. Membrane {ECO:0000269|PubMed:9121475}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q16513}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q16513}. Cleavage furrow {ECO:0000250|UniProtKB:Q16513}. Midbody {ECO:0000250|UniProtKB:Q16513}. Cell junction {ECO:0000250|UniProtKB:Q16513}. Note=Colocalizes with PTPN13 in lamellipodia-like structures, regions of large actin turnover. Accumulates during telophase at the cleavage furrow and concentrates finally around the midbody in cytokinesis. Recruited to nascent cell-cell contacts at the apical surface of cells. {ECO:0000250|UniProtKB:Q16513}. SUBUNIT: Interacts (via the REM repeats) with RHOA (GTP-bound form preferentially) and interacts (via the REM repeats) with RAC1 (GTP-bound form preferentially); the interactions induce its autophosphorylation (PubMed:17403031, PubMed:20974804). Interacts with NCK1 (via SH3 domains) (PubMed:8910519). Interacts with RHOC. Interacts with NCK1 and NCK2 (By similarity). Interacts with CD44 (PubMed:17403031). Interacts (via C-terminal kinase domain) with PDPK1; the interaction stimulates PDPK1 kinase activity (By similarity). Interacts with MAP3K2; the interaction activates PRK2 kinase activity in a MAP3K2-independent kinase activity (PubMed:10818102). Interacts (via C-terminal domain) with AKT1; the interaction occurs with the C-terminal cleavage product of PRK2 in apoptotic cells. Interacts (via C-terminus) with PTPN13 (via PDZ 3 domain). Interacts with CDK10 (By similarity). {ECO:0000250|UniProtKB:Q16513, ECO:0000269|PubMed:10818102, ECO:0000269|PubMed:17403031, ECO:0000269|PubMed:20974804, ECO:0000269|PubMed:8910519}. DOMAIN: The N-terminal regioninterferes with the interaction between AKT1 and the C-terminal regionof PKN2. {ECO:0000250}.; DOMAIN: The C1 domain does not bind the diacylglycerol (DAG).; DOMAIN: The apoptotic C-terminal cleavage product inhibits EGF-induced kinase activity of AKT1 phosphorylation at 'Thr-308' and 'Ser-473' sites, PDPK1 autophosphorylation and kinases PRKCD and PRKCZ phosphorylations. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. Highly expressed in liver and lung Expressed in astrocytes (at protein level). Ubiquitous. {ECO:0000269|PubMed:11777936, ECO:0000269|PubMed:17403031, ECO:0000269|PubMed:8910519, ECO:0000269|PubMed:9121475}. +P08553 NFM_MOUSE Neurofilament medium polypeptide (NF-M) (160 kDa neurofilament protein) (Neurofilament 3) (Neurofilament triplet M protein) 848 95,916 Chain (1); Domain (1); Glycosylation (2); Initiator methionine (1); Modified residue (28); Region (9); Sequence conflict (12) FUNCTION: Neurofilaments usually contain three intermediate filament proteins: L, M, and H which are involved in the maintenance of neuronal caliber. PTM: There are a number of repeats of the tripeptide K-S-P, NFM is phosphorylated on a number of the serines in this motif. It is thought that phosphorylation of NFM results in the formation of interfilament cross bridges that are important in the maintenance of axonal caliber.; PTM: Phosphorylation seems to play a major role in the functioning of the larger neurofilament polypeptides (NF-M and NF-H), the levels of phosphorylation being altered developmentally and coincidentally with a change in the neurofilament function.; PTM: Phosphorylated in the head and rod regions by the PKC kinase PKN1, leading to the inhibition of polymerization. {ECO:0000250}. +Q02257 PLAK_MOUSE Junction plakoglobin (Desmoplakin III) (Desmoplakin-3) 745 81,801 Chain (1); Glycosylation (1); Modified residue (6); Region (2); Repeat (12) FUNCTION: Common junctional plaque protein. The membrane-associated plaques are architectural elements in an important strategic position to influence the arrangement and function of both the cytoskeleton and the cells within the tissue. The presence of plakoglobin in both the desmosomes and in the intermediate junctions suggests that it plays a central role in the structure and function of submembranous plaques. Acts as a substrate for VE-PTP and is required by it to stimulate VE-cadherin function in endothelial cells. Can replace beta-catenin in E-cadherin/catenin adhesion complexes which are proposed to couple cadherins to the actin cytoskeleton. {ECO:0000269|PubMed:19015309}. PTM: May be phosphorylated by FER. {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, adherens junction. Cell junction, desmosome. Cytoplasm, cytoskeleton. Membrane; Peripheral membrane protein. Note=Cytoplasmic in a soluble and membrane-associated form. SUBUNIT: Homodimer. Component of an E-cadherin/catenin adhesion complex composed of at least E-cadherin/CDH1 and gamma-catenin/JUP, and possibly alpha-catenin/CTNNA1; the complex is located to adherens junctions. The stable association of CTNNA1 is controversial as CTNNA1 was shown not to bind to F-actin when assembled in the complex. Interacts with MUC1. Interacts with CAV1. Interacts with PTPRJ. Interacts with DSG1. Interacts with DSC1 and DSC2. Interacts with PKP2 (By similarity). {ECO:0000250}. DOMAIN: The entire ARM repeats region mediates binding to CDH1/E-cadherin. The N-terminus and first three ARM repeats are sufficient for binding to DSG1. The N-terminus and first ARM repeat are sufficient for association with CTNNA1. DSC1 association requires both ends of the ARM repeat region (By similarity). {ECO:0000250}. +Q9CRB2 NHP2_MOUSE H/ACA ribonucleoprotein complex subunit 2 (Nucleolar protein family A member 2) (snoRNP protein NHP2) 153 17,247 Chain (1); Cross-link (4); Modified residue (1) "FUNCTION: Required for ribosome biogenesis and telomere maintenance. Part of the H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Each rRNA can contain up to 100 pseudouridine (""psi"") residues, which may serve to stabilize the conformation of rRNAs. May also be required for correct processing or intranuclear trafficking of TERC, the RNA component of the telomerase reverse transcriptase (TERT) holoenzyme (By similarity). {ECO:0000250}." SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Nucleus, Cajal body {ECO:0000250}. Note=Also localized to Cajal bodies (coiled bodies). {ECO:0000250}. SUBUNIT: Part of the H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which contains NHP2/NOLA2, GAR1/NOLA1, NOP10/NOLA3, and DKC1/NOLA4, which is presumed to be the catalytic subunit. The complex contains a stable core formed by binding of one or two NOP10-DKC1 heterodimers to NHP2; GAR1 subsequently binds to this core via DKC1. The complex binds a box H/ACA small nucleolar RNA (snoRNA), which may target the specific site of modification within the RNA substrate. During assembly, the complex contains NAF1 instead of GAR1/NOLA1. The complex also interacts with TERC, which contains a 3'-terminal domain related to the box H/ACA snoRNAs. Specific interactions with snoRNAs or TERC are mediated by GAR1 and NHP2. Associates with NOLC1/NOPP140. H/ACA snoRNPs interact with the SMN complex, consisting of SMN1 or SMN2, GEMIN2/SIP1, DDX20/GEMIN3, and GEMIN4. This is mediated by interaction between GAR1 and SMN1 or SMN2. The SMN complex may be required for correct assembly of the H/ACA snoRNP complex. Component of the telomerase holoenzyme complex composed of one molecule of TERT, one molecule of WRAP53/TCAB1, two molecules of H/ACA ribonucleoprotein complex subunits DKC1, NOP10, NHP2 and GAR1, and a telomerase RNA template component (TERC). The telomerase holoenzyme complex is associated with TEP1, SMG6/EST1A and POT1. {ECO:0000250|UniProtKB:Q9NX24}. +Q9EQ80 NIF3L_MOUSE NIF3-like protein 1 376 41,746 Chain (1); Modified residue (3); Region (1); Sequence conflict (7) FUNCTION: May function as a transcriptional corepressor through its interaction with COPS2, negatively regulating the expression of genes involved in neuronal differentiation. {ECO:0000269|PubMed:12522100}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12522100}. Nucleus {ECO:0000269|PubMed:12522100}. Note=Interaction with COPS2 may regulate localization to the nucleus. {ECO:0000269|PubMed:12522100}. SUBUNIT: Homodimer (By similarity). Interacts with COPS2 (PubMed:12522100). Interacts with THOC7 (PubMed:12951069). {ECO:0000250|UniProtKB:Q9GZT8, ECO:0000269|PubMed:12522100, ECO:0000269|PubMed:12951069}. TISSUE SPECIFICITY: Ubiquitous. Detected in all tissues tested with higher expression in cerebellum, heart and kidney and to a lower level in cerebrum, lung, liver, spleen and muscle. {ECO:0000269|PubMed:11124544, ECO:0000269|PubMed:12522100}. +Q99MJ6 NHRF4_MOUSE Na(+)/H(+) exchange regulatory cofactor NHE-RF4 (NHERF-4) (Natrium-phosphate cotransporter IIa C-terminal-associated protein 2) (Na/Pi cotransporter C-terminal-associated protein 2) (NaPi-Cap2) (PDZ domain-containing protein 2) (PDZ domain-containing protein 3) (Sodium-hydrogen exchanger regulatory factor 4) 498 53,525 Chain (1); Domain (4); Sequence conflict (1) FUNCTION: Acts as a regulatory protein that associates with GUCY2C and negatively modulates its heat-stable enterotoxin-mediated activation (By similarity). Stimulates SLC9A3 activity in the presence of elevated calcium ions (By similarity). {ECO:0000250|UniProtKB:Q86UT5}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:26756164}; Peripheral membrane protein {ECO:0000305|PubMed:26756164}. Cytoplasm {ECO:0000269|PubMed:26756164}. Note=In kidney, predominantly localized to the subapical compartment of proximal tubular cells (PubMed:11099500). In intestinal epithelial cells, localizes to the ileal brush border and in a juxtanuclear compartment (PubMed:19088451). Expressed in the membrane, with relatively low expression in the cytoplasm (PubMed:26756164). {ECO:0000269|PubMed:11099500, ECO:0000269|PubMed:19088451, ECO:0000269|PubMed:26756164}. SUBUNIT: Interacts with the C-terminal region of GUCY2C (By similarity). Interacts with C-terminal region of SLC9A3 and the interactions decrease in response to elevated calcium ion levels (By similarity). Interacts with the C-terminal region of SLC34A1 (PubMed:11099500). Interacts with USP2 isoform 2 (PubMed:26756164). {ECO:0000250|UniProtKB:Q86UT5, ECO:0000269|PubMed:11099500, ECO:0000269|PubMed:26756164}. TISSUE SPECIFICITY: Expressed in kidney and small intestine. Not detected in heart, brain, spleen, lung, liver, skeletal muscle or testis. {ECO:0000269|PubMed:11099500}. +Q9CXK8 NIP7_MOUSE 60S ribosome subunit biogenesis protein NIP7 homolog (PEachy) (kDa93) 180 20,452 Chain (1); Domain (1); Region (2); Sequence conflict (1) FUNCTION: Required for proper 34S pre-rRNA processing and 60S ribosome subunit assembly. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. SUBUNIT: Monomer. Interacts with pre-ribosome complex. May bind to RNA. Interacts with NOL8. Interacts with FTSJ3 (By similarity). {ECO:0000250}. +Q9JHK5 PLEK_MOUSE Pleckstrin 350 39,901 Beta strand (6); Chain (1); Domain (3); Helix (4); Modified residue (3); Sequence conflict (2); Turn (1) FUNCTION: Major protein kinase C substrate of platelets. +Q61043 NIN_MOUSE Ninein 2113 243,718 Alternative sequence (6); Chain (1); Coiled coil (7); Domain (5); Erroneous initiation (2); Modified residue (4); Nucleotide binding (3); Region (1); Sequence conflict (31) FUNCTION: Centrosomal protein required for the positioning and anchorage of the microtubule minus-end in epithelial cells (PubMed:15784680, PubMed:10934040). May also act as a centrosome maturation factor (By similarity). May play a role in microtubule nucleation, by recruiting the gamma-tubulin ring complex to the centrosome (PubMed:15784680). Overexpression does not perturb nucleation or elongation of microtubules but suppresses release of microtubules (By similarity). Required for centriole organization and microtubule anchoring at the mother centriole (By similarity). {ECO:0000250|UniProtKB:Q8N4C6, ECO:0000269|PubMed:10934040, ECO:0000269|PubMed:15784680}. PTM: Phosphorylated by AURKA/Aurora kinase A and PKA kinases but not CK2 or AURKB/Aurora kinase B. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:27565344, ECO:0000269|PubMed:8834802}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:15784680}. Note=Component of the core centrosome. Arranged in a tubular conformation with an open and a closed end within the centrosome. In the mother centrosome, it localizes at both ends of the centrosome tube, including the site of centrosome duplication, while in the daughter centrosome it is present only at the closed end. Requires PCM1 for centrosome localization. Localizes to the subdistal appendage region of the centriole in a DCTN1-dependent manner. {ECO:0000250|UniProtKB:Q8N4C6}.; SUBCELLULAR LOCATION: Isoform 4: Cytoplasm {ECO:0000269|PubMed:27565344}. Note=Seems to have a dominant-negative effect on localization of other isoforms, promoting their dissociation from the centrosome. {ECO:0000269|PubMed:27565344}. SUBUNIT: Homooligomer (By similarity). Interacts with GSK3B/GSK3-beta via its C-terminal domain (By similarity). Interacts with C14ORF166, such interaction may prevent its phosphorylation by GSK3B (By similarity). Interacts with AUNIP (via N-terminus) (By similarity). Identified in a complex with AUNIP and AURKA (By similarity). Interacts with CCDC120 (By similarity). Interacts (via C-terminus) with CEP250 (PubMed:27565344). Interacts with CEP170 (PubMed:27565344). Interacts (via N-terminus) with the gamma-tubulin ring complex component TUBGCP3 (PubMed:15784680). Interacts with gamma-tubulin (PubMed:15784680). Isoform 4 does not interact with CEP170 or CEP250 (PubMed:27565344). {ECO:0000250|UniProtKB:Q8N4C6, ECO:0000269|PubMed:15784680, ECO:0000269|PubMed:27565344}. DOMAIN: There is conflicting information regarding the regions required for centrosomal localization (PubMed:15784680). One study shows that the region 1591-1671 is necessary and sufficient for targeting to the centrosome (By similarity). Another study shows that a separate region within the coiled-coil domain, 1279-1565, is important for centrosomal localization (By similarity). However, a third study shows that the coiled-coil region (373-1874) is not sufficient for centrosomal localization and instead localizes to cytoplasmic speckles (PubMed:15784680). The observed differences might be due to oligomerization of the longer coiled-coil domain-containing sequence, which would mask the shorter centrosomal targeting sequences (PubMed:15784680). {ECO:0000250|UniProtKB:Q8N4C6, ECO:0000269|PubMed:15784680}.; DOMAIN: The N-terminal domain is important for targeting to the mother centriole, although it is not sufficient by itself for centrosomal localization. {ECO:0000269|PubMed:8834802}. TISSUE SPECIFICITY: Widely expressed. Highly expressed in spleen, bone marrow and skin. Weakly expressed in liver and small intestine. Expressed in brain. {ECO:0000269|PubMed:8834802}. +Q99MA9 NKX61_MOUSE Homeobox protein Nkx-6.1 (Homeobox protein NK-6 homolog A) 365 37,705 Chain (1); Compositional bias (5); DNA binding (1); Modified residue (1); Region (2) FUNCTION: Transcription factor which binds to specific A/T-rich DNA sequences in the promoter regions of a number of genes. Required for the development of insulin-producing beta cells in the islets of Langerhans at the secondary transition (PubMed:11076772). Involved in transcriptional regulation of the insulin gene. Together with NKX2-2 and IRX3, restricts the generation of motor neurons to the appropriate region of the neural tube. Belongs to the class II proteins of neuronal progenitor factors, which are induced by SHH signals. {ECO:0000269|PubMed:10830170, ECO:0000269|PubMed:11076772}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11076772}. DOMAIN: The C-terminal domain contributes to sequence-specific DNA-binding. TISSUE SPECIFICITY: Expressed by neuronal progenitor cells in discrete domains of the ventral neural tube (PubMed:10830170). In the pancreas, expressed exclusively in insulin-producing beta cells of the islets of Langerhans (at protein level) (PubMed:11076772). {ECO:0000269|PubMed:10830170, ECO:0000269|PubMed:11076772}. +Q8K3Z0 NOD2_MOUSE Nucleotide-binding oligomerization domain-containing protein 2 (Caspase recruitment domain-containing protein 15) 1020 113,562 Alternative sequence (2); Chain (1); Domain (3); Erroneous initiation (1); Motif (1); Natural variant (7); Region (1); Repeat (10) FUNCTION: Involved in gastrointestinal immunity. Upon stimulation by muramyl dipeptide (MDP), a fragment of bacterial peptidoglycan, binds the proximal adapter receptor-interacting RIPK2, which recruits ubiquitin ligases as XIAP, BIRC2, BIRC3, INAVA and the LUBAC complex, triggering activation of MAP kinases and activation of NF-kappa-B signaling. This in turn leads to the transcriptional activation of hundreds of genes involved in immune response (PubMed:22607974). Required for MDP-induced NLRP1-dependent CASP1 activation and IL1B release in macrophages (PubMed:18511561). Component of an autophagy-mediated antibacterial pathway together with ATG16L1. Plays also a role in sensing single-stranded RNA (ssRNA) from viruses. Interacts with mitochondrial antiviral signaling/MAVS, leading to activation of interferon regulatory factor-3/IRF3 and expression of type I interferon. {ECO:0000250|UniProtKB:Q9HC29, ECO:0000269|PubMed:18511561, ECO:0000269|PubMed:22607974}. PTM: Polyubiquitinated following MDP stimulation, leading to proteasome-mediated degradation. {ECO:0000250|UniProtKB:Q9HC29}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9HC29}. Membrane {ECO:0000250|UniProtKB:Q9HC29}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q9HC29}. SUBUNIT: Component of a signaling complex consisting of ARHGEF2, NOD2 and RIPK2. Interacts (via CARD domain) with RIPK2 (via CARD domain). Interacts with ATG16L1. Interacts (via NACHT domain) with CARD9 (PubMed:17187069). Interacts with ANKRD17 (via N-terminus). Interacts with HSPA1A; the interaction enhances NOD2 stability. Interacts (via both CARD domains) with HSP90; the interaction enhances NOD2 stability (PubMed:23019338). Interacts (via CARD domain) with SOCS3; the interaction promotes NOD2 degradation. Interacts (via CARD domain) with ERBBI2P; the interaction inhibits activation of NOD2 (PubMed:16203728). Interacts (via CARD domain) with CASP1; this interaction leads to IL1B processing (PubMed:18511561). Also interacts with CASP4. Interacts with NLRP1; this interaction is enhanced in the presence of muramyl dipeptide (MDP) and leads to increased IL1B release. Interacts with MAPKBP1; the interaction is enhanced in the presence of muramyl dipeptide (MDP). Interacts with INAVA; the interaction takes place upon PRR stimulation. Interacts with ANKHD1, C10ORF67, CHMP5, DOCK7, ENTR1, KRT15, LDOC1, PPP1R12C, PPP2R3B, TRIM41 and VIM (By similarity). {ECO:0000250|UniProtKB:Q9HC29, ECO:0000269|PubMed:16203728, ECO:0000269|PubMed:17187069, ECO:0000269|PubMed:18511561, ECO:0000269|PubMed:23019338}. DOMAIN: The ATG16L1-binding motif mediates interaction with ATG16L1. {ECO:0000250}.; DOMAIN: Intramolecular interactions between the N-terminal moiety and the leucine-rich repeats (LRR) may be important for autoinhibition in the absence of activating signal. In the absence of LRRs, the protein becomes a constitutive activator of CASP1 cleavage and proIL1B processing. {ECO:0000250|UniProtKB:Q9HC29}. +P51860 NP1L2_MOUSE Nucleosome assembly protein 1-like 2 (Brain-specific protein, X-linked) 460 52,158 Chain (1); Compositional bias (1); Motif (1); Sequence conflict (1) FUNCTION: Acidic protein which may be involved in interactions with other proteins or DNA. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: Brain, specifically expressed in neurons. +P29477 NOS2_MOUSE Nitric oxide synthase, inducible (EC 1.14.13.39) (Inducible NO synthase) (Inducible NOS) (iNOS) (Macrophage NOS) (MAC-NOS) (NOS type II) (Peptidyl-cysteine S-nitrosylase NOS2) 1144 130,575 Beta strand (19); Chain (1); Domain (2); Helix (24); Metal binding (3); Modified residue (1); Motif (1); Mutagenesis (6); Natural variant (3); Nucleotide binding (5); Region (1); Sequence conflict (8); Turn (4) FUNCTION: Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body (PubMed:7503239). In macrophages, NO mediates tumoricidal and bactericidal actions. Also has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such PTGS2/COX2 (PubMed:16373578). As component of the iNOS-S100A8/9 transnitrosylase complex involved in the selective inflammatory stimulus-dependent S-nitrosylation of GAPDH implicated in regulation of the GAIT complex activity and probably multiple targets including ANXA5, EZR, MSN and VIM (By similarity). Involved in inflammation, enhances the synthesis of proinflammatory mediators such as IL6 and IL8 (By similarity). {ECO:0000250|UniProtKB:P35228, ECO:0000250|UniProtKB:P79290, ECO:0000269|PubMed:16373578, ECO:0000269|PubMed:7503239}. PTM: Polyubiquitinated; mediated by SPSB1, SPSB2 and SPSB4, leading to proteasomal degradation. {ECO:0000269|PubMed:20603330, ECO:0000269|PubMed:21199876}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P35228}. Note=Localizes as discrete foci scattered throughout the cytosol and in the presence of SPSB1 and SPSB4, exhibits a more diffuse cytosolic localization. {ECO:0000250|UniProtKB:P35228}. SUBUNIT: Homodimer (PubMed:10769116, PubMed:11669619). Interacts with SLC9A3R1 (By similarity). Interacts with GAPDH (By similarity). Interacts with S100A8 and S100A9 to form the iNOS-S100A8/9 transnitrosylase complex (By similarity). Interacts with SPSB1, SPSB2 and SPSB4 (PubMed:20603330). Interacts with ELOC and CUL5 in the presence of SPSB1 or SPSB2 or SPSB4 (By similarity). {ECO:0000250|UniProtKB:P35228, ECO:0000269|PubMed:10769116, ECO:0000269|PubMed:11669619, ECO:0000269|PubMed:20603330}. TISSUE SPECIFICITY: Macrophages. +Q9Z0J0 NPC2_MOUSE NPC intracellular cholesterol transporter 2 (Epididymal secretory protein E1) (mE1) (Niemann Pick type C2 protein homolog) 149 16,442 Chain (1); Disulfide bond (3); Glycosylation (2); Modified residue (1); Mutagenesis (16); Signal peptide (1) FUNCTION: Intracellular cholesterol transporter which acts in concert with NPC1 and plays an important role in the egress of cholesterol from the lysosomal compartment (PubMed:12591949, PubMed:17018531, PubMed:21315718, PubMed:26296895). Unesterified cholesterol that has been released from LDLs in the lumen of the late endosomes/lysosomes is transferred by NPC2 to the cholesterol-binding pocket in the N-terminal domain of NPC1. May bind and mobilize cholesterol that is associated with membranes. NPC2 binds cholesterol with a 1:1 stoichiometry. Can bind a variety of sterols, including lathosterol, desmosterol and the plant sterols stigmasterol and beta-sitosterol (By similarity). The secreted form of NCP2 regulates biliary cholesterol secretion via stimulation of ABCG5/ABCG8-mediated cholesterol transport (PubMed:21315718). {ECO:0000250|UniProtKB:P61916, ECO:0000269|PubMed:12591949, ECO:0000269|PubMed:17018531, ECO:0000269|PubMed:21315718, ECO:0000269|PubMed:26296895}. PTM: N-glycosylated. {ECO:0000269|PubMed:10863096}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10863096, ECO:0000269|PubMed:12591949, ECO:0000269|PubMed:21315718}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P61916}. Lysosome {ECO:0000250|UniProtKB:P61916}. Note=Interaction with cell-surface M6PR mediates endocytosis and targeting to lysosomes. {ECO:0000305|PubMed:12591949}. SUBUNIT: Interacts with NPC1 (via the second lumenal domain) in a cholestrol-dependent manner. Interacts with NUS1/NgBR, the interaction stabilizes NCP2 and regulates cholesterol trafficking. Interacts with DHDDS. Interacts with NEDD4L (via C2 domain). Interacts with NPC1L1. {ECO:0000250|UniProtKB:P61916}. DOMAIN: Binds cholesterol in a hydrophobic pocket; there are no hydrogen bonds between the sterol and the protein. {ECO:0000250|UniProtKB:P79345}. TISSUE SPECIFICITY: Detected in liver and bile (PubMed:21315718). Detected in epididymis (at protein level). Detected in caput epididymis, corpus epididymis, cauda epididymis and ovary (PubMed:10863096). {ECO:0000269|PubMed:10863096, ECO:0000269|PubMed:21315718}. +Q8BJ52 PLPR5_MOUSE Phospholipid phosphatase-related protein type 5 (EC 3.1.3.-) (Lipid phosphate phosphatase-related protein type 5) (Plasticity-related gene 5 protein) (PRG-5) 321 35,388 Alternative sequence (1); Chain (1); Sequence conflict (2); Transmembrane (6) TRANSMEM 6 26 Helical. {ECO:0000255}.; TRANSMEM 62 82 Helical. {ECO:0000255}.; TRANSMEM 122 142 Helical. {ECO:0000255}.; TRANSMEM 196 213 Helical. {ECO:0000255}.; TRANSMEM 225 245 Helical. {ECO:0000255}.; TRANSMEM 252 272 Helical. {ECO:0000255}. FUNCTION: Induces filopodia formation and promotes neurite growth in a CDC42-independent manner; impedes neurite growth inhibitory-mediated axonal retraction. {ECO:0000269|PubMed:20032306}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20032306}; Multi-pass membrane protein {ECO:0000305}. +O35604 NPC1_MOUSE NPC intracellular cholesterol transporter 1 (Niemann-Pick C1 protein) 1277 142,885 Binding site (2); Chain (1); Compositional bias (1); Disulfide bond (15); Domain (1); Glycosylation (16); Motif (1); Mutagenesis (8); Region (2); Sequence conflict (6); Signal peptide (1); Site (1); Topological domain (14); Transmembrane (13) TRANSMEM 270 290 Helical. {ECO:0000255}.; TRANSMEM 351 371 Helical. {ECO:0000255}.; TRANSMEM 622 642 Helical. {ECO:0000255}.; TRANSMEM 654 674 Helical. {ECO:0000255}.; TRANSMEM 684 704 Helical. {ECO:0000255}.; TRANSMEM 731 751 Helical. {ECO:0000255}.; TRANSMEM 760 780 Helical. {ECO:0000255}.; TRANSMEM 833 853 Helical. {ECO:0000255}.; TRANSMEM 1098 1118 Helical. {ECO:0000255}.; TRANSMEM 1124 1144 Helical. {ECO:0000255}.; TRANSMEM 1146 1166 Helical. {ECO:0000255}.; TRANSMEM 1195 1215 Helical. {ECO:0000255}.; TRANSMEM 1227 1247 Helical. {ECO:0000255}. TOPO_DOM 23 269 Lumenal. {ECO:0000305}.; TOPO_DOM 291 350 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 372 621 Lumenal. {ECO:0000305}.; TOPO_DOM 643 653 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 675 683 Lumenal. {ECO:0000305}.; TOPO_DOM 705 730 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 752 759 Lumenal. {ECO:0000305}.; TOPO_DOM 781 832 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 854 1097 Lumenal. {ECO:0000305}.; TOPO_DOM 1119 1123 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1145 1145 Lumenal. {ECO:0000305}.; TOPO_DOM 1167 1194 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1216 1226 Lumenal. {ECO:0000305}.; TOPO_DOM 1248 1277 Cytoplasmic. {ECO:0000305}. FUNCTION: Intracellular cholesterol transporter which acts in concert with NPC2 and plays an important role in the egress of cholesterol from the endosomal/lysosomal compartment (PubMed:21896731, PubMed:22048958, PubMed:27551080). Unesterified cholesterol that has been released from LDLs in the lumen of the late endosomes/lysosomes is transferred by NPC2 to the cholesterol-binding pocket in the N-terminal domain of NPC1. Cholesterol binds to NPC1 with the hydroxyl group buried in the binding pocket (By similarity). May play a role in vesicular trafficking in glia, a process that may be crucial for maintaining the structural and functional integrity of nerve terminals (Probable). {ECO:0000250|UniProtKB:O15118, ECO:0000269|PubMed:21896731, ECO:0000269|PubMed:22048958, ECO:0000269|PubMed:27551080, ECO:0000305}. PTM: N-glycosylated. {ECO:0000269|PubMed:21896731, ECO:0000269|PubMed:22065762}. SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250|UniProtKB:O15118}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O15118}. Lysosome membrane {ECO:0000269|PubMed:21896731, ECO:0000269|PubMed:22065762, ECO:0000269|PubMed:27551080}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O15118}. SUBUNIT: Interacts (via the second lumenal domain) with NPC2 (PubMed:22065762, PubMed:27551080). Interacts with TMEM97. Interacts with TIM1 (By similarity). {ECO:0000250|UniProtKB:O15118, ECO:0000269|PubMed:22065762, ECO:0000269|PubMed:27551080}. DOMAIN: A cysteine-rich N-terminal domain and a C-terminal domain containing a di-leucine motif necessary for lysosomal targeting are critical for mobilization of cholesterol from lysosomes. {ECO:0000250|UniProtKB:O15118}. TISSUE SPECIFICITY: Detected in liver (at protein level) (PubMed:21896731, PubMed:22048958). Ubiquitous (PubMed:9211850). Detected in adult heart, spleen, lung, liver, skeletal muscle, kidney, testis (PubMed:9211850). {ECO:0000269|PubMed:21896731, ECO:0000269|PubMed:22048958, ECO:0000269|PubMed:9211850}. DISEASE: Note=Defects in Npc1 cause a lysosomal storage disorder characterized by accumulation of cholesterol in lysosomes and impaired cholesterol homeostasis. Causes age-dependent loss of Purkinje cells, loss of body weight and leads then to ataxia and premature death at a median age of 72 days. {ECO:0000269|PubMed:22048958, ECO:0000269|PubMed:9211850}. +Q9DCW2 PLS2_MOUSE Phospholipid scramblase 2 (PL scramblase 2) (Ca(2+)-dependent phospholipid scramblase 2) 307 34,052 Chain (1); Compositional bias (1); Lipidation (4); Modified residue (1); Motif (2); Region (1); Sequence conflict (5); Topological domain (2); Transmembrane (1) TRANSMEM 287 303 Helical. {ECO:0000255}. TOPO_DOM 1 286 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 304 307 Extracellular. {ECO:0000250}. FUNCTION: May mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions that results in a loss of phospholipid asymmetry in the plasma membrane. May play a central role in the initiation of fibrin clot formation, in the activation of mast cells and in the recognition of apoptotic and injured cells by the reticuloendothelial system. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. DOMAIN: The N-terminal proline-rich domain (PRD) is required for phospholipid scramblase activity. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in erythrocyte membranes, blood platelets, blood leukocytes, T- and B-lymphocytes, vascular endothelium, spleen, thymus, prostate, testis, uterus, intestine and colon. +Q924H0 NPFF2_MOUSE Neuropeptide FF receptor 2 (G-protein coupled receptor 74) (Neuropeptide NPFF receptor) 417 47,449 Chain (1); Disulfide bond (1); Glycosylation (4); Sequence conflict (3); Topological domain (8); Transmembrane (7) TRANSMEM 46 66 Helical; Name=1. {ECO:0000255}.; TRANSMEM 83 103 Helical; Name=2. {ECO:0000255}.; TRANSMEM 120 140 Helical; Name=3. {ECO:0000255}.; TRANSMEM 161 181 Helical; Name=4. {ECO:0000255}.; TRANSMEM 218 238 Helical; Name=5. {ECO:0000255}.; TRANSMEM 275 295 Helical; Name=6. {ECO:0000255}.; TRANSMEM 311 331 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 45 Extracellular. {ECO:0000255}.; TOPO_DOM 67 82 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 104 119 Extracellular. {ECO:0000255}.; TOPO_DOM 141 160 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 182 217 Extracellular. {ECO:0000255}.; TOPO_DOM 239 274 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 296 310 Extracellular. {ECO:0000255}.; TOPO_DOM 332 417 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for NPAF (A-18-F-amide) and NPFF (F-8-F-amide) neuropeptides, also known as morphine-modulating peptides. Can also be activated by a variety of naturally occurring or synthetic FMRF-amide like ligands. This receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q9WVA8 NPFF_MOUSE Pro-FMRFamide-related neuropeptide FF (FMRFamide-related peptides) [Cleaved into: Neuropeptide SF (NPSF); Neuropeptide FF (NPFF); Neuropeptide AF-like (NPAF)] 114 13,012 Modified residue (2); Peptide (3); Propeptide (2); Signal peptide (1) FUNCTION: Morphine modulating peptides. Have wide-ranging physiologic effects, including the modulation of morphine-induced analgesia, elevation of arterial blood pressure, and increased somatostatin secretion from the pancreas. Neuropeptide FF potentiates and sensitizes ASIC1 and ASIC3 channels. {ECO:0000269|PubMed:10798398}. SUBCELLULAR LOCATION: Secreted. +P59240 NPHP4_MOUSE Nephrocystin-4 (Nephroretinin) 1425 157,269 Chain (1); Modified residue (1); Region (1) FUNCTION: Involved in the organization of apical junctions; the function is proposed to implicate a NPHP1-4-8 module. Does not seem to be strictly required for ciliogenesis (By similarity). Required for building functional cilia. Involved in the organization of the subapical actin network in multiciliated epithelial cells. Seems to recruit INT to basal bodies of motile cilia which subsequently interacts with actin-modifying proteins such as DAAM1 (By similarity). In cooperation with INVS may downregulate the canonical Wnt pathway and promote the Wnt-PCP pathway by regulating expression and subcellular location of disheveled proteins. Stabilizes protein levels of JADE1 and promotes its translocation to the nucleus leading to cooperative inhibition of canonical Wnt signaling (By similarity). Acts as negative regulator of the hippo pathway by association with LATS1 and modifying LATS1-dependent phosphorylation and localization of WWTR1/TAZ (By similarity). {ECO:0000250|UniProtKB:B0DOB4, ECO:0000250|UniProtKB:O75161}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:21565611}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cell junction, tight junction {ECO:0000269|PubMed:21565611}. Note=In cultured renal cells, it localizes diffusely in the cytoplasm but, as cells approach confluence, it accumulates to basolateral tight junctions. Localizes to the ciliary transition zone. {ECO:0000250|UniProtKB:O75161, ECO:0000269|PubMed:21565611}. SUBUNIT: Interacts with NPHP1 and RPGRIP1L/NPHP8; NPHP1, NPHP4 and RPGRIP1L are proposed to form a functional NPHP1-4-8 module localized to cell-cell contacts and the ciliary transition zone; NPHP4 mediates the interaction between NPHP1 and RPGRIP1L. Interacts with IQCB1/NPHP5; the interaction likely requires additional interactors (PubMed:21565611). Interacts with RPGRIP1, CEP164, JADE1, MPP5, INADL, PARD6A, INVS, DVL2. Interacts with INTU; INTU mediates the interaction between NPHP4 and DAAM1. Interacts with JADE1 (By similarity). {ECO:0000250|UniProtKB:O75161, ECO:0000269|PubMed:21565611}. +Q8VIJ8 NPRL3_MOUSE GATOR complex protein NPRL3 (Nitrogen permease regulator 3-like protein) 569 63,618 Chain (1); Modified residue (1) FUNCTION: As a component of the GATOR1 complex functions as an inhibitor of the amino acid-sensing branch of the TORC1 pathway. The GATOR1 complex strongly increases GTP hydrolysis by RRAGA and RRAGB within RRAGC-containing heterodimers, thereby deactivating RRAGs, releasing mTORC1 from lysosomal surface and inhibiting mTORC1 signaling. The GATOR1 complex is negatively regulated by GATOR2 the other GATOR subcomplex in this amino acid-sensing branch of the TORC1 pathway. {ECO:0000250|UniProtKB:Q12980}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q12980}. Note=Localization to lysosomes is amino acid-independent. {ECO:0000250|UniProtKB:Q12980}. SUBUNIT: Forms a heterodimer with NPRL2 (By similarity). Within the GATOR complex, component of the GATOR1 subcomplex, made of DEPDC5, NPRL2 and NPRL3. GATOR1 mediates the strong interaction of the GATOR complex with RRAGA/RRAGC and RRAGB/RRAGC heterodimers (By similarity). {ECO:0000250}. +Q9DBP0 NPT2B_MOUSE Sodium-dependent phosphate transport protein 2B (Sodium-phosphate transport protein 2B) (Na(+)-dependent phosphate cotransporter 2B) (Sodium/phosphate cotransporter 2B) (Na(+)/Pi cotransporter 2B) (NaPi-2b) (Solute carrier family 34 member 2) 697 76,245 Chain (1); Compositional bias (5); Disulfide bond (1); Glycosylation (4); Sequence conflict (3); Topological domain (9); Transmembrane (8) TRANSMEM 92 112 Helical; Name=M1. {ECO:0000255}.; TRANSMEM 137 157 Helical; Name=M2. {ECO:0000255}.; TRANSMEM 214 234 Helical; Name=M3. {ECO:0000255}.; TRANSMEM 364 384 Helical; Name=M4. {ECO:0000255}.; TRANSMEM 409 429 Helical; Name=M5. {ECO:0000255}.; TRANSMEM 487 507 Helical; Name=M6. {ECO:0000255}.; TRANSMEM 527 547 Helical; Name=M7. {ECO:0000255}.; TRANSMEM 552 572 Helical; Name=M8. {ECO:0000255}. TOPO_DOM 1 91 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 113 136 Extracellular. {ECO:0000255}.; TOPO_DOM 158 213 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 235 363 Extracellular. {ECO:0000255}.; TOPO_DOM 385 408 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 430 486 Extracellular. {ECO:0000255}.; TOPO_DOM 508 526 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 548 551 Extracellular. {ECO:0000255}.; TOPO_DOM 573 696 Cytoplasmic. {ECO:0000255}. FUNCTION: May be involved in actively transporting phosphate into cells via Na(+) cotransport. It may be the main phosphate transport protein in the intestinal brush border membrane. May have a role in the synthesis of surfactant in lungs' alveoli. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Highly abundant in the ileum of small intestine, whereas it is almost absent in the duodenum and in the jejunum. {ECO:0000269|PubMed:15701623}. +Q80SU6 NPT2C_MOUSE Sodium-dependent phosphate transport protein 2C (Sodium-phosphate transport protein 2C) (Na(+)-dependent phosphate cotransporter 2C) (Sodium/phosphate cotransporter 2C) (Na(+)/Pi cotransporter 2C) (NaPi-2c) (Solute carrier family 34 member 3) 601 63,939 Chain (1); Compositional bias (1); Disulfide bond (1); Glycosylation (3); Modified residue (1); Mutagenesis (2); Sequence conflict (4); Topological domain (9); Transmembrane (8) TRANSMEM 76 96 Helical; Name=M1. {ECO:0000255}.; TRANSMEM 111 131 Helical; Name=M2. {ECO:0000255}.; TRANSMEM 188 208 Helical; Name=M3. {ECO:0000255}.; TRANSMEM 325 345 Helical; Name=M4. {ECO:0000255}.; TRANSMEM 370 390 Helical; Name=M5. {ECO:0000255}.; TRANSMEM 442 462 Helical; Name=M6. {ECO:0000255}.; TRANSMEM 488 508 Helical; Name=M7. {ECO:0000255}.; TRANSMEM 513 533 Helical; Name=M8. {ECO:0000255}. TOPO_DOM 1 75 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 97 110 Extracellular. {ECO:0000255}.; TOPO_DOM 132 187 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 209 324 Extracellular. {ECO:0000255}.; TOPO_DOM 346 369 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 391 441 Extracellular. {ECO:0000255}.; TOPO_DOM 463 487 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 509 512 Extracellular. {ECO:0000255}.; TOPO_DOM 534 601 Cytoplasmic. {ECO:0000255}. FUNCTION: May be involved in actively transporting phosphate into cells via Na(+) cotransport in the renal brush border membrane. Probably mediates 20-30% of the apical influx. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Observed only in kidney. +P97300 NPTN_MOUSE Neuroplastin (Stromal cell-derived receptor 1) (SDR-1) 397 44,373 Alternative sequence (4); Chain (1); Disulfide bond (3); Domain (3); Glycosylation (6); Region (1); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 339 359 Helical. {ECO:0000255}. TOPO_DOM 29 338 Extracellular. {ECO:0000255}.; TOPO_DOM 360 397 Cytoplasmic. {ECO:0000255}. FUNCTION: Probable homophilic and heterophilic cell adhesion molecule involved in long term potentiation at hippocampal excitatory synapses through activation of p38MAPK. May also regulate neurite outgrowth by activating the FGFR1 signaling pathway. May play a role in synaptic plasticity (By similarity). {ECO:0000250}. PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Enriched at postsynaptic density. {ECO:0000250}. DOMAIN: Some isoforms lack the first Ig-like domain which may confer homophilic adhesion activity. However, they can bind and activate FGFR1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Isoform 1 and isoform 2 are widely expressed with variable levels in brain. Isoform 1 is expressed in cerebellum and midbrain. Isoform 1 and isoform 2 are expressed in cerebral cortex, hipoccampus and striatum. Isoform 2 is more abundant in the cerebral cortex than isoform 1. {ECO:0000269|PubMed:8938438, ECO:0000269|Ref.5}. +O70340 NPTX2_MOUSE Neuronal pentraxin-2 (NP2) (Neuronal pentraxin II) (NP-II) 429 47,137 Chain (1); Disulfide bond (1); Domain (1); Glycosylation (3); Metal binding (7); Signal peptide (1) FUNCTION: Likely to play role in the modification of cellular properties that underlie long-term plasticity. Binds to agar matrix in a calcium-dependent manner (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Homooligomer or heterooligomer (probably pentamer) with neuronal pentraxin receptor (NPTXR). {ECO:0000250}. +Q99J85 NPTXR_MOUSE Neuronal pentraxin receptor 493 52,285 Chain (1); Disulfide bond (1); Domain (1); Glycosylation (3); Metal binding (7); Topological domain (2); Transmembrane (1) TRANSMEM 3 23 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 2 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 24 493 Extracellular. {ECO:0000255}. FUNCTION: May be involved in mediating uptake of synaptic material during synapse remodeling or in mediating the synaptic clustering of AMPA glutamate receptors at a subset of excitatory synapses. {ECO:0000250}. PTM: Ubiquitinated by a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex containing KLHL2. {ECO:0000269|PubMed:21549840}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. SUBUNIT: Heteropentamer with NPTX1 and/or NPTX2. Also binds taipoxin-associated calcium-binding protein 49 (TCBP49/RCN2) (By similarity). Interacts with KLHL2. {ECO:0000250, ECO:0000269|PubMed:21549840}. +Q3V0K9 PLSI_MOUSE Plastin-1 630 70,408 Calcium binding (2); Chain (1); Domain (6); Modified residue (1); Region (2) FUNCTION: Actin-bundling protein in the absence of calcium. {ECO:0000250}. PTM: Phosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. +Q62227 NR0B2_MOUSE Nuclear receptor subfamily 0 group B member 2 (Orphan nuclear receptor SHP) (Small heterodimer partner) 260 28,763 Beta strand (1); Chain (1); Domain (1); Helix (12); Modified residue (1); Natural variant (1) FUNCTION: Acts as a transcriptional regulator. Acts as a negative regulator of receptor-dependent signaling pathways. Specifically inhibits transactivation of the nuclear receptor with whom it interacts. Inhibits transcriptional activity of NEUROD1 on E-box-containing promoter by interfering with the coactivation function of the p300/CBP-mediated transcription complex for NEUROD1. {ECO:0000269|PubMed:8650544}. PTM: Arginine methylation by PRMT5 enhances repression activity of metabolic genes in liver in response to bile acid signaling, by increasing interaction with cofactors. {ECO:0000269|PubMed:21262773}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus. Note=Colocalizes with NEUROD1 in the nucleus. {ECO:0000250}. SUBUNIT: Heterodimer; efficient DNA binding requires dimerization with another bHLH protein. Interacts (via N-terminus) with NEUROD1 (via N-terminus an C-terminus). Interacts with ID2. Interacts with NR5A2, PPARA and PPARG. May also interact with HNF4A (By similarity). Interacts with RARA, RXRA, THRB, NR5A1, NR1I3 and EID1. {ECO:0000250, ECO:0000269|PubMed:11964378, ECO:0000269|PubMed:15707893, ECO:0000269|PubMed:8650544}. TISSUE SPECIFICITY: Expressed in islets of Langerhans (at protein level). {ECO:0000269|PubMed:14752053}. +P41251 NRAM1_MOUSE Natural resistance-associated macrophage protein 1 (NRAMP 1) (Solute carrier family 11 member 1) 548 59,741 Chain (1); Compositional bias (1); Glycosylation (2); Natural variant (1); Topological domain (13); Transmembrane (12) TRANSMEM 56 73 Helical. {ECO:0000255}.; TRANSMEM 83 102 Helical. {ECO:0000255}.; TRANSMEM 140 160 Helical. {ECO:0000255}.; TRANSMEM 165 184 Helical. {ECO:0000255}.; TRANSMEM 194 214 Helical. {ECO:0000255}.; TRANSMEM 238 256 Helical. {ECO:0000255}.; TRANSMEM 285 304 Helical. {ECO:0000255}.; TRANSMEM 347 366 Helical. {ECO:0000255}.; TRANSMEM 398 415 Helical. {ECO:0000255}.; TRANSMEM 427 447 Helical. {ECO:0000255}.; TRANSMEM 464 485 Helical. {ECO:0000255}.; TRANSMEM 494 513 Helical. {ECO:0000255}. TOPO_DOM 1 55 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 74 82 Extracellular. {ECO:0000255}.; TOPO_DOM 103 139 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 161 164 Extracellular. {ECO:0000255}.; TOPO_DOM 185 193 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 215 237 Extracellular. {ECO:0000255}.; TOPO_DOM 257 284 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 305 346 Extracellular. {ECO:0000255}.; TOPO_DOM 367 397 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 416 426 Extracellular. {ECO:0000255}.; TOPO_DOM 448 463 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 486 493 Extracellular. {ECO:0000255}.; TOPO_DOM 514 548 Cytoplasmic. {ECO:0000255}. FUNCTION: Divalent transition metal (iron and manganese) transporter involved in iron metabolism and host resistance to certain pathogens. Macrophage-specific membrane transport function. Controls natural resistance to infection with intracellular parasites. Pathogen resistance involves sequestration of Fe(2+) and Mn(2+), cofactors of both prokaryotic and eukaryotic catalases and superoxide dismutases, not only to protect the macrophage against its own generation of reactive oxygen species, but to deny the cations to the pathogen for synthesis of its protective enzymes. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Macrophages; spleen and liver. +Q60644 NR1H2_MOUSE Oxysterols receptor LXR-beta (Liver X receptor beta) (Nuclear receptor subfamily 1 group H member 2) (Retinoid X receptor-interacting protein No.15) (Ubiquitously-expressed nuclear receptor) 446 49,720 Chain (1); Compositional bias (2); Cross-link (2); DNA binding (1); Domain (1); Region (2); Zinc finger (2) FUNCTION: Nuclear receptor that exhibits a ligand-dependent transcriptional activation activity (PubMed:18055760, PubMed:19520913, PubMed:20427281). Binds preferentially to double-stranded oligonucleotide direct repeats having the consensus half-site sequence 5'-AGGTCA-3' and 4-nt spacing (DR-4) (PubMed:18055760, PubMed:19520913, PubMed:20427281). Regulates cholesterol uptake through MYLIP-dependent ubiquitination of LDLR, VLDLR and LRP8; DLDLR and LRP8 (PubMed:18055760, PubMed:19520913, PubMed:20427281). Interplays functionally with RORA for the regulation of genes involved in liver metabolism (PubMed:18055760, PubMed:19520913, PubMed:20427281). Plays an anti-inflammatory role during the hepatic acute phase response by acting as a corepressor: inhibits the hepatic acute phase response by preventing dissociation of the N-Cor corepressor complex (By similarity). {ECO:0000250|UniProtKB:P55055, ECO:0000269|PubMed:18055760, ECO:0000269|PubMed:19520913, ECO:0000269|PubMed:20427281}. PTM: Sumoylated by SUMO2 at Lys-395 and Lys-433 during the hepatic acute phase response, leading to promote interaction with GPS2 and prevent N-Cor corepressor complex dissociation. {ECO:0000250|UniProtKB:P55055}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}. SUBUNIT: Forms a heterodimer with RXR. Interacts with CCAR2 (via N-terminus) in a ligand-independent manner. Interacts (when sumoylated) with GPS2; interaction with GPS2 onto hepatic acute phase protein promoters prevents N-Cor corepressor complex dissociation. {ECO:0000250|UniProtKB:P55055}. TISSUE SPECIFICITY: Ubiquitous. +Q9Z0Y9 NR1H3_MOUSE Oxysterols receptor LXR-alpha (Liver X receptor alpha) (Nuclear receptor subfamily 1 group H member 3) 445 50,418 Beta strand (2); Chain (1); DNA binding (1); Domain (1); Helix (10); Modified residue (1); Region (2); Sequence conflict (2); Turn (4); Zinc finger (2) FUNCTION: Nuclear receptor that exhibits a ligand-dependent transcriptional activation activity (PubMed:18055760, PubMed:19520913, PubMed:20427281). Interaction with retinoic acid receptor (RXR) shifts RXR from its role as a silent DNA-binding partner to an active ligand-binding subunit in mediating retinoid responses through target genes defined by LXRES. LXRES are DR4-type response elements characterized by direct repeats of two similar hexanuclotide half-sites spaced by four nucleotides. Plays an important role in the regulation of cholesterol homeostasis, regulating cholesterol uptake through MYLIP-dependent ubiquitination of LDLR, VLDLR and LRP8. Interplays functionally with RORA for the regulation of genes involved in liver metabolism. {ECO:0000250|UniProtKB:Q13133, ECO:0000269|PubMed:18055760, ECO:0000269|PubMed:19520913, ECO:0000269|PubMed:20427281}. PTM: Ubiquitinated leading to its degradation by the proteasome. {ECO:0000269|PubMed:27383786}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407, ECO:0000269|PubMed:27383786}. Cytoplasm {ECO:0000269|PubMed:27383786}. SUBUNIT: Heterodimer of NR1H3 and RXR (retinoic acid receptor). Interacts with CCAR2 (via N-terminus) in a ligand-independent manner. Interacts with SIRT1 and this interaction is inhibited by CCAR2 (By similarity). {ECO:0000250|UniProtKB:Q13133}. +Q9DBW3 NATD1_MOUSE Protein NATD1 (Gene trap locus protein F3-2) (Gene trap locus protein F3b) (N-acetyltransferase domain-containing protein 1) 110 12,731 Chain (1); Domain (1) TISSUE SPECIFICITY: Expressed in the heart, testis, kidney and lung. {ECO:0000269|PubMed:10402672}. +Q60974 NCOR1_MOUSE Nuclear receptor corepressor 1 (N-CoR) (N-CoR1) (Retinoid X receptor-interacting protein 13) (RIP13) 2453 270,642 Alternative sequence (1); Chain (1); Coiled coil (3); Compositional bias (6); Cross-link (6); Domain (2); Modified residue (25); Motif (3); Region (6); Sequence conflict (2) FUNCTION: Mediates transcriptional repression by certain nuclear receptors. Part of a complex which promotes histone deacetylation and the formation of repressive chromatin structures which may impede the access of basal transcription factors. Participates in the transcriptional repressor activity produced by BCL6. Recruited by ZBTB7A to the androgen response elements/ARE on target genes, negatively regulates androgen receptor signaling and androgen-induced cell proliferation. {ECO:0000250|UniProtKB:O75376}. PTM: Ubiquitinated; mediated by SIAH2 and leading to its subsequent proteasomal degradation. {ECO:0000305}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Forms a large corepressor complex that contains SIN3A/B and histone deacetylases HDAC1 and HDAC2. This complex associates with the thyroid receptor (TR) and the retinoid acid receptor (RAR) in the absence of ligand. Interacts directly with RARA; the interaction is facilitated with RARA trimethylation. Component of the N-Cor repressor complex, at least composed of CBFA2T3, HEXIM1, NCOR1, NCOR2, HDAC3, TBL1X, TBL1XR1, CORO2A and GPS2. Interacts with ZBTB33; the interaction serves to recruit the N-CoR complex to promoter regions containing methylated CpG dinucleotides. Interacts with TRIM28 and KDM3A. Interacts (via the RD1 domain) with BAZ1A (via its N-terminal); the interaction corepresses a number of NCOR1-regulated genes. Interacts with BCL6, C1D, DACH1, HEXIM1, HDAC7, RORA, RORC, SAP30, SIAH2, SIN3A and SIN3B (PubMed:10984530). May interact with DEAF1. Interacts with RXRA. Interacts with SETD5 (PubMed:27864380). Interacts with VDR (By similarity). Interacts with ZBTB7A (By similarity). Interacts with AR (By similarity). {ECO:0000250|UniProtKB:O75376, ECO:0000269|PubMed:10984530, ECO:0000269|PubMed:11533236, ECO:0000269|PubMed:12130660, ECO:0000269|PubMed:17205979, ECO:0000269|PubMed:19078967, ECO:0000269|PubMed:19786558, ECO:0000269|PubMed:21499262, ECO:0000269|PubMed:27864380, ECO:0000269|PubMed:8961273, ECO:0000269|PubMed:9139820, ECO:0000269|PubMed:9405624, ECO:0000269|PubMed:9637679, ECO:0000269|PubMed:9702189}. DOMAIN: The N-terminal region contains three independent domains that are capable of mediating transcriptional repression (RD1, RD2 and RD3). {ECO:0000269|PubMed:8961273}.; DOMAIN: The C-terminal region contains two separate nuclear receptor-interacting domains (ID1 and ID2), each of which contains a conserved sequence referred to as the CORNR box. This motif is necessary and sufficient for binding to unligated nuclear hormone receptors, while sequences flanking the CORNR box determine the precise nuclear hormone receptor specificity. {ECO:0000269|PubMed:8961273}. TISSUE SPECIFICITY: Ubiquitous. +O88425 NDK6_MOUSE Nucleoside diphosphate kinase 6 (NDK 6) (NDP kinase 6) (EC 2.7.4.6) (nm23-M6) 189 21,778 Active site (1); Binding site (6); Chain (1); Sequence conflict (2) FUNCTION: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. +O88907 PIAS1_MOUSE E3 SUMO-protein ligase PIAS1 (EC 2.3.2.27) (DEAD/H box-binding protein 1) (Protein inhibitor of activated STAT protein 1) (RING-type E3 ubiquitin transferase PIAS1) 651 71,618 Chain (1); Compositional bias (1); Cross-link (6); Domain (2); Initiator methionine (1); Modified residue (11); Motif (3); Mutagenesis (6); Region (2); Repeat (4); Sequence conflict (1); Zinc finger (1) Protein modification; protein sumoylation. FUNCTION: Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor. Plays a crucial role as a transcriptional coregulation in various cellular pathways, including the STAT pathway, the p53 pathway and the steroid hormone signaling pathway. In vitro, binds A/T-rich DNA (By similarity). The effects of this transcriptional coregulation, transactivation or silencing, may vary depending upon the biological context. Sumoylates PML (at'Lys-65' and 'Lys-160') and PML-RAR and promotes their ubiquitin-mediated degradation. PIAS1-mediated sumoylation of PML promotes its interaction with CSNK2A1/CK2 which in turn promotes PML phosphorylation and degradation. Enhances the sumoylation of MTA1 and may participate in its paralog-selective sumoylation. Plays a dynamic role in adipogenesis by promoting the SUMOylation and degradation of CEBPB (PubMed:24061474). {ECO:0000250|UniProtKB:O75925, ECO:0000269|PubMed:22406621, ECO:0000269|PubMed:24061474}. PTM: Sumoylated. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}. Nucleus, PML body {ECO:0000269|PubMed:12077349, ECO:0000269|PubMed:22406621}. Note=Interaction with CSRP2 may induce a partial redistribution along the cytoskeleton. {ECO:0000250}. SUBUNIT: Interacts with NR2C1; the interaction promotes its sumoylation. Interacts with DDX21, CSRP2, AXIN1, JUN, SATB2, PLAG1, TP53 and STAT1 (dimer), following IFNA1-stimulation. Interacts with SP3 (preferentially when SUMO-modified). Interacts with KLF8; the interaction results in SUMO ligation and repression of KLF8 transcriptional activity and of its cell cycle progression into G(1) phase (By similarity). Interacts with CHUK/IKKA; this interaction induces PIAS1 phosphorylation. Interacts with PTK2/FAK1; the interaction promotes its sumoylation (By similarity). Interacts with SUMO1, UBE2I, NCOA2 and AR. Interacts with NR2C1; the interaction promotes its sumoylation. Interacts with DDX5. Interacts with MTA1 (By similarity). Interacts with PML (isoform PML-12). {ECO:0000250, ECO:0000269|PubMed:11117529, ECO:0000269|PubMed:12077349, ECO:0000269|PubMed:17187077, ECO:0000269|PubMed:22406621}. DOMAIN: The LXXLL motif is a transcriptional coregulator signature.; DOMAIN: The SP-RING-type domain is required for promoting EKLF sumoylation. TISSUE SPECIFICITY: Expressed in kidney, heart, spleen, brain and cerebellum; weak expression, if any, in liver and lung. {ECO:0000269|PubMed:10854042}. +P15532 NDKA_MOUSE Nucleoside diphosphate kinase A (NDK A) (NDP kinase A) (EC 2.7.4.6) (Metastasis inhibition factor NM23) (NDPK-A) (Tumor metastatic process-associated protein) (nm23-M1) 152 17,208 Active site (1); Binding site (6); Chain (1); Cross-link (1); Erroneous initiation (1); Modified residue (4) FUNCTION: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Possesses nucleoside-diphosphate kinase, serine/threonine-specific protein kinase, geranyl and farnesyl pyrophosphate kinase, histidine protein kinase and 3'-5' exonuclease activities. Involved in cell proliferation, differentiation and development, signal transduction, G protein-coupled receptor endocytosis, and gene expression. Required for neural development including neural patterning and cell fate determination. During GZMA-mediated cell death, works in concert with TREX1. NME1 nicks one strand of DNA and TREX1 removes bases from the free 3' end to enhance DNA damage and prevent DNA end reannealing and rapid repair (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. SUBUNIT: Hexamer of two different chains: A and B (A6, A5B, A4B2, A3B3, A2B4, AB5, B6). Interacts with PRUNE1. Component of the SET complex, composed of at least ANP32A, APEX1, HMGB2, NME1, SET and TREX1. Within this complex, interacts directly with SET. Also interacts with TREX1, but only following translocation to the nucleus. {ECO:0000250|UniProtKB:P15531}. DISEASE: Note=This protein is found in reduced amount in tumor cells of high metastatic potential. +O09101 PIGF_MOUSE Phosphatidylinositol-glycan biosynthesis class F protein (PIG-F) 219 24,825 Chain (1); Transmembrane (6) TRANSMEM 11 31 Helical. {ECO:0000255}.; TRANSMEM 42 62 Helical. {ECO:0000255}.; TRANSMEM 86 106 Helical. {ECO:0000255}.; TRANSMEM 113 133 Helical. {ECO:0000255}.; TRANSMEM 155 175 Helical. {ECO:0000255}.; TRANSMEM 189 209 Helical. {ECO:0000255}. Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis. FUNCTION: Involved in GPI-anchor biosynthesis through the transfer of ethanolamine phosphate to the third mannose of GPI. {ECO:0000269|PubMed:10781593}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10781593}; Multi-pass membrane protein {ECO:0000269|PubMed:10781593}. SUBUNIT: Forms a complex with PIGG and PIGO. PIGF is required to stabilize PIGG and PIGO. {ECO:0000269|PubMed:10781593}. +Q9CQ91 NDUA3_MOUSE NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3 (Complex I-B9) (CI-B9) (NADH-ubiquinone oxidoreductase B9 subunit) 84 9,331 Beta strand (1); Chain (1); Helix (5); Initiator methionine (1); Modified residue (1); Transmembrane (1); Turn (1) TRANSMEM 19 39 Helical. {ECO:0000255}. FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. {ECO:0000250|UniProtKB:O95167}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:O95167}; Single-pass membrane protein {ECO:0000255}. SUBUNIT: Complex I is composed of 45 different subunits. {ECO:0000250|UniProtKB:O95167}. +O70570 PIGR_MOUSE Polymeric immunoglobulin receptor (PIgR) (Poly-Ig receptor) [Cleaved into: Secretory component] 771 84,999 Beta strand (16); Chain (2); Disulfide bond (5); Domain (5); Glycosylation (6); Helix (7); Modified residue (4); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (3) TRANSMEM 646 668 Helical. {ECO:0000255}. TOPO_DOM 19 645 Extracellular. {ECO:0000255}.; TOPO_DOM 669 771 Cytoplasmic. {ECO:0000255}. FUNCTION: This receptor binds polymeric IgA and IgM at the basolateral surface of epithelial cells. The complex is then transported across the cell to be secreted at the apical surface. During this process a cleavage occurs that separates the extracellular (known as the secretory component) from the transmembrane segment (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Secretory component: Secreted. +Q9QYF9 NDRG3_MOUSE Protein NDRG3 (N-myc downstream-regulated gene 3 protein) (Protein Ndr3) 375 41,555 Chain (1); Modified residue (13) TISSUE SPECIFICITY: Expressed at high levels in brain, followed by small intestine and kidney (at protein level). Also expressed in thymus. {ECO:0000269|PubMed:21636852}. +Q9D6J6 NDUV2_MOUSE NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial (EC 1.6.99.3) (EC 7.1.1.2) (NADH-ubiquinone oxidoreductase 24 kDa subunit) 248 27,285 Alternative sequence (1); Beta strand (8); Chain (1); Helix (8); Metal binding (4); Modified residue (2); Sequence conflict (1); Transit peptide (1); Turn (1) FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}. SUBUNIT: Complex I is composed of 45 different subunits. This is a component of the flavoprotein-sulfur (FP) fragment of the enzyme (By similarity). {ECO:0000250}. +Q9D6J4 NECA3_MOUSE N-terminal EF-hand calcium-binding protein 3 (Amyloid-beta A4 protein-binding family A member 2-binding protein) (X11L-binding protein 51) (mXB51) 353 39,906 Alternative sequence (1); Calcium binding (1); Chain (1); Domain (2); Erroneous initiation (3); Region (1); Sequence conflict (2) FUNCTION: Inhibits the interaction of APBA2 with amyloid-beta precursor protein (APP), and hence allows formation of amyloid-beta (By similarity). May enhance the activity of HIF1A and thus promote glycolysis under normoxic conditions; the function requires its ABM domain and may implicate the stabilization of the interaction between HIF1AN and APBA3 (By similarity). {ECO:0000250|UniProtKB:Q96P71}. PTM: Phosphorylated by NEK2. {ECO:0000250|UniProtKB:Q96P71}. SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:Q96P71}. SUBUNIT: Interacts with the N-terminal domain of APBA2. Interacts with NEK2 (By similarity). Interacts with APBA3; APBA3 seems to mediate the interaction between NECAB3 and HIF1AN (By similarity). {ECO:0000250|UniProtKB:Q96P71}. TISSUE SPECIFICITY: Widely expressed, with highest levels in the brain. {ECO:0000269|PubMed:14697346}. +O35942 NEK2_MOUSE Serine/threonine-protein kinase Nek2 (EC 2.7.11.1) (Never in mitosis A-related kinase 2) (NimA-related protein kinase 2) 443 51,243 Active site (1); Binding site (1); Chain (1); Coiled coil (2); Domain (1); Modified residue (12); Nucleotide binding (1); Region (6); Sequence conflict (9) FUNCTION: Protein kinase which is involved in the control of centrosome separation and bipolar spindle formation in mitotic cells and chromatin condensation in meiotic cells. Regulates centrosome separation (essential for the formation of bipolar spindles and high-fidelity chromosome separation) by phosphorylating centrosomal proteins such as CROCC, CEP250 and NINL, resulting in their displacement from the centrosomes. Regulates kinetochore microtubule attachment stability in mitosis via phosphorylation of NDC80. Involved in regulation of mitotic checkpoint protein complex via phosphorylation of CDC20 and MAD2L1. Plays an active role in chromatin condensation during the first meiotic division through phosphorylation of HMGA2. Phosphorylates: PPP1CC; SGO1; NECAB3 and NPM1. Essential for localization of MAD2L1 to kinetochore and MAPK1 and NPM1 to the centrosome. Phosphorylates CEP68 and CNTLN directly or indirectly (By similarity). NEK2-mediated phosphorylation of CEP68 promotes CEP68 dissociation from the centrosome and its degradation at the onset of mitosis (By similarity). Phosphorylates and activates NEK11 in G1/S-arrested cells. Involved in the regulation of centrosome disjunction (By similarity). {ECO:0000250|UniProtKB:P51955, ECO:0000269|PubMed:14668482, ECO:0000269|PubMed:14697346}. PTM: Activated by autophosphorylation. Protein phosphatase 1 represses autophosphorylation and activation of isoform 1 by dephosphorylation. Phosphorylation by STK3/MST2 is necessary for its localization to the centrosome. {ECO:0000250|UniProtKB:P51955}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9187143}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P51955}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P51955}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Chromosome, centromere {ECO:0000269|PubMed:9187143}. Note=STK3/MST2 and SAV1 are required for its targeting to the centrosome. Colocalizes with SGO1 and MAD1L1 at the kinetochore. Not associated with kinetochore in the interphase but becomes associated with it upon the breakdown of the nuclear envelope. Has a nucleolar targeting/ retention activity via a coiled-coil domain at the C-terminal end (By similarity). {ECO:0000250}. SUBUNIT: Forms homodimers and heterodimers. Interacts with CDC20, CTNB1, MAD1L1, MAD2L1, MAPK, NEK11, NPM1, NDC80, PCNT, PPP1CA, PPP1CC and SGO1. Interacts with STK3/MST2 (via SARAH domain) and SAV1 (via SARAH domain) (By similarity). Interacts with NECAB3 and HMGA2 (PubMed:14697346, PubMed:14668482). Interacts with CEP68; the interaction leads to phosphorylation of CEP68. Interacts with CNTLN; the interaction leads to phosphorylation of CNTLN. Interacts with CEP85 (By similarity). {ECO:0000250|UniProtKB:P51955, ECO:0000269|PubMed:14668482, ECO:0000269|PubMed:14697346}. DOMAIN: The leucine-zipper domain is required for its dimerization and activation. {ECO:0000250|UniProtKB:P51955}. TISSUE SPECIFICITY: Most abundantly expressed in testis. Low levels found in mid-gestation embryo, ovary, placenta, intestine, thymus and skin. Within the testis, expression restricted to germ cells with highest levels detected in spermatocytes at pachytene and diplotene stages. Also expressed in meiotic pachytene oocytes. {ECO:0000269|PubMed:9187143, ECO:0000269|PubMed:9434622}. +Q9CQ76 NEPN_MOUSE Nephrocan 512 57,705 Chain (1); Compositional bias (1); Domain (1); Glycosylation (1); Repeat (17); Signal peptide (1) FUNCTION: May inhibit TGF-beta signaling. {ECO:0000269|PubMed:16990280}. PTM: N-glycosylated. {ECO:0000269|PubMed:16990280}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16990280}. TISSUE SPECIFICITY: Expressed at highest levels in the kidney, where it is primarily detected in the epithelial cells of distal tubules and collecting ducts, and more weakly in proximal epithelial cells. Expressed at lower levels in heart and lung (at protein level). Detected in skeletal muscle. {ECO:0000269|PubMed:16990280}. +Q8K3J1 NDUS8_MOUSE NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial (EC 1.6.99.3) (EC 7.1.1.2) (Complex I-23kD) (CI-23kD) (NADH-ubiquinone oxidoreductase 23 kDa subunit) 212 24,038 Beta strand (8); Chain (1); Domain (2); Helix (5); Metal binding (8); Transit peptide (1); Turn (6) FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. SUBUNIT: Complex I is composed of 45 different subunits This is a component of the iron-sulfur (IP) fragment of the enzyme. {ECO:0000250}. +P32507 NECT2_MOUSE Nectin-2 (Herpes virus entry mediator B) (Herpesvirus entry mediator B) (HveB) (Murine herpes virus entry protein B) (mHveB) (Nectin cell adhesion molecule 2) (Poliovirus receptor homolog) (Poliovirus receptor-related protein 2) (CD antigen CD112) 530 57,318 Alternative sequence (2); Beta strand (21); Chain (1); Disulfide bond (3); Domain (3); Glycosylation (3); Helix (3); Modified residue (2); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (2) TRANSMEM 352 372 Helical. {ECO:0000255}. TOPO_DOM 32 351 Extracellular. {ECO:0000255}.; TOPO_DOM 373 530 Cytoplasmic. {ECO:0000255}. FUNCTION: Modulator of T-cell signaling. Can be either a costimulator of T-cell function, or a coinhibitor, depending on the receptor it binds to. Upon binding to CD226, stimulates T-cell proliferation and cytokine production, including that of IL2, IL5, IL10, IL13, and IFNG. Upon interaction with PVRIG, inhibits T-cell proliferation. These interactions are competitive. Probable cell adhesion protein. {ECO:0000250|UniProtKB:Q92692}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q92692}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Can form trans-heterodimers with NECTIN3 (PubMed:10744716, PubMed:22902367). Interacts with CD226 or with PVRIG; these interactions are competitive and have a differential functional outcome on T-cell activation, either positive or negative, respectively. Binds with low affinity to TIGIT (By similarity). {ECO:0000250|UniProtKB:Q92692, ECO:0000269|PubMed:10744716, ECO:0000269|PubMed:22902367}. TISSUE SPECIFICITY: Brain, spinal cord, spleen, kidney, heart and liver. +Q8K4Q6 NEIL1_MOUSE Endonuclease 8-like 1 (EC 3.2.2.-) (EC 4.2.99.18) (DNA glycosylase/AP lyase Neil1) (DNA-(apurinic or apyrimidinic site) lyase Neil1) (Endonuclease VIII-like 1) (Nei homolog 1) (NEH1) (Nei-like protein 1) 389 43,586 Active site (3); Alternative sequence (1); Binding site (1); Chain (1); Frameshift (1); Initiator methionine (1) FUNCTION: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized pyrimidines, such as thymine glycol, formamidopyrimidine (Fapy) and 5-hydroxyuracil. Has marginal activity towards 8-oxoguanine. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. Has DNA glycosylase/lyase activity towards mismatched uracil and thymine, in particular in U:C and T:C mismatches. Specifically binds 5-hydroxymethylcytosine (5hmC), suggesting that it acts as a specific reader of 5hmC. {ECO:0000269|PubMed:12200441, ECO:0000269|PubMed:23434322}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Nucleus. Chromosome. Note=During mitosis, associates with centrosomes and condensed chromatin. {ECO:0000250}. TISSUE SPECIFICITY: Detected in heart, spleen and lung. {ECO:0000269|PubMed:12200441}. +Q8K203 NEIL3_MOUSE Endonuclease 8-like 3 (EC 3.2.2.-) (EC 4.2.99.18) (DNA glycosylase FPG2) (DNA glycosylase/AP lyase Neil3) (Endonuclease VIII-like 3) (Nei-like protein 3) 606 67,416 Active site (1); Alternative sequence (1); Beta strand (9); Binding site (2); Chain (1); Helix (11); Initiator methionine (1); Modified residue (1); Natural variant (10); Site (2); Turn (4); Zinc finger (2) FUNCTION: DNA glycosylase which prefers single-stranded DNA (ssDNA), or partially ssDNA structures such as bubble and fork structures, to double-stranded DNA (dsDNA). In vitro, displays strong glycosylase activity towards the hydantoin lesions spiroiminodihydantoin (Sp) and guanidinohydantoin (Gh) in both ssDNA and dsDNA; also recognizes FapyA, FapyG, 5-OHU, 5-OHC, 5-OHMH, Tg and 8-oxoA lesions in ssDNA. No activity on 8-oxoG detected. Also shows weak DNA-(apurinic or apyrimidinic site) lyase activity. In vivo, appears to be the primary enzyme involved in removing Sp and Gh from ssDNA in neonatal tissues. Seems to be an important facilitator of cell proliferation in certain populations, for example neural stem/progenitor cells and tumor cells, suggesting a role in replication-associated DNA repair. {ECO:0000269|PubMed:20185759, ECO:0000269|PubMed:22065741, ECO:0000269|PubMed:22569481, ECO:0000269|PubMed:22959434, ECO:0000269|PubMed:23305905, ECO:0000269|PubMed:23313161}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16428305}. DOMAIN: The N-terminal region (2-282) contains the glycosylase and lyase activities. TISSUE SPECIFICITY: Expressed in testis, thymus, spleen and bone marrow. In young mice, expressed at higher levels in thymocytes than splenocytes. At E12, abundant in the subventricular zone (SVZ) of the lateral ventricles. At E17.5 and P0, expression is limited to distinct cells in the cortical SVZ, in cells of the secondary matrix, the dentate gyrus migratory route and the dentate gyrus. {ECO:0000269|PubMed:16428305, ECO:0000269|PubMed:19170771, ECO:0000269|PubMed:19426544, ECO:0000269|PubMed:23305905}. +O09130 NF2IP_MOUSE NFATC2-interacting protein (45 kDa NF-AT-interacting protein) (45 kDa NFAT-interacting protein) (Nuclear factor of activated T-cells, cytoplasmic 2-interacting protein) 412 45,121 Beta strand (5); Chain (1); Coiled coil (1); Cross-link (1); Domain (1); Frameshift (1); Helix (2); Modified residue (13); Sequence conflict (3) FUNCTION: In T-helper 2 (Th2) cells, regulates the magnitude of NFAT-driven transcription of a specific subset of cytokine genes, including IL3, IL4, IL5 and IL13, but not IL2. Recruits PRMT1 to the IL4 promoter; this leads to enhancement of histone H4 'Arg-3'-methylation and facilitates subsequent histone acetylation at the IL4 locus, thus promotes robust cytokine expression. Down-regulates formation of poly-SUMO chains by UBE2I/UBC9. {ECO:0000269|PubMed:20077568, ECO:0000269|PubMed:20133688}. PTM: Methylation at the N-terminus by PRMT1 modulates interaction with the NFAT complex and results in augmented cytokine production. {ECO:0000269|PubMed:15327772}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=TRAF1 is associated with a fraction of NFATC2IP in the cytoplasm and prevents its translocation to the nucleus. SUBUNIT: Interacts with NFATC2, TRAF1, TRAF2 and PRMT1. Interacts with UBE2I/UBC9. {ECO:0000269|PubMed:11435475, ECO:0000269|PubMed:16352630, ECO:0000269|PubMed:20077568, ECO:0000269|PubMed:8943202}. TISSUE SPECIFICITY: Highest level detected in spleen, thymus and testis. {ECO:0000269|PubMed:8943202}. +Q810U3 NFASC_MOUSE Neurofascin 1240 137,975 Chain (1); Compositional bias (1); Disulfide bond (6); Domain (10); Glycosylation (8); Modified residue (9); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1111 1131 Helical. {ECO:0000255}. TOPO_DOM 25 1110 Extracellular. {ECO:0000255}.; TOPO_DOM 1132 1240 Cytoplasmic. {ECO:0000255}. FUNCTION: Cell adhesion, ankyrin-binding protein which may be involved in neurite extension, axonal guidance, synaptogenesis, myelination and neuron-glial cell interactions. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SUBUNIT: Horseshoe-shaped homodimer. Probable constituent of a NFASC/NRCAM/ankyrin-G complex. Associates with the sodium channel beta-1 (SCN1B) and beta-3 (SCN3B) subunits. Interacts with GLDN/gliomedin (By similarity). Interacts with MYOC. {ECO:0000250, ECO:0000269|PubMed:23897819}. DOMAIN: Homophilic adhesion is primarily mediated by the interaction of the second Ig-like domains. {ECO:0000250}. +Q6ZQ12 NINL_MOUSE Ninein-like protein 1394 157,838 Alternative sequence (2); Calcium binding (1); Chain (1); Coiled coil (6); Compositional bias (1); Domain (4); Erroneous initiation (1); Modified residue (1); Motif (2); Sequence conflict (8) FUNCTION: Involved in the microtubule organization in interphase cells. Overexpression induces the fragmentation of the Golgi, and causes lysosomes to disperse toward the cell periphery; it also interferes with mitotic spindle assembly (By similarity). {ECO:0000250}. PTM: Phosphorylated by PLK1 which disrupts its centrosome association and interaction with gamma-tubulin. {ECO:0000250}.; PTM: Ubiquitinated by the APC/C complex leading to its degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9Y2I6}. Cytoplasm {ECO:0000250|UniProtKB:Q9Y2I6}. Note=In interphase cells, NLP is transported to the centrosomes by the dynein-dynactin motor complex. During centrosome maturation, PLK1 directly phosphorylates NLP resulting in its release into the cytoplasm. {ECO:0000250|UniProtKB:Q9Y2I6}. SUBUNIT: Interacts with gamma-tubulin and TUBGCP4. Interacts with anaphase promoting complex/cyclosome (APC/C). Interacts with CDC20 and FZR1. Interacts with LCA5 and USH2A (By similarity). {ECO:0000250}. DOMAIN: The KEN and D (destructive) boxes are required for the cell cycle-controlled NINL degradation by the APC/C pathway. {ECO:0000250}. +P97436 NKX31_MOUSE Homeobox protein Nkx-3.1 (Homeobox protein NK-3 homolog A) 237 26,824 Chain (1); DNA binding (1) FUNCTION: Transcription factor, which binds preferentially the consensus sequence 5'-TAAGT[AG]-3' and can behave as a transcriptional repressor (By similarity). Plays an important role in normal prostate development, regulating proliferation of glandular epithelium and in the formation of ducts in prostate. Acts as a tumor suppressor controlling prostate carcinogenesis, as shown by the ability to suppress growth and tumorigenicity of prostate carcinoma cells. Plays a role in the formation of minor salivary glands (particularly palatine and lingual glands). Essential for appropriate differentiation and secretory function of the bulbourethral gland. {ECO:0000250, ECO:0000269|PubMed:12036903}. PTM: Ubiquitinated by TOPORS; monoubiquitinated at several residues and also polyubiquitinated on single residues. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. SUBUNIT: Interacts with serum response factor (SRF). Interacts with SPDEF (By similarity). Interacts with WDR77 (By similarity). Interacts with TOPORS which polyubiquitinates NKX3-1 and induces its proteasomal degradation (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed mostly in the male urogenital tract, with highest expression in the epithelial cells lining the ducts of anterior, dorsolateral and ventral prostate and in the bulbourethral gland, and much lower in the seminal vesicle and the testis. Expression in the prostate increases during sexual maturation and is drastically reduced following castration. Expressed also in brain (hippocampus and external granular layer of the cerebral cortex), kidney (intralobular arteries), thymus and adrenal and salivary glands. +Q8BHI9 NIM1_MOUSE Serine/threonine-protein kinase NIM1 (EC 2.7.11.1) (NIM1 serine/threonine-protein kinase) 436 49,777 Active site (1); Binding site (1); Chain (1); Domain (1); Modified residue (1); Nucleotide binding (1); Sequence conflict (1) +Q3UHX8 NKX63_MOUSE Homeobox protein Nkx-6.3 262 28,779 Chain (1); DNA binding (1); Sequence conflict (2) FUNCTION: Putative transcription factor, which may be involved in patterning of central nervous system and pancreas. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. TISSUE SPECIFICITY: Expressed in the developing CNS and gastro-intestinal tract. {ECO:0000269|PubMed:16326147}. +Q2LKV5 NL1B3_MOUSE NACHT, LRR and PYD domains-containing protein 1b allele 3 1172 133,631 Chain (1); Domain (3); Mutagenesis (3); Nucleotide binding (1); Repeat (2); Site (1) FUNCTION: As the sensor component of the NLRP1 inflammasome, plays a crucial role in innate immunity and inflammation. In response to pathogens and other damage-associated signals, initiates the formation of the inflammasome polymeric complex, made of Nlrp1b, CASP1, and possibly PYCARD. Recruitment of proCASP1 to the inflammasome promotes its activation and CASP1-catalyzed IL1B and IL18 maturation and secretion in the extracellular milieu. Activation of NLRP1 inflammasome is also required for HMGB1 secretion. The active cytokines and HMGB1 stimulate inflammatory responses. Inflammasomes can also induce pyroptosis, an inflammatory form of programmed cell death (By similarity). Contrary to Nlrp1b allele 1, allele 3 is not activated by Bacillus anthracis lethal toxin, nor by metabolic inhibitors, such as 2-deoxy-D-glucose and sodium azide (PubMed:16429160, PubMed:19651869, PubMed:23230290). {ECO:0000250|UniProtKB:Q2LKW6, ECO:0000269|PubMed:16429160, ECO:0000269|PubMed:19651869, ECO:0000269|PubMed:23230290}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9C000}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9C000}. Inflammasome {ECO:0000250|UniProtKB:Q2LKW6}. SUBUNIT: Sensor component of NLRP1 inflammasomes. Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other damage-associated signals and play critical roles in innate immunity and inflammation. Classical inflammasomes consist of a signal sensor component, an adapter (ASC/PYCARD), which recruits an effector proinflammatory caspase (CASP1 and possibly CASP4/CASP11). CASP1 filament formation increases local enzyme concentration, resulting in trans-autocleavage and activation. Active CASP1 then processes IL1B and IL18 precursors, leading to the release of mature cytokines in the extracellular milieu and inflammatory response. In NLRP1 inflammasome, the role of PYCARD is not clear. Following activation, Nlrp1b may directly interact with CASP1 (through the CARD domain) to form a functional inflammasome. Hence PYCARD may not be necessary for NLRP1 and CASP1 interaction, but is required for speck formation and full inflammasome activity (By similarity). Homomer (By similarity). Interacts (via LRR repeats) with BCL2 and BCL2L1 (via the loop between motifs BH4 and BH3); these interactions reduce NLRP1 inflammasome-induced CASP1 activation and IL1B release, possibly by impairing NLRP1 interaction with PYCARD. Interacts with NOD2; this interaction may increase IL1B release. Interacts with EIF2AK2/PKR; this interaction requires EIF2AK2 activity, is accompanied by EIF2AK2 autophosphorylation and promotes inflammasome assembly in response to danger-associated signals. Interacts with MEFV; this interaction targets NLRP1 to degradation by autophagy, hence preventing excessive IL1B- and IL18-mediated inflammation (By similarity). {ECO:0000250|UniProtKB:Q2LKW6, ECO:0000250|UniProtKB:Q9C000}. DOMAIN: The CARD domain is involved in the interaction with PYCARD, CASP1 and CASP4/CASP11. {ECO:0000250|UniProtKB:Q9C000}.; DOMAIN: The leucine-rich repeat (LRR) domain may be involved in autoinhibition in the absence of activating signal, possibly through intramolecular interaction with the NACHT domain. {ECO:0000250|UniProtKB:Q2LKW6}.; DOMAIN: The FIIND (domain with function to find) region may be involved in homomerization, but not in CASP1-binding. Contrary to allele 1, allele 3 does not undergo autocatalytic cleavage in this region. {ECO:0000269|PubMed:22536155}. TISSUE SPECIFICITY: Expressed in macrophages. {ECO:0000269|PubMed:16429160, ECO:0000269|PubMed:23506131}. +Q8BHK1 NIPA1_MOUSE Magnesium transporter NIPA1 (Non-imprinted in Prader-Willi/Angelman syndrome region protein 1 homolog) 323 34,105 Chain (1); Mutagenesis (2); Topological domain (10); Transmembrane (9) TRANSMEM 22 42 Helical. {ECO:0000255}.; TRANSMEM 61 81 Helical. {ECO:0000255}.; TRANSMEM 83 103 Helical. {ECO:0000255}.; TRANSMEM 112 132 Helical. {ECO:0000255}.; TRANSMEM 154 174 Helical. {ECO:0000255}.; TRANSMEM 178 198 Helical. {ECO:0000255}.; TRANSMEM 219 239 Helical. {ECO:0000255}.; TRANSMEM 254 274 Helical. {ECO:0000255}.; TRANSMEM 285 305 Helical. {ECO:0000255}. TOPO_DOM 1 21 Extracellular. {ECO:0000255}.; TOPO_DOM 43 60 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 82 82 Extracellular. {ECO:0000255}.; TOPO_DOM 104 111 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 133 153 Extracellular. {ECO:0000255}.; TOPO_DOM 175 177 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 199 218 Extracellular. {ECO:0000255}.; TOPO_DOM 240 253 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 275 284 Extracellular. {ECO:0000255}.; TOPO_DOM 306 323 Cytoplasmic. {ECO:0000255}. FUNCTION: Acts as a Mg(2+) transporter. Can also transport other divalent cations such as Fe(2+), Sr(2+), Ba(2+), Mn(2+) and Co(2+) but to a much less extent than Mg(2+). {ECO:0000269|PubMed:17166836}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Early endosome {ECO:0000269|PubMed:17166836}. Note=Recruited to the cell membrane in response to low extracellular magnesium. SUBUNIT: Homodimer. {ECO:0000305}. TISSUE SPECIFICITY: Widely expressed. Predominantly expressed in neuronal tissues. Brain, heart, kidney, liver and colon (at protein level). {ECO:0000269|PubMed:14508708, ECO:0000269|PubMed:17166836}. +P97334 NKX23_MOUSE Homeobox protein Nkx-2.3 (Homeobox protein NK-2 homolog 3) (Homeobox protein NK-2 homolog C) (Nkx2-C) 362 38,090 Chain (1); Compositional bias (4); DNA binding (1); Sequence conflict (6) FUNCTION: Transcriptional regulator essential for normal development and functions of the small intestine and spleen. Activates directly MADCAM1 expression. Required for homing of lymphocytes in spleen and mucosa-associated lymphoid tissue. May have a role during pharyngeal organogenesis. {ECO:0000269|PubMed:10790368}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: Expressed in spleen and intestine. Also expressed in salivary gland and tongue. {ECO:0000269|PubMed:12141427}. +Q9EQM3 NKX24_MOUSE Homeobox protein Nkx-2.4 (Homeobox protein NK-2 homolog D) 354 36,225 Chain (1); Compositional bias (3); DNA binding (1) FUNCTION: Probable transcription factor. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. TISSUE SPECIFICITY: In the embryo it is detected in the posterior hypotalamus and later in the head. In the adult it is detected only in testis. +Q80YV2 NIPA_MOUSE Nuclear-interacting partner of ALK (Nuclear-interacting partner of anaplastic lymphoma kinase) (mNIPA) (Zinc finger C3HC-type protein 1) 501 55,196 Alternative sequence (1); Chain (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (21); Motif (1); Region (1); Sequence conflict (1); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: Essential component of a SCF-type E3 ligase complex, SCF(NIPA), a complex that controls mitotic entry by mediating ubiquitination and subsequent degradation of cyclin B1 (CCNB1). Its cell-cycle-dependent phosphorylation regulates the assembly of the SCF(NIPA) complex, restricting CCNB1 ubiquitination activity to interphase. Its inactivation results in nuclear accumulation of CCNB1 in interphase and premature mitotic entry (By similarity). Overexpression may be able to protect from apoptosis induced by IL-3 withdrawal. {ECO:0000250}. PTM: Phosphorylated. Phosphorylated on Ser residues at G2/M phase, but not during S and G0 phases. May also be weakly phosphorylated on Tyr residues. Ser-353 phosphorylation, a major site during the course of cell-cycle-dedendent phosphorylation, results in its dissociation from the SCF(NIPA) complex, thereby preventing CCNB1 degradation leading to mitotic entry (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with SKP1. Component of a SCF(NIPA) E3 complex with SKP1, RBX1 and CUL1 when not phosphorylated on Ser-353. Interacts with CCNB1 (By similarity). {ECO:0000250}. DOMAIN: The F-box-like region is required for the interaction with SKP1. {ECO:0000250}. +Q3UFM5 NOM1_MOUSE Nucleolar MIF4G domain-containing protein 1 (SGD1 homolog) 854 95,960 Chain (1); Domain (2); Modified residue (4); Motif (1); Region (1); Sequence conflict (1) FUNCTION: Plays a role in targeting PPP1CA to the nucleolus. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. SUBUNIT: May interact with EIF4A1, EIF4A2 and EIF4A3. Interacts with PPP1CA and PPP1CC (By similarity). {ECO:0000250}. +P60954 NOL4_MOUSE Nucleolar protein 4 483 53,479 Alternative sequence (3); Chain (1); Erroneous initiation (1) SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. +O88998 NOE1_MOUSE Noelin (Neuronal olfactomedin-related ER localized protein) (Olfactomedin-1) (Pancortin) 485 55,398 Alternative sequence (3); Beta strand (23); Chain (1); Coiled coil (1); Disulfide bond (2); Domain (1); Glycosylation (8); Helix (2); Motif (1); Mutagenesis (1); Sequence conflict (3); Signal peptide (1); Turn (6) FUNCTION: Contributes to the regulation of axonal growth in the embryonic and adult central nervous system by inhibiting interactions between RTN4R and LINGO1. Inhibits RTN4R-mediated axon growth cone collapse (PubMed:22923615). May play an important role in regulating the production of neural crest cells by the neural tube (By similarity). May be required for normal responses to olfactory stimuli (PubMed:26107991). {ECO:0000250|UniProtKB:Q9IAK4, ECO:0000269|PubMed:22923615, ECO:0000269|PubMed:26107991}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22923615, ECO:0000305|PubMed:22632720}. Cell junction, synapse {ECO:0000305|PubMed:22632720}. Endoplasmic reticulum {ECO:0000269|PubMed:22923615}. Cell projection, axon {ECO:0000269|PubMed:22923615, ECO:0000269|PubMed:26107991}. Perikaryon {ECO:0000269|PubMed:22923615}.; SUBCELLULAR LOCATION: Isoform 1: Endoplasmic reticulum {ECO:0000269|PubMed:9473566, ECO:0000305|PubMed:25903135}. SUBUNIT: Homotetramer; disulfide-linked. Dimer of dimers, giving rise to a V-shaped homotretramer (PubMed:25903135). Isoform 1 and isoform 3 interact with RTN4R (PubMed:22923615). Identified in a complex with RTN4R and LINGO1 (PubMed:22923615). Peripherally associated with AMPAR complex. AMPAR complex consists of an inner core made of 4 pore-forming GluA/GRIA proteins (GRIA1, GRIA2, GRIA3 and GRIA4) and 4 major auxiliary subunits arranged in a twofold symmetry. One of the two pairs of distinct binding sites is occupied either by CNIH2, CNIH3 or CACNG2, CACNG3. The other harbors CACNG2, CACNG3, CACNG4, CACNG8 or GSG1L. This inner core of AMPAR complex is complemented by outer core constituents binding directly to the GluA/GRIA proteins at sites distinct from the interaction sites of the inner core constituents. Outer core constituents include at least PRRT1, PRRT2, CKAMP44/SHISA9, FRRS1L and NRN1. The proteins of the inner and outer core serve as a platform for other, more peripherally associated AMPAR constituents, including OLFM1. Alone or in combination, these auxiliary subunits control the gating and pharmacology of the AMPAR complex and profoundly impact their biogenesis and protein processing (PubMed:22632720). Interacts with OLFM2 (By similarity). {ECO:0000250|UniProtKB:Q99784, ECO:0000269|PubMed:22632720, ECO:0000269|PubMed:22923615, ECO:0000269|PubMed:25903135}. DOMAIN: The protein contains a globular N-terminal tetramerization domain, a long stalk formed by the coiled coil region and a C-terminal olfactomedin-like domain. Interactions between dimers are mediated by the coiled coil region. The dimers interact mostly via the N-terminal tetramerization domain, giving rise to a V-shaped overall architecture of the tetramer. {ECO:0000269|PubMed:25903135}. TISSUE SPECIFICITY: Expressed in the brain cortex, olfactory bulb and vomeronasal neuroepithelium (at protein level) (PubMed:9473566, PubMed:26107991, PubMed:22923615, PubMed:22632720). Detected in brain cortex, hippocampus, dorsal root ganglion and olfactory bulb (PubMed:9473566, PubMed:22923615). {ECO:0000269|PubMed:22632720, ECO:0000269|PubMed:22923615, ECO:0000269|PubMed:26107991, ECO:0000269|PubMed:9473566}. +P63056 NOE3_MOUSE Noelin-3 (Olfactomedin-3) (Optimedin) 478 54,886 Alternative sequence (1); Chain (1); Coiled coil (1); Disulfide bond (1); Domain (1); Glycosylation (5); Sequence conflict (2); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22632720}. Cell junction, synapse {ECO:0000305|PubMed:22632720}. Note=Isoform 2 is secreted more efficiently than isoform 1. SUBUNIT: Peripherally associated with AMPAR complex. AMPAR complex consists of an inner core made of 4 pore-forming GluA/GRIA proteins (GRIA1, GRIA2, GRIA3 and GRIA4) and 4 major auxiliary subunits arranged in a twofold symmetry. One of the two pairs of distinct binding sites is occupied either by CNIH2, CNIH3 or CACNG2, CACNG3. The other harbors CACNG2, CACNG3, CACNG4, CACNG8 or GSG1L. This inner core of AMPAR complex is complemented by outer core constituents binding directly to the GluA/GRIA proteins at sites distinct from the interaction sites of the inner core constituents. Outer core constituents include at least PRRT1, PRRT2, CKAMP44/SHISA9, FRRS1L and NRN1. The proteins of the inner and outer core serve as a platform for other, more peripherally associated AMPAR constituents, including OLFM3. Alone or in combination, these auxiliary subunits control the gating and pharmacology of the AMPAR complex and profoundly impact their biogenesis and protein processing (PubMed:22632720). Homodimer. Interacts with MYOC (PubMed:12019210). Interacts with OLFM2 (By similarity). {ECO:0000250|UniProtKB:Q96PB7, ECO:0000269|PubMed:12019210, ECO:0000269|PubMed:22632720}. TISSUE SPECIFICITY: Expressed in the brain (at protein level). {ECO:0000269|PubMed:22632720}. +Q8BJ56 PLPL2_MOUSE Patatin-like phospholipase domain-containing protein 2 (EC 3.1.1.3) (Adipose triglyceride lipase) (Desnutrin) 486 53,657 Active site (2); Alternative sequence (3); Chain (1); Domain (1); Frameshift (1); Glycosylation (1); Modified residue (5); Motif (3); Mutagenesis (3); Sequence conflict (8); Topological domain (2); Transmembrane (1) TRANSMEM 9 29 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 8 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 30 486 Lumenal. {ECO:0000255}. Glycerolipid metabolism; triacylglycerol degradation. FUNCTION: Catalyzes the initial step in triglyceride hydrolysis in adipocyte and non-adipocyte lipid droplets (PubMed:15550674). Also has acylglycerol transacylase activity. May act coordinately with LIPE/HLS within the lipolytic cascade. Regulates adiposome size and may be involved in the degradation of adiposomes. May play an important role in energy homeostasis. May play a role in the response of the organism to starvation, enhancing hydrolysis of triglycerides and providing free fatty acids to other tissues to be oxidized in situations of energy depletion. {ECO:0000269|PubMed:15337759, ECO:0000269|PubMed:15550674, ECO:0000269|PubMed:16150821, ECO:0000269|PubMed:16675698, ECO:0000269|PubMed:16679289, ECO:0000269|PubMed:17074755}. PTM: Phosphorylation at Ser-406 by PKA is increased during fasting and moderate intensity exercise, and moderately increases lipolytic activity. {ECO:0000269|PubMed:15550674, ECO:0000269|PubMed:22733971}. SUBCELLULAR LOCATION: Lipid droplet. Cell membrane; Single-pass type II membrane protein. SUBUNIT: Interacts with ABHD5; this association stimulates PNPLA2 triglyceride hydrolase activity (PubMed:16679289, PubMed:17189257). Interacts with SERPINF1; interacts at one site of interaction (By similarity). Despite a colocalization in lipid droplets, it probably does not interact with PLIN (PubMed:17189257). Interacts with PLIN5; prevents interaction with ABHD5 (PubMed:21148142, PubMed:21393244). Interacts with FAF2 (By similarity). {ECO:0000250|UniProtKB:Q96AD5, ECO:0000269|PubMed:16679289, ECO:0000269|PubMed:17189257, ECO:0000269|PubMed:21148142, ECO:0000269|PubMed:21393244}. TISSUE SPECIFICITY: Expressed at high levels in white and brown adipose tissue, and to a lesser degree in testis and cardiac muscle. Barely detected in liver, spleen, thymus, kidney, skeletal muscle, and brain. Among the white adipose depots, gonadal fat showed the highest level of expression compared with inguinal and renal white adipose tissues. {ECO:0000269|PubMed:15337759, ECO:0000269|PubMed:15550674, ECO:0000269|PubMed:16150821, ECO:0000269|PubMed:16705060}. +Q8BGN5 NPAL3_MOUSE NIPA-like protein 3 410 44,808 Chain (1); Erroneous termination (1); Modified residue (1); Sequence conflict (3); Transmembrane (9) TRANSMEM 37 57 Helical. {ECO:0000255}.; TRANSMEM 80 100 Helical. {ECO:0000255}.; TRANSMEM 105 125 Helical. {ECO:0000255}.; TRANSMEM 139 159 Helical. {ECO:0000255}.; TRANSMEM 175 195 Helical. {ECO:0000255}.; TRANSMEM 206 226 Helical. {ECO:0000255}.; TRANSMEM 244 264 Helical. {ECO:0000255}.; TRANSMEM 275 295 Helical. {ECO:0000255}.; TRANSMEM 304 324 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q3UMZ3 PLPP5_MOUSE Phospholipid phosphatase 5 (EC 3.1.3.4) (Phosphatidic acid phosphatase type 2 domain-containing protein 1B) 260 29,223 Alternative sequence (2); Chain (1); Region (3); Transmembrane (5) TRANSMEM 51 71 Helical. {ECO:0000255}.; TRANSMEM 87 107 Helical. {ECO:0000255}.; TRANSMEM 151 171 Helical. {ECO:0000255}.; TRANSMEM 176 196 Helical. {ECO:0000255}.; TRANSMEM 206 223 Helical. {ECO:0000255}. FUNCTION: Displays magnesium-independent phosphatidate phosphatase activity in vitro. Catalyzes the conversion of phosphatidic acid to diacylglycerol (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9D4F2 PLPP6_MOUSE Phospholipid phosphatase 6 (EC 3.1.3.-) (Phosphatidic acid phosphatase type 2 domain-containing protein 2) (Presqualene diphosphate phosphatase) 292 31,744 Chain (1); Modified residue (2); Transmembrane (4) TRANSMEM 132 152 Helical. {ECO:0000255}.; TRANSMEM 162 182 Helical. {ECO:0000255}.; TRANSMEM 226 246 Helical. {ECO:0000255}.; TRANSMEM 258 278 Helical. {ECO:0000255}. FUNCTION: Phosphatase that dephosphorylates presqualene diphosphate (PSDP) into presqualene monophosphate (PSMP), suggesting that it may be indirectly involved in innate immunity. PSDP is a bioactive lipid that rapidly remodels to presqualene monophosphate PSMP upon cell activation. Displays diphosphate phosphatase activity with a substrate preference for PSDP > FDP > phosphatidic acid (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q91WB2 PLPP7_MOUSE Inactive phospholipid phosphatase 7 (Nuclear envelope transmembrane protein 39) (Phosphatidic acid phosphatase type 2 domain-containing protein 3) 271 29,710 Chain (1); Modified residue (2); Region (1); Topological domain (5); Transmembrane (4) TRANSMEM 113 133 Helical. {ECO:0000255}.; TRANSMEM 142 162 Helical. {ECO:0000255}.; TRANSMEM 203 223 Helical. {ECO:0000255}.; TRANSMEM 240 260 Helical. {ECO:0000255}. TOPO_DOM 1 112 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 134 141 Extracellular. {ECO:0000255}.; TOPO_DOM 163 202 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 224 239 Extracellular. {ECO:0000255}.; TOPO_DOM 261 271 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a role as negative regulator of myoblast differentiation, in part through effects on MTOR signaling. Has no detectable enzymatic activity. Knockdown in myoblasts strongly promotes differentiation, whereas overexpression represses myogenesis. {ECO:0000269|PubMed:19704009}. SUBCELLULAR LOCATION: Nucleus envelope. Endoplasmic reticulum membrane. Membrane; Multi-pass membrane protein. Note=Both the N- and C-terminal are exposed to the cytoplasm/nucleoplasm. SUBUNIT: Homo- and heterooligomer. Interacts with MTOR; controls MTOR-dependent IGF2 expression during myoblast differentiation. {ECO:0000269|PubMed:19704009}. TISSUE SPECIFICITY: Highly expressed in heart and muscle. {ECO:0000269|PubMed:17062158, ECO:0000269|PubMed:19704009}. +Q8R116 NOTUM_MOUSE Palmitoleoyl-protein carboxylesterase NOTUM (EC 3.1.1.98) 503 56,584 Active site (3); Alternative sequence (2); Chain (1); Compositional bias (1); Glycosylation (1); Modified residue (1); Mutagenesis (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Carboxylesterase that acts as a key negative regulator of the Wnt signaling pathway by specifically mediating depalmitoleoylation of WNT proteins. Serine palmitoleoylation of WNT proteins is required for efficient binding to frizzled receptors. {ECO:0000269|PubMed:25771893}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9VUX3}. TISSUE SPECIFICITY: Widely expressed. Expressed in lung, ovary, kidney, liver and brain. Not detected in thymus, heart, spleen, stomach, skeletal muscle and bone marrow. {ECO:0000269|PubMed:17967162}. +Q8BMA5 NPAT_MOUSE Protein NPAT 1420 152,176 Chain (1); Cross-link (3); Domain (1); Modified residue (11); Region (9); Sequence conflict (1) FUNCTION: Required for progression through the G1 and S phases of the cell cycle and for S phase entry. Activates transcription of the histone H2A, histone H2B, histone H3 and histone H4 genes in conjunction with MIZF. Also positively regulates the ATM, MIZF and PRKDC promoters. Transcriptional activation may be accomplished at least in part by the recruitment of the NuA4 histone acetyltransferase (HAT) complex to target gene promoters (By similarity). Required for early embryonic development. {ECO:0000250, ECO:0000269|PubMed:9199343}. PTM: Phosphorylated at Ser-771, Ser-773, Ser-1096, Thr-1264 and Thr-1343 by CCNE1/CDK2 at G1-S transition and until prophase, which promotes association with histone gene clusters and stimulates activation of histone transcription. Also phosphorylated by CCNA1/CDK2 in vitro (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17003125}. Note=Concentrates in Cajal bodies tethered to histone gene clusters. {ECO:0000250}. SUBUNIT: Interacts with the cylin/CDK complexes CCNE1/CDK2 and CCNA1/CDK2. Interacts with BZW1, CASP8AP2, CREBBP, MIZF and YY1. Interacts with the RUVBL1, RUVBL2 and TRRAP subunits of the NuA4 complex. May also interact with GAPDH, NME1, NME2 and STIP1 (By similarity). {ECO:0000250}. DOMAIN: The LisH domain is required for the activation of histone gene transcription. {ECO:0000250}. +Q6T3U4 NPCL1_MOUSE NPC1-like intracellular cholesterol transporter 1 (Niemann-Pick C1-like protein 1) 1333 147,132 Chain (1); Compositional bias (2); Disulfide bond (14); Domain (1); Sequence conflict (1); Signal peptide (1); Topological domain (14); Transmembrane (13) TRANSMEM 285 305 Helical; Name=1. {ECO:0000255}.; TRANSMEM 353 373 Helical; Name=2. {ECO:0000255}.; TRANSMEM 633 653 Helical; Name=3. {ECO:0000255}.; TRANSMEM 666 686 Helical; Name=4. {ECO:0000255}.; TRANSMEM 697 717 Helical; Name=5. {ECO:0000255}.; TRANSMEM 743 763 Helical; Name=6. {ECO:0000255}.; TRANSMEM 777 797 Helical; Name=7. {ECO:0000255}.; TRANSMEM 847 867 Helical; Name=8. {ECO:0000255}.; TRANSMEM 1114 1134 Helical; Name=9. {ECO:0000255}.; TRANSMEM 1143 1163 Helical; Name=10. {ECO:0000255}.; TRANSMEM 1166 1186 Helical; Name=11. {ECO:0000255}.; TRANSMEM 1207 1227 Helical; Name=12. {ECO:0000255}.; TRANSMEM 1243 1263 Helical; Name=13. {ECO:0000255}. TOPO_DOM 21 284 Extracellular. {ECO:0000255}.; TOPO_DOM 306 352 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 374 632 Extracellular. {ECO:0000255}.; TOPO_DOM 654 665 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 687 696 Extracellular. {ECO:0000255}.; TOPO_DOM 718 742 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 764 776 Extracellular. {ECO:0000255}.; TOPO_DOM 798 846 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 868 1113 Extracellular. {ECO:0000255}.; TOPO_DOM 1135 1142 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1164 1165 Extracellular. {ECO:0000255}.; TOPO_DOM 1187 1206 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1228 1242 Extracellular. {ECO:0000255}.; TOPO_DOM 1264 1333 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a major role in cholesterol homeostasis. Is critical for the uptake of both phytosterol and cholesterol across the plasma membrane of the intestinal enterocyte. Is the direct molecular target of ezetimibe, a drug that inhibits cholesterol absorption (By similarity). The protein may have a function in the transport of multiple lipids and their homeostasis, and may play a critical role in regulating lipid metabolism. Acts as a negative regulator of NPC2 and down-regulates its expression and secretion by inhibiting its maturation and accelerating its degradation (By similarity). {ECO:0000250, ECO:0000269|PubMed:14976318, ECO:0000269|PubMed:15173162, ECO:0000269|PubMed:15671032}. PTM: Highly glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Apical cell membrane; Multi-pass membrane protein. Cell membrane {ECO:0000250|UniProtKB:Q6T3U3}; Multi-pass membrane protein. Note=Subfractionation of brush border membranes from proximal enterocytes suggests considerable association with the apical membrane fraction. Exists as a predominantly cell surface membrane expressed protein. SUBUNIT: Interacts with RAB11A, MYO5B and RAB11FIP2. Interaction with RAB11A, MYO5B and RAB11FIP2 is required for proper transport to the plasma membrane upon cholesterol depletion (By similarity). Interacts with NPC2 (By similarity). Interacts with LIMA1 (PubMed:29880681). {ECO:0000250, ECO:0000269|PubMed:29880681}. TISSUE SPECIFICITY: Expressed in small intestine, stomach and muscle, along with detectable expression in lung, heart, gall bladder, brain, testis, skin and liver. Expression in liver is extremely low. {ECO:0000269|PubMed:14976318, ECO:0000269|PubMed:15671032}. +Q9JIZ9 PLS3_MOUSE Phospholipid scramblase 3 (PL scramblase 3) (Ca(2+)-dependent phospholipid scramblase 3) 296 31,803 Chain (1); Compositional bias (2); Lipidation (3); Motif (4); Region (1); Topological domain (2); Transmembrane (1) TRANSMEM 267 283 Helical. {ECO:0000255}. TOPO_DOM 1 266 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 284 296 Extracellular. {ECO:0000250}. FUNCTION: May mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions that results in a loss of phospholipid asymmetry in the plasma membrane. May play a central role in the initiation of fibrin clot formation, in the activation of mast cells and in the recognition of apoptotic and injured cells by the reticuloendothelial system. Seems to play a role in apoptosis, through translocation of cardiolipin from the inner to the outer mitochondrial membrane which promotes BID recruitment and enhances tBid-induced mitochondrial damages. {ECO:0000269|PubMed:19428821}. SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. SUBUNIT: Interacts with PDCD6 in a calcium-dependent manner. {ECO:0000250}. DOMAIN: The Proline-rich domain is required for phospholipid scramblase activity. {ECO:0000250}. +Q99MD9 NASP_MOUSE Nuclear autoantigenic sperm protein (NASP) 773 83,954 Alternative sequence (2); Chain (1); Coiled coil (2); Compositional bias (1); Cross-link (1); Initiator methionine (1); Modified residue (30); Motif (1); Region (3); Repeat (4); Sequence conflict (3) FUNCTION: Required for DNA replication, normal cell cycle progression and cell proliferation. Forms a cytoplasmic complex with HSP90 and linker H1 histones and stimulates HSP90 ATPase activity. NASP and H1 histone are subsequently released from the complex and translocate to the nucleus where the histone is released for binding to DNA. {ECO:0000269|PubMed:12509435, ECO:0000269|PubMed:15533935, ECO:0000269|PubMed:16728391}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10893414, ECO:0000269|PubMed:12509435, ECO:0000269|PubMed:16728391}. Nucleus {ECO:0000269|PubMed:10893414, ECO:0000269|PubMed:12509435, ECO:0000269|PubMed:16728391}. SUBUNIT: Binds to linker H1 histones but not to core histones (PubMed:10893414, PubMed:12509435). Interacts with histones H2A, H2B, H3 and H4 (By similarity). Also binds to HSP90 in the cytoplasm (PubMed:15533935). This interaction stimulates binding of NASP to HIST1H1T/H1T (PubMed:15533935). {ECO:0000250|UniProtKB:P49321, ECO:0000269|PubMed:10893414, ECO:0000269|PubMed:12509435, ECO:0000269|PubMed:15533935}. TISSUE SPECIFICITY: Isoform 1 is found in gametes, embryonic cells and transformed cells. Isoform 2 is found in dividing somatic cells (at protein level). {ECO:0000269|PubMed:10893414}. +Q09014 NCF1_MOUSE Neutrophil cytosol factor 1 (NCF-1) (47 kDa neutrophil oxidase factor) (NCF-47K) (Neutrophil NADPH oxidase factor 1) (p47-phox) 390 44,667 Chain (1); Compositional bias (2); Domain (3); Modified residue (4); Sequence conflict (3) FUNCTION: NCF2, NCF1, and a membrane bound cytochrome b558 are required for activation of the latent NADPH oxidase (necessary for superoxide production). {ECO:0000250|UniProtKB:P14598, ECO:0000269|PubMed:9490028}. PTM: Phosphorylated by PRKCD; phosphorylation induces activation of NCF1 and NADPH oxidase activity. {ECO:0000250|UniProtKB:P14598, ECO:0000269|PubMed:26021615}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:26021615}. Membrane {ECO:0000269|PubMed:26021615}; Peripheral membrane protein {ECO:0000250|UniProtKB:P14598}; Cytoplasmic side {ECO:0000250|UniProtKB:P14598}. SUBUNIT: Component of an NADPH oxidase complex composed of a heterodimer formed by the membrane proteins CYBA and CYBB and the cytosolic subunits NCF1, NCF2 and NCF4. Interacts (via C-terminus) with NCF2 (via the C-terminal SH3 domain). Interacts with NCF4. Interacts with CYBB. Interacts (via the second SH3 domain) with CYBA. Interacts with NOXA1. Interacts with ADAM15. Interacts with TRAF4. Interacts with FASLG (By similarity). Interacts with PARK7 (via C-terminus); the interaction is enhanced by LPS and modulates NCF1 phosphorylation and membrane translocation (PubMed:26021615). {ECO:0000250|UniProtKB:P14598, ECO:0000269|PubMed:26021615}. DOMAIN: The PX domain mediates interaction with phosphatidylinositol 3,4-bisphosphate and other anionic phospholipids. In the autoinhibited, unphosphorylated state an intramolecular interaction with the C-terminal SH3 domain precludes phospholipid binding and interaction with CYBA. Phosphorylation disrupts the autoinhibited state (By similarity). {ECO:0000250|UniProtKB:P14598}. +Q61477 NBL1_MOUSE Neuroblastoma suppressor of tumorigenicity 1 (N03) (Zinc finger protein DAN) 178 19,107 Chain (1); Compositional bias (1); Disulfide bond (5); Domain (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Possible candidate as a tumor suppressor gene of neuroblastoma. May play an important role in preventing cells from entering the final stage (G1/S) of the transformation process. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23063586}. SUBUNIT: Homodimer. {ECO:0000269|PubMed:23063586}. +Q99PD7 NCKX3_MOUSE Sodium/potassium/calcium exchanger 3 (Na(+)/K(+)/Ca(2+)-exchange protein 3) (Solute carrier family 24 member 3) 645 71,942 Chain (1); Compositional bias (1); Glycosylation (2); Modified residue (1); Repeat (2); Sequence conflict (1); Signal peptide (1); Topological domain (11); Transmembrane (10) TRANSMEM 107 127 Helical. {ECO:0000255}.; TRANSMEM 152 172 Helical. {ECO:0000255}.; TRANSMEM 182 202 Helical. {ECO:0000255}.; TRANSMEM 210 230 Helical. {ECO:0000255}.; TRANSMEM 235 255 Helical. {ECO:0000255}.; TRANSMEM 487 507 Helical. {ECO:0000255}.; TRANSMEM 513 533 Helical. {ECO:0000255}.; TRANSMEM 552 572 Helical. {ECO:0000255}.; TRANSMEM 583 603 Helical. {ECO:0000255}.; TRANSMEM 618 638 Helical. {ECO:0000255}. TOPO_DOM 44 106 Extracellular. {ECO:0000255}.; TOPO_DOM 128 151 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 173 181 Extracellular. {ECO:0000255}.; TOPO_DOM 203 209 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 231 234 Extracellular. {ECO:0000255}.; TOPO_DOM 256 486 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 508 512 Extracellular. {ECO:0000255}.; TOPO_DOM 534 551 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 573 582 Extracellular. {ECO:0000255}.; TOPO_DOM 604 617 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 639 645 Extracellular. {ECO:0000255}. FUNCTION: Transports 1 Ca(2+) and 1 K(+) in exchange for 4 Na(+). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Abundant in the brain. Highest levels found in selected thalamic nuclei, hippocampal CA1 neurons and in layer IV of the cerebral cortex. Expressed in dental tissues. {ECO:0000269|PubMed:22677781}. +Q9Z1J3 NFS1_MOUSE Cysteine desulfurase, mitochondrial (m-Nfs1) (EC 2.8.1.7) 459 50,570 Active site (1); Binding site (3); Chain (1); Metal binding (1); Modified residue (1); Region (2); Sequence conflict (3); Transit peptide (1) FUNCTION: Catalyzes the removal of elemental sulfur from cysteine to produce alanine. It supplies the inorganic sulfur for iron-sulfur (Fe-S) clusters. May be involved in the biosynthesis of molybdenum cofactor (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:9738949}. Cytoplasm {ECO:0000250|UniProtKB:Q9Y697}. Nucleus {ECO:0000250|UniProtKB:Q9Y697}. SUBUNIT: Binds ISCU/NIFUN. Forms a complex with LYRM4. Interacts with HSPA9. {ECO:0000250|UniProtKB:Q9Y697}. TISSUE SPECIFICITY: Ubiquitous. +O35684 NEUS_MOUSE Neuroserpin (Peptidase inhibitor 12) (PI-12) (Serine protease inhibitor 17) (Serpin I1) 410 46,348 Beta strand (18); Chain (1); Glycosylation (3); Helix (8); Sequence conflict (1); Signal peptide (1); Site (1); Turn (4) FUNCTION: Serine protease inhibitor that inhibits plasminogen activators and plasmin but not thrombin (PubMed:9364046, PubMed:11557034). May be involved in the formation or reorganization of synaptic connections as well as for synaptic plasticity in the adult nervous system. May protect neurons from cell damage by tissue-type plasminogen activator (Probable). {ECO:0000269|PubMed:11557034, ECO:0000269|PubMed:9364046, ECO:0000305}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q90935}. Cytoplasmic vesicle, secretory vesicle lumen {ECO:0000269|PubMed:17040209}. Perikaryon {ECO:0000269|PubMed:17040209}. TISSUE SPECIFICITY: Detected in neurons in embryonic brain cortex (at protein level) (PubMed:17040209). During embryonic development mostly expressed in CNS (PubMed:9364046). In adult expressed in brain and much less in spinal cord, heart, kidney and testis (PubMed:9364046). {ECO:0000269|PubMed:17040209, ECO:0000269|PubMed:9364046}. +P97350 PKP1_MOUSE Plakophilin-1 728 80,896 Chain (1); Modified residue (2); Repeat (9) FUNCTION: Seems to play a role in junctional plaques. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cell junction, desmosome {ECO:0000250}. Note=Nuclear and associated with desmosomes. {ECO:0000250}. +P23708 NFYA_MOUSE Nuclear transcription factor Y subunit alpha (CAAT box DNA-binding protein subunit A) (Nuclear transcription factor Y subunit A) (NF-YA) 346 36,779 Alternative sequence (1); Chain (1); Compositional bias (1); DNA binding (1); Modified residue (1); Motif (1); Sequence conflict (1) FUNCTION: Component of the sequence-specific heterotrimeric transcription factor (NF-Y) which specifically recognizes a 5'-CCAAT-3' box motif found in the promoters of its target genes. NF-Y can function as both an activator and a repressor, depending on its interacting cofactors. NF-YA positively regulates the transcription of the core clock component ARNTL/BMAL1. {ECO:0000269|PubMed:24030830}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Heterotrimeric transcription factor composed of three components, NF-YA, NF-YB and NF-YC. NF-YB and NF-YC must interact and dimerize for NF-YA association and DNA binding (By similarity). Interacts with SP1; the interaction is inhibited by glycosylation of SP1. Interacts (via N-terminus) with ZHX2 (via homeobox domain). Interacts with ZFX3. Interacts with ZHX1 (By similarity). {ECO:0000250}. +Q07279 NFE2_MOUSE Transcription factor NF-E2 45 kDa subunit (Leucine zipper protein NF-E2) (Nuclear factor, erythroid-derived 2 45 kDa subunit) (p45 NF-E2) 373 41,565 Chain (1); Cross-link (2); Domain (1); Modified residue (2); Motif (2); Mutagenesis (3); Region (4); Sequence conflict (1) FUNCTION: Component of the NF-E2 complex essential for regulating erythroid and megakaryocytic maturation and differentiation. Binds to the hypersensitive site 2 (HS2) of the beta-globin control region (LCR). This subunit (NFE2) recognizes the TCAT/C sequence of the AP-1-like core palindrome present in a number of erythroid and megakaryocytic gene promoters. Requires MAFK or other small MAF proteins for binding to the NF-E2 motif. May play a role in all aspects of hemoglobin production from globin and heme synthesis to procurement of iron. {ECO:0000269|PubMed:9558374}. PTM: Phosphorylated on serine residues. In undifferentiated erythrocytes, phosphorylated by MAPK8 which then leads to ubiquitination and protein degradation (By similarity). {ECO:0000250}.; PTM: Sumoylated. Sumoylation is required for translocation to nuclear bodies PODs, anchoring to the gene loci, and transactivation of the beta-globin gene (By similarity). {ECO:0000250}.; PTM: Ubiquitinated mainly by 'Lys63'-linked ubiquitin (By similarity). Polyubiquitination with 'Lys63'-linked ubiquitin by ITCH retains NFE2 in the cytoplasm preventing its transactivation activity (By similarity). In undifferentiated erythrocyte, ubiquitinated after MAPK8-mediatd phosphorylation leading to protein degradation. {ECO:0000250, ECO:0000269|PubMed:19966288, ECO:0000269|PubMed:9558374}. SUBCELLULAR LOCATION: Nucleus, PML body. Cytoplasm {ECO:0000250}. Note=The sumoylated form locates to the nuclear bodies PML oncogenic domains (PODs). Translocated to the cytoplasm through interaction with ITCH (By similarity). {ECO:0000250}. SUBUNIT: Homodimer; can bind DNA as a homodimer (By similarity). Erythroid transcription activator nuclear factor erythroid-derived 2 (NF-E2), composed of a heterodimer of NFE2 and MAFK, possesses transactivation activity on beta-globin. Also forms high affinity heterodimer with MAFG; the interaction promotes erythropoiesis. Interacts (via the PXY motif 1) with ITCH (via the WW 1 domain); the interaction promotes 'Lys63'-linked ubiquitination of NFE2, translocates it to the cytoplasm and inhibits its transactivation activity. Interacts with KMT2D/MLL2; the interaction promotes transactivation of the beta-globin locus. Interacts with MAPK8 (phosphorylated form); the interaction leads to phosphorylation of NFE2 in undifferentiated cells. {ECO:0000250, ECO:0000269|PubMed:17707229, ECO:0000269|PubMed:19966288}. DOMAIN: The PXY motifs are required for binding WW domains. PXY1 is required to promote transactivation of beta-globin and for hyperacetylation of histone H3, but not for binding to the HS2 promoter site. +Q9JI78 NGLY1_MOUSE Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase (PNGase) (mPNGase) (EC 3.5.1.52) (N-glycanase 1) (Peptide:N-glycanase) 651 74,275 Active site (3); Beta strand (28); Chain (1); Domain (2); Helix (24); Initiator methionine (1); Metal binding (4); Modified residue (1); Mutagenesis (4); Sequence conflict (2); Turn (10) FUNCTION: Specifically deglycosylates the denatured form of N-linked glycoproteins in the cytoplasm and assists their proteasome-mediated degradation. Cleaves the beta-aspartyl-glucosamine (GlcNAc) of the glycan and the amide side chain of Asn, converting Asn to Asp. Prefers proteins containing high-mannose over those bearing complex type oligosaccharides. Can recognize misfolded proteins in the endoplasmic reticulum that are exported to the cytosol to be destroyed and deglycosylate them, while it has no activity toward native proteins. Deglycosylation is a prerequisite for subsequent proteasome-mediated degradation of some, but not all, misfolded glycoproteins. {ECO:0000269|PubMed:11562482, ECO:0000269|PubMed:12606569, ECO:0000269|PubMed:15358861}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11562482, ECO:0000269|PubMed:12606569, ECO:0000269|PubMed:16055502}. SUBUNIT: Component of a complex required to couple retrotranslocation, ubiquitination and deglycosylation composed of NGLY1, SAKS1, AMFR, VCP and RAD23B. Interacts with the proteasome components RAD23B and PSMC1. Interacts with directly with VCP. Interacts with DERL1, bringing it close to the endoplasmic reticulum membrane. Interacts with SAKS1. {ECO:0000269|PubMed:11562482, ECO:0000269|PubMed:15358861, ECO:0000269|PubMed:16055502, ECO:0000269|PubMed:16249333, ECO:0000269|PubMed:16500903, ECO:0000269|PubMed:16709668}. DOMAIN: The PUB domain mediates the interaction with VCP. {ECO:0000269|PubMed:16709668}. TISSUE SPECIFICITY: Ubiquitously expressed with highest level in testis. {ECO:0000269|PubMed:11562482, ECO:0000269|PubMed:12711318}. +P70660 NGN1_MOUSE Neurogenin-1 (NGN-1) (Helix-loop-helix protein mATH-4C) (mATH4C) (Neurogenic basic-helix-loop-helix protein) (Neurogenic differentiation factor 3) (NeuroD3) 244 26,300 Chain (1); Domain (1) FUNCTION: Acts as a transcriptional regulator. Involved in the initiation of neuronal differentiation. Activates transcription by binding to the E box (5'-CANNTG-3'). Associates with chromatin to enhancer regulatory elements in genes encoding key transcriptional regulators of neurogenesis. {ECO:0000269|PubMed:10648228, ECO:0000269|PubMed:14697366, ECO:0000269|PubMed:18007592}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Efficient DNA binding requires dimerization with another bHLH protein. TISSUE SPECIFICITY: Expression restricted to the embryonic nervous system. +O08692 NGP_MOUSE Neutrophilic granule protein (NGP) (Cystatin-like protein) (Myeloid bactenecin protein) (Myeloid secondary granule protein) 167 19,332 Chain (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Acts as an inhibitor of cathepsin B (CTSB) activity. Plays a role as a negative regulator of tumor vascular development, cell invasion and metastasis. {ECO:0000269|PubMed:21518852}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21518852}. Cytoplasmic granule {ECO:0000269|PubMed:8749713}. Note=Localizes in cytoplasmic granules of neutrophilic precursors (PubMed:8749713). {ECO:0000269|PubMed:21518852, ECO:0000269|PubMed:8749713}. SUBUNIT: Monomer. Homodimer; disulfide-linked. {ECO:0000269|PubMed:21518852}. TISSUE SPECIFICITY: Expressed in myeloid bone marrow cells. Expressed in neutrophilic precursors (at protein level) (PubMed:8749713). Expressed in myeloid bone marrow cells (PubMed:21518852). {ECO:0000269|PubMed:21518852, ECO:0000269|PubMed:8749713}. +Q3KNJ2 NHEJ1_MOUSE Non-homologous end-joining factor 1 (Protein cernunnos) (XRCC4-like factor) 295 32,739 Alternative sequence (1); Chain (1); Coiled coil (1); Erroneous initiation (1); Modified residue (1); Region (1); Sequence conflict (2) FUNCTION: DNA repair protein involved in DNA nonhomologous end joining (NHEJ) required for double-strand break (DSB) repair and V(D)J recombination. May serve as a bridge between XRCC4 and the other NHEJ factors located at DNA ends, or may participate in reconfiguration of the end bound NHEJ factors to allow XRCC4 access to the DNA termini. It may act in concert with XRCC6/XRCC5 (Ku) to stimulate XRCC4-mediated joining of blunt ends and several types of mismatched ends that are noncomplementary or partially complementary (PubMed:17360556). Binds DNA in a length-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q9H9Q4, ECO:0000269|PubMed:17360556}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Exists mainly as a homodimer. Associates with the non-homologous end joining (NHEJ) complex which is at least composed of the core proteins XRCC5/Ku80, XRCC6/Ku70, PRKDC/DNA-PKcs, LIG4 and XRCC4. {ECO:0000250|UniProtKB:Q9H9Q4}. DOMAIN: The coiled-coil region mediates homodimerization. {ECO:0000250}. +Q8BR37 NHLC1_MOUSE E3 ubiquitin-protein ligase NHLRC1 (EC 2.3.2.27) (Malin) (NHL repeat-containing protein 1) (RING-type E3 ubiquitin transferase NHLRC1) 401 42,690 Chain (1); Repeat (6); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase. Together with the phosphatase EPM2A/laforin, appears to be involved in the clearance of toxic polyglucosan and protein aggregates via multiple pathways. In complex with EPM2A/laforin and HSP70, suppresses the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system (UPS). Ubiquitinates the glycogen-targeting protein phosphatase subunits PPP1R3C/PTG and PPP1R3D in a laforin-dependent manner and targets them for proteasome-dependent degradation, thus decreasing glycogen accumulation. Polyubiquitinates EPM2A/laforin and ubiquitinates AGL and targets them for proteasome-dependent degradation. Also promotes proteasome-independent protein degradation through the macroautophagy pathway. {ECO:0000269|PubMed:19036738, ECO:0000269|PubMed:21077101, ECO:0000269|PubMed:22186026, ECO:0000269|PubMed:22669944}. SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250}. Nucleus {ECO:0000250}. Note=Localizes at the endoplasmic reticulum and, to a lesser extent, in the nucleus. {ECO:0000250}. SUBUNIT: Interacts with AGL. Interacts (via the NHL repeats) with EPM2A/laforin (By similarity). Forms a complex with EPM2A/laforin and HSP70. Interacts with PRDM8 (By similarity). {ECO:0000250|UniProtKB:Q6VVB1}. DOMAIN: The RING domain is essential for ubiquitin E3 ligase activity. {ECO:0000250}. +Q9CQM0 NICN1_MOUSE Nicolin-1 (Tubulin polyglutamylase complex subunit 5) (PGs5) (p24) 213 24,360 Chain (1) SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Part of the neuronal tubulin polyglutamylase complex which contains TPGS1, TPGS2, TTLL1, LRRC49 and NICN1. TISSUE SPECIFICITY: High expression level is found in brain, testis, liver and kidney. Weak expression in spleen, leukocytes, small intestin and colon. {ECO:0000269|PubMed:12392556}. +Q80TM9 NISCH_MOUSE Nischarin (Imidazoline receptor 1) (I-1) (IR1) (Imidazoline receptor I-1-like protein) (Imidazoline-1 receptor) (I1R) 1593 175,012 Alternative sequence (10); Chain (1); Coiled coil (1); Compositional bias (2); Domain (1); Erroneous initiation (3); Frameshift (1); Modified residue (5); Region (6); Repeat (16); Sequence conflict (4) FUNCTION: Acts either as the functional imidazoline-1 receptor (I1R) candidate or as a membrane-associated mediator of the I1R signaling. Binds numerous imidazoline ligands that induces initiation of cell-signaling cascades triggering to cell survival, growth and migration. Its activation by the agonist rilmenidine induces an increase in phosphorylation of mitogen-activated protein kinases MAPK1 and MAPK3 in rostral ventrolateral medulla (RVLM) neurons that exhibited rilmenidine-evoked hypotension (By similarity). Blocking its activation with efaroxan abolished rilmenidine-induced mitogen-activated protein kinase phosphorylation in RVLM neurons (By similarity). Acts as a modulator of Rac-regulated signal transduction pathways. Suppresses Rac1-stimulated cell migration by interacting with PAK1 and inhibiting its kinase activity. Also blocks Pak-independent Rac signaling by interacting with RAC1 and inhibiting Rac1-stimulated NF-kB response element and cyclin D1 promoter activation. Inhibits also LIMK1 kinase activity by reducing LIMK1 'Tyr-508' phosphorylation. Inhibits Rac-induced cell migration and invasion in breast and colon epithelial cells. Inhibits lamellipodia formation, when overexpressed. Plays a role in protection against apoptosis (By similarity). Involved in association with IRS4 in the enhancement of insulin activation of MAPK1 and MAPK3 (By similarity). When overexpressed, induces a redistribution of cell surface ITGA5 integrin to intracellular endosomal structures (By similarity). {ECO:0000250, ECO:0000269|PubMed:11121431, ECO:0000269|PubMed:12915132, ECO:0000269|PubMed:15229651, ECO:0000269|PubMed:16002401, ECO:0000269|PubMed:16678176, ECO:0000269|PubMed:18332102}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:11121431, ECO:0000269|PubMed:15229651, ECO:0000269|PubMed:16002401, ECO:0000269|PubMed:16678176}. Early endosome {ECO:0000250}. Recycling endosome {ECO:0000250}. Note=Enriched in the early/sorting and recycling endosomes (By similarity). Colocalized in early/sorting endosomes with EEA1 and SNX2 and in recycling endosomes with transferrin receptor (By similarity). Colocalized with MAPK1 and MAPK3 in RVLM neurons (By similarity). Detected in the perinuclear region partially associated with punctate structures. Colocalizes with PAK1 in cytoplasm, vesicular structures in the perinuclear area and membrane ruffles. Colocalizes with RAC1 in the cytoplasm and vesicles structures. {ECO:0000250}. SUBUNIT: Homooligomer (By similarity). Interacts with GRB2 (By similarity). Interacts with PIK3R1; probably associates with the PI3-kinase complex (By similarity). Interacts with IRS4 (By similarity). Found in a complex with ITGA5 and PAK1. Found in a complex with LIMK1 and PAK1. Interacts with ITGA5 (via cytoplasmic domain); this interaction is direct. Interacts with PAK1 (via kinase domain); this interaction is direct and is increased upon activation of PAK1. Interacts with LIMK1 (via PDZ and kinase domain); this interaction is direct. Interacts with LIMK2; this interaction depends on LIMK2 activity. Interacts with RAC1 (activated state). Interacts with STK11; this interaction may increase STK11 activity (By similarity). {ECO:0000250}. DOMAIN: Both the presence of the PX domain and the coiled coil region are necessary for its endosomal targeting. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in brain and kidney. Moderately expressed in heart, liver, lung and skeletal muscle. Not detected in spleen and testis. {ECO:0000269|PubMed:11121431}. +Q9JMG4 NKAI4_MOUSE Sodium/potassium-transporting ATPase subunit beta-1-interacting protein 4 (Na(+)/K(+)-transporting ATPase subunit beta-1-interacting protein 4) (Protein FAM77A) 208 23,042 Alternative sequence (2); Chain (1); Sequence conflict (2); Transmembrane (3) TRANSMEM 35 55 Helical. {ECO:0000255}.; TRANSMEM 62 82 Helical. {ECO:0000255}.; TRANSMEM 151 171 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Interacts with ATP1B1. {ECO:0000269|PubMed:17606467}. TISSUE SPECIFICITY: Ubiquitous. Expressed in multiple regions of the brain such as cerebral cortex, thalamus, hippocampus, olfactory bulb and brainstem as well as in cerebellum with low expression in granular cell layer. {ECO:0000269|PubMed:17606467}. +Q2LKV2 NL1B4_MOUSE NACHT, LRR and PYD domains-containing protein 1b allele 4 906 103,119 Alternative sequence (2); Chain (1); Domain (2); Nucleotide binding (1); Repeat (2) FUNCTION: As the sensor component of the NLRP1 inflammasome, plays a crucial role in innate immunity and inflammation. In response to pathogens and other damage-associated signals, initiates the formation of the inflammasome polymeric complex, made of Nlrp1b, CASP1, and possibly PYCARD. Recruitment of proCASP1 to the inflammasome promotes its activation and CASP1-catalyzed IL1B and IL18 maturation and secretion in the extracellular milieu. Activation of NLRP1 inflammasome is also required for HMGB1 secretion. The active cytokines and HMGB1 stimulate inflammatory responses. Inflammasomes can also induce pyroptosis, an inflammatory form of programmed cell death (By similarity). Contrary to Nlrp1b allele 1, allele 4 is not activated by Bacillus anthracis lethal toxin and no other activation signal is reported (PubMed:16429160). In addition, allele 4 is missing a CARD domain, which has been shown in other alleles to be involved in the interaction with PYCARD, CASP1 and CASP4/CASP11. It is thus unclear if this allele is able to promote inflammasome assembly. {ECO:0000250|UniProtKB:Q2LKW6, ECO:0000269|PubMed:16429160, ECO:0000305}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9C000}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9C000}. Inflammasome {ECO:0000250|UniProtKB:Q2LKW6}. SUBUNIT: Sensor component of NLRP1 inflammasomes. Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other damage-associated signals and play critical roles in innate immunity and inflammation. Classical inflammasomes consist of a signal sensor component, an adapter (ASC/PYCARD), which recruits an effector proinflammatory caspase (CASP1 and possibly CASP4/CASP11). CASP1 filament formation increases local enzyme concentration, resulting in trans-autocleavage and activation. Active CASP1 then processes IL1B and IL18 precursors, leading to the release of mature cytokines in the extracellular milieu and inflammatory response. In NLRP1 inflammasome, the role of PYCARD is not clear. Following activation, Nlrp1b may directly interact with CASP1 to form a functional inflammasome. Hence PYCARD may not be necessary for NLRP1 and CASP1 interaction, but is required for speck formation and full inflammasome activity (By similarity). However, allele 4 is missing a CARD domain, which has been shown in other alleles to be involved in the interaction with PYCARD, CASP1 and CASP4/CASP11. It is thus unclear if this allele is able to promote inflammasome assembly (Probable). Homomer (By similarity). Interacts (via LRR repeats) with BCL2 and BCL2L1 (via the loop between motifs BH4 and BH3); these interactions reduce NLRP1 inflammasome-induced CASP1 activation and IL1B release, possibly by impairing NLRP1 interaction with PYCARD. Interacts with NOD2; this interaction may increase IL1B release. Interacts with EIF2AK2/PKR; this interaction requires EIF2AK2 activity, is accompanied by EIF2AK2 autophosphorylation and promotes inflammasome assembly in response to danger-associated signals. Interacts with MEFV; this interaction targets NLRP1 to degradation by autophagy, hence preventing excessive IL1B- and IL18-mediated inflammation (By similarity). {ECO:0000250|UniProtKB:Q2LKW6, ECO:0000250|UniProtKB:Q9C000, ECO:0000305}. DOMAIN: Contrary to Nlrp1b alleles 1, 2, 3 and 5, allele 4 is missing a CARD domain, which has been shown in other alleles to be involved in the interaction with PYCARD, CASP1 and CASP4/CASP11. It is thus unclear if this allele is able to promote inflammasome assembly. {ECO:0000305}.; DOMAIN: The leucine-rich repeat (LRR) domain may be involved in autoinhibition in the absence of activating signal, possibly through intramolecular interaction with the NACHT domain. {ECO:0000250|UniProtKB:Q2LKW6}.; DOMAIN: The FIIND (domain with function to find) region may be involved in homomerization, but not in CASP1-binding. In allele 4, the FIIND region is truncated and hence does not contain the activating cleavage reported for allele 1. Consequently, it may not undergo autocatalytic cleavage in this region. {ECO:0000305}. TISSUE SPECIFICITY: Expressed in macrophages. {ECO:0000269|PubMed:16429160, ECO:0000269|PubMed:23506131}. +P49764 PLGF_MOUSE Placenta growth factor (PlGF) 158 17,876 Chain (1); Disulfide bond (5); Glycosylation (3); Signal peptide (1) FUNCTION: Growth factor active in angiogenesis and endothelial cell growth, stimulating their proliferation and migration. It binds to the receptor FLT1/VEGFR-1. Also promotes cell tumor growth (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Antiparallel homodimer; disulfide-linked. Also found as heterodimer with VEGFA/VEGF (By similarity). {ECO:0000250}. +Q9D1X0 NOL3_MOUSE Nucleolar protein 3 (Apoptosis repressor with CARD) 220 24,568 Chain (1); Compositional bias (1); Domain (1); Initiator methionine (1); Lipidation (1); Modified residue (1); Mutagenesis (2); Region (1) FUNCTION: Apoptosis repressor that blocks multiple modes of cell death. Inhibits extrinsic apoptotic pathways through two different ways. Firstly by interacting with FAS and FADD upon FAS activation blocking death-inducing signaling complex (DISC) assembly (By similarity). Secondly by interacting with CASP8 in a mitochondria localization- and phosphorylation-dependent manner, limiting the amount of soluble CASP8 available for DISC-mediated activation (By similarity). Inhibits intrinsic apoptotic pathway in response to a wide range of stresses, through its interaction with BAX resulting in BAX inactivation, preventing mitochondrial dysfunction and release of pro-apoptotic factors (PubMed:16505176) (PubMed:24312627). Inhibits calcium-mediated cell death by functioning as a cytosolic calcium buffer, dissociating its interaction with CASP8 and maintaining calcium homeostasis (By similarity). Negatively regulates oxidative stress-induced apoptosis by phosphorylation-dependent suppression of the mitochondria-mediated intrinsic pathway, by blocking CASP2 activation and BAX translocation (By similarity). Negatively regulates hypoxia-induced apoptosis in part by inhibiting the release of cytochrome c from mitochondria in a caspase-independent manner (By similarity). Also inhibits TNF-induced necrosis by preventing TNF-signaling pathway through TNFRSF1A interaction abrogating the recruitment of RIPK1 to complex I (PubMed:24440909). Finally through its role as apoptosis repressor, promotes vascular remodeling through inhibition of apoptosis and stimulation of proliferation, in response to hypoxia (PubMed:22082675). Inhibits too myoblast differentiation through caspase inhibition (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O60936, ECO:0000250|UniProtKB:Q62881, ECO:0000269|PubMed:16505176, ECO:0000269|PubMed:22082675, ECO:0000269|PubMed:24312627, ECO:0000269|PubMed:24440909}. PTM: Phosphorylation at Thr-149 is required for its antiapoptotic effect by blocking death-inducing signaling complex death-inducing signaling complex (DISC) activity through the control of interaction with CASP8. Phosphorylation at Thr-149 results in translocation to mitochondria and this translocation enables the binding to CASP8. Dephosphorylated at Thr-149 by calcineurin; doesn't inhibit the association between FADD and CASP8 and the consequent apoptosis. {ECO:0000250|UniProtKB:Q62881}.; PTM: Polyubiquitinated by MDM2; promoting proteasomal-dependent degradation in response to apoptotic stimuli. {ECO:0000250|UniProtKB:O60936, ECO:0000250|UniProtKB:Q62881}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O60936, ECO:0000250|UniProtKB:Q62881}. Mitochondrion {ECO:0000250|UniProtKB:Q62881}. Sarcoplasmic reticulum {ECO:0000250|UniProtKB:Q62881}. Membrane {ECO:0000250|UniProtKB:O60936}; Lipid-anchor {ECO:0000250|UniProtKB:O60936}. Note=Phosphorylation at Thr-149 results in translocation to mitochondria. Colocalized with mitochondria in response to oxidative stress. {ECO:0000250|UniProtKB:Q62881}. SUBUNIT: Oligomerizes (via CARD doamin) (By similarity). Interacts (via CARD domain) with CASP2; inhibits CASP2 activity in a phosphorylation-dependent manner (By similarity). Interacts with CASP8; decreases CASP8 activity in a mitochondria localization- and phosphorylation-dependent manner and this interaction is dissociated by calcium. Interacts with TFPT; translocates NOL3 into the nucleus and negatively regulated TFPT-induced cell death (By similarity). Interacts directly (via CARD domain) with FAS and FADD (via DED domain); inhibits death-inducing signaling complex (DISC) assembly by inhibiting the increase in FAS-FADD binding induced by FAS activation. Interacts (via CARD domain) with BAX (via a C-terminal 33 residues); inhibits BAX activation and translocation and consequently cytochrome c release from mitochondria. Interacts with PPM1G; may dephosphorylate NOL3 (By similarity). Interacts (via CARD domain) with BBC3 (via BH3 domain); preventing the association of BBC3 with BCL2 and resulting in activation of CASP8 (By similarity). Interacts (via CARD domain) with BAD(via BH3 domain); preventing the association of BAD with BCL2 (By similarity). Interacts directly (via CARD domain) with TNFRSF1A; inhibits TNF-signaling pathway. {ECO:0000250|UniProtKB:O60936, ECO:0000250|UniProtKB:Q62881, ECO:0000269|PubMed:15383280, ECO:0000269|PubMed:24440909}. DOMAIN: CARD is critical for both extrinsic and intrinsic apoptotic pathways (By similarity). CARD domain mediates a protective effect against myocardial ischemia/reperfusion, oxidative stress and TNF-induced necrosis (PubMed:24440909). The calcium binding domain plays a protective role in calcium-mediated cell death (By similarity). {ECO:0000250|UniProtKB:O60936, ECO:0000250|UniProtKB:Q62881, ECO:0000269|PubMed:24440909}. +Q61066 NR0B1_MOUSE Nuclear receptor subfamily 0 group B member 1 (Nuclear receptor DAX-1) 472 52,576 Chain (1); Domain (1); Helix (10); Motif (4); Region (1); Repeat (4) FUNCTION: Orphan nuclear receptor. Component of a cascade required for the development of the hypothalamic-pituitary-adrenal-gonadal axis. Acts as a coregulatory protein that inhibits the transcriptional activity of other nuclear receptors through heterodimeric interactions. May also have a role in the development of the embryo and in the maintenance of embryonic stem cell pluripotency (By similarity). {ECO:0000250, ECO:0000269|PubMed:16466956}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Shuttles between the cytoplasm and nucleus. Homodimers exits in the cytoplasm and in the nucleus (By similarity). {ECO:0000250}. SUBUNIT: Homodimer. Interacts with NR5A1, NR5A2, NR0B2 and with COPS2 (By similarity). Interacts with ESRRB; represses ESRRB activity at the GATA6 promoter (PubMed:27601327). {ECO:0000250, ECO:0000269|PubMed:27601327}. DOMAIN: Homodimerization involved an interaction between amino and carboxy termini involving LXXLL motifs and steroid binding domain (AF-2 motif). Heterodimerizes with NR5A1 and NROB2 through its N-terminal LXXLL motifs (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in adult cerebral cortex, spinal cord, thymus, heart, lung, ovary, testis, adrenal gland, hypothalamus, spleen and kidney. {ECO:0000269|PubMed:8756567}. +Q8BNX7 NRAC_MOUSE Nutritionally-regulated adipose and cardiac-enriched protein 165 18,347 Chain (1); Sequence conflict (10); Transmembrane (1) TRANSMEM 112 132 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23029450}; Single-pass membrane protein {ECO:0000269|PubMed:23029450}. TISSUE SPECIFICITY: Predominantly expressed in white adipose tissue (at protein level) and brown adipose tissue. Also detected in heart. {ECO:0000269|PubMed:23029450}. +Q8CJ26 NRADD_MOUSE Death domain-containing membrane protein NRADD (Neurotrophin receptor homolog-2) (NRH2) (Neurotrophin receptor-alike death domain protein) 228 24,727 Beta strand (1); Chain (1); Compositional bias (1); Domain (1); Glycosylation (2); Helix (7); Sequence conflict (1); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 53 73 Helical; Signal-anchor for type III membrane protein. {ECO:0000255}. TOPO_DOM 1 52 Extracellular. {ECO:0000305}.; TOPO_DOM 74 228 Cytoplasmic. {ECO:0000305}. FUNCTION: Modulates NTRK1 signaling. Can activate several intracellular signaling pathways, leading to activation of JUN. Promotes apoptosis. Promotes translocation of SORT1 to the cell membrane, and thereby hinders lysosomal degradation of SOTR1 and promotes its interaction with NGFR. {ECO:0000269|PubMed:12728256, ECO:0000269|PubMed:12843241, ECO:0000269|PubMed:19407813}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type III membrane protein. Nucleus. Note=Proteolytic processing gives rise to an intracellular domain that translocates to the nucleus. SUBUNIT: Interacts with NGFR. Interacts with NTRK1. Interacts with SORT1. {ECO:0000269|PubMed:18624909, ECO:0000269|PubMed:19407813}. TISSUE SPECIFICITY: Detected in lung and testis. +Q60674 NR1D2_MOUSE Nuclear receptor subfamily 1 group D member 2 (Orphan nuclear receptor RVR) (Rev-erb-beta) 576 64,302 Binding site (2); Chain (1); Compositional bias (2); DNA binding (1); Disulfide bond (2); Domain (1); Modified residue (3); Region (2); Zinc finger (2) FUNCTION: Transcriptional repressor which coordinates circadian rhythm and metabolic pathways in a heme-dependent manner. Integral component of the complex transcription machinery that governs circadian rhythmicity and forms a critical negative limb of the circadian clock by directly repressing the expression of core clock components ARNTL/BMAL1 and CLOCK. Also regulates genes involved in metabolic functions, including lipid metabolism and the inflammatory response. Acts as a receptor for heme which stimulates its interaction with the NCOR1/HDAC3 corepressor complex, enhancing transcriptional repression. Recognizes two classes of DNA response elements within the promoter of its target genes and can bind to DNA as either monomers or homodimers, depending on the nature of the response element. Binds as a monomer to a response element composed of the consensus half-site motif 5'-[A/G]GGTCA-3' preceded by an A/T-rich 5' sequence (RevRE), or as a homodimer to a direct repeat of the core motif spaced by two nuclegotides (RevDR-2). Acts as a potent competitive repressor of ROR alpha (RORA) function and also negatively regulates the expression of NR1D1. Regulates lipid and energy homeostasis in the skeletal muscle via repression of genes involved in lipid metabolism and myogenesis including: CD36, FABP3, FABP4, UCP3, SCD1 and MSTN. Regulates hepatic lipid metabolism via the repression of APOC3. Represses gene expression at a distance in macrophages by inhibiting the transcription of enhancer-derived RNAs (eRNAs). In addition to its activity as a repressor, can also act as a transcriptional activator. Acts as a transcriptional activator of the sterol regulatory element-binding protein 1 (SREBF1) and the inflammatory mediator interleukin-6 (IL6) in the skeletal muscle. {ECO:0000269|PubMed:15623503, ECO:0000269|PubMed:18454201, ECO:0000269|PubMed:19682428, ECO:0000269|PubMed:22474260, ECO:0000269|PubMed:23221024, ECO:0000269|PubMed:23728303}. PTM: Deacetylated by HDAC1 (By similarity). Acetylation and deacetylation regulate its transcriptional regulatory activity (By similarity). {ECO:0000250|UniProtKB:Q14995}.; PTM: Under more reducing intracellular redox conditions, Cys-381 is in its heme-bound state, which is optimal for recruitment of the NCOR1/HDAC3 corepressor complex and repression of target genes (By similarity). When subjected to oxidative stress conditions, Cys-381 undergoes oxidation to form a disulfide bridge with Cys-371, also triggering a ligand switch that results in release of bound heme and derepression of target genes (By similarity). {ECO:0000250|UniProtKB:Q14995}.; PTM: Ubiquitinated by SIAH2; leading to its proteasomal degradation. {ECO:0000250|UniProtKB:Q14995}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}. SUBUNIT: Binds DNA as a monomer or a homodimer (By similarity). Interacts with NCOA5 coactivator, leading to a strong increase of transcription of target genes (By similarity). Interacts (via N-terminus) with KAT5 (By similarity). Interacts (via C-terminus) with HDAC1 (By similarity). Interacts with ZNHIT1 (By similarity). Interacts with SIAH2 (By similarity). {ECO:0000250|UniProtKB:Q14995}. DOMAIN: Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain. TISSUE SPECIFICITY: Ubiquitious. Expressed abundantly in skeletal muscle and brown adipose tissue. Expressed during skeletal muscle myogenesis. {ECO:0000269|PubMed:15623503, ECO:0000269|PubMed:18454201}. +P49282 NRAM2_MOUSE Natural resistance-associated macrophage protein 2 (NRAMP 2) (Divalent cation transporter 1) (Divalent metal transporter 1) (DMT-1) (Solute carrier family 11 member 2) 568 62,368 Alternative sequence (2); Chain (1); Frameshift (1); Glycosylation (2); Modified residue (4); Natural variant (1); Sequence conflict (6); Topological domain (13); Transmembrane (12) TRANSMEM 70 90 Helical. {ECO:0000255}.; TRANSMEM 96 117 Helical. {ECO:0000255}.; TRANSMEM 155 175 Helical. {ECO:0000255}.; TRANSMEM 180 194 Helical. {ECO:0000255}.; TRANSMEM 209 229 Helical. {ECO:0000255}.; TRANSMEM 256 276 Helical. {ECO:0000255}.; TRANSMEM 302 322 Helical. {ECO:0000255}.; TRANSMEM 361 381 Helical. {ECO:0000255}.; TRANSMEM 409 429 Helical. {ECO:0000255}.; TRANSMEM 441 461 Helical. {ECO:0000255}.; TRANSMEM 483 503 Helical. {ECO:0000255}.; TRANSMEM 507 527 Helical. {ECO:0000255}. TOPO_DOM 1 69 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 91 95 Extracellular. {ECO:0000255}.; TOPO_DOM 118 154 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 176 179 Extracellular. {ECO:0000255}.; TOPO_DOM 195 208 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 230 255 Extracellular. {ECO:0000255}.; TOPO_DOM 277 301 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 323 360 Extracellular. {ECO:0000255}.; TOPO_DOM 382 408 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 430 440 Extracellular. {ECO:0000255}.; TOPO_DOM 462 482 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 504 506 Extracellular. {ECO:0000255}.; TOPO_DOM 528 568 Cytoplasmic. {ECO:0000255}. FUNCTION: May serve to import iron into the mitochondria (By similarity). Important in metal transport, in particular iron. Involved in apical iron uptake into duodenal enterocytes. Involved in iron transport from acidified endosomes into the cytoplasm of erythroid precursor cells. May play an important role in hepatic iron accumulation and tissue iron distribution. {ECO:0000250|UniProtKB:P49281, ECO:0000269|PubMed:11739192, ECO:0000269|PubMed:15849611}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:P49281}.; PTM: Ubiquitinated by WWP2. {ECO:0000269|PubMed:18776082}. SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250|UniProtKB:P49281}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P49281}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:P49281}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P49281}. Cell membrane {ECO:0000269|PubMed:27462458}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P49281}. Note=Also found in extracellular vesicles different from exosomes. {ECO:0000269|PubMed:27462458}. SUBUNIT: Forms a complex with NDFIP1 and NEDD4L, in cortical neurons, in response to iron and colbalt exposure; this interaction leads to ubiquitination by NEDD4L and proteasome-dependent degradation. Interacts with NDFIP2. Interacts with COX2 and TOM6 at the outer mitochondrion membrane (By similarity). Interacts with ARRDC1; controls the incorporation of SLC11A2 into extracellular vesicles through an ubiquitination-dependent mechanism (By similarity). Interacts with ARRDC4; controls the incorporation of SLC11A2 into extracellular vesicles through an ubiquitination-dependent mechanism (PubMed:27462458). {ECO:0000250|UniProtKB:P49281, ECO:0000269|PubMed:27462458}. TISSUE SPECIFICITY: Isoform 2 is abundantly expressed in erythroid precursor cells (at protein level). Expressed at low levels in most tissues analyzed. Expressed at low levels in small intestine and at higher levels in kidney. {ECO:0000269|PubMed:10361139, ECO:0000269|PubMed:11739192}. DISEASE: Note=Defects in Slc11a2 are the cause of microcytic anemia (mk). Homozygous mk/mk mice have hypochromic microcytic anemia due to severe defects in intestinal iron absorption and erythroid iron utilization. +P49117 NR2C2_MOUSE Nuclear receptor subfamily 2 group C member 2 (Orphan nuclear receptor TAK1) (Orphan nuclear receptor TR4) (Testicular receptor 4) 596 65,239 Chain (1); Cross-link (1); DNA binding (1); Domain (1); Erroneous initiation (2); Modified residue (7); Mutagenesis (5); Sequence conflict (10); Zinc finger (2) FUNCTION: Orphan nuclear receptor that can act as a repressor or activator of transcription. An important repressor of nuclear receptor signaling pathways such as retinoic acid receptor, retinoid X, vitamin D3 receptor, thyroid hormone receptor and estrogen receptor pathways. May regulate gene expression during the late phase of spermatogenesis. Activates transcriptional activity of LHCG and is antagonist of PPARA-mediated transactivation (By similarity). Together with NR2C1, forms the core of the DRED (direct repeat erythroid-definitive) complex that represses embryonic and fetal globin transcription including that of GATA1. Binds to hormone response elements (HREs) consisting of two 5'-AGGTCA-3' half site direct repeat consensus sequences. Plays a fundamental role in early embryonic development and embryonic stem cells. Required for normal spermatogenesis and cerebellum development. Appears to be important for neurodevelopmentally regulated behavior. {ECO:0000250, ECO:0000269|PubMed:12093744, ECO:0000269|PubMed:15199144, ECO:0000269|PubMed:16887930, ECO:0000269|PubMed:17706948, ECO:0000269|PubMed:17974920, ECO:0000269|PubMed:19131575, ECO:0000269|PubMed:20393820}. PTM: Phosphorylation on Ser-19 and Ser-68 is an important regulator of NR2C2-mediated transcriptional activity. Phosphorylation on these residues recruits the corepressor, NRIP1, leading to transcripional repression, whereas the non-phosphorylated form preferentially recruits the coactivator, PCAF. {ECO:0000269|PubMed:16887930}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}. SUBUNIT: Homodimer; can bind DNA as homodimer (By similarity). Heterodimer; binds DNA as a heterodimer with NR2C1 required for chromatin remodeling and for binding to promoter regions such as globin DR1 repeats. Interacts with NR2C2AP; the interaction represses selective NR2C2-mediated transcriptional activity (By similarity). Interacts with PCAF; the interaction preferentially occurs on the non-phosphorylated form and induces NR2C2-mediated transactivation activity and does not require the ligand-binding domain (PubMed:16887930). Interacts (MAPK-mediated phosphorylated form) with NRIP1; the interaction promotes repression of NR2C2-mediated activity (PubMed:16887930). Interacts with NLRP10. Interacts (via ligand-binding region) with transcriptional corepressor JAZF1; the interaction promotes NR2C2-mediated transcriptional repression (By similarity). {ECO:0000250|UniProtKB:P49116, ECO:0000269|PubMed:16887930}. TISSUE SPECIFICITY: Expressed, during embryogenesis, in perichondrium, developing glomeruli structures and tubules of kidney, as well as in intestiinal villi. Also expressed in lung and hair follicles. {ECO:0000269|PubMed:10347174, ECO:0000269|PubMed:15199144, ECO:0000269|PubMed:17706948}. +Q60641 NR1H4_MOUSE Bile acid receptor (Farnesoid X-activated receptor) (Farnesol receptor HRR-1) (Nuclear receptor subfamily 1 group H member 4) (Retinoid X receptor-interacting protein 14) (RXR-interacting protein 14) 488 55,994 Alternative sequence (2); Binding site (4); Chain (1); Cross-link (2); DNA binding (1); Domain (1); Modified residue (6); Mutagenesis (2); Region (1); Sequence conflict (10); Zinc finger (2) FUNCTION: Ligand-activated transcription factor. Receptor for bile acids (BAs) such as chenodeoxycholic acid (CDCA), lithocholic acid, deoxycholic acid (DCA) and allocholic acid (ACA). Plays a essential role in BA homeostasis through the regulation of genes involved in BA synthesis, conjugation and enterohepatic circulation. Also regulates lipid and glucose homeostasis and is involved in innate immune response (PubMed:11030617, PubMed:21383957, PubMed:22820415). The FXR-RXR heterodimer binds predominantly to farnesoid X receptor response elements (FXREs) containing two inverted repeats of the consensus sequence 5'-AGGTCA-3' in which the monomers are spaced by 1 nucleotide (IR-1) but also to tandem repeat DR1 sites with lower affinity, and can be activated by either FXR or RXR-specific ligands. It is proposed that monomeric nuclear receptors such as NR5A2/LRH-1 bound to coregulatory nuclear responsive element (NRE) halfsites located in close proximity to FXREs modulate transcriptional activity (PubMed:20091679, PubMed:20483916). In the liver activates transcription of the corepressor NR0B2 thereby indirectly inhibiting CYP7A1 and CYP8B1 (involved in BA synthesis) implicating at least in part histone demethylase KDM1A resulting in epigenomic repression, and SLC10A1/NTCP (involved in hepatic uptake of conjugated BAs). Activates transcription of the repressor MAFG (involved in regulation of BA synthesis) (PubMed:21383957, PubMed:25651182, PubMed:25545350). Activates transcription of SLC27A5/BACS and BAAT (involved in BA conjugation), ABCB11/BSEP (involved in bile salt export) by directly recruiting histone methyltransferase CARM1, and ABCC2/MRP2 (involved in secretion of conjugated BAs) and ABCB4 (involved in secretion of phosphatidylcholine in the small intestine) (PubMed:21383957). In ileal enterocytes activates FABP6/IBABP (involved in cytosolic transport), SLC51A/OSTA and SLC51B/OSTB (involved in secretion of conjugated BAs to the portal blood), and repressor NR0B2/SHP thereby indirectly inhibiting SLC10A2/ASBT (involved in BA uptake) (By similarity). In the intestine activates FGF15 expression and secretion leading to hepatic CYP7A1 repression; the function also involves the coordinated induction of hepatic KLB/beta-klotho expression (PubMed:16213224, PubMed:26505219). Transcriptional activation of FABP6/IBAP and SCD1 but not of ABCB11 is isoform-specific (PubMed:12393883). Regulates transcription of liver UGT2B4 and SULT2A1 involved in BA detoxification; binding to the UGT2B4 promoter seems to imply a monomeric transactivation independent of RXRA (By similarity). Modulates lipid homeostasis by activating liver NR0B2/SHP-mediated repression of SREBF1 isoform SREBP-1C (involved in de novo lipogenesis), expression of PLTP (involved in HDL formation), SCARB1 (involved in HDL hepatic uptake), APOE, APOC1, APOC4, VLDLR and SDC1 (involved in the hepatic uptake of LDL and IDL remnants), and inhibiting expression of MTTP (involved in VLDL assembly) (PubMed:12421815, PubMed:15146238). Increases expression of APOC2 (promoting lipoprotein lipase activity implicated in triglyceride clearance) (PubMed:11579204). Transrepresses APOA1 probably involving a monomeric competition with NR2A1 for binding to a DR1 element (PubMed:21804189). Also reduces triglyceride clearance by inhibiting expression of ANGPTL3 and APOC3 (both involved in inhibition of lipoprotein lipase) (PubMed:12891557, PubMed:15146238). Involved in glucose homeostasis by modulating hepatic gluconeogenesis through activation of NR0B2/SHP-mediated repression of respective genes. Modulates glycogen synthesis (inducing phosphorylation of glycogen synthase kinase-3). Modulates glucose-stimulated insulin secretion and is involved in insulin resistance (PubMed:15564327, PubMed:16446356, PubMed:16557297, PubMed:16410358, PubMed:20447400). Involved in intestinal innate immunity. Plays a role in protecting the distal small intestine against bacterial overgrowth and preservation of the epithelial barrier (PubMed:16473946, PubMed:21242261). Down-regulates inflammatory cytokine expression in several types of immune cells including macrophages and mononuclear cells (PubMed:19864602). Mediates transrepression of TLR4-induced cytokine expression; the function seems to require its sumoylation and prevents N-CoR nuclear receptor corepressor clearance from target genes such as IL1B and NOS2 (By similarity). Involved in the TLR9-mediated protective mechanism in intestinal inflammation (PubMed:23372731). Plays a anti-inflammatory role in liver inflammation; proposed to inhibit proinflammatory (but not antiapoptotic) NF-kappa-B signaling (PubMed:18972444). {ECO:0000250|UniProtKB:Q62735, ECO:0000250|UniProtKB:Q96RI1, ECO:0000269|PubMed:11030617, ECO:0000269|PubMed:11579204, ECO:0000269|PubMed:11706036, ECO:0000269|PubMed:12004058, ECO:0000269|PubMed:12393883, ECO:0000269|PubMed:12421815, ECO:0000269|PubMed:12660231, ECO:0000269|PubMed:12891557, ECO:0000269|PubMed:15146238, ECO:0000269|PubMed:15564327, ECO:0000269|PubMed:16213224, ECO:0000269|PubMed:16410358, ECO:0000269|PubMed:16446356, ECO:0000269|PubMed:16473946, ECO:0000269|PubMed:16557297, ECO:0000269|PubMed:16946559, ECO:0000269|PubMed:18972444, ECO:0000269|PubMed:19864602, ECO:0000269|PubMed:20091679, ECO:0000269|PubMed:20447400, ECO:0000269|PubMed:20483916, ECO:0000269|PubMed:21242261, ECO:0000269|PubMed:21804189, ECO:0000269|PubMed:23372731, ECO:0000269|PubMed:25545350, ECO:0000269|PubMed:25651182, ECO:0000269|PubMed:26505219, ECO:0000305|PubMed:21383957, ECO:0000305|PubMed:22820415}.; FUNCTION: Isoform 2: Activates transcription of IBAP and SDC1. {ECO:0000269|PubMed:12393883}.; FUNCTION: Isoform 4: Activates transcription of IBAP and SDC1. {ECO:0000269|PubMed:12393883}. PTM: Acetylated by EP300 (PubMed:18842595). Lys-228 as is the major acetylation site for EP300; the dynamicly regulated acetylation inhibits heterodimerization with RXRA and transactivation activity. Deacetylated by SIRT1 (By similarity). Elevated acetylation levels are found in metabolic disease states (mouse models of obesity and type II diabetes) (PubMed:19883617). {ECO:0000250|UniProtKB:Q96RI1, ECO:0000269|PubMed:18842595, ECO:0000269|PubMed:19883617}.; PTM: Methylation may increase transactivation of target genes. {ECO:0000250|UniProtKB:Q96RI1}.; PTM: Phosphorylation by PKC/PRKCA increases transactivation activity by promoting association with PPARGC1A. {ECO:0000250|UniProtKB:Q96RI1}.; PTM: Sumoylated upon ligand binding. {ECO:0000250|UniProtKB:Q96RI1}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19864602, ECO:0000305}. SUBUNIT: Binds DNA predominantly as a heterodimer with RXRA (PubMed:7760852). After activation by agonist binding interacts with coactivators. Interacts with PPARGC1A, SMARCA4 and EP300 (PubMed:14729567, PubMed:18842595, PubMed:19805516). Interacts with NCOA1, NCOA2, CARM1, SETD7, PRMT1, GPS2, SMARCA4 and MED1. Interacts with XRCC5 and XRCC6; decreasing NR1H4/FXR transactivation activity towards ABCB11/BSEP. Interacts with PAGR1 AND NCOA6; indicative for an association with an MLL2/MLL3 complex (ASCOM) (By similarity). Interacts with NR5A2 (PubMed:20483916). {ECO:0000250|UniProtKB:Q62735, ECO:0000250|UniProtKB:Q96RI1, ECO:0000269|PubMed:14729567, ECO:0000269|PubMed:18842595, ECO:0000269|PubMed:19805516, ECO:0000269|PubMed:20483916, ECO:0000269|PubMed:7760852}. TISSUE SPECIFICITY: Expressed in liver and kidney. Expressed in pancreatic beta cells and macrophages. Expressed in the villus epithelium in adult ileum, with highest expression in the intervillus regions. Expression in colon is reduced by inflammation. {ECO:0000269|PubMed:16473946, ECO:0000269|PubMed:19393742, ECO:0000269|PubMed:19864602, ECO:0000269|PubMed:20447400}. DISEASE: Note=Activation protects mice against cholestasis, development of chronical intestinal inflammation and fibrosis. May suppress intestinal tumorigenesis. {ECO:0000269|PubMed:19047134, ECO:0000269|PubMed:19864602, ECO:0000269|PubMed:22057115}. +Q8VCQ3 NRBF2_MOUSE Nuclear receptor-binding factor 2 (NRBF-2) 287 32,501 Chain (1); Coiled coil (1); Helix (3); Modified residue (2); Motif (1); Sequence conflict (2) FUNCTION: May modulate transcriptional activation by target nuclear receptors. Can act as transcriptional activator (in vitro) (By similarity). {ECO:0000250|UniProtKB:Q96F24}.; FUNCTION: Involved in starvation-induced autophagy probably by its association with PI3K complex I (PI3KC3-C1). However, effects has been described variably. Involved in the induction of starvation-induced autophagy (By similarity). Stabilzes PI3KC3-C1 assembly and enhances ATG14-linked lipid kinase activity of PIK3C3 (PubMed:24849286). Proposed to negatively regulate basal and starvation-induced autophagy and to inhibit PIK3C3 activity by modulating interactions in PI3KC3-C1 (By similarity). May be involved in autophagosome biogenesis (By similarity). May play a role in neural progenitor cell survival during differentiation (PubMed:18619852). {ECO:0000250|UniProtKB:Q96F24, ECO:0000269|PubMed:18619852, ECO:0000269|PubMed:24849286}.; FUNCTION: Involved in the induction of starvation-induced autophagy. Modulates ATG14-linked lipid kinase activity of PIK3C3 and stabilzes PI3K complex I (PI3KC3-C1) assembly (PubMed:24849286). May play a role in neural progenitor cell survival during differentiation (PubMed:18619852). {ECO:0000250|UniProtKB:Q96F24, ECO:0000269|PubMed:18619852, ECO:0000269|PubMed:24849286}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9QYK3}. Cytoplasm {ECO:0000269|PubMed:18619852}. Cytoplasmic vesicle, autophagosome {ECO:0000305}. SUBUNIT: Interacts with RRARA, PPARD and PPARG. Interacts with THRB, RARA, RARG and RXRA in the presence of bound ligand (By similarity). Interacts with SCOC (By similarity). Associates with the PI3K complex I (PI3KC3-C1); the direct binding partner in the complex is reported variably as PIK3R4 or ATG14 (PubMed:24849286). {ECO:0000250|UniProtKB:Q96F24, ECO:0000269|PubMed:24849286}. +P54846 NRL_MOUSE Neural retina-specific leucine zipper protein (NRL) 237 26,083 Chain (1); Cross-link (2); Domain (1); Region (3) FUNCTION: Acts as a transcriptional activator which regulates the expression of several rod-specific genes, including RHO and PDE6B. Functions also as a transcriptional coactivator, stimulating transcription mediated by the transcription factor CRX and NR2E3. Binds in a sequence-specific manner to the rhodopsin promoter. {ECO:0000250|UniProtKB:P54845}. PTM: Disumoylated at Lys-20. Sumoylation modulates the transcriptional activity of NRL on RHO and NR2E3 promoters, and is required for normal rod differentiation. {ECO:0000269|PubMed:20551322}.; PTM: Phosphorylated. {ECO:0000250|UniProtKB:P54845}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P54845}. Nucleus {ECO:0000250|UniProtKB:P54845}. SUBUNIT: Interacts with FIZ1; this interaction represses transactivation. Interacts (via the leucine-zipper domain) with CRX. {ECO:0000250|UniProtKB:P54845}. DOMAIN: The minimal transactivation domain (MTD) is conserved across the MAF family, it may activate transcription by recruiting TBP and associated factors at the promoters of target genes. {ECO:0000250|UniProtKB:P54845}. TISSUE SPECIFICITY: Expressed in the retina (at protein level) (PubMed:11477108). {ECO:0000269|PubMed:11477108}. +P56974 NRG2_MOUSE Pro-neuregulin-2, membrane-bound isoform (Pro-NRG2) [Cleaved into: Neuregulin-2 (NRG-2) (Divergent of neuregulin 1) (DON-1)] 756 82,213 Alternative sequence (5); Chain (2); Compositional bias (2); Disulfide bond (4); Domain (2); Glycosylation (4); Propeptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 316 336 Helical; Note=Internal signal sequence. {ECO:0000255}. TOPO_DOM 20 315 Extracellular. {ECO:0000255}.; TOPO_DOM 337 756 Cytoplasmic. {ECO:0000255}. FUNCTION: Direct ligand for ERBB3 and ERBB4 tyrosine kinase receptors. Concomitantly recruits ERBB1 and ERBB2 coreceptors, resulting in ligand-stimulated tyrosine phosphorylation and activation of the ERBB receptors. May also promote the heterodimerization with the EGF receptor. {ECO:0000269|PubMed:9168115}. PTM: Proteolytic cleavage close to the plasma membrane on the external face leads to the release of the soluble growth factor form. {ECO:0000250}.; PTM: Extensive glycosylation precedes the proteolytic cleavage. {ECO:0000250}. SUBCELLULAR LOCATION: Pro-neuregulin-2, membrane-bound isoform: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Does not seem to be active. {ECO:0000250}.; SUBCELLULAR LOCATION: Neuregulin-2: Secreted {ECO:0000250}. SUBUNIT: Interacts with ERBB3 and ERBB4. {ECO:0000269|PubMed:9168115}. DOMAIN: The cytoplasmic domain may be involved in the regulation of trafficking and proteolytic processing. Regulation of the proteolytic processing involves initial intracellular domain dimerization (By similarity). {ECO:0000250}.; DOMAIN: ERBB receptor binding is elicited entirely by the EGF-like domain. {ECO:0000250}. TISSUE SPECIFICITY: Highest expression in the brain, with lower levels in the lung. In the cerebellum, found in granule and Purkinje cells. +Q921B4 NRIF2_MOUSE Neurotrophin receptor-interacting factor 2 (Zinc finger protein 369) 824 93,244 Alternative sequence (2); Chain (1); Cross-link (1); Domain (3); Sequence conflict (2); Zinc finger (5) FUNCTION: Transcription regulator which may participate in NGFR/p75(NTR)-mediated apoptosis. Probably acts as a transcription repressor: specifically binds to the 3'-end of zinc-finger coding genes and recruiting chromatin-modifying proteins such as SETDB1 and TRIM28/KAP1, leading to transcription repression (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11750124}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187, ECO:0000269|PubMed:11750124}. SUBUNIT: Interacts with NGFR/p75(NTR). {ECO:0000269|PubMed:11750124}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:11750124}. +P97333 NRP1_MOUSE Neuropilin-1 (A5 protein) (CD antigen CD304) 923 103,000 Beta strand (38); Chain (1); Disulfide bond (6); Domain (5); Glycosylation (7); Helix (8); Metal binding (3); Modified residue (1); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (8) TRANSMEM 857 879 Helical. {ECO:0000255}. TOPO_DOM 22 856 Extracellular. {ECO:0000255}.; TOPO_DOM 880 923 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor involved in the development of the cardiovascular system, in angiogenesis, in the formation of certain neuronal circuits and in organogenesis outside the nervous system. Mediates the chemorepulsant activity of semaphorins. Binds to semaphorin 3A, the PLGF-2 isoform of PGF, the VEGF165 isoform of VEGFA and VEGFB. Coexpression with KDR results in increased VEGF165 binding to KDR as well as increased chemotaxis. Regulates VEGF-induced angiogenesis (By similarity). Binding to VEGFA initiates a signaling pathway needed for motor neuron axon guidance and cell body migration, including for the caudal migration of facial motor neurons from rhombomere 4 to rhombomere 6 during embryonic development (PubMed:26503042). {ECO:0000250, ECO:0000269|PubMed:26503042}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Homodimer, and heterodimer with NRP2. Binds PLXNB1 (By similarity). Interacts with FER. Interacts with VEGFA (PubMed:26503042). {ECO:0000250, ECO:0000269|PubMed:20133938, ECO:0000269|PubMed:26503042}. DOMAIN: The tandem CUB domains mediate binding to semaphorin, while the tandem F5/8 domains are responsible for heparin and VEGF binding. {ECO:0000250}. TISSUE SPECIFICITY: Nervous system. +Q9CPR8 NSE3_MOUSE Non-structural maintenance of chromosomes element 3 homolog (Non-SMC element 3 homolog) (MAGE-G1 antigen) (Necdin-like protein 2) 279 31,460 Chain (1); Domain (1); Modified residue (1); Region (1); Sequence conflict (1) FUNCTION: Component of the SMC5-SMC6 complex, a complex involved in repair of DNA double-strand breaks by homologous recombination. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The complex is required for telomere maintenance via recombination in ALT (alternative lengthening of telomeres) cell lines and mediates sumoylation of shelterin complex (telosome) components which is proposed to lead to shelterin complex disassembly in ALT-associated PML bodies (APBs). In vitro enhances ubiquitin ligase activity of NSMCE1. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex (By similarity). May be a growth suppressor that facilitates the entry of the cell into cell cycle arrest (PubMed:14593116). {ECO:0000250|UniProtKB:Q96MG7, ECO:0000269|PubMed:14593116}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14593116}. Nucleus {ECO:0000269|PubMed:14593116}. Chromosome, telomere {ECO:0000250}. SUBUNIT: Component of the SMC5-SMC6 complex which consists at least of SMC5, SMC6, NSMCE2, NSMCE1, NSMCE4A or EID3 and NSMCE3. NSMCE1, NSMCE4A or EID3 and NSMCE3 probably form a subcomplex that bridges the head domains of the SMC5:SMC6 heterodimer. Interacts with PJA1 (By similarity). Interacts with E2F1 (via C-terminus) (PubMed:14593116). Interacts with NGFR (via C-terminus) (PubMed:14593116). Interacts with NSMCE1. Interacts with NSMCE4. Interacts with SMC6. Interacts with EID3 (By similarity). {ECO:0000250|UniProtKB:Q96MG7, ECO:0000269|PubMed:14593116}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11782285, ECO:0000269|PubMed:14593116}. +Q9D7Z3 NOL7_MOUSE Nucleolar protein 7 254 28,970 Alternative sequence (1); Chain (1); Cross-link (2); Frameshift (1); Modified residue (1) SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. +Q6DFW4 NOP58_MOUSE Nucleolar protein 58 (MSSP) (Nucleolar protein 5) (SIK-similar protein) 536 60,343 Chain (1); Compositional bias (1); Cross-link (15); Domain (1); Frameshift (1); Modified residue (6); Sequence conflict (3) FUNCTION: Required for 60S ribosomal subunit biogenesis (By similarity). Core component of box C/D small nucleolar ribonucleoprotein (snoRNP) particles. Required for the biogenesis of box C/D snoRNAs such as U3, U8 and U14 snoRNAs (By similarity). {ECO:0000250}. PTM: Sumoylation is essential for high-affinity binding to snoRNAs. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. SUBUNIT: Core component of box C/D small nucleolar ribonucleoprotein (snoRNP) particles; the core proteins SNU13, NOP56, NOP58 and FBL assemble stepwise onto the snoRNA. Interacts with NOLC1/Nopp140. Interacts with NUFIP1, RUVBL1 AND RUVBL2; RUVBL1:RUVBL2 seem to bridge the association of NOP58 with NUFIP1. Interacts with PIH1D1. {ECO:0000250|UniProtKB:Q9Y2X3, ECO:0000269|PubMed:10864044}. +P97819 PLPL9_MOUSE 85/88 kDa calcium-independent phospholipase A2 (CaI-PLA2) (EC 3.1.1.4) (Group VI phospholipase A2) (GVI PLA2) (Intracellular membrane-associated calcium-independent phospholipase A2 beta) (iPLA2-beta) (Patatin-like phospholipase domain-containing protein 9) (PNPLA9) 807 89,560 Active site (2); Alternative sequence (1); Chain (1); Domain (1); Modified residue (1); Motif (3); Region (2); Repeat (7) FUNCTION: Catalyzes the release of fatty acids from phospholipids. It has been implicated in normal phospholipid remodeling, nitric oxide-induced or vasopressin-induced arachidonic acid release and in leukotriene and prostaglandin production. May participate in fas mediated apoptosis and in regulating transmembrane ion flux in glucose-stimulated B-cells. Has a role in cardiolipin (CL) deacylation. Required for both speed and directionality of monocyte MCP1/CCL2-induced chemotaxis through regulation of F-actin polymerization at the pseudopods (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Isoform Long: Membrane; Peripheral membrane protein. Note=Recruited to the membrane-enriched pseudopod upon MCP1/CCL2 stimulation in monocytes. {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform Short: Cytoplasm. +Q61469 PLPP1_MOUSE Phospholipid phosphatase 1 (EC 3.1.3.4) (35 kDa PAP) (mPAP) (Hydrogen peroxide-inducible protein 53) (Hic53) (Lipid phosphate phosphohydrolase 1) (PAP2-alpha) (Phosphatidate phosphohydrolase type 2a) (Phosphatidic acid phosphatase 2a) (PAP-2a) (PAP2a) 283 31,892 Alternative sequence (1); Chain (1); Frameshift (1); Glycosylation (1); Topological domain (7); Transmembrane (6) TRANSMEM 7 27 Helical. {ECO:0000255}.; TRANSMEM 54 74 Helical. {ECO:0000255}.; TRANSMEM 89 109 Helical. {ECO:0000255}.; TRANSMEM 165 185 Helical. {ECO:0000255}.; TRANSMEM 200 220 Helical. {ECO:0000255}.; TRANSMEM 230 250 Helical. {ECO:0000255}. TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 28 53 Extracellular. {ECO:0000255}.; TOPO_DOM 75 88 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 110 164 Extracellular. {ECO:0000255}.; TOPO_DOM 186 199 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 221 229 Extracellular. {ECO:0000255}.; TOPO_DOM 251 283 Cytoplasmic. {ECO:0000255}. FUNCTION: Broad-specificity phosphohydrolase that dephosphorylates exogenous bioactive glycerolipids and sphingolipids. Catalyzes the conversion of phosphatidic acid (PA) to diacylglycerol (DG). In addition it hydrolyzes lysophosphatidic acid (LPA), diacyl glycerol pyrophosphate (DGPP), ceramide-1-phosphate (C-1-P) and sphingosine-1-phosphate (S-1-P). The relative catalytic efficiency is LPA > PA > C-1-P > S-1-P. PTM: N-glycosylated. Contains high-mannose oligosaccharide. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Note=Found predominantly in plasma membrane. SUBUNIT: Homodimer. This complex seems not to be involved in substrate recognition, it may confer only structural or functional stability. {ECO:0000269|PubMed:14725715}. TISSUE SPECIFICITY: Highly expressed in kidney and lung. Almost undetectable in brain, heart, bone, muscle or spleen. +Q8CJ00 NOXA1_MOUSE NADPH oxidase activator 1 444 48,880 Alternative sequence (1); Chain (1); Domain (2); Region (1); Repeat (4); Sequence conflict (5) FUNCTION: Functions as an activator of NOX1, a superoxide-producing NADPH oxidase. Functions in the production of reactive oxygen species (ROS) which participate in a variety of biological processes including host defense, hormone biosynthesis, oxygen sensing and signal transduction. May also activate CYBB/gp91phox and NOX3. {ECO:0000269|PubMed:12473664, ECO:0000269|PubMed:15326186, ECO:0000269|PubMed:16814099}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16814099}. Cell membrane {ECO:0000269|PubMed:16814099}. Note=Translocation to membranes depends on NOXO1 or NCF1 and maybe RAC1. SUBUNIT: NOX1, NOXA1, NOXO1, RAC1 and CYBA forms a functional multimeric complex supporting ROS production. Interaction with YWHAZ prevents the interaction of NOXA1 with NOXO1 and RAC1 and its targeting to membranes, hence reducing its ability to activate NOX1. Interacts (via N-terminus) with SH3PXD2A and SH3PXD2B; the interaction is direct (By similarity). {ECO:0000250}. DOMAIN: The SH3 domain mediates interaction with NOXO1 and NCF1 and has autoregulatory function. {ECO:0000250}.; DOMAIN: The TPR repeats mediate interaction with RAC1. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed with a tissue distribution similar to the one of NOX1. Detected in colon, uterus, prostate, small intestine, stomach, lung, thyroid, aorta, inner ear and salivary glands. Expressed in colon, small intestine and aortic smooth muscle cells (at protein level). {ECO:0000269|PubMed:12473664, ECO:0000269|PubMed:12657628, ECO:0000269|PubMed:15949904, ECO:0000269|PubMed:16814099}. +Q61982 NOTC3_MOUSE Neurogenic locus notch homolog protein 3 (Notch 3) [Cleaved into: Notch 3 extracellular truncation; Notch 3 intracellular domain] 2318 244,248 Chain (3); Disulfide bond (111); Domain (34); Glycosylation (3); Modified residue (1); Mutagenesis (1); Region (1); Repeat (8); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 1644 1664 Helical. {ECO:0000255}. TOPO_DOM 40 1643 Extracellular.; TOPO_DOM 1665 2318 Cytoplasmic. FUNCTION: Functions as a receptor for membrane-bound ligands Jagged1, Jagged2 and Delta1 to regulate cell-fate determination. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. Affects the implementation of differentiation, proliferation and apoptotic programs (By similarity). May play a role during CNS development. {ECO:0000250|UniProtKB:Q9R172, ECO:0000250|UniProtKB:Q9UM47}. PTM: Synthesized in the endoplasmic reticulum as an inactive form which is proteolytically cleaved by a furin-like convertase in the trans-Golgi network before it reaches the plasma membrane to yield an active, ligand-accessible form. Cleavage results in a C-terminal fragment N(TM) and a N-terminal fragment N(EC). Following ligand binding, it is cleaved by TNF-alpha converting enzyme (TACE) to yield a membrane-associated intermediate fragment called notch extracellular truncation (NEXT). This fragment is then cleaved by presenilin dependent gamma-secretase to release a notch-derived peptide containing the intracellular domain (NICD) from the membrane. {ECO:0000269|PubMed:11459941, ECO:0000269|PubMed:11518718}.; PTM: Phosphorylated.; PTM: Hydroxylated by HIF1AN. {ECO:0000269|PubMed:18299578}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9UM47}; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Notch 3 intracellular domain: Nucleus. Note=Following proteolytical processing NICD is translocated to the nucleus. SUBUNIT: Interacts with PSMA1 (By similarity). Heterodimer of a C-terminal fragment N(TM) and a N-terminal fragment N(EC) which are probably linked by disulfide bonds. Interacts with MAML1, MAML2 and MAML3 which act as transcriptional coactivators for NOTCH3. Interacts with HIF1AN. {ECO:0000250, ECO:0000269|PubMed:15019995, ECO:0000269|PubMed:17573339}. DOMAIN: The EGF-like domains 10 and 11 are required for binding the ligands JAG1 and DLL1. {ECO:0000250|UniProtKB:Q9UM47}. TISSUE SPECIFICITY: Proliferating neuroepithelium. +P31695 NOTC4_MOUSE Neurogenic locus notch homolog protein 4 (Notch 4) [Cleaved into: Transforming protein Int-3; Notch 4 extracellular truncation; Notch 4 intracellular domain] 1964 206,693 Chain (4); Disulfide bond (95); Domain (29); Erroneous initiation (2); Glycosylation (3); Mutagenesis (1); Repeat (8); Sequence caution (1); Sequence conflict (32); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1444 1464 Helical. {ECO:0000255}. TOPO_DOM 21 1443 Extracellular. {ECO:0000255}.; TOPO_DOM 1465 1964 Cytoplasmic. {ECO:0000255}. FUNCTION: Functions as a receptor for membrane-bound ligands Jagged1, Jagged2 and Delta1 to regulate cell-fate determination. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. Affects the implementation of differentiation, proliferation and apoptotic programs (By similarity). May regulate branching morphogenesis in the developing vascular system. {ECO:0000250, ECO:0000269|PubMed:11344305}. PTM: Synthesized in the endoplasmic reticulum as an inactive form which is proteolytically cleaved by a furin-like convertase in the trans-Golgi network before it reaches the plasma membrane to yield an active, ligand-accessible form. Cleavage results in a C-terminal fragment N(TM) and a N-terminal fragment N(EC). Following ligand binding, it is cleaved by TNF-alpha converting enzyme (TACE) to yield a membrane-associated intermediate fragment called notch extracellular truncation (NEXT). This fragment is then cleaved by presenilin dependent gamma-secretase to release a notch-derived peptide containing the intracellular domain (NICD) from the membrane. {ECO:0000269|PubMed:11459941, ECO:0000269|PubMed:11518718}.; PTM: Phosphorylated. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Notch 4 intracellular domain: Nucleus. Note=Following proteolytical processing NICD is translocated to the nucleus. SUBUNIT: Heterodimer of a C-terminal fragment N(TM) and a N-terminal fragment N(EC) which are probably linked by disulfide bonds. Interacts with MAML1, MAML2 and MAML3 which act as transcriptional coactivators for NOTCH4. {ECO:0000269|PubMed:15019995}. TISSUE SPECIFICITY: Highly expressed in lung, moderately in heart kidney, and at lower levels in the ovary and skeletal muscle. A very low expression is seen in the brain, intestine, liver and testis. DISEASE: Note=Loss of the extracellular domain causes constitutive activation of the Notch protein, which leads to hyperproliferation of glandular epithelial tissues and development of mammary carcinomas. {ECO:0000303|PubMed:8681805}. +Q9QXZ7 NR2E3_MOUSE Photoreceptor-specific nuclear receptor (Nuclear receptor subfamily 2 group E member 3) (Retina-specific nuclear receptor) 395 43,177 Chain (1); Compositional bias (1); Cross-link (3); DNA binding (1); Domain (1); Mutagenesis (3); Zinc finger (2) FUNCTION: Orphan nuclear receptor of retinal photoreceptor cells. Transcriptional factor that is an activator of rod development and repressor of cone development. Binds the promoter region of a number of rod- and cone-specific genes, including rhodopsin, M- and S-opsin and rod-specific phosphodiesterase beta subunit. Enhances rhodopsin expression. Represses M- and S-cone opsin expression. {ECO:0000269|PubMed:15190009, ECO:0000269|PubMed:15634773, ECO:0000269|PubMed:19186166, ECO:0000269|PubMed:21408158}. PTM: Di- and tri-sumoylated in developing retina. PIAS3-mediated sumoylation promotes repression of cone-specific gene expression and activation of rod-specific genes. Sumoylation on Lys-178 appears to be the main site. {ECO:0000269|PubMed:19186166}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407, ECO:0000269|PubMed:15190009, ECO:0000269|PubMed:19186166}. SUBUNIT: Homodimer. Interacts with PIAS3; the interaction sumoylates NR2E3 and promotes repression of cone-specific gene transcription and activation of rod-specific genes. Component of a rod photoreceptor complex that includes NR2E3, PIAS3, NRL, CRX and/or NR1D1. Binds directly in the complex with CRX, PIAS3 and NR1D1 (By similarity). Interacts (via the DNA-binding domain) with CRX (via its DNA binding domain); the interaction represses S- and M-cone opsin expression. {ECO:0000250, ECO:0000269|PubMed:19186166}. TISSUE SPECIFICITY: Retina. Rod-specific. Expressed in the outer nuclear lyer of the mature retina. {ECO:0000269|PubMed:10611353, ECO:0000269|PubMed:10805811, ECO:0000269|PubMed:15190009, ECO:0000269|PubMed:15634773, ECO:0000269|PubMed:21408158}. +P43136 NR2F6_MOUSE Nuclear receptor subfamily 2 group F member 6 (COUP transcription factor 3) (COUP-TF3) (V-erbA-related protein 2) (EAR-2) 390 41,968 Chain (1); DNA binding (1); Domain (1); Modified residue (3); Region (1); Sequence conflict (8); Zinc finger (2) FUNCTION: Transcription factor predominantly involved in transcriptional repression. Binds to promoter/enhancer response elements that contain the imperfect 5'-AGGTCA-3' direct or inverted repeats with various spacings which are also recognized by other nuclear hormone receptors. Involved in modulation of hormonal responses. Represses transcriptional activity of the lutropin-choriogonadotropic hormone receptor/LHCGR gene, the renin/REN gene and the oxytocin-neurophysin/OXT gene. Represses the triiodothyronine-dependent and -independent transcriptional activity of the thyroid hormone receptor gene in a cell type-specific manner. The corepressing function towards thyroid hormone receptor beta/THRB involves at least in part the inhibition of THRB binding to triiodothyronine response elements (TREs) by NR2F6. Inhibits NFATC transcription factor DNA binding and subsequently its transcriptional activity. Acts as transcriptional repressor of IL-17 expression in Th-17 differentiated CD4(+) T cells and may be involved in induction and/or maintenance of peripheral immunological tolerance and autoimmunity. Involved in development of forebrain circadian clock; is required early in the development of the locus coeruleus (LC). {ECO:0000269|PubMed:12690040, ECO:0000269|PubMed:15741322, ECO:0000269|PubMed:18701084}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407, ECO:0000269|PubMed:12690040}. SUBUNIT: Binds DNA as dimer; homodimer and heterodimer with NR2F2 and probably NR2F1. Interacts with THRB (By similarity). {ECO:0000250}. +Q80XB4 NRAP_MOUSE Nebulin-related-anchoring protein (N-RAP) 1728 195,756 Alternative sequence (3); Chain (1); Domain (1); Frameshift (1); Modified residue (2); Repeat (41); Sequence conflict (10) FUNCTION: May be involved in anchoring the terminal actin filaments in the myofibril to the membrane and in transmitting tension from the myofibrils to the extracellular matrix. {ECO:0000269|PubMed:10320340, ECO:0000269|PubMed:11732910, ECO:0000269|PubMed:9295142}. SUBCELLULAR LOCATION: Note=Localized at the myotendinous junction in skeletal muscle and at the intercalated disk in cardiac muscle. {ECO:0000269|PubMed:11732910, ECO:0000269|PubMed:15765519, ECO:0000269|PubMed:9295142}. SUBUNIT: Interacts with actin, alpha-actinin, KLHL41, TLN1 and VCL. Interacts with CSRP3. {ECO:0000250|UniProtKB:Q86VF7, ECO:0000269|PubMed:10320340, ECO:0000269|PubMed:11732910, ECO:0000269|PubMed:12692149, ECO:0000269|PubMed:9295142}. TISSUE SPECIFICITY: Expressed in cardiac and skeletal muscle. Not detected in kidney, spleen, liver, brain, lung, stomach or uterus. {ECO:0000269|PubMed:11732910, ECO:0000269|PubMed:9295142}. +Q91ZA8 NRARP_MOUSE Notch-regulated ankyrin repeat-containing protein 114 12,492 Alternative sequence (2); Chain (1); Repeat (2) FUNCTION: Downstream effector of Notch signaling. Involved in the regulation of liver cancer cells self-renewal (By similarity). Involved in the regulation of canonical Wnt signaling by stabilizing LEF1 (By similarity). Involved in angiogenesis acting downstream of Notch at branch points to regulate vascular density. Proposed to integrate endothelial Notch and Wnt signaling to control stalk cell proliferation and to stablilize new endothelial connections during angiogenesis (PubMed:19154719). During somitogenesis involved in maintenance of proper somite segmentation and proper numbers of somites and vertebrae. Required for proper anterior-posterior somite patterning. Proposed to function in a negative feedback loop to destabilize Notch 1 intracellular domain (NICD) and downregulate the Notch signal, preventing expansion of the Notch signal into the anterior somite domain (PubMed:21795391, PubMed:21998026). {ECO:0000250|UniProtKB:Q7T3Y0, ECO:0000250|UniProtKB:Q7Z6K4, ECO:0000269|PubMed:11783997, ECO:0000269|PubMed:19154719, ECO:0000269|PubMed:21795391, ECO:0000269|PubMed:21998026, ECO:0000305|PubMed:21998026}. SUBUNIT: Interacts with LEF1. {ECO:0000269|PubMed:19154719}. TISSUE SPECIFICITY: Expressed at high levels in the brain, heart, colon, kidney, liver, lung and small intestine. Expressed in retina, most prominent in endothelial cells at the migrating point of the vasculature behind leading tip cells. Expressed in testis. {ECO:0000269|PubMed:11783997, ECO:0000269|PubMed:19154719, ECO:0000269|PubMed:24015274}. +Q91V36 NRBP2_MOUSE Nuclear receptor-binding protein 2 499 57,348 Chain (1); Domain (1); Erroneous initiation (2); Modified residue (2); Sequence conflict (1) FUNCTION: May regulate apoptosis of neural progenitor cells during their differentiation. {ECO:0000269|PubMed:18619852}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18619852}. DOMAIN: The protein kinase domain is predicted to be catalytically inactive. TISSUE SPECIFICITY: Expressed in Purkinje cells of the cerebellum and neurons in the CA3 region of the hippocampus. Also detected in non-neural tissues including mesenchymal layer adjacent to epithelium in developing bronchi of the lung, the epithelium of the stomach as well as cells in the liver. {ECO:0000269|PubMed:18619852}. +Q810U4 NRCAM_MOUSE Neuronal cell adhesion molecule (Nr-CAM) (Neuronal surface protein Bravo) (mBravo) (NgCAM-related cell adhesion molecule) (Ng-CAM-related) 1256 138,522 Alternative sequence (8); Chain (1); Disulfide bond (6); Domain (10); Erroneous initiation (2); Glycosylation (17); Modified residue (9); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1120 1142 Helical. {ECO:0000255}. TOPO_DOM 30 1119 Extracellular. {ECO:0000255}.; TOPO_DOM 1143 1256 Cytoplasmic. {ECO:0000255}. FUNCTION: Cell adhesion protein that is required for normal responses to cell-cell contacts in brain and in the peripheral nervous system. Plays a role in neurite outgrowth in response to contactin binding (PubMed:11564762). Plays a role in mediating cell-cell contacts between Schwann cells and axons (PubMed:20188654). Plays a role in the formation and maintenance of the nodes of Ranvier on myelinated axons. Nodes of Ranvier contain clustered sodium channels that are crucial for the saltatory propagation of action potentials along myelinated axons. During development, nodes of Ranvier are formed by the fusion of two heminodes. Required for normal clustering of sodium channels at heminodes; not required for the formation of mature nodes with normal sodium channel clusters (PubMed:14602817, PubMed:20188654). Required, together with GLDN, for maintaining NFASC and sodium channel clusters at mature nodes of Ranvier (PubMed:24719088). {ECO:0000269|PubMed:11564762, ECO:0000269|PubMed:14602817, ECO:0000269|PubMed:16039564, ECO:0000269|PubMed:20188654, ECO:0000269|PubMed:24719088}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20188654}; Single-pass type I membrane protein {ECO:0000305}. Cell projection, axon {ECO:0000269|PubMed:14602817}. Secreted {ECO:0000269|PubMed:20188654}. Note=Detected at nodes of Ranvier (PubMed:14602817, PubMed:20188654, PubMed:24719088). {ECO:0000269|PubMed:14602817, ECO:0000269|PubMed:20188654, ECO:0000269|PubMed:24719088}. SUBUNIT: Constituent of a NFASC/NRCAM/ankyrin-G complex (Probable). Detected in a complex with CNTN1 and PTPRB (PubMed:11564762). Interacts with GLDN/gliomedin and MYOC (PubMed:16039564, PubMed:23897819). {ECO:0000269|PubMed:11564762, ECO:0000269|PubMed:16039564, ECO:0000269|PubMed:23897819, ECO:0000305|PubMed:20188654}. TISSUE SPECIFICITY: Detected in sciatic nerve (PubMed:14602817, PubMed:20188654, PubMed:24719088). Detected in brain, especially in the cerebellum Purkinje cell layer, inner granule cell layer and molecular layer (at protein level) (PubMed:11564762). Detected in neurons and Schwann cells (PubMed:20188654). {ECO:0000269|PubMed:11564762, ECO:0000269|PubMed:14602817, ECO:0000269|PubMed:20188654, ECO:0000269|PubMed:24719088}. +Q9QZB6 NR4A3_MOUSE Nuclear receptor subfamily 4 group A member 3 (Orphan nuclear receptor TEC) (Translocated in extraskeletal chondrosarcoma) 627 68,454 Alternative sequence (2); Chain (1); Compositional bias (3); DNA binding (1); Domain (1); Region (4); Zinc finger (2) FUNCTION: Transcriptional activator that binds to regulatory elements in promoter regions in a cell- and response element (target)-specific manner (PubMed:12709428). Induces gene expression by binding as monomers to the NR4A1 response element (NBRE) 5'-AAAAGGTCA-3' site and as homodimers to the Nur response element (NurRE) site in the promoter of their regulated target genes (By similarity). Plays a role in the regulation of proliferation, survival and differentiation of many different cell types and also in metabolism and inflammation. Mediates proliferation of vascular smooth muscle, myeloid progenitor cell and type B pancreatic cells; promotes mitogen-induced vascular smooth muscle cell proliferation through transactivation of SKP2 promoter by binding a NBRE site (PubMed:21868379). Upon PDGF stimulation, stimulates vascular smooth muscle cell proliferation by regulating CCND1 and CCND2 expression. In islets, induces type B pancreatic cell proliferation through up-regulation of genes that activate cell cycle, as well as genes that cause degradation of the CDKN1A (By similarity). Negatively regulates myeloid progenitor cell proliferation by repressing RUNX1 in a NBRE site-independent manner (PubMed:24806827). During inner ear, plays a role as a key mediator of the proliferative growth phase of semicircular canal development (PubMed:11784868). Mediates also survival of neuron and smooth muscle cells; mediates CREB-induced neuronal survival, and during hippocampus development, plays a critical role in pyramidal cell survival and axonal guidance (PubMed:20566846, PubMed:15456880). Is required for S phase entry of the cell cycle and survival of smooth muscle cells by inducing CCND1, resulting in RB1 phosphorylation. Binds to NBRE motif in CCND1 promoter, resulting in the activation of the promoter and CCND1 transcription (PubMed:19153266). Plays also a role in inflammation; upon TNF stimulation, mediates monocyte adhesion by inducing the expression of VCAM1 and ICAM1 by binding to the NBRE consensus site (PubMed:20558821). In mast cells activated by Fc-epsilon receptor cross-linking, promotes the synthesis and release of cytokines but impairs events leading to degranulation (PubMed:24586680). Plays also a role in metabolism; by modulating feeding behavior; and by playing a role in energy balance by inhibiting the glucocorticoid-induced orexigenic neuropeptides AGRP expression, at least in part by forming a complex with activated NR3C1 on the AGRP- glucocorticoid response element (GRE), and thus weakening the DNA binding activity of NR3C1 (PubMed:23897430, PubMed:19523439). Upon catecholamines stimulation, regulates gene expression that controls oxidative metabolism in skeletal muscle (PubMed:18325999). Plays a role in glucose transport by regulating translocation of the SLC2A4 glucose transporter to the cell surface (By similarity). Finally, during gastrulation plays a crucial role in the formation of anterior mesoderm by controlling cell migration (PubMed:13129926). Inhibits adipogenesis (PubMed:18945812). Also participates in cardiac hypertrophy by activating PARP1 (By similarity). {ECO:0000250|UniProtKB:P51179, ECO:0000250|UniProtKB:Q92570, ECO:0000269|PubMed:11784868, ECO:0000269|PubMed:12709428, ECO:0000269|PubMed:13129926, ECO:0000269|PubMed:15456880, ECO:0000269|PubMed:18325999, ECO:0000269|PubMed:18945812, ECO:0000269|PubMed:19153266, ECO:0000269|PubMed:19523439, ECO:0000269|PubMed:20558821, ECO:0000269|PubMed:20566846, ECO:0000269|PubMed:21868379, ECO:0000269|PubMed:23897430, ECO:0000269|PubMed:24586680, ECO:0000269|PubMed:24806827}. PTM: Phosphorylated by PRKDC. {ECO:0000250|UniProtKB:Q92570}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}. SUBUNIT: Interacts with SIX3 (via homeobox); differentially regulates the transcriptional activities of NR4A3. Interacts with NCOA2; potentiates the activity of the NR4A3 (PubMed:12709428). Interacts with NCOA1, NCOA3, MED1 and KAT2B. Interacts with EP300 and NCOA2; mediates the recruitment of MED1 in the coactivator complex (PubMed:12709428). Interacts with the constituents of DNA-PK heterotrimer PRKDC, XRCC6 and XRCC5; phosphorylates and prevents NR4A3 ubiquitinylation and degradation (By similarity). Interacts with NR3C1 (via nuclear receptor DNA-binding domain); the interactions represses transcription activity of NR4A3 on the POMC promoter Nur response element (NurRE). Interacts with TRIM28; the interactions potentiates NR4A3 activity on NurRE promoter. Binds DNA as a monomer and homodimer. Interacts with PARP1; activates PARP1 by improving acetylation of PARP1 and suppressing the interaction between PARP1 and SIRT1 (By similarity). {ECO:0000250|UniProtKB:P51179, ECO:0000250|UniProtKB:Q92570, ECO:0000269|PubMed:12709428}. DOMAIN: The AF-1 domain mediates transcription activation. The N-terminal region (1-292) directly interacts with the C-terminal LBD (380-627): the interaction is potentiated by AF-1-mediated recruitment of NCOA2. {ECO:0000269|PubMed:12709428}. TISSUE SPECIFICITY: Ubiquitous. Highest levels of expression in brain. Widely expressed throughout the arcuate nucleus region of the hypothalamus, namely in AgRP neurons. +Q62092 NSG1_MOUSE Neuronal vesicle trafficking-associated protein 1 (M234) (Neuron-enriched endosomal protein of 21 kDa) (Neuron-specific protein family member 1) (p21) 185 20,929 Chain (1); Region (1); Sequence conflict (3); Topological domain (2); Transmembrane (1) TRANSMEM 83 103 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 82 Cytoplasmic. {ECO:0000250|UniProtKB:P02683}.; TOPO_DOM 104 185 Lumenal. {ECO:0000250|UniProtKB:P02683}. FUNCTION: Plays a role in the recycling mechanism in neurons of multiple receptors, including AMPAR, APP and L1CAM and acts at the level of early endosomes to promote sorting of receptors toward a recycling pathway (PubMed:15187090, PubMed:12070131, PubMed:21084623, PubMed:16037816). Regulates sorting and recycling of GRIA2 through interaction with GRIP1 and then contributes to the regulation of synaptic transmission and plasticity by affecting the recycling and targeting of AMPA receptors to the synapse (PubMed:16037816). Is required for faithful sorting of L1CAM to axons by facilitating trafficking from somatodendritic early endosome or the recycling endosome (By similarity). In an other hand, induces apoptosis via the activation of CASP3 in response to DNA damage (By similarity). {ECO:0000250|UniProtKB:P02683, ECO:0000250|UniProtKB:P42857, ECO:0000269|PubMed:12070131, ECO:0000269|PubMed:15187090, ECO:0000269|PubMed:16037816, ECO:0000269|PubMed:21084623}. SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P02683}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P02683}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:P02683}. Endosome membrane {ECO:0000250|UniProtKB:P02683}. Cell projection, dendrite {ECO:0000250|UniProtKB:P02683}. Early endosome membrane {ECO:0000250|UniProtKB:P02683}. Late endosome membrane {ECO:0000269|PubMed:28874679}. Lysosome lumen {ECO:0000250|UniProtKB:P02683}. Recycling endosome membrane {ECO:0000250|UniProtKB:P02683}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P02683}. Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:P02683}. Endosome, multivesicular body membrane {ECO:0000250|UniProtKB:P02683}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P42857}. Note=Endocytosed from the cell surface, thus enters into early endosomes, trafficks to late endosomes and degradates in lysosomes (By similarity). Endoplasmic reticulum targeting is essential for apoptosis (By similarity). Found in both stationary and motile endosomes (PubMed:28874679). A previous study supports a type I membrane protein topology (PubMed:12070131). {ECO:0000250|UniProtKB:P02683, ECO:0000250|UniProtKB:P42857, ECO:0000269|PubMed:12070131, ECO:0000269|PubMed:28874679}. SUBUNIT: Forms a complex with GRIP1, GRIA2 and STX12 through direct interaction with GRIP1; controls the intracellular fate of AMPAR and the endosomal sorting of the GRIA2 subunit toward recycling and membrane targeting. Interacts with STX12 (PubMed:12070131). Interacts with APP; could regulate APP processing (PubMed:21084623). {ECO:0000269|PubMed:12070131, ECO:0000269|PubMed:21084623}. TISSUE SPECIFICITY: Pituitary and less in adrenal gland and testis. Expressed in the hippocampus throughout development. At P0, highly and broadly expressed throughout the cortical plate, but is down-regulated overall at P8 and P14, but remains relatively enriched in layer V. At P0 is expressed ubiquitously in the developing cerebellum namely Purkinje neurons as well as granule neurons. However, it becomes restricted to Purkinje cells by P8. This exclusive expression in Purkinje cells is maintained throughout adulthood. {ECO:0000269|PubMed:28299779}. +O70572 NSMA_MOUSE Sphingomyelin phosphodiesterase 2 (EC 3.1.4.12) (Lyso-platelet-activating factor-phospholipase C) (Lyso-PAF-PLC) (Neutral sphingomyelinase) (N-SMase) (nSMase) 419 47,467 Active site (1); Chain (1); Metal binding (1); Site (1); Transmembrane (2) TRANSMEM 326 346 Helical. {ECO:0000255}.; TRANSMEM 354 374 Helical. {ECO:0000255}. Lipid metabolism; sphingolipid metabolism. FUNCTION: Converts sphingomyelin to ceramide. Hydrolyze 1-acyl-2-lyso-sn-glycero-3-phosphocholine (lyso-PC) and 1-O-alkyl-2-lyso-sn-glycero-3-phosphocholine (lyso-platelet-activating factor). The physiological substrate seems to be Lyso-PAF (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Although widely expressed in all tissues examined, except the spleen, high enzymatic activity occurs only in the brain. {ECO:0000269|PubMed:9520418}. +Q9DD16 NUD22_MOUSE Uridine diphosphate glucose pyrophosphatase (UDPG pyrophosphatase) (UGPPase) (EC 3.6.1.45) (Nucleoside diphosphate-linked moiety X motif 22) (Nudix motif 22) 308 33,376 Binding site (8); Chain (1); Domain (1); Metal binding (2); Motif (1); Sequence conflict (1) FUNCTION: Hydrolyzes UDP-glucose to glucose 1-phosphate and UMP and UDP-galactose to galactose 1-phosphate and UMP. Preferred substrate is UDP-glucose. {ECO:0000250|UniProtKB:Q9BRQ3}. +Q6PIP5 NUDC1_MOUSE NudC domain-containing protein 1 582 66,705 Chain (1); Domain (1); Modified residue (2); Sequence conflict (13) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. +Q9QXX8 NUFP1_MOUSE Nuclear fragile X mental retardation-interacting protein 1 (Nuclear FMRP-interacting protein 1) 484 54,713 Chain (1); Compositional bias (1); Modified residue (4); Motif (1); Zinc finger (1) FUNCTION: Binds RNA. {ECO:0000269|PubMed:10556305}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10556305}. Note=Distributed in the nucleus in a dot-like pattern. SUBUNIT: Interacts with FMR1 (PubMed:10556305). Interacts with ZNHIT3 (By similarity). {ECO:0000250|UniProtKB:Q9UHK0, ECO:0000269|PubMed:10556305}. TISSUE SPECIFICITY: Expressed in the brain; in neurons and not in glial cells. {ECO:0000269|PubMed:10556305}. +Q9Z2U0 PSA7_MOUSE Proteasome subunit alpha type-7 (EC 3.4.25.1) (Proteasome subunit RC6-1) 248 27,855 Beta strand (14); Chain (1); Glycosylation (1); Helix (6); Modified residue (2); Turn (3) FUNCTION: Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). {ECO:0000269|PubMed:16581775, ECO:0000269|PubMed:22341445}. PTM: Phosphorylation by ABL1 or ABL2 leads to an inhibition of proteasomal activity and cell cycle transition blocks. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O14818}. Nucleus {ECO:0000250|UniProtKB:O14818}. SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is a barrel-shaped complex made of 28 subunits that are arranged in four stacked rings. The two outer rings are each formed by seven alpha subunits, and the two inner rings are formed by seven beta subunits. The proteolytic activity is exerted by three beta-subunits PSMB5, PSMB6 and PSMB7 (PubMed:16857966, PubMed:22341445). PSMA7 interacts directly with the PSMG1-PSMG2 heterodimer which promotes 20S proteasome assembly (By similarity). Interacts with HIF1A (By similarity). Interacts with RAB7A (By similarity). Interacts with PRKN (By similarity). Interacts with ABL1 and ABL2 (By similarity). Interacts with EMAP2 (By similarity). Interacts with MAVS (By similarity). {ECO:0000250|UniProtKB:O14818, ECO:0000269|PubMed:16857966, ECO:0000269|PubMed:22341445}. TISSUE SPECIFICITY: Detected in liver (at protein level). {ECO:0000269|PubMed:22341445}. +Q91X97 NCALD_MOUSE Neurocalcin-delta 193 22,245 Calcium binding (3); Chain (1); Domain (4); Initiator methionine (1); Lipidation (1); Sequence conflict (2) FUNCTION: May be involved in the calcium-dependent regulation of rhodopsin phosphorylation. Binds three calcium ions (By similarity). {ECO:0000250}. +P59644 PI5PA_MOUSE Phosphatidylinositol 4,5-bisphosphate 5-phosphatase A (EC 3.1.3.56) (Inositol polyphosphate 5-phosphatase J) 1003 107,544 Chain (1); Compositional bias (2); Modified residue (11); Motif (6); Region (2); Sequence conflict (1) FUNCTION: Inositol 5-phosphatase, which converts inositol 1,4,5-trisphosphate to inositol 1,4-bisphosphate. Also converts phosphatidylinositol 4,5-bisphosphate to phosphatidylinositol 4-phosphate and inositol 1,3,4,5-tetrakisphosphate to inositol 1,3,4-trisphosphate in vitro. May be involved in modulation of the function of inositol and phosphatidylinositol polyphosphate-binding proteins that are present at membranes ruffles (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12536145}. Note=Predominantly localized to membrane ruffles. DOMAIN: The 5 Arg-Ser-Xaa-Ser-Xaa-Xaa (RSXSXX) motifs may constitute binding sites for the 14-3-3 protein. +Q7M6Y3 PICAL_MOUSE Phosphatidylinositol-binding clathrin assembly protein (Clathrin assembly lymphoid myeloid leukemia) (CALM) 660 71,543 Alternative sequence (3); Chain (1); Cross-link (1); Domain (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (5); Region (1); Sequence conflict (4) FUNCTION: Assembly protein recruiting clathrin and adapter protein complex 2 (AP2) to cell membranes at sites of coated-pit formation and clathrin-vesicle assembly. May be required to determine the amount of membrane to be recycled, possibly by regulating the size of the clathrin cage. Involved in AP2-dependent clathrin-mediated endocytosis at the neuromuscular junction. Plays a crucial role in fetal and adult hematopoiesis, and normal prenatal and postnatal growth and viability. {ECO:0000269|PubMed:12832620, ECO:0000269|PubMed:9292517}. SUBCELLULAR LOCATION: Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:Q13492}. Golgi apparatus {ECO:0000250|UniProtKB:Q13492}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:Q13492}. Nucleus {ECO:0000250|UniProtKB:Q13492}. Note=Colocalized with clathrin in the Golgi area. Interaction with PIMREG may target PICALM to the nucleus in some cells. {ECO:0000250|UniProtKB:Q13492}. SUBUNIT: Binds clathrin; involves primarily the C-terminal sequences, but the full-length protein is required for full binding capacity. Binds phosphatidylinositol 4,5- bisphosphate. Interacts with PIMREG; this interaction may change the subcellular location into the nucleus. {ECO:0000250|UniProtKB:Q13492}. TISSUE SPECIFICITY: Skins and livers of 1-week-old mice. {ECO:0000269|PubMed:12832620}. +Q01768 NDKB_MOUSE Nucleoside diphosphate kinase B (NDK B) (NDP kinase B) (EC 2.7.4.6) (Histidine protein kinase NDKB) (EC 2.7.13.3) (P18) (nm23-M2) 152 17,363 Active site (1); Binding site (6); Chain (1); Region (1) FUNCTION: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate (By similarity). Negatively regulates Rho activity by interacting with AKAP13/LBC. Acts as a transcriptional activator of the MYC gene; binds DNA non-specifically. Binds to both single-stranded guanine- and cytosine-rich strands within the nuclease hypersensitive element (NHE) III(1) region of the MYC gene promoter. Does not bind to duplex NHE III(1). Has G-quadruplex (G4) DNA-binding activity, which is independent of its nucleotide-binding and kinase activity. Binds both folded and unfolded G4 with similar low nanomolar affinities. Stabilizes folded G4s regardless of whether they are prefolded or not. Exhibits histidine protein kinase activity (By similarity). {ECO:0000250|UniProtKB:P22392, ECO:0000250|UniProtKB:P36010, ECO:0000269|PubMed:20884616}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P22392}. Nucleus {ECO:0000250|UniProtKB:P22392}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:P22392}. Cell projection, ruffle {ECO:0000250|UniProtKB:P22392}. Note=Colocalizes with ITGB1 and ITGB1BP1 at the edge or peripheral ruffles and lamellipodia during the early stages of cell spreading on fibronectin or collagen but not on vitronectin or laminin substrates. {ECO:0000250|UniProtKB:P22392}. SUBUNIT: Hexamer of two different chains: A and B (A6, A5B, A4B2, A3B3, A2B4, AB5, B6) (By similarity). Interacts with CAPN8 (PubMed:16476741). Interacts with AKAP13. Interacts ITGB1BP1 (via C-terminal domain region) (By similarity). {ECO:0000250|UniProtKB:P22392, ECO:0000269|PubMed:16476741}. TISSUE SPECIFICITY: Expressed in the base region of the oxyntic and pyloric mucosae. {ECO:0000269|PubMed:16476741}. +A2AI05 NDOR1_MOUSE NADPH-dependent diflavin oxidoreductase 1 (EC 1.18.1.-) (NADPH-dependent FMN and FAD-containing oxidoreductase) 598 67,183 Alternative sequence (4); Binding site (5); Chain (1); Domain (2); Nucleotide binding (7) FUNCTION: Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis. Transfers electrons from NADPH to the Fe/S cluster of CIAPIN1. {ECO:0000255|HAMAP-Rule:MF_03178}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000255|HAMAP-Rule:MF_03178}. Note=Concentrated in perinuclear structure. {ECO:0000255|HAMAP-Rule:MF_03178}. SUBUNIT: Interacts with CIAPIN1. Interacts with DCPS. {ECO:0000255|HAMAP-Rule:MF_03178}. +O35683 NDUA1_MOUSE NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1 (Complex I-MWFE) (CI-MWFE) (NADH-ubiquinone oxidoreductase MWFE subunit) 70 8,139 Beta strand (1); Chain (1); Helix (5); Transmembrane (1) TRANSMEM 1 21 Helical. {ECO:0000255}. FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. {ECO:0000250|UniProtKB:O15239}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:O15239}; Single-pass membrane protein {ECO:0000255}; Matrix side {ECO:0000250|UniProtKB:O15239}. SUBUNIT: Complex I is composed of 45 different subunits. {ECO:0000250|UniProtKB:O15239}. +Q62433 NDRG1_MOUSE Protein NDRG1 (N-myc downstream-regulated gene 1 protein) (Protein Ndr1) 394 43,009 Chain (1); Initiator methionine (1); Modified residue (19); Region (1); Repeat (3); Sequence conflict (7) FUNCTION: Stress-responsive protein involved in hormone responses, cell growth, and differentiation. Acts as a tumor suppressor in many cell types. Necessary but not sufficient for p53/TP53-mediated caspase activation and apoptosis. Required for vesicular recycling of CDH1 and TF. May also function in lipid trafficking. Protects cells from spindle disruption damage. Functions in p53/TP53-dependent mitotic spindle checkpoint. Regulates microtubule dynamics and maintains euploidy (By similarity). Has a role in cell trafficking notably of the Schwann cell and is necessary for the maintenance and development of the peripheral nerve myelin sheath. {ECO:0000250, ECO:0000269|PubMed:15082788, ECO:0000269|PubMed:21303696}. PTM: Under stress conditions, phosphorylated in the C-terminal on many serine and threonine residues. Phosphorylated in vitro by PKA. Phosphorylation enhanced by increased intracellular cAMP levels. Homocysteine induces dephosphorylation. Phosphorylation by SGK1 is cell cycle dependent (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Nucleus. Cell membrane {ECO:0000250}. Note=Mainly cytoplasmic but differentially localized to other regions. Associates with the plasma membrane in intestinal epithelia and lactating mammary gland. Translocated to the nucleus in a p53/TP53-dependent manner. In prostate epithelium and placental chorion, located in both the cytoplasm and in the nucleus. No nuclear localization in colon epithelium cells. In intestinal mucosa, prostate and renal cortex, located predominantly adjacent to adherens junctions. Cytoplasmic with granular staining in proximal tubular cells of the kidney and salivary gland ducts. Recruits to the membrane of recycling/sorting and late endosomes via binding to phosphatidylinositol 4-phosphate. Associates with microtubules. Colocalizes with TUBG1 in the centrosome. Cytoplasmic location increased with hypoxia. Phosphorylated form found associated with centromeres during S-phase of mitosis and with the plasma membrane (By similarity). {ECO:0000250}. SUBUNIT: Interacts with RAB4A (membrane-bound form); the interaction involves NDRG1 in vesicular recycling of CDH1. Interacts with APOA1, APOA2, PRA1 and RTN1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed, with highest levels in kidney followed by brain, pancreas, small intestine, colon and spleen (at protein level). Also detected in heart and preputial gland, and in much smaller quantities in other tissues. Not detected in duodenum and prostate. Highly expressed in Schwann cells. {ECO:0000269|PubMed:15082788, ECO:0000269|PubMed:15461589, ECO:0000269|PubMed:21636852, ECO:0000269|PubMed:9144177}. +Q9CQ75 NDUA2_MOUSE NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2 (Complex I-B8) (CI-B8) (NADH-ubiquinone oxidoreductase B8 subunit) 99 10,916 Beta strand (4); Chain (1); Disulfide bond (1); Helix (3); Initiator methionine (1); Modified residue (4); Sequence conflict (1); Turn (1) FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. {ECO:0000250|UniProtKB:O43678}. PTM: Acetylation of Lys-64 and Lys-75 is observed in liver mitochondria from fasted mice but not from fed mice. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:O43678}; Peripheral membrane protein {ECO:0000250|UniProtKB:O43678}; Matrix side {ECO:0000250|UniProtKB:O43678}. SUBUNIT: Complex I is composed of 45 different subunits. {ECO:0000250|UniProtKB:O43678}. +Q9QYT7 PIGQ_MOUSE Phosphatidylinositol N-acetylglucosaminyltransferase subunit Q (EC 2.4.1.198) (MGpi1p) (N-acetylglucosamyl transferase component GPI1) (Phosphatidylinositol-glycan biosynthesis class Q protein) (PIG-Q) 581 66,264 Chain (1); Sequence conflict (23); Transmembrane (5) TRANSMEM 276 298 Helical. {ECO:0000255}.; TRANSMEM 344 366 Helical. {ECO:0000255}.; TRANSMEM 381 403 Helical. {ECO:0000255}.; TRANSMEM 446 468 Helical. {ECO:0000255}.; TRANSMEM 478 500 Helical. {ECO:0000255}. Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis. FUNCTION: Part of the complex catalyzing the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Associates with PIGA, PIGC, PIGH, PIGP and DPM2. The latter is not essential for activity. +Q8BXQ2 PIGT_MOUSE GPI transamidase component PIG-T (Neuronal development-associated protein 7) (Phosphatidylinositol-glycan biosynthesis class T protein) 582 65,705 Chain (1); Disulfide bond (1); Erroneous initiation (4); Glycosylation (3); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 526 548 Helical. {ECO:0000255}. TOPO_DOM 26 525 Lumenal. {ECO:0000255}.; TOPO_DOM 549 582 Cytoplasmic. {ECO:0000255}. Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis. FUNCTION: Component of the GPI transamidase complex. Essential for transfer of GPI to proteins, particularly for formation of carbonyl intermediates (By similarity). {ECO:0000250}. PTM: The disulfide bond between PIGK/GPI8 and PIGT is important for normal enzyme activity. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein. SUBUNIT: Forms a complex with PIGK/GPI8, PIGS, PIGU and GPAA1/GAA1. Has a critical role in maintaining the complex by stabilizing the expression of GPAA1 and GPI8 and linking them to PIGS (By similarity). {ECO:0000250}. +Q9CQZ6 NDUB3_MOUSE NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3 (Complex I-B12) (CI-B12) (NADH-ubiquinone oxidoreductase B12 subunit) 104 11,692 Beta strand (4); Chain (1); Helix (2); Initiator methionine (1); Modified residue (8); Transmembrane (1); Turn (4) TRANSMEM 72 90 Helical. {ECO:0000255}. FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. {ECO:0000250|UniProtKB:O43676}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:O43676}; Single-pass membrane protein {ECO:0000250|UniProtKB:O43676}; Matrix side {ECO:0000250|UniProtKB:O43676}. SUBUNIT: Complex I is composed of 45 different subunits. {ECO:0000250|UniProtKB:O43676}. +P29595 NEDD8_MOUSE NEDD8 (Neddylin) (Neural precursor cell expressed developmentally down-regulated protein 8) (NEDD-8) (Ubiquitin-like protein Nedd8) 81 8,972 Chain (1); Cross-link (1); Modified residue (1); Propeptide (1); Region (1); Site (2) FUNCTION: Ubiquitin-like protein which plays an important role in cell cycle control and embryogenesis. Covalent attachment to its substrates requires prior activation by the E1 complex UBE1C-APPBP1 and linkage to the E2 enzyme UBE2M. Attachment of NEDD8 to cullins activates their associated E3 ubiquitin ligase activity, and thus promotes polyubiquitination and proteasomal degradation of cyclins and other regulatory proteins. {ECO:0000269|PubMed:11696557}. PTM: Cleavage of precursor form by UCHL3 or SENP8 is necessary for function. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12215427}. Note=Mainly nuclear. SUBUNIT: Directly interacts with NUB1. Covalently attached to cullins and p53 (By similarity). Interacts with AHR. {ECO:0000250, ECO:0000269|PubMed:12215427}. TISSUE SPECIFICITY: Ubiquitously expressed (at protein level). {ECO:0000269|PubMed:15183309, ECO:0000269|PubMed:8395831}. +Q9JKF6 NECT1_MOUSE Nectin-1 (Herpes virus entry mediator C) (Herpesvirus entry mediator C) (HveC) (Nectin cell adhesion molecule 1) (Poliovirus receptor-related protein 1) (CD antigen CD111) 515 57,035 Beta strand (9); Chain (1); Compositional bias (2); Disulfide bond (3); Domain (3); Glycosylation (7); Helix (1); Modified residue (5); Region (1); Sequence conflict (6); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (2) TRANSMEM 355 375 Helical. {ECO:0000255}. TOPO_DOM 31 354 Extracellular. {ECO:0000255}.; TOPO_DOM 376 515 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in cell adhesion and synaptogegesis. Has some neurite outgrowth-promoting activity. Receptor for alphaherpesvirus (HSV-1, HSV-2 and pseudorabies virus) entry into cells. {ECO:0000269|PubMed:11827984, ECO:0000269|PubMed:22955284}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11827984}; Single-pass type I membrane protein {ECO:0000269|PubMed:11827984}. Cell junction, synapse, presynaptic cell membrane {ECO:0000269|PubMed:11827984}. SUBUNIT: Cis- and trans-homodimer. Can form trans-heterodimers with NECTIN3. Interaction between NECTIN1 and NECTIN3 on the pre- and postsynaptic sites, respectively, initiates the formation of puncta adherentia junctions between axons and dendrites. Interacts (via Ig-like C2-type domain 2) with FGFR1, FGFR2 and FGFR3. Interacts (via Cytoplasmic domain) with AFDN, providing a connection with the actin cytoskeleton. Interacts with HSV glycoprotein D (gD). {ECO:0000269|PubMed:10744716, ECO:0000269|PubMed:11827984, ECO:0000269|PubMed:22955284}. DOMAIN: Ig-like C2-type 2 mediates neurite outgrowth through binding, induction of phosphorylation, and activation of FGFR. +Q5DTT1 NEXMI_MOUSE Neurite extension and migration factor (KIAA2022 protein associated with intellectual disability, language impairment and autistic behavior homolog) (KIDLIA) 1515 167,102 Alternative sequence (1); Chain (1); Erroneous initiation (1); Sequence conflict (1) FUNCTION: Involved in neurite outgrowth by regulating cell-cell adhesion via the N-cadherin signaling pathway. May act by regulating expression of protein-coding genes, such as N-cadherins and integrin beta-1 (ITGB1). {ECO:0000269|PubMed:27822498}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22531377, ECO:0000269|PubMed:27822498}. Cytoplasm {ECO:0000269|PubMed:22531377}. TISSUE SPECIFICITY: Expressed in the brain, particularly during the late embryonic and perinatal stages of development (PubMed:22531377). In the developing brain, it is expressed only in the cortical plate and subplate region but not in the intermediate or ventricular zone (PubMed:27822498). {ECO:0000269|PubMed:22531377, ECO:0000269|PubMed:27822498}. +Q9QZ23 NFU1_MOUSE NFU1 iron-sulfur cluster scaffold homolog, mitochondrial (HIRA-interacting protein 5) (mHIRIP5) 255 28,568 Beta strand (3); Chain (1); Erroneous initiation (1); Frameshift (2); Helix (4); Metal binding (2); Region (1); Sequence conflict (8); Transit peptide (1) FUNCTION: Iron-sulfur cluster scaffold protein which can assemble [4Fe-4S] clusters and deliver them to target proteins. {ECO:0000250|UniProtKB:Q9UMS0}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. SUBUNIT: Monomer and homohexamer; the apo-NFU1 is a monomer, while the holo-NFU1 is a hexamer composed of a trimer of dimer that is probably linked by some 4Fe-4S cluster. Interacts with HIRA and EPM2A/laforin. Interacts with BOLA3. Interacts with HSPA9. {ECO:0000250|UniProtKB:Q9UMS0}. +Q7TPW1 NEXN_MOUSE Nexilin (F-actin-binding protein) 607 72,108 Chain (1); Compositional bias (1); Domain (1); Modified residue (9); Sequence conflict (3) FUNCTION: Involved in regulating cell migration through association with the actin cytoskeleton. Has an essential role in the maintenance of Z line and sarcomere integrity. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q0ZGT2, ECO:0000250|UniProtKB:Q9Z2J4}. Cell junction, adherens junction {ECO:0000250|UniProtKB:Q0ZGT2, ECO:0000250|UniProtKB:Q9Z2J4}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:Q9Z2J4}. Note=Localizes to the cell-matrix AJ. Not found at the cell-cell AJ. {ECO:0000250|UniProtKB:Q0ZGT2, ECO:0000250|UniProtKB:Q9Z2J4}. SUBUNIT: Interacts with F-actin. {ECO:0000250|UniProtKB:Q0ZGT2}. +Q8K120 NFAC4_MOUSE Nuclear factor of activated T-cells, cytoplasmic 4 (NF-ATc4) (NFATc4) (T-cell transcription factor NFAT3) (NF-AT3) 901 95,782 Alternative sequence (2); Chain (1); Compositional bias (2); Cross-link (1); DNA binding (1); Domain (2); Modified residue (7); Motif (2); Region (2); Repeat (2); Sequence conflict (12) FUNCTION: Plays a role in the inducible expression of cytokine genes in T-cells, especially in the induction of the IL-2 and IL-4. Transcriptionally repressed by estrogen receptors; this inhibition is further enhanced by estrogen. Increases the transcriptional activity of PPARG and has a direct role in adipocyte differentiation. May play an important role in myotube differentiation (By similarity). May play a critical role in cardiac development and hypertrophy. May play a role in deafferentation-induced apoptosis of sensory neurons. {ECO:0000250|UniProtKB:Q14934, ECO:0000269|PubMed:17198697, ECO:0000269|PubMed:18354019, ECO:0000269|PubMed:9568714}. PTM: Phosphorylated by NFATC-kinases; dephosphorylated by calcineurin. Phosphorylated on Ser-168 and Ser-170 by MTOR, IRAK1, MAPK7 and MAPK14, on Ser-213 and Ser-217 by MAPK8 and MAPK9, and on Ser-289 and Ser-344 by RPS6KA3. Phosphorylated by GSK3B. {ECO:0000269|PubMed:18691762}.; PTM: Ubiquitinated, leading to its degradation by the proteasome and reduced transcriptional activity. Ubiquitination and reduction in transcriptional activity can be further facilitated through GSK3B-dependent phosphorylation. Polyubiquitin linkage is mainly through 'Lys-48' (By similarity). {ECO:0000250|UniProtKB:Q14934}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}. Note=Cytoplasmic for the phosphorylated form and nuclear after activation that is controlled by calcineurin-mediated dephosphorylation. Rapid nuclear exit of NFATC is thought to be one mechanism by which cells distinguish between sustained and transient calcium signals. The subcellular localization of NFATC plays a key role in the regulation of gene transcription. {ECO:0000305}. SUBUNIT: Member of the multicomponent NFATC transcription complex that consists of at least two components, a pre-existing cytoplasmic component NFATC2 and an inducible nuclear component NFATC1. Other members such as NFATC4, NFATC3 or members of the activating protein-1 family, MAF, GATA4 and Cbp/p300 can also bind the complex. NFATC proteins bind to DNA as monomers. Interacts with CREBBP, GATA4, IRAK1, MAPK8, MAPK9 and RPS6KA3. Interacts with HOMER2 and HOMER3 (By similarity). {ECO:0000250|UniProtKB:Q14934, ECO:0000269|PubMed:9568714}. DOMAIN: Rel Similarity Domain (RSD) allows DNA-binding and cooperative interactions with AP1 factors. {ECO:0000250|UniProtKB:O95644}. TISSUE SPECIFICITY: Expressed in all tissues analyzed including brain, lung, heart, testis and muscle. {ECO:0000269|PubMed:18675896}. +Q61985 NF2L1_MOUSE Endoplasmic reticulum membrane sensor NFE2L1 (Locus control region-factor 1) (LCR-F1) (Nuclear factor erythroid 2-related factor 1) (NF-E2-related factor 1) (NFE2-related factor 1) (Nuclear factor, erythroid derived 2, like 1) [Cleaved into: Transcription factor NRF1] 741 81,575 Alternative sequence (4); Chain (2); Compositional bias (3); Domain (1); Glycosylation (3); Modified residue (2); Motif (2); Mutagenesis (6); Region (4); Sequence conflict (2); Site (1); Transmembrane (1) TRANSMEM 7 24 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. FUNCTION: Endoplasmic reticulum membrane sensor NFE2L1: Endoplasmic reticulum membrane sensor that translocates into the nucleus in response to various stresses to act as a transcription factor (PubMed:20385086, PubMed:21536885, PubMed:23816881, PubMed:29149604). Constitutes a precursor of the transcription factor NRF1. Able to detect various cellular stresses, such as cholesterol excess, oxidative stress or proteasome inhibition (PubMed:20385086, PubMed:21536885, PubMed:23816881, PubMed:29149604). In response to stress, it is released from the endoplasmic reticulum membrane following cleavage by the protease DDI2 and translocates into the nucleus to form the transcription factor NRF1 (PubMed:29149604). Acts as a key sensor of cholesterol excess: in excess cholesterol conditions, the endoplasmic reticulum membrane form of the protein directly binds cholesterol via its CRAC motif, preventing cleavage and release of the transcription factor NRF1, thereby allowing expression of genes promoting cholesterol removal, such as CD36 (PubMed:29149604). Involved in proteasome homeostasis: in response to proteasome inhibition, it is released from the endoplasmic reticulum membrane, translocates to the nucleus and activates expression of genes encoding proteasome subunits (PubMed:20385086, PubMed:21536885, PubMed:23816881). {ECO:0000269|PubMed:20385086, ECO:0000269|PubMed:21536885, ECO:0000269|PubMed:23816881, ECO:0000269|PubMed:29149604}.; FUNCTION: Transcription factor NRF1: CNC-type bZIP family transcription factor that translocates to the nucleus and regulates expression of target genes in response to various stresses (PubMed:10601325, PubMed:11342101, PubMed:23144760, PubMed:16872277, PubMed:21911472, PubMed:23816881, PubMed:29149604). Heterodimerizes with small-Maf proteins (MAFF, MAFG or MAFK) and binds DNA motifs including the antioxidant response elements (AREs), which regulate expression of genes involved in oxidative stress response (PubMed:12808106, PubMed:15738389, PubMed:23144760, PubMed:16872277, PubMed:21911472, PubMed:23816881). Activates or represses expression of target genes, depending on the context (PubMed:12808106, PubMed:15738389, PubMed:23144760, PubMed:16872277, PubMed:21911472, PubMed:23816881). Plays a key role in cholesterol homeostasis by acting as a sensor of cholesterol excess: in low cholesterol conditions, translocates into the nucleus and represses expression of genes involved in defense against cholesterol excess, such as CD36 (PubMed:29149604). In excess cholesterol conditions, the endoplasmic reticulum membrane form of the protein directly binds cholesterol via its CRAC motif, preventing cleavage and release of the transcription factor NRF1, thereby allowing expression of genes promoting cholesterol removal (PubMed:29149604). Critical for redox balance in response to oxidative stress: acts by binding the AREs motifs on promoters and mediating activation of oxidative stress response genes, such as GCLC, GCLM, GSS, MT1 and MT2 (PubMed:10601325, PubMed:11342101, PubMed:12968018, PubMed:15738389, PubMed:18826952). Plays an essential role during fetal liver hematopoiesis: probably has a protective function against oxidative stress and is involved in lipid homeostasis in the liver (PubMed:9501099, PubMed:12808106, PubMed:15738389, PubMed:18826952, PubMed:22586274). Involved in proteasome homeostasis: in response to proteasome inhibition, mediates the 'bounce-back' of proteasome subunits by translocating into the nucleus and activating expression of genes encoding proteasome subunits (PubMed:20385086, PubMed:21536885, PubMed:23816881). Also involved in regulating glucose flux (PubMed:25041126). Together with CEBPB; represses expression of DSPP during odontoblast differentiation (By similarity). In response to ascorbic acid induction, activates expression of SP7/Osterix in osteoblasts (PubMed:17510056). {ECO:0000250|UniProtKB:Q14494, ECO:0000269|PubMed:10601325, ECO:0000269|PubMed:11342101, ECO:0000269|PubMed:12808106, ECO:0000269|PubMed:12968018, ECO:0000269|PubMed:15738389, ECO:0000269|PubMed:16872277, ECO:0000269|PubMed:17510056, ECO:0000269|PubMed:18826952, ECO:0000269|PubMed:20385086, ECO:0000269|PubMed:21536885, ECO:0000269|PubMed:21911472, ECO:0000269|PubMed:22586274, ECO:0000269|PubMed:23144760, ECO:0000269|PubMed:23816881, ECO:0000269|PubMed:25041126, ECO:0000269|PubMed:29149604, ECO:0000269|PubMed:9501099}.; FUNCTION: Isoform 2: Transcription factor that binds the antioxidant response elements (ARE) consensus sequence on promoters and activates their expression. {ECO:0000269|PubMed:23144760, ECO:0000269|PubMed:9580677}.; FUNCTION: Isoform 3: Transcription factor that binds the extended kappa 3 site of the TNF-alpha promoter after Fc gamma RIII stimulation and participates in the induction of this cytokine (PubMed:9580677). {ECO:0000269|PubMed:9580677}. PTM: Endoplasmic reticulum membrane sensor NFE2L1: Cleaved at Leu-104 by the aspartyl protease DDI2 following retrotranslocation, releasing the protein from the endoplasmic reticulum membrane and forming the transcription factor NRF1 that translocates into the nucleus. Ubiquitination is prerequisite for cleavage by aspartyl protease DDI2. {ECO:0000250|UniProtKB:Q14494}.; PTM: Endoplasmic reticulum membrane sensor NFE2L1: N-glycosylated in normal conditions, when it has a single-pass type II membrane protein topology, with the DNA-binding domain facing the endoplasmic reticulum lumen (PubMed:17705787, PubMed:18990090). Deglycosylated during retrotranslocation to the cytosolic side of the membrane, to have a single-pass type III membrane protein topology with the major part of the protein facing the cytosol (By similarity). {ECO:0000250|UniProtKB:Q14494, ECO:0000269|PubMed:17705787, ECO:0000269|PubMed:18990090}.; PTM: Endoplasmic reticulum membrane sensor NFE2L1: Ubiquitinated by the SCF(FBXW7) complex and SYVN1/HRD1, leading to its degradation by the proteasome (PubMed:21953459, PubMed:21911472). Ubiquitinated during retrotranslocation to the cytosolic side of the membrane: ubiquitination does not lead to degradation and is required for processing by the aspartyl protease DDI2 and subsequent release from the endoplasmic reticulum membrane (By similarity). {ECO:0000250|UniProtKB:Q14494, ECO:0000269|PubMed:21911472, ECO:0000269|PubMed:21953459}.; PTM: Transcription factor NRF1: Phosphorylation by CK2 at Ser-497 inhibits transcription factor activity, possibly by affecting DNA-binding activity (PubMed:9580677, PubMed:23816881). Phosphorylation at Ser-568 is required for interaction with CEBPB (By similarity). {ECO:0000250|UniProtKB:Q14494, ECO:0000269|PubMed:23816881, ECO:0000269|PubMed:9580677}.; PTM: Transcription factor NRF1: Ubiquitinated by the SCF(BTRC) complex in the nucleus, leading to its degradation by the proteasome. {ECO:0000269|PubMed:21911472}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane sensor NFE2L1: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16872277, ECO:0000269|PubMed:17705787, ECO:0000269|PubMed:18990090, ECO:0000269|PubMed:20629635, ECO:0000269|PubMed:21911472, ECO:0000269|PubMed:29149604}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q14494}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:16872277, ECO:0000269|PubMed:17705787, ECO:0000269|PubMed:18990090, ECO:0000269|PubMed:20629635, ECO:0000269|PubMed:21911472, ECO:0000269|PubMed:29149604}; Single-pass type III membrane protein {ECO:0000250|UniProtKB:Q14494}. Note=In normal conditions, probably has a single-pass type II membrane protein topology, with the DNA-binding domain facing the endoplasmic reticulum lumen (By similarity). Following cellular stress, it is rapidly and efficiently retrotranslocated to the cytosolic side of the membrane, a process dependent on p97/VCP, to have a single-pass type III membrane protein topology with the major part of the protein facing the cytosol (By similarity). Retrotranslocated proteins are normally rapidly degraded by the proteasome and active species do not accumulate (By similarity). However, retrotranslocated protein NFE2L1 escapes degradation and is cleaved at Leu-104 by DDI2, releasing the protein from the endoplasmic reticulum membrane and forming the transcription factor NRF1 that translocates into the nucleus (By similarity). {ECO:0000250|UniProtKB:Q14494}.; SUBCELLULAR LOCATION: Transcription factor NRF1: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:21911472, ECO:0000269|PubMed:23144760, ECO:0000269|PubMed:29149604}. Note=Translocates into the nucleus following cleavage of Endoplasmic reticulum membrane sensor NFE2L1 by aspartyl protease DDI2. {ECO:0000305|PubMed:29149604}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm {ECO:0000269|PubMed:23144760}. Nucleus {ECO:0000269|PubMed:23144760}. SUBUNIT: Interacts with KEAP1 (By similarity). Endoplasmic reticulum membrane sensor NFE2L1: Interacts (via CPD region) with FBXW7; leading to its ubiquitination and degradation (PubMed:21953459). Endoplasmic reticulum membrane sensor NFE2L1: Interacts with SYVN1/HRD1; leading to its ubiquitination and degradation (PubMed:21911472). Endoplasmic reticulum membrane sensor NFE2L1: Interacts (when ubiquitinated) with DDI2; leading to its cleavage (By similarity). Transcription factor NRF1: Interacts (via the bZIP domain) with small MAF protein (MAFF, MAFG or MAFK); required for binding to antioxidant response elements (AREs) on DNA (PubMed:11342101, PubMed:23144760). Transcription factor NRF1: Interacts (via Destruction motif) with BTRC; leading to its ubiquitination and degradation (PubMed:21911472). Transcription factor NRF1: Interacts with CEBPB; the heterodimer represses expression of DSPP during odontoblast differentiation (By similarity). {ECO:0000250|UniProtKB:Q14494, ECO:0000269|PubMed:11342101, ECO:0000269|PubMed:18990090, ECO:0000269|PubMed:21911472, ECO:0000269|PubMed:21953459, ECO:0000269|PubMed:23144760}. DOMAIN: The cholesterol recognition/amino acid consensus (CRAC) region directly binds cholesterol, as well as campesterol and 27-hydroxycholesterol (PubMed:29149604). Has much lower affinity for epicholesterol (PubMed:29149604). {ECO:0000269|PubMed:29149604}. TISSUE SPECIFICITY: Isoform 1: Widely expressed including kidney, brown fat, white fat, large intestine, small intestine, stomach, lung, brain and liver (PubMed:23144760). Isoform 1: Expressed in mouse embryonic fibroblasts (MEF) (PubMed:23144760). Isoform 2: Widely expressed including kidney, brown fat, white fat, large intestine, small intestine, stomach, lung, brain and liver (PubMed:23144760). Isoform 2: levels in white fat, lung and liver are increased compared to isoform 1 (at protein level) (PubMed:23144760). Isoform 2: levels are elevated in brown fat and brain, but are reduced in liver compared to isoform 1 levels (PubMed:23144760). Isoform 2: Expressed in mouse embryonic fibroblasts (MEF) (PubMed:23144760). {ECO:0000269|PubMed:23144760}. +Q8BG99 PKNX2_MOUSE Homeobox protein PKNOX2 (Homeobox protein PREP-2) (PBX/knotted homeobox 2) 474 52,331 Chain (1); Compositional bias (2); DNA binding (1); Erroneous initiation (1) SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. +P47937 NK3R_MOUSE Neuromedin-K receptor (NKR) (NK-3 receptor) (NK-3R) (Neurokinin B receptor) (Tachykinin receptor 3) 452 51,026 Chain (1); Disulfide bond (1); Glycosylation (4); Lipidation (1); Sequence conflict (4); Topological domain (8); Transmembrane (7) TRANSMEM 72 94 Helical; Name=1. {ECO:0000255}.; TRANSMEM 105 126 Helical; Name=2. {ECO:0000255}.; TRANSMEM 147 168 Helical; Name=3. {ECO:0000255}.; TRANSMEM 189 209 Helical; Name=4. {ECO:0000255}.; TRANSMEM 233 257 Helical; Name=5. {ECO:0000255}.; TRANSMEM 287 308 Helical; Name=6. {ECO:0000255}.; TRANSMEM 322 346 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 71 Extracellular. {ECO:0000255}.; TOPO_DOM 95 104 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 127 146 Extracellular. {ECO:0000255}.; TOPO_DOM 169 188 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 210 232 Extracellular. {ECO:0000255}.; TOPO_DOM 258 286 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 309 321 Extracellular. {ECO:0000255}.; TOPO_DOM 347 452 Cytoplasmic. {ECO:0000255}. FUNCTION: This is a receptor for the tachykinin neuropeptide neuromedin-K (neurokinin B). It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system. PTM: The anchoring of this receptor to the plasma membrane is probably mediated by the palmitoylation of a cysteine residue. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q5SZT7 NKAPL_MOUSE NKAP-like protein 395 44,894 Chain (1); Compositional bias (1); Modified residue (3); Sequence caution (1); Sequence conflict (7) FUNCTION: Transcriptional repressor of Notch-mediated signaling. Required for spermatogenesis. {ECO:0000269|PubMed:25875095}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25875095}. SUBUNIT: Interacts with RBPJ, CIR1 and HDAC3. {ECO:0000269|PubMed:25875095}. TISSUE SPECIFICITY: Specific to testis (at protein level). Detected in differenting spermatogonia and early spermatocytes (at protein level). {ECO:0000269|PubMed:25875095}. +Q99MH6 NKD1_MOUSE Protein naked cuticle homolog 1 (Naked-1) (mNkd) (mNkd1) 471 52,391 Calcium binding (1); Chain (1); Compositional bias (1); Domain (1); Frameshift (1); Initiator methionine (1); Lipidation (1); Mutagenesis (4); Region (1); Sequence conflict (5) FUNCTION: Cell autonomous antagonist of the canonical Wnt signaling pathway. May activate a second Wnt signaling pathway that controls planar cell polarity. Required for spermatogenesis. {ECO:0000269|PubMed:11274398, ECO:0000269|PubMed:11356022, ECO:0000269|PubMed:15546883}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with DVL1, DVL2, DVL3 and PPP2R3A. {ECO:0000269|PubMed:11274398, ECO:0000269|PubMed:11356022, ECO:0000269|PubMed:15687260}. TISSUE SPECIFICITY: Highly expressed in lung. Also expressed in brain, heart, kidney, liver, skin, stomach and testis. Within the testis expression is found in the seminiferous epithelium and round and elongating spermatids. {ECO:0000269|PubMed:11274398, ECO:0000269|PubMed:11356022, ECO:0000269|PubMed:15546883}. +Q9JJC8 NIPA2_MOUSE Magnesium transporter NIPA2 (Non-imprinted in Prader-Willi/Angelman syndrome region protein 2 homolog) 359 39,091 Chain (1); Topological domain (10); Transmembrane (9) TRANSMEM 10 30 Helical. {ECO:0000255}.; TRANSMEM 57 77 Helical. {ECO:0000255}.; TRANSMEM 79 99 Helical. {ECO:0000255}.; TRANSMEM 108 128 Helical. {ECO:0000255}.; TRANSMEM 150 170 Helical. {ECO:0000255}.; TRANSMEM 176 196 Helical. {ECO:0000255}.; TRANSMEM 216 236 Helical. {ECO:0000255}.; TRANSMEM 247 267 Helical. {ECO:0000255}.; TRANSMEM 279 299 Helical. {ECO:0000255}. TOPO_DOM 1 9 Extracellular. {ECO:0000255}.; TOPO_DOM 31 56 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 78 78 Extracellular. {ECO:0000255}.; TOPO_DOM 100 107 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 129 149 Extracellular. {ECO:0000255}.; TOPO_DOM 171 175 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 197 215 Extracellular. {ECO:0000255}.; TOPO_DOM 237 246 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 268 278 Extracellular. {ECO:0000255}.; TOPO_DOM 300 359 Cytoplasmic. {ECO:0000255}. FUNCTION: Acts as a selective Mg(2+) transporter. {ECO:0000269|PubMed:18667602}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Early endosome {ECO:0000269|PubMed:18667602}. Note=Recruited to the cell membrane in response to low extracellular magnesium. TISSUE SPECIFICITY: Widely expressed. Expressed at high levels in the kidney. {ECO:0000269|PubMed:14508708, ECO:0000269|PubMed:18667602}. +Q69ZK9 NLGN2_MOUSE Neuroligin-2 836 90,989 Beta strand (24); Chain (1); Disulfide bond (3); Erroneous initiation (1); Glycosylation (3); Helix (24); Modified residue (2); Region (1); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (5) TRANSMEM 679 699 Helical. {ECO:0000255}. TOPO_DOM 15 678 Extracellular. {ECO:0000255}.; TOPO_DOM 700 836 Cytoplasmic. {ECO:0000255}. FUNCTION: Transmembrane scaffolding protein involved in cell-cell interactions via its interactions with neurexin family members. Mediates cell-cell interactions both in neurons and in other types of cells, such as Langerhans beta cells. Mediates cell-cell interactions between Langerhans beta cells and modulates insulin secretion (By similarity). Plays a role in synapse function and synaptic signal transmission, especially via gamma-aminobutyric acid receptors (GABA(A) receptors). Functions by recruiting and clustering synaptic proteins. Promotes clustering of postsynaptic GABRG2 and GPHN. Promotes clustering of postsynaptic LHFPL4 (PubMed:29742426). Modulates signaling by inhibitory synapses, and thereby plays a role in controlling the ratio of signaling by excitatory and inhibitory synapses and information processing. Required for normal signal amplitude from inhibitory synapses, but is not essential for normal signal frequency. May promote the initial formation of synapses, but is not essential for this. In vitro, triggers the de novo formation of presynaptic structures. {ECO:0000250, ECO:0000269|PubMed:10892652, ECO:0000269|PubMed:15620359, ECO:0000269|PubMed:16982420, ECO:0000269|PubMed:19553444, ECO:0000269|PubMed:19889999, ECO:0000269|PubMed:20530218, ECO:0000269|PubMed:29742426}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Cell junction, synapse, postsynaptic cell membrane {ECO:0000269|PubMed:29742426}. Cell junction, synapse, presynaptic cell membrane. Note=Detected at postsynaptic membranes in brain. Detected at dendritic spines in cultured neurons. Colocalizes with GPHN and ARHGEF9 at neuronal cell membranes (By similarity). Localized at presynaptic membranes in retina. Colocalizes with GABRG2 at inhibitory synapses in the retina. {ECO:0000250}. SUBUNIT: Interacts with NRXN1, NRXN2 and NRXN3. Interacts (via its C-terminus) with DLG4/PSD-95 (via PDZ domain 3). Interacts with PATJ (By similarity). Interacts with MDGA2 (By similarity). Interacts with GPHN (PubMed:19755106). Interacts with MDGA1 (PubMed:23358245). Found in a complex with MAGI2 and IGSF9B, where it interacts with MAGI2 (via WW 1, WW 2 and PDZ 2 domains) (PubMed:23751499). Identified in a complex of 720 kDa composed of LHFPL4, NLGN2, GABRA1, GABRB2, GABRG2 and GABRB3 (By similarity). Interacts with LHFPL4; leading to mutual regulation of the protein level and synaptic clustering (PubMed:29742426, PubMed:28279354). Interacts with GABRA1 (By similarity). {ECO:0000250|UniProtKB:Q62888, ECO:0000250|UniProtKB:Q8NFZ4, ECO:0000269|PubMed:17897391, ECO:0000269|PubMed:19755106, ECO:0000269|PubMed:23358245, ECO:0000269|PubMed:28279354, ECO:0000269|PubMed:29742426}. TISSUE SPECIFICITY: Brain and arteries. Detected in the retina outer plexiform layer (at protein level). Widely expressed. Detected in heart, brain, spleen, lung, liver, skeletal muscle, kidney and testis. {ECO:0000269|PubMed:16982420, ECO:0000269|PubMed:18434543, ECO:0000269|PubMed:19755106, ECO:0000269|PubMed:19859968, ECO:0000269|PubMed:19926856}. +Q8BMW7 NIPA3_MOUSE Magnesium transporter NIPA3 (NIPA-like protein 1) (Non-imprinted in Prader-Willi/Angelman syndrome region protein 3 homolog) 416 45,159 Chain (1); Frameshift (1); Glycosylation (4); Topological domain (10); Transmembrane (9) TRANSMEM 68 88 Helical. {ECO:0000255}.; TRANSMEM 115 135 Helical. {ECO:0000255}.; TRANSMEM 137 157 Helical. {ECO:0000255}.; TRANSMEM 166 186 Helical. {ECO:0000255}.; TRANSMEM 208 228 Helical. {ECO:0000255}.; TRANSMEM 234 254 Helical. {ECO:0000255}.; TRANSMEM 274 294 Helical. {ECO:0000255}.; TRANSMEM 306 326 Helical. {ECO:0000255}.; TRANSMEM 337 357 Helical. {ECO:0000255}. TOPO_DOM 1 67 Extracellular. {ECO:0000255}.; TOPO_DOM 89 114 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 136 136 Extracellular. {ECO:0000255}.; TOPO_DOM 158 165 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 187 207 Extracellular. {ECO:0000255}.; TOPO_DOM 229 233 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 255 273 Extracellular. {ECO:0000255}.; TOPO_DOM 295 305 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 327 336 Extracellular. {ECO:0000255}.; TOPO_DOM 358 416 Cytoplasmic. {ECO:0000255}. FUNCTION: Acts as a Mg(2+) transporter. Can also transport other divalent cations such as Fe(2+), Sr(2+), Ba(2+), Mn(2+), Cu(2+) and Co(2+) but to a much less extent than Mg(2+). {ECO:0000269|PubMed:18667602}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8BYM5 NLGN3_MOUSE Neuroligin-3 (Gliotactin homolog) 825 91,162 Chain (1); Disulfide bond (3); Glycosylation (2); Modified residue (2); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 687 707 Helical. {ECO:0000255}. TOPO_DOM 35 686 Extracellular. {ECO:0000255}.; TOPO_DOM 708 825 Cytoplasmic. {ECO:0000255}. FUNCTION: Cell surface protein involved in cell-cell-interactions via its interactions with neurexin family members. Plays a role in synapse function and synaptic signal transmission, and probably mediates its effects by recruiting and clustering other synaptic proteins. May promote the initial formation of synapses, but is not essential for this. May also play a role in glia-glia or glia-neuron interactions in the developing peripheral nervous system. {ECO:0000269|PubMed:16982420}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17897391}; Single-pass type I membrane protein {ECO:0000269|PubMed:17897391}. Cell junction, synapse {ECO:0000269|PubMed:17897391}. Note=Detected at both glutamatergic and GABAergic synapses. SUBUNIT: Interacts with NRXN1, NRXN2 and NRXN3. Interacts (via its C-terminus) with DLG4/PSD-95 (via PDZ domain 3) (By similarity). Homodimer, and heterodimer with NLGN1 and NLGN2 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Brain and arteries (at protein level). Detected in heart, brain, spleen, lung, liver, skeletal muscle, kidney and testis. Expressed in olfactory bulb and olfactory epithelium. Found in olfactory ensheathing glia but not in olfactory neurons, and in developing peripheral glia. {ECO:0000269|PubMed:11329178, ECO:0000269|PubMed:16982420, ECO:0000269|PubMed:17897391, ECO:0000269|PubMed:18434543, ECO:0000269|PubMed:19926856}. +P53351 PLK2_MOUSE Serine/threonine-protein kinase PLK2 (EC 2.7.11.21) (Polo-like kinase 2) (PLK-2) (Serine/threonine-protein kinase SNK) (Serum-inducible kinase) 682 77,812 Active site (1); Binding site (1); Chain (1); Compositional bias (1); Domain (3); Modified residue (1); Mutagenesis (3); Nucleotide binding (1) FUNCTION: Tumor suppressor serine/threonine-protein kinase involved in synaptic plasticity, centriole duplication and G1/S phase transition. Polo-like kinases act by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates CENPJ, NPM1, RAPGEF2, RASGRF1, SNCA, SIPA1L1 and SYNGAP1. Plays a key role in synaptic plasticity and memory by regulating the Ras and Rap protein signaling: required for overactivity-dependent spine remodeling by phosphorylating the Ras activator RASGRF1 and the Rap inhibitor SIPA1L1 leading to their degradation by the proteasome. Conversely, phosphorylates the Rap activator RAPGEF2 and the Ras inhibitor SYNGAP1, promoting their activity. Also regulates synaptic plasticity independently of kinase activity, via its interaction with NSF that disrupts the interaction between NSF and the GRIA2 subunit of AMPARs, leading to a rapid rundown of AMPAR-mediated current that occludes long term depression. Required for procentriole formation and centriole duplication by phosphorylating CENPJ and NPM1, respectively. Its induction by p53/TP53 suggests that it may participate in the mitotic checkpoint following stress. {ECO:0000269|PubMed:12651910, ECO:0000269|PubMed:12897130, ECO:0000269|PubMed:19004816, ECO:0000269|PubMed:21382555}. PTM: Catalytic activity is enhanced by phosphorylation of Thr-236. {ECO:0000269|PubMed:12651910}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Note=Localizes to centrosomes during early G1 phase where it only associates to the mother centriole and then distributes equally to both mother and daughter centrioles at the onset of S phase. {ECO:0000250}. SUBUNIT: Interacts with NSF; causing NSF dissociation from GRIA2 (By similarity). Interacts with CIB1. {ECO:0000250}. DOMAIN: The POLO box domains act as phosphopeptide-binding module that recognize and bind serine-[phosphothreonine/phosphoserine]-(proline/X) motifs. PLK2 recognizes and binds docking proteins that are already phosphorylated on these motifs, and then phosphorylates them (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Brain, lung and heart. {ECO:0000269|PubMed:1508211}. +O55125 NIPS1_MOUSE Protein NipSnap homolog 1 (NipSnap1) 284 33,363 Chain (1); Modified residue (12) +Q64702 PLK4_MOUSE Serine/threonine-protein kinase PLK4 (EC 2.7.11.21) (Polo-like kinase 4) (PLK-4) (Serine/threonine-protein kinase 18) (Serine/threonine-protein kinase Sak) 925 103,746 Active site (1); Alternative sequence (3); Beta strand (5); Binding site (1); Chain (1); Domain (2); Erroneous initiation (1); Helix (1); Modified residue (4); Mutagenesis (1); Nucleotide binding (1); Sequence conflict (9); Turn (1) FUNCTION: Serine/threonine-protein kinase that plays a central role in centriole duplication. Able to trigger procentriole formation on the surface of the parental centriole cylinder, leading to the recruitment of centriole biogenesis proteins such as SASS6, CENPJ/CPAP, CCP110, CEP135 and gamma-tubulin. When overexpressed, it is able to induce centrosome amplification through the simultaneous generation of multiple procentrioles adjoining each parental centriole during S phase. Phosphorylates 'Ser-151' of FBXW5 during the G1/S transition, leading to inhibit FBXW5 ability to ubiquitinate SASS6. Its central role in centriole replication suggests a possible role in tumorigenesis, centrosome aberrations being frequently observed in tumors. Phosphorylates CDC25C and CHEK2. Also involved in deuterosome-mediated centriole amplification in multiciliated that can generate more than 100 centrioles. Also involved in trophoblast differentiation by phosphorylating HAND1, leading to disrupt the interaction between HAND1 and MDFIC and activate HAND1. Required for the recruitment of STIL to the centriole and for STIL-mediated centriole amplification (By similarity). {ECO:0000250|UniProtKB:O00444, ECO:0000269|PubMed:17891141, ECO:0000269|PubMed:24240477}. PTM: Ubiquitinated; leading to its degradation by the proteasome. {ECO:0000269|PubMed:8756623}.; PTM: Tyrosine-phosphorylated by TEC. {ECO:0000250}.; PTM: Acetylation by KAT2A and KAT2B impairs kinase activity by shifting the kinase to an inactive conformation. {ECO:0000250|UniProtKB:O00444}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:11301255}. Nucleus, nucleolus {ECO:0000269|PubMed:11301255}. Cleavage furrow {ECO:0000269|PubMed:11301255}. Note=Associates with centrioles throughout the cell cycle. According to PubMed:11301255, it localizes to the nucleolus during G2, to the centrosomes in G2/M, and to the cleavage furrow during cytokinesis. Component of the deuterosome, a structure that promotes de novo centriole amplification in multiciliated cells that can generate more than 100 centrioles. SUBUNIT: Homodimer (PubMed:12352953). Interacts with CEP152 (via N-terminus) (By similarity). Interacts with CEP78; this interaction may be important for proper PLK4 localization to the centriole and PLK4-induced overduplication of centrioles (By similarity). {ECO:0000250|UniProtKB:O00444, ECO:0000269|PubMed:12352953}. TISSUE SPECIFICITY: expressed in tissues associated with mitotic and meiotic cell division. Highly expressed in testis. {ECO:0000269|PubMed:8022793}. +Q4FZD7 PLK5_MOUSE Inactive serine/threonine-protein kinase PLK5 (Polo-like kinase 5) (PLK-5) 595 66,055 Active site (1); Binding site (1); Chain (1); Domain (2); Erroneous initiation (1); Frameshift (1); Mutagenesis (2); Nucleotide binding (1); Sequence conflict (1) FUNCTION: Inactive serine/threonine-protein kinase that plays a role in cell cycle progression and neuronal differentiation. {ECO:0000269|PubMed:20100802, ECO:0000269|PubMed:21245385}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:20100802}. Cytoplasm {ECO:0000250}. DOMAIN: The protein kinase domain is predicted to be catalytically inactive; has lost the main activatory autophosphorylation site and the conserved key residues involved in phospho-substrate. The C-terminal region (containing the POLO box domain) is sufficient for inducing cell cycle arrest (By similarity). {ECO:0000255|PROSITE-ProRule:PRU00159}. TISSUE SPECIFICITY: Expressed in the cerebellum, eye and brain cortex (at protein level). Expressed in highly differentiated tissues, such as brain, eyes and ovary. Not detectable in proliferating tissues, such as the colon, spleen and placenta. +Q9DCU2 PLLP_MOUSE Plasmolipin (Plasma membrane proteolipid) 182 19,801 Chain (1); Domain (1); Modified residue (1); Topological domain (5); Transmembrane (4) TRANSMEM 36 56 Helical. {ECO:0000255}.; TRANSMEM 69 89 Helical. {ECO:0000255}.; TRANSMEM 100 120 Helical. {ECO:0000255}.; TRANSMEM 142 162 Helical. {ECO:0000255}. TOPO_DOM 1 35 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 57 68 Extracellular. {ECO:0000255}.; TOPO_DOM 90 99 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 121 141 Extracellular. {ECO:0000255}.; TOPO_DOM 163 182 Cytoplasmic. {ECO:0000255}. FUNCTION: Appears to be involved in myelination. Could also participate in ion transport events as addition of plasmolipin to lipid bilayers induces the formation of ion channels, which are voltage-dependent and K(+)-selective (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SUBUNIT: Hexamer arranged as a trimer of two plasmolipin subunits. {ECO:0000250}. +Q9R1Q7 PLP2_MOUSE Proteolipid protein 2 152 16,608 Chain (1); Domain (1); Transmembrane (4) TRANSMEM 25 45 Helical. {ECO:0000255}.; TRANSMEM 48 68 Helical. {ECO:0000255}.; TRANSMEM 85 105 Helical. {ECO:0000255}.; TRANSMEM 112 132 Helical. {ECO:0000255}. FUNCTION: May play a role in cell differentiation in the intestinal epithelium. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q8BW10 NOB1_MOUSE RNA-binding protein NOB1 403 45,464 Beta strand (5); Chain (1); Compositional bias (1); Domain (1); Metal binding (4); Modified residue (3) FUNCTION: May play a role in mRNA degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: May interact with UPF2. {ECO:0000305|Ref.3}. +Q9ESX4 NO40_MOUSE Nucleolar protein of 40 kDa (pNO40) (Putative S1 RNA-binding domain protein) (PS1D protein) (Zinc finger CCHC domain-containing protein 17) 241 27,472 Alternative sequence (1); Chain (1); Compositional bias (2); Domain (1); Modified residue (3); Zinc finger (1) SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12202495, ECO:0000269|PubMed:12893261}. SUBUNIT: Interacts with PNN (By similarity). Associates with the 60S ribosomal subunit. {ECO:0000250, ECO:0000269|PubMed:12202495}. TISSUE SPECIFICITY: Expressed in liver, brain, heart, kidney testis, stomach, small intestine, skin, thymus, uterus, placenta, spleen, lung and skeletal muscle. {ECO:0000269|PubMed:12202495, ECO:0000269|PubMed:12893261}. +Q9D6Z1 NOP56_MOUSE Nucleolar protein 56 (Nucleolar protein 5A) 580 64,464 Chain (1); Compositional bias (1); Cross-link (4); Domain (1); Modified residue (16); Sequence conflict (3) FUNCTION: Involved in the early to middle stages of 60S ribosomal subunit biogenesis. Core component of box C/D small nucleolar ribonucleoprotein (snoRNP) particles. Required for the biogenesis of box C/D snoRNAs such U3, U8 and U14 snoRNAs (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:21683323}. Nucleus, nucleoplasm {ECO:0000250}. SUBUNIT: Part of a large pre-ribosomal ribonucleoprotein (RNP) complex, that consists of at least 62 ribosomal proteins, 45 nonribosomal proteins and both pre-rRNA and mature rRNA species. Within this complex directly interacts with TCOF1 in an RNA-independent manner. Core component of box C/D small nucleolar ribonucleoprotein (snoRNP) particles; the core proteins SNU13, NOP56, NOP58 and FBL assemble stepwise onto the snoRNA. Interacts NOP1 and NOP58. Interacts with NUFIP1, RUVBL1 and RUVBL2; RUVBL1:RUVBL2 seem to bridge the association of NOP56 with NUFIP1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed, with highest levels in the central nervous system (CNS), including cerebral cortex and cerebellum, and spleen. In the CNS, expressed in Purkinje cells of the cerebellum, as well as in motor neurons of the hypoglossal nucleus and in the spinal cord anterior horn (at protein level). {ECO:0000269|PubMed:21683323}. +Q3V1D5 PLPL1_MOUSE Patatin-like phospholipase domain-containing protein 1 (EC 3.1.1.-) 599 65,170 Active site (2); Chain (1); Compositional bias (2); Domain (1); Motif (2) FUNCTION: Lipid hydrolase. {ECO:0000250}. +E9Q5C9 NOLC1_MOUSE Nucleolar and coiled-body phosphoprotein 1 (140 kDa nucleolar phosphoprotein) (Nopp140) 702 73,698 Alternative sequence (2); Chain (1); Compositional bias (1); Cross-link (21); Domain (1); Modified residue (19); Motif (3); Region (2); Repeat (11); Sequence conflict (16) FUNCTION: Nucleolar protein that acts as a regulator of RNA polymerase I by connecting RNA polymerase I with enzymes responsible for ribosomal processing and modification (By similarity). Required for neural crest specification: following monoubiquitination by the BCR(KBTBD8) complex, associates with TCOF1 and acts as a platform to connect RNA polymerase I with enzymes responsible for ribosomal processing and modification, leading to remodel the translational program of differentiating cells in favor of neural crest specification (By similarity). Involved in nucleologenesis, possibly by playing a role in the maintenance of the fundamental structure of the fibrillar center and dense fibrillar component in the nucleolus (PubMed:11424213). It has intrinsic GTPase and ATPase activities (By similarity). {ECO:0000250|UniProtKB:Q14978, ECO:0000269|PubMed:11424213}. PTM: Undergoes rapid and massive phosphorylation/dephosphorylation cycles on CK2 and PKC sites. NOLC1 is one of the mostly phosphorylated proteins in the cell. {ECO:0000250|UniProtKB:Q14978}.; PTM: Ubiquitinated. Monoubiquitination by the BCR(KBTBD8) complex promotes the formation of a NOLC1-TCOF1 complex that acts as a platform to connect RNA polymerase I with enzymes responsible for ribosomal processing and modification, leading to remodel the translational program of differentiating cells in favor of neural crest specification. {ECO:0000250|UniProtKB:Q14978}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q14978}. Cytoplasm {ECO:0000250|UniProtKB:Q14978}. Note=Shuttles between the nucleolus and the cytoplasm. At telophase it begins to assemble into granular-like pre-nucleolar bodies which are subsequently relocated to nucleoli at the early G1-phase. {ECO:0000250|UniProtKB:Q14978}. SUBUNIT: Interacts with RNA polymerase I 194 kDa subunit (RPA194) and with casein kinase-II (By similarity). Interacts with DKC1/NAP57, NOP58 and fibrillarin (By similarity). {ECO:0000250|UniProtKB:P41777, ECO:0000250|UniProtKB:Q14978}. +P43021 NODAL_MOUSE Nodal 354 40,476 Chain (1); Disulfide bond (4); Glycosylation (1); Propeptide (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Essential for mesoderm formation and axial patterning during embryonic development. {ECO:0000269|PubMed:8429908, ECO:0000269|PubMed:8582278}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}. +Q8K1N1 PLPL8_MOUSE Calcium-independent phospholipase A2-gamma (EC 3.1.1.5) (Intracellular membrane-associated calcium-independent phospholipase A2 gamma) (iPLA2-gamma) (Patatin-like phospholipase domain-containing protein 8) 776 87,381 Active site (2); Chain (1); Domain (1); Erroneous initiation (1); Erroneous termination (1); Glycosylation (2); Modified residue (1); Motif (3); Sequence conflict (3); Transmembrane (1) TRANSMEM 469 489 Helical. {ECO:0000255}. FUNCTION: Calcium-independent phospholipase A2, which catalyzes the hydrolysis of the sn-2 position of glycerophospholipids, PtdSer and to a lower extent PtdCho. Cleaves membrane phospholipids (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. +Q99JY8 PLPP3_MOUSE Phospholipid phosphatase 3 (EC 3.1.3.4) (Lipid phosphate phosphohydrolase 3) (PAP2-beta) (Phosphatidate phosphohydrolase type 2b) (Phosphatidic acid phosphatase 2b) (PAP-2b) (PAP2b) 312 35,216 Chain (1); Glycosylation (1); Modified residue (1); Sequence conflict (1); Topological domain (7); Transmembrane (6) TRANSMEM 34 54 Helical. {ECO:0000255}.; TRANSMEM 86 106 Helical. {ECO:0000255}.; TRANSMEM 124 144 Helical. {ECO:0000255}.; TRANSMEM 195 215 Helical. {ECO:0000255}.; TRANSMEM 227 247 Helical. {ECO:0000255}.; TRANSMEM 259 279 Helical. {ECO:0000255}. TOPO_DOM 1 33 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 55 85 Lumenal. {ECO:0000255}.; TOPO_DOM 107 123 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 145 194 Lumenal. {ECO:0000255}.; TOPO_DOM 216 226 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 248 258 Lumenal. {ECO:0000255}.; TOPO_DOM 280 312 Cytoplasmic. {ECO:0000255}. FUNCTION: Catalyzes the conversion of phosphatidic acid (PA) to diacylglycerol (DG). In addition it hydrolyzes lysophosphatidic acid (LPA), ceramide-1-phosphate (C-1-P) and sphingosine-1-phosphate (S-1-P) (By similarity). Essential to the formation of the chorioallantoic placenta and extraembryonic vasculature. Also mediates gastrulation and axis formation, probably by regulating the Wnt signaling pathway. {ECO:0000250, ECO:0000269|PubMed:12925589}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. DISEASE: Note=Ppap2b deficient embryos fail to form a chorioallantoic placenta and yolk sac vasculature. A subset of embryos also show a shortening of the anterior-posterior axis and frequent duplication of axial structures. Loss of Ppap2b results in a marked increase in beta-catenin-mediated T-cell factor (TCF) transcription. {ECO:0000269|PubMed:12925589}. +Q8VCM2 NOXO1_MOUSE NADPH oxidase organizer 1 (Nox organizer 1) (Sorting nexin-28) 349 38,827 Alternative sequence (2); Chain (1); Domain (3); Region (1); Sequence conflict (5) FUNCTION: Constitutively potentiates the superoxide-generating activity of NOX1 and NOX3 and is required for the biogenesis of otoconia/otolith, which are crystalline structures of the inner ear involved in the perception of gravity. Isoform 3 is more potent than isoform 1 in activating NOX3. Together with NOXA1, may also substitute to NCF1/p47phox and NCF2/p67phox in supporting the phagocyte NOX2/gp91phox superoxide-generating activity. {ECO:0000269|PubMed:12473664, ECO:0000269|PubMed:16431374}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8NFA2}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8NFA2}; Cytoplasmic side {ECO:0000250|UniProtKB:Q8NFA2}. Note=Associates with the plasma membrane in a lipid-dependent manner. {ECO:0000250|UniProtKB:Q8NFA2}. SUBUNIT: Interacts with NOX1, NOXA1, CYBA/p22phox and NCF2/p67phox. Interacts with SH3PXD2A and SH3PXD2B. {ECO:0000250}. DOMAIN: The PX domain mediates lipid-binding, localization to the plasma membrane and is required for NOX1 activation. {ECO:0000250}.; DOMAIN: The SH3 domains mediate interaction with CYBA/p22phox. {ECO:0000250}. TISSUE SPECIFICITY: Strongly expressed by colon epithelial cells and to a lower extent in small intestine, uterus, stomach and testis. Expressed in different parts of the inner ear including sensory and nonsensory cell layers of the saccule, ampullae of the semicircular canals, the stria vascularis and the spiral glanglion neurons. {ECO:0000269|PubMed:12473664, ECO:0000269|PubMed:15949904, ECO:0000269|PubMed:16431374}. +O09159 MA2B1_MOUSE Lysosomal alpha-mannosidase (Laman) (EC 3.2.1.24) (Lysosomal acid alpha-mannosidase) (Mannosidase alpha class 2B member 1) (Mannosidase alpha-B) 1013 114,648 Active site (1); Chain (1); Disulfide bond (4); Erroneous initiation (2); Glycosylation (11); Metal binding (4); Sequence conflict (10); Signal peptide (1) FUNCTION: Necessary for the catabolism of N-linked carbohydrates released during glycoprotein turnover. SUBCELLULAR LOCATION: Lysosome. +Q9WU40 MAN1_MOUSE Inner nuclear membrane protein Man1 (LEM domain-containing protein 3) 921 100,307 Alternative sequence (1); Chain (1); Compositional bias (9); DNA binding (1); Domain (1); Frameshift (1); Modified residue (11); Region (1); Sequence conflict (2); Transmembrane (2) TRANSMEM 486 506 Helical. {ECO:0000255}.; TRANSMEM 637 657 Helical. {ECO:0000255}. FUNCTION: Can function as a specific repressor of TGF-beta, activin, and BMP signaling through its interaction with the R-SMAD proteins. Antagonizes TGF-beta-induced cell proliferation arrest (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus inner membrane; Multi-pass membrane protein. SUBUNIT: Interacts with SMAD1, SMAD2, SMAD3 and SMAD5. Binds to both phosphorylated and unphosphorylated R-SMADS (By similarity). {ECO:0000250}. +Q7TQJ1 MALD1_MOUSE MARVEL domain-containing protein 1 173 19,087 Chain (1); Compositional bias (1); Domain (1); Modified residue (1); Sequence conflict (1); Topological domain (5); Transmembrane (4) TRANSMEM 30 50 Helical. {ECO:0000255}.; TRANSMEM 60 80 Helical. {ECO:0000255}.; TRANSMEM 95 115 Helical. {ECO:0000255}.; TRANSMEM 139 159 Helical. {ECO:0000255}. TOPO_DOM 1 29 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 51 59 Extracellular. {ECO:0000255}.; TOPO_DOM 81 94 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 116 138 Extracellular. {ECO:0000255}.; TOPO_DOM 160 173 Cytoplasmic. {ECO:0000255}. FUNCTION: Microtubule-associated protein that exhibits cell cycle-dependent localization and can inhibit cell proliferation and migration. {ECO:0000269|PubMed:21347699}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21347699}; Multi-pass membrane protein {ECO:0000269|PubMed:21347699}. Nucleus {ECO:0000269|PubMed:21347699}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:21347699}. Note=Observed in the nucleus and at the perinuclear region during interphase, but localizes at the mitotic spindle and midbody at metaphase. A significant fraction of MARVELD1 translocates to the plasma membrane during anaphase or upon microtubule depolymerization. +Q91WD5 NDUS2_MOUSE NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial (EC 1.6.99.3) (EC 7.1.1.2) (Complex I-49kD) (CI-49kD) (NADH-ubiquinone oxidoreductase 49 kDa subunit) 463 52,626 Beta strand (11); Chain (1); Erroneous initiation (1); Helix (18); Metal binding (3); Modified residue (2); Sequence conflict (5); Transit peptide (1); Turn (10) FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. {ECO:0000250|UniProtKB:O75306}. PTM: Dimethylation at Arg-118 by NDUFAF7 takes place after NDUFS2 assembles into the complex I, leading to stabilize the early intermediate complex. {ECO:0000250|UniProtKB:O75306}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:O75306}; Peripheral membrane protein {ECO:0000250|UniProtKB:O75306}; Matrix side {ECO:0000250|UniProtKB:O75306}. SUBUNIT: Complex I is composed of 45 different subunits. Component of the iron-sulfur (IP) fragment of the enzyme. Interacts with NDUFAF3. Interacts with NDUFAF7. {ECO:0000250|UniProtKB:O75306}. +Q6P1J0 MANEL_MOUSE Glycoprotein endo-alpha-1,2-mannosidase-like protein (EC 3.2.1.-) 452 51,106 Chain (1); Compositional bias (2); Topological domain (2); Transmembrane (1) TRANSMEM 9 29 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 8 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 30 452 Lumenal. {ECO:0000255}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. +Q9CXZ1 NDUS4_MOUSE NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial (Complex I-18 kDa) (CI-18 kDa) (Complex I-AQDQ) (CI-AQDQ) (NADH-ubiquinone oxidoreductase 18 kDa subunit) 175 19,785 Beta strand (1); Chain (1); Erroneous initiation (1); Helix (3); Sequence conflict (1); Transit peptide (1); Turn (3) FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. {ECO:0000250|UniProtKB:O43181}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:O43181}; Peripheral membrane protein {ECO:0000250|UniProtKB:O43181}; Matrix side {ECO:0000250|UniProtKB:O43181}. SUBUNIT: Mammalian complex I is composed of 45 different subunits. This is a component of the iron-sulfur (IP) fragment of the enzyme. {ECO:0000250|UniProtKB:O43181}. +P06801 MAOX_MOUSE NADP-dependent malic enzyme (NADP-ME) (EC 1.1.1.40) (Malic enzyme 1) 572 63,954 Active site (2); Binding site (2); Chain (1); Metal binding (3); Modified residue (2); Nucleotide binding (1); Sequence conflict (6); Site (1) SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Homotetramer. +Q8R4I7 NETO1_MOUSE Neuropilin and tolloid-like protein 1 (Brain-specific transmembrane protein containing 2 CUB and 1 LDL-receptor class A domains protein 1) 533 60,242 Chain (1); Disulfide bond (7); Domain (3); Glycosylation (2); Modified residue (1); Motif (1); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 345 365 Helical. {ECO:0000255}. TOPO_DOM 23 344 Extracellular. {ECO:0000255}.; TOPO_DOM 366 533 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in the development and/or maintenance of neuronal circuitry. Accessory subunit of the neuronal N-methyl-D-aspartate receptor (NMDAR) critical for maintaining the abundance of GRIN2A-containing NMDARs in the postsynaptic density. Regulates long-term NMDA receptor-dependent synaptic plasticity and cognition, at least in the context of spatial learning and memory. {ECO:0000269|PubMed:12810072, ECO:0000269|PubMed:19243221}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000269|PubMed:19243221}. Note=Component of the postsynaptic density (PSD) of excitatory synapses. SUBUNIT: Interacts with PLZ domains of DLG2, DLG3 and DLG4 via its C-terminal TRV domain. Interacts with GRIN2A and GRIN2B via its CUB domains. {ECO:0000269|PubMed:19243221}. TISSUE SPECIFICITY: Expressed only in brain. Present throughout the central nervous system. Highly expressed in the hippocampal CA3 region, olfactory bulb and tubercle, caudate putamen, and neocortex in the adult brain. {ECO:0000269|PubMed:12810072, ECO:0000269|PubMed:15464227, ECO:0000269|PubMed:19243221}. +Q8BJS7 MAP10_MOUSE Microtubule-associated protein 10 (Microtubule regulator of 120 KDa) 891 96,155 Chain (1); Compositional bias (1); Sequence conflict (6) FUNCTION: Microtubule-associated protein (MAP) that plays a role in the regulation of cell division; promotes microtubule stability and participates in the organization of the spindle midzone and normal progress of cytokinesis. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Midbody {ECO:0000250}. Note=Localized at stabilized microtubules (MTs) during interphase and to the mitotic apparatus during mitosis. Localized at spindle poles in metaphase and spindle midzone during telophase. Colocalized with Polo-like kinase PLK1 to the center of spindle midzone. Localized at the midbody during cytokinesis. Colocalized with acetylated-tubulin at MTs (By similarity). {ECO:0000250}. SUBUNIT: Interacts (via middle region) with microtubules. {ECO:0000250}. +O08762 NETR_MOUSE Neurotrypsin (EC 3.4.21.-) (Brain-specific serine protease 3) (BSSP-3) (Motopsin) (Serine protease 12) 761 84,118 Active site (3); Chain (1); Disulfide bond (17); Domain (5); Glycosylation (3); Region (1); Signal peptide (1); Site (1) FUNCTION: Plays a role in neuronal plasticity and the proteolytic action may subserve structural reorganizations associated with learning and memory operations. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Most abundant in cerebral cortex, hippocampus and amygdala. +Q9CPW9 MAP12_MOUSE Methionine aminopeptidase 1D, mitochondrial (MAP 1D) (MetAP 1D) (EC 3.4.11.18) (Methionyl aminopeptidase type 1D, mitochondrial) (Peptidase M 1D) 335 37,262 Alternative sequence (1); Binding site (2); Chain (1); Metal binding (7); Sequence conflict (1); Transit peptide (1) FUNCTION: Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed. {ECO:0000255|HAMAP-Rule:MF_03174}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03174}. +Q8JZL2 MCHR1_MOUSE Melanin-concentrating hormone receptor 1 (MCH receptor 1) (MCH-R1) (MCHR-1) (G-protein coupled receptor 24) (MCH-1R) (MCH1R) (MCHR) (SLC-1) (Somatostatin receptor-like protein) 353 39,120 Alternative sequence (1); Chain (1); Glycosylation (3); Topological domain (8); Transmembrane (7) TRANSMEM 46 66 Helical; Name=1. {ECO:0000255}.; TRANSMEM 80 100 Helical; Name=2. {ECO:0000255}.; TRANSMEM 117 139 Helical; Name=3. {ECO:0000255}.; TRANSMEM 162 182 Helical; Name=4. {ECO:0000255}.; TRANSMEM 205 225 Helical; Name=5. {ECO:0000255}.; TRANSMEM 257 277 Helical; Name=6. {ECO:0000255}.; TRANSMEM 295 315 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 45 Extracellular. {ECO:0000305}.; TOPO_DOM 67 79 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 101 116 Extracellular. {ECO:0000305}.; TOPO_DOM 140 161 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 183 204 Extracellular. {ECO:0000305}.; TOPO_DOM 226 256 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 278 294 Extracellular. {ECO:0000305}.; TOPO_DOM 316 353 Cytoplasmic. {ECO:0000305}. FUNCTION: Receptor for melanin-concentrating hormone, coupled to both G proteins that inhibit adenylyl cyclase and G proteins that activate phosphoinositide hydrolysis. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBUNIT: Interacts with NCDN. {ECO:0000250}. TISSUE SPECIFICITY: Expressed predominantly in the brain. Expression in brain is negatively regulated by leptin. Also found in the epithelium of the tongue and kidney. {ECO:0000269|PubMed:11159839}. +Q8BL03 MCATL_MOUSE Mitochondrial basic amino acids transporter (Carnitine/acylcarnitine translocase-like) (CACT-like) (Mitochondrial carnitine/acylcarnitine carrier protein CACL) (Mitochondrial ornithine transporter 3) (Solute carrier family 25 member 29) 306 32,672 Chain (1); Repeat (3); Transmembrane (6) TRANSMEM 2 22 Helical; Name=1. {ECO:0000255}.; TRANSMEM 61 81 Helical; Name=2. {ECO:0000255}.; TRANSMEM 96 116 Helical; Name=3. {ECO:0000255}.; TRANSMEM 153 172 Helical; Name=4. {ECO:0000255}.; TRANSMEM 187 207 Helical; Name=5. {ECO:0000255}.; TRANSMEM 255 275 Helical; Name=6. {ECO:0000255}. FUNCTION: Transports arginine, lysine, homoarginine, methylarginine and, to a much lesser extent, ornithine and histidine. Does not transport carnitine nor acylcarnitines. Functions by both counter-exchange and uniport mechanisms (By similarity). Can restore ornithine transport in cells lacking the primary mitochondrial ornithine transporter SLC25A15 (PubMed:19287344). {ECO:0000250|UniProtKB:Q8N8R3, ECO:0000269|PubMed:19287344}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:12882971, ECO:0000269|PubMed:19287344}; Multi-pass membrane protein {ECO:0000269|PubMed:12882971, ECO:0000269|PubMed:19287344}. TISSUE SPECIFICITY: Widely expressed, with highest levels in the brain, including cortex, cerebellum, hippocampus and hypothalamus, and moderate levels in liver, kidney, heart and testis. {ECO:0000269|PubMed:12882971, ECO:0000269|PubMed:19287344}. +P97310 MCM2_MOUSE DNA replication licensing factor MCM2 (EC 3.6.4.12) (Minichromosome maintenance protein 2 homolog) (Nuclear protein BM28) 904 102,078 Chain (1); Cross-link (1); Domain (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (19); Motif (1); Mutagenesis (1); Nucleotide binding (1); Region (1); Sequence conflict (8); Zinc finger (1) FUNCTION: Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. Required for the entry in S phase and for cell division. Plays a role in terminally differentiated hair cells development of the cochlea and induces cells apoptosis. {ECO:0000250|UniProtKB:P49736}. PTM: Phosphorylated on Ser-108 by ATR in proliferating cells. Ser-108 proliferation is increased by genotoxic agents. Ser-40 is mediated by the CDC7-DBF4 and CDC7-DBF4B complexes, while Ser-53 phosphorylation is only mediated by the CDC7-DBF4 complex. Phosphorylation by the CDC7-DBF4 complex during G1/S phase is required for the initiation of DNA replication (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P49736}. SUBUNIT: Component of the MCM2-7 complex. The complex forms a toroidal hexameric ring with the proposed subunit order MCM2-MCM6-MCM4-MCM7-MCM3-MCM5. Interacts with KAT7 and DBF4. May interact with MCM10 (By similarity). Component of the replisome complex composed of at least DONSON, MCM2, MCM7, PCNA and TICRR (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P49736}. +P25206 MCM3_MOUSE DNA replication licensing factor MCM3 (EC 3.6.4.12) (DNA polymerase alpha holoenzyme-associated protein P1) (P1-MCM3) 812 91,546 Chain (1); Domain (1); Initiator methionine (1); Modified residue (15); Motif (1); Nucleotide binding (1); Sequence conflict (1) FUNCTION: Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. Required for DNA replication and cell proliferation. PTM: O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Component of the MCM2-7 complex. The complex forms a toroidal hexameric ring with the proposed subunit order MCM2-MCM6-MCM4-MCM7-MCM3-MCM5 (Probable). Associated with the replication-specific DNA polymerase alpha. Interacts with MCMBP. Interacts with ANKRD17. {ECO:0000250|UniProtKB:P25205, ECO:0000305}. +Q8R4F0 MCLN3_MOUSE Mucolipin-3 (Transient receptor potential channel mucolipin 3) (TRPML3) 553 63,748 Chain (1); Disulfide bond (2); Erroneous initiation (3); Glycosylation (2); Intramembrane (1); Motif (1); Mutagenesis (1); Natural variant (2); Region (2); Sequence conflict (3); Site (1); Topological domain (8); Transmembrane (6) INTRAMEM 444 464 Pore-forming. {ECO:0000250|UniProtKB:F6RG56}. TRANSMEM 63 83 Helical. {ECO:0000250|UniProtKB:F6RG56}.; TRANSMEM 284 304 Helical. {ECO:0000250|UniProtKB:F6RG56}.; TRANSMEM 342 362 Helical. {ECO:0000250|UniProtKB:F6RG56}.; TRANSMEM 372 392 Helical. {ECO:0000250|UniProtKB:F6RG56}.; TRANSMEM 415 435 Helical. {ECO:0000250|UniProtKB:F6RG56}.; TRANSMEM 476 497 Helical. {ECO:0000250|UniProtKB:F6RG56}. TOPO_DOM 1 62 Cytoplasmic. {ECO:0000250|UniProtKB:F6RG56}.; TOPO_DOM 84 283 Extracellular. {ECO:0000250|UniProtKB:F6RG56}.; TOPO_DOM 305 341 Cytoplasmic. {ECO:0000250|UniProtKB:F6RG56}.; TOPO_DOM 363 371 Extracellular. {ECO:0000250|UniProtKB:F6RG56}.; TOPO_DOM 393 414 Cytoplasmic. {ECO:0000250|UniProtKB:F6RG56}.; TOPO_DOM 436 443 Extracellular. {ECO:0000250|UniProtKB:F6RG56}.; TOPO_DOM 465 475 Extracellular. {ECO:0000250|UniProtKB:F6RG56}.; TOPO_DOM 498 553 Cytoplasmic. {ECO:0000250|UniProtKB:F6RG56}. FUNCTION: Nonselective ligand-gated cation channel probably playing a role in the regulation of membrane trafficking events. Acts as Ca(2+)-permeable cation channel with inwardly rectifying activity (PubMed:17989217). Mediates release of Ca(2+) from endosomes to the cytoplasm, contributes to endosomal acidification and is involved in the regulation of membrane trafficking and fusion in the endosomal pathway (By similarity). Does not seem to act as mechanosensory transduction channel in inner ear sensory hair cells. Proposed to play a critical role at the cochlear stereocilia ankle-link region during hair-bundle growth (PubMed:18801844). Involved in the regulation of autophagy. Through association with GABARAPL2 may be involved in autophagosome formation possibly providing Ca(2+) for the fusion process (PubMed:24269818). Through a possible and probably tissue-specific heteromerization with MCOLN1 may be at least in part involved in many lysosome-dependent cellular events. Possible heteromeric ion channel assemblies with TRPV5 show pharmacological similarity with TRPML3 (By similarity). {ECO:0000250|UniProtKB:Q8TDD5, ECO:0000269|PubMed:17989217, ECO:0000269|PubMed:18801844, ECO:0000269|PubMed:24269818}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q8TDD5}. SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000250|UniProtKB:Q8TDD5}; Multi-pass membrane protein {ECO:0000250|UniProtKB:F6RG56}. Late endosome membrane {ECO:0000269|PubMed:17989217}; Multi-pass membrane protein {ECO:0000250|UniProtKB:F6RG56}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:24269818}; Multi-pass membrane protein {ECO:0000250|UniProtKB:F6RG56}. Cell projection, stereocilium membrane {ECO:0000269|PubMed:18801844}; Multi-pass membrane protein {ECO:0000250|UniProtKB:F6RG56}. Note=Recycles between the plasma membrane and intracellular compartments by a dynamin-dependent endocytic pathway (By similarity). In the cochlea located at the base of stereocilia near the position of the ankle links. {ECO:0000250|UniProtKB:Q8TDD5, ECO:0000269|PubMed:18801844}. SUBUNIT: Homotetramer. Can heterooligomerize with MCOLN1; heteromeric assemblies have different channel properties as compared to the respective homooligomers and may be tissue-specific. May heterooligomerize with TRPV5 to form a functional distinct ion channel (By similarity). Interacts with GABARAPL2 (PubMed:24269818). {ECO:0000250|UniProtKB:Q8TDD5, ECO:0000269|PubMed:24269818}. DOMAIN: The most N-terminal extracellular/lumenal domain (referred to as I-II linker or polycystin-mucolipin domain) contributes to a structure with a four-fold rotational symmetry in a tetrameric assembly; the structure contains a central highly electronegative pore with a 14 A diameter. The pore is critical for Ca(2+) and pH regulation. The protruding structure formed by the I-II linkers may contain all the interaction sites with lipids and proteins in the endolysosomal lumen. {ECO:0000250|UniProtKB:Q9GZU1}. TISSUE SPECIFICITY: Expressed in the cochlea; particularly in the inner and outer hair cells (at protein level). {ECO:0000269|PubMed:12403827, ECO:0000269|PubMed:18801844}. DISEASE: Note=Defects in Mcoln3 are the cause of the varitin-waddler (Va) phenotype. Classical Va mice exhibit early-onset hearing loss, vestibular defects, pigmentation abnormalities and perinatal lethality. The phenotype varitin-waddler Jackcon (Va-J), which arose in a cross segregating for Va, is similar but less severe. {ECO:0000269|PubMed:12403827, ECO:0000269|PubMed:18048323}. +C3VPR6 NLRC5_MOUSE Protein NLRC5 1915 211,710 Alternative sequence (2); Beta strand (1); Chain (1); Domain (1); Helix (7); Nucleotide binding (1); Repeat (27); Sequence conflict (9) FUNCTION: Probable regulator of the NF-kappa-B and type I interferon signaling pathways. May also regulate the type II interferon signaling pathway. Plays a role in homeostatic control of innate immunity and in antiviral defense mechanisms. {ECO:0000269|PubMed:20434986}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with CHUK and IKBKB; prevents CHUK and IKBKB phosphorylation and inhibits their kinase activity. Interacts with DDX58 and IFIH1; blocks the interaction of MAVS to DDX58. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in spleen, thymus and lung. {ECO:0000269|PubMed:20434986}. +Q8VCB2 MED25_MOUSE Mediator of RNA polymerase II transcription subunit 25 (Mediator complex subunit 25) (mMED25) 745 78,113 Alternative sequence (4); Chain (1); Compositional bias (2); Modified residue (1); Motif (1); Region (5) FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. Required for RARA/RXRA-mediated transcription (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the Mediator complex, which is composed of MED1, MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L, MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23, MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8 subunits form a distinct module termed the CDK8 module. Mediator containing the CDK8 module is less active than Mediator lacking this module in supporting transcriptional activation. Individual preparations of the Mediator complex lacking one or more distinct subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and TRAP. Interacts with CREBBP. Interacts with ESR1, GR and THRB in a ligand-dependent fashion. Binds the Herpes simplex virus activator VP16 (By similarity). Interacts with RARA and RXRA in a ligand-dependent fashion. {ECO:0000250, ECO:0000269|PubMed:17641689}. +Q9CXU1 MED31_MOUSE Mediator of RNA polymerase II transcription subunit 31 (Mediator complex subunit 31) (Mediator complex subunit SOH1) 131 15,771 Chain (1); Compositional bias (1); Initiator methionine (1); Modified residue (1); Sequence conflict (1) FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Component of the Mediator complex, which is composed of MED1, MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L, MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23, MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8 subunits form a distinct module termed the CDK8 module. Mediator containing the CDK8 module is less active than Mediator lacking this module in supporting transcriptional activation. Individual preparations of the Mediator complex lacking one or more distinct subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and TRAP (By similarity). {ECO:0000250}. +Q921D4 MED6_MOUSE Mediator of RNA polymerase II transcription subunit 6 (Mediator complex subunit 6) 246 28,434 Chain (1); Cross-link (1); Erroneous initiation (1); Frameshift (1); Modified residue (2) FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the Mediator complex, which is composed of MED1, MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L, MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23, MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8 subunits form a distinct module termed the CDK8 module. Mediator containing the CDK8 module is less active than Mediator lacking this module in supporting transcriptional activation. Individual preparations of the Mediator complex lacking one or more distinct subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and TRAP. Interacts with CTNNB1 and GLI3 (By similarity). {ECO:0000250}. +Q61941 NNTM_MOUSE NAD(P) transhydrogenase, mitochondrial (EC 7.1.1.1) (Nicotinamide nucleotide transhydrogenase) (Pyridine nucleotide transhydrogenase) 1086 113,838 Chain (1); Modified residue (7); Nucleotide binding (5); Sequence conflict (3); Topological domain (4); Transit peptide (1); Transmembrane (14) TRANSMEM 475 493 Helical. {ECO:0000255}.; TRANSMEM 501 521 Helical. {ECO:0000255}.; TRANSMEM 527 546 Helical. {ECO:0000255}.; TRANSMEM 558 578 Helical. {ECO:0000255}.; TRANSMEM 596 616 Helical. {ECO:0000255}.; TRANSMEM 622 642 Helical. {ECO:0000255}.; TRANSMEM 646 666 Helical. {ECO:0000255}.; TRANSMEM 672 691 Helical. {ECO:0000255}.; TRANSMEM 702 722 Helical. {ECO:0000255}.; TRANSMEM 740 760 Helical. {ECO:0000255}.; TRANSMEM 778 797 Helical. {ECO:0000255}.; TRANSMEM 801 819 Helical. {ECO:0000255}.; TRANSMEM 833 853 Helical. {ECO:0000255}.; TRANSMEM 857 879 Helical. {ECO:0000255}. TOPO_DOM 44 474 Mitochondrial matrix.; TOPO_DOM 579 595 Mitochondrial matrix.; TOPO_DOM 723 739 Cytoplasmic.; TOPO_DOM 880 1086 Mitochondrial matrix. FUNCTION: The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane. May play a role in reactive oxygen species (ROS) detoxification in the adrenal gland (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}; Matrix side {ECO:0000305}. SUBUNIT: Homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed with expression most readily detectable in adrenal, heart, kidney, thyroid and adipose tissues. {ECO:0000269|PubMed:22634753}. +Q80T91 MEG11_MOUSE Multiple epidermal growth factor-like domains protein 11 (Multiple EGF-like domains protein 11) 1091 116,059 Alternative sequence (7); Chain (1); Compositional bias (1); Disulfide bond (47); Domain (16); Erroneous initiation (1); Glycosylation (2); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 848 868 Helical. {ECO:0000255}. TOPO_DOM 19 847 Extracellular. {ECO:0000255}.; TOPO_DOM 869 1091 Cytoplasmic. {ECO:0000255}. FUNCTION: May regulate the mosaic spacing of specific neuron subtypes in the retina through homotypic retinal neuron repulsion. Mosaics provide a mechanism to distribute each cell type evenly across the retina, ensuring that all parts of the visual field have access to a full set of processing elements. {ECO:0000269|PubMed:22407321}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Basolateral cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Forms an irregular, mosaic-like adhesion pattern in region of the cell that becomes firmely fixed to the substrate. Localized to protruding lamellipodia. Does not localize with MEGF10 (By similarity). {ECO:0000250}. SUBUNIT: Homopolymer. Does not interact with MEGF10. {ECO:0000250}. +P60882 MEGF8_MOUSE Multiple epidermal growth factor-like domains protein 8 (Multiple EGF-like domains protein 8) (Epidermal growth factor-like protein 4) (EGF-like protein 4) 2789 297,487 Chain (1); Compositional bias (3); Disulfide bond (32); Domain (18); Glycosylation (7); Modified residue (1); Repeat (12); Sequence caution (2); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 2592 2612 Helical. {ECO:0000255}. TOPO_DOM 28 2591 Extracellular. {ECO:0000255}.; TOPO_DOM 2613 2789 Cytoplasmic. {ECO:0000255}. FUNCTION: Acts as a negative regulator of hedgehog signaling (PubMed:29290584). {ECO:0000269|PubMed:29290584}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Highest expression in brain, testis and kidney. {ECO:0000269|PubMed:18821597}. +P46662 MERL_MOUSE Merlin (Moesin-ezrin-radixin-like protein) (Neurofibromin-2) (Schwannomin) 596 69,776 Alternative sequence (1); Beta strand (16); Chain (1); Compositional bias (1); Domain (1); Helix (12); Modified residue (2); Sequence conflict (4); Turn (5) FUNCTION: Probable regulator of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a pivotal role in tumor suppression by restricting proliferation and promoting apoptosis. Along with WWC1 can synergistically induce the phosphorylation of LATS1 and LATS2 and can probably function in the regulation of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway. May act as a membrane stabilizing protein. May inhibit PI3 kinase by binding to AGAP2 and impairing its stimulating activity. Suppresses cell proliferation and tumorigenesis by inhibiting the CUL4A-RBX1-DDB1-VprBP/DCAF1 E3 ubiquitin-protein ligase complex (By similarity). Plays a role in lens development and is required for complete fiber cell terminal differentiation, maintenance of cell polarity and separation of the lens vesicle from the corneal epithelium. {ECO:0000250|UniProtKB:P35240, ECO:0000269|PubMed:20181838}. PTM: Phosphorylation of Ser-518 inhibits nuclear localization by disrupting the intramolecular association of the FERM domain with the C-terminal tail. The dephosphorylation of Ser-518 favors the interaction with NOP53. {ECO:0000250|UniProtKB:P35240}.; PTM: Ubiquitinated by the CUL4A-RBX1-DDB1-DCAF1/VprBP E3 ubiquitin-protein ligase complex for ubiquitination and subsequent proteasome-dependent degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell projection {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Nucleus {ECO:0000250}. Note=Colocalizes with MPP1 in non-myelin-forming Schwann cells. Binds with DCAF1 in the nucleus. The intramolecular association of the FERM domain with the C-terminal tail promotes nuclear accumulation. The unphosphorylated form accumulates predominantly in the nucleus while the phosphorylated form is largely confined to the non-nuclear fractions (By similarity). {ECO:0000250}. SUBUNIT: Interacts with SLC9A3R1, HGS and AGAP2. Interacts with SGSM3. Interacts (via FERM domain) with MPP1 (By similarity). Interacts with LAYN (PubMed:15913605). Interacts with WWC1. Interacts with the CUL4A-RBX1-DDB1-VprBP/DCAF1 E3 ubiquitin-protein ligase complex. The unphosphorylated form interacts (via FERM domain) with VPRBP/DCAF1. Interacts (via FERM domain) with NOP53; the interaction is direct (By similarity). Interacts with SCHIP1; the interaction is direct (By similarity). {ECO:0000250|UniProtKB:P35240, ECO:0000269|PubMed:15913605}. +Q60805 MERTK_MOUSE Tyrosine-protein kinase Mer (EC 2.7.10.1) (Proto-oncogene c-Mer) (Receptor tyrosine kinase MerTK) 994 110,157 Active site (1); Binding site (1); Chain (1); Disulfide bond (2); Domain (5); Glycosylation (15); Modified residue (5); Mutagenesis (1); Nucleotide binding (1); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 498 518 Helical. {ECO:0000255}. TOPO_DOM 19 497 Extracellular. {ECO:0000255}.; TOPO_DOM 519 994 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to several ligands including LGALS3, TUB, TULP1 or GAS6. Regulates many physiological processes including cell survival, migration, differentiation, and phagocytosis of apoptotic cells (efferocytosis). Ligand binding at the cell surface induces autophosphorylation of MERTK on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with GRB2 or PLCG2 and induces phosphorylation of MAPK1, MAPK2, FAK/PTK2 or RAC1. MERTK signaling plays a role in various processes such as macrophage clearance of apoptotic cells, platelet aggregation, cytoskeleton reorganization and engulfment. Functions in the retinal pigment epithelium (RPE) as a regulator of rod outer segments fragments phagocytosis. Plays also an important role in inhibition of Toll-like receptors (TLRs)-mediated innate immune response by activating STAT1, which selectively induces production of suppressors of cytokine signaling SOCS1 and SOCS3. {ECO:0000269|PubMed:19117932, ECO:0000269|PubMed:20363878}. PTM: Autophosphorylated on Tyr-744, Tyr-748 and Tyr-749 in the activation loop allowing full activity (By similarity). Autophosphorylated on Tyr-867 leading to recruitment of downstream partners of the signaling cascade such as PLCG2. {ECO:0000250, ECO:0000269|PubMed:18039660}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Interacts (upon activation) with TNK2; stimulates TNK2 autophosphorylation. Interacts (via N-terminus) with extracellular ligands LGALS3, TUB, TULP1 and GAS6. Interacts with VAV1 in a phosphotyrosine-independent manner (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed predominantly in the hematopoietic lineages: macrophages, NK cells, NKT cells, dendritic cells and platelets. {ECO:0000269|PubMed:12884290}. +Q07646 MEST_MOUSE Mesoderm-specific transcript protein (EC 3.-.-.-) (Paternally-expressed gene 1 protein) 335 38,907 Alternative sequence (1); Chain (1); Domain (1); Glycosylation (1); Motif (1); Sequence conflict (2); Transmembrane (3) TRANSMEM 13 33 Helical. {ECO:0000255}.; TRANSMEM 63 83 Helical. {ECO:0000255}.; TRANSMEM 266 286 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18644838}; Multi-pass membrane protein {ECO:0000269|PubMed:18644838}. TISSUE SPECIFICITY: Expressed in mesodermal tissues. Isoform 1 is exclusively expressed from the paternal allele in all fetal tissues and cell lines examined, whereas isoform 2 is preferentially expressed from the paternal allele in a tissue-type-specific manner. {ECO:0000269|PubMed:7550314}. +Q9WU00 NRF1_MOUSE Nuclear respiratory factor 1 (NRF-1) (Alpha palindromic-binding protein) (Alpha-pal) 503 53,571 Alternative sequence (1); Chain (1); Compositional bias (2); Cross-link (1); DNA binding (1); Modified residue (5); Motif (1); Region (2); Sequence conflict (1) FUNCTION: Transcription factor that activates the expression of the EIF2S1 (EIF2-alpha) gene. Links the transcriptional modulation of key metabolic genes to cellular growth and development. Implicated in the control of nuclear genes required for respiration, heme biosynthesis, and mitochondrial DNA transcription and replication (By similarity). {ECO:0000250}. PTM: Phosphorylation enhances DNA binding. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Homodimer. Binds DNA as a dimer. Interacts with PPRC1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed in embryonic, fetal, and adult tissues. +Q9DCL4 MET15_MOUSE Probable methyltransferase-like protein 15 (EC 2.1.1.-) (Methyltransferase 5 domain-containing protein 1) 406 45,282 Binding site (4); Chain (1); Modified residue (1); Region (1); Sequence conflict (1) FUNCTION: Probable S-adenosyl-L-methionine-dependent methyltransferase. {ECO:0000250}. +Q8BSU7 MOB3A_MOUSE MOB kinase activator 3A (Mob1 homolog 2A) (Mps one binder kinase activator-like 2A) 217 25,552 Chain (1); Metal binding (4) FUNCTION: May regulate the activity of kinases. {ECO:0000250}. +Q8BJG4 MOB3C_MOUSE MOB kinase activator 3C (Mob1 homolog 2C) (Mps one binder kinase activator-like 2C) 216 25,521 Chain (1); Metal binding (4) FUNCTION: May regulate the activity of kinases. {ECO:0000250}. +Q3U095 NXPE2_MOUSE NXPE family member 2 (Protein FAM55B) 558 63,966 Chain (1); Sequence conflict (14); Transmembrane (1) TRANSMEM 17 37 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q8BM65 NYAP2_MOUSE Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 2 682 73,897 Alternative sequence (3); Chain (1); Compositional bias (2); Modified residue (5); Mutagenesis (2); Region (1); Sequence conflict (4) FUNCTION: Activates PI3K and concomitantly recruits the WAVE1 complex to the close vicinity of PI3K and regulates neuronal morphogenesis. {ECO:0000269|PubMed:21946561}. PTM: Phosphorylated on tyrosine residues by FYN upon stimulation with CNTN5. Phosphorylation begins at E16 and persists in adult brain. {ECO:0000269|PubMed:21946561}. SUBUNIT: Interacts with ACOT9, ARHGAP26 and PIK3R2. Interacts with components of the WAVE1 complex, CYFIP1 and NCKAP1; this interaction mediates PI3K-WAVE1 association and actin cytoskeleton remodeling. {ECO:0000269|PubMed:21946561}. TISSUE SPECIFICITY: Expressed predominantly in brain where it is present in the neurons, but not in astrocytes or oligodendrites. {ECO:0000269|PubMed:21946561}. +O35308 MOT3_MOUSE Monocarboxylate transporter 3 (MCT 3) (Proton-coupled monocarboxylate transporter 3) (Solute carrier family 16 member 8) 492 51,556 Chain (1); Topological domain (13); Transmembrane (12) TRANSMEM 15 35 Helical. {ECO:0000255}.; TRANSMEM 59 79 Helical. {ECO:0000255}.; TRANSMEM 86 106 Helical. {ECO:0000255}.; TRANSMEM 116 136 Helical. {ECO:0000255}.; TRANSMEM 147 167 Helical. {ECO:0000255}.; TRANSMEM 173 193 Helical. {ECO:0000255}.; TRANSMEM 229 249 Helical. {ECO:0000255}.; TRANSMEM 258 278 Helical. {ECO:0000255}.; TRANSMEM 294 314 Helical. {ECO:0000255}.; TRANSMEM 319 339 Helical. {ECO:0000255}.; TRANSMEM 353 373 Helical. {ECO:0000255}.; TRANSMEM 387 407 Helical. {ECO:0000255}. TOPO_DOM 1 14 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 36 58 Extracellular. {ECO:0000255}.; TOPO_DOM 80 85 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 107 115 Extracellular. {ECO:0000255}.; TOPO_DOM 137 146 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 168 172 Extracellular. {ECO:0000255}.; TOPO_DOM 194 228 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 250 257 Extracellular. {ECO:0000255}.; TOPO_DOM 279 293 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 315 318 Extracellular. {ECO:0000255}.; TOPO_DOM 340 352 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 374 386 Extracellular. {ECO:0000255}.; TOPO_DOM 408 492 Cytoplasmic. {ECO:0000255}. FUNCTION: Proton-linked monocarboxylate transporter. Catalyzes the rapid transport across the plasma membrane of many monocarboxylates such as lactate, pyruvate, branched-chain oxo acids derived from leucine, valine and isoleucine, and the ketone bodies acetoacetate, beta-hydroxybutyrate and acetate (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Retinal pigment epithelium. +Q9CQ74 LERL1_MOUSE Leptin receptor overlapping transcript-like 1 (Endospanin-2) 131 14,414 Chain (1); Transmembrane (4) TRANSMEM 7 27 Helical. {ECO:0000255}.; TRANSMEM 32 52 Helical. {ECO:0000255}.; TRANSMEM 69 89 Helical. {ECO:0000255}.; TRANSMEM 100 120 Helical. {ECO:0000255}. FUNCTION: Negatively regulates growth hormone (GH) receptor cell surface expression in liver. May play a role in liver resistance to GH during periods of reduced nutrient availability. {ECO:0000269|PubMed:19907080}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Interacts with RAB13. {ECO:0000250}. +P57785 LFTY2_MOUSE Left-right determination factor 2 (Left-right determination factor B) (Protein lefty-2) (Protein lefty-B) 368 41,175 Chain (1); Disulfide bond (4); Glycosylation (1); Propeptide (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Required for left-right asymmetry determination of organ systems in mammals. PTM: The processing of the protein may also occur at the second R-X-X-R site located at AA 132-135. Processing appears to be regulated in a cell-type specific manner. SUBCELLULAR LOCATION: Secreted. +Q8K4Z0 LGI2_MOUSE Leucine-rich repeat LGI family member 2 (Leucine-rich glioma-inactivated protein 2) 550 63,006 Alternative sequence (2); Chain (1); Domain (2); Erroneous initiation (1); Glycosylation (4); Repeat (9); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q8K1S1 LGI4_MOUSE Leucine-rich repeat LGI family member 4 (LGI1-like protein 3) (Leucine-rich glioma-inactivated protein 4) 537 59,377 Chain (1); Domain (1); Glycosylation (1); Repeat (11); Sequence conflict (1); Signal peptide (1) FUNCTION: Component of Schwann cell signaling pathway(s) that controls axon segregation and myelin formation. {ECO:0000269|PubMed:16341215}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. SUBUNIT: Can bind to ADAM11, ADAM22 and ADAM23. TISSUE SPECIFICITY: Expressed in the entire developing peripheral nerves. Strongly expressed in the trigeminal nerve and ganglion and particularly abundant in the boundary cap cells - a transient population of cells that contributes to the Schwann cell population of the dorsal root nerve. {ECO:0000269|PubMed:16341215}. DISEASE: Note=Defects in Lgi4 are the cause of the claw paw (clp) phenotype. Mice are characterized by limb posture abnormalities and peripheral hypomyelination, with no sign of dysmyelination in the CNS. {ECO:0000269|PubMed:16341215}. +A2ARI4 LGR4_MOUSE Leucine-rich repeat-containing G-protein coupled receptor 4 (G-protein coupled receptor 48) 951 104,150 Alternative sequence (1); Chain (1); Disulfide bond (6); Domain (1); Glycosylation (5); Modified residue (1); Mutagenesis (1); Repeat (15); Sequence conflict (4); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 545 565 Helical; Name=1. {ECO:0000255}.; TRANSMEM 576 596 Helical; Name=2. {ECO:0000255}.; TRANSMEM 620 640 Helical; Name=3. {ECO:0000255}.; TRANSMEM 662 682 Helical; Name=4. {ECO:0000255}.; TRANSMEM 704 724 Helical; Name=5. {ECO:0000255}.; TRANSMEM 757 777 Helical; Name=6. {ECO:0000255}.; TRANSMEM 784 804 Helical; Name=7. {ECO:0000255}. TOPO_DOM 25 544 Extracellular. {ECO:0000255}.; TOPO_DOM 566 575 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 597 619 Extracellular. {ECO:0000255}.; TOPO_DOM 641 661 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 683 703 Extracellular. {ECO:0000255}.; TOPO_DOM 725 756 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 778 783 Extracellular. {ECO:0000255}.; TOPO_DOM 805 951 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for R-spondins that potentiates the canonical Wnt signaling pathway and is involved in the formation of various organs. Upon binding to R-spondins (RSPO1, RSPO2, RSPO3 or RSPO4), associates with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increase expression of target genes. In contrast to classical G-protein coupled receptors, does not activate heterotrimeric G-proteins to transduce the signal. Its function as activator of the Wnt signaling pathway is required for the development of various organs, including liver, kidney, intestine, bone, reproductive tract and eye. May also act as a receptor for norrin (NDP), such results however require additional confirmation in vivo. Required during spermatogenesis to activate the Wnt signaling pathway in peritubular myoid cells. Required for the maintenance of intestinal stem cells and Paneth cell differentiation in postnatal intestinal crypts. Acts as a regulator of bone formation and remodeling. Involved in kidney development; required for maintaining the ureteric bud in an undifferentiated state. Involved in the development of the anterior segment of the eye. Required during erythropoiesis. Also acts as a negative regulator of innate immunity by inhibiting TLR2/TLR4 associated pattern-recognition and proinflammatory cytokine production. Plays an important role in regulating the circadian rhythms of plasma lipids, partially through regulating the rhythmic expression of MTTP (PubMed:24353284). {ECO:0000269|PubMed:18955481, ECO:0000269|PubMed:19605502, ECO:0000269|PubMed:21508962, ECO:0000269|PubMed:21693646, ECO:0000269|PubMed:21727895, ECO:0000269|PubMed:23393138, ECO:0000269|PubMed:23444378, ECO:0000269|PubMed:23533175, ECO:0000269|PubMed:23589304, ECO:0000269|PubMed:24353284}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21693646}; Multi-pass membrane protein {ECO:0000269|PubMed:21693646}. +Q9Z1P4 LGR5_MOUSE Leucine-rich repeat-containing G-protein coupled receptor 5 (G-protein coupled receptor 49) (Orphan G-protein coupled receptor FEX) 907 99,666 Chain (1); Disulfide bond (5); Domain (1); Glycosylation (4); Repeat (16); Sequence conflict (3); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 562 582 Helical; Name=1. {ECO:0000255}.; TRANSMEM 594 614 Helical; Name=2. {ECO:0000255}.; TRANSMEM 639 659 Helical; Name=3. {ECO:0000255}.; TRANSMEM 683 703 Helical; Name=4. {ECO:0000255}.; TRANSMEM 724 744 Helical; Name=5. {ECO:0000255}.; TRANSMEM 768 788 Helical; Name=6. {ECO:0000255}.; TRANSMEM 803 823 Helical; Name=7. {ECO:0000255}. TOPO_DOM 22 561 Extracellular. {ECO:0000255}.; TOPO_DOM 583 593 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 615 638 Extracellular. {ECO:0000255}.; TOPO_DOM 660 682 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 704 723 Extracellular. {ECO:0000255}.; TOPO_DOM 745 767 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 789 802 Extracellular. {ECO:0000255}.; TOPO_DOM 824 907 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for R-spondins that potentiates the canonical Wnt signaling pathway and acts as a stem cell marker of the intestinal epithelium and the hair follicle. Upon binding to R-spondins (RSPO1, RSPO2, RSPO3 or RSPO4), associates with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increase expression of target genes. In contrast to classical G-protein coupled receptors, does not activate heterotrimeric G-proteins to transduce the signal. Involved in the development and/or maintenance of the adult intestinal stem cells during postembryonic development. {ECO:0000269|PubMed:21727895}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Rapidly and constitutively internalized to the trans-Golgi network at steady state. {ECO:0000250}. SUBUNIT: Identified in a complex composed of RNF43, LGR5 and RSPO1 (By similarity). Also interacts with other R-spondin ligands, including RSPO2, RSPO3 and RSPO4 (By similarity). {ECO:0000250|UniProtKB:O75473}. TISSUE SPECIFICITY: Expressed in the gonads, the adrenal gland, and in the brain. In the central nervous system expression is restricted to the olfactory bulb. In the adrenal gland detected only in the neural-crest derived chromaffin cells of the medulla, but not in the cells of the adrenal cortex. In the gonads, the expression is high in Graafian follicle, but absent from primary and secondary follicles. In the intestine, exclusively expressed in cycling crypt base columnar cells. Expressed in the lower bulge and secondary germ area of telogen hair follicles and in the lower outer root sheath of anagen hair follicle. {ECO:0000269|PubMed:17934449, ECO:0000269|PubMed:18849992, ECO:0000269|PubMed:9920770}. +Q8BM86 LHPL6_MOUSE LHFPL tetraspan subfamily member 6 protein (Lipoma HMGIC fusion partner) 200 21,626 Chain (1); Sequence conflict (1); Signal peptide (1); Transmembrane (3) TRANSMEM 84 104 Helical. {ECO:0000255}.; TRANSMEM 123 143 Helical. {ECO:0000255}.; TRANSMEM 166 186 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9D7I5 LHPP_MOUSE Phospholysine phosphohistidine inorganic pyrophosphate phosphatase (EC 3.1.3.-) (EC 3.6.1.1) 270 29,144 Alternative sequence (2); Binding site (1); Chain (1); Metal binding (3); Region (2) FUNCTION: Phosphatase that hydrolyzes imidodiphosphate, 3-phosphohistidine and 6-phospholysine. Has broad substrate specificity and can also hydrolyze inorganic diphosphate, but with lower efficiency (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +Q3U3R4 LMF1_MOUSE Lipase maturation factor 1 (Transmembrane protein 112) 574 65,878 Alternative sequence (4); Chain (1); Sequence conflict (1); Topological domain (6); Transmembrane (5) TRANSMEM 50 72 Helical. {ECO:0000255}.; TRANSMEM 128 151 Helical. {ECO:0000255}.; TRANSMEM 208 221 Helical. {ECO:0000255}.; TRANSMEM 293 321 Helical. {ECO:0000255}.; TRANSMEM 368 388 Helical. {ECO:0000255}. TOPO_DOM 1 49 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 73 127 Lumenal. {ECO:0000255}.; TOPO_DOM 152 207 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 222 292 Lumenal. {ECO:0000255}.; TOPO_DOM 322 367 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 389 574 Lumenal. {ECO:0000255}. FUNCTION: Involved in the maturation of specific proteins in the endoplasmic reticulum. Required for maturation and transport of active lipoprotein lipase (LPL) through the secretory pathway. Each LMF1 molecule chaperones 50 or more molecules of LPL. {ECO:0000250|UniProtKB:Q96S06, ECO:0000269|PubMed:17994020}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:17994020, ECO:0000269|PubMed:19783858}; Multi-pass membrane protein {ECO:0000269|PubMed:17994020, ECO:0000269|PubMed:19783858}. SUBUNIT: Interacts with LPL and SEL1L. {ECO:0000269|PubMed:25066055}. TISSUE SPECIFICITY: Expressed in all tissues synthesizing lipoprotein lipase (Lpl) and hepatic lipase (Lipc), including adipose tissue, skeletal muscle, heart, and liver. Expressed at higher levels in tissues that express little or no lipase activity such as testis and pancreas suggesting additional functions in these tissues. {ECO:0000269|PubMed:17994020}. DISEASE: Note=Defects in Lmf1 are the cause of combined lipase deficiency (cld). Cld is characterized by severe hypertriglyceridemia with accumulation of chylomicrons that gradually pack the lumina of capillaries and sinusoids. Severe hypertriglyceridemia causes an increase in blood viscosity, ischemia, and cyanosis, and the inability of tissues to access circulating triglycerides results in starvation, poor thermoregulation, and death 2 to 3 days after birth. The disorder is caused by a decrease in the activity of lipoprotein lipase (Lpl) and the related hepatic lipase (Lipc), caused by impaired maturation of nascent Lpl and hepatic lipase polypeptides in the endoplasmic reticulum. +O88609 LMX1B_MOUSE LIM homeobox transcription factor 1-beta (LIM/homeobox protein 1.2) (LMX-1.2) (LIM/homeobox protein LMX1B) 395 44,102 Chain (1); Compositional bias (1); DNA binding (1); Domain (2); Erroneous initiation (5); Sequence conflict (1) FUNCTION: Essential for the specification of dorsal limb fate at both the zeugopodal and autopodal levels. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. SUBUNIT: Interacts with DHX9. {ECO:0000250|UniProtKB:O60663}. +Q8BZL8 LMO3_MOUSE LIM domain only protein 3 (LMO-3) (Neuronal-specific transcription factor DAT1) 145 16,594 Chain (1); Domain (2) +Q8BVA4 LMOD1_MOUSE Leiomodin-1 595 66,310 Chain (1); Domain (1); Modified residue (4); Region (2); Repeat (8) FUNCTION: Mediates nucleation of actin filaments. {ECO:0000250|UniProtKB:P29536}. SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere {ECO:0000250|UniProtKB:A0A0G2K0D3}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:A0A0G2K0D3}. Note=Colocalizes with actin filaments in sarcomeres. {ECO:0000250|UniProtKB:A0A0G2K0D3}. TISSUE SPECIFICITY: Detected in aorta, urinary bladder and uterus (at protein level). Detected in smooth muscle cells. Detected in aorta, bladder, colon, intestine, stomach and uterus. {ECO:0000269|PubMed:22157009}. +P11260 LORF1_MOUSE LINE-1 retrotransposable element ORF1 protein (L1-ORF1p) (LINE retrotransposable element 1) (LINE1 retrotransposable element 1) (Transposase element L1Md-A101/L1Md-A102/L1Md-A2) 357 41,226 Beta strand (3); Chain (1); Coiled coil (1); Helix (3); Region (2); Turn (3) FUNCTION: Nucleic acid-binding protein which is essential for retrotransposition of LINE-1 elements in the genome. Functions as a nucleic acid chaperone binding its own transcript and therefore preferentially mobilizing the transcript from which they are encoded. {ECO:0000269|PubMed:11134335, ECO:0000269|PubMed:28806172}. PTM: Polyubiquitinated, probably by UBR2, which induces its degradation. {ECO:0000269|PubMed:28806172}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9UN81}. Cytoplasm {ECO:0000269|PubMed:28806172}. Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000250|UniProtKB:Q9UN81}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q9UN81}. Note=Colocalizes with its encoding RNA in cytoplasmic ribonucleoprotein particle. Mainly cytoplasmic, rarely detected in the nucleus, possibly within the nucleolus. {ECO:0000250|UniProtKB:Q9UN81}. SUBUNIT: Homotrimer (via coiled coil domain). May also form larger homooligomers. Interacst with Tex19.1 and UBR2 (PubMed:28806172). Interacts with MOV10 (PubMed:28662698). {ECO:0000269|PubMed:14615577, ECO:0000269|PubMed:28662698, ECO:0000269|PubMed:28806172}. DOMAIN: The coiled coil domain mediates homotrimerization. {ECO:0000250}.; DOMAIN: The RRM and the CTD domain are both required for proper RNA-binding activity. TISSUE SPECIFICITY: Expressed in meiotic spermatocytes and in the cerebellum (at protein level). {ECO:0000269|PubMed:28806172}. +P39655 LOX12_MOUSE Arachidonate 12-lipoxygenase, 12S-type (12S-LOX) (12S-lipoxygenase) (EC 1.13.11.31) (Lipoxin synthase 12-LO) (EC 3.3.2.-) (Platelet-type lipoxygenase 12) (P-12LO) 663 75,390 Chain (1); Domain (2); Metal binding (5); Modified residue (1); Mutagenesis (3); Sequence conflict (5) Lipid metabolism; hydroperoxy eicosatetraenoic acid biosynthesis. FUNCTION: Non-heme iron-containing dioxygenase that catalyzes the stereo-specific peroxidation of free and esterified polyunsaturated fatty acids generating a spectrum of bioactive lipid mediators. Mainly converts arachidonic acid to (12S)-hydroperoxyeicosatetraenoic acid/(12S)-HPETE but can also metabolize linoleic acid. Has a dual activity since it also converts leukotriene A4/LTA4 into both the bioactive lipoxin A4/LXA4 and lipoxin B4/LXB4. Through the production of specific bioactive lipids like (12S)-HPETE it regulates different biological processes including platelet activation. It also probably positively regulates angiogenesis through regulation of the expression of the vascular endothelial growth factor. Plays a role in apoptotic process, promoting the survival of vascular smooth muscle cells for instance. May also play a role in the control of cell migration and proliferation. {ECO:0000269|PubMed:9501222}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:7868854}. Membrane {ECO:0000250}. Note=Membrane association is stimulated by EGF. {ECO:0000250}. TISSUE SPECIFICITY: Found primarily in platelets and in microsomal and cytosolic fractions of the epidermis (at protein level). {ECO:0000269|PubMed:10383730, ECO:0000269|PubMed:8188678, ECO:0000269|PubMed:9501222}. +Q149R9 LPAR5_MOUSE Lysophosphatidic acid receptor 5 (LPA receptor 5) (LPA-5) (G-protein coupled receptor 92) 372 41,394 Chain (1); Disulfide bond (1); Glycosylation (4); Sequence conflict (2); Topological domain (8); Transmembrane (7) TRANSMEM 31 51 Helical; Name=1. {ECO:0000255}.; TRANSMEM 60 80 Helical; Name=2. {ECO:0000255}.; TRANSMEM 101 121 Helical; Name=3. {ECO:0000255}.; TRANSMEM 141 161 Helical; Name=4. {ECO:0000255}.; TRANSMEM 192 212 Helical; Name=5. {ECO:0000255}.; TRANSMEM 244 264 Helical; Name=6. {ECO:0000255}.; TRANSMEM 281 301 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 30 Extracellular. {ECO:0000255}.; TOPO_DOM 52 59 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 81 100 Extracellular. {ECO:0000255}.; TOPO_DOM 122 140 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 162 191 Extracellular. {ECO:0000255}.; TOPO_DOM 213 243 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 265 280 Extracellular. {ECO:0000255}.; TOPO_DOM 302 372 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for lysophosphatidic acid (LPA), a mediator of diverse cellular activities. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q99PI5 LPIN2_MOUSE Phosphatidate phosphatase LPIN2 (EC 3.1.3.4) (Lipin-2) 893 99,613 Alternative sequence (2); Chain (1); Modified residue (7); Motif (3); Mutagenesis (2); Region (2); Sequence conflict (1) FUNCTION: Plays important roles in controlling the metabolism of fatty acids at different levels. Acts as a magnesium-dependent phosphatidate phosphatase enzyme which catalyzes the conversion of phosphatidic acid to diacylglycerol during triglyceride, phosphatidylcholine and phosphatidylethanolamine biosynthesis in the reticulum endoplasmic membrane. Acts also as a nuclear transcriptional coactivator for PPARGC1A to modulate lipid metabolism. {ECO:0000269|PubMed:19136718, ECO:0000269|PubMed:19717560}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytosol. Endoplasmic reticulum membrane. Note=Translocates from cytosol to endoplasmic reticulum membrane with increasing levels of oleate. DOMAIN: Contains 1 Asp-Xaa-Asp-Xaa-Thr (DXDXT) motif, a catalytic motif known to be essential for phosphatidate phosphatase activity. {ECO:0000250}.; DOMAIN: Contains one Leu-Xaa-Xaa-Ile-Leu (LXXIL) motif, a motif known to be a transcriptional binding motif. {ECO:0000250}. TISSUE SPECIFICITY: Expressed at high level in liver and to some extend in lung, kidney, placenta, spleen, thymus, lymph node, prostate, testes, small intestine, and colon. Expressed also in circulating red blood cells and site of lymphopoiesis. {ECO:0000269|PubMed:17158099, ECO:0000269|PubMed:19717560}. +Q6DVA0 LEMD2_MOUSE LEM domain-containing protein 2 (Nuclear envelope transmembrane protein 25) (NET25) 511 57,507 Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (1); Frameshift (1); Initiator methionine (1); Modified residue (4); Region (1); Sequence conflict (1); Transmembrane (2) TRANSMEM 221 241 Helical. {ECO:0000255}.; TRANSMEM 385 405 Helical. {ECO:0000255}. FUNCTION: Involved in nuclear structure organization (PubMed:16339967). Required for maintaining the integrity of the nuclear envelope (By similarity). {ECO:0000250|UniProtKB:Q8NC56, ECO:0000269|PubMed:16339967}.; FUNCTION: Required for embryonic development and is involved in regulation of several signaling pathways such as MAPK and AKT (PubMed:25790465). Required for myoblast differentiation involving regulation of ERK signaling (PubMed:17062158, PubMed:19720741). {ECO:0000269|PubMed:17062158, ECO:0000269|PubMed:19720741, ECO:0000269|PubMed:25790465}. SUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000269|PubMed:16339967, ECO:0000269|PubMed:17062158}; Multi-pass membrane protein {ECO:0000269|PubMed:16339967}. Note=Lamina-associated protein residing in the inner nuclear membrane (INM). Localized exclusively to the nuclear envelope, giving rise to a typical rim-like staining of the nuclear periphery. SUBUNIT: Binds to the lamin tail, in vitro. {ECO:0000269|PubMed:16339967}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:16339967}. +Q8K406 LGI3_MOUSE Leucine-rich repeat LGI family member 3 (Leubrin) (Leucine-rich glioma-inactivated protein 3) 548 61,818 Chain (1); Domain (2); Glycosylation (2); Repeat (10); Signal peptide (1) FUNCTION: May participate in the regulation of neuronal exocytosis. {ECO:0000269|PubMed:18760330}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000269|PubMed:18760330}. Cell junction, synapse, synaptosome {ECO:0000269|PubMed:18760330}. Note=Found in the synaptosomal membrane fraction. SUBUNIT: Interacts with STX1A. {ECO:0000269|PubMed:18760330}. +O89017 LGMN_MOUSE Legumain (EC 3.4.22.34) (Asparaginyl endopeptidase) (Protease, cysteine 1) 435 49,373 Active site (2); Beta strand (12); Chain (1); Disulfide bond (2); Glycosylation (4); Helix (20); Mutagenesis (9); Propeptide (1); Signal peptide (1); Site (1); Turn (3) FUNCTION: Has a strict specificity for hydrolysis of asparaginyl bonds. Can also cleave aspartyl bonds slowly, especially under acidic conditions. May be involved in the processing of proteins for MHC class II antigen presentation in the lysosomal/endosomal system. Required for normal lysosomal protein degradation in renal proximal tubules. Required for normal degradation of internalized EGFR. Plays a role in the regulation of cell proliferation via its role in EGFR degradation. {ECO:0000269|PubMed:17350006, ECO:0000269|PubMed:21292981, ECO:0000269|PubMed:24407422, ECO:0000269|PubMed:9742219}. PTM: Glycosylated. {ECO:0000305|PubMed:24407422}.; PTM: Activated by autocatalytic processing at pH 4. SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:21292981, ECO:0000269|PubMed:9742219}. SUBUNIT: May interact with integrins (By similarity). Monomer after autocatalytic processing. Homodimer before autocatalytic removal of the propeptide. {ECO:0000250, ECO:0000269|PubMed:24407422}. DOMAIN: In the zymogen form, the uncleaved propeptide blocks access to the active site. {ECO:0000250}. TISSUE SPECIFICITY: Detected in kidney proximal tubules (at protein level). Ubiquitous. Particularly abundant in kidney and placenta. {ECO:0000269|PubMed:21292981, ECO:0000269|PubMed:9742219}. +P53776 LHX4_MOUSE LIM/homeobox protein Lhx4 (LIM homeobox protein 4) 390 43,078 Beta strand (8); Chain (1); DNA binding (1); Domain (2); Erroneous initiation (1); Helix (3); Region (2); Sequence conflict (1); Turn (5) FUNCTION: May play a critical role in the development of respiratory control mechanisms and in the normal growth and maturation of the lung. Binds preferentially to methylated DNA (By similarity). {ECO:0000250|UniProtKB:Q969G2}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. TISSUE SPECIFICITY: Transient expression in ventrolateral regions of the developing neural tube and hindbrain. +Q9D945 LLPH_MOUSE Protein LLP homolog (Protein LAPS18-like) 130 15,391 Alternative sequence (1); Chain (1); Coiled coil (1); Cross-link (1) FUNCTION: In hippocampal neurons, regulates dendritic and spine growth and synaptic transmission. {ECO:0000269|PubMed:26961175}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:26961175}. Chromosome {ECO:0000250|UniProtKB:Q9BRT6}. Note=Cell-permeable protein. 22 hours after injection in the hippocampal area CA1, internalized by most cells at the injection site (PubMed:26961175). Localizes at the chromosome periphery during mitosis (By similarity). {ECO:0000250|UniProtKB:Q9BRT6, ECO:0000269|PubMed:26961175}. SUBUNIT: Interacts with CTCF, MYO1C and with the transcriptional machinery, including RNA polymerase II and TBP. {ECO:0000269|PubMed:26961175}. TISSUE SPECIFICITY: Widely expressed, with high levels in testis and spleen and low levels in heart. In the brain, expressed in the cortex and hippocampus, and at very low levels in the cerebellum. {ECO:0000269|PubMed:26961175}. +Q8K3Y3 LN28A_MOUSE Protein lin-28 homolog A (Lin-28A) (Testis-expressed protein 17) 209 22,720 Beta strand (6); Chain (1); Domain (1); Helix (4); Initiator methionine (1); Modified residue (4); Mutagenesis (10); Region (1); Sequence conflict (1); Turn (5); Zinc finger (2) FUNCTION: RNA-binding protein that inhibits processing of pre-let-7 miRNAs and regulates translation of mRNAs that control developmental timing, pluripotency and metabolism (PubMed:17473174, PubMed:18604195, PubMed:18566191, PubMed:18292307, PubMed:19703396, PubMed:23102813, PubMed:24209617). Seems to recognize a common structural G-quartet (G4) feature in its miRNA and mRNA targets (PubMed:26045559). 'Translational enhancer' that drives specific mRNAs to polysomes and increases the efficiency of protein synthesis. Its association with the translational machinery and target mRNAs results in an increased number of initiation events per molecule of mRNA and, indirectly, in mRNA stabilization. Binds IGF2 mRNA, MYOD1 mRNA, ARBP/36B4 ribosomal protein mRNA and its own mRNA. Essential for skeletal muscle differentiation program through the translational up-regulation of IGF2 expression (PubMed:17473174). Suppressor of microRNA (miRNA) biogenesis, including that of let-7, miR107, miR-143 and miR-200c. Specifically binds the miRNA precursors (pre-miRNAs), recognizing an 5'-GGAG-3' motif found in pre-miRNA terminal loop, and recruits TUT4 and TUT7 uridylyltransferaseS. This results in the terminal uridylation of target pre-miRNAs. Uridylated pre-miRNAs fail to be processed by Dicer and undergo degradation. The repression of let-7 expression is required for normal development and contributes to maintain the pluripotent state by preventing let-7-mediated differentiation of embryonic stem cells (PubMed:19703396, PubMed:28671666). Localized to the periendoplasmic reticulum area, binds to a large number of spliced mRNAs and inhibits the translation of mRNAs destined for the ER, reducing the synthesis of transmembrane proteins, ER or Golgi lumen proteins, and secretory proteins (PubMed:23102813). Binds to and enhances the translation of mRNAs for several metabolic enzymes, such as PFKP, PDHA1 or SDHA, increasing glycolysis and oxidative phosphorylation. Which, with the let-7 repression may enhance tissue repair in adult tissue (PubMed:24209617). {ECO:0000269|PubMed:17473174, ECO:0000269|PubMed:18292307, ECO:0000269|PubMed:18566191, ECO:0000269|PubMed:18604195, ECO:0000269|PubMed:19703396, ECO:0000269|PubMed:23102813, ECO:0000269|PubMed:24209617, ECO:0000269|PubMed:26045559, ECO:0000269|PubMed:28671666}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12798299, ECO:0000269|PubMed:17473174}. Rough endoplasmic reticulum {ECO:0000269|PubMed:23102813}. Cytoplasm, P-body {ECO:0000250|UniProtKB:Q9H9Z2}. Cytoplasm, Stress granule {ECO:0000269|PubMed:17473174}. Nucleus, nucleolus {ECO:0000269|PubMed:17473174}. Note=Predominantly cytoplasmic (PubMed:12798299). In the cytoplasm, localizes to peri-endoplasmic reticulum regions and detected in the microsomal fraction derived from rough endoplasmic reticulum (RER) following subcellular fractionation. May be bound to the cytosolic surface of RER on which ER-associated mRNAs are translated (PubMed:23102813). Shuttle from the nucleus to the cytoplasm requires RNA-binding (PubMed:17473174). Nucleolar localization observed in 10-15% of the nuclei in differentiated myotubes (PubMed:17473174). {ECO:0000269|PubMed:12798299, ECO:0000269|PubMed:17473174, ECO:0000269|PubMed:23102813}. SUBUNIT: Monomer (PubMed:22078496). During skeletal muscle differentiation, associated with translation initiation complexes in the polysomal compartment (By similarity). Directly interacts with EIF3S2 (PubMed:17473174). Interacts with NCL in an RNA-dependent manner (By similarity). Interacts with TUT4 in the presence of pre-let-7 RNA (PubMed:28671666). {ECO:0000250, ECO:0000250|UniProtKB:Q9H9Z2, ECO:0000269|PubMed:17473174, ECO:0000269|PubMed:22078496, ECO:0000269|PubMed:28671666}. DOMAIN: The CSD domain is required for function in muscle differentiation. {ECO:0000269|PubMed:22078496}.; DOMAIN: The CCHC zinc fingers interact with the GGAG motif at the 3' end of let-7 miRNAs precursors, more generally they bind the 5'-NGNNG-3' consensus motif with micromolar affinity. The CSD domain recognizes the loop at the 5' end. The flexible linker allows accommodating variable sequences and lengths among let-7 family members. {ECO:0000269|PubMed:22078496, ECO:0000269|PubMed:28671666}. TISSUE SPECIFICITY: Expressed in embryonic stem cells (ES cells), spermatagonia and testis. Expressed in numerous epithelial tissues including the epithelia of the small intestine, the intralobular duct epithelium of the mammary gland and the epithelia of Henle's loop in the kidney and in the collecting duct (at protein level). Also expressed in the myocardium and skeletal muscle (at protein level). {ECO:0000269|PubMed:11279525, ECO:0000269|PubMed:12798299, ECO:0000269|PubMed:14643679, ECO:0000269|PubMed:15722555}. +Q45KJ6 LN28B_MOUSE Protein lin-28 homolog B (Lin-28B) 247 26,903 Alternative sequence (7); Chain (1); Domain (1); Metal binding (8); Modified residue (3); Zinc finger (2) FUNCTION: Suppressor of microRNA (miRNA) biogenesis, including that of let-7 and possibly of miR107, miR-143 and miR-200c. Binds primary let-7 transcripts (pri-let-7), including pri-let-7g and pri-let-7a-1, and sequester them in the nucleolus, away from the microprocessor complex, hence preventing their processing into mature miRNA. Does not act on pri-miR21. The repression of let-7 expression is required for normal development and contributes to maintain the pluripotent state of embryonic stem cells by preventing let-7-mediated differentiation. When overexpressed, recruits ZCCHC11/TUT4 uridylyltransferase to pre-let-7 transcripts, leading to their terminal uridylation and degradation. This activity might not be relevant in vivo, as LIN28B-mediated inhibition of let-7 miRNA maturation appears to be ZCCHC11-independent. Interaction with target pre-miRNAs occurs via an 5'-GGAG-3' motif in the pre-miRNA terminal loop (By similarity). Mediates MYC-induced let-7 repression (PubMed:19211792). When overexpressed, may stimulate growth of carcinoma cell lines (By similarity). {ECO:0000250|UniProtKB:Q6ZN17, ECO:0000269|PubMed:19211792}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q6ZN17}. DOMAIN: The tandem zinc fingers, also referred as zinc knuckle domain (ZKD), mediate specific binding to the GGAG/GGUG motif while the CSD shows only limited pyrimidine-rich sequence specificity. Both domains bind single-stranded nucleic acids (By similarity). {ECO:0000250}. +P13542 MYH8_MOUSE Myosin-8 (Myosin heavy chain 8) (Myosin heavy chain, skeletal muscle, perinatal) (MyHC-perinatal) 1937 222,708 Chain (1); Coiled coil (1); Domain (3); Modified residue (32); Nucleotide binding (1); Region (2) FUNCTION: Muscle contraction. SUBCELLULAR LOCATION: Cytoplasm, myofibril. Note=Thick filaments of the myofibrils. SUBUNIT: Muscle myosin is a hexameric protein that consists of 2 heavy chain subunits (MHC), 2 alkali light chain subunits (MLC) and 2 regulatory light chain subunits (MLC-2). DOMAIN: The rodlike tail sequence is highly repetitive, showing cycles of a 28-residue repeat pattern composed of 4 heptapeptides, characteristic for alpha-helical coiled coils.; DOMAIN: Limited proteolysis of myosin heavy chain produces 1 light meromyosin (LMM) and 1 heavy meromyosin (HMM). HMM can be further cleaved into 2 globular subfragments (S1) and 1 rod-shaped subfragment (S2). {ECO:0000305}. +D3YY23 LONF1_MOUSE LON peptidase N-terminal domain and RING finger protein 1 762 85,106 Chain (1); Domain (1); Modified residue (1); Repeat (4); Zinc finger (2) +Q9D7F2 LPD6B_MOUSE Ly6/PLAUR domain-containing protein 6B 191 21,762 Alternative sequence (1); Chain (1); Disulfide bond (5); Domain (1); Lipidation (1); Propeptide (1); Signal peptide (1) FUNCTION: Believed to act as a modulator of nicotinic acetylcholine receptors (nAChRs) activity. In vitro acts on nAChRs in a subtype- and stoichiometry-dependent manner. Modulates specifically alpha-3(3):beta-4(2) nAChRs by enhancing the sensitivity to ACh, decreasing ACh-induced maximal current response and increasing the rate of desensitization to ACh; has no effect on alpha-7 homomeric nAChRs. {ECO:0000250|UniProtKB:Q8NI32}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}. +P61793 LPAR1_MOUSE Lysophosphatidic acid receptor 1 (LPA receptor 1) (LPA-1) (Lysophosphatidic acid receptor Edg-2) (Rec1.3) (VZG-1) 364 41,119 Alternative sequence (1); Binding site (2); Chain (1); Disulfide bond (3); Glycosylation (2); Modified residue (2); Region (1); Sequence conflict (5); Topological domain (8); Transmembrane (7) TRANSMEM 51 75 Helical; Name=1. {ECO:0000250|UniProtKB:Q92633}.; TRANSMEM 84 107 Helical; Name=2. {ECO:0000250|UniProtKB:Q92633}.; TRANSMEM 122 144 Helical; Name=3. {ECO:0000250|UniProtKB:Q92633}.; TRANSMEM 164 184 Helical; Name=4. {ECO:0000250|UniProtKB:Q92633}.; TRANSMEM 205 225 Helical; Name=5. {ECO:0000250|UniProtKB:Q92633}.; TRANSMEM 256 280 Helical; Name=6. {ECO:0000250|UniProtKB:Q92633}.; TRANSMEM 295 315 Helical; Name=7. {ECO:0000250|UniProtKB:Q92633}. TOPO_DOM 1 50 Extracellular. {ECO:0000250|UniProtKB:Q92633}.; TOPO_DOM 76 83 Cytoplasmic. {ECO:0000250|UniProtKB:Q92633}.; TOPO_DOM 108 121 Extracellular. {ECO:0000250|UniProtKB:Q92633}.; TOPO_DOM 145 163 Cytoplasmic. {ECO:0000250|UniProtKB:Q92633}.; TOPO_DOM 185 204 Extracellular. {ECO:0000250|UniProtKB:Q92633}.; TOPO_DOM 226 255 Cytoplasmic. {ECO:0000250|UniProtKB:Q92633}.; TOPO_DOM 281 294 Extracellular. {ECO:0000250|UniProtKB:Q92633}.; TOPO_DOM 316 364 Cytoplasmic. {ECO:0000250|UniProtKB:Q92633}. FUNCTION: Receptor for lysophosphatidic acid (LPA) (PubMed:11087877, PubMed:18066075). Plays a role in the reorganization of the actin cytoskeleton, cell migration, differentiation and proliferation, and thereby contributes to the responses to tissue damage and infectious agents. Activates downstream signaling cascades via the G(i)/G(o), G(12)/G(13), and G(q) families of heteromeric G proteins (PubMed:8922387, PubMed:9600933, PubMed:11040035, PubMed:18157949, PubMed:18066075, PubMed:23478264). Signaling inhibits adenylyl cyclase activity and decreases cellular cAMP levels (PubMed:11040035, PubMed:12215548). Signaling triggers an increase of cytoplasmic Ca(2+) levels (PubMed:12215548). Activates RALA; this leads to the activation of phospholipase C (PLC) and the formation of inositol 1,4,5-trisphosphate (PubMed:11040035, PubMed:12215548, PubMed:23478264). Signaling mediates activation of down-stream MAP kinases (PubMed:11040035). Contributes to the regulation of cell shape (PubMed:8922387, PubMed:9600933, PubMed:11040035, PubMed:11087877). Promotes Rho-dependent reorganization of the actin cytoskeleton in neuronal cells and neurite retraction (PubMed:9600933, PubMed:11040035, PubMed:12181339). Promotes the activation of Rho and the formation of actin stress fibers (PubMed:9600933, PubMed:12215548). Promotes formation of lamellipodia at the leading edge of migrating cells via activation of RAC1 (PubMed:23478264). Through its function as lysophosphatidic acid receptor, plays a role in chemotaxis and cell migration, including responses to injury and wounding (PubMed:11087877, PubMed:18066075, PubMed:23478264). Plays a role in triggering inflammation in response to bacterial lipopolysaccharide (LPS) via its interaction with CD14 (PubMed:21821728). Promotes cell proliferation in response to lysophosphatidic acid (PubMed:9600933, PubMed:11087877, PubMed:12215548, PubMed:18157949, PubMed:17692995, PubMed:23478264). Required for normal skeleton development (PubMed:21569876). May play a role in osteoblast differentiation (PubMed:21569876). Required for normal brain development (PubMed:17656621, PubMed:18708146). Required for normal proliferation, survival and maturation of newly formed neurons in the adult dentate gyrus (PubMed:18708146). Plays a role in pain perception and in the initiation of neuropathic pain (PubMed:15195086, PubMed:19689455). {ECO:0000269|PubMed:11040035, ECO:0000269|PubMed:11087877, ECO:0000269|PubMed:12181339, ECO:0000269|PubMed:12215548, ECO:0000269|PubMed:15195086, ECO:0000269|PubMed:17656621, ECO:0000269|PubMed:17692995, ECO:0000269|PubMed:18066075, ECO:0000269|PubMed:18157949, ECO:0000269|PubMed:18708146, ECO:0000269|PubMed:19689455, ECO:0000269|PubMed:21569876, ECO:0000269|PubMed:23478264, ECO:0000269|PubMed:8922387, ECO:0000269|PubMed:9600933}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q92633}. SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:8922387}. Cell membrane {ECO:0000269|PubMed:18157949, ECO:0000269|PubMed:21821728, ECO:0000269|PubMed:9600933, ECO:0000305|PubMed:8922387}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q92633}. Endosome {ECO:0000250|UniProtKB:Q92633, ECO:0000305|PubMed:18157949}. Note=Prior to LPA treatment found predominantly at the cell surface. Internalized after LPA treatment (PubMed:18157949). Colocalizes with RALA in endocytic vesicles after LPA treatment. {ECO:0000250|UniProtKB:Q92633, ECO:0000269|PubMed:18157949}. SUBUNIT: Interacts with RALA and GRK2 (By similarity). Interacts with GNAQ and GNA13 (PubMed:23478264). Interacts with CD14; the interaction is enhanced by exposure to bacterial lipopolysaccharide (LPS) (PubMed:21821728). {ECO:0000250|UniProtKB:Q92633, ECO:0000269|PubMed:21821728, ECO:0000269|PubMed:23478264}. TISSUE SPECIFICITY: Detected in lung (PubMed:21821728). Detected in oligodendrocytes in corpus callosum in brain cortex (at protein level) (PubMed:25226845). Expressed within the embryonic cerebral cortex, where it is enriched in the ventricular zone (PubMed:8922387). In the adult brain, also expressed in oligodendrocytes, as well as Schwann cells of the peripheral nervous system (PubMed:9013780, PubMed:25226845). Expressed in many other tissues, including lung, heart, intestine, spleen, thymus, and stomach. No expression in liver (PubMed:9013780). Detected in kidney and testis (PubMed:9013780, PubMed:12215548). Detected in embryonic fibroblasts (PubMed:12215548). Detected in adult lung fibroblasts and lung endothelial cells (PubMed:18066075). Detected in dorsal root ganglion and dorsal root (PubMed:15195086). Detected in astrocytes (PubMed:17692995). Detected in bone (PubMed:21569876). {ECO:0000269|PubMed:12215548, ECO:0000269|PubMed:15195086, ECO:0000269|PubMed:18066075, ECO:0000269|PubMed:21569876, ECO:0000269|PubMed:25226845, ECO:0000269|PubMed:8922387, ECO:0000269|PubMed:9013780}. +Q6PB66 LPPRC_MOUSE Leucine-rich PPR motif-containing protein, mitochondrial (130 kDa leucine-rich protein) (LRP 130) (mLRP130) 1392 156,615 Chain (1); Erroneous initiation (1); Erroneous translation (1); Modified residue (10); Region (1); Repeat (20); Sequence conflict (4); Transit peptide (1) FUNCTION: May play a role in RNA metabolism in both nuclei and mitochondria. In the nucleus binds to HNRPA1-associated poly(A) mRNAs and is part of nmRNP complexes at late stages of mRNA maturation which are possibly associated with nuclear mRNA export. May bind mature mRNA in the nucleus outer membrane. In mitochondria binds to poly(A) mRNA. Plays a role in translation or stability of mitochondrially encoded cytochrome c oxidase (COX) subunits. May be involved in transcription regulation. Cooperates with PPARGC1A to regulate certain mitochondrially encoded genes and gluconeogenic genes and may regulate docking of PPARGC1A to transcription factors. Seems to be involved in the transcription regulation of the multidrug-related genes MDR1 and MVP. Part of a nuclear factor that binds to the invMED1 element of MDR1 and MVP gene promoters (By similarity). Binds single-stranded DNA. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Nucleus {ECO:0000269|PubMed:12071956}. Nucleus, nucleoplasm {ECO:0000250}. Nucleus inner membrane {ECO:0000250}. Nucleus outer membrane {ECO:0000250}. SUBUNIT: Interacts with CECR2, HEBP2, MAP1S and UXT (By similarity). Interacts with PPARGC1A (By similarity). Interacts with FOXO1. Component of mRNP complexes associated with HNRPA1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Strongly expressed in heart, liver and kidney. Weakly expressed in brain, skeletal muscle and testes. {ECO:0000269|PubMed:12071956}. +Q9CRC8 LRC40_MOUSE Leucine-rich repeat-containing protein 40 602 68,076 Chain (1); Modified residue (1); Repeat (21); Sequence conflict (3) +Q9DA39 LFG4_MOUSE Protein lifeguard 4 (Transmembrane BAX inhibitor motif-containing protein 4) (Z-protein) 238 26,647 Chain (1); Intramembrane (1); Topological domain (8); Transmembrane (6) INTRAMEM 209 229 Helical. {ECO:0000255}. TRANSMEM 39 59 Helical. {ECO:0000255}.; TRANSMEM 69 89 Helical. {ECO:0000255}.; TRANSMEM 98 118 Helical. {ECO:0000255}.; TRANSMEM 121 141 Helical. {ECO:0000255}.; TRANSMEM 152 172 Helical. {ECO:0000255}.; TRANSMEM 176 196 Helical. {ECO:0000255}. TOPO_DOM 1 38 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 60 68 Lumenal. {ECO:0000255}.; TOPO_DOM 90 97 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 119 120 Lumenal. {ECO:0000255}.; TOPO_DOM 142 151 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 173 175 Lumenal. {ECO:0000255}.; TOPO_DOM 197 208 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 230 238 Cytoplasmic. {ECO:0000255}. FUNCTION: Anti-apoptotic protein which can inhibit apoptosis induced by intrinsic and extrinsic apoptotic stimuli. Can modulate both capacitative Ca2+ entry and inositol 1,4,5-trisphosphate (IP3)-mediated Ca2+ release (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane protein. SUBUNIT: Interacts with ITPR3. {ECO:0000250}. +Q64280 LFTY1_MOUSE Left-right determination factor 1 (Protein lefty-1) (Lefty protein) (Stimulated by retinoic acid gene 3 protein) (Transforming growth factor beta-4) (TGF-beta-4) 368 41,498 Chain (1); Disulfide bond (4); Glycosylation (1); Propeptide (1); Signal peptide (1) FUNCTION: Required for left-right axis determination as a regulator of LEFTY2 and NODAL. {ECO:0000269|PubMed:9708731}. PTM: The processing of the protein may also occur at the second R-X-X-R site located at AA 132-135. Processing appears to be regulated in a cell-type specific manner. SUBCELLULAR LOCATION: Secreted. +Q9CTN8 LHPL3_MOUSE LHFPL tetraspan subfamily member 3 protein (Lipoma HMGIC fusion partner-like 3 protein) 222 24,686 Chain (1); Transmembrane (4) TRANSMEM 22 42 Helical. {ECO:0000255}.; TRANSMEM 96 116 Helical. {ECO:0000255}.; TRANSMEM 126 146 Helical. {ECO:0000255}.; TRANSMEM 177 197 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Brain-specific. {ECO:0000269|PubMed:26964900}. +Q9R1R0 LHX6_MOUSE LIM/homeobox protein Lhx6 (LIM homeobox protein 6) (LIM/homeobox protein Lhx6.1) 363 40,044 Alternative sequence (1); Chain (1); DNA binding (1); Domain (2); Region (1); Sequence caution (1); Sequence conflict (6) FUNCTION: Probable transcription factor required for the expression of a subset of genes involved in interneurons migration and development. Functions in the specification of cortical interneuron subtypes and in the migration of GABAergic interneuron precursors from the subpallium to the cerebral cortex. {ECO:0000269|PubMed:10393337, ECO:0000269|PubMed:15201337, ECO:0000269|PubMed:17376969, ECO:0000269|PubMed:18339674, ECO:0000269|PubMed:18613121}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Interacts with LDB1 (via the LIM zinc-binding domains). {ECO:0000269|PubMed:10393337}. TISSUE SPECIFICITY: Brain specific. Expressed by neurons in the amygdala that are activated by reproductive olfactory stimuli and project in regions of the hypothalamus involved in reproduction (at protein level). {ECO:0000269|PubMed:10393337, ECO:0000269|PubMed:15944132}. +Q9WUH2 LHX9_MOUSE LIM/homeobox protein Lhx9 (LIM homeobox protein 9) 397 44,045 Alternative sequence (2); Chain (1); DNA binding (1); Domain (2); Sequence conflict (4) FUNCTION: Involved in gonadal development. {ECO:0000269|PubMed:10706291}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:10706291}. SUBUNIT: Interacts with LDB1 and LDB2. {ECO:0000269|PubMed:10330499, ECO:0000269|PubMed:9880598}. TISSUE SPECIFICITY: Expressed in the dorsal thalamus and inner nuclei of the cerebellum. {ECO:0000269|PubMed:9880598}. +Q99M04 LIAS_MOUSE Lipoyl synthase, mitochondrial (EC 2.8.1.8) (Lipoate synthase) (LS) (Lip-syn) (mLIP1) (Lipoic acid synthase) 373 41,879 Chain (1); Metal binding (6); Transit peptide (1) Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 2/2. FUNCTION: Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. {ECO:0000305}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03123, ECO:0000269|PubMed:11389890}. TISSUE SPECIFICITY: Expressed predominantly in heart, testis, and liver. {ECO:0000269|PubMed:11389890}. +P09056 LIF_MOUSE Leukemia inhibitory factor (LIF) (Differentiation-stimulating factor) (D factor) 203 22,287 Beta strand (2); Chain (1); Disulfide bond (3); Glycosylation (6); Helix (7); Signal peptide (1) FUNCTION: LIF has the capacity to induce terminal differentiation in leukemic cells. Its activities include the induction of hematopoietic differentiation in normal and myeloid leukemia cells, the induction of neuronal cell differentiation, and the stimulation of acute-phase protein synthesis in hepatocytes. SUBCELLULAR LOCATION: Secreted. +O54785 LIMK2_MOUSE LIM domain kinase 2 (LIMK-2) (EC 2.7.11.1) 638 72,202 Active site (1); Alternative sequence (2); Beta strand (7); Binding site (1); Chain (1); Domain (4); Helix (2); Modified residue (4); Nucleotide binding (1); Turn (2) FUNCTION: Displays serine/threonine-specific phosphorylation of myelin basic protein and histone (MBP) in vitro. {ECO:0000250|UniProtKB:P53671}. PTM: Phosphorylated on serine and/or threonine residues by ROCK1. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Binds ROCK1 and MARF1 (By similarity). Interacts with PARD3 (By similarity). Interacts with NISCH. {ECO:0000250|UniProtKB:P53671, ECO:0000269|PubMed:18332102}. TISSUE SPECIFICITY: Isoform 3 is testis specific. +Q8CD94 LIN52_MOUSE Protein lin-52 homolog 116 13,001 Chain (1); Modified residue (2) SUBUNIT: Component of the DREAM complex (also named LINC complex) at least composed of E2F4, E2F5, LIN9, LIN37, LIN52, LIN54, MYBL1, MYBL2, RBL1, RBL2, RBBP4, TFDP1 and TFDP2. The complex exists in quiescent cells where it represses cell cycle-dependent genes. It dissociates in S phase when LIN9, LIN37, LIN52 and LIN54 form a subcomplex that binds to MYBL2 (By similarity). {ECO:0000250}. +Q9QXD8 LIMD1_MOUSE LIM domain-containing protein 1 668 71,422 Chain (1); Domain (3); Modified residue (7); Region (4); Sequence conflict (3) FUNCTION: Adapter or scaffold protein which participates in the assembly of numerous protein complexes and is involved in several cellular processes such as cell fate determination, cytoskeletal organization, repression of gene transcription, cell-cell adhesion, cell differentiation, proliferation and migration. Positively regulates microRNA (miRNA)-mediated gene silencing and is essential for P-body formation and integrity. Acts as a hypoxic regulator by bridging an association between the prolyl hydroxylases and VHL enabling efficient degradation of HIF1A. Acts as a transcriptional corepressor for SNAI1- and SNAI2/SLUG-dependent repression of E-cadherin transcription. Negatively regulates the Hippo signaling pathway and antagonizes phosphorylation of YAP1. Inhibits E2F-mediated transcription, and suppresses the expression of the majority of genes with E2F1-responsive elements. Regulates osteoblast development, function, differentiation and stress osteoclastogenesis. Enhances the ability of TRAF6 to activate adapter protein complex 1 (AP-1) and negatively regulates the canonical Wnt receptor signaling pathway in osteoblasts. May act as a tumor suppressor by inhibiting cell proliferation. {ECO:0000269|PubMed:17092936, ECO:0000269|PubMed:18657804}. PTM: Phosphorylated during mitosis. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18657804}. Nucleus {ECO:0000250}. Cytoplasm, P-body {ECO:0000250}. Cell junction, adherens junction {ECO:0000250}. Cell junction, focal adhesion {ECO:0000250}. Note=Shuttles between cytoplasm and nucleus but is localized predominantly to the cytoplasm. Found in the nucleus but not nucleoli. Colocalizes with VCL in the focal adhesions (By similarity). {ECO:0000250}. SUBUNIT: Interacts with SQSTM1 and RB1. Interacts with EIF4E, AGO1, AGO2, DCP2, DDX6, LATS1, LATS2, EGLN1/PHD2, EGLN2/PHD1 and EGLN3/PHD3. Interacts (via LIM zinc-binding 2) with VHL. Found in a complex composed of LIMD1, VHL, EGLN1/PHD2, ELOB and CUL2 (By similarity). Interacts (via LIM domains) with SNAI1 (via SNAG domain), SNAI2/SLUG (via SNAG domain) and SCRT1 (via SNAG domain). Found in a complex with TRAF6, PRKCZ and SQSTM1. Interacts (via LIM domains) with TRAF6. {ECO:0000250, ECO:0000269|PubMed:17092936, ECO:0000269|PubMed:18331720}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10647888}. +Q6NVG1 LPCT4_MOUSE Lysophospholipid acyltransferase LPCAT4 (1-acylglycerol-3-phosphate O-acyltransferase 7) (1-AGP acyltransferase 7) (1-AGPAT 7) (1-acylglycerophosphocholine O-acyltransferase) (EC 2.3.1.23) (1-acylglycerophosphoserine O-acyltransferase) (EC 2.3.1.n6) (1-alkenylglycerophosphoethanolamine O-acyltransferase) (EC 2.3.1.121) (1-alkylglycerophosphocholine O-acetyltransferase) (EC 2.3.1.67) (Acyltransferase-like 3) (Lysophosphatidylcholine acyltransferase 4) (Lysophosphatidylethanolamine acyltransferase 2) (EC 2.3.1.n7) (Plasmalogen synthase) 524 57,143 Chain (1); Glycosylation (1); Motif (1); Sequence conflict (1); Transmembrane (2) TRANSMEM 40 62 Helical. {ECO:0000255}.; TRANSMEM 87 107 Helical. {ECO:0000255}. Lipid metabolism; phospholipid metabolism. FUNCTION: Displays acyl-CoA-dependent lysophospholipid acyltransferase activity with a subset of lysophospholipids as substrates; converts lysophosphatidylethanolamine to phosphatidylethanolamine, 1-alkenyl-lysophatidylethanolamine to 1-alkenyl-phosphatidylethanolamine, lysophosphatidylglycerol and alkyl-lysophosphatidylcholine to phosphatidylglycerol and alkyl-phosphatidylcholine, respectively. In contrast, has no lysophosphatidylinositol, glycerol-3-phosphate, diacylglycerol or lysophosphatidic acid acyltransferase activity. Prefers long chain acyl-CoAs (C16, C18) as acyl donors (By similarity). Converts lysophosphatidylcholine to phosphatidycholine. {ECO:0000250, ECO:0000269|PubMed:18156367}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed with much higher level in brain. Expressed in erythroleukemic cells but not in reticulocytes. {ECO:0000269|PubMed:18156367, ECO:0000269|PubMed:18458083}. +Q3UJB3 LR14B_MOUSE Leucine-rich repeat-containing protein 14B 510 56,543 Chain (1); Erroneous initiation (1); Repeat (8) +Q8K0B3 LRC66_MOUSE Leucine-rich repeat-containing protein 66 872 97,626 Chain (1); Glycosylation (3); Modified residue (2); Repeat (5); Transmembrane (2) TRANSMEM 4 24 Helical. {ECO:0000255}.; TRANSMEM 371 391 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q7TPD7 LR75B_MOUSE Leucine-rich repeat-containing protein 75B (Leucine-rich repeat-containing protein FAM211B) 306 34,160 Chain (1); Repeat (2) +Q3UHC2 LRRK1_MOUSE Leucine-rich repeat serine/threonine-protein kinase 1 (EC 2.7.11.1) 2014 225,470 Active site (1); Alternative sequence (4); Binding site (1); Chain (1); Domain (2); Erroneous initiation (3); Nucleotide binding (1); Repeat (17); Sequence conflict (18) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q38SD2}. SUBUNIT: Homodimer. {ECO:0000250}. +Q5M8M9 LRC52_MOUSE Leucine-rich repeat-containing protein 52 (BK channel auxiliary gamma subunit LRRC52) 314 35,295 Chain (1); Disulfide bond (4); Domain (2); Glycosylation (5); Repeat (5); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 245 265 Helical. {ECO:0000255}. TOPO_DOM 24 244 Extracellular. {ECO:0000255}.; TOPO_DOM 266 314 Cytoplasmic. {ECO:0000255}. FUNCTION: Auxiliary protein of the large-conductance, voltage and calcium-activated potassium channel (BK alpha). Modulates gating properties by producing a marked shift in the BK channel's voltage dependence of activation in the hyperpolarizing direction, and in the absence of calcium (By similarity). KCNU1 channel auxiliary protein. May modulate KCNU1 gating properties, shifting KCNU1 gating to more negative potentials at a given pH. {ECO:0000250, ECO:0000269|PubMed:22084117}. PTM: N-glycosylated. {ECO:0000269|PubMed:22084117}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22084117}; Single-pass membrane protein {ECO:0000269|PubMed:22084117}. Note=Expression at the cell surface may require the presence of KCNU1. SUBUNIT: Interacts with KCNMA1 (By similarity). May interact with KCNU1; this interaction may be required for LRRC52 stability and may change the channel gating properties. {ECO:0000250, ECO:0000269|PubMed:22084117}. DOMAIN: The transmembrane domain is necessary for interaction with KCNMA1. {ECO:0000250}. TISSUE SPECIFICITY: Testis-specific (at protein level). At the mRNA level, also detected in kidney, ventricle, spinal cord and skeletal muscle, although at lower levels compared to testis. Expression in testis at the protein level requires the presence of KCNU1. {ECO:0000269|PubMed:22084117}. +Q8K3W2 LRC10_MOUSE Leucine-rich repeat-containing protein 10 (Heart-restricted leucine-rich repeat protein) 274 31,263 Chain (1); Compositional bias (1); Repeat (8); Sequence conflict (2) FUNCTION: May play important roles in cardiac development and/or cardiac function. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14751244}. TISSUE SPECIFICITY: Detected specifically in the heart. {ECO:0000269|PubMed:14751244}. +Q66L42 M3K10_MOUSE Mitogen-activated protein kinase kinase kinase 10 (EC 2.7.11.25) 940 103,187 Active site (1); Binding site (1); Chain (1); Compositional bias (1); Domain (2); Modified residue (7); Nucleotide binding (1); Region (2); Sequence conflict (1) FUNCTION: Activates the JUN N-terminal pathway. {ECO:0000250}. PTM: Autophosphorylation on serine and threonine residues within the activation loop plays a role in enzyme activation. {ECO:0000250}. SUBUNIT: Homodimer. Interacts with SH3RF2. {ECO:0000250, ECO:0000250|UniProtKB:D3ZG83}. +Q6NS57 MABP1_MOUSE Mitogen-activated protein kinase-binding protein 1 (JNK-binding protein 1) (JNKBP-1) 1503 162,892 Alternative sequence (1); Chain (1); Compositional bias (2); Modified residue (1); Repeat (12); Sequence conflict (31) FUNCTION: Negative regulator of NOD2 function. It down-regulates NOD2-induced processes such as activation of NF-kappa-B signaling, IL8 secretion and antibacterial response (By similarity). Involved in JNK signaling pathway (PubMed:10471813). {ECO:0000250|UniProtKB:O60336, ECO:0000269|PubMed:10471813}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O60336}. Nucleus {ECO:0000250|UniProtKB:O60336}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:O60336}. Note=Not detected in the cilium. Localized around the poles of the mitotic spindle from prophase to anaphase in mitotic cells. {ECO:0000250|UniProtKB:O60336}. SUBUNIT: Can form homodimers (via C-terminus). Interacts (via C-terminus) with WDR62 (via C-terminus). Interacts with MAPK9. Interacts (via N-terminus) with NOD2; the interaction is enhanced in presence of muramyl dipeptide (MDP) (By similarity). Interacts with MAPK10 (PubMed:10471813). {ECO:0000250|UniProtKB:O60336, ECO:0000269|PubMed:10471813}. DOMAIN: The N-terminal WD40 domain is necessary for the interaction with NOD2 and down-regulation of NOD2 function. {ECO:0000250|UniProtKB:O60336}. TISSUE SPECIFICITY: Ubiquitously expressed. Highest expression observed in brain. {ECO:0000269|PubMed:10471813}. +Q9ESL4 M3K20_MOUSE Mitogen-activated protein kinase kinase kinase 20 (EC 2.7.11.25) (Human cervical cancer suppressor gene 4 protein) (HCCS-4) (Leucine zipper- and sterile alpha motif kinase ZAK) (Leucine zipper- and sterile alpha motif-containing kinase) (MLK-like mitogen-activated protein triple kinase) (Mitogen-activated protein kinase kinase kinase MLT) (Mixed lineage kinase-related kinase) (MLK-related kinase) (MRK) (Sterile alpha motif- and leucine zipper-containing kinase AZK) 802 91,720 Active site (1); Alternative sequence (4); Binding site (1); Chain (1); Domain (2); Initiator methionine (1); Modified residue (18); Mutagenesis (1); Nucleotide binding (1); Region (1); Sequence conflict (1) FUNCTION: Stress-activated component of a protein kinase signal transduction cascade. Regulates the JNK and p38 pathways (PubMed:11042189). Part of a signaling cascade that begins with the activation of the adrenergic receptor ADRA1B and leads to the activation of MAPK14 (By similarity). Pro-apoptotic. Role in regulation of S and G2 cell cycle checkpoint by direct phosphorylation of CHEK2 (By similarity). Involved in limb development (PubMed:26755636). {ECO:0000250|UniProtKB:Q9NYL2, ECO:0000269|PubMed:11042189, ECO:0000269|PubMed:26755636}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11042189}. Nucleus {ECO:0000269|PubMed:11042189}. Note=Appears to shuttle between nucleus and cytoplasm. {ECO:0000269|PubMed:11042189}. SUBUNIT: Homodimer (PubMed:11042189). Interacts with PKN1 and ZNF33A. Component of a signaling complex containing at least AKAP13, PKN1, MAPK14, MAP3K20 and MAP2K3. Within this complex, AKAP13 interacts directly with PKN1, which in turn recruits MAPK14, MAP2K3 and MAP3K20. {ECO:0000250|UniProtKB:Q9NYL2, ECO:0000269|PubMed:11042189}. +Q9QZ04 MAGL2_MOUSE MAGE-like protein 2 (Protein nS7) 1284 137,987 Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (2) FUNCTION: Probably enhances ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases, possibly through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex. Acts as a regulator of retrograde transport via its interaction with VPS35. Recruited to retromer-containing endosomes and promotes the formation of 'Lys-63'-linked polyubiquitin chains at 'Lys-220' of WASHC1 together with TRIM27, leading to promote endosomal F-actin assembly (By similarity). Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer. Significantly promotes the cytoplasmic accumulation of CLOCK (PubMed:22208286). {ECO:0000250|UniProtKB:Q9UJ55, ECO:0000269|PubMed:22208286}. SUBCELLULAR LOCATION: Early endosome. Cytoplasm {ECO:0000269|PubMed:22208286}. Nucleus {ECO:0000269|PubMed:22208286}. Note=Recruited to retromer-containing endosomes via interaction with VPS35. Colocalizes with CLOCK and ARNTL/BMLA1 in the cytoplasm, and with PER2 in the cytoplasm and nucleus. {ECO:0000250|UniProtKB:Q9UJ55, ECO:0000269|PubMed:22208286}. SUBUNIT: Interacts with TRIM27. Interacts with VPS35; leading to recruitment at retromer-containing endosomes (By similarity). Interacts with ARNTL/BMAL1 and PER2. {ECO:0000250|UniProtKB:Q9UJ55, ECO:0000269|PubMed:22208286}. TISSUE SPECIFICITY: Expressed predominantly in late development stages and adult brain. {ECO:0000269|PubMed:10915770}. +P97820 M4K4_MOUSE Mitogen-activated protein kinase kinase kinase kinase 4 (EC 2.7.11.1) (HPK/GCK-like kinase HGK) (MAPK/ERK kinase kinase kinase 4) (MEK kinase kinase 4) (MEKKK 4) (Nck-interacting kinase) 1233 140,602 Active site (1); Binding site (1); Chain (1); Domain (2); Initiator methionine (1); Modified residue (22); Nucleotide binding (1); Region (1) FUNCTION: Serine/threonine kinase that may play a role in the response to environmental stress and cytokines such as TNF-alpha. Appears to act upstream of the JUN N-terminal pathway. Phosphorylates SMAD1 on Thr-322 (By similarity). {ECO:0000250, ECO:0000269|PubMed:10669731, ECO:0000269|PubMed:9135144}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with the SH3 domain of the adapter proteins Nck. Interacts (via its CNH regulatory domain) with ATL1 (via the N-terminal region). Interacts with RAP2A (GTP-bound form preferentially) (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Appears to be ubiquitous, expressed in all tissue types examined. Highest levels observed in heart and brain. {ECO:0000269|PubMed:9135144}. +Q8BI08 MAL2_MOUSE Protein MAL2 175 19,094 Chain (1); Domain (1); Glycosylation (1); Topological domain (5); Transmembrane (4) TRANSMEM 34 54 Helical. {ECO:0000255}.; TRANSMEM 66 86 Helical. {ECO:0000255}.; TRANSMEM 102 122 Helical. {ECO:0000255}.; TRANSMEM 149 169 Helical. {ECO:0000255}. TOPO_DOM 1 33 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 55 65 Lumenal. {ECO:0000255}.; TOPO_DOM 87 101 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 123 148 Lumenal. {ECO:0000255}.; TOPO_DOM 170 175 Cytoplasmic. {ECO:0000255}. FUNCTION: Member of the machinery of polarized transport. Required for the indirect transcytotic route at the step of the egress of the transcytosing cargo from perinuclear endosomes in order for it to travel to the apical surface via a raft-dependent pathway (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Apical cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Associated with lipid rafts. In polarized epithelial cells, restricted to the apical surface (By similarity). {ECO:0000250}. SUBUNIT: Interacts with TPD52L2. {ECO:0000250}. +Q8CG85 MAMC2_MOUSE MAM domain-containing protein 2 (MAM domain-containing proteoglycan) (Mamcan) 686 77,324 Chain (1); Domain (4); Glycosylation (3); Sequence conflict (3); Signal peptide (1) PTM: O-glycosylated; contains chondroitin sulfate. {ECO:0000269|PubMed:18757743}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:18757743}. +A2AJX4 MALR1_MOUSE MAM and LDL-receptor class A domain-containing protein 1 2123 236,194 Chain (1); Disulfide bond (31); Domain (20); Glycosylation (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 2040 2060 Helical. {ECO:0000255}. TOPO_DOM 27 2039 Vesicular. {ECO:0000305}.; TOPO_DOM 2061 2123 Cytoplasmic. {ECO:0000305}. FUNCTION: Enhances production and/or transport of FGF15 and thus has a role in regulation of bile acid synthesis. {ECO:0000269|PubMed:23747249}. SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:23747249}; Single-pass type I membrane protein {ECO:0000255}. SUBUNIT: Interacts with FGF15. {ECO:0000269|PubMed:23747249}. TISSUE SPECIFICITY: Strongly expressed in epithelial cells of the small intestine. Also detected in kidney cortex, and testis. {ECO:0000269|PubMed:23747249}. +Q9EQJ9 MAGI3_MOUSE Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 3 (Membrane-associated guanylate kinase inverted 3) (MAGI-3) 1476 161,672 Alternative sequence (2); Chain (1); Compositional bias (2); Domain (9); Modified residue (6); Nucleotide binding (1); Region (4); Sequence caution (1); Sequence conflict (1) FUNCTION: Acts as a scaffolding protein at cell-cell junctions, thereby regulating various cellular and signaling processes. Cooperates with PTEN to modulate the kinase activity of AKT1. Its interaction with PTPRB and tyrosine phosphorylated proteins suggests that it may link receptor tyrosine phosphatase with its substrates at the plasma membrane. In polarized epithelial cells, involved in efficient trafficking of TGFA to the cell surface. Regulates the ability of LPAR2 to activate ERK and RhoA pathways. Regulates the JNK signaling cascade via its interaction with FZD4 and VANGL2. {ECO:0000269|PubMed:15195140, ECO:0000269|PubMed:15652357}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15195140}; Peripheral membrane protein {ECO:0000269|PubMed:15195140}. Cell junction, tight junction {ECO:0000269|PubMed:15195140}. Nucleus {ECO:0000250}. Note=Concentrates in specific sites at the plasma membrane and in the nucleus. In epithelial cells, it localizes at tight junctions (By similarity). {ECO:0000250}. SUBUNIT: Interacts with ADRB1, ADGRB1, LPAR2/EDG4, GRIN2B, PTEN, and PTPRB. Interacts with unidentified tyrosine phosphorylated proteins (By similarity). Interacts with FZD4, FZD7, TGFA and VANGL2. Interacts with DLL1 (PubMed:15509766). {ECO:0000250|UniProtKB:Q5TCQ9, ECO:0000250|UniProtKB:Q9JK71, ECO:0000269|PubMed:15195140, ECO:0000269|PubMed:15509766, ECO:0000269|PubMed:15652357}. TISSUE SPECIFICITY: Widely expressed. Colocalizes with TGFA in neurons in the cortex and dentate gyrus, as well as in ependymal cells and some astrocytes (at protein level). Present in lens epithelium. {ECO:0000269|PubMed:14645510, ECO:0000269|PubMed:15652357}. +Q8K2I4 MANBA_MOUSE Beta-mannosidase (EC 3.2.1.25) (Lysosomal beta A mannosidase) (Mannanase) (Mannase) 879 100,831 Active site (1); Chain (1); Glycosylation (10); Sequence conflict (20); Signal peptide (1) Glycan metabolism; N-glycan degradation. FUNCTION: Exoglycosidase that cleaves the single beta-linked mannose residue from the non-reducing end of all N-linked glycoprotein oligosaccharides. {ECO:0000250|UniProtKB:O00462}. SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:O00462}. TISSUE SPECIFICITY: Highest level in liver, high levels in lung, testis, skin and spleen, moderate level in thymus. Activity found in plasma, kidney, liver, spleen, pancreas, brain, testis, epididymis, heart, lung and skeletal muscle. {ECO:0000269|PubMed:11892998, ECO:0000269|PubMed:16377659}. +Q9QYR6 MAP1A_MOUSE Microtubule-associated protein 1A (MAP-1A) [Cleaved into: MAP1A heavy chain; MAP1 light chain LC2] 2776 300,140 Alternative sequence (1); Chain (3); Compositional bias (4); Helix (2); Modified residue (77); Region (1); Repeat (11); Sequence conflict (1) FUNCTION: Structural protein involved in the filamentous cross-bridging between microtubules and other skeletal elements. PTM: Phosphorylated by CSNK1D. {ECO:0000250}.; PTM: LC2 is generated from MAP1A by proteolytic processing. It is free to associate with both MAP1A and MAP1B (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. SUBUNIT: 3 different light chains, LC1, LC2 and LC3, can associate with MAP1A and MAP1B proteins. Interacts with guanylate kinase-like domain of DLG1, DLG2 and DLG4. Binds to CSNK1D (By similarity). Interacts with TIAM2. {ECO:0000250, ECO:0000269|PubMed:17320046}. DOMAIN: The basic region containing the repeats may be responsible for the binding of MAP1A to microtubules. TISSUE SPECIFICITY: Both isoforms highly expressed in brain, and to a lesser extent in embryo. Isoform 1 is also expressed at a low level in other tissues including heart and muscle. {ECO:0000269|PubMed:11311937}. +Q8C052 MAP1S_MOUSE Microtubule-associated protein 1S (MAP-1S) (BPY2-interacting protein 1) (Microtubule-associated protein 8) [Cleaved into: MAP1S heavy chain; MAP1S light chain] 973 102,939 Chain (3); Compositional bias (1); Erroneous initiation (1); Modified residue (7); Region (5); Sequence caution (1); Sequence conflict (3) FUNCTION: Microtubule-associated protein that mediates aggregation of mitochondria resulting in cell death and genomic destruction (MAGD). Plays a role in anchoring the microtubule organizing center to the centrosomes. Binds to DNA. Plays a role in apoptosis (By similarity). Involved in the formation of microtubule bundles. {ECO:0000250, ECO:0000269|PubMed:15528209}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15528209}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:15528209}. Note=Detected in perinuclear punctate network corresponding to mitochondrial aggregates and in the nucleus in cells exhibiting apoptosis. Associated specifically with microtubules stabilized by paclitaxel and colocalizes with RASSF1. In interphase cells, shows a diffuse cytoplasmic staining with partial localization to the microtubules. During the different stages of mitosis detected at the spindle microtubules. Detected in filopodia-like protrusions and synapses (By similarity). {ECO:0000250}. SUBUNIT: Heterodimer of a heavy and a light chain. Interacts with microtubules and actin. Both MAP1S heavy and light chains interact with microtubules. MAP1S light chain interacts with actin. Interacts with ESR1, LRPPRC, RASSF1, microtubules and VCY2. Interacts with WDR47 (via N-terminus of light chain) (By similarity). Interacts (via C-terminus) with GAN (via Kelch domains). {ECO:0000250, ECO:0000269|PubMed:15528209, ECO:0000269|PubMed:16297881, ECO:0000269|PubMed:16565160}. DOMAIN: Its C-terminal part of the heavy chain interacts with ESR1 (By similarity). The N-terminus of the heavy chain associates with the C-terminus of the light chain to form the heterodimer complex. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in ventral and dorsal horns of the spinal cord, hippocampus, cerebral cortex, molecular, Purkinje and granular cell layers of the cerebellum and in dorsal root ganglia of the PNS (at protein level). Expressed in brain, testis, heart, lung, kidney and liver. {ECO:0000269|PubMed:15528209, ECO:0000269|PubMed:16297881}. +P51942 MATN1_MOUSE Cartilage matrix protein (Matrilin-1) 500 54,421 Chain (1); Coiled coil (1); Disulfide bond (5); Domain (3); Glycosylation (2); Sequence conflict (4); Signal peptide (1) FUNCTION: Cartilage matrix protein is a major component of the extracellular matrix of non-articular cartilage. It binds to collagen. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. SUBUNIT: Homotrimer. Interacts with COMP (By similarity). {ECO:0000250}. +O08746 MATN2_MOUSE Matrilin-2 956 106,748 Alternative sequence (1); Chain (1); Coiled coil (1); Disulfide bond (30); Domain (12); Glycosylation (2); Sequence conflict (1); Signal peptide (1) FUNCTION: Involved in matrix assembly. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Detected in a variety of organs, including calvaria, uterus, heart and brain, as well as fibroblast and osteoblast cell lines. +Q8R4B8 NLRP3_MOUSE NACHT, LRR and PYD domains-containing protein 3 (Cold autoinflammatory syndrome 1 protein homolog) (Cryopyrin) (Mast cell maturation-associated-inducible protein 1) (PYRIN-containing APAF1-like protein 1) 1033 118,275 Alternative sequence (3); Chain (1); Disulfide bond (1); Domain (2); Nucleotide binding (1); Repeat (9); Sequence conflict (1) FUNCTION: As the sensor component of the NLRP3 inflammasome, plays a crucial role in innate immunity and inflammation. In response to pathogens and other damage-associated signals, initiates the formation of the inflammasome polymeric complex, made of NLRP3, PYCARD and CASP1 (or possibly CASP4/CASP11). Recruitment of proCASP1 to the inflammasome promotes its activation and CASP1-catalyzed IL1B and IL18 maturation and secretion in the extracellular milieu (PubMed:28847925). Activation of NLRP3 inflammasome is also required for HMGB1 secretion (PubMed:22801494). The active cytokines and HMGB1 stimulate inflammatory responses. Inflammasomes can also induce pyroptosis, an inflammatory form of programmed cell death. Under resting conditions, NLRP3 is autoinhibited. NLRP3 activation stimuli include extracellular ATP, reactive oxygen species, K(+) efflux, crystals of monosodium urate or cholesterol, amyloid-beta fibers, environmental or industrial particles and nanoparticles, cytosolic dsRNA, etc. However, it is unclear what constitutes the direct NLRP3 activator. Activation in presence of cytosolic dsRNA is mediated by DHX33 (By similarity). Independently of inflammasome activation, regulates the differentiation of T helper 2 (Th2) cells and has a role in Th2 cell-dependent asthma and tumor growth. During Th2 differentiation, required for optimal IRF4 binding to IL4 promoter and for IRF4-dependent IL4 transcription. Binds to the consensus DNA sequence 5'-GRRGGNRGAG-3'. May also participate in the transcription of IL5, IL13, GATA3, CCR3, CCR4 and MAF (PubMed:26098997). {ECO:0000250|UniProtKB:Q96P20, ECO:0000269|PubMed:16407888, ECO:0000269|PubMed:16407890, ECO:0000269|PubMed:16546100, ECO:0000269|PubMed:17008311, ECO:0000269|PubMed:22801494, ECO:0000269|PubMed:26098997, ECO:0000269|PubMed:28847925}. PTM: Ubiquitinated; undergoes both 'Lys-48'- and 'Lys-63'-linked polyubiquitination. Ubiquitination does not lead to degradation, but inhibits inflammasome activation (PubMed:23246432). Deubiquitination is catalyzed by BRCC3 and associated with NLRP3 activation and inflammasome assembly. This process can be induced by the activation of Toll-like receptors (by LPS), through a non-transcriptional pathway dependent on the mitochondrial production of reactive oxygen species, and by ATP. {ECO:0000269|PubMed:22948162, ECO:0000269|PubMed:23246432}.; PTM: The disulfide bond in the pyrin domain might play a role in reactive oxygen species-mediated activation. {ECO:0000250|UniProtKB:Q96P20}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:14688236, ECO:0000269|PubMed:23502856, ECO:0000269|PubMed:26098997}. Inflammasome {ECO:0000269|PubMed:14688236, ECO:0000269|PubMed:23502856, ECO:0000269|PubMed:26098997}. Endoplasmic reticulum {ECO:0000269|PubMed:23502856}. Secreted {ECO:0000269|PubMed:24952504}. Nucleus {ECO:0000269|PubMed:26098997}. Note=In macrophages, under resting conditions, mainly located in the cytosol, on the endoplasmic reticulum. After stimulation with inducers of the NLRP3 inflammasome, mitochondria redistribute in the vicinity of the endoplasmic reticulum in the perinuclear region, which results in colocalization of NLRP3 on the endoplasmic reticulum and PYCARD on mitochondria, allowing the activation of inflammasome assembly (PubMed:23502856). After the induction of pyroptosis, inflammasome specks are released into the extracellular space where they can further promote IL1B processing and where they can be engulfed by macrophages. Phagocytosis induces lysosomal damage and inflammasome activation in the recipient cells (PubMed:24952505)(PubMed:24952504). In the Th2 subset of CD4(+) helper T-cells, mainly located in the nucleus. Nuclear localization depends upon KPNA2 (PubMed:26098997). In the Th1 subset of CD4(+) helper T-cells, mainly cytoplasmic (PubMed:26098997). {ECO:0000269|PubMed:23502856, ECO:0000269|PubMed:24952504, ECO:0000269|PubMed:24952505}. SUBUNIT: Sensor component of NLRP3 inflammasomes. Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other damage-associated signals and play critical roles in innate immunity and inflammation. The core of NLRP3 inflammasomes consists of a signal sensor component (NLRP3), an adapter (ASC/PYCARD), which recruits an effector proinflammatory caspase (CASP1 and, possibly, CASP4 and CASP5). Within the complex, NLRP3 and PYCARD interact via their respective pyrin domains. This interaction initiates speck formation (nucleation) which greatly enhances further addition of soluble PYCARD molecules to the speck in a prion-like polymerization process. NLRP3 localizes at the end of each PYCARD filament. Clustered PYCARD nucleates the formation of CASP1 filaments through the interaction of their respective CARD domains, acting as a platform for CASP1 polymerization. CASP1 filament formation increases local enzyme concentration, resulting in trans-autocleavage and activation. Active CASP1 then processes IL1B and IL18 precursors, leading to the release of mature cytokines in the extracellular milieu and inflammatory response. Reconstituted ternary inflammasomes show star-shaped structures, in which multiple filaments, containing CASP1, protrude radially from a single central hub, containing the sensor protein and PYCARD. In this complex, the sensor protein is sub-stoichiometric to PYCARD, and PYCARD is further substoichiometric to CASP1, suggesting amplifications of signal transduction from the sensor, via the adapter, to the effector (By similarity). Interacts with MEFV; this interaction targets NLRP3 to degradation by autophagy, hence preventing excessive IL1B- and IL18-mediated inflammation (By similarity). Interacts with GBP5 (via DAPIN domain); this interaction promotes inflammasome assembly in response to microbial and soluble, but not crystalline, agents (By similarity). Interacts with EIF2AK2/PKR; this interaction requires EIF2AK2 activity, is accompanied by EIF2AK2 autophosphorylation and promotes inflammasome assembly in response to specific stimuli (PubMed:22801494). Interacts with PML (isoform PML-1) (via the LRR region); PML-mediated increase in NLRP3 inflammasome activation does not depend upon this interaction. Directly interacts with IRF4 (via LRR region); this interaction is required for optimal IRF4 binding to IL4 promoter and efficient IL4 transactivation during differentiation of Th2 helper T-cells (PubMed:26098997). Interacts (via NACHT domain) with DHX33 (via DEAH box) (By similarity). Interacts with PYDC5 (By similarity). {ECO:0000250|UniProtKB:Q96P20, ECO:0000269|PubMed:22801494, ECO:0000269|PubMed:26098997}. DOMAIN: The LRR domain mediates the interaction with IRF4 and PML. {ECO:0000250|UniProtKB:Q96P20, ECO:0000269|PubMed:26098997}.; DOMAIN: Intramolecular interactions between NACHT and leucine-rich repeat (LRR) domains may be important for autoinhibition in the absence of activating signal. {ECO:0000250|UniProtKB:Q9EPB4}.; DOMAIN: The pyrin domain (also called DAPIN domain or PYD) is involved in PYCARD-binding. TISSUE SPECIFICITY: Expressed with high levels in peripheral blood leukocytes, including Th2 lymphocytes and macrophages (PubMed:15302403, PubMed:26098997, PubMed:16546100, PubMed:28847925). Expressed at low levels in resting osteoblasts (at protein level) (PubMed:17907925). {ECO:0000269|PubMed:15302403, ECO:0000269|PubMed:16546100, ECO:0000269|PubMed:17907925, ECO:0000269|PubMed:26098997, ECO:0000269|PubMed:28847925}. +Q91WS2 NLRP6_MOUSE NACHT, LRR and PYD domains-containing protein 6 (Angiotensin II/vasopressin receptor) (Non-angiotensin-vasopressin receptor) (Non-AVR) (PYRIN-containing APAF1-like protein 5-like) 869 97,402 Alternative sequence (2); Chain (1); Compositional bias (2); Domain (2); Frameshift (1); Nucleotide binding (1); Repeat (3); Sequence conflict (4) FUNCTION: As the sensor component of the NLRP6 inflammasome, plays a crucial role in innate immunity and inflammation. In response to yet unidentified signals, initiates the formation of the inflammasome polymeric complex, made of NLRP6, PYCARD and CASP1 (or possibly CASP4/CASP11). Recruitment of proCASP1 to the inflammasome promotes its activation and CASP1-catalyzed IL1B and IL18 maturation and secretion in the extracellular milieu. The precise NLRP6 activation stimulus has not been identified yet (By similarity) (PubMed:21593405). Essential for gut mucosal self-renewal and proliferation (PubMed:21593405, PubMed:21565393, PubMed:21543645). Maintains intestinal homeostasis and a healthy intestinal microbiota (PubMed:21565393, PubMed:22763455). This function is, at least partially, mediated by IL18, and not IL1B, produced by nonhematopoietic cells (PubMed:21565393). Influences intestinal barrier function and microbial homeostasis through the regulation of goblet cell mucus secretion. Acts by promoting autophagy in goblet cells, an essential step for mucus granule exocytosis. Its role in goblet cell physiology is inflammasome-dependent, but IL1B- and IL18-independent (PubMed:24581500). During systemic bacterial infections, may negatively regulate inflammatory signaling and inhibit the influx of monocytes and neutrophils to the circulation and to the peritoneum (PubMed:22763455). May promote peripheral nerve recovery following injury via an inflammasome-independent mechanism (PubMed:26253422). {ECO:0000250|UniProtKB:Q96P20, ECO:0000269|PubMed:21543645, ECO:0000269|PubMed:21565393, ECO:0000269|PubMed:21593405, ECO:0000269|PubMed:22763455, ECO:0000269|PubMed:24581500, ECO:0000269|PubMed:26253422}. SUBCELLULAR LOCATION: Isoform 1: Cytoplasm {ECO:0000250|UniProtKB:Q63035}. Inflammasome {ECO:0000250|UniProtKB:P59044}. Cell membrane {ECO:0000250|UniProtKB:Q63035}. Nucleus membrane {ECO:0000250|UniProtKB:Q63035}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm {ECO:0000250|UniProtKB:Q63035}. Cell membrane {ECO:0000250|UniProtKB:Q63035}. Note=Predominantly expressed in the cell membrane. {ECO:0000250|UniProtKB:Q63035}. SUBUNIT: Sensor component of NLRP6 inflammasomes. Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other damage-associated signals and play critical roles in innate immunity and inflammation. The core of NLRP6 inflammasomes consists of a signal sensor component (NLRP6), an adapter (ASC/PYCARD), which recruits an effector proinflammatory caspase (CASP1 and, possibly, CASP4/CASP11). Within the complex, NLRP6 and PYCARD interact via their respective pyrin domains. This interaction initiates speck formation (nucleation) which greatly enhances further addition of soluble PYCARD molecules to the speck in a prion-like polymerization process. NLRP6 localizes at the end of each PYCARD filament. Clustered PYCARD nucleates the formation of CASP1 filaments through the interaction of their respective CARD domains, acting as a platform for CASP1 polymerization. CASP1 filament formation increases local enzyme concentration, resulting in trans-autocleavage and activation. Active CASP1 then processes IL1B and IL18 precursors, leading to the release of mature cytokines in the extracellular milieu and inflammatory response. In this complex, the sensor protein is sub-stoichiometric to PYCARD, and PYCARD is further substoichiometric to CASP1, suggesting amplifications of signal transduction from the sensor, via the adapter, to the effector. {ECO:0000250|UniProtKB:Q96P20}. TISSUE SPECIFICITY: Highly expressed in the gastrointestinal tract, predominantly in colonic myofibroblasts and in colonic epithelial and endothelial cells. Within the intestinal mucosa, highly expressed by goblet cells. Also expressed in hepatocytes and in immune cells, including CD4(+) and CD8(+) T-cells, dendritic cells, mastocytes and peritoneal macrophages, as well as in lung, kidney, bladder and gonads. {ECO:0000269|PubMed:21543645, ECO:0000269|PubMed:21565393, ECO:0000269|PubMed:21593405, ECO:0000269|PubMed:22763455, ECO:0000269|PubMed:24581500}. +Q3TL44 NLRX1_MOUSE NLR family member X1 975 107,831 Chain (1); Domain (3); Nucleotide binding (1); Region (2); Repeat (8); Sequence conflict (3); Transit peptide (1) FUNCTION: Participates in antiviral signaling. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250}. SUBUNIT: Homohexamer. Interacts with MAVS (By similarity). {ECO:0000250}. DOMAIN: The LRRCT domain mediates homodimerization and LRRNT mediates trimerization of the dimers. {ECO:0000250}. +Q9DA75 NLS1_MOUSE Sodium-dependent lysophosphatidylcholine symporter 1 (NLS1) (Sodium-dependent LPC symporter 1) (Major facilitator superfamily domain-containing protein 2A) 534 58,984 Chain (1); Glycosylation (2); Mutagenesis (2); Sequence conflict (1); Topological domain (12); Transmembrane (11) TRANSMEM 46 66 Helical. {ECO:0000255}.; TRANSMEM 68 88 Helical. {ECO:0000255}.; TRANSMEM 115 135 Helical. {ECO:0000255}.; TRANSMEM 147 167 Helical. {ECO:0000255}.; TRANSMEM 248 268 Helical. {ECO:0000255}.; TRANSMEM 302 322 Helical. {ECO:0000255}.; TRANSMEM 336 356 Helical. {ECO:0000255}.; TRANSMEM 362 382 Helical. {ECO:0000255}.; TRANSMEM 385 405 Helical. {ECO:0000255}.; TRANSMEM 429 449 Helical. {ECO:0000255}.; TRANSMEM 476 496 Helical. {ECO:0000255}. TOPO_DOM 1 45 Extracellular. {ECO:0000255}.; TOPO_DOM 67 67 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 89 114 Extracellular. {ECO:0000255}.; TOPO_DOM 136 146 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 168 247 Extracellular. {ECO:0000255}.; TOPO_DOM 269 301 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 323 335 Extracellular. {ECO:0000255}.; TOPO_DOM 357 361 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 383 384 Extracellular. {ECO:0000255}.; TOPO_DOM 406 428 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 450 475 Extracellular. {ECO:0000255}.; TOPO_DOM 497 534 Cytoplasmic. {ECO:0000255}. FUNCTION: Sodium-dependent lysophosphatidylcholine (LPC) symporter, which plays an essential role for blood-brain barrier formation and function (PubMed:24828044, PubMed:24828040). Specifically expressed in endothelium of the blood-brain barrier of micro-vessels and transports LPC into the brain. Transport of LPC is essential because it constitutes the major mechanism by which docosahexaenoic acid (DHA), an omega-3 fatty acid that is essential for normal brain growth and cognitive function, enters the brain. Transports LPC carrying long-chain fatty acids such LPC oleate and LPC palmitate with a minimum acyl chain length of 14 carbons. Does not transport docosahexaenoic acid in unesterified fatty acid (PubMed:24828044). Specifically required for blood-brain barrier formation and function, probably by mediating lipid transport. Not required for central nervous system vascular morphogenesis (PubMed:24828040). Acts as a transporter for tunicamycin, an inhibitor of asparagine-linked glycosylation. {ECO:0000269|PubMed:18694395, ECO:0000269|PubMed:23209793, ECO:0000269|PubMed:24828040, ECO:0000269|PubMed:24828044}. PTM: N-glycosylated. {ECO:0000269|PubMed:23209793}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23209793, ECO:0000269|PubMed:24828040}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:18694395}; Multi-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Widely expressed. Exhibits an oscillatory pattern of expression in brown adipose tissue and liver consistent with a circadian rhythm. Enriched in brain micro-vessels, where it is specifically present in endothelium constituting the blood-brain barrier (at protein level) (PubMed:24828044, PubMed:24828040). {ECO:0000269|PubMed:18694395, ECO:0000269|PubMed:23209793, ECO:0000269|PubMed:24828040, ECO:0000269|PubMed:24828044}. +Q8BZ39 NMUR2_MOUSE Neuromedin-U receptor 2 (NMU-R2) 395 44,827 Chain (1); Disulfide bond (1); Glycosylation (3); Sequence conflict (1); Topological domain (8); Transmembrane (7) TRANSMEM 42 62 Helical; Name=1. {ECO:0000255}.; TRANSMEM 75 95 Helical; Name=2. {ECO:0000255}.; TRANSMEM 116 138 Helical; Name=3. {ECO:0000255}.; TRANSMEM 158 178 Helical; Name=4. {ECO:0000255}.; TRANSMEM 213 233 Helical; Name=5. {ECO:0000255}.; TRANSMEM 258 278 Helical; Name=6. {ECO:0000255}.; TRANSMEM 294 314 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 41 Extracellular. {ECO:0000255}.; TOPO_DOM 63 74 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 96 115 Extracellular. {ECO:0000255}.; TOPO_DOM 139 157 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 179 212 Extracellular. {ECO:0000255}.; TOPO_DOM 234 257 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 279 293 Extracellular. {ECO:0000255}.; TOPO_DOM 315 395 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for the neuromedin-U and neuromedin-S neuropeptides. {ECO:0000250, ECO:0000269|PubMed:12217421}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed primarily in brain tissues, more specifically in medulla and spinal cord. Widespread distribution in peripheral tissues. {ECO:0000269|PubMed:12217421}. +Q9QXK8 NMU_MOUSE Neuromedin-U [Cleaved into: Neuromedin precursor-related peptide 36 (NURP36); Neuromedin precursor-related peptide 33 (NURP33); Neuromedin-U-23 (NmU-23)] 174 19,429 Modified residue (2); Peptide (3); Propeptide (2); Signal peptide (1) FUNCTION: Neuromedin-U-23: Ligand for receptors NMUR1 and NMUR2 (By similarity). Stimulates muscle contractions of specific regions of the gastrointestinal tract. {ECO:0000250|UniProtKB:P12760}.; FUNCTION: Neuromedin precursor-related peptide 33: Does not function as a ligand for either NMUR1 or NMUR2. Indirectly induces prolactin release although its potency is much lower than that of neuromedin precursor-related peptide 36. {ECO:0000250|UniProtKB:P12760}.; FUNCTION: Neuromedin precursor-related peptide 36: Does not function as a ligand for either NMUR1 or NMUR2. Indirectly induces prolactin release from lactotroph cells in the pituitary gland, probably via the hypothalamic dopaminergic system. {ECO:0000250|UniProtKB:P12760}.; FUNCTION: Stimulates muscle contractions of specific regions of the gastrointestinal tract. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. +Q924H2 MED15_MOUSE Mediator of RNA polymerase II transcription subunit 15 (Mediator complex subunit 15) (Positive cofactor 2 glutamine/Q-rich-associated protein) (PC2 glutamine/Q-rich-associated protein) (mPcqap) 789 86,607 Chain (1); Compositional bias (7); Frameshift (1); Modified residue (2); Motif (1); Region (1); Sequence conflict (5) FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. Required for cholesterol-dependent gene regulation. Positively regulates the Nodal signaling pathway (By similarity). {ECO:0000250}. PTM: Ubiquitinated by TRIM11, leading to proteasomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Component of the Mediator complex, which is composed of MED1, MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L, MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23, MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8 subunits form a distinct module termed the CDK8 module. Mediator containing the CDK8 module is less active than Mediator lacking this module in supporting transcriptional activation. Individual preparations of the Mediator complex lacking one or more distinct subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and TRAP. Interacts with SMAD2, SMAD3, SREBF1 and SREBF2. Interacts with WWTR1 (By similarity). Interacts with TRIM11 (By similarity). {ECO:0000250}. +Q6PGF3 MED16_MOUSE Mediator of RNA polymerase II transcription subunit 16 (Mediator complex subunit 16) (Thyroid hormone receptor-associated protein 5) (Thyroid hormone receptor-associated protein complex 95 kDa component) (Trap95) (Vitamin D3 receptor-interacting protein complex 92 kDa component) (DRIP92) 828 91,786 Chain (1); Repeat (5); Sequence conflict (3) FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Component of the Mediator complex, which is composed of MED1, MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L, MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23, MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8 subunits form a distinct module termed the CDK8 module. Mediator containing the CDK8 module is less active than Mediator lacking this module in supporting transcriptional activation. Individual preparations of the Mediator complex lacking one or more distinct subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and TRAP (By similarity). {ECO:0000250}. +Q9DB91 MED29_MOUSE Mediator of RNA polymerase II transcription subunit 29 (Intersex-like protein) (Mediator complex subunit 29) 199 21,011 Chain (1); Compositional bias (1); Initiator methionine (1); Modified residue (1) FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the Mediator complex, which is composed of MED1, MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L, MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23, MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8 subunits form a distinct module termed the CDK8 module. Mediator containing the CDK8 module is less active than Mediator lacking this module in supporting transcriptional activation. Individual preparations of the Mediator complex lacking one or more distinct subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and TRAP. Associates with the MED18/MED20 heteromer (By similarity). {ECO:0000250}. +Q7TN02 MED26_MOUSE Mediator of RNA polymerase II transcription subunit 26 (Cofactor required for Sp1 transcriptional activation subunit 7) (CRSP complex subunit 7) (Mediator complex subunit 26) 588 64,680 Chain (1); Compositional bias (1); Domain (1); Modified residue (2); Sequence conflict (2) FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional pre-initiation complex with RNA polymerase II and the general transcription factors (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Component of the Mediator complex, which is composed of MED1, MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L, MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23, MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8 subunits form a distinct module termed the CDK8 module. Mediator containing the CDK8 module is less active than Mediator lacking this module in supporting transcriptional activation. Individual preparations of the Mediator complex lacking one or more distinct subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and TRAP (By similarity). Interacts with CEBPB (when not methylated)(PubMed:20111005). {ECO:0000250|UniProtKB:O95402, ECO:0000269|PubMed:20111005}. +Q9DB40 MED27_MOUSE Mediator of RNA polymerase II transcription subunit 27 (Cofactor required for Sp1 transcriptional activation subunit 8) (CRSP complex subunit 8) (Mediator complex subunit 27) 311 35,298 Alternative sequence (2); Chain (1); Erroneous initiation (1); Modified residue (2) FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the Mediator complex, which is composed of MED1, MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L, MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23, MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8 subunits form a distinct module termed the CDK8 module. Mediator containing the CDK8 module is less active than Mediator lacking this module in supporting transcriptional activation. Individual preparations of the Mediator complex lacking one or more distinct subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and TRAP (By similarity). {ECO:0000250}. +Q920D3 MED28_MOUSE Mediator of RNA polymerase II transcription subunit 28 (Mediator complex subunit 28) 178 19,538 Chain (1); Coiled coil (1); Sequence conflict (1) FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. May be part of a complex containing NF2/merlin that participates in cellular signaling to the actin cytoskeleton downstream of tyrosine kinase signaling pathways (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}. Note=May be also cytoplasmic and membrane-associated. {ECO:0000250}. SUBUNIT: Component of the Mediator complex, which is composed of MED1, MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L, MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23, MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8 subunits form a distinct module termed the CDK8 module. Mediator containing the CDK8 module is less active than Mediator lacking this module in supporting transcriptional activation. Individual preparations of the Mediator complex lacking one or more distinct subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and TRAP. Forms a ternary complex with NF2/merlin and GRB2. Binds to actin (By similarity). {ECO:0000250}. +Q9CZB6 MED7_MOUSE Mediator of RNA polymerase II transcription subunit 7 (Cofactor required for Sp1 transcriptional activation subunit 9) (CRSP complex subunit 9) (Mediator complex subunit 7) 233 27,205 Chain (1); Compositional bias (2); Cross-link (2); Modified residue (1); Sequence conflict (7) FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the Mediator complex, which is composed of MED1, MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L, MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23, MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8 subunits form a distinct module termed the CDK8 module. Mediator containing the CDK8 module is less active than Mediator lacking this module in supporting transcriptional activation. Individual preparations of the Mediator complex lacking one or more distinct subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and TRAP (By similarity). {ECO:0000250}. +O55087 MEF2B_MOUSE Myocyte-specific enhancer factor 2B 349 37,435 Alternative sequence (5); Chain (1); DNA binding (1); Domain (1); Sequence conflict (2) FUNCTION: Transcriptional activator which binds specifically to the MEF2 element, 5'-YTA[AT](4)TAR-3', found in numerous muscle-specific genes. Activates transcription via this element. May be involved in muscle-specific and/or growth factor-related transcription. {ECO:0000269|PubMed:8668199, ECO:0000269|PubMed:9443808}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251}. SUBUNIT: Heterodimer. Interacts with HDAC9 (By similarity). Interacts with HDAC7. {ECO:0000250, ECO:0000269|PubMed:11585834}. TISSUE SPECIFICITY: Highest expression found in embryonic heart and skeletal muscle. Low levels found in adult spleen, lung and testis while no expression is found in adult heart, brain or skeletal muscle. {ECO:0000269|PubMed:7646512, ECO:0000269|PubMed:8668199, ECO:0000269|PubMed:9443808}. +Q8CFN5 MEF2C_MOUSE Myocyte-specific enhancer factor 2C (Myocyte enhancer factor 2C) 474 51,278 Alternative sequence (5); Beta strand (3); Chain (1); Compositional bias (2); Cross-link (1); DNA binding (1); Domain (1); Helix (3); Modified residue (21); Mutagenesis (7); Region (2); Sequence conflict (3); Site (1) FUNCTION: Transcription activator which binds specifically to the MEF2 element present in the regulatory regions of many muscle-specific genes. Controls cardiac morphogenesis and myogenesis, and is also involved in vascular development. May also be involved in neurogenesis and in the development of cortical architecture. Isoform 3 and isoform 4, which lack the repressor domain, are more active than isoform 1, isoform 2 and isoform 5 (By similarity). Plays an essential role in hippocampal-dependent learning and memory by suppressing the number of excitatory synapses and thus regulating basal and evoked synaptic transmission. Crucial for normal neuronal development, distribution, and electrical activity in the neocortex. Necessary for proper development of megakaryocytes and platelets and for bone marrow B-lymphopoiesis. Required for B-cell survival and proliferation in response to BCR stimulation, efficient IgG1 antibody responses to T-cell-dependent antigens and for normal induction of germinal center B-cells. {ECO:0000250|UniProtKB:Q06413, ECO:0000269|PubMed:18086704, ECO:0000269|PubMed:18438409, ECO:0000269|PubMed:18599437, ECO:0000269|PubMed:18599438, ECO:0000269|PubMed:19211936, ECO:0000269|PubMed:9162005, ECO:0000269|PubMed:9778514}. PTM: Phosphorylation on Ser-59 enhances DNA binding activity (By similarity). Phosphorylation on Ser-396 is required for Lys-391 sumoylation and inhibits transcriptional activity. {ECO:0000250, ECO:0000269|PubMed:8663403}.; PTM: Acetylated by p300 on several sites in diffentiating myocytes (By similarity). Acetylation on Lys-4 increases DNA binding and transactivation. {ECO:0000250, ECO:0000269|PubMed:18086704}.; PTM: Sumoylated on Lys-391 with SUMO2 but not by SUMO1 represses transcriptional activity. {ECO:0000250}.; PTM: Proteolytically cleaved in cerebellar granule neurons, probably by caspase 7, following neurotoxicity. Preferentially cleaves the CDK5-mediated hyperphosphorylated form which leads to neuron apoptosis and transcriptional inactivation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:A0A096MJY4}. Cytoplasm, sarcoplasm {ECO:0000250|UniProtKB:A0A096MJY4}. SUBUNIT: Forms a complex with class II HDACs in undifferentiating cells. On myogenic differentiation, HDACs are released into the cytoplasm allowing MEF2s to interact with other proteins for activation. Interacts with EP300 in differentiating cells; the interaction acetylates MEF2C leading to increased DNA binding and activation (By similarity). Interacts with HDAC7 and CARM1 (PubMed:11279209, PubMed:11713257). Interacts with HDAC4, HDAC7 AND HDAC9; the interaction with HDACs represses transcriptional activity (By similarity). Interacts with LPIN1 (PubMed:19753306). Interacts with MYOCD (PubMed:16818234). Interacts with AKAP13 (PubMed:20139090). Interacts with FOXK1; the interaction inhibits MEF2C transactivation activity (PubMed:22956541). Interacts (via N-terminus) with HABP4; this interaction decreases DNA-binding activity of MEF2C in myocardial cells in response to mechanical stress (By similarity). {ECO:0000250|UniProtKB:A0A096MJY4, ECO:0000250|UniProtKB:Q06413, ECO:0000269|PubMed:11279209, ECO:0000269|PubMed:11713257, ECO:0000269|PubMed:16818234, ECO:0000269|PubMed:19753306, ECO:0000269|PubMed:20139090, ECO:0000269|PubMed:22956541}. DOMAIN: The beta domain, missing in a number of isoforms, is required for enhancement of transcriptional activity. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed though mainly restricted to skeletal and cardiac muscle, brain, neurons and lymphocytes. Beta domain-lacking isoforms are the most predominantly expressed in all tissues including skeletal and cardiac muscle and brain. Only brain expresses all isoforms. Expression occurs primarily in the internal granule cell layer of the olfactory bulb, cortex, thalamus, hippocampus and cerebellum. Low levels in the cerebellum and hindbrain. Expressed throughout the cortex, including the frontal and entorhinal cortex, dentate gyrus, and basolateral amygdala. Selectively expressed in B-cells but not in T-cells, and its expression increases as B-cells mature. {ECO:0000269|PubMed:15340086, ECO:0000269|PubMed:15834131, ECO:0000269|PubMed:18438409, ECO:0000269|PubMed:18599438, ECO:0000269|PubMed:8506376, ECO:0000269|PubMed:9013788}. +Q63943 MEF2D_MOUSE Myocyte-specific enhancer factor 2D 514 55,065 Alternative sequence (2); Chain (1); Compositional bias (4); Cross-link (1); DNA binding (1); Domain (1); Modified residue (13); Mutagenesis (5); Region (1); Sequence conflict (1); Site (1) FUNCTION: Transcriptional activator which binds specifically to the MEF2 element, 5'-YTA[AT](4)TAR-3', found in numerous muscle-specific, growth factor- and stress-induced genes. Mediates cellular functions not only in skeletal and cardiac muscle development, but also in neuronal differentiation and survival. Plays diverse roles in the control of cell growth, survival and apoptosis via p38 MAPK signaling in muscle-specific and/or growth factor-related transcription. Plays a critical role in the regulation of neuronal apoptosis. {ECO:0000269|PubMed:16407541, ECO:0000269|PubMed:18299387}. PTM: Phosphorylated on Ser-437 is which is required for Lys-432 sumoylation and inhibits transcriptional activity. Phosphorylation on this residue by CDK5 is dependent on p35 and calpains. Phosphorylated by PKA at Ser-121 and Ser-190 represses transcriptional activity in embryonic and postnatal skeletal muscle, and stabilizes protein levels. No in vitro phosphorylation by PKA on Thr-20. Phosphorylated and activated by CaMK4 (By similarity). {ECO:0000250}.; PTM: Acetylated on Lys-432 by CREBBP. Acetylated by EP300. Deacetylated by SIRT1 and HDAC3 (By similarity). {ECO:0000250|UniProtKB:Q14814}.; PTM: Sumoylated on Lys-432 with SUMO2 but not SUMO1; which inhibits transcriptional activity and myogenic activity. Desumoylated by SENP3 (By similarity). {ECO:0000250}.; PTM: Proteolytically cleaved in cerebellar granule neurons by caspase 7 following neurotoxicity. Preferentially cleaves the CDK5-mediated hyperphosphorylated form which leads to neuron apoptosis and transcriptional inactivation. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251, ECO:0000269|PubMed:18299387}. Note=Translocated by HDAC4 to nuclear dots. {ECO:0000250}. SUBUNIT: Forms a complex with class II HDACs in undifferentiating cells. On myogenic differentiation, HDACs are released into the cytoplasm allowing MEF2s to interact with other proteins for activation. Interacts with HDAC4 (in undifferentiating cells); the interaction translocates MEF2D to nuclear dots. Forms a heterodimer with MEF2A (By similarity). Interacts with MAPK7; the interaction phosphorylates but does not activate MEF2D (By similarity). Interacts with MYOG. Interacts with CCAR2 and HDAC3 (By similarity). {ECO:0000250|UniProtKB:O89038, ECO:0000250|UniProtKB:Q14814, ECO:0000269|PubMed:16424906, ECO:0000269|PubMed:18299387}. TISSUE SPECIFICITY: Widely expressed though mainly restricted to skeletal and cardiac muscle, brain, neurons and lymphocytes. Differentially expressed depending on if isoforms contain the beta domain or not, with the total expression of the beta domain-lacking isoforms vastly exceding that of the beta domain-containing isoforms. Isoforms containing the beta domain are expressed primarily in skeletal and cardiac muscle and in brain. Also present in lung and testis. Splicing to include the beta domain is induced in differentiating myocytes. Isoforms lacking the beta domain are expressed less abundantly in skeletal muscle, brain and lymphocytes, and are uniquely found in ovary, liver, spleen and kidney. In embryos, the beta domain-containing and beta domain-lacking isoforms are equally expressed. Also expressed cerebellar granule neurons and other regions of the CNS. Highest levels in the olfactory bulb, cortex, hippocampus, thalamus and cerebellum. {ECO:0000269|PubMed:15834131, ECO:0000269|PubMed:16407541, ECO:0000269|PubMed:9013788}. +Q9JJ26 MEFV_MOUSE Pyrin (Marenostrin) 767 86,409 Chain (1); Coiled coil (1); Domain (1); Region (1); Sequence conflict (2); Zinc finger (1) FUNCTION: Involved in the regulation of innate immunity and the inflammatory response in response to IFNG/IFN-gamma. Organizes autophagic machinery by serving as a platform for the assembly of ULK1, Beclin 1/BECN1, ATG16L1, and ATG8 family members and recognizes specific autophagy targets, thus coordinating target recognition with assembly of the autophagic apparatus and initiation of autophagy. Acts as an autophagy receptor for the degradation of several inflammasome components, including CASP1, NLRP1 and NLRP3, hence preventing excessive IL1B- and IL18-mediated inflammation. However, it may also have a positive effect in the inflammatory pathway. In different experimental systems, it has been shown to activate IL1B production. It has also been shown to be required for PSTPIP1-induced PYCARD oligomerization and for formation of inflammasomes. Recruits PSTPIP1 to inflammasomes, and is required for PSTPIP1 oligomerization. {ECO:0000250|UniProtKB:O15553}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell projection, ruffle {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Cytoplasm {ECO:0000250|UniProtKB:O15553}. Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:O15553}. Nucleus {ECO:0000250}. Note=Associated with microtubules and with the filamentous actin of perinuclear filaments and peripheral lamellar ruffles. In pre-apoptotic cells, colocalizes with PYCARD/ASC in large specks (pyroptosomes). In migrating monocytes, strongly polarized at the leading edge of the cell where it colocalizes with polymerizing actin and PYCARD/ASC (By similarity). {ECO:0000250}. SUBUNIT: Homotrimer. Interacts (via the B box-type zinc finger) with PSTPIP1. Interacts (via the B30.2/SPRY domain) with several components of the inflammasome complex, including CASP1 p20 and p10 subunits, CASP5, PYCARD, NLRP1, NLRP2 AND NLRP3, as well as with unprocessed IL1B; this interaction may lead to autophagic degradation of these proteins. Interacts with NFKBIA and RELA. Interacts weakly with VASP and ACTR3. Interacts with active ULK1 (phosphorylated on 'Ser-317') and BECN1 simultaneously. Also interacts with ATG16L1 (via WD repeats), and with ATG8 family members, including GABARAP, GABARAPL1 and, to a lesser extent, GABARAPL2, MAP1LC3A/LC3A and MAP1LC3C/LC3C. Interacts with TRIM21. {ECO:0000250|UniProtKB:O15553}. DOMAIN: The B box-type zinc finger interacts, possibly intramolecularly, with the pyrin domain; this may be an autoinhibitory mechanism released by PSTPIP1 binding. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in spleen peripheral blood granulocytes. Not expressed in lymphocytes, thymus, testis, ovary, heart, brain, lung, liver, kidney and muscle. {ECO:0000269|PubMed:10818206}. +Q6DIB5 MEG10_MOUSE Multiple epidermal growth factor-like domains protein 10 (Multiple EGF-like domains protein 10) 1147 122,972 Chain (1); Compositional bias (1); Disulfide bond (47); Domain (16); Glycosylation (2); Modified residue (1); Region (2); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 858 878 Helical. {ECO:0000255}. TOPO_DOM 26 857 Extracellular. {ECO:0000255}.; TOPO_DOM 879 1147 Cytoplasmic. {ECO:0000255}. FUNCTION: Membrane receptor involved in phagocytosis by macrophages and astrocytes of apoptotic cells. Receptor for C1q, an eat-me signal, that binds phosphatidylserine expressed on the surface of apoptotic cells (PubMed:27170117). Cooperates with ABCA1 within the process of engulfment (By similarity). Promotes the formation of large intracellular vacuoles and may be responsible for the uptake of amyloid-beta peptides (PubMed:20828568). Necessary for astrocyte-dependent apoptotic neuron clearance in the developing cerebellum (PubMed:27170117). Plays role in muscle cell proliferation, adhesion and motility. Is also an essential factor in the regulation of myogenesis. Controls the balance between skeletal muscle satellite cells proliferation and differentiation through regulation of the notch signaling pathway (PubMed:28498977). May also function in the mosaic spacing of specific neuron subtypes in the retina through homotypic retinal neuron repulsion. Mosaics provide a mechanism to distribute each cell type evenly across the retina, ensuring that all parts of the visual field have access to a full set of processing elements (PubMed:22407321). {ECO:0000250|UniProtKB:Q96KG7, ECO:0000269|PubMed:18056409, ECO:0000269|PubMed:20828568, ECO:0000269|PubMed:22407321, ECO:0000269|PubMed:27170117, ECO:0000269|PubMed:28498977}. PTM: Ubiquitinated; mono- and polyubiquitinated forms are detected. {ECO:0000250|UniProtKB:Q96KG7}.; PTM: Phosphorylated on tyrosine residues. Phosphorylation at Tyr-1030 may be important for muscle cell proliferation. {ECO:0000250|UniProtKB:Q96KG7}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17643423, ECO:0000269|PubMed:28498977}; Single-pass type I membrane protein {ECO:0000269|PubMed:17643423}. Cell projection, phagocytic cup {ECO:0000250|UniProtKB:Q96KG7}. Note=Forms an irregular, mosaic-like adhesion pattern in region of the cell surface that becomes firmely fixed to the substrate. Expressed at the cell surface in clusters around cell corpses during engulfment. During the engulfment of apoptotic thymocytes, recruited at the bottom of the forming phagocytic cup. Colocalizes with ABCA1 in absence of any phagocytic challenge. Does not localize within lamellipodia. Does not localize with MEGF11 (By similarity). Enriched at the sites of contact with apoptotic thymocyte cells. {ECO:0000250|UniProtKB:Q96KG7}. SUBUNIT: Homopolymer (Probable). Interacts with GULP1 and ABCA1. Interacts with AP2M1. Does not interact with MEGF11 (By similarity). Binds with high affinity to complement C1q (By similarity). Interacts (via the cytoplasmic domain) with NOTCH1 (via NICD domain) (PubMed:28498977). {ECO:0000250|UniProtKB:Q96KG7, ECO:0000269|PubMed:28498977, ECO:0000305}. DOMAIN: The EMI and EGF-like domains work in concert to promote self-assembly. TISSUE SPECIFICITY: Expressed in cerebellum (at protein level). Expressed in kidney, stellate cells of the cerebellum and macrophage cell lines. {ECO:0000269|PubMed:17205124, ECO:0000269|PubMed:17643423, ECO:0000269|PubMed:18056409}. +Q9D114 MESH1_MOUSE Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase MESH1 (EC 3.1.7.2) (HD domain-containing protein 3) (Metazoan SpoT homolog 1) (MESH1) (Penta-phosphate guanosine-3'-pyrophosphohydrolase) ((ppGpp)ase) 179 20,262 Active site (2); Chain (1); Domain (1); Initiator methionine (1); Metal binding (4); Modified residue (4) FUNCTION: ppGpp hydrolyzing enzyme involved in starvation response. {ECO:0000250}. +Q8R2R5 LRC61_MOUSE Leucine-rich repeat-containing protein 61 259 27,964 Chain (1); Domain (1); Repeat (3); Sequence conflict (4) +Q8K1T1 LRC25_MOUSE Leucine-rich repeat-containing protein 25 (Monocyte and plasmacytoid-activated protein) 297 32,673 Chain (1); Glycosylation (4); Modified residue (4); Repeat (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 170 190 Helical. {ECO:0000255}. TOPO_DOM 26 169 Extracellular. {ECO:0000255}.; TOPO_DOM 191 297 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a role in the inhibition of RLR-mediated type I interferon signaling pathway by targeting DDX58/RIG-I for autophagic degradation. Interacts specifically with ISG15-associated DDX58 to promote interaction between DDX58 and the autophagic cargo receptor p62/SQSTM1 to mediate DDX58 degradation via selective autophagy. Plays also a role in the inhibition of NF-kappa-B signaling pathway and inflammatory response by promoting the degradation of p65/RELA. {ECO:0000250|UniProtKB:Q8N386}. SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q8N386}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q8N386}. Cytoplasm {ECO:0000250|UniProtKB:Q8N386}. SUBUNIT: Interacts with DDX58. Interacts with SQSTM1. Interacts with p65/RELA; this interaction promotes the degradation of RELA through autophagy. {ECO:0000250|UniProtKB:Q8N386}. +P0C192 LRC4B_MOUSE Leucine-rich repeat-containing protein 4B (Netrin-G3 ligand) (NGL-3) 709 76,156 Beta strand (20); Chain (1); Compositional bias (3); Disulfide bond (1); Domain (3); Glycosylation (9); Helix (7); Modified residue (1); Repeat (9); Sequence conflict (1); Signal peptide (1); Transmembrane (1); Turn (7) TRANSMEM 575 595 Helical. {ECO:0000255}. FUNCTION: Synaptic adhesion protein. Regulates the formation of excitatory synapses. The trans-synaptic adhesion between LRRC4B and PTPRF regulates the formation of excitatory synapses in a bidirectional manner (By similarity). {ECO:0000250}. PTM: N-glycosylated. O-glycosylated; contains sialic acid. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. Cell junction, synapse, presynaptic cell membrane {ECO:0000250}. SUBUNIT: Interacts with PTPRF (By similarity). Interacts with DLG4. {ECO:0000250, ECO:0000269|PubMed:16980967}. DOMAIN: The extreme C-terminus binds to the first 2 PDZ domains of DLG4. +P70193 LRIG1_MOUSE Leucine-rich repeats and immunoglobulin-like domains protein 1 (LIG-1) 1091 119,156 Chain (1); Compositional bias (1); Disulfide bond (6); Domain (5); Glycosylation (7); Repeat (15); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 797 817 Helical. {ECO:0000255}. TOPO_DOM 35 796 Extracellular. {ECO:0000255}.; TOPO_DOM 818 1091 Cytoplasmic. {ECO:0000255}. FUNCTION: Acts as a feedback negative regulator of signaling by receptor tyrosine kinases, through a mechanism that involves enhancement of receptor ubiquitination and accelerated intracellular degradation. {ECO:0000250|UniProtKB:Q96JA1}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12067728}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Interacts (via extracellular LRR and Ig-like domains) with EGFR/ERBB1, ERBB2, ERBB3 and ERBB4 (via extracellular domain). The physiological relevance of the interaction is controversial; LRIG1 may have low affinity for EGFR, and interaction may occur only when high levels of both proteins are present. {ECO:0000250|UniProtKB:Q96JA1}. DOMAIN: Contains LRR and Ig-domains that can mediate low-affinity interaction with EGFR. The LRRs and the Ig-domains are each sufficient for EGFR/ERBB1 binding. This interaction is abolished only when both the LRRs and the Ig-domains are deleted. {ECO:0000250|UniProtKB:Q96JA1}. TISSUE SPECIFICITY: Detected in brain (at protein level) (PubMed:12067728). Predominantly expressed in the brain, restricted to a small subset of glial cells, such as Bergmann glial cells of the cerebellum and glial cells in the nerve fiber layer of the olfactory bulb. Expressed also in the skin. Low expression is detected in the thymus and heart. No expression in the kidney, liver, lung or small intestine. {ECO:0000269|PubMed:12067728, ECO:0000269|PubMed:8798419}. +Q8BGR2 LRC8D_MOUSE Volume-regulated anion channel subunit LRRC8D (Leucine-rich repeat-containing protein 5) (Leucine-rich repeat-containing protein 8D) 859 98,113 Chain (1); Disulfide bond (1); Modified residue (3); Repeat (13); Sequence conflict (2); Topological domain (5); Transmembrane (4) TRANSMEM 23 43 Helical. {ECO:0000255}.; TRANSMEM 165 185 Helical. {ECO:0000255}.; TRANSMEM 320 340 Helical. {ECO:0000255}.; TRANSMEM 366 386 Helical. {ECO:0000255}. TOPO_DOM 1 22 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 44 164 Extracellular. {ECO:0000255}.; TOPO_DOM 186 319 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 341 365 Extracellular. {ECO:0000255}.; TOPO_DOM 387 859 Cytoplasmic. {ECO:0000255}. FUNCTION: Non-essential component of the volume-regulated anion channel (VRAC, also named VSOAC channel), an anion channel required to maintain a constant cell volume in response to extracellular or intracellular osmotic changes. The VRAC channel conducts iodide better than chloride and can also conduct organic osmolytes like taurine. Plays a redundant role in the efflux of amino acids, such as aspartate, in response to osmotic stress. Channel activity requires LRRC8A plus at least one other family member (LRRC8B, LRRC8C, LRRC8D or LRRC8E); channel characteristics depend on the precise subunit composition. {ECO:0000250|UniProtKB:Q7L1W4}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q7L1W4}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q7L1W4}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q7L1W4}. Note=In the absence of LRRC8A, resides primarily in a cytoplasmic compartment, probably the endoplasmic reticulum. Requires LRRC8A for expression at the cell membrane. {ECO:0000250|UniProtKB:Q7L1W4}. SUBUNIT: Heterohexamer (Probable). Oligomerizes with other LRRC8 proteins (LRRC8A, LRRC8B, LRRC8C and/or LRRC8E) to form a heterohexamer. In vivo, the subunit composition may depend primarily on expression levels, and heterooligomeric channels containing various proportions of the different LRRC8 proteins may coexist (PubMed:24782309). {ECO:0000269|PubMed:24782309, ECO:0000305}. +Q8BXA0 LRFN5_MOUSE Leucine-rich repeat and fibronectin type-III domain-containing protein 5 719 79,371 Alternative sequence (1); Beta strand (16); Chain (1); Disulfide bond (1); Domain (4); Erroneous initiation (1); Glycosylation (6); Helix (5); Repeat (7); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (4) TRANSMEM 530 550 Helical. {ECO:0000255}. TOPO_DOM 18 529 Extracellular. {ECO:0000255}.; TOPO_DOM 551 719 Cytoplasmic. {ECO:0000255}. FUNCTION: Cell adhesion molecule that mediates homophilic cell-cell adhesion in a Ca(2+)-independent manner. Promotes neurite outgrowth in hippocampal neurons (By similarity). {ECO:0000250}. PTM: Glycosylated. {ECO:0000269|PubMed:16828986}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:16828986}; Single-pass type I membrane protein {ECO:0000269|PubMed:16828986}. SUBUNIT: Can form heteromeric complexes with LRFN1, LRFN2, LRFN3 and LFRN4 (By similarity). Able to form homomeric complexes across cell junctions, between adjacent cells (By similarity). Does not interact with DLG1, DLG2 or DLG3 (By similarity). Does not interact with DLG4. {ECO:0000250}. DOMAIN: Lacks a cytoplasmic PDZ-binding motif, which has been implicated in function of related LRFN proteins. TISSUE SPECIFICITY: Predominantly expressed in the brain, with a weak, but broad expression in the cerebral cortex and diencephalic nuclei. Strongly expressed in both the pyramidal layer and the dentate gyrus of the hippocampus. Also detected in other parts of the central nervous system, including the olfactory bulb, pons, cerebellum, and medulla oblongata, as well as in the peripheral nervous system, such as the ganglia of cranial nerves and the dorsal root ganglion during gestation. {ECO:0000269|PubMed:16828986}. +Q8BUJ9 LRP12_MOUSE Low-density lipoprotein receptor-related protein 12 (LRP-12) 858 94,551 Alternative sequence (1); Chain (1); Disulfide bond (18); Domain (7); Frameshift (1); Glycosylation (5); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 493 513 Helical. {ECO:0000255}. TOPO_DOM 33 492 Extracellular. {ECO:0000255}.; TOPO_DOM 514 858 Cytoplasmic. {ECO:0000255}. FUNCTION: Probable receptor, which may be involved in the internalization of lipophilic molecules and/or signal transduction. May act as a tumor suppressor (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Membrane, coated pit {ECO:0000250}. SUBUNIT: May interact with RACK1, ZFYVE9 and NMRK2. {ECO:0000250}. +Q8VCH9 LRC3B_MOUSE Leucine-rich repeat-containing protein 3B (Leucine-rich repeat protein LRP15) 259 29,261 Chain (1); Domain (2); Glycosylation (2); Repeat (3); Signal peptide (1); Transmembrane (1) TRANSMEM 205 225 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q91ZX7 LRP1_MOUSE Prolow-density lipoprotein receptor-related protein 1 (LRP-1) (Alpha-2-macroglobulin receptor) (A2MR) (CD antigen CD91) [Cleaved into: Low-density lipoprotein receptor-related protein 1 85 kDa subunit (LRP-85); Low-density lipoprotein receptor-related protein 1 515 kDa subunit (LRP-515); Low-density lipoprotein receptor-related protein 1 intracellular domain (LRPICD)] 4545 504,742 Chain (4); Disulfide bond (159); Domain (53); Glycosylation (51); Metal binding (18); Modified residue (6); Motif (2); Region (1); Repeat (34); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 4425 4445 Helical. {ECO:0000255}. TOPO_DOM 20 4424 Extracellular. {ECO:0000255}.; TOPO_DOM 4446 4545 Cytoplasmic. {ECO:0000255}. FUNCTION: Endocytic receptor involved in endocytosis and in phagocytosis of apoptotic cells. Required for early embryonic development (PubMed:1423604). Involved in cellular lipid homeostasis. Involved in the plasma clearance of chylomicron remnants and activated LRPAP1 (alpha 2-macroglobulin), as well as the local metabolism of complexes between plasminogen activators and their endogenous inhibitors. May modulate cellular events, such as APP metabolism, kinase-dependent intracellular signaling, neuronal calcium signaling as well as neurotransmission. Acts as an alpha-2-macroglobulin receptor (By similarity). {ECO:0000250|UniProtKB:Q07954, ECO:0000269|PubMed:1423604}.; FUNCTION: (Microbial infection) Functions as a receptor for Vibrio cholerae cholix toxin and for Pseudomonas aeruginosa exotoxin A. {ECO:0000269|PubMed:1618748, ECO:0000269|PubMed:18276581}. PTM: Phosphorylated on serine and threonine residues. {ECO:0000250}.; PTM: Phosphorylated on tyrosine residues upon stimulation with PDGF. Tyrosine phosphorylation promotes interaction with SHC1 (By similarity). {ECO:0000250}.; PTM: Cleaved into a 85 kDa membrane-spanning subunit (LRP-85) and a 515 kDa large extracellular domain (LRP-515) that remains non-covalently associated. Gamma-secretase-dependent cleavage of LRP-85 releases the intracellular domain from the membrane (By similarity). {ECO:0000250|UniProtKB:Q07954}. SUBCELLULAR LOCATION: Low-density lipoprotein receptor-related protein 1 85 kDa subunit: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Membrane, coated pit {ECO:0000250}.; SUBCELLULAR LOCATION: Low-density lipoprotein receptor-related protein 1 515 kDa subunit: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Extracellular side {ECO:0000250}. Membrane, coated pit {ECO:0000250}.; SUBCELLULAR LOCATION: Low-density lipoprotein receptor-related protein 1 intracellular domain: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=After cleavage, the intracellular domain (LRPICD) is detected both in the cytoplasm and in the nucleus. {ECO:0000250}. SUBUNIT: Heterodimer of an 85-kDa membrane-bound carboxyl subunit and a non-covalently attached 515-kDa N-terminal subunit. Found in a complex with PID1/PCLI1, LRP1 and CUBNI. Interacts with SNX17, PID1/PCLI1, PDGF and CUBN. The intracellular domain interacts with SHC1, GULP1 and DAB1. Interacts with LRPAP1 (By similarity). Intracellular domain interacts with MAFB. Can weakly interact (via NPXY motif) with DAB2 (via PID domain); the interaction is enhanced by tyrosine phosphorylation of the NPXY motif. Interacts with bacterial exotoxins. {ECO:0000250, ECO:0000269|PubMed:11247302, ECO:0000269|PubMed:15135046}. +Q8BGA3 LRRT2_MOUSE Leucine-rich repeat transmembrane neuronal protein 2 515 58,816 Chain (1); Domain (2); Erroneous initiation (1); Glycosylation (4); Motif (1); Repeat (10); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 422 442 Helical. {ECO:0000255}. TOPO_DOM 34 421 Extracellular. {ECO:0000255}.; TOPO_DOM 443 515 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in the development and maintenance of excitatory synapse in the vertebrate nervous system. Regulates surface expression of AMPA receptors and instructs the development of functional glutamate release sites. Acts as a ligand for the presynaptic receptors NRXN1-A and NRXN1-B (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Cell junction, synapse, postsynaptic cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Localized to excitatory synapses. {ECO:0000250}. SUBUNIT: Interacts with DLG4 and NRXN1. {ECO:0000250}. DOMAIN: Synaptogenic effects are mediated by the extracellular LRR region. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in neuronal tissues. {ECO:0000269|PubMed:12676565}. +Q61810 LTBP3_MOUSE Latent-transforming growth factor beta-binding protein 3 (LTBP-3) 1253 134,363 Alternative sequence (2); Chain (1); Compositional bias (5); Disulfide bond (49); Domain (16); Erroneous initiation (1); Frameshift (1); Glycosylation (5); Sequence conflict (13); Signal peptide (1) FUNCTION: Key regulator of transforming growth factor beta (TGFB1, TGFB2 and TGFB3) that controls TGF-beta activation by maintaining it in a latent state during storage in extracellular space. Associates specifically via disulfide bonds with the Latency-associated peptide (LAP), which is the regulatory chain of TGF-beta, and regulates integrin-dependent activation of TGF-beta. {ECO:0000303|PubMed:10743502, ECO:0000303|PubMed:11104663}. PTM: Contains hydroxylated asparagine residues. {ECO:0000250|UniProtKB:Q14766}.; PTM: Two intrachain disulfide bonds from the TB3 domain are rearranged upon TGFB1 binding, and form interchain bonds with TGFB1 propeptide, anchoring it to the extracellular matrix. {ECO:0000250|UniProtKB:Q14766}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9NS15}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q9NS15}. Note=Secretion occurs after coexpression with TGFB1 and requires complexing with 'Cys-33' of the TGFB1 propeptide. {ECO:0000250|UniProtKB:Q9NS15}. SUBUNIT: Forms part of the large latent transforming growth factor beta (TGFB1) precursor complex; removal is essential for activation of complex. {ECO:0000269|PubMed:12062452, ECO:0000269|PubMed:9602168}. +Q6ZPK7 LST2_MOUSE Lateral signaling target protein 2 homolog (Zinc finger FYVE domain-containing protein 28) 905 99,787 Chain (1); Cross-link (1); Erroneous initiation (1); Modified residue (3); Zinc finger (1) FUNCTION: Negative regulator of epidermal growth factor receptor (EGFR) signaling. Acts by promoting EGFR degradation in endosomes when not monoubiquitinated (By similarity). {ECO:0000250}. PTM: Monoubiquitination at Lys-87 prevents binding to phosphatidylinositol 3-phosphate (PI3P) and localization to early endosome membranes. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol. Early endosome membrane. Note=Localizes to early endosome membrane in absence of Lys-87 monoubiquitination. Localizes to cytosol when monoubiquitinated (By similarity). {ECO:0000250}. SUBUNIT: Interacts with TRIM3. {ECO:0000250}. DOMAIN: The FYVE-type zinc finger mediates the interaction with phosphatidylinositol 3-phosphate (PI3P) and localization to early endosome membranes when not monoubiquitinated at Lys-87. {ECO:0000250}. TISSUE SPECIFICITY: Enriched in brain (at protein level). {ECO:0000269|PubMed:19460345}. +O88855 LT4R1_MOUSE Leukotriene B4 receptor 1 (LTB4-R 1) (LTB4-R1) 351 38,252 Chain (1); Glycosylation (2); Topological domain (8); Transmembrane (7) TRANSMEM 22 44 Helical; Name=1. {ECO:0000255}.; TRANSMEM 57 77 Helical; Name=2. {ECO:0000255}.; TRANSMEM 94 115 Helical; Name=3. {ECO:0000255}.; TRANSMEM 141 161 Helical; Name=4. {ECO:0000255}.; TRANSMEM 180 200 Helical; Name=5. {ECO:0000255}.; TRANSMEM 223 243 Helical; Name=6. {ECO:0000255}.; TRANSMEM 269 289 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 21 Extracellular. {ECO:0000255}.; TOPO_DOM 45 56 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 78 93 Extracellular. {ECO:0000255}.; TOPO_DOM 116 140 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 162 179 Extracellular. {ECO:0000255}.; TOPO_DOM 201 222 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 244 268 Extracellular. {ECO:0000255}.; TOPO_DOM 290 351 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for leukotriene B4, a potent chemoattractant involved in inflammation and immune response. PTM: Phosphorylated by GRK6 upon leukotriene B4 binding; which promotes desensitization. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Highly expressed on activated leukocytes, including eosinophils. +O08999 LTBP2_MOUSE Latent-transforming growth factor beta-binding protein 2 (LTBP-2) 1813 195,829 Chain (1); Compositional bias (1); Disulfide bond (75); Domain (24); Erroneous initiation (2); Glycosylation (8); Modified residue (1); Region (4); Sequence conflict (7); Signal peptide (1) FUNCTION: May play an integral structural role in elastic-fiber architectural organization and/or assembly. {ECO:0000250|UniProtKB:Q14767}. PTM: N-Glycosylated. {ECO:0000250|UniProtKB:Q14767}.; PTM: Contains hydroxylated asparagine residues. {ECO:0000250|UniProtKB:Q14766}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q14767}. SUBUNIT: Forms part of the large latent transforming growth factor beta precursor complex; removal is essential for activation of complex. Interacts with SDC4. Interacts (via C-terminal domain) with FBN1 (via N-terminal domain) in a Ca(+2)-dependent manner. {ECO:0000250|UniProtKB:Q14767}. TISSUE SPECIFICITY: Expressed in the anterior chamber of the eye. {ECO:0000269|PubMed:19361779}. +A2AHG0 LZTS3_MOUSE Leucine zipper putative tumor suppressor 3 (ProSAP-interacting protein 1) (ProSAPiP1) 700 74,986 Alternative sequence (3); Chain (1); Coiled coil (2); Compositional bias (1); Erroneous initiation (1); Modified residue (2); Sequence conflict (1) FUNCTION: May be involved in promoting the maturation of dendritic spines, probably via regulating SIPA1L1 levels at the postsynaptic density of synapses. {ECO:0000250|UniProtKB:Q8K1Q4}. SUBCELLULAR LOCATION: Cell junction, synapse {ECO:0000250|UniProtKB:Q8K1Q4}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250|UniProtKB:Q8K1Q4}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q8K1Q4}. Note=Detected at synapses, postsynaptic density, synaptic spines and dendrites. Rather found at excitatory than inhibitory synapses. {ECO:0000250|UniProtKB:Q8K1Q4}. SUBUNIT: Interacts (via C-terminus) with SHANK3 (via PDZ domain). Interacts (via coiled coil) with SIPA1L1. Can form homooligomers. {ECO:0000250|UniProtKB:Q8K1Q4}. +Q9DC69 NDUA9_MOUSE NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial (Complex I-39kD) (CI-39kD) (NADH-ubiquinone oxidoreductase 39 kDa subunit) 377 42,525 Beta strand (14); Chain (1); Helix (13); Modified residue (3); Sequence conflict (1); Transit peptide (1); Turn (6) FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. {ECO:0000250|UniProtKB:Q16795}. PTM: Acetylated on lysine residues. BLOC1S1 is required for acetylation. Acetylated by CLOCK in a circadian manner. {ECO:0000250|UniProtKB:Q16795}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:Q16795}. SUBUNIT: Complex I is composed of 45 different subunits. This a component of the hydrophobic protein fraction. Interacts with BLOC1S1 (By similarity). Interacts with SLC2A4. Interacts with CLOCK (By similarity). {ECO:0000250|UniProtKB:Q16795, ECO:0000250|UniProtKB:Q5BK63}. +Q61161 M4K2_MOUSE Mitogen-activated protein kinase kinase kinase kinase 2 (EC 2.7.11.1) (Germinal center kinase) (GCK) (MAPK/ERK kinase kinase kinase 2) (MEK kinase kinase 2) (MEKKK 2) (Rab8-interacting protein) 821 91,265 Active site (1); Binding site (1); Chain (1); Domain (2); Modified residue (2); Nucleotide binding (1); Region (3); Sequence conflict (1) FUNCTION: Serine/threonine-protein kinase which acts as an essential component of the MAP kinase signal transduction pathway (PubMed:8643544). Acts as a MAPK kinase kinase kinase (MAP4K) and is an upstream activator of the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway and to a lesser extent of the p38 MAPKs signaling pathway (By similarity). Required for the efficient activation of JNKs by TRAF6-dependent stimuli, including pathogen-associated molecular patterns (PAMPs) such as polyinosine-polycytidine (poly(IC)), lipopolysaccharides (LPS), lipid A, peptidoglycan (PGN), or bacterial flagellin (By similarity). To a lesser degree, IL-1 and engagement of CD40 also stimulate MAP4K2-mediated JNKs activation (By similarity). The requirement for MAP4K2/GCK is most pronounced for LPS signaling, and extends to LPS stimulation of c-Jun phosphorylation and induction of IL-8 (By similarity). Enhances MAP3K1 oligomerization, which may relieve N-terminal mediated MAP3K1 autoinhibition and lead to activation following autophosphorylation (By similarity). Mediates also the SAP/JNK signaling pathway and the p38 MAPKs signaling pathway through activation of the MAP3Ks MAP3K10/MLK2 and MAP3K11/MLK3 (By similarity). May play a role in the regulation of vesicle targeting or fusion (By similarity). {ECO:0000250|UniProtKB:Q12851, ECO:0000269|PubMed:8643544}. PTM: Polyubiquitinated through 'Lys-48'-polyubiquitin chains, allowing proteasomal turnover. Ubiquitination requires the kinase activity of MAP4K2/GCK.; PTM: Autophosphorylated in response to tumor necrosis factor (TNF), endotoxins or proinflammatory stimuli. Autophosphorylation leads to activation. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8643544}. Basolateral cell membrane {ECO:0000269|PubMed:8643544}; Peripheral membrane protein {ECO:0000269|PubMed:8643544}. Golgi apparatus membrane {ECO:0000269|PubMed:8643544}; Peripheral membrane protein {ECO:0000269|PubMed:8643544}. SUBUNIT: Interacts with TRAF2, TRAF6, MAP3K1/MEKK1 and MAP3K11/MLK3 (By similarity). Interacts with RAB8A. {ECO:0000250, ECO:0000269|PubMed:8643544}. DOMAIN: The PEST domains are Pro-, Glu-, Ser-, and Thr-rich domains. Proteins with PEST domains are frequently targets of degradation by the ubiquitin proteasome. +O54782 MA2B2_MOUSE Epididymis-specific alpha-mannosidase (EC 3.2.1.24) (Mannosidase alpha class 2B member 2) 1018 115,610 Active site (1); Chain (1); Glycosylation (10); Metal binding (4); Sequence conflict (2); Signal peptide (1) FUNCTION: Plays an important role in the early step of spermatogenesis. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Mainly expressed in the narrow region between the caput and corpus epididymis. +Q8CF90 MAFA_MOUSE Transcription factor MafA (Pancreatic beta-cell-specific transcriptional activator) (V-maf musculoaponeurotic fibrosarcoma oncogene homolog A) 359 37,576 Chain (1); Compositional bias (2); Cross-link (1); Domain (1); Modified residue (6); Region (2) FUNCTION: Transcriptional factor that activates insulin gene expression (PubMed:12368292, PubMed:15665000). Acts synergistically with NEUROD1/BETA2 and PDX1 (PubMed:15665000). Binds the insulin enhancer C1/RIPE3b element (PubMed:12917329, PubMed:14680841, PubMed:14973194, PubMed:15665000). Binds to consensus TRE-type MARE 5'-TGCTGACTCAGCA-3' DNA sequence (By similarity). {ECO:0000250|UniProtKB:Q8NHW3, ECO:0000269|PubMed:12368292, ECO:0000269|PubMed:12917329, ECO:0000269|PubMed:14680841, ECO:0000269|PubMed:14973194, ECO:0000269|PubMed:15665000}. PTM: Ubiquitinated, leading to its degradation by the proteasome. {ECO:0000250|UniProtKB:O57342}.; PTM: Phosphorylated at tyrosines. {ECO:0000269|PubMed:12917329}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12368292, ECO:0000269|PubMed:12917329, ECO:0000269|PubMed:14973194}. SUBUNIT: Forms homodimers (By similarity). Interacts with NEUROD1 and PDX1 (PubMed:15665000). May interact with MAFB, FOS, JUN and PCAF (By similarity). {ECO:0000250|UniProtKB:O57342, ECO:0000250|UniProtKB:Q8NHW3, ECO:0000269|PubMed:15665000}. TISSUE SPECIFICITY: Expressed in brain, lung, spleen, pancreas and kidney (PubMed:12368292, PubMed:14680841). In the pancreas, expressed in the insulin-producing beta-cells of the islets of Langerhans (at protein level) (PubMed:12917329, PubMed:15923615). Also expressed in the eye (PubMed:12368292, PubMed:15923615). {ECO:0000269|PubMed:12368292, ECO:0000269|PubMed:12917329, ECO:0000269|PubMed:14680841, ECO:0000269|PubMed:15923615}. +Q8BPM2 M4K5_MOUSE Mitogen-activated protein kinase kinase kinase kinase 5 (EC 2.7.11.1) (MAPK/ERK kinase kinase kinase 5) (MEK kinase kinase 5) (MEKKK 5) 847 95,045 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Domain (2); Modified residue (2); Nucleotide binding (1); Sequence conflict (5) FUNCTION: May play a role in the response to environmental stress. Appears to act upstream of the JUN N-terminal pathway (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with both SH3 domains of the adapter proteins CRK and CRKL. {ECO:0000250|UniProtKB:Q9Y4K4}. +Q1HKZ5 M3K13_MOUSE Mitogen-activated protein kinase kinase kinase 13 (EC 2.7.11.25) 959 106,987 Active site (1); Binding site (1); Chain (1); Domain (1); Nucleotide binding (1); Region (2) FUNCTION: Activates the JUN N-terminal pathway through activation of the MAP kinase kinase MAP2K7. Acts synergistically with PRDX3 to regulate the activation of NF-kappa-B in the cytosol. This activation is kinase-dependent and involves activating the IKK complex, the IKBKB-containing complex that phosphorylates inhibitors of NF-kappa-B (By similarity). {ECO:0000250}. PTM: Autophosphorylated on serine and threonine residues. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. SUBUNIT: Homodimer; forms dimers through the leucine-zipper motif. Interacts with the C-terminus of MAPK8IP1 through the kinase catalytic domain. Binds PRDX3. Associates with the IKK complex through the kinase domain. +O54791 MAFF_MOUSE Transcription factor MafF (V-maf musculoaponeurotic fibrosarcoma oncogene homolog F) 156 16,955 Chain (1); Domain (1); Region (2) FUNCTION: Since they lack a putative transactivation domain, the small Mafs behave as transcriptional repressors when they dimerize among themselves. However, they seem to serve as transcriptional activators by dimerizing with other (usually larger) basic-zipper proteins, such as NFE2L1/NRF1, and recruiting them to specific DNA-binding sites. Interacts with the upstream promoter region of the oxytocin receptor gene. May be a transcriptional enhancer in the up-regulation of the oxytocin receptor gene at parturition. {ECO:0000250|UniProtKB:Q9ULX9}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}. SUBUNIT: Monomer and homo- or heterodimer. Interacts with MIP. Forms high affinity heterodimers with members of the CNC-bZIP family such as NFE2L1/NRF1. {ECO:0000250|UniProtKB:Q9ULX9}. TISSUE SPECIFICITY: Highly expressed in the lung, lower expression in the brain, thymus, liver, spleen, intestine, kidney, heart, muscle, and ovary. Not significantly expressed in hematopoietic cells. +Q2TBA3 MALT1_MOUSE Mucosa-associated lymphoid tissue lymphoma translocation protein 1 homolog (EC 3.4.22.-) (Paracaspase) 832 93,216 Active site (2); Alternative sequence (1); Beta strand (19); Chain (1); Disulfide bond (2); Domain (3); Helix (11); Initiator methionine (1); Modified residue (2); Motif (1); Region (1); Sequence conflict (3); Turn (5) FUNCTION: Enhances BCL10-induced activation of NF-kappa-B. Involved in nuclear export of BCL10. Binds to TRAF6, inducing TRAF6 oligomerization and activation of its ligase activity. Has ubiquitin ligase activity (By similarity). MALT1-dependent BCL10 cleavage plays an important role in T-cell antigen receptor-induced integrin adhesion (By similarity). Involved in the induction of T helper 17 cells (Th17) differentiation. Cleaves RC3H1 and ZC3H12A in response to T-cell receptor (TCR) stimulation which releases their cooperatively repressed targets to promote Th17 cell differentiation (PubMed:25282160). {ECO:0000250|UniProtKB:Q9UDY8, ECO:0000269|PubMed:25282160}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000250|UniProtKB:Q9UDY8}. Note=Shuttles between the nucleus and cytoplasm. Found in perinuclear structures together with BCL10 (By similarity). {ECO:0000250|UniProtKB:Q9UDY8}. SUBUNIT: Binds through its Ig-like domains to BCL10. Forms oligomers which bind to TRAF6. Forms a complex with CARD14 and BCL10; resulting in the formation of a CBM (CARD14-BCL10-MALT1) complex. Interacts with BCL10; as part of a CBM (CARD11-BCL10-MALT1) complex involved in NF-kappa-B activation. {ECO:0000250|UniProtKB:Q9UDY8}. +P58500 M3KCL_MOUSE MAP3K7 C-terminal-like protein (TAK1-like protein) 142 16,271 Chain (1) DOMAIN: Contains a C-terminal domain similar to that of the C-terminal section of MAP3K7. TISSUE SPECIFICITY: Ubiquitous. +Q9JKP5 MBNL1_MOUSE Muscleblind-like protein 1 (Triplet-expansion RNA-binding protein) 341 36,976 Chain (1); Modified residue (1); Zinc finger (4) FUNCTION: Mediates pre-mRNA alternative splicing regulation. Acts either as activator or repressor of splicing on specific pre-mRNA targets. Inhibits cardiac troponin-T (TNNT2) pre-mRNA exon inclusion but induces insulin receptor (IR) pre-mRNA exon inclusion in muscle. Antagonizes the alternative splicing activity pattern of CELF proteins. Regulates the TNNT2 exon 5 skipping through competition with U2AF2. Inhibits the formation of the spliceosome A complex on intron 4 of TNNT2 pre-mRNA. Binds to the stem-loop structure within the polypyrimidine tract of TNNT2 intron 4 during spliceosome assembly. Binds to the 5'-YGCU(U/G)Y-3'consensus sequence. Binds to the IR RNA. Binds to CUG triplet repeat expansion in myotonic dystrophy muscle cells by sequestering the target RNAs (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NR56}. Cytoplasm {ECO:0000250|UniProtKB:Q9NR56}. Cytoplasmic granule {ECO:0000250|UniProtKB:Q9NR56}. Note=Localized with DDX1, TIAL1 and YBX1 in stress granules upon stress. Localized in the cytoplasm of multinucleated myotubes. {ECO:0000250|UniProtKB:Q9NR56}. SUBUNIT: Interacts with DDX1 and YBX1. Interacts with HNRNPH1; the interaction in RNA-independent (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in cardiac and skeletal muscle. Weakly expressed in heart and eye (at protein level). {ECO:0000269|PubMed:10970838}. +P56450 MC4R_MOUSE Melanocortin receptor 4 (MC4-R) 332 36,959 Chain (1); Disulfide bond (1); Glycosylation (4); Lipidation (1); Sequence conflict (2); Topological domain (8); Transmembrane (7) TRANSMEM 44 69 Helical; Name=1. {ECO:0000255}.; TRANSMEM 82 106 Helical; Name=2. {ECO:0000255}.; TRANSMEM 124 145 Helical; Name=3. {ECO:0000255}.; TRANSMEM 166 186 Helical; Name=4. {ECO:0000255}.; TRANSMEM 192 215 Helical; Name=5. {ECO:0000255}.; TRANSMEM 249 271 Helical; Name=6. {ECO:0000255}.; TRANSMEM 281 304 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 43 Extracellular. {ECO:0000255}.; TOPO_DOM 70 81 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 107 123 Extracellular. {ECO:0000255}.; TOPO_DOM 146 165 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 187 191 Extracellular. {ECO:0000255}.; TOPO_DOM 216 248 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 272 280 Extracellular. {ECO:0000255}.; TOPO_DOM 305 332 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor specific to the heptapeptide core common to adrenocorticotropic hormone and alpha-, beta-, and gamma-MSH. Plays a central role in energy homeostasis and somatic growth. This receptor is mediated by G proteins that stimulate adenylate cyclase (cAMP). {ECO:0000269|PubMed:23869016}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P32245}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Interacts with ATRNL1. Homodimer; disulfide-linked, also forms higher order oligomers. Interacts with MGRN1, but does not undergo MGRN1-mediated ubiquitination; this interaction competes with GNAS-binding and thus inhibits agonist-induced cAMP production (By similarity). Interacts with MRAP and MRAP2; these associated factors increase ligand-sensitivity and generation of cAMP. {ECO:0000250, ECO:0000269|PubMed:14531729, ECO:0000269|PubMed:23869016}. +P41149 MC5R_MOUSE Melanocortin receptor 5 (MC5-R) 325 36,953 Chain (1); Erroneous initiation (1); Glycosylation (4); Lipidation (2); Sequence conflict (2); Topological domain (8); Transmembrane (7) TRANSMEM 38 61 Helical; Name=1. {ECO:0000255}.; TRANSMEM 74 97 Helical; Name=2. {ECO:0000255}.; TRANSMEM 115 138 Helical; Name=3. {ECO:0000255}.; TRANSMEM 156 179 Helical; Name=4. {ECO:0000255}.; TRANSMEM 187 211 Helical; Name=5. {ECO:0000255}.; TRANSMEM 240 265 Helical; Name=6. {ECO:0000255}.; TRANSMEM 274 297 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 37 Extracellular. {ECO:0000255}.; TOPO_DOM 62 73 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 98 114 Extracellular. {ECO:0000255}.; TOPO_DOM 139 155 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 180 186 Extracellular. {ECO:0000255}.; TOPO_DOM 212 239 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 266 273 Extracellular. {ECO:0000255}.; TOPO_DOM 298 325 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for MSH (alpha, beta and gamma) and ACTH. The activity of this receptor is mediated by G proteins which activate adenylate cyclase. This receptor is a possible mediator of the immunomodulation properties of melanocortins. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Skin, adrenal gland, skeletal muscle, bone marrow, spleen, thymus, gonads, uterus and brain. +Q80V70 MEGF6_MOUSE Multiple epidermal growth factor-like domains protein 6 (Multiple EGF-like domains protein 6) (Epidermal growth factor-like protein 3) (EGF-like protein 3) 1572 164,723 Chain (1); Disulfide bond (66); Domain (22); Glycosylation (1); Sequence conflict (4); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q8K4L6 MEPE_MOUSE Matrix extracellular phosphoglycoprotein (Osteoblast/osteocyte factor 45) (OF45) (Osteoregulin) 441 46,872 Chain (1); Compositional bias (1); Erroneous gene model prediction (1); Erroneous initiation (2); Glycosylation (1); Motif (1); Region (2); Sequence conflict (9); Signal peptide (1) FUNCTION: Regulates renal phosphate and uric acid excretion (PubMed:26051469). Regulates bone mineralization by osteoblasts and cartilage mineralization by chondrocytes (PubMed:11414762, PubMed:12421822, PubMed:15843468, PubMed:22766095). Regulates the mineralization of the extracellular matrix of the craniofacial complex, such as teeth, bone and cartilage (PubMed:26927967). Increases dental pulp stem cell proliferation (By similarity). {ECO:0000250|UniProtKB:Q9NQ76, ECO:0000269|PubMed:11414762, ECO:0000269|PubMed:12421822, ECO:0000269|PubMed:15843468, ECO:0000269|PubMed:22766095, ECO:0000269|PubMed:26051469, ECO:0000269|PubMed:26927967}. PTM: Phosphorylated on serine residues in the ASARM motif; the phosphorylation is important for the inhibition of bone mineralization. {ECO:0000269|PubMed:15843468, ECO:0000269|PubMed:18597632, ECO:0000269|PubMed:22766095}.; PTM: Cleaved by CTSB/cathepsin B; the cleavage is blocked by metalloprotease PHEX. {ECO:0000250|UniProtKB:Q9NQ76}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:12421822, ECO:0000269|PubMed:18597632, ECO:0000269|PubMed:26051469}. SUBUNIT: Interacts (via ASARM motif) with PHEX; the interaction is zinc-dependent. {ECO:0000250|UniProtKB:Q9NQ76}. DOMAIN: The acidic serine aspartate-rich MEPE-associated (ASARM) motif is sufficient when phosphorylated to inhibit bone mineralization by osteoblasts and cartilage mineralization by chondrocytes by binding hydroxyapatite crystals during the mineralization stage (PubMed:15843468, PubMed:22766095, PubMed:26051469). It can also inhibit dentin mineralization (By similarity). {ECO:0000250|UniProtKB:Q9NQ76, ECO:0000269|PubMed:15843468, ECO:0000269|PubMed:22766095, ECO:0000269|PubMed:26051469}.; DOMAIN: The dentonin region is sufficient to promote dental pulp stem cell proliferation. It can also stimulate bone formation, osteoblast differentiation, and activate integrin signaling pathways. {ECO:0000250|UniProtKB:Q9NQ76}. TISSUE SPECIFICITY: Expressed in osteocytes (at protein level) (PubMed:12421822, PubMed:15221418). Expressed by chondrocytes, specifically in the hypertrophic zone of the bone growth plate (at protein level) (PubMed:22766095). Expressed in osteoblasts in bone (at protein level) (PubMed:11414762, PubMed:15221418, PubMed:18597632). Expressed by osteoblasts within the metaphysis (at protein level) (PubMed:15221418, PubMed:22766095). Expressed at low levels in white fat, brown fat, testes, brain and aorta (PubMed:12421822). Expressed in the craniofacial complex (at protein level) (PubMed:26927967). Expressed in odontoblasts, ameloblasts and in predentin during tooth development (at protein level) (PubMed:22042093). Expressed in the kidney (at protein level) (PubMed:26051469). Expressed in osteocytes in mandibular condylar cartilage and tibial cartilage (at protein level) (PubMed:26428891). Expressed in salivary glands (PubMed:15329369). {ECO:0000269|PubMed:11414762, ECO:0000269|PubMed:12421822, ECO:0000269|PubMed:15329369, ECO:0000269|PubMed:18597632, ECO:0000269|PubMed:22042093, ECO:0000269|PubMed:22766095, ECO:0000269|PubMed:26051469, ECO:0000269|PubMed:26428891, ECO:0000269|PubMed:26927967}. +Q07475 NREP_MOUSE Neuronal regeneration-related protein (Neuronal protein 3.1) (Protein p311) 68 7,688 Chain (1) FUNCTION: May have roles in cellular differentiation. Ectopic expression induces differentiation of fibroblast into myofibroblast and myofibroblast ameboid migration. Increases retinoic-acid regulation of lipid-droplet biogenesis. May also have neural functions. Promotes axonal regeneration and augments motility of gliomas. Down-regulates the expression of TGFB1 and TGFB2 but not of TGFB3. May play a role in the regulation of alveolar generation. {ECO:0000269|PubMed:12417574, ECO:0000269|PubMed:14985127, ECO:0000269|PubMed:16934802, ECO:0000269|PubMed:18664493}. PTM: Phosphorylated on Ser-59. Phosphorylation decreases stability and activity. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with FLNA (By similarity). Interacts with the latency-associated peptides (LAP) of TGFB1 and TGFB2; the interaction results in a decrease in TGFB autoinduction. {ECO:0000250, ECO:0000269|PubMed:14985127}. TISSUE SPECIFICITY: Expressed in brain and fetal lung. {ECO:0000269|PubMed:16484684, ECO:0000269|PubMed:8261136}. +P27808 MGAT1_MOUSE Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase (EC 2.4.1.101) (N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase I) (GNT-I) (GlcNAc-T I) 447 51,690 Active site (1); Binding site (5); Chain (1); Disulfide bond (2); Metal binding (1); Topological domain (2); Transmembrane (1) TRANSMEM 7 29 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 30 447 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Initiates complex N-linked carbohydrate formation. Essential for the conversion of high-mannose to hybrid and complex N-glycans. {ECO:0000269|PubMed:1421759}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:P26572}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P26572}. SUBUNIT: Interacts with MGAT4D. {ECO:0000269|PubMed:20805325}. TISSUE SPECIFICITY: Detected in kidney, liver and brain. {ECO:0000269|PubMed:1533386}. +P61327 MGN_MOUSE Protein mago nashi homolog 146 17,164 Chain (1); Modified residue (1) FUNCTION: Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). The MAGOH-RBM8A heterodimer inhibits the ATPase activity of EIF4A3, thereby trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The MAGOH-RBM8A heterodimer interacts with the EJC key regulator PYM1 leading to EJC disassembly in the cytoplasm and translation enhancement of EJC-bearing spliced mRNAs by recruiting them to the ribosomal 48S preinitiation complex. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms; the function is different from the established EJC assembly (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus speckle {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Detected in granule-like structures in the dendroplasm. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. Colocalizes with the core EJC, ALYREF/THOC4, NXF1 and UAP56 in the nucleus and nuclear speckles (By similarity). {ECO:0000250}. SUBUNIT: Heterodimer with RBM8A. Part of the mRNA splicing-dependent exon junction complex (EJC) complex; the core complex contains CASC3, EIF4A3, MAGOH and RBM8A. Interacts with PYM1; the interaction is direct and dissociates the EJC from spliced mRNAs. Identified in the spliceosome C complex (By similarity). {ECO:0000250}. +Q921V5 MGAT2_MOUSE Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase (EC 2.4.1.143) (Beta-1,2-N-acetylglucosaminyltransferase II) (GlcNAc-T II) (GNT-II) (Mannoside acetylglucosaminyltransferase 2) (N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase II) 442 51,030 Binding site (2); Chain (1); Disulfide bond (5); Glycosylation (2); Metal binding (2); Region (2); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 10 29 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 9 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 30 442 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Plays an essential role in protein N-glycosylation. Catalyzes the transfer of N-acetylglucosamine (GlcNAc) onto the free terminal mannose moiety in the core structure of the nascent N-linked glycan chain, giving rise to the second branch in complex glycans. {ECO:0000269|PubMed:11805078}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q10469}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q10469}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q10469}. TISSUE SPECIFICITY: Detected in liver, lung, testis, kidney, brain, spleen, thymus, uterus and intestine. {ECO:0000269|PubMed:11805078}. +Q8R3N2 MFS6L_MOUSE Major facilitator superfamily domain-containing protein 6-like 586 63,430 Chain (1); Transmembrane (11) TRANSMEM 50 70 Helical. {ECO:0000255}.; TRANSMEM 78 98 Helical. {ECO:0000255}.; TRANSMEM 240 260 Helical. {ECO:0000255}.; TRANSMEM 284 304 Helical. {ECO:0000255}.; TRANSMEM 318 338 Helical. {ECO:0000255}.; TRANSMEM 365 385 Helical. {ECO:0000255}.; TRANSMEM 397 417 Helical. {ECO:0000255}.; TRANSMEM 428 448 Helical. {ECO:0000255}.; TRANSMEM 454 474 Helical. {ECO:0000255}.; TRANSMEM 494 514 Helical. {ECO:0000255}.; TRANSMEM 519 538 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +O35678 MGLL_MOUSE Monoglyceride lipase (MGL) (EC 3.1.1.23) (Monoacylglycerol lipase) (MAGL) 303 33,388 Active site (3); Alternative sequence (1); Chain (1); Modified residue (3); Mutagenesis (7) Glycerolipid metabolism; triacylglycerol degradation. FUNCTION: Converts monoacylglycerides to free fatty acids and glycerol. Hydrolyzes the endocannabinoid 2-arachidonoylglycerol, and thereby contributes to the regulation of endocannabinoid signaling, nociperception and perception of pain (PubMed:9341166, PubMed:17700715, PubMed:18096503, PubMed:19029917, PubMed:20729846). Regulates the levels of fatty acids that serve as signaling molecules and promote cancer cell migration, invasion and tumor growth (By similarity). {ECO:0000250|UniProtKB:Q99685, ECO:0000269|PubMed:17700715, ECO:0000269|PubMed:18096503, ECO:0000269|PubMed:19029917, ECO:0000269|PubMed:20729846, ECO:0000269|PubMed:9341166}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:18096503}. Membrane; Peripheral membrane protein {ECO:0000269|PubMed:18096503}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q99685}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11470505}. +Q9CXC3 MGME1_MOUSE Mitochondrial genome maintenance exonuclease 1 (EC 3.1.-.-) 338 38,391 Active site (3); Chain (1); Sequence conflict (1); Transit peptide (1) FUNCTION: Metal-dependent single-stranded DNA (ssDNA) exonuclease involved in mitochondrial genome maintenance. Has preference for 5'-3' exonuclease activity but is also capable of endoduclease activity on linear substrates. Necessary for maintenance of proper 7S DNA levels. Probably involved in mitochondrial DNA (mtDNA) repair, possibly via the processing of displaced DNA containing Okazaki fragments during RNA-primed DNA synthesis on the lagging strand or via processing of DNA flaps during long-patch base excision repair (By similarity). Specifically binds 5-hydroxymethylcytosine (5hmC)-containing DNA in stem cells. {ECO:0000255|HAMAP-Rule:MF_03030, ECO:0000269|PubMed:23434322}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03030}. +A2AWL7 MGAP_MOUSE MAX gene-associated protein 3003 328,802 Alternative sequence (7); Chain (1); Compositional bias (4); Cross-link (41); DNA binding (1); Domain (1); Erroneous initiation (1); Modified residue (10); Sequence conflict (40) FUNCTION: Functions as a dual-specificity transcription factor, regulating the expression of both MAX-network and T-box family target genes. Functions as a repressor or an activator. Binds to 5'-AATTTCACACCTAGGTGTGAAATT-3' core sequence and seems to regulate MYC-MAX target genes. Suppresses transcriptional activation by MYC and inhibits MYC-dependent cell transformation. Function activated by heterodimerization with MAX. This heterodimerization serves the dual function of both generating an E-box-binding heterodimer and simultaneously blocking interaction of a corepressor. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Interacts with ZMYND11 (By similarity). Interacts with MAX. Requires heterodimerization with MAX for E-box binding. {ECO:0000250}. DOMAIN: Transcription repression is enhanced or dependent on the presence of the T-box DNA-binding domain. +Q14AW5 NSUN7_MOUSE Putative methyltransferase NSUN7 (EC 2.1.1.-) (NOL1/NOP2/Sun domain family member 7) 724 81,968 Active site (1); Alternative sequence (4); Chain (1); Erroneous initiation (1) FUNCTION: May have S-adenosyl-L-methionine-dependent methyl-transferase activity. {ECO:0000305}. TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:17442852}. +Q9D967 MGDP1_MOUSE Magnesium-dependent phosphatase 1 (MDP-1) (EC 3.1.3.-) (EC 3.1.3.48) 164 18,582 Active site (2); Beta strand (9); Binding site (7); Chain (1); Helix (7); Metal binding (3); Mutagenesis (9); Turn (4) FUNCTION: Magnesium-dependent phosphatase which may act as a tyrosine phosphatase. {ECO:0000269|PubMed:10889041, ECO:0000269|PubMed:11601995, ECO:0000269|PubMed:15461449}. +Q9CQL1 MGN2_MOUSE Protein mago nashi homolog 2 146 17,092 Chain (1); Erroneous initiation (1) FUNCTION: Involved in mRNA splicing and in the nonsense-mediated decay (NMD) pathway. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with RBM8A and is part of the exon junction complex (EJC). {ECO:0000250}. +Q3UHG7 LCHN_MOUSE Protein LCHN 455 51,428 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (3); Initiator methionine (1); Modified residue (2) FUNCTION: May play a role in neuritogenesis, as well as in neuronal recovery and/or restructuring in the hippocampus following transient cerebral ischemia. {ECO:0000250}. +Q5SUF2 LC7L3_MOUSE Luc7-like protein 3 (Cisplatin resistance-associated-overexpressed protein) 432 51,450 Alternative sequence (2); Chain (1); Coiled coil (1); Compositional bias (2); Cross-link (2); Modified residue (8); Sequence conflict (1) FUNCTION: Binds cAMP regulatory element DNA sequence. May play a role in RNA splicing (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}. SUBUNIT: May interact with SFRS1 and form homodimers. Interacts with JMJD6. Interacts with RBM25. Interacts with RSRC1 (via Arg/Ser-rich domain). Interacts with RRP1B. {ECO:0000250|UniProtKB:O95232}. +P06240 LCK_MOUSE Proto-oncogene tyrosine-protein kinase LCK (EC 2.7.10.2) (Leukocyte C-terminal Src kinase) (LSK) (Lymphocyte cell-specific protein-tyrosine kinase) (p56-LCK) 509 57,943 Active site (1); Binding site (1); Chain (1); Domain (3); Initiator methionine (1); Lipidation (3); Modified residue (7); Mutagenesis (16); Nucleotide binding (1); Region (2) FUNCTION: Non-receptor tyrosine-protein kinase that plays an essential role in the selection and maturation of developing T-cells in the thymus and in the function of mature T-cells. Plays a key role in T-cell antigen receptor (TCR)-linked signal transduction pathways. Constitutively associated with the cytoplasmic portions of the CD4 and CD8 surface receptors. Association of the TCR with a peptide antigen-bound MHC complex facilitates the interaction of CD4 and CD8 with MHC class II and class I molecules, respectively, thereby recruiting the associated LCK protein to the vicinity of the TCR/CD3 complex. LCK then phosphorylates tyrosine residues within the immunoreceptor tyrosine-based activation motifs (ITAM) of the cytoplasmic tails of the TCR-gamma chains and CD3 subunits, initiating the TCR/CD3 signaling pathway. Once stimulated, the TCR recruits the tyrosine kinase ZAP70, that becomes phosphorylated and activated by LCK. Following this, a large number of signaling molecules are recruited, ultimately leading to lymphokine production. LCK also contributes to signaling by other receptor molecules. Associates directly with the cytoplasmic tail of CD2, which leads to hyperphosphorylation and activation of LCK. Also plays a role in the IL2 receptor-linked signaling pathway that controls the T-cell proliferative response. Binding of IL2 to its receptor results in increased activity of LCK. Is expressed at all stages of thymocyte development and is required for the regulation of maturation events that are governed by both pre-TCR and mature alpha beta TCR. Phosphorylates other substrates including RUNX3, PTK2B/PYK2, the microtubule-associated protein MAPT, RHOH or TYROBP (By similarity). Interacts with UNC119; this interaction plays a crucial role in activation of LCK (By similarity). {ECO:0000250}. PTM: Autophosphorylated on Tyr-394, increasing enzymatic activity, this site is dephosphorylated by PTN22. Phosphorylated on Tyr-505 by CSK, decreasing activity. Dephosphorylated by PTPRC/CD45. Dephosphorylation at Tyr-394 by PTPN2 negatively regulates T-cells differentiation (By similarity). {ECO:0000250}.; PTM: Myristoylation is required prior to palmitoylation. {ECO:0000269|PubMed:7980442, ECO:0000269|PubMed:8413237}.; PTM: Palmitoylation regulates subcellular location. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12218089}. Cell membrane {ECO:0000269|PubMed:12218089}; Lipid-anchor {ECO:0000269|PubMed:12218089}; Cytoplasmic side {ECO:0000269|PubMed:12218089}. Note=Present in lipid rafts in an inactive form. SUBUNIT: Binds to the cytoplasmic domain of cell surface receptors, such as AXL, CD2, CD4, CD5, CD8, CD44, CD45 and CD122. Also binds to effector molecules, such as PI4K, VAV1, RASA1, FYB1 and to other protein kinases including CDK1, RAF1, ZAP70 and SYK. Binds to phosphatidylinositol 3'-kinase (PI3K) from T-lymphocytes through its SH3 domain and to the tyrosine phosphorylated form of KHDRBS1/p70 through its SH2 domain. Interacts with SQSTM1. Interacts with phosphorylated LIME1. Interacts with CBLB and PTPRH. Interacts with RUNX3. Forms a signaling complex with EPHA1, PTK2B AND PI3-KINASE; upon activation by EFNA1 which may regulate T-lymphocytes migration. Associates with ZAP70 and RHOH; these interactions allow LCK-mediated RHOH and CD3 subunit phosphorylation in the presence of functional ZAP70. Interacts with CEACAM1 (via cytoplasmic domain); mediates CEACAM1 phosphorylation resulting in PTPN6 recruitment that dephosphorylates TCR stimulation-induced CD247 and ZAP70. Interacts with FYB2 (By similarity). Interacts with CD160. {ECO:0000250|UniProtKB:P06239}. DOMAIN: The SH2 domain mediates interaction with SQSTM1. Interaction is regulated by Ser-59 phosphorylation (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Present at a low level in most T-cells, and at an elevated level in LSTRA and Thy19 (T-cell lymphoma) cells. +Q924P3 LCN8_MOUSE Epididymal-specific lipocalin-8 (Epididymal 17 kDa lipocalin) (EP17) (mEP17) 175 19,866 Chain (1); Disulfide bond (1); Glycosylation (2); Signal peptide (1) FUNCTION: May play a role in male fertility. May act as a retinoid carrier protein within the epididymis. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. TISSUE SPECIFICITY: Predominantly expressed in epididymis. {ECO:0000269|PubMed:11181548}. +Q9D267 LCN9_MOUSE Epididymal-specific lipocalin-9 (MUP-like lipocalin) 178 20,503 Chain (1); Disulfide bond (1); Glycosylation (3); Sequence conflict (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Expressed in epididymis. Not detected in all other tissues tested. {ECO:0000269|PubMed:15363845}. +P70662 LDB1_MOUSE LIM domain-binding protein 1 (LDB-1) (Carboxyl-terminal LIM domain-binding protein 2) (CLIM-2) (LIM domain-binding factor CLIM2) (mLdb1) (Nuclear LIM interactor) 411 46,503 Alternative sequence (3); Beta strand (4); Chain (1); Initiator methionine (1); Modified residue (4); Region (1); Sequence conflict (3) FUNCTION: Binds to the LIM domain of a wide variety of LIM domain-containing transcription factors. May regulate the transcriptional activity of LIM-containing proteins by determining specific partner interactions. Plays a role in the development of interneurons and motor neurons in cooperation with LHX3 and ISL1. Acts synergistically with LHX1/LIM1 in axis formation and activation of gene expression. Acts with LMO2 in the regulation of red blood cell development, maintaining erythroid precursors in an immature state. {ECO:0000269|PubMed:12150931, ECO:0000269|PubMed:16815859, ECO:0000269|PubMed:8876198, ECO:0000269|PubMed:8918878, ECO:0000269|PubMed:9192866, ECO:0000269|PubMed:9315627, ECO:0000269|PubMed:9391090}. PTM: Ubiquitinated by RLIM/RNF12, leading to its degradation by the proteasome. {ECO:0000269|PubMed:11882901}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8876198, ECO:0000269|PubMed:9315627, ECO:0000269|PubMed:9391090}. Note=Colocalizes with SLK at leading edges (PubMed:19675209). {ECO:0000269|PubMed:19675209}. SUBUNIT: Interacts with ESR1 (By similarity). Forms homodimers and heterodimers. Interacts with and activates LHX1/LIM1. Interacts with the LIM domains of ISL1 and LMO2. Can assemble in a complex with LMO2 and TAL1/SCL but does not interact with TAL1/SCL directly. Strongly interacts with the LIM2 domain of LMX1A and more weakly with the LIM1 domain. Homodimerization is not required for, and does not effect, LMX1A-binding. Component of a nuclear TAL-1 complex composed at least of CBFA2T3, LDB1, TAL1 and TCF3. Interacts with LHX6 and LHX9. At neuronal promoters, forms a complex with LHX3 involved in the specification of interneurons, in motor neurons, it is displaced by ISL1 to form a ternary complex in which ISL1 contacts both LHX3 and LDB1. Interacts with SLK; leading to negatively regulate SLK kinase activity (PubMed:19675209). {ECO:0000250, ECO:0000269|PubMed:10330499, ECO:0000269|PubMed:10393337, ECO:0000269|PubMed:11882901, ECO:0000269|PubMed:12150931, ECO:0000269|PubMed:15343268, ECO:0000269|PubMed:16407974, ECO:0000269|PubMed:19675209, ECO:0000269|PubMed:8918878, ECO:0000269|PubMed:9315627, ECO:0000269|PubMed:9391090, ECO:0000269|PubMed:9468533}. DOMAIN: The dimerization domain is located in the N-terminus. {ECO:0000269|PubMed:9468533}. TISSUE SPECIFICITY: Expression overlaps that of LIM domain-containing proteins. Expressed widely in the embryo with highest expression in several regions of the brain the central nervous system ganglia. Also expressed in fetal liver, lung, kidney, thymus and olfactory epithelium. Expressed in multiple adult tissues including heart, brain, liver, kidney, testis, lung and muscle and a diverse range of neuronal cell types, with expression highest in the pituitary gland and skin. Expressed in both embryonic and adult hemopoietic cells, including the erythroid lineage. {ECO:0000269|PubMed:16815859, ECO:0000269|PubMed:8918878, ECO:0000269|PubMed:9192866, ECO:0000269|PubMed:9391090}. +P06151 LDHA_MOUSE L-lactate dehydrogenase A chain (LDH-A) (EC 1.1.1.27) (LDH muscle subunit) (LDH-M) 332 36,499 Active site (1); Binding site (5); Chain (1); Cross-link (1); Initiator methionine (1); Modified residue (17); Nucleotide binding (1); Sequence conflict (1) Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1. PTM: ISGylated. {ECO:0000269|PubMed:16139798}. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Homotetramer. +Q91V13 LEAP2_MOUSE Liver-expressed antimicrobial peptide 2 (LEAP-2) 76 8,536 Chain (1); Disulfide bond (2); Propeptide (1); Signal peptide (1) FUNCTION: Has an antimicrobial activity. SUBCELLULAR LOCATION: Secreted. +P15702 LEUK_MOUSE Leukosialin (B-cell differentiation antigen LP-3) (Leukocyte sialoglycoprotein) (Lymphocyte antigen 48) (Ly-48) (Sialophorin) (CD antigen CD43) [Cleaved into: CD43 cytoplasmic tail (CD43-ct) (CD43ct)] 395 40,038 Beta strand (1); Chain (2); Glycosylation (1); Modified residue (8); Mutagenesis (4); Region (1); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 249 271 Helical. {ECO:0000255}. TOPO_DOM 20 248 Extracellular. {ECO:0000255}.; TOPO_DOM 272 395 Cytoplasmic. {ECO:0000255}. FUNCTION: Predominant cell surface sialoprotein of leukocytes which regulates multiple T-cell functions, including T-cell activation, proliferation, differentiation, trafficking and migration. Positively regulates T-cell trafficking to lymph-nodes via its association with ERM proteins (EZR, RDX and MSN) (PubMed:17638845, PubMed:21289089, PubMed:11728336). Negatively regulates Th2 cell differentiation and predisposes the differentiation of T-cells towards a Th1 lineage commitment (PubMed:18490738). Promotes the expression of IFN-gamma by T-cells during T-cell receptor (TCR) activation of naive cells and induces the expression of IFN-gamma by CD4(+) T-cells and to a lesser extent by CD8(+) T-cells. Plays a role in preparing T-cells for cytokine sensing and differentiation into effector cells by inducing the expression of cytokine receptors IFNGR and IL4R, promoting IFNGR and IL4R signaling and by mediating the clustering of IFNGR with TCR (By similarity). Acts as a major E-selectin ligand responsible for Th17 cell rolling on activated vasculature and recruitment during inflammation. Mediates Th17 cells, but not Th1 cells, adhesion to E-selectin (PubMed:26700769). Acts as a T-cell counter-receptor for SIGLEC1 (PubMed:11238599). {ECO:0000250|UniProtKB:P16150, ECO:0000269|PubMed:11238599, ECO:0000269|PubMed:11728336, ECO:0000269|PubMed:17638845, ECO:0000269|PubMed:18490738, ECO:0000269|PubMed:21289089, ECO:0000269|PubMed:26700769}.; FUNCTION: CD43 cytoplasmic tail: Protects cells from apoptotic signals, promoting cell survival. {ECO:0000269|PubMed:19696198}. PTM: Phosphorylation at Ser-347 is regulated by chemokines, requires its association with ERM proteins (EZR, RDX and MSN) and is essential for its function in the regulation of T-cell trafficking to lymph nodes. {ECO:0000269|PubMed:17638845, ECO:0000269|PubMed:21289089}.; PTM: Has a high content of sialic acid and O-linked carbohydrate structures.; PTM: Cleavage by CTSG releases its extracellular domain and triggers its intramembrane proteolysis by gamma-secretase releasing the CD43 cytoplasmic tail chain (CD43-ct) which translocates to the nucleus. {ECO:0000269|PubMed:19696198}.; PTM: CD43 cytoplasmic tail: Sumoylated. {ECO:0000269|PubMed:19696198}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, microvillus {ECO:0000250|UniProtKB:P13838}. Cell projection, uropodium {ECO:0000269|PubMed:21289089}. Note=Localizes to the uropodium and microvilli via its interaction with ERM proteins (EZR, RDX and MSN). {ECO:0000250|UniProtKB:P13838, ECO:0000269|PubMed:21289089}.; SUBCELLULAR LOCATION: CD43 cytoplasmic tail: Nucleus {ECO:0000269|PubMed:19696198}. Nucleus, PML body {ECO:0000269|PubMed:19696198}. SUBUNIT: Interacts with HIPK2 via the cytoplasmic domain (PubMed:11078605). Interacts with SIGLEC1 (PubMed:11238599). Interacts with RDX (PubMed:18614175). Interacts with EZR (PubMed:21289089). Interacts with MSN (By similarity). {ECO:0000250|UniProtKB:P13838, ECO:0000269|PubMed:11078605, ECO:0000269|PubMed:11238599, ECO:0000269|PubMed:18614175, ECO:0000269|PubMed:21289089}. TISSUE SPECIFICITY: Cell surface of thymocytes, T-lymphocytes, neutrophils, plasma cells and myelomas. +O09010 LFNG_MOUSE Beta-1,3-N-acetylglucosaminyltransferase lunatic fringe (EC 2.4.1.222) (O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase) 378 41,952 Active site (1); Binding site (2); Chain (1); Disulfide bond (3); Glycosylation (1); Metal binding (2); Sequence conflict (2); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 9 29 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 8 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 30 378 Lumenal. {ECO:0000255}. FUNCTION: Glycosyltransferase that initiates the elongation of O-linked fucose residues attached to EGF-like repeats in the extracellular domain of Notch molecules. Modulates NOTCH1 activity by modifying O-fucose residues at specific EGF-like domains resulting in inhibition of NOTCH1 activation by JAG1 and enhancement of NOTCH1 activation by DLL1 via an increase in its binding to DLL1 (PubMed:28089369). Decreases the binding of JAG1 to NOTCH2 but not that of DLL1 (By similarity). Essential mediator of somite segmentation and patterning. During somite boundary formation, it restricts Notch activity in the presomitic mesoderm to a boundary-forming territory in the posterior half of the prospective somite. In this region, Notch function activates a set of genes that are involved in boundary formation and in anterior-posterior somite identity (PubMed:10330372). Ectopically expressed in the thymus, Lfgn inhibits Notch signaling which results in inhibition of T-cell commitment and promotes B-cell development in lymphoid progenitors (PubMed:11520458). May play a role in boundary formation of the enamel knot (PubMed:12167404). {ECO:0000250|UniProtKB:Q8NES3, ECO:0000269|PubMed:10330372, ECO:0000269|PubMed:11520458, ECO:0000269|PubMed:12167404, ECO:0000269|PubMed:28089369}. PTM: A soluble form may be derived from the membrane form by proteolytic processing. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Detected at 12.5 dpc in all tissues examined with the highest level observed in adult brain and spleen. Detected in the dental epithelium. +A2AVQ5 LEXM_MOUSE Lymphocyte expansion molecule 414 47,584 Chain (1); Erroneous initiation (1); Sequence conflict (1) +Q3UVD5 LGR6_MOUSE Leucine-rich repeat-containing G-protein coupled receptor 6 967 104,267 Chain (1); Compositional bias (1); Disulfide bond (1); Domain (1); Glycosylation (2); Repeat (15); Sequence conflict (9); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 568 588 Helical; Name=1. {ECO:0000255}.; TRANSMEM 599 619 Helical; Name=2. {ECO:0000255}.; TRANSMEM 645 665 Helical; Name=3. {ECO:0000255}.; TRANSMEM 688 708 Helical; Name=4. {ECO:0000255}.; TRANSMEM 728 748 Helical; Name=5. {ECO:0000255}.; TRANSMEM 775 795 Helical; Name=6. {ECO:0000255}.; TRANSMEM 810 830 Helical; Name=7. {ECO:0000255}. TOPO_DOM 25 567 Extracellular. {ECO:0000255}.; TOPO_DOM 589 598 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 620 644 Extracellular. {ECO:0000255}.; TOPO_DOM 666 687 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 709 727 Extracellular. {ECO:0000255}.; TOPO_DOM 749 774 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 796 809 Extracellular. {ECO:0000255}.; TOPO_DOM 831 967 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for R-spondins that potentiates the canonical Wnt signaling pathway and acts as a marker of multipotent stem cells in the epidermis. Upon binding to R-spondins (RSPO1, RSPO2, RSPO3 or RSPO4), associates with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increase expression of target genes. In contrast to classical G-protein coupled receptors, does not activate heterotrimeric G-proteins to transduce the signal (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Specifically expressed in multipotent stem cells in the epidermis. {ECO:0000269|PubMed:20223988}. +Q80SV1 LHPL1_MOUSE LHFPL tetraspan subfamily member 1 protein (Lipoma HMGIC fusion partner-like 1 protein) 220 23,787 Chain (1); Glycosylation (1); Signal peptide (1); Transmembrane (3) TRANSMEM 86 106 Helical. {ECO:0000255}.; TRANSMEM 122 142 Helical. {ECO:0000255}.; TRANSMEM 165 185 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Widely expressed (PubMed:26964900). Strongly expressed in vagina and ovary. Weakly expressed in spleen, kidney, thymus, testis, brain, lung, intestine and uterus (PubMed:26964900). {ECO:0000269|PubMed:26964900}. +Q9Z0S2 LHX2_MOUSE LIM/homeobox protein Lhx2 (Homeobox protein LH-2) (LIM homeobox protein 2) 406 44,419 Chain (1); Compositional bias (1); DNA binding (1); Domain (2); Motif (1); Mutagenesis (2) FUNCTION: Acts as a transcriptional activator. Stimulates the promoter of the alpha-glycoprotein gene. Transcriptional regulatory protein involved in the control of cell differentiation in developing lymphoid and neural cell types. {ECO:0000269|PubMed:10593900}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Interacts (via LIM domains) with CITED2 (PubMed:10593900). Interacts with POU4F2 isoform 1 (PubMed:24643061). {ECO:0000269|PubMed:10593900, ECO:0000269|PubMed:24643061}. DOMAIN: LIM domains are necessary for transcription activation. +Q9EQR5 LIME1_MOUSE Lck-interacting transmembrane adapter 1 (Lck-interacting molecule) 269 29,551 Chain (1); Lipidation (2); Modified residue (6); Mutagenesis (5); Region (5); Topological domain (2); Transmembrane (1) TRANSMEM 8 28 Helical; Signal-anchor for type III membrane protein. {ECO:0000255}. TOPO_DOM 1 7 Extracellular. {ECO:0000255}.; TOPO_DOM 29 269 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in BCR (B-cell antigen receptor)-mediated signaling in B-cells and TCR (T-cell antigen receptor)-mediated T-cell signaling in T-cells. In absence of TCR signaling, may be involved in CD4-mediated inhibition of T-cell activation. Couples activation of these receptors and their associated kinases with distal intracellular events such as calcium mobilization or MAPK activation through the recruitment of PLCG2, GRB2, GRAP2, and other signaling molecules. {ECO:0000269|PubMed:14610044, ECO:0000269|PubMed:16249387}. PTM: Palmitoylation of Cys-28 and Cys-31 is required for raft targeting. {ECO:0000269|PubMed:14610044}.; PTM: Phosphorylated on tyrosines upon TCR activation and/or CD4 coreceptor stimulation, or upon BCR stimulation; which leads to the recruitment of SH2-containing proteins. {ECO:0000269|PubMed:14610044, ECO:0000269|PubMed:16249387}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14610044}; Single-pass type III membrane protein {ECO:0000269|PubMed:14610044}. Note=Present in lipid rafts. Recruited to the immunological synapse upon conjugation of T-cell with antigen-presenting cell. SUBUNIT: When phosphorylated in response to TCR stimulation and/or CD4 costimulation, interacts with LCK, CSK, FYN, PTPN11/SHP2, GRB2, PIK3R1 and GRAP2 (By similarity). When phosphorylated in response to BCR activation, interacts with LYN, PIK3R1, PLCG2 and GRB2. {ECO:0000250, ECO:0000269|PubMed:14610044, ECO:0000269|PubMed:16249387}. TISSUE SPECIFICITY: Expressed in spleen and lung. Present in primary B-cells and peripheral T-cells (at protein level). {ECO:0000269|PubMed:14610044, ECO:0000269|PubMed:16249387}. +Q9D8N6 LIN37_MOUSE Protein lin-37 homolog (Antolefinin) (Antolefinine) 246 28,378 Chain (1); Compositional bias (1); Cross-link (2); Modified residue (6) SUBUNIT: Component of the DREAM complex (also named LINC complex) at least composed of E2F4, E2F5, LIN9, LIN37, LIN52, LIN54, MYBL1, MYBL2, RBL1, RBL2, RBBP4, TFDP1 and TFDP2. The complex exists in quiescent cells where it represses cell cycle-dependent genes. It dissociates in S phase when LIN9, LIN37, LIN52 and LIN54 form a subcomplex that binds to MYBL2 (By similarity). {ECO:0000250}. +A2AJ15 MA1B1_MOUSE Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase (EC 3.2.1.113) (ER alpha-1,2-mannosidase) (ER mannosidase 1) (ERMan1) (Man9GlcNAc2-specific-processing alpha-mannosidase) (Mannosidase alpha class 1B member 1) 658 75,150 Active site (4); Chain (1); Disulfide bond (1); Metal binding (1); Modified residue (1); Topological domain (2); Transmembrane (1) TRANSMEM 51 71 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 50 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 72 658 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Involved in glycoprotein quality control targeting of misfolded glycoproteins for degradation. It primarily trims a single alpha-1,2-linked mannose residue from Man(9)GlcNAc(2) to produce Man(8)GlcNAc(2), but at high enzyme concentrations, as found in the ER quality control compartment (ERQC), it further trims the carbohydrates to Man(5-6)GlcNAc(2) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein. +Q9CQY5 MAGT1_MOUSE Magnesium transporter protein 1 (MagT1) (Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit MAGT1) (Oligosaccharyl transferase subunit MAGT1) (Implantation-associated protein) (IAP) 335 37,970 Alternative sequence (2); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (1); Sequence conflict (3); Signal peptide (1); Topological domain (5); Transmembrane (4) TRANSMEM 185 205 Helical. {ECO:0000255}.; TRANSMEM 210 230 Helical. {ECO:0000255}.; TRANSMEM 271 291 Helical. {ECO:0000255}.; TRANSMEM 301 321 Helical. {ECO:0000255}. TOPO_DOM 30 184 Extracellular. {ECO:0000255}.; TOPO_DOM 206 209 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 231 270 Extracellular. {ECO:0000255}.; TOPO_DOM 292 300 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 322 335 Extracellular. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Acts as accessory component of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. Involved in N-glycosylation of STT3B-dependent substrates. Specifically required for the glycosylation of a subset of acceptor sites that are near cysteine residues; in this function seems to act redundantly with TUSC3. In its oxidized form proposed to form transient mixed disulfides with a glycoprotein substrate to facilitate access of STT3B to the unmodified acceptor site. Has also oxidoreductase-independent functions in the STT3B-containing OST complex possibly involving substrate recognition. {ECO:0000250|UniProtKB:Q9H0U3}.; FUNCTION: May be involved in Mg(2+) transport in epithelial cells. {ECO:0000305|PubMed:15804357}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9H0U3}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9H0U3}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9H0U3}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Accessory component of the STT3B-containing form of the oligosaccharyltransferase (OST) complex. OST exists in two different complex forms which contain common core subunits RPN1, RPN2, OST48, OST4, DAD1 and TMEM258, either STT3A or STT3B as catalytic subunits, and form-specific accessory subunits. OST can form stable complexes with the Sec61 complex or with both the Sec61 and TRAP complexes. The association of TUSC3 or MAGT1 with the STT3B-containing complex seems to be mutually exclusvice. {ECO:0000250|UniProtKB:Q9H0U3}. TISSUE SPECIFICITY: Expressed at high levels in kidney, colon, heart and liver. Expressed at lower levels in intestine, spleen, brain and lung. {ECO:0000269|PubMed:15804357}. +Q3UYG8 MACD2_MOUSE ADP-ribose glycohydrolase MACROD2 (MACRO domain-containing protein 2) (O-acetyl-ADP-ribose deacetylase MACROD2) (EC 3.5.1.-) ([Protein ADP-ribosylaspartate] hydrolase MACROD2) (EC 3.2.2.-) ([Protein ADP-ribosylglutamate] hydrolase MACROD2) (EC 3.2.2.-) 475 52,145 Binding site (1); Chain (1); Compositional bias (1); Cross-link (1); Domain (1); Region (4) FUNCTION: Removes ADP-ribose from asparatate and glutamate residues in proteins bearing a single ADP-ribose moiety. Inactive towards proteins bearing poly-ADP-ribose. Deacetylates O-acetyl-ADP ribose, a signaling molecule generated by the deacetylation of acetylated lysine residues in histones and other proteins. {ECO:0000250|UniProtKB:A1Z1Q3}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:A1Z1Q3}. Note=Recruited to DNA lesions, probably via mono-APD-ribosylated proteins. {ECO:0000250|UniProtKB:A1Z1Q3}. SUBUNIT: Interacts with ADP-ribosylated PARP1. {ECO:0000250|UniProtKB:A1Z1Q3}. TISSUE SPECIFICITY: Expressed in the kidney. {ECO:0000269|PubMed:17586838}. +Q80US8 MAD3_MOUSE Max dimerization protein 3 (Max dimerizer 3) (Max-associated protein 3) 206 23,635 Chain (1); Domain (1); Region (1); Sequence conflict (1) FUNCTION: Transcriptional repressor. Binds with MAX to form a sequence-specific DNA-binding protein complex which recognizes the core sequence 5'-CAC[GA]TG-3'. Antagonizes MYC transcriptional activity by competing for MAX and suppresses MYC dependent cell transformation. {ECO:0000269|PubMed:8521822}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:8521822}. SUBUNIT: Efficient DNA binding requires dimerization with another bHLH protein. Binds DNA as a heterodimer with MAX. Interacts with SIN3A AND SIN3B. Interacts with RNF17. {ECO:0000269|PubMed:10597267, ECO:0000269|PubMed:8521822}. TISSUE SPECIFICITY: Expressed only in the proliferating areas of the testis and thymus. {ECO:0000269|PubMed:11154258}. +Q9WVL0 MAAI_MOUSE Maleylacetoacetate isomerase (MAAI) (EC 5.2.1.2) (GSTZ1-1) (Glutathione S-transferase zeta 1) (EC 2.5.1.18) 216 24,275 Beta strand (5); Binding site (3); Chain (1); Domain (2); Helix (13); Modified residue (6); Region (3); Turn (1) Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 5/6. FUNCTION: Probable bifunctional enzyme showing minimal glutathione-conjugating activity with ethacrynic acid and 7-chloro-4-nitrobenz-2-oxa-1, 3-diazole and maleylacetoacetate isomerase activity. Has also low glutathione peroxidase activity with t-butyl and cumene hydroperoxides. Is able to catalyze the glutathione dependent oxygenation of dichloroacetic acid to glyoxylic acid (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000305|Ref.7}. TISSUE SPECIFICITY: Expressed in liver, kidney, seminal glands and breast. +Q6RHR9 MAGI1_MOUSE Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1 (BAI1-associated protein 1) (BAP-1) (Membrane-associated guanylate kinase inverted 1) (MAGI-1) 1471 161,974 Alternative sequence (7); Beta strand (5); Chain (1); Compositional bias (4); Domain (9); Helix (2); Modified residue (7); Nucleotide binding (1); Region (1); Sequence conflict (2) FUNCTION: May play a role as scaffolding protein at cell-cell junctions. May regulate acid-induced ASIC3 currents by modulating its expression at the cell surface. {ECO:0000269|PubMed:15317815}. SUBCELLULAR LOCATION: Isoform 2: Cytoplasm {ECO:0000305}. Cell membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Cell junction, tight junction {ECO:0000250}. Note=Localizes to epithelial cells tight junctions. {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 3: Cytoplasm {ECO:0000305}. Cell membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: Isoform 1: Nucleus {ECO:0000305}. SUBUNIT: Interacts through its WW 2 domain with SYNPO and through its PDZ 5 domain with ACTN4. Interacts with cytoplasmic domain of ADGRB1. Interacts via its WW domains with DRPLA (By similarity). Interacts with ESAM, LRP2 and CXADR (PubMed:15383320, PubMed:11274227, PubMed:15304526). Isoform 2 interacts with CTNNB1 (PubMed:10772923). Interacts through its PDZ 1 domain with NET1 (PubMed:11350080). Interacts with ASIC3 and AMOT (By similarity) (PubMed:15317815). Interacts with FCHSD2 (By similarity). Interacts with IGSF5/JAM4 and through its PDZ 2 and 3 domains with NPHS1 forming a tripartite complex (By similarity). Interacts with DDN. May interact (via PDZ domain) with RAPGEF2 (By similarity). Interacts with DLL1 (PubMed:15509766). Interacts with KCNJ10 and possibly with KCNJ10/KCNJ16 heterodimer; this interaction may facilitate KCNJ10/KCNJ16 potassium channel expression at the basolateral membrane in kidney tubular cells (By similarity). {ECO:0000250|UniProtKB:Q4L1J4, ECO:0000250|UniProtKB:Q96QZ7, ECO:0000269|PubMed:10772923, ECO:0000269|PubMed:11274227, ECO:0000269|PubMed:11350080, ECO:0000269|PubMed:15304526, ECO:0000269|PubMed:15317815, ECO:0000269|PubMed:15383320, ECO:0000269|PubMed:15509766}. TISSUE SPECIFICITY: Widely expressed, including kidney glomeruli. {ECO:0000269|PubMed:11274227, ECO:0000269|PubMed:9395497}. +Q9WVQ1 MAGI2_MOUSE Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2 (Activin receptor-interacting protein 1) (Acvrip1) (Atrophin-1-interacting protein 1) (AIP-1) (Membrane-associated guanylate kinase inverted 2) (MAGI-2) 1275 140,919 Alternative sequence (4); Chain (1); Domain (9); Modified residue (6); Region (1) FUNCTION: Seems to act as scaffold molecule at synaptic junctions by assembling neurotransmitter receptors and cell adhesion proteins. Plays a role in nerve growth factor (NGF)-induced recruitment of RAPGEF2 to late endosomes and neurite outgrowth. May play a role in regulating activin-mediated signaling in neuronal cells. Enhances the ability of PTEN to suppress AKT1 activation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Late endosome {ECO:0000250}. Cell junction, synapse, synaptosome {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Localized diffusely in the cytoplasm before nerve growth factor (NGF) stimulation. Recruted to late endosomes after NGF stimulation. Membrane-associated in synaptosomes (By similarity). {ECO:0000250}. SUBUNIT: Interacts (via its WW domains) with DRPLA (By similarity). Interacts (via its second PDZ domain) with PTEN (via unphosphorylated C-terminus); this interaction diminishes the degradation rate of PTEN (By similarity). Interacts (via guanylate kinase domain) with DLGAP1 (By similarity). Interacts (via the PDZ domains) with GRIN2A, GRID2 and NLGN1 (By similarity). Interacts with CTNND2, CTNNB1 and MAGUIN-1 (By similarity). Interacts with ACVR2A, SMAD2 and SMAD3 (PubMed:10681527). Part of a complex consisting of AIP1, ACVR2A, ACVR1B and SMAD3 (PubMed:10681527). May interact with HTR2A (PubMed:14988405). Interacts with RAPGEF2 (By similarity). Identified in a complex with ACTN4, CASK, IQGAP1, NPHS1, SPTAN1 and SPTBN1 (By similarity). Interacts with DDN (By similarity). Found in a complex, at least composed of KIDINS220, MAGI2, NTRK1 and RAPGEF2; the complex is mainly formed at late endosomes in a NGF-dependent manner (By similarity). Interacts with RAPGEF2; the interaction occurs before or after nerve growth factor (NGF) stimulation (By similarity). Interacts (via PDZ domain) with KIDINS220 (via C-terminal domain) (By similarity). Interacts with IGSF9 and HTR4 (PubMed:15466885, PubMed:15340156). Interacts with DLL1 (PubMed:15509766). Found in a complex with IGSF9B and NLGN2; the interaction with IGSF9B is mediated via the PDZ 5 and PDZ 6 domains, while the interaction with NLGN2 is mediated via the WW1, WW2 and PDZ2 domains (PubMed:23751499). {ECO:0000250|UniProtKB:O88382, ECO:0000269|PubMed:10681527, ECO:0000269|PubMed:14988405, ECO:0000269|PubMed:15340156, ECO:0000269|PubMed:15466885, ECO:0000269|PubMed:15509766, ECO:0000269|PubMed:23751499}. TISSUE SPECIFICITY: Specifically expressed in brain. +Q9CXI5 MANF_MOUSE Mesencephalic astrocyte-derived neurotrophic factor (Arginine-rich protein) (Protein ARMET) 179 20,374 Beta strand (3); Chain (1); Disulfide bond (4); Helix (11); Modified residue (1); Signal peptide (1); Turn (5) FUNCTION: Selectively promotes the survival of dopaminergic neurons of the ventral mid-brain. Modulates GABAergic transmission to the dopaminergic neurons of the substantia nigra. Enhances spontaneous, as well as evoked, GABAergic inhibitory postsynaptic currents in dopaminergic neurons. Inhibits cell proliferation and endoplasmic reticulum (ER) stress-induced cell death. Retained in the ER/sarcoplasmic reticulum (SR) through association with the endoplasmic reticulum chaperone protein HSPA5 under normal conditions. Up-regulated and secreted by the ER/SR in response to ER stress and hypoxia. Following secretion by the ER/SR, directly binds to 3-O-sulfogalactosylceramide, a lipid sulfatide in the outer cell membrane of target cells. Sulfatide binding promotes its cellular uptake by endocytosis, and is required for its role in alleviating ER stress and cell toxicity under hypoxic and ER stress conditions. {ECO:0000250|UniProtKB:P0C5H9, ECO:0000250|UniProtKB:P55145}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17507765}. Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:P55145}. Sarcoplasmic reticulum lumen {ECO:0000250|UniProtKB:P55145}. Note=Retained in the endoplasmic reticulum (ER), and sarcoplasmic reticulum (SR) under normal conditions. Up-regulated and secreted by the ER/SR in response to ER stress and hypoxia. {ECO:0000250|UniProtKB:P55145}. DOMAIN: The N-terminal region may be responsible for neurotrophic activity while the C-terminal region may play a role in the ER stress response. {ECO:0000250}. TISSUE SPECIFICITY: Strongly expressed in pancreatic islets and spermatocytes (at protein level). {ECO:0000269|PubMed:17507765}. +Q3ULD5 MCCB_MOUSE Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial (MCCase subunit beta) (EC 6.4.1.4) (3-methylcrotonyl-CoA carboxylase 2) (3-methylcrotonyl-CoA carboxylase non-biotin-containing subunit) (3-methylcrotonyl-CoA:carbon dioxide ligase subunit beta) 563 61,379 Chain (1); Domain (2); Modified residue (7); Region (2); Sequence conflict (1); Transit peptide (1) Amino-acid degradation; L-leucine degradation; (S)-3-hydroxy-3-methylglutaryl-CoA from 3-isovaleryl-CoA: step 2/3. FUNCTION: Carboxyltransferase subunit of the 3-methylcrotonyl-CoA carboxylase, an enzyme that catalyzes the conversion of 3-methylcrotonyl-CoA to 3-methylglutaconyl-CoA, a critical step for leucine and isovaleric acid catabolism. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. SUBUNIT: Probably a dodecamer composed of six biotin-containing alpha subunits (MCCC1) and six beta (MCCC2) subunits. {ECO:0000250}. +Q99MR8 MCCA_MOUSE Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial (MCCase subunit alpha) (EC 6.4.1.4) (3-methylcrotonyl-CoA carboxylase 1) (3-methylcrotonyl-CoA carboxylase biotin-containing subunit) (3-methylcrotonyl-CoA:carbon dioxide ligase subunit alpha) 717 79,344 Active site (1); Binding site (3); Chain (1); Domain (3); Modified residue (7); Sequence conflict (2); Transit peptide (1) Amino-acid degradation; L-leucine degradation; (S)-3-hydroxy-3-methylglutaryl-CoA from 3-isovaleryl-CoA: step 2/3. FUNCTION: Biotin-attachment subunit of the 3-methylcrotonyl-CoA carboxylase, an enzyme that catalyzes the conversion of 3-methylcrotonyl-CoA to 3-methylglutaconyl-CoA, a critical step for leucine and isovaleric acid catabolism. {ECO:0000250}. PTM: Acetylated. {ECO:0000269|PubMed:23438705}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. SUBUNIT: Probably a dodecamer composed of six biotin-containing alpha subunits (MCCC1) and six beta (MCCC2) subunits (By similarity). Interacts (via the biotin carboxylation domain) with SIRT4 (PubMed:23438705). {ECO:0000250|UniProtKB:Q96RQ3, ECO:0000269|PubMed:23438705}. +A6H5Y3 METH_MOUSE Methionine synthase (EC 2.1.1.13) (5-methyltetrahydrofolate--homocysteine methyltransferase) (Vitamin-B12 dependent methionine synthase) (MS) 1253 139,069 Binding site (10); Chain (1); Domain (5); Metal binding (4); Modified residue (1); Region (3); Sequence conflict (1) Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetH route): step 1/1. FUNCTION: Catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Monomer. Dimer. Mainly monomer. Interacts with MTRR. {ECO:0000250|UniProtKB:Q99707}. DOMAIN: Modular enzyme with four functionally distinct domains. The isolated Hcy-binding domain catalyzes methyl transfer from free methylcobalamin to homocysteine. The Hcy-binding domain in association with the pterin-binding domain catalyzes the methylation of cob(I)alamin by methyltetrahydrofolate and the methylation of homocysteine. The B12-binding domain binds the cofactor. The AdoMet activation domain binds S-adenosyl-L-methionine. Under aerobic conditions cob(I)alamin can be converted to inactive cob(II)alamin. Reductive methylation by S-adenosyl-L-methionine and flavodoxin regenerates methylcobalamin (By similarity). {ECO:0000250}. +Q9CQG2 MET16_MOUSE RNA N6-adenosine-methyltransferase METTL16 (Methyltransferase 10 domain-containing protein) (Methyltransferase-like protein 16) (N6-adenosine-methyltransferase METTL16) (EC 2.1.1.348) (U6 small nuclear RNA (adenine-(43)-N(6))-methyltransferase) (EC 2.1.1.346) 553 62,341 Alternative sequence (1); Binding site (6); Chain (1); Modified residue (4); Region (7); Sequence conflict (2) FUNCTION: RNA N6-methyltransferase that methylates adenosine residues at the N(6) position of a subset of RNAs and is involved in S-adenosyl-L-methionine homeostasis by regulating expression of MAT2A transcripts (PubMed:29262316, PubMed:30197299). Able to N6-methylate a subset of mRNAs and U6 small nuclear RNAs (U6 snRNAs) (By similarity). In contrast to the METTL3-METTL14 heterodimer, only able to methylate a limited number of RNAs: requires both a 5'UACAGAGAA-3' nonamer sequence and a specific RNA structure (By similarity). Plays a key role in S-adenosyl-L-methionine homeostasis by mediating N6-methylation of MAT2A mRNAs, altering splicing and/or stability of MAT2A transcripts: in presence of S-adenosyl-L-methionine, binds the 3'-UTR region of MAT2A mRNA and specifically N6-methylates the first hairpin of MAT2A mRNA, impairing MAT2A expression (PubMed:29262316, PubMed:30197299). In S-adenosyl-L-methionine-limiting conditions, binds the 3'-UTR region of MAT2A mRNA but stalls due to the lack of a methyl donor, preventing N6-methylation and promoting expression of MAT2A (PubMed:29262316). In addition to mRNAs, also able to mediate N6-methylation of U6 small nuclear RNA (U6 snRNA): specifically N6-methylates adenine in position 43 of U6 snRNAs (By similarity). Also able to bind various lncRNAs (By similarity). Specifically binds the 3'-end of the MALAT1 long non-coding RNA (By similarity) (PubMed:29262316, PubMed:30197299). {ECO:0000250|UniProtKB:Q86W50, ECO:0000269|PubMed:29262316, ECO:0000269|PubMed:30197299}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q86W50}. SUBUNIT: Interacts with MEPCE. Interacts with LARP7. {ECO:0000250|UniProtKB:Q86W50}. DOMAIN: The VCR (vertebrate conserved) regions bind the first hairpin of MAT2A mRNAs. {ECO:0000250|UniProtKB:Q86W50}.; DOMAIN: The K-loop region occludes the S-adenosyl-L-methionine-binding pocket. Upon activation, conformation of the K-loop changes, allowing S-adenosyl-L-methionine-binding. {ECO:0000250|UniProtKB:Q86W50}. +Q3U2U7 MET17_MOUSE Methyltransferase-like protein 17, mitochondrial (EC 2.1.1.-) (Methyltransferase 11 domain-containing protein 1) (Protein RSM22 homolog, mitochondrial) 461 52,061 Chain (1); Sequence conflict (3); Transit peptide (1) FUNCTION: May be a component of the mitochondrial small ribosomal subunit. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. +Q8BJ51 MFS11_MOUSE UNC93-like protein MFSD11 (Major facilitator superfamily domain-containing protein 11) (Protein ET) 449 49,133 Alternative sequence (1); Chain (1); Glycosylation (1); Modified residue (1); Sequence conflict (6); Transmembrane (12) TRANSMEM 8 28 Helical. {ECO:0000255}.; TRANSMEM 53 73 Helical. {ECO:0000255}.; TRANSMEM 74 94 Helical. {ECO:0000255}.; TRANSMEM 96 116 Helical. {ECO:0000255}.; TRANSMEM 138 158 Helical. {ECO:0000255}.; TRANSMEM 170 190 Helical. {ECO:0000255}.; TRANSMEM 239 259 Helical. {ECO:0000255}.; TRANSMEM 277 297 Helical. {ECO:0000255}.; TRANSMEM 309 329 Helical. {ECO:0000255}.; TRANSMEM 359 379 Helical. {ECO:0000255}.; TRANSMEM 385 405 Helical. {ECO:0000255}.; TRANSMEM 410 430 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9358160}. +Q3U481 MFS12_MOUSE Major facilitator superfamily domain-containing protein 12 476 51,504 Chain (1); Modified residue (1); Sequence conflict (1); Transmembrane (12) TRANSMEM 26 46 Helical. {ECO:0000255}.; TRANSMEM 56 76 Helical. {ECO:0000255}.; TRANSMEM 95 115 Helical. {ECO:0000255}.; TRANSMEM 122 142 Helical. {ECO:0000255}.; TRANSMEM 168 188 Helical. {ECO:0000255}.; TRANSMEM 214 234 Helical. {ECO:0000255}.; TRANSMEM 285 305 Helical. {ECO:0000255}.; TRANSMEM 307 327 Helical. {ECO:0000255}.; TRANSMEM 344 364 Helical. {ECO:0000255}.; TRANSMEM 365 385 Helical. {ECO:0000255}.; TRANSMEM 399 419 Helical. {ECO:0000255}.; TRANSMEM 445 465 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9DC37 MFSD1_MOUSE Major facilitator superfamily domain-containing protein 1 464 51,396 Chain (1); Modified residue (1); Sequence conflict (2); Transmembrane (11) TRANSMEM 38 58 Helical. {ECO:0000255}.; TRANSMEM 82 102 Helical. {ECO:0000255}.; TRANSMEM 112 132 Helical. {ECO:0000255}.; TRANSMEM 134 154 Helical. {ECO:0000255}.; TRANSMEM 214 234 Helical. {ECO:0000255}.; TRANSMEM 265 285 Helical. {ECO:0000255}.; TRANSMEM 303 323 Helical. {ECO:0000255}.; TRANSMEM 330 350 Helical. {ECO:0000255}.; TRANSMEM 360 380 Helical. {ECO:0000255}.; TRANSMEM 391 411 Helical. {ECO:0000255}.; TRANSMEM 417 437 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q7TS68 NSUN6_MOUSE Putative methyltransferase NSUN6 (EC 2.1.1.-) (NOL1/NOP2/Sun domain family member 6) 476 52,279 Active site (1); Binding site (3); Chain (1); Domain (1); Erroneous initiation (1); Modified residue (1); Region (1); Sequence conflict (1) FUNCTION: May have S-adenosyl-L-methionine-dependent methyl-transferase activity. {ECO:0000305}. +Q9QZW9 MNX1_MOUSE Motor neuron and pancreas homeobox protein 1 (Homeobox protein HB9) 404 41,331 Chain (1); Compositional bias (5); DNA binding (1); Modified residue (3); Sequence conflict (1) FUNCTION: Putative transcription factor involved in pancreas development and function. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. +Q9ES57 MO2R1_MOUSE Cell surface glycoprotein CD200 receptor 1 (CD200 cell surface glycoprotein receptor) (Cell surface glycoprotein OX2 receptor 1) 326 35,505 Beta strand (18); Chain (1); Disulfide bond (4); Domain (2); Glycosylation (11); Helix (1); Mutagenesis (1); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (4) TRANSMEM 239 259 Helical. {ECO:0000255}. TOPO_DOM 26 238 Extracellular. {ECO:0000255}.; TOPO_DOM 260 326 Cytoplasmic. {ECO:0000255}. FUNCTION: Inhibitory receptor for the CD200/OX2 cell surface glycoprotein. Limits inflammation by inhibiting the expression of proinflammatory molecules including TNF-alpha, interferons, and inducible nitric oxide synthase (iNOS) in response to selected stimuli. {ECO:0000269|PubMed:12960329, ECO:0000269|PubMed:15187158}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SUBUNIT: CD200 and CD200R1 interact via their respective N-terminal Ig-like domains. {ECO:0000269|PubMed:23602662}. TISSUE SPECIFICITY: Expressed in granulocytes, monocytes, most T-cells and a subset of NK, NKT and B-cells (at protein level). Expressed in the spleen, lung, liver, testis, bone marrow, lymph nodes, spinal cord, kidney, uterus and small intestine. Expressed in mast and dendritic cells. Expressed in the lung of N. brasiliensis-infected mice. {ECO:0000269|PubMed:12960329, ECO:0000269|PubMed:15187158, ECO:0000269|PubMed:15274657, ECO:0000269|PubMed:15471863}. +Q5UKY4 MO2R3_MOUSE Cell surface glycoprotein CD200 receptor 3 (CD200 cell surface glycoprotein receptor-like 3) (CD200 receptor-like 3) (CD200 cell surface glycoprotein receptor-like b) (CD200RLb) (Cell surface glycoprotein OX2 receptor 3) 296 33,625 Alternative sequence (6); Chain (1); Disulfide bond (2); Domain (2); Glycosylation (2); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 246 266 Helical. {ECO:0000255}. TOPO_DOM 26 245 Extracellular. {ECO:0000255}.; TOPO_DOM 267 296 Cytoplasmic. {ECO:0000255}. FUNCTION: According to PubMed:15187158 isoform 4 is a receptor for the CD200 cell surface glycoprotein. According to PubMed:16081818 isoform 4 is not a receptor for the CD200/OX2 cell surface glycoprotein. Isoform 1, isoform 2 and isoform 3 are involved in the recruitment or surface expression of the TYROBP receptor. Isoform 6, isoform 7 and isoform 8 are not involved in the recruitment or surface expression of the TYROBP receptor. {ECO:0000269|PubMed:12960329, ECO:0000269|PubMed:15187158, ECO:0000269|PubMed:15471863, ECO:0000269|PubMed:16081818}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Isoform 3 interacts with TYROBP. Isoform 8 does not interact with TYROBP. {ECO:0000269|PubMed:12960329, ECO:0000269|PubMed:15471863}. TISSUE SPECIFICITY: Expressed in uterus and bone marrow-derived mast cells (at protein level). Expressed in uterus, spleen, bone marrow-derived dendritic, basophil and mast cells. Expressed in the lung of N.brasiliensis-infected mice. Weakly expressed in brain, testis, lung and thymus. {ECO:0000269|PubMed:12960329, ECO:0000269|PubMed:15187158, ECO:0000269|PubMed:15274657, ECO:0000269|PubMed:15471863}. +Q6XJV4 MO2R4_MOUSE Cell surface glycoprotein CD200 receptor 4 (CD200 cell surface glycoprotein receptor-like 4) (CD200 receptor-like 4) (CD200 cell surface glycoprotein receptor-like a) (CD200RLa) (Cell surface glycoprotein OX2 receptor 4) 270 29,625 Beta strand (18); Chain (1); Disulfide bond (4); Domain (2); Glycosylation (3); Helix (1); Mutagenesis (3); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (2) TRANSMEM 242 262 Helical. {ECO:0000255}. TOPO_DOM 26 241 Extracellular. {ECO:0000255}.; TOPO_DOM 263 270 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in the recruitment or surface expression of the TYROBP receptor. {ECO:0000269|PubMed:12960329, ECO:0000269|PubMed:15187158, ECO:0000269|PubMed:15471863, ECO:0000269|PubMed:16081818}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Interacts with TYROBP. {ECO:0000269|PubMed:12960329}. TISSUE SPECIFICITY: Highly expressed in monocytes, NK cells and a subset of NKT cells. Weakly expressed in granulocytes and B-cells (at protein level). Expressed in brain, lung, testis, thymus, intestine and uterus. Expressed in bone marrow derived-macrophage and dendritic cells and mast cells. {ECO:0000269|PubMed:12960329, ECO:0000269|PubMed:15187158, ECO:0000269|PubMed:15274657}. +Q9ERH6 MOAP1_MOUSE Modulator of apoptosis 1 (MAP-1) 352 39,404 Chain (1); Compositional bias (1); Region (2); Sequence conflict (1) FUNCTION: Required for death receptor-dependent apoptosis. When associated with RASSF1, promotes BAX conformational change and translocation to mitochondrial membranes in response to TNF and TNFSF10 stimulation (By similarity). {ECO:0000250}. PTM: Ubiquitinated and degraded during mitotic exit by APC/C-Cdh1, this modification is inhibited by TRIM39. {ECO:0000250}. SUBUNIT: Homodimer. Under normal circumstances, held in an inactive conformation by an intramolecular interaction. Binding to RASSF1 isoform A (RASSF1A) relieves this inhibitory interaction and allows further binding to BAX. Binds also to BCL2 and BCLX. Recruited to the TNFRSF1A and TNFRSF10A complexes in response to their respective cognate ligand, after internalization (By similarity). Interacts with TRIM39 (By similarity). Interacts with RASSF6. {ECO:0000250, ECO:0000269|PubMed:17404571}. DOMAIN: The BH3-like domain is required for association with BAX and for mediating apoptosis. The three BH domains (BH1, BH2, and BH3) of BAX are all required for mediating protein-protein interaction (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed, including in the brain. High expression levels in testis. {ECO:0000269|PubMed:19366867}. +Q80UN9 MOD5_MOUSE tRNA dimethylallyltransferase (EC 2.5.1.75) (Isopentenyl-diphosphate:tRNA isopentenyltransferase) (IPP transferase) (IPPT) (tRNA isopentenyltransferase) (IPTase) 467 52,437 Alternative sequence (1); Chain (1); Modified residue (2); Region (7); Sequence conflict (2); Site (2); Transit peptide (1); Zinc finger (1) FUNCTION: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 of both cytosolic and mitochondrial tRNAs, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A). {ECO:0000250|UniProtKB:Q9H3H1}. SUBCELLULAR LOCATION: Isoform 1: Mitochondrion {ECO:0000250|UniProtKB:Q9H3H1}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}. +Q14CH1 MOCOS_MOUSE Molybdenum cofactor sulfurase (MCS) (MOS) (MoCo sulfurase) (EC 2.8.1.9) (Molybdenum cofactor sulfurtransferase) 862 95,013 Active site (1); Chain (1); Domain (1); Modified residue (3) FUNCTION: Sulfurates the molybdenum cofactor. Sulfation of molybdenum is essential for xanthine dehydrogenase (XDH) and aldehyde oxidase (ADO) enzymes in which molybdenum cofactor is liganded by 1 oxygen and 1 sulfur atom in active form. {ECO:0000255|HAMAP-Rule:MF_03050}. +Q5RKZ7 MOCS1_MOUSE Molybdenum cofactor biosynthesis protein 1 [Includes: GTP 3',8-cyclase (EC 4.1.99.22) (Molybdenum cofactor biosynthesis protein A); Cyclic pyranopterin monophosphate synthase (EC 4.6.1.17) (Molybdenum cofactor biosynthesis protein C)] 636 69,859 Active site (1); Alternative sequence (3); Binding site (8); Chain (1); Erroneous initiation (1); Metal binding (6); Modified residue (3); Region (3); Sequence conflict (3) Cofactor biosynthesis; molybdopterin biosynthesis. FUNCTION: Isoform Mocs1a and isoform Mocs1b probably form a complex that catalyzes the conversion of 5'-GTP to cyclic pyranopterin monophosphate (cPMP). Mocs1a catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate and Mocs1b catalyzes the subsequent conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cPMP. {ECO:0000250|UniProtKB:Q9NZB8}. SUBUNIT: Isoform Mocs1a and isoform Mocs1b probably form a heterooligomer. {ECO:0000250|UniProtKB:Q9NZB8}. +Q5DTZ0 NYNRI_MOUSE Protein NYNRIN (NYN domain and retroviral integrase catalytic domain-containing protein) (Pol-like protein) 1840 203,068 Chain (1); Domain (1); Erroneous gene model prediction (1); Sequence conflict (1); Transmembrane (2) TRANSMEM 1315 1335 Helical. {ECO:0000255}.; TRANSMEM 1351 1371 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8VGS3 O1019_MOUSE Olfactory receptor 1019 (Olfactory receptor 180-1) 310 34,860 Chain (1); Disulfide bond (1); Glycosylation (1); Metal binding (3); Mutagenesis (3); Topological domain (8); Transmembrane (7) TRANSMEM 26 46 Helical; Name=1. {ECO:0000255}.; TRANSMEM 55 75 Helical; Name=2. {ECO:0000255}.; TRANSMEM 100 120 Helical; Name=3. {ECO:0000255}.; TRANSMEM 134 154 Helical; Name=4. {ECO:0000255}.; TRANSMEM 197 217 Helical; Name=5. {ECO:0000255}.; TRANSMEM 238 258 Helical; Name=6. {ECO:0000255}.; TRANSMEM 272 292 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 25 Extracellular. {ECO:0000255}.; TOPO_DOM 47 54 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 76 99 Extracellular. {ECO:0000255}.; TOPO_DOM 121 133 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 155 196 Extracellular. {ECO:0000255}.; TOPO_DOM 218 237 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 259 271 Extracellular. {ECO:0000255}.; TOPO_DOM 293 310 Cytoplasmic. {ECO:0000255}. FUNCTION: Olfactory receptor that is activated by the binding of organosulfur odorants with thioether groups such as (methylthio)methanethiol (MTMT). The activity of this receptor is mediated by G proteins which activate adenylyl cyclase (Probable). {ECO:0000269|PubMed:29659735, ECO:0000305}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:29659735}; Multi-pass membrane protein {ECO:0000255}. +A1L314 MPEG1_MOUSE Macrophage-expressed gene 1 protein (Macrophage gene 1 protein) (Mpg-1) (Protein MPS1) 713 78,390 Chain (1); Domain (1); Frameshift (1); Glycosylation (3); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 654 674 Helical. {ECO:0000255}. TOPO_DOM 20 653 Extracellular. {ECO:0000255}.; TOPO_DOM 675 713 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Specifically expressed in macrophages. {ECO:0000269|PubMed:7888681}. +P30306 MPIP2_MOUSE M-phase inducer phosphatase 2 (EC 3.1.3.48) (Dual specificity phosphatase Cdc25B) 576 65,490 Active site (1); Chain (1); Domain (1); Modified residue (7); Sequence conflict (1) FUNCTION: Tyrosine protein phosphatase which functions as a dosage-dependent inducer of mitotic progression. Required for G2/M phases of the cell cycle progression and abscission during cytokinesis in a ECT2-dependent manner. Directly dephosphorylates CDK1 and stimulates its kinase activity (By similarity). {ECO:0000250}. PTM: Phosphorylated by BRSK1 in vitro. Phosphorylated by CHEK1, which inhibits the activity of this protein. Phosphorylation at Ser-351 by AURKA might locally participate in the control of the onset of mitosis. Phosphorylation by MELK at Ser-167 promotes localization to the centrosome and the spindle poles during mitosis. Phosphorylation at Ser-321 and Ser-372 by MAPK14 is required for binding to 14-3-3 proteins (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P30305}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:P30305}. SUBUNIT: Interacts with MAPK14 and 14-3-3 proteins. {ECO:0000250}. TISSUE SPECIFICITY: Expressed predominantly in spleen, lung, heart, brain, intestine, and muscle. +O88910 MPP3_MOUSE MAGUK p55 subfamily member 3 (Discs large homolog 3) (Protein MPP3) 568 64,401 Chain (1); Domain (5); Modified residue (1); Sequence conflict (4) SUBUNIT: May interact with HTR2A. Interacts (via PDZ domain) with CADM1 (via C-terminus). Interacts with HTR4. {ECO:0000269|PubMed:14988405, ECO:0000269|PubMed:15466885}. TISSUE SPECIFICITY: Expressed in brain, skeletal muscle, testis, kidney, and lung. +Q80XL7 MPPE1_MOUSE Metallophosphoesterase 1 (EC 3.1.-.-) (Post-GPI attachment to proteins factor 5) 396 46,012 Alternative sequence (3); Chain (1); Metal binding (7); Sequence conflict (1); Transmembrane (2) TRANSMEM 28 48 Helical. {ECO:0000255}.; TRANSMEM 356 376 Helical. {ECO:0000255}. FUNCTION: Metallophosphoesterase required for transport of GPI-anchor proteins from the endoplasmic reticulum to the Golgi. Acts in lipid remodeling steps of GPI-anchor maturation by mediating the removal of a side-chain ethanolamine-phosphate (EtNP) from the second Man (Man2) of the GPI intermediate, an essential step for efficient transport of GPI-anchor proteins (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Also localizes to endoplasmic reticulum exit site. {ECO:0000250}. SUBUNIT: Interacts with GPI-anchor proteins. Interacts with TMED10 (By similarity). {ECO:0000250}. +Q3TYA6 MPP8_MOUSE M-phase phosphoprotein 8 858 97,467 Chain (1); Compositional bias (3); Domain (1); Erroneous initiation (1); Modified residue (16); Region (1); Repeat (4); Sequence conflict (1); Site (1) FUNCTION: Heterochromatin component that specifically recognizes and binds methylated 'Lys-9' of histone H3 (H3K9me) and promotes recruitment of proteins that mediate epigenetic repression. Mediates recruitment of the HUSH complex to H3K9me3 sites: the HUSH complex is recruited to genomic loci rich in H3K9me3 and is probably required to maintain transcriptional silencing by promoting recruitment of SETDB1, a histone methyltransferase that mediates further deposition of H3K9me3. Binds H3K9me and promotes DNA methylation by recruiting DNMT3A to target CpG sites; these can be situated within the coding region of the gene. Mediates down-regulation of CDH1 expression. {ECO:0000250|UniProtKB:Q99549}. PTM: Phosphorylated in M (mitotic) phase. Phosphorylation by CDK1 promotes dissociation from chromatin. {ECO:0000250|UniProtKB:Q99549}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23416073}. Chromosome {ECO:0000269|PubMed:23416073}. Note=Detected on heterochromatin (PubMed:23416073). Dissociates from chromatin during interphase and early mitosis (PubMed:23416073). Detected on nucleosomes (By similarity). {ECO:0000250|UniProtKB:Q99549, ECO:0000269|PubMed:23416073}. SUBUNIT: Homodimer. Interacts (via chromo domain) with histone H3K9me3. Has the highest affinity for H3K9me3, and lesser affinity for H3K9me2 and H3K9me1. Component of the HUSH complex; at least composed of FAM208A/TASOR, PPHLN1 and MPHOSPH8. Interacts with DNMT3, EHMT1 and SETDB1. {ECO:0000250|UniProtKB:Q99549}. DOMAIN: The chromo domain mediates interaction with methylated 'Lys-9' of histone H3 (H3K9me), with the highest affinity for the trimethylated form (H3K9me3). {ECO:0000250|UniProtKB:Q99549}. +Q7TM99 MOT9_MOUSE Monocarboxylate transporter 9 (MCT 9) (Solute carrier family 16 member 9) 508 55,757 Chain (1); Frameshift (1); Topological domain (2); Transmembrane (12) TRANSMEM 13 33 Helical. {ECO:0000255}.; TRANSMEM 53 73 Helical. {ECO:0000255}.; TRANSMEM 80 100 Helical. {ECO:0000255}.; TRANSMEM 102 122 Helical. {ECO:0000255}.; TRANSMEM 137 157 Helical. {ECO:0000255}.; TRANSMEM 164 184 Helical. {ECO:0000255}.; TRANSMEM 303 323 Helical. {ECO:0000255}.; TRANSMEM 341 361 Helical. {ECO:0000255}.; TRANSMEM 370 390 Helical. {ECO:0000255}.; TRANSMEM 396 416 Helical. {ECO:0000255}.; TRANSMEM 431 451 Helical. {ECO:0000255}.; TRANSMEM 460 480 Helical. {ECO:0000255}. TOPO_DOM 1 12 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 481 508 Cytoplasmic. {ECO:0000255}. FUNCTION: Proton-linked monocarboxylate transporter. May catalyze the transport of monocarboxylates across the plasma membrane. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +P97434 MPRIP_MOUSE Myosin phosphatase Rho-interacting protein (Rho-interacting protein 3) (RIP3) (p116Rip) 1024 116,408 Alternative sequence (4); Chain (1); Coiled coil (1); Compositional bias (1); Domain (2); Erroneous initiation (1); Modified residue (21); Mutagenesis (3); Region (3); Sequence conflict (8) FUNCTION: Targets myosin phosphatase to the actin cytoskeleton. Required for the regulation of the actin cytoskeleton by RhoA and ROCK1. Depletion leads to an increased number of stress fibers in smooth muscle cells through stabilization of actin fibers by phosphorylated myosin. Overexpression of MRIP as well as its F-actin-binding region leads to disassembly of stress fibers in neuronal cells. {ECO:0000269|PubMed:12732640, ECO:0000269|PubMed:15469989}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12732640}. Note=Colocalizes with F-actin. SUBUNIT: Binds RHOA, PPP1R12A/MBS and PPP1R12C/MBS85 through adjacent coiled coil domains. Interacts with MYZAP. Binds F-actin through its N-terminus. {ECO:0000269|PubMed:12732640, ECO:0000269|PubMed:15469989, ECO:0000269|PubMed:20093627, ECO:0000269|PubMed:9199174}. TISSUE SPECIFICITY: Expressed in Kidney, Brain, Heart and Lung. {ECO:0000269|PubMed:9199174}. +Q9CXT8 MPPB_MOUSE Mitochondrial-processing peptidase subunit beta (EC 3.4.24.64) (Beta-MPP) (P-52) 489 54,614 Active site (1); Chain (1); Metal binding (3); Transit peptide (1) FUNCTION: Catalytic subunit of the essential mitochondrial processing protease (MPP), which is required for maturation of the majority of mitochondrial precursor proteins (By similarity). Most MPP cleavage sites follow an arginine at position -2 (By similarity). {ECO:0000250|UniProtKB:O75439, ECO:0000250|UniProtKB:P20069}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. SUBUNIT: Heterodimer of PMPCA (alpha) and PMPCB (beta) subunits, forming the mitochondrial processing protease (MPP) in which PMPCA is involved in substrate recognition and binding and PMPCB is the catalytic subunit. {ECO:0000250}. +Q9CXD9 LRC17_MOUSE Leucine-rich repeat-containing protein 17 443 51,852 Chain (1); Domain (3); Repeat (6); Signal peptide (1) FUNCTION: Involved in bone homeostasis. Acts as a negative regulator of RANKL-induced osteoclast precursor differentiation from bone marrow precursors. {ECO:0000269|PubMed:19336404}. SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000269|PubMed:19336404}. TISSUE SPECIFICITY: Expressed in osteoblasts, spleen, lung and heart. {ECO:0000269|PubMed:19336404}. +A6H694 LRC63_MOUSE Leucine-rich repeat-containing protein 63 637 71,451 Chain (1); Compositional bias (2); Erroneous initiation (1); Repeat (7); Sequence conflict (2) +Q9DAP0 LRC46_MOUSE Leucine-rich repeat-containing protein 46 323 36,048 Chain (1); Coiled coil (1); Compositional bias (1); Domain (1); Modified residue (5); Repeat (4); Sequence conflict (1) +Q5DU41 LRC8B_MOUSE Volume-regulated anion channel subunit LRRC8B (Leucine-rich repeat-containing protein 8B) (T-cell activation leucine repeat-rich protein) (TA-LRRP) 803 92,186 Alternative sequence (1); Chain (1); Disulfide bond (2); Erroneous initiation (1); Glycosylation (1); Modified residue (2); Repeat (15); Topological domain (5); Transmembrane (4) TRANSMEM 26 46 Helical. {ECO:0000255}.; TRANSMEM 120 140 Helical. {ECO:0000255}.; TRANSMEM 262 282 Helical. {ECO:0000255}.; TRANSMEM 308 328 Helical. {ECO:0000255}. TOPO_DOM 1 25 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 47 119 Extracellular. {ECO:0000255}.; TOPO_DOM 141 261 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 283 307 Extracellular. {ECO:0000255}.; TOPO_DOM 329 803 Cytoplasmic. {ECO:0000255}. FUNCTION: Non-essential component of the volume-regulated anion channel (VRAC, also named VSOAC channel), an anion channel required to maintain a constant cell volume in response to extracellular or intracellular osmotic changes. The VRAC channel conducts iodide better than chloride and can also conduct organic osmolytes like taurine. Channel activity requires LRRC8A plus at least one other family member (LRRC8B, LRRC8C, LRRC8D or LRRC8E); channel characteristics depend on the precise subunit composition. {ECO:0000250|UniProtKB:Q6P9F7}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6P9F7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q6P9F7}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q6P9F7}. Note=In the absence of LRRC8A, resides primarily in a cytoplasmic compartment, probably the endoplasmic reticulum. Requires LRRC8A for expression at the cell membrane. {ECO:0000250|UniProtKB:Q6P9F7}. SUBUNIT: Heterohexamer. Oligomerizes with other LRRC8 proteins (LRRC8A, LRRC8C, LRRC8D and/or LRRC8E) to form a heterohexamer (PubMed:24782309). In vivo, the subunit composition may depend primarily on expression levels, and heterooligomeric channels containing various proportions of the different LRRC8 proteins may coexist (Probable). {ECO:0000269|PubMed:24782309, ECO:0000305}. +Q3UV48 LRC30_MOUSE Leucine-rich repeat-containing protein 30 300 33,931 Chain (1); Repeat (10) +G3XA59 LRC32_MOUSE Transforming growth factor beta activator LRRC32 (Garpin) (Glycoprotein A repetitions predominant) (GARP) (Leucine-rich repeat-containing protein 32) 663 72,418 Chain (1); Disulfide bond (2); Domain (2); Glycosylation (6); Repeat (21); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 629 649 Helical. {ECO:0000255}. TOPO_DOM 18 628 Extracellular. {ECO:0000305}.; TOPO_DOM 650 663 Cytoplasmic. {ECO:0000305}. FUNCTION: Key regulator of transforming growth factor beta (TGFB1, TGFB2 and TGFB3) that controls TGF-beta activation by maintaining it in a latent state during storage in extracellular space (PubMed:25127859). Associates specifically via disulfide bonds with the Latency-associated peptide (LAP), which is the regulatory chain of TGF-beta, and regulates integrin-dependent activation of TGF-beta (PubMed:25127859, PubMed:28912269). Able to outcompete LTBP1 for binding to LAP regulatory chain of TGF-beta (By similarity). Controls activation of TGF-beta-1 (TGFB1) on the surface of activated regulatory T-cells (Tregs) (PubMed:25127859). Required for epithelial fusion during palate development by regulating activation of TGF-beta-3 (TGFB3) (PubMed:28912269). {ECO:0000250|UniProtKB:Q14392, ECO:0000269|PubMed:25127859, ECO:0000269|PubMed:28912269}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q14392}; Single-pass type I membrane protein {ECO:0000255}. Cell surface {ECO:0000250|UniProtKB:Q14392}. SUBUNIT: Interacts with TGFB1; associates via disulfide bonds with the Latency-associated peptide chain (LAP) regulatory chain of TGFB1, leading to regulate activation of TGF-beta-1 (By similarity). Interacts with TGFB2 (By similarity). Interacts with TGFB3; associates via disulfide bonds with the Latency-associated peptide chain (LAP) regulatory chain of TGFB3, leading to regulate activation of TGF-beta-3 (PubMed:28912269). Interacts with LAPTM4B; decreases TGFB1 production in regulatory T-cells (By similarity). {ECO:0000250|UniProtKB:Q14392, ECO:0000269|PubMed:28912269}. TISSUE SPECIFICITY: Present in medial edge epithelial cells at E14.5 (at protein level). {ECO:0000269|PubMed:28912269}. +Q60664 LRMP_MOUSE Lymphoid-restricted membrane protein (Protein Jaw1) [Cleaved into: Processed lymphoid-restricted membrane protein] 539 59,588 Chain (2); Coiled coil (1); Modified residue (4); Mutagenesis (1); Sequence conflict (6); Topological domain (2); Transmembrane (1) TRANSMEM 480 500 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 1 479 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 501 539 Lumenal. {ECO:0000255}. FUNCTION: Plays a role in the delivery of peptides to major histocompatibility complex (MHC) class I molecules; this occurs in a transporter associated with antigen processing (TAP)-independent manner. May play a role in taste signal transduction via ITPR3. May play a role during fertilization in pronucleus congression and fusion. {ECO:0000269|PubMed:9314557}. PTM: The removal of the C-terminal lumenal domain occurs by proteolytic processing. {ECO:0000269|PubMed:8798562, ECO:0000269|PubMed:9314557}. SUBCELLULAR LOCATION: Processed lymphoid-restricted membrane protein: Cytoplasm.; SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type IV membrane protein. Membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}. Nucleus envelope {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. Chromosome {ECO:0000250}. Note=Colocalized with ITPR3 on the endoplasmic reticulum membrane. SUBUNIT: Interacts (via coiled-coil domain) with ITPR3. {ECO:0000269|PubMed:20071408}. TISSUE SPECIFICITY: Spleen and thymus. Expressed at high levels in pre B-cells, mature B-cells and pre T-cells. Expressed at low levels in mature T-cells and plasma B-cells. Expressed in circumvallate (CV), foliate (FL) and fungiform (FF) taste papillae cells of the tongue epithelium. {ECO:0000269|PubMed:20071408, ECO:0000269|PubMed:8021504}. +Q69ZB0 LRCC1_MOUSE Leucine-rich repeat and coiled-coil domain-containing protein 1 1026 119,169 Alternative sequence (3); Chain (1); Coiled coil (1); Domain (1); Erroneous initiation (1); Frameshift (2); Repeat (5); Sequence caution (2); Sequence conflict (17) FUNCTION: Required for the organization of the mitotic spindle. Maintains the structural integrity of centrosomes during mitosis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Note=Associates with the centrosome throughout the cell cycle and extensively accumulates during the mitotic phase. {ECO:0000250}. +Q8K375 LRC56_MOUSE Leucine-rich repeat-containing protein 56 552 60,483 Chain (1); Erroneous initiation (1); Repeat (5) +Q3V0M2 LRC36_MOUSE Leucine-rich repeat-containing protein 36 755 83,763 Alternative sequence (2); Chain (1); Coiled coil (1); Compositional bias (1); Domain (1); Repeat (2) +Q8VC85 LSM1_MOUSE U6 snRNA-associated Sm-like protein LSm1 133 15,236 Chain (1); Modified residue (2) FUNCTION: Plays a role in the degradation of histone mRNAs, the only eukaryotic mRNAs that are not polyadenylated (By similarity). Probably also part of an LSm subunits-containing complex involved in the general process of mRNA degradation (By similarity). {ECO:0000250|UniProtKB:O15116, ECO:0000250|UniProtKB:P47017}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O15116}. Cytoplasm, P-body {ECO:0000250|UniProtKB:O15116}. SUBUNIT: Interacts with SLBP; interaction with SLBP occurs when histone mRNA is being rapidly degraded during the S phase (By similarity). LSm subunits form a heteromer with a donut shape (By similarity). {ECO:0000250|UniProtKB:O15116, ECO:0000250|UniProtKB:P47017}. +Q91WK0 LRRF2_MOUSE Leucine-rich repeat flightless-interacting protein 2 (LRR FLII-interacting protein 2) 415 47,148 Alternative sequence (1); Chain (1); Coiled coil (3); Modified residue (9); Sequence conflict (1) FUNCTION: May function as activator of the canonical Wnt signaling pathway, in association with DVL3, upstream of CTNNB1/beta-catenin. Positively regulates Toll-like receptor (TLR) signaling in response to agonist probably by competing with the negative FLII regulator for MYD88-binding (By similarity). {ECO:0000250}. SUBUNIT: Interacts with DVL3 and FLII (By similarity). Weakly interacts with MYD88 in resting cells. Following LPS-stimulation, the interaction with MYD88 is rapidly enhanced; the complex gradually dissociates to basal levels after 6 hours of stimulation. Interaction with MYD88 is regulated by LPS-induced phosphorylation. In the presence of LPS, competes with FLII for MYD88-binding (By similarity). {ECO:0000250}. +O35900 LSM2_MOUSE U6 snRNA-associated Sm-like protein LSm2 (Protein G7b) (snRNP core Sm-like protein Sm-x5) 95 10,835 Chain (1); Modified residue (1) FUNCTION: Plays role in pre-mRNA splicing as component of the U4/U6-U5 tri-snRNP complex that is involved in spliceosome assembly, and as component of the precatalytic spliceosome (spliceosome B complex). The heptameric LSM2-8 complex binds specifically to the 3'-terminal U-tract of U6 snRNA. {ECO:0000250|UniProtKB:Q9Y333}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y333}. SUBUNIT: Component of the precatalytic spliceosome (spliceosome B complex). Component of the U4/U6-U5 tri-snRNP complex, a building block of the precatalytic spliceosome (spliceosome B complex). The U4/U6-U5 tri-snRNP complex is composed of the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39, plus LSM2, LSM3, LSM4, LSM5, LSM6, LSM7 and LSM8. LSM2, LSM3, LSM4, LSM5, LSM6, LSM7 and LSM8 form a heptameric, ring-shaped subcomplex (the LSM2-8 complex) that is part of the U4/U6-U5 tri-snRNP complex and the precatalytic spliceosome. {ECO:0000250|UniProtKB:Q9Y333}. +Q3UM18 LSG1_MOUSE Large subunit GTPase 1 homolog (EC 3.6.1.-) 644 73,157 Alternative sequence (1); Chain (1); Domain (1); Modified residue (2); Nucleotide binding (3); Sequence conflict (6) FUNCTION: GTPase required for the XPO1/CRM1-mediated nuclear export of the 60S ribosomal subunit. Probably acts by mediating the release of NMD3 from the 60S ribosomal subunit after export into the cytoplasm (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Note=Shuttles between the Cajal bodies in the nucleus and the endoplasmic reticulum. {ECO:0000250}. DOMAIN: In contrast to other GTP-binding proteins, this family is characterized by a circular permutation of the GTPase motifs described by a G4-G1-G3 pattern. +Q8BUI3 LRWD1_MOUSE Leucine-rich repeat and WD repeat-containing protein 1 (ORC-associated protein) (ORCA) (Origin recognition complex-associated protein) 648 71,594 Chain (1); Modified residue (1); Repeat (9); Sequence caution (2) FUNCTION: Required for G1/S transition. Recruits and stabilizes the origin recognition complex (ORC) onto chromatin during G1 to establish pre-replication complex (preRC) and to heterochromatic sites in post-replicated cells. Binds a combination of DNA and histone methylation repressive marks on heterochromatin. Binds histone H3 and H4 trimethylation marks H3K9me3, H3K27me3 and H4K20me3 in a cooperative manner with DNA methylation (By similarity). Required for silencing of major satellite repeats. May be important ORC2, ORC3 and ORC4 stability. {ECO:0000250, ECO:0000269|PubMed:22427655}. PTM: Ubiquitinated; undergoes 'Lys-48'-linked polyubiquitination leading to proteasomal degradation. Ubiquitination occurs within the WD repeats at the end of the G1 phase. Ubiquitination may be catalyzed by the CUL4-DDB1 E3 ubiquitin-protein ligase complex and other E3 ligases (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UFC0}. Chromosome, centromere {ECO:0000250|UniProtKB:Q9UFC0}. Chromosome, telomere {ECO:0000250|UniProtKB:Q9UFC0}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:20180869}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q9UFC0}. Note=Localizes to heterochromatin during G1 phase. Restricted to centromeres or telomeres as cells progress though S phase. When cells enter mitosis, relocalizes to centromeres. Recruitment to pericentric heterochromatin largely depends on the presence of H3K9me3. {ECO:0000250|UniProtKB:Q9UFC0}. SUBUNIT: Integral component of the ORC complex (By similarity). Directly interacts with CDT1, GMNN and ORC2. Interacts with ORC2 only when non-ubiquitinated; this interaction prevents LRWD1 ubiquitination and degradation. Some of these interactions are regulated in a cell-cycle dependent manner. Interaction with ORC1 occurs predominantly during G1. Association with phosphorylated ORC1 during mitosis is not efficient. Interaction with CDT1 occurs during G1 phase, as well as during mitosis with phosphorylated CDT1. Interaction with GMNN occurs from G1/S to mitosis. Interaction with ORC2 is observed throughout the cell cycle. The stoichiometry of the ORCA/ORC/CDT1/GMNN complex is 1:1:1:2 (By similarity). Interacts with CUL4A and DDB1; this interaction may lead to ubiquitination (By similarity). {ECO:0000250}. DOMAIN: The entire WD repeat region is required for the interaction with ORC, CDT1 and GMNN, as well as for association with chromatin and for binding to histone H3 and H4 trimethylation marks H3K9me3 and H4K20me3 (By similarity). Centrosomal localization requires additional conformation. {ECO:0000250}. TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:17074343}. +Q9QXA5 LSM4_MOUSE U6 snRNA-associated Sm-like protein LSm4 137 15,076 Chain (1); Modified residue (1) FUNCTION: Plays role in pre-mRNA splicing as component of the U4/U6-U5 tri-snRNP complex that is involved in spliceosome assembly, and as component of the precatalytic spliceosome (spliceosome B complex). The heptameric LSM2-8 complex binds specifically to the 3'-terminal U-tract of U6 snRNA. {ECO:0000250|UniProtKB:Q9Y4Z0}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10629062}. SUBUNIT: Component of the precatalytic spliceosome (spliceosome B complex). Component of the U4/U6-U5 tri-snRNP complex, a building block of the precatalytic spliceosome (spliceosome B complex). The U4/U6-U5 tri-snRNP complex is composed of the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39, plus LSM2, LSM3, LSM4, LSM5, LSM6, LSM7 and LSM8. LSM2, LSM3, LSM4, LSM5, LSM6, LSM7 and LSM8 form a heptameric, ring-shaped subcomplex (the LSM2-8 complex) that is part of the U4/U6-U5 tri-snRNP complex and the precatalytic spliceosome. {ECO:0000250|UniProtKB:Q9Y4Z0}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10629062}. +O08843 LST1_MOUSE Leukocyte-specific transcript 1 protein (Protein B144) 95 10,325 Alternative sequence (1); Chain (1); Erroneous gene model prediction (1); Frameshift (1); Modified residue (1); Sequence conflict (7); Transmembrane (1) TRANSMEM 22 42 Helical. {ECO:0000255}. FUNCTION: Possible role in modulating immune responses. Has an inhibitory effect on lymphocyte proliferation. Induces morphological changes including production of filopodia and microspikes when overexpressed in a variety of cell types and may be involved in dendritic cell maturation. {ECO:0000250|UniProtKB:O00453, ECO:0000269|PubMed:11478849, ECO:0000303|PubMed:11478849}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=Also detected in a perinuclear region corresponding to the localization of the Golgi apparatus and throughout the cytoplasm. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in spleen and at lower levels in thymus and liver. {ECO:0000269|PubMed:11478849}. +Q60860 LTC4S_MOUSE Leukotriene C4 synthase (LTC4 synthase) (EC 4.4.1.20) (Leukotriene-C(4) synthase) 150 16,814 Active site (2); Binding site (1); Chain (1); Helix (6); Region (3); Topological domain (5); Transmembrane (4) TRANSMEM 7 27 Helical. {ECO:0000250}.; TRANSMEM 49 69 Helical. {ECO:0000250}.; TRANSMEM 74 94 Helical. {ECO:0000250}.; TRANSMEM 105 124 Helical. {ECO:0000250}. TOPO_DOM 1 6 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 28 48 Lumenal. {ECO:0000250}.; TOPO_DOM 70 73 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 95 104 Lumenal. {ECO:0000250}.; TOPO_DOM 125 150 Cytoplasmic. {ECO:0000250}. FUNCTION: Catalyzes the conjugation of leukotriene A4 with reduced glutathione to form leukotriene C4. SUBCELLULAR LOCATION: Nucleus outer membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Homotrimer. Interacts with ALOX5AP and ALOX5 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:8706658}. +P08923 LTK_MOUSE Leukocyte tyrosine kinase receptor (EC 2.7.10.1) 888 94,471 Active site (1); Alternative sequence (3); Binding site (1); Chain (1); Domain (1); Erroneous initiation (1); Glycosylation (2); Modified residue (1); Natural variant (1); Nucleotide binding (1); Sequence conflict (6); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 422 446 Helical. {ECO:0000255}. TOPO_DOM 17 421 Extracellular. {ECO:0000255}.; TOPO_DOM 447 888 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor with a tyrosine-protein kinase activity. The exact function of this protein is not known. Studies with chimeric proteins (replacing its extracellular region with that of several known growth factor receptors, such as EGFR and CSFIR) demonstrate its ability to promote growth and specifically neurite outgrowth, and cell survival. Signaling appears to involve the PI3 kinase pathway. Involved in regulation of the secretory pathway involving endoplasmic reticulum (ER) export sites (ERESs) and ER to Golgi transport (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8995435}; Single-pass type I membrane protein {ECO:0000269|PubMed:8995435}.; SUBCELLULAR LOCATION: Isoform A: Endoplasmic reticulum. Note=Retained in the endoplasmic reticulum.; SUBCELLULAR LOCATION: Isoform B: Endoplasmic reticulum. Note=Retained in the endoplasmic reticulum. SUBUNIT: Homodimer when bound to ligand (Probable). Part of a complex including LTK, TNK2 and GRB2, in which GRB2 promotes LTK recruitment by TNK2 (By similarity). Isoform A binds calnexin. {ECO:0000250, ECO:0000305}. TISSUE SPECIFICITY: Subsets of lymphoid and neuronal cells. +Q924L1 LTMD1_MOUSE LETM1 domain-containing protein 1 (Cervical cancer receptor) (MCC-32) 360 41,701 Alternative sequence (2); Chain (1); Domain (1); Modified residue (1); Region (1); Sequence conflict (3); Topological domain (2); Transmembrane (1) TRANSMEM 138 158 Helical. {ECO:0000255}. TOPO_DOM 1 137 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 159 360 Mitochondrial intermembrane. {ECO:0000255}. FUNCTION: Involved in tumorigenesis and may function as a negative regulator of the p53/TP53. {ECO:0000269|PubMed:12879013}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with BRI3BP. {ECO:0000250}. +Q8BHC0 LYVE1_MOUSE Lymphatic vessel endothelial hyaluronic acid receptor 1 (LYVE-1) (Cell surface retention sequence-binding protein 1) (CRSBP-1) (Extracellular link domain-containing protein 1) 318 34,574 Chain (1); Disulfide bond (2); Domain (1); Glycosylation (2); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 235 255 Helical. {ECO:0000255}. TOPO_DOM 24 234 Extracellular. {ECO:0000255}.; TOPO_DOM 256 318 Cytoplasmic. {ECO:0000255}. FUNCTION: Ligand-specific transporter trafficking between intracellular organelles (TGN) and the plasma membrane. Plays a role in autocrine regulation of cell growth mediated by growth regulators containing cell surface retention sequence binding (CRS). May act as a hyaluronan (HA) transporter, either mediating its uptake for catabolism within lymphatic endothelial cells themselves, or its transport into the lumen of afferent lymphatic vessels for subsequent re-uptake and degradation in lymph nodes. {ECO:0000269|PubMed:10187853}. PTM: O-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10187853}; Single-pass type I membrane protein {ECO:0000269|PubMed:10187853}. Note=Localized to the plasma membrane and in vesicles near extranuclear membranes which may represent trans-Golgi network (TGN) and endosomes/prelysosomeal compartments. Undergoes ligand-dependent internalization and recycling at the cell surface. SUBUNIT: Homodimer; disulfide-linked. Interacts with PDGFB and IGFBP3. Forms a transient ternary complex with PDGFB and PDGFRB in TGN. {ECO:0000269|PubMed:10187853}. +Q9JHQ5 LZTL1_MOUSE Leucine zipper transcription factor-like protein 1 299 34,773 Chain (1); Coiled coil (1); Frameshift (1); Region (1); Sequence conflict (2) FUNCTION: Regulates ciliary localization of the BBSome complex. Together with the BBSome complex, controls SMO ciliary trafficking and contributes to the sonic hedgehog (SHH) pathway regulation. May play a role in neurite outgrowth. May have tumor suppressor function. {ECO:0000269|PubMed:20233871, ECO:0000269|PubMed:22093827}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22072986, ECO:0000269|PubMed:22093827}. SUBUNIT: Self-associates. Interacts with BBS9; the interaction mediates the association of LZTL1 with the BBsome complex and regulates BBSome ciliary trafficking. TISSUE SPECIFICITY: Highly expressed in testis. Expressed in brain, cerebellum, eye, heart, kidney, liver, lung and trachea. In small intestine, graded expression along the crypt-villus axis with high levels in the villus apex and lower levels in the crypt stem cells (at protein level). Not expressed in skeletal muscle and white adipose tissue. {ECO:0000269|PubMed:11352561, ECO:0000269|PubMed:20233871, ECO:0000269|PubMed:22072986, ECO:0000269|PubMed:22093827}. +Q8R2G4 NAR3_MOUSE Ecto-ADP-ribosyltransferase 3 (EC 2.4.2.31) (ADP-ribosyltransferase C2 and C3 toxin-like 3) (ARTC3) (Mono(ADP-ribosyl)transferase 3) (NAD(P)(+)--arginine ADP-ribosyltransferase 3) 371 42,015 Active site (1); Alternative sequence (2); Binding site (2); Chain (1); Disulfide bond (1); Erroneous gene model prediction (1); Lipidation (1); Propeptide (1); Sequence caution (4); Sequence conflict (2); Signal peptide (1) SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. +Q9Z1P6 NDUA7_MOUSE NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7 (Complex I-B14.5a) (CI-B14.5a) (NADH-ubiquinone oxidoreductase subunit B14.5a) 113 12,576 Beta strand (4); Chain (1); Helix (3); Initiator methionine (1); Modified residue (3); Turn (2) FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. {ECO:0000250|UniProtKB:O95182}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:O95182}; Peripheral membrane protein {ECO:0000250|UniProtKB:O95182}; Matrix side {ECO:0000250|UniProtKB:O95182}. SUBUNIT: Complex I is composed of 45 different subunits. {ECO:0000250|UniProtKB:O95182}. +Q61084 M3K3_MOUSE Mitogen-activated protein kinase kinase kinase 3 (EC 2.7.11.25) (MAPK/ERK kinase kinase 3) (MEK kinase 3) (MEKK 3) 626 70,776 Active site (1); Binding site (1); Chain (1); Domain (2); Modified residue (6); Nucleotide binding (1) FUNCTION: Component of a protein kinase signal transduction cascade. Mediates activation of the NF-kappa-B, AP1 and DDIT3 transcriptional regulators. {ECO:0000269|PubMed:8621389}. PTM: Phosphorylation at Ser-166 and Ser-337 by SGK1 inhibits its activity. {ECO:0000250}. SUBUNIT: Binds both upstream activators and downstream substrates in multimolecular complexes. Part of a complex with MAP2K3, RAC1 and CCM2. Interacts with MAP2K5 and SPAG9. {ECO:0000269|PubMed:12391307, ECO:0000269|PubMed:14634666}. +Q14BB9 MA6D1_MOUSE MAP6 domain-containing protein 1 (21 kDa STOP-like protein) (SL21) 191 20,433 Chain (1); Erroneous initiation (1); Frameshift (2); Lipidation (3); Modified residue (3); Sequence conflict (1) FUNCTION: May have microtubule-stabilizing activity. PTM: Palmitoylated. Palmitoylation enhances association with microtubules (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:16837464}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16837464}. Note=According to PubMed:16837464, it colocalizes with microtubules. SUBUNIT: Interacts with calmodulin. {ECO:0000269|PubMed:16837464}. TISSUE SPECIFICITY: Expressed in brain. Found in neurons in primary cultures, but absent in glial cells. {ECO:0000269|PubMed:16837464}. +Q8BHE8 MAIP1_MOUSE m-AAA protease-interacting protein 1, mitochondrial (Matrix AAA peptidase-interacting protein 1) 291 32,985 Chain (1); Erroneous initiation (1); Transit peptide (1) FUNCTION: Promotes sorting of SMDT1/EMRE in mitochondria by ensuring its maturation. Interacts with the transit peptide region of SMDT1/EMRE precursor protein in the mitochondrial matrix, leading to protect it against protein degradation by YME1L1, thereby ensuring SMDT1/EMRE maturation by the mitochondrial processing peptidase (PMPCA and PMPCB). {ECO:0000250|UniProtKB:Q8WWC4}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:Q8WWC4}. SUBUNIT: Interacts with AFG3L2 (PubMed:27642048). Interacts with SPG7 (By similarity). Interacts with SMDT1/EMRE (via the N-terminal transit peptide); interaction is direct and takes place before maturation of SMDT1/EMRE (By similarity). {ECO:0000250|UniProtKB:Q8WWC4, ECO:0000269|PubMed:27642048}. +Q9JKL4 NDUF3_MOUSE NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 3 (Protein 2P1) 185 20,734 Chain (1); Sequence conflict (1) FUNCTION: Essential factor for the assembly of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Mitochondrion inner membrane {ECO:0000250}. SUBUNIT: Interacts with NDUFAF4, NDUFS2 and NDUFS3. {ECO:0000250}. TISSUE SPECIFICITY: Strongly expressed in testis and weakly expressed in the epididymis. Expressed in spermatocytes. {ECO:0000269|PubMed:12653254}. +A2AG50 MA7D2_MOUSE MAP7 domain-containing protein 2 781 86,050 Alternative sequence (4); Chain (1); Coiled coil (1); Frameshift (1) +Q9D992 MAJIN_MOUSE Membrane-anchored junction protein 256 29,175 Alternative sequence (1); Chain (1); Mutagenesis (1); Topological domain (2); Transmembrane (1) TRANSMEM 233 251 Helical. {ECO:0000255}. TOPO_DOM 1 232 Nuclear. {ECO:0000305}.; TOPO_DOM 252 256 Perinuclear space. {ECO:0000305}. FUNCTION: Meiosis-specific telomere-associated protein involved in meiotic telomere attachment to the nucleus inner membrane, a crucial step for homologous pairing and synapsis. Component of the MAJIN-TERB1-TERB2 complex, which promotes telomere cap exchange by mediating attachment of telomeric DNA to the inner nuclear membrane and replacement of the protective cap of telomeric chromosomes: in early meiosis, the MAJIN-TERB1-TERB2 complex associates with telomeric DNA and the shelterin/telosome complex. During prophase, the complex matures and promotes release of the shelterin/telosome complex from telomeric DNA. In the complex, MAJIN acts as the anchoring subunit to the nucleus inner membrane. MAJIN shows DNA-binding activity, possibly for the stabilization of telomere attachment on the nucleus inner membrane. {ECO:0000269|PubMed:26548954}. SUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000269|PubMed:26548954}; Single-pass membrane protein {ECO:0000305|PubMed:26548954}. Chromosome, telomere {ECO:0000269|PubMed:26548954}. Note=Localizes to telomeres throughout meiotic prophase I and disapears in metaphase I. In leptotene spermatocytes, localizes to telomeres that localize to the nucleus inner membrane. {ECO:0000269|PubMed:26548954}. SUBUNIT: Component of the MAJIN-TERB1-TERB2 complex, composed of MAJIN, TERB1 and TERB2. {ECO:0000269|PubMed:26548954}. TISSUE SPECIFICITY: Specifically expressed in germline tissues. {ECO:0000269|PubMed:26548954}. +Q04859 MAK_MOUSE Serine/threonine-protein kinase MAK (EC 2.7.11.1) (Male germ cell-associated kinase) (Protein kinase RCK) 622 70,080 Active site (1); Alternative sequence (3); Binding site (1); Chain (1); Compositional bias (1); Domain (1); Modified residue (2); Nucleotide binding (1); Sequence conflict (3) FUNCTION: Essential for the regulation of ciliary length and required for the long-term survival of photoreceptors. Could have an important function in sensory cells and in spermatogenesis. May participate in signaling pathways used in visual and olfactory sensory transduction. Phosphorylates FZR1 in a cell cycle-dependent manner. Plays a role in the transcriptional coactivation of AR (By similarity). {ECO:0000250, ECO:0000269|PubMed:21148103}. PTM: Autophosphorylated. Phosphorylated on serine and threonine residues (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Midbody {ECO:0000250}. Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:21148103}. Photoreceptor inner segment {ECO:0000250}. Note=Localizes in both the connecting cilia and the outer segment axonemes. SUBUNIT: Interacts with AR and CDK20. Found in a complex containing MAK, AR and NCOA3. Interacts with FZR1 (via WD repeats) (By similarity). Interacts with RP1. {ECO:0000250, ECO:0000269|PubMed:21148103}. TISSUE SPECIFICITY: In pre- and postmeiotic male germ cells in testis. In photoreceptor cells of the retina and in the olfactory receptors, and in certain epithelia of the respiratory tract and choroid plexus (brain). {ECO:0000269|PubMed:21148103}. +Q3UU94 MANS4_MOUSE MANSC domain-containing protein 4 337 36,857 Chain (1); Domain (1); Glycosylation (3); Sequence conflict (12); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 279 299 Helical. {ECO:0000255}. TOPO_DOM 19 278 Extracellular. {ECO:0000255}.; TOPO_DOM 300 337 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q8BP48 MAP11_MOUSE Methionine aminopeptidase 1 (MAP 1) (MetAP 1) (EC 3.4.11.18) (Peptidase M 1) 386 43,221 Binding site (2); Chain (1); Initiator methionine (1); Metal binding (7); Modified residue (1); Region (1) FUNCTION: Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). {ECO:0000255|HAMAP-Rule:MF_03174}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03174}. SUBUNIT: Associates with the 60S ribosomal subunit of the 80S translational complex. {ECO:0000255|HAMAP-Rule:MF_03174}. +Q0MW30 NEU1B_MOUSE E3 ubiquitin-protein ligase NEURL1B (EC 2.3.2.27) (Neuralized-2) (NEUR2) (Neuralized-like protein 1B) (Neuralized-like protein 2) (Neuralized-like protein 3) (RING-type E3 ubiquitin transferase NEURL1B) 546 58,527 Chain (1); Compositional bias (1); Domain (2); Modified residue (1); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase involved in regulation of the Notch pathway through influencing the stability and activity of several Notch ligands. {ECO:0000269|PubMed:17003037, ECO:0000269|PubMed:19723503}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19723503}. SUBUNIT: Interacts with DLL1 and DLL4. {ECO:0000269|PubMed:19723503}. TISSUE SPECIFICITY: Expressed in the limb buds and dorsal root ganglia. Expressed in brain and kidney and at low levels in the heart. {ECO:0000269|PubMed:17003037}. +P35454 NEU1_MOUSE Oxytocin-neurophysin 1 (OT-NPI) [Cleaved into: Oxytocin (Ocytocin); Neurophysin 1] 125 12,851 Chain (1); Disulfide bond (8); Modified residue (1); Peptide (1); Signal peptide (1) FUNCTION: Neurophysin 1 specifically binds oxytocin.; FUNCTION: Oxytocin causes contraction of the smooth muscle of the uterus and of the mammary gland. Acts by binding to oxytocin receptor (OXTR) (By similarity). {ECO:0000250|UniProtKB:P01178}. SUBUNIT: Interacts with oxytocin receptor (Ki=1.5 nM) (By similarity). Interacts with vasopressin V1aR/AVPR1A (Ki=37 nM), V1bR/AVPR1B (Ki=222 nM), and V2R/AVPR2 receptors (Ki=823 nM) (By similarity). {ECO:0000250|UniProtKB:P01178}. +P41242 MATK_MOUSE Megakaryocyte-associated tyrosine-protein kinase (EC 2.7.10.2) (Protein kinase NTK) (Tyrosine-protein kinase CTK) 505 56,056 Active site (1); Alternative sequence (2); Binding site (1); Chain (1); Domain (3); Nucleotide binding (1); Sequence conflict (2) FUNCTION: Could play a significant role in the signal transduction of hematopoietic cells. May regulate tyrosine kinase activity of SRC-family members in brain by specifically phosphorylating their C-terminal regulatory tyrosine residue which acts as a negative regulatory site. It may play an inhibitory role in the control of T-cell proliferation. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7970703}. Membrane {ECO:0000250}. Note=In platelets, 90% of MATK localizes to the membrane fraction, and translocates to the cytoskeleton upon thrombin stimulation. {ECO:0000250}. SUBUNIT: Interacts with KIT. {ECO:0000250}. TISSUE SPECIFICITY: Most abundant in brain, and to a lesser extent in the spleen, the thymus and the liver. Also found in the T-cell lineage. +P14873 MAP1B_MOUSE Microtubule-associated protein 1B (MAP-1B) (MAP1(X)) (MAP1.2) [Cleaved into: MAP1B heavy chain; MAP1 light chain LC1] 2464 270,255 Chain (3); Compositional bias (1); Initiator methionine (1); Modified residue (100); Region (1); Repeat (10); Sequence conflict (8) FUNCTION: Phosphorylated MAP1B may play a role in the cytoskeletal changes that accompany neurite extension. Possibly MAP1B binds to at least two tubulin subunits in the polymer, and this bridging of subunits might be involved in nucleating microtubule polymerization and in stabilizing microtubules. Acts as a positive cofactor in DAPK1-mediated autophagic vesicle formation and membrane blebbing (By similarity). Facilitates tyrosination of alpha-tubulin in neuronal microtubules. Required for synaptic maturation. {ECO:0000250, ECO:0000269|PubMed:18075266, ECO:0000269|PubMed:21984824}. PTM: LC1 is coexpressed with MAP1B. It is a polypeptide generated from MAP1B by proteolytic processing. It is free to associate with both MAP1A and MAP1B. It interacts with the N-terminal region of MAP1B.; PTM: S-nitrosylation at Cys-2460 enhances interaction with microtubules, and may act as an effector modification for neuronal nitric oxide synthase control of growth-cone size, growth-cone collapse and axon retraction. {ECO:0000269|PubMed:17704770}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305|PubMed:21984824}. Cytoplasm {ECO:0000250}. Cell junction, synapse {ECO:0000269|PubMed:21984824}. Cell projection, dendritic spine {ECO:0000269|PubMed:21984824}. Note=Colocalizes with DAPK1 in the microtubules and cortical actin fibers. {ECO:0000250}. SUBUNIT: 3 different light chains, LC1, LC2 and LC3, can associate with MAP1A and MAP1B proteins. LC1 interacts with the amino-terminal region of MAP1B. Interacts with ANP32A and TIAM2 (PubMed:12807913, PubMed:17320046). Interacts with the tubulin tyrosine TTL (PubMed:18075266). Interacts (via C-terminus) with GAN (via Kelch domains) (PubMed:12147674). Interacts (via N-terminus) with DAPK1 (By similarity). Interacts with TMEM185A (By similarity). Interacts with MAP1LC3B (By similarity). Interacts with KIRREL3 (By similarity). {ECO:0000250|UniProtKB:P46821, ECO:0000269|PubMed:12147674, ECO:0000269|PubMed:12807913, ECO:0000269|PubMed:17320046, ECO:0000269|PubMed:18075266}. DOMAIN: Has a highly basic region with many copies of the sequence KKEE and KKEI/V, repeated but not at fixed intervals, which is responsible for the binding of MAP1B to microtubules. {ECO:0000269|PubMed:2480963}. +Q8BGB5 LIMD2_MOUSE LIM domain-containing protein 2 128 14,237 Chain (1); Domain (1); Metal binding (8); Modified residue (1) FUNCTION: Acts as an activator of the protein-kinase ILK, thereby regulating cell motility. {ECO:0000250|UniProtKB:Q9BT23}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BT23}. Nucleus {ECO:0000250|UniProtKB:Q9BT23}. Note=Mainly found in cytoplasm, concentrated in membrane ruffles and in streaks reminiscent of focal adhesion plaques. Also found in nucleus. {ECO:0000250|UniProtKB:Q9BT23}. SUBUNIT: Interacts with ILK. {ECO:0000250|UniProtKB:Q9BT23}. +Q99JW4 LIMS1_MOUSE LIM and senescent cell antigen-like-containing domain protein 1 (Particularly interesting new Cys-His protein 1) (PINCH-1) 325 37,240 Chain (1); Domain (5); Erroneous initiation (8); Initiator methionine (1); Modified residue (1); Sequence conflict (4) FUNCTION: Adapter protein in a cytoplasmic complex linking beta-integrins to the actin cytoskeleton, bridges the complex to cell surface receptor tyrosine kinases and growth factor receptors. Involved in the regulation of cell survival, cell proliferation and cell differentiation. SUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. SUBUNIT: Interacts with integrin-linked protein kinase 1 (ILK) via the first LIM domain, and in competition with LIMS2. Part of the heterotrimeric IPP complex composed of integrin-linked kinase (ILK), LIMS1 or LIMS2, and PARVA. Interacts with SH3/SH2 adapter NCK2, thereby linking the complex to cell surface receptors (By similarity). Interacts (via LIM zinc-binding 5) with TGFB1I1. {ECO:0000250, ECO:0000269|PubMed:16737959}. +O35711 LIPB2_MOUSE Liprin-beta-2 (Coiled-coil-like protein 1) (Protein tyrosine phosphatase receptor type f polypeptide-interacting protein-binding protein 2) (PTPRF-interacting protein-binding protein 2) 882 98,753 Alternative sequence (4); Chain (1); Coiled coil (1); Domain (3); Modified residue (5); Sequence conflict (3) FUNCTION: May regulate the disassembly of focal adhesions. Did not bind receptor-like tyrosine phosphatases type 2A (By similarity). {ECO:0000250|UniProtKB:Q8ND30}. SUBUNIT: Forms homodimers and heterodimers. {ECO:0000250|UniProtKB:Q8ND30}. DOMAIN: The N-terminal coiled coil regions mediate homodimerization preferentially and heterodimerization type beta/beta. The C-terminal, non-coiled coil regions mediate heterodimerization type beta/alpha (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed widely. Strong expression in liver, kidney, intestine, heart, lung and testis. Low expression in brain and thymus. {ECO:0000269|PubMed:9199242}. +P54310 LIPS_MOUSE Hormone-sensitive lipase (HSL) (EC 3.1.1.79) 759 83,348 Active site (3); Alternative sequence (1); Chain (1); Modified residue (8); Motif (1); Sequence conflict (4) Glycerolipid metabolism; triacylglycerol degradation. FUNCTION: In adipose tissue and heart, it primarily hydrolyzes stored triglycerides to free fatty acids, while in steroidogenic tissues, it principally converts cholesteryl esters to free cholesterol for steroid hormone production. {ECO:0000269|PubMed:23291629}. PTM: Phosphorylation by AMPK may block translocation to lipid droplets. {ECO:0000269|PubMed:15878856, ECO:0000269|PubMed:19921680}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Membrane, caveola {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Note=Found in the high-density caveolae. Translocates to the cytoplasm from the caveolae upon insulin stimulation. {ECO:0000250}. SUBUNIT: Interacts with CAVIN1 in the adipocyte cytoplasm (By similarity). Interacts with PLIN5 (PubMed:19717842). {ECO:0000250|UniProtKB:Q05469, ECO:0000269|PubMed:19717842}. +Q8CIV3 LIPH_MOUSE Lipase member H (EC 3.1.1.-) 451 50,675 Active site (3); Alternative sequence (2); Chain (1); Disulfide bond (4); Glycosylation (1); Sequence conflict (4); Signal peptide (1) FUNCTION: Hydrolyzes specifically phosphatidic acid (PA) to produce lysophosphatidic acid (LPA). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Expressed in placenta and colon. Weakly expressed in small intestine. {ECO:0000269|PubMed:12213196}. +Q8VCM4 LIPT_MOUSE Lipoyltransferase 1, mitochondrial (EC 2.3.1.-) (Lipoate biosynthesis protein) (Lipoate-protein ligase) (Lipoyl ligase) 373 42,146 Binding site (4); Chain (1); Domain (1); Transit peptide (1) Protein modification; protein lipoylation via exogenous pathway; protein N(6)-(lipoyl)lysine from lipoate: step 2/2. FUNCTION: Catalyzes the transfer of the lipoyl group from lipoyl-AMP to the specific lysine residue of lipoyl domains of lipoate-dependent enzymes. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. +Q6P8U6 LIPP_MOUSE Pancreatic triacylglycerol lipase (PL) (PTL) (Pancreatic lipase) (EC 3.1.1.3) 465 51,428 Active site (3); Chain (1); Disulfide bond (6); Domain (1); Metal binding (4); Signal peptide (1) FUNCTION: Plays an important role in fat metabolism. It preferentially splits the esters of long-chain fatty acids at positions 1 and 3, producing mainly 2-monoacylglycerol and free fatty acids, and shows considerably higher activity against insoluble emulsified substrates than against soluble ones (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. TISSUE SPECIFICITY: Pancreas. {ECO:0000269|PubMed:10769148}. +Q9JLJ0 LITAF_MOUSE Lipopolysaccharide-induced tumor necrosis factor-alpha factor homolog (LPS-induced TNF-alpha factor homolog) (Estrogen-enhanced transcript protein) (mEET) (LITAF-like protein) (NEDD4 WW domain-binding protein 3) 161 16,946 Chain (1); Domain (1); Erroneous initiation (1); Metal binding (4); Motif (1); Mutagenesis (2); Region (1) FUNCTION: Plays a role in endosomal protein trafficking and in targeting proteins for lysosomal degradation. Plays a role in targeting endocytosed EGFR and ERGG3 for lysosomal degradation, and thereby helps downregulate downstream signaling cascades (PubMed:23166352). Helps recruit the ESCRT complex components TSG101, HGS and STAM to cytoplasmic membranes. Probably plays a role in regulating protein degradation via its interaction with NEDD4 (By similarity). May also contribute to the regulation of gene expression in the nucleus. Binds DNA (in vitro) and may play a synergistic role with STAT6 in the nucleus in regulating the expression of various cytokines (PubMed:15793005, PubMed:21980379). May regulate the expression of numerous cytokines, such as TNF, CCL2, CCL5, CXCL1, IL1A and IL10 (PubMed:12355436, PubMed:15025820, PubMed:16954198, PubMed:21980379, PubMed:22160695). {ECO:0000250|UniProtKB:Q99732, ECO:0000269|PubMed:12355436, ECO:0000269|PubMed:15025820, ECO:0000269|PubMed:15793005, ECO:0000269|PubMed:16954198, ECO:0000269|PubMed:21980379, ECO:0000269|PubMed:23166352}. PTM: Phosphorylated on tyrosine residues in response to EGF. {ECO:0000250|UniProtKB:Q99732}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q99732}. Nucleus {ECO:0000250|UniProtKB:Q99732}. Lysosome membrane {ECO:0000250|UniProtKB:Q99732}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q99732}; Cytoplasmic side {ECO:0000250|UniProtKB:Q99732}. Early endosome membrane {ECO:0000250|UniProtKB:Q99732}. Late endosome membrane {ECO:0000250|UniProtKB:Q99732}. Endosome membrane {ECO:0000250|UniProtKB:Q99732}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q99732}; Cytoplasmic side {ECO:0000250|UniProtKB:Q99732}. Cell membrane {ECO:0000250|UniProtKB:Q99732}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q99732}; Cytoplasmic side {ECO:0000250|UniProtKB:Q99732}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q99732}. Note=Associated with membranes of lysosomes, early and late endosomes. Can translocate from the cytoplasm into the nucleus (By similarity). Detected at Schmidt-Lanterman incisures and in nodal regions of myelinating Schwann cells (PubMed:22729949). {ECO:0000250|UniProtKB:Q99732, ECO:0000269|PubMed:22729949}. SUBUNIT: Monomer. Interacts with NEDD4 (PubMed:11042109). Interacts (via PSAP motif) with TSG101, a component of the ESCRT-I complex (endosomal sorting complex required for transport I). Interacts with WWOX. Interacts with STAM, a component of the ESCRT-0 complex; the interaction is direct. Identified in a complex with STAM and HGS; within this complex, interacts directly with STAM, but not with HGS. Interacts with STAT6 (PubMed:15793005). {ECO:0000250|UniProtKB:Q99732, ECO:0000269|PubMed:11042109, ECO:0000269|PubMed:15793005}. DOMAIN: The PPxY motif mediates interaction with WWOX and NEDD4. {ECO:0000250|UniProtKB:Q99732}.; DOMAIN: The LITAF domain is stabilized by a bound zinc ion. The LITAF domain contains an amphiphatic helix that mediates interaction with lipid membranes. It interacts specifically with phosphatidylethanolamine lipid headgroups, but not with phosphoglycerol, phosphocholine, phosphoserine or inositolhexakisphosphate. {ECO:0000250|UniProtKB:Q99732}. TISSUE SPECIFICITY: Detected in brain, heart, lung, liver, spleen and bone marrow (PubMed:22160695). Detected in myelinating Schwann cells in sciatic nerve and in bone marrow-derived macrophages (at protein level) (PubMed:22729949). Widely expressed. Highly expressed in liver. {ECO:0000269|PubMed:12355436, ECO:0000269|PubMed:15025820, ECO:0000269|PubMed:22160695, ECO:0000269|PubMed:22729949}. +Q587J6 LITD1_MOUSE LINE-1 type transposase domain-containing protein 1 (ES cell-associated protein 11) 782 88,189 Chain (1); Compositional bias (3); Erroneous initiation (1); Modified residue (8) +Q9D4C1 LMTD1_MOUSE Lamin tail domain-containing protein 1 (Intermediate filament tail domain-containing protein 1) (Lamin-A-related sequence 1 protein) 413 45,937 Chain (1); Domain (1); Sequence conflict (2) +Q8K0B2 LMBD1_MOUSE Probable lysosomal cobalamin transporter (LMBR1 domain-containing protein 1) (Protein N90b) 537 61,062 Alternative sequence (3); Chain (1); Glycosylation (7); Modified residue (3); Sequence conflict (6); Topological domain (10); Transmembrane (9) TRANSMEM 8 28 Helical; Name=1. {ECO:0000255}.; TRANSMEM 48 68 Helical; Name=2. {ECO:0000255}.; TRANSMEM 98 118 Helical; Name=3. {ECO:0000255}.; TRANSMEM 142 162 Helical; Name=4. {ECO:0000255}.; TRANSMEM 186 206 Helical; Name=5. {ECO:0000255}.; TRANSMEM 303 323 Helical; Name=6. {ECO:0000255}.; TRANSMEM 362 382 Helical; Name=7. {ECO:0000255}.; TRANSMEM 406 426 Helical; Name=8. {ECO:0000255}.; TRANSMEM 484 504 Helical; Name=9. {ECO:0000255}. TOPO_DOM 1 7 Extracellular. {ECO:0000255}.; TOPO_DOM 29 47 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 69 97 Extracellular. {ECO:0000255}.; TOPO_DOM 119 141 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 163 185 Extracellular. {ECO:0000255}.; TOPO_DOM 207 302 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 324 361 Extracellular. {ECO:0000255}.; TOPO_DOM 383 405 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 427 483 Extracellular. {ECO:0000255}.; TOPO_DOM 505 537 Cytoplasmic. {ECO:0000255}. FUNCTION: Probable lysosomal cobalamin transporter. Required to export cobalamin from lysosomes allowing its conversion to cofactors (By similarity). {ECO:0000250}. PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q8C561 LMBD2_MOUSE LMBR1 domain-containing protein 2 694 81,101 Alternative sequence (2); Chain (1); Coiled coil (2); Glycosylation (1); Modified residue (1); Sequence conflict (1); Topological domain (10); Transmembrane (9) TRANSMEM 4 21 Helical. {ECO:0000255}.; TRANSMEM 33 53 Helical. {ECO:0000255}.; TRANSMEM 106 126 Helical. {ECO:0000255}.; TRANSMEM 151 171 Helical. {ECO:0000255}.; TRANSMEM 187 207 Helical. {ECO:0000255}.; TRANSMEM 388 408 Helical. {ECO:0000255}.; TRANSMEM 433 453 Helical. {ECO:0000255}.; TRANSMEM 474 494 Helical. {ECO:0000255}.; TRANSMEM 522 542 Helical. {ECO:0000255}. TOPO_DOM 1 3 Extracellular. {ECO:0000255}.; TOPO_DOM 22 32 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 54 105 Extracellular. {ECO:0000255}.; TOPO_DOM 127 150 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 172 186 Extracellular. {ECO:0000255}.; TOPO_DOM 208 387 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 409 432 Extracellular. {ECO:0000255}.; TOPO_DOM 454 473 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 495 521 Extracellular. {ECO:0000255}.; TOPO_DOM 543 694 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8BMN4 LMLN_MOUSE Leishmanolysin-like peptidase (EC 3.4.24.-) 681 76,575 Active site (1); Chain (1); Metal binding (3) FUNCTION: Metalloprotease. {ECO:0000250|UniProtKB:Q9VH19}. SUBCELLULAR LOCATION: Cytoplasm. Lipid droplet {ECO:0000250}. Note=Found in ring-like structures resembling invadopodia. In migrating cells it relocalizes from internal structures to the leading edge of cells (By similarity). {ECO:0000250}. +Q9D0F3 LMAN1_MOUSE Protein ERGIC-53 (ER-Golgi intermediate compartment 53 kDa protein) (Lectin mannose-binding 1) (p58) 517 57,789 Binding site (4); Chain (1); Disulfide bond (3); Domain (1); Metal binding (4); Modified residue (1); Motif (1); Region (2); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 485 505 Helical. {ECO:0000255}. TOPO_DOM 31 484 Lumenal. {ECO:0000255}.; TOPO_DOM 506 517 Cytoplasmic. {ECO:0000255}. FUNCTION: Mannose-specific lectin. May recognize sugar residues of glycoproteins, glycolipids, or glycosylphosphatidyl inositol anchors and may be involved in the sorting or recycling of proteins, lipids, or both. The LMAN1-MCFD2 complex forms a specific cargo receptor for the ER-to-Golgi transport of selected proteins (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. SUBUNIT: Exists both as a covalent disulfide-linked homohexamer, and a complex of three disulfide-linked dimers non-covalently kept together. Interacts with MCFD2. May interact with TMEM115. Interacts with RAB3GAP1 and RAB3GAP2. Interacts with UBXN6. {ECO:0000250|UniProtKB:P49257}. DOMAIN: The FF ER export motif at the C-terminus is not sufficient to support endoplasmic reticulum exit, and needs assistance of Gln-508 for proper recognition of COPII coat components. {ECO:0000250}. +Q60605 MYL6_MOUSE Myosin light polypeptide 6 (17 kDa myosin light chain) (LC17) (Myosin light chain 3) (MLC-3) (Myosin light chain alkali 3) (Myosin light chain A3) (Smooth muscle and nonmuscle myosin light chain alkali 6) 151 16,930 Alternative sequence (1); Chain (1); Domain (3); Initiator methionine (1); Modified residue (4); Sequence conflict (2) FUNCTION: Regulatory light chain of myosin. Does not bind calcium. SUBUNIT: Myosin is a hexamer of 2 heavy chains and 4 light chains. Interacts with SPATA6 (PubMed:25605924). {ECO:0000269|PubMed:25605924}. +Q9CQ19 MYL9_MOUSE Myosin regulatory light polypeptide 9 (Myosin regulatory light chain 2, smooth muscle isoform) (Myosin regulatory light chain 9) 172 19,854 Calcium binding (1); Chain (1); Domain (3); Initiator methionine (1); Modified residue (3); Sequence conflict (1) FUNCTION: Myosin regulatory subunit that plays an important role in regulation of both smooth muscle and nonmuscle cell contractile activity via its phosphorylation. Implicated in cytokinesis, receptor capping, and cell locomotion. {ECO:0000250|UniProtKB:P24844}. PTM: Phosphorylation increases the actin-activated myosin ATPase activity and thereby regulates the contractile activity. It is required to generate the driving force in the migration of the cells but not necessary for localization of myosin-2 at the leading edge. {ECO:0000250|UniProtKB:P24844}. SUBUNIT: Myosin is a hexamer of 2 heavy chains and 4 light chains: interacts with myosin heavy chain MYO19. {ECO:0000269|PubMed:24825904}. +Q9DC07 LNEBL_MOUSE LIM zinc-binding domain-containing Nebulette (Actin-binding Z-disk protein) 270 31,113 Chain (1); Domain (2); Modified residue (4); Repeat (3) FUNCTION: Binds to actin and plays an important role in the assembly of the Z-disk. Isoform 2 might play a role in the assembly of focal adhesion (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Isoform 2: Cytoplasm {ECO:0000250}. +Q9Z175 LOXL3_MOUSE Lysyl oxidase homolog 3 (EC 1.4.3.-) (EC 1.4.3.13) (Lysyl oxidase-like protein 3) (Lysyl oxidase-related protein 2) 754 83,740 Chain (1); Cross-link (1); Disulfide bond (17); Domain (4); Glycosylation (5); Metal binding (3); Modified residue (1); Region (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Protein-lysine 6-oxidase that mediates the oxidation of peptidyl lysine residues to allysine in target proteins (PubMed:26954549). Catalyzes the post-translational oxidative deamination of peptidyl lysine residues in precursors of elastin and different types of collagens, a prerequisite in the formation of cross-links between collagens and elastin (PubMed:26307084). Required for somite boundary formation by catalyzing oxidation of fibronectin (FN1), enhancing integrin signaling in myofibers and their adhesion to the myotendinous junction (MTJ) (PubMed:26954549). Acts as a regulator of inflammatory response by inhibiting differentiation of naive CD4(+) T-cells into T-helper Th17 or regulatory T-cells (Treg): acts by interacting with STAT3 in the nucleus and catalyzing both deacetylation and oxidation of lysine residues on STAT3, leading to disrupt STAT3 dimerization and inhibit STAT3 transcription activity (PubMed:28065600). Oxidation of lysine residues to allysine on STAT3 preferentially takes place on lysine residues that are acetylated (By similarity). Also able to catalyze deacetylation of lysine residues on STAT3 (By similarity). {ECO:0000250|UniProtKB:P58215, ECO:0000269|PubMed:26307084, ECO:0000269|PubMed:26954549, ECO:0000269|PubMed:28065600}. PTM: The lysine tyrosylquinone cross-link (LTQ) is generated by condensation of the epsilon-amino group of a lysine with a topaquinone produced by oxidation of tyrosine. {ECO:0000250|UniProtKB:P33072}. SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000269|PubMed:26954549}. Cytoplasm {ECO:0000250|UniProtKB:P58215}. Nucleus {ECO:0000250|UniProtKB:P58215}. Note=It is unclear how LOXL3 is both intracellular (cytoplasmic and nuclear) and extracellular: it contains a clear signal sequence and is predicted to localize in the extracellular medium. However, the intracellular location is clearly reported and at least another protein of the family (LOXL2) also has intracellular and extracellular localization despite the presence of a signal sequence. {ECO:0000250|UniProtKB:P58215}. TISSUE SPECIFICITY: Expressed in palate: predominantly present in the palate mesenchyme and tongue (at protein level) (PubMed:26307084). In spine, expressed in the original intervertebral disk, cartilage primordia, anterior and posterior longitudinal ligaments, meninges of spinal cord, lung and heart (PubMed:26307084). In eyes, strongly expressed in the skin of the eyelid and weakly expressed in the cornea and sclera (PubMed:26307084). In lung, predominantly expressed in the pulmonary mesenchyme (PubMed:27645581). In developing muscle, expressed at myofiber ends (at protein level) (PubMed:26954549). {ECO:0000269|PubMed:26307084, ECO:0000269|PubMed:26954549, ECO:0000269|PubMed:27645581}. +Q7TSF4 LR75A_MOUSE Leucine-rich repeat-containing protein 75A (Leucine-rich repeat-containing protein FAM211A) 339 37,574 Alternative sequence (1); Chain (1); Modified residue (2); Repeat (2) +Q6P1C6 LRIG3_MOUSE Leucine-rich repeats and immunoglobulin-like domains protein 3 (LIG-3) 1117 122,688 Beta strand (9); Chain (1); Disulfide bond (3); Domain (5); Erroneous initiation (1); Frameshift (1); Glycosylation (7); Helix (2); Repeat (15); Sequence conflict (3); Signal peptide (1); Transmembrane (1); Turn (1) TRANSMEM 810 830 Helical. {ECO:0000255}. FUNCTION: Plays a role in craniofacial and inner ear morphogenesis during embryonic development. Acts within the otic vesicle epithelium to control formation of the lateral semicircular canal in the inner ear, possibly by restricting the expression of NTN1. {ECO:0000269|PubMed:19004851, ECO:0000269|PubMed:20126551}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20126551}; Single-pass type I membrane protein {ECO:0000269|PubMed:20126551}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:20126551}; Single-pass type I membrane protein {ECO:0000269|PubMed:20126551}. Note=Detected in cytoplasmic vesicles when coexpressed with ERBB4. SUBUNIT: Interacts with EGFR, ERBB2 and ERBB4 (in vitro). {ECO:0000269|PubMed:20126551}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15203213}. +Q99N69 LPXN_MOUSE Leupaxin 386 43,478 Chain (1); Domain (4); Modified residue (7); Motif (3) FUNCTION: Transcriptional coactivator for androgen receptor (AR) and serum response factor (SRF). Contributes to the regulation of cell adhesion, spreading and cell migration and acts as a negative regulator in integrin-mediated cell adhesion events. Suppresses the integrin-induced tyrosine phosphorylation of paxillin (PXN). May play a critical role as an adapter protein in the formation of the adhesion zone in osteoclasts. Negatively regulates B-cell antigen receptor (BCR) signaling. {ECO:0000269|PubMed:12674328, ECO:0000269|PubMed:17640867, ECO:0000269|PubMed:18497331, ECO:0000269|PubMed:19917054}. PTM: Phosphorylated on tyrosine residues. Phosphorylation on Tyr-72 is important for its inhibitory function. Bombesin stimulates phosphorylation on Tyr-22, Tyr-62 and Tyr-72 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell junction, focal adhesion. Nucleus. Cytoplasm, perinuclear region. Cell projection, podosome. Cell membrane. Note=Shuttles between the cytoplasm and nucleus. Recruited to the cell membrane following B-cell antigen receptor (BCR) cross-linking in B-cells. Enhanced focal adhesion kinase activity (PTK2/FAK) attenuates its nuclear accumulation and limits its ability to enhance serum response factor (SRF)-dependent gene transcription. Targeting to focal adhesions is essential for its tyrosine phosphorylation in response to bombesin (By similarity). {ECO:0000250}. SUBUNIT: Interacts with unphosphorylated ITGA4. Interacts with AR and SRF (By similarity). Interacts with PTK2B/PYK2, PTPN22 and PTPN12. Interacts (via LD motif 3) with LYN and the interaction is induced upon B-cell antigen receptor (BCR) activation. Interacts (via LD motif 3) with PTK2/FAK. {ECO:0000250, ECO:0000269|PubMed:12674328, ECO:0000269|PubMed:15786712, ECO:0000269|PubMed:17640867, ECO:0000269|PubMed:19917054}. DOMAIN: The LIM domain 3 is critical for focal adhesion targeting and the suppression of paxillin (PXN) tyrosine phosphorylation. The LIM domain 3 alone or both LIM domains 3 and 4 can mediate interaction with AR. {ECO:0000269|PubMed:19917054}. TISSUE SPECIFICITY: Expressed in osteoclasts (at protein level). Highly expressed in vascular smooth muscle. {ECO:0000269|PubMed:12674328, ECO:0000269|PubMed:18497331}. +Q9D820 PRXD1_MOUSE Prolyl-tRNA synthetase associated domain-containing protein 1 (PrdX deacylase domain-containing protein 1) 169 18,862 Alternative sequence (1); Chain (1); Compositional bias (1); Erroneous gene model prediction (1) +P0C028 NUD11_MOUSE Diphosphoinositol polyphosphate phosphohydrolase 3-beta (DIPP-3-beta) (DIPP3-beta) (EC 3.6.1.52) (Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 3-beta) (Diadenosine hexaphosphate hydrolase (AMP-forming)) (EC 3.6.1.60) (Nucleoside diphosphate-linked moiety X motif 11) (Nudix motif 11) 164 18,593 Active site (1); Binding site (3); Chain (1); Domain (1); Metal binding (4); Motif (1); Natural variant (1); Region (3) FUNCTION: Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate), suggesting that it may play a role in signal transduction. Also able to catalyze the hydrolysis of dinucleoside oligophosphates, with Ap6A and Ap5A being the preferred substrates. The major reaction products are ADP and p4a from Ap6A and ADP and ATP from Ap5A. Also able to hydrolyze 5-phosphoribose 1-diphosphate; however, the relevance of such activity in vivo remains unclear. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96G61}. TISSUE SPECIFICITY: Predominantly expressed in brain and is weakly or not expressed in other tissues. {ECO:0000269|PubMed:12689335}. +Q9D142 NUD14_MOUSE Uridine diphosphate glucose pyrophosphatase (UDPG pyrophosphatase) (UGPPase) (EC 3.6.1.45) (Nucleoside diphosphate-linked moiety X motif 14) (Nudix motif 14) 222 24,444 Chain (1); Domain (1); Motif (1); Sequence conflict (1) FUNCTION: Hydrolyzes UDP-glucose to glucose 1-phosphate and UMP and ADP-ribose to ribose 5-phosphate and AMP. The physiological substrate is probably UDP-glucose. Poor activity on other substrates such as ADP-glucose, CDP-glucose, GDP-glucose and GDP-mannose (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +Q80ZC9 PS1C2_MOUSE Psoriasis susceptibility 1 candidate gene 2 protein homolog (Protein SPR1) 134 14,414 Chain (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q5F2E7 NUFP2_MOUSE Nuclear fragile X mental retardation-interacting protein 2 (82 kDa FMRP-interacting protein) (82-FIP) (FMRP-interacting protein 2) 692 75,657 Alternative sequence (1); Chain (1); Compositional bias (2); Cross-link (10); Erroneous initiation (1); Modified residue (21); Sequence conflict (2) FUNCTION: Binds RNA. {ECO:0000250|UniProtKB:Q7Z417}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12837692}. Cytoplasm {ECO:0000269|PubMed:12837692}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q7Z417}. Note=Localized in both nucleus and cytoplasm in most neurons. In the cortex, distributed in a diffuse way in the nucleus and in the cytoplasm. Localized in the cytoplasm in neurons of the dentate gyrus in the olfactive bulb, in the ependymal epithelium and in the granular layer of the cerebellum. In Purkinje cells, distributed in both cell compartments and in nuclear dots adjacent to the nucleolus (PubMed:12837692). {ECO:0000250|UniProtKB:Q7Z417, ECO:0000269|PubMed:12837692}. SUBUNIT: Interacts with FMR1 (via N-terminus) (PubMed:12837692). Interacts with DDX6 (By similarity). {ECO:0000250|UniProtKB:Q7Z417, ECO:0000269|PubMed:12837692}. +Q6P3D0 NUD16_MOUSE U8 snoRNA-decapping enzyme (EC 3.6.1.62) (IDP phosphatase) (IDPase) (EC 3.6.1.64) (Inosine diphosphate phosphatase) (Nucleoside diphosphate-linked moiety X motif 16) (Nudix motif 16) (m7GpppN-mRNA hydrolase) 195 21,825 Binding site (4); Chain (1); Domain (1); Frameshift (1); Metal binding (7); Motif (1); Sequence conflict (1) FUNCTION: RNA-binding and decapping enzyme that catalyzes the cleavage of the cap structure of snoRNAs and mRNAs in a metal-dependent manner. Part of the U8 snoRNP complex that is required for the accumulation of mature 5.8S and 28S rRNA. Has diphosphatase activity and removes m7G and/or m227G caps from U8 snoRNA and leaves a 5'monophosphate on the RNA. Catalyzes also the cleavage of the cap structure on mRNAs. Does not hydrolyze cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG). Also hydrolysis m7G- and m227G U3-capped RNAs but with less efficiencies. Has broad substrate specificity with manganese or cobalt as cofactor and can act on various RNA species. Binds to the U8 snoRNA; metal is not required for RNA-binding. May play a role in the regulation of snoRNAs and mRNAs degradation (By similarity). Acts also as a phosphatase; hydrolyzes the non-canonical purine nucleotides inosine diphosphate (IDP) and deoxyinosine diphosphate (dITP) as well as guanosine diphosphate (GDP), deoxyguanosine diphosphate (dGDP), xanthine diphosphate (XDP), inosine triphosphate (ITP) and deoxyinosine triphosphate (ITP) to their respective monophosphate derivatives and does not distinguish between the deoxy- and ribose forms. The order of activity with different substrates is IDP > dIDP >> GDP = dGDP > XDP = ITP = dITP. Binds strongly to GTP, ITP and XTP. Participates in the hydrolysis of dIDP/IDP and probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions. {ECO:0000250|UniProtKB:Q96DE0, ECO:0000269|PubMed:20081199, ECO:0000269|PubMed:20385596, ECO:0000269|PubMed:21070968}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96DE0}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q6TEC1}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q6TEC1}. Cytoplasm {ECO:0000250|UniProtKB:Q96DE0}. Note=Localized predominantly in the cytoplasm. Localized in nucleolus, and in a minor proportion in distinct foci in the nucleoplasm. {ECO:0000250|UniProtKB:Q6TEC1, ECO:0000250|UniProtKB:Q96DE0}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q96DE0}. TISSUE SPECIFICITY: Expressed in brain, testis, spleen, lung, heart, liver, kidney and muscle (at protein level). {ECO:0000269|PubMed:21070968}. +Q8K561 OTOAN_MOUSE Otoancorin 1137 126,430 Chain (1); Glycosylation (11); Lipidation (1); Propeptide (1); Signal peptide (1) FUNCTION: May act as an adhesion molecule. {ECO:0000269|PubMed:11972037}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000305|PubMed:11972037}; Lipid-anchor, GPI-anchor {ECO:0000305|PubMed:11972037}; Extracellular side {ECO:0000305|PubMed:11972037}. Secreted, extracellular space, extracellular matrix {ECO:0000305|PubMed:11972037}. Note=At the interface between the apical surface of the epithelia and the overlying acellular gel of the tectorial and otoconial membranes. TISSUE SPECIFICITY: Expressed in the inner ear and vestibule. {ECO:0000269|PubMed:11972037}. +Q80UF9 OTOP3_MOUSE Proton channel OTOP3 (Otopetrin-3) 577 64,743 Alternative sequence (1); Chain (1); Sequence conflict (2); Transmembrane (12) TRANSMEM 71 91 Helical. {ECO:0000255}.; TRANSMEM 102 122 Helical. {ECO:0000255}.; TRANSMEM 140 160 Helical. {ECO:0000255}.; TRANSMEM 175 195 Helical. {ECO:0000255}.; TRANSMEM 208 228 Helical. {ECO:0000255}.; TRANSMEM 272 292 Helical. {ECO:0000255}.; TRANSMEM 319 339 Helical. {ECO:0000255}.; TRANSMEM 353 373 Helical. {ECO:0000255}.; TRANSMEM 398 418 Helical. {ECO:0000255}.; TRANSMEM 430 450 Helical. {ECO:0000255}.; TRANSMEM 511 531 Helical. {ECO:0000255}.; TRANSMEM 551 571 Helical. {ECO:0000255}. FUNCTION: Proton-selective channel that specifically transports protons into cells. Proton-selective channel activity is probably required in cell types that use changes in intracellular pH for cell signaling or to regulate biochemical or developmental processes. {ECO:0000269|PubMed:29371428}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q80VM9}; Multi-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Expressed in epidermis, small intestine, stomach and retina. {ECO:0000269|PubMed:29371428}. +B0V2N1 PTPRS_MOUSE Receptor-type tyrosine-protein phosphatase S (R-PTP-S) (EC 3.1.3.48) (PTPNU-3) (Receptor-type tyrosine-protein phosphatase sigma) (R-PTP-sigma) 1907 211,904 Active site (2); Alternative sequence (6); Beta strand (26); Binding site (2); Chain (1); Disulfide bond (3); Domain (13); Glycosylation (4); Helix (18); Mutagenesis (1); Region (2); Sequence conflict (9); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1); Turn (7) TRANSMEM 1258 1278 Helical. {ECO:0000255}. TOPO_DOM 30 1257 Extracellular. {ECO:0000255}.; TOPO_DOM 1279 1907 Cytoplasmic. {ECO:0000255}. FUNCTION: Cell surface receptor that binds to glycosaminoglycans, including chondroitin sulfate proteoglycans and heparan sulfate proteoglycans (PubMed:19833921, PubMed:21454754, PubMed:22406547). Binding to chondroitin sulfate and heparan sulfate proteoglycans has opposite effects on PTPRS oligomerization and regulation of neurite outgrowth (PubMed:21454754). Contributes to the inhibition of neurite and axonal outgrowth by chondroitin sulfate proteoglycans, also after nerve transection (PubMed:15797710, PubMed:19833921, PubMed:19780196, PubMed:21454754, PubMed:22519304, PubMed:22406547). Plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2 (PubMed:21454754). Required for normal brain development, especially for normal development of the pituitary gland and the olfactory bulb (PubMed:10080191). Functions as tyrosine phosphatase (PubMed:7529177). Mediates dephosphorylation of NTRK1, NTRK2 and NTRK3 (By similarity). Plays a role in down-regulation of signaling cascades that lead to the activation of Akt and MAP kinases (PubMed:15797710). Down-regulates TLR9-mediated activation of NF-kappa-B, as well as production of TNF, interferon alpha and interferon beta (PubMed:26231120). {ECO:0000250|UniProtKB:F1NWE3, ECO:0000269|PubMed:10080191, ECO:0000269|PubMed:15797710, ECO:0000269|PubMed:19780196, ECO:0000269|PubMed:19833921, ECO:0000269|PubMed:21454754, ECO:0000269|PubMed:22406547, ECO:0000269|PubMed:26231120, ECO:0000269|PubMed:7529177}. PTM: A cleavage occurs, separating the extracellular domain from the transmembrane segment. This process called 'ectodomain shedding' is thought to be involved in receptor desensitization, signal transduction and/or membrane localization (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26231120}; Single-pass type I membrane protein {ECO:0000305}. Cell projection, axon {ECO:0000269|PubMed:21454754}. Perikaryon {ECO:0000269|PubMed:21454754}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q64605}. Cell junction, synapse, synaptosome {ECO:0000250|UniProtKB:Q64605}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250|UniProtKB:Q64605}. Note=Is rapidly internalized when dendritic cells are stimulated with the TLR9 ligand cytidine-phosphate-guanosine (CpG) (PubMed:26231120). Detected in a punctate pattern along neurites and axon growth cones (PubMed:21454754). {ECO:0000269|PubMed:21454754, ECO:0000269|PubMed:26231120}. SUBUNIT: Binding to large heparan sulfate proteoglycan structures promotes oligomerization (PubMed:21454754). Binding to chondroitin sulfate proteoglycan does not lead to oligomerization (PubMed:21454754). Interacts (via Ig-like domains) with NTRK3 (PubMed:25385546). Interacts (via Ig-like domains) with NTRK1, but does not form detectable complexes with NTRK2 (By similarity). Interacts with PPFIA1, PPFIA2 and PPFIA3 (By similarity). {ECO:0000250|UniProtKB:Q13332, ECO:0000250|UniProtKB:Q64605, ECO:0000269|PubMed:21454754, ECO:0000269|PubMed:25385546}. TISSUE SPECIFICITY: Detected in brain cortex, cerebellum and thoracic spinal cord (at protein level) (PubMed:19780196, PubMed:22519304). Detected in motor cortex and white matter of the spinal cord, but not in spinal cord gray matter (PubMed:19780196). Isoform 1 and isoform 6 are predominantly expressed in the brain (cerebrum and cerebellum) and to a lesser extent in the heart and skeletal muscle. Also found in neuronal-derived cell lines (PubMed:7529177). Detected in the ganglion cell layer of the retina and in glial cells along the optic nerve (PubMed:15797710). Detected in bone marrow and spleen plasmacytoid dendritic cells (PubMed:26231120). {ECO:0000269|PubMed:15797710, ECO:0000269|PubMed:19780196, ECO:0000269|PubMed:22519304, ECO:0000269|PubMed:26231120, ECO:0000269|PubMed:7529177}. +Q6IE21 OTU6A_MOUSE OTU domain-containing protein 6A (EC 3.4.19.12) (Hin-6 protease) 290 33,738 Active site (3); Chain (1); Domain (1); Region (3) FUNCTION: Deubiquitinating enzyme that hydrolyzes 'Lys-27'-, 'Lys-29'- and 'Lys-33'-linked polyubiquitin chains. Also able to hydrolyze 'Lys-11'-linked ubiquitin chains (By similarity). {ECO:0000250}. +Q8K2H2 OTU6B_MOUSE Deubiquitinase OTUD6B (OTU domain-containing protein 6B) (EC 3.4.19.12) 294 33,758 Active site (3); Chain (1); Domain (1); Modified residue (1); Region (3); Sequence conflict (5) FUNCTION: Deubiquitinating enzyme that may play a role in the ubiquitin-dependent regulation of protein synthesis, downstream of mTORC1 (By similarity). May associate with the protein synthesis initiation complex and modify its ubiquitination to repress translation (By similarity). May also repress DNA synthesis and modify different cellular targets thereby regulating cell growth and proliferation (By similarity). May also play a role in proteasome assembly and function (By similarity). {ECO:0000250|UniProtKB:Q8N6M0}. SUBUNIT: Interacts with the eukaryotic translation initiation factor 4F complex. {ECO:0000250|UniProtKB:Q8N6M0}. TISSUE SPECIFICITY: Ubiquitously expressed. Expression is observed in several organ systems including the cardiovascular, digestive, central and peripheral nervous and musculoskeletal systems. {ECO:0000269|PubMed:21267069, ECO:0000269|PubMed:28343629}. +Q8R554 OTU7A_MOUSE OTU domain-containing protein 7A (EC 3.4.19.12) (Zinc finger protein Cezanne 2) 926 100,797 Active site (3); Chain (1); Domain (1); Modified residue (2); Motif (1); Region (2); Zinc finger (1) FUNCTION: Has deubiquitinating activity towards 'Lys-11'-linked polyubiquitin chains. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. +B2RUR8 OTU7B_MOUSE OTU domain-containing protein 7B (EC 3.4.19.12) (Cellular zinc finger anti-NF-kappa-B protein) (Zinc finger A20 domain-containing protein 1) (Zinc finger protein Cezanne) 840 91,983 Active site (3); Chain (1); Domain (1); Modified residue (5); Motif (1); Mutagenesis (2); Region (3); Sequence caution (1); Site (1); Zinc finger (1) FUNCTION: Negative regulator of the non-canonical NF-kappa-B pathway that acts by mediating deubiquitination of TRAF3, an inhibitor of the NF-kappa-B pathway, thereby acting as a negative regulator of B-cell responses. In response to non-canonical NF-kappa-B stimuli, deubiquitinates 'Lys-48'-linked polyubiquitin chains of TRAF3, preventing TRAF3 proteolysis and over-activation of non-canonical NF-kappa-B (PubMed:23334419). Negatively regulates mucosal immunity against infections (PubMed:23334419). Deubiquitinates ZAP70, and thereby regulates T cell receptor (TCR) signaling that leads to the activation of NF-kappa-B (PubMed:26903241). Plays a role in T cell homeostasis and is required for normal T cell responses, including production of IFNG and IL2 (PubMed:26903241). Mediates deubiquitination of EGFR (By similarity). Has deubiquitinating activity toward 'Lys-11', 'Lys-48' and 'Lys-63'-linked polyubiquitin chains. Has a much higher catalytic rate with 'Lys-11'-linked polyubiquitin chains (in vitro); however the physiological significance of these data are unsure. Hydrolyzes both linear and branched forms of polyubiquitin (By similarity). {ECO:0000250|UniProtKB:Q6GQQ9, ECO:0000269|PubMed:23334419, ECO:0000269|PubMed:26903241}. PTM: Phosphorylated by EGFR. {ECO:0000250|UniProtKB:Q6GQQ9}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6GQQ9}. Nucleus {ECO:0000250|UniProtKB:Q6GQQ9}. Note=Shuttles be cytoplasm and the nucleus in a XPO1/CRM1-dependent manner. {ECO:0000250|UniProtKB:Q6GQQ9}. SUBUNIT: Interacts with TRAF6. Interacts with PARK7, leading to inhibit deubiquitinase activity. Interacts with EGFR, ITCH and NEDD4 (By similarity). Interacts with TRAF3 (PubMed:23334419). Interacts with ZAP70 in activated T cells, but not in resting T cells (PubMed:26903241). {ECO:0000250|UniProtKB:Q6GQQ9, ECO:0000269|PubMed:23334419, ECO:0000269|PubMed:26903241}. DOMAIN: The protein undergoes a significant conformation change upon binding to ubiquitinated substrates. The loop that precedes the active site is in an autoinhibitory conformation in the apoprotein. Ubiquitin binding leads to a conformation change; the loop is stabilized in a catalytically competent conformation with the result that the active site Cys can form the reaction state intermediate. {ECO:0000250|UniProtKB:Q6GQQ9}. +Q9D7E3 OVCA2_MOUSE Esterase OVCA2 (EC 3.1.2.-) (Ovarian cancer-associated gene 2 protein homolog) 225 24,246 Active site (3); Chain (1) TISSUE SPECIFICITY: Strongly expressed in kidney and liver. Moderately expressed in brain, skin and testis. Weakly expressed in heart, lung, small intestine, spleen, stomach and thymus. {ECO:0000269|PubMed:11527402}. +P58307 OX1R_MOUSE Orexin receptor type 1 (Ox-1-R) (Ox1-R) (Ox1R) (Hypocretin receptor type 1) 416 46,781 Binding site (1); Chain (1); Disulfide bond (1); Glycosylation (1); Region (1); Sequence conflict (4); Site (1); Topological domain (8); Transmembrane (7) TRANSMEM 47 67 Helical; Name=1. {ECO:0000250|UniProtKB:O43613}.; TRANSMEM 83 105 Helical; Name=2. {ECO:0000250|UniProtKB:O43613}.; TRANSMEM 120 140 Helical; Name=3. {ECO:0000255}.; TRANSMEM 161 182 Helical; Name=4. {ECO:0000250|UniProtKB:O43613}.; TRANSMEM 214 235 Helical; Name=5. {ECO:0000250|UniProtKB:O43613}.; TRANSMEM 299 321 Helical; Name=6. {ECO:0000250|UniProtKB:O43613}.; TRANSMEM 337 360 Helical; Name=7. {ECO:0000250|UniProtKB:O43613}. TOPO_DOM 1 46 Extracellular. {ECO:0000250|UniProtKB:O43613}.; TOPO_DOM 68 82 Cytoplasmic. {ECO:0000250|UniProtKB:O43613}.; TOPO_DOM 106 119 Extracellular. {ECO:0000250|UniProtKB:O43613}.; TOPO_DOM 141 160 Cytoplasmic. {ECO:0000250|UniProtKB:O43613}.; TOPO_DOM 183 213 Extracellular. {ECO:0000250|UniProtKB:O43613}.; TOPO_DOM 236 298 Cytoplasmic. {ECO:0000250|UniProtKB:O43613}.; TOPO_DOM 322 336 Extracellular. {ECO:0000250|UniProtKB:O43613}.; TOPO_DOM 361 416 Cytoplasmic. {ECO:0000250|UniProtKB:O43613}. FUNCTION: Moderately selective excitatory receptor for orexin-A and, with a lower affinity, for orexin-B neuropeptide. Triggers an increase in cytoplasmic Ca(2+) levels in response to orexin-A binding. {ECO:0000250|UniProtKB:O43613}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O43613}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O43613}. DOMAIN: The N-terminal region is required for orexin signaling. {ECO:0000250|UniProtKB:O43613}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15256537}. +Q9WTJ2 OVOL1_MOUSE Putative transcription factor Ovo-like 1 (mOvo1) (mOvo1a) 267 30,222 Chain (1); Zinc finger (4) FUNCTION: Putative transcription factor. Involved in hair formation and spermatogenesis. May function in the differentiation and/or maintenance of the urogenital system. {ECO:0000269|PubMed:9808631}. SUBCELLULAR LOCATION: Nucleus. TISSUE SPECIFICITY: Expressed in skin, testis, kidney and weakly in lung. Not detected in heart, brain, spleen, liver and skeletal muscle. +O54901 OX2G_MOUSE OX-2 membrane glycoprotein (MRC OX-2 antigen) (CD antigen CD200) 278 31,256 Beta strand (19); Chain (1); Disulfide bond (3); Domain (2); Glycosylation (6); Helix (2); Mutagenesis (8); Sequence conflict (5); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (3) TRANSMEM 233 259 Helical. {ECO:0000255}. TOPO_DOM 31 232 Extracellular. {ECO:0000255}.; TOPO_DOM 260 278 Cytoplasmic. {ECO:0000255}. FUNCTION: Costimulates T-cell proliferation. May regulate myeloid cell activity in a variety of tissues (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SUBUNIT: CD200 and CD200R1 interact via their respective N-terminal Ig-like domains. {ECO:0000269|PubMed:23602662}. +Q8BGA9 OXA1L_MOUSE Mitochondrial inner membrane protein OXA1L (Oxidase assembly 1-like protein) (OXA1-like protein) 433 48,220 Chain (1); Modified residue (3); Sequence conflict (8); Topological domain (6); Transit peptide (1); Transmembrane (5) TRANSMEM 109 129 Helical. {ECO:0000255}.; TRANSMEM 135 155 Helical. {ECO:0000255}.; TRANSMEM 208 228 Helical. {ECO:0000255}.; TRANSMEM 256 276 Helical. {ECO:0000255}.; TRANSMEM 294 314 Helical. {ECO:0000255}. TOPO_DOM 1 108 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 130 134 Mitochondrial matrix. {ECO:0000255}.; TOPO_DOM 156 207 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 229 255 Mitochondrial matrix. {ECO:0000255}.; TOPO_DOM 277 293 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 315 433 Mitochondrial matrix. {ECO:0000255}. FUNCTION: Required for the insertion of integral membrane proteins into the mitochondrial inner membrane. Essential for the activity and assembly of cytochrome oxidase. Required for the correct biogenesis of ATP synthase and complex I in mitochondria (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Monomer; predominantly monomeric at low salt concentrations. Homooligomer; predominantly homooligomeric at high salt concentrations. Homodimer. Homotetramer. Interacts with MRPL13, MRPL20, MRPL28, MRPL48, MRPL49 and MRPL51. Associates preferentially as a dimer with the large ribosomal subunit 39S of the mitochondrial ribosome (By similarity). {ECO:0000250}. +P80205 OTX1_MOUSE Homeobox protein OTX1 (Orthodenticle homolog 1) 355 37,532 Chain (1); Compositional bias (1); Cross-link (1); DNA binding (1) FUNCTION: Probably plays a role in the development of the brain and the sense organs. Can bind to the BCD target sequence (BTS): 5'-TCTAATCCC-3'. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: Brain: restricted regions of the developing rostral brain including the presumptive cerebral cortex and olfactory bulbs; expressed in the developing olfactory, auricolar and ocular systems, including the covering of the optic nerve. +Q9D9N8 PADC1_MOUSE Protease-associated domain-containing protein 1 (Protease-associated domain-containing protein of 21 kDa) 188 21,085 Chain (1); Domain (1); Glycosylation (2); Signal peptide (1) PTM: N-glycosylated; required for efficient secretion. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +Q61644 PACN1_MOUSE Protein kinase C and casein kinase substrate in neurons protein 1 (Syndapin-1) 441 50,575 Beta strand (7); Chain (1); Coiled coil (1); Domain (2); Helix (9); Modified residue (11); Mutagenesis (7); Turn (1) FUNCTION: Binds to membranes via its F-BAR domain and mediates membrane tubulation. Plays a role in the reorganization of the microtubule cytoskeleton via its interaction with MAPT; this decreases microtubule stability and inhibits MAPT-induced microtubule polymerization. Plays a role in cellular transport processes by recruiting DNM1, DNM2 and DNM3 to membranes. Plays a role in the reorganization of the actin cytoskeleton and in neuron morphogenesis via its interaction with COBL and WASL, and by recruiting COBL to the cell cortex. Plays a role in the regulation of neurite formation, neurite branching and the regulation of neurite length. Required for normal synaptic vesicle endocytosis; this process retrieves previously released neurotransmitters to accommodate multiple cycles of neurotransmission. Required for normal excitatory and inhibitory synaptic transmission. {ECO:0000269|PubMed:11082044, ECO:0000269|PubMed:20404169, ECO:0000269|PubMed:21926968, ECO:0000269|PubMed:23035120}. PTM: Phosphorylated by casein kinase 2 (CK2) and protein kinase C (PKC). SUBCELLULAR LOCATION: Cytoplasm. Cell projection {ECO:0000250}. Cell junction, synapse, synaptosome {ECO:0000250}. Cell projection, ruffle membrane. Membrane; Peripheral membrane protein. Cytoplasmic vesicle membrane; Peripheral membrane protein. Cell junction, synapse. Cytoplasm, cytosol. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=In primary neuronal cultures, present at a high level in presynaptic nerve terminals and in the cell body. Colocalizes with DNM1 at vesicular structures in the cell body and neurites (By similarity). Colocalizes with MAPT in axons. {ECO:0000250}. SUBUNIT: Homodimer. May form heterooligomers with other PACSINs. Interacts with both COBL and DBNL. Identified in a complex composed of COBL, PACSIN1 and WASL. Interacts with EHD3 (By similarity). Interacts (via SH3 domain) with SYNJ1 and WASL. Interacts (via SH3 domain) with DNM1; the interaction is reduced by DNM1 phosphorylation. Interacts with DNM2 and DNM3. Interacts with MAPT. Interacts with EHD1. Interacts with TRPV4. {ECO:0000250, ECO:0000269|PubMed:11082044, ECO:0000269|PubMed:15930129, ECO:0000269|PubMed:16627472, ECO:0000269|PubMed:20404169, ECO:0000269|PubMed:21926968, ECO:0000269|PubMed:23035120}. DOMAIN: The F-BAR domain forms a coiled coil and mediates membrane-binding and membrane tubulation. In the autoinhibited conformation, interaction with the SH3 domain inhibits membrane tubulation mediated by the F-BAR domain. DNM1 binding abolishes autoinhibition. {ECO:0000269|PubMed:20404169}. TISSUE SPECIFICITY: Highly expressed in brain. Detected in hippocampus and dorsal root ganglion neurons. Detected in rod photoreceptor terminals in the outer plexiform layer of the retina (at protein level). In CNS neurons, high levels in the pyramidal cells of the hippocampus, Purkinje cells of the cerebellum and large neurons of the cortex and brain stem. {ECO:0000269|PubMed:11082044, ECO:0000269|PubMed:21926968, ECO:0000269|PubMed:23035120, ECO:0000269|PubMed:9746365}. +Q9Z185 PADI1_MOUSE Protein-arginine deiminase type-1 (EC 3.5.3.15) (Peptidylarginine deiminase I) (Protein-arginine deiminase type I) 662 73,824 Active site (1); Chain (1); Metal binding (17) FUNCTION: Catalyzes the deimination of arginine residues of proteins. {ECO:0000250|UniProtKB:Q9ULC6}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9ULC6}. SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9ULC6}. TISSUE SPECIFICITY: Expressed only in the epidermis and uterus. {ECO:0000269|PubMed:1778991}. +Q08642 PADI2_MOUSE Protein-arginine deiminase type-2 (EC 3.5.3.15) (Peptidylarginine deiminase II) (Protein-arginine deiminase type II) 673 76,250 Active site (1); Chain (1); Metal binding (21); Modified residue (2); Sequence conflict (3) FUNCTION: Catalyzes the deimination of arginine residues of proteins. {ECO:0000250|UniProtKB:Q9Y2J8}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y2J8}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9Y2J8}. TISSUE SPECIFICITY: Expressed in various tissues including muscle, uterus, spinal cord, salivary gland and pancreas. {ECO:0000269|PubMed:1778991}. +Q9Z184 PADI3_MOUSE Protein-arginine deiminase type-3 (EC 3.5.3.15) (Peptidylarginine deiminase III) (Protein-arginine deiminase type III) 664 75,073 Chain (1); Sequence conflict (5) FUNCTION: Catalyzes the deimination of arginine residues of proteins. {ECO:0000250|UniProtKB:Q9ULW8}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9ULW8}. TISSUE SPECIFICITY: Epidermis and hair follicles. {ECO:0000269|PubMed:1778991}. +Q9Z183 PADI4_MOUSE Protein-arginine deiminase type-4 (EC 3.5.3.15) (Peptidylarginine deiminase IV) (Protein-arginine deiminase type IV) 666 74,415 Active site (4); Binding site (1); Chain (1); Metal binding (17); Modified residue (5); Sequence conflict (10) FUNCTION: Catalyzes the citrullination/deimination of arginine residues of proteins such as histones, thereby playing a key role in histone code and regulation of stem cell maintenance. Citrullinates histone H1 at 'Arg-54' (to form H1R54ci), histone H3 at 'Arg-2', 'Arg-8', 'Arg-17' and/or 'Arg-26' (to form H3R2ci, H3R8ci, H3R17ci, H3R26ci, respectively) and histone H4 at 'Arg-3' (to form H4R3ci). Acts as a key regulator of stem cell maintenance by mediating citrullination of histone H1: citrullination of 'Arg-54' of histone H1 (H1R54ci) results in H1 displacement from chromatin and global chromatin decondensation, thereby promoting pluripotency and stem cell maintenance. Promotes profound chromatin decondensation during the innate immune response to infection in neutrophils by mediating formation of H1R54ci. Citrullination of histone H3 prevents their methylation by CARM1 and HRMT1L2/PRMT1 and represses transcription. Citrullinates EP300/P300 at 'Arg-2142', which favors its interaction with NCOA2/GRIP1. {ECO:0000269|PubMed:15339660, ECO:0000269|PubMed:20733033, ECO:0000269|PubMed:23650392, ECO:0000269|PubMed:24463520}. PTM: Autocitrullination at Arg-372 and Arg-374 inactivates the enzyme. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. TISSUE SPECIFICITY: Expressed in pluripotent embryonic stem and induced pluripotent stem cells but not multipotent neural stem cells. {ECO:0000269|PubMed:24463520}. +Q2EMV9 PAR14_MOUSE Protein mono-ADP-ribosyltransferase PARP14 (EC 2.4.2.-) (ADP-ribosyltransferase diphtheria toxin-like 8) (ARTD8) (Collaborator of STAT6) (CoaSt6) (Poly [ADP-ribose] polymerase 14) (PARP-14) 1817 203,802 Alternative sequence (1); Beta strand (7); Binding site (6); Chain (1); Compositional bias (1); Domain (5); Erroneous initiation (1); Helix (2); Modified residue (2); Natural variant (3); Region (7); Sequence caution (1); Sequence conflict (5); Turn (2) FUNCTION: ADP-ribosyltransferase that mediates mono-ADP-ribosylation of glutamate residues on target proteins (PubMed:27796300). In contrast to PARP1 and PARP2, it is not able to mediate poly-ADP-ribosylation (By similarity). Catalyzes mono-ADP-ribosylating STAT1 at 'Glu-657' and 'Glu-705' and thus decreasing STAT1 phosphorylation, negatively regulates pro-inflammatory cytokines production in macrophages in response to IFNG stimulation (PubMed:27796300). Mono-ADP-ribosylates STAT6; enhancing STAT6-dependent transcription (PubMed:27796300). In macrophages, positively regulates MRC1 expression in response to IL4 stimulation by promoting STAT6 phosphorylation (PubMed:27796300). Mono-ADP-ribosylates PARP9 (By similarity). {ECO:0000250|UniProtKB:Q460N5, ECO:0000269|PubMed:27796300}. PTM: Auto-ADP-ribosylated. {ECO:0000250|UniProtKB:Q460N5}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16537510}. Cytoplasm {ECO:0000269|PubMed:16537510}. Note=In steady state cells the protein is mostly nuclear (PubMed:16537510). A minor proportion is detected in the cytoplasm (PubMed:16537510). In macrophages, mainly localizes to the cytoplasm (By similarity). {ECO:0000250|UniProtKB:Q460N5, ECO:0000269|PubMed:16537510}. SUBUNIT: Interacts with STAT6 (PubMed:16537510). Interacts with PARP10 (By similarity). Interacts with PARP9 in IFNG-stimulated macrophages; the interaction prevents PARP14-mediated STAT1 and STAT6 ADP-riboslylation (By similarity). {ECO:0000250|UniProtKB:Q460N5, ECO:0000269|PubMed:16537510}. TISSUE SPECIFICITY: Weakly expressed in the thymus during development and in adulthood (PubMed:18069692). Expressed in macrophages (PubMed:27796300). {ECO:0000269|PubMed:18069692, ECO:0000269|PubMed:27796300}. +Q99NH2 PARD3_MOUSE Partitioning defective 3 homolog (PAR-3) (PARD-3) (Atypical PKC isotype-specific-interacting protein) (ASIP) (Ephrin-interacting protein) (PHIP) 1333 149,075 Alternative sequence (8); Beta strand (15); Chain (1); Coiled coil (4); Compositional bias (1); Domain (3); Helix (5); Modified residue (23); Mutagenesis (5); Region (3); Sequence conflict (3); Turn (1) FUNCTION: Adapter protein involved in asymmetrical cell division and cell polarization processes (By similarity). Seems to play a central role in the formation of epithelial tight junctions (By similarity). Targets the phosphatase PTEN to cell junctions (By similarity). Association with PARD6B may prevent the interaction of PARD3 with F11R/JAM1, thereby preventing tight junction assembly (PubMed:11839275). The PARD6-PARD3 complex links GTP-bound Rho small GTPases to atypical protein kinase C proteins (By similarity). Required for establishment of neuronal polarity and normal axon formation in cultured hippocampal neurons (By similarity). Involved in Schwann cell peripheral myelination (PubMed:21949390). {ECO:0000250|UniProtKB:Q8TEW0, ECO:0000250|UniProtKB:Q9Z340, ECO:0000269|PubMed:11839275, ECO:0000269|PubMed:21949390}. PTM: Acetylated. Deacetylated by SIRT2, thereby inhibiting Schwann cell peripheral myelination. {ECO:0000269|PubMed:21949390}.; PTM: Phosphorylation at Ser-824 by PRKCZ and PRKCI occurs at the most apical tip of epithelial cell-cell contacts during the initial phase of tight junction formation and may promote dissociation of the complex with PARD6. EGF-induced Tyr-1123 phosphorylation mediates dissociation from LIMK2 (By similarity). Phosphorylation by AURKA at Ser-958 is required for the normal establishment of neuronal polarity (By similarity). Isoform 4 and isoform 5 are phosphorylated during oocyte maturation (Probable). {ECO:0000250, ECO:0000305}. SUBCELLULAR LOCATION: Cytoplasm. Endomembrane system. Cell junction. Cell junction, tight junction {ECO:0000269|PubMed:10934475, ECO:0000269|PubMed:20080746}. Cell junction, adherens junction {ECO:0000269|PubMed:20080746}. Cytoplasm, cell cortex. Cytoplasm, cytoskeleton. Cell membrane {ECO:0000250}. Note=Localized along the cell-cell contact region. Colocalizes with PARD6A and PRKCI at epithelial tight junctions. Colocalizes with the cortical actin that overlays the meiotic spindle during metaphase I and metaphase II. Presence of KRIT1, CDH5 and RAP1B is required for its localization to the cell junction (By similarity). Colocalized with SIRT2 in internode region of myelin sheat. {ECO:0000250}. SUBUNIT: Isoform 2, but not at least isoform 3 interacts with PRKCZ. Interacts with PRCKI and CDH5. Interacts (via PDZ 3 domain) with PTEN (via C-terminus). Component of a complex whose core is composed of ARHGAP17, AMOT, MPP5/PALS1, PATJ and PARD3/PAR3. Interacts with LIMK2, AURKA and AURKB. Component of the Par polarity complex, composed of at least phosphorylated PRKCZ, PARD3 and TIAM1. Interacts with ECT2 and FBF1 (By similarity). Interacts (via PDZ 1 domain) with F11R/JAM1, PARD6A and PARD6B. Part of a complex with PARD6A or PARD6B, PRKCI or PRKCZ and CDC42 or RAC1. Directly interacts with TIAM1 and TIAM2. Interacts with SIRT2. Interacts (via coiled-coil domain) with FRMD4A (PubMed:20080746). Found in a complex with PARD3, CYTH1 and FRMD4A (PubMed:20080746). Interacts with SAPCD2 (By similarity). Interacts with PRKCA (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q8TEW0, ECO:0000269|PubMed:10934474, ECO:0000269|PubMed:10934475, ECO:0000269|PubMed:11447115, ECO:0000269|PubMed:11839275, ECO:0000269|PubMed:19893486, ECO:0000269|PubMed:20047332, ECO:0000269|PubMed:20080746}. DOMAIN: Contains a conserved N-terminal oligomerization domain (NTD) that is involved in oligomerization and is essential for proper subapical membrane localization. {ECO:0000250}.; DOMAIN: The second PDZ domain mediates interaction with membranes containing phosphoinositol lipids. {ECO:0000250}. TISSUE SPECIFICITY: All isoforms are expressed in heart, while expression in brain is mainly limited to isoform 1, and to isoform 3 to a weaker level. +O88622 PARG_MOUSE Poly(ADP-ribose) glycohydrolase (EC 3.2.1.143) 969 109,324 Active site (3); Alternative sequence (2); Beta strand (19); Binding site (3); Chain (1); Erroneous termination (2); Helix (24); Modified residue (12); Motif (2); Region (4); Sequence conflict (5); Turn (8) FUNCTION: Poly(ADP-ribose) glycohydrolase that degrades poly(ADP-ribose) by hydrolyzing the ribose-ribose bonds present in poly(ADP-ribose). PARG acts both as an endo- and exoglycosidase, releasing poly(ADP-ribose) of different length as well as ADP-ribose monomers. It is however unable to cleave the ester bond between the terminal ADP-ribose and ADP-ribosylated residues, leaving proteins that are mono-ADP-ribosylated. Poly(ADP-ribose) is synthesized after DNA damage is only present transiently and is rapidly degraded by PARG. Required to prevent detrimental accumulation of poly(ADP-ribose) upon prolonged replicative stress, while it is not required for recovery from transient replicative stress. Required for retinoid acid-dependent gene transactivation, probably by removing poly(ADP-ribose) from histone demethylase KDM4D, allowing chromatin derepression at RAR-dependent gene promoters. Involved in the synthesis of ATP in the nucleus, together with PARP1, NMNAT1 and NUDT5. Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming. {ECO:0000250|UniProtKB:Q86W56}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q86W56}. Note=Colocalizes with PCNA at replication foci. Relocalizes to the cytoplasm in response to DNA damage (By similarity). {ECO:0000250|UniProtKB:Q86W56}. SUBUNIT: Interacts with PCNA. Interacts with NUDT5. {ECO:0000250|UniProtKB:Q86W56}. DOMAIN: The PIP-box mediates interaction with PCNA and localization to replication foci. {ECO:0000250|UniProtKB:Q86W56}. +Q6IRT3 PARI_MOUSE PCNA-interacting partner (PARI) (PARP-1 binding protein) (PARP1-binding protein) (PARPBP) 573 64,105 Chain (1); Erroneous initiation (1); Sequence conflict (5) FUNCTION: Required to suppress inappropriate homologous recombination, thereby playing a central role DNA repair and in the maintenance of genomic stability. Antagonizes homologous recombination by interfering with the formation of the RAD51-DNA homologous recombination structure. Binds single-strand DNA and poly(A) homopolymers. Positively regulate the poly(ADP-ribosyl)ation activity of PARP1; however such function may be indirect (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Localizes to chromatin in response to S phase arrest but not in mitosis. Targeted to chromatin via its interaction with PCNA (By similarity). {ECO:0000250}. SUBUNIT: Interacts with RAD51 and PCNA. Interacts with PARP1 (By similarity). {ECO:0000250}. +Q80ZE4 PAQR7_MOUSE Membrane progestin receptor alpha (mPR alpha) (Membrane progesterone P4 receptor alpha) (Membrane progesterone receptor alpha) (PPAR-gamma-induced liver protein) (Progesterone and adipoQ receptor family member 7) (Progestin and adipoQ receptor family member 7) (Progestin and adipoQ receptor family member VII) 345 39,306 Chain (1); Sequence conflict (2); Topological domain (8); Transmembrane (7) TRANSMEM 75 95 Helical; Name=1. {ECO:0000255}.; TRANSMEM 103 123 Helical; Name=2. {ECO:0000255}.; TRANSMEM 137 157 Helical; Name=3. {ECO:0000255}.; TRANSMEM 169 189 Helical; Name=4. {ECO:0000255}.; TRANSMEM 244 264 Helical; Name=5. {ECO:0000255}.; TRANSMEM 269 289 Helical; Name=6. {ECO:0000255}.; TRANSMEM 316 336 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 74 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 96 102 Extracellular. {ECO:0000255}.; TOPO_DOM 124 136 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 158 168 Extracellular. {ECO:0000255}.; TOPO_DOM 190 243 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 265 268 Extracellular. {ECO:0000255}.; TOPO_DOM 290 315 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 337 345 Extracellular. {ECO:0000255}. FUNCTION: Plasma membrane progesterone (P4) receptor coupled to G proteins. Seems to act through a G(i) mediated pathway. May be involved in oocyte maturation. Involved in neurosteroid inhibition of apoptosis. Also binds dehydroepiandrosterone (DHEA), pregnanolone, pregnenolone and allopregnanolone. {ECO:0000250|UniProtKB:Q86WK9}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q86WK9}; Multi-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Detected in most adult tissues. Higher expression found in white fat and liver than brown fat and skeletal muscle. {ECO:0000269|PubMed:15589683}. +Q8R189 PAQRA_MOUSE Monocyte to macrophage differentiation factor 2 (Progestin and adipoQ receptor family member 10) (Progestin and adipoQ receptor family member X) 247 28,910 Chain (1); Topological domain (8); Transmembrane (7) TRANSMEM 40 60 Helical. {ECO:0000255}.; TRANSMEM 67 87 Helical. {ECO:0000255}.; TRANSMEM 104 124 Helical. {ECO:0000255}.; TRANSMEM 134 154 Helical. {ECO:0000255}.; TRANSMEM 160 180 Helical. {ECO:0000255}.; TRANSMEM 183 203 Helical. {ECO:0000255}.; TRANSMEM 211 231 Helical. {ECO:0000255}. TOPO_DOM 1 39 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 61 66 Lumenal. {ECO:0000255}.; TOPO_DOM 88 103 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 125 133 Lumenal. {ECO:0000255}.; TOPO_DOM 155 159 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 181 182 Lumenal. {ECO:0000255}.; TOPO_DOM 204 210 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 232 247 Lumenal. {ECO:0000255}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q8CIE4 PAR10_MOUSE Protein mono-ADP-ribosyltransferase PARP10 (EC 2.4.2.-) (ADP-ribosyltransferase diphtheria toxin-like 10) (ARTD10) (Poly [ADP-ribose] polymerase 10) (PARP-10) 960 103,679 Chain (1); Domain (1); Erroneous initiation (1); Frameshift (1); Modified residue (5); Motif (2); Region (1); Sequence conflict (5) FUNCTION: ADP-ribosyltransferase that mediates mono-ADP-ribosylation of glutamate and aspartate residues on target proteins. In contrast to PARP1 and PARP2, it is not able to mediate poly-ADP-ribosylation. Catalyzes mono-ADP-ribosylation of GSK3B, leading to negatively regulate GSK3B kinase activity. Involved in translesion DNA synthesis in response to DNA damage via its interaction with PCNA. {ECO:0000250|UniProtKB:Q53GL7}. PTM: Stimulated through its phosphorylation by CDK2. Acquires CDK-dependent phosphorylation through late-G1 to S phase, and from prometaphase to cytokinesis in the nucleolar organizing regions. Phosphorylation is suppressed in growth-arrested cells. {ECO:0000250|UniProtKB:Q53GL7}.; PTM: Auto-mono-ADP-ribosylated on glutamate and lysine residues. {ECO:0000250|UniProtKB:Q53GL7}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8K3Y6}. Nucleus {ECO:0000250|UniProtKB:Q8K3Y6}. Note=Localizes in the cytoplasm at steady state, but shuttles between nucleus and cytoplasm in a XPO1-dependent manner. {ECO:0000250|UniProtKB:Q8K3Y6}. SUBUNIT: Interacts with MYC. Interacts with PARP14. Interacts (via-PIP box and ubiquitin-interacting motifs) with PCNA. {ECO:0000250|UniProtKB:Q53GL7}. DOMAIN: The PIP-box mediates the interaction with PCNA. {ECO:0000250|UniProtKB:Q53GL7}. +Q6NZQ4 PAXI1_MOUSE PAX-interacting protein 1 (PAX transactivation activation domain-interacting protein) 1056 119,269 Chain (1); Compositional bias (2); Domain (6); Modified residue (2); Motif (1); Region (2) FUNCTION: Involved in DNA damage response and in transcriptional regulation through histone methyltransferase (HMT) complexes such as the MLL2/MLL3 complex. Plays a role in early development. In DNA damage response is required for cell survival after ionizing radiation. In vitro shown to be involved in the homologous recombination mechanism for the repair of double-strand breaks (DSBs). Its localization to DNA damage foci requires Rnf8 and Ube2n. Recruits Tp53bp1 to DNA damage foci and, at least in particular repair processes, effective DNA damage response appears to require the association with Tp53bp1 phosphorylated by Atm. Together with Tp53bp1 regulates Atm association (By similarity). Proposed to recruit Pagr1 to sites of DNA damage and the Pagr1:Paxip1 complex is required for cell survival in response to DNA damage independently of the MLL2/MLL3 complex. However, this function has been questioned (PubMed:19124460, PubMed:26744420). Promotes ubiquitination of PCNA following UV irradiation and may regulate recruitment of polymerase eta and Rad51 to chromatin after DNA damage. Proposed to be involved in transcriptional regulation by linking MLL-containing histone methyltransferase (HMT) complexes to gene promoters by interacting with promoter-bound transcription factors such as Pax2. Associates with gene promoters that are known to be regulated by Kmt2d/Mll2 (By similarity). During immunoglobulin class switching in activated B-cells is involved in trimethylation of histone H3 at 'Lys-4' and in transcription initiation of downstream switch regions at the immunoglobulin heavy-chain (Igh) locus; this function appears to involve the recruitment of MLL-containing HMT complexes. Conflictingly, its function in transcriptional regulation during immunoglobulin class switching is reported to be independent of the MLL2/MLL3 complex (PubMed:20671152, PubMed:26744420). {ECO:0000250, ECO:0000269|PubMed:10908331, ECO:0000269|PubMed:12588986, ECO:0000269|PubMed:17925232, ECO:0000269|PubMed:19124460, ECO:0000269|PubMed:19414588, ECO:0000269|PubMed:20671152, ECO:0000269|PubMed:26744420}. SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000269|PubMed:10908331, ECO:0000269|PubMed:19124460}. Chromosome {ECO:0000250|UniProtKB:Q6ZW49}. Note=Localizes to DNA damage foci upon ionizing radiation. {ECO:0000250|UniProtKB:Q6ZW49}. SUBUNIT: Interacts with the C-terminal transactivation domain of PAX2 (PubMed:10908331). Forms a constitutive complex with PAGR1 independently of the MLL2/MLL3 complex (PubMed:19124460, PubMed:26744420). Interacts with TP53BP1 (when phosphorylated at the N-terminus by ATM) (By similarity). Interacts with HLTF (By similarity). Component of the KMT2 family MLL2/MLL3 complex (also named ASCOM complex), at least composed of the HMTs KMT2D and/or KMT2C, the common subunits ASH2L, RBBP5, WDR5 and DPY30, and the complex type-specific subunits PAXIP1/PTIP, PAGR1, NCOA6 and KDM6A; required for the association of PAGR1 with the MLL2/MLL3 complex (By similarity). {ECO:0000250|UniProtKB:Q6ZW49, ECO:0000269|PubMed:10908331, ECO:0000269|PubMed:19124460, ECO:0000269|PubMed:26744420}. DOMAIN: The BRCT 1 and 2 domains mediate the interaction with PAGR1A. {ECO:0000269|PubMed:26744420}.; DOMAIN: The BRCT 5 and 6 domains mediate the association with the MLL2/MLL3 complex (PubMed:26744420). The BRCT 5 and 6 domains function as a single module and are necessary and sufficient for in vitro phospho-specific binding (substrates phosphorylated by the kinases ataxia telangiectasia-mutated (ATM), ataxia telangiectasia and RAD3-related (ATR) in response to gamma irradiation). In contrast, in vivo two pairs of BRCT domains (3-6) bind to phosphorylated TP53BP1 much more efficiently. {ECO:0000269|PubMed:26744420}. TISSUE SPECIFICITY: Expression detected in all tissues examined, including brain stem, cerebellum, cortex, heart, spleen, kidney, liver, thymus and lung. {ECO:0000269|PubMed:10908331}. +Q3ULW8 PARP3_MOUSE Protein mono-ADP-ribosyltransferase PARP3 (EC 2.4.2.-) (ADP-ribosyltransferase diphtheria toxin-like 3) (ARTD3) (DNA ADP-ribosyltransferase PARP3) (EC 2.4.2.-) (NAD(+) ADP-ribosyltransferase 3) (ADPRT-3) (Poly [ADP-ribose] polymerase 3) (PARP-3) (Poly[ADP-ribose] synthase 3) (pADPRT-3) 533 59,949 Alternative sequence (1); Chain (1); Domain (2); Modified residue (9); Motif (1); Sequence conflict (15) FUNCTION: Mono-ADP-ribosyltransferase that mediates mono-ADP-ribosylation of target proteins and plays a key role in the response to DNA damage (PubMed:21270334, PubMed:24598253). Mediates mono-ADP-ribosylation of glutamate, aspartate or lysine residues on target proteins (By similarity). In contrast to PARP1 and PARP2, it is not able to mediate poly-ADP-ribosylation (By similarity). Associates with a number of DNA repair factors and is involved in the response to exogenous and endogenous DNA strand breaks (PubMed:21270334). Together with APLF, promotes the retention of the LIG4-XRCC4 complex on chromatin and accelerate DNA ligation during non-homologous end-joining (NHEJ) (By similarity). Cooperates with the XRRC6-XRCC5 (Ku70-Ku80) heterodimer to limit end-resection thereby promoting accurate NHEJ (PubMed:24598253). Involved in DNA repair by mediating mono-ADP-ribosylation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism, such as XRRC5 and XRCC6 (By similarity). ADP-ribosylation follows DNA damage and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks (By similarity). May link the DNA damage surveillance network to the mitotic fidelity checkpoint (By similarity). In addition to proteins, also able to ADP-ribosylate DNA: mediates DNA mono-ADP-ribosylation of DNA strand break termini via covalent addition of a single ADP-ribose moiety to a 5'- or 3'-terminal phosphate residues in DNA containing multiple strand breaks (By similarity). Acts as a negative regulator of immunoglobulin class switch recombination, probably by controlling the level of AICDA /AID on the chromatin (PubMed:26000965). {ECO:0000250|UniProtKB:Q9Y6F1, ECO:0000269|PubMed:21270334, ECO:0000269|PubMed:24598253, ECO:0000269|PubMed:26000965}. PTM: Auto-ADP-ribosylated. {ECO:0000250|UniProtKB:Q9Y6F1}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8K3Y6}. Nucleus {ECO:0000250|UniProtKB:Q8K3Y6}. Note=Localizes in the cytoplasm at steady state, but shuttles between nucleus and cytoplasm in a XPO1-dependent manner. {ECO:0000250|UniProtKB:Q8K3Y6}. SUBUNIT: Interacts with PARP1; leading to activate PARP1 in absence of DNA. Interacts with PRKDC. Interacts with XRCC5/Ku80; the interaction is dependent on nucleic acids. Interacts with XRCC6/Ku70; the interaction is dependent on nucleic acids. Interacts with EZH2, HDAC1, HDAC2, SUZ12, YY1, LRIG3 and LIG4. {ECO:0000250|UniProtKB:Q9Y6F1}. +P24610 PAX3_MOUSE Paired box protein Pax-3 479 52,949 Chain (1); DNA binding (1); Domain (1); Modified residue (3); Natural variant (1); Sequence conflict (2) FUNCTION: Transcription factor that may regulate cell proliferation, migration and apoptosis. Involved in neural development and myogenesis. Transcriptional activator of MITF, acting synergistically with SOX10 (By similarity). {ECO:0000250|UniProtKB:P23760, ECO:0000269|PubMed:1682057, ECO:0000269|PubMed:22862948}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P23760}. SUBUNIT: Can bind to DNA as homodimer or a heterodimer with PAX7. Interacts with DAXX. Interacts with PAXBP1; the interaction links PAX3 to a WDR5-containing histone methyltransferase complex. Interacts with TBX18. Interacts with SOX10 (By similarity). {ECO:0000250|UniProtKB:P23760, ECO:0000269|PubMed:18644785, ECO:0000269|PubMed:22862948}. DISEASE: Note=The Splotch (Sp) mouse mutant displays defects in neural tube closure in the form of exencephaly and spina bifida. The splotch-delayed (Spd) phenotype is less severe than the other Sp alleles. {ECO:0000269|PubMed:1682057}. +Q99LX0 PARK7_MOUSE Protein/nucleic acid deglycase DJ-1 (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase) (Parkinson disease protein 7 homolog) (Parkinsonism-associated deglycase) (Protein DJ-1) (DJ-1) 189 20,021 Active site (2); Chain (1); Cross-link (1); Initiator methionine (1); Lipidation (3); Modified residue (5); Mutagenesis (3); Propeptide (1); Sequence conflict (1) FUNCTION: Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of advanced glycation endproducts (AGE) that cause irreversible damage. Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair (By similarity). Also displays an apparent glyoxalase activity that in fact reflects its deglycase activity (PubMed:22523093). Plays an important role in cell protection against oxidative stress and cell death acting as oxidative stress sensor and redox-sensitive chaperone and protease; functions probably related to its primary function (PubMed:15784737, PubMed:17015834, PubMed:20800516, PubMed:21068725). It is involved in neuroprotective mechanisms like the stabilization of NFE2L2 and PINK1 proteins, male fertility as a positive regulator of androgen signaling pathway as well as cell growth and transformation through, for instance, the modulation of NF-kappa-B signaling pathway (PubMed:17015834, PubMed:21097510). Eliminates hydrogen peroxide and protects cells against hydrogen peroxide-induced cell death (PubMed:17766438). Required for correct mitochondrial morphology and function as well as for autophagy of dysfunctional mitochondria (PubMed:20186336). Plays a role in regulating expression or stability of the mitochondrial uncoupling proteins SLC25A14 and SLC25A27 in dopaminergic neurons of the substantia nigra pars compacta and attenuates the oxidative stress induced by calcium entry into the neurons via L-type channels during pacemaking (PubMed:21068725). Regulates astrocyte inflammatory responses, may modulate lipid rafts-dependent endocytosis in astrocytes and neuronal cells (PubMed:23847046, PubMed:19276172). In pancreatic islets, involved in the maintenance of mitochondrial reactive oxygen species (ROS) levels and glucose homeostasis in an age- and diet dependent manner (PubMed:22611253). Protects pancreatic beta cells from cell death induced by inflammatory and cytotoxic setting (PubMed:26422139). Binds to a number of mRNAs containing multiple copies of GG or CC motifs and partially inhibits their translation but dissociates following oxidative stress (By similarity). Metal-binding protein able to bind copper as well as toxic mercury ions, enhances the cell protection mechanism against induced metal toxicity (PubMed:23792957). In macrophages, interacts with the NADPH oxidase subunit NCF1 to direct NADPH oxidase-dependent ROS production, and protects against sepsis (PubMed:26021615). {ECO:0000250|UniProtKB:Q99497, ECO:0000269|PubMed:15784737, ECO:0000269|PubMed:17015834, ECO:0000269|PubMed:17766438, ECO:0000269|PubMed:19276172, ECO:0000269|PubMed:20186336, ECO:0000269|PubMed:20800516, ECO:0000269|PubMed:21068725, ECO:0000269|PubMed:22523093, ECO:0000269|PubMed:22611253, ECO:0000269|PubMed:23792957, ECO:0000269|PubMed:23847046, ECO:0000269|PubMed:26021615, ECO:0000269|PubMed:26422139}. PTM: Sumoylated on Lys-130 by PIAS2 or PIAS4; which is essential for cell-growth promoting activity and transforming activity. {ECO:0000250|UniProtKB:Q99497}.; PTM: Undergoes cleavage of a C-terminal peptide and subsequent activation of protease activity in response to oxidative stress. {ECO:0000250|UniProtKB:Q99497}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23847046}; Lipid-anchor {ECO:0000269|PubMed:23847046}. Cytoplasm {ECO:0000250|UniProtKB:Q99497}. Membrane raft {ECO:0000269|PubMed:23847046}. Nucleus {ECO:0000250|UniProtKB:Q99497}. Mitochondrion {ECO:0000250|UniProtKB:Q99497}. Note=Under normal conditions, located predominantly in the cytoplasm and, to a lesser extent, in the nucleus and mitochondrion. Translocates to the mitochondrion and subsequently to the nucleus in response to oxidative stress and exerts an increased cytoprotective effect against oxidative damage (By similarity). Membrane raft localization in astrocytes and neuronal cells requires palmitoylation (PubMed:23847046). {ECO:0000250|UniProtKB:Q99497, ECO:0000269|PubMed:23847046}. SUBUNIT: Homodimer. Binds EFCAB6/DJBP and PIAS2. Part of a ternary complex containing PARK7, EFCAB6/DJBP and AR. Binds to HIPK1 (By similarity). Interacts (via N-terminus) with OTUD7B (PubMed:21097510). Interacts with BBS1, CLCF1 and MTERF (PubMed:21097510). Interacts (via C-terminus) with NCF1; the interaction is enhanced by LPS and modulates NCF1 phosphorylation and membrane translocation (PubMed:26021615). {ECO:0000250|UniProtKB:Q99497, ECO:0000269|PubMed:21097510, ECO:0000269|PubMed:26021615}. TISSUE SPECIFICITY: Expressed in erythroblasts and in mature red blood cells from peripheral blood (at protein level) (PubMed:20800516). In pancreas, expression is higher in islets than surrounding exocrine tissues (PubMed:22611253). {ECO:0000269|PubMed:20800516, ECO:0000269|PubMed:22611253}. +Q8C1B2 PARPT_MOUSE Protein mono-ADP-ribosyltransferase TIPARP (EC 2.4.2.-) (ADP-ribosyltransferase diphtheria toxin-like 14) (ARTD14) (TCDD-inducible poly [ADP-ribose] polymerase) 657 75,901 Chain (1); Domain (2); Modified residue (1); Motif (1); Sequence conflict (2); Zinc finger (1) FUNCTION: ADP-ribosyltransferase that mediates mono-ADP-ribosylation of glutamate, aspartate and cysteine residues on target proteins (By similarity). Acts as a negative regulator of AHR by mediating mono-ADP-ribosylation of AHR, leading to inhibit transcription activator activity of AHR (Probable). {ECO:0000250|UniProtKB:Q7Z3E1, ECO:0000305|PubMed:23275542}. PTM: Auto-mono-ADP-ribosylated. {ECO:0000250|UniProtKB:Q7Z3E1}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23275542}. SUBUNIT: Interacts with AHR. {ECO:0000250|UniProtKB:Q7Z3E1}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:11716501}. +Q923D3 PARM1_MOUSE Prostate androgen-regulated mucin-like protein 1 homolog (PARM-1) 296 30,667 Chain (1); Glycosylation (3); Modified residue (1); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 245 265 Helical. {ECO:0000255}. TOPO_DOM 21 244 Extracellular. {ECO:0000255}.; TOPO_DOM 266 296 Cytoplasmic. {ECO:0000255}. FUNCTION: May regulate TLP1 expression and telomerase activity, thus enabling certain prostatic cells to resist apoptosis. {ECO:0000250}. PTM: Highly N-glycosylated and O-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Endosome membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. +Q8VHR0 PCD18_MOUSE Protocadherin 18 1134 125,420 Chain (1); Domain (6); Erroneous initiation (1); Glycosylation (3); Region (1); Sequence conflict (5); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 700 720 Helical. {ECO:0000255}. TOPO_DOM 28 699 Extracellular. {ECO:0000255}.; TOPO_DOM 721 1134 Cytoplasmic. {ECO:0000255}. FUNCTION: Potential calcium-dependent cell-adhesion protein. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Interacts with DAB1. {ECO:0000269|PubMed:11716507}. TISSUE SPECIFICITY: Predominantly expressed in kidney and lung. {ECO:0000269|PubMed:11716507}. +Q91Y02 PCDBI_MOUSE Protocadherin beta-18 (PCDH-beta-18) 792 86,959 Chain (1); Domain (6); Glycosylation (3); Signal peptide (1); Transmembrane (1) TRANSMEM 693 713 Helical. {ECO:0000255}. FUNCTION: Potential calcium-dependent cell-adhesion protein. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q99MN9 PCCB_MOUSE Propionyl-CoA carboxylase beta chain, mitochondrial (PCCase subunit beta) (EC 6.4.1.3) (Propanoyl-CoA:carbon dioxide ligase subunit beta) 541 58,409 Chain (1); Domain (2); Modified residue (8); Region (2); Sequence conflict (1); Transit peptide (1) Metabolic intermediate metabolism; propanoyl-CoA degradation; succinyl-CoA from propanoyl-CoA: step 1/3. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. SUBUNIT: Probably a dodecamer composed of six biotin-containing alpha subunits and six beta subunits. {ECO:0000250}. TISSUE SPECIFICITY: Broadly expressed. Most abundantly expressed in the kidney, liver, small intestine and stomach. {ECO:0000269|PubMed:11245989}. +Q6PEM8 PCFT_MOUSE Proton-coupled folate transporter (Heme carrier protein 1) (PCFT/HCP1) (Solute carrier family 46 member 1) 459 50,089 Chain (1); Erroneous gene model prediction (1); Erroneous initiation (1); Glycosylation (2); Modified residue (3); Sequence conflict (1); Topological domain (13); Transmembrane (12) TRANSMEM 25 48 Helical. {ECO:0000255}.; TRANSMEM 85 107 Helical. {ECO:0000255}.; TRANSMEM 114 137 Helical. {ECO:0000255}.; TRANSMEM 146 168 Helical. {ECO:0000255}.; TRANSMEM 181 203 Helical. {ECO:0000255}.; TRANSMEM 213 236 Helical. {ECO:0000255}.; TRANSMEM 266 288 Helical. {ECO:0000255}.; TRANSMEM 310 328 Helical. {ECO:0000255}.; TRANSMEM 332 356 Helical. {ECO:0000255}.; TRANSMEM 360 381 Helical. {ECO:0000255}.; TRANSMEM 394 412 Helical. {ECO:0000255}.; TRANSMEM 425 449 Helical. {ECO:0000255}. TOPO_DOM 1 24 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 49 84 Extracellular. {ECO:0000255}.; TOPO_DOM 108 113 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 138 145 Extracellular. {ECO:0000255}.; TOPO_DOM 169 180 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 204 212 Extracellular. {ECO:0000255}.; TOPO_DOM 237 265 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 289 309 Extracellular. {ECO:0000255}.; TOPO_DOM 329 331 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 357 359 Extracellular. {ECO:0000255}.; TOPO_DOM 382 393 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 413 424 Extracellular. {ECO:0000255}.; TOPO_DOM 450 459 Cytoplasmic. {ECO:0000255}. FUNCTION: Has been shown to act both as an intestinal proton-coupled high-affinity folate transporter and as an intestinal heme transporter which mediates heme uptake from the gut lumen into duodenal epithelial cells. The iron is then released from heme and may be transported into the bloodstream. Dietary heme iron is an important nutritional source of iron. Shows a higher affinity for folate than heme. {ECO:0000269|PubMed:16143108}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:16143108}; Multi-pass membrane protein {ECO:0000269|PubMed:16143108}. Cytoplasm {ECO:0000269|PubMed:16143108}. Note=Localizes to the apical membrane of intestinal cells in iron-deficient cells, while it resides in internal cellular compartments in iron-replete cells. SUBUNIT: Monomer. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in duodenum, especially in duodenal mucosa, the main site of intestinal heme absorption. Weakly expressed in the kidney. Not expressed in duodenum before weaning or in placenta. Weakly or not expressed in brain, heart, lung, skeletal muscle, testis and neonatal liver. {ECO:0000269|PubMed:16143108}. +Q99NA9 PCGF6_MOUSE Polycomb group RING finger protein 6 (Mel18 and Bmi1-like RING finger) (RING finger protein 134) 353 39,820 Chain (1); Coiled coil (1); Compositional bias (2); Cross-link (2); Modified residue (2); Zinc finger (1) FUNCTION: Transcriptional repressor. May modulate the levels of histone H3K4Me3 by activating KDM5D histone demethylase. Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. Within the PRC1-like complex, regulates RNF2 ubiquitin ligase activity. {ECO:0000250|UniProtKB:Q9BYE7}. PTM: Phosphorylated during mitosis. {ECO:0000250|UniProtKB:Q9BYE7}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BYE7}. SUBUNIT: Component of a PRC1-like complex. Interacts with BMI1/PCGF4, RING1 and RNF2. Interacts with KDM5D. Interacts with CBX4, CBX6, CBX7 and CBX8. {ECO:0000250|UniProtKB:Q9BYE7}. TISSUE SPECIFICITY: Expressed in ovary, testis, stomach, liver, thymus and kidney (at protein level). {ECO:0000269|PubMed:12167161}. +Q3UA06 PCH2_MOUSE Pachytene checkpoint protein 2 homolog (Thyroid hormone receptor interactor 13) (Thyroid receptor-interacting protein 13) (TR-interacting protein 13) (TRIP-13) 432 48,377 Alternative sequence (1); Chain (1); Modified residue (1); Nucleotide binding (1); Sequence conflict (3) FUNCTION: Plays a key role in chromosome recombination and chromosome structure development during meiosis. Required at early steps in meiotic recombination that leads to non-crossovers pathways. Also needed for efficient completion of homologous synapsis by influencing crossover distribution along the chromosomes affecting both crossovers and non-crossovers pathways. Also required for development of higher-order chromosome structures and is needed for synaptonemal-complex formation. In males, required for efficient synapsis of the sex chromosomes and for sex body formation. Promotes early steps of the DNA double-strand breaks (DSBs) repair process upstream of the assembly of RAD51 complexes. Required for depletion of HORMAD1 and HORMAD2 from synapsed chromosomes (PubMed:17696610, PubMed:19851446, PubMed:20711356). Plays a role in mitotic spindle assembly checkpoint (SAC) activation (By similarity). {ECO:0000250|UniProtKB:Q15645, ECO:0000269|PubMed:17696610, ECO:0000269|PubMed:19851446, ECO:0000269|PubMed:20711356}. SUBUNIT: Specifically interacts with the ligand binding domain of the thyroid receptor (TR). This interaction does not require the presence of thyroid hormone for its interaction (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed, including in testis. {ECO:0000269|PubMed:20711356}. +P59913 PCMD1_MOUSE Protein-L-isoaspartate O-methyltransferase domain-containing protein 1 357 40,693 Active site (1); Chain (1); Initiator methionine (1); Lipidation (1) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250|UniProtKB:Q96MG8}; Lipid-anchor {ECO:0000250|UniProtKB:Q96MG8}. +Q7TMR0 PCP_MOUSE Lysosomal Pro-X carboxypeptidase (EC 3.4.16.2) (Proline carboxypeptidase) (Prolylcarboxypeptidase) (PRCP) 491 55,027 Active site (3); Alternative sequence (1); Chain (1); Disulfide bond (4); Glycosylation (5); Propeptide (1); Region (1); Sequence conflict (4); Signal peptide (1) FUNCTION: Cleaves C-terminal amino acids linked to proline in peptides such as angiotensin II, III and des-Arg9-bradykinin. This cleavage occurs at acidic pH, but enzymatic activity is retained with some substrates at neutral pH (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Lysosome {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +Q8BXR6 PELI3_MOUSE E3 ubiquitin-protein ligase pellino homolog 3 (Pellino-3) (EC 2.3.2.27) (RING-type E3 ubiquitin transferase pellino homolog 3) 445 48,168 Chain (1); Modified residue (1); Sequence conflict (1) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins. Involved in the TLR and IL-1 signaling pathways via interaction with the complex containing IRAK kinases and TRAF6. Mediates 'Lys-63'-linked polyubiquitination of IRAK1. Can activate AP1/JUN and ELK1. Not required for NF-kappa-B activation. {ECO:0000250}. PTM: Phosphorylated by IRAK1 enhancing its E3 ligase activity. {ECO:0000250}. SUBUNIT: Interacts with TRAF6, IRAK1, MAP3K14 and MAP3K7. {ECO:0000250}. +Q9CQR7 PEN2_MOUSE Gamma-secretase subunit PEN-2 (Presenilin enhancer protein 2) 101 11,999 Chain (1); Intramembrane (1); Topological domain (3); Transmembrane (1) INTRAMEM 18 36 Helical. {ECO:0000250|UniProtKB:Q9NZ42}. TRANSMEM 58 78 Helical. {ECO:0000250|UniProtKB:Q9NZ42}. TOPO_DOM 1 17 Cytoplasmic. {ECO:0000250|UniProtKB:Q9NZ42}.; TOPO_DOM 37 57 Cytoplasmic. {ECO:0000250|UniProtKB:Q9NZ42}.; TOPO_DOM 79 101 Lumenal. {ECO:0000250|UniProtKB:Q9NZ42}. FUNCTION: Essential subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (amyloid-beta precursor protein) (PubMed:12522139, PubMed:24941111). The gamma-secretase complex plays a role in Notch and Wnt signaling cascades and regulation of downstream processes via its role in processing key regulatory proteins, and by regulating cytosolic CTNNB1 levels (Probable). PSENEN modulates both endoproteolysis of presenilin and gamma-secretase activity (PubMed:12522139, PubMed:24941111). {ECO:0000269|PubMed:12522139, ECO:0000269|PubMed:24941111, ECO:0000305}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12522139}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9NZ42}. Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:12522139}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9NZ42}. Cell membrane {ECO:0000250|UniProtKB:Q9NZ42}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9NZ42}. Membrane {ECO:0000250|UniProtKB:Q9NZ42}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9NZ42}. Note=Predominantly located in the endoplasmic reticulum and in the cis-Golgi. {ECO:0000269|PubMed:12522139}. SUBUNIT: The functional gamma-secretase complex is composed of at least four polypeptides: a presenilin homodimer (PSEN1 or PSEN2), nicastrin (NCSTN), APH1 (APH1A or APH1B) and PEN2. {ECO:0000269|PubMed:12522139, ECO:0000269|PubMed:24941111}. +P11247 PERM_MOUSE Myeloperoxidase (MPO) (EC 1.11.2.2) [Cleaved into: Myeloperoxidase light chain; Myeloperoxidase heavy chain] 718 81,182 Active site (1); Binding site (3); Chain (3); Disulfide bond (6); Glycosylation (6); Metal binding (6); Modified residue (1); Propeptide (1); Sequence conflict (10); Signal peptide (1); Site (1) FUNCTION: Part of the host defense system of polymorphonuclear leukocytes. It is responsible for microbicidal activity against a wide range of organisms. In the stimulated PMN, MPO catalyzes the production of hypohalous acids, primarily hypochlorous acid in physiologic situations, and other toxic intermediates that greatly enhance PMN microbicidal activity. {ECO:0000269|PubMed:11593004}. SUBCELLULAR LOCATION: Lysosome. SUBUNIT: Homodimer; disulfide-linked. Each monomer consists of a light and a heavy chain (By similarity). {ECO:0000250}. +Q3TC46 PATL1_MOUSE Protein PAT1 homolog 1 (PAT1-like protein 1) (Protein PAT1 homolog b) (Pat1b) 770 86,770 Chain (1); Compositional bias (1); Modified residue (11); Motif (1); Region (7); Sequence conflict (11) FUNCTION: RNA-binding protein involved in deadenylation-dependent decapping of mRNAs, leading to the degradation of mRNAs. Acts as a scaffold protein that connects deadenylation and decapping machinery. Required for cytoplasmic mRNA processing body (P-body) assembly (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000250}. Nucleus {ECO:0000250}. Nucleus, PML body {ECO:0000250}. Nucleus speckle {ECO:0000250}. Note=Predominantly cytoplasmic. Shuttles between the nucleus and the cytoplasm in a CRM1-dependent manner. Enriched in splicing specklesLocalization to nuclear foci and speckles requires active transcription. Excluded from the nucleolus (By similarity). {ECO:0000250}. SUBUNIT: Interacts (via region A) with DDX6/RCK. Interacts (via region H and region C) with LSM1 and LSM4. Interacts (via region N) with DCP1A, DCP2, EDC3, EDC4 and XRN1. Interacts with the CCR4-NOT complex. Interacts with the Lsm-containing SMN-Sm protein complex (By similarity). {ECO:0000250}. DOMAIN: The region C, also named Pat-C, is required for RNA-binding and mediates the binding with the Lsm-containing SMN-Sm protein complex and the decapping machinery. It folds into an alpha-alpha superhelix, exposing conserved and basic residues on one side of the domain. {ECO:0000250}. +Q8CAS9 PARP9_MOUSE Protein mono-ADP-ribosyltransferase PARP9 (EC 2.4.2.-) (ADP-ribosyltransferase diphtheria toxin-like 9) (ARTD9) (B aggressive lymphoma protein homolog) (Poly [ADP-ribose] polymerase 9) (PARP-9) 866 96,659 Alternative sequence (2); Chain (1); Domain (3); Modified residue (1) FUNCTION: ADP-ribosyltransferase which, in association with E3 ligase DTX3L, plays a role in DNA damage repair and in immune responses including interferon-mediated antiviral defenses (PubMed:27796300). Within the complex, enhances DTX3L E3 ligase activity which is further enhanced by PARP9 binding to poly(ADP-ribose) (By similarity). In addition, positively regulates DTXL3 protein levels (By similarity). In association with DTX3L and in presence of E1 and E2 enzymes, mediates NAD(+)-dependent mono-ADP-ribosylation of ubiquitin which prevents ubiquitin conjugation to substrates such as histones (By similarity). During DNA repair, PARP1 recruits PARP9/BAL1-DTX3L complex to DNA damage sites via PARP9 binding to ribosylated PARP1 (By similarity). Subsequent PARP1-dependent PARP9/BAL1-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage sites (By similarity). In response to DNA damage, PARP9-DTX3L complex is required for efficient non-homologous end joining (NHEJ) but the complex function is restrained by PARP9 activity (By similarity). Dispensable for B-cell receptor (BCR) assembly through V(D)J recombination and class switch recombination (CSR) (PubMed:28105679). In macrophages, positively regulates pro-inflammatory cytokines production in response to IFNG stimulation by suppressing PARP14-mediated STAT1 ADP-ribosylation and thus promoting STAT1 phosphorylation (PubMed:27796300). Also suppresses PARP14-mediated STAT6 ADP-ribosylation (By similarity). {ECO:0000250|UniProtKB:Q8IXQ6, ECO:0000269|PubMed:27796300, ECO:0000269|PubMed:28105679}. PTM: ADP-ribosylated by PARP14. {ECO:0000250|UniProtKB:Q8IXQ6}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8IXQ6}. Nucleus {ECO:0000250|UniProtKB:Q8IXQ6}. Note=Shuttles between the nucleus and the cytosol. Translocates to the nucleus in response to IFNG or IFNB1 stimulation. Export to the cytosol depends on the interaction with DTX3L. Localizes at sites of DNA damage in a PARP1-dependent manner. {ECO:0000250|UniProtKB:Q8IXQ6}. SUBUNIT: Forms a stable complex with E3 ligase DTX3L; the interaction is required for PARP9 mediated ADP-ribosylation of ubiquitin. Interacts (via PARP catalytic domain) with DTX3L (via N-terminus). Forms a complex with STAT1 and DTX3L independently of IFNB1 or IFNG-mediated STAT1 'Tyr-701' phosphorylation. Forms a complex with STAT1, DTX3L and histone H2B HIST1H2BH/H2BJ; the interaction is likely to induce HIST1H2BH/H2BJ ubiquitination. Interacts (via N-terminus) with STAT1. Interacts with PARP14 in IFNG-stimulated macrophages; the interaction prevents PARP14-mediated STAT1 and STAT6 ADP-riboslylation. Interacts with PARP1 (when poly-ADP-ribosylated). {ECO:0000250|UniProtKB:Q8IXQ6}. DOMAIN: Macro domains 1 and 2 may be involved in the binding to poly(ADP-ribose). Macro domain 2 is required for recruitment to DNA damage sites. Macro domains 1 and 2 are probably dispensable for the interaction with STAT1 and DTX3L and for STAT1 phosphorylation. {ECO:0000250|UniProtKB:Q8IXQ6}. TISSUE SPECIFICITY: Highly expressed in the thymus and intestine (PubMed:18069692). Expressed in macrophages (PubMed:27796300). {ECO:0000269|PubMed:18069692, ECO:0000269|PubMed:27796300}. +Q9JK83 PAR6B_MOUSE Partitioning defective 6 homolog beta (PAR-6 beta) (PAR-6B) 371 41,067 Alternative sequence (2); Beta strand (7); Chain (1); Domain (3); Helix (2); Modified residue (2); Mutagenesis (5); Region (1); Sequence conflict (3); Turn (1) FUNCTION: Adapter protein involved in asymmetrical cell division and cell polarization processes. Probably involved in formation of epithelial tight junctions. Association with PARD3 may prevent the interaction of PARD3 with F11R/JAM1, thereby preventing tight junction assembly. The PARD6-PARD3 complex links GTP-bound Rho small GTPases to atypical protein kinase C proteins. {ECO:0000269|PubMed:10934474, ECO:0000269|PubMed:11839275}. SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Cell junction, tight junction. Note=Colocalizes with active form of CDC42 or RAC1 at membrane ruffles. Also localizes to tight junctions. SUBUNIT: Interacts with PARD3. Interacts with GTP-bound forms of CDC42, ARHQ/TC10 and RAC1. Interacts with the N-terminal part of PRKCI and PRKCZ. Part of a complex with PARD3, CDC42 or RAC1 and PRKCI or PRKCZ. Part of a complex with LLGL1 and PRKCI. Interacts with ALS2CR19. Interacts with ECT2 (By similarity). Interacts with MPP5. {ECO:0000250, ECO:0000269|PubMed:10934474, ECO:0000269|PubMed:12545177, ECO:0000269|PubMed:12606577, ECO:0000269|PubMed:15140881}. DOMAIN: The pseudo-CRIB domain together with the PDZ domain is required for the interaction with Rho small GTPases. {ECO:0000269|PubMed:12545177}.; DOMAIN: The PDZ domain mediates the interaction with MPP5. {ECO:0000269|PubMed:12545177}. TISSUE SPECIFICITY: Expressed in pancreas and in both adult and fetal kidney. Weakly expressed in placenta and lung. Not expressed in other tissues. +Q9JK84 PAR6G_MOUSE Partitioning defective 6 homolog gamma (PAR-6 gamma) (PAR6A) 382 42,341 Chain (1); Domain (3); Region (1) FUNCTION: Adapter protein involved in asymmetrical cell division and cell polarization processes. May play a role in the formation of epithelial tight junctions. The PARD6-PARD3 complex links GTP-bound Rho small GTPases to atypical protein kinase C proteins (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Cell membrane {ECO:0000250}. Cell junction, tight junction {ECO:0000250}. SUBUNIT: Interacts with PARD3 (Probable). Interacts with GTP-bound forms of CDC42, ARHQ/TC10 and RAC1 (By similarity). Interacts with the N-terminal part of PRKCI and PRKCZ (By similarity). {ECO:0000250, ECO:0000305}. DOMAIN: The pseudo-CRIB domain together with the PDZ domain is required for the interaction with Rho small GTPases. {ECO:0000250}. +Q91ZQ1 PDE6C_MOUSE Cone cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha' (EC 3.1.4.35) (cGMP phosphodiesterase 6C) 861 98,785 Active site (1); Alternative sequence (1); Binding site (3); Chain (1); Domain (3); Lipidation (1); Metal binding (5); Modified residue (1); Nucleotide binding (1); Propeptide (1) FUNCTION: As cone-specific cGMP phosphodiesterase, it plays an essential role in light detection and cone phototransduction by rapidly decreasing intracellular levels of cGMP. {ECO:0000250|UniProtKB:P51160}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. SUBUNIT: Composed of two alpha' subunits that are associated with 3 smaller proteins of 11, 13, and 15 kDa. {ECO:0000250}. +Q9DAN1 PDILT_MOUSE Protein disulfide-isomerase-like protein of the testis 588 67,759 Chain (1); Domain (1); Erroneous initiation (1); Glycosylation (3); Motif (1); Signal peptide (1) FUNCTION: Probable redox-inactive chaperone involved in spermatogenesis. {ECO:0000250}. PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000255|PROSITE-ProRule:PRU10138}. SUBUNIT: Homodimer. The homodimer is not disulfide-linked. Interacts with CLGN and ERO1A (By similarity). {ECO:0000250}. DOMAIN: The thioredoxin domain lacks the conserved redox-active Cys at position 414 which is replaced by a Ser residue, suggesting that it lacks thioredoxin activity. TISSUE SPECIFICITY: Testis-specific (at protein level). {ECO:0000269|PubMed:15475357, ECO:0000269|PubMed:17507649}. +Q8BG81 PDIP3_MOUSE Polymerase delta-interacting protein 3 (S6K1 Aly/REF-like target) (SKAR) 420 46,132 Chain (1); Cross-link (5); Domain (1); Initiator methionine (1); Modified residue (10) FUNCTION: Is involved in regulation of translation. Is preferentially associated with CBC-bound spliced mRNA-protein complexes during the pioneer round of mRNA translation. Contributes to enhanced translational efficiency of spliced over nonspliced mRNAs. Recruits activated ribosomal protein S6 kinase beta-1 I/RPS6KB1 to newly synthesized mRNA. Involved in nuclear mRNA export; probably mediated by association with the TREX complex (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus speckle {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Nucleocytoplasmic shuttling protein. {ECO:0000250}. SUBUNIT: Interacts with POLD2. Interacts with NCBP1 and EIF4A3. Associates with the multiprotein exon junction complex (EJC). Interacts with RPS6KB1 (activated). Interacts with ERH. Interacts with THOC2, DDX39B and ZC3H11A; the interactions are ATP-dependent and indicative for an association with the TREX complex (By similarity). {ECO:0000250}. +P08003 PDIA4_MOUSE Protein disulfide-isomerase A4 (EC 5.3.4.1) (Endoplasmic reticulum resident protein 72) (ER protein 72) (ERp-72) (ERp72) 638 71,982 Beta strand (19); Chain (1); Compositional bias (1); Disulfide bond (3); Domain (3); Frameshift (1); Glycosylation (1); Helix (12); Modified residue (1); Motif (1); Sequence conflict (8); Signal peptide (1); Turn (7) SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:P13667}. Melanosome {ECO:0000250|UniProtKB:P13667}. SUBUNIT: Part of a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX. +Q921X9 PDIA5_MOUSE Protein disulfide-isomerase A5 (EC 5.3.4.1) (Protein disulfide isomerase-related protein) 517 59,267 Chain (1); Disulfide bond (4); Domain (3); Motif (1); Signal peptide (1) SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138}. SUBUNIT: Interacts with CALR (via P-domain). {ECO:0000250|UniProtKB:Q14554}. +O70209 PDLI3_MOUSE PDZ and LIM domain protein 3 (Actinin-associated LIM protein) (Alpha-actinin-2-associated LIM protein) 316 34,300 Beta strand (10); Chain (1); Domain (2); Helix (3); Modified residue (3); Turn (5) FUNCTION: May play a role in the organization of actin filament arrays within muscle cells. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250}. Note=Localizes to myofiber Z-lines. {ECO:0000250}. SUBUNIT: Interacts with ACTN2 (By similarity). Forms a heterodimer with PDLIM4 (via LIM domain) (PubMed:15663004). {ECO:0000250|UniProtKB:Q66HS7, ECO:0000269|PubMed:15663004}. +P70271 PDLI4_MOUSE PDZ and LIM domain protein 4 (LIM protein RIL) (Reversion-induced LIM protein) 330 35,556 Chain (1); Domain (2); Modified residue (7); Mutagenesis (21); Sequence conflict (3) FUNCTION: Suppresses SRC activation by recognizing and binding to active SRC and facilitating PTPN13-mediated dephosphorylation of SRC 'Tyr-419' leading to its inactivation. Inactivated SRC dissociates from this protein allowing the initiation of a new SRC inactivation cycle. Involved in reorganization of the actin cytoskeleton (By similarity). In nonmuscle cells, binds to ACTN1 (alpha-actinin-1), increases the affinity of ACTN1 to F-actin (filamentous actin), and promotes formation of actin stress fibers. Involved in regulation of the synaptic AMPA receptor transport in dendritic spines of hippocampal pyramidal neurons directing the receptors toward an insertion at the postsynaptic membrane. Links endosomal surface-internalized GRIA1-containing AMPA receptors to the alpha-actinin/actin cytoskeleton. Increases AMPA receptor-mediated excitatory postsynaptic currents in neurons (By similarity). {ECO:0000250|UniProtKB:P36202, ECO:0000250|UniProtKB:P50479}. PTM: Phosphorylated on tyrosine residue(s). Can be dephosphorylated by PTPN13. {ECO:0000269|PubMed:9487134}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P36202}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:P36202}. Early endosome membrane {ECO:0000250|UniProtKB:P36202}; Peripheral membrane protein {ECO:0000250|UniProtKB:P36202}; Cytoplasmic side {ECO:0000250|UniProtKB:P36202}. Recycling endosome membrane {ECO:0000250|UniProtKB:P36202}; Peripheral membrane protein {ECO:0000250|UniProtKB:P36202}; Cytoplasmic side {ECO:0000250|UniProtKB:P36202}. Nucleus {ECO:0000250|UniProtKB:P50479}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P50479}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:P50479}. Cell junction, synapse, synaptosome {ECO:0000250|UniProtKB:P36202}. Note=Localizes to actin stress fibers in nonmuscle cells. Colocalizes with GRIA1 in early endosomes. Enriched in numerous but not all spine-like structures along dendritic branches. Colocalizes with actin and enriched at sites containing larger amounts of actin and alpha-actinin. Targeted efficiently to spines via its PDZ domain-mediated interaction with the alpha-actinin/actin cytoskeletal complex. Localizes to synaptosomes in brain (By similarity). Colocalizes with F-actin. Colocalizes with TRIP6 at cell-cell contacts and lamellipodia. In the cytoplasm, displays a fibrillar pattern with characteristic thick fibers and occasional clusters. Colocalizes with the actin stress fibers. Oxidative stress induces redistribution from cytoskeleton to cytosol. Colocalizes with SRC at the perinuclear region, but not at focal adhesions (By similarity). {ECO:0000250|UniProtKB:P36202, ECO:0000250|UniProtKB:P50479}. SUBUNIT: Homodimer (By similarity). Interacts (via C-terminus only or via combined C-terminus and LIM domain, but not LIM domain only) with PTPN13 (via the second or fourth PDZ domains) (PubMed:9487134, PubMed:15663004). Found in a complex with PTPN13 and TRIP6 (PubMed:10826496). Interacts (via PDZ domain) with ACTN1 and ACTN2 (via C-terminal SDL residues) (By similarity). Interacts (via PDZ domain) with TRIP6 (via the second LIM domain or via the third LIM domain plus C-terminus) (PubMed:10826496). Interacts (via LIM domain) with GRIA1 (via C-terminus); this interaction as well as the interaction with alpha-actinin is required for their colocalization in early endosomes. Interacts with PDLIM1 (By similarity). Forms (via LIM domain) a heterodimer with PDLIM3 (PubMed:15663004). Interacts directly with SRC (via kinase domain and to a lesser extent the SH2 domain) (By similarity). {ECO:0000250|UniProtKB:P36202, ECO:0000250|UniProtKB:P50479, ECO:0000269|PubMed:10826496, ECO:0000269|PubMed:15663004, ECO:0000269|PubMed:9487134}. TISSUE SPECIFICITY: Expressed in several non-muscle tissues including lung, brain, ovary and uterus, and especially in epithelial cells on embryonic day 14 (E14). In the uterus, high expression in the glandular epithelium, but absent in the simple columnar epithelium lining the uterus cavity. {ECO:0000269|PubMed:14729062}. +Q8CI51 PDLI5_MOUSE PDZ and LIM domain protein 5 (Enigma homolog) (Enigma-like PDZ and LIM domains protein) 591 63,299 Alternative sequence (4); Beta strand (5); Chain (1); Cross-link (1); Domain (4); Helix (2); Initiator methionine (1); Modified residue (18); Sequence conflict (12); Turn (1) FUNCTION: May play an important role in the heart development by scaffolding PKC to the Z-disk region. Isoform 2 and isoform 3 may negatively modulate the scaffolding activity of isoform 1. May play a role in the regulation of cardiomyocyte expansion. Overexpression promotes the development of heart hypertrophy. Contributes to the regulation of dendritic spine morphogenesis in neurons. May restrain postsynaptic growth of excitatory synapses (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250}. Cell junction, synapse, synaptosome {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Detected both at presynaptic and postsynaptic sites. {ECO:0000250}. SUBUNIT: Interacts with various PKC isoforms through the LIM domains. Interacts (via LIM domains) with SIPA1L1. Interacts (via PDZ domain) with actin and ACTN1 (By similarity). {ECO:0000250}. +Q3TJD7 PDLI7_MOUSE PDZ and LIM domain protein 7 (LIM mineralization protein) (LMP) (Protein enigma) 457 50,119 Alternative sequence (5); Chain (1); Domain (4); Modified residue (5); Sequence conflict (2) FUNCTION: May function as a scaffold on which the coordinated assembly of proteins can occur. May play a role as an adapter that, via its PDZ domain, localizes LIM-binding proteins to actin filaments of both skeletal muscle and nonmuscle tissues. Involved in both of the two fundamental mechanisms of bone formation, direct bone formation (e.g. embryonic flat bones mandible and cranium), and endochondral bone formation (e.g. embryonic long bone development). Plays a role during fracture repair. Involved in BMP6 signaling pathway (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Colocalizes with RET to the cell periphery and in some cytoskeletal components. Colocalizes with TPM2 near the Z line in muscle. Colocalizes with TBX4 and TBX5 to actin filaments (By similarity). {ECO:0000250}. SUBUNIT: Specifically binds via its LIM zinc-binding 3 domain (LIM 3) domain to endocytic codes of INSR, but not with those of IGF1R, LDLR, TFRC, or EGFR. Interacts with various PKC isoforms through the LIM zinc-binding domains. Binds to RET in a phosphorylation-independent manner via its LIM zinc-binding domain 2 (LIM 2). Probably part of a complex with SHC and the RET dimer. Interacts with TPM2, TBX4 and TBX5 (By similarity). {ECO:0000250}. DOMAIN: The LIM zinc-binding 2 domain (LIM 2) interacts with TBX4. {ECO:0000250}.; DOMAIN: The LIM zinc-binding 3 domain (LIM 3) provides the structural basis for recognition of tyrosine-containing tight turn structures. This domain is necessary and sufficient for interaction with TBX5 (By similarity). {ECO:0000250}.; DOMAIN: Anchored to cell periphery via its N-terminal PDZ domain. {ECO:0000250}. +Q6A026 PDS5A_MOUSE Sister chromatid cohesion protein PDS5 homolog A 1332 150,327 Chain (1); Erroneous initiation (1); Modified residue (9); Repeat (1); Sequence conflict (1) FUNCTION: Probable regulator of sister chromatid cohesion in mitosis which may stabilize cohesin complex association with chromatin. May couple sister chromatid cohesion during mitosis to DNA replication. Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q29RF7}. Note=Associated with chromatin through most of the cell cycle. Dissociates from chromatin in late prophase, reassociates during late telophase (By similarity). {ECO:0000250|UniProtKB:Q29RF7}. SUBUNIT: Interacts with the cohesin complex. Interacts with WAPL (via FGF motifs) or CDCA5 (via the FGF motif); the interaction is direct, cohesin-dependent and competitive. Interacts with SMC3. Interacts with TP63 (By similarity). {ECO:0000250}. +P35375 PE2R1_MOUSE Prostaglandin E2 receptor EP1 subtype (PGE receptor EP1 subtype) (PGE2 receptor EP1 subtype) (Prostanoid EP1 receptor) 405 42,966 Chain (1); Disulfide bond (1); Glycosylation (3); Topological domain (8); Transmembrane (7) TRANSMEM 40 62 Helical; Name=1. {ECO:0000255}.; TRANSMEM 81 99 Helical; Name=2. {ECO:0000255}.; TRANSMEM 114 135 Helical; Name=3. {ECO:0000255}.; TRANSMEM 158 179 Helical; Name=4. {ECO:0000255}.; TRANSMEM 203 228 Helical; Name=5. {ECO:0000255}.; TRANSMEM 302 323 Helical; Name=6. {ECO:0000255}.; TRANSMEM 338 357 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 39 Extracellular. {ECO:0000255}.; TOPO_DOM 63 80 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 100 113 Extracellular. {ECO:0000255}.; TOPO_DOM 136 157 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 180 202 Extracellular. {ECO:0000255}.; TOPO_DOM 229 301 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 324 337 Extracellular. {ECO:0000255}.; TOPO_DOM 358 405 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for prostaglandin E2 (PGE2). The activity of this receptor is mediated by G(q) proteins which activate a phosphatidylinositol-calcium second messenger system. May play a role as an important modulator of renal function. Implicated the smooth muscle contractile response to PGE2 in various tissues. PTM: Phosphorylated. {ECO:0000305}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Abundant in kidney and in a lesser amount in lung. +Q9D9G2 PEBP4_MOUSE Phosphatidylethanolamine-binding protein 4 (PEBP-4) 242 26,908 Chain (1); Signal peptide (1) FUNCTION: Seems to promote cellular resistance to TNF-induced apoptosis by inhibiting activation of the Raf-1/MEK/ERK pathway, JNK and phosphatidylethanolamine externalization. {ECO:0000250}. SUBCELLULAR LOCATION: Lysosome {ECO:0000250}. +Q3URU2 PEG3_MOUSE Paternally-expressed gene 3 protein (ASF-1) 1571 178,932 Alternative sequence (3); Chain (1); Compositional bias (3); Erroneous initiation (1); Frameshift (2); Region (2); Repeat (13); Sequence conflict (29); Zinc finger (12) FUNCTION: Induces apoptosis in cooperation with SIAH1A. Acts as a mediator between p53/TP53 and BAX in a neuronal death pathway that is activated by DNA damage. Acts synergistically with TRAF2 and inhibits TNF induced apoptosis through activation of NF-kappa-B. Plays a role in regulating maternal behavior and offspring growth. {ECO:0000269|PubMed:10195900, ECO:0000269|PubMed:10681424, ECO:0000269|PubMed:11943780, ECO:0000269|PubMed:9500555}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. SUBUNIT: Homodimer. Interacts with SIAH1A and SIAH2. Interacts with TRAF2. {ECO:0000269|PubMed:10681424, ECO:0000269|PubMed:8806818, ECO:0000269|PubMed:9500555}. DOMAIN: The SCAN domain enables PEG3 homo- or heterodimerization to control gene expression in a combinatorial fashion. {ECO:0000250}. TISSUE SPECIFICITY: Brain, glial cells, neurons, skeletal muscle, uterus and placenta. In the placenta it found in all trophoblast cells. {ECO:0000269|PubMed:11260267, ECO:0000269|PubMed:11331620, ECO:0000269|PubMed:8563758, ECO:0000269|PubMed:8806818}. +P47857 PFKAM_MOUSE ATP-dependent 6-phosphofructokinase, muscle type (ATP-PFK) (PFK-M) (EC 2.7.1.11) (6-phosphofructokinase type A) (Phosphofructo-1-kinase isozyme A) (PFK-A) (Phosphohexokinase) 780 85,269 Active site (1); Alternative sequence (2); Binding site (9); Chain (1); Glycosylation (1); Initiator methionine (1); Metal binding (1); Modified residue (5); Nucleotide binding (2); Region (9); Sequence caution (1) Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. {ECO:0000255|HAMAP-Rule:MF_03184, ECO:0000269|PubMed:19889946}. PTM: GlcNAcylation decreases enzyme activity. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184}.; SUBCELLULAR LOCATION: Isoform 2: Cell projection, cilium, flagellum {ECO:0000269|PubMed:19889946}. Note=Principal piece region of the sperm flagellum. {ECO:0000269|PubMed:19889946}.; SUBCELLULAR LOCATION: Isoform 3: Cell projection, cilium, flagellum {ECO:0000269|PubMed:19889946}. Note=Principal piece region of the sperm flagellum. {ECO:0000269|PubMed:19889946}. SUBUNIT: Homo- and heterotetramers (By similarity). Phosphofructokinase (PFK) enzyme functions as a tetramer composed of different combinations of 3 types of subunits, called PFKM (M), PFKL (L) and PFKP (P). The composition of the PFK tetramer differs according to the tissue type it is present in. The kinetic and regulatory properties of the tetrameric enzyme are dependent on the subunit composition, hence can vary across tissues (Probable). Isoform 2 and isoform 3 interact (via N-terminal testis-specific region) with GSTM5. Isoform 2 and isoform 3 interact (via C-terminus) with HK1 (via N-terminal spermatogenic cell-specific region). {ECO:0000255|HAMAP-Rule:MF_03184, ECO:0000269|PubMed:19889946, ECO:0000305}. TISSUE SPECIFICITY: Isoform 1 is expressed in skeletal muscle (at protein level). Isoform 2 and isoform 3 are testis-specific and are detected in quiescent sperm (at protein level). They are first detected in the cytoplasm of round spermatids and subsequently in the flagellum of elongated spermatids extending into the seminiferous tubule lumen (at protein level). Isoform 2 is expressed at higher level than isoform 3 in testis. {ECO:0000269|PubMed:19889946}. +Q99P27 PG12B_MOUSE Group XIIB secretory phospholipase A2-like protein (Group XIII secretory phospholipase A2-like protein) (GXIII sPLA2-like) (sPLA2-GXIIB) (GXIIB) 195 21,736 Chain (1); Metal binding (4); Signal peptide (1) FUNCTION: Not known; does not seem to have catalytic activity. SUBCELLULAR LOCATION: Secreted. +Q9DBJ1 PGAM1_MOUSE Phosphoglycerate mutase 1 (EC 5.4.2.11) (EC 5.4.2.4) (BPG-dependent PGAM 1) (Phosphoglycerate mutase isozyme B) (PGAM-B) 254 28,832 Active site (2); Binding site (2); Chain (1); Compositional bias (1); Modified residue (10); Region (5); Sequence conflict (6); Site (1) FUNCTION: Interconversion of 3- and 2-phosphoglycerate with 2,3-bisphosphoglycerate as the primer of the reaction. Can also catalyze the reaction of EC 5.4.2.4 (synthase), but with a reduced activity. PTM: Acetylated at Lys-253, Lys-253 and Lys-254 under high glucose condition. Acetylation increases catalytic activity. Under glucose restriction SIRT1 levels dramatically increase and it deacetylates the enzyme (By similarity). {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P18669}. +Q05769 PGH2_MOUSE Prostaglandin G/H synthase 2 (EC 1.14.99.1) (Cyclooxygenase-2) (COX-2) (Glucocorticoid-regulated inflammatory cyclooxygenase) (Gripghs) (Macrophage activation-associated marker protein P71/73) (PES-2) (PHS II) (Prostaglandin H2 synthase 2) (PGH synthase 2) (PGHS-2) (Prostaglandin-endoperoxide synthase 2) (TIS10 protein) 604 69,013 Active site (2); Beta strand (21); Binding site (2); Chain (1); Disulfide bond (5); Domain (1); Glycosylation (4); Helix (32); Metal binding (1); Mutagenesis (2); Sequence conflict (4); Signal peptide (1); Site (2); Turn (6) Lipid metabolism; prostaglandin biosynthesis. FUNCTION: Converts arachidonate to prostaglandin H2 (PGH2), a committed step in prostanoid synthesis. Constitutively expressed in some tissues in physiological conditions, such as the endothelium, kidney and brain, and in pathological conditions, such as in cancer. PTGS2 is responsible for production of inflammatory prostaglandins. Up-regulation of PTGS2 is also associated with increased cell adhesion, phenotypic changes, resistance to apoptosis and tumor angiogenesis. In cancer cells, PTGS2 is a key step in the production of prostaglandin E2 (PGE2), which plays important roles in modulating motility, proliferation and resistance to apoptosis. {ECO:0000269|PubMed:12925531, ECO:0000269|PubMed:20463020, ECO:0000269|PubMed:20810665, ECO:0000269|PubMed:21489986, ECO:0000269|PubMed:22465430}. PTM: S-nitrosylation by NOS2 (iNOS) activates enzyme activity. S-nitrosylation may take place on different Cys residues in addition to Cys-526 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Microsome membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Peripheral membrane protein. SUBUNIT: Homodimer. {ECO:0000269|PubMed:10811226, ECO:0000269|PubMed:12925531, ECO:0000269|PubMed:20463020, ECO:0000269|PubMed:21467029, ECO:0000269|PubMed:21489986, ECO:0000269|PubMed:8967954}. TISSUE SPECIFICITY: Following colon injury, expressed in the wound bed mesenchyme during the first phase of repair, probably by colonic mesenchymal stem cells (at protein level). {ECO:0000269|PubMed:22465430}. +P09411 PGK1_MOUSE Phosphoglycerate kinase 1 (EC 2.7.2.3) 417 44,550 Beta strand (19); Binding site (6); Chain (1); Helix (20); Initiator methionine (1); Modified residue (22); Nucleotide binding (1); Region (2); Sequence conflict (3); Turn (3) Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5. FUNCTION: In addition to its role as a glycolytic enzyme, it seems that PGK-1 acts as a polymerase alpha cofactor protein (primer recognition protein). May play a role in sperm motility. {ECO:0000250|UniProtKB:P00558}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P00558}. TISSUE SPECIFICITY: Testis, lung, brain, skeletal muscle, liver, intestine, and kidney (at protein level). {ECO:0000269|PubMed:19759366}. +Q9D0F9 PGM1_MOUSE Phosphoglucomutase-1 (PGM 1) (EC 5.4.2.2) (Glucose phosphomutase 1) (Phosphoglucomutase-2) 562 61,418 Active site (1); Binding site (6); Chain (1); Metal binding (4); Modified residue (19); Region (3); Sequence conflict (1) FUNCTION: This enzyme participates in both the breakdown and synthesis of glucose. {ECO:0000250}. PTM: Phosphorylation at Thr-467 by PAK1 significantly enhances enzymatic activity. {ECO:0000250|UniProtKB:P36871}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. +Q8CAA7 PGM2L_MOUSE Glucose 1,6-bisphosphate synthase (EC 2.7.1.106) (Phosphoglucomutase-2-like 1) 621 70,279 Active site (1); Binding site (3); Chain (1); Metal binding (4); Modified residue (1); Region (3) FUNCTION: Glucose 1,6-bisphosphate synthase using 1,3-bisphosphoglycerate as a phosphate donor and a series of 1-phosphate sugars as acceptors, including glucose 1-phosphate, mannose 1-phosphate, ribose 1-phosphate and deoxyribose 1-phosphate. 5 or 6-phosphosugars are bad substrates, with the exception of glucose 6-phosphate. Also synthesizes ribose 1,5-bisphosphate. Has only low phosphopentomutase and phosphoglucomutase activities (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed at highest levels in the brain and testis, at intermediate levels in thymus, spleen, lung and skeletal muscle, and at lowest levels in kidney, liver and heart. {ECO:0000269|PubMed:17804405}. +Q6P6P7 PARP6_MOUSE Protein mono-ADP-ribosyltransferase PARP6 (EC 2.4.2.-) (ADP-ribosyltransferase diphtheria toxin-like 17) (ARTD17) (Poly [ADP-ribose] polymerase 6) (PARP-6) 630 71,176 Alternative sequence (3); Chain (1); Domain (1); Modified residue (2); Sequence conflict (1) FUNCTION: Mono-ADP-ribosyltransferase that mediates mono-ADP-ribosylation of target proteins. {ECO:0000250|UniProtKB:Q2NL67}. PTM: Auto-mono-ADP-ribosylated. {ECO:0000250|UniProtKB:Q2NL67}. +P63015 PAX6_MOUSE Paired box protein Pax-6 (Oculorhombin) 422 46,683 Alternative sequence (2); Chain (1); Compositional bias (2); DNA binding (1); Domain (1); Erroneous initiation (1); Natural variant (1); Sequence conflict (4) FUNCTION: Transcription factor with important functions in the development of the eye, nose, central nervous system and pancreas. Required for the differentiation of pancreatic islet alpha cells. Competes with PAX4 in binding to a common element in the glucagon, insulin and somatostatin promoters. Regulates specification of the ventral neuron subtypes by establishing the correct progenitor domains (By similarity). {ECO:0000250, ECO:0000269|PubMed:9163426}. PTM: Ubiquitinated by TRIM11, leading to ubiquitination and proteasomal degradation. Isoform 3 is sumoylated by SUMO1 at 'Lys-91'. {ECO:0000269|PubMed:18628401, ECO:0000269|PubMed:21084637}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with MAF and MAFB. Interacts with TRIM11; this interaction leads to ubiquitination and proteasomal degradation, as well as inhibition of transactivation, possibly in part by preventing PAX6 binding to consensus DNA sequences. {ECO:0000269|PubMed:17901057, ECO:0000269|PubMed:18628401}. TISSUE SPECIFICITY: Isoform 1 and isoform 3 are the major isoforms among different eye tissues. Isoform 1 and isoform 3 are expressed in the retina and cornea. In the lens epithelium, isoform 1 is relatively abundant, but isoform 3 is barely detectable. {ECO:0000269|PubMed:21084637}. DISEASE: Note=Defects in Pax6 are the cause of a condition known as small eye (Sey) which results in the complete lack of eyes and nasal primordia. {ECO:0000269|PubMed:1684639}. +Q8BHD8 PCMD2_MOUSE Protein-L-isoaspartate O-methyltransferase domain-containing protein 2 359 40,756 Active site (1); Chain (1); Compositional bias (1); Erroneous initiation (1); Initiator methionine (1); Lipidation (1); Sequence conflict (3) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +Q69Z38 PEAK1_MOUSE Inactive tyrosine-protein kinase PEAK1 (Pseudopodium-enriched atypical kinase 1) (Sugen kinase 269) (Tyrosine-protein kinase SgK269) 1735 191,097 Chain (1); Compositional bias (4); Domain (1); Modified residue (14); Region (2); Sequence conflict (5) FUNCTION: Probable catalytically inactive kinase. Scaffolding protein that regulates the cytoskeleton to control cell spreading and migration by modulating focal adhesion dynamics. Acts as a scaffold for mediating EGFR signaling. {ECO:0000250|UniProtKB:Q9H792}. PTM: Phosphorylated on tyrosine in a CSK-dependent manner in response to adhesion to fibronectin and to EGF stimulation (PubMed:20534451). Phosphorylation at Tyr-662 by a Src family kinase controls subcellular localization to focal adhesion and focal adhesion dynamics. Phosphorylation at Tyr-1177 is essential for binding to SHC1. {ECO:0000250|UniProtKB:Q9H792, ECO:0000269|PubMed:20534451}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:20534451}. Cell junction, focal adhesion {ECO:0000269|PubMed:20534451}. Note=Colocalizes with actin (PubMed:20534451). SUBUNIT: Homodimer (By similarity). Interacts with BCAR1 and CRK (By similarity). Interacts with PRAG1 (By similarity). Interacts (when phosphorylated at Tyr-1177) with SHC1 (via PID domain) (By similarity). Found in a complex with PPP1CA, PPP1CC and SHC1 (By similarity). {ECO:0000250|UniProtKB:Q9H792}. DOMAIN: The dimerization region encompasses helices both from the N- and C-terminal of the protein kinase domain. {ECO:0000250|UniProtKB:Q9H792}. +Q9DBD5 PELP1_MOUSE Proline-, glutamic acid- and leucine-rich protein 1 (Modulator of non-genomic activity of estrogen receptor) 1123 118,069 Chain (1); Compositional bias (4); Initiator methionine (1); Modified residue (8); Motif (11); Sequence conflict (3) FUNCTION: Coactivator of estrogen receptor-mediated transcription and a corepressor of other nuclear hormone receptors and sequence-specific transcription factors. Plays a role in estrogen receptor (ER) genomic activity when present in the nuclear compartment by activating the ER target genes in a hormonal stimulation dependent manner. Can facilitate ER non-genomic signaling via SRC and PI3K interaction in the cytosol. Plays a role in E2-mediated cell cycle progression by interacting with RB1. May have important functional implications in ER/growth factor cross-talk. Interacts with several growth factor signaling components including EGFR and HRS. Involved in nuclear receptor signaling via its interaction with AR and NR3C1. May promote tumorigenesis via its interaction with and modulation of several oncogenes including SRC, PI3K, STAT3 and EGFR. Plays a role in cancer cell metastasis via its ability to modulate E2-mediated cytoskeleton changes and cell migration via its interaction with SRC and PI3K (By similarity). Functions as the key stabilizing component of the Five Friends of Methylated CHTOP (5FMC) complex; the 5FMC complex is recruited to ZNF148 by methylated CHTOP, leading to desumoylation of ZNF148 and subsequent transactivation of ZNF148 target genes (PubMed:22872859). Component of the PELP1 complex involved in the nucleolar steps of 28S rRNA maturation and the subsequent nucleoplasmic transit of the pre-60S ribosomal subunit. Regulates pre-60S association of the critical remodeling factor MDN1 (By similarity). {ECO:0000250|UniProtKB:Q8IZL8, ECO:0000269|PubMed:22872859}. PTM: Transiently sumoylated, preferentially conjugated to SUMO2 or SUMO3. Sumoylation causes nucleolar exclusion of PELP1 and promotes the recruitment of MDN1 to pre-60S particles. Desumoylation by SUMO isopeptidase SENP3 is needed to release both PELP1 and MDN1 from pre-ribosomes. {ECO:0000250|UniProtKB:Q8IZL8}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q8IZL8}. Nucleus, nucleoplasm {ECO:0000269|PubMed:22872859}. Nucleus {ECO:0000269|PubMed:22872859}. Cytoplasm {ECO:0000269|PubMed:22872859}. Note=Mainly found in the nucleoplasm, with low levels detected in the cytoplasm. Also found associated with the plasma membrane. {ECO:0000269|PubMed:22872859}. SUBUNIT: Interacts with HRS, RXRA, SUMO2, HDAC2, RB1 and STAT3. Interacts with PI3K, SRC and EGFR in cytoplasm. Interacts with ESR1 and ESR2 and this interaction is enhanced by 17-beta-estradiol. Interacts with CREBBP, EP300, AR and NR3C1 in a ligand-dependent manner. Forms two complexes in the presence of 17-beta-estradiol; one with SRC and ESR1 and another with LCK and ESR1. Interacts with histone H1 and H3 with a greater affinity for H1. Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, KAT8/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10 (By similarity). Core component of the 5FMC complex, at least composed of PELP1, LAS1L, TEX10, WDR18 and SENP3; the complex interacts with methylated CHTOP and ZNF148. Interacts with NOL9 (PubMed:22872859). Interacts with BCAS3 (By similarity). Component of the PELP1 complex, composed of at least PELP1, TEX10 and WDR18. The complex interacts (via PELP1) with MDN1 (via its hexameric AAA ATPase ring) and the pre-60S ribosome particles (By similarity). {ECO:0000250|UniProtKB:Q8IZL8, ECO:0000269|PubMed:22872859}. DOMAIN: The Glu-rich region mediates histones interaction. {ECO:0000250}.; DOMAIN: The Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs are required for the association with nuclear receptor ESR1. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed with high levels in testis, ovary, uterus and pituitary gland. {ECO:0000269|PubMed:11481323}. +E9Q9W7 PDZD7_MOUSE PDZ domain-containing protein 7 1021 110,694 Alternative sequence (7); Chain (1); Domain (3) FUNCTION: In cochlear developing hair cells, essential in organizing the USH2 complex at stereocilia ankle links (PubMed:24334608). Blocks inhibition of adenylate cyclase activity mediated by ADGRV1 (PubMed:24962568). {ECO:0000269|PubMed:24334608, ECO:0000269|PubMed:24962568}. SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000250|UniProtKB:Q9H5P4}. Nucleus {ECO:0000250|UniProtKB:Q9H5P4}. Cell projection, stereocilium {ECO:0000269|PubMed:24334608, ECO:0000269|PubMed:27525485}. Note=Localizes at the ankle region of the stereocilia. {ECO:0000269|PubMed:24334608, ECO:0000269|PubMed:27525485}. SUBUNIT: Homodimerizes (via PDZ2 domain) (PubMed:25406310). Component of USH2 complex, composed of ADGRV1, PDZD7, USH2A and WHRN (PubMed:25406310). Interacts (via PDZ domains) with WHRN; the interaction is direct (PubMed:25406310). Interacts with USH1G (By similarity). Interacts with ADGRV1 (via the cytoplasmic region) (PubMed:24962568, PubMed:23055499). Interacts with USH2A (via the cytoplasmic region) (PubMed:23055499). Interacts with MYO7A (via MyTH4-FERM domains) (PubMed:27525485). {ECO:0000250|UniProtKB:Q9H5P4, ECO:0000269|PubMed:23055499, ECO:0000269|PubMed:24962568, ECO:0000269|PubMed:25406310, ECO:0000269|PubMed:27525485}. TISSUE SPECIFICITY: Isoform 1 is expressed in developing and adult cochlea but not retina (PubMed:24334608). Isoform 2 is expressed in developing and adult cochlea and retina (PubMed:24334608). Isoform 3 is expressed in adult cochlea and retina (PubMed:24334608). Isoform 4 is expressed in retina and developing cochlea but not adult cochlea (PubMed:24334608). Isoform 5 is expressed in adult cochlea but not in developing cochlea or retina (PubMed:24334608). {ECO:0000269|PubMed:24334608}. +B9EJ80 PDZD8_MOUSE PDZ domain-containing protein 8 1147 127,739 Chain (1); Coiled coil (1); Compositional bias (1); Domain (2); Modified residue (5); Sequence conflict (1); Transmembrane (1); Zinc finger (1) TRANSMEM 2 24 Helical. {ECO:0000255}. FUNCTION: Molecular tethering protein that connects endoplasmic reticulum and mitochondria membranes (PubMed:29097544). PDZD8-dependent endoplasmic reticulum-mitochondria membrane tethering is essential for endoplasmic reticulum-mitochondria Ca(2+) transfer (PubMed:29097544). In neurons, involved in the regulation of dendritic Ca(2+) dynamics by regulating mitochondrial Ca(2+) uptake in neurons (PubMed:29097544). {ECO:0000269|PubMed:29097544}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:29097544}; Single-pass membrane protein {ECO:0000255}. Note=Localizes at mitochondria-endoplasmic reticulum contact sites. {ECO:0000269|PubMed:29097544}. SUBUNIT: Interacts with MSN. {ECO:0000250|UniProtKB:Q8NEN9}. DOMAIN: The SMP-LTD domain is a barrel-like domain that binds phospholipids. {ECO:0000250|UniProtKB:A0FGR8}. +Q9WU28 PFD5_MOUSE Prefoldin subunit 5 (EIG-1) (Myc modulator 1) (c-Myc-binding protein Mm-1) 154 17,356 Chain (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (3) FUNCTION: Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins. Represses the transcriptional activity of MYC (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Heterohexamer of two PFD-alpha type and four PFD-beta type subunits. {ECO:0000250}. +P12382 PFKAL_MOUSE ATP-dependent 6-phosphofructokinase, liver type (ATP-PFK) (PFK-L) (EC 2.7.1.11) (6-phosphofructokinase type B) (Phosphofructo-1-kinase isozyme B) (PFK-B) (Phosphohexokinase) 780 85,360 Active site (1); Binding site (9); Chain (1); Glycosylation (1); Initiator methionine (1); Metal binding (1); Modified residue (4); Nucleotide binding (2); Region (9); Sequence conflict (1) Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis (By similarity). Negatively regulates the phagocyte oxidative burst in response to bacterial infection by controlling cellular NADPH biosynthesis and NADPH oxidase-derived reactive oxygen species. Upon macrophage activation, drives the metabolic switch toward glycolysis, thus preventing glucose turnover that produces NADPH via pentose phosphate pathway (PubMed:26194095). {ECO:0000255|HAMAP-Rule:MF_03184, ECO:0000269|PubMed:26194095}. PTM: GlcNAcylation at Ser-529 by OGT decreases enzyme activity, leading to redirect glucose flux through the oxidative pentose phosphate pathway. Glycosylation is stimulated by both hypoxia and glucose deprivation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184}. SUBUNIT: Homo- and heterotetramers (By similarity). Phosphofructokinase (PFK) enzyme functions as a tetramer composed of different combinations of 3 types of subunits, called PFKM (M), PFKL (L) and PFKP (P). The composition of the PFK tetramer differs according to the tissue type it is present in. The kinetic and regulatory properties of the tetrameric enzyme are dependent on the subunit composition, hence can vary across tissues (Probable). {ECO:0000255|HAMAP-Rule:MF_03184, ECO:0000305}. +Q61361 PGCB_MOUSE Brevican core protein 883 95,815 Chain (1); Disulfide bond (13); Domain (6); Glycosylation (2); Modified residue (2); Sequence conflict (5); Signal peptide (1) FUNCTION: May play a role in the terminally differentiating and the adult nervous system during postnatal development. Could stabilize interactions between hyaluronan (HA) and brain proteoglycans. PTM: Contains mostly chondroitin sulfate. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. SUBUNIT: Interacts with TNR. {ECO:0000250}. TISSUE SPECIFICITY: Brain. +Q3U1F9 PHAG1_MOUSE Phosphoprotein associated with glycosphingolipid-enriched microdomains 1 (Csk-binding protein) (Transmembrane phosphoprotein Cbp) 429 46,549 Chain (1); Lipidation (2); Modified residue (13); Mutagenesis (2); Region (2); Sequence conflict (3); Topological domain (2); Transmembrane (1) TRANSMEM 18 38 Helical; Signal-anchor for type III membrane protein. {ECO:0000255}. TOPO_DOM 1 17 Extracellular. {ECO:0000255}.; TOPO_DOM 39 429 Cytoplasmic. {ECO:0000255}. FUNCTION: Negatively regulates TCR (T-cell antigen receptor)-mediated signaling in T-cells and FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Promotes CSK activation and recruitment to lipid rafts, which results in LCK inhibition. Inhibits immunological synapse formation by preventing dynamic arrangement of lipid raft proteins. May be involved in cell adhesion signaling. {ECO:0000269|PubMed:12218089, ECO:0000269|PubMed:12612075, ECO:0000269|PubMed:14645715, ECO:0000269|PubMed:16166631}. PTM: Palmitoylated. {ECO:0000269|PubMed:12626544}.; PTM: Phosphorylated by FYN on Tyr-314 in resting T-cells; which promotes interaction with CSK. Dephosphorylated by PTPRC/CD45 upon TCR activation; which leads to CSK dissociation. May also be dephosphorylated by PTPN11. Hyperphosphorylated in mast cells upon FCER1 activation. {ECO:0000269|PubMed:11777944, ECO:0000269|PubMed:12218089, ECO:0000269|PubMed:12612075, ECO:0000269|PubMed:14645715, ECO:0000269|PubMed:14967142}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11777944, ECO:0000269|PubMed:12612075, ECO:0000269|PubMed:14645715, ECO:0000269|PubMed:16166631}; Single-pass type III membrane protein {ECO:0000269|PubMed:11777944, ECO:0000269|PubMed:12612075, ECO:0000269|PubMed:14645715, ECO:0000269|PubMed:16166631}. Note=Present in lipid rafts. SUBUNIT: When phosphorylated, interacts with CSK. Interacts with SLC9A3R1/EBP50. In resting T-cells, part of a PAG1-SLC9A3R1-MSN complex which is disrupted upon TCR activation. {ECO:0000269|PubMed:11777944, ECO:0000269|PubMed:12218089, ECO:0000269|PubMed:12612075, ECO:0000269|PubMed:14967142}. TISSUE SPECIFICITY: Present in T-cells (at protein level). {ECO:0000269|PubMed:16166631}. +Q501J7 PHAR4_MOUSE Phosphatase and actin regulator 4 (Protein Humpty dumpty) (Humdy) 694 76,632 Alternative sequence (2); Chain (1); Compositional bias (4); Erroneous gene model prediction (1); Erroneous initiation (1); Modified residue (18); Mutagenesis (1); Repeat (3); Sequence conflict (2) FUNCTION: Regulator of protein phosphatase 1 (PP1) required for neural tube and optic fissure closure, and enteric neural crest cell (ENCCs) migration during development. Acts as an activator of PP1 by interacting with PPP1CA and preventing phosphorylation of PPP1CA at 'Thr-320'. During neural tube closure, localizes to the ventral neural tube and activates PP1, leading to down-regulate cell proliferation within cranial neural tissue and the neural retina. Also acts as a regulator of migration of enteric neural crest cells (ENCCs) by activating PP1, leading to dephosphorylation and subsequent activation of cofilin (COF1 or COF2) and repression of the integrin signaling through the RHO/ROCK pathway. {ECO:0000269|PubMed:17609112, ECO:0000269|PubMed:22215812}. SUBCELLULAR LOCATION: Cytoplasm. Cell projection, lamellipodium. SUBUNIT: Binds PPP1CA and actin. +Q8BZ20 PAR12_MOUSE Protein mono-ADP-ribosyltransferase PARP12 (EC 2.4.2.-) (ADP-ribosyltransferase diphtheria toxin-like 12) (ARTD12) (Poly [ADP-ribose] polymerase 12) (PARP-12) (Zinc finger CCCH domain-containing protein 1) 711 79,917 Chain (1); Compositional bias (1); Domain (3); Modified residue (4); Sequence conflict (2); Zinc finger (5) FUNCTION: Mono-ADP-ribosyltransferase that mediates mono-ADP-ribosylation of target proteins. {ECO:0000250|UniProtKB:Q9H0J9}. PTM: Auto-mono-ADP-ribosylated. {ECO:0000250|UniProtKB:Q9H0J9}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +O88428 PAPS2_MOUSE Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 2 (PAPS synthase 2) (PAPSS 2) (Sulfurylase kinase 2) (SK 2) (SK2) [Includes: Sulfate adenylyltransferase (EC 2.7.7.4) (ATP-sulfurylase) (Sulfate adenylate transferase) (SAT); Adenylyl-sulfate kinase (EC 2.7.1.25) (3'-phosphoadenosine-5'-phosphosulfate synthase) (APS kinase) (Adenosine-5'-phosphosulfate 3'-phosphotransferase) (Adenylylsulfate 3'-phosphotransferase)] 621 70,351 Binding site (4); Chain (1); Natural variant (2); Nucleotide binding (3); Region (6); Sequence conflict (2) Sulfur metabolism; sulfate assimilation. FUNCTION: Bifunctional enzyme with both ATP sulfurylase and APS kinase activity, which mediates two steps in the sulfate activation pathway. The first step is the transfer of a sulfate group to ATP to yield adenosine 5'-phosphosulfate (APS), and the second step is the transfer of a phosphate group from ATP to APS yielding 3'-phosphoadenylylsulfate (PAPS: activated sulfate donor used by sulfotransferase). In mammals, PAPS is the sole source of sulfate; APS appears to be only an intermediate in the sulfate-activation pathway. May have a important role in skeletogenesis during postnatal growth. TISSUE SPECIFICITY: Expressed in liver, cartilage, skin and brain. DISEASE: Note=Defects in Papss2 are the cause of brachymorphism (bm), a autosomal recessive disease, which is characterized by abnormal hepatic detoxification, bleeding times and postnatal growth, such as dome-shaped skull, short thick tail, and shortened but not widened limbs. The abnormal postnatal growth has been attributed to undersulfation of cartilage proteoglycans. +Q7TMM8 PAR16_MOUSE Protein mono-ADP-ribosyltransferase PARP16 (EC 2.4.2.-) (ADP-ribosyltransferase diphtheria toxin-like 15) (Poly [ADP-ribose] polymerase 16) (PARP-16) 322 36,764 Binding site (3); Chain (1); Compositional bias (1); Domain (2); Sequence conflict (3); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 288 308 Helical. {ECO:0000255}. TOPO_DOM 1 287 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 309 322 Lumenal. {ECO:0000255}. FUNCTION: Intracellular mono-ADP-ribosyltransferase that may play a role in different processes through the mono-ADP-ribosylation of proteins involved in those processes. May play a role in the unfolded protein response (UPR), by ADP-ribosylating and activating EIF2AK3 and ERN1, two important UPR effectors. May also mediate mono-ADP-ribosylation of karyopherin KPNB1 a nuclear import factor. May not modify proteins on arginine or cysteine residues compared to other mono-ADP-ribosyltransferases. {ECO:0000250|UniProtKB:Q8N5Y8}. PTM: Auto-mono-ADP-ribosylated. {ECO:0000250|UniProtKB:Q8N5Y8}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8N5Y8}; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:Q8N5Y8}. SUBUNIT: Interacts with KPNB1. {ECO:0000250|UniProtKB:Q8N5Y8}. DOMAIN: The N-terminal PARP alpha-helical domain is regulatory, it packs against the catalytic domain, and may relay effector-binding event to the NAD-binding site. {ECO:0000250|UniProtKB:Q8N5Y8}. +Q9JJE4 PAQR4_MOUSE Progestin and adipoQ receptor family member 4 (Progestin and adipoQ receptor family member IV) 273 29,215 Chain (1); Transmembrane (5) TRANSMEM 52 72 Helical. {ECO:0000255}.; TRANSMEM 79 99 Helical. {ECO:0000255}.; TRANSMEM 115 135 Helical. {ECO:0000255}.; TRANSMEM 185 205 Helical. {ECO:0000255}.; TRANSMEM 245 265 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +P30558 PAR1_MOUSE Proteinase-activated receptor 1 (PAR-1) (Thrombin receptor) 430 47,790 Chain (1); Compositional bias (2); Disulfide bond (1); Glycosylation (3); Modified residue (1); Propeptide (1); Sequence conflict (5); Signal peptide (1); Site (1); Topological domain (8); Transmembrane (7) TRANSMEM 108 133 Helical; Name=1. {ECO:0000255}.; TRANSMEM 143 162 Helical; Name=2. {ECO:0000255}.; TRANSMEM 182 203 Helical; Name=3. {ECO:0000255}.; TRANSMEM 224 244 Helical; Name=4. {ECO:0000255}.; TRANSMEM 274 293 Helical; Name=5. {ECO:0000255}.; TRANSMEM 317 339 Helical; Name=6. {ECO:0000255}.; TRANSMEM 355 379 Helical; Name=7. {ECO:0000255}. TOPO_DOM 42 107 Extracellular. {ECO:0000255}.; TOPO_DOM 134 142 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 163 181 Extracellular. {ECO:0000255}.; TOPO_DOM 204 223 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 245 273 Extracellular. {ECO:0000255}.; TOPO_DOM 294 316 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 340 354 Extracellular. {ECO:0000255}.; TOPO_DOM 380 430 Cytoplasmic. {ECO:0000255}. FUNCTION: High affinity receptor for activated thrombin coupled to G proteins that stimulate phosphoinositide hydrolysis. PTM: A proteolytic cleavage generates a new N-terminus that functions as a tethered ligand.; PTM: Phosphorylated in the C-terminal tail; probably mediating desensitization prior to the uncoupling and internalization of the receptor. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. DOMAIN: The cleaved signal peptide may not be degraded and may function as an intracellular angiogenesis inhibitor peptide known as parstatin. {ECO:0000250}. +Q6TCG5 PAQR6_MOUSE Membrane progestin receptor delta (mPR delta) (Membrane progesterone P4 receptor delta) (Membrane progesterone receptor delta) (Progesterone and adipoQ receptor family member 6) (Progestin and adipoQ receptor family member 6) (Progestin and adipoQ receptor family member VI) 343 38,176 Chain (1); Topological domain (8); Transmembrane (7) TRANSMEM 50 70 Helical. {ECO:0000255}.; TRANSMEM 80 100 Helical. {ECO:0000255}.; TRANSMEM 113 133 Helical. {ECO:0000255}.; TRANSMEM 147 167 Helical. {ECO:0000255}.; TRANSMEM 217 237 Helical. {ECO:0000255}.; TRANSMEM 258 278 Helical. {ECO:0000255}.; TRANSMEM 292 312 Helical. {ECO:0000255}. TOPO_DOM 1 49 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 71 79 Extracellular. {ECO:0000255}.; TOPO_DOM 101 112 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 134 146 Extracellular. {ECO:0000255}.; TOPO_DOM 168 216 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 238 257 Extracellular. {ECO:0000255}.; TOPO_DOM 279 291 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 313 343 Extracellular. {ECO:0000255}. FUNCTION: Plasma membrane progesterone (P4) receptor coupled to G proteins. Seems to act through a G(s) mediated pathway. Involved in neurosteroid inhibition of apoptosis. May be involved in regulating rapid P4 signaling in the nervous system. Also binds dehydroepiandrosterone (DHEA), pregnanolone, pregnenolone and allopregnanolone. {ECO:0000250|UniProtKB:Q6TCH4}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6TCH4}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q6TCH4}. +Q6TCG2 PAQR9_MOUSE Membrane progesterone receptor epsilon (mPR epsilon) (Membrane progesterone P4 receptor epsilon) (Membrane progestin receptor epsilon) (Progesterone and adipoQ receptor family member 9) (Progestin and adipoQ receptor family member 9) (Progestin and adipoQ receptor family member IX) 375 42,741 Chain (1); Sequence conflict (1); Topological domain (8); Transmembrane (7) TRANSMEM 85 105 Helical. {ECO:0000255}.; TRANSMEM 115 135 Helical. {ECO:0000255}.; TRANSMEM 161 181 Helical. {ECO:0000255}.; TRANSMEM 204 224 Helical. {ECO:0000255}.; TRANSMEM 242 262 Helical. {ECO:0000255}.; TRANSMEM 300 320 Helical. {ECO:0000255}.; TRANSMEM 342 362 Helical. {ECO:0000255}. TOPO_DOM 1 84 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 106 114 Extracellular. {ECO:0000255}.; TOPO_DOM 136 160 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 182 203 Extracellular. {ECO:0000255}.; TOPO_DOM 225 241 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 263 299 Extracellular. {ECO:0000255}.; TOPO_DOM 321 341 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 363 375 Extracellular. {ECO:0000255}. FUNCTION: Plasma membrane progesterone (P4) receptor coupled to G proteins. Seems to act through a G(s) mediated pathway. May be involved in regulating rapid P4 signaling in the nervous system. Also binds dehydroepiandrosterone (DHEA), pregnanolone, pregnenolone and allopregnanolone. {ECO:0000250|UniProtKB:Q6ZVX9}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6ZVX9}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q6ZVX9}. +Q9CSB4 PAR3L_MOUSE Partitioning defective 3 homolog B (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 19 protein homolog) (PAR3-beta) (Partitioning defective 3-like protein) (PAR3-L protein) 1203 132,780 Alternative sequence (1); Beta strand (9); Chain (1); Compositional bias (1); Domain (3); Helix (2); Modified residue (14); Turn (2) FUNCTION: Putative adapter protein involved in asymmetrical cell division and cell polarization processes. May play a role in the formation of epithelial tight junctions (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}. Cell junction {ECO:0000250}. Cell junction, tight junction {ECO:0000250}. Note=Partially localized along the cell-cell contact region. Colocalizes with TJP1 to epithelial tight junctions (By similarity). {ECO:0000250}. SUBUNIT: Interacts with PARD6B. Interacts with INSC/inscuteable (By similarity). {ECO:0000250}. +O08675 PAR3_MOUSE Proteinase-activated receptor 3 (PAR-3) (Coagulation factor II receptor-like 2) (Thrombin receptor-like 2) 369 41,697 Chain (1); Disulfide bond (1); Glycosylation (2); Helix (1); Propeptide (1); Sequence conflict (8); Signal peptide (1); Site (1); Topological domain (8); Transmembrane (7) TRANSMEM 94 119 Helical; Name=1. {ECO:0000255}.; TRANSMEM 128 147 Helical; Name=2. {ECO:0000255}.; TRANSMEM 167 188 Helical; Name=3. {ECO:0000255}.; TRANSMEM 206 229 Helical; Name=4. {ECO:0000255}.; TRANSMEM 260 279 Helical; Name=5. {ECO:0000255}.; TRANSMEM 297 321 Helical; Name=6. {ECO:0000255}.; TRANSMEM 336 360 Helical; Name=7. {ECO:0000255}. TOPO_DOM 38 93 Extracellular. {ECO:0000255}.; TOPO_DOM 120 127 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 148 166 Extracellular. {ECO:0000255}.; TOPO_DOM 189 205 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 230 259 Extracellular. {ECO:0000255}.; TOPO_DOM 280 296 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 322 335 Extracellular. {ECO:0000255}.; TOPO_DOM 361 369 Cytoplasmic. {ECO:0000255}. FUNCTION: High affinity receptor for activated thrombin coupled to G proteins that stimulate phosphoinositide hydrolysis. May play a role in platelets activation. PTM: A proteolytic cleavage generates a new N-terminus that functions as a tethered ligand. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBUNIT: Interacts with INSC/inscuteable and GPSM2. {ECO:0000269|PubMed:16094321}. +Q9Z101 PAR6A_MOUSE Partitioning defective 6 homolog alpha (PAR-6) (PAR-6 alpha) (PAR-6A) 346 37,333 Alternative sequence (2); Chain (1); Domain (3); Frameshift (1); Modified residue (2); Region (2); Sequence conflict (1) FUNCTION: Adapter protein involved in asymmetrical cell division and cell polarization processes. Probably involved in the formation of epithelial tight junctions. Association with PARD3 may prevent the interaction of PARD3 with F11R/JAM1, thereby preventing tight junction assembly. The PARD6-PARD3 complex links GTP-bound Rho small GTPases to atypical protein kinase C proteins (PubMed:15761148). Regulates centrosome organization and function. Essential for the centrosomal recruitment of key proteins that control centrosomal microtubule organization (By similarity). {ECO:0000250|UniProtKB:Q9NPB6, ECO:0000269|PubMed:15761148}. PTM: Phosphorylated by the TGF-beta receptor. {ECO:0000269|PubMed:15761148}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Cell junction, tight junction {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000250|UniProtKB:Q9NPB6}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9NPB6}. Note=Colocalizes with GTP-bound CDC42 or RAC1 at membrane ruffles and with PARD3 at epithelial tight junctions. Recruited to the centrosome by a microtubule and dynein-dynactin-dependent mechanism. {ECO:0000250|UniProtKB:Q9NPB6}. SUBUNIT: Interacts with ECT2 ('Thr-359' phosphorylated form) and PRKCI. Interacts with MPP5 and CRB3 (By similarity). Interacts with PARD3. Interacts with GTP-bound forms of CDC42, ARHQ/TC10 and RAC1. Interacts with the N-terminal part of PRKCI and PRKCZ. Part of a complex with PARD3, CDC42 or RAC1 and PRKCI or PRKCZ. Part of a complex with LLGL1 and PRKCI. Interacts with MAP2K5. Interacts with TGFBR1; involved in TGF-beta induced epithelial to mesenchymal transition. Interacts with DCTN1 and PCM1 (By similarity). {ECO:0000250|UniProtKB:Q9NPB6, ECO:0000269|PubMed:10934475, ECO:0000269|PubMed:12629547, ECO:0000269|PubMed:12813044, ECO:0000269|PubMed:15761148}. DOMAIN: The PB1 domain mediates interactions with MAP2K5. {ECO:0000269|PubMed:12813044}.; DOMAIN: The pseudo-CRIB domain together with the PDZ domain is required for the interaction with Rho small GTPases. {ECO:0000250}.; DOMAIN: The PDZ domain mediates the interaction with CRB3. {ECO:0000250}. +Q9ES46 PARVB_MOUSE Beta-parvin 365 41,669 Chain (1); Domain (2); Modified residue (1) FUNCTION: Adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases CDC42 and RAC1 by guanine exchange factors, such as ARHGEF6. Is involved in the reorganization of the actin cytoskeleton and formation of lamellipodia. Plays a role in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration (By similarity). {ECO:0000250}. PTM: Phosphorylated by ILK. {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, focal adhesion. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Cytoplasm, myofibril, sarcomere {ECO:0000250}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250}. Note=Constituent of focal adhesions. Detected at the tips of the leading edge of cells. Colocalizes with F-actin at the tips of lamellipodia (By similarity). {ECO:0000250}. SUBUNIT: Interacts with ILK, ARHGEF6, PXN (via LD motifs), ACTN2 and actin (By similarity). Interacts with DYSF. {ECO:0000250, ECO:0000269|PubMed:15835269}. TISSUE SPECIFICITY: Expressed predominantly in heart and moderately in spleen, lung and skeletal muscle. {ECO:0000269|PubMed:11722847}. +Q3TVI8 PBIP1_MOUSE Pre-B-cell leukemia transcription factor-interacting protein 1 (Hematopoietic PBX-interacting protein) 727 81,164 Chain (1); Coiled coil (2); Compositional bias (1); Modified residue (7); Motif (2); Sequence conflict (5) FUNCTION: Regulator of pre-B-cell leukemia transcription factors (BPXs) function. Inhibits the binding of PBX1-HOX complex to DNA and blocks the transcriptional activity of E2A-PBX1. Tethers estrogen receptor-alpha (ESR1) to microtubules and allows them to influence estrogen receptors-alpha signaling (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q96AQ6}. Nucleus {ECO:0000250|UniProtKB:Q96AQ6}. Note=Shuttles between the nucleus and the cytosol. Mainly localized in the cytoplasm, associated with microtubules. Detected in small amounts in the nucleus. {ECO:0000250|UniProtKB:Q96AQ6}. SUBUNIT: Interacts with ESR1, PBX1, PBX2 and PBX3 (By similarity). Interacts with TEX11. {ECO:0000250, ECO:0000269|PubMed:22383461}. DOMAIN: The C-terminal domain (AA 443-731) contains a nuclear export signal. {ECO:0000250}.; DOMAIN: Association to the cytoskeleton through a N-terminal leucine rich-domain (AA 190-218). {ECO:0000250}. +P60335 PCBP1_MOUSE Poly(rC)-binding protein 1 (Alpha-CP1) (Heterogeneous nuclear ribonucleoprotein E1) (hnRNP E1) 356 37,498 Chain (1); Cross-link (1); Domain (3); Modified residue (7) FUNCTION: Single-stranded nucleic acid binding protein that binds preferentially to oligo dC. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +P59114 PCIF1_MOUSE Phosphorylated CTD-interacting factor 1 706 80,504 Chain (1); Compositional bias (1); Domain (1); Modified residue (3); Motif (2) FUNCTION: May play a role in transcription elongation or in coupling transcription to pre-mRNA processing through its association with the phosphorylated C-terminal domain (CTD) of RNAPII largest subunit. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with the phosphorylated C-terminal domain (CTD) of RNAPII largest subunit. {ECO:0000250}. DOMAIN: The WW domain is sufficient for direct and specific interaction with the phosphorylated CTD of RNAPII largest subunit. {ECO:0000250}. +Q8R023 PCGF1_MOUSE Polycomb group RING finger protein 1 (Nervous system Polycomb-1) (NSPc1) (RING finger protein 68) 259 30,318 Chain (1); Cross-link (2); Erroneous initiation (1); Initiator methionine (1); Modified residue (2); Region (2); Zinc finger (1) FUNCTION: Component of the Polycomb group (PcG) multiprotein BCOR complex, a complex required to maintain the transcriptionally repressive state of some genes, such as BCL6 and the cyclin-dependent kinase inhibitor, CDKN1A. Transcriptional repressor that may be targeted to the DNA by BCL6; this transcription repressor activity may be related to PKC signaling pathway. Represses CDKN1A expression by binding to its promoter, and this repression is dependent on the retinoic acid response element (RARE element). Promotes cell cycle progression and enhances cell proliferation as well. May have a positive role in tumor cell growth by down-regulating CDKN1A. Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. Within the PRC1-like complex, regulates RNF2 ubiquitin ligase activity. Regulates the expression of DPPA4 and NANOG in the NT2 embryonic carcinoma cells. {ECO:0000250|UniProtKB:Q9BSM1}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BSM1}. SUBUNIT: Component of the repressive BCOR complex containing a Polycomb group subcomplex at least composed of RYBP, RING1 and RNF2/RING2. Specifically interacts with BCOR, RING1 and RNF2/RING2. Also interacts with BCORL1, the interaction is direct. Component of a PRC1-like complex. Interacts with CBX6, CBX7 and CBX8. Interacts with DPPA4, NANOG, POU5F1 and RYBP. {ECO:0000250|UniProtKB:Q9BSM1}. +Q9QYX7 PCLO_MOUSE Protein piccolo (Aczonin) (Brain-derived HLMN protein) (Multidomain presynaptic cytomatrix protein) 5068 550,834 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (3); Glycosylation (2); Modified residue (66); Region (1); Sequence caution (4); Sequence conflict (35); Zinc finger (2) FUNCTION: May act as a scaffolding protein involved in the organization of synaptic active zones and in synaptic vesicle trafficking. {ECO:0000303|PubMed:10508862}. SUBCELLULAR LOCATION: Cell junction, synapse {ECO:0000269|PubMed:10508862}. Note=Concentrated at the presynaptic side of synaptic junctions. SUBUNIT: Interacts with RABAC1/PRA1, RIMS2 and profilin. {ECO:0000269|PubMed:10508862, ECO:0000269|PubMed:12401793}. DOMAIN: C2 domain 1 is involved in binding calcium and phospholipids. Calcium binds with low affinity but with high specificity and induces a large conformational change. {ECO:0000250|UniProtKB:Q9JKS6}. TISSUE SPECIFICITY: Highly expressed in brain. Moderately expressed in pituitary gland and pancreatic islets. Low levels found in stomach. {ECO:0000269|PubMed:10508862, ECO:0000269|PubMed:12401793}. +Q9R0L6 PCM1_MOUSE Pericentriolar material 1 protein (PCM-1) (mPCM-1) 2025 228,847 Alternative sequence (1); Chain (1); Coiled coil (7); Initiator methionine (1); Modified residue (44); Sequence conflict (7) FUNCTION: Required for centrosome assembly and function (PubMed:12112146). Essential for the correct localization of several centrosomal proteins including CEP250, CETN3, PCNT and NEK2 (By similarity). Required to anchor microtubules to the centrosome (By similarity). Involved in the biogenesis of cilia (By similarity). {ECO:0000250|UniProtKB:Q15154, ECO:0000269|PubMed:12112146}. PTM: Ubiquitinated. Undergoes monoubiquitination catalyzed by the E3 ubiquitin-protein ligase MIB1 in proliferating cells, preventing cilia formation. Monoubiquitination by MIB1 is inhibited in response to cellular stress, such as ultraviolet light (UV) radiation or heat shock, resulting in cilia formation initiation. {ECO:0000250|UniProtKB:Q15154}.; PTM: Phosphorylated on multiple serine and threonine residues by DYRK3 during the G2-to-M transition, after the nuclear-envelope breakdown. Phosphorylation by DYRK3 promotes disassembly of pericentriolar material. {ECO:0000250|UniProtKB:Q15154}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:10579718, ECO:0000269|PubMed:12112146, ECO:0000269|PubMed:12403812}. Cytoplasmic granule {ECO:0000269|PubMed:12403812, ECO:0000269|PubMed:12571289}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000269|PubMed:10579718, ECO:0000269|PubMed:12403812, ECO:0000269|PubMed:12571289}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q15154}. Note=Recruitment to the centrosome requires microtubules and dynein. Displaced from centriolar satellites and centrosome in response to cellular stress, such as ultraviolet light (UV) radiation or heat shock, in a process that requires p38 MAP kinase signaling (By similarity). The majority of the protein dissociates from the centrosome during metaphase and subsequently localizes to the cleavage site in telophase. {ECO:0000250|UniProtKB:Q15154}. SUBUNIT: Self-associates. Interacts with BBS4, BBS8, CETN3, HAP1, NDE1, NDEL1, MAP1LC3B, GABARAPAL2, and GABARAP. Interacts with CEP131; the interaction increases in response to ultraviolet light (UV) radiation. Associates with microtubule; association to microtubule is reduced in response to cellular stress, such as ultraviolet light (UV) radiation or heat shock, in a process that requires p38 MAP kinase signaling (By similarity). Interacts with C2CD3 (PubMed:24469809). Interacts with CCDC113 (By similarity). Interacts with SSX2IP (PubMed:24356449). Interacts with CCDC13 (By similarity). Interacts with CEP290 (PubMed:17705300). Interacts with PARD6A (By similarity). Interacts with KIAA0753/OFIP, FOPNL/FOR20 and OFD1; the interaction with FOPNL/FOR20 and OFD1 may be mediated by KIAA0753/OFIP (PubMed:26643951). Interacts with CCDC66 (By similarity). {ECO:0000250|UniProtKB:Q15154, ECO:0000269|PubMed:17705300, ECO:0000269|PubMed:24356449, ECO:0000269|PubMed:24469809, ECO:0000269|PubMed:26643951}. TISSUE SPECIFICITY: Expressed in the hippocampus and dentate gyrus, the columnar epithelial cells of bronchioles, the olfactory epithelium, the pericardium and the inner segment of the retina. {ECO:0000269|PubMed:15107855}. +Q8BH04 PCKGM_MOUSE Phosphoenolpyruvate carboxykinase [GTP], mitochondrial (PEPCK-M) (EC 4.1.1.32) 640 70,528 Active site (1); Binding site (4); Chain (1); Erroneous initiation (1); Metal binding (3); Modified residue (5); Nucleotide binding (2); Region (2); Sequence conflict (2); Transit peptide (1) Carbohydrate biosynthesis; gluconeogenesis. FUNCTION: Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. SUBUNIT: Monomer. +Q8K183 PDXK_MOUSE Pyridoxal kinase (EC 2.7.1.35) (Pyridoxine kinase) 312 35,015 Binding site (4); Chain (1); Modified residue (5); Nucleotide binding (2); Sequence conflict (1) FUNCTION: Required for synthesis of pyridoxal-5-phosphate from vitamin B6. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +O35417 PDYN_MOUSE Proenkephalin-B (Beta-neoendorphin-dynorphin) (Preprodynorphin) [Cleaved into: Alpha-neoendorphin; Beta-neoendorphin; Big dynorphin (Big Dyn); Dynorphin A(1-17) (Dyn-A17) (Dynorphin A); Dynorphin A(1-13); Dynorphin A(1-8); Leu-enkephalin; Rimorphin (Dynorphin B) (Dyn-B) (Dynorphin B(1-13)); Leumorphin (Dynorphin B-29)] 248 28,055 Peptide (11); Propeptide (2); Signal peptide (1) FUNCTION: Leu-enkephalins compete with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress (By similarity). {ECO:0000250}.; FUNCTION: Dynorphin peptides differentially regulate the kappa opioid receptor. Dynorphin A(1-13) has a typical opiod activity, it is 700 times more potent than Leu-enkephalin (By similarity). {ECO:0000250}.; FUNCTION: Leumorphin has a typical opiod activity and may have anti-apoptotic effect. {ECO:0000250}. PTM: The N-terminal domain contains 6 conserved cysteines thought to be involved in disulfide bonding and/or processing. SUBCELLULAR LOCATION: Secreted. +P43117 PF2R_MOUSE Prostaglandin F2-alpha receptor (PGF receptor) (PGF2-alpha receptor) (Prostanoid FP receptor) 366 40,700 Chain (1); Disulfide bond (1); Glycosylation (2); Topological domain (8); Transmembrane (7) TRANSMEM 32 55 Helical; Name=1. {ECO:0000255}.; TRANSMEM 70 90 Helical; Name=2. {ECO:0000255}.; TRANSMEM 110 131 Helical; Name=3. {ECO:0000255}.; TRANSMEM 153 175 Helical; Name=4. {ECO:0000255}.; TRANSMEM 199 224 Helical; Name=5. {ECO:0000255}.; TRANSMEM 251 267 Helical; Name=6. {ECO:0000255}.; TRANSMEM 286 307 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 31 Extracellular. {ECO:0000255}.; TOPO_DOM 56 69 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 91 109 Extracellular. {ECO:0000255}.; TOPO_DOM 132 152 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 176 198 Extracellular. {ECO:0000255}.; TOPO_DOM 225 250 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 268 285 Extracellular. {ECO:0000255}.; TOPO_DOM 308 366 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for prostaglandin F2-alpha (PGF2-alpha). The activity of this receptor is mediated by G proteins which activate a phosphatidylinositol-calcium second messenger system. Initiates luteolysis in the corpus luteum (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q8BX10 PGAM5_MOUSE Serine/threonine-protein phosphatase PGAM5, mitochondrial (EC 3.1.3.16) (Phosphoglycerate mutase family member 5) 288 31,994 Alternative sequence (1); Chain (1); Frameshift (1); Modified residue (5); Region (1); Sequence conflict (3); Transmembrane (1) TRANSMEM 7 29 Helical. {ECO:0000255}. FUNCTION: Displays phosphatase activity for serine/threonine residues, and, dephosphorylates and activates MAP3K5 kinase. Has apparently no phosphoglycerate mutase activity. May be regulator of mitochondrial dynamics. Substrate for a KEAP1-dependent ubiquitin ligase complex. Contributes to the repression of NFE2L2-dependent gene expression (By similarity). Acts as a central mediator for programmed necrosis induced by TNF, by reactive oxygen species and by calcium ionophore. {ECO:0000250, ECO:0000269|PubMed:22265414}. PTM: Phosphorylated by the RIPK1/RIPK3 complex under necrotic conditions. This phosphorylation increases PGAM5 phosphatase activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. SUBUNIT: Dimer. Forms a ternary complex with NFE2L2 and KEAP1. Interacts with BCL2L1 and MAP3K5 (By similarity). Upon TNF-induced necrosis, forms in complex with RIPK1, RIPK3 and MLKL; the formation of this complex leads to PGAM5 phosphorylation (By similarity). Interacts with DNM1L; this interaction leads to DNM1L dephosphorylation and activation and eventually to mitochondria fragmentation (By similarity). {ECO:0000250}. DOMAIN: The N-terminal 35 amino acids, including the potential transmembrane alpha-helix, function as a non-cleaved mitochondrial targeting sequence that targets the protein to the cytosolic side of the outer mitochondrial membrane. {ECO:0000250}. +Q8CFF0 PAR11_MOUSE Protein mono-ADP-ribosyltransferase PARP11 (EC 2.4.2.-) (ADP-ribosyltransferase diphtheria toxin-like 11) (ARTD11) (Poly [ADP-ribose] polymerase 11) (PARP-11) 331 38,737 Alternative sequence (2); Chain (1); Domain (2); Modified residue (4) FUNCTION: Mono-ADP-ribosyltransferase that mediates mono-ADP-ribosylation of target proteins (By similarity). Plays a role in nuclear envelope stability and nuclear remodeling during spermiogenesis (PubMed:25673562). {ECO:0000250|UniProtKB:Q9NR21, ECO:0000269|PubMed:25673562}. PTM: Auto-mono-ADP-ribosylated. {ECO:0000250|UniProtKB:Q9NR21}. SUBCELLULAR LOCATION: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q9NR21}. Note=Colocalizes with NUP153 at nuclear pores. {ECO:0000250|UniProtKB:Q9NR21}. TISSUE SPECIFICITY: Predominantly expressed in testis, preferentially in postmeiotic germ cells. Also detectable in other tissues, including liver, lung, spleen, thymus and brain. {ECO:0000269|PubMed:25673562}. +Q8VDG3 PARN_MOUSE Poly(A)-specific ribonuclease PARN (EC 3.1.13.4) (Polyadenylate-specific ribonuclease) 624 71,559 Beta strand (21); Chain (1); Domain (1); Helix (22); Metal binding (4); Modified residue (10); Sequence conflict (6); Site (1); Turn (2) FUNCTION: 3'-exoribonuclease that has a preference for poly(A) tails of mRNAs, thereby efficiently degrading poly(A) tails. Exonucleolytic degradation of the poly(A) tail is often the first step in the decay of eukaryotic mRNAs and is also used to silence certain maternal mRNAs translationally during oocyte maturation and early embryonic development. Interacts with both the 3'-end poly(A) tail and the 5'-end cap structure during degradation, the interaction with the cap structure being required for an efficient degradation of poly(A) tails. Involved in nonsense-mediated mRNA decay, a critical process of selective degradation of mRNAs that contain premature stop codons. Also involved in degradation of inherently unstable mRNAs that contain AU-rich elements (AREs) in their 3'-UTR, possibly via its interaction with KHSRP. Probably mediates the removal of poly(A) tails of AREs mRNAs, which constitutes the first step of destabilization (By similarity). Also able to recognize poly(A) tails of microRNAs such as MIR21 and H/ACA box snoRNAs (small nucleolar RNAs) leading to leading to microRNAs degradation or snoRNA increased stability (By similarity). {ECO:0000250|UniProtKB:O95453}. PTM: Phosphorylation by MAPKAPK2, preventing GADD45A mRNA degradation after genotoxic stress. {ECO:0000250|UniProtKB:O95453}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O95453}. Cytoplasm {ECO:0000250|UniProtKB:O95453}. Nucleus, nucleolus {ECO:0000250|UniProtKB:O95453}. Note=Some nuclear fraction is nucleolar. {ECO:0000250|UniProtKB:O95453}. SUBUNIT: Homodimer. Found in a mRNA decay complex with RENT1, RENT2 and RENT3B. Interacts with KHSRP. Interacts with CELF1/CUGBP1. Interacts with ZC3HAV1 in an RNA-independent manner. Interacts with DHX36. {ECO:0000250|UniProtKB:O95453}. +Q91VH1 PAQR1_MOUSE Adiponectin receptor protein 1 (Progestin and adipoQ receptor family member 1) (Progestin and adipoQ receptor family member I) 375 42,366 Chain (1); Erroneous termination (1); Frameshift (1); Metal binding (3); Topological domain (8); Transmembrane (7) TRANSMEM 137 157 Helical; Name=1. {ECO:0000250|UniProtKB:Q96A54}.; TRANSMEM 171 191 Helical; Name=2. {ECO:0000250|UniProtKB:Q96A54}.; TRANSMEM 204 224 Helical; Name=3. {ECO:0000250|UniProtKB:Q96A54}.; TRANSMEM 235 255 Helical; Name=4. {ECO:0000250|UniProtKB:Q96A54}.; TRANSMEM 265 285 Helical; Name=5. {ECO:0000250|UniProtKB:Q96A54}.; TRANSMEM 299 319 Helical; Name=6. {ECO:0000250|UniProtKB:Q96A54}.; TRANSMEM 338 358 Helical; Name=7. {ECO:0000250|UniProtKB:Q96A54}. TOPO_DOM 1 136 Cytoplasmic. {ECO:0000250|UniProtKB:Q96A54}.; TOPO_DOM 158 170 Extracellular. {ECO:0000250|UniProtKB:Q96A54}.; TOPO_DOM 192 203 Cytoplasmic. {ECO:0000250|UniProtKB:Q96A54}.; TOPO_DOM 225 234 Extracellular. {ECO:0000250|UniProtKB:Q96A54}.; TOPO_DOM 256 264 Cytoplasmic. {ECO:0000250|UniProtKB:Q96A54}.; TOPO_DOM 286 298 Extracellular. {ECO:0000250|UniProtKB:Q96A54}.; TOPO_DOM 320 337 Cytoplasmic. {ECO:0000250|UniProtKB:Q96A54}.; TOPO_DOM 359 375 Extracellular. {ECO:0000250|UniProtKB:Q96A54}. FUNCTION: Receptor for ADIPOQ, an essential hormone secreted by adipocytes that regulates glucose and lipid metabolism (PubMed:17327425, PubMed:17268472, PubMed:24742672). Required for normal glucose and fat homeostasis and for maintaining a normal body weight (PubMed:17327425, PubMed:24742672). ADIPOQ-binding activates a signaling cascade that leads to increased AMPK activity, and ultimately to increased fatty acid oxidation, increased glucose uptake and decreased gluconeogenesis (PubMed:12802337, PubMed:17327425, PubMed:17268472, PubMed:24742672). Has high affinity for globular adiponectin and low affinity for full-length adiponectin (PubMed:12802337). {ECO:0000269|PubMed:12802337, ECO:0000269|PubMed:17268472, ECO:0000269|PubMed:17327425, ECO:0000269|PubMed:24742672}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17268472}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q96A54}. Note=Localized to the cell membrane and intracellular organelles. {ECO:0000250|UniProtKB:Q96A54}. SUBUNIT: May form homooligomers and heterooligomers with ADIPOR2. {ECO:0000250|UniProtKB:Q96A54}. DOMAIN: The N-terminus is cytoplasmic and the C-terminus is extracellular, contrary to what is observed for G-protein coupled receptors. Unlike G-protein coupled receptors, transmembrane helices are not kinked or tilted relative to the plane of the membrane. {ECO:0000250|UniProtKB:Q96A54}. TISSUE SPECIFICITY: Detected in brain and quadriceps muscle (at protein level) (PubMed:17327425). Widely expressed (PubMed:12802337). Expressed in heart, kidney, liver, lung, skeletal muscle, white adipose tissue, brown adipose tissue, aorta and spleen (PubMed:12802337, PubMed:24742672). Weakly expressed in brain and testis (PubMed:12802337). {ECO:0000269|PubMed:12802337, ECO:0000269|PubMed:17268472, ECO:0000269|PubMed:17327425, ECO:0000269|PubMed:24742672}. +Q8BQS5 PAQR2_MOUSE Adiponectin receptor protein 2 (Progestin and adipoQ receptor family member 2) (Progestin and adipoQ receptor family member II) 386 43,981 Alternative sequence (2); Chain (1); Metal binding (3); Sequence conflict (1); Topological domain (8); Transmembrane (7) TRANSMEM 148 168 Helical; Name=1. {ECO:0000250|UniProtKB:Q86V24}.; TRANSMEM 182 202 Helical; Name=2. {ECO:0000250|UniProtKB:Q86V24}.; TRANSMEM 214 234 Helical; Name=3. {ECO:0000250|UniProtKB:Q86V24}.; TRANSMEM 246 266 Helical; Name=4. {ECO:0000250|UniProtKB:Q86V24}.; TRANSMEM 274 294 Helical; Name=5. {ECO:0000250|UniProtKB:Q86V24}.; TRANSMEM 310 330 Helical; Name=6. {ECO:0000250|UniProtKB:Q86V24}.; TRANSMEM 349 369 Helical; Name=7. {ECO:0000250|UniProtKB:Q86V24}. TOPO_DOM 1 147 Cytoplasmic. {ECO:0000250|UniProtKB:Q86V24}.; TOPO_DOM 169 181 Extracellular. {ECO:0000250|UniProtKB:Q86V24}.; TOPO_DOM 203 213 Cytoplasmic. {ECO:0000250|UniProtKB:Q86V24}.; TOPO_DOM 235 245 Extracellular. {ECO:0000250|UniProtKB:Q86V24}.; TOPO_DOM 267 273 Cytoplasmic. {ECO:0000250|UniProtKB:Q86V24}.; TOPO_DOM 295 309 Extracellular. {ECO:0000250|UniProtKB:Q86V24}.; TOPO_DOM 331 348 Cytoplasmic. {ECO:0000250|UniProtKB:Q86V24}.; TOPO_DOM 370 386 Extracellular. {ECO:0000250|UniProtKB:Q86V24}. FUNCTION: Receptor for ADIPOQ, an essential hormone secreted by adipocytes that regulates glucose and lipid metabolism (PubMed:17327425, PubMed:17068142, PubMed:17268472, PubMed:24742672). Required for normal body fat and glucose homeostasis (PubMed:17327425, PubMed:17068142, PubMed:17268472, PubMed:24742672). ADIPOQ-binding activates a signaling cascade that leads to increased PPARA activity, and ultimately to increased fatty acid oxidation and glucose uptake (PubMed:12802337, PubMed:17268472, PubMed:24742672). Has intermediate affinity for globular and full-length adiponectin (PubMed:12802337). Required for normal revascularization after chronic ischemia caused by severing of blood vessels (PubMed:24742672). {ECO:0000269|PubMed:12802337, ECO:0000269|PubMed:17068142, ECO:0000269|PubMed:17268472, ECO:0000269|PubMed:17327425, ECO:0000269|PubMed:24742672}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q86V24}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q86V24}. Note=Localized to the cell membrane and intracellular organelles. {ECO:0000250|UniProtKB:Q86V24}. SUBUNIT: May form homooligomers and heterooligomers with ADIPOR1. {ECO:0000250|UniProtKB:Q86V24}. DOMAIN: The N-terminus is cytoplasmic and the C-terminus is extracellular, contrary to what is observed for G-protein coupled receptors. Unlike G-protein coupled receptors, transmembrane helices are not kinked or tilted relative to the plane of the membrane. {ECO:0000250|UniProtKB:Q86V24}. TISSUE SPECIFICITY: Detected in liver and quadriceps muscle (at protein level) (PubMed:17327425). Highly expressed in liver (PubMed:12802337). Highly expressed in white adipose tissue, and at intermediate levels in brown adipose tissue (PubMed:24742672). Expressed at intermediate level in heart, kidney, lung and skeletal muscle. Weakly expressed in brain, spleen and testis. {ECO:0000269|PubMed:12802337, ECO:0000269|PubMed:17327425, ECO:0000269|PubMed:24742672}. +P32114 PAX2_MOUSE Paired box protein Pax-2 414 44,580 Alternative sequence (1); Chain (1); Domain (1); Modified residue (1); Sequence conflict (8) FUNCTION: Transcription factor that may have a role in kidney cell differentiation. {ECO:0000250|UniProtKB:Q02962}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with ELGN3; the interaction targets PAX2 for destruction. Interacts with TLE4. {ECO:0000250|UniProtKB:Q02962}. TISSUE SPECIFICITY: Kidney and nephrogenic rests. DISEASE: Note=Defects in Pax2 are a cause of developmental defects of the kidney, brain, ear and eye. {ECO:0000269|PubMed:8943028}. +Q8K0Y7 PAXX_MOUSE Protein PAXX (Paralog of XRCC4 and XLF) 205 21,977 Chain (1); Domain (1); Modified residue (1); Region (1) FUNCTION: Involved in non-homologous end joining (NHEJ), a major pathway to repair double-strand breaks in DNA. May act as a scaffold required to stabilize the Ku heterodimer, composed of XRCC5/Ku80 and XRCC6/Ku70, at DNA ends and thus promote assembly and/or stability of the NHEJ machinery at double-strand break sites. {ECO:0000250|UniProtKB:Q9BUH6}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BUH6}. Note=Predominantly localizes to the nucleus. Accumulates at sites of DNA damage generated by laser microirradiation. {ECO:0000250|UniProtKB:Q9BUH6}. SUBUNIT: Homodimer. Interacts with the DNA-bound XRCC5/Ku80 and XRCC6/Ku70 heterodimer (Ku complex); the interaction is direct. Associates with the non-homologous end joining (NHEJ) complex which is at least composed of the core proteins XRCC5/Ku80, XRCC6/Ku70, PRKDC/DNA-PKcs, LIG4 and XRCC4. Additional components of the NHEJ complex include NHEJ1/XLF and PAXX. {ECO:0000250|UniProtKB:Q9BUH6}. DOMAIN: The N-terminus (residues 1-115) forms a head domain that is structurally related to those of XRCC4, XLF/NHEJ1, and SASS6. {ECO:0000250|UniProtKB:Q9BUH6}. +Q02650 PAX5_MOUSE Paired box protein Pax-5 (B-cell-specific transcription factor) (BSAP) 391 42,231 Chain (1); Domain (1) FUNCTION: May play an important role in B-cell differentiation as well as neural development and spermatogenesis. Involved in the regulation of the CD19 gene, a B-lymphoid-specific target gene. PTM: O-glycosylated. {ECO:0000305}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with ETS1, altering its DNA-binding properties (By similarity). Interacts with DAXX and TLE4. Binds DNA as a monomer. {ECO:0000250, ECO:0000269|PubMed:11799127}. +Q80TF3 PCD19_MOUSE Protocadherin-19 1145 126,035 Chain (1); Domain (6); Frameshift (1); Glycosylation (6); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 679 699 Helical. {ECO:0000255}. TOPO_DOM 22 678 Extracellular. {ECO:0000255}.; TOPO_DOM 700 1145 Cytoplasmic. {ECO:0000255}. FUNCTION: Potential calcium-dependent cell-adhesion protein. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. +O88689 PCDA4_MOUSE Protocadherin alpha-4 (PCDH-alpha-4) 947 103,143 Alternative sequence (3); Beta strand (32); Chain (1); Compositional bias (1); Disulfide bond (1); Domain (6); Glycosylation (6); Helix (7); Region (2); Repeat (6); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (7) TRANSMEM 698 718 Helical. {ECO:0000255}. TOPO_DOM 30 697 Extracellular. {ECO:0000305|PubMed:27161523}.; TOPO_DOM 719 947 Cytoplasmic. {ECO:0000305|PubMed:9655502}. FUNCTION: Calcium-dependent cell-adhesion protein involved in cells self-recognition and non-self discrimination (Probable). Thereby, it is involved in the establishment and maintenance of specific neuronal connections in the brain (PubMed:27161523). {ECO:0000305|PubMed:27161523}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9655502}; Single-pass type I membrane protein {ECO:0000305|PubMed:27161523, ECO:0000305|PubMed:9655502}. Note=Detected in dendrites and synapses. {ECO:0000269|PubMed:9655502}. SUBUNIT: Forms homodimers in trans (molecules expressed by two different cells) (PubMed:27161523). Forms promiscuous heterodimers in cis (at the plasma membrane of the same cell) with other protocadherins (PubMed:27161523). Interacts with FYN (PubMed:9655502). {ECO:0000269|PubMed:27161523, ECO:0000269|PubMed:9655502}. DOMAIN: Cadherin 1 to cadherin 4 domains mediate homophilic trans-interaction, the interaction with an identical protocadherin expressed by a neighboring cell (PubMed:27161523). This is an head-to-tail interaction, the cadherin 1 domain interacting with the cadherin 4 domain and the cadherin 2 domain interacting the cadherin 3 domain of the other protocadherin (PubMed:27161523). The cadherin 6 domain mediates promiscuous interactions with protocadherins on the same cell membrane (PubMed:27161523). Each cadherin domain binds three calcium ions (PubMed:27161523). {ECO:0000269|PubMed:27161523, ECO:0000312|PDB:5DZW}. TISSUE SPECIFICITY: Detected in brain throughout embryonic development. Detected in adult brain, in particular in cerebellum and forebrain. {ECO:0000269|PubMed:9655502}. +Q7TSK3 PCDH8_MOUSE Protocadherin-8 (Arcadlin) (Paraxial protocadherin) 1070 113,260 Alternative sequence (3); Chain (1); Domain (6); Glycosylation (1); Modified residue (1); Sequence conflict (7); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 748 768 Helical. {ECO:0000255}. TOPO_DOM 30 747 Extracellular. {ECO:0000255}.; TOPO_DOM 769 1070 Cytoplasmic. {ECO:0000255}. FUNCTION: Calcium-dependent cell-adhesion protein (By similarity). May play a role in activity-induced synaptic reorganization underlying long term memory (By similarity). Could be involved in CDH2 internalization through TAOK2/p38 MAPK pathway (By similarity). In hippocampal neurons, may play a role in the down-regulation of dendritic spines, maybe through its action on CDH2 endocytosis. {ECO:0000250, ECO:0000269|PubMed:17988630}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cell junction, synapse, presynaptic cell membrane. Cell junction, synapse, postsynaptic cell membrane {ECO:0000250}. Note=Expressed in neuronal cell bodies and dendrites. Localized to excitatory, but not with inhibitory, synapses. {ECO:0000250}. SUBUNIT: The N-terminal extracellular domain forms homophilic interactions; these interactions activate p38 MAPK via TAOK2 and trigger endocytosis. Interacts with CDH2; this interaction may lead to CDH2 cointernalization. Interacts with CDH11. Interacts with TAOK2. {ECO:0000250}. +Q91Y20 PCDAA_MOUSE Protocadherin alpha-10 (PCDH-alpha-10) 946 102,057 Chain (1); Compositional bias (1); Domain (6); Glycosylation (2); Region (1); Repeat (6); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 698 718 Helical. {ECO:0000255}. TOPO_DOM 31 697 Extracellular. {ECO:0000305}.; TOPO_DOM 719 946 Cytoplasmic. {ECO:0000305}. FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain. {ECO:0000303|PubMed:11230163}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000303|PubMed:11230163}; Single-pass type I membrane protein {ECO:0000303|PubMed:11230163}. +Q8CAE9 PDXL2_MOUSE Podocalyxin-like protein 2 (Endoglycan) 603 64,973 Alternative sequence (3); Chain (1); Compositional bias (1); Glycosylation (3); Modified residue (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 500 520 Helical. {ECO:0000255}. TOPO_DOM 29 499 Extracellular. {ECO:0000255}.; TOPO_DOM 521 603 Cytoplasmic. {ECO:0000255}. FUNCTION: Acts as a ligand for vascular selectins. Mediates rapid rolling of leukocytes over vascular surfaces through high affinity divalent cation-dependent interactions with E-, P- and L-selectins (By similarity). {ECO:0000250}. PTM: Glycosylated; contains chondroitin sulfate. Displays sialylated O-linked oligosaccharides (By similarity). {ECO:0000250}.; PTM: Sulfation is necessary for interaction with SELL. Sialylated O-linked oligosaccharides are necessary for interaction with SELL, SELE and SELP (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Homodimer; disulfide-linked. Interacts with SELL, SELE and SELP (By similarity). {ECO:0000250}. +P70296 PEBP1_MOUSE Phosphatidylethanolamine-binding protein 1 (PEBP-1) (HCNPpp) [Cleaved into: Hippocampal cholinergic neurostimulating peptide (HCNP)] 187 20,830 Beta strand (10); Chain (1); Helix (6); Initiator methionine (1); Modified residue (8); Peptide (1); Region (1); Sequence conflict (1) FUNCTION: Binds ATP, opioids and phosphatidylethanolamine. Has lower affinity for phosphatidylinositol and phosphatidylcholine. Serine protease inhibitor which inhibits thrombin, neuropsin and chymotrypsin but not trypsin, tissue type plasminogen activator and elastase. Inhibits the kinase activity of RAF1 by inhibiting its activation and by dissociating the RAF1/MEK complex and acting as a competitive inhibitor of MEK phosphorylation (By similarity). {ECO:0000250}.; FUNCTION: HCNP may be involved in the function of the presynaptic cholinergic neurons of the central nervous system. HCNP increases the production of choline acetyltransferase but not acetylcholinesterase. Seems to be mediated by a specific receptor (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Has a tendency to form dimers by disulfide cross-linking. Interacts with RAF1 and this interaction is enhanced if RAF1 is phosphorylated on residues 'Ser-338', 'Ser-339', 'Tyr-340' and 'Tyr-341'. Interacts with ALOX15; in response to IL13/interleukin-13, prevents the interaction of PEBP1 with RAF1 to activate the ERK signaling cascade (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: HCNP is expressed in brain. Increased expression in aged senescence-accelerated mice. +Q8VIN1 PEBP2_MOUSE Phosphatidylethanolamine-binding protein 2 (PEBP-2) 187 21,191 Alternative sequence (1); Beta strand (10); Chain (1); Helix (5); Modified residue (3) FUNCTION: May bind to phospholipids. May act as serine protease inhibitor (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12193403}. Note=At the cell periphery in pachytene spermatocytes and round spermatids, in the distal dorsal region of the sperm head and in the sperm tail. TISSUE SPECIFICITY: Testis specific. {ECO:0000269|PubMed:12193403}. +Q62048 PEA15_MOUSE Astrocytic phosphoprotein PEA-15 (15 kDa phosphoprotein enriched in astrocytes) 130 15,054 Alternative sequence (2); Chain (1); Domain (1); Helix (6); Modified residue (4); Mutagenesis (2); Region (2); Turn (2) FUNCTION: Blocks Ras-mediated inhibition of integrin activation and modulates the ERK MAP kinase cascade. Inhibits RPS6KA3 activities by retaining it in the cytoplasm. Inhibits both TNFRSF6- and TNFRSF1A-mediated CASP8 activity and apoptosis. Regulates glucose transport by controlling both the content of SLC2A1 glucose transporters on the plasma membrane and the insulin-dependent trafficking of SLC2A4 from the cell interior to the surface (By similarity). {ECO:0000250, ECO:0000269|PubMed:10588860}. PTM: Phosphorylated by protein kinase C and calcium-calmodulin-dependent protein kinase. These phosphorylation events are modulated by neurotransmitters or hormones. {ECO:0000269|PubMed:10588860}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10926929}. Note=Associated with microtubules. SUBUNIT: Binds RPS6KA3, MAPK3 and MAPK1. Interacts with CASP8 and FADD (By similarity). Transient interaction with PLD1 and PLD2. {ECO:0000250, ECO:0000269|PubMed:10926929}. TISSUE SPECIFICITY: Predominantly expressed in the brain. Low levels in some peripheral organs. +Q9D106 PEPA5_MOUSE Pepsin A-5 (EC 3.4.23.1) (Pepsin F) 387 42,824 Active site (2); Chain (1); Disulfide bond (3); Domain (1); Propeptide (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Shows particularly broad specificity; although bonds involving phenylalanine and leucine are preferred, many others are also cleaved to some extent (By similarity). May play a role as a specialized neonatal digestive enzyme (Probable). {ECO:0000250|UniProtKB:Q9N2D4, ECO:0000305|PubMed:11566730}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Expressed in glandular chief cells of the neonatal stomach. Expressed in yolk sacs of the placenta (at protein level). {ECO:0000269|PubMed:11566730}. +Q6DID5 PWP3A_MOUSE PWWP domain-containing DNA repair factor 3A (PWWP3A) (Mutated melanoma-associated antigen 1) (MUM-1) (PWWP domain-containing protein MUM1) 682 76,069 Chain (1); Domain (1); Erroneous initiation (1); Frameshift (1); Modified residue (4); Sequence caution (1); Sequence conflict (3) FUNCTION: Involved in the DNA damage response pathway by contributing to the maintenance of chromatin architecture. Recruited to the vicinity of DNA breaks by TP53BP1 and plays an accessory role to facilitate damage-induced chromatin changes and promoting chromatin relaxation. Required for efficient DNA repair and cell survival following DNA damage (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Recruited to DNA damage sites via its interaction with the BRCT domain of TP53BP1. {ECO:0000250}. SUBUNIT: Interacts with TP53BP1 (via BRCT domain); the interaction is not dependent on its phosphorylation status. Binds nucleosomes. Interacts with trimethylated 'Lys-36' of histone H3 (H3K36me3) (in vitro) (By similarity). {ECO:0000250}. DOMAIN: The PWWP domain mediates the interaction with nucleosomes. +Q4VA55 PWP3B_MOUSE PWWP domain-containing DNA repair factor 3B (PWWP3B) (Mutated melanoma-associated antigen 1-like protein 1) (MUM1-like protein 1) (PWWP domain-containing protein MUM1L1) 681 76,989 Chain (1); Domain (1); Erroneous initiation (1); Modified residue (1); Sequence conflict (1) +Q61907 PEMT_MOUSE Phosphatidylethanolamine N-methyltransferase (PEAMT) (PEMT) (EC 2.1.1.17) (EC 2.1.1.71) (Phospholipid methyltransferase) (PLMT) 199 22,579 Alternative sequence (1); Chain (1); Frameshift (1); Intramembrane (1); Region (2); Sequence conflict (2); Topological domain (5); Transmembrane (3) INTRAMEM 13 33 Helical. {ECO:0000255|HAMAP-Rule:MF_03216}. TRANSMEM 46 66 Helical. {ECO:0000255|HAMAP-Rule:MF_03216}.; TRANSMEM 94 114 Helical. {ECO:0000255|HAMAP-Rule:MF_03216}.; TRANSMEM 158 178 Helical. {ECO:0000255|HAMAP-Rule:MF_03216}. TOPO_DOM 1 12 Lumenal. {ECO:0000255|HAMAP-Rule:MF_03216}.; TOPO_DOM 34 45 Lumenal. {ECO:0000255|HAMAP-Rule:MF_03216}.; TOPO_DOM 67 93 Cytoplasmic. {ECO:0000255|HAMAP-Rule:MF_03216}.; TOPO_DOM 115 157 Lumenal. {ECO:0000255|HAMAP-Rule:MF_03216}.; TOPO_DOM 179 199 Cytoplasmic. {ECO:0000255|HAMAP-Rule:MF_03216}. Phospholipid metabolism; phosphatidylcholine biosynthesis. FUNCTION: Catalyzes the three sequential steps of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylethanolamine (PE) to phosphatidylmonomethylethanolamine (PMME), PMME to phosphatidyldimethylethanolamine (PDME), and PDME to phosphatidylcholine (PC). {ECO:0000255|HAMAP-Rule:MF_03216, ECO:0000269|PubMed:9371769, ECO:0000269|PubMed:9765216}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03216}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03216}. Mitochondrion membrane {ECO:0000255|HAMAP-Rule:MF_03216}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03216}. Note=Found in endoplasmic reticulum where most PEMT activity is generated and in mitochondria. {ECO:0000255|HAMAP-Rule:MF_03216}. TISSUE SPECIFICITY: Liver. +Q9D9M4 PDZD9_MOUSE PDZ domain-containing protein 9 266 29,761 Beta strand (7); Chain (1); Domain (1); Helix (2); Sequence conflict (3); Turn (1) +P49290 PERE_MOUSE Eosinophil peroxidase (EPO) (EC 1.11.1.7) [Cleaved into: Eosinophil peroxidase light chain; Eosinophil peroxidase heavy chain] 716 81,380 Active site (1); Binding site (2); Chain (2); Disulfide bond (6); Erroneous initiation (1); Glycosylation (5); Metal binding (6); Modified residue (1); Propeptide (1); Sequence conflict (4); Signal peptide (1); Site (1) FUNCTION: Mediates tyrosine nitration of secondary granule proteins in mature resting eosinophils. {ECO:0000250, ECO:0000269|PubMed:18694936}. SUBCELLULAR LOCATION: Cytoplasmic granule. Note=Cytoplasmic granules of eosinophils. SUBUNIT: Tetramer of two light chains and two heavy chains. {ECO:0000250}. +P97865 PEX7_MOUSE Peroxisomal targeting signal 2 receptor (PTS2 receptor) (Peroxin-7) 318 35,502 Chain (1); Repeat (6) FUNCTION: Binds to the N-terminal PTS2-type peroxisomal targeting signal and plays an essential role in peroxisomal protein import. {ECO:0000250|UniProtKB:Q8R537}. SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:Q8R537}. Cytoplasm {ECO:0000250|UniProtKB:Q8R537}. SUBUNIT: Interacts with PEX5 and VWA8. {ECO:0000250|UniProtKB:Q8R537}. +Q99LC9 PEX6_MOUSE Peroxisome assembly factor 2 (PAF-2) (Peroxin-6) (Peroxisomal biogenesis factor 6) (Peroxisomal-type ATPase 1) 981 104,549 Chain (1); Modified residue (1); Nucleotide binding (2); Sequence conflict (2) FUNCTION: Involved in peroxisome biosynthesis. Required for stability of the PTS1 receptor. Probably required for protein import into peroxisomes. Anchored by PEX26 to peroxisome membranes, possibly to form heteromeric AAA ATPase complexes required for the import of proteins into peroxisomes (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Peroxisome membrane {ECO:0000250|UniProtKB:Q13608}. Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:26593283}. Note=Associated with peroxisomal membranes (By similarity). Localized at the base of the outer segment of photoreceptor cells (PubMed:26593283). {ECO:0000250|UniProtKB:Q13608, ECO:0000269|PubMed:26593283}. SUBUNIT: Interacts directly with PEX26 and PEX1. Mediates the indirect interaction between PEX1 and PEX26. Interacts with ZFAND6 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: In the teeth, expressed in ameloblasts and odontoblasts (PubMed:26593283). Expressed in the retina, at higher levels in the ganglion cell layer and photoreceptor layer at the joint between the outer and inner segments (PubMed:26593283, PubMed:27302843). {ECO:0000269|PubMed:26593283, ECO:0000269|PubMed:27302843}. +Q9ERU9 RBP2_MOUSE E3 SUMO-protein ligase RanBP2 (EC 2.3.2.-) (Ran-binding protein 2) (RanBP2) 3053 341,121 Chain (1); Compositional bias (3); Cross-link (14); Domain (5); Modified residue (45); Region (7); Repeat (29); Sequence conflict (11); Zinc finger (6) Protein modification; protein sumoylation. FUNCTION: E3 SUMO-protein ligase which facilitates SUMO1 and SUMO2 conjugation by UBE2I. Involved in transport factor (Ran-GTP, karyopherin)-mediated protein import via the F-G repeat-containing domain which acts as a docking site for substrates. Binds single-stranded RNA (in vitro). May bind DNA. Component of the nuclear export pathway. Specific docking site for the nuclear export factor exportin-1 (By similarity). Sumoylates PML at 'Lys-490' which is essential for the proper assembly of PML-NB. Recruits BICD2 to the nuclear envelope and cytoplasmic stacks of nuclear pore complex known as annulate lamellae during G2 phase of cell cycle. Probable inactive PPIase with no peptidyl-prolyl cis-trans isomerase activity. {ECO:0000250|UniProtKB:P49792}. PTM: Polyubiquitinated by PRKN, which leads to proteasomal degradation. {ECO:0000250|UniProtKB:P49792}.; PTM: The inner channel of the NPC has a different redox environment from the cytoplasm and allows the formation of interchain disulfide bonds between some nucleoporins, the significant increase of these linkages upon oxidative stress reduces the permeability of the NPC. {ECO:0000269|PubMed:23641069}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P49792}. Nucleus membrane {ECO:0000250|UniProtKB:P49792}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P49792}. Nucleus envelope {ECO:0000250|UniProtKB:P49792}. Note=Detected in diffuse and discrete intranuclear foci. Cytoplasmic filaments. {ECO:0000250|UniProtKB:P49792}. SUBUNIT: Forms a complex with NXT1, NXF1 and RANGAP1 (By similarity). Forms a tight complex with RANBP1 and UBE2I (By similarity). Interacts with SUMO1 but not SUMO2 (By similarity). Interacts with sumoylated RANGAP1 (By similarity). Interacts with CDCA8 (By similarity). Interacts with PML (By similarity). Interacts with BICD2 (By similarity). Interacts with PRKN (PubMed:16332688). {ECO:0000250|UniProtKB:P49792, ECO:0000269|PubMed:16332688}. DOMAIN: Contains FG repeats. FG repeats are interaction sites for karyopherins (importins, exportins) and form probably an affinity gradient, guiding the transport proteins unidirectionally with their cargo through the NPC. FG repeat regions are highly flexible and lack ordered secondary structure. The overall conservation of FG repeats regarding exact sequence, spacing, and repeat unit length is limited. {ECO:0000305}.; DOMAIN: The PPIase cyclophilin-type domain has high structural similarity with PPIA, but has extremely low and barely detectable proline isomerase activity (in vitro) (By similarity). Only about half of the residues that surround the PPIA active site cleft are conserved. {ECO:0000250|UniProtKB:P49792}. +O70250 PGAM2_MOUSE Phosphoglycerate mutase 2 (EC 5.4.2.11) (EC 5.4.2.4) (BPG-dependent PGAM 2) (Muscle-specific phosphoglycerate mutase) (Phosphoglycerate mutase isozyme M) (PGAM-M) 253 28,827 Active site (2); Binding site (2); Chain (1); Compositional bias (1); Modified residue (8); Region (5); Site (1) FUNCTION: Interconversion of 3- and 2-phosphoglycerate with 2,3-bisphosphoglycerate as the primer of the reaction. Can also catalyze the reaction of EC 5.4.2.4 (synthase), but with a reduced activity. SUBUNIT: Homodimer (By similarity). Interacts with ENO1 (PubMed:23446454). {ECO:0000250|UniProtKB:P18669, ECO:0000269|PubMed:23446454}. TISSUE SPECIFICITY: Testis. {ECO:0000269|PubMed:23446454}. +A1A547 PGRP3_MOUSE Peptidoglycan recognition protein 3 (Peptidoglycan recognition protein I-alpha) (PGLYRPIalpha) (PGRP-I-alpha) (Peptidoglycan recognition protein intermediate alpha) 347 38,503 Binding site (2); Chain (1); Disulfide bond (3); Domain (2); Glycosylation (1); Region (1); Sequence conflict (5); Signal peptide (1) FUNCTION: Pattern receptor that binds to murein peptidoglycans (PGN) of Gram-positive bacteria. Has bactericidal activity towards Gram-positive bacteria. May kill Gram-positive bacteria by interfering with peptidoglycan biosynthesis. Binds also to Gram-negative bacteria, and has bacteriostatic activity towards Gram-negative bacteria. Plays a role in innate immunity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Monomer. Homodimer; disulfide-linked. Heterodimer with PGLYRP4; disulfide-linked (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Detected in lung, spleen and stomach, and at low levels in eye, heart, thymus and testis. {ECO:0000269|PubMed:15177568}. +Q9CWB5 PGPIL_MOUSE Pyroglutamyl-peptidase 1-like protein (EC 3.4.19.-) 130 14,267 Active site (3); Chain (1) +Q9ESW8 PGPI_MOUSE Pyroglutamyl-peptidase 1 (EC 3.4.19.3) (5-oxoprolyl-peptidase) (Pyroglutamyl aminopeptidase I) (PAP-I) (Pyroglutamyl-peptidase I) (PGP-I) (Pyrrolidone-carboxylate peptidase) 209 22,934 Active site (3); Chain (1) FUNCTION: Removes 5-oxoproline from various penultimate amino acid residues except L-proline. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. +Q8BYK5 PHAR3_MOUSE Phosphatase and actin regulator 3 (Scaffold-associated PP1-inhibiting protein) (Scapinin) 558 62,652 Alternative sequence (3); Chain (1); Coiled coil (1); Compositional bias (1); Modified residue (3); Repeat (4) SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000250}. Note=Localized to the nuclear matrix-intermediate filament scaffold. {ECO:0000250}. SUBUNIT: Binds PPP1CA and actin; thus inhibiting the protein phosphatase 1 (PP1) activity. {ECO:0000250}. +P67778 PHB_MOUSE Prohibitin (B-cell receptor-associated protein 32) (BAP 32) 272 29,820 Chain (1); Coiled coil (1); Initiator methionine (1); Modified residue (7); Sequence conflict (2) FUNCTION: Prohibitin inhibits DNA synthesis. It has a role in regulating proliferation. As yet it is unclear if the protein or the mRNA exhibits this effect. May play a role in regulating mitochondrial respiration activity and in aging (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:11302691}. SUBUNIT: Interacts with PHB2. Interacts with STOML2 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed in different tissues. {ECO:0000269|PubMed:8070406}. +Q8BGT8 PHIPL_MOUSE Phytanoyl-CoA hydroxylase-interacting protein-like 375 42,341 Alternative sequence (1); Chain (1); Domain (1); Frameshift (1); Glycosylation (2); Modified residue (4); Sequence caution (1); Sequence conflict (2) FUNCTION: May play a role in the development of the central system. {ECO:0000250}. +Q8VDD9 PHIP_MOUSE PH-interacting protein (PHIP) (IRS-1 PH domain-binding protein) (Neuronal differentiation-related protein) (NDRP) (WD repeat-containing protein 11) 1821 206,726 Chain (1); Compositional bias (2); Cross-link (5); Domain (2); Modified residue (25); Region (1); Repeat (8); Sequence caution (3); Sequence conflict (7) FUNCTION: Probable regulator of the insulin and insulin-like growth factor signaling pathways. Stimulates cell proliferation through regulation of cyclin transcription and has an anti-apoptotic activity through AKT1 phosphorylation and activation. Plays a role in the regulation of cell morphology and cytoskeletal organization. {ECO:0000269|PubMed:11018022, ECO:0000269|PubMed:12242307, ECO:0000269|PubMed:17636024}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17636024}. SUBUNIT: Interacts (via bromo domain) with acetylated lysine residues on histone H1.4, histone H3 and H4 (in vitro) (By similarity). Interacts with IRS1 and IRS2. {ECO:0000250, ECO:0000269|PubMed:11018022}. TISSUE SPECIFICITY: Widely expressed with most abundant expression detected in pancreatic islets, brain and skeletal muscle. Predominantly expressed in developing and regenerating neurons. Expressed in adult brain (granular layer of the olfactorium bulb, hippocampus, dentate gyrus and cerebellum internal granular layer). Expressed in the CA3 region of adult hippocampus, adult and fetal retina, perinatal dorsal root ganglion and embryonal olfactory epithelia (at protein level). {ECO:0000269|PubMed:11018022, ECO:0000269|PubMed:11098134, ECO:0000269|PubMed:17636024}. +P07934 PHKG1_MOUSE Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoform (EC 2.7.11.19) (Phosphorylase kinase subunit gamma-1) (Serine/threonine-protein kinase PHKG1) (EC 2.7.11.1) (EC 2.7.11.26) 388 44,960 Active site (1); Binding site (1); Chain (1); Domain (1); Nucleotide binding (1); Region (2); Sequence conflict (1) FUNCTION: Catalytic subunit of the phosphorylase b kinase (PHK), which mediates the neural and hormonal regulation of glycogen breakdown (glycogenolysis) by phosphorylating and thereby activating glycogen phosphorylase. In vitro, phosphorylates PYGM, TNNI3, MAPT/TAU, GAP43 and NRGN/RC3 (By similarity). {ECO:0000250}. SUBUNIT: Hexadecamer of 4 heterotetramers, each composed of alpha, beta, gamma, and delta subunits. Alpha (PHKA1 or PHKA2) and beta (PHKB) are regulatory subunits, gamma (PHKG1 or PHKG2) is the catalytic subunit, and delta is calmodulin. DOMAIN: The two calmodulin-binding domains appear to act in concert to bind a single molecule of calmodulin and are pseudosubstrate/autoinhibitory domains. {ECO:0000250}. +Q9DBX2 PHLP_MOUSE Phosducin-like protein (PHLP) 301 34,407 Chain (1); Initiator methionine (1); Modified residue (6); Region (1) FUNCTION: Functions as a co-chaperone for CCT in the assembly of heterotrimeric G protein complexes, facilitates the assembly of both Gbeta-Ggamma and RGS-Gbeta5 heterodimers (PubMed:23637185). Acts also as a positive regulator of hedgehog signaling and regulates ciliary function (PubMed:29290584). {ECO:0000269|PubMed:23637185, ECO:0000269|PubMed:29290584}. SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000269|PubMed:29290584}. SUBUNIT: Forms a complex with the beta and gamma subunits of the GTP-binding protein, transducin. Interacts with the CCT chaperonin complex (By similarity). {ECO:0000250}. +O08969 PHLA2_MOUSE Pleckstrin homology-like domain family A member 2 (Imprinted in placenta and liver protein) (Protein 50C15) 144 16,727 Chain (1); Domain (1); Modified residue (1); Mutagenesis (3) FUNCTION: Plays a role in regulating placenta growth. May act via its PH domain that competes with other PH domain-containing proteins, thereby preventing their binding to membrane lipids. {ECO:0000269|PubMed:12032310}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12374806}. Membrane {ECO:0000269|PubMed:12374806}; Peripheral membrane protein {ECO:0000269|PubMed:12374806}. DOMAIN: The PH domain binds phosphoinositides with a broad specificity. It may compete with the PH domain of some other proteins, thereby interfering with their binding to phosphatidylinositol 4,5-bisphosphate (PIP2) and phosphatidylinositol 3,4,5-trisphosphate (PIP3) (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Specifically expressed at high levels in extraembryonic tissues in the developing conceptus (at protein level). Expressed in placenta and yolc sac. Expressed at low levels in fetal liver and kidney. {ECO:0000269|PubMed:10594239}. +Q6PDH0 PHLB1_MOUSE Pleckstrin homology-like domain family B member 1 (Protein LL5-alpha) 1371 150,070 Alternative sequence (3); Chain (1); Coiled coil (2); Domain (2); Modified residue (29); Sequence conflict (1) DOMAIN: The PH domain mediates the binding to phosphoinositides. {ECO:0000250}. +A6H5X4 PHF11_MOUSE PHD finger protein 11 (PHD finger protein 11-like) (PHD finger protein 11D) 337 37,728 Alternative sequence (2); Chain (1); Erroneous initiation (1); Sequence conflict (4); Zinc finger (2) FUNCTION: Positive regulator of Th1-type cytokine gene expression. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with BRCA1 and RELA. {ECO:0000250}. +Q9DAG9 PHF7_MOUSE PHD finger protein 7 (Testis development protein NYD-SP6) 307 35,381 Alternative sequence (1); Beta strand (2); Chain (1); Helix (1); Turn (1); Zinc finger (3) FUNCTION: May play a role in spermatogenesis. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in Sertoli cells in testis. {ECO:0000269|PubMed:11829468}. +Q8R2H9 PHOP1_MOUSE Phosphoethanolamine/phosphocholine phosphatase (EC 3.1.3.75) 267 29,911 Active site (2); Binding site (2); Chain (1); Metal binding (3) FUNCTION: Phosphatase that has a high activity toward phosphoethanolamine (PEA) and phosphocholine (PCho). Involved in the generation of inorganic phosphate for bone mineralization. {ECO:0000269|PubMed:17227223}. TISSUE SPECIFICITY: Has a 120-fold higher level of expression in bone compared with a range of soft tissues. {ECO:0000269|PubMed:17227223}. +P15973 PHXR1_MOUSE Putative per-hexamer repeat protein 1 60 6,756 Chain (1) +P15972 PHXR2_MOUSE Putative per-hexamer repeat protein 2 65 7,277 Chain (1) +Q9Z129 RECQ1_MOUSE ATP-dependent DNA helicase Q1 (EC 3.6.4.12) (DNA-dependent ATPase Q1) (RecQ protein-like 1) 648 72,484 Alternative sequence (1); Chain (1); Domain (2); Modified residue (4); Motif (1); Nucleotide binding (1); Sequence conflict (8) FUNCTION: Isoform alpha is a DNA helicase that may play a role in the repair of DNA that is damaged by ultraviolet light or other mutagens. Isoform beta may have important roles in the meiotic process. Both isoforms exhibit a magnesium-dependent ATP-dependent DNA-helicase activity that unwinds single- and double-stranded DNA in a 3'-5' direction. {ECO:0000269|PubMed:9838113}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with EXO1 and MLH1. {ECO:0000250}. TISSUE SPECIFICITY: Isoform alpha is expressed in all tissues examined. Isoform beta is only expressed in spermatocytes, expression increases at pachytene (17 days old) and decreases after completion of meiosis II (7 weeks old). {ECO:0000269|PubMed:9838113}. +Q75NR7 RECQ4_MOUSE ATP-dependent DNA helicase Q4 (EC 3.6.4.12) (DNA helicase, RecQ-like type 4) (RecQ4) (RecQ protein-like 4) 1216 135,124 Alternative sequence (1); Chain (1); Domain (2); Modified residue (2); Motif (1); Nucleotide binding (1); Sequence conflict (5); Zinc finger (1) FUNCTION: DNA-dependent ATPase (By similarity). May play a role in development of the palate and the limbs. May modulate chromosome segregation. {ECO:0000250, ECO:0000269|PubMed:12915449, ECO:0000269|PubMed:15703196}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O94761}. Nucleus {ECO:0000250|UniProtKB:O94761}. SUBUNIT: Interacts with UBR1 and UBR2. Interacts with MCM10; this interaction regulates RECQL4 unwinding activity (By similarity). {ECO:0000250}. +Q8VID5 RECQ5_MOUSE ATP-dependent DNA helicase Q5 (EC 3.6.4.12) (DNA helicase, RecQ-like type 5) (RecQ5) (RECQL5beta) (RecQ protein-like 5) 982 108,246 Chain (1); Domain (2); Modified residue (4); Motif (1); Nucleotide binding (1); Region (2); Sequence conflict (2) FUNCTION: DNA helicase that plays an important role in DNA replication, transcription and repair. Inhibits elongation of stalled transcripts at DNA damage sites by binding to the RNA polymerase II subunit POLR2A and blocking the TCEA1 binding site. Required for mitotic chromosome separation after cross-over events and cell cycle progress. Required for efficient DNA repair, including repair of inter-strand cross-links. Stimulates DNA decatenation mediated by TOP2A. Prevents sister chromatid exchange and homologous recombination (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:O94762}. Note=Recruited to sites of DNA damage, such as single-strand breaks and inter-strand cross-links, and at stalled replication forks. {ECO:0000250|UniProtKB:O94762}. SUBUNIT: Monomer. Interacts with TOP2A, TOP3A and TOP3B. Interacts with RNA polymerase II subunit POLR2A. Identified in a complex with the RNA polymerase II core bound to DNA. Interacts with RAD51 (By similarity). {ECO:0000250}. +P58750 PIM3_MOUSE Serine/threonine-protein kinase pim-3 (EC 2.7.11.1) 326 35,970 Active site (1); Binding site (1); Chain (1); Domain (1); Mutagenesis (1); Nucleotide binding (1) FUNCTION: Proto-oncogene with serine/threonine kinase activity that can prevent apoptosis and promote cell survival and protein translation. May contribute to tumorigenesis through: the delivery of survival signaling through phosphorylation of BAD which induces release of the anti-apoptotic protein Bcl-X(L), the regulation of cell cycle progression and protein synthesis and by regulation of MYC transcriptional activity. Additionally to this role on tumorigenesis, can also negatively regulate insulin secretion by inhibiting the activation of MAPK1/3 (ERK1/2), through SOCS6. Involved also in the control of energy metabolism and regulation of AMPK activity in modulating MYC and PPARGC1A protein levels and cell growth. {ECO:0000269|PubMed:15199164, ECO:0000269|PubMed:21099329, ECO:0000269|PubMed:21187426}. PTM: Ubiquitinated, leading to proteasomal degradation. {ECO:0000250}.; PTM: Phosphorylated. Interaction with PPP2CA promotes dephosphorylation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with BAD (By similarity). Interacts with PPP2CA; this interaction promotes dephosphorylation of PIM3, ubiquitination and proteasomal degradation (By similarity). Interacts with SOCS6. {ECO:0000250, ECO:0000269|PubMed:21099329}. TISSUE SPECIFICITY: Detected in pancreas but exclusively in beta-cells. {ECO:0000269|PubMed:21099329}. +Q8BFY6 PEF1_MOUSE Peflin (PEF protein with a long N-terminal hydrophobic domain) (Penta-EF hand domain-containing protein 1) 275 29,228 Calcium binding (2); Chain (1); Domain (5); Frameshift (1); Region (2); Repeat (8); Sequence conflict (3) FUNCTION: Calcium-binding protein that acts as an adapter that bridges unrelated proteins or stabilizes weak protein-protein complexes in response to calcium. Together with PDCD6, acts as calcium-dependent adapter for the BCR(KLHL12) complex, a complex involved in endoplasmic reticulum (ER)-Golgi transport by regulating the size of COPII coats. In response to cytosolic calcium increase, the heterodimer formed with PDCD6 interacts with, and bridges together the BCR(KLHL12) complex and SEC31 (SEC31A or SEC31B), promoting monoubiquitination of SEC31 and subsequent collagen export, which is required for neural crest specification. Its role in the heterodimer formed with PDCD6 is however unclear: some evidences show that PEF1 and PDCD6 work together and promote association between PDCD6 and SEC31 in presence of calcium. Other reports show that PEF1 dissociates from PDCD6 in presence of calcium, and may act as a negative regulator of PDCD6 (By similarity). Also acts as a negative regulator of ER-Golgi transport; possibly by inhibiting interaction between PDCD6 and SEC31 (By similarity). {ECO:0000250|UniProtKB:Q641Z8, ECO:0000250|UniProtKB:Q9UBV8}. PTM: Ubiquitinated by the BCR(KLHL12) E3 ubiquitin ligase complex. {ECO:0000250|UniProtKB:Q9UBV8}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UBV8}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q641Z8}. Membrane {ECO:0000250|UniProtKB:Q9UBV8}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9UBV8}. Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250|UniProtKB:Q9UBV8}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9UBV8}. Note=Membrane-associated in the presence of Ca(2+) (By similarity). Localizes to endoplasmic reticulum exit site (ERES) (By similarity). {ECO:0000250|UniProtKB:Q641Z8, ECO:0000250|UniProtKB:Q9UBV8}. SUBUNIT: Heterodimer; heterodimerizes (via the EF-hand 5) with PDCD6. Dissociates from PDCD6 in presence of calcium. {ECO:0000250|UniProtKB:Q9UBV8}. +Q9Z211 PX11A_MOUSE Peroxisomal membrane protein 11A (Peroxin-11A) (Peroxisomal biogenesis factor 11A) (Protein PEX11 homolog alpha) (PEX11-alpha) 246 28,153 Chain (1); Region (1); Topological domain (3); Transmembrane (2) TRANSMEM 94 114 Helical. {ECO:0000255}.; TRANSMEM 218 238 Helical. {ECO:0000255}. TOPO_DOM 1 93 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 115 217 Lumenal. {ECO:0000255}.; TOPO_DOM 239 246 Cytoplasmic. {ECO:0000255}. FUNCTION: May be involved in peroxisomal proliferation and may regulate peroxisomes division. May mediate binding of coatomer proteins to the peroxisomal membrane (By similarity). Promotes membrane protrusion and elongation on the peroxisomal surface. {ECO:0000250|UniProtKB:O70597, ECO:0000250|UniProtKB:O75192, ECO:0000269|PubMed:12417726}. SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000250|UniProtKB:O75192}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O75192}. SUBUNIT: Homodimer. Heterodimer with PEX11G. Probably interacts with COPB2 and COPA. Interacts with PEX19. Interacts with FIS1. {ECO:0000250|UniProtKB:O70597, ECO:0000250|UniProtKB:O75192}. TISSUE SPECIFICITY: Strongly expressed in liver and at lower levels in heart, brain, kidney and testis. {ECO:0000269|PubMed:12417726}. +Q11136 PEPD_MOUSE Xaa-Pro dipeptidase (X-Pro dipeptidase) (EC 3.4.13.9) (Imidodipeptidase) (Peptidase 4) (Peptidase D) (Proline dipeptidase) (Prolidase) 493 55,029 Chain (1); Initiator methionine (1); Metal binding (7); Modified residue (2); Sequence conflict (3) FUNCTION: Splits dipeptides with a prolyl or hydroxyprolyl residue in the C-terminal position. Plays an important role in collagen metabolism because of the high level of iminoacids in collagen. SUBUNIT: Homodimer. +Q6P6M5 PX11C_MOUSE Peroxisomal membrane protein 11C (Peroxin-11C) (Peroxisomal biogenesis factor 11C) (Protein PEX11 homolog gamma) (PEX11-gamma) 241 27,152 Alternative sequence (2); Chain (1); Sequence conflict (1); Topological domain (3); Transmembrane (2) TRANSMEM 123 149 Helical. {ECO:0000255}.; TRANSMEM 212 227 Helical. {ECO:0000255}. TOPO_DOM 1 122 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 150 211 Lumenal. {ECO:0000255}.; TOPO_DOM 228 241 Cytoplasmic. {ECO:0000255}. FUNCTION: Promotes membrane protrusion and elongation on the peroxisomal surface. {ECO:0000250|UniProtKB:Q96HA9}. SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000250|UniProtKB:Q96HA9}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q96HA9}. SUBUNIT: Homodimer. Heterodimer with either PEX11A or PEX11B. Interacts with FIS1. {ECO:0000250|UniProtKB:Q96HA9}. TISSUE SPECIFICITY: Expressed in liver and at much lower levels in heart, kidney and testis. {ECO:0000269|PubMed:12417726}. +Q9DC11 PXDC2_MOUSE Plexin domain-containing protein 2 (Tumor endothelial marker 7-related protein) 530 59,616 Chain (1); Compositional bias (1); Domain (1); Glycosylation (2); Modified residue (1); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 456 476 Helical. {ECO:0000255}. TOPO_DOM 31 455 Extracellular. {ECO:0000255}.; TOPO_DOM 477 530 Cytoplasmic. {ECO:0000255}. FUNCTION: May play a role in tumor angiogenesis. {ECO:0000269|PubMed:11559528}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Interacts with CTTN. {ECO:0000269|PubMed:15574754}. TISSUE SPECIFICITY: Expressed in tumor endothelium and in vessels of some normal tissues, such as the muscle and lung. {ECO:0000269|PubMed:11559528}. +Q6NSR8 PEPL1_MOUSE Probable aminopeptidase NPEPL1 (EC 3.4.11.-) (Aminopeptidase-like 1) 524 55,940 Active site (2); Chain (1); Metal binding (7) FUNCTION: Probably catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. {ECO:0000250}. +Q9R269 PEPL_MOUSE Periplakin 1755 204,004 Chain (1); Coiled coil (4); Domain (1); Modified residue (6); Repeat (5); Sequence conflict (7) FUNCTION: Component of the cornified envelope of keratinocytes. May link the cornified envelope to desmosomes and intermediate filaments. May act as a localization signal in PKB/AKT-mediated signaling. SUBCELLULAR LOCATION: Cell junction, desmosome. Cytoplasm, cytoskeleton. Cell membrane. Nucleus. Mitochondrion. Note=Associated with desmosomes and intermediate filaments. SUBUNIT: Homodimer or a heterodimer with EVPL. Interacts with PPHLN1 and VIM. Binds to the PH domain of AKT1. Interacts with FCGR1A (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Upper granular cell layer of dorsal lip and tongue, palate and dorsal epidermis. {ECO:0000269|PubMed:15226441}. +O08674 RBPJL_MOUSE Recombining binding protein suppressor of hairless-like protein (Transcription factor RBP-L) 515 56,780 Chain (1); DNA binding (3); Domain (1) FUNCTION: Putative transcription factor, which cooperates with EBNA2 to activate transcription. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9111338}. SUBUNIT: Interacts weakly with EBNA2. Does not interact with any Notch proteins. {ECO:0000269|PubMed:9111338}. TISSUE SPECIFICITY: Highly expressed in lung. Also detected in spleen, and brain. {ECO:0000269|PubMed:9111338}. +Q7TSV4 PGM2_MOUSE Phosphoglucomutase-2 (PGM 2) (EC 5.4.2.2) (Glucose phosphomutase 2) (Phosphodeoxyribomutase) (Phosphoglucomutase-1) (Phosphopentomutase) (EC 5.4.2.7) 620 68,748 Active site (1); Binding site (4); Chain (1); Metal binding (4); Modified residue (1); Region (3) Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 1/2. FUNCTION: Catalyzes the conversion of the nucleoside breakdown products ribose-1-phosphate and deoxyribose-1-phosphate to the corresponding 5-phosphopentoses. May also catalyze the interconversion of glucose-1-phosphate and glucose-6-phosphate. Has low glucose 1,6-bisphosphate synthase activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in lung, spleen and thymus. Expressed at lower levels in liver, brain, kidney, skeletal muscle, testis and heart. {ECO:0000269|PubMed:17804405}. +Q9QWH1 PHC2_MOUSE Polyhomeotic-like protein 2 (mPH2) (Early development regulatory protein 2) (p36) 850 89,799 Alternative sequence (1); Beta strand (2); Chain (1); Compositional bias (2); Cross-link (5); Domain (1); Helix (1); Modified residue (3); Motif (1); Region (2); Turn (1); Zinc finger (1) FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. {ECO:0000269|PubMed:16024804}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8IXK0}. SUBUNIT: Component of a PRC1-like complex. Interacts with CBX4 (By similarity). Interacts with BMI1, PCGF2, PHC1 and RNF2 (PubMed:9627119, PubMed:16024804, PubMed:27827373). Interacts with CHTOP (PubMed:22872859). Interacts with the N-terminal region of the SP1 transcription factor and with MAPKAPK2 (By similarity). {ECO:0000250|UniProtKB:Q8IXK0, ECO:0000269|PubMed:16024804, ECO:0000269|PubMed:22872859, ECO:0000269|PubMed:27827373, ECO:0000269|PubMed:9627119}. DOMAIN: HD1 motif interacts with SAM domain of PHC1. {ECO:0000269|PubMed:12034499}. TISSUE SPECIFICITY: Isoform 2 is ubiquitously expressed in embryos and adult tissues at much higher level than isoform 1. {ECO:0000269|PubMed:12034499}. +Q8BLG0 PHF20_MOUSE PHD finger protein 20 (Hepatocellular carcinoma-associated antigen 58 homolog) 1010 115,280 Alternative sequence (1); Chain (1); Compositional bias (3); DNA binding (1); Disulfide bond (2); Domain (2); Modified residue (4); Mutagenesis (2); Sequence conflict (1); Zinc finger (2) FUNCTION: Contributes to methyllysine-dependent p53/TP53 stabilization and up-regulation after DNA damage (By similarity). Methyllysine-binding protein, component of the MOF histone acetyltransferase protein complex. Not required for maintaining the global histone H4 'Lys-16' acetylation (H4K16ac) levels or locus specific histone acetylation, but instead works downstream in transcriptional regulation of MOF target genes. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. {ECO:0000250, ECO:0000269|PubMed:22072714}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22072714}. SUBUNIT: Homodimer; disulfide-linked. Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Component of the NSL complex at least composed of MOF/KAT8, KANSL1, KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT, WDR5 and HCFC1 (By similarity). {ECO:0000250}. DOMAIN: The Tudor domain 2 mediates reading of dimethyl-lysine residues.; DOMAIN: The Tudor domain 1 doesn't bind dimethyl-lysine residues, due to an atypical and occluded aromatic cage. {ECO:0000250}. +P70669 PHEX_MOUSE Phosphate-regulating neutral endopeptidase PHEX (Metalloendopeptidase homolog PEX) (EC 3.4.24.-) (Phosphate regulating neutral endopeptidase) (Vitamin D-resistant hypophosphatemic rickets protein) (X-linked hypophosphatemia protein) (HYP) 749 86,419 Active site (2); Chain (1); Glycosylation (8); Metal binding (3); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 21 37 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 20 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 38 749 Extracellular. {ECO:0000255}. FUNCTION: Peptidase that cleaves SIBLING (small integrin-binding ligand, N-linked glycoprotein)-derived ASARM peptides, thus regulating their biological activity (By similarity). Cleaves ASARM peptides between Ser and Glu or Asp residues (By similarity). Regulates osteogenic cell differentiation and bone mineralization through the cleavage of the MEPE-derived ASARM peptide (PubMed:11159866, PubMed:18597632, PubMed:26051469). Promotes dentin mineralization and renal phosphate reabsorption by cleaving DMP1- and MEPE-derived ASARM peptides (PubMed:26051469). Inhibits the cleavage of MEPE by CTSB/cathepsin B thus preventing MEPE degradation (By similarity). {ECO:0000250|UniProtKB:P78562, ECO:0000269|PubMed:11159866, ECO:0000269|PubMed:26051469, ECO:0000305|PubMed:18597632}. PTM: N-glycosylated. {ECO:0000269|PubMed:11811562}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11811562}; Single-pass type II membrane protein {ECO:0000305}. SUBUNIT: Interacts with MEPE; the interaction is zinc-dependent (via ASARM motif). {ECO:0000250|UniProtKB:P78562}. TISSUE SPECIFICITY: Expressed in bone, specifically in the osteoid and in osteocytes (PubMed:11159866, PubMed:18597632). Expressed in teeth, specifically in odontoblasts and ameloblasts (PubMed:11811562). Expressed moderately by macrophages in the liver and has minimal expression in brown adipose tissue (PubMed:11811562). Also expressed in suprabasal layers of the skin (PubMed:11811562). {ECO:0000269|PubMed:11159866, ECO:0000269|PubMed:11811562, ECO:0000269|PubMed:18597632}. +Q9DB30 PHKG2_MOUSE Phosphorylase b kinase gamma catalytic chain, liver/testis isoform (PHK-gamma-LT) (PHK-gamma-T) (EC 2.7.11.19) (Phosphorylase kinase subunit gamma-2) 406 46,572 Active site (1); Binding site (1); Chain (1); Domain (1); Nucleotide binding (1); Region (2); Sequence conflict (1) FUNCTION: Catalytic subunit of the phosphorylase b kinase (PHK), which mediates the neural and hormonal regulation of glycogen breakdown (glycogenolysis) by phosphorylating and thereby activating glycogen phosphorylase. May regulate glycogeneolysis in the testis. In vitro, phosphorylates PYGM (By similarity). {ECO:0000250}. SUBUNIT: Hexadecamer of 4 heterotetramers, each composed of alpha, beta, gamma, and delta subunits. Alpha (PHKA1 or PHKA2) and beta (PHKB) are regulatory subunits, gamma (PHKG1 or PHKG2) is the catalytic subunit, and delta is calmodulin (By similarity). {ECO:0000250}. +Q9QY39 PDZD4_MOUSE PDZ domain-containing protein 4 (PDZ domain-containing RING finger protein 4-like protein) 772 86,819 Chain (1); Coiled coil (1); Domain (1); Erroneous initiation (1); Modified residue (2) SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000250}. Note=Mainly localized under the plasma membrane. {ECO:0000250}. +Q8CIW5 PEO1_MOUSE Twinkle protein, mitochondrial (EC 3.6.4.12) (Progressive external ophthalmoplegia 1 protein homolog) (T7 gp4-like protein with intramitochondrial nucleoid localization) (T7-like mitochondrial DNA helicase) (Twinkle mtDNA helicase) 685 76,993 Alternative sequence (2); Chain (1); Coiled coil (1); Domain (1); Nucleotide binding (1); Transit peptide (1) FUNCTION: Involved in mitochondrial DNA (mtDNA) metabolism. Could function as an adenine nucleotide-dependent DNA helicase. Function infered to be critical for lifetime maintenance of mtDNA integrity. May be a key regulator of mtDNA copy number in mammals. {ECO:0000269|PubMed:15509589}. SUBCELLULAR LOCATION: Mitochondrion matrix, mitochondrion nucleoid {ECO:0000250}. Note=Colocalizes with mtDNA in mitochondrial nucleoids, a nucleoproteins complex consisting of a number of copies of proteins associated with mtDNA, probably involved in mtDNA maintenance and expression. {ECO:0000250}. SUBUNIT: Forms multimers in vitro, including hexamers. Interacts with LONP1. {ECO:0000250|UniProtKB:Q96RR1}. TISSUE SPECIFICITY: Ubiquitous with the highest levels in the liver, heart and kidneys. The skeletal muscle, brain and testis showed lower but detectable expression. Expression is coregulated with MRPL43. {ECO:0000269|PubMed:15509589}. +Q6P1Z5 PED1A_MOUSE PC-esterase domain-containing protein 1A (Protein FAM113A) 449 51,311 Chain (1); Compositional bias (2); Sequence conflict (2) +Q8BGX1 PED1B_MOUSE PC-esterase domain-containing protein 1B (Protein FAM113B) 433 49,968 Chain (1); Compositional bias (1); Sequence conflict (2) +P97298 PEDF_MOUSE Pigment epithelium-derived factor (PEDF) (Caspin) (Serpin F1) (Stromal cell-derived factor 3) (SDF-3) 417 46,234 Chain (1); Glycosylation (1); Modified residue (2); Sequence conflict (5); Signal peptide (1) FUNCTION: Neurotrophic protein; induces extensive neuronal differentiation in retinoblastoma cells. Potent inhibitor of angiogenesis. As it does not undergo the S (stressed) to R (relaxed) conformational transition characteristic of active serpins, it exhibits no serine protease inhibitory activity. {ECO:0000269|PubMed:12632345}. SUBCELLULAR LOCATION: Secreted. Melanosome {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in the liver, gastric glandular mucosa and renal tubules. It is also expressed in the brain, heart, lung retina and testes. {ECO:0000269|PubMed:9565647, ECO:0000269|PubMed:9614124}. +O09012 PEX5_MOUSE Peroxisomal targeting signal 1 receptor (PTS1 receptor) (PTS1R) (PTS1-BP) (PXR1P) (Peroxin-5) (Peroxisomal C-terminal targeting signal import receptor) (Peroxisome receptor 1) 639 70,756 Alternative sequence (1); Chain (1); Cross-link (1); Modified residue (5); Repeat (7); Sequence conflict (9) FUNCTION: Binds to the C-terminal PTS1-type tripeptide peroxisomal targeting signal (SKL-type) and plays an essential role in peroxisomal protein import. {ECO:0000250|UniProtKB:Q920N5}. PTM: Monoubiquitination at Cys-11 is required for proper export from peroxisomes and recycling. {ECO:0000250|UniProtKB:Q920N5}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q920N5}. Peroxisome membrane {ECO:0000250|UniProtKB:Q920N5}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q920N5}. Note=Its distribution appears to be dynamic. It is probably a cycling receptor found mainly in the cytoplasm and as well associated to the peroxisomal membrane through a docking factor (PEX13). SUBUNIT: Interacts with PEX7, PEX12, PEX13 and PEX14. Interacts (Cys-linked ubiquitinated) with ZFAND6 (By similarity). Interacts with VWA8 in a PEX7-dependent manner (By similarity). {ECO:0000250|UniProtKB:P50542, ECO:0000250|UniProtKB:Q920N5}. +Q9CWM4 PFD1_MOUSE Prefoldin subunit 1 122 14,255 Chain (1); Initiator methionine (1); Modified residue (1) FUNCTION: Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins (By similarity). {ECO:0000250}. SUBUNIT: Heterohexamer of two PFD-alpha type and four PFD-beta type subunits. {ECO:0000250}. +O35129 PHB2_MOUSE Prohibitin-2 (B-cell receptor-associated protein BAP37) (Repressor of estrogen receptor activity) 299 33,296 Chain (1); Coiled coil (1); Initiator methionine (1); Modified residue (8); Region (2); Sequence conflict (7) FUNCTION: Acts as a mediator of transcriptional repression by nuclear hormone receptors via recruitment of histone deacetylases. Functions as an estrogen receptor (ER)-selective coregulator that potentiates the inhibitory activities of antiestrogens and represses the activity of estrogens. Competes with NCOA1 for modulation of ER transcriptional activity. Probably involved in regulating mitochondrial respiration activity and in aging. {ECO:0000250|UniProtKB:Q99623, ECO:0000269|PubMed:12878603, ECO:0000269|PubMed:15140878}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:11302691}. Cytoplasm {ECO:0000269|PubMed:15140878}. Nucleus {ECO:0000269|PubMed:15140878}. SUBUNIT: Interacts with PHB (PubMed:11302691). Interacts with ESR1, HDAC1 and HDAC5 (PubMed:12878603, PubMed:15140878). Interacts with ZNF703 (By similarity). Interacts with STOML2 (By similarity). Interacts with ARFGEF3 (By similarity). {ECO:0000250|UniProtKB:Q99623, ECO:0000269|PubMed:11302691, ECO:0000269|PubMed:12878603, ECO:0000269|PubMed:15140878}. TISSUE SPECIFICITY: Widely expressed in different tissues. {ECO:0000269|PubMed:11302691, ECO:0000269|PubMed:15140878, ECO:0000269|PubMed:8070406}. +Q8K2W6 PHF13_MOUSE PHD finger protein 13 296 33,424 Chain (1); Motif (1); Region (1); Zinc finger (1) FUNCTION: Modulates chromatin structure. Required for normal chromosome condensation during the early stages of mitosis. Required for normal chromosome separation during mitosis (By similarity). {ECO:0000250}. PTM: Subject to proteasomal degradation. Stable when bound to chromatin. The soluble form is rapidly degraded (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Note=Predominantly bound to chromatin, but a minor proportion is also detected in the nucleoplasm. {ECO:0000250}. SUBUNIT: Interacts with histone H3 that is trimethylated at 'Lys-4' (H3K4me3). Interacts with GSK3B (By similarity). {ECO:0000250}. +Q9D4H9 PHF14_MOUSE PHD finger protein 14 881 99,105 Alternative sequence (2); Chain (1); Compositional bias (1); Erroneous initiation (1); Modified residue (17); Sequence conflict (1); Zinc finger (4) +Q8BSN5 PHF23_MOUSE PHD finger protein 23 (PDH-containing protein JUNE-1) 401 43,547 Alternative sequence (2); Chain (1); Compositional bias (1); Erroneous initiation (2); Modified residue (8); Sequence conflict (3); Zinc finger (1) FUNCTION: Acts as a negative regulator of autophagy, through promoting ubiquitination and degradation of LRSAM1, an E3 ubiquitin ligase that promotes autophagy in response to starvation or infecting bacteria. {ECO:0000250|UniProtKB:Q9BUL5}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BUL5}. Cytoplasm {ECO:0000250|UniProtKB:Q9BUL5}. Note=Mainly present in the nucleus and part in the cytoplasm. {ECO:0000250|UniProtKB:Q9BUL5}. SUBUNIT: Interacts with LRSAM1. {ECO:0000250|UniProtKB:Q9BUL5}. DOMAIN: The PHD-type zinc-finger domain is required for interaction with LRSAM1 and negative regulation of autophagy. {ECO:0000250|UniProtKB:Q9BUL5}. +Q5BL07 PEX1_MOUSE Peroxisome biogenesis factor 1 (Peroxin-1) 1284 141,428 Alternative sequence (1); Beta strand (13); Chain (1); Helix (4); Modified residue (3); Mutagenesis (2); Nucleotide binding (2) FUNCTION: Required for stability of PEX5 and protein import into the peroxisome matrix. Anchored by PEX26 to peroxisome membranes, possibly to form heteromeric AAA ATPase complexes required for the import of proteins into peroxisomes (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Peroxisome membrane {ECO:0000250}. Note=Associated with peroxisomal membranes. {ECO:0000250}. SUBUNIT: Interacts directly with PEX6. Interacts indirectly with PEX26, via its interaction with PEX6 (By similarity). {ECO:0000250}. DOMAIN: The N-terminal domain shows evolutionary conservation with that of VCP, and is able to bind phospholipids with a preference for phosphatidylinositol monophosphates. +Q9QXY9 PEX3_MOUSE Peroxisomal biogenesis factor 3 (Peroxin-3) (Peroxisomal assembly protein PEX3) 372 42,224 Chain (1); Region (2); Topological domain (3); Transmembrane (2) TRANSMEM 16 36 Helical. {ECO:0000255}.; TRANSMEM 117 140 Helical. {ECO:0000255}. TOPO_DOM 1 15 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 37 116 Peroxisomal. {ECO:0000255}.; TOPO_DOM 141 372 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in peroxisome biosynthesis and integrity. Assembles membrane vesicles before the matrix proteins are translocated. As a docking factor for PEX19, is necessary for the import of peroxisomal membrane proteins in the peroxisomes. {ECO:0000250|UniProtKB:P56589}. SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000250|UniProtKB:P56589}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Interacts with PEX19. {ECO:0000250|UniProtKB:P56589}. TISSUE SPECIFICITY: Identified in all tissues analyzed, with the strongest expression in liver and in testis. +Q61282 PGCA_MOUSE Aggrecan core protein (Cartilage-specific proteoglycan core protein) (CSPCP) 2132 221,941 Chain (1); Disulfide bond (14); Domain (7); Glycosylation (9); Metal binding (13); Motif (1); Region (9); Sequence conflict (9); Signal peptide (1) FUNCTION: This proteoglycan is a major component of extracellular matrix of cartilagenous tissues. A major function of this protein is to resist compression in cartilage. It binds avidly to hyaluronic acid via an N-terminal globular region. May play a regulatory role in the matrix assembly of the cartilage. PTM: Contains mostly chondroitin sulfate, but also keratan sulfate chains, N-linked and O-linked oligosaccharides. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. SUBUNIT: Interacts with COMP (By similarity). Interacts with FBLN1. {ECO:0000250, ECO:0000269|PubMed:10400671}. DOMAIN: Two globular domains, G1 and G2, comprise the N-terminus of the proteoglycan, while another globular region, G3, makes up the C-terminus. G1 contains Link domains and thus consists of three disulfide-bonded loop structures designated as the A, B, B' motifs. G2 is similar to G1. The keratan sulfate (KS) and the chondroitin sulfate (CS) attachment domains lie between G2 and G3. TISSUE SPECIFICITY: Specifically expressed in cartilage tissues. {ECO:0000269|PubMed:7524681}. DISEASE: Note=Defects in Acan are the cause of cartilage matrix deficiency (CMD). CMD is an autosomal recessive syndrome characterized by cleft palate, short limbs, tail and snout. Mutation in strain CMD causes absence of aggrecan by truncation of the protein (mutation in the G1 domain). +Q3UUQ7 PGAP1_MOUSE GPI inositol-deacylase (EC 3.1.-.-) (Post-GPI attachment to proteins factor 1) 922 104,578 Active site (1); Alternative sequence (2); Chain (1); Glycosylation (3); Sequence conflict (2); Topological domain (9); Transmembrane (8) TRANSMEM 12 32 Helical. {ECO:0000255}.; TRANSMEM 598 618 Helical. {ECO:0000255}.; TRANSMEM 642 662 Helical. {ECO:0000255}.; TRANSMEM 669 689 Helical. {ECO:0000255}.; TRANSMEM 695 715 Helical. {ECO:0000255}.; TRANSMEM 734 754 Helical. {ECO:0000255}.; TRANSMEM 818 838 Helical. {ECO:0000255}.; TRANSMEM 895 915 Helical. {ECO:0000255}. TOPO_DOM 1 11 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 33 597 Lumenal. {ECO:0000255}.; TOPO_DOM 619 641 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 663 668 Lumenal. {ECO:0000255}.; TOPO_DOM 690 694 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 716 733 Lumenal. {ECO:0000255}.; TOPO_DOM 755 817 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 839 894 Lumenal. {ECO:0000255}.; TOPO_DOM 916 922 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in inositol deacylation of GPI-anchored proteins. GPI inositol deacylation may important for efficient transport of GPI-anchored proteins from the endoplasmic reticulum to the Golgi (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +P22437 PGH1_MOUSE Prostaglandin G/H synthase 1 (EC 1.14.99.1) (Cyclooxygenase-1) (COX-1) (Prostaglandin H2 synthase 1) (PGH synthase 1) (PGHS-1) (PHS 1) (Prostaglandin-endoperoxide synthase 1) 602 69,042 Active site (2); Chain (1); Disulfide bond (5); Domain (1); Glycosylation (3); Metal binding (1); Signal peptide (1); Site (1) Lipid metabolism; prostaglandin biosynthesis. FUNCTION: Converts arachidonate to prostaglandin H2 (PGH2), a committed step in prostanoid synthesis. Involved in the constitutive production of prostanoids in particular in the stomach and platelets. In gastric epithelial cells, it is a key step in the generation of prostaglandins, such as prostaglandin E2 (PGE2), which plays an important role in cytoprotection. In platelets, it is involved in the generation of thromboxane A2 (TXA2), which promotes platelet activation and aggregation, vasoconstriction and proliferation of vascular smooth muscle cells. SUBCELLULAR LOCATION: Microsome membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Peripheral membrane protein. SUBUNIT: Homodimer. +P28653 PGS1_MOUSE Biglycan (Bone/cartilage proteoglycan I) (PG-S1) 369 41,639 Chain (1); Compositional bias (1); Disulfide bond (3); Glycosylation (4); Propeptide (1); Repeat (12); Sequence conflict (1); Signal peptide (1) FUNCTION: May be involved in collagen fiber assembly. {ECO:0000250}. PTM: The two attached glycosaminoglycan chains can be either chondroitin sulfate or dermatan sulfate. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. TISSUE SPECIFICITY: Found in several connective tissues, especially in articular cartilages. +Q62392 PHLA1_MOUSE Pleckstrin homology-like domain family A member 1 (Proline- and glutamine-rich protein) (PQ-rich protein) (PQR protein) (T-cell death-associated gene 51 protein) 405 45,583 Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (2); Frameshift (1); Region (2); Sequence conflict (1) FUNCTION: Seems to be involved in regulation of apoptosis. May be involved in detachment-mediated programmed cell death. May mediate apoptosis during neuronal development. May be involved in regulation of anti-apoptotic effects of IGF1. Required for TCR-induced apoptosis and expression of TNFRSF6/FAS in a T-cell hybridoma cell line. May be involved in translational regulation. {ECO:0000269|PubMed:15037619, ECO:0000269|PubMed:8673705}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8WV24}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q8WV24}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q8WV24}. Note=Colocalizes with intracellular vesicles. {ECO:0000250|UniProtKB:Q8WV24}. SUBUNIT: Interacts with RPL14, EIF3S7 and PABPC4. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed with very high levels in adult liver and high levels in adult lung. According to PubMed:10428057 expressed at low levels in liver. Expressed at increased levels in atherosclerotic lesions observed in hyperhomocysteinema. {ECO:0000269|PubMed:10428057, ECO:0000269|PubMed:10594239, ECO:0000269|PubMed:12738777}. +Q9WTU0 PHF2_MOUSE Lysine-specific demethylase PHF2 (EC 1.14.11.-) (GRC5) (PHD finger protein 2) 1096 120,814 Binding site (5); Chain (1); Compositional bias (2); Cross-link (1); Domain (1); Metal binding (3); Modified residue (16); Sequence conflict (2); Zinc finger (1) FUNCTION: Lysine demethylase that demethylates both histones and non-histone proteins. Enzymatically inactive by itself, and becomes active following phosphorylation by PKA: forms a complex with ARID5B and mediates demethylation of methylated ARID5B. Demethylation of ARID5B leads to target the PHF2-ARID5B complex to target promoters, where PHF2 mediates demethylation of dimethylated 'Lys-9' of histone H3 (H3K9me2), followed by transcription activation of target genes. The PHF2-ARID5B complex acts as a coactivator of HNF4A in liver. PHF2 is recruited to trimethylated 'Lys-4' of histone H3 (H3K4me3) at rDNA promoters and promotes expression of rDNA (By similarity). {ECO:0000250}. PTM: Phosphorylated by PKA on specific serine residues, leading to the formation of an active lysine demethylase complex. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:O75151}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:O75151}. SUBUNIT: Component of the PHF2-ARID5B complex, at least composed of PHF2 and ARID5B. Interacts with HNF4A and NR1H4 (By similarity). {ECO:0000250}. DOMAIN: The PHD-type zinc finger mediates the binding to H3K4me2 and H3K4me3. {ECO:0000250}. +P09922 MX1_MOUSE Interferon-induced GTP-binding protein Mx1 (Influenza resistance protein) (Myxoma resistance protein 1) (Myxovirus resistance protein 1) 631 72,038 Chain (1); Domain (2); Mutagenesis (2); Nucleotide binding (3); Region (9) FUNCTION: Interferon-induced dynamin-like GTPase with antiviral activity against influenza A virus, (IAV), influenza B virus (IBV) and Thogoto virus (THOV). Inhibits FLUAV by interfering with the process of primary transcription, probably by affecting the viral polymerase function. {ECO:0000269|PubMed:17652381, ECO:0000269|PubMed:21651940}. PTM: ISGylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21859714}. Nucleus {ECO:0000269|PubMed:21859714}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P20591}; Peripheral membrane protein {ECO:0000250|UniProtKB:P20591}; Cytoplasmic side {ECO:0000250|UniProtKB:P20591}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P20591}. Note=Binds preferentially to negatively charged phospholipids. Colocalizes with CCHFV protein N in the perinuclear region. {ECO:0000250|UniProtKB:P20591}. SUBUNIT: Homooligomer. Oligomerizes into multimeric filamentous or ring-like structures by virtue of its stalk domain. Oligomerization is critical for GTPase activity, protein stability, and recognition of viral target structures (By similarity). Interacts with TRPC1, TRPC3, TRPC4, TRPC5, TRPC6 and TRPC7 (By similarity). Interacts with HSPA5 (By similarity). Interacts with TUBB/TUBB5 (By similarity). Interacts with DDX39A and DDX39B. {ECO:0000250, ECO:0000269|PubMed:21859714}. DOMAIN: The C-terminal GTPase effector domain (GED) is involved in oligomerization and viral target recognition. {ECO:0000250}.; DOMAIN: The middle domain mediates self-assembly and oligomerization. {ECO:0000250}. +O35682 MYADM_MOUSE Myeloid-associated differentiation marker (Myeloid up-regulated protein) 320 35,285 Chain (1); Domain (2); Frameshift (1); Sequence conflict (1); Transmembrane (8) TRANSMEM 35 55 Helical. {ECO:0000255}.; TRANSMEM 61 81 Helical. {ECO:0000255}.; TRANSMEM 95 115 Helical. {ECO:0000255}.; TRANSMEM 131 151 Helical. {ECO:0000255}.; TRANSMEM 165 185 Helical. {ECO:0000255}.; TRANSMEM 197 217 Helical. {ECO:0000255}.; TRANSMEM 233 253 Helical. {ECO:0000255}.; TRANSMEM 292 312 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +P27573 MYP0_MOUSE Myelin protein P0 (Myelin peripheral protein) (MPP) (Myelin protein zero) 248 27,622 Chain (1); Disulfide bond (1); Domain (1); Glycosylation (1); Modified residue (6); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 154 179 Helical. {ECO:0000250}. TOPO_DOM 30 153 Extracellular. {ECO:0000250}.; TOPO_DOM 180 248 Cytoplasmic. {ECO:0000250}. FUNCTION: Is an adhesion molecule necessary for normal myelination in the peripheral nervous system. It mediates adhesion between adjacent myelin wraps and ultimately drives myelin compaction. {ECO:0000250|UniProtKB:P25189}. PTM: N-glycosylated; contains sulfate-substituted glycan. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P25189}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P25189}. SUBUNIT: Homodimer and homotetramer. {ECO:0000250}. TISSUE SPECIFICITY: Found only in peripheral nervous system Schwann cells. +Q5XKE0 MYPC2_MOUSE Myosin-binding protein C, fast-type (Fast MyBP-C) (C-protein, skeletal muscle fast isoform) 1136 127,352 Beta strand (14); Chain (1); Domain (10); Sequence conflict (3); Turn (1) FUNCTION: Thick filament-associated protein located in the crossbridge region of vertebrate striated muscle a bands. In vitro it binds MHC, F-actin and native thin filaments, and modifies the activity of actin-activated myosin ATPase. It may modulate muscle contraction or may play a more structural role (By similarity). {ECO:0000250}. +Q9D8I1 MZB1_MOUSE Marginal zone B- and B1-cell-specific protein (Plasma cell-induced resident endoplasmic reticulum protein) (Plasma cell-induced resident ER protein) (pERp1) (Proapoptotic caspase adapter protein) 188 20,580 Chain (1); Disulfide bond (3); Motif (1); Mutagenesis (6); Sequence conflict (6); Signal peptide (1) FUNCTION: Associates with immunoglobulin M (IgM) heavy and light chains and promotes IgM assembly and secretion. May exert its effect by acting as a molecular chaperone or as an oxidoreductase as it displays a low level of oxidoreductase activity. Helps to diversify peripheral B-cell functions by regulating Ca(2+) stores, antibody secretion and integrin activation.; FUNCTION: Acts as a hormone-regulated adipokine/proinflammatory cytokine that is implicated in causing chronic inflammation, affecting cellular expansion and blunting insulin response in adipocytes. May have a role in the onset of insulin resistance. PTM: Forms an interchain disulfide bond with IgM monomers. SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:19805154}. Endoplasmic reticulum lumen {ECO:0000269|PubMed:21093319}. Secreted {ECO:0000269|PubMed:21688198}. SUBUNIT: Part of the ER chaperone complex, a multi-protein complex in the endoplasmic reticulum containing a large number of molecular chaperones which associates with unassembled incompletely folded immunoglobulin heavy chains. Interacts with HSP90B1 and PDIA3 in a calcium-dependent manner. {ECO:0000269|PubMed:19805157, ECO:0000269|PubMed:21093319}. TISSUE SPECIFICITY: Expressed predominantly in the spleen and lymph nodes. Abundantly expressed in marginal zone B and B1 cells. High expression in mesenteric adipose tissue (MAT). Expressed also in pancreas, perigonadal adipose tissue (PAT), uterus, subcutaneous adipose tissue, heart, muscle, ovary and liver. Very low expression is detected in brown adipose tissue. In PAT, significantly higher expression in stromal-vascular cell than in adipocytes. Expressed in macrophage RAW 264.7 cell line. Down-regulated in For-knockout female MAT at 5 months (obese state) followed by steep up-regulation at 9 months (prediabetic condition) when mutants progress towards the metabolic syndrome. {ECO:0000269|PubMed:19805154, ECO:0000269|PubMed:21093319, ECO:0000269|PubMed:21688198}. +Q99MZ6 MYO7B_MOUSE Unconventional myosin-VIIb 2113 240,859 Beta strand (18); Chain (1); Domain (13); Helix (20); Modified residue (4); Nucleotide binding (1); Region (3); Sequence conflict (2); Turn (7) FUNCTION: Myosins are actin-based motor molecules with ATPase activity. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments. As part of the intermicrovillar adhesion complex/IMAC plays a role in epithelial brush border differentiation, controlling microvilli organization and length. May link the complex to the actin core bundle of microvilli. {ECO:0000250|UniProtKB:Q6PIF6}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305|PubMed:11401444}. Cell projection, microvillus {ECO:0000269|PubMed:11401444, ECO:0000269|PubMed:24725409}. Note=Enriched in the microvilli of the intestinal brush border. {ECO:0000269|PubMed:11401444, ECO:0000269|PubMed:24725409}. SUBUNIT: Part of the IMAC/intermicrovillar adhesion complex/intermicrovillar tip-link complex composed of ANKS4B, MYO7B, USH1C, CDHR2 and CDHR5. Interacts with CDHR2. Interacts with CDHR5. Interacts with USH1C (By similarity). Interacts with ANKS4B; requires initial interaction with USH1C (Probable). {ECO:0000250|UniProtKB:Q6PIF6, ECO:0000305|PubMed:26812017}. TISSUE SPECIFICITY: Expressed primarily in kidney and intestine. Detected in proximal tubule cells of the kidney and enterocytes of the intestine, specifically the distal tips of apical microvilli on these transporting epithelial cells (at protein level). {ECO:0000269|PubMed:11401444, ECO:0000269|PubMed:24725409}. +P70248 MYO1F_MOUSE Unconventional myosin-If 1099 125,947 Chain (1); Domain (4); Modified residue (1); Nucleotide binding (1); Region (1) FUNCTION: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in liver, kidney, spleen, eye, brain, lung, small intestine, testis and cochlea. Barely detectable in heart. {ECO:0000269|PubMed:9119401}. +Q9EQ61 PESC_MOUSE Pescadillo homolog 584 67,796 Chain (1); Compositional bias (1); Cross-link (2); Domain (1); Modified residue (1); Region (4) FUNCTION: Component of the PeBoW complex, which is required for maturation of 28S and 5.8S ribosomal RNAs and formation of the 60S ribosome. {ECO:0000255|HAMAP-Rule:MF_03028, ECO:0000269|PubMed:15225545, ECO:0000269|PubMed:17308336}. PTM: Sumoylated. {ECO:0000255|HAMAP-Rule:MF_03028}. SUBCELLULAR LOCATION: Nucleus, nucleolus. Nucleus, nucleoplasm. Chromosome. Note=Appears to localize to the periphery of metaphase chromosomes during mitosis and to the prenucleolar bodies that form in mitotic cells prior to the actual nucleoli. SUBUNIT: Component of the PeBoW complex, composed of BOP1, PES1 and WDR12 (PubMed:15225545). The complex is held together by BOP1, which interacts with PES1 via its N-terminal domain and with WDR12 via a high-affinity interaction between the seven-bladed beta-propeller domains of the 2 proteins. The PeBoW complex associates with the 66S pre-ribosome (By similarity). The PeBoW complex also associates with DDX27, PES1 interacts directly with DDX27 (By similarity). Interacts with IRS1 and UBTF (PubMed:15169904). May interact with MAP1B (PubMed:17308336). {ECO:0000255|HAMAP-Rule:MF_03028, ECO:0000269|PubMed:15169904, ECO:0000269|PubMed:15225545, ECO:0000269|PubMed:17308336}. TISSUE SPECIFICITY: Ubiquitous. Highest levels appear to be found in tissues that contain a population of proliferating cells, such as ovary and testis. Also appears to be highly expressed in kidney and liver. In the brain expression is restricted to neural progenitor cells and postmitotic neurons. Highly expressed in malignant astrocytes. {ECO:0000269|PubMed:11112348, ECO:0000269|PubMed:12237316}. +Q6PHQ8 NAA35_MOUSE N-alpha-acetyltransferase 35, NatC auxiliary subunit (Embryonic growth-associated protein) (Protein MAK10 homolog) 725 83,306 Chain (1); Modified residue (1); Sequence caution (1); Sequence conflict (3) FUNCTION: Auxillary component of the N-terminal acetyltransferase C (NatC) complex which catalyzes acetylation of N-terminal methionine residues. Involved in regulation of apoptosis and proliferation of smooth muscle cells. {ECO:0000269|PubMed:16484612}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16484612}. SUBUNIT: Component of the N-terminal acetyltransferase C (NatC) complex, which is composed of NAA35, NAA38 and NAA30. +Q8K596 NAC2_MOUSE Sodium/calcium exchanger 2 (Na(+)/Ca(2+)-exchange protein 2) (Solute carrier family 8 member 2) 921 100,711 Alternative sequence (1); Chain (1); Domain (2); Glycosylation (2); Metal binding (26); Modified residue (1); Region (1); Sequence conflict (2); Signal peptide (1); Transmembrane (11) TRANSMEM 69 89 Helical. {ECO:0000255}.; TRANSMEM 131 151 Helical. {ECO:0000255}.; TRANSMEM 165 185 Helical. {ECO:0000255}.; TRANSMEM 197 217 Helical. {ECO:0000255}.; TRANSMEM 226 246 Helical. {ECO:0000255}.; TRANSMEM 721 741 Helical. {ECO:0000255}.; TRANSMEM 749 769 Helical. {ECO:0000255}.; TRANSMEM 786 806 Helical. {ECO:0000255}.; TRANSMEM 823 843 Helical. {ECO:0000255}.; TRANSMEM 855 875 Helical. {ECO:0000255}.; TRANSMEM 893 913 Helical. {ECO:0000255}. FUNCTION: Mediates the electrogenic exchange of Ca(2+) against Na(+) ions across the cell membrane, and thereby contributes to the regulation of cytoplasmic Ca(2+) levels and Ca(2+)-dependent cellular processes. Contributes to cellular Ca(2+) homeostasis in excitable cells. Contributes to the rapid decrease of cytoplasmic Ca(2+) levels back to baseline after neuronal activation, and thereby contributes to modulate synaptic plasticity, learning and memory (PubMed:12818181). Plays a role in regulating urinary Ca(2+) and Na(+) excretion (PubMed:25498502). {ECO:0000269|PubMed:12818181}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12818181}; Multi-pass membrane protein {ECO:0000305}. Basolateral cell membrane {ECO:0000269|PubMed:25498502}; Multi-pass membrane protein {ECO:0000305}. DOMAIN: The cytoplasmic Calx-beta domains bind the regulatory Ca(2+). The first Calx-beta domain can bind up to four Ca(2+) ions. The second domain can bind another two Ca(2+) ions that are essential for calcium-regulated ion exchange. {ECO:0000250|UniProtKB:P23685}. TISSUE SPECIFICITY: Detected in kidney cortex, in distal convoluted tubules and connecting segments (PubMed:25498502). Detected in brain and spinal cord (at protein level) (PubMed:12818181). Detected in brain, especially in hippocampus CA1, CA2 and CA3 fiels, dentate gyrus, cerebellum and brain cortex (PubMed:12818181). {ECO:0000269|PubMed:12818181, ECO:0000269|PubMed:25498502}. +Q711T7 NADE_MOUSE Glutamine-dependent NAD(+) synthetase (EC 6.3.5.1) (NAD(+) synthase [glutamine-hydrolyzing]) (NAD(+) synthetase) (NH3-dependent NAD(+) synthetase-like protein) 725 81,652 Active site (4); Chain (1); Domain (1); Erroneous gene model prediction (1); Nucleotide binding (1); Region (1); Sequence conflict (5) Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (L-Gln route): step 1/1. SUBUNIT: Homohexamer. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in small intestine, kidney, liver and testis. Weakly expressed in skeletal muscle, spleen, lung, heart and brain. {ECO:0000269|PubMed:12547821}. +Q91YL7 PG2IP_MOUSE PGAP2-interacting protein (Cell wall biogenesis protein 43 C-terminal homolog) 699 78,180 Alternative sequence (1); Chain (1); Glycosylation (1); Region (1); Transmembrane (10) TRANSMEM 13 33 Helical. {ECO:0000255}.; TRANSMEM 41 61 Helical. {ECO:0000255}.; TRANSMEM 93 113 Helical. {ECO:0000255}.; TRANSMEM 123 143 Helical. {ECO:0000255}.; TRANSMEM 194 214 Helical. {ECO:0000255}.; TRANSMEM 237 257 Helical. {ECO:0000255}.; TRANSMEM 282 302 Helical. {ECO:0000255}.; TRANSMEM 316 336 Helical. {ECO:0000255}.; TRANSMEM 349 369 Helical. {ECO:0000255}.; TRANSMEM 390 410 Helical. {ECO:0000255}. FUNCTION: Involved in lipid remodeling during GPI-anchor maturation. {ECO:0000269|PubMed:17761529}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Interacts with PGAP2/FRAG1. {ECO:0000269|PubMed:17761529}. +P58058 NADK_MOUSE NAD kinase (EC 2.7.1.23) (Poly(P)/ATP NAD kinase) 439 48,597 Chain (1); Compositional bias (1); Modified residue (5); Sequence conflict (1) +Q3KNK3 NB5R2_MOUSE NADH-cytochrome b5 reductase 2 (b5R.2) (EC 1.6.2.2) 276 31,360 Alternative sequence (1); Chain (1); Domain (1); Modified residue (2); Nucleotide binding (2); Sequence conflict (3) FUNCTION: NADH-cytochrome b5 reductases are involved in desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction. Responsible for NADH-dependent lucigenin chemiluminescence in spermatozoa by reducing both lucigenin and 2-[4-iodophenyl]-3-[4-nitrophenyl]-5-[2,4-disulfophenyl]-2H tetrazolium monosodium salt (WST-1) (By similarity). {ECO:0000250}. +Q3TDX8 NB5R4_MOUSE Cytochrome b5 reductase 4 (EC 1.6.2.2) (Flavohemoprotein b5/b5R) (b5+b5R) (N-terminal cytochrome b5 and cytochrome b5 oxidoreductase domain-containing protein) (cb5/cb5R) 528 59,716 Alternative sequence (1); Chain (1); Domain (3); Erroneous initiation (4); Metal binding (2); Modified residue (1); Natural variant (1); Nucleotide binding (2); Sequence conflict (34) FUNCTION: NADH-cytochrome b5 reductase involved in endoplasmic reticulum stress response pathway. Plays a critical role in protecting pancreatic beta-cells against oxidant stress, possibly by protecting the cell from excess buildup of reactive oxygen species (ROS). {ECO:0000269|PubMed:15247412}. SUBCELLULAR LOCATION: Endoplasmic reticulum. Note=Soluble protein. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed. Isoform 2 is expressed in testis, brain, skeletal muscle and in the male germline. {ECO:0000269|PubMed:14962668, ECO:0000269|PubMed:16814408}. +P97369 NCF4_MOUSE Neutrophil cytosol factor 4 (NCF-4) (Neutrophil NADPH oxidase factor 4) (p40-phox) (p40phox) 339 38,707 Chain (1); Domain (3); Modified residue (2); Region (2); Sequence conflict (3) FUNCTION: Component of the NADPH-oxidase, a multicomponent enzyme system responsible for the oxidative burst in which electrons are transported from NADPH to molecular oxygen, generating reactive oxidant intermediates. It may be important for the assembly and/or activation of the NADPH-oxidase complex. {ECO:0000269|PubMed:8995189}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q15080}. Endosome membrane {ECO:0000250|UniProtKB:Q15080}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q15080}; Cytoplasmic side {ECO:0000250|UniProtKB:Q15080}. Membrane {ECO:0000250|UniProtKB:Q15080}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q15080}. SUBUNIT: Component of an NADPH oxidase complex composed of a heterodimer formed by the membrane proteins CYBA and CYBB and the cytosolic subunits NCF1, NCF2 and NCF4. NCF4 interacts primarily with NCF2 to form a complex with NCF1 (By similarity). {ECO:0000250}. DOMAIN: The PB1 domain mediates the association with NCF2/p67-PHOX. {ECO:0000250}.; DOMAIN: The PX domain mediates interaction with membranes enriched in phosphatidylnositol 3-phosphate. {ECO:0000250}. +Q9ERR1 NDEL1_MOUSE Nuclear distribution protein nudE-like 1 (Protein mNudE-like) (Protein Nudel) (mNudE-L) 345 38,366 Alternative sequence (1); Chain (1); Coiled coil (1); Helix (1); Lipidation (1); Modified residue (6); Mutagenesis (5); Region (9); Sequence conflict (1) FUNCTION: Required for organization of the cellular microtubule array and microtubule anchoring at the centrosome. May regulate microtubule organization at least in part by targeting the microtubule severing protein KATNA1 to the centrosome. Also positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus ends. Required for several dynein- and microtubule-dependent processes such as the maintenance of Golgi integrity, the centripetal motion of secretory vesicles and the coupling of the nucleus and centrosome. Also required during brain development for the migration of newly formed neurons from the ventricular/subventricular zone toward the cortical plate. Plays a role, together with DISC1, in the regulation of neurite outgrowth. Required for mitosis in some cell types but appears to be dispensible for mitosis in cortical neuronal progenitors, which instead requires NDE1. Facilitates the polymerization of neurofilaments from the individual subunits NEFH and NEFL. Positively regulates lysosome peripheral distribution and ruffled border formation in osteoclasts (PubMed:27777970). {ECO:0000269|PubMed:12796778, ECO:0000269|PubMed:15208636, ECO:0000269|PubMed:15473966, ECO:0000269|PubMed:16107726, ECO:0000269|PubMed:16203747, ECO:0000269|PubMed:27777970}. PTM: Phosphorylated by CDK1 and MAPK1 (By similarity). Phosphorylated in mitosis. Phosphorylated by CDK5. Phosphorylation by CDK5 promotes interaction with KATNA1 and YWHAE. {ECO:0000250, ECO:0000269|PubMed:11163259, ECO:0000269|PubMed:12796778, ECO:0000269|PubMed:16203747}.; PTM: Palmitoylation at Cys-273 reduces affinity for dynein. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Chromosome, centromere, kinetochore {ECO:0000250}. Cytoplasm, cytoskeleton, spindle. Note=Localizes to the kinetochore in a CENPF-dependent manner. Colocalizes with DISC1 in the perinuclear region, including the centrosome (By similarity). Localizes to the interphase centrosome and the mitotic spindle. Localizes to the cell body of the motor neurons and colocalizes with assembled neurofilaments within axonal processes. Localizes to the microtubules of the manchette in elongated spermatids. Localizes to the interphase centrosome and the mitotic spindle. {ECO:0000250}. SUBUNIT: Interacts with PLEKHM1 (via N- and C-terminus) (PubMed:27777970). Interacts with dynactin, PCM1 and PCNT. Interacts (via C-terminus) with CENPF (By similarity). Self-associates. Interacts with DISC1, dynein, tubulin gamma, KATNA1, KATNB1, microtubules, PAFAHB1 and YWHAE. Interacts directly with NEFL and indirectly with NEFH. Interacts with ZNF365 (By similarity). {ECO:0000250, ECO:0000269|PubMed:27777970}. TISSUE SPECIFICITY: Expressed in brain, liver, lung and testis (at protein level). Expressed in brain, epididymis, eye, heart, kidney, large intestine, liver, ovary, pancreas, prostate, skeletal muscle, smooth muscle, spleen, submaxillary gland, testis, thymus and thyroid. Within the brain expression is pronounced in the cortex, hippocampus, olfactory bulb, striatum, thalamic and hypothalamic structures and in the molecular layer of the cerebellum. Largely excluded from cortical progenitor cells which express NDE1. {ECO:0000269|PubMed:11163259, ECO:0000269|PubMed:11163260, ECO:0000269|PubMed:11231056, ECO:0000269|PubMed:15147871}. +Q5SW28 PI3R5_MOUSE Phosphoinositide 3-kinase regulatory subunit 5 (PI3-kinase regulatory subunit 5) (PI3-kinase p101 subunit) (Phosphatidylinositol 4,5-bisphosphate 3-kinase regulatory subunit) (PtdIns-3-kinase regulatory subunit) (PtdIns-3-kinase p101) (p101-PI3K) 871 96,954 Chain (1); Modified residue (3); Region (2); Sequence conflict (7) FUNCTION: Regulatory subunit of the PI3K gamma complex. Required for recruitment of the catalytic subunit to the plasma membrane via interaction with beta-gamma G protein dimers. Required for G protein-mediated activation of PIK3CG (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O02696}. Cytoplasm {ECO:0000250|UniProtKB:O02696}. Cell membrane {ECO:0000250|UniProtKB:O02696}; Peripheral membrane protein {ECO:0000250|UniProtKB:O02696}. Note=Predominantly localized in the nucleus in absence of PIK3CG/p120. Colocalizes with PIK3CG/p120 in the cytoplasm. Translocated to the plasma membrane in a beta-gamma G protein-dependent manner. {ECO:0000250|UniProtKB:O02696}. SUBUNIT: Heterodimer of a catalytic subunit (PIK3CG/p120) and a regulatory (PIK3R5a/p101) subunit. Interacts with beta-gamma G protein dimers (By similarity). {ECO:0000250}. DOMAIN: The heterodimerization region allows the binding to the catalytic subunit. {ECO:0000250}. +O55203 LDB2_MOUSE LIM domain-binding protein 2 (LDB-2) (Carboxyl-terminal LIM domain-binding protein 1) (CLIM-1) (LIM domain-binding factor CLIM1) 373 42,691 Alternative sequence (3); Chain (1); Region (1); Sequence conflict (4) FUNCTION: Binds to the LIM domain of a wide variety of LIM domain-containing transcription factors. PTM: Ubiquitinated by RLIM/RNF12, leading to its degradation by the proteasome. {ECO:0000269|PubMed:11882901}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Note=Colocalizes with SLK at leading edges (PubMed:19675209). {ECO:0000269|PubMed:19675209}. SUBUNIT: Interacts with LHX9 (PubMed:10330499). Interacts with SLK; leading to negatively regulate SLK kinase activity (PubMed:19675209). {ECO:0000269|PubMed:10330499, ECO:0000269|PubMed:11882901, ECO:0000269|PubMed:19675209}. +Q9JKS4 LDB3_MOUSE LIM domain-binding protein 3 (Protein cypher) (Protein oracle) (Z-band alternatively spliced PDZ-motif protein) 723 76,432 Alternative sequence (4); Beta strand (6); Chain (1); Domain (4); Erroneous initiation (1); Helix (2); Modified residue (18); Sequence caution (1); Sequence conflict (6); Turn (1) FUNCTION: May function as an adapter in striated muscle to couple protein kinase C-mediated signaling via its LIM domains to the cytoskeleton. {ECO:0000303|PubMed:10391924}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:10391924}. Cell projection, pseudopodium {ECO:0000269|PubMed:10391924}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10391924}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:10391924}. Note=Localized to the cytoplasm around nuclei and pseudopodia of undifferentiated cells and detected throughout the myotubes of differentiated cells. Colocalizes with ACTN2 at the Z-lines. SUBUNIT: Interacts via its LIM domains with various PKC isoforms. Interacts via its PDZ domain with the ACTN2 C-terminal region. Interacts with MYOZ1, MYOZ2 and MYOZ3. {ECO:0000250|UniProtKB:O75112, ECO:0000269|PubMed:10391924}. TISSUE SPECIFICITY: Expressed primarily in adult heart and skeletal muscle, and detected at lower levels in lung. Isoforms are expressed in a tissue-specific manner. Isoform 1, isoform 3 and isoform 5 are expressed in heart, whereas isoform 2, isoform 4 and isoform 6 are expressed in skeletal muscle. {ECO:0000269|PubMed:10391924, ECO:0000269|PubMed:10427098, ECO:0000269|PubMed:10727866, ECO:0000269|PubMed:12499364}. +Q7TPY9 LDOC1_MOUSE Protein LDOC1 151 17,546 Chain (1); Compositional bias (1) FUNCTION: May have an important role in the development and/or progression of some cancers. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with NOD2. {ECO:0000250|UniProtKB:O95751}. +Q14C37 LEMD1_MOUSE LEM domain-containing protein 1 129 14,258 Chain (1); Domain (1) +P41160 LEP_MOUSE Leptin (Obesity factor) 167 18,709 Chain (1); Disulfide bond (1); Natural variant (1); Signal peptide (1) FUNCTION: Key player in the regulation of energy balance and body weight control. Once released into the circulation, has central and peripheral effects by binding LEPR, found in many tissues, which results in the activation of several major signaling pathways (PubMed:15899045, PubMed:16825198, PubMed:11373681, PubMed:12594516, PubMed:20620997). In the hypothalamus, acts as an appetite-regulating factor that induces a decrease in food intake and an increase in energy consumption by inducing anorexinogenic factors and suppressing orexigenic neuropeptides, also regulates bone mass and secretion of hypothalamo-pituitary-adrenal hormones. In the periphery, increases basal metabolism, influences reproductive function, regulates pancreatic beta-cell function and insulin secretion, is pro-angiogenic for endothelial cell and affects innate and adaptive immunity (By similarity) (PubMed:8589726, PubMed:10660043, PubMed:25383904, PubMed:25060689, PubMed:9732873, PubMed:12594516). In the arcuate nucleus of the hypothalamus, activates by depolarization POMC neurons inducing FOS and SOCS3 expression to release anorexigenic peptides and inhibits by hyperpolarization NPY neurons inducing SOCS3 with a consequent reduction on release of orexigenic peptides (By similarity) (PubMed:20620997, PubMed:11373681). In addition to its known satiety inducing effect, has a modulatory role in nutrient absorption. In the intestine, reduces glucose absorption by enterocytes by activating PKC and leading to a sequential activation of p38, PI3K and ERK signaling pathways which exerts an inhibitory effect on glucose absorption. Acts as a growth factor on certain tissues, through the activation of different signaling pathways increases expression of genes involved in cell cycle regulation such as CCND1, via JAK2-STAT3 pathway, or VEGFA, via MAPK1/3 and PI3K-AKT1 pathways (By similarity) (PubMed:16825198, PubMed:20620997). May also play an apoptotic role via JAK2-STAT3 pathway and up-regulation of BIRC5 expression (By similarity). Pro-angiogenic, has mitogenic activity on vascular endothelial cells and plays a role in matrix remodeling by regulating the expression of matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs) (PubMed:16825198). In innate immunity, modulates the activity and function of neutrophils by increasing chemotaxis and the secretion of oxygen radicals. Increases phagocytosis by macrophages and enhances secretion of pro-inflammatory mediators. Increases cytotoxic ability of NK cells (Probable). Plays a pro-inflammatory role, in synergy with IL1B, by inducing NOS2 wich promotes the production of IL6, IL8 and Prostaglandin E2, through a signaling pathway that involves JAK2, PI3K, MAP2K1/MEK1 and MAPK14/p38 (PubMed:15899045). In adaptive immunity, promotes the switch of memory T-cells towards T helper-1 cell immune responses (By similarity). Increases CD4(+)CD25(-) T cells proliferation and reduces autophagy during TCR (T cell receptor) stimulation, through MTOR signaling pathway activation and BCL2 up-regulation (PubMed:25060689). {ECO:0000250|UniProtKB:P41159, ECO:0000250|UniProtKB:P50596, ECO:0000269|PubMed:10660043, ECO:0000269|PubMed:11373681, ECO:0000269|PubMed:12594516, ECO:0000269|PubMed:15899045, ECO:0000269|PubMed:16825198, ECO:0000269|PubMed:20620997, ECO:0000269|PubMed:25060689, ECO:0000269|PubMed:25383904, ECO:0000269|PubMed:8589726, ECO:0000269|PubMed:9732873, ECO:0000305|PubMed:15122202, ECO:0000305|PubMed:25232147}. SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:25232147}. DISEASE: Note=Defects in Lep are the cause of profound obesity and type II diabetes. +Q8K4B0 MTA1_MOUSE Metastasis-associated protein MTA1 715 80,798 Chain (1); Compositional bias (1); Cross-link (4); Domain (3); Erroneous initiation (1); Modified residue (8); Motif (3); Mutagenesis (1); Sequence conflict (3); Zinc finger (1) FUNCTION: Transcriptional coregulator which can act as both a transcriptional corepressor and coactivator. As a part of the histone-deacetylase multiprotein complex (NuRD), regulates transcription of its targets by modifying the acetylation status of the target chromatin and cofactor accessibility to the target DNA. In conjunction with other components of NuRD, acts as a transcriptional corepressor of BRCA1, ESR1, TFF1 and CDKN1A. Acts as a transcriptional coactivator of BCAS3, PAX5 and SUMO2, independent of the NuRD complex. Stimulates the expression of WNT1 by inhibiting the expression of its transcriptional corepressor SIX3. Regulates p53-dependent and -independent DNA repair processes following genotoxic stress. Regulates the stability and function of p53/TP53 by inhibiting its ubiquitination by COP1 and MDM2 thereby regulating the p53-dependent DNA repair. Plays an important role in tumorigenesis, tumor invasion, and metastasis. Plays a role in the regulation of the circadian clock and is essential for the generation and maintenance of circadian rhythms under constant light and for normal entrainment of behavior to light-dark (LD) cycles. Positively regulates the CLOCK-ARNTL/BMAL1 heterodimer mediated transcriptional activation of its own transcription and the transcription of CRY1. Regulates deacetylation of ARNTL/BMAL1 by regulating SIRT1 expression, resulting in derepressing CRY1-mediated transcription repression. With Tfcp2l1, promotes establishment and maintenance of pluripotency in embryonic stem cells (ESCs) and inhibits endoderm differentiation (PubMed:28982712). {ECO:0000269|PubMed:17671180, ECO:0000269|PubMed:19805145, ECO:0000269|PubMed:19837670, ECO:0000269|PubMed:20071335, ECO:0000269|PubMed:20682799, ECO:0000269|PubMed:21965678, ECO:0000269|PubMed:24089055, ECO:0000269|PubMed:28982712}. PTM: Phosphorylation by CSNK1G2/CK1 triggered by estrogen enhances corepression of estrogen receptor (ER). {ECO:0000269|PubMed:15077195}.; PTM: Acetylation is essential for its transcriptional coactivator activity. {ECO:0000250}.; PTM: Sumoylation positively regulates its transcriptional corepressor activity but does not affect the protein stability. Sumoylated preferentially by SUMO2 or SUMO3 than SUMO1. Sumoylation is enhanced by PIAS1/3/4 and preferentially sumoylated by SUMO2 in the presence of PIAS1/3/4. Desumoylated by SENP1 (By similarity). {ECO:0000250}.; PTM: Ubiquitinated by COP1, which leads to proteasomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Nucleus envelope {ECO:0000255|PROSITE-ProRule:PRU00512, ECO:0000255|PROSITE-ProRule:PRU00624}. Cytoplasm. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Associated with microtubules. Primarily localized in the cytoplasm in embryonic tissues. Localization at the nuclear envelope is TPR-dependent. SUBUNIT: Component of the nucleosome-remodeling and histone-deacetylase multiprotein complex (NuRD). Interacts with HDAC1 and ITGB3BP/CENPR (By similarity). Binds to CSNK1G2 in the cytoplasm (PubMed:15077195). Interacts with NACC2. Interacts with EP300, TFAP2C, IFI16, TPR, UBE2I/UBC9, PIAS1, PIAS3, PIAS4, MDM2, COP1, SUMO1, SUMO2, SENP1 and SENP2 (By similarity). Interacts with ARNTL/BMAL1 and CLOCK (PubMed:24089055). Interacts with p53/TP53 (PubMed:19837670). Interacts with HDAC2 (By similarity). Interacts with SIX3; facilitates the binding of SIX3 to the core DNA motif of SIX3 promoter (PubMed:17666527). Interacts with TFCP2L1; which is indispensable for TFCP2L1-mediated self-renewal-promoting effect and endoderm-inhibiting action (PubMed:28982712). {ECO:0000250|UniProtKB:Q13330, ECO:0000269|PubMed:15077195, ECO:0000269|PubMed:17666527, ECO:0000269|PubMed:19837670, ECO:0000269|PubMed:20682799, ECO:0000269|PubMed:24089055, ECO:0000269|PubMed:28982712}. TISSUE SPECIFICITY: Widely expressed but not in skeletal muscle. Highly expressed in the brain, liver, kidney and cardiac muscle and in mammary tumors. {ECO:0000269|PubMed:16617102, ECO:0000269|PubMed:24970816}. +Q8C3P7 MTA70_MOUSE N6-adenosine-methyltransferase subunit METTL3 (EC 2.1.1.348) (Methyltransferase-like protein 3) (N6-adenosine-methyltransferase 70 kDa subunit) (MT-A70) 580 64,616 Alternative sequence (2); Binding site (4); Chain (1); Cross-link (4); Initiator methionine (1); Modified residue (8); Motif (1); Mutagenesis (1); Region (9); Sequence conflict (4) FUNCTION: The METTL3-METTL14 heterodimer forms a N6-methyltransferase complex that methylates adenosine residues at the N(6) position of some RNAs and regulates various processes such as the circadian clock, differentiation of embryonic and haematopoietic stem cells, cortical neurogenesis, response to DNA damage, differentiation of T-cells and primary miRNA processing (PubMed:25456834, PubMed:24394384, PubMed:25569111, PubMed:28809392, PubMed:28792938, PubMed:28869969, PubMed:28965759). In the heterodimer formed with METTL14, METTL3 constitutes the catalytic core (By similarity). N6-methyladenosine (m6A), which takes place at the 5'-[AG]GAC-3' consensus sites of some mRNAs, plays a role in mRNA stability, processing, translation efficiency and editing (By similarity). M6A acts as a key regulator of mRNA stability: methylation is completed upon the release of mRNA into the nucleoplasm and promotes mRNA destabilization and degradation (PubMed:28637692). In embryonic stem cells (ESCs), m6A methylation of mRNAs encoding key naive pluripotency-promoting transcripts results in transcript destabilization, promoting differentiation of ESCs (PubMed:25456834, PubMed:24394384, PubMed:25569111). M6A regulates the length of the circadian clock: acts as an early pace-setter in the circadian loop by putting mRNA production on a fast-track for facilitating nuclear processing, thereby providing an early point of control in setting the dynamics of the feedback loop (PubMed:24209618). M6A regulates spermatogonial differentiation and meiosis and is essential for male fertility and spermatogenesis (PubMed:28809392, PubMed:28914256). Involved in the response to DNA damage: in response to ultraviolet irradiation, METTL3 rapidly catalyzes the formation of m6A on poly(A) transcripts at DNA damage sites, leading to the recruitment of POLK to DNA damage sites (By similarity). M6A is also required for T-cell homeostasis and differentiation: m6A methylation of transcripts of SOCS family members (SOCS1, SOCS3 and CISH) in naive T-cells promotes mRNA destabilization and degradation, promoting T-cell differentiation (PubMed:28792938). M6A also regulates cortical neurogenesis: m6A methylation of transcripts related to transcription factors, neural stem cells, the cell cycle and neuronal differentiation during brain development promotes their destabilization and decay, promoting differentiation of radial glial cells (PubMed:28965759). M6A also takes place in other RNA molecules, such as primary miRNA (pri-miRNAs) (By similarity). Mediates m6A methylation of Xist RNA, thereby participating in random X inactivation: m6A methylation of Xist leads to target YTHDC1 reader on Xist and promote transcription repression activity of Xist (By similarity). METTL3 mediates methylation of pri-miRNAs, marking them for recognition and processing by DGCR8 (By similarity). Acts as a positive regulator of mRNA translation independently of the methyltransferase activity: promotes translation by interacting with the translation initiation machinery in the cytoplasm (By similarity). {ECO:0000250|UniProtKB:Q86U44, ECO:0000269|PubMed:24209618, ECO:0000269|PubMed:24394384, ECO:0000269|PubMed:25456834, ECO:0000269|PubMed:25569111, ECO:0000269|PubMed:28637692, ECO:0000269|PubMed:28792938, ECO:0000269|PubMed:28809392, ECO:0000269|PubMed:28869969, ECO:0000269|PubMed:28914256, ECO:0000269|PubMed:28965759}. PTM: Sumoylation inhibits the N6-adenosine-methyltransferase activity. Sumoylation does not affect subcellular location or interaction with METTL14. Desumoylated by SENP1. {ECO:0000250|UniProtKB:Q86U44}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28914256}. Nucleus speckle {ECO:0000269|PubMed:24394384, ECO:0000269|PubMed:25683224}. Cytoplasm {ECO:0000250|UniProtKB:Q86U44}. Note=Colocalizes with speckles in interphase nuclei. Suggesting that it may be associated with nuclear pre-mRNA splicing components (PubMed:24394384). In response to ultraviolet irradiation, colocalizes to DNA damage sites however, it probably does not bind DNA but localizes in the vicinity of DNA damage site (By similarity). {ECO:0000250|UniProtKB:Q86U44, ECO:0000269|PubMed:24394384}. SUBUNIT: Heterodimer; heterodimerizes with METTL14 to form an antiparallel heterodimer that constitutes an active methyltransferase (By similarity). Component of the WMM complex, a N6-methyltransferase complex composed of a catalytic subcomplex, named MAC, and of an associated subcomplex, named MACOM (PubMed:29535189, PubMed:29547716). The MAC subcomplex is composed of METTL3 and METTL14 (PubMed:29535189, PubMed:29547716). The MACOM subcomplex is composed of WTAP, ZC3H13, CBLL1/HAKAI, VIRMA, and, in some cases of RBM15 (RBM15 or RBM15B) (PubMed:29535189, PubMed:29547716). Interacts with NCBP1/CBP80 (By similarity). Interacts with EIF4E (By similarity). Interacts with EIF3B (By similarity). {ECO:0000250|UniProtKB:Q86U44, ECO:0000269|PubMed:29535189, ECO:0000269|PubMed:29547716}. DOMAIN: Gate loop 1 and gate loop 2 regions are adjacent to the S-adenosyl-L-homocysteine-binding site and display large conformational changes upon ligand-binding. They may play an important role in adenosine recognition. The interface loop contributes to the heterodimer interaction. {ECO:0000250|UniProtKB:Q86U44}. TISSUE SPECIFICITY: Present in both germ cells and somatic cells during testis development (at protein level) (PubMed:28809392). {ECO:0000269|PubMed:28809392, ECO:0000269|PubMed:28914256}. +Q8CIX8 LGSN_MOUSE Lengsin (Glutamate-ammonia ligase domain-containing protein 1) (Lens glutamine synthase-like) 563 62,164 Chain (1) FUNCTION: May act as a component of the cytoskeleton or as a chaperone for the reorganization of intermediate filament proteins during terminal differentiation in the lens. Does not seem to have enzymatic activity. {ECO:0000269|PubMed:18178558}. SUBUNIT: Dodecamer. Interacts with BFSP2 AND VIM. {ECO:0000269|PubMed:17161372, ECO:0000269|PubMed:18178558}. TISSUE SPECIFICITY: Expressed in lens. {ECO:0000269|PubMed:18178558}. +P61375 LHX5_MOUSE LIM/homeobox protein Lhx5 (LIM homeobox protein 5) 402 44,388 Chain (1); DNA binding (1); Domain (2) FUNCTION: Plays an essential role in the regulation of neuronal differentiation and migration during development of the central nervous system. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q8BGA2 LHPL2_MOUSE LHFPL tetraspan subfamily member 2 protein (Lipoma HMGIC fusion partner-like 2 protein) 222 23,873 Chain (1); Natural variant (1); Transmembrane (4) TRANSMEM 11 31 Helical. {ECO:0000255}.; TRANSMEM 97 117 Helical. {ECO:0000255}.; TRANSMEM 127 147 Helical. {ECO:0000255}.; TRANSMEM 175 195 Helical. {ECO:0000255}. FUNCTION: Plays a role in female and male fertility. Involved in distal reproductive tract development (PubMed:26964900). {ECO:0000269|PubMed:26964900}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in the epithelium of the vas deferens (at protein level). Widely expressed (PubMed:26964900). Strongly expressed in heart, spleen, liver, kidney, thymus, testis, brain, lung, intestine, vagina, ovary and uterus (PubMed:26964900). Expressed in follicle cells of the ovary, epithelial cells of the oviduct, both luminal and glandular epithelial cells of the uterus, and epithelial cells of the vagina (PubMed:26964900). {ECO:0000269|PubMed:26964900}. +Q810M6 LIAT1_MOUSE Protein LIAT1 (Ligand of ATE1 protein) 228 25,512 Chain (1); Compositional bias (2); Region (1); Repeat (1) FUNCTION: May be involved in ATE1-mediated N-terminal arginylation. {ECO:0000269|PubMed:25369936}. SUBUNIT: Interacts with ATE1; it is not a substrate of LIAT1. Interacts with JMJD6 and MRPS14. {ECO:0000269|PubMed:25369936}. DOMAIN: LIAT1 proteins of some primates, from macaques to humans, contain tandem repeats of a 10-residue sequence, whereas LIAT1 proteins of other mammals contain a single copy of this motif. Quantities of these repeats are, in general, different in LIAT1 of different primates. For example, there are 1, 4, 13, 13, 17, and 17 repeats in the gibbon, gorilla, orangutan, bonobo, neanderthal, and human LIAT1, respectively. {ECO:0000305|PubMed:25369936}. TISSUE SPECIFICITY: Highly expressed in spleen, thymus, liver and brown adipose tissue. Moderately expressed in liver, testis and lung. {ECO:0000269|PubMed:25369936}. +P53668 LIMK1_MOUSE LIM domain kinase 1 (LIMK-1) (EC 2.7.11.1) (KIZ-1) 647 72,793 Active site (1); Binding site (1); Chain (1); Domain (4); Modified residue (9); Mutagenesis (1); Nucleotide binding (1); Sequence conflict (4) FUNCTION: Serine/threonine-protein kinase that plays an essential role in the regulation of actin filament dynamics. Acts downstream of several Rho family GTPase signal transduction pathways. Activated by upstream kinases including ROCK1, PAK1 and PAK4, which phosphorylate LIMK1 on a threonine residue located in its activation loop. LIMK1 subsequently phosphorylates and inactivates the actin binding/depolymerizing factors cofilin-1/CFL1, cofilin-2/CFL2 and destrin/DSTN, thereby preventing the cleavage of filamentous actin (F-actin), and stabilizing the actin cytoskeleton. In this way LIMK1 regulates several actin-dependent biological processes including cell motility, cell cycle progression, and differentiation. Phosphorylates TPPP on serine residues, thereby promoting microtubule disassembly. axonal outgrowth and may be involved in brain development. Required for atypical chemokine receptor ACKR2-induced phosphorylation of cofilin (CFL1) (By similarity). Stimulates axonal outgrowth and may be involved in brain development. {ECO:0000250, ECO:0000269|PubMed:15056216, ECO:0000269|PubMed:16204183}. PTM: Autophosphorylated. Phosphorylated on Thr-508 by ROCK1 and PAK1, resulting in activation. Phosphorylated by PAK4 which increases the ability of LIMK1 to phosphorylate cofilin. Phosphorylated at Ser-323 by MAPKAPK2 during activation of VEGFA-induced signaling, which results in activation of LIMK1 and promotion of actin reorganization, cell migration, and tubule formation of endothelial cells. Dephosphorylated and inactivated by SSH1. Phosphorylated by CDC42BP (By similarity). {ECO:0000250}.; PTM: Ubiquitinated. 'Lys-48'-linked polyubiquitination by RNF6 leads to proteasomal degradation through the 26S proteasome, modulating LIMK1 levels in the growth cone and its effect on axonal outgrowth. Also polyubiquitinated by RLIM. {ECO:0000269|PubMed:16204183}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16204183}. Nucleus. Cell projection, lamellipodium {ECO:0000269|PubMed:25107909}. Note=Predominantly found in the cytoplasm (By similarity). Localizes in the lamellipodium in a CDC42BPA, CDC42BPB and FAM89B/LRAP25-dependent manner. {ECO:0000250|UniProtKB:P53667, ECO:0000269|PubMed:25107909}. SUBUNIT: Self-associates to form homodimers. Interacts with HSP90AA1; this interaction promotes LIMK1 dimerization and subsequent transphosphorylation. Interacts with CDKN1C (By similarity). Interacts (via LIM domain) with the cytoplasmic domain of NRG1 (By similarity). Interacts with NISCH (PubMed:18332102). Interacts with SSH1 (PubMed:15660133). Interacts with RLIM and RNF6 (PubMed:16204183). Interacts (via LIM zinc-binding domains) with FAM89B/LRAP25 (via LRR repeat). Forms a tripartite complex with CDC42BPA, CDC42BPB and FAM89B/LRAP25 (PubMed:25107909). {ECO:0000250|UniProtKB:P53667, ECO:0000269|PubMed:15660133, ECO:0000269|PubMed:16204183, ECO:0000269|PubMed:18332102, ECO:0000269|PubMed:25107909}. TISSUE SPECIFICITY: Highest expression in the nervous system, particularly in the spinal cord and the cranial nerve and dorsal root ganglia. +Q9Z0M5 LICH_MOUSE Lysosomal acid lipase/cholesteryl ester hydrolase (Acid cholesteryl ester hydrolase) (LAL) (EC 3.1.1.13) (Cholesteryl esterase) (Lipase A) (Sterol esterase) 397 45,325 Active site (2); Chain (1); Domain (1); Glycosylation (5); Sequence conflict (3); Signal peptide (1) FUNCTION: Crucial for the intracellular hydrolysis of cholesteryl esters and triglycerides that have been internalized via receptor-mediated endocytosis of lipoprotein particles. Important in mediating the effect of LDL (low density lipoprotein) uptake on suppression of hydroxymethylglutaryl-CoA reductase and activation of endogenous cellular cholesteryl ester formation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Lysosome. TISSUE SPECIFICITY: Expressed at low levels in most tissues. High level expression is found in hepatocytes and splenic and thymic cells. Very high level expression is observed in cells of the small intestinal villi, the zona fasciculata and reticularis of the adrenal cortex, pancreatic acini, and renal tubular epithelium. +Q571G4 LIN54_MOUSE Protein lin-54 homolog 749 79,566 Alternative sequence (3); Chain (1); Cross-link (5); Domain (1); Erroneous initiation (1); Metal binding (24); Modified residue (7); Region (3); Sequence caution (1); Site (3) FUNCTION: Component of the DREAM complex, a multiprotein complex that can both act as a transcription activator or repressor depending on the context. In G0 phase, the complex binds to more than 800 promoters and is required for repression of E2F target genes. In S phase, the complex selectively binds to the promoters of G2/M genes whose products are required for mitosis and participates in their cell cycle dependent activation. In the complex, acts as a DNA-binding protein that binds the promoter of CDK1 in a sequence-specific manner. Specifically recognizes the consensus motif 5'-TTYRAA-3' in target DNA. {ECO:0000250|UniProtKB:Q6MZP7}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the DREAM complex (also named LINC complex) at least composed of E2F4, E2F5, LIN9, LIN37, LIN52, LIN54, MYBL1, MYBL2, RBL1, RBL2, RBBP4, RBL2, TFDP1 and TFDP2. The complex exists in quiescent cells where it represses cell cycle-dependent genes. It dissociates in S phase when LIN9, LIN37, LIN52 and LIN54 form a subcomplex that binds to MYBL2 (By similarity). {ECO:0000250}. DOMAIN: The CRC domain mediates DNA-binding. It contains two CXC subdomains (joined by a flexible linker) which are both required for efficient association with target DNA. Each CXC subdomain coordinates three Zn(2+) ions. {ECO:0000250|UniProtKB:Q6MZP7}. +O88803 LECT2_MOUSE Leukocyte cell-derived chemotaxin-2 (LECT-2) (Chondromodulin II) (ChM-II) 151 16,405 Alternative sequence (1); Chain (1); Disulfide bond (3); Metal binding (3); Natural variant (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Has a neutrophil chemotactic activity. Also a positive regulator of chondrocyte proliferation. {ECO:0000269|PubMed:10050029}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O14960}. TISSUE SPECIFICITY: Highly expressed in liver and weakly in testis. Not expressed in heart, brain, spleen, lung, skeletal muscle and kidney. {ECO:0000269|PubMed:10050029}. +Q7TNU7 LETM2_MOUSE LETM1 domain-containing protein LETM2, mitochondrial (LETM1 and EF-hand domain-containing protein 2) (Leucine zipper-EF-hand-containing transmembrane protein 1-like) 480 54,458 Chain (1); Compositional bias (1); Domain (1); Topological domain (2); Transit peptide (1); Transmembrane (1) TRANSMEM 176 196 Helical. {ECO:0000255}. TOPO_DOM 26 175 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 197 480 Mitochondrial matrix. {ECO:0000255}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. +Q8CHZ8 LEU7_MOUSE Leukemia-associated protein 7 homolog (Deleted in lymphocytic leukemia 7 homolog) 209 22,444 Chain (1) +Q07797 LG3BP_MOUSE Galectin-3-binding protein (Cyp-C-associated protein) (CyCAP) (Lectin galactoside-binding soluble 3-binding protein) (Protein MAMA) 577 64,491 Chain (1); Disulfide bond (3); Domain (3); Glycosylation (6); Sequence conflict (7); Signal peptide (1) FUNCTION: Promotes integrin-mediated cell adhesion. May stimulate host defense against viruses and tumor cells (By similarity). {ECO:0000250|UniProtKB:Q08380}. PTM: N-glycosylated. {ECO:0000269|PubMed:8341703}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q08380}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:8119883}. SUBUNIT: Homodimers and homomultimers. The multimers form ring-like structures with a diameter of 30-40 nm. Binds LGALS1 and LGALS3. Binds ITGB1, COL4A1, COL5A1, COL6A1, FN1 and NID (By similarity). Interacts with PPIC (in vitro). The unglycosylated form interacts with PDE4DIP isoform 2/MMG8/SMYLE; this interaction may connect a pericentrosomal complex to the gamma-tubulin ring complex (gamma-TuRC) to promote microtubule assembly and acetylation (By similarity). {ECO:0000250|UniProtKB:Q08380, ECO:0000269|PubMed:8341703}. TISSUE SPECIFICITY: Detected in embryo, liver, spleen, kidney, lung, heart, intestine, thymus and lymph node. {ECO:0000269|PubMed:8119883, ECO:0000269|PubMed:8341703}. +Q91YX5 LGAT1_MOUSE Acyl-CoA:lysophosphatidylglycerol acyltransferase 1 (EC 2.3.1.-) 370 43,088 Chain (1); Motif (1); Transmembrane (2) TRANSMEM 22 42 Helical. {ECO:0000255}.; TRANSMEM 342 362 Helical. {ECO:0000255}. FUNCTION: Lysophosphatidylglycerol (LPG) specific acyltransferase that recognizes various acyl-CoAs and LPGs as substrates but demonstrates a clear preference for long chain saturated fatty acyl-CoAs and oleoyl-CoA as acyl donors. Prefers oleoyl-LPG over palmitoyl-LPG as an acyl receptor and oleoyl-CoA over lauroyl-CoA as an acyl donor (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. DOMAIN: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate. {ECO:0000250}. +Q8C735 LIN9_MOUSE Protein lin-9 homolog (mLin-9) (TUDOR gene similar 1 protein) (Type I interferon receptor beta chain-associated protein) 542 61,759 Alternative sequence (3); Chain (1); Cross-link (1); Erroneous initiation (1); Frameshift (1); Initiator methionine (1); Modified residue (7); Sequence conflict (1) FUNCTION: Acts as a tumor suppressor. Inhibits DNA synthesis. Its ability to inhibit oncogenic transformation is mediated through its association with RB1. Plays a role in the expression of genes required for the G1/S transition (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}. Note=Found in perinucleolar structures. Associated with chromatin. {ECO:0000250}. SUBUNIT: Component of the DREAM complex (also named LINC complex) at least composed of E2F4, E2F5, LIN9, LIN37, LIN52, LIN54, MYBL1, MYBL2, RBL1, RBL2, RBBP4, TFDP1 and TFDP2. The complex exists in quiescent cells where it represses cell cycle-dependent genes. It dissociates in S phase when LIN9, LIN37, LIN52 and LIN54 form a subcomplex that binds to MYBL2. Interacts with RB1 (By similarity). {ECO:0000250}. +Q6GQU6 LIGO3_MOUSE Leucine-rich repeat and immunoglobulin-like domain-containing nogo receptor-interacting protein 3 (Leucine-rich repeat neuronal protein 6B) 589 64,683 Chain (1); Compositional bias (1); Disulfide bond (1); Domain (3); Glycosylation (8); Repeat (11); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 529 549 Helical. {ECO:0000255}. TOPO_DOM 24 528 Extracellular. {ECO:0000255}.; TOPO_DOM 550 589 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q3U1D0 LINES_MOUSE Protein Lines homolog 1 (Protein Lines homolog 2) (Wnt-signaling molecule Lines homolog 1) 764 85,642 Alternative sequence (2); Chain (1); Erroneous initiation (1); Modified residue (1); Sequence caution (1); Sequence conflict (1) +Q8BSS9 LIPA2_MOUSE Liprin-alpha-2 (Protein tyrosine phosphatase receptor type f polypeptide-interacting protein alpha-2) (PTPRF-interacting protein alpha-2) 1257 143,234 Chain (1); Coiled coil (5); Compositional bias (2); Domain (3); Modified residue (7); Sequence conflict (2) FUNCTION: Alters PTPRF cellular localization and induces PTPRF clustering. May regulate the disassembly of focal adhesions. May localize receptor-like tyrosine phosphatases type 2A at specific sites on the plasma membrane, possibly regulating their interaction with the extracellular environment and their association with substrates (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell surface {ECO:0000250}. Note=Colocalizes with PTPRF at the cell surface. {ECO:0000250}. SUBUNIT: Forms homodimers and heterodimers with liprins-alpha and liprins-beta. Interacts with the second PTPase domain of PTPRD, PTPRF and PTPRS (By similarity). {ECO:0000250}. DOMAIN: The N-terminal coiled coil regions mediate homodimerization preferentially and heterodimerization type alpha/alpha. The C-terminal, non-coiled coil regions mediate heterodimerization type alpha/beta and interaction with PTPRD, PTPRF and PTPRS (By similarity). {ECO:0000250}. +P27656 LIPC_MOUSE Hepatic triacylglycerol lipase (HL) (Hepatic lipase) (EC 3.1.1.3) (Lipase member C) 510 57,389 Active site (3); Chain (1); Domain (1); Glycosylation (2); Region (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Hepatic lipase has the capacity to catalyze hydrolysis of phospholipids, mono-, di-, and triglycerides, and acyl-CoA thioesters. It is an important enzyme in HDL metabolism. Hepatic lipase binds heparin. SUBCELLULAR LOCATION: Secreted. +Q9D009 LIPT2_MOUSE Putative lipoyltransferase 2, mitochondrial (EC 2.3.1.181) (Lipoate-protein ligase B) (Lipoyl/octanoyl transferase) (Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase) 231 24,955 Active site (1); Chain (1); Domain (1); Modified residue (1); Region (3); Sequence conflict (1); Site (1); Transit peptide (1) Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2. FUNCTION: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes, which catalyze essential redox reactions (By similarity). Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:A6NK58}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:A6NK58}. +Q8BIG2 LKAM1_MOUSE Protein LKAAEAR1 (LKAAEAR motif-containing protein 1) 198 22,126 Chain (1); Sequence conflict (1) +Q9D1E5 LMBRL_MOUSE Protein LMBR1L (Uteroglobin receptor) 489 54,958 Alternative sequence (1); Chain (1); Erroneous initiation (1); Sequence conflict (3); Topological domain (10); Transmembrane (9) TRANSMEM 22 42 Helical. {ECO:0000255}.; TRANSMEM 67 87 Helical. {ECO:0000255}.; TRANSMEM 115 135 Helical. {ECO:0000255}.; TRANSMEM 155 175 Helical. {ECO:0000255}.; TRANSMEM 197 217 Helical. {ECO:0000255}.; TRANSMEM 306 326 Helical. {ECO:0000255}.; TRANSMEM 351 371 Helical. {ECO:0000255}.; TRANSMEM 389 409 Helical. {ECO:0000255}.; TRANSMEM 432 452 Helical. {ECO:0000255}. TOPO_DOM 1 21 Extracellular. {ECO:0000255}.; TOPO_DOM 43 66 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 88 114 Extracellular. {ECO:0000255}.; TOPO_DOM 136 154 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 176 196 Extracellular. {ECO:0000255}.; TOPO_DOM 218 305 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 327 350 Extracellular. {ECO:0000255}.; TOPO_DOM 372 388 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 410 431 Extracellular. {ECO:0000255}.; TOPO_DOM 453 489 Cytoplasmic. {ECO:0000255}. FUNCTION: Probable receptor which may mediate endocytosis of its ligand. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q5XJV6 LMTK3_MOUSE Serine/threonine-protein kinase LMTK3 (EC 2.7.11.1) (Apoptosis-associated tyrosine kinase 3) (Lemur tyrosine kinase 3) 1424 150,891 Active site (1); Binding site (1); Chain (1); Compositional bias (3); Domain (1); Modified residue (7); Mutagenesis (1); Nucleotide binding (1); Sequence conflict (8); Signal peptide (1); Transmembrane (1) TRANSMEM 40 60 Helical. {ECO:0000255}. FUNCTION: Protein kinase which phosphorylates ESR1 (in vitro) and protects it against proteasomal degradation. May also regulate ESR1 levels indirectly via a PKC-AKT-FOXO3 pathway where it decreases the activity of PKC and the phosphorylation of AKT, thereby increasing binding of transcriptional activator FOXO3 to the ESR1 promoter and increasing ESR1 transcription (By similarity). Involved in endocytic trafficking of N-methyl-D-aspartate receptors (NMDAR) in neurons (PubMed:24760852). {ECO:0000250|UniProtKB:Q96Q04, ECO:0000269|PubMed:24760852}. PTM: Autophosphorylated. {ECO:0000269|PubMed:17651901}. SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:17651901}; Single-pass membrane protein {ECO:0000305|PubMed:17651901}. Cell projection, axon {ECO:0000269|PubMed:17651901}. Cell projection, dendrite {ECO:0000269|PubMed:17651901}. Golgi apparatus membrane {ECO:0000269|PubMed:24760852}. Note=Punctate pattern in cell projections. SUBUNIT: Interacts with ESR1 (By similarity). Interacts with AP-2 complex subunit alpha (PubMed:24760852). {ECO:0000250|UniProtKB:Q96Q04, ECO:0000269|PubMed:24760852}. TISSUE SPECIFICITY: Expressed in brain. Predominantly expressed in cerebral cortex, thalamus, the cerebellum and hippocampal formation (at protein level). {ECO:0000269|PubMed:17651901, ECO:0000269|PubMed:24760852}. +Q8K097 LFG2_MOUSE Protein lifeguard 2 (Fas apoptotic inhibitory molecule 2) (Neural membrane protein 35) 317 35,258 Alternative sequence (1); Chain (1); Erroneous initiation (1); Glycosylation (1); Sequence conflict (2); Transmembrane (7) TRANSMEM 107 127 Helical. {ECO:0000255}.; TRANSMEM 139 159 Helical. {ECO:0000255}.; TRANSMEM 166 186 Helical. {ECO:0000255}.; TRANSMEM 195 215 Helical. {ECO:0000255}.; TRANSMEM 226 246 Helical. {ECO:0000255}.; TRANSMEM 252 272 Helical. {ECO:0000255}.; TRANSMEM 291 311 Helical. {ECO:0000255}. FUNCTION: Antiapoptotic protein which protects cells uniquely from Fas-induced apoptosis. Regulates Fas-mediated apoptosis in neurons by interfering with caspase-8 activation. Plays a role in cerebellar development by affecting cerebellar size, internal granular layer (IGL) thickness, and Purkinje cell (PC) development. {ECO:0000269|PubMed:17635665, ECO:0000269|PubMed:21209208, ECO:0000269|PubMed:21957071}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Membrane raft {ECO:0000269|PubMed:17635665}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000250}. SUBUNIT: Interacts with FAS/TNFRSF6 and BAX. {ECO:0000250}. TISSUE SPECIFICITY: Brain. Highly expressed in cerebellum, also found in cortex, olfactory bulb, and hippocampus. {ECO:0000269|PubMed:17635665, ECO:0000269|PubMed:21957071}. +O35652 LHX8_MOUSE LIM/homeobox protein Lhx8 (LIM homeobox protein 8) (L3) (LIM/homeobox protein Lhx7) (LIM homeobox protein 7) 367 40,710 Chain (1); DNA binding (1); Domain (2); Erroneous initiation (1); Sequence conflict (12) FUNCTION: Transcription factor involved in differentiation of certain neurons and mesenchymal cells. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q149C3 LIGO4_MOUSE Leucine-rich repeat and immunoglobulin-like domain containing-NOGO receptor-interacting protein 4 (Leucine-rich repeat neuronal protein 6D) 593 64,189 Chain (1); Disulfide bond (1); Domain (3); Erroneous initiation (2); Frameshift (1); Glycosylation (6); Repeat (11); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 534 554 Helical. {ECO:0000255}. TOPO_DOM 30 533 Extracellular. {ECO:0000255}.; TOPO_DOM 555 593 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q8JZS0 LIN7A_MOUSE Protein lin-7 homolog A (Lin-7A) (mLin-7) (Mammalian lin-seven protein 1) (MALS-1) (Vertebrate lin-7 homolog 1) (Veli-1) 233 25,993 Chain (1); Compositional bias (2); Domain (2); Motif (1) FUNCTION: Plays a role in establishing and maintaining the asymmetric distribution of channels and receptors at the plasma membrane of polarized cells. Forms membrane-associated multiprotein complexes that may regulate delivery and recycling of proteins to the correct membrane domains. The tripartite complex composed of LIN7 (LIN7A, LIN7B or LIN7C), CASK and APBA1 may have the potential to couple synaptic vesicle exocytosis to cell adhesion in brain. Ensures the proper localization of GRIN2B (subunit 2B of the NMDA receptor) to neuronal postsynaptic density and may function in localizing synaptic vesicles at synapses where it is recruited by beta-catenin and cadherin. Required to localize Kir2 channels, GABA transporter (SLC6A12) and EGFR/ERBB1, ERBB2, ERBB3 and ERBB4 to the basolateral membrane of epithelial cells. {ECO:0000269|PubMed:14622577}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15494546}; Peripheral membrane protein {ECO:0000269|PubMed:15494546}. Basolateral cell membrane {ECO:0000269|PubMed:15494546}; Peripheral membrane protein {ECO:0000269|PubMed:15494546}. Cell junction {ECO:0000269|PubMed:15494546}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000269|PubMed:15494546}; Peripheral membrane protein {ECO:0000269|PubMed:15494546}. Cell junction, tight junction {ECO:0000269|PubMed:15494546}. Cell junction, synapse, synaptosome {ECO:0000269|PubMed:15494546}. Note=Enriched in synaptosomes and at epithelial cell-cell junctions. Mainly basolateral in renal epithelial cells. SUBUNIT: Forms two exclusive ternary complexes with CASK and APBA1 or CASKIN1 (By similarity). Can also interact with other modular proteins containing protein-protein interaction domains like MPP5, MPP6, MPP7, DLG1, DLG2 and DLG3 through its L27 domain. Interacts with DLG4, GRIN2B and MARCH11 as well as CDH1 and CTNNB1, the channels KCNJ12/Kir2.2, KCNJ4/Kir2.3 and probably KCNJ2/Kir2.1 and SLC6A12/BGT-1 via its PDZ domain. The association of LIN7A with cadherin and beta-catenin is calcium-dependent, occurs at synaptic junctions and requires the actin cytoskeleton. Interacts with EGFR, ERBB2, ERBB3 and ERBB4 with both PDZ and KID domains. Associates with KIF17 via APBA1. Interacts with HTR4. Forms a tripartite complex composed of DLG1, MPP7 and LIN7 (LIN7A or LIN7C) (By similarity). {ECO:0000250}. DOMAIN: The kinase interacting site is required for proper delivery of ERBB2 to the basolateral membrane. {ECO:0000250}.; DOMAIN: The PDZ domain regulates endocytosis and recycling of the receptor at the membrane. {ECO:0000250}.; DOMAIN: The L27 domain mediates interaction with CASK and is involved in the formation of multimeric complexes and the association of LIN7 to membranes. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the kidney, along the length of the nephron. {ECO:0000269|PubMed:15494546}. +O88951 LIN7B_MOUSE Protein lin-7 homolog B (Lin-7B) (Mammalian lin-seven protein 2) (MALS-2) (Vertebrate lin-7 homolog 2) (Veli-2) 207 22,914 Chain (1); Domain (2); Helix (3); Motif (1) FUNCTION: Plays a role in establishing and maintaining the asymmetric distribution of channels and receptors at the plasma membrane of polarized cells. Forms membrane-associated multiprotein complexes that may regulate delivery and recycling of proteins to the correct membrane domains. The tripartite complex composed of LIN7 (LIN7A, LIN7B or LIN7C), CASK and APBA1 may have the potential to couple synaptic vesicle exocytosis to cell adhesion in brain. Ensures the proper localization of GRIN2B (subunit 2B of the NMDA receptor) to neuronal postsynaptic density and may function in localizing synaptic vesicles at synapses where it is recruited by beta-catenin and cadherin. Required to localize Kir2 channels, GABA transporter (SLC6A12) and EGFR/ERBB1, ERBB2, ERBB3 and ERBB4 to the basolateral membrane of epithelial cells. May increase the amplitude of ASIC3 acid-evoked currents by stabilizing the channel at the cell surface. {ECO:0000269|PubMed:15317815}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15494546}; Peripheral membrane protein {ECO:0000269|PubMed:15494546}. Basolateral cell membrane {ECO:0000269|PubMed:15494546}; Peripheral membrane protein {ECO:0000269|PubMed:15494546}. Cell junction {ECO:0000269|PubMed:15494546}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000269|PubMed:15494546}; Peripheral membrane protein {ECO:0000269|PubMed:15494546}. Cell junction, tight junction {ECO:0000269|PubMed:15494546}. Cell junction, synapse, synaptosome {ECO:0000269|PubMed:15494546}. Note=Enriched in synaptosomes and at epithelial cell-cell junctions. Mainly basolateral in renal epithelial cells. SUBUNIT: Forms two exclusive ternary complexes with CASK and APBA1 or CASKIN1. Can also interact with other modular proteins containing protein-protein interaction domains like MPP5, MPP6, MPP7, DLG1, DLG2 and DLG3 through its L27 domain. Interacts with DLG4 and GRIN2B as well as CDH1 and CTNNB1, the channels KCNJ12/Kir2.2, KCNJ4/Kir2.3 and probably KCNJ2/Kir2.1 and SLC6A12/BGT-1 via its PDZ domain. The association of LIN7A with cadherin and beta-catenin is calcium-dependent, occurs at synaptic junctions and requires the actin cytoskeleton. Interacts with EGFR, ERBB2, ERBB3 and ERBB4 with both PDZ and KID domains. Associates with KIF17 via APBA1. Interacts with ASIC3. Interacts with RTKN (By similarity). {ECO:0000250}. DOMAIN: The kinase interacting site is required for proper delivery of ERBB2 to the basolateral membrane. {ECO:0000250}.; DOMAIN: The PDZ domain regulates endocytosis and recycling of the receptor at the membrane. {ECO:0000250}.; DOMAIN: The L27 domain mediates interaction with CASK and is involved in the formation of multimeric complexes and the association of LIN7 to membranes. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the kidney; predominantly in the vasa recta. {ECO:0000269|PubMed:11742811, ECO:0000269|PubMed:15494546}. +O88952 LIN7C_MOUSE Protein lin-7 homolog C (Lin-7C) (mLin7C) (Mammalian lin-seven protein 3) (MALS-3) (Vertebrate lin-7 homolog 3) (Veli-3) 197 21,834 Chain (1); Domain (2); Initiator methionine (1); Modified residue (1); Motif (1) FUNCTION: Plays a role in establishing and maintaining the asymmetric distribution of channels and receptors at the plasma membrane of polarized cells. Forms membrane-associated multiprotein complexes that may regulate delivery and recycling of proteins to the correct membrane domains. The tripartite complex composed of LIN7 (LIN7A, LIN7B or LIN7C), CASK and APBA1 may have the potential to couple synaptic vesicle exocytosis to cell adhesion in brain. Ensures the proper localization of GRIN2B (subunit 2B of the NMDA receptor) to neuronal postsynaptic density and may function in localizing synaptic vesicles at synapses where it is recruited by beta-catenin and cadherin. Required to localize Kir2 channels, GABA transporter (SLC6A12) and EGFR/ERBB1, ERBB2, ERBB3 and ERBB4 to the basolateral membrane of epithelial cells. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. Basolateral cell membrane; Peripheral membrane protein. Cell junction. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density; Peripheral membrane protein. Cell junction, tight junction. Cell junction, synapse, synaptosome. Note=Enriched in synaptosomes and at epithelial cell-cell junctions. Mainly basolateral in renal epithelial cells. SUBUNIT: Forms two exclusive ternary complexes with CASK and APBA1 or CASKIN1 (By similarity). Can also interact with other modular proteins containing protein-protein interaction domains like MPP5, MPP6, MPP7, DLG1, DLG2 and DLG3 through its L27 domain. Interacts with DLG4 and GRIN2B as well as CDH1 and CTNNB1, the channels KCNJ12/Kir2.2, KCNJ4/Kir2.3 and probably KCNJ2/Kir2.1 and SLC6A12/BGT-1 via its PDZ domain. The association of LIN7A with cadherin and beta-catenin is calcium-dependent, occurs at synaptic junctions and requires the actin cytoskeleton. Interacts with EGFR, ERBB2, ERBB3 and ERBB4 with both PDZ and KID domains. Associates with KIF17 via APBA1. Interacts with HTR4. Forms a tripartite complex composed of DLG1, MPP7 and LIN7 (LIN7A or LIN7C) (By similarity). Interacts with MAPK12. {ECO:0000250, ECO:0000269|PubMed:10710551, ECO:0000269|PubMed:10753959, ECO:0000269|PubMed:15466885, ECO:0000269|PubMed:15878399, ECO:0000269|PubMed:9753324}. DOMAIN: The kinase interacting site is required for proper delivery of ERBB2 to the basolateral membrane. {ECO:0000250}.; DOMAIN: The PDZ domain regulates endocytosis and recycling of the receptor at the membrane. {ECO:0000250}.; DOMAIN: The L27 domain mediates interaction with CASK and is involved in the formation of multimeric complexes and the association of LIN7 to membranes. {ECO:0000269|PubMed:10710551}. TISSUE SPECIFICITY: Expressed in the kidney; particularly in the outer medullary collecting duct. {ECO:0000269|PubMed:15494546}. +Q9CPP7 LIPG_MOUSE Gastric triacylglycerol lipase (GL) (Gastric lipase) (EC 3.1.1.3) 395 44,637 Active site (3); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (2); Sequence conflict (27); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P07098}. +Q9JIT0 LMBR1_MOUSE Limb region 1 protein 490 55,115 Alternative sequence (3); Chain (1); Coiled coil (1); Frameshift (1); Topological domain (10); Transmembrane (9) TRANSMEM 20 40 Helical. {ECO:0000255}.; TRANSMEM 63 83 Helical. {ECO:0000255}.; TRANSMEM 111 131 Helical. {ECO:0000255}.; TRANSMEM 152 172 Helical. {ECO:0000255}.; TRANSMEM 188 208 Helical. {ECO:0000255}.; TRANSMEM 292 312 Helical. {ECO:0000255}.; TRANSMEM 340 360 Helical. {ECO:0000255}.; TRANSMEM 384 404 Helical. {ECO:0000255}.; TRANSMEM 427 447 Helical. {ECO:0000255}. TOPO_DOM 1 19 Extracellular. {ECO:0000255}.; TOPO_DOM 41 62 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 84 110 Extracellular. {ECO:0000255}.; TOPO_DOM 132 151 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 173 187 Extracellular. {ECO:0000255}.; TOPO_DOM 209 291 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 313 339 Extracellular. {ECO:0000255}.; TOPO_DOM 361 383 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 405 426 Extracellular. {ECO:0000255}.; TOPO_DOM 448 490 Cytoplasmic. {ECO:0000255}. FUNCTION: Putative membrane receptor. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +P48678 LMNA_MOUSE Prelamin-A/C [Cleaved into: Lamin-A/C] 665 74,238 Alternative sequence (4); Beta strand (13); Chain (2); Cross-link (19); Domain (2); Erroneous initiation (1); Lipidation (1); Modified residue (64); Motif (1); Mutagenesis (2); Propeptide (2); Region (8); Sequence conflict (12); Site (4); Turn (1) FUNCTION: Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin. Lamin A and C are present in equal amounts in the lamina of mammals. Plays an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics. Required for normal development of peripheral nervous system and skeletal muscle and for muscle satellite cell proliferation. Required for osteoblastogenesis and bone formation. Also prevents fat infiltration of muscle and bone marrow, helping to maintain the volume and strength of skeletal muscle and bone. Required for cardiac homeostasis (PubMed:26436652). Isoform C2 may have a role in determining the organization of nuclear and chromosomal structures during spermatogenesis. {ECO:0000269|PubMed:10579712, ECO:0000269|PubMed:11799477, ECO:0000269|PubMed:19124654, ECO:0000269|PubMed:21547077, ECO:0000269|PubMed:21982926, ECO:0000269|PubMed:23535822, ECO:0000269|PubMed:26436652}.; FUNCTION: Prelamin-A/C can accelerate smooth muscle cell senescence. It acts to disrupt mitosis and induce DNA damage in vascular smooth muscle cells (VSMCs), leading to mitotic failure, genomic instability, and premature senescence (By similarity). {ECO:0000250}. PTM: Proteolytic cleavage of the C-terminal of 18 residues of prelamin-A/C results in the production of lamin-A/C. The prelamin-A/C maturation pathway includes farnesylation of CAAX motif, ZMPSTE24/FACE1 mediated cleavage of the last three amino acids, methylation of the C-terminal cysteine and endoproteolytic removal of the last 15 C-terminal amino acids. Proteolytic cleavage requires prior farnesylation and methylation, and absence of these blocks cleavage (By similarity). {ECO:0000250}.; PTM: Sumoylation is necessary for the localization to the nuclear envelope. {ECO:0000250}.; PTM: Farnesylation of prelamin-A/C facilitates nuclear envelope targeting. {ECO:0000250}.; PTM: Increased phosphorylation of the lamins occurs before envelope disintegration and probably plays a role in regulating lamin associations.; PTM: Isoform C is phosphorylated on Ser-392, Ser-407 and Ser-409 at interphase. {ECO:0000269|PubMed:1959608}.; PTM: The N-terminus is blocked. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26436652}. Nucleus envelope. Nucleus lamina {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Note=Farnesylation of prelamin-A/C facilitates nuclear envelope targeting and subsequent cleaveage by ZMPSTE24/FACE1 to remove the farnesyl group produces mature lamin-A/C, which can then be inserted into the nuclear lamina. EMD is required for proper localization of non-farnesylated prelamin-A/C (By similarity). {ECO:0000250}. SUBUNIT: Homodimer of lamin A and lamin C. Interacts with lamin-associated polypeptides IA, IB and TMPO-alpha, RB1 and with emerin. Proteolytically processed isoform A interacts with NARF (By similarity). Interacts with SREBF1, SREBF2, SUN1, SUN2 and TMEM43. Interacts with TMEM201. Prelamin-A/C interacts with EMD. Interacts with DMPK; may regulate nuclear envelope stability (By similarity). Interacts with MLIP (PubMed:26436652, PubMed:21498514). Interacts with SUV39H1; the interaction increases stability of SUV39H1. Interacts with ITSN1 isoform 2 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P02545, ECO:0000269|PubMed:11929849, ECO:0000269|PubMed:16380439, ECO:0000269|PubMed:16648470, ECO:0000269|PubMed:18230648, ECO:0000269|PubMed:19843581, ECO:0000269|PubMed:19933576, ECO:0000269|PubMed:21498514, ECO:0000269|PubMed:22349700, ECO:0000269|PubMed:23695662, ECO:0000269|PubMed:26436652}. TISSUE SPECIFICITY: Expressed in liver and in bone marrow (at protein level). Isoform C2 is specifically expressed in germ cells. Expressed in cardiomyocytes (PubMed:26436652). {ECO:0000269|PubMed:10579712, ECO:0000269|PubMed:21547077, ECO:0000269|PubMed:26436652}. +Q3TYD6 LMTK2_MOUSE Serine/threonine-protein kinase LMTK2 (EC 2.7.11.1) (Brain-enriched kinase) (Lemur tyrosine kinase 2) 1471 160,508 Active site (1); Binding site (1); Chain (1); Domain (1); Modified residue (12); Nucleotide binding (1); Sequence conflict (1); Topological domain (3); Transmembrane (2) TRANSMEM 11 31 Helical. {ECO:0000255}.; TRANSMEM 42 62 Helical. {ECO:0000255}. TOPO_DOM 1 10 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 32 41 Lumenal. {ECO:0000255}.; TOPO_DOM 63 1471 Cytoplasmic. {ECO:0000255}. FUNCTION: Phosphorylates PPP1C, phosphorylase b and CFTR. {ECO:0000250}. PTM: Autophosphorylated. Phosphorylated (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein. SUBUNIT: Interacts with PPP1C and inhibitor-2. {ECO:0000250}. TISSUE SPECIFICITY: Mainly expressed in brain, especially in the olfactory bulb, olfactory tubercle, hippocampus, striatum, cerebellum and cerebral cortex. Weakly expressed in skeletal muscle and not expressed in liver. {ECO:0000269|PubMed:15005709}. +A2A5N8 LMBL1_MOUSE Lethal(3)malignant brain tumor-like protein 1 (H-l(3)mbt) (H-l(3)mbt protein) (L(3)mbt-like) (L(3)mbt protein homolog) 826 91,781 Chain (1); Domain (1); Modified residue (1); Region (1); Repeat (3); Sequence conflict (1); Site (2); Zinc finger (1) FUNCTION: Polycomb group (PcG) protein that specifically recognizes and binds mono- and dimethyllysine residues on target proteins, therey acting as a 'reader' of a network of post-translational modifications. PcG proteins maintain the transcriptionally repressive state of genes: acts as a chromatin compaction factor by recognizing and binding mono- and dimethylated histone H1b/HIST1H1E at 'Lys-26' (H1bK26me1 and H1bK26me2) and histone H4 at 'Lys-20' (H4K20me1 and H4K20me2), leading to condense chromatin and repress transcription. Recognizes and binds p53/TP53 monomethylated at 'Lys-382', leading to repress p53/TP53-target genes. Also recognizes and binds RB1/RB monomethylated at 'Lys-860'. Participates in the ETV6-mediated repression. Probably plays a role in cell proliferation. Overexpression induces multinucleated cells, suggesting that it is required to accomplish normal mitosis (By similarity). {ECO:0000250}. PTM: Ubiquitinated in a VCP/p97-dependent way following DNA damage, leading to its removal from DNA damage sites, promoting accessibility of H4K20me2 mark for DNA repair protein TP53BP1, which is then recruited to DNA damage sites. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Excluded from the nucleolus. Does not colocalizes with the PcG protein BMI1, suggesting that these two proteins do not belong to the same complex (By similarity). {ECO:0000250}. SUBUNIT: Homodimer. Interacts with RB1/RB (when monomethylated at 'Lys-860'). Interacts with p53/TP53 (when monomethylated at 'Lys-382'). Interacts with CBX3, ETV6, KMT5A and VCP/p97 (By similarity). {ECO:0000250}. DOMAIN: The MBT repeat 2 specifically recognizes and binds monomethylated and dimethylated proteins. In contrast, it does not bind trimethylated proteins. The MBT repeat 1 does not bind methylated peptides but inserts a proline ring in a Pro-Ser-Ser/Thr sequence context (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in brain, testis, eyes, and ES cells. {ECO:0000269|PubMed:20592034}. +A2AQP0 MYH7B_MOUSE Myosin-7B (Myosin cardiac muscle beta chain) (Myosin heavy chain 7B, cardiac muscle beta isoform) 1941 221,497 Chain (1); Coiled coil (1); Domain (3); Nucleotide binding (1); Region (2) FUNCTION: Involved in muscle contraction. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. SUBUNIT: Muscle myosin is a hexameric protein that consists of 2 heavy chain subunits (MHC), 2 alkali light chain subunits (MLC) and 2 regulatory light chain subunits (MLC-2). {ECO:0000250}. +Q8VDD5 MYH9_MOUSE Myosin-9 (Cellular myosin heavy chain, type A) (Myosin heavy chain 9) (Myosin heavy chain, non-muscle IIa) (Non-muscle myosin heavy chain A) (NMMHC-A) (Non-muscle myosin heavy chain IIa) (NMMHC II-a) (NMMHC-IIA) 1960 226,372 Chain (1); Coiled coil (1); Domain (3); Erroneous initiation (1); Initiator methionine (1); Modified residue (30); Nucleotide binding (1); Region (2); Sequence conflict (1) FUNCTION: During cell spreading, plays an important role in cytoskeleton reorganization, focal contacts formation (in the margins but not the central part of spreading cells), and lamellipodial retraction; this function is mechanically antagonized by MYH10 (By similarity). Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping. {ECO:0000250, ECO:0000269|PubMed:19401332}. PTM: ISGylated. {ECO:0000269|PubMed:16139798}.; PTM: Ubiquitination. {ECO:0000269|PubMed:27331610}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19401332}. Cytoplasm, cell cortex {ECO:0000269|PubMed:19401332}. Note=Colocalizes with actin filaments at lamellipodia margins and at the leading edge of migrating cells (By similarity). In retinal pigment epithelial cells, predominantly localized to stress fiber-like structures with some localization to cytoplasmic puncta (By similarity). {ECO:0000250|UniProtKB:P35579}. SUBUNIT: Myosin is a hexameric protein that consists of 2 heavy chain subunits (MHC), 2 alkali light chain subunits (MLC) and 2 regulatory light chain subunits (MLC-2). Interacts with RASIP1 (PubMed:21396893). Interacts with DDR1 (PubMed:19401332). Interacts with SLC6A4 (By similarity). Interacts with PDLIM2 (By similarity). Interacts with SVIL (By similarity). Interacts with HTRA3 (By similarity). Interacts with Myo7a (PubMed:27331610). Interacts with C9orf135 homolog (By similarity). Interacts with LIMCH1; independently of the integration of MYH9 into the myosin complex (By similarity). {ECO:0000250|UniProtKB:P35579, ECO:0000250|UniProtKB:Q62812, ECO:0000269|PubMed:19401332, ECO:0000269|PubMed:21396893, ECO:0000269|PubMed:27331610}. DOMAIN: The rodlike tail sequence is highly repetitive, showing cycles of a 28-residue repeat pattern composed of 4 heptapeptides, characteristic for alpha-helical coiled coils. +P05977 MYL1_MOUSE Myosin light chain 1/3, skeletal muscle isoform (MLC1/MLC3) (MLC1F/MLC3F) (Myosin light chain alkali 1/2) (Myosin light chain A1/A2) 188 20,595 Alternative sequence (1); Chain (1); Domain (3); Initiator methionine (2); Modified residue (6) FUNCTION: Regulatory light chain of myosin. Does not bind calcium. PTM: Isoform MLC3 is acetylated at position 2. {ECO:0000250}. SUBUNIT: Myosin is a hexamer of 2 heavy chains and 4 light chains. +Q9D4H7 LONF3_MOUSE LON peptidase N-terminal domain and RING finger protein 3 (RING finger protein 127) 753 83,656 Chain (1); Domain (1); Repeat (4); Zinc finger (2) +Q9JL06 LPAR2_MOUSE Lysophosphatidic acid receptor 2 (LPA receptor 2) (LPA-2) (Lysophosphatidic acid receptor Edg-4) 348 38,777 Chain (1); Glycosylation (2); Lipidation (1); Motif (1); Topological domain (8); Transmembrane (7) TRANSMEM 31 51 Helical; Name=1. {ECO:0000255}.; TRANSMEM 67 87 Helical; Name=2. {ECO:0000255}.; TRANSMEM 105 124 Helical; Name=3. {ECO:0000255}.; TRANSMEM 145 165 Helical; Name=4. {ECO:0000255}.; TRANSMEM 186 206 Helical; Name=5. {ECO:0000255}.; TRANSMEM 240 260 Helical; Name=6. {ECO:0000255}.; TRANSMEM 271 291 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 30 Extracellular. {ECO:0000255}.; TOPO_DOM 52 66 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 88 104 Extracellular. {ECO:0000255}.; TOPO_DOM 125 144 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 166 185 Extracellular. {ECO:0000255}.; TOPO_DOM 207 239 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 261 270 Extracellular. {ECO:0000255}.; TOPO_DOM 292 348 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for lysophosphatidic acid (LPA), a mediator of diverse cellular activities. Seems to be coupled to the G(i)/G(o), G(12)/G(13), and G(q) families of heteromeric G proteins. Plays a key role in phospholipase C-beta (PLC-beta) signaling pathway Stimulates phospholipase C (PLC) activity in a manner that is independent of RALA activation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell surface {ECO:0000250}. Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=Prior to LPA treatment found predominantly at the cell surface but in the presence of LPA colocalizes with RALA in the endocytic vesicles. {ECO:0000250}. SUBUNIT: Interacts with SLC9A3R2/NHERF2, MAGI3 and PLCB3. Interacts with RALA and GRK2 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Most abundantly expressed in testes, kidney, and embryonic brain. Other organs also express the transcript, including heart, lung, spleen, thymus, stomach, and adult brain. Several have little or no expression, including liver, small intestine, and skeletal muscle. +Q8BMC0 LPAR6_MOUSE Lysophosphatidic acid receptor 6 (LPA receptor 6) (LPA-6) (Oleoyl-L-alpha-lysophosphatidic acid receptor) (P2Y purinoceptor 5) (P2Y5) (Purinergic receptor 5) 344 39,439 Chain (1); Disulfide bond (1); Glycosylation (4); Lipidation (1); Topological domain (8); Transmembrane (7) TRANSMEM 26 46 Helical; Name=1. {ECO:0000255}.; TRANSMEM 57 77 Helical; Name=2. {ECO:0000255}.; TRANSMEM 91 111 Helical; Name=3. {ECO:0000255}.; TRANSMEM 135 155 Helical; Name=4. {ECO:0000255}.; TRANSMEM 184 204 Helical; Name=5. {ECO:0000255}.; TRANSMEM 231 251 Helical; Name=6. {ECO:0000255}.; TRANSMEM 273 293 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 25 Extracellular. {ECO:0000255}.; TOPO_DOM 47 56 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 78 90 Extracellular. {ECO:0000255}.; TOPO_DOM 112 134 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 156 183 Extracellular. {ECO:0000255}.; TOPO_DOM 205 230 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 252 272 Extracellular. {ECO:0000255}.; TOPO_DOM 294 344 Cytoplasmic. {ECO:0000255}. FUNCTION: Binds to oleoyl-L-alpha-lysophosphatidic acid (LPA). Intracellular cAMP is involved in the receptor activation. Important for the maintenance of hair growth and texture (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Ubiquitously expressed. Detected in the hair follicles and skin (at protein level). {ECO:0000269|PubMed:18297070, ECO:0000269|PubMed:18297072}. +P39654 LOX15_MOUSE Arachidonate 15-lipoxygenase (15-LOX) (EC 1.13.11.33) (12/15-lipoxygenase) (12/15-LO) (Arachidonate 12-lipoxygenase, leukocyte-type) (12-LOX) (L-12LO) (EC 1.13.11.31) (Arachidonate omega-6 lipoxygenase) 663 75,445 Chain (1); Domain (2); Metal binding (5); Sequence conflict (6) Lipid metabolism; hydroperoxy eicosatetraenoic acid biosynthesis. FUNCTION: Non-heme iron-containing dioxygenase that catalyzes the stereo-specific peroxidation of free and esterified polyunsaturated fatty acids generating a spectrum of bioactive lipid mediators. Converts arachidonic acid into 12-hydroperoxyeicosatetraenoic acid/12-HPETE and 15-hydroperoxyeicosatetraenoic acid/15-HPETE. Also converts linoleic acid to 13-hydroperoxyoctadecadienoic acid. May also act on (12S)-hydroperoxyeicosatetraenoic acid/(12S)-HPETE to produce hepoxilin A3. Probably plays an important role in the immune and inflammatory responses. Through the oxygenation of membrane-bound phosphatidylethanolamine in macrophages may favor clearance of apoptotic cells during inflammation by resident macrophages and prevent an autoimmune response associated with the clearance of apoptotic cells by inflammatory monocytes. In parallel, may regulate actin polymerization which is crucial for several biological processes, including macrophage function. May also regulate macrophage function through regulation of the peroxisome proliferator activated receptor signaling pathway. Finally, it is also involved in the cellular response to IL13/interleukin-13. In addition to its role in the immune and inflammatory responses, may play a role in epithelial wound healing in the cornea maybe through production of lipoxin A4. May also play a role in endoplasmic reticulum stress response and the regulation of bone mass. {ECO:0000269|PubMed:10432118, ECO:0000269|PubMed:11278875, ECO:0000269|PubMed:14716014, ECO:0000269|PubMed:15708862, ECO:0000269|PubMed:22215650, ECO:0000269|PubMed:22503541}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:11278875}. Cell membrane {ECO:0000269|PubMed:11278875}; Peripheral membrane protein {ECO:0000269|PubMed:11278875}. Lipid droplet {ECO:0000250}. Note=Predominantly cytosolic; becomes enriched at membranes upon calcium binding. Translocates from the cytosol to the plasma membrane when stimulated by IL13/interleukin-13 and in macrophages binding apoptotic cells. SUBUNIT: Interacts with PEBP1; in response to IL13/interleukin-13, prevents the interaction of PEBP1 with RAF1 to activate the ERK signaling cascade. {ECO:0000250}. DOMAIN: The PLAT domain can bind calcium ions; this promotes association with membranes. {ECO:0000250}. TISSUE SPECIFICITY: Found in pituitary and pineal glands as well as leukocytes, kidney, aorta, small intestine and cornea. Also expressed by resident peritoneal macrophages (at protein level). {ECO:0000269|PubMed:15708862, ECO:0000269|PubMed:22503541, ECO:0000269|PubMed:8188678, ECO:0000269|PubMed:8798642}. +Q91ZP3 LPIN1_MOUSE Phosphatidate phosphatase LPIN1 (EC 3.1.3.4) (Fatty liver dystrophy protein) (Lipin-1) 924 102,002 Alternative sequence (1); Chain (1); Compositional bias (1); Cross-link (2); Modified residue (15); Motif (3); Mutagenesis (6); Natural variant (1); Region (2); Sequence conflict (5) FUNCTION: Plays important roles in controlling the metabolism of fatty acids at different levels. Acts as a magnesium-dependent phosphatidate phosphatase enzyme which catalyzes the conversion of phosphatidic acid to diacylglycerol during triglyceride, phosphatidylcholine and phosphatidylethanolamine biosynthesis. Acts also as nuclear transcriptional coactivator for PPARGC1A/PPARA regulatory pathway to modulate lipid metabolism gene expression. Is involved in adipocyte differentiation. Isoform 1 is recruited at the mitochondrion outer membrane and is involved in mitochondrial fission by converting phosphatidic acid to diacylglycerol. {ECO:0000269|PubMed:16950137}. PTM: Phosphorylated at multiple sites in response to insulin. Phosphorylation is controlled by the mTOR signaling pathway. Phosphorylation is decreased by epinephrine. Phosphorylation may not directly affect the catalytic activity but may regulate the localization. Dephosphorylated by the CTDNEP1-CNEP1R1 complex. {ECO:0000269|PubMed:17105729}.; PTM: Sumoylation is important in brain and is marginal in other tissues. Sumoylation facilitates nuclear localization of isoform 2 in neuronals cells and its transcriptional coactivator activity. {ECO:0000269|PubMed:19753306}. SUBCELLULAR LOCATION: Isoform 1: Mitochondrion outer membrane {ECO:0000269|PubMed:21397848}. Cytoplasm {ECO:0000269|PubMed:21397848}. Nucleus membrane {ECO:0000269|PubMed:21397848}. Note=Recruited at the mitochondrion outer membrane following phosphatidic acid formation mediated by PLD6. In neuronals cells, isoform 1 is exclusively cytoplasmic. In 3T3-L1 pre-adipocytes, it primarily located in the cytoplasm.; SUBCELLULAR LOCATION: Isoform 2: Nucleus. Cytoplasm. Endoplasmic reticulum membrane. Note=Nuclear localization requires both CNEP1R1 and CTDNEP1. In neuronals cells, localized in both the cytoplasm and the nucleus. In 3T3-L1 pre-adipocytes, it is predominantly nuclear. SUBUNIT: Interacts (via LXXIL motif) with PPARA. Interacts with PPARGC1A. Interaction with PPARA and PPARGC1A leads to the formation of a complex that modulates gene transcription. Interacts with MEF2C. {ECO:0000269|PubMed:16950137, ECO:0000269|PubMed:19753306}. DOMAIN: Contains one Asp-Xaa-Asp-Xaa-Thr (DXDXT) motif, a catalytic motif essential for phosphatidate phosphatase activity.; DOMAIN: Contains one Leu-Xaa-Xaa-Ile-Leu (LXXIL), a transcriptional binding motif, which mediates interaction with PPARA. TISSUE SPECIFICITY: Specifically expressed in skeletal muscle. Also expressed prominently in adipose tissue, and testis. Lower expression also detected in kidney, lung, brain and liver. Isoform 1 is the predominant isoform in the liver. Isoform 2 is the major form in the brain. {ECO:0000269|PubMed:16049017, ECO:0000269|PubMed:17158099, ECO:0000269|PubMed:19753306, ECO:0000269|PubMed:22134922}. DISEASE: Note=Defects in Lpin1 are the cause of the fatty liver dystrophy phenotype (fld). Fld mutant mices are characterized by neonatal fatty liver and hypertriglyceridemia that resolve at weaning, and neuropathy affecting peripheral nerve in adulthood. Adipose tissue deficiency, glucose intolerance and increased susceptibility to atherosclerosis are associated with this mutation too. Two independent mutant alleles are characterized in this phenotype, fld and fld2j. +Q9ESF4 LFG1_MOUSE Protein lifeguard 1 (Glutamate [NMDA] receptor-associated protein 1) (NMDA receptor glutamate-binding subunit) 345 38,408 Chain (1); Compositional bias (1); Transmembrane (7) TRANSMEM 139 159 Helical. {ECO:0000255}.; TRANSMEM 171 191 Helical. {ECO:0000255}.; TRANSMEM 202 222 Helical. {ECO:0000255}.; TRANSMEM 227 247 Helical. {ECO:0000255}.; TRANSMEM 257 277 Helical. {ECO:0000255}.; TRANSMEM 281 301 Helical. {ECO:0000255}.; TRANSMEM 320 340 Helical. {ECO:0000255}. FUNCTION: Potential apoptotic regulator. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q4KL25 LHPL5_MOUSE LHFPL tetraspan subfamily member 5 protein (Lipoma HMGIC fusion partner-like 5 protein) (Tetraspan membrane protein of hair cell stereocilia) 219 24,186 Chain (1); Natural variant (1); Topological domain (5); Transmembrane (4) TRANSMEM 25 45 Helical. {ECO:0000255}.; TRANSMEM 99 119 Helical. {ECO:0000255}.; TRANSMEM 129 149 Helical. {ECO:0000255}.; TRANSMEM 179 199 Helical. {ECO:0000255}. TOPO_DOM 1 24 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 46 98 Extracellular. {ECO:0000255}.; TOPO_DOM 120 128 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 150 178 Extracellular. {ECO:0000255}.; TOPO_DOM 200 219 Cytoplasmic. {ECO:0000255}. FUNCTION: In the inner ear, may be a component of the hair cell's mechanotransduction machinery that functionally couples PCDH15 to the transduction channel. Regulates transducer channel conductance and is required for fast channel adaptation. {ECO:0000269|PubMed:15905332, ECO:0000269|PubMed:23217710}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23217710}; Multi-pass membrane protein {ECO:0000255}. Note=Efficient localization to the plasma membrane requires the presence of PCDH15. {ECO:0000269|PubMed:23217710}. SUBUNIT: Found in a complex with TMIE and PCDH15 (PubMed:25467981). Interacts with PCDH15; this interaction is required for efficient localization to hair bundles (PubMed:23217710). Interacts with TOMT (PubMed:28504928). {ECO:0000269|PubMed:23217710, ECO:0000269|PubMed:25467981, ECO:0000269|PubMed:28504928}. TISSUE SPECIFICITY: Brain, inner ear hair cells and vestibular neuroepithelia of the inner ear (PubMed:16459341, PubMed:23217710, PubMed:15905332). In inner ear, expressed in stereocilia in a punctate pattern and at the tip-link region (at protein level) (PubMed:16459341, PubMed:23217710, PubMed:15905332). Strongly expressed in brain (PubMed:26964900). Weakly expressed in heart, testis and intestine (PubMed:26964900). {ECO:0000269|PubMed:15905332, ECO:0000269|PubMed:16459341, ECO:0000269|PubMed:23217710, ECO:0000269|PubMed:26964900}. DISEASE: Note=Defects in Lhfpl5 are the cause of the hurry-scurry (hscy) phenotype which is characterized by rapid circling behavior, frequent shaking of head from side to side, deafness and vestibular dysfunction. {ECO:0000269|PubMed:15905332}. +Q9CPU0 LGUL_MOUSE Lactoylglutathione lyase (EC 4.4.1.5) (Aldoketomutase) (Glyoxalase I) (Glx I) (Ketone-aldehyde mutase) (Methylglyoxalase) (S-D-lactoylglutathione methylglyoxal lyase) 184 20,810 Active site (1); Beta strand (11); Binding site (5); Chain (1); Disulfide bond (1); Domain (1); Helix (9); Initiator methionine (1); Metal binding (4); Modified residue (6); Region (1); Sequence conflict (1); Turn (1) Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 1/2. FUNCTION: Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. Involved in the regulation of TNF-induced transcriptional activity of NF-kappa-B. Required for normal osteoclastogenesis. {ECO:0000269|PubMed:18695250}. PTM: Glutathionylation at Cys-139 inhibits enzyme activity. {ECO:0000250}.; PTM: Phosphorylated at Thr-107 in the presence of CaMK2. However, this is a consensus site for phosphorylation by CK2 so phosphorylation may be mediated by CK2 rather than CaMK2. Phosphorylation is induced by TNF and suppresses the TNF-induced transcriptional activity of NF-kappa-B (By similarity). {ECO:0000250}.; PTM: Exists in a nitric oxide (NO)-modified form. The exact nature of the modification is unknown, but it suppresses the TNF-induced transcriptional activity of NF-kappa-B (By similarity). {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000269|PubMed:18695250}. +P63006 LHX1_MOUSE LIM/homeobox protein Lhx1 (LIM homeobox protein 1) (Homeobox protein Lim-1) 406 44,780 Chain (1); DNA binding (1); Domain (2); Modified residue (1); Mutagenesis (2); Sequence conflict (4) FUNCTION: Potential transcription factor. May play a role in early mesoderm formation and later in lateral mesoderm differentiation and neurogenesis. {ECO:0000269|PubMed:7904966}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:8793615}. SUBUNIT: Interacts with LDB1 via the tandem LIM domains. {ECO:0000269|PubMed:8918878, ECO:0000269|PubMed:9468533}. DOMAIN: The LIM domains exert a negative regulatory function and disruption of the LIM domains produces an activated form. In addition, two activation domains and a negative regulatory domain exist C-terminally to the homeobox (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: In mid to late stage embryos, expressed in a restricted region of mesoderm in the primitive streak. At 7.5 days, expressed in a horseshoe shape at the periphery of the node, as well as along both sides of the adjacent notochord. Also present in presumptive lateral and intermediate mesoderm. Later, expression become progressively restricted to intermediate mesoderm, and the developing excretory system including the pronephric region, mesonephros, nephric duct and metanephros. In the metanephros, strongly expressed in renal vesicles and S-shaped and coma-shaped bodies, as well as in the ureteric bud and its derivatives. Also expressed in the dorsal root ganglia. By stage 10.5, also expressed in regions of the central nervous system in the telencephalon through to the spinal cord. In adults, expressed in the cerebellum/medulla and kidney, and at very low levels in the cerebrum. {ECO:0000269|PubMed:7904966, ECO:0000269|PubMed:7909459, ECO:0000269|PubMed:8793615}. +P42703 LIFR_MOUSE Leukemia inhibitory factor receptor (LIF receptor) (LIF-R) (D-factor/LIF receptor) (CD antigen CD118) 1092 122,574 Alternative sequence (2); Chain (1); Disulfide bond (5); Domain (6); Glycosylation (16); Modified residue (2); Motif (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 829 853 Helical. {ECO:0000255}. TOPO_DOM 44 828 Extracellular. {ECO:0000255}.; TOPO_DOM 854 1092 Cytoplasmic. {ECO:0000255}. FUNCTION: Signal-transducing molecule. May have a common pathway with IL6ST. The soluble form inhibits the biological activity of LIF by blocking its binding to receptors on target cells. SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Isoform 2: Secreted. SUBUNIT: Heterodimer composed of LIFR and IL6ST. The heterodimer formed by LIFR and IL6ST interacts with the complex formed by CNTF and CNTFR (By similarity). {ECO:0000250}. DOMAIN: The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.; DOMAIN: The box 1 motif is required for JAK interaction and/or activation. TISSUE SPECIFICITY: Placenta, liver, kidney, heart, lung, brain, and embryos. The liver may be the primary site of synthesis of the secreted form. +P50481 LHX3_MOUSE LIM/homeobox protein Lhx3 (LIM homeobox protein 3) (Homeobox protein LIM-3) (Homeobox protein P-LIM) 400 44,010 Alternative sequence (1); Beta strand (9); Chain (1); DNA binding (1); Domain (2); Helix (4); Modified residue (4); Sequence conflict (4); Turn (4) FUNCTION: Required for the establishment of the specialized cells of the pituitary gland and the nervous system (By similarity). Involved in the development of interneurons and motor neurons in cooperation with LDB1 and ISL1. Acts as a transcriptional activator. Binds to and activates the promoter of the alpha-glycoprotein gene, and synergistically enhances transcription from the prolactin promoter in cooperation with Pou1f1/Pit-1. {ECO:0000250, ECO:0000269|PubMed:10593900, ECO:0000269|PubMed:12150931}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Interacts with POU1F1 (By similarity). At neuronal promoters, interacts with LDB1, in motor neurons LDB1 is displaced by ISL1 and a ternary complex is formed in which ISL1 contacts both LHX3 and LDB1 (PubMed:12150931, PubMed:18583962). {ECO:0000250|UniProtKB:Q9UBR4, ECO:0000269|PubMed:12150931, ECO:0000269|PubMed:18583962}. DOMAIN: The LIM domain specifically interacts with the Pit-1 POU domain and is required for synergistic interactions with Pit-1, but not for basal transcriptional activation events. TISSUE SPECIFICITY: Mostly expressed in the pituitary anterior and intermediate lobes of the adult mouse. It is also expressed in the pineal gland and transiently in the primordia of motor neurons including the spinal cord, pons and medulla oblongata. +Q9D1T0 LIGO1_MOUSE Leucine-rich repeat and immunoglobulin-like domain-containing nogo receptor-interacting protein 1 (Leucine-rich repeat neuronal protein 1) (Leucine-rich repeat neuronal protein 6A) 614 69,101 Chain (1); Disulfide bond (5); Domain (3); Glycosylation (8); Modified residue (1); Repeat (11); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 556 576 Helical. {ECO:0000255}. TOPO_DOM 36 555 Extracellular. {ECO:0000255}.; TOPO_DOM 577 614 Cytoplasmic. {ECO:0000255}. FUNCTION: Functional component of the Nogo receptor signaling complex (RTN4R/NGFR) in RhoA activation responsible for some inhibition of axonal regeneration by myelin-associated factors. Is also an important negative regulator of oligodentrocyte differentiation and axonal myelination (By similarity). Acts in conjunction with RTN4 and RTN4R in regulating neuronal precursor cell motility during cortical development. {ECO:0000250|UniProtKB:Q96FE5, ECO:0000269|PubMed:20093372, ECO:0000305|PubMed:22923615}. PTM: N-glycosylated. Contains predominantly high-mannose glycans (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18186492}; Single-pass type I membrane protein {ECO:0000269|PubMed:18186492}. SUBUNIT: Homotetramer. Forms a ternary complex with RTN4R/NGFR and RTN4R/TNFRSF19 (By similarity). Interacts with NGRF and MYT1L (PubMed:18186492). Interacts with RTN4R (PubMed:18186492, PubMed:22923615). {ECO:0000250|UniProtKB:Q96FE5, ECO:0000269|PubMed:18186492, ECO:0000269|PubMed:22923615}. DOMAIN: The intracellular domain of LINGO1 interacts with MYT1L. {ECO:0000269|PubMed:18186492}. TISSUE SPECIFICITY: Highly specific expression in the central nervous system. Predominant expression in neocortex, amygdala, hippocampus, thalamus and entorhinal cortex, with lower levels in cerebellum and basal nuclei. {ECO:0000269|PubMed:14686891, ECO:0000269|PubMed:18186492}. +Q91XD2 LIMS2_MOUSE LIM and senescent cell antigen-like-containing domain protein 2 (Particularly interesting new Cys-His protein 2) (PINCH-2) 341 39,031 Chain (1); Domain (5); Modified residue (1) FUNCTION: Adapter protein in a cytoplasmic complex linking beta-integrins to the actin cytoskeleton, bridges the complex to cell surface receptor tyrosine kinases and growth factor receptors. {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000269|PubMed:12651156}. Cell membrane {ECO:0000269|PubMed:12651156}; Peripheral membrane protein {ECO:0000269|PubMed:12651156}; Cytoplasmic side {ECO:0000269|PubMed:12651156}. SUBUNIT: Interacts with integrin-linked protein kinase 1 (ILK) via the first LIM domain, and in competition with LIMS1. Part of the heterotrimeric IPP complex composed of integrin-linked kinase (ILK), LIMS1 or LIMS2, and PARVA (By similarity). Interacts with TGFB1I1. {ECO:0000250, ECO:0000269|PubMed:16737959}. TISSUE SPECIFICITY: Detected in heart, lung, kidney, liver, urinary bladder, fat, skin, skeletal muscle, uterus, large intestine and testis. {ECO:0000269|PubMed:12651156}. +Q8C8U0 LIPB1_MOUSE Liprin-beta-1 (Protein tyrosine phosphatase receptor type f polypeptide-interacting protein-binding protein 1) (PTPRF-interacting protein-binding protein 1) 969 108,540 Alternative sequence (2); Beta strand (1); Chain (1); Coiled coil (1); Cross-link (1); Domain (3); Erroneous initiation (1); Helix (21); Modified residue (16); Sequence conflict (5); Turn (4) FUNCTION: May regulate the disassembly of focal adhesions. Did not bind receptor-like tyrosine phosphatases type 2A (By similarity). {ECO:0000250}. SUBUNIT: Forms homodimers and heterodimers. Interacts with S100A4 in a calcium-dependent mode (By similarity). {ECO:0000250}. DOMAIN: The N-terminal coiled coil regions mediate homodimerization preferentially and heterodimerization type beta/beta. The C-terminal, non-coiled coil regions mediate heterodimerization type beta/alpha and interaction with S100A4 (By similarity). {ECO:0000250}. +Q3U4B4 LIPN_MOUSE Lipase member N (EC 3.1.1.-) (Lipase-like abhydrolase domain-containing protein 4) 400 45,744 Active site (3); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (1); Signal peptide (1) FUNCTION: Plays a highly specific role in the last step of keratinocyte differentiation. May have an essential function in lipid metabolism of the most differentiated epidermal layers (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +P97484 LIRB3_MOUSE Leukocyte immunoglobulin-like receptor subfamily B member 3 (LIR-3) (Leukocyte immunoglobulin-like receptor 3) (Cell-surface glycoprotein p91) (Paired immunoglobulin-like receptor B) (PIR-B) 841 93,054 Chain (1); Disulfide bond (5); Domain (6); Glycosylation (2); Modified residue (4); Motif (3); Mutagenesis (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 643 663 Helical. {ECO:0000255}. TOPO_DOM 25 642 Extracellular. {ECO:0000255}.; TOPO_DOM 664 841 Cytoplasmic. {ECO:0000255}. FUNCTION: May act as receptor for class I MHC antigens. Becomes activated upon coligation of LILRB3 and immune receptors, such as FCGR2B and the B-cell receptor. Down-regulates antigen-induced B-cell activation by recruiting phosphatases to its immunoreceptor tyrosine-based inhibitor motifs (ITIM). {ECO:0000269|PubMed:10327049, ECO:0000269|PubMed:10611342, ECO:0000269|PubMed:9482905}. PTM: Phosphorylated on tyrosine residues by LYN. Phosphorylation at Tyr-794 and Tyr-824 is important for interaction with PTPN6/SHP-1 and PTPN11/SHP-2. {ECO:0000269|PubMed:10327049, ECO:0000269|PubMed:10611342}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10327049, ECO:0000269|PubMed:9054430, ECO:0000269|PubMed:9482905}; Single-pass type I membrane protein {ECO:0000269|PubMed:10327049, ECO:0000269|PubMed:9054430, ECO:0000269|PubMed:9482905}. SUBUNIT: Interacts with LYN, PTPN6/SHP-1 and PTPN11/SHP-2. {ECO:0000269|PubMed:10327049, ECO:0000269|PubMed:10611342, ECO:0000269|PubMed:9482905}. DOMAIN: Contains 3 copies of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is involved in modulation of cellular responses. The phosphorylated ITIM motif can bind the SH2 domain of several SH2-containing phosphatases, including PTPN6/SHP-1, resulting in the dephosphorylation of the downstream protein kinases SYK and BTK. {ECO:0000269|PubMed:10327049}. TISSUE SPECIFICITY: Detected in macrophages, splenocytes and B lymphocytes (at protein level). Detected in macrophages, mast cells, splenocytes, peritoneal cells and natural killer cells. {ECO:0000269|PubMed:10611342, ECO:0000269|PubMed:9054430}. +Q64281 LIRB4_MOUSE Leukocyte immunoglobulin-like receptor subfamily B member 4 (Mast cell surface glycoprotein Gp49B) (CD antigen CD85k) 335 37,544 Alternative sequence (2); Chain (1); Disulfide bond (2); Domain (2); Glycosylation (2); Motif (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 239 260 Helical. {ECO:0000255}. TOPO_DOM 24 238 Extracellular. {ECO:0000255}.; TOPO_DOM 261 335 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for class I MHC antigens. Involved in the down-regulation of the immune response and the development of tolerance. Interferes with TNFRSF5-signaling and NF-kappa-B up-regulation. Inhibits receptor-mediated phosphorylation of cellular proteins and mobilization of intracellular calcium ions (By similarity). {ECO:0000250}. PTM: Phosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Ligand binding leads to internalization and translocation to an antigen-processing compartment. {ECO:0000250}. SUBUNIT: Binds PTPN6 when phosphorylated. {ECO:0000250}. DOMAIN: Contains 2 copies of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is involved in modulation of cellular responses. The phosphorylated ITIM motif can bind the SH2 domain of several SH2-containing phosphatases. +Q8VEE1 LMCD1_MOUSE LIM and cysteine-rich domains protein 1 365 40,996 Chain (1); Compositional bias (1); Domain (3); Modified residue (1) FUNCTION: Transcriptional cofactor that restricts GATA6 function by inhibiting DNA-binding, resulting in repression of GATA6 transcriptional activation of downstream target genes. Represses GATA6-mediated trans activation of lung- and cardiac tissue-specific promoters. Inhibits DNA-binding by GATA4 and GATA1 to the cTNC promoter. Plays a critical role in the development of cardiac hypertrophy via activation of calcineurin/nuclear factor of activated T-cells signaling pathway. {ECO:0000269|PubMed:16199866, ECO:0000269|PubMed:20026769}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16199866}. Nucleus {ECO:0000269|PubMed:16199866}. Note=May shuttle between the cytoplasm and the nucleus. SUBUNIT: Interacts with beta-dystroglycan (By similarity). Interacts with GATA1, GATA4 and GATA6. {ECO:0000250, ECO:0000269|PubMed:16199866}. DOMAIN: The LIM zinc-binding domains and the Cys-rich region mediate interaction with GATA6. {ECO:0000269|PubMed:16199866}. TISSUE SPECIFICITY: Expressed in distal airway epithelium of the lung, vascular smooth muscle, and myocardium. {ECO:0000269|PubMed:16199866}. +P14733 LMNB1_MOUSE Lamin-B1 588 66,786 Chain (1); Compositional bias (1); Cross-link (12); Disulfide bond (1); Domain (2); Initiator methionine (1); Lipidation (1); Modified residue (24); Motif (1); Propeptide (1); Region (7); Sequence conflict (2) FUNCTION: Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin. PTM: B-type lamins undergo a series of modifications, such as farnesylation and phosphorylation. Increased phosphorylation of the lamins occurs before envelope disintegration and probably plays a role in regulating lamin associations. SUBCELLULAR LOCATION: Nucleus inner membrane; Lipid-anchor; Nucleoplasmic side. SUBUNIT: Homodimer. Interacts with lamin-associated polypeptides IA, IB and 2. Interacts with SPAG4 and SEPT12 (By similarity). {ECO:0000250|UniProtKB:P20700}. +Q7TQ95 LNP_MOUSE Endoplasmic reticulum junction formation protein lunapark (ER junction formation factor lunapark) (Protein ulnaless) 425 47,500 Chain (1); Coiled coil (2); Compositional bias (1); Erroneous initiation (1); Frameshift (1); Initiator methionine (1); Lipidation (1); Modified residue (11); Topological domain (3); Transmembrane (2); Zinc finger (1) TRANSMEM 46 66 Helical. {ECO:0000255}.; TRANSMEM 78 98 Helical. {ECO:0000255}. TOPO_DOM 2 45 Cytoplasmic. {ECO:0000250|UniProtKB:Q9C0E8}.; TOPO_DOM 67 77 Lumenal. {ECO:0000250|UniProtKB:Q9C0E8}.; TOPO_DOM 99 425 Cytoplasmic. {ECO:0000250|UniProtKB:Q9C0E8}. FUNCTION: Endoplasmic reticulum (ER)-shaping membrane protein that plays a role in determining ER morphology. Involved in the stabilization of nascent three-way ER tubular junctions within the ER network. May also play a role as a curvature-stabilizing protein within three-way ER tubular junction network. May be involved in limb and central nervous system development (PubMed:12732147). {ECO:0000250|UniProtKB:Q9C0E8, ECO:0000269|PubMed:12732147}. PTM: Myristoylated; myristoylation is necessary for the endoplasmic reticulum (ER) three-way ER tubular junction formation, but is not required neither for membrane translocation, membrane topology formation, nor for the specific localization to ER membranes. {ECO:0000250|UniProtKB:Q9C0E8}.; PTM: Phosphorylated. Phosphorylation occurs at Ser-177, Ser-182, Ser-222, Ser-316 and Ser-380 during interphase. Phosphorylation occurs at Ser-114, Ser-153, Ser-194, Thr-211 and Ser-348 during mitosis; these phosphorylations reduce both its homodimerization and the ER three-way tubular junction formation. {ECO:0000250|UniProtKB:Q9C0E8}.; PTM: Subject to proteasomal degradation following phosphorylation during mitosis. {ECO:0000250|UniProtKB:Q9C0E8}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9C0E8}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9C0E8}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9C0E8}. Note=Localizes at endoplasmic reticulum (ER) three-way tubular junctions, which represent crossing-points at which the tubules build a polygonal network. {ECO:0000250|UniProtKB:Q9C0E8}. SUBUNIT: Homodimer; homodimerization requires the C4-type zinc finger motif and decreases during mitosis in a phosphorylation-dependent manner. {ECO:0000250|UniProtKB:Q9C0E8}. DOMAIN: The transmembrane domain 1 and 2 function as a signal-anchor and stop-transfer sequence, respectively, generating a double-spanning integral membrane protein with a N- and C-terminal cytoplasmic orientation. Transmembrane domain 1 and 2 are probably sufficient to mediate membrane translocation and topology formation in a N-myristoylation-independent manner. Transmembrane domain 2 is sufficient to block the protein secretion pathway. The two coiled-coil domains are necessary for its endoplasmic reticulum (ER) three-way tubular junction localization. The C4-type zinc finger motif is necessary both for its ER three-way tubular junction localization and formation. {ECO:0000250|UniProtKB:Q9C0E8}. TISSUE SPECIFICITY: Expressed in most tissues at basal level, with reinforcement in distal limb buds, genital bud, and in parts of the central nervous system. {ECO:0000269|PubMed:12732147}. +P61969 LMO4_MOUSE LIM domain transcription factor LMO4 (Breast tumor autoantigen) (LIM domain only protein 4) (LMO-4) 165 17,994 Beta strand (8); Chain (1); Domain (2); Helix (5); Turn (5) FUNCTION: Probable transcriptional factor. SUBUNIT: Interacts strongly with LDBS. Interacts with CLIM1 and CLIM2. Interacts (via the LIM zinc-binding domain 1) with RBBP8. Interacts with BRCA1 (via the BRCT domains); the interaction represses BRCA1 transcriptional activity. Interacts with DEAF1; LMO4 blocks export from nucleus. {ECO:0000269|PubMed:11751867, ECO:0000269|PubMed:12727888, ECO:0000269|PubMed:15343268, ECO:0000269|PubMed:17001033, ECO:0000269|PubMed:22723967}. TISSUE SPECIFICITY: Expressed in a wide variety of tissues. +Q91XL2 LNX2_MOUSE Ligand of Numb protein X 2 (Numb-binding protein 2) 687 75,129 Chain (1); Domain (4); Motif (1); Mutagenesis (1); Sequence conflict (1); Zinc finger (1) SUBUNIT: Interacts with the phosphotyrosine interaction domain of NUMB. {ECO:0000269|PubMed:11922143}. DOMAIN: The NPXY motif is required for the interaction with the PID domain of NUMB. It is however not sufficient. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11922143}. +Q3UHZ5 LMOD2_MOUSE Leiomodin-2 (Cardiac leiomodin) (C-LMOD) (Leiomodin) 550 62,018 Chain (1); Coiled coil (1); Compositional bias (2); Domain (1); Erroneous initiation (1); Modified residue (4); Region (4); Sequence conflict (1) FUNCTION: Mediates nucleation of actin filaments and thereby promotes actin polymerization (By similarity). Plays a role in the regulation of actin filament length (PubMed:26487682). Required for normal sarcomere organization in the heart, and for normal heart function (PubMed:26487682, PubMed:27274810). {ECO:0000250|UniProtKB:Q6P5Q4, ECO:0000269|PubMed:26487682, ECO:0000269|PubMed:27274810}. SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere {ECO:0000250|UniProtKB:Q6P5Q4}. Cytoplasm, myofibril {ECO:0000250|UniProtKB:Q6P5Q4}. Cytoplasm, myofibril, sarcomere, M line {ECO:0000250|UniProtKB:Q6P5Q4}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q6P5Q4}. Note=Colocalizes with actin filaments in sarcomeres. Detected close to the M line. {ECO:0000250|UniProtKB:Q6P5Q4}. SUBUNIT: Can bind at least three actin monomers and thereby provides a nucleus for actin filament formation. Interacts (via N-terminus) with tropomyosin alpha (TPM1) (via N-terminus). May also interact with TPM2 (via N-terminus) (PubMed:17572376). {ECO:0000250|UniProtKB:Q6P5Q4, ECO:0000269|PubMed:17572376}. TISSUE SPECIFICITY: Detected in neonate heart (at protein level) (PubMed:26487682). Detected in embryonic heart and in pharyngeal arches (PubMed:26487682). Detected in adult heart (PubMed:27274810). {ECO:0000269|PubMed:26487682, ECO:0000269|PubMed:27274810}. +E9QA62 LMOD3_MOUSE Leiomodin-3 571 65,689 Chain (1); Coiled coil (1); Compositional bias (2); Domain (1); Erroneous initiation (1); Sequence conflict (4) FUNCTION: Essential for the organization of sarcomeric actin thin filaments in skeletal muscle (PubMed:25774500, PubMed:26035871). Increases the rate of actin polymerization (By similarity). {ECO:0000250|UniProtKB:Q0VAK6, ECO:0000269|PubMed:26035871}. PTM: Ubiquitinated, leading to its degradation. Interaction with KLHL40 negatively regulates ubiquitination and degradation. {ECO:0000269|PubMed:24960163}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q0VAK6}. Cytoplasm, myofibril, sarcomere, A band {ECO:0000269|PubMed:24960163}. Cytoplasm, myofibril, sarcomere, M line {ECO:0000250|UniProtKB:Q0VAK6}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q0VAK6}. Note=Highly expressed in nonstriated areas of developing myotubes, where it shows a granular cytoplasmic pattern. In sarcomeres, highly expressed in the M band region and, at lower levels, along actin thin filaments. Not detected in Z-disks. In sarcomeres, may be located near, but not at, actin thin filament pointed end. {ECO:0000250|UniProtKB:Q0VAK6}. SUBUNIT: May interact with tropomyosin alpha (TPM1/2) N-terminus (By similarity). Interacts with KLHL40; leading to stabilization (PubMed:24960163). {ECO:0000250|UniProtKB:Q0VAK6, ECO:0000269|PubMed:24960163}. TISSUE SPECIFICITY: Skeletal muscle and heart-specific (at protein level). {ECO:0000269|PubMed:25774500}. +P60469 LIPA3_MOUSE Liprin-alpha-3 (Protein tyrosine phosphatase receptor type f polypeptide-interacting protein alpha-3) (PTPRF-interacting protein alpha-3) 1194 133,426 Alternative sequence (1); Chain (1); Coiled coil (4); Domain (3); Helix (1); Modified residue (15) FUNCTION: May regulate the disassembly of focal adhesions. May localize receptor-like tyrosine phosphatases type 2A at specific sites on the plasma membrane, possibly regulating their interaction with the extracellular environment and their association with substrates. {ECO:0000250|UniProtKB:O75145}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q91Z79}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:23124857}. Note=Also detected in epididymosome. {ECO:0000250|UniProtKB:Q91Z79}. SUBUNIT: Forms homodimers and heterodimers with liprins-alpha and liprins-beta. Interacts with the second PTPase domain of PTPRD, PTPRF and PTPRS. Binds RIMS1, RIMS2, RIMS3 and RIMS4. {ECO:0000250|UniProtKB:O75145, ECO:0000250|UniProtKB:Q91Z79}. DOMAIN: The N-terminal coiled coil regions mediate homodimerization preferentially and heterodimerization type alpha/alpha. The C-terminal, non-coiled coil regions mediate heterodimerization type alpha/beta and interaction with PTPRD, PTPRF and PTPRS. {ECO:0000250|UniProtKB:O75145}. TISSUE SPECIFICITY: Detected in sperm (at protein level). {ECO:0000269|PubMed:23124857}. +Q1PSW8 LIN41_MOUSE E3 ubiquitin-protein ligase TRIM71 (EC 2.3.2.27) (Protein lin-41 homolog) (mLin41) (RING-type E3 ubiquitin transferase TRIM71) (Tripartite motif-containing protein 71) 855 92,054 Chain (1); Coiled coil (2); Compositional bias (1); Initiator methionine (1); Modified residue (1); Mutagenesis (2); Repeat (7); Zinc finger (3) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that cooperates with the microRNAs (miRNAs) machinery and promotes embryonic stem cells proliferation and maintenance (PubMed:19898466). Binds to miRNAs and associates with AGO2, participating in post-transcriptional repression of transcripts such as CDKN1A. Facilitates the G1-S transition to promote rapid embryonic stem cell self-renewal by repressing CDKN1A expression (PubMed:22735451). In addition, participates in post-transcriptional mRNA repression in a miRNA independent mechanism (PubMed:23125361). Required to maintain proliferation and prevent premature differentiation of neural progenitor cells during early neural development: positively regulates FGF signaling by controlling the stability of SHCBP1 (PubMed:22735451). Specific regulator of miRNA biogenesis. miRNA Binds MIR29A hairpin and postranscriptionally modulates MIR29A levels, which indirectly regulates TET proteins expression (By similarity). {ECO:0000250|UniProtKB:Q2Q1W2, ECO:0000269|PubMed:19898466, ECO:0000269|PubMed:22735451, ECO:0000269|PubMed:23125361}. PTM: Autoubiquitinated. {ECO:0000269|PubMed:22508726}. SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:19898466, ECO:0000269|PubMed:22508726, ECO:0000269|PubMed:22735451}. SUBUNIT: Interacts (via NHL repeats) with AGO2; the interaction increases in presence of RNA (PubMed:19898466, PubMed:22508726, PubMed:22735451). Interacts with HSP90AA1. Interacts (via NHL repeats) with MOV10, PABPC1, PUM1, PUM2, STAU2, XRN1 and XRN2 in an RNA-dependent manner (By similarity). Interacts with SHCBP1; leading to enhance its stability (PubMed:22508726). {ECO:0000250|UniProtKB:Q2Q1W2, ECO:0000269|PubMed:19898466, ECO:0000269|PubMed:22508726, ECO:0000269|PubMed:22735451}. DOMAIN: The NHL domain, containing the 6 NHL repeats, is necessary and sufficient to target RNA but not to repress mRNA. The minimal region needed to execute repression consists of the coiled coil domain and the Filamin repeat. The RING-type domain is dispensable for mRNA repression. {ECO:0000250|UniProtKB:Q2Q1W2}. TISSUE SPECIFICITY: Highly expressed in undifferentiated embryonic stem cells (ESCs). Expressed in the epiblast and in interfollicular epidermal stem cells during early development. Also expressed in male germ cells and in the reproductive tract. Highly expressed in neuroepithelial cells, and its expression declines as neurogenesis proceeds (at protein level). Expressed in ependymal cells of the brain (PubMed:25883935). {ECO:0000269|PubMed:19898466, ECO:0000269|PubMed:22508726, ECO:0000269|PubMed:22735451, ECO:0000269|PubMed:25883935}. +Q8BM14 LIPK_MOUSE Lipase member K (EC 3.1.1.-) (Lipase-like abhydrolase domain-containing protein 2) 398 45,243 Active site (3); Alternative sequence (1); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (2); Sequence conflict (1); Signal peptide (1) FUNCTION: Plays a highly specific role in the last step of keratinocyte differentiation. May have an essential function in lipid metabolism of the most differentiated epidermal layers (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +P63005 LIS1_MOUSE Platelet-activating factor acetylhydrolase IB subunit alpha (Lissencephaly-1 protein) (LIS-1) (PAF acetylhydrolase 45 kDa subunit) (PAF-AH 45 kDa subunit) (PAF-AH alpha) (PAFAH alpha) 410 46,670 Alternative sequence (1); Beta strand (30); Chain (1); Coiled coil (1); Domain (1); Helix (6); Modified residue (2); Mutagenesis (9); Region (6); Repeat (7); Turn (5) FUNCTION: Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes such as the maintenance of Golgi integrity, the peripheral transport of microtubule fragments and the coupling of the nucleus and centrosome. Required during brain development for the proliferation of neuronal precursors and the migration of newly formed neurons from the ventricular/subventricular zone toward the cortical plate. Neuronal migration involves a process called nucleokinesis, whereby migrating cells extend an anterior process into which the nucleus subsequently translocates. During nucleokinesis dynein at the nuclear surface may translocate the nucleus towards the centrosome by exerting force on centrosomal microtubules. Also required for proper activation of Rho GTPases and actin polymerization at the leading edge of locomoting cerebellar neurons and postmigratory hippocampal neurons in response to calcium influx triggered via NMDA receptors. May also play a role in other forms of cell locomotion including the migration of fibroblasts during wound healing. Non-catalytic subunit of an acetylhydrolase complex which inactivates platelet-activating factor (PAF) by removing the acetyl group at the SN-2 position. Required for dynein recruitment to microtubule plus ends and BICD2-bound cargos (By similarity). {ECO:0000250|UniProtKB:P43034, ECO:0000255|HAMAP-Rule:MF_03141, ECO:0000269|PubMed:11056530, ECO:0000269|PubMed:11344260, ECO:0000269|PubMed:12796778, ECO:0000269|PubMed:12911752, ECO:0000269|PubMed:14507966, ECO:0000269|PubMed:14578885, ECO:0000269|PubMed:14691133, ECO:0000269|PubMed:15173193, ECO:0000269|PubMed:15473966, ECO:0000269|PubMed:16107726, ECO:0000269|PubMed:16203747, ECO:0000269|PubMed:16369480, ECO:0000269|PubMed:16481446}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle. Nucleus membrane {ECO:0000255|HAMAP-Rule:MF_03141}. Note=May localize to the nuclear membrane (By similarity). Localizes to the plus end of microtubules and to the centrosome. Redistributes to axons during neuronal development. Also localizes to the microtubules of the manchette in elongating spermatids and to the meiotic spindle in spermatocytes. {ECO:0000250}. SUBUNIT: Interacts with DISC1, and this interaction is enhanced by NDEL1 (By similarity). Component of cytosolic PAF-AH IB, which is composed of PAFAH1B1 (alpha), PAFAH1B2 (beta) and PAFAH1B3 (gamma) subunits. Trimer formation is not essential for the catalytic activity of the enzyme which is contributed solely by the PAFAH1B2 (beta) and PAFAH1B3 (gamma) subunits. Can self-associate. Interacts with DCX, dynein, dynactin, IQGAP1, KATNB1, NDE1, NDEL1, NUDC, and RSN. Interacts with DAB1 when DAB1 is phosphorylated in response to RELN/reelin signaling. Interacts with ASUN. Interacts with DCDC1 (By similarity). {ECO:0000250|UniProtKB:P43034, ECO:0000269|PubMed:11001923, ECO:0000269|PubMed:11056530, ECO:0000269|PubMed:11163258, ECO:0000269|PubMed:11163259, ECO:0000269|PubMed:11163260, ECO:0000269|PubMed:11231056, ECO:0000269|PubMed:11344260, ECO:0000269|PubMed:11940666, ECO:0000269|PubMed:12885786, ECO:0000269|PubMed:14578885, ECO:0000269|PubMed:15173193, ECO:0000269|PubMed:15473966, ECO:0000269|PubMed:15473967, ECO:0000269|PubMed:15572112, ECO:0000269|PubMed:16203747, ECO:0000269|PubMed:16291865, ECO:0000269|PubMed:16369480, ECO:0000269|PubMed:16481446, ECO:0000269|PubMed:23097494}. DOMAIN: Dimerization mediated by the LisH domain may be required to activate dynein. {ECO:0000255|HAMAP-Rule:MF_03141, ECO:0000269|PubMed:15274919, ECO:0000269|PubMed:16258276}. TISSUE SPECIFICITY: Highly expressed in brain, particularly the hippocampus and the olfactory bulb. Also highly expressed in testis, including all seminiferous tubule cell types, all types of spermatogenic and Sertoli cells, and meiotically dividing and elongating spermatids. Expressed at lower levels in heart, kidney, large intestine, liver, lung, ovary, small intestine and spleen. {ECO:0000269|PubMed:11163259, ECO:0000269|PubMed:11163260, ECO:0000269|PubMed:12551946}. +Q8BLB7 LMBL3_MOUSE Lethal(3)malignant brain tumor-like protein 3 (L(3)mbt-like protein 3) (MBT-1) 883 99,137 Alternative sequence (3); Chain (1); Compositional bias (1); Cross-link (1); Domain (1); Repeat (3); Sequence conflict (2); Zinc finger (1) FUNCTION: Putative Polycomb group (PcG) protein. PcG proteins maintain the transcriptionally repressive state of genes, probably via a modification of chromatin, rendering it heritably changed in its expressibility (By similarity). Required for normal maturation of myeloid progenitor cells. {ECO:0000250, ECO:0000269|PubMed:15889154}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15889154}. SUBUNIT: Interacts with RNF2. {ECO:0000269|PubMed:15889154}. TISSUE SPECIFICITY: Detected in hematopoietic progenitor cells in fetal liver. Detected in adult bone marrow, heart, brain, spleen, lung, liver, kidney and testis. {ECO:0000269|PubMed:15889154}. +Q0VET5 LMTD2_MOUSE Lamin tail domain-containing protein 2 664 73,784 Chain (1); Coiled coil (1); Domain (1) +Q80YE4 LMTK1_MOUSE Serine/threonine-protein kinase LMTK1 (EC 2.7.11.1) (Apoptosis-associated tyrosine kinase) (AATYK) (Brain apoptosis-associated tyrosine kinase) (Lemur tyrosine kinase 1) 1365 144,607 Active site (1); Alternative sequence (4); Binding site (1); Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (1); Modified residue (8); Mutagenesis (1); Nucleotide binding (1); Sequence conflict (8); Transmembrane (1) TRANSMEM 32 52 Helical. {ECO:0000255}. FUNCTION: May be involved in neuronal differentiation. {ECO:0000250}. PTM: Autophosphorylated. Phosphorylated by CDK5 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:17651901}; Single-pass type I membrane protein {ECO:0000269|PubMed:17651901}. Cytoplasm {ECO:0000269|PubMed:17651901}. Cytoplasm, perinuclear region {ECO:0000250}. Cell projection, dendrite {ECO:0000269|PubMed:17651901}. Cell projection, axon {ECO:0000269|PubMed:17651901}. Cell projection, growth cone {ECO:0000269|PubMed:17651901}. Note=Predominantly perinuclear. {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 2: Membrane. Note=Peripheral membrane protein.; SUBCELLULAR LOCATION: Isoform 3: Membrane; Single-pass type I membrane protein. SUBUNIT: Interacts with CDK5. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain, and, to a lower extent, in kidney, heart, lung and skeletal muscle. In the brain, expressed in the olfactory bulb, cerebellum, striatum, hippocampal formation, thalamus, hypothalamus, and pontine nuclei (at protein level). {ECO:0000269|PubMed:11314039, ECO:0000269|PubMed:11314040, ECO:0000269|PubMed:17651901, ECO:0000269|PubMed:9444961}. +Q9JKU8 LMX1A_MOUSE LIM homeobox transcription factor 1-alpha (LIM/homeobox protein 1.1) (LMX-1.1) (LIM/homeobox protein LMX1A) 382 42,857 Chain (1); Compositional bias (2); DNA binding (1); Domain (2) FUNCTION: Acts as a transcriptional activator by binding to an A/T-rich sequence, the FLAT element, in the insulin gene promoter. Required for development of the roof plate and, in turn, for specification of dorsal cell fates in the CNS and developing vertebrae. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. DISEASE: Note=Defects in Lmx1a are the cause of the spontaneous neurologic mutant mouse, called 'dreher' (dr) and results from a failure of the roof plate to develop. +P21619 LMNB2_MOUSE Lamin-B2 596 67,318 Alternative sequence (1); Chain (1); Compositional bias (1); Cross-link (4); Domain (2); Erroneous initiation (2); Lipidation (1); Modified residue (10); Motif (1); Propeptide (1); Region (7); Sequence conflict (8) FUNCTION: Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin. PTM: B-type lamins undergo a series of modifications, such as farnesylation and phosphorylation. Increased phosphorylation of the lamins occurs before envelope disintegration and probably plays a role in regulating lamin associations. SUBCELLULAR LOCATION: Nucleus inner membrane; Lipid-anchor; Nucleoplasmic side. SUBUNIT: Interacts with TMEM43. {ECO:0000269|PubMed:18230648}. TISSUE SPECIFICITY: Isoform B3 is germ cell specific. +Q9DBH5 LMAN2_MOUSE Vesicular integral-membrane protein VIP36 (Lectin mannose-binding 2) (Vesicular integral-membrane protein 36) (VIP36) 358 40,430 Binding site (3); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (1); Metal binding (4); Region (2); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 325 347 Helical. {ECO:0000255}. TOPO_DOM 47 324 Lumenal. {ECO:0000255}.; TOPO_DOM 348 358 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a role as an intracellular lectin in the early secretory pathway. Interacts with N-acetyl-D-galactosamine and high-mannose type glycans and may also bind to O-linked glycans. Involved in the transport and sorting of glycoproteins carrying high mannose-type glycans (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. +Q9WV07 LOXE3_MOUSE Hydroperoxide isomerase ALOXE3 (EC 5.4.4.7) (Epidermis-type lipoxygenase 3) (Epidermal LOX-3) (e-LOX-3) (eLOX-3) (Hydroperoxy icosatetraenoate dehydratase) (EC 4.2.1.152) 711 80,473 Chain (1); Domain (2); Metal binding (5); Sequence conflict (3) Lipid metabolism; hydroperoxy eicosatetraenoic acid biosynthesis. Lipid metabolism; sphingolipid metabolism. FUNCTION: Non-heme iron-containing lipoxygenase which is atypical in that it displays a prominent hydroperoxide isomerase activity and a reduced dioxygenase activity compared to other lipoxygenases. The hydroperoxide isomerase activity catalyzes the isomerization of hydroperoxides, derived from arachidonic and linoleic acid by ALOX12B, into hepoxilin-type epoxyalcohols. The dioxygenase activity requires a step of activation of the enzyme by molecular oxygen. In presence of oxygen, oxygenates polyunsaturated fatty acids, including arachidonic acid, to produce fatty acid hydroperoxides. In the skin, acts downstream of ALOX12B on the linoleate moiety of esterified omega-hydroxyacyl-sphingosine (EOS) ceramides to produce an epoxy-ketone derivative, a crucial step in the conjugation of omega-hydroxyceramide to membrane proteins. Therefore plays a crucial role in the synthesis of corneocytes lipid envelope and the establishment of the skin barrier to water loss. In parallel, it may have a signaling function in barrier formation through the production of hepoxilins metabolites. Plays also a role in adipocyte differentiation through hepoxilin A3 and hepoxilin B3 production which in turn activate PPARG. Through the production of hepoxilins in the spinal cord, it may regulate inflammatory tactile allodynia. {ECO:0000269|PubMed:17045234, ECO:0000269|PubMed:20530198, ECO:0000269|PubMed:22832496}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00726}. TISSUE SPECIFICITY: Skin specific. +Q9EQ31 LPAR3_MOUSE Lysophosphatidic acid receptor 3 (LPA receptor 3) (LPA-3) (Lysophosphatidic acid receptor Edg-7) 354 40,316 Chain (1); Glycosylation (2); Lipidation (1); Topological domain (8); Transmembrane (7) TRANSMEM 32 52 Helical; Name=1. {ECO:0000255}.; TRANSMEM 68 88 Helical; Name=2. {ECO:0000255}.; TRANSMEM 102 124 Helical; Name=3. {ECO:0000255}.; TRANSMEM 147 167 Helical; Name=4. {ECO:0000255}.; TRANSMEM 187 207 Helical; Name=5. {ECO:0000255}.; TRANSMEM 241 261 Helical; Name=6. {ECO:0000255}.; TRANSMEM 277 295 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 31 Extracellular. {ECO:0000255}.; TOPO_DOM 53 67 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 89 101 Extracellular. {ECO:0000255}.; TOPO_DOM 125 146 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 168 186 Extracellular. {ECO:0000255}.; TOPO_DOM 208 240 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 262 276 Extracellular. {ECO:0000255}.; TOPO_DOM 296 354 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for lysophosphatidic acid (LPA), a mediator of diverse cellular activities. Seems to be coupled to the G(i)/G(o) and G(q) families of heteromeric G proteins. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Most abundantly expressed in testes, kidney, and lung, with moderate levels in small intestine, and low levels in heart, stomach, spleen, and adult and perinatal brain. Little or no expression in embryonic brain, liver, or thymus. +P11369 LORF2_MOUSE LINE-1 retrotransposable element ORF2 protein (ORF2p) (Long interspersed element-1) (L1) (Retrovirus-related Pol polyprotein LINE-1) [Includes: Reverse transcriptase (EC 2.7.7.49); Endonuclease (EC 3.1.21.-)] 1281 149,581 Chain (1); Domain (2); Frameshift (1); Metal binding (3); Region (1); Sequence conflict (7) FUNCTION: Has a reverse transcriptase activity required for target-primed reverse transcription of the LINE-1 element mRNA, a crucial step in LINE-1 retrotransposition. Has also an endonuclease activity that allows the introduction of nicks in the chromosomal target DNA. Cleaves DNA in AT-rich regions between a 5' stretch of purines and a 3' stretch of pyrimidines, corresponding to sites of LINE-1 integration in the genome. SUBUNIT: Interacts with MOV10. {ECO:0000269|PubMed:28662698}. +P58022 LOXL2_MOUSE Lysyl oxidase homolog 2 (EC 1.4.3.13) (Lysyl oxidase-like protein 2) 776 87,003 Alternative sequence (2); Chain (1); Cross-link (1); Disulfide bond (17); Domain (4); Glycosylation (4); Metal binding (9); Modified residue (1); Mutagenesis (1); Region (1); Sequence conflict (2); Signal peptide (1) FUNCTION: Mediates the post-translational oxidative deamination of lysine residues on target proteins leading to the formation of deaminated lysine (allysine) (By similarity). Acts as a transcription corepressor and specifically mediates deamination of trimethylated 'Lys-4' of histone H3 (H3K4me3), a specific tag for epigenetic transcriptional activation (By similarity). Shows no activity against histone H3 when it is trimethylated on 'Lys-9' (H3K9me3) or 'Lys-27' (H3K27me3) or when 'Lys-4' is monomethylated (H3K4me1) or dimethylated (H3K4me2) (By similarity). Also mediates deamination of methylated TAF10, a member of the transcription factor IID (TFIID) complex, which induces release of TAF10 from promoters, leading to inhibition of TFIID-dependent transcription (By similarity). LOXL2-mediated deamination of TAF10 results in transcriptional repression of genes required for embryonic stem cell pluripotency including POU5F1/OCT4, NANOG, KLF4 and SOX2 (PubMed:25959397). Involved in epithelial to mesenchymal transition (EMT) via interaction with SNAI1 and participates in repression of E-cadherin, probably by mediating deamination of histone H3 (By similarity). During EMT, involved with SNAI1 in negatively regulating pericentromeric heterochromatin transcription (By similarity). SNAI1 recruits LOXL2 to pericentromeric regions to oxidize histone H3 and repress transcription which leads to release of heterochromatin component CBX5/HP1A, enabling chromatin reorganization and acquisition of mesenchymal traits (By similarity). Interacts with the endoplasmic reticulum protein HSPA5 which activates the IRE1-XBP1 pathway of the unfolded protein response, leading to expression of several transcription factors involved in EMT and subsequent EMT induction (By similarity). When secreted into the extracellular matrix, promotes cross-linking of extracellular matrix proteins by mediating oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin (By similarity). Acts as a regulator of sprouting angiogenesis, probably via collagen IV scaffolding (By similarity). Acts as a regulator of chondrocyte differentiation, probably by regulating expression of factors that control chondrocyte differentiation (PubMed:21071451). {ECO:0000250|UniProtKB:Q9Y4K0, ECO:0000269|PubMed:21071451, ECO:0000269|PubMed:25959397}. PTM: The lysine tyrosylquinone cross-link (LTQ) is generated by condensation of the epsilon-amino group of a lysine with a topaquinone produced by oxidation of tyrosine. {ECO:0000250|UniProtKB:Q9Y4K0}.; PTM: N-glycosylated. N-glycosylation on Asn-458 and Asn-646 may be essential for proper folding and secretion; may be composed of a fucosylated carbohydrates attached to a trimannose N-linked glycan core. {ECO:0000250|UniProtKB:Q9Y4K0}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000250|UniProtKB:Q9Y4K0}. Nucleus {ECO:0000250|UniProtKB:Q9Y4K0}. Chromosome {ECO:0000250|UniProtKB:Q9Y4K0}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9Y4K0}. Note=Associated with chromatin. It is unclear how LOXL2 is nuclear as it contains a signal sequence and has been shown to be secreted. However, a number of reports confirm its intracellular location and its key role in transcription regulation. {ECO:0000250|UniProtKB:Q9Y4K0}. SUBUNIT: Component of some chromatin repressor complex. Interacts with SNAI1. Interacts with TAF10. Interacts with HSPA5. {ECO:0000250|UniProtKB:Q9Y4K0}. TISSUE SPECIFICITY: Ubiquitous. Highest expression in skin, lung and thymus. Present in chondrocytes: mainly expressed by chondrocytes in healing fractures and in epiphyseal growth plates (at protein level). {ECO:0000269|PubMed:21071451}. +A0JNU3 LPP60_MOUSE 60 kDa lysophospholipase (EC 3.1.1.5) [Includes: L-asparaginase (EC 3.5.1.1) (L-asparagine amidohydrolase); Platelet-activating factor acetylhydrolase (PAF acetylhydrolase) (EC 3.1.1.47)] 564 60,595 Active site (1); Chain (1); Domain (1); Modified residue (1); Region (3); Repeat (5) FUNCTION: Exhibits lysophospholipase, transacylase, PAF acetylhydrolase and asparaginase activities. SUBUNIT: Monomer. {ECO:0000250}. +Q8BFW7 LPP_MOUSE Lipoma-preferred partner homolog 613 65,891 Alternative sequence (7); Chain (1); Compositional bias (1); Cross-link (1); Domain (3); Modified residue (6); Sequence conflict (6) FUNCTION: May play a structural role at sites of cell adhesion in maintaining cell shape and motility. In addition to these structural functions, it may also be implicated in signaling events and activation of gene transcription. May be involved in signal transduction from cell adhesion sites to the nucleus allowing successful integration of signals arising from soluble factors and cell-cell adhesion sites. Also suggested to serve as a scaffold protein upon which distinct protein complexes are assembled in the cytoplasm and in the nucleus (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell junction {ECO:0000250}. Note=Found in the nucleus, in the cytoplasm and at cell adhesion sites. {ECO:0000250}. SUBUNIT: Interacts with VASP, with PDZ domains of SCRIB and with ACTN1/alpha-actinin. {ECO:0000250}. +Q3V0L5 LRC43_MOUSE Leucine-rich repeat-containing protein 43 667 74,942 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (1); Repeat (4) +Q91YK0 LRC49_MOUSE Leucine-rich repeat-containing protein 49 (Tubulin polyglutamylase complex subunit 4) (PGs4) (p79) 686 78,876 Alternative sequence (3); Chain (1); Coiled coil (1); Domain (1); Frameshift (1); Repeat (7); Sequence conflict (2) SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SUBUNIT: Part of the neuronal tubulin polyglutamylase complex which contains TPGS1, TPGS2, TTLL1, LRRC49 and NICN1. +Q80XU8 LRFN4_MOUSE Leucine-rich repeat and fibronectin type-III domain-containing protein 4 636 67,252 Chain (1); Disulfide bond (1); Domain (4); Glycosylation (6); Modified residue (2); Motif (1); Repeat (7); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 519 539 Helical. {ECO:0000255}. TOPO_DOM 17 518 Extracellular. {ECO:0000255}.; TOPO_DOM 540 636 Cytoplasmic. {ECO:0000255}. FUNCTION: Promotes neurite outgrowth in hippocampal neurons. May play a role in redistributing DLG4 to the cell periphery. {ECO:0000269|PubMed:16828986, ECO:0000269|PubMed:18585462}. PTM: Glycosylated. {ECO:0000269|PubMed:16828986}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:16828986, ECO:0000269|PubMed:18227064}; Single-pass type I membrane protein {ECO:0000269|PubMed:16828986, ECO:0000269|PubMed:18227064}. SUBUNIT: Can form heteromeric complexes with LRFN1, LRFN2, LRFN3 and LRFN5. Unable to form homophilic interactions across cell junctions. Interacts with DLG1, DLG2 and DLG3 (By similarity). Also interacts with DLG4. {ECO:0000250, ECO:0000269|PubMed:16828986, ECO:0000269|PubMed:18227064}. DOMAIN: The PDZ-binding motif is required for neurite outgrowth promotion. This motif is also involved in DLG1-, DLG3- and DLG4-binding (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain and testis. In the brain, weak, but broad expression in the cerebral cortex and diencephalic nuclei. Also detected in other parts of the central nervous system, including the olfactory bulb, pons, cerebellum, and medulla oblongata, as well as in the peripheral nervous system, such as the ganglia of cranial nerves and the dorsal root ganglion during gestation. {ECO:0000269|PubMed:16828986}. +Q8BMT4 LRC33_MOUSE Transforming growth factor beta activator LRRC33 (Leucine-rich repeat-containing protein 33) (Negative regulator of reactive oxygen species) 693 77,140 Alternative sequence (2); Chain (1); Disulfide bond (2); Domain (2); Erroneous initiation (1); Frameshift (2); Glycosylation (11); Mutagenesis (2); Repeat (21); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 652 672 Helical. {ECO:0000255}. TOPO_DOM 20 651 Extracellular. {ECO:0000305}.; TOPO_DOM 673 693 Cytoplasmic. {ECO:0000305}. FUNCTION: Key regulator of transforming growth factor beta-1 (TGFB1) specifically required for microglia function in the nervous system (PubMed:29909984). Required for activation of latent TGF-beta-1 in macrophages and microglia: associates specifically via disulfide bonds with the Latency-associated peptide (LAP), which is the regulatory chain of TGFB1, and regulates integrin-dependent activation of TGF-beta-1 (PubMed:29909984). TGF-beta-1 activation mediated by LRRC33/NRROS is highly localized: there is little spreading of TGF-beta-1 activated from one microglial cell to neighboring microglia, suggesting the existence of localized and selective activation of TGF-beta-1 by LRRC33/NRROS (PubMed:29909984). Indirectly plays a role in Toll-like receptor (TLR) signaling: ability to inhibit TLR-mediated NF-kappa-B activation and cytokine production is probably a consequence of its role in TGF-beta-1 signaling (Probable). {ECO:0000269|PubMed:29909984, ECO:0000305|PubMed:24550525, ECO:0000305|PubMed:29909984}. PTM: N-glycosylated. {ECO:0000269|PubMed:29909984}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24739962, ECO:0000269|PubMed:29909984}; Single-pass type I membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:24739962}; Single-pass type I membrane protein {ECO:0000255}. SUBUNIT: Interacts with TGFB1; associates via disulfide bonds with the Latency-associated peptide chain (LAP) regulatory chain of TGFB1, leading to regulate activation of TGF-beta-1 (PubMed:29909984). Interacts (via LRR repeats) with TLR2, TLR3, TLR4, TLR9 and probably other Toll-like receptors (By similarity). Interacts with CYBB/NOX2; the interaction is direct (PubMed:24739962). {ECO:0000250|UniProtKB:Q86YC3, ECO:0000269|PubMed:24739962, ECO:0000269|PubMed:29909984}. TISSUE SPECIFICITY: Mainly expressed in cells of hematopoietic origin, such as in immune organs such as lymph nodes, thymus and spleen (PubMed:24739962, PubMed:29909984). Among leukocytes, expressed at higher level in myeloid cell such as macrophages, neutrophils and dendritic cells (PubMed:24739962). Highly expressed in central nervous system-resident macrophages, including microglia and perivascular macrophages (PubMed:28459434, PubMed:29909984). {ECO:0000269|PubMed:24739962, ECO:0000269|PubMed:28459434, ECO:0000269|PubMed:29909984}. +Q3UY51 LRC55_MOUSE Leucine-rich repeat-containing protein 55 (BK channel auxiliary gamma subunit LRRC55) 298 33,030 Chain (1); Compositional bias (1); Disulfide bond (4); Domain (2); Repeat (5); Signal peptide (1); Transmembrane (1) TRANSMEM 259 279 Helical. {ECO:0000255}. FUNCTION: Auxiliary protein of the large-conductance, voltage and calcium-activated potassium channel (BK alpha). Modulates gating properties by producing a marked shift in the BK channel's voltage dependence of activation in the hyperpolarizing direction, and in the absence of calcium (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with KCNMA1. {ECO:0000250}. DOMAIN: The transmembrane domain is necessary for interaction with KCNMA1. {ECO:0000250}. +Q9DAM1 LRC34_MOUSE Leucine-rich repeat-containing protein 34 415 46,635 Chain (1); Repeat (2) FUNCTION: Highly expressed in stem cells where it may be involved in regulation of pluripotency. In embryonic stem cells (ESCs), important for normal expression of the pluripotency regulators POU5F1/OCT4 and KLF4. Also important for expression of the ectodermal marker gene NES and the endodermal marker gene GATA4. Promotes stem cell proliferation in vitro. {ECO:0000269|PubMed:24991885}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24435972, ECO:0000269|PubMed:24991885}. Nucleus, nucleolus {ECO:0000269|PubMed:24991885}. Cytoplasm {ECO:0000269|PubMed:24435972, ECO:0000269|PubMed:24991885}. Note=As stem cells differentiate, translocates from the nucleolus to the nucleus and then to the cytoplasm. Colocalizes with NPM1 and NCL in the nucleolus. {ECO:0000269|PubMed:24991885}. SUBUNIT: Interacts with NPM1 and NCL. {ECO:0000269|PubMed:24991885}. TISSUE SPECIFICITY: Expressed in testis where it specifically localizes to germ cells (at protein level) (PubMed:24435972, PubMed:24991885). Not detected in other tissues tested (at protein level) (PubMed:24435972, PubMed:24991885). Expressed in pluripotent embryonic stem cells and multipotent adult germline stem cells (PubMed:24991885). {ECO:0000269|PubMed:24435972, ECO:0000269|PubMed:24991885}. +Q9JI18 LRP1B_MOUSE Low-density lipoprotein receptor-related protein 1B (LRP-1B) (Low-density lipoprotein receptor-related protein-deleted in tumor) (LRP-DIT) 4599 513,634 Chain (1); Disulfide bond (140); Domain (54); Glycosylation (46); Motif (2); Repeat (34); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 4445 4467 Helical. {ECO:0000255}. TOPO_DOM 21 4444 Extracellular. {ECO:0000255}.; TOPO_DOM 4468 4599 Cytoplasmic. {ECO:0000255}. FUNCTION: Potential cell surface proteins that bind and internalize ligands in the process of receptor-mediated endocytosis. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Binds LRPAP1, PLAU, PLAT and SERPINE1; binding is followed by internalization and degradation of the ligands. {ECO:0000250}. +Q8VC16 LRC14_MOUSE Leucine-rich repeat-containing protein 14 493 54,969 Chain (1); Repeat (9); Sequence caution (1); Sequence conflict (6) FUNCTION: Negatively regulates Toll-like receptor-mediated NF-kappa-B signaling by disrupting IKK core complex formation through interaction with IKBKB. {ECO:0000250|UniProtKB:Q15048}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q15048}. SUBUNIT: Interacts with IKBKB; disrupts IKBKB-IKBKG interaction preventing I-kappa-B-kinase (IKK) core complex formation and leading to a decrease of IKBKB phosphorylation and NF-kappaB activation. Interacts with CHUK. {ECO:0000250|UniProtKB:Q15048}. +Q80X72 LRC15_MOUSE Leucine-rich repeat-containing protein 15 579 64,177 Chain (1); Domain (2); Glycosylation (2); Repeat (15); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 537 557 Helical. {ECO:0000255}. TOPO_DOM 22 536 Extracellular. {ECO:0000255}.; TOPO_DOM 558 579 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q9D4C6 LR2BP_MOUSE LRP2-binding protein 346 39,746 Alternative sequence (1); Chain (1); Frameshift (1); Repeat (7); Sequence conflict (1) FUNCTION: May act as an adapter that regulates LRP2 function. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Detected in a vesicular staining pattern close to the plasma membrane and throughout the cytoplasm. {ECO:0000250}. SUBUNIT: Interacts with LRP2. {ECO:0000250}. +Q8BHA1 LRC24_MOUSE Leucine-rich repeat-containing protein 24 521 56,334 Chain (1); Compositional bias (1); Disulfide bond (1); Domain (3); Glycosylation (3); Repeat (6); Signal peptide (1); Transmembrane (1) TRANSMEM 414 434 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q9D3W5 LRC71_MOUSE Leucine-rich repeat-containing protein 71 558 61,351 Chain (1); Erroneous termination (1); Repeat (4) +Q80YS5 LRC27_MOUSE Leucine-rich repeat-containing protein 27 523 59,853 Chain (1); Coiled coil (2); Erroneous initiation (2); Repeat (5) +Q8CH62 LTO1_MOUSE Protein LTO1 homolog (Oral cancer-overexpressed protein 1 homolog) 137 15,221 Chain (1); Erroneous initiation (3); Initiator methionine (1); Modified residue (1); Region (1); Sequence conflict (1) FUNCTION: The complex LTO1:YAE1 functions as a target specific adapter that probably recruits apo-ABCE1 to the cytosolic iron-sulfur protein assembly (CIA) complex machinery. May be required for biogenesis of the large ribosomal subunit and initiation of translation. May play a role in the regulation of proline metabolism and ROS production. {ECO:0000250|UniProtKB:Q8WV07}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P53846}. SUBUNIT: Forms a complex with YAE1. Interacts with PYCR1 and PYCR2. {ECO:0000250|UniProtKB:Q8WV07}. +Q9CQ20 M1IP1_MOUSE Mid1-interacting protein 1 (Gastrulation-specific G12-like protein) (Mid1-interacting G12-like protein) (Protein STRAIT11499 homolog) (Spot 14-related protein) (S14R) (Spot 14-R) 182 20,356 Chain (1); Erroneous initiation (1); Modified residue (4); Sequence conflict (1) FUNCTION: Plays a role in the regulation of lipogenesis in liver. Up-regulates ACACA enzyme activity. Required for efficient lipid biosynthesis, including triacylglycerol, diacylglycerol and phospholipid. Involved in stabilization of microtubules. {ECO:0000269|PubMed:15070402, ECO:0000269|PubMed:20457939, ECO:0000269|PubMed:20952656}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15070402}. Cytoplasm {ECO:0000269|PubMed:15070402, ECO:0000269|PubMed:20457939}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15070402}. Note=Associated with microtubules (PubMed:15070402). SUBUNIT: Homodimer in the absence of THRSP. Heterodimer with THRSP. The homodimer interacts with ACACA and ACACB. Promotes polymerization of Acetyl-CoA carboxylase to form complexes that contain MID1IP1 and ACACA and/or ACACB. Interaction with THRSP interferes with ACACA binding. {ECO:0000269|PubMed:15070402, ECO:0000269|PubMed:20457939, ECO:0000269|PubMed:20952656}. TISSUE SPECIFICITY: During embryonic development, expressed mainly in the neuroepithelial midline, urogenital apparatus and digits. Detected in adult white fat, liver, heart, brain and kidney. Expressed at very low levels in lactating mammary gland. {ECO:0000269|PubMed:15070402, ECO:0000269|PubMed:15890771, ECO:0000269|PubMed:20457939}. +Q99N05 M4A4D_MOUSE Membrane-spanning 4-domains subfamily A member 4D 225 23,859 Chain (1); Topological domain (5); Transmembrane (4) TRANSMEM 43 63 Helical. {ECO:0000255}.; TRANSMEM 74 94 Helical. {ECO:0000255}.; TRANSMEM 114 134 Helical. {ECO:0000255}.; TRANSMEM 149 169 Helical. {ECO:0000255}. TOPO_DOM 1 42 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 64 73 Extracellular. {ECO:0000255}.; TOPO_DOM 95 113 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 135 148 Extracellular. {ECO:0000255}.; TOPO_DOM 170 225 Cytoplasmic. {ECO:0000255}. FUNCTION: May be involved in signal transduction as a component of a multimeric receptor complex. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed in thymus, spleen, peripheral lymph node, liver, kidney, heart, colon, lung, and testes. +Q99N10 M4A8_MOUSE Membrane-spanning 4-domains subfamily A member 8 (CD20 antigen-like 5) (Membrane-spanning 4-domains subfamily A member 8A) 290 30,858 Alternative sequence (1); Chain (1); Sequence caution (1); Sequence conflict (5); Topological domain (5); Transmembrane (4) TRANSMEM 109 129 Helical. {ECO:0000255}.; TRANSMEM 139 159 Helical. {ECO:0000255}.; TRANSMEM 175 195 Helical. {ECO:0000255}.; TRANSMEM 221 241 Helical. {ECO:0000255}. TOPO_DOM 1 108 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 130 138 Extracellular. {ECO:0000255}.; TOPO_DOM 160 174 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 196 220 Extracellular. {ECO:0000255}.; TOPO_DOM 242 290 Cytoplasmic. {ECO:0000255}. FUNCTION: May be involved in signal transduction as a component of a multimeric receptor complex. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed strongly in intestine and colon and minimally in lung and ovary. {ECO:0000269|PubMed:11245982}. +O54790 MAFG_MOUSE Transcription factor MafG (V-maf musculoaponeurotic fibrosarcoma oncogene homolog G) 162 17,877 Beta strand (1); Chain (1); Cross-link (2); Domain (1); Helix (4); Modified residue (5); Region (2); Turn (4) FUNCTION: Since they lack a putative transactivation domain, the small Mafs behave as transcriptional repressors when they dimerize among themselves (PubMed:16738329, PubMed:9679061). However, they seem to serve as transcriptional activators by dimerizing with other (usually larger) basic-zipper proteins, such as NFE2, NFE2L1 and NFE2L2, and recruiting them to specific DNA-binding sites (PubMed:16738329, PubMed:9679061). Small Maf proteins heterodimerize with Fos and may act as competitive repressors of the NFE2L2 transcription factor. Transcription factor, component of erythroid-specific transcription factor NFE2L2. Activates globin gene expression when associated with NFE2L2 (By similarity). May be involved in signal transduction of extracellular H(+) (By similarity). {ECO:0000250|UniProtKB:O15525, ECO:0000250|UniProtKB:Q76MX4}. PTM: Sumoylation at Lys-14 is required for active transcriptional repression. {ECO:0000269|PubMed:16738329}.; PTM: Acetylated in erythroid cells by CREB-binding protein (CBP). Acetylation augments the DNA-binding activity of NFE2, but has no effect on binding NFE2. {ECO:0000250|UniProtKB:O15525}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O15525, ECO:0000255|PROSITE-ProRule:PRU00978}. SUBUNIT: Homodimer or heterodimer. Homodimerization leads to transcriptional repression. Forms high affinity heterodimers with members of the CNC-bZIP family such as NFE2, NFE2L1/NRF1, NFE2L2/NRF2 and NFE2L3/NRF3. Interacts with CREBBP; the interaction leads to acetylation of the basic region of MAFG and stimulation of NFE2 transcriptional activity through increased DNA binding. {ECO:0000250|UniProtKB:O15525}. +Q80XI6 M3K11_MOUSE Mitogen-activated protein kinase kinase kinase 11 (EC 2.7.11.25) (Mixed lineage kinase 3) 850 93,226 Active site (1); Binding site (1); Chain (1); Compositional bias (3); Domain (2); Modified residue (22); Nucleotide binding (1); Region (2); Sequence conflict (2) FUNCTION: Activates the JUN N-terminal pathway. Required for serum-stimulated cell proliferation and for mitogen and cytokine activation of MAPK14 (p38), MAPK3 (ERK) and MAPK8 (JNK1) through phosphorylation and activation of MAP2K4/MKK4 and MAP2K7/MKK7. Plays a role in mitogen-stimulated phosphorylation and activation of BRAF, but does not phosphorylate BRAF directly. Influences microtubule organization during the cell cycle (By similarity). {ECO:0000250}. PTM: Autophosphorylation on serine and threonine residues within the activation loop plays a role in enzyme activation. Thr-278 is likely to be the main autophosphorylation site. Phosphorylation of Ser-556 and Ser-557 is induced by CDC42 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Location is cell cycle dependent. {ECO:0000250}. SUBUNIT: Homodimer; undergoes dimerization during activation. Interacts with MAP2K4/MKK4 and MAP2K7/MKK7 (By similarity). Found in a complex with SH3RF1, RAC1, MAP2K7/MKK7, MAPK8IP1/JIP1 and MAPK8/JNK1 (PubMed:23963642). {ECO:0000250|UniProtKB:Q16584, ECO:0000250|UniProtKB:Q66HA1, ECO:0000269|PubMed:23963642}. +Q8BGS0 MAK16_MOUSE Protein MAK16 homolog (Protein RBM13) 296 35,185 Alternative sequence (1); Chain (1); Compositional bias (1); Cross-link (2); Modified residue (5); Sequence conflict (2) SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. +Q9CWG8 NDUF7_MOUSE Protein arginine methyltransferase NDUFAF7, mitochondrial (EC 2.1.1.320) (NADH dehydrogenase [ubiquinone] complex I, assembly factor 7) (Protein midA homolog) 436 48,385 Alternative sequence (1); Chain (1); Sequence conflict (6); Transit peptide (1) FUNCTION: Arginine methyltransferase involved in the assembly or stability of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I). Acts by mediating symmetric dimethylation of 'Arg-118' of NDUFS2 after it assembles into the complex I, stabilizing the early intermediate complex. {ECO:0000250|UniProtKB:Q7L592}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q7L592}. SUBUNIT: Interacts with NDUFS2. {ECO:0000250|UniProtKB:Q7L592}. +Q62073 M3K7_MOUSE Mitogen-activated protein kinase kinase kinase 7 (EC 2.7.11.25) (Transforming growth factor-beta-activated kinase 1) (TGF-beta-activated kinase 1) 579 64,228 Active site (1); Binding site (1); Chain (1); Compositional bias (1); Cross-link (3); Domain (1); Modified residue (7); Mutagenesis (4); Nucleotide binding (1); Region (1) FUNCTION: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. Plays an important role in the cascades of cellular responses evoked by changes in the environment. Mediates signal transduction of TRAF6, various cytokines including interleukin-1 (IL-1), transforming growth factor-beta (TGFB), TGFB-related factors like BMP2 and BMP4, toll-like receptors (TLR), tumor necrosis factor receptor CD40 and B-cell receptor (BCR) (PubMed:10748100, PubMed:16157589, PubMed:21183079, PubMed:29291351). Ceramides are also able to activate MAP3K7/TAK1. Once activated, acts as an upstream activator of the MKK/JNK signal transduction cascade and the p38 MAPK signal transduction cascade through the phosphorylation and activation of several MAP kinase kinases like MAP2K1/MEK1, MAP2K3/MKK3, MAP2K6/MKK6 and MAP2K7/MKK7. These MAP2Ks in turn activate p38 MAPKs, c-jun N-terminal kinases (JNKs) and I-kappa-B kinase complex (IKK). Both p38 MAPK and JNK pathways control the transcription factors activator protein-1 (AP-1), while nuclear factor-kappa B is activated by IKK (PubMed:16157589, PubMed:8533096, PubMed:29291351). MAP3K7 activates also IKBKB and MAPK8/JNK1 in response to TRAF6 signaling and mediates BMP2-induced apoptosis (PubMed:10748100). In osmotic stress signaling, plays a major role in the activation of MAPK8/JNK1, but not that of NF-kappa-B. Promotes TRIM5 capsid-specific restriction activity (By similarity). {ECO:0000250|UniProtKB:O43318, ECO:0000269|PubMed:10748100, ECO:0000269|PubMed:16157589, ECO:0000269|PubMed:21183079, ECO:0000269|PubMed:29291351, ECO:0000269|PubMed:8533096}. PTM: Association with TAB1/MAP3K7IP1 promotes autophosphorylation and subsequent activation. Association with TAB2/MAP3K7IP2, itself associated with free unanchored Lys-63 polyubiquitin chain, promotes autophosphorylation and subsequent activation of MAP3K7. Dephosphorylation at Thr-187 by PP2A and PPP6C leads to inactivation (By similarity). {ECO:0000250}.; PTM: 'Lys-48'-linked polyubiquitination at Lys-72 is induced by TNFalpha, and leads to proteasomal degradation (PubMed:16157589). Undergoes 'Lys-48'-linked polyubiquitination catalyzed by ITCH (PubMed:25632008). 'Lys-63'-linked polyubiquitination at Lys-158 by TRIM8 does not lead to proteasomal degradation but contributes to autophosphorylation and activation. Deubiquitinated by CYLD, a protease that selectively cleaves 'Lys-63'-linked ubiquitin chains (PubMed:17548520, PubMed:29291351). {ECO:0000250|UniProtKB:O43318, ECO:0000269|PubMed:16157589, ECO:0000269|PubMed:17548520, ECO:0000269|PubMed:25632008, ECO:0000269|PubMed:29291351}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Although the majority of MAP3K7/TAK1 is found in the cytosol, when complexed with TAB1/MAP3K7IP1 and TAB2/MAP3K7IP2, it is also localized at the cell membrane. {ECO:0000250}. SUBUNIT: Can form homodimer (By similarity). Binds both upstream activators and downstream substrates in multimolecular complexes (By similarity). Interacts with TAB1/MAP3K7IP1, TAB2/MAP3K7IP2 and TAB3/MAP3K7IP3 (By similarity). Identified in the TRIKA2 complex composed of MAP3K7/TAK1, TAB1/MAP3K7IP1 and TAB2/MAP3K7IP2 (By similarity). Interacts with PPM1L and PPM1B/PP2CB (PubMed:12556533). Interaction with PP2A and PPP6C leads to its repressed activity (By similarity). Interacts with TRAF6 and TAB1/MAP3K7IP1; during IL-1 signaling (By similarity). Interacts with TAOK1 and TAOK2; interaction with TAOK2 interferes with MAP3K7 interaction with IKKA, thus preventing NF-kappa-B activation (By similarity). Interacts with WDR34 (via WD domains) (By similarity). Interacts with CYLD and RBCK1 (PubMed:17548520). Interacts with TGFBR1; induces MAP3K7/TAK1 activation by TRAF6 (By similarity). Interacts with MAPK8IP1 and SMAD6 (PubMed:10748100, PubMed:17709393). Interacts with isoform 1 of VRK2 (PubMed:17709393). Interacts with DAB2; the interaction is induced by TGF-beta stimulation and may mediate TGF-beta stimulated JNK activation (By similarity). Interacts with TRIM5 (By similarity). Part of a complex containing ITCH, NDFIP1 and MAP3K7 (PubMed:25632008). Interacts with PLEKHM1 (via N- and C-terminus) (PubMed:27777970). Interacts with TRIM8 (By similarity). Found in a complex with SH3RF1, RAC2, MAP2K7/MKK7, MAPK8IP1/JIP1, MAPK8/JNK1 and MAPK9/JNK2 (PubMed:27084103). {ECO:0000250|UniProtKB:O43318, ECO:0000269|PubMed:10748100, ECO:0000269|PubMed:12556533, ECO:0000269|PubMed:17548520, ECO:0000269|PubMed:17709393, ECO:0000269|PubMed:25632008, ECO:0000269|PubMed:27084103, ECO:0000269|PubMed:27777970}. +Q91VD9 NDUS1_MOUSE NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial (EC 1.6.99.3) (EC 7.1.1.2) (Complex I-75kD) (CI-75kD) 727 79,777 Beta strand (27); Chain (1); Domain (3); Helix (21); Metal binding (12); Modified residue (5); Sequence conflict (2); Transit peptide (1); Turn (11) FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). This is the largest subunit of complex I and it is a component of the iron-sulfur (IP) fragment of the enzyme. It may form part of the active site crevice where NADH is oxidized (By similarity). {ECO:0000250}. PTM: Acetylation of Lys-84 is observed in liver mitochondria from fasted mice but not from fed mice. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}. Note=Matrix and cytoplasmic side of the mitochondrial inner membrane. {ECO:0000250}. SUBUNIT: Complex I is composed of 45 different subunits. {ECO:0000250}. +O09198 MAL_MOUSE Myelin and lymphocyte protein (T-lymphocyte maturation-associated protein) 153 16,596 Alternative sequence (1); Chain (1); Domain (1); Topological domain (5); Transmembrane (4) TRANSMEM 25 46 Helical. {ECO:0000255}.; TRANSMEM 54 75 Helical. {ECO:0000255}.; TRANSMEM 93 114 Helical. {ECO:0000255}.; TRANSMEM 126 147 Helical. {ECO:0000255}. TOPO_DOM 1 24 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 47 53 Extracellular. {ECO:0000255}.; TOPO_DOM 76 92 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 115 125 Extracellular. {ECO:0000255}.; TOPO_DOM 148 153 Cytoplasmic. {ECO:0000255}. FUNCTION: Could be an important component in vesicular trafficking cycling between the Golgi complex and the apical plasma membrane. Plays a role in the maintenance of the myelin sheath and in axon-glia and glia-glia interactions. {ECO:0000269|PubMed:15337780}. PTM: Lipoprotein. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane protein. Apical cell membrane; Multi-pass membrane protein. Note=Found in lipid raft. TISSUE SPECIFICITY: Expressed in the spinal cord, brain, kidney and gastrointestinal tract especially in the stomach and caecum. Highly expressed by myelinating glial cells. {ECO:0000269|PubMed:15337780}. +P35455 NEU2_MOUSE Vasopressin-neurophysin 2-copeptin (AVP-NPII) [Cleaved into: Arg-vasopressin (Arginine-vasopressin); Neurophysin 2 (Neurophysin-I); Copeptin] 168 17,900 Chain (1); Disulfide bond (8); Glycosylation (1); Modified residue (1); Peptide (2); Signal peptide (1); Site (1) FUNCTION: Neurophysin 2 specifically binds vasopressin.; FUNCTION: Vasopressin has a direct antidiuretic action on the kidney, it also causes vasoconstriction of the peripheral vessels. Acts by binding to vasopressin receptors (V1bR/AVPR1B, V1aR/AVPR1A, and V2R/AVPR2) (By similarity). {ECO:0000250|UniProtKB:P01185}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Interacts with vasopressin receptors V1bR/AVPR1B (Ki=85 pM), V1aR/AVPR1A (Ki=0.6 nM) and V2R/AVPR2 (Ki=4.9 nM) (By similarity). Interacts with oxytocin receptor (OXTR) (Ki=110 nM) (By similarity). {ECO:0000250|UniProtKB:P01185}. +Q7TT18 MCAF1_MOUSE Activating transcription factor 7-interacting protein 1 (ATFa-associated modulator) (mAM) (MBD1-containing chromatin-associated factor 1) 1306 138,593 Alternative sequence (2); Chain (1); Coiled coil (1); Compositional bias (3); Cross-link (4); Domain (2); Frameshift (1); Modified residue (12); Motif (1); Region (3); Sequence conflict (26) FUNCTION: Recruiter that couples transcriptional factors to general transcription apparatus and thereby modulates transcription regulation and chromatin formation. Can both act as an activator or a repressor depending on the context. Mediates MBD1-dependent transcriptional repression, probably by recruiting complexes containing SETDB1. Required to stimulate histone methyltransferase activity of SETDB1 and facilitate the conversion of dimethylated to trimethylated H3 'Lys-9' (H3K9me3). The complex formed with MBD1 and SETDB1 represses transcription and couples DNA methylation and histone H3 'Lys-9' trimethylation (H3K9me3). May have ATPase activity. {ECO:0000269|PubMed:10777215, ECO:0000269|PubMed:14536086}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10777215}. SUBUNIT: Interacts with MBD1; the interaction is enhanced when MBD1 is sumoylated. Probably forms a complex with SETDB1 and MBD1. Interacts with SUMO ubiquitin-like proteins (SUMO1, SUNO2 and SUMO3), with a preference for SUMO2 and SUMO3. Interacts with SP1 and ZHX1 (By similarity). Interacts with the general transcription machinery, including ERCC2, ERCC3, GTF2E1, GTF2E2 and POLR2A (By similarity). Interacts with SETDB1 and ATF7. {ECO:0000250, ECO:0000269|PubMed:14536086}. TISSUE SPECIFICITY: Ubiquitously expressed at all stages studied. {ECO:0000269|PubMed:10777215}. +Q9WTZ2 MBTP1_MOUSE Membrane-bound transcription factor site-1 protease (EC 3.4.21.112) (Endopeptidase S1P) (Sterol-regulated luminal protease) (Subtilisin/kexin isozyme 1) (SKI-1) 1052 117,457 Active site (3); Chain (1); Compositional bias (1); Domain (1); Glycosylation (6); Modified residue (1); Propeptide (1); Sequence conflict (1); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 1000 1022 Helical. {ECO:0000255}. TOPO_DOM 187 999 Lumenal. {ECO:0000255}.; TOPO_DOM 1023 1052 Cytoplasmic. {ECO:0000255}. FUNCTION: Serine protease that catalyzes the first step in the proteolytic activation of the sterol regulatory element-binding proteins (SREBPs). Other known substrates are BDNF, GNPTAB and ATF6. Cleaves after hydrophobic or small residues, provided that Arg or Lys is in position P4. Cleaves known substrates after Arg-Ser-Val-Leu (SERBP-2), Arg-His-Leu-Leu (ATF6), Arg-Gly-Leu-Thr (BDNF) and its own propeptide after Arg-Arg-Leu-Leu. Mediates the protein cleavage of GNPTAB into subunit alpha and beta, thereby participating in biogenesis of lysosomes (By similarity). {ECO:0000250}. PTM: The 148 kDa zymogen is processed progressively into two membrane-bound 120 and 106 kDa forms in the endoplasmic reticulum, and late into a secreted 98 kDa form. The propeptide is autocatalytically removed through an intramolecular cleavage after Leu-186. Further cleavage generates 14, 10, and 8 kDa intermediates (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=May sort to other organelles, including lysosomal and/or endosomal compartments. {ECO:0000250}. +Q8K595 MCLN2_MOUSE Mucolipin-2 (Transient receptor potential channel mucolipin 2) (TRPML2) 566 65,450 Alternative sequence (1); Chain (1); Disulfide bond (2); Intramembrane (1); Motif (1); Region (1); Sequence conflict (1); Topological domain (8); Transmembrane (6) INTRAMEM 449 469 Pore-forming. {ECO:0000250|UniProtKB:F6RG56}. TRANSMEM 66 86 Helical. {ECO:0000250|UniProtKB:F6RG56}.; TRANSMEM 289 309 Helical. {ECO:0000250|UniProtKB:F6RG56}.; TRANSMEM 347 367 Helical. {ECO:0000250|UniProtKB:F6RG56}.; TRANSMEM 377 397 Helical. {ECO:0000250|UniProtKB:F6RG56}.; TRANSMEM 420 440 Helical. {ECO:0000250|UniProtKB:F6RG56}.; TRANSMEM 481 502 Helical. {ECO:0000250|UniProtKB:F6RG56}. TOPO_DOM 1 65 Cytoplasmic. {ECO:0000250|UniProtKB:F6RG56}.; TOPO_DOM 87 288 Extracellular. {ECO:0000250|UniProtKB:F6RG56}.; TOPO_DOM 310 346 Cytoplasmic. {ECO:0000250|UniProtKB:F6RG56}.; TOPO_DOM 368 376 Extracellular. {ECO:0000250|UniProtKB:F6RG56}.; TOPO_DOM 398 419 Cytoplasmic. {ECO:0000250|UniProtKB:F6RG56}.; TOPO_DOM 441 448 Extracellular. {ECO:0000250|UniProtKB:F6RG56}.; TOPO_DOM 470 480 Extracellular. {ECO:0000250|UniProtKB:F6RG56}.; TOPO_DOM 503 566 Cytoplasmic. {ECO:0000250|UniProtKB:F6RG56}. FUNCTION: Nonselective cation channel probably playing a role in the regulation of membrane trafficking events. Acts as Ca(2+)-permeable cation channel with inwardly rectifying activity (PubMed:19763610). May activate ARF6 and be involved in the trafficking of GPI-anchored cargo proteins to the cell surface via the ARF6-regulated recycling pathway (By similarity). May play a role in immune processes. In adaptive immunity, TRPML2 and TRPML1 may play redundant roles in the function of the specialized lysosomes of B cells (PubMed:17050035). In the innate immune response, may play a role in the regulation of chemokine secretion and macrophage migration (PubMed:26432893). Through a possible and probably tissue-specific heteromerization with MCOLN1 may be at least in part involved in many lysosome-dependent cellular events. {ECO:0000250|UniProtKB:Q8IZK6, ECO:0000269|PubMed:17050035, ECO:0000269|PubMed:19763610, ECO:0000269|PubMed:22753890, ECO:0000269|PubMed:26432893, ECO:0000305}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8IZK6}; Multi-pass membrane protein {ECO:0000250|UniProtKB:F6RG56}. Lysosome membrane {ECO:0000305|PubMed:17050035}; Multi-pass membrane protein {ECO:0000250|UniProtKB:F6RG56}. Recycling endosome membrane {ECO:0000269|PubMed:26432893}; Multi-pass membrane protein {ECO:0000250|UniProtKB:F6RG56}. Note=Localizes to recycling endosomes in activated macrophages and microglia. {ECO:0000269|PubMed:26432893}. SUBUNIT: Forms homooligomeric complexes; probably tetrameric. Can heterooligomerize with MCOLN1; heteromeric assemblies have different channel properties as compared to the respective homooligomers and may be tissue-specific. Interacts with TMEM176A. {ECO:0000250|UniProtKB:Q8IZK6}. DOMAIN: The most N-terminal extracellular/lumenal domain (referred to as I-II linker or polycystin-mucolipin domain) contributes to a structure with a four-fold rotational symmetry in a tetrameric assembly; the structure contains a central highly electronegative pore with a 14 A diameter. The pore is critical for Ca(2+) and pH regulation. The protruding structure formed by the I-II linkers may contain all the interaction sites with lipids and proteins in the endolysosomal lumen. {ECO:0000250|UniProtKB:Q9GZU1}. TISSUE SPECIFICITY: Isoform 1 is widely expressed at very low levels. Isoform 2 is expressed at high levels in lymphoid tissues (thymus and spleen) and kidney, and at moderate levels in heart, lung, liver and stomach. Expressed in activated macrophages and microglia (at protein level). {ECO:0000269|PubMed:19763610, ECO:0000269|PubMed:26432893}. +P14152 MDHC_MOUSE Malate dehydrogenase, cytoplasmic (EC 1.1.1.37) (Cytosolic malate dehydrogenase) 334 36,511 Active site (1); Binding site (6); Chain (1); Initiator methionine (1); Modified residue (14); Nucleotide binding (2); Sequence conflict (4) PTM: ISGylated. {ECO:0000269|PubMed:16139798}.; PTM: Acetylation at Lys-118 dramatically enhances enzymatic activity and promotes adipogenic differentiation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Homodimer. +O54949 NLK_MOUSE Serine/threonine-protein kinase NLK (EC 2.7.11.24) (Nemo-like kinase) 527 58,313 Active site (1); Binding site (1); Chain (1); Compositional bias (6); Domain (1); Erroneous initiation (1); Modified residue (2); Motif (1); Mutagenesis (5); Nucleotide binding (1); Region (5); Sequence conflict (1) FUNCTION: Serine/threonine-protein kinase that regulates a number of transcription factors with key roles in cell fate determination. Positive effector of the non-canonical Wnt signaling pathway, acting downstream of WNT5A, MAP3K7/TAK1 and HIPK2. Activation of this pathway causes binding to and phosphorylation of the histone methyltransferase SETDB1. The NLK-SETDB1 complex subsequently interacts with PPARG, leading to methylation of PPARG target promoters at histone H3K9 and transcriptional silencing. The resulting loss of PPARG target gene transcription inhibits adipogenesis and promotes osteoblastogenesis in mesenchymal stem cells (MSCs). Negative regulator of the canonical Wnt/beta-catenin signaling pathway. Binds to and phosphorylates TCF7L2/TCF4 and LEF1, promoting the dissociation of the TCF7L2/LEF1/beta-catenin complex from DNA, as well as the ubiquitination and subsequent proteolysis of LEF1. Together these effects inhibit the transcriptional activation of canonical Wnt/beta-catenin target genes. Negative regulator of the Notch signaling pathway. Binds to and phosphorylates NOTCH1, thereby preventing the formation of a transcriptionally active ternary complex of NOTCH1, RBPJ/RBPSUH and MAML1. Negative regulator of the MYB family of transcription factors. Phosphorylation of MYB leads to its subsequent proteolysis while phosphorylation of MYBL1 and MYBL2 inhibits their interaction with the coactivator CREBBP. Other transcription factors may also be inhibited by direct phosphorylation of CREBBP itself. Acts downstream of IL6 and MAP3K7/TAK1 to phosphorylate STAT3, which is in turn required for activation of NLK by MAP3K7/TAK1. Upon IL1B stimulus, cooperates with ATF5 to activate the transactivation activity of C/EBP subfamily members. Phosphorylates ATF5 but also stabilizes ATF5 protein levels in a kinase-independent manner (By similarity). {ECO:0000250|UniProtKB:Q9UBE8, ECO:0000269|PubMed:10391247, ECO:0000269|PubMed:11745377, ECO:0000269|PubMed:12482967, ECO:0000269|PubMed:12556497, ECO:0000269|PubMed:14720327, ECO:0000269|PubMed:15004007, ECO:0000269|PubMed:15082531, ECO:0000269|PubMed:15308626, ECO:0000269|PubMed:16055500, ECO:0000269|PubMed:17785444, ECO:0000269|PubMed:18765672, ECO:0000269|PubMed:20118921, ECO:0000269|PubMed:20194509, ECO:0000269|PubMed:20874444, ECO:0000269|PubMed:21118996, ECO:0000269|PubMed:9448268}. PTM: Phosphorylated on Thr-298. Intermolecular autophosphorylation on Thr-298 activates the enzyme. {ECO:0000269|PubMed:21118996}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Predominantly nuclear. A smaller fraction is cytoplasmic. SUBUNIT: Homodimer. Homodimerization is required for intermolecular autophosphorylation, kinase activation and nuclear localization (PubMed:21118996). Interacts with RNF138/NARF (By similarity). Forms a complex with CHD7, PPARG and SETDB1 in response to WNT5A signaling (By similarity). Interacts with DAPK3/ZIPK, and this interaction may disrupt interaction with transcription factors such as TCF7L2/TCF4 (By similarity). Interacts with FOXO1 and FOXO3 (By similarity). Interacts with the upstream activating kinases HIPK2 and MAP3K7/TAK1. Interaction with MAP3K7/TAK1 seems to be indirect, and may be mediated by other proteins such as STAT3, TAB1 and TAB2. Interacts with and phosphorylates a number of transcription factors including FOXO4, LEF1, MYB, MYBL1, MYBL2, NOTCH1 and TCF7L2/TCF4. May interact with components of cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes. Interacts with MEF2A (PubMed:12556497, PubMed:15004007, PubMed:15082531, PubMed:15308626, PubMed:16055500, PubMed:17785444, PubMed:18765672, PubMed:20118921, PubMed:20194509, PubMed:20874444). Interacts with ATF5; the interaction stabilizes ATF5 at the protein level in a kinase-independent manner (By similarity). {ECO:0000250|UniProtKB:Q9UBE8, ECO:0000269|PubMed:12556497, ECO:0000269|PubMed:15004007, ECO:0000269|PubMed:15082531, ECO:0000269|PubMed:15308626, ECO:0000269|PubMed:16055500, ECO:0000269|PubMed:17785444, ECO:0000269|PubMed:18765672, ECO:0000269|PubMed:20118921, ECO:0000269|PubMed:20194509, ECO:0000269|PubMed:20874444, ECO:0000269|PubMed:21118996}. DOMAIN: Contains a TQE activation loop motif in which autophosphorylation of the threonine residue (Thr-298) is sufficient for kinase activation. This mode of activation contrasts with that of classical MAP kinases, which contain a TXY activation loop motif in which phosphorylation of both the threonine and tyrosine residues is required for kinase activation. TISSUE SPECIFICITY: Expressed at high levels in the brain, and at lower levels in heart, kidney, lung and liver. {ECO:0000269|PubMed:9448268}. +P08249 MDHM_MOUSE Malate dehydrogenase, mitochondrial (EC 1.1.1.37) 338 35,611 Active site (1); Binding site (7); Chain (1); Frameshift (1); Glycosylation (1); Modified residue (34); Nucleotide binding (2); Sequence conflict (3); Transit peptide (1) PTM: Acetylation is enhanced after treatment either with trichostin A (TCA) or with nicotinamide (NAM) with the appearance of tri- and tetraacetylations. Glucose also increases acetylation (By similarity). Acetylation of Lys-239 and Lys-314 is observed in liver mitochondria from fasted mice but not from fed mice. {ECO:0000250|UniProtKB:P40926}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:P04636}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P00346}. +Q66X01 NLR9C_MOUSE NACHT, LRR and PYD domains-containing protein 9C (NALP-zeta) 1004 115,722 Alternative sequence (3); Chain (1); Domain (2); Nucleotide binding (1); Repeat (5); Sequence conflict (2) FUNCTION: May be involved in inflammation. {ECO:0000305}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q66X22}. TISSUE SPECIFICITY: Oocyte specific. {ECO:0000269|PubMed:15317747}. +Q5DU56 NLRC3_MOUSE Protein NLRC3 1064 115,993 Alternative sequence (11); Chain (1); Domain (1); Erroneous initiation (1); Nucleotide binding (1); Repeat (16) FUNCTION: Negative regulator of the innate immune response. Attenuates signaling pathways activated by Toll-like receptors (TLRs) and the DNA sensor STING/TMEM173 in response to pathogen-associated molecular patterns, such as intracellular poly(dA:dT), but not poly(I:C), or in response to DNA virus infection, including that of Herpes simplex virus 1 (HSV1) (PubMed:22863753, PubMed:24560620). May affect TLR4 signaling by acting at the level of TRAF6 ubiquitination, decreasing the activating 'Lys-63'-linked ubiquitination and leaving unchanged the degradative 'Lys-48'-linked ubiquitination (PubMed:22863753). Inhibits the PI3K-AKT-mTOR pathway possibly by directly interacting with the posphatidylinositol 3-kinase regulatory subunit p85 (PIK3R1/PIK3R2) and disrupting the association between PIK3R1/PIK3R2 and the catalytic subunit p110 (PIK3CA/PIK3CB/PIK3CD) and reducing PIK3R1/PIK3R2 activation. Via its regulation of the PI3K-AKT-mTOR pathway, controls cell proliferation, predominantly in intestinal epithelial cells (PubMed:27951586). May also affect NOD1- or NOD2-mediated NF-kappa-B activation (By similarity). Might also affect the inflammatory response by preventing NLRP3 inflammasome formation, CASP1 cleavage and IL1B maturation (By similarity). {ECO:0000250|UniProtKB:Q7RTR2, ECO:0000269|PubMed:22863753, ECO:0000269|PubMed:24560620, ECO:0000269|PubMed:27951586}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q7RTR2}. SUBUNIT: Directly interacts (via CARD) with TMEM173/STING; this interaction reduces TMEM173 trafficking to the perinuclear region in response to interferon stimulatory DNA. Also interacts, but to a lesser extent, with TBK1 (PubMed:24560620). Interacts with TRAF6; this interaction results in decreased TRAF6 'Lys-63'-linked polyubiquitination, but leaves 'Lys-48'-linked chains unchanged, promoting TRAF6 protein degradation (By similarity). Interacts with PIK3R1/PIK3R2; this interaction disrupts the association between PIK3R1/PIK3R2 and the p110 catalytic subunit PIK3CA/PIK3CB/PIK3CD and reduces PIK3R1/PIK3R2 activation (PubMed:27951586). Weakly interacts with PYCARD/ASC. Interacts with CASP1 and CASP5 (By similarity). {ECO:0000250|UniProtKB:Q7RTR2, ECO:0000269|PubMed:24560620, ECO:0000269|PubMed:27951586}. DOMAIN: The leucine-rich repeat domain may reduce the interaction with TMEM173/STING. {ECO:0000250|UniProtKB:Q7RTR2}. TISSUE SPECIFICITY: Expressed in bone marrow-derived macrophages. {ECO:0000269|PubMed:22863753}. +Q3UP24 NLRC4_MOUSE NLR family CARD domain-containing protein 4 (Caspase recruitment domain-containing protein 12) (Ice protease-activating factor) (Ipaf) 1024 116,749 Beta strand (26); Binding site (2); Chain (1); Domain (2); Helix (48); Modified residue (1); Mutagenesis (3); Nucleotide binding (1); Region (2); Repeat (12); Sequence conflict (8); Turn (5) FUNCTION: Key component of inflammasomes that indirectly senses specific proteins from pathogenic bacteria and fungi and responds by assembling an inflammasome complex that promotes caspase-1 activation, cytokine production and macrophage pyroptosis. The NLRC4 inflammasome is activated as part of the innate immune response to a range of intracellular bacteria. It senses pathogenic proteins of the type III secretion system (T3SS) and type IV secretion system (T4SS) such as flagellin and PrgJ-like rod proteins via the Naip proteins (Naip1, Naip2 or Naip5): specific Naip proteins recognize and bind pathogenic proteins, driving assembly and activation of the NLRC4 inflammasome. The NLRC4 inflammasome senses Gram-negative bacteria such as L.pneumophila and P.aeruginosa, enteric pathogens S.typhimurium (Salmonella) and S.flexneri and fungal pathogen C.albicans. In intestine, the NLRC4 inflammasome is able to discriminate between commensal and pathogenic bacteria and specifically drives production of interleukin-1 beta (IL1B) in response to infection by Salmonella or P.aeruginosa. In case of L.pneumophila infection the inflammasome acts by activating caspase-7. {ECO:0000269|PubMed:15190255, ECO:0000269|PubMed:16648852, ECO:0000269|PubMed:16648853, ECO:0000269|PubMed:18070936, ECO:0000269|PubMed:19343209, ECO:0000269|PubMed:20133635, ECO:0000269|PubMed:20603313, ECO:0000269|PubMed:21874021, ECO:0000269|PubMed:21918512, ECO:0000269|PubMed:22174673, ECO:0000269|PubMed:22231517, ECO:0000269|PubMed:22484733, ECO:0000269|PubMed:22547706, ECO:0000269|PubMed:22885697, ECO:0000269|PubMed:29146805, ECO:0000269|PubMed:29182158}. PTM: Phosphorylated at Ser-533 following infection of macrophages with S.typhimurium (Salmonella). Phosphorylation is essential for NLRC4 inflammasome function to promote caspase-1 activation and pyroptosis. PRKCD phosphorylates Ser-533 in vitro. {ECO:0000269|PubMed:22885697, ECO:0000269|PubMed:23765277}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:22885697}. SUBUNIT: Homooligomer; homooligomerizes following activation of Naip proteins by pathogenic proteins such as S.typhimurium (Salmonella) flagellin or PrgJ (PubMed:23765277, PubMed:26449474, PubMed:26585513, PubMed:29146805). Component of the NLRC4 inflammasome, at least composed of NLRC4, caspase-1 (CASP1) and some NAIP protein (Naip, Naip2 or Naip5) (PubMed:21874021, PubMed:21918512, PubMed:26585513). Interacts with Naip5 and Naip6; following Naip5 and Naip6 engagement by Salmonella flagellin (PubMed:21874021, PubMed:21918512, PubMed:29182158, PubMed:29146805). Interacts with Naip2; following Naip2 engagement by Salmonella PrgJ (PubMed:21874021, PubMed:21918512, PubMed:26449474). The inflammasome is a huge complex that contains multiple copies of NLRC4 and a single Naip protein chain (PubMed:26449474, PubMed:29146805). Interacts with EIF2AK2/PKR (By similarity). {ECO:0000250|UniProtKB:Q9NPP4, ECO:0000269|PubMed:21874021, ECO:0000269|PubMed:21918512, ECO:0000269|PubMed:23765277, ECO:0000269|PubMed:26449474, ECO:0000269|PubMed:26585513, ECO:0000269|PubMed:29146805}. DOMAIN: In an autoinhibited form the C-terminal leucine-rich repeat (LRR) domain is positioned to sterically occlude one side of the NBD domain and consequently sequester NLRC4 in a monomeric state. An ADP-mediated interaction between the NBD and the WHD also contributes to the autoinhibition (PubMed:23765277). {ECO:0000269|PubMed:23765277}. TISSUE SPECIFICITY: Expressed by intestinal mononuclear phagocytes. {ECO:0000269|PubMed:22484733}. +Q9QUI1 LRA25_MOUSE Leucine repeat adapter protein 25 (C184L ORF2 protein) (C184M protein) (MMTV receptor) 189 20,140 Alternative sequence (1); Chain (1); Modified residue (2); Repeat (1); Sequence conflict (3) FUNCTION: Negatively regulates TGF-beta-induced signaling; in cooperation with SKI prevents the translocation of SMAD2 from the nucleus to the cytoplasm in response to TGF-beta (PubMed:12646588). Acts as an adapter that mediates the specific recognition of LIMK1 by CDC42BPA and CDC42BPB in the lamellipodia. LRAP25-mediated CDC42BPA/CDC42BPB targeting to LIMK1 and the lamellipodium results in LIMK1 activation and the subsequent phosphorylation of CFL1 which is important for lamellipodial F-actin regulation (PubMed:25107909). {ECO:0000269|PubMed:12646588, ECO:0000269|PubMed:25107909}.; FUNCTION: (Microbial infection) Isoform 2: May be a receptor for mouse mammary tumor virus (MMTV). {ECO:0000269|PubMed:9525630}. SUBCELLULAR LOCATION: Isoform 1: Cytoplasm {ECO:0000269|PubMed:12646588}. Cell projection, lamellipodium {ECO:0000269|PubMed:25107909}. Note=Co-localizes with CDC42BPA, CDC42BPB and LIMK1 in the lamellipodium. {ECO:0000269|PubMed:25107909}.; SUBCELLULAR LOCATION: Isoform 2: Cell surface {ECO:0000269|PubMed:9525630}. SUBUNIT: Interacts with SKI (PubMed:12646588). Interacts (via LRR repeat) with CDC42BPA (via AGC-kinase C-terminal domain), CDC42BPB (via AGC-kinase C-terminal domain) and LIMK1 (via LIM zinc-binding domains). Forms a tripartite complex with CDC42BPA, CDC42BPB and LIMK1 (PubMed:25107909). {ECO:0000269|PubMed:12646588, ECO:0000269|PubMed:25107909}.; SUBUNIT: (Microbial infection) Isoform 2: Interacts with mouse mammary tumor virus (MMTV) envelope glycoprotein gp70. {ECO:0000269|PubMed:9525630}. TISSUE SPECIFICITY: Widely expressed. Expressed in the early postnatal brain. {ECO:0000269|PubMed:10512749, ECO:0000269|PubMed:9525630}. +Q8BLY3 LRFN3_MOUSE Leucine-rich repeat and fibronectin type-III domain-containing protein 3 (Synaptic adhesion-like molecule 4) 626 66,056 Chain (1); Disulfide bond (1); Domain (4); Glycosylation (5); Repeat (6); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 540 560 Helical. {ECO:0000255}. TOPO_DOM 17 539 Extracellular. {ECO:0000255}.; TOPO_DOM 561 626 Cytoplasmic. {ECO:0000255}. FUNCTION: Cell adhesion molecule that mediates homophilic cell-cell adhesion in a Ca(2+)-independent manner. Promotes neurite outgrowth in hippocampal neurons. {ECO:0000269|PubMed:18227064, ECO:0000269|PubMed:18585462}. PTM: N-glycosylated. {ECO:0000269|PubMed:16828986}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16828986}; Single-pass type I membrane protein {ECO:0000269|PubMed:16828986}. Cell projection, axon {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cell junction, synapse {ECO:0000250}. Cell junction, synapse, presynaptic cell membrane {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000250}. SUBUNIT: Can form heteromeric complexes with LRFN1, LRFN2, LRFN4 and LRFN5. Able to form homomeric complexes across cell junctions, between adjacent cells. Does not interact with DLG4. DOMAIN: Lacks a cytoplasmic PDZ-binding domain, which has been implicated in function of related Lrfn proteins. TISSUE SPECIFICITY: Expressed in brain, testis, stomach, small intestine and kidney. Residually expressed in heart, lung, liver, skeletal muscle and uterus. In the brain, weak, but broad expression in the cerebral cortex and diencephalic nuclei. Also detected in other parts of the central nervous system, including the olfactory bulb, pons, cerebellum, and medulla oblongata, as well as in the peripheral nervous system, such as the ganglia of cranial nerves and the dorsal root ganglion during gestation. {ECO:0000269|PubMed:16828986}. +Q8CB67 LRP11_MOUSE Low-density lipoprotein receptor-related protein 11 (LRP-11) 483 51,814 Chain (1); Disulfide bond (3); Domain (3); Glycosylation (3); Modified residue (1); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 434 456 Helical. {ECO:0000255}. TOPO_DOM 33 433 Extracellular. {ECO:0000255}.; TOPO_DOM 457 483 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q9ESE1 LRBA_MOUSE Lipopolysaccharide-responsive and beige-like anchor protein (Beige-like protein) 2856 317,064 Alternative sequence (4); Chain (1); Compositional bias (1); Domain (2); Initiator methionine (1); Modified residue (19); Repeat (6); Transmembrane (1) TRANSMEM 1529 1545 Helical. {ECO:0000255}. FUNCTION: May be involved in coupling signal transduction and vesicle trafficking to enable polarized secretion and/or membrane deposition of immune effector molecules. {ECO:0000269|PubMed:11254716}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Endoplasmic reticulum {ECO:0000269|PubMed:11254716}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:11254716}. Lysosome {ECO:0000269|PubMed:11254716}. TISSUE SPECIFICITY: Isoform 1 is expressed in the brain, is absent from the lung and the bone marrow and is less abundant in the spleen. Isoform 2 is expressed in the spleen, lung, brain and bone marrow. Isoform 3 is expressed in the brain, is absent from the bone marrow and is less abundant in the spleen and lung. {ECO:0000269|PubMed:11254716}. +Q8VDB8 LRRC2_MOUSE Leucine-rich repeat-containing protein 2 371 42,956 Chain (1); Repeat (9); Sequence conflict (1) +Q9CQ22 LTOR1_MOUSE Ragulator complex protein LAMTOR1 (Late endosomal/lysosomal adaptor and MAPK and MTOR activator 1) (Lipid raft adaptor protein p18) 161 17,749 Chain (1); Initiator methionine (1); Lipidation (1); Modified residue (6); Region (1); Sequence conflict (1) FUNCTION: As part of the Ragulator complex it is involved in amino acid sensing and activation of mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids. Activated by amino acids through a mechanism involving the lysosomal V-ATPase, the Ragulator functions as a guanine nucleotide exchange factor activating the small GTPases Rag. Activated Ragulator and Rag GTPases function as a scaffold recruiting mTORC1 to lysosomes where it is in turn activated. LAMTOR1 is directly responsible for anchoring the Ragulator complex to membranes. Also required for late endosomes/lysosomes biogenesis it may regulate both the recycling of receptors through endosomes and the MAPK signaling pathway through recruitment of some of its components to late endosomes. May be involved in cholesterol homeostasis regulating LDL uptake and cholesterol release from late endosomes/lysosomes. May also play a role in RHOA activation. {ECO:0000269|PubMed:19177150}. SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Lysosome membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell membrane {ECO:0000250|UniProtKB:Q6IAA8}; Lipid-anchor {ECO:0000250|UniProtKB:Q6IAA8}. SUBUNIT: Part of the Ragulator complex composed of LAMTOR1, LAMTOR2, LAMTOR3, LAMTOR4 and LAMTOR5. LAMTOR4 and LAMTOR5 form a heterodimer that interacts, through LAMTOR1, with a LAMTOR2, LAMTOR3 heterodimer. The Ragulator complex interacts with both the mTORC1 complex and heterodimers constituted of the Rag GTPases RRAGA, RRAGB, RRAGC and RRAGD; regulated by amino acid availability. The Ragulator complex interacts with SLC38A9; the probable amino acid sensor (By similarity). Interacts with LAMTOR2 and LAMTOR3; the interaction is direct (PubMed:19177150). Interacts with RRAGB and RRAGD; the interaction is direct indicating that it probably constitutes the main RAG-interacting subunit of the Ragulator complex. Interacts with MMP14. Interacts with CDKN1B; prevents the interaction of CDKN1B with RHOA leaving RHOA in a form accessible to activation by ARHGEF2 (By similarity). {ECO:0000250|UniProtKB:Q6IAA8, ECO:0000269|PubMed:19177150}. +Q8CG19 LTBP1_MOUSE Latent-transforming growth factor beta-binding protein 1 (LTBP-1) (Transforming growth factor beta-1-binding protein 1) (TGF-beta1-BP-1) 1712 186,717 Alternative sequence (3); Chain (1); Compositional bias (1); Disulfide bond (71); Domain (22); Glycosylation (7); Modified residue (5); Region (2); Sequence conflict (13); Signal peptide (1) FUNCTION: Key regulator of transforming growth factor beta (TGFB1, TGFB2 and TGFB3) that controls TGF-beta activation by maintaining it in a latent state during storage in extracellular space. Associates specifically via disulfide bonds with the Latency-associated peptide (LAP), which is the regulatory chain of TGF-beta, and regulates integrin-dependent activation of TGF-beta. Outcompeted by LRRC32/GARP for binding to LAP regulatory chain of TGF-beta. {ECO:0000250|UniProtKB:Q14766}. PTM: Contains hydroxylated asparagine residues. {ECO:0000250|UniProtKB:Q14766}.; PTM: Two intrachain disulfide bonds from the TB3 domain are rearranged upon TGFB1 binding, and form interchain bonds with TGFB1 propeptide, anchoring it to the extracellular matrix. {ECO:0000250|UniProtKB:Q14766}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q14766}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q14766}. SUBUNIT: Interacts with TGFB1; associates via disulfide bonds with the Latency-associated peptide chain (LAP) regulatory chain of TGFB1, leading to regulate activation of TGF-beta-1. LTBP1 does not bind directly to TGF-beta-1, the active chain of TGFB1. Interacts (via C-terminal domain) with FBN1 (via N-terminal domain). Interacts with FBN2. Interacts with ADAMTSL2. {ECO:0000250|UniProtKB:Q14766}. DOMAIN: The 8-Cys3 region in the third TB domain mediates the interchain disulfide bond interaction with the Latency-associated peptide chain (LAP) regulatory chain of TGFB1. {ECO:0000250|UniProtKB:Q14766}. +P51885 LUM_MOUSE Lumican (Keratan sulfate proteoglycan lumican) (KSPG lumican) 338 38,265 Chain (1); Compositional bias (1); Disulfide bond (1); Domain (1); Glycosylation (4); Modified residue (6); Repeat (11); Sequence conflict (5); Signal peptide (1) PTM: Cys-37, Cys-41, Cys-43 and Cys-53 are involved in disulfide bonds. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. SUBUNIT: Binds to laminin. {ECO:0000250}. TISSUE SPECIFICITY: Cornea and other tissues. +P70202 LXN_MOUSE Latexin (Endogenous carboxypeptidase inhibitor) (ECI) (Tissue carboxypeptidase inhibitor) (TCI) 222 25,492 Beta strand (10); Chain (1); Helix (4); Modified residue (1); Region (3); Sequence conflict (2); Turn (4) FUNCTION: Hardly reversible, non-competitive, and potent inhibitor of CPA1, CPA2 and CPA4 (By similarity). May play a role in inflammation. {ECO:0000250, ECO:0000269|PubMed:15698574}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. TISSUE SPECIFICITY: Highly enriched in macrophages. {ECO:0000269|PubMed:15698574}. +Q8K1T4 LY65B_MOUSE Lymphocyte antigen 6 complex locus protein G5b 194 21,615 Alternative sequence (1); Chain (1); Disulfide bond (5); Domain (1); Glycosylation (2); Signal peptide (1) PTM: N-glycosylated. {ECO:0000269|PubMed:17008713}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. SUBUNIT: Monomer. {ECO:0000269|PubMed:17008713}. +Q8BH82 NAPEP_MOUSE N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D (N-acyl phosphatidylethanolamine phospholipase D) (NAPE-PLD) (NAPE-hydrolyzing phospholipase D) (EC 3.1.4.54) 396 45,816 Binding site (2); Chain (1); Metal binding (8); Modified residue (1) FUNCTION: Hydrolyzes N-acyl-phosphatidylethanolamines (NAPEs) to produce N-acylethanolamines (NAEs) and phosphatidic acid. Responsible for the generation of these bioactive fatty acid ethanolamides (FAEs), including anandamide (N-arachidonoylethanolamine), the ligand of cannabinoid and vanilloid receptors (PubMed:14634025). As a regulator of lipid metabolism in the adipose tissue, mediates the crosstalk between adipocytes, gut microbiota and immune cells to control body temperature and weight. In particular, regulates energy homeostasis by promoting cold-induced brown or beige adipocyte differentiation program to generate heat from fatty acids and glucose (PubMed:25757720). {ECO:0000269|PubMed:14634025, ECO:0000269|PubMed:25757720}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q6IQ20}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q6IQ20}. Early endosome membrane {ECO:0000250|UniProtKB:Q6IQ20}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q6IQ20}. Nucleus envelope {ECO:0000250|UniProtKB:Q6IQ20}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q6IQ20}. Note=Localized in the proximity of the cellular membranes likely through interaction with membrane phopholipids. {ECO:0000250|UniProtKB:Q6IQ20}. SUBUNIT: Homodimer. Bile acids promote the assembly of inactive monomers into an active dimer and enable catalysis. {ECO:0000250|UniProtKB:Q6IQ20}. TISSUE SPECIFICITY: Widely expressed. Highest expression in brain, kidney and testis (at protein level) (PubMed:14634025). Expressed in adipose tissue (at protein level) (PubMed:25757720). {ECO:0000269|PubMed:14634025, ECO:0000269|PubMed:25757720}. +P60853 LZTS1_MOUSE Leucine zipper putative tumor suppressor 1 (F37/Esophageal cancer-related gene-coding leucine-zipper motif) (Fez1) 599 67,290 Chain (1); Coiled coil (1); Initiator methionine (1); Lipidation (1); Sequence conflict (1) FUNCTION: Involved in the regulation of cell growth. May stabilize the active CDC2-cyclin B1 complex and thereby contribute to the regulation of the cell cycle and the prevention of uncontrolled cell proliferation. May act as tumor suppressor (By similarity). {ECO:0000250}. PTM: Phosphorylated on serine residues. Hyperphosphorylated by the cAMP-dependent kinase PKA during cell-cycle progression (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Cell projection, dendritic spine {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250}. Cell junction, synapse {ECO:0000250}. Note=Associated with the plasma membrane and with microtubules. Detected in dendritic spines, especially in the postsynaptic density (By similarity). {ECO:0000250}. SUBUNIT: Binds EEF1G, TLK2 and CDK1. {ECO:0000250}. +O35975 NAR2B_MOUSE T-cell ecto-ADP-ribosyltransferase 2 (EC 2.4.2.31) (ADP-ribosyltransferase C2 and C3 toxin-like 2) (ARTC2) (Mono(ADP-ribosyl)transferase 2B) (NAD(+) glycohydrolase) (EC 3.2.2.5) (T-cell NAD(P)(+)--arginine ADP-ribosyltransferase 2) (T-cell differentiation marker Rt6 homolog 2) (T-cell mono(ADP-ribosyl)transferase 2) 289 33,124 Active site (1); Binding site (4); Chain (1); Disulfide bond (2); Glycosylation (2); Lipidation (1); Mutagenesis (2); Propeptide (1); Sequence conflict (14); Signal peptide (1) FUNCTION: Has both NAD(+) glycohydrolase and ADP-ribosyltransferase activity. {ECO:0000269|PubMed:17928361, ECO:0000269|PubMed:9300695}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. TISSUE SPECIFICITY: Expressed in spleen, intestine and thymus. {ECO:0000269|PubMed:9300695}. +Q99N03 M4A10_MOUSE Membrane-spanning 4-domains subfamily A member 10 267 28,972 Alternative sequence (1); Chain (1); Frameshift (1); Sequence conflict (1); Topological domain (5); Transmembrane (4) TRANSMEM 57 77 Helical. {ECO:0000255}.; TRANSMEM 84 104 Helical. {ECO:0000255}.; TRANSMEM 119 139 Helical. {ECO:0000255}.; TRANSMEM 169 189 Helical. {ECO:0000255}. TOPO_DOM 1 56 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 78 83 Extracellular. {ECO:0000255}.; TOPO_DOM 105 118 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 140 168 Extracellular. {ECO:0000255}.; TOPO_DOM 190 267 Cytoplasmic. {ECO:0000255}. FUNCTION: May be involved in signal transduction as a component of a multimeric receptor complex. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed in thymus, kidney, colon, brain and testis. Expressed also by various hematopoietic and lymphoblastoid cell lines. +Q5FWC3 M4A13_MOUSE Membrane-spanning 4-domains subfamily A member 13 (Testis-expressed transmembrane protein 4.2) (Tetm4.2) 203 22,802 Alternative sequence (1); Chain (1); Transmembrane (4) TRANSMEM 15 35 Helical. {ECO:0000255}.; TRANSMEM 56 76 Helical. {ECO:0000255}.; TRANSMEM 84 104 Helical. {ECO:0000255}.; TRANSMEM 141 161 Helical. {ECO:0000255}. FUNCTION: May be involved in signal transduction as a component of a multimeric receptor complex. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +E9Q3S4 M3K19_MOUSE Mitogen-activated protein kinase kinase kinase 19 (EC 2.7.11.1) (SPS1/STE20-related protein kinase YSK4) 1311 146,412 Active site (1); Binding site (1); Chain (1); Domain (1); Nucleotide binding (1) +P70218 M4K1_MOUSE Mitogen-activated protein kinase kinase kinase kinase 1 (EC 2.7.11.1) (Hematopoietic progenitor kinase) (HPK) (MAPK/ERK kinase kinase kinase 1) (MEK kinase kinase 1) (MEKKK 1) 827 91,535 Active site (1); Binding site (1); Chain (1); Domain (2); Helix (1); Modified residue (10); Mutagenesis (1); Nucleotide binding (1); Sequence caution (1); Sequence conflict (4) FUNCTION: Serine/threonine-protein kinase, which may play a role in the response to environmental stress. Appears to act upstream of the JUN N-terminal pathway. May play a role in hematopoietic lineage decisions and growth regulation. Able to autophosphorylate. {ECO:0000269|PubMed:9003777}. PTM: Autophosphorylates: phosphorylation promotes ubiquitination by the Cul7-RING(FBXW8) ubiquitin-protein ligase complex, leading to its degradation by the proteasome. {ECO:0000250}.; PTM: Ubiquitinated by the Cul7-RING(FBXW8) ubiquitin-protein ligase complex following autophosphorylation, leading to its degradation by the proteasome. {ECO:0000250}. SUBUNIT: Interacts with MAP3K1. Interacts with FBXW8 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed in all tissues examined at embryonic stage E16.5 with high levels in lung, heart and fetal liver. In the neonate, expression is restricted to the tissues which undergo lineage decisions, lung, thymus, liver, kidney and brain. In the adult, expression is limited to hemopoietic organs, thymus, bone marrow, and spleen and to the testis. {ECO:0000269|PubMed:9003777}. +O08648 M3K4_MOUSE Mitogen-activated protein kinase kinase kinase 4 (EC 2.7.11.25) (MAPK/ERK kinase kinase 4) (MEK kinase 4) (MEKK 4) 1597 179,834 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Compositional bias (1); Domain (1); Modified residue (9); Mutagenesis (1); Nucleotide binding (1); Sequence conflict (4) FUNCTION: Component of a protein kinase signal transduction cascade. Activates the CSBP2, P38 and JNK MAPK pathways, but not the ERK pathway. Specifically phosphorylates and activates MAP2K4 and MAP2K6. {ECO:0000269|PubMed:16157600, ECO:0000269|PubMed:9079650}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:16157600}. Note=Localized in perinuclear vesicular-like structures, probably Golgi-associated vesicles. SUBUNIT: Monomer and homodimer. Homodimerization enhances kinase activity. Interacts with CDC42 (PubMed:9079650). Interacts with TRAF4; this promotes homodimerization (PubMed:16157600). Binds both upstream activators and downstream substrates in multimolecular complexes. Interacts with AXIN1 and DIXDC1; interaction with DIXDC1 prevents interaction with AXIN1 (PubMed:15262978). Interacts with GADD45 and MAP2K6 (By similarity). Interacts with ZFP36; this interaction enhances the association with SH3KBP1/CIN85. Interacts with SH3KBP1; this interaction enhances the association with ZFP36 (By similarity). {ECO:0000250|UniProtKB:Q9Y6R4, ECO:0000269|PubMed:15262978, ECO:0000269|PubMed:16157600, ECO:0000269|PubMed:9079650}. TISSUE SPECIFICITY: Widely expressed. High expression was found in skeletal muscle, kidney, testis followed by heart brain and lung. Low expression was found in spleen. +Q9D1H6 NDUF4_MOUSE NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 4 (Hormone-regulated proliferation-associated protein of 20 kDa homolog) 173 20,082 Chain (1); Initiator methionine (1); Lipidation (1); Modified residue (1) FUNCTION: May be involved in cell proliferation and survival of hormone-dependent tumor cells. Involved in the assembly of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I) (By similarity). {ECO:0000250}. PTM: Phosphorylated on serine. Prolactin stimulate serine phosphorylation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Membrane {ECO:0000250|UniProtKB:Q9P032}; Lipid-anchor {ECO:0000250|UniProtKB:Q9P032}. SUBUNIT: Binds calmodulin. Interacts with NDUFAF3. {ECO:0000250}. +Q6PCZ4 MAGE1_MOUSE Melanoma-associated antigen E1 (Alpha-dystrobrevin-associated MAGE Protein) (DAMAGE) (MAGE-E1 antigen) 918 101,632 Chain (1); Compositional bias (1); Domain (2); Erroneous gene model prediction (1); Erroneous initiation (2); Frameshift (1); Region (1); Sequence conflict (8) FUNCTION: May enhance ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:14623885}. Nucleus {ECO:0000269|PubMed:14623885}. Cell membrane {ECO:0000269|PubMed:14623885}. Note=In the skeletal muscle, found at the postsynaptic membrane and is associated with a subset of myonuclei. May reside within nuclei and/or in perinuclear compartments. In peripheral nerves, colocalizes with DTNA in the Schwann cell membrane. SUBUNIT: Interacts with DTNA. Interacts with TRIM28 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in cell bodies and dendrites of hippocampal and Purkinje neurons. Also expressed in peripheral nerve, where it localizes to the perineurium and myelin (at protein level). Predominantly expressed in brain and at low levels in the heart, liver, kidney, spleen, testis, lung, thymus, placenta and skeletal muscle. {ECO:0000269|PubMed:14623885}. +Q07174 M3K8_MOUSE Mitogen-activated protein kinase kinase kinase 8 (EC 2.7.11.25) (Cancer Osaka thyroid oncogene) (Proto-oncogene c-Cot) (Serine/threonine-protein kinase cot) (Tumor progression locus 2) (TPL-2) 467 52,942 Active site (1); Binding site (1); Chain (1); Domain (1); Modified residue (5); Nucleotide binding (1) FUNCTION: Required for lipopolysaccharide (LPS)-induced, TLR4-mediated activation of the MAPK/ERK pathway in macrophages, thus being critical for production of the proinflammatory cytokine TNF-alpha (TNF) during immune responses. Involved in the regulation of T-helper cell differentiation and IFNG expression in T-cells. Involved in mediating host resistance to bacterial infection through negative regulation of type I interferon (IFN) production. Transduces CD40 and TNFRSF1A signals that activate ERK in B-cells and macrophages, and thus may play a role in the regulation of immunoglobulin production. May also play a role in the transduction of TNF signals that activate JNK and NF-kappa-B in some cell types. In adipocytes, activates MAPK/ERK pathway in an IKBKB-dependent manner in response to IL1B and TNF, but not insulin, leading to induction of lipolysis. Plays a role in the cell cycle. {ECO:0000269|PubMed:11163183, ECO:0000269|PubMed:12667451, ECO:0000269|PubMed:12881420, ECO:0000269|PubMed:15833743, ECO:0000269|PubMed:19001140, ECO:0000269|PubMed:19808894, ECO:0000269|PubMed:23842752}. PTM: Autophosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Forms a ternary complex with NFKB1/p105 and TNIP2. Interacts with NFKB1; the interaction increases the stability of MAP3K8 but inhibits its MEK phosphorylation activity, whereas loss of interaction following LPS stimulation leads to its degradation. Interacts with CD40 and TRAF6; the interaction is required for ERK activation. Interacts with KSR2; the interaction inhibits ERK and NF-kappa-B activation. {ECO:0000269|PubMed:12667451, ECO:0000269|PubMed:12881420}. TISSUE SPECIFICITY: Expressed in bone marrow-derived macrophages, peritoneal macrophages, splenocytes and 3T3-L1 fibroblasts and differentiated adipocytes (at protein level). Highly expressed in adult submandibular gland, thymus, spleen and newborn digestive tract. {ECO:0000269|PubMed:12667451, ECO:0000269|PubMed:19808894}. +Q3U1V8 M3K9_MOUSE Mitogen-activated protein kinase kinase kinase 9 (EC 2.7.11.25) 1077 118,805 Active site (1); Binding site (1); Chain (1); Compositional bias (3); Domain (2); Modified residue (5); Nucleotide binding (1); Region (2); Sequence conflict (2) FUNCTION: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. Plays an important role in the cascades of cellular responses evoked by changes in the environment. Once activated, acts as an upstream activator of the MKK/JNK signal transduction cascade through the phosphorylation of MAP2K4/MKK4 and MAP2K7/MKK7 which in turn activate the JNKs. The MKK/JNK signaling pathway regulates stress response via activator protein-1 (JUN) and GATA4 transcription factors. Plays also a role in mitochondrial death signaling pathway, including the release cytochrome c, leading to apoptosis (By similarity). {ECO:0000250}. PTM: Autophosphorylation on serine and threonine residues within the activation loop plays a role in enzyme activation. Thr-305 is likely to be the main autophosphorylation site (By similarity). Autophosphorylation also occurs on Thr-297 and Ser-301 (By similarity). {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in cochlea and utricle. {ECO:0000269|PubMed:20971179}. +Q9DCT2 NDUS3_MOUSE NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial (EC 1.6.99.3) (EC 7.1.1.2) (Complex I-30kD) (CI-30kD) (NADH-ubiquinone oxidoreductase 30 kDa subunit) 263 30,149 Beta strand (10); Chain (1); Helix (5); Sequence conflict (3); Transit peptide (1); Turn (3) FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}. Note=Matrix and cytoplasmic side of the mitochondrial inner membrane. {ECO:0000250}. SUBUNIT: Complex I is composed of 45 different subunits. Interacts with NDUFAF3. {ECO:0000250}. +Q8BNJ6 NETO2_MOUSE Neuropilin and tolloid-like protein 2 (Brain-specific transmembrane protein containing 2 CUB and 1 LDL-receptor class A domains protein 2) 525 59,368 Alternative sequence (2); Chain (1); Disulfide bond (7); Domain (3); Erroneous initiation (1); Glycosylation (1); Modified residue (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 348 368 Helical. {ECO:0000255}. TOPO_DOM 23 347 Extracellular. {ECO:0000255}.; TOPO_DOM 369 525 Cytoplasmic. {ECO:0000255}. FUNCTION: Accessory subunit of neuronal kainate-sensitive glutamate receptors, GRIK2 and GRIK3. Increases kainate-receptor channel activity, slowing the decay kinetics of the receptors, without affecting their expression at the cell surface, and increasing the open probability of the receptor channels. Modulates the agonist sensitivity of kainate receptors. Slows the decay of kainate receptor-mediated excitatory postsynaptic currents (EPSCs), thus directly influencing synaptic transmission (By similarity). {ECO:0000250}. PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Isoform 1: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: Isoform 2: Cell membrane; Multi-pass membrane protein. SUBUNIT: Interacts with GRIK2 and GRIK3, but neither with AMPA-nor with NMDA-sensitive glutamate receptors. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain tissues, including cerebellar granule cells (at protein level). {ECO:0000269|PubMed:15464227, ECO:0000269|PubMed:19217376}. +Q8K310 MATR3_MOUSE Matrin-3 846 94,630 Beta strand (12); Chain (1); Cross-link (18); Domain (2); Helix (5); Initiator methionine (1); Modified residue (42); Motif (1); Turn (3); Zinc finger (1) FUNCTION: May play a role in transcription or may interact with other nuclear matrix proteins to form the internal fibrogranular network. In association with the SFPQ-NONO heteromer may play a role in nuclear retention of defective RNAs (By similarity). {ECO:0000250}.; FUNCTION: May play a role in transcription or may interact with other nuclear matrix proteins to form the internal fibrogranular network. In association with the SFPQ-NONO heteromer may play a role in nuclear retention of defective RNAs. Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway. May bind to specific miRNA hairpins (By similarity). {ECO:0000250|UniProtKB:P43243}. SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000255|PROSITE-ProRule:PRU00130}. SUBUNIT: Part of a complex consisting of SFPQ, NONO and MATR3. Interacts with AGO1 and AGO2 (By similarity). Part of a complex composed at least of ASCL2, EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; this complex may have a histone H3-specific methyltransferase activity. Interacts with TARDBP. Part of the HDP-RNP complex composed of at least HEXIM1, PRKDC, XRCC5, XRCC6, paraspeckle proteins (SFPQ, NONO, PSPC1, RBM14, and MATR3) and NEAT1 RNA. Interacts with FUS. {ECO:0000250|UniProtKB:P43243}. +Q8R003 MBNL3_MOUSE Muscleblind-like protein 3 (Cys3His CCG1-required protein) (Muscleblind-like X-linked protein) (Protein MCHCR) 342 37,570 Chain (1); Compositional bias (1); Zinc finger (4) FUNCTION: Mediates pre-mRNA alternative splicing regulation. Acts either as activator or repressor of splicing on specific pre-mRNA targets. Inhibits cardiac troponin-T (TNNT2) pre-mRNA exon inclusion but induces insulin receptor (IR) pre-mRNA exon inclusion in muscle. Antagonizes the alternative splicing activity pattern of CELF proteins (By similarity). Could inhibit terminal muscle differentiation, acting at approximately the time of myogenin induction. {ECO:0000250, ECO:0000269|PubMed:12297108}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Mostly nuclear. {ECO:0000250}. +Q9WVB6 LENEP_MOUSE Lens epithelial cell protein LEP503 61 6,923 Chain (1) +Q9DB98 LENG1_MOUSE Leukocyte receptor cluster member 1 homolog 261 30,469 Chain (1); Coiled coil (2); Modified residue (2) +Q8CBY3 LENG8_MOUSE Leukocyte receptor cluster member 8 homolog 785 86,767 Alternative sequence (2); Chain (1); Compositional bias (2); Domain (1); Initiator methionine (1); Modified residue (2); Sequence conflict (1) SUBUNIT: May be part of a SEM1-containing complex. {ECO:0000250|UniProtKB:Q96PV6}. +Q5XJE5 LEO1_MOUSE RNA polymerase-associated protein LEO1 667 75,597 Alternative sequence (2); Chain (1); Compositional bias (1); Initiator methionine (1); Modified residue (30); Sequence conflict (1) FUNCTION: Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and is involved in transcriptional elongation, acting both indepentently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1. PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B ubiquitination is proposed to be coupled to transcription. PAF1C is involved in mRNA 3' end formation probably through association with cleavage and poly(A) factors. Involved in polyadenylation of mRNA precursors. Connects PAF1C to Wnt signaling (By similarity). {ECO:0000250, ECO:0000269|PubMed:19345177}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the PAF1 complex, which consists of CDC73, PAF1, LEO1, CTR9, RTF1 and WDR61. The PAF1 complex interacts with PHF5A (PubMed:27749823). Interacts with TCEA1, SUPT5H and CTNNB1 (By similarity). Interacts with SETD5 (PubMed:27864380). {ECO:0000250|UniProtKB:Q8WVC0, ECO:0000269|PubMed:27749823, ECO:0000269|PubMed:27864380}. +P48356 LEPR_MOUSE Leptin receptor (LEP-R) (B219) (OB receptor) (OB-R) (CD antigen CD295) 1162 130,789 Alternative sequence (8); Chain (1); Disulfide bond (10); Domain (5); Glycosylation (16); Modified residue (4); Motif (2); Mutagenesis (9); Natural variant (4); Region (3); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 840 860 Helical. {ECO:0000255}. TOPO_DOM 22 839 Extracellular. {ECO:0000255}.; TOPO_DOM 861 1162 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for hormone LEP/leptin (Probable) (PubMed:11861497). On ligand binding, mediates LEP central and peripheral effects through the activation of different signaling pathways such as JAK2/STAT3 and MAPK cascade/FOS (PubMed:10799542, PubMed:25383904, PubMed:11923481, PubMed:11861497). In the hypothalamus, LEP acts as an appetite-regulating factor that induces a decrease in food intake and an increase in energy consumption by inducing anorexinogenic factors and suppressing orexigenic neuropeptides, also regulates bone mass and secretion of hypothalamo-pituitary-adrenal hormones (PubMed:10660043, PubMed:12594516). In the periphery, increases basal metabolism, influences reproductive function, regulates pancreatic beta-cell function and insulin secretion, is pro-angiogenic and affects innate and adaptive immunity (PubMed:25383904, PubMed:11923481). Control of energy homeostasis and melanocortin production (stimulation of POMC and full repression of AgRP transcription) is mediated by STAT3 signaling, whereas distinct signals regulate NPY and the control of fertility, growth and glucose homeostasis (PubMed:12594516). Involved in the regulation of counter-regulatory response to hypoglycemia by inhibiting neurons of the parabrachial nucleus (PubMed:25383904). Has a specific effect on T lymphocyte responses, differentially regulating the proliferation of naive and memory T-cells. Leptin increases Th1 and suppresses Th2 cytokine production (PubMed:9732873). {ECO:0000269|PubMed:10660043, ECO:0000269|PubMed:10799542, ECO:0000269|PubMed:11861497, ECO:0000269|PubMed:11923481, ECO:0000269|PubMed:12594516, ECO:0000269|PubMed:25383904, ECO:0000269|PubMed:9732873, ECO:0000305|PubMed:25232147}.; FUNCTION: Isoform A: May transport LEP across the blood-brain barrier. Binds LEP and mediates LEP endocytosis (PubMed:17620316, PubMed:20223942). Does not induce phosphorylation of and activate STAT3 (PubMed:11923481, PubMed:20223942). {ECO:0000269|PubMed:11923481, ECO:0000269|PubMed:17620316, ECO:0000269|PubMed:20223942}.; FUNCTION: Isoform E: Antagonizes Isoform A and isoform B-mediated LEP binding and endocytosis. {ECO:0000269|PubMed:17620316}. PTM: On ligand binding, phosphorylated on two conserved C-terminal tyrosine residues (isoform B only) by JAK2. Tyr-985 is required for complete binding and activation of PTPN11, ERK/FOS activation,for interaction with SOCS3 and SOCS3 mediated inhibition of leptin signaling. Phosphorylation on Tyr-1138 is required for STAT3 binding/activation. Phosphorylation of Tyr-1077 has a more accessory role. {ECO:0000269|PubMed:10799542, ECO:0000269|PubMed:11108838}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P48357}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P48357}. Basolateral cell membrane {ECO:0000250|UniProtKB:P48357}.; SUBCELLULAR LOCATION: Isoform E: Secreted {ECO:0000305|PubMed:17620316}. SUBUNIT: Present as a mixture of monomers and dimers (Probable). The phosphorylated receptor binds a number of SH2 domain-containing proteins such as JAK2, STAT3, PTPN11, and SOCS3 (By similarity) (PubMed:11018044, PubMed:11923481). Interaction with SOCS3 inhibits JAK/STAT signaling and MAPK cascade (PubMed:11018044). {ECO:0000250|UniProtKB:P48357, ECO:0000269|PubMed:11018044, ECO:0000269|PubMed:11923481, ECO:0000305|PubMed:25232147}. DOMAIN: The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding. {ECO:0000269|PubMed:12196522}.; DOMAIN: The box 1 motif is required for JAK interaction and/or activation. {ECO:0000269|PubMed:12196522}. TISSUE SPECIFICITY: Isoform A: highest level of expression in lung and kidney, also present in heart, brain, spleen, liver, muscle, choroid plexus and hypothalamus. Isoform B: highest levels of expression in hypothalamus and lower levels in brain, testes and adipose tissue. Expressed by neurons of the parabrachial nucleus (PubMed:25383904). Expressed by peripheral blood mononuclear cells and CD4(+) T-cells (PubMed:9732873). Isoform E: expressed in adipose tissue, liver, hypothalamus, cerebral microvessels, heart, and testes (PubMed:17620316). {ECO:0000269|PubMed:17620316, ECO:0000269|PubMed:25383904, ECO:0000269|PubMed:9732873}. +Q9Z2I0 LETM1_MOUSE Mitochondrial proton/calcium exchanger protein (Leucine zipper-EF-hand-containing transmembrane protein 1) 738 82,989 Calcium binding (1); Chain (1); Coiled coil (5); Domain (2); Modified residue (1); Mutagenesis (3); Sequence caution (3); Sequence conflict (1); Topological domain (2); Transit peptide (1); Transmembrane (1) TRANSMEM 208 228 Helical. {ECO:0000255}. TOPO_DOM 115 207 Mitochondrial intermembrane. {ECO:0000305|PubMed:27669901}.; TOPO_DOM 229 738 Mitochondrial matrix. {ECO:0000305|PubMed:27669901}. FUNCTION: Mitochondrial proton/calcium antiporter that mediates proton-dependent calcium efflux from mitochondrion (PubMed:27669901). Crucial for the maintenance of mitochondrial tubular networks and for the assembly of the supercomplexes of the respiratory chain (By similarity). Required for the maintenance of the tubular shape and cristae organization (By similarity). In contrast to SLC8B1/NCLX, does not constitute the major factor for mitochondrial calcium extrusion (By similarity). {ECO:0000250|UniProtKB:O95202, ECO:0000269|PubMed:27669901}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:27669901}; Single-pass membrane protein {ECO:0000305}. SUBUNIT: Homohexamer (PubMed:27669901). Interacts with BCS1L (By similarity). {ECO:0000250|UniProtKB:O95202, ECO:0000269|PubMed:27669901}. +P47945 MT4_MOUSE Metallothionein-4 (MT-4) (Metallothionein-IV) (MT-IV) 62 6,277 Chain (1); Metal binding (20) FUNCTION: Seems to bind zinc and copper. Could play a special role in regulating zinc metabolism during the differentiation of stratified epithelia. TISSUE SPECIFICITY: Expressed exclusively in stratified squamous epithelia associated with oral epithelia, esophagus, upper stomach, tail, footpads and neonatal skin. +Q8BJZ3 LFG3_MOUSE Protein lifeguard 3 (Responsive to centrifugal force and shear stress gene 1 protein) (Protein RECS1) (Transmembrane BAX inhibitor motif-containing protein 1) 309 34,393 Alternative sequence (2); Chain (1); Modified residue (2); Sequence conflict (2); Transmembrane (7) TRANSMEM 101 121 Helical. {ECO:0000255}.; TRANSMEM 132 152 Helical. {ECO:0000255}.; TRANSMEM 163 183 Helical. {ECO:0000255}.; TRANSMEM 188 208 Helical. {ECO:0000255}.; TRANSMEM 221 241 Helical. {ECO:0000255}.; TRANSMEM 244 264 Helical. {ECO:0000255}.; TRANSMEM 286 306 Helical. {ECO:0000255}. FUNCTION: Negatively regulates aortic matrix metalloproteinase-9 (MMP9) production and may play a protective role in vascular remodeling. {ECO:0000269|PubMed:16607040, ECO:0000269|PubMed:16636500}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Lysosome membrane {ECO:0000250}. Endosome membrane {ECO:0000250}. TISSUE SPECIFICITY: Expressed in most tissues except spleen, thymus and testis. {ECO:0000269|PubMed:16607040}. +Q9R190 MTA2_MOUSE Metastasis-associated protein MTA2 (Metastasis-associated 1-like 1) 668 75,030 Chain (1); Cross-link (5); Domain (3); Modified residue (9); Sequence conflict (1); Zinc finger (1) FUNCTION: May be involved in the regulation of gene expression as repressor and activator. The repression might be related to covalent modification of histone proteins. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00512, ECO:0000255|PROSITE-ProRule:PRU00624, ECO:0000269|PubMed:11749719}. SUBUNIT: Component of the nucleosome-remodeling and histone-deacetylase multiprotein complex (NuRD). Interacts with HDAC7, p53/TP53, MINT and MBD3 (By similarity). Interacts with PIMREG (By similarity). Interacts with NACC2 (By similarity). {ECO:0000250}. +Q924K8 MTA3_MOUSE Metastasis-associated protein MTA3 591 67,077 Alternative sequence (2); Beta strand (1); Chain (1); Domain (3); Helix (3); Modified residue (4); Sequence conflict (1); Zinc finger (1) FUNCTION: Plays a role in maintenance of the normal epithelial architecture through the repression of SNAI1 transcription in a histone deacetylase-dependent manner, and thus the regulation of E-cadherin levels. Contributes to transcriptional repression by BCL6 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00512, ECO:0000255|PROSITE-ProRule:PRU00624, ECO:0000269|PubMed:11483358}. Cytoplasm {ECO:0000269|PubMed:11483358}. SUBUNIT: Component of the nucleosome-remodeling and histone-deacetylase multiprotein complex (NuRD). Interacts with BCL6 (By similarity). Interacts with NACC2 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in heart, brain, spleen, lung, liver and kidney. +Q9JIA1 LGI1_MOUSE Leucine-rich glioma-inactivated protein 1 557 63,644 Chain (1); Domain (2); Glycosylation (3); Repeat (10); Signal peptide (1) FUNCTION: Regulates voltage-gated potassium channels assembled from KCNA1, KCNA4 and KCNAB1. It slows down channel inactivation by precluding channel closure mediated by the KCNAB1 subunit. Ligand for ADAM22 that positively regulates synaptic transmission mediated by AMPA-type glutamate receptors. Plays a role in suppressing the production of MMP1/3 through the phosphatidylinositol 3-kinase/ERK pathway (By similarity). {ECO:0000250}. PTM: Glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15857855, ECO:0000269|PubMed:16787412}. Cell junction, synapse {ECO:0000250}. Note=Isoform 1 and isoform 2 are detected in the cytosolic and microsomal fractions respectively. SUBUNIT: Oligomer (By similarity). Interacts with KCNA1 within a complex containing KCNA1, KCNA4 and KCNAB1 (By similarity). Part of a complex containing ADAM22, DLG4/PSD95 and CACNG2 (stargazin) (By similarity). Can bind to ADAM11 and ADAM23. {ECO:0000250, ECO:0000269|PubMed:18974846}. TISSUE SPECIFICITY: Brain. {ECO:0000269|PubMed:16787412}. +Q5U4E0 LHPL4_MOUSE LHFPL tetraspan subfamily member 4 protein (GABAA receptor regulatory Lhfpl4) (Lipoma HMGIC fusion partner-like 4 protein) 247 27,050 Chain (1); Erroneous initiation (1); Sequence conflict (1); Transmembrane (4) TRANSMEM 22 42 Helical. {ECO:0000255}.; TRANSMEM 97 117 Helical. {ECO:0000255}.; TRANSMEM 127 147 Helical. {ECO:0000255}.; TRANSMEM 178 198 Helical. {ECO:0000255}. FUNCTION: Plays a role in the regulation of inhibitory synapse formation and function by being involved in maintening gamma-aminobutyric acid receptors (GABAARs) clustering and their associated scaffold proteins at inhibitory synaptic sites (PubMed:28978485, PubMed:28279354, PubMed:29742426). Acts in concert with NLGN2 to recruit or stabilize GABAARs (PubMed:29742426). {ECO:0000269|PubMed:28279354, ECO:0000269|PubMed:28978485, ECO:0000269|PubMed:29742426}. SUBCELLULAR LOCATION: Cell projection, dendrite {ECO:0000250|UniProtKB:Q7TSY2}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000269|PubMed:28978485, ECO:0000269|PubMed:29742426}; Multi-pass membrane protein {ECO:0000255}. Note=Specifically localizes to inhibitory postsynaptic sites (PubMed:28978485, PubMed:29742426). Colocalizes with GPHN, GABRG2 and NLGN2 at inhibitory postsynaptic sites (By similarity) (PubMed:29742426). {ECO:0000250|UniProtKB:Q7TSY2, ECO:0000269|PubMed:28978485, ECO:0000269|PubMed:29742426}. SUBUNIT: Interacts with GABA(A) receptor subunits (PubMed:28279354, PubMed:28978485, PubMed:29742426). Interacts with GABRB3 (PubMed:28978485). Interacts with GABRA2 (PubMed:28978485). Interacts with GABRG2 (PubMed:28978485, PubMed:29742426). Interacts with GABRA1 (PubMed:29742426). Identified in a complex of 720 kDa composed of LHFPL4, NLGN2, GABRA1, GABRB2, GABRG2 and GABRB3 (By similarity). Interacts with NLGN2; leading to mutual regulation of protein level and synaptic clustering (PubMed:29742426, PubMed:28978485). {ECO:0000250|UniProtKB:Q7TSY2, ECO:0000269|PubMed:28279354, ECO:0000269|PubMed:28978485, ECO:0000269|PubMed:29742426}. TISSUE SPECIFICITY: Highly expressed in the brain, including the cortex, hippocampus, midbrain, olfactory bulb pona plus medulla (at protein level) (PubMed:26964900, PubMed:28279354, PubMed:29742426). Expressed in the in the cerebellar granular layer and in granular layer. Colocalized with GPHN at inhibitory synapses (PubMed:29742426). Weakly expressed in heart, testis, lung, intestine, vagina, ovary and uterus (PubMed:26964900). {ECO:0000269|PubMed:26964900, ECO:0000269|PubMed:28279354, ECO:0000269|PubMed:29742426}. +Q3UH68 LIMC1_MOUSE LIM and calponin homology domains-containing protein 1 1057 118,196 Alternative sequence (4); Chain (1); Coiled coil (2); Domain (2); Modified residue (31); Region (1); Sequence conflict (1) FUNCTION: Actin stress fibers-associated protein that activates non-muscle myosin IIa. Activates the non-muscle myosin IIa complex by promoting the phosphorylation of its regulatory subunit MRLC/MYL9. Through the activation of non-muscle myosin IIa, positively regulates actin stress fibers assembly and stabilizes focal adhesions. It therefore negatively regulates cell spreading and cell migration. {ECO:0000250|UniProtKB:Q9UPQ0}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:Q9UPQ0}. SUBUNIT: Interacts with MYH9; independently of the integration of MYH9 into the myosin complex. {ECO:0000250|UniProtKB:Q9UPQ0}. +Q5BKQ4 LIPR1_MOUSE Inactive pancreatic lipase-related protein 1 (PL-RP1) 473 52,696 Active site (3); Chain (1); Disulfide bond (6); Domain (1); Metal binding (4); Sequence conflict (7); Signal peptide (1) FUNCTION: May function as inhibitor of dietary triglyceride digestion. Lacks detectable lipase activity (in vitro) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10235541}. Note=Secreted in acinar cells. TISSUE SPECIFICITY: Expressed in female, but not in male, lacrimal gland. Expressed in male and female sublingual gland and pancreas. {ECO:0000269|PubMed:10235541}. +Q08731 LIT2_MOUSE Lithostathine-2 (Islet of Langerhans regenerating protein 2) (REG-2) (Pancreatic stone protein 2) (PSP) (Pancreatic thread protein 2) (PTP) 173 19,407 Chain (1); Disulfide bond (3); Domain (1); Signal peptide (1) FUNCTION: Might act as an inhibitor of spontaneous calcium carbonate precipitation. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. TISSUE SPECIFICITY: Expressed only in regenerating islets and normal exocrine pancreas, but not in normal pancreatic islets. Expressed strongly in pancreas, weakly in liver, but not at all in gall bladder. +Q8CI43 MYL6B_MOUSE Myosin light chain 6B (Smooth muscle and nonmuscle myosin light chain alkali 6B) 207 22,749 Chain (1); Domain (3) FUNCTION: Regulatory light chain of myosin. Does not bind calcium. {ECO:0000305}. SUBUNIT: Myosin is a hexamer of 2 heavy chains and 4 light chains. +Q9DBN5 LONP2_MOUSE Lon protease homolog 2, peroxisomal (EC 3.4.21.53) (Lon protease-like protein 2) (Lon protease 2) (Peroxisomal Lon protease) 852 94,526 Active site (2); Alternative sequence (3); Chain (1); Domain (2); Initiator methionine (1); Modified residue (1); Motif (1); Nucleotide binding (1); Sequence conflict (4) FUNCTION: ATP-dependent serine protease that mediates the selective degradation of misfolded and unassembled polypeptides in the peroxisomal matrix. Necessary for type 2 peroxisome targeting signal (PTS2)-containing protein processing and facilitates peroxisome matrix protein import. May indirectly regulate peroxisomal fatty acid beta-oxidation through degradation of the self-processed forms of TYSND1. {ECO:0000255|HAMAP-Rule:MF_03121}. SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000250|UniProtKB:Q86WA8, ECO:0000255|HAMAP-Rule:MF_03121}. SUBUNIT: Interacts with PEX5. Interacts with TYSND1 (By similarity). May interact with enzymes involved in beta-oxidation of fatty acids, including ACOX1/AOX (By similarity). {ECO:0000250|UniProtKB:Q86WA8, ECO:0000255|HAMAP-Rule:MF_03121}. +P18165 LORI_MOUSE Loricrin 486 38,200 Chain (1); Sequence conflict (6) FUNCTION: Major keratinocyte cell envelope protein. PTM: Substrate of transglutaminases. Some glutamines and lysines are cross-linked to other loricrin molecules and to SPRRs proteins.; PTM: Contains inter- or intramolecular disulfide-bonds. {ECO:0000250}. +P97873 LOXL1_MOUSE Lysyl oxidase homolog 1 (EC 1.4.3.-) (Lysyl oxidase 2) (Lysyl oxidase-like protein 1) 607 66,506 Chain (1); Cross-link (1); Disulfide bond (5); Metal binding (3); Modified residue (1); Propeptide (1); Region (1); Sequence conflict (4); Signal peptide (1) FUNCTION: Active on elastin and collagen substrates. {ECO:0000250}. PTM: The lysine tyrosylquinone cross-link (LTQ) is generated by condensation of the epsilon-amino group of a lysine with a topaquinone produced by oxidation of tyrosine. {ECO:0000250|UniProtKB:P33072}. SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000305}. +Q8BLG2 LPAR4_MOUSE Lysophosphatidic acid receptor 4 (LPA receptor 4) (LPA-4) (G-protein coupled receptor 23) (P2Y purinoceptor 9) (P2Y9) (Purinergic receptor 9) 370 41,899 Chain (1); Disulfide bond (1); Glycosylation (4); Sequence conflict (3); Topological domain (8); Transmembrane (7) TRANSMEM 44 64 Helical; Name=1. {ECO:0000255}.; TRANSMEM 74 94 Helical; Name=2. {ECO:0000255}.; TRANSMEM 113 133 Helical; Name=3. {ECO:0000255}.; TRANSMEM 156 176 Helical; Name=4. {ECO:0000255}.; TRANSMEM 204 224 Helical; Name=5. {ECO:0000255}.; TRANSMEM 255 275 Helical; Name=6. {ECO:0000255}.; TRANSMEM 295 315 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 43 Extracellular. {ECO:0000255}.; TOPO_DOM 65 73 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 95 112 Extracellular. {ECO:0000255}.; TOPO_DOM 134 155 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 177 203 Extracellular. {ECO:0000255}.; TOPO_DOM 225 254 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 276 294 Extracellular. {ECO:0000255}.; TOPO_DOM 316 370 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for lysophosphatidic acid (LPA), a mediator of diverse cellular activities. Transduces a signal by increasing the intracellular calcium ions and by stimulating adenylyl cyclase activity. The rank order of potency for agonists of this receptor is 1-oleoyl- > 1-stearoyl- > 1-palmitoyl- > 1-myristoyl- > 1-alkyl- > 1-alkenyl-LPA (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +P48999 LOX5_MOUSE Arachidonate 5-lipoxygenase (5-LO) (5-lipoxygenase) (EC 1.13.11.34) 674 77,967 Chain (1); Domain (2); Metal binding (13); Modified residue (2); Mutagenesis (1); Sequence conflict (2); Site (1) Lipid metabolism; leukotriene A4 biosynthesis. FUNCTION: Catalyzes the first step in leukotriene biosynthesis, and thereby plays a role in inflammatory processes. {ECO:0000269|PubMed:7629107}. PTM: Serine phosphorylation by MAPKAPK2 is stimulated by arachidonic acid. Phosphorylation on Ser-524 by PKA has an inhibitory effect. Phosphorylation on Ser-272 prevents export from the nucleus (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00726, ECO:0000269|PubMed:7629107}. Nucleus matrix {ECO:0000269|PubMed:7629107}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Shuttles between cytoplasm and nucleus. Found exclusively in the nucleus, when phosphorylated on Ser-272. Calcium binding promotes translocation from the cytosol and the nuclear matrix to the nuclear envelope and membrane association (By similarity). {ECO:0000250}. SUBUNIT: Interacts with ALOX5AP and LTC4S. Interacts with COTL1, the interaction is required for stability and efficient catalytic activity (By similarity). {ECO:0000250}. +Q3UGP9 LRC58_MOUSE Leucine-rich repeat-containing protein 58 366 40,139 Chain (1); Modified residue (1); Repeat (9); Sequence conflict (1) +Q921G6 LRCH4_MOUSE Leucine-rich repeat and calponin homology domain-containing protein 4 680 73,163 Chain (1); Domain (1); Modified residue (12); Repeat (9) +W8DXL4 LRIT3_MOUSE Leucine-rich repeat, immunoglobulin-like domain and transmembrane domain-containing protein 3 681 74,827 Chain (1); Disulfide bond (1); Domain (1); Glycosylation (4); Repeat (5); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 585 605 Helical. {ECO:0000255}. TOPO_DOM 20 584 Lumenal. {ECO:0000305}.; TOPO_DOM 606 681 Cytoplasmic. {ECO:0000305}. FUNCTION: Required in retinal ON-bipolar cells for normal localization of the cation channel TRPM1 at dendrite tips (PubMed:25997951). May also have a role in cone synapse formation (PubMed:25997951). Might facilitate FGFR1 exit from the endoplasmic reticulum to the Golgi (By similarity). Could be a regulator of the FGFRs (By similarity). {ECO:0000250|UniProtKB:Q3SXY7, ECO:0000269|PubMed:25997951}. SUBCELLULAR LOCATION: Cell projection, dendrite {ECO:0000269|PubMed:25997951}. Perikaryon {ECO:0000269|PubMed:25997951}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q3SXY7}; Single-pass type I membrane protein {ECO:0000305}. Note=Punctate expression at dendrite tips. {ECO:0000269|PubMed:25997951}. TISSUE SPECIFICITY: Detected in the outer plexiform layer (OPL) of the retina, where it localizes to rod and cone ON-bipolar cells (at protein level). Also detected in bipolar cell bodies in the inner retinal layer (INL) (at protein level). {ECO:0000269|PubMed:25997951}. +Q91W20 LRC26_MOUSE Leucine-rich repeat-containing protein 26 (BK channel auxiliary gamma subunit LRRC26) 331 35,696 Chain (1); Disulfide bond (4); Domain (2); Repeat (5); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 262 282 Helical. {ECO:0000255}. TOPO_DOM 27 261 Extracellular. {ECO:0000255}.; TOPO_DOM 283 331 Cytoplasmic. {ECO:0000255}. FUNCTION: Auxiliary protein of the large-conductance, voltage and calcium-activated potassium channel (BK alpha). Required for the conversion of BK alpha channels from a high-voltage to a low-voltage activated channel type in non-excitable cells. These are characterized by negative membrane voltages and constant low levels of calcium (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Localizes to the cytoplasm when expressed at high levels. {ECO:0000250}. SUBUNIT: Interacts with KCNMA1. {ECO:0000250}. DOMAIN: The transmembrane domain is necessary for interaction with KCNMA1. {ECO:0000250}. +Q8BWJ4 LRAD4_MOUSE Low-density lipoprotein receptor class A domain-containing protein 4 306 33,857 Chain (1); Disulfide bond (2); Domain (1); Motif (3); Topological domain (2); Transmembrane (1) TRANSMEM 65 85 Helical. {ECO:0000255}. TOPO_DOM 1 64 Lumenal. {ECO:0000255}.; TOPO_DOM 86 306 Cytoplasmic. {ECO:0000255}. FUNCTION: Functions as a negative regulator of TGF-beta signaling and thereby probably plays a role in cell proliferation, differentiation, apoptosis, motility, extracellular matrix production and immunosuppression. In the canonical TGF-beta pathway, ZFYVE9/SARA recruits the intracellular signal transducer and transcriptional modulators SMAD2 and SMAD3 to the TGF-beta receptor. Phosphorylated by the receptor, SMAD2 and SMAD3 then form a heteromeric complex with SMAD4 that translocates to the nucleus to regulate transcription. Through interaction with SMAD2 and SMAD3, LDLRAD4 may compete with ZFYVE9 and SMAD4 and prevent propagation of the intracellular signal. {ECO:0000269|PubMed:24627487}. SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with PMEPA1. Interacts (via the SMAD interaction motif) with SMAD2 and SMAD3 (By similarity). {ECO:0000250}. DOMAIN: The SMAD interaction motif is required for interaction with SMAD2 and SMAD3 and the negative regulation of TGF-beta signaling. {ECO:0000250}. TISSUE SPECIFICITY: Detected in all tissues tested. {ECO:0000269|PubMed:24627487}. +Q8C031 LRC4C_MOUSE Leucine-rich repeat-containing protein 4C (Netrin-G1 ligand) (NGL-1) 640 71,992 Chain (1); Disulfide bond (1); Domain (3); Modified residue (1); Repeat (9); Sequence conflict (1); Signal peptide (1); Transmembrane (1) TRANSMEM 528 548 Helical. {ECO:0000255}. FUNCTION: May promote neurite outgrowth of developing thalamic neurons. {ECO:0000269|PubMed:14595443}. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane {ECO:0000250}; Single-pass type I membrane protein. SUBUNIT: Interacts with NTNG1 and WHRN. {ECO:0000269|PubMed:15590698}. DOMAIN: The LRR region is both necessary and sufficient for the interaction with NTNG1. {ECO:0000250}. +P62046 LRCH1_MOUSE Leucine-rich repeat and calponin homology domain-containing protein 1 (Calponin homology domain-containing protein 1) 709 79,076 Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (1); Modified residue (4); Repeat (9); Sequence conflict (2) FUNCTION: Acts as a negative regulator of GTPase CDC42 by sequestering CDC42-guanine exchange factor DOCK8. Probably by preventing CDC42 activation, negatively regulates CD4(+) T-cell migration in response to chemokine stimulation. {ECO:0000269|PubMed:28028151}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y2L9}. SUBUNIT: Interacts (via LRR repeats) with unphosphorylated DOCK8 (via DHR-2 domain); the interaction prevents the association between DOCK8 and CDC42. {ECO:0000269|PubMed:28028151}. +Q3UMG5 LRCH2_MOUSE Leucine-rich repeat and calponin homology domain-containing protein 2 773 84,989 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (2); Repeat (9); Sequence caution (1); Sequence conflict (1) +Q8CGC4 LS14B_MOUSE Protein LSM14 homolog B (Protein FAM61B) (RNA-associated protein 55B) (mRAP55B) 385 42,310 Chain (1); Cross-link (1); Domain (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (8); Motif (2); Sequence conflict (1) FUNCTION: May play a role in control of mRNA translation. {ECO:0000250}. SUBUNIT: Component of a ribonucleoprotein (RNP) complex. {ECO:0000250}. +O88653 LTOR3_MOUSE Ragulator complex protein LAMTOR3 (Late endosomal/lysosomal adaptor and MAPK and MTOR activator 3) (MEK-binding partner 1) (Mp1) (Mitogen-activated protein kinase kinase 1-interacting protein 1) (Mitogen-activated protein kinase scaffold protein 1) 124 13,553 Beta strand (6); Chain (1); Helix (6); Region (1); Turn (1) FUNCTION: As part of the Ragulator complex it is involved in amino acid sensing and activation of mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids. Activated by amino acids through a mechanism involving the lysosomal V-ATPase, the Ragulator functions as a guanine nucleotide exchange factor activating the small GTPases Rag. Activated Ragulator and Rag GTPases function as a scaffold recruiting mTORC1 to lysosomes where it is in turn activated. Adapter protein that enhances the efficiency of the MAP kinase cascade facilitating the activation of MAPK2. {ECO:0000269|PubMed:15263099, ECO:0000269|PubMed:9733512}. SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000269|PubMed:15263099, ECO:0000269|PubMed:19177150}; Peripheral membrane protein {ECO:0000269|PubMed:15263099, ECO:0000269|PubMed:19177150}; Cytoplasmic side {ECO:0000269|PubMed:15263099, ECO:0000269|PubMed:19177150}. SUBUNIT: Part of the Ragulator complex composed of LAMTOR1, LAMTOR2, LAMTOR3, LAMTOR4 and LAMTOR5. LAMTOR4 and LAMTOR5 form a heterodimer that interacts, through LAMTOR1, with a LAMTOR2, LAMTOR3 heterodimer. The Ragulator complex interacts with both the mTORC1 complex and heterodimers constituted of the Rag GTPases RRAGA, RRAGB, RRAGC and RRAGD; regulated by amino acid availability. The Ragulator complex interacts with SLC38A9; the probable amino acid sensor (By similarity). Interacts with LAMTOR1 and LAMTOR2; the interaction is direct (PubMed:11266467, PubMed:15263099, PubMed:19177150). Interacts with MAP2K1/MEK1 and MAPK2 (PubMed:9733512). Interacts with MORG1 (PubMed:15118098). {ECO:0000250|UniProtKB:Q9UHA4, ECO:0000269|PubMed:11266467, ECO:0000269|PubMed:15118098, ECO:0000269|PubMed:15263099, ECO:0000269|PubMed:19177150, ECO:0000269|PubMed:9733512}. +Q9D6I9 LURA1_MOUSE Leucine rich adaptor protein 1 (Leucine repeat adapter protein 35A) 239 25,830 Chain (1); Modified residue (3); Repeat (2) FUNCTION: Acts as an activator of the canonical NF-kappa-B pathway and drive the production of proinflammatory cytokines. Promotes the antigen (Ag)-presenting and priming function of dendritic cells via the canonical NF-kappa-B pathway. In concert with MYO18A and CDC42BPA/CDC42BPB, is involved in modulating lamellar actomyosin retrograde flow that is crucial to cell protrusion and migration. Activates CDC42BPA/CDC42BPB and targets it to actomyosin through its interaction with MYO18A, leading to MYL9/MLC2 phosphorylation and MYH9/MYH10-dependent actomyosin assembly in the lamella (By similarity). {ECO:0000250|UniProtKB:D4A8G3}. PTM: Phosphorylated. {ECO:0000250|UniProtKB:D4A8G3}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96LR2}. SUBUNIT: Forms a tripartite complex with CDC42BPA/CDC42BPB and MYO18A acting as an adapter connecting both. Its binding to CDC42BPA/CDC42BPB results in their activation by abolition of their negative autoregulation. Interacts with CDC42BPA and CDC42BPB. {ECO:0000250|UniProtKB:D4A8G3}. +Q8CC84 LYSM4_MOUSE LysM and putative peptidoglycan-binding domain-containing protein 4 293 31,660 Alternative sequence (1); Chain (1); Domain (1); Glycosylation (1); Topological domain (2); Transmembrane (1) TRANSMEM 215 235 Helical. {ECO:0000255}. TOPO_DOM 1 214 Extracellular. {ECO:0000255}.; TOPO_DOM 236 293 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +A2AE20 LYZL5_MOUSE Sperm acrosome-associated protein 5 (EC 3.2.1.17) (Lysozyme-like protein 5) 160 18,005 Active site (1); Chain (1); Disulfide bond (4); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q8BQ89 LIX1L_MOUSE LIX1-like protein 337 36,606 Chain (1); Erroneous initiation (1) +Q6P566 LIX1_MOUSE Protein limb expression 1 homolog 282 31,915 Chain (1); Frameshift (1); Sequence conflict (1) +P24527 LKHA4_MOUSE Leukotriene A-4 hydrolase (LTA-4 hydrolase) (EC 3.3.2.6) (Leukotriene A(4) hydrolase) 611 69,051 Active site (2); Chain (1); Metal binding (3); Modified residue (5); Mutagenesis (4); Region (3); Sequence conflict (2); Site (2) Lipid metabolism; leukotriene B4 biosynthesis. FUNCTION: Epoxide hydrolase that catalyzes the final step in the biosynthesis of the proinflammatory mediator leukotriene B4. Has also aminopeptidase activity. {ECO:0000269|PubMed:9287304}. PTM: Phosphorylation at Ser-416 inhibits enzymatic activity. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. +B1B1A0 LMBL4_MOUSE Lethal(3)malignant brain tumor-like protein 4 (L(3)mbt-like protein 4) 621 70,898 Alternative sequence (2); Chain (1); Domain (1); Repeat (3); Zinc finger (1) FUNCTION: Putative Polycomb group (PcG) protein. PcG proteins maintain the transcriptionally repressive state of genes, probably via a modification of chromatin, rendering it heritably changed in its expressibility (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q8C3X8 LMF2_MOUSE Lipase maturation factor 2 (Transmembrane protein 112B) (Transmembrane protein 153) 702 79,997 Chain (1); Glycosylation (1); Transmembrane (9) TRANSMEM 10 30 Helical. {ECO:0000255}.; TRANSMEM 75 95 Helical. {ECO:0000255}.; TRANSMEM 164 184 Helical. {ECO:0000255}.; TRANSMEM 226 246 Helical. {ECO:0000255}.; TRANSMEM 259 279 Helical. {ECO:0000255}.; TRANSMEM 316 336 Helical. {ECO:0000255}.; TRANSMEM 363 383 Helical. {ECO:0000255}.; TRANSMEM 398 418 Helical. {ECO:0000255}.; TRANSMEM 636 656 Helical. {ECO:0000255}. FUNCTION: Involved in the maturation of specific proteins in the endoplasmic reticulum. May be required for maturation and transport of active lipoprotein lipase (LPL) through the secretory pathway (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +P56563 LMIP_MOUSE Lens fiber membrane intrinsic protein (MP17) (MP18) (MP19) (MP20) 173 19,621 Chain (1); Glycosylation (3); Modified residue (1); Natural variant (1); Topological domain (5); Transmembrane (4) TRANSMEM 4 24 Helical. {ECO:0000255}.; TRANSMEM 67 87 Helical. {ECO:0000255}.; TRANSMEM 99 119 Helical. {ECO:0000255}.; TRANSMEM 141 161 Helical. {ECO:0000255}. TOPO_DOM 1 3 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 25 66 Extracellular. {ECO:0000255}.; TOPO_DOM 88 98 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 120 140 Extracellular. {ECO:0000255}.; TOPO_DOM 162 173 Cytoplasmic. {ECO:0000255}. FUNCTION: Present in the thicker 16-17 nm junctions of mammalian lens fiber cells, where it may contribute to cell junctional organization. Acts as a receptor for calmodulin. May play an important role in both lens development and cataractogenesis. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SUBUNIT: Seems to be associated with itself or another lens membrane component via disulfide bonds. {ECO:0000250}. DISEASE: Note=Defects in Lim2 are the cause of the cataractous mouse mutant with total opacity of lens 3 (To3). Mice heterozygous or homozygous for the To3 mutation have total opacity of the lens with a dense cataract. In addition, the To3/To3 homozygotes exhibit microphthalmia, abnormally small eyes. {ECO:0000269|PubMed:9238094}. +P59178 LMBL2_MOUSE Lethal(3)malignant brain tumor-like protein 2 (L(3)mbt-like protein 2) 703 78,971 Chain (1); Compositional bias (2); Cross-link (5); Modified residue (6); Repeat (4); Sequence conflict (2); Zinc finger (1) FUNCTION: Putative Polycomb group (PcG) protein. PcG proteins maintain the transcriptionally repressive state of genes, probably via a modification of chromatin, rendering it heritably changed in its expressibility. Its association with a chromatin-remodeling complex suggests that it may contribute to prevent expression of genes that trigger the cell into mitosis. Binds to monomethylated and dimethylated 'Lys-20' on histone H4. Binds histone H3 peptides that are monomethylated or dimethylated on 'Lys-4', 'Lys-9' or 'Lys-27' (By similarity). {ECO:0000250}. PTM: Phosphorylated. {ECO:0000269|PubMed:14597177}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14597177}. SUBUNIT: Part of the E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1, RING1, RNF2, MBLR, BAT8 and YAF2. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:14597177}. +Q8VCD3 LMA1L_MOUSE Protein ERGIC-53-like (ERGIC53-like protein) (Lectin mannose-binding 1-like) (LMAN1-like protein) (Sublingual acinar membrane protein) (Slamp) 505 56,312 Alternative sequence (2); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 439 459 Helical. {ECO:0000255}. TOPO_DOM 26 438 Lumenal. {ECO:0000255}.; TOPO_DOM 460 505 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. +O70263 LNX1_MOUSE E3 ubiquitin-protein ligase LNX (EC 2.3.2.27) (Ligand of Numb protein X 1) (Ligand of Numb-binding protein 1) (Numb-binding protein 1) (RING-type E3 ubiquitin transferase LNX) 728 80,157 Alternative sequence (3); Beta strand (6); Chain (1); Domain (4); Helix (2); Modified residue (1); Motif (1); Mutagenesis (9); Region (1); Sequence conflict (1); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of NUMB. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates ubiquitination of isoform p66 and isoform p72 of NUMB, but not that of isoform p71 or isoform p65. {ECO:0000269|PubMed:11782429, ECO:0000269|PubMed:14990566, ECO:0000269|PubMed:9535908}.; FUNCTION: Isoform 2 provides an endocytic scaffold for IGSF5/JAM4. {ECO:0000269|PubMed:9535908}. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Interacts with CXADR. Interacts with MAGEB18 and MAGEF1 (By similarity). Interacts with the phosphotyrosine interaction domain of all isoforms of NUMB. IGSF5/JAM4 interacts with isoform 2 through the second PDZ domain, other isoforms may also interact with IGSF5/JAM4. {ECO:0000250, ECO:0000269|PubMed:14990566, ECO:0000269|PubMed:16832352}. DOMAIN: The NPXY motif is required for the interaction with the PID domain of NUMB. It is however not sufficient.; DOMAIN: The PDZ 1 domain participates in the interaction with the PID domain of NUMB, and participates in the isoform-specific ubiquitination of NUMB. The PDZ 2 domain of isoform 2 participates in the interaction with IGSF5/JAM4, other isoforms containing this domain may also interact with IGSF5/JAM4. TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in the heart. Isoform 1 is also expressed in kidney, lung and skeletal muscle while isoform 2 is also expressed in brain. {ECO:0000269|PubMed:9535908}. +Q3URS3 LRCL1_MOUSE Leucine-rich colipase-like protein 1 (Colipase-like protein 3) 161 18,181 Alternative sequence (1); Chain (1); Signal peptide (1) +Q14BP6 LR74B_MOUSE Leucine-rich repeat-containing protein 74B 391 41,701 Alternative sequence (3); Chain (1); Repeat (9) +Q9D5S7 LRGUK_MOUSE Leucine-rich repeat and guanylate kinase domain-containing protein 820 93,190 Chain (1); Domain (2); Nucleotide binding (1); Repeat (9) FUNCTION: Involved in multiple aspects of sperm assembly including acrosome attachment, shaping of the sperm head and in the early aspects of axoneme development (PubMed:25781171). Not essential for primary cilium biogenesis (PubMed:28003339). {ECO:0000269|PubMed:25781171, ECO:0000269|PubMed:28003339}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:25781171, ECO:0000269|PubMed:28003339}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:28003339}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:28003339}. Note=Localizes to the acrosome and acroplaxome in round spermatids. Localizes to the manchette during spermiogenesis. Also found in the basal body of elongating spermatids, and in primary cilia of somatic cells. {ECO:0000269|PubMed:25781171, ECO:0000269|PubMed:28003339}. SUBUNIT: Interacts (via guanylate kinase-like domain) with RIMBP3 (via coiled-coil region) (PubMed:28003339). Interacts (via guanylate kinase-like domain) with HOOK2 (PubMed:25781171, PubMed:28003339). Interacts (via LRRCT domain) with KLC3. Interacts with HOOK1 and HOOK3 (PubMed:28003339). {ECO:0000269|PubMed:25781171, ECO:0000269|PubMed:28003339}. TISSUE SPECIFICITY: Highly expressed in the testis (PubMed:25781171). During spermatid development is initially localised to a supra-nuclear region of round spermatids, and is particularly evident at the leading edge of the developing acrosome and acroplaxome. As maturation proceeded and nuclear elongation initiated, LRGUK moves distally to ultimately reside on the microtubules of the manchette. LRGUK is also evident in the sperm basal body and the sperm tail (PubMed:25781171). {ECO:0000269|PubMed:25781171}. +Q505F5 LRC47_MOUSE Leucine-rich repeat-containing protein 47 581 63,590 Chain (1); Coiled coil (1); Compositional bias (1); Modified residue (3); Repeat (7); Sequence conflict (2) +Q9JI60 LRAT_MOUSE Lecithin retinol acyltransferase (EC 2.3.1.135) (Phosphatidylcholine--retinol O-acyltransferase) (Phosphatidylcholine-retinol-O-acyltransferase) 231 25,820 Active site (1); Beta strand (2); Chain (1); Helix (1); Topological domain (2); Transmembrane (1) TRANSMEM 195 215 Helical. {ECO:0000255}. TOPO_DOM 1 194 Cytoplasmic. {ECO:0000269|PubMed:17114808}.; TOPO_DOM 216 231 Lumenal. {ECO:0000269|PubMed:17114808}. Cofactor metabolism; retinol metabolism. FUNCTION: Transfers the acyl group from the sn-1 position of phosphatidylcholine to all-trans retinol, producing all-trans retinyl esters. Retinyl esters are storage forms of vitamin A. LRAT plays a critical role in vision. It provides the all-trans retinyl ester substrates for the isomerohydrolase which processes the esters into 11-cis-retinol in the retinal pigment epithelium; due to a membrane-associated alcohol dehydrogenase, 11 cis-retinol is oxidized and converted into 11-cis-retinaldehyde which is the chromophore for rhodopsin and the cone photopigments (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:17114808}; Single-pass membrane protein {ECO:0000269|PubMed:17114808}. Rough endoplasmic reticulum {ECO:0000250}. Endosome, multivesicular body {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Present in the rough endoplasmic reticulum and multivesicular body in hepatic stellate cells. Present in the rough endoplasmic reticulum and perinuclear region in endothelial cells (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Hepatic stellate cells and endothelial cells (at protein level). {ECO:0000269|PubMed:18544127}. +A6H6A4 LRIQ4_MOUSE Leucine-rich repeat and IQ domain-containing protein 4 596 68,010 Alternative sequence (1); Chain (1); Domain (1); Repeat (22) +Q80VQ1 LRRC1_MOUSE Leucine-rich repeat-containing protein 1 524 59,412 Alternative sequence (3); Chain (1); Coiled coil (1); Compositional bias (1); Erroneous initiation (1); Modified residue (1); Repeat (17); Sequence conflict (2) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Localized at the basolateral side of epithelial cells. {ECO:0000250}. SUBUNIT: Interacts with DLG1. May form a complex with DLG1 and ERBIN, where interaction between LRRC1 and ERBIN is indirect (By similarity). {ECO:0000250}. +Q99PH1 LRRC4_MOUSE Leucine-rich repeat-containing protein 4 (Brain tumor-associated protein MBAG1) (Netrin-G2 ligand) (NGL-2) 652 72,619 Chain (1); Compositional bias (1); Disulfide bond (5); Domain (3); Glycosylation (8); Repeat (9); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 527 547 Helical. {ECO:0000255}. TOPO_DOM 41 526 Extracellular. {ECO:0000255}.; TOPO_DOM 548 652 Cytoplasmic. {ECO:0000255}. FUNCTION: Synaptic adhesion protein. Regulates the formation of exitatory synapses through the recruitment of pre-and-postsynaptic proteins. Organize the lamina/pathway-specific differentiation of dendrites. Plays a important role for auditory synaptic responses. Involved in the suppression of glioma. {ECO:0000269|PubMed:15967442, ECO:0000269|PubMed:16980967, ECO:0000269|PubMed:17785411}. PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. Cell junction, synapse, postsynaptic cell membrane {ECO:0000250}. Note=LRRC4 and DLG4 are interdependent for synaptic localization. {ECO:0000250}. SUBUNIT: Interacts (via LRR repeats) with NTNG2. Interacts with DLG4. Forms a complex with DLG4 and with NMDA receptors. {ECO:0000269|PubMed:16980967, ECO:0000269|PubMed:17973922}. DOMAIN: The last 4 C-terminal residues bind to the first 2 PDZ domains of DLG4. TISSUE SPECIFICITY: Specifically expressed in brain. In the hippocampus, parietal cortex and piriform cortex expressed in proximal segments of CA1 pyramidal neurons. {ECO:0000269|PubMed:15967442, ECO:0000269|PubMed:17785411}. +Q8VI56 LRP4_MOUSE Low-density lipoprotein receptor-related protein 4 (LRP-4) (LDLR dan) 1905 211,954 Alternative sequence (1); Chain (1); Disulfide bond (33); Domain (11); Glycosylation (7); Repeat (20); Sequence caution (2); Sequence conflict (5); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1726 1746 Helical. {ECO:0000255}. TOPO_DOM 21 1725 Extracellular. {ECO:0000255}.; TOPO_DOM 1747 1905 Cytoplasmic. {ECO:0000255}. FUNCTION: Mediates SOST-dependent inhibition of bone formation. Functions as a specific facilitator of SOST-mediated inhibition of Wnt signaling. Plays a key role in the formation and the maintenance of the neuromuscular junction (NMJ), the synapse between motor neuron and skeletal muscle. Directly binds AGRIN and recruits it to the MUSK signaling complex. Mediates the AGRIN-induced phosphorylation of MUSK, the kinase of the complex. The activation of MUSK in myotubes induces the formation of NMJ by regulating different processes including the transcription of specific genes and the clustering of AChR in the postsynaptic membrane. Alternatively, may be involved in the negative regulation of the canonical Wnt signaling pathway, being able to antagonize the LRP6-mediated activation of this pathway. More generally, has been proposed to function as a cell surface endocytic receptor binding and internalizing extracellular ligands for degradation by lysosomes. Plays an essential role in the process of digit differentiation (PubMed:16517118). {ECO:0000269|PubMed:16517118, ECO:0000269|PubMed:18848351, ECO:0000269|PubMed:21471202}. PTM: N-glycosylation is required for cell surface location. {ECO:0000269|PubMed:24140340}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24140340}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Homooligomer. Interacts with MUSK; the heterodimer forms an AGRIN receptor complex that binds AGRIN resulting in activation of MUSK. Interacts (via the extracellular domain) with SOST; the interaction facilitates the inhibition of Wnt signaling (By similarity). Interacts with MESD; the interaction promotes glycosylation of LRP4 and its cell-surface expression (PubMed:24140340). {ECO:0000250, ECO:0000269|PubMed:24140340}. DISEASE: Note=Defects in Lrp4 are the cause of digitation anormale (dan) phenotype, this mutation is the consequence of a retroviral insertion. Dan mice shown growth retardation in 10-day-old mice dan/dan and polysyndactyly (PubMed:16517118). Defects in Lrp4 are the cause of malformed digits (mdig) phenotype. It is a spontaneous, autosomal recessive mutation resulting in polysyndactyly (PubMed:16517118). {ECO:0000269|PubMed:16517118}. +Q91VN0 LRP5_MOUSE Low-density lipoprotein receptor-related protein 5 (LRP-5) (Low-density lipoprotein receptor-related protein 7) (LRP-7) 1614 178,885 Chain (1); Disulfide bond (21); Domain (7); Glycosylation (6); Motif (5); Region (4); Repeat (20); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1384 1406 Helical. {ECO:0000255}. TOPO_DOM 31 1383 Extracellular. {ECO:0000255}.; TOPO_DOM 1407 1614 Cytoplasmic. {ECO:0000255}. FUNCTION: Acts as a coreceptor with members of the frizzled family of seven-transmembrane spanning receptors to transduce signal by Wnt proteins. Activates the canonical Wnt signaling pathway that controls cell fate determination and self-renewal during embryonic development and adult tissue regeneration (PubMed:11956231). In particular, may play an important role in the development of the posterior patterning of the epiblast during gastrulation (PubMed:15142971). During bone development, regulates osteoblast proliferation and differentiation thus determining bone mass (PubMed:11956231). Mechanistically, the formation of the signaling complex between Wnt ligand, frizzled receptor and LRP5 coreceptor promotes the recruitment of AXIN1 to LRP5, stabilizing beta-catenin/CTNNB1 and activating TCF/LEF-mediated transcriptional programs (By similarity). Acts as a coreceptor for non-Wnt proteins, such as norrin/NDP. Binding of norrin/NDP to frizzled 4/FZD4-LRP5 receptor complex triggers beta-catenin/CTNNB1-dependent signaling known to be required for retinal vascular development (By similarity). Plays a role in controlling postnatal vascular regression in retina via macrophage-induced endothelial cell apoptosis (PubMed:11956231). {ECO:0000250|UniProtKB:O75197, ECO:0000269|PubMed:11956231, ECO:0000269|PubMed:15142971}. PTM: Phosphorylation of cytoplasmic PPPSP motifs regulates the signal transduction of the Wnt signaling pathway through acting as a docking site for AXIN1. {ECO:0000250|UniProtKB:O75197}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12581525}; Single-pass type I membrane protein {ECO:0000269|PubMed:12581525}. Endoplasmic reticulum {ECO:0000269|PubMed:12581525}. Note=Chaperoned to the plasma membrane by MESD. {ECO:0000250}. SUBUNIT: Homodimer; disulfide-linked. Forms phosphorylated oligomer aggregates on Wnt-signaling (PubMed:12581525). Component of a WNT-signaling complex that contains a WNT protein, a FZD protein and LRP5 or LRP6. Interacts with FZD8; the interaction is formed on WNT-binding and signaling. Interacts (via the phosphorylated PPPSP motif domains) with AXIN1; the interaction prevents inhibition of beta-catenin phosphorylation and signaling and is enhanced in the presence of GSK3B and WNT1 or WNT3A. Interacts (via beta-propeller regions 3 and 4) with DKK1; the interaction, enhanced by MESD and/or KREMEN, inhibits beta-catenin signaling by preventing GSK3-mediated phosphorylation of the PPPSP motifs and subsequent, AXIN1 binding. Interacts with CSNK1E. Interacts with SOST; the interaction antagonizes canonical Wnt signaling. Interacts with APCDD1 (By similarity). Interacts with MESD; the interaction prevents the formation of LRP5 aggregates, targets LRP5 to the plasma membrane and, when complexed with KREMEN2, increases DKK1 binding (PubMed:12581525). Interacts with CAPRIN2 (By similarity). {ECO:0000250|UniProtKB:O75197, ECO:0000269|PubMed:12581525}. TISSUE SPECIFICITY: Widely expressed, with the highest expression levels in liver, heart, and lung and the lowest levels in brain and spleen. {ECO:0000269|PubMed:10049586, ECO:0000269|PubMed:11956231}. +O88572 LRP6_MOUSE Low-density lipoprotein receptor-related protein 6 (LRP-6) 1613 180,255 Chain (1); Compositional bias (3); Cross-link (1); Disulfide bond (21); Domain (7); Glycosylation (9); Lipidation (2); Modified residue (5); Motif (5); Natural variant (1); Region (4); Repeat (20); Sequence conflict (5); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1371 1393 Helical. {ECO:0000255}. TOPO_DOM 20 1370 Extracellular. {ECO:0000255}.; TOPO_DOM 1394 1613 Cytoplasmic. {ECO:0000255}. FUNCTION: Component of the Wnt-Fzd-LRP5-LRP6 complex that triggers beta-catenin signaling through inducing aggregation of receptor-ligand complexes into ribosome-sized signalsomes. Cell-surface coreceptor of Wnt/beta-catenin signaling, which plays a pivotal role in bone formation. The Wnt-induced Fzd/LRP6 coreceptor complex recruits DVL1 polymers to the plasma membrane which, in turn, recruits the AXIN1/GSK3B-complex to the cell surface promoting the formation of signalsomes and inhibiting AXIN1/GSK3-mediated phosphorylation and destruction of beta-catenin. Required for posterior patterning of the epiblast during gastrulation (By similarity). {ECO:0000250, ECO:0000269|PubMed:15142971}. PTM: Dual phosphorylation of cytoplasmic PPPSP motifs sequentially by GSK3 and CK1 is required for AXIN1-binding, and subsequent stabilization and activation of beta-catenin via preventing GSK3-mediated phosphorylation of beta-catenin. Phosphorylated, in vitro, by GRK5/6 within and outside the PPPSP motifs. Phosphorylation at Ser-1490 by CDK14 during G2/M phase leads to regulation of the Wnt signaling pathway during the cell cycle. Phosphorylation by GSK3B is induced by RPSO1 binding and inhibited by DKK1. Phosphorylated, in vitro, by casein kinase I on Thr-1479 (By similarity). {ECO:0000250}.; PTM: Undergoes gamma-secretase-dependent regulated intramembrane proteolysis (RIP). The extracellular domain is first released by shedding, and then, through the action of gamma-secretase, the intracellular domain (ICD) is released into the cytoplasm where it is free to bind to GSK3B and to activate canonical Wnt signaling (By similarity). {ECO:0000250}.; PTM: Palmitoylation on the two sites near the transmembrane domain leads to release of LRP6 from the endoplasmic reticulum. {ECO:0000250}.; PTM: Mono-ubiquitinated which retains LRP6 in the endoplasmic reticulum. Ubiquitinated by ZNRF3, leading to its degradation by the proteasome (By similarity). {ECO:0000250}.; PTM: N-glycosylation is required for cell surface location. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Endoplasmic reticulum. Membrane raft {ECO:0000250|UniProtKB:O75581}. Note=On Wnt signaling, undergoes a cycle of caveolin- or clathrin-mediated endocytosis and plasma membrane location. Released from the endoplasmic reticulum on palmitoylation. Mono-ubiquitination retains it in the endoplasmic reticulum in the absence of palmitoylation. On Wnt signaling, phosphorylated, aggregates and colocalizes with AXIN1 and GSK3B at the plasma membrane in LRP6-signalsomes (By similarity). Chaperoned to the plasma membrane by MESD. {ECO:0000250}. SUBUNIT: Homodimer; disulfide-linked (By similarity). Forms phosphorylated oligomer aggregates on Wnt-signaling (By similarity). Component of the Wnt-Fzd-LRP5-LRP6 complex. Interacts (via the extracellular domain) with WNT1; the interaction is enhanced by prior formation of the Wnt/Fzd complex. Interacts (via the beta-propeller regions 3 and 4) with WNT3A. Interacts (via the beta-propeller regions 1 and 2) with WNT9B. Interacts with FZD5; the interaction forms a coreceptor complex for Wnt signaling and is inhibited by DKK1 and DRAXIN. Interacts (via beta propeller region) with DKK1; the interaction inhibits FZD5/LRP6 complex formation. Interacts with DKK2. Interacts (via the phosphorylated PPPSP motifs) with AXIN1; the interaction recruits the AXIN1/GSK3B complex to cell surface LRP6 signalsomes. Interacts (via the extracellular domain) with RSPO1; the interaction activates Wnt/beta-catenin signaling. Interacts (via the extracellular domain) with RSPO3 (via the cysteine rich domain); the interaction activates Wnt/beta-catenin signaling. Interacts (via the beta-propeller regions 1 and 2) with SOST; the interaction competes with DKK1 for binding for inhibiting beta-catenin signaling. Interacts (via the cytoplasmic domain) with CSNKIE; the interaction phosphorylates LRP6, binds AXIN1 and inhibits AXIN1/GSK3B-mediated phosphorylation of beta-catenin (By similarity). Interacts with DRAXIN; the interaction inhibits Wnt signaling. Interacts with GRB10; the interaction prevents AXIN1 binding, thus negatively regulating the Wnt signaling pathway. Interacts with MESD; the interaction prevents the formation of LRP6 aggregates and targets LRP6 to the plasma membrane. Interacts with MACF1. Interacts with DAB2; the interaction involves LRP6 phosphorylation by CK2 and sequesters LRP6 towards clathrin-mediated endocytosis. Interacts with TMEM198 (By similarity). Interacts with CAPRIN2; the interaction promotes LRP6 phosphorylation at Ser-1490 (By similarity). Found in a complex with CAPRIN2, CCNY and CDK14 during G2/M stage; CAPRIN2 functions as a scaffold for the complex by binding to CCNY via its N terminus and to CDK14 via its C terminus. Interacts with LYPD6. Forms a ternary complex with DKK1 and KREM1 (By similarity). Interacts with KREM1 in a DKK1-dependent manner (By similarity). {ECO:0000250|UniProtKB:O75581, ECO:0000269|PubMed:12581525, ECO:0000269|PubMed:16543246, ECO:0000269|PubMed:17376403, ECO:0000269|PubMed:18505367, ECO:0000269|PubMed:19857465}. DOMAIN: The YWTD-EGF-like domains 1 and 2 are required for the interaction with Wnt-frizzled complex. The YWTD-EGF-like domains 3 and 4 are required for the interaction with DKK1 (By similarity). {ECO:0000250}.; DOMAIN: The PPPSP motifs play a central role in signal transduction by being phosphorylated, leading to activate the Wnt signaling pathway. TISSUE SPECIFICITY: Expressed in early embryo. Broadly expressed throughout the embryonic ectoderm and in nascent mesoderm, and in endoderm emerging from the primitive streak. {ECO:0000269|PubMed:15142971}. DISEASE: Note=Defects in Lrp6 are the cause of Ringelschwanz (rs) phenotype. Rs phenotype is a spontaneous mutation that is characterized by a combination of multiple Wnt-deficient phenotypes including dysmorphologies of the axial skeleton, digits and the neural tube. The establishment of the anteroposterior somite compartments, the epithelialization of nascent somites, and the formation of segment borders are disturbed in (rs) mutants. There is delayed ossification at birth and a low bone mass phenotype in adults. Functional analyzes reveal impaired targeting to the plasma surface due to reduced interaction with MESD leading to inhibited Wnt/beta-catenin signaling. {ECO:0000269|PubMed:15469977, ECO:0000269|PubMed:18505367}. +Q9DCJ1 LST8_MOUSE Target of rapamycin complex subunit LST8 (TORC subunit LST8) (G protein beta subunit-like) (Protein GbetaL) (Mammalian lethal with SEC13 protein 8) (mLST8) 326 35,851 Chain (1); Modified residue (1); Repeat (7); Sequence conflict (6) FUNCTION: Subunit of both mTORC1 and mTORC2, which regulates cell growth and survival in response to nutrient and hormonal signals. mTORC1 is activated in response to growth factors or amino acids. Growth factor-stimulated mTORC1 activation involves a AKT1-mediated phosphorylation of TSC1-TSC2, which leads to the activation of the RHEB GTPase that potently activates the protein kinase activity of mTORC1. Amino acid-signaling to mTORC1 requires its relocalization to the lysosomes mediated by the Ragulator complex and the Rag GTPases. Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. mTORC1 phosphorylates EIF4EBP1 and releases it from inhibiting the elongation initiation factor 4E (eiF4E). mTORC1 phosphorylates and activates S6K1 at 'Thr-389', which then promotes protein synthesis by phosphorylating PDCD4 and targeting it for degradation. Within mTORC1, LST8 interacts directly with MTOR and enhances its kinase activity. In nutrient-poor conditions, stabilizes the MTOR-RPTOR interaction and favors RPTOR-mediated inhibition of MTOR activity. mTORC2 is also activated by growth factors, but seems to be nutrient-insensitive. mTORC2 seems to function upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors. mTORC2 promotes the serum-induced formation of stress-fibers or F-actin. mTORC2 plays a critical role in AKT1 'Ser-473' phosphorylation, which may facilitate the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1 which is a prerequisite for full activation. mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422'. mTORC2 also modulates the phosphorylation of PRKCA on 'Ser-657'. {ECO:0000269|PubMed:17141160}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Part of the mammalian target of rapamycin complex 1 (mTORC1) which contains MTOR, MLST8, RPTOR, AKT1S1/PRAS40 and DEPTOR (By similarity). mTORC1 binds to and is inhibited by FKBP12-rapamycin. Part of the mammalian target of rapamycin complex 2 (mTORC2) which contains MTOR, MLST8, PRR5, RICTOR, MAPKAP1 and DEPTOR (By similarity). Contrary to mTORC1, mTORC2 does not bind to and is not sensitive to FKBP12-rapamycin. Interacts directly with MTOR and RPTOR. Interacts with RHEB (By similarity). Interacts with MTOR. {ECO:0000250, ECO:0000269|PubMed:12718876, ECO:0000269|PubMed:20801936}. +Q8R4H7 NAGS_MOUSE N-acetylglutamate synthase, mitochondrial (EC 2.3.1.1) (Amino-acid acetyltransferase) [Cleaved into: N-acetylglutamate synthase long form; N-acetylglutamate synthase short form; N-acetylglutamate synthase conserved domain form] 527 57,489 Alternative sequence (1); Binding site (2); Chain (3); Domain (1); Region (2); Sequence conflict (1); Transit peptide (1) Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4. FUNCTION: Plays a role in the regulation of ureagenesis by producing the essential cofactor N-acetylglutamate (NAG), thus modulating carbamoylphosphate synthase I (CPS1) activity. {ECO:0000269|PubMed:12049647}. PTM: Probably processed by mitochondrial processing peptidase (MPP). The long form has not yet been isolated. {ECO:0000269|PubMed:15050968}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:Q8N159}. SUBUNIT: Homodimer (By similarity). Homotetramer (PubMed:23894642). {ECO:0000250|UniProtKB:Q8N159, ECO:0000269|PubMed:23894642}. DOMAIN: The amino-acid kinase (AAK) domain mediates binding of the allosteric activator L-arginine. {ECO:0000250|UniProtKB:Q8N159}. TISSUE SPECIFICITY: Highly expressed in the liver and small intestine. Weakly expressed in the kidney, spleen and testis. {ECO:0000269|PubMed:12049647}. +Q8C5H8 NAKD2_MOUSE NAD kinase 2, mitochondrial (EC 2.7.1.23) (Mitochondrial NAD kinase) (NAD kinase domain-containing protein 1, mitochondrial) 452 50,859 Alternative sequence (3); Chain (1); Erroneous initiation (1); Frameshift (1); Modified residue (8); Sequence conflict (3); Transit peptide (1) FUNCTION: Mitochondrial NAD(+) kinase that phosphorylates NAD(+) to yield NADP(+). Can use both ATP or inorganic polyphosphate as the phosphoryl donor (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +Q3TKR3 NAL4C_MOUSE NACHT, LRR and PYD domains-containing protein 4C (NALP-alpha) 982 112,674 Chain (1); Domain (2); Nucleotide binding (1); Repeat (7); Sequence conflict (1) FUNCTION: May be involved in inflammation and recognition of cytosolic pathogen-associated molecular patterns (PAMPs) not intercepted by membrane-bound receptors. {ECO:0000250}. +Q66X05 NAL4F_MOUSE NACHT, LRR and PYD domains-containing protein 4F (NALP-kappa) 959 110,368 Chain (1); Domain (2); Nucleotide binding (1); Repeat (8) FUNCTION: May be involved in inflammation and recognition of cytosolic pathogen-associated molecular patterns (PAMPs) not intercepted by membrane-bound receptors. {ECO:0000250}. +Q7M758 NALDL_MOUSE N-acetylated-alpha-linked acidic dipeptidase-like protein (NAALADase L) (EC 3.4.17.21) 745 80,513 Active site (4); Chain (1); Compositional bias (1); Glycosylation (10); Metal binding (6); Region (1); Topological domain (2); Transmembrane (1) TRANSMEM 7 28 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 29 745 Extracellular. {ECO:0000255}. FUNCTION: Has no NAAG hydrolyzing activity (By similarity). Exhibits a dipeptidyl-peptidase IV type activity. In vitro, cleaves Gly-Pro-AMC (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Ileal brush border membrane. {ECO:0000250}. +Q80TN7 NAV3_MOUSE Neuron navigator 3 (Pore membrane and/or filament-interacting-like protein 1) 2359 252,301 Chain (1); Coiled coil (3); Compositional bias (3); Domain (1); Erroneous termination (1); Modified residue (2) FUNCTION: May regulate IL2 production by T-cells. May be involved in neuron regeneration. {ECO:0000269|PubMed:12062803}. SUBCELLULAR LOCATION: Nucleus outer membrane {ECO:0000269|PubMed:12062803}. TISSUE SPECIFICITY: Present in neurons from central and peripheral nervous systems (at protein level). Highly expressed in brain cortex, midbrain, cerebellum and hippocampus. {ECO:0000269|PubMed:12062803}. +Q9WV84 NDKM_MOUSE Nucleoside diphosphate kinase, mitochondrial (NDK) (NDP kinase, mitochondrial) (EC 2.7.4.6) (Nucleoside diphosphate kinase D) (NDPKD) (nm23-M4) 186 20,549 Active site (1); Binding site (6); Chain (1); Transit peptide (1) FUNCTION: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Through the catalyzed exchange of gamma-phosphate between di- and triphosphonucleosides participates in regulation of intracellular nucleotide homeostasis. Binds to anionic phospholipids, predominantly to cardiolipin; the binding inhibits its phosphotransfer activity. Acts as mitochondria-specific NDK; its association with cardiolipin-containing mitochondrial inner membrane is coupled to respiration suggesting that ADP locally regenerated in the mitochondrion innermembrane space by its activity is directly taken up via ANT ADP/ATP translocase into the matrix space to stimulate respiratory ATP regeneration. Proposed to increase GTP-loading on dynamin-related GTPase OPA1 in mitochondria. In vitro can induce liposome cross-linking suggesting that it can cross-link inner and outer membranes to form contact sites, and promotes intermembrane migration of anionic phosphoplipids. Promotes the redistribution of cardiolipin between the mitochondrial inner membrane and outer membrane which is implicated in pro-apoptotic signaling (By similarity). {ECO:0000250|UniProtKB:O00746}. SUBCELLULAR LOCATION: Mitochondrion intermembrane space {ECO:0000250|UniProtKB:O00746}; Peripheral membrane protein. Mitochondrion matrix {ECO:0000250|UniProtKB:O00746}. Note=Predominantly localized in the mitochondrion intermembrane space. Colocalizes with OPA1 in mitochondria (By similarity). {ECO:0000250|UniProtKB:O00746}. SUBUNIT: Homohexamer (By similarity). Interacts with OPA1 (By similarity). Interacts with CAPN8 (PubMed:16476741). {ECO:0000250|UniProtKB:O00746, ECO:0000269|PubMed:16476741}. TISSUE SPECIFICITY: Expressed in the base region of the oxyntic and pyloric mucosae. {ECO:0000269|PubMed:16476741}. +Q8C5D8 PIAS2_MOUSE E3 SUMO-protein ligase PIAS2 (EC 2.3.2.27) (Androgen receptor-interacting protein 3) (ARIP3) (DAB2-interacting protein) (DIP) (Msx-interacting zinc finger protein) (Protein inhibitor of activated STAT x) (Protein inhibitor of activated STAT2) (RING-type E3 ubiquitin transferase PIAS2) 621 68,426 Alternative sequence (5); Chain (1); Compositional bias (2); Cross-link (8); Domain (2); Erroneous initiation (1); Frameshift (1); Modified residue (4); Motif (2); Region (1); Sequence conflict (17); Zinc finger (1) Protein modification; protein sumoylation. FUNCTION: Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor. Plays a crucial role as a transcriptional coregulation in various cellular pathways, including the STAT pathway, the p53 pathway and the steroid hormone signaling pathway. The effects of this transcriptional coregulation, transactivation or silencing may vary depending upon the biological context and PIAS2 isoform studied. However, it seems to be mostly involved in gene silencing. Binds to sumoylated ELK1 and enhances its transcriptional activity by preventing recruitment of HDAC2 by ELK1, thus reversing SUMO-mediated repression of ELK1 transactivation activity. Isoform PIASx-beta, but not isoform PIASx-alpha, promotes MDM2 sumoylation. Isoform PIASx-alpha promotes PARK7 sumoylation. Isoform PIASx-beta promotes NCOA2 sumoylation more efficiently than isoform PIASx-alpha (By similarity). Sumoylates PML at'Lys-65' and 'Lys-160' (By similarity). {ECO:0000250}. PTM: Sumoylated. {ECO:0000269|PubMed:12077349}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:12077349}. Nucleus, PML body {ECO:0000250|UniProtKB:O75928}. Nucleus {ECO:0000269|PubMed:12193603}. Note=Colocalizes at least partially with promyelocytic leukemia nuclear bodies (PML NBs) (By similarity). Colocalizes with SUMO1 in nuclear granules (PubMed:12077349). {ECO:0000250|UniProtKB:O75928, ECO:0000269|PubMed:12077349}. SUBUNIT: Binds SUMO1 and UBE2I. Interacts with AXIN1, JUN, MDM2, PARK7, TP53 and TP73 isoform alpha, but not TP73 isoform beta. Interacts with STAT4 following IL12 and IFN-alpha stimulation of T-cells. Interacts also with GTF2I, GTF2IRD1, IKFZ1, DAB2 and MSX2, as well as with several steroid receptors, including ESR1, ESR2, NR3C1, PGR, AR, and with NCOA2. Sumoylation of a target protein seems to enhance the interaction. Binds to sumoylated ELK1. Interacts with PLAG1 (By similarity). Binds DNA, such as CDKN1A promoter, in a sequence-specific manner. Interacts with KLF8; the interaction results in SUMO ligation and repression of KLF8 transcriptional activity and of its cell cycle progression into G(1) phase (By similarity). Interacts with IFIH1/MDA5 (By similarity). Interacts with PML (By similarity). {ECO:0000250}. DOMAIN: The LXXLL motif is a transcriptional coregulator signature. +Q9JJI6 PIGO_MOUSE GPI ethanolamine phosphate transferase 3 (EC 2.-.-.-) (Phosphatidylinositol-glycan biosynthesis class O protein) (PIG-O) 1093 119,156 Chain (1); Erroneous initiation (1); Glycosylation (1); Sequence conflict (1); Transmembrane (12) TRANSMEM 4 24 Helical. {ECO:0000255}.; TRANSMEM 460 480 Helical. {ECO:0000255}.; TRANSMEM 483 503 Helical. {ECO:0000255}.; TRANSMEM 512 532 Helical. {ECO:0000255}.; TRANSMEM 669 689 Helical. {ECO:0000255}.; TRANSMEM 702 722 Helical. {ECO:0000255}.; TRANSMEM 748 768 Helical. {ECO:0000255}.; TRANSMEM 831 851 Helical. {ECO:0000255}.; TRANSMEM 856 876 Helical. {ECO:0000255}.; TRANSMEM 945 965 Helical. {ECO:0000255}.; TRANSMEM 1018 1038 Helical. {ECO:0000255}.; TRANSMEM 1052 1072 Helical. {ECO:0000255}. Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis. FUNCTION: Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the GPI third mannose which links the GPI-anchor to the C-terminus of the proteins by an amide bond. {ECO:0000269|PubMed:10781593}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10781593}; Multi-pass membrane protein {ECO:0000269|PubMed:10781593}. SUBUNIT: Forms a complex with PIGF. PIGF is required to stabilize PIGO. {ECO:0000269|PubMed:10781593}. +Q9QYG0 NDRG2_MOUSE Protein NDRG2 (N-myc downstream-regulated gene 2 protein) (Protein Ndr2) 371 40,789 Alternative sequence (1); Beta strand (9); Chain (1); Helix (15); Initiator methionine (1); Modified residue (17); Sequence conflict (2); Turn (1) FUNCTION: Contributes to the regulation of the Wnt signaling pathway. Down-regulates CTNNB1-mediated transcriptional activation of target genes, such as CCND1, and may thereby act as tumor suppressor. May be involved in dendritic cell and neuron differentiation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14985363, ECO:0000269|PubMed:16520977}. Cytoplasm, perinuclear region {ECO:0000250}. Cell projection, growth cone {ECO:0000250}. Note=In neurons, seems to concentrate at axonal growth cone. Perinuclear in neurons (By similarity). {ECO:0000250}. SUBUNIT: Interacts with CTNNB1. {ECO:0000250}. TISSUE SPECIFICITY: Expressed at highest levels in brain, heart and liver, and at lower levels in kidney, colon, skeletal muscle, adrenal gland, ovary and uterus (at protein level). {ECO:0000269|PubMed:15461589, ECO:0000269|PubMed:16520977, ECO:0000269|PubMed:21636852}. +Q8K358 PIGU_MOUSE Phosphatidylinositol glycan anchor biosynthesis class U protein (Cell division cycle protein 91-like 1) (Protein CDC91-like 1) (GPI transamidase component PIG-U) 434 49,804 Chain (1); Erroneous initiation (1); Region (1); Transmembrane (9) TRANSMEM 66 86 Helical. {ECO:0000255}.; TRANSMEM 165 185 Helical. {ECO:0000255}.; TRANSMEM 187 207 Helical. {ECO:0000255}.; TRANSMEM 236 256 Helical. {ECO:0000255}.; TRANSMEM 258 278 Helical. {ECO:0000255}.; TRANSMEM 285 305 Helical. {ECO:0000255}.; TRANSMEM 312 332 Helical. {ECO:0000255}.; TRANSMEM 354 374 Helical. {ECO:0000255}.; TRANSMEM 385 405 Helical. {ECO:0000255}. Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis. FUNCTION: Component of the GPI transamidase complex. May be involved in the recognition of either the GPI attachment signal or the lipid portion of GPI (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Forms a complex with PIGK/GPI8, PIGS, PIGT and GPAA1/GAA1. {ECO:0000250}. +Q9D6J5 NDUB8_MOUSE NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial (Complex I-ASHI) (CI-ASHI) (NADH-ubiquinone oxidoreductase ASHI subunit) 186 21,876 Beta strand (5); Chain (1); Helix (4); Sequence conflict (1); Transit peptide (1); Transmembrane (1); Turn (3) TRANSMEM 133 153 Helical. {ECO:0000255}. FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. {ECO:0000250|UniProtKB:O95169}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:O95169}; Single-pass membrane protein {ECO:0000255}; Matrix side {ECO:0000250|UniProtKB:O95169}. SUBUNIT: Complex I is composed of 45 different subunits. {ECO:0000250|UniProtKB:O95169}. +Q9CQZ5 NDUA6_MOUSE NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6 (Complex I-B14) (CI-B14) (NADH-ubiquinone oxidoreductase B14 subunit) 131 15,283 Chain (1); Helix (7); Turn (2) FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed to be not involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. {ECO:0000250|UniProtKB:P56556}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P56556}; Peripheral membrane protein {ECO:0000250|UniProtKB:P56556}; Matrix side {ECO:0000250|UniProtKB:P56556}. SUBUNIT: Mammalian complex I is composed of 45 different subunits. {ECO:0000250|UniProtKB:P56556}. +Q8C398 PIGW_MOUSE Phosphatidylinositol-glycan biosynthesis class W protein (PIG-W) (EC 2.3.-.-) 503 56,841 Chain (1); Frameshift (1); Glycosylation (1); Modified residue (1); Topological domain (1); Transmembrane (12) TRANSMEM 22 42 Helical. {ECO:0000255}.; TRANSMEM 61 81 Helical. {ECO:0000255}.; TRANSMEM 132 152 Helical. {ECO:0000255}.; TRANSMEM 161 181 Helical. {ECO:0000255}.; TRANSMEM 202 222 Helical. {ECO:0000255}.; TRANSMEM 237 257 Helical. {ECO:0000255}.; TRANSMEM 260 280 Helical. {ECO:0000255}.; TRANSMEM 305 325 Helical. {ECO:0000255}.; TRANSMEM 340 360 Helical. {ECO:0000255}.; TRANSMEM 381 401 Helical. {ECO:0000255}.; TRANSMEM 448 468 Helical. {ECO:0000255}.; TRANSMEM 473 493 Helical. {ECO:0000255}. TOPO_DOM 1 21 Lumenal. {ECO:0000255}. Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis. FUNCTION: Required for the transport of GPI-anchored proteins to the plasma membrane. Probable acetyltransferase, which acetylates the inositol ring of phosphatidylinositol during biosynthesis of GPI-anchor. Acetylation during GPI-anchor biosynthesis is not essential for the subsequent mannosylation and is usually removed soon after the attachment of GPIs to proteins. {ECO:0000250|UniProtKB:Q7TSN4}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q7TSN4}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q7TSN4}. +P52850 NDST2_MOUSE Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 2 (EC 2.8.2.8) (Glucosaminyl N-deacetylase/N-sulfotransferase 2) (NDST-2) (Mndns) (N-heparan sulfate sulfotransferase 2) (N-HSST 2) [Includes: Heparan sulfate N-deacetylase 2 (EC 3.-.-.-); Heparan sulfate N-sulfotransferase 2 (EC 2.8.2.-)] 883 101,202 Active site (1); Binding site (1); Chain (1); Disulfide bond (1); Glycosylation (6); Nucleotide binding (2); Region (2); Sequence conflict (3); Topological domain (2); Transmembrane (1) TRANSMEM 19 39 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 18 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 40 883 Lumenal. {ECO:0000255}. Glycan metabolism; heparan sulfate biosynthesis. Glycan metabolism; heparin biosynthesis. FUNCTION: Essential bifunctional enzyme that catalyzes both the N-deacetylation and the N-sulfation of glucosamine (GlcNAc) of the glycosaminoglycan in heparan sulfate. Modifies the GlcNAc-GlcA disaccharide repeating sugar backbone to make N-sulfated heparosan, a prerequisite substrate for later modifications in heparin biosynthesis. Plays a role in determining the extent and pattern of sulfation of heparan sulfate. Required for the exosomal release of SDCBP, CD63 and syndecan (By similarity). {ECO:0000250|UniProtKB:P52849, ECO:0000269|PubMed:10466726, ECO:0000269|PubMed:10466727}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed in adult and throughout development. +Q3UIU2 NDUB6_MOUSE NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6 (Complex I-B17) (CI-B17) (NADH-ubiquinone oxidoreductase B17 subunit) 128 15,515 Beta strand (1); Chain (1); Helix (4); Initiator methionine (1); Modified residue (2); Transmembrane (1); Turn (4) TRANSMEM 64 86 Helical. {ECO:0000255}. FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. {ECO:0000250|UniProtKB:O95139}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:O95139}; Single-pass membrane protein {ECO:0000255}; Matrix side {ECO:0000250|UniProtKB:O95139}. SUBUNIT: Complex I is composed of 45 different subunits. {ECO:0000250|UniProtKB:O95139}. +Q9CQY9 NDUC1_MOUSE NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial (Complex I-KFYI) (CI-KFYI) (NADH-ubiquinone oxidoreductase KFYI subunit) 76 8,625 Chain (1); Helix (1); Transit peptide (1); Transmembrane (1) TRANSMEM 40 59 Helical. {ECO:0000255}. FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. {ECO:0000250|UniProtKB:O43677}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q02376}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q02376}; Matrix side {ECO:0000250|UniProtKB:Q02376}. SUBUNIT: Complex I is composed of 45 different subunits. {ECO:0000250|UniProtKB:O43677}. +Q59J78 NDUF2_MOUSE NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 2 (Mimitin) (Myc-induced mitochondrial protein) (MMTN) (NDUFA12-like protein) 168 19,628 Chain (1); Frameshift (1); Modified residue (1); Transit peptide (1) FUNCTION: Acts as a molecular chaperone for mitochondrial complex I assembly. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. {ECO:0000250|UniProtKB:Q8N183}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q8N183}. +P21661 NEC2_MOUSE Neuroendocrine convertase 2 (NEC 2) (EC 3.4.21.94) (KEX2-like endoprotease 2) (Prohormone convertase 2) (Proprotein convertase 2) (PC2) 637 70,785 Active site (3); Chain (1); Disulfide bond (3); Domain (2); Glycosylation (3); Propeptide (1); Signal peptide (1) FUNCTION: Involved in the processing of hormone and other protein precursors at sites comprised of pairs of basic amino acid residues. Responsible for the release of glucagon from proglucagon in pancreatic A cells (By similarity). {ECO:0000250|UniProtKB:P16519}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniProtKB:P16519}. Secreted {ECO:0000250|UniProtKB:P16519}. Note=Localized in the secretion granules. {ECO:0000250|UniProtKB:P16519}. +Q9CQ45 NENF_MOUSE Neudesin (Neuron-derived neurotrophic factor) (Secreted protein of unknown function) (SPUF protein) 171 18,904 Chain (1); Domain (1); Modified residue (1); Mutagenesis (1); Signal peptide (1) FUNCTION: Acts as a neurotrophic factor in postnatal mature neurons, enhancing neuronal survival (PubMed:15605373). Promotes cell proliferation and neurogenesis in undifferentiated neural pro-genitor cells at the embryonic stage and inhibits differentiation of astrocyte (PubMed:16547973). Its neurotrophic activity is exerted via MAPK1/ERK2, MAPK3/ERK1 and AKT1/AKT pathways (PubMed:15605373, PubMed:16547973). Neurotrophic activity is enhanced by binding to heme (PubMed:18056703). Acts also as an anorexigenic neurotrophic factor that contributes to energy balance (PubMed:23576617). {ECO:0000269|PubMed:15605373, ECO:0000269|PubMed:16547973, ECO:0000269|PubMed:18056703, ECO:0000269|PubMed:23576617}. SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000269|PubMed:15605373}. DOMAIN: The cytochrome b5 heme-binding domain was proven to bind heme, although it lacks the conserved iron-binding His residue at position 81. TISSUE SPECIFICITY: In the embryo, expressed most abundantly in brain and spinal cord. Widely expressed in adult tissues including brain, heart, lung and kidney. In brain, expressed in neurons but not in glial cells (PubMed:15605373). In the hypothalamus is expressed primarily in the paraventricular nucleus (PVN), with lower levels of expression in the arcuate nucleus (ARC)(PubMed:23576617). {ECO:0000269|PubMed:15605373, ECO:0000269|PubMed:23576617}. +Q8BK30 NDUV3_MOUSE NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial (Complex I-9kD) (CI-9kD) (NADH-ubiquinone oxidoreductase 9 kDa subunit) 104 11,813 Beta strand (1); Chain (1); Helix (2); Modified residue (1); Transit peptide (1) FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. May be the terminally assembled subunit of Complex I. {ECO:0000250|UniProtKB:P56181}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P56181}; Peripheral membrane protein {ECO:0000250|UniProtKB:P56181}; Matrix side {ECO:0000250|UniProtKB:P56181}. SUBUNIT: Complex I is composed of 45 different subunits. This is a component of the flavoprotein-sulfur (FP) fragment of the enzyme. {ECO:0000250|UniProtKB:P56181}. +Q9D6N5 NC2A_MOUSE Dr1-associated corepressor (Dr1-associated protein 1) (Negative cofactor 2-alpha) (NC2-alpha) 205 22,278 Chain (1); Compositional bias (2); Domain (1) FUNCTION: The association of the DR1/DRAP1 heterodimer with TBP results in a functional repression of both activated and basal transcription of class II genes. This interaction precludes the formation of a transcription-competent complex by inhibiting the association of TFIIA and/or TFIIB with TBP. Can bind to DNA on its own (By similarity). {ECO:0000250}. PTM: Phosphorylation reduces DNA binding, but has no effect on heterodimerization and TBP binding. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Heterodimer with DR1. Binds BTAF1 (By similarity). {ECO:0000250}. +Q99M51 NCK1_MOUSE Cytoplasmic protein NCK1 (NCK adaptor protein 1) (Nck-1) 377 42,891 Chain (1); Domain (4); Initiator methionine (1); Modified residue (6); Sequence conflict (10) FUNCTION: Adapter protein which associates with tyrosine-phosphorylated growth factor receptors, such as KDR and PDGFRB, or their cellular substrates. Maintains low levels of EIF2S1 phosphorylation by promoting its dephosphorylation by PP1. Plays a role in the DNA damage response, not in the detection of the damage by ATM/ATR, but for efficient activation of downstream effectors, such as that of CHEK2. Plays a role in ELK1-dependent transcriptional activation in response to activated Ras signaling. Modulates the activation of EIF2AK2/PKR by dsRNA (By similarity). {ECO:0000250}. PTM: Phosphorylated on Ser and Tyr residues. Phosphorylated in response to activation of EGFR and FcERI. Phosphorylated by activated PDGFRB (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Nucleus {ECO:0000250}. Note=Mostly cytoplasmic, but shuttles between the cytoplasm and the nucleus. Import into the nucleus requires interaction with SOCS7. Predominantly nuclear following genotoxic stresses, such as UV irradiation, hydroxyurea or mitomycin C treatments (By similarity). {ECO:0000250}. SUBUNIT: Associates with BLNK, PLCG1, VAV1 and NCK1 in a B-cell antigen receptor-dependent fashion. Interacts with SOCS7. This interaction is required for nuclear import. Part of a complex containing PPP1R15B, PP1 and NCK1. Interacts with RALGPS1. Interacts with CAV2 (tyrosine phosphorylated form). Interacts with ADAM15. Interacts with FASLG. Directly interacts with RASA1. Interacts with MINK1. Interacts with KDR (tyrosine phosphorylated). Interacts (via SH2 domain) with EPHB1; activates the JUN cascade to regulate cell adhesion. Interacts with EPHA2. Interacts (via SH2 domain) with PDGFRB (tyrosine phosphorylated). Interacts (via SH2 domain and SH3 domain 2) with EGFR. Interacts with PAK1 and SOS1. Interacts (via SH3 domains) with PKN2 (By similarity). Interacts with FLT1 (tyrosine phosphorylated). Interacts with the inactive form of EIF2AK2/PKR (By similarity). {ECO:0000250}. DOMAIN: Only the first and third SH3 domains seem to be involved in RASA1-binding; the second SH3 domain and the SH2 domains do not seem to be involved. {ECO:0000250}. +Q9R207 NBN_MOUSE Nibrin (Cell cycle regulatory protein p95) (Nijmegen breakage syndrome protein 1 homolog) 751 83,795 Chain (1); Compositional bias (1); Cross-link (2); Domain (2); Modified residue (6); Motif (2); Region (2); Sequence conflict (9) FUNCTION: Component of the MRE11-RAD50-NBN (MRN complex) which plays a critical role in the cellular response to DNA damage and the maintenance of chromosome integrity. The complex is involved in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity, cell cycle checkpoint control and meiosis. The complex possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by MRE11. RAD50 may be required to bind DNA ends and hold them in close proximity. NBN modulate the DNA damage signal sensing by recruiting PI3/PI4-kinase family members ATM, ATR, and probably DNA-PKcs to the DNA damage sites and activating their functions. It can also recruit MRE11 and RAD50 to the proximity of DSBs by an interaction with the histone H2AX. NBN also functions in telomere length maintenance by generating the 3' overhang which serves as a primer for telomerase dependent telomere elongation. NBN is a major player in the control of intra-S-phase checkpoint and there is some evidence that NBN is involved in G1 and G2 checkpoints. The roles of NBS1/MRN encompass DNA damage sensor, signal transducer, and effector, which enable cells to maintain DNA integrity and genomic stability. Forms a complex with RBBP8 to link DNA double-strand break sensing to resection. Enhances AKT1 phosphorylation possibly by association with the mTORC2 complex (By similarity). {ECO:0000250}. PTM: Phosphorylated by ATM in response of ionizing radiation, and such phosphorylation is responsible intra-S phase checkpoint control and telomere maintenance. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O60934}. Nucleus, PML body {ECO:0000250|UniProtKB:O60934}. Chromosome, telomere {ECO:0000250|UniProtKB:O60934}. Chromosome {ECO:0000250|UniProtKB:O60934}. Note=Localizes to discrete nuclear foci after treatment with genotoxic agents. {ECO:0000250|UniProtKB:O60934}. SUBUNIT: Component of the MRN complex composed of two heterodimers RAD50/MRE11 associated with a single NBN (By similarity). As part of the MRN complex, interacts with MCM9; the interaction recruits the complex to DNA repair sites (By similarity). Component of the BASC complex, at least composed of BRCA1, MSH2, MSH6, MLH1, ATM, BLM, RAD50, MRE11 and NBN (By similarity). Interacts with histone H2AFX this requires phosphorylation of H2AFX on 'Ser-139' (By similarity). Interacts with HJURP, INTS3, KPNA2 and TERF2 (By similarity). Interacts with RBBP8; the interaction links the role of the MRN complex in DNA double-strand break sensing to resection (By similarity). Interacts with SP100; recruits NBN to PML bodies (PubMed:12470659). Interacts with ATF2 (By similarity). Interacts with MTOR, MAPKAP1 isoform 2 and RICTOR; indicative for an association with the mTORC2 complex (By similarity). Interacts with MRNIP (By similarity). {ECO:0000250|UniProtKB:O60934, ECO:0000269|PubMed:12470659}. DOMAIN: The FHA and BRCT domains are likely to have a crucial role for both binding to histone H2AFX and for relocalization of MRE11/RAD50 complex to the vicinity of DNA damage. {ECO:0000250}.; DOMAIN: The C-terminal domain contains a MRE11-binding site, and this interaction is required for the nuclear localization of the MRN complex. {ECO:0000250}.; DOMAIN: The EEXXXDDL motif at the C-terminus is required for the interaction with ATM and its recruitment to sites of DNA damage and promote the phosphorylation of ATM substrates, leading to the events of DNA damage response. {ECO:0000250}. TISSUE SPECIFICITY: High expression in the liver, heart and testis. Low expression in all other tissues analyzed. In the cerebellum the postmitotic Purkinje cells are marked specifically. {ECO:0000269|PubMed:10915761}. +Q9JL19 NCOA6_MOUSE Nuclear receptor coactivator 6 (Activating signal cointegrator 2) (ASC-2) (Amplified in breast cancer protein 3) (Cancer-amplified transcriptional coactivator ASC-2) (Nuclear receptor coactivator RAP250) (NRC) (Nuclear receptor-activating protein, 250 kDa) (Peroxisome proliferator-activated receptor-interacting protein) (PPAR-interacting protein) (Thyroid hormone receptor-binding protein) 2067 219,663 Alternative sequence (1); Chain (1); Compositional bias (4); Modified residue (8); Motif (2); Mutagenesis (1); Region (5); Sequence conflict (6) FUNCTION: Nuclear receptor coactivator that directly binds nuclear receptors and stimulates the transcriptional activities in a hormone-dependent fashion. Coactivates expression in an agonist- and AF2-dependent manner. Involved in the coactivation of different nuclear receptors, such as for steroids (GR and ERs), retinoids (RARs and RXRs), thyroid hormone (TRs), vitamin D3 (VDR) and prostanoids (PPARs). Probably functions as a general coactivator, rather than just a nuclear receptor coactivator. May also be involved in the coactivation of the NF-kappa-B pathway. May coactivate expression via a remodeling of chromatin and its interaction with histone acetyltransferase proteins. Involved in placental, cardiac, hepatic and embryonic development. PTM: Phosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Monomer and homodimer. Interacts in vitro with the basal transcription factors GTF2A and TBP, suggesting an autonomous transactivation function. Interacts with NCOA1, CRSP3, RBM14, the histone acetyltransferase proteins EP300 and CREBBP, and with methyltransferase proteins NCOA6IP and PRMT2 (By similarity). Interacts with RBM39. Component of the MLL2/3 complex (also named ASCOM complex), at least composed of KMT2D/MLL2 or KMT2C/MLL3, ASH2L, RBBP5, WDR5, NCOA6, DPY30, KDM6A, PAXIP1/PTIP, PAGR1 and alpha- and beta-tubulin (By similarity). Interacts with ZNF335; may enhance ligand-dependent transcriptional activation by nuclear hormone receptors (By similarity). {ECO:0000250}. DOMAIN: Contains two Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs. Only motif 1 is essential for the association with nuclear receptors. TISSUE SPECIFICITY: Widely expressed. High expression in testis and weak expression in small intestine. +Q6DFV7 NCOA7_MOUSE Nuclear receptor coactivator 7 943 106,357 Alternative sequence (9); Chain (1); Coiled coil (1); Domain (2); Frameshift (1); Modified residue (11) FUNCTION: Enhances the transcriptional activities of several nuclear receptors. Involved in the coactivation of different nuclear receptors, such as ESR1, THRB, PPARG and RARA (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with ESR1, ESR2A, ESR2B, THRB, PPARG and RARA in a ligand-inducible manner. Interacts with the heterodimer AHR-ARNT (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in brain and kidney. Weakly expressed in mammary gland, lung and testis. In brain, expression is found in neurons of cerebral cortex, thalamus, hypothalamus, hippocampus, cerebellum, striatum and choroid plexus. {ECO:0000269|PubMed:11971969}. +O09105 NDF4_MOUSE Neurogenic differentiation factor 4 (NeuroD4) (Helix-loop-helix protein mATH-3) (mATH3) (Protein atonal homolog 3) 330 37,133 Chain (1); Compositional bias (1); Domain (1) FUNCTION: Probably acts as a transcriptional activator. Mediates neuronal differentiation. Required for the regulation of amacrine cell fate specification in the retina. {ECO:0000269|PubMed:11861467}. PTM: Serine or threonine phosphorylation within the basic region may regulate neurogenic activity. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}. SUBUNIT: Efficient DNA binding requires dimerization with another bHLH protein. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in retinal interneurons amacrine cells (at protein level). Expressed in neurons of ventricular zone of the retina at postnatal day 1 (P1). Expressed transiently in amacrine and horizontal cells of the inner nuclear layer (INL) of the retina at P7 until P14. {ECO:0000269|PubMed:11861467, ECO:0000269|PubMed:9029157, ECO:0000269|PubMed:9497361}. +Q6U7H8 PI5L1_MOUSE Phosphatidylinositol 4-phosphate 5-kinase-like protein 1 (PI(4)P 5-kinase-like protein 1) (PtdIns(4)P-5-kinase-like protein 1) (EC 2.7.1.68) (Phosphatidylinositol phosphate kinase homolog) (PIPKH) 395 45,293 Alternative sequence (5); Chain (1); Domain (1); Mutagenesis (2); Sequence conflict (2) FUNCTION: May act as a scaffold to localize and regulate type I PI(4)P 5-kinases to specific compartments within the cell, where they generate PI(4,5)P2 for actin nucleation, signaling and scaffold protein recruitment and conversion to PI(3,4,5)P3. {ECO:0000269|PubMed:14701839}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14701839}. Membrane {ECO:0000269|PubMed:14701839}. Note=Localized to large cytoplasmic vesicular structures. SUBUNIT: Heterodimerizes with other type I phosphatidylinositol 4-phosphate 5-kinase. TISSUE SPECIFICITY: Highly expressed in brain and testis, relatively to heart, spleen, lung, liver, skeletal muscle and kidney. {ECO:0000269|PubMed:14701839}. +Q62083 PICK1_MOUSE PRKCA-binding protein (Protein interacting with C kinase 1) (Protein kinase C-alpha-binding protein) 416 46,597 Chain (1); Compositional bias (1); Domain (2); Lipidation (1); Metal binding (2); Modified residue (1); Mutagenesis (3); Sequence conflict (3) FUNCTION: Probable adapter protein that bind to and organize the subcellular localization of a variety of membrane proteins containing some PDZ recognition sequence. Involved in the clustering of various receptors, possibly by acting at the receptor internalization level. Plays a role in synaptic plasticity by regulating the trafficking and internalization of AMPA receptors. May be regulated upon PRKCA activation. May regulate ASIC1/ASIC3 channel. Regulates actin polymerization by inhibiting the actin-nucleating activity of the Arp2/3 complex; the function is competetive with nucleation promoting factors and is linked to neuronal morphology regulation and AMPA receptor (AMPAR) endocytosis. Via interaction with the Arp2/3 complex involved in regulation of synaptic plasicity of excitatory synapses and required for spine shrinkage during long-term depression (LTD). Involved in regulation of astrocyte morphology, antagonistic to Arp2/3 complex activator WASL/N-WASP function. {ECO:0000269|PubMed:14976185, ECO:0000269|PubMed:20445062}. PTM: Phosphorylation at Thr-82 appears to inhibit the interaction with AMPA receptors (By similarity). Phosphorylated on tyrosine residues by EPHB2 and on serine or threonine residues by PKC. {ECO:0000250, ECO:0000269|PubMed:7844141, ECO:0000269|PubMed:9883737}.; PTM: Palmitoylation on Cys-414 is essential for long-term synaptic depression (LTD). {ECO:0000269|PubMed:24068808}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Membrane {ECO:0000269|PubMed:24068808}; Lipid-anchor {ECO:0000269|PubMed:24068808}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250}. Cell junction, synapse, synaptosome {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Also membrane-associated, present at excitatory synapses. {ECO:0000250}. SUBUNIT: Monomer and homodimer. Interacts with CXADR. Interacts presynaptically with the glutamate receptors GRIA2, GRIA3, GRIK3, isoform 3 of GRIA4, isoform A of GRM4, GRM7 and GRM8; with NAPA and NAPB; and with BTG2. The interaction with NAPA and NAPB disrupts the interaction with GRIA2, conducting to the internalization of GRIA2. Interacts with PRKCA; with the amine transporters SLC6A2 and SLC6A3; with the channels ASIC1 and ASIC2; with the GTP-binding proteins ARF1 and ARF3; with the ephrin receptor tyrosine kinases EPHA7, EPHB1 and EPHB2; with ERBB2 and through its PDZ domain with the C-terminal tail of PRLHR. Interacts with UNC5A. Interacts (via AH domain) with NCS1/FREQ; in a calcium-dependent manner. Interacts with F-actin and associates with the ARP2/3 complex. Interacts (via PDZ domain) with ARF1 (activated); the interaction blocks Arp2/3 complex inhibition. {ECO:0000269|PubMed:10340301, ECO:0000269|PubMed:11278603, ECO:0000269|PubMed:12065412, ECO:0000269|PubMed:7844141, ECO:0000269|PubMed:9883737}. DOMAIN: The AH domain mediates binding to F-actin. {ECO:0000250}.; DOMAIN: The unoccupied PDZ domain is probably involved in allosteric modulation by forming an intramolecular bridge with the AH domain leading to a 'closed' formation. Binding of a PDZ ligand, such as GRIA2, allows enhanced interactions with F-actin and the Arp2/3 complex thus enhanced inhibition of actin polymerization (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in all tissues examined, with highest levels in brain and testes and lowest levels in lung. +E2JF22 PIEZ1_MOUSE Piezo-type mechanosensitive ion channel component 1 (Protein FAM38A) 2547 292,002 Beta strand (12); Chain (1); Coiled coil (1); Compositional bias (2); Disulfide bond (1); Glycosylation (2); Helix (7); Modified residue (6); Topological domain (1); Transmembrane (35); Turn (1) TRANSMEM 5 25 Helical. {ECO:0000255}.; TRANSMEM 27 47 Helical. {ECO:0000255}.; TRANSMEM 62 82 Helical. {ECO:0000255}.; TRANSMEM 120 140 Helical. {ECO:0000255}.; TRANSMEM 217 237 Helical. {ECO:0000255}.; TRANSMEM 250 270 Helical. {ECO:0000255}.; TRANSMEM 317 337 Helical. {ECO:0000255}.; TRANSMEM 435 455 Helical. {ECO:0000255}.; TRANSMEM 467 487 Helical. {ECO:0000255}.; TRANSMEM 520 540 Helical. {ECO:0000255}.; TRANSMEM 577 597 Helical. {ECO:0000255}.; TRANSMEM 608 628 Helical. {ECO:0000255}.; TRANSMEM 635 655 Helical. {ECO:0000255}.; TRANSMEM 687 707 Helical. {ECO:0000255}.; TRANSMEM 818 838 Helical. {ECO:0000255}.; TRANSMEM 847 867 Helical. {ECO:0000255}.; TRANSMEM 921 941 Helical. {ECO:0000255}.; TRANSMEM 982 1002 Helical. {ECO:0000255}.; TRANSMEM 1006 1023 Helical. {ECO:0000255}.; TRANSMEM 1038 1058 Helical. {ECO:0000255}.; TRANSMEM 1155 1175 Helical. {ECO:0000255}.; TRANSMEM 1179 1199 Helical. {ECO:0000255}.; TRANSMEM 1207 1227 Helical. {ECO:0000255}.; TRANSMEM 1232 1252 Helical. {ECO:0000255}.; TRANSMEM 1272 1292 Helical. {ECO:0000255}.; TRANSMEM 1678 1698 Helical. {ECO:0000255}.; TRANSMEM 1700 1720 Helical. {ECO:0000255}.; TRANSMEM 1734 1754 Helical. {ECO:0000255}.; TRANSMEM 1978 1998 Helical. {ECO:0000255}.; TRANSMEM 2019 2039 Helical. {ECO:0000255}.; TRANSMEM 2048 2068 Helical. {ECO:0000255}.; TRANSMEM 2077 2097 Helical. {ECO:0000255}.; TRANSMEM 2145 2165 Helical. {ECO:0000255}.; TRANSMEM 2193 2213 Helical. {ECO:0000255}.; TRANSMEM 2458 2478 Helical. {ECO:0000255}. TOPO_DOM 2214 2457 Extracellular. {ECO:0000269|PubMed:26390154}. FUNCTION: Pore-forming subunit of a mechanosensitive non-specific cation channel. Generates currents characterized by a linear current-voltage relationship that are sensitive to ruthenium red and gadolinium. Plays a key role in epithelial cell adhesion by maintaining integrin activation through R-Ras recruitment to the ER, most probably in its activated state, and subsequent stimulation of calpain signaling. In the kidney, may contribute to the detection of intraluminal pressure changes and to urine flow sensing. Acts as shear-stress sensor that promotes endothelial cell organization and alignment in the direction of blood flow through calpain activation. Plays a key role in blood vessel formation and vascular structure in both development and adult physiology. {ECO:0000269|PubMed:20813920, ECO:0000269|PubMed:22343900, ECO:0000269|PubMed:24157948, ECO:0000269|PubMed:24958852, ECO:0000269|PubMed:25119035}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q92508}; Multi-pass membrane protein. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q0KL00}. Cell membrane {ECO:0000269|PubMed:20813920, ECO:0000269|PubMed:26390154}; Multi-pass membrane protein {ECO:0000269|PubMed:26390154}. Cell projection, lamellipodium membrane {ECO:0000250|UniProtKB:Q92508}. Note=In erythrocytes, located in the plasma membrane (PubMed:23479567). Accumulates at the leading apical lamellipodia of endothelial cells in response to shear stress (By similarity). {ECO:0000250|UniProtKB:Q92508, ECO:0000269|PubMed:23479567}. SUBUNIT: Homotrimer (PubMed:26390154). Interacts with PKD2 (PubMed:24157948). Interacts with STOML3 (PubMed:24662763). {ECO:0000269|PubMed:22343900, ECO:0000269|PubMed:24157948, ECO:0000269|PubMed:24662763, ECO:0000269|PubMed:26390154}. TISSUE SPECIFICITY: Expressed in bladder, colon, kidney and skin. Also expressed in bone marrow, liver, lung, spleen and erythrocytes (at protein level). {ECO:0000269|PubMed:20813920, ECO:0000269|PubMed:23479567, ECO:0000269|PubMed:24958852}. +P19426 NELFE_MOUSE Negative elongation factor E (NELF-E) (RNA-binding protein RD) 375 42,554 Alternative sequence (1); Chain (1); Coiled coil (1); Cross-link (3); Domain (1); Modified residue (14); Natural variant (2); Region (1); Repeat (32); Sequence conflict (1) FUNCTION: Essential component of the NELF complex, a complex that negatively regulates the elongation of transcription by RNA polymerase II (By similarity). The NELF complex, which acts via an association with the DSIF complex and causes transcriptional pausing, is counteracted by the P-TEFb kinase complex (By similarity). Provides the strongest RNA binding activity of the NELF complex and may initially recruit the NELF complex to RNA (By similarity). {ECO:0000250|UniProtKB:P18615}. PTM: Sumoylated. {ECO:0000250|UniProtKB:P18615}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P18615}. SUBUNIT: The NELF complex is composed of NELFA, NELFB, NELFCD and NELFE (By similarity). Interacts with NELFB (PubMed:26010750). {ECO:0000250|UniProtKB:P18615, ECO:0000269|PubMed:26010750}. DOMAIN: The RRM domain interacts with RNA, and is essential for NELF complex function. It is however not required for the NELF complex formation (By similarity). {ECO:0000250|UniProtKB:P18615}. +Q91ZP9 NECA2_MOUSE N-terminal EF-hand calcium-binding protein 2 (EF-hand calcium-binding protein 2) (Neuronal calcium-binding protein 2) 389 43,441 Alternative sequence (1); Calcium binding (2); Chain (1); Coiled coil (1); Domain (3); Erroneous initiation (1); Modified residue (2) FUNCTION: May act as a signaling scaffold protein that senses intracellular calcium. Can modulate ligand-induced internalization of ADORA2A and coupling efficiency of mGluR5/GRM5; for both receptors may regulate signaling activity such as promoting MAPK1/3 (ERK1/2) activation. {ECO:0000250|UniProtKB:Q7Z6G3}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11641222}. Cell projection, dendrite {ECO:0000250|UniProtKB:F1LQY6}. Cell projection, axon {ECO:0000250|UniProtKB:F1LQY6}. Cell membrane {ECO:0000250|UniProtKB:Q7Z6G3}. Note=Colocalizes with ADORA2A and/or mGluR5/GRM5 at the plasma membrane (By similarity). Found in neuronal somata (PubMed:26843217). Detected in the cytoplasm of striatal neurons, at postsynaptic sites, filling dendritic shafts and spines, and at presynaptic sites, filling axon terminals (By similarity). {ECO:0000250|UniProtKB:F1LQY6, ECO:0000250|UniProtKB:Q7Z6G3, ECO:0000269|PubMed:26843217}. SUBUNIT: Interacts (calcium-dependent) with ADORA2A and GRM5. {ECO:0000250|UniProtKB:F1LQY6, ECO:0000250|UniProtKB:Q7Z6G3}. TISSUE SPECIFICITY: Expressed in the iris, in the ciliary margin of the retina and in the inner portion of the neural retina. Expressed in the spinal dorsal horn with especially strong expression in lamina IIi; found in excitory synaptic boutons (at protein level). {ECO:0000269|PubMed:11641222, ECO:0000269|PubMed:26843217}. +P97798 NEO1_MOUSE Neogenin 1493 163,160 Alternative sequence (4); Beta strand (24); Chain (1); Compositional bias (1); Disulfide bond (4); Domain (10); Glycosylation (8); Helix (1); Modified residue (8); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1137 1157 Helical. {ECO:0000255}. TOPO_DOM 37 1136 Extracellular. {ECO:0000255}.; TOPO_DOM 1158 1493 Cytoplasmic. {ECO:0000255}. FUNCTION: Multi-functional cell surface receptor regulating cell adhesion in many diverse developmental processes, including neural tube and mammary gland formation, myogenesis and angiogenesis. Receptor for members of the BMP, netrin, and repulsive guidance molecule (RGM) families. Netrin-Neogenin interactions result in a chemoattractive axon guidance response and cell-cell adhesion, the interaction between NEO1/Neogenin and RGMa and RGMb induces a chemorepulsive response. {ECO:0000269|PubMed:23744777}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SUBUNIT: Interacts with BMP2, BMP4, BMP6, and BMP7 (By similarity). Interacts with RGMA and RGMB. Interacts with MYO10. {ECO:0000250, ECO:0000269|PubMed:17237772, ECO:0000269|PubMed:17389603, ECO:0000269|PubMed:23744777}. DOMAIN: The Fibronectin repeats 5 and 6 mediate interaction with RGM family molecules. TISSUE SPECIFICITY: Widely expressed. +Q9R0A5 NEK3_MOUSE Serine/threonine-protein kinase Nek3 (EC 2.7.11.1) (Never in mitosis A-related kinase 3) (NimA-related protein kinase 3) 511 57,464 Active site (1); Binding site (1); Chain (1); Domain (1); Modified residue (3); Mutagenesis (1); Nucleotide binding (1); Region (1); Sequence conflict (16) FUNCTION: Protein kinase which influences neuronal morphogenesis and polarity through effects on microtubules. Regulates microtubule acetylation in neurons. Contributes to prolactin-mediated phosphorylation of PXN and VAV2. {ECO:0000269|PubMed:19509051}. PTM: Phosphorylation at Thr-477 regulates its catalytic activity. {ECO:0000269|PubMed:19509051}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19509051}. Cell projection, axon {ECO:0000269|PubMed:19509051}. SUBUNIT: Interacts with PXN, PRLR, VAV1 and VAV2 and this interaction is prolactin-dependent. {ECO:0000250}. TISSUE SPECIFICITY: Brain. {ECO:0000269|PubMed:19509051}. +Q61391 NEP_MOUSE Neprilysin (EC 3.4.24.11) (Atriopeptidase) (Enkephalinase) (Neutral endopeptidase 24.11) (NEP) (Neutral endopeptidase) (Skin fibroblast elastase) (SFE) (CD antigen CD10) 750 85,702 Active site (2); Beta strand (2); Binding site (1); Chain (1); Disulfide bond (6); Glycosylation (6); Initiator methionine (1); Lipidation (1); Metal binding (3); Modified residue (2); Motif (1); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 29 51 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 2 28 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 52 750 Extracellular. {ECO:0000255}. FUNCTION: Thermolysin-like specificity, but is almost confined on acting on polypeptides of up to 30 amino acids. Biologically important in the destruction of opioid peptides such as Met- and Leu-enkephalins by cleavage of a Gly-Phe bond. Able to cleave angiotensin-1, angiotensin-2 and angiotensin 1-9. Involved in the degradation of atrial natriuretic factor (ANF) (By similarity). Displays UV-inducible elastase activity toward skin preelastic and elastic fibers (PubMed:20876573). {ECO:0000250|UniProtKB:P08473, ECO:0000269|PubMed:20876573}. PTM: Myristoylation is a determinant of membrane targeting. {ECO:0000250}.; PTM: Glycosylation at Asn-628 is necessary both for surface expression and neutral endopeptidase activity. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein. +Q8R2U2 NEPRO_MOUSE Nucleolus and neural progenitor protein (Neural progenitor protein) 564 63,394 Chain (1); Region (1) FUNCTION: May play a role in cortex development as part of the Notch signaling pathway. Downstream of Notch may repress the expression of proneural genes and inhibit neuronal differentiation thereby maintaining neural progenitors (PubMed:19906856). May also play a role in preimplentation embryo development (PubMed:26178919). {ECO:0000269|PubMed:19906856, ECO:0000269|PubMed:26178919}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19906856}. Nucleus, nucleolus {ECO:0000269|PubMed:26178919}. +Q922L6 NELFD_MOUSE Negative elongation factor D (NELF-D) (TH1-like protein) 591 66,276 Chain (1); Erroneous initiation (6); Sequence conflict (3) FUNCTION: Essential component of the NELF complex, a complex that negatively regulates the elongation of transcription by RNA polymerase II (By similarity). The NELF complex, which acts via an association with the DSIF complex and causes transcriptional pausing, is counteracted by the P-TEFb kinase complex (By similarity). {ECO:0000250|UniProtKB:Q8IXH7}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8IXH7}. SUBUNIT: The NELF complex is composed of NELFA, NELFB, NELFCD and NELFE; NELFA and NELFCD form a stable subcomplex that binds primarily through NELFCD to the N-terminus of NELFB (By similarity). Binds RNA which may help to stabilize the NELF complex on nucleic acid (By similarity). In vitro, the NELFA:NELFCD subcomplex binds to ssDNA and ssRNA in a sequence- and structure-dependent manner (By similarity). Interacts with ARAF1 (By similarity). Interacts with PCF11 (By similarity). Interacts with NELFB (PubMed:26010750). {ECO:0000250|UniProtKB:Q8IXH7, ECO:0000269|PubMed:26010750}. +P06837 NEUM_MOUSE Neuromodulin (Axonal membrane protein GAP-43) (Calmodulin-binding protein P-57) (Growth-associated protein 43) 227 23,632 Chain (1); Domain (1); Helix (1); Lipidation (2); Modified residue (10); Region (1) "FUNCTION: This protein is associated with nerve growth. It is a major component of the motile ""growth cones"" that form the tips of elongating axons. Plays a role in axonal and dendritic filopodia induction." PTM: Palmitoylation by ARF6 is essential for plasma membrane association and axonal and dendritic filopodia induction. Deacylated by LYPLA2 (By similarity). {ECO:0000250}.; PTM: Phosphorylated at Ser-41 by PHK. Phosphorylation of this protein by a protein kinase C is specifically correlated with certain forms of synaptic plasticity. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection, growth cone membrane; Peripheral membrane protein; Cytoplasmic side. Cell junction, synapse. Cell projection, filopodium membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Cytoplasmic surface of growth cone and synaptic plasma membranes. SUBUNIT: Binds calmodulin with a greater affinity in the absence of Ca(2+) than in its presence (By similarity). Identified in a complex containing FGFR4, NCAM1, CDH2, PLCG1, FRS2, SRC, SHC1, GAP43 and CTTN. {ECO:0000250, ECO:0000269|PubMed:11433297}. +O35657 NEUR1_MOUSE Sialidase-1 (EC 3.2.1.18) (G9 sialidase) (Lysosomal sialidase) (N-acetyl-alpha-neuraminidase 1) 409 44,591 Active site (4); Binding site (5); Chain (1); Glycosylation (4); Motif (2); Natural variant (1); Repeat (4); Sequence conflict (6); Signal peptide (1) FUNCTION: Catalyzes the removal of sialic acid (N-acetylneuraminic acid) moities from glycoproteins and glycolipids. To be active, it is strictly dependent on its presence in the multienzyme complex. Appears to have a preference for alpha 2-3 and alpha 2-6 sialyl linkage. {ECO:0000269|PubMed:9363440, ECO:0000269|PubMed:9384611}. PTM: N-glycosylated. {ECO:0000305}.; PTM: Phosphorylation of tyrosine within the internalization signal results in inhibition of sialidase internalization and blockage on the plasma membrane. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:9384611}; Peripheral membrane protein {ECO:0000269|PubMed:9384611}; Lumenal side {ECO:0000269|PubMed:9384611}. Lysosome lumen {ECO:0000269|PubMed:9384611}. Cell membrane {ECO:0000269|PubMed:9384611}. Cytoplasmic vesicle {ECO:0000269|PubMed:9384611}. Note=Localized not only on the inner side of the lysosomal membrane and in the lysosomal lumen, but also on the plasma membrane and in intracellular vesicles. SUBUNIT: Interacts with cathepsin A (protective protein), beta-galactosidase and N-acetylgalactosamine-6-sulfate sulfatase in a multienzyme complex. DOMAIN: A C-terminal internalization signal (YGTL) appears to allow the targeting of plasma membrane proteins to endosomes. TISSUE SPECIFICITY: Highly expressed in kidney, epididymis, followed by brain, spinal cord and weakly expressed in adrenal, heart, liver, lung and spleen. {ECO:0000269|PubMed:9384611}. +Q9JMH3 NEUR2_MOUSE Sialidase-2 (EC 3.2.1.18) (Cytosolic sialidase) (Mouse skeletal muscle sialidase) (MSS) (Murine thymic sialidase) (MTS) (N-acetyl-alpha-neuraminidase 2) 379 42,403 Active site (4); Binding site (7); Chain (1); Erroneous initiation (1); Motif (1); Repeat (2); Sequence conflict (2) FUNCTION: Catalyzes the removal of sialic acid (N-acetylneuraminic acid) moities from glycoproteins, oligosaccharides and gangliosides. SUBCELLULAR LOCATION: Cytoplasm. TISSUE SPECIFICITY: Highly expressed in heart. {ECO:0000269|PubMed:10713120}. +Q5SSH8 NEUFC_MOUSE Neuferricin (Cytochrome b5 domain-containing protein 2) 263 29,162 Alternative sequence (1); Chain (1); Domain (1); Sequence caution (3); Sequence conflict (1); Signal peptide (1) FUNCTION: Heme-binding protein which promotes neuronal but not astrocyte differentiation. {ECO:0000269|PubMed:19968755}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19968755}. DOMAIN: The cytochrome b5 heme-binding domain was proven to bind heme, although it lacks the conserved iron-binding His residues at position 73 and 106. TISSUE SPECIFICITY: Expressed in various tissues including brain, heart, adrenal gland, and kidney. In the brain, mainly expressed in pyramidal cells around the CA3 region of Ammon horn in hippocampus. Present in brain (at protein level). {ECO:0000269|PubMed:19968755}. +Q04690 NF1_MOUSE Neurofibromin (Neurofibromatosis-related protein NF-1) 2841 319,596 Alternative sequence (3); Chain (1); Compositional bias (1); Domain (2); Initiator methionine (1); Modified residue (14); Motif (1); Region (1) FUNCTION: Stimulates the GTPase activity of Ras. NF1 shows greater affinity for Ras GAP, but lower specific activity. May be a regulator of Ras activity. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. SUBUNIT: Interacts with HTR6 (By similarity). {ECO:0000250|UniProtKB:P21359}. DOMAIN: Binds phospholipids via a region that includes the CRAL-TRIO domain. Binds primarily glycerophospholipids with monounsaturated C18:1 and/or C16:1 fatty acid moieties and a phosphatidylethanolamine or phosphatidylcholine headgroup. Has lesser affinity for lipids containing phosphatidylserine and phosphatidylinositol (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Isoform 1 is expressed predominantly in brain, spinal cord and testis. Isoform 2 is expressed predominantly in adrenal gland, kidney, ovary and lung. Isoform 3 is expressed predominantly in adrenal gland and isoform 4 is expressed mainly in the testis. +Q8R4V1 NFAM1_MOUSE NFAT activation molecule 1 (Calcineurin/NFAT-activating ITAM-containing protein) (NFAT-activating protein with ITAM motif 1) 264 29,988 Alternative sequence (2); Chain (1); Disulfide bond (1); Domain (2); Glycosylation (2); Modified residue (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 160 180 Helical. {ECO:0000255}. TOPO_DOM 38 159 Extracellular. {ECO:0000255}.; TOPO_DOM 181 264 Cytoplasmic. {ECO:0000255}. FUNCTION: May function in immune system as a receptor which activates via the calcineurin/NFAT-signaling pathway the downstream cytokine gene promoters. Activates the transcription of IL-13 and TNF-alpha promoters (By similarity). May be involved in the regulation of B-cell, but not T-cell, development. {ECO:0000250}. PTM: N-glycosylated. {ECO:0000269|PubMed:15143214}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Partially recruited to lipid rafts upon BCR stimulation. {ECO:0000250}. SUBUNIT: No direct interaction with the B-cell antigen receptor (BCR). Interacts with SYK; probably involved in BCR signaling. Interacts with ZAP70. {ECO:0000269|PubMed:15143214}. DOMAIN: The ITAM domain displays no close similarity to any existing ITAMs, except for four conserved positions. The phosphorylated ITAM domain binds ZAP70 and SYK. TISSUE SPECIFICITY: Highly expressed in the spleen, expressed by both B- and CD4+ and CD8+ T-cells, as well as non-T- and non-B-cells, including macrophages and neutrophils. Expressed at low levels, if any, in non-immune tissue. {ECO:0000269|PubMed:15143214}. +Q9D0S4 NEUL2_MOUSE Neuralized-like protein 2 285 31,537 Chain (1); Domain (2) Protein modification; protein ubiquitination. FUNCTION: Plays an important role in the process of myofiber differentiation and maturation. Probable substrate-recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex, which mediates the ubiquitination of proteins. Probably contributes to catalysis through recognition and positioning of the substrate and the ubiquitin-conjugating enzyme. During myogenesis, controls the ubiquitination and degradation of the specific pool of CTNNB1/beta-catenin located at the sarcolemma. {ECO:0000269|PubMed:14960280}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14960280}. Note=In primary myoblasts, localized predominantly at the tips of differentiating myofibers. SUBUNIT: Probable component the ECS(NEURL2) E3 ubiquitin-protein ligase complex consisting of ELOB/Elongin B, ELOC/Elongin C, CUL5, RBX1 and NEURL2. Interacts with CTNNB1. {ECO:0000269|PubMed:14960280}. DOMAIN: The SOCS domain mediates the interaction with ELOB and ELOC, while the NHR domain may be involved in ubiquitination substrate binding. {ECO:0000250}. TISSUE SPECIFICITY: Expressed specifically in skeletal and cardiac muscles. {ECO:0000269|PubMed:14960280}. +P70353 NFYC_MOUSE Nuclear transcription factor Y subunit gamma (CAAT box DNA-binding protein subunit C) (Nuclear transcription factor Y subunit C) (NF-YC) 335 37,254 Chain (1); Sequence conflict (7) FUNCTION: Component of the sequence-specific heterotrimeric transcription factor (NF-Y) which specifically recognizes a 5'-CCAAT-3' box motif found in the promoters of its target genes. NF-Y can function as both an activator and a repressor, depending on its interacting cofactors. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Heterotrimeric transcription factor composed of three components, NF-YA, NF-YB and NF-YC. NF-YB and NF-YC must interact and dimerize for NF-YA association and DNA binding (By similarity). {ECO:0000250}. +O88322 NID2_MOUSE Nidogen-2 (NID-2) (Entactin-2) 1403 153,913 Chain (1); Disulfide bond (21); Domain (9); Glycosylation (4); Modified residue (1); Motif (1); Repeat (5); Sequence conflict (9); Signal peptide (1) FUNCTION: Cell adhesion glycoprotein. Might be involved in osteoblast differentiation. It probably has a role in cell-extracellular matrix interactions. PTM: Highly N- and O-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane. SUBUNIT: Interacts with LAMA2. Interacts with COL13A1 (By similarity). {ECO:0000250}. +Q3UW53 NIBAN_MOUSE Protein Niban (Protein FAM129A) 926 102,649 Chain (1); Erroneous initiation (3); Initiator methionine (1); Lipidation (1); Modified residue (8); Sequence caution (2); Sequence conflict (8) FUNCTION: Regulates phosphorylation of a number of proteins involved in translation regulation including EIF2A, EIF4EBP1 and RPS6KB1. May be involved in the endoplasmic reticulum stress response. {ECO:0000269|PubMed:17588536}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9ESN0}. Membrane {ECO:0000250|UniProtKB:Q9BZQ8}; Lipid-anchor {ECO:0000250|UniProtKB:Q9BZQ8}. +P57716 NICA_MOUSE Nicastrin 708 78,492 Chain (1); Disulfide bond (5); Glycosylation (16); Sequence conflict (5); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 669 689 Helical. {ECO:0000250|UniProtKB:Q92542}. TOPO_DOM 28 668 Lumenal. {ECO:0000250|UniProtKB:Q92542}.; TOPO_DOM 690 708 Cytoplasmic. {ECO:0000250|UniProtKB:Q92542}. FUNCTION: Essential subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (amyloid-beta precursor protein). The gamma-secretase complex plays a role in Notch and Wnt signaling cascades and regulation of downstream processes via its role in processing key regulatory proteins, and by regulating cytosolic CTNNB1 levels. {ECO:0000269|PubMed:12716934}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q92542}. SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q92542}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q92542}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q92542}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q92542}. Melanosome {ECO:0000250|UniProtKB:Q92542}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. {ECO:0000250|UniProtKB:Q92542}. SUBUNIT: Component of the gamma-secretase complex. The functional gamma-secretase complex is composed of at least four polypeptides: a presenilin homodimer (PSEN1 or PSEN2), nicastrin (NCSTN), APH1 (APH1A or APH1B) and PEN2 (PubMed:12716934). Binds to proteolytic processed C-terminal fragments C83 and C99 of the amyloid precursor protein (APP). Interacts with PSEN1 and PSEN2. {ECO:0000250|UniProtKB:Q92542, ECO:0000269|PubMed:12716934}. +Q9JIL4 NHRF3_MOUSE Na(+)/H(+) exchange regulatory cofactor NHE-RF3 (NHERF-3) (CFTR-associated protein of 70 kDa) (Na(+)/H(+) exchanger regulatory factor 3) (Na/Pi cotransporter C-terminal-associated protein 1) (NaPi-Cap1) (PDZ domain-containing protein 1) (Sodium-hydrogen exchanger regulatory factor 3) 519 56,499 Beta strand (18); Chain (1); Domain (4); Frameshift (2); Helix (8); Modified residue (16); Mutagenesis (3); Sequence conflict (8); Turn (2) FUNCTION: A scaffold protein that connects plasma membrane proteins and regulatory components, regulating their surface expression in epithelial cells apical domains. May be involved in the coordination of a diverse range of regulatory processes for ion transport and second messenger cascades. In complex with SLC9A3R1, may cluster proteins that are functionally dependent in a mutual fashion and modulate the trafficking and the activity of the associated membrane proteins. May play a role in the cellular mechanisms associated with multidrug resistance through its interaction with ABCC2 and PDZK1IP1. May potentiate the CFTR chloride channel activity (By similarity). Required for normal cell-surface expression of SCARB1. Plays a role in maintaining normal plasma cholesterol levels via its effects on SCARB1. Plays a role in the normal localization and function of the chloride-anion exchanger SLC26A6 to the plasma membrane in the brush border of the proximal tubule of the kidney. May be involved in the regulation of proximal tubular Na(+)-dependent inorganic phosphate cotransport therefore playing an important role in tubule function. {ECO:0000250, ECO:0000269|PubMed:11051556, ECO:0000269|PubMed:12556478, ECO:0000269|PubMed:14531806, ECO:0000269|PubMed:15523054, ECO:0000269|PubMed:16141316, ECO:0000269|PubMed:20739281, ECO:0000269|PubMed:21602281}. SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9JJ40}. Cell membrane {ECO:0000269|PubMed:11051556, ECO:0000269|PubMed:16141316}. Note=Localized in the brush border membrane of renal proximal tubule cells (PubMed:11051556, PubMed:16141316). Associated with peripheral membranes (By similarity). Localizes to the apical compartment of proximal cells and to sinusoidal liver membranes (By similarity). {ECO:0000250|UniProtKB:Q9JJ40, ECO:0000269|PubMed:11051556, ECO:0000269|PubMed:16141316}. SUBUNIT: Interacts with PDZK1IP1 and ABCC2. Binds to the C-terminal region of SLC26A3. Interacts (via C-terminal PDZ domain) with SLC26A6 (via C-terminal domain). Interacts (via C-terminal PDZ domain) with SLC9A3 (via C-terminal domain) (By similarity). Component of a complex, composed of PDZK1, SYNGAP1, KLHL17 and NMDA receptors. Interacts (via PDZ1 domain) directly with KLHL17; the interaction is important for integrity of actin cytoskeleton structures in neurons (By similarity). Forms a heterodimeric complex with SLC9A3R1. Interacts with AKAP2, BCR, CFTR, SLCO1A1, SLC22A12, SLC22A4, SLC22A5, SLC26A6, SLC9A3R2 and SLC17A1. Interacts (via the first PDZ domain) with PTGIR (via non-isoprenylated C-terminus). Interacts (via PDZ domains 1 and 3) with SCARB1 (C-terminal domain). {ECO:0000250, ECO:0000269|PubMed:11051556, ECO:0000269|PubMed:11099500, ECO:0000269|PubMed:14531806, ECO:0000269|PubMed:15523054, ECO:0000269|PubMed:20739281, ECO:0000269|PubMed:21602281, ECO:0000269|PubMed:23457445}. DOMAIN: The PDZ 2 and 3 domains seem to be involved in the interaction with SLC26A3. {ECO:0000250}.; DOMAIN: Interaction with the C-terminus of CFTR could be mediated through independent binding of PDZ 1, 3 and 4 domains.; DOMAIN: The PDZ 1 and 3 domains seem to be involved in the interaction with SLCO1A1. {ECO:0000250}.; DOMAIN: The PDZ 1 domain interacts with BCR. {ECO:0000250}.; DOMAIN: The PDZ 2 and 4 domains do not interact with the C-terminal region of SCARB1. TISSUE SPECIFICITY: Expressed in kidney, liver, small intestine. brain, lung, and testis (at protein level). {ECO:0000269|PubMed:11051556, ECO:0000269|PubMed:12556478}. +Q9DCN2 NB5R3_MOUSE NADH-cytochrome b5 reductase 3 (B5R) (Cytochrome b5 reductase) (EC 1.6.2.2) (Diaphorase-1) [Cleaved into: NADH-cytochrome b5 reductase 3 membrane-bound form; NADH-cytochrome b5 reductase 3 soluble form] 301 34,128 Alternative sequence (1); Chain (2); Domain (1); Initiator methionine (1); Lipidation (1); Modified residue (4); Nucleotide binding (2) FUNCTION: Desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction. {ECO:0000250}. SUBCELLULAR LOCATION: Isoform 1: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P00387}; Lipid-anchor {ECO:0000250|UniProtKB:P00387}; Cytoplasmic side {ECO:0000250|UniProtKB:P00387}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:P00387}; Lipid-anchor {ECO:0000250|UniProtKB:P00387}; Cytoplasmic side {ECO:0000250|UniProtKB:P00387}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Note=Produces the soluble form found in erythrocytes. {ECO:0000250|UniProtKB:P00387}. SUBUNIT: Component of a complex composed of cytochrome b5, NADH-cytochrome b5 reductase (CYB5R3) and MOSC2. {ECO:0000250}. +P97432 NBR1_MOUSE Next to BRCA1 gene 1 protein (Membrane component chromosome 17 surface marker 2 homolog) (Neighbor of BRCA1 gene 1 protein) 988 109,958 Chain (1); Compositional bias (1); Domain (2); Modified residue (5); Region (2); Sequence conflict (1); Zinc finger (1) FUNCTION: Acts probably as a receptor for selective autophagosomal degradation of ubiquitinated targets. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14596}. Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:Q14596}. Lysosome {ECO:0000250|UniProtKB:Q14596}. Cytoplasm, myofibril, sarcomere, M line {ECO:0000250|UniProtKB:Q501R9}. Note=In cardiac muscles localizes to the sarcomeric M line (By similarity). Is targeted to lysosomes for degradation (By similarity). {ECO:0000250|UniProtKB:Q14596, ECO:0000250|UniProtKB:Q501R9}. SUBUNIT: Homooligomer and heterooligomer. Interacts with SQSTM1, titin/TTN, TRIM55, RNF29, USP8, SQSTM1, MAP1LC3A, MAP1LC3B, MAP1LC3C, GABARAP, GABARAPL1 and GABARAPL2. Binds to ubiquitin and ubiquitinated proteins. {ECO:0000250}. DOMAIN: The PB1 domain mediates interaction with SQSTM1. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain. +Q9CQ49 NCBP2_MOUSE Nuclear cap-binding protein subunit 2 (20 kDa nuclear cap-binding protein) (NCBP 20 kDa subunit) (CBP20) 156 18,017 Binding site (2); Chain (1); Domain (1); Initiator methionine (1); Modified residue (4); Region (3) FUNCTION: Component of the cap-binding complex (CBC), which binds co-transcriptionally to the 5' cap of pre-mRNAs and is involved in various processes such as pre-mRNA splicing, translation regulation, nonsense-mediated mRNA decay, RNA-mediated gene silencing (RNAi) by microRNAs (miRNAs) and mRNA export. The CBC complex is involved in mRNA export from the nucleus via its interaction with ALYREF/THOC4/ALY, leading to the recruitment of the mRNA export machinery to the 5' end of mRNA and to mRNA export in a 5' to 3' direction through the nuclear pore. The CBC complex is also involved in mediating U snRNA and intronless mRNAs export from the nucleus. The CBC complex is essential for a pioneer round of mRNA translation, before steady state translation when the CBC complex is replaced by cytoplasmic cap-binding protein eIF4E. The pioneer round of mRNA translation mediated by the CBC complex plays a central role in nonsense-mediated mRNA decay (NMD), NMD only taking place in mRNAs bound to the CBC complex, but not on eIF4E-bound mRNAs. The CBC complex enhances NMD in mRNAs containing at least one exon-junction complex (EJC) via its interaction with UPF1, promoting the interaction between UPF1 and UPF2. The CBC complex is also involved in 'failsafe' NMD, which is independent of the EJC complex, while it does not participate in Staufen-mediated mRNA decay (SMD). During cell proliferation, the CBC complex is also involved in microRNAs (miRNAs) biogenesis via its interaction with SRRT/ARS2, thereby being required for miRNA-mediated RNA interference. The CBC complex also acts as a negative regulator of PARN, thereby acting as an inhibitor of mRNA deadenylation. In the CBC complex, NCBP2/CBP20 recognizes and binds capped RNAs (m7GpppG-capped RNA) but requires NCBP1/CBP80 to stabilize the movement of its N-terminal loop and lock the CBC into a high affinity cap-binding state with the cap structure. The conventional cap-binding complex with NCBP2 binds both small nuclear RNA (snRNA) and messenger (mRNA) and is involved in their export from the nucleus (By similarity). {ECO:0000250|UniProtKB:P52298, ECO:0000269|PubMed:19632182}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P52298}. Cytoplasm {ECO:0000250|UniProtKB:P52298}. SUBUNIT: Component of the nuclear cap-binding complex (CBC), a heterodimer composed of NCBP1/CBP80 and NCBP2/CBP20 that interacts with m7GpppG-capped RNA (By similarity). Found in a U snRNA export complex with PHAX/RNUXA, NCBP1/CBP80, NCBP2/CBP20, RAN, XPO1 and m7G-capped RNA (PubMed:10786834). Interacts with PHAX/RNUXA, EIF4G1, HNRNPF, HNRNPH1 and ALYREF/THOC4/ALY (By similarity). Interacts with SRRT/ARS2 and KPNA3 (By similarity). {ECO:0000250|UniProtKB:P52298, ECO:0000269|PubMed:10786834}. +Q8VCM8 NCLN_MOUSE Nicalin (Nicastrin-like protein) 563 62,908 Chain (1); Erroneous initiation (1); Glycosylation (2); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 523 543 Helical. {ECO:0000255}. TOPO_DOM 43 522 Lumenal. {ECO:0000255}.; TOPO_DOM 544 563 Cytoplasmic. {ECO:0000255}. FUNCTION: May antagonize Nodal signaling and subsequent organization of axial structures during mesodermal patterning. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. SUBUNIT: Forms a complex with NOMO and TMEM147, resulting in a stabilization of the 3 proteins, which are otherwise quickly degraded by the proteasome. Participates in a large protein complex, which is not related to the gamma-secretase complex (By similarity). {ECO:0000250}. +Q80XI4 PI42B_MOUSE Phosphatidylinositol 5-phosphate 4-kinase type-2 beta (EC 2.7.1.149) (1-phosphatidylinositol 5-phosphate 4-kinase 2-beta) (Diphosphoinositide kinase 2-beta) (Phosphatidylinositol 5-phosphate 4-kinase type II beta) (PI(5)P 4-kinase type II beta) (PIP4KII-beta) (PtdIns(5)P-4-kinase isoform 2-beta) 416 47,319 Chain (1); Compositional bias (1); Domain (1); Initiator methionine (1); Modified residue (7) FUNCTION: Participates in the biosynthesis of phosphatidylinositol 4,5-bisphosphate. {ECO:0000250}. PTM: Phosphorylated on serine residues (By similarity). Ubiquitinated by the SPOP/CUL3 complex. Ubiquitination is stimulated by PtdIns5P levels (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Associated with the plasma membrane and the endoplasmic reticulum. {ECO:0000250}. SUBUNIT: Homodimer. Binds TNFRSF1A. Interacts with PIP4K2A. Interaction with PIP4K2A suppresses ubiquitination by the SPOP/ CUL3 complex (By similarity). {ECO:0000250}. +Q9CXR4 PIGC_MOUSE Phosphatidylinositol N-acetylglucosaminyltransferase subunit C (EC 2.4.1.198) (Phosphatidylinositol-glycan biosynthesis class C protein) (PIG-C) 297 33,724 Chain (1); Transmembrane (4) TRANSMEM 67 87 Helical. {ECO:0000255}.; TRANSMEM 88 108 Helical. {ECO:0000255}.; TRANSMEM 153 173 Helical. {ECO:0000255}.; TRANSMEM 239 259 Helical. {ECO:0000255}. Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis. FUNCTION: Involved in GPI anchor biosynthesis. Part of the complex catalyzing the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis. {ECO:0000250|UniProtKB:Q92535}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Associates with PIGA, PIGH, PIGP, PIGQ and DPM2. The latter is not essential for activity (By similarity). {ECO:0000250}. +Q9ERS2 NDUAD_MOUSE NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13 (Cell death regulatory protein GRIM-19) (Complex I-B16.6) (CI-B16.6) (Gene associated with retinoic and interferon-induced mortality 19 protein) (GRIM-19) (Gene associated with retinoic and IFN-induced mortality 19 protein) (NADH-ubiquinone oxidoreductase B16.6 subunit) 144 16,860 Beta strand (2); Chain (1); Erroneous initiation (1); Helix (3); Initiator methionine (1); Modified residue (1); Sequence conflict (2); Transmembrane (1); Turn (4) TRANSMEM 30 51 Helical. {ECO:0000255}. FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. Involved in the interferon/all-trans-retinoic acid (IFN/RA) induced cell death. This apoptotic activity is inhibited by interaction with viral IRF1. Prevents the transactivation of STAT3 target genes. May play a role in CARD15-mediated innate mucosal responses and serve to regulate intestinal epithelial cell responses to microbes. {ECO:0000250|UniProtKB:Q9P0J0}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305|PubMed:12628925}; Single-pass membrane protein {ECO:0000305|PubMed:12628925}; Matrix side {ECO:0000305|PubMed:12628925}. Nucleus {ECO:0000269|PubMed:12628925}. Note=Localizes mainly in the mitochondrion. May be translocated into the nucleus upon IFN/RA treatment. {ECO:0000250|UniProtKB:Q9P0J0}. SUBUNIT: Complex I is composed of 45 different subunits. Interacts with CARD15, but not with CARD4. Interacts with STAT3, but not with STAT1, STAT2 and STAT5A. Interacts with OLFM4. {ECO:0000250|UniProtKB:Q9P0J0}. +Q9CQC7 NDUB4_MOUSE NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4 (Complex I-B15) (CI-B15) (NADH-ubiquinone oxidoreductase B15 subunit) 129 15,081 Beta strand (3); Chain (1); Helix (6); Initiator methionine (1); Modified residue (2); Transmembrane (1); Turn (3) TRANSMEM 88 105 Helical. {ECO:0000255}. FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. {ECO:0000250|UniProtKB:O95168}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:O95168}; Single-pass membrane protein {ECO:0000255}; Matrix side {ECO:0000250|UniProtKB:O95168}. SUBUNIT: Complex I is composed of 45 different subunits. {ECO:0000250|UniProtKB:O95168}. +P0C1P0 PIGY_MOUSE Phosphatidylinositol N-acetylglucosaminyltransferase subunit Y (Phosphatidylinositol-glycan biosynthesis class Y protein) (PIG-Y) 71 7,952 Chain (1); Topological domain (3); Transmembrane (2) TRANSMEM 6 26 Helical. {ECO:0000255}.; TRANSMEM 45 65 Helical. {ECO:0000255}. TOPO_DOM 1 5 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 27 44 Lumenal. {ECO:0000255}.; TOPO_DOM 66 71 Cytoplasmic. {ECO:0000255}. Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis. FUNCTION: Component of the GPI-GlcNAc transferase (GPI-GnT) complex in the endoplasmic reticulum, a complex that catalyzes transfer of GlcNAc from UDP-GlcNAc to an acceptor phosphatidylinositol, the first step in the production of GPI-anchors for cell surface proteins. May act by regulating the catalytic subunit PIGA (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with the GPI-GnT complex composed of PIGA, PIGC, PIGH, PIGP, PIGQ and DPM2. Interacts directly with PIGA. Does not interact with Ras proteins (By similarity). {ECO:0000250}. +Q9CQH3 NDUB5_MOUSE NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mitochondrial (Complex I-SGDH) (CI-SGDH) (NADH-ubiquinone oxidoreductase SGDH subunit) 189 21,710 Chain (1); Helix (4); Transit peptide (1); Transmembrane (1) TRANSMEM 73 93 Helical. {ECO:0000255}. FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. {ECO:0000250|UniProtKB:O43674}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:O43674}; Single-pass membrane protein {ECO:0000250|UniProtKB:O43674}; Matrix side {ECO:0000250|UniProtKB:O43674}. SUBUNIT: Complex I is composed of 45 different subunits. {ECO:0000250|UniProtKB:O43674}. +Q9EQH7 NDST3_MOUSE Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 3 (EC 2.8.2.8) (Glucosaminyl N-deacetylase/N-sulfotransferase 3) (NDST-3) (N-heparan sulfate sulfotransferase 3) (N-HSST 3) [Includes: Heparan sulfate N-deacetylase 3 (EC 3.-.-.-); Heparan sulfate N-sulfotransferase 3 (EC 2.8.2.-)] 873 101,040 Active site (1); Alternative sequence (3); Binding site (1); Chain (1); Disulfide bond (1); Glycosylation (6); Nucleotide binding (2); Region (2); Sequence conflict (5); Topological domain (2); Transmembrane (1) TRANSMEM 14 34 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 13 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 35 873 Lumenal. {ECO:0000255}. Glycan metabolism; heparan sulfate biosynthesis. Glycan metabolism; heparin biosynthesis. FUNCTION: Essential bifunctional enzyme that catalyzes both the N-deacetylation and the N-sulfation of glucosamine (GlcNAc) of the glycosaminoglycan in heparan sulfate. Modifies the GlcNAc-GlcA disaccharide repeating sugar backbone to make N-sulfated heparosan, a prerequisite substrate for later modifications in heparin biosynthesis. Has high deacetylase activity but low sulfotransferase activity. {ECO:0000269|PubMed:11087757}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. TISSUE SPECIFICITY: Strongly expressed strongly in brain. Expressed at high level at embryonic day 11 compared to other stages of development. Weakly expressed in adult heart, kidney, muscle, endothelial cells and testis but not in other tissues. {ECO:0000269|PubMed:11087757, ECO:0000269|PubMed:16056228}. +Q9EQW8 NDST4_MOUSE Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 4 (EC 2.8.2.8) (Glucosaminyl N-deacetylase/N-sulfotransferase 4) (NDST-4) (N-heparan sulfate sulfotransferase 4) (N-HSST 4) [Includes: Heparan sulfate N-deacetylase 4 (EC 3.-.-.-); Heparan sulfate N-sulfotransferase 4 (EC 2.8.2.-)] 872 100,655 Active site (1); Binding site (1); Chain (1); Disulfide bond (1); Glycosylation (5); Nucleotide binding (2); Region (2); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 14 34 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 13 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 35 872 Lumenal. {ECO:0000255}. Glycan metabolism; heparan sulfate biosynthesis. Glycan metabolism; heparin biosynthesis. FUNCTION: Essential bifunctional enzyme that catalyzes both the N-deacetylation and the N-sulfation of glucosamine (GlcNAc) of the glycosaminoglycan in heparan sulfate. Modifies the GlcNAc-GlcA disaccharide repeating sugar backbone to make N-sulfated heparosan, a prerequisite substrate for later modifications in heparin biosynthesis. Has low deacetylase activity but high sulfotransferase activity. {ECO:0000269|PubMed:11087757}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. TISSUE SPECIFICITY: Expressed at low level in brain and throughout embryogenesis. Not expressed in other tissues. {ECO:0000269|PubMed:11087757}. +O09111 NDUBB_MOUSE NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mitochondrial (Complex I-ESSS) (CI-ESSS) (NADH-ubiquinone oxidoreductase ESSS subunit) (Neuronal protein 15.6) (Np15.6) (p15.6) 151 17,444 Beta strand (2); Chain (1); Erroneous initiation (3); Helix (7); Transit peptide (1); Transmembrane (1); Turn (2) TRANSMEM 87 107 Helical. {ECO:0000255}. FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. {ECO:0000250|UniProtKB:Q9NX14}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9NX14}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9NX14}. SUBUNIT: Complex I is composed of 45 different subunits. {ECO:0000250|UniProtKB:Q9NX14}. +P46935 NEDD4_MOUSE E3 ubiquitin-protein ligase NEDD4 (EC 2.3.2.26) (HECT-type E3 ubiquitin transferase NEDD4) (Neural precursor cell expressed developmentally down-regulated protein 4) (NEDD-4) 887 102,706 Active site (1); Beta strand (8); Chain (1); Domain (5); Frameshift (1); Modified residue (5); Mutagenesis (1); Region (1); Turn (2) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Specifically ubiquitinates 'Lys-63' in target proteins (By similarity). Monoubiquitinates IGF1R at multiple sites, thus leading to receptor internalization and degradation in lysosomes. Ubiquitinates FGFR1, leading to receptor internalization and degradation in lysosomes. Involved in ubiquitination of ERBB4 intracellular domain E4ICD1 (PubMed:19193720). Predominantly involved in ubiquitination of membrane bound forms of ERBB4 rather than processed precursors and intermediate membrane-anchored 80 kDa fragments (m80HER4), with a lesser role in ubiquitination of ERBB4 intracellular domain E4ICD1 (PubMed:19047365). Promotes ubiquitination of RAPGEF2. Involved in the pathway leading to the degradation of VEGFR-2/KDFR, independently of its ubiquitin-ligase activity. Part of a signaling complex composed of NEDD4, RAP2A and TNIK which regulates neuronal dendrite extension and arborization during development. Ubiquitinates TNK2 and regulates EGF-induced degradation of EGFR and TNF2 (By similarity). Involved in the ubiquitination of ebola virus VP40 protein and this ubiquitination plays a role in facilitating viral budding. Ubiquitinates BRAT1 and this ubiquitination is enhanced in the presence of NDFIP1 (By similarity). {ECO:0000250|UniProtKB:P46934, ECO:0000269|PubMed:19047365, ECO:0000269|PubMed:19193720}. PTM: Auto-ubiquitinated. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral membrane protein. Note=Recruited to the plasma membrane by GRB10. Once complexed with GRB10 and IGF1R, follows IGF1R internalization, remaining associated with early endosomes. Uncouples from IGF1R-containing endosomes before the sorting of the receptor to the lysosomal compartment (By similarity). May be recruited to exosomes by NDFIP1. {ECO:0000250}. SUBUNIT: Binds SCNN1A, SCNN1B and SCNN1G. Interacts with NDFIP1 and NDFIP2; this interaction activates the E3 ubiquitin-protein ligase and may induce its recruitment to exosomes. Interacts with UBE2D2 (PubMed:9182527). Binds, in vitro, through the WW2 and WW3 domains, to neural isoforms of ENAH that contain the PPSY motif (PubMed:9407065). Interacts with BEAN1, LITAF, RNF11, WBP1, WBP2, PMEPAI and PRRG2 (PubMed:11042109). Interacts with murine leukemia virus Gag polyprotein (via PPXY motif) (PubMed:15908698). Interacts (via C2 domain) with GRB10 (via SH2 domain) (PubMed:12697834, PubMed:15060076, PubMed:18286479, PubMed:20980250). Interacts with ERBB4 (PubMed:19193720, PubMed:19047365). Interacts with TNIK; the interaction is direct, allows the TNIK-dependent recruitment of RAP2A and its ubiquitination by NEDD4 (PubMed:20159449). Interacts (via WW3 domain) with TNK2; EGF promotes this interaction. Interacts (via WW3 domain) with FGFR1 (via C-terminus). Interacts with OTUD7B (By similarity). Interacts with ISG15 (By similarity). Interacts (via WW domain) with RAPGEF2; this interaction leads to ubiquitination and degradation via the proteasome pathway. Interacts (via WW domains) with ARRDC3 (via PPXY motifs) (By similarity). Interacts with LAPTM4B; may play a role in the lysosomal sorting of LAPTM4B (By similarity). Interacts with ZBTB7B (PubMed:28784777). {ECO:0000250|UniProtKB:P46934, ECO:0000269|PubMed:11042109, ECO:0000269|PubMed:12697834, ECO:0000269|PubMed:15060076, ECO:0000269|PubMed:15908698, ECO:0000269|PubMed:18286479, ECO:0000269|PubMed:19047365, ECO:0000269|PubMed:19193720, ECO:0000269|PubMed:20159449, ECO:0000269|PubMed:20980250, ECO:0000269|PubMed:28784777, ECO:0000269|PubMed:9182527, ECO:0000269|PubMed:9407065}. DOMAIN: The WW domains mediate interaction with PPxY motif-containing proteins (By similarity). The WW domains mediate interaction with LITAF, RNF11, WBP1, WBP2, PMEPAI, NDFIP1 and PRRG2 (PubMed:11042109). {ECO:0000250|UniProtKB:P46934, ECO:0000269|PubMed:11042109}. TISSUE SPECIFICITY: Brain. +Q0II04 NEBL_MOUSE Nebulette (Actin-binding Z-disk protein) 452 52,201 Chain (1); Repeat (12) FUNCTION: Binds to actin and plays an important role in the assembly of the Z-disk. May functionally link sarcomeric actin to the desmin intermediate filaments in the heart muscle sarcomeres. Isoform 2 might play a role in the assembly of focal adhesion (By similarity). {ECO:0000250|UniProtKB:O76041}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O76041}. SUBUNIT: Interacts (via nebulin repeats 1-5) with DESM (via rod region). {ECO:0000250|UniProtKB:O76041}. +Q91WE2 PIP30_MOUSE PSME3-interacting protein (NEFA-interacting nuclear protein NIP30) (PA28G-interacting protein) 254 28,702 Chain (1); Modified residue (5); Region (1); Sequence conflict (2) FUNCTION: Promotes the association of the proteasome activator complex subunit PSME3 with the 20S proteasome and regulates its activity. Inhibits PSME3-mediated degradation of some proteasome substrates, probably by affecting their diffusion rate into the catalytic chamber of the proteasome. Also inhibits the interaction of PSME3 with COIL, inhibits accumulation of PSME3 in Cajal bodies and positively regulates the number of Cajal bodies in the nucleus. {ECO:0000250|UniProtKB:Q9GZU8}. PTM: Phosphorylation by CK2 stabilizes the interaction with PSME3. {ECO:0000250|UniProtKB:Q9GZU8}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26497270}. SUBUNIT: Interacts (via C-terminus) with both free and 20S proteasome-bound forms of the proteasome activator complex subunit PSME3/PA28G; the interaction is direct. {ECO:0000250|UniProtKB:Q9GZU8}. TISSUE SPECIFICITY: Expressed in skeletal muscle. {ECO:0000269|PubMed:26497270}. +Q5NCX5 NEUL4_MOUSE Neuralized-like protein 4 1563 167,637 Alternative sequence (1); Chain (1); Domain (6); Erroneous gene model prediction (1); Modified residue (2); Sequence conflict (1) FUNCTION: Promotes CCP110 ubiquitination and proteasome-dependent degradation. By counteracting accumulation of CP110, maintains normal centriolar homeostasis and preventing formation of ectopic microtubular organizing centers (By similarity). {ECO:0000250}. PTM: Ubiquitinated; undergoes HERC2-dependent 'Lys-48' ubiquitination. This ubiquitination leads to proteasomal degradation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250}. SUBUNIT: Interacts with CCP110; this interaction propmotes CCP110 ubiquitination and degradation via the proteasome pathway. Via its interaction with CCP110, may indirectly interact with CEP97. Interacts with the E3 ubiquitin-protein ligase HERC2 and UBE3A. May interact with MAPK6 and hence mediate MAPK6 interaction with UBE3A. Interaction with UBE3A may be indirect and mediated by HERC2 (By similarity). {ECO:0000250}. +Q9D3P9 NEUT_MOUSE Neurotensin/neuromedin N [Cleaved into: Large neuromedin N (NmN-125); Neuromedin N (NN) (NmN); Neurotensin (NT); Tail peptide] 169 19,608 Chain (1); Peptide (3); Signal peptide (1) FUNCTION: Neurotensin may play an endocrine or paracrine role in the regulation of fat metabolism. It causes contraction of smooth muscle (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250}. Note=Packaged within secretory vesicles. {ECO:0000250}. SUBUNIT: Interacts with NTSR1. Interacts with SORT1 (By similarity). {ECO:0000250}. +Q68FH0 PKP4_MOUSE Plakophilin-4 (Armadillo-related protein) 1190 131,551 Alternative sequence (4); Chain (1); Coiled coil (1); Compositional bias (1); Erroneous initiation (1); Modified residue (36); Repeat (4); Sequence conflict (4) FUNCTION: Plays a role as a regulator of Rho activity during cytokinesis. May play a role in junctional plaques (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, desmosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. Midbody {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Associated with the pericentrosomal region in interphase and with spindle poles during mitosis. In anaphase, during chromosome segregation, is recruited to the central microtubule bundle, focussed at the spindle midzone and ultimately localizes to the midbody at cytokinesis. Constituent of the midbody cytoskeletal matrix. Colocalized with desmoplakin at desmosomal junctional plaques in cultured epithelial cells (By similarity). {ECO:0000250}. SUBUNIT: Interacts (via the C-terminus) with FRMPD2 (via the PDZ 2 domain). Interacts with PDZD2. Interacts with RHOA; the interaction is detected at the midbody. Interacts with ECT2; the interaction is detected at the midbody (By similarity). {ECO:0000250}. +Q8K458 PKR2_MOUSE Prokineticin receptor 2 (PK-R2) (G-protein coupled receptor 73-like 1) 381 43,375 Chain (1); Disulfide bond (1); Erroneous initiation (1); Glycosylation (2); Sequence conflict (2); Topological domain (8); Transmembrane (7) TRANSMEM 52 72 Helical; Name=1. {ECO:0000255}.; TRANSMEM 87 107 Helical; Name=2. {ECO:0000255}.; TRANSMEM 134 154 Helical; Name=3. {ECO:0000255}.; TRANSMEM 169 189 Helical; Name=4. {ECO:0000255}.; TRANSMEM 221 241 Helical; Name=5. {ECO:0000255}.; TRANSMEM 271 291 Helical; Name=6. {ECO:0000255}.; TRANSMEM 311 331 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 51 Extracellular. {ECO:0000255}.; TOPO_DOM 73 86 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 108 133 Extracellular. {ECO:0000255}.; TOPO_DOM 155 168 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 190 220 Extracellular. {ECO:0000255}.; TOPO_DOM 242 270 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 292 310 Extracellular. {ECO:0000255}.; TOPO_DOM 332 381 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for prokineticin 2. Exclusively coupled to the G(q) subclass of heteromeric G proteins. Activation leads to mobilization of calcium, stimulation of phosphoinositide turnover and activation of p44/p42 mitogen-activated protein kinase (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8NFJ6}; Multi-pass membrane protein. SUBUNIT: Homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in several regions of the brain, including paraventricular hypothalamic nucleus, dorsal medial hypothalamic nucleus, paratenial thalamic nuclei, paracentral thalamic nucleus, lateral habenular nucleus, lateral septal nucleus, lateral globus pallidus and amygdala. Highest expression seen in paraventricular thalamic nuclei and is also extensively expressed in the suprachiasmatic nucleus. +P11672 NGAL_MOUSE Neutrophil gelatinase-associated lipocalin (NGAL) (Lipocalin-2) (Oncogene 24p3) (24p3) (SV-40-induced 24p3 protein) (Siderocalin LCN2) (p25) 200 22,875 Beta strand (10); Binding site (3); Chain (1); Disulfide bond (1); Glycosylation (2); Helix (3); Modified residue (1); Signal peptide (1); Turn (3) FUNCTION: Iron-trafficking protein involved in multiple processes such as apoptosis, innate immunity and renal development (PubMed:12453413). Binds iron through association with 2,5-dihydroxybenzoic acid (2,5-DHBA), a siderophore that shares structural similarities with bacterial enterobactin, and delivers or removes iron from the cell, depending on the context. Iron-bound form (holo-24p3) is internalized following binding to the SLC22A17 (24p3R) receptor, leading to release of iron and subsequent increase of intracellular iron concentration. In contrast, association of the iron-free form (apo-24p3) with the SLC22A17 (24p3R) receptor is followed by association with an intracellular siderophore, iron chelation and iron transfer to the extracellular medium, thereby reducing intracellular iron concentration. Involved in apoptosis due to interleukin-3 (IL3) deprivation: iron-loaded form increases intracellular iron concentration without promoting apoptosis, while iron-free form decreases intracellular iron levels, inducing expression of the proapoptotic protein BCL2L11/BIM, resulting in apoptosis. Involved in innate immunity; limits bacterial proliferation by sequestering iron bound to microbial siderophores, such as enterobactin (PubMed:15531878, PubMed:16446425). Can also bind siderophores from M.tuberculosis (By similarity). {ECO:0000250|UniProtKB:P80188, ECO:0000269|PubMed:12453413, ECO:0000269|PubMed:15531878, ECO:0000269|PubMed:16377569, ECO:0000269|PubMed:16446425, ECO:0000269|PubMed:20550936}. PTM: N-glycosylated. {ECO:0000269|PubMed:21911364, ECO:0000269|PubMed:8687399}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12453413, ECO:0000269|PubMed:20550936, ECO:0000269|PubMed:8687399}. Cytoplasmic granule lumen {ECO:0000250|UniProtKB:P80188}. Cytoplasmic vesicle lumen {ECO:0000250|UniProtKB:P80188}. Note=Upon binding to the SLC22A17 (24p3R) receptor, it is internalized (PubMed:16377569). Releases the bound iron in the acidic lumen of cytoplasmic vesicles (By similarity). {ECO:0000250|UniProtKB:P80188, ECO:0000269|PubMed:16377569}. SUBUNIT: Monomer. Homodimer; disulfide-linked. Heterodimer; disulfide-linked with MMP9. {ECO:0000250|UniProtKB:P80188}. TISSUE SPECIFICITY: Detected in lung, spleen, uterus, vagina and epididymis. {ECO:0000269|PubMed:8687399}. +P70447 NGN2_MOUSE Neurogenin-2 (NGN-2) (Helix-loop-helix protein mATH-4A) (mATH4A) (Protein atonal homolog 4) 263 28,216 Chain (1); Domain (1); Sequence conflict (1) FUNCTION: Transcriptional regulator. Involved in neuronal differentiation. Activates transcription by binding to the E box (5'-CANNTG-3'). {ECO:0000269|PubMed:14697366}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}. SUBUNIT: Efficient DNA binding requires dimerization with another bHLH protein. +P70661 NGN3_MOUSE Neurogenin-3 (NGN-3) (Helix-loop-helix protein mATH-4B) (mATH4B) (Protein atonal homolog 5) 214 23,267 Chain (1); Domain (1) FUNCTION: Acts as a transcriptional regulator. Together with NKX2-2, initiates transcriptional activation of NEUROD1. Involved in neurogenesis. Also required for the specification of a common precursor of the 4 pancreatic endocrine cell types. {ECO:0000269|PubMed:10677506, ECO:0000269|PubMed:19759004}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}. SUBUNIT: Efficient DNA binding requires dimerization with another bHLH protein. Interacts with ATOH8. {ECO:0000269|PubMed:18560595}. +Q99KS2 NGRN_MOUSE Neugrin (FI58Gm) (Neurite outgrowth-associated protein) (m-Neugrin) 293 32,447 Alternative sequence (2); Chain (1); Erroneous initiation (2); Erroneous translation (2); Frameshift (1); Glycosylation (1); Modified residue (1); Sequence caution (1); Sequence conflict (5); Signal peptide (1) FUNCTION: Plays an essential role in mitochondrial ribosome biogenesis. As a component of a functional protein-RNA module, consisting of RCC1L, NGRN, RPUSD3, RPUSD4, TRUB2, FASTKD2 and 16S mitochondrial ribosomal RNA (16S mt-rRNA), controls 16S mt-rRNA abundance and is required for intra-mitochondrial translation of core subunits of the oxidative phosphorylation system. {ECO:0000250|UniProtKB:Q9NPE2}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NPE2}. Secreted {ECO:0000250|UniProtKB:Q9NPE2}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q9NPE2}. SUBUNIT: Forms a regulatory protein-RNA complex, consisting of RCC1L, NGRN, RPUSD3, RPUSD4, TRUB2, FASTKD2 and 16S mt-rRNA. Interacts with 16S mt-rRNA; this interaction is direct. {ECO:0000250|UniProtKB:Q9NPE2}. TISSUE SPECIFICITY: Expressed in heart, brain, liver and kidney. In brain, mainly expressed in neurons rather than glial cells. {ECO:0000269|PubMed:11118320}. +Q8VI78 PLA1A_MOUSE Phospholipase A1 member A (EC 3.1.1.-) (Phosphatidylserine-specific phospholipase A1) (PS-PLA1) 456 49,984 Active site (3); Chain (1); Disulfide bond (3); Glycosylation (1); Sequence conflict (3); Signal peptide (1) FUNCTION: Hydrolyzes the ester bond at the sn-1 position of glycerophospholipids and produces 2-acyl lysophospholipids. Hydrolyzes phosphatidylserine (PS) in the form of liposomes and 1-acyl-2 lysophosphatidylserine (lyso-PS), but not triolein, phosphatidylcholine (PC), phosphatidylethanolamine (PE), phosphatidic acid (PA) or phosphatidylinositol (PI). Hydrolysis of lyso-PS in peritoneal mast cells activated by receptors for IgE leads to stimulate histamine production (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q62028 PLA2R_MOUSE Secretory phospholipase A2 receptor (PLA2-R) (PLA2R) (180 kDa secretory phospholipase A2 receptor) (M-type receptor) [Cleaved into: Soluble secretory phospholipase A2 receptor (Soluble PLA2-R) (Soluble PLA2R)] 1487 170,512 Alternative sequence (2); Chain (2); Disulfide bond (17); Domain (10); Erroneous initiation (2); Glycosylation (6); Motif (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1397 1417 Helical. {ECO:0000255}. TOPO_DOM 27 1396 Extracellular. {ECO:0000255}.; TOPO_DOM 1418 1487 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for secretory phospholipase A2 (sPLA2). Acts as a receptor for phosholipases sPLA2-IB/PLA2G1B, sPLA2-X/PLA2G10 and, with lower affinity, sPLA2-IIA/PLA2G2A. Also able to bind to snake PA2-like toxins. Although its precise function remains unclear, binding of sPLA2 to its receptor participates in both positive and negative regulation of sPLA2 functions as well as clearance of sPLA2. Binding of sPLA2-IB/PLA2G1B induces various effects depending on the cell type, such as activation of the mitogen-activated protein kinase (MAPK) cascade to induce cell proliferation, the production of lipid mediators, selective release of arachidonic acid in bone marrow-derived mast cells. In neutrophils, binding of sPLA2-IB/PLA2G1B can activate p38 MAPK to stimulate elastase release and cell adhesion. May be involved in responses in proinflammatory cytokine productions during endotoxic shock. Also has endocytic properties and rapidly internalizes sPLA2 ligands, which is particularly important for the clearance of extracellular sPLA2s to protect their potent enzymatic activities. The soluble secretory phospholipase A2 receptor form is circulating and acts as a negative regulator of sPLA2 functions by blocking the biological functions of sPLA2-IB/PLA2G1B and sPLA2-X/PLA2G10. {ECO:0000269|PubMed:10922494, ECO:0000269|PubMed:10946309, ECO:0000269|PubMed:11019817, ECO:0000269|PubMed:11481246, ECO:0000269|PubMed:11741598, ECO:0000269|PubMed:11830583, ECO:0000269|PubMed:12225974, ECO:0000269|PubMed:16815622, ECO:0000269|PubMed:17279628, ECO:0000269|PubMed:7925459, ECO:0000269|PubMed:9407054}. PTM: The secretory phospholipase A2 receptor form may be produced by the action of metalloproteinases. It contains all extracellular domains and only lacks transmembrane and cytosolic regions. It is however unclear whether this form is produced by proteolytic cleavage as suggested by some experiments reported by PubMed:11830583, or by alternative splicing. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11830583}; Single-pass type I membrane protein {ECO:0000269|PubMed:11830583}.; SUBCELLULAR LOCATION: Soluble secretory phospholipase A2 receptor: Secreted. DOMAIN: C-type lectin domains 3-5 mediate the interaction with phospholipase PLA2G1B. {ECO:0000269|PubMed:7925459}.; DOMAIN: The endocytosis signal probably mediates endocytosis via clathrin-coated pits. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. Present in type II alveolar epithelial cells and a subset of splenic lymphocytes. Present at the surface of polymorphonuclear neutrophils (at protein level). {ECO:0000269|PubMed:10864436, ECO:0000269|PubMed:12225974, ECO:0000269|PubMed:7925459}. +Q3UP44 NHLC4_MOUSE NHL-repeat-containing protein 4 136 14,169 Chain (1); Repeat (2) +Q8VD65 PI3R4_MOUSE Phosphoinositide 3-kinase regulatory subunit 4 (PI3-kinase regulatory subunit 4) (EC 2.7.11.1) 1358 152,599 Active site (1); Binding site (1); Chain (1); Compositional bias (2); Domain (1); Initiator methionine (1); Lipidation (1); Modified residue (5); Nucleotide binding (1); Repeat (11); Sequence conflict (5) FUNCTION: Regulatory subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate; different complex forms are believed to play a role in multiple membrane trafficking pathways: PI3KC3-C1 is involved in initiation of autophagosomes and PI3KC3-C2 in maturation of autophagosomes and endocytosis. Involved in regulation of degradative endocytic trafficking and cytokinesis, probably in the context of PI3KC3-C2 (By similarity). {ECO:0000250|UniProtKB:Q99570}. PTM: Myristoylated. {ECO:0000250}.; PTM: Probably autophosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Late endosome {ECO:0000250}. Cytoplasmic vesicle, autophagosome {ECO:0000305}. Membrane {ECO:0000250|UniProtKB:Q99570}; Lipid-anchor {ECO:0000250|UniProtKB:Q99570}. Note=As component of the PI3K complex I localized to pre-autophagosome structures. As component of the PI3K complex II localized predominantly to endosomes. Localizes also to discrete punctae along the ciliary axoneme (PubMed:24089209). {ECO:0000269|PubMed:24089209, ECO:0000305}. SUBUNIT: Component of the PI3K (PI3KC3/PI3K-III/class III phosphatidylinositol 3-kinase) complex the core of which is composed of the catalytic subunit PIK3C3, the regulatory subunit PIK3R4 and BECN1 associating with additional regulatory/auxilliary subunits to form alternative complex forms. Alternative complex forms containing a forth regulatory subunit in a mutually exclusive manner are PI3K complex I (PI3KC3-C1) containing ATG14, and PI3K complex II (PI3KC3-C2) containing UVRAG (PubMed:23332761). PI3KC3-C1 displays a V-shaped architecture with PIK3R4 serving as a bridge between PIK3C3 and the ATG14:BECN1 subcomplex. Both, PI3KC3-C1 and PI3KC3-C2, can associate with further regulatory subunits, such as RUBCN, SH3GLB1/Bif-1, AMBRA1 and NRBF2 (By similarity). PI3KC3-C1 probably associates with PIK3CB (PubMed:21059846). Interacts with RAB7A in the presence of PIK3C3/VPS34 (By similarity). Interacts with NRBF2 (By similarity). {ECO:0000250|UniProtKB:Q99570, ECO:0000269|PubMed:21059846, ECO:0000269|PubMed:23332761}. +Q8C261 NCKX5_MOUSE Sodium/potassium/calcium exchanger 5 (Na(+)/K(+)/Ca(2+)-exchange protein 5) (Solute carrier family 24 member 5) 501 54,984 Chain (1); Frameshift (1); Sequence conflict (6); Signal peptide (1); Topological domain (12); Transmembrane (11) TRANSMEM 67 87 Helical; Name=1. {ECO:0000255}.; TRANSMEM 112 132 Helical; Name=2. {ECO:0000255}.; TRANSMEM 137 157 Helical; Name=3. {ECO:0000255}.; TRANSMEM 171 191 Helical; Name=4. {ECO:0000255}.; TRANSMEM 195 215 Helical; Name=5. {ECO:0000255}.; TRANSMEM 306 326 Helical; Name=6. {ECO:0000255}.; TRANSMEM 335 355 Helical; Name=7. {ECO:0000255}.; TRANSMEM 363 383 Helical; Name=8. {ECO:0000255}.; TRANSMEM 401 421 Helical; Name=9. {ECO:0000255}.; TRANSMEM 439 459 Helical; Name=10. {ECO:0000255}.; TRANSMEM 471 491 Helical; Name=11. {ECO:0000255}. TOPO_DOM 30 66 Extracellular. {ECO:0000255}.; TOPO_DOM 88 111 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 133 136 Extracellular. {ECO:0000255}.; TOPO_DOM 158 170 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 192 194 Extracellular. {ECO:0000255}.; TOPO_DOM 216 305 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 327 334 Extracellular. {ECO:0000255}.; TOPO_DOM 356 362 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 384 400 Extracellular. {ECO:0000255}.; TOPO_DOM 422 438 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 460 470 Extracellular. {ECO:0000255}.; TOPO_DOM 492 501 Cytoplasmic. {ECO:0000255}. FUNCTION: Cation exchanger involved in pigmentation, possibly by participating in ion transport in melanosomes. Predominant sodium-Calcium exchanger in melanocytes. Probably transports 1 Ca(2+) and 1 K(+) to the melanosome in exchange for 4 cytoplasmic Na(+) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q71RS6}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q71RS6}. Melanosome {ECO:0000250|UniProtKB:Q71RS6}. TISSUE SPECIFICITY: Highly expressed in melanin-producing cells such as skin and eye compared to other tissues. Strongly overexpressed in melanoma cell lines. Expressed in dental tissues. {ECO:0000269|PubMed:16357253, ECO:0000269|PubMed:22677781}. +Q3U6Q4 PI3R6_MOUSE Phosphoinositide 3-kinase regulatory subunit 6 (Phosphoinositide 3-kinase gamma adapter protein of 87 kDa) (p84 PI3K adapter protein) (p84 PIKAP) (p87 PI3K adapter protein) (p87PIKAP) 756 84,663 Alternative sequence (3); Chain (1); Sequence conflict (1) FUNCTION: Regulatory subunit of the PI3K gamma complex. Acts as an adapter to drive activation of PIK3CG by beta-gamma G protein dimers. The PIK3CG:PIK3R6 heterodimer is much less sensitive to beta-gamma G proteins than PIK3CG:PIK3R5 and its membrane recruitment and beta-gamma G protein dimer-dependent activation requires HRAS bound to PIK3CG. Recruits of the PI3K gamma complex to a PDE3B:RAPGEF3 signaling complex involved in angiogenesis; signaling seems to involve RRAS. {ECO:0000269|PubMed:15797027, ECO:0000269|PubMed:16476736, ECO:0000269|PubMed:19906996}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16476736}. Cell membrane {ECO:0000269|PubMed:19906996}; Peripheral membrane protein {ECO:0000269|PubMed:19906996}. Note=Translocated to the plasma membrane in a Ras-dependent manner (PubMed:19906996). {ECO:0000269|PubMed:19906996}. SUBUNIT: Heterodimer of a catalytic subunit (PIK3CG) and a regulatory (PIK3R6) subunit. The binding of PIK3R6 to PIK3CG may exclude the binding of PIK3R5 to PIK3CG. Interacts with beta-gamma G protein dimers. Interacts with PDE3B; the interaction allows recruitment of the PI3K gamma complex to a PDE3B:RAPGEF3 complex. {ECO:0000269|PubMed:15797027, ECO:0000269|PubMed:16476736}. TISSUE SPECIFICITY: Highly expressed in heart. In a lower extent, also expressed in brain, spleen, lung, liver, kidney, prostate, thyroid, salivary gland, dendritic cells, macrophages and neutrophils. {ECO:0000269|PubMed:16476736}. +Q91XU3 PI42C_MOUSE Phosphatidylinositol 5-phosphate 4-kinase type-2 gamma (EC 2.7.1.149) (Phosphatidylinositol 5-phosphate 4-kinase type II gamma) (PI(5)P 4-kinase type II gamma) (PIP4KII-gamma) 421 47,336 Chain (1); Domain (1); Initiator methionine (1); Modified residue (3); Sequence conflict (1) FUNCTION: May play an important role in the production of Phosphatidylinositol bisphosphate (PIP2), in the endoplasmic reticulum. {ECO:0000250}. PTM: Phosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Membrane. Note=Mostly found in the cytosol and surrounding plasma membrane. However, its presence in the endoplasmic reticulum seems to be a prerequisite for PIP2 synthesis (By similarity). {ECO:0000250}. +Q9ERV7 PIDD1_MOUSE p53-induced death domain-containing protein 1 (EC 3.4.21.-) (Leucine-rich repeat and death domain-containing protein) [Cleaved into: PIDD-N; PIDD-C; PIDD-CC] 915 101,141 Active site (4); Chain (4); Domain (3); Initiator methionine (1); Modified residue (2); Region (3); Repeat (7); Site (2) FUNCTION: Component of the DNA damage/stress response pathway that functions downstream of p53/TP53 and can either promote cell survival or apoptosis (PubMed:10973264). Associated with CRADD and the CASP2 caspase, it forms the PIDDosome a complex that activates CASP2 and triggers apoptosis. Associated with IKBKG and RIPK1, it enhances sumoylation and ubiquitination of IKBKG which is important for activation of the transcription factor NF-kappa-B (By similarity). {ECO:0000250|UniProtKB:Q9HB75, ECO:0000269|PubMed:10973264}. PTM: Undergoes autoproteolytic processing whose extent either directs cells towards survival or apoptotic pathways. Autoproteolytically cleaved into two main fragments PIDD-N and PIDD-C. PIDD-C can be further processed into PIDD-CC, a processing which is enhanced by DNA damage. The cleavage producing PIDD-C is required for translocation of PIDD1 to the nucleus upon DNA damage and activation of NF-kappa-B. PIDD-CC mediates the interaction with CRADD and the cleavage producing PIDD-CC is required for the activation of CASP2. PIDD-N remains associated with PIDD-C and PIDD-CC after cleavage. {ECO:0000250|UniProtKB:Q9HB75}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9HB75}. Nucleus {ECO:0000250|UniProtKB:Q9HB75}. Note=Enriched in the nucleus upon DNA damage. {ECO:0000250|UniProtKB:Q9HB75}. SUBUNIT: Forms a complex named the PIDDosome with CASP2 and CRADD (PubMed:22279524). Forms a complex with IKBKG and RIPK1. Interacts with FADD and MADD (By similarity). {ECO:0000250|UniProtKB:Q9HB75, ECO:0000269|PubMed:22279524}. DOMAIN: The Death domain mediates the interaction with CRADD and the formation of a complex composed of 5 PIDD1 and 7 CRADD proteins which in turn recruit 7 CASP2 to form the PIDDosome. {ECO:0000250|UniProtKB:Q9HB75}.; DOMAIN: The LRR repeat-containing domain has a regulatory activity, being autoinhibitory for the activation of NF-kappa-B. {ECO:0000250|UniProtKB:Q9HB75}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10973264}. +Q9JJQ0 PIGB_MOUSE GPI mannosyltransferase 3 (EC 2.4.1.-) (GPI mannosyltransferase III) (GPI-MT-III) (Phosphatidylinositol-glycan biosynthesis class B protein) (PIG-B) 542 63,120 Chain (1); Glycosylation (1); Sequence conflict (2); Transmembrane (8) TRANSMEM 52 72 Helical. {ECO:0000255}.; TRANSMEM 125 145 Helical. {ECO:0000255}.; TRANSMEM 213 233 Helical. {ECO:0000255}.; TRANSMEM 244 264 Helical. {ECO:0000255}.; TRANSMEM 304 324 Helical. {ECO:0000255}.; TRANSMEM 327 347 Helical. {ECO:0000255}.; TRANSMEM 351 371 Helical. {ECO:0000255}.; TRANSMEM 376 396 Helical. {ECO:0000255}. Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis. FUNCTION: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the third alpha-1,2-mannose to Man2-GlcN-acyl-PI during GPI precursor assembly (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q5M9N4 PIGH_MOUSE Phosphatidylinositol N-acetylglucosaminyltransferase subunit H (EC 2.4.1.198) (Phosphatidylinositol-glycan biosynthesis class H protein) (PIG-H) 188 21,078 Chain (1) Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis. FUNCTION: Part of the complex catalyzing the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Associates with PIGA, PIGC, PIGP, PIGQ and DPM2. The latter is not essential for activity (By similarity). {ECO:0000250}. +Q9R1S3 PIGN_MOUSE GPI ethanolamine phosphate transferase 1 (EC 2.-.-.-) (Phosphatidylinositol-glycan biosynthesis class N protein) (PIG-N) 931 105,045 Alternative sequence (6); Chain (1); Glycosylation (5); Sequence conflict (7); Topological domain (16); Transmembrane (15) TRANSMEM 2 22 Helical. {ECO:0000255}.; TRANSMEM 443 463 Helical. {ECO:0000255}.; TRANSMEM 481 501 Helical. {ECO:0000255}.; TRANSMEM 503 523 Helical. {ECO:0000255}.; TRANSMEM 544 564 Helical. {ECO:0000255}.; TRANSMEM 566 586 Helical. {ECO:0000255}.; TRANSMEM 592 612 Helical. {ECO:0000255}.; TRANSMEM 619 639 Helical. {ECO:0000255}.; TRANSMEM 650 670 Helical. {ECO:0000255}.; TRANSMEM 686 706 Helical. {ECO:0000255}.; TRANSMEM 724 744 Helical. {ECO:0000255}.; TRANSMEM 787 807 Helical. {ECO:0000255}.; TRANSMEM 825 845 Helical. {ECO:0000255}.; TRANSMEM 859 879 Helical. {ECO:0000255}.; TRANSMEM 895 915 Helical. {ECO:0000255}. TOPO_DOM 1 1 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 23 442 Lumenal. {ECO:0000255}.; TOPO_DOM 464 480 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 502 502 Lumenal. {ECO:0000255}.; TOPO_DOM 524 543 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 565 565 Lumenal. {ECO:0000255}.; TOPO_DOM 587 591 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 613 618 Lumenal. {ECO:0000255}.; TOPO_DOM 640 649 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 671 685 Lumenal. {ECO:0000255}.; TOPO_DOM 707 723 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 745 786 Lumenal. {ECO:0000255}.; TOPO_DOM 808 824 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 846 858 Lumenal. {ECO:0000255}.; TOPO_DOM 880 894 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 916 931 Lumenal. {ECO:0000255}. Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis. FUNCTION: Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. May act as suppressor of replication stress and chromosome missegregation. {ECO:0000269|PubMed:10574991}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10574991}; Multi-pass membrane protein {ECO:0000269|PubMed:10574991}. +P48744 NDP_MOUSE Norrin (Norrie disease protein homolog) 131 14,700 Chain (1); Disulfide bond (7); Domain (1); Signal peptide (1) FUNCTION: Activates the canonical Wnt signaling pathway through FZD4 and LRP5 coreceptor. Plays a central role in retinal vascularization by acting as a ligand for FZD4 that signals via stabilizing beta-catenin (CTNNB1) and activating LEF/TCF-mediated transcriptional programs. Acts in concert with TSPAN12 to activate FZD4 independently of the Wnt-dependent activation of FZD4, suggesting the existence of a Wnt-independent signaling that also promote accumulation the beta-catenin (CTNNB1). May be involved in a pathway that regulates neural cell differentiation and proliferation. Possible role in neuroectodermal cell-cell interaction. {ECO:0000269|PubMed:15035989, ECO:0000269|PubMed:19837033}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Homodimer; disulfide-linked (By similarity). Component of a complex, at least composed of TSPAN12, FZD4, LRP5/6 and norrin (NDP). Binds FZD4 with high affinity. Interacts with LRP6 (via Beta-propellers 1 and 2). {ECO:0000250|UniProtKB:Q00604, ECO:0000269|PubMed:15035989, ECO:0000269|PubMed:19837033}. TISSUE SPECIFICITY: Expressed in the outer nuclear, inner nuclear and ganglion cell layers of the retina. {ECO:0000269|PubMed:10452356}. +Q9JHG1 PIGP_MOUSE Phosphatidylinositol N-acetylglucosaminyltransferase subunit P (EC 2.4.1.198) (Down syndrome critical region protein 5 homolog) (Phosphatidylinositol-glycan biosynthesis class P protein) (PIG-P) 132 15,101 Chain (1); Transmembrane (2) TRANSMEM 16 36 Helical. {ECO:0000255}.; TRANSMEM 56 76 Helical. {ECO:0000255}. Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis. FUNCTION: Part of the complex catalyzing the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis. {ECO:0000250|UniProtKB:P57054}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Associates with PIGA, PIGC, PIGH, PIGQ and DPM2. The latter is not essential for activity (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in tongue. {ECO:0000269|PubMed:11331941}. +Q7TPN3 PIGV_MOUSE GPI mannosyltransferase 2 (EC 2.4.1.-) (GPI mannosyltransferase II) (GPI-MT-II) (Phosphatidylinositol-glycan biosynthesis class V protein) (PIG-V) 493 55,026 Alternative sequence (1); Chain (1); Erroneous initiation (1); Sequence conflict (2); Topological domain (11); Transmembrane (10) TRANSMEM 14 34 Helical. {ECO:0000255}.; TRANSMEM 78 98 Helical. {ECO:0000255}.; TRANSMEM 114 134 Helical. {ECO:0000255}.; TRANSMEM 137 157 Helical. {ECO:0000255}.; TRANSMEM 162 182 Helical. {ECO:0000255}.; TRANSMEM 193 213 Helical. {ECO:0000255}.; TRANSMEM 235 255 Helical. {ECO:0000255}.; TRANSMEM 328 348 Helical. {ECO:0000255}.; TRANSMEM 379 399 Helical. {ECO:0000255}.; TRANSMEM 470 490 Helical. {ECO:0000255}. TOPO_DOM 1 13 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 35 77 Lumenal. {ECO:0000255}.; TOPO_DOM 99 113 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 135 136 Lumenal. {ECO:0000255}.; TOPO_DOM 158 161 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 183 192 Lumenal. {ECO:0000255}.; TOPO_DOM 214 234 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 256 327 Lumenal. {ECO:0000255}.; TOPO_DOM 349 378 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 400 469 Lumenal. {ECO:0000255}.; TOPO_DOM 491 493 Cytoplasmic. {ECO:0000255}. Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis. FUNCTION: Alpha-1,6-mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the second mannose to the glycosylphosphatidylinositol during GPI precursor assembly (By similarity). {ECO:0000250}. PTM: Not N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q99LV7 PIGX_MOUSE Phosphatidylinositol-glycan biosynthesis class X protein (PIG-X) 254 28,644 Alternative sequence (1); Chain (1); Glycosylation (1); Sequence caution (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 227 247 Helical. {ECO:0000255}. TOPO_DOM 23 226 Lumenal. {ECO:0000255}.; TOPO_DOM 248 254 Cytoplasmic. {ECO:0000255}. Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis. FUNCTION: Essential component of glycosylphosphatidylinositol-mannosyltransferase 1 which transfers the first of the 4 mannoses in the GPI-anchor precursors during GPI-anchor biosynthesis. Probably acts by stabilizing the mannosyltransferase PIGM (By similarity). {ECO:0000250}. PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Interacts with PIGM. {ECO:0000250}. +Q8BTP0 PIGZ_MOUSE GPI mannosyltransferase 4 (EC 2.4.1.-) (GPI mannosyltransferase IV) (GPI-MT-IV) (Phosphatidylinositol-glycan biosynthesis class Z protein) (PIG-Z) 560 62,043 Chain (1); Sequence conflict (1); Transmembrane (8) TRANSMEM 102 122 Helical. {ECO:0000255}.; TRANSMEM 126 143 Helical. {ECO:0000255}.; TRANSMEM 147 167 Helical. {ECO:0000255}.; TRANSMEM 186 206 Helical. {ECO:0000255}.; TRANSMEM 225 245 Helical. {ECO:0000255}.; TRANSMEM 333 353 Helical. {ECO:0000255}.; TRANSMEM 363 383 Helical. {ECO:0000255}.; TRANSMEM 388 408 Helical. {ECO:0000255}. Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis. FUNCTION: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers a fourth mannose to some trimannosyl-GPIs during GPI precursor assembly. The presence of a fourth mannose in GPI is facultative and only scarcely detected, suggesting that it only exists in some tissues (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q8CHR9 PIHD2_MOUSE PIH1 domain-containing protein 2 315 35,583 Alternative sequence (2); Chain (1); Erroneous translation (1) +Q3KNI6 PIHD3_MOUSE Protein PIH1D3 (PIH1 domain-containing protein 3) 218 24,501 Chain (1) FUNCTION: Plays a role in cytoplasmic pre-assembly of axonemal dynein. {ECO:0000269|PubMed:24421334}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24421334}. Note=Localized to the cytoplasm of spermatogenic cells. {ECO:0000269|PubMed:24421334}. SUBUNIT: Interacts with HSPA1A/B, HSP90AA1 and DNAI2 (PubMed:24421334). Interacts with DNAAF2 and DNAAF4 (By similarity). {ECO:0000250|UniProtKB:Q9NQM4, ECO:0000269|PubMed:24421334}. TISSUE SPECIFICITY: Specifically expressed in testis. Detected in pachytene spermatocytes from 5 weeks of age and in pachytene and diplotene spermatocytes of adult mice. Not detected in spermatids or mature sperm. {ECO:0000269|PubMed:24421334}. +Q9DCS9 NDUBA_MOUSE NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10 (Complex I-PDSW) (CI-PDSW) (NADH-ubiquinone oxidoreductase PDSW subunit) 176 21,024 Beta strand (3); Chain (1); Helix (5); Modified residue (2); Turn (3) FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. {ECO:0000250|UniProtKB:O96000}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:O96000}; Peripheral membrane protein {ECO:0000250|UniProtKB:O96000}; Matrix side {ECO:0000250|UniProtKB:O96000}. SUBUNIT: Complex I is composed of 45 different subunits. {ECO:0000250|UniProtKB:O96000}. +Q9CQ54 NDUC2_MOUSE NADH dehydrogenase [ubiquinone] 1 subunit C2 (Complex I-B14.5b) (CI-B14.5b) (NADH-ubiquinone oxidoreductase subunit B14.5b) 120 14,164 Beta strand (2); Chain (1); Helix (4); Transmembrane (1) TRANSMEM 57 76 Helical. {ECO:0000255}. FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. {ECO:0000250|UniProtKB:O95298}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:O95298}; Single-pass membrane protein {ECO:0000255}; Matrix side {ECO:0000250|UniProtKB:O95298}. SUBUNIT: Complex I is composed of 45 different subunits. {ECO:0000250|UniProtKB:O95298}. +Q9DC70 NDUS7_MOUSE NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial (EC 1.6.99.3) (EC 7.1.1.2) (Complex I-20kD) (CI-20kD) (NADH-ubiquinone oxidoreductase 20 kDa subunit) 224 24,683 Beta strand (7); Chain (1); Helix (9); Metal binding (4); Modified residue (2); Transit peptide (1); Turn (2) FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. {ECO:0000250|UniProtKB:O75251}. PTM: Hydroxylated ar Arg-111 by NDUFAF5 early in the pathway of assembly of complex I, before the formation of the juncture between peripheral and membrane arms. {ECO:0000250|UniProtKB:O75251}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:O75251}. SUBUNIT: Complex I is composed of 45 different subunits This is a component of the iron-sulfur (IP) fragment of the enzyme. {ECO:0000250|UniProtKB:O75251}. +Q8CB65 NEMP2_MOUSE Nuclear envelope integral membrane protein 2 421 47,894 Alternative sequence (2); Chain (1); Sequence conflict (1); Signal peptide (1); Transmembrane (6) TRANSMEM 64 84 Helical. {ECO:0000255}.; TRANSMEM 147 167 Helical. {ECO:0000255}.; TRANSMEM 175 195 Helical. {ECO:0000255}.; TRANSMEM 206 226 Helical. {ECO:0000255}.; TRANSMEM 238 258 Helical. {ECO:0000255}.; TRANSMEM 281 301 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000250|UniProtKB:Q6ZQE4}; Multi-pass membrane protein {ECO:0000255}; Nucleoplasmic side {ECO:0000250|UniProtKB:B9X187}. +Q9ES74 NEK7_MOUSE Serine/threonine-protein kinase Nek7 (EC 2.7.11.1) (Never in mitosis A-related kinase 7) (NimA-related protein kinase 7) 302 34,537 Active site (1); Binding site (1); Chain (1); Domain (1); Modified residue (3); Nucleotide binding (1); Region (1); Site (1) FUNCTION: Protein kinase which plays an important role in mitotic cell cycle progression. Required for microtubule nucleation activity of the centrosome, robust mitotic spindle formation and cytokinesis. Phosphorylates RPS6KB1. {ECO:0000269|PubMed:20473324}. PTM: Phosphorylation at Ser-195 required for its activation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Note=Present at centrosome throughout the cell cycle. Also detected at spindle midzone of the anaphase cells and eventually concentrates at the midbody (By similarity). {ECO:0000250}. SUBUNIT: Monomer. Interacts with NEK9 (By similarity). {ECO:0000250}. DOMAIN: Displays an autoinhibited conformation: Tyr-97 side chain points into the active site, interacts with the activation loop, and blocks the alphaC helix. The autoinhibitory conformation is released upon binding with NEK9 (By similarity). {ECO:0000250}.; DOMAIN: The NTE (N-terminal extension) motif is a structural component of the catalytic domain and thus contributes to activity. {ECO:0000250}. +P02816 PIP_MOUSE Prolactin-inducible protein homolog (14 kDa submandibular gland protein) (SMGP) (Gross cystic disease fluid protein 15) (GCDFP-15) (Prolactin-induced protein) 146 16,823 Chain (1); Disulfide bond (2); Modified residue (1); Sequence conflict (4); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. SUBUNIT: Monomer. Interacts with AZGP1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Lacrimal and submaxillary glands. +P33215 NEDD1_MOUSE Protein NEDD1 (Neural precursor cell expressed developmentally down-regulated protein 1) (NEDD-1) 660 71,292 Alternative sequence (2); Chain (1); Modified residue (8); Repeat (8); Sequence conflict (5) FUNCTION: Required for mitosis progression. Promotes the nucleation of microtubules from the spindle (By similarity). May play an important role during the embryonic development and differentiation of the central nervous system (PubMed:1378265). {ECO:0000250|UniProtKB:Q8NHV4, ECO:0000269|PubMed:1378265}. PTM: During mitosis, prior phosphorylation on Thr-550 by CDK1 promotes subsequent phosphorylation by PLK1 on Ser-397, Ser-426 and Ser-637. Phosphorylated NEDD1 can interact with gamma-tubulin for targeting the gamma-tubulin ring complex (gTuRC) to the centrosome, an important step for spindle formation. {ECO:0000250|UniProtKB:Q8NHV4}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q8NHV4}. SUBUNIT: Interacts with FAM29A. Interacts with HSPA1A and HSPA1B. Interacts with gamma-tubulin in a HSPA1A/B-dependent manner. {ECO:0000250|UniProtKB:Q8NHV4}. +Q8K1R7 NEK9_MOUSE Serine/threonine-protein kinase Nek9 (EC 2.7.11.1) (Nercc1 kinase) (Never in mitosis A-related kinase 9) (NimA-related protein kinase 9) 984 107,143 Active site (1); Binding site (1); Chain (1); Coiled coil (1); Compositional bias (2); Domain (1); Erroneous initiation (1); Helix (1); Initiator methionine (1); Modified residue (17); Nucleotide binding (1); Region (1); Repeat (6); Sequence conflict (1) FUNCTION: Pleiotropic regulator of mitotic progression, participating in the control of spindle dynamics and chromosome separation. Phosphorylates different histones, myelin basic protein, beta-casein, and BICD2. Phosphorylates histone H3 on serine and threonine residues and beta-casein on serine residues Important for G1/S transition and S phase progression. Phosphorylates NEK6 and NEK7 and stimulates their activity by releasing the autoinhibitory functions of Tyr-108 and Tyr-97 respectively (By similarity). {ECO:0000250}. PTM: Autophosphorylated on serine and threonine residues. When complexed with FACT, exhibits markedly elevated phosphorylation on Thr-210. During mitosis, not phosphorylated on Thr-210 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Homodimer. Binds to Ran GTPase. Has a greater affinity for Ran-GDP over Ran-GTP. Interacts with NEK6, NEK7 and BICD2. Interacts with SSRP1 and SUPT16H, the 2 subunits of the FACT complex. Interacts with DYNLL1; phosphorylation at Ser-949 strongly reduces DYNLL1 binding (By similarity). {ECO:0000250}. DOMAIN: Dimerizes through its coiled-coil domain. {ECO:0000250}. +Q8BZL1 NEUR4_MOUSE Sialidase-4 (EC 3.2.1.18) (N-acetyl-alpha-neuraminidase 4) (Neuraminidase 4) 478 52,426 Active site (4); Alternative sequence (1); Binding site (7); Chain (1); Motif (1); Repeat (3) FUNCTION: May function in lysosomal catabolism of sialylated glycoconjugates. Has sialidase activity towards synthetic substrates, such as 2'-(4-methylumbelliferyl)-alpha-D-N-acetylneuraminic acid (4-MU-NANA or 4MU-NeuAc). Has a broad substrate specificity being active on glycoproteins, oligosaccharides and sialylated glycolipids (By similarity). {ECO:0000250, ECO:0000269|PubMed:14637003}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Expressed predominantly in brain. {ECO:0000269|PubMed:14637003}. +P08551 NFL_MOUSE Neurofilament light polypeptide (NF-L) (68 kDa neurofilament protein) (Neurofilament triplet L protein) 543 61,508 Chain (1); Domain (1); Glycosylation (2); Initiator methionine (1); Modified residue (13); Region (12); Sequence conflict (8) FUNCTION: Neurofilaments usually contain three intermediate filament proteins: L, M, and H which are involved in the maintenance of neuronal caliber. PTM: O-glycosylated. {ECO:0000269|PubMed:16452088}.; PTM: Phosphorylated in the head and rod regions by the PKC kinase PKN1, leading to the inhibition of polymerization. {ECO:0000250}.; PTM: Ubiquitinated in the presence of TRIM2 and UBE2D1. {ECO:0000269|PubMed:18687884}. SUBUNIT: Interacts with ARHGEF28. Interacts with TRIM2. {ECO:0000269|PubMed:16236762, ECO:0000269|PubMed:18687884}. DOMAIN: The extra mass and high charge density that distinguish the neurofilament proteins from all other intermediate filament proteins are due to the tailpiece extensions. This region may form a charged scaffolding structure suitable for interaction with other neuronal components or ions. +P19246 NFH_MOUSE Neurofilament heavy polypeptide (NF-H) (200 kDa neurofilament protein) (Neurofilament triplet H protein) 1090 116,994 Chain (1); Compositional bias (2); Domain (1); Erroneous initiation (2); Modified residue (59); Region (10); Repeat (52); Sequence conflict (17) FUNCTION: Neurofilaments usually contain three intermediate filament proteins: L, M, and H which are involved in the maintenance of neuronal caliber. NF-H has an important function in mature axons that is not subserved by the two smaller NF proteins. PTM: There are a number of repeats of the tripeptide K-S-P, NFH is phosphorylated on a number of the serines in this motif. It is thought that phosphorylation of NFH results in the formation of interfilament cross bridges that are important in the maintenance of axonal caliber.; PTM: Phosphorylation seems to play a major role in the functioning of the larger neurofilament polypeptides (NF-M and NF-H), the levels of phosphorylation being altered developmentally and coincidentally with a change in the neurofilament function.; PTM: Phosphorylated in the head and rod regions by the PKC kinase PKN1, leading to the inhibition of polymerization. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P12036}. +Q8CAF4 NHSL1_MOUSE NHS-like protein 1 1587 169,419 Alternative sequence (2); Chain (1); Compositional bias (2); Erroneous initiation (4); Modified residue (11); Sequence caution (2); Sequence conflict (3) +B1AXH1 NHSL2_MOUSE NHS-like protein 2 854 91,873 Chain (1); Modified residue (5) +P30548 NK1R_MOUSE Substance-P receptor (SPR) (NK-1 receptor) (NK-1R) (Tachykinin receptor 1) 407 46,322 Chain (1); Disulfide bond (1); Glycosylation (2); Lipidation (1); Sequence conflict (1); Topological domain (8); Transmembrane (7) TRANSMEM 32 54 Helical; Name=1. {ECO:0000255}.; TRANSMEM 65 86 Helical; Name=2. {ECO:0000255}.; TRANSMEM 107 128 Helical; Name=3. {ECO:0000255}.; TRANSMEM 149 169 Helical; Name=4. {ECO:0000255}.; TRANSMEM 195 219 Helical; Name=5. {ECO:0000255}.; TRANSMEM 249 270 Helical; Name=6. {ECO:0000255}.; TRANSMEM 284 308 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 31 Extracellular. {ECO:0000255}.; TOPO_DOM 55 64 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 87 106 Extracellular. {ECO:0000255}.; TOPO_DOM 129 148 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 170 194 Extracellular. {ECO:0000255}.; TOPO_DOM 220 248 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 271 283 Extracellular. {ECO:0000255}.; TOPO_DOM 309 407 Cytoplasmic. {ECO:0000255}. FUNCTION: This is a receptor for the tachykinin neuropeptide substance P. It is probably associated with G proteins that activate a phosphatidylinositol-calcium second messenger system. The rank order of affinity of this receptor to tachykinins is: substance P > substance K > neuromedin K. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBUNIT: Interacts with ARRB1. {ECO:0000250}. +Q8VDK1 NIT1_MOUSE Deaminated glutathione amidase (dGSH amidase) (EC 3.5.1.128) (Nitrilase homolog 1) 323 35,705 Active site (3); Alternative sequence (1); Chain (1); Domain (1); Sequence conflict (2); Transit peptide (1) FUNCTION: Catalyzes the hydrolysation of the amide bond in N-(4-oxoglutarate)-L-cysteinylglycine (deaminated glutathione), a metabolite repair reaction to dispose of the harmful deaminated glutathione. Plays a role in cell growth and apoptosis: loss of expression promotes cell growth, resistance to DNA damage stress and increased incidence to NMBA-induced tumors. Has tumor suppressor properties that enhances the apoptotic responsiveness in cancer cells; this effect is additive to the tumor suppressor activity of FHIT. It is also a negative regulator of primary T-cells. {ECO:0000269|PubMed:16864578, ECO:0000269|PubMed:19395373, ECO:0000269|PubMed:19479888, ECO:0000269|PubMed:19595734, ECO:0000269|PubMed:19596042}. SUBCELLULAR LOCATION: Isoform 1: Mitochondrion {ECO:0000269|PubMed:19479888, ECO:0000269|PubMed:28373563}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm {ECO:0000269|PubMed:19479888, ECO:0000269|PubMed:28373563}. TISSUE SPECIFICITY: Expressed in most tissues with higher expression in adult liver and kidney as well as in fetal adrenal gland and skeletal muscle. {ECO:0000269|PubMed:16864578, ECO:0000269|PubMed:9671749}. +P97503 NKX32_MOUSE Homeobox protein Nkx-3.2 (Bagpipe homeobox protein homolog 1) (Homeobox protein NK-3 homolog B) 333 35,167 Chain (1); Compositional bias (2); DNA binding (1); Sequence conflict (3) FUNCTION: Transcriptional repressor that acts as a negative regulator of chondrocyte maturation. PLays a role in distal stomach development; required for proper antral-pyloric morphogenesis and development of antral-type epithelium. In concert with GSC, defines the structural components of the middle ear; required for tympanic ring and gonium development and in the regulation of the width of the malleus. {ECO:0000269|PubMed:14973294, ECO:0000269|PubMed:16421188, ECO:0000269|PubMed:19208343}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: Expressed widely in mesoderm at the gastroduodenal junction (at protein level). Expressed in visceral mesoderm and embryonic skeleton. Expression is restricted to immature proliferative chondrocytes during endochondral ossification. {ECO:0000269|PubMed:16421188, ECO:0000269|PubMed:19208343}. +Q8VEN2 PLET1_MOUSE Placenta-expressed transcript 1 protein (Antigen mAgK114) 237 25,006 Alternative sequence (1); Chain (1); Compositional bias (1); Frameshift (1); Glycosylation (4); Lipidation (1); Propeptide (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Modulates leading keratinocyte migration and cellular adhesion to matrix proteins during a wound-healing response and promotes wound repair. May play a role during trichilemmal differentiation of the hair follicle. {ECO:0000269|PubMed:20130590}. PTM: N-glycosylated. {ECO:0000269|PubMed:20130590}.; PTM: GPI-anchored. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:20130590}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:20130590}. Note=Localized at the apical membrane of the most differentiated keratinocytes of the outer root sheath (ORS), clustered mainly in planar regions of the plasma membrane at the base of microvilli. TISSUE SPECIFICITY: Present in hair follicle cells and sebaceous gland of skin, ciliated epithelial cells of trachea and bronchial tube, striated portion of submandibular gland, distal convoluted tubule cells of kidney, ciliated epithelial cells of oviduct, medulla of adrenal gland and anterior lobe of pituitary gland. Expressed in keratinocytes of the hair follicle at the trichilemmal zone corresponding to the terminally differentiated outermost suprabasal outer root sheath (ORS), including that of the sebaceous gland duct (SGD) and the directly adjacent upper distal end of the companion layer (CL). Expression is similar in all hair follicle growth stages. Also detected during both the early and late anagen phases above the bulge of stem cells. Expressed at the leading edge of the epidermal wound. Not expressed in the interfollicular epidermis (IFE), inner root sheath (IRS) and hair fiber. Highly expressed in placenta. Detected in mammary and prostate epithelia and in the pancreas (at protein level). {ECO:0000269|PubMed:15203209, ECO:0000269|PubMed:16219980, ECO:0000269|PubMed:18195351, ECO:0000269|PubMed:20130590}. +Q4PNJ2 NKAI2_MOUSE Sodium/potassium-transporting ATPase subunit beta-1-interacting protein 2 (Na(+)/K(+)-transporting ATPase subunit beta-1-interacting protein 2) (T-cell lymphoma breakpoint-associated target protein 1) 208 23,895 Alternative sequence (2); Chain (1); Sequence conflict (4); Transmembrane (4) TRANSMEM 1 23 Helical. {ECO:0000255}.; TRANSMEM 35 55 Helical. {ECO:0000255}.; TRANSMEM 64 84 Helical. {ECO:0000255}.; TRANSMEM 148 168 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Interacts with ATP1B1. {ECO:0000269|PubMed:17606467}. TISSUE SPECIFICITY: Detected in the brain only and specifically in neurons; expressed in multiple regions such as cerebral cortex, thalamus, cerebellum, olfactory bulb and brainstem, but not in the hippocampus. {ECO:0000269|PubMed:17606467}. +Q9D0F4 NKAP_MOUSE NF-kappa-B-activating protein 415 47,227 Chain (1); Compositional bias (2); Cross-link (2); Modified residue (7); Region (2); Sequence conflict (4) FUNCTION: Acts as a transcriptional repressor. Plays a role as a transcriptional corepressor of the Notch-mediated signaling required for T-cell development. Also involved in the TNF and IL-1 induced NF-kappa-B activation. Associates with chromatin at the Notch-regulated SKP2 promoter (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the Notch corepressor complex. Interacts with CIR1 and HDAC3 (By similarity). {ECO:0000250}. +Q9JHP7 PLGT2_MOUSE Protein O-glucosyltransferase 2 (EC 2.4.1.-) (Endoplasmic reticulum resident protein 58) (ER protein 58) (ERp58) (KDEL motif-containing protein 1) (Protein O-xylosyltransferase POGLUT2) (EC 2.4.2.26) 502 57,985 Alternative sequence (2); Chain (1); Glycosylation (3); Motif (1); Repeat (1); Sequence conflict (4); Signal peptide (1) Protein modification; protein glycosylation. FUNCTION: Protein glucosyltransferase that catalyzes the transfer of glucose from UDP-glucose to a serine residue within the consensus sequence peptide C-X-N-T-X-G-S-F-X-C. Can also catalyze the transfer of xylose from UDP-xylose but less efficiently. Specifically targets extracellular EGF repeats of proteins such as NOTCH1 and NOTCH3. May regulate the transport of NOTCH1 and NOTCH3 to the plasma membrane and thereby the Notch signaling pathway. {ECO:0000250|UniProtKB:Q6UW63}. PTM: N-glycosylated. {ECO:0000269|PubMed:11167020}. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138, ECO:0000269|PubMed:11167020}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11167020}. +Q9CYI0 NJMU_MOUSE Protein Njmu-R1 393 44,422 Chain (1); Modified residue (2) FUNCTION: May have a role in spermatogenesis. {ECO:0000250}. SUBUNIT: Interacts with TBC1D23; this interaction may be indirect. {ECO:0000269|PubMed:29084197}. +P30415 NKTR_MOUSE NK-tumor recognition protein (NK-TR protein) (Natural-killer cells cyclophilin-related protein) (Peptidyl-prolyl cis-trans isomerase NKTR) (PPIase) (EC 5.2.1.8) 1453 163,449 Chain (1); Compositional bias (6); Cross-link (8); Domain (1); Erroneous initiation (1); Modified residue (12); Region (1); Sequence conflict (7) FUNCTION: PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. Component of a putative tumor-recognition complex involved in the function of NK cells. {ECO:0000250|UniProtKB:P30414}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P30414}. +Q8VE28 NKD2_MOUSE Protein naked cuticle homolog 2 (Naked-2) (mNkd2) 461 51,501 Alternative sequence (1); Calcium binding (1); Chain (1); Compositional bias (1); Domain (1); Initiator methionine (1); Lipidation (1); Region (2); Sequence conflict (10) FUNCTION: Cell autonomous antagonist of the canonical Wnt signaling pathway. May activate a second Wnt signaling pathway that controls planar cell polarity. Required for processing of TGFA and for targeting of TGFA to the basolateral membrane of polarized epithelial cells (By similarity). {ECO:0000250}. PTM: Ubiquitinated, leading to rapid proteasomal degradation. Interaction with TGFA interferes with RNF25 binding and protects against ubiquitination mediated by RNF25 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q969F2}. Cytoplasm {ECO:0000250|UniProtKB:Q969F2}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q969F2}. SUBUNIT: Interacts with RNF25, TGFA (via cytoplasmic domain), and PPP2R3A (By similarity). Interacts with DVL1, DVL2 and DVL3. {ECO:0000250, ECO:0000269|PubMed:11356022}. DOMAIN: The N-terminal domain comprising the first 224 amino acid residues is mostly unstructured. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the cecum, colon, esophagus, ileum, jejunum, skin and stomach. {ECO:0000269|PubMed:11356022, ECO:0000269|PubMed:15064403, ECO:0000269|PubMed:15546883}. +Q99K10 NLGN1_MOUSE Neuroligin-1 843 94,149 Alternative sequence (3); Beta strand (25); Chain (1); Disulfide bond (3); Erroneous initiation (1); Glycosylation (6); Helix (23); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (5) TRANSMEM 698 718 Helical. {ECO:0000255}. TOPO_DOM 46 697 Extracellular. {ECO:0000255}.; TOPO_DOM 719 843 Cytoplasmic. {ECO:0000255}. FUNCTION: Cell surface protein involved in cell-cell-interactions via its interactions with neurexin family members. Plays a role in synapse function and synaptic signal transmission, and probably mediates its effects by recruiting and clustering other synaptic proteins. May promote the initial formation of synapses, but is not essential for this. In vitro, triggers the de novo formation of presynaptic structures. May be involved in specification of excitatory synapses. Required to maintain wakefulness quality and normal synchrony of cerebral cortex activity during wakefulness and sleep (PubMed:23716671). {ECO:0000269|PubMed:10892652, ECO:0000269|PubMed:15620359, ECO:0000269|PubMed:16982420, ECO:0000269|PubMed:23716671}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cell junction, synapse {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250}. Note=Enriched in synaptic plasma membranes and clustered in synaptic clefts and postsynaptic densities. Detected at dendritic spines. Colocalized with DLG4/PSD-95 and GRIN1/NMDAR1 (By similarity). {ECO:0000250}. SUBUNIT: Interacts with NRXN1, NRXN2 and NRXN3. Interacts (via its C-terminus) with DLG4/PSD-95 (via PDZ domain 3). Interacts with AIP1, GOPC and PDZRN3 (By similarity). Interacts with NLGN3. {ECO:0000250, ECO:0000269|PubMed:17897391, ECO:0000269|PubMed:18084303}. TISSUE SPECIFICITY: Brain and arteries (at protein level). Expressed in olfactory bulb. Detected in brain. {ECO:0000269|PubMed:11329178, ECO:0000269|PubMed:16982420, ECO:0000269|PubMed:18434543, ECO:0000269|PubMed:19926856}. +O70145 NCF2_MOUSE Neutrophil cytosol factor 2 (NCF-2) (67 kDa neutrophil oxidase factor) (NADPH oxidase activator 2) (Neutrophil NADPH oxidase factor 2) (p67-phox) 525 59,485 Chain (1); Domain (3); Modified residue (3); Repeat (3); Sequence conflict (5) FUNCTION: NCF2, NCF1, and a membrane bound cytochrome b558 are required for activation of the latent NADPH oxidase (necessary for superoxide production). {ECO:0000250|UniProtKB:P19878}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P19878}. SUBUNIT: Component of an NADPH oxidase complex composed of a heterodimer formed by the membrane proteins CYBA and CYBB and the cytosolic subunits NCF1, NCF2 and NCF4. Interacts with NCF4. Interacts (via the C-terminal SH3 domain) with NCF1 (via C-terminus). Interacts with SYTL1 and RAC1. May interact with NOXO1. Interacts with S100A8 and calprotectin (S100A8/9) (By similarity). {ECO:0000250}. DOMAIN: The OPR/PB1 domain mediates the association with NCF4/p40-PHOX. {ECO:0000250}. +Q3UYV9 NCBP1_MOUSE Nuclear cap-binding protein subunit 1 (80 kDa nuclear cap-binding protein) (CBP80) (NCBP 80 kDa subunit) 790 91,927 Chain (1); Coiled coil (1); Cross-link (1); Domain (1); Modified residue (6); Motif (1); Sequence conflict (4) FUNCTION: Component of the cap-binding complex (CBC), which binds cotranscriptionally to the 5'-cap of pre-mRNAs and is involved in various processes such as pre-mRNA splicing, translation regulation, nonsense-mediated mRNA decay, RNA-mediated gene silencing (RNAi) by microRNAs (miRNAs) and mRNA export. The CBC complex is involved in mRNA export from the nucleus via its interaction with ALYREF/THOC4/ALY, leading to the recruitment of the mRNA export machinery to the 5'-end of mRNA and to mRNA export in a 5' to 3' direction through the nuclear pore. The CBC complex is also involved in mediating U snRNA and intronless mRNAs export from the nucleus. The CBC complex is essential for a pioneer round of mRNA translation, before steady state translation when the CBC complex is replaced by cytoplasmic cap-binding protein eIF4E. The pioneer round of mRNA translation mediated by the CBC complex plays a central role in nonsense-mediated mRNA decay (NMD), NMD only taking place in mRNAs bound to the CBC complex, but not on eIF4E-bound mRNAs. The CBC complex enhances NMD in mRNAs containing at least one exon-junction complex (EJC) via its interaction with UPF1, promoting the interaction between UPF1 and UPF2. The CBC complex is also involved in 'failsafe' NMD, which is independent of the EJC complex, while it does not participate in Staufen-mediated mRNA decay (SMD). During cell proliferation, the CBC complex is also involved in microRNAs (miRNAs) biogenesis via its interaction with SRRT/ARS2 and is required for miRNA-mediated RNA interference. The CBC complex also acts as a negative regulator of PARN, thereby acting as an inhibitor of mRNA deadenylation. In the CBC complex, NCBP1/CBP80 does not bind directly capped RNAs (m7GpppG-capped RNA) but is required to stabilize the movement of the N-terminal loop of NCBP2/CBP20 and lock the CBC into a high affinity cap-binding state with the cap structure. Associates with NCBP3 to form an alternative cap-binding complex (CBC) which plays a key role in mRNA export and is particularly important in cellular stress situations such as virus infections. The conventional CBC with NCBP2 binds both small nuclear RNA (snRNA) and messenger (mRNA) and is involved in their export from the nucleus whereas the alternative CBC with NCBP3 does not bind snRNA and associates only with mRNA thereby playing a role only in mRNA export. NCBP1/CBP80 is required for cell growth and viability (By similarity). {ECO:0000250|UniProtKB:Q09161, ECO:0000269|PubMed:19632182}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22767893}. Cytoplasm {ECO:0000250|UniProtKB:Q09161}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. {ECO:0000250|UniProtKB:Q09161}. SUBUNIT: Component of the nuclear cap-binding complex (CBC), a heterodimer composed of NCBP1/CBP80 and NCBP2/CBP20 that interacts with m7GpppG-capped RNA. Found in a U snRNA export complex containing PHAX/RNUXA, NCBP1/CBP80, NCBP2/CBP20, RAN, XPO1 and m7G-capped RNA. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with PHAX/RNUXA, SRRT/ARS2, EIF4G2, IGF2BP1, HNRNPF, HNRNPH1, KIAA0427/CTIF, PARN, DROSHA, UPF1 and ALYREF/THOC4. May interact with EIF4G1; the interaction is however controversial. The large PER complex involved in the repression of transcriptional termination is composed of at least PER2, CDK9, DDX5, DHX9, NCBP1/CBP80 and POLR2A (active). Component of an alternative nuclear cap-binding complex (CBC) composed of NCBP1/CBP80 and NCBP3 (By similarity). Interacts with METTL3 (By similarity). Interacts with ZFC3H1 in a RNase-insensitive manner (By similarity). {ECO:0000250|UniProtKB:Q09161, ECO:0000269|PubMed:10786834, ECO:0000269|PubMed:11333016, ECO:0000269|PubMed:19632182, ECO:0000269|PubMed:22767893}. +P55066 NCAN_MOUSE Neurocan core protein (Chondroitin sulfate proteoglycan 3) 1268 137,200 Chain (1); Disulfide bond (16); Domain (7); Glycosylation (5); Sequence conflict (4); Signal peptide (1) FUNCTION: May modulate neuronal adhesion and neurite growth during development by binding to neural cell adhesion molecules (NG-CAM and N-CAM). Chondroitin sulfate proteoglycan; binds to hyaluronic acid. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. TISSUE SPECIFICITY: Brain. +Q91ZP6 NFIP2_MOUSE NEDD4 family-interacting protein 2 (NEDD4 WW domain-binding protein 5A) (Fragment) 311 33,638 Alternative sequence (2); Chain (1); Erroneous initiation (4); Modified residue (4); Motif (3); Non-terminal residue (1); Region (1); Sequence conflict (4); Topological domain (4); Transmembrane (3) TRANSMEM 207 227 Helical. {ECO:0000255}.; TRANSMEM 233 253 Helical. {ECO:0000255}.; TRANSMEM 263 283 Helical. {ECO:0000255}. TOPO_DOM <1 206 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 228 232 Extracellular. {ECO:0000255}.; TOPO_DOM 254 262 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 284 311 Extracellular. {ECO:0000255}. FUNCTION: Activates HECT domain-containing E3 ubiquitin-protein ligases, including ITCH, NEDD4, NEDD4L, SMURF2, WWP1 and WWP2, and consequently modulates the stability of their targets. As a result, may control many cellular processes. Recruits ITCH, NEDD4 and SMURF2 to endosomal membranes. Negatively regulates KCNH2 potassium channel activity by decreasing its cell-surface expression and interfering with channel maturation through recruitment of NEDD4L to the Golgi apparatus and multivesicular body where it mediates KCNH2 degradation (By similarity). May modulate EGFR signaling (By similarity). Together with NDFIP1, limits the cytokine signaling and expansion of effector Th2 T-cells by promoting degradation of JAK1, probably by ITCH- and NEDD4L-mediated ubiquitination (PubMed:27088444). {ECO:0000250|UniProtKB:Q9NV92, ECO:0000269|PubMed:12050153, ECO:0000269|PubMed:15252135, ECO:0000269|PubMed:27088444}. PTM: Ubiquitinated by NEDD4 and NEDD4L; which does not affect turnover (Probable). Also ubiquitinated by ITCH (By similarity). {ECO:0000250, ECO:0000305}.; PTM: Undergoes transient tyrosine-phosphorylation following EGF stimulation, most probably catalyzed by SRC. Phosphorylation on Tyr-126, Tyr-146 and Tyr-152 are dependent on the phosphorylation on Tyr-142. Also phosphorylated by LYN and FYN (By similarity). {ECO:0000250|UniProtKB:Q9NV92}. SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:12050153}; Multi-pass membrane protein {ECO:0000269|PubMed:12050153}. Golgi apparatus membrane {ECO:0000269|PubMed:15252135}. Endosome, multivesicular body membrane {ECO:0000269|PubMed:15252135}; Multi-pass membrane protein {ECO:0000269|PubMed:15252135}. SUBUNIT: Forms heterodimers with NDFIP1 (By similarity). Interacts with HECT domain-containing E3 ubiquitin-protein ligases, including NEDD4 (PubMed:12050153, PubMed:15252135). Interacts with NEDD4L (PubMed:12050153). When phosphorylated at Tyr-142, interacts with SRC and LYN SH2 domain (By similarity). May thus act as a scaffold that recruits SRC to NDFIP1, enhancing NDFIP1 phosphorylation (By similarity). Interacts with SLC11A2/DMT1 (By similarity). May interact with phosphorylated EGFR (By similarity). Interacts with KCNH2 (By similarity). {ECO:0000250|UniProtKB:Q9NV92, ECO:0000269|PubMed:12050153, ECO:0000269|PubMed:15252135}. DOMAIN: The PPxY motifs are required for E3 ubiquitin-protein ligase activation and for ubiquitination. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in brain, liver, kidney and testis. {ECO:0000269|PubMed:12050153}. +O09118 NET1_MOUSE Netrin-1 604 67,810 Beta strand (22); Chain (1); Disulfide bond (15); Domain (5); Glycosylation (4); Helix (6); Motif (1); Sequence conflict (4); Signal peptide (1); Turn (8) FUNCTION: Netrins control guidance of CNS commissural axons and peripheral motor axons. Its association with either DCC or some UNC5 receptors will lead to axon attraction or repulsion, respectively. It also serve as a survival factor via its association with its receptors which prevent the initiation of apoptosis. Involved in colorectal tumorigenesis by regulating apoptosis (By similarity). {ECO:0000250, ECO:0000269|PubMed:10381568, ECO:0000269|PubMed:8978605}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:7604039}. SUBUNIT: Binds to its receptors; DCC, UNC5A, UNC5B, UNC5C and probably UNC5D (By similarity). Binds to its receptor; DSCAM. {ECO:0000250}. TISSUE SPECIFICITY: In the embryo, widely expressed in the developing nervous system and in mesodermal tissues. {ECO:0000269|PubMed:10381568}. +P63139 NFYB_MOUSE Nuclear transcription factor Y subunit beta (CAAT box DNA-binding protein subunit B) (Nuclear transcription factor Y subunit B) (NF-YB) 207 22,787 Chain (1); Cross-link (1); DNA binding (1); Region (4) FUNCTION: Component of the sequence-specific heterotrimeric transcription factor (NF-Y) which specifically recognizes a 5'-CCAAT-3' box motif found in the promoters of its target genes. NF-Y can function as both an activator and a repressor, depending on its interacting cofactors. PTM: Monoubiquitination at Lys-140 plays an important role in transcriptional activation by allowing the deposition of histone H3 methylations as well as histone H2B monoubiquitination at 'Lys-121'. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Heterotrimeric transcription factor composed of three components, NF-YA, NF-YB and NF-YC. NF-YB and NF-YC must interact and dimerize for NF-YA association and DNA binding. Interacts with C1QBP (By similarity). {ECO:0000250}. DOMAIN: Can be divided into 3 domains: the weakly conserved A domain, the highly conserved B domain thought to be involved in subunit interaction and DNA binding, and the Glu-rich C domain. +Q9JI33 NET4_MOUSE Netrin-4 (Beta-netrin) 628 69,867 Beta strand (21); Chain (1); Disulfide bond (14); Domain (5); Glycosylation (4); Helix (7); Sequence conflict (2); Signal peptide (1); Turn (6) FUNCTION: May play an important role in neural, kidney and vascular development. Promotes neurite elongation from olfactory bulb explants. {ECO:0000269|PubMed:11038171}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane. Note=Major component. SUBUNIT: May form a homodimer. TISSUE SPECIFICITY: Expressed in kidney, liver, heart, ovary, testis, retina, brain, olfactory bulb, and widely expressed in embryo. {ECO:0000269|PubMed:10940631, ECO:0000269|PubMed:11038171}. +B1AY10 NFX1_MOUSE Transcriptional repressor NF-X1 (m-Nfx.1) (EC 2.3.2.-) (Nuclear transcription factor, X box-binding protein 1) 1114 123,811 Alternative sequence (4); Chain (1); Compositional bias (1); Domain (1); Frameshift (1); Modified residue (7); Region (1); Sequence conflict (5); Zinc finger (9) FUNCTION: Binds to the X-box motif of MHC class II genes and represses their expression. May play an important role in regulating the duration of an inflammatory response by limiting the period in which MHC class II molecules are induced by interferon-gamma. Together with PABPC1 or PABPC4, acts as a coactivator for TERT expression. Mediates E2-dependent ubiquitination. {ECO:0000269|PubMed:12047746}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with PABPC1 and PABPC4. {ECO:0000250}. DOMAIN: The RING-type zinc finger domain interacts with an ubiquitin-conjugating enzyme (E2) and facilitates ubiquitination. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in thymus. {ECO:0000269|PubMed:12047746}. +Q8CHT1 NGEF_MOUSE Ephexin-1 (Eph-interacting exchange protein) (Neuronal guanine nucleotide exchange factor) 710 82,199 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (3); Erroneous initiation (1); Frameshift (1); Modified residue (1); Mutagenesis (1); Region (1); Sequence conflict (1) FUNCTION: Acts as a guanine nucleotide exchange factor (GEF) which differentially activates the GTPases RHOA, RAC1 and CDC42. Plays a role in axon guidance regulating ephrin-induced growth cone collapse and dendritic spine morphogenesis. Upon activation by ephrin through EPHA4, the GEF activity switches toward RHOA resulting in its activation. Activated RHOA promotes cone retraction at the expense of RAC1- and CDC42-stimulated growth cone extension. {ECO:0000269|PubMed:11336673, ECO:0000269|PubMed:15848799, ECO:0000269|PubMed:17143272}. PTM: Src-dependent phosphorylation at Tyr-177 upon EPHA4 activation increases the guanine exchange factor activity toward RHOA. Phosphorylation by CDK5 upon EPHA4 activation by EFNA1 may regulate dendritic spine morphogenesis. {ECO:0000269|PubMed:15254079, ECO:0000269|PubMed:17143272}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}. Cell projection, growth cone {ECO:0000250}. Note=Associated with membranes. Localizes to axonal growth cones (By similarity). {ECO:0000250}. SUBUNIT: Interacts with CDK5R1 and EPHA4; activated by EPHA4 through the CDK5 kinase. {ECO:0000269|PubMed:11336673, ECO:0000269|PubMed:17143272}. DOMAIN: The DH domain and the PH domain are both required to mediate interaction with EPHA4. TISSUE SPECIFICITY: Highly expressed in brain and to a lower extent in eye. {ECO:0000269|PubMed:10777665}. +Q9JKL1 PKR1_MOUSE Prokineticin receptor 1 (PK-R1) (G-protein coupled receptor 73) 393 44,597 Chain (1); Disulfide bond (1); Glycosylation (1); Sequence conflict (2); Topological domain (8); Transmembrane (7) TRANSMEM 63 83 Helical; Name=1. {ECO:0000255}.; TRANSMEM 99 119 Helical; Name=2. {ECO:0000255}.; TRANSMEM 147 167 Helical; Name=3. {ECO:0000255}.; TRANSMEM 180 200 Helical; Name=4. {ECO:0000255}.; TRANSMEM 233 253 Helical; Name=5. {ECO:0000255}.; TRANSMEM 283 303 Helical; Name=6. {ECO:0000255}.; TRANSMEM 323 343 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 62 Extracellular. {ECO:0000255}.; TOPO_DOM 84 98 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 120 146 Extracellular. {ECO:0000255}.; TOPO_DOM 168 179 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 201 232 Extracellular. {ECO:0000255}.; TOPO_DOM 254 282 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 304 322 Extracellular. {ECO:0000255}.; TOPO_DOM 344 393 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for prokineticin 1. Exclusively coupled to the G(q) subclass of heteromeric G proteins. Activation leads to mobilization of calcium, stimulation of phosphoinositide turnover and activation of p44/p42 mitogen-activated protein kinase. May play a role during early pregnancy (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed at high levels in the heart, skeletal muscle and pancreas. Expressed at lower levels in the brain, lung, liver and kidney. +Q02780 NFIA_MOUSE Nuclear factor 1 A-type (NF1-A) (Nuclear factor 1/A) (CCAAT-box-binding transcription factor) (CTF) (Nuclear factor I/A) (NF-I/A) (NFI-A) (TGGCA-binding protein) 532 58,553 Alternative sequence (8); Chain (1); DNA binding (1); Modified residue (11) FUNCTION: Recognizes and binds the palindromic sequence 5'-TTGGCNNNNNGCCAA-3' present in viral and cellular promoters and in the origin of replication of adenovirus type 2. These proteins are individually capable of activating transcription and replication. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Binds DNA as a homodimer. +Q9CWV6 PKRI1_MOUSE PRKR-interacting protein 1 (Protein C114) 186 21,492 Chain (1); Coiled coil (1); Erroneous initiation (1); Region (3); Sequence conflict (3) FUNCTION: Binds double-stranded RNA. Inhibits EIF2AK2 kinase activity. {ECO:0000269|PubMed:12679338}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12679338}. SUBUNIT: Interacts with EIF2AK2. {ECO:0000269|PubMed:12679338}. TISSUE SPECIFICITY: Broadly expressed, with highest levels in liver, kidney, brain and heart. {ECO:0000269|PubMed:12679338}. +P97863 NFIB_MOUSE Nuclear factor 1 B-type (NF1-B) (Nuclear factor 1/B) (CCAAT-box-binding transcription factor) (CTF) (Nuclear factor I/B) (NF-I/B) (NFI-B) (TGGCA-binding protein) 570 63,507 Alternative sequence (3); Chain (1); DNA binding (1); Modified residue (9); Natural variant (1) FUNCTION: Recognizes and binds the palindromic sequence 5'-TTGGCNNNNNGCCAA-3' present in viral and cellular promoters and in the origin of replication of adenovirus type 2. These proteins are individually capable of activating transcription and replication. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Binds DNA as a homodimer. TISSUE SPECIFICITY: Highest expression in lung, skeletal muscle and heart. Lower levels in liver, kidney and brain. Very low levels in testis and spleen. +Q99LJ8 NGBR_MOUSE Dehydrodolichyl diphosphate synthase complex subunit Nus1 (EC 2.5.1.87) (Nogo-B receptor) (NgBR) (Nuclear undecaprenyl pyrophosphate synthase 1 homolog) 297 33,485 Chain (1); Frameshift (2); Glycosylation (2); Motif (1); Sequence conflict (3); Transmembrane (3) TRANSMEM 7 26 Helical; Name=1. {ECO:0000250|UniProtKB:Q96E22}.; TRANSMEM 40 56 Helical; Name=2. {ECO:0000250|UniProtKB:Q96E22}.; TRANSMEM 121 139 Helical; Name=3. {ECO:0000250|UniProtKB:Q96E22}. Protein modification; protein glycosylation. Lipid metabolism. FUNCTION: With DHDDS, forms the dehydrodolichyl diphosphate synthase (DDS) complex, an essential component of the dolichol monophosphate (Dol-P) biosynthetic machinery. Both subunits contribute to enzymatic activity, i.e. condensation of multiple copies of isopentenyl pyrophosphate (IPP) to farnesyl pyrophosphate (FPP) to produce dehydrodolichyl diphosphate (Dedol-PP), a precursor of dolichol phosphate which is utilized as a sugar carrier in protein glycosylation in the endoplasmic reticulum (ER). Regulates the glycosylation and stability of nascent NPC2, thereby promoting trafficking of LDL-derived cholesterol. Acts as a specific receptor for the N-terminus of Nogo-B, a neural and cardiovascular regulator. {ECO:0000250|UniProtKB:Q96E22}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q96E22}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q96E22}. Note=Colocalizes with Nogo-B during VEGF and wound healing angiogenesis. {ECO:0000250|UniProtKB:Q96E22}. SUBUNIT: Forms an active dehydrodolichyl diphosphate synthase complex with DHDDS. Interacts with NPC2. {ECO:0000250|UniProtKB:Q96E22}. TISSUE SPECIFICITY: Highly expressed in heart, liver, kidney and pancreas. {ECO:0000269|PubMed:16835300}. +Q9ER97 NGB_MOUSE Neuroglobin 151 17,037 Beta strand (1); Chain (1); Helix (11); Metal binding (2); Mutagenesis (1); Region (1); Turn (1) FUNCTION: Involved in oxygen transport in the brain. Hexacoordinate globin, displaying competitive binding of oxygen or the distal His residue to the iron atom. Not capable of penetrating cell membranes. The deoxygenated form exhibits nitrite reductase activity inhibiting cellular respiration via NO-binding to cytochrome c oxidase. Involved in neuroprotection during oxidative stress. May exert its anti-apoptotic activity by acting to reset the trigger level of mitochondrial cytochrome c release necessary to commit the cells to apoptosis. {ECO:0000269|PubMed:11473111, ECO:0000269|PubMed:11473128}. PTM: A redox disulfide bond regulates the heme pocket coordination and the rate of nitrite reduction to NO. {ECO:0000250}.; PTM: Phosphorylated in vitro by ERK1, ERK2 and PKA, and in vivo during hypoxia. Phosphorylation increases nitrite reductase activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Perikaryon {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:22659017}. Mitochondrion {ECO:0000269|PubMed:22659017}. SUBUNIT: Monomer. Homodimer and homotetramer; disulfide-linked (Probable). Interacts with 14-3-3 (By similarity). {ECO:0000250, ECO:0000305}. TISSUE SPECIFICITY: Predominantly expressed in brain. +Q08EJ0 PL8L1_MOUSE PLAC8-like protein 1 177 20,115 Chain (1); Sequence conflict (1) +Q8BZW8 NHLC2_MOUSE NHL repeat-containing protein 2 725 78,430 Chain (1); Domain (1); Repeat (6) FUNCTION: Required for normal embryonic development. {ECO:0000269|PubMed:29423877, ECO:0000269|Ref.4}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8NBF2}. SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q8NBF2}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:29423877}. +Q8CCH2 NHLC3_MOUSE NHL repeat-containing protein 3 347 38,195 Chain (1); Glycosylation (3); Repeat (4); Signal peptide (1) +Q9JI83 PLAC1_MOUSE Placenta-specific protein 1 (EPCS26) 173 19,626 Chain (1); Sequence conflict (3); Signal peptide (1) FUNCTION: May play a role in placental development. {ECO:0000269|PubMed:10995572}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Expressed in placenta. {ECO:0000269|PubMed:10995572}. +Q9JI48 PLAC8_MOUSE Placenta-specific gene 8 protein (Onzin) (Protein C15) 112 12,353 Chain (1) +Q8K262 PLAC9_MOUSE Placenta-specific protein 9 108 11,275 Chain (1); Coiled coil (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Highly expressed in placenta, and weakly in ovary, testis, and lung. {ECO:0000269|PubMed:12758124}. +Q9QYE0 PLAG1_MOUSE Zinc finger protein PLAG1 (Pleiomorphic adenoma gene 1 protein) 499 55,579 Chain (1); Compositional bias (1); Cross-link (2); Erroneous initiation (1); Motif (1); Region (5); Sequence conflict (2); Zinc finger (7) FUNCTION: Transcription factor whose activation results in up-regulation of target genes, such as IGFII, leading to uncontrolled cell proliferation: when overexpressed in cultured cells, higher proliferation rate and transformation are observed. Other target genes such as CRLF1, CRABP2, CRIP2, PIGF are strongly induced in cells with PLAG1 induction. Proto-oncogene whose ectopic expression can trigger the development of pleomorphic adenomas of the salivary gland and lipoblastomas. Cooperates with CBFB-MYH11. {ECO:0000269|PubMed:15044690, ECO:0000269|PubMed:15930271, ECO:0000269|PubMed:16108035}. PTM: Sumoylated with SUMO1; which inhibits transcriptional activity, but does not affect nuclear localization. Blockers of sumoylation pathway such as SENP3 and inactive UBE2I increases transcriptional capacity. Sumoylation is increased in the presence of PIAS1 (By similarity). {ECO:0000250}.; PTM: Acetylated by lysine acetyltransferase EP300; which activates transcriptional capacity. Lysine residues that are sumoylated also seem to be target for acetylation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Note=Strong nucleolar localization when sumoylation is inhibited. {ECO:0000250}. SUBUNIT: Interacts with KPNA2, which escorts protein to the nucleus via interaction with nuclear localization signal. Interacts with E3 SUMO-protein ligase PIAS1, PIAS2 and PIAS4 (By similarity). {ECO:0000250}. DOMAIN: C2H2-type zinc fingers 3 interacts with DNA-binding site G-clusterinc fingers. C2H2-type zinc fingers 6 and 7 interact with DNA-binding site core sequence (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in heart, spleen, lung, kidney, brain, testis and epididymis but not in salivary glands. {ECO:0000269|PubMed:16193498}. +P10493 NID1_MOUSE Nidogen-1 (NID-1) (Entactin) 1245 136,538 Beta strand (40); Chain (1); Disulfide bond (22); Domain (9); Glycosylation (9); Helix (7); Modified residue (2); Motif (1); Repeat (4); Sequence conflict (3); Signal peptide (1); Site (3); Turn (11) FUNCTION: Sulfated glycoprotein widely distributed in basement membranes and tightly associated with laminin. Also binds to collagen IV and perlecan. It probably has a role in cell-extracellular matrix interactions. PTM: N- and O-glycosylated. {ECO:0000269|PubMed:8326911}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane. SUBUNIT: Interacts with FBLN1 and LGALS3BP. Interacts with PLXDC1. {ECO:0000269|PubMed:11589703, ECO:0000269|PubMed:16574105, ECO:0000269|PubMed:9299350, ECO:0000269|PubMed:9501082}. +P70441 NHRF1_MOUSE Na(+)/H(+) exchange regulatory cofactor NHE-RF1 (NHERF-1) (Ezrin-radixin-moesin-binding phosphoprotein 50) (EBP50) (Regulatory cofactor of Na(+)/H(+) exchanger) (Sodium-hydrogen exchanger regulatory factor 1) (Solute carrier family 9 isoform A3 regulatory factor 1) 355 38,600 Alternative sequence (2); Chain (1); Domain (2); Initiator methionine (1); Modified residue (11) FUNCTION: Scaffold protein that connects plasma membrane proteins with members of the ezrin/moesin/radixin family and thereby helps to link them to the actin cytoskeleton and to regulate their surface expression. Necessary for recycling of internalized ADRB2. Was first known to play a role in the regulation of the activity and subcellular location of SLC9A3. Necessary for cAMP-mediated phosphorylation and inhibition of SLC9A3. May enhance Wnt signaling (By similarity). May participate in HTR4 targeting to microvilli. Involved in the regulation of phosphate reabsorption in the renal proximal tubules (By similarity). Involved in sperm capacitation. May participate in the regulation of the chloride and bicarbonate homeostasis in spermatozoa. {ECO:0000250, ECO:0000269|PubMed:21976599, ECO:0000269|PubMed:9560162}. SUBCELLULAR LOCATION: Cytoplasm. Apical cell membrane. Cell projection, filopodium {ECO:0000250}. Cell projection, ruffle {ECO:0000250}. Cell projection, microvillus {ECO:0000250}. Endomembrane system {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Colocalizes with actin in microvilli-rich apical regions of the syncytiotrophoblast. Present in lipid rafts of T-cells (By similarity). Translocates from the cytoplasm to the apical cell membrane in a PODXL-dependent manner. Colocalizes with CFTR at the midpiece of sperm tail. {ECO:0000250}. SUBUNIT: Homodimer, and heterodimer with SLC9A3R2. Binds the N-termini of EZR, RDX and MSN. Binds the C-termini of PDGFRA, PDGFRB, ADRB2 and NOS2. Binds ARHGAP17, EPI64, RACK1, OPRK1, GNAQ, CTNNB1, PLCB3 and CLCN3. Forms a complex with CFTR and SLC4A7. Forms a complex with SLC4A7 and ATP6V1B1 (By similarity). Binds PDZK1. Binds the C-terminus of PAG1. In resting T-cells, part of a PAG1-SLC9A3R1-MSN complex which is disrupted upon TCR activation. Directly interacts with HTR4. Interacts with MCC (By similarity). Interacts with TRPC4 (via the PDZ-binding domain) (By similarity). Interacts (via the PDZ 1 domain) with PODXL (via the C-terminal PDZ-binding motif DTHL); interaction is not detected in glomerular epithelium cells (By similarity). Interacts (via the PDZ 1 domain) with PODXL (via the C-terminal PDZ-binding motif DTHL); the interaction take place early in the secretory pathway and is necessary for its apical membrane sorting (By similarity). Interacts with SLC34A1 (By similarity). Interacts with CFTR, SLC26A3 and SLC26A6. {ECO:0000250, ECO:0000269|PubMed:11777944, ECO:0000269|PubMed:14531806, ECO:0000269|PubMed:15466885, ECO:0000269|PubMed:21976599, ECO:0000269|PubMed:9560162}. TISSUE SPECIFICITY: Expressed in spermatogenic cells. {ECO:0000269|PubMed:21976599}. +Q9QXS1 PLEC_MOUSE Plectin (PCN) (PLTN) (Plectin-1) (Plectin-6) 4691 534,188 Alternative sequence (18); Beta strand (1); Chain (1); Coiled coil (2); Domain (3); Helix (15); Modified residue (48); Region (6); Repeat (37); Sequence conflict (3); Turn (2) FUNCTION: Interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. May be involved not only in the cross-linking and stabilization of cytoskeletal intermediate filaments network, but also in the regulation of their dynamics. PTM: Phosphorylated by CDK1; regulates dissociation from intermediate filaments during mitosis. Isoform PLEC-1A is phosphorylated on Ser-21. Isoform PLEC-1A is phosphorylated on Tyr-26. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell junction, hemidesmosome {ECO:0000250}. SUBUNIT: Homodimer or homotetramer (By similarity). Interacts (via actin-binding domain) with SYNE3 (PubMed:16330710). Interacts (via calponin-homology (CH) 1 domain) with VIM (via rod region) (PubMed:15128297). Interacts (via N-terminus) with DST isoform 2 (via N-terminus) (PubMed:19932097). Interacts with FER (PubMed:12200133). Interacts with TOR1A (PubMed:18827015). Interacts with ANK3 (By similarity). Identified in complexes that contain VIM, EZR, AHNAK, BFSP1, BFSP2, ANK2, PLEC, PRX and spectrin (PubMed:21745462). {ECO:0000250, ECO:0000250|UniProtKB:P30427, ECO:0000269|PubMed:12200133, ECO:0000269|PubMed:15128297, ECO:0000269|PubMed:16330710, ECO:0000269|PubMed:18827015, ECO:0000269|PubMed:19932097, ECO:0000269|PubMed:21745462}. DOMAIN: The N-terminus interacts with actin, the C-terminus with vimentin, desmin, GFAP, cytokeratins, lamin B; whereas both the N- and the C-terminus can bind integrin beta-4. TISSUE SPECIFICITY: Detected in eye lens fiber cells (at protein level) (PubMed:21745462). Expressed at high levels in lung, brain, small intestine, muscle, heart and skin with lower levels found in kidney, liver, uterus, spleen and salivary gland (PubMed:10556294). {ECO:0000269|PubMed:10556294, ECO:0000269|PubMed:21745462}. +Q9JL89 NINJ2_MOUSE Ninjurin-2 (Nerve injury-induced protein 2) 143 15,994 Chain (1); Topological domain (3); Transmembrane (2) TRANSMEM 71 91 Helical. {ECO:0000255}.; TRANSMEM 108 128 Helical. {ECO:0000255}. TOPO_DOM 1 70 Extracellular. {ECO:0000255}.; TOPO_DOM 92 107 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 129 143 Extracellular. {ECO:0000255}. FUNCTION: Homophilic cell adhesion molecule that promotes axonal growth. May play a role in nerve regeneration and in the formation and function of other tissues. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. +O70584 NKX28_MOUSE Homeobox protein Nkx-2.8 (Homeobox protein NK-2 homolog H) (Homeobox protein Nkx-2.9) 235 26,133 Chain (1); DNA binding (1); Sequence conflict (4) FUNCTION: Possible role in the specification of a distinct subset of neurons. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: Prominent expression in ventral brain and neural tube structures. +Q9Z126 PLF4_MOUSE Platelet factor 4 (PF-4) (C-X-C motif chemokine 4) 105 11,243 Chain (1); Disulfide bond (2); Glycosylation (1); Modified residue (1); Region (1); Signal peptide (1) FUNCTION: Released during platelet aggregation. Neutralizes the anticoagulant effect of heparin because it binds more strongly to heparin than to the chondroitin-4-sulfate chains of the carrier molecule. Chemotactic for neutrophils and monocytes. Inhibits endothelial cell proliferation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Homotetramer. {ECO:0000250}. +A1Z198 NL1B2_MOUSE NACHT, LRR and PYD domains-containing protein 1b allele 2 1177 134,163 Alternative sequence (3); Chain (1); Domain (3); Nucleotide binding (1); Repeat (2); Site (1) FUNCTION: As the sensor component of the NLRP1 inflammasome, plays a crucial role in innate immunity and inflammation. In response to pathogens and other damage-associated signals, initiates the formation of the inflammasome polymeric complex, made of Nlrp1b, CASP1, and possibly PYCARD. Recruitment of proCASP1 to the inflammasome promotes its activation and CASP1-catalyzed IL1B and IL18 maturation and secretion in the extracellular milieu. Activation of NLRP1 inflammasome is also required for HMGB1 secretion. The active cytokines and HMGB1 stimulate inflammatory responses. Inflammasomes can also induce pyroptosis, an inflammatory form of programmed cell death (By similarity). May be activated by muramyl dipeptide (MDP), a fragment of bacterial peptidoglycan, in a NOD2-dependent manner (PubMed:18511561). Might be activated by Toxoplasma gondii, although at a lower extent than allele 1 (PubMed:24218483). Contrary to Nlrp1b allele 1, allele 2 is not activated by Bacillus anthracis lethal toxin (PubMed:16429160, PubMed:21170303, PubMed:24492532). {ECO:0000250|UniProtKB:Q2LKW6, ECO:0000269|PubMed:16429160, ECO:0000269|PubMed:18511561, ECO:0000269|PubMed:21170303, ECO:0000269|PubMed:24492532}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9C000}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9C000}. Inflammasome {ECO:0000250|UniProtKB:Q2LKW6}. SUBUNIT: Sensor component of NLRP1 inflammasomes. Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other damage-associated signals and play critical roles in innate immunity and inflammation. Classical inflammasomes consist of a signal sensor component, an adapter (ASC/PYCARD), which recruits an effector proinflammatory caspase (CASP1 and possibly CASP4/CASP11). CASP1 filament formation increases local enzyme concentration, resulting in trans-autocleavage and activation. Active CASP1 then processes IL1B and IL18 precursors, leading to the release of mature cytokines in the extracellular milieu and inflammatory response. In NLRP1 inflammasome, the role of PYCARD is not clear. Following activation, Nlrp1b may directly interact with CASP1 (through the CARD domain) to form a functional inflammasome. Hence PYCARD may not be necessary for NLRP1 and CASP1 interaction, but is required for speck formation and full inflammasome activity (By similarity). Homomer (By similarity). Interacts (via LRR repeats) with BCL2 and BCL2L1 (via the loop between motifs BH4 and BH3); these interactions reduce NLRP1 inflammasome-induced CASP1 activation and IL1B release, possibly by impairing NLRP1 interaction with PYCARD. Interacts with NOD2; this interaction may increase IL1B release. Interacts with EIF2AK2/PKR; this interaction requires EIF2AK2 activity, is accompanied by EIF2AK2 autophosphorylation and promotes inflammasome assembly in response to danger-associated signals. Interacts with MEFV; this interaction targets NLRP1 to degradation by autophagy, hence preventing excessive IL1B- and IL18-mediated inflammation (By similarity). {ECO:0000250|UniProtKB:Q2LKW6, ECO:0000250|UniProtKB:Q9C000}. DOMAIN: The CARD domain is involved in the interaction with PYCARD, CASP1 and CASP4/CASP11. {ECO:0000250|UniProtKB:Q9C000}.; DOMAIN: The leucine-rich repeat (LRR) domain may be involved in autoinhibition in the absence of activating signal, possibly through intramolecular interaction with the NACHT domain. {ECO:0000250|UniProtKB:Q2LKW6}.; DOMAIN: The FIIND (domain with function to find) region is involved in homomerization, but not in CASP1-binding. In allele 1, autocatalytic cleavage in this region occurs constitutively, prior to activation signals, and is required for inflammasome activity (IL1B release), possibly by facilitating CASP1 binding. Both N- and C-terminal fragments remain associated (By similarity). It is not known whether this modification occurs in allele 2 (Probable). {ECO:0000250|UniProtKB:Q2LKW6, ECO:0000305}. TISSUE SPECIFICITY: Widely expressed, including in macrophages and, at lower levels, in the peripheral nervous system, including in the sciatic nerve, Schwann cells, sensory neurons and motor neurons. {ECO:0000269|PubMed:16429160, ECO:0000269|PubMed:23506131, ECO:0000269|PubMed:26253422}. +Q0GKD5 NL1B5_MOUSE NACHT, LRR and PYD domains-containing protein 1b allele 5 1196 136,518 Alternative sequence (1); Chain (1); Domain (3); Nucleotide binding (1); Repeat (2); Site (2) FUNCTION: As the sensor component of the NLRP1 inflammasome, plays a crucial role in innate immunity and inflammation. In response to pathogens and other damage-associated signals, initiates the formation of the inflammasome polymeric complex, made of Nlrp1b, CASP1, and possibly PYCARD. Recruitment of proCASP1 to the inflammasome promotes its activation and CASP1-catalyzed IL1B and IL18 maturation and secretion in the extracellular milieu. Activation of NLRP1 inflammasome is also required for HMGB1 secretion. The active cytokines and HMGB1 stimulate inflammatory responses. Inflammasomes can also induce pyroptosis, an inflammatory form of programmed cell death. Activated by cleavage by Bacillus anthracis lethal toxin (LT) endopeptidase component. Activated by metabolic inhibitors, such as 2-deoxy-D-glucose and sodium azide (PubMed:24935976). Not activated by muramyl dipeptide, nor by full-length bacterial peptidoglycan. Primary mediator of macrophage susceptibility to LT. In response to Bacillus anthracis infection, macrophages and dendritic cells release IL1B and undergo pyroptosis, an inflammatory form of programmed cell death. This early inflammatory response to the toxin increases resistance to infection by B. anthracis spores. Binds ATP. {ECO:0000250|UniProtKB:Q2LKW6, ECO:0000250|UniProtKB:Q9C000, ECO:0000269|PubMed:16429160, ECO:0000269|PubMed:24935976}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9C000}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9C000}. Inflammasome {ECO:0000250|UniProtKB:Q2LKW6}. SUBUNIT: Sensor component of NLRP1 inflammasomes. Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other damage-associated signals and play critical roles in innate immunity and inflammation. Classical inflammasomes consist of a signal sensor component, an adapter (ASC/PYCARD), which recruits an effector proinflammatory caspase (CASP1 and possibly CASP4/CASP11). CASP1 filament formation increases local enzyme concentration, resulting in trans-autocleavage and activation. Active CASP1 then processes IL1B and IL18 precursors, leading to the release of mature cytokines in the extracellular milieu and inflammatory response. In NLRP1 inflammasome, the role of PYCARD is not clear. Following activation, Nlrp1b may directly interact with CASP1 (through the CARD domain) to form a functional inflammasome. Hence PYCARD may not be necessary for NLRP1 and CASP1 interaction, but is required for speck formation and full inflammasome activity (By similarity). Homomer (By similarity). Interacts (via LRR repeats) with BCL2 and BCL2L1 (via the loop between motifs BH4 and BH3); these interactions reduce NLRP1 inflammasome-induced CASP1 activation and IL1B release, possibly by impairing NLRP1 interaction with PYCARD (By similarity). Interacts with NOD2; this interaction may lead to increased IL1B release (By similarity). Interacts with EIF2AK2/PKR; this interaction requires EIF2AK2 activity, is accompanied by EIF2AK2 autophosphorylation and promotes inflammasome assembly in response to Bacillus anthracis lethal toxin (By similarity). Interacts with MEFV; this interaction targets NLRP1 to degradation by autophagy, hence preventing excessive IL1B- and IL18-mediated inflammation (By similarity). {ECO:0000250|UniProtKB:Q2LKW6, ECO:0000250|UniProtKB:Q9C000}. DOMAIN: The CARD domain is involved in the interaction with PYCARD, CASP1 and CASP4/CASP11. {ECO:0000250|UniProtKB:Q9C000}.; DOMAIN: The leucine-rich repeat (LRR) domain may be involved in autoinhibition in the absence of activating signal, possibly through intramolecular interaction with the NACHT domain. {ECO:0000250|UniProtKB:Q2LKW6}.; DOMAIN: The FIIND (domain with function to find) region is involved in homomerization, but not in CASP1-binding. Autocatalytic cleavage in this region occurs constitutively, prior to activation signals, and is required for inflammasome activity (IL1B release), possibly by facilitating CASP1 binding. Both N- and C-terminal fragments remain associated. {ECO:0000250|UniProtKB:Q2LKW6}. TISSUE SPECIFICITY: Expressed in macrophages. {ECO:0000269|PubMed:16429160, ECO:0000269|PubMed:23506131}. +Q0VF94 NKPD1_MOUSE NTPase KAP family P-loop domain-containing protein 1 599 66,831 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (1); Transmembrane (3) TRANSMEM 25 45 Helical. {ECO:0000255}.; TRANSMEM 119 139 Helical. {ECO:0000255}.; TRANSMEM 156 176 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8BY02 NKRF_MOUSE NF-kappa-B-repressing factor (NFkB-repressing factor) (Transcription factor NRF) 690 77,739 Chain (1); Cross-link (4); DNA binding (1); Domain (2); Modified residue (1); Motif (1); Region (1); Sequence conflict (1) FUNCTION: Interacts with a specific negative regulatory element (NRE) 5'-AATTCCTCTGA-3' to mediate transcriptional repression of certain NK-kappa-B responsive genes. Involved in the constitutive silencing of the interferon beta promoter, independently of the virus-induced signals, and in the inhibition of the basal and cytokine-induced iNOS promoter activity. Also involved in the regulation of IL-8 transcription (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. SUBUNIT: Interacts with NF-kappa-B. Interacts with XRN2. {ECO:0000250|UniProtKB:O15226}. +B2RPU2 PLHD1_MOUSE Pleckstrin homology domain-containing family D member 1 (PH domain-containing family D member 1) 505 59,097 Chain (1); Coiled coil (1); Domain (1); Modified residue (1) +P42586 NKX22_MOUSE Homeobox protein Nkx-2.2 (Homeobox protein NK-2 homolog B) 273 30,126 Chain (1); DNA binding (1); Mutagenesis (1) FUNCTION: Transcriptional activator involved in the development of insulin-producting beta cells in the endocrine pancreas (PubMed:11076772). May also be involved in specifying diencephalic neuromeric boundaries, and in controlling the expression of genes that play a role in axonal guidance. Binds to elements within the NEUROD1 promoter (PubMed:19759004). {ECO:0000269|PubMed:11076772, ECO:0000269|PubMed:19759004}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:14573534}. SUBUNIT: Interacts with OLIG2. {ECO:0000269|PubMed:14573534}. DOMAIN: The homeodomain is essential for interaction with OLIG2. TISSUE SPECIFICITY: Expressed in restricted areas of the developing CNS: the hindbrain and forebrain, and pancreas. +Q8BZF2 NIPA4_MOUSE Magnesium transporter NIPA4 (Ichthyin) (NIPA-like protein 4) (Non-imprinted in Prader-Willi/Angelman syndrome region protein 4 homolog) 406 44,059 Chain (1); Glycosylation (4); Topological domain (9); Transmembrane (8) TRANSMEM 58 78 Helical. {ECO:0000255}.; TRANSMEM 127 147 Helical. {ECO:0000255}.; TRANSMEM 156 176 Helical. {ECO:0000255}.; TRANSMEM 198 218 Helical. {ECO:0000255}.; TRANSMEM 226 246 Helical. {ECO:0000255}.; TRANSMEM 264 284 Helical. {ECO:0000255}.; TRANSMEM 296 316 Helical. {ECO:0000255}.; TRANSMEM 327 347 Helical. {ECO:0000255}. TOPO_DOM 1 57 Extracellular. {ECO:0000255}.; TOPO_DOM 79 126 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 148 155 Extracellular. {ECO:0000255}.; TOPO_DOM 177 197 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 219 225 Extracellular. {ECO:0000255}.; TOPO_DOM 247 263 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 285 295 Extracellular. {ECO:0000255}.; TOPO_DOM 317 326 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 348 406 Extracellular. {ECO:0000255}. FUNCTION: Acts as a Mg(2+) transporter. Can also transport other divalent cations such as Ba(2+), Mn(2+), Sr(2+) and Co(2+) but to a much less extent than Mg(2+). May be a receptor for ligands (trioxilins A3 and B3) from the hepoxilin pathway (By similarity). {ECO:0000250, ECO:0000269|PubMed:18667602}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q07832 PLK1_MOUSE Serine/threonine-protein kinase PLK1 (EC 2.7.11.21) (Polo-like kinase 1) (PLK-1) (Serine/threonine-protein kinase 13) (STPK13) 603 68,301 Active site (1); Beta strand (14); Binding site (3); Chain (1); Cross-link (3); Domain (3); Helix (7); Modified residue (9); Motif (1); Mutagenesis (6); Nucleotide binding (2); Region (3); Sequence conflict (8); Turn (4) FUNCTION: Serine/threonine-protein kinase that performs several important functions throughout M phase of the cell cycle, including the regulation of centrosome maturation and spindle assembly, the removal of cohesins from chromosome arms, the inactivation of anaphase-promoting complex/cyclosome (APC/C) inhibitors, and the regulation of mitotic exit and cytokinesis. Polo-like kinase proteins acts by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates BORA, BUB1B/BUBR1, CCNB1, CDC25C, CEP55, ECT2, ERCC6L, FBXO5/EMI1, FOXM1, KIF20A/MKLP2, CENPU, NEDD1, NINL, NPM1, NUDC, PKMYT1/MYT1, KIZ, PPP1R12A/MYPT1, PRC1, RACGAP1/CYK4, SGO1, STAG2/SA2, TEX14, TOPORS, p73/TP73, TPT1, WEE1 and HNRNPU. Plays a key role in centrosome functions and the assembly of bipolar spindles by phosphorylating KIZ, NEDD1 and NINL. NEDD1 phosphorylation promotes subsequent targeting of the gamma-tubulin ring complex (gTuRC) to the centrosome, an important step for spindle formation. Phosphorylation of NINL component of the centrosome leads to NINL dissociation from other centrosomal proteins. Involved in mitosis exit and cytokinesis by phosphorylating CEP55, ECT2, KIF20A/MKLP2, CENPU, PRC1 and RACGAP1. Recruited at the central spindle by phosphorylating and docking PRC1 and KIF20A/MKLP2; creates its own docking sites on PRC1 and KIF20A/MKLP2 by mediating phosphorylation of sites subsequently recognized by the POLO box domains. Phosphorylates RACGAP1, thereby creating a docking site for the Rho GTP exchange factor ECT2 that is essential for the cleavage furrow formation. Promotes the central spindle recruitment of ECT2. Plays a central role in G2/M transition of mitotic cell cycle by phosphorylating CCNB1, CDC25C, FOXM1, CENPU, PKMYT1/MYT1, PPP1R12A/MYPT1 and WEE1. Part of a regulatory circuit that promotes the activation of CDK1 by phosphorylating the positive regulator CDC25C and inhibiting the negative regulators WEE1 and PKMYT1/MYT1. Also acts by mediating phosphorylation of cyclin-B1 (CCNB1) on centrosomes in prophase. Phosphorylates FOXM1, a key mitotic transcription regulator, leading to enhance FOXM1 transcriptional activity. Involved in kinetochore functions and sister chromatid cohesion by phosphorylating BUB1B/BUBR1, FBXO5/EMI1 and STAG2/SA2. PLK1 is high on non-attached kinetochores suggesting a role of PLK1 in kinetochore attachment or in spindle assembly checkpoint (SAC) regulation. Required for kinetochore localization of BUB1B. Regulates the dissociation of cohesin from chromosomes by phosphorylating cohesin subunits such as STAG2/SA2. Phosphorylates SGO1: required for spindle pole localization of isoform 3 of SGO1 and plays a role in regulating its centriole cohesion function. Mediates phosphorylation of FBXO5/EMI1, a negative regulator of the APC/C complex during prophase, leading to FBXO5/EMI1 ubiquitination and degradation by the proteasome. Acts as a negative regulator of p53 family members: phosphorylates TOPORS, leading to inhibit the sumoylation of p53/TP53 and simultaneously enhance the ubiquitination and subsequent degradation of p53/TP53. Phosphorylates the transactivation domain of the transcription factor p73/TP73, leading to inhibit p73/TP73-mediated transcriptional activation and pro-apoptotic functions. Phosphorylates BORA, and thereby promotes the degradation of BORA. Contributes to the regulation of AURKA function. Also required for recovery after DNA damage checkpoint and entry into mitosis.Phosphorylates MISP, leading to stabilization of cortical and astral microtubule attachments required for proper spindle positioning (By similarity). Together with MEIKIN, acts as a regulator of kinetochore function during meiosis I: required both for mono-orientation of kinetochores on sister chromosomes and protection of centromeric cohesin from separase-mediated cleavage (PubMed:25533956). Phosphorylates CEP68 and is required for its degradation. Regulates nuclear envelope breakdown during prophase by phosphorylating DCTN1 resulting in its localization in the nuclear envelope (By similarity). Phosphorylates the heat shock transcription factor HSF1, promoting HSF1 nuclear translocation upon heat shock (By similarity). Phosphorylates HSF1 also in the early mitotic period; this phosphorylation regulates HSF1 localization to the spindle pole, the recruitment of the SCF(BTRC) ubiquitin ligase complex induicing HSF1 degradation, and hence mitotic progression (By similarity). Regulates mitotic progression by phosphorylating RIOK2 (By similarity). {ECO:0000250|UniProtKB:P53350, ECO:0000269|PubMed:22405274, ECO:0000269|PubMed:25533956}. PTM: Catalytic activity is enhanced by phosphorylation of Thr-210. Phosphorylation at Thr-210 is first detected on centrosomes in the G2 phase of the cell cycle, peaks in prometaphase and gradually disappears from centrosomes during anaphase. Dephosphorylation at Thr-210 at centrosomes is probably mediated by protein phosphatase 1C (PP1C), via interaction with PPP1R12A/MYPT1. Autophosphorylation and phosphorylation of Ser-137 may not be significant for the activation of PLK1 during mitosis, but may enhance catalytic activity during recovery after DNA damage checkpoint. Phosphorylated in vitro by STK10 (By similarity). {ECO:0000250|UniProtKB:P53350}.; PTM: Ubiquitinated by the anaphase promoting complex/cyclosome (APC/C) in anaphase and following DNA damage, leading to its degradation by the proteasome. Ubiquitination is mediated via its interaction with FZR1/CDH1. Ubiquitination and subsequent degradation prevents entry into mitosis and is essential to maintain an efficient G2 DNA damage checkpoint. Monoubiquitination at Lys-492 by the BCR(KLHL22) ubiquitin ligase complex does not lead to degradation: it promotes PLK1 dissociation from phosphoreceptor proteins and subsequent removal from kinetochores, allowing silencing of the spindle assembly checkpoint (SAC) and chromosome segregation (By similarity). {ECO:0000250|UniProtKB:P53350}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P53350}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:25533956}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P53350}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P53350}. Midbody {ECO:0000250|UniProtKB:P53350}. Note=localization at the centrosome starts at the G1/S transition (By similarity). During early stages of mitosis, the phosphorylated form is detected on centrosomes and kinetochores. Localizes to the outer kinetochore. Presence of SGO1 and interaction with the phosphorylated form of BUB1 is required for the kinetochore localization. Localizes onto the central spindle by phosphorylating and docking at midzone proteins KIF20A/MKLP2 and PRC1 (By similarity). Colocalizes with FRY to separating centrosomes and spindle poles from prophase to metaphase in mitosis, but not in other stages of the cell cycle (By similarity). Localization to the centrosome is required for S phase progression (By similarity). Colocalizes with HSF1 at the spindle poles during prometaphase (By similarity). {ECO:0000250|UniProtKB:P53350}. SUBUNIT: Interacts with CEP170 and EVI5. Interacts and phosphorylates ERCC6L. Interacts with FAM29A. Interacts with SLX4/BTBD12 and TTDN1. Interacts with BUB1B. Interacts (via POLO-box domain) with the phosphorylated form of BUB1, CENPU and CDC25C. Interacts with isoform 3 of SGO1. Interacts with BORA, KIF2A and AURKA. Interacts with TOPORS and CYLD. Interacts with ECT2; the interaction is stimulated upon phosphorylation of ECT2 on 'Thr-444'. Interacts with PRC1. Interacts with KIF20A/MKLP2 (when phosphorylated), leading to the recruitment at the central spindle. Interacts (via POLO box domains) with PPP1R12A/MYPT1 (when previously phosphorylated by CDK1) (By similarity). Part of an astrin (SPAG5)-kinastrin (SKAP) complex containing KNSTRN, SPAG5, PLK1, DYNLL1 and SGO2 (By similarity). Interacts with BIRC6/bruce (By similarity). Interacts with CDK1-phosphorylated DCTN6 during mitotic prometaphase; the interaction facilitates recruitment to kinetochores (By similarity). Interacts with CDK1-phosphorylated FRY; this interaction occurs in mitotic cells, but not in interphase cells. FRY interaction facilitates AURKA-mediated PLK1 phosphorylation. Interacts with CEP68; the interaction phosphorylates CEP68. Interacts (via POLO-box domain) with DCTN1 (By similarity). Interacts with FOPNL in later G1, S, G2 and M phases of the cell cycle; this interaction recruits PLK1 to centrosomes, a step required for S phase progression (By similarity). Interacts with HSF1; this interaction increases upon heat shock but does not modulate neither HSF1 homotrimerization nor DNA-binding activities (By similarity). Interacts with HNRNPU; this interaction induces phosphorylation of HNRNPU in mitosis (By similarity). Interacts (via its N-terminus) with RIOK2 (By similarity). Interacts with KLHL22 (By similarity). {ECO:0000250|UniProtKB:P53350, ECO:0000269|PubMed:22753416}. DOMAIN: The POLO box domains act as phosphopeptide-binding module that recognize and bind serine-[phosphothreonine/phosphoserine]-(proline/X) motifs. PLK1 recognizes and binds docking proteins that are already phosphorylated on these motifs, and then phosphorylates them. PLK1 can also create its own docking sites by mediating phosphorylation of serine-[phosphothreonine/phosphoserine]-(proline/X) motifs subsequently recognized by the POLO box domains (By similarity). {ECO:0000250|UniProtKB:P53350}. TISSUE SPECIFICITY: Newborn and adult spleen, fetal and newborn kidney, liver, brain, thymus and adult bone marrow, thymus, ovary and testes. +P42582 NKX25_MOUSE Homeobox protein Nkx-2.5 (Cardiac-specific homeobox) (Homeobox protein CSX) (Homeobox protein NK-2 homolog E) 318 34,163 Chain (1); Compositional bias (2); DNA binding (1); Helix (4); Sequence conflict (4) FUNCTION: Implicated in commitment to and/or differentiation of the myocardial lineage. Acts as a transcriptional activator of ANF in cooperation with GATA4. Binds to the core DNA motif of NPPA promoter. It is transcriptionally controlled by PBX1 and acts as a transcriptional repressor of CDKN2B. Together with PBX1, it is required for spleen development through a mechanism that involves CDKN2B repression. {ECO:0000250|UniProtKB:P52952, ECO:0000269|PubMed:22560297, ECO:0000269|PubMed:9584153}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Homodimer (via the homeobox); binds DNA as homodimer. Interacts (via the homeobox) with TBX5 (via the T-box); this complex binds DNA (By similarity). Interacts with HIPK1 and HIPK2, but not HIPK3 (PubMed:9748262). Interacts with the C-terminal zinc finger of GATA4 through its homeobox domain (PubMed:9584153). Also interacts with JARID2 which represses its ability to activate transcription of ANF (PubMed:15542826). Interacts with FBLIM1 (PubMed:14757752). Interacts with TBX18 (PubMed:17584735). {ECO:0000250|UniProtKB:P52952, ECO:0000269|PubMed:14757752, ECO:0000269|PubMed:15542826, ECO:0000269|PubMed:17584735, ECO:0000269|PubMed:9584153, ECO:0000269|PubMed:9748262}. DOMAIN: The homeobox domain binds to double-stranded DNA. {ECO:0000250|UniProtKB:P52952}. TISSUE SPECIFICITY: Predominantly in the adult and embryonic heart, and to a lesser extent in lingual muscle, spleen and stomach. +Q99ME9 NOG1_MOUSE Nucleolar GTP-binding protein 1 (Chronic renal failure gene protein) (GTP-binding protein NGB) 634 74,113 Chain (1); Cross-link (3); Domain (1); Initiator methionine (1); Modified residue (7); Nucleotide binding (3); Sequence conflict (8) FUNCTION: Involved in the biogenesis of the 60S ribosomal subunit. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. +Q8VI84 NOC3L_MOUSE Nucleolar complex protein 3 homolog (NOC3 protein homolog) (Factor for adipocyte differentiation 24) (NOC3-like protein) (Nucleolar complex-associated protein 3-like protein) 807 93,211 Chain (1); Coiled coil (1); Cross-link (1); Sequence conflict (4) FUNCTION: May be required for adipogenesis. {ECO:0000269|PubMed:15564382}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:15564382}. Nucleus speckle {ECO:0000269|PubMed:15564382}. +Q8CH77 NAV1_MOUSE Neuron navigator 1 (Pore membrane and/or filament-interacting-like protein 3) 1875 202,368 Alternative sequence (8); Chain (1); Coiled coil (4); Compositional bias (1); Erroneous initiation (1); Modified residue (33); Sequence conflict (12) FUNCTION: May be involved in neuronal migration. {ECO:0000269|PubMed:15797708}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15797708}. Note=Associates with a subset of microtubule plus ends. Enriched in neuronal growth cones. SUBUNIT: Interacts with tubulin. {ECO:0000269|PubMed:15797708}. TISSUE SPECIFICITY: Expressed in heart and brain. Present in brain (at protein level). In adult brain, found almost exclusively in areas of secondary neurogenesis from the hippocampus and the subventricular zone. {ECO:0000269|PubMed:15797708}. +Q61026 NCOA2_MOUSE Nuclear receptor coactivator 2 (NCoA-2) (Glucocorticoid receptor-interacting protein 1) (GRIP-1) (Steroid receptor coactivator 2) (SRC-2) (Transcriptional intermediary factor 2) 1462 158,466 Chain (1); Cross-link (6); Domain (2); Frameshift (1); Helix (2); Initiator methionine (1); Modified residue (27); Motif (5); Mutagenesis (3); Region (2); Sequence conflict (18) FUNCTION: Transcriptional coactivator for steroid receptors and nuclear receptors. Coactivator of the steroid binding domain (AF-2) but not of the modulating N-terminal domain (AF-1). Required with NCOA1 to control energy balance between white and brown adipose tissues. Critical regulator of glucose metabolism regulation, acts as RORA coactivator to specifically modulate G6PC expression. Involved in the positive regulation of the transcriptional activity of the glucocorticoid receptor NR3C1 by sumoylation enhancer RWDD3. Positively regulates the circadian clock by acting as a transcriptional coactivator for the CLOCK-ARNTL/BMAL1 heterodimer (PubMed:24529706). {ECO:0000269|PubMed:11997499, ECO:0000269|PubMed:12507421, ECO:0000269|PubMed:16148126, ECO:0000269|PubMed:19039140, ECO:0000269|PubMed:24529706}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Present in a complex containing NCOA3, IKKA, IKKB, IKBKG and CREBBP. Interacts (via C-terminus) with CREBBP. Interacts with ESR1, HIF1A, NCOA1, APEX, NR3C1, NR3C2, CARM1, RARA, and RXRA. Present in a complex containing CARM1 and EP300/P300. Interacts with CASP8AP2 and TTLL5/STAMP. Interacts with PSMB9 and DDX5. Interacts (via LXXLL 1, 2 and 3 motifs) with RORA and RORC (via AF-2 motif). Interacts with RWDD3. Interacts with CLOCK and ARNTL/BMAL1. Interacts with NR4A3; potentiates the activity of the NR4A3 (PubMed:12709428). Interacts with NR1H3 (By similarity). {ECO:0000250|UniProtKB:Q15596, ECO:0000269|PubMed:10381882, ECO:0000269|PubMed:11997499, ECO:0000269|PubMed:12477726, ECO:0000269|PubMed:12709428, ECO:0000269|PubMed:16148126, ECO:0000269|PubMed:19039140, ECO:0000269|PubMed:24529706, ECO:0000269|PubMed:9111344}. DOMAIN: Contains four Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs. The LXXLL motifs are essential for the association with nuclear receptors and are, at least in part, functionally redundant (PubMed:16148126). {ECO:0000269|PubMed:16148126}.; DOMAIN: The LLXXLXXXL motif is involved in transcriptional coactivation and CREBBP/CBP binding. {ECO:0000250}.; DOMAIN: Contains 2 C-terminal transcription activation domains (AD1 and AD2) that can function independently. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. +Q8K1X4 NCKPL_MOUSE Nck-associated protein 1-like (Hematopoietic protein 1) 1134 128,905 Chain (1); Transmembrane (1) TRANSMEM 999 1019 Helical. {ECO:0000255}. FUNCTION: Essential hematopoietic-specific regulator of the actin cytoskeleton. Controls lymphocyte development, activation, proliferation and homeostasis, erythrocyte membrane stability, as well as phagocytosis and migration by neutrophils and macrophages (PubMed:19015308, PubMed:23424621). Component of the WAVE2 complex which signals downstream of RAC to stimulate F-actin polymerization (PubMed:23424621). Required for stabilization and/or translation of the WAVE2 complex proteins in hematopoietic cells (PubMed:19015308). Exhibits complex cycles of activation and inhibition to generate waves of propagating the assembly with actin. Also involved in mechanisms WAVE independent to regulate myosin and actin polymerization during neutrophil chemotaxis (By similarity). {ECO:0000250|UniProtKB:P55160, ECO:0000269|PubMed:19015308, ECO:0000269|PubMed:23424621}. SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P55160}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:P55160}. Note=Localizes to the leading edge of polarized neutrophils. {ECO:0000250|UniProtKB:P55160}. TISSUE SPECIFICITY: Predominantly expressed in developing and mature hematopoietic cells. Also detected in urogenital tissues, including testis. {ECO:0000269|PubMed:19015308}. +Q8CGQ8 NCKX4_MOUSE Sodium/potassium/calcium exchanger 4 (Na(+)/K(+)/Ca(2+)-exchange protein 4) (Solute carrier family 24 member 4) 622 68,974 Alternative sequence (2); Chain (1); Compositional bias (1); Erroneous initiation (1); Frameshift (1); Glycosylation (1); Repeat (2); Sequence caution (1); Sequence conflict (1); Signal peptide (1); Topological domain (11); Transmembrane (10) TRANSMEM 98 118 Helical. {ECO:0000255}.; TRANSMEM 143 163 Helical. {ECO:0000255}.; TRANSMEM 173 193 Helical. {ECO:0000255}.; TRANSMEM 201 221 Helical. {ECO:0000255}.; TRANSMEM 225 245 Helical. {ECO:0000255}.; TRANSMEM 458 478 Helical. {ECO:0000255}.; TRANSMEM 480 500 Helical. {ECO:0000255}.; TRANSMEM 527 547 Helical. {ECO:0000255}.; TRANSMEM 558 578 Helical. {ECO:0000255}.; TRANSMEM 587 607 Helical. {ECO:0000255}. TOPO_DOM 39 97 Extracellular. {ECO:0000305}.; TOPO_DOM 119 142 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 164 172 Extracellular. {ECO:0000305}.; TOPO_DOM 194 200 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 222 224 Extracellular. {ECO:0000305}.; TOPO_DOM 246 457 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 479 479 Extracellular. {ECO:0000305}.; TOPO_DOM 501 526 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 548 557 Extracellular. {ECO:0000305}.; TOPO_DOM 579 586 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 608 622 Extracellular. {ECO:0000305}. FUNCTION: Transports 1 Ca(2+) and 1 K(+) in exchange for 4 Na(+). Controls the rapid response termination and proper regulation of adaptation in olfactory sensory neurons (OSNs) which subsequently influences how odor information is encoded and perceived. May play a role in calcium transport during amelogenesis. {ECO:0000269|PubMed:22057188, ECO:0000269|PubMed:23375655}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24621671, ECO:0000269|PubMed:26247047}. Cell membrane {ECO:0000269|PubMed:24621671, ECO:0000269|PubMed:26247047}; Multi-pass membrane protein {ECO:0000269|PubMed:24621671}. TISSUE SPECIFICITY: Expressed in late secretory-stage and maturation-stage ameloblasts, with significantly increased expression during the late stages of amelogenesis (at protein level) (PubMed:22677781, PubMed:24621671, PubMed:26247047). Widely expressed in most regions of the brain, including hippocampus, neocortex, thalamus, striatum and olfactory bulb (PubMed:12379639). Expressed in the olfactory sensory neurons (PubMed:22057188). {ECO:0000269|PubMed:22057188, ECO:0000269|PubMed:22677781, ECO:0000269|PubMed:24621671, ECO:0000269|PubMed:26247047}. +Q62414 NDF2_MOUSE Neurogenic differentiation factor 2 (NeuroD2) (NeuroD-related factor) (NDRF) 383 41,493 Chain (1); Compositional bias (2); Domain (1); Motif (1); Mutagenesis (1); Sequence conflict (1) FUNCTION: Transcriptional regulator implicated in neuronal determination. Mediates calcium-dependent transcription activation by binding to E box-containing promoter. Critical factor essential for the repression of the genetic program for neuronal differentiation; prevents the formation of synaptic vesicle clustering at active zone to the presynaptic membrane in postmitotic neurons. Induces transcription of ZEB1, which in turn represses neuronal differentiation by down-regulating REST expression. Plays a role in the establishment and maturation of thalamocortical connections; involved in the segregation of thalamic afferents into distinct barrel domains within layer VI of the somatosensory cortex. Involved in the development of the cerebellar and hippocampal granular neurons, neurons in the basolateral nucleus of amygdala and the hypothalamic-pituitary axis. Associates with chromatin to the DPYSL3 E box-containing promoter. {ECO:0000269|PubMed:10648228, ECO:0000269|PubMed:14697366, ECO:0000269|PubMed:16203979, ECO:0000269|PubMed:16504944, ECO:0000269|PubMed:16730830, ECO:0000269|PubMed:18214987, ECO:0000269|PubMed:19900895, ECO:0000269|PubMed:20346398}. PTM: Ubiquitinated by the APC/C complex; leading to its degradation in neurons. The CDC20-APC/C-induced degradation of NEUROD2 drives presynaptic differentiation. {ECO:0000269|PubMed:19900895}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:10648228, ECO:0000269|PubMed:16730830}. SUBUNIT: Interacts with TCF3, TCF4 and TCF12. Interacts with CDC20. Efficient DNA-binding and transcription activation require dimerization with another bHLH protein. {ECO:0000269|PubMed:18214987, ECO:0000269|PubMed:19900895}. DOMAIN: The C-terminal region is necessary for depolarization-induced and calcium-dependent transcription activation. TISSUE SPECIFICITY: Expressed in the external germinal layer (EGL) and internal granular layer (IGL) of the cerebellum (at protein level). Expressed in layers V and VI of the neocortex at postnatal day 1. Expressed in all layers of the neocortex at postnatal day 4. Strongly expressed in layer IV of the neocortex, particularly in the barrel cortex at postnatal day 7. Expressed in the CA1, CA2 and CA3 and dentate gyrus of the hippocampus and many nuclei such as the habenular thalamic nuclei, paraventricular hypothalamic nuclei, amygdala nuclei, and pyramidal nucleus. Expressed in granule cells, molecular layer neurons, and deep cerebella nuclei of the cerebellum. Expressed in brainstem neurons in the external cuneate nucleus and central gray. {ECO:0000269|PubMed:14697366, ECO:0000269|PubMed:16504944, ECO:0000269|PubMed:20346398}. +O70172 PI42A_MOUSE Phosphatidylinositol 5-phosphate 4-kinase type-2 alpha (EC 2.7.1.149) (1-phosphatidylinositol 5-phosphate 4-kinase 2-alpha) (Diphosphoinositide kinase 2-alpha) (Phosphatidylinositol 5-phosphate 4-kinase type II alpha) (PI(5)P 4-kinase type II alpha) (PIP4KII-alpha) (PtdIns(5)P-4-kinase isoform 2-alpha) 405 46,152 Chain (1); Domain (1); Initiator methionine (1); Modified residue (5) FUNCTION: Catalyzes the phosphorylation of phosphatidylinositol 5-phosphate (PtdIns5P) on the fourth hydroxyl of the myo-inositol ring, to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). May exert its function by regulating the levels of PtdIns5P, which functions in the cytosol by increasing AKT activity and in the nucleus signals through ING2. May regulate the pool of cytosolic PtdIns5P in response to the activation of tyrosine phosphorylation. May negatively regulate insulin-stimulated glucose uptake by lowering the levels of PtdIns5P (By similarity). May be involved in thrombopoiesis and the terminal maturation of megakaryocytes and regulation of their size. {ECO:0000250, ECO:0000269|PubMed:16434494}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm. Cell membrane. Note=Localization to the nucleus is modulated by the interaction with PIP4K2B (By similarity). Localized to the demarcation membrane system (DMS). May translocate from the cytosol to the cell membrane upon activation of tyrosine phosphorylation. May translocate from the inner to the outer segments of the rod photoreceptor cells in response to light. {ECO:0000250}. SUBUNIT: Homodimer. Interacts with PIP4K2B. Interaction with PIP4K2B may modulate localization to the nucleus (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Detected in rod photoreceptor cells. {ECO:0000269|PubMed:20204506}. +Q9WV85 NDK3_MOUSE Nucleoside diphosphate kinase 3 (NDK 3) (NDP kinase 3) (EC 2.7.4.6) (DR-nm23) (Nucleoside diphosphate kinase C) (NDPKC) (nm23-M3) 169 19,099 Active site (1); Binding site (6); Chain (1); Sequence conflict (3) FUNCTION: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Probably has a role in normal hematopoiesis by inhibition of granulocyte differentiation and induction of apoptosis (By similarity). {ECO:0000250}. +P70181 PI51B_MOUSE Phosphatidylinositol 4-phosphate 5-kinase type-1 beta (PIP5K1-beta) (PtdIns(4)P-5-kinase 1 beta) (EC 2.7.1.68) (Phosphatidylinositol 4-phosphate 5-kinase type I alpha) (PIP5KIalpha) (Phosphatidylinositol 4-phosphate 5-kinase type I beta) (PIP5KIbeta) 539 60,803 Alternative sequence (1); Chain (1); Domain (1); Modified residue (3); Mutagenesis (2); Sequence conflict (4) FUNCTION: Participates in the biosynthesis of phosphatidylinositol 4,5-bisphosphate. Mediates RAC1-dependent reorganization of actin filaments. Contributes to the activation of PLD2. Together with PIP5K1A is required after stimulation of G-protein coupled receptors for stable platelet adhesion. {ECO:0000269|PubMed:10679324, ECO:0000269|PubMed:18772378, ECO:0000269|PubMed:8798574}. SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}. Note=Associated with membranes. {ECO:0000250}. SUBUNIT: Interacts with RAC1, AJUBA, PLD1, PLD2 and ARF1. {ECO:0000269|PubMed:10679324, ECO:0000269|PubMed:10747863, ECO:0000269|PubMed:11032811, ECO:0000269|PubMed:15870270}. TISSUE SPECIFICITY: Highly expressed in brain and testis. Barely detectable in liver and skeletal muscle. {ECO:0000269|PubMed:8798574}. +O70161 PI51C_MOUSE Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma (PIP5K1-gamma) (PtdIns(4)P-5-kinase 1 gamma) (EC 2.7.1.68) (Phosphatidylinositol 4-phosphate 5-kinase type I gamma) (PIP5KIgamma) 661 72,408 Alternative sequence (3); Beta strand (1); Chain (1); Domain (1); Erroneous initiation (1); Helix (1); Modified residue (11); Mutagenesis (8); Region (1); Sequence conflict (2) FUNCTION: Catalyzes the phosphorylation of phosphatidylinositol 4-phosphate (PtdIns4P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). PtdIns(4,5)P2 is involved in a variety of cellular processes and is the substrate to form phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3), another second messenger. The majority of PtdIns(4,5)P2 is thought to occur via type I phosphatidylinositol 4-phosphate 5-kinases given the abundance of PtdIns4P. Participates in a variety of cellular processes such as vesicle mediated transport, cell adhesion, cell polarization and cell migration. Together with PIP5K1A is required for phagocytosis, but they regulate different types of actin remodeling at sequential steps. Promotes particle attachment by generating the pool of PtdIns(4,5)P2 that induces controlled actin depolymerization to facilitate Fc-gamma-R clustering. Mediates RAC1-dependent reorganization of actin filaments. Required for synaptic vesicle transport. Controls the plasma membrane pool of PtdIns(4,5)P2 implicated in synaptic vesicle endocytosis and exocytosis. Plays a role in endocytosis mediated by clathrin and AP-2 (adaptor protein complex 2). Required for clathrin-coated pits assembly at the synapse. Participates in cell junction assembly. Modulates adherens junctions formation by facilitating CDH1 trafficking. Required for focal adhesion dynamics. Modulates the targeting of talins (TLN1 and TLN2) to the plasma membrane and their efficient assembly into focal adhesions. Regulates the interaction between talins (TLN1 and TLN2) and beta-integrins. Required for uropodium formation and retraction of the cell rear during directed migration. Has a role in growth factor- stimulated directional cell migration and adhesion. Required for talin assembly into nascent adhesions forming at the leading edge toward the direction of the growth factor. Negative regulator of T-cell activation and adhesion. Negatively regulates integrin alpha-L/beta-2 (LFA-1) polarization and adhesion induced by T-cell receptor. Together with PIP5K1A has a role during embryogenesis and together with PIP5K1B may have a role immediately after birth. {ECO:0000269|PubMed:12422220, ECO:0000269|PubMed:15386003, ECO:0000269|PubMed:16707488, ECO:0000269|PubMed:17609388, ECO:0000269|PubMed:17635937, ECO:0000269|PubMed:17928408, ECO:0000269|PubMed:19153220, ECO:0000269|PubMed:20622009, ECO:0000269|PubMed:20855869, ECO:0000269|PubMed:9535851}. PTM: Phosphorylation on Ser-645 negatively regulates binding to TLN2 and is strongly stimulated in mitosis. Phosphorylation on Tyr-644 is necessary for targeting to focal adhesions. Phosphorylation on Ser-645 and Tyr-644 are mutually exclusive. Phosphorylated by SYK and CSK. Tyrosine phosphorylation is enhanced by PTK2 signaling. Phosphorylated at Tyr-634 upon EGF stimulation. Some studies suggest that phosphorylation on Tyr-644 enhances binding to tailins (TLN1 and TLN2); others that phosphorylation at Tyr-644 does not directly enhance binding to tailins (TLN1 and TLN2) but may act indirectly by inhibiting phosphorylation at Ser-645. {ECO:0000269|PubMed:12422220, ECO:0000269|PubMed:14691141, ECO:0000269|PubMed:16707488, ECO:0000269|PubMed:17635937, ECO:0000269|PubMed:19153220}.; PTM: Acetylation at Lys-265 and Lys-268 seems to decrease lipid kinase activity. Deacetylation of these sites by SIRT1 positively regulates the exocytosis of TSH-containing granules from pituitary cells (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. Endomembrane system. Cytoplasm. Cell junction, focal adhesion. Cell junction, adherens junction. Cell projection, ruffle membrane. Cell projection, phagocytic cup. Cell projection, uropodium. Note=During directional migration isoform 1 localized at the uropodium, and isoform 3 localized all along cell membrane including the uropodium and the leading edge. SUBUNIT: Isoform 1 interacts with TLN1. Interacts with TLN2; interaction stimulates lipid kinase activity. May compete with beta-integrins for the same binding site on TLN1 and TLN2. Interacts with ARF6 (By similarity). Interacts with AP2B1. Isoform 1 interacts with AP2M1; phosphorylation of PIP5K1C by CSK disrupts the interaction; clathrin competes with PIP5K1C. Interacts with CDH1 (By similarity). Interacts with CSK. Interacts with PLCG1; interaction is abolished upon EGF stimulation. Interacts with LAPTM4B; promotes SNX5 association with LAPTM4B; kinase activity of PIP5K1C is required; interaction is regulated by phosphatidylinositol 4,5-bisphosphate generated by PIP5K1C (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O60331, ECO:0000269|PubMed:12422220, ECO:0000269|PubMed:14691141, ECO:0000269|PubMed:15623515, ECO:0000269|PubMed:16707488, ECO:0000269|PubMed:17635937, ECO:0000269|PubMed:19287005}. TISSUE SPECIFICITY: High expression in brain. Also detected in lung, thymus, heart, testicle, kidney and embryo. Highly expressed in forebrain, in particular in cerebellum, hippocampus and cerebral cortex. {ECO:0000269|PubMed:14741049, ECO:0000269|PubMed:20622009, ECO:0000269|PubMed:9535851}. +Q6P1B3 PIANP_MOUSE PILR alpha-associated neural protein (Brain protein 1) (PILR-associating neural protein) (Paired immunoglobin-like type 2 receptor-associating neural protein) 278 29,744 Chain (1); Glycosylation (1); Sequence caution (1); Sequence conflict (5); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 175 195 Helical. {ECO:0000255}. TOPO_DOM 28 174 Extracellular. {ECO:0000255}.; TOPO_DOM 196 278 Cytoplasmic. {ECO:0000255}. FUNCTION: Acts as a ligand for PILRA in neuronal tissues, where it may be involved in immune regulation. {ECO:0000269|PubMed:21241660}. PTM: O-glycosylation at Thr-136 is essential for recognition by PILRA. {ECO:0000269|PubMed:21241660}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Mainly expressed in brain and spinal cord. Weak expression also detected in heart, kidney, spleen and lymph node. Virtually no expression detected in liver and embryo relative to brain. {ECO:0000269|PubMed:21241660}. +Q9QXL8 NDK7_MOUSE Nucleoside diphosphate kinase 7 (NDK 7) (NDP kinase 7) (EC 2.7.4.6) (nm23-M7) 395 44,434 Active site (1); Binding site (4); Chain (1); Domain (1) FUNCTION: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. +Q9JM05 PIAS4_MOUSE E3 SUMO-protein ligase PIAS4 (EC 2.3.2.27) (PIASy) (Protein inhibitor of activated STAT protein 4) (Protein inhibitor of activated STAT protein gamma) (PIAS-gamma) (RING-type E3 ubiquitin transferase PIAS4) 507 55,570 Chain (1); Compositional bias (1); Cross-link (9); Domain (2); Initiator methionine (1); Modified residue (2); Motif (1); Mutagenesis (5); Sequence conflict (3); Zinc finger (1) Protein modification; protein sumoylation. FUNCTION: Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor. Plays a crucial role as a transcriptional coregulation in various cellular pathways, including the STAT pathway, the p53/TP53 pathway, the Wnt pathway and the steroid hormone signaling pathway. Involved in gene silencing. Mediates sumoylation of CEBPA, PARK7, HERC2, MYB, TCF4 and RNF168. In Wnt signaling, represses LEF1 and enhances TCF4 transcriptional activities through promoting their sumoylations. Enhances the sumoylation of MTA1 and may participate in its paralog-selective sumoylation (By similarity). {ECO:0000250}. PTM: Sumoylated. Lys-35 is the main site of sumoylation. Sumoylation is required for TCF4 sumoylation and transcriptional activation. Represses LEF1 transcriptional activity. SUMO1 is the preferred conjugate. {ECO:0000269|PubMed:11731474}.; PTM: Ubiquitinated by TRIM32 upon treatment with UVB and TNF-alpha. {ECO:0000269|PubMed:16816390}. SUBCELLULAR LOCATION: Nucleus, PML body {ECO:0000269|PubMed:11731474, ECO:0000269|PubMed:16816390}. Note=Colocalizes with SUMO1 and TCF7L2/TCF4 and LEF1 in a subset of PML (promyelocytic leukemia) nuclear bodies. Accumulates in the cytoplasm upon treatment with UVB and TNF-alpha. SUBUNIT: Interacts with AR, AXIN1, GATA2, LEF1, TP53 and STAT1, after treatment with IFNG. Binds to AT-rich DNA sequences, known as matrix or scaffold attachment regions (MARs/SARs) (By similarity). Interacts with TICAM1 (By similarity). Interacts with Moloney murine leukemia virus CA. Interacts with KLF8; the interaction results in SUMO ligation and repression of KLF8 transcriptional activity and of its cell cycle progression into G(1) phase. Interacts with MTA1 (By similarity). Interacts with TRIM32 upon treatment with UVB and TNF-alpha. {ECO:0000250, ECO:0000269|PubMed:11731474, ECO:0000269|PubMed:16352559, ECO:0000269|PubMed:16816390}. DOMAIN: The LXXLL motif is a coregulator signature that is essential for transcriptional corepression. TISSUE SPECIFICITY: Widely expressed, with highest levels in testis. Also expressed in vascular endothelial cells, in primary keratinocytes and in the CNS, including cortex, olfactory bulb, spinal cord, thalamus and trigeminal ganglion. Low expression, if any, in liver and lung. {ECO:0000269|PubMed:10854042, ECO:0000269|PubMed:12750312}. +Q80SX8 PIF1_MOUSE ATP-dependent DNA helicase PIF1 (EC 3.6.4.12) (DNA repair and recombination helicase PIF1) (Pif1/Rrm3 DNA helicase-like protein) 650 70,942 Alternative sequence (3); Chain (1); DNA binding (1); Modified residue (2); Nucleotide binding (1); Region (1); Sequence conflict (10) FUNCTION: DNA-dependent ATPase and 5'-3' DNA helicase required for the maintenance of both mitochondrial and nuclear genome stability. Efficiently unwinds G-quadruplex (G4) DNA structures and forked RNA-DNA hybrids. Resolves G4 structures, preventing replication pausing and double-strand breaks (DSBs) at G4 motifs. Involved in the maintenance of telomeric DNA. Inhibits telomere elongation, de novo telomere formation and telomere addition to DSBs via catalytic inhibition of telomerase. Reduces the processivity of telomerase by displacing active telomerase from DNA ends. Releases telomerase by unwinding the short telomerase RNA/telomeric DNA hybrid that is the intermediate in the telomerase reaction. Possesses an intrinsic strand annealing activity. {ECO:0000255|HAMAP-Rule:MF_03176}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03176, ECO:0000269|PubMed:17130244}.; SUBCELLULAR LOCATION: Isoform 3: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03176, ECO:0000269|PubMed:23275553}. SUBUNIT: Monomer (By similarity). Interacts with telomerase. {ECO:0000255|HAMAP-Rule:MF_03176, ECO:0000269|PubMed:17130244}. DOMAIN: The PIF1 N-terminal (PINT) domain enhances the interaction with ssDNA through intrinsic binding activity, it also harbors DNA strand-annealing activity. {ECO:0000250}. +Q5SX19 PIGL_MOUSE N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase (EC 3.5.1.89) (Phosphatidylinositol-glycan biosynthesis class L protein) (PIG-L) 252 28,183 Chain (1); Topological domain (1); Transmembrane (1) TRANSMEM 2 22 Helical. {ECO:0000255}. TOPO_DOM 23 252 Cytoplasmic. {ECO:0000255}. Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis. FUNCTION: Involved in the second step of GPI biosynthesis. De-N-acetylation of N-acetylglucosaminyl-phosphatidylinositol (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. +Q3UHN9 NDST1_MOUSE Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 1 (EC 2.8.2.8) (Glucosaminyl N-deacetylase/N-sulfotransferase 1) (NDST-1) (N-heparan sulfate sulfotransferase 1) (N-HSST 1) ([Heparan sulfate]-glucosamine N-sulfotransferase 1) (HSNST 1) [Includes: Heparan sulfate N-deacetylase 1 (EC 3.-.-.-); Heparan sulfate N-sulfotransferase 1 (EC 2.8.2.-)] 882 100,726 Active site (1); Alternative sequence (4); Binding site (1); Chain (1); Disulfide bond (1); Frameshift (1); Glycosylation (4); Mutagenesis (2); Nucleotide binding (2); Region (2); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 18 38 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 17 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 39 882 Lumenal. {ECO:0000255}. Glycan metabolism; heparan sulfate biosynthesis. Glycan metabolism; heparin biosynthesis. FUNCTION: Essential bifunctional enzyme that catalyzes both the N-deacetylation and the N-sulfation of glucosamine (GlcNAc) of the glycosaminoglycan in heparan sulfate. Modifies the GlcNAc-GlcA disaccharide repeating sugar backbone to make N-sulfated heparosan, a prerequisite substrate for later modifications in heparin biosynthesis. Plays a role in determining the extent and pattern of sulfation of heparan sulfate. Compared to other NDST enzymes, its presence is absolutely required. Participates in biosynthesis of heparan sulfate that can ultimately serve as L-selectin ligands, thereby playing a role in inflammatory response. Required for the exosomal release of SDCBP, CD63 and syndecan (By similarity). {ECO:0000250|UniProtKB:P52848, ECO:0000269|PubMed:10664446, ECO:0000269|PubMed:10852901, ECO:0000269|PubMed:11087757, ECO:0000269|PubMed:12692154, ECO:0000269|PubMed:16020517, ECO:0000269|PubMed:16056228}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:P52848}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P52848}. SUBUNIT: Monomer. Interacts with EXT2. {ECO:0000250|UniProtKB:P52848}. TISSUE SPECIFICITY: Widely expressed in adult and throughout development. {ECO:0000269|PubMed:11087757}. +Q99LY9 NDUS5_MOUSE NADH dehydrogenase [ubiquinone] iron-sulfur protein 5 (Complex I-15 kDa) (CI-15 kDa) (NADH-ubiquinone oxidoreductase 15 kDa subunit) 106 12,648 Beta strand (4); Chain (1); Disulfide bond (2); Domain (1); Helix (5); Motif (2); Turn (2) FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. {ECO:0000250|UniProtKB:O43920}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:O43920}; Peripheral membrane protein {ECO:0000250|UniProtKB:O43920}. Mitochondrion intermembrane space {ECO:0000250|UniProtKB:O43920}. SUBUNIT: Mammalian complex I is composed of 45 different subunits. This is a component of the iron-sulfur (IP) fragment of the enzyme. {ECO:0000250|UniProtKB:O43920}. DOMAIN: Contains two C-X9-C motifs that are predicted to form a helix-coil-helix structure, permitting the formation of intramolecular disulfide bonds. {ECO:0000250|UniProtKB:O43920}. +Q8CCP0 NEMF_MOUSE Nuclear export mediator factor Nemf (Serologically defined colon cancer antigen 1 homolog) 1064 121,188 Alternative sequence (6); Chain (1); Coiled coil (3); Erroneous initiation (4); Frameshift (2); Modified residue (3); Sequence caution (1); Sequence conflict (8) FUNCTION: Component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation. NEMF is responsible for selective recognition of stalled 60S subunits by recognizing an exposed, nascent chain-conjugated tRNA moiety. Nemf is important for the stable association of Ltn1 to the complex. May indirectly play a role in nuclear export. {ECO:0000250|UniProtKB:O60524}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Component of the ribosome quality control complex (RQC), composed of at least the E3 ubiquitin ligase Ltn1 and Nemf. The complex probably also contains Tcf25 as well as Vcp/p97 and its ubiquitin-binding cofactors. RQC forms a stable complex with 60S ribosomal subunits. Interacts (via its N-terminus) with Xpo1. {ECO:0000250|UniProtKB:O60524, ECO:0000250|UniProtKB:Q04781, ECO:0000250|UniProtKB:Q9VBX1}. DOMAIN: The N-terminal domain contains a nuclear export signal. The C-terminal domain may interact with cargo proteins (By similarity). {ECO:0000250}. +Q9Z1J2 NEK4_MOUSE Serine/threonine-protein kinase Nek4 (EC 2.7.11.1) (Never in mitosis A-related kinase 4) (NimA-related protein kinase 4) (Serine/threonine-protein kinase 2) 792 88,994 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Domain (1); Modified residue (5); Nucleotide binding (1); Sequence conflict (1) FUNCTION: Required for normal entry into proliferative arrest after a limited number of cell divisions, also called replicative senescence. Required for normal cell cycle arrest in response to double-stranded DNA damage (By similarity). Protein kinase that seems to act exclusively upon threonine residues. {ECO:0000250|UniProtKB:P51957, ECO:0000269|PubMed:10529384}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10529384}. Cell projection, cilium {ECO:0000250|UniProtKB:P51957}. TISSUE SPECIFICITY: Expressed ubiquitously among various organs and is up-regulated in the testis. {ECO:0000269|PubMed:10529384}. +P53810 PIPNA_MOUSE Phosphatidylinositol transfer protein alpha isoform (PI-TP-alpha) (PtdIns transfer protein alpha) (PtdInsTP alpha) 271 31,893 Beta strand (8); Binding site (6); Chain (1); Helix (12); Modified residue (1); Turn (5) FUNCTION: Catalyzes the transfer of PtdIns and phosphatidylcholine between membranes. SUBCELLULAR LOCATION: Cytoplasm. DISEASE: Note=Defects in Pitpna are the cause of the vibrator phenotype which is characterized by early-onset progressive action tremor, degeneration of brain stem and spinal cord neurons, and juvenile death. The mutation is due to the insertion of an intracisternal A particle retrotransposon in intron 4 which results in a 5-fold reduction in protein levels. {ECO:0000269|PubMed:9182797}. +Q7TSC3 NEK5_MOUSE Serine/threonine-protein kinase Nek5 (EC 2.7.11.1) (Never in mitosis A-related kinase 5) (NimA-related protein kinase 5) 627 71,790 Active site (1); Alternative sequence (3); Binding site (1); Chain (1); Domain (1); Nucleotide binding (1) +Q6ZQE4 NEMP1_MOUSE Nuclear envelope integral membrane protein 1 437 49,817 Chain (1); Erroneous initiation (1); Glycosylation (1); Modified residue (3); Mutagenesis (5); Region (3); Signal peptide (1); Transmembrane (5) TRANSMEM 159 179 Helical. {ECO:0000255}.; TRANSMEM 183 203 Helical. {ECO:0000255}.; TRANSMEM 214 234 Helical. {ECO:0000255}.; TRANSMEM 244 264 Helical. {ECO:0000255}.; TRANSMEM 288 308 Helical. {ECO:0000255}. PTM: Phosphorylated. Phosphorylation may regulate its interaction with RAN-GTP. {ECO:0000269|PubMed:25946333}. SUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000269|PubMed:25946333}; Multi-pass membrane protein {ECO:0000255}; Nucleoplasmic side {ECO:0000250|UniProtKB:B9X187}. Nucleus envelope {ECO:0000269|PubMed:25946333}. Note=Colocalizes with lamins and RAN-GTP at the nuclear envelope. {ECO:0000269|PubMed:25946333}. SUBUNIT: Homooligomer (By similarity). Interacts with RAN-GTP. {ECO:0000250|UniProtKB:B9X187, ECO:0000269|PubMed:25946333}. DOMAIN: The transmembrane domains are required and sufficient for its oligomerization. {ECO:0000250|UniProtKB:B9X187}. +Q8CFI0 NED4L_MOUSE E3 ubiquitin-protein ligase NEDD4-like (EC 2.3.2.26) (HECT-type E3 ubiquitin transferase NED4L) (NEDD4.2) (Nedd4-2) 1004 115,419 Active site (1); Alternative sequence (2); Beta strand (11); Chain (1); Compositional bias (1); Domain (6); Erroneous initiation (1); Helix (1); Modified residue (12); Mutagenesis (3); Sequence conflict (7); Turn (3) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Inhibits TGF-beta signaling by triggering SMAD2 and TGFBR1 ubiquitination and proteasome-dependent degradation. Promotes ubiquitination and internalization of various plasma membrane channels such as ENaC, SCN2A/Nav1.2, SCN3A/Nav1.3, SCN5A/Nav1.5, SCN9A/Nav1.7, SCN10A/Nav1.8, KCNA3/Kv1.3, KCNH2, EAAT1, KCNQ2/Kv7.2, KCNQ3/Kv7.3 or CLC5. Promotes ubiquitination and degradation of SGK1 and TNK2. Ubiquitinates BRAT1 and this ubiquitination is enhanced in the presence of NDFIP1. Plays a role in dendrite formation by melanocytes (By similarity). Involved in the regulation of TOR signaling (By similarity). Ubiquitinates and regulates protein levels of NTRK1 once this one is activated by NGF (By similarity). {ECO:0000250|UniProtKB:Q96PU5, ECO:0000269|PubMed:11149908, ECO:0000269|PubMed:11244092, ECO:0000269|PubMed:11742982, ECO:0000269|PubMed:12424229, ECO:0000269|PubMed:15123669}. PTM: Phosphorylated; which impairs interaction with SCNN. Interaction with YWHAH inhibits dephosphorylation (By similarity). Aldosterone induces Ser-477 phosphorylation by SGK1. {ECO:0000250, ECO:0000269|PubMed:11742982, ECO:0000269|PubMed:15958725}.; PTM: Auto-ubiquitinated. Deubiquitinated by USP36, no effect on NEDD4L protein levels. Both proteins interact and regulate each other's ubiquitination levels. {ECO:0000250|UniProtKB:Q96PU5}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12050153}. Golgi apparatus {ECO:0000250|UniProtKB:Q96PU5}. Endosome, multivesicular body {ECO:0000250|UniProtKB:Q96PU5}. SUBUNIT: Interacts with SMAD2, SMAD3, SMAD6 and SMAD7 (By similarity). Interacts with CLCN5 (By similarity). The phosphorylated form interacts with 14-3-3 proteins (By similarity). Interacts via its WW domains with SCNN1A, SCNN1B, SCNN1G, SCN1A, SCN2A, SCN3A, SCN5A, SCN8A, SCN9A and SCN10A (PubMed:11244092., PubMed:11742982, PubMed:12424229, PubMed:15123669). Interacts with NDFIP1 and NDFIP2; this interaction activates the E3 ubiquitin-protein ligase (PubMed:12050153). Interacts with TNK2 (By similarity). Interacts (via C2 domain) with NPC2 (By similarity). Interacts with ARRDC4 (By similarity). Interacts with KCNQ1; promotes internalization of KCNQ1 (By similarity). Interacts (via domains WW1, 3 and 4) with USP36; the interaction inhibits ubiquitination of, at least, NTRK1, KCNQ2 and KCNQ3 by NEDD4L (By similarity). {ECO:0000250|UniProtKB:Q96PU5, ECO:0000269|PubMed:11244092, ECO:0000269|PubMed:11742982, ECO:0000269|PubMed:12050153, ECO:0000269|PubMed:12424229, ECO:0000269|PubMed:14993279, ECO:0000269|PubMed:15123669}. TISSUE SPECIFICITY: Highly expressed in liver and kidney. Also expressed in heart, brain and lung. Isoform 1 is expressed in kidney, lung and gut. Isoform 3 is ubiquitously expressed. {ECO:0000269|PubMed:11149908, ECO:0000269|PubMed:11244092}. +Q3UJ81 NEPR1_MOUSE Nuclear envelope phosphatase-regulatory subunit 1 (NEP1-R1) (Transmembrane protein 188) 125 14,267 Alternative sequence (3); Chain (1); Modified residue (1); Transmembrane (2) TRANSMEM 33 53 Helical. {ECO:0000255}.; TRANSMEM 65 85 Helical. {ECO:0000255}. FUNCTION: Forms with the serine/threonine protein phosphatase CTDNEP1 an active complex which dephosphorylates and may activate LPIN1 and LPIN2. LPIN1 and LPIN2 are phosphatidate phosphatases that catalyze the conversion of phosphatidic acid to diacylglycerol and control the metabolism of fatty acids at different levels. May indirectly modulate the lipid composition of nuclear and/or endoplasmic reticulum membranes and be required for proper nuclear membrane morphology and/or dynamics. May also indirectly regulate the production of lipid droplets and triacylglycerol (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Filamentous pattern in the cytoplasm. {ECO:0000250}. SUBUNIT: Interacts with CTDNEP1; the complex dephosphorylates LPIN1 and LPIN2. {ECO:0000250}. TISSUE SPECIFICITY: Muscle specific with lower expression in other metabolic tissues. {ECO:0000269|PubMed:22134922}. +P70268 PKN1_MOUSE Serine/threonine-protein kinase N1 (EC 2.7.11.13) (Protein kinase C-like 1) (Protein kinase C-like PKN) (Protein-kinase C-related kinase 1) (Serine-threonine protein kinase N) 946 104,411 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Domain (6); Initiator methionine (1); Modified residue (13); Nucleotide binding (1); Site (3) FUNCTION: PKC-related serine/threonine-protein kinase involved in various processes such as regulation of the intermediate filaments of the actin cytoskeleton, cell migration, tumor cell invasion and transcription regulation. Part of a signaling cascade that begins with the activation of the adrenergic receptor ADRA1B and leads to the activation of MAPK14. Regulates the cytoskeletal network by phosphorylating proteins such as VIM and neurofilament proteins NEFH, NEFL and NEFM, leading to inhibit their polymerization. Phosphorylates 'Ser-575', 'Ser-637' and 'Ser-669' of MAPT/Tau, lowering its ability to bind to microtubules, resulting in disruption of tubulin assembly. Acts as a key coactivator of androgen receptor (ANDR)-dependent transcription, by being recruited to ANDR target genes and specifically mediating phosphorylation of 'Thr-11' of histone H3 (H3T11ph), a specific tag for epigenetic transcriptional activation that promotes demethylation of histone H3 'Lys-9' (H3K9me) by KDM4C/JMJD2C. Phosphorylates HDAC5, HDAC7 and HDAC9, leading to impair their import in the nucleus. Phosphorylates 'Thr-38' of PPP1R14A, 'Ser-159', 'Ser-163' and 'Ser-170' of MARCKS, and GFAP. Able to phosphorylate RPS6 in vitro. {ECO:0000250|UniProtKB:Q16512}. PTM: Autophosphorylated; preferably on serine. {ECO:0000250}.; PTM: Activated by limited proteolysis with trypsin. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q16512}. Nucleus {ECO:0000250|UniProtKB:Q16512}. Endosome {ECO:0000250|UniProtKB:Q16512}. Cell membrane {ECO:0000250|UniProtKB:Q63433}; Peripheral membrane protein {ECO:0000250}. Cleavage furrow {ECO:0000250|UniProtKB:Q16512}. Midbody {ECO:0000250|UniProtKB:Q16512}. Note=Associates with chromatin in a ligand-dependent manner. Localization to endosomes is mediated via its interaction with RHOB. Association to the cell membrane is dependent on Ser-377 phosphorylation. Accumulates during telophase at the cleavage furrow and finally concentrates around the midbody in cytokinesis. {ECO:0000250|UniProtKB:Q16512, ECO:0000250|UniProtKB:Q63433}. SUBUNIT: Interacts with ZFAND6 (PubMed:11054541). Interacts with ANDR. Interacts with PRKCB. Interacts (via REM 1 and REM 2 repeats) with RAC1 (By similarity). Interacts (via REM 1 repeat) with RHOA (PubMed:8571127). Interacts with RHOB. Interacts (via C-terminus) with PDPK1. Interacts with CCNT2; enhances MYOD1-dependent transcription. Component of a signaling complex containing at least AKAP13, PKN1, MAPK14, ZAK and MAP2K3. Within this complex, AKAP13 interacts directly with PKN1, which in turn recruits MAPK14, MAP2K3 and ZAK (By similarity). {ECO:0000250|UniProtKB:Q16512, ECO:0000269|PubMed:11054541, ECO:0000269|PubMed:8571127}. DOMAIN: The C1 domain does not bind the diacylglycerol (DAG). {ECO:0000250}. +Q8C4Y3 NELFB_MOUSE Negative elongation factor B (NELF-B) (Cofactor of BRCA1) 580 65,636 Alternative sequence (1); Chain (1); Erroneous initiation (2); Frameshift (1); Modified residue (2); Sequence conflict (2) FUNCTION: Essential component of the NELF complex, a complex that negatively regulates the elongation of transcription by RNA polymerase II (Pol II) (PubMed:25773599). The NELF complex, which acts via an association with the DSIF complex and causes transcriptional pausing, is counteracted by the P-TEFb kinase complex (By similarity). May be able to induce chromatin unfolding (By similarity). Essential for early embryogenesis; plays an important role in maintaining the undifferentiated state of embryonic stem cells (ESCs) by preventing unscheduled expression of developmental genes (PubMed:19340312). Plays a key role in establishing the responsiveness of stem cells to developmental cues; facilitates plasticity and cell fate commitment in ESCs by establishing the appropriate expression level of signaling molecules (PubMed:25773599). Supports the transcription of genes involved in energy metabolism in cardiomyocytes; facilitates the association of transcription initiation factors with the promoters of the metabolism-related genes (PubMed:24656816). {ECO:0000250|UniProtKB:Q8WX92, ECO:0000269|PubMed:19340312, ECO:0000269|PubMed:24656816, ECO:0000269|PubMed:25773599}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8WX92}. SUBUNIT: The NELF complex is composed of NELFA, NELFB, NELFCD and NELFE; the N-terminus of NELFB binds to the NELFA:NELFCD subcomplex (By similarity). Binds RNA which may help to stabilize the NELF complex on nucleic acid (By similarity) Interacts with the first BRCT repeat of BRCA1 (By similarity). Interacts with KIAA1191 (By similarity). Isoform 1 and isoform 2 interact with NELFA, NELFCD and NELFE (PubMed:26010750). {ECO:0000250|UniProtKB:Q8WX92, ECO:0000269|PubMed:26010750}. TISSUE SPECIFICITY: Isoform 1 is expressed in the kidney, liver, adipose and lung (PubMed:26010750). Isoform 2 is widely expressed (PubMed:26010750). {ECO:0000269|PubMed:26010750}. +Q6P5H2 NEST_MOUSE Nestin 1864 207,124 Alternative sequence (1); Chain (1); Domain (1); Modified residue (34); Region (9); Sequence conflict (27) FUNCTION: Required for brain and eye development. Promotes the disassembly of phosphorylated vimentin intermediate filaments (IF) during mitosis and may play a role in the trafficking and distribution of IF proteins and other cellular factors to daughter cells during progenitor cell division (By similarity). Required for survival, renewal and mitogen-stimulated proliferation of neural progenitor cells. {ECO:0000250, ECO:0000269|PubMed:20963821}. PTM: Constitutively phosphorylated. This increases during mitosis when the cytoplasmic intermediate filament network is reorganized (By similarity). {ECO:0000250}. SUBUNIT: Forms homodimers and homotetramers in vitro. In mixtures with other intermediate filament proteins such as vimentin and alpha-internexin, this protein preferentially forms heterodimers which can assemble to form intermediate filaments if nestin does not exceed 25%. Interacts with FHOD3 (By similarity). {ECO:0000250}. +O88942 NFAC1_MOUSE Nuclear factor of activated T-cells, cytoplasmic 1 (NF-ATc1) (NFATc1) (NFAT transcription complex cytosolic component) (NF-ATc) (NFATc) 717 77,833 Alternative sequence (2); Chain (1); DNA binding (1); Domain (1); Modified residue (5); Motif (3); Region (3); Repeat (3) FUNCTION: Plays a role in the inducible expression of cytokine genes in T-cells, especially in the induction of the IL-2 or IL-4 gene transcription. Also controls gene expression in embryonic cardiac cells. Could regulate not only the activation and proliferation but also the differentiation and programmed death of T-lymphocytes as well as lymphoid and non-lymphoid cells (By similarity). Required for osteoclastogenesis and regulates many genes important for osteoclast differentiation and function (PubMed:26644563). {ECO:0000250|UniProtKB:O95644, ECO:0000303|PubMed:26644563}. PTM: Phosphorylated by NFATC-kinase and GSK3B; phosphorylation induces NFATC1 nuclear exit and dephosphorylation by calcineurin promotes nuclear import. Phosphorylation by PKA and DYRK2 negatively modulates nuclear accumulation, and promotes subsequent phosphorylation by GSK3B or casein kinase 1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28341745}. Nucleus {ECO:0000269|PubMed:24039232, ECO:0000269|PubMed:26644563, ECO:0000269|PubMed:28341745}. Note=Cytoplasmic for the phosphorylated form and nuclear after activation that is controlled by calcineurin-mediated dephosphorylation. Rapid nuclear exit of NFATC is thought to be one mechanism by which cells distinguish between sustained and transient calcium signals. The subcellular localization of NFATC plays a key role in the regulation of gene transcription (By similarity). Nuclear translocation of NFATC1 is enhanced in the presence of TNFSF11 (PubMed:26644563). Nuclear translocation is decreased in the presence of FBN1 which can bind and sequester TNFSF11 (PubMed:24039232). {ECO:0000250|UniProtKB:O95644, ECO:0000269|PubMed:24039232, ECO:0000269|PubMed:26644563}. SUBUNIT: Member of the multicomponent NFATC transcription complex that consists of at least two components, a pre-existing cytoplasmic component NFATC2 and an inducible nuclear component NFATC1. Other members such as NFATC4, NFATC3 or members of the activating protein-1 family, MAF, GATA4 and Cbp/p300 can also bind the complex. NFATC proteins bind to DNA as monomers (By similarity). Interacts with HOMER2 and HOMER3 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O95644}. DOMAIN: Rel Similarity Domain (RSD) allows DNA-binding and cooperative interactions with AP1 factors. {ECO:0000250}.; DOMAIN: The N-terminal transactivation domain (TAD-A) binds to and is activated by Cbp/p300. The dephosphorylated form contains two unmasked nuclear localization signals (NLS), which allow translocation of the protein to the nucleus (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in spleen, lung, skeletal muscle, thymus and skin (PubMed:9388475). Weakly expressed in heart, brain, liver and kidney. Not expressed in testis (PubMed:10072529). {ECO:0000269|PubMed:10072529, ECO:0000269|PubMed:9388475}. +P60761 NEUG_MOUSE Neurogranin (Ng) (RC3) [Cleaved into: NEUG(55-78)] 78 7,496 Chain (1); Disulfide bond (1); Domain (2); Helix (1); Modified residue (4); Mutagenesis (1); Peptide (1); Site (1) FUNCTION: Regulates the affinity of calmodulin for calcium. Involved in synaptic plasticity and spatial learning. {ECO:0000269|PubMed:11016969}. PTM: Disulfide bond formation is redox-sensitive. The cysteine residues are readily oxidized by several nitric acid (NO) donors and other oxidants to form intramolecular disulfide. Cys-51 can form a disulfide with any other of the cysteine residues with an order of reactivity Cys-9 > Cys-4 > Cys-3 (By similarity). {ECO:0000250}.; PTM: Phosphorylated at Ser-36 by PHK and PKC, phosphorylation prevents interaction with Calmodulin and interrupts several learning- and memory-associated functions. {ECO:0000269|PubMed:23462742}. SUBCELLULAR LOCATION: Cytoplasm. Cell junction, synapse. Cell projection, dendritic spine. Note=Restricted to dendritic spines of a subset of neurons. {ECO:0000250}. SUBUNIT: Interacts with apo-calmodulin; this interaction decreases the affinity of calmodulin for calcium ions. {ECO:0000269|PubMed:23462742}. DOMAIN: Neurogranin is intrinsically unstructured; however, upon binding with CaM, The IQ domain adopts a helical conformation. +Q8VCB1 NDC1_MOUSE Nucleoporin NDC1 (Transmembrane protein 48) 673 75,409 Chain (1); Modified residue (8); Topological domain (7); Transmembrane (6) TRANSMEM 26 46 Helical; Name=1. {ECO:0000255}.; TRANSMEM 72 92 Helical; Name=2. {ECO:0000255}.; TRANSMEM 116 136 Helical; Name=3. {ECO:0000255}.; TRANSMEM 167 187 Helical; Name=4. {ECO:0000255}.; TRANSMEM 227 247 Helical; Name=5. {ECO:0000255}.; TRANSMEM 262 282 Helical; Name=6. {ECO:0000255}. TOPO_DOM 1 25 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 47 71 Perinuclear space. {ECO:0000255}.; TOPO_DOM 93 115 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 137 166 Perinuclear space. {ECO:0000255}.; TOPO_DOM 188 226 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 248 261 Perinuclear space. {ECO:0000255}.; TOPO_DOM 283 673 Cytoplasmic. {ECO:0000255}. FUNCTION: Component of the nuclear pore complex (NPC), which plays a key role in de novo assembly and insertion of NPC in the nuclear envelope. Required for NPC and nuclear envelope assembly, possibly by forming a link between the nuclear envelope membrane and soluble nucleoporins, thereby anchoring the NPC in the membrane (By similarity). {ECO:0000250}. PTM: Phosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nuclear pore complex {ECO:0000250}. Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Central core structure of the nuclear pore complex. {ECO:0000250}. SUBUNIT: Interacts with the NUP35/NUP53. {ECO:0000250|UniProtKB:Q6AXN4}. +Q8BNY6 NCS1_MOUSE Neuronal calcium sensor 1 (NCS-1) (Frequenin homolog) 190 21,879 Calcium binding (3); Chain (1); Domain (4); Initiator methionine (1); Lipidation (1); Region (1); Sequence conflict (1) FUNCTION: Neuronal calcium sensor, regulator of G protein-coupled receptor phosphorylation in a calcium dependent manner. Directly regulates GRK1 (RHOK), but not GRK2 to GRK5. Can substitute for calmodulin (By similarity). Stimulates PI4KB kinase activity (By similarity). Involved in long-term synaptic plasticity through its interaction with PICK1 (By similarity). May also play a role in neuron differentiation through inhibition of the activity of N-type voltage-gated calcium channel (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:P62166}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250|UniProtKB:P62166}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P62166}. Cytoplasm {ECO:0000250|UniProtKB:P62168}. Cell membrane {ECO:0000250|UniProtKB:P62166}; Peripheral membrane protein {ECO:0000250|UniProtKB:P62166}. Membrane {ECO:0000250|UniProtKB:P62166, ECO:0000250|UniProtKB:P62168}; Lipid-anchor {ECO:0000250|UniProtKB:P62166}. Note=Associated with Golgi stacks. Post-synaptic densities of dendrites, and in the pre-synaptic nerve terminal at neuromuscular junctions. {ECO:0000250|UniProtKB:P62166}. SUBUNIT: Interacts with KCND2, ARF1, ARF3, ARF5 and ARF6 (By similarity). Interacts in a calcium-independent manner with PI4KB. This binding competes with CALN2/CABP7 binding to PI4KB (By similarity). Interacts in a calcium-dependent manner with PICK1 (via AH domain) (By similarity). Interacts with IL1RAPL1 (By similarity). {ECO:0000250}. +Q91W39 NCOA5_MOUSE Nuclear receptor coactivator 5 (NCoA-5) (Coactivator independent of AF-2) (CIA) 579 65,319 Chain (1); Compositional bias (1); Modified residue (14); Motif (1); Region (2) FUNCTION: Nuclear receptor coregulator that can have both coactivator and corepressor functions. Interacts with nuclear receptors for steroids (ESR1 and ESR2) independently of the steroid binding domain (AF-2) of the ESR receptors, and with the orphan nuclear receptor NR1D2. Involved in the coactivation of nuclear steroid receptors (ER) as well as the corepression of MYC in response to 17-beta-estradiol (E2) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Binds HTATIP2/TIP30. Interacts with YLPM1. Forms a complex with ILF2, ILF3, YLPM1, KHDRBS1, RBMX and PPP1CA (By similarity). {ECO:0000250}. DOMAIN: Contains one Leu-Xaa-Xaa-Leu-Leu (LxxLL) motif that is essential for the association with nuclear receptors. {ECO:0000250}. +P70182 PI51A_MOUSE Phosphatidylinositol 4-phosphate 5-kinase type-1 alpha (PIP5K1-alpha) (PtdIns(4)P-5-kinase 1 alpha) (EC 2.7.1.68) (68 kDa type I phosphatidylinositol 4-phosphate 5-kinase) (Phosphatidylinositol 4-phosphate 5-kinase type I alpha) (PIP5KIalpha) (Phosphatidylinositol 4-phosphate 5-kinase type I beta) (PI4P5KIbeta) 546 60,485 Alternative sequence (2); Chain (1); Cross-link (1); Domain (1); Sequence conflict (4) FUNCTION: Catalyzes the phosphorylation of phosphatidylinositol 4-phosphate (PtdIns4P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). PtdIns(4,5)P2 is involved in a variety of cellular processes and is the substrate to form phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3), another second messenger. The majority of PtdIns(4,5)P2 is thought to occur via type I phosphatidylinositol 4-phosphate 5-kinases given the abundance of PtdIns4P. Participates in a variety of cellular processes such as actin cytoskeleton organization, cell adhesion, migration and phagocytosis. Required for membrane ruffling formation, actin organization and focal adhesion formation during directional cell migration by controlling integrin-induced translocation of RAC1 to the plasma membrane. Together with PIP5K1C is required for phagocytosis, but they regulate different types of actin remodeling at sequential steps. Promotes particle ingestion by activating WAS that induces Arp2/3 dependent actin polymerization at the nascent phagocytic cup. Together with PIP5K1B is required after stimulation of G-protein coupled receptors for stable platelet adhesion. Plays a role during calcium-induced keratinocyte differentiation. Recruited to the plasma membrane by the E-cadherin/beta-catenin complex where it provides the substrate PtdIns(4,5)P2 for the production of PtdIns(3,4,5)P3, diacylglycerol and inositol 1,4,5-trisphosphate that mobilize internal calcium and drive keratinocyte differentiation. Together with PIP5K1C have a role during embryogenesis. Functions also in the nucleus where acts as an activator of TUT1 adenylyltransferase activity in nuclear speckles, thereby regulating mRNA polyadenylation of a select set of mRNAs (PubMed:10679324, PubMed:18772378, PubMed:19153220, PubMed:20622009, PubMed:8798574). Positively regulates insulin-induced translocation of SLC2A4 to the cell membrane in adipocytes (PubMed:27739494). {ECO:0000269|PubMed:10679324, ECO:0000269|PubMed:18772378, ECO:0000269|PubMed:19153220, ECO:0000269|PubMed:20622009, ECO:0000269|PubMed:27739494, ECO:0000269|PubMed:8798574}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20622009}. Nucleus speckle {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:20622009}. Cell projection, ruffle {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q99755}. Nucleus {ECO:0000250|UniProtKB:Q99755}. Note=Colocalizes with RAC1 at actin-rich membrane ruffles. Localizes to nuclear speckles and associates with TUT1 to regulate polyadenylation of selected mRNAs. {ECO:0000250}. SUBUNIT: Interacts with RAC1 (PubMed:10679324). Interacts with TUT1 (By similarity). Forms a complex with CDH1/E-cadherin, CTNNB1/beta-catenin and CTNND1 at the plasma membrane upon calcium stimulation (By similarity). Found in a ternary complex with IRS1 and DGKZ in the absence of insulin stimulation (PubMed:27739494). Interacts with DGKZ (By similarity). {ECO:0000250|UniProtKB:Q99755, ECO:0000269|PubMed:10679324, ECO:0000269|PubMed:27739494}. TISSUE SPECIFICITY: Highest expression in brain. Also detected in skeletal muscle, testis, brain and lung. {ECO:0000269|PubMed:20622009, ECO:0000269|PubMed:8798574}. +Q99MH5 NDK5_MOUSE Nucleoside diphosphate kinase homolog 5 (NDK-H 5) (NDP kinase homolog 5) (nm23-M5) 211 24,002 Active site (1); Alternative sequence (2); Chain (1); Sequence conflict (1) FUNCTION: Does not seem to have NDK kinase activity. Confers protection from cell death by Bax and alters the cellular levels of several antioxidant enzymes including Gpx5. May play a role in spermiogenesis by increasing the ability of late-stage spermatids to eliminate reactive oxygen species. {ECO:0000269|PubMed:12788088}. TISSUE SPECIFICITY: Expressed predominantly in germ cells of the testis. Not expressed in testicular somatic cells. {ECO:0000269|PubMed:12788088}. +O54714 PIAS3_MOUSE E3 SUMO-protein ligase PIAS3 (EC 2.3.2.-) (E3 SUMO-protein transferase PIAS3) (Protein inhibitor of activated STAT protein 3) 628 68,318 Alternative sequence (2); Chain (1); Compositional bias (1); Cross-link (6); Domain (2); Motif (1); Mutagenesis (7); Region (2); Zinc finger (1) Protein modification; protein sumoylation. FUNCTION: Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor. Plays a crucial role as a transcriptional coregulation in various cellular pathways, including the STAT pathway and the steroid hormone signaling pathway. Repressor of STAT3 signaling via inhibiting STAT3 DNA-binding and suppressing cell growth. Repressor of MITF transcriptional activity. Enhances the sumoylation of MTA1 and may participate in its paralog-selective sumoylation. Sumoylates CCAR2 which promotes its interaction with SIRT1 (By similarity). Diminishes the sumoylation of ZFHX3 by preventing the colocalization of ZFHX3 with SUMO1 in the nucleus (By similarity). {ECO:0000250|UniProtKB:Q9Y6X2, ECO:0000269|PubMed:11060035, ECO:0000269|PubMed:11709556, ECO:0000269|PubMed:14596924}. PTM: Sumoylated. {ECO:0000269|PubMed:12387893}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11060035, ECO:0000269|PubMed:11709556}. Nucleus {ECO:0000269|PubMed:11060035, ECO:0000269|PubMed:11709556, ECO:0000269|PubMed:14596924}. Nucleus speckle {ECO:0000269|PubMed:12077349}. Note=Colocalizes with MITF in the nucleus (PubMed:11709556). Colocalizes with GFI1 in nuclear dots (PubMed:11060035). Colocalizes with SUMO1 in nuclear granules (PubMed:12077349). {ECO:0000269|PubMed:11060035, ECO:0000269|PubMed:11709556, ECO:0000269|PubMed:12077349}. SUBUNIT: Monomer. Interacts with PLAG1 and ZFHX3. Interacts with STAT5A; the interaction occurs on stimulation by PRL (By similarity). Binds SUMO1 and UBE2I. Interacts with AR, BCL11A, HMGA2, IRF1 and NCOA2. Interacts with MITF; the interaction inhibits the transcriptional activity of MITF. Interacts with STAT3; the interaction occurs on stimulation by IL6, CNTF or OSM and inhibits the DNA binding activity of STAT3. Interacts with GFI1; the interaction relieves the inhibitory effect of PIAS3 on STAT3-mediated transcriptional activity. Interacts with MTA1. Interacts with CCAR2 (via N-terminus) (By similarity). Interacts with TRIM8 (By similarity). {ECO:0000250|UniProtKB:Q9Y6X2, ECO:0000269|PubMed:11060035, ECO:0000269|PubMed:11117529, ECO:0000269|PubMed:11390395, ECO:0000269|PubMed:11709556, ECO:0000269|PubMed:12077349, ECO:0000269|PubMed:12208521, ECO:0000269|PubMed:12387893, ECO:0000269|PubMed:18681895, ECO:0000269|PubMed:9388184}. DOMAIN: The LXXLL motif is a transcriptional coregulator signature. TISSUE SPECIFICITY: Expressed in kidney, heart, spleen, brain and cerebellum; weak expression, if any, in liver and lung. {ECO:0000269|PubMed:10854042, ECO:0000269|PubMed:14596924}. +Q62425 NDUA4_MOUSE Cytochrome c oxidase subunit NDUFA4 82 9,327 Chain (1); Modified residue (2) FUNCTION: Cytochrome c oxidase (COX, complex IV) is the terminal component of the mitochondrial respiratory chain that catalyzes the reduction of oxygen to water. Required for complex IV maintenance (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Matrix side {ECO:0000250}. SUBUNIT: Component of the cytochrome c oxidase complex (COX, complex IV). {ECO:0000269|PubMed:11994422}. +Q8BG18 NECA1_MOUSE N-terminal EF-hand calcium-binding protein 1 (EF-hand calcium-binding protein 1) 352 40,934 Calcium binding (1); Chain (1); Coiled coil (2); Domain (3); Modified residue (3); Sequence conflict (1) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12044471}. SUBUNIT: Interacts with STX1. May interact with CPNE6. {ECO:0000250|UniProtKB:Q8N987}. TISSUE SPECIFICITY: Expressed in brain (at protein level). Expressed in the cerebral cortex only in layer 4, thalamic nuclei (the mediodorsal nucleus), hippocampus (a small band of pyramidal neurons at the boundary between CA1 and CA3), interneurons interspersed throughout the hippocampus proper, interneurons in the hilus, bodies of the neurons but also their dendritic projections (at protein level). {ECO:0000269|PubMed:12044471}. +P51954 NEK1_MOUSE Serine/threonine-protein kinase Nek1 (EC 2.7.11.1) (Never in mitosis A-related kinase 1) (NimA-related protein kinase 1) 1203 136,690 Active site (1); Binding site (1); Chain (1); Domain (1); Modified residue (12); Mutagenesis (1); Nucleotide binding (1) FUNCTION: Phosphorylates serines and threonines, but also appears to possess tyrosine kinase activity (PubMed:1382974). Involved in DNA damage checkpoint control and for proper DNA damage repair (PubMed:18843199). In response to injury that includes DNA damage, NEK1 phosphorylates VDAC1 to limit mitochondrial cell death (By similarity). May be implicated in the control of meiosis (PubMed:1382974). Involved in cilium assembly (By similarity). {ECO:0000250|UniProtKB:Q96PY6, ECO:0000269|PubMed:1382974, ECO:0000269|PubMed:18843199}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:16267153}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:16267153}. Note=Associated with the pericentriolar material (By similarity). Localizes to centrosome during interphase and mitosis (PubMed:16267153). {ECO:0000250|UniProtKB:Q96PY6, ECO:0000269|PubMed:16267153}. SUBUNIT: Binds to SPERT (PubMed:12204287). Found in a complex with CFAP410, NEK1 and SPATA7 (By similarity). Interacts with CFAP410 (By similarity). Interacts (via Ser-997 phosphorylated form) with 14-3-3 proteins (PubMed:28235073). {ECO:0000250|UniProtKB:Q96PY6, ECO:0000269|PubMed:12204287, ECO:0000269|PubMed:28235073}. TISSUE SPECIFICITY: Predominantly in testes (germ cells and Sertoli cells). Lower levels in ovary (oocytes and granulosa cells), thymus and lung. {ECO:0000269|PubMed:1382974}. +P25233 NECD_MOUSE Necdin 325 36,832 Chain (1); Domain (1); Natural variant (1) FUNCTION: Growth suppressor that facilitates the entry of the cell into cell cycle arrest. Functionally similar to the retinoblastoma protein it binds to and represses the activity of cell-cycle-promoting proteins such as SV40 large T antigen, adenovirus E1A, and the transcription factor E2F. Necdin also interacts with p53 and works in an additive manner to inhibit cell growth. Functions also as transcription factor and binds directly to specific guanosine-rich DNA sequences. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10965153}. Nucleus, nucleoplasm {ECO:0000269|PubMed:10965153}. Nucleus matrix {ECO:0000269|PubMed:10965153}. Note=Mainly cytoplasmic. Translocates to the nucleus where it is found associated with the nuclear matrix. SUBUNIT: Binds to the transactivation domains of E2F1 and p53. Binds also SV40 large T antigen and adenovirus E1A. Interacts with nucleobindin 1 and 2. {ECO:0000269|PubMed:10347180, ECO:0000269|PubMed:9422723}. TISSUE SPECIFICITY: Brain specific. Not detected in other tissues. Expressed in postmitotic neurons. In adult brain the highest expression is in hypothalamus. Highly expressed in thalamus and midbrain. Relatively low levels are in cerebral cortex, hippocampus, striatum, olfactory bulb, cerebellum, pons and spinal cord. Also detected in neurally differentiated embryonal carcinoma cells. +Q9JLB9 NECT3_MOUSE Nectin-3 (Nectin cell adhesion molecule 3) (Poliovirus receptor-related protein 3) (CD antigen CD113) 549 60,583 Alternative sequence (4); Beta strand (16); Chain (1); Disulfide bond (3); Domain (3); Glycosylation (6); Helix (3); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 405 425 Helical. {ECO:0000255}. TOPO_DOM 58 404 Extracellular. {ECO:0000255}.; TOPO_DOM 426 549 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a role in cell-cell adhesion through heterophilic trans-interactions with nectins-like or other nectins, such as trans-interaction with NECTIN2 at Sertoli-spermatid junctions. Trans-interaction with PVR induces activation of CDC42 and RAC small G proteins through common signaling molecules such as SRC and RAP1. Also involved in the formation of cell-cell junctions, including adherens junctions and synapses. Induces endocytosis-mediated down-regulation of PVR from the cell surface, resulting in reduction of cell movement and proliferation. Plays a role in the morphology of the ciliary body. {ECO:0000269|PubMed:10744716, ECO:0000269|PubMed:11827984, ECO:0000269|PubMed:12121624, ECO:0000269|PubMed:12558799, ECO:0000269|PubMed:16128743}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000269|PubMed:11827984}. SUBUNIT: Cis- and trans-homodimer. Can form trans-heterodimers with NECTIN1, NECTIN2, PVR, IGSF4B/Necl-1 and with IGSF4. Interaction between NECTIN1 and NECTIN3 on the pre- and postsynaptic sites, respectively, initiates the formation of puncta adherentia junctions between axons and dendrites. Interacts (via Cytoplasmic domain) with AFDN, providing a connection with the actin cytoskeleton. Binds with low affinity to TIGIT. {ECO:0000269|PubMed:10744716, ECO:0000269|PubMed:11827984, ECO:0000269|PubMed:12826663, ECO:0000269|PubMed:15741237, ECO:0000269|PubMed:16128743}. TISSUE SPECIFICITY: Ubiquitous with high expression in testes. Localized in spermatids at Sertoli-spermatid junctions. Expressed in ovarian granulosa cells, but only faintly expressed after ovulation. {ECO:0000269|PubMed:10744716, ECO:0000269|PubMed:12121624}. +P70257 NFIX_MOUSE Nuclear factor 1 X-type (NF1-X) (Nuclear factor 1/X) (CCAAT-box-binding transcription factor) (CTF) (Nuclear factor I/X) (NF-I/X) (NFI-X) (TGGCA-binding protein) 488 53,394 Alternative sequence (3); Chain (1); Cross-link (1); DNA binding (1); Modified residue (9); Sequence conflict (1) FUNCTION: Recognizes and binds the palindromic sequence 5'-TTGGCNNNNNGCCAA-3' present in viral and cellular promoters and in the origin of replication of adenovirus type 2. These proteins are individually capable of activating transcription and replication. Isoform NFIX1 acts as a transcriptional activator while isoform NFIX3 acts as a repressor. {ECO:0000269|PubMed:8581067}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Binds DNA as a homodimer. +Q8CJC5 NEUL3_MOUSE E3 ubiquitin-protein ligase NEURL3 (EC 2.3.2.27) (Lung-inducible neuralized-related C3CH4 RING domain protein) (Neuralized-like protein 3) (RING-type E3 ubiquitin transferase NEURL3) 254 28,040 Alternative sequence (2); Chain (1); Domain (1); Erroneous initiation (1); Sequence conflict (1); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase. Seems to utilize UBE2E1. In vitro, generates polyubiquitin chains via non-canonical lysine residues suggesting that it is not involved in tagging substrates for proteasomal degradation. {ECO:0000269|PubMed:15936721}. TISSUE SPECIFICITY: Expressed in alveolar epithelial type II cells. {ECO:0000269|PubMed:15936721}. +Q3UQ22 NET5_MOUSE Netrin-5 (Netrin-1-like protein) 452 48,837 Chain (1); Disulfide bond (11); Domain (3); Frameshift (1); Glycosylation (1); Signal peptide (1) FUNCTION: Plays a role in neurogenesis. Prevents motor neuron cell body migration out of the neural tube. {ECO:0000269|PubMed:26858598}. SUBCELLULAR LOCATION: Secreted {ECO:0000255}. +O70477 PKNX1_MOUSE Homeobox protein PKNOX1 (PBX/knotted homeobox 1) 436 47,539 Chain (1); DNA binding (1); Erroneous initiation (1); Modified residue (2); Sequence conflict (1) FUNCTION: Activates transcription in the presence of PBX1A and HOXA1. {ECO:0000269|PubMed:29465778}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q60795 NF2L2_MOUSE Nuclear factor erythroid 2-related factor 2 (NF-E2-related factor 2) (NFE2-related factor 2) (Nuclear factor, erythroid derived 2, like 2) 597 66,901 Chain (1); Domain (1); Helix (3); Modified residue (4); Region (3); Turn (1) FUNCTION: Transcription activator that binds to antioxidant response (ARE) elements in the promoter regions of target genes. Important for the coordinated up-regulation of genes in response to oxidative stress and the regulation of cellular redox conditions. May be involved in the transcriptional activation of genes of the beta-globin cluster by mediating enhancer activity of hypersensitive site 2 of the beta-globin locus control region. {ECO:0000269|PubMed:9887101}. PTM: Phosphorylation of Ser-40 by PKC in response to oxidative stress dissociates NFE2L2 from its cytoplasmic inhibitor KEAP1, promoting its translocation into the nucleus. {ECO:0000250|UniProtKB:O54968}.; PTM: Acetylation at Lys-588 and Lys-591 increases nuclear localization whereas deacetylation by SIRT1 enhances cytoplasmic presence. {ECO:0000250}.; PTM: Ubiquitinated by the KEAP1-CUL3-RBX1 E3 ubiquitin ligase complex and subject to proteasomal degradation. Ubiquitination is inhibited by sulforaphane (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:9887101}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:9887101}. Note=Cytosolic under unstressed conditions, translocates into the nucleus upon induction by electrophilic agents. {ECO:0000250|UniProtKB:Q16236}. SUBUNIT: Heterodimer. Forms a ternary complex with PGAM5 and KEAP1. Interacts with EEF1D at heat shock promoter elements (HSE). Interacts with KEAP1. Interacts via its leucine-zipper domain with the coiled-coil domain of PMF1. Interacts (via the bZIP domain) with MAFK; required for binding to antioxidant response elements (AREs) on DNA. Interacts with CHD6; involved in activation of the transcription. Interacts with ESRRB; represses NFE2L2 transcriptional activity (PubMed:17920186). {ECO:0000269|PubMed:11583586, ECO:0000269|PubMed:16507366, ECO:0000269|PubMed:17920186, ECO:0000269|PubMed:9887101}. TISSUE SPECIFICITY: Widely expressed. Highest expression in liver, skeletal muscle, luminal cells of the stomach and intestine, lining of the bronchi and alveoli, and in renal tubules; followed by heart, spleen, testis and brain. +P01139 NGF_MOUSE Beta-nerve growth factor (Beta-NGF) 241 27,077 Beta strand (9); Chain (1); Disulfide bond (3); Erroneous initiation (5); Glycosylation (2); Helix (1); Propeptide (1); Sequence conflict (1); Signal peptide (1); Turn (1) FUNCTION: Nerve growth factor is important for the development and maintenance of the sympathetic and sensory nervous systems. Extracellular ligand for the NTRK1 and NGFR receptors, activates cellular signaling cascades through those receptor tyrosine kinase to regulate neuronal proliferation, differentiation and survival. Inhibits metalloproteinase dependent proteolysis of platelet glycoprotein VI. {ECO:0000250|UniProtKB:P01138}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Homodimer. Interacts with ADAM10 in a divalent cation-dependent manner. {ECO:0000250|UniProtKB:P01138}. +Q9WTM4 NF2L3_MOUSE Nuclear factor erythroid 2-related factor 3 (NF-E2-related factor 3) (NFE2-related factor 3) (Nuclear factor, erythroid derived 2, like 3) 660 72,707 Chain (1); Domain (1); Region (2) FUNCTION: Activates erythroid-specific, globin gene expression. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}. SUBUNIT: Heterodimer with MAFG, MAFK and other small MAF proteins that binds to the MAF recognition elements (MARE). {ECO:0000250}. TISSUE SPECIFICITY: High level expression in brain, thymus, testis and placenta. Medium level expression in uterus, stomach and lung. Low level expression in kidney. No expression in heart, liver, spleen and ovary. {ECO:0000269|PubMed:15060151}. +Q9D0T1 NH2L1_MOUSE NHP2-like protein 1 (Fertilization antigen 1) (FA-1) (High mobility group-like nuclear protein 2 homolog 1) (Sperm-specific antigen 1) (U4/U6.U5 small nuclear ribonucleoprotein SNU13) (U4/U6.U5 tri-snRNP 15.5 kDa protein) [Cleaved into: NHP2-like protein 1, N-terminally processed] 128 14,174 Chain (2); Frameshift (1); Initiator methionine (1); Modified residue (4); Region (2); Sequence conflict (1); Site (2) FUNCTION: Involved in pre-mRNA splicing as component of the spliceosome. Binds to the 5'-stem-loop of U4 snRNA and thereby contributes to spliceosome assembly. The protein undergoes a conformational change upon RNA-binding. {ECO:0000250|UniProtKB:P55769}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P55769}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P55769}. Note=Concentrated in the dense fibrillar component of the nucleolus. {ECO:0000250|UniProtKB:P55769}. SUBUNIT: Identified in the spliceosome B complex. Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, WDR57, SNRNP40, DDX23, CD2BP2, PPIH, NHP2L1, EFTUD2, SART1 and USP39. Interacts with RAD17 and PRPF31. The complex formed by SNU13 and PRPF31 binds U4 snRNA. The complex formed by SNU13 and PRPF31 binds also U4atac snRNA, a characteristic component of specific, less abundant spliceosomal complexes. {ECO:0000250|UniProtKB:P55769}. +Q3T9M1 MFS2B_MOUSE Major facilitator superfamily domain-containing protein 2B (mMfsd2b) 494 52,797 Alternative sequence (3); Chain (1); Erroneous termination (1); Sequence conflict (1); Transmembrane (10) TRANSMEM 103 123 Helical. {ECO:0000255}.; TRANSMEM 140 160 Helical. {ECO:0000255}.; TRANSMEM 179 199 Helical. {ECO:0000255}.; TRANSMEM 223 243 Helical. {ECO:0000255}.; TRANSMEM 277 297 Helical. {ECO:0000255}.; TRANSMEM 310 330 Helical. {ECO:0000255}.; TRANSMEM 339 359 Helical. {ECO:0000255}.; TRANSMEM 360 380 Helical. {ECO:0000255}.; TRANSMEM 402 422 Helical. {ECO:0000255}.; TRANSMEM 449 469 Helical. {ECO:0000255}. FUNCTION: Cation-dependent lipid transporter that specifically mediates export of sphingosine-1-phosphate in red blood cells and platelets (PubMed:29045386). Sphingosine-1-phosphate is a signaling sphingolipid and its export from red blood cells into in the plasma is required for red blood cell morphology (PubMed:29045386). Does not transport lysophosphatidylcholine (LPC) (PubMed:29045386). {ECO:0000269|PubMed:29045386}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:29045386}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to the cell membrane and intracellular membranes. {ECO:0000269|PubMed:29045386}. TISSUE SPECIFICITY: Widely expressed with highest expression in spleen, lung and testis (PubMed:18694395). Predominantly expressed in erythroid lineages giving rise to erythrocytes and platelets, but absent in lymphoid lineages (PubMed:29045386). {ECO:0000269|PubMed:18694395, ECO:0000269|PubMed:29045386}. +Q921Y4 MFSD5_MOUSE Molybdate-anion transporter (Major facilitator superfamily domain-containing protein 5) (Molybdate transporter 2 homolog) 450 49,679 Chain (1); Transmembrane (12) TRANSMEM 1 21 Helical. {ECO:0000255}.; TRANSMEM 38 58 Helical. {ECO:0000255}.; TRANSMEM 79 99 Helical. {ECO:0000255}.; TRANSMEM 128 148 Helical. {ECO:0000255}.; TRANSMEM 167 187 Helical. {ECO:0000255}.; TRANSMEM 191 211 Helical. {ECO:0000255}.; TRANSMEM 249 269 Helical. {ECO:0000255}.; TRANSMEM 278 298 Helical. {ECO:0000255}.; TRANSMEM 311 331 Helical. {ECO:0000255}.; TRANSMEM 344 364 Helical. {ECO:0000255}.; TRANSMEM 376 396 Helical. {ECO:0000255}.; TRANSMEM 409 429 Helical. {ECO:0000255}. FUNCTION: Mediates high-affinity intracellular uptake of the rare oligo-element molybdenum. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q8CIC2 NUPL2_MOUSE Nucleoporin-like protein 2 (NLP-1) 420 44,337 Alternative sequence (2); Chain (1); Compositional bias (1); Frameshift (1); Region (1); Repeat (11); Sequence conflict (7); Zinc finger (1) FUNCTION: Required for the export of mRNAs containing poly(A) tails from the nucleus into the cytoplasm. {ECO:0000250}. PTM: O-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:O15504}. Nucleus membrane {ECO:0000250|UniProtKB:O15504}; Peripheral membrane protein {ECO:0000250|UniProtKB:O15504}; Cytoplasmic side {ECO:0000250|UniProtKB:O15504}. Note=Excluded from the nucleolus. {ECO:0000250|UniProtKB:O15504}. SUBUNIT: Probable component of the nuclear pore complex (NPC). Interacts with nuclear export protein NXF1. Interacts with GLE1. Able to form a heterotrimer with NUP155 and GLE1 in vitro (By similarity). {ECO:0000250}. DOMAIN: The FG repeats are interaction sites for karyopherins (importins, exportins) and form probably an affinity gradient, guiding the transport proteins unidirectionally with their cargo through the NPC. {ECO:0000250}. +Q9WVL5 MORC1_MOUSE MORC family CW-type zinc finger protein 1 (Protein microrchidia) 950 108,310 Chain (1); Coiled coil (2); Zinc finger (1) FUNCTION: Required for spermatogenesis. {ECO:0000269|PubMed:10369865}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10369865}. TISSUE SPECIFICITY: Expressed at very low level in male germ cells. {ECO:0000269|PubMed:10369865}. +Q9D281 NXP20_MOUSE Protein Noxp20 (Nervous system overexpressed protein 20) (Protein FAM114A1) 569 61,013 Chain (1); Compositional bias (2); Modified residue (2); Sequence conflict (4) FUNCTION: May play a role in neuronal cell development. SUBCELLULAR LOCATION: Cytoplasm. TISSUE SPECIFICITY: Over-expressed in brain. Also detected in lung, stomach, and in a lower extent in testis and thymus. +Q91ZV4 MOGT1_MOUSE 2-acylglycerol O-acyltransferase 1 (EC 2.3.1.22) (Acyl-CoA:monoacylglycerol acyltransferase 1) (MGAT1) (Diacylglycerol acyltransferase 2-like protein 1) (Monoacylglycerol O-acyltransferase 1) 335 38,791 Chain (1); Glycosylation (1); Sequence conflict (3); Transmembrane (2) TRANSMEM 24 44 Helical. {ECO:0000255}.; TRANSMEM 104 124 Helical. {ECO:0000255}. Glycerolipid metabolism; triacylglycerol biosynthesis. FUNCTION: Catalyzes the formation of diacylglycerol from 2-monoacylglycerol and fatty acyl-CoA. Probably not involved in absorption of dietary fat in the small intestine. {ECO:0000269|PubMed:12077311}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305|PubMed:12077311}; Multi-pass membrane protein {ECO:0000305|PubMed:12077311}. TISSUE SPECIFICITY: Expressed at high level in kidney and stomach. Expressed at lower level in brown and white adipose tissue, uterus and liver. Not detected in small intestine. {ECO:0000269|PubMed:12077311}. +Q9CXI3 MOXD1_MOUSE DBH-like monooxygenase protein 1 (EC 1.14.17.-) (DBH-related protein) (Monooxygenase X) 613 69,678 Active site (2); Chain (1); Disulfide bond (5); Domain (1); Frameshift (1); Glycosylation (4); Metal binding (6); Sequence conflict (11); Signal peptide (1); Topological domain (1); Transmembrane (1) TRANSMEM 588 608 Helical. {ECO:0000255}. TOPO_DOM 20 587 Lumenal. {ECO:0000255}. PTM: N-glycosylated. {ECO:0000269|PubMed:15337741}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15337741}; Single-pass type I membrane protein {ECO:0000269|PubMed:15337741}. TISSUE SPECIFICITY: Broadly exprressed, with highest levels in salivary gland and ovary. {ECO:0000269|PubMed:15337741}. +Q5NC32 MOT11_MOUSE Monocarboxylate transporter 11 (MCT 11) (Solute carrier family 16 member 11) 447 45,235 Chain (1); Compositional bias (1); Erroneous gene model prediction (2); Erroneous initiation (1); Topological domain (2); Transmembrane (12) TRANSMEM 12 32 Helical. {ECO:0000255}.; TRANSMEM 54 74 Helical. {ECO:0000255}.; TRANSMEM 80 100 Helical. {ECO:0000255}.; TRANSMEM 107 127 Helical. {ECO:0000255}.; TRANSMEM 139 159 Helical. {ECO:0000255}.; TRANSMEM 162 182 Helical. {ECO:0000255}.; TRANSMEM 219 239 Helical. {ECO:0000255}.; TRANSMEM 249 269 Helical. {ECO:0000255}.; TRANSMEM 288 308 Helical. {ECO:0000255}.; TRANSMEM 330 350 Helical. {ECO:0000255}.; TRANSMEM 354 374 Helical. {ECO:0000255}.; TRANSMEM 383 403 Helical. {ECO:0000255}. TOPO_DOM 1 11 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 404 447 Cytoplasmic. {ECO:0000305}. FUNCTION: Proton-linked monocarboxylate transporter. It catalyzes the transport of pyruvate across the plasma membrane. Probably involved in hepatic lipid metabolism: overexpression results in an increase of triacylglycerol(TAG) levels, small increases in intracellular diacylglycerols and decreases in lysophosphatidylcholine, cholesterol ester and sphingomyelin lipids. {ECO:0000250|UniProtKB:Q8NCK7}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8NCK7}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q8NCK7}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Interacts with BSG. {ECO:0000250|UniProtKB:Q8NCK7}. +Q8BGC3 MOT12_MOUSE Monocarboxylate transporter 12 (MCT 12) (Solute carrier family 16 member 12) 486 53,152 Chain (1); Sequence conflict (3); Topological domain (2); Transmembrane (12) TRANSMEM 10 30 Helical. {ECO:0000255}.; TRANSMEM 58 78 Helical. {ECO:0000255}.; TRANSMEM 86 106 Helical. {ECO:0000255}.; TRANSMEM 115 135 Helical. {ECO:0000255}.; TRANSMEM 148 168 Helical. {ECO:0000255}.; TRANSMEM 177 197 Helical. {ECO:0000255}.; TRANSMEM 253 273 Helical. {ECO:0000255}.; TRANSMEM 289 309 Helical. {ECO:0000255}.; TRANSMEM 320 340 Helical. {ECO:0000255}.; TRANSMEM 353 373 Helical. {ECO:0000255}.; TRANSMEM 383 403 Helical. {ECO:0000255}.; TRANSMEM 410 430 Helical. {ECO:0000255}. TOPO_DOM 1 9 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 431 486 Cytoplasmic. {ECO:0000255}. FUNCTION: Proton-linked monocarboxylate transporter that mediates creatine transport across the plasma membrane. {ECO:0000250|UniProtKB:Q6ZSM3}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6ZSM3}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Interacts with BSG. {ECO:0000250|UniProtKB:Q6ZSM3}. TISSUE SPECIFICITY: Expressed in eye lens. {ECO:0000269|PubMed:21778275}. +Q8VF13 O1094_MOUSE Olfactory receptor 1094 (Olfactory receptor 179-7) 330 37,363 Chain (1); Disulfide bond (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 38 58 Helical; Name=1. {ECO:0000255}.; TRANSMEM 67 87 Helical; Name=2. {ECO:0000255}.; TRANSMEM 112 132 Helical; Name=3. {ECO:0000255}.; TRANSMEM 146 166 Helical; Name=4. {ECO:0000255}.; TRANSMEM 209 229 Helical; Name=5. {ECO:0000255}.; TRANSMEM 250 270 Helical; Name=6. {ECO:0000255}.; TRANSMEM 284 304 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 37 Extracellular. {ECO:0000255}.; TOPO_DOM 59 66 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 88 111 Extracellular. {ECO:0000255}.; TOPO_DOM 133 145 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 167 208 Extracellular. {ECO:0000255}.; TOPO_DOM 230 249 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 271 283 Extracellular. {ECO:0000255}.; TOPO_DOM 305 330 Cytoplasmic. {ECO:0000255}. FUNCTION: Potential odorant receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +P48964 MPIP1_MOUSE M-phase inducer phosphatase 1 (EC 3.1.3.48) (Dual specificity phosphatase Cdc25A) 514 57,806 Active site (1); Chain (1); Domain (1); Modified residue (13); Motif (2); Sequence conflict (14) FUNCTION: Tyrosine protein phosphatase which functions as a dosage-dependent inducer of mitotic progression. Directly dephosphorylates CDK1 and stimulates its kinase activity. Also dephosphorylates CDK2 in complex with cyclin E, in vitro (By similarity). Phosphorylation by PIM1 leads to an increase in phosphatase activity (By similarity). {ECO:0000250}. PTM: Phosphorylated by CHEK1 on Ser-75, Ser-123, Ser-172, Ser-271, Ser-284 and Thr-497 during checkpoint mediated cell cycle arrest. Also phosphorylated by CHEK2 on Ser-123, Ser-271, and Ser-284 during checkpoint mediated cell cycle arrest. Phosphorylation on Ser-172 and Thr-497 creates binding sites for YWHAE/14-3-3 epsilon which inhibits CDC25A. Phosphorylation on Ser-75, Ser-123, Ser-172, Ser-271 and Ser-284 may also promote ubiquitin-dependent proteolysis of CDC25A by the SCF complex. Phosphorylation of CDC25A at Ser-75 by CHEK1 primes it for subsequent phosphorylation at Ser-75, Ser-81 and Ser-87 by NEK11. Phosphorylation by NEK11 is required for BTRC-mediated polyubiquitination and degradation. Phosphorylation by PIM1 leads to an increase in phosphatase activity. Phosphorylated by PLK3 following DNA damage, leading to promote its ubiquitination and degradation (By similarity). {ECO:0000250}.; PTM: Ubiquitinated by the anaphase promoting complex/cyclosome (APC/C) ubiquitin ligase complex that contains FZR1/CDH1 during G1 phase leading to its degradation by the proteasome. Ubiquitinated by a SCF complex containing BTRC and FBXW11 during S phase leading to its degradation by the proteasome. Deubiquitination by USP17L2/DUB3 leads to its stabilization (By similarity). {ECO:0000250}. SUBUNIT: Interacts with CCNB1/cyclin B1. Interacts with YWHAE/14-3-3 epsilon when phosphorylated. Interacts with CUL1 specifically when CUL1 is neddylated and active. Interacts with BTRC/BTRCP1 and FBXW11/BTRCP2. Interactions with CUL1, BTRC and FBXW11 are enhanced upon DNA damage. Interacts with PIM1. Interacts with CHEK2; mediates CDC25A phosphorylation and degradation in response to infrared-induced DNA damages (By similarity). Interacts with HSP90AB1; prevents heat shock-mediated CDC25A degradation and contributes to cell cycle progression (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P30304}. DOMAIN: The phosphodegron motif mediates interaction with specific F-box proteins when phosphorylated. Putative phosphorylation sites at Ser-78 and Ser-81 appear to be essential for this interaction (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed in most developing tissue. High levels in the testis and lower levels in the ovary, particularly in germ cells. Lower levels also in kidney, liver, heart and muscle. {ECO:0000269|PubMed:7635051}. +Q9JLB2 MPP5_MOUSE MAGUK p55 subfamily member 5 (Protein associated with Lin-7 1) 675 77,229 Beta strand (6); Chain (1); Domain (5); Helix (5); Modified residue (4); Mutagenesis (20); Region (2) FUNCTION: May play a role in tight junctions biogenesis and in the establishment of cell polarity in epithelial cells. May modulate SC6A1/GAT1-mediated GABA uptake by stabilizing the transporter. Required for localization of EZR to the apical membrane of parietal cells and may play a role in the dynamic remodeling of the apical cytoskeleton. {ECO:0000269|PubMed:15677456}. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. Endomembrane system; Peripheral membrane protein. Cell junction, tight junction. Note=Localized to the tight junctions of epithelial cells and a subset of intracellular vesicles. Localized to the Purkinje cell body and axon. Localized to apical membrane domains of the outer limiting membrane junctions in the retina. Colocalizes with MPP1 in the retina at the outer limiting membrane (OLM) (By similarity). {ECO:0000250}. SUBUNIT: Heterodimer with MPP1. Interacts with MPP7. Forms a complex with CRB1 and MPP4. Component of a complex whose core is composed of ARHGAP17, AMOT, MPP5/PALS1, PATJ and PARD3/PAR3 (By similarity). Interacts with CRB3, EZR, PATJ, LIN7C, MPDZ, PARD6B and SC6A1. {ECO:0000250, ECO:0000269|PubMed:10753959, ECO:0000269|PubMed:11927608, ECO:0000269|PubMed:12527193, ECO:0000269|PubMed:12545177, ECO:0000269|PubMed:15140881, ECO:0000269|PubMed:15234345, ECO:0000269|PubMed:15316081, ECO:0000269|PubMed:15677456}. DOMAIN: The L27 domain 1 functions in targeting to the tight junctions by binding to PATJ.; DOMAIN: The PDZ domain binds to the C-terminus of SC6A1. TISSUE SPECIFICITY: Expressed in retina, lung, kidney, and heart. In the brain, expressed in the dentate gyrus of hippocampus, striatum and cerebellum (at protein level). Expressed in placenta, kidney, brain, heart, skeletal muscles, lung, pancreas and liver. {ECO:0000269|PubMed:10753959, ECO:0000269|PubMed:15234345, ECO:0000269|PubMed:15558731}. +Q8BVD5 MPP7_MOUSE MAGUK p55 subfamily member 7 576 65,540 Alternative sequence (7); Chain (1); Domain (5); Modified residue (1) FUNCTION: Acts as an important adapter that promotes epithelial cell polarity and tight junction formation via its interaction with DLG1. Involved in the assembly of protein complexes at sites of cell-cell contact (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell junction, tight junction {ECO:0000250}. Cell junction, adherens junction {ECO:0000250}. SUBUNIT: Heterodimer; able to heterodimerize via its C-terminal L27 domain with LIN7A, LIN7B and LIN7C. Forms a tripartite complex composed of DLG1, MPP7 and LIN7 (LIN7A or LIN7C). Interacts with DLG1 via its N-terminal L27 domain. Interacts with MPP5 and PATJ (By similarity). {ECO:0000250}. +G5E8K6 MOT6_MOUSE Monocarboxylate transporter 6 (MCT 6) (Monocarboxylate transporter 5) (MCT 5) (Solute carrier family 16 member 5) 468 51,018 Chain (1); Erroneous gene model prediction (3); Topological domain (13); Transmembrane (12) TRANSMEM 14 34 Helical. {ECO:0000255}.; TRANSMEM 54 74 Helical. {ECO:0000255}.; TRANSMEM 81 101 Helical. {ECO:0000255}.; TRANSMEM 103 122 Helical. {ECO:0000255}.; TRANSMEM 139 159 Helical. {ECO:0000255}.; TRANSMEM 172 192 Helical. {ECO:0000255}.; TRANSMEM 240 260 Helical. {ECO:0000255}.; TRANSMEM 275 295 Helical. {ECO:0000255}.; TRANSMEM 307 327 Helical. {ECO:0000255}.; TRANSMEM 331 351 Helical. {ECO:0000255}.; TRANSMEM 369 389 Helical. {ECO:0000255}.; TRANSMEM 397 417 Helical. {ECO:0000255}. TOPO_DOM 1 13 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 35 53 Extracellular. {ECO:0000255}.; TOPO_DOM 75 80 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 102 102 Extracellular. {ECO:0000255}.; TOPO_DOM 123 138 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 160 171 Extracellular. {ECO:0000255}.; TOPO_DOM 193 239 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 261 274 Extracellular. {ECO:0000255}.; TOPO_DOM 296 306 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 328 330 Extracellular. {ECO:0000255}.; TOPO_DOM 352 368 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 390 396 Extracellular. {ECO:0000255}.; TOPO_DOM 418 468 Cytoplasmic. {ECO:0000255}. FUNCTION: Proton-linked monocarboxylate transporter. Catalyzes the rapid transport across the plasma membrane of many monocarboxylates such as lactate, pyruvate, branched-chain oxo acids derived from leucine, valine and isoleucine, and the ketone bodies acetoacetate, beta-hydroxybutyrate and acetate (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q9DC61 MPPA_MOUSE Mitochondrial-processing peptidase subunit alpha (Alpha-MPP) (P-55) 524 58,279 Chain (1); Modified residue (2); Transit peptide (1) FUNCTION: Substrate recognition and binding subunit of the essential mitochondrial processing protease (MPP), which is required for maturation of the majority of mitochondrial precursor proteins (By similarity). Most MPP cleavage sites follow an arginine at position -2 (By similarity). {ECO:0000250|UniProtKB:P20069, ECO:0000250|UniProtKB:Q10713}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:P20069}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q10713}. SUBUNIT: Heterodimer of PMPCA (alpha) and PMPCB (beta) subunits, forming the mitochondrial processing protease (MPP) in which PMPCA is involved in substrate recognition and binding and PMPCB is the catalytic subunit. {ECO:0000250}. +Q9D011 MPLKI_MOUSE M-phase-specific PLK1-interacting protein (TTD non-photosensitive 1 protein homolog) 178 19,060 Chain (1); Modified residue (17) FUNCTION: May play a role in maintenance of cell cycle integrity by regulating mitosis or cytokinesis. {ECO:0000250}. PTM: Phosphorylated during mitosis in the cell cycle probably by CDK1. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Note=The subcellular location is regulated during cell cycle. During interphase located in the nucleus. During mitosis located at the centrosome and dispersed in the cytoplasm. During telophase located in the midbody. Colocalizes with PLK1 at the centrosome in M phase. SUBUNIT: Interacts with PLK1; phosphorylation-dependent. {ECO:0000250}. +Q3TV65 MPND_MOUSE MPN domain-containing protein (EC 3.4.-.-) 487 53,376 Chain (1); Compositional bias (3); Domain (1); Erroneous initiation (1); Frameshift (1); Initiator methionine (1); Metal binding (3); Modified residue (4); Motif (1); Sequence conflict (1) FUNCTION: Probable protease. {ECO:0000250}. DOMAIN: The JAMM motif may mediate the protease activity. {ECO:0000250}. +Q8R1M8 MPTX_MOUSE Mucosal pentraxin 219 24,538 Chain (1); Disulfide bond (1); Domain (1); Glycosylation (1); Metal binding (8); Sequence conflict (11); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Homopentamer. Pentraxin (or pentaxin) have a discoid arrangement of 5 non-covalently bound subunits (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in colon. {ECO:0000269|PubMed:18850182}. +Q9CZJ0 MPPD2_MOUSE Metallophosphoesterase MPPED2 (EC 3.1.-.-) (Metallophosphoesterase domain-containing protein 2) 294 33,374 Chain (1) FUNCTION: Displays low metallophosphoesterase activity (in vitro). May play a role in the development of the nervous system (By similarity). {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +D3Z1Q2 MRAP2_MOUSE Melanocortin-2 receptor accessory protein 2 207 23,678 Chain (1); Glycosylation (1); Modified residue (1); Transmembrane (1) TRANSMEM 47 67 Helical. {ECO:0000255}. FUNCTION: Modulator of melanocortin receptor 4 (MC4R), a receptor involved in energy homeostasis. Plays a central role in the control of energy homeostasis and body weight regulation by increasing ligand-sensitivity of MC4R and MC4R-mediated generation of cAMP. May also act as a negative regulator of MC2R: competes with MRAP for binding to MC2R and impairs the binding of corticotropin (ACTH) to MC2R. May also regulate activity of other melanocortin receptors (MC1R, MC3R and MC5R); however, additional evidences are required in vivo. {ECO:0000269|PubMed:20371771, ECO:0000269|PubMed:23869016}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=The formation of antiparallel homo- and heterodimers suggest that N- and C-terminus can both localize in the cytoplasmic and extracellular parts, depending on the context. {ECO:0000250}. SUBUNIT: Homodimer and heterodimer. Forms antiparallel homodimers and heterodimers with MRAP. Interacts with MC1R, MC2R, MC3R and MC5R (By similarity). Interacts with MC4R. {ECO:0000250, ECO:0000269|PubMed:23869016}. TISSUE SPECIFICITY: Predominantly expressed in the brain, mainly in the pons and cerebellum but also in regions involved in energy homeostasis, such as the hypothalamus and brainstem. {ECO:0000269|PubMed:23869016}. +Q8VBV9 O51E2_MOUSE Olfactory receptor 51E2 (Olfactory receptor 78) 320 35,578 Chain (1); Disulfide bond (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 28 48 Helical; Name=1. {ECO:0000255}.; TRANSMEM 54 74 Helical; Name=2. {ECO:0000255}.; TRANSMEM 99 119 Helical; Name=3. {ECO:0000255}.; TRANSMEM 142 162 Helical; Name=4. {ECO:0000255}.; TRANSMEM 201 221 Helical; Name=5. {ECO:0000255}.; TRANSMEM 240 260 Helical; Name=6. {ECO:0000255}.; TRANSMEM 270 290 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 27 Extracellular. {ECO:0000255}.; TOPO_DOM 49 53 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 75 98 Extracellular. {ECO:0000255}.; TOPO_DOM 120 141 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 163 200 Extracellular. {ECO:0000255}.; TOPO_DOM 222 239 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 261 269 Extracellular. {ECO:0000255}.; TOPO_DOM 291 320 Cytoplasmic. {ECO:0000255}. FUNCTION: Probable G protein-coupled receptor that is activated by the short chain fatty acids (SCFA) acetate and propionate. In response to SCFA, may positively regulate renin secretion and increase blood pressure (PubMed:23401498). May also be activated by steroid hormones and regulate cell proliferation. May also function as an olfactory receptor being activated by beta-ionone. {ECO:0000269|PubMed:23401498}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23401498}; Multi-pass membrane protein {ECO:0000269|PubMed:23401498}. TISSUE SPECIFICITY: In brain, expressed in medulla oblongata by cells close to the fourth ventricle, in the area postrema, the nucleus tractus solitarius. Expressed in olfactory epithelium and vomeronasal organ. Expressed in kidney by large renal vessels, renal afferent arterioles, and extrarenal vascular beds. In small resistance vessels the expression is restricted to cells of the juxtaglomerular afferent arteriole, which mediate renin secretion. Also detected in small blood vessels in a variety of tissues including heart, diaphragm, skeletal muscle, and skin. In the heart, esophagus, and stomach it is detected in axons of autonomic neurons and neurons of the enteric plexus. Also detected in colon and liver. {ECO:0000269|PubMed:11069588, ECO:0000269|PubMed:11707321, ECO:0000269|PubMed:23401498}. +P11928 OAS1A_MOUSE 2'-5'-oligoadenylate synthase 1A ((2-5')oligo(A) synthase 1A) (2-5A synthase 1A) (EC 2.7.7.84) (p42 OAS) 367 42,429 Binding site (4); Chain (1); Metal binding (3); Region (2); Sequence conflict (8) FUNCTION: Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response. In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation. Synthesizes higher oligomers of 2'-5'-oligoadenylates (2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L (RNase L) leading to its dimerization and subsequent activation. Activation of RNase L leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication. Can mediate the antiviral effect via the classical RNase L-dependent pathway or an alternative antiviral pathway independent of RNase L. {ECO:0000269|PubMed:12396720}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15899864}. Mitochondrion {ECO:0000250|UniProtKB:P00973}. Nucleus {ECO:0000250|UniProtKB:P00973}. Microsome {ECO:0000250|UniProtKB:P00973}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P00973}. Note=Associated with different subcellular fractions such as mitochondrial, nuclear, and rough/smooth microsomal fractions. {ECO:0000250|UniProtKB:P00973}. SUBUNIT: Monomer (By similarity). Homotetramer (By similarity). Interacts with OAS1D; the interaction inhibits OAS1A catalytic activity (PubMed:15899864). {ECO:0000250|UniProtKB:P00973, ECO:0000269|PubMed:15899864}. TISSUE SPECIFICITY: Expressed in oocytes and granulosa cells of ovary, in intestine, stomach, spleen and uterus (at protein level) (PubMed:15899864). Expressed at high levels in the digestive tract and lymphoid organs (PubMed:12396720). Expressed in ovary and spleen (PubMed:27663720). {ECO:0000269|PubMed:12396720, ECO:0000269|PubMed:15899864, ECO:0000269|PubMed:27663720}. +Q8VI93 OAS3_MOUSE 2'-5'-oligoadenylate synthase 3 ((2-5')oligo(A) synthase 3) (2-5A synthase 3) (EC 2.7.7.84) (2',5'-oligoadenylate synthetase-like 10) 1138 126,333 Binding site (4); Chain (1); Metal binding (3); Modified residue (1); Region (6); Sequence conflict (6); Site (2) FUNCTION: Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response. In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation. Synthesizes preferentially dimers of 2'-5'-oligoadenylates (2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L (RNase L) leading to its dimerization and subsequent activation. Activation of RNase L leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication. Can mediate the antiviral effect via the classical RNase L-dependent pathway or an alternative antiviral pathway independent of RNase L. {ECO:0000269|PubMed:12396720}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. DOMAIN: OAS domain 3 is catalytically active. OAS domain 1 has no catalytic activity but is essential for recognition of long dsRNAs. {ECO:0000250|UniProtKB:Q9Y6K5}. TISSUE SPECIFICITY: Intestine. {ECO:0000269|PubMed:12396720}. +Q8VI94 OASL1_MOUSE 2'-5'-oligoadenylate synthase-like protein 1 (2',5'-oligoadenylate synthetase-like 9) 511 59,088 Chain (1); Domain (2); Frameshift (1); Sequence conflict (19) FUNCTION: Does not have 2'-5'-OAS activity, but can bind double-stranded RNA. Displays antiviral activity via an alternative antiviral pathway independent of RNase L. {ECO:0000269|PubMed:12396720, ECO:0000269|PubMed:12799444}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Cytoplasm {ECO:0000250}. SUBUNIT: Specifically interacts with the ligand binding domain of the thyroid receptor (TR). TRIP14 does not require the presence of thyroid hormone for its interaction. Binds MBD1 (By similarity). {ECO:0000250}. +Q91WW2 MRGA4_MOUSE Mas-related G-protein coupled receptor member A4 (RF-amide G-protein coupled receptor) 313 35,682 Chain (1); Glycosylation (2); Sequence conflict (1); Topological domain (8); Transmembrane (7) TRANSMEM 26 46 Helical; Name=1. {ECO:0000255}.; TRANSMEM 55 75 Helical; Name=2. {ECO:0000255}.; TRANSMEM 94 114 Helical; Name=3. {ECO:0000255}.; TRANSMEM 138 158 Helical; Name=4. {ECO:0000255}.; TRANSMEM 183 203 Helical; Name=5. {ECO:0000255}.; TRANSMEM 220 240 Helical; Name=6. {ECO:0000255}.; TRANSMEM 256 276 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 25 Extracellular. {ECO:0000255}.; TOPO_DOM 47 54 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 76 93 Extracellular. {ECO:0000255}.; TOPO_DOM 115 137 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 159 182 Extracellular. {ECO:0000255}.; TOPO_DOM 204 219 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 241 255 Extracellular. {ECO:0000255}.; TOPO_DOM 277 313 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan receptor. May be a receptor for RFamide-family neuropeptides such as NPFF and NPAF, which are analgesic in vivo. May regulate nociceptor function and/or development, including the sensation or modulation of pain. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11551509}; Multi-pass membrane protein {ECO:0000269|PubMed:11551509}. TISSUE SPECIFICITY: Expressed in a subset of sensory neurons that includes nociceptors. Expressed in the subclass of non-peptidergic sensory neurons that are IB4(+) and VR1(-). {ECO:0000269|PubMed:11551509}. +Q91ZC5 MRGA7_MOUSE Mas-related G-protein coupled receptor member A7 305 35,034 Chain (1); Topological domain (8); Transmembrane (7) TRANSMEM 18 38 Helical; Name=1. {ECO:0000255}.; TRANSMEM 47 67 Helical; Name=2. {ECO:0000255}.; TRANSMEM 82 102 Helical; Name=3. {ECO:0000255}.; TRANSMEM 130 150 Helical; Name=4. {ECO:0000255}.; TRANSMEM 168 188 Helical; Name=5. {ECO:0000255}.; TRANSMEM 212 232 Helical; Name=6. {ECO:0000255}.; TRANSMEM 245 265 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 17 Extracellular. {ECO:0000255}.; TOPO_DOM 39 46 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 68 81 Extracellular. {ECO:0000255}.; TOPO_DOM 103 129 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 151 167 Extracellular. {ECO:0000255}.; TOPO_DOM 189 211 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 233 244 Extracellular. {ECO:0000255}.; TOPO_DOM 266 305 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan receptor. May be a receptor for RFamide-family neuropeptides such as NPFF and NPAF, which are analgesic in vivo. May regulate nociceptor function and/or development, including the sensation or modulation of pain (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed in a subset of sensory neurons that includes nociceptors. Expressed in the subclass of non-peptidergic sensory neurons that are IB4(+) and VR1(-). {ECO:0000269|PubMed:11551509}. +Q8BVU0 LRCH3_MOUSE Leucine-rich repeat and calponin homology domain-containing protein 3 778 86,341 Chain (1); Compositional bias (2); Domain (1); Erroneous initiation (1); Frameshift (1); Modified residue (5); Repeat (9); Sequence conflict (4); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q8K1C9 LRC41_MOUSE Leucine-rich repeat-containing protein 41 (Protein Muf1) 807 88,180 Chain (1); Erroneous initiation (1); Modified residue (5); Mutagenesis (2); Region (1); Repeat (7); Sequence conflict (4) Protein modification; protein ubiquitination. FUNCTION: Probable substrate recognition component of an ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000250}. SUBUNIT: Part of an E3 ubiquitin-protein ligase complex with Elongin BC (ELOB and ELOC), RBX1 and CUL5. Component of a probable ECS(LRRC41) complex which contains CUL5, RNF7/RBX2, Elongin BC and LRRC41. Interacts with CUL5, RNF7, ELOB and ELOC (By similarity). {ECO:0000250}. DOMAIN: The Elongin BC complex binding domain is also known as BC-box with the consensus [APST]-L-x(3)-C-x(3)-[AILV]. +Q3TX51 LRC28_MOUSE Leucine-rich repeat-containing protein 28 367 41,735 Chain (1); Repeat (9); Sequence conflict (2) +Q8R502 LRC8C_MOUSE Volume-regulated anion channel subunit LRRC8C (Factor for adipocyte differentiation 158) (Leucine-rich repeat-containing protein 8C) 803 92,372 Chain (1); Disulfide bond (2); Modified residue (2); Mutagenesis (1); Repeat (17); Sequence conflict (4); Topological domain (5); Transmembrane (4) TRANSMEM 23 43 Helical. {ECO:0000255}.; TRANSMEM 126 146 Helical. {ECO:0000255}.; TRANSMEM 267 287 Helical. {ECO:0000255}.; TRANSMEM 321 341 Helical. {ECO:0000255}. TOPO_DOM 1 22 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 44 125 Extracellular. {ECO:0000255}.; TOPO_DOM 147 266 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 288 320 Extracellular. {ECO:0000255}.; TOPO_DOM 342 803 Cytoplasmic. {ECO:0000255}. FUNCTION: Non-essential component of the volume-regulated anion channel (VRAC, also named VSOAC channel), an anion channel required to maintain a constant cell volume in response to extracellular or intracellular osmotic changes (PubMed:29769723). The VRAC channel conducts iodide better than chloride and can also conduct organic osmolytes like taurine. Plays a redundant role in the efflux of amino acids, such as aspartate and glutamate, in response to osmotic stress. Channel activity requires LRRC8A plus at least one other family member (LRRC8B, LRRC8C, LRRC8D or LRRC8E); channel characteristics depend on the precise subunit composition (By similarity). May play a role in adipogenesis (PubMed:15564382, PubMed:15184384, PubMed:21804215). {ECO:0000250|UniProtKB:Q8TDW0, ECO:0000269|PubMed:15184384, ECO:0000269|PubMed:15564382, ECO:0000269|PubMed:21804215, ECO:0000269|PubMed:29769723}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:29769723}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8TDW0}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8TDW0}. Note=In the absence of LRRC8A, resides primarily in a cytoplasmic compartment, probably the endoplasmic reticulum. Requires LRRC8A for expression at the cell membrane. {ECO:0000250|UniProtKB:Q8TDW0}. SUBUNIT: Heterohexamer (PubMed:29769723). Oligomerizes with other LRRC8 proteins (LRRC8A, LRRC8B, LRRC8D and/or LRRC8E) to form a heterohexamer (PubMed:24782309, PubMed:29769723). Detected in a channel complex that contains LRRC8A, LRRC8C and LRRC8E (By similarity). In vivo, the subunit composition may depend primarily on expression levels, and heterooligomeric channels containing various proportions of the different LRRC8 proteins may coexist (Probable). {ECO:0000250|UniProtKB:Q8TDW0, ECO:0000269|PubMed:24782309, ECO:0000269|PubMed:29769723, ECO:0000305}. TISSUE SPECIFICITY: Expressed at very low levels in adipose tissue. {ECO:0000269|PubMed:15184384, ECO:0000269|PubMed:15564382}. +Q8BGI7 LRC39_MOUSE Leucine-rich repeat-containing protein 39 (Myosin-interacting M-band-associated stress-responsive protein) (Myomasp) 337 39,061 Chain (1); Repeat (9) FUNCTION: Component of the sarcomeric M-band which plays a role in myocyte response to biomechanical stress. May regulate expression of other M-band proteins via an SRF-dependent pathway. Important for normal contractile function in heart. {ECO:0000250|UniProtKB:D3ZXS4}. SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, M line {ECO:0000250|UniProtKB:D3ZXS4}. SUBUNIT: Interacts with MYH7 (via C-terminus). {ECO:0000250|UniProtKB:Q96DD0}. TISSUE SPECIFICITY: Expressed in heart and skeletal muscle. {ECO:0000269|PubMed:20847312}. +Q8CBC6 LRRN3_MOUSE Leucine-rich repeat neuronal protein 3 (Neuronal leucine-rich repeat protein 3) (NLRR-3) 707 79,176 Chain (1); Disulfide bond (1); Domain (4); Glycosylation (8); Repeat (12); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 627 647 Helical. {ECO:0000255}. TOPO_DOM 23 626 Extracellular. {ECO:0000255}.; TOPO_DOM 648 707 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in the brain, in Stronger expression in the ventricular zone and anlage of thalamus, spinal cord, and dorsal root ganglion in E11-17 cerebellum and cerebral cortex in adults. {ECO:0000269|PubMed:9011764}. +P59383 LRRN4_MOUSE Leucine-rich repeat neuronal protein 4 (Neuronal leucine-rich repeat protein 4) (NLRR-4) 733 80,489 Chain (1); Domain (2); Glycosylation (8); Repeat (10); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 677 697 Helical. {ECO:0000255}. TOPO_DOM 20 676 Extracellular. {ECO:0000255}.; TOPO_DOM 698 733 Cytoplasmic. {ECO:0000255}. FUNCTION: May play an important role in hippocampus-dependent long-lasting memory. {ECO:0000269|PubMed:15870286}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q3UZ39 LRRF1_MOUSE Leucine-rich repeat flightless-interacting protein 1 (LRR FLII-interacting protein 1) (FLI-LRR-associated protein 1) (Flap-1) (H186 FLAP) 729 79,249 Alternative sequence (7); Chain (1); Coiled coil (1); Compositional bias (1); Cross-link (1); Initiator methionine (1); Modified residue (15); Region (1); Sequence conflict (1) FUNCTION: Transcriptional repressor which preferentially binds to the GC-rich consensus sequence (5'-AGCCCCCGGCG-3') and may regulate expression of TNF, EGFR and PDGFA. May control smooth muscle cells proliferation following artery injury through PDGFA repression. May also bind double-stranded RNA (By similarity). Positively regulates Toll-like receptor (TLR) signaling in response to agonist probably by competing with the negative FLII regulator for MYD88-binding (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm {ECO:0000250}. SUBUNIT: Homodimer. May also form higher oligomers. Interacts with FLII. Interacts with MYD88 (By similarity). Competes with FLII for MyD88-binding, even in the absence of LPS (By similarity). {ECO:0000250}. DOMAIN: The DNA-binding domain is intrinsically unstructured. {ECO:0000250}.; DOMAIN: The coiled coil mediates dimerization. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:9525888}. +Q8BZ81 LRRT3_MOUSE Leucine-rich repeat transmembrane neuronal protein 3 582 66,088 Alternative sequence (2); Chain (1); Domain (2); Glycosylation (2); Repeat (10); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 421 441 Helical. {ECO:0000255}. TOPO_DOM 31 420 Extracellular. {ECO:0000255}.; TOPO_DOM 442 582 Cytoplasmic. {ECO:0000255}. FUNCTION: May play a role in the development and maintenance of the vertebrate nervous system. Exhibits a limited synaptogenic activity in vitro, restricted to excitatory presynaptic differentiation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Expressed in neuronal tissues. {ECO:0000269|PubMed:12676565}. +Q6A009 LTN1_MOUSE E3 ubiquitin-protein ligase listerin (EC 2.3.2.27) (RING finger protein 160) (RING-type E3 ubiquitin transferase listerin) (Zinc finger protein 294) (Zfp-294) 1767 198,921 Chain (1); Erroneous initiation (2); Repeat (14); Sequence conflict (2); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase (PubMed:19196968). Component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation (By similarity). Ubiquitination leads to Vcp/p97 recruitment for extraction and degradation of the incomplete translation product (By similarity). {ECO:0000250|UniProtKB:O94822, ECO:0000250|UniProtKB:Q04781, ECO:0000269|PubMed:19196968}. PTM: Autoubiquitinated. {ECO:0000269|PubMed:19196968}. SUBUNIT: Component of the ribosome quality control complex (RQC), composed of at least the E3 ubiquitin ligase Ltn1 and Nemf. The complex probably also contains Tcf25 as well as Vcp/p97 and its ubiquitin-binding cofactors. RQC forms a stable complex with 60S ribosomal subunits. {ECO:0000250|UniProtKB:O94822, ECO:0000250|UniProtKB:Q04781}. TISSUE SPECIFICITY: Widely expressed, including in the brain and spinal cord. {ECO:0000269|PubMed:19196968}. +Q9DA11 LYZL6_MOUSE Lysozyme-like protein 6 (EC 3.2.1.17) 148 16,818 Active site (2); Chain (1); Disulfide bond (4); Glycosylation (1); Signal peptide (1) FUNCTION: May be involved sperm-egg plasma membrane adhesion and fusion during fertilization. Exhibits bacteriolytic activity in vitro against Micrococcus luteus and Staphylococcus aureus. Shows weak bacteriolytic activity against Gram-positive bacteria at physiological pH. Bacteriolytic activity is pH-dependent, with a maximum at around pH 5.6 (By similarity). {ECO:0000250|UniProtKB:O75951}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O75951}. Cell surface {ECO:0000250|UniProtKB:O75951}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:24013621}. Note=Detected in the postacrosomal area and midpiece of mature spermatozoa (PubMed:24013621). {ECO:0000269|PubMed:24013621}. SUBUNIT: Monomer. {ECO:0000305}. TISSUE SPECIFICITY: Expressed strongly in testis and epididymis and weakly in seminal vesicle, vas deferens, kidney and spleen (PubMed:24013621). Highly expressed in primary spermatocytes and round spermatids (at protein level) (PubMed:24013621). {ECO:0000269|PubMed:24013621}. +Q9DCJ5 NDUA8_MOUSE NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8 (Complex I-19kD) (CI-19kD) (Complex I-PGIV) (CI-PGIV) (NADH-ubiquinone oxidoreductase 19 kDa subunit) 172 19,992 Beta strand (1); Chain (1); Disulfide bond (4); Domain (2); Helix (8); Initiator methionine (1); Motif (4); Turn (3) FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. {ECO:0000250|UniProtKB:P51970}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P51970}; Peripheral membrane protein {ECO:0000250|UniProtKB:P51970}. Mitochondrion intermembrane space {ECO:0000250|UniProtKB:P51970}. Mitochondrion {ECO:0000250|UniProtKB:P51970}. SUBUNIT: Complex I is composed of 45 different subunits. {ECO:0000250|UniProtKB:P51970}. DOMAIN: Contains four C-X9-C motifs that are predicted to form a helix-coil-helix structure, permitting the formation of intramolecular disulfide bonds. {ECO:0000250|UniProtKB:P51970}. +P45700 MA1A1_MOUSE Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA (EC 3.2.1.113) (Man(9)-alpha-mannosidase) (Man9-mannosidase) (Mannosidase alpha class 1A member 1) (Processing alpha-1,2-mannosidase IA) (Alpha-1,2-mannosidase IA) 655 73,276 Active site (1); Beta strand (18); Chain (1); Disulfide bond (1); Glycosylation (1); Helix (22); Metal binding (1); Topological domain (2); Transmembrane (1); Turn (7) TRANSMEM 44 64 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 43 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 65 655 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Involved in the maturation of Asn-linked oligosaccharides. Progressively trim alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce Man(5)GlcNAc(2). PTM: N-linked glycan at Asn-515 consists of Man(6)-GlcNAc(2). {ECO:0000269|PubMed:15102839}. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein. +P39098 MA1A2_MOUSE Mannosyl-oligosaccharide 1,2-alpha-mannosidase IB (EC 3.2.1.113) (Mannosidase alpha class 1A member 2) (Processing alpha-1,2-mannosidase IB) (Alpha-1,2-mannosidase IB) 641 72,871 Active site (1); Alternative sequence (1); Chain (1); Disulfide bond (1); Glycosylation (1); Initiator methionine (1); Metal binding (1); Modified residue (1); Sequence conflict (3); Topological domain (2); Transmembrane (1) TRANSMEM 37 57 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 2 36 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 58 641 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Involved in the maturation of Asn-linked oligosaccharides. Progressively trim alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce Man(5)GlcNAc(2). SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein. +Q99LC3 NDUAA_MOUSE NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial (Complex I-42kD) (CI-42kD) (NADH-ubiquinone oxidoreductase 42 kDa subunit) 355 40,603 Beta strand (5); Chain (1); Erroneous initiation (1); Helix (17); Modified residue (4); Mutagenesis (2); Sequence conflict (3); Transit peptide (1); Turn (10) FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. {ECO:0000269|PubMed:24652937}. PTM: Phosphorylation at Ser-250 by PINK1 is required for the binding and/or reduction of the complex I substrate ubiquinone. {ECO:0000269|PubMed:24652937}.; PTM: Acetylation of Lys-242 is observed in liver mitochondria from fasted mice but not from fed mice. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:O95299}. SUBUNIT: Complex I is composed of 45 different subunits. This a component of the hydrophobic protein fraction. {ECO:0000250|UniProtKB:O95299}. +A2AIL4 NDUF6_MOUSE NADH dehydrogenase (ubiquinone) complex I, assembly factor 6 333 38,362 Chain (1); Transit peptide (1) FUNCTION: Involved in the assembly of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I) at early stages. May play a role in the biogenesis of MT-ND1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:18614015}. Note=Peripherally localized on the matrix face of the mitochondrial inner membrane. {ECO:0000250}. +Q8R2U7 LRC42_MOUSE Leucine-rich repeat-containing protein 42 421 47,949 Chain (1); Erroneous initiation (1); Modified residue (1); Repeat (5) +Q52KR2 LRIG2_MOUSE Leucine-rich repeats and immunoglobulin-like domains protein 2 (LIG-2) 1054 117,863 Alternative sequence (2); Chain (1); Disulfide bond (3); Domain (5); Erroneous initiation (1); Glycosylation (13); Modified residue (1); Repeat (15); Signal peptide (1); Transmembrane (1) TRANSMEM 807 827 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. +Q7TQH7 LRP10_MOUSE Low-density lipoprotein receptor-related protein 10 (LRP-10) 713 76,461 Chain (1); Compositional bias (1); Disulfide bond (15); Domain (6); Erroneous initiation (1); Glycosylation (4); Modified residue (1); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 442 462 Helical. {ECO:0000255}. TOPO_DOM 18 441 Extracellular. {ECO:0000255}.; TOPO_DOM 463 713 Cytoplasmic. {ECO:0000255}. FUNCTION: Probable receptor, which is involved in the internalization of lipophilic molecules and/or signal transduction. May be involved in the uptake of lipoprotein APOE in liver. {ECO:0000269|PubMed:11123907}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Membrane, coated pit {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in heart, lung, liver and liver. Expressed at low level in brain and spleen. Weakly or not expressed in testis and skeletal muscle. In liver, it is expressed in hepatocytes and at higher level in sinusoidal lining. In the kidney, it is expressed in peritubular capillaries. In brain, it is expressed in the epithelium of the choroid plexus ependymal cells of the third ventricle pia matter, and to lesser extent in hippocampal fields CA2 and CA3. {ECO:0000269|PubMed:11123907}. +O09108 LSHB_MOUSE Lutropin subunit beta (Lutropin beta chain) (Luteinizing hormone subunit beta) (LH-B) (LSH-B) (LSH-beta) 141 15,028 Chain (1); Disulfide bond (5); Glycosylation (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Promotes spermatogenesis and ovulation by stimulating the testes and ovaries to synthesize steroids. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Heterodimer of a common alpha chain and a unique beta chain which confers biological specificity to thyrotropin, lutropin, follitropin and gonadotropin. +P59034 LRRC3_MOUSE Leucine-rich repeat-containing protein 3 257 28,119 Chain (1); Domain (2); Repeat (3); Signal peptide (1); Transmembrane (1) TRANSMEM 205 225 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q61809 LRRN1_MOUSE Leucine-rich repeat neuronal protein 1 (Neuronal leucine-rich repeat protein 1) (NLRR-1) 716 80,548 Chain (1); Disulfide bond (1); Domain (4); Erroneous initiation (1); Glycosylation (5); Repeat (9); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 632 652 Helical. {ECO:0000255}. TOPO_DOM 26 631 Extracellular. {ECO:0000255}.; TOPO_DOM 653 716 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in brain. {ECO:0000269|PubMed:8717337}. +Q80TE7 LRRC7_MOUSE Leucine-rich repeat-containing protein 7 (Densin-180) (Densin) (Protein LAP1) 1490 166,901 Chain (1); Domain (1); Erroneous initiation (1); Modified residue (14); Repeat (17) FUNCTION: Required for normal synaptic spine architecture and function. Necessary for DISC1 and GRM5 localization to postsynaptic density complexes and for both N-methyl D-aspartate receptor-dependent and metabotropic glutamate receptor-dependent long term depression. {ECO:0000269|PubMed:22072671}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000269|PubMed:22072671}. SUBUNIT: Interacts with CNKSR2 and DLG4 (By similarity). Interacts with CTNND2/Catenin delta-2. Forms a complex with N-cadherin through CTNND2. Interacts with CAMK2A (By similarity). {ECO:0000250|UniProtKB:P70587, ECO:0000250|UniProtKB:Q96NW7}. TISSUE SPECIFICITY: Expressed in brain (at protein level). {ECO:0000269|PubMed:22072671}. +Q8K377 LRRT1_MOUSE Leucine-rich repeat transmembrane neuronal protein 1 522 58,718 Chain (1); Domain (2); Glycosylation (4); Repeat (10); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 428 448 Helical. {ECO:0000255}. TOPO_DOM 35 427 Extracellular. {ECO:0000255}.; TOPO_DOM 449 522 Cytoplasmic. {ECO:0000255}. FUNCTION: Exhibits strong synaptogenic activity, restricted to excitatory presynaptic differentiation, acting at both pre- and postsynaptic level. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Accumulates extensively in the endoplasmic reticulum of transfected nonneuronal cells. {ECO:0000269|PubMed:17667961, ECO:0000269|Ref.5}. TISSUE SPECIFICITY: Expressed predominantly in the nervous system by postmitotic neurons, but also in some non-neuronal tissues. In adult brain expression is most prominent in the forebraain, particularly in the thalamus and in the cortical areas including hippocampus, piriform and posterior cingulate. {ECO:0000269|PubMed:12676565, ECO:0000269|PubMed:17667961}. +P30730 LSHR_MOUSE Lutropin-choriogonadotropic hormone receptor (LH/CG-R) (Luteinizing hormone receptor) (LSH-R) 700 78,215 Chain (1); Disulfide bond (1); Glycosylation (6); Lipidation (2); Modified residue (1); Repeat (4); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 363 390 Helical; Name=1. {ECO:0000255}.; TRANSMEM 400 422 Helical; Name=2. {ECO:0000255}.; TRANSMEM 444 466 Helical; Name=3. {ECO:0000255}.; TRANSMEM 487 509 Helical; Name=4. {ECO:0000255}.; TRANSMEM 530 551 Helical; Name=5. {ECO:0000255}.; TRANSMEM 575 598 Helical; Name=6. {ECO:0000255}.; TRANSMEM 610 631 Helical; Name=7. {ECO:0000255}. TOPO_DOM 27 362 Extracellular. {ECO:0000255}.; TOPO_DOM 391 399 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 423 443 Extracellular. {ECO:0000255}.; TOPO_DOM 467 486 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 510 529 Extracellular. {ECO:0000255}.; TOPO_DOM 552 574 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 599 609 Extracellular. {ECO:0000255}.; TOPO_DOM 632 700 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for lutropin-choriogonadotropic hormone. The activity of this receptor is mediated by G proteins which activate adenylate cyclase. {ECO:0000250|UniProtKB:P22888}. PTM: Sulfated. {ECO:0000250|UniProtKB:P22888}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P22888}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P22888}. +Q8QZX5 LSM10_MOUSE U7 snRNA-associated Sm-like protein LSm10 122 13,881 Chain (1) FUNCTION: Appears to function in the U7 snRNP complex that is involved in histone 3'-end processing (By similarity). Increases U7 snRNA levels but not histone 3'-end pre-mRNA processing activity, when overexpressed (By similarity). Required for cell cycle progression from G1 to S phases (By similarity). Binds specifically to U7 snRNA (By similarity). Binds specifically to U7 snRNA (By similarity). Binds to the downstream cleavage product (DCP) of histone pre-mRNA. {ECO:0000250}. PTM: Not methylated. Methylation is not necessary for interaction with SMN (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the heptameric ring U7 snRNP complex, or U7 Sm protein core complex, at least composed of LSM10, LSM11, SNRPB, SNRPD3, SNRPE, SNRPF, SNRPG and U7 snRNA. Formation of the U7 snRNP is an ATP-dependent process mediated by a specialized SMN complex containing at least the Sm protein core complex and additionally, the U7-specific LSM10 and LSM11 proteins. Interacts with CLNS1A and SMN (By similarity). {ECO:0000250}. +Q8BUV6 LSM11_MOUSE U7 snRNA-associated Sm-like protein LSm11 361 39,907 Chain (1); Cross-link (1); Modified residue (5); Mutagenesis (4); Region (2) FUNCTION: Component of the U7 snRNP complex that is involved in the histone 3'-end pre-mRNA processing. Increases U7 snRNA levels but not histone 3'-end pre-mRNA processing activity, when overexpressed. Required for cell cycle progression from G1 to S phases. Binds specifically to the Sm-binding site of U7 snRNA. {ECO:0000269|PubMed:12975319, ECO:0000269|PubMed:15824063, ECO:0000269|PubMed:16914750}. PTM: Not methylated. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Identified in a histone pre-mRNA complex, at least composed of ERI1, LSM11, SLBP, SNRPB, SYNCRIP and YBX1. Interacts (via the Sm domains) with CLNS1A. Interacts with PRMT5, SMN, ZNF473 and WDR77. Component of the heptameric ring U7 snRNP complex, or U7 Sm protein core complex, at least composed of LSM10, LSM11, SNRPB, SNRPD3, SNRPE, SNRPF, SNRPG and U7 snRNA (By similarity). Formation of the U7 snRNP is an ATP-dependent process mediated by a specialized SMN complex containing at least the Sm protein core complex and additionally, the U7-specific LSM10 and LSM11 proteins (By similarity). Interacts with LSM10 and SNRPB (By similarity). {ECO:0000250}. DOMAIN: The C-terminal SM 1 domain is both necessary for the binding to the Sm-binding site of U7 snRNA and U7 snRNP assembly. The N-terminal domain is essential for histone pre-mRNA cleavage (By similarity). Amino acids 63-82 are sufficient to interact with ZNF473 (By similarity). {ECO:0000250}. +Q9D0R8 LSM12_MOUSE Protein LSM12 homolog 195 21,701 Chain (1); Erroneous gene model prediction (2); Initiator methionine (1); Modified residue (2) +Q8BXQ3 LRTM1_MOUSE Leucine-rich repeat and transmembrane domain-containing protein 1 356 38,542 Chain (1); Domain (2); Glycosylation (3); Repeat (5); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 300 320 Helical. {ECO:0000255}. TOPO_DOM 33 299 Extracellular. {ECO:0000255}.; TOPO_DOM 321 356 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q8BGX3 LRTM2_MOUSE Leucine-rich repeat and transmembrane domain-containing protein 2 370 41,038 Chain (1); Domain (2); Glycosylation (4); Repeat (5); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 307 327 Helical. {ECO:0000255}. TOPO_DOM 36 306 Extracellular. {ECO:0000255}.; TOPO_DOM 328 370 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +P62311 LSM3_MOUSE U6 snRNA-associated Sm-like protein LSm3 102 11,845 Chain (1); Initiator methionine (1); Modified residue (1) FUNCTION: Plays role in pre-mRNA splicing as component of the U4/U6-U5 tri-snRNP complex that is involved in spliceosome assembly, and as component of the precatalytic spliceosome (spliceosome B complex). The heptameric LSM2-8 complex binds specifically to the 3'-terminal U-tract of U6 snRNA. {ECO:0000250|UniProtKB:P62310}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P62310}. SUBUNIT: Component of the precatalytic spliceosome (spliceosome B complex). Component of the U4/U6-U5 tri-snRNP complex, a building block of the precatalytic spliceosome (spliceosome B complex). The U4/U6-U5 tri-snRNP complex is composed of the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39, plus LSM2, LSM3, LSM4, LSM5, LSM6, LSM7 and LSM8. LSM2, LSM3, LSM4, LSM5, LSM6, LSM7 and LSM8 form a heptameric, ring-shaped subcomplex (the LSM2-8 complex) that is part of the U4/U6-U5 tri-snRNP complex and the precatalytic spliceosome. {ECO:0000250|UniProtKB:P62310}. +P62322 LSM5_MOUSE U6 snRNA-associated Sm-like protein LSm5 91 9,937 Chain (1); Initiator methionine (1); Modified residue (1) FUNCTION: Plays role in pre-mRNA splicing as component of the U4/U6-U5 tri-snRNP complex that is involved in spliceosome assembly, and as component of the precatalytic spliceosome (spliceosome B complex). The heptameric LSM2-8 complex binds specifically to the 3'-terminal U-tract of U6 snRNA. {ECO:0000250|UniProtKB:Q9Y4Y9}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y4Y9}. SUBUNIT: Component of the precatalytic spliceosome (spliceosome B complex). Component of the U4/U6-U5 tri-snRNP complex, a building block of the precatalytic spliceosome (spliceosome B complex). The U4/U6-U5 tri-snRNP complex is composed of the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39, plus LSM2, LSM3, LSM4, LSM5, LSM6, LSM7 and LSM8. LSM2, LSM3, LSM4, LSM5, LSM6, LSM7 and LSM8 form a heptameric, ring-shaped subcomplex (the LSM2-8 complex) that is part of the U4/U6-U5 tri-snRNP complex and the precatalytic spliceosome. {ECO:0000250|UniProtKB:Q9Y4Y9}. +Q9JJL9 LT4R2_MOUSE Leukotriene B4 receptor 2 (LTB4-R 2) (LTB4-R2) (Leukotriene B4 receptor BLT2) 360 37,867 Chain (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 25 45 Helical; Name=1. {ECO:0000255}.; TRANSMEM 61 81 Helical; Name=2. {ECO:0000255}.; TRANSMEM 97 117 Helical; Name=3. {ECO:0000255}.; TRANSMEM 141 161 Helical; Name=4. {ECO:0000255}.; TRANSMEM 186 206 Helical; Name=5. {ECO:0000255}.; TRANSMEM 225 245 Helical; Name=6. {ECO:0000255}.; TRANSMEM 276 296 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 24 Extracellular. {ECO:0000255}.; TOPO_DOM 46 60 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 82 96 Extracellular. {ECO:0000255}.; TOPO_DOM 118 140 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 162 185 Extracellular. {ECO:0000255}.; TOPO_DOM 207 224 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 246 275 Extracellular. {ECO:0000255}.; TOPO_DOM 297 360 Cytoplasmic. {ECO:0000255}. FUNCTION: Low-affinity receptor for leukotrienes including leukotriene B4. Mediates chemotaxis of granulocytes and macrophages. The response is mediated via G-proteins that activate a phosphatidylinositol-calcium second messenger system (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q9JHS3 LTOR2_MOUSE Ragulator complex protein LAMTOR2 (Endosomal adaptor protein p14) (Late endosomal/lysosomal Mp1-interacting protein) (Late endosomal/lysosomal adaptor and MAPK and MTOR activator 2) (Mitogen-activated protein-binding protein-interacting protein) (Roadblock domain-containing protein 3) 125 13,480 Beta strand (7); Chain (1); Helix (4); Region (1); Turn (2) FUNCTION: As part of the Ragulator complex it is involved in amino acid sensing and activation of mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids. Activated by amino acids through a mechanism involving the lysosomal V-ATPase, the Ragulator functions as a guanine nucleotide exchange factor activating the small GTPases Rag. Activated Ragulator and Rag GTPases function as a scaffold recruiting mTORC1 to lysosomes where it is in turn activated. Adapter protein that enhances the efficiency of the MAP kinase cascade facilitating the activation of MAPK2. {ECO:0000269|PubMed:15263099}. SUBCELLULAR LOCATION: Late endosome membrane; Peripheral membrane protein; Cytoplasmic side. Lysosome membrane; Peripheral membrane protein; Cytoplasmic side. SUBUNIT: Part of the Ragulator complex composed of LAMTOR1, LAMTOR2, LAMTOR3, LAMTOR4 and LAMTOR5. LAMTOR4 and LAMTOR5 form a heterodimer that interacts, through LAMTOR1, with a LAMTOR2, LAMTOR3 heterodimer. The Ragulator complex interacts with both the mTORC1 complex and heterodimers constituted of the Rag GTPases RRAGA, RRAGB, RRAGC and RRAGD; regulated by amino acid availability (PubMed:15016825, PubMed:15263099, PubMed:15740743, PubMed:19177150). The Ragulator complex interacts with SLC38A9; the probable amino acid sensor (By similarity). Interacts with LAMTOR1 and LAMTOR3; the interaction is direct. Interacts with MAPK1 and MAP2K1 (PubMed:11266467). {ECO:0000250|UniProtKB:Q9Y2Q5, ECO:0000269|PubMed:11266467, ECO:0000269|PubMed:15016825, ECO:0000269|PubMed:15263099, ECO:0000269|PubMed:15740743, ECO:0000269|PubMed:19177150}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11266467}. +Q9CPX3 LYZL1_MOUSE Lysozyme-like protein 1 (EC 3.2.1.17) 148 16,802 Active site (2); Chain (1); Disulfide bond (4); Glycosylation (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. SUBUNIT: Monomer. {ECO:0000305}. +P17981 NAR2A_MOUSE T-cell ecto-ADP-ribosyltransferase 1 (EC 2.4.2.31) (ADP-ribosyltransferase 2a pseudogene) (ADP-ribosyltransferase C2 and C3 toxin-like 2) (ARTC2) (Mono(ADP-ribosyl)transferase 2A) (NAD(+) glycohydrolase) (EC 3.2.2.5) (T-cell NAD(P)(+)--arginine ADP-ribosyltransferase 1) (T-cell differentiation marker Rt6 homolog 1) (T-cell mono(ADP-ribosyl)transferase 1) 287 32,801 Active site (1); Binding site (3); Chain (1); Disulfide bond (3); Glycosylation (2); Lipidation (1); Mutagenesis (2); Natural variant (4); Propeptide (1); Sequence conflict (5); Signal peptide (1); Site (2) FUNCTION: Has both ADP-ribosyltransferase activity and thiol-dependent NAD(+) glycohydrolase activity. {ECO:0000269|PubMed:11011142, ECO:0000269|PubMed:9300695}. PTM: It is proposed that in the absence of reducing agents, a disulfide bond is formed between Cys-80 and Cys-201, leading to a conformational change that reduces the catalytic rate of NAD glycohydrolysis. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. TISSUE SPECIFICITY: Expressed in spleen, intestine and thymus. {ECO:0000269|PubMed:7547715, ECO:0000269|PubMed:9300695}. DISEASE: Note=A subset of Rt6+ regulatory T-cells may confer protection to autoimmune disease, and failure to develop this subset may result in enhanced susceptibility for autoimmune disease. +Q99MV5 M10L1_MOUSE RNA helicase Mov10l1 (EC 3.6.4.13) (Cardiac helicase activated by MEF2 protein) (Cardiac-specific RNA helicase) (Moloney leukemia virus 10-like protein 1 homolog) (MOV10-like protein 1 homolog) 1187 132,792 Alternative sequence (2); Chain (1); Erroneous initiation (1); Motif (1); Mutagenesis (2); Nucleotide binding (1); Region (1); Repeat (5); Sequence conflict (2) FUNCTION: Isoform 1: ATP-dependent RNA helicase required during spermatogenesis to repress transposable elements and prevent their mobilization, which is essential for germline integrity (PubMed:20534472, PubMed:20547853, PubMed:23166510, PubMed:25762440). Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons (PubMed:20534472, PubMed:20547853, PubMed:23166510, PubMed:25762440). Involved in the primary piRNA metabolic process (PubMed:20534472, PubMed:20547853, PubMed:23166510, PubMed:25762440). Specifically binds to piRNA precursors and promotes the generation of intermediate piRNA processing fragments that are subsequently loaded to Piwi proteins (PubMed:25762440). Acts via its ATP-dependent RNA helicase activity: displays 5'-3' RNA unwinding activity and probably mediates unwinding and funneling of single-stranded piRNA precursor transcripts to the endonuclease that catalyzes the first cleavage step of piRNA processing to generate piRNA intermediate fragments that are subsequently loaded to Piwi proteins (PubMed:25762440). {ECO:0000269|PubMed:20534472, ECO:0000269|PubMed:20547853, ECO:0000269|PubMed:23166510, ECO:0000269|PubMed:25762440}.; FUNCTION: Isoform 2: May act downstream of MEF2C during heart formation. Acts as a cardiac-specific suppressor of cardiomyocyte hypertrophy and cell cycle progression, suggesting that it may suppress these processes through the regulation of CDKN1A. Such results however require additional evidence. {ECO:0000305|PubMed:11854500}. SUBCELLULAR LOCATION: Isoform 1: Cytoplasm {ECO:0000269|PubMed:20534472, ECO:0000269|PubMed:23166510}. Note=Component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis (PubMed:20534472, PubMed:23166510). {ECO:0000269|PubMed:23166510, ECO:0000305|PubMed:20534472}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm {ECO:0000269|PubMed:11854500}. SUBUNIT: Interacts with PIWIL1 (PubMed:20534472). Interacts with PIWIL2 (PubMed:20534472, PubMed:20547853). Interacts with PIWIL4 (PubMed:20534472, PubMed:20547853). Interacts with HSPA2 (PubMed:20547853). Interacts with PLD6 (PubMed:25762440). {ECO:0000269|PubMed:20534472, ECO:0000269|PubMed:20547853, ECO:0000269|PubMed:25762440}. TISSUE SPECIFICITY: Isoform 1: Specifically expressed in testis (PubMed:12754203). Isoform 1: In testis, present in pachytene spermatocytes but absent in postmeiotic spermatids (at protein level) (PubMed:20534472, PubMed:20547853). Isoform 2: Present in cardiomyocytes (at protein level) (PubMed:11279525). Isoform 2: Heart specific (PubMed:11854500). Isoform 3: Heart specific and is specifically expressed in cardiac myocytes (PubMed:12754203). {ECO:0000269|PubMed:11279525, ECO:0000269|PubMed:11854500, ECO:0000269|PubMed:12754203, ECO:0000269|PubMed:20547853}. +Q3UPL6 M4A15_MOUSE Membrane-spanning 4-domains subfamily A member 15 245 25,941 Chain (1); Transmembrane (4) TRANSMEM 78 98 Helical. {ECO:0000255}.; TRANSMEM 103 123 Helical. {ECO:0000255}.; TRANSMEM 147 167 Helical. {ECO:0000255}.; TRANSMEM 176 196 Helical. {ECO:0000255}. FUNCTION: May be involved in signal transduction as a component of a multimeric receptor complex. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q99N07 M4A6D_MOUSE Membrane-spanning 4-domains subfamily A member 6D (CD20 antigen-like 8) 247 26,383 Chain (1); Frameshift (1); Modified residue (1); Sequence conflict (12); Topological domain (5); Transmembrane (4) TRANSMEM 47 67 Helical. {ECO:0000255}.; TRANSMEM 81 101 Helical. {ECO:0000255}.; TRANSMEM 122 142 Helical. {ECO:0000255}.; TRANSMEM 181 201 Helical. {ECO:0000255}. TOPO_DOM 1 46 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 68 80 Extracellular. {ECO:0000255}.; TOPO_DOM 102 121 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 143 180 Extracellular. {ECO:0000255}.; TOPO_DOM 202 247 Cytoplasmic. {ECO:0000255}. FUNCTION: May be involved in signal transduction as a component of a multimeric receptor complex. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed in thymus, spleen, intestine, colon, testis, heart, liver, brain, kidney, peripheral lymph node and bone marrow. +P53349 M3K1_MOUSE Mitogen-activated protein kinase kinase kinase 1 (EC 2.7.11.25) (MAPK/ERK kinase kinase 1) (MEK kinase 1) (MEKK 1) 1493 161,289 Active site (1); Binding site (1); Chain (1); Compositional bias (4); Domain (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (15); Mutagenesis (13); Nucleotide binding (1); Sequence conflict (8); Zinc finger (2) FUNCTION: Component of a protein kinase signal transduction cascade (PubMed:14500727). Activates the ERK and JNK kinase pathways by phosphorylation of MAP2K1 and MAP2K4 (PubMed:14500727). May phosphorylate the MAPK8/JNK1 kinase (PubMed:17761173). Activates CHUK and IKBKB, the central protein kinases of the NF-kappa-B pathway (PubMed:14500727). {ECO:0000269|PubMed:14500727, ECO:0000269|PubMed:17761173}. PTM: Autophosphorylated. {ECO:0000269|PubMed:9078260}. SUBUNIT: Binds both upstream activators and downstream substrates in multimolecular complexes through its N-terminus. Oligomerizes after binding MAP4K2 or TRAF2. Interacts with AXIN1. Interacts (via the kinase catalytic domain) with STK38 (By similarity). Interacts with GRIPAP1 (By similarity). {ECO:0000250|UniProtKB:Q13233, ECO:0000250|UniProtKB:Q62925}. TISSUE SPECIFICITY: Highly expressed in the heart and spleen while a lower level expression is seen in the liver. +Q61827 MAFK_MOUSE Transcription factor MafK (Erythroid transcription factor NF-E2 p18 subunit) 156 17,537 Chain (1); Cross-link (1); Domain (1); Modified residue (1); Region (2); Sequence conflict (1) FUNCTION: Since they lack a putative transactivation domain, the small Mafs behave as transcriptional repressors when they dimerize among themselves. However, they seem to serve as transcriptional activators by dimerizing with other (usually larger) basic-zipper proteins, such as NFE2, NFE2L1/NRF1, NFE2L2/NRF2 and NFE2L3/NRF3, and recruiting them to specific DNA-binding sites. Small Maf proteins heterodimerize with Fos and may act as competitive repressors of the NF-E2 transcription factor. {ECO:0000250|UniProtKB:O60675}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Homodimer or heterodimer. It can form high affinity heterodimers with members of the CNC-bZIP family such as NFE2, NFE2L1/NRF1, NFE2L2/NRF2 and NFE2L3/NRF3. {ECO:0000250|UniProtKB:O60675}. TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle and placenta. Also expressed in erythroid cells. +Q91X49 MALL_MOUSE MAL-like protein (Protein BENE) 154 17,470 Chain (1); Domain (1); Transmembrane (4) TRANSMEM 24 44 Helical. {ECO:0000255}.; TRANSMEM 61 81 Helical. {ECO:0000255}.; TRANSMEM 99 119 Helical. {ECO:0000255}.; TRANSMEM 131 151 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q6T264 MAML1_MOUSE Mastermind-like protein 1 (Mam-1) 1020 107,726 Chain (1); Compositional bias (2); Erroneous initiation (3); Modified residue (7); Region (1); Sequence conflict (10) FUNCTION: Acts as a transcriptional coactivator for NOTCH proteins. Has been shown to amplify NOTCH-induced transcription of HES1. Enhances phosphorylation and proteolytic turnover of the NOTCH intracellular domain in the nucleus through interaction with CDK8. Binds to CREBBP/CBP which promotes nucleosome acetylation at NOTCH enhancers and activates transcription. Induces phosphorylation and localization of CREBBP to nuclear foci. Plays a role in hematopoietic development by regulating NOTCH-mediated lymphoid cell fate decisions. {ECO:0000269|PubMed:15019995, ECO:0000269|PubMed:15187027}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:15019995}. Note=Nuclear, in a punctate manner. SUBUNIT: Interacts (via N-terminus) with NOTCH1, NOTCH2, NOTCH3 and NOTCH4 (via ankyrin repeat region). Interacts (via N-terminus) with p53 (via DNA-binding region). Forms a DNA-binding complex with Notch proteins and RBPSUH/RBP-J kappa/CBF1. Also binds CREBBP/CBP and CDK8. Forms a complex with PRAG1, NOTCH1 and MAML1, in a MAML1-dependent manner (PubMed:25038227). {ECO:0000269|PubMed:15019995, ECO:0000269|PubMed:25038227}. DOMAIN: The C-terminal region is required for transcriptional activation. {ECO:0000269|PubMed:15019995}. TISSUE SPECIFICITY: At E9.5, strongly expressed in the telencephalon, first branchial arch, forelimb buds and somites. By E10.5, continuously expressed in brain and spinal cord. Also expressed in first and second branchial arches and limb buds. By E11.5, expression in CNS is weak but increases in mesodermal tissues. At E14.5, detected in epithelial cells in trachea, esophagus and proximal and distal tubules of the developing lungs. {ECO:0000269|PubMed:15019995}. +Q9CR33 MANS1_MOUSE MANSC domain-containing protein 1 414 44,823 Chain (1); Domain (1); Glycosylation (3); Sequence conflict (8); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 370 392 Helical. {ECO:0000255}. TOPO_DOM 25 369 Extracellular. {ECO:0000255}.; TOPO_DOM 393 414 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q3UMQ8 NAF1_MOUSE H/ACA ribonucleoprotein complex non-core subunit NAF1 489 53,246 Chain (1); Compositional bias (3); Cross-link (1); Erroneous initiation (1); Modified residue (2) FUNCTION: RNA-binding protein required for the maturation of box H/ACA snoRNPs complex and ribosome biogenesis. During assembly of the H/ACA snoRNPs complex, it associates with the complex and disappears during maturation of the complex and is replaced by NOLA1/GAR1 to yield mature H/ACA snoRNPs complex. Probably competes with NOLA1/GAR1 for binding with DKC1/NOLA4 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Shuttles between the cytoplasm and the nucleus. Absent from the nucleolus (By similarity). {ECO:0000250}. SUBUNIT: During assembly of the complex, component of the small nucleolar ribonucleoprotein particles containing H/ACA-type snoRNAs (H/ACA snoRNPs) which contains NOLA2/NHP2, NOLA3/NOP10, NAF1 and DKC1/NOLA4. Interacts directly with DKC1/NOLA4 (By similarity). {ECO:0000250}. +P60322 NANO2_MOUSE Nanos homolog 2 (NOS-2) 136 15,597 Chain (1); Motif (2); Sequence conflict (1); Zinc finger (1) FUNCTION: Plays a key role in the sexual differentiation of germ cells by promoting the male fate but suppressing the female fate. Represses the female fate pathways by suppressing meiosis, which in turn results in the promotion of the male fate. Maintains the suppression of meiosis by preventing STRA8 expression, which is required for premeiotic DNA replication, after CYP26B1 is decreased. Regulates the localization of the CCR4-NOT deadenylation complex to P-bodies and plays a role in recruiting the complex to trigger the degradation of mRNAs involved in meiosis. Required for the maintenance of the spermatogonial stem cell population. Not essential for the assembly of P-bodies but is required for the maintenance of their normal state. {ECO:0000269|PubMed:12947200, ECO:0000269|PubMed:17138666, ECO:0000269|PubMed:18281459, ECO:0000269|PubMed:19745153, ECO:0000269|PubMed:20133598}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20133598}. Cytoplasm, P-body {ECO:0000269|PubMed:20133598}. Cytoplasm, perinuclear region {ECO:0000250}. Note=More abundant in perinuclear region of the cytoplasm of the germ cells of the adult testis (By similarity). Localizes at P-bodies during gonocyte development. {ECO:0000250}. SUBUNIT: Interacts with CNOT1, CNOT3, CNOT6L, CNOT7 and CNOT9. {ECO:0000269|PubMed:20133598}. DOMAIN: The Nanos-type zinc finger is composed of two C2HC motifs, each motif binding one molecule of zinc. It is essential for the translation repression activity of the protein. {ECO:0000255|PROSITE-ProRule:PRU00855}. TISSUE SPECIFICITY: Predominantly expressed in male germ cells. Expressed in self-renewing spermatogonial stem cells and developing gonads. {ECO:0000269|PubMed:12947200, ECO:0000269|PubMed:19745153}. +Q80Z64 NANOG_MOUSE Homeobox protein NANOG (ES cell-associated protein 4) (Early embryo specific expression NK-type homeobox protein) (Homeobox transcription factor Nanog) 305 34,240 Alternative sequence (1); Chain (1); Compositional bias (1); DNA binding (1); Helix (4); Mutagenesis (22); Region (5); Repeat (10); Sequence conflict (1) FUNCTION: Transcription regulator involved in inner cell mass and embryonic stem (ES) cells proliferation and self-renewal (PubMed:25825768). Imposes pluripotency on ES cells and prevents their differentiation towards extraembryonic endoderm and trophectoderm lineages. Blocks bone morphogenetic protein-induced mesoderm differentiation of ES cells by physically interacting with SMAD1 and interfering with the recruitment of coactivators to the active SMAD transcriptional complexes. Acts as a transcriptional activator or repressor. Binds optimally to the DNA consensus sequence 5'-TAAT[GT][GT]-3' or 5'-[CG][GA][CG]C[GC]ATTAN[GC]-3'. Binds to the POU5F1/OCT4 promoter (By similarity). Able to autorepress its expression in differentiating (ES) cells: binds to its own promoter following interaction with ZNF281/ZFP281, leading to recruitment of the NuRD complex and subsequent repression of expression. When overexpressed, promotes cells to enter into S phase and proliferation. {ECO:0000250|UniProtKB:Q9H9S0, ECO:0000269|PubMed:12787504, ECO:0000269|PubMed:12787505, ECO:0000269|PubMed:14728807, ECO:0000269|PubMed:15502159, ECO:0000269|PubMed:16518401, ECO:0000269|PubMed:16791199, ECO:0000269|PubMed:16801560, ECO:0000269|PubMed:21915945, ECO:0000269|PubMed:22988117, ECO:0000269|PubMed:25825768}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:15582778}. SUBUNIT: Interacts with SMAD1 and SALL4. Interacts with ZNF281/ZFP281. Interacts with PCGF1 (By similarity). Interacts with ESRRB; reciprocally modulates their transcriptional activities (PubMed:18957414). {ECO:0000250|UniProtKB:Q9H9S0, ECO:0000269|PubMed:16801560, ECO:0000269|PubMed:16840789, ECO:0000269|PubMed:18177668, ECO:0000269|PubMed:18957414, ECO:0000269|PubMed:21915945, ECO:0000269|PubMed:22988117}. TISSUE SPECIFICITY: Not expressed in oocytes and spermatogonia (at protein level). Not expressed in many somatic organs, ovary, testis, fibroblast and hematopoietic cell lines. {ECO:0000269|PubMed:12787504, ECO:0000269|PubMed:12787505, ECO:0000269|PubMed:15108323, ECO:0000269|PubMed:15939376}. +Q8BZR9 NCBP3_MOUSE Nuclear cap-binding protein subunit 3 615 70,043 Alternative sequence (4); Chain (1); Compositional bias (1); Cross-link (4); Erroneous initiation (2); Modified residue (8); Motif (1); Region (1); Sequence conflict (7) FUNCTION: Associates with NCBP1/CBP80 to form an alternative cap-binding complex (CBC) which plays a key role in mRNA export. NCBP3 serves as adapter protein linking the capped RNAs (m7GpppG-capped RNA) to NCBP1/CBP80. Unlike the conventional CBC with NCBP2 which binds both small nuclear RNA (snRNA) and messenger (mRNA) and is involved in their export from the nucleus, the alternative CBC with NCBP3 does not bind snRNA and associates only with mRNA thereby playing a role in only mRNA export. The alternative CBC is particularly important in cellular stress situations such as virus infections and the NCBP3 activity is critical to inhibit virus growth (PubMed:26382858). {ECO:0000269|PubMed:26382858}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q53F19}. Cytoplasm {ECO:0000250|UniProtKB:Q53F19}. SUBUNIT: Component of an alternative cap-binding complex (CBC) composed of NCBP1/CBP80 and NCBP3. Interacts with SRRT, KPNA3, THOC5 and EIF4A3. {ECO:0000250|UniProtKB:Q53F19}. +Q99JS0 NCMAP_MOUSE Noncompact myelin-associated protein (Myelin protein of 11 kDa) (MP11) 100 10,846 Chain (1); Compositional bias (1); Topological domain (2); Transmembrane (1) TRANSMEM 29 49 Helical. {ECO:0000255}. TOPO_DOM 1 28 Extracellular. {ECO:0000255}.; TOPO_DOM 50 100 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a role in myelin formation. {ECO:0000250}. PTM: Glycosylated. {ECO:0000269|PubMed:18650334}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18650334}; Single-pass type I membrane protein {ECO:0000269|PubMed:18650334}. Note=Localized mainly in the Schmidt-Lanterman incisures and paranodes of noncompact peripheral nerve myelin. {ECO:0000250}. TISSUE SPECIFICITY: Found in the peripheral nervous system (PNS) Schwann cells (at protein level). Expressed in the PNS, primarily limited to Schwann cells. {ECO:0000269|PubMed:18650334}. +P70232 NCHL1_MOUSE Neural cell adhesion molecule L1-like protein (Cell adhesion molecule with homology to L1CAM) (Chl1-like protein) (Close homolog of L1) [Cleaved into: Processed neural cell adhesion molecule L1-like protein] 1209 135,074 Alternative sequence (3); Chain (2); Disulfide bond (6); Domain (10); Frameshift (1); Glycosylation (10); Modified residue (3); Motif (2); Mutagenesis (2); Sequence conflict (5); Signal peptide (1); Site (2); Topological domain (2); Transmembrane (1) TRANSMEM 1084 1104 Helical. {ECO:0000255}. TOPO_DOM 26 1083 Extracellular. {ECO:0000255}.; TOPO_DOM 1105 1209 Cytoplasmic. {ECO:0000255}. FUNCTION: Extracellular matrix and cell adhesion protein that plays a role in nervous system development and in synaptic plasticity. Both soluble and membranous forms promote neurite outgrowth of cerebellar and hippocampal neurons and suppress neuronal cell death. Plays a role in neuronal positioning of pyramidal neurons as well as in regulation of both the number of interneurons and the efficacy of GABAergic synapses. May play a role in regulating cell migration in nerve regeneration and cortical development. Potentiates integrin-dependent cell migration towards extracellular matrix proteins. Recruits ANK3 to the plasma membrane. {ECO:0000269|PubMed:10022583, ECO:0000269|PubMed:10103075, ECO:0000269|PubMed:12391163, ECO:0000269|PubMed:12721290, ECO:0000269|PubMed:12812975, ECO:0000269|PubMed:14659567, ECO:0000269|PubMed:14761956, ECO:0000269|PubMed:15504324, ECO:0000269|PubMed:16623841}. PTM: Cleavage by metalloprotease ADAM8 in the extracellular part generates 2 soluble forms (125 kDa and 165 kDa) in vitro and is inhibited by metalloprotease inhibitors. In brain extracts, these two soluble forms are also present and are dramatically reduced in mice lacking ADAM8.; PTM: N-glycosylated. Contains N-linked oligosaccharides with a sulfated carbohydrate structure type HNK-1 (SO4-3-GlcUABeta1,3GalBeta1,4GlcNAc). {ECO:0000269|PubMed:8921253}.; PTM: O-glycosylated. {ECO:0000269|PubMed:8921253}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Note=Soluble forms produced by cleavage/shedding also exist.; SUBCELLULAR LOCATION: Processed neural cell adhesion molecule L1-like protein: Secreted, extracellular space, extracellular matrix. SUBUNIT: May interact with L1CAM. May interact with ITGB1/ITGA1 heterodimer and ITGB1/ITGA2 heterodimer as well as with ANK3. DOMAIN: The FIG[AQ]Y motif seems to be an ankyrin recruitment region.; DOMAIN: The DGEA motif seems to be a recognition site for integrin. TISSUE SPECIFICITY: Expressed in the brain, in the cerebellum and in the spinal cord. Detected in the retina and the optic nerve. Expressed in neurons and glial cells in the central nervous system and by Schwann cells in the peripheral nervous system. {ECO:0000269|PubMed:10103075, ECO:0000269|PubMed:15504324, ECO:0000269|PubMed:8921253}. +Q9Z0E0 NCDN_MOUSE Neurochondrin (M-Sema F-associating protein of 75 kDa) (Norbin) 729 78,895 Alternative sequence (1); Chain (1); Initiator methionine (1); Modified residue (4); Sequence conflict (2) FUNCTION: Probably involved in signal transduction, in the nervous system, via increasing cell surface localization of GRM5 and positively regulating its signaling. Required for the spatial learning process. Acts as a negative regulator of Ca(2+)-calmodulin-dependent protein kinase 2 (CaMK2) phosphorylation. May play a role in modulating melanin-concentrating hormone-mediated functions via its interaction with MCHR1 that interferes with G protein-coupled signal transduction. May be involved in bone metabolism. May also be involved in neurite outgrowth. {ECO:0000269|PubMed:15790563, ECO:0000269|PubMed:18572016, ECO:0000269|PubMed:20007903}. SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell projection, dendrite. Note=Localizes to somatic regions of neurons. {ECO:0000250}. SUBUNIT: Interacts with MCHR1 and GRM5 (By similarity). Interacts with SEMA4C and DIAPH1 (via FH3 domain). {ECO:0000250, ECO:0000269|PubMed:11162505, ECO:0000269|PubMed:18572016}. TISSUE SPECIFICITY: Expressed in the neuronal, chondral and bone tissues. Expressed in dendrites. Enriched in the brain in the surface layer I-IV. In brains, protein level increases in male but decreases in female with advancing age (at protein level). In adult brains, it is highly expressed in the forebrain and hindbrain. Highly expressed in the hippocampus, piriform cortex, septum, amygdaloid complex, medial geniculate nucleus, inferior colliculus, cerebellar nuclei and the nuclei of the Vth, VIIth, and XIIth cranial nerves. In bone tissues, it is expressed in osteoblasts and osteocytes. {ECO:0000269|PubMed:11162505, ECO:0000269|PubMed:11445285, ECO:0000269|PubMed:15007648, ECO:0000269|PubMed:20007903}. +P37040 NCPR_MOUSE NADPH--cytochrome P450 reductase (CPR) (P450R) (EC 1.6.2.4) 678 77,044 Binding site (7); Chain (1); Domain (2); Initiator methionine (1); Modified residue (1); Nucleotide binding (8); Topological domain (2); Transmembrane (1) TRANSMEM 23 43 Helical. {ECO:0000255|HAMAP-Rule:MF_03212}. TOPO_DOM 2 22 Lumenal. {ECO:0000255|HAMAP-Rule:MF_03212}.; TOPO_DOM 44 678 Cytoplasmic. {ECO:0000255|HAMAP-Rule:MF_03212}. FUNCTION: This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5. {ECO:0000255|HAMAP-Rule:MF_03212}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03212}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03212}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03212}. +E0CYC6 NAT8B_MOUSE Putative N-acetyltransferase 8B (EC 2.3.1.-) (Camello-like protein 2) (Putative acetyltransferase 1) (ATase1) 232 26,389 Chain (1); Domain (1); Topological domain (2); Transmembrane (1) TRANSMEM 63 83 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 62 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 84 232 Lumenal. {ECO:0000255}. FUNCTION: May have a lysine N-acetyltransferase activity catalyzing peptidyl-lysine N6-acetylation of various proteins. Thereby, may regulate apoptosis through the acetylation and the regulation of the expression of PROM1. May also regulate amyloid beta-peptide secretion through acetylation of BACE1 and the regulation of its expression in neurons. {ECO:0000250|UniProtKB:Q9UHF3}. SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q9UHF3}; Single-pass type II membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9UHF3}; Single-pass type II membrane protein {ECO:0000255}. Note=Enriched in the endoplasmic reticulum-Golgi intermediate compartment. {ECO:0000250|UniProtKB:Q9UHF3}. SUBUNIT: Interacts with PROM1. Interacts with BACE1. {ECO:0000250|UniProtKB:Q9UHF3}. TISSUE SPECIFICITY: Expressed in brain (at protein level). {ECO:0000269|PubMed:22267734}. +Q9WU42 NCOR2_MOUSE Nuclear receptor corepressor 2 (N-CoR2) (Silencing mediator of retinoic acid and thyroid hormone receptor) (SMRT) (SMRTe) (T3 receptor-associating factor) (TRAC) (Thyroid-, retinoic-acid-receptor-associated corepressor) 2472 269,807 Alternative sequence (1); Chain (1); Coiled coil (3); Compositional bias (6); Domain (2); Modified residue (42); Motif (2); Region (2); Sequence conflict (31) FUNCTION: Transcriptional corepressor. Mediates the transcriptional repression activity of some nuclear receptors by promoting chromatin condensation, thus preventing access of the basal transcription. Isoform 1 and isoform 5 have different affinities for different nuclear receptors. Involved in the regulation BCL6-dependent of the germinal center (GC) reactions, mainly through the control of the GC B-cells proliferation and survival. Recruited by ZBTB7A to the androgen response elements/ARE on target genes, negatively regulates androgen receptor signaling and androgen-induced cell proliferation. {ECO:0000250|UniProtKB:Q9Y618, ECO:0000269|PubMed:19144721}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Forms a large corepressor complex that contains SIN3A/B and histone deacetylases HDAC1 and HDAC2. This complex associates with the thyroid (TR) and the retinoid acid receptors (RAR) in the absence of ligand, and may stabilize their interaction with TFIIB. Interacts directly with RARA in the absence of ligand; the interaction represses RARA activity. Interacts (isoform SMRT) with HDAC10. Interacts with MINT. Component of the N-Cor repressor complex, at least composed of NCOR1, NCOR2, HDAC3, TBL1X, TBL1R, CORO2A and GPS2. Interacts with CBFA2T3 and ATXN1L. Interacts with RARB; the interaction is weak and does not repress RARB transactivational activity. Interacts with HDAC7 and C1D. Interacts with NR4A2; this interaction increases in the absence of PITX3. Interacts with BCL6 (via the BTB domain), required for BCL6 transcriptional repressor activity on a subset of target genes. Forms ternary complexes with BCOR and BCL6 on target gene promoters but, on enhancer elements, interacts with BCL6 and HDAC3 to repress proximal gene expression. May interact with DEAF1. Interacts with RXRA. Interacts with MECP2. Interacts with ZBTB7A (By similarity). Interacts with AR (By similarity). {ECO:0000250|UniProtKB:Q9Y618, ECO:0000269|PubMed:10640276, ECO:0000269|PubMed:11533236, ECO:0000269|PubMed:19144721, ECO:0000269|PubMed:23455674, ECO:0000269|PubMed:23770565, ECO:0000269|PubMed:9405624}. DOMAIN: The N-terminal region contains repression functions that are divided into three independent repression domains (RD1, RD2 and RD3). The C-terminal region contains the nuclear receptor-interacting domains that are divided in two separate interaction domains (ID1 and ID2).; DOMAIN: The two interaction domains (ID) contain a conserved sequence referred to as the CORNR box. This motif is required and sufficient to permit binding to unligated TR and RARS. Sequences flanking the CORNR box determine nuclear hormone receptor specificity. TISSUE SPECIFICITY: Ubiquitous. Also widely expressed in early embryos. +P48986 NDF6_MOUSE Neurogenic differentiation factor 6 (NeuroD6) (Helix-loop-helix protein mATH-2) (mATH2) (Protein NEX-1) (Protein atonal homolog 2) 337 38,644 Chain (1); Compositional bias (1); Domain (1); Motif (1) FUNCTION: Activates E box-dependent transcription in collaboration with TCF3/E47. May be a trans-acting factor involved in the development and maintenance of the mammalian nervous system. Transactivates the promoter of its own gene. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Efficient DNA binding requires dimerization with another bHLH protein. TISSUE SPECIFICITY: Specific to the nervous system of both embryos and adults. Highest levels in the cortical plate of the cerebrum. +Q8BKC8 PI4KB_MOUSE Phosphatidylinositol 4-kinase beta (PI4K-beta) (PI4Kbeta) (PtdIns 4-kinase beta) (EC 2.7.1.67) 816 91,515 Alternative sequence (2); Chain (1); Domain (2); Initiator methionine (1); Modified residue (14); Region (1); Sequence conflict (3) FUNCTION: Phosphorylates phosphatidylinositol (PI) in the first committed step in the production of the second messenger inositol-1,4,5,-trisphosphate (PIP). May regulate Golgi disintegration/reorganization during mitosis, possibly via its phosphorylation (By similarity). Involved in Golgi-to-plasma membrane trafficking (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}. Mitochondrion outer membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Rough endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Golgi apparatus {ECO:0000250}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9UBF8}. Note=Found in the outer membrane of mitochondria and membranes of the rough endoplasmic reticulum. Recruited to the Golgi complex by the small GTPase ARF to stimulate the synthesis of phosphatidylinositol 4,5-bisphosphate (PIP2) on the Golgi complex. Recruited to the Golgi apparatus membrane by ACBD3, GGA2 is also involved in the recruitment (By similarity). {ECO:0000250|UniProtKB:Q9UBF8}. SUBUNIT: Interacts with ARF1 and ARF3 in the Golgi complex, but not with ARF4, ARF5 or ARF6 (By similarity). Interacts with NCS1/FREQ in a calcium-independent manner. Interacts with CALN1/CABP8 and CALN2/CABP7; in a calcium-dependent manner; this interaction competes with NCS1/FREQ binding (By similarity). Interacts with ACBD3. Interacts with ARMH3, YWHAB, YWHAE, YWHAG, YWHAH, YWHAQ, YWHAZ and SFN (By similarity). Interacts with GGA2 (via VHS domain); the interaction is important for PI4KB location at the Golgi apparatus membrane (By similarity). {ECO:0000250|UniProtKB:O08561, ECO:0000250|UniProtKB:Q9UBF8}. +Q8CD54 PIEZ2_MOUSE Piezo-type mechanosensitive ion channel component 2 (Protein FAM38B) 2822 325,628 Alternative sequence (4); Chain (1); Coiled coil (2); Compositional bias (4); Erroneous initiation (3); Glycosylation (4); Modified residue (1); Sequence conflict (1); Transmembrane (37) TRANSMEM 5 25 Helical. {ECO:0000255}.; TRANSMEM 27 47 Helical. {ECO:0000255}.; TRANSMEM 62 82 Helical. {ECO:0000255}.; TRANSMEM 119 139 Helical. {ECO:0000255}.; TRANSMEM 214 234 Helical. {ECO:0000255}.; TRANSMEM 237 257 Helical. {ECO:0000255}.; TRANSMEM 266 286 Helical. {ECO:0000255}.; TRANSMEM 336 356 Helical. {ECO:0000255}.; TRANSMEM 505 525 Helical. {ECO:0000255}.; TRANSMEM 541 561 Helical. {ECO:0000255}.; TRANSMEM 581 598 Helical. {ECO:0000255}.; TRANSMEM 682 702 Helical. {ECO:0000255}.; TRANSMEM 708 728 Helical. {ECO:0000255}.; TRANSMEM 736 756 Helical. {ECO:0000255}.; TRANSMEM 786 806 Helical. {ECO:0000255}.; TRANSMEM 949 969 Helical. {ECO:0000255}.; TRANSMEM 975 995 Helical. {ECO:0000255}.; TRANSMEM 1002 1022 Helical. {ECO:0000255}.; TRANSMEM 1070 1090 Helical. {ECO:0000255}.; TRANSMEM 1151 1171 Helical. {ECO:0000255}.; TRANSMEM 1187 1207 Helical. {ECO:0000255}.; TRANSMEM 1234 1254 Helical. {ECO:0000255}.; TRANSMEM 1308 1328 Helical. {ECO:0000255}.; TRANSMEM 1332 1352 Helical. {ECO:0000255}.; TRANSMEM 1371 1391 Helical. {ECO:0000255}.; TRANSMEM 1422 1442 Helical. {ECO:0000255}.; TRANSMEM 1979 2001 Helical. {ECO:0000255}.; TRANSMEM 2008 2028 Helical. {ECO:0000255}.; TRANSMEM 2037 2057 Helical. {ECO:0000255}.; TRANSMEM 2261 2281 Helical. {ECO:0000255}.; TRANSMEM 2302 2322 Helical. {ECO:0000255}.; TRANSMEM 2330 2350 Helical. {ECO:0000255}.; TRANSMEM 2360 2380 Helical. {ECO:0000255}.; TRANSMEM 2397 2414 Helical. {ECO:0000255}.; TRANSMEM 2428 2448 Helical. {ECO:0000255}.; TRANSMEM 2476 2496 Helical. {ECO:0000255}.; TRANSMEM 2732 2752 Helical. {ECO:0000255}. FUNCTION: Component of a mechanosensitive channel required for rapidly adapting mechanically activated (MA) currents (PubMed:20813920, PubMed:24717433). Required for Merkel-cell mechanotransduction (PubMed:24717433). Plays a major role in light-touch mechanosensation (PubMed:25471886). {ECO:0000269|PubMed:20813920, ECO:0000269|PubMed:24717433, ECO:0000269|PubMed:25471886}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Homooligomer, most likely homotetramer. Interacts with STOML3. {ECO:0000269|PubMed:22343900, ECO:0000269|PubMed:24662763}. TISSUE SPECIFICITY: Expressed in bladder, colon, and lung, but less abundant in kidney or skin (PubMed:20813920). Strong expression is observed in dorsal root ganglia (DRG) sensory neurons (PubMed:20813920). Expressed in a wide range of cutaneous low-threshold mechanoreceptors (LTMRs), including Merkel cells and Meissner's corpuscles (PubMed:24717433, PubMed:25471886). {ECO:0000269|PubMed:20813920, ECO:0000269|PubMed:24717433, ECO:0000269|PubMed:25471886}. +Q64323 PIGA_MOUSE N-acetylglucosaminyl-phosphatidylinositol biosynthetic protein (GlcNAc-PI synthesis protein) (Phosphatidylinositol-glycan biosynthesis class A protein) (PIG-A) 485 54,469 Chain (1); Modified residue (1); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 423 443 Helical. {ECO:0000255}. TOPO_DOM 1 422 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 444 485 Lumenal. {ECO:0000255}. Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis. FUNCTION: Necessary for the synthesis of N-acetylglucosaminyl-phosphatidylinositol, the very early intermediate in GPI-anchor biosynthesis. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. SUBUNIT: Associates with PIGC, PIGH, PIGP, PIGQ and DPM2. The latter is not essential for activity. Interacts directly with PIGY (By similarity). {ECO:0000250}. +Q8BTG7 NDRG4_MOUSE Protein NDRG4 (N-myc downstream-regulated gene 4 protein) (Protein Ndr4) 352 38,509 Alternative sequence (2); Chain (1); Compositional bias (1); Erroneous initiation (1); Modified residue (4) FUNCTION: Contributes to the maintenance of intracerebral BDNF levels within the normal range, which is necessary for the preservation of spatial learning and the resistance to neuronal cell death caused by ischemic stress. May enhance growth factor-induced ERK1 and ERK2 phosphorylation. May attenuate NGF-promoted ELK1 phosphorylation in a microtubule-dependent manner. {ECO:0000269|PubMed:21636852}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. TISSUE SPECIFICITY: Predominantly expressed in the brain (at protein level). Detected in neurons of various parts of brain, including the olfactory bulb, olfactory tuberculum, cerebral cortex, striatum, hippocampus, dentate gyrus, thalamus, hypothalamus, mesencephalon, cerebellum, pons and medulla oblongata. {ECO:0000269|PubMed:21636852}. +Q9CPP6 NDUA5_MOUSE NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5 (Complex I subunit B13) (Complex I-13kD-B) (CI-13kD-B) (NADH-ubiquinone oxidoreductase 13 kDa-B subunit) 116 13,360 Beta strand (3); Chain (1); Helix (4); Initiator methionine (1); Modified residue (8); Sequence conflict (4); Turn (2) FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. {ECO:0000269|PubMed:24154540}. PTM: Acetylation of Lys-98 is observed in liver mitochondria from fasted mice but not from fed mice. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q16718}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q16718}; Matrix side {ECO:0000250|UniProtKB:Q16718}. SUBUNIT: Complex I is composed of 45 different subunits. {ECO:0000250|UniProtKB:Q16718}. +Q9CPU2 NDUB2_MOUSE NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, mitochondrial (Complex I-AGGG) (CI-AGGG) (NADH-ubiquinone oxidoreductase AGGG subunit) 105 11,967 Beta strand (2); Chain (1); Helix (1); Transit peptide (1); Turn (1) FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. {ECO:0000250|UniProtKB:O95178}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:O95178}; Peripheral membrane protein {ECO:0000250|UniProtKB:O95178}; Matrix side {ECO:0000250|UniProtKB:O95178}. SUBUNIT: Complex I is composed of 45 different subunits. {ECO:0000250|UniProtKB:O95178}. +Q9CQJ8 NDUB9_MOUSE NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9 (Complex I-B22) (CI-B22) (NADH-ubiquinone oxidoreductase B22 subunit) 179 21,984 Beta strand (5); Chain (1); Helix (12); Initiator methionine (1); Modified residue (2); Turn (2) FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed to be not involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. {ECO:0000250|UniProtKB:Q9Y6M9}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9Y6M9}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9Y6M9}; Matrix side {ECO:0000250|UniProtKB:Q9Y6M9}. SUBUNIT: Mammalian complex I is composed of 45 different subunits. {ECO:0000250|UniProtKB:Q9Y6M9}. +Q09098 PATE4_MOUSE Prostate and testis expressed protein 4 (Calcium transport inhibitor) (Caltrin) (PATE-like protein B) (PATE-B) (Seminal vesicle protein 7) (Seminal vesicle protein VII) (SVS VII) 99 11,058 Chain (1); Disulfide bond (4); Domain (1); Mass spectrometry (1); Sequence conflict (4); Signal peptide (1) FUNCTION: Enhances sperm motility. Binds to calmodulin and inhibits calcium transport into spermatozoa. May modulate the function of nicotinic acetylcholine receptors. {ECO:0000269|PubMed:11118436}. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Expressed in prostate, testis, eye, kidney and skeletal muscle. Expressed in the dorsal lobe of prostate. Not expressed in the ventral lobe of prostate. {ECO:0000269|PubMed:18387948}. +Q9WVP9 MX2_MOUSE Interferon-induced GTP-binding protein Mx2 (Myxovirus resistance protein 2) 655 74,292 Chain (1); Domain (2); Nucleotide binding (3); Region (5); Sequence conflict (1) FUNCTION: Interferon-induced dynamin-like GTPase with antiviral activity against vesicular stomatitis virus (VSV) and Hantaan virus (HNTV). {ECO:0000269|PubMed:10233954, ECO:0000269|PubMed:11266216}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10233954}. +P22366 MYD88_MOUSE Myeloid differentiation primary response protein MyD88 296 33,753 Alternative sequence (1); Chain (1); Domain (2); Erroneous initiation (1); Modified residue (1); Mutagenesis (1); Region (1); Sequence conflict (2) FUNCTION: Adapter protein involved in the Toll-like receptor and IL-1 receptor signaling pathway in the innate immune response (PubMed:9697844). Acts via IRAK1, IRAK2, IRF7 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (PubMed:9575168, PubMed:9697844). Increases IL-8 transcription. Involved in IL-18-mediated signaling pathway (PubMed:9697844). Isoform 2 is defective in its ability to induce IRAK phosphorylation and NF-kappa-B activation and can function as a negative regulator of activation by IL-1 or lipopolysaccharide (LPS) (PubMed:11909531). Activates IRF1 resulting in its rapid migration into the nucleus to mediate an efficient induction of IFN-beta, NOS2/INOS, and IL12A genes (PubMed:17018642). MyD88-mediated signaling in intestinal epithelial cells is crucial for maintenance of gut homeostasis and controls the expression of the antimicrobial lectin REG3G in the small intestine (PubMed:17635956, PubMed:21998396). Mediates leukocyte recruitment at the inflammatory site (PubMed:18941239). {ECO:0000269|PubMed:11909531, ECO:0000269|PubMed:17018642, ECO:0000269|PubMed:17635956, ECO:0000269|PubMed:18941239, ECO:0000269|PubMed:21998396, ECO:0000269|PubMed:9575168, ECO:0000269|PubMed:9697844}. PTM: Ubiquitinated; undergoes 'Lys-63'-linked polyubiquitination. OTUD4 specifically hydrolyzes 'Lys-63'-linked polyubiquitinated MYD88. {ECO:0000250|UniProtKB:Q99836}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17018642}. Nucleus {ECO:0000250|UniProtKB:Q99836}. SUBUNIT: Homodimer. Also forms heterodimers with TIRAP. Binds to TLR2, TLR4, IRAK1, IRAK2 and IRAK4 via their respective TIR domains. Interacts with IL18R1. Interacts with BMX, IL1RL1, IKBKE and IRF7. Interacts with LRRFIP1 and LRRFIP2; this interaction positively regulates Toll-like receptor (TLR) signaling in response to agonist. Interacts with FLII. LRRFIP1 and LRRFIP2 compete with FLII for MYD88-binding. Interacts with IRF1. Upon IL1B treatment, forms a complex with PELI1, IRAK1, IRAK4 and TRAF6; this complex recruits MAP3K7/TAK1, TAB1 and TAB2 to mediate NF-kappa-B activation. Direct binding of SMAD6 to PELI1 prevents the complex formation and hence negatively regulates IL1R-TLR signaling and eventually NF-kappa-B-mediated gene expression. May interact with PIK3AP1. Interacts (via TIR domain) with DHX9 (via H2A and OB-fold regions); this interaction is direct. Interacts with OTUD4 deubiquitinase; the interaction is direct (PubMed:29395066). {ECO:0000250|UniProtKB:Q99836, ECO:0000269|PubMed:11909531, ECO:0000269|PubMed:16951688, ECO:0000269|PubMed:17018642, ECO:0000269|PubMed:22187460, ECO:0000269|PubMed:29395066, ECO:0000269|PubMed:9575168, ECO:0000269|PubMed:9697844}. DOMAIN: The intermediate domain (ID) is required for the phosphorylation and activation of IRAK. {ECO:0000269|PubMed:11909531}. TISSUE SPECIFICITY: Detected in bone marrow. Isoform 1 is expressed in testis, kidney, lung, ovary, adrenal gland, provstate, thymus and heart, and weakly in skeletal muscle, liver, spleen and brain. Isoform 2 is mainly expressed in the spleen and weakly in brain. {ECO:0000269|PubMed:11909531, ECO:0000269|PubMed:21998396, ECO:0000269|PubMed:2374694, ECO:0000269|PubMed:9013863, ECO:0000269|PubMed:9575168}. +Q8C854 MYEF2_MOUSE Myelin expression factor 2 (MEF-2) (MyEF-2) 591 63,295 Alternative sequence (7); Chain (1); Compositional bias (1); Cross-link (1); Domain (3); Erroneous initiation (2); Modified residue (3); Sequence conflict (2) FUNCTION: Transcriptional repressor of the myelin basic protein gene (MBP). Binds to the proximal MB1 element 5'-TTGTCC-3' of the MBP promoter. Its binding to MB1 and function are inhibited by PURA. {ECO:0000269|PubMed:7534248, ECO:0000269|PubMed:7539003, ECO:0000269|PubMed:9282330}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Monomer. {ECO:0000269|PubMed:9282330}. TISSUE SPECIFICITY: Highly expressed in the brain. {ECO:0000269|PubMed:7539003}. +P13541 MYH3_MOUSE Myosin-3 (Myosin heavy chain 3) 1940 223,791 Chain (1); Coiled coil (1); Domain (3); Modified residue (1); Nucleotide binding (1); Region (2); Sequence conflict (2) FUNCTION: Muscle contraction. SUBCELLULAR LOCATION: Cytoplasm, myofibril. Note=Thick filaments of the myofibrils. SUBUNIT: Muscle myosin is a hexameric protein that consists of 2 heavy chain subunits (MHC), 2 alkali light chain subunits (MLC) and 2 regulatory light chain subunits (MLC-2). DOMAIN: The rodlike tail sequence is highly repetitive, showing cycles of a 28-residue repeat pattern composed of 4 heptapeptides, characteristic for alpha-helical coiled coils.; DOMAIN: Limited proteolysis of myosin heavy chain produces 1 light meromyosin (LMM) and 1 heavy meromyosin (HMM). HMM can be further cleaved into 2 globular subfragments (S1) and 1 rod-shaped subfragment (S2). {ECO:0000305}. +Q5SX39 MYH4_MOUSE Myosin-4 (Myosin heavy chain 2b) (MyHC-2b) (Myosin heavy chain 4) 1939 222,859 Chain (1); Coiled coil (1); Domain (3); Modified residue (48); Nucleotide binding (1); Region (2) FUNCTION: Muscle contraction. SUBCELLULAR LOCATION: Cytoplasm, myofibril. Note=Thick filaments of the myofibrils. SUBUNIT: Muscle myosin is a hexameric protein that consists of 2 heavy chain subunits (MHC), 2 alkali light chain subunits (MLC) and 2 regulatory light chain subunits (MLC-2). DOMAIN: The rodlike tail sequence is highly repetitive, showing cycles of a 28-residue repeat pattern composed of 4 heptapeptides, characteristic for alpha-helical coiled coils.; DOMAIN: Limited proteolysis of myosin heavy chain produces 1 light meromyosin (LMM) and 1 heavy meromyosin (HMM). HMM can be further cleaved into 2 globular subfragments (S1) and 1 rod-shaped subfragment (S2). {ECO:0000305}. +Q8CFC2 MYT1_MOUSE Myelin transcription factor 1 (MyT1) (Neural zinc finger factor 2) (NZF-2) 1127 123,576 Alternative sequence (2); Beta strand (6); Chain (1); Compositional bias (2); Erroneous initiation (1); Sequence conflict (7); Turn (1); Zinc finger (7) FUNCTION: Binds to the promoter region of genes encoding proteolipid proteins of the central nervous system. May play a role in the development of neurons and oligodendroglia in the CNS. May regulate a critical transition point in oligodendrocyte lineage development by modulating oligodendrocyte progenitor proliferation relative to terminal differentiation and up-regulation of myelin gene transcription (By similarity). {ECO:0000250, ECO:0000269|PubMed:9373037}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with STEAP3. {ECO:0000250}. DOMAIN: Contains 7 zinc fingers of the C2HC class arranged in two widely separated clusters. These two domains of DNA binding can function independently and recognize the same DNA sequence. TISSUE SPECIFICITY: Isoform 1 is more predominant than isoform 2 at all stages of development and adulthood. Expressed in differentiated neurons especially at higher levels in newly generated ones. {ECO:0000269|PubMed:12351189}. +Q3UIJ9 MYZAP_MOUSE Myocardial zonula adherens protein 466 53,897 Chain (1); Coiled coil (2); Signal peptide (1) FUNCTION: Plays a role in cellular signaling via Rho-related GTP-binding proteins and activation of transcription factor SRF. Targets TJP1 to cell junctions (By similarity). In cortical neurons, may play a role in glutaminergic signal transduction through interaction with the NMDA receptor subunit GRIN1 (By similarity). {ECO:0000250, ECO:0000269|PubMed:20093627}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:20093627}. Cell membrane {ECO:0000269|PubMed:20093627}; Peripheral membrane protein {ECO:0000269|PubMed:20093627}; Cytoplasmic side {ECO:0000269|PubMed:20093627}. Cytoplasm, myofibril, sarcomere, I band {ECO:0000269|PubMed:20093627}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:20093627}. Cell junction {ECO:0000250|UniProtKB:P0CAP1}. Note=Detected predominantly at the intercalated disk in cardiomyocytes, and at low levels on sarcomeric Z disks. Colocalizes with F-actin. Colocalizes with cortical actin. SUBUNIT: Interacts with DSP, MPRIP and TJP1/ZO1. Interaction with MPRIP inhibits the activation of transcription factor SRF. Interacts with GRIN1. Interacts with DYNLL1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Detected in heart myocardium and lung. {ECO:0000269|PubMed:20093627}. +O35973 PER1_MOUSE Period circadian protein homolog 1 (mPER1) (Circadian clock protein PERIOD 1) (Circadian pacemaker protein Rigui) 1291 136,373 Beta strand (15); Chain (1); Compositional bias (7); Domain (3); Helix (11); Modified residue (9); Motif (5); Mutagenesis (8); Region (3); Sequence conflict (3); Turn (4) FUNCTION: Transcriptional repressor which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, ARNTL/BMAL1, ARNTL2/BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and ARNTL/BMAL1 or ARNTL2/BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-ARNTL/BMAL1|ARNTL2/BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress ARNTL/BMAL1 transcription, respectively. Regulates circadian target genes expression at post-transcriptional levels, but may not be required for the repression at transcriptional level. Controls PER2 protein decay. Represses CRY2 preventing its repression on CLOCK/ARNTL target genes such as FXYD5 and SCNN1A in kidney and PPARA in liver. Besides its involvement in the maintenance of the circadian clock, has an important function in the regulation of several processes. Participates in the repression of glucocorticoid receptor NR3C1/GR-induced transcriptional activity by reducing the association of NR3C1/GR to glucocorticoid response elements (GREs) by ARNTL:CLOCK. Plays a role in the modulation of the neuroinflammatory state via the regulation of inflammatory mediators release, such as CCL2 and IL6. In spinal astrocytes, negatively regulates the MAPK14/p38 and MAPK8/JNK MAPK cascades as well as the subsequent activation of NFkappaB. Coordinately regulates the expression of multiple genes that are involved in the regulation of renal sodium reabsorption. Can act as gene expression activator in a gene and tissue specific manner, in kidney enhances WNK1 and SLC12A3 expression in collaboration with CLOCK. Modulates hair follicle cycling. Represses the CLOCK-ARNTL/BMAL1 induced transcription of BHLHE40/DEC1. {ECO:0000269|PubMed:11395012, ECO:0000269|PubMed:14672706, ECO:0000269|PubMed:15888647, ECO:0000269|PubMed:21930935, ECO:0000269|PubMed:22331899, ECO:0000269|PubMed:24154698, ECO:0000269|PubMed:24378737, ECO:0000269|PubMed:24610784, ECO:0000269|PubMed:9856465}. PTM: Phosphorylated on serine residues by CSNK1D, CSNK1E and probably also by CSNK1G2. Phosphorylation by CSNK1D or CSNK1E promotes nuclear location of PER proteins as well as ubiquitination and subsequent degradation. May be dephosphorylated by PP1. {ECO:0000269|PubMed:11865049}.; PTM: Ubiquitinated; requires phosphorylation by CSNK1E and interaction with BTRC and FBXW11. Deubiquitinated by USP2. {ECO:0000269|PubMed:11865049, ECO:0000269|PubMed:23213472}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Nucleocytoplasmic shuttling is effected by interaction with other circadian core oscillator proteins and/or by phosphorylation. Retention of PER1 in the cytoplasm occurs through PER1-PER2 heterodimer formation. Translocate to the nucleus after phosphorylation by CSNK1D or CSNK1E. Also translocated to the nucleus by CRY1 or CRY2. SUBUNIT: Homodimer. Component of the circadian core oscillator, which includes the CRY proteins, CLOCK or NPAS2, ARNTL/BMAL1 or ARNTL2/BMAL2, CSNK1D and/or CSNK1E, TIMELESS, and the PER proteins. Interacts directly with TIMELESS, PER2, PER3 and, through a C-terminal domain, with CRY1 and CRY2. Interacts with ARNTL/BMAL1 and CLOCK. Interacts with GPRASP1. Interacts (phosphorylated) with BTRC and FBXW11; the interactions trigger proteasomal degradation. Interacts with NONO, WDR5 and SFPQ. Interacts with U2af1l4 (Isoform 3). Interacts with USP2. {ECO:0000269|PubMed:10231394, ECO:0000269|PubMed:10428031, ECO:0000269|PubMed:10848614, ECO:0000269|PubMed:11875063, ECO:0000269|PubMed:14701732, ECO:0000269|PubMed:16478995, ECO:0000269|PubMed:16717091, ECO:0000269|PubMed:22331899, ECO:0000269|PubMed:22966205, ECO:0000269|PubMed:23213472, ECO:0000269|PubMed:24154698, ECO:0000269|PubMed:24837677, ECO:0000269|PubMed:9856465}. TISSUE SPECIFICITY: In brain, highest expression is observed in the SCN. Highly expressed in the pyramidal cell layer of the piriform cortex, the periventricular part of the caudate-putamen, many thalamic nuclei, and the granular layer of the cerebellar cortex. Weaker expression is detected in most area of the brain, including cortical and non cortical structures. Expression but no oscillations occurs in the glomerular and mitral cell layers of the olfactory bulb, the internal granular layer of the cerebellum, the cornu ammonis and dentate gyrus of the hyppocampus, the cerebral and piriform cortices. Expressed in the renal cortex (at protein level). Also found in heart, brain, bladder, lumbar spinal cord, spleen, lung, liver, skeletal muscle and testis. {ECO:0000269|PubMed:10521578, ECO:0000269|PubMed:16790549, ECO:0000269|PubMed:24154698, ECO:0000269|PubMed:24603368, ECO:0000269|PubMed:24610784, ECO:0000269|PubMed:9333243, ECO:0000269|PubMed:9427249}. +Q99MD8 MYNN_MOUSE Myoneurin 610 68,593 Alternative sequence (3); Chain (1); Compositional bias (1); Domain (1); Motif (2); Sequence conflict (7); Zinc finger (8) SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14694499}. TISSUE SPECIFICITY: Mainly expressed in the neuromuscular system. Located in and around synaptic myonuclei in adult muscle. Expression is dysregulated after nerve injury. Also found in the cerebellum, testis, heart, brain and liver. {ECO:0000269|PubMed:10873615, ECO:0000269|PubMed:14694499}. +Q9QY36 NAA10_MOUSE N-alpha-acetyltransferase 10 (EC 2.3.1.255) (N-terminal acetyltransferase complex ARD1 subunit homolog A) (NatA catalytic subunit Naa10) 235 26,520 Chain (1); Domain (1); Modified residue (6); Region (1) FUNCTION: Catalytic subunit of the N-terminal acetyltransferase A (NatA) complex which displays alpha (N-terminal) acetyltransferase activity (PubMed:12888564). Acetylates amino termini that are devoid of initiator methionine (By similarity). The alpha (N-terminal) acetyltransferase activity may be important for vascular, hematopoietic and neuronal growth and development (By similarity). Without NAA15, displays epsilon (internal) acetyltransferase activity towards HIF1A, thereby promoting its degradation (PubMed:12464182). Represses MYLK kinase activity by acetylation, and thus represses tumor cell migration (By similarity). Acetylates, and stabilizes TSC2, thereby repressing mTOR activity and suppressing cancer development (By similarity). Acetylates HSPA1A and HSPA1B at 'Lys-77' which enhances its chaperone activity and leads to preferential binding to co-chaperone HOPX (By similarity). Acts as a negative regulator of sister chromatid cohesion during mitosis (By similarity). {ECO:0000250|UniProtKB:P41227, ECO:0000269|PubMed:12464182, ECO:0000269|PubMed:12888564}. PTM: Cleaved by caspases during apoptosis. {ECO:0000250|UniProtKB:P41227}.; PTM: Phosphorylation by IKBKB/IKKB at Ser-209 destabilises NAA10 and promotes its proteasome-mediated degradation.; PTM: Autoacetylated at Lys-136 which stimulates its catalytic activity. {ECO:0000250|UniProtKB:P41227}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12888564}. Nucleus {ECO:0000250|UniProtKB:P41227}. Note=Also present in the free cytosolic and cytoskeleton-bound polysomes. {ECO:0000250|UniProtKB:P41227}. SUBUNIT: Component of the N-terminal acetyltransferase A (NatA) complex composed of NAA10 and NAA15 or NAA16 (By similarity). Interacts with HIF1A (via its ODD domain); the interaction increases HIF1A protein stability during normoxia, an down-regulates it when induced by hypoxia (PubMed:12464182). Interacts with NAA50 and with the ribosome (By similarity). Binds to MYLK (By similarity). Associates with HYPK when in complex with NAA15 (By similarity). Interacts with NAA15 (PubMed:12888564). Interacts with NAA16 (By similarity). Interacts (via its C-terminal domain) with TSC2, leading to its acetylation (By similarity). Interacts with NAA16 (By similarity). Interacts with IKBKB (By similarity). Interacts with HSPA1A and HSPA1B leading to its acetylation (By similarity). {ECO:0000250|UniProtKB:P41227, ECO:0000269|PubMed:12464182, ECO:0000269|PubMed:12888564}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12888564}. +Q6A037 N4BP1_MOUSE NEDD4-binding protein 1 (N4BP1) 893 99,147 Chain (1); Erroneous initiation (1); Modified residue (5); Sequence conflict (4) FUNCTION: Inhibitor of the E3 ubiquitin-protein ligase ITCH. Acts by interacting with the second WW domain of ITCH, leading to compete with ITCH's substrates and impairing ubiquitination of substrates. {ECO:0000269|PubMed:17592138}. PTM: Monoubiquitinated by NEDD4. Polyubiquitinated, leading to its degradation by the proteasome. Sumoylated with SUMO1, abrogating polyubiquitination and subsequent degradation. Desumoylated by SENP1, leading to accumulation in PML nuclear bodies. {ECO:0000269|PubMed:11717310, ECO:0000269|PubMed:20233849}. SUBCELLULAR LOCATION: Nucleus, nucleolus. Nucleus, PML body. Note=Primarily localizes to the nucleolus. Also localizes to the PML nuclear bodies, when desumoylated. SUBUNIT: Interacts with NEDD4. Interacts with ITCH (via WW domain 2). {ECO:0000269|PubMed:11717310, ECO:0000269|PubMed:17592138}. +Q9R123 NAA80_MOUSE N-alpha-acetyltransferase 80 (EC 2.3.1.-) (N-acetyltransferase 6) (Protein fusion-2 homolog) (Protein fus-2) 314 34,583 Binding site (2); Chain (1); Domain (1); Region (3) FUNCTION: N-alpha-acetyltransferase that specifically mediates the acetylation of the acidic amino terminus of processed forms of beta- and gamma-actin (ACTB and ACTG, respectively). N-terminal acetylation of processed beta- and gamma-actin regulates actin filament depolymerization and elongation. In vivo, preferentially displays N-terminal acetyltransferase activity towards acid N-terminal sequences starting with Asp-Asp-Asp and Glu-Glu-Glu. In vitro, shows high activity towards Met-Asp-Glu-Leu and Met-Asp-Asp-Asp. May act as a tumor suppressor. {ECO:0000250|UniProtKB:Q93015}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q93015}. +Q8VC48 PEX12_MOUSE Peroxisome assembly protein 12 (Peroxin-12) 359 40,633 Chain (1); Compositional bias (1); Topological domain (3); Transmembrane (2); Zinc finger (1) TRANSMEM 159 179 Helical. {ECO:0000255}.; TRANSMEM 240 260 Helical. {ECO:0000255}. TOPO_DOM 1 158 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 180 239 Peroxisomal matrix. {ECO:0000255}.; TOPO_DOM 261 359 Cytoplasmic. {ECO:0000255}. FUNCTION: Required for protein import into peroxisomes. SUBCELLULAR LOCATION: Peroxisome membrane; Multi-pass membrane protein. SUBUNIT: Interacts with PEX5 and PEX10. Interacts with PEX19 via its cytoplasmic domain (By similarity). {ECO:0000250}. +Q8JZV7 NAGA_MOUSE N-acetylglucosamine-6-phosphate deacetylase (GlcNAc 6-P deacetylase) (EC 3.5.1.25) (Amidohydrolase domain-containing protein 2) 409 43,501 Active site (1); Binding site (1); Chain (1); Metal binding (3); Region (4); Sequence conflict (1) Amino-sugar metabolism; N-acetylneuraminate degradation. FUNCTION: Hydrolyzes the N-glycolyl group from N-glycolylglucosamine 6-phosphate (GlcNGc-6-P) in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway. {ECO:0000250|UniProtKB:Q9Y303}. +Q99P21 MUTYH_MOUSE Adenine DNA glycosylase (EC 3.2.2.31) (MutY homolog) (mMYH) 515 57,723 Active site (1); Chain (1); Domain (1); Metal binding (4); Motif (1); Sequence conflict (5); Site (1) FUNCTION: Involved in oxidative DNA damage repair. Initiates repair of A*oxoG to C*G by removing the inappropriately paired adenine base from the DNA backbone. Possesses both adenine and 2-OH-A DNA glycosylase activities. {ECO:0000269|PubMed:11160897, ECO:0000269|PubMed:14742662}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14742662}. Mitochondrion {ECO:0000269|PubMed:14742662}. TISSUE SPECIFICITY: Expressed in heart, lung, liver, intestine, brain and thymus. {ECO:0000269|PubMed:14742662}. +Q99JF5 MVD1_MOUSE Diphosphomevalonate decarboxylase (EC 4.1.1.33) (Mevalonate (diphospho)decarboxylase) (MDDase) (Mevalonate pyrophosphate decarboxylase) 401 44,072 Beta strand (20); Chain (1); Compositional bias (1); Helix (15); Initiator methionine (1); Modified residue (1); Sequence conflict (9); Turn (2) Steroid biosynthesis; cholesterol biosynthesis. FUNCTION: Performs the first committed step in the biosynthesis of isoprenes. SUBUNIT: Homodimer. {ECO:0000250}. +Q61879 MYH10_MOUSE Myosin-10 (Cellular myosin heavy chain, type B) (Myosin heavy chain 10) (Myosin heavy chain, non-muscle IIb) (Non-muscle myosin heavy chain B) (NMMHC-B) (Non-muscle myosin heavy chain IIb) (NMMHC II-b) (NMMHC-IIB) 1976 228,996 Chain (1); Coiled coil (1); Domain (3); Modified residue (16); Nucleotide binding (1); Region (1) FUNCTION: Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2. During cell spreading, plays an important role in cytoskeleton reorganization, focal contacts formation (in the central part but not the margins of spreading cells), and lamellipodial extension; this function is mechanically antagonized by MYH9 (By similarity). Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping. {ECO:0000250}. PTM: Phosphorylated by ABL2. {ECO:0000269|PubMed:17892306}. SUBCELLULAR LOCATION: Cell projection, lamellipodium {ECO:0000250}. Note=Colocalizes with MCC at the leading edge of migrating cells. {ECO:0000250}. SUBUNIT: Myosin is a hexameric protein that consists of 2 heavy chain subunits (MHC), 2 alkali light chain subunits (MLC) and 2 regulatory light chain subunits (MLC-2). Interacts with PLEKHG6 (By similarity). Interacts with ECPAS (By similarity). Interacts with LARP6 (By similarity). Interacts with MCC (By similarity). Interacts with KIF26B (PubMed:20439720). Interacts with C9orf135 homolog (By similarity). {ECO:0000250|UniProtKB:P35580, ECO:0000269|PubMed:20439720}. DOMAIN: The rodlike tail sequence is highly repetitive, showing cycles of a 28-residue repeat pattern composed of 4 heptapeptides, characteristic for alpha-helical coiled coils. TISSUE SPECIFICITY: In newborn kidney, expressed in the mesenchyme and ureteric buds. {ECO:0000269|PubMed:20439720}. +Q7TPH6 MYCB2_MOUSE E3 ubiquitin-protein ligase MYCBP2 (EC 2.3.2.-) (Myc-binding protein 2) (Pam/highwire/rpm-1 protein) (Protein Magellan) (Protein associated with Myc) 4749 521,232 Active site (2); Alternative sequence (1); Beta strand (27); Chain (1); Compositional bias (6); Disulfide bond (1); Domain (1); Helix (1); Metal binding (24); Modified residue (20); Mutagenesis (1); Region (4); Repeat (6); Sequence conflict (6); Site (3); Turn (1); Zinc finger (2) Protein modification; protein ubiquitination. FUNCTION: Atypical E3 ubiquitin-protein ligase which specifically mediates ubiquitination of threonine and serine residues on target proteins, instead of ubiquitinating lysine residues (By similarity). Shows esterification activity towards both threonine and serine, with a preference for threonine, and acts via two essential catalytic cysteine residues that relay ubiquitin to its substrate via thioester intermediates (By similarity). Interacts with the E2 enzymes UBE2D1, UBE2D3, UBE2E1 and UBE2L3 (By similarity). Plays a key role in neural development, probably by mediating ubiquitination of threonine residues on target proteins (By similarity). Involved in different processes such as regulation of neurite outgrowth, synaptic growth, synaptogenesis and axon degeneration (PubMed:14729956, PubMed:17901218, PubMed:18031680). Required for the formation of major central nervous system axon tracts (PubMed:17901218, PubMed:18031680). Required for proper axon growth by regulating axon navigation and axon branching: acts by regulating the subcellular location and stability of MAP3K12/DLK (PubMed:18031680). Required for proper localization of retinogeniculate projections but not for eye-specific segregation (PubMed:19371781, PubMed:21324225). Regulates axon guidance in the olfactory system (PubMed:23525682). Involved in Wallerian axon degeneration, an evolutionarily conserved process that drives the loss of damaged axons: acts by promoting destabilization of NMNAT2, probably via ubiquitination of NMNAT2 (PubMed:23665224). Catalyzes ubiquitination of threonine and/or serine residues on NMNAT2, consequences of threonine and/or serine ubiquitination are however unknown (By similarity). Regulates the internalization of TRPV1 in peripheral sensory neurons (PubMed:21098484). May mediate ubiquitination and subsequent proteasomal degradation of TSC2/tuberin (By similarity). Independently of the E3 ubiquitin-protein ligase activity, also acts as a guanosine exchange factor (GEF) for RAN in neurons of dorsal root ganglia (PubMed:26304119). May function as a facilitator or regulator of transcriptional activation by MYC (By similarity). {ECO:0000250|UniProtKB:O75592, ECO:0000269|PubMed:14729956, ECO:0000269|PubMed:17901218, ECO:0000269|PubMed:18031680, ECO:0000269|PubMed:19371781, ECO:0000269|PubMed:21098484, ECO:0000269|PubMed:21324225, ECO:0000269|PubMed:23525682, ECO:0000269|PubMed:23665224, ECO:0000269|PubMed:26304119}. PTM: Autoubiquitinated. {ECO:0000250|UniProtKB:O75592}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26304119}. Cell projection, axon {ECO:0000269|PubMed:18031680}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:18031680}. Note=Localizes to axon shafts and associates with microtubule cytoskeleton (PubMed:18031680). Translocates to the nucleus following interaction with sumoylated RANGAP1 (PubMed:26304119). {ECO:0000269|PubMed:18031680, ECO:0000269|PubMed:26304119}. SUBUNIT: Interacts with MYC (By similarity). Interacts with TSC2 (tuberin) when TSC2 is in complex with TSC1 (hamartin) (By similarity). Interacts with FBXO45 (PubMed:19398581). Interacts with RAE1 (By similarity). Interacts with CPNE1 (via VWFA domain) and CPNE4 (via VWFA domain) (PubMed:12522145). Interacts with (sumoylated) RANGAP1; interaction with sumoylated RANGAP1 inhibits E3 ubiquitin-protein ligase activity and promotes MYCBP2 translocation to the nucleus (PubMed:26304119). Interacts with RAN (PubMed:26304119). {ECO:0000250|UniProtKB:O75592, ECO:0000269|PubMed:12522145, ECO:0000269|PubMed:19398581, ECO:0000269|PubMed:26304119}. DOMAIN: The PHR domains are compact beta-sandwich folds composed of 11 antiparallel strands and decorated with conserved apical loops. They are likely to play a structural role and mediate interactions with substrates or partners. {ECO:0000269|PubMed:20156452}.; DOMAIN: The tandem cysteine domain region confers threonine specificity and contains the two essential catalytic cysteine residues that relay ubiquitin. It binds four zinc ions in a C5HC7HC2 configuration. {ECO:0000250|UniProtKB:O75592}. TISSUE SPECIFICITY: Expression is mostly restricted to the nervous system, including expression in motor and sensory axons (PubMed:18031680). During postnatal development, expression is particularly strong in the cerebellum, hippocampus and retina (PubMed:14729956). Lower levels of expression are observed throughout the cerebral cortex (PubMed:14729956). {ECO:0000269|PubMed:14729956, ECO:0000269|PubMed:18031680}. +O08638 MYH11_MOUSE Myosin-11 (Myosin heavy chain 11) (Myosin heavy chain, smooth muscle isoform) (SMMHC) 1972 227,028 Alternative sequence (1); Chain (1); Coiled coil (1); Domain (3); Modified residue (10); Nucleotide binding (1); Region (3); Sequence conflict (3) FUNCTION: Muscle contraction. SUBCELLULAR LOCATION: Melanosome {ECO:0000250}. Cytoplasm, myofibril. Note=Thick filaments of the myofibrils. SUBUNIT: Muscle myosin is a hexameric protein that consists of 2 heavy chain subunits (MHC), 2 alkali light chain subunits (MLC) and 2 regulatory light chain subunits (MLC-2). DOMAIN: The rodlike tail sequence is highly repetitive, showing cycles of a 28-residue repeat pattern composed of 4 heptapeptides, characteristic for alpha-helical coiled coils.; DOMAIN: Limited proteolysis of myosin heavy chain produces 1 light meromyosin (LMM) and 1 heavy meromyosin (HMM). HMM can be further cleaved into 2 globular subfragments (S1) and 1 rod-shaped subfragment (S2). {ECO:0000305}. +Q9EQS3 MYCBP_MOUSE c-Myc-binding protein (Associate of Myc 1) (AMY-1) 103 11,970 Chain (1); Sequence conflict (2) FUNCTION: May control the transcriptional activity of MYC. Stimulates the activation of E box-dependent transcription by MYC (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Translocates into the nucleus in the S phase of the cell cycle. {ECO:0000250}. SUBUNIT: Binds via its C-terminal region to the N-terminal region of MYC. Associates with AKAP1/S-AKAP84. Interacts with MYCBPAP (By similarity). {ECO:0000250}. +Q6P8Z1 MYCB_MOUSE Protein B-Myc 170 18,526 Chain (1); Frameshift (1); Modified residue (2); Mutagenesis (2) FUNCTION: Seems to act as an inhibitor of cellular proliferation. {ECO:0000269|PubMed:11039906}. PTM: Rapidly degraded via the ubiquitin-proteasome pathway. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11039906}. TISSUE SPECIFICITY: Highly expressed in epididymis. Also expressed in hypothalamus, pituitary, uterus and ovary. Low expression in testis. Not detected in heart. {ECO:0000269|PubMed:11039906}. +Q9CPT4 MYDGF_MOUSE Myeloid-derived growth factor (MYDGF) 166 17,982 Chain (1); Erroneous initiation (1); Signal peptide (1) FUNCTION: Bone marrow-derived monocyte and paracrine-acting protein that promotes cardiac myocyte survival and adaptive angiogenesis for cardiac protection and/or repair after myocardial infarction (MI). Stimulates endothelial cell proliferation through a MAPK1/3-, STAT3- and CCND1-mediated signaling pathway. Inhibits cardiac myocyte apoptosis in a PI3K/AKT-dependent signaling pathway. {ECO:0000269|PubMed:25581518}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15378209, ECO:0000269|PubMed:25581518}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250|UniProtKB:Q969H8}. Note=Secreted into blood plasma. {ECO:0000269|PubMed:25581518}. TISSUE SPECIFICITY: Expressed in prostate, spleen and lung, and weakly expressed in the left ventricle (LF) and liver. Expressed predominantly in inflammatory cells, such as monocytes and macrophages, and weakly expressed in neutrophils, T-cells, B-cells, endothelial cells and cardiac myocytes, after myocardial infarction (MI) (at protein level). {ECO:0000269|PubMed:25581518}. +F8VQB6 MYO10_MOUSE Unconventional myosin-X (Unconventional myosin-10) 2062 237,323 Alternative sequence (1); Chain (1); Domain (8); Modified residue (5); Nucleotide binding (1); Region (3); Sequence conflict (16) FUNCTION: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. MYO10 binds to actin filaments and actin bundles and functions as plus end-directed motor. The tail domain binds to membranous compartments containing phosphatidylinositol 3,4,5-trisphosphate or integrins, and mediates cargo transport along actin filaments (By similarity). Regulates cell shape, cell spreading and cell adhesion. Stimulates the formation and elongation of filopodia. May play a role in neurite outgrowth and axon guidance. In hippocampal neurons it induces the formation of dendritic filopodia by trafficking the actin-remodeling protein VASP to the tips of filopodia, where it promotes actin elongation. Plays a role in formation of the podosome belt in osteoclasts. {ECO:0000250, ECO:0000269|PubMed:17237772, ECO:0000269|PubMed:20081229}.; FUNCTION: Isoform Headless: Functions as a dominant-negative regulator of isoform 1, suppressing its filopodia-inducing and axon outgrowth-promoting activities. In hippocampal neurons, it increases VASP retention in spine heads to induce spine formation and spine head expansion. PTM: The initiator methionine for isoform Headless is removed. SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell projection, lamellipodium {ECO:0000250}. Cell projection, ruffle {ECO:0000250}. Cytoplasm, cytoskeleton. Cell projection, filopodium tip. Cytoplasm, cell cortex. Cell projection, filopodium membrane; Peripheral membrane protein. Note=May be in an inactive, monomeric conformation in the cytosol. Detected in cytoplasmic punctae and in cell projections. Colocalizes with actin fibers. Interacts with microtubules. Undergoes forward and rearward movements within filopodia. Interaction with membranes containing phosphatidylinositol 3,4,5-trisphosphate mediates localization at filopodium membranes (By similarity). {ECO:0000250}. SUBUNIT: Monomer, when in an inactive confomation in the cytosol. Homodimer in its active, membrane-bound conformation; antiparallel coiled coil-mediated dimer formation. Interacts with ECPAS. Interacts with DCC and ITGB5; the presence of DCC inhibits ITGB5 binding. Interacts with tubulin; ITGB5 or DCC binding inhibits tubulin binding. Interacts strongly with CALM3 and weakly with CALM, the CALM3 interaction is essential for function in filopodial extension and motility. Interacts with ITGB1, ITGB3 and ITGB5 (By similarity). Interacts with NEO1. Interacts with VASP. {ECO:0000250, ECO:0000269|PubMed:17237772, ECO:0000269|PubMed:20081229}. DOMAIN: Interaction between the motor domain and the tail leads to an inactive, monomeric conformation. Phospholipid binding via the PH domains leads to the formation of the active, dimeric form of the protein and strongly increases actin-dependent ATPase activity and motor activity (By similarity). {ECO:0000250}.; DOMAIN: Interacts with membranes containing phosphatidylinositol-3,4,5-trisphosphate via the PH domains. {ECO:0000250}.; DOMAIN: IQ 3 domain mediates high-affinity calcium-dependent binding to CALM3/CLP. {ECO:0000250}.; DOMAIN: The SAH (single alpha-helix) region is characterized by a high content of charged residues which are predicted to stabilize the alpha-helical structure by ionic bonds. It can refold after extension suggesting an in vivo force-dependent function. The isolated SAH domain is monomeric; however, in its distal part seems to form a semirigid helical structure which overlaps with a region shown to mediate antiparallel coiled coil-mediated dimerization. {ECO:0000305, ECO:0000305|PubMed:16030012}. TISSUE SPECIFICITY: Detected in brain, heart, kidney, liver, stomach, skeletal muscle, lung, testis and skin. Isoform Headless is expressed in embryonic and neuronal stem cells, and enriched in proliferating and migrating cells. {ECO:0000269|PubMed:10799329, ECO:0000269|PubMed:22661706}. +P97500 MYT1L_MOUSE Myelin transcription factor 1-like protein (MyT1-L) (MyT1L) (Neural zinc finger factor 1) (NZF-1) (Postmitotic neural gene 1 protein) (Zinc finger protein Png-1) 1187 132,945 Alternative sequence (6); Chain (1); Coiled coil (1); Compositional bias (2); Erroneous initiation (1); Frameshift (1); Modified residue (1); Sequence conflict (18); Zinc finger (6) FUNCTION: Transcription factor that plays a key role in neuronal differentiation by specifically repressing expression of non-neuronal genes during neuron differentiation (PubMed:28379941). In contrast to other transcription repressors that inhibit specific lineages, mediates repression of multiple differentiation programs (PubMed:28379941). Also represses expression of negative regulators of neurogenesis, such as members of the Notch signaling pathway, including HES1 (PubMed:28379941). The combination of three transcription factors, ASCL1, POU3F2/BRN2 and MYT1L, is sufficient to reprogram fibroblasts and other somatic cells into induced neuronal (iN) cells in vitro (PubMed:20107439, PubMed:24243019, PubMed:27281220). Directly binds the 5'-AAGTT-3' core motif present on the promoter of target genes and represses transcription by recruiting a multiprotein complex containing SIN3B (PubMed:28379941). The 5'-AAGTT-3' core motif is absent from the promoter of neural genes (PubMed:28379941). {ECO:0000269|PubMed:20107439, ECO:0000269|PubMed:24243019, ECO:0000269|PubMed:27281220, ECO:0000269|PubMed:28379941, ECO:0000269|PubMed:9130664, ECO:0000269|PubMed:9373037}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24243019, ECO:0000269|PubMed:28379941, ECO:0000269|PubMed:9373037}. Chromosome {ECO:0000269|PubMed:28379941}. Note=Preferentially binds to DNA binding sites that are in an open chromatin configuration (PubMed:28379941). {ECO:0000269|PubMed:28379941}. SUBUNIT: Interacts with SIN3B. {ECO:0000269|PubMed:28379941}. TISSUE SPECIFICITY: Brain. {ECO:0000269|PubMed:9130664}. +Q9QY06 MYO9B_MOUSE Unconventional myosin-IXb (Unconventional myosin-9b) 2114 238,834 Alternative sequence (3); Chain (1); Coiled coil (3); Domain (7); Initiator methionine (1); Modified residue (28); Natural variant (2); Nucleotide binding (1); Region (4); Zinc finger (1) FUNCTION: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Binds actin with high affinity both in the absence and presence of ATP and its mechanochemical activity is inhibited by calcium ions. Also acts as a GTPase activator for RHOA. Plays a role in the regulation of cell migration via its role as RHOA GTPase activator. This is regulated by its interaction with the SLIT2 receptor ROBO1; interaction with ROBO1 impairs interaction with RHOA and subsequent activation of RHOA GTPase activity, and thereby leads to increased levels of active, GTP-bound RHOA. {ECO:0000250|UniProtKB:Q13459}. SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q13459}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q13459}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q13459}. Note=In undifferentiated cells colocalizes with F-actin in the cell periphery while in differentiated cells its localization is cytoplasmic with the highest levels in the perinuclear region. {ECO:0000250|UniProtKB:Q13459}. SUBUNIT: Interacts (via IQ domains) with CALM. Interacts with RHOA. Interacts (via Rho-GAP domain) with ROBO1; this inhibits the interaction with RHOA and the stimulation of RHOA GTPase activity, and thereby increases the levels of active RHOA. {ECO:0000250|UniProtKB:Q13459}. TISSUE SPECIFICITY: Expressed in the brain, heart, muscle and inner ear. {ECO:0000269|PubMed:10580159}. +Q8BWZ3 NAA25_MOUSE N-alpha-acetyltransferase 25, NatB auxiliary subunit (Mitochondrial distribution and morphology protein 20) (N-terminal acetyltransferase B complex subunit MDM20) (NatB complex subunit MDM20) (N-terminal acetyltransferase B complex subunit NAA25) 972 111,708 Alternative sequence (1); Chain (1); Compositional bias (1); Repeat (4); Sequence conflict (2) FUNCTION: Non-catalytic subunit of the NatB complex which catalyzes acetylation of the N-terminal methionine residues of peptides beginning with Met-Asp-Glu. May play a role in normal cell-cycle progression. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Component of the N-terminal acetyltransferase B (NatB) complex which is composed of NAA20 and NAA25. {ECO:0000250}. +Q9DBU2 NAA60_MOUSE N-alpha-acetyltransferase 60 (EC 2.3.1.259) (Histone acetyltransferase type B protein 4) (HAT4) (EC 2.3.1.48) (N-acetyltransferase 15) (N-alpha-acetyltransferase F) (NatF) 242 27,507 Active site (2); Binding site (4); Chain (1); Domain (1); Intramembrane (1); Modified residue (4); Region (4); Topological domain (2) INTRAMEM 193 236 Helical. {ECO:0000250|UniProtKB:Q9H7X0}. TOPO_DOM 1 192 Cytoplasmic. {ECO:0000250|UniProtKB:Q9H7X0}.; TOPO_DOM 237 242 Cytoplasmic. {ECO:0000250|UniProtKB:Q9H7X0}. FUNCTION: N-alpha-acetyltransferase that specifically mediates the acetylation of N-terminal residues of the transmembrane proteins, with a strong preference for N-termini facing the cytosol. Displays N-terminal acetyltransferase activity towards a range of N-terminal sequences including those starting with Met-Lys, Met-Val, Met-Ala and Met-Met. Required for normal chromosomal segregation during anaphase. May also show histone acetyltransferase activity; such results are however unclear in vivo and would require additional experimental evidences. {ECO:0000250|UniProtKB:Q9H7X0}. PTM: Acetylated: autoacetylation is required for optimal acetyltransferase activity. {ECO:0000250|UniProtKB:Q9H7X0}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9H7X0}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9H7X0}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9H7X0}. Note=Probably forms a intramembrane hairpin-like structure in the membrane. {ECO:0000250|UniProtKB:Q9H7X0}. SUBUNIT: Monomer and homodimer; monomer in presence of substrate and homodimer in its absence. {ECO:0000250|UniProtKB:Q9H7X0}. +Q9QWR8 NAGAB_MOUSE Alpha-N-acetylgalactosaminidase (EC 3.2.1.49) (Alpha-galactosidase B) 415 47,235 Active site (2); Binding site (4); Chain (1); Disulfide bond (4); Erroneous initiation (1); Glycosylation (3); Modified residue (2); Region (1); Sequence conflict (2); Signal peptide (1) FUNCTION: Removes terminal alpha-N-acetylgalactosamine residues from glycolipids and glycopeptides. Required for the breakdown of glycolipids (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Lysosome {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +Q9CYQ7 NARF_MOUSE Nuclear prelamin A recognition factor (Iron-only hydrogenase-like protein 2) (IOP2) 462 51,816 Chain (1); Modified residue (1); Sequence conflict (1) SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with LMNA and binds to the farnesylated C-terminal domain. {ECO:0000250}. +P13595 NCAM1_MOUSE Neural cell adhesion molecule 1 (N-CAM-1) (NCAM-1) (CD antigen CD56) 1115 119,427 Alternative sequence (5); Beta strand (19); Chain (1); Disulfide bond (5); Domain (7); Glycosylation (6); Helix (1); Lipidation (1); Modified residue (11); Region (2); Sequence conflict (22); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (3) TRANSMEM 712 729 Helical. {ECO:0000255}. TOPO_DOM 20 711 Extracellular. {ECO:0000255}.; TOPO_DOM 730 1115 Cytoplasmic. {ECO:0000255}. FUNCTION: This protein is a cell adhesion molecule involved in neuron-neuron adhesion, neurite fasciculation, outgrowth of neurites, etc. SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Isoform 2: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Isoform 3: Cell membrane; Lipid-anchor, GPI-anchor. +Q8K480 MFRP_MOUSE Membrane frizzled-related protein (Membrane-type frizzled-related protein) 584 63,669 Alternative sequence (1); Chain (1); Compositional bias (1); Disulfide bond (14); Domain (5); Glycosylation (3); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 70 90 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 69 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 91 584 Extracellular. {ECO:0000255}. FUNCTION: May play a role in eye development. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:17122143}; Single-pass type II membrane protein {ECO:0000269|PubMed:17122143}. SUBUNIT: Interacts with C1QTNF5. {ECO:0000269|PubMed:17122143}. TISSUE SPECIFICITY: Expressed in retinal pigment epithelium and ciliary epithelium of the eye. {ECO:0000269|PubMed:12140190, ECO:0000269|PubMed:17122143}. DISEASE: Note=Defects in Mfrp are the cause of retinal degeneration 6 (RD6). RD6 is an autosomal recessive degeneration of the photoreceptors causing dysfunction of both rods and cones. {ECO:0000269|PubMed:12140190}. +Q8CBH5 MFSD6_MOUSE Major facilitator superfamily domain-containing protein 6 (Macrophage MHC class I receptor 2) 775 86,076 Alternative sequence (1); Chain (1); Compositional bias (1); Erroneous initiation (3); Frameshift (1); Modified residue (1); Transmembrane (12) TRANSMEM 74 94 Helical. {ECO:0000255}.; TRANSMEM 106 126 Helical. {ECO:0000255}.; TRANSMEM 133 153 Helical. {ECO:0000255}.; TRANSMEM 289 309 Helical. {ECO:0000255}.; TRANSMEM 338 358 Helical. {ECO:0000255}.; TRANSMEM 372 392 Helical. {ECO:0000255}.; TRANSMEM 453 473 Helical. {ECO:0000255}.; TRANSMEM 482 502 Helical. {ECO:0000255}.; TRANSMEM 510 530 Helical. {ECO:0000255}.; TRANSMEM 547 567 Helical. {ECO:0000255}.; TRANSMEM 582 602 Helical. {ECO:0000255}.; TRANSMEM 608 628 Helical. {ECO:0000255}. FUNCTION: MHC class I receptor. Binds only to H-2 class I histocompatibility antigen, K-D alpha chain (H-2K(D)). {ECO:0000269|PubMed:17010536}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q10470 MGAT3_MOUSE Beta-1,4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase (EC 2.4.1.144) (N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase III) (GNT-III) (GlcNAc-T III) (N-acetylglucosaminyltransferase III) 538 62,003 Chain (1); Compositional bias (1); Erroneous initiation (1); Glycosylation (3); Natural variant (7); Topological domain (2); Transmembrane (1) TRANSMEM 8 23 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 7 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 24 538 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: It is involved in the regulation of the biosynthesis and biological function of glycoprotein oligosaccharides. Catalyzes the addition of N-acetylglucosamine in beta 1-4 linkage to the beta-linked mannose of the trimannosyl core of N-linked sugar chains, called bisecting N-acetylglucosamine (GlcNAc). It is one of the most important enzymes involved in the regulation of the biosynthesis of glycoprotein oligosaccharides (PubMed:25592972, PubMed:11986323). The addition of this bisecting GlcNAc residue alters not only the composition, but also the conformation of the N-glycan. The introduction of the bisecting GlcNAc residue results in the suppression of further processing and elongation of N-glycans, precluding the formation of beta-1,6 GlcNAc branching, catalyzed by MGAT5 since it is unable to use the bisected oligosaccharide as a substrate (By similarity). Addition of bisecting N-acetylglucosamine to CDH1/E-cadherin modulates CDH1 cell membrane location. Inhibits NeuAc-alpha-2,3-Gal-beta-1,4-GlcNAc- formation which modulates sialylation levels and plays a role in cell migration regulation (By similarity). In brain, addition of bisecting N-acetylglucosamine to BACE1 blocks its lysosomal targeting in response to oxidative stress and further degradation which increases its location to early endosome and the APP cleavage (PubMed:25592972, PubMed:26467158). {ECO:0000250|UniProtKB:Q09327, ECO:0000269|PubMed:11986323, ECO:0000269|PubMed:25592972, ECO:0000269|PubMed:26467158}. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein. SUBUNIT: Interacts with MGAT4D. {ECO:0000269|PubMed:20805325}. TISSUE SPECIFICITY: Highly expressed in brain and kidney and to a much lesser extent in stomach, heart, intestine, uterus, testis, ovary and lung. Not present in spleen, liver and muscle. In brain, expressed in neurons of hippocampus (PubMed:11986323). {ECO:0000269|PubMed:11986323}. +Q5U419 MFSD3_MOUSE Major facilitator superfamily domain-containing protein 3 412 43,165 Chain (1); Compositional bias (1); Sequence conflict (9); Transmembrane (12) TRANSMEM 10 30 Helical. {ECO:0000255}.; TRANSMEM 40 60 Helical. {ECO:0000255}.; TRANSMEM 68 88 Helical. {ECO:0000255}.; TRANSMEM 99 119 Helical. {ECO:0000255}.; TRANSMEM 152 172 Helical. {ECO:0000255}.; TRANSMEM 173 193 Helical. {ECO:0000255}.; TRANSMEM 204 224 Helical. {ECO:0000255}.; TRANSMEM 252 272 Helical. {ECO:0000255}.; TRANSMEM 291 311 Helical. {ECO:0000255}.; TRANSMEM 320 340 Helical. {ECO:0000255}.; TRANSMEM 361 381 Helical. {ECO:0000255}.; TRANSMEM 384 404 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +P19788 MGP_MOUSE Matrix Gla protein (MGP) 104 12,359 Chain (1); Disulfide bond (1); Domain (1); Modified residue (7); Sequence conflict (2); Signal peptide (1) FUNCTION: Associates with the organic matrix of bone and cartilage. Thought to act as an inhibitor of bone formation. PTM: Requires vitamin K-dependent gamma-carboxylation for its function. SUBCELLULAR LOCATION: Secreted. +Q9CZ57 NSUN4_MOUSE 5-methylcytosine rRNA methyltransferase NSUN4 (EC 2.1.1.-) (NOL1/NOP2/Sun domain family member 4) (Sperm head and tail associated protein) 381 42,853 Active site (1); Alternative sequence (2); Binding site (2); Chain (1); Modified residue (1); Region (1); Transit peptide (1) FUNCTION: Involved in mitochondrial ribosome assembly. 5-methylcytosine rRNA methyltransferase that probably is involved in mitochondrial ribosome small subunit (SSU) maturation by methylation of mitochondrial 12S rRNA at position 911; the function is independent of MTERFD2/MTERF4 and assembled mitochondrial ribosome large subunit (LSU). Targeted to LSU by MTERFD2/MTERF4 and probably is involved in a final step in ribosome biogenesis to ensure that SSU and LSU are assembled. In vitro can methylate 16S rRNA of the LSU; the methylation is enhanced by MTERFD/MTERF4. {ECO:0000269|PubMed:24516400}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:21531335}. SUBUNIT: Heterodimer with MTERFD2/MTERF4; this interaction seems to be required for NSUN4 recruitment to the mitochondrial large ribosomal subunit. {ECO:0000250}. +O08605 MKNK1_MOUSE MAP kinase-interacting serine/threonine-protein kinase 1 (EC 2.7.11.1) (MAP kinase signal-integrating kinase 1) (MAPK signal-integrating kinase 1) (Mnk1) 427 47,915 Active site (1); Binding site (1); Chain (1); Domain (1); Erroneous initiation (1); Modified residue (7); Mutagenesis (2); Nucleotide binding (1) FUNCTION: May play a role in the response to environmental stress and cytokines. Appears to regulate translation by phosphorylating EIF4E, thus increasing the affinity of this protein for the 7-methylguanosine-containing mRNA cap. {ECO:0000269|PubMed:9155017}. PTM: Dual phosphorylation of Thr-209 and Thr-214 activates the kinase. Phosphorylation of Thr-344 activates the kinase. MAPK3/ERK1 is one of the kinases which activate MKNK1/MNK1. Phosphorylation by PAK2 leads to a reduced phosphorylation of EIF4G1 (By similarity). {ECO:0000250}. SUBUNIT: Interacts with the C-terminal regions of EIF4G1 and EIF4G2. Also binds to dephosphorylated ERK1 and ERK2, and to the p38 kinases. {ECO:0000269|PubMed:9155017}. TISSUE SPECIFICITY: Ubiquitously expressed in all tissues examined, with high levels in skeletal muscle. {ECO:0000269|PubMed:9155017}. +P03911 NU4M_MOUSE NADH-ubiquinone oxidoreductase chain 4 (EC 7.1.1.2) (NADH dehydrogenase subunit 4) 459 51,882 Beta strand (7); Chain (1); Helix (24); Transmembrane (13); Turn (5) TRANSMEM 23 43 Helical. {ECO:0000255}.; TRANSMEM 60 80 Helical. {ECO:0000255}.; TRANSMEM 90 110 Helical. {ECO:0000255}.; TRANSMEM 113 133 Helical. {ECO:0000255}.; TRANSMEM 147 167 Helical. {ECO:0000255}.; TRANSMEM 194 214 Helical. {ECO:0000255}.; TRANSMEM 224 244 Helical. {ECO:0000255}.; TRANSMEM 257 277 Helical. {ECO:0000255}.; TRANSMEM 284 303 Helical. {ECO:0000255}.; TRANSMEM 308 330 Helical. {ECO:0000255}.; TRANSMEM 350 370 Helical. {ECO:0000255}.; TRANSMEM 392 412 Helical. {ECO:0000255}.; TRANSMEM 434 454 Helical. {ECO:0000255}. FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q8VI95 OAS1D_MOUSE Inactive 2'-5'-oligoadenylate synthase 1D 361 42,831 Chain (1); Sequence conflict (2) FUNCTION: Does not have 2'-5'-olygoadenylate synthetase activity, but can bind double-stranded RNA (PubMed:15899864, PubMed:12396720). May play a role in the control of female fertility, possibly by binding to and inhibiting OAS1A (PubMed:15899864). {ECO:0000269|PubMed:12396720, ECO:0000269|PubMed:15899864}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15899864}. SUBUNIT: Interacts with OAS1A, the interaction inhibits OAS1A catalytic activity. {ECO:0000269|PubMed:15899864}. TISSUE SPECIFICITY: Expressed specifically in oocytes (at protein level) (PubMed:15899864). Expressed at highest level in ovary with lesser amounts in intestine, brain, thymus lung, kidney, liver and uterus (PubMed:17567914, PubMed:27663720). {ECO:0000269|PubMed:15899864, ECO:0000269|PubMed:17567914, ECO:0000269|PubMed:27663720}. +Q9Z2F2 OASL2_MOUSE 2'-5'-oligoadenylate synthase-like protein 2 (EC 2.7.7.84) (54 kDa 2'-5'-oligoadenylate synthase-like protein) (p54 OASL) (M1204) 508 58,767 Binding site (3); Chain (1); Domain (1); Metal binding (3); Sequence conflict (2) FUNCTION: Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response. Synthesizes oligomers of 2'-5'-oligoadenylates (2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L (RNase L) leading to its dimerization and subsequent activation. Activation of RNase L leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication. Can mediate the antiviral effect via the classical RNase L-dependent pathway or an alternative antiviral pathway independent of RNase L. {ECO:0000269|PubMed:12396720, ECO:0000269|PubMed:12799444}. TISSUE SPECIFICITY: Strongly expressed in spleen dendritic cells, whereas, in bone marrow-derived dendritic cells, the amount increases during the maturation process. Expressed in many organs, the highest levels being in thymus, lung, and bone marrow. {ECO:0000269|PubMed:12396720}. +Q91WW4 MRGA2_MOUSE Mas-related G-protein coupled receptor member A2 305 34,427 Chain (1); Erroneous initiation (1); Sequence conflict (3); Topological domain (8); Transmembrane (7) TRANSMEM 18 38 Helical; Name=1. {ECO:0000255}.; TRANSMEM 54 74 Helical; Name=2. {ECO:0000255}.; TRANSMEM 79 99 Helical; Name=3. {ECO:0000255}.; TRANSMEM 133 153 Helical; Name=4. {ECO:0000255}.; TRANSMEM 168 188 Helical; Name=5. {ECO:0000255}.; TRANSMEM 208 228 Helical; Name=6. {ECO:0000255}.; TRANSMEM 245 265 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 17 Extracellular. {ECO:0000255}.; TOPO_DOM 39 53 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 75 78 Extracellular. {ECO:0000255}.; TOPO_DOM 100 132 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 154 167 Extracellular. {ECO:0000255}.; TOPO_DOM 189 207 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 229 244 Extracellular. {ECO:0000255}.; TOPO_DOM 266 305 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan receptor. May be a receptor for RFamide-family neuropeptides such as NPFF and NPAF, which are analgesic in vivo. May regulate nociceptor function and/or development, including the sensation or modulation of pain (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed in a subset of sensory neurons that includes nociceptors. Expressed in the subclass of non-peptidergic sensory neurons that are IB4(+) and VR1(-). {ECO:0000269|PubMed:11551509}. +Q91ZC0 MRGB4_MOUSE Mas-related G-protein coupled receptor member B4 321 36,338 Chain (1); Glycosylation (3); Topological domain (8); Transmembrane (7) TRANSMEM 34 54 Helical; Name=1. {ECO:0000255}.; TRANSMEM 63 83 Helical; Name=2. {ECO:0000255}.; TRANSMEM 98 118 Helical; Name=3. {ECO:0000255}.; TRANSMEM 147 167 Helical; Name=4. {ECO:0000255}.; TRANSMEM 173 193 Helical; Name=5. {ECO:0000255}.; TRANSMEM 216 236 Helical; Name=6. {ECO:0000255}.; TRANSMEM 258 278 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 33 Extracellular. {ECO:0000255}.; TOPO_DOM 55 62 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 84 97 Extracellular. {ECO:0000255}.; TOPO_DOM 119 146 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 168 172 Extracellular. {ECO:0000255}.; TOPO_DOM 194 215 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 237 257 Extracellular. {ECO:0000255}.; TOPO_DOM 279 321 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan receptor. Probably involved in the function of nociceptive neurons. May regulate nociceptor function and/or development, including the sensation or modulation of pain (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q3UU96 MRCKA_MOUSE Serine/threonine-protein kinase MRCK alpha (EC 2.7.11.1) (CDC42-binding protein kinase alpha) 1719 195,536 Active site (1); Alternative sequence (2); Binding site (1); Chain (1); Coiled coil (3); Compositional bias (1); Domain (5); Modified residue (13); Nucleotide binding (1); Sequence conflict (3); Zinc finger (1) FUNCTION: Serine/threonine-protein kinase which is an important downstream effector of CDC42 and plays a role in the regulation of cytoskeleton reorganization and cell migration. Regulates actin cytoskeletal reorganization via phosphorylation of PPP1R12C and MYL9/MLC2. In concert with MYO18A and LRP35A, is involved in modulating lamellar actomyosin retrograde flow that is crucial to cell protrusion and migration. Phosphorylates: PPP1R12A and LIMK2. May play a role in TFRC-mediated iron uptake (By similarity). In concert with FAM89B/LRAP25 mediates the targeting of LIMK1 to the lamellipodium resulting in its activation and subsequent phosphorylation of CFL1 which is important for lamellipodial F-actin regulation (PubMed:25107909). {ECO:0000250|UniProtKB:Q5VT25, ECO:0000269|PubMed:25107909}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell projection, lamellipodium {ECO:0000269|PubMed:25107909}. Note=Displays a dispersed punctate distribution and concentrates along the cell periphery, especially at the leading edge and cell-cell junction. This concentration is PH-domain dependent (By similarity). Localizes in the lamellipodium in a FAM89B/LRAP25-dependent manner (PubMed:25107909). {ECO:0000250|UniProtKB:O54874, ECO:0000269|PubMed:25107909}. SUBUNIT: Homodimer and homotetramer via the coiled coil regions. Interacts tightly with GTP-bound but not GDP-bound CDC42. Forms a tripartite complex with MYO18A and LRP35A with the latter acting as an adapter connecting CDC42BPA and MYO18A. LRP35A binding results in activation of CDC42BPA by abolition of its negative autoregulation. Interacts with LURAP1 (By similarity). Interacts (via AGC-kinase C-terminal domain) with FAM89B/LRAP25 (via LRR repeat). Forms a tripartite complex with FAM89B/LRAP25 and LIMK1 (PubMed:25107909). {ECO:0000250|UniProtKB:O54874, ECO:0000269|PubMed:25107909}. +Q5ND52 MRM3_MOUSE rRNA methyltransferase 3, mitochondrial (EC 2.1.1.-) (16S rRNA (guanosine(1370)-2'-O)-methyltransferase) (16S rRNA [Gm1370] 2'-O-methyltransferase) (RNA methyltransferase-like protein 1) 418 46,796 Binding site (3); Chain (1); Erroneous initiation (4); Frameshift (1); Sequence conflict (7); Transit peptide (1) FUNCTION: S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of 2'-O-methylguanosine at position 1370 (Gm1370) in the 16S mitochondrial large subunit ribosomal RNA (mtLSU rRNA), a conserved modification in the peptidyl transferase domain of the mtLSU rRNA. {ECO:0000250|UniProtKB:Q9HC36}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:24036117}. +Q91ZB8 MRGRD_MOUSE Mas-related G-protein coupled receptor member D (Beta-alanine receptor) (G-protein coupled receptor TGR7) 321 36,126 Chain (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 9 29 Helical; Name=1. {ECO:0000255}.; TRANSMEM 31 51 Helical; Name=2. {ECO:0000255}.; TRANSMEM 73 93 Helical; Name=3. {ECO:0000255}.; TRANSMEM 147 167 Helical; Name=4. {ECO:0000255}.; TRANSMEM 182 202 Helical; Name=5. {ECO:0000255}.; TRANSMEM 221 241 Helical; Name=6. {ECO:0000255}.; TRANSMEM 261 281 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 8 Extracellular. {ECO:0000255}.; TOPO_DOM 30 30 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 52 72 Extracellular. {ECO:0000255}.; TOPO_DOM 94 146 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 168 181 Extracellular. {ECO:0000255}.; TOPO_DOM 203 220 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 242 260 Extracellular. {ECO:0000255}.; TOPO_DOM 282 321 Cytoplasmic. {ECO:0000255}. FUNCTION: May regulate nociceptor function and/or development, including the sensation or modulation of pain. Functions as a specific membrane receptor for beta-alanine. The receptor couples with G-protein G(q) and G(i) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed in a subset of sensory neurons that includes nociceptors. Expressed in the subclass of non-peptidergic sensory neurons that are IB4(+) and VR1(-). {ECO:0000269|PubMed:11551509}. +Q99J25 MRM1_MOUSE rRNA methyltransferase 1, mitochondrial (EC 2.1.1.-) (16S rRNA (guanosine(1145)-2'-O)-methyltransferase) (16S rRNA [Gm1145] 2'-O-methyltransferase) 320 34,843 Chain (1); Frameshift (1); Transit peptide (1) FUNCTION: S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of 2'-O-methylguanosine at position 1145 (Gm1145) in the 16S mitochondrial large subunit ribosomal RNA (mtLSU rRNA), a universally conserved modification in the peptidyl transferase domain of the mtLSU rRNA. {ECO:0000250|UniProtKB:Q6IN84}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:24036117}. +D3Z750 MRO2A_MOUSE Maestro heat-like repeat-containing protein family member 2A (HEAT repeat-containing protein 7B1) 1679 190,012 Chain (1); Repeat (15) +Q9R1X5 MRP5_MOUSE Multidrug resistance-associated protein 5 (ATP-binding cassette sub-family C member 5) (Multi-specific organic anion transporter C) (MOAT-C) (SMRP) 1436 161,125 Chain (1); Domain (4); Glycosylation (8); Modified residue (7); Nucleotide binding (2); Sequence conflict (10); Transmembrane (13) TRANSMEM 179 199 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 219 239 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 296 316 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 317 337 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 400 420 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 426 446 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 608 628 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 847 867 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 916 936 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 996 1016 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 1017 1037 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 1101 1121 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 1126 1146 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}. FUNCTION: Acts as a multispecific organic anion pump which can transport nucleotide analogs. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. +Q9R1S7 MRP6_MOUSE Multidrug resistance-associated protein 6 (ATP-binding cassette sub-family C member 6) 1498 164,857 Chain (1); Domain (4); Glycosylation (2); Modified residue (1); Nucleotide binding (2); Sequence conflict (33); Topological domain (18); Transmembrane (17) TRANSMEM 38 58 Helical; Name=1. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 79 99 Helical; Name=2. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 105 125 Helical; Name=3. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 138 155 Helical; Name=4. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 174 194 Helical; Name=5. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 301 321 Helical; Name=6. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 348 368 Helical; Name=7. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 425 445 Helical; Name=8. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 449 469 Helical; Name=9. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 532 552 Helical; Name=10. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 575 595 Helical; Name=11. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 935 955 Helical; Name=12. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 993 1013 Helical; Name=13. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 1057 1077 Helical; Name=14. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 1079 1099 Helical; Name=15. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 1171 1191 Helical; Name=16. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 1194 1214 Helical; Name=17. {ECO:0000255|PROSITE-ProRule:PRU00441}. TOPO_DOM 1 37 Extracellular. {ECO:0000250}.; TOPO_DOM 59 78 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 100 104 Extracellular. {ECO:0000250}.; TOPO_DOM 126 137 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 156 173 Extracellular. {ECO:0000250}.; TOPO_DOM 195 300 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 322 347 Extracellular. {ECO:0000250}.; TOPO_DOM 369 424 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 446 448 Extracellular. {ECO:0000250}.; TOPO_DOM 470 531 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 553 574 Extracellular. {ECO:0000250}.; TOPO_DOM 596 934 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 956 992 Extracellular. {ECO:0000250}.; TOPO_DOM 1014 1056 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 1078 1078 Extracellular. {ECO:0000250}.; TOPO_DOM 1100 1170 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 1192 1193 Extracellular. {ECO:0000250}.; TOPO_DOM 1215 1498 Cytoplasmic. {ECO:0000250}. FUNCTION: May participate directly in the active transport of drugs into subcellular organelles or influence drug distribution indirectly. {ECO:0000250}. SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000269|PubMed:23625951}; Multi-pass membrane protein {ECO:0000255, ECO:0000269|PubMed:23625951}. +Q9D0I8 MRT4_MOUSE mRNA turnover protein 4 homolog (Ribosome assembly factor Mrto4) 239 27,546 Chain (1); Modified residue (3); Sequence conflict (1) FUNCTION: Component of the ribosome assembly machinery. Nuclear paralog of the ribosomal protein P0, it binds pre-60S subunits at an early stage of assembly in the nucleolus, and is replaced by P0 in cytoplasmic pre-60S subunits and mature 80S ribosomes. {ECO:0000250|UniProtKB:P33201}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:P33201}. Cytoplasm {ECO:0000250|UniProtKB:P33201}. Note=Shuttles between the nucleus and the cytoplasm. {ECO:0000250|UniProtKB:P33201}. SUBUNIT: Associates with the pre-60S ribosomal particle. {ECO:0000250|UniProtKB:P33201}. +Q8K4J6 MRTFA_MOUSE Myocardin-related transcription factor A (MRTF-A) (Basic SAP coiled-coil transcription activator) (MKL/myocardin-like protein 1) (Megakaryoblastic leukemia 1 protein homolog) (Megakaryocytic acute leukemia protein homolog) 964 102,546 Alternative sequence (1); Beta strand (1); Chain (1); Coiled coil (1); Compositional bias (2); Domain (1); Helix (6); Modified residue (36); Mutagenesis (14); Region (3); Repeat (3); Sequence conflict (3) FUNCTION: Transcription coactivator that associates with the serum response factor (SRF) transcription factor to control expression of genes regulating the cytoskeleton during development, morphogenesis and cell migration (PubMed:12019265, PubMed:12732141, PubMed:17588931, PubMed:19350017, PubMed:24732378). The SRF-MRTFA complex activity responds to Rho GTPase-induced changes in cellular globular actin (G-actin) concentration, thereby coupling cytoskeletal gene expression to cytoskeletal dynamics (PubMed:24732378). MRTFA binds G-actin via its RPEL repeats, regulating activity of the MRTFA-SRF complex (PubMed:12732141, PubMed:17588931). Activity is also regulated by filamentous actin (F-actin) in the nucleus (PubMed:23558171, PubMed:25759381). {ECO:0000269|PubMed:12019265, ECO:0000269|PubMed:12732141, ECO:0000269|PubMed:17588931, ECO:0000269|PubMed:19350017, ECO:0000269|PubMed:23558171, ECO:0000269|PubMed:24732378, ECO:0000269|PubMed:25759381}. PTM: Phosphorylation at Ser-41 by Erk inhibits binding of globular actin (G-actin), unmasking the nuclear localization signal (NLS) and promoting nuclear import. {ECO:0000269|PubMed:27304076}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12732141, ECO:0000269|PubMed:17588931, ECO:0000269|PubMed:19008859, ECO:0000269|PubMed:21673315, ECO:0000269|PubMed:25759381, ECO:0000269|PubMed:27304076}. Nucleus {ECO:0000269|PubMed:12019265, ECO:0000269|PubMed:12732141, ECO:0000269|PubMed:17588931, ECO:0000269|PubMed:19008859, ECO:0000269|PubMed:21673315, ECO:0000269|PubMed:25759381, ECO:0000269|PubMed:27304076}. Note=Subcellular location is tightly regulated by actin both in cytoplasm and nucleus: high levels of G-actin in the nucleus observed during serum deprivation lead to low levels of nuclear MRTFA, while reduced levels of nuclear G-actin result in accumulation of MRTFA in the nucleus (PubMed:17588931, PubMed:21673315). G-actin-binding in the cytoplasm inhibits nuclear import by masking the nuclear localization signal (NLS) (PubMed:17588931, PubMed:21673315). In contrast, binding to nuclear globular actin (G-actin) promotes nuclear export to the cytoplasm (PubMed:17588931). Nuclear localization is regulated by MICAL2, which mediates depolymerization of nuclear actin, which decreases nuclear G-actin pool, thereby promoting retention of MRTFA in the nucleus and subsequent formation of an active complex with SRF (By similarity). {ECO:0000250|UniProtKB:Q969V6, ECO:0000269|PubMed:17588931, ECO:0000269|PubMed:21673315}. SUBUNIT: Interacts with SRF, forming the SRF-MRTFA nuclear complex which binds the 5'-CArG-3' consensus motif (CArG box) on DNA via SRF (PubMed:12732141, PubMed:19350017). Interacts (via RPEL repeats) with globular actin (G-actin), thereby regulating its subcellular location and activity of the complex formed with SRF (PubMed:12732141, PubMed:17588931, PubMed:19350017, PubMed:19008859, PubMed:27304076, PubMed:21673315). Either forms a trivalent (by binding three G-actin monomers) or pentavalent (by binding five G-actin monomers) complex with G-actin (PubMed:21673315). Forms a nuclear ternary complex with SCAI and SRF, leading to suppress MRTFA-induced SRF transcriptional activity (PubMed:19350017). Interacts with beta-actin (ACTB); interaction with ACTB prevents interaction with SCAI (PubMed:19350017). Interacts with MRTFB (By similarity). {ECO:0000250|UniProtKB:Q969V6, ECO:0000269|PubMed:12732141, ECO:0000269|PubMed:17588931, ECO:0000269|PubMed:19008859, ECO:0000269|PubMed:19350017, ECO:0000269|PubMed:21673315, ECO:0000269|PubMed:27304076}. DOMAIN: The N-terminal region is required for nuclear localization and the C-terminal region mediates transcriptional activity. {ECO:0000269|PubMed:19008859}.; DOMAIN: The RPEL repeats mediate binding to globular actin (G-actin); each RPEL repeat-binding to one G-actin monomer (PubMed:19008859, PubMed:21673315). In addition, each intervening spacer sequence region can bind one G-actin monomer, to reach a pentavalent complex (PubMed:21673315). {ECO:0000269|PubMed:19008859, ECO:0000269|PubMed:21673315}. TISSUE SPECIFICITY: Expressed in heart, brain, spleen, lung, liver, muscle, kidney and testis. {ECO:0000269|PubMed:12019265}. +Q9Z304 MYCS_MOUSE Protein S-Myc 431 47,680 Chain (1); Domain (1); Modified residue (1); Region (1); Sequence conflict (2) FUNCTION: Has apoptosis-inducing activity. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}. SUBUNIT: Efficient DNA binding requires dimerization with another bHLH protein. +Q5DU14 MYO16_MOUSE Unconventional myosin-XVI (Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3) (Unconventional myosin-16) 1919 211,383 Alternative sequence (3); Chain (1); Domain (2); Mutagenesis (2); Nucleotide binding (1); Region (1); Repeat (8); Sequence conflict (3) FUNCTION: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments. May be involved in targeting of the catalytic subunit of protein phosphatase 1 during brain development (By similarity). Activates PI3K and concomitantly recruits the WAVE1 complex to the close vicinity of PI3K and regulates neuronal morphogenesis. {ECO:0000250, ECO:0000269|PubMed:21946561}. PTM: Phosphorylated on tyrosine residues by FYN upon stimulation with CNTN5. Phosphorylation begins at E14, reaches a peak during perinatal days in brain, then gradually decreases. {ECO:0000269|PubMed:21946561}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9ERC1}. Note=Found in puncta in soma and processes of astrocytes and dissociated cerebellar cells with the morphology of migrating granule cells. {ECO:0000250|UniProtKB:Q9ERC1}. SUBUNIT: Binds PPP1CA and/or PPP1CC. Binds F-actin in an ATP-sensitive manner (By similarity). Interacts with ACOT9, ARHGAP26 and PIK3R2. Interacts with components of the WAVE1 complex, CYFIP1 and NCKAP1; this interaction mediates PI3K-WAVE1 association and actin cytoskeleton remodeling (PubMed:21946561). Interacts with KIRREL3 (By similarity). {ECO:0000250|UniProtKB:Q9ERC1, ECO:0000250|UniProtKB:Q9Y6X6, ECO:0000269|PubMed:21946561}. TISSUE SPECIFICITY: Expressed predominantly in brain where it is present in the neurons, but not in astrocytes or oligodendrites. {ECO:0000269|PubMed:21946561}. +Q3UIZ8 MYLK3_MOUSE Myosin light chain kinase 3 (EC 2.7.11.18) (Cardiac-MyBP-C-associated Ca/CaM kinase) (Cardiac-MLCK) 795 86,372 Active site (1); Alternative sequence (2); Binding site (1); Chain (1); Domain (1); Modified residue (3); Nucleotide binding (1) FUNCTION: Kinase that phosphorylates MYL2 in vitro. Has been proposed to be calmodulin-dependent (PubMed:17885681), although MYL2 phosphorylation has also been observed in the presence or absence of calmodulin (PubMed:18202317). Promotes sarcomere formation in cardiomyocytes and increases cardiomyocyte contractility. {ECO:0000269|PubMed:17885681, ECO:0000269|PubMed:18202317}. PTM: Phosphorylated on serine residues. {ECO:0000269|PubMed:18202317}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18202317}. TISSUE SPECIFICITY: Restricted to cardiomyocytes (at protein level). Down-regulated in heart after experimental myocardial infarction at the protein level; no significant changes at the mRNA level. {ECO:0000269|PubMed:18202317}. +P12979 MYOG_MOUSE Myogenin (MYOD1-related protein) 224 25,203 Chain (1); Domain (1); Modified residue (3) FUNCTION: Acts as a transcriptional activator that promotes transcription of muscle-specific target genes and plays a role in muscle differentiation, cell cycle exit and muscle atrophy. Essential for the development of functional embryonic skeletal fiber muscle differentiation. However is dispensable for postnatal skeletal muscle growth; phosphorylation by CAMK2G inhibits its transcriptional activity in respons to muscle activity. Required for the recruitment of the FACT complex to muscle-specific promoter regions, thus promoting gene expression initiation. During terminal myoblast differentiation, plays a role as a strong activator of transcription at loci with an open chromatin structure previously initiated by MYOD1. Together with MYF5 and MYOD1, co-occupies muscle-specific gene promoter core regions during myogenesis. Cooperates also with myocyte-specific enhancer factor MEF2D and BRG1-dependent recruitment of SWI/SNF chromatin-remodeling enzymes to alter chromatin structure at myogenic late gene promoters. Facilitates cell cycle exit during terminal muscle differentiation through the up-regulation of miR-20a expression, which in turn represses genes involved in cell cycle progression. Binds to the E-box containing (E1) promoter region of the miR-20a gene. Plays also a role in preventing reversal of muscle cell differentiation. Contributes to the atrophy-related gene expression in adult denervated muscles. Induces fibroblasts to differentiate into myoblasts. {ECO:0000269|PubMed:15706034, ECO:0000269|PubMed:16407395, ECO:0000269|PubMed:16424906, ECO:0000269|PubMed:16437161, ECO:0000269|PubMed:21465538, ECO:0000269|PubMed:21798092, ECO:0000269|PubMed:22235349, ECO:0000269|PubMed:22847234, ECO:0000269|PubMed:23364797, ECO:0000269|PubMed:8393145, ECO:0000269|PubMed:8393146}. PTM: Phosphorylated by CAMK2G on threonine and serine amino acids in a muscle activity-dependent manner. Phosphorylation of Thr-87 impairs both DNA-binding and trans-activation functions in contracting muscles (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:16424906}. Note=Recruited to late myogenic gene promoter regulatory sequences with SMARCA4/BRG1/BAF190A and SWI/SNF chromatin-remodeling enzymes to promote chromatin-remodeling and transcription initiation in developing embryos. SUBUNIT: Homodimer and heterodimer with E12; heterodimerization enhances MYOG DNA-binding and transcriptional activities. Interacts with SMARCA4/BRG1/BAF190A. Interacts (via C-terminal region) with SSRP1 and SUPT16H; the interaction is indicative of an interaction with the FACT complex. nteracts with CSRP3 (By similarity). {ECO:0000250|UniProtKB:P20428, ECO:0000269|PubMed:12196028, ECO:0000269|PubMed:16424906, ECO:0000269|PubMed:23364797}. TISSUE SPECIFICITY: Expressed in myoblast cells. Expressed weakly in myotubes (at protein level). Expressed strongly in denervated muscles and in satellite cells isolated from denervated muscles. Expressed weakly in innervated muscle and in satellite cells isolated from innervated muscles. {ECO:0000269|PubMed:21465538, ECO:0000269|PubMed:21798092}. +Q8K3H5 MYO3A_MOUSE Myosin-IIIa (EC 2.7.11.1) 1613 184,730 Active site (1); Binding site (1); Chain (1); Domain (4); Nucleotide binding (1); Region (2) FUNCTION: Probable actin-based motor with a protein kinase activity. Probably plays a role in vision and hearing (By similarity). Required for normal cochlear hair bundle development and hearing. Plays an important role in the early steps of cochlear hair bundle morphogenesis. Influences the number and lengths of stereocilia to be produced and limits the growth of microvilli within the forming auditory hair bundles thereby contributing to the architecture of the hair bundle, including its staircase pattern (PubMed:26754646). Involved in the elongation of actin in stereocilia tips by transporting the actin regulatory factor ESPN to the plus ends of actin filaments (PubMed:19287378). {ECO:0000250|UniProtKB:Q8NEV4, ECO:0000269|PubMed:19287378, ECO:0000269|PubMed:26754646}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm {ECO:0000269|PubMed:26754646}. Cell projection, filopodium tip {ECO:0000250|UniProtKB:Q8NEV4}. Cell projection, stereocilium {ECO:0000269|PubMed:26754646}. Note=Increased localization at the filodium tip seen in the presence of MORN4. {ECO:0000250|UniProtKB:Q8NEV4}. SUBUNIT: Interacts with MORN4 (PubMed:26754646). Interacts (via C-terminus) with ESPN and ESPNL (PubMed:26926603). {ECO:0000269|PubMed:26754646, ECO:0000269|PubMed:26926603}. TISSUE SPECIFICITY: Expressed in the cochlear hair cells (at protein level) (PubMed:26754646). Expressed in utricle hair bundles (at protein level) (PubMed:26926603). {ECO:0000269|PubMed:26754646, ECO:0000269|PubMed:26926603}. +E9Q634 MYO1E_MOUSE Unconventional myosin-Ie (Unconventional myosin 1E) 1107 126,818 Beta strand (5); Chain (1); Domain (4); Helix (1); Modified residue (1); Nucleotide binding (1); Region (1); Sequence conflict (1) FUNCTION: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails bind to membranous compartments, which are then moved relative to actin filaments. Binds to membranes containing anionic phospholipids via its tail domain (By similarity). Required for normal morphology of the glomerular basement membrane, normal development of foot processes by kidney podocytes and normal kidney function. In dendritic cells, may control the movement of class II-containing cytoplasmic vesicles along the actin cytoskeleton by connecting them with the actin network via ARL14EP and ARL14 (By similarity). {ECO:0000250, ECO:0000269|PubMed:19005011}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19005011}. Cell junction {ECO:0000269|PubMed:19005011}. Cytoplasmic vesicle {ECO:0000305|PubMed:19005011}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:19005011}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19005011}. Note=In podocytes, it localizes close to and is associated with the cytoplasmic membrane, with enrichment at the lamellipodia tips. Colocalizes with F-actin (By similarity). Detected in cytoplasmic punctae. {ECO:0000250}. SUBUNIT: Interacts with CALM and F-actin. Interacts (via SH3 domain) with SYNJ1, DNM1 and DNM2. Interacts with ARL14EP. Interacts with CARMIL1. {ECO:0000250|UniProtKB:Q12965}. TISSUE SPECIFICITY: Detected in kidney glomeruli (at protein level). Detected in utricle. {ECO:0000269|PubMed:12486594, ECO:0000269|PubMed:19005011}. +Q61122 NAB1_MOUSE NGFI-A-binding protein 1 (EGR-1-binding protein 1) 486 54,010 Chain (1); Cross-link (14); Modified residue (4); Mutagenesis (3); Region (3); Sequence conflict (1) FUNCTION: Acts as a transcriptional repressor for zinc finger transcription factors EGR1 and EGR2. {ECO:0000250, ECO:0000269|PubMed:9774344}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Homomultimers may associate with EGR1 bound to DNA. DOMAIN: The NAB conserved domain 1 (NCD1) interacts with EGR1 inhibitory domain and mediates multimerization.; DOMAIN: The NAB conserved domain 2 (NCD2) is necessary for transcriptional repression. TISSUE SPECIFICITY: Widely expressed in adult. In day 16 embryo highest levels in forebrain, thymus, salivary gland and cartilage. +Q3V2Q8 N42L1_MOUSE NEDD4-binding protein 2-like 1 238 28,038 Alternative sequence (1); Chain (1); Frameshift (1); Sequence conflict (1) +P10085 MYOD1_MOUSE Myoblast determination protein 1 318 34,233 Chain (1); Cross-link (1); Domain (1); Helix (2); Modified residue (1); Sequence conflict (9) FUNCTION: Acts as a transcriptional activator that promotes transcription of muscle-specific target genes and plays a role in muscle differentiation (PubMed:16901893). Together with MYF5 and MYOG, co-occupies muscle-specific gene promoter core region during myogenesis. Induces fibroblasts to differentiate into myoblasts. Interacts with and is inhibited by the twist protein. This interaction probably involves the basic domains of both proteins (PubMed:21798092, PubMed:3175662). {ECO:0000269|PubMed:16901893, ECO:0000269|PubMed:21798092, ECO:0000269|PubMed:3175662}. PTM: Acetylated by a complex containing EP300 and PCAF. The acetylation is essential to activate target genes. Conversely, its deacetylation by SIRT1 inhibits its function. {ECO:0000269|PubMed:9029156}.; PTM: Ubiquitinated on the N-terminus; which is required for proteasomal degradation. {ECO:0000250}.; PTM: Phosphorylated by CDK9. This phosphorylation promotes its function in muscle differentiation (By similarity). {ECO:0000250}.; PTM: Methylation at Lys-104 by EHMT2/G9a inhibits myogenic activity. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16901893}. SUBUNIT: Interacts with SUV39H1 (By similarity). Efficient DNA binding requires dimerization with another bHLH protein. Seems to form active heterodimers with ITF-2. Interacts with DDX5. Interacts with CHD2. Interacts with TSC22D3 isoform 1 and isoform 4. Interacts with SETD3 (PubMed:21832073). Interacts with P-TEFB complex; promotes the transcriptional activity of MYOD1 through its CDK9-mediated phosphorylation (PubMed:12037670). Interacts with CSRP3 (By similarity). {ECO:0000250|UniProtKB:P15172, ECO:0000269|PubMed:12037670, ECO:0000269|PubMed:17011493, ECO:0000269|PubMed:20124407, ECO:0000269|PubMed:21832073, ECO:0000269|PubMed:22569126}. +Q7TSZ8 NACC1_MOUSE Nucleus accumbens-associated protein 1 (NAC-1) (BTB/POZ domain-containing protein 14B) 514 56,537 Chain (1); Cross-link (7); Domain (2); Modified residue (4); Sequence conflict (2) FUNCTION: Functions as a transcriptional repressor. Seems to function as a transcriptional corepressor in neuronal cells through recruitment of HDAC3 and HDAC4. Contributes to tumor progression, and tumor cell proliferation and survival. This may be mediated at least in part through repressing transcriptional activity of GADD45GIP1. Required for recruiting the proteasome from the nucleus to the cytoplasm and dendritic spines. Involved in the acute behavioral and neurological responses to cocaine and amphetamines. {ECO:0000269|PubMed:17130457, ECO:0000269|PubMed:17945361}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Distribution in the cytoplasm is dependent on phosphorylation. {ECO:0000250}. SUBUNIT: Homooligomer; mediated by the BTB domain. Interacts with HDAC3 and HDAC4. Interacts (via BTB domain) with CUL3, PSMD7 AND RCOR1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed with higher expression in the brain, kidney and liver, and at lower levels in heart, lung and testes. {ECO:0000269|PubMed:14521994}. +Q60817 NACA_MOUSE Nascent polypeptide-associated complex subunit alpha (Alpha-NAC) (Alpha-NAC/1.9.2) 215 23,384 Chain (1); Cross-link (1); Domain (2); Modified residue (9); Region (2); Sequence conflict (1) FUNCTION: Prevents inappropriate targeting of non-secretory polypeptides to the endoplasmic reticulum (ER). Binds to nascent polypeptide chains as they emerge from the ribosome and blocks their interaction with the signal recognition particle (SRP), which normally targets nascent secretory peptides to the ER. Also reduces the inherent affinity of ribosomes for protein translocation sites in the ER membrane (M sites) (By similarity). Isoform 1 and isoform 2 appear to bind DNA and play roles in transcription. Isoform 1 may function as a specific coactivator for JUN, acting to stabilize the interaction of JUN homodimers with promoter elements. {ECO:0000250, ECO:0000269|PubMed:15299025, ECO:0000269|PubMed:15831452, ECO:0000269|PubMed:8698236, ECO:0000269|PubMed:9488445, ECO:0000269|PubMed:9488446}. PTM: Phosphorylation of Ser-43 by ILK during cell adhesion may promote nuclear localization. Phosphorylation of Thr-159 by GSK3B may promote proteasome mediated degradation. {ECO:0000269|PubMed:15005626, ECO:0000269|PubMed:15299025}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=The heterodimer is located mainly in the cytosol, and the homodimer in the nucleus. {ECO:0000250}. SUBUNIT: Part of the nascent polypeptide-associated complex (NAC), which is a heterodimer of NACA and BTF3 (via NAC-A/B domains). NAC associates with ribosomes through the BTF3/NACB subunit and contacts the ribosomal protein L23, which is positioned near the exiting site. Both subunits can contact nascent polypeptide chains. NACA may also form homodimers, and only this form binds DNA (By similarity). Interacts with TBP and JUN. {ECO:0000250, ECO:0000269|PubMed:15299025, ECO:0000269|PubMed:9488445, ECO:0000269|PubMed:9488446}. DOMAIN: The positively charged inner surface of the NAC-A/B domain is crucial for NACA localization in the nucleus and DNA-binding. This region is blocked from binding nucleic acids in the heterodimeric complex by a helix region in the beta-subunit, it also displays much higher affinity for RNA than DNA (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Isoform 1 appears to be ubiquitously expressed. {ECO:0000269|PubMed:10224091, ECO:0000269|PubMed:8698236, ECO:0000269|PubMed:9877153}. +Q9DBR7 MYPT1_MOUSE Protein phosphatase 1 regulatory subunit 12A (Myosin phosphatase-targeting subunit 1) (Myosin phosphatase target subunit 1) 1029 114,996 Alternative sequence (1); Chain (1); Compositional bias (2); Modified residue (27); Motif (1); Region (1); Repeat (6) FUNCTION: Key regulator of protein phosphatase 1C (PPP1C). Mediates binding to myosin. As part of the PPP1C complex, involved in dephosphorylation of PLK1. Capable of inhibiting HIF1AN-dependent suppression of HIF1A activity (By similarity). {ECO:0000250|UniProtKB:O14974, ECO:0000250|UniProtKB:Q10728}. PTM: Phosphorylated by CIT (Rho-associated kinase) (By similarity). Phosphorylated cooperatively by ROCK1 and CDC42BP on Thr-694 (By similarity). Phosphorylated on upon DNA damage, probably by ATM or ATR. In vitro, phosphorylation of Ser-693 by PKA and PKG appears to prevent phosphorylation of the inhibitory site Thr-694, probably mediated by PRKG1. Phosphorylation at Ser-445, Ser-472 and Ser-909 by NUAK1 promotes interaction with 14-3-3, leading to inhibit interaction with myosin light chain MLC2, preventing dephosphorylation of MLC2. May be phosphorylated at Thr-694 by DMPK; may inhibit the myosin phosphatase activity (By similarity). Phosphorylated at Ser-473 by CDK1 during mitosis, creating docking sites for the POLO box domains of PLK1. Subsequently, PLK1 binds and phosphorylates PPP1R12A (By similarity). {ECO:0000250|UniProtKB:O14974}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O14974}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:O14974}. Note=Also along actomyosin filaments. {ECO:0000250|UniProtKB:O14974}. SUBUNIT: PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or PPP1CC, and one or several targeting or regulatory subunits. PPP1R12A mediates binding to myosin. Interacts with ARHA and CIT (By similarity). Binds PPP1R12B, ROCK1 and IL16. Interacts directly with PRKG1. Non-covalent dimer of 2 dimers; PRKG1-PRKG1 and PPP1R12A-PPP1R12A. Interacts with SMTNL1 (By similarity). Interacts with PPP1CB; the interaction is direct. Interacts (when phosphorylated at Ser-445, Ser-472 and Ser-910) with 14-3-3. Interacts with ROCK1 and ROCK2. Interacts with isoform 1 and isoform 2 of ZIPK/DAPK3. Interacts with RAF1. Interacts with HIF1AN (By similarity). Interacts with NCKAP1L (By similarity). {ECO:0000250|UniProtKB:O14974}. DOMAIN: Heterotetramerization is mediated by the interaction between a coiled-coil of PRKG1 and the leucine/isoleucine zipper of PPP1R12A/MBS, the myosin-binding subunit of the myosin phosphatase. {ECO:0000250}.; DOMAIN: The KVKF motif mediates interaction with PPP1CB. {ECO:0000250|UniProtKB:O14974}. TISSUE SPECIFICITY: Expressed in striated and vascular smooth muscle, specificcally in type 2a fibers (at protein level). Expression levels are 20-30% higher in developed males than females (at protein level). {ECO:0000269|PubMed:20634291}. +Q8BU40 NAL4A_MOUSE NACHT, LRR and PYD domains-containing protein 4A (NALP-ita) 982 112,601 Chain (1); Domain (2); Nucleotide binding (1); Repeat (10) FUNCTION: May be involved in inflammation and recognition of cytosolic pathogen-associated molecular patterns (PAMPs) not intercepted by membrane-bound receptors. {ECO:0000250}. +Q9CZR2 NALD2_MOUSE N-acetylated-alpha-linked acidic dipeptidase 2 (EC 3.4.17.21) (Glutamate carboxypeptidase III) (GCPIII) (N-acetylaspartylglutamate peptidase II) (NAAG-peptidase II) (N-acetylated-alpha-linked acidic dipeptidase II) (NAALADase II) 740 82,801 Active site (4); Binding site (4); Chain (1); Glycosylation (7); Metal binding (10); Region (5); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 8 31 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 7 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 32 740 Extracellular. {ECO:0000255}. FUNCTION: Has N-acetylated-alpha-linked-acidic dipeptidase (NAALADase) activity. Also exhibits a dipeptidyl-peptidase IV type activity. Inactivate the peptide neurotransmitter N-acetylaspartylglutamate. {ECO:0000269|PubMed:15086519}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q04609}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q04609}. SUBUNIT: Homodimer. {ECO:0000250}. DOMAIN: The NAALADase activity is found in the central region, the dipeptidyl peptidase IV type activity in the C-terminal. TISSUE SPECIFICITY: Expressed ovary, testes and lung, but not brain. {ECO:0000269|PubMed:15086519}. +Q9JIY7 NAT8_MOUSE N-acetyltransferase 8 (EC 2.3.1.-) (Acetyltransferase 2) (ATase2) (Camello-like protein 4) (Cysteinyl-conjugate N-acetyltransferase) (CCNAT) (EC 2.3.1.80) 227 25,638 Chain (1); Domain (1); Topological domain (2); Transmembrane (1) TRANSMEM 36 56 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 35 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 57 227 Lumenal. {ECO:0000255}. Sulfur metabolism; glutathione metabolism. FUNCTION: Acetylates the free alpha-amino group of cysteine S-conjugates to form mercapturic acids. This is the final step in a major route for detoxification of a wide variety of reactive electrophiles which starts with their incorporation into glutathione S-conjugates. The glutathione S-conjugates are then further processed into cysteine S-conjugates and finally mercapturic acids which are water soluble and can be readily excreted in urine or bile. Alternatively, may have a lysine N-acetyltransferase activity catalyzing peptidyl-lysine N6-acetylation of various proteins. Thereby, may regulate apoptosis through the acetylation and the regulation of the expression of PROM1. May also regulate amyloid beta-peptide secretion through acetylation of BACE1 and the regulation of its expression in neurons (By similarity). {ECO:0000250, ECO:0000269|PubMed:11397015}. SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. SUBUNIT: Interacts with PROM1. Interacts with BACE1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain (at protein level). {ECO:0000269|PubMed:22267734}. +Q6ZQA0 NBEL2_MOUSE Neurobeachin-like protein 2 2742 301,924 Alternative sequence (1); Chain (1); Domain (2); Modified residue (3); Repeat (7) FUNCTION: Probably involved in thrombopoiesis. Plays a role in the development or secretion of alpha-granules, that contain several growth factors important for platelet biogenesis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250}. +Q8BS03 PI15_MOUSE Peptidase inhibitor 15 (PI-15) (SugarCrisp) 258 29,151 Chain (1); Domain (1); Erroneous initiation (1); Glycosylation (2); Propeptide (1); Sequence conflict (2); Signal peptide (1) FUNCTION: Serine protease inhibitor which displays weak inhibitory activity against trypsin (By similarity). May play a role in facial patterning during embryonic development (By similarity). {ECO:0000250|UniProtKB:O43692, ECO:0000250|UniProtKB:Q98ST6}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:O43692}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O43692}. TISSUE SPECIFICITY: Weakly expressed. Expressed at low level in prostate, mammary gland, salivary gland and thyroid gland. {ECO:0000269|PubMed:11287197}. +P43252 PI2R_MOUSE Prostacyclin receptor (Prostaglandin I2 receptor) (PGI receptor) (PGI2 receptor) (Prostanoid IP receptor) 415 44,463 Beta strand (1); Chain (1); Disulfide bond (2); Erroneous initiation (1); Glycosylation (1); Lipidation (3); Modified residue (2); Mutagenesis (1); Propeptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 45 66 Helical; Name=1. {ECO:0000255}.; TRANSMEM 80 104 Helical; Name=2. {ECO:0000255}.; TRANSMEM 123 143 Helical; Name=3. {ECO:0000255}.; TRANSMEM 163 186 Helical; Name=4. {ECO:0000255}.; TRANSMEM 216 236 Helical; Name=5. {ECO:0000255}.; TRANSMEM 264 288 Helical; Name=6. {ECO:0000255}.; TRANSMEM 302 322 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 44 Extracellular. {ECO:0000255}.; TOPO_DOM 67 79 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 105 122 Extracellular. {ECO:0000255}.; TOPO_DOM 144 162 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 187 215 Extracellular. {ECO:0000255}.; TOPO_DOM 237 263 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 289 301 Extracellular. {ECO:0000255}.; TOPO_DOM 323 415 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for prostacyclin (prostaglandin I2 or PGI2). The activity of this receptor is mediated by G(s) proteins which activate adenylate cyclase. PTM: Isoprenylation does not influence ligand binding but is required for efficient coupling to the effectors adenylyl cyclase and phospholipase C. {ECO:0000269|PubMed:10446129}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBUNIT: Interacts (non-isoprenylated C-terminus) with PDZK1. {ECO:0000269|PubMed:23457445}. +Q3UWS6 MYCOS_MOUSE Myocilin opposite strand protein 143 15,568 Chain (1) +Q6URW6 MYH14_MOUSE Myosin-14 (Myosin heavy chain 14) (Myosin heavy chain, non-muscle IIc) (Non-muscle myosin heavy chain IIc) (NMHC II-C) 2000 228,586 Alternative sequence (2); Chain (1); Coiled coil (1); Domain (3); Initiator methionine (1); Modified residue (10); Nucleotide binding (1); Region (1) FUNCTION: Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping. {ECO:0000250}. SUBUNIT: Myosin is a hexameric protein that consists of 2 heavy chain subunits (MHC), 2 alkali light chain subunits (MLC) and 2 regulatory light chain subunits (MLC-2). {ECO:0000250}. DOMAIN: The rodlike tail sequence is highly repetitive, showing cycles of a 28-residue repeat pattern composed of 4 heptapeptides, characteristic for alpha-helical coiled coils. {ECO:0000250}. TISSUE SPECIFICITY: Highest levels in lung, kidney, brain and colon, very low levels in liver and bladder and no expression in spleen or seminal vesicle (at protein level). Isoform 1 is expressed in liver, kidney and testis with low levels in skeletal muscle and heart. Isoform 1 and isoform 2 are expressed in brain and lung. Isoform 2 is the main isoform expressed in skeletal muscle and heart. Isoform 3 is limited to brain stem, cerebellum and spinal cord. {ECO:0000269|PubMed:14594953, ECO:0000269|PubMed:19240025}. +Q5SUV2 MYBPP_MOUSE MYCBP-associated protein (AMAM-1) (AMY-1-binding protein 1) (AMAP-1) 932 106,452 Alternative sequence (2); Chain (1); Erroneous initiation (1); Modified residue (3); Sequence conflict (1) FUNCTION: May play a role in spermatogenesis. May be involved in synaptic processes (By similarity). {ECO:0000250|UniProtKB:Q69CM7, ECO:0000250|UniProtKB:Q8TBZ2}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q69CM7, ECO:0000250|UniProtKB:Q8TBZ2}. Membrane {ECO:0000250|UniProtKB:Q69CM7, ECO:0000250|UniProtKB:Q8TBZ2}. Note=Colocalizes with MYCBP in the cytoplasm. {ECO:0000250|UniProtKB:Q69CM7, ECO:0000250|UniProtKB:Q8TBZ2}. SUBUNIT: Interacts with MYCBP. {ECO:0000250|UniProtKB:Q8TBZ2}. +Q69ZN7 MYOF_MOUSE Myoferlin (Fer-1-like protein 3) 2048 233,324 Alternative sequence (6); Chain (1); Compositional bias (5); Domain (5); Erroneous initiation (1); Frameshift (1); Modified residue (5); Mutagenesis (1); Region (1); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 2013 2033 Helical. {ECO:0000255}. TOPO_DOM 1 2012 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 2034 2048 Extracellular. {ECO:0000255}. FUNCTION: Calcium/phospholipid-binding protein that plays a role in the plasmalemma repair mechanism of endothelial cells that permits rapid resealing of membranes disrupted by mechanical stress. Involved in endocytic recycling. Implicated in VEGF signal transduction by regulating the levels of the receptor KDR. {ECO:0000269|PubMed:16280346, ECO:0000269|PubMed:17702744, ECO:0000269|PubMed:18502764}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Found at nuclear and plasma membranes. Enriched in undifferentiated myoblasts near the plasma membrane in puncate structures (By similarity). Concentrated at the membrane sites of both myoblast-myoblast and myoblast-myotube fusions. Detected at the plasmalemma in endothelial cells lining intact blood vessels. {ECO:0000250, ECO:0000269|PubMed:16280346, ECO:0000269|PubMed:17702744}. SUBUNIT: Interacts with EHD1 (PubMed:21177873). Interacts with EHD2; the interaction is direct (PubMed:21177873). Interacts with DNM2 and KDR (PubMed:21177873). Interacts with RIPOR2 (By similarity). {ECO:0000250|UniProtKB:Q9NZM1, ECO:0000269|PubMed:17702744, ECO:0000269|PubMed:21177873}. DOMAIN: The C2 1 domain associates with lipid membranes in a calcium-dependent manner. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in myoblasts (at protein level). Expressed in endothelial cells. {ECO:0000269|PubMed:16280346, ECO:0000269|PubMed:17702744}. +Q9D1N4 MYMK_MOUSE Protein myomaker (Myoblast fusion maker) (Transmembrane protein 8C) 221 24,792 Chain (1); Transmembrane (6) TRANSMEM 4 24 Helical. {ECO:0000255}.; TRANSMEM 30 50 Helical. {ECO:0000255}.; TRANSMEM 65 85 Helical. {ECO:0000255}.; TRANSMEM 114 134 Helical. {ECO:0000255}.; TRANSMEM 154 174 Helical. {ECO:0000255}.; TRANSMEM 176 196 Helical. {ECO:0000255}. FUNCTION: Myoblast-specific protein that mediates myoblast fusion, an essential step for the formation of multi-nucleated muscle fibers. Actively participates in the membrane fusion reaction. Associates with MYMX to promote myoblast fusion. {ECO:0000269|PubMed:23868259, ECO:0000269|PubMed:28386024, ECO:0000269|PubMed:28681861}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23868259}; Multi-pass membrane protein {ECO:0000269|PubMed:23868259}. Note=Localizes on the cell surface of myoblasts during fusion and is down-regulated thereafter. SUBUNIT: Interacts with MYMX (PubMed:28386024). {ECO:0000269|PubMed:28386024}. TISSUE SPECIFICITY: Specifically expressed in skeletal muscle during embryogenesis and adult muscle regeneration. {ECO:0000269|PubMed:23868259, ECO:0000269|PubMed:28681861}. +A2ABU4 MYOM3_MOUSE Myomesin-3 (Myomesin family member 3) 1439 161,778 Chain (1); Coiled coil (1); Domain (9) FUNCTION: May link the intermediate filament cytoskeleton to the M-disk of the myofibrils in striated muscle. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, M line {ECO:0000269|PubMed:18177667}. SUBUNIT: Homodimer. {ECO:0000269|PubMed:18177667}. TISSUE SPECIFICITY: Mainly expressed in slow muscle, extraocular muscle and embryonic/neonatal skeletal muscle (at protein level). Expression in skeletal muscle is fiber type specific, with the highest levels in type IIA fibers (intermediate speed) and lower levels in type I fibers. {ECO:0000269|PubMed:18177667}. +Q80YT7 MYOME_MOUSE Myomegalin (Phosphodiesterase 4D-interacting protein) 2224 250,631 Alternative sequence (3); Chain (1); Coiled coil (12); Domain (1); Erroneous initiation (1); Modified residue (1); Sequence caution (1); Sequence conflict (3) FUNCTION: Functions as an anchor sequestering components of the cAMP-dependent pathway to Golgi and/or centrosomes (By similarity). {ECO:0000250|UniProtKB:Q9WUJ3}.; FUNCTION: Isoform 2: Participates in microtubule dynamics, promoting microtubule assembly. Depending upon the cell context, may act at the level of the Golgi apparatus or that of the centrosome. In complex with AKAP9, recruits CAMSAP2 to the Golgi apparatus and tethers non-centrosomal minus-end microtubules to the Golgi, an important step for polarized cell movement. In complex with AKAP9, EB1/MAPRE1 and CDK5RAP2, contributes to microtubules nucleation and extension from the centrosome to the cell periphery, a crucial process for directed cell migration, mitotic spindle orientation and cell-cycle progression. {ECO:0000250|UniProtKB:Q5VU43}. SUBCELLULAR LOCATION: Isoform 2: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q5VU43}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q5VU43}. Golgi apparatus {ECO:0000250|UniProtKB:Q5VU43}. Note=Associated with the microtubule network at the growing distal tip of microtubules. Targeting to the Golgi apparatus requires AKAP9. {ECO:0000250|UniProtKB:Q5VU43}. SUBUNIT: Interacts with PDE4D (By similarity). Isoform 2 interacts with MAPRE1 and MAPRE3. Isoform 2 forms a pericentrosomal complex with AKAP9, CDK5RAP2 and EB1/MAPRE1; within this complex, may mediate MAPRE1-binding to CDK5RAP2. Interaction with AKAP9 stabilizes both proteins. Isoform 2 interacts (via N-terminus) with CAMSAP2; this interaction is much stronger in the presence of AKAP9. In complex with AKAP9, Isoform 2 recruits CAMSAP2 to the Golgi apparatus. Isoform 2 interacts with unglycosylated LGALS3BP; this interaction may connect the pericentrosomal complex to the gamma-tubulin ring complex (gamma-TuRC) to promote microtubule assembly and acetylation (By similarity). {ECO:0000250|UniProtKB:Q5VU43, ECO:0000250|UniProtKB:Q9WUJ3}. DOMAIN: Isoform 2: residues 1-150 are involved in AKAP9-binding. {ECO:0000250|UniProtKB:Q5VU43}. +Q8BUR9 MZT1_MOUSE Mitotic-spindle organizing protein 1 (Mitotic-spindle organizing protein associated with a ring of gamma-tubulin 1) 78 8,132 Chain (1); Initiator methionine (1); Modified residue (1) FUNCTION: Required for gamma-tubulin complex recruitment to the centrosome. {ECO:0000269|PubMed:20360068}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:20360068}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:20360068}. SUBUNIT: Part of the gamma-tubulin complex. Interacts with TUBG1. {ECO:0000269|PubMed:20360068}. +Q5SUA5 MYO1G_MOUSE Unconventional myosin-Ig 1024 117,227 Chain (1); Domain (3); Frameshift (1); Mutagenesis (4); Nucleotide binding (1); Region (1); Sequence conflict (3) FUNCTION: Unconventional myosin required during immune response for detection of rare antigen-presenting cells by regulating T-cell migration (PubMed:25083865). Unconventional myosins are actin-based motor molecules with ATPase activity and serve in intracellular movements. Acts as a regulator of T-cell migration by generating membrane tension, enforcing cell-intrinsic meandering search, thereby enhancing detection of rare antigens during lymph-node surveillance, enabling pathogen eradication (PubMed:25083865). Also required in B-cells, where it regulates different membrane/cytoskeleton-dependent processes (PubMed:24310084). Involved in Fc-gamma receptor (Fc-gamma-R) phagocytosis (PubMed:23038771). {ECO:0000269|PubMed:23038771, ECO:0000269|PubMed:24310084, ECO:0000269|PubMed:25083865}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19968988, ECO:0000269|PubMed:20071333, ECO:0000269|PubMed:24310084, ECO:0000269|PubMed:25083865}; Peripheral membrane protein {ECO:0000269|PubMed:19968988, ECO:0000269|PubMed:20071333, ECO:0000269|PubMed:24310084, ECO:0000269|PubMed:25083865}. Cell projection, phagocytic cup {ECO:0000269|PubMed:23038771}. Note=Recruited to Fc-gamma receptor (Fc-gamma-R) phagocytic cup (PubMed:23038771). In T-cells, transiently accumulates in discrete areas at the plasma membrane of migrating cells or when membranes are deformed (PubMed:25083865). {ECO:0000269|PubMed:23038771, ECO:0000269|PubMed:25083865}. SUBUNIT: Interacts with calmodulin; via its IQ motifs. {ECO:0000250}. DOMAIN: The myosin tail domain mediates binding to phosphatidylinositol-3,4-bisphosphate (PtdIns(3,4)P2), phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P2) and phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) and binds to membranous compartments. It is required for recruitment to Fc-gamma receptor (Fc-gamma-R) phagocytic cups. {ECO:0000269|PubMed:23038771}. TISSUE SPECIFICITY: Specifically expressed in hematopoietic cells. Detected in adult tissues of the immune system such as thymus, lymph nodes and spleen, but not in brain, lung, heart, liver, small intestine, testis and kidney (at protein level). Highly expressed in T-lymphocytes; constitutes the most highly expressed class I myosin in naive CD4 and CD8 T-cells. Also present in B-lymphocytes. {ECO:0000269|PubMed:19968988, ECO:0000269|PubMed:20071333, ECO:0000269|PubMed:24310084, ECO:0000269|PubMed:25083865}. +S4R2P9 NAC3_MOUSE Sodium/calcium exchanger 3 (Na(+)/Ca(2+)-exchange protein 3) (Solute carrier family 8 member 3) 928 102,984 Alternative sequence (1); Beta strand (9); Chain (1); Domain (2); Glycosylation (2); Helix (2); Metal binding (24); Region (1); Sequence conflict (1); Signal peptide (1); Topological domain (12); Transmembrane (11); Turn (1) TRANSMEM 74 94 Helical. {ECO:0000255}.; TRANSMEM 148 168 Helical. {ECO:0000255}.; TRANSMEM 170 190 Helical. {ECO:0000255}.; TRANSMEM 202 222 Helical. {ECO:0000255}.; TRANSMEM 231 251 Helical. {ECO:0000255}.; TRANSMEM 728 748 Helical. {ECO:0000255}.; TRANSMEM 756 776 Helical. {ECO:0000255}.; TRANSMEM 780 800 Helical. {ECO:0000255}.; TRANSMEM 830 850 Helical. {ECO:0000255}.; TRANSMEM 862 882 Helical. {ECO:0000255}.; TRANSMEM 905 925 Helical. {ECO:0000255}. TOPO_DOM 31 73 Extracellular. {ECO:0000305}.; TOPO_DOM 95 147 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 169 169 Extracellular. {ECO:0000305}.; TOPO_DOM 191 201 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 223 230 Extracellular. {ECO:0000305}.; TOPO_DOM 252 727 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 749 755 Extracellular. {ECO:0000305}.; TOPO_DOM 777 779 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 801 829 Extracellular. {ECO:0000305}.; TOPO_DOM 851 861 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 883 904 Extracellular. {ECO:0000305}.; TOPO_DOM 926 928 Cytoplasmic. {ECO:0000305}. FUNCTION: Mediates the electrogenic exchange of Ca(2+) against Na(+) ions across the cell membrane, and thereby contributes to the regulation of cytoplasmic Ca(2+) levels and Ca(2+)-dependent cellular processes. Contributes to cellular Ca(2+) homeostasis in excitable cells, both in muscle and in brain (PubMed:14722618, PubMed:21593315). In a first phase, voltage-gated channels mediate the rapid increase of cytoplasmic Ca(2+) levels due to release of Ca(2+) stores from the endoplasmic reticulum. SLC8A3 mediates the export of Ca(2+) from the cell during the next phase, so that cytoplasmic Ca(2+) levels rapidly return to baseline (PubMed:14722618, PubMed:21593315). Contributes to Ca(2+) transport during excitation-contraction coupling in muscle (PubMed:14722618). In neurons, contributes to the rapid decrease of cytoplasmic Ca(2+) levels back to baseline after neuronal activation, and thereby contributes to modulate synaptic plasticity, learning and memory (PubMed:21593315). Required for normal oligodendrocyte differentiation and for normal myelination (PubMed:21959935). Mediates Ca(2+) efflux from mitochondria and contributes to mitochondrial Ca(2+) ion homeostasis (PubMed:24616101). Isoform 1 displays higher calcium exchanger activity than isoform 2, probably because isoform 1 has a lower threshold for activation by cytoplasmic Ca(2+) (PubMed:24616101). {ECO:0000269|PubMed:14722618, ECO:0000269|PubMed:21593315, ECO:0000269|PubMed:21959935, ECO:0000269|PubMed:24616101}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14722618, ECO:0000269|PubMed:24101730}; Multi-pass membrane protein {ECO:0000305}. Perikaryon {ECO:0000250|UniProtKB:P70549}. Cell projection, dendrite {ECO:0000250|UniProtKB:P70549}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:P70549}. Cell membrane, sarcolemma {ECO:0000269|PubMed:14722618}. Cytoplasm, sarcoplasm {ECO:0000269|PubMed:14722618}. Cell junction {ECO:0000269|PubMed:14722618}. Mitochondrion outer membrane {ECO:0000269|PubMed:24101730}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P57103}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:24101730}; Multi-pass membrane protein {ECO:0000305}. Note=Detected at neuromuscular junctions. {ECO:0000269|PubMed:14722618}.; SUBCELLULAR LOCATION: Isoform 1: Cell membrane {ECO:0000269|PubMed:24616101}; Multi-pass membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: Isoform 2: Cell membrane {ECO:0000269|PubMed:24616101}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Interacts with AKAP1. {ECO:0000269|PubMed:24616101}. DOMAIN: The cytoplasmic Calx-beta domains bind the regulatory Ca(2+). The first Calx-beta domain can bind up to four Ca(2+) ions. The second domain can bind another two Ca(2+) ions that are essential for calcium-regulated ion exchange. {ECO:0000250|UniProtKB:P23685}. TISSUE SPECIFICITY: Detected in gray and white matter in the spinal cord (PubMed:21959935). Detected in hippocampus neurons (PubMed:21593315). Detected in brain cortex neurons (PubMed:24101730). Detected in skeletal muscle (at protein level) (PubMed:14722618). Isoform 1 and isoform 2 are highly expressed in brain; levels are higher for isoform 2 (PubMed:24616101). Isoform 1 and isoform 2 are detected in soleus muscle; levels are higher for isoform 1 (PubMed:24616101). Detected in gastrocnemius muscle (PubMed:14722618). {ECO:0000269|PubMed:14722618, ECO:0000269|PubMed:21593315, ECO:0000269|PubMed:21959935, ECO:0000269|PubMed:24101730, ECO:0000269|PubMed:24616101}. +Q6PGB6 NAA50_MOUSE N-alpha-acetyltransferase 50 (EC 2.3.1.258) (N-acetyltransferase NAT13) (N-epsilon-acetyltransferase 50) (EC 2.3.1.-) (NatE catalytic subunit) 169 19,414 Active site (2); Alternative sequence (4); Binding site (2); Chain (1); Domain (1); Erroneous termination (1); Modified residue (5); Region (3) FUNCTION: N-alpha-acetyltransferase that acetylates the N-terminus of proteins that retain their initiating methionine. Has a broad substrate specificity: able to acetylate the initiator methionine of most peptides, except for those with a proline in second position. Also displays N-epsilon-acetyltransferase activity by mediating acetylation of the side chain of specific lysines on proteins. Autoacetylates in vivo. The relevance of N-epsilon-acetyltransferase activity is however unclear: able to acetylate H4 in vitro, but this result has not been confirmed in vivo. Component of a N-alpha-acetyltransferase complex containing NAA10 and NAA15, but NAA50 does not influence the acetyltransferase activity of NAA10: this multiprotein complex probably constitutes the major contributor for N-terminal acetylation at the ribosome exit tunnel, with NAA10 acetylating all amino termini that are devoid of methionine and NAA50 acetylating other peptides. Required for sister chromatid cohesion during mitosis by promoting binding of CDCA5/sororin to cohesin: may act by counteracting the function of NAA10. {ECO:0000250|UniProtKB:Q9GZZ1}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16484612}. Nucleus {ECO:0000250|UniProtKB:Q9GZZ1}. Note=Localizes to the cytoplasm in interphase cells. {ECO:0000250|UniProtKB:Q9GZZ1}. SUBUNIT: Component of a complex composed of NAA50, NAA15 and NAA10 (By similarity). Interacts with NAA35 (PubMed:16484612). {ECO:0000250|UniProtKB:Q9GZZ1, ECO:0000269|PubMed:16484612}. +P61600 NAA20_MOUSE N-alpha-acetyltransferase 20 (EC 2.3.1.254) (Methionine N-acetyltransferase) (N-acetyltransferase 5) (N-terminal acetyltransferase B complex catalytic subunit NAA20) (N-terminal acetyltransferase B complex catalytic subunit NAT5) (NatB complex subunit NAT5) (NatB catalytic subunit) 178 20,368 Chain (1); Domain (1) FUNCTION: Catalytic subunit of the NatB complex which catalyzes acetylation of the N-terminal methionine residues of peptides beginning with Met-Asp, Met-Glu, Met-Asn and Met-Gln. Proteins with cell cycle functions are overrepresented in the pool of NatB substrates. Required for maintaining the structure and function of actomyosin fibers and for proper cellular migration. {ECO:0000250|UniProtKB:P61599}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P61599}. Nucleus {ECO:0000250|UniProtKB:P61599}. SUBUNIT: Component of the N-terminal acetyltransferase B (NatB) complex which is composed of NAA20 and NAA25. {ECO:0000250}. +Q5DTJ9 MYPN_MOUSE Myopalladin 1315 144,114 Chain (1); Coiled coil (1); Compositional bias (1); Disulfide bond (3); Domain (5); Erroneous initiation (1); Modified residue (9); Sequence conflict (1) FUNCTION: Component of the sarcomere that tethers together nebulin (skeletal muscle) and nebulette (cardiac muscle) to alpha-actinin, at the Z lines. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q86TC9}. Nucleus {ECO:0000250|UniProtKB:Q86TC9}. Cytoplasm, myofibril, sarcomere {ECO:0000250|UniProtKB:Q86TC9}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:Q86TC9}. Note=Bound to sarcomere both at the Z-line periphery and in the central I-band region. {ECO:0000250|UniProtKB:Q86TC9}. SUBUNIT: Interacts with TTN/titin, NEB, NEBL, ACTN2 and CARP. {ECO:0000250}. +B1AS42 NB5R5_MOUSE NADH-cytochrome b5 reductase-like (EC 1.6.2.2) 316 35,884 Alternative sequence (6); Chain (1); Domain (2); Erroneous initiation (2); Nucleotide binding (2) FUNCTION: NADH-cytochrome b5 reductases are involved in desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction. {ECO:0000250}. +Q3UGX3 NAT8L_MOUSE N-acetylaspartate synthetase (NAA synthetase) (EC 2.3.1.17) (N-acetyltransferase 8-like protein) (Protein Shati) 299 32,777 Chain (1); Domain (1); Erroneous initiation (2); Sequence conflict (3); Transmembrane (1) TRANSMEM 118 138 Helical. {ECO:0000255}. FUNCTION: Plays a role in the regulation of lipogenesis by producing N-acetylaspartate acid (NAA), a brain-specific metabolite. NAA occurs in high concentration in brain and its hydrolysis plays a significant part in the maintenance of intact white matter. Promotes dopamine uptake by regulating TNF-alpha expression. Attenuates methamphetamine-induced inhibition of dopamine uptake. {ECO:0000269|PubMed:19014384, ECO:0000269|PubMed:19807691, ECO:0000269|PubMed:20385109, ECO:0000269|PubMed:20643647}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Microsome membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Mitochondrion membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Rough endoplasmic reticulum membrane; Single-pass membrane protein. TISSUE SPECIFICITY: Expressed in brain, kidney, liver and spleen. In brain, present in neurons but not in astrocytes (at protein level). Expressed in brain, thymus and spleen. {ECO:0000269|PubMed:17626222, ECO:0000269|PubMed:19807691, ECO:0000269|PubMed:20385109}. +Q60867 NDF1_MOUSE Neurogenic differentiation factor 1 (NeuroD1) (Beta-cell E-box transcriptional activator 2) (Beta2) 357 39,999 Beta strand (2); Chain (1); Compositional bias (4); Domain (1); Helix (2); Modified residue (5); Motif (1); Mutagenesis (5) FUNCTION: Acts as a transcriptional activator: mediates transcriptional activation by binding to E box-containing promoter consensus core sequences 5'-CANNTG-3'. Associates with the p300/CBP transcription coactivator complex to stimulate transcription of the secretin gene as well as the gene encoding the cyclin-dependent kinase inhibitor CDKN1A. Contributes to the regulation of several cell differentiation pathways, like those that promote the formation of early retinal ganglion cells, inner ear sensory neurons, granule cells forming either the cerebellum or the dentate gyrus cell layer of the hippocampus, endocrine islet cells of the pancreas and enteroendocrine cells of the small intestine. Together with PAX6 or SIX3, is required for the regulation of amacrine cell fate specification. Also required for dendrite morphogenesis and maintenance in the cerebellar cortex. Associates with chromatin to enhancer regulatory elements in genes encoding key transcriptional regulators of neurogenesis. {ECO:0000269|PubMed:10398678, ECO:0000269|PubMed:10639171, ECO:0000269|PubMed:11152640, ECO:0000269|PubMed:11861467, ECO:0000269|PubMed:11970861, ECO:0000269|PubMed:12810726, ECO:0000269|PubMed:14697366, ECO:0000269|PubMed:15797719, ECO:0000269|PubMed:18007592, ECO:0000269|PubMed:18339630, ECO:0000269|PubMed:19200230, ECO:0000269|PubMed:19759004, ECO:0000269|PubMed:21593321, ECO:0000269|PubMed:9308961, ECO:0000269|PubMed:9512516}. PTM: In islet cells, phosphorylated on Ser-274 upon glucose stimulation; which may be required for nuclear localization. In activated neurons, phosphorylated on Ser-336; which promotes dendritic growth (By similarity). Phosphorylated by MAPK1; phosphorylation regulates heterodimerization and DNA-binding activities. Phosphorylation on Ser-266 and Ser-274 increases transactivation on the insulin promoter in glucose-stimulated insulinoma cells. {ECO:0000250, ECO:0000269|PubMed:12810726, ECO:0000269|PubMed:15797719}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}. Note=In pancreatic islet cells, shuttles to the nucleus in response to glucose stimulation. Colocalizes with NR0B2 in the nucleus (By similarity). {ECO:0000250}. SUBUNIT: Heterodimer with TCF3/E47; the heterodimer is inhibited in presence of ID2, but not NR0B2, to E-box element. Interacts with EP300; the interaction is inhibited by NR0B2. Interacts with TCF3; the interaction is inhibited by ID2. Interacts with RREB1 (By similarity). Heterodimer with TCF3/E47. Efficient DNA-binding requires dimerization with another bHLH protein. Interacts (via helix-loop-helix motif domain) with EP300 (via C-terminus). Interacts with ATOH8. {ECO:0000250, ECO:0000269|PubMed:18069799, ECO:0000269|PubMed:18560595, ECO:0000269|PubMed:9512516}. TISSUE SPECIFICITY: Expressed in pancreatic beta cells, pulmonary neuroendocrine cells and retinal interneurons amacrine cells (at protein level). Expressed in endocrine cells of the pancreas. Expressed in the inner layer of cerebellar external granular layer (EGL). Expressed in the Ammon's horn (AH), which includes the CA1-CA3 pyramidal layer and in granule cells of the dentate gyrus (DG). Expressed in photoreceptors of the outer nuclear layer (ONL), in a subset of cells in the lower half of the inner nuclear layer (INL), and in a subset of cells in the ganglion cell layer (GCL) of the retina. Expressed in cholinergic and AII amacrine cell types. Expressed in differentiating neurons of both the central and peripheral nervous systems. {ECO:0000269|PubMed:10398678, ECO:0000269|PubMed:11861467, ECO:0000269|PubMed:12810726, ECO:0000269|PubMed:14752053, ECO:0000269|PubMed:19759004, ECO:0000269|PubMed:9308961}. +E9Q3L2 PI4KA_MOUSE Phosphatidylinositol 4-kinase alpha (PI4-kinase alpha) (PI4K-alpha) (PtdIns-4-kinase alpha) (EC 2.7.1.67) 2105 237,042 Chain (1); Domain (2); Modified residue (9); Sequence conflict (1) FUNCTION: Acts on phosphatidylinositol (PtdIns) in the first committed step in the production of the second messenger inositol-1,4,5,-trisphosphate. {ECO:0000250|UniProtKB:P42356}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P42356}. Cell membrane {ECO:0000250|UniProtKB:P42356}. Note=Localization to the plasma membrane is mediated by the PI4K complex and association with EFR3 (EFR3A or EFR3B), TTC7 (TTC7A or TTC7B) and FAM126 (FAM126A or FAM126B). Localization to the plasma membrane is regulated by TMEM150A. {ECO:0000250|UniProtKB:P42356}. SUBUNIT: Component of a phosphatidylinositol 4-kinase (PI4K) complex, composed of PI4KA, EFR3 (EFR3A or EFR3B), TTC7 (TTC7A or TTC7B) and FAM126 (FAM126A or FAM126B). Interacts with TMEM150A; regulating recruitment to the plasma membrane. {ECO:0000250|UniProtKB:P42356}. +Q3URE9 LIGO2_MOUSE Leucine-rich repeat and immunoglobulin-like domain-containing nogo receptor-interacting protein 2 (Leucine-rich repeat neuronal protein 6C) 606 68,069 Chain (1); Disulfide bond (1); Domain (2); Glycosylation (10); Repeat (12); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 546 566 Helical. {ECO:0000255}. TOPO_DOM 28 545 Extracellular. {ECO:0000255}.; TOPO_DOM 567 606 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q9ERG0 LIMA1_MOUSE LIM domain and actin-binding protein 1 (Epithelial protein lost in neoplasm) (mEPLIN) 753 84,060 Alternative sequence (1); Chain (1); Domain (1); Modified residue (22); Motif (1); Mutagenesis (4); Region (1); Sequence conflict (6) FUNCTION: Actin-binding protein involved in actin cytoskeleton regulation and dynamics. Increases the number and size of actin stress fibers and inhibits membrane ruffling. Inhibits actin filament depolymerization. Bundles actin filaments, delays filament nucleation and reduces formation of branched filaments (By similarity). Plays a role in cholesterol homeostasis. Influences plasma cholesterol levels through regulation of intestinal cholesterol absorption. May act as a scaffold protein by regulating NPC1L1 transportation, an essential protein for cholesterol absorption, to the plasma membrane by recruiting MYO5B to NPC1L1, and thus facilitates cholesterol uptake (PubMed:29880681). {ECO:0000250|UniProtKB:Q9UHB6, ECO:0000269|PubMed:29880681}. PTM: Phosphorylation of the C-terminal region by MAPK1/MAPK3 reduces its association with F-actin and contributes to actin filament reorganization and enhances cell motility. {ECO:0000269|PubMed:17875928}. SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9UHB6}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000269|PubMed:17875928}. Cell membrane {ECO:0000269|PubMed:29880681}. Cell projection, ruffle {ECO:0000269|PubMed:17875928}. Note=Expressed mainly in the brush border membrane of the small intestine and colocalizes with NPC1L1 and MYO5B (PubMed:29880681). Colocalizes with PXN at focal adhesions in mesangial cells (By similarity). Colocalizes with actin stress fibers in quiescent cells. PDGF stimulation induced disassembly of stress fibers and formation of peripheral and dorsal ruffles, where LIMA1 is relocalized (PubMed:17875928). {ECO:0000250|UniProtKB:Q9UHB6, ECO:0000269|PubMed:17875928, ECO:0000269|PubMed:29880681}. SUBUNIT: Interacts with NPC1L1; bridges NPC1L1 with MYO5B (PubMed:29880681). Interacts with MYO5B; bridges MYO5B with NPC1L1 (PubMed:29880681). Interacts with PXN; this complex stabilizes actin dynamics (By similarity). Binds to G-actin and F-actin (PubMed:17875928) (By similarity). {ECO:0000250|UniProtKB:Q9UHB6, ECO:0000269|PubMed:17875928, ECO:0000269|PubMed:29880681}. DOMAIN: Contains at least 2 actin-binding domains, one on each side of the LIM domain. Both domains bind actin monomers and filaments. The C-terminal domain binds filaments more efficiently than the N-terminus (By similarity). {ECO:0000250|UniProtKB:Q9UHB6}. TISSUE SPECIFICITY: Highly expressed in the small intestine, including the duodenum, jejunum, and ileum. Low expression in the liver and very low expressed in the heart, spleen, lung, brain, and pancreas (PubMed:29880681). Isoform Alpha is highly expressed in embryos from day 7-11 and in adult spleen and lung. Isoform Beta expression is highest in adult kidney, testis, lung and liver, intermediate in heart, brain, spleen, skeletal muscle and low in embryos. {ECO:0000269|PubMed:29880681}. +Q9WVG5 LIPE_MOUSE Endothelial lipase (EC 3.1.1.3) (Endothelial cell-derived lipase) (EDL) 500 56,629 Active site (3); Chain (1); Compositional bias (1); Disulfide bond (5); Domain (1); Glycosylation (6); Region (1); Sequence conflict (2); Signal peptide (1) FUNCTION: Has phospholipase and triglyceride lipase activities. Hydrolyzes high density lipoproteins (HDL) more efficiently than other lipoproteins. Binds heparin (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Head to tail homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in placenta, lung, liver, testis and spleen. +Q8K2A6 LIPM_MOUSE Lipase member M (EC 3.1.1.-) (Lipase-like abhydrolase domain-containing protein 3) 422 48,254 Active site (3); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Plays a highly specific role in the last step of keratinocyte differentiation. May have an essential function in lipid metabolism of the most differentiated epidermal layers (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +P17892 LIPR2_MOUSE Pancreatic lipase-related protein 2 (PL-RP2) (EC 3.1.1.26) (EC 3.1.1.3) (Cytotoxic T-lymphocyte lipase) (Galactolipase) 482 54,017 Active site (3); Chain (1); Disulfide bond (5); Domain (1); Glycosylation (2); Metal binding (4); Sequence conflict (9); Signal peptide (1) FUNCTION: Lipase with broad substrate specificity. Can hydrolyze both phospholipids and galactolipids. Acts preferentially on monoglycerides, phospholipids and galactolipids. Contributes to milk fat hydrolysis (By similarity). {ECO:0000250|UniProtKB:P54317, ECO:0000269|PubMed:21382969, ECO:0000269|PubMed:2302735}. SUBCELLULAR LOCATION: Secreted. +P43137 LIT1_MOUSE Lithostathine-1 (Islet of Langerhans regenerating protein 1) (REG 1) (Pancreatic stone protein 1) (PSP) (Pancreatic thread protein 1) (PTP) (Regenerating protein 1) 165 18,519 Chain (1); Disulfide bond (3); Domain (1); Glycosylation (1); Modified residue (1); Signal peptide (1) FUNCTION: Might act as an inhibitor of spontaneous calcium carbonate precipitation. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. TISSUE SPECIFICITY: Expressed only in regenerating islets and normal exocrine pancreas, but not in normal pancreatic islets. Expressed strongly in pancreas, moderately in gall bladder, and weakly in liver. +P11152 LIPL_MOUSE Lipoprotein lipase (LPL) (EC 3.1.1.34) 474 53,109 Active site (3); Chain (1); Disulfide bond (5); Domain (1); Glycosylation (2); Modified residue (3); Region (1); Sequence conflict (4); Signal peptide (1) FUNCTION: The primary function of this lipase is the hydrolysis of triglycerides of circulating chylomicrons and very low density lipoproteins (VLDL). Binding to heparin sulfate proteogylcans at the cell surface is vital to the function. The apolipoprotein, APOC2, acts as a coactivator of LPL activity in the presence of lipids on the luminal surface of vascular endothelium. {ECO:0000250, ECO:0000250|UniProtKB:P06858}. PTM: Tyrosine nitration after lipopolysaccharide (LPS) challenge down-regulates the lipase activity. {ECO:0000250|UniProtKB:Q06000}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. Secreted {ECO:0000250|UniProtKB:P06858}. Note=Locates to the plasma membrane of microvilli of hepatocytes with triacyl-glycerol-rich lipoproteins (TRL). Some of the bound LPL is then internalized and located inside non-coated endocytic vesicles (By similarity). {ECO:0000250}. SUBUNIT: Homodimer (PubMed:25066055). Interacts with APOC2; the interaction activates LPL activity in the presence of lipids (By similarity). Interacts with GPIHBP1 (PubMed:17403372). Interacts with LMF1 and SEL1L (PubMed:25066055). {ECO:0000250|UniProtKB:P11151, ECO:0000269|PubMed:17403372, ECO:0000269|PubMed:25066055}. TISSUE SPECIFICITY: Expressed in liver, epididymal fat, heart, psoas muscle, lactating mammary gland, adrenal, lung, and ovary. Highest levels in heart and adrenal gland. {ECO:0000269|PubMed:2723548}. +P59481 LMA2L_MOUSE VIP36-like protein (Lectin mannose-binding 2-like) (LMAN2-like protein) 347 39,881 Binding site (3); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (1); Metal binding (4); Motif (1); Region (2); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 313 335 Helical. {ECO:0000255}. TOPO_DOM 44 312 Lumenal. {ECO:0000255}.; TOPO_DOM 336 347 Cytoplasmic. {ECO:0000255}. FUNCTION: May be involved in the regulation of export from the endoplasmic reticulum of a subset of glycoproteins. May function as a regulator of ERGIC-53 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Predominantly found in the endoplasmic reticulum. Partly found in the Golgi. {ECO:0000250}. +Q02566 MYH6_MOUSE Myosin-6 (Myosin heavy chain 6) (Myosin heavy chain, cardiac muscle alpha isoform) (MyHC-alpha) 1938 223,565 Chain (1); Coiled coil (1); Domain (3); Modified residue (14); Natural variant (3); Nucleotide binding (1); Region (4) FUNCTION: Muscle contraction. SUBCELLULAR LOCATION: Cytoplasm, myofibril. Note=Thick filaments of the myofibrils. SUBUNIT: Muscle myosin is a hexameric protein that consists of 2 heavy chain subunits (MHC), 2 alkali light chain subunits (MLC) and 2 regulatory light chain subunits (MLC-2). DOMAIN: The rodlike tail sequence is highly repetitive, showing cycles of a 28-residue repeat pattern composed of 4 heptapeptides, characteristic for alpha-helical coiled coils.; DOMAIN: Limited proteolysis of myosin heavy chain produces 1 light meromyosin (LMM) and 1 heavy meromyosin (HMM). HMM can be further cleaved into 2 globular subfragments (S1) and 1 rod-shaped subfragment (S2). {ECO:0000305}. +Q922Q8 LRC59_MOUSE Leucine-rich repeat-containing protein 59 [Cleaved into: Leucine-rich repeat-containing protein 59, N-terminally processed] 307 34,877 Chain (2); Coiled coil (1); Compositional bias (1); Erroneous initiation (4); Initiator methionine (1); Modified residue (6); Repeat (5); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 245 265 Helical. {ECO:0000255}. TOPO_DOM 2 244 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 266 307 Lumenal. {ECO:0000255}. FUNCTION: Required for nuclear import of FGF1, but not that of FGF2. Might regulate nuclear import of exogenous FGF1 by facilitating interaction with the nuclear import machinery and by transporting cytosolic FGF1 to, and possibly through, the nuclear pores (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Nucleus envelope {ECO:0000250}. Note=Localization in the nuclear envelope depends upon the nuclear import machinery, including KPNB1. {ECO:0000250}. SUBUNIT: Can form homodimers. Interacts with SGO1. Interacts with FGF1. {ECO:0000250}. +Q9D9Q0 LRC69_MOUSE Leucine-rich repeat-containing protein 69 347 40,066 Chain (1); Repeat (9) +Q80ZI6 LRSM1_MOUSE E3 ubiquitin-protein ligase LRSAM1 (EC 2.3.2.27) (Leucine-rich repeat and sterile alpha motif-containing protein 1) (RING-type E3 ubiquitin transferase LRSAM1) (Tsg101-associated ligase) 727 83,976 Chain (1); Coiled coil (2); Domain (1); Modified residue (2); Motif (2); Repeat (6); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that mediates monoubiquitination of TSG101 at multiple sites, leading to inactivate the ability of TSG101 to sort endocytic (EGF receptors) and exocytic (viral proteins) cargos (By similarity). Bacterial recognition protein that defends the cytoplasm from invasive pathogens (By similarity). Localizes to several intracellular bacterial pathogens and generates the bacteria-associated ubiquitin signal leading to autophagy-mediated intracellular bacteria degradation (xenophagy) (By similarity). {ECO:0000250|UniProtKB:Q6UWE0}. PTM: Ubiquitination promoted by PHF23 leads to proteasomal degradation. {ECO:0000250|UniProtKB:Q6UWE0}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6UWE0}. Note=Displays a punctuate distribution and localizes to a submembranal ring (PubMed:15256501). Localizes to intracellular bacterial pathogens (By similarity). {ECO:0000250|UniProtKB:Q6UWE0}. SUBUNIT: Interacts with TSG101. Interacts with PHF23. Interacts with FUS. {ECO:0000250|UniProtKB:Q6UWE0}. DOMAIN: The coiled coil domains interact with the SB domain of TSG101. {ECO:0000250|UniProtKB:Q6UWE0}.; DOMAIN: The PTAP motifs mediate the binding to UEV domains. {ECO:0000250|UniProtKB:Q6UWE0}.; DOMAIN: The LRR domain is necessary and sufficient for localization to bacterial targets. {ECO:0000250|UniProtKB:Q6UWE0}.; DOMAIN: The RING domain is required for ubiquitination. {ECO:0000250|UniProtKB:Q6UWE0}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15256501}. +Q6NSQ7 LTV1_MOUSE Protein LTV1 homolog 470 54,023 Chain (1); Coiled coil (1); Compositional bias (1); Modified residue (5); Sequence conflict (2) +Q9CQ33 LZTR1_MOUSE Leucine-zipper-like transcriptional regulator 1 (LZTR-1) 837 94,476 Alternative sequence (1); Chain (1); Domain (2); Erroneous initiation (1); Initiator methionine (1); Modified residue (1); Repeat (6); Sequence conflict (5) FUNCTION: Probable transcriptional regulator that may play a crucial role in embryogenesis. {ECO:0000250}. +Q91ZJ0 MUS81_MOUSE Crossover junction endonuclease MUS81 (EC 3.1.22.-) 551 61,531 Chain (1); Domain (1); Helix (4); Modified residue (1); Region (1); Sequence conflict (5); Turn (1) FUNCTION: Interacts with EME1 and EME2 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of stalled or collapsed replication forks. {ECO:0000269|PubMed:14609959, ECO:0000269|PubMed:15205536, ECO:0000269|PubMed:16107704}. SUBCELLULAR LOCATION: Nucleus, nucleolus. Note=Recruited to foci of DNA damage in S-phase cells. {ECO:0000250}. SUBUNIT: May self-associate. Interacts with CHEK2. Interacts with BLM, and this interaction may stimulate the endonuclease activity of MUS81. Interacts with EME2. Interacts with SLX4/BTBD12; this interaction is direct and links the MUS81-EME1 complex to SLX4, which may coordinate the action of the structure-specific endonuclease during DNA repair. Interacts with DCLRE1B/Apollo (By similarity). Interacts with EME1. {ECO:0000250, ECO:0000269|PubMed:14609959}. TISSUE SPECIFICITY: Expressed highly in testis. Expressed also in bone marrow, brain, thymus and to a lesser extent in heart and skeletal muscle, colon, kidney and spleen. {ECO:0000269|PubMed:27010503}. +Q3UHK1 MYCT_MOUSE Proton myo-inositol cotransporter (H(+)-myo-inositol cotransporter) (Hmit) (H(+)-myo-inositol symporter) (Solute carrier family 2 member 13) 637 69,062 Chain (1); Erroneous initiation (1); Glycosylation (3); Modified residue (5); Topological domain (13); Transmembrane (12) TRANSMEM 66 86 Helical; Name=1. {ECO:0000255}.; TRANSMEM 115 135 Helical; Name=2. {ECO:0000255}.; TRANSMEM 138 158 Helical; Name=3. {ECO:0000255}.; TRANSMEM 168 188 Helical; Name=4. {ECO:0000255}.; TRANSMEM 202 222 Helical; Name=5. {ECO:0000255}.; TRANSMEM 229 249 Helical; Name=6. {ECO:0000255}.; TRANSMEM 314 334 Helical; Name=7. {ECO:0000255}.; TRANSMEM 353 373 Helical; Name=8. {ECO:0000255}.; TRANSMEM 383 403 Helical; Name=9. {ECO:0000255}.; TRANSMEM 498 518 Helical; Name=10. {ECO:0000255}.; TRANSMEM 539 559 Helical; Name=11. {ECO:0000255}.; TRANSMEM 563 583 Helical; Name=12. {ECO:0000255}. TOPO_DOM 1 65 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 87 114 Extracellular. {ECO:0000255}.; TOPO_DOM 136 137 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 159 167 Extracellular. {ECO:0000255}.; TOPO_DOM 189 201 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 223 228 Extracellular. {ECO:0000255}.; TOPO_DOM 250 313 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 335 352 Extracellular. {ECO:0000255}.; TOPO_DOM 374 382 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 404 497 Extracellular. {ECO:0000255}.; TOPO_DOM 519 538 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 560 562 Extracellular. {ECO:0000255}.; TOPO_DOM 584 637 Cytoplasmic. {ECO:0000255}. FUNCTION: H(+)-myo-inositol cotransporter. Can also transport related stereoisomers (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q64331 MYO6_MOUSE Unconventional myosin-VI (Unconventional myosin-6) 1265 146,409 Beta strand (5); Chain (1); Domain (3); Helix (11); Modified residue (5); Natural variant (1); Nucleotide binding (1); Region (6); Turn (2) FUNCTION: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Myosin 6 is a reverse-direction motor protein that moves towards the minus-end of actin filaments. Has slow rate of actin-activated ADP release due to weak ATP binding. Functions in a variety of intracellular processes such as vesicular membrane trafficking and cell migration. Required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway. Appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells. May act as a regulator of F-actin dynamics. May play a role in transporting DAB2 from the plasma membrane to specific cellular targets. Required for structural integrity of inner ear hair cells. PTM: Phosphorylation in the motor domain, induced by EGF, results in translocation of MYO6 from the cell surface to membrane ruffles and affects F-actin dynamics. Phosphorylated in vitro by p21-activated kinase (PAK) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein. Golgi apparatus {ECO:0000250}. Nucleus. Cytoplasm, perinuclear region. Membrane, clathrin-coated pit. Cell projection, ruffle. Cytoplasmic vesicle. Note=Also present in endocyctic vesicles, and membrane ruffles. Translocates from membrane ruffles, endocytic vesicles and cytoplasm to Golgi apparatus, perinuclear membrane and nucleus through induction by p53 and p53-induced DNA damage. Recruited into membrane ruffles from cell surface by EGF-stimulation. Colocalizes with DAB2 in clathrin-coated pits/vesicles. Colocalizes with OPTN at the Golgi complex and in vesicular structures close to the plasma membrane (By similarity). {ECO:0000250}. SUBUNIT: Homodimer; dimerization seems to implicate the unfolding of the three-helix bundle region creating an additional calmodulin binding site, and cargo binding (By similarity). Binding to calmodulin through a unique insert, not found in other myosins, located in the neck region between the motor domain and the IQ domain appears to contribute to the directionality reversal. This interaction occurs only if the C-terminal lobe of calmodulin is occupied by calcium. Interaction with F-actin/ACTN1 occurs only at the apical brush border domain of the proximal tubule cells (By similarity). Interacts with DAB2. In vitro, the C-terminal globular tail binds a C-terminal region of DAB2. Interacts with CFTR. Forms a complex with CFTR and DAB2 in the apical membrane of epithelial cells. Interacts with OPTN (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q29122}. DOMAIN: Divided into three regions: a N-terminal motor (head) domain, followed by a neck domain consisting of a calmodulin-binding linker domain and a single IQ motif, and a C-terminal tail region with a three-helix bundle region, a SAH domain and a unique globular domain required for interaction with other proteins such as cargo-binding. {ECO:0000305}.; DOMAIN: The SAH (single alpha-helix) region is characterized by a high content of charged residues which are predicted to stabilize the alpha-helical structure by ionic bonds. Its contribution to the mechanism confering the myosin movement on actin filaments is debated. {ECO:0000250|UniProtKB:Q29122, ECO:0000250|UniProtKB:Q9UM54}. TISSUE SPECIFICITY: Widely expressed. Within the cochlea, expressed specifically within the sensory hair cells. DISEASE: Note=Defects in Myo6 are the cause of Snell's waltzer, a condition characterized by circling, head-tossing, deafness and hyperactivity. +Q8K3I4 MYRIP_MOUSE Rab effector MyRIP (Exophilin-8) (Myosin-VIIa- and Rab-interacting protein) (Synaptotagmin-like protein lacking C2 domains C) (SlaC2-c) (Slp homolog lacking C2 domains c) 856 94,924 Chain (1); Domain (1); Modified residue (2); Mutagenesis (4); Region (4); Sequence conflict (7); Zinc finger (1) FUNCTION: Rab effector protein involved in melanosome transport. Serves as link between melanosome-bound RAB27A and the motor proteins MYO5A and MYO7A. May link RAB27A-containing vesicles to actin filaments. Functions as a protein kinase A-anchoring protein (AKAP). May act as a scaffolding protein that links PKA to components of the exocytosis machinery, thus facilitating exocytosis, including insulin release. {ECO:0000269|PubMed:17827149}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12221080}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q7TNY7}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniProtKB:Q7TNY7}. Melanosome {ECO:0000269|PubMed:11964381, ECO:0000269|PubMed:12221080}. Note=In presynaptic and postsynaptic areas in photoreceptor cells and in the basal microvilli of retinal pigment epithelium cells. Associated with melanosomes. Colocalizes with actin filaments. In insulin-secreting cells, associated with dense core secretory granules. {ECO:0000269|PubMed:11964381, ECO:0000269|PubMed:12221080}. SUBUNIT: Binds RAB27A that has been activated by GTP-binding via its N-terminus. Binds MYO5A, MYO7A and F-actin. Interacts with PRKAR2A. Interacts with components of the exocyst complex, including EXOC3 and EXOC4. {ECO:0000269|PubMed:12221080, ECO:0000269|PubMed:17827149}. TISSUE SPECIFICITY: Detected in brain, skin, heart, lung, adrenal medulla, pancreas, intestine, liver, kidney, skeletal muscle and testis. Detected in cochlear and vestibular hair cells in the inner ear, and in photoreceptor and pigment epithelium cells in the retina. {ECO:0000269|PubMed:11964381, ECO:0000269|PubMed:12221080}. +P15375 MYF6_MOUSE Myogenic factor 6 (Myf-6) (Herculin) (Muscle-specific regulatory factor 4) 242 26,987 Chain (1); Domain (1) FUNCTION: Involved in muscle differentiation (myogenic factor). Induces fibroblasts to differentiate into myoblasts. Probable sequence specific DNA-binding protein. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Efficient DNA binding requires dimerization with another bHLH protein. Interacts with CSRP3. {ECO:0000250|UniProtKB:P19335}. TISSUE SPECIFICITY: Skeletal muscle. +Q5SV80 MYO19_MOUSE Unconventional myosin-XIX (Myosin head domain-containing protein 1) 963 108,075 Alternative sequence (2); Chain (1); Domain (3); Nucleotide binding (1); Region (2); Sequence conflict (3) FUNCTION: Actin-based motor molecule with ATPase activity that localizes to the mitochondrion outer membrane (PubMed:24825904). Motor protein that moves towards the plus-end of actin filaments (PubMed:24825904). Required for mitochondrial inheritance during mitosis (By similarity). May be involved in mitochondrial transport or positioning (By similarity). {ECO:0000250|UniProtKB:Q96H55, ECO:0000269|PubMed:24825904}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q96H55}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q96H55}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q96H55}. SUBUNIT: Myosin is a hexamer of 2 heavy chains and 4 light chains: interacts with myosin light chains MYL9 and MYL12B. {ECO:0000269|PubMed:24825904}. DOMAIN: The MyMOMA (MYO19-specific mitochondrial outer membrane-association) region mediates association with the mitochondrion outer membrane via electrostatic interaction. {ECO:0000250|UniProtKB:Q96H55}. +P97479 MYO7A_MOUSE Unconventional myosin-VIIa 2215 254,939 Alternative sequence (1); Beta strand (19); Chain (1); Domain (11); Helix (28); Modified residue (3); Mutagenesis (2); Natural variant (2); Nucleotide binding (1); Region (2); Sequence conflict (5); Turn (6) FUNCTION: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails bind to membranous compartments, which are then moved relative to actin filaments. In the retina, plays an important role in the renewal of the outer photoreceptor disks. Plays an important role in the distribution and migration of retinal pigment epithelial (RPE) melanosomes and phagosomes, and in the regulation of opsin transport in retinal photoreceptors. Mediates intracellular transport of RPE65 in the retina pigment epithelium. In the inner ear, plays an important role in differentiation, morphogenesis and organization of cochlear hair cell bundles. Motor protein that is a part of the functional network formed by USH1C, USH1G, CDH23 and MYO7A that mediates mechanotransduction in cochlear hair cells. Required for normal hearing. Involved in hair-cell vesicle trafficking of aminoglycosides, which are known to induce ototoxicity. {ECO:0000269|PubMed:21493626, ECO:0000269|PubMed:21709241, ECO:0000269|PubMed:27525485}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21709241}. Cytoplasm, cell cortex {ECO:0000269|PubMed:21709241}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:21709241}. Note=In the photoreceptor cells, mainly localized in the inner and base of outer segments as well as in the synaptic ending region (By similarity). In retinal pigment epithelial cells colocalizes with a subset of melanosomes, displays predominant localization to stress fiber-like structures and some localization to cytoplasmic puncta (By similarity). Detected at the tip of cochlear hair cell stereocilia (PubMed:27525485). The complex formed by MYO7A, USH1C and USH1G colocalizes with F-actin (By similarity). {ECO:0000250|UniProtKB:Q13402, ECO:0000269|PubMed:27525485}. SUBUNIT: Might homodimerize in a two headed molecule through the formation of a coiled-coil rod (By similarity). Identified in a complex with USH1C and USH1G (By similarity). Interacts with MYRIP (PubMed:12221080). Interacts with RPE65 (PubMed:21493626). Interacts with CIB2 (By similarity). May interact with CALM (By similarity). Interacts with WHRN (PubMed:15590698). Interacts with PLEKHB1 (via PH domain) (PubMed:15976448). Interacts with PCDH15 (PubMed:16481439). Interacts with TWF2 (PubMed:19774077). Interacts with USH1G (PubMed:21311020). Interacts with MYH9 (PubMed:27331610). Interacts (via MyTH4-FERM domains) with cytoplasmic regions of ADGRV1 and USH2A (PubMed:17567809). Interacts with PDZD7 (via MyTH4-FERM domains) (PubMed:27525485). {ECO:0000250, ECO:0000250|UniProtKB:Q13402, ECO:0000269|PubMed:12221080, ECO:0000269|PubMed:15590698, ECO:0000269|PubMed:15976448, ECO:0000269|PubMed:16481439, ECO:0000269|PubMed:17567809, ECO:0000269|PubMed:19774077, ECO:0000269|PubMed:21311020, ECO:0000269|PubMed:21493626, ECO:0000269|PubMed:27331610, ECO:0000269|PubMed:27525485}. DOMAIN: The SAH (single alpha-helix) region is characterized by a high content of charged residues which are predicted to stabilize the alpha-helical structure by ionic bonds. {ECO:0000250|UniProtKB:Q13402}. TISSUE SPECIFICITY: Detected in mechanosensory stereocilia of cochlea hair cells (at protein level). Expressed in the retina, cochlea, kidney and liver. {ECO:0000269|PubMed:15654330, ECO:0000269|PubMed:21493626, ECO:0000269|PubMed:21709241}. DISEASE: Note=Defects in Myo7a are the cause of the shaker-1 (sh-1) phenotype which affects only the inner ear. Sh-1 homozygote mutants show hyperactivity, head tossing and circling due to vestibular dysfunction, together with typical neuroepithelial-type cochlear defects involving dysfunction and progressive degeneration of the organ of Corti. {ECO:0000269|PubMed:7870172}. +Q9WTI7 MYO1C_MOUSE Unconventional myosin-Ic (Myosin I beta) (MMI-beta) (MMIb) 1063 121,944 Alternative sequence (3); Binding site (2); Chain (1); Domain (4); Modified residue (8); Mutagenesis (2); Nucleotide binding (2); Region (1); Sequence conflict (17) FUNCTION: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails bind to membranous compartments, which then are moved relative to actin filaments. Involved in glucose transporter recycling in response to insulin by regulating movement of intracellular GLUT4-containing vesicles to the plasma membrane. Component of the hair cell's (the sensory cells of the inner ear) adaptation-motor complex. Acts as a mediator of adaptation of mechanoelectrical transduction in stereocilia of vestibular hair cells. Binds phosphoinositides and links the actin cytoskeleton to cellular membranes. {ECO:0000269|PubMed:16971510}.; FUNCTION: Isoform 3 is involved in regulation of transcription. Associated with transcriptional active ribosomal genes. Appears to cooperate with the WICH chromatin-remodeling complex to facilitate transcription. Necessary for the formation of the first phosphodiester bond during transcription initiation. PTM: Isoform 2 contains a N-acetylmethionine at position 1. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection, stereocilium membrane. Cytoplasmic vesicle. Cell projection, ruffle. Note=Colocalizes with CABP1 and CIB1 at cell margin, membrane ruffles and punctate regions on the cell membrane. Colocalizes in adipocytes with GLUT4 at actin-based membranes. Colocalizes with GLUT4 at insulin-induced ruffles at the cell membrane. Localizes transiently at cell membrane to region known to be enriched in PIP2. Activation of phospholipase C results in its redistribution to the cytoplasm.; SUBCELLULAR LOCATION: Isoform 3: Nucleus, nucleolus. Nucleus, nucleoplasm {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250}. Note=In the nucleolus, is localized predominantly in dense fibrillar component (DFC) and in granular component (GC). Accumulates strongly in DFC and GC during activation of transcription. Colocalizes with transcription sites. Colocalizes in the granular cortex at the periphery of the nucleolus with RPS6. Colocalizes in nucleoplasm with RPS6 and actin that are in contact with RNP particles. Colocalizes with RPS6 at the nuclear pore level (By similarity). Colocalizes with RNA polymerase II in the nucleus. Colocalizes with RNA polymerase I in nucleoli. {ECO:0000250}. SUBUNIT: Interacts (via its IQ motifs) with CALM; this precludes interaction with YWHAB. Interacts with YWHAB; this precludes interaction with CALM. Interacts with RPS6 (By similarity). Interacts with actin filaments. Interacts (via its IQ motifs) with CABP1 and CIB1; the interaction with CABP1 and CIB1 is calcium-dependent. Interacts (via tail domain) with PLEKHB1 (via PH domain); the interaction is not affected by the presence or absence of calcium and CALM. Interacts with POLR1A and POLR2A. Component of the B-WICH complex, at least composed of SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21. Interacts with GLUT4. Interacts with LLPH (PubMed:26961175). {ECO:0000250, ECO:0000269|PubMed:11030652, ECO:0000269|PubMed:15976448, ECO:0000269|PubMed:16514417, ECO:0000269|PubMed:16960872, ECO:0000269|PubMed:17994197, ECO:0000269|PubMed:22918957, ECO:0000269|PubMed:26961175}. DOMAIN: Binds directly to large unilamellar vesicles (LUVs) containing phosphatidylinositol 4,5-bisphosphate (PIP2) or inositol 1,4,5-trisphosphate (InsP3). The PIP2-binding site corresponds to the myosin tail domain (PH-like) present in its tail domain. {ECO:0000269|PubMed:16971510}. TISSUE SPECIFICITY: Isoform 3 is expressed in small intestine, pancreas, brain, kidney, skin, heart muscle, testis, striated muscle, spleen, liver and lung (at protein level). Expressed in brain, testis, adrenal glands, thymus, spleen, kidney, lung, heart, cochlea and vestibule. Expressed in sensory hair cells of the inner ear. Expressed in adipocytes. {ECO:0000269|PubMed:12490950, ECO:0000269|PubMed:16102537, ECO:0000269|PubMed:16957816, ECO:0000269|PubMed:9119401}. +Q5SYD0 MYO1D_MOUSE Unconventional myosin-Id 1006 116,081 Alternative sequence (2); Chain (1); Domain (4); Frameshift (1); Initiator methionine (1); Modified residue (3); Nucleotide binding (1); Region (1) FUNCTION: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments (By similarity). {ECO:0000250|UniProtKB:P97479}. SUBUNIT: Binds calmodulin through its IQ motifs. {ECO:0000250|UniProtKB:Q63357}. +Q69ZQ1 MYORG_MOUSE Myogenesis-regulating glycosidase (EC 3.2.1.-) (Nuclear envelope transmembrane protein 37) (Uncharacterized family 31 glucosidase KIAA1161) 716 81,362 Active site (3); Chain (1); Erroneous initiation (1); Glycosylation (3); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 56 76 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 55 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 77 716 Extracellular. {ECO:0000255}. FUNCTION: Putative glycosidase. Promotes myogenesis by activating AKT signaling through the maturation and secretion of IGF2 (PubMed:19706595). {ECO:0000269|PubMed:19706595}. SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:17062158, ECO:0000269|PubMed:19706595}; Single-pass type II membrane protein {ECO:0000269|PubMed:19706595}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:19706595}; Single-pass type II membrane protein {ECO:0000269|PubMed:19706595}. Note=Only a minor fraction is present in the peripheral endoplasmic reticulum (PubMed:19706595). {ECO:0000269|PubMed:19706595}. SUBUNIT: Interacts with IGF2; this interaction is required for IGF2 secretion (PubMed:19706595). {ECO:0000269|PubMed:19706595}. TISSUE SPECIFICITY: Highly expressed in skeletal muscle (at protein level) (PubMed:19706595). {ECO:0000269|PubMed:19706595}. +Q9JIF9 MYOTI_MOUSE Myotilin (Myofibrillar titin-like Ig domains protein) (Titin immunoglobulin domain protein) 496 55,316 Chain (1); Domain (2); Modified residue (1); Region (3) FUNCTION: Component of a complex of multiple actin cross-linking proteins. Involved in the control of myofibril assembly and stability at the Z lines in muscle cells (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000250|UniProtKB:Q9UBF9}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9UBF9}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:Q9UBF9}. Note=Sarcomeric, also localized to the sarcolemma. Colocalizes with MYOZ1 at the Z-lines in skeletal muscle. {ECO:0000250|UniProtKB:Q9UBF9}. SUBUNIT: Homodimer. Interacts with ACTA1, ACTN1, FLNA, FLNB, FLNC, and MYOZ2. Interacts with the C-terminal region of MYOZ1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in skeletal muscle (at protein level). {ECO:0000269|PubMed:17074808}. +Q6PFD7 NAIF1_MOUSE Nuclear apoptosis-inducing factor 1 327 35,152 Chain (1); Compositional bias (1); Region (1) FUNCTION: Induces apoptosis. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with HARBI1. {ECO:0000250}. +E9Q5R7 NAL12_MOUSE NACHT, LRR and PYD domains-containing protein 12 (Monarch-1) (PYRIN-containing APAF1-like protein 7) (PYPAF7) 1054 119,319 Chain (1); Domain (2); Nucleotide binding (1); Repeat (8) FUNCTION: May mediate activation of CASP1 via ASC and promote activation of NF-kappa-B via IKK. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Binds to ASC with its pyrin domain. Interacts with FAF1 UBA domain via its pyrin domain (By similarity). {ECO:0000250}. +Q6B966 NAL14_MOUSE NACHT, LRR and PYD domains-containing protein 14 (NALP-iota) (Germ cell specific leucine-rich repeat NTPase) 993 113,386 Chain (1); Domain (1); Erroneous initiation (1); Nucleotide binding (1); Repeat (9); Sequence conflict (2) FUNCTION: May be involved in inflammation and spermatogenesis. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15590904}. TISSUE SPECIFICITY: Detected in adult ovary and testis. Detected in oocytes and in germ cell elements in seminiferous tubules in adult testis (at protein level). {ECO:0000269|PubMed:15590904}. +Q8C6J9 NAL4B_MOUSE NACHT, LRR and PYD domains-containing protein 4B (NALP-gamma) 863 99,955 Chain (1); Domain (2); Nucleotide binding (1); Repeat (7); Sequence conflict (2) FUNCTION: May be involved in inflammation and recognition of cytosolic pathogen-associated molecular patterns (PAMPs) not intercepted by membrane-bound receptors. {ECO:0000250}. +Q66X19 NAL4E_MOUSE NACHT, LRR and PYD domains-containing protein 4E (NALP-epsilon) 978 112,473 Chain (1); Domain (2); Nucleotide binding (1); Repeat (6); Sequence conflict (2) FUNCTION: May be involved in inflammation and recognition of cytosolic pathogen-associated molecular patterns (PAMPs) not intercepted by membrane-bound receptors. {ECO:0000250}. +Q9R1M5 NALP5_MOUSE NACHT, LRR and PYD domains-containing protein 5 (Maternal antigen that embryos require) (Mater protein) (Ooplasm-specific protein 1) (OP1) 1163 131,318 Alternative sequence (8); Chain (1); Domain (1); Natural variant (8); Nucleotide binding (1); Repeat (11); Sequence conflict (1) FUNCTION: As a member of the subcortical maternal complex (SCMC), plays an essential role for zygotes to progress beyond the first embryonic cell divisions. {ECO:0000269|PubMed:11062459, ECO:0000269|PubMed:18804437}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14670992}. Nucleus, nucleolus {ECO:0000269|PubMed:14670992}. Cytoplasm {ECO:0000269|PubMed:14670992}. Note=Located in mitochondria and nucleoli in primary follicle oocytes. Not detected in oocyte mitochondria in type 2 follicles. In the subcortical cytoplasm of early embryos from the 1-cell to the blastocyst stages. From the 2-cell stage, still detected in the subcortex, but excluded from cell-cell contact regions. SUBUNIT: Component of the SCMC which also includes KHDC3, OOEP and TLE6. Within the complex, interacts with KHDC3. {ECO:0000269|PubMed:18804437}. TISSUE SPECIFICITY: Oocyte-specific. {ECO:0000269|PubMed:10433232}. +Q9CRA0 NAR4_MOUSE Ecto-ADP-ribosyltransferase 4 (EC 2.4.2.31) (ADP-ribosyltransferase C2 and C3 toxin-like 4) (ARTC4) (Mono(ADP-ribosyl)transferase 4) (NAD(P)(+)--arginine ADP-ribosyltransferase 4) (CD antigen CD297) 300 33,080 Active site (1); Binding site (2); Chain (1); Disulfide bond (2); Glycosylation (4); Lipidation (1); Propeptide (1); Sequence conflict (7); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 270 286 Helical. {ECO:0000255}. TOPO_DOM 24 269 Extracellular. {ECO:0000255}.; TOPO_DOM 287 300 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. +P70352 NAR5_MOUSE Ecto-ADP-ribosyltransferase 5 (EC 2.4.2.31) (ADP-ribosyltransferase C2 and C3 toxin-like 5) (ARTC5) (Mono(ADP-ribosyl)transferase 5) (NAD(P)(+)--arginine ADP-ribosyltransferase 5) (YAC-2) 309 34,333 Active site (1); Alternative sequence (4); Binding site (4); Chain (1); Disulfide bond (1); Glycosylation (2); Sequence conflict (8); Signal peptide (1) SUBCELLULAR LOCATION: Secreted. Membrane. Note=Membrane-associated. TISSUE SPECIFICITY: Abundantly expressed in testis. Lower levels in cardiac and skeletal muscle. +Q3UG98 NAT9_MOUSE N-acetyltransferase 9 (EC 2.3.1.-) 241 27,663 Chain (1); Domain (1); Frameshift (1); Sequence conflict (2) +Q91WV0 NC2B_MOUSE Protein Dr1 (Down-regulator of transcription 1) (Negative cofactor 2-beta) (NC2-beta) (TATA-binding protein-associated phosphoprotein) 176 19,431 Chain (1); Compositional bias (1); Domain (1); Initiator methionine (1); Modified residue (5); Motif (1) FUNCTION: The association of the DR1/DRAP1 heterodimer with TBP results in a functional repression of both activated and basal transcription of class II genes. This interaction precludes the formation of a transcription-competent complex by inhibiting the association of TFIIA and/or TFIIB with TBP. Can bind to DNA on its own. Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4 (By similarity). {ECO:0000250}. PTM: Phosphorylation regulates its interaction with TBP. Not phosphorylated when bound to DRAP1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Heterodimer with DRAP1. DR1 exists in solution as a homotetramer that dissociates during interaction with TBP and then, after complexing with TBP, reassociates at a slow rate, to reconstitute the tetramer. Interacts with NFIL3. Component of the ADA2A-containing complex (ATAC), composed of KAT14, KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1 (By similarity). {ECO:0000250}. +Q9JMH9 MY18A_MOUSE Unconventional myosin-XVIIIa (Molecule associated with JAK3 N-terminus) (MAJN) (Myosin containing a PDZ domain) (Surfactant protein receptor SP-R210) (SP-R210) 2050 232,755 Alternative sequence (6); Chain (1); Coiled coil (1); Compositional bias (1); Domain (4); Modified residue (34); Motif (1); Mutagenesis (1); Nucleotide binding (1); Region (1); Sequence conflict (10) FUNCTION: May link Golgi membranes to the cytoskeleton and participate in the tensile force required for vesicle budding from the Golgi. Thereby, may play a role in Golgi membrane trafficking and could indirectly give its flattened shape to the Golgi apparatus (PubMed:19837035). Alternatively, in concert with LURAP1 and CDC42BPA/CDC42BPB, has been involved in modulating lamellar actomyosin retrograde flow that is crucial to cell protrusion and migration (By similarity). May be involved in the maintenance of the stromal cell architectures required for cell to cell contact (PubMed:10733906). Regulates trafficking, expression, and activation of innate immune receptors on macrophages. Plays a role to suppress inflammatory responsiveness of macrophages via a mechanism that modulates CD14 trafficking (PubMed:25965346). Acts as a receptor of surfactant-associated protein A (SFTPA1/SP-A) and plays an important role in internalization and clearance of SFTPA1-opsonized S.aureus by alveolar macrophages (PubMed:21123169). Strongly enhances natural killer cell cytotoxicity (By similarity). {ECO:0000250|UniProtKB:Q92614, ECO:0000269|PubMed:10733906, ECO:0000269|PubMed:19837035, ECO:0000269|PubMed:21123169, ECO:0000269|PubMed:25965346}. PTM: Phosphorylated on tyrosine upon CSF1R activation. Isoform 6 is phosphorylated on Ser-340. {ECO:0000269|PubMed:14969583}. SUBCELLULAR LOCATION: Isoform 1: Endoplasmic reticulum-Golgi intermediate compartment. Cytoplasm, cytoskeleton. Note=Colocalizes with actin.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Note=Lacks the PDZ domain. Diffusely localized in the cytoplasm.; SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Note=Recruited to the Golgi apparatus by GOLPH3. {ECO:0000250}. SUBUNIT: Homodimer. Forms a tripartite complex with CDC42BPA/CDC42BPB and LURAP1 with the latter acting as an adapter connecting CDC42BPA/CDC42BPB and MYO18A (By similarity). Binds F-actin; regulated by ADP and GOLPH3 (PubMed:15582604). Interacts with GOLPH3; the interaction is direct and may link Golgi membranes to the actin cytoskeleton (By similarity). Interacts with JAK3 (PubMed:10733938). Interacts with MSR1 and CD14 (By similarity). {ECO:0000250|UniProtKB:Q92614, ECO:0000269|PubMed:10733938, ECO:0000269|PubMed:15582604}. DOMAIN: The myosin motor domain binds ADP and ATP but has no intrinsic ATPase activity. Mediates ADP-dependent binding to actin (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Isoform 1; Expressed ubiquitously. Isoform 2: Specifically expressed in most hematopoietic cells. Isoform 3: Predominantly expressed in alveolar macrophages (PubMed:25965346). {ECO:0000269|PubMed:25965346}. +P04247 MYG_MOUSE Myoglobin 154 17,070 Chain (1); Initiator methionine (1); Metal binding (2); Modified residue (4); Sequence conflict (1) FUNCTION: Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles. +P51960 MYBA_MOUSE Myb-related protein A (A-Myb) (Myb-like protein 1) 751 85,728 Alternative sequence (1); Chain (1); Cross-link (3); DNA binding (3); Domain (3); Modified residue (1); Mutagenesis (1); Natural variant (4); Region (2); Sequence conflict (5) FUNCTION: Transcription factor that specifically recognizes the sequence 5'-YAAC[GT]G-3' (PubMed:7813437, PubMed:23523368). Acts as a master regulator of male meiosis by promoting expression of piRNAs: activates expression of both piRNA precursor RNAs and expression of protein-coding genes involved in piRNA metabolism, such as PIWIL1 (PubMed:21750041, PubMed:23523368). The piRNA metabolic process mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons, which is essential for the germline integrity (PubMed:23523368). {ECO:0000269|PubMed:21750041, ECO:0000269|PubMed:23523368, ECO:0000269|PubMed:7813437}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21750041}. SUBUNIT: Component of the DREAM complex (also named LINC complex) at least composed of E2F4, E2F5, LIN9, LIN37, LIN52, LIN54, MYBL1, MYBL2, RBL1, RBL2, RBBP4, TFDP1 and TFDP2. The complex exists in quiescent cells where it represses cell cycle-dependent genes. It dissociates in S phase when LIN9, LIN37, LIN52 and LIN54 form a subcomplex that binds to MYBL2 (By similarity). {ECO:0000250|UniProtKB:P10243}. TISSUE SPECIFICITY: Predominantly in the testis. Very low levels in the ovaries, spleen and brain. {ECO:0000269|PubMed:7813437, ECO:0000269|PubMed:8084617}. +Q9QZZ4 MYO15_MOUSE Unconventional myosin-XV (Unconventional myosin-15) 3511 395,622 Alternative sequence (2); Chain (1); Coiled coil (1); Domain (7); Natural variant (1); Nucleotide binding (1); Region (3); Sequence conflict (15) FUNCTION: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments (By similarity). Required for the arrangement of stereocilia in mature hair bundles. {ECO:0000250, ECO:0000269|PubMed:14610277, ECO:0000269|PubMed:15654330}. SUBCELLULAR LOCATION: Cell projection, stereocilium {ECO:0000269|PubMed:14610277}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:14610277}. Note=Localizes to stereocilium tips in cochlear and vestibular hair cells. SUBUNIT: Interacts with the third PDZ domain of WHRN which is necessary for localization of WHRN to stereocilium tips. Interacts with FASLG (By similarity). Interacts with EPS8. {ECO:0000250, ECO:0000269|PubMed:15654330, ECO:0000269|PubMed:21236676}. TISSUE SPECIFICITY: In the developing inner ear, expressed in cochlea and vestibular apparatus. Expression appears to be restricted to cochlear neurosensory cells and upper epithelial layer of macula saccula. Also expressed in macula utriculi and cristae ampullaris of the semicircular canals. In adult cochlear hair cells, highest expression in stereocilia and apical body. {ECO:0000269|PubMed:10552926}. DISEASE: Note=Defects in Myo15a are the cause of shaker-2 (sh-2), a condition causing deafness, circling behavior, head tossing and hyperactivity. Auditory hair cells of affected animals have very short stereocilia and a long actin-containing protrusion at their basal end. +Q5SUV5 MYLK4_MOUSE Myosin light chain kinase family member 4 (EC 2.7.11.1) (Sugen kinase 85) (SgK085) 386 43,905 Active site (1); Binding site (1); Chain (1); Domain (1); Modified residue (1); Nucleotide binding (1) +Q62234 MYOM1_MOUSE Myomesin-1 (Myomesin family member 1) (Skelemin) 1667 185,464 Alternative sequence (1); Beta strand (18); Chain (1); Domain (10); Helix (4); Modified residue (5); Sequence conflict (6); Turn (3) FUNCTION: May link the intermediate filament cytoskeleton to the M-disk of the myofibrils in striated muscle. May also contact myosin filaments. Also binds beta-integrins. SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, M line {ECO:0000269|PubMed:18177667, ECO:0000269|PubMed:22562206}. SUBUNIT: Homodimer. Interacts with TTN/titin and PNKD (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed in all striated muscles. Expressed in all fiber types. {ECO:0000269|PubMed:18177667}. +Q9D6A1 MYO1H_MOUSE Unconventional myosin-Ih 958 109,993 Alternative sequence (2); Chain (1); Domain (4); Modified residue (1); Nucleotide binding (1); Region (1) FUNCTION: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in neonatal inner-ear organs. {ECO:0000269|PubMed:12486594}. +Q5SWP3 NACAD_MOUSE NAC-alpha domain-containing protein 1 1504 156,764 Chain (1); Compositional bias (5); Domain (1); Modified residue (2); Sequence conflict (10) FUNCTION: May prevent inappropriate targeting of non-secretory polypeptides to the endoplasmic reticulum (ER). May bind to nascent polypeptide chains as they emerge from the ribosome and block their interaction with the signal recognition particle (SRP), which normally targets nascent secretory peptides to the ER. May also reduce the inherent affinity of ribosomes for protein translocation sites in the ER membrane (M sites) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. +O70624 MYOC_MOUSE Myocilin (Trabecular meshwork-induced glucocorticoid response protein) [Cleaved into: Myocilin, N-terminal fragment (Myocilin 20 kDa N-terminal fragment); Myocilin, C-terminal fragment (Myocilin 35 kDa N-terminal fragment)] 490 55,314 Chain (3); Coiled coil (1); Disulfide bond (1); Domain (1); Glycosylation (1); Helix (1); Metal binding (5); Natural variant (1); Signal peptide (1); Site (1) FUNCTION: Secreted glycoprotein regulating the activation of different signaling pathways in adjacent cells to control different processes including cell adhesion, cell-matrix adhesion, cytoskeleton organization and cell migration. Promotes substrate adhesion, spreading and formation of focal contacts. Negatively regulates cell-matrix adhesion and stress fiber assembly through Rho protein signal transduction. Modulates the organization of actin cytoskeleton by stimulating the formation of stress fibers through interactions with components of Wnt signaling pathways. Promotes cell migration through activation of PTK2 and the downstream phosphatidylinositol 3-kinase signaling (By similarity). Plays a role in bone formation and promotes osteoblast differentiation in a dose-dependent manner through mitogen-activated protein kinase signaling (PubMed:23629661). Mediates myelination in the peripheral nervous system through ERBB2/ERBB3 signaling (PubMed:23897819). Plays a role as a regulator of muscle hypertrophy through the components of dystrophin-associated protein complex (PubMed:22371502). Involved in positive regulation of mitochondrial depolarization. Plays a role in neurite outgrowth. May participate in the obstruction of fluid outflow in the trabecular meshwork (By similarity). {ECO:0000250|UniProtKB:Q99972, ECO:0000269|PubMed:22371502, ECO:0000269|PubMed:23629661, ECO:0000269|PubMed:23897819}. PTM: Palmitoylated. {ECO:0000250|UniProtKB:Q2PT31}.; PTM: Undergoes a calcium-dependent proteolytic cleavage at Gln-212 by CAPN2 in the endoplasmic reticulum. The result is the production of two fragments, one of 35 kDa containing the C-terminal olfactomedin-like domain, and another of 20 kDa containing the N-terminal leucine zipper-like domain (By similarity). {ECO:0000250}.; PTM: Glycosylated. {ECO:0000250|UniProtKB:Q99972}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16392033}. Golgi apparatus {ECO:0000269|PubMed:23629661}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q99972}. Secreted, extracellular space {ECO:0000250|UniProtKB:Q99972}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q99972}. Secreted, exosome {ECO:0000250|UniProtKB:Q99972}. Mitochondrion {ECO:0000250|UniProtKB:Q99972}. Mitochondrion intermembrane space {ECO:0000250|UniProtKB:Q99972}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q99972}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q99972}. Rough endoplasmic reticulum {ECO:0000269|PubMed:23629661}. Cell projection {ECO:0000250|UniProtKB:Q99972}. Cell projection, cilium {ECO:0000250|UniProtKB:Q99972}. Note=Located preferentially in the ciliary rootlet and basal body of the connecting cilium of photoreceptor cells, and in the rough endoplasmic reticulum. It is only imported to mitochondria in the trabecular meshwork. Localizes to the Golgi apparatus in Schlemm's canal endothelial cells. Appears in the extracellular space of trabecular meshwork cells by an unconventional mechanism, likely associated with exosome-like vesicles. Localizes in trabecular meshwork extracellular matrix. {ECO:0000250|UniProtKB:Q99972}.; SUBCELLULAR LOCATION: Myocilin, C-terminal fragment: Secreted {ECO:0000250}.; SUBCELLULAR LOCATION: Myocilin, N-terminal fragment: Endoplasmic reticulum. Note=Remains retained in the endoplasmic reticulum. {ECO:0000250}. SUBUNIT: Homodimer (via N-terminus). Interacts with OLFM3, FN1, NRCAM, GLDN and NFASC. Interacts (via N-terminus) with MYL2. Interacts with SFRP1, FRZB, FZD7, FZD10, FZD1 and WIF1; regulates Wnt signaling. Interacts with SNTA1; regulates muscle hypertrophy (PubMed:22371502). Interacts with ERBB2 and ERBB3; acivates ERBB2-ERBB3 signaling pathway (PubMed:23897819). Interacts with SNCG; affects its secretion and its aggregation (PubMed:16392033). {ECO:0000250|UniProtKB:Q99972, ECO:0000269|PubMed:12019210, ECO:0000269|PubMed:16392033, ECO:0000269|PubMed:19188438, ECO:0000269|PubMed:22371502, ECO:0000269|PubMed:23897819}. TISSUE SPECIFICITY: Expressed in ciliary body, iris, retina, trabecular network and sclera but not in lens or cornea. Also expressed strongly in skeletal muscle and weakly in heart, brain, testis, liver, kidney, thyroid and epididymis. No expression detected in embryo. Expressed in sciatic nerve. {ECO:0000269|PubMed:23897819, ECO:0000269|PubMed:9588210, ECO:0000269|PubMed:9675094, ECO:0000269|PubMed:9680392}. +Q9DBB4 NAA16_MOUSE N-alpha-acetyltransferase 16, NatA auxiliary subunit (NMDA receptor-regulated 1-like protein) (NARG1-like protein) 864 101,284 Chain (1); Compositional bias (1); Repeat (7) FUNCTION: Auxillary subunit of the N-terminal acetyltransferase A (NatA) complex which displays alpha (N-terminal) acetyltransferase activity. {ECO:0000250}. SUBUNIT: Component of the N-terminal acetyltransferase A (NatA) complex composed of NAA10 and NAA16. {ECO:0000250}. TISSUE SPECIFICITY: Highest levels in the kidney and testes. Moderate expression in the liver, thymus and skin. {ECO:0000269|PubMed:12888564}. +P70414 NAC1_MOUSE Sodium/calcium exchanger 1 (Na(+)/Ca(2+)-exchange protein 1) (Solute carrier family 8 member 1) 970 108,035 Chain (1); Compositional bias (3); Domain (2); Glycosylation (2); Metal binding (27); Modified residue (2); Region (1); Repeat (2); Signal peptide (1); Topological domain (11); Transmembrane (10) TRANSMEM 72 92 Helical. {ECO:0000255}.; TRANSMEM 134 154 Helical. {ECO:0000255}.; TRANSMEM 168 188 Helical. {ECO:0000255}.; TRANSMEM 202 222 Helical. {ECO:0000255}.; TRANSMEM 229 249 Helical. {ECO:0000255}.; TRANSMEM 798 818 Helical. {ECO:0000255}.; TRANSMEM 822 842 Helical. {ECO:0000255}.; TRANSMEM 872 892 Helical. {ECO:0000255}.; TRANSMEM 904 924 Helical. {ECO:0000255}.; TRANSMEM 942 962 Helical. {ECO:0000255}. TOPO_DOM 33 71 Extracellular. {ECO:0000255}.; TOPO_DOM 93 133 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 155 167 Extracellular. {ECO:0000255}.; TOPO_DOM 189 201 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 223 228 Extracellular. {ECO:0000255}.; TOPO_DOM 250 797 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 819 821 Extracellular. {ECO:0000255}.; TOPO_DOM 843 871 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 893 903 Extracellular. {ECO:0000255}.; TOPO_DOM 925 941 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 963 970 Extracellular. {ECO:0000255}. FUNCTION: Mediates the exchange of one Ca(2+) ion against three to four Na(+) ions across the cell membrane, and thereby contributes to the regulation of cytoplasmic Ca(2+) levels and Ca(2+)-dependent cellular processes (PubMed:8659820). Contributes to Ca(2+) transport during excitation-contraction coupling in muscle. In a first phase, voltage-gated channels mediate the rapid increase of cytoplasmic Ca(2+) levels due to release of Ca(2+) stores from the endoplasmic reticulum. SLC8A1 mediates the export of Ca(2+) from the cell during the next phase, so that cytoplasmic Ca(2+) levels rapidly return to baseline (PubMed:10967099). Required for normal embryonic heart development and the onset of heart contractions (PubMed:10967099). {ECO:0000269|PubMed:10967099, ECO:0000269|PubMed:8659820, ECO:0000305}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8659820}; Multi-pass membrane protein {ECO:0000305}. DOMAIN: The cytoplasmic Calx-beta domains bind the regulatory Ca(2+). The first Calx-beta domain can bind up to four Ca(2+) ions. The second domain can bind another two Ca(2+) ions that are essential for calcium-regulated ion exchange. {ECO:0000250|UniProtKB:P23685}. TISSUE SPECIFICITY: Detected in heart, kidney and brain (at protein level). {ECO:0000269|PubMed:12781968}. +Q9D7V9 NAAA_MOUSE N-acylethanolamine-hydrolyzing acid amidase (EC 3.5.1.-) (N-acylsphingosine amidohydrolase-like) (ASAH-like protein) [Cleaved into: N-acylethanolamine-hydrolyzing acid amidase subunit alpha; N-acylethanolamine-hydrolyzing acid amidase subunit beta] 362 40,075 Active site (1); Chain (3); Glycosylation (4); Sequence caution (1); Sequence conflict (4); Signal peptide (1) FUNCTION: Degrades bioactive fatty acid amides to their corresponding acids, with a preference for N-palmitoylethanolamine. {ECO:0000250}. PTM: Autoproteolytic cleavage in the acidic lumen of the lysosome activates the enzyme. {ECO:0000250}. SUBCELLULAR LOCATION: Lysosome {ECO:0000250}. SUBUNIT: Heterodimer of an alpha and a beta subunit, non-covalently linked. {ECO:0000250}. +Q9QZ08 NAGK_MOUSE N-acetyl-D-glucosamine kinase (N-acetylglucosamine kinase) (EC 2.7.1.59) (GlcNAc kinase) 343 37,268 Binding site (8); Chain (1); Initiator methionine (1); Modified residue (3); Region (2) Amino-sugar metabolism; N-acetylneuraminate degradation. FUNCTION: Converts endogenous N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, from lysosomal degradation or nutritional sources into GlcNAc 6-phosphate. Involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway. Also has ManNAc kinase activity. {ECO:0000269|PubMed:10824116}. SUBUNIT: Homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10824116}. +Q8BXR5 NALCN_MOUSE Sodium leak channel non-selective protein (Voltage gated channel-like protein 1) 1738 200,441 Alternative sequence (1); Chain (1); Coiled coil (1); Frameshift (1); Sequence conflict (2); Topological domain (25); Transmembrane (24) TRANSMEM 41 61 Helical; Name=S1 of repeat I. {ECO:0000255}.; TRANSMEM 67 87 Helical; Name=S2 of repeat I. {ECO:0000255}.; TRANSMEM 107 127 Helical; Name=S3 of repeat I. {ECO:0000255}.; TRANSMEM 139 158 Helical; Voltage-sensor; Name=S4 of repeat I. {ECO:0000255}.; TRANSMEM 183 203 Helical; Name=S5 of repeat I. {ECO:0000255}.; TRANSMEM 302 322 Helical; Name=S6 of repeat I. {ECO:0000255}.; TRANSMEM 383 403 Helical; Name=S1 of repeat II. {ECO:0000255}.; TRANSMEM 423 443 Helical; Name=S2 of repeat II. {ECO:0000255}.; TRANSMEM 449 468 Helical; Name=S3 of repeat II. {ECO:0000255}.; TRANSMEM 477 500 Helical; Voltage-sensor; Name=S4 of repeat II. {ECO:0000255}.; TRANSMEM 510 530 Helical; Name=S5 of repeat II. {ECO:0000255}.; TRANSMEM 579 599 Helical; Name=S6 of repeat II. {ECO:0000255}.; TRANSMEM 881 901 Helical; Name=S1 of repeat III. {ECO:0000255}.; TRANSMEM 924 944 Helical; Name=S2 of repeat III. {ECO:0000255}.; TRANSMEM 953 973 Helical; Name=S3 of repeat III. {ECO:0000255}.; TRANSMEM 980 997 Helical; Voltage-sensor; Name=S4 of repeat III. {ECO:0000255}.; TRANSMEM 1016 1036 Helical; Name=S5 of repeat III. {ECO:0000255}.; TRANSMEM 1136 1156 Helical; Name=S6 of repeat III. {ECO:0000255}.; TRANSMEM 1210 1227 Helical; Name=S1 of repeat IV. {ECO:0000255}.; TRANSMEM 1236 1256 Helical; Name=S2 of repeat IV. {ECO:0000255}.; TRANSMEM 1278 1298 Helical; Name=S3 of repeat IV. {ECO:0000255}.; TRANSMEM 1300 1316 Helical; Voltage-sensor; Name=S4 of repeat IV. {ECO:0000255}.; TRANSMEM 1336 1356 Helical; Name=S5 of repeat IV. {ECO:0000255}.; TRANSMEM 1427 1447 Helical; Name=S6 of repeat IV. {ECO:0000255}. TOPO_DOM 1 40 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 62 66 Extracellular. {ECO:0000255}.; TOPO_DOM 88 106 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 128 138 Extracellular. {ECO:0000255}.; TOPO_DOM 159 182 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 204 301 Extracellular. {ECO:0000255}.; TOPO_DOM 323 382 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 404 422 Extracellular. {ECO:0000255}.; TOPO_DOM 444 448 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 469 476 Extracellular. {ECO:0000255}.; TOPO_DOM 501 509 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 531 578 Extracellular. {ECO:0000255}.; TOPO_DOM 600 880 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 902 923 Extracellular. {ECO:0000255}.; TOPO_DOM 945 952 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 974 979 Extracellular. {ECO:0000255}.; TOPO_DOM 998 1015 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1037 1135 Extracellular. {ECO:0000255}.; TOPO_DOM 1157 1209 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1228 1235 Extracellular. {ECO:0000255}.; TOPO_DOM 1257 1277 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1299 1299 Extracellular. {ECO:0000255}.; TOPO_DOM 1317 1335 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1357 1426 Extracellular. {ECO:0000255}.; TOPO_DOM 1448 1738 Cytoplasmic. {ECO:0000255}. FUNCTION: Voltage-independent, cation-nonselective channel which is permeable to sodium, potassium and calcium ions (PubMed:17448995). Regulates the resting membrane potential and controls neuronal excitability. Neuropeptides such as neurotensin and substance P (SP) stimulate the firing of action potentials by activating NALCN through a SRC family kinases-dependent pathway (PubMed:19092807). In addition to its baseline activity, NALCN activity is enhanced/modulated by several GPCRs (PubMed:19092807, PubMed:19575010, PubMed:21040849). Required for normal respiratory rhythm and neonatal survival. Involved in systemic osmoregulation by controlling the serum sodium concentration (PubMed:21177381). NALCN is partly responsible for the substance P-induced depolarization and regulation of the intestinal pace-making activity in the interstitial cells of Cajal (PubMed:22508057). Plays a critical role in both maintenance of spontaneous firing of substantia nigra pars reticulata (SNr) neurons and physiological modulation of SNr neuron excitability (PubMed:27177420). {ECO:0000269|PubMed:17448995, ECO:0000269|PubMed:19092807, ECO:0000269|PubMed:19575010, ECO:0000269|PubMed:21177381, ECO:0000269|PubMed:22508057, ECO:0000269|PubMed:27177420}. PTM: Phosphorylated on tyrosine residues. {ECO:0000269|PubMed:19092807}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Interacts with UNC80; required for the NALCN activation/inhibition by GPCRs in neurons (PubMed:21040849, PubMed:19092807). Found in a complex with NALCN, UNC79 and UNC80; UNC80 bridges NALCN to UNC79. Interacts with CHRM3 (PubMed:19575010). {ECO:0000269|PubMed:19092807, ECO:0000269|PubMed:19575010, ECO:0000269|PubMed:21040849}. DOMAIN: Each of the four internal repeats contains five hydrophobic transmembrane segments (S1, S2, S3, S5, S6) and one positively charged transmembrane segment (S4). S4 segments probably represent the voltage-sensor. S4 transmembrane segments lack some of the charged residues (K and R) found at every third position in the S4s of the NaV, CaV, and KV channels. Pore-forming loops (P loops) between S5 and S6 of each domain form an EEKE sodium- ion selectivity filter a mixture between the EEEE found in the CaVs and the DEKA of NaVs. {ECO:0000305}. TISSUE SPECIFICITY: Widely expressed in the brain and spinal cord neurons (PubMed:17448995). Expressed also in pancreatic islet cells (PubMed:19575010). {ECO:0000269|PubMed:17448995, ECO:0000269|PubMed:19575010}. +Q80WY3 NANO1_MOUSE Nanos homolog 1 (NOS-1) 267 28,151 Chain (1); Erroneous initiation (1); Motif (2); Region (1); Sequence conflict (1); Zinc finger (1) FUNCTION: May act as a translational repressor which regulates translation of specific mRNAs by forming a complex with PUM2 that associates with the 3'-UTR of mRNA targets. Capable of interfering with the proadhesive and anti-invasive functions of E-cadherin. Up-regulates the production of MMP14 to promote tumor cell invasion (By similarity). Not essential for normal development. {ECO:0000250, ECO:0000269|PubMed:12834871}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8WY41}. Cytoplasm {ECO:0000250|UniProtKB:Q8WY41}. Note=Colocalizes with SNAPIN and PUM2 in the perinuclear region of germ cells. {ECO:0000250|UniProtKB:Q8WY41}. SUBUNIT: Interacts with PUM2, SNAPIN and CTNNB1. Interacts (via N-terminal region) with CTNND1. Interacts with DDX20 (via N-terminal region) (By similarity). {ECO:0000250}. DOMAIN: The N-terminal region and C-terminal zinc-finger RNA-binding domain are both necessary for interaction with SNAPIN. {ECO:0000250}.; DOMAIN: The Nanos-type zinc finger is composed of two C2HC motifs, each motif binding one molecule of zinc. It is essential for the translation repression activity of the protein. {ECO:0000255|PROSITE-ProRule:PRU00855}. TISSUE SPECIFICITY: Expressed in the oocyte. Transiently expressed in eight-cell embryos. At 12.5 dpc, it is re-expressed in the central nervous system and the expression continues in the adult brain, in which the hippocampal formation is the predominant region. Expressed in the seminiferous tubules of mature testis, but not in the primordial germ cells. {ECO:0000269|PubMed:12834871}. +P60324 NANO3_MOUSE Nanos homolog 3 (NOS-3) 178 19,241 Chain (1); Motif (2); Zinc finger (1) FUNCTION: Plays a role in the maintenance of the undifferentiated state of germ cells regulating the spermatogonia cell cycle and inducing a prolonged transit in G1 phase. Affects cell proliferation probably by repressing translation of specific mRNAs. Maintains the germ cell lineage by suppressing both Bax-dependent and -independent apoptotic pathways. Essential in the early stage embryo to protect the migrating primordial germ cells (PGCs) from apoptosis. {ECO:0000269|PubMed:12947200, ECO:0000269|PubMed:17138666, ECO:0000269|PubMed:18089289, ECO:0000269|PubMed:18436203}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19861488, ECO:0000269|PubMed:21421998}. Cytoplasm {ECO:0000269|PubMed:19861488, ECO:0000269|PubMed:21421998}. Cytoplasm, Stress granule {ECO:0000269|PubMed:19861488}. Cytoplasm, P-body {ECO:0000269|PubMed:19861488}. Note=Co-localizes with PUM2, EIF2S1 and TIAL1 in the stress granules. Co-localizes with DCP1A in the P-body. {ECO:0000269|PubMed:19861488}. SUBUNIT: Binds mRNA from germ cells. Interacts with PUM2. {ECO:0000269|PubMed:18089289}. DOMAIN: The Nanos-type zinc finger is composed of two C2HC motifs, each motif binding one molecule of zinc. It is essential for the translation repression activity of the protein. {ECO:0000255|PROSITE-ProRule:PRU00855}. TISSUE SPECIFICITY: Expressed in undifferentiated spermatogonial cells. {ECO:0000269|PubMed:12947200, ECO:0000269|PubMed:18089289, ECO:0000269|PubMed:19861488}. +Q9CPT3 NANP_MOUSE N-acylneuraminate-9-phosphatase (EC 3.1.3.29) (Haloacid dehalogenase-like hydrolase domain-containing protein 4) (Neu5Ac-9-Pase) 248 27,808 Beta strand (7); Binding site (1); Chain (1); Helix (13); Region (2); Turn (2) Amino-sugar metabolism; N-acetylneuraminate biosynthesis. +Q6A000 MOONR_MOUSE Protein moonraker (MNR) 959 108,875 Chain (1); Coiled coil (1); Erroneous initiation (1); Modified residue (2); Region (1); Sequence conflict (5) FUNCTION: Involved in centriole duplication. Positively regulates CEP63 centrosomal localization. Required for WDR62 centrosomal localization and promotes the centrosomal localization of CDK2. {ECO:0000250|UniProtKB:Q2KHM9}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000250|UniProtKB:Q2KHM9}. SUBUNIT: Interacts with CEP63 and WDR62 (By similarity). Forms a complex with OFD1 and FOPNL/FOR20 (PubMed:26643951). Interacts with PCM1 (PubMed:26643951). {ECO:0000250|UniProtKB:Q2KHM9, ECO:0000269|PubMed:26643951}. +Q52KP5 NXPE4_MOUSE NXPE family member 4 (Protein FAM55D) 543 61,551 Alternative sequence (1); Chain (1); Glycosylation (3); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q3U9N9 MOT10_MOUSE Monocarboxylate transporter 10 (MCT 10) (Aromatic amino acid transporter 1) (Solute carrier family 16 member 10) (T-type amino acid transporter 1) 512 55,320 Alternative sequence (2); Chain (1); Erroneous initiation (1); Modified residue (5); Sequence conflict (1); Topological domain (2); Transmembrane (12) TRANSMEM 64 84 Helical. {ECO:0000255}.; TRANSMEM 112 132 Helical. {ECO:0000255}.; TRANSMEM 142 162 Helical. {ECO:0000255}.; TRANSMEM 169 189 Helical. {ECO:0000255}.; TRANSMEM 202 222 Helical. {ECO:0000255}.; TRANSMEM 233 253 Helical. {ECO:0000255}.; TRANSMEM 292 312 Helical. {ECO:0000255}.; TRANSMEM 327 347 Helical. {ECO:0000255}.; TRANSMEM 363 383 Helical. {ECO:0000255}.; TRANSMEM 385 405 Helical. {ECO:0000255}.; TRANSMEM 417 437 Helical. {ECO:0000255}.; TRANSMEM 449 469 Helical. {ECO:0000255}. TOPO_DOM 1 63 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 470 512 Cytoplasmic. {ECO:0000255}. FUNCTION: Sodium-independent transporter that mediates the uptake of aromatic acids. Can function as a net efflux pathway for aromatic amino acids in the basosolateral epithelial cells. {ECO:0000269|PubMed:16245314}. PTM: Not N-glycosylated. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16245314}; Multi-pass membrane protein {ECO:0000269|PubMed:16245314}. Basolateral cell membrane {ECO:0000269|PubMed:16245314}. Note=Detected in basolateral membrane of kidney proximal tubule starting at he beginning of the proximal tubule epithelium within the glomerular capsule and extending to the S1 and S2 segments. Localizes also to the basolateral membrane of small intestine enterocytes and to sinusoidal side of perivenous hepatocytes. TISSUE SPECIFICITY: Highly expressed in small intestine, particularly in jejunum and ileum, scarcely in colon and substantially in kidney, liver and skeletal muscle. {ECO:0000269|PubMed:16245314}. +Q8VFL5 O1030_MOUSE Olfactory receptor 1030 (Olfactory receptor 196-2) 318 36,382 Chain (1); Disulfide bond (1); Erroneous initiation (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 32 52 Helical; Name=1. {ECO:0000255}.; TRANSMEM 61 81 Helical; Name=2. {ECO:0000255}.; TRANSMEM 106 126 Helical; Name=3. {ECO:0000255}.; TRANSMEM 140 160 Helical; Name=4. {ECO:0000255}.; TRANSMEM 203 223 Helical; Name=5. {ECO:0000255}.; TRANSMEM 244 264 Helical; Name=6. {ECO:0000255}.; TRANSMEM 278 298 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 31 Extracellular. {ECO:0000255}.; TOPO_DOM 53 60 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 82 105 Extracellular. {ECO:0000255}.; TOPO_DOM 127 139 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 161 202 Extracellular. {ECO:0000255}.; TOPO_DOM 224 243 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 265 277 Extracellular. {ECO:0000255}.; TOPO_DOM 299 318 Cytoplasmic. {ECO:0000255}. FUNCTION: Potential odorant receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +P47809 MP2K4_MOUSE Dual specificity mitogen-activated protein kinase kinase 4 (MAP kinase kinase 4) (MAPKK 4) (EC 2.7.12.2) (C-JUN N-terminal kinase kinase 1) (JNK kinase 1) (JNKK 1) (JNK-activating kinase 1) (MAPK/ERK kinase 4) (MEK 4) (SAPK/ERK kinase 1) (SEK1) 397 44,114 Active site (1); Binding site (1); Chain (1); Compositional bias (1); Domain (1); Initiator methionine (1); Modified residue (6); Mutagenesis (1); Nucleotide binding (1); Region (2) FUNCTION: Dual specificity protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. Essential component of the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. With MAP2K7/MKK7, is the one of the only known kinase to directly activate the stress-activated protein kinase/c-Jun N-terminal kinases MAPK8/JNK1, MAPK9/JNK2 and MAPK10/JNK3. MAP2K4/MKK4 and MAP2K7/MKK7 both activate the JNKs by phosphorylation, but they differ in their preference for the phosphorylation site in the Thr-Pro-Tyr motif. MAP2K4 shows preference for phosphorylation of the Tyr residue and MAP2K7/MKK7 for the Thr residue. The phosphorylation of the Thr residue by MAP2K7/MKK7 seems to be the prerequisite for JNK activation at least in response to proinflammatory cytokines, while other stimuli activate both MAP2K4/MKK4 and MAP2K7/MKK7 which synergistically phosphorylate JNKs. MAP2K4 is required for maintaining peripheral lymphoid homeostasis. The MKK/JNK signaling pathway is also involved in mitochondrial death signaling pathway, including the release cytochrome c, leading to apoptosis. Whereas MAP2K7/MKK7 exclusively activates JNKs, MAP2K4/MKK4 additionally activates the p38 MAPKs MAPK11, MAPK12, MAPK13 and MAPK14. {ECO:0000269|PubMed:11390361, ECO:0000269|PubMed:12624093, ECO:0000269|PubMed:7997269, ECO:0000269|PubMed:9620683, ECO:0000269|PubMed:9891090}. PTM: Activated by phosphorylation on Ser-255 and Thr-259 by MAP kinase kinase kinases (MAP3Ks). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9891090}. Nucleus {ECO:0000269|PubMed:9891090}. SUBUNIT: Interacts with SPAG9. Interacts (via its D domain) with its substrates MAPK8/JNK1, MAPK9/JNK2, MAPK10/JNK3, MAPK11 and MAPK14 (By similarity). Interacts (via its DVD domain) with MAP3Ks activators like MAP3K1/MEKK1 and MAP3K11/MLK3. Interacts with ARRB1, ARRB2 and MAPK8IP3/JIP3 (By similarity). {ECO:0000250}. DOMAIN: The DVD domain (residues 362-385) contains a conserved docking site and is found in the mammalian MAP kinase kinases (MAP2Ks). The DVD sites bind to their specific upstream MAP kinase kinase kinases (MAP3Ks) and are essential for activation (By similarity). {ECO:0000250}.; DOMAIN: The D domain (residues 35-50) contains a conserved docking site and is required for the binding to MAPk substrates. TISSUE SPECIFICITY: Strong expression is detected in most of the central nervous system and in liver and thymus during early stages of development. While expression in nervous system increases over time, expression in fetal liver and thymus gradually decreases as embryogenesis proceeds. High level of expression in the central nervous system persists throughout postnatal development and remained at a stable level in adult brain. {ECO:0000269|PubMed:10095085}. +Q07113 MPRI_MOUSE Cation-independent mannose-6-phosphate receptor (CI Man-6-P receptor) (CI-MPR) (M6PR) (300 kDa mannose 6-phosphate receptor) (MPR 300) (Insulin-like growth factor 2 receptor) (Insulin-like growth factor II receptor) (IGF-II receptor) (M6P/IGF2 receptor) (M6P/IGF2R) (CD antigen CD222) 2483 273,815 Chain (1); Disulfide bond (33); Domain (1); Glycosylation (20); Modified residue (5); Repeat (15); Sequence conflict (10); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 2296 2316 Helical. {ECO:0000255}. TOPO_DOM 36 2295 Lumenal. {ECO:0000255}.; TOPO_DOM 2317 2483 Cytoplasmic. {ECO:0000255}. FUNCTION: Acts as a positive regulator of T-cell coactivation, by binding DPP4 (By similarity). Transport of phosphorylated lysosomal enzymes from the Golgi complex and the cell surface to lysosomes. Lysosomal enzymes bearing phosphomannosyl residues bind specifically to mannose-6-phosphate receptors in the Golgi apparatus and the resulting receptor-ligand complex is transported to an acidic prelyosomal compartment where the low pH mediates the dissociation of the complex. This receptor also binds IGF2. {ECO:0000250}. SUBCELLULAR LOCATION: Lysosome membrane; Single-pass type I membrane protein. SUBUNIT: Interacts with DPP4; the interaction is direct. Binds GGA1, GGA2 and GGA3. Binds HA-I and HA-II plasma membrane adapters (By similarity). {ECO:0000250}. DOMAIN: Contains 15 repeating units of approximately 147 AA harboring four disulfide bonds each. The most highly conserved region within the repeat consists of a stretch of 13 AA that contains cysteines at both ends. +P34983 O1537_MOUSE Olfactory receptor 1537 (Odorant receptor K4) (Olfactory receptor 144) (Olfactory receptor 7B) 314 35,267 Chain (1); Sequence conflict (1); Topological domain (8); Transmembrane (7) TRANSMEM 32 52 Helical; Name=1. {ECO:0000255}.; TRANSMEM 69 89 Helical; Name=2. {ECO:0000255}.; TRANSMEM 101 121 Helical; Name=3. {ECO:0000255}.; TRANSMEM 147 167 Helical; Name=4. {ECO:0000255}.; TRANSMEM 185 205 Helical; Name=5. {ECO:0000255}.; TRANSMEM 211 231 Helical; Name=6. {ECO:0000255}.; TRANSMEM 248 268 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 31 Extracellular. {ECO:0000255}.; TOPO_DOM 53 68 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 90 100 Extracellular. {ECO:0000255}.; TOPO_DOM 122 146 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 168 184 Extracellular. {ECO:0000255}.; TOPO_DOM 206 210 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 232 247 Extracellular. {ECO:0000255}.; TOPO_DOM 269 314 Cytoplasmic. {ECO:0000255}. FUNCTION: Odorant receptor. {ECO:0000305}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +P24668 MPRD_MOUSE Cation-dependent mannose-6-phosphate receptor (CD Man-6-P receptor) (CD-MPR) (46 kDa mannose 6-phosphate receptor) (MPR 46) 278 31,172 Chain (1); Glycosylation (5); Modified residue (1); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 187 211 Helical. {ECO:0000255}. TOPO_DOM 22 186 Lumenal. {ECO:0000255}.; TOPO_DOM 212 278 Cytoplasmic. {ECO:0000255}. FUNCTION: Transport of phosphorylated lysosomal enzymes from the Golgi complex and the cell surface to lysosomes. Lysosomal enzymes bearing phosphomannosyl residues bind specifically to mannose-6-phosphate receptors in the Golgi apparatus and the resulting receptor-ligand complex is transported to an acidic prelyosomal compartment where the low pH mediates the dissociation of the complex. SUBCELLULAR LOCATION: Lysosome membrane; Single-pass type I membrane protein. SUBUNIT: Homodimer. Binds GGA1, GGA2 and GGA3 (By similarity). {ECO:0000250}. DOMAIN: The extracellular domain is homologous to the repeating units (of approximately 147 AA) of the cation-independent mannose 6-phosphate receptor. +Q3TEW6 MPZL1_MOUSE Myelin protein zero-like protein 1 (Protein zero-related) 270 29,495 Alternative sequence (1); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (2); Modified residue (7); Motif (2); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 163 183 Helical. {ECO:0000255}. TOPO_DOM 36 162 Extracellular. {ECO:0000255}.; TOPO_DOM 184 270 Cytoplasmic. {ECO:0000255}. FUNCTION: Cell surface receptor, which is involved in signal transduction processes. Recruits PTPN11/SHP-2 to the cell membrane and is a putative substrate of PTPN11/SHP-2. Is a major receptor for concanavalin-A (ConA) and is involved in cellular signaling induced by ConA, which probably includes Src family tyrosine-protein kinases. Isoform 2 seems to have a dominant negative role; it blocks tyrosine phosphorylation of MPZL1 induced by ConA. Isoform 1, but not isoform 2, may be involved in regulation of integrin-mediated cell motility (By similarity). {ECO:0000250}. PTM: Phosphorylated on tyrosine residues upon stimulation with pervanadate and concanavalin-A (ConA). Phosphorylation at Tyr-242 and Tyr-264 is required for interaction with PTPN11/SHP-2. Dephosphorylated by PTPN11/SHP-2 (in vitro) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Interacts with phosphorylated PTPN11/SHP-2. {ECO:0000250}. DOMAIN: Contains 2 copies of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is involved in modulation of cellular responses. The phosphorylated ITIM motif can bind the SH2 domain of several SH2-containing phosphatases. +Q9D159 MRAP_MOUSE Melanocortin-2 receptor accessory protein (Fat cell-specific low molecular weight protein) (Fat tissue-specific low MW protein) 127 14,170 Alternative sequence (2); Chain (1); Modified residue (1); Transmembrane (1) TRANSMEM 38 58 Helical. {ECO:0000255}. FUNCTION: Modulator of melanocortin receptors (MC1R, MC2R, MC3R, MC4R and MC5R). Acts by increasing ligand-sensitivity of melanocortin receptors and enhancing generation of cAMP by the receptors. Required both for MC2R trafficking to the cell surface of adrenal cells and for signaling in response to corticotropin (ACTH). May be involved in the intracellular trafficking pathways in adipocyte cells (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=The formation of antiparallel homo- and heterodimers suggest that N- and C-terminus can both localize in the cytoplasmic and extracellular parts, depending on the context. Upon insulin stimulation, it is redistributed into spotty structures throughout the cytoplasm (By similarity). {ECO:0000250}. SUBUNIT: Homodimer and heterodimer. Forms antiparallel homodimers and heterodimers with MRAP2. Interacts with MC1R, MC2R, MC3R, MC4R and MC5R (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Largely restricted to fat tissues. Predominantly expressed in mouse epididymal (white adipose tissue) and interscapular (brown adipose tissue) fat pads. Expression is weak or absent in lung, spleen, intestine, kidney, heart and skeletal muscle. +Q6DIB4 NOL4L_MOUSE Nucleolar protein 4-like 494 53,912 Chain (1); Compositional bias (1); Modified residue (2) +Q8BM13 NOE2_MOUSE Noelin-2 (Olfactomedin-2) 448 50,720 Chain (1); Coiled coil (2); Disulfide bond (1); Domain (1); Glycosylation (6); Sequence conflict (1); Signal peptide (1) FUNCTION: Involved in transforming growth factor beta (TGF-beta)-induced smooth muscle differentiation (By similarity). TGF-beta induces expression and nuclear translocation of OLFM2 where it binds to SRF, causing its dissociation from the transcriptional repressor HEY2/HERP1 and facilitating binding of SRF to target genes (By similarity). Plays a role in AMPAR complex organization (PubMed:25218043). Is a regulator of vascular smooth-muscle cell (SMC) phenotypic switching, that acts by promoting RUNX2 and inhibiting MYOCD binding to SRF. SMC phenotypic switching is the process through which vascular SMCs undergo transition between a quiescent contractile phenotype and a proliferative synthetic phenotype in response to pathological stimuli. SMC phenotypic plasticity is essential for vascular development and remodeling (By similarity). {ECO:0000250|UniProtKB:O95897, ECO:0000250|UniProtKB:Q568Y7, ECO:0000269|PubMed:25218043}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O95897}. Cell junction, synapse {ECO:0000269|PubMed:25218043, ECO:0000305|PubMed:22632720}. Membrane {ECO:0000269|PubMed:25218043}. Nucleus {ECO:0000250|UniProtKB:O95897}. Cytoplasm {ECO:0000250|UniProtKB:O95897}. Note=Nuclear localization is induced by TGF-beta. {ECO:0000250|UniProtKB:O95897}. SUBUNIT: Peripherally associated with AMPAR complex. AMPAR complex consists of an inner core made of 4 pore-forming GluA/GRIA proteins (GRIA1, GRIA2, GRIA3 and GRIA4) and 4 major auxiliary subunits arranged in a twofold symmetry. One of the two pairs of distinct binding sites is occupied either by CNIH2, CNIH3 or CACNG2, CACNG3. The other harbors CACNG2, CACNG3, CACNG4, CACNG8 or GSG1L. This inner core of AMPAR complex is complemented by outer core constituents binding directly to the GluA/GRIA proteins at sites distinct from the interaction sites of the inner core constituents. Outer core constituents include at least PRRT1, PRRT2, CKAMP44/SHISA9, FRRS1L and NRN1. The proteins of the inner and outer core serve as a platform for other, more peripherally associated AMPAR constituents, including OLFM2. Alone or in combination, these auxiliary subunits control the gating and pharmacology of the AMPAR complex and profoundly impact their biogenesis and protein processing (PubMed:22632720). Interacts with GRIA2 (PubMed:25218043). Interacts with OLFM1 and OLFM3 (By similarity). Interacts with SRF; the interaction promotes dissociation of SRF from the transcriptional repressor HEY2 (By similarity). Interacts with RUNX2 (By similarity). {ECO:0000250|UniProtKB:O95897, ECO:0000250|UniProtKB:Q568Y7, ECO:0000269|PubMed:22632720, ECO:0000269|PubMed:25218043}. TISSUE SPECIFICITY: Expressed in the brain (at protein level) (PubMed:22632720). In the developing eye, first detected at 12 dpc in the retinal pigmented epithelium and preferentially expressed in differentiating retinal ganglion cells between 15 and 18 dpc (PubMed:21228389). In the brain, expression is detected mainly in the olfactory bulb, cortex, piriform cortex, olfactory trabeculae, and inferior and superior colliculus (PubMed:25218043). In the adult eye, expression is detected mainly in retinal ganglion cells (PubMed:25218043). Expressed in carotid arteries (PubMed:28062493). {ECO:0000269|PubMed:21228389, ECO:0000269|PubMed:22632720, ECO:0000269|PubMed:25218043, ECO:0000269|PubMed:28062493}. +Q3TZX8 NOL9_MOUSE Polynucleotide 5'-hydroxyl-kinase NOL9 (EC 2.7.1.-) (Nucleolar protein 9) 714 80,840 Alternative sequence (4); Chain (1); Compositional bias (1); Cross-link (1); Initiator methionine (1); Modified residue (3); Nucleotide binding (1); Sequence caution (1); Sequence conflict (4) FUNCTION: Polynucleotide 5'-kinase involved in rRNA processing. The kinase activity is required for the processing of the 32S precursor into 5.8S and 28S rRNAs, more specifically for the generation of the major 5.8S(S) form. In vitro, has both DNA and RNA 5'-kinase activities. Probably binds RNA (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q5SY16}. Nucleus {ECO:0000269|PubMed:22872859}. Note=Colocalizes with pre-60S rRNP particles. {ECO:0000250}. SUBUNIT: Interacts with PELP1, WDR18 and SENP3. {ECO:0000269|PubMed:22872859}. +O35710 NOCT_MOUSE Nocturnin (EC 3.1.13.4) (Carbon catabolite repression 4-like protein) (Circadian deadenylase NOC) 429 48,301 Active site (3); Alternative sequence (1); Chain (1); Frameshift (1); Metal binding (4); Region (1) FUNCTION: Circadian deadenylase which plays an important role in post-transcriptional regulation of metabolic genes under circadian control. Degrades poly(A) tails of specific target mRNAs leading to their degradation and suppression of translation. Exerts a rhythmic post-transcriptional control of genes necessary for metabolic functions including nutrient absorption, glucose/insulin sensitivity, lipid metabolism, adipogenesis, inflammation and osteogenesis. Plays an important role in favoring adipogenesis over osteoblastogenesis and acts as a key regulator of the adipogenesis/osteogenesis balance. Promotes adipogenesis by activating PPARG transcriptional activity in a deadenylase-independent manner by facilitating its nuclear translocation. Regulates circadian expression of NOS2 in the liver and negatively regulates the circadian expression of IGF1 in the bone. Critical for proper development of early embryos. {ECO:0000269|PubMed:17400819, ECO:0000269|PubMed:20498072, ECO:0000269|PubMed:20685873, ECO:0000269|PubMed:21820310, ECO:0000269|PubMed:22073225, ECO:0000269|PubMed:22082366, ECO:0000269|PubMed:22331129, ECO:0000269|PubMed:23449310}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, perinuclear region. SUBUNIT: Interacts with PPARG. {ECO:0000269|PubMed:20498072}. TISSUE SPECIFICITY: Highly expressed in the differentiated adipocyte (at protein level). Ubiquitous. {ECO:0000269|PubMed:10521507, ECO:0000269|PubMed:11394964, ECO:0000269|PubMed:20392228}. +Q5RJG1 NOL10_MOUSE Nucleolar protein 10 687 80,077 Chain (1); Coiled coil (3); Modified residue (5); Repeat (5) SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. +Q91WW7 PLPL3_MOUSE 1-acylglycerol-3-phosphate O-acyltransferase Pnpla3 (EC 2.3.1.51) (Acylglycerol transacylase) (Adiponutrin) (ADPN) (Calcium-independent phospholipase A2-epsilon) (iPLA2-epsilon) (Lysophosphatidic acid acyltransferase) (Patatin-like phospholipase domain-containing protein 3) (EC 3.1.1.3) 413 45,772 Active site (2); Chain (1); Domain (1); Glycosylation (2); Motif (3); Mutagenesis (1); Topological domain (2); Transmembrane (1) TRANSMEM 43 63 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 42 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 64 413 Lumenal. {ECO:0000255}. Phospholipid metabolism. Glycerolipid metabolism. FUNCTION: Specifically catalyzes coenzyme A (CoA)-dependent acylation of 1-acyl-sn-glycerol 3-phosphate (2-lysophosphatidic acid/LPA) to generate phosphatidic acid (PA), an important metabolic intermediate and precursor for both triglycerides and glycerophospholipids. Does not esterify other lysophospholipids. Acyl donors are long chain (at least C16) fatty acyl-CoAs: arachidonoyl-CoA, linoleoyl-CoA, oleoyl-CoA and at a lesser extent palmitoyl-CoA (PubMed:22560221). Additionally possesses low triacylglycerol lipase and CoA-independent acylglycerol transacylase activities and thus may play a role in acyl-chain remodeling of triglycerides (By similarity). {ECO:0000250|UniProtKB:Q9NST1, ECO:0000269|PubMed:22560221}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11431482, ECO:0000269|PubMed:22560221}; Single-pass membrane protein {ECO:0000269|PubMed:11431482}. Lipid droplet {ECO:0000269|PubMed:22560221}. TISSUE SPECIFICITY: Restricted to adipose tissue. Expressed in inguinal and epididymal white adipose tissues and in interscapular brown adipose tissue (PubMed:11431482). Also expressed in liver in response to high-sucrose diet (PubMed:22560221). {ECO:0000269|PubMed:11431482, ECO:0000269|PubMed:22560221}. +Q3TRM4 PLPL6_MOUSE Neuropathy target esterase (EC 3.1.1.5) (Patatin-like phospholipase domain-containing protein 6) 1355 149,537 Active site (2); Alternative sequence (4); Chain (1); Domain (1); Glycosylation (1); Modified residue (5); Motif (3); Nucleotide binding (3); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 44 64 Helical. {ECO:0000255}. TOPO_DOM 1 43 Lumenal. {ECO:0000255}.; TOPO_DOM 65 1355 Cytoplasmic. {ECO:0000255}. FUNCTION: Phospholipase B that deacylates intracellular phosphatidylcholine (PtdCho), generating glycerophosphocholine (GroPtdCho). This deacylation occurs at both sn-2 and sn-1 positions of PtdCho. Its specific chemical modification by certain organophosphorus (OP) compounds leads to distal axonopathy. {ECO:0000269|PubMed:12640454, ECO:0000269|PubMed:16963094}. PTM: Glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16963094}; Single-pass type I membrane protein {ECO:0000269|PubMed:16963094}; Cytoplasmic side {ECO:0000269|PubMed:16963094}. Note=Anchored to the cytoplasmic face of the endoplasmic reticulum by its amino-terminal transmembrane segment. TISSUE SPECIFICITY: Expressed ubiquitously in brain of young mice. Reaching adulthood, there is a most prominent expression in Purkinje cells, granule cells and pyramidal neurons of the hippocampus and some large neurons in the medulla oblongata, nucleus dentatus and pons. {ECO:0000269|PubMed:10640712}. +O35516 NOTC2_MOUSE Neurogenic locus notch homolog protein 2 (Notch 2) (Motch B) [Cleaved into: Notch 2 extracellular truncation; Notch 2 intracellular domain] 2470 265,327 Alternative sequence (1); Chain (3); Compositional bias (5); Disulfide bond (114); Domain (35); Glycosylation (7); Modified residue (11); Mutagenesis (3); Region (1); Repeat (9); Sequence conflict (4); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 1678 1698 Helical. {ECO:0000255}. TOPO_DOM 26 1677 Extracellular. {ECO:0000255}.; TOPO_DOM 1699 2470 Cytoplasmic. {ECO:0000255}. FUNCTION: Functions as a receptor for membrane-bound ligands Jagged-1 (JAG1), Jagged-2 (JAG2) and Delta-1 (DLL1) to regulate cell-fate determination (PubMed:10393120). Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus (PubMed:10393120, PubMed:18710934). Affects the implementation of differentiation, proliferation and apoptotic programs (PubMed:10393120, PubMed:18710934). May play an essential role in postimplantation development, probably in some aspect of cell specification and/or differentiation (By similarity). In collaboration with RELA/p65 enhances NFATc1 promoter activity and positively regulates RANKL-induced osteoclast differentiation (PubMed:18710934). Positively regulates self-renewal of liver cancer cells (By similarity). {ECO:0000250|UniProtKB:Q04721, ECO:0000269|PubMed:10393120, ECO:0000269|PubMed:18710934}. PTM: Synthesized in the endoplasmic reticulum as an inactive form which is proteolytically cleaved by a furin-like convertase in the trans-Golgi network before it reaches the plasma membrane to yield an active, ligand-accessible form (PubMed:11459941, PubMed:11518718). Cleavage results in a C-terminal fragment N(TM) and a N-terminal fragment N(EC) (PubMed:11459941, PubMed:11518718). Following ligand binding, it is cleaved by TNF-alpha converting enzyme (TACE) to yield a membrane-associated intermediate fragment called notch extracellular truncation (NEXT) (By similarity). This fragment is then cleaved by presenilin dependent gamma-secretase to release a notch-derived peptide containing the intracellular domain (NICD) from the membrane (PubMed:11459941, PubMed:11518718). {ECO:0000250|UniProtKB:Q01705, ECO:0000269|PubMed:11459941, ECO:0000269|PubMed:11518718}.; PTM: Hydroxylated by HIF1AN. {ECO:0000269|PubMed:18299578}.; PTM: Can be either O-glucosylated or O-xylosylated at Ser-611 by POGLUT1. {ECO:0000269|PubMed:21949356}.; PTM: Phosphorylated by GSK3. GSK3-mediated phosphorylation is necessary for NOTCH2 recognition by FBXW7, ubiquitination and degradation via the ubiquitin proteasome pathway. {ECO:0000250|UniProtKB:Q04721}. SUBCELLULAR LOCATION: Notch 2 extracellular truncation: Cell membrane {ECO:0000250|UniProtKB:Q04721}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q04721}.; SUBCELLULAR LOCATION: Notch 2 intracellular domain: Nucleus {ECO:0000250|UniProtKB:Q04721}. Cytoplasm {ECO:0000250|UniProtKB:Q04721}. Note=Following proteolytical processing NICD is translocated to the nucleus. Retained at the cytoplasm by TCIM. {ECO:0000250|UniProtKB:Q04721}. SUBUNIT: Heterodimer of a C-terminal fragment N(TM) and an N-terminal fragment N(EC) which are probably linked by disulfide bonds. Interacts with MAML1, MAML2 and MAML3 which act as transcriptional coactivators for NOTCH2. Interacts with RELA/p65. Interacts with HIF1AN. Interacts (via ANK repeats) with TCIM, the interaction inhibits the nuclear translocation of NOTCH2 N2ICD (By similarity). Interacts with CUL1, RBX1, SKP1 and FBXW7 that are SCF(FBXW7) E3 ubiquitin-protein ligase complex components. Interacts with MINAR1; this interaction increases MINAR1 stability and function (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q04721, ECO:0000269|PubMed:15019995, ECO:0000269|PubMed:17573339, ECO:0000269|PubMed:18710934}. TISSUE SPECIFICITY: Expressed in the brain, liver, kidney, neuroepithelia, somites, optic vesicles and branchial arches, but not heart. +Q8VCY8 PLPR2_MOUSE Phospholipid phosphatase-related protein type 2 (EC 3.1.3.4) (Lipid phosphate phosphatase-related protein type 2) (Plasticity-related gene 4 protein) (PRG-4) 343 36,936 Alternative sequence (1); Chain (1); Glycosylation (1); Modified residue (3); Transmembrane (6) TRANSMEM 12 32 Helical. {ECO:0000255}.; TRANSMEM 72 92 Helical. {ECO:0000255}.; TRANSMEM 129 149 Helical. {ECO:0000255}.; TRANSMEM 210 230 Helical. {ECO:0000255}.; TRANSMEM 239 259 Helical. {ECO:0000255}.; TRANSMEM 266 286 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q7TME0 PLPR4_MOUSE Phospholipid phosphatase-related protein type 4 (EC 3.1.3.4) (Brain-specific phosphatidic acid phosphatase-like protein 1) (Lipid phosphate phosphatase-related protein type 4) (Plasticity-related gene 1 protein) (PRG-1) 766 83,290 Chain (1); Compositional bias (1); Erroneous initiation (2); Glycosylation (9); Modified residue (7); Sequence conflict (12); Transmembrane (6) TRANSMEM 68 88 Helical. {ECO:0000255}.; TRANSMEM 120 140 Helical. {ECO:0000255}.; TRANSMEM 179 199 Helical. {ECO:0000255}.; TRANSMEM 248 268 Helical. {ECO:0000255}.; TRANSMEM 277 297 Helical. {ECO:0000255}.; TRANSMEM 309 329 Helical. {ECO:0000255}. FUNCTION: Hydrolyzes lysophosphatidic acid (LPA). Facilitates axonal outgrowth during development and regenerative sprouting. In the outgrowing axons acts as an ecto-enzyme and attenuates phospholipid-induced axon collapse in neurons and facilitates outgrowth in the hippocampus (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9JJ00 PLS1_MOUSE Phospholipid scramblase 1 (PL scramblase 1) (Ca(2+)-dependent phospholipid scramblase 1) (Transplantability-associated protein 1) (NOR1) (TRA1) 328 35,914 Chain (1); Compositional bias (2); Erroneous initiation (1); Frameshift (1); Lipidation (4); Modified residue (2); Motif (5); Region (1); Sequence conflict (3); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 298 314 Helical. {ECO:0000255}. TOPO_DOM 1 297 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 315 328 Extracellular. {ECO:0000250}. FUNCTION: May mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions that results in a loss of phospholipid asymmetry in the plasma membrane. May play a central role in the initiation of fibrin clot formation, in the activation of mast cells and in the recognition of apoptotic and injured cells by the reticuloendothelial system. {ECO:0000269|PubMed:12010804}.; FUNCTION: May play a role in the antiviral response of interferon (IFN) by amplifying and enhancing the IFN response through increased expression of select subset of potent antiviral genes. May contribute to cytokine-regulated cell proliferation and differentiation. {ECO:0000269|PubMed:12010804}. PTM: Phosphorylated by OXSR1 in the presence of RELT. {ECO:0000250|UniProtKB:O15162}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O15162}; Single-pass type II membrane protein. Membrane; Lipid-anchor {ECO:0000250}; Cytoplasmic side. Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250|UniProtKB:O15162}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O15162}. Note=Localizes to the perinuclear region in the presence of RELT. {ECO:0000250|UniProtKB:O15162}. SUBUNIT: Interacts with ABL. Interacts with RELT, RELL1 and RELL2. Interacts with OXSR1 in the presence of RELT. {ECO:0000250|UniProtKB:O15162}. DOMAIN: The N-terminal proline-rich domain (PRD) is required for phospholipid scramblase activity. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in kidney, lung, liver and bone marrow, slightly in spleen, heart and macrophage. DISEASE: Note=Participates in a chromosomal translocation that produces MMTRA1A which is leukemogenic to syngenic SL mice and athymic nude mice. +Q9D6T0 NOSIP_MOUSE Nitric oxide synthase-interacting protein (E3 ubiquitin-protein ligase NOSIP) (EC 2.3.2.27) (RING-type E3 ubiquitin transferase NOSIP) 301 33,209 Alternative sequence (1); Chain (1); Modified residue (1); Motif (1); Region (1) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that is essential for proper development of the forebrain, the eye and the face. Catalyzes monoubiquitination of serine/threonine-protein phosphatase 2A (PP2A) catalytic subunit PPP2CA/PPP2CB (PubMed:25546391). Negatively regulates nitric oxide production by inducing NOS1 and NOS3 translocation to actin cytoskeleton and inhibiting their enzymatic activity (By similarity). {ECO:0000250|UniProtKB:Q9Y314, ECO:0000269|PubMed:25546391}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y314}. Nucleus {ECO:0000250|UniProtKB:Q9Y314}. Note=Translocates from nucleus to cytoplasm in the G2 phase of the cell cycle. {ECO:0000250|UniProtKB:Q9Y314}. SUBUNIT: Interacts with NOS1 and NOS3 (By similarity). Interacts with PP2A holoenzyme, containing PPP2CA, PPP2CB, PPP2R1A and PPP2R2A subunits (PubMed:25546391). {ECO:0000250|UniProtKB:Q9Y314, ECO:0000269|PubMed:25546391}. DOMAIN: The U-box-like region is a truncated U-box domain. It is unknown whether it is functional or not. +P58196 PLS4_MOUSE Phospholipid scramblase 4 (PL scramblase 4) (Ca(2+)-dependent phospholipid scramblase 4) 326 36,579 Chain (1); Compositional bias (1); Lipidation (5); Modified residue (2); Motif (4); Region (1); Topological domain (2); Transmembrane (1) TRANSMEM 300 316 Helical. {ECO:0000255}. TOPO_DOM 1 299 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 317 326 Extracellular. {ECO:0000250}. FUNCTION: May mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions that results in a loss of phospholipid asymmetry in the plasma membrane. May play a central role in the initiation of fibrin clot formation, in the activation of mast cells and in the recognition of apoptotic and injured cells by the reticuloendothelial system. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. SUBUNIT: Interacts with PDCD6. {ECO:0000250}. DOMAIN: The N-terminal proline-rich domain (PRD) is required for phospholipid scramblase activity. {ECO:0000250}. +Q64104 NR2E1_MOUSE Nuclear receptor subfamily 2 group E member 1 (Nuclear receptor TLX) (Protein tailless homolog) (Tll) (mTll) 385 42,619 Chain (1); Compositional bias (1); DNA binding (1); Domain (1); Region (1); Zinc finger (2) FUNCTION: Orphan receptor that binds DNA as a monomer to hormone response elements (HRE) containing an extended core motif half-site sequence 5'-AAGGTCA-3' in which the 5' flanking nucleotides participate in determining receptor specificity (By similarity). Regulates cell cycle progression in neural stem cells of rhe developing brain. Involved in the regulation of retinal development and essential for vision. During retinogenesis, regulates PTEN-Cyclin D expression via binding to the promoter region of PTEN and suppressing its activity. May be involved in retinoic acid receptor (RAR) regulation in retinal cells. {ECO:0000250, ECO:0000269|PubMed:10706625, ECO:0000269|PubMed:16702404, ECO:0000269|PubMed:17901127}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407, ECO:0000269|PubMed:17901127}. SUBUNIT: Monomer (By similarity). Interacts with ATN1; the interaction represses the transcription. {ECO:0000250, ECO:0000269|PubMed:16702404}. TISSUE SPECIFICITY: Expressed in embryonic developing forebrain and in dorsal midbrain. Outside the neural epithelium only found in the surface ectoderm at the site of nasal placode formation, where subsequently the nasal and olfactory epithelium is formed. Also expressed in adult brain. {ECO:0000269|PubMed:7720587}. +P12813 NR4A1_MOUSE Nuclear receptor subfamily 4 group A member 1 (Nuclear hormone receptor NUR/77) (Nuclear protein N10) (Orphan nuclear receptor HMR) 601 64,738 Chain (1); Compositional bias (3); DNA binding (1); Domain (1); Modified residue (2); Sequence conflict (1); Zinc finger (2) FUNCTION: Orphan nuclear receptor. May act concomitantly with NURR1 in regulating the expression of delayed-early genes during liver regeneration. Binds the NGFI-B response element (NBRE) 5'-AAAAGGTCA-3'. May inhibit NF-kappa-B transactivation of IL2. Participates in energy homeostasis by sequestrating the kinase STK11 in the nucleus, thereby attenuating cytoplasmic AMPK activation (By similarity). Plays a role in the vascular response to injury (PubMed:22427340). {ECO:0000250, ECO:0000269|PubMed:22427340}. PTM: Phosphorylated at Ser-354 by RPS6KA1 and RPS6KA3 in response to mitogenic or stress stimuli. {ECO:0000250}.; PTM: Acetylated by p300/CBP, acetylation increases stability. Deacetylated by HDAC1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:2555161}. Cytoplasm {ECO:0000250|UniProtKB:P22736}. Note=Nuclear export to the cytoplasm is XPO1-mediated and positively regulated by IFI27. {ECO:0000250|UniProtKB:P22736}. SUBUNIT: Binds DNA as a monomer (By similarity). Interacts with GADD45GIP1. Interacts with STK11 (By similarity). Interacts with IFI27 (By similarity). {ECO:0000250|UniProtKB:P22736, ECO:0000250|UniProtKB:P22829}. TISSUE SPECIFICITY: Highest levels occur in the testis followed by brain and muscle tissue. +Q99J45 NRBP_MOUSE Nuclear receptor-binding protein (HLS7-interacting protein kinase) (MLF1 adapter molecule) 535 59,866 Chain (1); Domain (1); Initiator methionine (1); Modified residue (4); Sequence conflict (5) FUNCTION: May play a role in subcellular trafficking between the endoplasmic reticulum and Golgi apparatus through interactions with the Rho-type GTPases. {ECO:0000250|UniProtKB:Q9UHY1}. SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000269|PubMed:12176995}. Endomembrane system {ECO:0000269|PubMed:12176995}. Cell projection, lamellipodium {ECO:0000269|PubMed:12176995}. Note=Colocalizes with activated RAC3 to endomembranes and at the cell periphery in lamellipodia. SUBUNIT: Homodimer. Binds to MLF1, recruiting a serine kinase which phosphorylates both itself and MLF1. Phosphorylated MLF1 binds to YWHAZ and is retained in the cytoplasm. {ECO:0000269|PubMed:12176995}. DOMAIN: The protein kinase domain is predicted to be catalytically inactive. +Q9R1J0 NSDHL_MOUSE Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating (EC 1.1.1.170) 362 40,686 Active site (1); Binding site (1); Chain (1); Modified residue (1); Motif (1); Transmembrane (1) TRANSMEM 287 307 Helical. {ECO:0000255}. Steroid biosynthesis; zymosterol biosynthesis; zymosterol from lanosterol: step 4/6. FUNCTION: Involved in the sequential removal of two C-4 methyl groups in post-squalene cholesterol biosynthesis. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Lipid droplet {ECO:0000250}. Note=Trafficking through the Golgi is necessary for ER membrane localization. {ECO:0000250}. +P97799 NRSN1_MOUSE Neurensin-1 (Neuro-p24) (Vesicular membrane protein of 24 kDa) (Vesicular membrane protein p24) 196 21,595 Chain (1); Transmembrane (2) TRANSMEM 67 87 Helical. {ECO:0000255}.; TRANSMEM 121 141 Helical. {ECO:0000255}. FUNCTION: May play an important role in neural organelle transport, and in transduction of nerve signals or in nerve growth (PubMed:12445626, PubMed:16527258, PubMed:16696124, PubMed:9191101). May play a role in neurite extension (PubMed:26430118). {ECO:0000269|PubMed:12445626, ECO:0000269|PubMed:16527258, ECO:0000269|PubMed:16696124, ECO:0000269|PubMed:26430118, ECO:0000269|PubMed:9191101}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=Localizes mainly to neurites. {ECO:0000269|PubMed:16527258}. TISSUE SPECIFICITY: Expressed predominantly in brain. Also weakly expressed in lung and spleen. In brain, expressed strongly in nerve fibers of the cerebral cortex, anterior cerebral nuclei, hypothalamus, amygdaloid complex, brain stem of the metaencephalon and medulla oblongata, and moderately expressed in soma of neurons of the dentate gyrus of the hippocampus and Purkinje cells of the cerebellum. {ECO:0000269|PubMed:9191101}. +Q5HZK2 NRSN2_MOUSE Neurensin-2 202 22,415 Chain (1); Frameshift (1); Transmembrane (2) TRANSMEM 65 85 Helical. {ECO:0000255}.; TRANSMEM 116 136 Helical. {ECO:0000255}. FUNCTION: May play a role in maintenance and/or transport of vesicles. {ECO:0000269|PubMed:16527258}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Expressed specifically in brain where it is widely expressed, with highest levels of expression in thalamus and hypothalamus. In brain, found in neural cell bodies and detected in many regions of the limbic system, such as the septum nucleus, horizontal and vertical limbs of the diagonal band, hippocampus, amygdaloid nucleus, and habernula nucleus. Also localizes to small vesicles found in the perinuclear region of Neuro2a and PC12 cells. {ECO:0000269|PubMed:16527258}. +Q9JM14 NT5C_MOUSE 5'(3')-deoxyribonucleotidase, cytosolic type (EC 3.1.3.-) (Cytosolic 5',3'-pyrimidine nucleotidase) (Deoxy-5'-nucleotidase 1) (dNT-1) 200 23,076 Active site (2); Beta strand (6); Binding site (5); Chain (1); Helix (10); Metal binding (3); Modified residue (2); Turn (3) FUNCTION: Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides, with a preference for dUMP and dTMP, intermediate activity towards dGMP, and low activity towards dCMP and dAMP. {ECO:0000269|PubMed:10681516}. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Homodimer. {ECO:0000269|PubMed:17985935}. +Q6P9K9 NRX3A_MOUSE Neurexin-3 (Neurexin III-alpha) (Neurexin-3-alpha) 1571 173,428 Alternative sequence (3); Beta strand (13); Chain (1); Compositional bias (1); Disulfide bond (12); Domain (9); Glycosylation (6); Helix (3); Metal binding (3); Sequence caution (1); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1497 1517 Helical. {ECO:0000255}. TOPO_DOM 28 1496 Extracellular. {ECO:0000255}.; TOPO_DOM 1518 1571 Cytoplasmic. {ECO:0000255}. FUNCTION: Neuronal cell surface protein that may be involved in cell recognition and cell adhesion. May mediate intracellular signaling (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: The laminin G-like domain 2 binds to NXPH1. Specific isoforms bind to alpha-dystroglycan. The cytoplasmic C-terminal region binds to CASK (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Brain and arteries (at protein level). {ECO:0000269|PubMed:19926856}. +Q8CHQ9 NT8F2_MOUSE N-acetyltransferase family 8 member 2 (EC 2.3.1.-) (Camello-like protein 2) (N-acetyltransferase-like protein CML2) 238 26,424 Chain (1); Domain (1); Modified residue (1); Sequence conflict (2); Transmembrane (2) TRANSMEM 36 56 Helical. {ECO:0000255}.; TRANSMEM 60 80 Helical. {ECO:0000255}. FUNCTION: Probable acetyltransferase (Probable). Has no detectable histone acetyltransferase activity towards histone H3 or H4. {ECO:0000269|PubMed:25123547, ECO:0000305}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. +Q9JHL0 NTAL_MOUSE Linker for activation of T-cells family member 2 (Linker for activation of B-cells) (Membrane-associated adapter molecule) (Non-T-cell activation linker) (Williams-Beuren syndrome chromosomal region 15 protein homolog) 203 22,876 Alternative sequence (1); Chain (1); Lipidation (2); Modified residue (6); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 7 27 Helical; Signal-anchor for type III membrane protein. {ECO:0000255}. TOPO_DOM 1 6 Extracellular. {ECO:0000255}.; TOPO_DOM 28 203 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. May also be involved in BCR (B-cell antigen receptor)-mediated signaling in B-cells and FCGR1 (high affinity immunoglobulin gamma Fc receptor I)-mediated signaling in myeloid cells. Couples activation of these receptors and their associated kinases with distal intracellular events through the recruitment of GRB2. {ECO:0000269|PubMed:15477348, ECO:0000269|PubMed:15477350, ECO:0000269|PubMed:15899851}. PTM: Phosphorylated on tyrosines following cross-linking of BCR in B-cells, high affinity IgG receptor (FCGR1) in myeloid cells, or high affinity IgE receptor (FCER1) in mast cells; which induces the recruitment of GRB2. {ECO:0000269|PubMed:15477350}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15477348, ECO:0000269|PubMed:15477350}; Single-pass type III membrane protein {ECO:0000269|PubMed:15477348, ECO:0000269|PubMed:15477350}. Note=Present in lipid rafts. SUBUNIT: When phosphorylated, interacts with GRB2. May also interact with SOS1, GAB1 and CBL. {ECO:0000269|PubMed:15477348, ECO:0000269|PubMed:15477350}. TISSUE SPECIFICITY: Strongly expressed in testis. Expressed in heart, spleen and lung. Present in B-cells and mast cells (at protein level). {ECO:0000269|PubMed:11124535, ECO:0000269|PubMed:15477350, ECO:0000269|PubMed:15539154}. +Q64311 NTAN1_MOUSE Protein N-terminal asparagine amidohydrolase (EC 3.5.1.121) (Protein NH2-terminal asparagine amidohydrolase) (PNAA) (Protein NH2-terminal asparagine deamidase) (PNAD) (Protein N-terminal Asn amidase) (Protein NTN-amidase) 310 34,595 Chain (1) FUNCTION: N-terminal asparagine deamidase that mediates deamidation of N-terminal asparagine residues to aspartate. Required for the ubiquitin-dependent turnover of intracellular proteins that initiate with Met-Asn. These proteins are acetylated on the retained initiator methionine and can subsequently be modified by the removal of N-acetyl methionine by acylaminoacid hydrolase (AAH). Conversion of the resulting N-terminal asparagine to aspartate by NTAN1/PNAD renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. This enzyme does not act on substrates with internal or C-terminal asparagines and does not act on glutamine residues in any position. {ECO:0000269|PubMed:8910481}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q28955}. SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q28955}. +Q8CH40 NUDT6_MOUSE Nucleoside diphosphate-linked moiety X motif 6 (Nudix motif 6) (EC 3.6.1.-) (Antisense basic fibroblast growth factor B) 313 35,197 Chain (1); Domain (1); Sequence conflict (2) FUNCTION: May contribute to the regulation of cell proliferation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Mitochondrion {ECO:0000250}. SUBUNIT: Monomer and homodimer. {ECO:0000250}. +Q99P30 NUDT7_MOUSE Peroxisomal coenzyme A diphosphatase NUDT7 (EC 3.6.1.-) (Nucleoside diphosphate-linked moiety X motif 7) (Nudix motif 7) 236 26,857 Alternative sequence (5); Chain (1); Domain (1); Erroneous initiation (1); Metal binding (2); Modified residue (2); Motif (2); Sequence conflict (1) FUNCTION: Coenzyme A diphosphatase which mediates the cleavage of CoA, CoA esters and oxidized CoA with similar efficiencies, yielding 3',5'-ADP and the corresponding 4'-phosphopantetheine derivative as products. CoA into 3',5'-ADP and 4'-phosphopantetheine. Has no activity toward NDP-sugars, CDP-alcohols, (deoxy)nucleoside 5'-triphosphates, nucleoside 5'-di or monophosphates, diadenosine polyphosphates, NAD, NADH, NADP, NADPH or thymidine-5'-monophospho-p-nitrophenyl ester. May be required to eliminate oxidized CoA from peroxisomes, or regulate CoA and acyl-CoA levels in this organelle in response to metabolic demand. Does not play a role in U8 snoRNA decapping activity. Binds U8 snoRNA. {ECO:0000269|PubMed:11415433}. SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:11415433}. TISSUE SPECIFICITY: Highly expressed in liver. Expressed at intermediate level in lung and kidney and at low level in brain and heart. {ECO:0000269|PubMed:11415433}. +Q9CR24 NUDT8_MOUSE Nucleoside diphosphate-linked moiety X motif 8 (Nudix motif 8) (EC 3.6.1.-) 210 23,253 Chain (1); Domain (1); Metal binding (2); Modified residue (2); Motif (1) FUNCTION: Probably mediates the hydrolysis of some nucleoside diphosphate derivatives. {ECO:0000250}. +Q9CWD3 NUD17_MOUSE Nucleoside diphosphate-linked moiety X motif 17 (Nudix motif 17) (EC 3.6.1.-) 296 32,681 Alternative sequence (1); Chain (1); Domain (1); Metal binding (2); Motif (1) FUNCTION: Probably mediates the hydrolysis of some nucleoside diphosphate derivatives. {ECO:0000250}. +P51576 P2RX1_MOUSE P2X purinoceptor 1 (P2X1) (ATP receptor) (Purinergic receptor) 399 44,851 Chain (1); Compositional bias (1); Disulfide bond (5); Glycosylation (4); Modified residue (3); Region (1); Topological domain (3); Transmembrane (2) TRANSMEM 29 50 Helical; Name=1. {ECO:0000255}.; TRANSMEM 339 358 Helical; Name=2. {ECO:0000255}. TOPO_DOM 1 28 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 51 338 Extracellular. {ECO:0000255}.; TOPO_DOM 359 399 Cytoplasmic. {ECO:0000255}. FUNCTION: Ligand-gated ion channel with relatively high calcium permeability. Binding to ATP mediates synaptic transmission between neurons and from neurons to smooth muscle. Seems to be linked to apoptosis, by increasing the intracellular concentration of calcium in the presence of ATP, leading to programmed cell death (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SUBUNIT: Homo- or heteropolymers. {ECO:0000250}. +Q9JJX6 P2RX4_MOUSE P2X purinoceptor 4 (P2X4) (ATP receptor) (Purinergic receptor) 388 43,438 Alternative sequence (2); Chain (1); Disulfide bond (5); Glycosylation (7); Topological domain (3); Transmembrane (2) TRANSMEM 34 54 Helical; Name=1. {ECO:0000255}.; TRANSMEM 339 359 Helical; Name=2. {ECO:0000255}. TOPO_DOM 1 33 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 55 338 Extracellular. {ECO:0000255}.; TOPO_DOM 360 388 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for ATP that acts as a ligand-gated ion channel. This receptor is insensitive to the antagonists PPADS and suramin (By similarity). {ECO:0000250|UniProtKB:P51577, ECO:0000250|UniProtKB:Q99571}. SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q99571}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Functional P2XRs are organized as homomeric and heteromeric trimers. {ECO:0000250}. +Q9JK24 P2R3C_MOUSE Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit gamma (Protein phosphatase subunit G5PR) 453 53,407 Calcium binding (1); Chain (1); Compositional bias (1); Domain (2); Sequence conflict (1) FUNCTION: May regulate MCM3AP phosphorylation through phosphatase recruitment. May act as a negative regulator of ABCB1 expression and function through the dephosphorylation of ABCB1 by TFPI2/PPP2R3C complex. May play a role in the activation-induced cell death of B-cells. {ECO:0000250|UniProtKB:Q969Q6, ECO:0000269|PubMed:12167160, ECO:0000269|PubMed:16129705, ECO:0000269|PubMed:16343422}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12167160}. Cytoplasm {ECO:0000269|PubMed:12167160}. Note=Excluded from the nucleoli. Localization is cell cycle-dependent. Localizes to the cytoplasm during cytokinesis. SUBUNIT: Interacts with MCM3AP/GANP, PPP5C, and the phosphatase 2A core enzyme composed of the PPP2CA catalytic subunit and the constant regulatory subunit PPP2R1A. Finds in a complex with ABCB1, TFPI2 and PPP2R3C; leading to the dephosphorylation of ABCB1. {ECO:0000250|UniProtKB:Q969Q6, ECO:0000269|PubMed:12167160}. TISSUE SPECIFICITY: Expressed in all tissues tested including heart, brain, spleen, thymus, lung, liver, kidney and testis. {ECO:0000269|PubMed:12167160}. +P49650 P2RY1_MOUSE P2Y purinoceptor 1 (P2Y1) (ADP receptor) (Purinergic receptor) 373 42,213 Binding site (2); Chain (1); Disulfide bond (2); Glycosylation (4); Nucleotide binding (3); Topological domain (8); Transmembrane (7) TRANSMEM 52 74 Helical; Name=1. {ECO:0000250|UniProtKB:P47900}.; TRANSMEM 88 109 Helical; Name=2. {ECO:0000250|UniProtKB:P47900}.; TRANSMEM 126 147 Helical; Name=3. {ECO:0000250|UniProtKB:P47900}.; TRANSMEM 167 188 Helical; Name=4. {ECO:0000250|UniProtKB:P47900}.; TRANSMEM 215 237 Helical; Name=5. {ECO:0000250|UniProtKB:P47900}.; TRANSMEM 261 284 Helical; Name=6. {ECO:0000250|UniProtKB:P47900}.; TRANSMEM 304 325 Helical; Name=7. {ECO:0000250|UniProtKB:P47900}. TOPO_DOM 1 51 Extracellular. {ECO:0000305}.; TOPO_DOM 75 87 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 110 125 Extracellular. {ECO:0000305}.; TOPO_DOM 148 166 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 189 214 Extracellular. {ECO:0000305}.; TOPO_DOM 238 260 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 285 303 Extracellular. {ECO:0000305}.; TOPO_DOM 326 373 Cytoplasmic. {ECO:0000305}. FUNCTION: Receptor for extracellular adenine nucleotides such as ADP. In platelets, binding to ADP leads to mobilization of intracellular calcium ions via activation of phospholipase C, a change in platelet shape, and ultimately platelet aggregation. {ECO:0000269|PubMed:10606627}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P47900}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P47900}. +Q3V1T4 P3H1_MOUSE Prolyl 3-hydroxylase 1 (EC 1.14.11.7) (Growth suppressor 1) (Leucine- and proline-enriched proteoglycan 1) (Leprecan-1) 739 83,651 Active site (1); Alternative sequence (3); Chain (1); Coiled coil (1); Domain (1); Frameshift (1); Glycosylation (3); Metal binding (3); Motif (1); Repeat (4); Sequence caution (1); Sequence conflict (17); Signal peptide (1) FUNCTION: Basement membrane-associated chondroitin sulfate proteoglycan (CSPG). Has prolyl 3-hydroxylase activity catalyzing the post-translational formation of 3-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens, especially types IV and V. May be involved in the secretory pathway of cells. Has growth suppressive activity in fibroblasts (By similarity). {ECO:0000250}. PTM: O-glycosylated; chondroitin sulfate. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000255|PROSITE-ProRule:PRU10138}. Secreted, extracellular space, extracellular matrix {ECO:0000250}. Note=Secreted into the extracellular matrix as a chondroitin sulfate proteoglycan (CSPG). +Q6W3F0 P4HA3_MOUSE Prolyl 4-hydroxylase subunit alpha-3 (4-PH alpha-3) (EC 1.14.11.2) (Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-3) 542 60,975 Alternative sequence (2); Binding site (1); Chain (1); Coiled coil (1); Domain (1); Glycosylation (2); Metal binding (3); Repeat (1); Signal peptide (1) FUNCTION: Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins. {ECO:0000250}. PTM: N-glycosylation plays no role in the catalytic activity. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250}. SUBUNIT: Heterotetramer of two alpha-3 chains and two beta chains (the beta chain is the multi-functional PDI). {ECO:0000250}. +Q8BG58 P4HTM_MOUSE Transmembrane prolyl 4-hydroxylase (P4H-TM) (EC 1.14.11.29) (Hypoxia-inducible factor prolyl hydroxylase 4) (HIF-PH4) (HIF-prolyl hydroxylase 4) (HPH-4) 503 57,049 Alternative sequence (2); Binding site (1); Calcium binding (2); Chain (1); Domain (3); Frameshift (1); Glycosylation (3); Metal binding (3); Sequence caution (1); Topological domain (2); Transmembrane (1) TRANSMEM 62 82 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 61 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 83 503 Lumenal. {ECO:0000255}. FUNCTION: Catalyzes the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates HIF1A at 'Pro-402' and 'Pro-564'. May function as a cellular oxygen sensor and, under normoxic conditions, may target HIF through the hydroxylation for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. {ECO:0000250|UniProtKB:Q9NXG6}. PTM: Glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9NXG6}. +Q9CUX1 P52K_MOUSE 52 kDa repressor of the inhibitor of the protein kinase (p52rIPK) (58 kDa interferon-induced protein kinase-interacting protein) (p58IPK-interacting protein) (THAP domain-containing protein 0) (THAP domain-containing protein 12) 758 87,021 Chain (1); Modified residue (1); Zinc finger (1) FUNCTION: Upstream regulator of interferon-induced serine/threonine protein kinase R (PKR). May block the PKR-inhibitory function of DNAJC3, resulting in restoration of kinase activity and suppression of cell growth. {ECO:0000250}. SUBUNIT: Interacts with DNAJC3, probably sequestring it. {ECO:0000250}. +P02340 P53_MOUSE Cellular tumor antigen p53 (Tumor suppressor p53) 390 43,458 Beta strand (12); Chain (1); Cross-link (3); DNA binding (1); Helix (6); Metal binding (4); Modified residue (22); Motif (3); Natural variant (3); Region (13); Sequence conflict (2); Site (1); Turn (4) FUNCTION: Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression. In cooperation with mitochondrial PPIF is involved in activating oxidative stress-induced necrosis; the function is largely independent of transcription. Prevents CDK7 kinase activity when associated to CAK complex in response to DNA damage, thus stopping cell cycle progression (By similarity). Induces the transcription of long intergenic non-coding RNA p21 (lincRNA-p21) and lincRNA-Mkln1. LincRNA-p21 participates in TP53-dependent transcriptional repression leading to apoptosis, but seems to have to effect on cell-cycle regulation. Regulates the circadian clock by repressing CLOCK-ARNTL/BMAL1-mediated transcriptional activation of PER2 (PubMed:24051492). {ECO:0000250|UniProtKB:P04637, ECO:0000269|PubMed:19556538, ECO:0000269|PubMed:20673990, ECO:0000269|PubMed:22726440, ECO:0000269|PubMed:24051492}. PTM: Phosphorylated on Ser-18 upon ultraviolet irradiation; which is enhanced by interaction with BANP (By similarity). Phosphorylation on Ser residues mediates transcriptional activation. Phosphorylation at Ser-12 by HIPK4 increases repression activity on BIRC5 promoter. Phosphorylated on Thr-21 by VRK1. Phosphorylated on Ser-23 by CHEK2 in response to DNA damage, which prevents ubiquitination by MDM2. Phosphorylated on Ser-23 by PLK3 in response to reactive oxygen species (ROS), promoting p53/TP53-mediated apoptosis. Probably phosphorylated on by CDK7 in a CAK complex in response to DNA damage. Stabilized by CDK5-mediated phosphorylation in response to genotoxic and oxidative stresses at Ser-18 leading to accumulation of p53/TP53, particularly in the nucleus, thus inducing the transactivation of p53/TP53 target genes (By similarity). Phosphorylated on Ser-389 following UV but not gamma irradiation. Phosphorylated by HIPK1. {ECO:0000250, ECO:0000269|PubMed:12702766, ECO:0000269|PubMed:15195100, ECO:0000269|PubMed:17254968, ECO:0000269|PubMed:18022393, ECO:0000269|PubMed:19556538, ECO:0000269|PubMed:2145148, ECO:0000269|PubMed:3006031}.; PTM: Deacetylation by SIRT2 impairs its ability to induce transcription activation in a AKT-dependent manner (By similarity). Acetylated. Its deacetylation by SIRT1 impairs its ability to induce proapoptotic program and modulate cell senescence. {ECO:0000250}.; PTM: Ubiquitinated by MDM2 and SYVN1, which leads to proteasomal degradation. Ubiquitinated by RFWD3, which works in cooperation with MDM2 and may catalyze the formation of short polyubiquitin chains on p53/TP53 that are not targeted to the proteasome. Ubiquitinated by MKRN1 at Lys-288 and Lys-289, which leads to proteasomal degradation. Deubiquitinated by USP10, leading to stabilize it. Ubiquitinated by TRIM24, RFFL, RNF34 and RNF125, which leads to proteasomal degradation. Ubiquitination by TOPORS induces degradation. Deubiquitination by USP7, leading to stabilize it. Ubiquitinated by COP1, which leads to proteasomal degradation (By similarity). Ubiquitination and subsequent proteasomal degradation is negatively regulated by CCAR2 (PubMed:25732823). Polyubiquitinated by C10orf90/FATS, polyubiquitination is 'Lys-48'-linkage independent and non-proteolytic, leading to TP53 stabilization (PubMed:24240685). {ECO:0000250|UniProtKB:P04637, ECO:0000269|PubMed:24240685, ECO:0000269|PubMed:25732823}.; PTM: Monomethylated at Lys-369 by SETD7, leading to stabilization and increased transcriptional activation. Monomethylated at Lys-367 by SMYD2, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity. Lys-369 monomethylation prevents interaction with SMYD2 and subsequent monomethylation at Lys-367. Dimethylated at Lys-370 by EHMT1 and EHMT2. Monomethylated at Lys-379 by KMT5A, promoting interaction with L3MBTL1 and leading to repress transcriptional activity. Demethylation of dimethylated Lys-367 by KDM1A prevents interaction with TP53BP1 and represses TP53-mediated transcriptional activation (By similarity). {ECO:0000250}.; PTM: Sumoylated with SUMO1. Sumoylated at Lys-383 by UBC9 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P04637}. Nucleus {ECO:0000250|UniProtKB:P04637}. Nucleus, PML body {ECO:0000250|UniProtKB:P04637}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P04637}. Mitochondrion matrix {ECO:0000250|UniProtKB:P04637}. Note=Interaction with BANP promotes nuclear localization. Recruited into PML bodies together with CHEK2. Translocates to mitochondria upon oxidative stress. Translocates to mitochondria in response to mitomycin C treatment (By similarity). {ECO:0000250|UniProtKB:P04637}. SUBUNIT: Binds DNA as a homotetramer. Interacts with AXIN1 (PubMed:15526030). Probably part of a complex consisting of TP53, HIPK2 and AXIN1 (PubMed:15526030). Interacts with histone acetyltransferases EP300 and methyltransferases HRMT1L2 and CARM1, and recruits them to promoters. Interacts (via C-terminus) with TAF1; when TAF1 is part of the TFIID complex. Interacts with ING4; this interaction may be indirect (PubMed:12702766). Found in a complex with CABLES1 and TP73 (PubMed:11706030). Interacts with HIPK1, HIPK2, and TP53INP1. Interacts with WWOX. Interacts with USP7 and SYVN1 (PubMed:14719112). Interacts with HSP90AB1. Interacts with CHD8; leading to recruit histone H1 and prevent transactivation activity (PubMed:19151705). Interacts with ARMC10, BANP, CDKN2AIP, NUAK1, STK11/LKB1, UHRF2 and E4F (PubMed:10644996). Interacts with YWHAZ; the interaction enhances TP53 transcriptional activity. Phosphorylation of YWHAZ on 'Ser-58' inhibits this interaction. Interacts (via DNA-binding domain) with MAML1 (via N-terminus). Interacts with MKRN1. Interacts with PML (via C-terminus). Interacts with MDM2; leading to ubiquitination and proteasomal degradation of TP53. Directly interacts with FBXO42; leading to ubiquitination and degradation of TP53. Interacts (phosphorylated at Ser-18 by ATM) with the phosphatase PP2A-PPP2R5C holoenzyme; regulates stress-induced TP53-dependent inhibition of cell proliferation. Interacts with PPP2R2A. Interacts with AURKA, DAXX, BRD7 and TRIM24 (PubMed:19556538). Interacts (when monomethylated at Lys-379) with L3MBTL1. Interacts with GRK5. Binds to the CAK complex (CDK7, cyclin H and MAT1) in response to DNA damage. Interacts with CDK5 in neurons. Interacts with AURKB, SETD2, UHRF2 and NOC2L. Interacts (via N-terminus) with PTK2/FAK1; this promotes ubiquitination by MDM2. Interacts with PTK2B/PYK2; this promotes ubiquitination by MDM2. Interacts with PRKCG. Interacts with PPIF; the association implicates preferentially tetrameric TP53, is induced by oxidative stress and is impaired by cyclosporin A (CsA). Interacts with SNAI1; the interaction induces SNAI1 degradation via MDM2-mediated ubiquitination and inhibits SNAI1-induced cell invasion. Interacts with KAT6A. Interacts with UBC9. Interacts with ZNF385B; the interaction is direct. Interacts (via DNA-binding domain) with ZNF385A; the interaction is direct and enhances p53/TP53 transactivation functions on cell-cycle arrest target genes, resulting in growth arrest (PubMed:17719541). Interacts with ANKRD2. Interacts with RFFL and RNF34; involved in p53/TP53 ubiquitination. Interacts with MTA1 and COP1. Interacts with CCAR2 (via N-terminus). Interacts with MORC3. Interacts (via C-terminus) with POU4F2 (via C-terminus). Interacts (via oligomerization region) with NOP53; the interaction is direct and may prevent the MDM2-mediated proteasomal degradation of TP53. Interacts with AFG1L; mediates mitochondrial translocation of TP53. Interacts with UBD (By similarity). Interacts with TAF6 (By similarity). Interacts with C10orf90/FATS; the interaction inhibits binding of TP53 and MDM2 (PubMed:24240685). {ECO:0000250|UniProtKB:P04637, ECO:0000250|UniProtKB:P10361, ECO:0000269|PubMed:10644996, ECO:0000269|PubMed:11706030, ECO:0000269|PubMed:12494467, ECO:0000269|PubMed:12702766, ECO:0000269|PubMed:14719112, ECO:0000269|PubMed:15526030, ECO:0000269|PubMed:17719541, ECO:0000269|PubMed:19151705, ECO:0000269|PubMed:19556538, ECO:0000269|PubMed:24240685}. DOMAIN: The [KR]-[STA]-K motif is specifically recognized by the SETD7 methyltransferase. {ECO:0000250}. DISEASE: Note=p53 is found in increased amounts in a wide variety of transformed cells. p53 is frequently mutated or inactivated in many types of cancer. +Q5F267 P5I13_MOUSE Tumor protein p53-inducible protein 13 385 41,766 Chain (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 302 322 Helical. {ECO:0000255}. TOPO_DOM 28 301 Extracellular. {ECO:0000255}.; TOPO_DOM 323 385 Cytoplasmic. {ECO:0000255}. FUNCTION: May act as a tumor suppressor. Inhibits tumor cell growth, when overexpressed (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}; Extracellular side {ECO:0000305}. Cytoplasm {ECO:0000250}. Note=Associates with unknown subcellular structures in the cytoplasm. {ECO:0000250}. +Q9Z110 P5CS_MOUSE Delta-1-pyrroline-5-carboxylate synthase (P5CS) (Aldehyde dehydrogenase family 18 member A1) [Includes: Glutamate 5-kinase (GK) (EC 2.7.2.11) (Gamma-glutamyl kinase); Gamma-glutamyl phosphate reductase (GPR) (EC 1.2.1.41) (Glutamate-5-semialdehyde dehydrogenase) (Glutamyl-gamma-semialdehyde dehydrogenase)] 795 87,266 Alternative sequence (1); Binding site (3); Chain (1); Modified residue (3); Nucleotide binding (2); Region (2); Sequence conflict (2) Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 1/2. Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2. FUNCTION: Bifunctional enzyme that converts glutamate to glutamate 5-semialdehyde, an intermediate in the biosynthesis of proline, ornithine and arginine. {ECO:0000250|UniProtKB:P54886}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P54886}. SUBUNIT: Homohexamer or homotetramer. {ECO:0000250|UniProtKB:P54886}. +Q9JJP2 P73_MOUSE Tumor protein p73 (p53-like transcription factor) (p53-related protein) 631 69,096 Alternative sequence (4); Chain (1); Compositional bias (2); Cross-link (2); Domain (1); Erroneous initiation (1); Metal binding (4); Modified residue (3); Motif (1); Region (4); Sequence conflict (5) FUNCTION: Participates in the apoptotic response to DNA damage. Isoforms containing the transactivation domain are pro-apoptotic, isoforms lacking the domain are anti-apoptotic and block the function of p53 and transactivating p73 isoforms. May be a tumor suppressor protein. {ECO:0000250|UniProtKB:O15350, ECO:0000269|PubMed:10232589, ECO:0000269|PubMed:11932750}. PTM: Sumoylated on Lys-622, which potentiates proteasomal degradation but does not affect transcriptional activity. {ECO:0000250}.; PTM: Phosphorylation by PLK1 and PLK3 inhibits the transcription regulator activity and pro-apoptotic function (By similarity). Higher levels of phosphorylation seen in striatal neurons of. mutant huntingtin (htt) transgenic mice. {ECO:0000250, ECO:0000269|PubMed:16461361}.; PTM: Polyubiquitinated by RCHY1/PIRH2; leading to its degradation by the proteasome. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15113856}. Cytoplasm {ECO:0000250}. Note=Accumulates in the nucleus in response to DNA damage. {ECO:0000269|PubMed:15113856}. SUBUNIT: Found in a complex with p53/TP53 and CABLES1. The C-terminal oligomerization domain binds to the ABL1 tyrosine kinase SH3 domain. Interacts with HECW2, HIPK2, RANBP9 and WWOX (By similarity). Interacts (via SAM domain) with FBXO45 (via B30.2/SPRY domain) (By similarity). Interacts with YAP1 (phosphorylated form) (By similarity). Interacts with HCK (via SH3 domain); this inhibits TP73 activity and degradation (By similarity). {ECO:0000250}. DOMAIN: Possesses an acidic transactivation domain, a central DNA binding domain and a C-terminal oligomerization domain that binds to the ABL1 tyrosine kinase SH3 domain. {ECO:0000250}.; DOMAIN: The PPxY motif mediates interaction with WWOX. {ECO:0000250|UniProtKB:O15350}. TISSUE SPECIFICITY: Found in striatal neurons of mutant huntingtin (htt) transgenic mice (at protein level). Isoform 1 is expressed in the nasal epithelium, the vomeronasal organ, the hippocampus and the hypothalamus. {ECO:0000269|PubMed:10716451, ECO:0000269|PubMed:16461361}. +P26450 P85A_MOUSE Phosphatidylinositol 3-kinase regulatory subunit alpha (PI3-kinase regulatory subunit alpha) (PI3K regulatory subunit alpha) (PtdIns-3-kinase regulatory subunit alpha) (Phosphatidylinositol 3-kinase 85 kDa regulatory subunit alpha) (PI3-kinase subunit p85-alpha) (PtdIns-3-kinase regulatory subunit p85-alpha) 724 83,517 Chain (1); Domain (4); Initiator methionine (1); Modified residue (6); Sequence conflict (2) FUNCTION: Binds to activated (phosphorylated) protein-Tyr kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane. Necessary for the insulin-stimulated increase in glucose uptake and glycogen synthesis in insulin-sensitive tissues. Plays an important role in signaling in response to FGFR1, FGFR2, FGFR3, FGFR4, KITLG/SCF, KIT, PDGFRA and PDGFRB. Likewise, plays a role in ITGB2 signaling (By similarity). Modulates the cellular response to ER stress by promoting nuclear translocation of XBP1 isoform 2 in a ER stress- and/or insulin-dependent manner during metabolic overloading in the liver and hence plays a role in glucose tolerance improvement (PubMed:20348926). {ECO:0000250, ECO:0000269|PubMed:20348926}. PTM: Polyubiquitinated in T-cells by CBLB; which does not promote proteasomal degradation but impairs association with CD28 and CD3Z upon T-cell activation. {ECO:0000269|PubMed:11526404}.; PTM: Phosphorylated. Tyrosine phosphorylated in response to signaling by FGFR1, FGFR2, FGFR3 and FGFR4. Dephosphorylated by PTPRJ. Phosphorylated by PIK3CA at Ser-608; phosphorylation is stimulated by insulin and PDGF. The relevance of phosphorylation by PIK3CA is however unclear. Phosphorylated in response to KIT and KITLG/SCF. Phosphorylated by FGR (By similarity). Phosphorylated by CSF1R. Phosphorylated by ERBB4. Phosphorylated on tyrosine residues by TEK/TIE2. {ECO:0000250, ECO:0000269|PubMed:10353604, ECO:0000269|PubMed:10521483, ECO:0000269|PubMed:11294897, ECO:0000269|PubMed:9312046}. SUBUNIT: Interacts with XBP1 isoform 2; the interaction is direct and induces translocation of XBP1 isoform 2 into the nucleus in a ER stress- and/or insulin-dependent but PI3K-independent manner (PubMed:20348926). Interacts with PIK3R2; the interaction is dissociated in an insulin-dependent manner (PubMed:20348926). Heterodimer of a regulatory subunit PIK3R1 and a p110 catalytic subunit (PIK3CA, PIK3CB or PIK3CD). Interacts with phosphorylated LAT, LAX1 and TRAT1 upon TCR activation. The SH2 domains interact with the YTHM motif of phosphorylated INSR in vitro. Also interacts with tyrosine-phosphorylated IGF1R in vitro. Interacts with IRS1 and phosphorylated IRS4. Interacts with NISCH and RUFY3 (By similarity). Interacts with phosphorylated TOM1L1. Interacts with phosphorylated LIME1 upon TCR or BCR activation. Interacts with CBLB. Interacts with CD28 and CD3Z upon T-cell activation. Interacts with SOCS7 and HCST. Interacts with AXL, FASLG, FGR, HCK, KIT and BCR. Interacts with PTK2/FAK1 (By similarity). Interacts with PDGFRB (tyrosine phosphorylated) (By similarity). Interacts with NTRK1 (phosphorylated upon ligand-binding) (By similarity). Interacts (via SH2 domain) with CSF1R (tyrosine phosphorylated) (PubMed:9312046). Interacts with FER. Interacts with FGFR1, FGFR2, FGFR3 and FGFR4 (phosphorylated) (Probable). Interacts with PDGFRA (tyrosine phosphorylated). Interacts with LYN (via SH3 domain); this enhances enzyme activity. Interacts with ERBB4. Interacts (via SH2 domain) with TEK/TIE2 (tyrosine phosphorylated). Interacts with FAM83B; activates the PI3K/AKT signaling cascade (By similarity). {ECO:0000250|UniProtKB:P23727, ECO:0000250|UniProtKB:P27986, ECO:0000250|UniProtKB:Q63787, ECO:0000269|PubMed:10353604, ECO:0000269|PubMed:10521483, ECO:0000269|PubMed:10528161, ECO:0000269|PubMed:10646608, ECO:0000269|PubMed:11006284, ECO:0000269|PubMed:11113178, ECO:0000269|PubMed:11294897, ECO:0000269|PubMed:11526404, ECO:0000269|PubMed:11711534, ECO:0000269|PubMed:12052866, ECO:0000269|PubMed:14610044, ECO:0000269|PubMed:16249387, ECO:0000269|PubMed:1646396, ECO:0000269|PubMed:20348926, ECO:0000269|PubMed:8128248, ECO:0000269|PubMed:8943348, ECO:0000269|PubMed:9312046, ECO:0000305}. DOMAIN: The SH3 domain mediates the binding to CBLB. {ECO:0000250}. +Q61205 PA1B3_MOUSE Platelet-activating factor acetylhydrolase IB subunit gamma (EC 3.1.1.47) (PAF acetylhydrolase 29 kDa subunit) (PAF-AH 29 kDa subunit) (PAF-AH subunit gamma) (PAFAH subunit gamma) 232 25,853 Active site (3); Chain (1); Initiator methionine (1); Modified residue (2) FUNCTION: Inactivates paf by removing the acetyl group at the sn-2 position. This is a catalytic subunit. Plays an important role during the development of brain. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Cytosolic PAF-AH IB is formed of three subunits of 45 kDa (alpha), 30 kDa (beta) and 29 kDa (gamma). The catalytic activity of the enzyme resides in the beta and gamma subunits, whereas the alpha subunit has regulatory activity. Trimer formation is not essential for the catalytic activity. +Q9Z0Y2 PA21B_MOUSE Phospholipase A2 (EC 3.1.1.4) (Group IB phospholipase A2) (PLA2-Ib) (Phosphatidylcholine 2-acylhydrolase 1B) 146 16,290 Active site (2); Chain (1); Disulfide bond (7); Metal binding (4); Propeptide (1); Sequence conflict (7); Signal peptide (1) FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides, this releases glycerophospholipids and arachidonic acid that serve as the precursors of signal molecules. PTM: Activated by trypsin cleavage in the duodenum. Can also be activated by thrombin or autocatalytically (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. Note=secreted from pancreatic acinar cells in its inactive form. {ECO:0000250}. SUBUNIT: Monomer or homodimer. The inactive pro-form is a homotrimer (By similarity). {ECO:0000250}. +P31482 PA2GA_MOUSE Phospholipase A2, membrane associated (EC 3.1.1.4) (Enhancing factor) (EF) (GIIC sPLA2) (Group IIA phospholipase A2) (Phosphatidylcholine 2-acylhydrolase 2A) 146 16,145 Active site (2); Chain (1); Disulfide bond (7); Erroneous initiation (1); Metal binding (4); Sequence conflict (2); Signal peptide (1); Site (1) FUNCTION: Catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides (PubMed:8425615). Thought to participate in the regulation of phospholipid metabolism in biomembranes including eicosanoid biosynthesis. Independent of its catalytic activity, acts as a ligand for integrins. Binds to and activates integrins ITGAV:ITGB3, ITGA4:ITGB1 and ITGA5:ITGB. Binds to a site (site 2) which is distinct from the classical ligand-binding site (site 1) and induces integrin conformational changes and enhanced ligand binding to site 1. Induces cell proliferation in an integrin-dependent manner (By similarity). {ECO:0000250|UniProtKB:P14555, ECO:0000269|PubMed:8425615}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000250|UniProtKB:P14555}. Secreted {ECO:0000250|UniProtKB:P14555}. TISSUE SPECIFICITY: Mainly in the Paneth cells adjacent to the stem population in the small intestines. Also expressed in regenerating liver and hyperplastic esophageal epithelium. +O70176 PACA_MOUSE Pituitary adenylate cyclase-activating polypeptide (PACAP) [Cleaved into: PACAP-related peptide (PRP-48); Pituitary adenylate cyclase-activating polypeptide 27 (PACAP-27) (PACAP27); Pituitary adenylate cyclase-activating polypeptide 38 (PACAP-38) (PACAP38)] 175 19,381 Modified residue (2); Peptide (3); Propeptide (2); Region (1); Signal peptide (1) FUNCTION: Binding to its receptor activates G proteins and stimulates adenylate cyclase in pituitary cells (By similarity). Promotes neuron projection development through the RAPGEF2/Rap1/B-Raf/ERK pathway (By similarity). In chromaffin cells, induces long-lasting increase of intracellular calcium concentrations and neuroendocrine secretion (By similarity). Involved in the control of glucose homeostasis, induces insulin secretion by pancreatic beta cells (PubMed:23913443). {ECO:0000250|UniProtKB:P13589, ECO:0000250|UniProtKB:P18509, ECO:0000250|UniProtKB:Q29W19, ECO:0000269|PubMed:23913443}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Interacts with ADCYAP1R1 (via N-terminal extracellular domain). {ECO:0000250|UniProtKB:P18509}. +Q9WVE8 PACN2_MOUSE Protein kinase C and casein kinase substrate in neurons protein 2 (Syndapin-2) (Syndapin-II) 486 55,833 Beta strand (1); Chain (1); Coiled coil (1); Domain (2); Helix (10); Modified residue (4); Motif (3); Mutagenesis (5); Turn (2) FUNCTION: Lipid-binding protein that is able to promote the tubulation of the phosphatidic acid-containing membranes it preferentially binds. Plays a role in intracellular vesicle-mediated transport. Involved in the endocytosis of cell-surface receptors like the EGF receptor, contributing to its internalization in the absence of EGF stimulus. May also play a role in the formation of caveolae at the cell membrane. Recruits DNM2 to caveolae, and thereby plays a role in caveola-mediated endocytosis. {ECO:0000269|PubMed:11082044, ECO:0000269|PubMed:15930129, ECO:0000269|PubMed:20188097, ECO:0000269|PubMed:21610094, ECO:0000269|PubMed:21693584, ECO:0000269|PubMed:21807942, ECO:0000269|PubMed:23129763}. PTM: Phosphorylated by casein kinase 2 (CK2) and protein kinase C (PKC). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection, ruffle membrane; Peripheral membrane protein; Cytoplasmic side. Early endosome. Recycling endosome membrane {ECO:0000250}. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection. Membrane, caveola. Note=Detected at the neck of flask-shaped caveolae. Localization to tubular recycling endosomes probably requires interaction with MICALL1 and EHD1. SUBUNIT: Homodimer. May form heterooligomers with other PACSINs. Interacts (via NPF motifs) with EHD1 (via EH domain). Interacts with EHD3. Interacts (via the SH3 domain) with MICALL1. Interacts with RAC1. Interacts (via SH3 domain) with DNM1, SYN1, SYNJ1 and WASL. Interacts with CAV1. Interacts with TRPV4. {ECO:0000269|PubMed:11082044, ECO:0000269|PubMed:15930129, ECO:0000269|PubMed:16627472, ECO:0000269|PubMed:20471395, ECO:0000269|PubMed:21610094, ECO:0000269|PubMed:21693584}. DOMAIN: The F-BAR domain forms a coiled coil and mediates membrane-binding and membrane tubulation. In the autoinhibited conformation, interaction with the SH3 domain inhibits membrane tubulation mediated by the F-BAR domain. {ECO:0000269|PubMed:20188097, ECO:0000269|PubMed:20471395}. TISSUE SPECIFICITY: Widely expressed (at protein level). {ECO:0000269|PubMed:10431838, ECO:0000269|PubMed:11082044}. +Q99JB8 PACN3_MOUSE Protein kinase C and casein kinase II substrate protein 3 424 48,585 Beta strand (3); Chain (1); Coiled coil (1); Domain (2); Helix (8); Modified residue (7); Mutagenesis (1); Sequence conflict (1); Turn (2) FUNCTION: Plays a role in endocytosis and regulates internalization of plasma membrane proteins. Overexpression impairs internalization of SLC2A1/GLUT1 and TRPV4 and increases the levels of SLC2A1/GLUT1 and TRPV4 at the cell membrane. Inhibits the TRPV4 calcium channel activity. {ECO:0000269|PubMed:11082044, ECO:0000269|PubMed:16627472, ECO:0000269|PubMed:17320047, ECO:0000269|PubMed:18174177}. PTM: Phosphorylated by casein kinase 2 (CK2) and protein kinase C (PKC). SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11082044}. Cell membrane {ECO:0000269|PubMed:11082044}; Peripheral membrane protein {ECO:0000269|PubMed:11082044}; Cytoplasmic side {ECO:0000269|PubMed:11082044}. Note=Detected at the inner aspect of the plasma membrane in myotubes. SUBUNIT: Homodimer. May form heterooligomers with other PACSINs. Interacts (via SH3 domain) with DNM1, SYNJ1 and WASL. Interacts with TRPV4. {ECO:0000269|PubMed:11082044, ECO:0000269|PubMed:16627472, ECO:0000269|PubMed:18174177, ECO:0000269|PubMed:22573331}. DOMAIN: The F-BAR domain forms a coiled coil and mediates membrane-binding and membrane tubulation. {ECO:0000269|PubMed:22573331}. TISSUE SPECIFICITY: Highly expressed in skeletal muscle, heart and lung; also detected in brain, kidney and uterus (at protein level). {ECO:0000269|PubMed:11082044}. +Q9DAK2 PACRG_MOUSE Parkin coregulated gene protein homolog (Hypertension-related protein 1-like protein) (PARK2 coregulated gene protein) 241 27,726 Chain (1) FUNCTION: Suppresses cell death induced by accumulation of unfolded Pael receptor (Pael-R, a substrate of Parkin). Facilitates the formation of inclusions consisting of Pael-R, molecular chaperones, protein degradation molecules and itself when proteasome is inhibited (By similarity). {ECO:0000250}. SUBUNIT: Forms a large molecular chaperone complex containing heat shock proteins 70 and 90 and chaperonin components. Interacts with STIP1, PRKN, GPR37, HSPA8, TCP1/CCT1, CCT2, CCT3, CCT4, CCT5, CCT6A, CCT7 and CCT8 (By similarity). Interacts with MEIG1. {ECO:0000250, ECO:0000269|PubMed:19805151}. +Q9D3X5 PACRL_MOUSE PACRG-like protein 248 27,290 Chain (1); Modified residue (2) +P70205 PACR_MOUSE Pituitary adenylate cyclase-activating polypeptide type I receptor (PACAP type I receptor) (PACAP-R-1) (PACAP-R1) 496 56,640 Chain (1); Disulfide bond (3); Glycosylation (3); Modified residue (2); Region (1); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 156 178 Helical; Name=1. {ECO:0000255}.; TRANSMEM 187 205 Helical; Name=2. {ECO:0000255}.; TRANSMEM 228 253 Helical; Name=3. {ECO:0000255}.; TRANSMEM 269 291 Helical; Name=4. {ECO:0000255}.; TRANSMEM 310 332 Helical; Name=5. {ECO:0000255}.; TRANSMEM 379 399 Helical; Name=6. {ECO:0000255}.; TRANSMEM 414 433 Helical; Name=7. {ECO:0000255}. TOPO_DOM 21 155 Extracellular. {ECO:0000255}.; TOPO_DOM 179 186 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 206 227 Extracellular. {ECO:0000255}.; TOPO_DOM 254 268 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 292 309 Extracellular. {ECO:0000255}.; TOPO_DOM 333 378 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 400 413 Extracellular. {ECO:0000255}.; TOPO_DOM 434 496 Cytoplasmic. {ECO:0000255}. FUNCTION: This is a receptor for PACAP-27 and PACAP-38. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. May regulate the release of adrenocorticotropin, luteinizing hormone, growth hormone, prolactin, epinephrine, and catecholamine. May play a role in spermatogenesis and sperm motility. Causes smooth muscle relaxation and secretion in the gastrointestinal tract. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBUNIT: Interacts (via N-terminal extracellular domain) with ADCYAP1. {ECO:0000250}. +Q8VDG7 PAFA2_MOUSE Platelet-activating factor acetylhydrolase 2, cytoplasmic (EC 3.1.1.47) (Serine-dependent phospholipase A2) (SD-PLA2) 390 43,562 Active site (3); Chain (1); Initiator methionine (1); Lipidation (1); Sequence conflict (3) FUNCTION: Has a marked selectivity for phospholipids with short acyl chains at the sn-2 position. May share a common physiologic function with the plasma-type enzyme (By similarity). {ECO:0000250|UniProtKB:P79106}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P79106}. Membrane {ECO:0000250|UniProtKB:P79106}; Lipid-anchor {ECO:0000250|UniProtKB:P79106}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P79106}; Lipid-anchor {ECO:0000250|UniProtKB:P79106}. Note=In resting cells, localizes to intracellular membranes and cytoplasm. Translocates from the cytoplasm to intracellular membranes upon oxidative stress. {ECO:0000250|UniProtKB:P79106}. SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P79106}. +O35386 PAHX_MOUSE Phytanoyl-CoA dioxygenase, peroxisomal (EC 1.14.11.18) (Lupus nephritis-associated peptide 1) (Phytanic acid oxidase) (Phytanoyl-CoA alpha-hydroxylase) (PhyH) 338 38,607 Binding site (5); Chain (1); Metal binding (3); Modified residue (4); Region (1); Sequence conflict (1); Transit peptide (1) Lipid metabolism; fatty acid metabolism. FUNCTION: Converts phytanoyl-CoA to 2-hydroxyphytanoyl-CoA. SUBCELLULAR LOCATION: Peroxisome. SUBUNIT: Interacts specifically with the immunophilin FKBP52 and PHYHIP. {ECO:0000269|PubMed:10686344}. TISSUE SPECIFICITY: Ubiquitously expressed in all tissues with significant levels detected in the embryonic and neonatal heart and liver. In the adult, significant levels are detected in the liver, kidney, heart, gut, brain and aorta. {ECO:0000269|PubMed:10686344}. DISEASE: Note=Defects in Phyh are the cause of lupus nephritis, a severe autoimmune disease. Phyh could be involved in a reaction against the progression of the disease, because its expression is low in the early stage of the disease in the renal cortex of MRL/lpr mice. {ECO:0000269|PubMed:8954131}. +P12388 PAI2_MOUSE Plasminogen activator inhibitor 2, macrophage (PAI-2) (Serpin B2) 415 46,292 Chain (1); Glycosylation (4); Natural variant (4); Sequence conflict (2); Signal peptide (1); Site (1) FUNCTION: Inhibits urokinase-type plasminogen activator. The monocyte derived PAI-2 is distinct from the endothelial cell-derived PAI-1. Not required for normal murine development or survival. PTM: The signal sequence is not cleaved. SUBCELLULAR LOCATION: Cytoplasm. Secreted, extracellular space. SUBUNIT: Interacts with PSMB1. {ECO:0000250}. +Q8VE62 PAIP1_MOUSE Polyadenylate-binding protein-interacting protein 1 (PABP-interacting protein 1) (PAIP-1) (Poly(A)-binding protein-interacting protein 1) 400 45,702 Chain (1); Domain (1); Region (2); Sequence conflict (1) FUNCTION: Acts as a coactivator in the regulation of translation initiation of poly(A)-containing mRNAs. Its stimulatory activity on translation is mediated via its action on PABPC1. Competes with PAIP2 for binding to PABPC1. Its association with EIF4A and PABPC1 may potentiate contacts between mRNA termini. May also be involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. SUBUNIT: Interacts with the RRM1-RRM2 and C-terminus regions of PABPC1 in a 1:1 stoichiometry. Interacts with EIF4A (By similarity). {ECO:0000250}. DOMAIN: Only the PABPC1-interacting motif-1 (PAM1) stimulates translation initiation. {ECO:0000250}. +Q9D6V8 PAIP2_MOUSE Polyadenylate-binding protein-interacting protein 2 (PABP-interacting protein 2) (PAIP-2) (Poly(A)-binding protein-interacting protein 2) 124 14,700 Chain (1); Region (2); Sequence conflict (1) FUNCTION: Acts as a repressor in the regulation of translation initiation of poly(A)-containing mRNAs. Its inhibitory activity on translation is mediated via its action on PABPC1. Displaces the interaction of PABPC1 with poly(A) RNA and competes with PAIP1 for binding to PABPC1. Its association with PABPC1 results in disruption of the cytoplasmic poly(A) RNP structure organization (By similarity). {ECO:0000250}. PTM: Ubiquitinated, leading to its degradation by the proteasome. {ECO:0000250|UniProtKB:Q9BPZ3}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with the second and third RRM domains and C-terminus regions of PABPC1 in a 2:1 stoichiometry. {ECO:0000250}. DOMAIN: Only the PABPC1-interacting motif-1 (PAM1) interferes with the binding of PABPC1 to poly(A) RNA and translation initiation. {ECO:0000250}. TISSUE SPECIFICITY: Expressed at high levels in testis with expression also detected in heart, brain, lung, liver, kidney, pancreas and small intestine (at protein level). {ECO:0000269|PubMed:16804161}. +Q61036 PAK3_MOUSE Serine/threonine-protein kinase PAK 3 (EC 2.7.11.1) (Beta-PAK) (CDC42/RAC effector kinase PAK-B) (p21-activated kinase 3) (PAK-3) 559 62,398 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Compositional bias (1); Domain (2); Helix (1); Modified residue (6); Mutagenesis (2); Nucleotide binding (1); Region (3); Sequence conflict (6) FUNCTION: Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell migration, or cell cycle regulation. Plays a role in dendrite spine morphogenesis as well as synapse formation and plasticity (PubMed:25851601). Acts as downstream effector of the small GTPases CDC42 and RAC1. Activation by the binding of active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Phosphorylates MAPK4 and MAPK6 and activates the downstream target MAPKAPK5, a regulator of F-actin polymerization and cell migration. Additionally, phosphorylates TNNI3/troponin I to modulate calcium sensitivity and relaxation kinetics of thin myofilaments. May also be involved in early neuronal development. {ECO:0000269|PubMed:12242269, ECO:0000269|PubMed:15574732, ECO:0000269|PubMed:17537723, ECO:0000269|PubMed:20540949, ECO:0000269|PubMed:25851601}. PTM: Autophosphorylated when activated by CDC42/p21.; PTM: Neddylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Interacts tightly with GTP-bound but not GDP-bound CDC42/p21 and RAC1. Shows highly specific binding to the SH3 domains of phospholipase C-gamma and of adapter protein NCK. Interacts with the C-terminal of APP. Interacts with ARHGEF6 and ARHGEF7 (By similarity). {ECO:0000250}. +Q8BTW9 PAK4_MOUSE Serine/threonine-protein kinase PAK 4 (EC 2.7.11.1) (p21-activated kinase 4) (PAK-4) 593 64,623 Active site (1); Binding site (1); Chain (1); Compositional bias (4); Domain (2); Erroneous initiation (1); Modified residue (12); Nucleotide binding (1); Region (1); Sequence conflict (3) FUNCTION: Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell migration, growth, proliferation or cell survival. Activation by various effectors including growth factor receptors or active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Phosphorylates and inactivates the protein phosphatase SSH1, leading to increased inhibitory phosphorylation of the actin binding/depolymerizing factor cofilin. Decreased cofilin activity may lead to stabilization of actin filaments. Phosphorylates LIMK1, a kinase that also inhibits the activity of cofilin. Phosphorylates integrin beta5/ITGB5 and thus regulates cell motility. Phosphorylates ARHGEF2 and activates the downstream target RHOA that plays a role in the regulation of assembly of focal adhesions and actin stress fibers. Stimulates cell survival by phosphorylating the BCL2 antagonist of cell death BAD. Alternatively, inhibits apoptosis by preventing caspase-8 binding to death domain receptors in a kinase independent manner. Plays a role in cell-cycle progression by controlling levels of the cell-cycle regulatory protein CDKN1A and by phosphorylating RAN. {ECO:0000269|PubMed:11413130, ECO:0000269|PubMed:21381077}. PTM: Autophosphorylated on serine residues when activated by CDC42/p21 (By similarity). Phosphorylated on tyrosine residues upon stimulation of FGFR2 (PubMed:12529371). {ECO:0000250|UniProtKB:O96013, ECO:0000269|PubMed:12529371}.; PTM: Polyubiquitinated, leading to its proteasomal degradation. {ECO:0000250|UniProtKB:O96013}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O96013}. Note=Seems to shuttle between cytoplasmic compartments depending on the activating effector. For example, can be found on the cell periphery after activation of growth-factor or integrin-mediated signaling pathways. {ECO:0000250|UniProtKB:O96013}. SUBUNIT: Interacts tightly with GTP-bound but not GDP-bound CDC42/p21 and weakly with RAC1 (By similarity). Interacts with FGFR2 and GRB2 (PubMed:12529371). Interacts with INKA1. Interacts with SH3RF2 (By similarity). {ECO:0000250|UniProtKB:O96013, ECO:0000269|PubMed:12529371}. +Q8C015 PAK5_MOUSE Serine/threonine-protein kinase PAK 5 (EC 2.7.11.1) (p21-activated kinase 5) (PAK-5) (p21-activated kinase 7) (PAK-7) 719 80,948 Active site (1); Binding site (1); Chain (1); Compositional bias (3); Domain (2); Modified residue (2); Nucleotide binding (1); Region (1); Sequence conflict (6) FUNCTION: Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell migration, proliferation or cell survival. Activation by various effectors including growth factor receptors or active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Phosphorylates the proto-oncogene RAF1 and stimulates its kinase activity. Promotes cell survival by phosphorylating the BCL2 antagonist of cell death BAD. Phosphorylates CTNND1, probably to regulate cytoskeletal organization and cell morphology. Keeps microtubules stable through MARK2 inhibition and destabilizes the F-actin network leading to the disappearance of stress fibers and focal adhesions (By similarity). {ECO:0000250, ECO:0000269|PubMed:11756552}. PTM: Autophosphorylated when activated by CDC42/p21. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Shuttles between the nucleus and the mitochondria, and mitochondrial localization is essential for the role in cell survival. {ECO:0000250}. SUBUNIT: Interacts tightly with GTP-bound but not GDP-bound CDC42/p21 and RAC1. Interacts with MARK2, leading to inhibit MARK2 independently of kinase activity. Interacts with RHOD and RHOH (By similarity). {ECO:0000250}. DOMAIN: An autoinhibitory domain is present in the N-terminal region of the protein. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in brain and eye. Also expressed in adrenal gland, pancreas, prostate and testes. Within the brain, expression is restricted to neurons. Present in brain but not in kidney, lung and spleen (at protein level). {ECO:0000269|PubMed:14517284}. +Q9ET54 PALLD_MOUSE Palladin 1408 152,131 Alternative sequence (6); Beta strand (7); Chain (1); Compositional bias (2); Disulfide bond (3); Domain (5); Erroneous initiation (1); Frameshift (1); Modified residue (17); Region (8); Sequence conflict (2); Turn (1) FUNCTION: Cytoskeletal protein required for organization of normal actin cytoskeleton. Roles in establishing cell morphology, motility, cell adhesion and cell-extracellular matrix interactions in a variety of cell types. May function as a scaffolding molecule with the potential to influence both actin polymerization and the assembly of existing actin filaments into higher-order arrays. Binds to proteins that bind to either monomeric or filamentous actin. Localizes at sites where active actin remodeling takes place, such as lamellipodia and membrane ruffles. Different isoforms may have functional differences. Involved in the control of morphological and cytoskeletal changes associated with dendritic cell maturation. Involved in targeting ACTN to specific May be required for the initiation of neural tube closure. {ECO:0000269|PubMed:10931874, ECO:0000269|PubMed:15950489, ECO:0000269|PubMed:16492705, ECO:0000269|PubMed:17115415}. PTM: Phosphorylated predominantly on serines and, to a lesser extent, on tyrosines. Phosphorylation at Ser-1143 by PKB/AKT1 modulates cytoskeletal organization and cell motility (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10931874}. Cell junction, focal adhesion {ECO:0000269|PubMed:10931874}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:10931874}. Cell projection, ruffle {ECO:0000250|UniProtKB:Q8WX93}. Cell projection, podosome {ECO:0000250|UniProtKB:P0C5E3}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q8WX93}. Cell projection, axon {ECO:0000250|UniProtKB:P0C5E3}. Cell projection, growth cone {ECO:0000250|UniProtKB:P0C5E3}. Note=Localizes to stress fibers and Z lines (PubMed:10931874). Preferentially expressed in the excitatory presynaptic terminals (By similarity). {ECO:0000250|UniProtKB:P0C5E3, ECO:0000269|PubMed:10931874}. SUBUNIT: Interacts with EPS8 (PubMed:16868024). Interacts with LASP1 (PubMed:16492705). Interacts with VASP (PubMed:14983521). Interacts with ACTN (By similarity). Interacts with ARGBP2 (By similarity). Interacts with PFN1 (By similarity). Interacts with LPP (By similarity). Interacts with SPIN90 (By similarity). Interacts with SRC (By similarity). Interacts with EZR (By similarity). Interacts with RAI14 (By similarity). {ECO:0000250|UniProtKB:P0C5E3, ECO:0000250|UniProtKB:Q8WX93, ECO:0000269|PubMed:14983521, ECO:0000269|PubMed:16492705, ECO:0000269|PubMed:16868024}. TISSUE SPECIFICITY: Detected in both muscle and non-muscle tissues and cells (at protein level). Isoform 3 is widely expressed, isoform 4 is particularly abundant in tissues rich in smooth muscle and in the cardiac muscle and isoform 1 is detected in heart. {ECO:0000269|PubMed:10931874, ECO:0000269|PubMed:11438925}. +Q8BR92 PALM2_MOUSE Paralemmin-2 376 42,095 Chain (1); Coiled coil (2); Lipidation (3); Modified residue (3); Propeptide (1) SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. +A2TJV2 PALM3_MOUSE Paralemmin-3 734 78,788 Chain (1); Coiled coil (2); Compositional bias (1); Erroneous initiation (1); Lipidation (3); Modified residue (13); Propeptide (1); Sequence caution (1) FUNCTION: ATP-binding protein, which may act as a adapter in the Toll-like receptor (TLR) signaling. {ECO:0000250}. PTM: Palmitoylated on Cys-728 and Cys-730 and prenylated on Cys-731; which is required for membrane association. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. SUBUNIT: Interacts with SIGIRR. {ECO:0000250}. +Q3ULB5 PAK6_MOUSE Serine/threonine-protein kinase PAK 6 (EC 2.7.11.1) (p21-activated kinase 6) (PAK-6) 682 74,867 Active site (1); Binding site (1); Chain (1); Compositional bias (1); Domain (2); Modified residue (1); Nucleotide binding (1); Region (1); Sequence conflict (2) FUNCTION: Serine/threonine protein kinase that plays a role in the regulation of gene transcription. The kinase activity is induced by various effectors including AR or MAP2K6/MAPKK6. Phosphorylates the DNA-binding domain of androgen receptor/AR and thereby inhibits AR-mediated transcription. Inhibits also ESR1-mediated transcription. May play a role in cytoskeleton regulation by interacting with IQGAP1. May protect cells from apoptosis through phosphorylation of BAD (By similarity). {ECO:0000250}. PTM: Autophosphorylated. Phosphorylated by MAP2K6/MAPKK6, leading to PAK6 activation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Cotranslocates into nucleus with AR in response to androgen induction. {ECO:0000250}. SUBUNIT: Interacts tightly with GTP-bound but not GDP-bound CDC42/p21 and RAC1. Interacts with the androgen receptor AR. Interacts with IQGAP1 and PPM1B (By similarity). {ECO:0000250}. +Q9Z0P4 PALM_MOUSE Paralemmin-1 (Paralemmin) 383 41,614 Alternative sequence (1); Chain (1); Coiled coil (1); Lipidation (3); Modified residue (18); Mutagenesis (1); Propeptide (1) FUNCTION: Involved in plasma membrane dynamics and cell process formation. Isoform 1 and isoform 2 are necessary for axonal and dendritic filopodia induction, for dendritic spine maturation and synapse formation in a palmitoylation-dependent manner. {ECO:0000269|PubMed:18287537}. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. Cell projection, filopodium membrane; Lipid-anchor. Cell projection, axon {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cell projection, dendritic spine. Basolateral cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Apicolateral cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Note=Translocation to the plasma membrane is enhanced upon stimulation of neuronal activity. {ECO:0000250}. SUBUNIT: Interacts with dopamine receptor DRD3. {ECO:0000250}. TISSUE SPECIFICITY: Expression is highest in brain, intermediate in adrenal gland and kidney, and much lower or undetectable in other tissues. Isoform 1 is the predominant isoform in most tissues except brain and kidney where isoform 2 predominates. {ECO:0000269|PubMed:9813098}. +Q640Q5 PAN3_MOUSE PAN2-PAN3 deadenylation complex subunit Pan3 (PAB1P-dependent poly(A)-specific ribonuclease) (Poly(A)-nuclease deadenylation complex subunit 3) (PAN deadenylation complex subunit 3) 837 89,745 Alternative sequence (2); Binding site (1); Chain (1); Coiled coil (1); Erroneous translation (1); Modified residue (2); Motif (1); Nucleotide binding (2); Region (2); Sequence caution (2); Zinc finger (1) FUNCTION: Regulatory subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in general and miRNA-mediated mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein (PABP). PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by XRN1. PAN3 acts as a positive regulator for PAN activity, recruiting the catalytic subunit PAN2 to mRNA via its interaction with RNA and PABP, and to miRNA targets via its interaction with GW182 family proteins. {ECO:0000255|HAMAP-Rule:MF_03181}. SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000255|HAMAP-Rule:MF_03181, ECO:0000269|PubMed:18625844}. SUBUNIT: Homodimer. Forms a heterotrimer with a catalytic subunit PAN2 to form the poly(A)-nuclease (PAN) deadenylation complex. Interacts (via PAM-2 motif) with poly(A)-binding protein PABPC1 (via PABC domain), conferring substrate specificity of the enzyme complex. Interacts with the GW182 family proteins TNRC6A, TNRC6B and TNRC6C. {ECO:0000255|HAMAP-Rule:MF_03181}. DOMAIN: The N-terminal zinc finger binds to poly(A) RNA. {ECO:0000255|HAMAP-Rule:MF_03181}.; DOMAIN: Contains a pseudokinase domain. The protein kinase domain is predicted to be catalytically inactive because some of the residues important for catalytic activity are substituted and it lacks the equivalent of the binding site for a peptide substrate. However, it has retained an ATP-binding site and ATP-binding is required for mRNA degradation, stimulating the activity of the PAN2 nuclease in vitro. The nucleotide-binding site is juxtaposed to the RNase active site of PAN2 in the complex and may actually bind nucleosides of a poly(A) RNA rather than ATP, feeding the poly(A)-tail to the active site of the deadenylase and thus increasing the efficiency with which this distributive enzyme degrades oligo(A) RNAs. {ECO:0000255|HAMAP-Rule:MF_03181}.; DOMAIN: The pseudokinase domain, the coiled-coil (CC), and C-terminal knob domain (CK) form a structural unit (PKC) that forms an extensive high-affinity interaction surface for PAN2. {ECO:0000255|HAMAP-Rule:MF_03181}. +Q8C0L6 PAOX_MOUSE Peroxisomal N(1)-acetyl-spermine/spermidine oxidase (EC 1.5.3.13) (Polyamine oxidase) 504 55,447 Alternative sequence (2); Beta strand (24); Chain (1); Helix (20); Motif (1); Turn (5) Amine and polyamine metabolism; spermine metabolism. FUNCTION: Flavoenzyme which catalyzes the oxidation of N(1)-acetylspermine to spermidine and is thus involved in the polyamine back-conversion. Can also oxidize N(1)-acetylspermidine to putrescine. Substrate specificity: N(1)-acetylspermine = N(1)-acetylspermidine > N(1),N(12)-diacylspermine >> spermine. Does not oxidize spermidine. Plays an important role in the regulation of polyamine intracellular concentration and has the potential to act as a determinant of cellular sensitivity to the antitumor polyamine analogs. SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}. Cytoplasm {ECO:0000250}. SUBUNIT: Monomer. TISSUE SPECIFICITY: Widely expressed at different developmental stages. Expressed at high level in the liver and the stomach, expressed at lower level in heart, spleen, thymus, small intestine, muscle, pancreas, uterus, and breast and expressed at very low level in brain, kidney, lung, testis, skin, adrenal gland and prostate gland. {ECO:0000269|PubMed:12660232}. +P11103 PARP1_MOUSE Poly [ADP-ribose] polymerase 1 (PARP-1) (EC 2.4.2.30) (ADP-ribosyltransferase diphtheria toxin-like 1) (ARTD1) (DNA ADP-ribosyltransferase PARP1) (EC 2.4.2.-) (NAD(+) ADP-ribosyltransferase 1) (ADPRT 1) (Poly[ADP-ribose] synthase 1) (msPARP) (Protein poly-ADP-ribosyltransferase PARP1) (EC 2.4.2.-) 1013 113,100 Alternative sequence (1); Chain (1); Cross-link (11); DNA binding (1); Domain (3); Erroneous initiation (1); Initiator methionine (1); Modified residue (32); Motif (2); Region (1); Sequence conflict (9); Zinc finger (2) FUNCTION: Poly-ADP-ribosyltransferase that mediates poly-ADP-ribosylation of proteins and plays a key role in DNA repair. Mainly mediates glutamate and aspartate ADP-ribosylation of target proteins: the ADP-D-ribosyl group of NAD(+) is transferred to the acceptor carboxyl group of glutamate and aspartate residues and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units. Mediates the poly(ADP-ribosyl)ation of a number of proteins, including itself, APLF and CHFR. Also mediates serine ADP-ribosylation of target proteins following interaction with HPF1; HPF1 conferring serine specificity. Probably also catalyzes tyrosine ADP-ribosylation of target proteins following interaction with HPF1. Catalyzes the poly-ADP-ribosylation of histones in a HPF1-dependent manner. Involved in the base excision repair (BER) pathway by catalyzing the poly-ADP-ribosylation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. ADP-ribosylation follows DNA damage and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks. In addition to base excision repair (BER) pathway, also involved in double-strand breaks (DSBs) repair: together with TIMELESS, accumulates at DNA damage sites and promotes homologous recombination repair by mediating poly-ADP-ribosylation. In addition to proteins, also able to ADP-ribosylate DNA: catalyzes ADP-ribosylation of DNA strand break termini containing terminal phosphates and a 2'-OH group in single- and double-stranded DNA, respectively. Required for PARP9 and DTX3L recruitment to DNA damage sites. PARP1-dependent PARP9-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage sites. Acts as a regulator of transcription: positively regulates the transcription of MTUS1 and negatively regulates the transcription of MTUS2/TIP150. With EEF1A1 and TXK, forms a complex that acts as a T-helper 1 (Th1) cell-specific transcription factor and binds the promoter of IFN-gamma to directly regulate its transcription, and is thus involved importantly in Th1 cytokine production. Involved in the synthesis of ATP in the nucleus, together with NMNAT1, PARG and NUDT5. Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming. {ECO:0000250|UniProtKB:P09874}. PTM: S-nitrosylated, leading to inhibit transcription regulation activity. {ECO:0000269|PubMed:16464859}.; PTM: Phosphorylated by PRKDC and TXK. {ECO:0000250|UniProtKB:P09874}.; PTM: Poly-ADP-ribosylated on glutamate and aspartate residues by autocatalysis. Poly-ADP-ribosylated by PARP2; poly-ADP-ribosylation mediates the recruitment of CHD1L to DNA damage sites. ADP-ribosylated on serine by autocatalysis; serine ADP-ribosylation takes place following interaction with HPF1. {ECO:0000250|UniProtKB:P09874}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P09874}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P09874}. Chromosome {ECO:0000250|UniProtKB:P09874}. Note=Localizes to sites of DNA damage. {ECO:0000250|UniProtKB:P09874}. SUBUNIT: Homo- and heterodimer with PARP2 (By similarity). Interacts with APTX (By similarity). Component of a base excision repair (BER) complex, containing at least XRCC1, PARP1, PARP2, POLB and LRIG3 (PubMed:11948190). Interacts with SRY (By similarity). The SWAP complex consists of NPM1, NCL, PARP1 and SWAP70 (PubMed:9642267). Interacts with TIAM2 (PubMed:17320046). Interacts with PARP3; leading to activate PARP1 in absence of DNA (By similarity). Interacts (when poly-ADP-ribosylated) with CHD1L (By similarity). Interacts with the DNA polymerase alpha catalytic subunit POLA1; this interaction functions as part of the control of replication fork progression (By similarity). Interacts with EEF1A1 and TXK (By similarity). Interacts with RNF4 (PubMed:19779455). Interacts with RNF146 (By similarity). Interacts with ZNF423 (PubMed:14623329). Interacts with APLF (By similarity). Interacts with SNAI1 (via zinc fingers); the interaction requires SNAI1 to be poly-ADP-ribosylated and non-phosphorylated (active) by GSK3B (PubMed:21577210). Interacts (when poly-ADP-ribosylated) with PARP9 (By similarity). Interacts with NR4A3; activates PARP1 by improving acetylation of PARP1 and suppressing the interaction between PARP1 and SIRT1 (By similarity). Interacts (via catalytic domain) with PUM3; the interaction inhibits the poly-ADP-ribosylation activity of PARP1 and the degradation of PARP1 by CASP3 following genotoxic stress (By similarity). Interacts (via the PARP catalytic domain) with HPF1 (By similarity). Interacts with ZNF365 (By similarity). Interacts with RRP1B (By similarity). Interacts with TIMELESS; the interaction is direct (By similarity). Interacts with CGAS; leading to impede the formation of the PARP1-TIMELESS complex (By similarity). {ECO:0000250|UniProtKB:P09874, ECO:0000250|UniProtKB:P27008, ECO:0000269|PubMed:11948190, ECO:0000269|PubMed:14623329, ECO:0000269|PubMed:17320046, ECO:0000269|PubMed:19779455, ECO:0000269|PubMed:21577210, ECO:0000269|PubMed:9642267}. TISSUE SPECIFICITY: Widely expressed (PubMed:9642267). Expression is correlated with proliferation, with higher levels occurring during early fetal development and organogenesis and in the highly proliferative cell compartments of adult (PubMed:9642267). Expressed in B-cells that have been induced to switch to various Ig isotypes (PubMed:9642267). {ECO:0000269|PubMed:9642267}. +Q80ZE5 PAQR8_MOUSE Membrane progestin receptor beta (mPR beta) (Lysosomal membrane protein in brain 1) (Membrane progesterone P4 receptor beta) (Membrane progesterone receptor beta) (Progesterone and adipoQ receptor family member 8) (Progestin and adipoQ receptor family member 8) (Progestin and adipoQ receptor family member VIII) 354 40,430 Chain (1); Frameshift (1); Sequence conflict (5); Topological domain (8); Transmembrane (7) TRANSMEM 77 97 Helical; Name=1. {ECO:0000255}.; TRANSMEM 112 132 Helical; Name=2. {ECO:0000255}.; TRANSMEM 174 194 Helical; Name=3. {ECO:0000255}.; TRANSMEM 214 234 Helical; Name=4. {ECO:0000255}.; TRANSMEM 244 264 Helical; Name=5. {ECO:0000255}.; TRANSMEM 284 304 Helical; Name=6. {ECO:0000255}.; TRANSMEM 316 336 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 76 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 98 111 Extracellular. {ECO:0000255}.; TOPO_DOM 133 173 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 195 213 Extracellular. {ECO:0000255}.; TOPO_DOM 235 243 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 265 283 Extracellular. {ECO:0000255}.; TOPO_DOM 305 315 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 337 354 Extracellular. {ECO:0000255}. FUNCTION: Plasma membrane progesterone (P4) receptor coupled to G proteins. Seems to act through a G(i) mediated pathway (By similarity). May be involved in oocyte maturation (PubMed:12601167). Also binds dehydroepiandrosterone (DHEA), pregnanolone, pregnenolone and allopregnanolone (By similarity). {ECO:0000250|UniProtKB:Q8TEZ7, ECO:0000269|PubMed:12601167}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8TEZ7}; Multi-pass membrane protein {ECO:0000255}. Note=Colocalizes with a lysosomal protein CTSD/cathepsin D. {ECO:0000250|UniProtKB:Q8TEZ7}. TISSUE SPECIFICITY: Expressed in brain and testis. {ECO:0000269|PubMed:11676489}. +Q8VI36 PAXI_MOUSE Paxillin 591 64,476 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (4); Helix (1); Modified residue (25); Motif (5); Sequence conflict (3) FUNCTION: Cytoskeletal protein involved in actin-membrane attachment at sites of cell adhesion to the extracellular matrix (focal adhesion). {ECO:0000250}. PTM: Phosphorylated by MAPK1/ERK2. Phosphorylated on tyrosine residues during integrin-mediated cell adhesion, embryonic development, fibroblast transformation and following stimulation of cells by mitogens. Phosphorylation at Ser-244 by CDK5 reduces its interaction with PTK2/FAK1 in matrix-cell focal adhesions (MCFA) during oligodendrocytes (OLs) differentiation (By similarity). Phosphorylation at Tyr-31 and Tyr-118 by PTK6 promote the activation of RAC1 via CRK/CrKII, thereby promoting migration and invasion (By similarity). Phosphorylation at Ser-250 by SLK is required for PXN redistribution and cell motility (By similarity). {ECO:0000250|UniProtKB:P49023}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P49023}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:P49023}. Cytoplasm, cell cortex {ECO:0000269|PubMed:8940124}. Note=Colocalizes with integrins at the cell periphery. Colocalizes with PXN to membrane ruffles and the leading edge of migrating cells (By similarity). {ECO:0000250|UniProtKB:P49023}. SUBUNIT: Interacts with VCL and SRC (via SH3 domain). Interacts with GIT1, NUDT16L1/SDOS and TGFB1I1. Component of cytoplasmic complexes, which also contain GIT1, ARHGEF6 and PAK1. Binds ASAP2. Interacts with RNF5 and PDCD10 (By similarity). Interacts with SORBS1, PARVA and PARVB. Interacts with NEK3 and this interaction is prolactin-dependent (By similarity). Interacts with PTK2/FAK1. Interacts with PTK6 (By similarity). Interacts with PTK2B/PYK2. Interacts with CD36. Interacts (via cytoplasmic domain) with CEACAM1; the interaction is phosphotyrosyl-dependent (By similarity). Interacts with LIMA1; this complex stabilizes actin dynamics (By similarity). {ECO:0000250|UniProtKB:P49023, ECO:0000269|PubMed:11134073, ECO:0000269|PubMed:11799401, ECO:0000269|PubMed:8940124}. +Q9EPC1 PARVA_MOUSE Alpha-parvin (Actopaxin) 372 42,330 Chain (1); Domain (2); Initiator methionine (1); Modified residue (6); Region (1); Sequence conflict (2) FUNCTION: Plays a role in the reorganization of the actin cytoskeleton, formation of lamellipodia and ciliogenesis. Plays a role in the establishement of cell polarity, cell adhesion, cell spreading, and directed cell migration. Plays a role in sarcomere organization and in smooth muscle cell contraction. Required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Plays a role in sprouting angiogenesis and is required for normal adhesion of vascular smooth muscle cells to endothelial cells during blood vessel development. {ECO:0000269|PubMed:11134073, ECO:0000269|PubMed:19798050}. SUBCELLULAR LOCATION: Cell junction, focal adhesion. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Cytoplasm, myofibril, sarcomere, Z line. Note=Constituent of focal adhesions. SUBUNIT: Interacts with ARHGAP31. Interacts with TGFB1I1. Interacts with ILK, LIMS1 and PXN (via LD motifs). Interacts with the actin cytoskeleton. {ECO:0000269|PubMed:11134073, ECO:0000269|PubMed:16860736}. +Q9ERD8 PARVG_MOUSE Gamma-parvin 331 37,603 Chain (1); Domain (2); Modified residue (1); Sequence conflict (3) FUNCTION: Probably plays a role in the regulation of cell adhesion and cytoskeleton organization. {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, focal adhesion. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Constituent of focal adhesions. {ECO:0000250}. SUBUNIT: Interacts with integrin-linked protein kinase and actin. {ECO:0000250}. TISSUE SPECIFICITY: Expressed strongly in spleen and testis, moderately in lung and weakly in brain and heart. {ECO:0000269|PubMed:11722847}. +O08976 PBAS_MOUSE Probasin (PB) 174 20,372 Chain (1); Disulfide bond (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q9D0B6 PBDC1_MOUSE Protein PBDC1 (Polysaccharide biosynthesis domain-containing protein 1) 198 22,223 Alternative sequence (1); Chain (1); Modified residue (2) +Q08351 TPOR_MOUSE Thrombopoietin receptor (TPO-R) (Myeloproliferative leukemia protein) (Proto-oncogene c-Mpl) (CD antigen CD110) 625 69,788 Alternative sequence (2); Chain (1); Compositional bias (1); Cross-link (2); Domain (2); Glycosylation (1); Motif (2); Sequence conflict (6); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 483 504 Helical. {ECO:0000255}. TOPO_DOM 26 482 Extracellular. {ECO:0000255}.; TOPO_DOM 505 625 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for thrombopoietin that acts as a primary regulator of megakaryopoiesis and platelet production. May represent a regulatory molecule specific for TPO-R-dependent immune responses. {ECO:0000269|PubMed:15210714}.; FUNCTION: Isoform Mpl-tr: Acts as an inhibitor of thrombopoietin signaling by promoting protein down-regulation of full-length isoform Mpl-fl. {ECO:0000269|PubMed:15210714}. PTM: Ubiquitination at Lys-544 and Lys-564 targets MPL for degradation by both the lysosomal and proteasomal pathways. The E3 ubiquitin-protein ligase CBL significantly contributes to this ubiquitination (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P40238}. Golgi apparatus {ECO:0000250|UniProtKB:P40238}. Cell surface {ECO:0000250|UniProtKB:P40238}. SUBUNIT: Homodimer. Interacts with ATXN2L. {ECO:0000250|UniProtKB:P40238}. DOMAIN: The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.; DOMAIN: The box 1 motif is required for JAK interaction and/or activation. +Q9CRB6 TPPP3_MOUSE Tubulin polymerization-promoting protein family member 3 176 18,965 Beta strand (4); Chain (1); Helix (6); Initiator methionine (1); Modified residue (1) FUNCTION: Binds tubulin and has microtubule bundling activity. May play a role in cell proliferation and mitosis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. +Q8VD31 TPSNR_MOUSE Tapasin-related protein (TAPASIN-R) (TAP-binding protein-like) (TAP-binding protein-related protein) (TAPBP-R) (Tapasin-like) 451 48,733 Chain (1); Disulfide bond (2); Domain (2); Glycosylation (2); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 413 433 Helical. {ECO:0000255}. TOPO_DOM 21 412 Lumenal. {ECO:0000255}.; TOPO_DOM 434 451 Cytoplasmic. {ECO:0000255}. FUNCTION: Component of the antigen processing and presentation pathway, which binds to MHC class I coupled with beta2-microglobulin/B2M. Association between TAPBPR and MHC class I occurs in the absence of a functional peptide-loading complex (PLC). Expression seems to slow down and down-regulate MHC class I surface expression. {ECO:0000250|UniProtKB:Q9BX59}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9BX59}; Single-pass type I membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9BX59}; Single-pass type I membrane protein {ECO:0000250}. Microsome membrane {ECO:0000250|UniProtKB:Q9BX59}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9BX59}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9BX59}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9BX59}. Note=Mainly found in endoplasmic reticulum but a minority is found on the cell surface. {ECO:0000250|UniProtKB:Q9BX59}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11920573}. +Q8QZZ7 TPRKB_MOUSE EKC/KEOPS complex subunit Tprkb (PRPK-binding protein) (TP53RK-binding protein) 175 19,556 Chain (1) FUNCTION: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. TPRKB acts as an allosteric effector that regulates the t(6)A activity of the complex. TPRKB is not required for tRNA modification. {ECO:0000250|UniProtKB:Q9Y3C4}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9Y3C4}. Nucleus {ECO:0000250|UniProtKB:Q9Y3C4}. SUBUNIT: Component of the EKC/KEOPS complex composed of at least GON7, TP53RK, TPRKB, OSGEP and LAGE3; the whole complex dimerizes. Interacts with TP53RK/PRPK. {ECO:0000250|UniProtKB:Q9Y3C4}. +Q64707 U2AFL_MOUSE U2 small nuclear ribonucleoprotein auxiliary factor 35 kDa subunit-related protein 1 (CCCH type zinc finger, RNA-binding motif and serine/arginine rich protein 1) (SP2) (U2(RNU2) small nuclear RNA auxiliary factor 1-like 1) 428 51,364 Chain (1); Compositional bias (2); Domain (1); Modified residue (3); Sequence conflict (1); Zinc finger (2) FUNCTION: Plays a role in splicing of the U12-type introns (PubMed:29617656). Implicated also in removal of U2 introns positioned adjacent to a U12 intron (PubMed:29617656). {ECO:0000269|PubMed:29617656}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with SF3B1 (PubMed:29617656). Interacts with ZCRB1 (PubMed:29617656). {ECO:0000269|PubMed:29617656}. TISSUE SPECIFICITY: Highest expression levels are detected in the brain, and lower expression levels in other tissues like epididymis, testis, bone marrow or muscle (PubMed:29617656). In testis, expressed in both Sertoli and spermatogenic cell (PubMed:29617656). {ECO:0000269|PubMed:29617656}. +Q78JW9 UBFD1_MOUSE Ubiquitin domain-containing protein UBFD1 368 40,143 Beta strand (5); Chain (1); Compositional bias (1); Domain (1); Helix (2) +Q3USZ2 UBFL1_MOUSE Upstream-binding factor 1-like protein 1 (HMG-box preimplantation embryo-specific protein) (HMGPI) 394 46,131 Chain (1); DNA binding (2); Sequence conflict (1) FUNCTION: Essential for proliferation of the inner cell mass and trophectodermal cells in peri-implantation development. {ECO:0000269|PubMed:19915186}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19915186}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267, ECO:0000269|PubMed:19915186}. Note=Mainly cytoplasmic from the 4-cell stage to the morula stage. Becomes nuclear at the blastocyst stage. In ES cells, found in both the nucleus and the cytoplasm. {ECO:0000269|PubMed:19915186}. +Q80U95 UBE3C_MOUSE Ubiquitin-protein ligase E3C (EC 2.3.2.26) (HECT-type ubiquitin transferase E3C) 1083 123,976 Active site (1); Chain (1); Domain (2); Erroneous initiation (1); Region (1); Sequence conflict (1) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that accepts ubiquitin from the E2 ubiquitin-conjugating enzyme UBE2D1 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Can assemble unanchored poly-ubiquitin chains in either 'Lys-29'- or 'Lys-48'-linked polyubiquitin chains. Has preference for 'Lys-48' linkages. It can target itself for ubiquitination in vitro and may promote its own degradation in vivo. {ECO:0000250|UniProtKB:Q15386}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Interacts with 26S proteasomes. Interacts (via the N-terminal) with CAND2; the interaction stimulates ubiquitination of CAND2 in vitro (By similarity). {ECO:0000250}. DOMAIN: The C-terminal is necessary and sufficient for the poly-ubiquitin chain assembly. {ECO:0000250}. +Q5FWH2 UNKL_MOUSE Putative E3 ubiquitin-protein ligase UNKL (EC 2.3.2.-) (RING finger protein unkempt-like) 727 79,636 Alternative sequence (4); Chain (1); Compositional bias (3); Sequence conflict (1); Zinc finger (5) Protein modification; protein ubiquitination. FUNCTION: May participate in a protein complex showing an E3 ligase activity regulated by Rac1. Ubiquitination is directed towards itself and possibly other substrates, such as Baf60b/Smarcd2. Intrinsic E3 ligase activity has not been proven. {ECO:0000250}. PTM: Ubiquitination is enhanced by activated Rac1. The presence of the RING finger domain is not essential for ubiquitination to occur (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Primarily localized in the cytoplasm but has the ability to shuttle between the nucleus and the cytoplasm. {ECO:0000250}. SUBUNIT: Interacts with the GTP-bound form of Rac1. Interacts with Baf60b/Smarcd2 (By similarity). {ECO:0000250}. DOMAIN: Although this protein contains a RING domain, intrinsic E3 ligase activity has not been proven. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. +Q9JKX8 UPK3A_MOUSE Uroplakin-3a (UP3a) (Uroplakin III) (UPIII) 287 30,990 Chain (1); Glycosylation (3); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 208 235 Helical. {ECO:0000255}. TOPO_DOM 19 207 Lumenal. {ECO:0000255}.; TOPO_DOM 236 287 Cytoplasmic. {ECO:0000255}. FUNCTION: Component of the asymmetric unit membrane (AUM); a highly specialized biomembrane elaborated by terminally differentiated urothelial cells. May play an important role in AUM-cytoskeleton interaction in terminally differentiated urothelial cells. It also contributes to the formation of urothelial glycocalyx which may play an important role in preventing bacterial adherence (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Heterodimer formation with UPK1B is a prerequisite to exit out of the endoplasmic reticulum (ER). {ECO:0000250}. SUBUNIT: Heterodimer with uroplakin-1B (UPK1B). {ECO:0000250}. +Q80YF6 UPK3B_MOUSE Uroplakin-3b (UP3b) (Uroplakin IIIb) (UPIIIb) (p35) 275 30,227 Alternative sequence (1); Chain (1); Glycosylation (1); Sequence caution (1); Sequence conflict (5); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 197 217 Helical. {ECO:0000255}. TOPO_DOM 27 196 Lumenal. {ECO:0000255}.; TOPO_DOM 218 275 Cytoplasmic. {ECO:0000255}. FUNCTION: Component of the asymmetric unit membrane (AUM); a highly specialized biomembrane elaborated by terminally differentiated urothelial cells. May play an important role in AUM-cytoskeleton interaction in terminally differentiated urothelial cells. It also contributes to the formation of urothelial glycocalyx which may play an important role in preventing bacterial adherence (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Heterodimer formation with UPK1B is a prerequisite to exit out of the endoplasmic reticulum (ER). {ECO:0000269|PubMed:12446744}. SUBUNIT: Heterodimer with uroplakin-1B (UPK1B). TISSUE SPECIFICITY: Expression is urothelium-specific. {ECO:0000269|PubMed:12446744}. +B1AVZ0 UPP_MOUSE Uracil phosphoribosyltransferase homolog 310 34,278 Binding site (5); Chain (1); Modified residue (1); Nucleotide binding (1); Region (2) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. +Q8K1B8 URP2_MOUSE Fermitin family homolog 3 (Kindlin-3) (Unc-112-related protein 2) 665 75,635 Beta strand (7); Chain (1); Domain (2); Helix (2); Modified residue (4); Mutagenesis (1); Turn (2) FUNCTION: Plays a central role in cell adhesion in hematopoietic cells (By similarity). Acts by activating the integrin beta-1-3 (ITGB1, ITGB2 and ITGB3) (PubMed:18278053). Required for integrin-mediated platelet adhesion and leukocyte adhesion to endothelial cells (PubMed:19234461). Required for activation of integrin beta-2 (ITGB2) in polymorphonuclear granulocytes (PMNs) (PubMed:18278053). {ECO:0000250|UniProtKB:Q86UX7, ECO:0000269|PubMed:18278053, ECO:0000269|PubMed:18662549, ECO:0000269|PubMed:19234461}. SUBCELLULAR LOCATION: Cell projection, podosome {ECO:0000269|PubMed:16876785}. Note=Present in the F-actin surrounding ring structure of podosomes, which are specialized adhesion structures of hematopoietic cells. SUBUNIT: Interacts with ITGB1, ITGB2 and ITGB3 (via cytoplasmic tails). {ECO:0000269|PubMed:18278053, ECO:0000269|PubMed:19234461}. DOMAIN: The FERM domain is not correctly detected by PROSITE or Pfam techniques because it contains the insertion of a PH domain. TISSUE SPECIFICITY: Specifically expressed in hematopoietic cells. {ECO:0000269|PubMed:16876785}. +Q3ULM6 USPL1_MOUSE SUMO-specific isopeptidase USPL1 (EC 3.4.22.-) (Ubiquitin-specific peptidase-like protein 1) 1089 118,390 Active site (2); Alternative sequence (3); Chain (1); Domain (1); Modified residue (1); Region (1); Sequence conflict (11) FUNCTION: SUMO-specific isopeptidase involved in protein desumoylation. Specifically binds SUMO proteins with a higher affinity for SUMO2 and SUMO3 which it cleaves more efficiently. Also able to process full-length SUMO proteins to their mature forms (By similarity). Plays a key role in RNA polymerase-II-mediated snRNA transcription in the Cajal bodies (By similarity). Is a component of complexes that can bind to U snRNA genes (By similarity). {ECO:0000250|UniProtKB:Q5W0Q7}. SUBCELLULAR LOCATION: Nucleus, Cajal body {ECO:0000250}. SUBUNIT: Interacts with ELL. {ECO:0000250|UniProtKB:Q5W0Q7}. +Q9CX11 UTP23_MOUSE rRNA-processing protein UTP23 homolog 249 28,380 Chain (1); Compositional bias (1); Cross-link (1); Modified residue (1); Sequence conflict (1) FUNCTION: Involved in rRNA-processing and ribosome biogenesis. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. +Q9D479 UVSSA_MOUSE UV-stimulated scaffold protein A 717 81,759 Chain (1); Coiled coil (1); Compositional bias (1); Erroneous initiation (2); Modified residue (3); Region (1); Sequence conflict (2) FUNCTION: Factor involved in transcription-coupled nucleotide excision repair (TC-NER) in response to UV damage. TC-NER allows RNA polymerase II-blocking lesions to be rapidly removed from the transcribed strand of active genes. Acts by promoting stabilization of ERCC6 by recruiting deubiquitinating enzyme USP7 to TC-NER complexes, preventing UV-induced degradation of ERCC6 by the proteasome. Interacts with the elongating form of RNA polymerase II (RNA pol IIo) and facilitates its ubiquitination at UV damage sites, leading to promote RNA pol IIo backtracking to allow access to the nucleotide excision repair machinery. Not involved in processing oxidative damage (By similarity). {ECO:0000250}. PTM: Monoubiquitinated: ubiquitination does not increase in response to UV. {ECO:0000250}. SUBCELLULAR LOCATION: Chromosome {ECO:0000250}. Note=Accumulates at UV DNA damage sites. {ECO:0000250}. SUBUNIT: Interacts with the elongating form of RNA polymerase II (RNA pol IIo). Interacts with ERCC6, ERCC8 and USP7 (By similarity). {ECO:0000250}. +B9EJX3 VAFNB_MOUSE Protein ATP6V1FNB (ATP6V1F neighbor gene protein homolog) 177 20,412 Chain (1) +Q8BVE3 VATH_MOUSE V-type proton ATPase subunit H (V-ATPase subunit H) (Vacuolar proton pump subunit H) 483 55,855 Chain (1); Modified residue (2); Sequence conflict (1) FUNCTION: Subunit of the peripheral V1 complex of vacuolar ATPase. Subunit H activates the ATPase activity of the enzyme and couples ATPase activity to proton flow. Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells, thus providing most of the energy required for transport processes in the vacuolar system. Involved in the endocytosis mediated by clathrin-coated pits, required for the formation of endosomes (By similarity). {ECO:0000250}. SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'' and d). Interacts with AP2M1 (By similarity). {ECO:0000250}. +Q00731 VEGFA_MOUSE Vascular endothelial growth factor A (VEGF-A) (Vascular permeability factor) (VPF) 214 25,283 Alternative sequence (8); Chain (1); Disulfide bond (5); Erroneous initiation (1); Glycosylation (1); Sequence conflict (2); Signal peptide (1) FUNCTION: Growth factor active in angiogenesis, vasculogenesis and endothelial cell growth. Induces endothelial cell proliferation, promotes cell migration, inhibits apoptosis and induces permeabilization of blood vessels. Binds to the FLT1/VEGFR1 and KDR/VEGFR2 receptors, heparan sulfate and heparin. May play a role in increasing vascular permeability during lactation, when increased transport of molecules from the blood is required for efficient milk protein synthesis (By similarity). Binding to NRP1 receptor initiates a signaling pathway needed for motor neuron axon guidance and cell body migration, including for the caudal migration of facial motor neurons from rhombomere 4 to rhombomere 6 during embryonic development (PubMed:26503042). {ECO:0000250, ECO:0000269|PubMed:26503042}. SUBCELLULAR LOCATION: Isoform VEGF-1: Secreted.; SUBCELLULAR LOCATION: Isoform VEGF-2: Secreted.; SUBCELLULAR LOCATION: Isoform VEGF-3: Cell membrane; Peripheral membrane protein. Note=Remains cell-surface associated unless released by heparin. SUBUNIT: Homodimer; disulfide-linked. Also found as heterodimer with PGF (By similarity). Interacts with NRP1 (PubMed:26503042). {ECO:0000250, ECO:0000269|PubMed:26503042}. DOMAIN: Isoform VEGF-3 contains a basic insert which acts as a cell retention signal. TISSUE SPECIFICITY: In developing embryos, expressed mainly in the choroid plexus, paraventricular neuroepithelium, placenta and kidney glomeruli. Also found in bronchial epithelium, adrenal gland and in seminiferous tubules of testis. High expression of VEGF continues in kidney glomeruli and choroid plexus in adults. +P97946 VEGFD_MOUSE Vascular endothelial growth factor D (VEGF-D) (c-Fos-induced growth factor) (FIGF) 358 40,909 Chain (1); Disulfide bond (5); Glycosylation (3); Propeptide (2); Region (1); Repeat (4); Signal peptide (1) FUNCTION: Growth factor active in angiogenesis, lymphangiogenesis and endothelial cell growth, stimulating their proliferation and migration and also has effects on the permeability of blood vessels. May function in the formation of the venous and lymphatic vascular systems during embryogenesis, and also in the maintenance of differentiated lymphatic endothelium in adults. Binds and activates VEGFR-3 (Flt4) receptor. PTM: Undergoes a complex proteolytic maturation which generates a variety of processed secreted forms with increased activity toward VEGFR-3 and VEGFR-2. VEGF-D first form an antiparallel homodimer linked by disulfide bonds before secretion. The fully processed VEGF-D is composed mostly of two VEGF homology domains (VHDs) bound by non-covalent interactions (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Homodimer; non-covalent and antiparallel. TISSUE SPECIFICITY: Highly expressed in fetal and adult lung. +Q8VE47 UBA5_MOUSE Ubiquitin-like modifier-activating enzyme 5 (Ubiquitin-activating enzyme 5) (UFM1-activating enzyme) (Ubiquitin-activating enzyme E1 domain-containing protein 1) 403 44,790 Active site (1); Binding site (5); Chain (1); Metal binding (4); Modified residue (2); Sequence conflict (10) FUNCTION: E1-like enzyme which activates UFM1 and SUMO2. {ECO:0000269|PubMed:20018847}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9GZZ9}. Nucleus {ECO:0000250|UniProtKB:Q9GZZ9}. Golgi apparatus {ECO:0000250|UniProtKB:Q9GZZ9}. Note=Localizes mainly in the cytoplasm, while it localizes to the nucleus in presence of SUMO2. {ECO:0000250|UniProtKB:Q9GZZ9}. SUBUNIT: Interacts (via C-terminus) with UFC1. Interacts with UFM1. {ECO:0000250|UniProtKB:Q9GZZ9}. +P63072 UBD_MOUSE Ubiquitin D (Diubiquitin) (Ubiquitin-like protein FAT10) 162 18,376 Chain (1); Domain (2); Mutagenesis (1); Site (1) FUNCTION: Ubiquitin-like protein modifier which can be covalently attached to target protein and subsequently leads to their degradation by the 26S proteasome, in a NUB1-dependent manner. Probably functions as a survival factor. Promotes the expression of the proteasome subunit beta type-9 (PSMB9/LMP2). Regulates TNF-alpha-induced and LPS-mediated activation of the central mediator of innate immunity NF-kappa-B by promoting TNF-alpha-mediated proteasomal degradation of ubiquitinated-I-kappa-B-alpha. Required for TNF-alpha-induced p65 nuclear translocation in renal tubular epithelial cells (RTECs). May be involved in dendritic cell (DC) maturation, the process by which immature dendritic cells differentiate into fully competent antigen-presenting cells that initiate T-cell responses. Mediates mitotic non-disjunction and chromosome instability, in long-term in vitro culture and cancers, by abbreviating mitotic phase and impairing the kinetochore localization of MAD2L1 during the prometaphase stage of the cell cycle. May be involved in the formation of aggresomes when proteasome is saturated or impaired. Mediates apoptosis in a caspase-dependent manner, especially in renal epithelium and tubular cells during renal diseases. {ECO:0000269|PubMed:11445583, ECO:0000269|PubMed:15831455, ECO:0000269|PubMed:16495380, ECO:0000269|PubMed:16782901, ECO:0000269|PubMed:17889673, ECO:0000269|PubMed:19959714}. PTM: Can be acetylated. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11445583}. Cytoplasm {ECO:0000269|PubMed:11445583}. Note=Accumulates in aggresomes under proteasome inhibition conditions. {ECO:0000250}. SUBUNIT: Interact directly with the 26S proteasome. The interaction with NUB1 via the N-terminal ubiquitin domain facilitates the linking of UBD-conjugated target protein to the proteasome complex and accelerates its own degradation and that of its conjugates. Interacts (via ubiquitin-like 1 domain) with the spindle checkpoint protein MAD2L1 during mitosis. Present in aggresomes of proteasome inhibited cells. Interacts with HDAC6 under proteasome impairment conditions (By similarity). Forms a thioester with UBA6 in cells stimulated with tumor necrosis factor-alpha (TNFa) and interferon-gamma (IFNg) (PubMed:17889673). Interacts with SQSTM1 and TP53/p53 (By similarity). {ECO:0000250|UniProtKB:O15205, ECO:0000269|PubMed:17889673}. TISSUE SPECIFICITY: Mostly expressed in thymus and intestine. {ECO:0000269|PubMed:16782901}. +P61079 UB2D3_MOUSE Ubiquitin-conjugating enzyme E2 D3 (EC 2.3.2.23) ((E3-independent) E2 ubiquitin-conjugating enzyme D3) (EC 2.3.2.24) (E2 ubiquitin-conjugating enzyme D3) (Ubiquitin carrier protein D3) (Ubiquitin-conjugating enzyme E2(17)KB 3) (Ubiquitin-conjugating enzyme E2-17 kDa 3) (Ubiquitin-protein ligase D3) 147 16,687 Active site (1); Chain (1); Disulfide bond (1) Protein modification; protein ubiquitination. FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'-, as well as 'Lys-48'-linked polyubiquitination. Cooperates with the E2 CDC34 and the SCF(FBXW11) E3 ligase complex for the polyubiquitination of NFKBIA leading to its subsequent proteasomal degradation. Acts as an initiator E2, priming the phosphorylated NFKBIA target at positions 'Lys-21' and/or 'Lys-22' with a monoubiquitin. Ubiquitin chain elongation is then performed by CDC34, building ubiquitin chains from the UBE2D3-primed NFKBIA-linked ubiquitin. Acts also as an initiator E2, in conjunction with RNF8, for the priming of PCNA. Monoubiquitination of PCNA, and its subsequent polyubiquitination, are essential events in the operation of the DNA damage tolerance (DDT) pathway that is activated after DNA damage caused by UV or chemical agents during S-phase. Associates with the BRCA1/BARD1 E3 ligase complex to perform ubiquitination at DNA damage sites following ionizing radiation leading to DNA repair. Targets DAPK3 for ubiquitination which influences promyelocytic leukemia protein nuclear body (PML-NB) formation in the nucleus. In conjunction with the MDM2 and TOPORS E3 ligases, functions ubiquitination of p53/TP53. Supports NRDP1-mediated ubiquitination and degradation of ERBB3 and of BRUCE which triggers apoptosis. In conjunction with the CBL E3 ligase, targets EGFR for polyubiquitination at the plasma membrane as well as during its internalization and transport on endosomes. In conjunction with the STUB1 E3 quality control E3 ligase, ubiquitinates unfolded proteins to catalyze their immediate destruction. {ECO:0000250|UniProtKB:P61077}. PTM: Phosphorylated by AURKB. {ECO:0000269|PubMed:24034696}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P61077}; Peripheral membrane protein {ECO:0000250|UniProtKB:P61077}. Endosome membrane {ECO:0000250|UniProtKB:P61077}; Peripheral membrane protein {ECO:0000250|UniProtKB:P61077}. SUBUNIT: Interacts with SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex; when Cullin is neddylated, the interaction between the E2 and the SCF complex is strengthened. Interacts with DAPK3. Interacts with BRCA1; the DNA damage checkpoint promotes the association with BRCA1 after ionizing radiation. Interacts non-covalently with ubiquitin. Interacts with E3 ubiquitin-protein ligase CBLC. Interacts with UBTD1 (By similarity). {ECO:0000250|UniProtKB:P61077, ECO:0000269|PubMed:18515077}. +Q8BGR9 UBCP1_MOUSE Ubiquitin-like domain-containing CTD phosphatase 1 (EC 3.1.3.16) (Nuclear proteasome inhibitor UBLCP1) 318 36,837 Alternative sequence (1); Beta strand (5); Chain (1); Domain (2); Helix (2); Initiator methionine (1); Modified residue (2); Region (1); Turn (1) FUNCTION: Dephosphorylates 26S nuclear proteasomes, thereby decreasing their proteolytic activity. The dephosphorylation may prevent assembly of the core and regulatory particles (CP and RP) into mature 26S proteasome (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Colocalizes with nuclear proteasomes. {ECO:0000250}. DOMAIN: The Ubiquitin-like domain mediates interaction with proteasomes. {ECO:0000250}. +Q9CWU6 UQCC1_MOUSE Ubiquinol-cytochrome-c reductase complex assembly factor 1 (Basic FGF-repressed Zic-binding protein) (mbFZb) (Ubiquinol-cytochrome c reductase complex chaperone CBP3 homolog) 295 34,300 Alternative sequence (2); Chain (1); Erroneous initiation (1); Erroneous termination (1); Sequence conflict (1) FUNCTION: Required for the assembly of the ubiquinol-cytochrome c reductase complex (mitochondrial respiratory chain complex III or cytochrome b-c1 complex). Involved in cytochrome b translation and/or stability. {ECO:0000250|UniProtKB:Q9NVA1}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9NVA1}. Cytoplasmic vesicle {ECO:0000305}. Note=Cytoplasmic vesicular structures. {ECO:0000305}. SUBUNIT: Interacts with UQCC2. {ECO:0000250|UniProtKB:Q9NVA1}. TISSUE SPECIFICITY: In the brain it is restricted to the olfactory bulb, the hippocampus, the piriform cortex and the Purkinje cells. {ECO:0000269|PubMed:11118897}. +Q9CQY6 UQCC2_MOUSE Ubiquinol-cytochrome-c reductase complex assembly factor 2 (Mitochondrial nucleoid factor 1) (Mitochondrial protein M19) 136 16,321 Chain (1); Transit peptide (1) FUNCTION: Required for the assembly of the ubiquinol-cytochrome c reductase complex (mitochondrial respiratory chain complex III or cytochrome b-c1 complex). Plays a role in the modulation of respiratory chain activities such as oxygen consumption and ATP production and via its modulation of the respiratory chain activity can regulate skeletal muscle differentiation and insulin secretion by pancreatic beta-cells. Involved in cytochrome b translation and/or stability. {ECO:0000250|UniProtKB:Q9BRT2, ECO:0000269|PubMed:22363741}. SUBCELLULAR LOCATION: Mitochondrion matrix, mitochondrion nucleoid {ECO:0000250}. Mitochondrion {ECO:0000269|PubMed:22363741}. Mitochondrion intermembrane space {ECO:0000269|PubMed:22363741}. Mitochondrion matrix {ECO:0000269|PubMed:22363741}. Mitochondrion inner membrane {ECO:0000269|PubMed:22363741}. Note=Predominantly expressed in the mitochondrial inner membrane. SUBUNIT: Interacts with UQCC1. {ECO:0000250|UniProtKB:Q9BRT2}. TISSUE SPECIFICITY: Widely expressed with highest levels in brain, liver, kidney, heart, skeletal muscle, thymus, testis and pancreas (at protein level). {ECO:0000269|PubMed:19643811}. +Q8CAV0 YBEY_MOUSE Endoribonuclease YbeY (EC 3.1.-.-) 164 18,989 Chain (1); Metal binding (3); Sequence conflict (1) FUNCTION: Single strand-specific metallo-endoribonuclease involved in rRNA maturation. {ECO:0000250|UniProtKB:P58557}. +Q5DID3 UROL1_MOUSE Uromodulin-like 1 (Olfactorin) 1319 145,320 Alternative sequence (2); Chain (1); Disulfide bond (12); Domain (10); Glycosylation (9); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1274 1294 Helical. {ECO:0000255}. TOPO_DOM 23 1273 Extracellular. {ECO:0000255}.; TOPO_DOM 1295 1319 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16026467}; Single-pass type I membrane protein {ECO:0000269|PubMed:16026467}. +Q765I1 UTS2B_MOUSE Urotensin-2B (Urotensin II-related peptide) (Urotensin IIB) (U-IIB) (UIIB) (Urotensin-2 domain-containing protein) 113 12,821 Disulfide bond (1); Peptide (1); Propeptide (1); Signal peptide (1) FUNCTION: Potent vasoconstrictor. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +P50516 VATA_MOUSE V-type proton ATPase catalytic subunit A (V-ATPase subunit A) (EC 7.1.2.2) (V-ATPase 69 kDa subunit) (Vacuolar proton pump subunit alpha) 617 68,326 Alternative sequence (2); Chain (1); Modified residue (1); Nucleotide binding (1); Sequence conflict (6) FUNCTION: Catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. In aerobic conditions, involved in intracellular iron homeostasis, thus triggering the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent proteasomal degradation. May play a role in neurite development and synaptic connectivity. {ECO:0000250|UniProtKB:P38606}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P38606}. SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (main components: subunits A, B, C, D, E, and F) attached to an integral membrane V0 proton pore complex (main component: the proteolipid protein). +Q62465 VAT1_MOUSE Synaptic vesicle membrane protein VAT-1 homolog (EC 1.-.-.-) 406 43,097 Chain (1); Initiator methionine (1); Modified residue (4) FUNCTION: Plays a part in calcium-regulated keratinocyte activation in epidermal repair mechanisms. Has no effect on cell proliferation (By similarity). Possesses ATPase activity. Negatively regulates mitochondrial fusion in cooperation with mitofusin proteins (MFN1-2) (By similarity). {ECO:0000250, ECO:0000269|PubMed:9581869}. SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion outer membrane; Peripheral membrane protein. Note=The majority is localized in the cytoplasm a small amount is associated with mitochondria. {ECO:0000250}. +Q80Z96 VANG1_MOUSE Vang-like protein 1 (Loop-tail protein 2) (Van Gogh-like protein 1) 526 60,064 Chain (1); Modified residue (2); Sequence conflict (1); Topological domain (5); Transmembrane (4) TRANSMEM 115 135 Helical; Name=1. {ECO:0000255}.; TRANSMEM 154 174 Helical; Name=2. {ECO:0000255}.; TRANSMEM 185 205 Helical; Name=3. {ECO:0000255}.; TRANSMEM 225 245 Helical; Name=4. {ECO:0000255}. TOPO_DOM 1 114 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 136 153 Extracellular. {ECO:0000255}.; TOPO_DOM 175 184 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 206 224 Extracellular. {ECO:0000255}.; TOPO_DOM 246 526 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23029439}; Multi-pass membrane protein {ECO:0000269|PubMed:23029439}. SUBUNIT: Heterodimer with Vangl2. Interacts through its C-terminal region with the N-terminal half of DVL1, DVL2 and DVL3. The PDZ domain of DVL1, DVL2 and DVL3 is required for the interaction. {ECO:0000269|PubMed:15456783, ECO:0000269|PubMed:23029439}. +Q99L60 VATC2_MOUSE V-type proton ATPase subunit C 2 (V-ATPase subunit C 2) (Vacuolar proton pump subunit C 2) 427 48,350 Alternative sequence (2); Chain (1); Sequence conflict (1) FUNCTION: Subunit of the peripheral V1 complex of vacuolar ATPase. Subunit C is necessary for the assembly of the catalytic sector of the enzyme and is likely to have a specific function in its catalytic activity. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'' and d). TISSUE SPECIFICITY: Predominantly expressed in the lung and kidney. Isoform 1 is lung-specific while isoform 3 is a kidney-specific isoform. Isoform 1 is localized in the lamellar bodies of type II alveolar cells. Isoform 2 is strongly expressed in the cortical and medulla collecting ducts and is found in the plasma membranes of renal alpha and beta intercalated cells. {ECO:0000269|PubMed:12527205, ECO:0000269|PubMed:12947086}. +P63082 VATL_MOUSE V-type proton ATPase 16 kDa proteolipid subunit (V-ATPase 16 kDa proteolipid subunit) (PL16) (Vacuolar proton pump 16 kDa proteolipid subunit) 155 15,808 Chain (1); Site (1); Topological domain (5); Transmembrane (4) TRANSMEM 11 33 Helical. {ECO:0000255}.; TRANSMEM 56 76 Helical. {ECO:0000255}.; TRANSMEM 93 114 Helical. {ECO:0000255}.; TRANSMEM 132 152 Helical. {ECO:0000255}. TOPO_DOM 1 10 Lumenal. {ECO:0000255}.; TOPO_DOM 34 55 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 77 92 Lumenal. {ECO:0000255}.; TOPO_DOM 115 131 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 153 155 Lumenal. {ECO:0000255}. FUNCTION: Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. PTM: Ubiquitinated by RNF182, leading to its degradation via the ubiquitin-proteasome pathway. {ECO:0000250}. SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein. SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (main components: subunits A, B, C, D, E, and F) attached to an integral membrane V0 proton pore complex (main component: the proteolipid protein; which is present as a hexamer that forms the proton-conducting pore). Interacts with RNF182; this interaction leads to ubiquitination and degradation via the proteasome pathway (By similarity). {ECO:0000250}. +Q8BQH4 UBAD2_MOUSE UBA-like domain-containing protein 2 164 17,671 Chain (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (1) +Q9ES00 UBE4B_MOUSE Ubiquitin conjugation factor E4 B (EC 2.3.2.27) (RING-type E3 ubiquitin transferase E4 B) (Ubiquitin fusion degradation protein 2) 1173 133,318 Beta strand (2); Chain (1); Domain (1); Helix (3); Modified residue (14); Mutagenesis (1); Sequence conflict (6); Site (2); Turn (3) Protein modification; protein ubiquitination. FUNCTION: Ubiquitin-protein ligase that probably functions as an E3 ligase in conjunction with specific E1 and E2 ligases (PubMed:11435423). May also function as an E4 ligase mediating the assembly of polyubiquitin chains on substrates ubiquitinated by another E3 ubiquitin ligase (By similarity). May regulate myosin assembly in striated muscles together with STUB1 and VCP/p97 by targeting myosin chaperone UNC45B for proteasomal degradation (By similarity). {ECO:0000250|UniProtKB:O95155, ECO:0000250|UniProtKB:P54860, ECO:0000269|PubMed:11435423}. PTM: Proteolytically cleaved by caspases during apoptosis. Cleaved efficiently at Asp-123 by caspase-6 and granzyme B. Cleaved with approximately 10-fold less efficiency at Asp-109 by caspase-3 and caspase-7 (By similarity). {ECO:0000250|UniProtKB:O95155}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11435423, ECO:0000269|PubMed:11770485, ECO:0000269|PubMed:12504083}. Nucleus {ECO:0000269|PubMed:11435423}. SUBUNIT: Interacts with VCP (PubMed:12504083). Interacts with STUB1/CHIP and UNC45B (By similarity). {ECO:0000250|UniProtKB:O95155, ECO:0000269|PubMed:12504083}. DOMAIN: The U-box domain is required for the ubiquitin protein ligase activity. {ECO:0000269|PubMed:11435423}. TISSUE SPECIFICITY: Expressed predominantly in neuronal tissues. Also detected in liver, heart, brain, kidney and testis. {ECO:0000269|PubMed:11435423, ECO:0000269|PubMed:12504083}. +Q8C7R4 UBA6_MOUSE Ubiquitin-like modifier-activating enzyme 6 (Ubiquitin-activating enzyme 6) (EC 6.2.1.45) (Ubiquitin-activating enzyme E1-like protein 2) (E1-L2) 1053 117,966 Active site (1); Binding site (4); Chain (1); Modified residue (5); Nucleotide binding (1) Protein modification; protein ubiquitination. FUNCTION: Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP. Specific for ubiquitin, does not activate ubiquitin-like peptides. Differs from UBE1 in its specificity for substrate E2 charging. Does not charge cell cycle E2s, such as CDC34 (By similarity). Essential for embryonic development. Required for UBD/FAT10 conjugation. {ECO:0000250, ECO:0000269|PubMed:17889673}. SUBUNIT: Forms a thioester with UBD in cells stimulated with tumor necrosis factor-alpha (TNFa) and interferon-gamma (IFNg) (PubMed:17889673). {ECO:0000269|PubMed:17889673}. +Q8K2Z8 UB2Q2_MOUSE Ubiquitin-conjugating enzyme E2 Q2 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme Q2) (Ubiquitin carrier protein Q2) (Ubiquitin-protein ligase Q2) 378 42,935 Active site (1); Alternative sequence (1); Chain (1); Compositional bias (2); Natural variant (1); Sequence conflict (1) Protein modification; protein ubiquitination. FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination. {ECO:0000250|UniProtKB:Q8WVN8}. PTM: Auto-ubiquitinated in vitro. {ECO:0000250|UniProtKB:Q8WVN8}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8WVN8}. +Q9CZY3 UB2V1_MOUSE Ubiquitin-conjugating enzyme E2 variant 1 (UEV-1) (CROC-1) 147 16,355 Alternative sequence (1); Chain (1); Initiator methionine (1); Modified residue (1); Sequence conflict (5) FUNCTION: Has no ubiquitin ligase activity on its own. The UBE2V1-UBE2N heterodimer catalyzes the synthesis of non-canonical poly-ubiquitin chains that are linked through 'Lys-63'. This type of poly-ubiquitination activates IKK and does not seem to involve protein degradation by the proteasome. Plays a role in the activation of NF-kappa-B mediated by IL1B, TNF, TRAF6 and TRAF2. Mediates transcriptional activation of target genes. Plays a role in the control of progress through the cell cycle and differentiation (By similarity). Plays a role in the error-free DNA repair pathway and contributes to the survival of cells after DNA damage. Promotes TRIM5 capsid-specific restriction activity and the UBE2V1-UBE2N heterodimer acts in concert with TRIM5 to generate 'Lys-63'-linked polyubiquitin chains which activate the MAP3K7/TAK1 complex which in turn results in the induction and expression of NF-kappa-B and MAPK-responsive inflammatory genes (By similarity). {ECO:0000250, ECO:0000269|PubMed:11406273}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Excluded from the nucleolus. {ECO:0000250}. SUBUNIT: Heterodimer with UBE2N. Interacts (UBE2V2-UBE2N heterodimer) with the E3 ligase STUB1 (via the U-box domain); the complex has a specific 'Lys-63'-linked polyubiquitination activity. Interacts with TRAF6 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. Highly expressed in heart, brain, liver, skeletal msucle, kidney and testis. Detected at lower levels in lung and spleen. {ECO:0000269|PubMed:11406273}. +P62254 UB2G1_MOUSE Ubiquitin-conjugating enzyme E2 G1 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme G1) (E217K) (UBC7) (Ubiquitin carrier protein G1) (Ubiquitin-protein ligase G1) [Cleaved into: Ubiquitin-conjugating enzyme E2 G1, N-terminally processed] 170 19,509 Active site (1); Chain (2); Initiator methionine (1); Modified residue (2) Protein modification; protein ubiquitination. FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-, as well as 'Lys-63'-linked polyubiquitination. May be involved in degradation of muscle-specific proteins. Mediates polyubiquitination of CYP3A4. {ECO:0000250|UniProtKB:P62253}. PTM: Autoubiquitinated. {ECO:0000250|UniProtKB:P62253}. +Q8K387 UBP45_MOUSE Ubiquitin carboxyl-terminal hydrolase 45 (EC 3.4.19.12) (Deubiquitinating enzyme 45) (Ubiquitin thioesterase 45) (Ubiquitin-specific-processing protease 45) 813 90,361 Active site (2); Alternative sequence (1); Chain (1); Domain (1); Erroneous initiation (1); Modified residue (4); Sequence conflict (1); Zinc finger (1) +Q8BW70 UBP38_MOUSE Ubiquitin carboxyl-terminal hydrolase 38 (EC 3.4.19.12) (Deubiquitinating enzyme 38) (Ubiquitin thioesterase 38) (Ubiquitin-specific-processing protease 38) 1042 116,102 Active site (2); Chain (1); Domain (1); Sequence conflict (4) FUNCTION: Deubiquitinating enzyme exhibiting a preference towards 'Lys-63'-linked ubiquitin chains. {ECO:0000250}. +Q91W36 UBP3_MOUSE Ubiquitin carboxyl-terminal hydrolase 3 (EC 3.4.19.12) (Deubiquitinating enzyme 3) (Ubiquitin thioesterase 3) (Ubiquitin-specific-processing protease 3) 520 58,868 Active site (2); Chain (1); Domain (1); Modified residue (1); Zinc finger (1) FUNCTION: Hydrolase that deubiquitinates monoubiquitinated target proteins such as histone H2A and H2B. Required for proper progression through S phase and subsequent mitotic entry. May regulate the DNA damage response (DDR) checkpoint through deubiquitination of H2A at DNA damage sites. Associates with the chromatin (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Note=Localizes preferentially with monoubiquitinated H2A to chromatin. SUBUNIT: Interacts (via UBP-type domain) with H2A; the interaction is less efficient than with monoubiquitinated H2A. {ECO:0000250}. DOMAIN: Both protease activity and an intact zinc finger are required for H2A monodeubiquitination. +Q3V0C5 UBP48_MOUSE Ubiquitin carboxyl-terminal hydrolase 48 (EC 3.4.19.12) (Deubiquitinating enzyme 48) (Ubiquitin thioesterase 48) (Ubiquitin-specific-processing protease 48) 1052 120,631 Active site (2); Alternative sequence (4); Chain (1); Domain (5); Erroneous initiation (1); Frameshift (1); Modified residue (4) FUNCTION: Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins. May be involved in the regulation of NF-kappa-B activation by TNF receptor superfamily via its interactions with RELA and TRAF2. May also play a regulatory role at postsynaptic sites (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Interacts with TRAF2 and RELA. {ECO:0000250}. +Q6P9L4 UBP49_MOUSE Ubiquitin carboxyl-terminal hydrolase 49 (EC 3.4.19.12) (Deubiquitinating enzyme 49) (Ubiquitin thioesterase 49) (Ubiquitin-specific-processing protease 49) 685 78,272 Active site (2); Chain (1); Domain (1); Zinc finger (1) FUNCTION: Specifically deubiquitinates histone H2B at 'Lys-120' (H2BK120Ub). H2BK120Ub is a specific tag for epigenetic transcriptional activation and acts as a regulator of mRNA splicing. Deubiquitination is required for efficient cotranscriptional splicing of a large set of exons (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of a complex with RUVBL1 and PSMC5. {ECO:0000250}. +Q6A4J8 UBP7_MOUSE Ubiquitin carboxyl-terminal hydrolase 7 (EC 3.4.19.12) (Deubiquitinating enzyme 7) (Herpesvirus-associated ubiquitin-specific protease) (mHAUSP) (Ubiquitin thioesterase 7) (Ubiquitin-specific-processing protease 7) 1103 128,475 Active site (2); Alternative sequence (3); Chain (1); Compositional bias (1); Cross-link (3); Domain (2); Modified residue (7); Mutagenesis (1); Region (3); Sequence conflict (1) FUNCTION: Hydrolase that deubiquitinates target proteins such as FOXO4, p53/TP53, MDM2, ERCC6, DNMT1, UHRF1, PTEN, KMT2E and DAXX (PubMed:21268065, PubMed:14719112, PubMed:19946331). Together with DAXX, prevents MDM2 self-ubiquitination and enhances the E3 ligase activity of MDM2 towards p53/TP53, thereby promoting p53/TP53 ubiquitination and proteasomal degradation. Deubiquitinates p53/TP53, preventing degradation of p53/TP53, and enhances p53/TP53-dependent transcription regulation, cell growth repression and apoptosis. Deubiquitinates p53/TP53 and MDM2 and strongly stabilizes p53/TP53 even in the presence of excess MDM2, and also induces p53/TP53-dependent cell growth repression and apoptosis. Deubiquitination of FOXO4 in presence of hydrogen peroxide is not dependent on p53/TP53 and inhibits FOXO4-induced transcriptional activity. In association with DAXX, is involved in the deubiquitination and translocation of PTEN from the nucleus to the cytoplasm, both processes that are counteracted by PML. Deubiquitinates KMT2E preventing KMT2E proteasomal-mediated degradation (By similarity). Involved in cell proliferation during early embryonic development. Involved in transcription-coupled nucleotide excision repair (TC-NER) in response to UV damage: recruited to DNA damage sites following interaction with KIAA1530/UVSSA and promotes deubiquitination of ERCC6, preventing UV-induced degradation of ERCC6 (By similarity). Involved in maintenance of DNA methylation via its interaction with UHRF1 and DNMT1: acts by mediating deubiquitination of UHRF1 and DNMT1, preventing their degradation and promoting DNA methylation by DNMT1. Deubiquitinates alkylation repair enzyme ALKBH3. OTUD4 recruits USP7 and USP9X to stabilize ALKBH3, thereby promoting the repair of alkylated DNA lesions (By similarity). Acts as a chromatin regulator via its association with the Polycomb group (PcG) multiprotein PRC1-like complex; may act by deubiquitinating components of the PRC1-like complex (By similarity). Able to mediate deubiquitination of histone H2B; it is however unsure whether this activity takes place in vivo (PubMed:27863226). Exhibits a preference towards 'Lys-48'-linked ubiquitin chains. Increases regulatory T-cells (Treg) suppressive capacity by deubiquitinating and stabilizing the transcription factor FOXP3 which is crucial for Treg cell function (PubMed:23973222). {ECO:0000250|UniProtKB:Q93009, ECO:0000269|PubMed:23973222, ECO:0000269|PubMed:27863226}. PTM: Polyneddylated. {ECO:0000250}.; PTM: Not sumoylated. {ECO:0000250}.; PTM: Polyubiquitinated. Ubiquitinated at Lys-870 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q93009}. Cytoplasm {ECO:0000250|UniProtKB:Q93009}. Nucleus, PML body {ECO:0000250|UniProtKB:Q93009}. Chromosome {ECO:0000250|UniProtKB:Q93009}. Note=Present in a minority of ND10 nuclear bodies. Association with ICP0/VMW110 at early times of infection leads to an increased proportion of USP7-containing ND10. Colocalizes with ATXN1 in the nucleus. Colocalized with DAXX in speckled structures. Colocalized with PML and PTEN in promyelocytic leukemia protein (PML) nuclear bodies. {ECO:0000250|UniProtKB:Q93009}. SUBUNIT: Monomer. Homodimer. Part of a complex with DAXX, MDM2, RASSF1 and USP7. Part of a complex with DAXX, MDM2 and USP7. Interacts with MDM2; the interaction is independent of p53/TP53. Interacts with DAXX; the interaction is direct and independent of MDM2 and p53/TP53. Component of a complex composed of KMT2E, OGT and USP7; the complex stabilizes KMT2E, preventing KMT2E ubiquitination and proteosomal-mediated degradation (By similarity). Interacts (via MATH domain) with KMT2E (By similarity). Interacts with OGT (By similarity). Interacts with FOXO4; the interaction is enhanced in presence of hydrogen peroxide and occurs independently of p53/TP53. Interacts with p53/TP53; the interaction is enhanced in response to DNA damage; the interaction is impaired by TSPYL5. Interacts with PTEN; the interaction is direct. Interacts with ATXN1 and the strength of interaction is influenced by the length of the poly-Gln region in ATXN1. A weaker interaction seen with mutants having longer poly-Gln regions. Interacts with KIAA1530/UVSSA. Interacts with MEX3C and antagonizes its ability to degrade mRNA (By similarity). Interacts with DNMT1 and UHRF1 (PubMed:21268065). Interacts with FOXP3 (By similarity). Interacts (via MATH domain) with RNF220 (By similarity). Associated component of the Polycomb group (PcG) multiprotein PRC1-like complex (By similarity). Interacts with EPOP (PubMed:27863226). Interacts with OTUD4 and USP9X; the interaction is direct (By similarity). {ECO:0000250|UniProtKB:Q93009, ECO:0000269|PubMed:14719112, ECO:0000269|PubMed:21268065, ECO:0000269|PubMed:27863226}. DOMAIN: The C-terminus plays a role in its oligomerization. {ECO:0000250}. TISSUE SPECIFICITY: Expressed at high levels in brain, lung, thymus and testis. Expressed at low levels in the liver. {ECO:0000269|PubMed:14719112}. +O70481 UBR1_MOUSE E3 ubiquitin-protein ligase UBR1 (EC 2.3.2.27) (N-recognin-1) (RING-type E3 ubiquitin transferase UBR1) (Ubiquitin-protein ligase E3-alpha-1) (Ubiquitin-protein ligase E3-alpha-I) 1757 200,240 Chain (1); Compositional bias (1); Initiator methionine (1); Modified residue (2); Sequence caution (1); Sequence conflict (11); Zinc finger (2) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. May be involved in pancreatic homeostasis. Binds leucine and is a negative regulator of the leucine-mTOR signaling pathway, thereby controlling cell growth (By similarity). {ECO:0000250, ECO:0000269|PubMed:11689692, ECO:0000269|PubMed:14585983, ECO:0000269|PubMed:16311597}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. SUBUNIT: Interacts with RECQL4. {ECO:0000250}. DOMAIN: The RING-H2 zinc finger is an atypical RING finger with a His ligand in place of the fourth Cys of the classical motif.; DOMAIN: The UBR-type zinc finger forms a pocket that mediates recognition of type 1 N-degrons. It exhibits preference for Arginine in first position, has poor affinity for histidine, and doesn't bind acetylated peptides (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Present in skeletal muscle and liver (at protein level). Broadly expressed, with highest levels in skeletal muscle and heart. Expressed in acinar cells of the pancreas. In testes, expressed primarily in spermatogonia. {ECO:0000269|PubMed:11689692, ECO:0000269|PubMed:14585983, ECO:0000269|PubMed:15548684, ECO:0000269|PubMed:16311597, ECO:0000269|PubMed:9653112}. +P56399 UBP5_MOUSE Ubiquitin carboxyl-terminal hydrolase 5 (EC 3.4.19.12) (Deubiquitinating enzyme 5) (Isopeptidase T) (Ubiquitin thioesterase 5) (Ubiquitin-specific-processing protease 5) 858 95,833 Active site (2); Binding site (4); Chain (1); Disulfide bond (1); Domain (3); Initiator methionine (1); Metal binding (4); Modified residue (7); Region (1); Zinc finger (1) FUNCTION: Cleaves linear and branched multiubiquitin polymers with a marked preference for branched polymers. Involved in unanchored 'Lys-48'-linked polyubiquitin disassembly. Binds linear and 'Lys-63'-linked polyubiquitin with a lower affinity (By similarity). {ECO:0000250}. SUBUNIT: Interacts with TRIML1. {ECO:0000269|PubMed:19156909}. +Q6P5G6 UBXN7_MOUSE UBX domain-containing protein 7 467 52,164 Chain (1); Compositional bias (1); Cross-link (2); Domain (2); Erroneous initiation (1); Initiator methionine (1); Modified residue (6); Repeat (1) FUNCTION: Ubiquitin-binding adapter that links a subset of NEDD8-associated cullin ring ligases (CRLs) to the segregase VCP/p97, to regulate turnover of their ubiquitination substrates (By similarity). {ECO:0000250|UniProtKB:O94888}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O94888}. SUBUNIT: Interacts with neddylated CUL2, ubiquitinated HIF1A, and VCP/p97. {ECO:0000250|UniProtKB:O94888}. DOMAIN: The UIM (ubiquitin-interacting motif) is required to engage the NEDD8 modification on cullins. {ECO:0000250|UniProtKB:O94888}.; DOMAIN: The UBX domain mediates interaction with VCP/p97. {ECO:0000250|UniProtKB:O94888}.; DOMAIN: The UBA domain is required for binding ubiquitinated-protein substrates. {ECO:0000250|UniProtKB:O94888}. +Q99NB8 UBQL4_MOUSE Ubiquilin-4 (Ataxin-1 interacting ubiquitin-like protein) (A1Up) (Ataxin-1 ubiquitin-like-interacting protein A1U) (Connexin43-interacting protein of 75 kDa) (CIP75) 596 63,506 Chain (1); Compositional bias (1); Cross-link (2); Domain (6); Helix (3); Modified residue (1); Turn (1) FUNCTION: Plays a role in the regulation of protein degradation via the ubiquitin-proteasome system (UPS). Mediates the proteasomal targeting of misfolded or accumulated proteins for degradation by binding (via UBA domain) to their polyubiquitin chains and by interacting (via ubiquitin-like domain) with the subunits of the proteasome (By similarity). Plays a role in the regulation of the proteasomal degradation of non-ubiquitinated GJA1 (PubMed:18079109, PubMed:20940304). Acts as an adapter protein that recruits UBQLN1 to the autophagy machinery. Mediates the association of UBQLN1 with autophagosomes and the autophagy-related protein LC3 (MAP1LC3A/B/C) and may assist in the maturation of autophagosomes to autolysosomes by mediating autophagosome-lysosome fusion (By similarity). {ECO:0000250|UniProtKB:Q9NRR5, ECO:0000269|PubMed:18079109, ECO:0000269|PubMed:20940304}. PTM: Ubiquitinated; this does not lead to proteasomal degradation. May undergo both 'Lys-48'- and 'Lys-63'-linked polyubiquitination (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NRR5}. Cytoplasm {ECO:0000269|PubMed:11162551}. Endoplasmic reticulum {ECO:0000269|PubMed:11162551, ECO:0000269|PubMed:18079109, ECO:0000269|PubMed:20940304}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:18079109}. Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:Q9NRR5}. Note=Colocalizes with the proteasome, both in nucleus and cytoplasm (By similarity). {ECO:0000250|UniProtKB:Q9NRR5}. SUBUNIT: Homooligomer. Binds ATXN1/SCA1. Interaction with ATXN1 inhibits polyubiquitination of UBQLN4 and interferes with PSMD4 binding (By similarity). Interacts (via ubiquitin-like domain) with PSMD2 and PSMD4, regulatory subunits of the proteasome (PubMed:18079109). Binds signal sequences of proteins that are targeted to the endoplasmic reticulum (PubMed:11162551). Interacts (via UBA domain) with GJA1 (not ubiquitinated) and with ubiquitin; both compete for the same binding site (PubMed:18079109, PubMed:20940304, PubMed:20127391). Interacts (via UBA domain) with polyubiquitin chains and polyubiquitinated proteins (PubMed:20940304). Interacts with HERPUD1. Interacts (via ubiquitin-like domain) with UBQLN1 (via UBA domain). Interacts (via STI1 1 and 2 domains) with MAP1LC3A/B/C. Interacts with UBQLN2 (By similarity). {ECO:0000250|UniProtKB:Q9NRR5, ECO:0000269|PubMed:11162551, ECO:0000269|PubMed:18079109, ECO:0000269|PubMed:20127391, ECO:0000269|PubMed:20940304}. TISSUE SPECIFICITY: Detected in testis, ovary, thyroid, kidney, thymus, heart, liver, lung and spleen (at protein level). Highly expressed in heart, skeletal muscle, kidney, liver and brain. Detected at lower levels in testis, lung and spleen. {ECO:0000269|PubMed:11162551, ECO:0000269|PubMed:20940304}. +Q0KL01 UBX2B_MOUSE UBX domain-containing protein 2B (NSFL1 cofactor p37) (p97 cofactor p37) 331 37,444 Chain (1); Domain (2); Initiator methionine (1); Modified residue (7); Sequence conflict (3) FUNCTION: Adapter protein required for Golgi and endoplasmic reticulum biogenesis. Involved in Golgi and endoplasmic reticulum maintenance during interphase and in their reassembly at the end of mitosis. The complex formed with VCP has membrane fusion activity; membrane fusion activity requires USO1-GOLGA2 tethering and BET1L. VCPIP1 is also required, but not its deubiquitinating activity. Together with NSFL1C/p47, regulates the centrosomal levels of kinase AURKA/Aurora A during mitotic progression by promoting AURKA removal from centrosomes in prophase. Also, regulates spindle orientation during mitosis. {ECO:0000250|UniProtKB:Q14CS0}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P0C627}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P0C627}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P0C627}. Golgi apparatus {ECO:0000250|UniProtKB:P0C627}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:23649807}. Note=Localizes to centrosome during mitotic prophase and metaphase. {ECO:0000269|PubMed:23649807}. SUBUNIT: Interacts with VCP. Does not bind ubiquitin. {ECO:0000269|PubMed:17141156}. +P56501 UCP3_MOUSE Mitochondrial uncoupling protein 3 (UCP 3) (Solute carrier family 25 member 9) 308 33,911 Chain (1); Region (1); Repeat (3); Sequence conflict (1); Transmembrane (6) TRANSMEM 11 32 Helical; Name=1. {ECO:0000255}.; TRANSMEM 74 96 Helical; Name=2. {ECO:0000255}.; TRANSMEM 117 133 Helical; Name=3. {ECO:0000255}.; TRANSMEM 180 196 Helical; Name=4. {ECO:0000255}.; TRANSMEM 214 233 Helical; Name=5. {ECO:0000255}.; TRANSMEM 268 290 Helical; Name=6. {ECO:0000255}. FUNCTION: UCP are mitochondrial transporter proteins that create proton leaks across the inner mitochondrial membrane, thus uncoupling oxidative phosphorylation. As a result, energy is dissipated in the form of heat. May play a role in the modulation of tissue respiratory control. Participates in thermogenesis and energy balance (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q3U1V6 UEVLD_MOUSE Ubiquitin-conjugating enzyme E2 variant 3 (UEV-3) (EV and lactate/malate dehydrogenase domain-containing protein) 471 51,681 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (1); Frameshift (1); Nucleotide binding (1); Sequence conflict (3) FUNCTION: Possible negative regulator of polyubiquitination. {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +P17717 UDB17_MOUSE UDP-glucuronosyltransferase 2B17 (EC 2.4.1.17) (M-1) (UDP-glucuronosyltransferase 2B5) (UDPGT 2B5) 530 60,856 Chain (1); Glycosylation (2); Signal peptide (1); Transmembrane (1) TRANSMEM 494 510 Helical. {ECO:0000255}. FUNCTION: UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. SUBCELLULAR LOCATION: Microsome membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q7TMI3 UHRF2_MOUSE E3 ubiquitin-protein ligase UHRF2 (EC 2.3.2.27) (NIRF) (Np95-like ring finger protein) (Nuclear protein 97) (Nuclear zinc finger protein Np97) (RING-type E3 ubiquitin transferase UHRF2) (Ubiquitin-like PHD and RING finger domain-containing protein 2) (Ubiquitin-like-containing PHD and RING finger domains protein 2) 803 90,106 Alternative sequence (3); Chain (1); Disulfide bond (1); Domain (2); Modified residue (1); Mutagenesis (2); Region (3); Sequence conflict (3); Zinc finger (2) Protein modification; protein ubiquitination. FUNCTION: E3 SUMO-, but not ubiquitin-, protein ligase for ZNF131 (By similarity). E3 ubiquitin-protein ligase that is an intermolecular hub protein in the cell cycle network. Ubiquitinates cyclins, CCND1 and CCNE1, in an apparently phosphorylation-independent manner and induces G1 arrest. Also ubiquitinates PCNP leading to its degradation by the proteasome. Through cooperative DNA and histone binding, may contribute to a tighter epigenetic control of gene expression in differentiated cells. {ECO:0000250, ECO:0000269|PubMed:21598301}. PTM: May be autoubiquitinated; which may lead to proteasomal degradation. {ECO:0000250}.; PTM: Phosphorylated. Phosphorylation may be mediated by CDK2 (By similarity). {ECO:0000250}.; PTM: Autosumoylated. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00358, ECO:0000269|PubMed:21598301}. Note=Enriched at pericentric heterochromatin (PH). This localization is dependent on the interaction with H3K9me3. SUBUNIT: Homodimer; disulfide-linked (By similarity). Binds methylated CpG containing oligonucleotides. Interacts with PCNP, HDAC1 and CDK2 (inactive form). Component of a complex at least composed of UHRF2, CDK2 and CCNE1. Interacts directly with CCNE1; the interaction ubiquitinates CCNE1 and appears independent of CCNE1 phosphorylation. Interacts with CCND1; the interaction ubiquitinates CCND1 and appears independent of CCND1 phosphorylation. Interacts with p53/TP53 and RB1 (By similarity). Interacts with H3; the interaction has a preference for the 'Lys-9' trimethylated form of H3 (H3K9me3). Interacts with UBE2I (By similarity). {ECO:0000250}. +Q91Z49 UIF_MOUSE UAP56-interacting factor (Forty-two-three domain-containing protein 1) (Protein 40-2-3) 317 35,887 Alternative sequence (3); Chain (1); Cross-link (2); Modified residue (5); Motif (1); Sequence conflict (4) FUNCTION: Required for mRNA export from the nucleus to the cytoplasm. Acts as an adapter that uses the DDX39B/UAP56-NFX1 pathway to ensure efficient mRNA export and delivering to the nuclear pore. Associates with spliced and unspliced mRNAs simultaneously with ALYREF/THOC4 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}. Nucleus speckle {ECO:0000250}. SUBUNIT: Interacts with DDX39B/UAP56 and NXF1; interaction with DDX39B/UAP56 and NXF1 are mutually exclusive. Interacts with SSRP1; required for its recruitment to mRNAs (By similarity). Interacts with CHTOP. {ECO:0000250, ECO:0000269|PubMed:22872859}. +Q5U5Q9 UIMC1_MOUSE BRCA1-A complex subunit RAP80 (Receptor-associated protein 80) (Ubiquitin interaction motif-containing protein 1) 727 81,478 Alternative sequence (3); Chain (1); Compositional bias (1); Cross-link (14); Domain (2); Erroneous initiation (1); Helix (1); Modified residue (12); Motif (1); Region (6); Sequence conflict (6) FUNCTION: Ubiquitin-binding protein. Specifically recognizes and binds 'Lys-63'-linked ubiquitin (PubMed:19536136). Plays a central role in the BRCA1-A complex by specifically binding 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). The BRCA1-A complex also possesses deubiquitinase activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. Also weakly binds monoubiquitin but with much less affinity than 'Lys-63'-linked ubiquitin. May interact with monoubiquitinated histones H2A and H2B; the relevance of such results is however unclear in vivo. Does not bind Lys-48'-linked ubiquitin. May indirectly act as a transcriptional repressor by inhibiting the interaction of NR6A1 with the corepressor NCOR1 (By similarity). {ECO:0000250|UniProtKB:Q96RL1, ECO:0000269|PubMed:19536136}. PTM: Sumoylated. {ECO:0000250|UniProtKB:Q96RL1}.; PTM: Phosphorylated upon DNA damage by ATM or ATR. {ECO:0000250|UniProtKB:Q96RL1}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96RL1}. Note=Localizes at sites of DNA damage at double-strand breaks (DSBs). {ECO:0000250|UniProtKB:Q96RL1}. SUBUNIT: Component of the ARISC complex, at least composed of UIMC1/RAP80, ABRAXAS1, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1. Component of the BRCA1-A complex, at least composed of the BRCA1, BARD1, UIMC1/RAP80, ABRAXAS1, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1. In the BRCA1-A complex, interacts directly with ABRAXAS1. Interacts with ESR1 and UBE2I (By similarity). Interacts with NR6A1 and TSP57 (PubMed:7760852, PubMed:12954732). {ECO:0000250|UniProtKB:Q96RL1, ECO:0000269|PubMed:12954732, ECO:0000269|PubMed:7760852}. DOMAIN: The tandem UIM domains form a continuous 60 Angstrom-long alpha-helix and mediate binding to 'Lys-63'-linked ubiquitins. UIM1 and UIM2 bind to the proximal and distal ubiquitin moieties and recognize an 'Ile-44'-centered hydrophobic patch. Since UIMs don't interact with the 'Lys-63' isopeptide bond the UIM-linker region between the 2 UIM domains determines the selectivity for 'Lys-63'-linkage, and its length is very important for specificity. {ECO:0000269|PubMed:19536136}.; DOMAIN: The Abraxas-interacting region (AIR) mediates the interaction with ABRAXAS1. {ECO:0000250|UniProtKB:Q96RL1}. +Q8VBW6 ULA1_MOUSE NEDD8-activating enzyme E1 regulatory subunit (Amyloid beta precursor protein-binding protein 1, 59 kDa) (APP-BP1) (Amyloid protein-binding protein 1) 534 60,274 Chain (1); Initiator methionine (1); Modified residue (3); Region (1); Sequence conflict (1); Site (1) Protein modification; protein neddylation. FUNCTION: Regulatory subunit of the dimeric UBA3-NAE1 E1 enzyme. E1 activates NEDD8 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-UBA3 thioester and free AMP. E1 finally transfers NEDD8 to the catalytic cysteine of UBE2M. Necessary for cell cycle progression through the S-M checkpoint. Overexpression of NAE1 causes apoptosis through deregulation of NEDD8 conjugation (By similarity). {ECO:0000250}. PTM: Ubiquitinated by TRIP12, leading to its degradation by the proteasome. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Note=Colocalizes with APP in lipid rafts. {ECO:0000250}. SUBUNIT: Heterodimer of UBA3 and NAE1. The complex binds NEDD8 and UBE2M. Binds APP and TP53BP2 (By similarity). {ECO:0000250}. +P99031 ULAK_MOUSE Unknown protein from spot 2D-0014LD of 2D-PAGE of liver tissue (Fragment) 9 1,109 Chain (1); Non-terminal residue (1) +Q9QY01 ULK2_MOUSE Serine/threonine-protein kinase ULK2 (EC 2.7.11.1) (Serine/threonine-protein kinase Unc51.2) (Unc-51-like kinase 2) 1037 112,877 Active site (1); Binding site (1); Chain (1); Domain (1); Erroneous initiation (1); Modified residue (3); Mutagenesis (1); Nucleotide binding (1); Region (1); Sequence conflict (1) FUNCTION: Serine/threonine-protein kinase involved in autophagy in response to starvation. Acts upstream of phosphatidylinositol 3-kinase PIK3C3 to regulate the formation of autophagophores, the precursors of autophagosomes. Part of regulatory feedback loops in autophagy: acts both as a downstream effector and a negative regulator of mammalian target of rapamycin complex 1 (mTORC1) via interaction with RPTOR. Activated via phosphorylation by AMPK, also acts as a negative regulator of AMPK through phosphorylation of the AMPK subunits PRKAA1, PRKAB2 and PRKAG1. May phosphorylate ATG13/KIAA0652, FRS2, FRS3 and RPTOR; however such data need additional evidences. Not involved in ammonia-induced autophagy or in autophagic response of cerebellar granule neurons (CGN) to low potassium concentration. Plays a role early in neuronal differentiation and is required for granule cell axon formation: may govern axon formation via Ras-like GTPase signaling and through regulation of the Rab5-mediated endocytic pathways within developing axons. {ECO:0000269|PubMed:10624947, ECO:0000269|PubMed:16887332, ECO:0000269|PubMed:18443221, ECO:0000269|PubMed:21460634}. PTM: Autophosphorylated. In response to nutrient limitation, probably phosphorylated and activated by AMPK, leading to activate autophagy. {ECO:0000269|PubMed:21258367}. SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:18443221}; Peripheral membrane protein {ECO:0000269|PubMed:18443221}. Note=Localizes to pre-autophagosomal membrane. SUBUNIT: Component of a complex consisting of ATG13/KIAA0652, ULK1 and RB1CC1/FIP200. Interacts (via C-terminus) with ATG13/KIAA0652. Associates with the mammalian target of rapamycin complex 1 (mTORC1) through an interaction with RPTOR (By similarity). Interacts with SYNGAP1. {ECO:0000250, ECO:0000269|PubMed:15014045, ECO:0000269|PubMed:18443221}. DOMAIN: The CTD-like region mediates membrane-binding and incorporation into large protein complexes. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10557072}. +P13439 UMPS_MOUSE Uridine 5'-monophosphate synthase (UMP synthase) [Includes: Orotate phosphoribosyltransferase (OPRTase) (EC 2.4.2.10); Orotidine 5'-phosphate decarboxylase (EC 4.1.1.23) (OMPdecase)] 481 52,292 Active site (2); Chain (1); Modified residue (1); Region (3) Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2. SUBUNIT: Homodimer. {ECO:0000250}. +Q8K0T7 UN13C_MOUSE Protein unc-13 homolog C (Munc13-3) 2210 249,844 Chain (1); Coiled coil (1); Domain (4); Modified residue (5); Sequence caution (1); Zinc finger (1) FUNCTION: May play a role in vesicle maturation during exocytosis as a target of the diacylglycerol second messenger pathway. May be involved in the regulation of synaptic transmission at parallel fiber - Purkinje cell synapses. {ECO:0000269|PubMed:11150314}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell junction, synapse, presynaptic cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Localized to presynaptic structures. {ECO:0000250}. SUBUNIT: Interacts with STX1A and/or STX1B1, VAMP2 and SNAP25. {ECO:0000250}. DOMAIN: The C2 domains are not involved in calcium-dependent phospholipid binding. {ECO:0000250}. TISSUE SPECIFICITY: Restricted to cerebellum, predominantly in the granule cell layer. Almost exclusively present in the molecular layer in which the parallel fiber axons of granule cells terminate on dendrites of Purkinje neurons (at protein level). {ECO:0000269|PubMed:11150314}. +Q99KD5 UN45A_MOUSE Protein unc-45 homolog A (Unc-45A) (Stromal membrane-associated protein 1) (SMAP-1) 944 103,447 Chain (1); Modified residue (2); Repeat (3); Sequence conflict (5) FUNCTION: May act as co-chaperone for HSP90 (Potential). Prevents the stimulation of HSP90AB1 ATPase activity by AHSA1. Positive factor in promoting PGR function in the cell (By similarity). May be necessary for proper folding of myosin (Potential). Necessary for normal cell proliferation. Necessary for normal myotube formation and myosin accumulation during muscle cell development. May play a role in erythropoiesis in stroma cells in the spleen. {ECO:0000250, ECO:0000269|PubMed:12356907, ECO:0000269|PubMed:9209433, ECO:0000305}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000250}. Note=Predominant in the perinuclear region. Little protein in the nucleus (By similarity). {ECO:0000250}. SUBUNIT: Interacts with PGR isoforms A and B as well as with NR3C1 in the absence of ligand, and with HSP90AB1. Binding to HSP90AB1 involves 2 UNC45A monomers per HSP90AB1 dimer (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Detected in spleen, bone marrow, lung and ovary, and at lower levels in testis, kidney, heart and brain (at protein level). Ubiquitous. Detected in uterus, large intestine, kidney, spleen, lung, brain, liver and ovary. {ECO:0000269|PubMed:12356907, ECO:0000269|PubMed:9209433}. +Q710D3 UN93A_MOUSE Protein unc-93 homolog A (Unc-93A) 458 50,370 Chain (1); Glycosylation (1); Transmembrane (12) TRANSMEM 8 28 Helical. {ECO:0000255}.; TRANSMEM 42 62 Helical. {ECO:0000255}.; TRANSMEM 69 89 Helical. {ECO:0000255}.; TRANSMEM 90 110 Helical. {ECO:0000255}.; TRANSMEM 140 160 Helical. {ECO:0000255}.; TRANSMEM 202 222 Helical. {ECO:0000255}.; TRANSMEM 258 275 Helical. {ECO:0000255}.; TRANSMEM 286 306 Helical. {ECO:0000255}.; TRANSMEM 321 341 Helical. {ECO:0000255}.; TRANSMEM 345 365 Helical. {ECO:0000255}.; TRANSMEM 390 410 Helical. {ECO:0000255}.; TRANSMEM 412 432 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q9Z1N9 UN13B_MOUSE Protein unc-13 homolog B (Munc13-2) (munc13) 1602 181,813 Alternative sequence (2); Chain (1); Coiled coil (1); Domain (5); Modified residue (3); Sequence conflict (17); Zinc finger (1) FUNCTION: Plays a role in vesicle maturation during exocytosis as a target of the diacylglycerol second messenger pathway. Is involved in neurotransmitter release by acting in synaptic vesicle priming prior to vesicle fusion and participates in the activity-depending refilling of readily releasable vesicle pool (RRP) (By similarity). Essential for synaptic vesicle maturation in a subset of excitatory/glutamatergic but not inhibitory/GABA-mediated synapses. {ECO:0000250, ECO:0000269|PubMed:12070347}. SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein. Golgi apparatus. Cell junction, synapse {ECO:0000250}. Note=Localized to synapses (By similarity). Translocates to the Golgi in response to phorbol ester binding. {ECO:0000250}. SUBUNIT: Interacts with RIMS1. {ECO:0000250}. DOMAIN: The C2 domains are not involved in calcium-dependent phospholipid binding. {ECO:0000250}. +O08934 UNC4_MOUSE Homeobox protein unc-4 homolog (Homeobox protein Uncx4.1) 530 53,936 Chain (1); Compositional bias (1); DNA binding (1); Sequence conflict (1) FUNCTION: Transcription factor involved in somitogenesis and neurogenesis. Required for the maintenance and differentiation of particular elements of the axial skeleton. May act upstream of PAX9. Plays a role in controlling the development of connections of hypothalamic neurons to pituitary elements, allowing central neurons to reach the peripheral blood circulation and to deliver hormones for control of peripheral functions. {ECO:0000269|PubMed:10804168, ECO:0000269|PubMed:10804169, ECO:0000269|PubMed:16461927}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. TISSUE SPECIFICITY: Expressed in the paraxial mesoderm, in the developing kidney and central nervous system. In the somite, it is restricted to the caudal half of the newly formed somite and sclerotome. In the central nervous system, it is detected in the developing spinal cord, hindbrain, mesencephalon and telencephalon. Expressed in adult and embryonic magnocellular neurons of the hypothalamo-neurohypophysial system. {ECO:0000269|PubMed:10330372, ECO:0000269|PubMed:10545229, ECO:0000269|PubMed:11747084, ECO:0000269|PubMed:11973278, ECO:0000269|PubMed:16461927, ECO:0000269|PubMed:16728472, ECO:0000269|PubMed:17477400, ECO:0000269|PubMed:17531978, ECO:0000269|PubMed:9286595}. +Q9CQ61 UNC50_MOUSE Protein unc-50 homolog (Periodontal ligament-specific protein 22) (PDLs22) 259 30,429 Chain (1); Modified residue (2); Topological domain (6); Transmembrane (5) TRANSMEM 83 103 Helical. {ECO:0000255}.; TRANSMEM 113 133 Helical. {ECO:0000255}.; TRANSMEM 164 184 Helical. {ECO:0000255}.; TRANSMEM 188 208 Helical. {ECO:0000255}.; TRANSMEM 223 243 Helical. {ECO:0000255}. TOPO_DOM 1 82 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 104 112 Lumenal. {ECO:0000255}.; TOPO_DOM 134 163 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 185 187 Lumenal. {ECO:0000255}.; TOPO_DOM 209 222 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 244 259 Lumenal. {ECO:0000255}. FUNCTION: May be involved in cell surface expression of neuronal nicotinic receptors. Binds RNA (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in periodontal ligament and bone marrow, but not in gingival fibroblasts. {ECO:0000269|PubMed:11302735}. +Q8K1S4 UNC5A_MOUSE Netrin receptor UNC5A (Protein unc-5 homolog 1) (Protein unc-5 homolog A) 898 98,857 Alternative sequence (2); Chain (1); Disulfide bond (9); Domain (6); Erroneous initiation (1); Glycosylation (3); Region (1); Sequence conflict (1); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 362 382 Helical. {ECO:0000255}. TOPO_DOM 26 361 Extracellular. {ECO:0000255}.; TOPO_DOM 383 898 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for netrin required for axon guidance. Functions in the netrin signaling pathway and promotes neurite outgrowth in response to NTN1. Mediates axon repulsion of neuronal growth cones in the developing nervous system in response to netrin. Axon repulsion in growth cones may be mediated by its association with DCC that may trigger signaling for repulsion. It also acts as a dependence receptor required for apoptosis induction when not associated with netrin ligand. {ECO:0000250|UniProtKB:O08721}. PTM: Phosphorylated on cytoplasmic tyrosine residues (By similarity). Phosphorylated by PKC in vitro (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O08721}.; PTM: Proteolytically cleaved by caspases during apoptosis. The cleavage does not take place when the receptor is associated with netrin ligand. Its cleavage by caspases is required to induce apoptosis. {ECO:0000250|UniProtKB:O08721}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O08721}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:O08721}. Membrane raft {ECO:0000250|UniProtKB:O08721}. Cell projection {ECO:0000250|UniProtKB:O08721}. Note=The interaction with PRKCABP regulates its surface expression and leads to its removal from the surface of neurons and growth cones. Detected in neurites. {ECO:0000250|UniProtKB:O08721}. SUBUNIT: Homodimer and homooligomer. Interacts with the cytoplasmic part of DCC. Interacts with MAGED1. Interacts with PRKCABP, possibly mediating some interaction with PKC (By similarity). Interacts (via extracellular domain) with FLRT2 (via extracellular domain) (PubMed:25374360). Interacts (via extracellular domain) with FLRT3 (via extracellular domain) (PubMed:22405201). {ECO:0000250|UniProtKB:O08721, ECO:0000269|PubMed:22405201, ECO:0000269|PubMed:25374360}. DOMAIN: The ZU5 domain mediates the interaction with MAGED1, which participates in the induction of apoptosis. {ECO:0000250|UniProtKB:O08721}. TISSUE SPECIFICITY: Restricted to central nervous system. {ECO:0000269|PubMed:12351186}. +Q8K1S2 UNC5D_MOUSE Netrin receptor UNC5D (Protein unc-5 homolog 4) (Protein unc-5 homolog D) 956 106,352 Chain (1); Disulfide bond (9); Domain (6); Glycosylation (4); Region (1); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 383 403 Helical. {ECO:0000255}. TOPO_DOM 31 382 Extracellular. {ECO:0000255}.; TOPO_DOM 404 956 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for the netrin NTN4 that promotes neuronal cell survival (PubMed:21216843). Plays a role in cell-cell adhesion and cell guidance. Receptor for netrin involved in cell migration (By similarity). Plays a role in the regulation of neuronal cell migration in the developing brain via its interaction with FLRT2 (PubMed:21673655). Plays a role in axon guidance by mediating axon repulsion of neuronal growth cones in the developing nervous system upon ligand binding (PubMed:21673655). May play a role in apoptosis in response to DNA damage. It also acts as a dependence receptor required for apoptosis induction when not associated with netrin ligand (By similarity). Mediates cell-cell adhesion via its interaction with FLRT3 on an adjacent cell (PubMed:26235030). {ECO:0000250|UniProtKB:Q6UXZ4, ECO:0000269|PubMed:21216843, ECO:0000269|PubMed:21673655, ECO:0000269|PubMed:26235030, ECO:0000305}. PTM: Proteolytically cleaved by caspases during apoptosis. The cleavage does not take place when the receptor is associated with netrin ligand. Its cleavage by caspases is required to induce apoptosis (By similarity). {ECO:0000250|UniProtKB:Q6UXZ4}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21216843, ECO:0000269|PubMed:21673655, ECO:0000269|PubMed:26235030}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Interacts (via extracellular domain) with FLRT2 and FLRT3 (via extracellular domain); the interaction is direct (PubMed:19492039, PubMed:21673655, PubMed:25374360, PubMed:26235030). Has higher affinity for FLRT2 (PubMed:25374360). Identified in a complex with FLRT3 and ADGRL3; does not interact with ADGRL3 by itself (PubMed:26235030). {ECO:0000269|PubMed:19492039, ECO:0000269|PubMed:21673655, ECO:0000269|PubMed:25374360, ECO:0000269|PubMed:26235030}. TISSUE SPECIFICITY: Detected in multipolar cells in the brain subventricular zone (at protein level) (PubMed:18547816). Detected in embryonic brain neocortex, especially in the subventricular zone (PubMed:21673655). Detected in multipolar cells in the brain subventricular zone (PubMed:18547816). Detected in brain neocortex from young pups, especially in the somatosensory cortex (PubMed:21216843). Expressed in developing limb and mammary gland (PubMed:12351186). {ECO:0000269|PubMed:12351186, ECO:0000269|PubMed:18547816, ECO:0000269|PubMed:21216843, ECO:0000269|PubMed:21673655}. +Q0KK59 UNC79_MOUSE Protein unc-79 homolog 2596 290,740 Chain (1); Erroneous initiation (1); Modified residue (2); Transmembrane (2) TRANSMEM 2184 2204 Helical. {ECO:0000255}.; TRANSMEM 2426 2446 Helical. {ECO:0000255}. FUNCTION: Component of the NALCN sodium channel complex, a cation channel activated either by neuropeptides substance P or neurotensin that controls neuronal excitability. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Found in a complex with NALCN, UNC79 and UNC80; UNC80 bridges NALCN to UNC79 (PubMed:21040849). Interacts with NALCN (PubMed:21040849). Interacts with UNC80 (PubMed:21040849). {ECO:0000269|PubMed:21040849}. +Q8BL48 UNK_MOUSE RING finger protein unkempt homolog (Zinc finger CCCH domain-containing protein 5) 810 88,058 Alternative sequence (1); Beta strand (9); Chain (1); Coiled coil (1); Compositional bias (1); Erroneous initiation (1); Helix (13); Modified residue (6); Sequence conflict (1); Turn (9); Zinc finger (6) FUNCTION: Sequence-specific RNA-binding protein which plays an important role in the establishment and maintenance of the early morphology of cortical neurons during embryonic development. Acts as a translation repressor and controls a translationally regulated cell morphology program to ensure proper structuring of the nervous system. Translational control depends on recognition of its binding element within target mRNAs which consists of a mandatory UAG trimer upstream of a U/A-rich motif. Associated with polysomes (PubMed:25737280). {ECO:0000269|PubMed:25737280}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25737280}. +Q8CGR7 UPP2_MOUSE Uridine phosphorylase 2 (UPase 2) (UrdPase 2) (EC 2.4.2.3) (Liver-specific uridine phosphorylase) (L-UrdPase) 320 35,755 Chain (1); Disulfide bond (1) Pyrimidine metabolism; UMP biosynthesis via salvage pathway; uracil from uridine (phosphorylase route): step 1/1. FUNCTION: Catalyzes the reversible phosphorylytic cleavage of uridine and deoxyuridine to uracil and ribose- or deoxyribose-1-phosphate. The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Liver specific. +Q9DAJ5 DLRB2_MOUSE Dynein light chain roadblock-type 2 (Dynein light chain 2B, cytoplasmic) 96 10,876 Alternative sequence (1); Chain (1) FUNCTION: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SUBUNIT: Homodimer (Probable). The cytoplasmic dynein 1 complex consists of two catalytic heavy chains (HCs) and a number of non-catalytic subunits presented by intermediate chains (ICs), light intermediate chains (LICs) and light chains (LCs); the composition seems to vary in respect to the IC, LIC and LC composition. The heavy chain homodimer serves as a scaffold for the probable homodimeric assembly of the respective non-catalytic subunits. The ICs and LICs bind directly to the HC dimer and the LCs assemble on the IC dimer. Interacts with DYNC1I1 and DYNC1I2. Self-associates. Interacts with DYNLRB1 (By similarity). {ECO:0000250, ECO:0000305}. +E9Q9R9 DLG5_MOUSE Disks large homolog 5 1921 214,386 Chain (1); Coiled coil (1); Compositional bias (2); Domain (7); Modified residue (12); Natural variant (1); Sequence conflict (1) FUNCTION: Acts as a regulator of the Hippo signaling pathway. Negatively regulates the Hippo signaling pathway by mediating the interaction of MARK3 with STK3/4, bringing them together to promote MARK3-dependent hyperphosphorylation and inactivation of STK3 kinase activity toward LATS1 (PubMed:28087714). Positively regulates the Hippo signaling by mediating the interaction of SCRIB with STK4/MST1 and LATS1 which is important for the activation of the Hippo signaling pathway. Involved in regulating cell proliferation, maintenance of epithelial polarity, epithelial-mesenchymal transition (EMT), cell migration and invasion (By similarity). Plays an important role in dendritic spine formation and synaptogenesis in cortical neurons; regulates synaptogenesis by enhancing the cell surface localization of N-cadherin (PubMed:25232112). Acts as a positive regulator of hedgehog (Hh) signaling pathway. Plays a critical role in the early point of the SMO activity cycle by interacting with SMO at the ciliary base to induce the accumulation of KIF7 and GLI2 at the ciliary tip for GLI2 activation (PubMed:25644602). {ECO:0000250|UniProtKB:Q8TDM6, ECO:0000269|PubMed:25232112, ECO:0000269|PubMed:25644602, ECO:0000269|PubMed:28087714}. SUBCELLULAR LOCATION: Cell junction {ECO:0000250|UniProtKB:Q8TDM6}. Cell membrane {ECO:0000250|UniProtKB:Q8TDM6}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8TDM6}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000269|PubMed:25232112}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:25644602}. Note=Localized at sites of cell-cell contact. {ECO:0000250|UniProtKB:Q8TDM6}. SUBUNIT: Interacts with MPP1. Interacts with CTNNB1 and with the third SH3 domain of SORBS3 to form a ternary complex (By similarity). Interacts (via coiled-coil domain) with MARK3. Interacts (via PDZ domain 3) with STK3/MST2 and STK4/MST1 (PubMed:28087714). Interacts with SCRIB (By similarity). Interacts with CTNB1 (PubMed:25232112). Interacts with SMO and (via PDZ4 or guanylate kinase-like domain) with KIF7 (PubMed:25644602). {ECO:0000250|UniProtKB:Q8TDM6, ECO:0000269|PubMed:25232112, ECO:0000269|PubMed:25644602, ECO:0000269|PubMed:28087714}. DOMAIN: The guanylate kinase-like domain interacts with the SH3 domain. {ECO:0000269|PubMed:25232112}. TISSUE SPECIFICITY: Brain (at protein level). {ECO:0000269|PubMed:25232112}. +P11531 DMD_MOUSE Dystrophin 3678 425,832 Chain (1); Domain (3); Modified residue (9); Region (5); Repeat (24); Sequence conflict (2); Zinc finger (1) FUNCTION: Anchors the extracellular matrix to the cytoskeleton via F-actin. Ligand for dystroglycan. Component of the dystrophin-associated glycoprotein complex which accumulates at the neuromuscular junction (NMJ) and at a variety of synapses in the peripheral and central nervous systems and has a structural function in stabilizing the sarcolemma. Also implicated in signaling events and synaptic transmission. {ECO:0000269|PubMed:7633443}. SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000269|PubMed:19109891}; Peripheral membrane protein {ECO:0000269|PubMed:19109891}; Cytoplasmic side {ECO:0000269|PubMed:19109891}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19109891}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000269|PubMed:19109891}. Note=In muscle cells, sarcolemma localization requires the presence of ANK2, while localization to costameres requires the presence of ANK3. Localizes to neuromuscular junctions (NMJs). In adult muscle, NMJ localization depends upon ANK2 presence, but not in newborn animals. SUBUNIT: Interacts with SYNM (PubMed:16777071). Interacts with the syntrophins SNTG1 and SNTG2. Interacts with KRT19. Component of the dystrophin-associated glycoprotein complex which is composed of three subcomplexes: a cytoplasmic complex comprised of DMD (or UTRN), DTNA and a number of syntrophins, such as SNTB1, SNTB2, SNTG1 and SNTG2, the transmembrane dystroglycan complex, and the sarcoglycan-sarcospan complex. Interacts with DAG1 (betaDAG1) with DMD; the interaction is inhibited by phosphorylation on the PPXY motif of DAG1 (By similarity). Interacts with SYNM; SNTA1 and SNTB1. Interacts with CMYA5 (PubMed:20634290). Directly interacts with ANK2 and ANK3; these interactions do not interfere with betaDAG1-binding and are necessary for proper localization in muscle cells (PubMed:19109891). Identified in a dystroglycan complex that contains at least PRX, DRP2, UTRN, DMD and DAG1 (PubMed:11430802). {ECO:0000250|UniProtKB:P11532, ECO:0000269|PubMed:11430802, ECO:0000269|PubMed:11520903, ECO:0000269|PubMed:16777071, ECO:0000269|PubMed:19109891, ECO:0000269|PubMed:20634290, ECO:0000269|PubMed:7547961, ECO:0000269|PubMed:9214383}. TISSUE SPECIFICITY: Detected in quadriceps muscle and in sciatic nerve (at protein level) (PubMed:11430802). Differentially expressed during skeletal muscle, heart, and brain development. Also expressed in retina (PubMed:7633443). {ECO:0000269|PubMed:11430802, ECO:0000269|PubMed:7633443}. +Q61089 FZD6_MOUSE Frizzled-6 (Fz-6) (mFz6) 709 79,082 Chain (1); Disulfide bond (5); Domain (1); Glycosylation (3); Modified residue (1); Motif (1); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 202 222 Helical; Name=1. {ECO:0000255}.; TRANSMEM 234 254 Helical; Name=2. {ECO:0000255}.; TRANSMEM 285 305 Helical; Name=3. {ECO:0000255}.; TRANSMEM 325 345 Helical; Name=4. {ECO:0000255}.; TRANSMEM 371 391 Helical; Name=5. {ECO:0000255}.; TRANSMEM 417 437 Helical; Name=6. {ECO:0000255}.; TRANSMEM 474 494 Helical; Name=7. {ECO:0000255}. TOPO_DOM 19 201 Extracellular. {ECO:0000255}.; TOPO_DOM 223 233 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 255 284 Extracellular. {ECO:0000255}.; TOPO_DOM 306 324 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 346 370 Extracellular. {ECO:0000255}.; TOPO_DOM 392 416 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 438 473 Extracellular. {ECO:0000255}.; TOPO_DOM 495 709 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for Wnt proteins. Most of frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. Activation by Wnt5A stimulates PKC activity via a G-protein-dependent mechanism. Involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues (By similarity). Together with FZD3, is involved in the neural tube closure and plays a role in the regulation of the establishment of planar cell polarity (PCP), particularly in the orientation of asymmetric bundles of stereocilia on the apical faces of a subset of auditory and vestibular sensory cells located in the inner ear. {ECO:0000250, ECO:0000269|PubMed:16495441}. PTM: Ubiquitinated by ZNRF3, leading to its degradation by the proteasome. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10097073}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:10097073}; Multi-pass membrane protein {ECO:0000255}. Cell surface {ECO:0000269|PubMed:16495441}. Apical cell membrane {ECO:0000269|PubMed:16495441}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:16495441}; Multi-pass membrane protein {ECO:0000255}. Note=Colocalizes with FZD3 at the apical face of cells (PubMed:16495441). {ECO:0000269|PubMed:16495441}. DOMAIN: Lys-Thr-X-X-X-Trp motif interacts with the PDZ domain of Dvl (Disheveled) family members and is involved in the activation of the Wnt/beta-catenin signaling pathway. {ECO:0000250}.; DOMAIN: The FZ domain is involved in binding with Wnt ligands. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in both hair cells and supporting cells in the utricle, saccule, cristae and the organ of Corti in the inner ear (at protein level). {ECO:0000269|PubMed:16495441}. +Q9R216 FZD9_MOUSE Frizzled-9 (Fz-9) (mFz3) (mFz9) (CD antigen CD349) 592 64,995 Chain (1); Disulfide bond (5); Domain (1); Glycosylation (2); Motif (1); Region (2); Sequence conflict (9); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 231 251 Helical; Name=1. {ECO:0000255}.; TRANSMEM 268 288 Helical; Name=2. {ECO:0000255}.; TRANSMEM 317 337 Helical; Name=3. {ECO:0000255}.; TRANSMEM 357 377 Helical; Name=4. {ECO:0000255}.; TRANSMEM 402 422 Helical; Name=5. {ECO:0000255}.; TRANSMEM 449 469 Helical; Name=6. {ECO:0000255}.; TRANSMEM 510 530 Helical; Name=7. {ECO:0000255}. TOPO_DOM 24 230 Extracellular.; TOPO_DOM 252 267 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 289 316 Extracellular. {ECO:0000255}.; TOPO_DOM 338 356 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 378 401 Extracellular. {ECO:0000255}.; TOPO_DOM 423 448 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 470 509 Extracellular. {ECO:0000255}.; TOPO_DOM 531 592 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for WNT2 that is coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes (By similarity). Plays a role in neuromuscular junction (NMJ) assembly by negatively regulating the clustering of acetylcholine receptors (AChR) through the beta-catenin canonical signaling pathway (PubMed:24860427). May play a role in neural progenitor cells (NPCs) viability through the beta-catenin canonical signaling pathway by negatively regulating cell cycle arrest leading to inhibition of neuron apoptotic process (By similarity). During hippocampal development, regulates neuroblast proliferation and apoptotic cell death (PubMed:15930120). Controls bone formation through non canonical Wnt signaling mediated via ISG15 (PubMed:21402791). Positively regulates bone regeneration through non canonical Wnt signaling (PubMed:24391920). {ECO:0000250|UniProtKB:O00144, ECO:0000250|UniProtKB:Q8K4C8, ECO:0000269|PubMed:15930120, ECO:0000269|PubMed:21402791, ECO:0000269|PubMed:24391920, ECO:0000269|PubMed:24860427}. PTM: Ubiquitinated by ZNRF3, leading to its degradation by the proteasome. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24860427}; Multi-pass membrane protein {ECO:0000255}. Note=Relocalizes DVL1 to the cell membrane leading to phosphorylation of DVL1 and AXIN1 relocalization to the cell membrane. {ECO:0000250|UniProtKB:Q8K4C8}. DOMAIN: Lys-Thr-X-X-X-Trp motif interacts with the PDZ domain of Dvl (Disheveled) family members and is involved in the activation of the Wnt/beta-catenin signaling pathway. {ECO:0000250}.; DOMAIN: The FZ domain is involved in binding with Wnt ligands. {ECO:0000250}. TISSUE SPECIFICITY: In the embryo, found in the neural tube, trunk skeletal muscle precursors (myotomes), limb skeletal anlagen, craniofacial regions and nephric ducts. In the adult, expression is abundant in heart, brain, testis and skeletal muscle. In the testis, expressed in all spermatogenic cell types. Lower levels in adult lung, liver and kidney. Barely detectable in spleen. Expressed also in chondrocytes. +P54103 DNJC2_MOUSE DnaJ homolog subfamily C member 2 (Mouse Id associate 1) (MIDA1) (Zuotin-related factor 1) 621 71,722 Chain (1); Domain (3); Modified residue (6); Region (1); Sequence conflict (3) FUNCTION: Acts both as a chaperone in the cytosol and as a chromatin regulator in the nucleus. When cytosolic, acts as a molecular chaperone: component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding-competent state. In the RAC complex, stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones HSPA14 that bind to the nascent polypeptide chain. When nuclear, mediates the switching from polycomb-repressed genes to an active state: specifically recruited at histone H2A ubiquitinated at 'Lys-119' (H2AK119ub), and promotes the displacement of the polycomb PRC1 complex from chromatin, thereby facilitating transcription activation (By similarity). Specifically binds DNA sequence 5'-GTCAAGC-3'. {ECO:0000250}. PTM: Phosphorylated in M (mitotic) phase. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00624, ECO:0000269|PubMed:8666407}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q99543}. SUBUNIT: Component of ribosome-associated complex (RAC), a heterodimer composed of Hsp70/DnaK-type chaperone HSPA14 and Hsp40/DnaJ-type chaperone DNAJC2 (By similarity). Interacts (via ZRF1-UBD region) with ID1. {ECO:0000250, ECO:0000269|PubMed:10581180, ECO:0000269|PubMed:7559602}. DOMAIN: The ZRF1-UBD region specifically recognizes and binds H2AK119ub. The ZRF1-UBD region is also involved in protein-protein interactions with other proteins, suggesting that it may be masked by some regulator, thereby preventing its association with H2AK119ub (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in all tissues. {ECO:0000269|PubMed:8666407}. +P51141 DVL1_MOUSE Segment polarity protein dishevelled homolog DVL-1 (Dishevelled-1) (DSH homolog 1) 695 75,359 Beta strand (21); Chain (1); Compositional bias (1); Domain (3); Helix (8); Modified residue (1); Mutagenesis (4); Sequence conflict (3); Turn (3) FUNCTION: Participates in Wnt signaling by binding to the cytoplasmic C-terminus of frizzled family members and transducing the Wnt signal to down-stream effectors. Plays a role both in canonical and non-canonical Wnt signaling. Plays a role in the signal transduction pathways mediated by multiple Wnt genes. Required for LEF1 activation upon WNT1 and WNT3A signaling. DVL1 and PAK1 form a ternary complex with MUSK which is important for MUSK-dependent regulation of AChR clustering during the formation of the neuromuscular junction (NMJ). {ECO:0000269|PubMed:11101902, ECO:0000269|PubMed:12165471, ECO:0000269|PubMed:15353129, ECO:0000269|PubMed:19637179}. PTM: Ubiquitinated; undergoes both 'Lys-48'-linked ubiquitination, leading to its subsequent degradation by the ubiquitin-proteasome pathway, and 'Lys-63'-linked ubiquitination. The interaction with INVS is required for ubiquitination (By similarity). Deubiquitinated by CYLD, which acts on 'Lys-63'-linked ubiquitin chains. {ECO:0000250, ECO:0000269|PubMed:20227366}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15353129}; Peripheral membrane protein {ECO:0000269|PubMed:15353129}; Cytoplasmic side {ECO:0000269|PubMed:15353129}. Cytoplasm, cytosol {ECO:0000269|PubMed:15353129}. Cytoplasmic vesicle {ECO:0000269|PubMed:15353129}. Note=Localizes at the cell membrane upon interaction with frizzled family members. SUBUNIT: Interacts with CXXC4 (By similarity). Interacts (via PDZ domain) with TMEM88 (By similarity). Interacts with BRD7 and INVS. Interacts through its PDZ domain with the C-terminal regions of VANGL1, VANGL2 and CCDC88C/DAPLE. Interacts (via PDZ domain) with NXN. Interacts with ARRB1; the interaction is enhanced by phosphorylation of DVL1 (By similarity). Interacts with CYLD. Interacts (via PDZ domain) with RYK. Self-associates (via DIX domain) and forms higher homooligomers. Interacts (via PDZ domain) with DACT1 and FZD7, where DACT1 and FZD7 compete for the same binding site. Interacts (via DEP domain) with MUSK; the interaction is direct and mediates the formation a DVL1, MUSK and PAK1 ternary complex involved in AChR clustering. Interacts with DCDC2. Interacts with FOXK2 (By similarity). Interacts with PKD1 (via extracellular domain) (PubMed:27214281). {ECO:0000250|UniProtKB:O14640, ECO:0000250|UniProtKB:Q9WVB9, ECO:0000269|PubMed:12165471, ECO:0000269|PubMed:12941796, ECO:0000269|PubMed:14636582, ECO:0000269|PubMed:15353129, ECO:0000269|PubMed:15454084, ECO:0000269|PubMed:15456783, ECO:0000269|PubMed:16604061, ECO:0000269|PubMed:19637179, ECO:0000269|PubMed:20227366, ECO:0000269|PubMed:21189423, ECO:0000269|PubMed:27214281}. DOMAIN: The DIX domain promotes homooligomerization.; DOMAIN: The DEP domain mediates interaction with the cell membrane. TISSUE SPECIFICITY: High levels are seen in the brain, testis and kidney, lower levels in the ovary, breast, muscle, liver and small intestine, and very low levels are seen in the spleen and thymus. A moderate level expression is seen in the heart. +Q60838 DVL2_MOUSE Segment polarity protein dishevelled homolog DVL-2 (Dishevelled-2) (DSH homolog 2) 736 78,861 Beta strand (5); Chain (1); Compositional bias (4); Domain (3); Helix (3); Modified residue (1); Mutagenesis (11); Sequence conflict (1) FUNCTION: Plays a role in the signal transduction pathways mediated by multiple Wnt genes. Participates both in canonical and non-canonical Wnt signaling by binding to the cytoplasmic C-terminus of frizzled family members and transducing the Wnt signal to down-stream effectors. Promotes internalization and degradation of frizzled proteins upon Wnt signaling. {ECO:0000269|PubMed:17199046, ECO:0000269|PubMed:20947020, ECO:0000269|PubMed:21189423}. PTM: Phosphorylated by CSNK1D (By similarity). WNT3A induces DVL2 phosphorylation by CSNK1E and MARK kinases (By similarity). {ECO:0000250|UniProtKB:O14641}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17199046, ECO:0000269|PubMed:20947020}; Peripheral membrane protein {ECO:0000269|PubMed:20947020}; Cytoplasmic side {ECO:0000269|PubMed:20947020}. Cytoplasm, cytosol {ECO:0000269|PubMed:21189423}. Cytoplasmic vesicle {ECO:0000269|PubMed:17199046, ECO:0000269|PubMed:21189423}. Nucleus {ECO:0000250|UniProtKB:O14641}. Note=Localizes at the cell membrane upon interaction with frizzled family members and promotes their internalization (PubMed:21189423). Localizes to cytoplasmic puncta. Interaction with FOXK1 and FOXK2 induces nuclear translocation (By similarity). {ECO:0000250|UniProtKB:O14641, ECO:0000269|PubMed:21189423}. SUBUNIT: Interacts through its PDZ domain with the C-terminal regions of VANGL1 and VANGL2. Interacts with Rac. Interacts with ARRB1; the interaction is enhanced by phosphorylation of DVL1 (By similarity). Can form large oligomers (via DIX domain). Interacts (via DIX domain) with DIXDC1 (via DIX domain). Interacts (via DEP domain) with AP2M1 and the AP-2 complex. Interacts with FAM105B/otulin. Interacts with DCDC2. Interacts (when phosphorylated) with FOXK1 and FOXK2; the interaction induces DVL2 nuclear translocation (By similarity). Interacts with MAPK15 (PubMed:25823377). Interacts with PKD1 (via extracellular domain) (PubMed:27214281). {ECO:0000250|UniProtKB:O14641, ECO:0000269|PubMed:15262978, ECO:0000269|PubMed:15456783, ECO:0000269|PubMed:17199046, ECO:0000269|PubMed:20947020, ECO:0000269|PubMed:21189423, ECO:0000269|PubMed:23708998, ECO:0000269|PubMed:25823377, ECO:0000269|PubMed:27214281}. DOMAIN: The DIX domain mediates homooligomerization. {ECO:0000269|PubMed:21189423}. TISSUE SPECIFICITY: Ubiquitous. +P48316 GA45A_MOUSE Growth arrest and DNA damage-inducible protein GADD45 alpha (DNA damage-inducible transcript 1 protein) (DDIT-1) 165 18,339 Chain (1); Modified residue (1); Region (2) FUNCTION: Might affect PCNA interaction with some CDK (cell division protein kinase) complexes; stimulates DNA excision repair in vitro and inhibits entry of cells into S phase. In T-cells, functions as a regulator of p38 MAPKs by inhibiting p88 phosphorylation and activity. {ECO:0000269|PubMed:15735649}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with AURKA, GADD45GIP1 and PCNA (By similarity). Interacts with MAPK14. {ECO:0000250, ECO:0000269|PubMed:15735649}. +P22339 GA45B_MOUSE Growth arrest and DNA damage-inducible protein GADD45 beta (Myeloid differentiation primary response protein MyD118) (Negative growth regulatory protein MyD118) 160 17,783 Chain (1) FUNCTION: Involved in the regulation of growth and apoptosis. Mediates activation of stress-responsive MTK1/MEKK4 MAPKKK (By similarity). {ECO:0000250}. SUBUNIT: Interacts with GADD45GIP1. {ECO:0000250}. TISSUE SPECIFICITY: In myeloid precursor enriched BM cells. +Q9QYY0 GAB1_MOUSE GRB2-associated-binding protein 1 (GRB2-associated binder 1) (Growth factor receptor bound protein 2-associated protein 1) 695 76,812 Chain (1); Compositional bias (1); Domain (1); Initiator methionine (1); Modified residue (13); Sequence conflict (3) FUNCTION: Adapter protein that plays a role in intracellular signaling cascades triggered by activated receptor-type kinases. Plays a role in FGFR1 signaling. Probably involved in signaling by the epidermal growth factor receptor (EGFR) and the insulin receptor (INSR). Involved in the MET/HGF-signaling pathway. {ECO:0000250|UniProtKB:Q13480}. PTM: Phosphorylated on tyrosine residue(s) by the epidermal growth factor receptor (EGFR) and the insulin receptor (INSR). Tyrosine phosphorylation of GAB1 mediates interaction with several proteins that contain SH2 domains. Phosphorylated on tyrosine residues by HCK upon IL6 signaling (By similarity). Phosphorylated in response to FGFR1 activation. {ECO:0000250, ECO:0000269|PubMed:11353842}. SUBUNIT: Interacts with GRB2 and with other SH2-containing proteins (PubMed:11353842). Interacts with phosphorylated LAT2. Interacts with PTPRJ (By similarity). Interacts (phosphorylated) with PTPN11 (By similarity). Interacts with HCK (By similarity). Identified in a complex containing FRS2, GRB2, GAB1, PIK3R1 and SOS1 (By similarity). Part of a tripartite complex containing GAB1, METTL13 and SPRY2. Interacts with METTL13 (By similarity). {ECO:0000250|UniProtKB:Q13480, ECO:0000269|PubMed:11353842}. TISSUE SPECIFICITY: Expressed in the inner ear. Expression is detected in the cochlear duct, spiral limbus region, efferent and afferent nerves, and in spiral ganglion neurons. {ECO:0000269|PubMed:29408807}. +Q61598 GDIB_MOUSE Rab GDP dissociation inhibitor beta (Rab GDI beta) (GDI-3) (Guanosine diphosphate dissociation inhibitor 2) (GDI-2) 445 50,537 Alternative sequence (1); Chain (1); Modified residue (6); Sequence conflict (2) FUNCTION: Regulates the GDP/GTP exchange reaction of most Rab proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. SUBUNIT: Interacts with RHOH. {ECO:0000250}. +Q66JS6 EI3JB_MOUSE Eukaryotic translation initiation factor 3 subunit J-B (eIF3j-B) (Eukaryotic translation initiation factor 3 subunit 1-B) (eIF-3-alpha-B) (eIF3 p35) 263 29,486 Chain (1); Coiled coil (1); Cross-link (1); Initiator methionine (1); Modified residue (7); Region (2); Sequence conflict (1) FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression. This subunit binds directly within the mRNA entry channel of the 40S ribosome to the aminoacyl (A) site. It may regulate the interaction between the 43S PIC and mRNA. {ECO:0000255|HAMAP-Rule:MF_03009}. PTM: Phosphorylated. Phosphorylation is enhanced upon serum stimulation. {ECO:0000255|HAMAP-Rule:MF_03009}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03009}. SUBUNIT: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B, EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and EIF3M. The eIF-3 complex appears to include 3 stable modules: module A is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D, EIF3E, EIF3K and EIF3L. EIF3C of module C binds EIF3B of module A and EIF3H of module B, thereby linking the three modules. EIF3J is a labile subunit that binds to the eIF-3 complex via EIF3B. The eIF-3 complex interacts with RPS6KB1 under conditions of nutrient depletion. Mitogenic stimulation leads to binding and activation of a complex composed of MTOR and RPTOR, leading to phosphorylation and release of RPS6KB1 and binding of EIF4B to eIF-3. {ECO:0000255|HAMAP-Rule:MF_03009}. +Q9DCH4 EIF3F_MOUSE Eukaryotic translation initiation factor 3 subunit F (eIF3f) (Deubiquitinating enzyme eIF3f) (EC 3.4.19.12) (Eukaryotic translation initiation factor 3 subunit 5) (eIF-3-epsilon) (eIF3 p47) 361 37,984 Chain (1); Domain (1); Initiator methionine (1); Modified residue (4); Sequence conflict (1) FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression. {ECO:0000255|HAMAP-Rule:MF_03005}.; FUNCTION: Deubiquitinates activated NOTCH1, promoting its nuclear import, thereby acting as a positive regulator of Notch signaling. {ECO:0000255|HAMAP-Rule:MF_03005, ECO:0000269|PubMed:17581632}. PTM: Phosphorylation is enhanced upon serum stimulation. Phosphorylated during apoptosis by caspase-processed CDK11 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03005}. SUBUNIT: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B, EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and EIF3M. The eIF-3 complex appears to include 3 stable modules: module A is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D, EIF3E, EIF3K and EIF3L. EIF3C of module C binds EIF3B of module A and EIF3H of module B, thereby linking the three modules. EIF3J is a labile subunit that binds to the eIF-3 complex via EIF3B. The eIF-3 complex may interact with RPS6KB1 under conditions of nutrient depletion. Mitogenic stimulation may lead to binding and activation of a complex composed of MTOR and RPTOR, leading to phosphorylation and release of RPS6KB1 and binding of EIF4B to eIF-3. Interacts with RNF139; the interaction leads to protein translation inhibitions in a ubiquitination-dependent manner. Interacts with DTX1, the interaction is required for deubiquitinating activity towards NOTCH1 (By similarity). {ECO:0000255|HAMAP-Rule:MF_03005}. DOMAIN: The MPN domain mediates deubiquitinating activity. {ECO:0000250}. +Q8BYZ7 ELMO3_MOUSE Engulfment and cell motility protein 3 720 81,758 Alternative sequence (1); Chain (1); Domain (2); Motif (1) FUNCTION: Involved in cytoskeletal rearrangements required for phagocytosis of apoptotic cells and cell motility. Acts in association with DOCK1 and CRK. Was initially proposed to be required in complex with DOCK1 to activate Rac Rho small GTPases. May enhance the guanine nucleotide exchange factor (GEF) activity of DOCK1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Probably interacts directly with the SH3-domain of DOCK1 via its SH3-binding site. Part of a complex with DOCK1 and RAC1 (By similarity). Interacts with ADGRB3 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q96BJ8}. +Q3UPW2 ELF3_MOUSE ETS-related transcription factor Elf-3 (E74-like factor 3) (Epithelial-restricted with serine box) (Epithelium-restricted Ets protein ESX) (Epithelium-specific Ets transcription factor 1) (ESE-1) 391 44,273 Alternative sequence (1); Beta strand (3); Chain (1); DNA binding (1); Domain (1); Helix (4); Mutagenesis (5); Turn (3) FUNCTION: Transcriptional activator that binds and transactivates ETS sequences containing the consensus nucleotide core sequence GGA[AT]. Acts synergistically with POU2F3 to transactivate the SPRR2A promoter and with RUNX1 to transactivate the ANGPT1 promoter (By similarity). Also transactivates collagenase, CCL20, CLND7, FLG, KRT8, NOS2, PTGS2, SPRR2B, TGFBR2 and TGM3 promoters. Represses KRT4 promoter activity (By similarity). Involved in mediating vascular inflammation. May play an important role in epithelial cell differentiation and tumorigenesis. May be a critical downstream effector of the ERBB2 signaling pathway (By similarity). May be associated with mammary gland development and involution. Plays an important role in the regulation of transcription with TATA-less promoters in preimplantation embryos, which is essential in preimplantation development. {ECO:0000250|UniProtKB:P78545, ECO:0000269|PubMed:11893733, ECO:0000269|PubMed:11984530, ECO:0000269|PubMed:16630543, ECO:0000269|PubMed:9806763}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P78545}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00237, ECO:0000269|PubMed:16516205}. SUBUNIT: Interacts with TBP. Interacts with CREBBP and EP300; these act as transcriptional coactivators of ELF3 and positively modulate its function. Interacts with XRCC5/KU86 and XRCC6/KU70; these inhibit the ability of ELF3 to bind DNA and negatively modulate its transcriptional activity. Associated with CLND7 and POU2F3 (By similarity). {ECO:0000250|UniProtKB:P78545}. TISSUE SPECIFICITY: Expressed in small intestine, colon, lung, kidney and uterus. Also expressed in the corneal epithelium and conjunctiva of the developing and adult eye. Not detected in liver, spleen, thymus, brain, heart, skeletal muscle or ovary. {ECO:0000269|PubMed:11025204, ECO:0000269|PubMed:9395241}. +P41969 ELK1_MOUSE ETS domain-containing protein Elk-1 429 45,271 Chain (1); Cross-link (3); DNA binding (1); Modified residue (9); Region (1); Sequence conflict (2) FUNCTION: Transcription factor that binds to purine-rich DNA sequences. Forms a ternary complex with SRF and the ETS and SRF motifs of the serum response element (SRE) on the promoter region of immediate early genes such as FOS and IER2 (By similarity). Induces target gene transcription upon JNK-signaling pathway stimulation (By similarity). {ECO:0000250|UniProtKB:A4GTP4, ECO:0000250|UniProtKB:P19419}. PTM: Sumoylation represses transcriptional activator activity as it results in recruitment of HDAC2 to target gene promoters which leads to decreased histone acetylation and reduced transactivator activity. It also regulates nuclear retention (By similarity). {ECO:0000250|UniProtKB:P19419}.; PTM: On mitogenic stimulation, phosphorylated on C-terminal serine and threonine residues by MAPK1 but also MAPK8 and/or MAPK9. Phosphorylation leads to loss of sumoylation and restores transcriptional activator activity. Phosphorylated and activated by CaMK4, MAPK11, MAPK12 and MAPK14 (By similarity). Upon bFGF stimulus, phosphorylated by PAK1 (By similarity). {ECO:0000250|UniProtKB:A4GTP4, ECO:0000250|UniProtKB:P19419}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts in its sumoylated form with PIAS2/PIASX which enhances its transcriptional activator activity. Interacts with MAD2L2; the interaction is direct and promotes phosphorylation by the kinases MAPK8 and/or MAPK9. Interacts with POU1F1. {ECO:0000250|UniProtKB:P19419}. TISSUE SPECIFICITY: Predominantly expressed in the brain, and to a lesser extent in the heart, liver and muscle. +Q80VR2 ELL3_MOUSE RNA polymerase II elongation factor ELL3 395 44,762 Chain (1); Modified residue (1) FUNCTION: Enhancer-binding elongation factor that specifically binds enhancers in embryonic stem cells (ES cells), marks them, and is required for their future activation during stem cell specification. Elongation factor component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. Component of the little elongation complex (LEC), a complex required to regulate small nuclear RNA (snRNA) gene transcription by RNA polymerase II and III. Does not only bind to enhancer regions of active genes, but also marks the enhancers that are in a poised or inactive state in ES cells and is required for establishing proper RNA polymerase II occupancy at developmentally regulated genes in a cohesin-dependent manner. Probably required for priming developmentally regulated genes for later recruitment of the super elongation complex (SEC), for transcriptional activation during differentiation. Required for recruitment of P-TEFb within SEC during differentiation. Probably preloaded on germ cell chromatin, suggesting that it may prime gene activation by marking enhancers as early as in the germ cells. Promoting epithelial-mesenchymal transition (EMT). {ECO:0000269|PubMed:22768269, ECO:0000269|PubMed:23273992}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23273992}. SUBUNIT: Component of the little elongation complex (LEC), at least composed of ELL (ELL, ELL2 or ELL3), ZC3H8, ICE1 and ICE2 (By similarity). Component of the super elongation complex (SEC), at least composed of EAF1, EAF2, CDK9, MLLT3/AF9, AFF (AFF1 or AFF4), the P-TEFb complex and ELL (ELL, ELL2 or ELL3). Interacts with AFF4. {ECO:0000250, ECO:0000269|PubMed:20159561, ECO:0000269|PubMed:23273992}. TISSUE SPECIFICITY: Actively expressed in embryonic stem cells (ES cells), while it is weakly expressed in differentiated cells. {ECO:0000269|PubMed:22768269}. +Q8CJF7 ELYS_MOUSE Protein ELYS (Embryonic large molecule derived from yolk sac) (Protein MEL-28) (Putative AT-hook-containing transcription factor 1) 2243 247,646 Beta strand (30); Chain (1); DNA binding (1); Helix (11); Modified residue (30); Mutagenesis (2); Region (7); Sequence conflict (5); Turn (5) FUNCTION: Required for the assembly of a functional nuclear pore complex (NPC) on the surface of chromosomes as nuclei form at the end of mitosis. May initiate NPC assembly by binding to chromatin and recruiting the Nup107-160 subcomplex of the NPC. Also required for the localization of the Nup107-160 subcomplex of the NPC to the kinetochore during mitosis and for the completion of cytokinesis (By similarity). Has also been proposed to function as a transcription factor which may play a specific role in hematopoietic tissues (PubMed:11952839). {ECO:0000250, ECO:0000269|PubMed:11952839}. SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000269|PubMed:11952839}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:23499022}. Nucleus matrix {ECO:0000269|PubMed:23499022}. Cytoplasm {ECO:0000269|PubMed:11952839}. Note=Localizes to the nuclear pore complex (NPC) throughout interphase. Localizes to the kinetochore from prophase, and this appears to require the Nup107-160 subcomplex of the NPC. Localizes to the periphery of chromatin from late anaphase (By similarity). {ECO:0000250|UniProtKB:Q8WYP5}. SUBUNIT: Associates with the Nup107-160 subcomplex of the NPC. {ECO:0000250}. DOMAIN: The N-terminus forms a highly conserved seven-bladed beta propeller decorated with long loops and mediates anchorage to the Nup107-160 subcomplex of the nuclear pore, synergistically with the central alpha domain. The disordered C-terminus is responsible for the interactions with chromatin (PubMed:23499022). {ECO:0000269|PubMed:23499022}. TISSUE SPECIFICITY: Widely expressed with higher expression in testis, lung and kidney. Expressed in T-cells, B-cells and granulocytes in bone marrow. {ECO:0000269|PubMed:11952839}. +Q8R0J8 GNTK_MOUSE Probable gluconokinase (EC 2.7.1.12) (Gluconate kinase) 184 19,981 Chain (1); Erroneous initiation (1); Nucleotide binding (1) Carbohydrate acid metabolism; D-gluconate degradation. +P08113 ENPL_MOUSE Endoplasmin (94 kDa glucose-regulated protein) (GRP-94) (Endoplasmic reticulum resident protein 99) (ERp99) (Heat shock protein 90 kDa beta member 1) (Polymorphic tumor rejection antigen 1) (Tumor rejection antigen gp96) 802 92,476 Binding site (6); Chain (1); Disulfide bond (1); Glycosylation (6); Modified residue (9); Motif (1); Mutagenesis (1); Signal peptide (1) FUNCTION: Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors. Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity (By similarity). {ECO:0000250, ECO:0000269|PubMed:20865800}. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000269|PubMed:20865800}. Melanosome {ECO:0000250}. SUBUNIT: Homodimer; disulfide-linked. Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5. Part of a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX. Interacts with OS9 (By similarity). Interacts with AIMP1; regulates its retention in the endoplasmic reticulum. Interacts with CNPY3; this interaction is disrupted in the presence of ATP. Interacts with TLR4, TLR9 and TLR11, but not with TLR3. Interacts with MZB1 in a calcium-dependent manner. Interacts with METTL23 (By similarity). {ECO:0000250}. +P06802 ENPP1_MOUSE Ectonucleotide pyrophosphatase/phosphodiesterase family member 1 (E-NPP 1) (Lymphocyte antigen 41) (Ly-41) (Phosphodiesterase I/nucleotide pyrophosphatase 1) (Plasma-cell membrane glycoprotein PC-1) [Includes: Alkaline phosphodiesterase I (EC 3.1.4.1); Nucleotide pyrophosphatase (NPPase) (EC 3.6.1.9) (Nucleotide diphosphatase)] 906 103,176 Active site (1); Alternative sequence (1); Beta strand (39); Binding site (3); Chain (1); Disulfide bond (16); Domain (2); Glycosylation (6); Helix (36); Metal binding (12); Modified residue (2); Motif (1); Mutagenesis (20); Natural variant (2); Region (3); Site (2); Topological domain (2); Transmembrane (1); Turn (14) TRANSMEM 59 79 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 58 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 80 906 Extracellular. {ECO:0000255}. FUNCTION: Appears to modulate insulin sensitivity (By similarity). By generating PPi, plays a role in regulating pyrophosphate levels, and functions in bone mineralization and soft tissue calcification. PPi inhibits mineralization by binding to nascent hydroxyapatite (HA) crystals, thereby preventing further growth of these crystals. Preferentially hydrolyzes ATP, but can also hydrolyze other nucleoside 5' triphosphates such as GTP, CTP, TTP and UTP to their corresponding monophosphates with release of pyrophosphate and diadenosine polyphosphates, and also 3',5'-cAMP to AMP. May also be involved in the regulation of the availability of nucleotide sugars in the endoplasmic reticulum and Golgi, and the regulation of purinergic signaling. {ECO:0000250|UniProtKB:P22413, ECO:0000269|PubMed:1647027, ECO:0000269|PubMed:9662402}. PTM: The N-terminal is blocked.; PTM: N-glycosylated. {ECO:0000269|PubMed:1647027, ECO:0000269|PubMed:19656770, ECO:0000269|PubMed:23027977, ECO:0000269|PubMed:23041369, ECO:0000269|PubMed:8223581}.; PTM: A secreted form is produced through cleavage at Lys-85 by intracellular processing. SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein. Basolateral cell membrane; Single-pass type II membrane protein. Secreted. Note=Targeted to the basolateral membrane in polarized epithelial cells and in hepatocytes, and to matrix vesicles in osteoblasts. In bile duct cells and cancer cells, located to the apical cytoplasmic side (By similarity). The proteolytically processed form is secreted. {ECO:0000250|UniProtKB:P22413}. SUBUNIT: Homodimer. The secreted form is monomeric. Interacts with INSR. {ECO:0000250}. DOMAIN: The di-leucine motif is required for basolateral targeting in polarized epithelial cells, and for targeting to matrix vesicles derived from mineralizing cells. TISSUE SPECIFICITY: Selectively expressed on the surface of antibody-secreting cells. DISEASE: Note=Defects in Enpp1 are the cause of the tiptoe walking (ttw) phenotype. Ttw mice exhibit ossification of the spinal ligaments. {ECO:0000269|PubMed:9662402}. +Q8BYG9 EPHAA_MOUSE Ephrin type-A receptor 10 (EC 2.7.10.1) 1007 109,100 Alternative sequence (2); Chain (1); Domain (5); Erroneous gene model prediction (1); Glycosylation (2); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 566 586 Helical. {ECO:0000255}. TOPO_DOM 23 565 Extracellular. {ECO:0000255}.; TOPO_DOM 587 1007 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for members of the ephrin-A family. Binds to EFNA3, EFNA4 and EFNA5 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. DOMAIN: The protein kinase domain is predicted to be catalytically inactive. +Q9WUA5 EPM2A_MOUSE Laforin (EC 3.1.3.-) (EC 3.1.3.16) (EC 3.1.3.48) (Glucan phosphatase) (Lafora PTPase) (LAFPTPase) 330 36,958 Active site (1); Binding site (6); Chain (1); Domain (2); Modified residue (1); Motif (1); Mutagenesis (8); Region (2); Sequence conflict (1); Site (1) FUNCTION: Plays an important role in preventing glycogen hyperphosphorylation and the formation of insoluble aggregates, via its activity as glycogen phosphatase, and by promoting the ubiquitination of proteins involved in glycogen metabolism via its interaction with the E3 ubiquitin ligase NHLRC1/malin (PubMed:18040046, PubMed:18852261, PubMed:19036738, PubMed:23663739, PubMed:24430976, PubMed:24068615). Dephosphorylates phosphotyrosine and synthetic substrates, such as para-nitrophenylphosphate (pNPP), and has low activity with phosphoserine and phosphothreonine substrates (in vitro) (PubMed:16971387, PubMed:24430976). Has also been shown to dephosphorylate MAPT (PubMed:19542233). Shows strong phosphatase activity towards complex carbohydrates in vitro, avoiding glycogen hyperphosphorylation which is associated with reduced branching and formation of insoluble aggregates (PubMed:18040046, PubMed:18852261, PubMed:23663739). Forms a complex with NHLRC1/malin and HSP70, which suppresses the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system (UPS) (PubMed:19036738, PubMed:24068615). Acts as a scaffold protein to facilitate PPP1R3C/PTG ubiquitination by NHLRC1/malin. Also promotes proteasome-independent protein degradation through the macroautophagy pathway (PubMed:20453062). {ECO:0000269|PubMed:16971387, ECO:0000269|PubMed:18040046, ECO:0000269|PubMed:18852261, ECO:0000269|PubMed:19036738, ECO:0000269|PubMed:19542233, ECO:0000269|PubMed:20453062, ECO:0000269|PubMed:22669944, ECO:0000269|PubMed:23663739, ECO:0000269|PubMed:24068615, ECO:0000269|PubMed:24430976}. PTM: Polyubiquitinated by NHLRC1/malin. {ECO:0000250|UniProtKB:O95278}.; PTM: Phosphorylation on Ser-25 by AMPK affects the phosphatase activity of the enzyme and its ability to homodimerize and interact with NHLRC1, PPP1R3C or PRKAA2. {ECO:0000250|UniProtKB:O95278}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O95278}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O95278}; Peripheral membrane protein {ECO:0000250|UniProtKB:O95278}; Cytoplasmic side {ECO:0000250|UniProtKB:O95278}. Cell membrane {ECO:0000250|UniProtKB:O95278}. Note=Colocalizes with glycogen synthase in punctate structures in the cytoplasm. Primarily associated with polyribosomes at the rough endoplasmic reticulum, and also detected at the plasma membrane. Under glycogenolytic conditions localizes to the nucleus. {ECO:0000250|UniProtKB:O95278}. SUBUNIT: Homodimer (PubMed:16971387). Interacts with PPP1R3B, PPP1R3C, HIRIP5, and EPM2AIP1 (By similarity). Binds glycogen and Lafora bodies. Interacts with NHLRC1/malin (via the NHL repeats) (By similarity). Forms a complex with NHLRC1/malin and HSP70 (PubMed:19036738). Interacts with PPP1R3D; in the presence of NHLC1/malin the interaction leads to ubiquitination and autophagic degradation of PPP1R3D (PubMed:23624058). Interacts (via the phosphatase domain) with MAPT/Tau; the interaction dephosphorylates MAPT (PubMed:19542233). Interacts with PRDM8 (By similarity). {ECO:0000250|UniProtKB:O95278, ECO:0000269|PubMed:16971387, ECO:0000269|PubMed:19036738, ECO:0000269|PubMed:19542233, ECO:0000269|PubMed:23624058}. DOMAIN: The CBM20 domain mediates binding to cytoplasmic glycogen and to Lafora polyglucosan bodies. {ECO:0000250|UniProtKB:O95278}. TISSUE SPECIFICITY: Detected in skeletal muscle and in brain (at protein level) (PubMed:24430976). Widely expressed. Higher levels of expression are found in heart, brain, liver, skeletal muscle and kidney (PubMed:10092504). {ECO:0000269|PubMed:10092504, ECO:0000269|PubMed:24430976}. +P54761 EPHB4_MOUSE Ephrin type-B receptor 4 (EC 2.7.10.1) (Developmental kinase 2) (mDK-2) (Hepatoma transmembrane kinase) (Tyrosine kinase MYK-1) 987 108,848 Active site (1); Binding site (1); Chain (1); Compositional bias (1); Disulfide bond (2); Domain (5); Glycosylation (3); Modified residue (4); Motif (1); Nucleotide binding (1); Sequence conflict (10); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 540 560 Helical. {ECO:0000255}. TOPO_DOM 16 539 Extracellular. {ECO:0000255}.; TOPO_DOM 561 987 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor tyrosine kinase which binds promiscuously transmembrane ephrin-B family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Together with its cognate ligand/functional ligand EFNB2 plays a central role in heart morphogenesis and angiogenesis through regulation of cell adhesion and cell migration. EPHB4-mediated forward signaling controls cellular repulsion and segregation form EFNB2-expressing cells. Plays also a role in postnatal blood vessel remodeling, morphogenesis and permeability and is thus important in the context of tumor angiogenesis. {ECO:0000269|PubMed:10518221}. PTM: Phosphorylated; autophosphorylation is stimulated by EFNB2. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Heterotetramer upon binding of the ligand. The heterotetramer is composed of an ephrin dimer and a receptor dimer. Oligomerization is probably required to induce biological responses (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in various organ systems, including lung, liver, kidney, intestine, muscle and heart (PubMed:7478528). Expressed in myogenic progenitor cells (PubMed:27446912). {ECO:0000269|PubMed:27446912, ECO:0000269|PubMed:7478528}. +Q9D9V2 EQTN_MOUSE Equatorin (Acrosome formation-associated factor) (MN9 antigen) 337 37,764 Alternative sequence (1); Chain (1); Glycosylation (1); Modified residue (1); Mutagenesis (5); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 184 204 Helical. {ECO:0000255}. TOPO_DOM 21 183 Lumenal. {ECO:0000305}.; TOPO_DOM 205 337 Cytoplasmic. {ECO:0000305}. FUNCTION: Acrosomal membrane-anchored protein involved in the process of fertilization and in acrosome biogenesis. {ECO:0000269|PubMed:16831425, ECO:0000269|PubMed:19285662, ECO:0000269|PubMed:9674989}. PTM: Highly N- and O-glycosylated; contains sialic acid. MN9 epitope is O-glycosylated. {ECO:0000269|PubMed:19605790}. SUBCELLULAR LOCATION: Isoform 1: Cytoplasmic vesicle, secretory vesicle, acrosome membrane; Single-pass type I membrane protein. Cytoplasmic vesicle, secretory vesicle, acrosome inner membrane; Single-pass type I membrane protein. Cytoplasmic vesicle, secretory vesicle, acrosome outer membrane; Single-pass type I membrane protein. Note=In the anterior acrosome region, enriched on the inner acrosomal membrane but minimal on the outer acrosomal membrane; in contrast in the posterior acrosome region enriched on both the inner and outer acrosomal membranes.; SUBCELLULAR LOCATION: Isoform 2: Nucleus. Cytoplasm. SUBUNIT: Interacts with SNAP25. {ECO:0000269|PubMed:19285662}. TISSUE SPECIFICITY: Sperm specific, including germ cells (at protein level). {ECO:0000269|PubMed:16831425, ECO:0000269|PubMed:19605790}. +Q62413 EPHA6_MOUSE Ephrin type-A receptor 6 (EC 2.7.10.1) (EPH homology kinase 2) (EHK-2) 1035 116,185 Active site (1); Beta strand (1); Binding site (1); Chain (1); Compositional bias (1); Domain (5); Glycosylation (3); Helix (6); Modified residue (4); Motif (1); Nucleotide binding (1); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 550 570 Helical. {ECO:0000255}. TOPO_DOM 23 549 Extracellular. {ECO:0000255}.; TOPO_DOM 571 1035 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor tyrosine kinase which binds promiscuously GPI-anchored ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Heterotetramer upon binding of the ligand. The heterotetramer is composed of an ephrin dimer and a receptor dimer. Oligomerization is probably required to induce biological responses (By similarity). Interacts (via SAM domain) with ANKS1A (via SAM domain) (PubMed:29749928). {ECO:0000250, ECO:0000269|PubMed:29749928}. +Q61521 EREG_MOUSE Proepiregulin [Cleaved into: Epiregulin (EPR)] 162 18,474 Chain (2); Compositional bias (1); Disulfide bond (3); Domain (1); Glycosylation (1); Propeptide (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 113 133 Helical. {ECO:0000255}. TOPO_DOM 53 112 Extracellular. {ECO:0000255}.; TOPO_DOM 134 162 Cytoplasmic. {ECO:0000255}. FUNCTION: Ligand of the EGF receptor/EGFR and ERBB4. Stimulates EGFR and ERBB4 tyrosine phosphorylation (By similarity). Contributes to inflammation, wound healing, tissue repair, and oocyte maturation by regulating angiogenesis and vascular remodeling and by stimulating cell proliferation (PubMed:24631357). {ECO:0000250|UniProtKB:O14944, ECO:0000303|PubMed:24631357}. SUBCELLULAR LOCATION: Epiregulin: Secreted, extracellular space {ECO:0000250|UniProtKB:O14944}.; SUBCELLULAR LOCATION: Proepiregulin: Cell membrane {ECO:0000250|UniProtKB:O14944}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:O14944}. SUBUNIT: Interacts with EGFR and ERBB4. {ECO:0000250|UniProtKB:O14944}. +Q9WUF2 EGR4_MOUSE Early growth response protein 4 (EGR-4) 478 49,554 Chain (1); Zinc finger (3) FUNCTION: Transcriptional regulator. Recognizes and binds to the DNA sequence 5'-GCGGGGGCG-3' (GSG). Activates the transcription of target genes whose products are required for mitogenesis and differentiation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. +Q91YE2 EGLN2_MOUSE Egl nine homolog 2 (EC 1.14.11.29) (Falkor) (Hypoxia-inducible factor prolyl hydroxylase 1) (HIF-PH1) (HIF-prolyl hydroxylase 1) (HPH-1) (Prolyl hydroxylase domain-containing protein 1) (PHD1) 419 45,109 Binding site (1); Chain (1); Domain (1); Frameshift (1); Metal binding (3); Modified residue (1); Motif (1); Region (1); Sequence conflict (3) FUNCTION: Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both HIF1A and HIF2A. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes. EGLN2 is involved in regulating hypoxia tolerance and apoptosis in cardiac and skeletal muscle. Also regulates susceptibility to normoxic oxidative neuronal death. Links oxygen sensing to cell cycle and primary cilia formation by hydroxylating the critical centrosome component CEP192 which promotes its ubiquitination and subsequent proteasomal degradation. Hydroxylates IKBKB, mediating NF-kappaB activation in hypoxic conditions. Target proteins are preferentially recognized via a LXXLAP motif. {ECO:0000269|PubMed:18176562, ECO:0000269|PubMed:19587290, ECO:0000269|PubMed:21083501}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12360397}. SUBUNIT: Interacts with E3 ligase SIAH2. Interacts with LIMD1, WTIP and AJUBA. {ECO:0000250|UniProtKB:Q96KS0}. DOMAIN: The Beta(2)beta(3) 'finger-like' loop domain is important for substrate (HIFs' CODD/NODD) selectivity. {ECO:0000250|UniProtKB:Q9GZT9}. TISSUE SPECIFICITY: Highly expressed in testis, expression was also detected in the heart brain, liver kidney and lung. Expression was lowest in spleen and skeletal muscle. Constitutively expressed during differentiation of C2C12 skeletal myocytes. {ECO:0000269|PubMed:12234095}. +Q69ZW3 EHBP1_MOUSE EH domain-binding protein 1 1231 139,104 Alternative sequence (1); Chain (1); Coiled coil (4); Compositional bias (2); Domain (3); Erroneous initiation (1); Modified residue (17); Motif (1); Sequence conflict (7) FUNCTION: May play a role in actin reorganization. Links clathrin-mediated endocytosis to the actin cytoskeleton. May act as Rab effector protein and play a role in vesicle trafficking (By similarity). Required for perinuclear sorting and insulin-regulated recycling of SLC2A4/GLUT4 in adipocytes. {ECO:0000250|UniProtKB:Q8NDI1, ECO:0000269|PubMed:15247266}. PTM: Prenylated (Probable). Farnelysation (predominant) and geranylgeranylation has been observed in vitro. {ECO:0000250|UniProtKB:Q8NDI1}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8NDI1}. Membrane {ECO:0000250|UniProtKB:Q8NDI1}. Endosome {ECO:0000250|UniProtKB:Q8NDI1}. Note=Mostly found in cytosol and plasma membrane. {ECO:0000250|UniProtKB:Q8NDI1}. SUBUNIT: Interacts with EHD1 (PubMed:15247266). Interacts with EHD2. Interacts with RAB8A, RAB10, RAB13 and RAB15 (in their GTP-bound forms); at least in case of RAB8A may bind 2 molecules of RAB8A simultaneously through a high and a low affinity binding site, respectively (By similarity). {ECO:0000250|UniProtKB:Q8NDI1, ECO:0000269|PubMed:15247266}. DOMAIN: The CAAX motif is a signal for prenylation and required for endosomal colocalization with Rab8 and Rab10. {ECO:0000250|UniProtKB:Q8NDI1}.; DOMAIN: The bivalent Mical/EHBP Rab binding (bMERB) domain, mediates binding to Rab8, Rab10, Rab10, Rab13 and Rab15 (in their GTP-bound form). {ECO:0000250|UniProtKB:Q8NDI1}. +Q60775 ELF1_MOUSE ETS-related transcription factor Elf-1 (E74-like factor 1) 612 66,221 Chain (1); Compositional bias (1); DNA binding (1); Modified residue (7) FUNCTION: Transcription factor that activates the LYN and BLK promoters. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Binds to the underphosphorylated form of RB. May interact with other transcription factors in order to regulate specific genes. Interacts with RUNX1. Interacts with SP1; the interaction is inhibited by glycosylation of SP1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Predominantly found in hematopoietic cells. Detected in other cell types such as fibroblasts. +Q9JHC9 ELF2_MOUSE ETS-related transcription factor Elf-2 (E74-like factor 2) (New ETS-related factor) 593 63,203 Alternative sequence (2); Chain (1); Cross-link (1); DNA binding (1); Modified residue (10); Sequence conflict (2) FUNCTION: Probably transcriptionally activates the LYN and BLK promoters and acts synergistically with RUNX1 to transactivate the BLK promoter. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with LIM domains of LMO2. Interacts via its N-terminal region with RUNX1. {ECO:0000250|UniProtKB:Q15723, ECO:0000269|PubMed:9001422}. TISSUE SPECIFICITY: Expressed in all tissues examined. Highest levels in thymocytes and bone marrow. {ECO:0000269|PubMed:9001422}. +P41158 ELK4_MOUSE ETS domain-containing protein Elk-4 (Serum response factor accessory protein 1) (SAP-1) (SRF accessory protein 1) 430 46,826 Chain (1); Cross-link (1); DNA binding (1); Sequence conflict (10) FUNCTION: Involved in both transcriptional activation and repression. Interaction with SIRT7 leads to recruitment and stabilization of SIRT7 at promoters, followed by deacetylation of histone H3 at 'Lys-18' (H3K18Ac) and subsequent transcription repression. Forms a ternary complex with the serum response factor (SRF). Requires DNA-bound SRF for ternary complex formation and makes extensive DNA contacts to the 5'side of SRF, but does not bind DNA autonomously (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with SIRT7. {ECO:0000250}. TISSUE SPECIFICITY: Lung and liver. +Q8VDK3 ELF5_MOUSE ETS-related transcription factor Elf-5 (E74-like factor 5) 253 29,873 Chain (1); DNA binding (1); Domain (1); Sequence conflict (2) FUNCTION: Transcriptionally activator that may play a role in regulating the later stages of keratinocytes terminal differentiation (By similarity). Binds to DNA sequences containing the consensus nucleotide core sequence GGA[AT]. Transcriptionally activates the TK promoter. {ECO:0000250, ECO:0000269|PubMed:16704374, ECO:0000269|PubMed:9840936}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00237}. DOMAIN: The PNT domain acts as a transcriptional activator. {ECO:0000269|PubMed:16704374}. TISSUE SPECIFICITY: Expressed in lung, kidney, stomach, brain, ovaries, tongue, bladder and mammary glands. {ECO:0000269|PubMed:9840936}. +Q8C8T7 ELFN1_MOUSE Protein ELFN1 (Extracellular leucine-rich repeat and fibronectin type-III domain-containing protein 1) (Protein phosphatase 1 regulatory subunit 28) 828 90,815 Chain (1); Compositional bias (2); Domain (2); Glycosylation (5); Modified residue (2); Repeat (5); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 419 439 Helical. {ECO:0000255}. TOPO_DOM 26 418 Extracellular. {ECO:0000255}.; TOPO_DOM 440 828 Cytoplasmic. {ECO:0000255}. FUNCTION: Postsynaptic protein that regulates circuit dynamics in the central nervous system by modulating the temporal dynamics of interneuron recruitment. Specifically present in excitatory synapses onto oriens-lacunosum molecular (OLM) interneurons and acts as a regulator of presynaptic release probability to direct the formation of highly facilitating pyramidal-OLM synapses. Inhibits phosphatase activity of protein phosphatase 1 (PP1) complexes. {ECO:0000269|PubMed:23042292}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Cell projection, dendrite {ECO:0000269|PubMed:23042292}. Note=Localizes to excitatory synapses onto somatostatin (Sst)-containing oriens-lacunosum moleculare (O-LM) interneurons. SUBUNIT: Interacts with PPP1CA. {ECO:0000250}. TISSUE SPECIFICITY: Selectively expressed in perialvear somatostatin (Sst)-containing interneurons. {ECO:0000269|PubMed:23042292}. +Q8CB77 ELOA1_MOUSE Elongin-A (EloA) (Elongin 110 kDa subunit) (RNA polymerase II transcription factor SIII subunit A1) (SIII p110) (Transcription elongation factor B polypeptide 3) 773 87,161 Chain (1); Domain (2); Modified residue (7); Region (2); Sequence conflict (9) FUNCTION: SIII, also known as elongin, is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. Subunit A is transcriptionally active and its transcription activity is strongly enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex). {ECO:0000250|UniProtKB:Q63187}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00649}. SUBUNIT: Heterotrimer of an A (ELOA, ELOA2 or ELOA3), ELOB and ELOC subunit. {ECO:0000250|UniProtKB:Q63187}. DOMAIN: The BC-box, which mediates binding to the elongin BC complex, has the consensus sequence [APST]-L-x(3)-C-x(3)-[AILV]. {ECO:0000250|UniProtKB:Q63187}. +Q3V1U8 ELMD1_MOUSE ELMO domain-containing protein 1 326 38,034 Chain (1); Domain (1); Erroneous initiation (1) FUNCTION: Acts as a GTPase-activating protein (GAP) toward guanine nucleotide exchange factors like ARL2, ARL3, ARF1 and ARF6, but not for GTPases outside the Arf family. {ECO:0000250}. +Q91YP6 ELMD3_MOUSE ELMO domain-containing protein 3 (RNA-binding motif and ELMO domain-containing protein 1) 381 42,659 Alternative sequence (2); Chain (1); Domain (1); Sequence conflict (1) FUNCTION: Acts as a GTPase-activating protein (GAP) for ARL2 with low specific activity. {ECO:0000250}. SUBCELLULAR LOCATION: Cell projection, stereocilium {ECO:0000269|PubMed:24039609}. Cell projection, kinocilium {ECO:0000269|PubMed:24039609}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:24039609}. Note=Also present in the cuticular plate of auditory hair cells. In the organ of Corti, in inner hair cells, expressed along the length of the stereocilia, but excluded from the very tip. Colocalizes with F-actin cytoskeleton. TISSUE SPECIFICITY: Both isoform 1 and isoform 2 are widely expressed. {ECO:0000269|PubMed:24039609}. +Q8BHI7 ELOV5_MOUSE Elongation of very long chain fatty acids protein 5 (EC 2.3.1.199) (3-keto acyl-CoA synthase Elovl5) (ELOVL fatty acid elongase 5) (ELOVL FA elongase 5) (Very long chain 3-ketoacyl-CoA synthase 5) (Very long chain 3-oxoacyl-CoA synthase 5) 299 35,332 Chain (1); Modified residue (1); Sequence conflict (4); Transmembrane (7) TRANSMEM 26 46 Helical. {ECO:0000255|HAMAP-Rule:MF_03205}.; TRANSMEM 64 84 Helical. {ECO:0000255|HAMAP-Rule:MF_03205}.; TRANSMEM 112 132 Helical. {ECO:0000255|HAMAP-Rule:MF_03205}.; TRANSMEM 139 158 Helical. {ECO:0000255|HAMAP-Rule:MF_03205}.; TRANSMEM 168 187 Helical. {ECO:0000255|HAMAP-Rule:MF_03205}.; TRANSMEM 205 225 Helical. {ECO:0000255|HAMAP-Rule:MF_03205}.; TRANSMEM 227 247 Helical. {ECO:0000255|HAMAP-Rule:MF_03205}. Lipid metabolism; polyunsaturated fatty acid biosynthesis. FUNCTION: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme that acts specifically toward polyunsaturated acyl-CoA with the higher activity toward C18:3(n-6) acyl-CoA. May participate in the production of monounsaturated and of polyunsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. {ECO:0000255|HAMAP-Rule:MF_03205}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03205}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03205}. Cell projection, dendrite {ECO:0000255|HAMAP-Rule:MF_03205}. Note=In Purkinje cells, the protein localizes to the soma and proximal portion of the dendritic tree. {ECO:0000255|HAMAP-Rule:MF_03205}. +Q8BHL5 ELMO2_MOUSE Engulfment and cell motility protein 2 (Protein ced-12 homolog A) 732 83,887 Alternative sequence (2); Chain (1); Domain (2); Modified residue (3); Motif (1); Sequence conflict (5) FUNCTION: Involved in cytoskeletal rearrangements required for phagocytosis of apoptotic cells and cell motility. Acts in association with DOCK1 and CRK. Was initially proposed to be required in complex with DOCK1 to activate Rac Rho small GTPases. May enhance the guanine nucleotide exchange factor (GEF) activity of DOCK1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96JJ3}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q96JJ3}. Membrane {ECO:0000250|UniProtKB:Q96JJ3}. SUBUNIT: Interacts directly with the SH3-domain of DOCK1 via its SH3-binding site (PubMed:25533347). Probably forms a heterotrimeric complex with DOCK1 and RAC1. Interacts with ARHGEF16, DOCK4 and EPHA2; mediates activation of RAC1 by EPHA2 (By similarity). Interacts with ADGRB3 (By similarity). Interacts with AUTS2; the interaction is direct (PubMed:25533347). {ECO:0000250|UniProtKB:Q96JJ3, ECO:0000269|PubMed:25533347}. +Q05BC3 EMAL1_MOUSE Echinoderm microtubule-associated protein-like 1 (EMAP-1) 814 89,680 Alternative sequence (2); Chain (1); Compositional bias (1); Mutagenesis (1); Region (1); Repeat (12); Sequence conflict (2) FUNCTION: Modulates the assembly and organization of the microtubule cytoskeleton, and probably plays a role in regulating the orientation of the mitotic spindle and the orientation of the plane of cell division. Required for normal proliferation of neuronal progenitor cells in the developing brain and for normal brain development. Does not affect neuron migration per se. {ECO:0000269|PubMed:24859200}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24859200}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:24859200}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:24859200}. Note=Detected in cytoplasmic punctae. Co-localizes with microtubules. Enriched in perinuclear regions during interphase and in the region of spindle microtubules during metaphase. Enriched at the midzone during telophase and cytokinesis. Detected at growth cones in neurons. {ECO:0000269|PubMed:24859200}. SUBUNIT: Binds unpolymerized tubulins via its WD repeat region (By similarity). Binds repolymerizing microtubules (PubMed:24859200). {ECO:0000250|UniProtKB:O00423, ECO:0000269|PubMed:24859200}. DOMAIN: Contains a tandem atypical propeller in EMLs (TAPE) domain. The N-terminal beta-propeller is formed by canonical WD repeats; in contrast, the second beta-propeller contains one blade that is formed by discontinuous parts of the polypeptide chain. {ECO:0000250|UniProtKB:O00423}. TISSUE SPECIFICITY: Detected in adult brain cortex, hippocampus and thalamus. {ECO:0000269|PubMed:24859200}. DISEASE: Note=Defects in Eml1 are the cause of the neuronal heterotopia observed in HeCo mice. These mice display heterotopic neurons in the rostro-medial part of the neocortex, together with epilepsy and subtle learning deficits in adults. At 17 dpc both Tbr1(+) and Cux1(+) neurons contribute to the heterotopia. Three days after birth, most Tbr1(+) have reached their final destination, but many Cux1(+) neurons remain in the heterotopia and fail to reach cortical layers II to IV, contrary to the situation in wild-type. Besides, progenitor cells continue to proliferate, resulting in large numbers of abnormally positioned actively proliferating cells during both early and late stages of corticogenesis. In HeCo mice, insertion of a retrotransposon into Eml1 leads to the absence of full-length Eml1 transcripts. +Q8BK75 ELP6_MOUSE Elongator complex protein 6 (Protein TMEM103) 266 29,327 Alternative sequence (1); Chain (1) FUNCTION: Acts as subunit of the RNA polymerase II elongator complex, which is a histone acetyltransferase component of the RNA polymerase II (Pol II) holoenzyme and is involved in transcriptional elongation. Elongator may play a role in chromatin remodeling and is involved in acetylation of histones H3 and probably H4. Involved in cell migration. {ECO:0000269|PubMed:22854966}. SUBUNIT: Component of the RNA polymerase II elongator complex (Elongator), which consists of ELP1, STIP1/ELP2, ELP3, ELP4, ELP5 and ELP6. {ECO:0000250}. +Q8BQM8 EMAL5_MOUSE Echinoderm microtubule-associated protein-like 5 (EMAP-5) 1977 220,106 Chain (1); Erroneous initiation (2); Repeat (29); Sequence conflict (2) FUNCTION: May modify the assembly dynamics of microtubules, such that microtubules are slightly longer, but more dynamic. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. +Q920L5 ELOV6_MOUSE Elongation of very long chain fatty acids protein 6 (EC 2.3.1.199) (3-keto acyl-CoA synthase Elovl6) (ELOVL fatty acid elongase 6) (ELOVL FA elongase 6) (Fatty acyl-CoA elongase) (Long chain fatty acid elongase) (Myelin-associated SUR4 protein) (Very long chain 3-ketoacyl-CoA synthase 6) (Very long chain 3-oxoacyl-CoA synthase 6) 267 31,610 Chain (1); Glycosylation (1); Sequence conflict (1); Transmembrane (7) TRANSMEM 34 51 Helical. {ECO:0000255|HAMAP-Rule:MF_03206}.; TRANSMEM 70 90 Helical. {ECO:0000255|HAMAP-Rule:MF_03206}.; TRANSMEM 111 131 Helical. {ECO:0000255|HAMAP-Rule:MF_03206}.; TRANSMEM 136 156 Helical. {ECO:0000255|HAMAP-Rule:MF_03206}.; TRANSMEM 159 179 Helical. {ECO:0000255|HAMAP-Rule:MF_03206}.; TRANSMEM 197 217 Helical. {ECO:0000255|HAMAP-Rule:MF_03206}.; TRANSMEM 234 254 Helical. {ECO:0000255|HAMAP-Rule:MF_03206}. Lipid metabolism; fatty acid biosynthesis. FUNCTION: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme that elongates fatty acids with 12, 14 and 16 carbons with higher activity toward C16:0 acyl-CoAs. Catalyzes the synthesis of unsaturated C16 long chain fatty acids and, to a lesser extent, C18:0 and those with low desaturation degree. May participate in the production of saturated and monounsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. {ECO:0000255|HAMAP-Rule:MF_03206, ECO:0000269|PubMed:11567032, ECO:0000269|PubMed:12032166}. PTM: N-Glycosylated. {ECO:0000255|HAMAP-Rule:MF_03206}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03206, ECO:0000269|PubMed:11567032, ECO:0000269|PubMed:12084938}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03206}. TISSUE SPECIFICITY: Highly expressed in adrenal gland, liver, white adipose tissue (WAT), adult and fetal brain, cerebellum, spinal cord, testis, skin and peripheral nerve; where lipogenesis and steroidogenesis are active. Weakly expressed in kidney, heart, skeletal muscle, lung, and spleen. {ECO:0000269|PubMed:11567032, ECO:0000269|PubMed:12032166, ECO:0000269|PubMed:12084938}. +Q9CZX9 EMC4_MOUSE ER membrane protein complex subunit 4 (Transmembrane protein 85) 183 20,117 Chain (1); Initiator methionine (1); Modified residue (2); Sequence conflict (1); Transmembrane (2) TRANSMEM 84 104 Helical. {ECO:0000255}.; TRANSMEM 129 149 Helical. {ECO:0000255}. FUNCTION: May mediate anti-apoptotic activity. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Component of the ER membrane protein complex (EMC). {ECO:0000250}. +Q9CRD2 EMC2_MOUSE ER membrane protein complex subunit 2 (Tetratricopeptide repeat protein 35) (TPR repeat protein 35) 297 34,935 Chain (1); Initiator methionine (1); Modified residue (2); Repeat (3) SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11593002}. Cytoplasm {ECO:0000250}. SUBUNIT: Component of the ER membrane protein complex (EMC). {ECO:0000250}. +Q56A04 EME2_MOUSE Probable crossover junction endonuclease EME2 (EC 3.1.22.-) 373 41,083 Chain (1) FUNCTION: Interacts with MUS81 to form a DNA structure-specific endonuclease which cleaves substrates such as 3'-flap structures. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Interacts with MUS81. {ECO:0000250}. +Q7TT37 ELP1_MOUSE Elongator complex protein 1 (ELP1) (IkappaB kinase complex-associated protein) (IKK complex-associated protein) 1333 149,584 Chain (1); Frameshift (2); Modified residue (3); Sequence conflict (18) FUNCTION: May act as a scaffold protein that may assemble active IKK-MAP3K14 complexes (IKKA, IKKB and MAP3K14/NIK). {ECO:0000250}.; FUNCTION: Acts as subunit of the RNA polymerase II elongator complex, which is a histone acetyltransferase component of the RNA polymerase II (Pol II) holoenzyme and is involved in transcriptional elongation. Elongator may play a role in chromatin remodeling and is involved in acetylation of histones H3 and probably H4. Involved in cell migration. Involved in neurogenesis (PubMed:19185337). Regulates the migration and branching of projection neurons in the developing cerebral cortex, through a process depending on alpha-tubulin acetylation (PubMed:19185337). {ECO:0000269|PubMed:19185337, ECO:0000269|PubMed:22854966}. PTM: Phosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19185337}. Nucleus {ECO:0000250|UniProtKB:O95163}. SUBUNIT: Interacts preferentially with MAP3K14/NIK followed by IKK-alpha and IKK-beta. Component of the RNA polymerase II elongator complex (Elongator), which consists of ELP1, STIP1/ELP2, ELP3, ELP4, ELP5 and ELP6. Elongator associates with the C-terminal domain (CTD) of Pol II largest subunit. Interacts with ELP3 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed with highest levels in brain. {ECO:0000269|PubMed:11747609}. +Q91VF5 EMID1_MOUSE EMI domain-containing protein 1 (Emilin and multimerin domain-containing protein 1) (Emu1) 444 45,634 Alternative sequence (1); Chain (1); Disulfide bond (3); Domain (2); Glycosylation (2); Signal peptide (1) SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SUBUNIT: Homo- or heteromers. +Q9DB10 EMRE_MOUSE Essential MCU regulator, mitochondrial (Single-pass membrane protein with aspartate-rich tail 1, mitochondrial) 107 11,542 Chain (1); Compositional bias (1); Frameshift (1); Motif (1); Mutagenesis (2); Topological domain (2); Transit peptide (1); Transmembrane (1) TRANSMEM 65 84 Helical. {ECO:0000255}. TOPO_DOM 48 64 Mitochondrial matrix. {ECO:0000305|PubMed:27001609}.; TOPO_DOM 85 107 Mitochondrial intermembrane. {ECO:0000305|PubMed:27001609}. FUNCTION: Essential regulatory subunit of the mitochondrial calcium uniporter complex (uniplex), a complex that mediates calcium uptake into mitochondria (PubMed:27001609). Required to bridge the calcium-sensing proteins MICU1 and MICU2 with the calcium-conducting subunit MCU. Plays a central role in regulating the uniplex complex response to intracellular calcium signaling. Acts by mediating activation of MCU and retention of MICU1 to the MCU pore, in order to ensure tight regulation of the uniplex complex and appropriate responses to intracellular calcium signaling (By similarity). {ECO:0000250|UniProtKB:Q9H4I9, ECO:0000269|PubMed:27001609}. PTM: Undergoes proteolytic degradation in neurons: degraded by AFG3L2 before SMDT1/EMRE assembly with the uniporter complex, limiting the availability of SMDT1/EMRE for MCU assembly and promoting efficient assembly of gatekeeper subunits with MCU. {ECO:0000250|UniProtKB:Q9H4I9}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:27001609}; Single-pass membrane protein {ECO:0000269|PubMed:27001609}. Note=MAIP1 is required to assist sorting of EMRE/SMDT1 into mitochondrion by protecting EMRE/SMDT1 against protein degradation by YME1L1, thereby ensuring SMDT1/EMRE maturation by the mitochondrial processing peptidase (PMPCA and PMPCB). {ECO:0000250|UniProtKB:Q9H4I9}. SUBUNIT: Component of the uniplex complex, composed of MCU, MCUB, MICU1, MICU2 and EMRE/SMDT1 (By similarity). Interacts (via the transmembrane region) with MCU (via the first transmembrane region); the interaction is direct (PubMed:27001609). Interacts (via the poly-Asp region) with MICU1 (via polybasic region); the interaction is direct (By similarity). Interacts (via its C-terminal poly-Asp tail) with MCUR1; the interaction is direct (By similarity). Unprocessed form interacts (via transit peptide) with MAIP1 (By similarity). {ECO:0000250|UniProtKB:Q9H4I9, ECO:0000269|PubMed:27001609}. DOMAIN: The GXXXX[G/A/S] motif at the C-terminal part of the transmembrane region mediates interaction with MCU and is required to activate the calcium-conducting pore in the uniporter complex. {ECO:0000250|UniProtKB:Q9H4I9}.; DOMAIN: The poly-Asp region at the C-terminus mediates interaction with the polybasic region of MICU1. {ECO:0000250|UniProtKB:Q9H4I9}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:24231807}. +Q8BMB0 EMSY_MOUSE BRCA2-interacting transcriptional repressor EMSY 1264 135,291 Alternative sequence (3); Chain (1); Compositional bias (6); Domain (1); Erroneous initiation (1); Frameshift (1); Glycosylation (7); Modified residue (7); Region (2); Sequence conflict (1) FUNCTION: Regulator which is able to repress transcription, possibly via its interaction with a multiprotein chromatin remodeling complex that modifies the chromatin. Its interaction with BRCA2 suggests that it may play a central role in the DNA repair function of BRCA2 (By similarity). As part of a H3-specific methyltransferase complex may mediate ligand-dependent transcriptional activation by nuclear hormone receptors (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14651845}. Note=Localizes to DNA damage markers in irradiated cells, suggesting that it participates in DNA repair process. SUBUNIT: Homodimer. Interacts with the transactivation domain of BRCA2. Interacts with the chromoshadow domain of CBX1 and with HCFC1. Interacts with the viral transactivator protein VP16. Part of a complex composed at least of ASCL2, EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; this complex may have a histone H3-specific methyltransferase activity. Interacts with ZMYND11. {ECO:0000269|PubMed:14651845}. +Q9DC51 GNAI3_MOUSE Guanine nucleotide-binding protein G(k) subunit alpha (G(i) alpha-3) 354 40,538 Binding site (1); Chain (1); Initiator methionine (1); Lipidation (2); Metal binding (2); Nucleotide binding (5) FUNCTION: Heterotrimeric guanine nucleotide-binding proteins (G proteins) function as transducers downstream of G protein-coupled receptors (GPCRs) in numerous signaling cascades. The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state. Signaling by an activated GPCR promotes GDP release and GTP binding. The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal. Both GDP release and GTP hydrolysis are modulated by numerous regulatory proteins. Signaling is mediated via effector proteins, such as adenylate cyclase. Inhibits adenylate cyclase activity, leading to decreased intracellular cAMP levels. Stimulates the activity of receptor-regulated K(+) channels. The active GTP-bound form prevents the association of RGS14 with centrosomes and is required for the translocation of RGS14 from the cytoplasm to the plasma membrane. May play a role in cell division. {ECO:0000250|UniProtKB:P08754}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P08754}. Cell membrane {ECO:0000250|UniProtKB:P08754}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P08754}. Membrane {ECO:0000250|UniProtKB:P08754}; Lipid-anchor {ECO:0000250|UniProtKB:P08754}. Note=Localizes in the centrosomes of interphase and mitotic cells. Detected at the cleavage furrow and/or the midbody. {ECO:0000250|UniProtKB:P08754}. SUBUNIT: Heterotrimeric G proteins are composed of 3 units; alpha, beta and gamma. The alpha subunit contains the guanine nucleotide binding site. GTP binding causes dissociation of the heterotrimer, liberating the individual subunits so that they can interact with downstream effector proteins (By similarity). Interacts with GPSM1 (PubMed:16009138). Interacts (GDP-bound form) with GPSM2 (via GoLoco domains). Does not interact with RGS2. Interacts with RGS8 and RGS10; this strongly enhances the intrinsic GTPase activity. Interacts with RGS16; this strongly enhances the intrinsic GTPase activity (By similarity). Interacts with RGS12 (By similarity). Interacts (via active GTP- or inactive GDP-bound form) with RGS14 (By similarity). {ECO:0000250|UniProtKB:P08753, ECO:0000250|UniProtKB:P08754, ECO:0000269|PubMed:16009138}. +O88958 GNPI1_MOUSE Glucosamine-6-phosphate isomerase 1 (EC 3.5.99.6) (Glucosamine-6-phosphate deaminase 1) (GNPDA 1) (GlcN6P deaminase 1) (Oscillin) 289 32,549 Active site (4); Chain (1); Modified residue (1); Sequence conflict (3) FUNCTION: Seems to trigger calcium oscillations in mammalian eggs. These oscillations serve as the essential trigger for egg activation and early development of the embryo (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10481053}. SUBUNIT: Homohexamer. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. Detected in brain, liver, kidney, muscle, ovary, testis, spermatids and spermatozoa. In spermatids, located close to the developing acrosome vesicle. In spermatozoa, found close to the acrosomal region. {ECO:0000269|PubMed:10481053}. +Q6S5C2 GNPTG_MOUSE N-acetylglucosamine-1-phosphotransferase subunit gamma (GlcNAc-1-phosphotransferase subunit gamma) (M6PR domain-containing protein 1) (UDP-N-acetylglucosamine-1-phosphotransferase subunit gamma) 307 34,169 Alternative sequence (1); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (2); Mutagenesis (7); Signal peptide (1) FUNCTION: Non-catalytic subunit of the N-acetylglucosamine-1-phosphotransferase complex, an enzyme that catalyzes the formation of mannose 6-phosphate (M6P) markers on high mannose type oligosaccharides in the Golgi apparatus. Binds and presents the high mannose glycans of the acceptor to the catalytic alpha and beta subunits (GNPTAB). Enhances the rate of N-acetylglucosamine-1-phosphate transfer to the oligosaccharides of acid hydrolase acceptors. {ECO:0000269|PubMed:15716021}. PTM: Cys-245 mediates the formation of the interchain disulfide bond for formation of the homofimer. Cys-142, Cys-157 and Cys-169 are involved in intramolecular disulfide bonds formation (PubMed:21173149). {ECO:0000269|PubMed:21173149}. SUBCELLULAR LOCATION: Secreted. Golgi apparatus. SUBUNIT: Homodimer; disulfide-linked. Hexamer of two alpha (GNPTAB), two beta (GNPTAB) and two gamma (GNPTG) subunits; disulfide-linked. The alpha and/or the beta subunits of the enzyme constitute the catalytic subunits (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. Highly expressed in the liver, intestine, brain, thymus, testis and ovary. {ECO:0000269|PubMed:15716021}. +Q8BFR4 GNS_MOUSE N-acetylglucosamine-6-sulfatase (EC 3.1.6.14) (Glucosamine-6-sulfatase) (G6S) 544 61,175 Active site (1); Chain (1); Glycosylation (12); Metal binding (5); Modified residue (2); Sequence conflict (3); Signal peptide (1) PTM: The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity. {ECO:0000250}. SUBCELLULAR LOCATION: Lysosome {ECO:0000250}. +P55937 GOGA3_MOUSE Golgin subfamily A member 3 (Golgin-160) (Male-enhanced antigen 2) (MEA-2) 1487 167,220 Alternative sequence (1); Chain (1); Coiled coil (1); Compositional bias (4); Modified residue (10); Region (2); Sequence conflict (9) FUNCTION: Plays an important role in spermatogenesis and/or testis development. Probably identical with the serologically detectable male antigen (SDM). Probably involved in maintaining Golgi structure. {ECO:0000269|PubMed:11835574}. PTM: Cleaved by caspases in apoptotic cells. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus, Golgi stack membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. SUBUNIT: Homodimer. Interacts with GOLGA7. Interacts with GOPC (By similarity). {ECO:0000250}. DOMAIN: Extended rod-like protein with coiled-coil domains. TISSUE SPECIFICITY: Highly expressed in testis. Transcripts can be found in spermatids during spermatogenesis. No expression in Leydig cells, spermatogonia or spermatocytes. Detected at low levels in all tissues. +Q8BGN3 ENPP6_MOUSE Ectonucleotide pyrophosphatase/phosphodiesterase family member 6 (E-NPP 6) (NPP-6) (EC 3.1.4.-) (EC 3.1.4.38) (Choline-specific glycerophosphodiester phosphodiesterase) (Glycerophosphocholine cholinephosphodiesterase) (GPC-Cpde) 440 50,618 Active site (1); Beta strand (17); Chain (1); Disulfide bond (2); Glycosylation (4); Helix (21); Lipidation (1); Modified residue (1); Propeptide (1); Sequence conflict (1); Signal peptide (1); Turn (7) FUNCTION: Choline-specific glycerophosphodiester phosphodiesterase. The preferred substrate may be lysosphingomyelin (By similarity). Hydrolyzes lysophosphatidylcholine (LPC) to form monoacylglycerol and phosphorylcholine but not lysophosphatidic acid, showing it has a lysophospholipase C activity. Has a preference for LPC with short (12:0 and 14:0) or polyunsaturated (18:2 and 20:4) fatty acids. Also hydrolyzes glycerophosphorylcholine and sphingosylphosphorylcholine efficiently. Hydrolyzes the classical substrate for phospholipase C, p-nitrophenyl phosphorylcholine in vitro, while it does not hydrolyze the classical nucleotide phosphodiesterase substrate, p-nitrophenyl thymidine 5'-monophosphate. Does not hydrolyze diacyl phospholipids such as phosphatidylethanolamine, phosphatidylinositol, phosphatidylserine, phosphatidylglycerol and phosphatidic acid (By similarity). {ECO:0000250, ECO:0000269|PubMed:15788404}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}. TISSUE SPECIFICITY: Predominantly expressed in kidney with a lesser expression in brain and heart. {ECO:0000269|PubMed:15788404}. +Q8BXA1 GOLI4_MOUSE Golgi integral membrane protein 4 (Decapacitation factor 10) (Golgi phosphoprotein 4) 655 76,785 Chain (1); Coiled coil (1); Compositional bias (2); Glycosylation (1); Initiator methionine (1); Lipidation (1); Modified residue (5); Region (3); Topological domain (2); Transmembrane (1) TRANSMEM 13 33 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 2 12 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 34 655 Lumenal. {ECO:0000255}. FUNCTION: Plays a role in endosome to Golgi protein trafficking; mediates protein transport along the late endosome-bypass pathway from the early endosome to the Golgi. {ECO:0000250}. PTM: Phosphorylated by c-AMP-dependent kinases most probably in its lumenal part. {ECO:0000250}.; PTM: O-glycosylated; modified by sialic acid residues. {ECO:0000250}.; PTM: N-glycosylated; N-glycans are of the complex type and modified by sialic acid residues. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Endosome membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Membrane {ECO:0000250|UniProtKB:O00461}; Lipid-anchor {ECO:0000250|UniProtKB:O00461}. Note=Localizes to cis and medial Golgi cisternae. Probably cycles between early Golgi and distal compartments like endosome (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed by spermatozoa (at protein level). {ECO:0000269|PubMed:16221991}. +Q8VEM1 GOLI_MOUSE E3 ubiquitin-protein ligase RNF130 (EC 2.3.2.27) (G1-related zinc finger protein) (Goliath homolog) (RING finger protein 130) (RING-type E3 ubiquitin transferase RNF130) 419 46,376 Chain (1); Domain (1); Glycosylation (6); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1); Zinc finger (1) TRANSMEM 195 217 Helical. {ECO:0000255}. TOPO_DOM 28 194 Extracellular. {ECO:0000255}.; TOPO_DOM 218 419 Cytoplasmic. {ECO:0000255}. Protein modification; protein ubiquitination. FUNCTION: Acts as an E3 ubiquitin-protein ligase (By similarity). May have a role during the programmed cell death of hematopoietic cells. {ECO:0000250, ECO:0000269|PubMed:10806348}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasm {ECO:0000250|UniProtKB:Q86XS8}. TISSUE SPECIFICITY: Expression is highest in liver, with lesser amounts in the lung, spleen, brain, heart, kidney and testis. {ECO:0000269|PubMed:10806348}. +Q91XA2 GOLM1_MOUSE Golgi membrane protein 1 (Golgi membrane protein GP73) (Golgi phosphoprotein 2) 393 44,326 Chain (1); Coiled coil (1); Glycosylation (3); Modified residue (2); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 13 35 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 12 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 36 393 Lumenal. {ECO:0000255}. FUNCTION: Unknown. Cellular response protein to viral infection (By similarity). {ECO:0000250}. PTM: Phosphorylation sites are present in the extracellular medium. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Early Golgi. Cycles via the cell surface and endosomes upon lumenal pH disruption (By similarity). {ECO:0000250}. SUBUNIT: Interacts with DYM. {ECO:0000250}. +Q8K0L2 ENTP8_MOUSE Ectonucleoside triphosphate diphosphohydrolase 8 (E-NTPDase 8) (NTPDase 8) (NTPDase8) (EC 3.6.1.5) 497 54,650 Active site (1); Alternative sequence (2); Chain (1); Disulfide bond (4); Glycosylation (2); Sequence conflict (1); Topological domain (3); Transmembrane (2) TRANSMEM 9 29 Helical. {ECO:0000255}.; TRANSMEM 474 494 Helical. {ECO:0000255}. TOPO_DOM 1 8 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 30 473 Extracellular. {ECO:0000255}.; TOPO_DOM 495 497 Cytoplasmic. {ECO:0000255}. FUNCTION: Canalicular ectonucleoside NTPDase responsible for the main hepatic NTPDase activity. Ectonucleoside NTPDases catalyze the hydrolysis of gamma- and beta-phosphate residues of nucleotides, playing a central role in concentration of extracellular nucleotides. Has activity toward ATP, ADP, UTP and UDP, but not toward AMP. {ECO:0000269|PubMed:15122917}. PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. DOMAIN: The transmembranous domains are involved in regulation of enzyme activity. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in liver, jejunum and kidney. {ECO:0000269|PubMed:15122917}. +A2AIW0 ENTR1_MOUSE Endosome-associated-trafficking regulator 1 (Serologically defined colon cancer antigen 3) 432 48,025 Alternative sequence (6); Chain (1); Coiled coil (2); Erroneous initiation (1); Frameshift (1); Modified residue (5); Region (1); Sequence conflict (4) FUNCTION: May be involved in modulation of TNF response. May be involved in presentation of TNFRSF1A on the cell surface (PubMed:16332174). Involved in the endosome-to-plasma membrane trafficking and recycling of SNX27-retromer-dependent cargo proteins, such as GLUT1. Involved in the regulation of cytokinesis; the function may involve PTPN13 and GIT1 (By similarity). {ECO:0000250|UniProtKB:Q96C92, ECO:0000269|PubMed:16332174}.; FUNCTION: Endosome-associated protein that plays a role in membrane receptor sorting, cytokinesis and ciliogenesis. Involved in the endosome-to-plasma membrane trafficking and recycling of SNX27-retromer-dependent cargo proteins, such as GLUT1. Involved in the regulation of cytokinesis; the function may involve PTPN13 and GIT1. Plays a role in the formation of cilia. Involved in cargo protein localization, such as PKD2, at primary cilia (By similarity). Involved in the presentation of the tumor necrosis factor (TNF) receptor TNFRSF1A on the cell surface, and hence in the modulation of the TNF-induced apoptosis (PubMed:16332174). {ECO:0000250|UniProtKB:Q96C92, ECO:0000269|PubMed:16332174}. PTM: Phosphorylated. {ECO:0000250|UniProtKB:Q96C92}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16332174}. Early endosome {ECO:0000250|UniProtKB:Q96C92}. Endosome {ECO:0000250|UniProtKB:Q96C92}. Recycling endosome {ECO:0000250|UniProtKB:Q96C92}. Midbody {ECO:0000250|UniProtKB:Q96C92}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q96C92}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q96C92}. Note=Colocalizes in a WASHC2-dependent manner with the retromer CSC complex at endosomes. During cytokinesis colocalized with PTPN13 at the midbody. Colocalizes with IFT88 and gamma-tubulin at the basal body of primary cilia. Colocalizes with IFT88 and pericentrin at the centrosome. {ECO:0000250|UniProtKB:Q96C92}. SUBUNIT: Found in a complex with ENTR1, PTPN13 and GIT1. Interacts with PTPN13 (via the FERM domain). Interacts (via N-terminus) with GIT1 (via N- and C-terminus); this interaction is direct. Interacts with NOD2. Interacts (via N-terminus) with IFT88. Interacts with VPS35. {ECO:0000250|UniProtKB:Q96C92}. DOMAIN: Tne N-terminal domain is necessary and sufficient for basal body localization and ciliogenesis. {ECO:0000250|UniProtKB:Q96C92}. +P13562 GON1_MOUSE Progonadoliberin-1 (Progonadoliberin I) [Cleaved into: Gonadoliberin-1 (Gonadoliberin I) (Gonadotropin-releasing hormone I) (GnRH-I) (Luliberin I) (Luteinizing hormone-releasing hormone I) (LH-RH I); Prolactin release-inhibiting factor 1 (Prolactin release-inhibiting factor I)] 90 10,337 Chain (1); Modified residue (2); Peptide (2); Signal peptide (1); Site (1) FUNCTION: Stimulates the secretion of gonadotropins; it stimulates the secretion of both luteinizing and follicle-stimulating hormones. SUBCELLULAR LOCATION: Secreted. +P0C8B4 GON7_MOUSE EKC/KEOPS complex subunit GON7 98 10,346 Chain (1); Modified residue (1) FUNCTION: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. GON7 likely plays a supporting role to the catalytic subunit OSGEP in the complex. {ECO:0000250|UniProtKB:P46984, ECO:0000250|UniProtKB:Q9BXV9}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BXV9}. SUBUNIT: Component of the EKC/KEOPS complex composed of at least GON7, TP53RK, TPRKB, OSGEP and LAGE3; the whole complex dimerizes. {ECO:0000250|UniProtKB:Q9BXV9}. +Q8BH60 GOPC_MOUSE Golgi-associated PDZ and coiled-coil motif-containing protein (PDZ protein interacting specifically with TC10) (PIST) 463 50,662 Alternative sequence (1); Chain (1); Coiled coil (1); Domain (1); Initiator methionine (1); Modified residue (3) FUNCTION: Plays a role in intracellular protein trafficking and degradation. May regulate CFTR chloride currents and acid-induced ASIC3 currents by modulating cell surface expression of both channels. May also regulate the intracellular trafficking of the ADR1B receptor. May play a role in autophagy. Overexpression results in CFTR intracellular retention and degradation in the lysosomes. {ECO:0000269|PubMed:12149515, ECO:0000269|PubMed:12372286, ECO:0000269|PubMed:15317815}. SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein. Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein. Cell junction, synapse. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density. Cell projection, dendrite. Note=Enriched in synaptosomal and postsynaptic densities (PSD) fractions. Expressed in cell bodies and dendrites of Purkinje cells. Localized at the trans-Golgi network (TGN) of spermatids and the medulla of round spermatides. SUBUNIT: Homooligomer. Interacts with NLGN1, STX6 and GOLGA3 (By similarity). Interacts with ASIC3, RHOQ, FZD5, FZD8, GRID2, BECN1, CSPG5, CFTR and CLCN3. May interact with CACNG2. {ECO:0000250, ECO:0000269|PubMed:11162552, ECO:0000269|PubMed:11520064, ECO:0000269|PubMed:12372286, ECO:0000269|PubMed:12471024, ECO:0000269|PubMed:12885772, ECO:0000269|PubMed:15136571, ECO:0000269|PubMed:15317815}. DOMAIN: The coiled-coil region probably mediates targeting to the Golgi, oligomerization and interaction with RHOQ. May also mediates association to membranes and interactions with GOLGA3 and STX6 (By similarity). {ECO:0000250}.; DOMAIN: The PDZ domain mediates interaction with ADRB1 (By similarity). Mediates also interactions with FZD5, FZD8, ASIC3, GRID2, CFTR, CLCN3. {ECO:0000250, ECO:0000269|PubMed:11520064, ECO:0000269|PubMed:12372286, ECO:0000269|PubMed:12471024}. TISSUE SPECIFICITY: Ubiquitously expressed (at protein level). Expressed in dorsal root glanglion (DRG), spinal chord and brain. Isoform 1 is preferentially expressed in whole brain (at protein level) and cerebellum. Expressed in spermatocytes and spermatides but not in Sertoli cells and spermatogonia. {ECO:0000269|PubMed:11384996, ECO:0000269|PubMed:12149515, ECO:0000269|PubMed:12372286, ECO:0000269|PubMed:15317815}. +Q8BRM2 GORAB_MOUSE RAB6-interacting golgin (N-terminal kinase-like-binding protein 1) (NTKL-BP1) (NTKL-binding protein 1) (mNTKL-BP1) (SCY1-like 1-binding protein 1) (SCYL1-BP1) (SCYL1-binding protein 1) 368 41,487 Alternative sequence (1); Chain (1); Coiled coil (1); Region (1) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12783284}. Golgi apparatus {ECO:0000269|PubMed:18997784}. SUBUNIT: Interacts with RCHY1 (By similarity). Interacts with SCYL1 and RAB6A/RAB6. {ECO:0000250, ECO:0000269|PubMed:12783284, ECO:0000269|PubMed:18997784}. TISSUE SPECIFICITY: Expressed in small intestine, kidney, skeletal muscle, lung, spleen, brain and heart. High expression is observed in osteoblasts and skin; also expressed in osteoclasts albeit at lower levels. {ECO:0000269|PubMed:12783284, ECO:0000269|PubMed:18997784}. +Q91X51 GORS1_MOUSE Golgi reassembly-stacking protein 1 (Golgi peripheral membrane protein p65) (Golgi reassembly-stacking protein of 65 kDa) (GRASP65) 446 46,882 Chain (1); Compositional bias (3); Domain (2); Erroneous initiation (1); Initiator methionine (1); Lipidation (1); Metal binding (3); Modified residue (6); Region (2) FUNCTION: Plays an important role in assembly and membrane stacking of the Golgi cisternae, and in the reassembly of Golgi stacks after breakdown during mitosis. Key structural protein required for the maintenance of the Golgi apparatus integrity: its caspase-mediated cleavage is required for fragmentation of the Golgi during apoptosis (By similarity). Also mediates, via its interaction with GOLGA2/GM130, the docking of transport vesicles with the Golgi membranes (By similarity). Mediates ER stress-induced unconventional (ER/Golgi-independent) trafficking of core-glycosylated CFTR to cell membrane (By similarity). {ECO:0000250|UniProtKB:O35254, ECO:0000250|UniProtKB:Q9BQQ3}. PTM: Phosphorylated by CDC2/B1 and PLK kinases during mitosis. Phosphorylation cycle correlates with the cisternal stacking cycle. Phosphorylation of the homodimer prevents the association of dimers into higher-order oligomers, leading to cisternal unstacking. {ECO:0000250|UniProtKB:O35254}.; PTM: Target for caspase-3 cleavage during apoptosis. The cleavage contributes to Golgi fragmentation and occurs very early in the execution phase of apoptosis. {ECO:0000250|UniProtKB:O35254}.; PTM: Myristoylated. {ECO:0000250|UniProtKB:O35254}. SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane {ECO:0000250|UniProtKB:O35254}; Peripheral membrane protein {ECO:0000250|UniProtKB:O35254}; Cytoplasmic side {ECO:0000250|UniProtKB:O35254}. SUBUNIT: Homodimer. Forms higher-order oligomers under interphase but not mitotic conditions. Dimers of the protein on one membrane might be able to interact with dimers on another and so stack cisternae. Interacts with the C-terminus of GOLGA2/GM130 under both mitotic and non-mitotic conditions. The interaction is critical for the correct targeting of both proteins to the cis-Golgi. Interacts with TMED2 and TMED3. {ECO:0000250, ECO:0000250|UniProtKB:O35254}. +Q99JX3 GORS2_MOUSE Golgi reassembly-stacking protein 2 (GRS2) (Golgi reassembly-stacking protein of 55 kDa) (GRASP55) 451 47,038 Alternative sequence (1); Beta strand (15); Chain (1); Compositional bias (1); Domain (2); Helix (6); Initiator methionine (1); Lipidation (1); Modified residue (12); Mutagenesis (2); Region (2); Sequence conflict (2); Turn (6) FUNCTION: Plays a role in assembly and membrane stacking of the Golgi cisternae, and in the process by which Golgi stacks reform after breakdown during mitosis and meiosis (PubMed:28617811). May regulate the intracellular transport and presentation of a defined set of transmembrane proteins, such as transmembrane TGFA (By similarity). Required for normal acrosome formation during spermiogenesis and normal male fertility, probably by promoting colocalization of JAM2 and JAM3 at contact sites between germ cells and Sertoli cells (PubMed:28617811). Mediates ER stress-induced unconventional (ER/Golgi-independent) trafficking of core-glycosylated CFTR to cell membrane (By similarity). {ECO:0000250|UniProtKB:Q9H8Y8, ECO:0000269|PubMed:28617811}. PTM: Myristoylated (By similarity). Myristoylation is essential for the Golgi targeting (By similarity). {ECO:0000250|UniProtKB:Q9H8Y8, ECO:0000250|UniProtKB:Q9R064}.; PTM: Palmitoylated. {ECO:0000250|UniProtKB:Q9H8Y8}.; PTM: Phosphorylated in mitotic cells. ER stress-induced phosphorylation at Ser-443 induces monomerization and subsequent relocalization from Golgi to ER which is essential for mediating unconventional (ER/Golgi-independent) trafficking of CFTR to the cell membrane. {ECO:0000250|UniProtKB:Q9H8Y8}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9R064}; Lipid-anchor {ECO:0000250|UniProtKB:Q9R064}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9H8Y8}. Golgi apparatus {ECO:0000250|UniProtKB:Q9H8Y8}. Note=Detected in the intermediate Golgi, membrane-associated. ER stress triggers its relocalization from Golgi to ER membrane. {ECO:0000250|UniProtKB:Q9H8Y8, ECO:0000250|UniProtKB:Q9R064}. SUBUNIT: Homodimer. Homooligomer. ER stress induces phosphorylation-dependent monomerization (By similarity). Interacts with BLZF1/Golgin 45 (PubMed:11739401, PubMed:28049725). Identified in a complex with RAB2 and GORASP2 (PubMed:11739401). Interacts with JAM2 and JAM3 (PubMed:28617811). Interacts with members of the p24 cargo receptors. Interacts with CNIH and the cytoplasmic domain of transmembrane TGFA, prior its transit in the trans-Golgi. Interacts with KCTD5 (By similarity). Interacts with TMED2 and TMED3 (By similarity). Interacts with SEC16A in response to ER stress (By similarity). Interacts (via PDZ GRASP-type 1 domain) with core-glycosylated CFTR in response to ER stress (By similarity). {ECO:0000250|UniProtKB:Q9H8Y8, ECO:0000250|UniProtKB:Q9R064, ECO:0000269|PubMed:11739401, ECO:0000269|PubMed:28049725, ECO:0000269|PubMed:28617811}. TISSUE SPECIFICITY: Detected in lung, heart and testis. Colocalized in a polarized fashion in the acrosome region with JAM3 in round spermatids (at protein level). {ECO:0000269|PubMed:28617811}. +O88630 GOSR1_MOUSE Golgi SNAP receptor complex member 1 (28 kDa Golgi SNARE protein) (28 kDa cis-Golgi SNARE p28) (GOS-28) 250 28,489 Chain (1); Coiled coil (2); Initiator methionine (1); Modified residue (2); Sequence conflict (1); Topological domain (1); Transmembrane (1) TRANSMEM 230 250 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 2 229 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in transport from the ER to the Golgi apparatus as well as in intra-Golgi transport. It belongs to a super-family of proteins called t-SNAREs or soluble NSF (N-ethylmaleimide-sensitive factor) attachment protein receptor. May play a protective role against hydrogen peroxide induced cytotoxicity under glutathione depleted conditions in neuronal cells by regulating the intracellular ROS levels via inhibition of p38 MAPK (MAPK11, MAPK12, MAPK13 and MAPK14). Participates in docking and fusion stage of ER to cis-Golgi transport. Plays an important physiological role in VLDL-transport vesicle-Golgi fusion and thus in VLDL delivery to the hepatic cis-Golgi (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:15250942}; Single-pass type IV membrane protein {ECO:0000269|PubMed:15250942}. Note=Localizes throughout the Golgi apparatus, with lowest levels in the trans-Golgi network. Enriched on vesicular components at the terminal rims of the Golgi. {ECO:0000250}. SUBUNIT: Component of several multiprotein Golgi SNARE complexes. Identified in a SNARE complex with BET1, STX5 and YKT6, in a SNARE complex with BET1L, STX5 and YKT6, in a SNARE complex with STX5, GOSR2, SEC22B and BET1, and in complex with STX5 and COG3. Interacts with GABARAPL2 (By similarity). {ECO:0000250}. +O35166 GOSR2_MOUSE Golgi SNAP receptor complex member 2 (27 kDa Golgi SNARE protein) (Membrin) 212 24,725 Chain (1); Coiled coil (1); Modified residue (1); Motif (1); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 191 211 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 1 190 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 212 212 Vesicular. {ECO:0000255}. FUNCTION: Involved in transport of proteins from the cis/medial-Golgi to the trans-Golgi network. {ECO:0000250|UniProtKB:O35165}. SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane {ECO:0000250|UniProtKB:O35165}; Single-pass type IV membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:O35165}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O35165}. Note=Concentrated most in the intermediate compartment/cis-Golgi network and the cis-Golgi cisternae 1 and 2. Greatly reduced in concentration at the trans end of the Golgi apparatus. {ECO:0000250|UniProtKB:O35165}. SUBUNIT: Part of a unique SNARE complex composed of the Golgi SNAREs GOSR1, STX5 and YKT6. {ECO:0000250|UniProtKB:O35165}. +Q8BG55 GP171_MOUSE Probable G-protein coupled receptor 171 319 36,720 Chain (1); Glycosylation (1); Sequence conflict (4); Topological domain (8); Transmembrane (7) TRANSMEM 22 42 Helical; Name=1. {ECO:0000255}.; TRANSMEM 49 69 Helical; Name=2. {ECO:0000255}.; TRANSMEM 90 110 Helical; Name=3. {ECO:0000255}.; TRANSMEM 133 153 Helical; Name=4. {ECO:0000255}.; TRANSMEM 182 202 Helical; Name=5. {ECO:0000255}.; TRANSMEM 225 245 Helical; Name=6. {ECO:0000255}.; TRANSMEM 269 289 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 21 Extracellular. {ECO:0000255}.; TOPO_DOM 43 48 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 70 89 Extracellular. {ECO:0000255}.; TOPO_DOM 111 132 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 154 181 Extracellular. {ECO:0000255}.; TOPO_DOM 203 224 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 246 268 Extracellular. {ECO:0000255}.; TOPO_DOM 290 319 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q6PI62 GP173_MOUSE Probable G-protein coupled receptor 173 (Super conserved receptor expressed in brain 3) 373 41,511 Chain (1); Disulfide bond (1); Glycosylation (2); Topological domain (8); Transmembrane (7) TRANSMEM 27 47 Helical; Name=1. {ECO:0000255}.; TRANSMEM 60 80 Helical; Name=2. {ECO:0000255}.; TRANSMEM 98 118 Helical; Name=3. {ECO:0000255}.; TRANSMEM 140 160 Helical; Name=4. {ECO:0000255}.; TRANSMEM 189 209 Helical; Name=5. {ECO:0000255}.; TRANSMEM 288 308 Helical; Name=6. {ECO:0000255}.; TRANSMEM 323 343 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 26 Extracellular. {ECO:0000255}.; TOPO_DOM 48 59 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 81 97 Extracellular. {ECO:0000255}.; TOPO_DOM 119 139 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 161 188 Extracellular. {ECO:0000255}.; TOPO_DOM 210 287 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 309 322 Extracellular. {ECO:0000255}.; TOPO_DOM 344 373 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan receptor. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q9JIM3 ER6L2_MOUSE DNA excision repair protein ERCC-6-like 2 (EC 3.6.4.-) (DNA repair and recombination protein RAD26-like) 1537 173,873 Alternative sequence (7); Chain (1); Domain (2); Erroneous initiation (2); Frameshift (1); Modified residue (2); Motif (1); Nucleotide binding (1); Sequence caution (1); Sequence conflict (8) FUNCTION: May be involved in early DNA damage response. {ECO:0000250}. PTM: Phosphorylated by NEK6. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Mitochondrion {ECO:0000250}. Note=Colocalizes with NEK6 in the centrosome. In response to DNA damage, translocates from the cytosol to mitochondria and nucleus in a reactive oxygen species (ROS)-dependent manner. {ECO:0000250}. SUBUNIT: Interacts with NEK6. {ECO:0000250}. +P60229 EIF3E_MOUSE Eukaryotic translation initiation factor 3 subunit E (eIF3e) (Eukaryotic translation initiation factor 3 subunit 6) (MMTV integration site 6) (Mammary tumor-associated protein INT-6) (Viral integration site protein INT-6) (eIF-3 p48) 445 52,221 Chain (1); Domain (1); Initiator methionine (1); Modified residue (5); Region (3) FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression. Required for nonsense-mediated mRNA decay (NMD); may act in conjunction with UPF2 to divert mRNAs from translation to the NMD pathway. May interact with MCM7 and EPAS1 and regulate the proteasome-mediated degradation of these proteins. {ECO:0000255|HAMAP-Rule:MF_03004, ECO:0000269|PubMed:17581632}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03004}. Nucleus, PML body {ECO:0000255|HAMAP-Rule:MF_03004}. SUBUNIT: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B, EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and EIF3M. The eIF-3 complex appears to include 3 stable modules: module A is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D, EIF3E, EIF3K and EIF3L. EIF3C of module C binds EIF3B of module A and EIF3H of module B, thereby linking the three modules. EIF3J is a labile subunit that binds to the eIF-3 complex via EIF3B. The eIF-3 complex interacts with RPS6KB1 under conditions of nutrient depletion. Mitogenic stimulation leads to binding and activation of a complex composed of MTOR and RPTOR, leading to phosphorylation and release of RPS6KB1 and binding of EIF4B to eIF-3. Interacts with COPS3, COPS6, COPS7 (COPS7A or COPS7B), EIF4G1, EPAS1, MCM7, NCBP1, PSMC6, TRIM27 and UPF2 (By similarity). Interacts with IFIT1 and IFIT2 (By similarity). {ECO:0000255|HAMAP-Rule:MF_03004}. TISSUE SPECIFICITY: Ubiquitously expressed. DISEASE: Note=EIF3E serves as a site for viral integration of mouse mammary tumor virus (MMTV) in mammary tumors. MMTV integration into EIF3E can result in EIF3E truncation and expression of chimeric RNA species which terminate at a cryptic transcription stop signal in the reverse U3 portion of the MMTV long terminal repeat. This causes deregulation of the normal control of mammary epithelial cell growth. {ECO:0000269|PubMed:7853537}. +Q6X7S9 EID2_MOUSE EP300-interacting inhibitor of differentiation 2 (EID-2) (CREBBP/EP300 inhibitor 2) (EID-1-like inhibitor of differentiation 2) 236 25,304 Chain (1); Coiled coil (1); Compositional bias (1); Modified residue (2) FUNCTION: Interacts with EP300 and acts as a repressor of MYOD-dependent transcription and muscle differentiation. Inhibits EP300 histone acetyltransferase activity. Acts as a repressor of TGFB/SMAD transcriptional responses. May act as a repressor of the TGFB/SMAD3-dependent signaling by selectively blocking formation of TGFB-induced SMAD3-SMAD4 complex (By similarity). {ECO:0000250|UniProtKB:Q8N6I1}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8N6I1}. SUBUNIT: Heterodimer with EID2B. Interacts with the C-terminus of EP300. Interacts with HDAC1 and HDAC2. Interacts with SMAD2, SMAD4 and with the MH2 domain of SMAD3 (By similarity). {ECO:0000250|UniProtKB:Q8N6I1}. DOMAIN: The N-terminal portion of EID2 is required for nuclear localization. {ECO:0000250|UniProtKB:Q8N6I1}. TISSUE SPECIFICITY: Expressed in heart, brain, kidney and pancreas. Not detected in placenta. {ECO:0000269|PubMed:14585496}. +Q8C522 ENDD1_MOUSE Endonuclease domain-containing 1 protein (EC 3.1.30.-) 501 55,262 Chain (1); Modified residue (1); Sequence conflict (5); Signal peptide (1) FUNCTION: May act as a DNase and a RNase. {ECO:0000305}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q3V188 ENDOU_MOUSE Poly(U)-specific endoribonuclease (EC 3.1.-.-) (Placental protein 11-related protein) (PP11-related protein) (Protein endoU) (T-cell-specific protein 30) (Tcl-30) (Uridylate-specific endoribonuclease) 412 47,010 Alternative sequence (1); Chain (1); Disulfide bond (14); Domain (2); Signal peptide (1) FUNCTION: Endoribonuclease that cleaves single-stranded RNAs at uridylates and releases products that have 2'-3'-cyclic phosphate termini. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. SUBUNIT: Monomer. {ECO:0000250}. TISSUE SPECIFICITY: Specifically expressed in T-cells during apoptosis. Expressed in surface heat stable antigen (HSA)-containing T-cells populations (CD4(-)CD8(-)HSA(+), CD4(+)CD8(-)HSA(+), CD4(-)CD8(+)HSA(+), and CD4(+)CD8(+)HSA(+)) and not in the HSA(-) single positive T-cell populations of the thymus or spleen, suggesting that expression is lost during T-cell maturation and is absent at the most mature stages of T-cell development. {ECO:0000269|PubMed:1506680, ECO:0000269|PubMed:8104059}. +Q99N64 GMCL2_MOUSE Germ cell-less protein-like 2 (BTB domain containing 35, family member 1) (Germ cell-less protein-like 1-like) (mGclh) 498 57,827 Chain (1); Domain (1); Motif (1); Sequence conflict (15) Protein modification; protein ubiquitination. FUNCTION: Possible function in spermatogenesis. Probable substrate-specific adapter of an E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000250|UniProtKB:Q8NEA9, ECO:0000250|UniProtKB:Q920G9}. SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000250|UniProtKB:Q920G9}. SUBUNIT: Interacts with CUL3. {ECO:0000250|UniProtKB:Q8NEA9}. +P58929 GMEB2_MOUSE Glucocorticoid modulatory element-binding protein 2 (GMEB-2) 530 56,631 Binding site (4); Chain (1); Coiled coil (2); Compositional bias (2); Cross-link (2); Domain (1); Metal binding (4); Modified residue (1) FUNCTION: Trans-acting factor that binds to glucocorticoid modulatory elements (GME) present in the TAT (tyrosine aminotransferase) promoter and increases sensitivity to low concentrations of glucocorticoids. Binds also to the transferrin receptor promoter (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00185}. Cytoplasm {ECO:0000250}. Note=May be also cytoplasmic. {ECO:0000250}. SUBUNIT: Homodimer, and heterodimer of GMEB1 and GMEB2. Interacts with the glucocorticoid receptor (NR3C1). May interact with CREB-binding protein (CBP) (By similarity). {ECO:0000250}. +Q8BTZ7 GMPPB_MOUSE Mannose-1-phosphate guanyltransferase beta (EC 2.7.7.13) (GDP-mannose pyrophosphorylase B) (GTP-mannose-1-phosphate guanylyltransferase beta) 360 39,917 Chain (1) Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; GDP-alpha-D-mannose from alpha-D-mannose 1-phosphate (GTP route): step 1/1. FUNCTION: Catalyzes the formation of GDP-mannose, an essential precursor of glycan moieties of glycoproteins and glycolipids. {ECO:0000250|UniProtKB:P0C5I2}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y5P6}. SUBUNIT: Associates with GMPPA. {ECO:0000250|UniProtKB:P0C5I2}. +P21278 GNA11_MOUSE Guanine nucleotide-binding protein subunit alpha-11 (G alpha-11) (G-protein subunit alpha-11) 359 42,024 Binding site (1); Chain (1); Lipidation (2); Metal binding (2); Nucleotide binding (4); Sequence conflict (1) FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Acts as an activator of phospholipase C. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Cytoplasm {ECO:0000250}. SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site. Interacts with RGS22. Interacts with NTSR1 (By similarity). {ECO:0000250}. +P27600 GNA12_MOUSE Guanine nucleotide-binding protein subunit alpha-12 (G alpha-12) (G-protein subunit alpha-12) 379 44,095 Beta strand (7); Binding site (1); Chain (1); Helix (17); Lipidation (1); Metal binding (2); Modified residue (1); Mutagenesis (3); Nucleotide binding (3); Turn (2) FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems (PubMed:19151758, PubMed:21212405, PubMed:22609986). Activates effector molecule RhoA by binding and activating RhoGEFs (ARHGEF12/LARG) (By similarity). GNA12-dependent Rho signaling subsequently regulates transcription factor AP-1 (activating protein-1) (PubMed:19151758, PubMed:21212405). GNA12-dependent Rho signaling also regulates protein phosphatese 2A activation causing dephosphorylation of its target proteins (By similarity). Promotes tumor cell invasion and metastasis by activating RhoA/ROCK signaling pathway and up-regulating proinflammatory cytokine production (By similarity). Inhibits CDH1-mediated cell adhesion in process independent from Rho activation (By similarity). Together with NAPA promotes CDH5 localization to plasma membrane (By similarity). May play a role in the control of cell migration through the TOR signaling cascade (PubMed:22609986). {ECO:0000250|UniProtKB:Q03113, ECO:0000269|PubMed:19151758, ECO:0000269|PubMed:21212405, ECO:0000269|PubMed:22609986}. PTM: Myristoylation of mutated N-terminus in place of original palmitoylation restores the transformation activity. {ECO:0000269|PubMed:9485474}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q03113}; Lipid-anchor {ECO:0000250|UniProtKB:Q63210}. Lateral cell membrane {ECO:0000250|UniProtKB:Q03113}; Lipid-anchor {ECO:0000250|UniProtKB:Q63210}. Cytoplasm {ECO:0000250|UniProtKB:Q03113}. Note=CDH1 enhances cell membrane localization. {ECO:0000250|UniProtKB:Q03113}. SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma (PubMed:16388592). The alpha chain contains the guanine nucleotide binding site (PubMed:16388592). Interacts with UBXD5 (By similarity). Interacts (in GTP-bound form) with PPP5C (via TPR repeats); activates PPP5C phosphatase activity and translocates PPP5C to the cell membrane (By similarity). Interacts with RGS22 (By similarity). Interacts (via N-terminus) with NAPA; the interaction promotes CDH5 localization to plasma membrane (By similarity). Interacts with CTNND1 (via N-terminus); the interaction regulates CDH1-mediated cell-cell adhesion (PubMed:15240885). Interacts with PPP2R1A; the interaction promotes protein phosphatase 2A activation causing dephosphorylation of MAPT (By similarity). Interacts (in GTP-bound form) with ARHGEF1 (PubMed:16388592). Interacts (in GTP-bound form) with ARHGEF11 (via RGS domain) (By similarity). Interacts (in GTP-bound form) with ARHGEF12 (via RGS domain) (PubMed:16388592). {ECO:0000250|UniProtKB:Q03113, ECO:0000269|PubMed:15240885, ECO:0000269|PubMed:16388592}. +P27601 GNA13_MOUSE Guanine nucleotide-binding protein subunit alpha-13 (G alpha-13) (G-protein subunit alpha-13) 377 44,055 Beta strand (9); Binding site (2); Chain (1); Helix (20); Lipidation (2); Metal binding (3); Modified residue (1); Nucleotide binding (3); Sequence conflict (1); Turn (1) FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems (PubMed:21212405, PubMed:19151758, PubMed:16388592). Activates effector molecule RhoA by binding and activating RhoGEFs (ARHGEF1/p115RhoGEF, ARHGEF11/PDZ-RhoGEF and ARHGEF12/LARG) (PubMed:16388592). GNA13-dependent Rho signaling subsequently regulates transcription factor AP-1 (activating protein-1) (PubMed:19151758, PubMed:21212405). Promotes tumor cell invasion and metastasis by activating Rho/ROCK signaling pathway (By similarity). Inhibits CDH1-mediated cell adhesion in process independent from Rho activation (By similarity). {ECO:0000250|UniProtKB:Q14344, ECO:0000269|PubMed:16388592, ECO:0000269|PubMed:19151758, ECO:0000269|PubMed:21212405}. PTM: Phosphorylation on Thr-203 destabilizes the heterotrimer of alpha, beta and gamma, and inhibits Rho activation. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:18703424}; Lipid-anchor {ECO:0000269|PubMed:18703424}. Melanosome {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:18703424}. Nucleus {ECO:0000269|PubMed:18703424}. Note=Cytoplasmic in adult somatic cells, but mainly nuclear in spermatids in the testes. Translocates from the cytoplasm to the nucleus during spermatogenesis, hence predominantly observed in the cytoplasm of round spermatids but localized in the nuclei of elongating or elongated spermatids and testicular spermatozoa. SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma (PubMed:16388592). The alpha chain contains the guanine nucleotide binding site (PubMed:16388592). Interacts with UBXD5 (By similarity). Interacts with HAX1 (By similarity). Interacts (in GTP-bound form) with PPP5C (via TPR repeats); activates PPP5C phosphatase activity and translocates PPP5C to the cell membrane (By similarity). Interacts with RGS22 (By similarity). Interacts (in GTP-bound form) with ARHGEF1 (PubMed:16388592). Interacts (in GTP-bound form) with ARHGEF11 (via RGS domain) (PubMed:18940608). Interacts (in GTP-bound form) with ARHGEF12 (via RGS domain) (PubMed:16388592). Interacts with CTNND1 (PubMed:15240885). {ECO:0000250|UniProtKB:Q14344, ECO:0000269|PubMed:15240885, ECO:0000269|PubMed:16388592, ECO:0000269|PubMed:18940608}. TISSUE SPECIFICITY: Expressed in brain and testis, as well as in kidney and sperm (at protein level). {ECO:0000269|PubMed:18703424}. +P30677 GNA14_MOUSE Guanine nucleotide-binding protein subunit alpha-14 (G alpha-14) (G-protein subunit alpha-14) 355 41,528 Binding site (1); Chain (1); Metal binding (2); Nucleotide binding (4); Sequence conflict (1) FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site. +P30678 GNA15_MOUSE Guanine nucleotide-binding protein subunit alpha-15 (G alpha-15) (G-protein subunit alpha-15) 374 43,536 Binding site (1); Chain (1); Metal binding (2); Nucleotide binding (4) FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site. TISSUE SPECIFICITY: Expressed primarily in hematopoietic cells. Coexpressed with EDG6 at the same relative levels in all tissues examined, with the highest levels in adult spleen and lung. {ECO:0000269|PubMed:12401211}. +Q9JK38 GNA1_MOUSE Glucosamine 6-phosphate N-acetyltransferase (EC 2.3.1.4) (Phosphoglucosamine acetylase) (Phosphoglucosamine transacetylase) (Protein EMeg32) 184 20,791 Binding site (3); Chain (1); Domain (1); Region (5) Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I): step 1/2. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:10777580}; Peripheral membrane protein {ECO:0000269|PubMed:10777580}. Endosome membrane {ECO:0000269|PubMed:10777580}; Peripheral membrane protein {ECO:0000269|PubMed:10777580}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q96EK6}. TISSUE SPECIFICITY: Ubiquitous. Shows a strong differential expression pattern in adult hematopoietic precursor cells. {ECO:0000269|PubMed:10777580}. +Q8BGB7 ENOPH_MOUSE Enolase-phosphatase E1 (EC 3.1.3.77) (2,3-diketo-5-methylthio-1-phosphopentane phosphatase) (MASA homolog) 257 28,600 Alternative sequence (1); Binding site (1); Chain (1); Frameshift (1); Metal binding (3); Region (1); Sequence conflict (4) Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 3/6. Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 4/6. FUNCTION: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene). {ECO:0000255|HAMAP-Rule:MF_03117}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03117}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03117}. SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03117}. +P08752 GNAI2_MOUSE Guanine nucleotide-binding protein G(i) subunit alpha-2 (Adenylate cyclase-inhibiting G alpha protein) 355 40,489 Binding site (1); Chain (1); Initiator methionine (1); Lipidation (2); Metal binding (2); Nucleotide binding (4); Sequence conflict (3) FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(i) proteins are involved in hormonal regulation of adenylate cyclase: they inhibit the cyclase in response to beta-adrenergic stimuli. May play a role in cell division. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cell membrane {ECO:0000250}. Membrane {ECO:0000250|UniProtKB:P04899}; Lipid-anchor {ECO:0000250|UniProtKB:P04899}. Note=Localizes in the centrosomes of interphase and mitotic cells. Detected at the cleavage furrow and/or the midbody (By similarity). {ECO:0000250}. SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site. Interacts with UNC5B. Interacts with GPSM1. Interacts with RGS12 and RGS14 (By similarity). {ECO:0000250}. +Q8CGK7 GNAL_MOUSE Guanine nucleotide-binding protein G(olf) subunit alpha (Adenylate cyclase-stimulating G alpha protein, olfactory type) 381 44,308 Binding site (1); Chain (1); Initiator methionine (1); Lipidation (2); Metal binding (2); Modified residue (1); Nucleotide binding (4) FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. G(olf) alpha mediates signal transduction within the olfactory neuroepithelium and the basal ganglia. May be involved in some aspect of visual transduction, and in mediating the effect of one or more hormones/neurotransmitters (By similarity). {ECO:0000250}. SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site. +P17183 ENOG_MOUSE Gamma-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 2) (Neural enolase) (Neuron-specific enolase) (NSE) 434 47,297 Active site (2); Binding site (5); Chain (1); Cross-link (1); Initiator methionine (1); Metal binding (3); Modified residue (23); Region (1) Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. FUNCTION: Has neurotrophic and neuroprotective properties on a broad spectrum of central nervous system (CNS) neurons. Binds, in a calcium-dependent manner, to cultured neocortical neurons and promotes cell survival (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Can translocate to the plasma membrane in either the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form. {ECO:0000250}. SUBUNIT: Mammalian enolase is composed of 3 isozyme subunits, alpha, beta and gamma, which can form homodimers or heterodimers which are cell-type and development-specific. TISSUE SPECIFICITY: Skeletal muscle (at protein level). The alpha/alpha homodimer is expressed in embryo and in most adult tissues. The alpha/beta heterodimer and the beta/beta homodimer are found in striated muscle, and the alpha/gamma heterodimer and the gamma/gamma homodimer in neurons. {ECO:0000269|PubMed:23446454, ECO:0000305|PubMed:11229603}. +Q9Z0F1 GNAS3_MOUSE Neuroendocrine secretory protein 55 (NESP55) [Cleaved into: LHAL tetrapeptide; GPIPIRRH peptide] 257 29,301 Alternative sequence (1); Chain (1); Compositional bias (1); Peptide (2); Sequence conflict (9); Signal peptide (1) PTM: Binds keratan sulfate chains. {ECO:0000250|UniProtKB:O18979}.; PTM: May be proteolytically processed to give rise to a number of active peptides. {ECO:0000250|UniProtKB:O18979}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle {ECO:0000250}. Secreted {ECO:0000250}. Note=Neuroendocrine secretory granules. {ECO:0000250}. +P20612 GNAT1_MOUSE Guanine nucleotide-binding protein G(t) subunit alpha-1 (Transducin alpha-1 chain) 350 39,967 Binding site (3); Chain (1); Initiator methionine (1); Lipidation (1); Metal binding (2); Modified residue (1); Nucleotide binding (3); Region (1) FUNCTION: Functions as signal transducer for the rod photoreceptor RHO. Required for normal RHO-mediated light perception by the retina (By similarity). Guanine nucleotide-binding proteins (G proteins) function as transducers downstream of G protein-coupled receptors (GPCRs), such as the photoreceptor RHO. The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state. Activated RHO promotes GDP release and GTP binding. Signaling is mediated via downstream effector proteins, such as cGMP-phosphodiesterase (By similarity). {ECO:0000250|UniProtKB:P04695, ECO:0000250|UniProtKB:P11488}. SUBCELLULAR LOCATION: Cell projection, cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:P04695}. Membrane {ECO:0000250|UniProtKB:P04695}; Peripheral membrane protein {ECO:0000250|UniProtKB:P04695}. SUBUNIT: Heterotrimeric G proteins are composed of 3 subunits alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site. Interacts with RHO. Interacts with RGS9 and PDE6G (By similarity). Interacts (when myristoylated) with UNC119; interaction is required for localization in sensory neurons (By similarity). {ECO:0000250|UniProtKB:P04695, ECO:0000250|UniProtKB:P11488}. TISSUE SPECIFICITY: Rod. +Q3V3I2 GNAT3_MOUSE Guanine nucleotide-binding protein G(t) subunit alpha-3 (Gustducin alpha-3 chain) 354 40,316 Binding site (1); Chain (1); Initiator methionine (1); Lipidation (1); Metal binding (2); Nucleotide binding (4) FUNCTION: Guanine nucleotide-binding protein (G protein) alpha subunit playing a prominent role in bitter and sweet taste transduction as well as in umami (monosodium glutamate, monopotassium glutamate, and inosine monophosphate) taste transduction. Transduction by this alpha subunit involves coupling of specific cell-surface receptors with a cGMP-phosphodiesterase; Activation of phosphodiesterase lowers intracellular levels of cAMP and cGMP which may open a cyclic nucleotide-suppressible cation channel leading to influx of calcium, ultimately leading to release of neurotransmitter. Indeed, denatonium and strychnine induce transient reduction in cAMP and cGMP in taste tissue, whereas this decrease is inhibited by GNAT3 antibody. Gustducin heterotrimer transduces response to bitter and sweet compounds via regulation of phosphodiesterase for alpha subunit, as well as via activation of phospholipase C for beta and gamma subunits, with ultimate increase inositol trisphosphate and increase of intracellular Calcium. GNAT3 can functionally couple to taste receptors to transmit intracellular signal: receptor heterodimer TAS1R2/TAS1R3 senses sweetness and TAS1R1/TAS1R3 transduces umami taste, whereas the T2R family GPCRs act as bitter sensors. Functions also as lumenal sugar sensors in the gut to control the expression of the Na+-glucose transporter SGLT1 in response to dietaty sugar, as well as the secretion of Glucagon-like peptide-1, GLP-1 and glucose-dependent insulinotropic polypeptide, GIP. Thus, may modulate the gut capacity to absorb sugars, with implications in malabsorption syndromes and diet-related disorders including diabetes and obesity. {ECO:0000269|PubMed:10570481, ECO:0000269|PubMed:11245589, ECO:0000269|PubMed:17724330, ECO:0000269|PubMed:17724332}. PTM: Potential N-myristoylation may anchor alpha-subunit to the inner surface of plasma membrane. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma, respectively GNAT3, GNB1 and GNG13 for Gustducin heterotrimer for bitter taste transduction. The alpha chain contains the guanine nucleotide binding site. Gustducin heterotrimer may also be composed of GNAT3, GNB3 and GNG13. {ECO:0000269|PubMed:10570481}. TISSUE SPECIFICITY: Expressed in taste buds (sensory organs of clustered epithelial cells) of the circumvallate and fungiform papillae of the tongue as well as in palatal taste buds at protein level. Expressed in enteroendocrine cells of the gut, such as in subsets of enteroendocrine cells in the midjejunum and brush cells. Detected also in spermatozoa. {ECO:0000269|PubMed:14637165, ECO:0000269|PubMed:17021831, ECO:0000269|PubMed:17229761, ECO:0000269|PubMed:17290008, ECO:0000269|PubMed:17724332}. +Q9EQ15 GNB1L_MOUSE Guanine nucleotide-binding protein subunit beta-like protein 1 (G protein subunit beta-like protein 1) (WD repeat-containing protein 14) (WD40 repeat-containing protein deleted in VCFS) (WDVCF) 326 35,663 Alternative sequence (2); Chain (1); Compositional bias (1); Frameshift (1); Repeat (6); Sequence conflict (11) TISSUE SPECIFICITY: Expressed at low levels in most tissues and highly expressed in adult testis. +Q8CI11 GNL3_MOUSE Guanine nucleotide-binding protein-like 3 (Nucleolar GTP-binding protein 3) (Nucleostemin) 538 60,786 Alternative sequence (1); Chain (1); Coiled coil (1); Cross-link (5); Domain (1); Modified residue (6); Mutagenesis (1); Nucleotide binding (3); Region (3); Sequence conflict (2) FUNCTION: May be required to maintain the proliferative capacity of stem cells (By similarity). Stabilizes MDM2 by preventing its ubiquitination, and hence proteasomal degradation. {ECO:0000250, ECO:0000269|PubMed:21132010}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21132010}. Nucleus, nucleolus {ECO:0000269|PubMed:12464630}. Note=Shuttles between the nucleus and nucleolus. {ECO:0000250|UniProtKB:Q811S9}. SUBUNIT: Interacts with MDM2; this interaction stabilizes MDM2. Interaction with MDM2 occurs in the nucleoplasm and is triggered by a nucleolar release mechanism, such as mitosis-induced nucleolar disassembly. Indirectly interacts with TP53, via MDM2-binding (By similarity). {ECO:0000250}. DOMAIN: The basic domain (B) allows nucleolar localization in the absence of GTP. The intermediate domain (I) inhibits nucleolar localization by the B domain and is required for exit from the nucleolus. Exit from the nucleolus to the nucleoplasm requires both the I and the acidic (A) domains, and may be triggered by GTP hydrolysis (By similarity). {ECO:0000250}.; DOMAIN: In contrast to other GTP-binding proteins, this family is characterized by a circular permutation of the GTPase motifs described by a G4-G1-G3 pattern. TISSUE SPECIFICITY: Expressed in the adult bone marrow population that is enriched in hematopoietic stem cells. {ECO:0000269|PubMed:12464630}. +Q9QXF8 GNMT_MOUSE Glycine N-methyltransferase (EC 2.1.1.20) 293 32,675 Beta strand (14); Binding site (10); Chain (1); Helix (11); Initiator methionine (1); Modified residue (7); Region (1); Sequence conflict (1); Turn (3) FUNCTION: Catalyzes the methylation of glycine by using S-adenosylmethionine (AdoMet) to form N-methylglycine (sarcosine) with the concomitant production of S-adenosylhomocysteine (AdoHcy). Possible crucial role in the regulation of tissue concentration of AdoMet and of metabolism of methionine (By similarity). {ECO:0000250, ECO:0000269|PubMed:15340920}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homotetramer. {ECO:0000250}. +Q9CRC9 GNPI2_MOUSE Glucosamine-6-phosphate isomerase 2 (EC 3.5.99.6) (Glucosamine-6-phosphate deaminase 2) (GNPDA 2) (GlcN6P deaminase 2) 276 31,084 Active site (4); Alternative sequence (1); Chain (1); Coiled coil (1); Modified residue (1); Sequence conflict (1) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homohexamer. {ECO:0000250}. +Q69ZN6 GNPTA_MOUSE N-acetylglucosamine-1-phosphotransferase subunits alpha/beta (EC 2.7.8.17) (GlcNAc-1-phosphotransferase subunits alpha/beta) (Stealth protein GNPTAB) (UDP-N-acetylglucosamine-1-phosphotransferase subunits alpha/beta) [Cleaved into: N-acetylglucosamine-1-phosphotransferase subunit alpha; N-acetylglucosamine-1-phosphotransferase subunit beta] 1235 140,984 Alternative sequence (2); Calcium binding (1); Chain (2); Compositional bias (1); Disulfide bond (4); Domain (2); Erroneous initiation (2); Glycosylation (8); Metal binding (6); Repeat (2); Sequence conflict (2); Site (1); Transmembrane (2) TRANSMEM 22 42 Helical. {ECO:0000255}.; TRANSMEM 1194 1214 Helical. {ECO:0000255}. FUNCTION: Catalyzes the formation of mannose 6-phosphate (M6P) markers on high mannose type oligosaccharides in the Golgi apparatus. M6P residues are required to bind to the M6P receptors (MPR), which mediate the vesicular transport of lysosomal enzymes to the endosomal/prelysosomal compartment. {ECO:0000250|UniProtKB:Q3T906}. PTM: The alpha- and beta-subunits are generated by a proteolytic cleavage by MBTPS1 protease at the Lys-907-Asp-908 bond. {ECO:0000250|UniProtKB:Q3T906}. SUBCELLULAR LOCATION: N-acetylglucosamine-1-phosphotransferase subunit alpha: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q3T906}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q3T906}.; SUBCELLULAR LOCATION: N-acetylglucosamine-1-phosphotransferase subunit beta: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q3T906}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q3T906}. SUBUNIT: Hexamer of two alpha, two beta and two gamma (GNPTG) subunits; disulfide-linked. The alpha and/or the beta subunits of the enzyme constitute the catalytic subunits. {ECO:0000250|UniProtKB:Q3T906}. DOMAIN: The DMAP-interaction domain mediates substrate recognition. It specifically recognizes a conformation-dependent protein determinant present in acid hydrolases. {ECO:0000250|UniProtKB:Q3T906}. +Q8R2X8 GO45_MOUSE Golgin-45 (Basic leucine zipper nuclear factor 1) 403 45,541 Alternative sequence (1); Chain (1); Coiled coil (1); Modified residue (2); Motif (1); Mutagenesis (3); Region (1); Sequence conflict (2) FUNCTION: Required for normal Golgi structure and for protein transport from the endoplasmic reticulum (ER) through the Golgi apparatus to the cell surface. {ECO:0000250|UniProtKB:Q9H2G9}. PTM: ADP-ribosylated by tankyrase TNKS and TNKS2. Poly-ADP-ribosylated protein is recognized by RNF146, followed by ubiquitination. {ECO:0000250|UniProtKB:Q9H2G9}.; PTM: Ubiquitinated by RNF146 when poly-ADP-ribosylated, leading to its degradation. {ECO:0000250|UniProtKB:Q9H2G9}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9H2G9}. SUBUNIT: Interacts with GORASP2 (PubMed:11739401, PubMed:28049725). Interacts with the GTP-bound form of RAB2, but not with other Golgi Rab proteins (PubMed:11739401). Identified in a complex with RAB2 and GORASP2 (PubMed:11739401). {ECO:0000269|PubMed:11739401, ECO:0000269|PubMed:28049725}. DOMAIN: The tankyrase-binding motif (also named TBD) is required for interaction with tankyrase TNKS and TNKS2. {ECO:0000250|UniProtKB:Q9H2G9}. +Q921M4 GOGA2_MOUSE Golgin subfamily A member 2 (130 kDa cis-Golgi matrix protein) (GM130) 999 113,278 Alternative sequence (1); Chain (1); Coiled coil (1); Compositional bias (3); Erroneous initiation (2); Modified residue (9); Motif (1); Region (2) FUNCTION: Peripheral membrane component of the cis-Golgi stack that acts as a membrane skeleton that maintains the structure of the Golgi apparatus, and as a vesicle thether that facilitates vesicle fusion to the Golgi membrane (PubMed:28028212). Required for normal protein transport from the endoplasmic reticulum to the Golgi apparatus and the cell membrane (PubMed:28028212). Together with p115/USO1 and STX5, involved in vesicle tethering and fusion at the cis-Golgi membrane to maintain the stacked and inter-connected structure of the Golgi apparatus. Plays a central role in mitotic Golgi disassembly: phosphorylation at Ser-37 by CDK1 at the onset of mitosis inhibits the interaction with p115/USO1, preventing tethering of COPI vesicles and thereby inhibiting transport through the Golgi apparatus during mitosis. Also plays a key role in spindle pole assembly and centrosome organization (By similarity). Promotes the mitotic spindle pole assembly by activating the spindle assembly factor TPX2 to nucleate microtubules around the Golgi and capture them to couple mitotic membranes to the spindle: upon phosphorylation at the onset of mitosis, GOLGA2 interacts with importin-alpha via the nuclear localization signal region, leading to recruit importin-alpha to the Golgi membranes and liberate the spindle assembly factor TPX2 from importin-alpha. TPX2 then activates AURKA kinase and stimulates local microtubule nucleation. Upon filament assembly, nascent microtubules are further captured by GOLGA2, thus linking Golgi membranes to the spindle (By similarity). Regulates the meiotic spindle pole assembly, probably via the same mechanism (PubMed:21552007). Also regulates the centrosome organization (By similarity). Also required for the Golgi ribbon formation and glycosylation of membrane and secretory proteins (By similarity). {ECO:0000250|UniProtKB:Q08379, ECO:0000250|UniProtKB:Q62839, ECO:0000269|PubMed:21552007, ECO:0000269|PubMed:28028212}. PTM: Phosphorylated at Ser-37 by CDK1 at the onset of mitosis, inhibiting the interaction with p115/USO1 and triggering Golgi disassembly. A report however suggests that Golgi disassembly is independent of phosphorylation at Ser-37. Phosphorylated at Ser-37 in prophase as the Golgi complex starts to break down, and remains phosphorylated during further breakdown and partitioning of the Golgi fragments in metaphase and anaphase. In telophase, GM130 is dephosphorylated by PP2A as the Golgi fragments start to reassemble. {ECO:0000250|UniProtKB:Q62839}.; PTM: Cleaved by caspases at the onset of apoptosis. {ECO:0000250|UniProtKB:Q08379}.; PTM: Methylation by PRMT5 is required for Golgi ribbon formation. {ECO:0000250|UniProtKB:Q08379}. SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane {ECO:0000250|UniProtKB:Q08379}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q08379}; Cytoplasmic side {ECO:0000250|UniProtKB:Q08379}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q08379}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q08379}; Cytoplasmic side {ECO:0000250|UniProtKB:Q08379}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q08379}. Note=Associates with the mitotic spindle during mitosis. {ECO:0000250|UniProtKB:Q08379, ECO:0000250|UniProtKB:Q62839}. SUBUNIT: Homodimer, may assemble into homohexamers (By similarity). Homotetramer; forms a parallel homotetramer with a flexible rod-like structure that can give rise to I- and Y-shaped conformations. Interacts with GORASP1/GRASP65. The homooligomer forms a complex with GORASP1 with a 1:1 stoichiometry (By similarity). Interacts with RAB1B that has been activated by GTP-binding. Interacts with p115/USO1; interaction with p115/USO1 inhibits interaction with STX5 and/or RAB1B. Interacts with STX5 (By similarity). Interacts with ZFPL1 (By similarity). Interacts with AKAP450/AKAP9; leading to recruit AKAP450/AKAP9 to the cis-Golgi (By similarity). {ECO:0000250|UniProtKB:Q08379, ECO:0000250|UniProtKB:Q62839}. DOMAIN: Extended rod-like protein with long coiled-coil domains. {ECO:0000250|UniProtKB:Q62839}.; DOMAIN: The nuclear localization signal (cNLS) mediates interaction with importin-alpha, recruiting importin-alpha to the Golgi membrane and liberating TPX2. {ECO:0000250|UniProtKB:Q08379}. TISSUE SPECIFICITY: Detected in brain, lung, liver, thymus and pancreas (PubMed:28028212). Detected in spermatocytes (PubMed:28617811). Present in oocytes during all oocyte meiotic maturation (at protein level). {ECO:0000269|PubMed:21552007, ECO:0000269|PubMed:28028212, ECO:0000269|PubMed:28617811}. +P97435 ENTK_MOUSE Enteropeptidase (EC 3.4.21.9) (Enterokinase) (Serine protease 7) (Transmembrane protease serine 15) [Cleaved into: Enteropeptidase non-catalytic heavy chain; Enteropeptidase catalytic light chain] 1069 118,735 Active site (3); Chain (2); Disulfide bond (14); Domain (8); Glycosylation (16); Topological domain (2); Transmembrane (1) TRANSMEM 19 47 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 18 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 48 1069 Extracellular. {ECO:0000255}. FUNCTION: Responsible for initiating activation of pancreatic proteolytic proenzymes (trypsin, chymotrypsin and carboxypeptidase A). It catalyzes the conversion of trypsinogen to trypsin which in turn activates other proenzymes including chymotrypsinogen, procarboxypeptidases, and proelastases (By similarity). {ECO:0000250}. PTM: The chains are derived from a single precursor that is cleaved by a trypsin-like protease. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. SUBUNIT: Heterodimer of a catalytic (light) chain and a multidomain (heavy) chain linked by a disulfide bond. {ECO:0000250}. +P55772 ENTP1_MOUSE Ectonucleoside triphosphate diphosphohydrolase 1 (NTPDase 1) (EC 3.6.1.5) (Ecto-ATP diphosphohydrolase 1) (Ecto-ATPDase 1) (Ecto-ATPase 1) (Ecto-apyrase) (Lymphoid cell activation antigen) (CD antigen CD39) 510 57,205 Active site (1); Chain (1); Disulfide bond (5); Glycosylation (6); Topological domain (3); Transmembrane (2) TRANSMEM 17 37 Helical. {ECO:0000255}.; TRANSMEM 479 499 Helical. {ECO:0000255}. TOPO_DOM 1 16 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 38 478 Extracellular. {ECO:0000255}.; TOPO_DOM 500 510 Cytoplasmic. {ECO:0000255}. FUNCTION: In the nervous system, could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. Could also be implicated in the prevention of platelet aggregation by hydrolyzing platelet-activating ADP to AMP. Hydrolyzes ATP and ADP equally well. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}. +Q9QYE6 GOGA5_MOUSE Golgin subfamily A member 5 (Golgin-84) (Protein Ret-II) (Protein Sumiko) 729 82,368 Chain (1); Coiled coil (1); Compositional bias (1); Initiator methionine (1); Modified residue (6); Sequence conflict (10); Topological domain (2); Transmembrane (1) TRANSMEM 697 717 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 2 696 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 718 729 Lumenal. {ECO:0000255}. FUNCTION: Involved in maintaining Golgi structure. Stimulates the formation of Golgi stacks and ribbons. Involved in intra-Golgi retrograde transport (By similarity). {ECO:0000250}. PTM: Highly phosphorylated during mitosis. Phosphorylation is barely detectable during interphase (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Note=Found throughout the Golgi. {ECO:0000250}. SUBUNIT: Homodimer. Interacts with RAB1A that has been activated by GTP-binding. Interacts with isoform CASP of CUX1 (By similarity). {ECO:0000250}. +P11370 ENV2_MOUSE Retrovirus-related Env polyprotein from Fv-4 locus 679 74,453 Chain (1); Compositional bias (1); Sequence conflict (6) +P60840 ENSA_MOUSE Alpha-endosulfine (ARPP-19e) 121 13,335 Alternative sequence (3); Chain (1); Initiator methionine (1); Modified residue (7); Sequence conflict (2) FUNCTION: Protein phosphatase inhibitor that specifically inhibits protein phosphatase 2A (PP2A) during mitosis. When phosphorylated at Ser-67 during mitosis, specifically interacts with PPP2R2D (PR55-delta) and inhibits its activity, leading to inactivation of PP2A, an essential condition to keep cyclin-B1-CDK1 activity high during M phase. Also acts as a stimulator of insulin secretion by interacting with sulfonylurea receptor (ABCC8), thereby preventing sulfonylurea from binding to its receptor and reducing K(ATP) channel currents (By similarity). {ECO:0000250}. PTM: Phosphorylation at Ser-67 by GWL during mitosis is essential for interaction with PPP2R2D (PR55-delta) and subsequent inactivation of PP2A. Phosphorylated by PKA (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Interacts (when phosphorylated at Ser-67) with PPP2R2D. Interacts with ABCC8. Interacts with SNCA; interaction is disrupted when phosphorylated at Ser-109 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Present in striatum (at protein level). {ECO:0000269|PubMed:11279279}. +P43300 EGR3_MOUSE Early growth response protein 3 (EGR-3) 387 42,635 Chain (1); Sequence conflict (1); Zinc finger (3) FUNCTION: Probable transcription factor involved in muscle spindle development. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q8K0G5 EIPR1_MOUSE EARP and GARP complex-interacting protein 1 (Endosome-associated recycling protein-interacting protein) (Golgi-associated retrograde protein-interacting protein) (Tumor-suppressing STF cDNA 1 protein) (Tumor-suppressing subchromosomal transferable fragment candidate gene 1 protein) 386 43,127 Chain (1); Modified residue (2); Repeat (5); Sequence conflict (1) FUNCTION: Acts as a component of endosomal retrieval machinery that is involved in protein transport from early endosomes to either recycling endosomes or the trans-Golgi network. Mediates the recruitment of Golgi-associated retrograde protein (GARP) complex to the trans-Golgi network and controls early endosome-to-Golgi transport of internalized protein. Promotes the recycling of internalized transferrin receptor (TFRC) to the plasma membrane through interaction with endosome-associated recycling protein (EARP) complex. {ECO:0000250|UniProtKB:Q53HC9}. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q53HC9}. SUBUNIT: Interacts with two multisubunit tethering complexes: EARP composed of VPS50, VPS51, VPS52 and VPS53 subunits and GARP complex composed of VPS51, VPS52, VPS53 and VPS54 subunits. Interacts with SNAP29. {ECO:0000250|UniProtKB:Q53HC9}. +Q61701 ELAV4_MOUSE ELAV-like protein 4 (Hu-antigen D) (HuD) (Paraneoplastic encephalomyelitis antigen HuD) 385 42,368 Alternative sequence (1); Chain (1); Domain (3); Modified residue (3) FUNCTION: May play a role in neuron-specific RNA processing. Protects CDKN1A mRNA from decay by binding to its 3'-UTR. Binds to AU-rich sequences (AREs) of target mRNAs, including VEGF and FOS mRNA (By similarity). {ECO:0000250}. PTM: Methylation at Arg-248 by CARM1 weakens protective binding to the 3'-UTR of CDKN1A mRNA and down-regulates CDKN1A protein expression, thereby maintaining cells in a proliferative state. Methylation is inhibited by NGF, which facilitates neurite outgrowth (By similarity). {ECO:0000250}. SUBUNIT: Component of a TAU mRNP complex, at least composed of IGF2BP1, ELAVL4 and G3BP. {ECO:0000269|PubMed:15086518}. TISSUE SPECIFICITY: Expressed in brain and testis. {ECO:0000269|PubMed:8535975}. +Q9JLJ5 ELOV1_MOUSE Elongation of very long chain fatty acids protein 1 (EC 2.3.1.199) (3-keto acyl-CoA synthase Elovl1) (ELOVL fatty acid elongase 1) (ELOVL FA elongase 1) (Very long chain 3-ketoacyl-CoA synthase 1) (Very long chain 3-oxoacyl-CoA synthase 1) 279 32,678 Chain (1); Modified residue (1); Motif (1); Sequence conflict (1); Transmembrane (7) TRANSMEM 23 43 Helical. {ECO:0000255|HAMAP-Rule:MF_03201}.; TRANSMEM 61 81 Helical. {ECO:0000255|HAMAP-Rule:MF_03201}.; TRANSMEM 110 130 Helical. {ECO:0000255|HAMAP-Rule:MF_03201}.; TRANSMEM 137 154 Helical. {ECO:0000255|HAMAP-Rule:MF_03201}.; TRANSMEM 176 196 Helical. {ECO:0000255|HAMAP-Rule:MF_03201}.; TRANSMEM 203 223 Helical. {ECO:0000255|HAMAP-Rule:MF_03201}.; TRANSMEM 231 251 Helical. {ECO:0000255|HAMAP-Rule:MF_03201}. Lipid metabolism; fatty acid biosynthesis. FUNCTION: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme that exhibits activity toward saturated C18 to C26 acyl-CoA substrates, with the highest activity towards C22:0 acyl-CoA. May participate in the production of both saturated and monounsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. Important for saturated C24:0 and monounsaturated C24:1 sphingolipid synthesis. Indirectly inhibits RPE65 via production of VLCFAs. {ECO:0000255|HAMAP-Rule:MF_03201, ECO:0000269|PubMed:10791983, ECO:0000269|PubMed:23407971}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03201}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03201}. SUBUNIT: Interacts with LASS2, TECR and HSD17B12. {ECO:0000255|HAMAP-Rule:MF_03201}. DOMAIN: The C-terminal di-lysine motif may confer endoplasmic reticulum localization. {ECO:0000255|HAMAP-Rule:MF_03201}. TISSUE SPECIFICITY: Expressed in a broad variety of tissues. Highly expressed in stomach, lung, kidney, skin and intestine. Moderately expressed in white adipose tissue, liver, spleen, brain, brown adipose tissue, heart and muscle. Weakly expressed in testis. {ECO:0000269|PubMed:10791983}. +P0DMC4 ELA_MOUSE Apelin receptor early endogenous ligand (Protein Elabela) (ELA) (Protein Toddler) 54 6,828 Chain (1); Frameshift (1); Sequence conflict (2); Signal peptide (1) FUNCTION: Endogenous ligand for the apelin receptor (APLNR) (By similarity). Hormone required for mesendodermal differentiation, blood vessels formation and heart morphogenesis during early development and for adult cardiovascular homeostasis (PubMed:28371822, PubMed:28854362, PubMed:28890073, PubMed:28663440). Drives internalization of the APLNR (By similarity). Acts as a motogen by promoting mesendodermal cell migration during gastrulation by binding and activating APLNR (By similarity). Acts as an early embryonic regulator of cellular movement with a role in migration and development of cardiac progenitor cells (PubMed:28854362). May act as a chemoattractant for the activation of angioblast migration toward the embryonic midline, i.e. the position of the future vessel formation, during vasculogenesis (By similarity). Positively regulates sinus venosus (SV)-derived endothelial cells migration into the developing heart to promote coronary blood vessel sprouting (PubMed:28890073). Plays a role in placental vascular development; promotes placental trophoblast invasion and spiral artery remodeling in the uterus (PubMed:28663440). Involved in the regulation of maternal cardiovascular homeostasis to prevent gestational hypertension and for potent cardioprotective functions during heart failure (PubMed:28371822, PubMed:28663440). Mediates myocardial contractility in an ERK1/2-dependent manner (By similarity). {ECO:0000250|UniProtKB:P0DMC2, ECO:0000250|UniProtKB:P0DMC3, ECO:0000250|UniProtKB:P0DP76, ECO:0000269|PubMed:28371822, ECO:0000269|PubMed:28663440, ECO:0000269|PubMed:28854362, ECO:0000269|PubMed:28890073}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28663440}. Secreted, extracellular space {ECO:0000269|PubMed:28663440}. Note=Found in blood plasma (By similarity). Found in serum of pregnant mice, peaking at midgestation; indicating a maternal and zygotic origin of circulating APELA during pregnancy (PubMed:28663440). {ECO:0000250|UniProtKB:P0DMC3, ECO:0000269|PubMed:28663440}. SUBUNIT: Interacts with APLNR. {ECO:0000250|UniProtKB:P0DMC3}. TISSUE SPECIFICITY: Expressed in the placenta (PubMed:28663440). Expressed in syncytiotrophoblasts of the placenta labyrinth at 10.5 dpc (PubMed:28663440). Expressed in placental chorionic trophoblasts (at protein level) (PubMed:28663440). Expressed in a small population of epiblast cells in the distal half of the embryo at 7 dpc (PubMed:20153842, PubMed:28854362). Expressed in newly formed definitive endoderm cells in the proximal half of the embryo, while it is not present in extra-embryonic endoderm at 7.5 dpc (PubMed:20153842, PubMed:28854362). This expression pattern then changes to the ventral aspect of the developing foregut pocket and the entire hindgut pocket at 8.5 dpc, before becoming restricted to the foregut overlying the heart and the posterior-most hindgut (PubMed:20153842). Not detected in endothelial precursor cells of the yolk sac at 8 dpc (PubMed:28663440). Expressed in extraembryonic tissues as well as in the chorion at 8.25 dpc (PubMed:28854362). Expressed in endometrial stroma of the uterus of pregnant mice at 8.5 dpc (PubMed:28663440). Expressed in the developing heart, caudal neural tube and trophobasts at 9 dpc (PubMed:28663440). Expressed in the chorionic plate of the chorioallantoic placenta at 9 dpc (PubMed:28663440). Expressed in the posterior half of the ventral neural tube at 9.25 dpc (PubMed:20153842). Expressed in trophoblast cells at the periphery of the placenta at 9.5 dpc (PubMed:28854362). Expressed in collecting ducts of the kidney of pregnant mice at 10.5 dpc (PubMed:28663440). Expressed in the epicardium of the developing heart at 11.5 dpc (PubMed:26611206, PubMed:28890073). Expressed weakly in the adult heart (PubMed:26611206). Expressed in endothelial cells and fibroblasts and weakly in cardiomyocytes (PubMed:26611206). {ECO:0000269|PubMed:20153842, ECO:0000269|PubMed:26611206, ECO:0000269|PubMed:28663440, ECO:0000269|PubMed:28854362, ECO:0000269|PubMed:28890073}. +Q3UKU1 ELL2_MOUSE RNA polymerase II elongation factor ELL2 639 72,125 Chain (1); Modified residue (2); Sequence conflict (1) FUNCTION: Elongation factor component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. Component of the little elongation complex (LEC), a complex required to regulate small nuclear RNA (snRNA) gene transcription by RNA polymerase II and III (By similarity). Plays a role in immunoglobulin secretion in plasma cells: directs efficient alternative mRNA processing, influencing both proximal poly(A) site choice and exon skipping, as well as immunoglobulin heavy chain (IgH) alternative processing. Probably acts by regulating histone modifications accompanying transition from membrane-specific to secretory IgH mRNA expression. {ECO:0000250, ECO:0000269|PubMed:19749764, ECO:0000269|PubMed:21832080}. PTM: Ubiquitinated by SIAH1, leading to its degradation by the proteaseome. Interaction with AFF4 stabilizeS ELL2 and prevent ELL2 ubiquitination (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the super elongation complex (SEC), at least composed of EAF1, EAF2, CDK9, MLLT3/AF9, AFF (AFF1 or AFF4), the P-TEFb complex and ELL (ELL, ELL2 or ELL3). Component of the little elongation complex (LEC), at least composed of ELL (ELL, ELL2 or ELL3), ZC3H8, ICE1 and ICE2. Interacts with AFF4; the interaction is direct and leads to stabilize ELL2 and prevent ELL2 ubiquitination. Interacts with EAF1 and EAF2 (By similarity). {ECO:0000250}. +Q8BPU7 ELMO1_MOUSE Engulfment and cell motility protein 1 (Protein ced-12 homolog) 727 83,936 Alternative sequence (5); Chain (1); Domain (2); Modified residue (8); Motif (1); Sequence conflict (2) FUNCTION: Involved in cytoskeletal rearrangements required for phagocytosis of apoptotic cells and cell motility. Acts in association with DOCK1 and CRK. Was initially proposed to be required in complex with DOCK1 to activate Rac Rho small GTPases. May enhance the guanine nucleotide exchange factor (GEF) activity of DOCK1 (By similarity). {ECO:0000250}. PTM: Phosphorylated by HCK. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Translocation to plasma membrane seems to be mediated by DOCK1 and CRK. {ECO:0000250}. SUBUNIT: Interacts directly with the SH3-domain of DOCK1 via its SH3-binding site. Probably forms a heterotrimeric complex with DOCK1 and RAC1 (By similarity). Interacts with PLEKHG6. Interacts with HCK (via SH3 domain) (By similarity). Interacts with ADGRB1 (PubMed:17960134). Interacts with ADGRB3 (By similarity). {ECO:0000250|UniProtKB:Q92556, ECO:0000269|PubMed:17960134}. +Q01776 GNRHR_MOUSE Gonadotropin-releasing hormone receptor (GnRH receptor) (GnRH-R) 327 37,684 Chain (1); Disulfide bond (1); Glycosylation (3); Sequence conflict (1); Topological domain (8); Transmembrane (7) TRANSMEM 39 58 Helical; Name=1. {ECO:0000255}.; TRANSMEM 78 97 Helical; Name=2. {ECO:0000255}.; TRANSMEM 116 137 Helical; Name=3. {ECO:0000255}.; TRANSMEM 165 184 Helical; Name=4. {ECO:0000255}.; TRANSMEM 212 231 Helical; Name=5. {ECO:0000255}.; TRANSMEM 281 299 Helical; Name=6. {ECO:0000255}.; TRANSMEM 306 325 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 38 Extracellular. {ECO:0000255}.; TOPO_DOM 59 77 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 98 115 Extracellular. {ECO:0000255}.; TOPO_DOM 138 164 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 185 211 Extracellular. {ECO:0000255}.; TOPO_DOM 232 280 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 300 305 Extracellular. {ECO:0000255}.; TOPO_DOM 326 327 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for gonadotropin releasing hormone (GnRH) that mediates the action of GnRH to stimulate the secretion of the gonadotropic hormones luteinizing hormone (LH) and follicle-stimulating hormone (FSH). This receptor mediates its action by association with G-proteins that activate a phosphatidylinositol-calcium second messenger system. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Pituitary gland. +Q9R1E6 ENPP2_MOUSE Ectonucleotide pyrophosphatase/phosphodiesterase family member 2 (E-NPP 2) (EC 3.1.4.39) (Autotaxin) (Extracellular lysophospholipase D) (LysoPLD) 862 98,885 Active site (1); Alternative sequence (2); Beta strand (28); Binding site (2); Chain (1); Disulfide bond (15); Domain (2); Glycosylation (4); Helix (43); Metal binding (12); Motif (1); Mutagenesis (25); Propeptide (1); Region (5); Sequence conflict (6); Signal peptide (1); Site (1); Turn (11) FUNCTION: Hydrolyzes lysophospholipids to produce the signaling molecule lysophosphatidic acid (LPA) in extracellular fluids (PubMed:17208043, PubMed:28414242, PubMed:27780639). Major substrate is lysophosphatidylcholine (PubMed:17208043, PubMed:27780639). Also can act on sphingosylphosphorylcholine producing sphingosine-1-phosphate, a modulator of cell motility. Can hydrolyze, in vitro, bis-pNPP, to some extent pNP-TMP, and barely ATP (PubMed:18175805). Involved in several motility-related processes such as angiogenesis and neurite outgrowth. Acts as an angiogenic factor by stimulating migration of smooth muscle cells and microtubule formation. Stimulates migration of melanoma cells, probably via a pertussis toxin-sensitive G protein. May have a role in induction of parturition (By similarity). Possible involvement in cell proliferation and adipose tissue development (Probable). Tumor cell motility-stimulating factor. {ECO:0000250|UniProtKB:Q13822, ECO:0000269|PubMed:17208043, ECO:0000269|PubMed:18175805, ECO:0000269|PubMed:21240269, ECO:0000269|PubMed:27780639, ECO:0000269|PubMed:28414242, ECO:0000305|PubMed:15700135}. PTM: N-glycosylation, but not furin-cleavage, plays a critical role on secretion and on lysoPLD activity. Secretion requires simultaneous glycosylation on Asn-53 and Asn-410, while probable glycosylation of Asn-410 has a preferential role on lysoPLD activity. Not O-glycosylated. {ECO:0000269|PubMed:17208043, ECO:0000269|PubMed:21240269, ECO:0000269|PubMed:23688339}.; PTM: The interdomain disulfide bond between Cys-413 and Cys-805 is essential for catalytic activity. {ECO:0000269|PubMed:19329427}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17208043, ECO:0000269|PubMed:19329427, ECO:0000269|PubMed:21240269}. TISSUE SPECIFICITY: Expressed in brain and adipose tissue. {ECO:0000269|PubMed:18175805}. DISEASE: Note=May contribute to obesity (PubMed:15700135). {ECO:0000269|PubMed:15700135}. +Q9EQG7 ENPP5_MOUSE Ectonucleotide pyrophosphatase/phosphodiesterase family member 5 (E-NPP 5) (NPP-5) (EC 3.1.-.-) 477 54,387 Active site (1); Beta strand (19); Chain (1); Glycosylation (8); Helix (20); Metal binding (7); Mutagenesis (3); Signal peptide (1); Transmembrane (1); Turn (5) TRANSMEM 432 452 Helical. {ECO:0000255}. FUNCTION: Can hydrolyze NAD but cannot hydrolyze nucleotide di- and triphosphates (PubMed:28898552). Lacks lysopholipase D activity. May play a role in neuronal cell communication (By similarity). {ECO:0000250|UniProtKB:P84039, ECO:0000269|PubMed:28898552}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:P84039}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed abundantly in the brain and kidney, and at lower levels in the liver. {ECO:0000269|PubMed:12927778}. +O55026 ENTP2_MOUSE Ectonucleoside triphosphate diphosphohydrolase 2 (NTPDase 2) (EC 3.6.1.-) (CD39 antigen-like 1) (Ecto-ATP diphosphohydrolase 2) (Ecto-ATPDase 2) (Ecto-ATPase 2) 495 54,319 Active site (1); Alternative sequence (2); Chain (1); Disulfide bond (5); Glycosylation (6); Nucleotide binding (1); Sequence conflict (3); Topological domain (3); Transmembrane (2) TRANSMEM 5 25 Helical. {ECO:0000255}.; TRANSMEM 463 483 Helical. {ECO:0000255}. TOPO_DOM 1 4 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 26 462 Extracellular. {ECO:0000255}.; TOPO_DOM 484 495 Cytoplasmic. {ECO:0000255}. FUNCTION: In the nervous system, could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. Hydrolyzes ADP only to a marginal extent (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Isoform Long: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q80TA9 EPG5_MOUSE Ectopic P granules protein 5 homolog 2572 290,801 Chain (1); Coiled coil (1) FUNCTION: Involved in autophagy. May play a role in a late step of autophagy, such as clearance of autophagosomal cargo (By similarity). {ECO:0000250}. +Q8BYW9 EOGT_MOUSE EGF domain-specific O-linked N-acetylglucosamine transferase (EC 2.4.1.255) (Extracellular O-linked N-acetylglucosamine transferase) 527 61,446 Chain (1); Glycosylation (1); Motif (2); Signal peptide (1) FUNCTION: Catalyzes the transfer of a single N-acetylglucosamine from UDP-GlcNAc to a serine or threonine residue in extracellular proteins resulting in their modification with a beta-linked N-acetylglucosamine (O-GlcNAc). Specifically glycosylates the Thr residue located between the fifth and sixth conserved cysteines of folded EGF-like domains. {ECO:0000269|PubMed:22310717}. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138}. TISSUE SPECIFICITY: Widely expressed. Expressed in brain, heart, kidney, lung, skeletal muscles and thymus. Highest expression is observed in lung and the lowest in skeletal muscles. {ECO:0000269|PubMed:22310717}. +P54754 EPHB3_MOUSE Ephrin type-B receptor 3 (EC 2.7.10.1) (Developmental kinase 5) (mDK-5) (Tyrosine-protein kinase receptor SEK-4) 993 109,662 Active site (1); Binding site (1); Chain (1); Compositional bias (1); Disulfide bond (1); Domain (5); Glycosylation (2); Modified residue (1); Motif (1); Nucleotide binding (1); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 555 575 Helical. {ECO:0000255}. TOPO_DOM 30 554 Extracellular. {ECO:0000255}.; TOPO_DOM 576 993 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor tyrosine kinase which binds promiscuously transmembrane ephrin-B family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Generally has an overlapping and redundant function with EPHB2. Like EPHB2, functions in axon guidance during development regulating for instance the neurons forming the corpus callosum and the anterior commissure, 2 major interhemispheric connections between the temporal lobes of the cerebral cortex. In addition to its role in axon guidance plays also an important redundant role with other ephrin-B receptors in development and maturation of dendritic spines and the formation of excitatory synapses. Controls other aspects of development through regulation of cell migration and positioning. This includes angiogenesis, palate development and thymic epithelium development for instance. Forward and reverse signaling through the EFNB2/EPHB3 complex also regulate migration and adhesion of cells that tubularize the urethra and septate the cloaca. Finally, plays an important role in intestinal epithelium differentiation segregating progenitor from differentiated cells in the crypt. {ECO:0000269|PubMed:12408869, ECO:0000269|PubMed:14691139, ECO:0000269|PubMed:15223334, ECO:0000269|PubMed:19598115, ECO:0000269|PubMed:8947026, ECO:0000269|PubMed:9990854}. PTM: Phosphorylated. Autophosphorylates upon ligand-binding. Autophosphorylation on Tyr-609 is required for interaction with SH2 domain-containing proteins (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14691139}; Single-pass type I membrane protein {ECO:0000269|PubMed:14691139}. Cell projection, dendrite {ECO:0000269|PubMed:14691139}. SUBUNIT: Heterotetramer upon binding of the ligand. The heterotetramer is composed of an ephrin dimer and a receptor dimer. Oligomerization is probably required to induce biological responses (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in cells of the retinal ganglion cell layer during retinal axon guidance to the optic disk. Expressed by Paneth and progenitor cells in the crypts of the intestinal epithelium (at protein level). Expressed in myogenic progenitor cells (PubMed:27446912). {ECO:0000269|PubMed:10704386, ECO:0000269|PubMed:12408869, ECO:0000269|PubMed:27446912}. +O35930 GP1BA_MOUSE Platelet glycoprotein Ib alpha chain (GP-Ib alpha) (GPIb-alpha) (GPIbA) (Glycoprotein Ibalpha) (CD antigen CD42b) 734 80,055 Beta strand (13); Chain (1); Disulfide bond (5); Domain (2); Helix (7); Modified residue (3); Repeat (7); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (6) TRANSMEM 613 633 Helical. {ECO:0000255}. TOPO_DOM 17 612 Extracellular. {ECO:0000255}.; TOPO_DOM 634 734 Cytoplasmic. {ECO:0000255}. FUNCTION: GP-Ib, a surface membrane protein of platelets, participates in the formation of platelet plugs by binding to the A1 domain of vWF, which is already bound to the subendothelium. {ECO:0000250}. PTM: O-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Two GP-Ib beta are disulfide-linked to one GP-Ib alpha. GP-IX is complexed with the GP-Ib heterodimer via a non covalent linkage. Interacts with FLNB. Interacts with FLNA (via filamin repeats 4, 9, 12, 17, 19, 21, and 23). {ECO:0000250|UniProtKB:P07359}. +P07321 EPO_MOUSE Erythropoietin 192 21,365 Chain (1); Disulfide bond (1); Glycosylation (3); Signal peptide (1) FUNCTION: Hormone involved in the regulation of erythrocyte proliferation and differentiation and the maintenance of a physiological level of circulating erythrocyte mass. Binds to EPOR leading to EPOR dimerization and JAK2 activation thereby activating specific downstream effectors, including STAT1 and STAT3. {ECO:0000250|UniProtKB:P01588}. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Produced by kidney or liver of adult mammals and by liver of fetal or neonatal mammals. +Q61450 GP49A_MOUSE Mast cell surface glycoprotein Gp49A 303 34,194 Chain (1); Disulfide bond (2); Domain (2); Glycosylation (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 239 260 Helical. {ECO:0000255}. TOPO_DOM 24 238 Extracellular. {ECO:0000255}.; TOPO_DOM 261 303 Cytoplasmic. {ECO:0000255}. FUNCTION: May play a role in cell-cell or cell-cytokine interactions during the development of mast cells. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. +Q8R1L4 ERD23_MOUSE ER lumen protein-retaining receptor 3 (KDEL endoplasmic reticulum protein retention receptor 3) (KDEL receptor 3) 214 25,111 Chain (1); Sequence conflict (1); Topological domain (8); Transmembrane (7) TRANSMEM 3 21 Helical. {ECO:0000255}.; TRANSMEM 36 53 Helical. {ECO:0000255}.; TRANSMEM 62 80 Helical. {ECO:0000255}.; TRANSMEM 97 110 Helical. {ECO:0000255}.; TRANSMEM 118 137 Helical. {ECO:0000255}.; TRANSMEM 150 168 Helical. {ECO:0000255}.; TRANSMEM 179 199 Helical. {ECO:0000255}. TOPO_DOM 1 2 Lumenal. {ECO:0000255}.; TOPO_DOM 22 35 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 54 61 Lumenal. {ECO:0000255}.; TOPO_DOM 81 96 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 111 117 Lumenal. {ECO:0000255}.; TOPO_DOM 138 149 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 169 178 Lumenal. {ECO:0000255}.; TOPO_DOM 200 214 Cytoplasmic. {ECO:0000255}. FUNCTION: Required for the retention of luminal endoplasmic reticulum proteins. Determines the specificity of the luminal ER protein retention system. Also required for normal vesicular traffic through the Golgi. This receptor recognizes K-D-E-L (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. +Q3UNU4 ERIC4_MOUSE Glutamate-rich protein 4 136 15,244 Chain (1); Compositional bias (1); Sequence conflict (1) +P70459 ERF_MOUSE ETS domain-containing transcription factor ERF 551 59,050 Chain (1); Compositional bias (4); Cross-link (3); DNA binding (1); Erroneous initiation (2); Modified residue (15); Sequence conflict (8) FUNCTION: Potent transcriptional repressor that binds to the H1 element of the Ets2 promoter. May regulate other genes involved in cellular proliferation (By similarity). Required for extraembryonic ectoderm differentiation, ectoplacental cone cavity closure, and chorioallantoic attachment. May be important for regulating trophoblast stem cell differentiation. {ECO:0000250, ECO:0000269|PubMed:17502352}. PTM: Phosphorylated by multiple kinases including MAPK1/ERK2 at THR-529. Phosphorylation regulates the activity of ERF (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. TISSUE SPECIFICITY: Expressed along the osteogenic margins of the developing calvarial bones, in a similar distribution to that observed for the master osteogenic regulator RUNX2. {ECO:0000269|PubMed:23354439}. +Q8C0L9 GPCP1_MOUSE Glycerophosphocholine phosphodiesterase GPCPD1 (EC 3.1.4.2) (Glycerophosphodiester phosphodiesterase 5) (Preimplantation protein 4) 675 76,579 Alternative sequence (2); Binding site (1); Chain (1); Compositional bias (1); Domain (2); Erroneous initiation (4); Modified residue (3); Region (1); Sequence conflict (6) FUNCTION: May be involved in the negative regulation of skeletal muscle differentiation, independently of its glycerophosphocholine phosphodiesterase activity. {ECO:0000269|PubMed:20576599}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:20576599}. TISSUE SPECIFICITY: Widely expressed with highest levels in skeletal muscle and heart. {ECO:0000269|PubMed:20576599}. +Q8CIB9 ESCO2_MOUSE N-acetyltransferase ESCO2 (EC 2.3.1.-) (Establishment of cohesion 1 homolog 2) (ECO1 homolog 2) 592 67,273 Chain (1); Erroneous termination (1); Modified residue (3); Sequence conflict (3); Zinc finger (1) FUNCTION: Acetyltransferase required for the establishment of sister chromatid cohesion. Couples the processes of cohesion and DNA replication to ensure that only sister chromatids become paired together. In contrast to the structural cohesins, the deposition and establishment factors are required only during the S phase. Acetylates the cohesin component SMC3. {ECO:0000250|UniProtKB:Q56NI9}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q56NI9}. Chromosome {ECO:0000250|UniProtKB:Q56NI9}. Note=Nuclear in interphase cells, excluded from chromosomes during metaphase but reassociates with chromosomes in telophase. {ECO:0000250|UniProtKB:Q56NI9}. DOMAIN: The N-terminal region seems to be responsible for association with chromosomes, thus excluding any involvement of the Zn finger in this process. {ECO:0000250|UniProtKB:Q56NI9}. +Q3V1V3 ESF1_MOUSE ESF1 homolog (ABT1-associated protein) 845 98,048 Chain (1); Coiled coil (1); Compositional bias (3); Initiator methionine (1); Modified residue (20) FUNCTION: May constitute a novel regulatory system for basal transcription. Negatively regulates ABT1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. SUBUNIT: Interacts with ABT1. Forms a complex with ABT1 and suppresses the ABT1-induced activation of polymerase II-directed transcription in mammalian cells (By similarity). {ECO:0000250}. +A8R0V4 ESP22_MOUSE Exocrine gland-secreted peptide 22 111 12,570 Chain (1); Signal peptide (1) FUNCTION: Pheromone produced by juveniles which activates a small number of vomeronasal organ sensory neurons and exhibits a powerful inhibitory effect on adult male mating behavior. {ECO:0000269|PubMed:24089208}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24089208}. Note=Secreted from the lacrimal gland into tears. {ECO:0000269|PubMed:24089208}. TISSUE SPECIFICITY: Expressed in acinar cells of the lacrimal gland from where it is secreted into tears. Not detected in a range of other tissues tested including other exocrine glands, internal organs and sensory epithelia. {ECO:0000269|PubMed:24089208}. +Q9ET47 ESPN_MOUSE Espin (Ectoplasmic specialization protein) 871 94,497 Alternative sequence (11); Chain (1); Coiled coil (1); Compositional bias (3); Domain (1); Helix (21); Modified residue (9); Repeat (9); Sequence conflict (4); Turn (2) FUNCTION: Multifunctional actin-bundling protein. Plays a major role in regulating the organization, dimension, dynamics and signaling capacities of the actin filament-rich microvilli in the mechanosensory and chemosensory cells (PubMed:14657236, PubMed:15190118). Required for the assembly and stabilization of the stereociliary parallel actin bundles. Plays a crucial role in the formation and maintenance of inner ear hair cell stereocilia (PubMed:21455486). Involved in the elongation of actin in stereocilia (PubMed:19287378, PubMed:22264607). In extrastriolar hair cells, required for targeting MYO3B to stereocilia tips, and for regulation of stereocilia diameter and staircase formation (PubMed:26926603). {ECO:0000269|PubMed:14657236, ECO:0000269|PubMed:15190118, ECO:0000269|PubMed:19287378, ECO:0000269|PubMed:21455486, ECO:0000269|PubMed:22264607, ECO:0000269|PubMed:26926603}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell projection, stereocilium {ECO:0000269|PubMed:26754646}. Cell projection, microvillus. Cell junction.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm, cytoskeleton. Cell projection, dendritic spine.; SUBCELLULAR LOCATION: Isoform 3: Cytoplasm, cytoskeleton. Cell projection, dendritic spine.; SUBCELLULAR LOCATION: Isoform 4: Cytoplasm, cytoskeleton. Cell projection, dendritic spine.; SUBCELLULAR LOCATION: Isoform 5: Cytoplasm, cytoskeleton. Cell projection, dendritic spine.; SUBCELLULAR LOCATION: Isoform 8: Cytoplasm, cytoskeleton. Cell junction. Note=Isoform 8 localizes to parallel actin bundles of ectoplasmic specializations between neighboring Sertoli cells and at sites where Sertoli cells contact the heads of elongate spermatids. SUBUNIT: Monomer (Probable). Binds F-actin in a Ca(2+)-resistant fashion (PubMed:10588661). Interacts (via N-terminus) with BAIAP2 (via SH3-domain) (PubMed:12598619). Interacts with PFN2 (PubMed:15190118). Interacts with MYO3A (via C-terminus) (PubMed:26926603). Interacts with MYO3B (via C-terminus) (PubMed:26926603, PubMed:26785147). {ECO:0000269|PubMed:10588661, ECO:0000269|PubMed:12598619, ECO:0000269|PubMed:15190118, ECO:0000269|PubMed:26785147, ECO:0000269|PubMed:26926603, ECO:0000305}. DOMAIN: The WH2-domain binds actin monomer and mediates actin bundle assembly. {ECO:0000269|PubMed:16569662}. TISSUE SPECIFICITY: Expressed at high concentration in the microvillar parallel actin bundle (PAB) of hair cells stereocilia in the cochlea and vestibular system. Detected also at high levels of a number of other sensory cell types, including taste receptor cells, solitary chemoreceptor cells, vomeronasal sensory neurons and Merkel cells. Isoforms 2, 3, 4 and 5 are expressed in Purkinje cells dendritic spines. Expressed in utricle hair bundles (at protein level) (PubMed:26926603). {ECO:0000269|PubMed:10975527, ECO:0000269|PubMed:12598619, ECO:0000269|PubMed:15190118, ECO:0000269|PubMed:26926603}. +Q3US41 ESRP1_MOUSE Epithelial splicing regulatory protein 1 (RNA-binding motif protein 35A) (RNA-binding protein 35A) 680 75,549 Alternative sequence (6); Chain (1); Domain (3); Erroneous gene model prediction (5); Modified residue (2); Sequence conflict (3) FUNCTION: mRNA splicing factor that regulates the formation of epithelial cell-specific isoforms. Specifically regulates the expression of FGFR2-IIIb, an epithelial cell-specific isoform of FGFR2. Also regulates the splicing of CD44, CTNND1, ENAH, 3 transcripts that undergo changes in splicing during the epithelial-to-mesenchymal transition (EMT). Acts by directly binding specific sequences in mRNAs. Binds the GU-rich sequence motifs in the ISE/ISS-3, a cis-element regulatory region present in the mRNA of FGFR2 (By similarity). Regulates splicing and expression of genes involved in inner ear development, auditory hair cell differentiation, and cell fate specification in the cochlear epithelium (PubMed:29107558). {ECO:0000250|UniProtKB:Q6NXG1, ECO:0000269|PubMed:29107558}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. TISSUE SPECIFICITY: Epithelial cell-specific. Epithelial-specific expression in diverse tissues and organs with particularly notable levels of expression in skin and gastrointestinal epithelia. {ECO:0000269|PubMed:19285943}. +Q8QZR3 EST2A_MOUSE Pyrethroid hydrolase Ces2a (EC 3.1.1.88) (carboxylesterase 2A) 558 61,940 Active site (3); Alternative sequence (1); Chain (1); Disulfide bond (2); Glycosylation (2); Modified residue (2); Sequence conflict (3); Signal peptide (1) FUNCTION: Carboxylesterases that catalyzes the hydrolysis of pyrethroids pesticides. Hydrolyzes permethrin faster than cypermethrin. {ECO:0000269|PubMed:15123619}. +A2A9A2 DMTA2_MOUSE Doublesex- and mab-3-related transcription factor A2 (Doublesex- and mab-3-related transcription factor 5) 531 52,927 Chain (1); Compositional bias (3); DNA binding (1); Sequence conflict (1) FUNCTION: May be involved in sexual development. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00070}. TISSUE SPECIFICITY: Expressed in adult brain and testis, as well as in embryonic ovary, kidney, heart, lung, stomach and brain. {ECO:0000269|PubMed:12609607}. +Q8CGW9 DMRTD_MOUSE Doublesex- and mab-3-related transcription factor C2 (Doublesex- and mab-3-related transcription factor 7) 370 39,095 Chain (1); Compositional bias (1); DNA binding (1) FUNCTION: May be involved in sexual development. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00070}. TISSUE SPECIFICITY: Expressed in testis. Highly expressed in ovary. +Q8BKG4 FZD10_MOUSE Frizzled-10 (Fz-10) (CD antigen CD350) 582 65,318 Chain (1); Disulfide bond (5); Domain (1); Glycosylation (3); Motif (2); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 227 247 Helical; Name=1. {ECO:0000255}.; TRANSMEM 264 284 Helical; Name=2. {ECO:0000255}.; TRANSMEM 313 333 Helical; Name=3. {ECO:0000255}.; TRANSMEM 353 373 Helical; Name=4. {ECO:0000255}.; TRANSMEM 395 415 Helical; Name=5. {ECO:0000255}.; TRANSMEM 445 465 Helical; Name=6. {ECO:0000255}.; TRANSMEM 504 524 Helical; Name=7. {ECO:0000255}. TOPO_DOM 22 226 Extracellular. {ECO:0000255}.; TOPO_DOM 248 263 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 285 312 Extracellular. {ECO:0000255}.; TOPO_DOM 334 352 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 374 394 Extracellular. {ECO:0000255}.; TOPO_DOM 416 444 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 466 503 Extracellular. {ECO:0000255}.; TOPO_DOM 525 582 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for Wnt proteins (PubMed:15923619). Functions in the canonical Wnt/beta-catenin signaling pathway (PubMed:15923619). The canonical Wnt/beta-catenin signaling pathway leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues (Probable). {ECO:0000269|PubMed:15923619}. PTM: Ubiquitinated by ZNRF3, leading to its degradation by the proteasome. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15923619}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Interacts with MYOC (By similarity). Interacts with WNT7B (PubMed:15923619). {ECO:0000250|UniProtKB:Q9ULW2, ECO:0000269|PubMed:15923619}. DOMAIN: Lys-Thr-X-X-X-Trp motif interacts with the PDZ domain of Dvl (Disheveled) family members and is involved in the activation of the Wnt/beta-catenin signaling pathway. {ECO:0000250}.; DOMAIN: The FZ domain is involved in binding with Wnt ligands. {ECO:0000250}. +A2AC93 DNAI2_MOUSE Dynein intermediate chain 2, axonemal (Axonemal dynein intermediate chain 2) 623 70,968 Alternative sequence (1); Chain (1); Compositional bias (1); Erroneous gene model prediction (1); Repeat (5) FUNCTION: Part of the dynein complex of respiratory cilia. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250}. SUBUNIT: Consists of at least two heavy chains and a number of intermediate and light chains (Probable). Interacts with DNAAF2 (PubMed:19052621). Interacts with PIH1D3 (PubMed:24421334). Interacts with HEATR2; probably involved in outer arm dynein assembly (By similarity). {ECO:0000250|UniProtKB:Q9GZS0, ECO:0000269|PubMed:19052621, ECO:0000269|PubMed:24421334, ECO:0000305}. TISSUE SPECIFICITY: Predominantly expressed in ovary, testis and lung. {ECO:0000269|PubMed:18547164}. +Q61086 FZD3_MOUSE Frizzled-3 (Fz-3) (mFz3) 666 76,208 Chain (1); Disulfide bond (5); Domain (1); Glycosylation (3); Motif (1); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 206 226 Helical; Name=1. {ECO:0000255}.; TRANSMEM 238 258 Helical; Name=2. {ECO:0000255}.; TRANSMEM 289 309 Helical; Name=3. {ECO:0000255}.; TRANSMEM 329 349 Helical; Name=4. {ECO:0000255}.; TRANSMEM 375 395 Helical; Name=5. {ECO:0000255}.; TRANSMEM 421 441 Helical; Name=6. {ECO:0000255}.; TRANSMEM 478 498 Helical; Name=7. {ECO:0000255}. TOPO_DOM 23 205 Extracellular. {ECO:0000255}.; TOPO_DOM 227 237 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 259 288 Extracellular. {ECO:0000255}.; TOPO_DOM 310 328 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 350 374 Extracellular. {ECO:0000255}.; TOPO_DOM 396 420 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 442 477 Extracellular. {ECO:0000255}.; TOPO_DOM 499 666 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for Wnt proteins. Most of frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. Activation by Wnt5A stimulates PKC activity via a G-protein-dependent mechanism. Involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues. Plays a role in controlling early axon growth and guidance processes necessary for the formation of a subset of central and peripheral major fiber tracts. Required for the development of major fiber tracts in the central nervous system, including: the anterior commissure, the corpus callosum, the thalamocortical, corticothalamic and nigrostriatal tracts, the corticospinal tract, the fasciculus retroflexus, the mammillothalamic tract, the medial lemniscus, and ascending fiber tracts from the spinal cord to the brain. In the peripheral nervous system, controls axon growth in distinct populations of cranial and spinal motor neurons, including the facial branchimotor nerve, the hypoglossal nerve, the phrenic nerve, and motor nerves innervating dorsal limbs. Involved in the migration of cranial neural crest cells. May also be implicated in the transmission of sensory information from the trunk and limbs to the brain. Controls commissural sensory axons guidance after midline crossing along the anterior-posterior axis in the developing spinal cord in a Wnt-dependent signaling pathway. Together with FZD6, is involved in the neural tube closure and plays a role in the regulation of the establishment of planar cell polarity (PCP), particularly in the orientation of asymmetric bundles of stereocilia on the apical faces of a subset of auditory and vestibular sensory cells located in the inner ear. Promotes neurogenesis by maintaining sympathetic neuroblasts within the cell cycle in a beta-catenin-dependent manner. {ECO:0000269|PubMed:12351730, ECO:0000269|PubMed:14671310, ECO:0000269|PubMed:16407530, ECO:0000269|PubMed:16495441, ECO:0000269|PubMed:21325504, ECO:0000269|PubMed:24347548, ECO:0000269|PubMed:24799694}. PTM: Ubiquitinated by ZNRF3, leading to its degradation by the proteasome. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell surface {ECO:0000269|PubMed:16495441}. Apical cell membrane {ECO:0000269|PubMed:16495441}; Multi-pass membrane protein. Note=Colocalizes with FZD6 at the apical face of the cell. {ECO:0000269|PubMed:16495441}. SUBUNIT: Interacts with VANGL2. {ECO:0000269|PubMed:16687519}. DOMAIN: Lys-Thr-X-X-X-Trp motif interacts with the PDZ domain of Dvl (Disheveled) family members and is involved in the activation of the Wnt/beta-catenin signaling pathway. {ECO:0000250}.; DOMAIN: The FZ domain is involved in binding with Wnt ligands. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the cortex, diencephalon, rostral brainstem and little or no staining is seen in the striatum or cerebellum. Expressed in both hair cells and supporting cells in the utricle, saccule, cristae and the organ of Corti in the inner ear (at protein level). Highly expressed in the CNS. In skin, it is restricted to the epidermis and to the developing hair follicle. {ECO:0000269|PubMed:11407985, ECO:0000269|PubMed:12351730, ECO:0000269|PubMed:16495441, ECO:0000269|PubMed:8626800}. +Q61214 DYR1A_MOUSE Dual specificity tyrosine-phosphorylation-regulated kinase 1A (EC 2.7.12.1) (Dual specificity YAK1-related kinase) (MP86) (Protein kinase minibrain homolog) (MNBH) 763 85,494 Active site (1); Binding site (1); Chain (1); Compositional bias (5); Domain (1); Modified residue (16); Motif (1); Nucleotide binding (2) FUNCTION: Dual-specificity kinase which possesses both serine/threonine and tyrosine kinase activities. May play a role in a signaling pathway regulating nuclear functions of cell proliferation. Modulates alternative splicing by phosphorylating the splice factor SRSF6 (By similarity). Exhibits a substrate preference for proline at position P+1 and arginine at position P-3. Has pro-survival function and negatively regulates the apoptotic process. Promotes cell survival upon genotoxic stress through phosphorylation of SIRT1. This in turn inhibits TP53 activity and apoptosis (PubMed:20167603). {ECO:0000250|UniProtKB:Q9NR20, ECO:0000269|PubMed:20123978, ECO:0000269|PubMed:20167603}. PTM: Autophosphorylated on numerous tyrosine residues. Can also autophosphorylate on serine and threonine residues (in vitro) (By similarity). {ECO:0000250|UniProtKB:Q13627}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:9070862}. SUBUNIT: Interacts with RANBP9 (By similarity). Interacts with RAD54L2/ARIP4 (PubMed:15199138). Interacts with WDR68 (By similarity). Interacts with CRY2 (PubMed:20123978). Interacts with SIRT1 (PubMed:20167603). {ECO:0000250|UniProtKB:Q13627, ECO:0000269|PubMed:15199138, ECO:0000269|PubMed:20123978, ECO:0000269|PubMed:20167603, ECO:0000269|PubMed:9070862}. DOMAIN: The polyhistidine repeats act as targeting signals to nuclear speckles. {ECO:0000250|UniProtKB:Q13627}. TISSUE SPECIFICITY: Detected in brain (at protein level). Expressed in a variety of embryonic and adult tissues. Expressed abundantly in neurons of the brain, spinal cord, and retina in developing embryos. {ECO:0000269|PubMed:22998443, ECO:0000269|PubMed:8975710}. +P56387 DYLT3_MOUSE Dynein light chain Tctex-type 3 (Protein 91/23) (T-complex-associated testis-expressed 1-like) 116 12,958 Chain (1); Modified residue (1) FUNCTION: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Probably binds BUB3 as part of transport cargo. Required for the efficient progression through mitosis. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. SUBUNIT: Homodimer. The cytoplasmic dynein 1 complex consists of two catalytic heavy chains (HCs) and a number of non-catalytic subunits presented by intermediate chains (ICs), light intermediate chains (LICs) and light chains (LCs); the composition seems to vary in respect to the IC, LIC and LC composition. The heavy chain homodimer serves as a scaffold for the probable homodimeric assembly of the respective non-catalytic subunits. The ICs and LICs bind directly to the HC dimer and the LCs assemble on the IC dimer. DYNLT1 and DYNLT3 compete for association with dynein IC (DYNC1I1 or DYNC1I2). Self-associates. Interacts with DYNC1I1 and DYNC1I2. Interacts with BUB3. Interacts with SATB1 in nucleus to form complex with matrix attachment regions (MARs) of DNA (By similarity). {ECO:0000250}. +P39053 DYN1_MOUSE Dynamin-1 (EC 3.6.5.5) 867 97,803 Alternative sequence (5); Chain (1); Domain (3); Erroneous initiation (1); Modified residue (14); Nucleotide binding (3); Region (5); Sequence conflict (9) FUNCTION: Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP. Most probably involved in vesicular trafficking processes. Involved in receptor-mediated endocytosis (By similarity). {ECO:0000250}. PTM: Phosphorylated in response to EGF stimulation in cells expressing truncated EGFR. {ECO:0000269|PubMed:11956154}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11082044}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11082044}. Note=Microtubule-associated. SUBUNIT: Binds SH3GL1, SH3GL2 and SH3GL3 (By similarity). Interacts with SNX9 (By similarity). Interacts with PHOCN. Interacts with MYO1E (via SH3 domain). Interacts with SNX33 (via SH3 domain) (By similarity). Interacts with CAV1 and SH3GLB1. Interacts with PACSIN1, PACSIN2 and PACSIN3. Interacts with UNC119; leading to a decrease of DNM1 GTPase activity. Interacts with DIAPH1 (By similarity). Interacts with AMPH, BIN1 AND SYNJ1 (By similarity). {ECO:0000250|UniProtKB:P21575, ECO:0000250|UniProtKB:Q05193, ECO:0000269|PubMed:11082044, ECO:0000269|PubMed:11956154, ECO:0000269|PubMed:12456676, ECO:0000269|PubMed:19781630}. +Q5U4C9 DYRK2_MOUSE Dual specificity tyrosine-phosphorylation-regulated kinase 2 (EC 2.7.12.1) 599 66,556 Active site (1); Binding site (1); Chain (1); Domain (1); Modified residue (6); Motif (1); Nucleotide binding (2) FUNCTION: Serine/threonine-protein kinase involved in the regulation of the mitotic cell cycle, cell proliferation, apoptosis, organization of the cytoskeleton and neurite outgrowth. Functions in part via its role in ubiquitin-dependent proteasomal protein degradation. Functions downstream of ATM and phosphorylates p53/TP53 at 'Ser-46', and thereby contributes to the induction of apoptosis in response to DNA damage. Phosphorylates NFATC1, and thereby inhibits its accumulation in the nucleus and its transcription factor activity. Phosphorylates EIF2B5 at 'Ser-544', enabling its subsequent phosphorylation and inhibition by GSK3B. Likewise, phosphorylation of NFATC1, CRMP2/DPYSL2 and CRMP4/DPYSL3 promotes their subsequent phosphorylation by GSK3B. May play a general role in the priming of GSK3 substrates. Inactivates GYS1 by phosphorylation at 'Ser-641', and potentially also a second phosphorylation site, thus regulating glycogen synthesis. Mediates EDVP E3 ligase complex formation and is required for the phosphorylation and subsequent degradation of KATNA1. Phosphorylates TERT at 'Ser-457', promoting TERT ubiquitination by the EDVP complex. Phosphorylates SIAH2, and thereby increases its ubiquitin ligase activity. Promotes the proteasomal degradation of MYC and JUN, and thereby regulates progress through the mitotic cell cycle and cell proliferation. Promotes proteasomal degradation of GLI2 and GLI3, and thereby plays a role in smoothened and sonic hedgehog signaling. Phosphorylates CRMP2/DPYSL2, CRMP4/DPYSL3, DCX, EIF2B5, EIF4EBP1, GLI2, GLI3, GYS1, JUN, MDM2, MYC, NFATC1, p53/TP53, TAU/MAPT and KATNA1. Can phosphorylate histone H1, histone H3 and histone H2B (in vitro). Can phosphorylate CARHSP1 (in vitro) (By similarity). Plays a role in cytoskeleton organization and neurite outgrowth via its phosphorylation of DCX. {ECO:0000250, ECO:0000269|PubMed:22359282}. PTM: Autophosphorylates cotranslationally on the second tyrosine residue in the Tyr-X-Tyr motif in the activation loop, but once mature, does not have any protein tyrosine kinase activity. Phosphorylated at Thr-104 and Ser-440 by ATM in response to genotoxic stress.; PTM: Under normal conditions, polyubiquitinated in the nucleus by MDM2, leading to its proteasomal degradation. Phosphorylation on Thr-104 and Ser-440 by ATM in response to genotoxic stress disrupts MDM2 binding and prevents MDM2-mediated ubiquitination and subsequent proteasomal degradation. Polyubiquitinated by SIAH2, leading to its proteasomal degradation. Polyubiquitinated by SIAH2 occurs under normal conditions, and is enhanced in response to hypoxia. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20167603}. Nucleus {ECO:0000250|UniProtKB:Q92630}. Note=Translocates into the nucleus following DNA damage. {ECO:0000250|UniProtKB:Q92630}. SUBUNIT: Component of an E3 ligase complex containing DYRK2, EDD/UBR5, DDB1 and DCAF1 (EDVP complex). Interacts directly with EDD/UBR5, DDB1 and DCAF1. Interacts with SIAH2 and MDM2. Interacts with MAP3K10 and NFATC1. May also interact with CCNL2 (By similarity). {ECO:0000250}. +Q8VE33 GD1L1_MOUSE Ganglioside-induced differentiation-associated protein 1-like 1 (GDAP1-L1) 370 42,318 Chain (1); Domain (2) +Q8BFR5 EFTU_MOUSE Elongation factor Tu, mitochondrial 452 49,508 Alternative sequence (1); Chain (1); Domain (1); Modified residue (10); Nucleotide binding (3); Region (5); Transit peptide (1) FUNCTION: Promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. Plays also a role in the regulation of autophagy and innate immunity. Recruits ATG5-ATG12 and NLRX1 at mitochondria and serves as a checkpoint of the RIG-I/DDX58-MAVS pathway. In turn, inhibits RLR-mediated type I interferon while promoting autophagy. {ECO:0000250|UniProtKB:P49411}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P49411}. SUBUNIT: Interacts with NLRX1. Interacts with ATG16L1. {ECO:0000250|UniProtKB:P49411}. +Q91YE3 EGLN1_MOUSE Egl nine homolog 1 (EC 1.14.11.29) (Hypoxia-inducible factor prolyl hydroxylase 2) (HIF-PH2) (HIF-prolyl hydroxylase 2) (HPH-2) (Prolyl hydroxylase domain-containing protein 2) (PHD2) (SM-20) 400 43,111 Binding site (1); Chain (1); Domain (1); Erroneous initiation (1); Initiator methionine (1); Metal binding (3); Modified residue (8); Region (2); Sequence conflict (1); Zinc finger (1) FUNCTION: Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both HIF1A and HIF1B. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes. EGLN1 is the most important isozyme under normoxia and, through regulating the stability of HIF1, involved in various hypoxia-influenced processes such as angiogenesis in retinal and cardiac functionality. Target proteins are preferentially recognized via a LXXLAP motif. {ECO:0000269|PubMed:18096761, ECO:0000269|PubMed:18500250, ECO:0000269|PubMed:21435465}. PTM: S-nitrosylation inhibits the enzyme activity up to 60% under aerobic conditions. Chelation of Fe(2+) has no effect on the S-nitrosylation. It is uncertain whether nitrosylation occurs on Cys-300 or Cys-303. {ECO:0000250|UniProtKB:Q9GZT9}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9GZT9}. Nucleus {ECO:0000250|UniProtKB:Q9GZT9}. Note=Mainly cytoplasmic. Shuttles between the nucleus and cytoplasm. Nuclear export requires functional XPO1. {ECO:0000250|UniProtKB:Q9GZT9}. SUBUNIT: Monomer. Interacts with ING4; the interaction inhibits the hydroxylation of HIF alpha proteins. Interacts with PTGES3 (via PXLE motif); thereby recruiting EGLN1 to the HSP90 pathway to facilitate HIF alpha proteins hydroxylation. Interacts with LIMD1. Found in a complex composed of LIMD1, VHL, EGLN1/PHD2, ELOB and CUL2. Interacts with EPAS1. Interacts with CBFA2T3 and HIF1A. {ECO:0000250|UniProtKB:Q9GZT9}. DOMAIN: The beta(2)beta(3) 'finger-like' loop domain is important for substrate (HIFs' CODD/NODD) selectivity. {ECO:0000250|UniProtKB:Q9GZT9}. TISSUE SPECIFICITY: Expressed in heart, brain liver, skeletal muscle and kidney. Low levels were detected in the lung. Constitutively expressed during differentiation of C2C12 skeletal myocytes. {ECO:0000269|PubMed:12234095}. +Q91UZ4 EGLN3_MOUSE Egl nine homolog 3 (EC 1.14.11.29) (Hypoxia-inducible factor prolyl hydroxylase 3) (HIF-PH3) (HIF-prolyl hydroxylase 3) (HPH-3) (Prolyl hydroxylase domain-containing protein 3) (PHD3) (SM-20) 239 27,302 Binding site (1); Chain (1); Domain (1); Erroneous initiation (1); Metal binding (3); Region (2); Sequence conflict (3) FUNCTION: Plays a crucial role in DNA damage response (DDR) by hydroxylating TELO2, promoting its interaction with ATR which is required for activation of the ATR/CHK1/p53 pathway (By similarity). Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both HIF1A and HIF2A. Hydroxylation on the NODD site by EGLN3 appears to require prior hydroxylation on the CODD site. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes. ELGN3 is the most important isozyme in limiting physiological activation of HIFs (particularly HIF2A) in hypoxia. Also hydroxylates PKM in hypoxia, limiting glycolysis. Under normoxia, hydroxylates and regulates the stability of ADRB2. Regulator of cardiomyocyte and neuronal apoptosis. In cardiomyocytes, inhibits the anti-apoptotic effect of BCL2 by disrupting the BAX-BCL2 complex. In neurons, has a NGF-induced proapoptotic effect, probably through regulating CASP3 activity. Also essential for hypoxic regulation of neutrophilic inflammation. Target proteins are preferentially recognized via a LXXLAP motif. {ECO:0000250, ECO:0000269|PubMed:21317538}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Colocalizes with WDR83 in the cytoplasm. {ECO:0000250}. SUBUNIT: Interacts with ADRB2; the interaction hydroxylates ADRB2 facilitating its ubiquitination by the VHL-E3 ligase complex. Interacts with PKM; the interaction hydroxylates PKM in hypoxia. Interacts with WDR83; the interaction leads to almost complete elimination of HIF-mediated reporter activity (By similarity). Interacts with BCL2 (via its BH4 domain); the interaction disrupts the BAX-BCL4 complex inhibiting the anti-apoptotic activity of BCL2. Interacts with LIMD1, WTIP and AJUBA (By similarity). {ECO:0000250}. DOMAIN: The Beta(2)beta(3) 'finger-like' loop domain is important for substrate (HIFs' CODD/NODD) selectivity. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in cardiac and smooth muscle. Also high expression in brain, skeletal muscle and kidney. Low levels in lung. {ECO:0000269|PubMed:12234095}. +Q63961 EGLN_MOUSE Endoglin (Cell surface MJ7/18 antigen) (CD antigen CD105) 653 70,021 Chain (1); Compositional bias (1); Disulfide bond (8); Domain (1); Glycosylation (5); Modified residue (2); Region (5); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 582 606 Helical. {ECO:0000255}. TOPO_DOM 27 581 Extracellular. {ECO:0000255}.; TOPO_DOM 607 653 Cytoplasmic. {ECO:0000255}. FUNCTION: Vascular endothelium glycoprotein that plays an important role in the regulation of angiogenesis (PubMed:10625534). Required for normal structure and integrity of adult vasculature (By similarity). Regulates the migration of vascular endothelial cells (PubMed:17540773). Required for normal extraembryonic angiogenesis and for embryonic heart development (PubMed:10625534). May regulate endothelial cell shape changes in response to blood flow, which drive vascular remodeling and establishment of normal vascular morphology during angiogenesis (PubMed:28530658). May play a role in the binding of endothelial cells to integrins. Acts as TGF-beta coreceptor and is involved in the TGF-beta/BMP signaling cascade that ultimately leads to the activation of SMAD transcription factors (PubMed:23300529). Required for GDF2/BMP9 signaling through SMAD1 in endothelial cells and modulates TGFB1 signaling through SMAD3 (By similarity). {ECO:0000250|UniProtKB:P17813, ECO:0000269|PubMed:10625534, ECO:0000269|PubMed:17540773, ECO:0000269|PubMed:23300529, ECO:0000269|PubMed:28530658}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8125301}; Single-pass type I membrane protein {ECO:0000305|PubMed:8125301}. SUBUNIT: Homodimer; disulfide-linked (PubMed:8194490). Forms a heteromeric complex with the signaling receptors for transforming growth factor-beta: TGFBR1 and/or TGFBR2. Interacts with TGFB1 (PubMed:8194490). It is able to bind TGFB1 and TGFB2 with high affinity, but not TGFB3. Interacts with GDF2, forming a heterotetramer with a 2:2 stoichiometry. Interacts with ACVRL1. Can form a heteromeric complex with GDF2 and ACVRL1. Interacts with BMP10. Interacts with TCTEX1D4. Interacts with ARRB2. {ECO:0000250|UniProtKB:P17813, ECO:0000269|PubMed:8194490}. DOMAIN: The ZP domain mediates dimerization. {ECO:0000250|UniProtKB:P17813}.; DOMAIN: The N-terminal OR region is composed of two intertwined domains (OR1 and OR2) with a common, novel fold. Each contains 12 beta-strands that form a parallel beta-helix-like structure, plus a single alpha-helix. The OR1 region mediates interaction with GDF2. {ECO:0000250|UniProtKB:P17813}. TISSUE SPECIFICITY: Detected on blood vessels (at protein level) (PubMed:8194490). Detected on adult pulmonary artery, capillaries supporting the heart muscle and lung alveolar capillary endothelial cells (PubMed:10625534). Endoglin is restricted to endothelial cells in all tissues except bone marrow and is also found in stromal cells within the connective tissue of intestine, stomach, heart, skeletal muscle, uterus, ovary, oviduct, testis and thymus (PubMed:8194490). {ECO:0000269|PubMed:8194490}. +Q9WVK4 EHD1_MOUSE EH domain-containing protein 1 (PAST homolog 1) (mPAST1) 534 60,603 Binding site (2); Calcium binding (1); Chain (1); Coiled coil (1); Domain (3); Modified residue (3); Mutagenesis (2); Nucleotide binding (1); Region (5) FUNCTION: ATP- and membrane-binding protein that controls membrane reorganization/tubulation upon ATP hydrolysis. In vitro causes vesiculation of endocytic membranes (By similarity). Acts in early endocytic membrane fusion and membrane trafficking of recycling endosomes (PubMed:15930129, PubMed:20159556). Recruited to endosomal membranes upon nerve growth factor stimulation, indirectly regulates neurite outgrowth (By similarity). Plays a role in myoblast fusion (PubMed:21177873). Involved in the unidirectional retrograde dendritic transport of endocytosed BACE1 and in efficient sorting of BACE1 to axons implicating a function in neuronal APP processing (PubMed:24373286). Plays a role in the formation of the ciliary vesicle (CV), an early step in cilium biogenesis. Proposed to be required for the fusion of distal appendage vesicles (DAVs) to form the CV by recruiting SNARE complex component SNAP29. Is required for recruitment of transition zone proteins CEP290, RPGRIP1L, TMEM67 and B9D2, and of IFT20 following DAV reorganization before Rab8-dependent ciliary membrane extension. Required for the loss of CCP110 form the mother centriole essential for the maturation of the basal body during ciliogenesis (By similarity). {ECO:0000250|UniProtKB:Q641Z6, ECO:0000250|UniProtKB:Q9H4M9, ECO:0000269|PubMed:15930129, ECO:0000269|PubMed:20159556, ECO:0000269|PubMed:21177873, ECO:0000269|PubMed:24373286}. SUBCELLULAR LOCATION: Recycling endosome membrane {ECO:0000250|UniProtKB:Q9H4M9}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Early endosome membrane {ECO:0000250|UniProtKB:Q9H4M9}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:21177873}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle {ECO:0000269|PubMed:24373286}. Cell projection, cilium membrane {ECO:0000250|UniProtKB:Q9H4M9}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Preferentially associates with tubular recycling endosomes (By similarity). Colocalizes with FER1L5 at plasma membrane in myoblasts and myotubes (PubMed:21177873). Localizes to the ciliary pocket from where the cilium protrudes (By similarity). Colocalizes with BACE1 in tubulovesicular cytoplasmic membranes. Colocalizes with BACE1 and APP amyloid beta proteins in hippocampal mossy fiber terminals. {ECO:0000250|UniProtKB:Q9H4M9, ECO:0000269|PubMed:21177873, ECO:0000269|PubMed:24373286}. SUBUNIT: Homooligomer, and heterooligomer with EHD2, EHD3 and EHD4, ATP-binding is required for heterooligomerization (By similarity). Interacts (via EH domain) with MICALL1 (via NPF1 motif); the interaction is direct and recruits EHD1 to membranes (PubMed:23572513). Interacts with RAB35; the interaction is indirect through MICALL1 and recruits EHD1 to membranes (PubMed:23572513). Interacts (via EH domain) with PACSIN2 (via NPF motifs); regulates localization to tubular recycling endosome membranes (PubMed:15930129). Interacts with PACSIN1 (PubMed:15930129). Interacts with RAB8A (By similarity). Interacts with FER1L5 (via second C2 domain) (PubMed:21177873). Interacts with MYOF (PubMed:21177873). Interacts with ZFYVE20 (By similarity). Interacts (via EH domain) with RAB11FIP2 (By similarity). {ECO:0000250|UniProtKB:Q9H4M9, ECO:0000269|PubMed:15930129, ECO:0000269|PubMed:21177873, ECO:0000269|PubMed:23572513}. DOMAIN: The EH domain interacts with Asn-Pro-Phe (NPF) motifs of target proteins. {ECO:0000269|PubMed:15930129}. TISSUE SPECIFICITY: Highly expressed in testis. Also expressed in kidney, heart, intestine, and brain. {ECO:0000269|PubMed:10395801}. +P08046 EGR1_MOUSE Early growth response protein 1 (EGR-1) (Nerve growth factor-induced protein A) (NGFI-A) (Transcription factor Zif268) (Zinc finger protein Krox-24) 533 56,590 Beta strand (5); Chain (1); Compositional bias (1); Cross-link (1); Helix (4); Sequence conflict (4); Site (9); Turn (2); Zinc finger (3) FUNCTION: Transcriptional regulator (PubMed:8336701, PubMed:8703054, PubMed:15958557). Recognizes and binds to the DNA sequence 5'-GCG(T/G)GGGCG-3'(EGR-site) in the promoter region of target genes (PubMed:8703054, PubMed:15958557, PubMed:2028256, PubMed:8939742). Binds double-stranded target DNA, irrespective of the cytosine methylation status (By similarity). Regulates the transcription of numerous target genes, and thereby plays an important role in regulating the response to growth factors, DNA damage, and ischemia (PubMed:11100120, PubMed:15958557). Plays a role in the regulation of cell survival, proliferation and cell death (PubMed:15265859, PubMed:15958557). Activates expression of p53/TP53 and TGFB1, and thereby helps prevent tumor formation (PubMed:15958557). Required for normal progress through mitosis and normal proliferation of hepatocytes after partial hepatectomy (PubMed:15265859). Mediates responses to ischemia and hypoxia; regulates the expression of proteins such as IL1B and CXCL2 that are involved in inflammatory processes and development of tissue damage after ischemia (PubMed:11100120). Regulates biosynthesis of luteinizing hormone (LHB) in the pituitary (PubMed:8703054). Regulates the amplitude of the expression rhythms of clock genes: ARNTL/BMAL1, PER2 and NR1D1 in the liver via the activation of PER1 (clock repressor) transcription (PubMed:26471974). Regulates the rhythmic expression of core-clock gene ARNTL/BMAL1 in the suprachiasmatic nucleus (SCN) (PubMed:29138967). {ECO:0000250|UniProtKB:P18146, ECO:0000269|PubMed:11100120, ECO:0000269|PubMed:15265859, ECO:0000269|PubMed:15958557, ECO:0000269|PubMed:2028256, ECO:0000269|PubMed:26471974, ECO:0000269|PubMed:29138967, ECO:0000269|PubMed:8336701, ECO:0000269|PubMed:8703054, ECO:0000269|PubMed:8939742, ECO:0000305}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11100120, ECO:0000269|PubMed:15958557, ECO:0000269|PubMed:8336701}. Cytoplasm {ECO:0000250|UniProtKB:P18146}. SUBUNIT: Interacts with SNAI1 and SP1 upon 12-O-tetradecanoylphorbol-13-acetate (TPA) induction. {ECO:0000250|UniProtKB:P18146}. DOMAIN: Binds to DNA motifs with the sequence 5'-GCG(T/G)GGGCG-3' via its C2H2-type zinc fingers (PubMed:1740423, PubMed:8336701, PubMed:2028256, PubMed:8939742). The first, most N-terminal zinc finger binds to the 3'-GCG motif, the middle zinc finger interacts with the central TGG motif, and the C-terminal zinc finger binds to the 5'-GCG motif (PubMed:2028256, PubMed:8939742). Binds double-stranded target DNA, irrespective of the cytosine methylation status. Has reduced affinity for target DNA where the cytosines have been oxidized to 5-hydroxymethylcytosine. Does not bind target DNA where the cytosines have been oxidized to 5-formylcytosine or 5-carboxylcytosine (By similarity). {ECO:0000250|UniProtKB:P18146, ECO:0000269|PubMed:1740423, ECO:0000269|PubMed:2028256, ECO:0000269|PubMed:8939742}. TISSUE SPECIFICITY: Detected in lung vasculature and in mononuclear phagocytes (PubMed:11100120). Detected in liver (at protein level) (PubMed:15265859). Detected in lung vasculature and in mononuclear phagocytes (PubMed:11100120). Expressed in the liver in a circadian manner (PubMed:26471974). {ECO:0000269|PubMed:11100120, ECO:0000269|PubMed:15265859, ECO:0000269|PubMed:26471974}. +P08152 EGR2_MOUSE E3 SUMO-protein ligase EGR2 (EC 2.3.2.-) (E3 SUMO-protein transferase ERG2) (Early growth response protein 2) (EGR-2) (Zinc finger protein Krox-20) 470 49,819 Alternative sequence (1); Chain (1); Compositional bias (1); Mutagenesis (3); Zinc finger (3) Protein modification; protein sumoylation. FUNCTION: Sequence-specific DNA-binding transcription factor. Binds to two specific DNA sites located in the promoter region of HOXA4. Binds to the promoter region of ERBB2. May play a role in the regulation of hindbrain segmentation, might act in combination with the Hox network to specify odd and even rhombomeres, and might participate in the control of the expression of some of the homeobox containing genes. {ECO:0000269|PubMed:1674431, ECO:0000269|PubMed:17938205, ECO:0000269|PubMed:1969796}.; FUNCTION: E3 SUMO-protein ligase helping SUMO1 conjugation to its coregulators NAB1 and NAB2, whose sumoylation down-regulates EGR2 own transcriptional activity. {ECO:0000250}. PTM: Ubiquitinated by WWP2 leading to proteasomal degradation. {ECO:0000269|PubMed:19651900}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17938205}. SUBUNIT: Interacts with HCFC1. Interacts with UBC9 (By similarity). Interacts with WWP2. Interacts with CITED1. Interacts (via phosphorylated form) with SFN. {ECO:0000250, ECO:0000269|PubMed:17938205, ECO:0000269|PubMed:19651900}. TISSUE SPECIFICITY: Expressed in mammary tumors (at protein level). Expressed mainly in adult thymus and embryonic nervous system. {ECO:0000269|PubMed:17938205}. +Q04744 EMX2_MOUSE Homeobox protein EMX2 (Empty spiracles homolog 2) (Empty spiracles-like protein 2) 253 28,374 Chain (1); DNA binding (1); Sequence conflict (1) FUNCTION: Transcription factor, which in cooperation with EMX2, acts to generate the boundary between the roof and archipallium in the developing brain. May function in combinations with OTX1/2 to specify cell fates in the developing central nervous system. {ECO:0000269|PubMed:1352754, ECO:0000269|PubMed:15147765}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: Cerebral cortex. {ECO:0000269|PubMed:1352754}. +Q9CQW0 EMC6_MOUSE ER membrane protein complex subunit 6 (Transmembrane protein 93) 110 12,017 Chain (1); Initiator methionine (1); Modified residue (1); Sequence conflict (2); Transmembrane (2) TRANSMEM 48 68 Helical. {ECO:0000255}.; TRANSMEM 87 107 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Component of the ER membrane protein complex (EMC). {ECO:0000250}. +Q03173 ENAH_MOUSE Protein enabled homolog (NPC-derived proline-rich protein 1) (NDPP-1) 802 85,844 Alternative sequence (6); Beta strand (7); Chain (1); Coiled coil (2); Compositional bias (1); Domain (1); Frameshift (2); Helix (2); Modified residue (6); Motif (1); Mutagenesis (4); Region (5); Repeat (7); Sequence conflict (1); Turn (3) FUNCTION: Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance and lamellipodial and filopodial dynamics in migrating cells. ENAH induces the formation of F-actin rich outgrowths in fibroblasts. Acts synergistically with BAIAP2-alpha and downstream of NTN1 to promote filipodia formation. {ECO:0000269|PubMed:10069337, ECO:0000269|PubMed:12134088, ECO:0000269|PubMed:15066263, ECO:0000269|PubMed:8861907}. PTM: NTN1-induced PKA phosphorylation on Ser-255 directly parallels the formation of filopodial protrusions. {ECO:0000269|PubMed:12672821, ECO:0000269|PubMed:15066263}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10069337, ECO:0000269|PubMed:12134088, ECO:0000269|PubMed:8861907}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Cell projection, filopodium {ECO:0000250}. Cell junction, synapse {ECO:0000250}. Cell junction, focal adhesion {ECO:0000250}. Note=Targeted to the leading edge of lamellipodia and filopodia by MRL family members. Colocalizes at filopodial tips with a number of other proteins including vinculin and zyxlin. Colocalizes with N-WASP at the leading edge. Colocalizes with GPHN and PFN at synapses (By similarity). {ECO:0000250}. SUBUNIT: Homotetramer (By similarity). Interacts with APBB1IP, APBB1, PFN1 and ROBO4. Isoforms, containing the polyproline-rich regions with PPLP motifs, bind the WW domain of APBB1IP. Isoforms, containing the PPSY motif, bind, in vitro, to the WW2 and WW3 domains of NEDD4 and to the WW1 domain of YAP1. Binds the SH3 domain of BAIAP2-alpha but only after the autoinhibitory region of BAIAP2-alpha has been blocked by interaction with CDC42. Interacts, via the EVH1/WH1 domain, with the Pro-rich domains from VCL, ZYX and Listeria monocytogenes actA and with TES (via LIM domain). The TES LIM domain and the Pro-rich domains from VCL or ZYX compete for the same binding site. Interaction with ZYX is important for targeting ENAH to focal adhesions and enhances production of actin-rich structures at the apical surface of cells. Interacts, through the Pro-rich region, with the C-terminal SH3 domain of DNMPB. Binds GPHN. Heterotrimer with TES and ACTL7A (By similarity). Interacts with FAT1 (via EVH1 domains). {ECO:0000250, ECO:0000269|PubMed:10338211, ECO:0000269|PubMed:12672821, ECO:0000269|PubMed:12941633, ECO:0000269|PubMed:14506234, ECO:0000269|PubMed:15148305, ECO:0000269|PubMed:15642358, ECO:0000269|PubMed:8861907, ECO:0000269|PubMed:9407065}. DOMAIN: The EVH2 domain is comprised of 3 regions. Block A is a thymosin-like domain required for G-actin binding. The KLKR motif within this block is essential for the G-actin binding and for actin polymerization. Block B is required for F-actin binding and subcellular location, and Block C for tetramerization. TISSUE SPECIFICITY: Expressed in heart and testis, lower levels in lung, skeletal muscle, kidney, pancreas and brain. Isoform 5 is expressed exclusively in the brain. Isoform 2 is expressed predominantly in brain, testis, ovary and fat. In the brain, isoforms 2 and 5 are expressed at highest levels in the hippocampus, cortex and midbrain, and at lowest levels in the striatum and cerebellum. Isoform 6 is expressed in brain and spleen. {ECO:0000269|PubMed:10069337, ECO:0000269|PubMed:1420303, ECO:0000269|PubMed:8861907}. +O55196 ENAM_MOUSE Enamelin 1274 140,954 Chain (1); Glycosylation (6); Modified residue (2); Signal peptide (1) FUNCTION: Involved in the mineralization and structural organization of enamel. Involved in the extension of enamel during the secretory stage of dental enamel formation. {ECO:0000250|UniProtKB:O97939}. PTM: Phosphorylated by FAM20C in vitro. {ECO:0000250|UniProtKB:Q9NRM1}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:O97939}. TISSUE SPECIFICITY: Expressed in developing teeth. {ECO:0000269|PubMed:11062988}. +Q9DB76 EMC9_MOUSE ER membrane protein complex subunit 9 (Protein FAM158A) 206 22,787 Chain (1); Domain (1) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Component of the ER membrane protein complex (EMC). {ECO:0000250}. +O08579 EMD_MOUSE Emerin 259 29,436 Chain (1); Compositional bias (2); Domain (1); Modified residue (13); Region (2); Sequence conflict (2); Transmembrane (1) TRANSMEM 224 244 Helical. {ECO:0000255}. FUNCTION: Stabilizes and promotes the formation of a nuclear actin cortical network. Stimulates actin polymerization in vitro by binding and stabilizing the pointed end of growing filaments. Inhibits beta-catenin activity by preventing its accumulation in the nucleus. Acts by influencing the nuclear accumulation of beta-catenin through a CRM1-dependent export pathway. Links centrosomes to the nuclear envelope via a microtubule association. Required for proper localization of non-farnesylated prelamin-A/C (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000250|UniProtKB:P50402}; Single-pass membrane protein; Nucleoplasmic side {ECO:0000250|UniProtKB:P50402}. Nucleus outer membrane. Note=Colocalized with BANF1 at the central region of the assembling nuclear rim, near spindle-attachment sites. The accumulation of different intermediates of prelamin-A/C (non-farnesylated or carboxymethylated farnesylated prelamin-A/C) in fibroblasts modify its localization in the nucleus (By similarity). {ECO:0000250}. SUBUNIT: Interacts with lamins A and C, BANF1, GMCL, BCLAF1 and YTHDC1/YT521. Interacts with TMEM43; the interaction retains emerin in the inner nuclear membrane. Interacts with ACTB, SPTAN1, F-actin, CTNNB1 and beta-tubulin (By similarity). Interacts with SUN1 and SUN2. Interacts with TMEM201. {ECO:0000250, ECO:0000269|PubMed:18230648, ECO:0000269|PubMed:19933576}. TISSUE SPECIFICITY: Detected in embryonic fibroblasts, skeletal muscle, heart muscle and tongue epithelium (at protein level). Widely expressed. {ECO:0000269|PubMed:10579712, ECO:0000269|PubMed:9107678}. +Q8K1D8 ENHO_MOUSE Adropin (Energy homeostasis-associated protein) 76 7,927 Chain (1); Signal peptide (1) FUNCTION: Involved in the regulation of glucose homeostasis and lipid metabolism. {ECO:0000269|PubMed:19041763}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19041763}. TISSUE SPECIFICITY: Expressed in liver and brain. Expressed in regions of the brain involved in metabolic regulation. {ECO:0000269|PubMed:19041763}. +Q8C042 ENO4_MOUSE Enolase 4 (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) 619 67,853 Active site (1); Alternative sequence (5); Binding site (2); Chain (1); Compositional bias (1); Erroneous initiation (2); Sequence conflict (1) Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. FUNCTION: Required for sperm motility, function and male fertility. May be involved in the normal assembly of the sperm fibrous sheath and provides most of the enolase activity in sperm (PubMed:23446454). {ECO:0000269|PubMed:23446454}. SUBUNIT: Interacts with ENO1 (PubMed:23446454). Isoform 1 and isoform 4 interact with AKAP4 (PubMed:23446454). {ECO:0000269|PubMed:23446454}. TISSUE SPECIFICITY: Testis-specific. Isoform 4 is expressed at higher levels in late spermatids than in pachytene spermatocytes. Isoform 5 is expressed at higher levels in pachytene spermatocytes than in late spermatids. {ECO:0000269|PubMed:23446454}. +Q8BHR2 ENOX1_MOUSE Ecto-NOX disulfide-thiol exchanger 1 (Constitutive Ecto-NOX) (cNOX) [Includes: Hydroquinone [NADH] oxidase (EC 1.-.-.-); Protein disulfide-thiol oxidoreductase (EC 1.-.-.-)] 643 73,281 Alternative sequence (1); Chain (1); Coiled coil (2); Compositional bias (1); Domain (1) FUNCTION: Probably acts as a terminal oxidase of plasma electron transport from cytosolic NAD(P)H via hydroquinones to acceptors at the cell surface. Hydroquinone oxidase activity alternates with a protein disulfide-thiol interchange/oxidoreductase activity which may control physical membrane displacements associated with vesicle budding or cell enlargement. The activities oscillate with a period length of 24 minutes and play a role in control of the ultradian cellular biological clock (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Secreted, extracellular space {ECO:0000250}. Note=Extracellular and plasma membrane-associated. {ECO:0000250}. +P21550 ENOB_MOUSE Beta-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 3) (Muscle-specific enolase) (MSE) (Skeletal muscle enolase) 434 47,025 Active site (2); Binding site (5); Chain (1); Initiator methionine (1); Metal binding (3); Modified residue (9); Region (1); Sequence conflict (1) Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. FUNCTION: Appears to have a function in striated muscle development and regeneration. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11229603}. Note=Localized to the Z line. Some colocalization with CKM at M-band (By similarity). {ECO:0000250}. SUBUNIT: Mammalian enolase is composed of 3 isozyme subunits, alpha, beta and gamma, which can form homodimers or heterodimers which are cell-type and development-specific. In vitro, interacts with several glycolytic enzymes including PKM, PGM, CKM and ALDO. Also binds PLG and troponin, in vitro. Interacts with PNKD (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Brain (at protein level). The alpha/alpha homodimer is expressed in embryo and in most adult tissues. The alpha/beta heterodimer and the beta/beta homodimer are found in striated muscle, and the alpha/gamma heterodimer and the gamma/gamma homodimer in neurons. In striated muscle, the fiber-type order of ENO3 expression is IIB > IIX > IIA > I. {ECO:0000269|PubMed:11229603, ECO:0000269|PubMed:23446454}. +P63094 GNAS2_MOUSE Guanine nucleotide-binding protein G(s) subunit alpha isoforms short (Adenylate cyclase-stimulating G alpha protein) 394 45,664 Alternative sequence (2); Binding site (1); Chain (1); Cross-link (1); Erroneous gene model prediction (1); Initiator methionine (1); Lipidation (2); Metal binding (2); Modified residue (1); Mutagenesis (1); Natural variant (1); Nucleotide binding (4); Sequence caution (1); Sequence conflict (10) FUNCTION: Guanine nucleotide-binding proteins (G proteins) function as transducers in numerous signaling pathways controlled by G protein-coupled receptors (GPCRs). Signaling involves the activation of adenylyl cyclases, resulting in increased levels of the signaling molecule cAMP. GNAS functions downstream of several GPCRs, including beta-adrenergic receptors. Stimulates the Ras signaling pathway via RAPGEF2. {ECO:0000250|UniProtKB:P63092}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8227063}; Lipid-anchor {ECO:0000269|PubMed:8227063}. SUBUNIT: Heterotrimeric G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site (By similarity). Interacts with CRY1; the interaction may block GPCR-mediated regulation of cAMP concentrations. Interacts with ADCY6 and stimulates its adenylyl cyclase activity (By similarity). Interacts with ADCY2 and ADCY5 (By similarity). Stimulates the ADCY5 adenylyl cyclase activity (By similarity). {ECO:0000250|UniProtKB:P04896, ECO:0000250|UniProtKB:P63092}. +Q6PGG6 GNL3L_MOUSE Guanine nucleotide-binding protein-like 3-like protein 577 65,195 Chain (1); Coiled coil (1); Domain (1); Mutagenesis (2); Nucleotide binding (3); Region (1) FUNCTION: Stabilizes TERF1 telomeric association by preventing TERF1 recruitment by PML. Stabilizes TERF1 protein by preventing its ubiquitination and hence proteasomal degradation. Does so by interfering with TERF1-binding to FBXO4 E3 ubiquitin-protein ligase. Required for cell proliferation. By stabilizing TRF1 protein during mitosis, promotes metaphase-to-anaphase transition. Stabilizes MDM2 protein by preventing its ubiquitination, and hence proteasomal degradation. By acting on MDM2, may affect TP53 activity. Required for normal processing of ribosomal pre-rRNA. Binds GTP (By similarity). {ECO:0000250, ECO:0000269|PubMed:19487455, ECO:0000269|PubMed:21132010}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:21132010}. SUBUNIT: Interacts with MDM2; this interaction, which occurs in the nucleoplasm, stabilizes MDM2. Indirectly interacts with TP53, via MDM2-binding. Interacts with TERF1; this interaction probably occurs in the nucleoplasm and is increased during mitosis, when the nucleolus is disassembled. This binding may promote TERF1 homodimerization. Interacts with TERT. {ECO:0000269|PubMed:19487455, ECO:0000269|PubMed:21132010}. DOMAIN: In contrast to other GTP-binding proteins, this family is characterized by a circular permutation of the GTPase motifs described by a G4-G1-G3 pattern. +Q9Z2U4 ELF4_MOUSE ETS-related transcription factor Elf-4 (E74-like factor 4) (Myeloid Elf-1-like factor) 655 70,800 Chain (1); DNA binding (1); Modified residue (3); Region (1); Sequence conflict (5) FUNCTION: Transcriptional activator that binds to DNA sequences containing the consensus 5'-WGGA-3'. Transactivates promoters of the hematopoietic growth factor genes CSF2, IL3, IL8, and of LYZ. Acts synergistically with RUNX1 to transactivate the IL3 promoter (By similarity). Also transactivates the PRF1 promoter in natural killer (NK) cells. Plays a role in the development and function of NK and NK T-cells and in innate immunity. Controls the proliferation and homing of CD8+ T-cells via the Kruppel-like factors KLF4 and KLF2. Controls cell senescence in a p53-dependent manner. Can also promote cellular transformation through inhibition of the p16 pathway. {ECO:0000250, ECO:0000269|PubMed:12387738, ECO:0000269|PubMed:19380490, ECO:0000269|PubMed:19412182}. SUBCELLULAR LOCATION: Nucleus, PML body {ECO:0000250}. Note=Accumulation into PML nuclear bodies is mediated by PML. {ECO:0000250}. SUBUNIT: Interacts with RUNX1 (via the Runt domain); the interaction transactivates the IL3 promoter. Interacts (via its C-terminus) with PML; the interaction translocates ELF4 to PML nuclear bodies and enhances transactivation of LYZ (By similarity). {ECO:0000250}. +A7MCT6 EKI2_MOUSE Ethanolamine kinase 2 (EKI 2) (EC 2.7.1.82) (Ethanolamine kinase-like protein) 385 44,567 Alternative sequence (1); Chain (1); Sequence conflict (3) Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from ethanolamine: step 1/3. FUNCTION: Highly specific for ethanolamine phosphorylation. Does not have choline kinase activity. {ECO:0000269|PubMed:16861741}. TISSUE SPECIFICITY: Expressed in testis and liver. Low expression in ovary and kidney. {ECO:0000269|PubMed:15161093, ECO:0000269|PubMed:16861741, ECO:0000269|PubMed:18755794}. +Q5SQM0 EMAL6_MOUSE Echinoderm microtubule-associated protein-like 6 (EMAP-6) (Echinoderm microtubule-associated protein-like 5-like) 1958 217,941 Chain (1); Compositional bias (1); Erroneous initiation (2); Repeat (30); Sequence conflict (1) FUNCTION: May modify the assembly dynamics of microtubules, such that microtubules are slightly longer, but more dynamic. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. +Q99KI3 EMC3_MOUSE ER membrane protein complex subunit 3 (Transmembrane protein 111) 261 29,980 Chain (1); Transmembrane (2) TRANSMEM 14 34 Helical. {ECO:0000255}.; TRANSMEM 118 138 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Component of the ER membrane protein complex (EMC). {ECO:0000250}. +P47801 EMP1_MOUSE Epithelial membrane protein 1 (EMP-1) (Tumor-associated membrane protein) 160 17,813 Chain (1); Glycosylation (3); Transmembrane (4) TRANSMEM 1 21 Helical. {ECO:0000255}.; TRANSMEM 67 87 Helical. {ECO:0000255}.; TRANSMEM 95 115 Helical. {ECO:0000255}.; TRANSMEM 137 157 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. +Q04742 EMX1_MOUSE Homeobox protein EMX1 (Empty spiracles homolog 1) (Empty spiracles-like protein 1) 257 28,173 Chain (1); DNA binding (1) FUNCTION: Transcription factor, which in cooperation with EMX2, acts to generate the boundary between the roof and archipallium in the developing brain. May function in combinations with OTX1/2 to specify cell fates in the developing central nervous system. {ECO:0000269|PubMed:1353865, ECO:0000269|PubMed:15147765}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29263200}. SUBUNIT: Interacts with WRD11 (via the N-terminal and the central portion of the protein); the interaction associates EMX1 with GLI3. {ECO:0000269|PubMed:29263200}. TISSUE SPECIFICITY: Cerebral cortex. Expressed in the olfactory bulbs. {ECO:0000269|PubMed:1353865, ECO:0000269|PubMed:20887964}. +Q9EP72 EMC7_MOUSE ER membrane protein complex subunit 7 241 26,310 Chain (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 159 179 Helical. {ECO:0000255}. TOPO_DOM 23 158 Extracellular. {ECO:0000255}.; TOPO_DOM 180 241 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Component of the ER membrane protein complex (EMC). {ECO:0000250}. +O70378 EMC8_MOUSE ER membrane protein complex subunit 8 (Neighbor of COX4) 207 23,348 Chain (1); Domain (1) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Component of the ER membrane protein complex (EMC). {ECO:0000250}. +Q8BX80 ENASE_MOUSE Cytosolic endo-beta-N-acetylglucosaminidase (ENGase) (EC 3.2.1.96) 734 82,945 Alternative sequence (2); Chain (1); Domain (1); Erroneous translation (1); Modified residue (1) FUNCTION: Endoglycosidase that releases N-glycans from glycoproteins by cleaving the beta-1,4-glycosidic bond in the N,N'-diacetylchitobiose core. Involved in the processing of free oligosaccharides in the cytosol (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. +O35709 ENC1_MOUSE Ectoderm-neural cortex protein 1 (ENC-1) 589 66,113 Chain (1); Domain (1); Repeat (6); Sequence conflict (1) FUNCTION: Actin-binding protein involved in the regulation of neuronal process formation and in differentiation of neural crest cells. Down-regulates transcription factor NF2L2/NRF2 by decreasing the rate of protein synthesis and not via a ubiquitin-mediated proteasomal degradation mechanism (By similarity). {ECO:0000250}. PTM: Ubiquitinated by E3 ubiquitin ligase complex formed by CUL3 and RBX1 and probably targeted for proteasome-independent degradation. Quinone-induced oxidative stress increases its ubiquitination (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000250}. Cytoplasm. Cytoplasm, cytoskeleton. Note=Interacts with the actin cytoskeleton. SUBUNIT: Binds to RB1. Hypophosphorylated RB1 associates with ENC1 during neuronal differentiation, while hyperphosphorylated RB1 associates with ENC1 in undifferentiating cells. Part of a complex that contains CUL3, RBX1 and ENC1 (By similarity). Interacts indirectly with KEAP1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Primarily expressed in the nervous system. +P50431 GLYC_MOUSE Serine hydroxymethyltransferase, cytosolic (SHMT) (EC 2.1.2.1) (Glycine hydroxymethyltransferase) (Serine methylase) 478 52,601 Beta strand (17); Chain (1); Helix (25); Modified residue (1); Sequence conflict (5); Turn (4) One-carbon metabolism; tetrahydrofolate interconversion. FUNCTION: Interconversion of serine and glycine. {ECO:0000250|UniProtKB:P34896}. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Homotetramer (PubMed:11063567). Identified in complex with FAM175B and the other subunits of the BRISC complex, at least composed of FAM175B/ABRO1, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1. {ECO:0000250|UniProtKB:P34896, ECO:0000269|PubMed:11063567}. +Q922P9 GLYR1_MOUSE Putative oxidoreductase GLYR1 (EC 1.-.-.-) (Glyoxylate reductase 1 homolog) (Nuclear protein NP60) 546 59,716 Binding site (2); Chain (1); Cross-link (10); DNA binding (1); Domain (1); Modified residue (3); Nucleotide binding (1); Region (2); Sequence conflict (4); Site (1) FUNCTION: Putative oxidoreductase that is recruited on chromatin and promotes KDM1B demethylase activity. Recognizes and binds trimethylated 'Lys-36' of histone H3 (H3K36me3). Regulates p38 MAP kinase activity by mediating stress activation of p38alpha/MAPK14 and specifically regulating MAPK14 signaling. Indirectly promotes phosphorylation of MAPK14 and activation of ATF2. The phosphorylation of MAPK14 requires upstream activity of MAP2K4 and MAP2K6. {ECO:0000250|UniProtKB:Q49A26}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q49A26}. SUBUNIT: Interacts with MAPK14. Interacts with KDM1B at nucleosomes; this interaction stimulates H3K4me1 and H3K4me2 demethylation. {ECO:0000250|UniProtKB:Q49A26}. DOMAIN: The A.T hook DNA-binding domain is required for the interaction with MAPK14. {ECO:0000250|UniProtKB:Q49A26}.; DOMAIN: The PWWP domain probably mediates the binding to H3K36me3. {ECO:0000250|UniProtKB:Q49A26}. +Q8C9A2 ENDOV_MOUSE Endonuclease V (EC 3.1.26.-) 338 37,174 Alternative sequence (1); Beta strand (10); Chain (1); Helix (8); Metal binding (2); Mutagenesis (2); Sequence caution (1); Sequence conflict (1); Site (1); Turn (1) FUNCTION: Endoribonuclease that specifically cleaves inosine-containing RNAs: cleaves RNA at the second phosphodiester bond 3' to inosine. Has strong preference for single-stranded RNAs (ssRNAs) toward double-stranded RNAs (dsRNAs). Cleaves mRNAs and tRNAs containing inosine. Also able to cleave structure-specific dsRNA substrates containing the specific sites 5'-IIUI-3' and 5'-UIUU-3'. Inosine is present in a number of RNAs following editing; the function of inosine-specific endoribonuclease is still unclear: it could either play a regulatory role in edited RNAs, or be involved in antiviral response by removing the hyperedited long viral dsRNA genome that has undergone A-to-I editing. Binds branched DNA structures (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus. TISSUE SPECIFICITY: Highest levels detected in liver with high levels also found in heart, kidney and testis. Expressed at low levels in brain. {ECO:0000269|PubMed:12853604}. +Q920G9 GMCL1_MOUSE Germ cell-less protein-like 1 (mGcl-1) (DP-interacting protein) (DIP) 524 59,654 Chain (1); Domain (1); Modified residue (2); Motif (2); Sequence conflict (5) FUNCTION: Possible function in spermatogenesis. Enhances the degradation of MDM2 and increases the amount of p53 probably by modulating the nucleocytoplasmic transport. SUBCELLULAR LOCATION: Nucleus matrix. SUBUNIT: Interacts with TMPO-Beta, TSG101 and TFDP2. Interacts with EMD (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed at low levels throughout development and in adult tissues. +Q8K0C9 GMDS_MOUSE GDP-mannose 4,6 dehydratase (EC 4.2.1.47) (GDP-D-mannose dehydratase) (GMD) 372 41,985 Active site (3); Binding site (4); Chain (1); Initiator methionine (1); Modified residue (2); Nucleotide binding (3) Nucleotide-sugar biosynthesis; GDP-L-fucose biosynthesis via de novo pathway; GDP-L-fucose from GDP-alpha-D-mannose: step 1/2. FUNCTION: Catalyzes the conversion of GDP-D-mannose to GDP-4-dehydro-6-deoxy-D-mannose. {ECO:0000250}. +Q9JL60 GMEB1_MOUSE Glucocorticoid modulatory element-binding protein 1 (GMEB-1) 562 61,058 Binding site (4); Chain (1); Coiled coil (1); Domain (1); Initiator methionine (1); Metal binding (4); Modified residue (1); Sequence conflict (1) FUNCTION: Trans-acting factor that binds to glucocorticoid modulatory elements (GME) present in the TAT (tyrosine aminotransferase) promoter and increases sensitivity to low concentrations of glucocorticoids. Binds also to the transferrin receptor promoter (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=May be also cytoplasmic. SUBUNIT: Homodimer, and heterodimer of GMEB1 and GMEB2. Interacts with TRIM63 (By similarity). Interacts with the glucocorticoid receptor (NR3C1) and NCOA2/TIF2. May interact with HSP27 and CREB-binding protein (CBP). {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. Low levels were detected in heart, brain, spleen, lung, liver, skeletal muscle, kidney and testis. +Q9CQI3 GMFB_MOUSE Glia maturation factor beta (GMF-beta) 142 16,723 Beta strand (7); Chain (1); Domain (1); Helix (6); Initiator methionine (1); Modified residue (1); Sequence conflict (1) FUNCTION: This protein causes differentiation of brain cells, stimulation of neural regeneration, and inhibition of proliferation of tumor cells. {ECO:0000250}. PTM: Phosphorylated; stimulated by phorbol ester. {ECO:0000250}. +Q9ERL7 GMFG_MOUSE Glia maturation factor gamma (GMF-gamma) 142 16,748 Beta strand (9); Chain (1); Domain (1); Helix (5); Initiator methionine (1); Modified residue (1); Turn (1) +Q6PGG2 GMIP_MOUSE GEM-interacting protein (GMIP) 971 107,545 Alternative sequence (2); Chain (1); Compositional bias (2); Domain (2); Modified residue (11); Zinc finger (1) FUNCTION: Stimulates, in vitro and in vivo, the GTPase activity of RhoA. {ECO:0000250}. SUBUNIT: Interacts with GEM through its N-terminal. {ECO:0000250}. +Q922H4 GMPPA_MOUSE Mannose-1-phosphate guanyltransferase alpha (GDP-mannose pyrophosphorylase A) (GTP-mannose-1-phosphate guanylyltransferase alpha) 420 46,244 Chain (1); Sequence conflict (1) FUNCTION: May serve as a regulatory subunit and allow allosteric feedback inhibition of GMPPB by GDP-mannose. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Associates with GMPPB. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:24035193}. +Q9DCZ1 GMPR1_MOUSE GMP reductase 1 (GMPR 1) (EC 1.7.1.7) (Guanosine 5'-monophosphate oxidoreductase 1) (Guanosine monophosphate reductase 1) 345 37,482 Active site (2); Binding site (2); Chain (1); Metal binding (4); Modified residue (1); Nucleotide binding (5); Region (4) FUNCTION: Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides. {ECO:0000255|HAMAP-Rule:MF_03195}. SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_03195}. +Q99L27 GMPR2_MOUSE GMP reductase 2 (GMPR 2) (EC 1.7.1.7) (Guanosine 5'-monophosphate oxidoreductase 2) (Guanosine monophosphate reductase 2) 348 38,019 Active site (2); Binding site (2); Chain (1); Metal binding (4); Modified residue (1); Nucleotide binding (5); Region (4); Sequence conflict (1) FUNCTION: Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides (Probable). Plays a role in modulating cellular differentiation (By similarity). {ECO:0000250|UniProtKB:Q9P2T1, ECO:0000255|HAMAP-Rule:MF_03195}. SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_03195}. +Q6NZQ2 DDX31_MOUSE Probable ATP-dependent RNA helicase DDX31 (EC 3.6.4.13) (DEAD box protein 31) 687 76,913 Chain (1); Domain (2); Motif (2); Nucleotide binding (1); Sequence conflict (3) FUNCTION: Probable ATP-dependent RNA helicase (By similarity). Plays a role in ribosome biogenesis and TP53/p53 regulation through its interaction with NPM1 (By similarity). {ECO:0000250|UniProtKB:Q9H8H2}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9H8H2}. Note=Colocalized with NPM1 in the nucleoli. {ECO:0000250|UniProtKB:Q9H8H2}. SUBUNIT: Interacts with NPM1; the interaction prevents interaction between NPM1 and HDM2. {ECO:0000250|UniProtKB:Q9H8H2}. +Q6AXC6 DDX11_MOUSE ATP-dependent DNA helicase DDX11 (EC 3.6.4.12) (DEAD/H-box protein 11) 906 101,968 Chain (1); Compositional bias (1); Domain (1); Metal binding (4); Modified residue (1); Motif (1); Nucleotide binding (1); Sequence caution (1) FUNCTION: DNA-dependent ATPase and ATP-dependent DNA helicase that participates in various functions in genomic stability, including DNA replication, DNA repair and heterochromatin organization as well as in ribosomal RNA synthesis. Its double-stranded DNA helicase activity requires either a minimal 5'-single-stranded tail length of approximately 15 nt (flap substrates) or 10 nt length single-stranded gapped DNA substrates of a partial duplex DNA structure for helicase loading and translocation along DNA in a 5' to 3' direction. The helicase activity is capable of displacing duplex regions up to 100 bp, which can be extended up to 500 bp by the replication protein A (RPA) or the cohesion CTF18-replication factor C (Ctf18-RFC) complex activities. Shows also ATPase- and helicase activities on substrates that mimic key DNA intermediates of replication, repair and homologous recombination reactions, including forked duplex, anti-parallel G-quadruplex and three-stranded D-loop DNA molecules. Plays a role in DNA double-strand break (DSB) repair at the DNA replication fork during DNA replication recovery from DNA damage. Recruited with TIMELESS factor upon DNA-replication stress response at DNA replication fork to preserve replication fork progression, and hence ensure DNA replication fidelity (By similarity). Cooperates also with TIMELESS factor during DNA replication to regulate proper sister chromatid cohesion and mitotic chromosome segregation (PubMed:17611414). Stimulates 5'-single-stranded DNA flap endonuclease activity of FEN1 in an ATP- and helicase-independent manner; and hence it may contribute in Okazaki fragment processing at DNA replication fork during lagging strand DNA synthesis. Its ability to function at DNA replication fork is modulated by its binding to long non-coding RNA (lncRNA) cohesion regulator non-coding RNA DDX11-AS1/CONCR, which is able to increase both DDX11 ATPase activity and binding to DNA replicating regions (By similarity). Plays also a role in heterochromatin organization (PubMed:21854770). Involved in rRNA transcription activation through binding to active hypomethylated rDNA gene loci by recruiting UBTF and the RNA polymerase Pol I transcriptional machinery (By similarity). Plays a role in embryonic development and prevention of aneuploidy (PubMed:17611414). Involved in melanoma cell proliferation and survival. Associates with chromatin at DNA replication fork regions. Binds to single- and double-stranded DNAs (By similarity). {ECO:0000250|UniProtKB:Q96FC9, ECO:0000269|PubMed:17611414, ECO:0000269|PubMed:21854770}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96FC9}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q96FC9}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q96FC9}. Midbody {ECO:0000250|UniProtKB:Q96FC9}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q96FC9}. Note=During the early stages of mitosis, localizes to condensed chromatin and is released from the chromatin with progression to metaphase. Also localizes to the spindle poles throughout mitosis and at the midbody at later stages of mitosis (metaphase to telophase). In interphase, colocalizes with nucleolin in the nucleolus. {ECO:0000250|UniProtKB:Q96FC9}. SUBUNIT: Associates with the CTF18-RFC complex. Associates with a cohesin complex composed of RAD21, SMC1 proteins and SMC3. Interacts with CHTF18. Interacts with DSCC1. Interacts with FEN1; this interaction is direct and increases flap endonuclease activity of FEN1. Interacts with PCNA. Interacts with POLR1A and UBTF. Interacts with RAD21, SMC1 proteins and SMC3. Interacts with RFC2. Interacts with TIMELESS; this interaction increases recruitment of both proteins onto chromatin in response to replication stress induction by hydroxyurea. {ECO:0000250|UniProtKB:Q96FC9}. +P50705 DEFA7_MOUSE Alpha-defensin 7 (Defensin-related cryptdin-7) 93 10,496 Disulfide bond (3); Peptide (1); Propeptide (1); Signal peptide (1) FUNCTION: Probably contributes to the antimicrobial barrier function of the small bowel mucosa. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Paneth cells of the small bowel. +P50706 DEFA8_MOUSE Alpha-defensin 8 (Defensin-related cryptdin-8) (Fragment) 81 9,226 Disulfide bond (3); Non-terminal residue (1); Peptide (1); Propeptide (1); Signal peptide (1) FUNCTION: Probably contributes to the antimicrobial barrier function of the small bowel mucosa. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Paneth cells of the small bowel. +A2RSQ0 DEN5B_MOUSE DENN domain-containing protein 5B (Rab6IP1-like protein) 1274 144,629 Chain (1); Domain (6); Initiator methionine (1); Modified residue (8); Sequence caution (3); Sequence conflict (5); Transmembrane (1) TRANSMEM 916 936 Helical. {ECO:0000255}. FUNCTION: Guanine nucleotide exchange factor (GEF) which may activate RAB39A and/or RAB39B. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +A2RT67 DEND3_MOUSE DENN domain-containing protein 3 1274 143,888 Beta strand (6); Chain (1); Domain (3); Erroneous initiation (2); Helix (11); Modified residue (3); Mutagenesis (4); Region (1); Repeat (7); Sequence conflict (3); Turn (1) FUNCTION: Guanine nucleotide exchange factor (GEF) activating Rab12. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab12 into its active GTP-bound form. Regulates autophagy in response to starvation through Rab12 activation (PubMed:24719330, PubMed:25925668, PubMed:28249939). Starvation leads to ULK1/2-dependent phosphorylation of Ser-554 and Ser-572, which in turn allows recruitment of 14-3-3 adapter proteins and leads to up-regulation of GEF activity towards Rab12 (PubMed:25925668). Also plays a role in protein transport from recycling endosomes to lysosomes, regulating, for instance, the degradation of the transferrin receptor and of the amino acid transporter PAT4 (PubMed:21718402, PubMed:24719330). Starvation also induces phosphorylation at Tyr-940, which leads to up-regulated GEF activity and initiates autophagy (PubMed:28249939). {ECO:0000269|PubMed:21718402, ECO:0000269|PubMed:24719330, ECO:0000269|PubMed:25925668, ECO:0000269|PubMed:28249939}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28249939}. Note=Transiently recruited to membranes to activate Rab12. {ECO:0000269|PubMed:28249939}. SUBUNIT: Forms oligomers (PubMed:28249939). Interacts with 6 of the 7 known isoforms of 14-3-3 proteins (PubMed:25925668). {ECO:0000269|PubMed:25925668, ECO:0000269|PubMed:28249939}. DOMAIN: Inactive Dennd3 is found in a closed conformation, in which the linker region interacts with the DENN domain. Phosphorylation of Tyr-940 in the linker region intereferes with this interaction leading to an open conformation and enhances the GEF activity of the protein towards Rab12. {ECO:0000269|PubMed:28249939}. +Q91YP3 DEOC_MOUSE Deoxyribose-phosphate aldolase (DERA) (EC 4.1.2.4) (2-deoxy-D-ribose 5-phosphate aldolase) (Phosphodeoxyriboaldolase) (Deoxyriboaldolase) 318 34,975 Active site (3); Chain (1) Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2. FUNCTION: Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate. Participates in stress granule (SG) assembly. May allow ATP production from extracellular deoxyinosine in conditions of energy deprivation. {ECO:0000250|UniProtKB:Q9Y315}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y315}. Cytoplasmic granule {ECO:0000250|UniProtKB:Q9Y315}. Nucleus {ECO:0000250|UniProtKB:Q9Y315}. Note=Recruited to stress granules but not to processing bodies upon arsenite or clotrimazole treatment or energy deprivation. {ECO:0000250|UniProtKB:Q9Y315}. SUBUNIT: Interacts with YBX1. {ECO:0000250|UniProtKB:Q9Y315}. +Q9D8K3 DERL3_MOUSE Derlin-3 (Degradation in endoplasmic reticulum protein 3) (Der1-like protein 3) (Protein IZP6) 228 25,978 Alternative sequence (1); Chain (1); Erroneous initiation (1); Sequence conflict (1); Topological domain (5); Transmembrane (4) TRANSMEM 23 43 Helical; Name=1. {ECO:0000255}.; TRANSMEM 58 78 Helical; Name=2. {ECO:0000255}.; TRANSMEM 99 119 Helical; Name=3. {ECO:0000255}.; TRANSMEM 169 189 Helical; Name=4. {ECO:0000255}. TOPO_DOM 1 22 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 44 57 Lumenal. {ECO:0000255}.; TOPO_DOM 79 98 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 120 168 Lumenal. {ECO:0000255}.; TOPO_DOM 190 228 Cytoplasmic. {ECO:0000255}. FUNCTION: Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal glycoproteins, but not that of misfolded nonglycoproteins. May act by forming a channel that allows the retrotranslocation of misfolded glycoproteins into the cytosol where they are ubiquitinated and degraded by the proteasome. May mediate the interaction between VCP and the misfolded glycoproteins. May be involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for proteasomal degradation. {ECO:0000250|UniProtKB:Q96Q80}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q96Q80}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q96Q80}. SUBUNIT: Forms homo- and heterooligomers with DERL2 and, to a lesser extent, with DERL1 (By similarity). Interacts with VCP and EDEM1 (By similarity). Interacts with SELENOK and SELENOS (PubMed:22016385). Interacts with the signal recognition particle/SRP and the SRP receptor; in the process of endoplasmic reticulum stress-induced pre-emptive quality control (By similarity). {ECO:0000250|UniProtKB:Q96Q80, ECO:0000269|PubMed:22016385}. TISSUE SPECIFICITY: Highly expressed in spleen, lung, liver, spleen and testis. Expressed at intermediate level in kidney. Weakly or not expressed in brain, heart and skeletal muscle. {ECO:0000269|PubMed:11422294}. +P61460 DEPD5_MOUSE GATOR complex protein DEPDC5 (DEP domain-containing protein 5) 1591 180,379 Alternative sequence (1); Chain (1); Domain (1); Erroneous initiation (1); Modified residue (1); Sequence conflict (2) FUNCTION: As a component of the GATOR1 complex functions as an inhibitor of the amino acid-sensing branch of the TORC1 pathway. The GATOR1 complex strongly increases GTP hydrolysis by RRAGA and RRAGB within RRAGC-containing heterodimers, thereby deactivating RRAGs, releasing mTORC1 from lysosomal surface and inhibiting mTORC1 signaling. The GATOR1 complex is negatively regulated by GATOR2 the other GATOR subcomplex in this amino acid-sensing branch of the TORC1 pathway. {ECO:0000250|UniProtKB:O75140}. PTM: Ubiquitinated. Amino acid-induced 'Lys-48'-linked polyubiquitination of DEPDC5 by the BCR(KLHL22) ubiquitin ligase complex leads to DEPDC5 proteasomal degradation and inhibition of the GATOR1 complex. Ubiquitination may occur at multiple lysines. {ECO:0000250|UniProtKB:O75140}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:23542697}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:23542697}. Lysosome membrane {ECO:0000250|UniProtKB:O75140}. Note=Localization to lysosomes is amino acid-independent. {ECO:0000250|UniProtKB:O75140}. SUBUNIT: Within the GATOR complex, component of the GATOR1 subcomplex, made of DEPDC5, NPRL2 and NPRL3. GATOR1 mediates the strong interaction of the GATOR complex with RRAGA/RRAGC and RRAGB/RRAGC heterodimers. Interacts (via DEP domain) with KLHL22; the interaction depends on amino acid availability. {ECO:0000250|UniProtKB:O75140}. DOMAIN: The DEP domain mediates the interaction with KLHL22. {ECO:0000250|UniProtKB:O75140}. TISSUE SPECIFICITY: Expressed at low levels in all brain regions. Expressed throughout brain development, including in midgestation embryonic head (11.5 dpc), neonatal brain and whole adult brain. Present in neurons and absent in non-neuronal cells, including astrocytes (at protein level). {ECO:0000269|PubMed:23542697}. +Q9EQ06 DHB11_MOUSE Estradiol 17-beta-dehydrogenase 11 (EC 1.1.1.62) (17-beta-hydroxysteroid dehydrogenase 11) (17-beta-HSD 11) (17bHSD11) (17betaHSD11) (17-beta-hydroxysteroid dehydrogenase XI) (17-beta-HSD XI) (17betaHSDXI) (Dehydrogenase/reductase SDR family member 8) 298 32,881 Active site (1); Alternative sequence (2); Binding site (1); Chain (1); Nucleotide binding (1); Signal peptide (1) FUNCTION: Can convert androstan-3-alpha,17-beta-diol (3-alpha-diol) to androsterone in vitro, suggesting that it may participate in androgen metabolism during steroidogenesis. May act by metabolizing compounds that stimulate steroid synthesis and/or by generating metabolites that inhibit it. Has no activity toward DHEA (dehydroepiandrosterone), or A-dione (4-androste-3,17-dione), and only a slight activity toward testosterone to A-dione. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Cytoplasm. Note=According to PubMed:12697717 it is cytoplasmic. However, the relevance of such result remains unclear. +Q91WG7 DGKG_MOUSE Diacylglycerol kinase gamma (DAG kinase gamma) (EC 2.7.1.107) (88 kDa diacylglycerol kinase) (Diglyceride kinase gamma) (DGK-gamma) 788 88,523 Calcium binding (2); Chain (1); Domain (3); Zinc finger (2) +Q8VCH6 DHC24_MOUSE Delta(24)-sterol reductase (EC 1.3.1.72) (24-dehydrocholesterol reductase) (3-beta-hydroxysterol Delta-24-reductase) 516 60,112 Chain (1); Domain (1); Erroneous initiation (1); Nucleotide binding (1); Sequence conflict (5); Signal peptide (1); Site (2); Topological domain (2); Transmembrane (1) TRANSMEM 32 52 Helical. {ECO:0000255}. TOPO_DOM 23 31 Lumenal. {ECO:0000255}.; TOPO_DOM 53 516 Cytoplasmic. {ECO:0000255}. Steroid biosynthesis; cholesterol biosynthesis. FUNCTION: Catalyzes the reduction of the Delta-24 double bond of sterol intermediates. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. +O88736 DHB7_MOUSE 3-keto-steroid reductase (EC 1.1.1.270) (17-beta-hydroxysteroid dehydrogenase 7) (17-beta-HSD 7) (Estradiol 17-beta-dehydrogenase 7) (EC 1.1.1.62) 334 37,317 Active site (1); Binding site (1); Chain (1); Glycosylation (4); Nucleotide binding (1); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 230 250 Helical. {ECO:0000255}. TOPO_DOM 1 229 Extracellular. {ECO:0000255}.; TOPO_DOM 251 334 Cytoplasmic. {ECO:0000255}. Steroid biosynthesis; estrogen biosynthesis. Steroid biosynthesis; zymosterol biosynthesis; zymosterol from lanosterol: step 5/6. FUNCTION: Responsible for the reduction of the keto group on the C-3 of sterols. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. TISSUE SPECIFICITY: Most abundant in ovaries of pregnant animals. Present also in nonpregnant animals in ovaries, mammary gland, liver, kidney and testis. +Q99LB2 DHRS4_MOUSE Dehydrogenase/reductase SDR family member 4 (EC 1.1.1.184) (NADPH-dependent carbonyl reductase/NADP-retinol dehydrogenase) (CR) (PHCR) (NADPH-dependent retinol dehydrogenase/reductase) (NDRD) (mouNRDR) (Peroxisomal short-chain alcohol dehydrogenase) (PSCD) 279 29,885 Active site (1); Binding site (1); Chain (1); Erroneous initiation (2); Modified residue (8); Motif (1); Nucleotide binding (1); Sequence conflict (2) FUNCTION: Reduces all-trans-retinal and 9-cis retinal. Can also catalyze the oxidation of all-trans-retinol with NADP as co-factor, but with much lower efficiency. Reduces alkyl phenyl ketones and alpha-dicarbonyl compounds with aromatic rings, such as pyrimidine-4-aldehyde, 3-benzoylpyridine, 4-benzoylpyridine, menadione and 4-hexanoylpyridine. Has no activity towards aliphatic aldehydes and ketones (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}. SUBUNIT: Homotetramer. {ECO:0000250}. +Q8R242 DIAC_MOUSE Di-N-acetylchitobiase (EC 3.2.1.-) 366 41,295 Active site (1); Alternative sequence (1); Chain (1); Glycosylation (5); Signal peptide (1) FUNCTION: Involved in the degradation of asparagine-linked glycoproteins. Hydrolyze of N-acetyl-beta-D-glucosamine (1-4)N-acetylglucosamine chitobiose core from the reducing end of the bond, it requires prior cleavage by glycosylasparaginase (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Lysosome {ECO:0000250}. +Q6PE54 DHX40_MOUSE Probable ATP-dependent RNA helicase DHX40 (EC 3.6.4.13) (DEAH box protein 40) 779 88,530 Chain (1); Domain (2); Erroneous initiation (2); Frameshift (3); Motif (1); Nucleotide binding (1) FUNCTION: Probable ATP-dependent RNA helicase. {ECO:0000250}. +Q9D6I7 DIK1A_MOUSE Divergent protein kinase domain 1A (Protein FAM69A) 428 48,936 Chain (1); Sequence conflict (3); Topological domain (2); Transmembrane (1) TRANSMEM 28 48 Helical. {ECO:0000255}. TOPO_DOM 1 27 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 49 428 Lumenal. {ECO:0000255}. PTM: Among the many cysteines in the lumenal domain, most are probably involved in disulfide bonds. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21334309}; Single-pass type II membrane protein {ECO:0000269|PubMed:21334309}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:21334309}. +A2A4P0 DHX8_MOUSE ATP-dependent RNA helicase DHX8 (EC 3.6.4.13) (DEAH box protein 8) 1244 142,572 Chain (1); Compositional bias (2); Cross-link (2); Domain (3); Modified residue (2); Motif (1); Nucleotide binding (1) FUNCTION: Involved in pre-mRNA splicing as component of the spliceosome. Facilitates nuclear export of spliced mRNA by releasing the RNA from the spliceosome. {ECO:0000250|UniProtKB:Q14562}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q14562}. SUBUNIT: Identified in the spliceosome C complex. Interacts with ARRB2; the interaction is detected in the nucleus upon OR1D2 stimulation. {ECO:0000250|UniProtKB:Q14562}. DOMAIN: The RS domain confers a nuclear localization signal, and appears to facilitate the interaction with the spliceosome. {ECO:0000250}. +Q9DC23 DJC10_MOUSE DnaJ homolog subfamily C member 10 (EC 1.8.4.-) (Endoplasmic reticulum DNA J domain-containing protein 5) (ER-resident protein ERdj5) (ERdj5) (Endoplasmic reticulum DnaJ-PDI fusion protein 1) (J domain-containing protein disulfide isomerase-like protein) (J domain-containing PDI-like protein) (JPDI) 793 90,583 Beta strand (33); Chain (1); Disulfide bond (4); Domain (5); Glycosylation (1); Helix (34); Motif (1); Mutagenesis (8); Region (2); Sequence conflict (9); Signal peptide (1); Turn (19) FUNCTION: Endoplasmic reticulum disulfide reductase involved both in the correct folding of proteins and degradation of misfolded proteins. Required for efficient folding of proteins in the endoplasmic reticulum by catalyzing the removal of non-native disulfide bonds formed during the folding of proteins, such as LDLR. Also involved in endoplasmic reticulum-associated degradation (ERAD) by reducing incorrect disulfide bonds in misfolded glycoproteins recognized by EDEM1. Interaction with HSPA5 is required its activity, not for the disulfide reductase activity, but to facilitate the release of DNAJC10 from its substrate. Promotes apoptotic signaling pathway in response to endoplasmic reticulum stress. {ECO:0000269|PubMed:12411443, ECO:0000269|PubMed:12446677, ECO:0000269|PubMed:18653895, ECO:0000269|PubMed:21329881}. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138, ECO:0000269|PubMed:12446677}. SUBUNIT: Interacts with HSPA5 (via its J domain). Interacts with EDEM1. {ECO:0000269|PubMed:12446677, ECO:0000269|PubMed:18653895, ECO:0000269|PubMed:21329881}. DOMAIN: Thioredoxin domains 3 and 4 are the primary reductase domains. {ECO:0000269|PubMed:21329881}.; DOMAIN: The thioredoxin-like regions Trxb 1 and 2 lack a redox-active CXXC motif. {ECO:0000269|PubMed:21329881}. TISSUE SPECIFICITY: Ubiquitous. Particularly abundant in secretory tissues. Ubiquitous in fetal tissues and tumor tissues. Higher expression in fetal tissues than in adult tissues. Expressed in testis, pancreas, fetal thymus and fetal kidney. High expression in heart, liver, kidney, and testis. Low expression in spleen and skeletal muscle. {ECO:0000269|PubMed:12411443, ECO:0000269|PubMed:12446677}. +Q8K1E3 DLK2_MOUSE Protein delta homolog 2 (DLK-2) (Endothelial cell-specific protein S-1) (Epidermal growth factor-like protein 9) (EGF-like protein 9) 382 40,404 Alternative sequence (2); Chain (1); Disulfide bond (17); Domain (6); Erroneous initiation (1); Glycosylation (1); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 306 326 Helical. {ECO:0000255}. TOPO_DOM 27 305 Extracellular. {ECO:0000255}.; TOPO_DOM 327 382 Cytoplasmic. {ECO:0000255}. FUNCTION: Regulates adipogenesis. {ECO:0000269|PubMed:17320102}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Detected in a number of tissues including lung, brain, adrenal gland, testis, adult liver, placenta, ovary and thymus. Not detected in fetal liver or in adult spleen, muscle and heart. {ECO:0000269|PubMed:17320102}. +Q60997 DMBT1_MOUSE Deleted in malignant brain tumors 1 protein (Apactin) (CRP-ductin) (Glycoprotein 300) (gp300) (Hensin) (Mucin-like glycoprotein) (Muclin) (Vomeroglandin) (p80) 2085 226,815 Alternative sequence (3); Chain (1); Compositional bias (1); Disulfide bond (35); Domain (14); Frameshift (1); Glycosylation (21); Modified residue (2); Mutagenesis (2); Sequence conflict (3); Signal peptide (1); Transmembrane (1) TRANSMEM 2050 2070 Helical. {ECO:0000255}. FUNCTION: May play roles in mucosal defense system and cellular immune defense. May play a role in liver regeneration. May be an important factor in fate decision and differentiation of transit-amplifying ductular (oval) cells within the hepatic lineage. May function as a binding protein in saliva for the regulation of taste sensation. May play a role as an opsonin receptor for SFTPD and SPAR in macrophage tissues throughout the body, including epithelial cells lining the gastrointestinal tract (By similarity). Required for terminal differentiation of columnar epithelial cells during early embryogenesis. Displays a broad calcium-dependent binding spectrum against both Gram-positive and Gram-negative bacteria, suggesting a role in defense against bacterial pathogens. Binds to a range of poly-sulfated and poly-phosphorylated ligands which may explain its broad bacterial-binding specificity. Inhibits cytoinvasion of S.enterica. Associates with the actin cytoskeleton and is involved in its remodeling during regulated exocytosis. Interacts with pancreatic zymogens in a pH-dependent manner and may act as a Golgi cargo receptor in the regulated secretory pathway of the pancreatic acinar cell. {ECO:0000250, ECO:0000269|PubMed:11152281, ECO:0000269|PubMed:12082154, ECO:0000269|PubMed:12884308, ECO:0000269|PubMed:15146979, ECO:0000269|PubMed:15292166, ECO:0000269|PubMed:15452149, ECO:0000269|PubMed:15987769, ECO:0000269|PubMed:8742698}. PTM: Highly N- and O-glycosylated. The O-glycans are heavily sulfated. O-glycosylation and sulfation in pancreatic acinar cells are required for zymogen granule maturation. Glycoconjugate composition changes during development with fucose only acquired post-natally during weaning. {ECO:0000269|PubMed:7876332, ECO:0000269|PubMed:8543783}. SUBCELLULAR LOCATION: Secreted. Cytoplasmic vesicle, secretory vesicle membrane; Single-pass membrane protein; Lumenal side. Note=Localized to the lumenal aspect of crypt cells in the small intestine. In the colon, seen in the lumenal aspect of surface epithelial cells. Formed in the ducts of von Ebner gland and released into the fluid bathing the taste buds contained in the taste papillae. In the CFTR knockout mouse, enhanced on the acinar luminar surface. SUBUNIT: Interacts with LGALS3. Binds SPAR in a calcium-dependent manner (By similarity). Binds SFTPD in a calcium-dependent manner. {ECO:0000250, ECO:0000269|PubMed:12884308}. DOMAIN: The SRCR domains mediate binding to bacteria. {ECO:0000250}. TISSUE SPECIFICITY: Strongly expressed in acini and duct epithelial cells of the exocrine pancreas but not in the islets of Langerhans. Expressed in gall bladder, salivary glands and in the epithelium lining larger hepatic ducts, but not in the liver parenchyma, stomach or lung. Expressed along the intestinal tract including duodenum, jejunum, ileum and colon (at protein level). Expressed in glands associated with vomeronasal tissues. Expressed in the vomeronasal gland and posterior gland of nasal septum. Weakly expressed in lateral nasal gland. CFTR knockout mice show increased expression in pancreas, duodenum and small intestine but not in gall bladder. In pancreas and small intestine, increased expression occurs after the appearance of dilated lumina. {ECO:0000269|PubMed:10679193, ECO:0000269|PubMed:12884308, ECO:0000269|PubMed:7537458, ECO:0000269|PubMed:8742698, ECO:0000269|PubMed:9247472, ECO:0000269|PubMed:9688648}. +Q8CFG4 DMRTA_MOUSE Doublesex- and mab-3-related transcription factor A1 (Doublesex- and mab-3-related transcription factor 4) 490 52,653 Chain (1); DNA binding (1) SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00070}. TISSUE SPECIFICITY: Widely expressed, with highest levels in ovary, testis, epididymis, preputial gland, vomeronasal organ, liver, salivary glands and heart. Also expressed throughout the brain with highest levels in the olfactory bulbs and medulla. Detected at similar levels in gonads of both sexes. {ECO:0000269|PubMed:12609607, ECO:0000269|PubMed:16982677}. +Q8CE22 DMTF1_MOUSE Cyclin-D-binding Myb-like transcription factor 1 (Cyclin-D-interacting Myb-like protein 1) (mDmp1) 761 84,644 Alternative sequence (8); Chain (1); DNA binding (1); Domain (3); Mutagenesis (1); Region (5); Sequence conflict (7) FUNCTION: Transcriptional activator which activates the CDKN2A/ARF locus in response to Ras-Raf signaling, thereby promoting p53/TP53-dependent growth arrest. May also cooperate with MYB to activate transcription of the ANPEP gene. Binds to the consensus sequence 5'-CCCG[GT]ATGT-3'. {ECO:0000269|PubMed:10097151, ECO:0000269|PubMed:10898794, ECO:0000269|PubMed:11711428, ECO:0000269|PubMed:15601844, ECO:0000269|PubMed:17936562, ECO:0000269|PubMed:8887674, ECO:0000269|PubMed:9488476, ECO:0000269|PubMed:9786929}. PTM: Phosphorylated by the cyclin-D2/CDK4, cyclin-D3/CDK4 and cyclin-D2/CDK6 complexes and to a lesser extent by the cyclin-D1/CDK4 complex. {ECO:0000269|PubMed:8887674, ECO:0000269|PubMed:9488476}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:10097151, ECO:0000269|PubMed:16878159, ECO:0000269|PubMed:17936562, ECO:0000269|PubMed:9488476}. SUBUNIT: Interacts with the D-type cyclins CCND1, CCND2 and CCND3. Interaction with D-type cyclins may modulate transcriptional activation by this protein. {ECO:0000269|PubMed:8887674, ECO:0000269|PubMed:9488476}. TISSUE SPECIFICITY: Ubiquitously expressed (at mRNA level). Expressed in brain, intestine, kidney, lung, pancreas, skin, spleen and tongue (at protein level). Expressed at high levels in testis and thymus (at protein level). In all tissues examined, expression is predominant in non-proliferating and differentiated cell types. These include epithelial, interstitial and smooth muscle cells of the intestine, differentiated spermatids, sperm and interstitial cells of the testis, and lymphoid cells of the medullary compartment of the thymus. {ECO:0000269|PubMed:10898794, ECO:0000269|PubMed:16878159, ECO:0000269|PubMed:8887674}. +Q61091 FZD8_MOUSE Frizzled-8 (Fz-8) (mFz8) 685 73,045 Beta strand (2); Chain (1); Compositional bias (3); Disulfide bond (5); Domain (1); Glycosylation (3); Helix (8); Motif (2); Mutagenesis (1); Region (3); Sequence conflict (2); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 273 293 Helical; Name=1. {ECO:0000255}.; TRANSMEM 310 330 Helical; Name=2. {ECO:0000255}.; TRANSMEM 395 415 Helical; Name=3. {ECO:0000255}.; TRANSMEM 438 458 Helical; Name=4. {ECO:0000255}.; TRANSMEM 482 502 Helical; Name=5. {ECO:0000255}.; TRANSMEM 531 551 Helical; Name=6. {ECO:0000255}.; TRANSMEM 583 603 Helical; Name=7. {ECO:0000255}. TOPO_DOM 28 272 Extracellular. {ECO:0000255}.; TOPO_DOM 294 309 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 331 394 Extracellular. {ECO:0000255}.; TOPO_DOM 416 437 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 459 481 Extracellular. {ECO:0000255}.; TOPO_DOM 503 530 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 552 582 Extracellular. {ECO:0000255}.; TOPO_DOM 604 685 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for Wnt proteins. Component of the Wnt-Fzd-LRP5-LRP6 complex that triggers beta-catenin signaling through inducing aggregation of receptor-ligand complexes into ribosome-sized signalsomes (By similarity). The beta-catenin canonical signaling pathway leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues. Coreceptor along with RYK of Wnt proteins, such as WNT1. {ECO:0000250, ECO:0000269|PubMed:10097073, ECO:0000269|PubMed:10395542, ECO:0000269|PubMed:15454084, ECO:0000269|PubMed:16543246}. PTM: Ubiquitinated by ZNRF3, leading to its degradation by the proteasome. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Golgi apparatus. Cell membrane; Multi-pass membrane protein. Note=Colocalizes with GOPC at the Golgi apparatus. SUBUNIT: Component of a Wnt-signaling complex that contains a WNT protein, a FZD protein and LRP5 or LRP6. Interacts directly with LRP5 or LRP6; the interaction is promoted by Wnt-binding and signaling and inhibited by DKK1 (By similarity). Interacts (via the PDZ-binding motif) with GPOC (via its PDZ domain). Interacts with RSPO1 and RSPO3. Interacts with glypican GPC3 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9H461, ECO:0000269|PubMed:11520064, ECO:0000269|PubMed:16543246, ECO:0000269|PubMed:22653731}. DOMAIN: Lys-Thr-X-X-X-Trp motif interacts with the PDZ domain of Dvl (Disheveled) family members and is involved in the activation of the Wnt/beta-catenin signaling pathway. {ECO:0000250}.; DOMAIN: The FZ domain is involved in binding with Wnt ligands. TISSUE SPECIFICITY: Expressed in chondrocytes. +P70694 DHB5_MOUSE Estradiol 17 beta-dehydrogenase 5 (EC 1.1.1.-) (17-beta-HSD 5) 323 37,048 Active site (1); Binding site (3); Chain (1); Nucleotide binding (4); Site (1) FUNCTION: Active toward androgens, estrogens, and xenobiotic substrates. Also exhibits low 20 alpha-HSD activity. Shows a-stereospecificity in hydrogen transfer between cofactors and substrates (A-specific). Preferentially catalyzes the reduction of 4-androstenedione, 5-alpha-androstane-3,17-dione, androsterone and dehydroepiandrosterone to testosterone, dihydrotestosterone, 5-alpha-androstane-3-alpha,17-beta-diol and 5-androstene-3-beta,17-beta-diol, respectively. {ECO:0000269|PubMed:10500239}. PTM: Three forms are detected, probably due to post-translational modifications. SUBUNIT: Monomer. TISSUE SPECIFICITY: Mainly found in liver. Also expressed weakly in kidney. {ECO:0000269|PubMed:10500239}. +Q3U0B3 DHR11_MOUSE Dehydrogenase/reductase SDR family member 11 (17-beta-hydroxysteroid dehydrogenase) (3-beta-hydroxysteroid 3-dehydrogenase) (EC 1.1.1.270) (Estradiol 17-beta-dehydrogenase) (EC 1.1.1.62) (Short-chain dehydrogenase/reductase family 24C member 1) 260 28,274 Active site (1); Binding site (7); Chain (1); Nucleotide binding (4); Signal peptide (1) Steroid biosynthesis; estrogen biosynthesis. FUNCTION: Catalyzes the conversion of the 17-keto group of estrone, 4- and 5-androstenes and 5-alpha-androstanes into their 17-beta-hydroxyl metabolites and the conversion of the 3-keto group of 3-, 3,17- and 3,20- diketosteroids into their 3-hydroxyl metabolites. Exhibits reductive 3-beta-hydroxysteroid dehydrogenase activity toward 5-beta-androstanes, 5-beta-pregnanes, 4-pregnenes and bile acids. May also reduce endogenous and exogenous alpha-dicarbonyl compounds and xenobiotic alicyclic ketones. {ECO:0000250|UniProtKB:Q6UWP2}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. SUBUNIT: Homotetramer. +Q80VY9 DHX33_MOUSE ATP-dependent RNA helicase DHX33 (EC 3.6.4.13) (DEAH box protein 33) 698 78,347 Chain (1); Domain (2); Motif (2); Mutagenesis (1); Nucleotide binding (1); Region (2); Sequence conflict (1) FUNCTION: Implicated in nucleolar organization, ribosome biogenesis, protein synthesis and cytoplasmic dsRNA sensing (By similarity) (PubMed:21930779). Stimulates RNA polymerase I transcription of the 47S precursor rRNA. Associates with ribosomal DNA (rDNA) loci where it is involved in POLR1A recruitment (PubMed:21930779). In the cytoplasm, promotes elongation-competent 80S ribosome assembly at the late stage of mRNA translation initiation (PubMed:26100019). Senses cytosolic dsRNA mediating NLRP3 inflammasome formation in macrophages and type I interferon production in myeloid dendritic cells (By similarity). Required for NLRP3 activation induced by viral dsRNA and bacterial RNA (By similarity). In dendritic cells, required for induction of type I interferon production induced by cytoplasmic dsRNA via the activation of MAPK and NF-kappa-B signaling pathways (PubMed:24037184). {ECO:0000250|UniProtKB:Q9H6R0, ECO:0000269|PubMed:21930779, ECO:0000269|PubMed:24037184, ECO:0000269|PubMed:26100019}. PTM: Ubiquitinated, leading to its degradation by the proteasome (PubMed:29273634). Deubiquitinated by USP36 (PubMed:29273634). {ECO:0000269|PubMed:29273634}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:21930779}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9H6R0}. Cytoplasm {ECO:0000250|UniProtKB:Q9H6R0}. Nucleus {ECO:0000250|UniProtKB:Q9H6R0}. Inflammasome {ECO:0000250|UniProtKB:Q9H6R0}. Note=Predominantly in the nucleolus. During mitosis, localizes with the nucleolar organizing regions. Upon dsRNA-binding, localizes in the inflammasome. {ECO:0000250|UniProtKB:Q9H6R0}. SUBUNIT: Interacts with UBTF (PubMed:21930779). Interacts with DDX3X, EIF3G and EIF3H; the interaction is independent of RNA (PubMed:26100019). Interacts (via HA2 region and Helicase C-terminal domain) with the components of the large ribosomal subunit RPL3, RPL7, RPL26 and RPL27 (PubMed:26100019). Binds to mRNA (PubMed:26100019). Interacts (via the helicase C-terminal domain) with MAVS (PubMed:24037184). Binds to double-stranded RNA (via the helicase C-terminal domain) (PubMed:24037184). {ECO:0000269|PubMed:21930779, ECO:0000269|PubMed:24037184, ECO:0000269|PubMed:26100019}. +Q8VHK9 DHX36_MOUSE ATP-dependent DNA/RNA helicase DHX36 (EC 3.6.4.13) (DEAD/H box polypeptide 36) (DEAH box protein 36) (MLE-like protein 1) (RNA helicase associated with AU-rich element ARE) 1001 113,883 Binding site (1); Chain (1); Coiled coil (1); Compositional bias (1); Domain (2); Metal binding (2); Modified residue (3); Motif (2); Nucleotide binding (2); Region (14); Sequence conflict (3) FUNCTION: Multifunctional ATP-dependent helicase that unwinds G-quadruplex (G4) structures (PubMed:25611385). Plays a role in many biological processes such as genomic integrity, gene expression regulations and as a sensor to initiate antiviral responses (PubMed:21703541, PubMed:21590736). G4 structures correspond to helical structures containing guanine tetrads (By similarity). Binds with high affinity to and unwinds G4 structures that are formed in nucleic acids (G4-ADN and G4-RNA) (By similarity). Plays a role in genomic integrity (By similarity). Converts the G4-RNA structure present in telomerase RNA template component (TREC) into a double-stranded RNA to promote P1 helix formation that acts as a template boundary ensuring accurate reverse transcription (By similarity). Plays a role in transcriptional regulation. Resolves G4-DNA structures in promoters of genes, such as YY1, KIT/c-kit and ALPL and positively regulates their expression (PubMed:25611385) (By similarity). Plays a role in post-transcriptional regulation (By similarity). Unwinds a G4-RNA structure located in the 3'-UTR polyadenylation site of the pre-mRNA TP53 and stimulates TP53 pre-mRNA 3'-end processing in response to ultraviolet (UV)-induced DNA damage (By similarity). Binds to the precursor-microRNA-134 (pre-miR-134) terminal loop and regulates its transport into the synapto-dendritic compartment (By similarity). Involved in the pre-miR-134-dependent inhibition of target gene expression and the control of dendritic spine size (By similarity). Plays a role in the regulation of cytoplasmic mRNA translation and mRNA stability (By similarity). Binds to both G4-RNA structures and alternative non-quadruplex-forming sequence within the 3'-UTR of the PITX1 mRNA regulating negatively PITX1 protein expression (By similarity). Binds to both G4-RNA structure in the 5'-UTR and AU-rich elements (AREs) localized in the 3'-UTR of NKX2-5 mRNA to either stimulate protein translation or induce mRNA decay in an ELAVL1-dependent manner, respectively (By similarity). Binds also to ARE sequences present in several mRNAs mediating exosome-mediated 3'-5' mRNA degradation (By similarity). Involved in cytoplasmic urokinase-type plasminogen activator (uPA) mRNA decay (By similarity). Component of a multi-helicase-TICAM1 complex that acts as a cytoplasmic sensor of viral double-stranded RNA (dsRNA) and plays a role in the activation of a cascade of antiviral responses including the induction of proinflammatory cytokines via the adapter molecule TICAM1 (PubMed:21703541). Required for the early embryonic development and hematopoiesis (PubMed:22422825). Involved in the regulation of cardioblast differentiation and proliferation during heart development (PubMed:26489465). Involved in spermatogonia differentiation (PubMed:25611385). May play a role in ossification (PubMed:21590736). {ECO:0000250|UniProtKB:D4A2Z8, ECO:0000250|UniProtKB:Q05B79, ECO:0000250|UniProtKB:Q9H2U1, ECO:0000269|PubMed:21590736, ECO:0000269|PubMed:21703541, ECO:0000269|PubMed:22422825, ECO:0000269|PubMed:25611385, ECO:0000269|PubMed:26489465}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H2U1}. Cytoplasm {ECO:0000250|UniProtKB:Q9H2U1}. Cytoplasm, cytosol {ECO:0000269|PubMed:21703541}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q9H2U1}. Nucleus speckle {ECO:0000250|UniProtKB:Q9H2U1}. Chromosome, telomere {ECO:0000250|UniProtKB:Q9H2U1}. Mitochondrion {ECO:0000269|PubMed:21703541}. Perikaryon {ECO:0000250|UniProtKB:D4A2Z8}. Cell projection, dendrite {ECO:0000250|UniProtKB:D4A2Z8}. Cell projection, axon {ECO:0000250|UniProtKB:D4A2Z8}. Note=Predominantly localized in the nucleus. Colocalizes with SRSF2 in nuclear speckles. Colocalizes with DDX5 in nucleolar caps upon transcription inhibition. Accumulates and colocalized with TIA1 in cytoplasmic stress granules (SGs) in an arsenite-, heat shock- and RNA-binding-dependent manner. Shuttles into and out of SGs in an ATPase-dependent manner (By similarity). Colocalizes in the cytosol with the multi-helicase-TICAM1 complex that translocates to the mitochondria upon poly(I:C) stimulation (PubMed:21703541). {ECO:0000250|UniProtKB:Q9H2U1, ECO:0000269|PubMed:21703541}. SUBUNIT: Found in a multi-helicase-TICAM1 complex at least composed of DHX36, DDX1, DDX21 and TICAM1; this complex exists in resting cells with or without dsRNA poly(I:C) ligand stimulation (PubMed:21703541). Interacts (via C-terminus) with TICAM1 (via TIR domain) (PubMed:21703541). Interacts (via C-terminus) with DDX21; this interaction serves as bridges to TICAM1 (PubMed:21703541). Interacts with TERT; this interaction is dependent on the ability of DHX36 to bind to the G-quadruplex RNA (G4-RNA) structure present in the telomerase RNA template component (TERC). Interacts with DKC1; this interaction is dependent on the ability of DHX36 to bind to the G4-RNA structure present in TERC. Interacts with PARN; this interaction stimulates PARN to enhance uPA mRNA decay. Interacts with EXOSC3; this interaction occurs in a RNase-insensitive manner. Interacts with EXOSC10; this interaction occurs in a RNase-insensitive manner. Interacts with ILF3; this interaction occurs in a RNA-dependent manner. Interacts with ELAVL1; this interaction occurs in an RNA-dependent manner. Interacts with DDX5; this interaction occurs in a RNA-dependent manner. Interacts with DDX17; this interaction occurs in a RNA-dependent manner. Interacts with HDAC1; this interaction occurs in a RNA-dependent manner (By similarity) (PubMed:21590736). Interacts with HDAC3; this interaction occurs in a RNA-dependent manner (By similarity). Interacts with HDAC4 (PubMed:21590736). Interacts with AGO1. Interacts with AGO2 (By similarity). {ECO:0000250|UniProtKB:Q9H2U1, ECO:0000269|PubMed:21590736, ECO:0000269|PubMed:21703541}. DOMAIN: The DHX36-specific motif (DSM) form folds into a DNA-binding-induced alpha-helix that together with the oligonucleotide and oligosaccharide-binding-fold-like (OB-fold-like) subdomain bind to Myc-promoter G4-DNA-containing structure in an ATP-dependent manner. Upon G4-DNA-binding, DHX36 pulls on DSM in the 3'-direction, inducing rearrangement of the RecA-like 1 and 2 and the degenerate-winged-helix (WH) regions; these rearrangements are propbably responsible for the ATP-independent repetitive G4-DNA unfolding activity, one residue at a time. Upon resolving of G4-DNA into separate nucleotide strands, and ATP hydrolysis, the apoprotein of DHX36 seems incompatible with G4-DNA-binding (By similarity). The N-terminus is necessary for its recruitment to cytoplasmic stress granules (SGs) upon arsenite-induced treatment (By similarity). {ECO:0000250|UniProtKB:Q05B79, ECO:0000250|UniProtKB:Q9H2U1}. TISSUE SPECIFICITY: Expressed in spermatogonia stem cells and primary spermatocytes (at protein level) (PubMed:25611385). Expressed strongly in testis. Weakly expressed in heart, lung, liver, kidney, small intestine, spleen, lymphe node and thymus (PubMed:25611385). {ECO:0000269|PubMed:25611385}. +Q9CZJ9 DJC18_MOUSE DnaJ homolog subfamily C member 18 357 41,434 Chain (1); Domain (1); Sequence conflict (1); Transmembrane (1) TRANSMEM 227 247 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +P70175 DLG3_MOUSE Disks large homolog 3 (Synapse-associated protein 102) (SAP-102) (SAP102) 849 93,482 Chain (1); Domain (5); Modified residue (2) FUNCTION: Required for learning most likely through its role in synaptic plasticity following NMDA receptor signaling. {ECO:0000250}. SUBUNIT: Interacts through its PDZ domains with NETO1, GRIN2B, SYNGAP1 and APC. Interacts through its first two PDZ domains with ERBB4. Interacts through its third PDZ domain with NLGN1, and probably with NLGN2 and NLGN3. Interacts through its guanylate kinase-like domain with DLGAP1, DLGAP2, DLGAP3 and DLGAP4 (By similarity). Interacts with FRMPD4 (via C-terminus) (By similarity). Interacts with LRFN1, LRFN2 and LRFN4 (By similarity). Interacts with FLTP. Interacts with GPR85 (PubMed:25780553). {ECO:0000250, ECO:0000269|PubMed:25296022, ECO:0000269|PubMed:25780553}. +Q08274 DMWD_MOUSE Dystrophia myotonica WD repeat-containing protein (Dystrophia myotonica-containing WD repeat motif protein) (Protein DMR-N9) 665 69,816 Chain (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (3); Repeat (6); Sequence conflict (2) SUBCELLULAR LOCATION: Perikaryon {ECO:0000269|PubMed:12691844}. Cell projection, dendrite {ECO:0000269|PubMed:12691844}. Nucleus {ECO:0000269|PubMed:12691844}. Note=In neurons, shows punctate expression throughout the cell body, nucleus and dendrites. Not detected in axons. {ECO:0000269|PubMed:12691844}. TISSUE SPECIFICITY: Widely expressed in brain where it localizes to the olfactory bulb, forebrain, thalamus, hippocampus, cerebellum, cortex and hypothalamus (at protein level) (PubMed:12691844). Expression seems to be particularly strong in areas of high synaptic density such as the glomerular layer of the olfactory bulb, and mossy fiber terminal fields of the hippocampus (at protein level) (PubMed:12691844). Expressed in retina, with strongest expression in the external and internal plexiform layers (at protein level) (PubMed:12691844). Strongly expressed in brain and testis (PubMed:7633444, PubMed:1302022). Also detected at lower levels in heart, kidney, liver, lung, ovary, uterus, bladder and skeletal muscle (PubMed:7633444, PubMed:1302022). In testis, expression seems to be restricted to secondary spermatocytes (PubMed:1302022). {ECO:0000269|PubMed:12691844, ECO:0000269|PubMed:1302022, ECO:0000269|PubMed:7633444}. +O70421 FZD1_MOUSE Frizzled-1 (Fz-1) (mFz1) 642 71,127 Chain (1); Compositional bias (1); Disulfide bond (5); Domain (1); Glycosylation (2); Motif (2); Sequence conflict (7); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 318 338 Helical; Name=1. {ECO:0000255}.; TRANSMEM 350 370 Helical; Name=2. {ECO:0000255}.; TRANSMEM 398 418 Helical; Name=3. {ECO:0000255}.; TRANSMEM 441 461 Helical; Name=4. {ECO:0000255}.; TRANSMEM 485 505 Helical; Name=5. {ECO:0000255}.; TRANSMEM 532 552 Helical; Name=6. {ECO:0000255}.; TRANSMEM 594 614 Helical; Name=7. {ECO:0000255}. TOPO_DOM 69 317 Extracellular. {ECO:0000255}.; TOPO_DOM 339 349 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 371 397 Extracellular. {ECO:0000255}.; TOPO_DOM 419 440 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 462 484 Extracellular. {ECO:0000255}.; TOPO_DOM 506 531 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 553 593 Extracellular. {ECO:0000255}.; TOPO_DOM 615 642 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for Wnt proteins (PubMed:15923619). Activated by WNT7B (PubMed:15923619). Activated by WNT3A, WNT3, WNT1 and to a lesser extent WNT2, but apparently not by WNT4, WNT5A, WNT5B, WNT6, WNT7A or WNT7B (By similarity). Contradictory results showing activation by WNT7B have been described for mouse (PubMed:15923619). Functions in the canonical Wnt/beta-catenin signaling pathway (PubMed:15923619). The canonical Wnt/beta-catenin signaling pathway leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes (PubMed:15923619). A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues (Probable). {ECO:0000250|UniProtKB:Q9UP38, ECO:0000269|PubMed:15923619, ECO:0000305}. PTM: Ubiquitinated by ZNRF3, leading to its degradation by the proteasome. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15923619}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Interacts with MYOC (By similarity). Interacts with WNT7B (PubMed:15923619). {ECO:0000250|UniProtKB:Q9UP38, ECO:0000269|PubMed:15923619}. DOMAIN: Lys-Thr-X-X-X-Trp motif interacts with the PDZ domain of Dvl (Disheveled) family members and is involved in the activation of the Wnt/beta-catenin signaling pathway. {ECO:0000250}.; DOMAIN: The FZ domain is involved in binding with Wnt ligands. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in chondrocytes. +Q9JIP6 FZD2_MOUSE Frizzled-2 (Fz-2) (mFz2) (Frizzled-10) (Fz-10) (mFz10) 570 64,059 Chain (1); Compositional bias (1); Disulfide bond (5); Domain (1); Glycosylation (2); Motif (2); Sequence conflict (1); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 253 273 Helical; Name=1. {ECO:0000255}.; TRANSMEM 285 305 Helical; Name=2. {ECO:0000255}.; TRANSMEM 333 353 Helical; Name=3. {ECO:0000255}.; TRANSMEM 376 396 Helical; Name=4. {ECO:0000255}.; TRANSMEM 420 440 Helical; Name=5. {ECO:0000255}.; TRANSMEM 467 487 Helical; Name=6. {ECO:0000255}.; TRANSMEM 525 545 Helical; Name=7. {ECO:0000255}. TOPO_DOM 29 252 Extracellular. {ECO:0000255}.; TOPO_DOM 274 284 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 306 332 Extracellular. {ECO:0000255}.; TOPO_DOM 354 375 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 397 419 Extracellular. {ECO:0000255}.; TOPO_DOM 441 466 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 488 524 Extracellular. {ECO:0000255}.; TOPO_DOM 546 570 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for Wnt proteins. Most of frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues. PTM: Ubiquitinated by ZNRF3, leading to its degradation by the proteasome. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. DOMAIN: Lys-Thr-X-X-X-Trp motif interacts with the PDZ domain of Dvl (Disheveled) family members and is involved in the activation of the Wnt/beta-catenin signaling pathway. {ECO:0000250}.; DOMAIN: The FZ domain is involved in binding with Wnt ligands. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in embryonic and adult heart, lung, chondrocytes and brain. Also expressed in the developing gastrointestinal tract (strongest in foregut), much weaker expression in the adult. No expression in fetal liver and adult spleen. Up-regulated in esophageal squamous cell carcinomas. +Q61088 FZD4_MOUSE Frizzled-4 (Fz-4) (mFz4) (CD antigen CD344) 537 60,143 Chain (1); Disulfide bond (5); Domain (1); Glycosylation (2); Motif (2); Sequence conflict (1); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 223 243 Helical; Name=1. {ECO:0000255}.; TRANSMEM 255 275 Helical; Name=2. {ECO:0000255}.; TRANSMEM 303 323 Helical; Name=3. {ECO:0000255}.; TRANSMEM 345 365 Helical; Name=4. {ECO:0000255}.; TRANSMEM 390 410 Helical; Name=5. {ECO:0000255}.; TRANSMEM 437 457 Helical; Name=6. {ECO:0000255}.; TRANSMEM 478 498 Helical; Name=7. {ECO:0000255}. TOPO_DOM 37 222 Extracellular. {ECO:0000255}.; TOPO_DOM 244 254 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 276 302 Extracellular. {ECO:0000255}.; TOPO_DOM 324 344 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 366 389 Extracellular. {ECO:0000255}.; TOPO_DOM 411 436 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 458 477 Extracellular. {ECO:0000255}.; TOPO_DOM 499 537 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for Wnt proteins. Most of frizzled receptors are coupled to the beta-catenin (CTNNB1) canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin (CTNNB1) and activation of Wnt target genes. Plays a critical role in retinal vascularization by acting as a receptor for Wnt proteins and norrin (NDP). In retina, it can be both activated by Wnt protein-binding, but also by a Wnt-independent signaling via binding of norrin (NDP), promoting in both cases beta-catenin (CTNNB1) accumulation and stimulation of LEF/TCF-mediated transcriptional programs. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues. Activation by Wnt5A stimulates PKC activity via a G-protein-dependent mechanism. {ECO:0000269|PubMed:10097073, ECO:0000269|PubMed:19837033}. PTM: Ubiquitinated by ZNRF3, leading to its degradation by the proteasome. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10097073}; Multi-pass membrane protein {ECO:0000269|PubMed:10097073}. Cell membrane {ECO:0000269|PubMed:10097073}; Multi-pass membrane protein {ECO:0000269|PubMed:10097073}. SUBUNIT: Interacts with MAGI3 and NDP (PubMed:15035989, PubMed:15195140). Component of a complex, at least composed of TSPAN12, FZD4 and norrin (NDP) (PubMed:19837033). Interacts (via FZ domain) with TSKU (PubMed:21856951). Interacts with glypican GPC3 (By similarity). {ECO:0000250|UniProtKB:Q9ULV1, ECO:0000269|PubMed:15035989, ECO:0000269|PubMed:15195140, ECO:0000269|PubMed:19837033, ECO:0000269|PubMed:21856951}. DOMAIN: Lys-Thr-X-X-X-Trp motif interacts with the PDZ domain of Dvl (Disheveled) family members and is involved in the activation of the Wnt/beta-catenin signaling pathway. {ECO:0000250}.; DOMAIN: The FZ domain is involved in binding with Wnt ligands. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in chondrocytes. +Q61090 FZD7_MOUSE Frizzled-7 (Fz-7) (mFz7) 572 63,733 Chain (1); Disulfide bond (5); Domain (1); Glycosylation (2); Motif (2); Sequence conflict (2); Signal peptide (1); Site (1); Topological domain (8); Transmembrane (7) TRANSMEM 255 275 Helical; Name=1. {ECO:0000255}.; TRANSMEM 287 307 Helical; Name=2. {ECO:0000255}.; TRANSMEM 335 355 Helical; Name=3. {ECO:0000255}.; TRANSMEM 378 398 Helical; Name=4. {ECO:0000255}.; TRANSMEM 422 442 Helical; Name=5. {ECO:0000255}.; TRANSMEM 469 489 Helical; Name=6. {ECO:0000255}.; TRANSMEM 527 547 Helical; Name=7. {ECO:0000255}. TOPO_DOM 33 254 Extracellular. {ECO:0000255}.; TOPO_DOM 276 286 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 308 334 Extracellular. {ECO:0000255}.; TOPO_DOM 356 377 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 399 421 Extracellular. {ECO:0000255}.; TOPO_DOM 443 468 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 490 526 Extracellular. {ECO:0000255}.; TOPO_DOM 548 572 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for Wnt proteins. Most of frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues. Activation by Wnt8 induces expression of beta-catenin target genes. {ECO:0000269|PubMed:10097073, ECO:0000269|PubMed:15353129}. PTM: Ubiquitinated by ZNRF3, leading to its degradation by the proteasome. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10097073, ECO:0000269|PubMed:15353129}; Multi-pass membrane protein {ECO:0000269|PubMed:10097073, ECO:0000269|PubMed:15353129}. Endosome membrane {ECO:0000250|UniProtKB:O75084}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O75084}. Note=Associated to the plasma membrane in the presence of FZD7 and phosphatidylinositol 4,5-bisphosphate (PIP2). Localized in recycling endosomes in other conditions. {ECO:0000250|UniProtKB:O75084}. SUBUNIT: Interacts with MAGI3 and DVL1. Interacts with MYOC (By similarity). Binds to SDCBP; this interaction is increased by inositol trisphosphate (IP3) (By similarity). Interacts with glypican GPC3 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O75084}. DOMAIN: Lys-Thr-X-X-X-Trp motif interacts with the PDZ domain of Dvl (Disheveled) family members and is involved in the activation of the Wnt/beta-catenin signaling pathway. {ECO:0000250}.; DOMAIN: The FZ domain is involved in binding with Wnt ligands. {ECO:0000250}. +E9Q8T7 DYH1_MOUSE Dynein heavy chain 1, axonemal (Axonemal beta dynein heavy chain 1) (Ciliary dynein heavy chain 1) (mDHC7) 4250 487,070 Alternative sequence (2); Chain (1); Coiled coil (1); Motif (2); Nucleotide binding (4); Region (8); Sequence conflict (10) FUNCTION: Force generating protein of cilia required for sperm flagellum motility (PubMed:11371505). Produces force towards the minus ends of microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP (By similarity). Required in spermatozoa for the formation of the inner dynein arms and biogenesis of the axoneme (By similarity). {ECO:0000250|UniProtKB:Q9P2D7, ECO:0000269|PubMed:11371505}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q9P2D7}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:11371505}. SUBUNIT: Consists of at least two heavy chains and a number of intermediate and light chains. {ECO:0000250|UniProtKB:Q8TE73}. +Q8BW94 DYH3_MOUSE Dynein heavy chain 3, axonemal (Axonemal beta dynein heavy chain 3) (Ciliary dynein heavy chain 3) 4083 467,777 Alternative sequence (5); Chain (1); Coiled coil (3); Erroneous initiation (1); Nucleotide binding (4); Region (8); Sequence conflict (5) FUNCTION: Force generating protein of respiratory cilia. Produces force towards the minus ends of microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Involved in sperm motility; implicated in sperm flagellar assembly (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000305}. SUBUNIT: Consists of at least two heavy chains and a number of intermediate and light chains. DOMAIN: Dynein heavy chains probably consist of an N-terminal stem (which binds cargo and interacts with other dynein components), and the head or motor domain. The motor contains six tandemly-linked AAA domains in the head, which form a ring. A stalk-like structure (formed by two of the coiled coil domains) protrudes between AAA 4 and AAA 5 and terminates in a microtubule-binding site. A seventh domain may also contribute to this ring; it is not clear whether the N-terminus or the C-terminus forms this extra domain. There are four well-conserved and two non-conserved ATPase sites, one per AAA domain. Probably only one of these (within AAA 1) actually hydrolyzes ATP, the others may serve a regulatory function (By similarity). {ECO:0000250}. +Q9Z188 DYR1B_MOUSE Dual specificity tyrosine-phosphorylation-regulated kinase 1B (EC 2.7.12.1) 629 69,178 Active site (1); Alternative sequence (2); Binding site (1); Chain (1); Compositional bias (2); Domain (1); Modified residue (10); Motif (1); Nucleotide binding (2); Region (1); Sequence conflict (2) FUNCTION: Dual-specificity kinase which possesses both serine/threonine and tyrosine kinase activity. Enhances the transcriptional activity of TCF1/HNF1A and FOXO1. Inhibits epithelial cell migration. Mediates colon carcinoma cell survival in mitogen-poor environments. Inhibits the SHH and WNT1 pathways, thereby enhancing adipogenesis. In addition, promotes expression of the gluconeogenic enzyme glucose-6-phosphatase (G6PC). {ECO:0000250|UniProtKB:Q9Y463, ECO:0000269|PubMed:12633499}. PTM: Phosphorylated by MAP kinase. Tyrosine phosphorylation may be required for dimerization (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Dimer. Interacts with DCOHM, MAP2K3/MKK3 and TCF1/HNF1A. Part of a complex consisting of RANBP9, RAN, DYRK1B and COPS5 (By similarity). Interacts with DCAF7 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Isoform 1 and isoform 2 are broadly expressed. Isoform 3 seems specific for skeletal muscle (at protein level). {ECO:0000269|PubMed:12633499}. +Q3V0Q1 DYH12_MOUSE Dynein heavy chain 12, axonemal (Axonemal beta dynein heavy chain 12) (Axonemal dynein heavy chain 12-like protein) (Axonemal dynein heavy chain 7-like protein) (Ciliary dynein heavy chain 12) 3086 356,231 Chain (1); Coiled coil (2); Motif (2); Nucleotide binding (4); Region (7) Protein modification; protein ubiquitination. FUNCTION: Force generating protein of respiratory cilia. Produces force towards the minus ends of microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Involved in sperm motility; implicated in sperm flagellar assembly (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000305}. SUBUNIT: Consists of at least two heavy chains and a number of intermediate and light chains. DOMAIN: Dynein heavy chains probably consist of an N-terminal stem (which binds cargo and interacts with other dynein components), and the head or motor domain. The motor contains six tandemly-linked AAA domains in the head, which form a ring. A stalk-like structure (formed by two of the coiled coil domains) protrudes between AAA 4 and AAA 5 and terminates in a microtubule-binding site. A seventh domain may also contribute to this ring; it is not clear whether the N-terminus or the C-terminus forms this extra domain. There are four well-conserved and two non-conserved ATPase sites, one per AAA domain. Probably only one of these (within AAA 1) actually hydrolyzes ATP, the others may serve a regulatory function (By similarity). {ECO:0000250}. +O88741 GDAP1_MOUSE Ganglioside-induced differentiation-associated protein 1 (GDAP1) 358 41,311 Alternative sequence (2); Chain (1); Cross-link (9); Domain (2); Modified residue (1); Region (1); Transmembrane (2) TRANSMEM 292 312 Helical. {ECO:0000255}.; TRANSMEM 320 340 Helical. {ECO:0000255}. FUNCTION: Regulates the mitochondrial network by promoting mitochondrial fission. {ECO:0000250, ECO:0000269|PubMed:16172208}. PTM: Ubiquitinated by PRKN during mitophagy, leading to its degradation and enhancement of mitophagy. Deubiquitinated by USP30. {ECO:0000250|UniProtKB:Q8TB36}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q8TB36}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8TB36}. Cytoplasm {ECO:0000269|PubMed:16172208}. SUBUNIT: Homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain, spinal cord, muscles and intestinal villi. In the central nervous system expressed most prominently in the cortex, cerebellum, thalamus, olfactory bulb, and spinal cord. Expressed also in sciatic nerves and in dorsal root ganglia. {ECO:0000269|PubMed:16172208}. +Q9CZR8 EFTS_MOUSE Elongation factor Ts, mitochondrial (EF-Ts) (EF-TsMt) 324 35,334 Chain (1); Modified residue (4); Transit peptide (1) FUNCTION: Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome. {ECO:0000255|HAMAP-Rule:MF_03135}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03135}. +Q01279 EGFR_MOUSE Epidermal growth factor receptor (EC 2.7.10.1) 1210 134,853 Active site (1); Binding site (2); Chain (1); Cross-link (6); Disulfide bond (25); Domain (1); Glycosylation (10); Lipidation (2); Modified residue (22); Nucleotide binding (2); Region (1); Repeat (2); Sequence conflict (3); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 648 670 Helical. {ECO:0000255}. TOPO_DOM 25 647 Extracellular. {ECO:0000255}.; TOPO_DOM 671 1210 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor tyrosine kinase binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses (PubMed:8404850). Known ligands include EGF, TGFA/TGF-alpha, AREG, epigen/EPGN, BTC/betacellulin, epiregulin/EREG and HBEGF/heparin-binding EGF. Ligand binding triggers receptor homo- and/or heterodimerization and autophosphorylation on key cytoplasmic residues. The phosphorylated receptor recruits adapter proteins like GRB2 which in turn activates complex downstream signaling cascades. Activates at least 4 major downstream signaling cascades including the RAS-RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC and STATs modules. May also activate the NF-kappa-B signaling cascade. Also directly phosphorylates other proteins like RGS16, activating its GTPase activity and probably coupling the EGF receptor signaling to the G protein-coupled receptor signaling. Also phosphorylates MUC1 and increases its interaction with SRC and CTNNB1/beta-catenin (By similarity). Plays a role in enhancing learning and memory performance (PubMed:20639532). {ECO:0000250|UniProtKB:P00533, ECO:0000269|PubMed:10953014, ECO:0000269|PubMed:20639532, ECO:0000269|PubMed:8404850}. PTM: Monoubiquitinated and polyubiquitinated upon EGF stimulation; which does not affect tyrosine kinase activity or signaling capacity but may play a role in lysosomal targeting. Polyubiquitin linkage is mainly through 'Lys-63', but linkage through 'Lys-48', 'Lys-11' and 'Lys-29' also occurs. Deubiquitinated by OTUD7B, preventing degradation (By similarity). Ubiquitinated by RNF115 and RNF126. {ECO:0000250|UniProtKB:P00533, ECO:0000269|PubMed:23418353}.; PTM: Phosphorylated on Tyr residues in response to EGF. Phosphorylation at Ser-697 is partial and occurs only if Thr-695 is phosphorylated. Phosphorylation at Thr-680 and Thr-695 by PRKD1 inhibits EGF-induced MAPK8/JNK1 activation. Dephosphorylation by PTPRJ prevents endocytosis and stabilizes the receptor at the plasma membrane. Autophosphorylation at Tyr-1199 is stimulated by methylation at Arg-1199 and enhances interaction with PTPN6. Autophosphorylation at Tyr-1092 and/or Tyr-1110 recruits STAT3. Dephosphorylated by PTPN1 and PTPN2. {ECO:0000250|UniProtKB:P00533}.; PTM: Palmitoylated on Cys residues by ZDHHC20. Palmitoylation inhibits internalization after ligand binding, and increases the persistence of tyrosine-phosphorylated EGFR at the cell membrane. Palmitoylation increases the amplitude and duration of EGFR signaling. {ECO:0000250|UniProtKB:P00533}.; PTM: Methylated. Methylation at Arg-1199 by PRMT5 stimulates phosphorylation at Tyr-1197. {ECO:0000250|UniProtKB:P00533}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P00533}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P00533}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P00533}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P00533}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P00533}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P00533}. Nucleus membrane {ECO:0000250|UniProtKB:P00533}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P00533}. Endosome {ECO:0000250|UniProtKB:P00533}. Endosome membrane {ECO:0000250|UniProtKB:P00533}. Nucleus {ECO:0000250|UniProtKB:P00533}. Note=In response to EGF, translocated from the cell membrane to the nucleus via Golgi and ER. Endocytosed upon activation by ligand. Colocalized with GPER1 in the nucleus of estrogen agonist-induced cancer-associated fibroblasts (CAF). {ECO:0000250|UniProtKB:P00533}. SUBUNIT: Binding of the ligand triggers homo- and/or heterodimerization of the receptor triggering its autophosphorylation. Heterodimer with ERBB2. Interacts with ERRFI1; inhibits dimerization of the kinase domain and autophosphorylation. Part of a complex with ERBB2 and either PIK3C2A or PIK3C2B. Interacts with GRB2; an adapter protein coupling the receptor to downstream signaling pathways. Interacts with GAB2; involved in signaling downstream of EGFR. Interacts with STAT3; mediates EGFR downstream signaling in cell proliferation. Interacts with RIPK1; involved in NF-kappa-B activation. Interacts (autophosphorylated) with CBL, CBLB and CBLC; involved in EGFR ubiquitination and regulation. Interacts with SOCS5; regulates EGFR degradation through ELOC- and ELOB-mediated ubiquitination and proteasomal degradation. Interacts with PRMT5; methylates EGFR and enhances interaction with PTPN6. Interacts (phosphorylated) with PTPN6; inhibits EGFR-dependent activation of MAPK/ERK. Interacts with COPG1; essential for regulation of EGF-dependent nuclear transport of EGFR by retrograde trafficking from the Golgi to the ER. Interacts with TNK2; this interaction is dependent on EGF stimulation and kinase activity of EGFR. Interacts with PCNA; positively regulates PCNA. Interacts with PELP1. Interacts with MUC1. Interacts with AP2M1. Interacts with FER. Interacts (via SH2 domains) with GRB2, NCK1 and NCK2. Interacts with EPS8; mediates EPS8 phosphorylation. Interacts with ATX2. Interacts with GAREM1. Interacts (ubiquitinated) with ANKRD13A/B/D; the interaction is direct and may regulate EGFR internalization after EGF stimulation. Interacts with GPER1; the interaction occurs in an estrogen-dependent manner. Interacts (via C-terminal cytoplasmic kinase domain) with ZPR1 (via zinc fingers). Interacts with RNF115 and RNF126. Interacts with GPRC5A (via its transmembrane domain) (PubMed:25744720). Interacts with FAM83B; positively regulates EGFR inducing its autophosphorylation in absence of stimulation by EGF (By similarity). Interacts with LAPTM4B; positively correlates with EGFR activation (By similarity). Interacts with STX19 (PubMed:16420529). {ECO:0000250|UniProtKB:P00533, ECO:0000269|PubMed:16420529, ECO:0000269|PubMed:23418353, ECO:0000269|PubMed:25744720, ECO:0000269|PubMed:8404850}. +Q99MS7 EH1L1_MOUSE EH domain-binding protein 1-like protein 1 (Tangerin) 1716 184,834 Alternative sequence (4); Chain (1); Coiled coil (2); Compositional bias (5); Domain (3); Modified residue (13); Motif (1); Region (1); Sequence conflict (6) FUNCTION: May act as Rab effector protein and play a role in vesicle trafficking (By similarity). Involved in apical-directed transport in polarized epithelial cells; the functions seems to implicate Rab8, BIN1 and possibly DNM1 (PubMed:26833786). {ECO:0000250|UniProtKB:Q8N3D4}. PTM: Prenylated (Probable). Farnelysation (predominant) and geranylgeranylation has been observed in vitro. {ECO:0000250|UniProtKB:Q8N3D4}. SUBCELLULAR LOCATION: Endosome {ECO:0000250|UniProtKB:Q8N3D4}. Recycling endosome {ECO:0000269|PubMed:26833786}. SUBUNIT: Interacts with RAB8A, RAB8B, RAB10, RAB13 and RAB15 (in their GTP-bound forms); at least in case of RAB8A can bind 2 molecules of RAB8A simultaneously. Interacts with BIN1 and AMPH. Interacts with DNM1. {ECO:0000250|UniProtKB:Q8N3D4, ECO:0000269|PubMed:26833786}. DOMAIN: The CAAX motif is a signal for prenylation and required for endosomal colocalization with Rab8 and Rab10. {ECO:0000250|UniProtKB:Q8N3D4}.; DOMAIN: The bivalent Mical/EHBP Rab binding (bMERB) domain, mediates binding to Rab8, Rab10, Rab10, Rab13 and Rab15 (in their GTP-bound forms). {ECO:0000250|UniProtKB:Q8N3D4}. +Q8CHW4 EI2BE_MOUSE Translation initiation factor eIF-2B subunit epsilon (eIF-2B GDP-GTP exchange factor subunit epsilon) 717 80,086 Chain (1); Cross-link (5); Domain (1); Modified residue (11); Sequence conflict (1) FUNCTION: Catalyzes the exchange of eukaryotic initiation factor 2-bound GDP for GTP. {ECO:0000250}. PTM: Phosphorylated at Ser-540 by DYRK2; this is required for subsequent phosphorylation by GSK3B. Phosphorylated on serine and threonine residues by GSK3B; phosphorylation inhibits its function (By similarity). {ECO:0000250}.; PTM: Polyubiquitinated, probably by NEDD4. {ECO:0000250}. SUBUNIT: Complex of five different subunits; alpha, beta, gamma, delta and epsilon. Interacts with RGS2 (By similarity). {ECO:0000250}. +Q3THJ3 EIF1A_MOUSE Probable RNA-binding protein EIF1AD (Eukaryotic translation initiation factor 1A domain-containing protein) 170 19,520 Chain (1); Compositional bias (1); Domain (1); Modified residue (7); Motif (2); Sequence conflict (3) FUNCTION: Plays a role into cellular response to oxidative stress. Decreases cell proliferation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with GAPDH and STAT1. {ECO:0000250}. +Q8BH64 EHD2_MOUSE EH domain-containing protein 2 543 61,174 Beta strand (13); Binding site (2); Calcium binding (1); Chain (1); Domain (3); Helix (28); Modified residue (7); Mutagenesis (10); Nucleotide binding (1); Region (6); Sequence conflict (1); Turn (2) FUNCTION: ATP- and membrane-binding protein that controls membrane reorganization/tubulation upon ATP hydrolysis (PubMed:24508342). Plays a role in membrane trafficking between the plasma membrane and endosomes. Important for the internalization of GLUT4 (PubMed:14676205). Required for fusion of myoblasts to skeletal muscle myotubes. Required for normal translocation of FER1L5 to the plasma membrane (PubMed:18502764, PubMed:21177873). Regulates the equilibrium between cell surface-associated and cell surface-dissociated caveolae by constraining caveolae at the cell membrane (By similarity). {ECO:0000250|UniProtKB:Q9NZN4, ECO:0000269|PubMed:14676205, ECO:0000269|PubMed:18502764, ECO:0000269|PubMed:21177873, ECO:0000269|PubMed:24508342}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14676205}; Peripheral membrane protein {ECO:0000269|PubMed:14676205}; Cytoplasmic side {ECO:0000269|PubMed:14676205}. Membrane, caveola {ECO:0000269|PubMed:24508342}; Peripheral membrane protein {ECO:0000269|PubMed:24508342}; Cytoplasmic side {ECO:0000269|PubMed:24508342}. Endosome membrane {ECO:0000250|UniProtKB:Q4V8H8}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q4V8H8}; Cytoplasmic side {ECO:0000250|UniProtKB:Q4V8H8}. Cytoplasm, cytosol {ECO:0000269|PubMed:14676205}. Note=Colocalizes with GLUT4 in intracellular tubulovesicular structures that are associated with cortical F-actin (PubMed:14676205). Colocalizes with FER1L5 at plasma membrane in myoblasts and myotubes (PubMed:18502764). {ECO:0000269|PubMed:14676205, ECO:0000269|PubMed:18502764}. SUBUNIT: Homodimer and homooligomer (By similarity). Interacts with EHD1 (By similarity). May also interact with EHD3 and EHD4 (By similarity). Interacts with MYOF (PubMed:18502764, PubMed:21177873). Interacts with EHBP1 (PubMed:14676205). Interacts with FER1L5 (via second C2 domain) (PubMed:21177873). Interacts with CAV1 in a cholesterol-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q9NZN4, ECO:0000269|PubMed:14676205, ECO:0000269|PubMed:17914359, ECO:0000269|PubMed:18502764, ECO:0000269|PubMed:21177873}. DOMAIN: The EH domain interacts with Asn-Pro-Phe (NPF) motifs of target proteins. {ECO:0000269|PubMed:14676205}. TISSUE SPECIFICITY: Detected in lung and adipocytes. Detected at lower levels in heart and skeletal muscle. {ECO:0000269|PubMed:14676205}. +Q8CI75 DI3L2_MOUSE DIS3-like exonuclease 2 (EC 3.1.13.-) 870 97,775 Alternative sequence (1); Beta strand (33); Chain (1); Frameshift (1); Helix (21); Metal binding (2); Modified residue (4); Mutagenesis (7); Site (1); Turn (5) FUNCTION: 3'-5'-exoribonuclease that specifically recognizes RNAs polyuridylated at their 3' end and mediates their degradation. Component of an exosome-independent RNA degradation pathway that mediates degradation of both mRNAs and miRNAs that have been polyuridylated by a terminal uridylyltransferase, such as ZCCHC11/TUT4. Mediates degradation of cytoplasmic mRNAs that have been deadenylated and subsequently uridylated at their 3'. Mediates degradation of uridylated pre-let-7 miRNAs, contributing to the maintenance of embryonic stem (ES) cells. Essential for correct mitosis, and negatively regulates cell proliferation. {ECO:0000255|HAMAP-Rule:MF_03045, ECO:0000269|PubMed:23594738, ECO:0000269|PubMed:25119025}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03045, ECO:0000269|PubMed:23594738}. Cytoplasm, P-body {ECO:0000255|HAMAP-Rule:MF_03045}. SUBUNIT: Interacts with XRN1. {ECO:0000250|UniProtKB:Q8IYB7}. DOMAIN: Specifically recognizes and binds polyuridylated RNAs via 3 RNA-binding regions (named U-zone 1, U-zone 2 and U-zone 3) that form an open funnel on one face of the catalytic domain, allowing RNA to navigate a path to the active site. {ECO:0000269|PubMed:25119025}. +Q91Z61 DIRA1_MOUSE GTP-binding protein Di-Ras1 (Distinct subgroup of the Ras family member 1) (Small GTP-binding tumor suppressor 1) 198 22,265 Binding site (1); Chain (1); Lipidation (1); Modified residue (1); Motif (1); Nucleotide binding (5); Propeptide (1) FUNCTION: Displays low GTPase activity and exists predominantly in the GTP-bound form. {ECO:0000250|UniProtKB:O95057}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. +Q8C3I9 DIK2B_MOUSE Divergent protein kinase domain 2B (Deleted in autism-related protein 1 homolog) 435 49,042 Chain (1); Glycosylation (2); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q3UH60 DIP2B_MOUSE Disco-interacting protein 2 homolog B (DIP2 homolog B) 1574 171,126 Alternative sequence (2); Chain (1); Compositional bias (4); Domain (1); Erroneous initiation (1); Modified residue (13); Sequence conflict (1) +O70133 DHX9_MOUSE ATP-dependent RNA helicase A (EC 3.6.4.13) (DEAH box protein 9) (mHEL-5) (Nuclear DNA helicase II) (NDH II) (RNA helicase A) (RHA) 1380 149,475 Alternative sequence (2); Beta strand (6); Chain (1); Compositional bias (1); Cross-link (1); Domain (4); Frameshift (1); Helix (5); Metal binding (2); Modified residue (20); Motif (3); Nucleotide binding (1); Region (14); Sequence caution (1); Sequence conflict (12); Turn (2) FUNCTION: Multifunctional ATP-dependent nucleic acid helicase that unwinds DNA and RNA in a 3' to 5' direction and that plays important roles in many processes, such as DNA replication, transcriptional activation, post-transcriptional RNA regulation, mRNA translation and RNA-mediated gene silencing. Requires a 3'-single-stranded tail as entry site for acid nuclei unwinding activities as well as the binding and hydrolyzing of any of the four ribo- or deoxyribo-nucleotide triphosphates (NTPs). Unwinds numerous nucleic acid substrates such as double-stranded (ds) DNA and RNA, DNA:RNA hybrids, DNA and RNA forks composed of either partially complementary DNA duplexes or DNA:RNA hybrids, respectively, and also DNA and RNA displacement loops (D- and R-loops), triplex-helical DNA (H-DNA) structure and DNA- and RNA-based G-quadruplexes. Binds dsDNA, single-stranded DNA (ssDNA), dsRNA, ssRNA and poly(A)-containing RNA. Binds also to circular dsDNA or dsRNA of either linear and/or circular forms and stimulates the relaxation of supercoiled DNAs catalyzed by topoisomerase TOP2A. Plays a role in DNA replication at origins of replication and cell cycle progression. Plays a role as a transcriptional coactivator acting as a bridging factor between polymerase II holoenzyme and transcription factors or cofactors, such as BRCA1, CREBBP, RELA and SMN1. Binds to the CDKN2A promoter. Plays several roles in post-transcriptional regulation of gene expression. In cooperation with NUP98, promotes pre-mRNA alternative splicing activities of a subset of genes (By similarity). As component of a large PER complex, is involved in the negative regulation of 3' transcriptional termination of circadian target genes such as PER1 and NR1D1 and the control of the circadian rhythms (PubMed:22767893). Acts also as a nuclear resolvase that is able to bind and neutralize harmful massive secondary double-stranded RNA structures formed by inverted-repeat Alu retrotransposon elements that are inserted and transcribed as parts of genes during the process of gene transposition (PubMed:28355180). Involved in the positive regulation of nuclear export of constitutive transport element (CTE)-containing unspliced mRNA. Component of the coding region determinant (CRD)-mediated complex that promotes cytoplasmic MYC mRNA stability. Plays a role in mRNA translation. Positively regulates translation of selected mRNAs through its binding to post-transcriptional control element (PCE) in the 5'-untranslated region (UTR). Involved with LARP6 in the translation stimulation of type I collagen mRNAs for CO1A1 and CO1A2 through binding of a specific stem-loop structure in their 5'-UTRs. Stimulates LIN28A-dependent mRNA translation probably by facilitating ribonucleoprotein remodeling during the process of translation. Plays also a role as a small interfering (siRNA)-loading factor involved in the RNA-induced silencing complex (RISC) loading complex (RLC) assembly, and hence functions in the RISC-mediated gene silencing process. Binds preferentially to short double-stranded RNA, such as those produced during rotavirus intestinal infection (PubMed:28636595). This interaction may mediate NLRP9 inflammasome activation and trigger inflammatory response, including IL18 release and pyroptosis (PubMed:28636595). Finally, mediates the attachment of heterogeneous nuclear ribonucleoproteins (hnRNPs) to actin filaments in the nucleus (By similarity). {ECO:0000250|UniProtKB:Q08211, ECO:0000269|PubMed:22767893, ECO:0000269|PubMed:28355180, ECO:0000269|PubMed:28636595}. PTM: Methylated. PRMT1-mediated methylation of undefined Arg residues in the nuclear transport domain (NTD) is required for nuclear import of DHX9. {ECO:0000250|UniProtKB:Q08211}.; PTM: Phosphorylated by PRKDC; phosphorylation occurs in a RNA-dependent manner. Phosphorylated by EIF2AK2/PKR; this phosphorylation reduces its association with double-stranded RNA. {ECO:0000250|UniProtKB:Q08211}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17303075}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q08211}. Nucleus, nucleolus {ECO:0000269|PubMed:10413677}. Cytoplasm {ECO:0000250|UniProtKB:Q08211}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q08211}. Note=Nucleoplasmic shuttling protein. Its nuclear import involves the nucleocytoplasmic transport receptor Importin alpha/Importin beta receptor pathway in a Ran-dependent manner. In interphase, localizes in nuclear stress granules and at perichromatin fibrils and in cytoplasmic ribonucleoprotein granules. Colocalizes with WRN and H2AFX at centrosomes in a microtubule-dependent manner following DNA damaging agent treatment. Excluded from the mitotic nucleus as early as prophase and re-entered the nucleus at telophase. Recruited in diffuse and discrete intranuclear foci (GLFG-body) in a NUP98-dependent manner (By similarity). Colocalizes with SP7 in the nucleus (PubMed:17303075). Colocalizes with ACTB at nuclear actin filaments inside the nucleus or at the nuclear pore. Colocalizes with HNRNPC at nuclear ribonucleoprotein complex proteins in the nucleus. Localized in cytoplasmic mRNP granules containing untranslated mRNAs (By similarity). {ECO:0000250|UniProtKB:Q08211, ECO:0000269|PubMed:17303075}. SUBUNIT: Component of the coding region determinant (CRD)-mediated complex, composed of DHX9, HNRNPU, IGF2BP1, SYNCRIP and YBX1. Identified in a mRNP complex, at least composed of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs (By similarity). The large PER complex involved in the repression of transcriptional termination is composed of at least PER2, CDK9, DDX5, DHX9, NCBP1 and POLR2A (active) (PubMed:22767893). Associates (via DRBM domains) with the RISC complex; this association occurs in a small interfering (siRNA)-dependent manner. Associates with the SMN complex; this association induces recruitment of DHX9 to the RNA polymerase II. Associates with polysomes in a LIN28A-dependent manner. Interacts (via C-terminus) with ACTB; this interaction is direct and mediates the attachment to nuclear ribonucleoprotein complexes (By similarity). Interacts with ADAR isoform 1; this interaction occurs in a RNA-independent manner (PubMed:28355180). Interacts (via DRBM domains) with AGO2 (via middle region); this interaction promotes active RISC assembly by promoting the association of siRNA with AGO2. Interacts (via NTD domain) with AKAP8L (via N-terminus). Interacts with BRCA1 (via C-terminus); this interaction is direct and links BRCA1 to the RNA polymerase II holoenzyme. Interacts (via N-terminus) with CREBBP; this interaction mediates association with RNA polymerase II holoenzyme and stimulates CREB-dependent transcriptional activation (By similarity). Interacts (via N-terminus) with EIF2AK2/PKR; this interaction is dependent upon the activation of the kinase (PubMed:19229320). Interacts (via DRBM domains) with DICER1. Interacts with H2AFX; this interaction is direct, requires phosphorylation of histone H2AFX on 'Ser-140' by PRKDC and promotes binding of DHX9 to transcriptionally stalled sites on chromosomal DNA in response to genotoxic stress. Interacts with HNRNPC; this interaction is direct, enhanced probably by their concomitant binding to RNA and mediates the attachment to actin filaments. Interacts (via NTD domain) with PRMT1. Interacts with IGF2BP1. Interacts with IGF2BP2, IGF2BP3. Interacts (via DRBM domains) with ILF3; this interaction occurs in a RNA-independent manner. Interacts with Importin alpha/Importin beta receptor. Interacts with LARP6 (via C-terminus); this interaction occurs in a mRNA-independent manner. Interacts (via N- and C-terminus) with LIN28A (via C-terminus); this interaction occurs in a RNA-independent manner. Interacts with LMX1B. Interacts (via helicase C-terminal domain, HA2 and OB-fold regions) with MAVS (via CARD domain); this interaction occurs in both resting and double-stranded RNA poly(I:C)-induced cells. Interacts with MBD2; this interaction stimulates transcriptional activation in a CREB-dependent manner. Interacts (via H2A and OB-fold regions) with MYD88 (via TIR domain); this interaction is direct. Interacts with NLRP9 upon rotavirus infection; this interaction may trigger NLRP9 inflammasome activation and inflammatory response. Interacts (via DRBM, OB-fold and RGG regions) with NUP98 (via N-terminus); this interaction occurs in a RNA-dependent manner and stimulates DHX9-mediated ATPase activity and regulates transcription and splicing of a subset of genes. Interacts (via N-terminus) with NXF1 (via N-terminus); this interaction is direct and negatively regulates NXF1-mediated nuclear export of constitutive transport element (CTE)-containing cellular mRNAs. Interacts with RELA; this interaction is direct and activates NF-kappa-B-mediated transcription. Interacts (via MTAD region) with RNA polymerase II holoenzyme; this interaction stimulates transcription activation in a CREB-dependent manner. Interacts (via RGG region) with SMN1; this interaction links SMN1 to the RNA polymerase II holoenzyme (By similarity). Interacts with SP7 (PubMed:17303075). Interacts (via DRBM domains) with TARBP2 (via DRBM first and second domains); this interaction occurs in a small interfering (siRNA)-dependent manner. Interacts with TOP2A; this interaction occurs in a E2 enzyme UBE2I- and RNA-dependent manner, negatively regulates DHX9-mediated double-stranded DNA and RNA duplex helicase activity and stimulates TOP2A-mediated supercoiled DNA relaxation activity. Interacts (via DRBM domains and C-terminus) with WRN (via 3'-5' exonuclease domain); this interaction inhibits the DNA-dependent NTPase and DNA helicase activities of DHX9 and stimulates the 3'-5' exonuclease activity of WRN. Interacts with XRCC5; this interaction occurs in a RNA-dependent manner (By similarity). Interacts with ZIC2 (via C2H2-type domain 3) (PubMed:17251188). {ECO:0000250|UniProtKB:Q08211, ECO:0000269|PubMed:17251188, ECO:0000269|PubMed:17303075, ECO:0000269|PubMed:19229320, ECO:0000269|PubMed:22767893, ECO:0000269|PubMed:28355180}. DOMAIN: DRBM domains cooperate for the binding to nucleic acid but not for unwinding helicase activity. The helicase-associated domain-2 (HA2) region is essential for the duplex RNA unwinding helicase activity. The minimal transactivation region (MTAD) mediates interaction with the RNA polymerase II holoenzyme and stimulates transcriptional activation in a CREB-dependent manner. The oligonucleotide- or oligosaccharide-binding (OB-fold) and the repeated arginine and glycine-glycine (RGG) regions are dispensable for both RNA-binding and unwinding helicase activities. The RGG region contains both nuclear localization signal (NLS) and nuclear export signal (NES) and is necessary and sufficient for nucleocytoplasmic shuttling in a RNA-independent manner. {ECO:0000250|UniProtKB:Q08211}. +Q8CFP6 DJC27_MOUSE DnaJ homolog subfamily C member 27 (Rab and DnaJ domain-containing protein) 273 30,831 Chain (1); Domain (1); Mutagenesis (3); Nucleotide binding (3); Region (1); Sequence conflict (6) FUNCTION: GTPase which can activate the MEK/ERK pathway and induce cell transformation when overexpressed. May act as a nuclear scaffold for MAPK1, probably by association with MAPK1 nuclear export signal leading to enhanced ERK1/ERK2 signaling. {ECO:0000269|PubMed:24746703}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24746703}. SUBUNIT: Interacts directly with MAPK1 (wild-type and kinase-deficient forms). Interacts directly (in GTP-bound form) with MAP2K1 (wild-type and kinase-deficient forms). {ECO:0000269|PubMed:24746703}. +Q09163 DLK1_MOUSE Protein delta homolog 1 (DLK-1) (Adipocyte differentiation inhibitor protein) (Preadipocyte factor 1) (Pref-1) [Cleaved into: Fetal antigen 1 (FA1)] 385 41,320 Alternative sequence (5); Chain (2); Disulfide bond (18); Domain (6); Glycosylation (10); Natural variant (1); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 306 329 Helical. {ECO:0000255}. TOPO_DOM 24 305 Extracellular. {ECO:0000255}.; TOPO_DOM 330 385 Cytoplasmic. {ECO:0000255}. FUNCTION: May have a role in neuroendocrine differentiation. Inhibits adipocyte differentiation. {ECO:0000269|PubMed:8095043, ECO:0000269|PubMed:8500166}. PTM: N- and O-glycosylated. {ECO:0000269|PubMed:9118998}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. Cytoplasm {ECO:0000250|UniProtKB:O70534}. SUBUNIT: Monomer. Interacts with SH3RF2 (By similarity). {ECO:0000250|UniProtKB:O70534}. TISSUE SPECIFICITY: Highly expressed in fetal liver, placenta, adult adrenal gland, brain, testis and ovary and, to a lesser degree, in adult kidney, muscle, thymus and heart. {ECO:0000269|PubMed:17320102}. +Q80TN4 DJC16_MOUSE DnaJ homolog subfamily C member 16 772 89,136 Beta strand (1); Chain (1); Domain (2); Erroneous initiation (2); Glycosylation (1); Helix (4); Natural variant (1); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 534 554 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 26 533 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 555 772 Extracellular. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}. +Q91WT4 DJC17_MOUSE DnaJ homolog subfamily C member 17 303 34,465 Chain (1); Compositional bias (1); Domain (2); Modified residue (2); Sequence conflict (5) FUNCTION: May negatively affect PAX8-induced thyroglobulin/TG transcription. {ECO:0000269|PubMed:20160132}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:D3ZSC8}. Nucleus {ECO:0000250|UniProtKB:D3ZSC8}. Note=Predominantly nuclear. {ECO:0000250|UniProtKB:D3ZSC8}. TISSUE SPECIFICITY: Expressed in the thyroid gland. {ECO:0000269|PubMed:20160132}. +Q9JI71 DLL4_MOUSE Delta-like protein 4 (Drosophila Delta homolog 4) (Delta4) 686 74,991 Chain (1); Disulfide bond (29); Domain (9); Glycosylation (5); Region (2); Sequence conflict (6); Signal peptide (1); Site (2); Topological domain (2); Transmembrane (1) TRANSMEM 533 553 Helical. {ECO:0000255}. TOPO_DOM 27 532 Extracellular. {ECO:0000255}.; TOPO_DOM 554 686 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in the Notch signaling pathway as Notch ligand (PubMed:11134954). Activates NOTCH1 and NOTCH4. Involved in angiogenesis; negatively regulates endothelial cell proliferation and migration and angiogenic sprouting (By similarity). Essential for retinal progenitor proliferation. Required for suppressing rod fates in late retinal progenitors as well as for proper generation of other retinal cell types (PubMed:22323600). During spinal cord neurogenesis, inhibits V2a interneuron fate (By similarity). {ECO:0000250|UniProtKB:Q9NR61, ECO:0000269|PubMed:11134954, ECO:0000269|PubMed:22323600}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Interacts with NOTCH4. Interacts (via N-terminal DSL and MNNL domains) with NOTCH1 (via EGF-like domains). {ECO:0000250|UniProtKB:D3ZHH1}. TISSUE SPECIFICITY: Expressed in vascular endothelium. Expressed in retina at least during embryogenesis. {ECO:0000269|PubMed:22323600}. +Q64205 DLX3_MOUSE Homeobox protein DLX-3 287 31,791 Chain (1); DNA binding (1); Region (1) FUNCTION: Likely to play a regulatory role in the development of the ventral forebrain. May play a role in craniofacial patterning and morphogenesis. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. SUBUNIT: Heterodimer with MEIS1. {ECO:0000250|UniProtKB:O60479}. TISSUE SPECIFICITY: Not expressed in the central nervous system. Expressed in a highly restricted region of the branchial arches. In later development, expressed in the developing middle and inner ear, teeth and whisker follicles. +Q91XM9 DLG2_MOUSE Disks large homolog 2 (Channel-associated protein of synapse-110) (Chapsyn-110) (Postsynaptic density protein PSD-93) 852 94,880 Alternative sequence (11); Beta strand (5); Chain (1); Domain (5); Helix (2); Lipidation (2); Modified residue (15); Sequence conflict (7); Turn (1) FUNCTION: Required for perception of chronic pain through NMDA receptor signaling. Regulates surface expression of NMDA receptors in dorsal horn neurons of the spinal cord. Interacts with the cytoplasmic tail of NMDA receptor subunits as well as inward rectifying potassium channels. Involved in regulation of synaptic stability at cholinergic synapses. Part of the postsynaptic protein scaffold of excitatory synapses. {ECO:0000269|PubMed:12890763}. PTM: Palmitoylation of isoform 1 and isoform 2 is not required for targeting to postsynaptic density. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:11997254}; Lipid-anchor {ECO:0000250|UniProtKB:Q63622}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250|UniProtKB:Q63622}. Cell junction, synapse {ECO:0000250}. Membrane {ECO:0000250|UniProtKB:Q63622}. Cell projection, axon {ECO:0000250|UniProtKB:Q63622}. Note=Concentrated in soma and postsynaptic density of a subset of neurons. {ECO:0000250|UniProtKB:Q63622}. SUBUNIT: Interacts with NOS1/nNOS through second PDZ domain. Interacts with KCNJ2/Kir2.1 (via C-terminus) through one of its PDZ domains (By similarity). Interacts with KCNJ4 (PubMed:11997254). Interacts with FRMPD4 (via C-terminus) (By similarity). Interacts through its PDZ domains with NETO1 (PubMed:19243221). Interacts with LRFN1, LRFN2 and LRFN4. Interacts with FASLG (By similarity). Interacts with KCNJ4 (By similarity). Interacts with ADAM22 (PubMed:20089912). {ECO:0000250|UniProtKB:Q15700, ECO:0000250|UniProtKB:Q63622, ECO:0000269|PubMed:11997254, ECO:0000269|PubMed:19243221, ECO:0000269|PubMed:20089912}. DOMAIN: Isoform 7 has an L27 domain close to N-terminus. TISSUE SPECIFICITY: Brain. Highest levels of isoform 1 in cortex, olfactory bulb, thalamus, hypothalamus, striatum and hippocampus. Highest level of isoform 2 in olfactory bulb. Reduced levels in cortex and hippocampus. Highest level of isoform 4 in spinal cord. Low levels of isoform 4, isoform 6, and isoform 7 in superior cervical ganglion. {ECO:0000269|PubMed:12890763, ECO:0000269|PubMed:15304517}. +P62627 DLRB1_MOUSE Dynein light chain roadblock-type 1 (Dynein light chain 2A, cytoplasmic) 96 10,990 Beta strand (5); Chain (1); Helix (2); Initiator methionine (1); Modified residue (1); Sequence conflict (1); Turn (1) FUNCTION: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SUBUNIT: Homodimer. The cytoplasmic dynein 1 complex consists of two catalytic heavy chains (HCs) and a number of non-catalytic subunits presented by intermediate chains (ICs), light intermediate chains (LICs) and light chains (LCs); the composition seems to vary in respect to the IC, LIC and LC composition. The heavy chain homodimer serves as a scaffold for the probable homodimeric assembly of the respective non-catalytic subunits. The ICs and LICs bind directly to the HC dimer and the LCs assemble on the IC dimer. Interacts with DYNC1I1 and DYNC1I2. Self-associates. Interacts with DYNLRB2. Interacts with RAB6A; the interaction is direct. Interacts with RAB6B (GDP-bound) (By similarity). {ECO:0000250}. +Q61712 DNJC1_MOUSE DnaJ homolog subfamily C member 1 (DnaJ protein homolog MTJ1) 552 63,870 Chain (1); Domain (3); Modified residue (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 150 170 Helical. {ECO:0000255}. TOPO_DOM 44 149 Lumenal. {ECO:0000250}.; TOPO_DOM 171 552 Cytoplasmic. {ECO:0000250}. FUNCTION: May modulate protein synthesis. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein. Nucleus membrane; Single-pass type I membrane protein. Microsome membrane; Single-pass type I membrane protein. SUBUNIT: Interacts (via J domain) with HSPA5. Interacts (via cytosolic domain) with ribosomes. Interacts (via SANT 2 domain) with SERPINA3; the interaction delays the formation of the covalent inhibitory complex SERPINA3-chymotrypsin, but does not alter the catalytic activity of SERPINA3. Interacts (via SANT 2 domain) with ITIH4 (via C-terminus); the interaction protects ITIH4 against in vitro cleavage by kallikrein (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. +Q9Z1N5 DX39B_MOUSE Spliceosome RNA helicase Ddx39b (EC 3.6.4.13) (56 kDa U2AF65-associated protein) (DEAD box protein UAP56) (HLA-B-associated transcript 1 protein) 428 49,035 Chain (1); Cross-link (1); Domain (2); Initiator methionine (1); Modified residue (5); Motif (2); Nucleotide binding (1) FUNCTION: Involved in nuclear export of spliced and unspliced mRNA. Assembling component of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NFX1 pathway. May undergo several rounds of ATP hydrolysis during assembly of TREX to drive subsequent loading of components such as ALYREF/THOC and CHTOP onto mRNA. Also associates with pre-mRNA independent of ALYREF/THOC4 and the THO complex. Involved in the nuclear export of intronless mRNA; the ATP-bound form is proposed to recruit export adapter ALYREF/THOC4 to intronless mRNA; its ATPase activity is cooperatively stimulated by RNA and ALYREF/THOC4 and ATP hydrolysis is thought to trigger the dissociation from RNA to allow the association of ALYREF/THOC4 and the NXF1-NXT1 heterodimer. Involved in transcription elongation and genome stability (By similarity). {ECO:0000250}.; FUNCTION: Splice factor that is required for the first ATP-dependent step in spliceosome assembly and for the interaction of U2 snRNP with the branchpoint. Has both RNA-stimulated ATP binding/hydrolysis activity and ATP-dependent RNA unwinding activity. Even with the stimulation of RNA, the ATPase activity is weak. Can only hydrolyze ATP but not other NTPs. The RNA stimulation of ATPase activity does not have a strong preference for the sequence and length of the RNA. However, ssRNA stimulates the ATPase activity much more strongly than dsRNA. Can unwind 5' or 3' overhangs or blunt end RNA duplexes in vitro. The ATPase and helicase activities are not influenced by U2AF2; the effect of ALYREF/THOC4 is reported conflictingly (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus speckle {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Can translocate to the cytoplasm in the presence of MX1. {ECO:0000250}. SUBUNIT: Homodimer, and heterodimer with DDX39A. Component of the transcription/export (TREX) complex at least composed of ALYREF/THOC4, DDX39B, SARNP/CIP29, CHTOP and the THO subcomplex; TREX seems to have dynamic structure involving ATP-dependent remodeling; in the complex bridges ALYREF/THOC4 and the THO complex, and, in a ATP-dependent manner, ALYREF/THOC4 and SARNP/CIP29. Component of the spliceosome. Interacts directly with U2AF2. Interacts with RBM8A, RNPS1 and SRRM1, FYTTD1/UIF, THOC1, MX1 and POLDIP3. Interacts with LUZP4 (By similarity). {ECO:0000250|UniProtKB:Q13838}. DOMAIN: The helicase C-terminal domain mediates interaction with ALYREF/THOC4. {ECO:0000250}. +Q6ZQ18 EFR3B_MOUSE Protein EFR3 homolog B 817 92,406 Alternative sequence (1); Chain (1); Modified residue (3) FUNCTION: Component of a complex required to localize phosphatidylinositol 4-kinase (PI4K) to the plasma membrane. The complex acts as a regulator of phosphatidylinositol 4-phosphate (PtdIns(4)P) synthesis. In the complex, EFR3B probably acts as the membrane-anchoring component. Also involved in responsiveness to G-protein-coupled receptors; it is however unclear whether this role is direct or indirect. {ECO:0000250|UniProtKB:Q9Y2G0}. PTM: Palmitoylated at its N-terminus, anchoring the protein to the plasma membrane. {ECO:0000250|UniProtKB:Q9Y2G0}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9Y2G0}; Lipid-anchor {ECO:0000250|UniProtKB:Q9Y2G0}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9Y2G0}. Note=Palmitoylation anchors the protein to the plasma membrane. A small amount is observed in the cytosol. {ECO:0000250|UniProtKB:Q9Y2G0}. SUBUNIT: Component of a phosphatidylinositol 4-kinase (PI4K) complex, composed of PI4KA, EFR3 (EFR3A or EFR3B), TTC7 (TTC7A or TTC7B) and FAM126 (FAM126A or FAM126B). {ECO:0000250|UniProtKB:Q9Y2G0}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:25380825}. +P50396 GDIA_MOUSE Rab GDP dissociation inhibitor alpha (Rab GDI alpha) (Guanosine diphosphate dissociation inhibitor 1) (GDI-1) 447 50,522 Chain (1); Modified residue (1); Sequence conflict (7) FUNCTION: Regulates the GDP/GTP exchange reaction of most Rab proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them. Promotes the dissociation of GDP-bound Rab proteins from the membrane and inhibits their activation. Promotes the dissociation of RAB1A, RAB3A, RAB5A and RAB10 from membranes. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus, trans-Golgi network {ECO:0000250}. SUBUNIT: Interacts with RHOH, RAB1A, RAB3A and RAB5A (By similarity). Interacts with RAB10. {ECO:0000250, ECO:0000269|PubMed:19570034}. TISSUE SPECIFICITY: High expression in brain, lower in other tissues. +Q8R1B4 EIF3C_MOUSE Eukaryotic translation initiation factor 3 subunit C (eIF3c) (Eukaryotic translation initiation factor 3 subunit 8) (eIF3 p110) 911 105,531 Chain (1); Compositional bias (3); Domain (1); Modified residue (15); Sequence conflict (2) FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression. {ECO:0000255|HAMAP-Rule:MF_03002, ECO:0000269|PubMed:17581632}. PTM: Phosphorylated. Phosphorylation is enhanced upon serum stimulation. {ECO:0000255|HAMAP-Rule:MF_03002}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03002}. SUBUNIT: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B, EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and EIF3M. The eIF-3 complex appears to include 3 stable modules: module A is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D, EIF3E, EIF3K and EIF3L. EIF3C of module C binds EIF3B of module A and EIF3H of module B, thereby linking the three modules. EIF3J is a labile subunit that binds to the eIF-3 complex via EIF3B. The eIF-3 complex may interact with RPS6KB1 under conditions of nutrient depletion. Mitogenic stimulation may lead to binding and activation of a complex composed of MTOR and RPTOR, leading to phosphorylation and release of RPS6KB1 and binding of EIF4B to eIF-3. Interacts with ALKBH4, IFIT1 and IFIT2 (By similarity). {ECO:0000255|HAMAP-Rule:MF_03002}. +Q9Z1D1 EIF3G_MOUSE Eukaryotic translation initiation factor 3 subunit G (eIF3g) (Eukaryotic translation initiation factor 3 RNA-binding subunit) (eIF-3 RNA-binding subunit) (Eukaryotic translation initiation factor 3 subunit 4) (eIF-3-delta) (eIF3 p42) (eIF3 p44) 320 35,638 Chain (1); Domain (1); Modified residue (8); Sequence conflict (7) FUNCTION: RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression. This subunit can bind 18S rRNA. {ECO:0000255|HAMAP-Rule:MF_03006, ECO:0000269|PubMed:17581632}. PTM: Phosphorylated. Phosphorylation is enhanced upon serum stimulation. {ECO:0000255|HAMAP-Rule:MF_03006}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03006}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03006}. Cytoplasm, perinuclear region {ECO:0000255|HAMAP-Rule:MF_03006}. Note=Colocalizes with AIFM1 in the nucleus and perinuclear region. {ECO:0000255|HAMAP-Rule:MF_03006}. SUBUNIT: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B, EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and EIF3M. The eIF-3 complex appears to include 3 stable modules: module A is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D, EIF3E, EIF3K and EIF3L. EIF3C of module C binds EIF3B of module A and EIF3H of module B, thereby linking the three modules. EIF3J is a labile subunit that binds to the eIF-3 complex via EIF3B. The eIF-3 complex may interact with RPS6KB1 under conditions of nutrient depletion. Mitogenic stimulation may lead to binding and activation of a complex composed of MTOR and RPTOR, leading to phosphorylation and release of RPS6KB1 and binding of EIF4B to eIF-3. Interacts (via C-terminus) with AIFM1 (via N-terminus) (By similarity). Interacts with DHX33; the interaction is independent of RNA (PubMed:26100019). {ECO:0000255|HAMAP-Rule:MF_03006, ECO:0000269|PubMed:26100019}. +P01132 EGF_MOUSE Pro-epidermal growth factor (EGF) [Cleaved into: Epidermal growth factor] 1217 133,072 Beta strand (5); Chain (2); Disulfide bond (24); Domain (9); Frameshift (1); Glycosylation (4); Region (1); Repeat (8); Sequence conflict (19); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (2) TRANSMEM 1039 1058 Helical. {ECO:0000255}. TOPO_DOM 29 1038 Extracellular. {ECO:0000255}.; TOPO_DOM 1059 1217 Cytoplasmic. {ECO:0000255}. FUNCTION: EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture. Magnesiotropic hormone that stimulates magnesium reabsorption in the renal distal convoluted tubule via engagement of EGFR and activation of the magnesium channel TRPM6 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Interacts with EGFR and promotes EGFR dimerization. Interacts with RHBDF1; may retain EGF in the endoplasmic reticulum and regulates its degradation through the endoplasmic reticulum-associated degradation (ERAD). Interacts with RHBDF2. {ECO:0000269|PubMed:21439629}. +Q3V124 EID3_MOUSE EP300-interacting inhibitor of differentiation 3 (EID-3) (EID-1-like inhibitor of differentiation 3) (Non-structural maintenance of chromosomes element 4 homolog B) (NS4EB) (Non-SMC element 4 homolog B) 375 43,308 Chain (1); Coiled coil (1); Erroneous initiation (2); Sequence conflict (7) FUNCTION: Tissue-specific component of the SMC5-SMC6 complex, a complex involved in repair of DNA double-strand breaks by homologous recombination. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The complex is required for telomere maintenance via recombination and mediates sumoylation of shelterin complex (telosome) components (By similarity). {ECO:0000250}.; FUNCTION: Acts as a repressor of nuclear receptor-dependent transcription possibly by interfering with CREBBP-dependent coactivation. May function as a coinhibitor of other CREBBP/EP300-dependent transcription factors (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8N140}. Cytoplasm {ECO:0000250|UniProtKB:Q8N140}. Chromosome, telomere {ECO:0000250}. Note=May shuttle between nucleus and cytoplasm. {ECO:0000250|UniProtKB:Q8N140}. SUBUNIT: Component of the SMC5-SMC6 complex which consists at least of SMC5, SMC6, NSMCE2, NSMCE1, NSMCE4A or EID3 and NSMCE3; EID3 seems to be a testis-specific subunit. NSMCE1, NSMCE4A or EID3 and NSMCE3 probably form a subcomplex that bridges the head domains of the SMC5:SMC6 heterodimer. Homodimer, and heterodimer with EID2. Interacts with the C-terminal region of CREBBP (By similarity). {ECO:0000250}. +Q8JZQ9 EIF3B_MOUSE Eukaryotic translation initiation factor 3 subunit B (eIF3b) (Eukaryotic translation initiation factor 3 subunit 9) (eIF-3-eta) (eIF3 p116) 803 91,370 Chain (1); Domain (1); Modified residue (22); Region (2); Repeat (5) FUNCTION: RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression. {ECO:0000255|HAMAP-Rule:MF_03001, ECO:0000269|PubMed:12038979, ECO:0000269|PubMed:17581632}. PTM: Phosphorylated. Phosphorylation is enhanced upon serum stimulation. {ECO:0000255|HAMAP-Rule:MF_03001}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03001}. SUBUNIT: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B, EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and EIF3M. The eIF-3 complex appears to include 3 stable modules: module A is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D, EIF3E, EIF3K and EIF3L. EIF3C of module C binds EIF3B of module A and EIF3H of module B, thereby linking the three modules. EIF3J is a labile subunit that binds to the eIF-3 complex via EIF3B. The eIF-3 complex interacts with RPS6KB1 under conditions of nutrient depletion. Mitogenic stimulation leads to binding and activation of a complex composed of MTOR and RPTOR, leading to phosphorylation and release of RPS6KB1 and binding of EIF4B to eIF-3. Also interacts with UPF2 and HNRPD. Interacts with METTL3. {ECO:0000255|HAMAP-Rule:MF_03001, ECO:0000269|PubMed:16541103, ECO:0000269|PubMed:17581632}. DOMAIN: The RRM domain mediates interaction with EIF3J. {ECO:0000255|HAMAP-Rule:MF_03001}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:12038979}. +Q9DBZ5 EIF3K_MOUSE Eukaryotic translation initiation factor 3 subunit K (eIF3k) (Eukaryotic translation initiation factor 3 subunit 12) (eIF-3 p25) 218 25,087 Alternative sequence (1); Chain (1); Domain (1); Initiator methionine (1); Modified residue (3) FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression. {ECO:0000255|HAMAP-Rule:MF_03010, ECO:0000269|PubMed:17581632}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03010}. Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03010}. SUBUNIT: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B, EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and EIF3M. The eIF-3 complex appears to include 3 stable modules: module A is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D, EIF3E, EIF3K and EIF3L. EIF3C of module C binds EIF3B of module A and EIF3H of module B, thereby linking the three modules. EIF3J is a labile subunit that binds to the eIF-3 complex via EIF3B. The eIF-3 complex interacts with RPS6KB1 under conditions of nutrient depletion. Mitogenic stimulation leads to binding and activation of a complex composed of MTOR and RPTOR, leading to phosphorylation and release of RPS6KB1 and binding of EIF4B to eIF-3. Identified in a HCV IRES-mediated translation complex, at least composed of EIF3C, IGF2BP1, RPS3 and HCV RNA-replicon. Interacts with ALKBH4, IFIT1 and IFIT2. {ECO:0000255|HAMAP-Rule:MF_03002, ECO:0000269|PubMed:17581632}. +P41971 ELK3_MOUSE ETS domain-containing protein Elk-3 (ETS-related protein ERP) (ETS-related protein NET) 409 44,414 Chain (1); Compositional bias (1); Cross-link (2); DNA binding (1); Modified residue (2); Motif (1); Sequence conflict (11) FUNCTION: May be a negative regulator of transcription, but can activate transcription when coexpressed with Ras, Src or Mos. Forms a ternary complex with the serum response factor and the ETS and SRF motifs of the Fos serum response element. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with CTBP1. TISSUE SPECIFICITY: Heart, liver, lung, kidney and muscle. +Q9EQC4 ELOV4_MOUSE Elongation of very long chain fatty acids protein 4 (EC 2.3.1.199) (3-keto acyl-CoA synthase Elovl4) (ELOVL fatty acid elongase 4) (ELOVL FA elongase 4) (Very long chain 3-ketoacyl-CoA synthase 4) (Very long chain 3-oxoacyl-CoA synthase 4) 312 36,506 Chain (1); Glycosylation (2); Motif (1); Sequence conflict (1); Transmembrane (7) TRANSMEM 42 62 Helical. {ECO:0000255|HAMAP-Rule:MF_03204}.; TRANSMEM 78 98 Helical. {ECO:0000255|HAMAP-Rule:MF_03204}.; TRANSMEM 127 147 Helical. {ECO:0000255|HAMAP-Rule:MF_03204}.; TRANSMEM 165 185 Helical. {ECO:0000255|HAMAP-Rule:MF_03204}.; TRANSMEM 188 208 Helical. {ECO:0000255|HAMAP-Rule:MF_03204}.; TRANSMEM 217 237 Helical. {ECO:0000255|HAMAP-Rule:MF_03204}.; TRANSMEM 246 266 Helical. {ECO:0000255|HAMAP-Rule:MF_03204}. Lipid metabolism; fatty acid biosynthesis. FUNCTION: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme that specifically elongates C24:0 and C26:0 acyl-CoAs. May participate in the production of saturated and monounsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. May play a critical role in early brain and skin development. {ECO:0000255|HAMAP-Rule:MF_03204}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03204}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03204}. SUBUNIT: Oligomer. {ECO:0000255|HAMAP-Rule:MF_03204}. DOMAIN: The C-terminal di-lysine motif may confer endoplasmic reticulum localization. {ECO:0000255|HAMAP-Rule:MF_03204}. TISSUE SPECIFICITY: Expressed in the retina, exclusively in photoreceptor cells and in the brain, skin, testis and lens. {ECO:0000269|PubMed:15028285}. +Q9ER73 ELP4_MOUSE Elongator complex protein 4 (PAX6 neighbor gene protein) 422 46,325 Chain (1); Sequence conflict (3) FUNCTION: Acts as subunit of the RNA polymerase II elongator complex, which is a histone acetyltransferase component of the RNA polymerase II (Pol II) holoenzyme and is involved in transcriptional elongation. Elongator may play a role in chromatin remodeling and is involved in acetylation of histones H3 and probably H4 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Component of the RNA polymerase II elongator complex (Elongator), which consists of ELP1, STIP1/ELP2, ELP3, ELP4, ELP5 and ELP6. Elongator associates with the C-terminal domain (CTD) of Pol II largest subunit (By similarity). {ECO:0000250}. +P70290 EM55_MOUSE 55 kDa erythrocyte membrane protein (p55) (Membrane protein, palmitoylated 1) 466 52,227 Chain (1); Domain (3); Initiator methionine (1); Modified residue (8); Region (1) FUNCTION: Essential regulator of neutrophil polarity. Regulates neutrophil polarization by regulating AKT1 phosphorylation through a mechanism that is independent of PIK3CG activity. {ECO:0000269|PubMed:19897731}. PTM: Palmitoylated. {ECO:0000250|UniProtKB:Q00013}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q00013}; Lipid-anchor {ECO:0000250|UniProtKB:Q00013}. Cell projection, stereocilium {ECO:0000269|PubMed:16829577, ECO:0000269|PubMed:17584769}. Note=Colocalizes with WHRN at stereocilium tip during hair cell development (PubMed:16829577). Colocalizes with MPP5 in the retina, at the outer limiting membrane (OLM) (PubMed:17584769). Colocalizes with WHRN in the retina, at the outer limiting membrane (OLM), outer plexifirm layer (OPL), basal bodies, and at connecting cilium (CC) (PubMed:17584769). Colocalizes with NF2 in non-myelin-forming Schwann cells (By similarity). {ECO:0000250|UniProtKB:Q00013, ECO:0000269|PubMed:16829577, ECO:0000269|PubMed:17584769}. SUBUNIT: Heterodimer with MPP5. Interacts with DLG5 and NF2. Interacts (via guanylate kinase-like domain) with WHRN (via third PDZ domain). {ECO:0000269|PubMed:16829577, ECO:0000269|PubMed:17584769}. TISSUE SPECIFICITY: Abundantly expressed in the erythrocytes (at protein level). {ECO:0000269|PubMed:19897731}. +Q8VC03 EMAL3_MOUSE Echinoderm microtubule-associated protein-like 3 (EMAP-3) 897 95,695 Chain (1); Compositional bias (4); Modified residue (6); Repeat (13) FUNCTION: May modify the assembly dynamics of microtubules, such that microtubules are slightly longer, but more dynamic. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. +Q3UMY5 EMAL4_MOUSE Echinoderm microtubule-associated protein-like 4 (EMAP-4) 988 110,027 Alternative sequence (4); Chain (1); Modified residue (17); Repeat (13); Sequence conflict (6) FUNCTION: May modify the assembly dynamics of microtubules, such that microtubules are slightly longer, but more dynamic. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. +Q9D2Y9 ELOV7_MOUSE Elongation of very long chain fatty acids protein 7 (EC 2.3.1.199) (3-keto acyl-CoA synthase Elovl7) (ELOVL fatty acid elongase 7) (ELOVL FA elongase 7) (Very long chain 3-ketoacyl-CoA synthase 7) (Very long chain 3-oxoacyl-CoA synthase 7) 281 33,479 Chain (1); Motif (1); Sequence conflict (2); Transmembrane (7) TRANSMEM 28 48 Helical. {ECO:0000255|HAMAP-Rule:MF_03207}.; TRANSMEM 73 93 Helical. {ECO:0000255|HAMAP-Rule:MF_03207}.; TRANSMEM 116 136 Helical. {ECO:0000255|HAMAP-Rule:MF_03207}.; TRANSMEM 143 162 Helical. {ECO:0000255|HAMAP-Rule:MF_03207}.; TRANSMEM 172 194 Helical. {ECO:0000255|HAMAP-Rule:MF_03207}.; TRANSMEM 207 227 Helical. {ECO:0000255|HAMAP-Rule:MF_03207}.; TRANSMEM 237 257 Helical. {ECO:0000255|HAMAP-Rule:MF_03207}. Lipid metabolism; fatty acid biosynthesis. FUNCTION: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme with higher activity toward C18 acyl-CoAs, especially C18:3(n-3) acyl-CoAs and C18:3(n-6)-CoAs. Also active toward C20:4-, C18:0-, C18:1-, C18:2- and C16:0-CoAs, and weakly toward C20:0-CoA. Little or no activity toward C22:0-, C24:0-, or C26:0-CoAs. May participate in the production of saturated and polyunsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. {ECO:0000255|HAMAP-Rule:MF_03207}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03207}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03207}. DOMAIN: The C-terminal di-lysine motif may confer endoplasmic reticulum localization. {ECO:0000255|HAMAP-Rule:MF_03207}. +Q91WG4 ELP2_MOUSE Elongator complex protein 2 (ELP2) (STAT3-interacting protein 1) (StIP1) 831 93,093 Alternative sequence (1); Chain (1); Repeat (13); Sequence conflict (5) FUNCTION: Regulates the ligand-dependent activation of STAT3. {ECO:0000269|PubMed:10954736}.; FUNCTION: Acts as subunit of the RNA polymerase II elongator complex, which is a histone acetyltransferase component of the RNA polymerase II (Pol II) holoenzyme and is involved in transcriptional elongation. Elongator may play a role in chromatin remodeling and is involved in acetylation of histones H3 and probably H4 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}. SUBUNIT: Component of the RNA polymerase II elongator complex (Elongator), which consists of ELP1, STIP1/ELP2, ELP3, ELP4, ELP5 and ELP6. Elongator associates with the C-terminal domain (CTD) of Pol II largest subunit (By similarity). Interacts with STAT3 and JAKs. {ECO:0000250, ECO:0000269|PubMed:10954736}. +Q8K482 EMIL2_MOUSE EMILIN-2 (Basilin) (Elastin microfibril interface-located protein 2) (Elastin microfibril interfacer 2) 1074 117,310 Chain (1); Coiled coil (5); Compositional bias (2); Disulfide bond (3); Domain (3); Glycosylation (7); Modified residue (1); Signal peptide (1) FUNCTION: May be responsible for anchoring smooth muscle cells to elastic fibers, and may be involved not only in the formation of the elastic fiber, but also in the processes that regulate vessel assembly. Has cell adhesive capacity. Major component of the cochlear basilar membrane (BM) which may contribute to the developmental assembly or function of the BM. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. Note=Found mainly at the interface between amorphous elastin and microfibrils. SUBUNIT: Homotrimer associated through a moderately stable interaction of the C-terminal globular C1q domains, allowing the nucleation of the triple helix and then a further quaternary assembly to higher-order polymers via intermolecular disulfide bonds (By similarity). Interacts with EMILIN1. {ECO:0000250}. TISSUE SPECIFICITY: Highest levels are present in cochlea of P8 pups, followed by modest levels in adult heart and lung, and much lower levels in forebrain, brainstem, cerebellum and hypothalamus. Very low levels detected in muscle, liver, kidney and eye. +P59900 EMIL3_MOUSE EMILIN-3 (EMILIN-5) (Elastin microfibril interface located protein 5) (Elastin microfibril interfacer 5) (Elastin microfibril interface-located protein 3) (Elastin microfibril interfacer 3) 758 82,396 Chain (1); Coiled coil (5); Disulfide bond (3); Domain (1); Glycosylation (5); Signal peptide (1) SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:14706625}. Note=According to PubMed:14706625 it is cytoplasmic. +O88662 EMP2_MOUSE Epithelial membrane protein 2 (EMP-2) (Protein XMP) 172 19,747 Chain (1); Glycosylation (2); Transmembrane (4) TRANSMEM 1 21 Helical. {ECO:0000255}.; TRANSMEM 72 92 Helical. {ECO:0000255}.; TRANSMEM 100 120 Helical. {ECO:0000255}.; TRANSMEM 148 168 Helical. {ECO:0000255}. FUNCTION: Functions as a key regulator of cell membrane composition by regulating proteins surface expression. Also, plays a role in regulation of processes including cell migration, cell proliferation, cell contraction and cell adhesion. Negatively regulates caveolae formation by reducing CAV1 expression and CAV1 amount by increasing lysosomal degradation (PubMed:17609206, PubMed:14978215). Facilitates surface trafficking and the formation of lipid rafts bearing GPI-anchor proteins (PubMed:14978215). Regulates surface expression of MHC1 and ICAM1 proteins increasing susceptibility to T-cell mediated cytotoxicity (PubMed:12763482). Regulates the plasma membrane expression of the integrin heterodimers ITGA6-ITGB1, ITGA5-ITGB3 and ITGA5-ITGB1 resulting in modulation of cell-matrix adhesion (PubMed:12189152). Also regulates many processes through PTK2. Regulates blood vessel endothelial cell migration and angiogenesis by regulating VEGF protein expression through PTK2 activation (By similarity). Regulates cell migration and cell contraction through PTK2 and SRC activation (By similarity). Regulates focal adhesion density, F-actin conformation and cell adhesion capacity through interaction with PTK2 (By similarity). Positively regulates cell proliferation (By similarity). Plays a role during cell death and cell blebbing (By similarity). Promotes angiogenesis and vasculogenesis through induction of VEGFA via a HIF1A-dependent pathway (By similarity). Also plays a role in embryo implantation by regulating surface trafficking of integrin heterodimer ITGA5-ITGB3 (PubMed:16487956, PubMed:16216233). May play a role in glomerular filtration (By similarity). {ECO:0000250|UniProtKB:F1QIK8, ECO:0000250|UniProtKB:P54851, ECO:0000269|PubMed:12189152, ECO:0000269|PubMed:12763482, ECO:0000269|PubMed:14978215, ECO:0000269|PubMed:16216233, ECO:0000269|PubMed:16487956, ECO:0000269|PubMed:17609206}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:12189152, ECO:0000269|PubMed:14978215, ECO:0000269|PubMed:16487956, ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:12189152}. Apical cell membrane {ECO:0000269|PubMed:16216233}. Membrane raft {ECO:0000269|PubMed:12763482, ECO:0000269|PubMed:14978215}. Cytoplasm {ECO:0000269|PubMed:16216233}. Nucleus {ECO:0000250|UniProtKB:Q66HH2}. Note=Localizes in cytoplasm, foot processes and cell bodies of podocytes and nucleus of endothelial cells of kidney (By similarity). Localizes to the apical cell surface in the luminal epithelium and glandular epithelium (PubMed:16487956). Colocalized with ITGB1 and GPI-anchor proteins on plasma membrane (PubMed:12189152) (PubMed:14978215). {ECO:0000250|UniProtKB:Q66HH2, ECO:0000269|PubMed:12189152, ECO:0000269|PubMed:14978215, ECO:0000269|PubMed:16487956}. SUBUNIT: Interacts with PTK2; regulates PTK2 activation and localization (By similarity). Interacts with ITGB3; regulates the levels of the heterodimer ITGA5-ITGB3 integrin surface expression (By similarity). Interacts with P2RX7 (via C-terminus) (By similarity). Interacts with ITGB1; the interaction may be direct or indirect and ITGB1 has a heterodimer form (PubMed:12189152). {ECO:0000250|UniProtKB:P54851, ECO:0000269|PubMed:12189152}. TISSUE SPECIFICITY: Expressed in both the endometrial epithelial and stromal cells during the embryo implantation period (PubMed:16487956). Expressed in the corneal epithelium, the sclera, the nerve fiber layer of the inner retina and retinal ganglion cell layer, the nonpigmented epithelium of the ciliary body and the optic nerve (PubMed:12710941). {ECO:0000269|PubMed:12710941, ECO:0000269|PubMed:16487956}. +O35912 EMP3_MOUSE Epithelial membrane protein 3 (EMP-3) (Hematopoietic neural membrane protein 1) (HNMP-1) (Protein YMP) 163 18,253 Chain (1); Glycosylation (2); Sequence conflict (6); Transmembrane (4) TRANSMEM 4 24 Helical. {ECO:0000255}.; TRANSMEM 66 86 Helical. {ECO:0000255}.; TRANSMEM 100 120 Helical. {ECO:0000255}.; TRANSMEM 139 159 Helical. {ECO:0000255}. FUNCTION: Probably involved in cell proliferation and cell-cell interactions. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. +Q8BJW7 EME1_MOUSE Crossover junction endonuclease EME1 (EC 3.1.22.-) 570 63,481 Chain (1); Cross-link (3); Modified residue (6) FUNCTION: Interacts with MUS81 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of stalled or collapsed replication forks. {ECO:0000269|PubMed:14609959}. SUBCELLULAR LOCATION: Nucleus, nucleolus. Note=Recruited to regions of DNA damage in S-phase cells. {ECO:0000250}. SUBUNIT: May self-associate (By similarity). Interacts with MUS81. {ECO:0000250, ECO:0000269|PubMed:14609959}. TISSUE SPECIFICITY: Weakly expressed in brain, heart, kidney, liver, lung, muscle, skin, small intestine, spleen, stomach, testis and thymus (PubMed:14609959, PubMed:27010503). Expressed in bone marrow (PubMed:27010503). Also expressed in embryonic stem cells (ES cells) (PubMed:14609959). {ECO:0000269|PubMed:14609959, ECO:0000269|PubMed:27010503}. +Q9R062 GLYG_MOUSE Glycogenin-1 (GN-1) (GN1) (EC 2.4.1.186) 333 37,402 Binding site (1); Chain (1); Glycosylation (1); Initiator methionine (1); Metal binding (3); Modified residue (2); Mutagenesis (7); Region (6); Site (1) Glycan biosynthesis; glycogen biosynthesis. FUNCTION: Self-glucosylates, via an inter-subunit mechanism, to form an oligosaccharide primer that serves as substrate for glycogen synthase. {ECO:0000250|UniProtKB:P46976}. PTM: Self-glycosylated by the transfer of glucose residues from UDP-glucose to itself, forming an alpha-1,4-glycan of around 10 residues attached to Tyr-195. {ECO:0000250|UniProtKB:P13280}.; PTM: Phosphorylated. {ECO:0000250|UniProtKB:P13280}. SUBUNIT: Homodimer. Interacts (via C-terminus) with glycogen synthase GYS1 (By similarity). Interacts (via C-terminus) with GYS2; required for GYS2-mediated glycogen synthesis (PubMed:24982189). {ECO:0000250|UniProtKB:P13280, ECO:0000250|UniProtKB:P46976, ECO:0000269|PubMed:24982189}. TISSUE SPECIFICITY: Skeletal muscle, heart, to a lesser extent in kidney, lung and brain. {ECO:0000269|PubMed:10542328}. +Q9CZN7 GLYM_MOUSE Serine hydroxymethyltransferase, mitochondrial (SHMT) (EC 2.1.2.1) (Glycine hydroxymethyltransferase) (Serine methylase) 504 55,759 Alternative sequence (1); Chain (1); Modified residue (9); Sequence conflict (4); Transit peptide (1) One-carbon metabolism; tetrahydrofolate interconversion. FUNCTION: Catalyzes the cleavage of serine to glycine accompanied with the production of 5,10-methylenetetrahydrofolate, an essential intermediate for purine biosynthesis (By similarity). Serine provides the major source of folate one-carbon in cells by catalyzing the transfer of one carbon from serine to tetrahydrofolate (By similarity). Contributes to the de novo mitochondrial thymidylate biosynthesis pathway via its role in glycine and tetrahydrofolate metabolism: thymidylate biosynthesis is required to prevent uracil accumulation in mtDNA (By similarity). Also required for mitochondrial translation by producing 5,10-methylenetetrahydrofolate; 5,10-methylenetetrahydrofolate providing methyl donors to produce the taurinomethyluridine base at the wobble position of some mitochondrial tRNAs (PubMed:29452640). Associates with mitochondrial DNA (By similarity). In addition to its role in mitochondria, also plays a role in the deubiquitination of target proteins as component of the BRISC complex: required for IFNAR1 deubiquitination by the BRISC complex (By similarity). {ECO:0000250|UniProtKB:P34897, ECO:0000269|PubMed:29452640}. PTM: Succinylation at Lys-280 inhibits the hydroxymethyltransferase activity. Desuccinylation by SIRT5 restores the activity, leading to promote cell proliferation. {ECO:0000250|UniProtKB:P34897}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P34897}. Mitochondrion matrix, mitochondrion nucleoid {ECO:0000250|UniProtKB:P34897}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:P34897}. Cytoplasm {ECO:0000250|UniProtKB:P34897}. Nucleus {ECO:0000250|UniProtKB:P34897}. Note=Mainly localizes in the mitochondrion. Also found in the cytoplasm and nucleus as part of the BRISC complex. {ECO:0000250|UniProtKB:P34897}. SUBUNIT: Homotetramer; in the presence of bound pyridoxal 5'-phosphate. Homodimer; in the absence of bound pyridoxal 5'-phosphate. Pyridoxal 5'-phosphate binding mediates an important conformation change that is required for tetramerization. Interacts with ABRAXAS2; the interaction is direct. Identified in a complex with ABRAXAS2 and the other subunits of the BRISC complex, at least composed of the ABRAXAS2, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1. Identified in a complex with ABRAXAS2 and IFNAR1. Interacts with KIRREL3. {ECO:0000250|UniProtKB:P34897}. +Q8C196 CPSM_MOUSE Carbamoyl-phosphate synthase [ammonia], mitochondrial (EC 6.3.4.16) (Carbamoyl-phosphate synthetase I) (CPSase I) 1500 164,618 Binding site (6); Chain (1); Domain (4); Glycosylation (3); Modified residue (157); Region (1); Sequence conflict (1); Transit peptide (1) FUNCTION: Involved in the urea cycle of ureotelic animals where the enzyme plays an important role in removing excess ammonia from the cell. {ECO:0000269|PubMed:24703693}. PTM: Undergoes proteolytic cleavage in the C-terminal region corresponding to the loss of approximately 12 AA residues from the C-terminus. {ECO:0000250|UniProtKB:P31327}.; PTM: Acetylation of Lys-287, Lys-603, Lys-841 and Lys-1291 is observed in liver mitochondria from fasted mice but not from fed mice. {ECO:0000269|PubMed:19410549, ECO:0000269|PubMed:22076378}.; PTM: Succinylated at Lys-44, Lys-287 and Lys-1291. Desuccinylated at Lys-1291 by SIRT5, leading to activation. {ECO:0000269|PubMed:22076378}.; PTM: Glutarylated. Glutarylation levels increase during fasting. Deglutarylated by SIRT5 at Lys-55, Lys-219, Lys-412, Lys-889, Lys-892, Lys-915, Lys-1360 and Lys-1486, leading to activation. {ECO:0000250|UniProtKB:P31327, ECO:0000269|PubMed:24703693}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P31327}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P31327}. SUBUNIT: Can form homooligomers (monomers as predominant form and dimers). {ECO:0000250|UniProtKB:P31327}. DOMAIN: The type-1 glutamine amidotransferase domain is defective. {ECO:0000250}. +Q9D7J7 CPNS2_MOUSE Calpain small subunit 2 (CSS2) (Calcium-dependent protease small subunit 2) 247 27,190 Calcium binding (3); Chain (1); Compositional bias (2); Domain (4); Metal binding (12) FUNCTION: Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. This small subunit may act as a tissue-specific chaperone of the large subunit, possibly by helping it fold into its correct conformation for activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Translocates to the plasma membrane upon calcium binding. {ECO:0000250}. SUBUNIT: Heterodimer of a large (catalytic) and a small (regulatory) subunit. {ECO:0000250}. +Q9QXK7 CPSF3_MOUSE Cleavage and polyadenylation specificity factor subunit 3 (EC 3.1.27.-) (Cleavage and polyadenylation specificity factor 73 kDa subunit) (CPSF 73 kDa subunit) (mRNA 3'-end-processing endonuclease CPSF-73) 684 77,505 Active site (1); Chain (1); Cross-link (3); Initiator methionine (1); Metal binding (8); Modified residue (3); Sequence conflict (3) FUNCTION: Component of the cleavage and polyadenylation specificity factor (CPSF) complex that play a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. Has endonuclease activity, and functions as mRNA 3'-end-processing endonuclease. Also involved in the histone 3'-end pre-mRNA processing. U7 snRNP-dependent protein that induces both the 3' endoribonucleolytic cleavage of histone pre-mRNAs and acts as a 5' to 3' exonuclease for degrading the subsequent downstream cleavage product (DCP) of mature histone mRNAs. Cleavage occurs after the 5'-ACCCA-3' sequence in the histone pre-mRNA leaving a 3'hydroxyl group on the upstream fragment containing the stem loop (SL) and 5' phosphate on the downstream cleavage product (DCP) starting with CU nucleotides. The U7-dependent 5' to 3' exonuclease activity is processive and degrades the DCP RNA substrate even after complete removal of the U7-binding site. Binds to the downstream cleavage product (DCP) of histone pre-mRNAs and the cleaved DCP RNA substrate in a U7 snRNP dependent manner. {ECO:0000269|PubMed:16213211, ECO:0000269|PubMed:18955505, ECO:0000269|PubMed:19470752}. PTM: Sumoylated on Lys-462, Lys-465 and Lys-545, preferentially by SUMO3. {ECO:0000250|UniProtKB:Q9UKF6}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UKF6}. SUBUNIT: Component of the cleavage and polyadenylation specificity factor (CPSF) complex, composed of CPSF1, CPSF2, CPSF3, CPSF4 and FIP1L1. Interacts with CPSF2, CSTF2 and SYMPK. Interacts with TUT1; the interaction is direct and mediates the recruitment of the CPSF complex on the 3'UTR of pre-mRNAs. Interacts with WDR33 (By similarity). Interacts with ZC3H3 (PubMed:16115198). {ECO:0000250|UniProtKB:Q9UKF6, ECO:0000269|PubMed:16115198}. +Q91WE4 CR032_MOUSE UPF0729 protein C18orf32 homolog 72 8,036 Chain (1) FUNCTION: May activate the NF-kappa-B signaling pathway. {ECO:0000250}. +P62696 CRBB2_MOUSE Beta-crystallin B2 (Beta-B2 crystallin) (Beta-crystallin Bp) 205 23,381 Beta strand (7); Chain (1); Domain (4); Helix (2); Initiator methionine (1); Modified residue (1); Region (3); Turn (1) FUNCTION: Crystallins are the dominant structural components of the vertebrate eye lens. SUBUNIT: Homo/heterodimer, or complexes of higher-order. The structure of beta-crystallin oligomers seems to be stabilized through interactions between the N-terminal arms (By similarity). {ECO:0000250}. DOMAIN: Has a two-domain beta-structure, folded into four very similar Greek key motifs. +P18340 CXCL9_MOUSE C-X-C motif chemokine 9 (Gamma-interferon-induced monokine) (Monokine induced by interferon-gamma) (MIG) (MuMIG) (Protein m119) (Small-inducible cytokine B9) 126 14,444 Chain (1); Disulfide bond (2); Glycosylation (1); Sequence conflict (3); Signal peptide (1) FUNCTION: May be a cytokine that affects the growth, movement, or activation state of cells that participate in immune and inflammatory response. SUBCELLULAR LOCATION: Secreted. +Q91YD1 CXD3_MOUSE Gap junction delta-3 protein (Connexin-30.2) (Cx30.2) (Gap junction alpha-11 protein) (Gap junction chi-1 protein) 278 30,220 Chain (1); Sequence conflict (2); Topological domain (5); Transmembrane (4) TRANSMEM 25 45 Helical. {ECO:0000255}.; TRANSMEM 77 97 Helical. {ECO:0000255}.; TRANSMEM 137 157 Helical. {ECO:0000255}.; TRANSMEM 189 209 Helical. {ECO:0000255}. TOPO_DOM 1 24 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 46 76 Extracellular. {ECO:0000255}.; TOPO_DOM 98 136 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 158 188 Extracellular. {ECO:0000255}.; TOPO_DOM 210 278 Cytoplasmic. {ECO:0000255}. FUNCTION: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell junction, gap junction {ECO:0000250}. SUBUNIT: A connexon is composed of a hexamer of connexins. {ECO:0000250}. +P28235 CXA4_MOUSE Gap junction alpha-4 protein (Connexin-37) (Cx37) 333 37,596 Chain (1); Natural variant (2); Topological domain (5); Transmembrane (4) TRANSMEM 21 40 Helical. {ECO:0000255}.; TRANSMEM 77 99 Helical. {ECO:0000255}.; TRANSMEM 149 171 Helical. {ECO:0000255}.; TRANSMEM 209 231 Helical. {ECO:0000255}. TOPO_DOM 1 20 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 41 76 Extracellular. {ECO:0000255}.; TOPO_DOM 100 148 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 172 208 Extracellular. {ECO:0000255}.; TOPO_DOM 232 333 Cytoplasmic. {ECO:0000255}. FUNCTION: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell junction, gap junction. SUBUNIT: A connexon is composed of a hexamer of connexins. TISSUE SPECIFICITY: Highly expressed in lung. +P35343 CXCR2_MOUSE C-X-C chemokine receptor type 2 (CXC-R2) (CXCR-2) (GRO/MGSA receptor) (High affinity interleukin-8 receptor B) (IL-8R B) (CD antigen CD182) 359 40,425 Chain (1); Disulfide bond (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 48 74 Helical; Name=1. {ECO:0000255}.; TRANSMEM 84 104 Helical; Name=2. {ECO:0000255}.; TRANSMEM 120 141 Helical; Name=3. {ECO:0000255}.; TRANSMEM 163 182 Helical; Name=4. {ECO:0000255}.; TRANSMEM 208 230 Helical; Name=5. {ECO:0000255}.; TRANSMEM 251 272 Helical; Name=6. {ECO:0000255}.; TRANSMEM 294 314 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 47 Extracellular. {ECO:0000255}.; TOPO_DOM 75 83 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 105 119 Extracellular. {ECO:0000255}.; TOPO_DOM 142 162 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 183 207 Extracellular. {ECO:0000255}.; TOPO_DOM 231 250 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 273 293 Extracellular. {ECO:0000255}.; TOPO_DOM 315 359 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for interleukin-8 which is a powerful neutrophil chemotactic factor. Binding of IL-8 to the receptor causes activation of neutrophils. This response is mediated via a G-protein that activates a phosphatidylinositol-calcium second messenger system. Binds to IL-8 with high affinity. Also binds with high affinity to CXCL3, GRO/MGSA and NAP-2. {ECO:0000269|PubMed:14764687}. PTM: Phosphorylated upon ligand binding; which is required for desensitization. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q9CX92 CXE1_MOUSE Gap junction epsilon-1 protein (Connexin-23) (Cx23) 205 23,831 Chain (1); Disulfide bond (2); Mutagenesis (1); Topological domain (5); Transmembrane (4) TRANSMEM 23 43 Helical. {ECO:0000255}.; TRANSMEM 75 95 Helical. {ECO:0000255}.; TRANSMEM 112 132 Helical. {ECO:0000255}.; TRANSMEM 171 191 Helical. {ECO:0000255}. TOPO_DOM 1 22 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 44 74 Extracellular. {ECO:0000255}.; TOPO_DOM 96 111 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 133 170 Extracellular. {ECO:0000255}.; TOPO_DOM 192 205 Cytoplasmic. {ECO:0000255}. FUNCTION: Mediates calcium-independent ATP release, suggesting activity as a hemichannel (PubMed:18849090). Does not form functional gap junctions (PubMed:18849090). May play a non-essential role in eye lens development (PubMed:18385072, PubMed:27038752). {ECO:0000269|PubMed:18385072, ECO:0000269|PubMed:27038752}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18849090}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: A connexon is composed of a hexamer of connexins. {ECO:0000250|UniProtKB:P08050}. TISSUE SPECIFICITY: Highly expressed in lens, where it is mainly found in lens fibers and to a lesser extent in lens epithelium (PubMed:18385072, PubMed:18849090). Weakly expressed in retina (PubMed:18849090). Not detected in other tissues tested (PubMed:18385072, PubMed:18849090). {ECO:0000269|PubMed:18385072, ECO:0000269|PubMed:18849090}. +P28236 CXA8_MOUSE Gap junction alpha-8 protein (Connexin-50) (Cx50) (Lens fiber protein MP70) 440 49,598 Chain (1); Topological domain (5); Transmembrane (4) TRANSMEM 24 46 Helical. {ECO:0000255}.; TRANSMEM 77 99 Helical. {ECO:0000255}.; TRANSMEM 158 180 Helical. {ECO:0000255}.; TRANSMEM 210 229 Helical. {ECO:0000255}. TOPO_DOM 1 23 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 47 76 Extracellular. {ECO:0000255}.; TOPO_DOM 100 157 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 181 209 Extracellular. {ECO:0000255}.; TOPO_DOM 230 440 Cytoplasmic. {ECO:0000255}. FUNCTION: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell junction, gap junction. SUBUNIT: A connexon is composed of a hexamer of connexins. This particular connexin only forms junctional channels. TISSUE SPECIFICITY: Eye lens. +P28229 CXG1_MOUSE Gap junction gamma-1 protein (Connexin-45) (Cx45) (Gap junction alpha-7 protein) 396 45,666 Chain (1); Topological domain (5); Transmembrane (4) TRANSMEM 23 45 Helical. {ECO:0000255}.; TRANSMEM 76 95 Helical. {ECO:0000255}.; TRANSMEM 176 198 Helical. {ECO:0000255}.; TRANSMEM 229 248 Helical. {ECO:0000255}. TOPO_DOM 1 22 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 46 75 Extracellular. {ECO:0000255}.; TOPO_DOM 96 175 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 199 228 Extracellular. {ECO:0000255}.; TOPO_DOM 249 396 Cytoplasmic. {ECO:0000255}. FUNCTION: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell junction, gap junction. SUBUNIT: A connexon is composed of a hexamer of connexins. Interacts with CNST. {ECO:0000269|PubMed:19864490}. +P17515 CXL10_MOUSE C-X-C motif chemokine 10 (10 kDa interferon gamma-induced protein) (Gamma-IP10) (IP-10) (C7) (Interferon-gamma induced protein CRG-2) (Small-inducible cytokine B10) 98 10,789 Beta strand (6); Chain (1); Disulfide bond (2); Helix (1); Modified residue (1); Signal peptide (1); Turn (1) FUNCTION: In addition to its role as a proinflammatory cytokine, may participate in T-cell effector function and perhaps T-cell development. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Expressed in the spleen, thymus, lymph nodes and liver. {ECO:0000269|PubMed:8145049}. +Q9JHH5 CXL11_MOUSE C-X-C motif chemokine 11 (Interferon-inducible T-cell alpha chemoattractant) (I-TAC) (Small-inducible cytokine B11) 100 11,266 Chain (1); Disulfide bond (2); Signal peptide (1) FUNCTION: Chemotactic for interleukin-activated T-cells but not unstimulated T-cells, neutrophils or monocytes. Induces calcium release in activated T-cells. Binds to CXCR3. May play an important role in CNS diseases which involve T-cell recruitment. May play a role in skin immune responses (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. +O55038 CXL13_MOUSE C-X-C motif chemokine 13 (B lymphocyte chemoattractant) (CXC chemokine BLC) (Small-inducible cytokine B13) 109 11,927 Beta strand (5); Chain (1); Disulfide bond (2); Helix (1); Signal peptide (1); Turn (1) FUNCTION: Strongly chemotactic for B-lymphocytes, weakly for spleen monocytes and macrophages but no chemotactic activity for granulocytes. Binds to BLR1/CXCR5. May play a role in directing the migration of B-lymphocytes to follicles in secondary lymphoid organs. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Found in spleen (B-cell-rich zone or follicles), Peyer patches (strongest within germinal centers and extending to the mantle zone) and lymph nodes (in reticular pattern in follicles). +P70658 CXCR4_MOUSE C-X-C chemokine receptor type 4 (CXC-R4) (CXCR-4) (Fusin) (Leukocyte-derived seven transmembrane domain receptor) (LESTR) (Pre-B-cell-derived chemokine receptor) (PB-CKR) (Stromal cell-derived factor 1 receptor) (SDF-1 receptor) (CD antigen CD184) 359 40,426 Alternative sequence (1); Binding site (2); Chain (1); Cross-link (1); Disulfide bond (2); Glycosylation (2); Modified residue (11); Motif (1); Region (7); Sequence conflict (2); Topological domain (8); Transmembrane (7) TRANSMEM 41 65 Helical; Name=1. {ECO:0000250|UniProtKB:P61073}.; TRANSMEM 80 101 Helical; Name=2. {ECO:0000250|UniProtKB:P61073}.; TRANSMEM 113 132 Helical; Name=3. {ECO:0000250|UniProtKB:P61073}.; TRANSMEM 157 176 Helical; Name=4. {ECO:0000250|UniProtKB:P61073}.; TRANSMEM 203 223 Helical; Name=5. {ECO:0000250|UniProtKB:P61073}.; TRANSMEM 249 268 Helical; Name=6. {ECO:0000250|UniProtKB:P61073}.; TRANSMEM 290 309 Helical; Name=7. {ECO:0000250|UniProtKB:P61073}. TOPO_DOM 1 40 Extracellular. {ECO:0000305}.; TOPO_DOM 66 79 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 102 112 Extracellular. {ECO:0000305}.; TOPO_DOM 133 156 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 177 202 Extracellular. {ECO:0000305}.; TOPO_DOM 224 248 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 269 289 Extracellular. {ECO:0000305}.; TOPO_DOM 310 359 Cytoplasmic. {ECO:0000305}. FUNCTION: Receptor for the C-X-C chemokine CXCL12/SDF-1 that transduces a signal by increasing intracellular calcium ion levels and enhancing MAPK1/MAPK3 activation (PubMed:8962122, PubMed:9295051, PubMed:9103415). Involved in the AKT signaling cascade (By similarity). Plays a role in regulation of cell migration, e.g. during wound healing. Acts as a receptor for extracellular ubiquitin; leading to enhanced intracellular calcium ions and reduced cellular cAMP levels. Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion by monocytes (By similarity). Involved in hematopoiesis and in cardiac ventricular septum formation (PubMed:9634237, PubMed:9634238, PubMed:9689100). Also plays an essential role in vascularization of the gastrointestinal tract, probably by regulating vascular branching and/or remodeling processes in endothelial cells (PubMed:9634237). Involved in cerebellar development. In the CNS, could mediate hippocampal-neuron survival (PubMed:9634238, PubMed:9689100). {ECO:0000250|UniProtKB:P61073, ECO:0000269|PubMed:8962122, ECO:0000269|PubMed:9103415, ECO:0000269|PubMed:9295051, ECO:0000269|PubMed:9634237, ECO:0000269|PubMed:9634238, ECO:0000269|PubMed:9689100}. PTM: Phosphorylated on agonist stimulation. Rapidly phosphorylated on serine and threonine residues in the C-terminal. Phosphorylation at Ser-331 and Ser-332 leads to recruitment of ITCH, ubiquitination and protein degradation. {ECO:0000250|UniProtKB:P61073}.; PTM: Ubiquitinated after ligand binding, leading to its degradation. Ubiquitinated by ITCH at the cell membrane on agonist stimulation. The ubiquitin-dependent mechanism, endosomal sorting complex required for transport (ESCRT), then targets CXCR4 for lysosomal degradation. This process is dependent also on prior Ser-/Thr-phosphorylation in the C-terminal of CXCR4. Also binding of ARRB1 to STAM negatively regulates CXCR4 sorting to lysosomes though modulating ubiquitination of SFR5S. {ECO:0000250|UniProtKB:P61073}.; PTM: Sulfation is required for efficient binding of CXCL12/SDF-1alpha and promotes its dimerization. {ECO:0000250|UniProtKB:P61073}.; PTM: O- and N-glycosylated. N-glycosylation can mask coreceptor function. The O-glycosylation chondroitin sulfate attachment does not affect interaction with CXCL12/SDF-1alpha nor its coreceptor activity. {ECO:0000250|UniProtKB:P61073}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8962122, ECO:0000269|PubMed:9295051}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P61073}. Cell junction {ECO:0000250}. Early endosome {ECO:0000250}. Late endosome {ECO:0000250}. Lysosome {ECO:0000250}. Note=In unstimulated cells, diffuse pattern on plasma membrane. On agonist stimulation, colocalizes with ITCH at the plasma membrane where it becomes ubiquitinated (By similarity). In the presence of antigen, distributes to the immunological synapse forming at the T-cell-APC contact area, where it localizes at the peripheral and distal supramolecular activation cluster (SMAC) (By similarity). {ECO:0000250}. SUBUNIT: Monomer. Can form homodimers. Interacts with CD164. Interacts with ARRB2; the interaction is dependent on the C-terminal phosphorylation of CXCR4 and allows activation of MAPK1 and MAPK3. Interacts with ARRC; the interaction is dependent on the C-terminal phosphorylation of CXCR4 and modulates calcium mobilization. Interacts with RNF113A; the interaction, enhanced by CXCL12, promotes CXCR4 ubiquitination and subsequent degradation. Interacts (via the cytoplasmic C-terminal) with ITCH (via the WW domains I and II); the interaction, enhanced by CXCL12, promotes CXCR4 ubiquitination and leads to its degradation. Interacts with extracellular ubiquitin. Interacts with DBN1; this interaction is enhanced by antigenic stimulation. Following LPS binding, may form a complex with GDF5, HSP90AA1 and HSPA8. {ECO:0000250|UniProtKB:P61073}. TISSUE SPECIFICITY: Lymphocytes, macrophages, neutrophils, microglial cells and astrocytes. Found in spleen, thymus, bone marrow, lymph nodes and, at lower levels in brain, small intestine, stomach and kidney. CXCR4-A is predominant in all tissues tested. During embryonic development, high levels are detected in the endothelium of developing blood vessels and in many regions of the developing brain including the olfactory epithelium, olfactory bulb, hippocampus, cerebellum and spinal cord. {ECO:0000269|PubMed:9634237, ECO:0000269|PubMed:9634238}. +Q9D0M3 CY1_MOUSE Cytochrome c1, heme protein, mitochondrial (Complex III subunit 4) (Complex III subunit IV) (Cytochrome b-c1 complex subunit 4) (Ubiquinol-cytochrome-c reductase complex cytochrome c1 subunit) (Cytochrome c-1) 325 35,328 Alternative sequence (1); Binding site (2); Chain (1); Domain (1); Erroneous initiation (1); Metal binding (2); Sequence conflict (2); Transit peptide (1); Transmembrane (1) TRANSMEM 292 306 Helical; Note=Anchors to the membrane. {ECO:0000255}. FUNCTION: This is the heme-containing component of the cytochrome b-c1 complex, which accepts electrons from Rieske protein and transfers electrons to cytochrome c in the mitochondrial respiratory chain. {ECO:0000250}. PTM: Binds 1 heme group per subunit. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein; Intermembrane side. SUBUNIT: The bc1 complex contains 11 subunits: 3 respiratory subunits (cytochrome b, cytochrome c1 and Rieske/UQCRFS1), 2 core proteins (UQCRC1/QCR1 and UQCRC2/QCR2) and 6 low-molecular weight proteins (UQCRH/QCR6, UQCRB/QCR7, UQCRQ/QCR8, UQCR10/QCR9, UQCR11/QCR10 and a cleavage product of Rieske/UQCRFS1). {ECO:0000250}. +Q04683 CXCR5_MOUSE C-X-C chemokine receptor type 5 (CXC-R5) (CXCR-5) (Burkitt lymphoma receptor 1 homolog) (CD antigen CD185) 374 42,115 Chain (1); Disulfide bond (1); Glycosylation (2); Sequence conflict (1); Topological domain (8); Transmembrane (7) TRANSMEM 58 78 Helical; Name=1. {ECO:0000255}.; TRANSMEM 91 111 Helical; Name=2. {ECO:0000255}.; TRANSMEM 127 147 Helical; Name=3. {ECO:0000255}.; TRANSMEM 170 190 Helical; Name=4. {ECO:0000255}.; TRANSMEM 222 242 Helical; Name=5. {ECO:0000255}.; TRANSMEM 262 282 Helical; Name=6. {ECO:0000255}.; TRANSMEM 307 327 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 57 Extracellular. {ECO:0000255}.; TOPO_DOM 79 90 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 112 126 Extracellular. {ECO:0000255}.; TOPO_DOM 148 169 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 191 221 Extracellular. {ECO:0000255}.; TOPO_DOM 243 261 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 283 306 Extracellular. {ECO:0000255}.; TOPO_DOM 328 374 Cytoplasmic. {ECO:0000255}. FUNCTION: Cytokine receptor that binds to B-lymphocyte chemoattractant (BLC). Involved in B-cell migration into B-cell follicles of spleen and Peyer patches but not into those of mesenteric or peripheral lymph nodes. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Mainly in spleen, in resting B-cells. +Q9CWW7 CXXC1_MOUSE CXXC-type zinc finger protein 1 (CpG-binding protein) (PHD finger and CXXC domain-containing protein 1) 660 76,167 Chain (1); Coiled coil (1); Compositional bias (3); Cross-link (1); Modified residue (6); Zinc finger (2) FUNCTION: Transcriptional activator that exhibits a unique DNA binding specificity for CpG unmethylated motifs with a preference for CpGG. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the SET1 complex, at least composed of the catalytic subunit (SETD1A or SETD1B), WDR5, WDR82, RBBP5, ASH2L/ASH2, CXXC1/CFP1, HCFC1 and DPY30. Interacts with SETD1A (By similarity). Interacts with ZNF335 (By similarity). {ECO:0000250}. +Q91WA4 CXXC5_MOUSE CXXC-type zinc finger protein 5 317 32,812 Chain (1); Compositional bias (1); Frameshift (2); Motif (1); Sequence conflict (2); Zinc finger (1) FUNCTION: May indirectly participate in activation of the NF-kappa-B and MAPK pathways. Acts as a mediator of BMP4-mediated modulation of canonical Wnt signaling activity in neural stem cells. Required for DNA damage-induced ATM phosphorylation, p53 activation and cell cycle arrest. Involved in myelopoiesis (By similarity). Binds to the oxygen responsive element of COX4I2 and represses its transcription under hypoxia conditions (4% oxygen), as well as normoxia conditions (20% oxygen). May repress COX4I2 transactivation induced by CHCHD2 and RBPJ (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q7LFL8}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Colocalizes with DVL1 in large bodies localized just outside the nuclear membrane. {ECO:0000250}. SUBUNIT: Interacts with DVL1. Interacts with RBPJ. {ECO:0000250|UniProtKB:Q5XIQ3, ECO:0000250|UniProtKB:Q7LFL8}. +Q61093 CY24B_MOUSE Cytochrome b-245 heavy chain (EC 1.-.-.-) (CGD91-phox) (Cytochrome b(558) subunit beta) (Cytochrome b558 subunit beta) (Heme-binding membrane glycoprotein gp91phox) (Neutrophil cytochrome b 91 kDa polypeptide) (gp91-1) (gp91-phox) (p22 phagocyte B-cytochrome) 570 65,305 Chain (1); Cross-link (11); Domain (2); Glycosylation (1); Metal binding (4); Nucleotide binding (1); Topological domain (7); Transmembrane (6) TRANSMEM 9 29 Helical. {ECO:0000255}.; TRANSMEM 49 69 Helical. {ECO:0000255}.; TRANSMEM 103 123 Helical. {ECO:0000255}.; TRANSMEM 170 190 Helical. {ECO:0000255}.; TRANSMEM 201 221 Helical. {ECO:0000255}.; TRANSMEM 262 282 Helical. {ECO:0000255}. TOPO_DOM 1 8 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 30 48 Extracellular. {ECO:0000255}.; TOPO_DOM 70 102 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 124 169 Extracellular. {ECO:0000255}.; TOPO_DOM 191 200 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 222 261 Extracellular. {ECO:0000255}.; TOPO_DOM 283 570 Cytoplasmic. {ECO:0000255}. FUNCTION: Critical component of the membrane-bound oxidase of phagocytes that generates superoxide. It is the terminal component of a respiratory chain that transfers single electrons from cytoplasmic NADPH across the plasma membrane to molecular oxygen on the exterior. Also functions as a voltage-gated proton channel that mediates the H(+) currents of resting phagocytes. {ECO:0000269|PubMed:24739962}. PTM: Glycosylated.; PTM: Phosphorylated on Ser and Thr residues. {ECO:0000250}.; PTM: Undergoes 'Lys-48'-linked polyubiquitination, likely by RNF145, triggering endoplasmic reticulum-associated degradation. {ECO:0000269|PubMed:26194095}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Note=As unassembled monomer may localize to the endoplasmic reticulum. {ECO:0000305|PubMed:28351984}. SUBUNIT: Composed of a heavy chain (beta) and a light chain (alpha). Component of an NADPH oxidase complex composed of a heterodimer formed by the membrane proteins CYBA and CYBB and the cytosolic subunits NCF1, NCF2 and NCF4. Interacts with NCF1. Interacts with calprotectin (S100A8/9) (By similarity). Interacts with NRROS; the interaction is direct and impairs formation of a stable NADPH oxidase complex (PubMed:24739962). Interacts with CYBC1; CYBC1 may act as a chaperone stabilizing Cytochrome b-245 heterodimer (By similarity). {ECO:0000250|UniProtKB:P04839, ECO:0000269|PubMed:24739962}. +Q6P1H1 CYAC3_MOUSE Cytochrome b ascorbate-dependent protein 3 (EC 1.-.-.-) (Cytochrome b561 family member A3) (Lysosomal cytochrome b) (LCytb) 242 27,086 Alternative sequence (2); Chain (1); Domain (1); Metal binding (6); Mutagenesis (12); Transmembrane (6) TRANSMEM 5 25 Helical; Name=1. {ECO:0000255}.; TRANSMEM 41 61 Helical; Name=2. {ECO:0000255}.; TRANSMEM 82 102 Helical; Name=3. {ECO:0000255}.; TRANSMEM 120 140 Helical; Name=4. {ECO:0000255}.; TRANSMEM 155 175 Helical; Name=5. {ECO:0000255}.; TRANSMEM 203 223 Helical; Name=6. {ECO:0000255}. FUNCTION: Ferric-chelate reductase that reduces Fe(3+) to Fe(2+) before its transport from the endosome to the cytoplasm. Probably uses ascorbate as electron donor. {ECO:0000269|PubMed:16911521}. PTM: N-glycosylated. {ECO:0000269|PubMed:16996694}. SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000269|PubMed:16996694}; Multi-pass membrane protein {ECO:0000269|PubMed:16996694}. Lysosome membrane {ECO:0000269|PubMed:16996694}; Multi-pass membrane protein {ECO:0000269|PubMed:16996694}. TISSUE SPECIFICITY: Present in lung, spleen, thymus and testis. Present at low level in brain, heart, liver and kidney. Expressed in the alveolar macrophages of the lung, in the white pulp of the spleen, widespread in the thymus, and in the Sertoli cells of the testis (at protein level). {ECO:0000269|PubMed:16996694}. +Q9D9T8 EFHC1_MOUSE EF-hand domain-containing protein 1 (Myoclonin-1) 648 75,142 Chain (1); Domain (4); Region (1) FUNCTION: Microtubule-associated protein which regulates cell division and neuronal migration during cortical development. Necessary for mitotic spindle organization. Necessary for radial and tangential cell migration during brain development, possibly acting as a regulator of cell morphology and process formation during migration (By similarity). May enhance calcium influx through CACNA1E and stimulate programmed cell death. Overexpression of EFHC1 in hippocampal primary culture neurons induced apoptosis. {ECO:0000250|UniProtKB:Q5JVL4, ECO:0000269|PubMed:15258581}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q5JVL4}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q5JVL4}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q5JVL4}. SUBUNIT: Interacts with the C-terminus of CACNA1E. InteractS with alpha-tubulin. {ECO:0000250|UniProtKB:Q5JVL4}. TISSUE SPECIFICITY: Expressed in adult brain including hippocampus, cerebellum, cerebral cortex, thalamus, hypothalamus, amygdala and upper brainstem. Expressed in soma and dentrites of pyramidal neurons of the hippocampal CA1 region, pyramidal neurons of the cerebral cortex and Purkinje cells of cerebellum. Highly expressed in testis, trachea, and oviduct, moderately in lung, and slightly in brain. Highly expressed in sperm flagella and tracheal cilia (at protein level). {ECO:0000269|PubMed:15258581, ECO:0000269|PubMed:15670853}. +Q9D485 EFHC2_MOUSE EF-hand domain-containing family member C2 750 87,646 Chain (1); Domain (4); Sequence conflict (3) +Q9D4J1 EFHD1_MOUSE EF-hand domain-containing protein D1 (EF-hand domain-containing protein 1) (Mitocalcin) (Swiprosin-2) 240 27,000 Calcium binding (2); Chain (1); Domain (2) FUNCTION: Acts as a calcium sensor for mitochondrial flash (mitoflash) activation, an event characterized by stochastic bursts of superoxide production (By similarity). May play a role in neuronal differentiation (PubMed:16336229). {ECO:0000250|UniProtKB:Q9BUP0, ECO:0000269|PubMed:16336229}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:16336229}. TISSUE SPECIFICITY: Widely expressed (PubMed:16336229). Highest expression in testis, followed by ovary, kidney, cerebrum, cerebellum, heart, liver, and spleen (PubMed:12270117). In the cerebrum and cerebellum, undetectable at embryonic stages, expression increases after birth up to adult stage (PubMed:12270117). In adult CNS, detected in neurons of the cerebellum, cerebrum and hippocampus formation, including dentate gyrus and Cornu Ammonis, but not in the white matter (PubMed:12270117). In the testis, expressed in spermatocytes, but not in spermatogonia nor in interstitial cells (PubMed:12270117). In ovary, found predominantly in mural granulosa cells and those of the cumulus oophorus (PubMed:12270117). In kidney, expressed in collecting ducts, but not in glomeruli (PubMed:12270117). Not detected in skeletal muscle (PubMed:12270117). {ECO:0000269|PubMed:12270117, ECO:0000269|PubMed:16336229}. +Q9D8Y0 EFHD2_MOUSE EF-hand domain-containing protein D2 (Swiprosin-1) 240 26,791 Calcium binding (2); Chain (1); Domain (2); Initiator methionine (1); Modified residue (6); Sequence conflict (2) FUNCTION: May regulate B-cell receptor (BCR)-induced immature and primary B-cell apoptosis. Plays a role as negative regulator of the canonical NF-kappa-B-activating branch. Controls spontaneous apoptosis through the regulation of BCL2L1 abundance. {ECO:0000269|PubMed:17673920}. SUBCELLULAR LOCATION: Membrane raft {ECO:0000269|PubMed:15749887}. Note=In immature B-cell line WEHI-231. SUBUNIT: Interacts with CASP9; with inactive form. {ECO:0000250}. TISSUE SPECIFICITY: Detected in thymus, kidney, spleen, lung, liver and brain. Highest abundance in brain and lowest in kidney and thymus. {ECO:0000269|PubMed:17673920}. +Q8C0D5 EFL1_MOUSE Elongation factor-like GTPase 1 (Elongation factor Tu GTP-binding domain-containing protein 1) (Elongation factor-like 1) (Protein FAM42A) 1127 125,777 Chain (1); Domain (1); Modified residue (1); Nucleotide binding (3); Sequence conflict (2) FUNCTION: Involved in the biogenesis of the 60S ribosomal subunit and translational activation of ribosomes. Together with SBDS, triggers the GTP-dependent release of EIF6 from 60S pre-ribosomes in the cytoplasm, thereby activating ribosomes for translation competence by allowing 80S ribosome assembly and facilitating EIF6 recycling to the nucleus, where it is required for 60S rRNA processing and nuclear export. Has low intrinsic GTPase activity. GTPase activity is increased by contact with 60S ribosome subunits (By similarity). {ECO:0000250}. SUBUNIT: Associates with the 60S ribosomal subunit. Found in a complex consisting of the 60S ribosomal subunit, SBDS and EFL1. {ECO:0000250|UniProtKB:Q7Z2Z2}. +Q9CY45 EFMT1_MOUSE EEF1A lysine methyltransferase 1 (EC 2.1.1.-) (N(6)-adenine-specific DNA methyltransferase 2) (Protein-lysine N-methyltransferase N6amt2) 214 24,499 Chain (1); Erroneous initiation (3); Initiator methionine (1); Modified residue (2) FUNCTION: Protein-lysine methyltransferase that selectively catalyzes the trimethylation of EEF1A at 'Lys-79'. {ECO:0000255|HAMAP-Rule:MF_03187}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03187}. +Q9D853 EFMT2_MOUSE EEF1A lysine methyltransferase 2 (EC 2.1.1.-) (Methyltransferase-like protein 10) (Protein-lysine N-methyltransferase Mettl10) 244 26,864 Chain (1); Modified residue (1); Sequence conflict (1) FUNCTION: Protein-lysine methyltransferase that selectively catalyzes the trimethylation of EEF1A at 'Lys-318'. {ECO:0000255|HAMAP-Rule:MF_03188}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03188}. Nucleus {ECO:0000250|UniProtKB:Q5JPI9, ECO:0000255|HAMAP-Rule:MF_03188}. +D3YWP0 EFMT3_MOUSE EEF1A lysine methyltransferase 3 (EC 2.1.1.-) (Methyltransferase-like protein 21B) (Protein-lysine methyltransferase METTL21B) 232 25,675 Binding site (4); Chain (1); Region (1) FUNCTION: Protein-lysine methyltransferase that selectively methylates EEF1A1 and EEF1A2 at 'Lys-165' in an aminoacyl-tRNA and GTP-dependent manner. EEF1A1 methylation by EEF1AKMT3 is dynamic as well as inducible by stress conditions, such as ER-stress, and plays a regulatory role on mRNA translation. {ECO:0000269|PubMed:28108655}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96AZ1}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q96AZ1}. SUBUNIT: Interacts with members of the heat shock protein 70 and 90 families and of the TCP-1 chaperonin family, as well as with HSPD1, STIP1 and tubulin; at least some of these proteins may be methylation substrates. {ECO:0000250|UniProtKB:Q96AZ1}. +P0DPE0 EFMT4_MOUSE EEF1A lysine methyltransferase 4 (EC 2.1.1.-) 255 28,531 Binding site (5); Chain (1); Frameshift (1); Modified residue (1); Motif (1); Region (2); Sequence conflict (1) FUNCTION: Protein-lysine methyltransferase that efficiently catalyzes three successive methylations on 'Lys-36' in eukaryotic translation elongation factor 1 alpha (EEF1A1 or EEF1A2). {ECO:0000250|UniProtKB:P0DPD7}. +P52793 EFNA1_MOUSE Ephrin-A1 (EPH-related receptor tyrosine kinase ligand 1) (LERK-1) (Immediate early response protein B61) [Cleaved into: Ephrin-A1, secreted form] 205 23,802 Chain (2); Disulfide bond (2); Domain (1); Glycosylation (1); Lipidation (1); Propeptide (1); Sequence conflict (13); Signal peptide (1) FUNCTION: Cell surface GPI-bound ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. Plays an important role in angiogenesis and tumor neovascularization. The recruitment of VAV2, VAV3 and PI3-kinase p85 subunit by phosphorylated EPHA2 is critical for EFNA1-induced RAC1 GTPase activation and vascular endothelial cell migration and assembly. Exerts anti-oncogenic effects in tumor cells through activation and down-regulation of EPHA2. Activates EPHA2 by inducing tyrosine phosphorylation which leads to its internalization and degradation. Acts as a negative regulator in the tumorigenesis of gliomas by down-regulating EPHA2 and FAK. Can evoke collapse of embryonic neuronal growth cone and regulates dendritic spine morphogenesis. {ECO:0000269|PubMed:16782872, ECO:0000269|PubMed:17143272, ECO:0000269|PubMed:18387945}. PTM: Undergoes proteolysis by a metalloprotease to give rise to a soluble monomeric form. {ECO:0000250}.; PTM: N-Glycosylation is required for binding to EPHA2 receptor and inducing its internalization. {ECO:0000250|UniProtKB:P20827}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P20827}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P20827}.; SUBCELLULAR LOCATION: Ephrin-A1, secreted form: Secreted {ECO:0000250|UniProtKB:P20827}. SUBUNIT: Monomer. Homodimer. Forms heterodimers with EPHA2. Binds to the receptor tyrosine kinases EPHA2, EPHA3, EPHA4, EPHA5, EPHA6 and EPHA7. Also binds with low affinity to EPHA1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in myogenic progenitor cells. {ECO:0000269|PubMed:27446912}. +P52801 EFNA2_MOUSE Ephrin-A2 (CEK7-ligand) (CEK7-L) (ELF-1) (EPH-related receptor tyrosine kinase ligand 6) (LERK-6) 209 23,586 Chain (1); Disulfide bond (2); Domain (1); Glycosylation (3); Lipidation (1); Propeptide (1); Signal peptide (1) FUNCTION: Cell surface GPI-bound ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. With the EPHA2 receptor may play a role in bone remodeling through regulation of osteoclastogenesis and osteoblastogenesis. {ECO:0000269|PubMed:19299512, ECO:0000269|PubMed:9053851}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}. SUBUNIT: Binds to the receptor tyrosine kinases EPHA3, EPHA4 and EPHA5. Interacts with EPHA8; activates EPHA8. {ECO:0000269|PubMed:9053851}. TISSUE SPECIFICITY: Expressed in myogenic progenitor cells. {ECO:0000269|PubMed:27446912}. +O08545 EFNA3_MOUSE Ephrin-A3 (EHK1 ligand) (EHK1-L) (EPH-related receptor tyrosine kinase ligand 3) (LERK-3) 230 25,632 Chain (1); Disulfide bond (2); Domain (1); Glycosylation (4); Lipidation (1); Propeptide (1); Sequence conflict (4); Signal peptide (1) FUNCTION: Cell surface GPI-bound ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. {ECO:0000269|PubMed:9053851}. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. SUBUNIT: Interacts with EPHA8; activates EPHA8. {ECO:0000269|PubMed:9053851}. TISSUE SPECIFICITY: Expressed in myogenic progenitor cells. {ECO:0000269|PubMed:27446912}. +O08542 EFNA4_MOUSE Ephrin-A4 (EPH-related receptor tyrosine kinase ligand 4) (LERK-4) 206 22,861 Chain (1); Disulfide bond (2); Domain (1); Glycosylation (2); Lipidation (1); Motif (1); Propeptide (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Cell surface GPI-bound ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. May play a role in the interaction between activated B-lymphocytes and dendritic cells in tonsils (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. TISSUE SPECIFICITY: Expressed in myogenic progenitor cells. {ECO:0000269|PubMed:27446912}. +O08543 EFNA5_MOUSE Ephrin-A5 (AL-1) (EPH-related receptor tyrosine kinase ligand 7) (LERK-7) 228 26,339 Alternative sequence (1); Beta strand (12); Chain (1); Disulfide bond (2); Domain (1); Glycosylation (2); Helix (2); Lipidation (1); Propeptide (1); Signal peptide (1); Turn (1) FUNCTION: Cell surface GPI-bound ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Induces compartmentalized signaling within a caveolae-like membrane microdomain when bound to the extracellular domain of its cognate receptor. This signaling event requires the activity of the Fyn tyrosine kinase. Activates the EPHA3 receptor to regulate cell-cell adhesion and cytoskeletal organization. With the receptor EPHA2 may regulate lens fiber cells shape and interactions and be important for lens transparency maintenance. May function actively to stimulate axon fasciculation. The interaction of EFNA5 with EPHA5 also mediates communication between pancreatic islet cells to regulate glucose-stimulated insulin secretion. Cognate/functional ligand for EPHA7, their interaction regulates brain development modulating cell-cell adhesion and repulsion. {ECO:0000269|PubMed:11089974, ECO:0000269|PubMed:17448994, ECO:0000269|PubMed:18948590, ECO:0000269|PubMed:9053851}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. Membrane, caveola {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. Note=Compartmentalized in discrete caveolae-like membrane microdomains. {ECO:0000250}. SUBUNIT: Binds to the receptor tyrosine kinases EPHA2, EPHA3 and EPHB1. Forms a ternary EFNA5-EPHA3-ADAM10 complex mediating EFNA5 extracellular domain shedding by ADAM10 which regulates the EFNA5-EPHA3 complex internalization and function (By similarity). Binds to EPHB2. Interacts with EPHA8; activates EPHA8. {ECO:0000250, ECO:0000269|PubMed:15107857, ECO:0000269|PubMed:9053851}. TISSUE SPECIFICITY: Expressed in myogenic progenitor cells. {ECO:0000269|PubMed:27446912}. +P35175 CYT1_MOUSE Stefin-1 97 11,007 Chain (1); Motif (1); Site (1) FUNCTION: This is an intracellular thiol proteinase inhibitor. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +Q99LC8 EI2BA_MOUSE Translation initiation factor eIF-2B subunit alpha (eIF-2B GDP-GTP exchange factor subunit alpha) 305 33,816 Chain (1); Modified residue (1) FUNCTION: Catalyzes the exchange of eukaryotic initiation factor 2-bound GDP for GTP. SUBUNIT: Complex of five different subunits; alpha, beta, gamma, delta and epsilon. +Q61749 EI2BD_MOUSE Translation initiation factor eIF-2B subunit delta (eIF-2B GDP-GTP exchange factor subunit delta) 524 57,624 Alternative sequence (1); Chain (1); Initiator methionine (1); Modified residue (3); Sequence conflict (2) FUNCTION: Catalyzes the exchange of eukaryotic initiation factor 2-bound GDP for GTP. SUBUNIT: Complex of five different subunits; alpha, beta, gamma, delta and epsilon. +Q8BWQ5 DCLK3_MOUSE Serine/threonine-protein kinase DCLK3 (EC 2.7.11.1) (CLICK-I and II-related) (CLr) (Doublecortin-like and CAM kinase-like 3) (Doublecortin-like kinase 3) 790 88,228 Active site (1); Binding site (1); Chain (1); Compositional bias (1); Domain (2); Erroneous initiation (1); Frameshift (1); Nucleotide binding (1) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16684769}. Nucleus {ECO:0000269|PubMed:16684769}. TISSUE SPECIFICITY: Highly expressed in brain and to a lower extent in liver and kidney. {ECO:0000269|PubMed:16684769}. +Q91X52 DCXR_MOUSE L-xylulose reductase (XR) (EC 1.1.1.10) (Dicarbonyl/L-xylulose reductase) 244 25,746 Active site (2); Binding site (1); Chain (1); Modified residue (2); Nucleotide binding (1); Sequence conflict (8) FUNCTION: Catalyzes the NADPH-dependent reduction of several pentoses, tetroses, trioses, alpha-dicarbonyl compounds and L-xylulose. Participates in the uronate cycle of glucose metabolism. May play a role in the water absorption and cellular osmoregulation in the proximal renal tubules by producing xylitol, an osmolyte, thereby preventing osmolytic stress from occurring in the renal tubules. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Apical cell membrane {ECO:0000269|PubMed:11882650}; Peripheral membrane protein {ECO:0000269|PubMed:11882650}. Note=Probably recruited to membranes via an interaction with phosphatidylinositol (By similarity). In kidney, it is localized in the brush border membranes of proximal tubular cells. {ECO:0000250}. SUBUNIT: Homotetramer. TISSUE SPECIFICITY: Highly expressed in kidney, liver and epididymis. Expressed at intermediate level in lung. Weakly or not expressed in brain, heart, spleen and testis. {ECO:0000269|PubMed:11882650}. +Q9D3F7 DDIT4_MOUSE DNA damage-inducible transcript 4 protein (Dexamethasone-induced gene 2 protein) (HIF-1 responsive protein RTP801) (Protein regulated in development and DNA damage response 1) (REDD-1) 229 24,871 Chain (1); Modified residue (3) FUNCTION: Regulates cell growth, proliferation and survival via inhibition of the activity of the mammalian target of rapamycin complex 1 (mTORC1). Inhibition of mTORC1 is mediated by a pathway that involves DDIT4/REDD1, AKT1, the TSC1-TSC2 complex and the GTPase RHEB. Plays an important role in responses to cellular energy levels and cellular stress, including responses to hypoxia and DNA damage. Regulates p53/TP53-mediated apoptosis in response to DNA damage via its effect on mTORC1 activity. Its role in the response to hypoxia depends on the cell type; it mediates mTORC1 inhibition in fibroblasts and thymocytes, but not in hepatocytes. Inhibits neuronal differentiation and neurite outgrowth mediated by NGF via its effect on mTORC1 activity. Required for normal neuron migration during embryonic brain development. Plays a role in neuronal cell death. Required for mTORC1-mediated defense against viral protein synthesis and virus replication. {ECO:0000269|PubMed:15545625, ECO:0000269|PubMed:15988001, ECO:0000269|PubMed:20176937, ECO:0000269|PubMed:21383064, ECO:0000269|PubMed:21896779, ECO:0000269|PubMed:21909097}. PTM: Phosphorylated by GSK3B; this promotes proteasomal degradation. {ECO:0000250}.; PTM: Polyubiquitinated by a DCX (DDB1-CUL4A-RBX1) E3 ubiquitin-protein ligase complex with BTRC as substrate-recognition component, leading to its proteasomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:20176937}. Cytoplasm, cytosol {ECO:0000269|PubMed:20176937}. SUBUNIT: Monomer. Interacts with BTRC. Identified in a complex with CUL4A, DDB1 and BTRC. Interacts with TXNIP; this inhibits the proteasomal degradation of DDIT4 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:12736248, ECO:0000269|PubMed:21383064}. +P28312 DEFA5_MOUSE Alpha-defensin 5 (Defensin-related cryptdin-5) 93 10,519 Disulfide bond (3); Peptide (1); Propeptide (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Probably contributes to the antimicrobial barrier function of the small bowel mucosa. SUBCELLULAR LOCATION: Secreted. +P50707 DEFA9_MOUSE Alpha-defensin 9 (Defensin-related cryptdin-9) 93 10,535 Disulfide bond (3); Peptide (1); Propeptide (1); Signal peptide (1) FUNCTION: Probably contributes to the antimicrobial barrier function of the small bowel mucosa. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Paneth cells of the small bowel. +Q8R2F2 DEGS2_MOUSE Sphingolipid delta(4)-desaturase/C4-monooxygenase DES2 (EC 1.14.18.5) (EC 1.14.19.17) (Degenerative spermatocyte homolog 2) (Sphingolipid 4-desaturase) (Sphingolipid C4-monooxygenase) 323 37,491 Alternative sequence (1); Chain (1); Initiator methionine (1); Lipidation (1); Motif (3); Region (1); Sequence conflict (1); Transmembrane (3) TRANSMEM 41 61 Helical. {ECO:0000255}.; TRANSMEM 68 88 Helical. {ECO:0000255}.; TRANSMEM 210 231 Helical. {ECO:0000255}. Membrane lipid metabolism; sphingolipid biosynthesis. FUNCTION: Bifunctional enzyme which acts as both a sphingolipid delta(4)-desaturase and a sphingolipid C4-monooxygenase. {ECO:0000269|PubMed:11937514, ECO:0000269|PubMed:14731113, ECO:0000269|PubMed:16571104}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16571104, ECO:0000305}; Multi-pass membrane protein {ECO:0000269|PubMed:16571104, ECO:0000305}. TISSUE SPECIFICITY: Highly expressed in intestinal crypt cells and adjacent epithelial cells (at protein level). {ECO:0000269|PubMed:14731113}. +Q8CFK6 DEN1C_MOUSE DENN domain-containing protein 1C (Connecdenn 3) 786 86,689 Alternative sequence (2); Chain (1); Domain (3); Modified residue (1); Motif (2) FUNCTION: Guanine nucleotide exchange factor (GEF) which may activate RAB8A, RAB13 and RAB35. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. {ECO:0000250|UniProtKB:Q8IV53}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8IV53}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:Q8IV53}. SUBUNIT: Exhibits low nucleotide-independent RAB35-binding activity. Interacts with clathrin heavy chain/CLTC and with AP2A2, but not with AP2B1. {ECO:0000250|UniProtKB:Q8IV53}. +Q8BH88 DEP1B_MOUSE DEP domain-containing protein 1B 529 61,908 Chain (1); Compositional bias (1); Domain (2); Modified residue (2); Sequence conflict (2) +P31001 DESM_MOUSE Desmin 469 53,498 Chain (1); Compositional bias (1); Domain (1); Modified residue (21); Mutagenesis (6); Region (11); Site (1) FUNCTION: Muscle-specific type III intermediate filament essential for proper muscular structure and function. Plays a crucial role in maintaining the structure of sarcomeres, inter-connecting the Z-disks and forming the myofibrils, linking them not only to the sarcolemmal cytoskeleton, but also to the nucleus and mitochondria, thus providing strength for the muscle fiber during activity (By similarity). In adult striated muscle they form a fibrous network connecting myofibrils to each other and to the plasma membrane from the periphery of the Z-line structures (PubMed:25394388). May act as a sarcomeric microtubule-anchoring protein: specifically associates with detyrosinated tubulin-alpha chains, leading to buckled microtubules and mechanical resistance to contraction (PubMed:27102488). Contributes to the transcriptional regulation of the NKX2-5 gene in cardiac progenitor cells during a short period of cardiomyogenesis and in cardiac side population stem cells in the adult. Plays a role in maintaining an optimal conformation of nebulette (NEB) on heart muscle sarcomeres to bind and recruit cardiac alpha-actin (PubMed:27733623). {ECO:0000250|UniProtKB:P17661, ECO:0000269|PubMed:25394388, ECO:0000269|PubMed:27102488, ECO:0000269|PubMed:27733623}. PTM: ADP-ribosylation prevents ability to form intermediate filaments. {ECO:0000250|UniProtKB:P48675}.; PTM: Phosphorylation at Ser-7, Ser-28 and Ser-32 by CDK1, phosphorylation at Ser-60 by AURKB and phosphorylation at Thr-76 by ROCK1 contribute to efficient separation of desmin intermediate filaments during mitosis. {ECO:0000269|PubMed:27565725}. SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:26787680, ECO:0000269|PubMed:28469177}. Cytoplasm {ECO:0000269|PubMed:25394388, ECO:0000269|PubMed:26787680}. Cell membrane, sarcolemma {ECO:0000269|PubMed:25394388}. Nucleus {ECO:0000269|PubMed:26787680}. Note=Localizes in the intercalated disks which occur at the Z line of cardiomyocytes (By similarity). Localizes in the nucleus exclusively in differentiating cardiac progenitor cells and premature cardiomyocytes (PubMed:26787680). {ECO:0000250|UniProtKB:P17661, ECO:0000269|PubMed:26787680}. SUBUNIT: Homopolymer. Interacts with MTM1 (By similarity). Interacts with DST (PubMed:10357897). Interacts with tubulin-alpha; specifically associates with detyrosinated tubulin-alpha (PubMed:27102488). Interacts with EPPK1; interaction is dependent of higher-order structure of intermediate filament. Interacts with CRYAB. Interacts with NEB (via nebulin repeats 160-164). Interacts (via rod region) with NEBL (via nebulin repeats 1-5) (By similarity). {ECO:0000250|UniProtKB:P17661, ECO:0000269|PubMed:10357897, ECO:0000269|PubMed:27102488}. TISSUE SPECIFICITY: Cardiac progenitor cells and immature cardiomyocytes (at protein level). {ECO:0000269|PubMed:26787680}. +Q9D0A0 DET1_MOUSE DET1 homolog (De-etiolated-1 homolog) 550 63,837 Chain (1) FUNCTION: Component of the E3 ubiquitin ligase DCX DET1-COP1 complex, which is required for ubiquitination and subsequent degradation of target proteins. The complex is involved in JUN ubiquitination and degradation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the DCX DET1-COP1 ubiquitin ligase complex at least composed of RBX1, DET1, DDB1, CUL4A and COP1. {ECO:0000250}. +Q3L180 DFA26_MOUSE Alpha-defensin 26 (Defensin-related cryptdin-26) 93 10,514 Disulfide bond (3); Peptide (1); Propeptide (1); Signal peptide (1) FUNCTION: May have microbicidal activities. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +Q70KL2 DFB40_MOUSE Beta-defensin 40 (BD-40) (mBD-40) (Defensin, beta 40) 73 8,616 Chain (1); Disulfide bond (3); Sequence conflict (1); Signal peptide (1) FUNCTION: Has antibacterial activity. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. TISSUE SPECIFICITY: Only expressed in epididymis (corpus, cauda and caput). {ECO:0000269|PubMed:14718547}. +Q30KP6 DFB41_MOUSE Beta-defensin 41 (BD-41) (mBD-41) (Defensin, beta 41) 65 7,663 Alternative sequence (1); Chain (1); Disulfide bond (3); Signal peptide (1) FUNCTION: Has bactericidal activity. {ECO:0000250|UniProtKB:P81534}.; FUNCTION: Isoform 2 may play a role in the antimicrobial protection of sperm and urogenital tract epithelia. {ECO:0000269|PubMed:16023745}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P60022}. TISSUE SPECIFICITY: Isoform 2 is epididymis-specific and expressed mainly in the proximal caput. {ECO:0000269|PubMed:16023745}. +Q6TU36 DFB50_MOUSE Beta-defensin 50 (BD-50) (mBD-50) (Defensin, beta 37) (Defensin, beta 50) (Prostate beta-defensin 1) 73 8,058 Chain (1); Disulfide bond (2); Signal peptide (1) FUNCTION: Has bactericidal activity. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in prostate. Not expressed in uterus, epididymis, ovary, testis, spleen, submaxillary gland, thymus, thyroid, pancreas, smooth muscle, skeletal muscle, heart, kidney, lung, liver, eye and brain. {ECO:0000269|PubMed:14659016}. +Q8R2I8 DFB10_MOUSE Beta-defensin 10 (BD-10) (mBD-10) (Defensin, beta 10) 73 8,393 Chain (1); Disulfide bond (3); Signal peptide (1) FUNCTION: Has antibacterial activity. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. TISSUE SPECIFICITY: Expressed in both adult and neonate brain, and very weakly in kidneys, epididymis, and testis. {ECO:0000269|PubMed:12644567}. +A2ADU8 DG2L6_MOUSE Diacylglycerol O-acyltransferase 2-like protein 6 (EC 2.3.1.-) 337 38,362 Chain (1); Transmembrane (2) TRANSMEM 22 42 Helical. {ECO:0000255}.; TRANSMEM 102 122 Helical. {ECO:0000255}. FUNCTION: Probable acyltransferase uses fatty acyl-CoA as substrate. Has no wax synthase activity to produce wax esters. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +O54788 DFFB_MOUSE DNA fragmentation factor subunit beta (EC 3.-.-.-) (Caspase-activated deoxyribonuclease) (CAD) (Caspase-activated DNase) (DNA fragmentation factor 40 kDa subunit) (DFF-40) 344 39,449 Beta strand (9); Chain (1); Domain (1); Helix (13); Turn (10) FUNCTION: Nuclease that induces DNA fragmentation and chromatin condensation during apoptosis. Degrades naked DNA and induces apoptotic morphology. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. SUBUNIT: Heterodimer of DFFA and DFFB. Interacts with HIST1H1A (By similarity). {ECO:0000250}. +Q30KN8 DFB25_MOUSE Beta-defensin 25 (BD-25) (mBD-25) (Defensin, beta 25) 71 7,961 Chain (1); Disulfide bond (3); Signal peptide (1) FUNCTION: Has antibacterial activity. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +P50714 DFA16_MOUSE Alpha-defensin 16 (Defensin-related cryptdin-16) 93 10,430 Disulfide bond (3); Peptide (1); Propeptide (1); Signal peptide (1) FUNCTION: Probably contributes to the antimicrobial barrier function of the small bowel mucosa. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Paneth cells of the small bowel. +Q9R1C6 DGKE_MOUSE Diacylglycerol kinase epsilon (DAG kinase epsilon) (EC 2.7.1.107) (Diglyceride kinase epsilon) (DGK-epsilon) 564 63,635 Chain (1); Domain (1); Transmembrane (2); Zinc finger (2) TRANSMEM 20 40 Helical. {ECO:0000255}.; TRANSMEM 433 453 Helical. {ECO:0000255}. FUNCTION: Highly selective for arachidonate-containing species of diacylglycerol (DAG). May terminate signals transmitted through arachidonoyl-DAG or may contribute to the synthesis of phospholipids with defined fatty acid composition (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}. TISSUE SPECIFICITY: Expressed in platelets. {ECO:0000269|PubMed:23542698}. +O70503 DHB12_MOUSE Very-long-chain 3-oxoacyl-CoA reductase (EC 1.1.1.330) (17-beta-hydroxysteroid dehydrogenase 12) (17-beta-HSD 12) (3-ketoacyl-CoA reductase) (KAR) (Estradiol 17-beta-dehydrogenase 12) (EC 1.1.1.62) (KIK-I) 312 34,742 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Motif (1); Nucleotide binding (1); Sequence conflict (3); Transmembrane (3) TRANSMEM 4 24 Helical. {ECO:0000255}.; TRANSMEM 182 202 Helical. {ECO:0000255}.; TRANSMEM 269 285 Helical. {ECO:0000255}. Lipid metabolism; fatty acid biosynthesis. Steroid biosynthesis; estrogen biosynthesis. FUNCTION: Catalyzes the second of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme has a 3-ketoacyl-CoA reductase activity, reducing 3-ketoacyl-CoA to 3-hydroxyacyl-CoA, within each cycle of fatty acid elongation. Thereby, it may participate in the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. May also catalyze the transformation of estrone (E1) into estradiol (E2) and play a role in estrogen formation. {ECO:0000250|UniProtKB:Q53GQ0}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q53GQ0}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q53GQ0}. DOMAIN: The di-lysine motif confers endoplasmic reticulum localization for type I membrane proteins. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in most tissues tested. {ECO:0000269|PubMed:12482854}. +P70385 DHB3_MOUSE Testosterone 17-beta-dehydrogenase 3 (EC 1.1.1.64) (17-beta-hydroxysteroid dehydrogenase type 3) (17-beta-HSD 3) (Testicular 17-beta-hydroxysteroid dehydrogenase) 305 34,330 Active site (1); Binding site (1); Chain (1); Nucleotide binding (1); Sequence conflict (3) Hormone biosynthesis; testosterone biosynthesis. FUNCTION: Favors the reduction of androstenedione to testosterone. Uses NADPH while the two other EDH17B enzymes use NADH. {ECO:0000250|UniProtKB:P37058}. SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:P37058}. +Q91WC9 DGLB_MOUSE Sn1-specific diacylglycerol lipase beta (DGL-beta) (EC 3.1.1.-) 669 73,905 Active site (2); Chain (1); Frameshift (1); Modified residue (3); Sequence conflict (1); Topological domain (5); Transmembrane (4) TRANSMEM 18 38 Helical. {ECO:0000255}.; TRANSMEM 59 79 Helical. {ECO:0000255}.; TRANSMEM 103 123 Helical. {ECO:0000255}.; TRANSMEM 129 149 Helical. {ECO:0000255}. TOPO_DOM 1 17 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 39 58 Extracellular. {ECO:0000255}.; TOPO_DOM 80 102 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 124 128 Extracellular. {ECO:0000255}.; TOPO_DOM 150 669 Cytoplasmic. {ECO:0000255}. FUNCTION: Catalyzes the hydrolysis of diacylglycerol (DAG) to 2-arachidonoyl-glycerol (2-AG), the most abundant endocannabinoid in tissues. Required for axonal growth during development and for retrograde synaptic signaling at mature synapses (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: In embryonic brains, it is present in axonal tracts, while in adults it localizes to dendritic fields, correlating with the developmental change in requirement for 2-AG synthesis from the pre- to the postsynaptic compartment (at protein level). {ECO:0000269|PubMed:14610053}. +B9EJR8 DAAF5_MOUSE Dynein assembly factor 5, axonemal (HEAT repeat-containing protein 2) 853 93,851 Chain (1); Initiator methionine (1); Modified residue (1); Repeat (9) FUNCTION: Cytoplasmic protein involved in the delivery of the dynein machinery to the motile cilium. It is required for the assembly of the axonemal dynein inner and outer arms, two structures attached to the peripheral outer doublet A microtubule of the axoneme, that play a crucial role in cilium motility. {ECO:0000250|UniProtKB:Q86Y56}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25232951}. Cytoplasmic granule {ECO:0000250|UniProtKB:Q86Y56}. Note=Observed only in the cytoplasm of ciliated cells and absent from cilia. {ECO:0000269|PubMed:25232951}. SUBUNIT: Interacts with DNAI2; probably involved in outer arm dynein assembly. {ECO:0000250|UniProtKB:Q86Y56}. TISSUE SPECIFICITY: Expressed in ciliated cells including ependymal cells lining the lateral ventricles and multiciliated epithelium of oviduct ampulla. {ECO:0000269|PubMed:25232951}. +P97318 DAB1_MOUSE Disabled homolog 1 588 63,578 Alternative sequence (9); Beta strand (8); Chain (1); Domain (1); Helix (5); Modified residue (4); Mutagenesis (10); Sequence conflict (5); Turn (2) FUNCTION: Adapter molecule functioning in neural development. May regulate SIAH1 activity. {ECO:0000269|PubMed:9009273}. PTM: Phosphorylated on Tyr-198 and Tyr-220 upon reelin induction in embryonic neurons (PubMed:11279201). Also found phosphorylated on Tyr-232 upon reelin induction (PubMed:15062102). Also phosphorylated on Ser-524 independently of reelin signaling. {ECO:0000269|PubMed:10959835, ECO:0000269|PubMed:11279201, ECO:0000269|PubMed:12077184, ECO:0000269|PubMed:15062102}. SUBUNIT: Associates with the SH2 domains of SRC, FYN and ABL. Interacts (phosphorylated on tyrosine residues) with CRK and CRKL (via respective SH2 domain) (PubMed:15062102). Interacts with SIAH1, LRP8 and VLDLR (PubMed:12646221, PubMed:12737822). Interacts with LRP1 (By similarity). Interacts with APLP1 (via NPXY motif) (PubMed:12826668). Interacts with DAB2IP (By similarity). {ECO:0000250|UniProtKB:O75553, ECO:0000250|UniProtKB:Q8CJH2, ECO:0000269|PubMed:12646221, ECO:0000269|PubMed:12737822, ECO:0000269|PubMed:12826668, ECO:0000269|PubMed:15062102, ECO:0000269|PubMed:9009273}. DOMAIN: The PID domain specifically binds to the Asn-Pro-Xaa-Tyr(P) motif found in many tyrosine-phosphorylated proteins. TISSUE SPECIFICITY: Expressed mainly in brain. {ECO:0000269|PubMed:9009273}. +O54784 DAPK3_MOUSE Death-associated protein kinase 3 (DAP kinase 3) (EC 2.7.11.1) (DAP-like kinase) (Dlk) (MYPT1 kinase) (ZIP-kinase) 448 51,422 Active site (1); Binding site (3); Chain (1); Domain (1); Modified residue (9); Mutagenesis (6); Nucleotide binding (1); Region (3) FUNCTION: Serine/threonine kinase which is involved in the regulation of apoptosis, autophagy, transcription, translation and actin cytoskeleton reorganization. Regulates both type I (caspase-dependent) apoptotic and type II (caspase-independent) autophagic cell deaths signal, depending on the cellular setting. Involved in formation of promyelocytic leukemia protein nuclear body (PML-NB). Involved in apoptosis involving PAWR which mediates cytoplasmic relocation; in vitro phosphorylates PAWR (By similarity). Phosphorylates MYL12B in non-muscle cells leading to reorganization of actin cytoskeleton such as in regulation of cell polarity and cell migration. Positively regulates canonical Wnt/beta-catenin signaling through interaction with NLK and TCF7L2; disrupts the NLK-TCF7L2 complex thereby influencing the phosphorylation of TCF7L2 by NLK. Phosphorylates STAT3 and enhances its transcriptional activity. Enhances transcription from AR-responsive promoters in a hormone- and kinase-dependent manner. Phosphorylates histone H3 on 'Thr-11' at centromeres during mitosis (By similarity). Phosphorylates RPL13A on 'Ser-77' upon interferon-gamma activation which is causing RPL13A release from the ribosome, RPL13A association with the GAIT complex and its subsequent involvement in transcript-selective translation inhibition. {ECO:0000250|UniProtKB:O88764, ECO:0000269|PubMed:12917339, ECO:0000269|PubMed:15096528, ECO:0000269|PubMed:16219639, ECO:0000269|PubMed:21454679, ECO:0000269|PubMed:23071094, ECO:0000269|PubMed:9488481}. PTM: Ubiquitinated. Ubiquitination mediated by the UBE2D3 E3 ligase does not lead to proteasomal degradation, but influences promyelocytic leukemia protein nuclear bodies (PML-NBs) formation in the nucleus. {ECO:0000269|PubMed:18515077}.; PTM: The phosphorylation status is critical for kinase activity, oligomerization and intracellular localization. Phosphorylation at Thr-180, Thr-225 and Thr-265 is essential for activity. The phosphorylated form is localized in the cytoplasm and nuclear translocation or retention is maximal when it is not phosphorylated. Phosphorylation increases the trimeric form, and its dephosphorylation favors a kinase-inactive monomeric form. {ECO:0000250|UniProtKB:O43293}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18515077, ECO:0000269|PubMed:20854903, ECO:0000269|PubMed:9488481}. Nucleus, PML body {ECO:0000269|PubMed:12917339}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:O88764}. Chromosome, centromere {ECO:0000250|UniProtKB:O88764}. Cytoplasm {ECO:0000250|UniProtKB:O88764}. Note=Predominantly localized to the nucleus. Relocates to the cytoplasm on binding PAWR where the complex appears to interact with actin filaments. Associated with the centrosomes throughout the mitotic cell cycle, with the centromeres from prophase to anaphase and with the contractile ring during cytokinesis (By similarity). {ECO:0000250|UniProtKB:O88764}. SUBUNIT: Homooligomer in its kinase-active form (homotrimers and homodimers are reported); monomeric in its kinase-inactive form. Homodimerization is required for activation segment autophosphorylation (By similarity). Interacts with DAXX, PAWR, ATF4, NLK, TCF7L2, UBE2D1, UBE2D2, UBE2D3, and CDC5L. Interacts with AR; enhanced by AATF. {ECO:0000250|UniProtKB:O43293, ECO:0000269|PubMed:12917339, ECO:0000269|PubMed:16219639, ECO:0000269|PubMed:18515077, ECO:0000269|PubMed:21454679, ECO:0000269|PubMed:9488481}. TISSUE SPECIFICITY: Highly expressed in heart, brain, lung, skeletal muscle, kidney and testis. Lower levels in liver and spleen. {ECO:0000269|PubMed:9488481}. +Q8BGZ3 DCA12_MOUSE DDB1- and CUL4-associated factor 12 (WD repeat-containing protein 40A) 453 50,459 Chain (1); Erroneous initiation (1); Frameshift (1); Modified residue (1); Repeat (4); Sequence conflict (4) Protein modification; protein ubiquitination. FUNCTION: May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. SUBUNIT: Interacts with DDB1. {ECO:0000250}. +Q9DC22 DCAF6_MOUSE DDB1- and CUL4-associated factor 6 (IQ motif and WD repeat-containing protein 1) (Nuclear receptor interaction protein) (NRIP) 876 97,588 Chain (1); Domain (1); Modified residue (6); Repeat (7) Protein modification; protein ubiquitination. FUNCTION: Ligand-dependent coactivator of nuclear receptors. Enhance transcriptional activity of the nuclear receptors NR3C1 and AR. May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with the nuclear receptors NR3C1 and AR in the presence of ligand. Interacts with DDB1, CUL4A and CUL4B (By similarity). {ECO:0000250}. +P61963 DCAF7_MOUSE DDB1- and CUL4-associated factor 7 (WD repeat-containing protein 68) (WD repeat-containing protein An11 homolog) 342 38,926 Chain (1); Repeat (4) Protein modification; protein ubiquitination. FUNCTION: Involved in craniofacial development. Acts upstream of the EDN1 pathway and is required for formation of the upper jaw equivalent, the palatoquadrate. The activity required for EDN1 pathway function differs between the first and second arches. Associates with DIAPH1 and controls GLI1 transcriptional activity. Could be involved in skin development. May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000250}. Note=Overexpression of DIAHP1 or active RHOA causes translocation from the nucleus to cytoplasm. SUBUNIT: Interacts with DYRK1A, DYRK1B and DIAPH1. Interacts with DDB1. Interacts with ZNF703 (By similarity). {ECO:0000250}. +Q8N7N5 DCAF8_MOUSE DDB1- and CUL4-associated factor 8 (WD repeat-containing protein 42A) 591 66,031 Alternative sequence (2); Chain (1); Erroneous initiation (1); Modified residue (6); Motif (1); Repeat (7) Protein modification; protein ubiquitination. FUNCTION: May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5TAQ9}. Cytoplasm {ECO:0000250|UniProtKB:Q5TAQ9}. Note=It shuttles between the nucleus and the cytoplasm. Nuclear import is mediated by KPNA1 and KPNB1 under the regulation of nuclear GTPase RAN. Nuclear export to the cytoplasm is XPO1 dependent. {ECO:0000250|UniProtKB:Q5TAQ9}. SUBUNIT: Interacts with DDB1, CUL4A and CUL4B. Interacts with KPNA1, KPNB1 and XPO1. {ECO:0000250, ECO:0000250|UniProtKB:Q5TAQ9}. TISSUE SPECIFICITY: Expressed in the brain. {ECO:0000269|PubMed:11401431}. +Q3TUL7 DCA17_MOUSE DDB1- and CUL4-associated factor 17 519 58,400 Alternative sequence (3); Chain (1); Compositional bias (1); Sequence conflict (2); Transmembrane (2) TRANSMEM 186 206 Helical. {ECO:0000255}.; TRANSMEM 222 242 Helical. {ECO:0000255}. Protein modification; protein ubiquitination. FUNCTION: May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Nucleus, nucleolus {ECO:0000269|PubMed:19026396}. Note=According to PubMed:19026396, it is a nucleolar protein, while sequence analysis programs clearly predict 2 transmembrane regions. SUBUNIT: Interacts with DDB1, CUL4A and CUL4B. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed in the embryo, with higher expression in brain, liver and skin tissues. {ECO:0000269|PubMed:19026396}. +P0DMN7 DCAM1_MOUSE S-adenosylmethionine decarboxylase proenzyme 1 (AdoMetDC 1) (SAMDC 1) (EC 4.1.1.50) [Cleaved into: S-adenosylmethionine decarboxylase 1 alpha chain; S-adenosylmethionine decarboxylase 1 beta chain] 334 38,272 Active site (6); Binding site (4); Chain (2); Modified residue (2); Site (1) Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1. FUNCTION: Essential for biosynthesis of the polyamines spermidine and spermine. Promotes maintenance and self-renewal of embryonic stem cells, by maintaining spermine levels. {ECO:0000269|PubMed:22391449}. PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain. {ECO:0000250|UniProtKB:P17707}. SUBUNIT: Heterotetramer of two alpha and two beta chains. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in embryonic stem cells; subsequently down-regulated in differentiating neural precursor cells. {ECO:0000269|PubMed:22391449}. +Q5DU00 DCDC2_MOUSE Doublecortin domain-containing protein 2 475 51,953 Alternative sequence (2); Chain (1); Domain (2); Erroneous initiation (1); Modified residue (1); Sequence conflict (2) FUNCTION: Protein that plays a role in the inhibition of canonical Wnt signaling pathway (By similarity). May be involved in neuronal migration during development of the cerebral neocortex (By similarity). Involved in the control of ciliogenesis and ciliary length (By similarity). {ECO:0000250|UniProtKB:D3ZR10, ECO:0000250|UniProtKB:Q9UHG0}. SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000250|UniProtKB:Q9UHG0}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q9UHG0}. Cell projection, kinocilium {ECO:0000250|UniProtKB:D3ZR10}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:D3ZR10}. Note=Localizes to the ciliary axoneme and to mitotic spindle fibers in a cell-cycle-dependent manner. {ECO:0000250|UniProtKB:Q9UHG0}. SUBUNIT: Interacts with DVL1, DVL2 and DVL3. {ECO:0000250|UniProtKB:Q9UHG0}. TISSUE SPECIFICITY: Expressed in hair cells of the inner ear. {ECO:0000269|PubMed:25601850}. +O88809 DCX_MOUSE Neuronal migration protein doublecortin (Doublin) (Lissencephalin-X) (Lis-X) 366 40,613 Chain (1); Compositional bias (1); Domain (2); Modified residue (24); Mutagenesis (8); Sequence conflict (2) FUNCTION: Microtubule-associated protein required for initial steps of neuronal dispersion and cortex lamination during cerebral cortex development. May act by competing with the putative neuronal protein kinase DCLK1 in binding to a target protein. May in that way participate in a signaling pathway that is crucial for neuronal interaction before and during migration, possibly as part of a calcium ion-dependent signal transduction pathway. May participate along with PAFAH1B1/LIS-1 in a distinct overlapping signaling pathway that promotes neuronal migration. {ECO:0000250|UniProtKB:Q9ESI7}. PTM: Phosphorylation by MARK1, MARK2 and PKA regulates its ability to bind microtubules (By similarity). Phosphorylation at Ser-265 and Ser-297 seems to occur only in neonatal brain, the levels falling precipitously by postnatal day 21 (PubMed:15099191, PubMed:22807455). {ECO:0000250|UniProtKB:Q9ESI7, ECO:0000269|PubMed:15099191, ECO:0000269|PubMed:22807455}.; PTM: Ubiquitinated by MDM2, leading to its degradation by the proteasome (PubMed:25088421). Ubiquitinated by MDM2 and subsequent degradation leads to reduce the dendritic spine density of olfactory bulb granule cells (PubMed:25088421). {ECO:0000269|PubMed:25088421}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Cell projection {ECO:0000250|UniProtKB:Q9ESI7}. Note=Localizes at neurite tips. {ECO:0000250|UniProtKB:Q9ESI7}. SUBUNIT: Interacts with tubulin. Interacts with USP9X. {ECO:0000250|UniProtKB:O43602}. TISSUE SPECIFICITY: In neonatal tissues, highly expressed in brain, but not expressed in heart, liver, kidney and spleen. In adult tissues, faintly expressed in brain but not expressed in muscle, heart, lung, liver, spleen, intestine, kidney, testis and placenta. +Q9D9Z5 DDA1_MOUSE DET1- and DDB1-associated protein 1 102 11,753 Chain (1); Initiator methionine (1); Modified residue (3) FUNCTION: May be involved in ubiquitination and subsequent proteasomal degradation of target proteins. Component of the DDD-E2 complexes which may provide a platform for interaction with CUL4A and WD repeat proteins (By similarity). {ECO:0000250}. SUBUNIT: Part of the DDD core complex containing DET1, DDA1 and DDB1. The DDD core complex recruits a specific UBE2E enzyme, such as UBE2E1, UBE2E2 UBE2E3, to form specific DDD-E2 complexes (By similarity). {ECO:0000250}. +Q9QY15 DDX25_MOUSE ATP-dependent RNA helicase DDX25 (EC 3.6.4.13) (DEAD box protein 25) (Gonadotropin-regulated testicular RNA helicase) 484 54,876 Alternative sequence (1); Chain (1); Domain (2); Modified residue (1); Motif (4); Nucleotide binding (1); Sequence conflict (1) FUNCTION: ATP-dependent RNA helicase. Required for mRNA export and translation regulation during spermatid development. {ECO:0000269|PubMed:16968703}. PTM: Phosphorylated on threonine residues. The phosphorylated form is found in the cytoplasm but not in the nucleus. {ECO:0000269|PubMed:16968703}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Detected in both cytoplasm and nucleus of testicular cells. Also detected in chromatoid bodies of round spermatids. TISSUE SPECIFICITY: Isoform 1 is expressed in germ cells. Isoform 2 is expressed in Leydig cells and in round spermatids of adult testis upon gonadotropin stimulation. {ECO:0000269|Ref.2}. +P56386 DEFB1_MOUSE Beta-defensin 1 (BD-1) (mBD-1) (Defensin, beta 1) 69 7,749 Disulfide bond (3); Peptide (1); Propeptide (1); Signal peptide (1) FUNCTION: Has bactericidal activity. May act as a ligand for C-C chemokine receptor CCR6. Positively regulates the sperm motility and bactericidal activity in a CCR6-dependent manner. Binds to CCR6 and triggers Ca2+ mobilization in the sperm which is important for its motility. {ECO:0000250|UniProtKB:P60022}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P60022}. Membrane {ECO:0000250|UniProtKB:P60022}. Note=Associates with tumor cell membrane-derived microvesicles. {ECO:0000250|UniProtKB:P60022}. SUBUNIT: Monomer. Homodimer. {ECO:0000250|UniProtKB:P60022}. TISSUE SPECIFICITY: Detected in kidney. {ECO:0000269|PubMed:10922379}. +Q9Z1T5 DEAF1_MOUSE Deformed epidermal autoregulatory factor 1 homolog (Nuclear DEAF-1-related transcriptional regulator) (NUDR) 566 59,633 Alternative sequence (3); Chain (1); Compositional bias (2); Domain (1); Modified residue (6); Motif (1); Mutagenesis (1); Region (1); Zinc finger (1) FUNCTION: Transcription factor that binds to sequence with multiple copies of 5'-TTC[CG]G-3' present in its own promoter and that of the HNRPA2B1 gene. Down-regulates transcription of these genes. Binds to the retinoic acid response element (RARE) 5'-AGGGTTCACCGAAAGTTCA-3'. Activates the proenkephalin gene independently of promoter binding, probably through protein-protein interaction (By similarity). Regulates epithelial cell proliferation and side-branching in the mammary gland. Required for neural tube closure and skeletal patterning. Controls the expression of peripheral tissue antigens in pancreatic lymph nodes. Isoform 1 displays greater transcriptional activity than isoform 2. Isoform 2 may inhibit transcriptional activity of isoform 1 by interacting with it and retaining it in the cytoplasm. Transcriptional activator of EIF4G3 (By similarity). May also involved in behavior (PubMed:24726472). {ECO:0000250|UniProtKB:O75398, ECO:0000269|PubMed:14966286, ECO:0000269|PubMed:18826651, ECO:0000269|PubMed:19668219, ECO:0000269|PubMed:24726472}. PTM: May be phosphorylated by DNA-PK complex in a DNA independent manner (in vitro). {ECO:0000250}. SUBCELLULAR LOCATION: Isoform 1: Nucleus. Cytoplasm {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Nucleus. Note=Displays some nuclear localization when expressed with isoform 1, suggesting that it may heterodimerize with isoform 1 and shuttle to the nucleus using the nuclear localization signal of isoform 1. SUBUNIT: Homodimer (By similarity). Isoform 1 and isoform 2 may form a heterodimer. May interact with the corepressors NCOR1 and NCRO2 (By similarity). Identified in a complex with XRCC5 and XRCC6. Interacts (via the SAND domain) with the DNA-PK complex subunit XRCC6; the interaction is direct with XRCC6 and may be inhibited by DNA-binding (By similarity). Interacts with LMO4; LMO4 blocks export from nucleus. Interacts with LMO2 and CLIM2. {ECO:0000250, ECO:0000269|PubMed:22723967, ECO:0000269|PubMed:9860983}. TISSUE SPECIFICITY: Ubiquitously expressed during embryogenesis, with higher expression in regions of the central nervous system, dorsal root ganglia, submandibular gland, epidermis and breast. In 12-week-old NOD mice, expression of isoform 2 is sevenfold higher in lymph node stromal elements than in T-cells and tenfold higher than in B-cells. {ECO:0000269|PubMed:9860983}. +Q9CWX9 DDX47_MOUSE Probable ATP-dependent RNA helicase DDX47 (EC 3.6.4.13) (DEAD box protein 47) 455 50,639 Chain (1); Domain (2); Initiator methionine (1); Modified residue (3); Motif (2); Nucleotide binding (1) FUNCTION: Involved in apoptosis. May have a role in rRNA processing and mRNA splicing. Associates with pre-rRNA precursors (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Note=Localizes in the nucleolar-organizing region during ribosome biogenesis. {ECO:0000250}. SUBUNIT: Interacts with AGO1 and AGO2. Interacts with GABARAP. Interacts with NOL8; the interaction is RNA-dependent (By similarity). {ECO:0000250}. +Q91VD6 DEFB6_MOUSE Beta-defensin 6 (BD-6) (mBD-6) (Defensin, beta 6) 63 6,977 Chain (1); Disulfide bond (3); Modified residue (1); Signal peptide (1) FUNCTION: Has potent antibacterial activity against E.coli (ATCC 25922). {ECO:0000269|PubMed:11408484}. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Predominantly expressed in skeletal muscle, also expressed in esophagus, tongue, and trachea. Also expressed in lung when induced by lipopolysaccharide. {ECO:0000269|PubMed:11408484}. +O08917 FLOT1_MOUSE Flotillin-1 428 47,513 Chain (1); Modified residue (4) FUNCTION: May act as a scaffolding protein within caveolar membranes, functionally participating in formation of caveolae or caveolae-like vesicles. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O75955}; Peripheral membrane protein {ECO:0000250|UniProtKB:O75955}. Endosome {ECO:0000250|UniProtKB:O75955}. Membrane, caveola {ECO:0000269|PubMed:9153235}; Peripheral membrane protein {ECO:0000269|PubMed:9153235}. Melanosome {ECO:0000250|UniProtKB:O75955}. Membrane raft {ECO:0000250|UniProtKB:O75955}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV (By similarity). Membrane-associated protein of caveola (PubMed:9153235). {ECO:0000250|UniProtKB:O75955, ECO:0000269|PubMed:9153235}. SUBUNIT: Heterooligomeric complex of flotillin-1 and flotillin-2 and caveolin-1 and caveolin-2. Interacts with ECPAS (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: High expression in brain, white adipose tissue, heart muscle, skeletal muscle and lung. Low expression in spleen, liver and testis. +P28309 DEFA2_MOUSE Alpha-defensin 2 (Cryptdin-1) (Defensin-related cryptdin-2) 93 10,560 Disulfide bond (3); Peptide (1); Propeptide (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Has broad-spectrum antimicrobial properties. Has antibacterial activity against the Gram-positive bacterium L.monocytogenes EGD and the Gram-negative bacteria E.coli ML-35p and avirulent S.typhimurium 7953, but not against the mouse-virulent S.typhimurium 14028S. Probably contributes to the antimicrobial barrier function of the small bowel mucosa. {ECO:0000269|PubMed:1500163}. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Paneth cells of the small bowel. +Q7TNV0 DEK_MOUSE Protein DEK 380 43,159 Chain (1); Compositional bias (4); DNA binding (2); Domain (1); Modified residue (27); Motif (1); Sequence conflict (2) FUNCTION: Involved in chromatin organization. {ECO:0000269|PubMed:17524367}. PTM: Phosphorylated by CK2. Phosphorylation fluctuates during the cell cycle with a moderate peak during G(1) phase, and weakens the binding of DEK to DNA (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17524367}. Note=Enriched in regions where chromatin is decondensed or sparse in the interphase nuclei. {ECO:0000250}. SUBUNIT: Found in a mRNA splicing-dependent exon junction complex (EJC) with DEK, RBM8A, RNPS1, SRRM1 and ALYREF/THOC4. Interacts with histones H2A, H2B, H3, H4, acetylated histone H4, non-phosphorylated DAXX and HDAC2. Component of the B-WICH complex, at least composed of SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21. Binds DNA (By similarity). {ECO:0000250}. +Q9CQJ6 DENR_MOUSE Density-regulated protein (DRP) 198 22,166 Chain (1); Domain (1); Initiator methionine (1); Modified residue (4) FUNCTION: May be involved in the translation of target mRNAs by scanning and recognition of the initiation codon. Involved in translation initiation; promotes recruitment of aminoacetyled initiator tRNA to P site of 40S ribosomes. Can promote release of deacylated tRNA and mRNA from recycled 40S subunits following ABCE1-mediated dissociation of post-termination ribosomal complexes into subunits (By similarity). {ECO:0000250}. SUBUNIT: Interacts with MCTS1. {ECO:0000250}. +Q91VV4 DEN2D_MOUSE DENN domain-containing protein 2D 469 53,211 Alternative sequence (1); Chain (1); Domain (3); Erroneous initiation (1); Sequence conflict (1) FUNCTION: Guanine nucleotide exchange factor (GEF) which may activate RAB9A and RAB9B. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +Q3U1Y4 DEN4B_MOUSE DENN domain-containing protein 4B (Brain-specific gene 4 protein) (Brain specific protein 4) 1499 164,740 Alternative sequence (5); Chain (1); Compositional bias (2); Domain (4); Erroneous initiation (2); Modified residue (2); Repeat (2); Sequence caution (1); Sequence conflict (1) FUNCTION: Guanine nucleotide exchange factor (GEF) which may activate RAB10. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus. +Q8CIG0 DEP1A_MOUSE DEP domain-containing protein 1A 804 92,201 Alternative sequence (3); Chain (1); Coiled coil (1); Domain (2); Erroneous initiation (1); Modified residue (1); Region (1) FUNCTION: May be involved in transcriptional regulation as a transcriptional corepressor. The DEPDC1A-ZNF224 complex may play a critical role in bladder carcinogenesis by repressing the transcription of the A20 gene, leading to transport of NF-KB protein into the nucleus, resulting in suppression of apoptosis of bladder cancer cells (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Colocalizes with ZNF224 at the nucleus. {ECO:0000250}. SUBUNIT: Can form dimers. Interacts with ZNF224 (By similarity). {ECO:0000250}. +Q9QZZ6 DERM_MOUSE Dermatopontin (Early quiescence protein 1) (EQ-1) (Tyrosine-rich acidic matrix protein) (TRAMP) 201 23,995 Chain (1); Disulfide bond (5); Modified residue (6); Region (2); Repeat (5); Sequence conflict (1); Signal peptide (1) FUNCTION: Seems to mediate adhesion by cell surface integrin binding. May serve as a communication link between the dermal fibroblast cell surface and its extracellular matrix environment. Enhances TGFB1 activity (By similarity). Inhibits cell proliferation. Accelerates collagen fibril formation, and stabilizes collagen fibrils against low-temperature dissociation. {ECO:0000250, ECO:0000269|PubMed:12230512, ECO:0000269|PubMed:14980498}. PTM: Sulfated on tyrosine residue(s). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. SUBUNIT: Interacts with TGFB1, DCN and collagen. {ECO:0000250}. +Q8K3U4 DFB36_MOUSE Beta-defensin 36 (BD-36) (mBD-36) (Defensin, beta 36) 67 7,755 Disulfide bond (3); Peptide (1); Signal peptide (1) FUNCTION: Has antibacterial activity. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +Q7M6Y5 DEUP1_MOUSE Deuterosome assembly protein 1 (Coiled-coil domain-containing protein 67) 601 69,678 Alternative sequence (1); Chain (1); Coiled coil (5); Erroneous initiation (2); Modified residue (1) FUNCTION: Key structural component of the deuterosome, a structure that promotes de novo centriole amplification in multiciliated cells. Deuterosome-mediated centriole amplification occurs in terminally differentiated multiciliated cells and can generate more than 100 centrioles. Probably sufficient for the specification and formation of the deuterosome inner core. Interacts with CEP152 and recruits PLK4 to activate centriole biogenesis. {ECO:0000269|PubMed:24240477}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24240477}. Note=Localizes to the deuterosome. SUBUNIT: Interacts with CEP152; the interaction is mutually exclusive with CEP63. {ECO:0000269|PubMed:24240477}. TISSUE SPECIFICITY: Highly enriched in multicilia-abundant tissues (trachea and oviduct). {ECO:0000269|PubMed:24240477}. +Q30KM9 DFB43_MOUSE Beta-defensin 43 (BD-43) (mBD-43) (Defensin, beta 43) 69 8,252 Chain (1); Disulfide bond (2); Signal peptide (1) FUNCTION: Has bactericidal activity. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +Q8K4N3 DFB12_MOUSE Beta-defensin 12 (BD-12) (mBD-12) (Defensin, beta 12) 78 8,872 Chain (1); Disulfide bond (3); Erroneous initiation (2); Signal peptide (1) FUNCTION: Has antibacterial activity. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. TISSUE SPECIFICITY: Only expressed in epididymis (caput, corpus and cauda). {ECO:0000269|PubMed:14718547}. +P21460 CYTC_MOUSE Cystatin-C (Cystatin-3) 140 15,531 Chain (1); Disulfide bond (2); Motif (1); Sequence conflict (2); Signal peptide (1); Site (1) FUNCTION: As an inhibitor of cysteine proteinases, this protein is thought to serve an important physiological role as a local regulator of this enzyme activity. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +Q9D665 D42E1_MOUSE Short-chain dehydrogenase/reductase family 42E member 1 (EC 1.1.1.-) 394 43,894 Active site (1); Binding site (1); Chain (1); Erroneous initiation (1); Transmembrane (2) TRANSMEM 283 303 Helical. {ECO:0000255}.; TRANSMEM 367 387 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8BPM0 DAAM1_MOUSE Disheveled-associated activator of morphogenesis 1 1077 123,370 Alternative sequence (3); Chain (1); Coiled coil (1); Compositional bias (1); Domain (4); Erroneous initiation (1); Modified residue (3); Region (1); Sequence conflict (3) FUNCTION: Binds to disheveled (Dvl) and Rho, and mediates Wnt-induced Dvl-Rho complex formation. May play a role as a scaffolding protein to recruit Rho-GDP and Rho-GEF, thereby enhancing Rho-GTP formation. Can direct nucleation and elongation of new actin filaments (By similarity). Involved in building functional cilia. Involved in the organization of the subapical actin network in multiciliated epithelial cells (By similarity). Together with DAAM2, required for myocardial maturation and sarcomere assembly (PubMed:26526197). {ECO:0000250|UniProtKB:B0DOB5, ECO:0000250|UniProtKB:Q9Y4D1, ECO:0000269|PubMed:26526197}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y4D1}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q9Y4D1}. Note=Perinuclear. {ECO:0000250|UniProtKB:Q9Y4D1}. SUBUNIT: Interacts with CIP4, FNBP1 and FNBP1L. Interacts with the SH3 domains of Abl, BTK, endophilin, spectrin and SRC. Binds specifically to GTP-bound CDC42 and RHOA. Interacts with INTU; INTU mediates the indirect interaction between DAAM1 and NPHP4 (By similarity). {ECO:0000250|UniProtKB:Q9Y4D1}. DOMAIN: The C-terminal DAD domain may participate in intramolecular interactions with the N-terminus.; DOMAIN: The DAD domain regulates activation via by an autoinhibitory interaction with the GBD/FH3 domain. This autoinhibition is released upon competitive binding of an activated GTPase. The release of DAD allows the FH2 domain to then nucleate and elongate nonbranched actin filaments (By similarity). {ECO:0000250|UniProtKB:O08808}. TISSUE SPECIFICITY: In early embryogenesis, expressed in embryonic and extraembryonic ectoderm. In later stages of gastrulation, expressed also in somites and ribs and posterior vertebrae of developing skeletal system. During organogenesis, expressed in CNS, PNS, stomach, liver and limb bud. {ECO:0000269|PubMed:15464228, ECO:0000269|PubMed:15533824}. +Q3UHC7 DAB2P_MOUSE Disabled homolog 2-interacting protein (DAB2-interacting protein) (ASK-interacting protein 1) (DOC-2/DAB-2 interactive protein) 1189 131,726 Alternative sequence (4); Chain (1); Coiled coil (1); Compositional bias (4); Domain (3); Erroneous initiation (3); Modified residue (4); Region (1); Sequence conflict (5) FUNCTION: Functions as a scaffold protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Involved in several processes such as innate immune response, inflammation and cell growth inhibition, apoptosis, cell survival, angiogenesis, cell migration and maturation. Plays also a role in cell cycle checkpoint control; reduces G1 phase cyclin levels resulting in G0/G1 cell cycle arrest. Mediates signal transduction by receptor-mediated inflammatory signals, such as the tumor necrosis factor (TNF), interferon (IFN) or lipopolysaccharide (LPS). Modulates the balance between phosphatidylinositol 3-kinase (PI3K)-AKT-mediated cell survival and apoptosis stimulated kinase (MAP3K5)-JNK signaling pathways; sequesters both AKT1 and MAP3K5 and counterbalances the activity of each kinase by modulating their phosphorylation status in response to proinflammatory stimuli. Acts as a regulator of the endoplasmic reticulum (ER) unfolded protein response (UPR) pathway; specifically involved in transduction of the ER stress-response to the JNK cascade through ERN1. Mediates TNF-alpha-induced apoptosis activation by facilitating dissociation of inhibitor 14-3-3 from MAP3K5; recruits the PP2A phosphatase complex which dephosphorylates MAP3K5 on 'Ser-966', leading to the dissociation of 13-3-3 proteins and activation of the MAP3K5-JNK signaling pathway in endothelial cells. Mediates also TNF/TRAF2-induced MAP3K5-JNK activation, while it inhibits CHUK-NF-kappa-B signaling. Acts a negative regulator in the IFN-gamma-mediated JAK-STAT signaling cascade by inhibiting smooth muscle cell (VSMCs) proliferation and intimal expansion, and thus, prevents graft arteriosclerosis (GA). Acts as a GTPase-activating protein (GAP) for the ADP ribosylation factor 6 (ARF6) and Ras. Promotes hydrolysis of the ARF6-bound GTP and thus, negatively regulates phosphatidylinositol 4,5-bisphosphate (PIP2)-dependent TLR4-TIRAP-MyD88 and NF-kappa-B signaling pathways in endothelial cells in response to lipopolysaccharides (LPS). Binds specifically to phosphatidylinositol 4-phosphate (PtdIns4P) and phosphatidylinositol 3-phosphate (PtdIns3P). In response to vascular endothelial growth factor (VEGFA), acts as a negative regulator of the VEGFR2-PI3K-mediated angiogenic signaling pathway by inhibiting endothelial cell migration and tube formation. In the developing brain, promotes both the transition from the multipolar to the bipolar stage and the radial migration of cortical neurons from the ventricular zone toward the superficial layer of the neocortex in a glial-dependent locomotion process. Probable downstream effector of the Reelin signaling pathway; promotes Purkinje cell (PC) dendrites development and formation of cerebellar synapses. Functions also as a tumor suppressor protein in prostate cancer progression; prevents cell proliferation and epithelial-to-mesenchymal transition (EMT) through activation of the glycogen synthase kinase-3 beta (GSK3B)-induced beta-catenin and inhibition of PI3K-AKT and Ras-MAPK survival downstream signaling cascades, respectively. {ECO:0000269|PubMed:18281285, ECO:0000269|PubMed:19033661, ECO:0000269|PubMed:19903888, ECO:0000269|PubMed:19948740, ECO:0000269|PubMed:20080667, ECO:0000269|PubMed:20154697, ECO:0000269|PubMed:21700930, ECO:0000269|PubMed:22696229, ECO:0000269|PubMed:23056358, ECO:0000269|PubMed:23326475}. PTM: In response to TNF-alpha-induction, phosphorylated at Ser-728; phosphorylation leads to a conformational change, and thus, increases its association with 14-3-3 proteins, MAP3K5, RIPK1 and TRAF2 in endothelial cells; also stimulates regulatory p85 subunit sequestring and PI3K-p85 complex activity inhibition. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Cell membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Cell projection, dendrite. Note=Colocalizes with TIRAP at the plasma membrane. Colocalizes with ARF6 at the plasma membrane and endocytic vesicles. Translocates from the plasma membrane to the cytoplasm in response to TNF-alpha. Phosphatidylinositol 4-phosphate (PtdIns4P) binding is essential for plasma membrane localization (By similarity). Localized in soma and dendrites of Purkinje cells as well as in scattered cell bodies in the molecular layer of the cerebellum. {ECO:0000250}. SUBUNIT: On plasma membrane, exists in an inactive form complexed with TNFR1; in response to TNF-alpha, dissociates from TNFR1 complex, translocates to cytoplasm and forms part of an intracellular signaling complex comprising TRADD, RALBP1, TRAF2 and MAP3K5. Interacts with DAB1. Part of a cytoplasmic complex made of HIPK1, DAB2IP and MAP3K5 in response to TNF-alpha; this complex formation promotes MAP3K5-JNK activation and subsequent apoptosis. Interacts (via N-terminal domain) with JAK2; the interaction occurs in a IFNG/IFN-gamma-dependent manner and inhibits JAK2 autophosphorylation activity. Interacts (via C2 domain) with GSK3B; the interaction stimulates GSK3B kinase activation. Interacts (via C2 domain) with PPP2CA. Interacts (via proline-rich motif) with a regulatory p85 subunit (via SH3 domain) of the PI3K complex; the interaction inhibits the PI3K-AKT complex activity in a TNF-alpha-dependent manner in prostate cancer (PCa) cells. Interacts with AKT1; the interaction is increased in a TNF-alpha-induced manner. Interacts (via C2 domain and active form preferentially) with KDR/VEGFR2 (tyrosine-phosphorylated active form preferentially); the interaction occurs at the late phase of VEGFA response and inhibits KDR/VEGFR2 activity. Interacts (via N-terminus C2 domain) with MAP3K5 ('Ser-966' dephosphorylated form preferentially); the interaction occurs in a TNF-alpha-induced manner. Interacts (via Ras-GAP domain) with the catalytic subunit of protein phosphatase PP2A; the interaction occurs in resting endothelial cells, is further enhanced by TNF-alpha stimulation and is required to bridge PP2A to MAP3K5. Interacts (via C-terminus PER domain) with TRAF2 (via zinc fingers); the interaction occurs in a TNF-alpha-dependent manner. Interacts with 14-3-3 proteins; the interaction occurs in a TNF-alpha-dependent manner. Interacts (via Ras-GAP domain) with RIPK1 (via kinase domain); the interaction occurs in a TNF-alpha-dependent manner (By similarity). Interacts (via PH domain) with ERN1. Interacts with TRAF2. Interacts (via NPXY motif) with DAB2 (via PID domain). {ECO:0000250, ECO:0000269|PubMed:12877983, ECO:0000269|PubMed:18281285}. DOMAIN: Exists in a closed inactive form by an intramolecular interaction between the N- and the C-terminal domains. The proline-rich motif is critical both for PI3K-AKT activity inhibition and MAP3K5 activation. The PH and C2 domains are necessary for the binding to phosphatidylinositol phosphate. The Ras-GAP domain is necessary for its tumor-suppressive function (By similarity). The C2 and GAP domains constitutively bind to MAP3K5 and facilitate the release of 14-3-3 proteins from MAP3K5. The PH and Ras-GAP domains, but not the NPXY motif, are crucial for its cell membrane localization and neuronal migration function. The PH domain is necessary but not sufficient to activate the JNK signaling pathway through ERN1. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in vascular endothelium of muscle and aorta, in smooth muscle cells of aorta and epithelial cells of lung. Expressed throughout the brain, including olfactory bulb, hypothalamus, cerebellum and cerebral cortex. Expressed in the soma and processes of neurons in a variety of brain structures, including the developing cerebral cortex, CA1 pyramidal neurons and Purkinje cells. Poorly expressed in medulloblastoma cells compared to cerebellar precursor proliferating progenitor cells (at protein level). Highly expressed in the brain, salivary gland, and testis; moderate expression in kidney and heart. Low expression in the lung, seminal vesicle, ventral prostate, epididymis, liver, and bladder. Very low expression in the coagulation gland and skeleton muscles. Lowest expression seen in spleen. {ECO:0000269|PubMed:12877983, ECO:0000269|PubMed:16629596, ECO:0000269|PubMed:19033661, ECO:0000269|PubMed:22696229, ECO:0000269|PubMed:23326475}. +Q6VGS5 DAPLE_MOUSE Protein Daple (Coiled-coil domain-containing protein 88C) (Dvl-associating protein with a high frequency of leucine residues) 2009 226,535 Alternative sequence (1); Chain (1); Coiled coil (3); Domain (1); Modified residue (6); Motif (1); Mutagenesis (2); Region (1) FUNCTION: Negative regulator of the canonical Wnt signaling pathway, acting downstream of DVL to inhibit CTNNB1/Beta-catenin stabilization (PubMed:14750955). May also activate the JNK signaling pathway (By similarity). {ECO:0000250|UniProtKB:Q9P219, ECO:0000269|PubMed:14750955}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9P219}. SUBUNIT: Homooligomer. Interacts with the PDZ domain of DVL1. {ECO:0000269|PubMed:14750955}. +P50716 DAR12_MOUSE Alpha-defensin-related sequence 12 (CRS4C5) (Cryptdin-related protein 4C-5) (Defensin-related cryptdin-related sequence 12) 91 10,146 Peptide (1); Propeptide (1); Region (1); Repeat (6); Sequence conflict (1); Signal peptide (1) FUNCTION: Apparent precursor of a secreted, cationic, proline- and cysteine-rich peptide that contains Cys-Pro-Xaa repeats. Unlike cryptdin, the proposed mature peptide region lacks the structural motif characteristic of defensins. It may have microbicidal activities (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Paneth cells of the small bowel. +Q80T85 DCAF5_MOUSE DDB1- and CUL4-associated factor 5 (WD repeat-containing protein 22) 946 103,676 Chain (1); Erroneous initiation (1); Modified residue (6); Repeat (6); Sequence conflict (5) Protein modification; protein ubiquitination. FUNCTION: May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex. {ECO:0000250}. SUBUNIT: Interacts with DDB1 and CUL4A. {ECO:0000250}. +Q6PAC3 DCA13_MOUSE DDB1- and CUL4-associated factor 13 (WD repeat and SOF domain-containing protein 1) 445 51,456 Chain (1); Modified residue (1); Repeat (7); Sequence conflict (1) Protein modification; protein ubiquitination. FUNCTION: Possible role in ribosomal RNA processing. May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9NV06}. Note=In the nucleolus, localizes predominantly in the granular component, but also detected in the fibrillar center and dense fibrillar component. {ECO:0000250|UniProtKB:Q9NV06}. SUBUNIT: Interacts with DDB1. Interacts with ESR1 and LATS1. {ECO:0000250|UniProtKB:Q9NV06}. +Q80TR8 DCAF1_MOUSE DDB1- and CUL4-associated factor 1 (Serine/threonine-protein kinase VPRBP) (EC 2.7.11.1) 1506 168,931 Alternative sequence (5); Chain (1); Compositional bias (2); Domain (2); Erroneous initiation (1); Modified residue (10); Motif (2); Region (3); Repeat (5); Sequence conflict (1) Protein modification; protein ubiquitination. FUNCTION: Acts both as a substrate recognition component of E3 ubiquitin-protein ligase complexes and as an atypical serine/threonine-protein kinase, playing key roles in various processes such as cell cycle, telomerase regulation and histone modification. Probable substrate-specific adapter of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex, named CUL4A-RBX1-DDB1-DCAF1/VPRBP complex, which mediates ubiquitination and proteasome-dependent degradation of proteins such as NF2. Involved in the turnover of methylated proteins: recognizes and binds methylated proteins via its chromo domain, leading to ubiquitination of target proteins by the RBX1-DDB1-DCAF1/VPRBP complex. The CUL4A-RBX1-DDB1-DCAF1/VPRBP complex is also involved in B-cell development: DCAF1 is recruited by RAG1 to ubiquitinate proteins, leading to limit error-prone repair during V(D)J recombination. Also part of the EDVP complex, an E3 ligase complex that mediates ubiquitination of proteins such as TERT, leading to TERT degradation and telomerase inhibition. Also acts as an atypical serine/threonine-protein kinase that specifically mediates phosphorylation of 'Thr-120' of histone H2A (H2AT120ph) in a nucleosomal context, thereby repressing transcription. H2AT120ph is present in the regulatory region of many tumor suppresor genes, down-regulates their transcription and is present at high level in a number of tumors. Involved in JNK-mediated apoptosis during cell competition process via its interaction with LLGL1 and LLGL2. {ECO:0000250|UniProtKB:Q9Y4B6, ECO:0000269|PubMed:22157821}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Associated with chromatin in a DDB1-independent and cell cycle-dependent manner: recruited to chromatin as DNA is being replicated and is released from chromatin before mitosis. {ECO:0000250}. SUBUNIT: Component of the DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex, named CUL4A-RBX1-DDB1-DCAF1/VPRBP complex. Interacts with DDB1; the interaction is direct. Also forms a ternary complex with DDA1 and DDB1. Interacts with NF2 (via FERM domain). Component of the EDVP complex, a E3 ligase complex containing DYRK2, EDD/UBR5, DDB1 and DCAF1. Interacts with DYRK2; the interaction is direct. Interacts with RAG1; the interaction is direct. Interacts with LLGL1 and LLGL2. Interacts with histone H3. Interacts with ESR1 and LATS1; probably recruited by LATS1 to promote ESR1 ubiquitination and ubiquitin-mediated proteasomal degradation. {ECO:0000250|UniProtKB:Q9Y4B6}. DOMAIN: The protein kinase-like region mediates the threonine-protein kinase activity. {ECO:0000250}.; DOMAIN: The DWD boxes are required for interaction with DDB1. {ECO:0000250}.; DOMAIN: The chromo domain with a restricted pocket directly recognizes monomethylated substrates. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:11223251}. +D3Z6H8 DCAM2_MOUSE S-adenosylmethionine decarboxylase proenzyme 2 (AdoMetDC 2) (SAMDC 2) (EC 4.1.1.50) [Cleaved into: S-adenosylmethionine decarboxylase 2 alpha chain; S-adenosylmethionine decarboxylase 2 beta chain] 334 38,295 Active site (6); Binding site (4); Chain (2); Modified residue (2); Sequence conflict (3); Site (1) Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1. FUNCTION: Essential for biosynthesis of the polyamines spermidine and spermine. Promotes maintenance and self-renewal of embryonic stem cells, by maintaining spermine levels. {ECO:0000250|UniProtKB:P0DMN7}. PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain. {ECO:0000250|UniProtKB:P17707, ECO:0000269|PubMed:7890685, ECO:0000269|PubMed:9620866}. SUBUNIT: Heterotetramer of two alpha and two beta chains. {ECO:0000250}. +Q80Y98 DDHD2_MOUSE Phospholipase DDHD2 (EC 3.1.1.-) (DDHD domain-containing protein 2) (SAM, WWE and DDHD domain-containing protein 1) 699 79,577 Active site (1); Alternative sequence (4); Chain (1); Domain (3); Erroneous initiation (2); Frameshift (1); Modified residue (1); Sequence conflict (2) FUNCTION: Phospholipase that hydrolyzes preferentially phosphatidic acid, including 1,2-dioleoyl-sn-phosphatidic acid, and phosphatidylethanolamine. Specifically binds to phosphatidylinositol 3-phosphate (PI(3)P), phosphatidylinositol 4-phosphate (PI(4)P), phosphatidylinositol 5-phosphate (PI(5)P) and possibly phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2). May be involved in the maintenance of the endoplasmic reticulum and/or Golgi structures. May regulate the transport between Golgi apparatus and plasma membrane (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250}. Golgi apparatus, cis-Golgi network {ECO:0000250}. Note=Cycles between the Golgi apparatus and the cytosol. DDHD2 recruitment to the Golgi/endoplasmic reticulum-Golgi intermediate compartment (ERGIC) is regulated by the levels of phosphoinositides, including PI(4)P (By similarity). {ECO:0000250}. SUBUNIT: Forms homooligomers and, to a much smaller extent, heterooligomers with DDHD1. {ECO:0000250}. DOMAIN: SAM and DDHD domains together are required for phospholipid binding. {ECO:0000250}. +P35639 DDIT3_MOUSE DNA damage-inducible transcript 3 protein (DDIT-3) (C/EBP zeta) (C/EBP-homologous protein) (CHOP) (C/EBP-homologous protein 10) (CHOP-10) (CCAAT/enhancer-binding protein homologous protein) (Growth arrest and DNA-damage-inducible protein GADD153) 168 19,189 Chain (1); Compositional bias (1); Domain (1); Modified residue (6); Mutagenesis (4); Region (4); Sequence conflict (1) FUNCTION: Multifunctional transcription factor in ER stress response. Plays an essential role in the response to a wide variety of cell stresses and induces cell cycle arrest and apoptosis in response to ER stress. Plays a dual role both as an inhibitor of CCAAT/enhancer-binding protein (C/EBP) function and as an activator of other genes. Acts as a dominant-negative regulator of C/EBP-induced transcription: dimerizes with members of the C/EBP family, impairs their association with C/EBP binding sites in the promoter regions, and inhibits the expression of C/EBP regulated genes. Positively regulates the transcription of TRIB3, IL6, IL8, IL23, TNFRSF10B/DR5, PPP1R15A/GADD34, BBC3/PUMA, BCL2L11/BIM and ERO1L. Negatively regulates; expression of BCL2 and MYOD1, ATF4-dependent transcriptional activation of asparagine synthetase (ASNS), CEBPA-dependent transcriptional activation of hepcidin (HAMP) and CEBPB-mediated expression of peroxisome proliferator-activated receptor gamma (PPARG). Inhibits the canonical Wnt signaling pathway by binding to TCF7L2/TCF4, impairing its DNA-binding properties and repressing its transcriptional activity. Plays a regulatory role in the inflammatory response through the induction of caspase-11 (CASP4/CASP11) which induces the activation of caspase-1 (CASP1) and both these caspases increase the activation of pro-IL1B to mature IL1B which is involved in the inflammatory response. Acts as a major regulator of postnatal neovascularization through regulation of endothelial nitric oxide synthase (NOS3)-related signaling. {ECO:0000269|PubMed:12706815, ECO:0000269|PubMed:14684614, ECO:0000269|PubMed:1547942, ECO:0000269|PubMed:15601821, ECO:0000269|PubMed:15775988, ECO:0000269|PubMed:16670335, ECO:0000269|PubMed:19752026, ECO:0000269|PubMed:19919955, ECO:0000269|PubMed:21159964, ECO:0000269|PubMed:22242125, ECO:0000269|PubMed:22265908}. PTM: Ubiquitinated, leading to its degradation by the proteasome. {ECO:0000250}.; PTM: Phosphorylation at serine residues by MAPK14 enhances its transcriptional activation activity while phosphorylation at serine residues by CK2 inhibits its transcriptional activation activity. {ECO:0000269|PubMed:12876286, ECO:0000269|PubMed:8650547}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Present in the cytoplasm under non-stressed conditions and ER stress leads to its nuclear accumulation. SUBUNIT: Heterodimer. Interacts with TCF7L2/TCF4, EP300/P300, HDAC5 and HDAC6. Interacts with TRIB3 which blocks its association with EP300/P300. Interacts with FOXO3, CEBPB and ATF4 (By similarity). Interacts with HDAC1. {ECO:0000250, ECO:0000269|PubMed:22242125}. DOMAIN: The N-terminal region is necessary for its proteasomal degradation, transcriptional activity and interaction with EP300/P300. {ECO:0000250}. +Q8K363 DDX18_MOUSE ATP-dependent RNA helicase DDX18 (EC 3.6.4.13) (DEAD box protein 18) 660 74,181 Chain (1); Domain (2); Motif (2); Nucleotide binding (1); Sequence conflict (3) FUNCTION: Probable RNA-dependent helicase. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9NVP1}. Chromosome {ECO:0000250|UniProtKB:Q9NVP1}. SUBUNIT: Interacts with NOL8; the interaction is RNA-dependent. {ECO:0000250}. +Q8R2I6 DEFB9_MOUSE Beta-defensin 9 (BD-9) (mBD-9) (Defensin, beta 9) 67 7,682 Chain (1); Disulfide bond (3); Signal peptide (1) FUNCTION: Has antibacterial activity. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. TISSUE SPECIFICITY: Weakly expressed in adult and neonatal brain. {ECO:0000269|PubMed:12644567}. +Q8C4S8 DEN2A_MOUSE DENN domain-containing protein 2A 1000 113,094 Chain (1); Compositional bias (1); Domain (3); Erroneous initiation (1); Modified residue (1); Sequence conflict (6) FUNCTION: Guanine nucleotide exchange factor (GEF) which may activate RAB9A and RAB9B. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. May play a role in late endosomes back to trans-Golgi network/TGN transport (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Note=Associated with actin filaments. {ECO:0000250}. +Q6P9P8 DEN2C_MOUSE DENN domain-containing protein 2C 914 103,937 Alternative sequence (2); Chain (1); Domain (3); Modified residue (1); Sequence conflict (1) FUNCTION: Guanine nucleotide exchange factor (GEF) which may activate RAB9A and RAB9B. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. +Q6PAL8 DEN5A_MOUSE DENN domain-containing protein 5A (Rab6-interacting protein 1) (Rab6IP1) 1287 146,653 Beta strand (9); Chain (1); Compositional bias (2); Domain (6); Helix (9); Modified residue (5); Mutagenesis (3); Sequence conflict (5); Turn (3) FUNCTION: Guanine nucleotide exchange factor (GEF) which may activate RAB6A and RAB39A and/or RAB39B. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form (By similarity). Involved in the negative regulation of neurite outgrowth (By similarity). {ECO:0000250|UniProtKB:G3V7Q0, ECO:0000250|UniProtKB:Q6IQ26}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:19141279, ECO:0000269|PubMed:22558185}. SUBUNIT: Interacts with RAB6A bound to GTP. {ECO:0000269|PubMed:19141279, ECO:0000269|PubMed:7782346}. +Q8BH65 DEN6A_MOUSE Protein DENND6A (DENN domain-containing protein 6A) 605 68,967 Alternative sequence (4); Chain (1); Domain (3); Erroneous initiation (1); Modified residue (2) FUNCTION: Guanine nucleotide exchange factor (GEF) for RAB14. Component of an endocytic recycling pathway that is required for the control of ADAM10 transport, shedding of N-cadherin/CDH2 by ADAM9 or ADAM10 and regulation of cell-cell junctions. Required for RAB14 recruitment to recycling endosomes (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Recycling endosome {ECO:0000250}. Cytoplasm {ECO:0000250}. +Q8BNI4 DERL2_MOUSE Derlin-2 (Degradation in endoplasmic reticulum protein 2) (Der1-like protein 2) (F-LANa) 239 27,640 Alternative sequence (1); Chain (1); Sequence conflict (1); Topological domain (5); Transmembrane (4) TRANSMEM 58 78 Helical; Name=1. {ECO:0000255}.; TRANSMEM 97 117 Helical; Name=2. {ECO:0000255}.; TRANSMEM 151 171 Helical; Name=3. {ECO:0000255}.; TRANSMEM 173 193 Helical; Name=4. {ECO:0000255}. TOPO_DOM 1 57 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 79 96 Lumenal. {ECO:0000255}.; TOPO_DOM 118 150 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 172 172 Lumenal. {ECO:0000255}.; TOPO_DOM 194 239 Cytoplasmic. {ECO:0000255}. FUNCTION: Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal glycoproteins, but not that of misfolded nonglycoproteins. May act by forming a channel that allows the retrotranslocation of misfolded glycoproteins into the cytosol where they are ubiquitinated and degraded by the proteasome. May mediate the interaction between VCP and misfolded glycoproteins. May also be involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for proteasomal degradation. {ECO:0000250|UniProtKB:Q9GZP9}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9GZP9}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9GZP9}. SUBUNIT: Forms homo- and heterooligomers with DERL3 and, to a lesser extent, with DERL1 (By similarity). Interacts with the SEL1L/SYVN1 and VCP/SELENOS protein complexes (PubMed:22016385). Mediates association between VCP and EDEM1, as well as that between VCP and the misfolded glycoproteins (By similarity). Interacts with OS9 (By similarity). Interacts with SELENOK and SELENOS (PubMed:22016385). Interacts with the signal recognition particle/SRP and the SRP receptor; in the process of endoplasmic reticulum stress-induced pre-emptive quality control (By similarity). {ECO:0000250|UniProtKB:Q9GZP9, ECO:0000269|PubMed:22016385}. TISSUE SPECIFICITY: Widely expressed, with lowest levels in brain and heart. {ECO:0000269|PubMed:11500051, ECO:0000269|PubMed:16186509}. +P51656 DHB1_MOUSE Estradiol 17-beta-dehydrogenase 1 (EC 1.1.1.62) (17-beta-hydroxysteroid dehydrogenase type 1) (17-beta-HSD 1) 344 36,785 Active site (1); Binding site (1); Chain (1); Nucleotide binding (1) Steroid biosynthesis; estrogen biosynthesis. FUNCTION: Favors the reduction of estrogens and androgens. Uses preferentially NADH. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Homodimer. {ECO:0000250}. +Q99KU1 DHDDS_MOUSE Dehydrodolichyl diphosphate synthase complex subunit Dhdds (EC 2.5.1.87) (Cis-isoprenyltransferase) (CIT) (Cis-IPTase) 333 38,509 Alternative sequence (1); Chain (1); Sequence conflict (1) Protein modification; protein glycosylation. Lipid metabolism. FUNCTION: With NUS1, forms the dehydrodolichyl diphosphate synthase (DDS) complex, an essential component of the dolichol monophosphate (Dol-P) biosynthetic machinery. Both subunits contribute to enzymatic activity, i.e. condensation of multiple copies of isopentenyl pyrophosphate (IPP) to farnesyl pyrophosphate (FPP) to produce dehydrodolichyl diphosphate (Dedol-PP), a precursor of dolichol phosphate which is utilized as a sugar carrier in protein glycosylation in the endoplasmic reticulum (ER). Regulates the glycosylation and stability of nascent NPC2, thereby promoting trafficking of LDL-derived cholesterol. {ECO:0000250|UniProtKB:Q86SQ9}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q86SQ9}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q86SQ9}. Note=colocalizes with calnexin. {ECO:0000250|UniProtKB:Q86SQ9}. SUBUNIT: Forms an active dehydrodolichyl diphosphate synthase complex with NUS1. Interacts with NPC2. {ECO:0000250|UniProtKB:Q86SQ9}. +P51660 DHB4_MOUSE Peroxisomal multifunctional enzyme type 2 (MFE-2) (17-beta-hydroxysteroid dehydrogenase 4) (17-beta-HSD 4) (D-bifunctional protein) (DBP) (Multifunctional protein 2) (MPF-2) [Cleaved into: (3R)-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.n12); Enoyl-CoA hydratase 2 (EC 4.2.1.107) (EC 4.2.1.119) (3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholest-24-enoyl-CoA hydratase)] 735 79,482 Active site (1); Binding site (9); Chain (3); Domain (2); Modified residue (18); Motif (1); Nucleotide binding (4); Region (4); Sequence conflict (2) Lipid metabolism; fatty acid beta-oxidation. FUNCTION: Bifunctional enzyme acting on the peroxisomal beta-oxidation pathway for fatty acids. Catalyzes the formation of 3-ketoacyl-CoA intermediates from both straight-chain and 2-methyl-branched-chain fatty acids (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Present in many tissues with highest concentrations in liver and kidney. +Q9DBB8 DHDH_MOUSE Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase (EC 1.3.1.20) (D-xylose 1-dehydrogenase) (D-xylose-NADP dehydrogenase) (EC 1.1.1.179) (Dimeric dihydrodiol dehydrogenase) 333 36,301 Chain (1); Sequence conflict (1); Site (5) SUBUNIT: Homodimer. {ECO:0000250}. +P51661 DHI2_MOUSE Corticosteroid 11-beta-dehydrogenase isozyme 2 (EC 1.1.1.-) (11-beta-hydroxysteroid dehydrogenase type 2) (11-DH2) (11-beta-HSD2) (NAD-dependent 11-beta-hydroxysteroid dehydrogenase) 386 42,187 Active site (1); Binding site (1); Chain (1); Frameshift (1); Nucleotide binding (1); Sequence conflict (14) FUNCTION: Catalyzes the conversion of cortisol to the inactive metabolite cortisone. Modulates intracellular glucocorticoid levels, thus protecting the nonselective mineralocorticoid receptor from occupation by glucocorticoids. SUBCELLULAR LOCATION: Microsome. Endoplasmic reticulum {ECO:0000305}. SUBUNIT: Interacts with ligand-free cytoplasmic NR3C2. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in kidney. Also found in colon and small intestine. Not expressed in the adrenal gland. +Q9D1B8 DCD2C_MOUSE Doublecortin domain-containing protein 2C 347 39,355 Alternative sequence (1); Chain (1); Domain (2) SUBCELLULAR LOCATION: Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:A8MYV0}. Cytoplasm {ECO:0000250|UniProtKB:A8MYV0}. Note=Detected along the length of the sperm flagellum and in the cytoplasm of the germ cells. {ECO:0000250|UniProtKB:A8MYV0}. +O88487 DC1I2_MOUSE Cytoplasmic dynein 1 intermediate chain 2 (Cytoplasmic dynein intermediate chain 2) (Dynein intermediate chain 2, cytosolic) (DH IC-2) 612 68,394 Chain (1); Initiator methionine (1); Modified residue (7); Repeat (7) FUNCTION: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. The intermediate chains mediate the binding of dynein to dynactin via its 150 kDa component (p150-glued) DCNT1. Involved in membrane-transport, such as Golgi apparatus, late endosomes and lysosomes (By similarity). {ECO:0000250}. PTM: The phosphorylation status of Ser-84 appears to be involved in dynactin-dependent target binding. {ECO:0000250|UniProtKB:Q62871}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:28619825}. Cytoplasm {ECO:0000269|PubMed:28619825}. Note=Detected in the cytoplasm of pachytene spermatocytes. Localizes to the manchette in elongating spermatids. {ECO:0000269|PubMed:28619825}. SUBUNIT: Homodimer (By similarity). The cytoplasmic dynein 1 complex consists of two catalytic heavy chains (HCs) and a number of non-catalytic subunits presented by intermediate chains (ICs), light intermediate chains (LICs) and light chains (LCs); the composition seems to vary in respect to the IC, LIC and LC composition. The heavy chain homodimer serves as a scaffold for the probable homodimeric assembly of the respective non-catalytic subunits. The ICs and LICs bind directly to the HC dimer and the LCs assemble on the IC dimer. Interacts with DYNLT1 and DYNLT3. Interacts with DCNT1 (By similarity). Interacts with BICD2 (PubMed:22956769). Interacts with SPEF2 (PubMed:28619825). {ECO:0000250|UniProtKB:Q62871, ECO:0000269|PubMed:22956769, ECO:0000269|PubMed:28619825}. +Q9JIC3 DCR1A_MOUSE DNA cross-link repair 1A protein (SNM1 homolog A) 1026 113,567 Chain (1); Cross-link (4); Modified residue (2); Region (2); Sequence caution (1); Sequence conflict (16) FUNCTION: May be required for DNA interstrand cross-link repair. Also required for checkpoint mediated cell cycle arrest in early prophase in response to mitotic spindle poisons. {ECO:0000269|PubMed:10848582, ECO:0000269|PubMed:15542852}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=In some cells it may be found in typically 1 or 2 discrete nuclear aggregates of unknown function which also contain TP53BP1. Also found in multiple discrete nuclear foci which increase in number following treatment with ionizing radiation or interstrand cross-linking agents. These foci overlap with those formed by the MRN complex (composed of MRE11, RAD50 and NBN) and BRCA1 (By similarity). {ECO:0000250}. SUBUNIT: Binds constitutively to TP53BP1. Binds CDC27, which is itself a component of the anaphase promoting complex (APC). Binds PIAS1 (By similarity). {ECO:0000250}. +Q7TNJ0 DCSTP_MOUSE Dendritic cell-specific transmembrane protein (DC-STAMP) (mDC-STAMP) (Dendrocyte-expressed seven transmembrane protein) (Transmembrane 7 superfamily member 4) 470 53,876 Alternative sequence (3); Chain (1); Sequence conflict (2); Topological domain (7); Transmembrane (6) TRANSMEM 34 54 Helical. {ECO:0000255}.; TRANSMEM 56 76 Helical. {ECO:0000255}.; TRANSMEM 98 118 Helical. {ECO:0000255}.; TRANSMEM 210 230 Helical. {ECO:0000255}.; TRANSMEM 293 313 Helical. {ECO:0000255}.; TRANSMEM 377 397 Helical. {ECO:0000255}. TOPO_DOM 1 33 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 55 55 Extracellular. {ECO:0000255}.; TOPO_DOM 77 97 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 119 209 Extracellular. {ECO:0000255}.; TOPO_DOM 231 292 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 314 376 Extracellular. {ECO:0000255}.; TOPO_DOM 398 470 Cytoplasmic. {ECO:0000255}. FUNCTION: Probable cell surface receptor that plays several roles in cellular fusion, cell differentiation, bone and immune homeostasis. Plays a role in TNFSF11-mediated osteoclastogenesis. Cooperates with OCSTAMP in modulating cell-cell fusion in both osteoclasts and foreign body giant cells (FBGCs). Participates in osteoclast bone resorption. Involved in inducing the expression of tartrate-resistant acid phosphatase in osteoclast precursors. Plays a role in haematopoietic stem cell differentiation of bone marrow cells toward the myeloid lineage. Inhibits the development of neutrophilic granulocytes. Plays also a role in the regulation of dendritic cell (DC) antigen presentation activity by controlling phagocytic activity. Involved in the maintenance of immune self-tolerance and avoidance of autoimmune reactions. {ECO:0000269|PubMed:15452179, ECO:0000269|PubMed:16061724, ECO:0000269|PubMed:16937266, ECO:0000269|PubMed:17164993, ECO:0000269|PubMed:17713547, ECO:0000269|PubMed:18653699, ECO:0000269|PubMed:18952287, ECO:0000269|PubMed:20039274, ECO:0000269|PubMed:22337159}. PTM: Glycosylated. {ECO:0000269|PubMed:15601667}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Endoplasmic reticulum membrane; Multi-pass membrane protein. Endoplasmic reticulum-Golgi intermediate compartment membrane; Multi-pass membrane protein. Endosome. Note=Localized to the cell surface in osteoclasts and undifferentiated monocytes. Intracellular internalized DCSTAMP is detected in a fraction of RANKL-induced osteoclast precursor. Colocalizes with OS9 in the endoplasmic reticulum (ER) of immature dendritic cell (DC). Translocates from the endoplasmic reticulum to the intermediate/Golgi compartment upon maturation of DC in a OS9-dependent manner. Colocalizes with LAMP1 in endosomes. SUBUNIT: Interacts with CREB3 (By similarity). Monomer. Homodimer. Isoform 1 interacts (via the C-terminus cytoplasmic tail) with OS9 isoform 1 (via the C-terminus tail); the interaction induces DCSTAMP redistribution to the endoplasmic reticulum-Golgi intermediate compartment. Isoform 1 interacts (via the C-terminus cytoplasmic tail) with OS9 isoform 2 (via the C-terminus tail). {ECO:0000250, ECO:0000269|PubMed:18952287}. DOMAIN: Several domains are necessary for interacting with OS9. The region in the cytoplasmic tail that is necessary for interaction with OS9, is also required for its transport. TISSUE SPECIFICITY: Expressed in macrophages and bone marrow dendritic cells (BM-DC). Weakly expressed in the spleen and lymph node. Highly expressed in multi-nuclear osteoclasts compared to mono-nuclear macrophages. Expressed in foreign body giant cells (FBGCs). Isoform 1 and isoform 2 are expressed in osteoclasts. {ECO:0000269|PubMed:15601667, ECO:0000269|PubMed:16061724, ECO:0000269|PubMed:22337159}. +Q8C7W7 DCR1B_MOUSE 5' exonuclease Apollo (EC 3.1.-.-) (DNA cross-link repair 1B protein) (SNM1 homolog B) 541 61,069 Alternative sequence (3); Chain (1); Cross-link (1); Erroneous initiation (2); Frameshift (1); Motif (1); Mutagenesis (4); Sequence conflict (5) FUNCTION: 5'-3' exonuclease that plays a central role in telomere maintenance and protection during S-phase. Participates in the protection of telomeres against non-homologous end-joining (NHEJ)-mediated repair, thereby ensuring that telomeres do not fuse. Plays a key role in telomeric loop (T loop) formation by being recruited by TERF2 at the leading end telomeres and by processing leading-end telomeres immediately after their replication via its exonuclease activity: generates 3' single-stranded overhang at the leading end telomeres avoiding blunt leading-end telomeres that are vulnerable to end-joining reactions and expose the telomere end in a manner that activates the DNA repair pathways. Together with TERF2, required to protect telomeres from replicative damage during replication by controlling the amount of DNA topoisomerase (TOP1, TOP2A and TOP2B) needed for telomere replication during fork passage and prevent aberrant telomere topology. Also involved in response to DNA damage: plays a role in response to DNA interstrand cross-links (ICLs) by facilitating double-strand break formation. In case of spindle stress, involved in prophase checkpoint. {ECO:0000269|PubMed:20551906, ECO:0000269|PubMed:20619712}. PTM: Ubiquitinated, leading to its degradation. Interaction with TERF2 protects it from ubiquitination (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Chromosome, telomere {ECO:0000269|PubMed:20551906, ECO:0000269|PubMed:20619712}. Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Note=Mainly localizes to telomeres, recruited via its interaction with TERF2. During mitosis, localizes to the centrosome. SUBUNIT: Interacts with MUS81, MRE11 and FANCD2. Interacts with HSPA2, HSPA8 and HSPA14. Interacts with SPAG5 (By similarity). Interacts with TERF2; the interaction is direct. {ECO:0000250, ECO:0000269|PubMed:20619712}. DOMAIN: The TBM domain mediates interaction with TERF2. {ECO:0000250}. +Q9WUB4 DCTN6_MOUSE Dynactin subunit 6 (Dynactin subunit p27) (Protein WS-3) 190 20,670 Chain (1); Modified residue (1); Sequence conflict (2) PTM: Phosphorylation at Thr-186 by CDK1 during mitotic prometaphase creates a binding site for PLK1 that facilitates its recruitment to kinetochores. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. SUBUNIT: Member of the pointed-end complex of the dynactin shoulder complex which contains DCTN4, DCTN5 and DCTN6 subunits and ACTR10. Within the complex DCTN6 forms a heterodimer with DCTN5. Interacts with PLK1 (By similarity). {ECO:0000250}. +O88533 DDC_MOUSE Aromatic-L-amino-acid decarboxylase (AADC) (EC 4.1.1.28) (DOPA decarboxylase) (DDC) 480 53,874 Binding site (6); Chain (1); Modified residue (2); Region (1); Repeat (2) Catecholamine biosynthesis; dopamine biosynthesis; dopamine from L-tyrosine: step 2/2. FUNCTION: Catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine (DOPA) to dopamine, L-5-hydroxytryptophan to serotonin and L-tryptophan to tryptamine. SUBUNIT: Homodimer. {ECO:0000250}. +Q9CWS0 DDAH1_MOUSE N(G),N(G)-dimethylarginine dimethylaminohydrolase 1 (DDAH-1) (Dimethylarginine dimethylaminohydrolase 1) (EC 3.5.3.18) (DDAHI) (Dimethylargininase-1) 285 31,381 Active site (2); Binding site (7); Chain (1); Initiator methionine (1); Metal binding (1); Modified residue (4) FUNCTION: Hydrolyzes N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-monomethyl-L-arginine (MMA) which act as inhibitors of NOS. Has therefore a role in the regulation of nitric oxide generation. {ECO:0000269|PubMed:17273169}. SUBUNIT: Monomer. {ECO:0000250}. TISSUE SPECIFICITY: Detected in skeletal muscle, lung, heart and brain (at protein level). Detected in liver, kidney and lung. {ECO:0000269|PubMed:17273169}. +Q62371 DDR2_MOUSE Discoidin domain-containing receptor 2 (Discoidin domain receptor 2) (EC 2.7.10.1) (CD167 antigen-like family member B) (Neurotrophic tyrosine kinase, receptor-related 3) (Receptor protein-tyrosine kinase TKT) (Tyrosine-protein kinase TYRO10) (CD antigen CD167b) 854 96,482 Active site (1); Binding site (1); Chain (1); Disulfide bond (2); Domain (2); Erroneous initiation (1); Glycosylation (5); Modified residue (4); Mutagenesis (2); Nucleotide binding (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 400 421 Helical. {ECO:0000255}. TOPO_DOM 22 399 Extracellular. {ECO:0000255}.; TOPO_DOM 422 854 Cytoplasmic. {ECO:0000255}. FUNCTION: Tyrosine kinase that functions as cell surface receptor for fibrillar collagen and regulates cell differentiation, remodeling of the extracellular matrix, cell migration and cell proliferation. Required for normal bone development. Regulates osteoblast differentiation and chondrocyte maturation via a signaling pathway that involves MAP kinases and leads to the activation of the transcription factor RUNX2. Regulates remodeling of the extracellular matrix by up-regulation of the collagenases MMP1, MMP2 and MMP13, and thereby facilitates cell migration and tumor cell invasion. Promotes fibroblast migration and proliferation, and thereby contributes to cutaneous wound healing. {ECO:0000269|PubMed:11375938, ECO:0000269|PubMed:11723120, ECO:0000269|PubMed:11884411, ECO:0000269|PubMed:15509586, ECO:0000269|PubMed:19681157}. PTM: N-glycosylated. {ECO:0000250}.; PTM: Tyrosine phosphorylated in response to collagen binding. Phosphorylated by SRC; this is required for activation and subsequent autophosphorylation on additional tyrosine residues (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SUBUNIT: Binds hydroxyproline-rich sequence motifs in fibrillar, glycosylated collagen, such as the GQOGVMGFO motif, where O stands for hydroxyproline. Interacts with SRC. Interacts (tyrosine phosphorylated) with SHC1. {ECO:0000269|PubMed:11884411}. TISSUE SPECIFICITY: Widely expressed. Detected in lung, ovary, skin and in testis Leydig cells (at protein level). Widely expressed. Detected at high levels in heart, lung, skeletal muscle, central nervous system (CNS) and kidney, and at lower levels in brain and testis. Detected in chondrocytes in tibia growth plates of young mice. {ECO:0000269|PubMed:11375938, ECO:0000269|PubMed:18483174, ECO:0000269|PubMed:19681157}. DISEASE: Note=Defects in Ddr2 are the cause of the smallie (sli) phenotype. Smallie mice show distinct dwarfing, with reduced body mass and reduced bone mineral content. Mice also have mild craniofacial deformities, such as protuberant eyes and snub noses. Smallie mice have a reduced life span, with about half of them dying within 6 months. Matings between male and female smallie mice do not yield any offspring. The levels of circulating steroid hormones remain at a level corresponding to prepubertal wild-type mice. Adult testes exhibit much reduced numbers of spermatids with atrophy of spermatogonia, Sertoli and Leydig cells. Ovaries show an absence of corpora lutea. +Q4FZF3 DDX49_MOUSE Probable ATP-dependent RNA helicase DDX49 (EC 3.6.4.13) (DEAD box protein 49) 480 54,094 Chain (1); Domain (2); Motif (2); Nucleotide binding (1) +Q8VHZ5 DDT4L_MOUSE DNA damage-inducible transcript 4-like protein (HIF-1 responsive protein RTP801-like) (Soleus muscle atrophied after hindlimb suspension protein 1) 193 21,581 Chain (1); Sequence conflict (3) FUNCTION: Inhibits cell growth by regulating the TOR signaling pathway upstream of the TSC1-TSC2 complex and downstream of AKT1. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +Q921N6 DDX27_MOUSE Probable ATP-dependent RNA helicase DDX27 (EC 3.6.4.13) (DEAD box protein 27) 760 85,939 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (2); Erroneous initiation (1); Modified residue (5); Motif (4); Nucleotide binding (1); Sequence conflict (1) FUNCTION: Probable ATP-dependent RNA helicase. Component of the nucleolar ribosomal RNA (rRNA) processing machinery that regulates 3' end formation of ribosomal 47S rRNA. {ECO:0000250|UniProtKB:Q96GQ7}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q96GQ7}. Chromosome {ECO:0000250|UniProtKB:Q96GQ7}. Note=Associates with 60S and 90S pre-ribosomal particles. {ECO:0000250|UniProtKB:Q96GQ7}. SUBUNIT: Associates with PeBoW complex, composed of BOP1, PES1 and WDR12. Interacts directly with BOP1 and PES1. {ECO:0000250|UniProtKB:Q96GQ7}. DOMAIN: The C-terminal domain regulates nucleolar localization. {ECO:0000250|UniProtKB:Q96GQ7}. +Q80Y44 DDX10_MOUSE Probable ATP-dependent RNA helicase DDX10 (EC 3.6.4.13) (DEAD box protein 10) 875 100,739 Binding site (1); Chain (1); Cross-link (1); Domain (2); Erroneous initiation (1); Modified residue (6); Motif (2); Nucleotide binding (2) FUNCTION: Putative ATP-dependent RNA helicase. {ECO:0000250}. DOMAIN: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis. +Q9CQ62 DECR_MOUSE 2,4-dienoyl-CoA reductase, mitochondrial (EC 1.3.1.34) (2,4-dienoyl-CoA reductase [NADPH]) (4-enoyl-CoA reductase [NADPH]) 335 36,214 Active site (1); Binding site (7); Chain (1); Modified residue (17); Nucleotide binding (2); Sequence conflict (1); Transit peptide (1) FUNCTION: Auxiliary enzyme of beta-oxidation. It participates in the metabolism of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions. Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. SUBUNIT: Homotetramer. {ECO:0000250}. +Q501J6 DDX17_MOUSE Probable ATP-dependent RNA helicase DDX17 (EC 3.6.4.13) (DEAD box protein 17) 650 72,399 Alternative sequence (2); Chain (1); Cross-link (4); Domain (2); Modified residue (5); Motif (2); Nucleotide binding (1); Region (2); Sequence conflict (2) FUNCTION: As an RNA helicase, unwinds RNA and alters RNA structures through ATP binding and hydrolysis. Involved in multiple cellular processes, including pre-mRNA splicing, alternative splicing, ribosomal RNA processing and miRNA processing, as well as transcription regulation. Regulates the alternative splicing of exons exhibiting specific features. This function requires the RNA helicase activity. Affects NFAT5 and histone macro-H2A.1/H2AFY alternative splicing in a CDK9-dependent manner. Affects splicing of mediators of steroid hormone signaling pathway, including kinases that phosphorylates ESR1 and transcriptional regulators. By acting splicing of regulatory factors, participates in ESR1 and AR stabilization. Promotes the inclusion of specific AC-rich alternative exons in CD44 transcripts. In myoblasts and epithelial cells, cooperates with HNRNPH1 to control the splicing of specific subsets of exons. In addition to binding mature mRNAs, also interacts with certain pri-microRNAs, including MIR132/miR-132, and stabilizes the primary transcript. Also participates in the MIR132 processing, resulting in significantly higher levels of mature MIR132 than MIR212 despite the fact that both are cotranscribed and co-regulated (PubMed:26947125). Binding of pri-microRNAs may occur on the 3' segment flanking the stem loop via the 5'-[ACG]CAUC[ACU]-3' consensus sequence (By similarity). Participates in MYC down-regulation at high cell density through the production of MYC-targeting microRNAs. Along with DDX5, may be involved in the processing of the 32S intermediate into the mature 28S rRNA. Promoter-specific transcription regulator, functioning as a coactivator or corepressor depending on the context of the promoter and the transcriptional complex in which it exists. Enhances NFAT5 transcriptional activity. Synergizes with TP53 in the activation of the MDM2 promoter; this activity requires acetylation on lysine residues. May also coactivate MDM2 transcription through a TP53-independent pathway. Coactivates MMP7 transcription. Along with CTNNB1, coactivates MYC, JUN, FOSL1 and cyclin D1/CCND1 transcription. Alone or in combination with DDX5 and/or SRA1 non-coding RNA, plays a critical role in promoting the assembly of proteins required for the formation of the transcription initiation complex and chromatin remodeling leading to coactivation of MYOD1-dependent transcription. This helicase-independent activity is required for skeletal muscle cells to properly differentiate into myotubes (PubMed:17011493). During epithelial-to-mesenchymal transition, coregulates SMAD-dependent transcriptional activity, directly controlling key effectors of differentiation, including miRNAs which in turn directly repress its expression. Plays a role in estrogen and testosterone signaling pathway at several levels. Mediates the use of alternative promoters in estrogen-responsive genes and regulates transcription and splicing of a large number of steroid hormone target genes. Contrary to the splicing regulation activity, transcriptional coregulation of the estrogen receptor ESR1 is helicase activity-independent. Plays a role in innate immunity. Specifically restricts bunyavirus infection, including Rift Valley fever virus (RVFV) or La Crosse virus (LACV), but not vesicular stomatitis virus (VSV), in an interferon- and DROSHA-independent manner. Binds to RVFV RNA, likely via structured viral RNA elements (By similarity). Promotes mRNA degradation mediated by the antiviral zinc-finger protein ZC3HAV1, in an ATPase-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q92841, ECO:0000269|PubMed:17011493, ECO:0000269|PubMed:26947125}. PTM: Sumoylation significantly increases stability. It also promotes interaction specifically with HDAC1 (but not HDAC2, nor HDAC3) and strongly stimulates ESR1 and TP53 coactivation. {ECO:0000250|UniProtKB:Q92841}.; PTM: Acetylation at lysine residues stabilizes the protein, stimulates interaction with HDAC1 and HDAC3, but not HDAC2, and represses ESR1 and TP53 coactivation activity. {ECO:0000250|UniProtKB:Q92841}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92841}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q92841}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q92841}. Note=In the course of bunyavirus infection, relocalizes from the nucleus to the cytosol where it binds viral RNA to antagonize replication. {ECO:0000250|UniProtKB:Q92841}. SUBUNIT: Interacts with DDX5 in an RNA-independent manner (By similarity). Interacts with CDK9 transcription elongation complex under basal conditions. Following cell stimulation with poly(I:C), a synthetic double-stranded RNA mimicking viral infection, the interaction with CDK9 is decreased (By similarity). Interacts with ESR1 in an estrogen-independent manner (By similarity). Interacts with HNRNPH1; this interaction is important for the regulation of alternative splicing on G-quadruplex structures (By similarity). At high, but not low, cell density, interacts with DROSHA and DGCR8, the core components of the microprocessor complex involved in the maturation of primary microRNAs (pri-miRNAs) into pre-miRNAs. The interaction with DGCR8 is reduced during mitosis. At low, but not high, cell density, interacts with YAP1 and with its paralog, WWTR1/TAZ. Interactions with DROSHA and YAP1 are mutually exclusive. In vitro, the pre-miRNA processing activity of the DDX17-containing microprocessor complex is weaker than that of the DROSHA/DGCR8 microprocessor complex (By similarity). Interacts with UPF3B (By similarity). Interacts with NFAT5; this interaction leads to DDX17 recruitment to LNC2 and S100A4 promoters and NFAT5-mediated DDX17-enhanced transactivation (By similarity). Interacts with HDAC1, HDAC2 and HDAC3; this interaction with HDAC1 and HDAC3, but not HDAC2, depends upon DDX17 acetylation (By similarity). Interacts with ZC3HAV1 (via N-terminal domain) in an RNA-independent manner. Interacts with EXOSC3/RRP40 and EXOSC5/RRP46; this interaction may be indirect and mediated by ZC3HAV1-binding (By similarity). Interacts with EP300; this interaction leads to acetylation at lysine residues (By similarity). Interacts with CREBBP/CBP and KAT2B/P/CAF (By similarity). Directly interacts with CTNNB1 (By similarity). Interacts with MYOD1 (PubMed:17011493). Interacts with TP53 (By similarity). Interacts with DCP1A in an RNA-independent manner. Interacts with DCP2 in an RNA-dependent manner (By similarity). Interacts with DHX36; this interaction occurs in a RNA-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q92841, ECO:0000269|PubMed:17011493}. +Q8BTM8 FLNA_MOUSE Filamin-A (FLN-A) (Actin-binding protein 280) (ABP-280) (Alpha-filamin) (Endothelial actin-binding protein) (Filamin-1) (Non-muscle filamin) 2647 281,222 Alternative sequence (2); Chain (1); Cross-link (5); Domain (2); Erroneous initiation (2); Frameshift (1); Initiator methionine (1); Modified residue (50); Region (5); Repeat (24); Sequence conflict (4) FUNCTION: Actin binding protein that promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. Anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins (By similarity). Interaction with FLNA may allow neuroblast migration from the ventricular zone into the cortical plate. Tethers cell surface-localized furin, modulates its rate of internalization and directs its intracellular trafficking. Involved in ciliogenesis. Plays a role in cell-cell contacts and adherens junctions during the development of blood vessels, heart and brain organs (PubMed:17172441). Plays a role in platelets morphology through interaction with SYK that regulates ITAM- and ITAM-like-containing receptor signaling, resulting in by platelet cytoskeleton organization maintenance (PubMed:20713593). {ECO:0000250, ECO:0000269|PubMed:17172441, ECO:0000269|PubMed:20713593, ECO:0000269|PubMed:22121117, ECO:0000269|PubMed:9412467}. PTM: Phosphorylation at Ser-2152 is negatively regulated by the autoinhibited conformation of filamin repeats 19-21. Ligand binding induces a conformational switch triggering phosphorylation at Ser-2152 by PKA. {ECO:0000250|UniProtKB:P21333}.; PTM: Polyubiquitination in the CH1 domain by a SCF-like complex containing ASB2 leads to proteasomal degradation. Prior dissociation from actin may be required to expose the target lysines. Ubiquitinated in endothelial cells by RNF213 downstream of the non-canonical Wnt signaling pathway, leading to its degradation by the proteasome. {ECO:0000250|UniProtKB:P21333}. SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. SUBUNIT: Homodimer. Interacts with FCGR1A, FLNB, FURIN, HSPB7, KCND2, INPPL1, MYOT, MYOZ1, PDLIM2, ARHGAP24, PSEN1, PSEN2 and ECSCR. Interacts also with various other binding partners in addition to filamentous actin. Interacts (via N-terminus) with TAF1B. Interacts (via N-terminus) with MIS18BP1 (via N-terminus) (By similarity). Interacts with TMEM67 (via C-terminus) and MKS1 (By similarity). Interacts (via actin-binding domain) with MICALL2 (via calponin-homology (CH) domain). Interacts with RFLNA and RFLNB (PubMed:24436304, PubMed:21709252). Interacts (via filamin repeat 5) with SYK; docks SYK to the plasma membrane. Interacts (via filamin repeats 19 and 21) with DRD3; increased PKA-mediated phosphorylation at Ser-2152. Interacts (via filamin repeat 21) with MAS1, AGTR1 and ADRA1D; increases PKA-mediated phosphorylation of FLNA at Ser-2152. Interacts (via filamin repeats 4, 9, 12, 17, 19, 21, and 23) with GP1BA (high affinity), ITGB7, ITGB2 and FBLIM1 (By similarity). Interacts with CEACAM1 (via cytoplasmic domain); inhibits cell migration and cell scattering by interfering with the interaction between FLNA and RALA (By similarity). Interacts with FOXC1 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P21333, ECO:0000269|PubMed:21709252, ECO:0000269|PubMed:23890175, ECO:0000269|PubMed:24436304, ECO:0000269|PubMed:9412467}. DOMAIN: Comprised of a NH2-terminal actin-binding domain, 24 immunoglobulin-like internally homologous repeats and two hinge regions. Repeat 24 and the second hinge domain are important for dimer formation. Filamin repeat 20 interacts with filamin repeat 21 masking the ligand binding site on filamin repeat 21, resulting in an autoinhibited conformation. The autoinhibition can be relieved by ligands like ITGB7 or FBLIM1. Filamin repeats 19 and 21 can simultaneously engage ligands. {ECO:0000250|UniProtKB:P21333}. TISSUE SPECIFICITY: Widely expressed. Highly expressed in Purkinje cells. +Q91VN6 DDX41_MOUSE Probable ATP-dependent RNA helicase DDX41 (EC 3.6.4.13) (DEAD box protein 41) 622 69,820 Chain (1); Cross-link (2); Domain (2); Modified residue (4); Motif (2); Nucleotide binding (1); Sequence conflict (1); Zinc finger (1) FUNCTION: Probable ATP-dependent RNA helicase. Is required during post-transcriptional gene expression. May be involved in pre-mRNA splicing. {ECO:0000250|UniProtKB:Q9UJV9}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UJV9}. SUBUNIT: Identified in the spliceosome C complex. {ECO:0000250|UniProtKB:Q9UJV9}. +Q9Z1L3 DEDD_MOUSE Death effector domain-containing protein (DEDPro1) 318 36,805 Chain (1); Domain (1); Sequence conflict (2) FUNCTION: A scaffold protein that directs CASP3 to certain substrates and facilitates their ordered degradation during apoptosis. May also play a role in mediating CASP3 cleavage of KRT18. Regulates degradation of intermediate filaments during apoptosis. May play a role in the general transcription machinery in the nucleus and might be an important regulator of the activity of GTF3C3 (By similarity). Inhibits DNA transcription in vitro. {ECO:0000250, ECO:0000269|PubMed:9774341}. PTM: Exists predominantly in a mono- or diubiquitinated form. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Note=Translocated to the nucleus during CD95-mediated apoptosis where it is localized in the nucleoli. Following apoptosis induction, the mono and/or diubiquitination form increases and forms filamentous structures that colocalize with KRT8 and KRT18 intermediate filament network in simple epithelial cells (By similarity). {ECO:0000250}. SUBUNIT: Interacts with CASP8, CASP10, KRT8, KRT18, CASP3 and FADD. Homodimerizes and heterodimerizes with DEDD2 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:9774341}. +Q569Z5 DDX46_MOUSE Probable ATP-dependent RNA helicase DDX46 (EC 3.6.4.13) (DEAD box protein 46) 1032 117,448 Alternative sequence (1); Chain (1); Coiled coil (1); Compositional bias (3); Cross-link (5); Domain (2); Erroneous initiation (2); Erroneous termination (1); Initiator methionine (1); Lipidation (1); Modified residue (10); Motif (2); Nucleotide binding (1) FUNCTION: Plays an essential role in splicing, either prior to, or during A complex formation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}. Nucleus, Cajal body {ECO:0000250}. Membrane {ECO:0000250|UniProtKB:Q7L014}; Lipid-anchor {ECO:0000250|UniProtKB:Q7L014}. Note=Present in Cajal bodies (CBs) and nuclear speckles. {ECO:0000250}. SUBUNIT: Integral component of the 17S U2 snRNP. {ECO:0000250}. +Q9JIK5 DDX21_MOUSE Nucleolar RNA helicase 2 (EC 3.6.4.13) (DEAD box protein 21) (Gu-alpha) (Nucleolar RNA helicase Gu) (Nucleolar RNA helicase II) (RH II/Gu) 851 93,551 Chain (1); Compositional bias (1); Domain (2); Helix (1); Modified residue (16); Motif (2); Nucleotide binding (1); Region (2); Repeat (6); Sequence conflict (2) FUNCTION: RNA helicase that acts as a sensor of the transcriptional status of both RNA polymerase (Pol) I and II: promotes ribosomal RNA (rRNA) processing and transcription from polymerase II (Pol II). Binds various RNAs, such as rRNAs, snoRNAs, 7SK and, at lower extent, mRNAs. In the nucleolus, localizes to rDNA locus, where it directly binds rRNAs and snoRNAs, and promotes rRNA transcription, processing and modification. Required for rRNA 2'-O-methylation, possibly by promoting the recruitment of late-acting snoRNAs SNORD56 and SNORD58 with pre-ribosomal complexes. In the nucleoplasm, binds 7SK RNA and is recruited to the promoters of Pol II-transcribed genes: acts by facilitating the release of P-TEFb from inhibitory 7SK snRNP in a manner that is dependent on its helicase activity, thereby promoting transcription of its target genes. Functions as cofactor for JUN-activated transcription: required for phosphorylation of JUN at 'Ser-77'. Can unwind double-stranded RNA (helicase) and can fold or introduce a secondary structure to a single-stranded RNA (foldase). Involved in rRNA processing. May bind to specific miRNA hairpins (By similarity). Component of a multi-helicase-TICAM1 complex that acts as a cytoplasmic sensor of viral double-stranded RNA (dsRNA) and plays a role in the activation of a cascade of antiviral responses including the induction of proinflammatory cytokines via the adapter molecule TICAM1 (PubMed:21703541). {ECO:0000250|UniProtKB:Q9NR30, ECO:0000269|PubMed:21703541}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9NR30}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9NR30}. Cytoplasm, cytosol {ECO:0000269|PubMed:21703541}. Mitochondrion {ECO:0000303|PubMed:21703541}. Note=Present both in nucleolus and nucleoplasm. Interaction with JUN promotes translocation from the nucleolus to the nucleoplasm. Interaction with WDR46 is required for localization to the nucleolus. Colocalizes in the cytosol with DDX1, DHX36 and TICAM1 (PubMed:21703541). The multi-helicase-TICAM1 complex may translocate to the mitochondria upon poly(I:C) RNA ligand stimulation (PubMed:21703541). {ECO:0000250|UniProtKB:Q9NR30, ECO:0000269|PubMed:21703541}. SUBUNIT: Homodimer; homodimerizes via its N-terminus (PubMed:21703541). Found in a multi-helicase-TICAM1 complex at least composed of DHX36, DDX1, DDX21 and TICAM1; this complex exists in resting cells with or without poly(I:C) RNA ligand stimulation (PubMed:21703541). Interacts (via C-terminus) with TICAM1 (via TIR domain) (PubMed:21703541). Interacts with DHX36 (via C-terminus); this interaction serves as bridges to TICAM1 (PubMed:21703541). Interacts (via C-terminus) with DDX1 (via B30.2/SPRY domain); this interaction serves as bridges to TICAM1 (PubMed:21703541). Component of the B-WICH complex, at least composed of SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21. Interacts with C1QBP. Interacts with JUN. Interacts with WDR46. {ECO:0000250|UniProtKB:Q9NR30, ECO:0000269|PubMed:21703541}. DOMAIN: The helicase and foldase activities reside in two separate domains, the helicase in the N-terminus and the foldase in the C-terminus. {ECO:0000250|UniProtKB:Q9NR30}.; DOMAIN: The 3 X 5 AA repeats seem to be critical for the RNA folding activity. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in liver and testis. Expressed at lower level in brain, lungs, and skeletal muscle. {ECO:0000269|PubMed:10860663}. +Q9WTL0 DEFB3_MOUSE Beta-defensin 3 (BD-3) (mBD-3) (Defensin, beta 3) 63 7,126 Disulfide bond (3); Peptide (1); Propeptide (1); Signal peptide (1) FUNCTION: Antimicrobial activity against Gram-negative bacteria E.coli and P.aeruginosa. {ECO:0000269|PubMed:10377137}. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Highest expression in salivary glands, epididymis, ovary and pancreas and to a lesser extent in lung, liver and brain. Low or no expression in skeletal muscle and tongue. {ECO:0000269|PubMed:10377137, ECO:0000269|PubMed:10922379}. +O09005 DEGS1_MOUSE Sphingolipid delta(4)-desaturase DES1 (EC 1.14.19.17) (Degenerative spermatocyte homolog 1) 323 38,241 Chain (1); Initiator methionine (1); Lipidation (1); Modified residue (1); Motif (3); Sequence conflict (1); Transmembrane (6) TRANSMEM 41 61 Helical. {ECO:0000255}.; TRANSMEM 68 88 Helical. {ECO:0000255}.; TRANSMEM 104 124 Helical. {ECO:0000255}.; TRANSMEM 152 172 Helical. {ECO:0000255}.; TRANSMEM 184 204 Helical. {ECO:0000255}.; TRANSMEM 209 229 Helical. {ECO:0000255}. FUNCTION: Has sphingolipid-delta-4-desaturase activity. Converts D-erythro-sphinganine to D-erythro-sphingosine (E-sphing-4-enine). {ECO:0000269|PubMed:11937514}. PTM: Myristoylation can target the enzyme to the mitochondria leading to an increase in ceramide levels. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:O15121}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O15121}; Multi-pass membrane protein {ECO:0000250}. Membrane {ECO:0000250|UniProtKB:O15121}; Lipid-anchor {ECO:0000250|UniProtKB:O15121}. TISSUE SPECIFICITY: Detected in testis. Detected in pachytene spermatocytes and round spermatids. {ECO:0000269|PubMed:9227906}. +Q80TS7 DEND_MOUSE Dendrin 710 76,407 Chain (1); Coiled coil (1); Erroneous initiation (4); Modified residue (1); Region (4); Sequence conflict (1) FUNCTION: Promotes apoptosis of kidney glomerular podocytes. Podocytes are highly specialized cells essential to the ultrafiltration of blood, resulting in the extraction of urine and the retention of protein. {ECO:0000269|PubMed:17537921}. SUBCELLULAR LOCATION: Cell projection, dendritic spine membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasm. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Perikaryon {ECO:0000250}. Nucleus. Note=Enriched at the cytoplasmic insertion of the slit diaphragm into the foot process of podocytes and associated with polyribosomes in dendrites. {ECO:0000250}. SUBUNIT: Forms a ternary complex with MAGI2 and SH3KBP1; recruits DDN to the cytoplasm (By similarity). Interacts with MAGI1 (By similarity). Interacts with ACTN1 and may interact with WWC1 (By similarity). Interacts with the podocyte slit diaphragm proteins CD2AP, NPHS1 and NPHS2; the interaction with CD2AP and NPHS1 is direct. {ECO:0000250, ECO:0000269|PubMed:17537921}. TISSUE SPECIFICITY: Two forms of 81 kDa and 89 kDa are expressed in brain. The 81 kDa form is the only one found in kidney podocytes. {ECO:0000269|PubMed:17251388, ECO:0000269|PubMed:17537921}. +Q3U564 DCP1B_MOUSE mRNA-decapping enzyme 1B (EC 3.-.-.-) 578 62,720 Alternative sequence (1); Chain (1); Initiator methionine (1); Modified residue (6) FUNCTION: May play a role in the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. May remove the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Binds DCP1A. Part of a complex containing enzymes involved in mRNA decay, including DCP2, LSM1, LSM3 and CNOT6 (By similarity). {ECO:0000250}. +Q8CCA0 DCNL4_MOUSE DCN1-like protein 4 (DCUN1 domain-containing protein 4) (Defective in cullin neddylation protein 1-like protein 4) 292 33,939 Chain (1); Cross-link (1); Domain (1) +Q6P9R1 DDX51_MOUSE ATP-dependent RNA helicase DDX51 (EC 3.6.4.13) (DEAD box protein 51) 639 70,368 Chain (1); Compositional bias (1); Domain (2); Initiator methionine (1); Modified residue (3); Motif (2); Nucleotide binding (1); Sequence conflict (1) FUNCTION: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. DOMAIN: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis. +Q62167 DDX3X_MOUSE ATP-dependent RNA helicase DDX3X (EC 3.6.4.13) (D1Pas1-related sequence 2) (DEAD box RNA helicase DEAD3) (mDEAD3) (DEAD box protein 3, X-chromosomal) (Embryonic RNA helicase) 662 73,101 Chain (1); Compositional bias (4); Cross-link (1); Domain (2); Initiator methionine (1); Modified residue (17); Motif (2); Nucleotide binding (2); Region (6) FUNCTION: Multifunctional ATP-dependent RNA helicase. The ATPase activity can be stimulated by various ribo- and deoxynucleic acids indicative for a relaxed substrate specificity. In vitro can unwind partially double-stranded DNA with a preference for 5'-single-stranded DNA overhangs. Is involved in several steps of gene expression, such as transcription, mRNA maturation, mRNA export and translation. However, the exact mechanisms are not known and some functions may be specific for a subset of mRNAs. Involved in transcriptional regulation. Can enhance transcription from the CDKN1A/WAF1 promoter in a SP1-dependent manner. Found associated with the E-cadherin promoter and can down-regulate transcription from the promoter. Involved in regulation of translation initiation. Proposed to be involved in positive regulation of translation such as of cyclin E1/CCNE1 mRNA and specifically of mRNAs containing complex secondary structures in their 5'UTRs; these functions seem to require RNA helicase activity. Specifically promotes translation of a subset of viral and cellular mRNAs carrying a 5'proximal stem-loop structure in their 5'UTRs and cooperates with the eIF4F complex. Proposed to act prior to 43S ribosomal scanning and to locally destabilize these RNA structures to allow recognition of the mRNA cap or loading onto the 40S subunit. After association with 40S ribosomal subunits seems to be involved in the functional assembly of 80S ribosomes; the function seems to cover translation of mRNAs with structured and non-structured 5'UTRs and is independent of RNA helicase activity. Also proposed to inhibit cap-dependent translation by competetive interaction with EIF4E which can block the EIF4E:EIF4G complex formation. Proposed to be involved in stress response and stress granule assembly; the function is independent of RNA helicase activity and seems to involve association with EIF4E. May be involved in nuclear export of specific mRNAs but not in bulk mRNA export via interactions with XPO1 and NXF1. Also associates with polyadenylated mRNAs independently of NXF1. Associates with spliced mRNAs in an exon junction complex (EJC)-dependent manner and seems not to be directly involved in splicing. May be involved in nuclear mRNA export by association with DDX5 and regulating its nuclear location. Involved in innate immune signaling promoting the production of type I interferon (IFN-alpha and IFN-beta); proposed to act as viral RNA sensor, signaling intermediate and transcriptional coactivator. Involved in TBK1 and IKBKE-dependent IRF3 activation leading to IFNB induction, plays a role of scaffolding adapter that links IKBKE and IRF3 and coordinates their activation. Also found associated with IFNB promoters; the function is independent of IRF3. Can bind to viral RNAs and via association with MAVS/IPS1 and DDX58/RIG-I is thought to induce signaling in early stages of infection. Involved in regulation of apoptosis. May be required for activation of the intrinsic but inhibit activation of the extrinsic apoptotic pathway. Acts as an antiapoptotic protein through association with GSK3A/B and BIRC2 in an apoptosis antagonizing signaling complex; activation of death receptors promotes caspase-dependent cleavage of BIRC2 and DDX3X and relieves the inhibition. May be involved in mitotic chromosome segregation. Is an allosteric activator of CSNK1E, it stimulates CSNK1E-mediated phosphorylation of DVL2 and is involved in the positive regulation of canonical Wnt signaling (By similarity). {ECO:0000250|UniProtKB:O00571}. PTM: Phosphorylated by TBK1; the phosphorylation is required to synergize with TBK1 in IFN-beta induction. Probably also phosphorylated by IKBKE (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}. Cytoplasm {ECO:0000250}. Mitochondrion outer membrane {ECO:0000250}. Note=Located predominantly in nuclear speckles and, at low levels, throughout the cytoplasm. Located to the outer side of nuclear pore complexes (NPC). Shuttles between the nucleus and the cytoplasm in a XPO1 and may be also in a NFX1-dependent manner. Associated with polyadenylated mRNAs in the cytoplasm and the nucleus. Predominantly located in nucleus during G(0) phase and in the cytoplasm during G1/S phase (By similarity). {ECO:0000250}. SUBUNIT: Binds RNA as a monomer at low DDX3X concentrations and as a dimer at high DDX3X concentrations. Interacts with XPO1, TDRD3, PABPC1, NXF1, EIF3C, MAVS, DDX58 and NCAPH. Interacts with DDX5; the interaction is regulated by the phosphorylation status of both proteins. Interacts with EIF4E; DDX3X competes with EIF4G1/EIF4G3 for interaction with EIF4E. Interacts with IKBKE; the interaction is direct. Interacts with IRF3; the interaction allows the phosphorylation and activation of IRF3 by IKBKE. Interacts with TBK1. Associates with the eukaryotic translation initiation factor 3 (eIF-3) complex. Associates with the 40S ribosome. Identified in a mRNP complex, at least composed of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1. Interacts with SP1. Interacts with GSK3A, GSK3B and TNFRSF10B. Interacts with CSNK1E; the interaction enhances CSNK1E recruitement to DVL2. Interacts with DHX33; the interaction is independent of RNA (PubMed:26100019). {ECO:0000250|UniProtKB:O00571, ECO:0000269|PubMed:26100019}. TISSUE SPECIFICITY: Developmentally regulated. +Q91VR5 DDX1_MOUSE ATP-dependent RNA helicase DDX1 (EC 3.6.4.13) (DEAD box protein 1) 740 82,500 Chain (1); Cross-link (1); Domain (3); Modified residue (4); Motif (1); Nucleotide binding (1); Region (4) FUNCTION: Acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. Possesses 5' single-stranded RNA overhang nuclease activity. Possesses ATPase activity on various RNA, but not DNA polynucleotides. May play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. Together with RELA, acts as a coactivator to enhance NF-kappa-B-mediated transcriptional activation (By similarity). Acts as a positive transcriptional regulator of cyclin CCND2 expression (PubMed:19398953). Binds to the cyclin CCND2 promoter region (PubMed:19398953). Associates with chromatin at the NF-kappa-B promoter region via association with RELA. Binds to poly(A) RNA. May be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. Component of the tRNA-splicing ligase complex required to facilitate the enzymatic turnover of catalytic subunit RTCB: together with archease (ZBTB8OS), acts by facilitating the guanylylation of RTCB, a key intermediate step in tRNA ligation (By similarity). Component of a multi-helicase-TICAM1 complex that acts as a cytoplasmic sensor of viral double-stranded RNA (dsRNA) and plays a role in the activation of a cascade of antiviral responses including the induction of proinflammatory cytokines via the adapter molecule TICAM1 (PubMed:21703541). Specifically binds (via helicase ATP-binding domain) on both short and long poly(I:C) dsRNA (PubMed:21703541). {ECO:0000250|UniProtKB:Q92499, ECO:0000269|PubMed:19398953, ECO:0000269|PubMed:21703541}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92499}. Cytoplasm, cytosol {ECO:0000269|PubMed:21703541}. Cytoplasm {ECO:0000250|UniProtKB:Q92499}. Cytoplasmic granule {ECO:0000250|UniProtKB:Q92499}. Mitochondrion {ECO:0000269|PubMed:21703541}. Note=Localized with MBNL1, TIAL1 and YBX1 in stress granules upon stress. Localized with CSTF2 in cleavage bodies. Forms large aggregates called DDX1 bodies. Relocalized into multiple foci (IR-induced foci or IRIF) after IR treatment, a process that depends on the presence of chromosomal DNA and/or RNA-DNA duplexes. Relocalized at sites of DNA double-strand breaks (DSBs) in an ATM-dependent manner after IR treatment. Colocalized with RELA in the nucleus upon TNF-alpha induction. Enters into the nucleus in case of active transcription while it accumulates in cytosol when transcription level is low (By similarity). Colocalizes in the cytosol with DDX21, DHX36 and TICAM1 (PubMed:21703541). Colocalizes in the mitochondria with TICAM1 and poly(I:C) RNA ligand (PubMed:21703541). The multi-helicase-TICAM1 complex may translocate to the mitochondria upon poly(I:C) stimulation (PubMed:21703541). {ECO:0000250|UniProtKB:Q92499, ECO:0000269|PubMed:21703541}. SUBUNIT: Found in a multi-helicase-TICAM1 complex at least composed of DHX36, DDX1, DDX21 and TICAM1; this complex exists in resting cells with or without poly(I:C) RNA ligand stimulation (PubMed:21703541). Interacts with DHX36 (PubMed:21703541). Interacts (via B30.2/SPRY domain) with DDX21 (via N-terminus); this interaction serves as bridges to TICAM1 (PubMed:21703541). Interacts with FAM98A (via N- and C-terminus). Interacts with MBNL1. Interacts with CSTF2. Interacts with HNRNPK. Interacts with ATM. Interacts with RELA (via C-terminus). Component of the tRNA-splicing ligase complex (By similarity). Interacts with PHF5A (via C-terminus) (PubMed:18758164). Interacts with PQBP1. {ECO:0000250|UniProtKB:Q92499, ECO:0000269|PubMed:18758164, ECO:0000269|PubMed:21703541}. DOMAIN: The helicase domain is involved in the stimulation of RELA transcriptional activity. {ECO:0000250}. TISSUE SPECIFICITY: Testis-specific. Expressed in the germ line stem cells, spermatogonia and spermatocytes of the testis. Also expressed in the seminoma and nonseminoma types of testicular germ cell tumors (TGCTs) (at protein level). {ECO:0000269|PubMed:19398953}. +Q6Q899 DDX58_MOUSE Probable ATP-dependent RNA helicase DDX58 (EC 3.6.4.13) (DEAD box protein 58) (RIG-I-like receptor 1) (RLR-1) (Retinoic acid-inducible gene 1 protein) (RIG-1) (Retinoic acid-inducible gene I protein) (RIG-I) 926 105,975 Alternative sequence (6); Beta strand (15); Chain (1); Cross-link (4); Domain (5); Helix (42); Metal binding (4); Modified residue (2); Motif (1); Mutagenesis (1); Nucleotide binding (1); Region (1); Sequence conflict (3); Turn (4) FUNCTION: Innate immune receptor which acts as a cytoplasmic sensor of viral nucleic acids and plays a major role in sensing viral infection and in the activation of a cascade of antiviral responses including the induction of type I interferons and proinflammatory cytokines. Its ligands include: 5'-triphosphorylated ssRNA and dsRNA and short dsRNA (<1 kb in length). In addition to the 5'-triphosphate moiety, blunt-end base pairing at the 5'-end of the RNA is very essential. Overhangs at the non-triphosphorylated end of the dsRNA RNA have no major impact on its activity. A 3'overhang at the 5'triphosphate end decreases and any 5'overhang at the 5' triphosphate end abolishes its activity. Upon ligand binding it associates with mitochondria antiviral signaling protein (MAVS/IPS1) which activates the IKK-related kinases: TBK1 and IKBKE which phosphorylate interferon regulatory factors: IRF3 and IRF7 which in turn activate transcription of antiviral immunological genes, including interferons (IFNs); IFN-alpha and IFN-beta. Detects both positive and negative strand RNA viruses including members of the families Paramyxoviridae: newcastle disease virus (NDV) and Sendai virus (SeV), Rhabdoviridae: vesicular stomatitis virus (VSV), Orthomyxoviridae: influenza A and B virus, Flaviviridae: Japanese encephalitis virus (JEV), hepatitis C virus (HCV), dengue virus (DENV) and west Nile virus (WNV). It also detects rotavirus and orthoreovirus. Also involved in antiviral signaling in response to viruses containing a dsDNA genome such as Epstein-Barr virus (EBV). Detects dsRNA produced from non-self dsDNA by RNA polymerase III, such as Epstein-Barr virus-encoded RNAs (EBERs). May play important roles in granulocyte production and differentiation, bacterial phagocytosis and in the regulation of cell migration. {ECO:0000269|PubMed:16039576, ECO:0000269|PubMed:16625202, ECO:0000269|PubMed:17942531, ECO:0000269|PubMed:19576794, ECO:0000269|PubMed:19609254, ECO:0000269|PubMed:19631370}. PTM: Phosphorylated in resting cells and dephosphorylated in RNA virus-infected cells. Phosphorylation at Thr-771 results in inhibition of its activity while dephosphorylation at these sites results in its activation. {ECO:0000250|UniProtKB:O95786}.; PTM: ISGylated. Conjugated to ubiquitin-like protein ISG15 upon IFN-beta stimulation. ISGylation negatively regulates its function in antiviral signaling response. {ECO:0000250|UniProtKB:O95786}.; PTM: Sumoylated, probably by MUL1; inhibiting its polyubiquitination. {ECO:0000250|UniProtKB:O95786}.; PTM: Ubiquitinated. Undergoes 'Lys-48'- and 'Lys-63'-linked ubiquitination. Lys-154 and Lys-164 are critical sites for RNF135-mediated and TRIM4-mediated ubiquitination. Deubiquitinated by CYLD, a protease that selectively cleaves 'Lys-63'-linked ubiquitin chains. Also probably deubiquitinated by USP17L2/USP17 that cleaves 'Lys-48'-and 'Lys-63'-linked ubiquitin chains and positively regulates the receptor. Ubiquitinated at Lys-181 by RNF125, leading to its degradation: ubiquitination takes place upon viral infection and is enhanced 'Lys-63'-linked ubiquitination of the CARD domains, which promote interaction with VCP/p97 and subsequent recruitment of RNF125 (By similarity). Ubiquitinated at Lys-813 by CBL, leading to its degradation: ubiquitination takes place upon viral infection and involves 'Lys-48'-linked ubiquitination (PubMed:23374343). {ECO:0000250|UniProtKB:O95786, ECO:0000269|PubMed:23374343}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell projection, ruffle membrane {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell junction, tight junction {ECO:0000250}. Note=Colocalized with TRIM25 at cytoplasmic perinuclear bodies. Associated with the actin cytoskeleton at membrane ruffles. {ECO:0000250}. SUBUNIT: Monomer; maintained as a monomer in an autoinhibited state (By similarity). Upon viral dsRNA binding and conformation shift, homomultimerizes and interacts (via tandem CARD domain) with MAVS/IPS1 promoting its filamentation (By similarity). Interacts with DHX58/LGP2, IKBKE, TBK1 and TMEM173/STING (By similarity). Interacts (via CARD domain) with TRIM25 (via SPRY domain) (By similarity). Interacts with RNF135 (By similarity). Interacts with CYLD (By similarity). Interacts with NLRC5; blocks the interaction of MAVS/IPS1 to DDX58 (By similarity). Interacts with SRC (By similarity). Interacts with DDX60 (By similarity). Interacts with isoform 2 of ZC3HAV1 (via zinc-fingers) in an RNA-dependent manner (By similarity). Interacts (via tandem CARD domain) with SEC14L1; the interaction is direct and impairs the interaction of DDX58 with MAVS/IPS1 (By similarity). Interacts with VCP/p97; interaction is direct and leads to recruit RNF125 and subsequent ubiquitination and degradation (By similarity). Interacts with NOP53; may regulate DDX58 through USP15-mediated 'Lys-63'-linked deubiquitination (By similarity). Interacts with SIGLEC10, CBL and PTPN11; these interactions are involved in 'Lys-48'-linked deubiquitination and degradation following infection with RNA viruses (PubMed:23374343). Interacts with LRRC25 (By similarity). Interacts with ZCCHC3; leading to activate DDX58/RIG-I (By similarity). {ECO:0000250|UniProtKB:O95786, ECO:0000269|PubMed:23374343}. DOMAIN: The helicase domain is responsible for dsRNA recognition. Interacts with IFIT3 (via N-terminus). {ECO:0000250}.; DOMAIN: The 2 CARD domains are responsible for interaction with and signaling through MAVS/IPS1 and for association with the actin cytoskeleton. {ECO:0000250}.; DOMAIN: The RLR CTR domain controls homomultimerization and interaction with MAVS/IPS1. In the absence of viral infection, the protein is maintained as a monomer in an autoinhibited state with the CARD domains masked through intramolecular interactions mediated by the RLR CTR domain. Upon binding to viral RNA in the presence of ATP, the RLR CTR domain induces a conformational change exposing the CARD domain and promotes dimerization and CARD interactions with the adapter protein MAVS/IPS1 leading to the induction of downstream signaling.; DOMAIN: The second CARD domain is the primary site for 'Lys-63'-linked ubiquitination. {ECO:0000250}. +Q80X90 FLNB_MOUSE Filamin-B (FLN-B) (ABP-280-like protein) (Actin-binding-like protein) (Beta-filamin) 2602 277,825 Chain (1); Cross-link (1); Domain (2); Modified residue (24); Region (4); Repeat (24) FUNCTION: Connects cell membrane constituents to the actin cytoskeleton. May promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. Anchors various transmembrane proteins to the actin cytoskeleton (By similarity). {ECO:0000250}. PTM: ISGylation prevents ability to interact with the upstream activators of the JNK cascade and inhibits IFNA-induced JNK signaling. {ECO:0000250}.; PTM: Ubiquitination by a SCF-like complex containing ASB2 isoform 2 leads to proteasomal degradation which promotes muscle differentiation. {ECO:0000250|UniProtKB:O75369}. SUBCELLULAR LOCATION: Cytoplasm, cell cortex. Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, stress fiber {ECO:0000250}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250}. SUBUNIT: Homodimer. Interacts with FLNA, FLNC, INPPL1, ITGB1A, ITGB1D, ITGB3, ITGB6, MYOT, MYOZ1, PSEN1 and PSEN2 (By similarity). Interacts with MICALL2. Interacts with RFLNA and RFLNB (PubMed:21709252,PubMed:24436304). {ECO:0000250, ECO:0000269|PubMed:21709252, ECO:0000269|PubMed:24436304}. DOMAIN: Comprised of a NH2-terminal actin-binding domain, 24 internally homologous repeats and two hinge regions. Repeat 24 and the second hinge domain are important for dimer formation. The first hinge region prevents binding to ITGA and ITGB subunits (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in hippocampus, cortex, cerebellar Purkinje cells and granule cell layers. {ECO:0000269|PubMed:12393796}. +Q9JJY4 DDX20_MOUSE Probable ATP-dependent RNA helicase DDX20 (EC 3.6.4.13) (Component of gems 3) (DEAD box protein 20) (DEAD box protein DP 103) (Gemin-3) (Regulator of steroidogenic factor 1) (ROSF-1) 825 91,710 Binding site (2); Chain (1); Domain (2); Modified residue (15); Motif (2); Nucleotide binding (2); Sequence conflict (4) FUNCTION: The SMN complex plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus. May also play a role in the metabolism of small nucleolar ribonucleoprotein (snoRNPs) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus, gem. Note=Localized in subnuclear structures next to coiled bodies, called Gemini of Cajal bodies (Gems). SUBUNIT: Part of the core SMN complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8 and STRAP/UNRIP. Part of the SMN-Sm complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8, STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG. Interacts directly with GEMIN5. Interacts directly with SNUPN. Interacts with PPP4R2. Interacts with FOXL2. Interacts with NANOS1 and PUM2. {ECO:0000269|PubMed:10767334, ECO:0000269|PubMed:16153597}. +P82020 DEFB2_MOUSE Beta-defensin 2 (BD-2) (mBD-2) (Defensin, beta 2) 71 7,820 Disulfide bond (3); Peptide (1); Signal peptide (1) FUNCTION: Has bactericidal activity. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. TISSUE SPECIFICITY: Kidney, uterus and to a lesser extent in heart. {ECO:0000269|PubMed:9923615}. +Q9EPV9 DEFB5_MOUSE Beta-defensin 5 (BD-5) (mBD-5) (Defensin, beta 5) 64 6,970 Chain (1); Disulfide bond (3); Sequence conflict (4); Signal peptide (1) FUNCTION: Has antibacterial activity. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +Q9WV68 DECR2_MOUSE Peroxisomal 2,4-dienoyl-CoA reductase (EC 1.3.1.34) (2,4-dienoyl-CoA reductase 2) 292 31,300 Binding site (6); Chain (1); Initiator methionine (1); Modified residue (5); Motif (1); Nucleotide binding (3); Region (1) FUNCTION: Auxiliary enzyme of beta-oxidation. Participates in the degradation of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions in peroxisome. Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA. Has activity towards short and medium chain 2,4-dienoyl-CoAs, but also towards 2,4,7,10,13,16,19-docosaheptaenoyl-CoA, suggesting that it does not constitute a rate limiting step in the peroxisomal degradation of docosahexaenoic acid. SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:10464321}. SUBUNIT: Monomer, dimer and oligomer. {ECO:0000250}. +Q9D9V7 DEN6B_MOUSE Protein DENND6B (DENN domain-containing protein 6B) 585 66,588 Chain (1); Domain (3); Erroneous initiation (1) FUNCTION: Guanine nucleotide exchange factor (GEF) for RAB14. Also has some, lesser GEF activity towards RAB35 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Recycling endosome {ECO:0000305}. Cytoplasm {ECO:0000305}. +Q8C1P2 DFA21_MOUSE Alpha-defensin 21 (Defensin-related cryptdin-21) 93 10,507 Disulfide bond (3); Peptide (1); Propeptide (1); Signal peptide (1) FUNCTION: May have microbicidal activities. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +Q7TNV7 DFB38_MOUSE Beta-defensin 38 (BD-38) (mBD-38) (Defensin, beta 38) 63 7,443 Chain (1); Disulfide bond (3); Signal peptide (1) FUNCTION: Synthetic Defb38 kills both Gram-negative (E.coli and P.aeruginosa) and Gram-positive (E.faecium) bacteria. {ECO:0000269|PubMed:14718547}. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Only expressed in epididymis (caput, corpus and cauda). {ECO:0000269|PubMed:14718547}. +P50715 DFAR7_MOUSE Alpha-defensin-related sequence 7 (CRS4C2) (Cryptdin-related protein 4C-2) (Defensin-related cryptdin-related sequence 7) 91 10,055 Peptide (1); Propeptide (1); Region (1); Repeat (6); Sequence conflict (1); Signal peptide (1) FUNCTION: Apparent precursor of a secreted, cationic, proline- and cysteine-rich peptide that contains Cys-Pro-Xaa repeats. Unlike cryptdin, the proposed mature peptide region lacks the structural motif characteristic of defensins. It may have microbicidal activities. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Paneth cells of the small bowel. +Q8R2I7 DFB11_MOUSE Beta-defensin 11 (BD-11) (mBD-11) (Defensin, beta 11) 77 8,666 Chain (1); Disulfide bond (3); Signal peptide (1) FUNCTION: Has antibacterial activity. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. TISSUE SPECIFICITY: Expressed in both adult and neonate brain, and very weakly in kidneys, epididymis, and testis. {ECO:0000269|PubMed:12644567}. +O54786 DFFA_MOUSE DNA fragmentation factor subunit alpha (DNA fragmentation factor 45 kDa subunit) (DFF-45) (Inhibitor of CAD) (ICAD) 331 36,572 Alternative sequence (2); Beta strand (7); Chain (1); Domain (1); Helix (2); Modified residue (2); Sequence conflict (3); Site (2) FUNCTION: Inhibitor of the caspase-activated DNase (DFF40). PTM: Caspase-3 cleaves DFF45 at 2 sites to generate an active factor. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Heterodimer of DFFA and DFFB. +Q8R2I5 DFB15_MOUSE Beta-defensin 15 (BD-15) (mBD-15) (Defensin, beta 15) 79 8,730 Chain (1); Disulfide bond (3); Signal peptide (1) FUNCTION: Has antibacterial activity. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. TISSUE SPECIFICITY: Expressed in testis and to a lesser extent in epididymis (caput, corpus and cauda). Also weakly expressed in kidneys and colon. {ECO:0000269|PubMed:14718547}. +Q8BVC1 DFB22_MOUSE Beta-defensin 22 (Defb22) 179 17,709 Chain (1); Compositional bias (1); Disulfide bond (3); Signal peptide (1) FUNCTION: Probable component of sperm glycocalyx. Likely protects and facilitates transport of sperm in the female reproductive tract. Probably released from the sperm surface during capacitation. {ECO:0000269|PubMed:18787081}. PTM: O-glycosylated; glycans contain alpha(2,3)-linked sialic acids. {ECO:0000250|UniProtKB:Q9BYW3}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:18787081}. Secreted, extracellular space {ECO:0000269|PubMed:18787081}. Note=In the corpus epididymis, located in vesicles below the apical surface of the plasma membrane. Secreted by epididymal cells and absorbed to the surface of sperm during transit through the epididymis. Coats the entire surface of ejaculated sperm although presence on the equatorial segment is less intense. {ECO:0000269|PubMed:18787081}. TISSUE SPECIFICITY: Specifically expressed in corpus epididymis and cauda epididymis with expression in corpus being highest (at protein level). Not detected in other tissues tested, including testis, prostate, seminal vesicle and vas deferens (at protein level). {ECO:0000269|PubMed:18787081}. +P50711 DFA13_MOUSE Alpha-defensin 13 (Defensin-related cryptdin-13) 93 10,565 Disulfide bond (3); Peptide (1); Propeptide (1); Signal peptide (1) FUNCTION: Probably contributes to the antimicrobial barrier function of the small bowel mucosa. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Paneth cells of the small bowel. +P50712 DFA14_MOUSE Alpha-defensin 14 (Defensin-related cryptdin-14) (Fragment) 85 9,589 Disulfide bond (3); Non-terminal residue (1); Peptide (1); Propeptide (1); Signal peptide (1) FUNCTION: Probably contributes to the antimicrobial barrier function of the small bowel mucosa. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Paneth cells of the small bowel. +Q9DCV3 DGAT2_MOUSE Diacylglycerol O-acyltransferase 2 (EC 2.3.1.20) (Acyl-CoA retinol O-fatty-acyltransferase) (ARAT) (Retinol O-fatty-acyltransferase) (EC 2.3.1.76) (Diglyceride acyltransferase 2) 388 43,770 Chain (1); Topological domain (3); Transmembrane (2) TRANSMEM 70 88 Helical. {ECO:0000255}.; TRANSMEM 93 112 Helical. {ECO:0000255}. TOPO_DOM 1 69 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 89 92 Lumenal. {ECO:0000255}.; TOPO_DOM 113 388 Cytoplasmic. {ECO:0000255}. Glycerolipid metabolism; triacylglycerol biosynthesis. FUNCTION: Essential acyltransferase that catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. Required for synthesis and storage of intracellular triglycerides. Probably plays a central role in cytosolic lipid accumulation. In liver, is primarily responsible for incorporating endogenously synthesized fatty acids into triglycerides. Functions also as an acyl-CoA retinol acyltransferase (ARAT) (By similarity). {ECO:0000250|UniProtKB:Q96PD7, ECO:0000269|PubMed:11481335, ECO:0000269|PubMed:15797871, ECO:0000269|PubMed:21680734, ECO:0000269|PubMed:22493088}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q96PD7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q96PD7}. Lipid droplet {ECO:0000250|UniProtKB:Q96PD7}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q96PD7}. SUBUNIT: Forms multimeric complexes consisting of several DGAT2 subunits. {ECO:0000250}. TISSUE SPECIFICITY: Predominantly expressed in liver. Also expressed in testis. {ECO:0000269|PubMed:11481335}. +P51658 DHB2_MOUSE Estradiol 17-beta-dehydrogenase 2 (EC 1.1.1.62) (17-beta-hydroxysteroid dehydrogenase type 2) (17-beta-HSD 2) (Testosterone 17-beta-dehydrogenase) (EC 1.1.1.239) 381 41,836 Active site (1); Binding site (1); Chain (1); Nucleotide binding (1); Sequence conflict (1); Transmembrane (1) TRANSMEM 4 24 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. FUNCTION: Capable of catalyzing the interconversion of testosterone and androstenedione, as well as estradiol and estrone. Also has 20-alpha-HSD activity. Uses NADH while EDH17B3 uses NADPH (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. +P50172 DHI1_MOUSE Corticosteroid 11-beta-dehydrogenase isozyme 1 (EC 1.1.1.146) (11-beta-hydroxysteroid dehydrogenase 1) (11-DH) (11-beta-HSD1) (11beta-HSD1A) 292 32,364 Active site (1); Beta strand (7); Binding site (1); Chain (1); Glycosylation (2); Helix (14); Nucleotide binding (5); Sequence conflict (4); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 8 24 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 7 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 25 292 Lumenal. {ECO:0000255}. FUNCTION: Catalyzes reversibly the conversion of cortisol to the inactive metabolite cortisone. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein. SUBUNIT: Homodimer. {ECO:0000269|PubMed:15865440}. TISSUE SPECIFICITY: Widely expressed. Highest expression in liver. +Q99L04 DHRS1_MOUSE Dehydrogenase/reductase SDR family member 1 (EC 1.1.-.-) 313 34,005 Active site (1); Binding site (1); Chain (1); Modified residue (1); Sequence conflict (2) +Q9CXV1 DHSD_MOUSE Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial (CybS) (CII-4) (QPs3) (Succinate dehydrogenase complex subunit D) (Succinate-ubiquinone oxidoreductase cytochrome b small subunit) (Succinate-ubiquinone reductase membrane anchor subunit) 159 17,014 Binding site (1); Chain (1); Metal binding (1); Topological domain (4); Transit peptide (1); Transmembrane (3) TRANSMEM 64 85 Helical. {ECO:0000250}.; TRANSMEM 91 111 Helical. {ECO:0000250}.; TRANSMEM 121 142 Helical. {ECO:0000250}. TOPO_DOM 57 63 Mitochondrial matrix. {ECO:0000250}.; TOPO_DOM 86 90 Mitochondrial intermembrane. {ECO:0000250}.; TOPO_DOM 112 120 Mitochondrial matrix. {ECO:0000250}.; TOPO_DOM 143 159 Mitochondrial intermembrane. {ECO:0000250}. Carbohydrate metabolism; tricarboxylic acid cycle. FUNCTION: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Component of complex II composed of four subunits: the flavoprotein (FP) SDHA, iron-sulfur protein (IP) SDHB, and a cytochrome b560 composed of SDHC and SDHD. {ECO:0000250}. +Q9CXR1 DHRS7_MOUSE Dehydrogenase/reductase SDR family member 7 (EC 1.1.-.-) (Retinal short-chain dehydrogenase/reductase 4) (retSDR4) 338 38,167 Active site (1); Binding site (1); Chain (1); Erroneous initiation (1); Frameshift (1); Nucleotide binding (1); Sequence conflict (1); Signal peptide (1) +A2ATU0 DHTK1_MOUSE Probable 2-oxoglutarate dehydrogenase E1 component DHKTD1, mitochondrial (EC 1.2.4.2) (Dehydrogenase E1 and transketolase domain-containing protein 1) 921 102,793 Chain (1); Modified residue (4); Sequence caution (1); Sequence conflict (2); Transit peptide (1) FUNCTION: The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. +Q99ML4 DIK1B_MOUSE Divergent protein kinase domain 1B (Pancreatitis-induced protein 49) (Protein FAM69B) 431 48,792 Chain (1); Disulfide bond (2); Erroneous initiation (3); Frameshift (1); Motif (1); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 31 51 Helical. {ECO:0000255}. TOPO_DOM 1 30 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 52 431 Lumenal. {ECO:0000255}. PTM: Among the many cysteines in the lumenal domain, most are probably involved in disulfide bonds. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21334309}; Single-pass type II membrane protein {ECO:0000269|PubMed:21334309}. TISSUE SPECIFICITY: Expressed in kidney, testis, lung, heart, stomach, intestine, pancreas, liver and salivary gland. Strongly expressed in acute pancreatitis, brain, and in peripheral endothelial cells. {ECO:0000269|PubMed:11281735, ECO:0000269|PubMed:21334309}. +Q8C9B9 DIDO1_MOUSE Death-inducer obliterator 1 (DIO-1) (Death-associated transcription factor 1) (DATF-1) 2256 247,176 Alternative sequence (4); Beta strand (3); Chain (1); Cross-link (1); Domain (1); Erroneous initiation (3); Helix (3); Modified residue (27); Motif (2); Sequence conflict (14); Zinc finger (1) FUNCTION: Required for early embryonic stem cell development (By similarity). Putative transcription factor, weakly pro-apoptotic when overexpressed. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Translocates to the mitotic spindle upon loss of interaction with H3K4me3 during early mitosis (By similarity). Translocates to the nucleus after pro-apoptotic stimuli. {ECO:0000250}. SUBUNIT: Interacts specifically (via PHD-type zinc finger) with histone H3 that is trimethylated at 'Lys-4' (H3K4me3), histone phosphorylation at 'Thr-3' or 'Thr-6' disrupts this binding and promotes translocation of DIDO1 from chromatin to the mitotic spindle during mitosis. {ECO:0000250}. DOMAIN: The PHD-type zinc finger forms an aromatic cage around H3K4me3. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. Expressed at intermediate levels. +Q9QYI4 DJB12_MOUSE DnaJ homolog subfamily B member 12 (mDj10) 376 41,988 Chain (1); Domain (1); Modified residue (1); Sequence conflict (1); Transmembrane (1) TRANSMEM 243 263 Helical. {ECO:0000255}. FUNCTION: Acts as a co-chaperone with HSPA8/Hsc70; required to promote protein folding and trafficking, prevent aggregation of client proteins, and promote unfolded proteins to endoplasmic reticulum-associated degradation (ERAD) pathway. Acts by determining HSPA8/Hsc70's ATPase and polypeptide-binding activities. Can also act independently of HSPA8/Hsc70: together with DNAJB14, acts as a chaperone that promotes maturation of potassium channels KCND2 and KCNH2 by stabilizing nascent channel subunits and assembling them into tetramers. While stabilization of nascent channel proteins is dependent on HSPA8/Hsc70, the process of oligomerization of channel subunits is independent of HSPA8/Hsc70. When overexpressed, forms membranous structures together with DNAJB14 and HSPA8/Hsc70 within the nucleus; the role of these structures, named DJANGOs, is still unclear. {ECO:0000250|UniProtKB:Q9NXW2}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9NXW2}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:Q9NXW2}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9NXW2}. Note=Localizes to the endoplasmic reticulum membrane. When overexpressed, forms membranous structures in the nucleus. {ECO:0000250|UniProtKB:Q9NXW2}. SUBUNIT: Homodimer and homotetramer. Interacts (via J domain) with HSPA8/Hsc70. Forms a multiprotein complex, at least composed of DNAJB12, DNAJB14, HSPA8/Hsc70 and SGTA; interaction with DNAJB14 and HSPA8/Hsc70 is direct. {ECO:0000250|UniProtKB:Q9NXW2}. +A2ALW5 DJC25_MOUSE DnaJ homolog subfamily C member 25 357 41,937 Alternative sequence (1); Chain (1); Domain (1); Erroneous gene model prediction (1); Erroneous initiation (1); Transmembrane (3) TRANSMEM 19 39 Helical. {ECO:0000255}.; TRANSMEM 147 167 Helical. {ECO:0000255}.; TRANSMEM 241 261 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q80Y75 DJB13_MOUSE DnaJ homolog subfamily B member 13 (Testis and spermatogenesis cell-related protein 6) (Testis spermatocyte apoptosis-related gene 6 protein) (Testis spermatogenesis apoptosis-related gene 3 protein) (Testis spermatogenesis apoptosis-related gene 6 protein) 316 36,155 Chain (1); Domain (1); Sequence conflict (1) FUNCTION: Plays a role in the formation of the central complex of ciliary and flagellar axonemes. {ECO:0000250|UniProtKB:P59910, ECO:0000269|PubMed:27530713}. SUBCELLULAR LOCATION: Cell projection, cilium, flagellum {ECO:0000269|PubMed:29298896}. Cell projection, cilium {ECO:0000269|PubMed:19919626}. Note=Localizes both to epithelial motile cilium and the sperm flagellum (By similarity). In spermatids, rapidly enriched in the coupling apparatus with the elongation of the spermatid. Tightly attached to the implantation fossa during the maturation of the spermatid. In mature spermatzoa evenly distributed along the flagellum at the radial spoke of the axoneme (PubMed:29298896, PubMed:19919626). {ECO:0000250|UniProtKB:P59910, ECO:0000269|PubMed:19919626, ECO:0000269|PubMed:29298896}. SUBUNIT: Homodimer (By similarity). Interacts with SUN5 (PubMed:29298896). {ECO:0000250|UniProtKB:P59910, ECO:0000269|PubMed:29298896}. TISSUE SPECIFICITY: Expressed in ciliated cell-containing tissues such as testis, brain, lung, ovary and oviduct. {ECO:0000269|PubMed:14673507, ECO:0000269|PubMed:19919626, ECO:0000269|PubMed:29298896}. +Q8CIP5 DISP2_MOUSE Protein dispatched homolog 2 1345 147,944 Alternative sequence (2); Chain (1); Domain (1); Glycosylation (3); Modified residue (1); Sequence conflict (3); Transmembrane (12) TRANSMEM 125 145 Helical. {ECO:0000255}.; TRANSMEM 440 460 Helical. {ECO:0000255}.; TRANSMEM 465 485 Helical. {ECO:0000255}.; TRANSMEM 497 517 Helical. {ECO:0000255}.; TRANSMEM 544 564 Helical. {ECO:0000255}.; TRANSMEM 572 592 Helical. {ECO:0000255}.; TRANSMEM 659 679 Helical. {ECO:0000255}.; TRANSMEM 919 939 Helical. {ECO:0000255}.; TRANSMEM 945 965 Helical. {ECO:0000255}.; TRANSMEM 974 994 Helical. {ECO:0000255}.; TRANSMEM 1019 1039 Helical. {ECO:0000255}.; TRANSMEM 1043 1063 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q64317 DLX1_MOUSE Homeobox protein DLX-1 255 27,309 Chain (1); DNA binding (1); Sequence conflict (2) FUNCTION: Plays a role as a transcriptional activator or repressor (PubMed:21875655). Inhibits several cytokine signaling pathways, such as TGFB1, activin-A/INHBA and BMP4 by interfering with the transcriptional stimulatory activity of transcription factors, such as MSX2, FAST2, SMAD2 and SMAD3 during hematopoietic cell differentiation (By similarity). Plays a role in terminal differentiation of interneurons, such as amacrine and bipolar cells in the developing retina (PubMed:21875655). Likely to play a regulatory role in the development of the ventral forebrain (PubMed:1676488). May play a role in craniofacial patterning and morphogenesis and may be involved in the early development of diencephalic subdivisions (PubMed:1676488). {ECO:0000250|UniProtKB:P56177, ECO:0000269|PubMed:1676488, ECO:0000269|PubMed:21875655}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P56177}. SUBUNIT: Interacts with SMAD4 (via homeobox DNA-binding domain) (By similarity). Interacts (via homeobox DNA-binding domain) with POU4F2; this interaction suppresses DLX1-mediated transcriptional activity in postnatal retina and enhances retinal ganglion cell (RGC) differentiation (PubMed:21875655). {ECO:0000250|UniProtKB:P56177, ECO:0000269|PubMed:21875655}. DOMAIN: The homeobox DNA-binding domain is necessary for its nuclear localization, transcriptional and erythroid differentiation activities. {ECO:0000250|UniProtKB:P56177}. TISSUE SPECIFICITY: Expressed in a restricted region of the developing brain, within the diencephalon and the adjacent telencephalic regions. {ECO:0000269|PubMed:1676488}. +P70697 DCUP_MOUSE Uroporphyrinogen decarboxylase (UPD) (URO-D) (EC 4.1.1.37) 367 40,692 Binding site (6); Chain (1); Modified residue (1); Region (1); Sequence conflict (2); Site (1) Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 4/4. FUNCTION: Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Homodimer. {ECO:0000250}. +Q99MJ9 DDX50_MOUSE ATP-dependent RNA helicase DDX50 (EC 3.6.4.13) (DEAD box protein 50) (Gu-beta) (Nucleolar protein Gu2) 734 82,175 Chain (1); Compositional bias (1); Cross-link (1); Domain (2); Modified residue (8); Motif (2); Nucleotide binding (1) SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. SUBUNIT: Interacts with C1QBP. {ECO:0000250}. +P16381 DDX3L_MOUSE Putative ATP-dependent RNA helicase Pl10 (EC 3.6.4.13) 660 73,141 Chain (1); Compositional bias (1); Cross-link (1); Domain (2); Initiator methionine (1); Modified residue (18); Motif (2); Nucleotide binding (2) FUNCTION: Putative ATP-dependent RNA helicase. Possible role in a key step of the spermatogenic process. TISSUE SPECIFICITY: Testis. +Q8K301 DDX52_MOUSE Probable ATP-dependent RNA helicase DDX52 (EC 3.6.4.13) (ATP-dependent RNA helicase ROK1-like) (DEAD box protein 52) 598 67,474 Chain (1); Compositional bias (1); Domain (2); Modified residue (2); Motif (2); Nucleotide binding (1); Sequence conflict (6) SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. +Q62095 DDX3Y_MOUSE ATP-dependent RNA helicase DDX3Y (EC 3.6.4.13) (D1Pas1-related sequence 1) (DEAD box protein 3, Y-chromosomal) (DEAD-box RNA helicase DEAD2) (mDEAD2) 658 73,428 Chain (1); Cross-link (1); Domain (2); Initiator methionine (1); Modified residue (16); Motif (2); Nucleotide binding (2); Sequence conflict (1) FUNCTION: Probable ATP-dependent RNA helicase. May play a role in spermatogenesis. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15383328}. Nucleus {ECO:0000269|PubMed:15383328}. Note=Shuttles between the nucleus and the cytoplasm in an XPO1-dependent manner. SUBUNIT: May interact with TDRD3. {ECO:0000250}. TISSUE SPECIFICITY: Found in heart, brain, liver, skeletal muscle, kidney and testis. Low expression detected in lung. In testis, expressed in all types of spermatogenic cells including spermatogonia, spermatocytes, spermatids and somatic Sertoli cells within the seminiferous tubules. Also expressed in Leydig cells and other interstitial cells. {ECO:0000269|PubMed:15383328, ECO:0000269|PubMed:8144024}. +Q9DBN9 DDX59_MOUSE Probable ATP-dependent RNA helicase DDX59 (EC 3.6.4.13) (DEAD box protein 59) 619 68,234 Alternative sequence (2); Chain (1); Cross-link (1); Domain (2); Modified residue (2); Motif (2); Nucleotide binding (1); Sequence conflict (1); Zinc finger (1) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. DOMAIN: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis. +Q8BZS9 DHX32_MOUSE Putative pre-mRNA-splicing factor ATP-dependent RNA helicase DHX32 (EC 3.6.4.13) (DEAH box protein 32) (MuDDX32) 744 83,941 Alternative sequence (1); Chain (1); Domain (2); Modified residue (1); Motif (1); Nucleotide binding (1); Sequence conflict (2) SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Mitochondrion {ECO:0000250}. +Q3TXU5 DHYS_MOUSE Deoxyhypusine synthase (DHS) (EC 2.5.1.46) 369 40,642 Active site (1); Binding site (5); Chain (1); Nucleotide binding (4); Region (3); Sequence conflict (1) Protein modification; eIF5A hypusination. FUNCTION: Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a critical lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue. This is the first step of the post-translational modification of that lysine into an unusual amino acid residue named hypusine. Hypusination is unique to mature eIF-5A factor and is essential for its function. {ECO:0000250|UniProtKB:P49366}. +Q6P5D3 DHX57_MOUSE Putative ATP-dependent RNA helicase DHX57 (EC 3.6.4.13) (DEAH box protein 57) 1388 155,762 Alternative sequence (6); Chain (1); Compositional bias (1); Domain (3); Modified residue (3); Motif (1); Nucleotide binding (1); Sequence conflict (4); Zinc finger (1) FUNCTION: Probable ATP-binding RNA helicase. +O70566 DIAP2_MOUSE Protein diaphanous homolog 2 (Diaphanous-related formin-2) (DRF2) (mDia3) 1098 124,871 Chain (1); Coiled coil (3); Compositional bias (2); Domain (4); Modified residue (1); Sequence caution (1); Sequence conflict (1) FUNCTION: May be involved in oogenesis. SUBUNIT: Interacts with MAPRE1 and APC. {ECO:0000269|PubMed:15311282}. DOMAIN: The DAD domain regulates activation via by an autoinhibitory interaction with the GBD/FH3 domain. This autoinhibition is released upon competitive binding of an activated GTPase. The release of DAD allows the FH2 domain to then nucleate and elongate nonbranched actin filaments (By similarity). {ECO:0000250}. +Q8CHS2 DJC22_MOUSE DnaJ homolog subfamily C member 22 339 37,942 Chain (1); Domain (1); Transmembrane (7) TRANSMEM 5 25 Helical. {ECO:0000255}.; TRANSMEM 30 50 Helical. {ECO:0000255}.; TRANSMEM 81 101 Helical. {ECO:0000255}.; TRANSMEM 105 125 Helical. {ECO:0000255}.; TRANSMEM 135 155 Helical. {ECO:0000255}.; TRANSMEM 185 205 Helical. {ECO:0000255}.; TRANSMEM 218 238 Helical. {ECO:0000255}. FUNCTION: May function as a co-chaperone. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8VCE1 DJC28_MOUSE DnaJ homolog subfamily C member 28 385 44,873 Chain (1); Coiled coil (1); Domain (1) FUNCTION: May have a role in protein folding or as a chaperone. +Q921R4 DJC14_MOUSE DnaJ homolog subfamily C member 14 703 78,919 Chain (1); Compositional bias (1); Domain (1); Natural variant (2); Sequence conflict (2); Transmembrane (2) TRANSMEM 305 325 Helical. {ECO:0000255}.; TRANSMEM 327 347 Helical. {ECO:0000255}. FUNCTION: Regulates the export of target proteins, such as DRD1, from the endoplasmic reticulum to the cell surface. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with the FxxxFxxxF motif of DRD1 via its C-terminal domain. {ECO:0000250}. +Q8VEJ3 DKK4_MOUSE Dickkopf-related protein 4 (Dickkopf-4) (Dkk-4) 221 24,261 Chain (1); Disulfide bond (5); Region (2); Signal peptide (1) FUNCTION: Antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by forming a ternary complex with the transmembrane protein KREMEN that promotes internalization of LRP5/6. DKKs play an important role in vertebrate development, where they locally inhibit Wnt regulated processes such as antero-posterior axial patterning, limb development, somitogenesis and eye formation. In the adult, Dkks are implicated in bone formation and bone disease, cancer and Alzheimer disease (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Interacts with LRP5 and LRP6. {ECO:0000250}. DOMAIN: The C-terminal cysteine-rich domain mediates interaction with LRP5 and LRP6. {ECO:0000250}. +P35737 DMB_MOUSE Class II histocompatibility antigen, M beta 1 chain (H2-M beta 1 chain) 261 28,899 Chain (1); Disulfide bond (2); Domain (1); Glycosylation (1); Motif (1); Region (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 219 239 Helical. {ECO:0000255}. TOPO_DOM 19 218 Lumenal. {ECO:0000255}.; TOPO_DOM 240 261 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a critical role in catalyzing the release of class II HLA-associated invariant chain-derived peptides (CLIP) from newly synthesized class II HLA molecules and freeing the peptide binding site for acquisition of antigenic peptides. SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000269|PubMed:7584146}; Single-pass type I membrane protein {ECO:0000269|PubMed:7584146}. Lysosome membrane {ECO:0000269|PubMed:7584146}; Single-pass type I membrane protein {ECO:0000269|PubMed:7584146}. Note=Localizes to late endocytic compartment. Associates with lysosome membranes. SUBUNIT: Heterodimer of an alpha chain (DMA) and a beta chain (DMB). DOMAIN: The YXXZ (Tyr-Xaa-Xaa-Zaa, where Zaa is a hydrophobic residue) motif mediates the targeting to the lysosomal compartments. +Q811D0 DLG1_MOUSE Disks large homolog 1 (Embryo-dlg/synapse-associated protein 97) (E-dlg/SAP97) (Synapse-associated protein 97) (SAP-97) (SAP97) 905 100,120 Alternative sequence (3); Beta strand (5); Chain (1); Domain (6); Helix (2); Modified residue (16); Region (1); Sequence conflict (14) FUNCTION: Essential multidomain scaffolding protein required for normal development. Recruits channels, receptors and signaling molecules to discrete plasma membrane domains in polarized cells. Regulates the excitability of cardiac myocytes by modulating the functional expression of Kv4 channels (By similarity). Functional regulator of Kv1.5 channel (By similarity). May play a role in adherens junction assembly, signal transduction, cell proliferation, synaptogenesis and lymphocyte activation. {ECO:0000250, ECO:0000269|PubMed:11238884}. PTM: Phosphorylated by MAPK12. Phosphorylation of Ser-232 regulates association with GRIN2A (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q62696}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q12959}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q62696}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q62696}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250|UniProtKB:Q62696}. Cell junction, synapse {ECO:0000250|UniProtKB:Q62696}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:Q62696}. Cell junction {ECO:0000250|UniProtKB:Q12959}. Cytoplasm {ECO:0000250|UniProtKB:Q12959}. Apical cell membrane {ECO:0000250|UniProtKB:Q12959}. Note=Colocalizes with EPB41 at regions of intercellular contacts. Basolateral in epithelial cells. May also associate with endoplasmic reticulum membranes. Mainly found in neurons soma, moderately found at postsynaptic densities. {ECO:0000250|UniProtKB:Q12959, ECO:0000250|UniProtKB:Q62696}. SUBUNIT: Homotetramer (Probable). Interacts (via guanylate kinase-like domain) with DLGAP1, DLGAP2, DLGAP3, DLGAP4, and MAP1A (By similarity). Interacts (via guanylate kinase-like domain) with KIF13B (By similarity). May interact with HTR2A (PubMed:14988405). Interacts (via PDZ domains) with GRIA1 (By similarity). Interacts (via PDZ domains) with GRIN2A (By similarity). Interacts (via PDZ domains) with KCND2 and KCND3 (By similarity). Interacts (via PDZ domains) with KCNA1, KCNA2, KCNA3, KCNA4, and ADGRA3 (By similarity). Interacts (via PDZ domains) with ADGRA3 (By similarity). Interacts with KCNF1 (By similarity). Interacts with CAMK2 (By similarity). Interacts with CAMK2 (By similarity). Interacts with cytoskeleton-associated protein EPB41 (By similarity). Interacts with cytoskeleton-associated protein EZR (PubMed:8922391). Found in a complex with KCNA5 and CAV3 (PubMed:15277200). Found in a complex with APC and CTNNB1 (PubMed:8638125). Interacts with CDH1 through binding to PIK3R1 (By similarity). Forms multiprotein complexes with CASK, LIN7A, LIN7B, LIN7C, APBA1, and KCNJ12 (By similarity). Interacts with TOPK (By similarity). Forms a tripartite complex composed of DLG1, MPP7 and LIN7 (LIN7A or LIN7C) (By similarity). May interact with TJAP1 (By similarity). Interacts with PTEN (By similarity). Interacts with LRFN1, LRFN2, LRFN4 and SFPQ (By similarity). Interacts with FRMPD4 (via C-terminus) (By similarity). Interacts (via PDZ domains) with ADGRA2 (via PDZ-binding motif) (PubMed:25558062). {ECO:0000250|UniProtKB:Q12959, ECO:0000250|UniProtKB:Q62696, ECO:0000269|PubMed:14988405, ECO:0000269|PubMed:15277200, ECO:0000269|PubMed:25558062, ECO:0000269|PubMed:8638125, ECO:0000305}. DOMAIN: The PDZ domains may also mediate association to membranes by binding to EPB41 and ADGRA2 together with the L27 domain that binds CASK and DLG2. {ECO:0000250}.; DOMAIN: The L27 domain may regulate DLG1 self-association. The N-terminal alternatively spliced region is capable of binding several SH3 domains and also moderates the level of protein oligomerization (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in epithelial, mesenchymal, neuronal, endothelial and hematopoietic cells during embryogenesis. Expressed in fibroblasts and T-cells. Widely expressed in adult mice. {ECO:0000269|PubMed:11238884}. +Q9D415 DLGP1_MOUSE Disks large-associated protein 1 (DAP-1) (Guanylate kinase-associated protein) (PSD-95/SAP90-binding protein 1) (SAP90/PSD-95-associated protein 1) (SAPAP1) 992 110,374 Alternative sequence (7); Chain (1); Erroneous initiation (1); Modified residue (21); Motif (1); Region (2); Sequence conflict (4) FUNCTION: Part of the postsynaptic scaffold in neuronal cells. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250}. Cell junction, synapse {ECO:0000269|PubMed:24153177}. SUBUNIT: Interacts with the guanylate kinase-like domain of DLG1, DLG2, DLG3, DLG4 and AIP1. Interacts with the PDZ domain of SHANK1, SHANK2 and SHANK3. Found in a complex with DLG4 and SHANK1, SHANK2 or SHANK3. Found in a complex with DLG4 and BEGAIN. Interacts with DYL2 and LRFN1. Interacts with MPP2 (via the SH3-Guanylate kinase-like sub-module) (By similarity). {ECO:0000250|UniProtKB:P97836, ECO:0000269|PubMed:24153177}. TISSUE SPECIFICITY: Highest levels in the neocortex, part of the hippocampus, the granule cell layer of the cerebellum, the glomerular layer of the olfactory bulb, the inner plexiform layer of the retina, the ventral and dorsal horn of the spinal chord, the neuromuscular junction and the submandibular ganglion. {ECO:0000269|PubMed:15024750}. +Q8BJ42 DLGP2_MOUSE Disks large-associated protein 2 (DAP-2) (PSD-95/SAP90-binding protein 2) (SAP90/PSD-95-associated protein 2) (SAPAP2) 1059 119,074 Alternative sequence (1); Chain (1); Modified residue (14); Sequence conflict (2) FUNCTION: May play a role in the molecular organization of synapses and neuronal cell signaling. Could be an adapter protein linking ion channel to the subsynaptic cytoskeleton. May induce enrichment of PSD-95/SAP90 at the plasma membrane. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250}. Cell junction, synapse {ECO:0000250}. Note=Postsynaptic density of neuronal cells. {ECO:0000250}. SUBUNIT: Interacts with DLG4/PSD-95. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in various brain areas. {ECO:0000269|PubMed:15024750}. +P54265 DMPK_MOUSE Myotonin-protein kinase (MT-PK) (EC 2.7.11.1) (DM-kinase) (DMK) (DMPK) (Myotonic dystrophy protein kinase) (MDPK) 631 69,602 Active site (1); Alternative sequence (11); Binding site (1); Chain (1); Coiled coil (1); Domain (2); Modified residue (3); Nucleotide binding (1); Topological domain (2); Transmembrane (1) TRANSMEM 593 613 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 1 592 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 614 631 Lumenal. {ECO:0000255}. FUNCTION: Non-receptor serine/threonine protein kinase which is necessary for the maintenance of skeletal muscle structure and function. May play a role in myocyte differentiation and survival by regulating the integrity of the nuclear envelope and the expression of muscle-specific genes. May also phosphorylate PPP1R12A and inhibit the myosin phosphatase activity to regulate myosin phosphorylation. Also critical to the modulation of cardiac contractility and to the maintenance of proper cardiac conduction activity probably through the regulation of cellular calcium homeostasis. Phosphorylates PLN, a regulator of calcium pumps and may regulate sarcoplasmic reticulum calcium uptake in myocytes. May also phosphorylate FXYD1/PLM which is able to induce chloride currents. May also play a role in synaptic plasticity. {ECO:0000269|PubMed:12612014, ECO:0000269|PubMed:15598648, ECO:0000269|PubMed:18729234, ECO:0000269|PubMed:21949239, ECO:0000269|PubMed:9294109}. PTM: Phosphorylated. Autophosphorylates. Phosphorylation by RAF1 may result in activation of DMPK (By similarity). {ECO:0000250}.; PTM: Proteolytic processing of the C-terminus may remove the transmembrane domain and release the kinase from membranes stimulating its activity. {ECO:0000250}. SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane. Cell membrane. Note=Localizes to sarcoplasmic reticulum membranes of cardiomyocytes.; SUBCELLULAR LOCATION: Isoform 1: Endoplasmic reticulum membrane; Single-pass type IV membrane protein; Cytoplasmic side. Nucleus outer membrane; Single-pass type IV membrane protein; Cytoplasmic side.; SUBCELLULAR LOCATION: Isoform 8: Mitochondrion outer membrane; Single-pass type IV membrane protein.; SUBCELLULAR LOCATION: Isoform 5: Cytoplasm, cytosol. SUBUNIT: Homodimer; homodimerization stimulates the kinase activity. Interacts with HSPB2; may enhance DMPK kinase activity. Interacts with PLN; phosphorylates PLN. May interact with RAC1; may regulate DMPK kinase activity. Interacts with LMNA; may regulate nuclear envelope stability (By similarity). {ECO:0000250}. DOMAIN: The coiled coil domain is required for homodimerization and regulates the enzymatic activity. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in all tissues tested, with a predominance in brain, skeletal muscle, heart, and other tissues containing smooth muscle. In the heart, expression is restricted to the cardiomyocytes in the ventricle and atrium. {ECO:0000269|PubMed:15598648}. +Q9QX11 CYH1_MOUSE Cytohesin-1 (PH, SEC7 and coiled-coil domain-containing protein 1) (CLM1) (SEC7 homolog A) (mSec7-1) 398 46,274 Alternative sequence (1); Binding site (4); Chain (1); Coiled coil (1); Domain (2); Modified residue (1); Mutagenesis (4); Region (3); Sequence conflict (1) FUNCTION: Promotes guanine-nucleotide exchange on ARF1, ARF5 and ARF6 (PubMed:18042453, PubMed:20080746). Promotes the activation of ARF factors through replacement of GDP with GTP (PubMed:18042453). Plays an important role in membrane trafficking, during junctional remodeling and epithelial polarization, through regulation of ARF6 activity (PubMed:20080746, PubMed:29420262). {ECO:0000269|PubMed:18042453, ECO:0000269|PubMed:20080746, ECO:0000269|PubMed:29420262}. PTM: Ubiquitinated by SCF(FBXW11) E3 ubiquitin-protein ligase complex. Ubiquitination induces proteasomal degradation. {ECO:0000269|PubMed:29420262}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18042453, ECO:0000269|PubMed:29420262}; Peripheral membrane protein {ECO:0000269|PubMed:18042453}. Cytoplasm, cytosol {ECO:0000269|PubMed:18042453, ECO:0000269|PubMed:29420262}. Cell junction, tight junction {ECO:0000269|PubMed:20080746}. Cell junction, adherens junction {ECO:0000269|PubMed:20080746}. Note=Colocalized with TJP1 during epithelial polarization (PubMed:20080746). {ECO:0000269|PubMed:20080746}. SUBUNIT: Interacts with TRIM23 and CYTIP (By similarity). Interacts (via coiled-coil domain) with FRMD4A (via coiled-coil domain)(PubMed:20080746). Interacts with FRMD4B (PubMed:20080746). Found in a complex with PARD3, CYTH1 and FRMD4A (PubMed:20080746). Interacts (via N-terminal domain) with INAVA (via N-terminal domain) (By similarity). {ECO:0000250|UniProtKB:Q15438, ECO:0000269|PubMed:20080746}. DOMAIN: Binds via its PH domain to the inositol head group of phosphatidylinositol 3,4,5-trisphosphate. {ECO:0000250}.; DOMAIN: Autoinhibited by its C-terminal basic region. {ECO:0000269|PubMed:18042453}. TISSUE SPECIFICITY: Expressed in colon and small intestine (at protein level). {ECO:0000269|PubMed:29420262}. +Q80TQ2 CYLD_MOUSE Ubiquitin carboxyl-terminal hydrolase CYLD (EC 3.4.19.12) (Deubiquitinating enzyme CYLD) (Ubiquitin thioesterase CYLD) (Ubiquitin-specific-processing protease CYLD) 952 106,586 Active site (2); Alternative sequence (3); Chain (1); Domain (4); Erroneous initiation (1); Metal binding (8); Modified residue (3); Region (4); Sequence conflict (1) FUNCTION: Deubiquitinase that specifically cleaves 'Lys-63'- and linear 'Met-1'-linked polyubiquitin chains and is involved in NF-kappa-B activation and TNF-alpha-induced necroptosis (PubMed:17548520, PubMed:28701375, PubMed:29291351). Plays an important role in the regulation of pathways leading to NF-kappa-B activation (PubMed:16713561). Contributes to the regulation of cell survival, proliferation and differentiation via its effects on NF-kappa-B activation (PubMed:16713561). Negative regulator of Wnt signaling. Inhibits HDAC6 and thereby promotes acetylation of alpha-tubulin and stabilization of microtubules (PubMed:19893491). Plays a role in the regulation of microtubule dynamics, and thereby contributes to the regulation of cell proliferation, cell polarization, cell migration, and angiogenesis (PubMed:16713561, PubMed:20194890, PubMed:19893491). Required for normal cell cycle progress and normal cytokinesis (PubMed:19893491). Inhibits nuclear translocation of NF-kappa-B (By similarity). Plays a role in the regulation of inflammation and the innate immune response, via its effects on NF-kappa-B activation (By similarity). Dispensable for the maturation of intrathymic natural killer cells, but required for the continued survival of immature natural killer cells (PubMed:16501569, PubMed:18643924). Negatively regulates TNFRSF11A signaling and osteoclastogenesis (PubMed:18382763). Involved in the regulation of ciliogenesis, allowing ciliary basal bodies to migrate and dock to the plasma membrane; this process does not depend on NF-kappa-B activation (PubMed:25134987). Ability to remove linear ('Met-1'-linked) polyubiquitin chains regulates innate immunity and TNF-alpha-induced necroptosis: recruited to the LUBAC complex via interaction with SPATA2 and restricts linear polyubiquitin formation on target proteins (PubMed:28701375). Regulates innate immunity by restricting linear polyubiquitin formation on RIPK2 in response to NOD2 stimulation (By similarity). Involved in TNF-alpha-induced necroptosis by removing linear ('Met-1'-linked) polyubiquitin chains from RIPK1, thereby regulating the kinase activity of RIPK1 (PubMed:28701375). Removes 'Lys-63' linked polyubiquitin chain of MAP3K7, which inhibits phosphorylation and blocks downstream activation of the JNK-p38 kinase cascades (PubMed:17548520, PubMed:29291351). {ECO:0000250|UniProtKB:Q9NQC7, ECO:0000269|PubMed:16501569, ECO:0000269|PubMed:16713561, ECO:0000269|PubMed:17548520, ECO:0000269|PubMed:18382763, ECO:0000269|PubMed:18643924, ECO:0000269|PubMed:19893491, ECO:0000269|PubMed:20194890, ECO:0000269|PubMed:25134987, ECO:0000269|PubMed:28701375, ECO:0000269|PubMed:29291351}. PTM: Phosphorylated on several serine residues by IKKA and/or IKKB in response to immune stimuli. Phosphorylation requires IKBKG. Phosphorylation abolishes TRAF2 deubiquitination, interferes with the activation of Jun kinases, and strongly reduces CD40-dependent gene activation by NF-kappa-B (By similarity). {ECO:0000250}.; PTM: Ubiquitinated. Polyubiquitinated in hepatocytes treated with palmitic acid. Ubiquitination is mediated by E3 ligase TRIM47 and leads to proteasomal degradation. {ECO:0000269|PubMed:29291351}. SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region. Cytoplasm, cytoskeleton. Cell membrane {ECO:0000250|UniProtKB:Q9NQC7}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9NQC7}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9NQC7}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9NQC7}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9NQC7}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:25134987}. Note=Detected at the microtubule cytoskeleton during interphase (By similarity). Detected at the midbody during telophase (By similarity). During metaphase, it remains localized to the centrosome but is also present along the spindle (By similarity). {ECO:0000250|UniProtKB:Q9NQC7, ECO:0000269|PubMed:25134987}. SUBUNIT: Interacts (via CAP-Gly domain) with IKBKG/NEMO (via proline-rich C-terminal region) (By similarity). Interacts with TRAF2 and TRIP (By similarity). Interacts with PLK1, DVL1, DVL3, MAVS, TBK1, IKKE and DDX58 (By similarity). Interacts (via CAP-Gly domain) with microtubules (PubMed:19893491). Interacts with HDAC6 and BCL3 (PubMed:16713561, PubMed:19893491). Interacts with MAP3K7 (PubMed:17548520). Identified in a complex with TRAF6 and SQSTM1 (PubMed:18382763). Interacts with CEP350 (By similarity). Interacts with RNF31; the interaction is indirect and is mediated via SPATA2 (By similarity). Interacts with SPATA2 (via the PUB domain); the interaction is direct and recruits CYLD to the LUBAC complex, thereby regulating TNF-alpha-induced necroptosis (By similarity). {ECO:0000250|UniProtKB:Q9NQC7, ECO:0000269|PubMed:16713561, ECO:0000269|PubMed:17548520, ECO:0000269|PubMed:18382763, ECO:0000269|PubMed:19893491}. +Q2KN98 CYTSA_MOUSE Cytospin-A (SPECC1-like protein) (Sperm antigen with calponin homology and coiled-coil domains 1-like) 1118 124,488 Chain (1); Coiled coil (3); Compositional bias (2); Domain (1); Erroneous initiation (1); Modified residue (6) FUNCTION: Involved in cytokinesis and spindle organization. May play a role in actin cytoskeleton organization and microtubule stabilization and hence required for proper cell adhesion and migration (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:21703590}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Cell junction, gap junction {ECO:0000250}. Note=Colocalizes with beta-tubulin, acetylated alpha-tubulin and F-actin. Also observed in a ring around gamma-tubulin containing centrioles possibly in the microtubule organizing center (By similarity). {ECO:0000250}. SUBUNIT: May interact with both microtubules and actin cytoskeleton. +Q8K353 CYTM1_MOUSE Cysteine-rich and transmembrane domain-containing protein 1 104 11,402 Chain (1); Compositional bias (2); Sequence conflict (1); Transmembrane (1) TRANSMEM 81 98 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q9QYB2 DACH1_MOUSE Dachshund homolog 1 (Dach1) 751 77,972 Alternative sequence (1); Chain (1); Coiled coil (1); Compositional bias (5); Erroneous initiation (1); Modified residue (1); Region (4); Sequence conflict (4) FUNCTION: Transcription factor that is involved in regulation of organogenesis. Seems to be a regulator of SIX1, SIX6 and probably SIX5. Corepression of precursor cell proliferation in myoblasts by SIX1 is switched to coactivation through recruitment of EYA3 to the SIX1-DACH1 complex. Transcriptional activation seems also to involve association of CREBBP. Seems to act as a corepressor of SIX6 in regulating proliferation by directly repressing cyclin-dependent kinase inhibitors, including the p27Kip1 promoter. Inhibits TGF-beta signaling through interaction with SMAD4 and NCOR1 (By similarity). Binds to chromatin DNA via its DACHbox-N domain. {ECO:0000250, ECO:0000269|PubMed:12130660, ECO:0000269|PubMed:12215533, ECO:0000269|PubMed:14628042}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with SIX1, SIX6 and EYA3. Interacts with NCOR1 and HDAC3 through its N-terminus. Interacts with SIN3A through its C-terminus. Interacts with SMAD3 and SMAD4 (By similarity). {ECO:0000250}. DOMAIN: The DACHbox-N/DD1 domain forms a structure containing a DNA binding motif similar to that of the forkhead/winged helix domain. {ECO:0000250}. TISSUE SPECIFICITY: Expressed at higher levels in adult kidney and lung, and at lower levels in brain and testis. Expressed in embryonal kidneys, eyes, cochleae and limb buds. {ECO:0000269|PubMed:10502110, ECO:0000269|PubMed:11543628}. +Q8CBW4 DC121_MOUSE DDB1- and CUL4-associated factor 12-like protein 1 (WD repeat-containing protein 40B) 501 54,366 Chain (1); Frameshift (1); Repeat (4); Sequence conflict (6) +Q8BGW4 DC122_MOUSE DDB1- and CUL4-associated factor 12-like protein 2 (WD repeat-containing protein 40C) 469 51,623 Chain (1); Repeat (4) +O88485 DC1I1_MOUSE Cytoplasmic dynein 1 intermediate chain 1 (Cytoplasmic dynein intermediate chain 1) (Dynein intermediate chain 1, cytosolic) (DH IC-1) 628 70,725 Alternative sequence (1); Chain (1); Initiator methionine (1); Modified residue (11); Mutagenesis (6); Region (1); Repeat (7); Sequence conflict (4) FUNCTION: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. The intermediate chains mediate the binding of dynein to dynactin via its 150 kDa component (p150-glued) DCNT1. May play a role in mediating the interaction of cytoplasmic dynein with membranous organelles and kinetochores. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. SUBUNIT: Homodimer (By similarity). The cytoplasmic dynein 1 complex consists of two catalytic heavy chains (HCs) and a number of non-catalytic subunits presented by intermediate chains (ICs), light intermediate chains (LICs) and light chains (LCs); the composition seems to vary in respect to the IC, LIC and LC composition. The heavy chain homodimer serves as a scaffold for the probable homodimeric assembly of the respective non-catalytic subunits. The ICs and LICs bind directly to the HC dimer and the LCs assemble on the IC dimer. Interacts with DYNC1H1. Interacts with DYNLT1 and DYNLT3. Interacts with DCNT1 (By similarity). Interacts with DYNLL2. {ECO:0000250, ECO:0000269|PubMed:11148209}. +P43346 DCK_MOUSE Deoxycytidine kinase (dCK) (EC 2.7.1.74) 260 30,367 Active site (1); Binding site (6); Chain (1); Modified residue (4); Nucleotide binding (3) FUNCTION: Required for the phosphorylation of the deoxyribonucleosides deoxycytidine (dC), deoxyguanosine (dG) and deoxyadenosine (dA). PTM: Phosphorylated and activated in vitro upon phosphorylation at Ser-74 by CSNK1D/CK1. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Homodimer. +P00860 DCOR_MOUSE Ornithine decarboxylase (ODC) (EC 4.1.1.17) 461 51,177 Active site (1); Beta strand (21); Binding site (4); Chain (1); Helix (18); Modified residue (3); Mutagenesis (2); Region (2); Sequence conflict (7); Site (1); Turn (1) Amine and polyamine biosynthesis; putrescine biosynthesis via L-ornithine pathway; putrescine from L-ornithine: step 1/1. FUNCTION: Catalyzes the first and rate-limiting step of polyamine biosynthesis that converts ornithine into putrescine, which is the precursor for the polyamines, spermidine and spermine. Polyamines are essential for cell proliferation and are implicated in cellular processes, ranging from DNA replication to apoptosis. {ECO:0000269|PubMed:18973822, ECO:0000269|PubMed:24967154}. SUBUNIT: Homodimer. Only the dimer is catalytically active, as the active sites are constructed of residues from both monomers (PubMed:8106349, PubMed:10378276). Does not form a heterodimer with AZIN2 (PubMed:24967154). {ECO:0000269|PubMed:10378276, ECO:0000269|PubMed:24967154, ECO:0000269|PubMed:8106349}. TISSUE SPECIFICITY: Expressed during testis development in the outer part of the seminiferous tubules. {ECO:0000269|PubMed:18973822}. +Q8K4J0 DCR1C_MOUSE Protein artemis (mArt) (EC 3.1.-.-) (DNA cross-link repair 1C protein) (SNM1-like protein) 705 78,834 Alternative sequence (4); Chain (1); Modified residue (3); Sequence conflict (6) FUNCTION: Required for V(D)J recombination, the process by which exons encoding the antigen-binding domains of immunoglobulins and T-cell receptor proteins are assembled from individual V, (D), and J gene segments. V(D)J recombination is initiated by the lymphoid specific RAG endonuclease complex, which generates site specific DNA double strand breaks (DSBs). These DSBs present two types of DNA end structures: hairpin sealed coding ends and phosphorylated blunt signal ends. These ends are independently repaired by the non homologous end joining (NHEJ) pathway to form coding and signal joints respectively. This protein likely exhibits single-strand specific 5'-3' exonuclease activity in isolation, and may acquire endonucleolytic activity on 5' and 3' hairpins and overhangs when in a complex with PRKDC. The latter activity may be required specifically for the resolution of closed hairpins prior to the formation of the coding joint. May also be required for the repair of complex DSBs induced by ionizing radiation, which require substantial end-processing prior to religation by NHEJ. {ECO:0000269|PubMed:12504013, ECO:0000269|PubMed:12615897, ECO:0000269|PubMed:15699179}. PTM: Phosphorylation on undefined residues by PRKDC may stimulate endonucleolytic activity on 5' and 3' hairpins and overhangs. PRKDC must remain present, even after phosphorylation, for efficient hairpin opening. Also phosphorylated by ATM in response to ionizing radiation (IR) and by ATR in response to ultraviolet (UV) radiation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with ATM, BRCA1, PRKDC and TP53BP1. Also exhibits ATM- and phosphorylation-dependent interaction with the MRN complex, composed of MRE11, RAD50, and NBN (By similarity). {ECO:0000250}. +Q80WW9 DDRGK_MOUSE DDRGK domain-containing protein 1 (UFM1-binding and PCI domain-containing protein 1) 315 35,977 Beta strand (4); Chain (1); Cross-link (1); Domain (1); Erroneous initiation (1); Helix (3); Modified residue (1); Region (3); Signal peptide (1) FUNCTION: Protein which interacts with the E3 UFM1-protein ligase UFL1 and one of its substrates TRIP4 and is required for TRIP4 ufmylation. Through TRIP4 ufmylation may regulate nuclear receptors-mediated transcription. May play a role in NF-kappa-B-mediated transcription through regulation of the phosphorylation and the degradation of NFKBIA, the inhibitor of NF-kappa-B (By similarity). May also play a role in the cellular response to endoplasmic reticulum stress (PubMed:21494687). Plays a role in cartilage development through SOX9, inhibiting the ubiquitin-mediated proteasomal degradation of this transcriptional regulator (PubMed:28263186). {ECO:0000250|UniProtKB:Q96HY6, ECO:0000269|PubMed:21494687, ECO:0000269|PubMed:28263186}. PTM: Ufmylated. Conjugated to ubiquitin-like protein UFM1, probably at Lys-268. {ECO:0000269|PubMed:21494687}.; PTM: Ubiquitinated. Ubiquitination probably triggers proteasomal degradation and is negatively regulated by UFL1, the enzyme involved in the ufmylation of DDRGK1. {ECO:0000250|UniProtKB:Q96HY6}. SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:21494687}. SUBUNIT: Interacts with TRIP4; the interaction with TRIP4 is direct. Interacts with UFL1. Interacts with NFKBIA. Interacts with CDK5RAP3. Interacts with SOX9. {ECO:0000250|UniProtKB:Q96HY6}. TISSUE SPECIFICITY: Ubiquitously expressed (PubMed:20228063). Higher expression in pancreatic islets, pancreatic acini and testis (at protein level) (PubMed:21494687). {ECO:0000269|PubMed:20228063, ECO:0000269|PubMed:21494687}. +Q8VHX6 FLNC_MOUSE Filamin-C (FLN-C) (ABP-280-like protein) (ABP-L) (Actin-binding-like protein) (Filamin-2) (Gamma-filamin) 2726 291,119 Alternative sequence (1); Chain (1); Domain (2); Modified residue (14); Region (6); Repeat (24); Sequence conflict (8) FUNCTION: Muscle-specific filamin, which plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. May be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. Critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. {ECO:0000269|PubMed:16914736}. PTM: Ubiquitinated by FBXL22, leading to proteasomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250}. Note=A small amount localizes at membranes. In striated muscle cells, it predominantly localizes in myofibrillar Z lines, while a minor fraction localizes with subsarcolemme (By similarity). Targeting to developing and mature Z lines is mediated by the intradomain insert (By similarity). {ECO:0000250}. SUBUNIT: Homodimer; the filamin repeat 24 and the second hinge domain are important for dimer formation (By similarity). Interacts with FLNB, INPPL1, ITGB1A, KCND2, MYOT, MYOZ1 and MYOZ3. Interacts with sarcoglycans SGCD and SGCG. Interacts (via filament repeats 17-18, 20-21 and 24) with USP25 (isoform USP25m only). Interacts with FBLIM1 (By similarity). Interacts with XIRP1; this interaction is mediated by filamin 20 repeat (By similarity). Interacts with KY. Interacts with IGFN1. Interacts with MICALL2. Interacts with ANK3. Interacts with MICALL2 (By similarity). Interacts with ANK3. Interacts with SYNPO2 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q14315}. +Q61656 DDX5_MOUSE Probable ATP-dependent RNA helicase DDX5 (EC 3.6.4.13) (DEAD box RNA helicase DEAD1) (mDEAD1) (DEAD box protein 5) (RNA helicase p68) 614 69,290 Binding site (1); Chain (1); Cross-link (14); Domain (2); Modified residue (8); Motif (2); Nucleotide binding (2); Region (1); Sequence conflict (4) FUNCTION: Involved in the alternative regulation of pre-mRNA splicing; its RNA helicase activity is necessary for increasing tau exon 10 inclusion and occurs in a RBM4-dependent manner. Binds to the tau pre-mRNA in the stem-loop region downstream of exon 10. The rate of ATP hydrolysis is highly stimulated by single-stranded RNA. Involved in transcriptional regulation; the function is independent of the RNA helicase activity. Transcriptional coactivator for androgen receptor AR but probably not ESR1. Synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and involved in skeletal muscle differentiation. Transcriptional coactivator for p53/TP53 and involved in p53/TP53 transcriptional response to DNA damage and p53/TP53-dependent apoptosis. Transcriptional coactivator for RUNX2 and involved in regulation of osteoblast differentiation. Acts as transcriptional repressor in a promoter-specific manner; the function probably involves association with histone deacetylases, such as HDAC1. As component of a large PER complex is involved in the inhibition of 3' transcriptional termination of circadian target genes such as PER1 and NR1D1 and the control of the circadian rhythms. {ECO:0000269|PubMed:17011493, ECO:0000269|PubMed:17960593, ECO:0000269|PubMed:22767893}. PTM: Sumoylated; sumoylation, promoted by PIAS1, promotes interaction with HDAC1 and transcriptional repression activity. Sumoylation also significantly increases stability, and reduces polyubiquitination (By similarity). {ECO:0000250}.; PTM: Polyubiquitinated, leading to proteasomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. SUBUNIT: Identified in the spliceosome C complex. Interacts with RBM4; the interaction occurs in an RNA-independent manner. Interacts with AGO1 and AGO2. Interacts with ESR1, AR, EP300, CREBBP, POLR2A, TP53, RUNX2 and HDAC1. Self-associates. Interacts with DDX17. Interacts with BRDT. The large PER complex involved in the repression of transcriptional termination is composed of at least PER2, CDK9, DDX5, DHX9, NCBP1 and POLR2A (active). Interacts with DHX36; this interaction occurs in a RNA-dependent manner (By similarity). {ECO:0000250|UniProtKB:P17844, ECO:0000269|PubMed:22570411, ECO:0000269|PubMed:22767893}. +Q91V70 DEFB7_MOUSE Beta-defensin 7 (BD-7) (mBD-7) (mBD7) (Defensin, beta 7) 71 8,292 Beta strand (4); Disulfide bond (3); Helix (1); Modified residue (1); Peptide (1); Propeptide (1); Signal peptide (1) FUNCTION: Has bactericidal activity. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q99J78 DEFI8_MOUSE Differentially expressed in FDCP 8 (DEF-8) 448 52,311 Alternative sequence (1); Chain (1); Erroneous initiation (1); Frameshift (1); Modified residue (1); Sequence conflict (7); Zinc finger (2) FUNCTION: Positively regulates lysosome peripheral distribution and ruffled border formation in osteoclasts (PubMed:27777970). Involved in bone resorption (PubMed:27777970). {ECO:0000269|PubMed:27777970}. SUBUNIT: Interacts (via C-terminus) with PLEKHM1; this interaction is weak but increased in a RAB7A-dependent manner (PubMed:27777970). {ECO:0000269|PubMed:27777970}. TISSUE SPECIFICITY: Abundantly expressed in peripheral blood leukocytes. Highly expressed in B-cells. Also present in lymph node and appendix. Down-regulated upon macrophage/granulocyte differentiation. Weakly expressed in bone marrow and spleen. Weakly or not expressed in thymus and fetal liver. {ECO:0000269|PubMed:10460589}. +Q6PGN3 DCLK2_MOUSE Serine/threonine-protein kinase DCLK2 (EC 2.7.11.1) (CaMK-like CREB regulatory kinase 2) (CL2) (CLICK-II) (CLICK2) (Doublecortin-like and CAM kinase-like 2) (Doublecortin-like kinase 2) 756 82,979 Active site (1); Alternative sequence (6); Binding site (1); Chain (1); Compositional bias (2); Domain (3); Modified residue (4); Mutagenesis (1); Nucleotide binding (1); Sequence conflict (1) FUNCTION: Protein kinase with a significantly reduced Ca(2+)+/CAM affinity and dependence compared to other members of the CaMK family. May play a role in the down-regulation of CRE-dependent gene activation probably by phosphorylation of the CREB coactivator CRTC2/TORC2 and the resulting retention of TORC2 in the cytoplasm. {ECO:0000269|PubMed:16684769}. PTM: Autophosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16628014, ECO:0000269|PubMed:16684769}. Note=Colocalizes with microtubules. SUBUNIT: Binds to and stabilizes microtubules (By similarity). Interacts with MAPK8IP1/JIP-1, MAPK8IP2/JIP-2, MAPK9/JNK2, PPP1R9B/NEURABIN-2 and actin. {ECO:0000250, ECO:0000269|PubMed:16628014}. DOMAIN: The doublecortin domains are involved in the colocalization with microtubules. TISSUE SPECIFICITY: Expressed in the central and peripheral nervous system including the brain, spinal cord, cranial and dorsal root ganglia and in the parasympathetic ganglia. Present in neurons, but not in glial cells, in most forebrain areas. Strong expression in the hippocampal CA1 pyramidal cell layer. Expressed in the photoreceptor sensory cilium complex and in eyes. Also detected in individual cells of the olfactory epithelium. {ECO:0000269|PubMed:16684769, ECO:0000269|PubMed:16869982, ECO:0000269|PubMed:18075264, ECO:0000269|PubMed:19342486}. +Q61496 DDX4_MOUSE ATP-dependent RNA helicase DDX4 (EC 3.6.4.13) (DEAD box protein 4) (Mvh) (Vasa homolog) 702 76,470 Chain (1); Compositional bias (1); Domain (2); Modified residue (3); Motif (2); Mutagenesis (1); Nucleotide binding (1); Region (1); Sequence conflict (13) FUNCTION: ATP-dependent RNA helicase required during spermatogenesis to repress transposable elements and preventing their mobilization, which is essential for the germline integrity (PubMed:20439430, PubMed:28633017). Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons (PubMed:20439430, PubMed:28633017). Involved in the secondary piRNAs metabolic process, the production of piRNAs in fetal male germ cells through a ping-pong amplification cycle (PubMed:20439430, PubMed:28633017). Required for PIWIL2 slicing-triggered piRNA biogenesis: helicase activity enables utilization of one of the slice cleavage fragments generated by PIWIL2 and processing these pre-piRNAs into piRNAs (PubMed:28633017). {ECO:0000269|PubMed:20439430, ECO:0000269|PubMed:28633017}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20439430, ECO:0000269|PubMed:22900038}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:22900038}. Note=Component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis. {ECO:0000269|PubMed:20439430}. SUBUNIT: Found in a mRNP complex, at least composed of TDRD1, TDRD6, TDRD7 and DDX4 (PubMed:17141210). Interacts with RANBP9 (PubMed:14648869, PubMed:27622290). Interacts with RANBP10 (PubMed:27622290). Interacts with PIWIL2 and MAEL (PubMed:14736746, PubMed:16787967). Interacts with ARNTL/BMAL1 and CLOCK (PubMed:22900038). Interacts with Tex19.1 and, probably, Tex19.2 (PubMed:28254886). {ECO:0000269|PubMed:14648869, ECO:0000269|PubMed:14736746, ECO:0000269|PubMed:16787967, ECO:0000269|PubMed:17141210, ECO:0000269|PubMed:22900038, ECO:0000269|PubMed:27622290, ECO:0000269|PubMed:28254886}. TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:22900038}. +Q6ZPL9 DDX55_MOUSE ATP-dependent RNA helicase DDX55 (EC 3.6.4.13) (DEAD box protein 55) 600 68,465 Chain (1); Compositional bias (1); Domain (2); Erroneous initiation (2); Modified residue (2); Motif (2); Nucleotide binding (1); Sequence conflict (2) FUNCTION: Probable ATP-binding RNA helicase. DOMAIN: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis. +Q9D0R4 DDX56_MOUSE Probable ATP-dependent RNA helicase DDX56 (EC 3.6.4.13) (ATP-dependent 61 kDa nucleolar RNA helicase) (DEAD box protein 56) 546 61,212 Chain (1); Domain (2); Modified residue (2); Motif (2); Nucleotide binding (1) FUNCTION: May play a role in later stages of the processing of the pre-ribosomal particles leading to mature 60S ribosomal subunits. Has intrinsic ATPase activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. SUBUNIT: May form homooligomeric complexes. +Q810A7 DDX42_MOUSE ATP-dependent RNA helicase DDX42 (EC 3.6.4.13) (DEAD box protein 42) 929 101,965 Alternative sequence (1); Chain (1); Coiled coil (1); Compositional bias (5); Cross-link (1); Domain (2); Erroneous initiation (1); Modified residue (8); Motif (2); Nucleotide binding (1); Region (1); Sequence conflict (3) FUNCTION: ATP-dependent RNA helicase. Binds to partially double-stranded RNAs (dsRNAs) in order to unwind RNA secondary structures. Unwinding is promoted in the presence of single-strand binding proteins. Mediates also RNA duplex formation thereby displacing the single-strand RNA binding protein. ATP and ADP modulate its activity: ATP binding and hydrolysis by DDX42 triggers RNA strand separation, whereas the ADP-bound form of the protein triggers annealing of complementary RNA strands. Involved in the survival of cells by interacting with TP53BP2 and thereby counteracting the apoptosis-stimulating activity of TP53BP2. Relocalizes TP53BP2 to the cytoplasm (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus speckle {ECO:0000250}. Nucleus, Cajal body {ECO:0000250}. SUBUNIT: Component of splicing factor SF3B complex which is composed of at least eight subunits; SF3B1, SF3B2, SF3B3, SF3B4, SF3B5, SF3B6, PHF5A/SF3B14B, and DDX42/SF3B125. Interacts (via the C-terminus) with TP53BP2; the interaction is not inhibitied by TP53BP2 ubiquitination and is independent of p53/TP53 (By similarity). {ECO:0000250}. +P82019 DEFB4_MOUSE Beta-defensin 4 (BD-4) (mBD-4) (Defensin, beta 4) 63 7,129 Disulfide bond (3); Modified residue (1); Natural variant (1); Peptide (1); Signal peptide (1) FUNCTION: Exhibits antimicrobial activity against Gram-negative bacteria and Gram-positive bacteria. May act as a ligand for C-C chemokine receptor CCR6. Can bind to mouse (but not human) CCR6 and induce chemotactic activity of CCR6-expressing cells (PubMed:20068036). {ECO:0000269|PubMed:20068036}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. TISSUE SPECIFICITY: Tongue, esophagus and trachea. {ECO:0000269|PubMed:10922379}. +P11477 DEFA1_MOUSE Alpha-defensin 1 (Cryptdin-1) (Defensin-related cryptdin peptide) 93 10,461 Disulfide bond (3); Peptide (1); Propeptide (1); Sequence conflict (4); Signal peptide (1) FUNCTION: Probably contributes to the antimicrobial barrier function of the small bowel mucosa. Has antibacterial activity against attenuated mutants of S.typhimurium. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Paneth cells of the small bowel. +Q91V82 DEFB8_MOUSE Beta-defensin 8 (BD-8) (mBD-8) (Defensin, beta 8) (Defensin-related peptide) (Defr1) 60 6,760 Beta strand (3); Disulfide bond (3); Helix (1); Peptide (1); Propeptide (1); Sequence conflict (2); Signal peptide (1) FUNCTION: A synthetic peptide displays antimicrobial activities against S.aureus, P.aeruginosa, E.coli and B.cepacia. The antimicrobial activity against S.aureus, E.coli and B.cepacia is reduced in raised concentration of NaCl, but its action against P.aeruginosa is independent of NaCl concentration. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. TISSUE SPECIFICITY: Most highly expressed in testis and heart. +P28310 DEFA3_MOUSE Alpha-defensin 3 (Defensin-related cryptdin-3) 93 10,528 Disulfide bond (3); Peptide (1); Propeptide (1); Signal peptide (1) FUNCTION: Probably contributes to the antimicrobial barrier function of the small bowel mucosa. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Paneth cells of the small bowel. +Q9WV69 DEMA_MOUSE Dematin (Dematin actin-binding protein) (Erythrocyte membrane protein band 4.9) 405 45,468 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (1); Modified residue (19); Region (1) FUNCTION: Membrane-cytoskeleton-associated protein with F-actin-binding activity that induces F-actin bundles formation and stabilization. Its F-actin-bundling activity is reversibly regulated upon its phosphorylation by the cAMP-dependent protein kinase A (PKA). Binds to the erythrocyte membrane glucose transporter-1 SLC2A1/GLUT1, and hence stabilizes and attaches the spectrin-actin network to the erythrocytic plasma membrane. Plays a role in maintaining the functional integrity of PKA-activated erythrocyte shape and the membrane mechanical properties. Plays also a role as a modulator of actin dynamics in fibroblasts; acts as negative regulator of the RhoA activation pathway. In platelets, functions as a regulator of internal calcium mobilization across the dense tubular system that affects platelet granule secretion pathways and aggregation. Also required for the formation of a diverse set of cell protrusions, such as filopodia and lamellipodia, necessary for platelet cell spreading, motility and migration. Acts as a tumor suppressor and inhibits malignant cell transformation. {ECO:0000269|PubMed:12011427, ECO:0000269|PubMed:18505823, ECO:0000269|PubMed:23060452}. PTM: Phosphorylated. Phosphorylation at Ser-403 by PKA causes the C-terminal headpiece domain to associate with the N-terminal core domain, and leads to the inhibition of its actin bundling activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytosol {ECO:0000269|PubMed:18505823}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:18505823}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000250}. Membrane {ECO:0000269|PubMed:18505823}. Endomembrane system {ECO:0000250}. Cell projection {ECO:0000269|PubMed:18505823}. Note=Localized at the spectrin-actin junction of erythrocyte plasma membrane. Localized to intracellular membranes and the cytoskeletal network. Localized at intracellular membrane-bounded organelle compartment in platelets that likely represent the dense tubular network membrane (By similarity). {ECO:0000250}. SUBUNIT: Monomeric (isoform 2); under reducing conditions. Self-associates. Exists under oxidizing condition as a trimer of two isoforms 2 and isoform 1 linked by disulfide bonds (Probable). Found in a complex with DMTN, F-actin and spectrin. Found in a complex with ADD2, DMTN and SLC2A1. Interacts with F-actin, ITPKB and spectrin. Isoform 2 interacts with SLC2A1 (via C-terminus cytoplasmic region) (By similarity). Interacts with RASGRF2. {ECO:0000250, ECO:0000269|PubMed:11856323, ECO:0000269|PubMed:12011427, ECO:0000305}. DOMAIN: Both the N-terminal core domain and the C-terminal headpiece domain are sufficient for binding to F-actin and necessary for actin bundling activity. TISSUE SPECIFICITY: Expressed in platelets. Isoform 1 and isoform 2 are expressed in mature erythrocytes (at protein level). {ECO:0000269|PubMed:12011427, ECO:0000269|PubMed:23060452}. +Q3U1T9 DEN1B_MOUSE DENN domain-containing protein 1B (Connecdenn 2) 766 85,526 Alternative sequence (5); Chain (1); Domain (3); Modified residue (7); Motif (2); Mutagenesis (3) FUNCTION: Guanine nucleotide exchange factor (GEF) for RAB35 that acts as a regulator of T-cell receptor (TCR) internalization in TH2 cells. Acts by promoting the exchange of GDP to GTP, converting inactive GDP-bound RAB35 into its active GTP-bound form. Plays a role in clathrin-mediated endocytosis. Controls cytokine production in TH2 lymphocytes by controlling the rate of TCR internalization and routing to endosomes: acts by mediating clathrin-mediated endocytosis of TCR via its interaction with the adapter protein complex 2 (AP-2) and GEF activity. Dysregulation leads to impaired TCR down-modulation and recycling, affecting cytokine production in TH2 cells. {ECO:0000269|PubMed:26774822}. PTM: Phosphorylated on serine and/or threonine, possibly regulating the guanine nucleotide exchange factor (GEF) activity. {ECO:0000250|UniProtKB:Q6P3S1}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q6P3S1}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:Q6P3S1}. SUBUNIT: Interacts with RAB35 (PubMed:26774822). Interacts with clathrin heavy chain/CLTC (By similarity). Interacts with components of the adapter protein complex 2 (AP-2) AP2A2 and AP2B1 (By similarity). Interacts with CD3E (PubMed:26774822). {ECO:0000250|UniProtKB:Q6P3S1, ECO:0000269|PubMed:26774822}. DOMAIN: The FXDXF motif mediates interaction the AP-2 complex. {ECO:0000269|PubMed:26774822}.; DOMAIN: The clathrin box motif mediates interaction with clathrin. {ECO:0000269|PubMed:26774822}. TISSUE SPECIFICITY: Expressed in a subset of dendritic cells (DCs). {ECO:0000269|PubMed:26774822}. +Q9D291 DESI2_MOUSE Deubiquitinase DESI2 (EC 3.4.19.12) (Desumoylating isopeptidase 2) (DeSI-2) (PPPDE peptidase domain-containing protein 1) (Protein FAM152A) 194 21,434 Active site (2); Chain (1); Domain (1) FUNCTION: Has deubiquitinating activity towards 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. Deubiquitinates 'Lys-48'-linked polyubiquitination of RPS7 leading to its stabilization. {ECO:0000250|UniProtKB:Q9BSY9}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22370726}. SUBUNIT: Interacts with RPS7. {ECO:0000250|UniProtKB:Q9BSY9}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:22370726}. +Q9WUQ7 DEXI_MOUSE Dexamethasone-induced protein (Protein MYLE) 95 10,402 Chain (1) +Q8BVB5 DFB42_MOUSE Beta-defensin 42 (BD-42) (mBD-42) (Defensin, beta 42) 75 8,287 Chain (1); Disulfide bond (3); Signal peptide (1) FUNCTION: Has bactericidal activity (By similarity). May play a role in the antimicrobial protection of sperm and urogenital tract epithelia (PubMed:16023745). {ECO:0000250|UniProtKB:P81534, ECO:0000269|PubMed:16023745}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P60022}. TISSUE SPECIFICITY: Epididymis-specific, with highest levels in the initial segment and distal caput. {ECO:0000269|PubMed:16023745}. +P17534 DFAR2_MOUSE Alpha-defensin-related sequence 2 (CRS4C1) (Cryptdin-related protein 4C-1) (Defensin-related cryptdin-related sequence 2) 91 9,980 Peptide (1); Propeptide (1); Region (1); Repeat (7); Signal peptide (1) FUNCTION: Apparent precursor of a secreted, cationic, proline- and cysteine-rich peptide that contains Cys-Pro-Xaa repeats. Unlike cryptdin, the proposed mature peptide region lacks the structural motif characteristic of defensins. It may have microbicidal activities. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Small bowel, spleen, colon, kidney, liver, stomach and femur marrow. +Q30KP3 DFB20_MOUSE Beta-defensin 20 (BD-20) (mBD-20) (Defensin, beta 20) 96 11,039 Chain (1); Disulfide bond (3); Erroneous initiation (1); Signal peptide (1) FUNCTION: Has antibacterial activity. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +P50713 DFA15_MOUSE Alpha-defensin 15 (Defensin-related cryptdin-15) 93 10,503 Disulfide bond (3); Peptide (1); Propeptide (1); Signal peptide (1) FUNCTION: Probably contributes to the antimicrobial barrier function of the small bowel mucosa. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Paneth cells of the small bowel. +Q9Z2A7 DGAT1_MOUSE Diacylglycerol O-acyltransferase 1 (EC 2.3.1.20) (Acyl-CoA retinol O-fatty-acyltransferase) (ARAT) (Retinol O-fatty-acyltransferase) (EC 2.3.1.76) (Diglyceride acyltransferase) 498 56,790 Active site (1); Chain (1); Modified residue (1); Mutagenesis (1); Region (1); Topological domain (4); Transmembrane (3) TRANSMEM 97 118 Helical. {ECO:0000255}.; TRANSMEM 231 240 Helical. {ECO:0000255}.; TRANSMEM 242 250 Helical. {ECO:0000255}. TOPO_DOM 1 96 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 119 230 Lumenal. {ECO:0000255}.; TOPO_DOM 241 241 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 251 498 Lumenal. {ECO:0000255}. Lipid metabolism; glycerolipid metabolism. FUNCTION: Catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. In contrast to DGAT2 it is not essential for survival. May be involved in VLDL (very low density lipoprotein) assembly. In liver, plays a role in esterifying exogenous fatty acids to glycerol. Functions as the major acyl-CoA retinol acyltransferase (ARAT) in the skin, where it acts to maintain retinoid homeostasis and prevent retinoid toxicity leading to skin and hair disorders. {ECO:0000269|PubMed:19028692, ECO:0000269|PubMed:20876538, ECO:0000269|PubMed:22493088}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:20876538}; Multi-pass membrane protein {ECO:0000269|PubMed:20876538}. SUBUNIT: Homodimer or homotetramer. {ECO:0000269|PubMed:20876538}. +O35347 DGCR6_MOUSE Protein DGCR6 (DiGeorge syndrome critical region 6 homolog) 198 22,837 Alternative sequence (2); Chain (1); Coiled coil (1); Sequence conflict (1) FUNCTION: May have a role in early embryogenesis. TISSUE SPECIFICITY: Expressed in all the examined tissues with highest expression in testis. +Q9EQM6 DGCR8_MOUSE Microprocessor complex subunit DGCR8 (DiGeorge syndrome critical region 8 homolog) (Gy1) 773 86,321 Chain (1); Cross-link (3); Domain (3); Metal binding (1); Modified residue (8); Region (4); Sequence conflict (1) FUNCTION: Component of the microprocessor complex that acts as a RNA- and heme-binding protein that is involved in the initial step of microRNA (miRNA) biogenesis (PubMed:17259983). Component of the microprocessor complex that is required to process primary miRNA transcripts (pri-miRNAs) to release precursor miRNA (pre-miRNA) in the nucleus. Within the microprocessor complex, DGCR8 function as a molecular anchor necessary for the recognition of pri-miRNA at dsRNA-ssRNA junction and directs DROSHA to cleave 11 bp away form the junction to release hairpin-shaped pre-miRNAs that are subsequently cut by the cytoplasmic DICER to generate mature miRNAs. The heme-bound DGCR8 dimer binds pri-miRNAs as a cooperative trimer (of dimers) and is active in triggering pri-miRNA cleavage, whereas the heme-free DGCR8 monomer binds pri-miRNAs as a dimer and is much less active. Both double-stranded and single-stranded regions of a pri-miRNA are required for its binding. Specifically recognizes and binds N6-methyladenosine (m6A)-containing pri-miRNAs, a modification required for pri-miRNAs processing (By similarity). Involved in the silencing of embryonic stem cell self-renewal (PubMed:17259983). {ECO:0000250|UniProtKB:Q8WYQ5, ECO:0000269|PubMed:17259983}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8WYQ5}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q8WYQ5}. Note=Colocalizes with nucleolin and DROSHA in the nucleolus. Mostly detected in the nucleolus as electron-dense granular patches around the fibrillar center (FC) and granular component (GC). Also detected in the nucleoplasm as small foci adjacent to splicing speckles near the chromatin structure. Localized with DROSHA in GW bodies (GWBs), also known as P-bodies. {ECO:0000250|UniProtKB:Q8WYQ5}. SUBUNIT: Monomer; in absence of heme. Homodimer; the association with heme promotes its dimerization. Component of the microprocessor complex, or pri-miRNA processing protein complex, which is composed of DROSHA and DGCR8. The microprocessor complex is a heterotrimer; each of the two DROSHA RNase III domains binds one DGCR8 (via C-terminal region). Interacts with ILF3, NCL and DROSHA. {ECO:0000250|UniProtKB:Q8WYQ5}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:12705904}. +O88673 DGKA_MOUSE Diacylglycerol kinase alpha (DAG kinase alpha) (EC 2.7.1.107) (80 kDa diacylglycerol kinase) (Diglyceride kinase alpha) (DGK-alpha) 730 82,762 Calcium binding (2); Chain (1); Domain (3); Modified residue (1); Sequence conflict (3); Zinc finger (2) FUNCTION: Upon cell stimulation converts the second messenger diacylglycerol into phosphatidate, initiating the resynthesis of phosphatidylinositols and attenuating protein kinase C activity. {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. +Q6P5E8 DGKQ_MOUSE Diacylglycerol kinase theta (DAG kinase theta) (EC 2.7.1.107) (Diglyceride kinase theta) (DGK-theta) 934 102,254 Alternative sequence (1); Chain (1); Domain (2); Modified residue (2); Zinc finger (3) FUNCTION: Phosphorylates diacylglycerol (DAG) to generate phosphatidic acid (PA). May regulate the activity of protein kinase C by controlling the balance between these two signaling lipids. Activated in the nucleus in response to alpha-thrombin and nerve growth factor (By similarity). May be involved in cAMP-induced activation of NR5A1 and subsequent steroidogenic gene transcription by delivering PA as ligand for NR5A1. Acts synergistically with NR5A1 on CYP17 transcriptional activity (By similarity). {ECO:0000250}. PTM: Phosphorylated by PRKCE and PRKCH in vitro. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P52824}. Cell membrane {ECO:0000250|UniProtKB:P52824}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P52824}. Nucleus {ECO:0000250|UniProtKB:P52824}. Nucleus speckle {ECO:0000250|UniProtKB:P52824}. Note=Translocates to the nucleus in response to thrombin stimulation. Translocates to the plasma membrane in response to steroid hormone receptor stimulation. Translocation to the plasma membrane is dependent on G-protein coupled receptor stimulation and subsequent activation of PRKCE and probably PRKCH. {ECO:0000250|UniProtKB:P52824}. SUBUNIT: Interacts with RHOA (constitutively activated, GTP-bound); the interaction inhibits DGKQ. Interacts with PRKCE. Interacts with PRKCH. Interacts with PLCB1. Interacts with NR5A1 (By similarity). {ECO:0000250}. +O88455 DHCR7_MOUSE 7-dehydrocholesterol reductase (7-DHC reductase) (EC 1.3.1.21) (Sterol Delta(7)-reductase) 471 53,919 Binding site (6); Chain (1); Modified residue (1); Nucleotide binding (2); Transmembrane (9) TRANSMEM 36 56 Helical. {ECO:0000255}.; TRANSMEM 95 115 Helical. {ECO:0000255}.; TRANSMEM 144 164 Helical. {ECO:0000255}.; TRANSMEM 173 193 Helical. {ECO:0000255}.; TRANSMEM 233 253 Helical. {ECO:0000255}.; TRANSMEM 262 282 Helical. {ECO:0000255}.; TRANSMEM 302 322 Helical. {ECO:0000255}.; TRANSMEM 327 347 Helical. {ECO:0000255}.; TRANSMEM 416 436 Helical. {ECO:0000255}. Steroid biosynthesis; cholesterol biosynthesis. FUNCTION: Production of cholesterol by reduction of C7-C8 double bond of 7-dehydrocholesterol (7-DHC). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. +P26443 DHE3_MOUSE Glutamate dehydrogenase 1, mitochondrial (GDH 1) (EC 1.4.1.3) 558 61,337 Active site (1); Binding site (12); Chain (1); Modified residue (55); Nucleotide binding (1); Sequence conflict (1); Transit peptide (1) FUNCTION: Mitochondrial glutamate dehydrogenase that converts L-glutamate into alpha-ketoglutarate. Plays a key role in glutamine anaplerosis by producing alpha-ketoglutarate, an important intermediate in the tricarboxylic acid cycle. May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate. {ECO:0000269|PubMed:23663782}. PTM: Acetylation of Lys-84 is observed in liver mitochondria from fasted mice but not from fed mice.; PTM: ADP-ribosylated by SIRT4, leading to inactivate glutamate dehydrogenase activity. Stoichiometry shows that ADP-ribosylation occurs in one subunit per catalytically active homohexamer. SUBCELLULAR LOCATION: Mitochondrion matrix. SUBUNIT: Homohexamer. +Q99PU8 DHX30_MOUSE ATP-dependent RNA helicase DHX30 (EC 3.6.4.13) (DEAH box protein 30) 1217 136,668 Alternative sequence (2); Chain (1); Compositional bias (2); Domain (3); Modified residue (4); Motif (1); Nucleotide binding (1); Sequence conflict (13) FUNCTION: RNA-dependent helicase (PubMed:25219788). Plays an important role in the assembly of the mitochondrial large ribosomal subunit (By similarity). Required for optimal function of the zinc-finger antiviral protein ZC3HAV1 (By similarity). Associates with mitochondrial DNA (By similarity). Involved in nervous system development and differentiation through its involvement in the up-regulation of a number of genes which are required for neurogenesis, including GSC, NCAM1, neurogenin, and NEUROD (PubMed:25219788). {ECO:0000250|UniProtKB:Q5BJS0, ECO:0000250|UniProtKB:Q7L2E3, ECO:0000269|PubMed:25219788}. PTM: Isoform 3: Phosphorylated on Ser-15. {ECO:0000250|UniProtKB:Q7L2E3}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25219788}. Mitochondrion {ECO:0000250|UniProtKB:Q7L2E3}. Mitochondrion matrix, mitochondrion nucleoid {ECO:0000250|UniProtKB:Q7L2E3}. Note=Localizes to mitochondrial RNA granules found in close proximity to the mitochondrial nucleoids. Relocalizes to stress granules upon heat stress. {ECO:0000250|UniProtKB:Q7L2E3}. SUBUNIT: Identified in a complex with TFAM and SSBP1. Interacts (via N-terminus) with ZC3HAV1 (via N-terminal domain) in an RNA-independent manner. Found in a complex with GRSF1, DDX28, FASTKD2 and FASTKD5. {ECO:0000250|UniProtKB:Q5BJS0, ECO:0000250|UniProtKB:Q7L2E3}. TISSUE SPECIFICITY: Expressed in the heart, brain, spleen, lung, liver, skeletal muscle, kidney, and testis. Expression is strongest in the testis and brain, while the lowest levels of expression are found in the spleen and lung. {ECO:0000269|PubMed:25219788}. +Q9DBV3 DHX34_MOUSE Probable ATP-dependent RNA helicase DHX34 (EC 3.6.4.13) (DEAH box protein 34) 1145 128,507 Chain (1); Domain (2); Erroneous initiation (1); Modified residue (2); Motif (1); Nucleotide binding (1); Sequence conflict (6) FUNCTION: Probable ATP-binding RNA helicase. +Q58NB6 DHRS9_MOUSE Dehydrogenase/reductase SDR family member 9 (EC 1.1.-.-) (3-alpha hydroxysteroid dehydrogenase) (3-alpha-HSD) (Short-chain dehydrogenase/reductase retSDR8) 319 35,242 Active site (1); Binding site (3); Chain (1); Nucleotide binding (1); Sequence conflict (3); Signal peptide (1) FUNCTION: 3-alpha-hydroxysteroid dehydrogenase that converts 3-alpha-tetrahydroprogesterone (allopregnanolone) to dihydroxyprogesterone and 3-alpha-androstanediol to dihydroxyprogesterone. May play a role in the biosynthesis of retinoic acid from retinaldehyde, but seems to have low activity with retinoids. Can utilize both NADH and NADPH (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Microsome membrane {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}. Note=Associated with microsomal membranes. {ECO:0000250}. SUBUNIT: Homotetramer. {ECO:0000250}. +Q9QZD8 DIC_MOUSE Mitochondrial dicarboxylate carrier (Solute carrier family 25 member 10) 287 31,715 Chain (1); Modified residue (1); Repeat (3); Sequence conflict (3); Transmembrane (6) TRANSMEM 9 29 Helical; Name=1. {ECO:0000255}.; TRANSMEM 62 81 Helical; Name=2. {ECO:0000255}.; TRANSMEM 102 122 Helical; Name=3. {ECO:0000255}.; TRANSMEM 162 181 Helical; Name=4. {ECO:0000255}.; TRANSMEM 202 222 Helical; Name=5. {ECO:0000255}.; TRANSMEM 254 274 Helical; Name=6. {ECO:0000255}. FUNCTION: Involved in translocation of malonate, malate and succinate in exchange for phosphate, sulfate, sulfite or thiosulfate across mitochondrial inner membrane. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed at very high levels in white adipocytes. +Q5SXY1 CYTSB_MOUSE Cytospin-B (Sperm antigen with calponin homology and coiled-coil domains 1) 1067 118,101 Alternative sequence (3); Chain (1); Coiled coil (1); Compositional bias (1); Domain (1); Erroneous initiation (1); Initiator methionine (1); Lipidation (1); Modified residue (18); Sequence conflict (1) SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 4: Membrane {ECO:0000250|UniProtKB:Q5M775}; Lipid-anchor {ECO:0000250|UniProtKB:Q5M775}. +Q5M8N4 D39U1_MOUSE Epimerase family protein SDR39U1 (EC 1.1.1.-) (Short-chain dehydrogenase/reductase family 39U member 1) 308 32,995 Alternative sequence (1); Binding site (1); Chain (1); Nucleotide binding (3); Sequence conflict (1) FUNCTION: Putative NADP-dependent oxidoreductase. {ECO:0000250}. +Q8BHG2 CZIB_MOUSE CXXC motif containing zinc binding protein (UPF0587 protein C1orf123 homolog) 160 18,020 Alternative sequence (2); Chain (1); Metal binding (4); Modified residue (1); Sequence conflict (1) SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9NWV4}. DOMAIN: The N-terminal and the C-terminal half of the protein have a very similar 3D-structure, suggesting they arose from duplication. Requires a bound zinc ion for normal folding and solubility. {ECO:0000250|UniProtKB:Q9NWV4}. +Q91VY6 CYTIP_MOUSE Cytohesin-interacting protein (Cytohesin-binding protein HE) (Cbp HE) (Pleckstrin homology Sec7 and coiled-coil domains-binding protein) 359 40,143 Chain (1); Coiled coil (1); Compositional bias (1); Domain (1); Region (1); Sequence conflict (1) FUNCTION: By its binding to cytohesin-1 (CYTH1), it modifies activation of ARFs by CYTH1 and its precise function may be to sequester CYTH1 in the cytoplasm. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Early endosome {ECO:0000250}. Note=Recruited from the cytosol to endosomes by SNX27. {ECO:0000250}. SUBUNIT: Interacts with CYTH1 and SNX27. {ECO:0000250}. +Q71B07 D19L3_MOUSE Probable C-mannosyltransferase DPY19L3 (EC 2.4.1.-) (Dpy-19-like protein 3) (Protein dpy-19 homolog 3) 716 82,990 Chain (1); Compositional bias (1); Frameshift (1); Sequence conflict (6); Transmembrane (12) TRANSMEM 48 68 Helical. {ECO:0000255}.; TRANSMEM 156 174 Helical. {ECO:0000255}.; TRANSMEM 179 195 Helical. {ECO:0000255}.; TRANSMEM 215 235 Helical. {ECO:0000255}.; TRANSMEM 241 258 Helical. {ECO:0000255}.; TRANSMEM 270 292 Helical. {ECO:0000255}.; TRANSMEM 302 324 Helical. {ECO:0000255}.; TRANSMEM 341 361 Helical. {ECO:0000255}.; TRANSMEM 417 437 Helical. {ECO:0000255}.; TRANSMEM 461 481 Helical. {ECO:0000255}.; TRANSMEM 489 509 Helical. {ECO:0000255}.; TRANSMEM 520 540 Helical. {ECO:0000255}. FUNCTION: Probable C-mannosyltransferase that mediates C-mannosylation of tryptophan residues on target proteins. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +P61804 DAD1_MOUSE Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1 (Oligosaccharyl transferase subunit DAD1) (Defender against cell death 1) (DAD-1) 113 12,497 Chain (1); Initiator methionine (1); Modified residue (1); Sequence conflict (4); Topological domain (3); Transmembrane (3) TRANSMEM 31 51 Helical. {ECO:0000255}.; TRANSMEM 53 73 Helical. {ECO:0000255}.; TRANSMEM 93 113 Helical. {ECO:0000255}. TOPO_DOM 2 30 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 52 52 Lumenal. {ECO:0000255}.; TOPO_DOM 74 92 Cytoplasmic. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. {ECO:0000250|UniProtKB:E2R4X3}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Component of the oligosaccharyltransferase (OST) complex. OST exists in two different complex forms which contain common core subunits RPN1, RPN2, OST48, OST4, DAD1 and TMEM258, either STT3A or STT3B as catalytic subunits, and form-specific accessory subunits. STT3A complex assembly occurs through the formation of 3 subcomplexes. Subcomplex 1 contains RPN1 and TMEM258, subcomplex 2 contains the STT3A-specific subunits STT3A, DC2/OSTC, and KCP2 as well as the core subunit OST4, and subcomplex 3 contains RPN2, DAD1, and OST48. The STT3A complex can form stable complexes with the Sec61 complex or with both the Sec61 and TRAP complexes. {ECO:0000250|UniProtKB:E2R4X3}. +Q8R368 DAAF4_MOUSE Dynein assembly factor 4, axonemal (Dyslexia susceptibility 1 candidate gene 1 protein homolog) 420 48,125 Chain (1); Domain (1); Region (1); Repeat (3); Sequence conflict (2) FUNCTION: Involved in neuronal migration during development of the cerebral neocortex. May regulate the stability and proteasomal degradation of the estrogen receptors that play an important role in neuronal differentiation, survival and plasticity (By similarity). Axonemal dynein assembly factor required for ciliary motility. {ECO:0000250|UniProtKB:Q8WXU2, ECO:0000269|PubMed:23872636}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:23872636}. SUBUNIT: Interacts with ZMYND10 (By similarity). Interacts with ESR1 and ESR2. Interacts with STUB1 (By similarity). Interacts with DNAAF2 (By similarity). Interacts with CCT3, CCT4, CCT5 and CCT8 (PubMed:23872636). Interacts with PIH1D3 (By similarity). {ECO:0000250|UniProtKB:Q8WXU2, ECO:0000269|PubMed:23872636}. +Q61476 DAF2_MOUSE Complement decay-accelerating factor transmembrane isoform (DAF-TM) (CD antigen CD55) 407 44,511 Chain (1); Compositional bias (1); Disulfide bond (8); Domain (4); Glycosylation (2); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 369 389 Helical. {ECO:0000255}. TOPO_DOM 40 368 Extracellular. {ECO:0000255}.; TOPO_DOM 390 407 Cytoplasmic. {ECO:0000255}. FUNCTION: This protein recognizes C4b and C3b fragments that condense with cell-surface hydroxyl or amino groups when nascent C4b and C3b are locally generated during C4 and c3 activation. Interaction of daf with cell-associated C4b and C3b polypeptides interferes with their ability to catalyze the conversion of C2 and factor B to enzymatically active C2a and Bb and thereby prevents the formation of C4b2a and C3bBb, the amplification convertases of the complement cascade. Inhibits complement activation by destabilizing and preventing the formation of C3 and C5 convertases, which prevents complement damage. {ECO:0000250|UniProtKB:P08174}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. DOMAIN: The first Sushi domain (SCR1) is not necessary for function. SCR2 and SCR4 provide the proper conformation for the active site on SCR3 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Testis, spleen and lymph node. +P98078 DAB2_MOUSE Disabled homolog 2 (Adaptor molecule disabled-2) (Differentially expressed in ovarian carcinoma 2) (DOC-2) (Mitogen-responsive phosphoprotein) 766 82,312 Alternative sequence (2); Beta strand (7); Chain (1); Domain (1); Helix (4); Initiator methionine (1); Modified residue (11); Motif (2); Mutagenesis (12); Region (6); Sequence conflict (16); Turn (2) FUNCTION: Adapter protein that functions as clathrin-associated sorting protein (CLASP) required for clathrin-mediated endocytosis of selected cargo proteins. Can bind and assemble clathrin, and binds simultaneously to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) and cargos containing non-phosphorylated NPXY internalization motifs, such as the LDL receptor, to recruit them to clathrin-coated pits. Can function in clathrin-mediated endocytosis independently of the AP-2 complex. Involved in endocytosis of integrin beta-1; this function seems to redundant with the AP-2 complex and seems to require DAB2 binding to endocytosis accessory EH domain-containing proteins such as EPS15, EPS15L1 and ITSN1. Involved in endocytosis of cystic fibrosis transmembrane conductance regulator/CFTR. Isoform p96 is involved in endocytosis of megalin/LRP2 lipoprotein receptor during embryonal development. Required for recycling of the TGF-beta receptor. Isoform p67 is not involved in LDL receptor endocytosis. Involved in CFTR trafficking to the late endosome. Involved in several receptor-mediated signaling pathways. Involved in TGF-beta receptor signaling and facilitates phosphorylation of the signal transducer SMAD2. Mediates TFG-beta-stimulated JNK activation. May inhibit the canoniocal Wnt/beta-catenin signaling pathway by stabilizing the beta-catenin destruction complex through a competing association with axin preventing its dephosphorylation through protein phosphatase 1 (PP1). Sequesters LRP6 towards clathrin-mediated endocytosis, leading to inhibition of Wnt/beta-catenin signaling. May activate non-canonical Wnt signaling. In cell surface growth factor/Ras signaling pathways proposed to inhibit ERK activation by interrupting the binding of GRB2 to SOS1 and to inhibit SRC by preventing its activating phosphorylation at 'Tyr-419'. Proposed to be involved in modulation of androgen receptor (AR) signaling mediated by SRC activation; seems to compete with AR for interaction with SRC. Plays a role in the CSF-1 signal transduction pathway. Plays a role in cellular differentiation. Involved in cell positioning and formation of visceral endoderm (VE) during embryogenesis and proposed to be required in the VE to respond to Nodal signaling coming from the epiblast. Required for the epithelial to mesenchymal transition, a process necessary for proper embryonic development. May be involved in myeloid cell differentiation and can induce macrophage adhesion and spreading. Isoform p67 may be involved in transcriptional regulation. May act as a tumor suppressor. {ECO:0000269|PubMed:11247302, ECO:0000269|PubMed:11823414, ECO:0000269|PubMed:11927540, ECO:0000269|PubMed:12234931, ECO:0000269|PubMed:12413896, ECO:0000269|PubMed:15734730, ECO:0000269|PubMed:15894542, ECO:0000269|PubMed:16263760, ECO:0000269|PubMed:16870701, ECO:0000269|PubMed:16984970, ECO:0000269|PubMed:19581931, ECO:0000269|PubMed:20881059}. PTM: Phosphorylated on serine residues in response to mitogenic growth-factor stimulation. Phosphorylation during mitosis is leading to membrane displacement (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle membrane. Membrane, clathrin-coated pit. Note=Colocalizes with large insert-containing isoforms of MYO6 at clathrin-coated pits/vesicles. During mitosis is progressively displaced from the membrane and translocated to the cytoplasm (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform p96: Membrane, clathrin-coated pit. Note=Colocalizes with LDLR at clathrin-coated pits.; SUBCELLULAR LOCATION: Isoform p67: Cytoplasm {ECO:0000269|PubMed:11104669}. Nucleus {ECO:0000269|PubMed:11104669}. Note=Diffuse localization in the cytoplasm; does not localize to clathrin-coated pits. SUBUNIT: Interacts (via NPXY motif) with DAB2 (via PID domain). Can interact (via PID domain) with LDLR, APP, APLP1 and APLP2, and weakly with INPP5D (via NPXY motifs); the interaction is impaired by tyrosine phosphorylation of the respective NPXY motifs. Can weakly interact (via PID domain) with LRP1 (via NPXY motif); the interaction is enhanced by tyrosine phosphorylation of the NPXY motif. Interacts with LRP2 (via NPXY motif); the interaction is not affected by tyrosine phosphorylation of the NPXY motif. Interacts with clathrin; in vitro can assemble clathrin triskelia into polyhedral coats. Interacts with AP2A2, ITGB1, ITGB3, ITGB5, PIAS2, DAB2IP, NOSTRIN, FCHO1, DVL3 and EPS15L1. Interacts with SH3KBP1 (via SH3 domains). Interacts with GRB2; competes with SOS1 for binding to GRB2 and the interaction is enhanced by EGF and NT-3 stimulation. Isoform p96 interacts with EPS15 and ITSN1; isoform p67 does not interact with EPS15 and only weakly interacts with ITSN1. Interacts with MAP3K7; the interaction is induced by TGF-beta stimulation and may mediate TGF-beta stimulated JNK activation. Interacts with AXIN1 and PPP1CA; the interactions are mutually exclusive. Interacts with the globular tail of MYO6. Interacts (via DPF motifs) with FCHO2; the interaction is direct and required for DAB2-mediated LDLR endocytosis. Interacts with LRP6; the interaction involves LRP6 phosphorylation by CK2 and sequesters LRP6 towards clathrin-mediated endocytosis. Associates with the TGF-beta receptor complex (Probable). Interacts with SMAD2 and SMAD3; the interactions are enhanced upon TGF-beta stimulation. Interacts with GRB2; the interaction is enhanced by EGF and NT-3 stimulation. Interacts with SRC; the interaction is enhanced by EGF stimulation. {ECO:0000269|PubMed:11104669, ECO:0000269|PubMed:11247302, ECO:0000269|PubMed:11906161, ECO:0000269|PubMed:12234931, ECO:0000269|PubMed:12606711, ECO:0000269|PubMed:12877983, ECO:0000269|PubMed:14596919, ECO:0000269|PubMed:15596140, ECO:0000269|PubMed:15734730, ECO:0000269|PubMed:15894542, ECO:0000269|PubMed:19581931, ECO:0000269|PubMed:22323290, ECO:0000269|PubMed:22648170, ECO:0000269|PubMed:9569023, ECO:0000305}. DOMAIN: The PID domain binds to predominantly non-phosphorylated NPXY internalization motifs present in members of the LDLR and APP family; it also mediates simultaneous binding to phosphatidylinositol 4,5-bisphosphate (PubMed:11247302, PubMed:12234931). {ECO:0000269|PubMed:11247302, ECO:0000269|PubMed:12234931}.; DOMAIN: The Asn-Pro-Phe (NPF) motifs, which are found in proteins involved in the endocytic pathway, mediate the interaction with the EH domain of EPS15, EPS15R and ITSN1. {ECO:0000269|PubMed:22648170}. TISSUE SPECIFICITY: Isoform p96 and isoform p67 are expressed in adult kidney and fibroblasts with isoform p96 being the predominant form. Isoform p67 is the predominant isoform expressed in embryonic visceral endoderm. {ECO:0000269|PubMed:16263760}. +O35613 DAXX_MOUSE Death domain-associated protein 6 (Daxx) 739 81,489 Chain (1); Coiled coil (3); Compositional bias (2); Cross-link (2); Modified residue (18); Motif (2); Mutagenesis (2); Region (5); Sequence conflict (3) FUNCTION: Transcription corepressor known to repress transcriptional potential of several sumoylated transcription factors. Down-regulates basal and activated transcription. Its transcription repressor activity is modulated by recruiting it to subnuclear compartments like the nucleolus or PML/POD/ND10 nuclear bodies through interactions with MCSR1 and PML, respectively. Seems to regulate transcription in PML/POD/ND10 nuclear bodies together with PML and may influence TNFRSF6-dependent apoptosis thereby. Inhibits transcriptional activation of PAX3 and ETS1 through direct protein-protein interactions. Modulates PAX5 activity; the function seems to involve CREBBP. Acts as an adapter protein in a MDM2-DAXX-USP7 complex by regulating the RING-finger E3 ligase MDM2 ubiquitination activity. Under non-stress condition, in association with the deubiquitinating USP7, prevents MDM2 self-ubiquitination and enhances the intrinsic E3 ligase activity of MDM2 towards TP53, thereby promoting TP53 ubiquitination and subsequent proteasomal degradation. Upon DNA damage, its association with MDM2 and USP7 is disrupted, resulting in increased MDM2 autoubiquitination and consequently, MDM2 degradation, which leads to TP53 stabilization. Acts as histone chaperone that facilitates deposition of histone H3.3. Acts as targeting component of the chromatin remodeling complex ATRX:DAXX which has ATP-dependent DNA translocase activity and catalyzes the replication-independent deposition of histone H3.3 in pericentric DNA repeats outside S-phase and telomeres, and the in vitro remodeling of H3.3-containing nucleosomes. Does not affect the ATPase activity of ATRX but alleviates its transcription repression activity. Upon neuronal activation associates with regulatory elements of selected immediate early genes where it promotes deposition of histone H3.3 which may be linked to transcriptional induction of these genes. Required for the recruitment of histone H3.3:H4 dimers to PML-nuclear bodies (PML-NBs); the process is independent of ATRX and facilitated by ASF1A; PML-NBs are suggested to function as regulatory sites for the incorporation of newly synthesized histone H3.3 into chromatin. Proposed to mediate activation of the JNK pathway and apoptosis via MAP3K5 in response to signaling from TNFRSF6 and TGFBR2. Interaction with HSPB1/HSP27 may prevent interaction with TNFRSF6 and MAP3K5 and block DAXX-mediated apoptosis. In contrast, in lymphoid cells JNC activation and TNFRSF6-mediated apoptosis may not involve DAXX. Plays a role as a positive regulator of the heat shock transcription factor HSF1 activity during the stress protein response (By similarity). {ECO:0000250|UniProtKB:Q9UER7, ECO:0000269|PubMed:10684855, ECO:0000269|PubMed:20651253, ECO:0000269|PubMed:22500635}. PTM: Sumoylated with SUMO1 on multiple lysine residues. {ECO:0000250}.; PTM: Repressor activity is down-regulated upon Ser-669 phosphorylation. Upon neuronal activation dephosphorylated by calcineurin in a Ca2+ dependent manner at Ser-669; dephosphorylation positively affects histone H3.3 loading and transcriptional activation. {ECO:0000269|PubMed:12529400}.; PTM: Polyubiquitinated; which is promoted by CUL3 and SPOP and results in proteasomal degradation. Ubiquitinated by MDM2; inducing its degradation. Deubiquitinated by USP7; leading to stabilize it (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10684855}. Nucleus, nucleoplasm {ECO:0000269|PubMed:22500635}. Nucleus, PML body {ECO:0000269|PubMed:10684855}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9UER7}. Chromosome, centromere {ECO:0000250|UniProtKB:Q9UER7}. Note=Dispersed throughout the nucleoplasm, in PML/POD/ND10 nuclear bodies, and in nucleoli. Colocalizes with histone H3.3, ATRX, HIRA and ASF1A at PML-nuclear bodies. Colocalizes with a subset of interphase centromeres, but is absent from mitotic centromeres. Detected in cytoplasmic punctate structures. Translocates from the nucleus to the cytoplasm upon glucose deprivation or oxidative stress. Colocalizes with RASSF1 in the nucleus. Colocalizes with USP7 in nucleoplasma with accumulation in speckled structures. {ECO:0000250|UniProtKB:Q9UER7}. SUBUNIT: Homomultimer. Interacts (via C-terminus) with TNFRSF6 (via death domain). Interacts with PAX5, SLC2A4/GLUT4, MAP3K5, TGFBR2, phosphorylated dimeric HSPB1/HSP27, CENPC, ETS1, sumoylated PML, UBE2I, MCRS1 and TP53. Interacts (via N-terminus) with HIPK2 and HIPK3. Interacts with HIPK1, which induces translocation from PML/POD/ND10 nuclear bodies to chromatin and enhances association with HDAC1. Interacts (non-phosphorylated) with PAX3, PAX7, DEK, HDAC1, HDAC2, HDAC3, acetylated histone H4 and histones H2A, H2B, H3, H3.3 and H4. Interacts with SPOP; mediating CUL3-dependent proteosomal degradation. Interacts with CBP; the interaction is dependent the sumoylation of CBP and suppresses CBP transcriptional activity via recruitment of HDAC2 directly in the complex with TP53 and HIPK2. Interacts with AXIN1; the interaction stimulates the interaction of DAXX with TP53, stimulates 'Ser-46' phosphorylation of TP53 on and induces cell death on UV irradiation. Interacts with MDM2; the interaction is direct. Interacts with USP7; the interaction is direct and independent of MDM2 and TP53. Part of a complex with DAXX, MDM2 and USP7 under non-stress conditions. Interacts (via N-terminus) with RASSF1 (via C-terminus); the interaction is independent of MDM2 and TP53; RASSF1 isoform A disrupts interactions among MDM2, DAXX and USP7, thus contributing to the efficient activation of TP53 by promoting MDM2 self-ubiquitination in cell-cycle checkpoint control in response to DNA damage. Interacts with ATRX to form the chromatin remodeling complex ATRX:DAXX. Interacts with HSF1 (via homotrimeric form preferentially); this interaction relieves homotrimeric HSF1 from repression of its transcriptional activity by HSP90-dependent multichaperone complex upon heat shock (By similarity). {ECO:0000250|UniProtKB:Q9UER7, ECO:0000269|PubMed:10684855, ECO:0000269|PubMed:11034606, ECO:0000269|PubMed:11799127, ECO:0000269|PubMed:12529400, ECO:0000269|PubMed:16287980, ECO:0000269|PubMed:20504901}. DOMAIN: The Sumo interaction motif mediates Sumo binding, and is required both for sumoylation and binding to sumoylated targets. {ECO:0000250}. +O09035 DBIL5_MOUSE Diazepam-binding inhibitor-like 5 (Endozepine-like peptide) (ELP) 87 9,865 Binding site (2); Chain (1); Domain (1); Region (1) FUNCTION: May be involved in the energy metabolism of the mature sperm. SUBCELLULAR LOCATION: Cytoplasm. TISSUE SPECIFICITY: Exclusively expressed in late spermatids and spermatozoa. Not found in epididymis, spleen, bone marrow, skin, liver, brain, heart, kidney, muscle. +Q9QZ41 DBF4A_MOUSE Protein DBF4 homolog A (MuDBF4) 663 74,176 Alternative sequence (3); Chain (1); Domain (2); Modified residue (5); Sequence caution (1); Zinc finger (1) FUNCTION: Regulatory subunit for CDC7 which activates its kinase activity thereby playing a central role DNA in replication and cell proliferation. Required for progression of S phase. The complex CDC7-DBF4A selectively phosphorylates MCM2 subunit at 'Ser-40' and 'Ser-53' and then is involved in regulating the initiation of DNA replication during cell cycle. {ECO:0000269|PubMed:10517317}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Forms a complex with CDC7. Note that CDC7 forms distinct complex either with DBF4A or DBF4B. Such complexes are stable upon replication stress. Interacts with MEN1, MCM2, ORC2, ORC4 and ORC6. {ECO:0000269|PubMed:10517317, ECO:0000269|PubMed:12614612}. +Q9JII5 DAZP1_MOUSE DAZ-associated protein 1 (Deleted in azoospermia-associated protein 1) 406 43,214 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (2); Modified residue (3); Sequence conflict (2) FUNCTION: RNA-binding protein, which may be required during spermatogenesis. {ECO:0000250}. PTM: Acetylation at Lys-150 is predominantly observed in the nuclear fraction, and may regulate nucleocytoplasmic transport. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Predominantly cytoplasmic. Nuclear at some stages of spermatozoides development. In midpachytene spermatocytes, it is localized in both the cytoplasm and the nuclei and is clearly excluded from the sex vesicles. In round spermatids, it localizes mainly in the nuclei, whereas in elongated spermatids, it localizes to the cytoplasm. SUBUNIT: Interacts with DAZ and DAZL. {ECO:0000250}. TISSUE SPECIFICITY: Mainly expressed in testis. Expressed at much lower level in liver, heart and brain. Also expressed in ovary. Expressed throughout testes development, in both the prenatal and postnatal periods. {ECO:0000269|PubMed:11604102}. +Q62418 DBNL_MOUSE Drebrin-like protein (Actin-binding protein 1) (SH3 domain-containing protein 7) 436 48,700 Alternative sequence (2); Chain (1); Coiled coil (1); Domain (2); Modified residue (11); Mutagenesis (2); Sequence conflict (5); Site (1) FUNCTION: Adapter protein that binds F-actin and DNM1, and thereby plays a role in receptor-mediated endocytosis. Plays a role in the reorganization of the actin cytoskeleton, formation of cell projections, such as neurites, in neuron morphogenesis and synapse formation via its interaction with WASL and COBL. Does not bind G-actin and promote actin polymerization by itself. Required for the formation of organized podosome rosettes. May act as a common effector of antigen receptor-signaling pathways in leukocytes. Acts as a key component of the immunological synapse that regulates T-cell activation by bridging TCRs and the actin cytoskeleton to gene activation and endocytic processes. {ECO:0000269|PubMed:11309416, ECO:0000269|PubMed:17476322, ECO:0000269|PubMed:18829961, ECO:0000269|PubMed:22303001, ECO:0000269|PubMed:23223303}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10637315, ECO:0000269|PubMed:17476322, ECO:0000269|PubMed:9891087}. Cell projection, lamellipodium {ECO:0000269|PubMed:10637315, ECO:0000269|PubMed:12913069}. Cell projection, ruffle {ECO:0000269|PubMed:12913069}. Cytoplasm, cell cortex {ECO:0000269|PubMed:10637315, ECO:0000269|PubMed:11309416, ECO:0000269|PubMed:23223303}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9JHL4}. Cell junction, synapse {ECO:0000250|UniProtKB:Q9JHL4, ECO:0000269|PubMed:11309416}. Cell projection {ECO:0000250|UniProtKB:Q9JHL4, ECO:0000269|PubMed:11309416, ECO:0000269|PubMed:17476322}. Cell membrane {ECO:0000250|UniProtKB:Q9JHL4}; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000305|PubMed:11309416}; Peripheral membrane protein; Cytoplasmic side. Golgi apparatus membrane {ECO:0000269|PubMed:16452483}; Peripheral membrane protein; Cytoplasmic side. Cell projection, podosome {ECO:0000269|PubMed:22303001}. Early endosome {ECO:0000250|UniProtKB:Q9UJU6}. Note=Detected in neuron cell body and cell projections, such as neurites. Colocalizes with cytosolic dynamin in hippocampus neurons (By similarity). Cortical actin cytoskeleton. Associates with lamellipodial actin and membrane ruffles. Colocalizes with actin and cortactin at podosome dots and podosome rosettes. {ECO:0000250|UniProtKB:Q9JHL4, ECO:0000269|PubMed:11309416, ECO:0000269|PubMed:12913069, ECO:0000269|PubMed:17476322, ECO:0000269|PubMed:22303001}. SUBUNIT: Interacts with SHANK3, SYN1 and PRAM1 (By similarity). Interacts with SHANK2. Interacts with FGD1, DNM1 and MAP4K1. Interacts with ANKRD54. Interacts with COBL. Interacts with WASL and WIPF1. {ECO:0000250, ECO:0000269|PubMed:10637315, ECO:0000269|PubMed:11309416, ECO:0000269|PubMed:12913069, ECO:0000269|PubMed:17476322, ECO:0000269|PubMed:18829961, ECO:0000269|PubMed:19064729, ECO:0000269|PubMed:22303001, ECO:0000269|PubMed:23223303}. DOMAIN: The SH3 domain mediates interaction with SHANK2, SHANK3 and PRAM1. {ECO:0000250}. TISSUE SPECIFICITY: Detected in hippocampus neurons and in the Purkinje cell layer in cerebellum (at protein level). Predominantly expressed in brain, thymus and spleen. Also found in testis, heart and lung. Little or no expression detected in ovary or muscle. {ECO:0000269|PubMed:10637315, ECO:0000269|PubMed:23223303, ECO:0000269|PubMed:9891087}. +Q8K0T2 DC2L1_MOUSE Cytoplasmic dynein 2 light intermediate chain 1 (mD2LIC) 351 39,469 Chain (1); Frameshift (1); Sequence conflict (3) FUNCTION: Required for correct intraflagellar transport (IFT), the bi-directional movement of particles required for the assembly, maintenance and functioning of primary cilia (PubMed:15371312). Involved in the regulation of ciliary length (By similarity). {ECO:0000250|UniProtKB:Q8TCX1, ECO:0000269|PubMed:15371312}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12802074}. Cell projection, cilium {ECO:0000250|UniProtKB:Q8TCX1}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q8TCX1}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:12802074}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q8TCX1}. Note=Localizes to the apical cytoplasm. {ECO:0000269|PubMed:12802074}. SUBUNIT: The cytoplasmic dynein complex 2 is probably composed by a DYNC2H1 homodimer and a number of DYNC2LI1 light intermediate chains. {ECO:0000250}. TISSUE SPECIFICITY: Specifically expressed by ciliated cells in brain, lung, spleen, testis and kidney (at protein level). Enriched in the ependymal layer lining the lateral ventricles (at protein level). {ECO:0000269|PubMed:11907264, ECO:0000269|PubMed:12432068, ECO:0000269|PubMed:12802074, ECO:0000269|PubMed:15371312}. +Q91VU6 DCA11_MOUSE DDB1- and CUL4-associated factor 11 (WD repeat-containing protein 23) 549 61,992 Alternative sequence (2); Chain (1); Modified residue (2); Repeat (7) Protein modification; protein ubiquitination. FUNCTION: May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex. {ECO:0000250}. SUBUNIT: Interacts with DDB1 and CUL4A. {ECO:0000250}. +Q14AI0 DCC1_MOUSE Sister chromatid cohesion protein DCC1 (Defective in sister chromatid cohesion protein 1 homolog) 399 45,522 Chain (1) FUNCTION: Loads PCNA onto primed templates regulating velocity, spacing and restart activity of replication forks. May couple DNA replication to sister chromatid cohesion through regulation of the acetylation of the cohesin subunit SMC3 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the CTF18-RFC complex which consists of CTF8, CTF18, DSCC1 and the RFC complex. Interacts with CTF8 and CTF18. Interacts with DDX11. {ECO:0000250|UniProtKB:Q9BVC3}. +Q9CXV9 DCNL5_MOUSE DCN1-like protein 5 (DCUN1 domain-containing protein 5) (Defective in cullin neddylation protein 1-like protein 5) 237 27,579 Chain (1); Domain (1); Frameshift (1); Modified residue (1); Sequence conflict (4) +Q9CYC6 DCP2_MOUSE m7GpppN-mRNA hydrolase (EC 3.6.1.62) (mRNA-decapping enzyme 2) 422 48,380 Chain (1); Domain (1); Metal binding (2); Modified residue (5); Motif (1); Sequence conflict (1) FUNCTION: Decapping metalloenzyme that catalyzes the cleavage of the cap structure on mRNAs (PubMed:21070968). Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP (PubMed:21070968). Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay (By similarity). Plays a role in replication-dependent histone mRNA degradation (By similarity). Has higher activity towards mRNAs that lack a poly(A) tail (PubMed:21070968). Has no activity towards a cap structure lacking an RNA moiety (PubMed:21070968). {ECO:0000250|UniProtKB:Q8IU60, ECO:0000269|PubMed:21070968}.; FUNCTION: Decapping metalloenzyme that catalyzes the cleavage of the cap structure on mRNAs (PubMed:21070968). Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP (PubMed:21070968). Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay (By similarity). Plays a role in replication-dependent histone mRNA degradation. Has higher activity towards mRNAs that lack a poly(A) tail (PubMed:21070968). Has no activity towards a cap structure lacking an RNA moiety (PubMed:21070968). The presence of a N(6)-methyladenosine methylation at the second transcribed position of mRNAs (N(6),2'-O-dimethyladenosine cap; m6A(m)) provides resistance to DCP2-mediated decapping (By similarity). Blocks autophagy in nutrient-rich conditions by repressing the expression of ATG-related genes through degration of their transcripts (By similarity). {ECO:0000250|UniProtKB:Q8IU60, ECO:0000269|PubMed:21070968}. SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000250|UniProtKB:Q8IU60}. Nucleus {ECO:0000250|UniProtKB:Q8IU60}. Note=Predominantly cytoplasmic, in processing bodies (PB) (By similarity). A minor amount is nuclear (By similarity). {ECO:0000250|UniProtKB:Q8IU60}. SUBUNIT: Found in a mRNA decay complex with LSM1, LSM3, LSM4, EXOSC2, EXOSC4, EXOSC10, PARN, XRN1, CNOT6, UPF1, UPF2 and UPF3B. Forms a complex with DCP1A, EDC3, DDX6 and EDC4/HEDLS, within this complex directly interacts with EDC4/HEDLS. Interacts with DPC1B, UPF1, UPF2 and UPF3B. Associates with polysomes. Interacts (via N-terminus and C-terminus) with TRIM21 (via N-terminus and C-terminus). Interacts with LIMD1, WTIP and AJUBA. Interacts with DDX17 in an RNA-dependent manner. Interacts with ZC3HAV1. Interacts with APOBEC3G in an RNA-dependent manner. Interacts with ZFP36L1 (via N-terminus). Interacts with NBDY. {ECO:0000250|UniProtKB:Q8IU60}. TISSUE SPECIFICITY: Strongly expressed in brain and testis. Weakly expressed in lung. Not detected in heart, liver, kidney and muscle (at protein level). {ECO:0000269|PubMed:21070968}. +Q99J39 DCMC_MOUSE Malonyl-CoA decarboxylase, mitochondrial (MCD) (EC 4.1.1.9) 492 54,736 Active site (2); Alternative sequence (1); Binding site (2); Chain (1); Disulfide bond (1); Modified residue (11); Motif (1); Mutagenesis (2); Region (3); Site (1); Transit peptide (1) Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from malonyl-CoA: step 1/1. FUNCTION: Catalyzes the conversion of malonyl-CoA to acetyl-CoA. In the fatty acid biosynthesis MCD selectively removes malonyl-CoA and thus assures that methyl-malonyl-CoA is the only chain elongating substrate for fatty acid synthase and that fatty acids with multiple methyl side chains are produced. In peroxisomes it may be involved in degrading intraperoxisomal malonyl-CoA, which is generated by the peroxisomal beta-oxidation of odd chain-length dicarboxylic fatty acids. Plays a role in the metabolic balance between glucose and lipid oxidation in muscle independent of alterations in insulin signaling. Plays a role in controlling the extent of ischemic injury by promoting glucose oxidation. {ECO:0000269|PubMed:17030679, ECO:0000269|PubMed:23746352}. PTM: Interchain disulfide bonds may form in peroxisomes (Potential). Interchain disulfide bonds are not expected to form in the reducing environment of the cytoplasm and mitochondria. {ECO:0000305}.; PTM: Acetylation at Lys-471 activates malonyl-CoA decarboxylase activity. Deacetylation at Lys-471 by SIRT4 represses activity, leading to promote lipogenesis. {ECO:0000269|PubMed:23746352}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Mitochondrion matrix {ECO:0000269|PubMed:23746352}. Peroxisome {ECO:0000250}. Peroxisome matrix {ECO:0000250}. Note=Enzymatically active in all three subcellular compartments. {ECO:0000250}. SUBUNIT: Homotetramer. Dimer of dimers. The two subunits within a dimer display conformational differences suggesting that at any given moment, only one of the two subunits is competent for malonyl-CoA binding and catalytic activity. Under oxidizing conditions, can form disulfide-linked homotetramers (in vitro). Associates with the peroxisomal targeting signal receptor PEX5 (By similarity). {ECO:0000250}. +Q99LD8 DDAH2_MOUSE N(G),N(G)-dimethylarginine dimethylaminohydrolase 2 (DDAH-2) (Dimethylarginine dimethylaminohydrolase 2) (EC 3.5.3.18) (DDAHII) (Dimethylargininase-2) 285 29,646 Active site (2); Chain (1) FUNCTION: Hydrolyzes N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-monomethyl-L-arginine (MMA) which act as inhibitors of NOS. Has therefore a role in the regulation of nitric oxide generation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Mitochondrion {ECO:0000250}. Note=Translocates from cytosol to mitochondrion upon IL-1beta stimulation in chondrocytes. {ECO:0000250}. +Q99J79 DDB2_MOUSE DNA damage-binding protein 2 (Damage-specific DNA-binding protein 2) 432 48,375 Chain (1); Motif (1); Region (3); Repeat (7) Protein modification; protein ubiquitination. FUNCTION: Required for DNA repair. Binds to DDB1 to form the UV-damaged DNA-binding protein complex (the UV-DDB complex). The UV-DDB complex may recognize UV-induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair. The UV-DDB complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and short mismatches. Also appears to function as the substrate recognition module for the DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex DDB1-CUL4-ROC1 (also known as CUL4-DDB-ROC1 and CUL4-DDB-RBX1). The DDB1-CUL4-ROC1 complex may ubiquitinate histone H2A, histone H3 and histone H4 at sites of UV-induced DNA damage. The ubiquitination of histones may facilitate their removal from the nucleosome and promote subsequent DNA repair. The DDB1-CUL4-ROC1 complex also ubiquitinates XPC, which may enhance DNA-binding by XPC and promote NER. {ECO:0000269|PubMed:12107171}. PTM: Phosphorylation by ABL1 negatively regulate UV-DDB activity. {ECO:0000269|PubMed:12107171}.; PTM: Ubiquitinated by CUL4A in response to UV irradiation. Ubiquitination appears to both impair DNA-binding and promotes ubiquitin-dependent proteolysis. Degradation of DDB2 at sites of DNA damage may be a prerequisite for their recognition by XPC and subsequent repair. CUL4A-mediated degradation appears to be promoted by ABL1 (By similarity). {ECO:0000250}.; PTM: Ubiquitinated, leading to proteasomal degradation, and deubiquitinated by USP24. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17635991}. Note=Accumulates at sites of DNA damage following UV irradiation. SUBUNIT: Component of the UV-DDB complex which includes DDB1 and DDB2. The UV-DDB complex interacts with monoubiquitinated histone H2A and binds to XPC via the DDB2 subunit. Component of the DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex DDB1-CUL4-ROC1 (also known as CUL4-DDB-ROC1 and CUL4-DDB-RBX1), which includes CUL4A or CUL4B, DDB1, DDB2 and RBX1. DDB2 may function as the substrate recognition module within this complex. The DDB1-CUL4-ROC1 complex may associate with the COP9 signalosome, and this inhibits the E3 ubiquitin-protein ligase activity of the complex. A large number of other DCX complexes may also exist in which an alternate substrate targeting subunit replaces DDB2. These targeting subunits are generally known as DCAF (DDB1- and CUL4-associated factor) or CDW (CUL4-DDB1-associated WD40-repeat) proteins (By similarity). {ECO:0000250}. DOMAIN: The DWD box is required for interaction with DDB1. {ECO:0000250}.; DOMAIN: Interblade loops of the WD repeat region mediate most of the interaction with DNA. A hairpin between blades 5 and 6 inserts into DNA minor groove and mediates recognition of lesions and separation of the damaged and undamaged strands (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in bone marrow, liver, lung, muscle, pancreas and spleen. {ECO:0000269|PubMed:15558025}. +Q9CWT6 DDX28_MOUSE Probable ATP-dependent RNA helicase DDX28 (EC 3.6.4.13) (Mitochondrial DEAD box protein 28) 540 59,515 Chain (1); Domain (2); Motif (5); Nucleotide binding (1); Sequence conflict (1) FUNCTION: Plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. May be involved in RNA processing or transport. Has RNA and Mg(2+)-dependent ATPase activity (By similarity). {ECO:0000250|UniProtKB:Q9NUL7}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NUL7}. Mitochondrion {ECO:0000250|UniProtKB:Q9NUL7}. Mitochondrion matrix, mitochondrion nucleoid {ECO:0000250|UniProtKB:Q9NUL7}. Mitochondrion matrix {ECO:0000250|UniProtKB:Q9NUL7}. Note=Transported between these two compartments. Nuclear localization depends on active RNA polymerase II transcription. Localizes to mitochondrial RNA granules found in close proximity to the mitochondrial nucleoids (By similarity). {ECO:0000250|UniProtKB:Q9NUL7}. SUBUNIT: Monomer. Found in a complex with GRSF1, DHX30, FASTKD2 and FASTKD5. Associates with the 16S mitochondrial rRNA (16S mt-rRNA) and with the mitochondrial ribosome large subunit (39S). {ECO:0000250|UniProtKB:Q9NUL7}. +Q8K4L0 DDX54_MOUSE ATP-dependent RNA helicase DDX54 (EC 3.6.4.13) (DEAD box protein 54) 874 97,748 Chain (1); Domain (2); Modified residue (9); Motif (2); Nucleotide binding (1) FUNCTION: Has RNA-dependent ATPase activity. Represses the transcriptional activity of nuclear receptors (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. SUBUNIT: Interacts in a hormone-dependent manner with nuclear receptors. {ECO:0000250}. +Q9JM93 AR6P4_MOUSE ADP-ribosylation factor-like protein 6-interacting protein 4 (ARL-6-interacting protein 4) (Aip-4) (Splicing factor SRrp37) 229 25,525 Chain (1); Compositional bias (2); Cross-link (1); Modified residue (2); Sequence caution (1) FUNCTION: Involved in modulating alternative pre-mRNA splicing with either 5' distal site activation or preferential use of 3' proximal site. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Nucleus speckle {ECO:0000250}. SUBUNIT: Interacts with ZCCHC17 (By similarity). Interacts with SRSF2 (By similarity). Interacts with ARL6. {ECO:0000250, ECO:0000269|PubMed:10508919}. TISSUE SPECIFICITY: Widely expressed. Expressed at high level in testis and thymus. {ECO:0000269|PubMed:10708573}. +Q64364 ARF_MOUSE Tumor suppressor ARF (Alternative reading frame) (ARF) (Cyclin-dependent kinase inhibitor 2A) (p19ARF) 169 19,238 Alternative sequence (1); Chain (1); Compositional bias (1); Helix (2); Mutagenesis (5); Region (1) FUNCTION: Capable of inducing cell cycle arrest in G1 and G2 phases. Acts as a tumor suppressor. Binds to MDM2 and blocks its nucleocytoplasmic shuttling by sequestering it in the nucleolus. This inhibits the oncogenic action of MDM2 by blocking MDM2-induced degradation of p53 and enhancing p53-dependent transactivation and apoptosis. Also induces G2 arrest and apoptosis in a p53-independent manner by preventing the activation of cyclin B1/CDC2 complexes. Binds to BCL6 and down-regulates BCL6-induced transcriptional repression. Binds to E2F1 and MYC and blocks their transcriptional activator activity but has no effect on MYC transcriptional repression. Binds to TOP1/TOPOI and stimulates its activity. This complex binds to rRNA gene promoters and may play a role in rRNA transcription and/or maturation. Interacts with NPM1/B23 and promotes its polyubiquitination and degradation, thus inhibiting rRNA processing. Interacts with COMMD1 and promotes its 'Lys63'-linked polyubiquitination (By similarity). Interacts with UBE2I/UBC9 and enhances sumoylation of a number of its binding partners including MDM2 and E2F1. Binds to HUWE1 and represses its ubiquitin ligase activity. May play a role in controlling cell proliferation and apoptosis during mammary gland development. Isoform smARF may be involved in regulation of autophagy and caspase-independent cell death; the short-lived mitochondrial isoform is stabilized by C1QBP. {ECO:0000250|UniProtKB:Q8N726, ECO:0000269|PubMed:10359817, ECO:0000269|PubMed:15361884, ECO:0000269|PubMed:15567177, ECO:0000269|PubMed:15601844, ECO:0000269|PubMed:17936562, ECO:0000269|PubMed:8521522, ECO:0000269|PubMed:9393858, ECO:0000269|PubMed:9529248}. PTM: Ubiquitinated in normal cells by TRIP12 via the ubiquitin fusion degradation (UFD) pathway, a process that mediates ubiquitination at the N-terminus, regardless of the absence of lysine residues. Ubiquitination leads to its proteasomal degradation. In cancer cells, however, TRIP12 is located in a different cell compartment, preventing ubiquitination and degradation. {ECO:0000250|UniProtKB:Q8N726}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q8N726, ECO:0000269|PubMed:10359817, ECO:0000269|PubMed:15567177, ECO:0000269|PubMed:15601844, ECO:0000269|PubMed:8521522}. Nucleus, nucleoplasm {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform smARF: Mitochondrion {ECO:0000269|PubMed:16713577}. SUBUNIT: Does not interact with cyclins, CDK1, CDK2, CDK4, CDK5 or CDK6. Interacts with COMMD1 (By similarity). Binds to BCL6, E2F1, HUWE1, MDM2, MYC, NPM1/B23, TOP1/TOPOI and UBE2I/UBC9. Interacts with TBRG1. Interacts with CDKN2AIP and E4F1. Isoform smARF interacts with C1QBP. Interacts with CDK5RAP3 and MDM2; form a ternary complex involved in regulation of p53/TP53. Interacts with NOP53; the interaction is direct and promotes ARF nucleoplasmic relocalization and ubiquitin-mediated proteasomal degradation (By similarity). {ECO:0000250|UniProtKB:Q8N726, ECO:0000269|PubMed:12154087, ECO:0000269|PubMed:15361884, ECO:0000269|PubMed:15567177, ECO:0000269|PubMed:17110379, ECO:0000269|PubMed:17486078, ECO:0000269|PubMed:9529248}. +Q810L3 CHFR_MOUSE E3 ubiquitin-protein ligase CHFR (EC 2.3.2.27) (Checkpoint with forkhead and RING finger domains protein) (RING-type E3 ubiquitin transferase CHFR) 664 73,871 Alternative sequence (3); Chain (1); Domain (1); Modified residue (1); Sequence conflict (4); Zinc finger (2) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that functions in the antephase checkpoint by actively delaying passage into mitosis in response to microtubule poisons. Acts in early prophase before chromosome condensation, when the centrosome move apart from each other along the periphery of the nucleus. Probably involved in signaling the presence of mitotic stress caused by microtubule poisons by mediating the 'Lys-48'-linked ubiquitination of target proteins, leading to their degradation by the proteasome. Promotes the ubiquitination and subsequent degradation of AURKA and PLK1. Probably acts as a tumor suppressor, possibly by mediating the polyubiquitination of HDAC1, leading to its degradation. May also promote the formation of 'Lys-63'-linked polyubiquitin chains and functions with the specific ubiquitin-conjugating UBC13-MMS2 (UBE2N-UBE2V2) heterodimer. Substrates that are polyubiquitinated at 'Lys-63' are usually not targeted for degradation, but are rather involved in signaling cellular stress (By similarity). {ECO:0000250|UniProtKB:Q96EP1, ECO:0000269|PubMed:15793587}. PTM: Poly-ADP-ribosylated. In addition to binding non covalently poly(ADP-ribose) via its PBZ-type zinc finger, the protein is also covalently poly-ADP-ribosylated by PARP1. {ECO:0000250|UniProtKB:Q96EP1}.; PTM: Autoubiquitinated; may regulate its cellular level. {ECO:0000250|UniProtKB:Q96EP1}.; PTM: Phosphorylated by PKB. Phosphorylation may affect its E3 ligase activity. {ECO:0000250|UniProtKB:Q96EP1}. SUBCELLULAR LOCATION: Nucleus, PML body {ECO:0000250|UniProtKB:Q96EP1}. SUBUNIT: Interacts with HDAC1 and HDAC2. Interacts with PML (with sumoylated form of PML). {ECO:0000250|UniProtKB:Q96EP1}. DOMAIN: The PBZ-type zinc finger (also named CYR) mediates non-covalent poly(ADP-ribose)-binding. Poly(ADP-ribose)-binding is dependent on the presence of zinc and is required for its function in antephase checkpoint. {ECO:0000250|UniProtKB:Q96EP1}.; DOMAIN: The FHA domain plays a key role in the anti-proliferative properties of the protein and is involved in initiating a cell cycle arrest at G2/M. The FHA domain may be required to interact with phosphorylated proteins. {ECO:0000250|UniProtKB:Q96EP1}. +Q922Q9 CHID1_MOUSE Chitinase domain-containing protein 1 393 44,906 Alternative sequence (1); Chain (1); Erroneous initiation (3); Erroneous termination (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Saccharide- and LPS-binding protein with possible roles in pathogen sensing and endotoxin neutralization. Ligand-binding specificity relates to the length of the oligosaccharides, with preference for chitotetraose (in vitro) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. Lysosome {ECO:0000250}. SUBUNIT: Interacts with STAB1. {ECO:0000250}. +Q91Z98 CHIL4_MOUSE Chitinase-like protein 4 (Chitinase-3-like protein 4) (Secreted protein Ym2) 402 44,975 Binding site (2); Chain (1); Disulfide bond (2); Sequence conflict (3); Signal peptide (1) FUNCTION: Has low chemotactic activity for eosinophils. May play a role in inflammation and allergy. Has no chitinase activity. {ECO:0000269|PubMed:11553626}. SUBCELLULAR LOCATION: Secreted. Cytoplasm. Note=Detected in the cytoplasm of keratinocytes. TISSUE SPECIFICITY: Detected in stratified squamous epithelium in the junctional region between forestomach and glandular stomach (at protein level). Expression is mainly restricted to stomach. {ECO:0000269|PubMed:15148607, ECO:0000269|PubMed:9828134}. +O54804 CHKA_MOUSE Choline kinase alpha (CK) (EC 2.7.1.32) (CHETK-alpha) (Ethanolamine kinase) (EK) (EC 2.7.1.82) 453 51,985 Alternative sequence (1); Binding site (3); Chain (1); Compositional bias (1); Erroneous gene model prediction (1); Modified residue (1); Nucleotide binding (2); Region (1); Sequence caution (4); Sequence conflict (3) Phospholipid metabolism; phosphatidylcholine biosynthesis; phosphocholine from choline: step 1/1. Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from ethanolamine: step 1/3. FUNCTION: Has a key role in phospholipid biosynthesis and may contribute to tumor cell growth. Catalyzes the first step in phosphatidylcholine biosynthesis. Contributes to phosphatidylethanolamine biosynthesis. Phosphorylates choline and ethanolamine. Has higher activity with choline (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Homodimer, and heterodimer with CHKB. {ECO:0000269|PubMed:16490392}. TISSUE SPECIFICITY: Expressed ubiquitously with the highest level in testis. +Q9CQ10 CHMP3_MOUSE Charged multivesicular body protein 3 (Chromatin-modifying protein 3) (Vacuolar protein sorting-associated protein 24) 224 25,219 Binding site (1); Chain (1); Coiled coil (2); Cross-link (1); Initiator methionine (1); Lipidation (1); Modified residue (1); Motif (1); Region (8); Sequence conflict (3); Site (1) FUNCTION: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis. ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. Selectively binds to phosphatidylinositol 3,5-bisphosphate PtdIns(3,5)P2 and PtdIns(3,4)P2 in preference to other phosphoinositides tested. Involved in late stages of cytokinesis. Plays a role in endosomal sorting/trafficking of EGF receptor (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Endosome {ECO:0000250}. Late endosome membrane {ECO:0000250}. Note=Localizes to the midbody of dividing cells. {ECO:0000250}. SUBUNIT: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III). ESCRT-III components are thought to multimerize to form a flat lattice on the perimeter membrane of the endosome. Several assembly forms of ESCRT-III may exist that interact and act sequentially. Forms a metastable monomer in solution; its core structure (without part of the putative autoinhibitory C-terminal acidic region) oligomerizes into a flat lattice via two different dimerization interfaces. In vitro, heteromerizes with CHMP2A (but not CHMP4) to form helical tubular structures that expose membrane-interacting sites on the outside whereas VPS4B can associate on the inside of the tubule. May interact with IGFBP7; the relevance of such interaction however remains unclear. Interacts with CHMP2A. Interacts with CHMP4A; the interaction requires the release of CHMP4A autoinhibition. Interacts with VPS4A. Interacts with STAMBP; the interaction appears to relieve the autoinhibition of CHMP3 (By similarity). Interacts with VTA1 (By similarity). {ECO:0000250}. DOMAIN: The acidic C-terminus and the basic N-termminus are thought to render the protein in a closed, soluble and inactive conformation through an autoinhibitory intramolecular interaction. The open and active conformation, which enables membrane binding and oligomerization, is achieved by interaction with other cellular binding partners, probably including other ESCRT components. TISSUE SPECIFICITY: Expressed in lung, testis, heart, spleen, skeletal muscle, kidney, liver and brain. {ECO:0000269|PubMed:17331679}. +Q9CXM0 CHODL_MOUSE Chondrolectin (Transmembrane protein MT75) 273 30,331 Alternative sequence (1); Chain (1); Disulfide bond (2); Domain (1); Glycosylation (1); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 217 237 Helical. {ECO:0000255}. TOPO_DOM 22 216 Extracellular. {ECO:0000255}.; TOPO_DOM 238 273 Cytoplasmic. {ECO:0000255}. FUNCTION: May play a role in the development of the nervous system such as in neurite outgrowth and elongation (PubMed:24067532). May be involved in motor axon growth and guidance (By similarity). {ECO:0000250|UniProtKB:Q568T5, ECO:0000305|PubMed:24067532}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Interacts with RABGGTB (PubMed:18161010). TISSUE SPECIFICITY: In adult mice preferentially expressed in skeletal muscle, testis, brain, and lung. Expressed in striated muscle (at protein level). Expressed in spinal chord. Detected in spinal chord fast motor neurons (at protein level). {ECO:0000269|PubMed:12711387, ECO:0000269|PubMed:20019802, ECO:0000269|PubMed:20437528}. +P61022 CHP1_MOUSE Calcineurin B homologous protein 1 (Calcineurin B-like protein) (Calcium-binding protein CHP) (Calcium-binding protein p22) (EF-hand calcium-binding domain-containing protein p22) (Sid 470) (p24) 195 22,432 Calcium binding (2); Chain (1); Domain (4); Initiator methionine (1); Lipidation (1); Motif (3) FUNCTION: Calcium-binding protein involved in different processes such as regulation of vesicular trafficking, plasma membrane Na(+)/H(+) exchanger and gene transcription. Involved in the constitutive exocytic membrane traffic. Mediates the association between microtubules and membrane-bound organelles of the endoplasmic reticulum and Golgi apparatus and is also required for the targeting and fusion of transcytotic vesicles (TCV) with the plasma membrane. Functions as an integral cofactor in cell pH regulation by controlling plasma membrane-type Na(+)/H(+) exchange activity. Affects the pH sensitivity of SLC9A1/NHE1 by increasing its sensitivity at acidic pH. Required for the stabilization and localization of SLC9A1/NHE1 at the plasma membranes. Inhibits serum- and GTPase-stimulated Na(+)/H(+) exchange. Plays a role as an inhibitor of ribosomal RNA transcription by repressing the nucleolar UBF1 transcriptional activity. May sequester UBF1 in the nucleoplasm and limit its translocation to the nucleolus. Associates to the ribosomal gene promoter. Acts as a negative regulator of the calcineurin/NFAT signaling pathway. Inhibits NFAT nuclear translocation and transcriptional activity by suppressing the calcium-dependent calcineurin phosphatase activity. Also negatively regulates the kinase activity of the apoptosis-induced kinase STK17B. Inhibits both STK17B auto- and substrate-phosphorylations in a calcium-dependent manner (By similarity). {ECO:0000250}. PTM: Phosphorylated; decreased phosphorylation is associated with an increase in SLC9A1/NHE1 Na(+)/H(+) exchange activity. Phosphorylation occurs in serum-dependent manner. The phosphorylation state may regulate the binding to SLC9A1/NHE1 (By similarity). {ECO:0000250}.; PTM: Both N-myristoylation and calcium-mediated conformational changes are essential for its function in exocytic traffic. N-myristoylation is required for its association with microtubules and interaction with GAPDH, but not for the constitutive association to membranes (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P61023}. Cytoplasm {ECO:0000250|UniProtKB:P61023}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P61023}. Endomembrane system {ECO:0000250|UniProtKB:P61023}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250|UniProtKB:P61023}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P61023}. Cell membrane {ECO:0000250|UniProtKB:P61023}. Membrane {ECO:0000250|UniProtKB:Q99653}; Lipid-anchor {ECO:0000250|UniProtKB:Q99653}. Note=Localizes in cytoplasmic compartments in dividing cells. Localizes in the nucleus in quiescent cells. Exported from the nucleus to the cytoplasm through a nuclear export signal (NES) and CRM1-dependent pathway. May shuttle between nucleus and cytoplasm. Localizes with the microtubule-organizing center (MTOC) and extends toward the periphery along microtubules. Associates with membranes of the early secretory pathway in a GAPDH-independent, N-myristoylation- and calcium-dependent manner. Colocalizes with the mitotic spindle microtubules. Colocalizes with GAPDH along microtubules. Colocalizes with SLC9A1 at the reticulum endoplasmic and plasma membrane. Colocalizes with STK17B at the plasma membrane. {ECO:0000250|UniProtKB:P61023}. SUBUNIT: Monomer. Interacts with STK17B; the interaction occurs in a calcium-independent manner and induces the translocation of CHP1 from the Golgi to the nucleus. Interacts with GAPDH; the interaction is direct, occurs in a N-myristoylation-dependent manner and facilitates the ability of CHP1 to bind microtubules. Interacts with KIF1B (via the C-terminal end of the kinesin-motor domain); the interaction occurs in a calcium-dependent manner. Associates (via C-terminal domain) with microtubules; the association occurs with polymerized microtubules during the cell cycle in a myristoylation- and calcium-independent manner and is enhanced by GAPDH. Interacts with PPP3CA. Interacts with SLC9A1/NHE1 (via the juxtamembrane region of the cytoplasmic C-terminal domain); the interaction occurs at the plasma membrane in a calcium-dependent manner and at a domain that is critical for growth factor stimulation of the exchanger (By similarity). Interacts with SLC9A1/NHE1. {ECO:0000250, ECO:0000269|PubMed:8967452}. +Q9DCB4 ARP21_MOUSE cAMP-regulated phosphoprotein 21 (ARPP-21) (Regulator of calmodulin signaling) (Thymocyte cAMP-regulated phosphoprotein) 807 88,567 Alternative sequence (16); Chain (1); Coiled coil (1); Compositional bias (2); Domain (2); Initiator methionine (1); Modified residue (10); Mutagenesis (1); Sequence conflict (1) FUNCTION: Isoform 2 may act as a competitive inhibitor of calmodulin-dependent enzymes such as calcineurin in neurons. {ECO:0000269|PubMed:15499021}. PTM: Phosphorylation of isoform 2 at Ser-55 is enhanced upon dopamine D1 receptor activation and favors interaction with CALM1. {ECO:0000269|PubMed:10854908, ECO:0000269|PubMed:15499021}.; PTM: Isoform 1 is methylated by CARM1 in immature thymocytes. {ECO:0000305|PubMed:15096520}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11298339, ECO:0000269|PubMed:15096520}. SUBUNIT: Interacts with CALM1. {ECO:0000269|PubMed:15499021}. TISSUE SPECIFICITY: Isoform 1 is present at high levels in thymus and low levels in brain. In thymus, isoform 1 is specifically found in immature thymocytes (at protein level). {ECO:0000269|PubMed:11298339}. +P56212 ARP19_MOUSE cAMP-regulated phosphoprotein 19 (ARPP-19) 112 12,293 Alternative sequence (1); Chain (1); Initiator methionine (1); Modified residue (7) FUNCTION: Protein phosphatase inhibitor that specifically inhibits protein phosphatase 2A (PP2A) during mitosis. When phosphorylated at Ser-62 during mitosis, specifically interacts with PPP2R2D (PR55-delta) and inhibits its activity, leading to inactivation of PP2A, an essential condition to keep cyclin-B1-CDK1 activity high during M phase. May indirectly enhance GAP-43 expression by binding to the NGF-regulatory region of its mRNA (By similarity). {ECO:0000250}. PTM: Phosphorylation at Ser-62 by GWL during mitosis is essential for interaction with PPP2R2D (PR55-delta) and subsequent inactivation of PP2A (By similarity). Phosphorylated by PKA. {ECO:0000250, ECO:0000269|PubMed:11279279, ECO:0000269|PubMed:2845422}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Interacts (when phosphorylated at Ser-62) with PPP2R2D. Interacts with SNCA (By similarity). {ECO:0000250}. +Q80US4 ARP5_MOUSE Actin-related protein 5 605 67,845 Alternative sequence (2); Chain (1); Coiled coil (2); Cross-link (1); Frameshift (1) FUNCTION: Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. Involved in DNA double-strand break repair and UV-damage excision repair (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H9F9}. SUBUNIT: Component of the chromatin remodeling INO80 complex; specifically part of a complex module associated with the helicase ATP-binding domain and helicase C-terminal of INO80. {ECO:0000250}. +Q99JY9 ARP3_MOUSE Actin-related protein 3 (Actin-like protein 3) 418 47,357 Chain (1); Initiator methionine (1); Modified residue (5); Sequence conflict (1) FUNCTION: ATP-binding component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility. Seems to contact the pointed end of the daughter actin filament. In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA. The Arp2/3 complex promotes homologous recombination (HR) repair in response to DNA damage by promoting nuclear actin polymerization, leading to drive motility of double-strand breaks (DSBs). Plays a role in ciliogenesis. {ECO:0000250|UniProtKB:P61158}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P61158}. Cell projection {ECO:0000250|UniProtKB:P61158}. Nucleus {ECO:0000250|UniProtKB:P61158}. Note=In pre-apoptotic cells, colocalizes with MEFV in large specks (pyroptosomes). {ECO:0000250|UniProtKB:P61158}. SUBUNIT: Component of the Arp2/3 complex composed of ACTR2/ARP2, ACTR3/ARP3, ARPC1B/p41-ARC, ARPC2/p34-ARC, ARPC3/p21-ARC, ARPC4/p20-ARC and ARPC5/p16-ARC. Interacts with WHDC1. Interacts weakly with MEFV. {ECO:0000250|UniProtKB:P61158}. +P20443 ARRS_MOUSE S-arrestin (48 kDa protein) (Retinal S-antigen) (S-AG) (Rod photoreceptor arrestin) 403 44,930 Beta strand (23); Chain (1); Helix (3); Modified residue (1); Mutagenesis (4); Region (1); Sequence conflict (1); Turn (3) FUNCTION: Binds to photoactivated, phosphorylated RHO and terminates RHO signaling via G-proteins by competing with G-proteins for the same binding site on RHO (PubMed:9333241, PubMed:16421323). May play a role in preventing light-dependent degeneration of retinal photoreceptor cells (PubMed:16421323). {ECO:0000269|PubMed:16421323, ECO:0000269|PubMed:9333241}. SUBCELLULAR LOCATION: Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:16421323}. Membrane {ECO:0000269|PubMed:16421323}; Peripheral membrane protein {ECO:0000269|PubMed:16421323}. Note=Highly expressed in photoreceptor outer segments in light-exposed retina. Evenly distributed throughout rod photoreceptor cells in dark-adapted retina (By similarity). Predominantly dectected at the proximal region of photoreceptor outer segments, near disk membranes. {ECO:0000250|UniProtKB:P08168, ECO:0000250|UniProtKB:P10523}. SUBUNIT: Monomer. Homodimer. Homotetramer (PubMed:21288033). Interacts with RHO (via the phosphorylated C-terminus) (PubMed:26200343, PubMed:28753425). {ECO:0000269|PubMed:21288033, ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425}. DOMAIN: The C-terminus interferes with binding to non-phosphorylated RHO. Interaction with phosphorylated RHO triggers displacement of the C-terminus and leads to a conformation change that mediates high-affinity RHO binding. {ECO:0000250|UniProtKB:P08168}. TISSUE SPECIFICITY: Detected in retina (at protein level). {ECO:0000269|PubMed:16421323, ECO:0000269|PubMed:9333241}. +Q9D668 ARRD2_MOUSE Arrestin domain-containing protein 2 407 44,259 Chain (1); Sequence conflict (2) SUBUNIT: Interacts with WWP1 (via WW domains). {ECO:0000250|UniProtKB:Q8TBH0}. +Q3TYD4 ARSG_MOUSE Arylsulfatase G (ASG) (EC 3.1.6.-) 525 57,434 Active site (2); Alternative sequence (2); Binding site (3); Chain (1); Glycosylation (1); Metal binding (5); Modified residue (1); Sequence conflict (2); Signal peptide (1) FUNCTION: Displays arylsulfatase activity with pseudosubstrates at acidic pH, such as p-nitrocatechol sulfate. {ECO:0000250}. PTM: N-glycosylated. {ECO:0000250}.; PTM: The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity. {ECO:0000250}.; PTM: Glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Lysosome. Note=Previously observed endoplasmic reticulum localization is most likely due to folding/maturation problems for overexpressed proteins. {ECO:0000250}. +Q9D0U9 ARV1_MOUSE Protein ARV1 266 30,535 Chain (1); Transmembrane (3) TRANSMEM 139 159 Helical. {ECO:0000255}.; TRANSMEM 173 193 Helical. {ECO:0000255}.; TRANSMEM 228 248 Helical. {ECO:0000255}. FUNCTION: Plays a role as a mediator in the endoplasmic reticulum (ER) cholesterol and bile acid homeostasis (PubMed:20663892). Participates in sterol transport out of the ER and distribution into plasma membranes (PubMed:20663892). {ECO:0000269|PubMed:20663892}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9H2C2}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Ubiquitous. Highly expressed in lung. {ECO:0000269|PubMed:20663892}. +Q8C6Y6 ASB14_MOUSE Ankyrin repeat and SOCS box protein 14 587 64,883 Alternative sequence (2); Chain (1); Domain (1); Erroneous initiation (1); Repeat (11); Sequence conflict (4) Protein modification; protein ubiquitination. FUNCTION: May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000250}. DOMAIN: The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin-protein ligase complexes. {ECO:0000250}. +Q8VHS5 ASB16_MOUSE Ankyrin repeat and SOCS box protein 16 (ASB-16) 453 49,097 Chain (1); Domain (1); Repeat (7) Protein modification; protein ubiquitination. FUNCTION: May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000250}. DOMAIN: The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin-protein ligase complexes. {ECO:0000250}. +Q8VHA6 ASB18_MOUSE Ankyrin repeat and SOCS box protein 18 (ASB-18) 467 50,700 Alternative sequence (4); Chain (1); Domain (1); Repeat (9) Protein modification; protein ubiquitination. FUNCTION: May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000250}. DOMAIN: The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin-protein ligase complexes. {ECO:0000250}. +Q9WV74 ASB1_MOUSE Ankyrin repeat and SOCS box protein 1 (ASB-1) 336 37,232 Chain (1); Domain (1); Repeat (6) Protein modification; protein ubiquitination. FUNCTION: May play a role in testis development. Probable substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). {ECO:0000250}. SUBUNIT: Interacts with CUL5 and RNF7. {ECO:0000250}. DOMAIN: The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin-protein ligase complexes. {ECO:0000250}. TISSUE SPECIFICITY: Highest expression in testis, spleen, bone marrow and salivary gland. {ECO:0000269|PubMed:11111040, ECO:0000269|PubMed:11509662}. +Q9WV72 ASB3_MOUSE Ankyrin repeat and SOCS box protein 3 (ASB-3) 525 58,283 Chain (1); Domain (1); Repeat (10); Sequence conflict (3) Protein modification; protein ubiquitination. FUNCTION: Probable substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Recognizes TNFRSF1B (By similarity). {ECO:0000250}. SUBUNIT: Interacts with ELOB and TNFRSF1B. {ECO:0000250}. DOMAIN: The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin-protein ligase complexes. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed; highest expression in testis and spleen. {ECO:0000269|PubMed:11111040}. +Q9D1A4 ASB5_MOUSE Ankyrin repeat and SOCS box protein 5 (ASB-5) 329 36,282 Chain (1); Domain (1); Repeat (6) Protein modification; protein ubiquitination. FUNCTION: May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. May play a role in the initiation of arteriogenesis (By similarity). {ECO:0000250}. DOMAIN: The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin-protein ligase complexes. {ECO:0000250}. +Q91ZT9 ASB8_MOUSE Ankyrin repeat and SOCS box protein 8 (ASB-8) 288 31,735 Chain (1); Domain (1); Repeat (4); Sequence conflict (1) Protein modification; protein ubiquitination. FUNCTION: May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. DOMAIN: The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin-protein ligase complexes. {ECO:0000250}. +Q812A3 ANR23_MOUSE Ankyrin repeat domain-containing protein 23 (Diabetes-related ankyrin repeat protein) 306 34,348 Chain (1); Coiled coil (1); Region (1); Repeat (4) FUNCTION: May be involved in the energy metabolism. Could be a molecular link between myofibrillar stretch-induced signaling pathways and muscle gene expression. SUBCELLULAR LOCATION: Nucleus. Note=Sarcomeric I-band and some intercalated disks. {ECO:0000250}. SUBUNIT: Interacts with titin/TTN and MYPN. {ECO:0000250}. +O54754 AOXA_MOUSE Aldehyde oxidase 1 (EC 1.2.3.1) (Azaheterocycle hydroxylase 1) (EC 1.17.3.-) (Retinal oxidase) 1333 146,678 Active site (1); Binding site (10); Chain (1); Domain (2); Metal binding (8); Modified residue (1); Mutagenesis (3); Natural variant (9); Nucleotide binding (1); Region (2) FUNCTION: Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide, N-methylphthalazinium and phthalazine, as well as aldehydes, such as benzaldehyde, retinal, pyridoxal, and vanillin. Plays a role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. Participates in the bioactivation of prodrugs such as famciclovir, catalyzing the oxidation step from 6-deoxypenciclovir to penciclovir, which is a potent antiviral agent. Also plays a role in the reductive metabolism of the xenobiotic imidacloprid (IMI) via its nitroreduction to nitrosoguanidine (IMI-NNO) and aminoguanidine (IMI-NNH(2)). Is probably involved in the regulation of reactive oxygen species homeostasis. May be a prominent source of superoxide generation via the one-electron reduction of molecular oxygen. Also may catalyze nitric oxide (NO) production via the reduction of nitrite to NO with NADH or aldehyde as electron donor. May play a role in adipogenesis. Cannot use xanthine and hypoxanthine as substrate. {ECO:0000269|PubMed:10190983, ECO:0000269|PubMed:18671973, ECO:0000269|PubMed:19401776, ECO:0000269|PubMed:23462233}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10377246}. SUBUNIT: Homodimer. {ECO:0000269|PubMed:19401776}. TISSUE SPECIFICITY: Highest expression in esophagus. Moderately low expression in lung, liver, heart, Harderian gland, olfactory mucosa, skin and testis. In brain, expression is very high in choroid plexus, high in hind brain and low in hippocampus and cerebellum. In spinal cord expression is strongest in anterior horns. Low expression detected in spleen and eye. AOX1 expression in the livers of mice is approximately seven times greater in males than females. {ECO:0000269|PubMed:10377246, ECO:0000269|PubMed:23263164, ECO:0000269|PubMed:23462233, ECO:0000269|PubMed:9243637}. +Q8R146 APEH_MOUSE Acylamino-acid-releasing enzyme (AARE) (EC 3.4.19.1) (Acyl-peptide hydrolase) (APH) (Acylaminoacyl-peptidase) 732 81,581 Active site (3); Alternative sequence (1); Chain (1); Modified residue (3); Sequence conflict (1) FUNCTION: This enzyme catalyzes the hydrolysis of the N-terminal peptide bond of an N-acetylated peptide to generate an N-acetylated amino acid and a peptide with a free N-terminus. It preferentially cleaves off Ac-Ala, Ac-Met and Ac-Ser (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homotetramer. {ECO:0000250}. +P53995 APC1_MOUSE Anaphase-promoting complex subunit 1 (APC1) (Cyclosome subunit 1) (Mitotic checkpoint regulator) (Testis-specific gene 24 protein) 1944 215,994 Chain (1); Modified residue (17); Repeat (4); Sequence conflict (4) Protein modification; protein ubiquitination. FUNCTION: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By similarity). {ECO:0000250}. PTM: Phosphorylated. Phosphorylation on Ser-355 occurs specifically during mitosis (By similarity). {ECO:0000250}. SUBUNIT: The mammalian APC/C is composed at least of 14 distinct subunits ANAPC1, ANAPC2, CDC27/APC3, ANAPC4, ANAPC5, CDC16/APC6, ANAPC7, CDC23/APC8, ANAPC10, ANAPC11, CDC26/APC12, ANAPC13, ANAPC15 and ANAPC16 that assemble into a complex of at least 19 chains with a combined molecular mass of around 1.2 MDa; APC/C interacts with FZR1 and FBXO5. {ECO:0000250|UniProtKB:Q9H1A4}. TISSUE SPECIFICITY: Abundantly expressed in proliferating fibroblasts, juvenile testis, adult brain and epididymis. +B2RXR6 ANR44_MOUSE Serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit B (PP6-ARS-B) (Serine/threonine-protein phosphatase 6 regulatory subunit ARS-B) (Ankyrin repeat domain-containing protein 44) 993 107,385 Chain (1); Repeat (28); Sequence conflict (1) FUNCTION: Putative regulatory subunit of protein phosphatase 6 (PP6) that may be involved in the recognition of phosphoprotein substrates. {ECO:0000250}. SUBUNIT: Protein phosphatase 6 (PP6) holoenzyme is proposed to be a heterotrimeric complex formed by the catalytic subunit, a SAPS domain-containing subunit (PP6R) and an ankyrin repeat-domain containing regulatory subunit (ARS). Interacts with PPP6R1 (By similarity). {ECO:0000250}. +Q7TQC5 APTX_MOUSE Aprataxin (EC 3.1.11.7) (EC 3.1.12.2) (Forkhead-associated domain histidine triad-like protein) (FHA-HIT) 342 38,723 Active site (1); Alternative sequence (3); Chain (1); Domain (2); Erroneous initiation (1); Modified residue (3); Motif (2); Region (3); Sequence conflict (2); Site (4); Zinc finger (1) FUNCTION: DNA-binding protein involved in single-strand DNA break repair, double-strand DNA break repair and base excision repair. Resolves abortive DNA ligation intermediates formed either at base excision sites, or when DNA ligases attempt to repair non-ligatable breaks induced by reactive oxygen species. Catalyzes the release of adenylate groups covalently linked to 5'-phosphate termini, resulting in the production of 5'-phosphate termini that can be efficiently rejoined (PubMed:16964241). Also able to hydrolyze adenosine 5'-monophosphoramidate (AMP-NH(2)) and diadenosine tetraphosphate (AppppA), but with lower catalytic activity (By similarity). Likewise, catalyzes the release of 3'-linked guanosine (DNAppG) and inosine (DNAppI) from DNA, but has higher specific activity with 5'-linked adenosine (AppDNA) (By similarity). {ECO:0000250|UniProtKB:O74859, ECO:0000250|UniProtKB:Q7Z2E3, ECO:0000269|PubMed:16964241}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q7Z2E3}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q7Z2E3}. Note=Upon genotoxic stress, colocalizes with XRCC1 at sites of DNA damage. Colocalizes with MDC1 at sites of DNA double-strand breaks. Interaction with NCL is required for nucleolar localization (By similarity). {ECO:0000250|UniProtKB:Q7Z2E3}. SUBUNIT: Interacts with single-strand break repair proteins XRCC1, XRCC4, ADPRT and p53/TP53. Interacts with NCL. Interacts (via FHA-like domain) with MDC1 (phosphorylated). {ECO:0000250|UniProtKB:Q7Z2E3}. DOMAIN: The histidine triad, also called HIT motif, forms part of the binding loop for the alpha-phosphate of purine mononucleotide. {ECO:0000250|UniProtKB:Q7Z2E3}.; DOMAIN: The FHA-like domain mediates interaction with NCL; XRCC1 and XRCC4. {ECO:0000250}.; DOMAIN: The HIT domain is required for enzymatic activity. {ECO:0000250}.; DOMAIN: The C2H2-type zinc finger mediates DNA-binding. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. Expressed in heart, liver, kidney, spleen, lung, muscle, brain stem, spinal cord, cerebellum and brain. {ECO:0000269|PubMed:11586300}. +Q8CGZ0 CHERP_MOUSE Calcium homeostasis endoplasmic reticulum protein (SR-related CTD-associated factor 6) 936 106,169 Chain (1); Compositional bias (3); Cross-link (2); Domain (2); Modified residue (12); Repeat (1); Sequence conflict (1) FUNCTION: Involved in calcium homeostasis, growth and proliferation. {ECO:0000250|UniProtKB:Q8IWX8}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8IWX8}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8IWX8}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q8IWX8}. Note=Distributed throughout the cytoplasm and also localizes to the perinuclear region. Colocalizes with ITPR1 (By similarity). {ECO:0000250|UniProtKB:Q8IWX8}. +Q91XA9 CHIA_MOUSE Acidic mammalian chitinase (AMCase) (EC 3.2.1.14) (YNL) 473 52,003 Active site (1); Binding site (2); Chain (1); Disulfide bond (4); Domain (1); Erroneous initiation (1); Mutagenesis (1); Region (3); Sequence conflict (2); Signal peptide (1) FUNCTION: Degrades chitin and chitotriose. May participate in the defense against nematodes, fungi and other pathogens. Plays a role in T-helper cell type 2 (Th2) immune response. Contributes to the response to IL-13 and inflammation in response to IL-13. Stimulates chemokine production by pulmonary epithelial cells. Protects lung epithelial cells against apoptosis and promotes phosphorylation of AKT1. Its function in the inflammatory response and in protecting cells against apoptosis is inhibited by allosamidin, suggesting that the function of this protein depends on carbohydrate binding. Presence in saliva and gastric juice suggests a function as a digestive enzyme. {ECO:0000269|PubMed:11085997, ECO:0000269|PubMed:12133911, ECO:0000269|PubMed:15192232, ECO:0000269|PubMed:19076793}. SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasmic granule. Note=Detected in secretory granules of parotid acinar cells and gastric chief cells and secreted from them into saliva and gastric juice, respectively. SUBUNIT: Interacts with EGFR. {ECO:0000250}. TISSUE SPECIFICITY: Detected in macrophages and lung epithelial cells. Detected in the acinar cells of parotid gland and von Ebner's gland but not in submandibular and sublingual glands. Detected in gastric chief cells. Also present in parotid glandular saliva and gastric juice (at protein level). Highly expressed in submandibular gland (PubMed:11085997) and stomach. Highly expressed in parotid gland but not in submandibular and sublingual glands (PubMed:12133911). In tongue, expressed only in von Ebner's gland. Expressed at lower levels in lung. {ECO:0000269|PubMed:11085997, ECO:0000269|PubMed:12133911, ECO:0000269|PubMed:12971947, ECO:0000269|PubMed:15192232, ECO:0000269|PubMed:18824549}. +O35744 CHIL3_MOUSE Chitinase-like protein 3 (EC 3.2.1.52) (Beta-N-acetylhexosaminidase Ym1) (Chitinase-3-like protein 3) (ECF-L) (Eosinophil chemotactic cytokine) (Secreted protein Ym1) 398 44,458 Beta strand (15); Binding site (2); Chain (1); Disulfide bond (3); Helix (18); Sequence conflict (4); Signal peptide (1); Turn (5) FUNCTION: Lectin that binds saccharides with a free amino group, such as glucosamine or galactosamine. Binding to oligomeric saccharides is much stronger than binding to mono- or disaccharides. Also binds chitin and heparin. Has weak hexosaminidase activity but no chitinase activity. Has chemotactic activity for T-lymphocytes, bone marrow cells and eosinophils. May play a role in inflammation and allergy. {ECO:0000269|PubMed:10625674, ECO:0000269|PubMed:11297523, ECO:0000269|PubMed:11733538}. SUBCELLULAR LOCATION: Secreted. Rough endoplasmic reticulum lumen. Nucleus envelope. Cytoplasm. Cytoplasmic granule. Note=Predominantly localizes to the lumen of rough endoplasmic reticulum (rER) and nuclear envelope in alveolar macrophages. Localizes to the dilated lumen of rER in immature neutrophils in spleen and in cytoplasmic granules in peritoneal neutrophils. Detected in needle-shaped crystals present in the cytoplasm of bone marrow macrophages. TISSUE SPECIFICITY: Expressed in peritoneal cavity macrophages and in peritoneal and bone marrow-derived neutrophils. Abundantly expressed in bone marrow, with moderate levels detected in gastric antrum, spleen and in alveolar macrophages in lung. Not detected in brain, heart, liver, kidney, stomach, intestine, skeletal muscle, ovary, testis, thymus and lymph nodes (at protein level). Detected at low levels in bone marrow, spleen, thymus and lung. Barely detectable in intestine, kidney and coecum. {ECO:0000269|PubMed:10625674, ECO:0000269|PubMed:11297523, ECO:0000269|PubMed:11733538, ECO:0000269|PubMed:12101265, ECO:0000269|PubMed:15148607, ECO:0000269|PubMed:9828134}. +Q9D7Q1 CHIT1_MOUSE Chitotriosidase-1 (EC 3.2.1.14) (Chitinase-1) 464 51,112 Active site (1); Alternative sequence (2); Binding site (2); Chain (1); Disulfide bond (3); Domain (1); Mutagenesis (2); Region (3); Signal peptide (1) FUNCTION: Degrades chitin, chitotriose and chitobiose. May participate in the defense against nematodes and other pathogens (By similarity). {ECO:0000250, ECO:0000269|PubMed:16005164}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16005164}. Lysosome {ECO:0000250}. Note=A small proportion is lysosomal. {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in tongue, stomach, kidney, brain, skin, testis, and bone marrow. Low level of expression was found in lung, heart, spleen, small intestine, and liver. Not detectable in pancreas, salivary gland, large intestine, uterus, or peripheral blood mononuclear cells (PBMC). {ECO:0000269|PubMed:15923370, ECO:0000269|PubMed:16005164}. +O35280 CHK1_MOUSE Serine/threonine-protein kinase Chk1 (EC 2.7.11.1) (CHK1 checkpoint homolog) (Checkpoint kinase-1) 476 54,381 Active site (1); Alternative sequence (2); Binding site (1); Chain (1); Cross-link (1); Domain (1); Erroneous initiation (1); Modified residue (9); Mutagenesis (2); Nucleotide binding (1); Region (2); Sequence conflict (6) FUNCTION: Serine/threonine-protein kinase which is required for checkpoint-mediated cell cycle arrest and activation of DNA repair in response to the presence of DNA damage or unreplicated DNA. May also negatively regulate cell cycle progression during unperturbed cell cycles. This regulation is achieved by a number of mechanisms that together help to preserve the integrity of the genome. Recognizes the substrate consensus sequence [R-X-X-S/T]. Binds to and phosphorylates CDC25A, CDC25B and CDC25C. This inhibits their activity through proteasomal degradation, nucleo-cytoplasmic shuttling and inhibition by proteins of the 13-3-3 family. Inhibition of CDC25 leads to increased inhibitory tyrosine phosphorylation of CDK-cyclin complexes and blocks cell cycle progression. Also phosphorylates NEK6. Binds to and phosphorylates RAD51 at 'Thr-309', which promotes the release of RAD51 from BRCA2 and enhances the association of RAD51 with chromatin, thereby promoting DNA repair by homologous recombination. Phosphorylates multiple sites within the C-terminus of TP53, which promotes activation of TP53 by acetylation and promotes cell cycle arrest and suppression of cellular proliferation. Also promotes repair of DNA cross-links through phosphorylation of FANCE. Binds to and phosphorylates TLK1, which prevents the TLK1-dependent phosphorylation of the chromatin assembly factor ASF1A. This may enhance chromatin assembly both in the presence or absence of DNA damage. May also play a role in replication fork maintenance through regulation of PCNA (By similarity). May regulate the transcription of genes that regulate cell-cycle progression through the phosphorylation of histones. Phosphorylates histone H3.1 (to form H3T11ph), which leads to epigenetic inhibition of a subset of genes. May also phosphorylate RB1 to promote its interaction with the E2F family of transcription factors and subsequent cell cycle arrest. {ECO:0000250, ECO:0000269|PubMed:10859163, ECO:0000269|PubMed:10859164, ECO:0000269|PubMed:15261141, ECO:0000269|PubMed:18243098}. PTM: Phosphorylated by ATR in a RAD17-dependent manner in response to ultraviolet irradiation and inhibition of DNA replication. Phosphorylated by ATM in response to ionizing irradiation. ATM and ATR can both phosphorylate Ser-317 and Ser-345 and this results in enhanced kinase activity. Phosphorylation at Ser-345 induces a change in the conformation of the protein, activates the kinase activity and is a prerequisite for interaction with FBXO6 and subsequent ubiquitination at Lys-436. Phosphorylation at Ser-345 also increases binding to 14-3-3 proteins and promotes nuclear retention. Conversely, dephosphorylation at Ser-345 by PPM1D may contribute to exit from checkpoint mediated cell cycle arrest. Phosphorylation at Ser-280 by AKT1/PKB, may promote mono and/or diubiquitination. Also phosphorylated at undefined residues during mitotic arrest, resulting in decreased activity. {ECO:0000269|PubMed:15710331, ECO:0000269|PubMed:17376776}.; PTM: Ubiquitinated. Mono or diubiquitination promotes nuclear exclusion. The activated form (phosphorylated on Ser-345) is polyubiquitinated at Lys-436 by some SCF-type E3 ubiquitin ligase complex containing FBXO6 promoting its degradation (By similarity). Ubiquitination and degradation are required to terminate the checkpoint and ensure that activated CHEK1 does not accumulate as cells progress through S phase, when replication forks encounter transient impediments during normal DNA replication (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Note=Nuclear export is mediated at least in part by XPO1/CRM1. Also localizes to the centrosome specifically during interphase, where it may protect centrosomal CDC2 kinase from inappropriate activation by cytoplasmic CDC25B (By similarity). {ECO:0000250}. SUBUNIT: Interacts (phosphorylated by ATR) with RAD51. Interacts with and phosphorylates CLSPN, an adapter protein that regulates the ATR-dependent phosphorylation of CHEK1. Interacts with BRCA1. Interacts with and phosphorylates CDC25A, CDC25B and CDC25C. Interacts with FBXO6, which regulates CHEK1. Interacts with PPM1D, which regulates CHEK1 through dephosphorylation (By similarity). Interacts with TIMELESS; DNA damage-dependent (PubMed:23418588). Interacts with FEM1B; activates CHEK1 in response to stress. Interacts with TLK1. Interacts with XPO1 and YWHAZ. Interacts with CDK5RAP3; antagonizes CHEK1 (By similarity). {ECO:0000250|UniProtKB:O14757, ECO:0000269|PubMed:23418588}. DOMAIN: The autoinhibitory region (AIR) inhibits the activity of the kinase domain. {ECO:0000250}. TISSUE SPECIFICITY: Found in all adult tissues tested. Elevated expression in testis, lung and spleen. 15.5 day old embryos show ubiquitous expression with strong expression in brain, liver, kidney, pancreas, intestine, thymus and lung. {ECO:0000269|PubMed:9278511}. +Q9Z265 CHK2_MOUSE Serine/threonine-protein kinase Chk2 (EC 2.7.11.1) (CHK2 checkpoint homolog) (Checkpoint kinase 2) 546 61,088 Active site (1); Binding site (2); Chain (1); Domain (2); Modified residue (8); Mutagenesis (1); Nucleotide binding (3); Region (1) FUNCTION: Serine/threonine-protein kinase which is required for checkpoint-mediated cell cycle arrest, activation of DNA repair and apoptosis in response to the presence of DNA double-strand breaks. May also negatively regulate cell cycle progression during unperturbed cell cycles. Following activation, phosphorylates numerous effectors preferentially at the consensus sequence [L-X-R-X-X-S/T]. Regulates cell cycle checkpoint arrest through phosphorylation of CDC25A, CDC25B and CDC25C, inhibiting their activity. Inhibition of CDC25 phosphatase activity leads to increased inhibitory tyrosine phosphorylation of CDK-cyclin complexes and blocks cell cycle progression. May also phosphorylate NEK6 which is involved in G2/M cell cycle arrest. Regulates DNA repair through phosphorylation of BRCA2, enhancing the association of RAD51 with chromatin which promotes DNA repair by homologous recombination. Also stimulates the transcription of genes involved in DNA repair (including BRCA2) through the phosphorylation and activation of the transcription factor FOXM1. Regulates apoptosis through the phosphorylation of p53/TP53, MDM4 and PML. Phosphorylation of p53/TP53 at 'Ser-20' by CHEK2 may alleviate inhibition by MDM2, leading to accumulation of active p53/TP53. Phosphorylation of MDM4 may also reduce degradation of p53/TP53. Also controls the transcription of pro-apoptotic genes through phosphorylation of the transcription factor E2F1. Tumor suppressor, it may also have a DNA damage-independent function in mitotic spindle assembly by phosphorylating BRCA1. Its absence may be a cause of the chromosomal instability observed in some cancer cells. Promotes the CCAR2-SIRT1 association and is required for CCAR2-mediated SIRT1 inhibition (By similarity). {ECO:0000250|UniProtKB:O96017, ECO:0000269|PubMed:12192050, ECO:0000269|PubMed:25619829}. PTM: Phosphorylated. Phosphorylated at Ser-82 by PLK3 in response to DNA damage, promoting phosphorylation at Thr-77 by ATM and the G2/M transition checkpoint. Phosphorylation at Thr-77 induces homodimerization. Autophosphorylates at Thr-387 and Thr-391 in the T-loop/activation segment upon dimerization to become fully active. DNA damage-induced autophosphorylation at Ser-383 induces CUL1-mediated ubiquitination and regulates the pro-apoptotic function. Phosphorylation at Ser-460 also regulates ubiquitination. Phosphorylated by PLK4 (By similarity). {ECO:0000250}.; PTM: Ubiquitinated. CUL1-mediated ubiquitination regulates the pro-apoptotic function. Ubiquitination may also regulate protein stability. Ubiquitinated by RNF8 via 'Lys-48'-linked ubiquitination (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, PML body {ECO:0000250}. Nucleus, nucleoplasm. Note=Recruited into PML bodies together with TP53. {ECO:0000250}. SUBUNIT: Homodimer. Homodimerization is part of the activation process but the dimer may dissociate following activation. Interacts with PML. Interacts with TP53. Interacts with RB1; phosphorylates RB1. Interacts with BRCA1. Interacts (phosphorylated at Thr-68) with MDC1; requires ATM-mediated phosphorylation of CHEK2. Interacts with TP53BP1; modulates CHEK2 phosphorylation at Thr-68 in response to ionizing radiation. Interacts with CDC25A; phosphorylates CDC25A and mediates its degradation in response to ionizing radiation. Interacts with CUL1; mediates CHEK2 ubiquitination and regulation. Interacts with CDKN2AIP. Interacts (via protein kinase domain) with CCAR2 (via N-terminus). Interacts with SIRT1 (By similarity). {ECO:0000250|UniProtKB:O96017}. TISSUE SPECIFICITY: Ubiquitously expressed with higher levels in the thymus, spleen and colon (at protein level). {ECO:0000269|PubMed:12192050}. +Q3V079 BBOF1_MOUSE Basal body-orientation factor 1 (Coiled-coil domain-containing protein 176) 533 62,499 Chain (1); Coiled coil (2); Sequence conflict (1) FUNCTION: Basal body protein required in multiciliate cells to align and maintain cilia orientation in response to flow. May act by mediating a maturation step that stabilizes and aligns cilia orientation. Not required to respond to planar cell polarity (PCP) or flow-based orientation cues (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250}. Note=Localizes to a polar structure adjacent to the basal body. {ECO:0000250}. +Q91YE5 BAZ2A_MOUSE Bromodomain adjacent to zinc finger domain protein 2A (Transcription termination factor I-interacting protein 5) (TTF-I-interacting protein 5) (Tip5) 1889 209,618 Alternative sequence (2); Chain (1); Coiled coil (1); Compositional bias (2); Cross-link (5); DNA binding (4); Domain (3); Modified residue (16); Mutagenesis (3); Sequence conflict (1); Zinc finger (1) FUNCTION: Essential component of the NoRC (nucleolar remodeling complex) complex, a complex that mediates silencing of a fraction of rDNA by recruiting histone-modifying enzymes and DNA methyltransferases, leading to heterochromatin formation and transcriptional silencing. In the complex, it plays a central role by being recruited to rDNA and by targeting chromatin modifying enzymes such as HDAC1, leading to repress RNA polymerase I transcription. Recruited to rDNA via its interaction with TTF1 and its ability to recognize and bind histone H4 acetylated on 'Lys-16' (H4K16ac), leading to deacetylation of H4K5ac, H4K8ac, H4K12ac but not H4K16ac. Specifically binds pRNAs, 150-250 nucleotide RNAs that are complementary in sequence to the rDNA promoter; pRNA-binding is required for heterochromatin formation and rDNA silencing. {ECO:0000269|PubMed:11532953, ECO:0000269|PubMed:12198165, ECO:0000269|PubMed:16085498}. PTM: Ubiquitinated. Deubiquitinated by USP21 leading to its stabilization. {ECO:0000250|UniProtKB:Q9UIF9}.; PTM: Acetylation at Lys-672 by KAT8/MOF promotes its dissociation from pRNA, affecting heterochromatin formation, nucleosome positioning and rDNA silencing. Deacetylation by SIRT1 in late S phase enhances pRNA-binding, allowing de novo DNA methylation and heterochromatin formation. Acetylation is high during S phase and declines to background levels in late S phase when the silent copies of rRNA genes are replicated. {ECO:0000269|PubMed:19578370}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11532953, ECO:0000269|PubMed:12198165, ECO:0000269|PubMed:16085498, ECO:0000269|PubMed:18600236, ECO:0000269|PubMed:19578370}. Note=Colocalizes with the basal RNA polymerase I transcription factor UBF in the nucleolus. SUBUNIT: Component of the NoRC complex, at least composed of SMARCA5/SNF2H and BAZ2A/TIP5. Interacts with TTF1; required for recruitment of the NoRC complex to rDNA. Interacts with DNMT1, DNM3B, HDAC1 and SIN3A. Interacts with BEND3 and USP21 (By similarity). {ECO:0000250|UniProtKB:Q9UIF9, ECO:0000269|PubMed:11532953, ECO:0000269|PubMed:12198165, ECO:0000269|PubMed:15292447, ECO:0000269|PubMed:16085498}. DOMAIN: The bromo domain and the PHD-type zinc finger recognize and bind histone H4 acetylated on 'Lys-16' (H4K16ac). These 2 domains play a central role in the recruitment of chromatin silencing proteins such as DNMT1, DNMT3B and HDAC1.; DOMAIN: The MBD (methyl-CpG-binding) domain, also named TAM domain, specifically recognizes and binds a conserved stem-loop structure the association within pRNA. Binding to pRNA induces a conformational change of BAZ2A/TIP5 and is essential for targeting the NoRC complex to the nucleolus. +O35284 BATF_MOUSE Basic leucine zipper transcriptional factor ATF-like (B-cell-activating transcription factor) (B-ATF) 125 14,065 Chain (1); Domain (1); Modified residue (2); Mutagenesis (8); Region (2) FUNCTION: AP-1 family transcription factor that controls the differentiation of lineage-specific cells in the immune system: specifically mediates the differentiation of T-helper 17 cells (Th17), follicular T-helper cells (TfH), CD8(+) dendritic cells and class-switch recombination (CSR) in B-cells. Acts via the formation of a heterodimer with JUNB that recognizes and binds DNA sequence 5'-TGA[CG]TCA-3'. The BATF-JUNB heterodimer also forms a complex with IRF4 (or IRF8) in immune cells, leading to recognition of AICE sequence (5'-TGAnTCA/GAAA-3'), an immune-specific regulatory element, followed by cooperative binding of BATF and IRF4 (or IRF8) and activation of genes. Controls differentiation of T-helper cells producing interleukin-17 (Th17 cells) by binding to Th17-associated gene promoters: regulates expression of the transcription factor RORC itself and RORC target genes such as IL17 (IL17A or IL17B). Also involved in differentiation of follicular T-helper cells (TfH) by directing expression of BCL6 and MAF. In B-cells, involved in class-switch recombination (CSR) by controlling the expression of both AICDA and of germline transcripts of the intervening heavy-chain region and constant heavy-chain region (I(H)-C(H)). Following infection, can participate in CD8(+) dendritic cell differentiation via interaction with IRF4 and IRF8 to mediate cooperative gene activation. Regulates effector CD8(+) T-cell differentiation by regulating expression of SIRT1. Following DNA damage, part of a differentiation checkpoint that limits self-renewal of hematopoietic stem cells (HSCs): up-regulated by STAT3, leading to differentiation of HSCs, thereby restricting self-renewal of HSCs. {ECO:0000269|PubMed:11466704, ECO:0000269|PubMed:12594265, ECO:0000269|PubMed:19578362, ECO:0000269|PubMed:20421391, ECO:0000269|PubMed:21572431, ECO:0000269|PubMed:22001828, ECO:0000269|PubMed:22385964, ECO:0000269|PubMed:22983707, ECO:0000269|PubMed:22992523, ECO:0000269|PubMed:22992524, ECO:0000269|PubMed:23021777}. PTM: Phosphorylated on serine and threonine residues and at least one tyrosine residue. Phosphorylation at Ser-43 inhibit DNA binding activity and transforms it as a negative regulator of AP-1 mediated transcription. {ECO:0000269|PubMed:12809553}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Present in the nucleus and cytoplasm, but shows increased nuclear translocation after activation of T-cells. SUBUNIT: Heterodimer; mainly heterodimerizes with JUNB. The BATF-JUNB heterodimer interacts with IRF4 and IRF8. Interacts (via bZIP domain) with IRF4 and IRF8; the interaction is direct. Also forms heterodimers with JUN and JUND. Also Interacts with IFI35. {ECO:0000269|PubMed:12809553, ECO:0000269|PubMed:19578362, ECO:0000269|PubMed:22983707, ECO:0000269|PubMed:22992523, ECO:0000269|PubMed:22992524}. TISSUE SPECIFICITY: Detected in postnatal and adult lymphoid tissues such as thymus, spleen and lymph nodes. In thymus most concentrated expression is found in the immediate cortical layer. Differentially expressed during T-cell development in thymus. Highly expressed in Th17, Th1 and Th2 cells and in activated B-cells. {ECO:0000269|PubMed:11466704, ECO:0000269|PubMed:19578362, ECO:0000269|PubMed:20421391}. +Q99ML1 BBC3_MOUSE Bcl-2-binding component 3 (p53 up-regulated modulator of apoptosis) 193 20,749 Chain (1); Helix (1); Modified residue (1); Motif (1) FUNCTION: Essential mediator of p53/TP53-dependent and p53/TP53-independent apoptosis. Functions by promoting partial unfolding of BCL2L1 and dissociation of BCL2L1 from p53/TP53 (By similarity). Regulates ER stress-induced neuronal apoptosis. {ECO:0000250, ECO:0000269|PubMed:21159964, ECO:0000269|PubMed:22761832}. SUBCELLULAR LOCATION: Mitochondrion. Note=Localized to the mitochondria in order to induce cytochrome c release. {ECO:0000250}. SUBUNIT: Interacts with MCL1 and BCL2A1 (PubMed:18589438, PubMed:18462686). Interacts with BCL2 and BCL2L1/BCL-XL (By similarity). Interacts (via BH3 domain) with NOL3 (via CARD domain); this interaction prevents BBC3 association with BCL2 and results in CASP8 activation (By similarity). {ECO:0000250|UniProtKB:Q80ZG6, ECO:0000250|UniProtKB:Q9BXH1, ECO:0000269|PubMed:18462686, ECO:0000269|PubMed:18589438}. DOMAIN: The BH3 motif is intrinsically disordered. {ECO:0000250}. +Q9D2V7 CORO7_MOUSE Coronin-7 (Crn7) (70 kDa WD repeat tumor rejection antigen homolog) 922 100,812 Chain (1); Cross-link (1); Modified residue (3); Repeat (8); Sequence conflict (4) FUNCTION: F-actin regulator involved in anterograde Golgi to endosome transport: upon ubiquitination via 'Lys-33'-linked ubiquitin chains by the BCR(KLHL20) E3 ubiquitin ligase complex, interacts with EPS15 and localizes to the trans-Golgi network, where it promotes actin polymerization, thereby facilitating post-Golgi trafficking. May play a role in the maintenance of the Golgi apparatus morphology (By similarity). {ECO:0000250}. PTM: The membrane-associated form is phosphorylated on tyrosine residues.; PTM: Ubiquitinated via 'Lys-33'-linked ubiquitin chains by the BCR(KLHL20) E3 ubiquitin ligase complex: 'Lys-33'-linked ubiquitination promotes interaction with EPS15 and facilitates actin polymerization at the trans-Golgi network, thereby facilitating post-Golgi trafficking. Deubiquitinated by ZRANB1/TRABID (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:15327992}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Cytoplasmic vesicle {ECO:0000269|PubMed:15327992}. Cytoplasm, cytosol {ECO:0000269|PubMed:15327992}. Note=Predominantly cytosolic. Detected on vesicle-like cytoplasmic structures and on the cis-Golgi. Not associated with actin filaments. SUBUNIT: Interacts with clathrin adapter AP1 complex. This interaction takes place at Golgi membranes and not AP1-positive endosomal membranes. Interacts (when ubiquitinated at Lys-469) with EPS15 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: In the adult, widely expressed with highest levels in brain, thymus and kidney and low levels in skeletal and heart muscle. Not expressed in lung. In the eye, strongly expressed in the outer plexiform layer of the retina. In the intestine, expressed both in terminally differentiated epithelial cells and in crypt epithelium. In the embryo, strongest expression is seen in brain, thymus, intestine, apical epidermal layers of the skin and developing lens fibers of the eye. {ECO:0000269|PubMed:15327992}. +Q9EQ32 BCAP_MOUSE Phosphoinositide 3-kinase adapter protein 1 (B-cell adapter for phosphoinositide 3-kinase) (B-cell phosphoinositide 3-kinase adapter protein 1) 811 90,928 Alternative sequence (3); Chain (1); Compositional bias (1); Domain (1); Modified residue (11); Mutagenesis (4); Region (1); Sequence conflict (6) FUNCTION: Signaling adapter that contributes to B-cell development by linking B-cell receptor (BCR) signaling to the phosphoinositide 3-kinase (PI3K)-Akt signaling pathway. Has a complementary role to the BCR coreceptor CD19, coupling BCR and PI3K activation by providing a docking site for the PI3K subunit PIK3R1. Alternatively, links Toll-like receptor (TLR) signaling to PI3K activation, a process preventing excessive inflammatory cytokine production. Also involved in the activation of PI3K in natural killer cells. May be involved in the survival of mature B-cells via activation of REL. {ECO:0000269|PubMed:11781242, ECO:0000269|PubMed:11877477, ECO:0000269|PubMed:12833156, ECO:0000269|PubMed:18025150, ECO:0000269|PubMed:18337558, ECO:0000269|PubMed:22187458, ECO:0000269|PubMed:22187460}. PTM: Constitutively phosphorylated. Phosphorylated on tyrosine residues in C-terminal region by ABL1 (By similarity). Phosphorylated on tyrosine residues within the YXXM motifs by BTK and SYK. Isoform 1 and isoform 2 are phosphorylated on tyrosine residues, most likely within the YXXM motifs, via CD19 activation. Toll-like receptor activation induces appearance of a phosphorylated form associated with membranes. {ECO:0000250, ECO:0000269|PubMed:11163197, ECO:0000269|PubMed:18025150, ECO:0000269|PubMed:20728433, ECO:0000269|PubMed:22187458, ECO:0000269|PubMed:22187460}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22187458}. Cell membrane {ECO:0000305|PubMed:22187458}; Peripheral membrane protein {ECO:0000305|PubMed:22187458}. SUBUNIT: Homooligomer (Probable). Interacts (phosphorylated on tyrosine residues within YXXM motifs) with PIK3R1 (via SH2 domain); required for BCR- and TLR-mediated activation of phosphoinositide 3-kinase. Interacts (via polyproline C-terminal region) with ABI1 (via SH3 domain); the interaction promotes phosphorylation of PIK3AP1 by ABL1 (By similarity). May interact with MYD88 and TIRAP. {ECO:0000250, ECO:0000269|PubMed:11163197, ECO:0000269|PubMed:18025150, ECO:0000269|PubMed:22187460, ECO:0000305}. DOMAIN: The DBB domain is required for dimerization. TISSUE SPECIFICITY: Predominantly expressed in spleen (at protein level). Expressed at lower levels in thymus, liver and lung. Expressed in B-cells, macrophages and natural killer (NK) cells. {ECO:0000269|PubMed:11163197, ECO:0000269|PubMed:18337558}. +Q61140 BCAR1_MOUSE Breast cancer anti-estrogen resistance protein 1 (CRK-associated substrate) (p130cas) 874 94,285 Alternative sequence (1); Chain (1); Compositional bias (2); Domain (1); Helix (4); Modified residue (13); Motif (1); Region (2); Sequence conflict (2) FUNCTION: Docking protein which plays a central coordinating role for tyrosine kinase-based signaling related to cell adhesion. Implicated in induction of cell migration (By similarity). Has been shown to be essential in cardiovascular development during embryogenesis. {ECO:0000250}. PTM: PTK2/FAK1 activation mediates phosphorylation at the YDYVHL motif; phosphorylation is most likely catalyzed by SRC family members. SRC-family kinases are recruited to the phosphorylated sites and can phosphorylate other tyrosine residues. Tyrosine phosphorylation is triggered by integrin mediated adhesion of cells to the extracellular matrix (By similarity). {ECO:0000250}.; PTM: Dephosphorylated by PTPN14 at Tyr-132. {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Unphosphorylated form localizes in the cytoplasm and can move to the membrane upon tyrosine phosphorylation. {ECO:0000250}. SUBUNIT: Forms complexes in vivo with PTK2/FAK1, adapter protein CRKL and LYN kinase. Can heterodimerize with NEDD9. Interacts with activated CSPG4. Interacts with BMX, INPPL1/SHIP2 and PEAK1 (By similarity). Part of a collagen stimulated complex involved in cell migration composed of CDC42, CRK, TNK2 and BCAR1/p130cas (By similarity). Interacts with BCAR3, the interaction regulates adhesion-dependent serine phosphorylation. Interacts with NPHP1, PTK2B/PYK2 and SH2D3C. {ECO:0000250, ECO:0000269|PubMed:10438950, ECO:0000269|PubMed:10692442, ECO:0000269|PubMed:10739664, ECO:0000269|PubMed:10896938, ECO:0000269|PubMed:12486027, ECO:0000269|PubMed:7479864}. DOMAIN: Contains a central domain (substrate domain) containing multiple potential SH2-binding sites and a C-terminal domain containing a divergent helix-loop-helix (HLH) motif. The SH2-binding sites putatively bind CRK, NCK and ABL SH2 domains. The HLH motif is absolutely required for the induction of pseudohyphal growth in yeast and mediates heterodimerization with NEDD9.; DOMAIN: A serine-rich region promotes activation of the serum response element (SRE). {ECO:0000250}.; DOMAIN: The SH3 domain is necessary for the localization of the protein to focal adhesions and interacts with one proline-rich region of PTK2/FAK1. +Q8CCN5 BCAS3_MOUSE Breast carcinoma-amplified sequence 3 homolog (K20D4) (Protein rudhira) 928 101,021 Alternative sequence (2); Chain (1); Cross-link (2); Erroneous termination (1); Modified residue (7); Sequence conflict (2) FUNCTION: Functions synergistically with PELP1 as a transcriptional coactivator of estrogen receptor-responsive genes. Stimulates histone acetyltransferase activity. Binds to chromatin (By similarity). Plays a role in angiogenesis. Participates in the regulation of cell polarity and directional endothelial cell migration by mediating both the activation and recruitment of CDC42 and the reorganization of the actin cytoskeleton at the cell leading edge. Promotes filipodia formation. {ECO:0000250|UniProtKB:Q9H6U6, ECO:0000269|PubMed:22300583}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H6U6}. Cytoplasm {ECO:0000269|PubMed:16099728, ECO:0000269|PubMed:22300583}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:22300583}. Note=Associates with chromatin. Recruited to estrogen receptor-induced promoters in a PELP1-dependent manner (By similarity). Localizes in the cytoplasm in stationary cells. Translocates from the cytoplasm to the leading edge in motile cells. Colocalizes with microtubules and intermediate filaments in both stationary and motile cells. {ECO:0000250|UniProtKB:Q9H6U6, ECO:0000269|PubMed:22300583}. SUBUNIT: Interacts with histone H3, ESR1, KAT2B and PELP1; the interactions occur in a estrogen-dependent manner. Interacts with beta-tubulin and VIM. {ECO:0000250|UniProtKB:Q9H6U6}. DOMAIN: Has been proposed to contain 7 WD repeats. This prediction could not be reproduced. {ECO:0000305|PubMed:16099728}. TISSUE SPECIFICITY: Expressed in blood islands and yolk sac blood islands (at protein level). Highly expressed in mammary tumors. Expressed in eostrogen-induced epithelial cells of mammary glands. Expressed in brain, heart, kidney, lung, liver and spleen. Expressed in embryonic stem cells, embryoid bodies, endothelial cells and fibroblasts. {ECO:0000269|PubMed:16099728, ECO:0000269|PubMed:16617102, ECO:0000269|PubMed:17505058}. +Q9JJS6 BCDO1_MOUSE Beta,beta-carotene 15,15'-dioxygenase (EC 1.13.11.63) (Beta-carotene dioxygenase 1) (Beta-carotene oxygenase 1) 566 63,864 Chain (1); Metal binding (4); Sequence conflict (1) Cofactor metabolism; retinol metabolism. FUNCTION: Symmetrically cleaves beta-carotene into two molecules of retinal using a dioxygenase mechanism. {ECO:0000250|UniProtKB:Q9HAY6}. TISSUE SPECIFICITY: Expressed in liver, kidney, small intestine and testis. {ECO:0000269|PubMed:11092891}. +Q9CQI6 COTL1_MOUSE Coactosin-like protein 142 15,944 Beta strand (6); Chain (1); Domain (1); Helix (7); Initiator methionine (1); Modified residue (3); Region (1); Turn (2) FUNCTION: Binds to F-actin in a calcium-independent manner. Has no direct effect on actin depolymerization. Acts as a chaperone for ALOX5 (5LO), influencing both its stability and activity in leukotrienes synthesis (By similarity). {ECO:0000250, ECO:0000269|PubMed:11785969}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14019}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q14019}. Nucleus {ECO:0000250|UniProtKB:Q14019}. SUBUNIT: Interacts with 5-lipoxygenase (ALOX5/5LO) in a calcium-independent manner. Binds to F-actin with a stoichiometry of 1:2 (By similarity). {ECO:0000250}. +Q9CWF6 BBS2_MOUSE Bardet-Biedl syndrome 2 protein homolog 721 79,932 Chain (1); Coiled coil (1) FUNCTION: The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor, which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane and binds to RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the Rab8-GTP localizes to the cilium and promotes docking and fusion of carrier vesicles to the base of the ciliary membrane. The BBSome complex, together with the LTZL1, controls SMO ciliary trafficking and contributes to the sonic hedgehog (SHH) pathway regulation. Required for proper BBSome complex assembly and its ciliary localization (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell projection, cilium membrane {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000250}. SUBUNIT: Part of BBSome complex, that contains BBS1, BBS2, BBS4, BBS5, BBS7, BBS8/TTC8, BBS9 and BBIP10. Interacts (via C-terminus) with BBS7. Interacts (via coiled coil domain) with MKKS. Interacts with CCDC28B. {ECO:0000269|PubMed:22072986}. +Q9CZQ9 BBS5_MOUSE Bardet-Biedl syndrome 5 protein homolog 341 38,862 Chain (1) FUNCTION: The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor, which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane and binds to RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the Rab8-GTP localizes to the cilium and promotes docking and fusion of carrier vesicles to the base of the ciliary membrane. The BBSome complex, together with the LTZL1, controls SMO ciliary trafficking and contributes to the sonic hedgehog (SHH) pathway regulation. Required for BBSome complex ciliary localization but not for the proper complex assembly (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell projection, cilium membrane {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:15137946}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000250}. Note=Localizes to basal bodies. SUBUNIT: PPart of BBSome complex, that contains BBS1, BBS2, BBS4, BBS5, BBS7, BBS8/TTC8, BBS9 and BBIP10. Binds to phosphoinositides. Interacts with CCDC28B. Interacts with SMO; the interaction is indicative for the association of SMO with the BBsome complex to facilitate ciliary localization of SMO. Interacts with PKD1 (By similarity). {ECO:0000250|UniProtKB:Q8N3I7, ECO:0000269|PubMed:22072986}. +O55028 BCKD_MOUSE [3-methyl-2-oxobutanoate dehydrogenase [lipoamide]] kinase, mitochondrial (EC 2.7.11.4) (Branched-chain alpha-ketoacid dehydrogenase kinase) (BCKD-kinase) (BCKDHKIN) 412 46,588 Chain (1); Domain (1); Modified residue (6); Transit peptide (1) FUNCTION: Catalyzes the phosphorylation and inactivation of the branched-chain alpha-ketoacid dehydrogenase complex, the key regulatory enzyme of the valine, leucine and isoleucine catabolic pathways. Key enzyme that regulate the activity state of the BCKD complex. {ECO:0000250|UniProtKB:O14874}. PTM: Autophosphorylated. {ECO:0000250|UniProtKB:O14874}. SUBCELLULAR LOCATION: Mitochondrion matrix. Mitochondrion {ECO:0000250|UniProtKB:O14874}. SUBUNIT: Monomer. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. +Q8CGN4 BCOR_MOUSE BCL-6 corepressor (BCoR) 1759 192,631 Alternative sequence (2); Chain (1); Cross-link (4); Erroneous initiation (1); Modified residue (12); Region (2); Repeat (3); Sequence conflict (17) FUNCTION: Transcriptional corepressor. May specifically inhibit gene expression when recruited to promoter regions by sequence-specific DNA-binding proteins such as BCL6 and MLLT3. This repression may be mediated at least in part by histone deacetylase activities which can associate with this corepressor. Involved in the repression of TFAP2A; impairs binding of BCL6 and KDM2B to TFAP2A promoter regions. Via repression of TFAP2A acts as a negative regulator of osteo-dentiogenic capacity in adult stem cells; the function implies inhibition of methylation on histone H3 'Lys-4' (H3K4me3) and 'Lys-36' (H3K36me2) (By similarity). {ECO:0000250, ECO:0000269|PubMed:12776190}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12776190}. SUBUNIT: Interacts with CPNE4 (via VWFA domain) (PubMed:12522145). Isoform 1 may interact with MLLT3/AF9 (PubMed:12776190). Interacts with BCL6; the interaction is direct. Forms ternary complexes with BCL6 and SMRT/NCOR2 on selected target genes promoters; potently repress expression. Can interact with HDAC1, HDAC3 and HDAC5. Interacts with PCGF1; the interaction is direct. Interacts with KDM2B. Component of an approximately 800 kDa repressive BCOR complex at least composed of BCOR, RYBP, PCGF1, RING1, RNF2/RING2, KDM2B and SKP1 (By similarity). {ECO:0000250|UniProtKB:Q6W2J9, ECO:0000269|PubMed:12522145, ECO:0000269|PubMed:12776190}. TISSUE SPECIFICITY: Expressed in heart, liver, lung, skeletal muscle, spleen and testis. {ECO:0000269|PubMed:12776190}. +Q6PAJ1 BCR_MOUSE Breakpoint cluster region protein (EC 2.7.11.1) 1270 143,072 Chain (1); Compositional bias (2); Domain (4); Modified residue (22); Region (1); Sequence conflict (2) FUNCTION: GTPase-activating protein for RAC1 and CDC42. Promotes the exchange of RAC or CDC42-bound GDP by GTP, thereby activating them. Displays serine/threonine kinase activity (By similarity). {ECO:0000250}. PTM: Autophosphorylated. Phosphorylated by FES/FPS on tyrosine residues, leading to down-regulation of the BCR kinase activity. Phosphorylation at Tyr-178 by HCK is important for interaction with GRB2 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000269|PubMed:25331951}. SUBUNIT: Homotetramer. Interacts with PDZK1. Interacts with HCK, FES/FPS, ABL1, PIK3R1 and GRB2 (By similarity). May interact with CCPG1. Interacts with SH2D5 (PubMed:25331951). {ECO:0000250|UniProtKB:P11274, ECO:0000269|PubMed:25331951}. DOMAIN: The region involved in binding to ABL1 SH2-domain is rich in serine residues and needs to be Ser/Thr phosphorylated prior to SH2 binding. This region is essential for the activation of the ABL1 tyrosine kinase (By similarity). {ECO:0000250}.; DOMAIN: The DH domain is involved in interaction with CCPG1. TISSUE SPECIFICITY: Expressed in brain. {ECO:0000269|PubMed:25331951}. +Q921K9 BCL7B_MOUSE B-cell CLL/lymphoma 7 protein family member B 202 22,238 Alternative sequence (2); Chain (1); Erroneous initiation (1); Modified residue (7); Sequence conflict (2) FUNCTION: Positive regulator of apoptosis. Plays a role in the Wnt signaling pathway, negatively regulating the expression of Wnt signaling components CTNNB1 and HMGA1 (By similarity). Involved in cell cycle progression, maintenance of the nuclear structure and stem cell differentiation (By similarity). May play a role in lung tumor development or progression. {ECO:0000250|UniProtKB:Q9BQE9, ECO:0000269|PubMed:14647414}. +Q67FY2 BCL9L_MOUSE B-cell CLL/lymphoma 9-like protein (B-cell lymphoma 9-like protein) (BCL9-like protein) (BCL9-related beta-catenin-binding protein) (Protein BCL9-2) 1494 156,680 Alternative sequence (1); Chain (1); Compositional bias (4); Cross-link (1); Modified residue (26); Region (1); Sequence conflict (1) FUNCTION: Transcriptional regulator that acts as an activator. Promotes beta-catenin transcriptional activity. Plays a role in tumorigenesis. Enhances the neoplastic transforming activity of CTNNB1. {ECO:0000269|PubMed:15371335}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15574752}. Note=localized also in punctate nuclear bodies as well in the cytoplasm. Colocalizes with CTNNB1. SUBUNIT: Found in a complex with CDC73; CTNNB1 and PYGO1 (By similarity). Interacts with CTNNB1. {ECO:0000250, ECO:0000269|PubMed:15371335, ECO:0000269|PubMed:15574752, ECO:0000269|PubMed:17052462}. DOMAIN: Tne C-terminal domain is important for its transactivation activity. TISSUE SPECIFICITY: Expressed in kidney, liver, lung, testis, brain, spleen, heart and skeletal muscle. Highly expressed in numerous colorectal tumors compared to corresponding non-cancerous tissues. {ECO:0000269|PubMed:15574752}. +E9Q6J5 BD1L1_MOUSE Biorientation of chromosomes in cell division protein 1-like 1 3032 327,453 Alternative sequence (2); Chain (1); Cross-link (2); DNA binding (1); Erroneous initiation (3); Modified residue (31); Sequence conflict (4) FUNCTION: Component of the fork protection machinery required to protect stalled/damaged replication forks from uncontrolled DNA2-dependent resection. Acts by stabilizing RAD51 at stalled replication forks and protecting RAD51 nucleofilaments from the antirecombinogenic activities of FBH1 and BLM. Does not regulate spindle orientation. {ECO:0000250|UniProtKB:Q8NFC6}. SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:26166705}. Note=Localizes at replication forks: following DNA damage, localizes to damaged replication forks undergoing resection. {ECO:0000250|UniProtKB:Q8NFC6}. +A2AG58 BCLA3_MOUSE BCLAF1 and THRAP3 family member 3 752 90,111 Alternative sequence (1); Chain (1); Cross-link (1); Erroneous gene model prediction (1); Modified residue (6); Sequence conflict (4) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}. +P19536 COX5B_MOUSE Cytochrome c oxidase subunit 5B, mitochondrial (Cytochrome c oxidase polypeptide Vb) 128 13,813 Chain (1); Metal binding (4); Modified residue (3); Transit peptide (1) FUNCTION: This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. SUBCELLULAR LOCATION: Mitochondrion inner membrane. +P17665 COX7C_MOUSE Cytochrome c oxidase subunit 7C, mitochondrial (Cytochrome c oxidase polypeptide VIIc) 63 7,333 Chain (1); Modified residue (2); Topological domain (2); Transit peptide (1); Transmembrane (1) TRANSMEM 34 60 Helical. {ECO:0000250}. TOPO_DOM 17 33 Mitochondrial matrix. {ECO:0000250}.; TOPO_DOM 61 63 Mitochondrial intermembrane. {ECO:0000250}. FUNCTION: This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}. +P48772 COX8B_MOUSE Cytochrome c oxidase subunit 8B, mitochondrial (Cytochrome c oxidase polypeptide VIII-heart) (Cytochrome c oxidase subunit 8-1) (Cytochrome c oxidase subunit 8H) 70 7,332 Chain (1); Topological domain (2); Transit peptide (1); Transmembrane (1) TRANSMEM 36 59 Helical. {ECO:0000250}. TOPO_DOM 25 35 Mitochondrial matrix. {ECO:0000250}.; TOPO_DOM 60 70 Mitochondrial intermembrane. {ECO:0000250}. FUNCTION: This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. SUBCELLULAR LOCATION: Mitochondrion inner membrane. +Q6NVD9 BFSP2_MOUSE Phakinin (49 kDa cytoskeletal protein) (Beaded filament structural protein 2) (Lens fiber cell beaded filament protein CP 49) (CP49) 416 45,740 Alternative sequence (1); Chain (1); Coiled coil (3); Domain (1); Region (2); Sequence conflict (1) FUNCTION: Involved in stabilization of lens fiber cell cytoskeleton. {ECO:0000269|PubMed:12573667}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q28177}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q28177}; Cytoplasmic side {ECO:0000250|UniProtKB:Q28177}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q28177}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q28177}. Note=Detected adjacent to the cell membrane. {ECO:0000250|UniProtKB:Q28177}. SUBUNIT: Associates with BFSP1 (By similarity). Interacts with LGSN (PubMed:18178558). Identified in complexes that contain VIM, EZR, AHNAK, BFSP1, BFSP2, ANK2, PLEC, PRX and spectrin (PubMed:21745462). {ECO:0000250|UniProtKB:Q28177, ECO:0000269|PubMed:18178558, ECO:0000269|PubMed:21745462}. TISSUE SPECIFICITY: Detected in eye lens fiber cells (at protein level) (PubMed:21745462). Lens (PubMed:7679620). {ECO:0000269|PubMed:21745462, ECO:0000269|PubMed:7679620}. +P23780 BGAL_MOUSE Beta-galactosidase (EC 3.2.1.23) (Acid beta-galactosidase) (Lactase) 647 73,121 Active site (2); Binding site (4); Chain (1); Disulfide bond (2); Glycosylation (8); Propeptide (1); Sequence conflict (2); Signal peptide (1) FUNCTION: Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans. {ECO:0000250|UniProtKB:P16278}. SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:P16278}. SUBUNIT: Homodimer. May form higher multimers. {ECO:0000250|UniProtKB:P16278}. +Q8BGW3 BHE23_MOUSE Class E basic helix-loop-helix protein 23 (bHLHe23) (Class B basic helix-loop-helix protein 4) (bHLHb4) 223 23,701 Chain (1); Compositional bias (1); Domain (1); Sequence conflict (2) FUNCTION: May function as transcriptional repressor. May modulate the expression of genes required for the differentiation and/or maintenance of pancreatic and neuronal cell types. May be important for rod bipolar cell maturation. {ECO:0000269|PubMed:11863370, ECO:0000269|PubMed:15363390}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: Expressed in brain and retina. +D3Z6Q9 BIN2_MOUSE Bridging integrator 2 489 52,554 Chain (1); Compositional bias (1); Domain (1); Modified residue (11) FUNCTION: Promotes cell motility and migration, probably via its interaction with the cell membrane and with podosome proteins that mediate interaction with the cytoskeleton. Modulates membrane curvature and mediates membrane tubulation. Inhibits phagocytosis (By similarity). Plays a role in podosome formation. {ECO:0000250, ECO:0000269|PubMed:23285027}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UBW5}. Cell projection, podosome membrane {ECO:0000269|PubMed:23285027}; Peripheral membrane protein {ECO:0000269|PubMed:23285027}; Cytoplasmic side {ECO:0000269|PubMed:23285027}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q9UBW5}. Cell projection, phagocytic cup {ECO:0000250|UniProtKB:Q9UBW5}. Note=Associates with membranes enriched in phosphoinositides. Detected in the actin-rich cell cortex at the leading edge of migrating cells. Detected at podosomes, at an actin-rich ring-like structure. {ECO:0000250|UniProtKB:Q9UBW5}. SUBUNIT: Homodimer. Interacts with BIN1. Interacts with ARHGEF6 (via SH3 domain), ARHGEF7 (via SH3 domain), SH3GL1, SH3GL2 and SH3GL3. Identified in a complex with ARHGEF6 and GIT2 (By similarity). {ECO:0000250}. DOMAIN: The BAR domain mediates dimerization and interaction with membranes enriched in phosphatidylinositides. {ECO:0000250}. +Q811W2 CP26B_MOUSE Cytochrome P450 26B1 (EC 1.14.13.-) (Cytochrome P450 retinoic acid-inactivating 2) (Cytochrome P450RAI-2) 512 57,375 Chain (1); Metal binding (1); Sequence conflict (1) FUNCTION: Involved in the metabolism of retinoic acid (RA), rendering this classical morphogen inactive through oxidation. Involved in the specific inactivation of all-trans-retinoic acid (all-trans-RA), with a preference for the following substrates: all-trans-RA > 9-cis-RA > 13-cis-RA. Generates several hydroxylated forms of RA, including 4-OH-RA, 4-oxo-RA, and 18-OH-RA. Essential for postnatal survival. Plays a central role in germ cell development: acts by degrading RA in the developing testis, preventing STRA8 expression, thereby leading to delay of meiosis. Required for the maintenance of the undifferentiated state of male germ cells during embryonic development in Sertoli cells, inducing arrest in G0 phase of the cell cycle and preventing meiotic entry. Plays a role in skeletal development, both at the level of patterning and in the ossification of bone and the establishment of some synovial joints. {ECO:0000269|PubMed:16461896, ECO:0000269|PubMed:16574820, ECO:0000269|PubMed:19838304, ECO:0000269|PubMed:22019272}.; FUNCTION: Has also a significant activity in oxidation of tazarotenic acid and may therefore metabolize that xenobiotic in vivo. {ECO:0000250|UniProtKB:Q9NR63}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Microsome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. +P32299 BKRB2_MOUSE B2 bradykinin receptor (B2R) (BK-2 receptor) 392 44,389 Alternative sequence (1); Chain (1); Disulfide bond (1); Glycosylation (3); Lipidation (1); Modified residue (6); Sequence conflict (2); Topological domain (8); Transmembrane (7) TRANSMEM 62 85 Helical; Name=1. {ECO:0000255}.; TRANSMEM 95 119 Helical; Name=2. {ECO:0000255}.; TRANSMEM 133 154 Helical; Name=3. {ECO:0000255}.; TRANSMEM 177 199 Helical; Name=4. {ECO:0000255}.; TRANSMEM 223 249 Helical; Name=5. {ECO:0000255}.; TRANSMEM 269 293 Helical; Name=6. {ECO:0000255}.; TRANSMEM 313 336 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 61 Extracellular. {ECO:0000255}.; TOPO_DOM 86 94 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 120 132 Extracellular. {ECO:0000255}.; TOPO_DOM 155 176 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 200 222 Extracellular. {ECO:0000255}.; TOPO_DOM 250 268 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 294 312 Extracellular. {ECO:0000255}.; TOPO_DOM 337 392 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for bradykinin. It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBUNIT: Forms a complex with PECAM1 and GNAQ. Interacts with PECAM1 (By similarity). {ECO:0000250}. +Q923D2 BLVRB_MOUSE Flavin reductase (NADPH) (FR) (EC 1.5.1.30) (Biliverdin reductase B) (BVR-B) (EC 1.3.1.24) (Biliverdin-IX beta-reductase) (NADPH-dependent diaphorase) (NADPH-flavin reductase) (FLR) 206 22,197 Binding site (4); Chain (1); Modified residue (2); Nucleotide binding (3) FUNCTION: Broad specificity oxidoreductase that catalyzes the NADPH-dependent reduction of a variety of flavins, such as riboflavin, FAD or FMN, biliverdins, methemoglobin and PQQ (pyrroloquinoline quinone). Contributes to heme catabolism and metabolizes linear tetrapyrroles. Can also reduce the complexed Fe(3+) iron to Fe(2+) in the presence of FMN and NADPH. In the liver, converts biliverdin to bilirubin. {ECO:0000250|UniProtKB:P30043}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P30043}. SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P30043}. +P34821 BMP8A_MOUSE Bone morphogenetic protein 8A (BMP-8A) (Osteogenic protein 2) (OP-2) 399 44,764 Alternative sequence (1); Chain (1); Disulfide bond (4); Glycosylation (2); Propeptide (1); Signal peptide (1) FUNCTION: Induces cartilage and bone formation. May be the osteoinductive factor responsible for the phenomenon of epithelial osteogenesis. Plays a role in calcium regulation and bone homeostasis (By similarity). Has only marginal osteoinductive activity in mesenchymal progenitor and osteoprogenior cells but shows activity in committed osteoblastic cells. {ECO:0000250, ECO:0000269|PubMed:12925636}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in testis. expressed in trophoblast cells of the labyrinthine region of the placenta and in the inner root sheath of hair follicles of early postnatal skin. {ECO:0000269|PubMed:8843393}. +Q8BGS2 BOLA2_MOUSE BolA-like protein 2 86 10,215 Alternative sequence (1); Beta strand (5); Chain (1); Helix (5); Modified residue (1); Turn (1) FUNCTION: Acts as a cytosolic iron-sulfur (Fe-S) cluster assembly factor that facilitates [2Fe-2S] cluster insertion into a subset of cytosolic proteins. Acts together with the monothiol glutaredoxin GLRX3. {ECO:0000250|UniProtKB:Q9H3K6}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H3K6}. Nucleus {ECO:0000250|UniProtKB:Q9H3K6}. SUBUNIT: Interacts with GLRX3; forms a heterotrimeric complex composed by two BOLA2 molecules and one GLRX3 molecule; linked by [2Fe-2S] clusters. {ECO:0000250|UniProtKB:Q9H3K6}. +Q8K3X6 ANS4B_MOUSE Ankyrin repeat and SAM domain-containing protein 4B (Harmonin-interacting ankyrin repeat-containing protein) (Harp) 423 47,975 Beta strand (2); Chain (1); Coiled coil (2); Compositional bias (1); Domain (1); Helix (6); Motif (1); Region (2); Repeat (3); Sequence conflict (2); Turn (1) FUNCTION: As part of the intermicrovillar adhesion complex/IMAC plays a role in epithelial brush border differentiation, controlling microvilli organization and length. Plays a role in assembly of the complex (By similarity). May play a role in cellular response to endoplasmic reticulum stress (PubMed:22589549). {ECO:0000250|UniProtKB:Q8N8V4, ECO:0000269|PubMed:22589549}. SUBCELLULAR LOCATION: Cell projection, microvillus {ECO:0000269|PubMed:26812018}. Note=Localizes at the tip of microvilli (PubMed:26812018). May associate with endoplasmic reticulum membranes (PubMed:22589549). {ECO:0000269|PubMed:22589549, ECO:0000269|PubMed:26812018}. SUBUNIT: Part of the IMAC/intermicrovillar adhesion complex/intermicrovillar tip-link complex composed of ANKS4B, MYO7B, USH1C, CDHR2 and CDHR5 (By similarity). Interacts with USH1C; the interaction is direct and is required for ANKS4B localization to the tip of microvilli (PubMed:15461667, PubMed:26812017). Interacts with MYO7B; the interaction is direct (PubMed:26812017). May interact with HSPA5 (PubMed:22589549). {ECO:0000250|UniProtKB:Q8N8V4, ECO:0000269|PubMed:15461667, ECO:0000269|PubMed:22589549, ECO:0000269|PubMed:26812017}. TISSUE SPECIFICITY: Cochlea, kidney, lung, liver, pancreas, salivary gland and small intestine (at protein level). Expressed in kidney, small intestine, pancreas, liver and colon. Not detected in heart, spleen and brain. {ECO:0000269|PubMed:15461667, ECO:0000269|PubMed:26812018}. +O35639 ANXA3_MOUSE Annexin A3 (35-alpha calcimedin) (Annexin III) (Annexin-3) (Lipocortin III) (Placental anticoagulant protein III) (PAP-III) 323 36,384 Chain (1); Initiator methionine (1); Modified residue (3); Repeat (4); Sequence conflict (1) FUNCTION: Inhibitor of phospholipase A2, also possesses anti-coagulant properties. DOMAIN: A pair of annexin repeats may form one binding site for calcium and phospholipid. +Q01339 APOH_MOUSE Beta-2-glycoprotein 1 (APC inhibitor) (Activated protein C-binding protein) (Apolipoprotein H) (Apo-H) (Beta-2-glycoprotein I) (B2GPI) (Beta(2)GPI) 345 38,619 Chain (1); Disulfide bond (11); Domain (4); Glycosylation (6); Region (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Binds to various kinds of negatively charged substances such as heparin, phospholipids, and dextran sulfate. May prevent activation of the intrinsic blood coagulation cascade by binding to phospholipids on the surface of damaged cells. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma. +Q8C7G5 APOA5_MOUSE Apolipoprotein A-V (Apo-AV) (ApoA-V) (Apolipoprotein A5) (Regeneration-associated protein 3) 368 41,262 Chain (1); Coiled coil (1); Modified residue (1); Sequence conflict (3); Signal peptide (1) FUNCTION: Minor apolipoprotein mainly associated with HDL and to a lesser extent with VLDL. May also be associated with chylomicrons. Important determinant of plasma triglyceride (TG) levels by both being a potent stimulator of apo-CII lipoprotein lipase (LPL) TG hydrolysis and a inhibitor of the hepatic VLDL-TG production rate (without affecting the VLDL-apoB production rate). Activates poorly lecithin:cholesterol acyltransferase (LCAT) and does not enhance efflux of cholesterol from macrophages (By similarity). {ECO:0000250, ECO:0000269|PubMed:11588264, ECO:0000269|PubMed:15090553}. PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000250|UniProtKB:Q6Q788}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11577099}. SUBUNIT: Interacts with GPIHBP1. {ECO:0000250}. TISSUE SPECIFICITY: Liver. {ECO:0000269|PubMed:11577099, ECO:0000269|PubMed:11588264}. +Q99K28 ARFG2_MOUSE ADP-ribosylation factor GTPase-activating protein 2 (ARF GAP 2) (GTPase-activating protein ZNF289) (Zinc finger protein 289) 520 56,598 Alternative sequence (1); Chain (1); Coiled coil (1); Domain (1); Initiator methionine (1); Modified residue (13); Region (1); Sequence conflict (1); Zinc finger (1) FUNCTION: GTPase-activating protein (GAP) for ADP ribosylation factor 1 (ARF1). May regulate coatomer-mediated protein transport from the Golgi complex to the endoplasmic reticulum. Hydrolysis of ARF1-bound GTP may lead to dissociation of coatomer from Golgi-derived membranes to allow fusion with target membranes (By similarity). {ECO:0000250, ECO:0000269|PubMed:11278321}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Also found on peripheral punctate structures likely to be endoplasmic reticulum-Golgi intermediate compartment. {ECO:0000250}. SUBUNIT: Interacts with the coatomer complex. Interacts with the C-terminal appendage domain of COPG1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in liver, heart and kidney. Low expression in skeletal muscle and spleen. {ECO:0000269|PubMed:11278321}. +A2AWP8 ARGAL_MOUSE Rho guanine nucleotide exchange factor 10-like protein (GrinchGEF) 1280 139,987 Alternative sequence (5); Chain (1); Domain (1); Erroneous initiation (1); Modified residue (4); Sequence conflict (3) FUNCTION: Acts as guanine nucleotide exchange factor (GEF) for RHOA, RHOB and RHOC. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with RHOA, RHOB and RHOC. {ECO:0000250}. +O55229 CHKB_MOUSE Choline/ethanolamine kinase (Choline kinase beta) (CK) (CKB) (EC 2.7.1.32) (Ethanolamine kinase) (EK) (EC 2.7.1.82) (choline/ethanolamine kinase beta) (CKEKB) 394 45,126 Binding site (3); Chain (1); Initiator methionine (1); Modified residue (1); Nucleotide binding (2); Region (1) Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from ethanolamine: step 1/3. FUNCTION: Has a key role in phospholipid biosynthesis. Catalyzes the first step in phosphatidylethanolamine biosynthesis. Phosphorylates ethanolamine, and can also act on choline (in vitro). Has higher activity with ethanolamine. May not significantly contribute to in vivo phosphatidylcholine biosynthesis (By similarity). {ECO:0000250}. SUBUNIT: Homodimer, and heterodimer with CHKA. {ECO:0000269|PubMed:16490392}. TISSUE SPECIFICITY: Expressed ubiquitously with the highest level in testis. DISEASE: Note=Defects in Chkb are a cause of rostrocaudal muscular dystrophy (rmd). The disease is characterized by rapidly progressive muscular dystrophy and neonatal forelimb bone deformity. The dystrophy is only evident in skeletal muscle tissues in an unusual rostral-to-caudal gradient. {ECO:0000269|PubMed:16371353}. +Q03311 CHLE_MOUSE Cholinesterase (EC 3.1.1.8) (Acylcholine acylhydrolase) (Butyrylcholine esterase) (Choline esterase II) (Pseudocholinesterase) 603 68,462 Active site (3); Chain (1); Disulfide bond (4); Glycosylation (7); Modified residue (1); Region (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Esterase with broad substrate specificity. Contributes to the inactivation of the neurotransmitter acetylcholine. Can degrade neurotoxic organophosphate esters. {ECO:0000269|PubMed:17212694, ECO:0000269|PubMed:17467011}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Homotetramer; disulfide-linked. Dimer of dimers (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Present in most cells except erythrocytes. +Q9DB34 CHM2A_MOUSE Charged multivesicular body protein 2a (Chromatin-modifying protein 2a) (CHMP2a) (Vacuolar protein sorting-associated protein 2) (mVps2) 222 25,134 Chain (1); Coiled coil (2); Modified residue (6); Motif (1); Region (2) FUNCTION: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis. Together with SPAST, the ESCRT-III complex promotes nuclear envelope sealing and mitotic spindle disassembly during late anaphase. ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. {ECO:0000250|UniProtKB:O43633}. PTM: ISGylated in a CHMP5-dependent manner. Isgylation weakens and inhibits its interactions with VPS4A and VTA1 respectively (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:15173323}. Note=Localizes to the midbody of dividing cells. Localized in two distinct rings on either side of the Fleming body. SUBUNIT: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III). ESCRT-III components are thought to multimerize to form a flat lattice on the perimeter membrane of the endosome. Several assembly forms of ESCRT-III may exist that interact and act sequentially. In vitro, heteromerizes with CHMP3 (but not CHMP4) to form helical tubular structures that expose membrane-interacting sites on the outside whereas VPS4B can associate on the inside of the tubule. Interacts with CHMP1B, CHMP2B, CHMP3, CHMP4A, CHMP4B, CHMP4C and CHMP5. Interacts with VPS4A; the interaction is direct. Interacts with VPS4B; the interaction is direct. Interacts with MITD1. Interacts with VTA1; the interaction probably involves the open conformation of CHMP2A (By similarity). {ECO:0000250}. DOMAIN: The acidic C-terminus and the basic N-termminus are thought to render the protein in a closed, soluble and inactive conformation through an autoinhibitory intramolecular interaction. The open and active conformation, which enables membrane binding and oligomerization, is achieved by interaction with other cellular binding partners, probably including other ESCRT components. TISSUE SPECIFICITY: Widely expressed. Highly expressed in brain, heart, liver and kidney. {ECO:0000269|PubMed:15173323}. +Q9D898 ARP5L_MOUSE Actin-related protein 2/3 complex subunit 5-like protein (Arp2/3 complex 16 kDa subunit 2) (ARC16-2) 153 16,980 Chain (1); Modified residue (1) FUNCTION: May function as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. SUBUNIT: May be a component of the Arp2/3 complex in which it may replace ARPC5. +Q8C6A8 BHE22_MOUSE Class E basic helix-loop-helix protein 22 (bHLHe22) (Class B basic helix-loop-helix protein 5) (bHLHb5) (Protein BETA3) 355 35,217 Chain (1); Compositional bias (3); Domain (1); Sequence conflict (3) FUNCTION: Inhibits DNA binding of TCF3/E47 homodimers and TCF3 (E47)/NEUROD1 heterodimers and acts as a strong repressor of Neurod1 and Myod-responsive genes, probably by heterodimerization with class a basic helix-loop-helix factors. Despite the presence of an intact basic domain, does not bind to DNA (By similarity). In the brain, may function as an area-specific transcription factor that regulates the postmitotic acquisition of area identities and elucidate the genetic hierarchy between progenitors and postmitotic neurons driving neocortical arealization. May be required for the survival of a specific population of inhibitory neurons in the superficial laminae of the spinal chord dorsal horn that may regulate pruritis. Seems to play a crucial role in the retinogenesis, in the specification of amacrine and bipolar subtypes. Forms with PRDM8 a transcriptional repressor complex controlling genes involved in neural development and neuronal differentiation (PubMed:22284184). {ECO:0000250, ECO:0000269|PubMed:17092954, ECO:0000269|PubMed:18957218, ECO:0000269|PubMed:20346763, ECO:0000269|PubMed:22284184}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Interacts with PRDM8. {ECO:0000269|PubMed:22284184}. TISSUE SPECIFICITY: Brain-specific, with the highest expression in the cerebellum. {ECO:0000269|PubMed:12213201}. +O35185 BHE40_MOUSE Class E basic helix-loop-helix protein 40 (bHLHe40) (Class B basic helix-loop-helix protein 2) (bHLHb2) (E47 interaction protein 1) (EIP1) (Stimulated by retinoic acid gene 13 protein) 411 45,361 Chain (1); Cross-link (6); Domain (2); Modified residue (2); Region (2); Sequence conflict (1) FUNCTION: Transcriptional repressor involved in the regulation of the circadian rhythm by negatively regulating the activity of the clock genes and clock-controlled genes. Acts as the negative limb of a novel autoregulatory feedback loop (DEC loop) which differs from the one formed by the PER and CRY transcriptional repressors (PER/CRY loop). Both these loops are interlocked as it represses the expression of PER1/2 and in turn is repressed by PER1/2 and CRY1/2. Represses the activity of the circadian transcriptional activator: CLOCK-ARNTL/BMAL1|ARNTL2/BMAL2 heterodimer by competing for the binding to E-box elements (5'-CACGTG-3') found within the promoters of its target genes. Negatively regulates its own expression and the expression of DBP and BHLHE41/DEC2. Acts as a corepressor of RXR and the RXR-LXR heterodimers and represses the ligand-induced RXRA and NR1H3/LXRA transactivation activity. May function as a transcriptional factor for neuronal differentiation. {ECO:0000269|PubMed:14672706, ECO:0000269|PubMed:18411297, ECO:0000269|PubMed:19786558}. PTM: Ubiquitinated; which may lead to proteasomal degradation. {ECO:0000250}.; PTM: Sumoylation inhibits its ubiquitination and promotes its negative regulation of the CLOCK-ARNTL/BMAL1 heterodimer transcriptional activator activity. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O14503}. Nucleus {ECO:0000250|UniProtKB:O14503}. Note=Predominantly localized in the nucleus (By similarity). {ECO:0000250|UniProtKB:O14503}. SUBUNIT: Homodimer. Heterodimer with BHLHE41/DEC2. Interacts with ubiquitin-conjugating enzyme UBE2I/UBC9. Interacts with HDAC1, SUMO1, RXRA and ARNTL/BMAL1 (By similarity). Interacts with TCF3/E47. {ECO:0000250, ECO:0000269|PubMed:9050988}. +P82198 BGH3_MOUSE Transforming growth factor-beta-induced protein ig-h3 (Beta ig-h3) 683 74,597 Chain (1); Disulfide bond (5); Domain (5); Modified residue (2); Motif (1); Signal peptide (1) FUNCTION: Plays a role in cell adhesion (PubMed:8024701). May play a role in cell-collagen interactions (By similarity). {ECO:0000250|UniProtKB:O11780, ECO:0000269|PubMed:8024701}. PTM: Gamma-carboxylation is controversial. Gamma-carboxyglutamated; gamma-carboxyglutamate residues are formed by vitamin K dependent carboxylation; this may be required for calcium binding. According to a more recent report, does not contain vitamin K-dependent gamma-carboxyglutamate residues. {ECO:0000250|UniProtKB:Q15582}.; PTM: The EMI domain contains 2 expected intradomain disulfide bridges (Cys-49-Cys85 and Cys-84-Cys-97) and one unusual interdomain disulfide bridge to the second FAS1 domain (Cys-74-Cys-339). This arrangement violates the predicted disulfide bridge pattern of an EMI domain. {ECO:0000250|UniProtKB:Q15582}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q15582}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q15582}. Note=May be associated both with microfibrils and with the cell surface. {ECO:0000250|UniProtKB:Q15582}. SUBUNIT: Binds to type I, II, and IV collagens. {ECO:0000250|UniProtKB:O11780}. TISSUE SPECIFICITY: Expressed in heart, kidney, liver, skeletal muscle, testis, thyroid and uterus (PubMed:8024701). {ECO:0000269|PubMed:8024701}. +P56593 CP2AC_MOUSE Cytochrome P450 2A12 (EC 1.14.14.1) (CYPIIA12) (Steroid hormones 7-alpha-hydroxylase) (Testosterone 7-alpha-hydroxylase) 492 56,179 Chain (1); Metal binding (1); Mutagenesis (3); Sequence conflict (4) FUNCTION: Highly active in the 7-alpha-hydroxylation of testosterone. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. TISSUE SPECIFICITY: Liver. +P12790 CP2B9_MOUSE Cytochrome P450 2B9 (EC 1.14.14.1) (CYPIIB9) (Cytochrome P450 clone PF26) (Cytochrome P450-16-alpha) (Testosterone 16-alpha hydroxylase) 491 55,741 Chain (1); Metal binding (1); Modified residue (1); Sequence conflict (2) FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. +P98063 BMP1_MOUSE Bone morphogenetic protein 1 (BMP-1) (EC 3.4.24.19) (Mammalian tolloid protein) (mTld) (Procollagen C-proteinase) (PCP) 991 111,666 Active site (1); Chain (1); Disulfide bond (19); Domain (8); Frameshift (1); Glycosylation (5); Metal binding (3); Modified residue (2); Propeptide (1); Sequence conflict (2); Signal peptide (1) FUNCTION: Cleaves the C-terminal propeptides of procollagen I, II and III. Induces cartilage and bone formation. May participate in dorsoventral patterning during early development by cleaving chordin (CHRD) (By similarity). Responsible for the proteolytic activation of lysyl oxidase LOX. {ECO:0000250, ECO:0000269|PubMed:20181949}. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:20181949}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:20181949}. Note=Co-localizes with POSTN in the Golgi. SUBUNIT: Interacts with POSTN, the interaction promotes deposition on the extracellular matrix. {ECO:0000269|PubMed:20181949}. TISSUE SPECIFICITY: At high levels in embryonic maternal deciduum and floor plate region of the neural tube. Less in developing membranous and endochondral bone, submucosa of intestine, dermis of skin and the mesenchyme of spleen and lung. +Q924M5 BOLL_MOUSE Protein boule-like 281 30,856 Alternative sequence (3); Chain (1); Domain (2); Modified residue (3); Sequence conflict (1) FUNCTION: Probable RNA-binding protein, which may be required during spermatogenesis. May act by binding to the 3'-UTR of mRNAs and regulating their translation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11390979}. SUBUNIT: Interacts with DAZ1 and DAZL. {ECO:0000250}. TISSUE SPECIFICITY: Testis specific. Not expressed in early embryos, primoridal germ cells and spermatogonial cells. First expressed in the cytoplasm of spermatocytes and then persists through meiosis. {ECO:0000269|PubMed:11390979}. +Q8BS90 BORA_MOUSE Protein aurora borealis 525 57,038 Alternative sequence (2); Chain (1); Compositional bias (1); Frameshift (1); Modified residue (6); Sequence conflict (1) FUNCTION: Required for the activation of AURKA at the onset of mitosis. {ECO:0000250}. PTM: Phosphorylated by AURKA. {ECO:0000250}. SUBUNIT: Interacts with AURKA. {ECO:0000250}. +Q9Z0X0 BORG3_MOUSE Cdc42 effector protein 5 (Binder of Rho GTPases 3) 150 15,545 Chain (1); Compositional bias (1); Domain (1); Modified residue (1); Mutagenesis (1); Sequence conflict (1) FUNCTION: Probably involved in the organization of the actin cytoskeleton. May act downstream of CDC42 to induce actin filament assembly leading to cell shape changes. Induces pseudopodia formation in fibroblasts. Inhibits MAPK8 independently of CDC42 binding. Controls septin organization and this effect is negatively regulated by CDC42. {ECO:0000269|PubMed:10490598, ECO:0000269|PubMed:11035016, ECO:0000269|PubMed:11584266}. SUBCELLULAR LOCATION: Endomembrane system {ECO:0000269|PubMed:11035016}; Peripheral membrane protein {ECO:0000269|PubMed:11035016}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11035016}. SUBUNIT: Interacts with CDC42 in a GTP-dependent manner, and with SEPT7. {ECO:0000269|PubMed:10490598, ECO:0000269|PubMed:11035016, ECO:0000269|PubMed:11584266}. DOMAIN: The CRIB domain mediates interaction with CDC42. TISSUE SPECIFICITY: Highly expressed in the skeletal muscle. {ECO:0000269|PubMed:10490598}. +Q9CRC6 BORC7_MOUSE BLOC-1-related complex subunit 7 105 11,546 Chain (1) FUNCTION: As part of the BORC complex may play a role in lysosomes movement and localization at the cell periphery. Associated with the cytosolic face of lysosomes, the BORC complex may recruit ARL8B and couple lysosomes to microtubule plus-end-directed kinesin motor. {ECO:0000250|UniProtKB:Q96B45}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q96B45}. SUBUNIT: Component of the BLOC-one-related complex (BORC) which is composed of BLOC1S1, BLOC1S2, BORCS5, BORCS6, BORCS7, BORCS8, KXD1 and SNAPIN. {ECO:0000250|UniProtKB:Q96B45}. +Q9D6Y4 BORC8_MOUSE BLOC-1-related complex subunit 8 120 13,565 Chain (1); Modified residue (1) FUNCTION: As part of the BORC complex may play a role in lysosomes movement and localization at the cell periphery. Associated with the cytosolic face of lysosomes, the BORC complex may recruit ARL8B and couple lysosomes to microtubule plus-end-directed kinesin motor. {ECO:0000250|UniProtKB:Q96FH0}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q96FH0}. SUBUNIT: Component of the BLOC-one-related complex (BORC) which is composed of BLOC1S1, BLOC1S2, BORCS5, BORCS6, BORCS7, BORCS8, KXD1 and SNAPIN. {ECO:0000250|UniProtKB:Q96FH0}. +Q8BU51 BPIB6_MOUSE BPI fold-containing family B member 6 (Bactericidal/permeability-increasing protein-like 3) 449 48,781 Chain (1); Disulfide bond (1); Erroneous initiation (1); Glycosylation (1); Sequence conflict (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +Q91W92 BORG5_MOUSE Cdc42 effector protein 1 (Binder of Rho GTPases 5) 409 43,096 Chain (1); Domain (1); Modified residue (19); Region (1); Repeat (3); Sequence conflict (3) FUNCTION: Probably involved in the organization of the actin cytoskeleton. Induced membrane extensions in fibroblasts (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. SUBUNIT: Interacts with RHOQ and CDC42, in a GTP-dependent manner. {ECO:0000250}. DOMAIN: The CRIB domain mediates interaction with CDC42. {ECO:0000250}. +P97361 BPIA1_MOUSE BPI fold-containing family A member 1 (Palate lung and nasal epithelium clone protein) 278 28,625 Beta strand (7); Chain (1); Disulfide bond (1); Glycosylation (2); Helix (9); Region (1); Repeat (4); Sequence conflict (2); Signal peptide (1) FUNCTION: Plays a role in the innate immune responses of the upper airways. Reduces the surface tension in secretions from airway epithelia and inhibits the formation of biofilm by pathogenic Gram-negative bacteria, such as P.aeruginosa and K.pneumoniae. Binds bacterial lipopolysaccharide (LPS). Negatively regulates proteolytic cleavage of SCNN1G, an event that is required for activation of the epithelial sodium channel (ENaC), and thereby contributes to airway surface liquid homeostasis and proper clearance of mucus (By similarity). Plays a role in the airway inflammatory response after exposure to irritants. May attract macrophages and neutrophils. May be associated with tumor progression. {ECO:0000250, ECO:0000269|PubMed:23499554}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23499554}. Note=Apical side of airway epithelial cells. Detected in airway surface liquid, nasal mucus and sputum. SUBUNIT: Monomer. Interacts (via N-terminus) with SCNN1B, a subunit of the heterotrimeric epithelial sodium channel (ENaC); this inhibits proteolytic activation of ENaC (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Detected in airway epithelia (trachea and lung) and in bronchoalveolar fluid (at protein level). Upper airways, nasopharyngeal epithelium and thymus. Highest expression in the trachea and progressive decrease from proximal (bronchial) to distal (bronchiolar) airways. No expression is detected in the terminal bronchioles, respiratory bronchioles or lung alveoli. {ECO:0000269|PubMed:10224143, ECO:0000269|PubMed:11396972, ECO:0000269|PubMed:23499554}. +Q9Z0S1 BPNT1_MOUSE 3'(2'),5'-bisphosphate nucleotidase 1 (EC 3.1.3.7) (Bisphosphate 3'-nucleotidase 1) (PAP-inositol 1,4-phosphatase) (PIP) 308 33,196 Binding site (2); Chain (1); Initiator methionine (1); Metal binding (6); Modified residue (4); Region (2); Sequence conflict (3) FUNCTION: Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine 5'- phosphate (PAP) to AMP. Has 1000-fold lower activity towards inositol 1,4-bisphosphate (Ins(1,4)P2) and inositol 1,3,4-trisphosphate (Ins(1,3,4)P3), but does not hydrolyze Ins(1)P, Ins(3,4)P2, Ins(1,3,4,5)P4 or InsP6. +P28028 BRAF_MOUSE Serine/threonine-protein kinase B-raf (EC 2.7.11.1) (Proto-oncogene B-Raf) 804 88,780 Active site (1); Alternative sequence (2); Binding site (1); Chain (1); Compositional bias (2); Cross-link (1); Domain (2); Erroneous initiation (1); Initiator methionine (1); Metal binding (8); Modified residue (14); Nucleotide binding (1); Sequence caution (1); Sequence conflict (1) FUNCTION: Involved in the transduction of mitogenic signals from the cell membrane to the nucleus. May play a role in the postsynaptic responses of hippocampal neuron (By similarity). {ECO:0000250}. PTM: Phosphorylation at Ser-348 by SGK1 inhibits its activity. {ECO:0000250}.; PTM: Methylation by PRMT5 decreases stability and kinase activity. {ECO:0000269|PubMed:21917714}.; PTM: Ubiquitinated by RNF149; which leads to proteasomal degradation. Polyubiquitinated at Lys-615 in response to EGF (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Colocalizes with RGS14 and RAF1 in both the cytoplasm and membranes. {ECO:0000250}. SUBUNIT: Monomer. Homodimer. Heterodimerizes with RAF1, and the heterodimer possesses a highly increased kinase activity compared to the respective homodimers or monomers. Heterodimerization is mitogen-regulated and enhanced by 14-3-3 proteins. MAPK1/ERK2 activation can induce a negative feedback that promotes the dissociation of the heterodimer by phosphorylating BRAF at Thr-790. Found in a complex with at least BRAF, HRAS, MAP2K1, MAPK3 and RGS14. Interacts with RIT1. Interacts (via N-terminus) with RGS14 (via RBD domains); the interaction mediates the formation of a ternary complex with RAF1, a ternary complex inhibited by GNAI1 (By similarity). Interacts with DGKH (By similarity). Interacts with PRMT5 (By similarity). Interacts with AKAP13, MAP2K1 and KSR1. Identified in a complex with AKAP13, KSR1 and MAP2K1 (PubMed:21102438). Interacts with FNIP1 and FNIP2 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P15056, ECO:0000269|PubMed:21102438}. DISEASE: Note=Participates in a chromosomal translocation that produces a Tif1a-BRAF (T18) oncogene originally isolated from a furfural-induced hepatoma. +Q99MP8 BRAP_MOUSE BRCA1-associated protein (EC 2.3.2.27) (BRAP2) (Impedes mitogenic signal propagation) (IMP) (RING-type E3 ubiquitin transferase BRAP2) 591 66,991 Alternative sequence (2); Chain (1); Coiled coil (1); Erroneous initiation (1); Modified residue (3); Sequence conflict (1); Zinc finger (2) Protein modification; protein ubiquitination. FUNCTION: Negatively regulates MAP kinase activation by limiting the formation of Raf/MEK complexes probably by inactivation of the KSR1 scaffold protein. Also acts as a Ras responsive E3 ubiquitin ligase that, on activation of Ras, is modified by auto-polyubiquitination resulting in the release of inhibition of Raf/MEK complex formation. May also act as a cytoplasmic retention protein with a role in regulating nuclear transport (By similarity). {ECO:0000250|UniProtKB:Q7Z569}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q7Z569}. SUBUNIT: Interacts with the nuclear localization signal of BRCA1 and with the N-terminal of KSR1. The C-terminal portion of BRCA1 interacts with DDB1. {ECO:0000250|UniProtKB:Q7Z569}. TISSUE SPECIFICITY: Isoform 2 is highly expressed in testis, lower levels in brain, heart, lung, stomach, colon, uterus, liver and kidney. Isoform 1 is only expressed in the testis. Isoform 2 is predominant over isoform 1 in both fetal and adult testis. {ECO:0000269|PubMed:14607334}. +Q8K2F0 BRD3_MOUSE Bromodomain-containing protein 3 (Bromodomain-containing FSH-like protein FSRG2) 726 79,762 Alternative sequence (1); Beta strand (3); Chain (1); Coiled coil (2); Compositional bias (4); Cross-link (1); Domain (3); Helix (8); Modified residue (3); Region (1); Sequence conflict (4); Turn (1) FUNCTION: Chromatin reader that recognizes and binds hyperacetylated chromatin and plays a role in the regulation of transcription, probably by chromatin remodeling and interaction with transcription factors (PubMed:21536911). Regulates transcription by promoting the binding of the transcription factor GATA1 to its targets (PubMed:21536911). {ECO:0000269|PubMed:21536911}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21536911}. Note=Detected on chromatin. {ECO:0000269|PubMed:21536911}. SUBUNIT: Interacts (via bromo domains) with acetylated lysine residues on the N-terminus of histone H2A, H2B, H3 and H4 (in vitro) (PubMed:21536911). Interacts (via bromo domain 1) with GATA1 acetylated at 'Lys-312' and 'Lys-315' (PubMed:21555453). Interacts (via bromo domain 1) with GATA2 acetylated on lysine residues (PubMed:21555453). {ECO:0000269|PubMed:21536911, ECO:0000269|PubMed:21555453}. DOMAIN: The Bromo domains specifically recognize and bind acetylated histones. {ECO:0000250|UniProtKB:Q15059}. +Q5RJI5 BRSK1_MOUSE Serine/threonine-protein kinase BRSK1 (EC 2.7.11.1) (EC 2.7.11.26) (Brain-specific serine/threonine-protein kinase 1) (BR serine/threonine-protein kinase 1) (Serine/threonine-protein kinase SAD-B) 778 85,155 Active site (1); Alternative sequence (2); Beta strand (7); Binding site (1); Chain (1); Compositional bias (1); Domain (2); Helix (3); Modified residue (18); Mutagenesis (2); Nucleotide binding (1); Sequence conflict (3) FUNCTION: Serine/threonine-protein kinase that plays a key role in polarization of neurons and centrosome duplication. Phosphorylates CDC25B, CDC25C, MAPT/TAU, RIMS1, TUBG1, TUBG2 and WEE1. Following phosphorylation and activation by STK11/LKB1, acts as a key regulator of polarization of cortical neurons, probably by mediating phosphorylation of microtubule-associated proteins such as MAPT/TAU at 'Thr-504' and 'Ser-554'. Also regulates neuron polarization by mediating phosphorylation of WEE1 at 'Ser-642' in post-mitotic neurons, leading to down-regulate WEE1 activity in polarized neurons. In neurons, localizes to synaptic vesicles and plays a role in neurotransmitter release, possibly by phosphorylating RIMS1. Also acts as a positive regulator of centrosome duplication by mediating phosphorylation of gamma-tubulin (TUBG1 and TUBG2) at 'Ser-131', leading to translocation of gamma-tubulin and its associated proteins to the centrosome. Involved in the UV-induced DNA damage checkpoint response, probably by inhibiting CDK1 activity through phosphorylation and activation of WEE1, and inhibition of CDC25B and CDC25C. {ECO:0000269|PubMed:15705853, ECO:0000269|PubMed:17482548, ECO:0000269|PubMed:19648910, ECO:0000269|PubMed:20026642}. PTM: Phosphorylated at Thr-189 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. Not phosphorylated at Thr-189 by CaMKK2. In contrast, it is phosphorylated and activated by CaMKK1. May be inactivated via dephosphorylation of Thr-189 by PP2C. {ECO:0000269|PubMed:17482548}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cell junction, synapse {ECO:0000250}. Note=Nuclear in the absence of DNA damage. Translocated to the nucleus in response to UV- or MMS-induced DNA damage. Localizes to synaptic vesicles in neurons (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Present in the gray matter of the brain and spinal cord (at protein level). Expressed in the nervous system, distributed within the brain and spinal cord of embryonic and postnatal animals. {ECO:0000269|PubMed:15705853}. +Q9Z2E9 BSCL2_MOUSE Seipin (Bernardinelli-Seip congenital lipodystrophy type 2 protein homolog) 383 43,105 Chain (1); Erroneous initiation (3); Glycosylation (2); Modified residue (3); Sequence conflict (1); Topological domain (3); Transmembrane (2) TRANSMEM 28 48 Helical. {ECO:0000255}.; TRANSMEM 243 263 Helical. {ECO:0000255}. TOPO_DOM 1 27 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 49 242 Lumenal. {ECO:0000255}.; TOPO_DOM 264 383 Cytoplasmic. {ECO:0000255}. FUNCTION: Is a regulator of lipid catabolism essential for adipocyte differentiation. Necessary for correct lipid storage and lipid droplets maintenance; may play a tissue-autonomous role in controlling lipid storage in adipocytes and in preventing ectopic lipid droplet formation in non-adipose tissues. May also be involved in the central regulation of energy homeostasis. {ECO:0000269|PubMed:18458148, ECO:0000269|PubMed:19574402, ECO:0000269|PubMed:21551454, ECO:0000269|PubMed:22269949}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19574402}; Multi-pass membrane protein {ECO:0000269|PubMed:19574402}. TISSUE SPECIFICITY: Expressed in the paraventricular nucleus of the hypothalamus (PVN) and brainstem dorsal vagal complex (DVC) in oxytocin and catecholaminergic neurons (at protein level). Highest expression detected in subcutaneous and epididymal white adipose tissue, brown adipose tissue and testis. Also expressed in brain, skeletal muscle and adrenal gland, with lower levels detected in liver, heart, kidney, spleen, lung and small intestine. In brain, detected in piriform cortex, olfactory tubercle, islands of Calleja, lateral septal nucleus, medial septal nucleus, nucleus of the vertical limb of the diagonal band, nucleus of the horizontal limb of the diagonal band, preoptic area, paraventricular thalamic nucleus, lateral globus pallidus, supraoptic nucleus, suprachiasmatic nucleus, subfornical organ, paraventricular nucleus of the hypothalamus, zona incerta, dorsomedial nucleus of the hypothalamus, ventromedial nucleus of the hypothalamus, arcuate nucleus of the hypothalamus, basomedial amygdaloid nucleus, medial amygdaloid nucleus, medial habenular, pyramidal cell layer of the hippocampus, granular layer of the dentate gyrus, posterior hypothalamus, supramammilliary nucleus, premammillary nucleus, nucleus of Darkschewitsch, Edinger-Westphal nucleus, ventral tegmental area, dorsal raphe nucleus, periaqueductal gray, median raphe nucleus, lateral parabrachial nucleus, dorsal tegmental nucleus, laterodorsal tegmental nucleus, locus coeruleus, Barrington's nucleus, medial vestibular nucleus, ambiguous nucleus, dorsal vagal complex and hypoglossal nucleus. {ECO:0000269|PubMed:18458148, ECO:0000269|PubMed:19574402, ECO:0000269|PubMed:23049863, ECO:0000269|PubMed:9790771}. +Q80U49 C170B_MOUSE Centrosomal protein of 170 kDa protein B (Centrosomal protein 170B) (Cep170B) 1574 170,821 Alternative sequence (1); Chain (1); Domain (1); Erroneous initiation (1); Modified residue (29); Sequence conflict (4) FUNCTION: Plays a role in microtubule organization. {ECO:0000250|UniProtKB:Q5SW79}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q498L0}. +O88992 C1QRF_MOUSE C1q-related factor (C1q and tumor necrosis factor-related protein 14) (C1q/TNF-related protein 14) (CTRP14) (Complement component 1 Q subcomponent-like 1) 258 26,500 Beta strand (11); Chain (1); Domain (2); Mutagenesis (2); Sequence conflict (1); Signal peptide (1); Turn (1) FUNCTION: May regulate the number of excitatory synapses that are formed on hippocampus neurons. Has no effect on inhibitory synapses. {ECO:0000269|PubMed:21262840}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Interacts with ADGRB3 (PubMed:21262840). Forms heterooligomers with C1QL4, when proteins are coexpressed; this interaction does not occur after secretion (PubMed:23449976). {ECO:0000269|PubMed:21262840, ECO:0000269|PubMed:23449976}. TISSUE SPECIFICITY: Expressed in brainstem. More abundant in areas of the nervous system involved in motor function, such as the Purkinje cells of the cerebellum, the accessory olivary nucleus, the pons and the red nucleus. +P08607 C4BPA_MOUSE C4b-binding protein (C4bp) 469 51,524 Chain (1); Disulfide bond (12); Domain (6); Erroneous initiation (1); Glycosylation (7); Signal peptide (1) FUNCTION: Controls the classical pathway of complement activation. It binds as a cofactor to C3b/C4b inactivator (C3bINA), which then hydrolyzes the complement fragment C4b. It also accelerates the degradation of the C4bC2a complex (C3 convertase) by dissociating the complement fragment C2a. Alpha chain binds C4b. It interacts also with serum amyloid P component. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Homoheptamer; not covalently linked. Mouse lacks the beta chain of C4BP. +Q8BVD7 C1QT7_MOUSE Complement C1q tumor necrosis factor-related protein 7 289 30,517 Chain (1); Domain (2); Sequence conflict (2); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q9EQG9 C43BP_MOUSE Collagen type IV alpha-3-binding protein (Ceramide transfer protein) (Goodpasture antigen-binding protein) (GPBP) (START domain-containing protein 11) (StARD11) (StAR-related lipid transfer protein 11) 624 71,111 Alternative sequence (3); Binding site (4); Chain (1); Coiled coil (1); Domain (2); Modified residue (8); Motif (1); Sequence caution (1); Sequence conflict (2) FUNCTION: Shelters ceramides and diacylglycerol lipids inside its START domain and mediates the intracellular trafficking of ceramides and diacylglycerol lipids in a non-vesicular manner. {ECO:0000250|UniProtKB:Q9Y5P4}. PTM: Phosphorylation on Ser-132 decreases the affinity toward phosphatidylinositol 4-phosphate at Golgi membranes and reduces ceramide transfer activity. Inactivated by hyperphosphorylation of serine residues by CSNK1G2/CK1 that triggers dissociation from the Golgi complex, thus down-regulating ER-to-Golgi transport of ceramide and sphingomyelin synthesis. {ECO:0000250|UniProtKB:Q9Y5P4}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y5P4}. Golgi apparatus {ECO:0000250|UniProtKB:Q9Y5P4}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9Y5P4}. Note=Preferentially localized to the Golgi apparatus. {ECO:0000250|UniProtKB:Q9Y5P4}. SUBUNIT: Interacts with COL4A3. Interacts with VAPA and VAPB. Interaction with VAPB is less efficient than with VAPA. {ECO:0000250|UniProtKB:Q9Y5P4}. DOMAIN: The START domain recognizes ceramides and diacylglycerol lipids, interacts with membranes, and mediates the intermembrane transfer of ceramides and diacylglycerol lipids. {ECO:0000250|UniProtKB:Q9Y5P4}.; DOMAIN: The PH domain targets the Golgi apparatus. {ECO:0000250|UniProtKB:Q9Y5P4}.; DOMAIN: The FFAT motif is required for interaction with VAPA and VAPB. {ECO:0000250|UniProtKB:Q9Y5P4}. +Q3UZ09 C1RL_MOUSE Complement C1r subcomponent-like protein (C1r-LP) (C1r-like protein) (EC 3.4.21.-) 482 53,435 Active site (3); Chain (1); Disulfide bond (3); Domain (2); Glycosylation (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Mediates the proteolytic cleavage of HP/haptoglobin in the endoplasmic reticulum. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Expressed in liver (at protein level). +Q8BW93 C5AR2_MOUSE C5a anaphylatoxin chemotactic receptor 2 (Complement component 5a receptor 2) (G-protein coupled receptor 77) 344 38,199 Chain (1); Disulfide bond (1); Erroneous initiation (1); Glycosylation (1); Modified residue (1); Sequence conflict (1); Topological domain (8); Transmembrane (7) TRANSMEM 45 67 Helical; Name=1. {ECO:0000255}.; TRANSMEM 79 101 Helical; Name=2. {ECO:0000255}.; TRANSMEM 121 143 Helical; Name=3. {ECO:0000255}.; TRANSMEM 156 178 Helical; Name=4. {ECO:0000255}.; TRANSMEM 209 231 Helical; Name=5. {ECO:0000255}.; TRANSMEM 244 266 Helical; Name=6. {ECO:0000255}.; TRANSMEM 281 300 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 44 Extracellular. {ECO:0000255}.; TOPO_DOM 68 78 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 102 120 Extracellular. {ECO:0000255}.; TOPO_DOM 144 155 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 179 208 Extracellular. {ECO:0000255}.; TOPO_DOM 232 243 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 267 280 Extracellular. {ECO:0000255}.; TOPO_DOM 301 344 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for the chemotactic and inflammatory C3a, C4a and C5a anaphylatoxin peptides and also for their dearginated forms ASP/C3adesArg, C4adesArg and C5adesArg respectively. Couples weakly to G(i)-mediated signaling pathways (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBUNIT: Interacts with C3 (the anaphylatoxin peptide C3a and the adipogenic hormone ASP); the interaction occurs with higher affinity for ASP, enhancing the phosphorylation and activation of GPR77, recruitment of ARRB2 to the cell surface and endocytosis of GRP77. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in liver and spleen. Lower levels in intestine, brain and kidney. Also expressed in adipose tissues with highest levels in gonadal and ingual fat depots. Lower levels in brown tissue. {ECO:0000269|PubMed:15833747}. +A2AGB2 CA087_MOUSE Uncharacterized protein C1orf87 homolog 545 62,440 Chain (1) +A2AQH4 BCORL_MOUSE BCL-6 corepressor-like protein 1 (BCoR-L1) (BCoR-like protein 1) 1781 190,487 Chain (1); Compositional bias (3); Cross-link (2); Erroneous initiation (2); Erroneous termination (1); Frameshift (1); Modified residue (5); Repeat (3); Sequence conflict (1) FUNCTION: Transcriptional corepressor. May specifically inhibit gene expression when recruited to promoter regions by sequence specific DNA-binding proteins such as BCL6. This repression may be mediated at least in part by histone deacetylase activities which can associate with this corepressor (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with CTBP1. Interacts with HDAC4, HDAC5 and HDAC7 (By similarity). Interacts with PCGF1; the interaction is direct (By similarity). {ECO:0000250}. +Q99PV8 BC11B_MOUSE B-cell lymphoma/leukemia 11B (BCL-11B) (B-cell CLL/lymphoma 11B) (COUP-TF-interacting protein 2) (Radiation-induced tumor suppressor gene 1 protein) (mRit1) 884 94,566 Alternative sequence (2); Chain (1); Compositional bias (1); Cross-link (5); Frameshift (1); Modified residue (25); Natural variant (3); Sequence conflict (3); Zinc finger (6) FUNCTION: Key regulator of both differentiation and survival of T-lymphocytes during thymocyte development in mammals (PubMed:12717433). Essential in controlling the responsiveness of hematopoietic stem cells to chemotactic signals by modulating the expression of receptors CCR7 and CCR9, which direct the movement of progenitor cells from the bone marrow to the thymus (By similarity). Is a regulator of IL2 promoter and enhances IL2 expression in activated CD4(+) T-lymphocytes (PubMed:16809611). Tumor-suppressor protein involved in T-cell lymphomas. May function on the P53-signaling pathway. Repress transcription through direct, TFCOUP2-independent binding to a GC-rich response element. {ECO:0000250|UniProtKB:Q9C0K0, ECO:0000269|PubMed:12717433, ECO:0000269|PubMed:16809611}. PTM: Sumoylated with SUMO1. {ECO:0000269|PubMed:23213215}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Interacts with TFCOUP1, SIRT1, ARP1 and EAR2 (PubMed:10744719, PubMed:12930829). Interacts with EP300; the interaction is detected in activated T-lymphocytes, but not under resting conditions (By similarity). {ECO:0000250|UniProtKB:Q9C0K0, ECO:0000269|PubMed:10744719, ECO:0000269|PubMed:12930829}. TISSUE SPECIFICITY: Expressed in brain and thymus. Expressed in splenic CD4(+) T-lymphocytes (PubMed:16809611). {ECO:0000269|PubMed:16809611}. +P00405 COX2_MOUSE Cytochrome c oxidase subunit 2 (Cytochrome c oxidase polypeptide II) 227 25,976 Chain (1); Metal binding (4); Modified residue (1); Topological domain (3); Transmembrane (2) TRANSMEM 27 48 Helical. {ECO:0000255}.; TRANSMEM 63 82 Helical. {ECO:0000255}. TOPO_DOM 1 26 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 49 62 Mitochondrial matrix. {ECO:0000255}.; TOPO_DOM 83 227 Mitochondrial intermembrane. {ECO:0000255}. FUNCTION: Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. Subunit 2 transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit 1. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SUBUNIT: Found in a complex with TMEM177, COA6, COX18, COX20, SCO1 and SCO2. Interacts with TMEM177 in a COX20-dependent manner. Interacts with COX20. Interacts with COX16. {ECO:0000250|UniProtKB:P00403}. +Q9Z2F6 BCL3_MOUSE B-cell lymphoma 3 protein homolog (BCL-3) 448 47,216 Chain (1); Compositional bias (1); Erroneous initiation (1); Modified residue (4); Repeat (7) FUNCTION: Contributes to the regulation of transcriptional activation of NF-kappa-B target genes. In the cytoplasm, inhibits the nuclear translocation of the NF-kappa-B p50 subunit (By similarity). In the nucleus, acts as transcriptional activator that promotes transcription of NF-kappa-B target genes. Contributes to the regulation of cell proliferation. {ECO:0000250, ECO:0000269|PubMed:16713561}. PTM: Polyubiquitinated. Ubiquitination via 'Lys-63'-linked ubiquitin chains is required for nuclear accumulation. Deubiquitinated by CYLD, which acts on 'Lys-63'-linked ubiquitin chains. Deubiquitination by CYLD prevents nuclear accumulation.; PTM: Activated by phosphorylation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16713561}. Cytoplasm {ECO:0000269|PubMed:16713561}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16713561}. Note=Ubiquitination via 'Lys-63'-linked ubiquitin chains is required for nuclear accumulation. SUBUNIT: Component of a complex consisting of the NF-kappa-B p52-p52 homodimer and BCL3. Component of a complex consisting of the NF-kappa-B p50-p50 homodimer and BCL3. Interacts with N4BP2, COPS5 and PIR (By similarity). Interacts with CYLD. {ECO:0000250, ECO:0000269|PubMed:16713561, ECO:0000269|PubMed:19893491}. +O88282 BCL6B_MOUSE B-cell CLL/lymphoma 6 member B protein (Bcl6-associated zinc finger protein) 474 51,339 Chain (1); Compositional bias (2); Domain (1); Zinc finger (5) FUNCTION: Acts as a sequence-specific transcriptional repressor in association with BCL6. Necessary for activation of naive T-cells to antigenic stimulation. May attenuate the regulatory effect of BCL6 on antigenic activation of naive CD4 T-cells by forming a heterodimer with BCL6. {ECO:0000269|PubMed:15314041, ECO:0000269|PubMed:9632807}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Associates with BCL6 through the BTB domain. DOMAIN: Amino acids 178-210 are essential for repression activity. TISSUE SPECIFICITY: Ubiquitously expressed with higher expression found in heart and lung. {ECO:0000269|PubMed:9632807}. +P41183 BCL6_MOUSE B-cell lymphoma 6 protein homolog 707 78,982 Chain (1); Domain (1); Modified residue (5); Mutagenesis (4); Region (1); Sequence conflict (1); Zinc finger (6) FUNCTION: Transcriptional repressor mainly required for germinal center (GC) formation and antibody affinity maturation which has different mechanisms of action specific to the lineage and biological functions. Forms complexes with different corepressors and histone deacetylases to repress the transcriptional expression of different subsets of target genes. Represses its target genes by binding directly to the DNA sequence 5'-TTCCTAGAA-3' (BCL6-binding site) or indirectly by repressing the transcriptional activity of transcription factors. In GC B-cells, represses genes that function in differentiation, inflammation, apoptosis and cell cycle control, also autoregulates its transcriptional expression and up-regulates, indirectly, the expression of some genes important for GC reactions, such as AICDA, through the repression of microRNAs expression, like miR155. An important function is to allow GC B-cells to proliferate very rapidly in response to T-cell dependent antigens and tolerate the physiological DNA breaks required for immunglobulin class switch recombination and somatic hypermutation without inducing a p53/TP53-dependent apoptotic response. In follicular helper CD4(+) T-cells (T(FH) cells), promotes the expression of T(FH)-related genes but inhibits the differentiation of T(H)1, T(H)2 and T(H)17 cells. Also required for the establishment and maintenance of immunological memory for both T- and B-cells. Suppresses macrophage proliferation through competition with STAT5 for STAT-binding motifs binding on certain target genes, such as CCL2 and CCND2. In response to genotoxic stress, controls cell cycle arrest in GC B-cells in both p53/TP53-dependedent and -independent manners. Besides, also controls neurogenesis through the alteration of the composition of NOTCH-dependent transcriptional complexes at selective NOTCH targets, such as HES5, including the recruitment of the deacetylase SIRT1 and resulting in an epigenetic silencing leading to neuronal differentiation. {ECO:0000269|PubMed:10981963, ECO:0000269|PubMed:12021781, ECO:0000269|PubMed:23160044, ECO:0000269|PubMed:23166356, ECO:0000269|PubMed:23455674}. PTM: Phosphorylated by MAPK1 in response to antigen receptor activation at Ser-334 and Ser-344. Phosphorylated by ATM in response to genotoxic stress. Phosphorylation induces its degradation by ubiquitin/proteasome pathway. {ECO:0000250|UniProtKB:P41182}.; PTM: Polyubiquitinated. Polyubiquitinated by SCF(FBXO11), leading to its degradation by the proteasome. Ubiquitinated by the SCF(FBXL17) complex, leading to its degradation by the proteaseome: ubiquitination by the SCF(FBXL17) complex takes place when aberrant BTB domain dimers are formed. {ECO:0000250|UniProtKB:P41182}.; PTM: Acetylated at Lys-380 by EP300 which inhibits the interaction with NuRD complex and the transcriptional repressor function. Deacetylated by HDAC- and SIR2-dependent pathways. {ECO:0000250|UniProtKB:P41182}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9927193}. SUBUNIT: Homodimer. Interacts (via BTB domain) with the corepressors BCOR, NCOR1 and SMRT/NCOR2; the interactions are direct. Forms preferably ternary complexes with BCOR and SMRT/NCOR2 on target gene promoters but, on enhancer elements, interacts with SMRT/NCOR2 and HDAC3 to repress proximal gene expression. Interacts with histone deacetylases HDAC2, HDAC5 and HDAC9 (via the catalytic domain). Interacts with ZBTB7 and BCL6B. Interacts with SCF(FBXO11) complex; the interaction is independent of phosphorylation and promotes ubiquitination. Interacts (when phosphorylated) with PIN1; the interaction is required for BCL6 degradation upon genotoxic stress. Interacts with ZBTB17; inhibits ZBTB17 transcriptional activity. Interacts with CTBP1, autoinhibits its transcriptional expression. Interacts with NOTCH1 NCID and SIRT1; leads to a epigenetic repression of selective NOTCH1-target genes. Interacts (nor via BTB domain neither acetylated) with the NuRD complex components CHD4, HDAC1, MBD3 and MTA3; the interaction with MTA3 inhibits BCL6 acetylation and is required for BCL6 transpriptional repression. {ECO:0000269|PubMed:23160044, ECO:0000269|PubMed:23455674, ECO:0000269|PubMed:9632807, ECO:0000269|PubMed:9927193}. DOMAIN: Interaction with corepressors through the BTB domain is needed to facilitate the rapid proliferation and survival of GC B-cells but is not involved in the T(FH) formation and BCL6-mediated suppression of T(H)2 and T(H)17 differentiation required for GC formation. {ECO:0000269|PubMed:23455674}. TISSUE SPECIFICITY: Expressed at least in germinal center B-cells of spleen. {ECO:0000269|PubMed:17828269, ECO:0000269|PubMed:23166356}. +Q9CZP5 BCS1_MOUSE Mitochondrial chaperone BCS1 (BCS1-like protein) 418 47,406 Chain (1); Initiator methionine (1); Modified residue (1); Nucleotide binding (1); Topological domain (2); Transmembrane (1) TRANSMEM 16 32 Helical. {ECO:0000255}. TOPO_DOM 2 15 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 33 418 Mitochondrial matrix. {ECO:0000255}. FUNCTION: Chaperone necessary for the assembly of mitochondrial respiratory chain complex III. Plays an important role in the maintenance of mitochondrial tubular networks, respiratory chain assembly and formation of the LETM1 complex (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with LETM1. {ECO:0000250}. +Q9D219 BCL9_MOUSE B-cell CLL/lymphoma 9 protein (B-cell lymphoma 9 protein) (Bcl-9) 1425 148,971 Chain (1); Compositional bias (2); Erroneous initiation (1); Modified residue (12); Region (2); Sequence conflict (1) FUNCTION: Promotes beta-catenin's transcriptional activity. Involved in signal transduction through the Wnt pathway (By similarity). {ECO:0000250, ECO:0000269|PubMed:15371335}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15371335}. SUBUNIT: Binds to beta-catenin (CTNNB1), PYGO1 and PYGO2; the interaction with PYGO1 increases PYGO1 affinity to histone H3 methylated at 'Lys 4'. {ECO:0000250}. +Q80XN0 BDH_MOUSE D-beta-hydroxybutyrate dehydrogenase, mitochondrial (EC 1.1.1.30) (3-hydroxybutyrate dehydrogenase) (BDH) 343 38,299 Active site (1); Binding site (1); Chain (1); Glycosylation (1); Modified residue (12); Nucleotide binding (1); Sequence conflict (4); Transit peptide (1) PTM: Acetylation of Lys-132 is observed in liver mitochondria from fasted mice but not from fed mice. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q02337}. Mitochondrion matrix {ECO:0000250|UniProtKB:Q02337}. SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q02337}. +Q9EQG5 BEAN1_MOUSE Protein BEAN1 (Brain-expressed protein associating with Nedd4) (BEAN) 255 28,538 Alternative sequence (1); Chain (1); Compositional bias (2); Erroneous initiation (1); Frameshift (1); Mutagenesis (2); Transmembrane (1) TRANSMEM 37 57 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. SUBUNIT: Interacts with NEDD4. {ECO:0000269|PubMed:11042109}. +O88597 BECN1_MOUSE Beclin-1 (Coiled-coil myosin-like BCL2-interacting protein) [Cleaved into: Beclin-1-C 35 kDa; Beclin-1-C 37 kDa] 448 51,589 Chain (3); Coiled coil (1); Cross-link (1); Helix (2); Modified residue (6); Motif (1); Mutagenesis (2); Region (3); Sequence conflict (3) FUNCTION: Plays a central role in autophagy (PubMed:10604474, PubMed:12372286, PubMed:19270693, PubMed:28445460). Acts as core subunit of different PI3K complex forms that mediate formation of phosphatidylinositol 3-phosphate and are believed to play a role in multiple membrane trafficking pathways: PI3KC3-C1 is involved in initiation of autophagosomes and PI3KC3-C2 in maturation of autophagosomes and endocytosis (PubMed:19270693, PubMed:25275521). Involved in regulation of degradative endocytic trafficking and required for the abcission step in cytokinesis, probably in the context of PI3KC3-C2 (By similarity). Essential for the formation of PI3KC3-C2 but not PI3KC3-C1 PI3K complex forms (PubMed:25275521). Involved in endocytosis including endosome formation in neuronal cells (PubMed:25275521). May play a role in antiviral host defense (By similarity). {ECO:0000250|UniProtKB:Q14457, ECO:0000269|PubMed:10604474, ECO:0000269|PubMed:12372286, ECO:0000269|PubMed:19270693, ECO:0000269|PubMed:25275521, ECO:0000269|PubMed:28445460}.; FUNCTION: Beclin-1-C 35 kDa localized to mitochondria can promote apoptosis; it induces the mitochondrial translocation of BAX and the release of proapoptotic factors (By similarity). {ECO:0000250|UniProtKB:Q14457}. PTM: Phosphorylation at Thr-117 by DAPK1 reduces its interaction with BCL2 and BCL2L1 and promotes induction of autophagy (By similarity). In response to autophagic stimuli, phosphorylated at serine residues by AMPK in an ATG14-dependent manner, and this phosphorylation is critical for maximally efficient autophagy. {ECO:0000250|UniProtKB:Q14457, ECO:0000269|PubMed:23332761}.; PTM: Polyubiquitinated by NEDD4, both with 'Lys-11'- and 'Lys-63'-linkages (By similarity). 'Lys-11'-linked poyubiquitination leads to degradation and is enhanced when the stabilizing interaction partner VPS34 is depleted (By similarity). Deubiquitinated by USP10 and USP13, leading to stabilize the PIK3C3/VPS34-containing complexes (By similarity). Polyubiquitinated at Lys-400 with 'Lys-48'-linkages (PubMed:28445460). 'Lys-48'-linked poyubiquitination of Lys-400 leads to degradation (PubMed:28445460). Deubiquitinated by ATXN3, leading to stabilization (PubMed:28445460). {ECO:0000250|UniProtKB:Q14457, ECO:0000269|PubMed:28445460}.; PTM: Proteolytically processed by caspases including CASP8 and CASP3; the C-terminal fragments lack autophagy-inducing capacity and are proposed to induce apoptosis. Thus the cleavage is proposed to be an determinant to switch from autophagy to apoptosis pathways affecting cellular homeostasis including viral infections and survival of tumor cells. {ECO:0000305|PubMed:21364619}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12372286}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q14457}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q14457}. Endosome membrane {ECO:0000250|UniProtKB:Q14457}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q14457}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q14457}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q14457}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q14457}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q14457}. Endosome {ECO:0000269|PubMed:25275521}. Cytoplasmic vesicle, autophagosome {ECO:0000305}. Note=Interaction with ATG14 promotes translocation to autophagosomes (By similarity). Expressed in dendrites and cell bodies of cerebellar Purkinje cells. Localized to endosomes in neurons (PubMed:25275521). {ECO:0000250|UniProtKB:Q14457, ECO:0000269|PubMed:12372286, ECO:0000269|PubMed:25275521}.; SUBCELLULAR LOCATION: Beclin-1-C 35 kDa: Mitochondrion {ECO:0000269|PubMed:21364619}. Nucleus {ECO:0000250|UniProtKB:Q14457}. Cytoplasm {ECO:0000250|UniProtKB:Q14457}.; SUBCELLULAR LOCATION: Beclin-1-C 37 kDa: Mitochondrion {ECO:0000269|PubMed:21364619}. SUBUNIT: A homodimeric form is proposed to exist; this metastable form readily transits to ATG14- or UVRAG-containing complexes with BECN1:UVRAG being more stable than BECN1:ATG14 (By similarity). Component of the PI3K (PI3KC3/PI3K-III/class III phosphatidylinositol 3-kinase) complex whose core is composed of the catalytic subunit PIK3C3, the regulatory subunit PIK3R4 and BECN1, and associates with additional regulatory/auxilliary subunits to form alternative complex forms. Accepted alternative complex forms containing a forth regulatory subunit in a mutually exclusive manner are PI3K complex I (PI3KC3-C1) containing ATG14, and PI3K complex II (PI3KC3-C2) containing UVRAG (PubMed:19270693, PubMed:23332761). PI3KC3-C1 displays a V-shaped architecture with PIK3R4 serving as a bridge between PIK3C3 and the ATG14:BECN1 subcomplex (By similarity). Both, PI3KC3-C1 and PI3KC3-C2, can associate with further regulatory subunits, such as RUBCN, SH3GLB1/Bif-1 and AMBRA1 (PubMed:19270693). PI3KC3-C1 probably associates with PIK3CB (PubMed:21059846.) Interacts with AMBRA1, GOPC, GRID2 and PIK3CB (PubMed:12372286, PubMed:17589504). Interacts with BCL2 and BCL2L1 isoform Bcl-X(L); the interaction inhibits BECN1 function in promoting autophagy by interfering with the formation of the PI3K complex (By similarity). Interacts with cytosolic HMGB1; inhibits the interaction of BECN1 and BCL2 leading to promotion of autophagy (PubMed:20819940). Interacts with USP10, USP13, VMP1, DAPK1 (By similarity). Interacts with the poly-Gln domain of ATXN3; the interaction causes deubiquitination at Lys-400 and stabilizes BECN1 (PubMed:28445460). Interacts with SLAMF1 (PubMed:22493499). Interacts with TRIM5; the interaction causes activation of BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2 (By similarity). Interacts with active ULK1 (phosphorylated on 'Ser-317') and MEFV simultaneously (By similarity). Interacts with TRIM50 (PubMed:29604308). Interacts with TRIM16 (By similarity). Interacts with WDR81 and WDR91; negatively regulates the PI3 kinase/PI3K activity associated with endosomal membranes (By similarity). Interacts with LAPTM4B; competes with EGFR for LAPTM4B binding; regulates EGFR activity (By similarity). {ECO:0000250|UniProtKB:Q14457, ECO:0000250|UniProtKB:Q91XJ1, ECO:0000269|PubMed:12372286, ECO:0000269|PubMed:17589504, ECO:0000269|PubMed:18248095, ECO:0000269|PubMed:19270693, ECO:0000269|PubMed:20819940, ECO:0000269|PubMed:21059846, ECO:0000269|PubMed:22493499, ECO:0000269|PubMed:23332761, ECO:0000269|PubMed:29604308, ECO:0000305, ECO:0000305|PubMed:28445460}.; SUBUNIT: (Microbial infection) Interacts with murine gammaherpesvirus 68 M11; the viral protein binds BECN1 with higher affinity than cellular BCL2. {ECO:0000269|PubMed:18248095}. DOMAIN: The coiled coil domain can form antiparallel homodimers and mediates dimerization with the coiled coil domains of ATG14 or UVRAG involved in the formation of PI3K complexes. {ECO:0000250|UniProtKB:Q91XJ1}.; DOMAIN: The C-terminal evolutionary conserved domain (ECD) contains poly-Gln-binding domains such as the ATXN3 poly-Gln motif, consistent with structural docking models revealing two highly scored poly-Gln-binding pockets in the ECD. As some binding is observed with BECN1 lacking the ECD, other domains of BECN1 may also interact with ATXN3. {ECO:0000305|PubMed:28445460}. +Q68EF6 BEGIN_MOUSE Brain-enriched guanylate kinase-associated protein 600 65,309 Chain (1); Modified residue (18) FUNCTION: May sustain the structure of the postsynaptic density (PSD). SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. SUBUNIT: Interacts with DLG4 and DLGAP1 and forms a ternary complex. {ECO:0000250}. +Q6PAL0 BEND3_MOUSE BEN domain-containing protein 3 825 94,155 Chain (1); Cross-link (18); Domain (4); Modified residue (2); Motif (1) FUNCTION: Transcriptional repressor which associates with the NoRC (nucleolar remodeling complex) complex and plays a key role in repressing rDNA transcription. The sumoylated form modulates the stability of the NoRC complex component BAZ2A/TIP5 by controlling its USP21-mediated deubiquitination (By similarity). Binds to unmethylated major satellite DNA and is involved in the recruitment of the Polycomb repressive complex 2 (PRC2) to major satellites (PubMed:25457167). Stimulates the ERCC6L translocase and ATPase activities (By similarity). {ECO:0000250|UniProtKB:Q5T5X7, ECO:0000269|PubMed:25457167}. PTM: Sumoylated at Lys-20 by SUMO1 and at Lys-509 by SUMO1, SUMO2 and SUMO3. Sumoylation probably occurs sequentially, with that of Lys-20 preceding that of Lys-509. It does not alter association with heterochromatin, but is required for the repression of transcription. {ECO:0000250|UniProtKB:Q5T5X7}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5T5X7}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q5T5X7}. Note=In the nucleus, observed in heterochromatic foci containing CBX1, CBX3, CBX5 and histone H3 trimethylated at 'Lys-9'. Released from chromatin during decondensation. Association with heterochromatin does not depend on sumoylation. {ECO:0000250|UniProtKB:Q5T5X7}. SUBUNIT: Homooligomer, probably a homooctamer. Interacts with HDAC2 and HDAC3, but not HDAC1. Interacts with SALL4. Interacts with SMARCA5/SNF2H, BAZ2A/TIP5 and USP21 (By similarity). Interacts with the nucleosome remodeling and histone deacetylase (NuRD) repressor complex (PubMed:25457167). Interacts (via BEN domains 1 and 3) with ERCC6L (via N-terminal TPR repeat); the interaction is direct (By similarity). {ECO:0000250|UniProtKB:Q5T5X7, ECO:0000269|PubMed:25457167}. DOMAIN: The BEN domain 4 is necessary and sufficient for the localization of BEND3 to heterochromatic regions. {ECO:0000250|UniProtKB:Q5T5X7}. +Q91W29 COX42_MOUSE Cytochrome c oxidase subunit 4 isoform 2, mitochondrial (Cytochrome c oxidase subunit IV isoform 2) (COX IV-2) 172 20,206 Chain (1); Disulfide bond (1); Transit peptide (1) FUNCTION: This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. SUBCELLULAR LOCATION: Mitochondrion inner membrane. +Q8BSV3 BEND7_MOUSE BEN domain-containing protein 7 434 48,451 Alternative sequence (2); Chain (1); Compositional bias (1); Cross-link (4); Domain (1); Frameshift (1); Modified residue (2); Sequence conflict (1) +Q8BGM5 BEST2_MOUSE Bestrophin-2 (Vitelliform macular dystrophy 2-like protein 1) 508 57,023 Chain (1); Erroneous initiation (4); Intramembrane (1); Sequence conflict (1); Topological domain (6); Transmembrane (4) INTRAMEM 229 249 {ECO:0000255}. TRANSMEM 26 46 Helical. {ECO:0000255}.; TRANSMEM 71 91 Helical. {ECO:0000255}.; TRANSMEM 179 199 Helical. {ECO:0000255}.; TRANSMEM 271 291 Helical. {ECO:0000255}. TOPO_DOM 1 25 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 47 70 Extracellular. {ECO:0000255}.; TOPO_DOM 92 178 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 200 228 Extracellular. {ECO:0000255}.; TOPO_DOM 250 270 Extracellular. {ECO:0000255}.; TOPO_DOM 292 508 Cytoplasmic. {ECO:0000255}. FUNCTION: Forms calcium-sensitive chloride channels. Permeable to bicarbonate. {ECO:0000269|PubMed:18400985}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Mainly confined to the retinal pigment epithelium and colon. +Q99PV5 BHE41_MOUSE Class E basic helix-loop-helix protein 41 (bHLHe41) (Class B basic helix-loop-helix protein 3) (bHLHb3) (Differentially expressed in chondrocytes protein 2) (mDEC2) 410 43,946 Chain (1); Compositional bias (1); Cross-link (3); Domain (2) FUNCTION: Transcriptional repressor involved in the regulation of the circadian rhythm by negatively regulating the activity of the clock genes and clock-controlled genes. Acts as the negative limb of a novel autoregulatory feedback loop (DEC loop) which differs from the one formed by the PER and CRY transcriptional repressors (PER/CRY loop). Both these loops are interlocked as it represses the expression of PER1 and in turn is repressed by PER1/2 and CRY1/2. Represses the activity of the circadian transcriptional activator: CLOCK-ARNTL/BMAL1 heterodimer by competing for the binding to E-box elements (5'-CACGTG-3') found within the promoters of its target genes. Negatively regulates its own expression and the expression of DBP and BHLHE41/DEC2. Acts as a corepressor of RXR and the RXR-LXR heterodimers and represses the ligand-induced RXRA/B/G, NR1H3/LXRA, NR1H4 and VDR transactivation activity. {ECO:0000269|PubMed:12397359, ECO:0000269|PubMed:14672706, ECO:0000269|PubMed:18411297, ECO:0000269|PubMed:19786558, ECO:0000269|PubMed:24736997}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00380, ECO:0000255|PROSITE-ProRule:PRU00981}. SUBUNIT: Homodimer. Interacts with CIART. Interacts with ARNTL/BMAL1 and RXRA. {ECO:0000269|PubMed:12397359, ECO:0000269|PubMed:24736997}. TISSUE SPECIFICITY: Expressed in skeletal muscle, brain and lung. +Q9JI08 BIN3_MOUSE Bridging integrator 3 253 29,651 Chain (1); Coiled coil (2); Domain (1) FUNCTION: Involved in cytokinesis and septation where it has a role in the localization of F-actin. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. +G3X9K3 BIG1_MOUSE Brefeldin A-inhibited guanine nucleotide-exchange protein 1 (BIG1) (Brefeldin A-inhibited GEP 1) (ADP-ribosylation factor guanine nucleotide-exchange factor 1) 1846 208,500 Chain (1); Domain (1); Modified residue (9); Motif (1); Region (2) FUNCTION: Promotes guanine-nucleotide exchange on ARF1 and ARF3. Promotes the activation of ARF1/ARF3 through replacement of GDP with GTP. Involved in vesicular trafficking. Required for the maintenance of Golgi structure; the function may be independent of its GEF activity. Required for the maturaion of integrin beta-1 in the Golgi. Involved in the establishment and persistence of cell polarity during directed cell movement in wound healing. Proposed to act as A kinase-anchoring protein (AKAP) and may mediate crosstalk between Arf and PKA pathways. Inhibits GAP activity of MYO9B probably through competetive RhoA binding. The function in the nucleus remains to be determined (By similarity). {ECO:0000250}. PTM: Phosphorylated. In vitro phosphorylated by PKA reducing its GEF activity and dephosphorylated by phosphatase PP1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Golgi apparatus {ECO:0000250}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Nucleus {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Nucleus matrix {ECO:0000250}. Membrane {ECO:0000250}. Note=Translocates from cytoplasm to membranes and nucleus upon cAMP treatment. {ECO:0000250}. SUBUNIT: Homodimer. Interacts with ARFGEF2/BIG2; both proteins are probably part of the same or very similar macromolecular complexes. Interacts with FKBP2. Interacts with MYO9B. Interacts with PRKAR1A and PRKAR2A. Interacts with PPP1CC. Interacts with NCL, FBL, NUP62 and U3 small nucleolar RNA. Interacts with DPY30. Interacts with PDE3A. Interacts with KANK1. Interacts with TBC1D22A and TBC1D22B. {ECO:0000250|UniProtKB:Q9Y6D6}. +Q9DBG1 CP27A_MOUSE Sterol 26-hydroxylase, mitochondrial (EC 1.14.15.15) (5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol 27-hydroxylase) (Cytochrome P-450C27/25) (Cytochrome P450 27) (Sterol 27-hydroxylase) (Vitamin D(3) 25-hydroxylase) 533 60,720 Chain (1); Metal binding (1); Modified residue (7); Region (1); Transit peptide (1) Hormone biosynthesis; cholecalciferol biosynthesis. FUNCTION: Catalyzes the first step in the oxidation of the side chain of sterol intermediates; the 27-hydroxylation of 5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol. Has also a vitamin D3-25-hydroxylase activity. {ECO:0000250|UniProtKB:P17177}. PTM: Acetylation of Lys-125 and Lys-285 is observed in liver mitochondria from fasted mice but not from fed mice. SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}. +P20852 CP2A5_MOUSE Cytochrome P450 2A5 (EC 1.14.14.1) (CYPIIA5) (Coumarin 7-hydroxylase) (Cytochrome P450-15-COH) (Cytochrome P450-IIA3.2) 494 56,741 Chain (1); Metal binding (1); Modified residue (2) FUNCTION: Exhibits a high coumarin 7-hydroxylase activity. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. TISSUE SPECIFICITY: Liver, with a strong circadian rhythmicity. Circadian expression is regulated by DBP. {ECO:0000269|PubMed:10490589}. +Q8VED2 BL1S4_MOUSE Biogenesis of lysosome-related organelles complex 1 subunit 4 (BLOC-1 subunit 4) (Protein cappuccino homolog) 215 23,112 Chain (1); Coiled coil (2); Modified residue (1) FUNCTION: Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. Plays a role in intracellular vesicle trafficking. {ECO:0000269|PubMed:16760431, ECO:0000269|PubMed:19546860, ECO:0000269|PubMed:21998198}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12576321}. SUBUNIT: Octamer composed of one copy each BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8 (By similarity). Component of the biogenesis of lysosome-related organelles complex 1 (BLOC-1) composed of BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. The BLOC-1 complex associates with the AP-3 protein complex and membrane protein cargos. Interacts with BLOC1S5 and BLOC1S6. {ECO:0000250, ECO:0000269|PubMed:12576321}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12576321}. DISEASE: Note=Defects in Cno are the cause of the cappuccino (Cno) mutant, which is characterized by a severe oculocutaneous albinism due to abnormal melanosome formation, and prolonged bleeding due to deficiency of platelet dense body contents. {ECO:0000269|PubMed:11110696}. +Q9CWG9 BL1S2_MOUSE Biogenesis of lysosome-related organelles complex 1 subunit 2 (BLOC-1 subunit 2) 143 16,300 Chain (1); Coiled coil (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (1) FUNCTION: Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes (By similarity). In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals (PubMed:16760431, PubMed:21998198). The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension (PubMed:19546860). As part of the BORC complex may play a role in lysosomes movement and localization at the cell periphery. Associated with the cytosolic face of lysosomes, the BORC complex may recruit ARL8B and couple lysosomes to microtubule plus-end-directed kinesin motor (By similarity). {ECO:0000250|UniProtKB:Q6QNY1, ECO:0000269|PubMed:16760431, ECO:0000269|PubMed:19546860, ECO:0000269|PubMed:21998198}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q6QNY1}. Lysosome membrane {ECO:0000250|UniProtKB:Q6QNY1}. Note=Localizes to the centrosomes in a microtubule-dependent manner. {ECO:0000250|UniProtKB:Q6QNY1}. SUBUNIT: Component of the biogenesis of lysosome-related organelles complex 1 (BLOC-1) composed of BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. Octamer composed of one copy each BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. Interacts directly with BLOC1S1, BLOC1S3, BLOC1S4, BLOC1S5 and SNAPIN (PubMed:15102850). The BLOC-1 complex associates with the AP-3 protein complex and membrane protein cargos (PubMed:21998198). Component of the BLOC-one-related complex (BORC) which is composed of BLOC1S1, BLOC1S2, BORCS5, BORCS6, BORCS7, BORCS8, KXD1 and SNAPIN (By similarity). Interacts with gamma-tubulin (By similarity). Interacts with IFT57 (PubMed:18188704). {ECO:0000250|UniProtKB:Q6QNY1, ECO:0000269|PubMed:15102850, ECO:0000269|PubMed:18188704, ECO:0000269|PubMed:21998198}. +P62951 BLCAP_MOUSE Bladder cancer-associated protein (Bladder cancer 10 kDa protein) (Bc10) 87 9,876 Chain (1); Sequence conflict (5); Transmembrane (2) TRANSMEM 19 39 Helical. {ECO:0000255}.; TRANSMEM 43 63 Helical. {ECO:0000255}. FUNCTION: May regulate cell proliferation and coordinate apoptosis and cell cycle progression via a novel mechanism independent of both p53/TP53 and NF-kappa-B. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9QUK4 BIR1B_MOUSE Baculoviral IAP repeat-containing protein 1b (Neuronal apoptosis inhibitory protein 2) 1447 164,083 Binding site (1); Chain (1); Domain (1); Metal binding (4); Repeat (3); Sequence conflict (15) FUNCTION: Sensor component of the NLRC4 inflammasome that specifically recognizes and binds type III secretion system (T3SS) rod proteins such as S.typhimurium (Salmonella) PrgJ and B.thailandensis BsaK from pathogenic bacteria. Association of pathogenic bacteria proteins drives in turn drive assembly and activation of the NLRC4 inflammasome, promoting caspase-1 activation, cytokine production and macrophage pyroptosis. The NLRC4 inflammasome is activated as part of the innate immune response to a range of intracellular bacteria. The NLRC4 inflammasome senses Gram-negative bacteria such as L.pneumophila and P.aeruginosa, enteric pathogens S.typhimurium (Salmonella) and S.flexneri. Prevents motor-neuron apoptosis induced by a variety of signals. {ECO:0000269|PubMed:21874021, ECO:0000269|PubMed:21918512}. SUBUNIT: Component of the NLRC4 inflammasome, at least composed of NLRC4, caspase-1 (CASP1) and some NAIP protein. Interacts with S.typhimurium (Salmonella) PrgJ and B.thailandensis BsaK. {ECO:0000269|PubMed:21874021, ECO:0000269|PubMed:21918512}. +Q99JU7 BNIPL_MOUSE Bcl-2/adenovirus E1B 19 kDa-interacting protein 2-like protein 328 36,785 Chain (1); Compositional bias (1); Domain (1) FUNCTION: May be a bridge molecule between BCL2 and ARHGAP1/CDC42 in promoting cell death. SUBUNIT: Homodimer. Interacts with BCL2, ARHGAP1, MIF and GFER (By similarity). {ECO:0000250}. +Q8C3R1 BRAT1_MOUSE BRCA1-associated ATM activator 1 (BRCA1-associated protein required for ATM activation protein 1) 822 89,086 Alternative sequence (2); Chain (1); Erroneous initiation (1); Frameshift (1); Modified residue (1); Region (1); Repeat (2); Sequence conflict (2) FUNCTION: Involved in DNA damage response; activates kinases ATM, SMC1A and PRKDC by modulating their phosphorylation status following ionizing radiation (IR) stress. Plays a role in regulating mitochondrial function and cell proliferation (By similarity). Required for protein stability of MTOR and MTOR-related proteins, and cell cycle progress by growth factors (PubMed:25657994). {ECO:0000250|UniProtKB:Q6PJG6, ECO:0000269|PubMed:25657994}. PTM: Ubiquitinated by NEDD4, NEDD4L and ITCH; mono- and polyubiquitinated forms are detected. {ECO:0000250|UniProtKB:Q6PJG6}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25631046}. Cytoplasm {ECO:0000269|PubMed:25631046}. Note=Present at double strand breaks (DSBs) following ionizing radiation treatment (By similarity). The ubiquitinated form localizes in the nucleus in a NDFIP1-dependent manner. {ECO:0000250|UniProtKB:Q6PJG6, ECO:0000269|PubMed:25631046}. SUBUNIT: Interacts with BRCA1 and ATM. Interacts with MTOR, RPTOR, NDFIP1, SMC1A and PRKDC. {ECO:0000250|UniProtKB:Q6PJG6}. TISSUE SPECIFICITY: High levels detected in the cortex and much lower levels detected in the cerebellum, spinal cord and lung (at protein level). {ECO:0000269|PubMed:22977523}. +O88379 BAZ1A_MOUSE Bromodomain adjacent to zinc finger domain protein 1A (Cbp146) 1555 178,459 Chain (1); Coiled coil (2); Compositional bias (3); Cross-link (1); Domain (3); Erroneous initiation (1); Modified residue (14); Region (3); Sequence conflict (3); Zinc finger (1) FUNCTION: Component of the ACF complex, an ATP-dependent chromatin remodeling complex, that regulates spacing of nucleosomes using ATP to generate evenly spaced nucleosomes along the chromatin. The ATPase activity of the complex is regulated by the length of flanking DNA. Also involved in facilitating the DNA replication process. BAZ1A is the accessory, non-catalytic subunit of the complex which can enhance and direct the process provided by the ATPase subunit, SMARCA5, probably through targeting pericentromeric heterochromatin in late S phase. Moves end-positioned nucleosomes to a predominantly central position. May have a role in nuclear receptor-mediated transcription repression (By similarity). {ECO:0000250}.; FUNCTION: Component of the histone-fold protein complex CHRAC complex which facilitates nucleosome sliding by the ACF complex and enhances ACF-mediated chromatin assembly. The C-terminal regions of both CHRAC1 and POLE1 are required for these functions (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Note=Concentrated in pericentric to heterochromatin. SUBUNIT: Component of the ACF chromatin remodeling complex that includes BAZ1A and SMARCA5. Additional this complex can form, together with CHRAC1 and POLE1, the histone-fold protein complex, CHRAC. Interacts with NCOR1 (via its RD1 domain); the interaction corepresses a number of NCOR1-regulated genes (By similarity). {ECO:0000250}. +Q9DBI2 BBS10_MOUSE Bardet-Biedl syndrome 10 protein homolog 713 78,924 Chain (1); Sequence caution (1) FUNCTION: Probable molecular chaperone that assists the folding of proteins upon ATP hydrolysis. Plays a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Involved in adipogenic differentiation. {ECO:0000250|UniProtKB:Q8TAM1}. SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000250|UniProtKB:Q8TAM1}. Note=Located within the basal body of the primary cilium of differentiating preadipocytes. {ECO:0000250|UniProtKB:Q8TAM1}. SUBUNIT: Component of a complex composed at least of MKKS, BBS10, BBS12, TCP1, CCT2, CCT3, CCT4, CCT5 AND CCT8. {ECO:0000250|UniProtKB:Q8TAM1}. +Q9Z319 CORIN_MOUSE Atrial natriuretic peptide-converting enzyme (EC 3.4.21.-) (Corin) (Low density lipoprotein receptor-related protein 4) (Pro-ANP-converting enzyme) [Cleaved into: Atrial natriuretic peptide-converting enzyme, N-terminal propeptide; Atrial natriuretic peptide-converting enzyme, activated protease fragment; Atrial natriuretic peptide-converting enzyme, 180 kDa soluble fragment] 1113 123,006 Active site (3); Alternative sequence (1); Chain (4); Disulfide bond (37); Domain (11); Glycosylation (17); Sequence conflict (4); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 113 133 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 112 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 134 1113 Extracellular. {ECO:0000255}. FUNCTION: Serine-type endopeptidase involved in atrial natriuretic peptide hormone (NPPA) processing. Converts through proteolytic cleavage the non-functional propeptide NPPA into the active hormone, thereby regulating blood pressure in heart and promoting natriuresis, diuresis and vasodilation. Proteolytic cleavage of pro-NPPA also plays a role in female pregnancy by promoting trophoblast invasion and spiral artery remodeling in uterus. Also acts as a regulator of sodium reabsorption in kidney. May also process pro-NPPB the B-type natriuretic peptide. {ECO:0000269|PubMed:11884416, ECO:0000269|PubMed:15637153, ECO:0000269|PubMed:20613715, ECO:0000269|PubMed:22418978, ECO:0000269|PubMed:22437503}. PTM: N-glycosylated; required for processing and activation. {ECO:0000250}.; PTM: Activated through proteolytic processing by a trypsin-like protease; cleaved into a N-terminal propeptide and an activated corin protease fragment. Atrial natriuretic peptide-converting enzyme, 180 kDa soluble fragment is produced by cleavage by ADAM10. Cleavage by ADAM10 to produce soluble 180 kDa soluble fragment takes place after the transmembrane region and before FZ 1 (By similarity). {ECO:0000250}.; PTM: A disulfide bond links the activated corin protease fragment and the N-terminal propeptide. The disulfide bond also links the activated corin protease fragment with Atrial natriuretic peptide-converting enzyme, 180 kDa soluble fragment (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: Atrial natriuretic peptide-converting enzyme, 180 kDa soluble fragment: Secreted {ECO:0000250}. Note=Soluble form produced following cleavage by ADAM10. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in heart. Also expressed in pregnant uterus. {ECO:0000269|PubMed:22437503}. +O08539 BIN1_MOUSE Myc box-dependent-interacting protein 1 (Amphiphysin II) (Amphiphysin-like protein) (Bridging integrator 1) (SH3 domain-containing protein 9) 588 64,470 Alternative sequence (2); Chain (1); Coiled coil (2); Domain (2); Initiator methionine (1); Modified residue (7); Region (2) FUNCTION: Is a key player in the control of plasma membrane curvature, and membrane shaping and remodeling. Required in muscle cells for the formation of T-tubules, tubular invaginations of the plasma membrane that function in depolarization-contraction coupling. Required in muscle cells for the formation of T-tubules, tubular invaginations of the plasma membrane that function in depolarization-contraction coupling (PubMed:12183633). Is a negative regulator of endocytosis (By similarity). Is also involved in the regulation of intracellular vesicles sorting, modulation of BACE1 trafficking and the control of amyloid-beta production (PubMed:12668730, PubMed:27179792). In neuronal circuits, endocytosis regulation may influence the internalization of PHF-tau aggregates (By similarity). May be involved in the regulation of MYC activity and the control cell proliferation (By similarity). {ECO:0000250|UniProtKB:O00499, ECO:0000250|UniProtKB:O08839, ECO:0000269|PubMed:12183633, ECO:0000269|PubMed:12668730, ECO:0000269|PubMed:27179792}. PTM: Phosphorylated by protein kinase C. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O00499}. Cytoplasm {ECO:0000269|PubMed:12668730}. Endosome {ECO:0000269|PubMed:12668730}. Cell membrane, sarcolemma, T-tubule {ECO:0000250|UniProtKB:O08839}. SUBUNIT: Heterodimer with AMPH (By similarity). Binds SH3GLB1 (PubMed:12456676). Interacts (via SH3 domain) with DNM1. Interacts with SYNJ1 (By similarity). Interacts (via SH3 domain) with DNM2. Interacts with CLTC (By similarity). Interacts with AP2A2. Interacts with AP2B1 (By similarity). Interacts with MYC (via N-terminal transactivation domain); the interaction requires the integrity of the conserved MYC box regions 1 and 2 (PubMed:8782822). Interacts with BIN2 (By similarity). Interacts with SNX4 (PubMed:12668730). Interacts (via BAR domain) with BACE1 (By similarity). Binds (via BAR domain) F-actin (By similarity). {ECO:0000250|UniProtKB:O00499, ECO:0000250|UniProtKB:O08839, ECO:0000269|PubMed:12456676, ECO:0000269|PubMed:12668730, ECO:0000269|PubMed:8782822}. TISSUE SPECIFICITY: Isoform 1 is expressed mainly in the brain. Isoform 2 is widely expressed. {ECO:0000269|PubMed:9182529}. +Q80Y61 BI2L2_MOUSE Brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 2 (BAI1-associated protein 2-like protein 2) (Planar intestinal- and kidney-specific BAR domain protein) (Pinkbar) 522 58,402 Alternative sequence (2); Beta strand (1); Chain (1); Domain (2); Helix (5); Modified residue (5); Mutagenesis (13) FUNCTION: Phosphoinositides-binding protein that induces the formation of planar or gently curved membrane structures. Binds to phosphoinositides, including to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) headgroups. There seems to be no clear preference for a specific phosphoinositide. {ECO:0000269|PubMed:21743456}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell junction {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}. Note=Localizes to RAB13-positive vesicles and to the plasma membrane at intercellular contacts. {ECO:0000250}. DOMAIN: The IMD domain consisting of an antiparallel dimer of three-helix bundles, featuring on one side a positively charged. The N-terminal alpha-helix inserts into the lipid bilayer. Also forms homodimers and homooligomers. The residue Trp-141 is essential for oligomer formation. TISSUE SPECIFICITY: Expressed in the epithelial layer of the intestine and in the kidney. {ECO:0000269|PubMed:21743456}. +Q6PB60 BHLH9_MOUSE Protein BHLHb9 (bHLHb9) 539 59,823 Chain (1); Erroneous initiation (1); Erroneous termination (1) FUNCTION: May play a role in the control of cellular aging and survival. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Mainly cytoplasmic, and nuclear at lower level. {ECO:0000250}. +O35490 BHMT1_MOUSE Betaine--homocysteine S-methyltransferase 1 (EC 2.1.1.5) 407 45,021 Chain (1); Domain (1); Metal binding (3); Modified residue (8); Sequence conflict (1) Amine and polyamine degradation; betaine degradation; sarcosine from betaine: step 1/2. Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (BhmT route): step 1/1. FUNCTION: Involved in the regulation of homocysteine metabolism. Converts betaine and homocysteine to dimethylglycine and methionine, respectively. This reaction is also required for the irreversible oxidation of choline. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Homotetramer. {ECO:0000250}. +O55102 BL1S1_MOUSE Biogenesis of lysosome-related organelles complex 1 subunit 1 (BLOC-1 subunit 1) (GCN5-like protein 1) 125 14,281 Chain (1); Coiled coil (1); Sequence conflict (3) FUNCTION: Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension (PubMed:16760431, PubMed:19546860, PubMed:21998198). As part of the BORC complex may play a role in lysosomes movement and localization at the cell periphery. The BORC complex is most probably associated with the cytosolic face of lysosomes, may recruit ARL8B and couple lysosomes to microtubule plus-end-directed kinesin motor (By similarity). {ECO:0000250|UniProtKB:P78537, ECO:0000269|PubMed:16760431, ECO:0000269|PubMed:19546860, ECO:0000269|PubMed:21998198}.; FUNCTION: May negatively regulate aerobic respiration through mitochondrial protein lysine-acetylation. May counteract the action of the deacetylase SIRT3 by acetylating and regulating proteins of the mitochondrial respiratory chain including ATP5F1A and NDUFA9. {ECO:0000250|UniProtKB:P78537}. SUBCELLULAR LOCATION: Mitochondrion intermembrane space {ECO:0000269|PubMed:22309213}. Mitochondrion matrix {ECO:0000269|PubMed:22309213}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P78537}. Lysosome membrane {ECO:0000250|UniProtKB:P78537}. SUBUNIT: Component of the biogenesis of lysosome-related organelles complex 1 (BLOC-1) composed of BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. Octamer composed of one copy each BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8 (PubMed:15102850). The BLOC-1 complex associates with the AP-3 protein complex and membrane protein cargos (PubMed:21998198). Interacts with ATP5F1A and NDUFA9; involved in their acetylation on lysine residues (By similarity). Interacts with KXD1 (PubMed:22554196). {ECO:0000250|UniProtKB:P78537, ECO:0000269|PubMed:15102850, ECO:0000269|PubMed:21998198, ECO:0000269|PubMed:22554196}. +P00158 CYB_MOUSE Cytochrome b (Complex III subunit 3) (Complex III subunit III) (Cytochrome b-c1 complex subunit 3) (Ubiquinol-cytochrome-c reductase complex cytochrome b subunit) 381 43,210 Binding site (1); Chain (1); Erroneous initiation (1); Metal binding (4); Transmembrane (8) TRANSMEM 33 53 Helical. {ECO:0000250|UniProtKB:P00157}.; TRANSMEM 77 98 Helical. {ECO:0000250|UniProtKB:P00157}.; TRANSMEM 113 133 Helical. {ECO:0000250|UniProtKB:P00157}.; TRANSMEM 178 198 Helical. {ECO:0000250|UniProtKB:P00157}.; TRANSMEM 226 246 Helical. {ECO:0000250|UniProtKB:P00157}.; TRANSMEM 288 308 Helical. {ECO:0000250|UniProtKB:P00157}.; TRANSMEM 320 340 Helical. {ECO:0000250|UniProtKB:P00157}.; TRANSMEM 347 367 Helical. {ECO:0000250|UniProtKB:P00157}. FUNCTION: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis. {ECO:0000250|UniProtKB:P00157}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:6326133}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P00157}. SUBUNIT: The cytochrome bc1 complex contains 11 subunits: 3 respiratory subunits (MT-CYB, CYC1 and UQCRFS1), 2 core proteins (UQCRC1 and UQCRC2) and 6 low-molecular weight proteins (UQCRH/QCR6, UQCRB/QCR7, UQCRQ/QCR8, UQCR10/QCR9, UQCR11/QCR10 and a cleavage product of UQCRFS1). This cytochrome bc1 complex then forms a dimer. {ECO:0000250|UniProtKB:P00157}. +Q9R016 BIR1E_MOUSE Baculoviral IAP repeat-containing protein 1e (Neuronal apoptosis inhibitory protein 5) 1403 159,839 Chain (1); Domain (1); Metal binding (4); Mutagenesis (18); Nucleotide binding (1); Repeat (3); Sequence conflict (19) FUNCTION: Sensor component of the NLRC4 inflammasome that specifically recognizes and binds flagellin from pathogenic bacteria such as Legionella or Salmonella (PubMed:12526741, PubMed:21874021, PubMed:21918512, PubMed:29146805, PubMed:29182158). Association of pathogenic bacteria proteins drives in turn drive assembly and activation of the NLRC4 inflammasome, promoting caspase-1 activation, cytokine production and macrophage pyroptosis (PubMed:21874021, PubMed:21918512, PubMed:29146805, PubMed:29182158). The NLRC4 inflammasome is activated as part of the innate immune response to a range of intracellular bacteria. The NLRC4 inflammasome senses Gram-negative bacteria such as L.pneumophila and P.aeruginosa, enteric pathogens S.typhimurium (Salmonella) and S.flexneri (PubMed:21874021, PubMed:21918512, PubMed:29146805, PubMed:29182158). May contribute to prevent motor-neuron apoptosis induced by a variety of signals (By similarity). {ECO:0000250|UniProtKB:Q13075, ECO:0000269|PubMed:12526741, ECO:0000269|PubMed:21874021, ECO:0000269|PubMed:21918512, ECO:0000269|PubMed:29146805, ECO:0000269|PubMed:29182158}. SUBUNIT: Component of the NLRC4 inflammasome, at least composed of NLRC4, caspase-1 (CASP1) and some NAIP protein. Flagellin binding by NAIP5 triggers assembly of the inflammasome, a huge complex that contains a single NAIP5 chain and multiple copies of NLRC4 (PubMed:29182158). {ECO:0000269|PubMed:21874021, ECO:0000269|PubMed:21918512, ECO:0000269|PubMed:29146805, ECO:0000269|PubMed:29182158}.; SUBUNIT: (Microbial infection) Interacts with S.typhimurium (Salmonella) flagellin. {ECO:0000269|PubMed:21874021, ECO:0000269|PubMed:21918512, ECO:0000269|PubMed:29182158}.; SUBUNIT: (Microbial infection) Interacts with L.pneumophila flagellin. {ECO:0000269|PubMed:29146805}. TISSUE SPECIFICITY: Detected in macrophages (at protein level). {ECO:0000269|PubMed:12526741}. +O88700 BLM_MOUSE Bloom syndrome protein homolog (mBLM) (EC 3.6.4.12) (RecQ helicase homolog) 1416 158,366 Binding site (2); Chain (1); Compositional bias (3); Cross-link (23); Domain (3); Metal binding (4); Modified residue (17); Motif (2); Mutagenesis (4); Nucleotide binding (2); Region (9); Sequence conflict (8); Site (6) FUNCTION: ATP-dependent DNA helicase that unwinds single- and double-stranded DNA in a 3'-5' direction (PubMed:9840919). Participates in DNA replication and repair (By similarity). Involved in 5'-end resection of DNA during double-strand break (DSB) repair: unwinds DNA and recruits DNA2 which mediates the cleavage of 5'-ssDNA (PubMed:9840919). Negatively regulates sister chromatid exchange (SCE) (PubMed:9840919, PubMed:27010503). Stimulates DNA 4-way junction branch migration and DNA Holliday junction dissolution. Binds single-stranded DNA (ssDNA), forked duplex DNA and DNA Holliday junction (By similarity). {ECO:0000250|UniProtKB:P54132, ECO:0000269|PubMed:27010503, ECO:0000269|PubMed:9840919}. PTM: Phosphorylated in response to DNA damage. Phosphorylation requires the FANCA-FANCC-FANCE-FANCF-FANCG protein complex, as well as the presence of RMI1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Together with SPIDR, is redistributed in discrete nuclear DNA damage-induced foci following hydroxyurea (HU) or camptothecin (CPT) treatment. Accumulated at sites of DNA damage in a RMI complex- and SPIDR-dependent manner (By similarity). {ECO:0000250}. SUBUNIT: Monomer. Homodimer (via N-terminus). Homotetramer (via N-terminus); dimer of dimers. Homohexamer (via N-terminus). Self-association negatively regulates DNA unwinding amplitude and rate. Oligomer complexes dissociate into monomer in presence of ATP. Part of the BRCA1-associated genome surveillance complex (BASC), which contains BRCA1, MSH2, MSH6, MLH1, ATM, BLM, PMS2 and the RAD50-MRE11-NBS1 protein complex. This association could be a dynamic process changing throughout the cell cycle and within subnuclear domains. Interacts with ubiquitinated FANCD2. Interacts with RMI complex. Interacts directly with RMI1 (via N-terminal region) component of RMI complex. Interacts with SUPV3L1. Found in a complex, at least composed of BLM, RAD51 and SPIDR; the complex formation is mediated by SPIDR. Interacts with TOP3A (via N-terminal region). Interacts with SPIDR (via C-terminal region); the interaction is direct and required to target BLM to sites of DNA damage. {ECO:0000250|UniProtKB:P54132}. DOMAIN: The N-terminal region mediates dimerization and homooligomerization. Both the helicase ATP-binding domain and the helicase C-terminal domain form intramolecular interactions with the HRDC domain in a ATP-dependent manner. The HRDC domain is required for single-stranded DNA (ssDNA) and DNA Holliday junction binding. {ECO:0000250|UniProtKB:P54132}. TISSUE SPECIFICITY: Highly expressed in testis 12-14 days after birth (corresponding to the pachytene phase) and at much lower levels in brain, heart, liver, lung, thymus, kidney and spleen (PubMed:9840919, PubMed:27010503). Expressed in bone marrow (PubMed:27010503). {ECO:0000269|PubMed:27010503, ECO:0000269|PubMed:9655940}. +P55105 BMP8B_MOUSE Bone morphogenetic protein 8B (BMP-8B) 399 44,943 Chain (1); Disulfide bond (4); Glycosylation (2); Propeptide (1); Sequence conflict (4); Signal peptide (1) FUNCTION: Induces cartilage and bone formation. May be the osteoinductive factor responsible for the phenomenon of epithelial osteogenesis. Plays a role in calcium regulation and bone homeostasis (By similarity). Involved in the generation of primordial germ cells; this function involves Bmp4 in a synergistic manner though separate receptor complexes seem to be involved. Required for the initiation and maintenance of spermatogenesis. Signaling protein involved in regulation of thermogenesis and energy balance. Proposed to increase the peripheral response of brown adipose tissue (BAT) to adrenergic stimulation while acting centrally in the hypothalamus to increase sympathetic output to BAT. {ECO:0000250, ECO:0000269|PubMed:10894154, ECO:0000269|PubMed:11427739, ECO:0000269|PubMed:22579288, ECO:0000269|PubMed:8682296}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Homodimer; disulfide-linked. {ECO:0000305|PubMed:11427739}. TISSUE SPECIFICITY: Expressed in testis. Expressed in decidual cells of the uterus and in trophoblast cells of the labyrinthine region of the placenta and in the inner root sheath of hair follicles of early postnatal skin. Expressed in the extraembryonic ectoderm in pregastrula and gastrula stage mouse embryos. Expressed in brown adipose tissue and brain. {ECO:0000269|PubMed:10894154, ECO:0000269|PubMed:22579288}. +Q61114 BPIB1_MOUSE BPI fold-containing family B member 1 (Long palate, lung and nasal epithelium carcinoma-associated protein 1) 474 52,455 Chain (1); Disulfide bond (1); Frameshift (1); Glycosylation (4); Sequence conflict (3); Signal peptide (1) FUNCTION: May play a role in innate immunity in mouth, nose and lungs. Binds bacterial lipopolysaccharide (LPS) and modulates the cellular responses to LPS. May be involved in formation of the left-right axis in the node of the developing embryo. {ECO:0000269|PubMed:14745963, ECO:0000269|PubMed:15028288}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14745963}. TISSUE SPECIFICITY: Expressed in tongue, lung, thymus, and stomach. Expressed in epithelia of palate, anterior pharynx, trachea and upper bronchi. Expressed in distal tip of papillae in the anterior third of the tongue and in serous cells of von Ebner glands in the posterior third of the tongue. Expressed in columnar epithelium of the duodenum in embryonic gut at 16.5 dpc. {ECO:0000269|PubMed:14745963, ECO:0000269|PubMed:15028288}. +Q3U1T3 BRM1L_MOUSE Breast cancer metastasis-suppressor 1-like protein 323 37,657 Alternative sequence (2); Chain (1); Coiled coil (2); Cross-link (2); Modified residue (1) FUNCTION: Involved in the histone deacetylase (HDAC1)-dependent transcriptional repression activity. When overexpressed in lung cancer cell line that lacks p53/TP53 expression, inhibits cell growth (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the Sin3/HDAC1 corepressor complex at least composed of BRMS1, BRMS1L and ING2/ING1L. Interacts with HDAC and SIN3A (By similarity). {ECO:0000250}. +Q8BXV2 BRI3B_MOUSE BRI3-binding protein (I3-binding protein) 253 28,263 Chain (1); Coiled coil (1); Modified residue (1); Sequence conflict (2); Transmembrane (4) TRANSMEM 19 39 Helical. {ECO:0000255}.; TRANSMEM 131 151 Helical. {ECO:0000255}.; TRANSMEM 164 181 Helical. {ECO:0000255}.; TRANSMEM 190 210 Helical. {ECO:0000255}. FUNCTION: Involved in tumorigenesis and may function by stabilizing p53/TP53. {ECO:0000269|PubMed:17943721}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with LETMD1. Interacts with BRI3. {ECO:0000250|UniProtKB:Q8WY22}. +Q99MQ1 BICC1_MOUSE Protein bicaudal C homolog 1 (Bic-C) 977 105,037 Alternative sequence (2); Chain (1); Domain (3); Modified residue (6); Sequence conflict (1) FUNCTION: Putative RNA-binding protein. May be involved in regulating gene expression during embryonic development. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19324013}. SUBUNIT: Interacts (via KH domains) with ANKS6 (via SAM domain) in an RNA-dependent manner. Interacts with ANKS3 (PubMed:25671767). {ECO:0000269|PubMed:19324013, ECO:0000269|PubMed:25671767}. TISSUE SPECIFICITY: In the adult, predominantly expressed in heart and kidney. In 8 week old mice, expressed in growing primary oocytes and in the stromal cells of the theca. {ECO:0000269|PubMed:11231089}. +O35084 CP27B_MOUSE 25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial (EC 1.14.15.18) (25-OHD-1 alpha-hydroxylase) (25-hydroxyvitamin D(3) 1-alpha-hydroxylase) (VD3 1A hydroxylase) (Calcidiol 1-monooxygenase) (Cytochrome P450 subfamily XXVIIB polypeptide 1) (Cytochrome P450C1 alpha) (Cytochrome P450VD1-alpha) (Cytochrome p450 27B1) 507 56,225 Chain (1); Erroneous initiation (1); Metal binding (1); Transit peptide (1) Hormone biosynthesis; cholecalciferol biosynthesis. FUNCTION: Catalyzes the conversion of 25-hydroxyvitamin D3 (25(OH)D3) to 1-alpha,25-dihydroxyvitamin D3 (1alpha,25(OH)(2)D3), and of 24,25-dihydroxyvitamin D3 (24,25(OH)(2)D3) to 1-alpha,24,25-trihydroxyvitamin D3 (1alpha,24,25(OH)(3)D3). Is also active with 25-hydroxy-24-oxo-vitamin D3. Plays an important role in normal bone growth, calcium metabolism, and tissue differentiation. {ECO:0000269|PubMed:10092858}. SUBCELLULAR LOCATION: Mitochondrion membrane. TISSUE SPECIFICITY: Kidney. +A0JNT9 BICL1_MOUSE BICD family-like cargo adapter 1 (Bicaudal D-related protein 1) (BICD-related protein 1) (BICDR-1) (Coiled-coil domain-containing protein 64A) 577 65,287 Alternative sequence (6); Chain (1); Coiled coil (2); Compositional bias (1); Helix (1); Mutagenesis (1); Sequence conflict (1) FUNCTION: Component of secretory vesicle machinery in developing neurons that acts as a regulator of neurite outgrowth. Regulates the secretory vesicle transport by controlling the accumulation of Rab6-containing secretory vesicles in the pericentrosomal region restricting anterograde secretory transport during the early phase of neuronal differentiation, thereby inhibiting neuritogenesis. {ECO:0000269|PubMed:20360680}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:20360680}. Note=Localizes around the centrosome. SUBUNIT: Interacts with KIF1C. Interacts with RAB6A and RAB6B; interaction is specific to Rab6. {ECO:0000269|PubMed:20360680}. TISSUE SPECIFICITY: Highly expressed during early embryonic development. Predominantly expressed in kidney, undifferentiated neural tissue and developing eye. {ECO:0000269|PubMed:20360680}. +Q5U5M8 BL1S3_MOUSE Biogenesis of lysosome-related organelles complex 1 subunit 3 (BLOC-1 subunit 3) (Reduced pigmentation protein) 195 20,398 Chain (1); Modified residue (2) FUNCTION: Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. Plays a role in intracellular vesicle trafficking. {ECO:0000269|PubMed:16760431, ECO:0000269|PubMed:19546860, ECO:0000269|PubMed:21998198}. PTM: Phosphorylated. {ECO:0000269|PubMed:15265785}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15265785}. SUBUNIT: Octamer composed of one copy each BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. Interacts directly with BLOC1S2 (By similarity). Component of the biogenesis of lysosome-related organelles complex 1 (BLOC-1) composed of BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. The BLOC-1 complex associates with the AP-3 protein complex and membrane protein cargos. Interacts with BLOC1S4, BLOC1S5 and BLOC1S6. {ECO:0000250, ECO:0000269|PubMed:15102850, ECO:0000269|PubMed:15265785, ECO:0000269|PubMed:17182842}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:15265785}. DISEASE: Note=Defects in Bloc1s3 are the cause of the reduced pigmentation (rp) mutation phenotype, a mouse model for human Hermansky-Pudlak syndrome (HPS). Rp mice are characterized by abnormal melanosomes and display altered expression levels of the proteins of the BLOC-1 complex. {ECO:0000269|PubMed:15265785}. +O35607 BMPR2_MOUSE Bone morphogenetic protein receptor type-2 (BMP type-2 receptor) (BMPR-2) (EC 2.7.11.30) (BRK-3) (Bone morphogenetic protein receptor type II) (BMP type II receptor) (BMPR-II) 1038 115,020 Active site (1); Binding site (2); Chain (1); Compositional bias (4); Disulfide bond (5); Domain (1); Glycosylation (3); Modified residue (5); Nucleotide binding (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 151 171 Helical. {ECO:0000255}. TOPO_DOM 27 150 Extracellular. {ECO:0000255}.; TOPO_DOM 172 1038 Cytoplasmic. {ECO:0000255}. FUNCTION: On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Binds to BMP7, BMP2 and, less efficiently, BMP4. Binding is weak but enhanced by the presence of type I receptors for BMPs. Mediates induction of adipogenesis by GDF6 (PubMed:23527555). {ECO:0000269|PubMed:23527555}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q13873}; Single-pass type I membrane protein. SUBUNIT: Interacts with GDF5. {ECO:0000250|UniProtKB:Q13873}. +O35425 BOK_MOUSE Bcl-2-related ovarian killer protein (Apoptosis activator Mtd) (Protein matador) 213 23,456 Alternative sequence (1); Chain (1); Cross-link (4); Modified residue (1); Motif (4); Mutagenesis (10); Region (2); Transmembrane (1) TRANSMEM 190 210 Helical. {ECO:0000255}. FUNCTION: Apoptosis regulator that functions through different apoptotic signaling pathways (PubMed:23429263, PubMed:26015568, PubMed:26949185, PubMed:27098698, PubMed:9535847). Plays a roles as pro-apoptotic protein that positively regulates intrinsic apoptotic process in a BAX- and BAK1-dependent manner or in a BAX- and BAK1-independent manner (PubMed:23429263, PubMed:26015568, PubMed:26949185). In response to endoplasmic reticulum stress promotes mitochondrial apoptosis through downstream BAX/BAK1 activation and positive regulation of PERK-mediated unfolded protein response (PubMed:26015568). Activates apoptosis independently of heterodimerization with survival-promoting BCL2 and BCL2L1 through induction of mitochondrial outer membrane permeabilization, in a BAX- and BAK1-independent manner, in response to inhibition of ERAD-proteasome degradation system, resulting in cytochrome c release (PubMed:9535847, PubMed:26949185). In response to DNA damage, mediates intrinsic apoptotic process in a TP53-dependent manner. Plays a role in granulosa cell apoptosis by CASP3 activation (By similarity). Plays a roles as anti-apoptotic protein during neuronal apoptotic process, by negatively regulating poly ADP-ribose polymerase-dependent cell death through regulation of neuronal calcium homeostasis and mitochondrial bioenergetics in response to NMDA excitation (PubMed:27098698). In addition to its role in apoptosis, may regulate trophoblast cell proliferation during the early stages of placental development, by acting on G1/S transition through regulation of CCNE1 expression.May also play a role as an inducer of autophagy by disrupting interaction between MCL1 and BECN1 (By similarity). {ECO:0000250|UniProtKB:Q9UMX3, ECO:0000269|PubMed:23429263, ECO:0000269|PubMed:26015568, ECO:0000269|PubMed:26949185, ECO:0000269|PubMed:27098698, ECO:0000269|PubMed:9535847}. PTM: Ubiquitinated by AMFR/gp78 E3 ubiquitin ligase complex; mediates degradation by ubiquitin-proteasome pathway in a VCP/p97-dependent manner; prevents from proapoptotic activity; promotes degradation of newly synthesized proteins that are not ITPR1 associated. {ECO:0000269|PubMed:23884412, ECO:0000269|PubMed:26949185, ECO:0000269|PubMed:27053113}. SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000269|PubMed:23429263, ECO:0000269|PubMed:26949185}; Single-pass membrane protein {ECO:0000269|PubMed:26949185}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:23429263, ECO:0000269|PubMed:26949185}; Single-pass membrane protein {ECO:0000269|PubMed:26949185}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9UMX3}. Cytoplasm {ECO:0000250|UniProtKB:Q9UMX3}. Nucleus {ECO:0000250|UniProtKB:Q9UMX3}. Mitochondrion {ECO:0000250|UniProtKB:Q9UMX3}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9UMX3}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q9UMX3}. Early endosome membrane {ECO:0000269|PubMed:23429263}. Recycling endosome membrane {ECO:0000269|PubMed:23429263}. Nucleus outer membrane {ECO:0000269|PubMed:23429263}. Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:23429263}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:23429263}. Membrane {ECO:0000250|UniProtKB:Q9UMX3}. Note=Nuclear and cytoplasmic compartments in the early stages of apoptosis and during apoptosis associates with mitochondria. In healthy cells, associates loosely with the membrane in a hit-and-run mode. The insertion and accumulation on membranes is enhanced through the activity of death signals, resulting in the integration of the membrane-bound protein into the membrane (By similarity). The transmembrane domain controls subcellular localization; constitutes a tail-anchor (PubMed:23429263, PubMed:26949185). Localizes in early and late endosome upon blocking of apoptosis (PubMed:23429263). Must localize to the mitochondria to induce mitochondrial outer membrane permeabilization and apoptosis (PubMed:26949185). {ECO:0000250|UniProtKB:Q9UMX3, ECO:0000269|PubMed:23429263, ECO:0000269|PubMed:26949185}. SUBUNIT: Monomer; positively regulates apoptotic process. Homodimer (PubMed:23429263). Heterodimer (By similarity). Oligomer; promoted by apoptotic stimuli and BH3-only proteins; mediates constitutive activation (PubMed:26949185). Interacts (via BH4 domain) with ITPR1; enhances BOK expression and stabilization; limits apoptosis and prevents ubiquitination and then degradation; protects ITPR1 from proteolysis by CASP3 during apoptosis (PubMed:27053113, PubMed:23884412). Interacts with ITPR2 AND ITPR3; binds most strongly to ITPR2, and barely to ITPR3; regulates their expression (PubMed:23884412). Interacts with XPO1; translocates to the cytoplasm (By similarity). Interacts with BNIP3; promotes oligomerization (By similarity). {ECO:0000250|UniProtKB:Q792S6, ECO:0000250|UniProtKB:Q9UMX3, ECO:0000269|PubMed:23429263, ECO:0000269|PubMed:23884412, ECO:0000269|PubMed:26949185, ECO:0000269|PubMed:27053113}. DOMAIN: BH4 domain mediates interaction with ITPR1. {ECO:0000269|PubMed:23884412, ECO:0000269|PubMed:27053113}. TISSUE SPECIFICITY: Widely expressed (PubMed:9535847, PubMed:23429263). Highly expressed in brain, kidney, and spleen (PubMed:27098698). {ECO:0000269|PubMed:23429263, ECO:0000269|PubMed:27098698, ECO:0000269|PubMed:9535847}. +Q8JZX9 BORG1_MOUSE Cdc42 effector protein 2 (Binder of Rho GTPases 1) 214 22,997 Chain (1); Domain (1); Initiator methionine (1); Modified residue (6) FUNCTION: Probably involved in the organization of the actin cytoskeleton. May act downstream of CDC42 to induce actin filament assembly leading to cell shape changes. Induces pseudopodia formation in fibroblasts in a CDC42-dependent manner (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. SUBUNIT: Interacts with CDC42 and RHOQ in a GTP-dependent manner, and with SEPT7. {ECO:0000250}. DOMAIN: The CRIB domain mediates interaction with CDC42. {ECO:0000250}. +Q9D920 BORC5_MOUSE BLOC-1-related complex subunit 5 195 22,120 Chain (1); Initiator methionine (1); Lipidation (1); Modified residue (2); Sequence conflict (1) FUNCTION: As part of the BORC complex may play a role in lysosomes movement and localization at the cell periphery. Associated with the cytosolic face of lysosomes, the BORC complex may recruit ARL8B and couple lysosomes to microtubule plus-end-directed kinesin motor. Thereby, it may indirectly play a role in cell spreading and motility. {ECO:0000250|UniProtKB:Q969J3}. PTM: Myristoylation at Gly-2 mediates attachment to lysosome membranes. {ECO:0000250|UniProtKB:Q969J3}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q969J3}; Lipid-anchor {ECO:0000250|UniProtKB:Q969J3}; Cytoplasmic side {ECO:0000250|UniProtKB:Q969J3}. SUBUNIT: Component of the BLOC-one-related complex (BORC) which is composed of BLOC1S1, BLOC1S2, BORCS5, BORCS6, BORCS7, BORCS8, KXD1 and SNAPIN. Interacts with ARL8B, KIF5A, KLC1 and PLEKHM2; links the lysosomal BORC complex to the microtubule plus-end-directed kinesin motor. {ECO:0000250|UniProtKB:Q969J3}. +Q8C186 BPIFC_MOUSE BPI fold-containing family C protein (Bactericidal/permeability-increasing protein-like 2) 509 56,616 Chain (1); Disulfide bond (1); Glycosylation (10); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +Q8R164 BPHL_MOUSE Valacyclovir hydrolase (VACVase) (Valacyclovirase) (EC 3.1.-.-) (Biphenyl hydrolase-like protein) 291 32,851 Active site (3); Chain (1); Domain (1); Erroneous initiation (1); Modified residue (15); Sequence conflict (3); Signal peptide (1); Site (1) FUNCTION: Serine hydrolase that catalyzes the hydrolytic activation of amino acid ester prodrugs of nucleoside analogs such as valacyclovir and valganciclovir. Activates valacyclovir to acyclovir. May play a role in detoxification processes. It is a specific alpha-amino acid ester hydrolase that prefers small, hydrophobic, and aromatic side chains and does not have a stringent requirement for the leaving group other than preferring a primary alcohol (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Monomer. May also form homodimers (By similarity). {ECO:0000250}. +Q91VR8 BRK1_MOUSE Protein BRICK1 (BRK1) 75 8,761 Chain (1); Coiled coil (1); Initiator methionine (1); Modified residue (1); Sequence conflict (1) FUNCTION: Involved in regulation of actin and microtubule organization. Part of a WAVE complex that activates the Arp2/3 complex (By similarity). As component of the WAVE1 complex, required for BDNF-NTRK2 endocytic trafficking and signaling from early endosomes (PubMed:27605705). {ECO:0000250|UniProtKB:Q8WUW1, ECO:0000269|PubMed:27605705}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. SUBUNIT: Homotrimer when in free form. Directly interacts with WASF2. Component of the WAVE1 complex composed of ABI2, CYFIP1 or CYFIP2, BRK1, NCKAP1 and WASF1/WAVE1. Within the complex, a heterodimer containing NCKAP1 and CYFIP1 interacts with a heterotrimer formed by WAVE1, ABI2 and BRK1 (By similarity). {ECO:0000250|UniProtKB:Q8WUW1}. +O54798 BRS3_MOUSE Bombesin receptor subtype-3 (BRS-3) 399 44,229 Chain (1); Disulfide bond (1); Glycosylation (3); Lipidation (1); Sequence conflict (1); Topological domain (8); Transmembrane (7) TRANSMEM 42 63 Helical; Name=1. {ECO:0000255}.; TRANSMEM 83 103 Helical; Name=2. {ECO:0000255}.; TRANSMEM 122 143 Helical; Name=3. {ECO:0000255}.; TRANSMEM 164 184 Helical; Name=4. {ECO:0000255}.; TRANSMEM 221 241 Helical; Name=5. {ECO:0000255}.; TRANSMEM 273 293 Helical; Name=6. {ECO:0000255}.; TRANSMEM 314 333 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 41 Extracellular. {ECO:0000255}.; TOPO_DOM 64 82 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 104 121 Extracellular. {ECO:0000255}.; TOPO_DOM 144 163 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 185 220 Extracellular. {ECO:0000255}.; TOPO_DOM 242 272 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 294 313 Extracellular. {ECO:0000255}.; TOPO_DOM 334 399 Cytoplasmic. {ECO:0000255}. FUNCTION: Role in sperm cell division, maturation, or function. This receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBUNIT: Interacts with C6orf89. {ECO:0000250}. +Q7M757 BRC3L_MOUSE Lys-63-specific deubiquitinase BRCC36-like (EC 3.4.19.-) 291 33,079 Chain (1); Domain (1); Metal binding (3); Motif (1) FUNCTION: Metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. {ECO:0000250}. +Q3UAW9 BRF2_MOUSE Transcription factor IIIB 50 kDa subunit (B-related factor 2) (BRF-2) 420 47,050 Chain (1); Compositional bias (1); Metal binding (3); Modified residue (2); Region (3); Repeat (2); Sequence conflict (3); Zinc finger (1) FUNCTION: General activator of RNA polymerase III transcription. Factor exclusively required for RNA polymerase III transcription of genes with promoter elements upstream of the initiation sites. Contributes to the regulation of gene expression; functions as activator in the absence of oxidative stress. Down-regulates expression of target genes in response to oxidative stress. Overexpression protects cells against apoptosis in response to oxidative stress. {ECO:0000250|UniProtKB:Q9HAW0}. PTM: In response to oxidative stress, Cys-362 is reversibly oxidized to cysteine sulfenic acid. Oxidation of Cys-362 impairs formation of a ternary complex with TBP and DNA and down-regulates expression of target genes in response to oxidative stress. {ECO:0000250|UniProtKB:Q9HAW0}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9HAW0}. SUBUNIT: Component of TFIIIB complexes. The TFIIIB complex has two activities, alpha and beta. The TFIIIB-alpha activity complex is composed of TBP, BDP1, and a complex containing both BRF2 and at least four stably associated proteins; this complex inhibits the transcription by pol III via its phosphorylation by CK2; YY1 facilitates the TFIIIB-alpha complex formation. Interacts with TBP; this interaction promotes recruitment of BRF2 to TATA box-containing promoters. Interacts with TBP and the BURE sequence (GC-rich sequence downstream from the TATA box) to form a strong ternary complex which is joined by BDP1; this ternary complex stimulates pol III transcription. Forms a trimeric complex composed of TBP, BRF2 and mini-SNAPc complex (SNAP43, SNAP50, and the N-terminal third of SNAP190) on the promoter. Assembly of the TBP-BRF2 complex is stimulated by SNAP190. Interacts with MAF1 and SNAPC4. {ECO:0000250|UniProtKB:Q9HAW0}. +Q8R3B7 BRD8_MOUSE Bromodomain-containing protein 8 951 102,610 Alternative sequence (1); Chain (1); Coiled coil (1); Cross-link (6); Domain (1); Erroneous initiation (2); Modified residue (8); Sequence caution (1); Sequence conflict (1) FUNCTION: May act as a coactivator during transcriptional activation by hormone-activated nuclear receptors (NR). Stimulates transcriptional activation by AR/DHTR, ESR1/NR3A1, RXRA/NR2B1 and THRB/ERBA2. Component of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AFZ from the nucleosome. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the NuA4 histone acetyltransferase complex which contains the catalytic subunit KAT5/TIP60 and the subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6. Component of a NuA4-related complex which contains EP400, TRRAP/PAF400, SRCAP, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, actin, ACTL6A/BAF53A, VPS72 and YEATS4/GAS41. BRD8 isoform 2 interacts with RXRA/NR2B1 and THRB/ERBA2. Component of a SWR1-like complex (By similarity). {ECO:0000250}. +Q9ER10 BSSP4_MOUSE Brain-specific serine protease 4 (BSSP-4) (EC 3.4.21.-) (Serine protease 22) (Serine protease 26) (Tryptase epsilon) 306 33,262 Active site (3); Chain (1); Disulfide bond (4); Domain (1); Glycosylation (1); Signal peptide (1) +Q62556 BT1A1_MOUSE Butyrophilin subfamily 1 member A1 (BT) 524 58,407 Chain (1); Disulfide bond (2); Domain (3); Frameshift (1); Glycosylation (2); Sequence conflict (10); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 248 268 Helical. {ECO:0000255}. TOPO_DOM 27 247 Extracellular. {ECO:0000255}.; TOPO_DOM 269 524 Cytoplasmic. {ECO:0000255}. FUNCTION: May function in the secretion of milk-fat droplets. May act as a specific membrane-associated receptor for the association of cytoplasmic droplets with the apical plasma membrane (By similarity). Inhibits the proliferation of CD4 and CD8 T-cells activated by anti-CD3 antibodies, T-cell metabolism and IL2 and IFNG secretion. {ECO:0000250, ECO:0000269|PubMed:20208008}. PTM: N-glycosylated. {ECO:0000269|PubMed:20208008}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. Note=Secreted in association with the milk-fat-globule membrane during lactation. SUBUNIT: Seems to associate with xanthine dehydrogenase/oxidase. TISSUE SPECIFICITY: Strongly expressed in lactating mammary tissue (at protein level). About 100-fold lower levels in virgin mammary tissue. Also detected in spleen and thymus at 10-20 times lower levels compared to those detected in virgin mammary gland. Very low levels in several other tissues, including brain, heart, kidney, lymph node, lung and small intestine. In the thymus, detected in the stroma, in epithelial cells (at protein level). Most prominent in medullary areas of the thymus and at the corticomedullary junction (at protein level). {ECO:0000269|PubMed:20208008}. +Q6GQW0 BTBDB_MOUSE Ankyrin repeat and BTB/POZ domain-containing protein BTBD11 (BTB/POZ domain-containing protein 11) 1109 121,561 Alternative sequence (5); Chain (1); Compositional bias (1); Domain (1); Repeat (5); Sequence conflict (1); Transmembrane (1) TRANSMEM 168 188 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +A4QPC6 BT2A2_MOUSE Butyrophilin subfamily 2 member A2 514 58,455 Alternative sequence (2); Chain (1); Coiled coil (1); Disulfide bond (2); Domain (3); Glycosylation (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 245 265 Helical. {ECO:0000255}. TOPO_DOM 30 244 Extracellular. {ECO:0000255}.; TOPO_DOM 266 514 Cytoplasmic. {ECO:0000255}. FUNCTION: Inhibits the proliferation of CD4 and CD8 T-cells activated by anti-CD3 antibodies, T-cell metabolism and IL2 and IFNG secretion. {ECO:0000269|PubMed:20208008}. PTM: N-glycosylated. {ECO:0000269|PubMed:20208008}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Widely expressed (at protein level). In the thymus, restricted to the corticomedullary junction, but not confined solely to epithelial cells (at protein level). Significant expression on naive B-cells, splenic natural killer cells, dendritic cells and peritoneal macrophages (at protein level). Negligible expression on naive T-cells up-regulated on activated T-cells (at protein level). {ECO:0000269|PubMed:20208008}. +O54825 BYST_MOUSE Bystin 436 49,784 Chain (1); Erroneous initiation (3); Modified residue (6); Sequence conflict (1) FUNCTION: Required for processing of 20S pre-rRNA precursor and biogenesis of 40S ribosomal subunits. {ECO:0000269|PubMed:17055491, ECO:0000269|PubMed:17242206}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17242206}. Nucleus, nucleolus {ECO:0000269|PubMed:17242206}. Note=Associated with 40S ribosomal subunits. SUBUNIT: Binds trophinin, tastin and cytokeratins. {ECO:0000250}. TISSUE SPECIFICITY: High levels in preimplantation embryos, bone marrow, brain, testis and ovary. {ECO:0000269|PubMed:17242206}. +Q7TPS5 C2CD5_MOUSE C2 domain-containing protein 5 (138 kDa C2 domain-containing phosphoprotein) 1016 111,664 Alternative sequence (3); Calcium binding (2); Chain (1); Domain (1); Erroneous initiation (1); Modified residue (20); Sequence conflict (7) FUNCTION: Required for insulin-stimulated glucose transport and glucose transporter SLC2A4/GLUT4 translocation from intracellular glucose storage vesicle (GSV) to the plasma membrane (PM) in adipocytes. Binds phospholipid membranes in a calcium-dependent manner and is necessary for the optimal membrane fusion between SLC2A4/GLUT4 GSV and the PM. {ECO:0000269|PubMed:21907143}. PTM: Phosphorylated on Ser-197 by active myristoylated kinase AKT2; insulin-stimulated phosphorylation by AKT2 regulates SLC2A4/GLUT4 translocation into the plasma membrane. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Cell membrane {ECO:0000250}. Cell projection, ruffle {ECO:0000250}. Note=Dynamically associated with GLUT4-containing glucose storage vesicles (GSV) and plasma membrane in response to insulin stimulation. {ECO:0000250}. DOMAIN: The C2 domain binds to calcium and membrane lipids. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in liver, muscle and fat. +Q8K1A6 C2D1A_MOUSE Coiled-coil and C2 domain-containing protein 1A (Five prime repressor element under dual repression-binding protein 1) (FRE under dual repression-binding protein 1) (Freud-1) 943 103,698 Chain (1); Coiled coil (2); Compositional bias (1); Domain (1); Erroneous initiation (2); Frameshift (1); Modified residue (3); Sequence conflict (2) FUNCTION: Transcription factor that binds specifically to the DRE (dual repressor element) and represses HTR1A gene transcription in neuronal cells. The combination of calcium and ATP specifically inactivates the binding with FRE. May play a role in the altered regulation of HTR1A associated with anxiety and major depression. Mediates HDAC-independent repression of HTR1A promoter in neuronal cell. Performs essential function in controlling functional maturation of synapses. {ECO:0000269|PubMed:12917378, ECO:0000269|PubMed:14756806, ECO:0000269|PubMed:21273312}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6P1N0}. Nucleus {ECO:0000250|UniProtKB:Q66HA5}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q6P1N0}. DOMAIN: The C2 domain is required for the repression. TISSUE SPECIFICITY: Highly expressed in brain, expression is enriched in the gray matter and strongest in the olfactory bulb. {ECO:0000269|PubMed:16033914, ECO:0000269|PubMed:21273312}. +Q9ESN4 C1QL3_MOUSE Complement C1q-like protein 3 (C1q and tumor necrosis factor-related protein 13) (C1q/TNF-related protein 13) (CTRP13) (Gliacolin) 255 26,687 Beta strand (12); Chain (1); Domain (2); Mutagenesis (4); Signal peptide (1); Turn (1) FUNCTION: May regulate the number of excitatory synapses that are formed on hippocampus neurons. Has no effect on inhibitory synapses. Plays a role in glucose homeostasis. Via AMPK signaling pathway, stimulates glucose uptake in adipocytes, myotubes and hepatocytes and enhances insulin-stimulated glucose uptake. In a hepatoma cell line, reduces the expression of gluconeogenic enzymes G6PC and PCK1 and hence decreases de novo glucose production. {ECO:0000269|PubMed:21262840, ECO:0000269|PubMed:21378161}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21378161}. SUBUNIT: Forms homooligomers. Interacts with ADGRB3 (PubMed:21262840). Forms heterooligomers with C1QL2 and C1QL4, when proteins are coexpressed; this interaction does not occur after secretion. {ECO:0000269|PubMed:21262840, ECO:0000269|PubMed:21378161, ECO:0000269|PubMed:23449976}. TISSUE SPECIFICITY: Highly expressed in brain and white adipose tissue. In gonadal fat pad, expressed at lower levels in adipocytes than in the stromal vascular fraction (VSP), which contains preadipocytes, fibroblasts, endothelial cells and occasional immune cells. Expression exhibits sexually dimorphism, with higher levels in females than in males (at protein level). Tends to be up-regulated in adipose tissue from obese males, but not females. Expressed in glial cells. {ECO:0000269|PubMed:21378161}. +P98086 C1QA_MOUSE Complement C1q subcomponent subunit A 245 25,974 Chain (1); Disulfide bond (1); Domain (2); Glycosylation (4); Modified residue (8); Sequence conflict (1); Signal peptide (1) FUNCTION: C1q associates with the proenzymes C1r and C1s to yield C1, the first component of the serum complement system. The collagen-like regions of C1q interact with the Ca(2+)-dependent C1r(2)C1s(2) proenzyme complex, and efficient activation of C1 takes place on interaction of the globular heads of C1q with the Fc regions of IgG or IgM antibody present in immune complexes. PTM: O-linked glycans are Glc-Gal disaccharides typically found as secondary modifications of hydroxylated lysines in collagen-like domains. {ECO:0000250|UniProtKB:P02745}.; PTM: Proline residues in the collagen-like domain motif, GXPG, are typically 4-hydroxylated. {ECO:0000250|UniProtKB:P02745}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: C1 is a calcium-dependent trimolecular complex of C1q, R and S in the molar ration of 1:2:2. C1q subcomponent is composed of nine subunits, six of which are disulfide-linked dimers of the A and B chains, and three of which are disulfide-linked dimers of the C chain. Interacts (via C-terminus) with CD33; this interaction activates CD33 inhibitory motifs. {ECO:0000250|UniProtKB:P02745}. +P12265 BGLR_MOUSE Beta-glucuronidase (EC 3.2.1.31) 648 74,195 Active site (1); Chain (1); Glycosylation (3); Natural variant (5); Sequence conflict (7); Signal peptide (1) FUNCTION: Plays an important role in the degradation of dermatan and keratan sulfates. SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:2394691}. Endoplasmic reticulum {ECO:0000269|PubMed:2394691}. Note=A small proportion is found in the endoplasmic reticulum. SUBUNIT: Homotetramer. +P70444 BID_MOUSE BH3-interacting domain death agonist (p22 BID) (BID) [Cleaved into: BH3-interacting domain death agonist p15 (p15 BID); BH3-interacting domain death agonist p13 (p13 BID); BH3-interacting domain death agonist p11 (p11 BID)] 195 21,952 Beta strand (3); Chain (4); Helix (8); Modified residue (2); Motif (1); Mutagenesis (1); Sequence conflict (1); Site (3) FUNCTION: Induces caspases and apoptosis. Counters the protective effect of Bcl-2. The major proteolytic product p15 BID allows the release of cytochrome c. {ECO:0000269|PubMed:9873064}. PTM: TNF-alpha induces a caspase-mediated cleavage of p22 BID into a major p15 and minor p13 and p11 products. {ECO:0000269|PubMed:9873064}.; PTM: p15 BID is ubiquitinated by ITCH; ubiquitination results in proteasome-dependent degradation. {ECO:0000269|PubMed:20392206}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9873064}. Mitochondrion membrane {ECO:0000269|PubMed:9873064}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:P55957}. Note=When uncleaved, it is predominantly cytoplasmic. {ECO:0000269|PubMed:9873064}.; SUBCELLULAR LOCATION: BH3-interacting domain death agonist p15: Mitochondrion membrane {ECO:0000269|PubMed:9873064}. Note=Translocates to mitochondria as an integral membrane protein. {ECO:0000269|PubMed:9873064}.; SUBCELLULAR LOCATION: BH3-interacting domain death agonist p13: Mitochondrion membrane {ECO:0000269|PubMed:9873064}. Note=Associated with the mitochondrial membrane. {ECO:0000269|PubMed:9873064}. SUBUNIT: Forms heterodimers either with the pro-apoptotic protein BAX or the anti-apoptotic protein Bcl-2 (PubMed:21183079). p15 BID interacts with ITCH (PubMed:20392206). Interacts with PLEKHN1 (By similarity). {ECO:0000250|UniProtKB:P55957, ECO:0000269|PubMed:20392206, ECO:0000269|PubMed:21183079}. DOMAIN: Intact BH3 motif is required by BIK, BID, BAK, BAD and BAX for their pro-apoptotic activity and for their interaction with anti-apoptotic members of the Bcl-2 family. Apoptotic members of the Bcl-2 family. +Q61125 BKRB1_MOUSE B1 bradykinin receptor (B1R) (BK-1 receptor) 334 37,886 Chain (1); Disulfide bond (1); Glycosylation (3); Sequence conflict (4); Topological domain (8); Transmembrane (7) TRANSMEM 42 62 Helical; Name=1. {ECO:0000255}.; TRANSMEM 81 101 Helical; Name=2. {ECO:0000255}.; TRANSMEM 119 139 Helical; Name=3. {ECO:0000255}.; TRANSMEM 162 182 Helical; Name=4. {ECO:0000255}.; TRANSMEM 215 235 Helical; Name=5. {ECO:0000255}.; TRANSMEM 259 279 Helical; Name=6. {ECO:0000255}.; TRANSMEM 303 323 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 41 Extracellular. {ECO:0000255}.; TOPO_DOM 63 80 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 102 118 Extracellular. {ECO:0000255}.; TOPO_DOM 140 161 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 183 214 Extracellular. {ECO:0000255}.; TOPO_DOM 236 258 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 280 302 Extracellular. {ECO:0000255}.; TOPO_DOM 324 334 Cytoplasmic. {ECO:0000255}. FUNCTION: This is a receptor for bradykinin. Could be a factor in chronic pain and inflammation. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed in heart, liver and lung. +Q9R0C0 BL1S6_MOUSE Biogenesis of lysosome-related organelles complex 1 subunit 6 (BLOC-1 subunit 6) (Pallid protein) (Pallidin) (Syntaxin 13-interacting protein) 172 19,682 Alternative sequence (2); Chain (1); Coiled coil (1); Natural variant (2) FUNCTION: Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. May play a role in intracellular vesicle trafficking, particularly in the vesicle-docking and fusion process. {ECO:0000269|PubMed:16760431, ECO:0000269|PubMed:17182842, ECO:0000269|PubMed:19546860, ECO:0000269|PubMed:21998198}. PTM: Phosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UL45}. Membrane {ECO:0000250|UniProtKB:Q9UL45}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9UL45}. Note=It can exist as a soluble protein as well as a peripheral membrane protein. {ECO:0000250|UniProtKB:Q9UL45}. SUBUNIT: Octamer composed of one copy each BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. Interacts with SNAP47 (By similarity). Homodimer. Component of the biogenesis of lysosome-related organelles complex 1 (BLOC-1) composed of BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. Interacts with BLOC1S4, BLOC1S5, DTNBP1/BLOC1S7, F-actin, SNAP25 isoform 1 and STX12. {ECO:0000250, ECO:0000269|PubMed:10610180, ECO:0000269|PubMed:12019270, ECO:0000269|PubMed:12576321, ECO:0000269|PubMed:12923531, ECO:0000269|PubMed:17182842, ECO:0000269|PubMed:19546860}. TISSUE SPECIFICITY: Expressed in liver, kidney and spleen (at protein level). Ubiquitously expressed, with the highest expression levels observed in brain, heart, liver and kidney. {ECO:0000269|PubMed:10610180, ECO:0000269|PubMed:12019270, ECO:0000269|PubMed:12191018}. DISEASE: Note=Defects in Pldn are the cause of the pallid (pa) phenotype that is characterized by an altered formation or function of intracellular storage granules in melanocytes, platelets, and lysosomes in kidney. Pallid mice have a prolonged bleeding time owing to the inability of immature platelet dense granules to accumulate normal amounts of ATP, ADP, and serotonin. Pa animals also suffer from pigment dilution, kidney lysosomal enzyme elevation and serum alpha1-antitrypsin activity deficiency. Finally, pallid mice exhibit defects in otolith formation that lead to balance abnormalities. {ECO:0000269|PubMed:10610180}. +P23359 BMP7_MOUSE Bone morphogenetic protein 7 (BMP-7) (Osteogenic protein 1) (OP-1) 430 49,199 Chain (1); Disulfide bond (4); Glycosylation (4); Propeptide (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Induces cartilage and bone formation. May be the osteoinductive factor responsible for the phenomenon of epithelial osteogenesis. Plays a role in calcium regulation and bone homeostasis. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Homodimer; disulfide-linked. Interacts with SOSTDC1 (PubMed:14623234). Interacts with TWSG1 (PubMed:15843411). Interacts with FBN1 (via N-terminal domain) and FBN2 (By similarity). {ECO:0000250|UniProtKB:P18075, ECO:0000269|PubMed:14623234, ECO:0000269|PubMed:15843411}. +P97504 BMX_MOUSE Cytoplasmic tyrosine-protein kinase BMX (EC 2.7.10.2) (Bone marrow tyrosine kinase gene in chromosome X protein homolog) 651 75,001 Active site (1); Binding site (1); Chain (1); Domain (3); Metal binding (4); Modified residue (1); Nucleotide binding (1); Zinc finger (1) FUNCTION: Non-receptor tyrosine kinase that plays central but diverse modulatory roles in various signaling processes involved in the regulation of actin reorganization, cell migration, cell proliferation and survival, cell adhesion, and apoptosis. Participates in signal transduction stimulated by growth factor receptors, cytokine receptors, G-protein coupled receptors, antigen receptors and integrins. Induces tyrosine phosphorylation of BCAR1 in response to integrin regulation. Activation of BMX by integrins is mediated by PTK2/FAK1, a key mediator of integrin signaling events leading to the regulation of actin cytoskeleton and cell motility. Plays a critical role in TNF-induced angiogenesis, and implicated in the signaling of TEK and FLT1 receptors, 2 important receptor families essential for angiogenesis. Required for the phosphorylation and activation of STAT3, a transcription factor involved in cell differentiation. Also involved in interleukin-6 (IL6) induced differentiation. Plays also a role in programming adaptive cytoprotection against extracellular stress in different cell systems, salivary epithelial cells, brain endothelial cells, and dermal fibroblasts. May be involved in regulation of endocytosis through its interaction with an endosomal protein RUFY1. May also play a role in the growth and differentiation of hematopoietic cells; as well as in signal transduction in endocardial and arterial endothelial cells. {ECO:0000269|PubMed:11416142}. PTM: Phosphorylated in response to protein I/II and to LPS. Phosphorylation at Tyr-542 by SRC and by autocatalysis leads to activation and is required for STAT3 phosphorylation by BMX. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Localizes to the edges of spreading cells when complexed with BCAR1. {ECO:0000250}. SUBUNIT: Interacts with BCAR1, CAV1, MYD88, PTK2/FAK1, RUFY1, RUFY2, STAT3, TIRAP and TNFRSF1B. {ECO:0000250}. DOMAIN: SH2 domain mediates interaction with RUFY1. {ECO:0000250}. TISSUE SPECIFICITY: Specifically expressed in the endocardium of the developing heart as well as in the endocardium of the left ventricle and in the endothelium of large arteries in adult mice. {ECO:0000269|PubMed:9323053}. +Q9Z0L4 BMP15_MOUSE Bone morphogenetic protein 15 (BMP-15) (Growth/differentiation factor 9B) (GDF-9B) 392 44,898 Chain (1); Disulfide bond (3); Glycosylation (5); Propeptide (1); Signal peptide (1) FUNCTION: May be involved in follicular development. Oocyte-specific growth/differentiation factor that stimulates folliculogenesis and granulosa cell (GC) growth (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Homodimer (By similarity). But, in contrast to other members of this family, cannot be disulfide-linked. {ECO:0000250}. TISSUE SPECIFICITY: Ovary specific. +O35914 BNC1_MOUSE Zinc finger protein basonuclin-1 961 106,659 Chain (1); Compositional bias (1); Modified residue (2); Motif (1); Region (1); Sequence conflict (2); Zinc finger (6) FUNCTION: Transcriptional activator (PubMed:9687312, PubMed:23707421). Likely specific for squamous epithelium and for the constituent keratinocytes at a stage either prior to or at the very beginning of terminal differentiation (By similarity). Required for the maintenance of spermatogenesis (PubMed:22266914). May also play a role in the differentiation of oocytes and the early development of embryos (PubMed:9687312). {ECO:0000250|UniProtKB:Q01954, ECO:0000269|PubMed:22266914, ECO:0000269|PubMed:23707421, ECO:0000269|PubMed:9687312}. PTM: Phosphorylation on Ser-505 and Ser-509 leads to cytoplasmic localization. {ECO:0000250|UniProtKB:Q01954}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23707421, ECO:0000269|PubMed:9687312}. Cytoplasm {ECO:0000269|PubMed:23707421, ECO:0000269|PubMed:9687312}. Nucleus, nucleoplasm {ECO:0000269|PubMed:23707421}. Note=Relocates to the midpiece of the flagellum during late spermiogenesis in spermatids. {ECO:0000269|PubMed:9687312}. SUBUNIT: Interacts with HSF2BP (via C-terminus). {ECO:0000269|PubMed:23707421}. TISSUE SPECIFICITY: Epidermis and germ cells of testis and ovary. {ECO:0000269|PubMed:9687312}. +Q91ZE9 BMF_MOUSE Bcl-2-modifying factor 185 20,682 Chain (1); Erroneous initiation (1); Helix (1); Motif (1); Mutagenesis (4); Region (1) FUNCTION: May play a role in apoptosis. SUBUNIT: Interacts with MCL1, BCL2, BCL2L1/BCL-Xl, BCL2A1 and BCL2L2/BCL-w. Interacts with the myosin V actin motor complex through its binding to DLC2. {ECO:0000269|PubMed:11546872, ECO:0000269|PubMed:18462686}. TISSUE SPECIFICITY: Widely expressed with an abundant expression in pancreas, liver kidney and hematopoietic tissues. {ECO:0000269|PubMed:14574334}. +P97452 BOP1_MOUSE Ribosome biogenesis protein BOP1 (Block of proliferation 1 protein) 732 82,546 Chain (1); Erroneous initiation (1); Modified residue (3); Region (1); Repeat (7); Sequence conflict (3) FUNCTION: Component of the PeBoW complex, which is required for maturation of 28S and 5.8S ribosomal RNAs and formation of the 60S ribosome. {ECO:0000255|HAMAP-Rule:MF_03027, ECO:0000269|PubMed:10891491, ECO:0000269|PubMed:11390653, ECO:0000269|PubMed:12048210}. SUBCELLULAR LOCATION: Nucleus, nucleolus. Nucleus, nucleoplasm. SUBUNIT: Component of the PeBoW complex, composed of BOP1, PES1 and WDR12 (PubMed:15225545, ECO:0000269|PubMed:17353269). The complex is held together by BOP1, which interacts with PES1 via its N-terminal domain and with WDR12 via a high-affinity interaction between the seven-bladed beta-propeller domains of the 2 proteins. The NOP7 complex associates with the 66S pre-ribosome. The PeBoW complex associates with DDX27, BOP1 interacts directly with DDX27 (By similarity). {ECO:0000255|HAMAP-Rule:MF_03027, ECO:0000269|PubMed:15225545, ECO:0000269|PubMed:17353269}. TISSUE SPECIFICITY: Expressed in brain, gut, heart, kidney, liver, lung, muscle, ovary, skin, spleen and testis. +O88737 BSN_MOUSE Protein bassoon 3942 418,843 Alternative sequence (1); Chain (1); Coiled coil (2); Compositional bias (3); Glycosylation (8); Initiator methionine (1); Lipidation (1); Modified residue (39); Region (2); Repeat (5); Sequence conflict (10); Zinc finger (4) FUNCTION: Is thought to be involved in the organization of the cytomatrix at the nerve terminals active zone (CAZ) which regulates neurotransmitter release (PubMed:12628169). Seems to act through binding to ERC2/CAST1 (By similarity). Essential in regulated neurotransmitter release from a subset of brain glutamatergic synapses (PubMed:12628169). Involved in the formation of the retinal photoreceptor ribbon synapses (PubMed:12628168). {ECO:0000250|UniProtKB:O88778, ECO:0000269|PubMed:12628168, ECO:0000269|PubMed:12628169}. PTM: Myristoylated. The N-terminal myristoylation is not sufficient for presynaptic localization (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O88778}. Cell junction, synapse, synaptosome {ECO:0000269|PubMed:12628169}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O88778}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:12628169}; Peripheral membrane protein {ECO:0000250|UniProtKB:O88778}. Note=Localized to the active zone of presynaptic density (PubMed:12628169, PubMed:12628168). In retina, is localized in the outer plexiform layer at ribbon synapses formed by rods and cones but was absent from basal synaptic contacts formed by cones. In the retinal inner plexiform layer localized to conventional inhibitory GABAergic synapses, made by amacrine cells, but absent from the bipolar cell ribbon synapses (By similarity). {ECO:0000250|UniProtKB:O88778, ECO:0000269|PubMed:12628168, ECO:0000269|PubMed:12628169}. SUBUNIT: Interacts with ERC2/CAST1, RIMS1 and UNC13A. Part of a complex consisting of ERC2, RIMS1 and BSN (By similarity). Interacts with TPRG1L (PubMed:17869247). {ECO:0000250|UniProtKB:O88778, ECO:0000269|PubMed:17869247}. TISSUE SPECIFICITY: Expressed in brain and retina. {ECO:0000269|PubMed:12628168, ECO:0000269|PubMed:12628169}. +O70552 BTG4_MOUSE Protein BTG4 (BTG family member 4) (Protein PC3b) 250 28,613 Chain (1); Sequence conflict (2) FUNCTION: Shows marked antiproliferative activity, being able to induce G(1) arrest. TISSUE SPECIFICITY: Highly expressed in testis and in olfactory epithelium. +Q80X66 BTBDA_MOUSE BTB/POZ domain-containing protein 10 (Glucose metabolism-related protein 1) 475 53,772 Chain (1); Compositional bias (1); Domain (1); Region (1) FUNCTION: Plays a major role as an activator of AKT family members by inhibiting PPP2CA-mediated dephosphorylation, thereby keeping AKTs activated. Plays a role in preventing motor neuronal death and in accelerating the growth of pancreatic beta cells. {ECO:0000269|PubMed:18160256, ECO:0000269|PubMed:21267538}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BSF8}. Cytoplasm {ECO:0000269|PubMed:18160256}. Note=Colocalizes with KCTD20 in filamentous structures. {ECO:0000269|PubMed:24156551}. SUBUNIT: Interacts (via C-terminal 330-amino-acid region) with AKT1; AKT2 and AKT3 (PubMed:18160256). Interacts with PPP2CA and PPP1CA (PubMed:18160256). {ECO:0000269|PubMed:18160256}. TISSUE SPECIFICITY: Ubiquitously expressed (at protein level). {ECO:0000269|PubMed:18160256}. +Q9DB72 BTBDH_MOUSE BTB/POZ domain-containing protein 17 (Galectin-3-binding protein-like) 478 52,602 Chain (1); Domain (2); Glycosylation (4); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +O08901 BUB1_MOUSE Mitotic checkpoint serine/threonine-protein kinase BUB1 (mBUB1) (EC 2.7.11.1) (BUB1A) 1058 119,563 Active site (1); Binding site (1); Chain (1); Domain (2); Erroneous initiation (1); Modified residue (9); Motif (3); Nucleotide binding (1); Region (4); Sequence conflict (1) FUNCTION: Serine/threonine-protein kinase that performs 2 crucial functions during mitosis: it is essential for spindle-assembly checkpoint signaling and for correct chromosome alignment. Has a key role in the assembly of checkpoint proteins at the kinetochore, being required for the subsequent localization of CENPF, BUB1B, CENPE and MAD2L1. Required for the kinetochore localization of PLK1. Required for centromeric enrichment of AUKRB in prometaphase. Plays an important role in defining SGO1 localization and thereby affects sister chromatid cohesion. Acts as a substrate for anaphase-promoting complex or cyclosome (APC/C) in complex with its activator CDH1 (APC/C-Cdh1). Necessary for ensuring proper chromosome segregation and binding to BUB3 is essential for this function. Can regulate chromosome segregation in a kinetochore-independent manner. Can phosphorylate BUB3. The BUB1-BUB3 complex plays a role in the inhibition of APC/C when spindle-assembly checkpoint is activated and inhibits the ubiquitin ligase activity of APC/C by phosphorylating its activator CDC20. This complex can also phosphorylate MAD1L1. Kinase activity is essential for inhibition of APC/CCDC20 and for chromosome alignment but does not play a major role in the spindle-assembly checkpoint activity. Mediates cell death in response to chromosome missegregation and acts to suppress spontaneous tumorigenesis. Essential during early and later stages of embryonic development. Necessary for postimplantation embryogenesis and proliferation of primary embryonic fibroblasts and plays an important role in spermatogenesis and fertility. {ECO:0000250|UniProtKB:O43683, ECO:0000269|PubMed:17925231, ECO:0000269|PubMed:17938250, ECO:0000269|PubMed:19772675}. PTM: Upon spindle-assembly checkpoint activation it is hyperphosphorylated and its kinase activity toward CDC20 is stimulated. Phosphorylation at Thr-595 is required for interaction with PLK1, phosphorylation at this site probably creates a binding site for the POLO-box domain of PLK1, thus enhancing the PLK1-BUB1 interaction (By similarity). {ECO:0000250}.; PTM: Ubiquitinated and degraded during mitotic exit by APC/C-Cdh1. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere, kinetochore. Note=Nuclear in interphase cells. Accumulates gradually during G1 and S phase of the cell cycle, peaks at G2/M, and drops dramatically after mitosis. Localizes to the outer kinetochore. Kinetochore localization is required for normal mitotic timing and checkpoint response to spindle damage and occurs very early in prophase. AURKB, KNL1 and INCENP are required for kinetochore localization (By similarity). {ECO:0000250}. SUBUNIT: Interacts with BUB3 and KNL1. Interacts (when phosphorylated) with PLK1. The BUB1-BUB3 complex interacts with MAD1L1 (By similarity). {ECO:0000250}. DOMAIN: The KEN box is required for its ubiquitination and degradation. {ECO:0000250}.; DOMAIN: BUB1 N-terminal domain directs kinetochore localization and binding to BUB3. TISSUE SPECIFICITY: Highly expressed in testis. Weakly expressed in spleen and lung. {ECO:0000269|PubMed:17925231}. +Q91WS4 BHMT2_MOUSE S-methylmethionine--homocysteine S-methyltransferase BHMT2 (SMM-hcy methyltransferase) (EC 2.1.1.10) (Betaine--homocysteine S-methyltransferase 2) 363 39,872 Chain (1); Domain (1); Metal binding (3); Modified residue (1); Sequence conflict (4) Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (BhmT route): step 1/1. FUNCTION: Involved in the regulation of homocysteine metabolism. Converts homocysteine to methionine using S-methylmethionine (SMM) as a methyl donor. {ECO:0000269|PubMed:18230605}. SUBUNIT: Homotetramer. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in fetal heart, lung, liver, kidney and eye. {ECO:0000269|PubMed:11087663}. +Q8BR07 BICD1_MOUSE Protein bicaudal D homolog 1 (Bic-D 1) 835 95,896 Alternative sequence (4); Chain (1); Coiled coil (3); Helix (3); Region (1); Sequence conflict (8) FUNCTION: Regulates coat complex coatomer protein I (COPI)-independent Golgi-endoplasmic reticulum transport by recruiting the dynein-dynactin motor complex. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|Ref.4}. SUBUNIT: Interacts with RAB6A. Interacts (via C-terminus) with RAB6B (GTP-bound); the interaction is direct (By similarity). Interacts with CLIP-115 and KIFC2. {ECO:0000250, ECO:0000269|Ref.4}. TISSUE SPECIFICITY: Expressed in the brain, heart and skeletal muscle. +Q8R015 BL1S5_MOUSE Biogenesis of lysosome-related organelles complex 1 subunit 5 (BLOC-1 subunit 5) (Protein Muted homolog) 185 21,283 Alternative sequence (1); Chain (1); Initiator methionine (1); Modified residue (1) FUNCTION: Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. Plays a role in intracellular vesicle trafficking. {ECO:0000269|PubMed:11912185, ECO:0000269|PubMed:12019270, ECO:0000269|PubMed:16760431, ECO:0000269|PubMed:19546860, ECO:0000269|PubMed:21998198}. SUBUNIT: Octamer composed of one copy each BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8 (By similarity). Component of the biogenesis of lysosome-related organelles complex 1 (BLOC-1) composed of BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. The BLOC-1 complex associates with the AP-3 protein complex and membrane protein cargos. Interacts with BLOC1S4, BLOC1S6, DTNBP1/BLOC1S7 and PI4K2A. {ECO:0000250, ECO:0000269|PubMed:12019270, ECO:0000269|PubMed:12576321, ECO:0000269|PubMed:12923531, ECO:0000269|PubMed:21998198}. TISSUE SPECIFICITY: Detected in heart, brain, spleen, lung, kidney and testis. {ECO:0000269|PubMed:11912185}. DISEASE: Note=Defects in Muted are the cause of the Muted (mu) mutant, which is characterized by light eyes at birth, hypopigmentation of the coat, platelet storage pool deficiency and lysosomal hyposecretion. {ECO:0000269|PubMed:11912185}. +Q9QWK5 BIR1A_MOUSE Baculoviral IAP repeat-containing protein 1a (Neuronal apoptosis inhibitory protein 1) 1403 158,724 Binding site (1); Chain (1); Domain (1); Metal binding (4); Repeat (3); Sequence conflict (12) FUNCTION: Anti-apoptotic protein which acts by inhibiting the activities of CASP3, CASP7 and CASP9. Can inhibit the autocleavage of pro-CASP9 and cleavage of pro-CASP3 by CASP9. Capable of inhibiting CASP9 autoproteolysis at 'Asp-315' and decreasing the rate of auto proteolysis at 'Asp-330'. Acts as a mediator of neuronal survival in pathological conditions. Prevents motor-neuron apoptosis induced by a variety of signals (By similarity). {ECO:0000250}. SUBUNIT: Interacts (via NACHT domain) with APAF1 (via CARD and NACHT domains). {ECO:0000250}. DOMAIN: Both the BIR and NACHT domains are essential for effective inhibition of pro-CASP9 cleavage. BIR3 domain binds to procaspase-9 and the NACHT domain interacts with the NACHT domain of APAF1 forming a bridge between pro-CASP9 and APAF1 (By similarity). {ECO:0000250}. +Q5SQY2 BOD1_MOUSE Biorientation of chromosomes in cell division protein 1 (Biorientation defective protein 1) (Protein FAM44B) 173 18,364 Chain (1) FUNCTION: Required for proper chromosome biorientation through the detection or correction of syntelic attachments in mitotic spindles. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Note=Localizes at the centrosomes throughout the cell cycle, only dissociating during cytokinesis. Localizes at the kinetochore from prometaphase until anaphase. {ECO:0000250}. +Q91Z96 BMP2K_MOUSE BMP-2-inducible protein kinase (BIKe) (EC 2.7.11.1) 1138 126,185 Active site (1); Alternative sequence (2); Binding site (1); Chain (1); Compositional bias (1); Domain (1); Modified residue (14); Nucleotide binding (1) FUNCTION: May be involved in osteoblast differentiation. PTM: Autophosphorylated. SUBCELLULAR LOCATION: Nucleus. TISSUE SPECIFICITY: Expressed in spleen, kidney, lung, brain, heart, diaphragm and calvaria but not in liver. +P36895 BMR1A_MOUSE Bone morphogenetic protein receptor type-1A (BMP type-1A receptor) (BMPR-1A) (EC 2.7.11.30) (Activin receptor-like kinase 3) (ALK-3) (BMP-2/BMP-4 receptor) (Serine/threonine-protein kinase receptor R5) (SKR5) (CD antigen CD292) 532 60,063 Active site (1); Binding site (1); Chain (1); Disulfide bond (5); Domain (2); Glycosylation (1); Mutagenesis (3); Nucleotide binding (1); Region (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 153 176 Helical. {ECO:0000255}. TOPO_DOM 24 152 Extracellular. {ECO:0000255}.; TOPO_DOM 177 532 Cytoplasmic. {ECO:0000255}. FUNCTION: On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for BMP2, BMP4, GDF5 and GDF6. Positively regulates chondrocyte differentiation through GDF5 interaction (PubMed:24098149). Mediates induction of adipogenesis by GDF6 (PubMed:23527555). {ECO:0000269|PubMed:23527555, ECO:0000269|PubMed:24098149}. PTM: Glycosylated. {ECO:0000269|PubMed:29415997}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P36898}; Single-pass type I membrane protein {ECO:0000255}. Cell surface {ECO:0000269|PubMed:29415997}. SUBUNIT: Interacts with low affinity with GDF5; positively regulates chondrocyte differentiation. {ECO:0000250|UniProtKB:P36894}. TISSUE SPECIFICITY: Widely expressed. +Q2VPD4 BMAL2_MOUSE Aryl hydrocarbon receptor nuclear translocator-like protein 2 (Brain and muscle ARNT-like 2) 579 64,399 Alternative sequence (2); Chain (1); Cross-link (2); Domain (4); Motif (3); Region (1); Sequence conflict (24) FUNCTION: Transcriptional activator which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, ARNTL/BMAL1, ARNTL2/BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and ARNTL/BMAL1 or ARNTL2/BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-ARNTL/BMAL1|ARNTL2/BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress ARNTL/BMAL1 transcription, respectively. The CLOCK-ARNTL2/BMAL2 heterodimer activates the transcription of SERPINE1/PAI1 and BHLHE40/DEC1. {ECO:0000269|PubMed:19605937, ECO:0000269|PubMed:20153195}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}. SUBUNIT: Component of the circadian core oscillator, which includes the CRY proteins, CLOCK, or NPAS2, ARNTL/BMAL1 or ARNTL2/BMAL2, CSNK1D and/or CSNK1E, TIMELESS and the PER proteins. Interacts directly with CLOCK to form the ARNTL2/BMAL2-CLOCK transactivator. Can form heterodimers or homodimers which interact directly with CLOCK to form the transcription activator. Interacts with NPAS2 and HIF1A (By similarity). Interacts with PER2. {ECO:0000250|UniProtKB:Q8WYA1, ECO:0000269|PubMed:19605937}. TISSUE SPECIFICITY: Expressed in the suprachiasmatic nucleus (SCN). +Q9CQC5 BORG2_MOUSE Cdc42 effector protein 3 (Binder of Rho GTPases 2) 254 27,686 Chain (1); Compositional bias (1); Domain (1); Frameshift (1); Modified residue (4) FUNCTION: Probably involved in the organization of the actin cytoskeleton. May act downstream of CDC42 to induce actin filament assembly leading to cell shape changes. Induces pseudopodia formation in fibroblasts (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. SUBUNIT: Interacts with RHOQ and CDC42, in a GTP-dependent manner, and with SEPT7. {ECO:0000250}. +O55003 BNIP3_MOUSE BCL2/adenovirus E1B 19 kDa protein-interacting protein 3 187 20,978 Chain (1); Modified residue (6); Motif (1); Transmembrane (1) TRANSMEM 157 177 Helical. {ECO:0000255}. FUNCTION: Apoptosis-inducing protein that can overcome BCL2 suppression. May play a role in repartitioning calcium between the two major intracellular calcium stores in association with BCL2 (By similarity). Involved in mitochondrial quality control via its interaction with SPATA18/MIEAP: in response to mitochondrial damage, participates in mitochondrial protein catabolic process (also named MALM) leading to the degradation of damaged proteins inside mitochondria. The physical interaction of SPATA18/MIEAP, BNIP3 and BNIP3L/NIX at the mitochondrial outer membrane may play a critical role in the translocation of lysosomal proteins from the cytoplasm to the mitochondrial matrix (By similarity). The physical interaction of SPATA18/MIEAP, BNIP3 and BNIP3L/NIX at the mitochondrial outer membrane regulates the opening of a pore in the mitochondrial double membrane in order to mediate the translocation of lysosomal proteins from the cytoplasm to the mitochondrial matrix (By similarity). Plays an important role in the calprotectin (S100A8/A9)-induced cell death pathway (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion outer membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=Coexpression with the EIB 19-kDa protein results in a shift in NIP3 localization pattern to the nuclear envelope. Colocalizes with ACAA2 in the mitochondria. Colocalizes with SPATA18 at the mitochondrion outer membrane (By similarity). {ECO:0000250}. SUBUNIT: Homodimer. Binds to BCL2. Interacts with BNIP3L and ACAA2. Interacts (via BH3 domain) with SPATA18 (via coiled-coil domains). Interacts with BOK; promotes BOK oligomerization. {ECO:0000250|UniProtKB:Q12983}. +A2BGH0 BPIB4_MOUSE BPI fold-containing family B member 4 (Long palate, lung and nasal epithelium carcinoma-associated protein 4) 617 65,723 Alternative sequence (2); Chain (1); Compositional bias (1); Disulfide bond (1); Glycosylation (1); Signal peptide (1) FUNCTION: May have the capacity to recognize and bind specific classes of odorants. May act as a carrier molecule, transporting odorants across the mucus layer to access receptor sites. May serve as a primary defense mechanism by recognizing and removing potentially harmful odorants or pathogenic microorganisms from the mucosa or clearing excess odorant from mucus to enable new odorant stimuli to be received (By similarity). {ECO:0000250|UniProtKB:Q05701}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P59827}. Cytoplasm {ECO:0000250|UniProtKB:P59827}. +Q9JM96 BORG4_MOUSE Cdc42 effector protein 4 (Binder of Rho GTPases 4) 349 37,869 Chain (1); Domain (1); Modified residue (14); Sequence conflict (1) FUNCTION: Probably involved in the organization of the actin cytoskeleton. May act downstream of CDC42 to induce actin filament assembly leading to cell shape changes. Induces pseudopodia formation, when overexpressed in fibroblasts. SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. SUBUNIT: Interacts with CDC42 and RHOQ, in a GTP-dependent manner. {ECO:0000269|PubMed:10490598}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11185749}. +P21275 BMP4_MOUSE Bone morphogenetic protein 4 (BMP-4) (Bone morphogenetic protein 2B) (BMP-2B) 408 46,497 Chain (1); Disulfide bond (4); Erroneous initiation (1); Glycosylation (4); Modified residue (1); Propeptide (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Induces cartilage and bone formation. Acts in concert with PTHLH/PTHRP to stimulate ductal outgrowth during embryonic mammary development and to inhibit hair follicle induction. {ECO:0000269|PubMed:14973287, ECO:0000269|PubMed:15206957, ECO:0000269|PubMed:17301089}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SUBUNIT: Homodimer; disulfide-linked (By similarity). Interacts with SOSTDC1, GREM2, RGMA, RGMB and RGMC. Part of a complex consisting of TWSG1 and CHRD. Interacts with the serine proteases, HTRA1 and HTRA3; the interaction with either inhibits BMP4-mediated signaling. The HTRA protease activity is required for this inhibition. Interacts with FBN1 (via N-terminal domain) and FBN2 (By similarity). {ECO:0000250|UniProtKB:P12644, ECO:0000269|PubMed:11260715, ECO:0000269|PubMed:14623234, ECO:0000269|PubMed:14973287, ECO:0000269|PubMed:15039429, ECO:0000269|PubMed:15206957, ECO:0000269|PubMed:15671031, ECO:0000269|PubMed:15975920, ECO:0000269|PubMed:16604073, ECO:0000269|PubMed:17472960}. +Q920N2 BPL1_MOUSE Biotin--protein ligase (EC 6.3.4.-) (Biotin apo-protein ligase) [Includes: Biotin--[methylmalonyl-CoA-carboxytransferase] ligase (EC 6.3.4.9); Biotin--[propionyl-CoA-carboxylase [ATP-hydrolyzing]] ligase (EC 6.3.4.10) (Holocarboxylase synthetase) (HCS); Biotin--[methylcrotonoyl-CoA-carboxylase] ligase (EC 6.3.4.11); Biotin--[acetyl-CoA-carboxylase] ligase (EC 6.3.4.15)] 722 78,516 Chain (1); Domain (1); Modified residue (1) FUNCTION: Post-translational modification of specific protein by attachment of biotin. Acts on various carboxylases such as acetyl-CoA-carboxylase, pyruvate carboxylase, propionyl CoA carboxylase, and 3-methylcrotonyl CoA carboxylase (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Mitochondrion {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. +P07743 BPIA2_MOUSE BPI fold-containing family A member 2 (Parotid secretory protein) (PSP) 235 24,753 Chain (1); Disulfide bond (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Has strong antibacterial activity against P. aeruginosa. {ECO:0000250|UniProtKB:Q96DR5}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9461541}. TISSUE SPECIFICITY: Predominates in the parotid glands, present in smaller amounts (1/10) in the submaxillary glands and in the sublingual glands, and at lower amount in the pancreas but undetectable in the liver. Found also in lacrimal gland. {ECO:0000269|PubMed:9461541}. +Q8C1E1 BPIB2_MOUSE BPI fold-containing family B member 2 (Bactericidal/permeability-increasing protein-like 1) 462 49,521 Chain (1); Disulfide bond (1); Glycosylation (3); Modified residue (2); Sequence conflict (7); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +P20722 BMP6_MOUSE Bone morphogenetic protein 6 (BMP-6) (VG-1-related protein) (VGR-1) 510 56,432 Chain (1); Disulfide bond (4); Glycosylation (5); Propeptide (1); Sequence conflict (3); Signal peptide (1) FUNCTION: Induces cartilage and bone formation. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Interacts with SOSTDC1. {ECO:0000269|PubMed:14623234}. TISSUE SPECIFICITY: Expressed in the lung. Low levels seen in the kidney. +Q91Y44 BRDT_MOUSE Bromodomain testis-specific protein (Bromodomain-containing female sterile homeotic-like protein) (RING3-like protein) 956 107,255 Alternative sequence (2); Beta strand (1); Binding site (3); Chain (1); Coiled coil (2); Compositional bias (3); Domain (3); Helix (16); Modified residue (1); Motif (1); Mutagenesis (4); Sequence conflict (2); Turn (1) FUNCTION: Testis-specific chromatin protein that specifically binds histone H4 acetylated at 'Lys-5' and 'Lys-8' (H4K5ac and H4K8ac, respectively) and plays a key role in spermatogenesis (PubMed:12861021, PubMed:19794495, PubMed:22901802, PubMed:22922464). Required in late pachytene spermatocytes: plays a role in meiotic and post-meiotic cells by binding to acetylated histones at the promoter of specific meiotic and post-meiotic genes, facilitating their activation at the appropriate time. In the post-meiotic phase of spermatogenesis, binds to hyperacetylated histones and participates in their general removal from DNA (PubMed:22901802). Also recognizes and binds a subset of butyrylated histones: able to bind histone H4 butyrylated at 'Lys-8' (H4K8ac), while it is not able to bind H4 butyrylated at 'Lys-5' (H4K5ac) (PubMed:27105113). Also acts as a component of the splicing machinery in pachytene spermatocytes and round spermatids and participates in 3'-UTR truncation of specific mRNAs in post-meiotic spermatids (PubMed:22570411). Required for chromocenter organization, a structure comprised of peri-centromeric heterochromatin (PubMed:22020252). {ECO:0000269|PubMed:12861021, ECO:0000269|PubMed:19794495, ECO:0000269|PubMed:22020252, ECO:0000269|PubMed:22570411, ECO:0000269|PubMed:22901802, ECO:0000269|PubMed:22922464, ECO:0000269|PubMed:27105113}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17728347, ECO:0000269|PubMed:19794495, ECO:0000269|PubMed:22020252}. Note=Detected on chromatin (PubMed:19794495). Excluded from the chromocenter. {ECO:0000269|PubMed:19794495, ECO:0000269|PubMed:22020252}. SUBUNIT: Interacts with SMARCE1 (By similarity). Interacts with mRNA splicing machinery proteins SRSF2, DDX5, HNRNPK and TARDBP. Interacts with the acetylated N-terminus of histone H1, H2, H3 and H4. Interacts with P-TEFb components CDK9 and CCNT1/cyclin-T1. {ECO:0000250|UniProtKB:Q58F21, ECO:0000269|PubMed:12861021, ECO:0000269|PubMed:19794495, ECO:0000269|PubMed:22570411, ECO:0000269|PubMed:22922464}. DOMAIN: Bromo domains mediate interaction with histones that have acetylated lysine residues at specific positions. Bromo domain 1 mediates binding with histone H4 acetylated at 'Lys-5' and 'Lys-8' (H4K5ac and H4K8ac, respectively) (PubMed:19794495). The bromo domains also recognize and bind a subset of butyrylated histones: able to bind histone H4 butyrylated at 'Lys-8' (H4K8ac), while it is not able to bind H4 butyrylated at 'Lys-5' (H4K5ac) (PubMed:27105113). {ECO:0000269|PubMed:19794495, ECO:0000269|PubMed:27105113}. TISSUE SPECIFICITY: Testis-specific. Expressed in germinal cells from the early meiotic (pachytene) spermatocytes and during spermiogenesis in the round and elongating spermatids until the condensed late spermatids. No expression seen in spermatogonia. {ECO:0000269|PubMed:15261828, ECO:0000269|PubMed:17049203, ECO:0000269|PubMed:17728347}. +Q5DTM8 BRE1A_MOUSE E3 ubiquitin-protein ligase BRE1A (BRE1-A) (EC 2.3.2.27) (RING finger protein 20) (RING-type E3 ubiquitin transferase BRE1A) 973 113,520 Alternative sequence (1); Chain (1); Coiled coil (3); Erroneous initiation (1); Modified residue (8); Sequence conflict (4); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: Component of the RNF20/40 E3 ubiquitin-protein ligase complex that mediates monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1). H2BK120ub1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation (H3K4me and H3K79me, respectively). It thereby plays a central role in histone code and gene regulation. The RNF20/40 complex forms a H2B ubiquitin ligase complex in cooperation with the E2 enzyme UBE2A or UBE2B; reports about the cooperation with UBE2E1/UBCH are contradictory. Required for transcriptional activation of Hox genes. Recruited to the MDM2 promoter, probably by being recruited by p53/TP53, and thereby acts as a transcriptional coactivator. Mediates the polyubiquitination of PA2G4 leading to its proteasome-mediated degradation. {ECO:0000250|UniProtKB:Q5VTR2}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5VTR2}. SUBUNIT: Component of the RNF20/40 complex (also known as BRE1 complex) probably composed of 2 copies of RNF20/BRE1A and 2 copies of RNF40/BRE1B. Interacts with UBE2E1/UBCH6. Interacts with p53/TP53 and WAC. Interacts with PAF1; the interaction mediates the association of the PAF1 and RNF20/40 complexes which is a prerequsite for recruitment of UBE2A/B. Interacts with PA2G4. {ECO:0000250|UniProtKB:Q5VTR2}. +Q9JK39 BTNLA_MOUSE Butyrophilin-like protein 10 275 29,549 Alternative sequence (1); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (3); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 195 211 Helical. {ECO:0000255}. TOPO_DOM 30 194 Extracellular. {ECO:0000255}.; TOPO_DOM 212 275 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +P97929 BRCA2_MOUSE Breast cancer type 2 susceptibility protein homolog (Fanconi anemia group D1 protein homolog) 3329 370,664 Beta strand (37); Chain (1); Helix (24); Modified residue (6); Motif (1); Natural variant (35); Region (4); Repeat (7); Sequence conflict (1); Turn (11) FUNCTION: Involved in double-strand break repair and/or homologous recombination. Binds RAD51 and potentiates recombinational DNA repair by promoting assembly of RAD51 onto single-stranded DNA (ssDNA). Acts by targeting RAD51 to ssDNA over double-stranded DNA, enabling RAD51 to displace replication protein-A (RPA) from ssDNA and stabilizing RAD51-ssDNA filaments by blocking ATP hydrolysis. Part of a PALB2-scaffolded HR complex containing RAD51C and which is thought to play a role in DNA repair by HR. May participate in S phase checkpoint activation. Binds selectively to ssDNA, and to ssDNA in tailed duplexes and replication fork structures. May play a role in the extension step after strand invasion at replication-dependent DNA double-strand breaks; together with PALB2 is involved in both POLH localization at collapsed replication forks and DNA polymerization activity. In concert with NPM1, regulates centrosome duplication. Interacts with the TREX-2 complex (transcription and export complex 2) subunits PCID2 and SEM1, and is required to prevent R-loop-associated DNA damage and thus transcription-associated genomic instability, independently of its known role in homologous recombination (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P51587}. PTM: Phosphorylation by CHEK1 and CHEK2 regulates interaction with RAD51. Phosphorylation at Ser-3214 by CDK1 and CDK2 is low in S phase when recombination is active, but increases as cells progress towards mitosis; this phosphorylation prevents homologous recombination-dependent repair during S phase and G2 by inhibiting RAD51 binding (By similarity). {ECO:0000250}.; PTM: Ubiquitinated in the absence of DNA damage; this does not lead to proteasomal degradation. In contrast, ubiquitination in response to DNA damage leads to proteasomal degradation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Monomer and dimer. Interacts with RAD51; regulates RAD51 recruitment and function at sites of DNA repair. Interacts with SEM1, WDR16, USP11, DMC1, ROCK2 and NPM1. Interacts with both nonubiquitinated and monoubiquitinated FANCD2; this complex also includes XRCC3 and phosphorylated FANCG. Part of a BRCA complex containing BRCA1, BRCA2 and PALB2. Interacts directly with PALB2 which may serve as a scaffold for a HR complex containing PALB2, BRCA2, RAD51C, RAD51 and XRCC3. Interacts with BRCA1 only in the presence of PALB2 which serves as the bridging protein. Interacts with POLH; the interaction is direct. Interacts with the TREX-2 complex subunits PCID2 and SEM1 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P51587, ECO:0000269|PubMed:12228710}. TISSUE SPECIFICITY: Widely expressed. Highest expression in cerebellum, testis, ileum, appendix, epididymis, ovary and mammary gland. No expression in lung. +Q5U465 CC125_MOUSE Coiled-coil domain-containing protein 125 500 56,655 Alternative sequence (4); Chain (1); Coiled coil (2); Modified residue (1); Sequence conflict (2) FUNCTION: May be involved in the regulation of cell migration. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. TISSUE SPECIFICITY: Expressed in many tissues, with highest levels in spleen, thymus and bone marrow. {ECO:0000269|PubMed:19787194}. +Q8BIS8 CC126_MOUSE Coiled-coil domain-containing protein 126 140 15,590 Alternative sequence (1); Chain (1); Glycosylation (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q3TC33 CC127_MOUSE Coiled-coil domain-containing protein 127 260 30,509 Alternative sequence (2); Chain (1); Coiled coil (1); Sequence conflict (1) +Q9DBY5 CBX6_MOUSE Chromobox protein homolog 6 414 44,460 Chain (1); Domain (1); Modified residue (1); Sequence conflict (1) FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. Possibly contributes to the target selectivity of the PRC1 complex by binding specific regions of chromatin (By similarity). Recruitment to chromatin might occur in an H3K27me3-independent fashion (PubMed:22226355, PubMed:16537902). May have a PRC1-independent function in embryonic stem cells (PubMed:22226355). {ECO:0000250|UniProtKB:O95503, ECO:0000269|PubMed:16537902, ECO:0000269|PubMed:22226355}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16537902}. Chromosome {ECO:0000269|PubMed:16537902}. Note=Localizes to the inactivated X chromosome in females. {ECO:0000269|PubMed:16537902}. SUBUNIT: Component of a PRC1-like complex. Distinct PRC1-like core complexes are composed of a RING1 subunit (RING1B or RING1A), one of the six PCGF proteins (PCGF1-6), one PHC protein (PHC1-3) and one of the CBX proteins (CBX2, CBX4, CBX6, CBX7 or CBX8). Interacts with PCGF1, PCGF2, PCGF3, BMI1, PCGF5, PCGF6, RING1 and RNF2. May interact with HIST2H3A and HIST1H3A (By similarity). Interacts (via chromodomain) with single-stranded RNA (ssRNA) (PubMed:16537902). {ECO:0000250|UniProtKB:O95503, ECO:0000269|PubMed:16537902}. TISSUE SPECIFICITY: Expressed in mouse embryonic stem cells. {ECO:0000269|PubMed:22226355}. +Q8C9S4 CC186_MOUSE Coiled-coil domain-containing protein 186 (Oocyte-testis gene 1 protein) 917 104,901 Chain (1); Coiled coil (3); Compositional bias (1); Modified residue (1); Sequence caution (1) TISSUE SPECIFICITY: Expressed in postnatal germ cells. +Q8VEK0 CC50A_MOUSE Cell cycle control protein 50A (P4-ATPase flippase complex beta subunit TMEM30A) (Transmembrane protein 30A) 364 41,061 Chain (1); Erroneous initiation (1); Frameshift (1); Glycosylation (2); Initiator methionine (1); Modified residue (1); Sequence conflict (2); Topological domain (3); Transmembrane (2) TRANSMEM 50 70 Helical. {ECO:0000255}.; TRANSMEM 329 349 Helical. {ECO:0000255}. TOPO_DOM 2 49 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 71 328 Exoplasmic loop. {ECO:0000255}.; TOPO_DOM 350 364 Cytoplasmic. {ECO:0000255}. FUNCTION: Accessory component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. The beta subunit may assist in binding of the phospholipid substrate. Required for the proper folding, assembly and ER to Golgi exit of the ATP8A2:TMEM30A flippase complex. ATP8A2:TMEM30A may be involved in regulation of neurite outgrowth, and, reconstituted to liposomes, predomiminantly transports phosphatidylserine (PS) and to a lesser extent phosphatidylethanolamine (PE). The ATP8A1:TMEM30A flippase complex seems to play a role in regulation of cell migration probably involving flippase-mediated translocation of phosphatidylethanolamine (PE) at the plasma membrane. Required for the formation of the ATP8A2, ATP8B1 and ATP8B2 P-type ATPAse intermediate phosphoenzymes. Involved in uptake of platelet-activating factor (PAF). Can also mediate the export of alpha subunits ATP8A1, ATP8B1, ATP8B2, ATP8B4, ATP10A, ATP10B, ATP10D, ATP11A, ATP11B and ATP11C from the ER to other membrane localizations. {ECO:0000269|PubMed:22641037, ECO:0000269|PubMed:23269685}. PTM: N-glycosylated. Contains high mannose-type oligosaccharides. {ECO:0000269|PubMed:22253360}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:22253360}; Multi-pass membrane protein {ECO:0000269|PubMed:22253360}. Cell membrane {ECO:0000250}. Golgi apparatus {ECO:0000269|PubMed:22253360}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000269|PubMed:22253360}. Apical cell membrane {ECO:0000269|PubMed:22253360}. SUBUNIT: Component of various P4-ATPase flippase complexes which consists of a catalytic alpha subunit and an accessory beta subunit. The ATP8A2:TMEM30A flippase complex has been purified, and ATP8B1:TMEM30A and ATP8B2:TMEM30A flippase complexes have been shown to form intermediate phosphoenzymes in vitro. Interacts with alpha subunits ATP8A1, ATP8B1, ATP8B2, ATP8B4, ATP11A, ATP11B and ATP11C. {ECO:0000269|PubMed:23269685}. DOMAIN: The N-terminal domain seems to play a role in the reaction cycle of thr catalytic subunit such as ATP8A2. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in photoreceptor cells; detected in retina outer segment (at protein level). Detetced in hepatocytes liver sinusoidal endothelial cells and kidney brush border of the proximal tubules (at protrein level). {ECO:0000269|PubMed:22253360, ECO:0000269|PubMed:22307598, ECO:0000269|PubMed:24413176}. +Q8C9M2 CCD15_MOUSE Coiled-coil domain-containing protein 15 810 93,527 Alternative sequence (3); Chain (1); Coiled coil (3) +Q9DBT3 CCD97_MOUSE Coiled-coil domain-containing protein 97 340 38,724 Chain (1); Coiled coil (1); Modified residue (5) +Q8CDN8 CCD38_MOUSE Coiled-coil domain-containing protein 38 563 65,835 Alternative sequence (2); Chain (1); Coiled coil (3); Sequence conflict (3) SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q502W7}. +Q8CH18 CCAR1_MOUSE Cell division cycle and apoptosis regulator protein 1 (Cell cycle and apoptosis regulatory protein 1) (CARP-1) 1146 132,060 Alternative sequence (3); Chain (1); Coiled coil (2); Compositional bias (3); Cross-link (5); Domain (1); Modified residue (6); Region (3); Sequence caution (6); Sequence conflict (4) FUNCTION: Associates with components of the Mediator and p160 coactivator complexes that play a role as intermediaries transducing regulatory signals from upstream transcriptional activator proteins to basal transcription machinery at the core promoter. Recruited to endogenous nuclear receptor target genes in response to the appropriate hormone. Also functions as a p53 coactivator. May thus play an important role in transcriptional regulation. May be involved in apoptosis signaling in the presence of the retinoid CD437. Apoptosis induction involves sequestration of 14-3-3 protein(s) and mediated altered expression of multiple cell cycle regulatory genes including MYC, CCNB1 and CDKN1A. Plays a role in cell cycle progression and/or cell proliferation (By similarity). In association with CALCOCO1 enhances GATA1- and MED1-mediated transcriptional activation from the gamma-globin promoter during erythroid differentiation of K562 erythroleukemia cells (PubMed:24245781). Can act as a both a coactivator and corepressor of AR-mediated transcription. Contributes to chromatin looping and AR transcription complex assembly by stabilizing AR-GATA2 association on chromatin and facilitating MED1 and RNA polymerase II recruitment to AR-binding sites. May play an important role in the growth and tumorigenesis of prostate cancer cells (PubMed:23887938). {ECO:0000250|UniProtKB:Q8IX12, ECO:0000269|PubMed:23887938, ECO:0000269|PubMed:24245781}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}. SUBUNIT: Directly interacts with ESR1, NR3C1 and p53/TP53. Interacts (via N-terminus) with CALCOCO1. Interacts with MED1 and GATA1. Interacts with AR and GATA2 (By similarity). {ECO:0000250|UniProtKB:Q8IX12, ECO:0000269|PubMed:18722177, ECO:0000269|PubMed:24245781}. +O88602 CCG2_MOUSE Voltage-dependent calcium channel gamma-2 subunit (Neuronal voltage-gated calcium channel gamma-2 subunit) (Stargazin) (Transmembrane AMPAR regulatory protein gamma-2) (TARP gamma-2) 323 35,895 Beta strand (2); Chain (1); Glycosylation (1); Modified residue (3); Mutagenesis (3); Transmembrane (4) TRANSMEM 10 30 Helical. {ECO:0000255}.; TRANSMEM 104 124 Helical. {ECO:0000255}.; TRANSMEM 134 154 Helical. {ECO:0000255}.; TRANSMEM 182 202 Helical. {ECO:0000255}. FUNCTION: Regulates the trafficking and gating properties of AMPA-selective glutamate receptors (AMPARs). Promotes their targeting to the cell membrane and synapses and modulates their gating properties by slowing their rates of activation, deactivation and desensitization. Does not show subunit-specific AMPA receptor regulation and regulates all AMPAR subunits. Thought to stabilize the calcium channel in an inactivated (closed) state (By similarity). {ECO:0000250|UniProtKB:Q71RJ2, ECO:0000250|UniProtKB:Q9Y698}. PTM: Phosphorylation of Thr-321 by PKA impairs interaction with DLG1 and DLG4. {ECO:0000269|PubMed:11805122}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Cell junction, synapse, synaptosome {ECO:0000250|UniProtKB:Q71RJ2}. SUBUNIT: The L-type calcium channel is composed of five subunits: alpha-1, alpha-2/delta, beta and gamma. Interacts with the PDZ domains of DLG4/PSD-95 and DLG1/SAP97. May interact with GOPC. Acts as an auxiliary subunit for AMPA-selective glutamate receptors (AMPARs). Found in a complex with GRIA1, GRIA2, GRIA3, GRIA4, CNIH2, CNIH3, CACNG3, CACNG4, CACNG5, CACNG7 and CACNG8. Interacts with GRIA1 and GRIA2 (By similarity). Interacts with MPP2. {ECO:0000250|UniProtKB:Q71RJ2, ECO:0000250|UniProtKB:Q9Y698}. TISSUE SPECIFICITY: Brain. DISEASE: Note=Defects in Cacng2 cause the stargazer (stg) phenotype. Stg mice have spike-wave seizures characteristic of absence epilepsy, with accompanying defects in the cerebellum and inner ear. {ECO:0000269|PubMed:9697694}. +D3YZV8 CCDC8_MOUSE Coiled-coil domain-containing protein 8 homolog 685 73,938 Chain (1); Compositional bias (1); Modified residue (2); Motif (1) FUNCTION: Core component of the 3M complex, a complex required to regulate microtubule dynamics and genome integrity. It is unclear how the 3M complex regulates microtubules, it could act by controlling the level of a microtubule stabilizer. Required for localization of CUL7 to the centrosome. {ECO:0000250|UniProtKB:Q9H0W5}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H0W5}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9H0W5}. SUBUNIT: Component of the 3M complex, composed of core components CUL7, CCDC8 and OBSL1. Interacts (via PxLPxI/L motif) with ANKRA2 (via ankyrin repeats); may link the 3M complex to histone deacetylases including HDAC4 and HDAC5. {ECO:0000250|UniProtKB:Q9H0W5}. DOMAIN: The PxLPxI/L motif mediates interaction with ankyrin repeats of ANKRA2. {ECO:0000250|UniProtKB:Q9H0W5}. +P25322 CCND1_MOUSE G1/S-specific cyclin-D1 295 33,429 Chain (1); Compositional bias (1); Cross-link (1); Domain (1); Modified residue (1); Mutagenesis (2) FUNCTION: Regulatory component of the cyclin D1-CDK4 (DC) complex that phosphorylates and inhibits members of the retinoblastoma (RB) protein family including RB1 and regulates the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complex and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also substrate for SMAD3, phosphorylating SMAD3 in a cell-cycle-dependent manner and repressing its transcriptional activity. Component of the ternary complex, cyclin D1/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex. Exhibits transcriptional corepressor activity with INSM1 on the NEUROD1 and INS promoters in a cell cycle-independent manner (By similarity). {ECO:0000250}. PTM: Phosphorylation at Thr-286 by MAP kinases is required for ubiquitination and degradation following DNA damage. It probably plays an essential role for recognition by the FBXO31 component of SCF (SKP1-cullin-F-box) protein ligase complex (By similarity). {ECO:0000250}.; PTM: Ubiquitinated, primarily as 'Lys-48'-linked polyubiquitination. Ubiquitinated by a SCF (SKP1-CUL1-F-box protein) ubiquitin-protein ligase complex containing FBXO4 and CRYAB. Following DNA damage it is ubiquitinated by some SCF (SKP1-cullin-F-box) protein ligase complex containing FBXO31. SCF-type ubiquitination is dependent on Thr-286 phosphorylation. Ubiquitinated also by UHRF2 apparently in a phosphorylation-independent manner (By similarity). Ubiquitination leads to its degradation and G1 arrest. Deubiquitinated by USP2; leading to its stabilization. {ECO:0000250, ECO:0000269|PubMed:17081987, ECO:0000269|PubMed:19767775}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19767775}. Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}. Note=Cyclin D-CDK4 complexes accumulate at the nuclear membrane and are then translocated into the nucleus through interaction with KIP/CIP family members. SUBUNIT: Interacts with USP2. Interacts with UHRF2; the interaction ubiquitinates CCND1 and appears independently of phosphorylation. Interacts (via cyclin N-terminal domain) with INSM1 (via N-terminal region); the interaction competes with the binding of CCND1 to CDK4 during cell cycle progression and inhibits CDK4 activity. Interacts with CDK4; the interaction is prevented with the binding of CCND1 to INSM1 during cell cycle progression (By similarity). Interacts with either CDK4 or CDK6 protein kinase to form a serine/threonine kinase holoenzyme complex. The cyclin subunit imparts substrate specificity to the complex. Component of the ternary complex cyclin D/CDK4/CDKN1B required for nuclear translocation and modulation of CDK4-mediated kinase activity. Interacts directly with CDKN1B. Can form similar complexes with either CDKN1A or CDKN2A. Interacts with FBXO4. {ECO:0000250, ECO:0000269|PubMed:17081987, ECO:0000269|PubMed:19767775, ECO:0000269|PubMed:8534916}. +O08918 CCNG2_MOUSE Cyclin-G2 344 38,848 Chain (1) FUNCTION: May play a role in growth regulation and in negative regulation of cell cycle progression. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Primarily found in the cytoplasm. A minor portion can be detected in some cells in the nucleus. TISSUE SPECIFICITY: Highest levels in intestine. Intermediate levels in spleen, brain and kidney. Low levels in testis, stomach, pancreas, liver, salivary gland and muscle. According to PubMed:9139721 also abundant in thymus. +Q810T2 CCNB3_MOUSE G2/mitotic-specific cyclin-B3 1396 158,969 Alternative sequence (1); Chain (1); Modified residue (1); Motif (1); Sequence conflict (3) FUNCTION: Cyclins are positive regulatory subunits of the cyclin-dependent kinases (CDKs), and thereby play an essential role in the control of the cell cycle, notably via their destruction during cell division. Its tissue specificity suggest that it may be required during early meiotic prophase I (By similarity). {ECO:0000250}. PTM: Ubiquitinated (Probable). Ubiquitination leads to its degradation during anaphase entry, after degradation of CCNB1 (By similarity). {ECO:0000250, ECO:0000305}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with CDK2 kinase. {ECO:0000250}. DOMAIN: The N-terminal destruction box (D-box) probably acts as a recognition signal for degradation via the ubiquitin-proteasome pathway. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in testis. Also expressed in the fetal ovary, but not in the adult. {ECO:0000269|PubMed:12185076}. +Q9Z2V9 CCNI_MOUSE Cyclin-I 377 42,197 Chain (1); Sequence conflict (2) +Q9Z238 CCNE2_MOUSE G1/S-specific cyclin-E2 404 46,669 Chain (1); Compositional bias (1); Modified residue (3); Sequence conflict (1) FUNCTION: Essential for the control of the cell cycle at the late G1 and early S phase. PTM: Phosphorylation by CDK2 triggers its release from CDK2 and degradation via the ubiquitin proteasome pathway. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with the CDK2 (in vivo) and CDK3 (in vitro) protein kinases to form a serine/threonine kinase holoenzyme complex. The cyclin subunit imparts substrate specificity to the complex (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highest levels in adult testis, thymus and brain. Lower levels in placenta, spleen and colon. +Q8QZR8 CCNQ_MOUSE Cyclin-Q (CDK10-activating cyclin) (Cyclin-M) (Cyclin-related protein FAM58A) (Cyclin-related protein FAM58B) 250 28,928 Chain (1); Modified residue (1) FUNCTION: Activating cyclin for the cyclin-associated kinase CDK10. {ECO:0000250}. SUBUNIT: Associates with CDK10 to promote its kinase activity. {ECO:0000250}. +Q63994 CD33_MOUSE Myeloid cell surface antigen CD33 (Sialic acid-binding Ig-like lectin 3) (Siglec-3) (CD antigen CD33) 403 44,824 Alternative sequence (1); Binding site (1); Chain (1); Disulfide bond (3); Domain (2); Glycosylation (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 241 267 Helical. {ECO:0000255}. TOPO_DOM 18 240 Extracellular. {ECO:0000255}.; TOPO_DOM 268 403 Cytoplasmic. {ECO:0000255}. FUNCTION: Sialic-acid-binding immunoglobulin-like lectin (Siglec) that plays a role in mediating cell-cell interactions and in maintaining immune cells in a resting state (By similarity). Preferentially binds sialic acid to the short O-linked glycans of certain mucins (PubMed:12773563). {ECO:0000250|UniProtKB:P20138, ECO:0000269|PubMed:12773563}. PTM: Glycosylated. {ECO:0000250|UniProtKB:P20138}.; PTM: Phosphorylation is involved in binding to PTPN6 and PTPN11. {ECO:0000250|UniProtKB:P20138}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P20138}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P20138}. SUBUNIT: Homodimer; disulfide-linked. Interacts with PTPN6/SHP-1 and PTPN11/SHP-2 upon phosphorylation. Interacts with C1QA (via C-terminus); this interaction activates CD33 inhibitory motifs. {ECO:0000250|UniProtKB:P20138}. TISSUE SPECIFICITY: Expressed on myeloid precursors in the bone marrow. In the peripheral blood, mostly expressed on granulocytes. {ECO:0000269|PubMed:12773563}. +P21855 CD72_MOUSE B-cell differentiation antigen CD72 (Lyb-2) (Lymphocyte antigen 32) (Ly-32) (CD antigen CD72) 354 40,347 Beta strand (5); Chain (1); Disulfide bond (3); Domain (1); Glycosylation (1); Helix (3); Modified residue (2); Natural variant (1); Sequence conflict (27); Topological domain (2); Transmembrane (1) TRANSMEM 96 116 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 95 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 117 354 Extracellular. {ECO:0000255}. FUNCTION: Plays a role in B-cell proliferation and differentiation. PTM: Phosphorylated upon engagement of the B-cell receptor, probably by LYN or SYK. Phosphorylation at Tyr-7 is important for interaction with PTPN6/SHP-1. {ECO:0000269|PubMed:9590210}. SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. SUBUNIT: Homodimer; disulfide-linked. Associates with CD5. Interacts (tyrosine phosphorylated) with PTPN6/SHP-1. {ECO:0000269|PubMed:9590210}. TISSUE SPECIFICITY: Pre-B-cells and B-cells but not terminally differentiated plasma cells. +Q8K4F0 CD226_MOUSE CD226 antigen (Platelet and T-cell activation antigen 1) (CD antigen CD226) 333 38,063 Chain (1); Disulfide bond (2); Domain (2); Glycosylation (7); Modified residue (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 255 275 Helical. {ECO:0000255}. TOPO_DOM 19 254 Extracellular. {ECO:0000255}.; TOPO_DOM 276 333 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in intercellular adhesion, lymphocyte signaling, cytotoxicity and lymphokine secretion mediated by cytotoxic T-lymphocyte (CTL) and NK cell. Cell surface receptor for NECTIN2. Upon ligand binding, stimulates T-cell proliferation and cytokine production, including that of IL2, IL5, IL10, IL13, and IFNG. Competes with PVRIG for NECTIN2-binding. {ECO:0000250|UniProtKB:Q15762}. PTM: Phosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Interacts with PVR and NECTIN2. Competes with PVRIG for NECTIN2-binding. {ECO:0000250|UniProtKB:Q15762}. +P11911 CD79A_MOUSE B-cell antigen receptor complex-associated protein alpha chain (Ig-alpha) (MB-1 membrane glycoprotein) (Membrane-bound immunoglobulin-associated protein) (Surface IgM-associated protein) (CD antigen CD79a) 220 24,583 Chain (1); Disulfide bond (2); Domain (2); Glycosylation (2); Modified residue (4); Mutagenesis (5); Sequence conflict (2); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 138 159 Helical. {ECO:0000255}. TOPO_DOM 29 137 Extracellular. {ECO:0000255}.; TOPO_DOM 160 220 Cytoplasmic. {ECO:0000255}. FUNCTION: Required in cooperation with CD79B for initiation of the signal transduction cascade activated by binding of antigen to the B-cell antigen receptor complex (BCR) which leads to internalization of the complex, trafficking to late endosomes and antigen presentation. Also required for BCR surface expression and for efficient differentiation of pro- and pre-B-cells. Stimulates SYK autophosphorylation and activation. Binds to BLNK, bringing BLNK into proximity with SYK and allowing SYK to phosphorylate BLNK. Also interacts with and increases activity of some Src-family tyrosine kinases. Represses BCR signaling during development of immature B-cells. {ECO:0000269|PubMed:10352267, ECO:0000269|PubMed:10591178, ECO:0000269|PubMed:11514602, ECO:0000269|PubMed:11859098, ECO:0000269|PubMed:12097390, ECO:0000269|PubMed:12356683, ECO:0000269|PubMed:15661879, ECO:0000269|PubMed:16860757, ECO:0000269|PubMed:17163454, ECO:0000269|PubMed:8175787, ECO:0000269|PubMed:9469435}. PTM: Phosphorylated on tyrosine, serine and threonine residues upon B-cell activation. Phosphorylation of tyrosine residues by Src-family kinases, including LYN, is an early and essential feature of the BCR signaling cascade. The phosphorylated tyrosines serve as docking sites for SH2-domain containing kinases, leading to their activation which in turn leads to phosphorylation of downstream targets. Phosphorylation of serine and threonine residues may prevent subsequent tyrosine phosphorylation. {ECO:0000269|PubMed:11449366, ECO:0000269|PubMed:15335855, ECO:0000269|PubMed:7592958, ECO:0000269|PubMed:8306975}.; PTM: Arginine methylation in the ITAM domain may interfere with the binding of SYK. It promotes signals leading to B-cell differentiation. {ECO:0000269|PubMed:20231378}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10587346, ECO:0000269|PubMed:11238609, ECO:0000269|PubMed:15661879}; Single-pass type I membrane protein {ECO:0000269|PubMed:10587346, ECO:0000269|PubMed:11238609, ECO:0000269|PubMed:15661879}. Note=Following antigen binding, the BCR has been shown to translocate from detergent-soluble regions of the cell membrane to lipid rafts although signal transduction through the complex can also occur outside lipid rafts. SUBUNIT: Heterodimer of alpha and beta chains; disulfide-linked. Part of the B-cell antigen receptor complex where the alpha/beta chain heterodimer is non-covalently associated with an antigen-specific membrane-bound surface immunoglobulin of two heavy chains and two light chains. Interacts through its phosphorylated ITAM domain with the SH2 domains of SYK which stimulates SYK autophosphorylation and activation. Also interacts, when phosphorylated on Tyr-204, with the SH2 domain of BLNK/SLP65, bringing BLNK into proximity with SYK and allowing SYK to phosphorylate BLNK which is necessary for trafficking of the BCR to late endosomes. Interacts with Src-family tyrosine kinases including FYN and LYN, increasing their activity. {ECO:0000269|PubMed:11449366, ECO:0000269|PubMed:11859098, ECO:0000269|PubMed:11909947, ECO:0000269|PubMed:1506682, ECO:0000269|PubMed:15335855, ECO:0000269|PubMed:7538118, ECO:0000269|PubMed:7592958, ECO:0000269|PubMed:8168489}. TISSUE SPECIFICITY: B-cells. +P58019 CD59B_MOUSE CD59B glycoprotein (MAC-inhibitory protein) (MAC-IP) (Membrane attack complex inhibition factor) (MACIF) (Protectin) (CD antigen CD59) 129 14,227 Chain (1); Disulfide bond (5); Domain (1); Glycosylation (1); Lipidation (1); Propeptide (1); Sequence conflict (2); Signal peptide (1) FUNCTION: Potent inhibitor of the complement membrane attack complex (MAC) action. Acts by binding to the C8 and/or C9 complements of the assembling MAC, thereby preventing incorporation of the multiple copies of C9 required for complete formation of the osmolytic pore (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. TISSUE SPECIFICITY: Widely expressed in the kidneys, brain, lungs, spleen and testis (PubMed:11471050) Testis specific (PubMed:10946279). {ECO:0000269|PubMed:10946279, ECO:0000269|PubMed:11471050}. +Q07763 CD244_MOUSE Natural killer cell receptor 2B4 (NK cell type I receptor protein 2B4) (NKR2B4) (Non-MHC restricted killing associated) (SLAM family member 4) (SLAMF4) (Signaling lymphocytic activation molecule 4) (CD antigen CD244) 397 44,836 Alternative sequence (2); Beta strand (10); Chain (1); Disulfide bond (2); Domain (2); Glycosylation (7); Helix (2); Modified residue (4); Motif (4); Mutagenesis (8); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 227 247 Helical. {ECO:0000255}. TOPO_DOM 20 226 Extracellular. {ECO:0000255}.; TOPO_DOM 248 397 Cytoplasmic. {ECO:0000255}. FUNCTION: Heterophilic receptor of the signaling lymphocytic activation molecule (SLAM) family; its ligand is CD48. SLAM receptors triggered by homo- or heterotypic cell-cell interactions are modulating the activation and differentiation of a wide variety of immune cells and thus are involved in the regulation and interconnection of both innate and adaptive immune response. Activities are controlled by presence or absence of small cytoplasmic adapter proteins, SH2D1A/SAP and/or SH2D1B/EAT-2. Acts as activating natural killer (NK) cell receptor (PubMed:8326140, PubMed:12734329, PubMed:19648922, PubMed:20962259). Activating function implicates association with SH2D1A and FYN. Downstreaming signaling involves predominantly VAV1, and, to a lesser degree, INPP5D/SHIP1 and CBL. Signal attenuation in the absence of SH2D1A is proposed to be dependent on INPP5D and to a lesser extent PTPN6/SHP-1 and PTPN11/SHP-2. Stimulates NK cell cytotoxicity, production of IFN-gamma and granule exocytosis (PubMed:8326140, PubMed:15169881, PubMed:15998796, PubMed:22683124). Optimal expansion and activation of NK cells seems to be dependent on the engagement of CD244 with CD48 expressed on neighboring NK cells (PubMed:15905190). Regulation of NK cell activity by adapters Sh2d1b and Sh2d1b2 is reported conflictingly (PubMed:16127454, PubMed:16425036). Acts as costimulator in NK activation by enhancing signals by other NK receptors such as NCR3 and NCR1. At early stages of NK cell differentiation may function as an inhibitory receptor possibly ensuring the self-tolerance of developing NK cells (By similarity). Involved in the regulation of CD8(+) T-cell proliferation; expression on activated T-cells and binding to CD488 provides costimulatory-like function for neighboring T-cells (PubMed:11739483). Inhibits inflammatory responses in dendritic cells (DCs) (PubMed:25643613). {ECO:0000250|UniProtKB:Q9BZW8, ECO:0000269|PubMed:11739483, ECO:0000269|PubMed:12734329, ECO:0000269|PubMed:15169881, ECO:0000269|PubMed:15998796, ECO:0000269|PubMed:19648922, ECO:0000269|PubMed:20962259, ECO:0000269|PubMed:22683124, ECO:0000269|PubMed:8326140, ECO:0000305|PubMed:16127454, ECO:0000305|PubMed:16425036}. PTM: N-linked glycosylation is essential for the binding to its ligand CD48. Also O-glycosylated, in contrast, O-linked sialylation has a negative impact on ligand binding (By similarity). {ECO:0000250}.; PTM: Phosphorylated by FYN and CSK at tyrosine residues following activation. Coligation with inhibitory receptors such as KIR2DL1 inhibits phosphorylation upon contact of NK cells with sensitive target cells. {ECO:0000250|UniProtKB:Q9BZW8}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Cell membrane {ECO:0000305}. Note=Receptor engagement results in a recruitment to lipid drafts essential for the subsequent tyrosine phosphorylation of the ITSMs. {ECO:0000250|UniProtKB:Q9BZW8}. SUBUNIT: Interacts with CD48 (PubMed:9841922, PubMed:15905190). Interacts (via phosphorylated ITSM 1-4) with SH2D1A/SAP (via SH2 domain); SH2D1A probably mediates association with FYN. Interacts (via phosphorylated ITSM 3) with PTPN11/SHP-2, INPP5D/SHIP1, PTPN6/SHP-1 and CSK; binding of SH2D1A prevents association with PTPN11, PTPN6 and CSK. Interacts weakly (via phosphorylated ITSM 2) with PTPN11 and CSK. Interacts with SH2D1B and SH2D1B2. Interacts with MHC class I proteins; the interaction is proposed to prevent self-killing of NK cells (By similarity). {ECO:0000250|UniProtKB:Q9BZW8, ECO:0000269|PubMed:15905190, ECO:0000269|PubMed:16127454, ECO:0000269|PubMed:9841922}. DOMAIN: The ITSMs (immunoreceptor tyrosine-based switch motifs) with the consensus sequence T-X-Y-X-X-[VI] present in SLAM family receptors have overlapping specificity for activating and inhibitory SH2 domain-containing binding partners. Especially they mediate the interaction with the SH2 domain of SH2D1A and SH2D1B. A 'three-pronged' mechanism is proposed involving threonine (position -2), phosphorylated tyrosine (position 0) and valine/isoleucine (position +3). {ECO:0000250|UniProtKB:Q13291, ECO:0000305|PubMed:15169881}. TISSUE SPECIFICITY: Expressed in natural killer (NK) cells, T cells and dendritic cells. {ECO:0000269|PubMed:25643613, ECO:0000269|PubMed:8326140}. +P24807 CD24_MOUSE Signal transducer CD24 (Lymphocyte antigen 52) (Ly-52) (M1/69-J11D heat stable antigen) (HSA) (Nectadrin) (R13-Ag) (X62 heat stable antigen) (CD antigen CD24) 76 7,797 Glycosylation (7); Lipidation (1); Peptide (1); Propeptide (1); Signal peptide (1); Site (1) FUNCTION: May have a pivotal role in cell differentiation of different cell types. May have a specific role in early thymocyte development. Signaling could be triggered by the binding of a lectin-like ligand to the CD24 carbohydrates, and transduced by the release of second messengers derived from the GPI-anchor. Modulates B-cell activation responses (By similarity). In association with SIGLEC10 may be involved in the selective suppression of the immune response to danger-associated molecular patterns (DAMPs) such as HMGB1, HSP70 and HSP90 (PubMed:19264983). Plays a role in the control of autoimmunity (PubMed:20200274). {ECO:0000250|UniProtKB:P25063, ECO:0000269|PubMed:19264983, ECO:0000269|PubMed:20200274}. PTM: The identity of the N- and O-linked polysaccharides are not reported in PubMed:1530634. The O-linked polysaccharides on Ser-30, Ser-41, Ser-43, and Thr-51 are probably the mucin type linked to GalNAc. {ECO:0000269|PubMed:1530634}. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. SUBUNIT: Interacts with SIGLEC10; the probable CD24:SIGLEC10 complex is proposed to inhibit HGMB1-mediated tissue damage immune response. {ECO:0000269|PubMed:19264983}. TISSUE SPECIFICITY: In lymphoid, myeloid, and erythroid cells. +P35762 CD81_MOUSE CD81 antigen (26 kDa cell surface protein TAPA-1) (Target of the antiproliferative antibody 1) (CD antigen CD81) 236 25,815 Binding site (1); Chain (1); Disulfide bond (2); Helix (6); Sequence conflict (1); Site (3); Topological domain (5); Transmembrane (4) TRANSMEM 13 33 Helical. {ECO:0000250|UniProtKB:P60033}.; TRANSMEM 64 84 Helical. {ECO:0000250|UniProtKB:P60033}.; TRANSMEM 90 112 Helical. {ECO:0000250|UniProtKB:P60033}.; TRANSMEM 202 224 Helical. {ECO:0000250|UniProtKB:P60033}. TOPO_DOM 1 12 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 34 63 Extracellular. {ECO:0000305}.; TOPO_DOM 85 89 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 113 201 Extracellular. {ECO:0000305}.; TOPO_DOM 225 236 Cytoplasmic. {ECO:0000305}. FUNCTION: Required for normal cell surface expression of CD19 and for normal adaptive immune responses (By similarity). Required for normal female fertility and normal sperm-egg fusion (PubMed:16380109). May be involved in the acrosome reaction. {ECO:0000250|UniProtKB:P60033, ECO:0000269|PubMed:16380109, ECO:0000269|PubMed:17290409}. PTM: Not glycosylated. {ECO:0000305}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23213457}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:P60033}; Multi-pass membrane protein {ECO:0000255}. Note=Associates with CLDN1 and the CLDN1-CD81 complex localizes to the basolateral cell membrane. {ECO:0000250|UniProtKB:P60033}. SUBUNIT: Homodimer. Interacts with CD53 and SCIMP (By similarity). Interacts directly with IGSF8 (PubMed:11673522). Interacts with IFITM2 and IFITM3 (PubMed:16395393). Interacts with IFITM1. Part of a complex composed of CD19, CR2/CD21, CD81 and IFITM1/CD225 in the membrane of mature B-cells (By similarity). Part of a GPCR-tetraspanin complex consisting at least of ADGRG1, CD81, eventually CD9, and GNA11 in which CD81 enhances the association of ADGRG1 with GNA11. Interacts with CLDN1, CLDN6 and CLDN9 (By similarity). Interacts (via the second extracellular domain) with integrin ITGAV:ITGB3 (By similarity). Interacts with glypican GPC3 and with transcriptional repressor HHEX; binding to GPC3 decreases the availability of free CD81 for binding to HHEX, resulting in nuclear translocation of HHEX and transcriptional repression (PubMed:23665349). {ECO:0000250|UniProtKB:P60033, ECO:0000269|PubMed:11673522, ECO:0000269|PubMed:16395393, ECO:0000269|PubMed:23665349}. DOMAIN: Binds cholesterol in a cavity lined by the transmembrane spans. {ECO:0000250|UniProtKB:P60033}. TISSUE SPECIFICITY: Expressed in oocytes (PubMed:16380109, PubMed:17290409, PubMed:23213457). Highly expressed in granulosa cells (PubMed:16380109). {ECO:0000269|PubMed:16380109, ECO:0000269|PubMed:17290409, ECO:0000269|PubMed:23213457}. +Q61470 CD37_MOUSE Leukocyte antigen CD37 (CD antigen CD37) 281 31,852 Chain (1); Glycosylation (3); Topological domain (5); Transmembrane (4) TRANSMEM 18 38 Helical. {ECO:0000255}.; TRANSMEM 60 74 Helical. {ECO:0000255}.; TRANSMEM 86 111 Helical. {ECO:0000255}.; TRANSMEM 242 266 Helical. {ECO:0000255}. TOPO_DOM 1 17 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 39 59 Extracellular. {ECO:0000255}.; TOPO_DOM 75 85 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 112 241 Extracellular. {ECO:0000255}.; TOPO_DOM 267 281 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SUBUNIT: Interacts with SCIMP. {ECO:0000250}. +P13379 CD5_MOUSE T-cell surface glycoprotein CD5 (Lymphocyte antigen 1) (Ly-1) (Lyt-1) (CD antigen CD5) 494 53,849 Chain (1); Disulfide bond (10); Domain (3); Glycosylation (4); Modified residue (5); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 372 401 Helical. {ECO:0000255}. TOPO_DOM 25 371 Extracellular. {ECO:0000255}.; TOPO_DOM 402 494 Cytoplasmic. {ECO:0000255}. FUNCTION: May act as a receptor in regulating T-cell proliferation. PTM: Phosphorylated on tyrosine residues by LYN; this creates binding sites for PTPN6/SHP-1. {ECO:0000269|PubMed:11007759}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SUBUNIT: Interacts with CD72/LYB-2. Interacts with PTPN6/SHP-1. {ECO:0000269|PubMed:11007759}. +P10300 CD8B_MOUSE T-cell surface glycoprotein CD8 beta chain (Lymphocyte antigen 3) (T-cell membrane glycoprotein Ly-3) (T-cell surface glycoprotein Lyt-3) (CD antigen CD8b) 213 24,288 Beta strand (13); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (1); Helix (2); Natural variant (2); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (2) TRANSMEM 176 196 Helical. {ECO:0000255}. TOPO_DOM 22 175 Extracellular. {ECO:0000255}.; TOPO_DOM 197 213 Cytoplasmic. {ECO:0000255}. FUNCTION: Integral membrane glycoprotein that plays an essential role in the immune response and serves multiple functions in responses against both external and internal offenses. In T-cells, functions primarily as a coreceptor for MHC class I molecule:peptide complex. The antigens presented by class I peptides are derived from cytosolic proteins while class II derived from extracellular proteins. Interacts simultaneously with the T-cell receptor (TCR) and the MHC class I proteins presented by antigen presenting cells (APCs). In turn, recruits the Src kinase LCK to the vicinity of the TCR-CD3 complex. A palmitoylation site in the cytoplasmic tail of CD8B chain contributes to partitioning of CD8 into the plasma membrane lipid rafts where signaling proteins are enriched. Once LCK recruited, it initiates different intracellular signaling pathways by phosphorylating various substrates ultimately leading to lymphokine production, motility, adhesion and activation of cytotoxic T-lymphocytes (CTLs). Additionally, plays a critical role in thymic selection of CD8+ T-cells. {ECO:0000250|UniProtKB:P10966, ECO:0000269|PubMed:12215456, ECO:0000269|PubMed:8064243, ECO:0000269|PubMed:8108731}. PTM: Palmitoylated at the cytoplasmic tail and thereby targets the heterodimer CD8A/CD8B to lipid rafts unlike CD8A homodimers. {ECO:0000250|UniProtKB:P10966}. SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P10966}; Single-pass type I membrane protein. Note=Requires the partner CD8A for efficient cell surface expression. The heterodimer CD8A/CD8B localizes to lipid rafts due to CD8B cytoplasmic tail palmitoylation. {ECO:0000250|UniProtKB:P10966}. SUBUNIT: Forms disulfide-linked heterodimers with CD8A at the cell surface. Interacts with CD3D; this interaction couples TCR-CD3 with CD8. Interacts with LCK. {ECO:0000250|UniProtKB:P10966, ECO:0000269|PubMed:12215456, ECO:0000269|PubMed:16356863, ECO:0000269|PubMed:18929574}. +Q04735 CDK16_MOUSE Cyclin-dependent kinase 16 (EC 2.7.11.22) (CRK5) (Cell division protein kinase 16) (PCTAIRE-motif protein kinase 1) (Serine/threonine-protein kinase PCTAIRE-1) 496 55,914 Active site (1); Alternative sequence (2); Binding site (1); Chain (1); Domain (1); Modified residue (11); Mutagenesis (1); Nucleotide binding (1) FUNCTION: Protein kinase that plays a role in vesicle-mediated transport processes and exocytosis. Can phosphorylate CCNY at 'Ser-336' (in vitro) (By similarity). Plays a role in the regulation of insulin secretion in response to changes in blood glucose levels. Regulates GH1 release by brain neurons. Phosphorylates NSF, and thereby regulates NSF oligomerization. Required for normal spermatogenesis. Regulates neuron differentiation and dendrite development. {ECO:0000250, ECO:0000269|PubMed:16461345, ECO:0000269|PubMed:21335063, ECO:0000269|PubMed:22184064, ECO:0000269|PubMed:22798068}. PTM: Phosphorylation at Ser-153 inhibits kinase activity. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle. Cell junction, synapse, synaptosome. Note=Colocalizes with insulin in pancreas islets. {ECO:0000250}. SUBUNIT: Found in a complex containing CABLES1, CDK17 and TDRD7. Interacts with BRSK2. Identified in a complex with NSF, syntaxin-1, synaptotagmin, SYN1, SYP and CDK5R1 (By similarity). Interacts with YWHAH, YWHAQ and YWHAZ. Interacts with CCNY; this increases the CDK16 kinase activity. Interacts with NSF. {ECO:0000250, ECO:0000269|PubMed:16461345, ECO:0000269|PubMed:22184064, ECO:0000269|PubMed:22796189, ECO:0000269|PubMed:9197417}. TISSUE SPECIFICITY: Highly expressed in testis and brain, and detected at lower levels in heart, skeletal muscle, adipose tissue, lung, spleen and pancreas (at protein level). Ubiquitous with highest levels in testis and brain, with longer form predominant in all tissues except the testis. {ECO:0000269|PubMed:22184064, ECO:0000269|PubMed:22796189, ECO:0000269|PubMed:22798068}. +Q8CEQ0 CDKL1_MOUSE Cyclin-dependent kinase-like 1 (EC 2.7.11.22) 352 41,024 Active site (1); Binding site (1); Chain (1); Domain (1); Motif (1); Nucleotide binding (1) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. DOMAIN: The [NKR]KIAxRE motif seems to be a cyclin-binding region. +Q03147 CDK7_MOUSE Cyclin-dependent kinase 7 (EC 2.7.11.22) (EC 2.7.11.23) (39 kDa protein kinase) (P39 Mo15) (CDK-activating kinase) (CR4 protein kinase) (CRK4) (Cell division protein kinase 7) (Protein-tyrosine kinase MPK-7) (TFIIH basal transcription factor complex kinase subunit) 346 38,968 Active site (1); Binding site (1); Chain (1); Domain (1); Initiator methionine (1); Modified residue (4); Nucleotide binding (1); Sequence conflict (6) FUNCTION: Serine/threonine kinase involved in cell cycle control and in RNA polymerase II-mediated RNA transcription. Cyclin-dependent kinases (CDKs) are activated by the binding to a cyclin and mediate the progression through the cell cycle. Each different complex controls a specific transition between 2 subsequent phases in the cell cycle. Required for both activation and complex formation of CDK1/cyclin-B during G2-M transition, and for activation of CDK2/cyclins during G1-S transition (but not complex formation). CDK7 is the catalytic subunit of the CDK-activating kinase (CAK) complex. Phosphorylates SPT5/SUPT5H, SF1/NR5A1, POLR2A, p53/TP53, CDK1, CDK2, CDK4, CDK6 and CDK11B/CDK11. CAK activates the cyclin-associated kinases CDK1, CDK2, CDK4 and CDK6 by threonine phosphorylation, thus regulating cell cycle progression. CAK complexed to the core-TFIIH basal transcription factor activates RNA polymerase II by serine phosphorylation of the repetitive C-terminal domain (CTD) of its large subunit (POLR2A), allowing its escape from the promoter and elongation of the transcripts. Phosphorylation of POLR2A in complex with DNA promotes transcription initiation by triggering dissociation from DNA. Its expression and activity are constant throughout the cell cycle. Upon DNA damage, triggers p53/TP53 activation by phosphorylation, but is inactivated in turn by p53/TP53; this feedback loop may lead to an arrest of the cell cycle and of the transcription, helping in cell recovery, or to apoptosis. Required for DNA-bound peptides-mediated transcription and cellular growth inhibition. PTM: Phosphorylation of Ser-164 during mitosis inactivates the enzyme. Phosphorylation of Thr-170 is required for activity. Phosphorylated at Ser-164 and Thr-170 by CDK2 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Colocalizes with PRKCI in the cytoplasm and nucleus. Translocates from the nucleus to cytoplasm and perinuclear region in response to DNA-bound peptides (By similarity). {ECO:0000250}. SUBUNIT: Associates primarily with cyclin-H (CCNH) and MAT1 to form the CAK complex. CAK can further associate with the core-TFIIH to form the TFIIH basal transcription factor; this complex is sensitive to UV light. The CAK complex binds to p53/TP53 in response to DNA damage. Interacts with CDK2, SF1/NR5A1, PUF60 and PRKCI (By similarity). {ECO:0000250}. +Q80X32 CE024_MOUSE UPF0461 protein C5orf24 homolog 188 20,139 Chain (1); Cross-link (2); Erroneous initiation (1); Modified residue (3) +A2AUM9 CE152_MOUSE Centrosomal protein of 152 kDa (Cep152) 1736 196,534 Chain (1); Coiled coil (6); Erroneous initiation (1); Modified residue (2); Region (1) FUNCTION: Necessary for centrosome duplication; the function seems also to involve CEP63, CDK5RAP2 and WDR62 through a stepwise assembled complex at the centrosome that recruits CDK2 required for centriole duplication (By similarity). Acts as a molecular scaffold facilitating the interaction of PLK4 and CENPJ, 2 molecules involved in centriole formation (By similarity). Proposed to snatch PLK4 away from PLK4:CEP92 complexes in early G1 daughter centriole and to reposition PLK4 at the outer boundary of a newly forming CEP152 ring structure (By similarity). Also plays a key role in deuterosome-mediated centriole amplification in multiciliated that can generate more than 100 centrioles (PubMed:24240477). Overexpression of cep152 can drive amplification of centrioles. {ECO:0000250|UniProtKB:O94986, ECO:0000250|UniProtKB:Q498G2, ECO:0000269|PubMed:24240477}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:O94986}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:O94986}. Note=Colocalizes with CDK5RAP2, WDR62 and CEP63 in a discrete ring around the proximal end of the parental centriole (By similarity). At this site, a cohesive structure is predicted to engage parental centrioles and procentrioles (By similarity). Localizes to the deuterosome (PubMed:24240477). Localizes to pericentriolar material (PCM) (By similarity). {ECO:0000250|UniProtKB:O94986, ECO:0000269|PubMed:24240477}. SUBUNIT: Interacts (via N-terminus) with PLK4; the interaction is mutally exclusive with a PLK4:CEP192 interaction. Interacts (via C-terminus) with CENPJ (via-N-terminus). Interacts with CINP. Interacts with CDK5RAP2, WDR62, CEP63 and CEP131. CEP63, CDK5RAP2, CEP152, WDR62 are proposed to form a stepwise assembled complex at the centrosome forming a ring near parental centrioles (By similarity). Interacts with DEUP1; this interaction recruits CEP152 to the deuterosome. The interactions with CEP63 and DEUP1 are mutually exclusive (PubMed:24240477). {ECO:0000250|UniProtKB:O94986, ECO:0000269|PubMed:24240477}. +Q14AX6 CDK12_MOUSE Cyclin-dependent kinase 12 (EC 2.7.11.22) (EC 2.7.11.23) (Cdc2-related kinase, arginine/serine-rich) (CrkRS) (Cell division cycle 2-related protein kinase 7) (CDC2-related protein kinase 7) (Cell division protein kinase 12) 1484 163,681 Active site (1); Alternative sequence (3); Binding site (2); Chain (1); Compositional bias (4); Cross-link (3); Domain (1); Erroneous gene model prediction (1); Modified residue (40); Nucleotide binding (2); Sequence conflict (9) FUNCTION: Cyclin-dependent kinase that phosphorylates the C-terminal domain (CTD) of the large subunit of RNA polymerase II (POLR2A), thereby acting as a key regulator of transcription elongation. Regulates the expression of genes involved in DNA repair and is required for the maintenance of genomic stability. Preferentially phosphorylates 'Ser-5' in CTD repeats that are already phosphorylated at 'Ser-7', but can also phosphorylate 'Ser-2'. Required for RNA splicing, possibly by phosphorylating SRSF1/SF2. Involved in regulation of MAP kinase activity, possibly leading to affect the response to estrogen inhibitors. {ECO:0000269|PubMed:22012619}. PTM: Phosphorylation at Thr-889 increases kinase activity. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus speckle {ECO:0000250}. Note=Colocalized with nuclear speckles throughout interphase. {ECO:0000250}. SUBUNIT: Interacts with CCNL1 and CCNL2. {ECO:0000250}. +Q0VBV7 CE126_MOUSE Centrosomal protein of 126 kDa 1103 123,685 Chain (1); Coiled coil (2) FUNCTION: Participate in cytokinesis (By similarity). Necessary for microtubules and mitotic spindle organization (By similarity). Involved in primary cilium formation (By similarity). {ECO:0000250|UniProtKB:Q9P2H0}. SUBCELLULAR LOCATION: Midbody {ECO:0000250|UniProtKB:Q9P2H0}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9P2H0}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q9P2H0}. SUBUNIT: Interacts with DCTN1 (By similarity). {ECO:0000250|UniProtKB:Q9P2H0}. +E9Q309 CE350_MOUSE Centrosome-associated protein 350 (Cep350) 3095 346,456 Chain (1); Coiled coil (6); Compositional bias (2); Domain (1); Modified residue (24); Sequence conflict (1) FUNCTION: Plays an essential role in centriole growth by stabilizing a procentriolar seed composed of at least, SASS6 and CENPJ. Required for anchoring microtubules to the centrosomes and for the integrity of the microtubule network. Recruits PPARA to discrete subcellular compartments and thereby modulates PPARA activity. Required for ciliation. {ECO:0000250|UniProtKB:Q5VT06}. PTM: Phosphorylated during mitosis. {ECO:0000250|UniProtKB:Q5VT06}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q5VT06}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q5VT06}. Nucleus {ECO:0000250|UniProtKB:Q5VT06}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q5VT06}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q5VT06}. Note=Associated with mitotic spindles. Nuclear, in discrete foci. Associated with intermediate filaments. Also present in the pericentrosomal area. Localizes on both mother and daughter centrioles. Localizes to an axial position on the mother centriole. Localizes to the distal end of the centriole on the subdistal appendage region. {ECO:0000250|UniProtKB:Q5VT06}. SUBUNIT: Part of a ternary complex that contains CEP350, FGFR1OP and MAPRE1. Interacts (via C-terminus) directly with FGFR1OP (via N-terminus). Interacts with NR1H3, PPARA, PPARD and PPARG. Interacts directly with microtubules. Interacts with the fusion protein FGFR1OP-FGFR1, and by doing so recruits and activates PI3K and PLC-gamma. Interacts with CYLD (By similarity). Interacts with CFAP157 (PubMed:27965440). Interacts with CEP19 (via C-terminus) (By similarity). {ECO:0000250|UniProtKB:Q5VT06, ECO:0000269|PubMed:27965440}. +Q8VDS7 CE57L_MOUSE Centrosomal protein CEP57L1 (Centrosomal protein 57kDa-like protein 1) (Centrosomal protein of 57 kDa-related protein) (Cep57R) (Cep57-related protein) 400 46,790 Alternative sequence (4); Chain (1); Coiled coil (3); Modified residue (1); Sequence conflict (1) FUNCTION: Centrosomal protein which may be required for microtubule attachment to centrosomes. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. +A0A0B4J1L0 CEA15_MOUSE Carcinoembryonic antigen-related cell adhesion molecule 15 234 26,408 Beta strand (9); Chain (1); Disulfide bond (1); Domain (1); Erroneous initiation (2); Glycosylation (4); Helix (1); Signal peptide (1); Turn (1) TISSUE SPECIFICITY: Detected in placenta. {ECO:0000269|PubMed:16139472}. +Q32MD9 CDON_MOUSE Cell adhesion molecule-related/down-regulated by oncogenes 1250 135,422 Chain (1); Disulfide bond (5); Domain (8); Glycosylation (8); Sequence conflict (9); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 963 983 Helical. {ECO:0000255}. TOPO_DOM 25 962 Extracellular. {ECO:0000255}.; TOPO_DOM 984 1250 Cytoplasmic. {ECO:0000255}. FUNCTION: Component of a cell-surface receptor complex that mediates cell-cell interactions between muscle precursor cells. Promotes differentiation of myogenic cells. Required for response to NTN3 and activation of NFATC3. {ECO:0000269|PubMed:15520228, ECO:0000269|PubMed:9786951}. PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. SUBUNIT: Part of a complex that contains BOC, CDON, NEO1, cadherins and CTNNB1. Interacts with NTN3. Interacts with DHH, IHH and SHH (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in somites and the dorsal lips of the neural tube during embryogenesis. Detected at very low levels in adult tissues. {ECO:0000269|PubMed:9786951}. +Q7TN33 CELF6_MOUSE CUGBP Elav-like family member 6 (CELF-6) (Bruno-like protein 6) (CUG-BP- and ETR-3-like factor 6) (RNA-binding protein BRUNOL-6) 460 48,206 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (3) FUNCTION: RNA-binding protein implicated in the regulation of pre-mRNA alternative splicing. Mediates exon inclusion and/or exclusion in pre-mRNA that are subject to tissue-specific and developmentally regulated alternative splicing. Specifically activates exon 5 inclusion of TNNT2 in a muscle-specific splicing enhancer (MSE)-dependent manner. Promotes also exon exclusion of INSR pre-mRNA (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. +Q3TJM4 CENPT_MOUSE Centromere protein T (CENP-T) 515 56,242 Chain (1); Frameshift (1); Modified residue (7); Region (1); Sequence conflict (3) FUNCTION: Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. Part of a nucleosome-associated complex that binds specifically to histone H3-containing nucleosomes at the centromere, as opposed to nucleosomes containing CENPA. Component of the heterotetrameric CENP-T-W-S-X complex that binds and supercoils DNA, and plays an important role in kinetochore assembly. CENPT has a fundamental role in kinetochore assembly and function. It is one of the inner kinetochore proteins, with most further proteins binding downstream. Required for normal chromosome organization and normal progress through mitosis. {ECO:0000250|UniProtKB:Q96BT3}. PTM: Dynamically phosphorylated during the cell cycle. Phosphorylated during G2 phase, metaphase and anaphase, but not during telophase or G1 phase. {ECO:0000250|UniProtKB:Q96BT3}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96BT3}. Chromosome, centromere {ECO:0000250|UniProtKB:Q96BT3}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q96BT3}. Note=Constitutively localizes to centromeres throughout the cell cycle, and to kinetochores during mitosis. Localizes to the inner kinetochore, and may connect it to the outer kinetochore via its N-terminus. {ECO:0000250|UniProtKB:Q96BT3}. SUBUNIT: Component of the CENPA-CAD complex, composed of CENPI, CENPK, CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS. The CENPA-CAD complex is probably recruited on centromeres by the CENPA-NAC complex, at least composed of CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and CENPU. Identified in a centromeric complex containing histones H2A, H2B, H3 and H4, and at least CENPA, CENPB, CENPC, CENPT, CENPN, HJURP, SUPT16H, SSRP1 and RSF1. Interacts (via N-terminus) with the NDC80 complex. Heterodimer with CENPW; this dimer coassembles with CENPS-CENPX heterodimers at centromeres to form the tetrameric CENP-T-W-S-X complex. {ECO:0000250|UniProtKB:Q96BT3}. DOMAIN: The largest part of the sequence forms an elongated and flexible stalk structure that is connected to a C-terminal globular domain with a histone-type fold. {ECO:0000250}. +Q8BVV7 CEP95_MOUSE Centrosomal protein of 95 kDa (Cep95) (Coiled-coil domain-containing protein 45) 827 95,210 Chain (1); Coiled coil (2); Compositional bias (1); Modified residue (3); Sequence conflict (3) SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. +P41209 CETN1_MOUSE Centrin-1 (Caltractin) 172 19,696 Beta strand (3); Calcium binding (2); Chain (1); Domain (4); Helix (7); Sequence conflict (2); Turn (1) FUNCTION: Plays a fundamental role in microtubule-organizing center structure and function (By similarity). Plays a role in sperm cilia formation (PubMed:27530713). {ECO:0000250|UniProtKB:Q12798, ECO:0000269|PubMed:27530713}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Centrosome of interphase and mitotic cells. SUBUNIT: Monomer (By similarity). Interacts with PIFO (PubMed:20643351). {ECO:0000250, ECO:0000269|PubMed:20643351}. TISSUE SPECIFICITY: Expressed exclusively in testis. Localizes to the caudal portion of spermatozoa in seminiferous tubule and epididymis. {ECO:0000269|PubMed:10486202}. +Q91WU0 CES1F_MOUSE Carboxylesterase 1F (EC 3.1.1.1) (Carboxylic ester hydrolase) (Triacylglycerol hydrolase 2) (TGH-2) 561 61,612 Active site (3); Alternative sequence (2); Chain (1); Disulfide bond (2); Motif (1); Sequence conflict (2); Signal peptide (1) FUNCTION: Hydrolyzes p-nitrophenyl butyrate (PNPB), triacylglycerol and monoacylglycerol. Shows higher activity against PNPB, a short-chain fatty acid ester, than against triolein, a long-chain fatty acid ester. Shows no detectable activity against diacylglycerol, cholesterol ester or phospholipids. May play a role in adipocyte lipolysis. {ECO:0000269|PubMed:16804080}. SUBCELLULAR LOCATION: Lipid droplet {ECO:0000305|PubMed:16804080}. Cytoplasm, cytosol {ECO:0000269|PubMed:16804080}. Endoplasmic reticulum {ECO:0000269|PubMed:16804080}. TISSUE SPECIFICITY: Expressed in liver, white and brown adipose tissue, kidney, intestine, adrenal, heart and ovary. Not detected in muscle, lung, testis, brain and spleen. {ECO:0000269|PubMed:16804080}. +Q8CC96 CF222_MOUSE Uncharacterized protein C6orf222 homolog 669 72,970 Chain (1); Cross-link (1); Sequence conflict (1) +Q3V037 CF163_MOUSE Uncharacterized protein C6orf163 homolog 328 38,548 Chain (1); Coiled coil (2) +Q1A3B0 CERS3_MOUSE Ceramide synthase 3 (CerS3) (EC 2.3.1.24) (Dihydroceramide synthase 3) (LAG1 longevity assurance homolog 3) 383 46,081 Alternative sequence (1); Chain (1); Compositional bias (1); DNA binding (1); Domain (1); Modified residue (1); Sequence conflict (1); Transmembrane (6) TRANSMEM 32 52 Helical. {ECO:0000255}.; TRANSMEM 139 159 Helical. {ECO:0000255}.; TRANSMEM 174 194 Helical. {ECO:0000255}.; TRANSMEM 205 225 Helical. {ECO:0000255}.; TRANSMEM 263 283 Helical. {ECO:0000255}.; TRANSMEM 302 322 Helical. {ECO:0000255}. FUNCTION: Has (dihydro)ceramide synthesis activity with relatively broad substrate specificity, but a preference for C18:0 and other middle- to long-chain fatty acyl-CoAs. It is crucial for the synthesis of very long-chain ceramides in the epidermis, to maintain epidermal lipid homeostasis and terminal differentiation (By similarity). {ECO:0000250, ECO:0000269|PubMed:16753040}. SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000255|PROSITE-ProRule:PRU00108}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Predominantly expressed in testis. {ECO:0000269|PubMed:16753040}. +Q8BL95 CF298_MOUSE Cilia- and flagella-associated protein 298 (Protein kurly homolog) 290 33,190 Chain (1); Sequence conflict (1) FUNCTION: Plays a role in motile cilium function, possibly by acting on outer dynein arm assembly. Seems to be important for initiation rather than maintenance of cilium motility. Required for correct positioning of cilia at the apical cell surface, suggesting an additional role in the planar cell polarity (PCP) pathway. May suppress canonical Wnt signaling activity. {ECO:0000250|UniProtKB:Q6DRC3}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q5U3Z0}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:A0A1L8HCK2}. Note=Partially colocalized with SASS6 in cytoplasmic puncta, suggesting a centrosomal localization. {ECO:0000250|UniProtKB:Q5U3Z0}. SUBUNIT: Interacts with ZMYND10. {ECO:0000250|UniProtKB:P57076}. +Q9DAN9 CF97D_MOUSE Uncharacterized protein CFAP97D1 (CFAP97 domain-containing protein 1) 164 19,775 Chain (1); Coiled coil (1) +Q64676 CGT_MOUSE 2-hydroxyacylsphingosine 1-beta-galactosyltransferase (EC 2.4.1.47) (Ceramide UDP-galactosyltransferase) (Cerebroside synthase) (UDP-galactose-ceramide galactosyltransferase) 541 61,249 Chain (1); Glycosylation (3); Sequence conflict (11); Signal peptide (1); Transmembrane (1) TRANSMEM 472 492 Helical. {ECO:0000255}. Sphingolipid metabolism; galactosylceramide biosynthesis. FUNCTION: Catalyzes the transfer of galactose to ceramide, a key enzymatic step in the biosynthesis of galactocerebrosides, which are abundant sphingolipids of the myelin membrane of the central nervous system and peripheral nervous system. {ECO:0000250|UniProtKB:Q09426}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q9D9C7 CC062_MOUSE Uncharacterized protein C3orf62 homolog 252 28,535 Chain (1); Compositional bias (1); Modified residue (2); Sequence conflict (1) +Q3ULW6 CCD33_MOUSE Coiled-coil domain-containing protein 33 (Speriolin-binding factor) 985 110,198 Alternative sequence (10); Chain (1); Coiled coil (2); Domain (1); Sequence conflict (18) +Q9CZH8 CCD77_MOUSE Coiled-coil domain-containing protein 77 489 57,569 Alternative sequence (1); Chain (1); Coiled coil (2); Modified residue (1); Sequence conflict (4) +Q8CDL9 CCD87_MOUSE Coiled-coil domain-containing protein 87 855 98,467 Chain (1); Coiled coil (2); Sequence conflict (2) FUNCTION: Plays a role in spermatogenesis, where it is important for normal sperm head morphology. Also required for the acrosome reaction and thus normal male fertility. {ECO:0000269|PubMed:29733332}. TISSUE SPECIFICITY: Specifically expressed in testis (at protein level). Not detected in other tissues tested (at protein level). In the testis, localizes to pachytene spermatocytes and spermatids. {ECO:0000269|PubMed:29733332}. +Q9Z121 CCL8_MOUSE C-C motif chemokine 8 (Monocyte chemoattractant protein 2) (Monocyte chemotactic protein 2) (MCP-2) (Small-inducible cytokine A8) 97 11,017 Chain (1); Disulfide bond (2); Signal peptide (1) FUNCTION: Chemotactic factor that attracts monocytes. This protein can bind heparin (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Monomer or homodimer; in equilibrium. {ECO:0000250}. +Q64314 CD34_MOUSE Hematopoietic progenitor cell antigen CD34 (CD antigen CD34) 382 40,983 Alternative sequence (2); Chain (1); Glycosylation (7); Modified residue (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 288 308 Helical. {ECO:0000255}. TOPO_DOM 35 287 Extracellular. {ECO:0000255}.; TOPO_DOM 309 382 Cytoplasmic. {ECO:0000255}. FUNCTION: Possible adhesion molecule with a role in early hematopoiesis by mediating the attachment of stem cells to the bone marrow extracellular matrix or directly to stromal cells. Could act as a scaffold for the attachment of lineage specific glycans, allowing stem cells to bind to lectins expressed by stromal cells or other marrow components. Presents carbohydrate ligands to selectins (By similarity). {ECO:0000250}. PTM: Highly glycosylated. {ECO:0000250}.; PTM: Phosphorylated on serine residues by PKC. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. TISSUE SPECIFICITY: Highly expressed in hematopoietic progenitor cell lines, brain and testis, and moderately in the thymus, spleen, and bone marrow, but not in adult liver. +P15530 CD79B_MOUSE B-cell antigen receptor complex-associated protein beta chain (B-cell-specific glycoprotein B29) (Ig-beta) (Immunoglobulin-associated B29 protein) (CD antigen CD79b) 228 25,726 Beta strand (10); Chain (1); Disulfide bond (3); Domain (2); Glycosylation (3); Helix (1); Modified residue (2); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 159 180 Helical. {ECO:0000255}. TOPO_DOM 26 158 Extracellular. {ECO:0000255}.; TOPO_DOM 181 228 Cytoplasmic. {ECO:0000255}. FUNCTION: Required in cooperation with CD79A for initiation of the signal transduction cascade activated by the B-cell antigen receptor complex (BCR) which leads to internalization of the complex, trafficking to late endosomes and antigen presentation. Enhances phosphorylation of CD79A, possibly by recruiting kinases which phosphorylate CD79A or by recruiting proteins which bind to CD79A and protect it from dephosphorylation. {ECO:0000269|PubMed:10352267, ECO:0000269|PubMed:12356683, ECO:0000269|PubMed:15661879, ECO:0000269|PubMed:8175787}. PTM: Phosphorylated on tyrosine upon B-cell activation by SRC-type Tyr-kinases such as BLK, LYN and SYK. {ECO:0000269|PubMed:15335855, ECO:0000269|PubMed:7592958}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10587346, ECO:0000269|PubMed:11238609, ECO:0000269|PubMed:15661879}; Single-pass type I membrane protein {ECO:0000269|PubMed:10587346, ECO:0000269|PubMed:11238609, ECO:0000269|PubMed:15661879}. Note=Following antigen binding, the BCR has been shown to translocate from detergent-soluble regions of the cell membrane to lipid rafts although signal transduction through the complex can also occur outside lipid rafts. SUBUNIT: Heterodimer of alpha and beta chains; disulfide-linked. Part of the B-cell antigen receptor complex where the alpha/beta chain heterodimer is non-covalently associated with an antigen-specific membrane-bound surface immunoglobulin of two heavy chains and two light chains. Interacts with LYN. {ECO:0000269|PubMed:1506682, ECO:0000269|PubMed:15335855, ECO:0000269|PubMed:20696394, ECO:0000269|PubMed:7592958}. TISSUE SPECIFICITY: B-cells. +Q91V98 CD248_MOUSE Endosialin (Tumor endothelial marker 1) (CD antigen CD248) 765 81,813 Chain (1); Compositional bias (1); Disulfide bond (6); Domain (3); Glycosylation (30); Modified residue (1); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 696 716 Helical. {ECO:0000255}. TOPO_DOM 18 695 Extracellular. {ECO:0000255}.; TOPO_DOM 717 765 Cytoplasmic. {ECO:0000255}. FUNCTION: May play a role in angiogenesis or vascular function. {ECO:0000269|PubMed:11489895}. PTM: O-glycosylated by sialylated oligosaccharides. {ECO:0000250}.; PTM: May be N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in cell lines derived from endothelial cells, embryonic fibroblasts and preadipocytes. {ECO:0000269|PubMed:11489895}. +P25918 CD19_MOUSE B-lymphocyte antigen CD19 (Differentiation antigen CD19) (CD antigen CD19) 547 60,149 Chain (1); Disulfide bond (3); Domain (2); Glycosylation (7); Modified residue (7); Propeptide (1); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 288 311 Helical. {ECO:0000255}. TOPO_DOM 19 287 Extracellular. {ECO:0000255}.; TOPO_DOM 312 547 Cytoplasmic. {ECO:0000255}. FUNCTION: Functions as coreceptor for the B-cell antigen receptor complex (BCR) on B-lymphocytes. Decreases the threshold for activation of downstream signaling pathways and for triggering B-cell responses to antigens (By similarity). Activates signaling pathways that lead to the activation of phosphatidylinositol 3-kinase and the mobilization of intracellular Ca(2+) stores (PubMed:9382888, PubMed:12387743, PubMed:20101619). Is not required for early steps during B cell differentiation in the blood marrow (PubMed:7542548, PubMed:7543183, PubMed:9317126). Required for normal differentiation of B-1 cells (PubMed:7542548, PubMed:7543183, PubMed:12387743). Required for normal B cell differentiation and proliferation in response to antigen challenges (PubMed:7542548, PubMed:9317126, PubMed:12387743). Required for normal levels of serum immunoglobulins, and for production of high-affinity antibodies in response to antigen challenge (PubMed:7542548, PubMed:7543183, PubMed:12387743). {ECO:0000250|UniProtKB:P15391, ECO:0000269|PubMed:12387743, ECO:0000269|PubMed:20101619, ECO:0000269|PubMed:7542548, ECO:0000269|PubMed:7543183, ECO:0000269|PubMed:9317126, ECO:0000269|PubMed:9382888}. PTM: Phosphorylated on tyrosine following B-cell activation (PubMed:20101619). Phosphorylated on tyrosine residues by LYN (By similarity). Tyrosine residues are phosphorylated sequentially after activation of the B cell receptor. Phosphorylation of Tyr-522 is extremely rapid, followed by phosphorylation at Tyr-402. In contrast, phosphorylation of Tyr-493 appears more slowly and is more transient, returning rapidly to basal levels (PubMed:20101619). {ECO:0000250|UniProtKB:P15391, ECO:0000269|PubMed:20101619}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12387743, ECO:0000269|PubMed:20101619, ECO:0000269|PubMed:7543183}; Single-pass type I membrane protein {ECO:0000305}. Membrane raft {ECO:0000269|PubMed:20101619}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Interacts with CR2/CD21. Part of a complex composed of CD19, CR2/CD21, CD81 and IFITM1/CD225 in the membrane of mature B-cells. Interacts with VAV. Interacts with GRB2 and SOS when phosphorylated on Tyr-346 and/or Tyr-376. Interacts with PLCG2 when phosphorylated on Tyr-402. Interacts with LYN. Interacts (when tyrosine phosphorylated) with the regulatory p85 subunit of phosphatidylinositol 3-kinase (PIK3R1 or PIK3R2). {ECO:0000250|UniProtKB:P15391}. TISSUE SPECIFICITY: Detected on B cells in spleen, bone marrow, thymus and lymph nodes (PubMed:12387743, PubMed:7542548, PubMed:20101619). Detected on peripheral blood lymphocytes (at protein level) (PubMed:7543183). {ECO:0000269|PubMed:12387743, ECO:0000269|PubMed:20101619, ECO:0000269|PubMed:7542548, ECO:0000269|PubMed:7543183}. +Q9CZP7 CD37L_MOUSE Hsp90 co-chaperone Cdc37-like 1 335 38,439 Alternative sequence (6); Chain (1); Coiled coil (1); Modified residue (2); Region (4); Sequence conflict (1) FUNCTION: Co-chaperone that binds to numerous proteins and promotes their interaction with Hsp70 and Hsp90. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Self-associates. Forms complexes with Hsp70 and Hsp90. Interacts with CDC37, FKBP4, PPID and STIP1. {ECO:0000250}. +P56528 CD38_MOUSE ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1 (EC 3.2.2.6) (2'-phospho-ADP-ribosyl cyclase) (2'-phospho-ADP-ribosyl cyclase/2'-phospho-cyclic-ADP-ribose transferase) (EC 2.4.99.20) (2'-phospho-cyclic-ADP-ribose transferase) (ADP-ribosyl cyclase 1) (ADPRC 1) (Cyclic ADP-ribose hydrolase 1) (cADPr hydrolase 1) (I-19) (NIM-R5 antigen) (CD antigen CD38) 304 34,408 Active site (2); Beta strand (4); Chain (1); Disulfide bond (5); Glycosylation (4); Helix (12); Sequence conflict (2); Topological domain (2); Transmembrane (1); Turn (2) TRANSMEM 22 44 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 21 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 45 304 Extracellular. {ECO:0000255}. FUNCTION: Synthesizes the second messagers cyclic ADP-ribose and nicotinate-adenine dinucleotide phosphate, the former a second messenger for glucose-induced insulin secretion. Also has cADPr hydrolase activity (By similarity). {ECO:0000250, ECO:0000269|PubMed:11829748}. SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. +P04235 CD3D_MOUSE T-cell surface glycoprotein CD3 delta chain (T-cell receptor T3 delta chain) (CD antigen CD3d) 173 19,032 Chain (1); Disulfide bond (1); Domain (1); Glycosylation (3); Modified residue (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 106 126 Helical. {ECO:0000255}. TOPO_DOM 22 105 Extracellular. {ECO:0000255}.; TOPO_DOM 127 173 Cytoplasmic. {ECO:0000255}. FUNCTION: Part of the TCR-CD3 complex present on T-lymphocyte cell surface that plays an essential role in adaptive immune response. When antigen presenting cells (APCs) activate T-cell receptor (TCR), TCR-mediated signals are transmitted across the cell membrane by the CD3 chains CD3D, CD3E, CD3G and CD3Z. All CD3 chains contain immunoreceptor tyrosine-based activation motifs (ITAMs) in their cytoplasmic domain. Upon TCR engagement, these motifs become phosphorylated by Src family protein tyrosine kinases LCK and FYN, resulting in the activation of downstream signaling pathways. In addition of this role of signal transduction in T-cell activation, CD3D plays an essential role in thymocyte differentiation. Indeed, participates in correct intracellular TCR-CD3 complex assembly and surface expression. In absence of a functional TCR-CD3 complex, thymocytes are unable to differentiate properly (PubMed:10935641). Interacts with CD4 and CD8 and thus serves to establish a functional link between the TCR and coreceptors CD4 and CD8, which is needed for activation and positive selection of CD4 or CD8 T-cells. {ECO:0000250|UniProtKB:P04234, ECO:0000269|PubMed:10935641}. PTM: Phosphorylated on Tyr residues after T-cell receptor triggering by LCK in association with CD4/CD8. {ECO:0000250|UniProtKB:P04234}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: The TCR-CD3 complex is composed of a CD3D/CD3E and a CD3G/CD3E heterodimers that preferentially associate with TCRalpha and TCRbeta, respectively, to form TCRalpha/CD3E/CD3G and TCRbeta/CD3G/CD3E trimers. In turn, the hexamer interacts with CD3Z homodimer to form the TCR-CD3 complex. Alternatively, TCRalpha and TCRbeta can be replaced by TCRgamma and TCRdelta. Interacts with coreceptors CD4 and CD8. {ECO:0000250|UniProtKB:P04234, ECO:0000269|PubMed:15459203}. +P18181 CD48_MOUSE CD48 antigen (BCM1 surface antigen) (BLAST-1) (HM48-1) (MRC OX-45 surface antigen) (SLAM family member 2) (SLAMF2) (Signaling lymphocytic activation molecule 2) (sgp-60) (CD antigen CD48) 240 27,383 Beta strand (9); Chain (1); Disulfide bond (1); Domain (2); Glycosylation (6); Helix (1); Lipidation (1); Propeptide (1); Signal peptide (1); Turn (2) FUNCTION: Ligand for CD2. Might facilitate interaction between activated lymphocytes. Probably involved in regulating T-cell activation. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1383383}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:1693656}. SUBUNIT: Interacts with CD2 (PubMed:1383383). Interacts with CD244 in a heterophilic manner (PubMed:17950006). {ECO:0000269|PubMed:1383383, ECO:0000269|PubMed:17950006}. +P31996 CD68_MOUSE Macrosialin (CD antigen CD68) 326 34,818 Alternative sequence (1); Chain (1); Compositional bias (1); Disulfide bond (2); Erroneous gene model prediction (1); Glycosylation (9); Region (1); Repeat (4); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 292 316 Helical. {ECO:0000255|PROSITE-ProRule:PRU00740}. TOPO_DOM 21 291 Extracellular. {ECO:0000255}.; TOPO_DOM 317 326 Cytoplasmic. {ECO:0000255|PROSITE-ProRule:PRU00740}. FUNCTION: Could play a role in phagocytic activities of tissue macrophages, both in intracellular lysosomal metabolism and extracellular cell-cell and cell-pathogen interactions. Binds to tissue- and organ-specific lectins or selectins, allowing homing of macrophage subsets to particular sites. Rapid recirculation of CD68 from endosomes and lysosomes to the plasma membrane may allow macrophages to crawl over selectin-bearing substrates or other cells. PTM: N- and O-glycosylated. SUBCELLULAR LOCATION: Isoform Long: Endosome membrane; Single-pass type I membrane protein. Lysosome membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Isoform Short: Cell membrane; Single-pass type I membrane protein. TISSUE SPECIFICITY: Expressed in tissue macrophages and to a lesser extent in dendritic cells. +Q9Z0M6 CD97_MOUSE CD97 antigen (CD antigen CD97) [Cleaved into: CD97 antigen subunit alpha; CD97 antigen subunit beta] 818 90,413 Alternative sequence (2); Chain (3); Disulfide bond (12); Domain (5); Glycosylation (7); Modified residue (5); Sequence conflict (8); Signal peptide (1); Site (1); Topological domain (8); Transmembrane (7) TRANSMEM 534 554 Helical; Name=1. {ECO:0000255}.; TRANSMEM 563 583 Helical; Name=2. {ECO:0000255}.; TRANSMEM 603 623 Helical; Name=3. {ECO:0000255}.; TRANSMEM 638 658 Helical; Name=4. {ECO:0000255}.; TRANSMEM 680 700 Helical; Name=5. {ECO:0000255}.; TRANSMEM 724 744 Helical; Name=6. {ECO:0000255}.; TRANSMEM 753 773 Helical; Name=7. {ECO:0000255}. TOPO_DOM 24 533 Extracellular. {ECO:0000255}.; TOPO_DOM 555 562 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 584 602 Extracellular. {ECO:0000255}.; TOPO_DOM 624 637 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 659 679 Extracellular. {ECO:0000255}.; TOPO_DOM 701 723 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 745 752 Extracellular. {ECO:0000255}.; TOPO_DOM 774 818 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor potentially involved in both adhesion and signaling processes early after leukocyte activation. Plays an essential role in leukocyte migration. {ECO:0000269|PubMed:14707087}. PTM: Proteolytically cleaved into 2 subunits, an extracellular alpha subunit and a seven-transmembrane subunit. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10540231}; Multi-pass membrane protein {ECO:0000269|PubMed:10540231}. SUBUNIT: Forms a heterodimer, consisting of a large extracellular region (alpha subunit) non-covalently linked to a seven-transmembrane moiety (beta subunit). Interacts with complement decay-accelerating factor (DAF). The largest isoform (isoform 1) do not interact with DAF. Interacts also with chondroitin sulfate (By similarity). {ECO:0000250}. DOMAIN: The first two EGF domains mediate the interaction with DAF. A third tandemly arranged EGF domain is necessary for the structural integrity of the binding region (By similarity). {ECO:0000250}.; DOMAIN: Binding to chondroitin sulfate is mediated by the fourth EGF domain. {ECO:0000250}. TISSUE SPECIFICITY: Although predominantly expressed by cells of the immune system is expressed ubiquitously, with particularly high levels of expression in the lung and the thymus gland. In the spleen, expression is detected on most myeloid cells and variable portions of T-cells, B-cells and NK cells. In the bone marrow, expressed in nearly all myeloid cells, whereas little if any expression is found on erythroid cells. +Q9DB75 CDIP1_MOUSE Cell death-inducing p53-target protein 1 (LITAF-like protein) 208 21,835 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (1); Metal binding (4); Region (1); Sequence conflict (2) FUNCTION: Acts as an important p53/TP53-apoptotic effector. Regulates TNF-alpha-mediated apoptosis in a p53/TP53-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q9H305}. SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250|UniProtKB:Q9H305}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9H305}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9H305}. Lysosome membrane {ECO:0000250|UniProtKB:Q9H305}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9H305}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9H305}. DOMAIN: The LITAF domain is stabilized by a bound zinc ion. The LITAF domain contains an amphiphatic helix that mediates interaction with lipid membranes. {ECO:0000250|UniProtKB:Q99732}. +Q04899 CDK18_MOUSE Cyclin-dependent kinase 18 (EC 2.7.11.22) (Cell division protein kinase 18) (PCTAIRE-motif protein kinase 3) (Serine/threonine-protein kinase PCTAIRE-3) 451 51,848 Active site (1); Binding site (1); Chain (1); Domain (1); Modified residue (7); Nucleotide binding (1) FUNCTION: May play a role in signal transduction cascades in terminally differentiated cells. TISSUE SPECIFICITY: In brain, kidney, intestine and at a much lower level, in fetal tissues. +Q99M54 CDCA3_MOUSE Cell division cycle-associated protein 3 (Gene-rich cluster protein C8) (Trigger of mitotic entry protein 1) (TOME-1) 266 28,708 Alternative sequence (2); Chain (1); Erroneous initiation (1); Modified residue (11); Motif (1); Region (1); Sequence conflict (2) Protein modification; protein ubiquitination. FUNCTION: F-box-like protein which is required for entry into mitosis. Acts by participating in E3 ligase complexes that mediate the ubiquitination and degradation of WEE1 kinase at G2/M phase (By similarity). {ECO:0000250}. PTM: Ubiquitinated and degraded by the APC/C-Cdh1 complex. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. SUBUNIT: Interacts with SKP1. Part of a SCF (SKP1-cullin-F-box) protein ligase complex. {ECO:0000269|PubMed:12679038}. DOMAIN: The KEN box is required for the association with the APC/C-Cdh1 complex. {ECO:0000250}. +P56389 CDD_MOUSE Cytidine deaminase (EC 3.5.4.5) (Cytidine aminohydrolase) 146 16,131 Active site (1); Beta strand (6); Chain (1); Domain (1); Helix (6); Metal binding (3); Region (1); Turn (1) FUNCTION: This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis. {ECO:0000250}. SUBUNIT: Homotetramer. {ECO:0000269|PubMed:16784234}. +Q9Z1X9 CDC45_MOUSE Cell division control protein 45 homolog (PORC-PI-1) 566 65,384 Chain (1); Modified residue (3); Sequence conflict (9) FUNCTION: Required for initiation of chromosomal DNA replication. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Associated with ORC2. Interacts with HELB. {ECO:0000250|UniProtKB:O75419}. TISSUE SPECIFICITY: Widely expressed. +Q3UMM4 CDK10_MOUSE Cyclin-dependent kinase 10 (EC 2.7.11.22) (Cell division protein kinase 10) 360 40,961 Active site (1); Binding site (1); Chain (1); Domain (1); Modified residue (1); Nucleotide binding (1) FUNCTION: Cyclin-dependent kinase that phosphorylates the transcription factor ETS2 (in vitro) and positively controls its proteasomal degradation (in cells). Involved in the regulation of actin cytoskeleton organization through the phosphorylation of actin dynamics regulators such as PKN2. Is a negative regulator of ciliogenesis through phosphorylation of PKN2 and promotion of RhoA signaling. {ECO:0000250|UniProtKB:Q15131}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q15131}. SUBUNIT: Heterodimer with CCNQ, the interaction is required for kinase activity. Interacts with ETS2. Interacts with PRK2. {ECO:0000250|UniProtKB:Q15131}. +P43241 CDX2_MOUSE Homeobox protein CDX-2 (Caudal-type homeobox protein 2) 311 33,476 Chain (1); Compositional bias (3); DNA binding (1); Modified residue (1); Region (2); Sequence conflict (1) FUNCTION: Involved in the transcriptional regulation of multiple genes expressed in the intestinal epithelium. Important in broad range of functions from early differentiation to maintenance of the intestinal epithelial lining of both the small and large intestine. Binds preferentially to methylated DNA. {ECO:0000250|UniProtKB:Q99626}. PTM: Phosphorylation of Ser-60 mediates the transactivation capacity. {ECO:0000269|PubMed:11729123}. SUBCELLULAR LOCATION: Nucleus. TISSUE SPECIFICITY: Intestine; expressed specifically in gut epithelium where it is not restricted to a particular cell lineage. Abundant expression is seen in the proximal colon with slightly lower levels in distal colon. Expression in the proximal colon is not restricted either to a particular cell lineage or stage of differentiation while in the distal colon it is more abundant in the differentiated cells towards the top of the crypt. +Q9D5R3 CEP83_MOUSE Centrosomal protein of 83 kDa (Cep83) (Coiled-coil domain-containing protein 41) 692 81,998 Alternative sequence (1); Chain (1); Coiled coil (2); Modified residue (1); Sequence conflict (1) FUNCTION: Component of the distal appendage region of the centriole involved in the initiation of primary cilium assembly. May collaborate with IFT20 in the trafficking of ciliary membrane proteins from the Golgi complex to the cilium during the initiation of primary cilium assembly. {ECO:0000269|PubMed:23348840}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q9Y592}. Note=Localizes specifically to the distal appendage region of the centriole, which anchors the mother centriole to the plasma membrane. Localizes to centrioles at all stages of the cell cycle, including mitosis. {ECO:0000250|UniProtKB:Q9Y592}. SUBUNIT: Interacts with CEP164 and IFT20. {ECO:0000250|UniProtKB:Q9Y592}. +Q924Z4 CERS2_MOUSE Ceramide synthase 2 (CerS2) (LAG1 longevity assurance homolog 2) (Translocating chain-associating membrane protein homolog 3) (TRAM homolog 3) 380 45,024 Chain (1); DNA binding (1); Domain (1); Glycosylation (1); Modified residue (4); Topological domain (7); Transmembrane (6) TRANSMEM 41 61 Helical. {ECO:0000255}.; TRANSMEM 140 160 Helical. {ECO:0000255}.; TRANSMEM 175 195 Helical. {ECO:0000255}.; TRANSMEM 209 229 Helical. {ECO:0000255}.; TRANSMEM 264 284 Helical. {ECO:0000255}.; TRANSMEM 304 324 Helical. {ECO:0000255}. TOPO_DOM 1 40 Lumenal. {ECO:0000255}.; TOPO_DOM 62 139 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 161 174 Lumenal. {ECO:0000255}.; TOPO_DOM 196 208 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 230 263 Lumenal. {ECO:0000255}.; TOPO_DOM 285 303 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 325 380 Lumenal. {ECO:0000255}. FUNCTION: Suppresses the growth of cancer cells. May be involved in sphingolipid synthesis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000255|PROSITE-ProRule:PRU00108}; Multi-pass membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:15823095}; Multi-pass membrane protein {ECO:0000269|PubMed:15823095}. SUBUNIT: Interacts with ATP6V0C, ASGR1, ASGR2 and SLC22A1/OCT1. {ECO:0000250}. TISSUE SPECIFICITY: Broadly expressed, with highest levels in liver and kidney. {ECO:0000269|PubMed:15823095}. +Q9D6J1 CERS4_MOUSE Ceramide synthase 4 (CerS4) (LAG1 longevity assurance homolog 4) (Translocating chain-associating membrane protein homolog 1) (TRAM homolog 1) 393 46,017 Chain (1); DNA binding (1); Domain (1); Modified residue (3); Sequence conflict (2); Transmembrane (6) TRANSMEM 32 52 Helical. {ECO:0000255}.; TRANSMEM 140 160 Helical. {ECO:0000255}.; TRANSMEM 179 199 Helical. {ECO:0000255}.; TRANSMEM 217 237 Helical. {ECO:0000255}.; TRANSMEM 265 285 Helical. {ECO:0000255}.; TRANSMEM 304 324 Helical. {ECO:0000255}. FUNCTION: May be either a bona fide (dihydro)ceramide synthase or a modulator of its activity. When overexpressed in cells is involved in the production of sphingolipids containing different fatty acid donors (N-linked stearoyl- (C18) or arachidoyl- (C20) ceramides) in a fumonisin B1-independent manner. {ECO:0000269|PubMed:12912983}. SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000255|PROSITE-ProRule:PRU00108}; Multi-pass membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:12912983}; Multi-pass membrane protein {ECO:0000269|PubMed:12912983}. TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in skin. {ECO:0000269|PubMed:12912983, ECO:0000269|PubMed:15823095}. +Q9CQF4 CF203_MOUSE Uncharacterized protein C6orf203 homolog 240 27,847 Chain (1); Compositional bias (1); Modified residue (2) +P04186 CFAB_MOUSE Complement factor B (EC 3.4.21.47) (C3/C5 convertase) [Cleaved into: Complement factor B Ba fragment; Complement factor B Bb fragment] 761 85,004 Active site (3); Chain (3); Disulfide bond (8); Domain (5); Glycosylation (4); Sequence conflict (2); Signal peptide (1) FUNCTION: Factor B which is part of the alternate pathway of the complement system is cleaved by factor D into 2 fragments: Ba and Bb. Bb, a serine protease, then combines with complement factor 3b to generate the C3 or C5 convertase. SUBCELLULAR LOCATION: Secreted. DOMAIN: The unliganded VWA domain has an inactive 'locked' conformation whereby the scissile Arg-256|Lys-257 bond is protected from proteolytic activation. {ECO:0000250}. +Q9Z1R4 CF047_MOUSE Uncharacterized protein C6orf47 homolog 293 32,015 Chain (1); Modified residue (3) +Q66JV7 CH058_MOUSE Uncharacterized protein C8orf58 homolog 365 40,582 Alternative sequence (1); Chain (1); Erroneous initiation (1); Sequence conflict (2) +Q8VE95 CH082_MOUSE UPF0598 protein C8orf82 homolog 218 24,330 Chain (1); Sequence conflict (1) +Q8BMJ7 CGRF1_MOUSE Cell growth regulator with RING finger domain protein 1 (Cell growth regulatory gene 19 protein) 332 37,899 Chain (1); Sequence conflict (1); Zinc finger (1) FUNCTION: Able to inhibit growth in several cell lines. {ECO:0000250|UniProtKB:P97587}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q99675}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q99675}. +Q9D5Y0 CG031_MOUSE Uncharacterized protein C7orf31 homolog (Protein TISP74) 588 67,661 Chain (1); Erroneous initiation (1); Modified residue (8); Sequence conflict (1) SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q8N865}. +Q64433 CH10_MOUSE 10 kDa heat shock protein, mitochondrial (Hsp10) (10 kDa chaperonin) (Chaperonin 10) (CPN10) 102 10,963 Chain (1); Initiator methionine (1); Modified residue (22) FUNCTION: Co-chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp60, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein. {ECO:0000250|UniProtKB:P61604}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:P61604}. SUBUNIT: Homoheptamer arranged in a ring structure. 2 heptameric Hsp10 rings interact with a Hsp60 tetradecamer in the structure of a back-to-back double heptameric ring to form the symmetrical football complex. {ECO:0000250|UniProtKB:P61604}. +P00186 CP1A2_MOUSE Cytochrome P450 1A2 (EC 1.14.14.1) (CYPIA2) (Cholesterol 25-hydroxylase) (Cytochrome P450-P2) (Cytochrome P450-P3) 513 58,184 Binding site (1); Chain (1); Glycosylation (1); Initiator methionine (1); Metal binding (1); Natural variant (1) FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. Most active in catalyzing 2-hydroxylation. {ECO:0000250|UniProtKB:P05177}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane {ECO:0000250|UniProtKB:P05177}; Peripheral membrane protein. +Q9D4A5 CP086_MOUSE Uncharacterized protein C16orf86 homolog 307 32,427 Alternative sequence (1); Chain (1) +Q9CR55 CP087_MOUSE UPF0547 protein C16orf87 homolog 154 17,829 Chain (1); Coiled coil (1); Modified residue (1) +Q99N16 CP4F3_MOUSE Leukotriene-B(4) omega-hydroxylase 2 (EC 1.14.14.94) (CYPIVF3) (Cytochrome P450 4F3) (Cytochrome P450-LTB-omega) (Leukotriene-B(4) 20-monooxygenase 2) 524 59,843 Chain (1); Metal binding (1); Sequence conflict (9); Transmembrane (1) TRANSMEM 15 35 Helical. {ECO:0000255}. Lipid metabolism; leukotriene B4 degradation. FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. Catalyzes the omega-hydroxylation of LTB4, a potent chemoattractant for polymorphonuclear leukocytes. {ECO:0000250|UniProtKB:Q08477, ECO:0000269|PubMed:16380383}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Microsome membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Highest level in polymorphonuclear leukocytes and dendritic cells. Detectable in lymph nodes, spleen, bone marrow and peripheral blood. Highly expressed in ovary. Very low level in liver, kidney, and smooth muscle. {ECO:0000269|PubMed:16380383}. +P56654 CP237_MOUSE Cytochrome P450 2C37 (EC 1.14.14.1) (CYPIIC37) 490 55,606 Chain (1); Metal binding (1); Modified residue (3); Sequence conflict (18) FUNCTION: Metabolizes arachidonic acid to produce 12-hydroxyeicosatetraenoic acid (HETE). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. TISSUE SPECIFICITY: Liver. +P56656 CP239_MOUSE Cytochrome P450 2C39 (EC 1.14.14.1) (CYPIIC39) 490 55,827 Chain (1); Metal binding (1); Sequence conflict (9) FUNCTION: Metabolizes arachidonic acid to produce 14,15-cis-epoxyeicosatrienoic acid (EET). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. TISSUE SPECIFICITY: Liver. +P56657 CP240_MOUSE Cytochrome P450 2C40 (EC 1.14.14.1) (CYPIIC40) 491 55,763 Chain (1); Metal binding (1); Sequence conflict (1) FUNCTION: Metabolizes arachidonic acid to produce an unidentified metabolite that coelutes with 16-,17-, and 18-hydroxyeicosatetraenoic acid (HETE). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. TISSUE SPECIFICITY: Liver, brain, kidney, and intestine, with trace amounts in lung and heart. +Q60952 CP250_MOUSE Centrosome-associated protein CEP250 (250 kDa centrosomal protein) (Cep250) (Centrosomal Nek2-associated protein 1) (C-Nap1) (Centrosomal protein 2) (Intranuclear matrix protein) 2414 276,814 Chain (1); Coiled coil (6); Compositional bias (1); Frameshift (1); Modified residue (3); Sequence conflict (23) FUNCTION: Probably plays an important role in centrosome cohesion during interphase. {ECO:0000250}. PTM: C-terminal part is phosphorylated by NEK2. Dephosphorylated in vitro by the PP1 phosphatase (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:16339073}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:16339073}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:16339073}. Note=Component of the core centrosome where it is found at the proximal ends of centrioles. In photoreceptors, found at the proximal ends of basal bodies. SUBUNIT: Monomer and homodimer (Probable). Forms a complex in vitro with both NEK2 kinase and the PPP1CC catalytic subunit of protein phosphatase 1 (PP1) (By similarity). Interacts with CEP135 (By similarity). Interacts with CROCC/rootletin (PubMed:16339073). Interacts with CNTLN (By similarity). Interacts with NIN (via C-terminus) (PubMed:27565344). {ECO:0000250|UniProtKB:Q9BV73, ECO:0000269|PubMed:16339073, ECO:0000269|PubMed:27565344, ECO:0000305}. +Q9DBW0 CP4V2_MOUSE Cytochrome P450 4V2 (EC 1.14.14.-) (Docosahexaenoic acid omega-hydroxylase CYP4V2) (EC 1.14.14.79) 525 60,939 Binding site (1); Chain (1); Metal binding (1); Transmembrane (1) TRANSMEM 14 34 Helical. {ECO:0000255}. Lipid metabolism. FUNCTION: Omega-hydroxylase that oxidizes medium-chain saturated fatty acids and polyunsaturated omega-3 fatty acids, and which plays a role in fatty acid and steroid metabolism in the eye. Catalyzes the omega-hydroxylation of medium-chain saturated fatty acids such as laurate, myristate and palmitate in an NADPH-dependent pathway. The substrate specificity is higher for myristate > laurate > palmitate (C14>C16>C12). Acts as a polyunsaturated omega-3 fatty acids hydroxylase by mediating oxidation of docosahexaenoate (DHA) to 22-hydroxydocosahexaenoate. Also produces some 21-hydroxydocosahexaenoate. Also converts eicosapentaenoate (EPA) to 20-hydroxyeicosapentaenoate (20-OH-EPA). {ECO:0000250|UniProtKB:Q6ZWL3}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q6ZWL3}; Single-pass membrane protein {ECO:0000305}. +O88833 CP4AA_MOUSE Cytochrome P450 4A10 (CYPIVA10) (Cytochrome P450-LA-omega 1) (Cytochrome P452) (Lauric acid omega-hydroxylase) (Long-chain fatty acid omega-monooxygenase) (EC 1.14.14.80) 509 58,330 Binding site (1); Chain (1); Metal binding (1); Modified residue (1); Sequence conflict (8) FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. {ECO:0000305}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. +Q6A152 CP4X1_MOUSE Cytochrome P450 4X1 (EC 1.14.14.1) (CYPIVX1) 507 58,557 Chain (1); Metal binding (1); Sequence conflict (4); Transmembrane (1) TRANSMEM 14 34 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000305}. Microsome membrane {ECO:0000269|PubMed:16478468}. TISSUE SPECIFICITY: Expressed in brain and aorta. In the brain, expressed in the Purkinje cells of the cerebellum, pyramidal neurons in the dentate gyrus of the hippocampus, cortical forebrain neurons and those of brain stem nuclei (at protein level). In addition to neurons, also expressed in cerebral vascular endothelial cells (at protein level). Also expressed in epithelial cells of the choroid plexus (at protein level). Hardly detectable in heart, lung, kidney and spleen. {ECO:0000269|PubMed:16478468}. +P33267 CP2F2_MOUSE Cytochrome P450 2F2 (EC 1.14.14.-) (CYPIIF2) (Cytochrome P450-NAH-2) (Naphthalene dehydrogenase) (Naphthalene hydroxylase) 491 55,949 Chain (1); Metal binding (1) FUNCTION: Involved in the regio- and stereoselective transformation of naphthalene to trans-1R-hydroxy-2R-glutathionyl-1,2-dihydronaphthalene in the presence of glutathione and glutathione S-transferases. It specifically catalyzes the production of a very reactive and potentially toxic intermediate, the 2R,2S arene oxide, that is associated with necrosis of the unciliated bronchiolar epithelial cells or Clara cells in lung. {ECO:0000269|PubMed:1742282, ECO:0000269|PubMed:1981702}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. TISSUE SPECIFICITY: Clara cells in lung and liver. {ECO:0000269|PubMed:1742282, ECO:0000269|PubMed:1981702}. +Q1RLL3 CPNE9_MOUSE Copine-9 (Copine IX) 553 61,852 Chain (1); Compositional bias (2); Domain (3); Sequence conflict (2) FUNCTION: Probable calcium-dependent phospholipid-binding protein that may play a role in calcium-mediated intracellular processes. Plays a role in dendrite formation by melanocytes. {ECO:0000250|UniProtKB:Q8IYJ1, ECO:0000250|UniProtKB:Q99829}. +Q9DAQ5 CQ098_MOUSE Uncharacterized protein C17orf98 homolog 155 17,772 Chain (1); Frameshift (1) +Q7TN99 CPEB3_MOUSE Cytoplasmic polyadenylation element-binding protein 3 (CPE-BP3) (CPE-binding protein 3) (mCPEB-3) 716 78,335 Alternative sequence (5); Chain (1); Compositional bias (3); Domain (2); Erroneous initiation (1); Modified residue (6); Mutagenesis (2); Sequence conflict (2); Site (3) FUNCTION: Sequence-specific RNA-binding protein which acts as a translational repressor in the basal unstimulated state but, following neuronal stimulation, acts as a translational activator (PubMed:17024188, PubMed:26074072). In contrast to CPEB1, does not bind to the cytoplasmic polyadenylation element (CPE), a uridine-rich sequence element within the mRNA 3'-UTR, but binds to a U-rich loop within a stem-loop structure (PubMed:17024188). Required for the consolidation and maintenance of hippocampal-based long term memory (PubMed:26074003). In the basal state, binds to the mRNA 3'-UTR of the glutamate receptors GRIA1 and GRIA2 and negatively regulates their translation (PubMed:17024188, PubMed:22153079). Also represses the translation of DLG4, GRIN1 GRIN2A and GRIN2B (PubMed:24155305). When activated, acts as a translational activator of GRIA1 and GRIA2 (PubMed:22153079, PubMed:26074003). In the basal state, suppresses SUMO2 translation but activates it following neuronal stimulation (PubMed:26074071). Binds to the 3'-UTR of TRPV1 mRNA and represses TRPV1 translation which is required to maintain normal thermoception (PubMed:26915043). Binds actin mRNA, leading to actin translational repression in the basal state and to translational activation following neuronal stimulation (PubMed:26074072). Negatively regulates target mRNA levels by binding to TOB1 which recruits CNOT7/CAF1 to a ternary complex and this leads to target mRNA deadenylation and decay (By similarity). In addition to its role in translation, binds to and inhibits the transcriptional activation activity of STAT5B without affecting its dimerization or DNA-binding activity. This, in turn, represses transcription of the STAT5B target gene EGFR which has been shown to play a role in enhancing learning and memory performance (By similarity). In contrast to CPEB1, CPEB2 and CPEB4, not required for cell cycle progression (By similarity). {ECO:0000250|UniProtKB:Q8NE35, ECO:0000269|PubMed:17024188, ECO:0000269|PubMed:22153079, ECO:0000269|PubMed:22711986, ECO:0000269|PubMed:24155305, ECO:0000269|PubMed:26074003, ECO:0000269|PubMed:26074071, ECO:0000269|PubMed:26074072, ECO:0000269|PubMed:26915043}. PTM: Activated by NEURL1-mediated monoubiquitination, resulting in the growth of new dendritic spines and increased levels of GRIA1 and GRIA2. NEURL1-mediated monoubiquitination facilitates synaptic plasticity and hippocampal-dependent memory storage. {ECO:0000269|PubMed:22153079}.; PTM: Under basal unstimulated conditions when CPEB3 is mainly unaggregated, sumoylated and acts as a translational repressor. Following neuronal stimulation, becomes desumoylated and aggregated which is required for the translation of mRNA targets and for dendritic filopodia formation. {ECO:0000269|PubMed:26074071}.; PTM: Following neuronal stimulation, cleaved by CAPN2 which abolishes its translational repressor activity, leading to translation of CPEB3 target mRNAs. {ECO:0000269|PubMed:22711986}.; PTM: Phosphorylation is enhanced by neuronal stimulation. {ECO:0000269|PubMed:26915047}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22711986}. Nucleus {ECO:0000269|PubMed:22711986}. Cell junction, synapse {ECO:0000269|PubMed:17024188}. Cell projection, dendrite {ECO:0000269|PubMed:17024188, ECO:0000269|PubMed:22153079, ECO:0000269|PubMed:22711986}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000269|PubMed:17024188}. Note=Predominantly cytoplasmic in unstimulated neurons but translocates to the nucleus following neuronal stimulation (PubMed:22711986). Nuclear import is mediated by importin IPO5 (PubMed:22730302). {ECO:0000269|PubMed:22711986, ECO:0000269|PubMed:22730302}. SUBUNIT: Following synaptic activity, aggregates to form amyloid-like oligomers (PubMed:26074003, PubMed:26074072). Aggregation requires an intact actin cytoskeleton (PubMed:26074072). Interacts with STAT5B; this inhibits STAT5B-mediated transcriptional activation (PubMed:20639532). Interacts with E3 ubiquitin-protein ligase NEURL1; this leads to monoubiquitination and activation of CPEB3 (PubMed:22153079). Interacts with CAPN2; this leads to cleavage of CPEB3 (PubMed:22711986). Interacts (via C-terminal RNA-binding region) with TOB1; TOB1 also binds CNOT7/CAF1 and recruits it to CPEB3 to form a ternary complex (By similarity). Interacts with SUMO-conjugating enzyme UBC9 (PubMed:26074071). Interacts with IPO5; the interaction is enhanced in a RAN-regulated manner following neuronal stimulation and mediates CPEB3 nuclear import (By similarity). Interacts with exportin XPO1/CRM1 (By similarity). {ECO:0000250|UniProtKB:Q8NE35, ECO:0000269|PubMed:20639532, ECO:0000269|PubMed:22153079, ECO:0000269|PubMed:22711986, ECO:0000269|PubMed:26074003, ECO:0000269|PubMed:26074071, ECO:0000269|PubMed:26074072}. DOMAIN: The N-terminal Gln-rich region is required for the formation of amyloid-like oligomers and for the stability of long-term potentiation and spatial memory. {ECO:0000269|PubMed:26074003}. TISSUE SPECIFICITY: Highly expressed in brain (at protein level) (PubMed:17024188). In brain, expressed in the hippocampus, granule cells and interneurons of the cerebellum, and mitral cells of the olfactory bulb (at protein level) (PubMed:17024188). Detected in the spinal cord and in peripheral dorsal root ganglia (at protein level) (PubMed:26915043). In the retina, strongly expressed in the retinal ganglion layer and, to a lesser extent, in the inner margin of the inner nuclear layer with expression also detected in the inner and outer plexiform layers (at protein level) (PubMed:20003455). Highly expressed in brain and heart, less in liver, kidney, embryo, skeletal muscle, lung and ovary (PubMed:12871996). Weakly expressed in granular cells of dentate gyrus and the pyramidal cells of CA3 and CA1 of the hippocampus (PubMed:12871996). {ECO:0000269|PubMed:12871996, ECO:0000269|PubMed:17024188, ECO:0000269|PubMed:20003455, ECO:0000269|PubMed:26915043}. +Q9DBB9 CPN2_MOUSE Carboxypeptidase N subunit 2 (Carboxypeptidase N 83 kDa chain) (Carboxypeptidase N large subunit) (Carboxypeptidase N polypeptide 2) (Carboxypeptidase N regulatory subunit) 547 60,479 Chain (1); Domain (2); Erroneous initiation (2); Glycosylation (9); Repeat (12); Signal peptide (1) FUNCTION: The 83 kDa subunit binds and stabilizes the catalytic subunit at 37 degrees Celsius and keeps it in circulation. Under some circumstances it may be an allosteric modifier of the catalytic subunit (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Tetramer of two catalytic chains and two glycosylated inactive chains. {ECO:0000250}. +Q8VHI4 CARTF_MOUSE Calcium-responsive transcription factor (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 8 protein) (Calcium-response factor) (CaRF) 689 76,397 Chain (1) FUNCTION: Acts as a transcriptional activator that mediates the calcium- and neuron-selective induction of BDNF exon III transcription. Binds to the consensus calcium-response element CaRE1 5'-CTATTTCGAG-3' sequence (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11832226}. DOMAIN: The N-terminus is necessary for DNA-binding. The C-terminus is necessary for transcriptional activation. TISSUE SPECIFICITY: Highly expressed in brain and testis. {ECO:0000269|PubMed:11832226}. +P56388 CART_MOUSE Cocaine- and amphetamine-regulated transcript protein [Cleaved into: CART(1-52); CART(55-102); CART(62-102)] 129 14,285 Alternative sequence (1); Chain (1); Disulfide bond (3); Modified residue (3); Peptide (3); Signal peptide (1) FUNCTION: Satiety factor closely associated with the actions of leptin and neuropeptide y; this anorectic peptide inhibits both normal and starvation-induced feeding and completely blocks the feeding response induced by neuropeptide Y and regulated by leptin in the hypothalamus. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q8BI72 CARF_MOUSE CDKN2A-interacting protein (Collaborator of ARF) 563 59,745 Chain (1); Compositional bias (1); Cross-link (1); Domain (2); Initiator methionine (1); Modified residue (5) FUNCTION: Regulates DNA damage response and cell proliferation in a dose-dependent manner through a number of signaling pathways involved in cell proliferation, apoptosis and senescence. {ECO:0000250|UniProtKB:Q9NXV6}. PTM: May be ubiquitinated. {ECO:0000250|UniProtKB:Q9NXV6}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9NXV6}. SUBUNIT: Interacts with CDKN2A/p14ARF, p53/TP53 and MDM2. Interacts with CHEK2 and MAPK3. Interacts with XRN2. {ECO:0000250|UniProtKB:Q9NXV6}. +O35177 CASL_MOUSE Enhancer of filamentation 1 (mEF1) (CRK-associated substrate-related protein) (CAS-L) (Neural precursor cell expressed developmentally down-regulated protein 9) (NEDD-9) (p105) 833 93,052 Chain (1); Domain (1); Modified residue (2); Motif (1); Region (1); Sequence conflict (17) FUNCTION: Docking protein which plays a central coordinating role for tyrosine-kinase-based signaling related to cell adhesion. May function in transmitting growth control signals between focal adhesions at the cell periphery and the mitotic spindle in response to adhesion or growth factor signals initiating cell proliferation. May play an important role in integrin beta-1 or B cell antigen receptor (BCR) mediated signaling in B- and T-cells. Integrin beta-1 stimulation leads to recruitment of various proteins including CRK, NCK and SHPTP2 to the tyrosine phosphorylated form (By similarity). {ECO:0000250}. PTM: PTK2/FAK1 phosphorylates the protein at the YDYVHL motif (conserved among all cas proteins). The SRC family kinases (FYN, SRC, LCK and CRK) are recruited to the phosphorylated sites and can phosphorylate other tyrosine residues. Ligation of either integrin beta-1 or B-cell antigen receptor on tonsillar B-cells and B-cell lines promotes tyrosine phosphorylation and both integrin and BCR-mediated tyrosine phosphorylation requires an intact actin network. In fibroblasts transformation with oncogene v-ABL results in an increase in tyrosine phosphorylation. Transiently phosphorylated following CD3 cross-linking and this phosphorylated form binds to CRK and C3G. A mutant lacking the SH3 domain is phosphorylated upon CD3 cross-linking but not upon integrin beta-1 cross-linking. Tyrosine phosphorylation occurs upon stimulation of the G-protein coupled C1a calcitonin receptor. Calcitonin-stimulated tyrosine phosphorylation is mediated by calcium- and protein kinase C-dependent mechanisms and requires the integrity of the actin cytoskeleton. Phosphorylation at Ser-368 induces proteasomal degradation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Localizes to both the cell nucleus and the cell periphery. {ECO:0000250}. SUBUNIT: Homodimer. Can heterodimerize with HLH proteins ID2, E12, E47 and also with p130cas. Forms complexes in vivo with related adhesion focal tyrosine kinase (RAFTK), adapter protein CRKL and LYN kinase. Interacts with MICAL and TXNL4/DIM1 (By similarity). Interacts with BCAR3 and SH2D3C. {ECO:0000250, ECO:0000269|PubMed:10692442, ECO:0000269|PubMed:12517963}. +P48318 DCE1_MOUSE Glutamate decarboxylase 1 (EC 4.1.1.15) (67 kDa glutamic acid decarboxylase) (GAD-67) (Glutamate decarboxylase 67 kDa isoform) 593 66,648 Binding site (1); Chain (1); Modified residue (2); Region (1); Sequence conflict (8) FUNCTION: Catalyzes the production of GABA. SUBUNIT: Homodimer. {ECO:0000250}. +P70677 CASP3_MOUSE Caspase-3 (CASP-3) (EC 3.4.22.56) (Apopain) (Cysteine protease CPP32) (CPP-32) (LICE) (Protein Yama) (SREBP cleavage activity 1) (SCA-1) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12] 277 31,475 Active site (2); Chain (2); Modified residue (4); Propeptide (2); Sequence conflict (3) FUNCTION: Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Triggers cell adhesion in sympathetic neurons through RET cleavage (By similarity). Cleaves IL-1 beta between an Asp and an Ala, releasing the mature cytokine which is involved in a variety of inflammatory processes. {ECO:0000250}. PTM: Cleavage by granzyme B, caspase-6, caspase-8 and caspase-10 generates the two active subunits. Additional processing of the propeptides is likely due to the autocatalytic activity of the activated protease. Active heterodimers between the small subunit of caspase-7 protease and the large subunit of caspase-3 also occur and vice versa (By similarity). {ECO:0000250}.; PTM: S-nitrosylated on its catalytic site cysteine in unstimulated human cell lines and denitrosylated upon activation of the Fas apoptotic pathway, associated with an increase in intracellular caspase activity. Fas therefore activates caspase-3 not only by inducing the cleavage of the caspase zymogen to its active subunits, but also by stimulating the denitrosylation of its active site thiol (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a 17 kDa (p17) and a 12 kDa (p12) subunit. Interacts with BIRC6/bruce. {ECO:0000250}. TISSUE SPECIFICITY: Highest expression in spleen, lung, liver, kidney and heart. Lower expression in brain, skeletal muscle and testis. +P49935 CATH_MOUSE Pro-cathepsin H (Cathepsin B3) (Cathepsin BA) [Cleaved into: Cathepsin H mini chain; Cathepsin H (EC 3.4.22.16); Cathepsin H heavy chain; Cathepsin H light chain] 333 37,170 Active site (3); Chain (4); Disulfide bond (4); Glycosylation (3); Propeptide (2); Sequence conflict (1); Signal peptide (1) FUNCTION: Important for the overall degradation of proteins in lysosomes. SUBCELLULAR LOCATION: Lysosome. SUBUNIT: Composed of a mini chain and a large chain. The large chain may be split into heavy and light chain. All chains are held together by disulfide bonds. TISSUE SPECIFICITY: Widely expressed with highest expression found in non-skeletal tissues. Low levels found in skeletal tissue. {ECO:0000269|PubMed:10395917}. +Q8BM88 CATO_MOUSE Cathepsin O (EC 3.4.22.42) 312 34,723 Active site (3); Chain (1); Disulfide bond (3); Glycosylation (2); Propeptide (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Proteolytic enzyme possibly involved in normal cellular protein degradation and turnover. {ECO:0000250}. SUBCELLULAR LOCATION: Lysosome {ECO:0000250}. +O89110 CASP8_MOUSE Caspase-8 (CASP-8) (EC 3.4.22.61) [Cleaved into: Caspase-8 subunit p18; Caspase-8 subunit p10] 480 55,357 Active site (2); Chain (2); Domain (2); Modified residue (5); Propeptide (2); Sequence conflict (5) FUNCTION: Most upstream protease of the activation cascade of caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death. Binding to the adapter molecule FADD recruits it to either receptor. The resulting aggregate called death-inducing signaling complex (DISC) performs CASP8 proteolytic activation. The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases. Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC. Cleaves and activates CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10. May participate in the GZMB apoptotic pathways. Cleaves ADPRT. Hydrolyzes the small-molecule substrate, Ac-Asp-Glu-Val-Asp-|-AMC. Likely target for the cowpox virus CRMA death inhibitory protein. PTM: Generation of the subunits requires association with the death-inducing signaling complex (DISC), whereas additional processing is likely due to the autocatalytic activity of the activated protease. GZMB and CASP10 can be involved in these processing events (By similarity). {ECO:0000250}.; PTM: Phosphorylation on Ser-389 during mitosis by CDK1 inhibits activation by proteolysis and prevents apoptosis. This phosphorylation occurs in cancer cell lines, as well as in primary breast tissues and lymphocytes (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a 18 kDa (p18) and a 10 kDa (p10) subunit (By similarity). Interacts with FADD, CFLAR and PEA15 (By similarity). Interacts with RFFL and RNF34; negatively regulate CASP8 through proteasomal degradation (By similarity). Interacts with TNFAIP8L2 (PubMed:18455983). Interacts with CASP8AP2 (PubMed:17245429). Interacts with NOL3; decreases CASP8 activity in a mitochondria localization- and phosphorylation-dependent manner and this interaction is dissociated by calcium (PubMed:15383280). Interacts with UBR2 (By similarity). {ECO:0000250|UniProtKB:Q14790, ECO:0000250|UniProtKB:Q9JHX4, ECO:0000269|PubMed:15383280, ECO:0000269|PubMed:17245429, ECO:0000269|PubMed:18455983}. TISSUE SPECIFICITY: Expressed in a wide variety of tissues. Highest expression in spleen, thymus, lung, liver and kidney. Lower expression in heart, brain, testis and skeletal muscle. +Q9DB16 CB39L_MOUSE Calcium-binding protein 39-like (MO25beta) (Mo25-like protein) 337 39,106 Alternative sequence (2); Chain (1); Erroneous initiation (1); Sequence conflict (2) FUNCTION: Component of a complex that binds and activates STK11/LKB1. In the complex, required to stabilize the interaction between CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta) and STK11/LKB1 (By similarity). {ECO:0000250}. SUBUNIT: Component of a trimeric complex composed of STK11/LKB1, STRAD (STRADA or STRADB) and CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta): the complex tethers STK11/LKB1 in the cytoplasm and stimulates its catalytic activity. {ECO:0000250}. +O54724 CAVN1_MOUSE Caveolae-associated protein 1 (Cav-p60) (Cavin-1) (Polymerase I and transcript release factor) 392 43,954 Chain (1); Coiled coil (1); Cross-link (7); Helix (2); Modified residue (23); Mutagenesis (3); Region (7) FUNCTION: Plays an important role in caveolae formation and organization. Essential for the formation of caveolae in all tissues (PubMed:18191225, PubMed:18840361, PubMed:18056712, PubMed:30188967). Core component of the CAVIN complex which is essential for recruitment of the complex to the caveolae in presence of calveolin-1 (CAV1) (PubMed:19546242). Essential for normal oligomerization of CAV1 (PubMed:23652019). Promotes ribosomal transcriptional activity in response to metabolic challenges in the adipocytes and plays an important role in the formation of the ribosomal transcriptional loop (PubMed:27528195). Dissociates transcription complexes paused by DNA-bound TTF1, thereby releasing both RNA polymerase I and pre-RNA from the template (PubMed:9582279, PubMed:11139612). The caveolae biogenesis pathway is required for the secretion of proteins such as GASK1A (PubMed:30188967). {ECO:0000269|PubMed:11139612, ECO:0000269|PubMed:18056712, ECO:0000269|PubMed:18191225, ECO:0000269|PubMed:18840361, ECO:0000269|PubMed:19546242, ECO:0000269|PubMed:23652019, ECO:0000269|PubMed:27528195, ECO:0000269|PubMed:30188967, ECO:0000269|PubMed:9582279}. PTM: Phosphorylated. Present in active and inactive forms. Changes in phosphorylation pattern may alter activity. Phosphorylation at Tyr-158 is essential for its function in the regulation of the ribosomal transcriptional activity. {ECO:0000269|PubMed:11139612, ECO:0000269|PubMed:27528195}.; PTM: Monoubiquitinated. {ECO:0000269|PubMed:27528195}. SUBCELLULAR LOCATION: Membrane, caveola {ECO:0000269|PubMed:18056712, ECO:0000269|PubMed:18191225, ECO:0000269|PubMed:19546242, ECO:0000269|PubMed:25514038}. Cell membrane {ECO:0000269|PubMed:18056712, ECO:0000269|PubMed:18191225}. Microsome {ECO:0000250|UniProtKB:Q6NZI2}. Endoplasmic reticulum {ECO:0000269|PubMed:30188967}. Cytoplasm, cytosol {ECO:0000269|PubMed:18191225, ECO:0000269|PubMed:19546242}. Mitochondrion {ECO:0000250|UniProtKB:Q6NZI2}. Nucleus {ECO:0000269|PubMed:25514038, ECO:0000269|PubMed:27528195}. Note=Translocates to the cytoplasm from caveolae upon insulin stimulation (By similarity). Colocalizes with CAV1 in lipid rafts in adipocytes (PubMed:18056712). Localizes in the caveolae in a caveolin-dependent manner (PubMed:19546242). {ECO:0000250|UniProtKB:Q6NZI2, ECO:0000269|PubMed:18056712, ECO:0000269|PubMed:19546242}. SUBUNIT: Component of the CAVIN complex composed of CAVIN1, CAVIN2, CAVIN3 and CAVIN4 (PubMed:19546242). Homotrimer (PubMed:25588833). Interacts with LIPE in the adipocyte cytoplasm (By similarity). Interacts with RNA polymerase I (PubMed:9582279). Interacts with TTF1 (PubMed:9582279, PubMed:27528195). Binds the 3' end of pre-rRNA (PubMed:9582279). Interacts with transcription factor ZNF148 (PubMed:10727401). Interacts with CAV1, CAVIN2 and CAVIN3 (PubMed:25588833, PubMed:19546242). Interacts with CAVIN4 (PubMed:19546242). {ECO:0000250|UniProtKB:Q6NZI2, ECO:0000269|PubMed:10727401, ECO:0000269|PubMed:19546242, ECO:0000269|PubMed:25588833, ECO:0000269|PubMed:27528195, ECO:0000269|PubMed:9582279}. DOMAIN: The leucine-zipper domain 1 is essential for its localization in the caveolae. {ECO:0000269|PubMed:25514038}. TISSUE SPECIFICITY: Expressed in the heart, stomach, adipose tissue and lung (at protein level). Expressed in testis, kidney, muscle, liver, spleen and brain. {ECO:0000269|PubMed:11161808, ECO:0000269|PubMed:18191225, ECO:0000269|PubMed:19546242}. +Q504N0 CBPA2_MOUSE Carboxypeptidase A2 (EC 3.4.17.15) 417 47,057 Active site (1); Binding site (2); Chain (1); Disulfide bond (2); Metal binding (3); Propeptide (1); Region (3); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +Q8CDP0 CBPC3_MOUSE Cytosolic carboxypeptidase 3 (EC 3.4.17.-) (ATP/GTP-binding protein-like 3) 1006 116,378 Active site (1); Alternative sequence (6); Chain (1); Metal binding (3); Mutagenesis (1) FUNCTION: Metallocarboxypeptidase that mediates both deglutamylation and deaspartylation of target proteins. Catalyzes the deglutamylation of polyglutamate side chains generated by post-translational polyglutamylation in proteins such as tubulins. Also removes gene-encoded polyglutamates or polyaspartates from the carboxy-terminus of target proteins such as MYLK. Does not show detyrosinase or deglycylase activities from the carboxy-terminus of tubulin. {ECO:0000269|PubMed:17244818, ECO:0000269|PubMed:25103237}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:17244818}. TISSUE SPECIFICITY: Widely expressed. Expressed abundantly in tissues with m otile cilia such as testis, lung and trachea. Abundantly expressed in pituitary and kidney, moderately expressed in brain, eye, fat, pancreas, stomach, and adrenal. {ECO:0000269|PubMed:17244818, ECO:0000269|PubMed:25103237}. +Q6P8K8 CBPA4_MOUSE Carboxypeptidase A4 (EC 3.4.17.-) 420 47,339 Active site (1); Binding site (2); Chain (1); Disulfide bond (1); Glycosylation (1); Metal binding (3); Propeptide (1); Region (3); Sequence conflict (1); Signal peptide (1) FUNCTION: Metalloprotease that could be involved in the histone hyperacetylation pathway. Releases a C-terminal amino acid, with preference for -Phe, -Leu, -Ile, -Met, -Tyr and -Val. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Interacts with LXN. {ECO:0000250}. +Q3TTA7 CBLB_MOUSE E3 ubiquitin-protein ligase CBL-B (EC 2.3.2.27) (Casitas B-lineage lymphoma proto-oncogene b) (RING-type E3 ubiquitin transferase CBL-B) (SH3-binding protein CBL-B) (Signal transduction protein CBL-B) 982 109,092 Alternative sequence (1); Beta strand (9); Binding site (1); Calcium binding (1); Chain (1); Compositional bias (3); Domain (2); Helix (18); Modified residue (12); Region (6); Sequence conflict (1); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and transfers it to substrates, generally promoting their degradation by the proteasome. Negatively regulates TCR (T-cell receptor), BCR (B-cell receptor) and FCER1 (high affinity immunoglobulin epsilon receptor) signal transduction pathways. In naive T-cells, inhibits VAV1 activation upon TCR engagement and imposes a requirement for CD28 costimulation for proliferation and IL-2 production. Also acts by promoting PIK3R1/p85 ubiquitination, which impairs its recruitment to the TCR and subsequent activation. In activated T-cells, inhibits PLCG1 activation and calcium mobilization upon restimulation and promotes anergy. In B-cells, acts by ubiquitinating SYK and promoting its proteasomal degradation. Slightly promotes SRC ubiquitination. May be involved in EGFR ubiquitination and internalization. May be functionally coupled with the E2 ubiquitin-protein ligase UB2D3. In association with CBL, required for proper feedback inhibition of ciliary platelet-derived growth factor receptor-alpha (PDGFRA) signaling pathway via ubiquitination and internalization of PDGFRA (PubMed:29237719). {ECO:0000269|PubMed:10646608, ECO:0000269|PubMed:10646609, ECO:0000269|PubMed:11070165, ECO:0000269|PubMed:11526404, ECO:0000269|PubMed:12771181, ECO:0000269|PubMed:15308098, ECO:0000269|PubMed:29237719}. PTM: Phosphorylated on tyrosine and serine residues upon TCR or BCR activation. Phosphorylated on Tyr-664 and Tyr-708 in adipocytes following insulin stimulation. {ECO:0000269|PubMed:12771181, ECO:0000269|PubMed:12842890}.; PTM: Auto-ubiquitinated upon EGF-mediated cell activation or upon T-cell costimulation by CD28; which promotes proteasomal degradation. {ECO:0000269|PubMed:12193687}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12842890}. Note=In adipocytes, translocates to the plasma membrane upon insulin stimulation. SUBUNIT: Interacts with SH3 domain-containing proteins LCK, CRK and SORBS1. Interacts with LCP2 and ZAP70. Interacts with CBL. Interacts with SH3 domain-containing proteins VAV1, FYN, FGR, PLCG1, GRB2, CRKL, PIK3R1 and SH3KBP1/CIN85. Identified in heterotrimeric complexes with SH3KBP1/CIN85, CD2AP and ARHGEF7, where one CBLB peptide binds two copies of the other protein. Interacts with poly-ubiquitinated proteins. Dimerization is required for the binding of poly-ubiquitin, but not for the binding of mono-ubiquitin. Interacts with EGFR (phosphorylated). Interacts with IFT20 (By similarity). {ECO:0000250|UniProtKB:Q13191, ECO:0000269|PubMed:10646608, ECO:0000269|PubMed:12842890}. DOMAIN: The N-terminus is composed of the phosphotyrosine binding (PTB) domain, a short linker region and the RING-type zinc finger. The PTB domain, which is also called TKB (tyrosine kinase binding) domain, is composed of three different subdomains: a four-helix bundle (4H), a calcium-binding EF hand and a divergent SH2 domain.; DOMAIN: The RING-type zinc finger domain mediates binding to an E2 ubiquitin-conjugating enzyme.; DOMAIN: The UBA domain interacts with poly-ubiquitinated proteins. {ECO:0000250|UniProtKB:Q13191}. +Q3UYG1 CC160_MOUSE Coiled-coil domain-containing protein 160 323 37,398 Chain (1); Coiled coil (1) +Q8CEG5 CC28B_MOUSE Coiled-coil domain-containing protein 28B 200 22,033 Chain (1); Coiled coil (1); Modified residue (3); Sequence conflict (2) FUNCTION: Involved in ciliogenesis. Regulates cilia length through its interaction with MAPKAP1/SIN1 but independently of mTORC2 complex. Modulates mTORC2 complex assembly and function, possibly enhances AKT1 phosphorylation. Does not seem to modulate assembly and function of mTORC1 complex. {ECO:0000269|PubMed:23727834}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Note=It localizes near centrosomes and basal bodies. {ECO:0000250}. SUBUNIT: Interacts with BBS1, BBS2, BBS4, BBS5, BBS6, BBS7 and TTC8/BBS8. Interacts with MAPKAP1/SIN1 isoform 1 and RICTOR (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the retina, pericardium and limb epithelium. {ECO:0000269|PubMed:16327777}. +Q61686 CBX5_MOUSE Chromobox protein homolog 5 (Heterochromatin protein 1 homolog alpha) (HP1 alpha) 191 22,186 Beta strand (4); Chain (1); Compositional bias (1); Cross-link (6); Domain (2); Helix (2); Modified residue (9); Sequence conflict (2); Turn (1) FUNCTION: Component of heterochromatin that recognizes and binds histone H3 tails methylated at 'Lys-9' (H3K9me), leading to epigenetic repression. In contrast, it is excluded from chromatin when 'Tyr-41' of histone H3 is phosphorylated (H3Y41ph). Can interact with lamin-B receptor (LBR). This interaction can contribute to the association of the heterochromatin with the inner nuclear membrane. Involved in the formation of functional kinetochore through interaction with MIS12 complex proteins (By similarity). {ECO:0000250|UniProtKB:P45973}. PTM: Phosphorylation of HP1 and LBR may be responsible for some of the alterations in chromatin organization and nuclear structure which occur at various times during the cell cycle. Phosphorylated during interphase and possibly hyper-phosphorylated during mitosis (By similarity). {ECO:0000250}.; PTM: Ubiquitinated. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P45973}. Chromosome. Chromosome, centromere. Note=Colocalizes with HNRNPU in the nucleus (By similarity). Component of centromeric and pericentromeric heterochromatin. Associates with chromosomes during mitosis. Associates specifically with chromatin during metaphase and anaphase. {ECO:0000250|UniProtKB:P45973}. SUBUNIT: Interacts directly with ATRX, CHAF1A, LBR, NIPBL, SP100 and STAM2 via the chromoshadow domain. Can interact directly with CBX3 via the chromoshadow domain. Interacts with histone H3 methylated at 'Lys-9'. Interacts with BAHD1, SETDB1, MIS12 and DSN1. Interacts with POGZ; POGZ and PXVXL motif-containing proteins such as INCENP and TRIM28 compete for interaction with CBX5. Interacts with INCENP. Interacts with CHAMP1 (By similarity). Interacts directly with TRIM28 via the chromoshadow domain (PubMed:8978696). Interacts with KMT5B and KMT5C (PubMed:15145825). Interacts with HP1BP3 and TRIM24 (PubMed:8978696). May form homodimers (PubMed:8978696). Interacts with PRR14 (via N-terminus) (By similarity). Interacts with RRP1B (By similarity). Interacts with HNRNPU (via C-terminus); this interaction is, at least in part, RNA-dependent (By similarity). Interacts with LRIF1 (via PxVxL motif) (By similarity). {ECO:0000250|UniProtKB:P45973, ECO:0000269|PubMed:15145825, ECO:0000269|PubMed:8978696}. +Q8BVF4 CCD30_MOUSE Coiled-coil domain-containing protein 30 (Prefoldin subunit 6-like protein) 654 76,048 Alternative sequence (5); Chain (1); Coiled coil (2); Sequence conflict (2) +D3YV10 CCD13_MOUSE Coiled-coil domain-containing protein 13 709 79,750 Chain (1); Coiled coil (5); Modified residue (3) FUNCTION: Required for primary cilia formation and promotes the localization of the ciliopathy protein BBS4 to both centriolar satellites and cilia. {ECO:0000250|UniProtKB:Q8IYE1}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000250|UniProtKB:Q8IYE1}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q8IYE1}. SUBUNIT: Interacts with PCM1, CEP290 and PCNT. {ECO:0000250|UniProtKB:Q8IYE1}. +Q6GQU0 CC070_MOUSE UPF0524 protein C3orf70 homolog 248 27,476 Chain (1); Sequence conflict (1) +Q9D9P2 CC103_MOUSE Coiled-coil domain-containing protein 103 237 26,861 Chain (1); Coiled coil (1) FUNCTION: Dynein-attachment factor required for cilia motility. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell projection, cilium, flagellum {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +Q9DAL3 CCD54_MOUSE Coiled-coil domain-containing protein 54 329 37,518 Chain (1); Coiled coil (1); Modified residue (1) +P09240 CCKN_MOUSE Cholecystokinin (CCK) [Cleaved into: Cholecystokinin-33 (CCK33); Cholecystokinin-12 (CCK12); Cholecystokinin-8 (CCK8)] 115 12,770 Chain (1); Modified residue (4); Peptide (3); Propeptide (2); Sequence conflict (3); Signal peptide (1) FUNCTION: This peptide hormone induces gall bladder contraction and the release of pancreatic enzymes in the gut. Its function in the brain is not clear. Binding to CCK-A receptors stimulates amylase release from the pancreas, binding to CCK-B receptors stimulates gastric acid secretion. PTM: The precursor is cleaved by proteases to produce a number of active cholecystokinins. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Binds to CCK-A receptors in the pancreas and CCK-B receptors in the brain. {ECO:0000250}. +Q8VDN4 CCD92_MOUSE Coiled-coil domain-containing protein 92 314 35,207 Chain (1); Coiled coil (2) SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250}. SUBUNIT: Interacts with CEP164. {ECO:0000250}. +O88430 CCL22_MOUSE C-C motif chemokine 22 (Activated B and dendritic cell-derived) (CC chemokine ABCD-1) (Small-inducible cytokine A22) 92 10,302 Chain (1); Disulfide bond (2); Signal peptide (1) FUNCTION: Chemotactic for activated T-lymphocytes. May play an important role in the collaboration of dendritic cells and B-lymphocytes with T-cells in immune responses. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Expressed by activated splenic B-lymphocytes and dendritic cells. Low expression in lung, thymocytes, lymph node, and unstimulated splenic cells. +Q9JKC0 CCL24_MOUSE C-C motif chemokine 24 (Eosinophil chemotactic protein 2) (Eotaxin-2) (Small-inducible cytokine A24) 119 12,871 Chain (1); Disulfide bond (2); Glycosylation (2); Signal peptide (1) FUNCTION: Chemotactic for resting T-lymphocytes, and eosinophils. Has lower chemotactic activity for neutrophils but none for monocytes and activated lymphocytes. Binds to CCR3 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Highest expression in jejunum and spleen. Lower levels found in liver and lung. No expression detected in kidney, thymus, brain or testis. {ECO:0000269|PubMed:11067944}. +Q64299 CCN3_MOUSE CCN family member 3 (Cellular communication network factor 3) (Nephroblastoma-overexpressed gene protein homolog) (Protein NOV homolog) (NovH) 354 38,928 Chain (1); Disulfide bond (5); Domain (4); Glycosylation (2); Lipidation (1); Mutagenesis (4); Sequence conflict (1); Signal peptide (1) FUNCTION: Immediate-early protein playing a role in various cellular processes including proliferation, adhesion, migration, differentiation and survival. Acts by binding to integrins or membrane receptors such as NOTCH1. Essential regulator of hematopoietic stem and progenitor cell function. Inhibits myogenic differentiation through the activation of Notch-signaling pathway. Inhibits vascular smooth muscle cells proliferation by increasing expression of cell-cycle regulators such as CDKN2B or CDKN1A independently of TGFB1 signaling. Ligand of integrins ITGAV:ITGB3 and ITGA5:ITGB1, acts directly upon endothelial cells to stimulate pro-angiogenic activities and induces angiogenesis. In endothelial cells, supports cell adhesion, induces directed cell migration (chemotaxis) and promotes cell survival. Plays also a role in cutaneous wound healing acting as integrin receptor ligand. Supports skin fibroblast adhesion through ITGA5:ITGB1 and ITGA6:ITGB1 and induces fibroblast chemotaxis through ITGAV:ITGB5. Seems to enhance bFGF-induced DNA synthesis in fibroblasts (By similarity). Involved in bone regeneration as a negative regulator (PubMed:23653360). Enhances the articular chondrocytic phenotype, whereas it repressed the one representing endochondral ossification (By similarity). Impairs pancreatic beta-cell function, inhibits beta-cell proliferation and insulin secretion (PubMed:23705021). Plays a role as negative regulator of endothelial pro-inflammatory activation reducing monocyte adhesion, its anti-inflammatory effects occur secondary to the inhibition of NF-kappaB signaling pathway (By similarity). Contributes to the control and coordination of inflammatory processes in atherosclerosis (PubMed:24722330). Attenuates inflammatory pain through regulation of IL1B- and TNF-induced MMP9, MMP2 and CCL2 expression. Inhibits MMP9 expression through ITGB1 engagement (By similarity). {ECO:0000250|UniProtKB:P48745, ECO:0000250|UniProtKB:Q9QZQ5, ECO:0000269|PubMed:23653360, ECO:0000269|PubMed:23705021, ECO:0000269|PubMed:24722330}. PTM: May be palmitoylated on Cys-241, which is important for extracellular secretion. {ECO:0000269|PubMed:29287726}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23705021, ECO:0000269|PubMed:29287726}. Cytoplasm {ECO:0000250|UniProtKB:P48745}. Cell junction, gap junction {ECO:0000250|UniProtKB:P48745}. Note=Localizes at the gap junction in presence of GJA1. {ECO:0000250|UniProtKB:Q9QZQ5}. SUBUNIT: Interacts with FBLN1. Interacts (via CTCK domain) with NOTCH1 (via the EGF-like repeat region). Interacts with GJA1/CX43. Interacts with ITGA5:ITGB1, ITGAV:ITGB3 and ITGAV:ITGB5. Interacts with ZDHHC22; the interaction may lead to CCN3 palmitoylation (PubMed:29287726). {ECO:0000250|UniProtKB:P48745, ECO:0000269|PubMed:29287726}. TISSUE SPECIFICITY: Expressed in large vessels including the ascending aorta, carotid arteries, and the thoracic aorta, in medium-sized vessels such as coronary arteries and small pulmonary veins and also in small vessels. In addition, also found to be present in the heart (at protein level) (PubMed:21063504). Expressed in astrocytes (at protein level) (PubMed:15213231). Detected in brain, bone, lung and muscle tissues (PubMed:20139355, PubMed:23653360). Expressed in skin, expression highly increases 5 days post-wounding, peaking on the 7th day to decline after 9 days (PubMed:15611078). Expressed in pancreatic ducts and beta-cell islets (PubMed:23705021). {ECO:0000269|PubMed:15213231, ECO:0000269|PubMed:15611078, ECO:0000269|PubMed:20139355, ECO:0000269|PubMed:21063504, ECO:0000269|PubMed:23653360, ECO:0000269|PubMed:23705021}. +P30280 CCND2_MOUSE G1/S-specific cyclin-D2 289 32,897 Chain (1); Domain (1); Modified residue (2) FUNCTION: Regulatory component of the cyclin D2-CDK4 (DC) complex that phosphorylates and inhibits members of the retinoblastoma (RB) protein family including RB1 and regulates the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complex and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also substrate for SMAD3, phosphorylating SMAD3 in a cell-cycle-dependent manner and repressing its transcriptional activity. Component of the ternary complex, cyclin D2/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex (By similarity). {ECO:0000250}. PTM: Polyubiquitinated by the SCF(FBXL2) complex, leading to proteasomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}. Note=Cyclin D-CDK4 complexes accumulate at the nuclear membrane and are then translocated into the nucleus through interaction with KIP/CIP family members. {ECO:0000250}. SUBUNIT: Interacts with either CDK4 or CDK6 protein kinase to form a serine/threonine kinase holoenzyme complex. The cyclin subunit imparts substrate specificity to the complex. Component of the ternary complex cyclin D/CDK4/CDKN1B required for nuclear translocation and modulation of CDK4-mediated kinase activity (By similarity). {ECO:0000250}. +Q9QWV9 CCNT1_MOUSE Cyclin-T1 (CycT1) (Cyclin-T) 724 80,598 Chain (1); Coiled coil (1); Compositional bias (4); Cross-link (3); Modified residue (5); Motif (1); Mutagenesis (5); Sequence conflict (2) FUNCTION: Regulatory subunit of the cyclin-dependent kinase pair (CDK9/cyclin-T1) complex, also called positive transcription elongation factor B (P-TEFb), which is proposed to facilitate the transition from abortive to productive elongation by phosphorylating the CTD (carboxy-terminal domain) of the large subunit of RNA polymerase II (RNA Pol II). SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Cyclin-T1 is the predominant cyclin that associates with CDK9 to form a heterodimer called P-TEFb. P-TEFb forms a complex with AFF4/AF5Q31. Component of a complex which is at least composed of HTATSF1/Tat-SF1, P-TEFb complex, RNA pol II, SUPT5H, and NCL/nucleolin. Component of the 7SK snRNP complex at least composed of P-TEFb (composed of CDK9 and CCNT1/cyclin-T1), HEXIM1, HEXIM2, BCDIN3, SART3 proteins and 7SK and U6 snRNAs. Interacts with BRD4, probably to target chromatin binding. Interacts with MDFIC. Interacts with HSF1. Interacts with HTATSF1. Interacts with AFF4. Interacts with TBX21 (PubMed:27292648). {ECO:0000250|UniProtKB:O60563, ECO:0000269|PubMed:27292648}. +Q8CDI6 CD158_MOUSE Coiled-coil domain-containing protein 158 1109 126,826 Alternative sequence (2); Chain (1); Coiled coil (3); Compositional bias (1) +P11942 CD3G_MOUSE T-cell surface glycoprotein CD3 gamma chain (T-cell receptor T3 gamma chain) (CD antigen CD3g) 182 20,234 Beta strand (7); Chain (1); Disulfide bond (1); Domain (2); Glycosylation (1); Modified residue (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 117 137 Helical. {ECO:0000255}. TOPO_DOM 23 116 Extracellular. {ECO:0000255}.; TOPO_DOM 138 182 Cytoplasmic. {ECO:0000255}. FUNCTION: Part of the TCR-CD3 complex present on T-lymphocyte cell surface that plays an essential role in adaptive immune response. When antigen presenting cells (APCs) activate T-cell receptor (TCR), TCR-mediated signals are transmitted across the cell membrane by the CD3 chains CD3D, CD3E, CD3G and CD3Z. All CD3 chains contain immunoreceptor tyrosine-based activation motifs (ITAMs) in their cytoplasmic domain. Upon TCR engagement, these motifs become phosphorylated by Src family protein tyrosine kinases LCK and FYN, resulting in the activation of downstream signaling pathways. In addition to this role of signal transduction in T-cell activation, CD3G plays an essential role in the dynamic regulation of TCR expression at the cell surface. Indeed, constitutive TCR cycling is dependent on the di-leucine-based (diL) receptor-sorting motif present in CD3G (PubMed:25920998). {ECO:0000250|UniProtKB:P09693, ECO:0000269|PubMed:25920998, ECO:0000269|PubMed:9524111}. PTM: Phosphorylated on Tyr residues after T-cell receptor triggering by LCK in association with CD4/CD8. Phosphorylated also by PKC; leading to the TCR complex down-regulation. {ECO:0000250|UniProtKB:P09693}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: The TCR-CD3 complex is composed of a CD3D/CD3E and a CD3G/CD3E heterodimers that preferentially associate with TCRalpha and TCRbeta, respectively, to form TCRalpha/CD3E/CD3G and TCRbeta/CD3G/CD3E trimers. In turn, the hexamer interacts with CD3Z homodimer to form the TCR-CD3 complex. Alternatively, TCRalpha and TCRbeta can be replaced by TCRgamma and TCRdelta. {ECO:0000250|UniProtKB:P09693}. +P40237 CD82_MOUSE CD82 antigen (C33 antigen) (IA4) (Inducible membrane protein R2) (Metastasis suppressor Kangai-1 homolog) (CD antigen CD82) 266 29,629 Chain (1); Glycosylation (4); Topological domain (5); Transmembrane (4) TRANSMEM 12 32 Helical. {ECO:0000255}.; TRANSMEM 54 72 Helical. {ECO:0000255}.; TRANSMEM 84 110 Helical. {ECO:0000255}.; TRANSMEM 228 249 Helical. {ECO:0000255}. TOPO_DOM 1 11 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 33 53 Extracellular. {ECO:0000255}.; TOPO_DOM 73 83 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 111 227 Extracellular. {ECO:0000255}.; TOPO_DOM 250 266 Cytoplasmic. {ECO:0000255}. FUNCTION: Associates with CD4 or CD8 and delivers costimulatory signals for the TCR/CD3 pathway. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SUBUNIT: Interacts directly with IGSF8. {ECO:0000250}. TISSUE SPECIFICITY: Highest expression in the spleen and the kidney. Low expression in skeletal muscle and in the heart. +Q9JJ66 CDC20_MOUSE Cell division cycle protein 20 homolog (mmCdc20) (p55CDC) 499 54,816 Chain (1); Cross-link (2); Modified residue (9); Repeat (7); Sequence conflict (2) Protein modification; protein ubiquitination. FUNCTION: Required for full ubiquitin ligase activity of the anaphase promoting complex/cyclosome (APC/C) and may confer substrate specificity upon the complex. Is regulated by MAD2L1: in metaphase the MAD2L1-CDC20-APC/C ternary complex is inactive and in anaphase the CDC20-APC/C binary complex is active in degrading substrates. The CDC20-APC/C complex positively regulates the formation of synaptic vesicle clustering at active zone to the presynaptic membrane in postmitotic neurons. CDC20-APC/C-induced degradation of NEUROD2 induces presynaptic differentiation. {ECO:0000269|PubMed:19900895}. PTM: Acetylated. Deacetylated at Lys-66 by SIRT2; deacetylation enhances the interaction of CDC20 with CDC27, leading to activation of anaphase promoting complex/cyclosome (APC/C). {ECO:0000269|PubMed:22014574}.; PTM: Phosphorylated during mitosis, probably by maturation promoting factor (MPF). Phosphorylated by BUB1 at Ser-41; Ser-72; Ser-92; Ser-153; Thr-157 and Ser-161. Phosphorylated by NEK2 (By similarity). {ECO:0000250}.; PTM: Dephosphorylated by CTDP1. {ECO:0000250}.; PTM: Ubiquitinated and degraded by the proteasome during spindle assembly checkpoint. Ubiquitinated at Lys-490 during prometaphase. Ubiquitination at Lys-485 and Lys-490 has no effect on its ability to bind the APC/C complex (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. SUBUNIT: Interacts with MAD2L1 and BUB1B. The phosphorylated form interacts with APC/C. Interacts with NINL and MAD2L1. Interacts with CDK5RAP2. Interacts with NEK2 (By similarity). Interacts with HSF1 (via phosphorylated form); this interaction occurs in mitosis in a MAD2L1-dependent manner and prevents PLK1-stimulated degradation of HSF1 by blocking the recruitment of the SCF(BTRC) ubiquitin ligase complex (By similarity). Found in a complex with CDC20, CDC27, SPATC1 and TUBG1. Interacts with NEUROD2, SIRT2 and SPATC1. Interacts (via the N-terminal substrate-binding domain) with FBXO5 (PubMed:15526037). {ECO:0000250|UniProtKB:Q12834, ECO:0000269|PubMed:15280373, ECO:0000269|PubMed:15526037, ECO:0000269|PubMed:19900895, ECO:0000269|PubMed:22014574}. +Q61735 CD47_MOUSE Leukocyte surface antigen CD47 (Integrin-associated protein) (IAP) (CD antigen CD47) 303 33,098 Alternative sequence (1); Chain (1); Disulfide bond (2); Domain (1); Glycosylation (7); Modified residue (3); Signal peptide (1); Topological domain (6); Transmembrane (5) TRANSMEM 141 161 Helical. {ECO:0000255}.; TRANSMEM 174 194 Helical. {ECO:0000255}.; TRANSMEM 207 227 Helical. {ECO:0000255}.; TRANSMEM 239 259 Helical. {ECO:0000255}.; TRANSMEM 267 287 Helical. {ECO:0000255}. TOPO_DOM 19 140 Extracellular. {ECO:0000255}.; TOPO_DOM 162 173 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 195 206 Extracellular. {ECO:0000255}.; TOPO_DOM 228 238 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 260 266 Extracellular. {ECO:0000255}.; TOPO_DOM 288 303 Cytoplasmic. {ECO:0000255}. FUNCTION: Has a role in both cell adhesion by acting as an adhesion receptor for THBS1 on platelets, and in the modulation of integrins. Plays an important role in memory formation and synaptic plasticity in the hippocampus. Receptor for SIRPA, binding to which prevents maturation of immature dendritic cells and inhibits cytokine production by mature dendritic cells. Interaction with SIRPG mediates cell-cell adhesion, enhances superantigen-dependent T-cell-mediated proliferation and costimulates T-cell activation. May play a role in membrane transport and/or integrin dependent signal transduction. May prevent premature elimination of red blood cells. May be involved in membrane permeability changes induced following virus infection (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7691831}; Multi-pass membrane protein {ECO:0000269|PubMed:7691831}. SUBUNIT: Monomer. Interacts with fibrinogen, PTPNS1, SIRPG, THBS1, UBQLN1 and UBQLN2 (By similarity). {ECO:0000250}. +Q61003 CD6_MOUSE T-cell differentiation antigen CD6 (CD antigen CD6) 665 72,255 Alternative sequence (3); Chain (1); Disulfide bond (11); Domain (3); Glycosylation (8); Modified residue (1); Sequence conflict (6); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 399 419 Helical. {ECO:0000255}. TOPO_DOM 17 398 Extracellular. {ECO:0000255}.; TOPO_DOM 420 665 Cytoplasmic. {ECO:0000255}. FUNCTION: Cell adhesion molecule that mediates cell-cell contacts and regulates T-cell responses via its interaction with ALCAM/CD166. Contributes to signaling cascades triggered by activation of the TCR/CD3 complex (PubMed:24584089). Functions as costimulatory molecule; promotes T-cell activation and proliferation. Contributes to the formation and maturation of the immunological synapse. Functions as calcium-dependent pattern receptor that binds and aggregates both Gram-positive and Gram-negative bacteria. Binds both lipopolysaccharide (LPS) from Gram-negative bacteria and lipoteichoic acid from Gram-positive bacteria. LPS binding leads to the activation of signaling cascades and down-stream MAP kinases. Mediates activation of the inflammatory response and the secretion of pro-inflammatory cytokines in response to LPS. {ECO:0000250|UniProtKB:P30203, ECO:0000269|PubMed:24584089}. PTM: After T-cell activation, becomes hyperphosphorylated on Ser and Thr residues (By similarity). Phosphorylated on tyrosine residues in response to stimulation of the TCR complex (PubMed:24584089). {ECO:0000250|UniProtKB:P30203, ECO:0000269|PubMed:24584089}.; PTM: Glycosylated. {ECO:0000250|UniProtKB:P30203}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16914752}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P30203}. Note=Detected at the immunological synapse, i.e, at the contact zone between antigen-presenting dendritic cells and T-cells. Colocalizes with the TCR/CD3 complex at the immunological synapse. {ECO:0000250|UniProtKB:P30203}. SUBUNIT: Interacts (via extracellular domain) with ALCAM/CD166 (via extracellular domain) (PubMed:16914752). Interacts with the TCR/CD3 complex subunit CD3E. Interacts (via tyrosine phosphorylated C-terminus) with LCP2 (via SH2 domain) (PubMed:24584089). Interacts (via glycosylated extracellular domain) with LGALS1 and LGALS3. Interaction with LGALS1 or LGALS3 inhibits interaction with ALCAM (By similarity). Interacts with VAV1 (PubMed:24584089). {ECO:0000250|UniProtKB:P30203, ECO:0000269|PubMed:16914752, ECO:0000269|PubMed:24584089}. TISSUE SPECIFICITY: Expressed predominantly in thymus, lymph node and spleen. +A2A6Q5 CDC27_MOUSE Cell division cycle protein 27 homolog 825 91,842 Alternative sequence (2); Chain (1); Modified residue (14); Repeat (13) Protein modification; protein ubiquitination. FUNCTION: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By similarity). {ECO:0000250}. PTM: Phosphorylated. Phosphorylation on Ser-427 and Thr-447 occurs specifically during mitosis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Homodimer. The mammalian APC/C is composed at least of 14 distinct subunits ANAPC1, ANAPC2, CDC27/APC3, ANAPC4, ANAPC5, CDC16/APC6, ANAPC7, CDC23/APC8, ANAPC10, ANAPC11, CDC26/APC12, ANAPC13, ANAPC15 and ANAPC16 that assemble into a complex of at least 19 chains with a combined molecular mass of around 1.2 MDa; APC/C interacts with FZR1 and FBXO5 (By similarity). Interacts with RB. Interacts with FAM168B/MANI (PubMed:20716133). Interacts with MCPH1 (By similarity). {ECO:0000250|UniProtKB:P30260, ECO:0000269|PubMed:20716133}. +Q9Z0H0 CDC7_MOUSE Cell division cycle 7-related protein kinase (CDC7-related kinase) (muCdc7) (EC 2.7.11.1) 564 62,770 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Cross-link (1); Domain (1); Modified residue (1); Nucleotide binding (1); Sequence conflict (18) FUNCTION: Seems to phosphorylate critical substrates that regulate the G1/S phase transition and/or DNA replication. Can phosphorylates MCM2 and MCM3. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Forms a complex with either DBF4/DBF4A or DBF4B, leading to the activation of the kinase activity. +Q8BWD8 CDK19_MOUSE Cyclin-dependent kinase 19 (EC 2.7.11.22) (CDC2-related protein kinase 6) (Cell division cycle 2-like protein kinase 6) (Cell division protein kinase 19) 501 56,570 Active site (1); Binding site (1); Chain (1); Compositional bias (3); Domain (1); Erroneous initiation (1); Modified residue (2); Nucleotide binding (1) +Q9D0M2 CDCA7_MOUSE Cell division cycle-associated protein 7 382 43,837 Chain (1); Cross-link (1); Modified residue (4); Motif (1); Region (2); Sequence conflict (4) FUNCTION: Participates in MYC-mediated cell transformation and apoptosis; induces anchorage-independent growth and clonogenicity in lymphoblastoid cells. Insufficient to induce tumorigenicity when overexpressed but contributes to MYC-mediated tumorigenesis. May play a role as transcriptional regulator (By similarity). {ECO:0000250, ECO:0000269|PubMed:16580749}. PTM: Phosphorylation at Thr-170 promotes interaction with YWHAE and YWHAZ, dissociation from MYC and sequestration in the cytoplasm. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Predominantly nuclear with some expression also seen in the cytoplasm. Predominantly cytoplasmic when phosphorylated at Thr-170 (By similarity). {ECO:0000250}. SUBUNIT: Interacts with MYC (via C-terminus), YWHAE and YWHAZ. {ECO:0000250}. +Q4VAA2 CDV3_MOUSE Protein CDV3 (Carnitine deficiency-associated protein 3) (Tyrosine-phosphorylated protein 36) (TPP36) 281 29,729 Alternative sequence (2); Chain (1); Compositional bias (3); Initiator methionine (1); Modified residue (9); Sequence conflict (3) PTM: Isoform 1 and isoform 2 are phosphorylated on tyrosines by ABL1 in B-cells. {ECO:0000269|PubMed:12606058}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12606058}. TISSUE SPECIFICITY: Ubiquitously expressed (at protein level). Up-regulated in ventricles of juvenile visceral steatosis mice. {ECO:0000269|PubMed:12359334, ECO:0000269|PubMed:12606058}. +Q9JHU3 CDK20_MOUSE Cyclin-dependent kinase 20 (EC 2.7.11.22) (CDK-activating kinase p42) (CAK-kinase p42) (CDK-related protein kinase PNQLARE) (Cell cycle-related kinase) (Cell division protein kinase 20) (Cyclin-dependent protein kinase H) (Cyclin-kinase-activating kinase p42) 346 38,379 Active site (1); Alternative sequence (2); Binding site (1); Chain (1); Domain (1); Nucleotide binding (1); Sequence conflict (6) FUNCTION: Involved in cell growth. Activates CDK2, a kinase involved in the control of the cell cycle, by phosphorylating residue 'Thr-160' (By similarity). Required for high-level Shh responses in the developing neural tube. Together with TBC1D32, controls the structure of the primary cilium by coordinating assembly of the ciliary membrane and axoneme, allowing GLI2 to be properly activated in response to SHH signaling. {ECO:0000250, ECO:0000269|PubMed:20159594}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20159594}. Cytoplasm {ECO:0000269|PubMed:20159594}. Cell projection, cilium {ECO:0000269|PubMed:20159594}. SUBUNIT: Monomer (By similarity). Interacts with MAK (By similarity). Interacts with TBC1D32. {ECO:0000250, ECO:0000269|PubMed:20159594}. +Q5DU05 CE164_MOUSE Centrosomal protein of 164 kDa (Cep164) 1446 162,601 Alternative sequence (4); Chain (1); Coiled coil (1); Compositional bias (2); Domain (1); Erroneous initiation (2); Modified residue (3); Region (1); Sequence conflict (3) FUNCTION: Plays a role in microtubule organization and/or maintenance for the formation of primary cilia (PC), a microtubule-based structure that protrudes from the surface of epithelial cells. Plays a critical role in G2/M checkpoint and nuclear divisions. A key player in the DNA damage-activated ATR/ATM signaling cascade since it is required for the proper phosphorylation of H2AX, RPA, CHEK2 and CHEK1. Plays a critical role in chromosome segregation, acting as a mediator required for the maintenance of genomic stability through modulation of MDC1, RPA and CHEK1 (By similarity). {ECO:0000250, ECO:0000269|PubMed:22863007}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:22863007, ECO:0000269|PubMed:26337392}. Nucleus {ECO:0000250|UniProtKB:Q9UPV0}. Note=Localizes specifically to very distally located appendage structures on the mature centriole from which initiate PC formation (PubMed:26337392). Persisted at centrioles throughout mitosis (By similarity). In response to DNA damage, it translocates to nuclear foci that contain the DNA damage response proteins KAT5/TIP60 and CHEK1 (By similarity). {ECO:0000250|UniProtKB:Q9UPV0, ECO:0000269|PubMed:26337392}. SUBUNIT: Interacts (via N-terminus) with ATRIP. Interacts with ATM, ATR and MDC1. Interacts with XPA (via N-terminus) upon UV irradiation (By similarity). Interacts with CEP83, CCDC92, TTBK2, DVL3, NPHP3 and weakly with NPHP4 (By similarity). {ECO:0000250}. +Q8BR90 CE051_MOUSE UPF0600 protein C5orf51 homolog 294 33,471 Alternative sequence (2); Chain (1); Initiator methionine (1); Modified residue (1) +Q69ZA1 CDK13_MOUSE Cyclin-dependent kinase 13 (EC 2.7.11.22) (EC 2.7.11.23) (CDC2-related protein kinase 5) (Cell division cycle 2-like protein kinase 5) (Cell division protein kinase 13) 1511 164,553 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Cross-link (2); Domain (1); Erroneous initiation (3); Frameshift (1); Modified residue (20); Nucleotide binding (1); Sequence conflict (7) FUNCTION: Cyclin-dependent kinase which displays CTD kinase activity and is required for RNA splicing. Has CTD kinase activity by hyperphosphorylating the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit RPB1, thereby acting as a key regulator of transcription elongation. Required for RNA splicing, probably by phosphorylating SRSF1/SF2. Required during hematopoiesis. {ECO:0000269|PubMed:17261272}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}. SUBUNIT: Interacts with C1QBP (By similarity). Interacts with CCNK, CCNL1 and CCNL2. {ECO:0000250, ECO:0000269|PubMed:17261272, ECO:0000269|PubMed:22012619}. +O35207 CDKA1_MOUSE Cyclin-dependent kinase 2-associated protein 1 (CDK2-associated protein 1) (Deleted in oral cancer 1) (DOC-1) (Putative oral cancer suppressor) 114 12,354 Chain (1); Disulfide bond (1); Modified residue (1); Region (2) FUNCTION: specific inhibitor of the cell-cycle kinase CDK2. {ECO:0000269|PubMed:10938106}. PTM: Phosphorylated in vitro by IKBKE at Ser-45. {ECO:0000250}. SUBUNIT: Homodimer (By similarity). Interacts with monomeric unphosphorylated CDK2 (PubMed:10938106). Interacts with CDK2AP2 (By similarity). {ECO:0000250|UniProtKB:O14519, ECO:0000269|PubMed:10938106}. +P14211 CALR_MOUSE Calreticulin (CRP55) (Calregulin) (Endoplasmic reticulum resident protein 60) (ERp60) (HACBP) 416 47,995 Beta strand (19); Binding site (5); Chain (1); Compositional bias (1); Disulfide bond (1); Helix (5); Metal binding (4); Modified residue (3); Motif (1); Region (6); Repeat (7); Sequence conflict (2); Signal peptide (1); Turn (3) FUNCTION: Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export. Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis (By similarity). {ECO:0000250, ECO:0000269|PubMed:20880849, ECO:0000269|PubMed:21652723}. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138, ECO:0000269|PubMed:8418194}. Cytoplasmic granule {ECO:0000269|PubMed:8418194}. Sarcoplasmic reticulum lumen {ECO:0000250|UniProtKB:P28491}. Note=Associated with the lytic granules in the cytolytic T-lymphocytes. SUBUNIT: Monomer. Interacts with GABARAP, NR3C1, PDIA3/ERp57 and TRIM21. Interacts (via P-domain) with PDIA5 (By similarity). Interacts with PPIB (PubMed:20801878). Interacts with SPACA9 (PubMed:24256100). Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5 (PubMed:16931514). {ECO:0000250|UniProtKB:P18418, ECO:0000250|UniProtKB:P27797, ECO:0000269|PubMed:16931514, ECO:0000269|PubMed:20801878, ECO:0000269|PubMed:24256100}. DOMAIN: Can be divided into a N-terminal globular domain, a proline-rich P-domain forming an elongated arm-like structure and a C-terminal acidic domain. The P-domain binds one molecule of calcium with high affinity, whereas the acidic C-domain binds multiple calcium ions with low affinity (By similarity). {ECO:0000250}.; DOMAIN: The interaction with glycans occurs through a binding site in the globular lectin domain. {ECO:0000250}.; DOMAIN: The zinc binding sites are localized to the N-domain. {ECO:0000250}.; DOMAIN: Associates with PDIA3 through the tip of the extended arm formed by the P-domain. {ECO:0000250}. +Q3V3V9 CARL2_MOUSE Capping protein, Arp2/3 and myosin-I linker protein 2 (Capping protein regulator and myosin 1 linker 2) (F-actin-uncapping protein RLTPR) (Leucine-rich repeat-containing protein 16C) (RGD, leucine-rich repeat, tropomodulin and proline-rich-containing protein) 1296 141,372 Alternative sequence (2); Chain (1); Compositional bias (1); Modified residue (6); Region (2); Repeat (15) FUNCTION: Cell membrane-cytoskeleton-associated protein that plays a role in the regulation of actin polymerization at the barbed end of actin filaments. Prevents F-actin heterodimeric capping protein (CP) activity at the leading edges of migrating cells, and hence generates uncapped barbed ends and enhances actin polymerization. Plays a role in cell protrusion formations; involved in cell polarity, lamellipodial assembly, membrane ruffling and macropinosome formations. Involved as well in cell migration and invadopodia formation during wound healing (By similarity). Required for CD28-mediated stimulation of NF-kappa-B signaling, involved in naive T cells activation, maturation into T memory cells, and differentiation into T helper cells (PubMed:27647348). Required for CD28-mediated differentiation of T regulatory cells (By similarity). {ECO:0000250|UniProtKB:Q6F5E8, ECO:0000269|PubMed:27647348}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6F5E8}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q6F5E8}. Cell membrane {ECO:0000250|UniProtKB:Q6F5E8}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q6F5E8}; Cytoplasmic side {ECO:0000250|UniProtKB:Q6F5E8}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q6F5E8}. Cell projection, ruffle {ECO:0000250|UniProtKB:Q6F5E8}. Note=Colocalizes to dynamic vimentin filaments both in the central cytoplasm and at leading edges of migrating cells. Colocalizes with F-actin, Arp2/3 complex and cortactin to leading edge lamellipodia, ruffles and macropinosomes of migrating cells. {ECO:0000250|UniProtKB:Q6F5E8}. SUBUNIT: Forms homodimers. Interacts (via C-terminus) with heterodimeric capping protein (CP); the interaction inhibits CP activity and hence promotes actin polymerization at the barbed end of actin filaments. {ECO:0000250|UniProtKB:Q6F5E8}. DOMAIN: The N-terminal leucine-rich repeat (LRR) domain is necessary for localization to vimentin filaments. The C-terminus is necessary for localization to the cell membrane. {ECO:0000250|UniProtKB:Q6F5E8}. +P29594 CASP2_MOUSE Caspase-2 (CASP-2) (EC 3.4.22.55) (Neural precursor cell expressed developmentally down-regulated protein 2) (NEDD-2) (Protease ICH-1) [Cleaved into: Caspase-2 subunit p18; Caspase-2 subunit p13; Caspase-2 subunit p12] 452 50,661 Active site (2); Chain (3); Domain (1); Initiator methionine (1); Modified residue (3); Mutagenesis (1); Propeptide (1); Sequence conflict (3) FUNCTION: Involved in the activation cascade of caspases responsible for apoptosis execution. Might function by either activating some proteins required for cell death or inactivating proteins necessary for cell survival (PubMed:7958843). Associates with PIDD1 and CRADD to form the PIDDosome, a complex that activates CASP2 and triggers apoptosis in response to genotoxic stress (By similarity). {ECO:0000250|UniProtKB:P42575, ECO:0000269|PubMed:7958843}. PTM: The mature protease can process its own propeptide, but not that of other caspases. {ECO:0000250}. SUBUNIT: Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a p18 subunit and a p12 subunit. Forms a complex named the PIDDosome with PIDD1 and CRADD. Interacts with NOL3 (via CARD domain); inhibits CASP2 activity in a phosphorylation-dependent manner. {ECO:0000250|UniProtKB:P42575}. DOMAIN: The CARD domain mediates a direct interaction with CRADD. {ECO:0000250|UniProtKB:P42575}. TISSUE SPECIFICITY: High level expression seen in the embryonic CNS, liver, lung, kidney, small intestine, and hair follicles of vibrissae. Moderate expression seen in the skin, oral mucosa, skeletal muscle, submandibular gland and thymus. In the adult, it is highly expressed in spleen, lung and kidney. Moderately in the brain, heart, testis, liver. Low levels in the thymus, skeletal muscle, ovary and gut. +P70403 CASP_MOUSE Protein CASP 678 77,269 Chain (1); Coiled coil (4); Modified residue (1); Sequence conflict (7); Topological domain (2); Transmembrane (1) TRANSMEM 620 640 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 1 619 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 641 678 Lumenal. {ECO:0000255}. FUNCTION: May be involved in intra-Golgi retrograde transport. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. SUBUNIT: Homodimer; disulfide-linked. Interacts with GOLGA5 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:9332351}. +Q9R014 CATJ_MOUSE Cathepsin J (EC 3.4.22.-) (Cathepsin L-related protein) (Cathepsin P) (Catlrp-p) 334 37,276 Active site (3); Chain (1); Disulfide bond (3); Glycosylation (4); Natural variant (1); Propeptide (1); Signal peptide (1) SUBCELLULAR LOCATION: Lysosome {ECO:0000305}. TISSUE SPECIFICITY: Expressed specifically in placenta. {ECO:0000269|PubMed:10526153}. +Q9WVC3 CAV2_MOUSE Caveolin-2 162 18,227 Chain (1); Intramembrane (1); Modified residue (5); Topological domain (2) INTRAMEM 87 107 Helical. {ECO:0000255}. TOPO_DOM 1 86 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 108 162 Cytoplasmic. {ECO:0000255}. FUNCTION: May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity. Acts as an accessory protein in conjunction with CAV1 in targeting to lipid rafts and driving caveolae formation. The Ser-36 phosphorylated form has a role in modulating mitosis in endothelial cells. Positive regulator of cellular mitogenesis of the MAPK signaling pathway. Required for the insulin-stimulated nuclear translocation and activation of MAPK1 and STAT3, and the subsequent regulation of cell cycle progression (By similarity). {ECO:0000250}. PTM: Phosphorylated on serine and tyrosine residues. CAV1 promotes phosphorylation on Ser-23 which then targets the complex to the plasma membrane, lipid rafts and caveolae. Phosphorylation on Ser-36 appears to modulate mitosis in endothelial cells. Phosphorylation on both Tyr-19 and Tyr-27 is required for insulin-induced 'Ser-727' phosphorylation of STAT3 and its activation. Phosphorylation on Tyr-19 is required for insulin-induced phosphorylation of MAPK1 and DNA binding of STAT3. Tyrosine phosphorylation is induced by both EGF and insulin (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein. Cell membrane; Peripheral membrane protein. Membrane, caveola; Peripheral membrane protein. Note=Potential hairpin-like structure in the membrane. Membrane protein of caveolae. Tyr-19-phosphorylated form is enriched at sites of cell-cell contact and is translocated to the nucleus in complex with MAPK1 in response to insulin. Tyr-27-phosphorylated form is located both in the cytoplasm and plasma membrane. CAV1-mediated Ser-23-phosphorylated form locates to the plasma membrane. Ser-36-phosphorylated form resides in intracellular compartments (By similarity). {ECO:0000250}. SUBUNIT: Monomer or homodimer. Interacts with CAV1; the interaction forms a stable heterooligomeric complex that is required for targeting to lipid rafts and for caveolae formation. Tyrosine phosphorylated forms do not form heterooligomers with the Tyr-19-phosphorylated form existing as a monomer or dimer, and the Tyr-27-form as a monomer only. Interacts (tyrosine phosphorylated form) with the SH2 domain-containing proteins, RASA1, NCK1 and SRC. Interacts (tyrosine phosphorylated form) with INSR, the interaction (Tyr-27-phosphorylated form) is increased on insulin stimulation. Interacts (Tyr-19 phosphorylated form) with MAPK1 (phosphorylated form); the interaction, promoted by insulin, leads to nuclear location and MAPK1 activation. Interacts with STAT3; the interaction is increased on insulin-induced tyrosine phosphorylation leading to STAT activation (By similarity). {ECO:0000250}. +P70269 CATE_MOUSE Cathepsin E (EC 3.4.23.34) 397 42,938 Active site (2); Chain (1); Disulfide bond (3); Domain (1); Glycosylation (2); Propeptide (1); Sequence conflict (7); Signal peptide (1) FUNCTION: May have a role in immune function. Probably involved in the processing of antigenic peptides during MHC class II-mediated antigen presentation. May play a role in activation-induced lymphocyte depletion in the thymus, and in neuronal degeneration and glial cell activation in the brain. {ECO:0000269|PubMed:11719510, ECO:0000269|PubMed:1601038}. PTM: Glycosylated. The nature of the carbohydrate chain varies between cell types. In fibroblasts, the proenzyme contains a high mannose-type oligosaccharide, while the mature enzyme contains a complex-type oligosaccharide. {ECO:0000269|PubMed:7983070}. SUBCELLULAR LOCATION: Endosome {ECO:0000269|PubMed:1601038}. Note=The proenzyme is localized to the endoplasmic reticulum and Golgi apparatus, while the mature enzyme is localized to the endosome. SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}. TISSUE SPECIFICITY: Expressed abundantly in the stomach, Clara cells and alveolar macrophages of the lung, brain microglia, spleen and activated B-lymphocytes. Not expressed in resting B-lymphocytes. {ECO:0000269|PubMed:11322887, ECO:0000269|Ref.3}. +Q8C3M9 CB080_MOUSE Uncharacterized protein C2orf80 homolog 231 25,767 Chain (1) +Q66L44 CBARP_MOUSE Voltage-dependent calcium channel beta subunit-associated regulatory protein (Downstream of Stk11 protein) 698 74,131 Chain (1); Glycosylation (1); Modified residue (9); Mutagenesis (3); Sequence caution (1); Sequence conflict (3); Topological domain (2); Transmembrane (1) TRANSMEM 42 62 Helical; Signal-anchor for type III membrane protein. {ECO:0000255}. TOPO_DOM 1 41 Extracellular. {ECO:0000269|PubMed:24751537}.; TOPO_DOM 63 698 Cytoplasmic. {ECO:0000269|PubMed:24751537}. FUNCTION: Negatively regulates voltage-gated calcium channels by preventing the interaction between their alpha and beta subunits. Thereby, negatively regulates calcium channels activity at the plasma membrane and indirectly inhibits calcium-regulated exocytosis. {ECO:0000269|PubMed:24751537}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:24751537}; Single-pass type III membrane protein {ECO:0000305|PubMed:24751537}. Cell membrane {ECO:0000269|PubMed:24751537}; Single-pass type III membrane protein {ECO:0000305|PubMed:24751537}. Cell projection, growth cone {ECO:0000269|PubMed:24751537}. SUBUNIT: Interacts with voltage-dependent calcium channels CACNB1, CACNB2, CACNB3 and CACNB4 beta subunits; prevents their interaction with the CACNA1C alpha subunit thereby negatively regulating the activity of the corresponding calcium channels. {ECO:0000269|PubMed:24751537}. TISSUE SPECIFICITY: Expressed by neurons in the cortex, cerebellum and hippocampus and by pancreatic beta cells (at protein level). {ECO:0000269|PubMed:24751537}. +P15089 CBPA3_MOUSE Mast cell carboxypeptidase A (MC-CPA) (EC 3.4.17.1) (Carboxypeptidase A3) 417 48,790 Active site (1); Chain (1); Disulfide bond (2); Metal binding (3); Propeptide (1); Signal peptide (1) SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle. Note=Secretory granules. +Q09M05 CBPC4_MOUSE Cytosolic carboxypeptidase 4 (EC 3.4.17.-) (ATP/GTP-binding protein-like 1) 972 109,368 Active site (1); Alternative sequence (5); Chain (1); Compositional bias (1); Metal binding (3); Mutagenesis (2); Sequence conflict (2) FUNCTION: Metallocarboxypeptidase that mediates deglutamylation of target proteins. Catalyzes the deglutamylation of polyglutamate side chains generated by post-translational polyglutamylation in proteins such as tubulins. Also removes gene-encoded polyglutamates from the carboxy-terminus of target proteins such as MYLK. Acts as a long-chain deglutamylase and specifically shortens long polyglutamate chains, while it is not able to remove the branching point glutamate, a process catalyzed by AGBL5/CCP5. {ECO:0000269|PubMed:21074048, ECO:0000269|PubMed:25103237}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q96MI9}. SUBUNIT: Interacts with TCF4 (By similarity). Interacts with MYLK. {ECO:0000250, ECO:0000269|PubMed:21074048}. TISSUE SPECIFICITY: Widely expressed at low level. Expressed in eye, muscle, pituitary, testis and to a lower extent in brain. {ECO:0000269|PubMed:17244818, ECO:0000269|PubMed:21074048, ECO:0000269|PubMed:25103237}. +Q9JHG0 CBLN3_MOUSE Cerebellin-3 197 21,077 Chain (1); Disulfide bond (2); Domain (1); Glycosylation (1); Mutagenesis (1); Region (1); Signal peptide (1) FUNCTION: May be involved in synaptic functions in the CNS. SUBCELLULAR LOCATION: Endoplasmic reticulum. Golgi apparatus, cis-Golgi network. Secreted. Cell junction, synapse. Note=In the absence of CBLN1, remains in the endoplasmic reticulum/cis-Golgi apparatus. Partial secretion depends on an association with CBLN1 and maybe CBLN4, but not on CBLN2. SUBUNIT: Heterohexamer; disulfide-linked heterotrimers (By similarity). Interacts with CBLN1. May also form oligomers with CBLN2 AND CBLN4. {ECO:0000250, ECO:0000269|PubMed:10964938, ECO:0000269|PubMed:17030622}. TISSUE SPECIFICITY: Expressed in brain, restricted to the cerebellar cortex. Within the cerebellum, expressed in granule layers (at protein level). Also detected in postsynaptic Purkinje cell spines (at protein level). {ECO:0000269|PubMed:16930405, ECO:0000269|PubMed:17331201}. +Q0VF22 CC138_MOUSE Coiled-coil domain-containing protein 138 680 77,947 Chain (1); Coiled coil (1); Modified residue (3) +Q00493 CBPE_MOUSE Carboxypeptidase E (CPE) (EC 3.4.17.10) (Carboxypeptidase H) (CPH) (Enkephalin convertase) (Prohormone-processing carboxypeptidase) 476 53,256 Active site (1); Chain (1); Glycosylation (2); Metal binding (3); Natural variant (1); Propeptide (1); Sequence conflict (11); Signal peptide (1) FUNCTION: Removes residual C-terminal Arg or Lys remaining after initial endoprotease cleavage during prohormone processing. Processes proinsulin. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:P15087}; Peripheral membrane protein {ECO:0000250|UniProtKB:P15087}. Secreted {ECO:0000250|UniProtKB:P15087}. Note=Associated with the secretory granule membrane through direct binding to lipid rafts in intragranular conditions. {ECO:0000250|UniProtKB:P15087}. DISEASE: Note=Defects in Cpe are the cause of the fat phenotype. Mice homozygous for the fat mutation develop obesity and hyperglycemia that can be suppressed by treatment with exogenous insulin. {ECO:0000269|PubMed:7663508}. +Q641K1 CBPC1_MOUSE Cytosolic carboxypeptidase 1 (EC 3.4.17.-) (ATP/GTP-binding protein 1) (Nervous system nuclear protein induced by axotomy protein 1) 1218 137,197 Active site (1); Alternative sequence (7); Chain (1); Erroneous initiation (1); Metal binding (3); Modified residue (1); Mutagenesis (5); Natural variant (1); Sequence conflict (10) FUNCTION: Metallocarboxypeptidase that mediates deglutamylation of target proteins. Catalyzes the deglutamylation of polyglutamate side chains generated by post-translational polyglutamylation in proteins such as tubulins. Also removes gene-encoded polyglutamates from the carboxy-terminus of target proteins such as MYLK. Acts as a long-chain deglutamylase and specifically shortens long polyglutamate chains, while it is not able to remove the branching point glutamate, a process catalyzed by AGBL5/CCP5. Deglutamylation plays a key role in cerebellar Purkinje cell differentiation, accumulation of tubulin polyglutamylation causing neurodegeneration. {ECO:0000269|PubMed:21074048, ECO:0000269|PubMed:25103237}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UPW5}. Cytoplasm, cytosol {ECO:0000269|PubMed:11083920}. Nucleus {ECO:0000269|PubMed:11083920}. Mitochondrion {ECO:0000269|PubMed:20620870}. Note=Localizes in both the cytoplasm and nuclei of interphase and dividing cells. {ECO:0000250|UniProtKB:Q9UPW5}. SUBUNIT: Interacts with MYLK. {ECO:0000269|PubMed:21074048}. TISSUE SPECIFICITY: Widely expressed. Highly expressed in the cerebellum and cortex of adult mouse brain. Expressed at similar levels in both the cerebellum and the cortex throughout all developmental stages. Also expressed in sciatic nerve transection, spinal motor neurons undergoing axon regeneration, testis, heart and in developing brain. Expression in cranial motor nuclei is the same as that observed in uninjured primary motor neurons. Expression is prevalent in sensory neurons and hippocampal CA3 neurons in addition to regenerating motor neurons. {ECO:0000269|PubMed:11884758, ECO:0000269|PubMed:21074048, ECO:0000269|PubMed:25103237}. DISEASE: Note=Defects in Agtpbp1 are the cause of Purkinje cell degeneration (pcd). Pcd is a spontaneous mutation that causes adult-onset degeneration of cerebellar Purkinje neurons, retinal photoreceptors, olfactory bulb mitral neurons, and selected thalamic neurons, and has defective spermatogenesis. Defects in mitochondrial metabolic functions are also observed. The molecular causes of neurodegeneration are still unclear, but they are probably due to an accumulation of glutamylation, either tubulin hyperglutamylation or another hyperglutamylated target proteins. An increase of intranuclear localization of lysyl oxidase (Lox) propeptide, which interferes with NF-kappa-B Rela signaling and microtubule-associated protein regulation of microtubule stability is also observed, possibly leading to underdevelopment of Purkinje cell dendrites. {ECO:0000269|PubMed:11884758, ECO:0000269|PubMed:16465590, ECO:0000269|PubMed:16942761, ECO:0000269|PubMed:16952463, ECO:0000269|PubMed:18602413, ECO:0000269|PubMed:20620870, ECO:0000269|PubMed:20920790, ECO:0000269|PubMed:21074048}. +P51676 CC1L1_MOUSE C-C chemokine receptor 1-like protein 1 (Macrophage inflammatory protein 1 alpha receptor-like 1) 356 40,849 Chain (1); Disulfide bond (1); Sequence conflict (3); Topological domain (8); Transmembrane (7) TRANSMEM 33 60 Helical; Name=1. {ECO:0000255}.; TRANSMEM 68 92 Helical; Name=2. {ECO:0000255}.; TRANSMEM 109 130 Helical; Name=3. {ECO:0000255}.; TRANSMEM 148 172 Helical; Name=4. {ECO:0000255}.; TRANSMEM 199 224 Helical; Name=5. {ECO:0000255}.; TRANSMEM 241 265 Helical; Name=6. {ECO:0000255}.; TRANSMEM 283 306 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 32 Extracellular. {ECO:0000255}.; TOPO_DOM 61 67 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 93 108 Extracellular. {ECO:0000255}.; TOPO_DOM 131 147 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 173 198 Extracellular. {ECO:0000255}.; TOPO_DOM 225 240 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 266 282 Extracellular. {ECO:0000255}.; TOPO_DOM 307 356 Cytoplasmic. {ECO:0000255}. FUNCTION: Probable receptor for a C-C type chemokine. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Detected in the spleen, liver and leukocytes. +Q8CDI7 CC150_MOUSE Coiled-coil domain-containing protein 150 1110 128,502 Chain (1); Coiled coil (4); Sequence conflict (1) +Q8C3X2 CC90B_MOUSE Coiled-coil domain-containing protein 90B, mitochondrial 256 29,597 Alternative sequence (1); Chain (1); Coiled coil (1); Sequence conflict (1); Transit peptide (1); Transmembrane (1) TRANSMEM 231 253 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250|UniProtKB:Q9GZT6}; Single-pass membrane protein {ECO:0000255}. SUBUNIT: Interacts with MCU. {ECO:0000250|UniProtKB:Q9GZT6}. +Q9D8X2 CC124_MOUSE Coiled-coil domain-containing protein 124 217 25,346 Chain (1); Coiled coil (1); Modified residue (2); Sequence conflict (2) FUNCTION: Required for proper progression of late cytokinetic stages. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Midbody {ECO:0000250}. Note=Colocalizes with gamma-tubulin at interphase, prophase, metaphase, and anaphase. Relocates from centrosome to midbody at telophase (By similarity). {ECO:0000250}. SUBUNIT: Interacts with RASGEF1B. {ECO:0000250}. +Q8BMK5 CC184_MOUSE Coiled-coil domain-containing protein 184 191 20,184 Alternative sequence (1); Chain (1); Coiled coil (1); Erroneous initiation (2); Sequence conflict (1) +Q8BHG3 CC50B_MOUSE Cell cycle control protein 50B (Transmembrane protein 30B) 353 39,218 Chain (1); Compositional bias (1); Glycosylation (2); Topological domain (3); Transmembrane (2) TRANSMEM 34 54 Helical. {ECO:0000255}.; TRANSMEM 316 336 Helical. {ECO:0000255}. TOPO_DOM 1 33 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 55 315 Exoplasmic loop. {ECO:0000255}.; TOPO_DOM 337 353 Cytoplasmic. {ECO:0000255}. FUNCTION: Accessory component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. The beta subunit may assist in binding of the phospholipid substrate (Probable). Can mediate the export of alpha subunits ATP8A1, ATP8B1, ATP8B2 and ATP8B4 from the ER to the plasma membrane (By similarity). {ECO:0000250, ECO:0000305}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein. SUBUNIT: Component of a P4-ATPase flippase complex which consists of a catalytic alpha subunit and an accessory beta subunit (Probable). Interacts with alpha subunits ATP8A1, ATP8B1, ATP8B2 and ATP8B4 (By similarity). {ECO:0000250, ECO:0000305}. +Q9D4D7 CC50C_MOUSE Cell cycle control protein 50C (Transmembrane protein 30C) 342 38,604 Chain (1); Glycosylation (4); Sequence conflict (5); Topological domain (3); Transmembrane (2) TRANSMEM 34 54 Helical. {ECO:0000255}.; TRANSMEM 307 327 Helical. {ECO:0000255}. TOPO_DOM 1 33 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 55 306 Extracellular. {ECO:0000255}.; TOPO_DOM 328 342 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Specifically expressed in testis. {ECO:0000269|PubMed:17258408}. +Q3UI66 CCD34_MOUSE Coiled-coil domain-containing protein 34 367 42,216 Chain (1); Coiled coil (2); Compositional bias (1); Modified residue (1) +Q9D6Y1 CCDC3_MOUSE Coiled-coil domain-containing protein 3 (Fat/vessel-derived secretory protein) (Favine) 273 31,093 Chain (1); Coiled coil (1); Glycosylation (1); Signal peptide (1) FUNCTION: Negatively regulates TNF-alpha-induced pro-inflammatory response in endothelial cells (ECs) via inhibition of TNF-alpha-induced NF-kappaB activation in ECs (By similarity). Positively regulates lipid accumulation in adipose cells (PubMed:25605713). {ECO:0000250|UniProtKB:Q9BQI4, ECO:0000269|PubMed:25605713}. PTM: N-glycosylated. {ECO:0000269|PubMed:20043878}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20043878}. SUBUNIT: Homodimer. {ECO:0000269|PubMed:20043878}. TISSUE SPECIFICITY: Expressed in aorta and adipose tissue. Enriched in mature adipocytes. Over-expressed in adipose tissue from either hormonally-induced or nutritionally-regulated obese mice models. {ECO:0000269|PubMed:20043878}. +P14097 CCL4_MOUSE C-C motif chemokine 4 (Immune activation protein 2) (ACT-2) (ACT2) (Macrophage inflammatory protein 1-beta) (MIP-1-beta) (Protein H400) (SIS-gamma) (Small-inducible cytokine A4) 92 10,168 Chain (1); Disulfide bond (2); Signal peptide (1) FUNCTION: Monokine with inflammatory and chemokinetic properties. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Homodimer. {ECO:0000250}. +Q9D8L5 CCD91_MOUSE Coiled-coil domain-containing protein 91 (GGA-binding partner) 442 50,007 Alternative sequence (3); Chain (1); Coiled coil (3); Erroneous initiation (1); Modified residue (2); Region (2); Sequence conflict (1) FUNCTION: Involved in the regulation of membrane traffic through the trans-Golgi network (TGN). Functions in close cooperation with the GGAs in the sorting of hydrolases to lysosomes. {ECO:0000250|UniProtKB:Q7Z6B0}. SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q7Z6B0}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q7Z6B0}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q7Z6B0}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q7Z6B0}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q7Z6B0}. Note=Colocalizes with GGA1, GGA2 and GGA3. {ECO:0000250|UniProtKB:Q7Z6B0}. SUBUNIT: Homodimer. Interacts with GGA1, GGA2 and AP1G1. {ECO:0000250|UniProtKB:Q7Z6B0}. +Q9D9B0 CCD70_MOUSE Coiled-coil domain-containing protein 70 223 27,598 Chain (1); Coiled coil (1); Sequence conflict (3); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +P51680 CCR4_MOUSE C-C chemokine receptor type 4 (C-C CKR-4) (CC-CKR-4) (CCR-4) (CCR4) (CD antigen CD194) 360 41,408 Chain (1); Compositional bias (1); Disulfide bond (1); Glycosylation (3); Sequence conflict (9); Topological domain (8); Transmembrane (7) TRANSMEM 40 67 Helical; Name=1. {ECO:0000255}.; TRANSMEM 78 98 Helical; Name=2. {ECO:0000255}.; TRANSMEM 112 133 Helical; Name=3. {ECO:0000255}.; TRANSMEM 151 175 Helical; Name=4. {ECO:0000255}.; TRANSMEM 207 226 Helical; Name=5. {ECO:0000255}.; TRANSMEM 243 267 Helical; Name=6. {ECO:0000255}.; TRANSMEM 285 308 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 39 Extracellular. {ECO:0000255}.; TOPO_DOM 68 77 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 99 111 Extracellular. {ECO:0000255}.; TOPO_DOM 134 150 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 176 206 Extracellular. {ECO:0000255}.; TOPO_DOM 227 242 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 268 284 Extracellular. {ECO:0000255}.; TOPO_DOM 309 360 Cytoplasmic. {ECO:0000255}. FUNCTION: High affinity receptor for the C-C type chemokines CCL17/TARC and CCL22/MDC. The activity of this receptor is mediated by G(i) proteins which activate a phosphatidylinositol-calcium second messenger system. Could play a role in lipopolysaccharide (LPS)-induced endotoxic shock. In the CNS, could mediate hippocampal-neuron survival. {ECO:0000269|PubMed:10811868}. PTM: In natural killer cells, CCL22 binding induces phosphorylation on yet undefined Ser/Thr residues, most probably by beta-adrenergic receptor kinases 1 and 2. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed in the thymus, macrophages and T- and B-cells. +P30276 CCNB2_MOUSE G2/mitotic-specific cyclin-B2 398 45,383 Chain (1); Modified residue (6); Sequence conflict (5) FUNCTION: Essential for the control of the cell cycle at the G2/M (mitosis) transition. SUBUNIT: Interacts with the CDK1 protein kinase to form a serine/threonine kinase holoenzyme complex also known as maturation promoting factor (MPF). The cyclin subunit imparts substrate specificity to the complex. +Q61458 CCNH_MOUSE Cyclin-H 323 37,506 Chain (1); Compositional bias (1); Modified residue (5) FUNCTION: Regulates CDK7, the catalytic subunit of the CDK-activating kinase (CAK) enzymatic complex. CAK activates the cyclin-associated kinases CDK1, CDK2, CDK4 and CDK6 by threonine phosphorylation. CAK complexed to the core-TFIIH basal transcription factor activates RNA polymerase II by serine phosphorylation of the repetitive C-terminal domain (CTD) of its large subunit (POLR2A), allowing its escape from the promoter and elongation of the transcripts. Involved in cell cycle control and in RNA transcription by RNA polymerase II. Its expression and activity are constant throughout the cell cycle. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Associates primarily with CDK7 and MAT1 to form the CAK complex. CAK can further associate with the core-TFIIH to form the TFIIH basal transcription factor. TISSUE SPECIFICITY: Expressed in both the germinal and somatic cells of the testis. +Q9JJA7 CCNL2_MOUSE Cyclin-L2 (Cyclin Ania-6b) (Paneth cell-enhanced expression protein) (PCEE) 518 58,005 Alternative sequence (3); Chain (1); Erroneous initiation (1); Erroneous termination (1); Modified residue (5); Region (3); Sequence conflict (12) FUNCTION: Involved in pre-mRNA splicing. May induce cell death, possibly by acting on the transcription and RNA processing of apoptosis-related factors. {ECO:0000250|UniProtKB:Q96S94}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q96S94}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q96S94}. SUBUNIT: Interacts with CDK11A, CDK11B, CDK12, CDK13 and POLR2A, the hyperphosphorylated C-terminal domain (CTD) of RNA polymerase II. May form a ternary complex with CDK11B and casein kinase II (CKII). Interacts with pre-mRNA-splicing factors, including at least SRSF1, SRSF2 AND SRSF7/SLU7. {ECO:0000250|UniProtKB:Q96S94, ECO:0000269|PubMed:17261272}. DOMAIN: Contains a RS region (arginine-serine dipeptide repeat) within the C-terminal domain which is the hallmark of the SR family of splicing factors. This region probably plays a role in protein-protein interactions (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed (at protein level). {ECO:0000269|PubMed:18216018}. +P51682 CCR5_MOUSE C-C chemokine receptor type 5 (C-C CKR-5) (CC-CKR-5) (CCR-5) (MIP-1 alpha receptor) (CD antigen CD195) 354 40,785 Chain (1); Disulfide bond (2); Glycosylation (1); Lipidation (2); Modified residue (7); Natural variant (7); Sequence conflict (9); Topological domain (8); Transmembrane (7) TRANSMEM 33 60 Helical; Name=1. {ECO:0000255}.; TRANSMEM 71 91 Helical; Name=2. {ECO:0000255}.; TRANSMEM 105 126 Helical; Name=3. {ECO:0000255}.; TRANSMEM 144 168 Helical; Name=4. {ECO:0000255}.; TRANSMEM 201 220 Helical; Name=5. {ECO:0000255}.; TRANSMEM 238 262 Helical; Name=6. {ECO:0000255}.; TRANSMEM 280 303 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 32 Extracellular. {ECO:0000255}.; TOPO_DOM 61 70 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 92 104 Extracellular. {ECO:0000255}.; TOPO_DOM 127 143 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 169 200 Extracellular. {ECO:0000255}.; TOPO_DOM 221 237 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 263 279 Extracellular. {ECO:0000255}.; TOPO_DOM 304 354 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for a number of inflammatory CC-chemokines including MIP-1-alpha, MIP-1-beta and RANTES and subsequently transduces a signal by increasing the intracellular calcium ion level. May play a role in the control of granulocytic lineage proliferation or differentiation (By similarity). {ECO:0000250|UniProtKB:P51681}. PTM: Sulfated on at least 2 of the N-terminal tyrosines. Sulfation is required for efficient binding of the chemokines, CCL3 and CCL4 (By similarity). {ECO:0000250|UniProtKB:P51681}.; PTM: O-glycosylated, but not N-glycosylated. Ser-6 appears to be the major site. Also sialylated glycans present which contribute to chemokine binding (By similarity). {ECO:0000250|UniProtKB:P51681}.; PTM: Palmitoylation in the C-terminal is important for cell surface expression. {ECO:0000250|UniProtKB:P51681}.; PTM: Phosphorylation on serine residues in the C-terminal is stimulated by binding CC chemokines especially by APO-RANTES. {ECO:0000250|UniProtKB:P51681}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBUNIT: Interacts with PRAF2. Efficient ligand binding to CCL3/MIP-1alpha and CCL4/MIP-1beta requires sulfation, O-glycosylation and sialic acid modifications. Glycosylation on Ser-6 is required for efficient binding of CCL4. Interacts with GRK2. Interacts with ARRB1 and ARRB2. Interacts with CNIH4. {ECO:0000250|UniProtKB:P51681}. +P47774 CCR7_MOUSE C-C chemokine receptor type 7 (C-C CKR-7) (CC-CKR-7) (CCR-7) (Epstein-Barr virus-induced G-protein coupled receptor 1) (EBI1) (EBV-induced G-protein coupled receptor 1) (MIP-3 beta receptor) (CD antigen CD197) 378 42,856 Chain (1); Disulfide bond (1); Glycosylation (1); Sequence conflict (1); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 60 86 Helical; Name=1. {ECO:0000255}.; TRANSMEM 96 116 Helical; Name=2. {ECO:0000255}.; TRANSMEM 131 152 Helical; Name=3. {ECO:0000255}.; TRANSMEM 171 191 Helical; Name=4. {ECO:0000255}.; TRANSMEM 220 247 Helical; Name=5. {ECO:0000255}.; TRANSMEM 264 289 Helical; Name=6. {ECO:0000255}.; TRANSMEM 314 331 Helical; Name=7. {ECO:0000255}. TOPO_DOM 25 59 Extracellular. {ECO:0000255}.; TOPO_DOM 87 95 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 117 130 Extracellular. {ECO:0000255}.; TOPO_DOM 153 170 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 192 219 Extracellular. {ECO:0000255}.; TOPO_DOM 248 263 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 290 313 Extracellular. {ECO:0000255}.; TOPO_DOM 332 378 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for the MIP-3-beta chemokine. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +P56484 CCR8_MOUSE C-C chemokine receptor type 8 (C-C CKR-8) (CC-CKR-8) (CCR-8) (CD antigen CDw198) 353 40,045 Chain (1); Disulfide bond (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 34 61 Helical; Name=1. {ECO:0000255}.; TRANSMEM 72 91 Helical; Name=2. {ECO:0000255}.; TRANSMEM 106 127 Helical; Name=3. {ECO:0000255}.; TRANSMEM 145 169 Helical; Name=4. {ECO:0000255}.; TRANSMEM 201 220 Helical; Name=5. {ECO:0000255}.; TRANSMEM 237 261 Helical; Name=6. {ECO:0000255}.; TRANSMEM 279 302 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 33 Extracellular. {ECO:0000255}.; TOPO_DOM 62 71 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 92 105 Extracellular. {ECO:0000255}.; TOPO_DOM 128 144 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 170 200 Extracellular. {ECO:0000255}.; TOPO_DOM 221 236 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 262 278 Extracellular. {ECO:0000255}.; TOPO_DOM 303 353 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for the CCL1/SCY1/TCA-3 chemokine. {ECO:0000269|PubMed:9469461}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed in thymus. {ECO:0000269|PubMed:9469461}. +Q8C1Y8 CCZ1_MOUSE Vacuolar fusion protein CCZ1 homolog 480 55,505 Chain (1); Initiator methionine (1); Modified residue (3) FUNCTION: Acts in concert with MON1A, as a guanine exchange factor (GEF) for RAB7, promotes the exchange of GDP to GTP, converting it from an inactive GDP-bound form into an active GTP-bound form. {ECO:0000250|UniProtKB:P86791}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250}. SUBUNIT: Interacts with MON1A. Found in a complex with RMC1, CCZ1 MON1A and MON1B. {ECO:0000250|UniProtKB:P86791}. +Q9WU84 CCS_MOUSE Copper chaperone for superoxide dismutase (Superoxide dismutase copper chaperone) 274 28,912 Chain (1); Cross-link (4); Disulfide bond (1); Domain (1); Metal binding (8); Modified residue (1); Region (1) FUNCTION: Delivers copper to copper zinc superoxide dismutase (SOD1). PTM: Ubiquitinion by XIAP/BIRC4 leads to enhancement of its chaperone activity toward its physiologic target, SOD1, rather than proteasomal degradation. XIAP/BIRC4 preferentially ubiquitinates at Lys-241 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homodimer, and heterodimer with SOD1. Interacts with COMMD1 (By similarity). Interacts with XIAP/BIRC4 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. +O35566 CD151_MOUSE CD151 antigen (GP27) (Membrane glycoprotein SFA-1) (Platelet-endothelial tetraspan antigen 3) (PETA-3) (CD antigen CD151) 253 28,246 Chain (1); Glycosylation (1); Lipidation (4); Sequence conflict (1); Topological domain (5); Transmembrane (4) TRANSMEM 19 39 Helical. {ECO:0000255}.; TRANSMEM 58 78 Helical. {ECO:0000255}.; TRANSMEM 92 112 Helical. {ECO:0000255}.; TRANSMEM 222 242 Helical. {ECO:0000255}. TOPO_DOM 1 18 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 40 57 Extracellular. {ECO:0000255}.; TOPO_DOM 79 91 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 113 221 Extracellular. {ECO:0000255}.; TOPO_DOM 243 253 Cytoplasmic. {ECO:0000255}. FUNCTION: Essential for the proper assembly of the glomerular and tubular basement membranes in kidney. {ECO:0000250|UniProtKB:P48509}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SUBUNIT: Interacts with integrins ITGA3:ITGB1, ITGA5:ITGB1, ITGA3:ITGB1 and ITGA6:ITGB4 and with CD9 and CD181. Interacts (via the second extracellular domain) with integrin ITGAV:ITGB3. {ECO:0000250|UniProtKB:P48509}. +Q3UUX7 CD046_MOUSE Uncharacterized protein C4orf46 homolog 111 11,861 Chain (1); Sequence conflict (1) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q504U0}. +Q8R2S8 CD177_MOUSE CD177 antigen (CD antigen CD177) 817 87,091 Chain (1); Domain (4); Glycosylation (4); Signal peptide (1); Topological domain (1); Transmembrane (1) TRANSMEM 797 817 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 22 796 Extracellular. {ECO:0000305}. FUNCTION: In association with beta-2 integrin heterodimer ITGAM/CD11b and ITGB2/CD18, mediates activation of TNF-alpha primed neutrophils including degranulation and superoxide production (By similarity). In addition, by preventing beta-2 integrin internalization and attenuating chemokine signaling favors adhesion over migration (By similarity). Heterophilic interaction with PECAM1 on endothelial cells plays a role in neutrophil transendothelial migration in vitro (By similarity). However, appears to be dispensable for neutrophil recruitment caused by bacterial infection in vivo (PubMed:25359465). Acts as a receptor for the mature form of protease PRTN3 allowing its display at the cell surface of neutrophils (By similarity). By displaying PRTN3 at the neutrophil cell surface, may play a role in enhancing endothelial cell junctional integrity and thus vascular integrity during neutrophil diapedesis (By similarity). {ECO:0000250|UniProtKB:Q8N6Q3, ECO:0000269|PubMed:25359465}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25359465}; Single-pass type IV membrane protein {ECO:0000305}. SUBUNIT: Found in a complex with integrin ITGAM/CD11b and ITGB2/CD18. Interacts with PECAM1 (via Ig-like C2-type domain 6); the interaction is Ca(2+)-dependent; the interaction is direct. Interacts with serine protease PRTN3/myeloblastin; the interaction tethers PRTN3 to the cell surface; the interaction is direct. {ECO:0000250|UniProtKB:Q8N6Q3}. TISSUE SPECIFICITY: Expressed in neutrophils. {ECO:0000269|PubMed:25359465}. +O55186 CD59A_MOUSE CD59A glycoprotein (MAC-inhibitory protein) (MAC-IP) (Membrane attack complex inhibition factor) (MACIF) (Protectin) (CD antigen CD59) 123 13,648 Chain (1); Disulfide bond (5); Domain (1); Glycosylation (2); Lipidation (1); Propeptide (1); Signal peptide (1) FUNCTION: Potent inhibitor of the complement membrane attack complex (MAC) action. Acts by binding to the C8 and/or C9 complements of the assembling MAC, thereby preventing incorporation of the multiple copies of C9 required for complete formation of the osmolytic pore (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. TISSUE SPECIFICITY: Expressed in all tissues examined (liver, kidney, spleen, thymus, brain and heart). Low levels in thymus. Also expressed in mononuclear cells, erythrocytes and platelets. Barely detected in neutrophils. +Q62192 CD180_MOUSE CD180 antigen (Lymphocyte antigen 78) (Ly-78) (Radioprotective 105 kDa protein) (CD antigen CD180) 661 74,302 Beta strand (29); Chain (1); Domain (2); Glycosylation (10); Helix (17); Repeat (19); Sequence conflict (5); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (13) TRANSMEM 627 650 Helical. {ECO:0000255}. TOPO_DOM 21 626 Extracellular.; TOPO_DOM 651 661 Cytoplasmic. FUNCTION: May cooperate with MD-1 and TLR4 to mediate the innate immune response to bacterial lipopolysaccharide (LPS) in B-cells. Leads to NF-kappa-B activation. Also involved in the life/death decision of B-cells. {ECO:0000269|PubMed:10880523}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SUBUNIT: M-shaped tetramer of two CD180-LY86 heterodimers. {ECO:0000269|PubMed:21959264}. TISSUE SPECIFICITY: B-lymphocytes and spleen. Not detected in thymus, kidney, muscle, heart, brain or liver. +Q8BMD5 CDAC1_MOUSE Cytidine and dCMP deaminase domain-containing protein 1 523 59,062 Active site (1); Alternative sequence (8); Chain (1); Domain (2); Frameshift (1); Metal binding (3); Sequence conflict (4) FUNCTION: May play an important role in testicular development and spermatogenesis. {ECO:0000250}. +P61809 CD5R1_MOUSE Cyclin-dependent kinase 5 activator 1 (CDK5 activator 1) (Cyclin-dependent kinase 5 regulatory subunit 1) (TPKII regulatory subunit) [Cleaved into: Cyclin-dependent kinase 5 activator 1, p35 (p35); Cyclin-dependent kinase 5 activator 1, p25 (p25) (Tau protein kinase II 23 kDa subunit) (p23)] 307 34,031 Chain (2); Initiator methionine (1); Lipidation (1); Modified residue (2); Mutagenesis (1); Site (1) FUNCTION: p35 is a neuron specific activator of CDK5. The complex p35/CDK5 is required for neurite outgrowth and cortical lamination. Involved in dendritic spine morphogenesis by mediating the EFNA1-EPHA4 signaling. Activator of TPKII. The complex p35/CDK5 participates in the regulation of the circadian clock by modulating the function of CLOCK protein: phosphorylates CLOCK at 'Thr-451' and 'Thr-461' and regulates the transcriptional activity of the CLOCK-ARNTL/BMAL1 heterodimer in association with altered stability and subcellular distribution. {ECO:0000269|PubMed:17143272, ECO:0000269|PubMed:24235147}. PTM: The p35 form is proteolytically cleaved by calpain, giving rise to the p25 form. P35 has a 5 to 10 fold shorter half-life compared to p25. The conversion results in deregulation of the CDK5 kinase: p25/CDK5 kinase displays an increased and altered tau phosphorylation in comparison to the p35/CDK5 kinase in vivo. {ECO:0000269|PubMed:10830966}.; PTM: Myristoylated. A proper myristoylation signal is essential for the proper distribution of p35 (By similarity). {ECO:0000250}.; PTM: Ubiquitinated. Degradation of p35 by proteasome results in down-regulation of CDK5 activity. During this process, CDK5 phosphorylates p35 and induces its ubiquitination and subsequent degradation (By similarity). {ECO:0000250}.; PTM: Phosphorylation at Ser-8 and Thr-138 by CDK5 prevents calpain-mediated proteolysis. {ECO:0000250}. SUBCELLULAR LOCATION: Cyclin-dependent kinase 5 activator 1, p35: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}.; SUBCELLULAR LOCATION: Cyclin-dependent kinase 5 activator 1, p25: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=The conversion of p35 to p25 relocalizes the protein from the cell periphery to the cytoplasm, in nuclear and perinuclear regions. {ECO:0000250}. SUBUNIT: Heterodimer composed of CDK5 and CDK5R (p25) and macromolecular complex composed of at least CDK5, CDK5R (p35) and CDK5RAP1 or CDK5RAP2 or CDK5RAP3. Only the heterodimer shows kinase activity. Interacts with RASGRF2 (By similarity). Interacts with EPHA4 and NGEF; may mediate the activation of NGEF by EPHA4. The complex p35/CDK5 interacts with CLOCK. {ECO:0000250, ECO:0000269|PubMed:11882646, ECO:0000269|PubMed:17143272, ECO:0000269|PubMed:24235147}. TISSUE SPECIFICITY: Brain and neuron specific. +O89033 CDC6_MOUSE Cell division control protein 6 homolog (CDC6-related protein) (p62(cdc6)) 562 62,614 Chain (1); Erroneous initiation (2); Modified residue (6); Nucleotide binding (1); Sequence conflict (1) FUNCTION: Involved in the initiation of DNA replication. Also participates in checkpoint controls that ensure DNA replication is completed before mitosis is initiated. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q99741}. Cytoplasm {ECO:0000250|UniProtKB:Q99741}. Note=The protein is nuclear in G1 and cytoplasmic in S-phase cells. {ECO:0000250|UniProtKB:Q99741}. SUBUNIT: Interacts with PCNA, ORC1, cyclin-CDK. Interacts with HUWE1. Interacts with ANKRD17. Interacts with GRWD1; origin binding of GRWD1 is dependent on CDC6. Interacts with CDT1; are mutually dependent on one another for loading MCM complexes onto chromatin. {ECO:0000250|UniProtKB:Q99741}. +Q8VHF2 CDHR5_MOUSE Cadherin-related family member 5 (Mu-protocadherin) 831 88,208 Alternative sequence (1); Chain (1); Domain (4); Glycosylation (11); Modified residue (10); Region (2); Repeat (3); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 642 662 Helical. {ECO:0000255}. TOPO_DOM 29 641 Extracellular. {ECO:0000255}.; TOPO_DOM 663 831 Cytoplasmic. {ECO:0000255}. FUNCTION: Intermicrovillar adhesion molecule that forms, via its extracellular domain, calcium-dependent heterophilic complexes with CDHR2 on adjacent microvilli. Thereby, controls the packing of microvilli at the apical membrane of epithelial cells. Through its cytoplasmic domain, interacts with microvillus cytoplasmic proteins to form the intermicrovillar adhesion complex/IMAC. This complex plays a central role in microvilli and epithelial brush border differentiation. {ECO:0000250|UniProtKB:Q9HBB8}. PTM: N- and O-glycosylated. {ECO:0000250|UniProtKB:Q9JIK1}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:Q9HBB8}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9HBB8}. Cell projection, microvillus membrane {ECO:0000250|UniProtKB:Q9HBB8}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9HBB8}. SUBUNIT: Part of the IMAC/intermicrovillar adhesion complex/intermicrovillar tip-link complex composed of ANKS4B, MYO7B, USH1C, CDHR2 and CDHR5. Interacts (via cytoplasmic domain) with USH1C and MYO7B; required for proper localization of CDHR5 to microvilli tips and its function in brush border differentiation. {ECO:0000250|UniProtKB:Q9HBB8}. +Q3V3A1 CDK15_MOUSE Cyclin-dependent kinase 15 (EC 2.7.11.22) (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 7 protein homolog) (Cell division protein kinase 15) (Serine/threonine-protein kinase ALS2CR7) (Serine/threonine-protein kinase PFTAIRE-2) 433 48,457 Active site (1); Alternative sequence (3); Binding site (1); Chain (1); Domain (1); Nucleotide binding (1) FUNCTION: Serine/threonine-protein kinase that acts like an antiapoptotic protein that counters TRAIL/TNFSF10-induced apoptosis by inducing phosphorylation of BIRC5 at 'Thr-34'. {ECO:0000250|UniProtKB:Q96Q40}. +Q61081 CDC37_MOUSE Hsp90 co-chaperone Cdc37 (Hsp90 chaperone protein kinase-targeting subunit) (p50Cdc37) [Cleaved into: Hsp90 co-chaperone Cdc37, N-terminally processed] 379 44,593 Chain (2); Initiator methionine (1); Modified residue (7) FUNCTION: Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity. Inhibits HSP90AA1 ATPase activity (By similarity). {ECO:0000250|UniProtKB:Q16543, ECO:0000269|PubMed:8666233}. PTM: Constitutively sumoylated by UBE2I. {ECO:0000250|UniProtKB:Q16543}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q16543}. SUBUNIT: Probably forms a complex composed of chaperones HSP90 and HSP70, co-chaperones STIP1/HOP, CDC37, PPP5C, PTGES3/p23, TSC1 and client protein TSC2 (By similarity). Probably forms a complex composed of chaperones HSP90 and HSP70, co-chaperones CDC37, PPP5C, TSC1 and client protein TSC2, CDK4, AKT, RAF1 and NR3C1; this complex does not contain co-chaperones STIP1/HOP and PTGES3/p23 (By similarity). Forms a complex with Hsp90/HSP90AB1 and CDK6 (By similarity). Interacts with HSP90AA1 (By similarity). Interacts with AR, CDK4, CDK6 and EIF2AK1 (By similarity). Interacts with RB1 (By similarity). Interacts with KSR1 (PubMed:10409742). Interacts with FLCN, FNIP1 and FNIP2 (By similarity). {ECO:0000250|UniProtKB:Q16543, ECO:0000250|UniProtKB:Q63692, ECO:0000269|PubMed:10409742}. +Q14B71 CDCA2_MOUSE Cell division cycle-associated protein 2 982 106,366 Alternative sequence (2); Chain (1); Compositional bias (1); Cross-link (1); Domain (1); Erroneous initiation (3); Modified residue (17); Sequence conflict (1) FUNCTION: Regulator of chromosome structure during mitosis required for condensin-depleted chromosomes to retain their compact architecture through anaphase. Acts by mediating the recruitment of phopsphatase PP1-gamma subunit (PPP1CC) to chromatin at anaphase and into the following interphase. At anaphase onset, its association with chromatin targets a pool of PPP1CC to dephosphorylate substrates (By similarity). {ECO:0000250}. PTM: Phosphorylated by CDK1. May regulate its subcellular location (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Excluded from the nucleolus. Present in nucleoplasm throughout the G1, S and G2 stages of the cell cycle. During M phase, it becomes diffuse throughout the cell as the nuclear membrane breaks down, and faintly accumulates later on metaphase chromatin. As the cell progresses to anaphase, it accumulates on chromatin (By similarity). {ECO:0000250}. SUBUNIT: Interacts with PPP1CC. {ECO:0000250}. +Q9CWM2 CDCA4_MOUSE Cell division cycle-associated protein 4 (Hematopoietic progenitor protein) 237 26,107 Chain (1); Domain (1); Erroneous initiation (1); Sequence conflict (2) FUNCTION: May participate in the regulation of cell proliferation through the E2F/RB pathway (By similarity). May be involved in molecular regulation of hematopoietic stem cells and progenitor cell lineage commitment and differentiation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. TISSUE SPECIFICITY: Expressed preferentially in hematopoietic progenitors and mature blood cells. Expressed at low levels in the heart, lung, spleen, and thymus and at a higher level in muscle. +P11440 CDK1_MOUSE Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase) 297 34,107 Active site (1); Binding site (1); Chain (1); Cross-link (4); Domain (1); Modified residue (16); Nucleotide binding (1); Sequence conflict (10) FUNCTION: Plays a key role in the control of the eukaryotic cell cycle by modulating the centrosome cycle as well as mitotic onset; promotes G2-M transition, and regulates G1 progress and G1-S transition via association with multiple interphase cyclins. Required in higher cells for entry into S-phase and mitosis. Phosphorylates PARVA/actopaxin, APC, AMPH, APC, BARD1, Bcl-xL/BCL2L1, BRCA2, CALD1, CASP8, CDC7, CDC20, CDC25A, CDC25C, CC2D1A, CENPA, CSNK2 proteins/CKII, FZR1/CDH1, CDK7, CEBPB, CHAMP1, DMD/dystrophin, EEF1 proteins/EF-1, EZH2, KIF11/EG5, EGFR, FANCG, FOS, GFAP, GOLGA2/GM130, GRASP1, UBE2A/hHR6A, HIST1H1 proteins/histone H1, HMGA1, HIVEP3/KRC, LMNA, LMNB, LMNC, LBR, LATS1, MAP1B, MAP4, MARCKS, MCM2, MCM4, MKLP1, MYB, NEFH, NFIC, NPC/nuclear pore complex, PITPNM1/NIR2, NPM1, NCL, NUCKS1, NPM1/numatrin, ORC1, PRKAR2A, EEF1E1/p18, EIF3F/p47, p53/TP53, NONO/p54NRB, PAPOLA, PLEC/plectin, RB1, UL40/R2, RAB4A, RAP1GAP, RCC1, RPS6KB1/S6K1, KHDRBS1/SAM68, ESPL1, SKI, BIRC5/survivin, STIP1, TEX14, beta-tubulins, MAPT/TAU, NEDD1, VIM/vimentin, TK1, FOXO1, RUNX1/AML1, SAMHD1, SIRT2 and RUNX2. CDK1/CDC2-cyclin-B controls pronuclear union in interphase fertilized eggs. Essential for early stages of embryonic development. During G2 and early mitosis, CDC25A/B/C-mediated dephosphorylation activates CDK1/cyclin complexes which phosphorylate several substrates that trigger at least centrosome separation, Golgi dynamics, nuclear envelope breakdown and chromosome condensation. Once chromosomes are condensed and aligned at the metaphase plate, CDK1 activity is switched off by WEE1- and PKMYT1-mediated phosphorylation to allow sister chromatid separation, chromosome decondensation, reformation of the nuclear envelope and cytokinesis. Inactivated by PKR/EIF2AK2- and WEE1-mediated phosphorylation upon DNA damage to stop cell cycle and genome replication at the G2 checkpoint thus facilitating DNA repair. Reactivated after successful DNA repair through WIP1-dependent signaling leading to CDC25A/B/C-mediated dephosphorylation and restoring cell cycle progression. In proliferating cells, CDK1-mediated FOXO1 phosphorylation at the G2-M phase represses FOXO1 interaction with 14-3-3 proteins and thereby promotes FOXO1 nuclear accumulation and transcription factor activity, leading to cell death of postmitotic neurons. The phosphorylation of beta-tubulins regulates microtubule dynamics during mitosis. NEDD1 phosphorylation promotes PLK1-mediated NEDD1 phosphorylation and subsequent targeting of the gamma-tubulin ring complex (gTuRC) to the centrosome, an important step for spindle formation. In addition, CC2D1A phosphorylation regulates CC2D1A spindle pole localization and association with SCC1/RAD21 and centriole cohesion during mitosis. The phosphorylation of Bcl-xL/BCL2L1 after prolongated G2 arrest upon DNA damage triggers apoptosis. In contrast, CASP8 phosphorylation during mitosis prevents its activation by proteolysis and subsequent apoptosis. This phosphorylation occurs in cancer cell lines, as well as in primary breast tissues and lymphocytes. EZH2 phosphorylation promotes H3K27me3 maintenance and epigenetic gene silencing. CALD1 phosphorylation promotes Schwann cell migration during peripheral nerve regeneration. CDK1-cyclin-B complex phosphorylates NCKAP5L and mediates its dissociation from centrosomes during mitosis. {ECO:0000250|UniProtKB:P06493, ECO:0000269|PubMed:16007079, ECO:0000269|PubMed:17700700, ECO:0000269|PubMed:17942597, ECO:0000269|PubMed:22405274}. PTM: Phosphorylation at Thr-161 by CAK/CDK7 activates kinase activity. Phosphorylation at Thr-14 and Tyr-15 by PKMYT1 prevents nuclear translocation. Phosphorylation at Tyr-15 by WEE1 and WEE2 inhibits the protein kinase activity and acts as a negative regulator of entry into mitosis (G2 to M transition). Phosphorylation by PKMYT1 and WEE1 takes place during mitosis to keep CDK1-cyclin-B complexes inactive until the end of G2. By the end of G2, PKMYT1 and WEE1 are inactivated, but CDC25A and CDC25B are activated. Dephosphorylation by active CDC25A and CDC25B at Thr-14 and Tyr-15, leads to CDK1 activation at the G2-M transition. Phosphorylation at Tyr-15 by WEE2 during oogenesis is required to maintain meiotic arrest in oocytes during the germinal vesicle (GV) stage, a long period of quiescence at dictyate prophase I, leading to prevent meiotic reentry. Phosphorylation by WEE2 is also required for metaphase II exit during egg activation to ensure exit from meiosis in oocytes and promote pronuclear formation. Phosphorylated at Tyr-4 by PKR/EIF2AK2 upon genotoxic stress. This phosphorylation triggers CDK1 polyubiquitination and subsequent proteolysis, thus leading to G2 arrest (By similarity). In response to UV irradiation, phosphorylation at Tyr-15 by PRKCD activates the G2/M DNA damage checkpoint. {ECO:0000250, ECO:0000269|PubMed:16169490, ECO:0000269|PubMed:19917613, ECO:0000269|PubMed:21454751}.; PTM: Polyubiquitinated upon genotoxic stress. {ECO:0000250|UniProtKB:P06493}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17942597}. Cytoplasm {ECO:0000269|PubMed:17942597}. Mitochondrion {ECO:0000269|PubMed:17942597}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Colocalizes with SIRT2 on centrosome during prophase and on splindle fibers during metaphase of the mitotic cell cycle (By similarity). Cytoplasmic during the interphase. Reversibly translocated from cytoplasm to nucleus when phosphorylated before G2-M transition when associated with cyclin-B1. Accumulates in mitochondria in G2-arrested cells upon DNA-damage. {ECO:0000250}. SUBUNIT: Forms a stable but non-covalent complex with a regulatory subunit and with a cyclin. Interacts with cyclins-B (CCNB1, CCNB2 and CCNB3) to form a serine/threonine kinase holoenzyme complex also known as maturation promoting factor (MPF). The cyclin subunit imparts substrate specificity to the complex. Can also form CDK1-cylin-D and CDK1-cyclin-E complexes that phosphorylate RB1 in vitro. Binds to RB1 and other transcription factors such as FOXO1 and RUNX2. Promotes G2-M transition when in complex with a cyclin-B. Interacts with DLGAP5. Binds to the CDK inhibitors CDKN1A/p21 and CDKN1B/p27. Isoform 2 is unable to complex with cyclin-B1 and also fails to bind to CDKN1A/p21. Interacts with catalytically active CCNB1 and RALBP1 during mitosis to form an endocytotic complex during interphase. Associates with cyclins-A and B1 during S-phase in regenerating hepatocytes. Interacts with FANCC. Interacts with CEP63; this interaction recruits CDK1 to centrosomes. Interacts with CENPA (By similarity). {ECO:0000250|UniProtKB:P06493, ECO:0000269|PubMed:16007079, ECO:0000269|PubMed:17942597}. +Q60772 CDN2C_MOUSE Cyclin-dependent kinase 4 inhibitor C (Cyclin-dependent kinase 6 inhibitor) (p18-INK4c) (p18-INK6) 168 18,066 Chain (1); Repeat (5) FUNCTION: Interacts strongly with CDK6, weakly with CDK4. Inhibits cell growth and proliferation with a correlated dependence on endogenous retinoblastoma protein RB. SUBUNIT: Heterodimer of p18 with CDK6. {ECO:0000250}. +Q99L43 CDS2_MOUSE Phosphatidate cytidylyltransferase 2 (EC 2.7.7.41) (CDP-DAG synthase 2) (CDP-DG synthase 2) (CDP-diacylglycerol synthase 2) (CDS 2) (CDP-diglyceride pyrophosphorylase 2) (CDP-diglyceride synthase 2) (CTP:phosphatidate cytidylyltransferase 2) 444 51,314 Chain (1); Modified residue (6); Sequence conflict (1); Transmembrane (6) TRANSMEM 78 98 Helical. {ECO:0000255}.; TRANSMEM 129 149 Helical. {ECO:0000255}.; TRANSMEM 165 185 Helical. {ECO:0000255}.; TRANSMEM 212 232 Helical. {ECO:0000255}.; TRANSMEM 261 281 Helical. {ECO:0000255}.; TRANSMEM 339 359 Helical. {ECO:0000255}. Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3. FUNCTION: Provides CDP-diacylglycerol, an important precursor for the synthesis of phosphatidylinositol, phosphatidylglycerol, and cardiolipin. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}; Matrix side {ECO:0000305}. +Q9DAQ4 CB081_MOUSE Uncharacterized protein C2orf81 homolog 598 65,778 Alternative sequence (2); Chain (1); Modified residue (2); Sequence conflict (1) +Q08EC4 CASS4_MOUSE Cas scaffolding protein family member 4 804 88,621 Alternative sequence (4); Chain (1); Compositional bias (1); Domain (1); Modified residue (2) FUNCTION: Docking protein that plays a role in tyrosine kinase-based signaling related to cell adhesion and cell spreading. Regulates PTK2/FAK1 activity, focal adhesion integrity, and cell spreading (By similarity). {ECO:0000250}. PTM: Phosphorylated on tyrosines by SRC. {ECO:0000250|UniProtKB:Q9NQ75}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9NQ75}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q9NQ75}. SUBUNIT: Interacts (via SH3 domain) with PTK2/FAK1 (via C-terminus). {ECO:0000250}. +Q9DAS2 CB070_MOUSE UPF0573 protein C2orf70 homolog 200 23,070 Alternative sequence (2); Chain (1) +Q9CWL2 CASZ1_MOUSE Zinc finger protein castor homolog 1 (Castor-related protein) 1761 191,188 Alternative sequence (2); Chain (1); Compositional bias (4); Cross-link (2); Frameshift (1); Modified residue (3); Sequence conflict (4); Zinc finger (8) FUNCTION: Transcription factor involved in vascular assembly and morphogenesis through direct transcriptional regulation of EGFL7. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: Expressed in the brain stem and the thalamencephalon. {ECO:0000269|PubMed:12351199, ECO:0000269|PubMed:16631614}. +P22682 CBL_MOUSE E3 ubiquitin-protein ligase CBL (EC 2.3.2.27) (Casitas B-lineage lymphoma proto-oncogene) (Proto-oncogene c-Cbl) (RING-type E3 ubiquitin transferase CBL) (Signal transduction protein CBL) 913 100,564 Binding site (1); Calcium binding (1); Chain (1); Compositional bias (3); Domain (2); Helix (3); Modified residue (14); Mutagenesis (1); Natural variant (1); Region (6); Sequence conflict (4); Turn (1); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: Adapter protein that functions as a negative regulator of many signaling pathways that are triggered by activation of cell surface receptors. Acts as an E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome. Recognizes activated receptor tyrosine kinases, including KIT, FLT1, FGFR1, FGFR2, PDGFRA, PDGFRB, EGFR, CSF1R, EPHA8 and KDR and terminates signaling. Recognizes membrane-bound HCK, SRC and other kinases of the SRC family and mediates their ubiquitination and degradation. Participates in signal transduction in hematopoietic cells. Plays an important role in the regulation of osteoblast differentiation and apoptosis. Essential for osteoclastic bone resorption. The 'Tyr-737' phosphorylated form induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function. May be functionally coupled with the E2 ubiquitin-protein ligase UB2D3 (PubMed:10393178, PubMed:12649282, PubMed:19265199, PubMed:20100865, PubMed:9653117). In association with CBLB, required for proper feedback inhibition of ciliary platelet-derived growth factor receptor-alpha (PDGFRA) signaling pathway via ubiquitination and internalization of PDGFRA (PubMed:29237719). {ECO:0000269|PubMed:10393178, ECO:0000269|PubMed:12649282, ECO:0000269|PubMed:19265199, ECO:0000269|PubMed:20100865, ECO:0000269|PubMed:29237719, ECO:0000269|PubMed:9653117}. PTM: Phosphorylated on tyrosine residues by ALK, EGFR, FGR, INSR, SYK, FYN and ZAP70. Phosphorylated on several tyrosine residues by constitutively activated FGFR3. Phosphorylated on tyrosine residues by activated PDGFRA and PDGFRB (By similarity). Phosphorylated on tyrosine residues in response to CSF1R, FLT1 and KIT signaling. Phosphorylated on tyrosine residues by HCK. {ECO:0000250, ECO:0000269|PubMed:10092522, ECO:0000269|PubMed:15001553, ECO:0000269|PubMed:17353186, ECO:0000269|PubMed:18034775, ECO:0000269|PubMed:19265199, ECO:0000269|PubMed:7782294, ECO:0000269|PubMed:8551236, ECO:0000269|PubMed:8798454}.; PTM: Ubiquitinated, leading to its degradation via the proteasome. Ubiquitination is negatively regulated by IFT20. {ECO:0000250|UniProtKB:P22681}. SUBCELLULAR LOCATION: Cytoplasm. Cell membrane {ECO:0000250}. Cell projection, cilium {ECO:0000269|PubMed:29237719}. Golgi apparatus {ECO:0000269|PubMed:29237719}. Note=Colocalizes with FGFR2 in lipid rafts at the cell membrane. {ECO:0000250}. SUBUNIT: Forms homodimers; IFT20 promotes the formation of stable homodimers (By similarity). Interacts (phosphorylated) with PIK3R1. Interacts with phosphorylated LAT2 (By similarity). Associates with NCK via its SH3 domain. The phosphorylated C-terminus interacts with CD2AP via its second SH3 domain. Binds to UBE2L3. Interacts with adapters SLA, SLA2 and with the phosphorylated C-terminus of SH2B2. Interacts with EGFR, SYK and ZAP70 via the highly conserved Cbl-N region. Interacts with FGR. Also interacts with BLK, SORBS1 and INPPL1/SHIP2. Interacts with CBLB. Interacts with TEK/TIE2 (tyrosine phosphorylated) (By similarity). Interacts with ALK, AXL and FGFR2. Interacts with CSF1R, EPHB1, FLT1, KDR, PDGFRA and PDGFRB; regulates receptor degradation through ubiquitination. Interacts with HCK and LYN. Interacts with ATX2. Interacts with SH3KBP1 and this interaction is inhibited in the presence of SHKBP1 (PubMed:21830225). Interacts with SIGLEC10 (PubMed:23374343). Interacts with IFT20 (By similarity). {ECO:0000250|UniProtKB:P22681, ECO:0000269|PubMed:10092522, ECO:0000269|PubMed:12024036, ECO:0000269|PubMed:12649282, ECO:0000269|PubMed:12842890, ECO:0000269|PubMed:15001553, ECO:0000269|PubMed:17353186, ECO:0000269|PubMed:17620338, ECO:0000269|PubMed:18034775, ECO:0000269|PubMed:18602463, ECO:0000269|PubMed:21830225, ECO:0000269|PubMed:23374343, ECO:0000269|PubMed:7782294, ECO:0000269|PubMed:9447983, ECO:0000269|PubMed:9722576}. DOMAIN: The RING-type zinc finger domain mediates binding to an E2 ubiquitin-conjugating enzyme. {ECO:0000250}.; DOMAIN: The N-terminus is composed of the phosphotyrosine binding (PTB) domain, a short linker region and the RING-type zinc finger. The PTB domain, which is also called TKB (tyrosine kinase binding) domain, is composed of three different subdomains: a four-helix bundle (4H), a calcium-binding EF hand and a divergent SH2 domain. DISEASE: Note=Can be converted to an oncogenic protein by deletions or mutations that disturb its ability to down-regulate RTKs. +Q7TPZ8 CBPA1_MOUSE Carboxypeptidase A1 (EC 3.4.17.1) 419 47,385 Active site (1); Binding site (2); Chain (1); Disulfide bond (1); Metal binding (3); Propeptide (1); Region (3); Signal peptide (1) FUNCTION: Carboxypeptidase that catalyzes the release of a C-terminal amino acid, but has little or no action with -Asp, -Glu, -Arg, -Lys or -Pro. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. +Q09M02 CBPC5_MOUSE Cytosolic carboxypeptidase-like protein 5 (EC 3.4.17.-) (ATP/GTP-binding protein-like 5) 886 97,607 Active site (1); Alternative sequence (8); Chain (1); Erroneous initiation (1); Metal binding (3); Modified residue (1); Mutagenesis (2); Sequence conflict (2) FUNCTION: Metallocarboxypeptidase that mediates protein deglutamylation. Specifically catalyzes the deglutamylation of the branching point glutamate side chains generated by post-translational glutamylation in proteins such as tubulins (PubMed:20519502, PubMed:21074048). In contrast, it is not able to act as a long-chain deglutamylase that shortens long polyglutamate chains, a process catalyzed by AGTPBP1/CCP1, AGBL2/CCP2, AGBL3/CCP3, AGBL1/CCP4 and AGBL4/CCP6 (PubMed:25103237). Mediates deglutamylation of CGAS, regulating the antiviral activity of CGAS (PubMed:26829768). {ECO:0000269|PubMed:20519502, ECO:0000269|PubMed:21074048, ECO:0000269|PubMed:25103237, ECO:0000269|PubMed:26829768}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:17244818}. Nucleus {ECO:0000269|PubMed:17244818}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q8NDL9}. Midbody {ECO:0000250|UniProtKB:Q8NDL9}. Note=Colocalizes with alpha-tubulin in the mitotic spindle and with midbody microtubules in the intercellular bridges formed during cytokinesis (By similarity). Mainly cytoplasmic. Slight accumulation in the nucleus is observed (PubMed:17244818). {ECO:0000250|UniProtKB:Q8NDL9, ECO:0000269|PubMed:17244818}. TISSUE SPECIFICITY: Widely expressed. Highly expressed in testis, and moderately in pituitary, brain, eye and kidney. {ECO:0000269|PubMed:17244818, ECO:0000269|PubMed:25103237}. +Q8C7V8 CC134_MOUSE Coiled-coil domain-containing protein 134 229 26,495 Alternative sequence (1); Chain (1); Coiled coil (1); Motif (1); Sequence conflict (1); Signal peptide (1) FUNCTION: In extracellular secreted form, promotes proliferation and activation of CD8(+) T cells, suggesting a cytokine-like function. Enhances cytotoxic anti-tumor activity of CD8(+) T cells. May inhibit ERK and JNK signaling activity. May suppress cell migration and invasion activity, via its effects on ERK and JNK signaling. {ECO:0000250|UniProtKB:Q9H6E4}.; FUNCTION: In the nucleus, enhances stability of the PCAF histone acetyltransferase (HAT) complex member TADA2A and thus promotes PCAF-mediated H3K14 and H4K8 HAT activity. May inhibit TADA2A-mediated TP53/p53 'Lys-321' acetylation, leading to reduced TP53 stability and transcriptional activity. May also promote TADA2A-mediated XRCC6 acetylation thus facilitating cell apoptosis in response to DNA damage. {ECO:0000250|UniProtKB:Q9H6E4}. PTM: O-glycosylated, with additional sialic acid modifications. {ECO:0000250|UniProtKB:Q9H6E4}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H6E4}. Cytoplasm {ECO:0000250|UniProtKB:Q9H6E4}. Secreted {ECO:0000250|UniProtKB:Q9H6E4}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9H6E4}. Note=Accumulates in the nucleus in response to UV irradiation. {ECO:0000250|UniProtKB:Q9H6E4}. SUBUNIT: Interacts with TADA2A. Associates with the PCAF complex via TADA2A binding. {ECO:0000250|UniProtKB:Q9H6E4}. +Q3V125 CC110_MOUSE Coiled-coil domain-containing protein 110 848 96,356 Chain (1); Coiled coil (1); Modified residue (1); Sequence conflict (1) SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +A0AUP1 CC112_MOUSE Coiled-coil domain-containing protein 112 442 52,777 Chain (1); Coiled coil (3); Erroneous initiation (2) +Q3TVA9 CC136_MOUSE Coiled-coil domain-containing protein 136 1136 131,930 Alternative sequence (3); Chain (1); Coiled coil (4); Compositional bias (2); Erroneous initiation (2); Erroneous termination (1); Modified residue (1); Sequence conflict (1); Transmembrane (1) TRANSMEM 1112 1132 Helical. {ECO:0000255}. FUNCTION: May play a role in acrosome formation in spermatogenesis and in fertilization. {ECO:0000269|PubMed:27076447}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome membrane {ECO:0000269|PubMed:27076447}; Single-pass membrane protein {ECO:0000305}. Note=Exclusively localized on a peripheral part of acrosome membrane (Golgi phase), localized on the equatorial segment of the acrosome (maturation phase). {ECO:0000269|PubMed:27076447}. TISSUE SPECIFICITY: Present at high level in testis (at protein level). {ECO:0000269|PubMed:27076447}. +Q80ZU5 CC181_MOUSE Coiled-coil domain-containing protein 181 509 59,241 Chain (1); Coiled coil (2); Sequence conflict (4) FUNCTION: Microtubule-binding protein that localizes to the microtubular manchette of elongating spermatids. {ECO:0000305|PubMed:28283191}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:28283191}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:28283191}. Note=Localizes to the microtubular manchette of elongating spermatids (PubMed:28283191). Localizes to the sperm flagella and to the basal half of motile cilia (PubMed:28283191). {ECO:0000269|PubMed:28283191}. SUBUNIT: Homodimer (PubMed:28283191). Interacts with HOOK1 (PubMed:28283191). Interacts with HOOK2 (PubMed:28283191). Interacts with HOOK3 (PubMed:28283191). {ECO:0000269|PubMed:28283191}. TISSUE SPECIFICITY: Predominantly expressed in testis (PubMed:28283191). Expressed at lower level in brain, eye, trachea and lung (PubMed:28283191). Barely expressed in tongue, heart, liver, kidney, spleen and muscle (PubMed:28283191). Present at high level in elongating spermatids, whereas lower levels are observed in round spermatids (at protein level) (PubMed:28283191). {ECO:0000269|PubMed:28283191}. +Q9D9C6 CC182_MOUSE Coiled-coil domain-containing protein 182 152 17,461 Chain (1); Coiled coil (1) +Q8CE13 CCD17_MOUSE Coiled-coil domain-containing protein 17 565 62,536 Chain (1); Coiled coil (2); Compositional bias (2); Erroneous gene model prediction (1) +Q8R3Q6 CCD58_MOUSE Coiled-coil domain-containing protein 58 144 16,665 Chain (1); Coiled coil (1); Initiator methionine (1); Modified residue (2); Sequence conflict (1) +Q9JJV5 CCG3_MOUSE Voltage-dependent calcium channel gamma-3 subunit (Neuronal voltage-gated calcium channel gamma-3 subunit) (Transmembrane AMPAR regulatory protein gamma-3) (TARP gamma-3) 315 35,516 Chain (1); Modified residue (1); Mutagenesis (1); Sequence conflict (1); Transmembrane (4) TRANSMEM 8 28 Helical. {ECO:0000255}.; TRANSMEM 104 124 Helical. {ECO:0000255}.; TRANSMEM 135 155 Helical. {ECO:0000255}.; TRANSMEM 181 201 Helical. {ECO:0000255}. FUNCTION: Regulates the trafficking to the somatodendritic compartment and gating properties of AMPA-selective glutamate receptors (AMPARs) (PubMed:18341993). Promotes their targeting to the cell membrane and synapses and modulates their gating properties by slowing their rates of activation, deactivation and desensitization. Does not show subunit-specific AMPA receptor regulation and regulates all AMPAR subunits. Thought to stabilize the calcium channel in an inactivated (closed) state (By similarity). {ECO:0000250|UniProtKB:Q8VHX0, ECO:0000269|PubMed:18341993}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Note=Displays a somatodendritic localization and is excluded from axons in neurons. {ECO:0000269|PubMed:18341993}. SUBUNIT: The L-type calcium channel is composed of five subunits: alpha-1, alpha-2/delta, beta and gamma. Acts as an auxiliary subunit for AMPA-selective glutamate receptors (AMPARs). Found in a complex with GRIA1, GRIA2, GRIA3, GRIA4, CNIH2, CNIH3, CACNG2, CACNG4, CACNG5, CACNG7 and CACNG8 (By similarity). Interacts with AP4M1 and GRIA1; associates GRIA1 with the adaptor protein complex 4 (AP-4) to target GRIA1 to the somatodendritic compartment of neurons (PubMed:18341993). {ECO:0000250|UniProtKB:Q8VHX0, ECO:0000269|PubMed:18341993}. +E9PVD1 CCD62_MOUSE Coiled-coil domain-containing protein 62 701 79,317 Chain (1); Coiled coil (2); Motif (2) FUNCTION: Nuclear receptor coactivator that can enhance preferentially estrogen receptors ESR1 and ESR2 transactivation. Modulates also progesterone/PGR, glucocorticoid/NR3C1 and androgen/AR receptors transactivation, although at lower level; little effect on vitamin D receptor/VDR (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus. Note=Mainly nuclear. {ECO:0000250}. SUBUNIT: Interacts with ESR1 and ESR2 in the presence of estradiol/E2. The interaction with ESR2 recruits CCDC62 to ER target genes, including cyclin-D1/CCND1 AP-1 promoter (By similarity). {ECO:0000250}. DOMAIN: Contains 2 Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs. The first one is essential for the association with ESR1 and ESR2 (By similarity). {ECO:0000250}. +Q9CQL2 CCER1_MOUSE Coiled-coil domain-containing glutamate-rich protein 1 403 46,213 Chain (1); Coiled coil (1); Compositional bias (1) +Q9CR29 CCD43_MOUSE Coiled-coil domain-containing protein 43 222 25,049 Alternative sequence (2); Chain (1); Coiled coil (2); Compositional bias (1); Cross-link (1); Modified residue (1) +Q810U5 CCD50_MOUSE Coiled-coil domain-containing protein 50 (Protein Ymer) 305 35,321 Alternative sequence (2); Chain (1); Coiled coil (1); Compositional bias (2); Frameshift (1); Initiator methionine (1); Modified residue (2); Sequence conflict (4) FUNCTION: Involved in EGFR signaling. {ECO:0000250}. PTM: Phosphorylated on tyrosine residues. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17503326}. Note=Associated with microtubules of the cytoskeleton and mitotic apparatus. SUBUNIT: Interacts with RNF126. {ECO:0000269|PubMed:23418353}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:17503326}. +P10148 CCL2_MOUSE C-C motif chemokine 2 (Monocyte chemoattractant protein 1) (Monocyte chemotactic protein 1) (MCP-1) (Platelet-derived growth factor-inducible protein JE) (Small-inducible cytokine A2) 148 16,326 Chain (1); Disulfide bond (2); Glycosylation (1); Modified residue (1); Natural variant (2); Signal peptide (1) FUNCTION: Chemotactic factor that attracts monocytes, but not neutrophils. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Monomer or homodimer; in equilibrium. {ECO:0000250}. +Q9JL21 CCR10_MOUSE C-C chemokine receptor type 10 (C-C CKR-10) (CC-CKR-10) (CCR-10) (Chemokine C-C receptor 9) (G-protein coupled receptor 2) 362 38,900 Chain (1); Disulfide bond (1); Sequence conflict (2); Topological domain (8); Transmembrane (7) TRANSMEM 49 69 Helical; Name=1. {ECO:0000255}.; TRANSMEM 81 101 Helical; Name=2. {ECO:0000255}.; TRANSMEM 116 136 Helical; Name=3. {ECO:0000255}.; TRANSMEM 160 180 Helical; Name=4. {ECO:0000255}.; TRANSMEM 209 229 Helical; Name=5. {ECO:0000255}.; TRANSMEM 248 268 Helical; Name=6. {ECO:0000255}.; TRANSMEM 292 312 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 48 Extracellular. {ECO:0000255}.; TOPO_DOM 70 80 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 102 115 Extracellular. {ECO:0000255}.; TOPO_DOM 137 159 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 181 208 Extracellular. {ECO:0000255}.; TOPO_DOM 230 247 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 269 291 Extracellular. {ECO:0000255}.; TOPO_DOM 313 362 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for chemokines SCYA27 and SCYA28. Subsequently transduces a signal by increasing the intracellular calcium ions level. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed at high levels in small intestine, colon, lymph nodes, Peyer patches and at lower levels in thymus, lung and spleen. {ECO:0000269|PubMed:10781587}. +Q61457 CCNE1_MOUSE G1/S-specific cyclin-E1 408 46,986 Chain (1); Frameshift (1); Modified residue (5); Sequence conflict (5) FUNCTION: Essential for the control of the cell cycle at the G1/S (start) transition. PTM: Phosphorylation of both Thr-393 by GSK3 and Ser-397 by CDK2 creates a high affinity degron recognized by FBXW7, and accelerates degradation via the ubiquitin proteasome pathway. Phosphorylation at Thr-74 creates a low affinity degron also recognized by FBXW7 (By similarity). {ECO:0000250|UniProtKB:P24864}.; PTM: Ubiquitinated by UHRF2; appears to occur independently of phosphorylation. {ECO:0000250|UniProtKB:P24864}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P24864}. SUBUNIT: Interacts with CDK2 protein kinase to form a serine/threonine kinase holoenzyme complex. The cyclin subunit imparts substrate specificity to the complex. Part of a complex consisting of UHRF2, CDK2 and CCNE1. Interacts directly with UHRF2; the interaction ubiquitinates CCNE1 and appears to occur independently of CCNE1 phosphorylation (By similarity). Found in a complex with CDK2, CABLES1 and CCNA1 (PubMed:11585773). Interacts with INCA1 (By similarity). {ECO:0000250|UniProtKB:P24864, ECO:0000269|PubMed:11585773}. TISSUE SPECIFICITY: Found in adult spleen, and to a lesser extent in adult testis and brain. +P15379 CD44_MOUSE CD44 antigen (Extracellular matrix receptor III) (ECMR-III) (GP90 lymphocyte homing/adhesion receptor) (HUTCH-I) (Hermes antigen) (Hyaluronate receptor) (Lymphocyte antigen 24) (Ly-24) (Phagocytic glycoprotein 1) (PGP-1) (Phagocytic glycoprotein I) (PGP-I) (CD antigen CD44) 778 85,617 Alternative sequence (15); Beta strand (9); Binding site (4); Chain (1); Compositional bias (1); Disulfide bond (3); Domain (1); Glycosylation (10); Helix (4); Modified residue (5); Mutagenesis (1); Natural variant (2); Region (2); Sequence conflict (10); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 686 706 Helical. {ECO:0000255}. TOPO_DOM 23 685 Extracellular. {ECO:0000255}.; TOPO_DOM 707 778 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for hyaluronic acid (HA). Mediates cell-cell and cell-matrix interactions through its affinity for HA, and possibly also through its affinity for other ligands such as osteopontin, collagens, and matrix metalloproteinases (MMPs). Adhesion with HA plays an important role in cell migration, tumor growth and progression. In cancer cells, may play an important role in invadopodia formation. Also involved in lymphocyte activation, recirculation and homing, and in hematopoiesis (By similarity). Receptor for LGALS9; the interaction enhances binding of SMAD3 to the FOXP3 promoter, leading to up-regulation of FOXP3 expression and increased induced regulatory T (iTreg) cell stability and suppressive function (PubMed:25065622). {ECO:0000250|UniProtKB:P16070, ECO:0000269|PubMed:25065622}. PTM: N-glycosylated. {ECO:0000250}.; PTM: O-glycosylated; contains chondroitin sulfate glycans which can be more or less sulfated. {ECO:0000250}.; PTM: Phosphorylated; activation of PKC results in the dephosphorylation of Ser-742 (constitutive phosphorylation site), and the phosphorylation of Ser-708. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17403031, ECO:0000269|PubMed:25065622}; Single-pass type I membrane protein {ECO:0000269|PubMed:17403031}. Cell projection, microvillus {ECO:0000269|PubMed:9472040}. Note=Colocalizes with actin in membrane protrusionFs at wounding edges. Co-localizes with RDX, EZR and MSN in microvilli. {ECO:0000269|PubMed:17403031, ECO:0000269|PubMed:9472040}. SUBUNIT: Interacts with HA, as well as other glycosaminoglycans, collagen, laminin, and fibronectin via its N-terminal segment (By similarity). Interacts with PKN2 (PubMed:17403031). Interacts with TIAM1 and TIAM2 (PubMed:19893486). Interacts with UNC119. Interacts with PDPN (via extracellular domain); this interaction is required for PDPN-mediated directional migration and regulation of lamellipodia extension/stabilization during cell spreading and migration (By similarity). Interacts with RDX, EZR and MSN (PubMed:9472040). {ECO:0000250|UniProtKB:P16070, ECO:0000269|PubMed:17403031, ECO:0000269|PubMed:19893486, ECO:0000269|PubMed:9472040}. DOMAIN: The lectin-like LINK domain is responsible for hyaluronan binding. +P41731 CD63_MOUSE CD63 antigen (CD antigen CD63) 238 25,767 Chain (1); Glycosylation (4); Motif (1); Mutagenesis (1); Topological domain (5); Transmembrane (4) TRANSMEM 12 32 Helical. {ECO:0000255}.; TRANSMEM 52 72 Helical. {ECO:0000255}.; TRANSMEM 82 102 Helical. {ECO:0000255}.; TRANSMEM 204 224 Helical. {ECO:0000255}. TOPO_DOM 1 11 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 33 51 Extracellular. {ECO:0000255}.; TOPO_DOM 73 81 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 103 203 Extracellular. {ECO:0000255}.; TOPO_DOM 225 238 Cytoplasmic. {ECO:0000255}. FUNCTION: Functions as cell surface receptor for TIMP1 and plays a role in the activation of cellular signaling cascades. Plays a role in the activation of ITGB1 and integrin signaling, leading to the activation of AKT, FAK/PTK2 and MAP kinases. Promotes cell survival, reorganization of the actin cytoskeleton, cell adhesion, spreading and migration, via its role in the activation of AKT and FAK/PTK2. Plays a role in VEGFA signaling via its role in regulating the internalization of KDR/VEGFR2. Plays a role in intracellular vesicular transport processes, and is required for normal trafficking of the PMEL luminal domain that is essential for the development and maturation of melanocytes. Plays a role in the adhesion of leukocytes onto endothelial cells via its role in the regulation of SELP trafficking. May play a role in mast cell degranulation in response to Ms4a2/FceRI stimulation, but not in mast cell degranulation in response to other stimuli. {ECO:0000269|PubMed:19075008, ECO:0000269|PubMed:21803846, ECO:0000269|PubMed:21962903, ECO:0000269|PubMed:23632027, ECO:0000269|PubMed:23945142}. PTM: Palmitoylated at a low, basal level in unstimulated platelets. The level of palmitoylation increases when platelets are activated by thrombin (in vitro) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P08962}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:19075008, ECO:0000269|PubMed:21041449, ECO:0000269|PubMed:23945142}; Multi-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000269|PubMed:23945142}; Multi-pass membrane protein {ECO:0000255}. Endosome, multivesicular body {ECO:0000250|UniProtKB:P08962}. Melanosome {ECO:0000250|UniProtKB:P08962}. Secreted, exosome {ECO:0000269|PubMed:26109643}. Cell surface {ECO:0000250|UniProtKB:P08962}. Note=Also found in Weibel-Palade bodies of endothelial cells. Located in platelet dense granules. Detected in a subset of pre-melanosomes. Detected on intralumenal vesicles (ILVs) within multivesicular bodies. {ECO:0000250|UniProtKB:P08962}. SUBUNIT: Interacts with TIMP1 and ITGB1 and recruits TIMP1 to ITGB1. Interacts with CD9. Identified in a complex with CD9 and ITGB3. Interacts with PMEL. Interacts with KDR/VEGFR2; identified in a complex with ITGB1 and KDR/VEGFR2 and is required to recruit KDR to ITGB1 complexes (By similarity). Interacts with SYT7 (PubMed:21041449). {ECO:0000250, ECO:0000269|PubMed:21041449}. TISSUE SPECIFICITY: Ubiquitous. Strongly expressed in kidney. Detected in spleen, bone marrow, peripheral blood mononuclear cells and macrophages. +P37217 CD69_MOUSE Early activation antigen CD69 (CD antigen CD69) 199 22,517 Chain (1); Disulfide bond (4); Domain (1); Glycosylation (3); Topological domain (2); Transmembrane (1) TRANSMEM 41 61 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 40 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 62 199 Extracellular. {ECO:0000255}. FUNCTION: Involved in lymphocyte proliferation and functions as a signal transmitting receptor in lymphocytes, natural killer (NK) cells, and platelets. PTM: Constitutive Ser/Thr phosphorylation in both mature thymocytes and activated T-lymphocytes. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. SUBUNIT: Homodimer; disulfide-linked. TISSUE SPECIFICITY: Expressed on the surface of activated T-cells, B-cells, natural killer cells, neutrophils and platelets. +P06332 CD4_MOUSE T-cell surface glycoprotein CD4 (T-cell differentiation antigen L3T4) (T-cell surface antigen T4/Leu-3) (CD antigen CD4) 457 51,297 Alternative sequence (1); Chain (1); Disulfide bond (3); Domain (4); Glycosylation (4); Lipidation (2); Modified residue (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 395 417 Helical. {ECO:0000255}. TOPO_DOM 27 394 Extracellular. {ECO:0000255}.; TOPO_DOM 418 457 Cytoplasmic. {ECO:0000255}. FUNCTION: Integral membrane glycoprotein that plays an essential role in the immune response and serves multiple functions in responses against both external and internal offenses. In T-cells, functions primarily as a coreceptor for MHC class II molecule:peptide complex. The antigens presented by class II peptides are derived from extracellular proteins while class I peptides are derived from cytosolic proteins. Interacts simultaneously with the T-cell receptor (TCR) and the MHC class II presented by antigen presenting cells (APCs). In turn, recruits the Src kinase LCK to the vicinity of the TCR-CD3 complex. LCK then initiates different intracellular signaling pathways by phosphorylating various substrates ultimately leading to lymphokine production, motility, adhesion and activation of T-helper cells. In other cells such as macrophages or NK cells, plays a role in differentiation/activation, cytokine expression and cell migration in a TCR/LCK-independent pathway. Participates in the development of T-helper cells in the thymus and triggers the differentiation of monocytes into functional mature macrophages. {ECO:0000250|UniProtKB:P01730, ECO:0000269|PubMed:16709847, ECO:0000269|PubMed:1832488, ECO:0000269|PubMed:2784195, ECO:0000269|PubMed:3262426}. PTM: Palmitoylation and association with LCK contribute to the enrichment of CD4 in lipid rafts. {ECO:0000250|UniProtKB:P01730}.; PTM: Phosphorylated by PKC; phosphorylation plays an important role for CD4 internalization. {ECO:0000269|PubMed:2512251}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P01730}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P01730}. SUBUNIT: Forms disulfide-linked homo-dimers at the cell surface. Interacts with LCK. Interacts with PTK2/FAK1. Binds to P4HB/PDI. Interacts with IL16; this interaction induces a CD4-dependent signaling in lymphocytes. {ECO:0000250|UniProtKB:P01730}. TISSUE SPECIFICITY: Highly expressed in T-helper cells. The presence of CD4 is a hallmark of T-helper cells which are specialized in the activation and growth of cytotoxic T-cells, regulation of B cells, or activation of phagocytes. CD4 is also present in other immune cells such as macrophages, dendritic cells or NK cells. {ECO:0000269|PubMed:10706685}. +Q8VHP6 CDHR1_MOUSE Cadherin-related family member 1 (Photoreceptor cadherin) (prCAD) (Protocadherin-21) 859 94,028 Chain (1); Compositional bias (1); Domain (6); Glycosylation (3); Sequence caution (1); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 702 722 Helical. {ECO:0000255}. TOPO_DOM 22 701 Extracellular. {ECO:0000255}.; TOPO_DOM 723 859 Cytoplasmic. {ECO:0000255}. FUNCTION: Potential calcium-dependent cell-adhesion protein. May be required for the structural integrity of the outer segment (OS) of photoreceptor cells. PTM: Undergoes proteolytic cleavage; produces a soluble 95 kDa N-terminal fragment and a 25 kDa cell-associated C-terminal fragment. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Note=Localized at the junction between the inner and outer segments of rod and cone photoreceptors cells. Confined to the base of the OS. Localized on the edges of nascent evaginating disks on the side of the OS opposite the connecting cilium. Expressed at postnatal day 2 at the apical tip of the rod photoreceptor cells, the site of the developing OS. Colocalized with rhodopsin between postnatal days 2 and 9 at the base of the growing OS region. {ECO:0000269|PubMed:11738025, ECO:0000269|PubMed:15284225}. SUBUNIT: Interacts with PROM1. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in cone and rod photoreceptor cells (at protein level). Expressed in photoreceptor cells of the outer nuclear layer of the retina. Expressed in mitral and tufted cells in the olfactory bulb. {ECO:0000269|PubMed:11738025, ECO:0000269|PubMed:15284225, ECO:0000269|PubMed:16106355}. +P39689 CDN1A_MOUSE Cyclin-dependent kinase inhibitor 1 (CDK-interacting protein 1) (Melanoma differentiation-associated protein) (p21) 159 17,785 Chain (1); Cross-link (1); Initiator methionine (1); Modified residue (6); Motif (1); Region (2); Sequence conflict (2); Zinc finger (1) FUNCTION: May be involved in p53/TP53 mediated inhibition of cellular proliferation in response to DNA damage. Binds to and inhibits cyclin-dependent kinase activity, preventing phosphorylation of critical cyclin-dependent kinase substrates and blocking cell cycle progression. Functions in the nuclear localization and assembly of cyclin D-CDK4 complex and promotes its kinase activity towards RB1. At higher stoichiometric ratios, inhibits the kinase activity of the cyclin D-CDK4 complex (PubMed:25329316). Inhibits DNA synthesis by DNA polymerase delta by competing with POLD3 for PCNA binding (By similarity). {ECO:0000250|UniProtKB:P38936, ECO:0000269|PubMed:25329316}. PTM: Phosphorylation of Thr-140 or Ser-141 impairs binding to PCNA. Phosphorylation at Ser-112 by GSK3-beta enhances ubiquitination by the DCX(DTL) complex (By similarity). Phosphorylation of Thr-140 by PIM2 enhances its stability and inhibits cell proliferation. Phosphorylation of Thr-140 by PIM1 results in the relocation of CDKN1A to the cytoplasm and enhanced CDKN1A protein stability. UV radiation-induced phosphorylation at Ser-78 and Ser-141 by NUAK1 leads to its degradation. {ECO:0000250|UniProtKB:P38936, ECO:0000269|PubMed:25329316}.; PTM: Ubiquitinated by MKRN1; leading to polyubiquitination and 26S proteasome-dependent degradation. Ubiquitinated by the DCX(DTL) complex, also named CRL4(CDT2) complex, leading to its degradation during S phase or following UV irradiation. Ubiquitination by the DCX(DTL) complex is essential to control replication licensing and is PCNA-dependent: interacts with PCNA via its PIP-box, while the presence of the containing the 'K+4' motif in the PIP box, recruit the DCX(DTL) complex, leading to its degradation. Ubiquitination at Ser-2 leads to degradation by the proteasome pathway. Ubiquitinated by RNF114; leading to proteasomal degradation (By similarity). {ECO:0000250}.; PTM: Acetylation leads to protein stability. Acetylated in vitro on Lys-136, Lys-149, Lys-156 and Lys-158. Deacetylation by HDAC1 is prevented by competitive binding of C10orf90/FATS to HDAC1. {ECO:0000269|PubMed:20154723}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000269|PubMed:20154723}. SUBUNIT: Interacts with HDAC1; the interaction is prevented by competitive binding of C10orf90/FATS to HDAC1 facilitating acetylation and protein stabilization of CDKN1A/p21 (PubMed:20154723). Interacts with MKRN1. Interacts with PSMA3. Interacts with PCNA. Component of the ternary complex, cyclin D-CDK4-CDKN1A. Interacts (via its N-terminal domain) with CDK4; the interaction promotes the assembly of the cyclin D-CDK4 complex, its nuclear translocation and promotes the cyclin D-dependent enzyme activity of CDK4. Binding to CDK2 leads to CDK2/cyclin E inactivation at the G1-S phase DNA damage checkpoint, thereby arresting cells at the G1-S transition during DNA repair. Interacts with PIM1 (By similarity). Interacts with STK11 (PubMed:25329316). Interacts with NUAK1 (By similarity). {ECO:0000250|UniProtKB:P38936, ECO:0000269|PubMed:20154723, ECO:0000269|PubMed:25329316}. DOMAIN: The C-terminal is required for nuclear localization of the cyclin D-CDK4 complex. {ECO:0000250}.; DOMAIN: The PIP-box K+4 motif mediates both the interaction with PCNA and the recruitment of the DCX(DTL) complex: while the PIP-box interacts with PCNA, the presence of the K+4 submotif, recruits the DCX(DTL) complex, leading to its ubiquitination. {ECO:0000250}. +Q8R4E9 CDT1_MOUSE DNA replication factor Cdt1 (Double parked homolog) (DUP) (Retroviral insertion site 2 protein) 557 61,510 Beta strand (6); Chain (1); Frameshift (1); Helix (15); Modified residue (4); Motif (2); Region (2); Sequence conflict (3); Turn (2) FUNCTION: Required for both DNA replication and mitosis. DNA replication licensing factor, required for pre-replication complex assembly. Cooperates with CDC6 and the origin recognition complex (ORC) during G1 phase of the cell cycle to promote the loading of the mini-chromosome maintenance (MCM) complex onto DNA to generate pre-replication complexes (pre-RC). Required also for mitosis by promoting stable kinetochore-microtubule attachments (By similarity). Potential oncogene (PubMed:11850834). {ECO:0000250|UniProtKB:Q9H211, ECO:0000269|PubMed:11850834, ECO:0000269|PubMed:12192004, ECO:0000269|PubMed:14993212}. PTM: Two independent E3 ubiquitin ligase complexes, SCF(SKP2) and the DCX(DTL) complex, mediated CDT1 degradation in S phase. Ubiquitinated by the DCX(DTL) complex, in response to DNA damage, leading to its degradation. Ubiquitination by the DCX(DTL) complex is necessary to ensure proper cell cycle regulation and is PCNA-dependent: interacts with PCNA via its PIP-box, while the presence of the containing the 'K+4' motif in the PIP box, recruit the DCX(DTL) complex, leading to its degradation. Phosphorylation at Thr-28 by CDK2 targets CDT1 for ubiquitynation by SCF(SKP2) E3 ubiquitin ligase and subsequent degradation. The interaction with GMNN protects it against ubiquitination. Deubiquitinated by USP37. {ECO:0000250|UniProtKB:Q9H211}.; PTM: Phosphorylation by cyclin A-dependent kinases at Thr-28 targets CDT1 for ubiquitynation by SCF(SKP2) E3 ubiquitin ligase and subsequent degradation. Phosphorylated at Thr-28 by MAPK8/JNK1, which blocks replication licensing in response to stress. Binding to GMNN is not affected by phosphorylation (PubMed:14993212). {ECO:0000250|UniProtKB:Q9H211, ECO:0000269|PubMed:14993212}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14993212}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q9H211}. Note=Transiently localizes to kinetochores during prometaphase and metaphase. {ECO:0000250|UniProtKB:Q9H211}. SUBUNIT: Interacts with GMNN; inhibits binding of the MCM complex to origins of replication (PubMed:12192004). Interacts with CDC6; are mutually dependent on one another for loading MCM complexes onto chromatin (By similarity). Interacts with PCNA (By similarity). Interacts with LRWD1 during G1 phase and during mitosis (By similarity). Interacts with NDC80 subunit of the NDC80 complex; leading to kinetochore localization (By similarity). Interacts with KAT7 (By similarity). Interacts with ubiquitin-binding protein FAF1; the interaction is likely to promote CDT1 degradation (By similarity). {ECO:0000250|UniProtKB:Q9H211, ECO:0000269|PubMed:12192004}. DOMAIN: The PIP-box K+4 motif mediates both the interaction with PCNA and the recruitment of the DCX(DTL) complex: while the PIP-box interacts with PCNA, the presence of the K+4 submotif, recruits the DCX(DTL) complex, leading to its ubiquitination. {ECO:0000250|UniProtKB:Q9I9A7}. +O35495 CDK14_MOUSE Cyclin-dependent kinase 14 (EC 2.7.11.22) (Cell division protein kinase 14) (Serine/threonine-protein kinase PFTAIRE-1) 469 52,996 Active site (1); Alternative sequence (2); Binding site (1); Chain (1); Domain (1); Modified residue (4); Nucleotide binding (1); Sequence conflict (3) FUNCTION: Serine/threonine-protein kinase involved in the control of the eukaryotic cell cycle, whose activity is controlled by an associated cyclin. Acts as a cell-cycle regulator of Wnt signaling pathway during G2/M phase by mediating the phosphorylation of LRP6 at 'Ser-1490', leading to the activation of the Wnt signaling pathway. Acts as a regulator of cell cycle progression and cell proliferation via its interaction with CCDN3. Phosphorylates RB1 in vitro, however the relevance of such result remains to be confirmed in vivo. May also play a role in meiosis, neuron differentiation and may indirectly act as a negative regulator of insulin-responsive glucose transport (By similarity). {ECO:0000250, ECO:0000269|PubMed:9547506}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasm. Nucleus. Note=Recruited to the cell membrane by CCNY. {ECO:0000250}. SUBUNIT: Found in a complex with LRP6, CCNY and CAPRIN2 during G2/M stage; CAPRIN2 functions as a scaffold for the complex by binding to CCNY via its N terminus and to CDK14 via its C terminus. Interacts with CCNY; CCNY mediates its recruitment to the plasma membrane and promotes phosphorylation of LRP6. Interacts with CCDN3 and CDKN1A. Interacts with SEPT8. Interacts with 14-3-3 proteina YWHAB, YWHAE, YWHAH and YWHAQ. {ECO:0000250|UniProtKB:O94921}. TISSUE SPECIFICITY: In the adult, widely expressed at low levels except in brain, kidney and testis where expression is high. In the brain, detected in cortex, hippocampus, dentate gyrus, amygdala cortex, parasubiculum and cerebellum. In the embryo, expressed predominantly in the nervous system. {ECO:0000269|PubMed:9547506}. +P53566 CEBPA_MOUSE CCAAT/enhancer-binding protein alpha (C/EBP alpha) 359 37,430 Alternative sequence (3); Chain (1); Compositional bias (3); Cross-link (2); DNA binding (1); Domain (1); Modified residue (5); Mutagenesis (9); Region (7); Sequence conflict (2) FUNCTION: Transcription factor that coordinates proliferation arrest and the differentiation of myeloid progenitors, adipocytes, hepatocytes, and cells of the lung and the placenta (PubMed:8415748, PubMed:15107404, PubMed:15589173). Binds directly to the consensus DNA sequence 5'-T[TG]NNGNAA[TG]-3' acting as an activator on distinct target genes. During early embryogenesis, plays essential and redundant functions with CEBPB (PubMed:15509779). Essential for the transition from common myeloid progenitors (CMP) to granulocyte/monocyte progenitors (GMP) (PubMed:24367003). Critical for the proper development of the liver and the lung (PubMed:8798745). Necessary for terminal adipocyte differentiation, is required for postnatal maintenance of systemic energy homeostasis and lipid storage (PubMed:1935900, PubMed:8090719). To regulate these different processes at the proper moment and tissue, interplays with other transcription factors and modulators. Downregulates the expression of genes that maintain cells in an undifferentiated and proliferative state through E2F1 repression, which is critical for its ability to induce adipocyte and granulocyte terminal differentiation. Reciprocally E2F1 blocks adipocyte differentiation by binding to specific promoters and repressing CEBPA binding to its target gene promoters (PubMed:11672531). Proliferation arrest also depends on a functional binding to SWI/SNF complex (PubMed:14660596). In liver, regulates gluconeogenesis and lipogenesis through different mechanisms. To regulate gluconeogenesis, functionally cooperates with FOXO1 binding to IRE-controlled promoters and regulating the expression of target genes such as PCK1 or G6PC (PubMed:17627282). To modulate lipogenesis, interacts and transcriptionally synergizes with SREBF1 in promoter activation of specific lipogenic target genes such as ACAS2 (PubMed:17290224). In adipose tissue, seems to act as FOXO1 coactivator accessing to ADIPOQ promoter through FOXO1 binding sites (PubMed:17090532). {ECO:0000250|UniProtKB:P05554, ECO:0000250|UniProtKB:P49715, ECO:0000269|PubMed:11672531, ECO:0000269|PubMed:14660596, ECO:0000269|PubMed:15107404, ECO:0000269|PubMed:15509779, ECO:0000269|PubMed:15589173, ECO:0000269|PubMed:17090532, ECO:0000269|PubMed:17290224, ECO:0000269|PubMed:17627282, ECO:0000269|PubMed:1935900, ECO:0000269|PubMed:24367003, ECO:0000269|PubMed:8090719, ECO:0000269|PubMed:8415748, ECO:0000269|PubMed:8798745}.; FUNCTION: Isoform 3: Can act as dominant-negative. Binds DNA and have transctivation activity, even if much less efficiently than isoform 2. Does not inhibit cell proliferation. {ECO:0000250|UniProtKB:P05554, ECO:0000250|UniProtKB:P49715, ECO:0000269|PubMed:8415748}.; FUNCTION: Isoform 4: Directly and specifically enhances ribosomal DNA transcription interacting with RNA polymerase I-specific cofactors and inducing histone acetylation. {ECO:0000250|UniProtKB:P49715}. PTM: Sumoylated, sumoylation blocks the inhibitory effect on cell proliferation by disrupting the interaction with SMARCA2. {ECO:0000250|UniProtKB:P05554}.; PTM: Phosphorylation at Ser-193 is required for interaction with CDK2, CDK4 and SWI/SNF complex leading to cell cycle inhibition. Dephosphorylated at Ser-193 by protein phosphatase 2A (PP2A) through PI3K/AKT signaling pathway regulation (PubMed:15107404). Phosphorylation at Thr-222 and Thr-226 by GSK3 is constitutive in adipose tissue and lung. In liver, both Thr-222 and Thr-226 are phosphorylated only during feeding but not during fasting (PubMed:17290224). Phosphorylation of the GSK3 consensus sites selectively decreases transactivation activity on IRE-controlled promoters (PubMed:17290224). {ECO:0000269|PubMed:15107404, ECO:0000269|PubMed:17290224}.; PTM: Ubiquitinated by COP1 upon interaction with TRIB1. {ECO:0000250|UniProtKB:P49715}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8415748}.; SUBCELLULAR LOCATION: Isoform 4: Nucleus, nucleolus {ECO:0000250|UniProtKB:P05554, ECO:0000250|UniProtKB:P49715}. SUBUNIT: Binds DNA as a homodimer and as a heterodimer. Can form stable heterodimers with CEBPB, CEBPD, CEBPE and CEBPG (By similarity). Interacts with PRDM16 (PubMed:19641492). Interacts with UBN1 (By similarity). Interacts with ZNF638; this interaction increases transcriptional activation (PubMed:21602272). Interacts with the complex TFDP2:E2F1; the interaction prevents CEBPA binding to target gene promoters and represses its transcriptional activity (By similarity). Interacts with RB1 (PubMed:15107404). Interacts (when phosphorylated at SER-193) with CDK2, CDK4, E2F4 and SMARCA2 (PubMed:15107404). Interacts with SREBPF1 (PubMed:17290224). Interacts with FOXO1 (via the Fork-head domain); the interaction increases when FOXO1 is deacetylated (PubMed:17090532, PubMed:17627282). Isoform 1 and isoform 4 interact with TAF1A and UBTF. Isoform 4 interacts with NPM1 (By similarity). Interacts (via recognition sequence) with TRIB1 (By similarity). {ECO:0000250|UniProtKB:P05554, ECO:0000250|UniProtKB:P49715, ECO:0000269|PubMed:15107404, ECO:0000269|PubMed:17090532, ECO:0000269|PubMed:17290224, ECO:0000269|PubMed:17627282, ECO:0000269|PubMed:19641492, ECO:0000269|PubMed:21602272}. DOMAIN: The recognition sequence (54-72) is required for interaction with TRIB1. {ECO:0000250|UniProtKB:P49715}. TISSUE SPECIFICITY: Isoform 2 and isoform 3 are expressed in adipose tissue and liver (at protein level). {ECO:0000269|PubMed:8415748}. +Q9D871 CEA18_MOUSE Carcinoembryonic antigen-related cell adhesion molecule 18 376 42,215 Chain (1); Disulfide bond (1); Domain (1); Glycosylation (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 331 351 Helical. {ECO:0000255}. TOPO_DOM 31 330 Extracellular. {ECO:0000255}.; TOPO_DOM 352 376 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Mostly expressed in the small and large intestine and at lower levels also in other organs. {ECO:0000269|PubMed:16139472}. +P06909 CFAH_MOUSE Complement factor H (Protein beta-1-H) 1234 139,138 Beta strand (10); Chain (1); Disulfide bond (40); Domain (20); Glycosylation (7); Helix (2); Modified residue (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Glycoprotein that plays an essential role in maintaining a well-balanced immune response by modulating complement activation. Acts as a soluble inhibitor of complement, where its binding to self markers such as glycan structures prevents complement activation and amplification on cell surfaces. Accelerates the decay of the complement alternative pathway (AP) C3 convertase C3bBb, thus preventing local formation of more C3b, the central player of the complement amplification loop. As a cofactor of the serine protease factor I, CFH also regulates proteolytic degradation of already-deposited C3b. In addition, mediates several cellular responses through interaction with specific receptors. For example, interacts with CR3/ITGAM receptor and thereby mediates the adhesion of human neutrophils to different pathogens. In turn, these pathogens are phagocytosed and destroyed. {ECO:0000250|UniProtKB:P08603}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P08603}. SUBUNIT: Homodimer. Forms also homooligomers. Interacts with complement protein C3b; this interaction inhibits complement activation. Interacts with complement protein C3d. Interacts with CR3/ITGAM; this interaction mediates adhesion of neutrophils to pathogens leading to pathogen clearance. {ECO:0000250|UniProtKB:P08603}. DOMAIN: Sushi 1-3 domain represents the minimal unit capable of cofactor activity. The property to discriminate self surfaces from non-self surfaces depends on the C-terminal region made of Sushis 19-20. {ECO:0000250|UniProtKB:P08603}. TISSUE SPECIFICITY: CFH is one of the most abundant complement components in blood where the liver is the major source of CFH protein in vivo. in addition, CFH is secreted by additional cell types including monocytes, fibroblasts, or endothelial cells. {ECO:0000250|UniProtKB:P08603}. +Q921C5 BICD2_MOUSE Protein bicaudal D homolog 2 (Bic-D 2) 820 93,391 Alternative sequence (3); Chain (1); Coiled coil (3); Erroneous initiation (1); Frameshift (1); Initiator methionine (1); Modified residue (11); Region (4) FUNCTION: Acts as an adapter protein linking the dynein motor complex to various cargos and converts dynein from a non-processive to a highly processive motor in the presence of dynactin. Facilitates and stabilizes the interaction between dynein and dynactin and activates dynein processivity (the ability to move along a microtubule for a long distance without falling off the track) (PubMed:11483508, PubMed:25035494, PubMed:24986880, PubMed:22956769). Facilitates the binding of RAB6A to the Golgi by stabilizing its GTP-bound form (PubMed:25962623). Regulates coat complex coatomer protein I (COPI)-independent Golgi-endoplasmic reticulum transport via its interaction with RAB6A and recruitment of the dynein-dynactin motor complex (PubMed:12447383, PubMed:25962623). Contributes to nuclear and centrosomal positioning prior to mitotic entry through regulation of both dynein and kinesin-1. During G2 phase of the cell cycle, associates with RANBP2 at the nuclear pores and recruits dynein and dynactin to the nuclear envelope to ensure proper positioning of the nucleus relative to centrosomes prior to the onset of mitosis (PubMed:20386726). {ECO:0000269|PubMed:11483508, ECO:0000269|PubMed:12447383, ECO:0000269|PubMed:20386726, ECO:0000269|PubMed:22956769, ECO:0000269|PubMed:24986880, ECO:0000269|PubMed:25035494, ECO:0000269|PubMed:25962623}. PTM: Phosphorylated by NEK9 in vitro. {ECO:0000250|UniProtKB:Q8TD16}. SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:11483508, ECO:0000269|PubMed:12447383, ECO:0000269|PubMed:25962623}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11483508}. Cytoplasm {ECO:0000250|UniProtKB:Q8TD16}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q8TD16}. Nucleus envelope {ECO:0000250|UniProtKB:Q8TD16}. Note=In interphase cells mainly localizes to the Golgi complex and colocalizes with dynactin at microtubule plus ends (PubMed:11483508). Localizes to the nuclear envelope and cytoplasmic stacks of nuclear pore complex known as annulate lamellae in a RANBP2-dependent manner during G2 phase of the cell cycle (By similarity). {ECO:0000250|UniProtKB:Q8TD16, ECO:0000269|PubMed:11483508}. SUBUNIT: Interacts with CPNE4 (via VWFA domain) (PubMed:12522145). Interacts with NEK9 (By similarity). Interacts with DCTN2 (PubMed:11483508, PubMed:22956769). Interacts with RAB6A (PubMed:12447383, PubMed:25962623). Interacts with DNAI1 (By similarity). Interacts with DYNLL1, DYNC1H1, DYNC1I2 and DCTN1 (PubMed:22956769). Forms a complex with dynein and dynactin (PubMed:24986880). The dynein-dynactin-BICD2 ternary complex (DDB) binds preferentially to tyrosinated microtubules than to detyrosinated microtubules (PubMed:26968983). Interacts with RANBP2, RAB6A and KIF5A (PubMed:20386726). Interacts with KIF1C (By similarity). {ECO:0000250|UniProtKB:Q8TD16, ECO:0000269|PubMed:11483508, ECO:0000269|PubMed:12447383, ECO:0000269|PubMed:12522145, ECO:0000269|PubMed:20386726, ECO:0000269|PubMed:22956769, ECO:0000269|PubMed:24986880, ECO:0000269|PubMed:25035494, ECO:0000269|PubMed:25962623, ECO:0000269|PubMed:26968983}. DOMAIN: The fourth coiled coil region is involved in Golgi targeting and in the interaction with DCTN2. {ECO:0000269|PubMed:11483508}. TISSUE SPECIFICITY: Ubiquitously expressed with high expression in the spinal cord. {ECO:0000269|PubMed:23664119}. +Q9D2C7 BI1_MOUSE Bax inhibitor 1 (BI-1) (Testis-enhanced gene transcript protein) (Transmembrane BAX inhibitor motif-containing protein 6) 237 26,478 Chain (1); Cross-link (1); Intramembrane (1); Sequence conflict (2); Topological domain (8); Transmembrane (6) INTRAMEM 207 227 Helical. {ECO:0000255}. TRANSMEM 30 50 Helical. {ECO:0000255}.; TRANSMEM 53 73 Helical. {ECO:0000255}.; TRANSMEM 87 107 Helical. {ECO:0000255}.; TRANSMEM 113 133 Helical. {ECO:0000255}.; TRANSMEM 140 160 Helical. {ECO:0000255}.; TRANSMEM 167 187 Helical. {ECO:0000255}. TOPO_DOM 1 29 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 51 52 Lumenal. {ECO:0000255}.; TOPO_DOM 74 86 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 108 112 Lumenal. {ECO:0000255}.; TOPO_DOM 134 139 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 161 166 Lumenal. {ECO:0000255}.; TOPO_DOM 188 206 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 228 237 Cytoplasmic. {ECO:0000255}. FUNCTION: Suppressor of apoptosis (By similarity). Modulates unfolded protein response signaling (By similarity). Modulates ER calcium homeostasis by acting as a calcium-leak channel (By similarity). Negatively regulates autophagy and autophagosome formation, especially during periods of nutrient deprivation, and reduces cell survival during starvation (PubMed:21926971). {ECO:0000250|UniProtKB:P55061, ECO:0000269|PubMed:21926971}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P55061}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P55061}. SUBUNIT: Interacts with BCL2 (By similarity). Interacts with BCL2L1 (PubMed:21926971). {ECO:0000250|UniProtKB:P55061, ECO:0000269|PubMed:21926971}. DOMAIN: The intra-membrane loop at the C-terminus acts as a calcium pore, mediating calcium leak from the ER into the cytosol. {ECO:0000250|UniProtKB:P55061}. TISSUE SPECIFICITY: Highly abundant in adult testis. {ECO:0000269|PubMed:8012111}. +Q8CHH5 BICRL_MOUSE BRD4-interacting chromatin-remodeling complex-associated protein-like 1074 114,350 Chain (1); Frameshift (1); Modified residue (2) FUNCTION: Component of SWI/SNF chromatin remodeling subcomplex GBAF that carries out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. {ECO:0000250|UniProtKB:Q6AI39}. SUBUNIT: Component of the multiprotein chromatin-remodeling complexes SWI/SNF: SWI/SNF-A (BAF), SWI/SNF-B (PBAF) and related complexes. The canonical complex contains a catalytic subunit (either SMARCA4/BRG1/BAF190A or SMARCA2/BRM/BAF190B) and at least SMARCE1, ACTL6A/BAF53, SMARCC1/BAF155, SMARCC2/BAF170, and SMARCB1/SNF5/BAF47. Other subunits specific to each of the complexes may also be present permitting several possible combinations developmentally and tissue specific. Component of the SWI/SNF (GBAF) subcomplex, which includes at least BICRA or BICRAL (mutually exclusive), BRD9, SS18, the core BAF subunits, SMARCA2/BRM, SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, SMARCC1/BAF155, and SMARCD1/BAF60A. {ECO:0000269|PubMed:29374058}. +P12791 CP2BA_MOUSE Cytochrome P450 2B10 (EC 1.14.14.1) (CYPIIB10) (CYPIIB20) (Cytochrome P450 2B20) (Cytochrome P450 clone PF3/46) (Cytochrome P450-16-alpha) (P24) (Testosterone 16-alpha hydroxylase) 500 56,744 Alternative sequence (1); Chain (1); Metal binding (1); Modified residue (1); Sequence conflict (10) FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. +O70201 BIRC5_MOUSE Baculoviral IAP repeat-containing protein 5 (Apoptosis inhibitor 4) (Apoptosis inhibitor survivin) (TIAP) 140 16,298 Alternative sequence (3); Beta strand (3); Chain (1); Helix (7); Metal binding (6); Modified residue (9); Repeat (1); Turn (1) FUNCTION: Multitasking protein that has dual roles in promoting cell proliferation and preventing apoptosis. Component of a chromosome passage protein complex (CPC) which is essential for chromosome alignment and segregation during mitosis and cytokinesis. Acts as an important regulator of the localization of this complex; directs CPC movement to different locations from the inner centromere during prometaphase to midbody during cytokinesis and participates in the organization of the center spindle by associating with polymerized microtubules. Involved in the recruitment of CPC to centromeres during early mitosis via association with histone H3 phosphorylated at 'Thr-3' (H3pT3) during mitosis. The complex with RAN plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. May counteract a default induction of apoptosis in G2/M phase. The acetylated form represses STAT3 transactivation of target gene promoters. May play a role in neoplasia. Inhibitor of CASP3 and CASP7. {ECO:0000250|UniProtKB:O15392}. PTM: Ubiquitinated by the Cul9-RING ubiquitin-protein ligase complex, leading to its degradation. Ubiquitination is required for centrosomal targeting. {ECO:0000250|UniProtKB:O15392}.; PTM: Acetylation at Lys-129 results in its homodimerization, while deacetylation promotes the formation of monomers which heterodimerize with XPO1/CRM1 which facilitates its nuclear export. The acetylated form represses STAT3 transactivation. The dynamic equilibrium between its acetylation and deacetylation at Lys-129 determines its interaction with XPO1/CRM1, its subsequent subcellular localization, and its ability to inhibit STAT3 transactivation. {ECO:0000250|UniProtKB:O15392}.; PTM: In vitro phosphorylation at Thr-117 by AURKB prevents interaction with INCENP and localization to mitotic chromosomes. Phosphorylation at Thr-48 by CK2 is critical for its mitotic and anti-apoptotic activities. Phosphorylation at Thr-34 by CDK15 is critical for its anti-apoptotic activity. {ECO:0000250|UniProtKB:O15392}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O15392}. Nucleus {ECO:0000250|UniProtKB:O15392}. Chromosome {ECO:0000250|UniProtKB:O15392}. Chromosome, centromere {ECO:0000250|UniProtKB:O15392}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:O15392}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:O15392}. Midbody {ECO:0000250|UniProtKB:O15392}. Note=Localizes at the centromeres from prophase to metaphase, at the spindle midzone during anaphase and a the midbody during telophase and cytokinesis. Accumulates in the nucleus upon treatment with leptomycin B (LMB), a XPO1/CRM1 nuclear export inhibitor (By similarity). Localizes on chromosome arms and inner centromeres from prophase through metaphase. Localizes to kinetochores in metaphase, distributes to the midzone microtubules in anaphase and at telophase, localizes exclusively to the midbody. Colocalizes with AURKB at mitotic chromosomes. Acetylation at Lys-129 directs its localization to the nucleus by enhancing homodimerization and thereby inhibiting XPO1/CRM1-mediated nuclear export (By similarity). {ECO:0000250|UniProtKB:E3SCZ8, ECO:0000250|UniProtKB:O15392}. SUBUNIT: Monomer or homodimer. Exists as a homodimer in the apo state and as a monomer in the CPC-bound state. The monomer protects cells against apoptosis more efficiently than the dimer. Only the dimeric form is capable of enhancing tubulin stability in cells. When phosphorylated, interacts with LAMTOR5/HBXIP; the resulting complex binds pro-CASP9, as well as active CASP9, but much less efficiently. Component of the chromosomal passenger complex (CPC) composed of at least BIRC5/survivin, CDCA8/borealin, INCENP, AURKB or AURKC; in the complex forms a triple-helix bundle-based subcomplex with INCENP and CDCA8. Interacts with JTB. Interacts (via BIR domain) with histone H3 phosphorylated at 'Thr-3' (H3pT3). Interacts with EVI5. Interacts with GTP-bound RAN in both the S and M phases of the cell cycle. Interacts with USP9X. Interacts with tubulin. Interacts with BIRC2/c-IAP1. The acetylated form at Lys-129 interacts with STAT3. The monomeric form deacetylated at Lys-129 interacts with XPO1/CRM1. The monomeric form interacts with XIAP/BIRC4. Both the dimeric and monomeric form can interact with DIABLO/SMAC. Interacts with BIRC6/bruce. {ECO:0000250|UniProtKB:O15392}. DOMAIN: The BIR repeat is necessary and sufficient for LAMTOR5 binding. {ECO:0000250|UniProtKB:O15392}. +O88738 BIRC6_MOUSE Baculoviral IAP repeat-containing protein 6 (EC 2.3.2.27) (BIR repeat-containing ubiquitin-conjugating enzyme) (BRUCE) (RING-type E3 ubiquitin transferase BIRC6) (Ubiquitin-conjugating BIR domain enzyme apollon) (APOLLON) 4882 532,170 Active site (1); Alternative sequence (2); Chain (1); Compositional bias (6); Erroneous initiation (3); Modified residue (10); Region (1); Repeat (1); Sequence conflict (11) FUNCTION: Anti-apoptotic protein which can regulate cell death by controlling caspases and by acting as an E3 ubiquitin-protein ligase. Has an unusual ubiquitin conjugation system in that it could combine in a single polypeptide, ubiquitin conjugating (E2) with ubiquitin ligase (E3) activity, forming a chimeric E2/E3 ubiquitin ligase. Its tragets include CASP9 and DIABLO/SMAC. Acts as an inhibitor of CASP3, CASP7 and CASP9. Important regulator for the final stages of cytokinesis. Crucial for normal vesicle targeting to the site of abscission, but also for the integrity of the midbody and the midbody ring, and its striking ubiquitin modification. Required for normal placenta development. {ECO:0000269|PubMed:15300255, ECO:0000269|PubMed:15485903, ECO:0000269|PubMed:9628897}. PTM: Ubiquitinated. Ubiquitination is mediated by the RNF41 E3 ligase and leads to proteasomal degradation, impairing inhibition of apoptosis. Deubiquitinated by USP8/UBPY (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q9NR09}. Endosome {ECO:0000250|UniProtKB:Q9NR09}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q9NR09}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9NR09}. Midbody, Midbody ring {ECO:0000250|UniProtKB:Q9NR09}. Note=Exhibits cell cycle-dependent localization. Concentrates in a pericentriolar compartment in interphase, moves partially to spindle poles in metaphase, and finally localizes to the spindle midzone and the midbody in telophase and during cytokinesis. On the midbody, localizes to the midbody ring, also called Flemming body. In interphase cells, localizes to the trans-Golgi network membrane and endosomes. During cytokinesis, a fraction moves to the midzone where it specifically arrives at the midbody ring. After abscission completion, travels with the midbody remnant into one daughter cell, and remains bound to it until a new midbody ring is formed during the next cell division. {ECO:0000250|UniProtKB:Q9NR09}. SUBUNIT: Homodimer. Binds the activated, processed forms of CASP3, CASP6 and CASP7. Interacts with RNF41, KIF23/MKLP1, USP8/UBPY, BIRC5/survivin, MAP2K1/MEK1, RAB8A/RAB8, RAB11A/RAB11, PLK1, EXOC3/SEC6 and EXOC4/SEC8 (By similarity). Interacts with CASP9, DIABLO/SMAC and HTRA2. {ECO:0000250, ECO:0000269|PubMed:15300255}. DOMAIN: The BIR domain is essential for its antiapoptotic function and is important for binding to DIABLO/SMAC and CASP9. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. Highly expressed in the brain and kidney. {ECO:0000269|PubMed:9628897}. +Q9R229 BMP10_MOUSE Bone morphogenetic protein 10 (BMP-10) 421 47,888 Chain (1); Disulfide bond (4); Glycosylation (2); Propeptide (1); Sequence conflict (5); Signal peptide (1) FUNCTION: Required for maintaining the proliferative activity of embryonic cardiomyocytes by preventing premature activation of the negative cell cycle regulator CDKN1C/p57KIP and maintaining the required expression levels of cardiogenic factors such as MEF2C and NKX2-5. Acts as a ligand for ACVRL1/ALK1, BMPR1A/ALK3 and BMPR1B/ALK6, leading to activation of SMAD1, SMAD5 and SMAD8 transcription factors. Inhibits endothelial cell migration and growth. May reduce cell migration and cell matrix adhesion in breast cancer cell lines (By similarity). {ECO:0000250|UniProtKB:O95393, ECO:0000269|PubMed:15073151, ECO:0000269|PubMed:15109497, ECO:0000269|PubMed:16798733}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Homodimer; disulfide-linked (By similarity). Interacts with FBN1 (via N-terminal domain) and FBN2 (By similarity). Interacts with ENG (PubMed:21737454). {ECO:0000250|UniProtKB:O95393, ECO:0000250|UniProtKB:P12643, ECO:0000269|PubMed:21737454}. TISSUE SPECIFICITY: In the embryo, expressed exclusively in the ventricular trabecular myocardium of the developing heart from E9.0-E13.5. By E16.5-E18.5, only detectable in atria. Highly expressed in the adult heart where it is found in the right atrium but not in the left atrium. Lower levels in adult liver and lung. {ECO:0000269|PubMed:10072785, ECO:0000269|PubMed:15073151, ECO:0000269|PubMed:15109497}. +Q91YP1 BN3D2_MOUSE Pre-miRNA 5'-monophosphate methyltransferase (EC 2.1.1.-) (BCDIN3 domain-containing protein) 285 32,035 Chain (1); Domain (1); Sequence conflict (6) FUNCTION: O-methyltransferase that specifically dimethylates the 5' monophosphate of pre-miRNAs, acting as a negative regulator of miRNA processing. The 5' monophosphate of pre-miRNAs is recognized by DICER1 and is required for pre-miRNAs processing: methylation at this position reduces the processing of pre-miRNAs by DICER1. Able to mediate methylation of pre-miR-145, as well as other pre-miRNAs (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with DICER1; the interaction may be mediated by RNA. {ECO:0000250}. +Q8BMQ3 BNC2_MOUSE Zinc finger protein basonuclin-2 1127 125,335 Alternative sequence (1); Chain (1); Compositional bias (1); Cross-link (7); Erroneous initiation (1); Modified residue (1); Sequence conflict (2); Zinc finger (4) FUNCTION: Probable transcription factor specific for skin keratinocytes. May play a role in the differentiation of spermatozoa and oocytes. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15081112}. TISSUE SPECIFICITY: Highly expressed in ovary, testis and kidney. Expressed at moderate levels in skin and small intestine, and at lower levels in lung. Trace amounts of expression detected in liver and colon. Not detected in brain, spleen or thymus. {ECO:0000269|PubMed:14988505, ECO:0000269|PubMed:15081112}. +Q8BHE5 BMP3_MOUSE Bone morphogenetic protein 3 (BMP-3) 468 52,774 Chain (1); Disulfide bond (4); Glycosylation (5); Propeptide (1); Signal peptide (1) FUNCTION: Negatively regulates bone density. Antagonizes the ability of certain osteogenic BMPs to induce osteoprogenitor differentitation and ossification. {ECO:0000269|PubMed:11138004}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}. +O54940 BNIP2_MOUSE BCL2/adenovirus E1B 19 kDa protein-interacting protein 2 326 37,769 Chain (1); Domain (1); Modified residue (5); Sequence conflict (1) FUNCTION: Implicated in the suppression of cell death. Interacts with the BCL-2 and adenovirus E1B 19 kDa proteins (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Localizes to the nuclear envelope region and to other cytoplasmic structures. {ECO:0000250}. +Q8CEI1 BOLA3_MOUSE BolA-like protein 3 110 12,228 Chain (1) FUNCTION: Acts as a mitochondrial iron-sulfur (Fe-S) cluster assembly factor that facilitates (Fe-S) cluster insertion into a subset of mitochondrial proteins. Probably acts together with NFU1. {ECO:0000250|UniProtKB:P39724, ECO:0000250|UniProtKB:Q53S33}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q53S33}. SUBUNIT: Interacts with NFU1. {ECO:0000250|UniProtKB:Q53S33}. +Q9D9J8 BPIA3_MOUSE BPI fold-containing family A member 3 (Short palate, lung and nasal epithelium carcinoma-associated protein 3) 232 25,713 Chain (1); Compositional bias (1); Disulfide bond (1); Glycosylation (3); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q64277 BST1_MOUSE ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2 (EC 3.2.2.6) (ADP-ribosyl cyclase 2) (Antigen BP3) (BP-3 alloantigen) (Bone marrow stromal antigen 1) (BST-1) (Cyclic ADP-ribose hydrolase 2) (cADPr hydrolase 2) (Leukocyte antigen 65) (Ly-65) (CD antigen CD157) 311 34,616 Chain (1); Disulfide bond (5); Glycosylation (4); Lipidation (1); Propeptide (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Synthesizes the second messagers cyclic ADP-ribose and nicotinate-adenine dinucleotide phosphate, the former a second messenger that elicits calcium release from intracellular stores. May be involved in pre-B-cell growth. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. SUBUNIT: Homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the bone marrow, spleen and thymus in lymphoid organs, and the lung, kidney and heart in non-lymphoid organs. +A2AHJ4 BRWD3_MOUSE Bromodomain and WD repeat-containing protein 3 1799 202,942 Alternative sequence (4); Chain (1); Compositional bias (6); Domain (2); Modified residue (6); Repeat (8) FUNCTION: Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape (By similarity). {ECO:0000250}. +Q64152 BTF3_MOUSE Transcription factor BTF3 (Nascent polypeptide-associated complex subunit beta) (NAC-beta) (RNA polymerase B transcription factor 3) 204 22,031 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (1); Modified residue (6); Sequence conflict (3) FUNCTION: When associated with NACA, prevents inappropriate targeting of non-secretory polypeptides to the endoplasmic reticulum (ER). Binds to nascent polypeptide chains as they emerge from the ribosome and blocks their interaction with the signal recognition particle (SRP), which normally targets nascent secretory peptides to the ER. BTF3 is also a general transcription factor that can form a stable complex with RNA polymerase II. Required for the initiation of transcription (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus. Note=The heterodimer with NACA is cytoplasmic. {ECO:0000250}. SUBUNIT: Part of the nascent polypeptide-associated complex (NAC), which is a heterodimer of NACA and BTF3 (via NAC-A/B domains). NAC associates with ribosomes through the BTF3/NACB subunit. Both subunits can contact nascent polypeptide chains (By similarity). {ECO:0000250}. +P50615 BTG3_MOUSE Protein BTG3 (Abundant in neuroepithelium area protein) (BTG family member 3) (Protein Tob5) 252 28,983 Chain (1); Compositional bias (1) FUNCTION: Overexpression impairs serum-induced cell cycle progression from the G0/G1 to S phase. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9067576}. +Q7TST0 BTNL1_MOUSE Butyrophilin-like protein 1 509 57,726 Chain (1); Disulfide bond (2); Domain (3); Erroneous gene model prediction (1); Erroneous initiation (1); Sequence caution (1); Sequence conflict (6); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 251 271 Helical. {ECO:0000255}. TOPO_DOM 28 250 Extracellular. {ECO:0000255}.; TOPO_DOM 272 509 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. +Q8K2J9 BTBD6_MOUSE BTB/POZ domain-containing protein 6 488 53,842 Chain (1); Domain (1); Erroneous initiation (1) FUNCTION: Adapter protein for the cul3 E3 ubiquitin-protein ligase complex (By similarity). Involved in late neuronal development and muscle formation (By similarity). {ECO:0000250|UniProtKB:A9JRD8, ECO:0000250|UniProtKB:Q2LE78}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q2LE78}. Note=Found in punctated bodies in the cytoplasm. {ECO:0000250|UniProtKB:Q2LE78}. +Q3U319 BRE1B_MOUSE E3 ubiquitin-protein ligase BRE1B (BRE1-B) (EC 2.3.2.27) (RING finger protein 40) (RING-type E3 ubiquitin transferase BRE1B) 1001 113,967 Chain (1); Coiled coil (4); Cross-link (2); Erroneous initiation (1); Modified residue (6); Sequence conflict (2); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: Component of the RNF20/40 E3 ubiquitin-protein ligase complex that mediates monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1). H2BK120ub1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation (H3K4me and H3K79me, respectively). It thereby plays a central role in histone code and gene regulation. The RNF20/40 complex forms a H2B ubiquitin ligase complex in cooperation with the E2 enzyme UBE2A or UBE2B; reports about the cooperation with UBE2E1/UBCH are contradictory. Required for transcriptional activation of Hox genes. {ECO:0000250|UniProtKB:O75150}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O75150}. SUBUNIT: Component of the RNF20/40 complex (also known as BRE1 complex) probably composed of 2 copies of RNF20/BRE1A and 2 copies of RNF40/BRE1B. Interacts with UBE2E1/UBCH6. Interacts with RB1 and WAC. {ECO:0000250|UniProtKB:O75150}. +P46737 BRCC3_MOUSE Lys-63-specific deubiquitinase BRCC36 (EC 3.4.19.-) (BRCA1-A complex subunit BRCC36) (BRCA1/BRCA2-containing complex subunit 3) (BRCA1/BRCA2-containing complex subunit 36) (BRISC complex subunit BRCC36) 291 33,340 Alternative sequence (1); Chain (1); Domain (1); Initiator methionine (1); Metal binding (3); Modified residue (2); Motif (1); Sequence conflict (3) FUNCTION: Metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Does not have activity toward 'Lys-48'-linked polyubiquitin chains. Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). In the BRCA1-A complex, it specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX, antagonizing the RNF8-dependent ubiquitination at double-strand breaks (DSBs). Catalytic subunit of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates. Mediates the specific 'Lys-63'-specific deubiquitination associated with the COP9 signalosome complex (CSN), via the interaction of the BRISC complex with the CSN complex. The BRISC complex is required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating NUMA1. Plays a role in interferon signaling via its role in the deubiquitination of the interferon receptor IFNAR1; deubiquitination increases IFNAR1 activity by enhancing its stability and cell surface expression. Down-regulates the response to bacterial lipopolysaccharide (LPS) via its role in IFNAR1 deubiquitination. {ECO:0000250|UniProtKB:P46736}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P46736}. Cytoplasm {ECO:0000250|UniProtKB:P46736}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:P46736}. Note=Localizes at sites of DNA damage at double-strand breaks (DSBs). Interaction with ABRAXAS2 retains BRCC3 in the cytoplasm. {ECO:0000250|UniProtKB:P46736}. SUBUNIT: Component of the ARISC complex, at least composed of UIMC1/RAP80, ABRAXAS1, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1. Component of the BRCA1-A complex, at least composed of BRCA1, BARD1, UIMC1/RAP80, ABRAXAS1, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1. In the BRCA1-A complex, interacts directly with ABRAXAS1 and BABAM2. Component of the BRISC complex, at least composed of ABRAXAS2, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1. Identified in a complex with SHMT2 and the other subunits of the BRISC complex. In the BRISC complex, interacts directly with ABRAXAS2. Identified in a complex with ABRAXAS2 and NUMA1. The BRISC complex interacts with the CSN complex. Component of the BRCA1/BRCA2 containing complex (BRCC), which also contains BRCA1, BRCA2, BARD1, BABAM2 and RAD51. BRCC is a ubiquitin E3 ligase complex that enhances cellular survival following DNA damage. Interacts with BRCA1. Binds polyubiquitin. {ECO:0000250|UniProtKB:P46736}. +Q9CY21 BUD23_MOUSE Probable 18S rRNA (guanine-N(7))-methyltransferase (EC 2.1.1.-) (Bud site selection protein 23 homolog) (Williams-Beuren syndrome chromosomal region 22 protein homolog) (rRNA methyltransferase and ribosome maturation factor) 281 31,587 Chain (1) FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(7) position of a guanine in 18S rRNA. Requires the methyltransferase adapter protein TRM112 for full rRNA methyltransferase activity. Involved in the pre-rRNA processing steps leading to small-subunit rRNA production independently of its RNA-modifying catalytic activity. Important for biogenesis end export of the 40S ribosomal subunit independent on its methyltransferase activity. Locus-specific steroid receptor coactivator. Potentiates transactivation by glucocorticoid (NR3C1), mineralocorticoid (NR3C2), androgen (AR) and progesterone (PGR) receptors. Required for the maintenance of open chromatin at the TSC22D3/GILZ locus to facilitate NR3C1 loading on the response elements. Required for maintenance of dimethylation on histone H3 'Lys-79' (H3K79me2), although direct histone methyltransferase activity is not observed in vitro. {ECO:0000250|UniProtKB:O43709}. PTM: May be ubiquitinated and targeted to degradation in response to proinflammatory cytokine signaling. {ECO:0000250|UniProtKB:O43709}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O43709}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P25627}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O43709}. Cytoplasm {ECO:0000250|UniProtKB:O43709}. Note=Localized diffusely throughout the nucleus and the cytoplasm. Localizes to a polarized perinuclear structure, overlapping partially with the Golgi and lysosomes. Localization is not affected by glucocorticoid treatment. {ECO:0000250|UniProtKB:O43709}. SUBUNIT: Heterodimer with TRMT112; this heterodimerization is necessary for the metabolic stability and activity of the catalytic subunit BUD23. Interacts with GRIP1. {ECO:0000250|UniProtKB:O43709}. +O35658 C1QBP_MOUSE Complement component 1 Q subcomponent-binding protein, mitochondrial (GC1q-R protein) (Glycoprotein gC1qBP) (C1qBP) 278 31,013 Chain (1); Modified residue (6); Mutagenesis (4); Region (2); Transit peptide (1) "FUNCTION: Is believed to be a multifunctional and multicompartmental protein involved in inflammation and infection processes, ribosome biogenesis, protein synthesis in mitochondria, regulation of apoptosis, transcriptional regulation and pre-mRNA splicing. At the cell surface is thought to act as an endothelial receptor for plasma proteins of the complement and kallikrein-kinin cascades. Putative receptor for C1q; specifically binds to the globular ""heads"" of C1q thus inhibiting C1; may perform the receptor function through a complex with C1qR/CD93. In complex with cytokeratin-1/KRT1 is a high affinity receptor for kininogen-1/HMWK. Can also bind other plasma proteins, such as coagulation factor XII leading to its autoactivation. May function to bind initially fluid kininogen-1 to the cell membrane. The secreted form may enhance both extrinsic and intrinsic coagulation pathways. It is postulated that the cell surface form requires docking with transmembrane proteins for downstream signaling which might be specific for a cell-type or response. By acting as C1q receptor is involved in chemotaxis of immature dendritic cells and neutrophils and is proposed to signal through CD209/DC-SIGN on immature dendritic cells, through integrin alpha-4/beta-1 during trophoblast invasion of the decidua, and through integrin beta-1 during endothelial cell adhesion and spreading. Signaling involved in inhibition of innate immune response is implicating the PI3K-AKT/PKB pathway. Required for protein synthesis in mitochondria (PubMed:22904065, PubMed:28942965). In mitochondrial translation may be involved in formation of functional 55S mitoribosomes; the function seems to involve its RNA-binding activity (PubMed:22904065, PubMed:28942965). May be involved in the nucleolar ribosome maturation process; the function may involve the exchange of FBL for RRP1 in the association with pre-ribosome particles. Involved in regulation of RNA splicing by inhibiting the RNA-binding capacity of SRSF1 and its phosphorylation. Is required for the nuclear translocation of splicing factor U2AF1L4. Involved in regulation of CDKN2A- and HRK-mediated apoptosis. May be involved in regulation of FOXC1 transcriptional activity and NFY/CCAAT-binding factor complex-mediated transcription. May play a role in antibacterial defense. {ECO:0000250|UniProtKB:Q07021, ECO:0000269|PubMed:17486078, ECO:0000269|PubMed:18166172, ECO:0000269|PubMed:18460468, ECO:0000269|PubMed:22904065, ECO:0000269|PubMed:28942965}." SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:17486078, ECO:0000269|PubMed:18166172}. Nucleus {ECO:0000250|UniProtKB:Q07021}. Cell membrane {ECO:0000250|UniProtKB:Q07021}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q07021}; Extracellular side {ECO:0000250|UniProtKB:Q07021}. Secreted {ECO:0000250|UniProtKB:Q07021}. Cytoplasm {ECO:0000250|UniProtKB:Q07021}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q07021}. Note=Seems to be predominantly localized to mitochondria (PubMed:17486078, PubMed:18166172). Secreted by activated lymphocytes (By similarity). {ECO:0000250|UniProtKB:Q07021, ECO:0000269|PubMed:17486078, ECO:0000269|PubMed:18166172}. SUBUNIT: Homotrimer; three monomers form a donut-shaped structure with an unusually asymmetric charge distribution on the surface (PubMed:22904065). Interacts with CDK13, HRK, VTN, NFYB, ADRA1B, FOXC1, DDX21, DDX50, NCL, SRSF1 and SRSF9 (PubMed:17486078). Interacts with CD93; the association may represent a cell surface C1q receptor. Interacts with KRT1; the association represents a cell surface kininogen receptor. Interacts with CD209; the interaction is indicative for a C1q:C1QBP:CD209 signaling complex. Interacts with FBL and RRP1; the respective interactions with C1QBP are competetive. Probably associates with the mitoribosome. Interacts with MAVS; the interaction occurs upon viral transfection. Interacts with PPIF (PubMed:20950273). Interacts with U2AF1L4 (PubMed:18460468). Interacts with PLEKHN1 (By similarity). {ECO:0000250|UniProtKB:Q07021, ECO:0000269|PubMed:17486078, ECO:0000269|PubMed:18460468, ECO:0000269|PubMed:20950273}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9414106}. +Q5HZI2 C2C4C_MOUSE C2 calcium-dependent domain-containing protein 4C (Nuclear-localized factor 3) (Protein FAM148C) 419 44,614 Chain (1); Domain (1); Modified residue (3); Sequence conflict (2) +P0CG09 C2C4D_MOUSE C2 calcium-dependent domain-containing protein 4D 341 36,865 Chain (1); Domain (1) +Q9JMG2 C1GLC_MOUSE C1GALT1-specific chaperone 1 (Core 1 beta1,3-galactosyltransferase 2) (C1Gal-T2) (C1GalT2) (Core 1 beta3-Gal-T2) (mC1Gal-T2) (Core 1 beta3-galactosyltransferase-specific molecular chaperone) 316 36,067 Chain (1); Topological domain (2); Transmembrane (1) TRANSMEM 7 26 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 27 316 Lumenal. {ECO:0000255}. FUNCTION: Probable chaperone required for the generation of 1 O-glycan Gal-beta1-3GalNAc-alpha1-Ser/Thr (T antigen), which is a precursor for many extended O-glycans in glycoproteins. Probably acts as a specific molecular chaperone assisting the folding/stability of core 1 beta-3-galactosyltransferase (C1GALT1) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. SUBUNIT: Associates with core 1 beta-3-galactosyltransferase (C1GALT1), probably not with the soluble active form. {ECO:0000250}. +Q8BRN9 C2D1B_MOUSE Coiled-coil and C2 domain-containing protein 1B (Five prime repressor element under dual repression-binding protein 2) (FRE under dual repression-binding protein 2) (Freud-2) 848 93,091 Chain (1); Coiled coil (2); Compositional bias (1); Domain (1); Modified residue (3); Sequence conflict (2) FUNCTION: Transcription factor that binds specifically to the DRE (dual repressor element) and represses HTR1A gene transcription in neuronal cells. {ECO:0000269|PubMed:21155902}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21155902}. +Q8CJ91 C209B_MOUSE CD209 antigen-like protein B (DC-SIGN-related protein 1) (DC-SIGNR1) (OtB7) (CD antigen CD209) 325 37,112 Alternative sequence (3); Beta strand (7); Chain (1); Disulfide bond (3); Domain (1); Erroneous initiation (1); Glycosylation (3); Helix (3); Metal binding (6); Sequence conflict (23); Topological domain (2); Transmembrane (1); Turn (2) TRANSMEM 53 73 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 52 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 74 325 Extracellular. {ECO:0000255}. FUNCTION: Probable pathogen-recognition receptor. May mediate the endocytosis of pathogens which are subsequently degraded in lysosomal compartments. May recognize in a calcium-dependent manner high mannose N-linked oligosaccharides in a variety of pathogen antigens. Is a receptor for ICAM3, probably by binding to mannose-like carbohydrates. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in skin, spleen and lung, probably in a subset of dendritic cells. Detected in spleen extrafollicular paracortical areas including the red pulp and marginal zones, and at lower levels, in the follicular area. Detected in skin suprabasal areas adjacent to the epidermis and in epidermal cell layer. {ECO:0000269|PubMed:12137941}. +Q497N6 C295L_MOUSE CEP295 N-terminal-like protein (Differential display clone 8) (KIAA1731 N-terminal like protein) 533 61,957 Chain (1); Coiled coil (2); Sequence conflict (3) SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000269|PubMed:19706271}. Note=Colocalizes to the motile cilium of mature spermatozoa. TISSUE SPECIFICITY: Expressed in mature spermatozoa (at protein level). Detected in retina, lung and kidney. In brain, highly expressed in brain-stem, cerebral cortex and thalamus with lesser expression in cerebellum and hippocampus. {ECO:0000269|PubMed:16985004, ECO:0000269|PubMed:19706271}. +Q3TQQ9 CA112_MOUSE Uncharacterized protein C1orf112 homolog 903 101,222 Alternative sequence (2); Chain (1); Modified residue (2); Sequence conflict (5) +Q8BGN9 CA115_MOUSE Uncharacterized protein C1orf115 homolog 141 15,388 Chain (1); Transmembrane (1) TRANSMEM 115 137 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q91ZM8 CABP7_MOUSE Calcium-binding protein 7 (CaBP7) (Calneuron II) (Calneuron-2) 215 24,453 Calcium binding (2); Chain (1); Domain (2); Topological domain (2); Transmembrane (1) TRANSMEM 189 209 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 1 188 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 210 215 Extracellular. {ECO:0000255}. FUNCTION: Negatively regulates Golgi-to-plasma membrane trafficking by interacting with PI4KB and inhibiting its activity. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. SUBUNIT: Interacts with PI4KB. This binding competes with FREQ/NCS1 binding in a calcium-dependent manner (By similarity). {ECO:0000250}. DOMAIN: The C-terminal transmembrane domain (TMD) is necessary and sufficient for membrane targeting. {ECO:0000250}. +P47934 CACP_MOUSE Carnitine O-acetyltransferase (Carnitine acetylase) (EC 2.3.1.7) (Carnitine acetyltransferase) (CAT) (CrAT) 626 70,840 Active site (1); Beta strand (24); Binding site (7); Chain (1); Helix (22); Modified residue (4); Motif (1); Mutagenesis (3); Region (1); Sequence conflict (6); Turn (6) FUNCTION: Catalyzes the reversible transfer of acyl groups from carnitine to coenzyme A (CoA) and regulates the acyl-CoA/CoA ratio. Also plays a crucial role in the transport of fatty acids for beta-oxidation. May be specific for short chain fatty acids. {ECO:0000250|UniProtKB:P43155}. SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000305}. Peroxisome {ECO:0000305}. Mitochondrion inner membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Matrix side {ECO:0000305}. SUBUNIT: Monomer. {ECO:0000269|PubMed:12526798, ECO:0000269|PubMed:15155726}. +Q8CAK1 CAF17_MOUSE Putative transferase CAF17 homolog, mitochondrial (EC 2.1.-.-) (Iron-sulfur cluster assembly factor homolog) 358 38,399 Chain (1); Modified residue (3); Sequence conflict (1); Transit peptide (1) FUNCTION: Involved in the maturation of mitochondrial 4Fe-4S proteins functioning late in the iron-sulfur cluster assembly pathway. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. +Q8R100 CAHM5_MOUSE Calcium homeostasis modulator protein 5 (Protein FAM26E) 309 35,285 Chain (1); Frameshift (1); Transmembrane (4) TRANSMEM 18 38 Helical. {ECO:0000255}.; TRANSMEM 49 69 Helical. {ECO:0000255}.; TRANSMEM 99 119 Helical. {ECO:0000255}.; TRANSMEM 181 201 Helical. {ECO:0000255}. FUNCTION: Pore-forming subunit of a voltage-gated ion channel. {ECO:0000250|UniProtKB:Q8IU99}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8CI85 CAH12_MOUSE Carbonic anhydrase 12 (EC 4.2.1.1) (Carbonate dehydratase XII) (Carbonic anhydrase XII) (CA-XII) 354 39,695 Active site (2); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (4); Metal binding (3); Region (1); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 302 322 Helical. {ECO:0000255}. TOPO_DOM 25 301 Extracellular. {ECO:0000255}.; TOPO_DOM 323 354 Cytoplasmic. {ECO:0000255}. FUNCTION: Reversible hydration of carbon dioxide. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +Q9D6N1 CAH13_MOUSE Carbonic anhydrase 13 (EC 4.2.1.1) (Carbonate dehydratase XIII) (Carbonic anhydrase XIII) (CA-XIII) 262 29,522 Active site (3); Chain (1); Domain (1); Metal binding (3); Region (1) FUNCTION: Reversible hydration of carbon dioxide. TISSUE SPECIFICITY: Expressed in spleen, lung, kidney, heart, brain, skeletal muscle and testis. {ECO:0000269|PubMed:14600151}. +Q9R100 CAD17_MOUSE Cadherin-17 (BILL-cadherin) (Liver-intestine cadherin) (LI-cadherin) (P130) 827 91,645 Chain (1); Domain (7); Glycosylation (7); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 787 807 Helical. {ECO:0000255}. TOPO_DOM 26 786 Extracellular. {ECO:0000255}.; TOPO_DOM 808 827 Cytoplasmic. {ECO:0000255}. FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. LI-cadherin may have a role in the morphological organization of liver and intestine. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. DOMAIN: Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain. {ECO:0000250}. TISSUE SPECIFICITY: Highest expression is found in intestine with lower expression in spleen, bone marrow, lung and testis. No expression detected in liver, kidney, heart, brain or skeletal muscle. Expressed in precursor B-cells and myeloid cells. {ECO:0000269|PubMed:10906147}. +Q6TDU8 CASC1_MOUSE Protein CASC1 (Cancer susceptibility candidate gene 1 protein homolog) (Lung adenoma susceptibility protein 1) 730 84,966 Alternative sequence (5); Chain (1); Compositional bias (1); Natural variant (1) TISSUE SPECIFICITY: Expressed in lung. {ECO:0000269|PubMed:14583591}. +P19228 CASA1_MOUSE Alpha-S1-casein (Alpha-casein) 313 35,602 Chain (1); Modified residue (6); Region (1); Repeat (15); Signal peptide (1) FUNCTION: Important role in the capacity of milk to transport calcium phosphate. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Mammary gland specific. Secreted in milk. +Q7TN73 CASD1_MOUSE N-acetylneuraminate 9-O-acetyltransferase (EC 2.3.1.45) (CAS1 domain-containing protein 1) (Sialate O-acetyltransferase) (SOAT) 797 91,603 Active site (3); Chain (1); Erroneous initiation (2); Glycosylation (3); Topological domain (16); Transmembrane (15) TRANSMEM 19 39 Helical. {ECO:0000255}.; TRANSMEM 314 334 Helical. {ECO:0000255}.; TRANSMEM 364 384 Helical. {ECO:0000255}.; TRANSMEM 396 416 Helical. {ECO:0000255}.; TRANSMEM 440 460 Helical. {ECO:0000255}.; TRANSMEM 462 482 Helical. {ECO:0000255}.; TRANSMEM 487 507 Helical. {ECO:0000255}.; TRANSMEM 514 534 Helical. {ECO:0000255}.; TRANSMEM 547 567 Helical. {ECO:0000255}.; TRANSMEM 600 620 Helical. {ECO:0000255}.; TRANSMEM 639 659 Helical. {ECO:0000255}.; TRANSMEM 672 692 Helical. {ECO:0000255}.; TRANSMEM 699 719 Helical. {ECO:0000255}.; TRANSMEM 726 746 Helical. {ECO:0000255}.; TRANSMEM 771 791 Helical. {ECO:0000255}. TOPO_DOM 1 18 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 40 313 Lumenal. {ECO:0000250|UniProtKB:Q96PB1}.; TOPO_DOM 335 363 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 385 395 Lumenal. {ECO:0000305}.; TOPO_DOM 417 439 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 461 461 Lumenal. {ECO:0000305}.; TOPO_DOM 483 486 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 508 513 Lumenal. {ECO:0000305}.; TOPO_DOM 535 546 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 568 599 Lumenal. {ECO:0000305}.; TOPO_DOM 621 638 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 660 671 Lumenal. {ECO:0000305}.; TOPO_DOM 693 698 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 720 725 Lumenal. {ECO:0000305}.; TOPO_DOM 747 770 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 792 797 Lumenal. {ECO:0000305}. FUNCTION: O-acetyltransferase that catalyzes 9-O-acetylation of sialic acids. Sialic acids are sugars at the reducing end of glycoproteins and glycolipids, and are involved in various processes such as cell-cell interactions, host-pathogen recognition. {ECO:0000250|UniProtKB:Q96PB1}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q96PB1}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q96PB1}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q96PB1}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:12840045}. +P29452 CASP1_MOUSE Caspase-1 (CASP-1) (EC 3.4.22.36) (Interleukin-1 beta convertase) (IL-1BC) (Interleukin-1 beta-converting enzyme) (ICE) (IL-1 beta-converting enzyme) (p45) [Cleaved into: Caspase-1 subunit p20; Caspase-1 subunit p10] 402 45,640 Active site (2); Chain (2); Domain (1); Modified residue (2); Propeptide (2); Sequence conflict (1) FUNCTION: Thiol protease that cleaves IL-1 beta between an Asp and an Ala, releasing the mature cytokine which is involved in a variety of inflammatory processes. Important for defense against pathogens. Cleaves and activates sterol regulatory element binding proteins (SREBPs). Can also promote apoptosis (By similarity). Upon inflammasome activation, during DNA virus infection but not RNA virus challenge, controls antiviral immunity through the cleavage of CGAS, rendering it inactive (PubMed:28314590). {ECO:0000250|UniProtKB:P29466, ECO:0000269|PubMed:28314590}. PTM: The two subunits are derived from the precursor sequence by a autocatalytic mechanism. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a 20 kDa (p20) and a 10 kDa (p10) subunit. The p20 subunit can also form a heterodimer with the epsilon isoform which then has an inhibitory effect. May be a component of the inflammasome, a protein complex which also includes PYCARD, CARD8 and NALP2 and whose function would be the activation of proinflammatory caspases. Both the p20 and p10 subunits interact with MEFV (By similarity). Interacts with CARD17/INCA and CARD18 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: High level expression seen in spleen and lung, low level expression seen in brain, heart, liver, kidney, testis and skeletal muscle. +P55097 CATK_MOUSE Cathepsin K (EC 3.4.22.38) 329 36,889 Active site (3); Beta strand (11); Chain (1); Disulfide bond (3); Glycosylation (2); Helix (8); Propeptide (1); Sequence conflict (2); Signal peptide (1); Turn (3) FUNCTION: Closely involved in osteoclastic bone resorption and may participate partially in the disorder of bone remodeling. Displays potent endoprotease activity against fibrinogen at acid pH. May play an important role in extracellular matrix degradation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Lysosome {ECO:0000250}. +Q5SPV6 CB073_MOUSE Uncharacterized protein C2orf73 homolog 233 26,410 Alternative sequence (1); Chain (1) +P06797 CATL1_MOUSE Cathepsin L1 (EC 3.4.22.15) (Cathepsin L) (Major excreted protein) (MEP) (p39 cysteine proteinase) [Cleaved into: Cathepsin L1 heavy chain; Cathepsin L1 light chain] 334 37,547 Active site (3); Chain (2); Disulfide bond (3); Glycosylation (1); Propeptide (2); Sequence conflict (5); Signal peptide (1) FUNCTION: Important for the overall degradation of proteins in lysosomes. SUBCELLULAR LOCATION: Lysosome. SUBUNIT: Dimer of a heavy and a light chain linked by disulfide bonds. +Q8R3C1 CB042_MOUSE Uncharacterized protein C2orf42 homolog 574 64,071 Alternative sequence (4); Chain (1); Sequence conflict (6) +Q63918 CAVN2_MOUSE Caveolae-associated protein 2 (Cavin-2) (Phosphatidylserine-binding protein) (Serum deprivation-response protein) 418 46,764 Chain (1); Coiled coil (2); Initiator methionine (1); Modified residue (23); Region (2); Sequence conflict (3) FUNCTION: Plays an important role in caveolar biogenesis and morphology. Regulates caveolae morphology by inducing membrane curvature within caveolae (By similarity). Plays a role in caveola formation in a tissue-specific manner. Required for the formation of caveolae in the lung and fat endothelia but not in the heart endothelia. Negatively regulates the size or stability of CAVIN complexes in the lung endothelial cells (PubMed:23652019). May play a role in targeting PRKCA to caveolae (By similarity). {ECO:0000250|UniProtKB:O95810, ECO:0000250|UniProtKB:Q66H98, ECO:0000269|PubMed:23652019}. PTM: The N-terminus is blocked. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:18332105, ECO:0000269|PubMed:19546242}. Membrane, caveola {ECO:0000269|PubMed:19546242}. Note=Localizes in the caveolae in a caveolin-dependent manner. {ECO:0000269|PubMed:19546242}. SUBUNIT: Component of the CAVIN complex composed of CAVIN1, CAVIN2, CAVIN3 and CAVIN4 (PubMed:19546242). Binds to PRKCA in the presence of phosphatidylserine. Interacts with CAVIN4; this augments the transactivation of NPPA by CAVIN4 (By similarity). Interacts with CAVIN1 (PubMed:25588833, PubMed:19546242). Interacts with CAV3 (By similarity). {ECO:0000250|UniProtKB:O95810, ECO:0000250|UniProtKB:Q66H98, ECO:0000269|PubMed:19546242, ECO:0000269|PubMed:25588833}. DOMAIN: The leucine-zipper domain is essential for its localization in the caveolae. {ECO:0000250|UniProtKB:O95810}. TISSUE SPECIFICITY: Heart, adipose tissue, lung and endothelial cells (at protein level). Highly expressed in kidney and expressed at lower levels in liver, spleen, thymus, stomach, intestine and uterus. {ECO:0000269|PubMed:19546242, ECO:0000269|PubMed:23652019, ECO:0000269|PubMed:8241023}. +Q06770 CBG_MOUSE Corticosteroid-binding globulin (CBG) (Serpin A6) (Transcortin) 397 44,769 Binding site (3); Chain (1); Glycosylation (6); Signal peptide (1); Site (1) FUNCTION: Major transport protein for glucocorticoids and progestins in the blood of almost all vertebrate species. SUBCELLULAR LOCATION: Secreted. DOMAIN: Proteolytic cleavage leads to an important conformation change. This reduces the affinity for steroids (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed by the liver; secreted in plasma. +Q91VJ2 CAVN3_MOUSE Caveolae-associated protein 3 (Cavin-3) (Protein kinase C delta-binding protein) (Serum deprivation response factor-related gene product that binds to C-kinase) 260 27,853 Chain (1); Cross-link (1); Modified residue (5); Region (3); Sequence conflict (1) FUNCTION: Regulates the traffic and/or budding of caveolae (By similarity). Plays a role in caveola formation in a tissue-specific manner. Required for the formation of caveolae in smooth muscle but not in the lung and heart endothelial cells (PubMed: 28285351, PubMed:23652019). Regulates the equilibrium between cell surface-associated and cell surface-dissociated caveolae by promoting the rapid release of caveolae from the cell surface (PubMed:25588833). Plays a role in the regulation of the circadian clock. Modulates the period length and phase of circadian gene expression and also regulates expression and interaction of the core clock components PER1/2 and CRY1/2 (PubMed:23079727). {ECO:0000250|UniProtKB:Q969G5, ECO:0000269|PubMed:23079727, ECO:0000269|PubMed:23652019, ECO:0000269|PubMed:25588833, ECO:0000269|PubMed:28285351}. PTM: In vitro, phosphorylated by PRKCD. {ECO:0000269|PubMed:9054438}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23079727}. Cytoplasm, cytosol {ECO:0000269|PubMed:19546242}. Membrane, caveola {ECO:0000269|PubMed:19546242, ECO:0000269|PubMed:25588833}. Note=Localizes in the caveolae in a caveolin-dependent manner. {ECO:0000269|PubMed:19546242, ECO:0000269|PubMed:25588833}. SUBUNIT: Component of the CAVIN complex composed of CAVIN1, CAVIN2, CAVIN3 and CAVIN4 (PubMed:19546242). Interacts with PRKCD and with phosphatidylserine. Phosphatidylserine may form a bridge between PKC and PKC-binding partners and stabilize the binding (PubMed:9054438). Interacts with PER2 (PubMed:23079727). Interacts with CAVIN1 (PubMed:19546242, PubMed:25588833). Interacts (via leucine-zipper domain) with CAV1 in a cholesterol-sensitive manner (PubMed:25588833). Interacts with EPS15L1 (By similarity). {ECO:0000250|UniProtKB:Q969G5, ECO:0000269|PubMed:19546242, ECO:0000269|PubMed:23079727, ECO:0000269|PubMed:25588833, ECO:0000269|PubMed:9054438}. DOMAIN: The leucine-zipper domain is essential for its localization in the caveolae and for its interaction with CAV1 and EPS15L1. {ECO:0000250|UniProtKB:Q969G5}. TISSUE SPECIFICITY: Lung, heart, skeletal muscle, liver, brain, vascular and urinary bladder smooth muscle (at protein level). Strongly expressed in uterus, ovary, mammary and epithelial cells. Also expressed in spleen, intestine, kidney and testis. {ECO:0000269|PubMed:19546242, ECO:0000269|PubMed:23652019, ECO:0000269|PubMed:28285351, ECO:0000269|PubMed:9054438}. +Q80XL1 CBLC_MOUSE E3 ubiquitin-protein ligase CBL-C (EC 2.3.2.27) (RING-type E3 ubiquitin transferase CBL-C) (SH3-binding protein CBL-3) (SH3-binding protein CBL-C) (Signal transduction protein CBL-C) 496 55,715 Alternative sequence (2); Binding site (1); Calcium binding (1); Chain (1); Domain (1); Modified residue (1); Region (5); Sequence conflict (4); Zinc finger (1) FUNCTION: Acts as an E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome. Functionally coupled with the E2 ubiquitin-protein ligases UB2D1, UB2D2 and UB2D3. Regulator of EGFR mediated signal transduction; upon EGF activation, ubiquitinates EGFR. Isoform 1, but not isoform 2, inhibits EGF stimulated MAPK1 activation. Promotes ubiquitination of SRC phosphorylated at 'Tyr-424', has the highest ubiquitin ligase activity among CBL family proteins. In collaboration with CD2AP may act as regulatory checkpoint for Ret signaling by modulating the rate of RET degradation after ligand activation; CD2AP converts it from an inhibitor to a promoter of RET degradation; the function limits the potency of GDNF on neuronal survival. {ECO:0000250|UniProtKB:Q9ULV8}. PTM: Phosphorylated on tyrosines by EGFR. {ECO:0000250}.; PTM: Phosphorylated on multiple tyrosine residues by SRC. Isoform 1, but not isoform 2, is phosphorylated on tyrosines by EGFR. {ECO:0000250|UniProtKB:Q9ULV8}.; PTM: Autoubiquitinated, when phosphorylated at Tyr-340. {ECO:0000250|UniProtKB:Q9ULV8}. SUBUNIT: Interacts with Ubiquitin-conjugating enzyme E2 UBE2D2 and UBE2D3. Isoform 1 interacts with EGFR (tyrosine phosphorylated). Interacts with the SH3 domain proteins LYN and CRK. Interacts (via RING-type zinc finger) with TGFB1I1 (via LIM zinc-binding domain 2); the interaction is direct and enhances the E3 activity. Interacts directly with RET (inactive) and CD2AP; dissociates from RET upon RET activation by GDNF which also increases the interaction with CD2AP suggesting dissociation as CBLC:CD2AP complex. Interacts with SRC; the interaction is enhanced when SRC is phosphorylated at 'Tyr-419'. {ECO:0000250|UniProtKB:Q9ULV8}. DOMAIN: EF-hand-like and Sh2-like domains are required for N-terminal inhibition of E3 activity. {ECO:0000250|UniProtKB:Q9ULV8}.; DOMAIN: The N-terminus is composed of the phosphotyrosine binding (PTB) domain, a short linker region and the RING-type zinc finger. The PTB domain, which is also called TKB (tyrosine kinase binding) domain, is composed of three different subdomains: a four-helix bundle (4H), a calcium-binding EF hand and a divergent SH2 domain. {ECO:0000255|PROSITE-ProRule:PRU00839}.; DOMAIN: The RING-type zinc finger domain mediates binding to an E2 ubiquitin-conjugating enzyme. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed in tissues, where the expression is restricted to epithelial cells (at protein level). {ECO:0000269|PubMed:11162497, ECO:0000269|PubMed:14560016}. +Q9JJN5 CBPN_MOUSE Carboxypeptidase N catalytic chain (CPN) (EC 3.4.17.3) (Carboxypeptidase N polypeptide 1) (Carboxypeptidase N small subunit) 457 51,845 Active site (1); Chain (1); Disulfide bond (2); Glycosylation (3); Metal binding (3); Region (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Protects the body from potent vasoactive and inflammatory peptides containing C-terminal Arg or Lys (such as kinins or anaphylatoxins) which are released into the circulation. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000269|PubMed:10878383}. SUBUNIT: Tetramer of two catalytic chains and two glycosylated inactive chains. {ECO:0000250}. TISSUE SPECIFICITY: Mainly expressed in liver. Also detected in lung, stomach, intestine, spleen and kidney. {ECO:0000269|PubMed:10878383, ECO:0000269|PubMed:11342641}. +Q9D1C2 CBY1_MOUSE Protein chibby homolog 1 (Cytosolic leucine-rich protein) (PIGEA-14) (PKD2 interactor, Golgi and endoplasmic reticulum-associated 1) 127 14,535 Chain (1); Coiled coil (1); Modified residue (2); Region (1) FUNCTION: Inhibits the Wnt/Wingless pathway by binding to CTNNB1/beta-catenin and inhibiting beta-catenin-mediated transcriptional activation through competition with TCF/LEF transcription factors. Has also been shown to play a role in regulating the intracellular trafficking of polycystin-2/PKD2 and possibly of other intracellular proteins. Promotes adipocyte and cardiomyocyte differentiation. {ECO:0000250|UniProtKB:Q9Y3M2, ECO:0000269|PubMed:17261658, ECO:0000269|PubMed:17403895}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q9Y3M2}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q9Y3M2}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q9Y3M2}. Golgi apparatus {ECO:0000250|UniProtKB:Q9Y3M2}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q9Y3M2}. SUBUNIT: Homodimer. Interacts with polycystin-2/PKD2 and GM130. Interacts with the C-terminal region of CTNNB1. Interacts (C-terminus) with TCIM (C-terminus), TCIM competes with CTNNB1 for the interaction with CBY1. Interacts with FAM92A; this interaction facilites targeting of FAM92A to cilium basal body. {ECO:0000250|UniProtKB:Q9Y3M2}. TISSUE SPECIFICITY: Found in heart, brain, lung, liver, muscle, kidney and testis. Levels are approximately 3-fold higher in embryonic and adult heart than in lung or liver. {ECO:0000269|PubMed:17261658}. +Q8BME9 CBLN4_MOUSE Cerebellin-4 (Cerebellin-like glycoprotein 1) 198 21,609 Beta strand (9); Chain (1); Disulfide bond (2); Domain (1); Glycosylation (2); Helix (1); Mutagenesis (2); Sequence conflict (1); Signal peptide (1); Turn (1) FUNCTION: May be involved in synaptic functions in the CNS. May play a role in CBLN3 export from the endoplasmic reticulum and secretion. SUBCELLULAR LOCATION: Secreted. Cell junction, synapse. SUBUNIT: Homohexamer; disulfide-linked homotrimers. The trimers are assembled via the globular C1q domains. The trimers associate via N-terminal cysteine residues to form disulfide-linked hexamers (By similarity). May form oligomers with CBLN1, CBLN2 and CBLN3 prior to secretion. Once secreted, does not interact with other CBLN family members. Strongly interacts with DCC in a NTN1-displaceable fashion. Weakly binds to NRXN1 and NRXN2 long and short isoforms produced by alternative promoter usage. Interaction with NRXN3 short isoform is hardly detectable; no interaction at all with NRXN3 long isoform. Does not interact with GRID1 and GRID2. {ECO:0000250, ECO:0000269|PubMed:17030622, ECO:0000269|PubMed:22220752}. TISSUE SPECIFICITY: Expressed in brain with high levels in particular thalamic nuclei. In the thalamus, predominantly expressed in neurons within the parafascicular nucleus (at protein level). Very low or no expression in most other brain regions. {ECO:0000269|PubMed:16930405, ECO:0000269|PubMed:22220752}. +Q8R0K4 CC137_MOUSE Coiled-coil domain-containing protein 137 290 32,918 Chain (1); Coiled coil (2); Erroneous termination (1) SUBCELLULAR LOCATION: Chromosome {ECO:0000250|UniProtKB:Q6PK04}. +Q8C5S3 CC022_MOUSE Uncharacterized protein C3orf22 homolog 137 15,533 Chain (1) +Q3UX62 CC114_MOUSE Coiled-coil domain-containing protein 114 658 74,120 Chain (1); Coiled coil (3); Compositional bias (1); Modified residue (4) FUNCTION: Probable component of the outer dynein arm complex required along the entire axoneme for tethering of outer dynein arms. {ECO:0000250|UniProtKB:Q96M63}. SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000250|UniProtKB:Q96M63}. SUBUNIT: Interacts with CCDC151. Interacts with TTC25; this interaction may facilitate the recruitment and/or attachment of outer dynein arm docking complex proteins, including CCDC114, CCDC151 and ARMC4, to ciliary axonemes. {ECO:0000250|UniProtKB:Q96M63}. TISSUE SPECIFICITY: Expressed in motile ciliated tissues. {ECO:0000269|PubMed:23261303}. +Q3URK1 CC190_MOUSE Coiled-coil domain-containing protein 190 288 32,592 Chain (1); Coiled coil (1) +Q6PFY9 CC14B_MOUSE Dual specificity protein phosphatase CDC14B (EC 3.1.3.16) (EC 3.1.3.48) (CDC14 cell division cycle 14 homolog B) 485 55,661 Active site (1); Alternative sequence (1); Chain (1); Motif (1); Region (3); Sequence conflict (1) FUNCTION: Dual-specificity phosphatase involved in DNA damage response. Essential regulator of the G2 DNA damage checkpoint: following DNA damage, translocates to the nucleus and dephosphorylates FZR1/CDH1, a key activator of the anaphase promoting complex/cyclosome (APC/C). Dephosphorylates SIRT2 around early anaphase. Dephosphorylation of FZR1/CDH1 activates the APC/C, leading to the ubiquitination of PLK1, preventing entry into mitosis. Preferentially dephosphorylates proteins modified by proline-directed kinases (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Note=Following DNA damage, translocates from the nucleolus to the nucleoplasm and interacts with FZR1/CDH1. {ECO:0000250}. SUBUNIT: Interacts with FZR1/CDH1. {ECO:0000250}. DOMAIN: Composed of two structurally equivalent A and B domains that adopt a dual specificity protein phosphatase (DSP) fold. +Q4QRL3 CC88B_MOUSE Coiled-coil domain-containing protein 88B (Gipie) (Hook-related protein 3) (HkRP3) 1481 166,608 Alternative sequence (1); Chain (1); Coiled coil (3); Compositional bias (1); Modified residue (4) FUNCTION: Acts as a positive regulator of T-cell maturation and inflammatory function. Required for several functions of T-cells in both the CD4(+) and the CD8(+) compartments and this includes expression of cell surface markers of activation, proliferation, and cytokine production in response to specific or non-specific stimulation and during the course of infection with the mouse malaria parasite Plasmodium berghei (PubMed:25403443). Enhances NK cell cytotoxicity by positively regulating polarization of microtubule-organizing center (MTOC) to cytotoxic synapse, lytic granule transport along microtubules, and dynein-mediated clustering to MTOC (By similarity). Interacts with HSPA5 and stabilizes the interaction between HSPA5 and ERN1, leading to suppression of ERN1-induced JNK activation and endoplasmic reticulum stress-induced apoptosis (PubMed:21289099). {ECO:0000250|UniProtKB:A6NC98, ECO:0000269|PubMed:21289099, ECO:0000269|PubMed:25403443}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:25403443}; Peripheral membrane protein {ECO:0000305}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000250|UniProtKB:A6NC98}. Endoplasmic reticulum {ECO:0000250|UniProtKB:A6NC98}. Golgi apparatus {ECO:0000250|UniProtKB:A6NC98}. Cytoplasm {ECO:0000250|UniProtKB:A6NC98}. SUBUNIT: Homodimer (By similarity). Interacts with DOCK8 (By similarity). Interacts (via C-terminus) with intact microtubules (By similarity). Interacts with dynein-dynactin motor complex (By similarity). Interacts (via C-terminus) with HSPA5 (PubMed:21289099). {ECO:0000250|UniProtKB:A6NC98, ECO:0000269|PubMed:21289099}. TISSUE SPECIFICITY: Abundantly expressed in immune cells, including both CD4(+) and CD8(+) T-cells and in myeloid cells (at protein level) (PubMed:25403443). Expressed in endothelium (at protein level) (PubMed:21289099). Expressed specifically in spleen, bone marrow, lymph nodes and thymus (PubMed:25403443). Expressed in liver and heart (PubMed:21289099). {ECO:0000269|PubMed:21289099, ECO:0000269|PubMed:25403443}. +P83917 CBX1_MOUSE Chromobox protein homolog 1 (Heterochromatin protein 1 homolog beta) (HP1 beta) (Heterochromatin protein p25) (M31) (Modifier 1 protein) 185 21,418 Beta strand (8); Binding site (16); Chain (1); Cross-link (4); Domain (2); Helix (4); Modified residue (3); Mutagenesis (4); Turn (3) FUNCTION: Component of heterochromatin. Recognizes and binds histone H3 tails methylated at 'Lys-9', leading to epigenetic repression. Interaction with lamin B receptor (LBR) can contribute to the association of the heterochromatin with the inner nuclear membrane. {ECO:0000269|PubMed:11242053, ECO:0000269|PubMed:11571267}. PTM: Not phosphorylated. {ECO:0000250}.; PTM: Ubiquitinated. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Unassociated with chromosomes during mitosis. {ECO:0000250}. SUBUNIT: Homodimer (PubMed:10747027). Interacts directly with CHAF1A, EMSY, LBR, TIF1/TIF1A and TRIM28/TIF1B PXVXL motif via the chromoshadow domain (PubMed:8978696, PubMed:10562550, PubMed:10747027). Interacts directly with histone H3 methylated at 'Lys-9' via the chromo domain (PubMed:11571267). Interacts with SUV39H1, SETDB1, KMT5B and KMT5C (PubMed:10202156, PubMed:15145825). Interacts with PRDM6 (PubMed:16537907). Interacts with POGZ (By similarity). Interacts with CHAMP1 (By similarity). Interacts with INCENP (By similarity). Interacts with SGO1; the CBX1 homodimer binds to one molecule of SGO1 (By similarity). Interacts with LRIF1 (via PxVxL motif) (By similarity). {ECO:0000250|UniProtKB:P83916, ECO:0000269|PubMed:10202156, ECO:0000269|PubMed:10562550, ECO:0000269|PubMed:10747027, ECO:0000269|PubMed:11571267, ECO:0000269|PubMed:15145825, ECO:0000269|PubMed:16537907, ECO:0000269|PubMed:8978696}. TISSUE SPECIFICITY: In all adult and embryonic tissues. {ECO:0000269|PubMed:1708124}. +J3QM76 CC179_MOUSE Coiled-coil domain-containing protein 179 67 7,928 Chain (1); Coiled coil (1) +P0C7Q1 CC153_MOUSE Coiled-coil domain-containing protein 153 202 23,394 Chain (1); Coiled coil (1) +Q5SPX1 CC157_MOUSE Coiled-coil domain-containing protein 157 718 79,795 Alternative sequence (1); Chain (1); Coiled coil (1); Erroneous initiation (2); Sequence conflict (1) +O55187 CBX4_MOUSE E3 SUMO-protein ligase CBX4 (EC 2.3.2.-) (Chromobox protein homolog 4) (E3 SUMO-protein transferase CBX4) (Polycomb 2 homolog) (Pc2) (mPc2) 551 60,523 Alternative sequence (1); Chain (1); Compositional bias (1); Cross-link (21); Domain (1); Modified residue (3); Sequence conflict (2) Protein modification; protein sumoylation. FUNCTION: E3 SUMO-protein ligase which facilitates SUMO1 conjugation by UBE2I. Involved in the sumoylation of HNRNPK, a p53/TP53 transcriptional coactivator, hence indirectly regulates p53/TP53 transcriptional activation resulting in p21/CDKN1A expression. {ECO:0000250|UniProtKB:O00257}.; FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development (By similarity). PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility (By similarity). Binds to histone H3 trimethylated at 'Lys-9' (H3K9me3) (PubMed:16537902). Plays a role in the lineage differentiation of the germ layers in embryonic development (PubMed:22226355). {ECO:0000250|UniProtKB:O00257, ECO:0000269|PubMed:16537902, ECO:0000269|PubMed:22226355}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O00257}. Nucleus speckle {ECO:0000250|UniProtKB:O00257}. SUBUNIT: Interacts with SUV39H1 and HIPK2 (By similarity). Interacts with CSNK2B (By similarity). Component of a PRC1-like complex (By similarity). The composition of the PRC1 complex differs between the PRC1 complex in pluripotent embryonic stem cells containing RNF2, CBX7 and PCGF2, and the PRC1 complex in differentiating cells containing RNF2, CBX2, CBX4 and BMI1 (PubMed:22226355). Interacts with RNF2 (PubMed:22226355). Interacts (via chromodomain) with histone H3K9Me3 and single-stranded RNA (ssRNA) (PubMed:16537902). Interacts with CHTOP (PubMed:22872859). May interact with HIST2H3A and HIST1H3A (By similarity). {ECO:0000250|UniProtKB:O00257, ECO:0000269|PubMed:16537902, ECO:0000269|PubMed:22226355, ECO:0000269|PubMed:22872859}. DOMAIN: The polyhistidine repeat may act as a targeting signal to nuclear speckles. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in embryoid bodies. {ECO:0000269|PubMed:22226355}. +Q8VDS3 CBX7_MOUSE Chromobox protein homolog 7 158 18,109 Beta strand (4); Chain (1); Domain (1); Helix (3); Mutagenesis (4) FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development (PubMed:16537902, PubMed:22226355). PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. Promotes histone H3 trimethylation at 'Lys-9' (H3K9me3) (By similarity). Binds to histone H3 trimethylated at 'Lys-9' (H3K9me3) or at 'Lys-27' (H3K27me3) (PubMed:16537902, PubMed:22226355). Trimethylation at 'Lys-27' (H3K27me3) is important for chromatin recruitment (PubMed:22226355, PubMed:16537902). May possibly also bind trimethylated lysine residues in other proteins (in vitro) (PubMed:16537902). Binds non-coding, single-stranded RNA and double-stranded RNA (PubMed:20541999, PubMed:16537902). Plays a role in the timely repression of differentiation-specific genes in pluripotent embryonic stem cells to maintain the undifferentiated state (PubMed:22226355). Regulator of cellular lifespan by maintaining the repression of CDKN2A, but not by inducing telomerase activity (PubMed:14647293). {ECO:0000250|UniProtKB:O95931, ECO:0000269|PubMed:14647293, ECO:0000269|PubMed:16537902, ECO:0000269|PubMed:20541999, ECO:0000269|PubMed:22226355}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14647293, ECO:0000269|PubMed:16537902, ECO:0000269|PubMed:20541999}. Chromosome {ECO:0000269|PubMed:16537902, ECO:0000269|PubMed:22226355}. Note=Requires trimethylation at 'Lys-27' (H3K27me3) for the localization to chromatin (PubMed:22226355). Localizes to facultative heterochromatin and to the inactivated X chromosome in females (PubMed:16537902). {ECO:0000269|PubMed:16537902, ECO:0000269|PubMed:22226355}. SUBUNIT: Component of a PRC1-like complex (PubMed:22226355). Distinct PRC1-like core complexes are composed of a RING1 subunit (RING1B or RING1A), one of the six PCGF proteins (PCGF1-6), one PHC protein (PHC1-3) and one of the CBX proteins (CBX2, CBX4, CBX6, CBX7 or CBX8) (PubMed:22226355). The composition of the PRC1 complex may differ between the PRC1 complex in pluripotent embryonic stem cells containing RNF2, CBX7 and PCGF2, and the PRC1 complex in differentiating cells containing RNF2, CBX2, CBX4 and BMI1 (PubMed:22226355). Interacts with RING1 (PubMed:14647293). Interacts with RNF2, PHC1 and PCGF2 (PubMed:22226355). Interacts (via chromodomain) with histone H3K9Me3 and H3K27me3 (PubMed:16537902). Interacts with H3K9Me2 and H4K20Me1 (PubMed:16537902). Interacts (via chromodomain) with single-stranded and double-stranded RNA; RNA binding seems to be required for the localization to chromatin (PubMed:16537902). Interacts with PCGF1, PCGF3, PCGF5 and PCGF6 (By similarity). {ECO:0000250|UniProtKB:O95931, ECO:0000269|PubMed:14647293, ECO:0000269|PubMed:16537902, ECO:0000269|PubMed:22226355}. TISSUE SPECIFICITY: Expressed in embryonic stem cells. {ECO:0000269|PubMed:16537902, ECO:0000269|PubMed:22226355}. +Q3TTL0 CC038_MOUSE Uncharacterized protein C3orf38 homolog 348 39,532 Chain (1); Sequence conflict (2) FUNCTION: May be involved in apoptosis regulation. {ECO:0000250}. +Q6P2K3 CC067_MOUSE Uncharacterized protein C3orf67 homolog 674 75,131 Chain (1); Sequence conflict (1) +E9Q0B3 CC080_MOUSE Uncharacterized membrane protein C3orf80 homolog 247 25,757 Chain (1); Compositional bias (1); Signal peptide (1); Transmembrane (1) TRANSMEM 82 102 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q8K2I2 CCHCR_MOUSE Coiled-coil alpha-helical rod protein 1 (Alpha-helical coiled-coil rod protein) 770 87,105 Chain (1); Coiled coil (3); Erroneous initiation (1); Sequence conflict (1) FUNCTION: May be a regulator of keratinocyte proliferation or differentiation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. +Q3TVC7 CCDB1_MOUSE Cyclin-D1-binding protein 1 (Grap2 and cyclin-D-interacting protein) (Maternal Id-like protein) (Stage specific embryonic cDNA-8 protein) (SSEC-8) 356 39,356 Alternative sequence (2); Chain (1); Frameshift (1); Initiator methionine (1); Modified residue (1); Region (5) FUNCTION: May negatively regulate cell cycle progression. May act at least in part via inhibition of the cyclin-D1/CDK4 complex, thereby preventing phosphorylation of RB1 and blocking E2F-dependent transcription (By similarity). May be required for hepatocyte proliferation. {ECO:0000250, ECO:0000269|PubMed:17256742}. PTM: Phosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Interacts with CCND1 and GRAP2. May also interact with COPS5, RPLP0, SIRT6, SYF2 and TCF3. {ECO:0000250}. TISSUE SPECIFICITY: Expressed at high levels in brain, intestine, muscle and ovary and at lower levels in heart, kidney, liver, lung, spleen and testis. {ECO:0000269|PubMed:9186056}. +Q3UJV1 CCD61_MOUSE Coiled-coil domain-containing protein 61 511 57,368 Chain (1); Coiled coil (1); Compositional bias (1); Modified residue (8) +O70460 CCL19_MOUSE C-C motif chemokine 19 (Epstein-Barr virus-induced molecule 1 ligand chemokine) (EBI1 ligand chemokine) (ELC) (Small-inducible cytokine A19) 108 11,911 Chain (1); Disulfide bond (2); Glycosylation (1); Signal peptide (1) FUNCTION: Strongly chemotactic for naive (L-selectinhi) CD4 T-cells and for CD8 T-cells and weakly attractive for resting B-cells and memory (L-selectinlo) CD4 T-cells. May play a role in promoting encounters between recirculating T-cells and dendritic cells and in the migration of activated B-cells into the T-zone of secondary lymphoid tissues. Binds to chemokine receptor CCR7. Binds to atypical chemokine receptor ACKR4 and mediates the recruitment of beta-arrestin (ARRB1/2) to ACKR4. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Highly expressed by dendritic cells in mesenteric and peripheral lymph nodes. Significant expression in spleen (T cell zone or periarteriolar lymphatic sheath) and Peyer patches. Low expression in thymus. +Q8VCC6 CCM2L_MOUSE Cerebral cavernous malformations 2 protein-like (CCM2-like) 481 52,174 Alternative sequence (2); Chain (1); Compositional bias (1) +Q03366 CCL7_MOUSE C-C motif chemokine 7 (Intercrine/chemokine MARC) (Monocyte chemoattractant protein 3) (Monocyte chemotactic protein 3) (MCP-3) (Protein FIC) (Small-inducible cytokine A7) 97 10,999 Chain (1); Disulfide bond (2); Glycosylation (1); Modified residue (1); Sequence conflict (2); Signal peptide (1) FUNCTION: Chemotactic factor that attracts monocytes and eosinophils, but not neutrophils. Augments monocyte anti-tumor activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Monomer. {ECO:0000250}. +Q9Z1X0 CCL27_MOUSE C-C motif chemokine 27 (CC chemokine ILC) (Cutaneous T-cell-attracting chemokine) (CTACK) (ESkine) (IL-11 R-alpha-locus chemokine) (ALP) (mILC) (Skinkine) (Small-inducible cytokine A27) 120 13,464 Alternative sequence (1); Chain (1); Disulfide bond (2); Sequence conflict (4); Signal peptide (1) FUNCTION: Chemotactic factor that attracts skin-associated memory T-lymphocytes. May play a role in mediating homing of lymphocytes to cutaneous sites. May play a role in cell migration during embryogenesis. Nuclear forms may facilitate cellular migration by inducing cytoskeletal relaxation. Binds to CCR10. SUBCELLULAR LOCATION: Isoform 1: Secreted {ECO:0000269|PubMed:10559234}. Nucleus {ECO:0000269|PubMed:10559234}. Note=May also be nuclear when following receptor (CCR10)-mediated internalization. {ECO:0000269|PubMed:10559234}.; SUBCELLULAR LOCATION: Isoform 2: Nucleus {ECO:0000269|PubMed:10559234, ECO:0000269|PubMed:12133963}. SUBUNIT: Monomer, dimer, and tetramer. Heparin avidly promotes oligomerization (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Isoform 1 is predominantly expressed in placenta and weakly in skin. Isoform 2 is predominantly expressed in testes and brain, weakly in kidney and liver and even lower in heart and muscle. Low expression of both isoforms in other tissues. +Q61456 CCNA1_MOUSE Cyclin-A1 421 47,772 Chain (1); Sequence conflict (1) FUNCTION: May be involved in the control of the cell cycle at the G1/S (start) and G2/M (mitosis) transitions. May primarily function in the control of the germline meiotic cell cycle and additionally in the control of mitotic cell cycle in some somatic cells. {ECO:0000269|PubMed:10068472, ECO:0000269|PubMed:9843212}. PTM: Polyubiquitinated via 'Lys-11'-linked ubiquitin by the anaphase-promoting complex (APC/C), leading to its degradation by the proteasome. Deubiquitinated and stabilized by USP37 enables entry into S phase (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, spindle. Note=In oocytes at least, it associates with the spindle during metaphase. SUBUNIT: Interacts with INCA1 and KLHDC9 (By similarity). Interacts with the CDK2 and CDC2 protein kinases to form a serine/threonine kinase holoenzyme complex. The cyclin subunit imparts substrate specificity to the complex. Found in a complex with CDK2, CABLES1 and CCNE1. {ECO:0000250|UniProtKB:P78396, ECO:0000269|PubMed:11585773}. TISSUE SPECIFICITY: Testis and ovaries. +P24860 CCNB1_MOUSE G2/mitotic-specific cyclin-B1 430 48,052 Chain (1); Compositional bias (1); Modified residue (6); Region (2); Sequence conflict (12) FUNCTION: Essential for the control of the cell cycle at the G2/M (mitosis) transition. PTM: Ubiquitinated by the SCF(NIPA) complex during interphase, leading to its destruction. Not ubiquitinated during G2/M phases (By similarity). {ECO:0000250}.; PTM: Phosphorylated by PLK1 at Ser-130 on centrosomes during prophase: phosphorylation by PLK1 does not cause nuclear import. Phosphorylation at Ser-144 was also reported to be mediated by PLK1 but Ser-130 seems to be the primary phosphorylation site (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. SUBUNIT: Interacts with the CDC2 protein kinase to form a serine/threonine kinase holoenzyme complex also known as maturation promoting factor (MPF). The cyclin subunit imparts substrate specificity to the complex. Binds HEI10. Interacts with catalytically active RALBP1 and CDC2 during mitosis to form an endocytotic complex during interphase. Interacts with CCNF; interaction is required for nuclear localization. Interacts with CDK5RAP3 (By similarity). Interacts with RFPL4A and UBE2A (PubMed:12525704). Interacts with INCA1 (By similarity). {ECO:0000250|UniProtKB:P14635, ECO:0000269|PubMed:12525704}. +P51945 CCNG1_MOUSE Cyclin-G1 (Cyclin-G) 294 33,903 Chain (1); Sequence conflict (2) FUNCTION: May play a role in growth regulation. Is associated with G2/M phase arrest in response to DNA damage. May be an intermediate by which p53 mediates its role as an inhibitor of cellular proliferation. {ECO:0000269|PubMed:8887688, ECO:0000269|PubMed:9696022}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9696022}. SUBUNIT: Binds to B' regulatory B subunits of protein phosphatase A (PP2A) following induction by p53 (in vitro). TISSUE SPECIFICITY: Highest levels in kidney, heart and skeletal muscle. +Q9WUT7 CCR9_MOUSE C-C chemokine receptor type 9 (C-C CKR-9) (CC-CKR-9) (CCR-9) (Chemokine C-C receptor 10) (CD antigen CDw199) 369 41,913 Chain (1); Disulfide bond (2); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 49 74 Helical; Name=1. {ECO:0000250|UniProtKB:P51686}.; TRANSMEM 86 109 Helical; Name=2. {ECO:0000250|UniProtKB:P51686}.; TRANSMEM 121 150 Helical; Name=3. {ECO:0000250|UniProtKB:P51686}.; TRANSMEM 160 185 Helical; Name=4. {ECO:0000250|UniProtKB:P51686}.; TRANSMEM 209 243 Helical; Name=5. {ECO:0000250|UniProtKB:P51686}.; TRANSMEM 249 283 Helical; Name=6. {ECO:0000250|UniProtKB:P51686}.; TRANSMEM 291 321 Helical; Name=7. {ECO:0000250|UniProtKB:P51686}. TOPO_DOM 1 48 Extracellular. {ECO:0000250|UniProtKB:P51686}.; TOPO_DOM 75 85 Cytoplasmic. {ECO:0000250|UniProtKB:P51686}.; TOPO_DOM 110 120 Extracellular. {ECO:0000250|UniProtKB:P51686}.; TOPO_DOM 151 159 Cytoplasmic. {ECO:0000250|UniProtKB:P51686}.; TOPO_DOM 186 208 Extracellular. {ECO:0000250|UniProtKB:P51686}.; TOPO_DOM 244 248 Cytoplasmic. {ECO:0000250|UniProtKB:P51686}.; TOPO_DOM 284 290 Extracellular. {ECO:0000250|UniProtKB:P51686}.; TOPO_DOM 322 369 Cytoplasmic. {ECO:0000250|UniProtKB:P51686}. FUNCTION: Receptor for chemokine SCYA25/TECK. Subsequently transduces a signal by increasing the intracellular calcium ions level. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P51686}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P51686}. TISSUE SPECIFICITY: Highly expressed in the thymus and low in lymph nodes and spleen. +Q3UHI0 CCSE2_MOUSE Serine-rich coiled-coil domain-containing protein 2 (Coiled-coil serine-rich protein 2) (Granule cell antiserum positive protein 14) (Protein GCAP14) 833 92,932 Alternative sequence (1); Chain (1); Coiled coil (1); Compositional bias (1); Erroneous initiation (1); Modified residue (3); Sequence conflict (15) FUNCTION: Microtubule-binding protein which might play a role in microtubule bundling. {ECO:0000269|PubMed:22673506}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:22673506}. Note=Associates with microtubules in interphase. Has diffuse expression throughout the cell during mitosis. {ECO:0000269|PubMed:22673506}. TISSUE SPECIFICITY: Expressed in brain (at protein level). {ECO:0000269|PubMed:22673506}. +Q9DAF8 CD051_MOUSE Uncharacterized protein C4orf51 homolog 208 23,497 Chain (1); Sequence conflict (1) +Q99M08 CD003_MOUSE Uncharacterized protein C4orf3 homolog 65 7,404 Chain (1); Modified residue (2); Sequence conflict (2); Transmembrane (1) TRANSMEM 44 64 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q99K99 CD019_MOUSE Uncharacterized protein C4orf19 homolog 313 33,916 Chain (1); Modified residue (6); Sequence conflict (6) +Q8BGN2 CD033_MOUSE UPF0462 protein C4orf33 homolog 192 22,460 Alternative sequence (1); Chain (1); Sequence conflict (2) +P24161 CD3Z_MOUSE T-cell surface glycoprotein CD3 zeta chain (T-cell receptor T3 zeta chain) (CD antigen CD247) 164 18,637 Alternative sequence (1); Chain (1); Domain (3); Modified residue (8); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 31 51 Helical. {ECO:0000255}. TOPO_DOM 22 30 Extracellular. {ECO:0000255}.; TOPO_DOM 52 164 Cytoplasmic. {ECO:0000255}. FUNCTION: Part of the TCR-CD3 complex present on T-lymphocyte cell surface that plays an essential role in adaptive immune response. When antigen presenting cells (APCs) activate T-cell receptor (TCR), TCR-mediated signals are transmitted across the cell membrane by the CD3 chains CD3D, CD3E, CD3G and CD3Z. All CD3 chains contain immunoreceptor tyrosine-based activation motifs (ITAMs) in their cytoplasmic domain. Upon TCR engagement, these motifs become phosphorylated by Src family protein tyrosine kinases LCK and FYN, resulting in the activation of downstream signaling pathways. CD3Z ITAMs phosphorylation creates multiple docking sites for the protein kinase ZAP70 leading to ZAP70 phosphorylation and its conversion into a catalytically active enzyme. Plays an important role in intrathymic T-cell differentiation. Additionally, participates in the activity-dependent synapse formation of retinal ganglion cells (RGCs) in both the retina and dorsal lateral geniculate nucleus (dLGN). {ECO:0000250|UniProtKB:P20963, ECO:0000269|PubMed:20188655, ECO:0000269|PubMed:8223495}. PTM: Phosphorylated on Tyr residues after T-cell receptor triggering by LCK in association with CD4/CD8. {ECO:0000250|UniProtKB:P20963}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: The TCR-CD3 complex is composed of a CD3D/CD3E and a CD3G/CD3E heterodimers that preferentially associate with TCRalpha and TCRbeta, respectively, to form TCRalpha/CD3E/CD3G and TCRbeta/CD3G/CD3E trimers. In turn, the hexamer interacts with CD3Z homodimer to form the TCR-CD3 complex. Alternatively, TCRalpha and TCRbeta can be replaced by TCRgamma and TCRdelta. Interacts with SLA (PubMed:10662792). Interacts with SLA2 (PubMed:11891219). Interacts with TRAT1. Interacts with DOCK2. Interacts with SHB. Interacts with ZAP70. Interacts (tyrosine phosphorylated) with SHC1 (via SH2 domain). Interacts with PTPRC (By similarity). Interacts with CRK; this interaction regulates CD3Z phosphorylation (By similarity). Interacts with CD160. {ECO:0000250|UniProtKB:P20963, ECO:0000269|PubMed:10662792, ECO:0000269|PubMed:11891219}. DOMAIN: The ITAM domains mediate interaction with SHB. {ECO:0000250}. TISSUE SPECIFICITY: CD3Z is expressed in normal lymphoid tissue and in peripheral blood mononuclear cells (PBMCs). Expressed also in retinal ganglion cells (PubMed:20188655). {ECO:0000269|PubMed:20188655, ECO:0000305}. +P11609 CD1D1_MOUSE Antigen-presenting glycoprotein CD1d1 (CD antigen CD1d.1) 336 38,554 Beta strand (18); Binding site (1); Chain (1); Disulfide bond (2); Domain (1); Glycosylation (5); Helix (7); Motif (1); Region (1); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (4) TRANSMEM 306 326 Helical. {ECO:0000255}. TOPO_DOM 22 305 Extracellular. {ECO:0000255}.; TOPO_DOM 327 336 Cytoplasmic. {ECO:0000255}. FUNCTION: Antigen-presenting protein that binds self and non-self glycolipids and presents them to T-cell receptors on natural killer T-cells. {ECO:0000269|PubMed:11754812, ECO:0000269|PubMed:16007091, ECO:0000269|PubMed:16314439}. PTM: N-glycosylated. {ECO:0000269|PubMed:11754812, ECO:0000269|PubMed:16002697, ECO:0000269|PubMed:16007091, ECO:0000269|PubMed:16314439, ECO:0000269|PubMed:16537470}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11754812}; Single-pass type I membrane protein {ECO:0000269|PubMed:11754812}. Endosome membrane {ECO:0000269|PubMed:11754812}. Lysosome membrane {ECO:0000269|PubMed:11754812}. Note=Subject to intracellular trafficking between the cell membrane, endosomes and lysosomes. {ECO:0000269|PubMed:11754812}. SUBUNIT: Heterodimer with B2M (beta-2-microglobulin). Interacts with MHC II and CD74. {ECO:0000269|PubMed:11754812, ECO:0000269|PubMed:16002697, ECO:0000269|PubMed:16007091, ECO:0000269|PubMed:16314439, ECO:0000269|PubMed:16537470, ECO:0000269|PubMed:9219685}. TISSUE SPECIFICITY: Expressed on cortical thymocytes, on certain T-cell leukemias, and in various other tissues. +Q5U462 CDCP1_MOUSE CUB domain-containing protein 1 (Membrane glycoprotein gp140) (Transmembrane and associated with src kinases) (CD antigen CD318) 833 92,726 Chain (1); Disulfide bond (1); Domain (1); Glycosylation (7); Modified residue (1); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 667 687 Helical. {ECO:0000255}. TOPO_DOM 30 666 Extracellular. {ECO:0000255}.; TOPO_DOM 688 833 Cytoplasmic. {ECO:0000255}. FUNCTION: May be involved in cell adhesion and cell matrix association. May play a role in the regulation of anchorage versus migration or proliferation versus differentiation via its phosphorylation. May be a novel marker for leukemia diagnosis and for immature hematopoietic stem cell subsets. Belongs to the tetraspanin web involved in tumor progression and metastasis. PTM: Phosphorylated on tyrosine by kinases of the SRC family such as SRC and YES as well as by the protein kinase C gamma/PRKCG. Dephosphorylated by phosphotyrosine phosphatases. Also phosphorylated by suramin, a heparin analog. Tyrosine phosphorylated in response to dissociation of integrin alpha-6 beta-4 from laminin-5 (By similarity). {ECO:0000250}.; PTM: N-glycosylated. {ECO:0000250}.; PTM: A soluble form may also be produced by proteolytic cleavage at the cell surface (shedding). Another peptide of 80 kDa (p80) is present in cultured keratinocytes probably due to tryptic cleavage at an unidentified site on the N-terminal side. Converted to p80 by plasmin, a trypsin-like protease (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Note=Its shedding may lead to a soluble peptide. {ECO:0000250}. SUBUNIT: Interacts with CDH2/N-cadherin, CDH3/P-cadherin, SDC1/syndecan-1, SDC4/syndecan-4 and the serine protease ST14/MT-SP1. Also interacts SRC and PRKCG/protein kinase C gamma (By similarity). {ECO:0000250}. +Q6A068 CDC5L_MOUSE Cell division cycle 5-like protein (Cdc5-like protein) 802 92,190 Chain (1); Coiled coil (3); Cross-link (3); DNA binding (2); Domain (2); Erroneous initiation (1); Modified residue (14); Motif (1); Region (4) FUNCTION: DNA-binding protein involved in cell cycle control. May act as a transcription activator. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. The PRP19-CDC5L complex may also play a role in the response to DNA damage (DDR). {ECO:0000250|UniProtKB:Q99459}. PTM: Phosphorylated on serine and threonine residues. Phosphorylation on Thr-411 and Thr-438 is required for CDC5L-mediated mRNA splicing. Has no effect on subcellular location nor on homodimerization. Phosphorylated in vitro by CDK2. Phosphorylation enhances interaction with PPP1R8. {ECO:0000250|UniProtKB:Q99459}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:10570151}. Nucleus speckle {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:10570151}. Cytoplasm {ECO:0000269|PubMed:10570151}. Note=May shuttle between cytoplasm and nucleus. {ECO:0000269|PubMed:10570151}. SUBUNIT: Homodimer. Interacts with DAPK3. Belongs to the spliceosome complex. Part of a spliceosomal 'core' complex consisting of CDC5L, PLRG1, SPF27, CCAP1, CCAP3 and CCAP6. Interacts with PLRG1, Lodestar/TTF2, and NIPP1/PPP1R8. Identified in the spliceosome C complex. Component of the PRP19-CDC5L splicing complex composed of a core complex comprising a homotetramer of PRPF19, CDC5L, PLRG1 and BCAS2, and at least three less stably associated proteins CTNNBL1, CWC15 and HSPA8. Interacts (via its C-terminus) directly in the complex with PRPF19 and BCAS2. Interacts (via its C-terminus) directly with PRGL1 (via its WD40 repeat domain); the interaction is required for mRNA splicing but not for spliceosome assembly. Also interacts with CTNNBL1. {ECO:0000250|UniProtKB:O08837, ECO:0000250|UniProtKB:Q99459}. +P22646 CD3E_MOUSE T-cell surface glycoprotein CD3 epsilon chain (T-cell surface antigen T3/Leu-4 epsilon chain) (CD antigen CD3e) 189 21,393 Beta strand (7); Chain (1); Disulfide bond (1); Domain (2); Helix (4); Modified residue (2); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (3) TRANSMEM 109 134 Helical. {ECO:0000255}. TOPO_DOM 23 108 Extracellular. {ECO:0000255}.; TOPO_DOM 135 189 Cytoplasmic. {ECO:0000255}. FUNCTION: Part of the TCR-CD3 complex present on T-lymphocyte cell surface that plays an essential role in adaptive immune response. When antigen presenting cells (APCs) activate T-cell receptor (TCR), TCR-mediated signals are transmitted across the cell membrane by the CD3 chains CD3D, CD3E, CD3G and CD3Z. All CD3 chains contain immunoreceptor tyrosine-based activation motifs (ITAMs) in their cytoplasmic domain. Upon TCR engagement, these motifs become phosphorylated by Src family protein tyrosine kinases LCK and FYN, resulting in the activation of downstream signaling pathways. In addition of this role of signal transduction in T-cell activation, CD3E plays an essential role in correct T-cell development (PubMed:19956738, PubMed:24899501). Participates also in internalization and cell surface down-regulation of TCR-CD3 complexes via endocytosis sequences present in CD3E cytosolic region. {ECO:0000250|UniProtKB:P07766, ECO:0000269|PubMed:19956738, ECO:0000269|PubMed:24470497, ECO:0000269|PubMed:24899501, ECO:0000269|PubMed:9843989}. PTM: Phosphorylated on Tyr residues after T-cell receptor triggering by LCK in association with CD4/CD8. {ECO:0000250|UniProtKB:P07766}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24470497}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P07766}. SUBUNIT: The TCR-CD3 complex is composed of a CD3D/CD3E and a CD3G/CD3E heterodimers that preferentially associate with TCRalpha and TCRbeta, respectively, to form TCRalpha/CD3E/CD3G and TCRbeta/CD3G/CD3E trimers. In turn, the hexamer interacts with CD3Z homodimer to form the TCR-CD3 complex. Alternatively, TCRalpha and TCRbeta can be replaced by TCRgamma and TCRdelta. Interacts with CD6. Interacts with NCK1 (PubMed:24470497). {ECO:0000250|UniProtKB:P07766, ECO:0000269|PubMed:24470497}. +Q8VCN6 CD99_MOUSE CD99 antigen (Paired immunoglobin-like type 2 receptor-ligand) (PILR-L) (CD antigen CD99) 175 16,783 Chain (1); Sequence conflict (8); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 138 158 Helical. {ECO:0000255}. TOPO_DOM 29 137 Extracellular. {ECO:0000255}.; TOPO_DOM 159 175 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in T-cell adhesion processes. Plays a role in a late step of leukocyte extravasation helping leukocytes to overcome the endothelial basement membrane. Acts at the same site as, but independently of, PECAM1. {ECO:0000269|PubMed:15280198, ECO:0000269|PubMed:20479283}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Homodimer. Interacts with PILRB. {ECO:0000269|PubMed:14970179, ECO:0000269|PubMed:15978751}. TISSUE SPECIFICITY: Widely expressed with high levels in lung, spleen, thymus, liver and spinal chord. Expressed on leukocytes and endothelial cell contacts. Detected in a wide range of T-cells, including CD4-/CD8- and CD4+/CD8+ thymocytes. Expression is much lower in peripheral T-cells than in thymocytes. {ECO:0000269|PubMed:14970179, ECO:0000269|PubMed:15280198}. +Q80YP0 CDK3_MOUSE Cyclin-dependent kinase 3 (EC 2.7.11.22) (Cell division protein kinase 3) 303 33,888 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Domain (1); Natural variant (1); Nucleotide binding (1) FUNCTION: Serine/threonine-protein kinase that plays a critical role in the control of the eukaryotic cell cycle; involved in G0-G1 and G1-S cell cycle transitions. Interacts with CCNC/cyclin-C during interphase. Phosphorylates histone H1, ATF1, RB1 and CABLES1. ATF1 phosphorylation triggers ATF1 transactivation and transcriptional activities, and promotes cell proliferation and transformation. CDK3/cyclin-C mediated RB1 phosphorylation is required for G0-G1 transition. Promotes G1-S transition probably by contributing to the activation of E2F1, E2F2 and E2F3 in a RB1-independent manner. {ECO:0000269|PubMed:11733001}. SUBUNIT: Interacts with CABLES1 and ATF1. Binding to CCNC/cyclin-C promotes RB1 phosphorylation (By similarity). Binds to CABLES2. {ECO:0000250, ECO:0000269|PubMed:11955625}. +P39038 CADH4_MOUSE Cadherin-4 (Retinal cadherin) (R-CAD) (R-cadherin) 913 100,030 Chain (1); Compositional bias (1); Domain (5); Glycosylation (7); Propeptide (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 732 753 Helical. {ECO:0000255}. TOPO_DOM 167 731 Extracellular. {ECO:0000255}.; TOPO_DOM 754 913 Cytoplasmic. {ECO:0000255}. FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. May play an important role in retinal development. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. DOMAIN: Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain. {ECO:0000250}. TISSUE SPECIFICITY: Distributed widely in mouse tissues with high levels present in brain, skeletal muscle and thymus. +P70160 CALC_MOUSE Calcitonin 136 15,141 Disulfide bond (1); Glycosylation (1); Modified residue (2); Peptide (1); Propeptide (2); Sequence conflict (1); Signal peptide (1) FUNCTION: Causes a rapid but short-lived drop in the level of calcium and phosphate in blood by promoting the incorporation of those ions in the bones. SUBCELLULAR LOCATION: Secreted. +Q9D6P8 CALL3_MOUSE Calmodulin-like protein 3 149 16,701 Calcium binding (4); Chain (1); Domain (4); Sequence conflict (1) FUNCTION: May function as a specific light chain of unconventional myosin-10 (MYO10), also enhances MYO10 translation, possibly by acting as a chaperone for the emerging MYO10 heavy chain protein. May compete with calmodulin by binding, with different affinities, to cellular substrates (By similarity). {ECO:0000250}. SUBUNIT: Interacts with MYO10, the interaction is calcium-dependent and essential for MYO10 function in filopodial extension. {ECO:0000250}. +P35564 CALX_MOUSE Calnexin 591 67,278 Binding site (4); Chain (1); Disulfide bond (2); Lipidation (2); Metal binding (3); Modified residue (5); Region (5); Repeat (8); Sequence conflict (5); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 483 503 Helical. {ECO:0000255}. TOPO_DOM 21 482 Lumenal. {ECO:0000255}.; TOPO_DOM 504 591 Cytoplasmic. {ECO:0000255}. FUNCTION: Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins. Associated with partial T-cell antigen receptor complexes that escape the ER of immature thymocytes, it may function as a signaling complex regulating thymocyte maturation. Additionally it may play a role in receptor-mediated endocytosis at the synapse. {ECO:0000269|PubMed:21747946, ECO:0000269|PubMed:7628443}. PTM: Phosphorylated at Ser-563 by MAPK3/ERK1. phosphorylation by MAPK3/ERK1 increases its association with ribosomes (By similarity). {ECO:0000250}.; PTM: Palmitoylation by DHHC6 leads to the preferential localization to the perinuclear rough ER. It mediates the association of calnexin with the ribosome-translocon complex (RTC) which is required for efficient folding of glycosylated proteins (By similarity). {ECO:0000250}.; PTM: Ubiquitinated, leading to proteasomal degradation. Probably ubiquitinated by ZNRF4. {ECO:0000250|UniProtKB:P27824}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:7628443}; Single-pass type I membrane protein {ECO:0000255}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P27824}. Melanosome {ECO:0000250|UniProtKB:P27824}. Note=The palmitoylated form preferentially localizes to the perinuclear rough ER (By similarity). When bound to CD3 epsilon chains, calnexin's ER retention signal can be masked, permitting it to escape ER retention. {ECO:0000250|UniProtKB:P27824}. SUBUNIT: Interacts with MAPK3/ERK1 (By similarity). Interacts with KCNH2 (By similarity). Associates with ribosomes (By similarity). The palmitoylated form interacts with the ribosome-translocon complex component SSR1, promoting efficient folding of glycoproteins (By similarity). Interacts with SERPINA2P/SERPINA2 and with the S and Z variants of SERPINA1 (By similarity). Interacts with SGIP1; involved in negative regulation of endocytosis (PubMed:21747946). Interacts with PPIB (By similarity). {ECO:0000250|UniProtKB:P27824, ECO:0000250|UniProtKB:P35565, ECO:0000269|PubMed:21747946}. +Q8VCF1 CANT1_MOUSE Soluble calcium-activated nucleotidase 1 (SCAN-1) (EC 3.6.1.6) (Apyrase homolog) 403 45,653 Alternative sequence (3); Chain (1); Frameshift (2); Glycosylation (1); Metal binding (6); Sequence conflict (2); Site (4); Topological domain (2); Transmembrane (1) TRANSMEM 45 61 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 44 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 62 403 Lumenal. {ECO:0000255}. FUNCTION: Calcium-dependent nucleotidase with a preference for UDP. The order of activity with different substrates is UDP > GDP > IDP >> UTP > CDP = GTP = ITP. Has very low activity towards ADP and even lower activity towards ATP. Does not hydrolyze AMP and GMP. Involved in proteoglycan synthesis. {ECO:0000250|UniProtKB:Q8WVQ1}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8K4Y7}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q8K4Y7}. Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:Q8K4Y7}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q8K4Y7}. Note=Processed form: Secreted. {ECO:0000250}. SUBUNIT: Monomer. Homodimer; dimerization is Ca(2+)-dependent. {ECO:0000250|UniProtKB:Q8WVQ1}. +Q9D3A8 CAPON_MOUSE Carboxyl-terminal PDZ ligand of neuronal nitric oxide synthase protein (C-terminal PDZ ligand of neuronal nitric oxide synthase protein) (Nitric oxide synthase 1 adaptor protein) 503 55,873 Alternative sequence (2); Chain (1); Coiled coil (1); Compositional bias (2); Domain (1); Modified residue (8); Motif (1); Region (1); Sequence conflict (5) FUNCTION: Adapter protein involved in neuronal nitric-oxide (NO) synthesis regulation via its association with nNOS/NOS1. The complex formed with NOS1 and synapsins is necessary for specific NO and synapsin functions at a presynaptic level. Mediates an indirect interaction between NOS1 and RASD1 leading to enhance the ability of NOS1 to activate RASD1. Competes with DLG4 for interaction with NOS1, possibly affecting NOS1 activity by regulating the interaction between NOS1 and DLG4 (By similarity). {ECO:0000250}. SUBUNIT: Interacts with the PDZ domain of NOS1 or the second PDZ domain of DLG4 through its C-terminus. Interacts with RASD1 and SYN1, SYN2 and SYN3 via its PID domain. Forms a ternary complex with NOS1 and SYN1 (By similarity). Forms a ternary complex with NOS1 and RASD1. {ECO:0000250, ECO:0000269|PubMed:11086993}. +O08688 CAN5_MOUSE Calpain-5 (EC 3.4.22.-) (New calpain 3) (nCL-3) 640 72,955 Active site (3); Chain (1); Domain (2); Natural variant (1); Region (1) FUNCTION: Calcium-regulated non-lysosomal thiol-protease. {ECO:0000250}. +P97821 CATC_MOUSE Dipeptidyl peptidase 1 (EC 3.4.14.1) (Cathepsin C) (Cathepsin J) (Dipeptidyl peptidase I) (DPP-I) (DPPI) (Dipeptidyl transferase) [Cleaved into: Dipeptidyl peptidase 1 exclusion domain chain (Dipeptidyl peptidase I exclusion domain chain); Dipeptidyl peptidase 1 heavy chain (Dipeptidyl peptidase I heavy chain); Dipeptidyl peptidase 1 light chain (Dipeptidyl peptidase I light chain)] 462 52,376 Active site (3); Binding site (3); Chain (3); Disulfide bond (5); Glycosylation (3); Propeptide (1); Signal peptide (1) FUNCTION: Thiol protease. Has dipeptidylpeptidase activity. Can act as both an exopeptidase and endopeptidase. Can degrade glucagon. Plays a role in the generation of cytotoxic lymphocyte effector function. SUBCELLULAR LOCATION: Lysosome. SUBUNIT: Tetramer of heterotrimers consisting of exclusion domain, heavy- and light chains. {ECO:0000250}. TISSUE SPECIFICITY: Broadly distributed, but higher levels found in lung, liver, kidney and spleen. Lower levels found in testis and brain. +Q8C3Q9 CASP9_MOUSE Caspase-9 (CASP-9) (EC 3.4.22.62) (Apoptotic protease Mch-6) (Apoptotic protease-activating factor 3) (APAF-3) (ICE-like apoptotic protease 6) (ICE-LAP6) [Cleaved into: Caspase-9 subunit p35; Caspase-9 subunit p10] 454 49,979 Active site (2); Chain (2); Domain (1); Modified residue (4); Propeptide (2) FUNCTION: Involved in the activation cascade of caspases responsible for apoptosis execution. Binding of caspase-9 to Apaf-1 leads to activation of the protease which then cleaves and activates caspase-3. Promotes DNA damage-induced apoptosis in a ABL1/c-Abl-dependent manner. Proteolytically cleaves poly(ADP-ribose) polymerase (PARP) (By similarity). {ECO:0000250}. PTM: Cleavages at Asp-353 by granzyme B and at Asp-368 by caspase-3 generate the two active subunits. Caspase-8 and -10 can also be involved in these processing events (By similarity). {ECO:0000250}.; PTM: Phosphorylated at Thr-163 by MAPK1/ERK2. Phosphorylation at Thr-163 is sufficient to block caspase-9 processing and subsequent caspase-3 activation (By similarity). Phosphorylation on Tyr-191 by ABL1/c-Abl; occurs in the response of cells to DNA damage. {ECO:0000250, ECO:0000269|PubMed:15657060}. SUBUNIT: Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a 35 kDa (p35) and a 10 kDa (p10) subunit. Caspase-9 and APAF1 bind to each other via their respective NH2-terminal CED-3 homologous domains in the presence of cytochrome C and ATP. Interacts (inactive form) with EFHD2. Interacts with HAX1. Interacts with BIRC2/c-IAP1, XIAP/BIRC4, BIRC5/survivin, BIRC6/bruce and BIRC7/livin. Interacts with ABL1 (via SH3 domain); the interaction is direct and increased in the response of cells to genotoxic stress and ABL1/c-Abl activation (By similarity). {ECO:0000250}. +P18242 CATD_MOUSE Cathepsin D (EC 3.4.23.5) 410 44,954 Active site (2); Chain (1); Disulfide bond (4); Domain (1); Glycosylation (2); Propeptide (1); Signal peptide (1) FUNCTION: Acid protease active in intracellular protein breakdown. Plays a role in APP processing following cleavage and activation by ADAM30 which leads to APP degradation. {ECO:0000250|UniProtKB:P07339}. PTM: N- and O-glycosylated. {ECO:0000250|UniProtKB:P07339, ECO:0000269|PubMed:16170054}.; PTM: Undergoes proteolytic cleavage and activation by ADAM30. {ECO:0000250|UniProtKB:P07339}. SUBCELLULAR LOCATION: Lysosome. Melanosome {ECO:0000250}. Secreted, extracellular space {ECO:0000250}. SUBUNIT: Consists of a light chain and a heavy chain. Interacts with ADAM30; this leads to activation of CTSD. {ECO:0000250|UniProtKB:P07339}. +P70190 CAZA3_MOUSE F-actin-capping protein subunit alpha-3 (CapZ alpha-3) (Germ cell-specific protein 3) 299 34,952 Chain (1); Modified residue (2); Sequence conflict (2) FUNCTION: F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. May play a role in the morphogenesis of spermatid. SUBUNIT: Heterodimer of an alpha and a beta subunit. Component of the WASH complex, composed of F-actin-capping protein subunit alpha (CAPZA1, CAPZA2 or CAPZA3), F-actin-capping protein subunit beta (CAPZB), WASHC1, WASHC2, WASHC3, WASHC4 and WASHC5 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Exclusively expressed in the testis. +Q9CWQ8 CAST1_MOUSE Cytosolic arginine sensor for mTORC1 subunit 1 (GATS-like protein 3) 331 36,575 Binding site (1); Chain (1); Domain (2); Region (3) FUNCTION: Functions as an intracellular arginine sensor within the amino acid-sensing branch of the TORC1 signaling pathway. As a homodimer or a heterodimer with CASTOR2, binds and inhibits the GATOR subcomplex GATOR2 and thereby mTORC1. Binding of arginine to CASTOR1 allosterically disrupts the interaction of CASTOR1-containing dimers with GATOR2 which can in turn activate mTORC1 and the TORC1 signaling pathway. {ECO:0000250|UniProtKB:Q8WTX7}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8WTX7}. SUBUNIT: Forms homodimers and heterodimers with CASTOR2. Interacts with the GATOR2 complex which is composed of MIOS, SEC13, SEH1L, WDR24 and WDR59; the interaction is negatively regulated by arginine. {ECO:0000250|UniProtKB:Q8WTX7}. DOMAIN: Based on x-ray crystallography data, the protein would be constituted of 4 tandem ACT domains instead of the 2 predicted from the sequence. {ECO:0000250|UniProtKB:Q8WTX7}. +Q8CAB8 CAST2_MOUSE Cytosolic arginine sensor for mTORC1 subunit 2 (GATS-like protein 2) 329 36,112 Chain (1); Domain (2); Sequence conflict (5) FUNCTION: Functions as a negative regulator of the TORC1 signaling pathway through the GATOR complex. As part of homodimers or heterodimers with CASTOR1, directly binds and inhibits the GATOR subcomplex GATOR2 and thereby mTORC1. Does not directly bind arginine, but binding of arginine to CASTOR1 disrupts the interaction of CASTOR2-containing heterodimers with GATOR2 which can in turn activate mTORC1 and the TORC1 signaling pathway. {ECO:0000250|UniProtKB:A6NHX0}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:A6NHX0}. SUBUNIT: Forms homodimers and heterodimers with CASTOR1. Interacts with the GATOR2 complex which is composed of MIOS, SEC13, SEH1L, WDR24 and WDR59; the interaction is not regulated by arginine. {ECO:0000250|UniProtKB:A6NHX0}. +Q8CDK2 CBPC2_MOUSE Cytosolic carboxypeptidase 2 (EC 3.4.17.-) (ATP/GTP-binding protein-like 2) 862 99,216 Active site (1); Alternative sequence (8); Chain (1); Erroneous gene model prediction (1); Erroneous initiation (6); Metal binding (3); Mutagenesis (1); Sequence conflict (4) FUNCTION: Metallocarboxypeptidase that mediates deglutamylation of target proteins. Catalyzes the deglutamylation of polyglutamate side chains generated by post-translational polyglutamylation in proteins such as tubulins. Also removes gene-encoded polyglutamates from the carboxy-terminus of target proteins such as MYLK. Does not show detyrosinase or deglycylase activities from the carboxy-terminus of tubulin. {ECO:0000269|PubMed:25103237}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:17244818}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q5U5Z8}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q5U5Z8}. Note=Colocalizes with gamma-tubulin in the centrioles and with glutamylated tubulin in the basal bodies of ciliated cells. {ECO:0000250|UniProtKB:Q5U5Z8}. TISSUE SPECIFICITY: Widely expressed. Expressed in tissues with motile cilia such as testis, lung and trachea. Also detected in brain, eye, muscle, pancreas, intestine, stomach, pituitary, spleen, adrenal and kidney. Expressed in mitral and granular cells in brain. {ECO:0000269|PubMed:17244818, ECO:0000269|PubMed:25103237}. +Q9R171 CBLN1_MOUSE Cerebellin-1 (Brain protein D3) (Precerebellin) [Cleaved into: Cerebellin (CER); [des-Ser1]-cerebellin (des-Ser1-cerebellin)] 193 21,113 Chain (1); Disulfide bond (2); Domain (1); Erroneous translation (1); Glycosylation (2); Mutagenesis (6); Peptide (2); Region (3); Sequence conflict (1); Signal peptide (1) FUNCTION: Required for synapse integrity and synaptic plasticity. During cerebellar synapse formation, essential for the matching and maintenance of pre- and post-synaptic elements at parallel fiber-Purkinje cell synapses, the establishment of the proper pattern of climbing fiber-Purkinje cell innervation, and induction of long-term depression at parallel fiber-Purkinje cell synapses (PubMed:16234806). Plays a role as a synaptic organizer that acts bidirectionally on both pre- and post-synaptic components (PubMed:20395510). On the one hand induces accumulation of synaptic vesicles in the pre-synaptic part by binding with NRXN1 and in other hand induces clustering of GRID2 and its associated proteins at the post-synaptic site through association of GRID2 (PubMed:21410790). NRXN1-CBLN1-GRID2 complex directly induces parallel fiber protrusions that encapsulate spines of Purkinje cells leading to accumulation of GRID2 and synaptic vesicles (PubMed:23141067). Required for CBLN3 export from the endoplasmic reticulum and secretion (PubMed:17030622, PubMed:17331201). NRXN1-CBLN1-GRID2 complex mediates the D-Serine-dependent long term depression signals and AMPA receptor endocytosis (By similarity). {ECO:0000250|UniProtKB:P23435, ECO:0000269|PubMed:16234806, ECO:0000269|PubMed:17030622, ECO:0000269|PubMed:17331201, ECO:0000269|PubMed:20395510, ECO:0000269|PubMed:21410790, ECO:0000269|PubMed:23141067}.; FUNCTION: The cerebellin peptide exerts neuromodulatory functions. Directly stimulates norepinephrine release via the adenylate cyclase/PKA-dependent signaling pathway; and indirectly enhances adrenocortical secretion in vivo, through a paracrine mechanism involving medullary catecholamine release (By similarity). {ECO:0000250|UniProtKB:P63182}. PTM: The proteolytic processing to yield cerebellin seems to occur either prior to the secretion by presynaptic neurons and subsequent oligomerization or in some other location after release of the mature protein. In the cerebellum, cerebellin is much more abundant than [des-Ser1]-cerebellin. SUBCELLULAR LOCATION: Secreted. Cell junction, synapse, postsynaptic cell membrane. Note=Interaction with CBLN3 may cause partial retention in the endoplasmic reticulum. SUBUNIT: Homohexamer; disulfide-linked homotrimers. The trimers are assembled via the globular C1q domains. The trimers associate via N-terminal cysteine residues to form disulfide-linked hexamers (PubMed:16135095). May form oligomers with CBLN2, CBLN3 AND CBLN4 prior to secretion. Once secreted, does not interact with other CBLN family members (PubMed:17030622, PubMed:17331201, PubMed:10964938). Interacts with GRID1 (PubMed:20395510, PubMed:22220752). Interacts with NRXN1 and NRXN2 long (alpha) and short (beta) isoforms produced by alternative promoter usage. Competes with NLGN1 for NRXN1-binding. Weakly interacts with NRXN3 short isoform and not at all with NRXN3 long isoform (PubMed:21410790, PubMed:22220752). Interacts (via C1q domain) with GRID2; GRID2-binding is calcium-independent; CBLN1 hexamers anchor GRID2 N-terminal domain dimers to monomeric NRXN1 isoform beta; promotes synaptogenesis and mediates the D-Serine-dependent long term depression signals and AMPA receptor endocytosis (PubMed:20395510, PubMed:22220752). Interacts with OTOL1 (PubMed:20856818). {ECO:0000269|PubMed:10964938, ECO:0000269|PubMed:16135095, ECO:0000269|PubMed:17030622, ECO:0000269|PubMed:17331201, ECO:0000269|PubMed:20395510, ECO:0000269|PubMed:20856818, ECO:0000269|PubMed:21410790, ECO:0000269|PubMed:22220752}. TISSUE SPECIFICITY: Expressed and secreted by presynaptic neurons, such as cerebellar granule cells. Following secretion, the protein binds to GRID2 on the postsynaptic Purkinje cell membranes. Expressed at the highest level in the cerebellar cortex. High levels are also seen in the olfactory bulb, posterior part of the cerebral cortex, certain thalamic nuclei, and deep cerebellar nuclei. Low to moderate levels are detected in some hypothalamic and brainstem nuclei. In the thalamus, expressed in parafascicular nucleus neurons and other regions (at protein level). {ECO:0000269|PubMed:16930405, ECO:0000269|PubMed:17030622, ECO:0000269|PubMed:22220752, ECO:0000269|PubMed:23141067, ECO:0000269|PubMed:3199194, ECO:0000269|PubMed:3420533}. +Q8BGU2 CBLN2_MOUSE Cerebellin-2 224 24,051 Chain (1); Domain (1); Glycosylation (2); Mutagenesis (2); Signal peptide (1) FUNCTION: May play role in synaptogenesis induction. {ECO:0000269|PubMed:21410790}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17030622, ECO:0000269|PubMed:17331201}. SUBUNIT: May form homooligomers or heterooligomers with CBLN1 and CBLN3 prior to secretion. Once secreted, does not interact with other CBLN family members. Interacts with GRID2, and more weakly with GRID1. Interacts with NRXN1 and NRXN2 long and short isoforms produced by alternative promoter usage. Weakly interacts with NRXN3 short isoform and not at all with NRXN3 long isoform. {ECO:0000269|PubMed:17030622, ECO:0000269|PubMed:21410790, ECO:0000269|PubMed:22220752}. TISSUE SPECIFICITY: Expressed in various brain regions with higher levels in the olfactory bulb, cerebral cortex, certain thalamic and hypothalamic nuclei, superior and inferior colliculi and some brainstem nuclei. {ECO:0000269|PubMed:16930405}. +P45481 CBP_MOUSE CREB-binding protein (EC 2.3.1.48) 2441 265,494 Beta strand (16); Binding site (3); Chain (1); Compositional bias (7); Cross-link (3); Domain (3); Helix (37); Initiator methionine (1); Metal binding (12); Modified residue (24); Mutagenesis (10); Region (6); Sequence conflict (16); Turn (9); Zinc finger (3) FUNCTION: Acetylates histones, giving a specific tag for transcriptional activation. Also acetylates non-histone proteins, like NCOA3 and FOXO1. Binds specifically to phosphorylated CREB and enhances its transcriptional activity toward cAMP-responsive genes. Acts as a coactivator of ALX1. Acts as a circadian transcriptional coactivator which enhances the activity of the circadian transcriptional activators: NPAS2-ARNTL/BMAL1 and CLOCK-ARNTL/BMAL1 heterodimers. Acetylates PCNA; acetylation promotes removal of chromatin-bound PCNA and its degradation during nucleotide excision repair (NER). Functions as a transcriptional coactivator for SMAD4 in the TGF-beta signaling pathway (By similarity). {ECO:0000250|UniProtKB:Q92793, ECO:0000269|PubMed:10207073, ECO:0000269|PubMed:11701890, ECO:0000269|PubMed:15220471, ECO:0000269|PubMed:16287980}. PTM: Methylation of the KIX domain by CARM1 blocks association with CREB. This results in the blockade of CREB signaling, and in activation of apoptotic response. {ECO:0000269|PubMed:11701890}.; PTM: Phosphorylated by CHUK/IKKA at Ser-1383 and Ser-1387; these phosphorylations promote cell growth by switching the binding preference of CREBBP from TP53 to NF-kappa-B. {ECO:0000250}.; PTM: Sumoylation negatively regulates transcriptional activity via the recruitment of DAAX. {ECO:0000269|PubMed:16287980}.; PTM: Autoacetylation is required for binding to protein substrates, such as acetylated histones and acetylated TP53/p53. {ECO:0000250|UniProtKB:Q92793}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q92793}. Nucleus. Note=Recruited to nuclear bodies by SS18L1/CREST. In the presence of ALX1 relocalizes from the cytoplasm to the nucleus. {ECO:0000250|UniProtKB:Q92793}. SUBUNIT: Interacts with DHX9 (via N-terminus); this interaction mediates association with RNA polymerase II holoenzyme and stimulates CREB-dependent transcriptional activation (By similarity). Interacts (via transactivation domain and C-terminus) with PCNA; the interaction occurs on chromatin in UV-irradiated damaged cells (By similarity). Found in a complex containing NCOA2; NCOA3; IKKA; IKKB and IKBKG. Probably part of a complex with HIF1A and EP300. The TAZ-type 1 domain interacts with HIF1A. Interacts with SRCAP, ELF3, MLLT7/FOXO4, N4BP2, NCOA6, PCAF, PELP1, PML, SMAD1, SMAD2, SMAD3, SPIB and TRERF1. Interacts with KLF1; the interaction results in acetylation and enhancement of transcriptional activity of KLF1. Interacts with MAFG; the interaction acetylates MAFG in the basic region and stimulates NFE2 transcriptional activity through increasing its DNA-binding activity. Interacts with IRF2; the interaction acetylates IRF2 and regulates its activity on the H4 promoter. Interacts (via N-terminus) with SS18L1/CREST (via C-terminus). Interacts with FOXO1; the interaction acetylates FOXO1 and inhibits its transcriptional activity. Interacts with MECOM and MTDH. Interacts with ASF1A and ASF1B; this promotes histone acetylation. Interacts with acetylated TP53/p53 and with the acetylated histones H3 and H4 (By similarity). Interacts with CITED1 (via C-terminus). Interacts with GATA1; the interaction results in acetylation and enhancement of transcriptional activity of GATA1. Interacts with MAF, CARM1. NCOA3, ZCCHC12, DDX17, DDX5 AND CITED4 (C-terminal region). Interacts with phosphorylated CREB1. Interacts with DAXX; the interaction is dependent on CBP sumoylation and results in suppression of the transcriptional activity via recruitment of HDAC2 to DAXX. Interacts with NPAS2, CLOCK and ARNTL/BMAL1. Interacts with SMAD4; negatively regulated by ZBTB7A (By similarity). {ECO:0000250|UniProtKB:Q92793, ECO:0000269|PubMed:10207073, ECO:0000269|PubMed:10722728, ECO:0000269|PubMed:11701890, ECO:0000269|PubMed:11943779, ECO:0000269|PubMed:12504852, ECO:0000269|PubMed:12527917, ECO:0000269|PubMed:14594809, ECO:0000269|PubMed:16287980, ECO:0000269|PubMed:17226766, ECO:0000269|PubMed:18160706, ECO:0000269|PubMed:24737000, ECO:0000269|PubMed:8552098, ECO:0000269|PubMed:8616895, ECO:0000269|PubMed:9192892}. +E9Q6B2 CC85C_MOUSE Coiled-coil domain-containing protein 85C 420 45,334 Chain (1); Coiled coil (2); Compositional bias (1); Initiator methionine (1); Modified residue (3) FUNCTION: May play an important role in cortical development, especially in the maintenance of radial glia. {ECO:0000269|PubMed:22056358}. SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000269|PubMed:22056358}. Note=Localizes to the apical junction of radial glia in the wall of lateral ventricles of the developing brain. Colocalizes with TJP1 on the meshwork-like structure of adherens junctions on the lateral ventricles wall. TISSUE SPECIFICITY: Predominantly expressed on the surface of the lateral ventricular walls of the developing cerebral cortex. {ECO:0000269|PubMed:22056358}. +Q3UHB8 CC177_MOUSE Coiled-coil domain-containing protein 177 706 79,857 Chain (1); Coiled coil (1); Compositional bias (3); Modified residue (1); Sequence conflict (1) +Q8BSN3 CC151_MOUSE Coiled-coil domain-containing protein 151 593 69,732 Alternative sequence (3); Chain (1); Coiled coil (2); Sequence conflict (2) FUNCTION: Ciliary protein involved in outer dynein arm assembly and required for motile cilia function. {ECO:0000269|PubMed:24067530}. SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000269|PubMed:24067530}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:24067530}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:24067530}. Note=Enriched at centrioles in IMCD3 dividing cells. {ECO:0000269|PubMed:24067530}. SUBUNIT: Interacts with CCDC114. {ECO:0000250|UniProtKB:A5D8V7}. +P84444 CC21A_MOUSE C-C motif chemokine 21a (6Ckine) (Beta-chemokine exodus-2) (Small-inducible cytokine A21a) (Thymus-derived chemotactic agent 4) (TCA4) 133 14,558 Chain (1); Disulfide bond (3); Region (1); Signal peptide (1) FUNCTION: Inhibits hemopoiesis and stimulates chemotaxis. Chemotactic in vitro for thymocytes and activated T-cells, but not for B-cells, macrophages, or neutrophils. Potent mesangial cell chemoattractant. Shows preferential activity towards naive T-cells. May play a role in mediating homing of lymphocytes to secondary lymphoid organs. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Binds to CCR7 and to CXCR3.Interacts with PDPN; relocalizes PDPN to the basolateral membrane. {ECO:0000250|UniProtKB:O00585}. TISSUE SPECIFICITY: Expressed strongly in lung, spleen, thymus, peripheral and mesentric lymph nodes. Also expressed in the testis, kidney, liver, and heart. DISEASE: Note=Mice carrying an autosomal recessive mutation designated paucity of lymph node T-cells (plt) show dramatically reduced numbers of T-cells in lymph nodes, Peyer patches, and the white pulp of the spleen. Plt seems to correspond to Scya21b. {ECO:0000269|PubMed:10523616}. +Q8K354 CBR3_MOUSE Carbonyl reductase [NADPH] 3 (EC 1.1.1.184) (NADPH-dependent carbonyl reductase 3) 277 30,953 Active site (1); Binding site (2); Chain (1); Initiator methionine (1); Modified residue (2); Nucleotide binding (4) FUNCTION: Has low NADPH-dependent oxidoreductase activity towards 4-benzoylpyridine and menadione (in vitro). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +Q0VG85 CC162_MOUSE Coiled-coil domain-containing protein 162 912 104,336 Alternative sequence (7); Chain (1); Coiled coil (2) +Q91VT4 CBR4_MOUSE Carbonyl reductase family member 4 (EC 1.-.-.-) (3-ketoacyl-[acyl-carrier-protein] reductase beta subunit) (KAR beta subunit) (3-oxoacyl-[acyl-carrier-protein] reductase) (EC 1.1.1.-) (Quinone reductase CBR4) 236 25,415 Active site (1); Binding site (4); Chain (1); Erroneous initiation (1); Modified residue (4); Nucleotide binding (4); Sequence conflict (1); Site (1) Lipid metabolism; fatty acid biosynthesis. FUNCTION: The heterotetramer with HSD17B8 has NADH-dependent 3-ketoacyl-acyl carrier protein reductase activity, and thereby plays a role in mitochondrial fatty acid biosynthesis. Within the heterotetramer, HSD17B8 binds NADH; CBR4 binds NADPD. The homotetramer has NADPH-dependent quinone reductase activity. Both homotetramer and the heterotetramer have broad in vitro substrate specificity and can reduce 9,10-phenanthrenequinone, 1,4-benzoquinone and various other o-quinones and p-quinones. {ECO:0000250|UniProtKB:Q8N4T8}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:Q8N4T8}. SUBUNIT: Homotetramer (in vitro). Heterotetramer with HSD17B8; contains two molecules each of HSD17B8 and CBR4. Does not form homotetramers when HSD17B8 is coexpressed, only heterotetramers (in vitro). {ECO:0000250|UniProtKB:Q8N4T8}. +Q9D516 CC130_MOUSE Coiled-coil domain-containing protein 130 385 43,880 Alternative sequence (2); Chain (1); Coiled coil (1); Modified residue (2) +Q640L5 CCD18_MOUSE Coiled-coil domain-containing protein 18 1455 169,741 Alternative sequence (7); Chain (1); Coiled coil (2); Compositional bias (1); Modified residue (2) +Q8VEG0 CCD71_MOUSE Coiled-coil domain-containing protein 71 433 46,010 Chain (1); Coiled coil (1); Compositional bias (1); Modified residue (1); Sequence conflict (1) +Q8CDM4 CCD73_MOUSE Coiled-coil domain-containing protein 73 1066 120,389 Chain (1); Coiled coil (2); Erroneous initiation (1); Sequence conflict (2) +O70578 CCG1_MOUSE Voltage-dependent calcium channel gamma-1 subunit (Dihydropyridine-sensitive L-type, skeletal muscle calcium channel subunit gamma) 223 25,120 Chain (1); Disulfide bond (1); Glycosylation (2); Topological domain (5); Transmembrane (4) TRANSMEM 11 29 Helical. {ECO:0000250|UniProtKB:P19518}.; TRANSMEM 110 130 Helical. {ECO:0000250|UniProtKB:P19518}.; TRANSMEM 136 156 Helical. {ECO:0000250|UniProtKB:P19518}.; TRANSMEM 181 205 Helical. {ECO:0000250|UniProtKB:P19518}. TOPO_DOM 1 10 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 30 109 Extracellular. {ECO:0000305}.; TOPO_DOM 131 135 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 157 180 Extracellular. {ECO:0000305}.; TOPO_DOM 206 223 Cytoplasmic. {ECO:0000305}. FUNCTION: Regulatory subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents in skeletal muscle. Regulates channel inactivation kinetics. {ECO:0000269|PubMed:10799530, ECO:0000269|PubMed:12409298}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:P19518}. SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000305|PubMed:10799530, ECO:0000305|PubMed:9504716}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P19518}. SUBUNIT: Component of a calcium channel complex consisting of a pore-forming alpha subunit (CACNA1S) and the ancillary subunits CACNB1 or CACNB2, CACNG1 and CACNA2D1 (PubMed:10799530, PubMed:12409298). The channel complex contains alpha, beta, gamma and delta subunits in a 1:1:1:1 ratio, i.e. it contains either CACNB1 or CACNB2 (By similarity). {ECO:0000250|UniProtKB:P19518, ECO:0000269|PubMed:10799530, ECO:0000269|PubMed:12409298}. TISSUE SPECIFICITY: Detected in skeletal muscle (at protein level). {ECO:0000269|PubMed:10799530, ECO:0000269|PubMed:9504716}. +Q6PG04 CCD82_MOUSE Coiled-coil domain-containing protein 82 518 61,008 Chain (1); Coiled coil (1); Compositional bias (2); Modified residue (4) +Q3MI99 CCBE1_MOUSE Collagen and calcium-binding EGF domain-containing protein 1 (Full of fluid protein homolog) 408 44,357 Chain (1); Disulfide bond (3); Domain (3); Erroneous initiation (1); Glycosylation (2); Sequence conflict (3); Signal peptide (1) FUNCTION: Required for lymphangioblast budding and angiogenic sprouting from venous endothelium during embryogenesis. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q5SV66 CCD42_MOUSE Coiled-coil domain-containing protein 42 316 37,989 Alternative sequence (2); Chain (1); Coiled coil (2) FUNCTION: Required for sperm development. {ECO:0000269|PubMed:26945718}. TISSUE SPECIFICITY: Only expressed in the brain and developing sperm. Expression in the testes appears at approximately ten days of age and is maintained into adulthood, corresponding with the onset of meiosis. Expression in the testes appears limited to adluminal spermatids that are engaged in the assembly of flagella. Strong expression is observed in the spermatids within the lumen of the seminiferous tubules in testes from 8-week-old mice, but not in cells adjacent to the basement membrane of the tubule, including Sertoli cells, spermatogonia and spermatocytes. Not expressed in ovaries. {ECO:0000269|PubMed:26945718}. +Q9DA73 CCD89_MOUSE Coiled-coil domain-containing protein 89 (Bc8 orange-interacting protein) 370 43,241 Chain (1); Coiled coil (1); Frameshift (1); Modified residue (1); Sequence caution (1); Sequence conflict (3) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q7ZW57}. Nucleus {ECO:0000250|UniProtKB:Q7ZW57}. Note=Uniformly distributed within the cell, but becomes recruited to the nucleus upon binding to HEY1. {ECO:0000250|UniProtKB:Q7ZW57}. SUBUNIT: Interacts with HEY1. {ECO:0000269|PubMed:14648848}. TISSUE SPECIFICITY: Expression is restricted to the adult testis, where localization is almost exclusive to round spermatids. {ECO:0000269|PubMed:14648848}. +Q3TCJ8 CCD69_MOUSE Coiled-coil domain-containing protein 69 202 23,296 Alternative sequence (1); Chain (1); Coiled coil (1); Initiator methionine (1); Lipidation (1); Modified residue (1) FUNCTION: May act as a scaffold to regulate the recruitment and assembly of spindle midzone components. Required for the localization of AURKB and PLK1 to the spindle midzone. {ECO:0000250|UniProtKB:A6NI79}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:A6NI79}. Midbody {ECO:0000250|UniProtKB:A6NI79}. Note=During early anaphase, localizes along overlapping interpolar microtubules between the separating chromosomes. During late anaphase, localizes to the center of spindle midzone. Concentrated at the midbody during telophase. {ECO:0000250|UniProtKB:A6NI79}. +P30882 CCL5_MOUSE C-C motif chemokine 5 (MuRantes) (SIS-delta) (Small-inducible cytokine A5) (T-cell-specific protein RANTES) 91 10,071 Beta strand (5); Chain (1); Disulfide bond (2); Helix (1); Sequence conflict (2); Signal peptide (1); Turn (1) FUNCTION: Chemoattractant for blood monocytes, memory T-helper cells and eosinophils. Causes the release of histamine from basophils and activates eosinophils. May activate several chemokine receptors including CCR1, CCR3, CCR4 and CCR5. May also be an agonist of the G protein-coupled receptor GPR75. Together with GPR75, may play a role in neuron survival through activation of a downstream signaling pathway involving the PI3, Akt and MAP kinases. By activating GPR75 may also play a role in insulin secretion by islet cells. {ECO:0000250|UniProtKB:P13501}. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: T-cell and macrophage specific. +P51670 CCL9_MOUSE C-C motif chemokine 9 (CCF18) (Macrophage inflammatory protein 1-gamma) (MIP-1-gamma) (Macrophage inflammatory protein-related protein 2) (MRP-2) (Small-inducible cytokine A9) [Cleaved into: CCL9(29-101); CCL9(30-101); CCL9(31-101)] 122 13,871 Chain (4); Disulfide bond (3); Sequence conflict (1); Signal peptide (1) FUNCTION: Monokine with inflammatory, pyrogenic and chemokinetic properties. Circulates at high concentrations in the blood of healthy animals. Binding to a high-affinity receptor activates calcium release in neutrophils. It also inhibits colony formation of bone marrow myeloid immature progenitors. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Expressed mainly in the liver, lung, and the thymus, although some expression has been detected in a wide variety of tissues except brain. +P70343 CASP4_MOUSE Caspase-4 (CASP-4) (EC 3.4.22.64) (Caspase-11) (CASP-11) (Protease ICH-3) [Cleaved into: Caspase-4 subunit p10; Caspase-4 subunit p20] 373 42,742 Active site (2); Alternative sequence (2); Chain (2); Domain (1); Modified residue (1); Mutagenesis (11); Propeptide (2); Region (1); Sequence conflict (2) FUNCTION: Proinflammatory caspase (PubMed:8702803, PubMed:9038361, PubMed:25119034). Essential effector of NLRP3 inflammasome-dependent CASP1 activation and IL1B and IL18 secretion in response to non-canonical activators, such as UVB radiation, cholera enterotoxin subunit B and cytosolic LPS, as well as infection with Gram-negative bacteria (PubMed:22002608). Independently of NLRP3 inflammasome and CASP1, promotes pyroptosis, through GSDMD cleavage and activation, and IL1A, IL18 and HMGB1 release in response to non-canonical inflammasome activators (PubMed:22002608, PubMed:26320999, PubMed:26375003). Plays a crucial role in the restriction of Salmonella typhimurium replication in colonic epithelial cells during infection. In later stages of the infection (>3 days post infection), LPS from cytosolic Salmonella triggers CASP4 activation, which ultimately results in the pyroptosis of the infected cells and their extrusion into the gut lumen, as well as in IL18 secretion. Pyroptosis limits bacterial replication, while cytokine secretion promotes the recruitment and activation of immune cells and triggers mucosal inflammation (PubMed:25121752). Involved in LPS-induced IL6 secretion; this activity may not require caspase enzymatic activity (By similarity). Involved in cell death induced by endoplasmic reticulum stress (By similarity). Activated by direct binding to LPS without the need of an upstream sensor (PubMed:25119034). Does not directly process IL1B (PubMed:8702803, PubMed:9038361). During non-canonical inflammasome activation, cuts CGAS and may play a role in the regulation of antiviral innate immune activation (PubMed:28314590). {ECO:0000250|UniProtKB:P49662, ECO:0000269|PubMed:22002608, ECO:0000269|PubMed:25119034, ECO:0000269|PubMed:25121752, ECO:0000269|PubMed:26320999, ECO:0000269|PubMed:26375003, ECO:0000269|PubMed:28314590, ECO:0000269|PubMed:8702803, ECO:0000269|PubMed:9038361}. PTM: In response to activation signals, including cholera enterotoxin subunit B, infection by E. coli or S. typhimurium or endoplasmic reticulum stress, undergoes autoproteolytic cleavage. {ECO:0000269|PubMed:22002608, ECO:0000269|PubMed:25121752}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P49662}. Cytoplasm {ECO:0000269|PubMed:16670335}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P49662}; Peripheral membrane protein {ECO:0000250|UniProtKB:P49662}; Cytoplasmic side {ECO:0000250|UniProtKB:P49662}. Mitochondrion {ECO:0000250|UniProtKB:P49662}. Inflammasome {ECO:0000269|PubMed:25119034}. Secreted {ECO:0000250|UniProtKB:P49662}. Note=Predominantly localizes to the endoplasmic reticulum (ER). Association with the ER membrane requires TMEM214. Released in the extracellular milieu by keratinocytes following UVB irradiation. {ECO:0000250|UniProtKB:P49662}. SUBUNIT: Upon direct LPS-binding, forms large homooligomers, resulting in its activation. These oligomers are often referred to as 'non-canonical inflammasomes' (PubMed:25119034). Active as a heterotetramer consisting of two anti-parallel arranged heterodimers, each one formed by a small and a large subunit (By similarity). In its precursor form, interacts with TMEM214; this interaction is required for association with the endoplasmic reticulum membrane. Interacts with CASP1. Interacts with NOD2. {ECO:0000250, ECO:0000250|UniProtKB:P49662, ECO:0000269|PubMed:25119034}. DOMAIN: The CARD domain mediates LPS recognition and homooligomerization. {ECO:0000269|PubMed:25119034}. TISSUE SPECIFICITY: Widely expressed, including in thymus, lung and spleen (at protein level). Very low levels, if any, in the brain. {ECO:0000269|PubMed:8702803, ECO:0000269|PubMed:9038361}. +Q9R013 CATF_MOUSE Cathepsin F (EC 3.4.22.41) 462 51,661 Active site (3); Chain (1); Disulfide bond (3); Glycosylation (6); Propeptide (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis. SUBCELLULAR LOCATION: Lysosome. +Q9CS00 CATIN_MOUSE Cactin 772 90,661 Chain (1); Coiled coil (2); Compositional bias (1); Cross-link (2); Modified residue (3) FUNCTION: Involved in the regulation of innate immune response. Acts as negative regulator of Toll-like receptor and interferon-regulatory factor (IRF) signaling pathways. Contributes to the regulation of transcriptional activation of NF-kappa-B target genes in response to endogenous proinflammatory stimuli. May play a role during early embryonic development. Probably involved in pre-mRNA splicing (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Nuclear localization with a speckled expression pattern in some cells. Colocalizes with NFKBIL1 in the nucleus (By similarity). {ECO:0000250}. SUBUNIT: Interacts (via N-terminal domain) with NFKBIL1; the interaction occurs in a proinflammatory-independent manner. Does not interact with RELA NF-kappa-B subunit. Identified in the spliceosome C complex (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in cortex, hippocampus, cerebellum, heart, lung, kidney, liver, spleen and thymus. {ECO:0000269|PubMed:20829348}. +Q8CDT7 CBCO1_MOUSE Ciliary-associated calcium-binding coiled-coil protein 1 208 24,087 Chain (1); Erroneous initiation (2) FUNCTION: Calcium-binding protein (PubMed:26990073). May be involved in the control of sperm flagellar movement (PubMed:26990073). {ECO:0000269|PubMed:26990073}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:26990073}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:26990073}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:26990073}. Note=Colocalized with pericentrin at centrosome of spermatocytes and round spermatids (PubMed:26990073). {ECO:0000269|PubMed:26990073}. TISSUE SPECIFICITY: Testis-specific (PubMed:26990073). Expressed in spermatocytes and round spermatids (at protein level) (PubMed:26990073). {ECO:0000269|PubMed:26990073}. +Q5U901 CBPA6_MOUSE Carboxypeptidase A6 (EC 3.4.17.-) 438 51,143 Active site (1); Alternative sequence (1); Binding site (2); Chain (1); Disulfide bond (1); Glycosylation (4); Metal binding (3); Propeptide (1); Region (3); Signal peptide (1) FUNCTION: May be involved in the proteolytic inactivation of enkephalins and neurotensin in some brain areas. May convert inactive angiotensin I into the biologically active angiotensin II. Releases a C-terminal amino acid, with preference for large hydrophobic C-terminal amino acids and shows only very weak activity toward small amino acids and histidine. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. TISSUE SPECIFICITY: In brain, highly expressed in the olfactory bulb with lower levels in other regions including cerebral cortex, hippocampus, hypothalamus, striatum and medulla. Within the olfactory bulb, highest levels occur in the mitral and granular layers with lower levels in the internal and external plexiform layers. Moderate levels are found in the epididymis with low levels in colon and spleen. Not detected in adrenal, liver, lung, ovary or testis. At embryonic day 14.5, enriched in eye, ear, osteoblasts, stomach, skin, dorsal root ganglia and throughout the CNS. {ECO:0000269|PubMed:15950771}. +Q80V42 CBPM_MOUSE Carboxypeptidase M (CPM) (EC 3.4.17.12) 443 50,556 Active site (1); Alternative sequence (2); Chain (1); Disulfide bond (3); Erroneous initiation (1); Glycosylation (3); Lipidation (1); Metal binding (3); Propeptide (1); Signal peptide (1) FUNCTION: Specifically removes C-terminal basic residues (Arg or Lys) from peptides and proteins. It is believed to play important roles in the control of peptide hormone and growth factor activity at the cell surface, and in the membrane-localized degradation of extracellular proteins (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. +Q8R4V4 CBPZ_MOUSE Carboxypeptidase Z (CPZ) (EC 3.4.17.-) 654 73,721 Active site (1); Chain (1); Disulfide bond (5); Domain (1); Glycosylation (2); Metal binding (3); Sequence conflict (1); Signal peptide (1) FUNCTION: Cleaves substrates with C-terminal arginine residues. Probably modulates the Wnt signaling pathway, by cleaving some undefined protein. May play a role in cleavage during prohormone processing (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. +Q8BGD0 CC014_MOUSE Uncharacterized protein C3orf14 homolog 127 14,729 Alternative sequence (1); Chain (1); Sequence conflict (1) +Q8VE99 CC115_MOUSE Coiled-coil domain-containing protein 115 (Coiled-coil protein 1) (Ccp1) 180 19,743 Chain (1); Coiled coil (1) FUNCTION: Accessory component of the proton-transporting vacuolar (V)-ATPase protein pump involved in intracellular iron homeostasis. In aerobic conditions, required for intracellular iron homeostasis, thus triggering the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent proteasomal degradation. Necessary for endolysosomal acidification and lysosomal degradation (By similarity). May be involved in Golgi homeostasis (By similarity). {ECO:0000250|UniProtKB:Q96NT0}. SUBCELLULAR LOCATION: Endosome {ECO:0000269|PubMed:16378758}. Lysosome {ECO:0000269|PubMed:16378758}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250|UniProtKB:Q96NT0}. Cytoplasmic vesicle, COPI-coated vesicle {ECO:0000250|UniProtKB:Q96NT0}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q96NT0}. Note=Seems not to be associated with recycling endosomes. {ECO:0000269|PubMed:16378758}. SUBUNIT: Accessory component of the multisubunit proton-transporting vacuolar (V)-ATPase protein pump. {ECO:0000250|UniProtKB:Q96NT0}. TISSUE SPECIFICITY: Predominantly expressed in the heart, liver, kidney and testis and at lower levels in the brain and lung. Undetectable in the spleen and muscles. {ECO:0000269|PubMed:16378758}. +E9Q1U1 CC171_MOUSE Coiled-coil domain-containing protein 171 1324 152,309 Alternative sequence (1); Chain (1); Coiled coil (5) +Q6GQT0 CC14A_MOUSE Dual specificity protein phosphatase CDC14A (EC 3.1.3.16) (EC 3.1.3.48) (CDC14 cell division cycle 14 homolog A) 603 67,634 Active site (1); Alternative sequence (1); Chain (1); Compositional bias (2); Modified residue (2); Mutagenesis (1); Region (3) FUNCTION: Dual-specificity phosphatase. Required for centrosome separation and productive cytokinesis during cell division. Dephosphorylates SIRT2 around early anaphase. May dephosphorylate the APC subunit FZR1/CDH1, thereby promoting APC-FZR1 dependent degradation of mitotic cyclins and subsequent exit from mitosis (By similarity). Required for normal hearing (PubMed:29293958). {ECO:0000250|UniProtKB:Q9UNH5, ECO:0000269|PubMed:29293958}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UNH5}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9UNH5}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9UNH5}. Cell projection, kinocilium {ECO:0000269|PubMed:27259055, ECO:0000269|PubMed:29293958}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q9UNH5}. Cell projection, stereocilium {ECO:0000269|PubMed:29293958}. Note=Centrosomal during interphase, released into the cytoplasm at the onset of mitosis. Subsequently localizes to the mitotic spindle pole and at the central spindle (By similarity). Present along both the transient kinocilia of developing cochlear hair cells and the persistent kinocilia of vestibular hair cells (PubMed:27259055). {ECO:0000250|UniProtKB:Q9UNH5, ECO:0000269|PubMed:27259055}. SUBUNIT: Interacts with KIF20A. Interaction is required to localize CDC14 to the midzone of the mitotic spindle (By similarity). {ECO:0000250}. DOMAIN: Composed of two structurally equivalent A and B domains that adopt a dual specificity protein phosphatase (DSP) fold. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the inner ear. {ECO:0000269|PubMed:29293958}. +P48758 CBR1_MOUSE Carbonyl reductase [NADPH] 1 (EC 1.1.1.184) (15-hydroxyprostaglandin dehydrogenase [NADP(+)]) (EC 1.1.1.197) (NADPH-dependent carbonyl reductase 1) (Prostaglandin 9-ketoreductase) (Prostaglandin-E(2) 9-reductase) (EC 1.1.1.189) 277 30,641 Active site (1); Binding site (3); Chain (1); Initiator methionine (1); Modified residue (3); Nucleotide binding (4); Region (2); Sequence conflict (3) FUNCTION: NADPH-dependent reductase with broad substrate specificity. Catalyzes the reduction of a wide variety of carbonyl compounds including quinones, prostaglandins, menadione, plus various xenobiotics. Catalyzes the reduction of the antitumor anthracyclines doxorubicin and daunorubicin to the cardiotoxic compounds doxorubicinol and daunorubicinol. Can convert prostaglandin E2 to prostaglandin F2-alpha. Can bind glutathione, which explains its higher affinity for glutathione-conjugated substrates. Catalyzes the reduction of S-nitrosoglutathione (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Monomer. {ECO:0000250}. +Q9CPZ1 CC198_MOUSE Uncharacterized protein CCDC198 294 34,455 Chain (1); Sequence conflict (4) +Q8BVN0 CC122_MOUSE Coiled-coil domain-containing protein 122 290 34,235 Chain (1); Coiled coil (2) +P30658 CBX2_MOUSE Chromobox protein homolog 2 (M33) (Modifier 3 protein) 519 54,918 Chain (1); Compositional bias (2); Cross-link (2); DNA binding (1); Domain (1); Modified residue (3); Motif (1); Sequence conflict (4) FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development (By similarity). PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility (By similarity). Binds to histone H3 trimethylated at 'Lys-9' (H3K9me3) or at 'Lys-27' (H3K27me3) (PubMed:16537902). Plays a role in the lineage differentiation of the germ layers in embryonic development (PubMed:22226355). Involved in sexual development, acting as activator of NR5A1 expression (By similarity). {ECO:0000250|UniProtKB:Q14781, ECO:0000269|PubMed:16537902, ECO:0000269|PubMed:22226355}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:9312051}. Chromosome {ECO:0000269|PubMed:16537902}. Note=Localizes to the inactivated X chromosome in females. {ECO:0000269|PubMed:16537902}. SUBUNIT: Component of a PRC1-like complex (By similarity). The composition of the PRC1 complex may differ between the PRC1 complex in pluripotent embryonic stem cells containing RNF2, CBX7 and PCGF2, and the PRC1 complex in differentiating cells containing RNF2, CBX2, CBX4 and BMI1 (PubMed:22226355). Interacts with RING1/RNF2 (PubMed:9312051, PubMed:22226355). Interacts (via chromodomain) with histone H3K9Me3 and H3K27me3 (PubMed:16537902). May interact with HIST2H3A and HIST1H3A (By similarity). {ECO:0000250|UniProtKB:Q14781, ECO:0000269|PubMed:16537902, ECO:0000269|PubMed:22226355, ECO:0000269|PubMed:9312051}. TISSUE SPECIFICITY: Expressed in embryoid bodies. {ECO:0000269|PubMed:22226355}. +Q8C963 CC159_MOUSE Coiled-coil domain-containing protein 159 411 46,342 Alternative sequence (3); Chain (1); Coiled coil (1); Sequence conflict (1) +Q8BN57 CC033_MOUSE Protein C3orf33 homolog 294 33,668 Chain (1); Initiator methionine (1); Modified residue (1); Transmembrane (1) TRANSMEM 36 53 Helical. {ECO:0000255}. FUNCTION: May play a role in transcription regulation. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q8K2J4 CCD14_MOUSE Coiled-coil domain-containing protein 14 934 102,630 Chain (1); Coiled coil (1); Erroneous initiation (2); Modified residue (4); Sequence caution (1); Sequence conflict (11) FUNCTION: Negatively regulates centriole duplication. Negatively regulates CEP63 and CDK2 centrosomal localization. {ECO:0000250|UniProtKB:Q49A88}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000250|UniProtKB:Q49A88}. Note=Colocalizes with PCM1 at centriolar satellites throughout the cell cycle. {ECO:0000250|UniProtKB:Q49A88}. SUBUNIT: Interacts with CEP63. {ECO:0000250|UniProtKB:Q49A88}. +D3Z5T1 CCD78_MOUSE Coiled-coil domain-containing protein 78 437 49,472 Chain (1); Coiled coil (3) FUNCTION: Component of the deuterosome, a structure that promotes de novo centriole amplification in multiciliated cells that can generate more than 100 centrioles. Deuterosome-mediated centriole amplification occurs in terminally differentiated multiciliated cells (G1/0) and not in S phase. Essential for centriole amplification and is required for CEP152 localization to the deuterosome (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane, sarcolemma {ECO:0000250}. Sarcoplasmic reticulum {ECO:0000250}. Note=Localizes to centrioles and deuterosome. Found primarily in the perinuclear region as well as along the sarcolemmal membrane and in reticular pattern within the sarcoplasm (By similarity). {ECO:0000250}. +Q4VA36 CCD84_MOUSE Coiled-coil domain-containing protein 84 332 37,701 Alternative sequence (4); Chain (1); Coiled coil (1); Compositional bias (1); Erroneous initiation (1) +P62956 CCG7_MOUSE Voltage-dependent calcium channel gamma-7 subunit (Neuronal voltage-gated calcium channel gamma-7 subunit) (Transmembrane AMPAR regulatory protein gamma-7) (TARP gamma-7) 275 31,003 Chain (1); Modified residue (3); Transmembrane (4) TRANSMEM 8 28 Helical. {ECO:0000255}.; TRANSMEM 103 123 Helical. {ECO:0000255}.; TRANSMEM 129 149 Helical. {ECO:0000255}.; TRANSMEM 179 199 Helical. {ECO:0000255}. FUNCTION: Regulates the activity of L-type calcium channels that contain CACNA1C as pore-forming subunit (By similarity). Regulates the trafficking and gating properties of AMPA-selective glutamate receptors (AMPARs). Promotes their targeting to the cell membrane and synapses and modulates their gating properties by slowing their rates of activation, deactivation and desensitization and by mediating their resensitization (By similarity). Shows specificity only for GRIA1 and GRIA2 (By similarity). {ECO:0000250|UniProtKB:P62955, ECO:0000250|UniProtKB:P62957}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P62955}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with CACNA1C. Identified in a complex with the L-type calcium channel subunits CACNA1C, CACNA2D1 and either CACNB1 or CACNB2 (By similarity). Acts as an auxiliary subunit for AMPA-selective glutamate receptors (AMPARs), such as GRIA1 and GRIA2 (By similarity). {ECO:0000250|UniProtKB:P62955, ECO:0000250|UniProtKB:P62957}. +P27784 CCL6_MOUSE C-C motif chemokine 6 (Protein C10) (Small-inducible cytokine A6) [Cleaved into: CCL6(22-95); CCL6(23-95)] 116 12,984 Chain (3); Disulfide bond (3); Sequence conflict (3); Signal peptide (1) FUNCTION: CCL6(22-95) and CCL6(23-95) are potent chemoattractants. {ECO:0000269|PubMed:15905581}. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Expressed in myelopoietic bone marrow cultures stimulated by GM-CSF. +Q62401 CCL12_MOUSE C-C motif chemokine 12 (MCP-1-related chemokine) (Monocyte chemoattractant protein 5) (Monocyte chemotactic protein 5) (MCP-5) (Small-inducible cytokine A12) 104 11,659 Chain (1); Disulfide bond (2); Natural variant (1); Signal peptide (1) FUNCTION: Chemotactic factor that attracts eosinophils, monocytes, and lymphocytes but not neutrophils. Potent monocyte active chemokine that signals through CCR2. Involved in allergic inflammation and the host response to pathogens and may play a pivotal role during early stages of allergic lung inflammation. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Predominantly expressed in the lymph nodes and thymus. Also found in the salivary glands containing lymph nodes, breast, heart, lung, brain, small intestine, kidney and colon. +Q9JIL2 CCL28_MOUSE C-C motif chemokine 28 (Small-inducible cytokine A28) 130 14,570 Chain (1); Disulfide bond (2); Glycosylation (1); Signal peptide (1) FUNCTION: Chemotactic for resting CD4, CD8 T-cells and eosinophils (By similarity). Binds to CCR10 and induces calcium mobilization in a dose-dependent manner. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. TISSUE SPECIFICITY: Mainly expressed in testis, epithelial cells of normal colon, kidney, Peyer patches, lymph nodes. Also found in lower levels in brain, spleen and lung. +Q62447 CCNC_MOUSE Cyclin-C 283 33,241 Chain (1); Domain (1); Modified residue (1); Sequence conflict (1) FUNCTION: Component of the Mediator complex, a coactivator involved in regulated gene transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. Binds to and activates cyclin-dependent kinase CDK8 that phosphorylates the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNAp II), which may inhibit the formation of a transcription initiation complex (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Component of the Mediator complex, which is composed of MED1, MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L, MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23, MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8 subunits form a distinct module termed the CDK8 module. Mediator containing the CDK8 module is less active than Mediator lacking this module in supporting transcriptional activation. Individual preparations of the Mediator complex lacking one or more distinct subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and TRAP. The cylin/CDK pair formed by CCNC/CDK8 also associates with the large subunit of RNA polymerase II (By similarity). {ECO:0000250}. +Q5SRT8 CCNJL_MOUSE Cyclin-J-like protein 387 43,530 Chain (1); Domain (1) +Q3TZI6 CCNJ_MOUSE Cyclin-J 379 43,488 Alternative sequence (1); Chain (1); Domain (1); Sequence conflict (1) +O88874 CCNK_MOUSE Cyclin-K 554 61,363 Chain (1); Modified residue (3); Sequence conflict (2) FUNCTION: Regulatory subunit of cyclin-dependent kinases that mediates activation of target kinases. Plays a role in transcriptional regulation via its role in regulating the phosphorylation of the C-terminal domain (CTD) of the large subunit of RNA polymerase II (POLR2A). {ECO:0000269|PubMed:22012619}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:22012619}. SUBUNIT: Regulatory subunit of cyclin-dependent kinases. Identified in a complex with a kinase and the RNA polymerase II holoenzyme. Interacts with POLR2A. Interacts with CDK12 and CDK13. Its interaction with CDK9 is controversial. {ECO:0000269|PubMed:22012619}. TISSUE SPECIFICITY: Ubiquitously expressed. Highest levels in testis. Present throughout the seminiferous epithelium. Also highly expressed in the developing oocyte. +O54689 CCR6_MOUSE C-C chemokine receptor type 6 (C-C CKR-6) (CC-CKR-6) (CCR-6) (KY411) (CD antigen CD196) 367 42,103 Chain (1); Disulfide bond (1); Glycosylation (2); Topological domain (8); Transmembrane (7) TRANSMEM 40 66 Helical; Name=1. {ECO:0000255}.; TRANSMEM 76 96 Helical; Name=2. {ECO:0000255}.; TRANSMEM 112 133 Helical; Name=3. {ECO:0000255}.; TRANSMEM 152 172 Helical; Name=4. {ECO:0000255}.; TRANSMEM 204 230 Helical; Name=5. {ECO:0000255}.; TRANSMEM 247 271 Helical; Name=6. {ECO:0000255}.; TRANSMEM 296 313 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 39 Extracellular. {ECO:0000255}.; TOPO_DOM 67 75 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 97 111 Extracellular. {ECO:0000255}.; TOPO_DOM 134 151 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 173 203 Extracellular. {ECO:0000255}.; TOPO_DOM 231 246 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 272 295 Extracellular. {ECO:0000255}.; TOPO_DOM 314 367 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for the C-C type chemokine CCL20. Binds to CCL20 and subsequently transduces a signal by increasing the intracellular calcium ion levels (PubMed:20068036). Although CCL20 is its major ligand it can also act as a receptor for non-chemokine ligands such as beta-defensins (PubMed:25122636). Binds to defensin DEFB1 leading to increase in intracellular calcium ions and cAMP levels. Its binding to DEFB1 is essential for the function of DEFB1 in regulating sperm motility and bactericidal activity (By similarity). Binds to defensins DEFB4 and DEFB4A/B and mediates their chemotactic effects (PubMed:20068036). The ligand-receptor pair CCL20-CCR6 is responsible for the chemotaxis of dendritic cells (DC), effector/memory T-cells and B-cells and plays an important role at skin and mucosal surfaces under homeostatic and inflammatory conditions, as well as in pathology, including cancer and various autoimmune diseases. CCR6-mediated signals are essential for immune responses to microbes in the intestinal mucosa and in the modulation of inflammatory responses initiated by tissue insult and trauma (PubMed:21376174). CCR6 is essential for the recruitment of both the proinflammatory IL17 producing helper T-cells (Th17) and the regulatory T-cells (Treg) to sites of inflammation (PubMed:19050256). Required for the normal migration of Th17 cells in Peyers patches and other related tissue sites of the intestine and plays a role in regulating effector T-cell balance and distribution in inflamed intestine (PubMed:19129757). Plays an important role in the coordination of early thymocyte precursor migration events important for normal subsequent thymocyte precursor development, but is not required for the formation of normal thymic natural regulatory T-cells (nTregs). Required for optimal differentiation of DN2 and DN3 thymocyte precursors (PubMed:24638065). Essential for B-cell localization in the subepithelial dome of Peyers-patches and for efficient B-cell isotype switching to IgA in the Peyers-patches (PubMed:27174992). Essential for appropriate anatomical distribution of memory B-cells in the spleen and for the secondary recall response of memory B-cells (PubMed:25505290). Positively regulates sperm motility and chemotaxis via its binding to CCL20 (PubMed:23765988). {ECO:0000250|UniProtKB:P51684, ECO:0000269|PubMed:19050256, ECO:0000269|PubMed:19129757, ECO:0000269|PubMed:20068036, ECO:0000269|PubMed:23765988, ECO:0000269|PubMed:24638065, ECO:0000269|PubMed:25122636, ECO:0000269|PubMed:25505290, ECO:0000269|PubMed:27174992, ECO:0000303|PubMed:21376174}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23765988}; Multi-pass membrane protein {ECO:0000255}. Cell surface {ECO:0000250|UniProtKB:P51684}. TISSUE SPECIFICITY: Sperm. Mainly localized in the principal piece and neck region of the tail but is also found in the acrosomal region in a small percentage of sperm cells. Expressed in natural regulatory T cells (nTregs) and a subset of early thymocyte progenitor double-negative 1 (DN1) cells. Expressed in memory B cells. Expressed by IL17 producing helper T-cells (Th17), type 1 effector cells (Th1), type 2 effector cells (Th2) and regulatory T-cells (Treg) (at protein level). Expressed by Th17 cells in spleen, Peyers patches, and lamina propria of small and large intestine. Highly expressed in testis, lung, colon, and dendritic cells. {ECO:0000269|PubMed:19050256, ECO:0000269|PubMed:19129757, ECO:0000269|PubMed:23765988, ECO:0000269|PubMed:24638065, ECO:0000269|PubMed:25505290}. +P51944 CCNF_MOUSE Cyclin-F 777 86,623 Alternative sequence (2); Chain (1); Domain (2); Motif (2); Region (1); Sequence conflict (36) FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of CP110 during G2 phase, thereby acting as an inhibitor of centrosome reduplication. {ECO:0000250}. PTM: Degraded when the spindle assembly checkpoint is activated during the G2-M transition. Degradation is not dependent on the proteasome or ubiquitin and depends on the C-terminal PEST sequence (By similarity). {ECO:0000250}.; PTM: Phosphorylated just before cells enter into mitosis. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250}. Note=Localization in the centrosome is rare in S phase cells and increases in G2 cells, Localizes on both the mother and daughter centrioles. Localization to centrosomes is not dependent on CP110. Also localizes to the nucleus (By similarity). {ECO:0000250}. SUBUNIT: Component of the SCF(CCNF) complex consisting of CUL1, RBX1, SKP1 and CCNF. Interacts with CCNB1; interaction is required for nuclear localization of CCNB1. Interacts with CCP110; this interaction leads to CCP110 ubiquitination and degradation via the proteasome pathway (By similarity). {ECO:0000250}. DOMAIN: The nuclear localization signals mediate the localization to the nucleus and are required for CCNB1 localization to the nucleus. {ECO:0000250}. +Q3U1D9 CD047_MOUSE UPF0602 protein C4orf47 homolog 316 35,260 Chain (1) SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:A7E2U8}. +Q9DCG2 CD302_MOUSE CD302 antigen (C-type lectin domain family 13 member A) (Type I transmembrane C-type lectin receptor DCL-1) (CD antigen CD302) 228 25,423 Alternative sequence (1); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 166 186 Helical. {ECO:0000255}. TOPO_DOM 21 165 Extracellular. {ECO:0000255}.; TOPO_DOM 187 228 Cytoplasmic. {ECO:0000255}. FUNCTION: Potential multifunctional C-type lectin receptor that may play roles in endocytosis and phagocytosis as well as in cell adhesion and migration. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Cell projection, filopodium {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Cell projection, microvillus {ECO:0000250}. Note=Colocalizes with F-actin in filopodia, cellular cortex and microvilli of the apical cell surface. {ECO:0000250}. +Q9Z1P5 CD320_MOUSE CD320 antigen (Transcobalamin receptor) (TCblR) (CD antigen CD320) 260 27,739 Alternative sequence (1); Chain (1); Disulfide bond (6); Domain (2); Glycosylation (2); Metal binding (12); Sequence caution (1); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 209 229 Helical. {ECO:0000255}. TOPO_DOM 29 208 Extracellular. {ECO:0000255}.; TOPO_DOM 230 260 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for transcobalamin saturated with cobalamin (TCbl). Plays an important role in cobalamin uptake. Plasma membrane protein that is expressed on follicular dendritic cells (FDC) and mediates interaction with germinal center B cells. Functions as costimulator to promote B cell responses to antigenic stimuli; promotes B cell differentiation and proliferation. Germinal center-B (GC-B) cells differentiate into memory B-cells and plasma cells (PC) through interaction with T-cells and follicular dendritic cells (FDC). CD320 augments the proliferation of PC precursors generated by IL-10. {ECO:0000250|UniProtKB:Q9NPF0}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9NPF0}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9NPF0}. SUBUNIT: Interacts (via LDL-receptor class A domains) with TCN2. {ECO:0000250|UniProtKB:Q9NPF0}. +P19437 CD20_MOUSE B-lymphocyte antigen CD20 (B-cell differentiation antigen Ly-44) (Lymphocyte antigen 44) (Membrane-spanning 4-domains subfamily A member 1) (CD antigen CD20) 291 31,958 Chain (1); Lipidation (1); Modified residue (3); Topological domain (5); Transmembrane (4) TRANSMEM 45 65 Helical. {ECO:0000255}.; TRANSMEM 69 89 Helical. {ECO:0000255}.; TRANSMEM 112 132 Helical. {ECO:0000255}.; TRANSMEM 183 203 Helical. {ECO:0000255}. TOPO_DOM 1 44 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 66 68 Extracellular. {ECO:0000255}.; TOPO_DOM 90 111 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 133 182 Extracellular. {ECO:0000255}.; TOPO_DOM 204 291 Cytoplasmic. {ECO:0000255}. FUNCTION: This protein may be involved in the regulation of B-cell activation and proliferation. PTM: Phosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein. Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. SUBUNIT: Homotrimer. {ECO:0000269|PubMed:8450218}. +Q8CII2 CD123_MOUSE Cell division cycle protein 123 homolog 336 38,816 Alternative sequence (2); Chain (1); Modified residue (1); Sequence conflict (1) FUNCTION: Required for S phase entry of the cell cycle. {ECO:0000250}. PTM: Phosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +Q64389 CD52_MOUSE CAMPATH-1 antigen (Lymphocyte differentiation antigen B7) (CD antigen CD52) 74 7,798 Glycosylation (1); Lipidation (1); Peptide (1); Propeptide (1); Signal peptide (1) FUNCTION: May play a role in carrying and orienting carbohydrate, as well as having a more specific role. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. TISSUE SPECIFICITY: Expressed on lymphohematopoietic tissues, including thymus, spleen, and bone marrow, but not in liver, kidney, and brain. +P10810 CD14_MOUSE Monocyte differentiation antigen CD14 (Myeloid cell-specific leucine-rich glycoprotein) (CD antigen CD14) 366 39,204 Beta strand (15); Chain (1); Disulfide bond (4); Glycosylation (5); Helix (7); Lipidation (1); Propeptide (1); Region (1); Repeat (11); Signal peptide (1); Turn (3) FUNCTION: Coreceptor for bacterial lipopolysaccharide. In concert with LBP, binds to monomeric lipopolysaccharide and delivers it to the LY96/TLR4 complex, thereby mediating the innate immune response to bacterial lipopolysaccharide (LPS) (PubMed:16148141). Acts via MyD88, TIRAP and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (PubMed:8612135, PubMed:15895089). Acts as a coreceptor for TLR2:TLR6 heterodimer in response to diacylated lipopeptides and for TLR2:TLR1 heterodimer in response to triacylated lipopeptides, these clusters trigger signaling from the cell surface and subsequently are targeted to the Golgi in a lipid-raft dependent pathway (By similarity). Acts as an accessory receptor for M.tuberculosis lipoproteins LprA, LprG and LpqH, in conjunction with coreceptors TLR2 and TLR1. The lipoproteins act as agonists to modulate antigen presenting cell functions in response to the pathogen (PubMed:19362712). Binds electronegative LDL (LDL(-)) and mediates the cytokine release induced by LDL(-) (By similarity). {ECO:0000250|UniProtKB:P08571, ECO:0000269|PubMed:15895089, ECO:0000269|PubMed:16148141, ECO:0000269|PubMed:19362712, ECO:0000269|PubMed:21821728, ECO:0000269|PubMed:8612135}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21821728, ECO:0000269|PubMed:8612135}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P08571}. Secreted {ECO:0000250|UniProtKB:P08571}. Membrane raft {ECO:0000250|UniProtKB:P08571}. Golgi apparatus {ECO:0000250|UniProtKB:P08571}. Note=Soluble, secreted forms seem to exist. They may arise by cleavage of the GPI anchor. {ECO:0000250|UniProtKB:P08571}. SUBUNIT: Belongs to the lipopolysaccharide (LPS) receptor, a multi-protein complex containing at least CD14, LY96 and TLR4 (By similarity). Interacts with LPS-bound LPB. Interacts with LPAR1 (PubMed:21821728). Interacts with the TLR2:TLR6 or TLR2:TLR1 heterodimers; upon interaction with ligands such as diacylated lipopeptides and triacylated lipopeptides, respectively. Interacts with MYO18A (By similarity). {ECO:0000250|UniProtKB:P08571, ECO:0000269|PubMed:21821728}. DOMAIN: The C-terminal leucine-rich repeat (LRR) region is required for responses to smooth LPS. {ECO:0000269|PubMed:15895089}. TISSUE SPECIFICITY: Detected on peritoneal macrophages (at protein level) (PubMed:8612135). Cell surface expression detected in lung alveolar macrophages, dendritic macrophages and lung macrophages (at protein level) (PubMed:19362712). {ECO:0000269|PubMed:19362712, ECO:0000269|PubMed:8612135}. +Q00609 CD80_MOUSE T-lymphocyte activation antigen CD80 (Activation B7-1 antigen) (B7) (CD antigen CD80) 306 34,590 Alternative sequence (1); Beta strand (9); Chain (1); Disulfide bond (2); Domain (2); Glycosylation (6); Helix (2); Region (1); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (3) TRANSMEM 247 268 Helical. {ECO:0000255}. TOPO_DOM 38 246 Extracellular. {ECO:0000255}.; TOPO_DOM 269 306 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in the costimulatory signal essential for T lymphocytes activation. T-cell proliferation and cytokine production is induced by the binding of CD28 or CTLA-4 to this receptor. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. TISSUE SPECIFICITY: Expressed on activated B-cells, gamma interferon stimulated monocytes and non-circulating B-cell malignancies. +Q8CC12 CDAN1_MOUSE Codanin-1 1239 135,883 Alternative sequence (2); Chain (1); Compositional bias (1); Erroneous gene model prediction (1); Frameshift (1); Initiator methionine (1); Modified residue (3); Region (1); Sequence conflict (2); Transmembrane (2) TRANSMEM 317 337 Helical. {ECO:0000255}.; TRANSMEM 631 651 Helical. {ECO:0000255}. FUNCTION: May act as a negative regulator of ASF1 in chromatin assembly. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=Mainly detected as a cytoplasmic protein. SUBUNIT: Interacts with ASF1A and ASF1B. Found in a cytosolic complex with ASF1A, ASF1B, IPO4 and histones H3.1 and H4. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed in adult mice, the highest levels can be measured in erythropoietic cells. {ECO:0000269|PubMed:21364188}. +Q9JLQ0 CD2AP_MOUSE CD2-associated protein (Mesenchyme-to-epithelium transition protein with SH3 domains 1) (METS-1) 637 70,450 Beta strand (17); Chain (1); Coiled coil (1); Compositional bias (1); Cross-link (2); Domain (3); Helix (2); Modified residue (9); Motif (3); Region (1); Sequence conflict (12); Turn (1) FUNCTION: Seems to act as an adapter protein between membrane proteins and the actin cytoskeleton (By similarity). In collaboration with CBLC, modulates the rate of RET turnover and may act as regulatory checkpoint that limits the potency of GDNF on neuronal survival. Controls CBLC function, converting it from an inhibitor to a promoter of RET degradation (By similarity). May play a role in receptor clustering and cytoskeletal polarity in the junction between T-cell and antigen-presenting cell (PubMed:9741631). May anchor the podocyte slit diaphragm to the actin cytoskeleton in renal glomerolus (PubMed:10514378). Also required for cytokinesis. Plays a role in epithelial cell junctions formation (By similarity). {ECO:0000250|UniProtKB:F1LRS8, ECO:0000250|UniProtKB:Q9Y5K6, ECO:0000269|PubMed:10514378, ECO:0000269|PubMed:9741631}. PTM: Phosphorylated on tyrosine residues; probably by c-Abl, Fyn and c-Src. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9Y5K6}. Cell projection, ruffle {ECO:0000250|UniProtKB:Q9Y5K6}. Cell junction {ECO:0000250|UniProtKB:Q9Y5K6}. Note=Colocalizes with F-actin and BCAR1/p130Cas in membrane ruffles (By similarity). Located at podocyte slit diaphragm between podocyte foot processes (PubMed:10514378, PubMed:11733379). During late anaphase and telophase, concentrates in the vicinity of the midzone microtubules and in the midbody in late telophase (By similarity). {ECO:0000250|UniProtKB:Q9Y5K6, ECO:0000269|PubMed:10514378, ECO:0000269|PubMed:11733379}. SUBUNIT: Homodimer. Interacts with F-actin, PKD2, NPHS1 and NPHS2. Interacts with WTIP. Interacts with DDN; interaction is direct. Interacts (via SH3 2 domain) with CBL (via phosphorylated C-terminus). Interacts with BCAR1/p130Cas (via SH3 domain). Interacts with MVB12A and ARHGAP17. Interacts with ANLN, CD2 and CBLB. Interacts with PDCD6IP and TSG101. Interacts with RIN3. Interacts directly with RET (inactive) and CBLC; upon RET activation by GDNF suggested to dissociate from RET as CBLC:CD2AP complex. Interacts with CGNL1 and SH3BP1; probably part of a complex at cell junctions. Interacts with CAPZA1. {ECO:0000250|UniProtKB:Q9Y5K6, ECO:0000269|PubMed:10514378, ECO:0000269|PubMed:10913159, ECO:0000269|PubMed:11733379, ECO:0000269|PubMed:11733557, ECO:0000269|PubMed:12217865, ECO:0000269|PubMed:14736876, ECO:0000269|PubMed:17537921, ECO:0000269|PubMed:18753381, ECO:0000269|PubMed:9741631, ECO:0000305}. DOMAIN: Potential homodimerization is mediated by the coiled coil domain. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in podocytes (at protein level). {ECO:0000269|PubMed:18753381}. +P15539 C11B2_MOUSE Cytochrome P450 11B2, mitochondrial (Aldosterone synthase) (CYPXIB2) (Cytochrome P450C11) (Steroid 11-beta-hydroxylase) (EC 1.14.15.4) (EC 1.14.15.5) 500 57,373 Chain (1); Metal binding (1); Sequence conflict (1); Transit peptide (1) FUNCTION: Forms corticosterone from 11-deoxycorticosterone. SUBCELLULAR LOCATION: Mitochondrion membrane. +Q9Z1L5 CA2D3_MOUSE Voltage-dependent calcium channel subunit alpha-2/delta-3 (Voltage-gated calcium channel subunit alpha-2/delta-3) [Cleaved into: Voltage-dependent calcium channel subunit alpha-2-3; Voltage-dependent calcium channel subunit delta-3] 1091 122,778 Chain (3); Disulfide bond (1); Domain (2); Glycosylation (4); Metal binding (3); Modified residue (1); Motif (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1069 1089 Helical. {ECO:0000255}. TOPO_DOM 34 1068 Extracellular. {ECO:0000255}.; TOPO_DOM 1090 1091 Cytoplasmic. {ECO:0000255}. FUNCTION: The alpha-2/delta subunit of voltage-dependent calcium channels regulates calcium current density and activation/inactivation kinetics of the calcium channel. Acts as a regulatory subunit for P/Q-type calcium channel (CACNA1A), N-type (CACNA1B), L-type (CACNA1C OR CACNA1D) but not T-type (CACNA1G). {ECO:0000269|PubMed:10200414, ECO:0000269|PubMed:9880589}. PTM: N-glycosylated. {ECO:0000269|PubMed:11306709}.; PTM: May be proteolytically processed into subunits alpha-2-3 and delta-3 that are disulfide-linked. It is however unclear whether such cleavage really takes place in vivo and has a functional role. {ECO:0000269|PubMed:11306709}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Dimer formed of alpha-2-2 and delta-2 chains; disulfide-linked. Voltage-dependent calcium channels are multisubunit complexes, consisting of alpha-1 (CACNA1), alpha-2 (CACNA2D), beta (CACNB) and delta (CACNA2D) subunits in a 1:1:1:1 ratio (By similarity). {ECO:0000250}. DOMAIN: The MIDAS-like motif in the VWFA domain binds divalent metal cations and is required to promote trafficking of the alpha-1 (CACNA1) subunit to the plasma membrane by an integrin-like switch. {ECO:0000250}. TISSUE SPECIFICITY: Brain-specific. Predominantly expressed in the caudate putamen, entorhinal complex, hippocampus and cortex. {ECO:0000269|PubMed:11687876, ECO:0000269|PubMed:9880589}. +Q80WR5 CA174_MOUSE UPF0688 protein C1orf174 homolog 230 24,774 Chain (1); Erroneous gene model prediction (1); Modified residue (1); Sequence conflict (1) SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +Q9QX15 CA3A1_MOUSE Calcium-activated chloride channel regulator 3A-1 (EC 3.4.-.-) 902 100,108 Active site (1); Chain (1); Domain (1); Glycosylation (8); Metal binding (3); Region (1); Sequence conflict (9); Signal peptide (1); Site (1) FUNCTION: Plays a role in modulating chloride current across the plasma membrane in a calcium-dependent manner. {ECO:0000269|PubMed:10072771, ECO:0000269|PubMed:9822685}. PTM: Glycosylated. {ECO:0000269|PubMed:9822685}.; PTM: The 130-kDa product is autoproteolytically processed by the metalloprotease domain and yields two subunits, a 90-kDa protein and a group of 32- to 38-kDa proteins (PubMed:9822685). The cleavage is necessary for calcium-activated chloride channel (CaCC) activation activity (By similarity). {ECO:0000250|UniProtKB:A8K7I4, ECO:0000269|PubMed:9822685}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Highly expressed in skin and spleen, and at lower levels in kidney and liver (PubMed:9822685, PubMed:10072771). Also detected in lung and brain (PubMed:9822685). Not detected in lung or brain (PubMed:10072771). In lung, localizes to respiratory epithelia of the bronchi and trachea and the submucosal glands (PubMed:9822685). {ECO:0000269|PubMed:10072771, ECO:0000269|PubMed:9822685}. +Q9D9D9 CA189_MOUSE Uncharacterized protein C1orf189 homolog 101 12,258 Chain (1); Erroneous initiation (2) +Q8C3W1 CA198_MOUSE Uncharacterized protein C1orf198 homolog 322 35,316 Chain (1); Initiator methionine (1); Modified residue (4); Sequence conflict (3) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +Q8BP99 CA216_MOUSE UPF0500 protein C1orf216 homolog 230 25,232 Chain (1); Sequence conflict (1) +Q8CC27 CACB2_MOUSE Voltage-dependent L-type calcium channel subunit beta-2 (CAB2) (Calcium channel voltage-dependent subunit beta 2) 655 73,149 Alternative sequence (3); Chain (1); Domain (1); Modified residue (5); Sequence conflict (1); Site (1) FUNCTION: The beta subunit of voltage-dependent calcium channels contributes to the function of the calcium channel by increasing peak calcium current, shifting the voltage dependencies of activation and inactivation, modulating G protein inhibition and controlling the alpha-1 subunit membrane targeting. {ECO:0000250, ECO:0000269|PubMed:14674701}. PTM: Regulated through phosphorylation at Thr-549 by CaMK2D. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. SUBUNIT: Component of a calcium channel complex consisting of a pore-forming alpha subunit (CACNA1S) and the ancillary subunits CACNB1 or CACNB2, CACNG1 and CACNA2D1. The channel complex contains alpha, beta, gamma and delta subunits in a 1:1:1:1 ratio, i.e. it contains either CACNB1 or CACNB2. Interacts with CACNA1C (By similarity). Interacts with RRAD. Interaction with RRAD regulates the trafficking of CACNA1C to the cell membrane. Interacts with TMIGD2 (By similarity). Interacts with CAMK2D (By similarity). Interacts with CBARP (PubMed:24751537). Interacts with CAMK2A (By similarity). {ECO:0000250|UniProtKB:Q08289, ECO:0000250|UniProtKB:Q8VGC3, ECO:0000269|PubMed:24751537}. +P61215 CAH10_MOUSE Carbonic anhydrase-related protein 10 (Carbonic anhydrase-related protein X) (CA-RP X) (CARP X) 328 37,563 Chain (1); Domain (1) FUNCTION: Does not have a catalytic activity. +P23589 CAH5A_MOUSE Carbonic anhydrase 5A, mitochondrial (EC 4.2.1.1) (Carbonate dehydratase VA) (CA Y) (Carbonic anhydrase VA) (CA-VA) 299 34,072 Active site (3); Beta strand (16); Chain (1); Domain (1); Helix (7); Metal binding (3); Modified residue (1); Mutagenesis (7); Natural variant (1); Region (1); Transit peptide (1); Turn (1) FUNCTION: Reversible hydration of carbon dioxide. Low activity. SUBCELLULAR LOCATION: Mitochondrion. TISSUE SPECIFICITY: Liver. +O35887 CALU_MOUSE Calumenin (Crocalbin) 315 37,064 Calcium binding (6); Chain (1); Domain (6); Glycosylation (1); Modified residue (7); Motif (1); Signal peptide (1) FUNCTION: Involved in regulation of vitamin K-dependent carboxylation of multiple N-terminal glutamate residues. Seems to inhibit gamma-carboxylase GGCX. Binds 7 calcium ions with a low affinity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O43852}. Golgi apparatus {ECO:0000250|UniProtKB:O43852}. Secreted {ECO:0000250|UniProtKB:O43852}. Melanosome {ECO:0000250|UniProtKB:O43852}. Sarcoplasmic reticulum lumen {ECO:0000250|UniProtKB:O43852}. SUBUNIT: Interacts with GGCX. {ECO:0000250}. +O08529 CAN2_MOUSE Calpain-2 catalytic subunit (EC 3.4.22.53) (80 kDa M-calpain subunit) (CALP80) (Calcium-activated neutral proteinase 2) (CANP 2) (Calpain M-type) (Calpain-2 large subunit) (Millimolar-calpain) (M-calpain) 700 79,872 Active site (3); Calcium binding (2); Chain (1); Domain (3); Initiator methionine (1); Metal binding (26); Modified residue (1); Propeptide (1); Region (3); Sequence conflict (3) FUNCTION: Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Proteolytically cleaves MYOC at 'Arg-226' (By similarity). Proteolytically cleaves CPEB3 following neuronal stimulation which abolishes CPEB3 translational repressor activity, leading to translation of CPEB3 target mRNAs (PubMed:22711986). {ECO:0000250|UniProtKB:P17655, ECO:0000269|PubMed:22711986}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Translocates to the plasma membrane upon Ca(2+) binding. {ECO:0000250}. SUBUNIT: Forms a heterodimer with a small (regulatory) subunit (CAPNS1) (By similarity). Interacts with CPEB3; this leads to cleavage of CPEB3 (PubMed:22711986). {ECO:0000250|UniProtKB:Q07009, ECO:0000269|PubMed:22711986}. TISSUE SPECIFICITY: Ubiquitous. +Q6J756 CAN11_MOUSE Calpain-11 (EC 3.4.22.-) (Calcium-activated neutral proteinase 11) (CANP 11) 714 82,970 Active site (3); Calcium binding (2); Chain (1); Domain (3); Region (3) FUNCTION: Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. {ECO:0000250|UniProtKB:Q9UMQ6}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:16541461}. SUBUNIT: Heterodimer of a large (catalytic) and a small (regulatory) subunit. {ECO:0000250|UniProtKB:Q9UMQ6}. TISSUE SPECIFICITY: Expressed exclusively in testis, where it is restricted to spermatocytes and during the later stages of meiosis (at protein level). {ECO:0000269|PubMed:10559499, ECO:0000269|PubMed:16541461}. +Q64691 CAN3_MOUSE Calpain-3 (EC 3.4.22.54) (Calcium-activated neutral proteinase 3) (CANP 3) (Calpain L3) (Calpain p94) (Muscle-specific calcium-activated neutral protease 3) 821 94,242 Active site (3); Alternative sequence (2); Calcium binding (4); Chain (1); Domain (5); Region (3); Sequence conflict (2) FUNCTION: Calcium-regulated non-lysosomal thiol-protease. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Homodimer; via EF-hand domain 4. Interacts with TTN/titin. Interacts with CMYA5; this interaction, which results in CMYA5 proteolysis, may protect CAPN3 from autolysis. {ECO:0000250|UniProtKB:P20807}. +Q9D805 CAN9_MOUSE Calpain-9 (EC 3.4.22.-) (Digestive tract-specific calpain) (New calpain 4) (nCL-4) 690 78,977 Active site (3); Calcium binding (2); Chain (1); Domain (4); Metal binding (9); Region (2); Sequence conflict (2) FUNCTION: Calcium-regulated non-lysosomal thiol-protease. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. TISSUE SPECIFICITY: Predominantly expressed in stomach and small intestine, although low levels of expression in other organs. +Q8CIS0 CAR11_MOUSE Caspase recruitment domain-containing protein 11 1159 134,040 Alternative sequence (1); Chain (1); Coiled coil (1); Compositional bias (1); Domain (3); Erroneous initiation (1); Helix (7); Modified residue (10); Sequence conflict (2); Turn (1) FUNCTION: Involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation (PubMed:12356734, PubMed:16356855). Its binding to DPP4 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. Activates NF-kappa-B via BCL10 and IKK. Stimulates the phosphorylation of BCL10. Also activates the TORC1 signaling pathway (By similarity). {ECO:0000250|UniProtKB:Q9BXL7, ECO:0000269|PubMed:12356734, ECO:0000269|PubMed:16356855}. PTM: Phosphorylation at Ser-564, Ser-649 and Ser-657 by PRKCB and PRKCQ leads to a shift from an inactive to an active form that activates the NF-kappa-B signaling. {ECO:0000269|PubMed:16356855}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BXL7}. Membrane raft {ECO:0000250|UniProtKB:Q9BXL7}. Note=Colocalized with DPP4 in membrane rafts. {ECO:0000250|UniProtKB:Q9BXL7}. SUBUNIT: Found in a membrane raft complex, at least composed of BCL10, CARD11, DPP4 and IKBKB. CARD11 and BCL10 bind to each other by CARD-CARD interaction. Interacts (via PDZ domain) with DPP4 (via cytoplasmic tail). Interacts with BCL10; as part of a CBM (CARD11-BCL10-MALT1) complex involved in NF-kappa-B activation. {ECO:0000250|UniProtKB:Q9BXL7}. +O89094 CASPE_MOUSE Caspase-14 (CASP-14) (EC 3.4.22.-) (Mini-ICE) (MICE) [Cleaved into: Caspase-14 subunit p17, mature form; Caspase-14 subunit p10, mature form; Caspase-14 subunit p20, intermediate form; Caspase-14 subunit p8, intermediate form] 257 29,458 Active site (2); Alternative sequence (2); Chain (4); Mutagenesis (1); Propeptide (2) FUNCTION: Non-apoptotic caspase which is involved in epidermal differentiation. Seems to play a role in keratinocyte differentiation and is required for cornification (PubMed:18156206). Regulates maturation of the epidermis by proteolytically processing filaggrin (PubMed:21654840). In vitro is equally active on the synthetic caspase substrates WEHD-ACF and IETD-AFC. Involved in processing of prosaposin in the epidermis (PubMed:24872419). May be involved in retinal pigment epithelium cell barrier function (By similarity). {ECO:0000250|UniProtKB:P31944, ECO:0000269|PubMed:11175259, ECO:0000269|PubMed:17515931, ECO:0000269|PubMed:18156206, ECO:0000269|PubMed:21654840, ECO:0000269|PubMed:24872419}. PTM: Maturation by proteolytic processing appears to be a two-step process. The precursor is processed by KLK7 to yield the p20/p8 intermediate form which acts the precursor to yield the p17/p10 mature form (By similarity). Initially it was reported that cleavage by granzyme B, caspase-8 and -10 generates the two active subunits, however the physiological relevance has not been established (PubMed:9823333). {ECO:0000250|UniProtKB:P31944, ECO:0000305|PubMed:9823333}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11175259}. Nucleus {ECO:0000269|PubMed:11175259}. SUBUNIT: Heterodimer of a large and a small subunit, both processed from the precursor; the mature active form is a p17/p10 dimer and the intermediate form a p20/p8 dimer. {ECO:0000250|UniProtKB:P31944}. TISSUE SPECIFICITY: Embryo, adult liver and less in adult brain and kidney. Expressed in differentiating keratinocytes of embryonic skin (at protein level). Expressed in keratinocytes of adult skin suprabasal layers (at protein level). {ECO:0000269|PubMed:10203698, ECO:0000269|PubMed:11175259}. +P97864 CASP7_MOUSE Caspase-7 (CASP-7) (EC 3.4.22.60) (Apoptotic protease Mch-3) (Cysteine protease LICE2) [Cleaved into: Caspase-7 subunit p20; Caspase-7 subunit p11] 303 34,061 Active site (2); Chain (2); Erroneous initiation (1); Modified residue (1); Propeptide (2); Sequence conflict (3) FUNCTION: Involved in the activation cascade of caspases responsible for apoptosis execution. Cleaves and activates sterol regulatory element binding proteins (SREBPs). Overexpression promotes programmed cell death (By similarity). {ECO:0000250}. PTM: Cleavages by granzyme B or caspase-10 generate the two active subunits. Propeptide domains can also be cleaved efficiently by caspase-3. Active heterodimers between the small subunit of caspase-7 and the large subunit of caspase-3, and vice versa, also occur (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a 20 kDa (p20) and a 11 kDa (p11) subunit. Interacts with BIRC6/bruce (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in heart, lung, liver and kidney. Low levels in spleen, skeletal muscle and testis. No expression in the brain. +Q9WUU7 CATZ_MOUSE Cathepsin Z (EC 3.4.18.1) 306 33,996 Active site (3); Chain (1); Disulfide bond (5); Glycosylation (2); Propeptide (1); Signal peptide (1) FUNCTION: Exhibits carboxy-monopeptidase as well as carboxy-dipeptidase activity. {ECO:0000250}. SUBCELLULAR LOCATION: Lysosome. TISSUE SPECIFICITY: Ubiquitous. +Q9JIA9 CATR_MOUSE Cathepsin R (EC 3.4.22.-) 334 37,421 Active site (3); Chain (1); Disulfide bond (3); Glycosylation (1); Propeptide (1); Signal peptide (1) SUBCELLULAR LOCATION: Lysosome {ECO:0000305}. TISSUE SPECIFICITY: Placenta. {ECO:0000269|PubMed:11004518}. +P47754 CAZA2_MOUSE F-actin-capping protein subunit alpha-2 (CapZ alpha-2) 286 32,967 Chain (1); Initiator methionine (1); Modified residue (2) FUNCTION: F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. SUBUNIT: Heterodimer of an alpha and a beta subunit. Component of the WASH complex, composed of F-actin-capping protein subunit alpha (CAPZA1, CAPZA2 or CAPZA3), F-actin-capping protein subunit beta (CAPZB), WASHC1, WASHC2, WASHC3, WASHC4 and WASHC5. Interacts with RCSD1/CAPZIP (By similarity). {ECO:0000250}. +P47753 CAZA1_MOUSE F-actin-capping protein subunit alpha-1 (CapZ alpha-1) 286 32,940 Chain (1); Initiator methionine (1); Modified residue (4); Sequence conflict (1) FUNCTION: F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. May play a role in the formation of epithelial cell junctions. {ECO:0000250|UniProtKB:P52907}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. SUBUNIT: Heterodimer of an alpha and a beta subunit. Component of the WASH complex, composed of F-actin-capping protein subunit alpha (CAPZA1, CAPZA2 or CAPZA3), F-actin-capping protein subunit beta (CAPZB), WASHC1, WASHC2, WASHC3, WASHC4 and WASHC5. Interacts with S100B and S100A. Interacts with SH3BP1; recruits CAPZA1 to forming cell junctions. Interacts with CD2AP. {ECO:0000250|UniProtKB:P52907}. +A0JLY1 CC173_MOUSE Coiled-coil domain-containing protein 173 547 65,132 Chain (1); Coiled coil (3) +P08074 CBR2_MOUSE Carbonyl reductase [NADPH] 2 (EC 1.1.1.184) (Adipocyte protein P27) (AP27) (Lung carbonyl reductase) (LCR) (NADPH-dependent carbonyl reductase 2) 244 25,958 Active site (1); Beta strand (7); Binding site (1); Chain (1); Helix (14); Modified residue (2); Mutagenesis (1); Nucleotide binding (1) FUNCTION: May function in the pulmonary metabolism of endogenous carbonyl compounds, such as aliphatic aldehydes and ketones derived from lipid peroxidation, 3-ketosteroids and fatty aldehydes, as well as in xenobiotic metabolism. {ECO:0000269|PubMed:7705352}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:8040004}. SUBUNIT: Homotetramer. {ECO:0000269|PubMed:8805511}. TISSUE SPECIFICITY: Lung (ciliated cells, non-ciliated bronchiolar cells and type-II alveolar pneumocytes). Low expression in adipose tissue > testis = heart > kidney = spleen > brain = liver. +P86792 CC21B_MOUSE C-C motif chemokine 21b (6Ckine) (Beta-chemokine exodus-2) (Small-inducible cytokine A21b) (Thymus-derived chemotactic agent 4) (TCA4) 133 14,584 Chain (1); Disulfide bond (3); Region (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Inhibits hemopoiesis and stimulates chemotaxis. Chemotactic in vitro for thymocytes and activated T-cells, but not for B-cells, macrophages, or neutrophils. Potent mesangial cell chemoattractant. Shows preferential activity towards naive T-cells. May play a role in mediating homing of lymphocytes to secondary lymphoid organs. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Binds to CCR7 and to CXCR3. Interacts with PDPN; relocalizes PDPN to the basolateral membrane. {ECO:0000250|UniProtKB:O00585}. TISSUE SPECIFICITY: Expressed strongly in lung, spleen, thymus, peripheral and mesentric lymph nodes. Also expressed in the testis, kidney, liver, and heart. +Q8C4J0 CCD60_MOUSE Coiled-coil domain-containing protein 60 545 62,969 Alternative sequence (2); Chain (1); Coiled coil (1) +Q8VC31 CCDC9_MOUSE Coiled-coil domain-containing protein 9 543 61,445 Chain (1); Coiled coil (2); Compositional bias (4); Modified residue (14) +Q8VHW4 CCG5_MOUSE Voltage-dependent calcium channel gamma-5 subunit (Neuronal voltage-gated calcium channel gamma-5 subunit) (Transmembrane AMPAR regulatory protein gamma-5) (TARP gamma-5) 275 30,894 Chain (1); Transmembrane (4) TRANSMEM 8 28 Helical. {ECO:0000255}.; TRANSMEM 103 123 Helical. {ECO:0000255}.; TRANSMEM 129 149 Helical. {ECO:0000255}.; TRANSMEM 181 201 Helical. {ECO:0000255}. FUNCTION: Regulates the gating properties of AMPA-selective glutamate receptors (AMPARs). Modulates their gating properties by accelerating their rates of activation, deactivation and desensitization. Displays subunit-specific AMPA receptor regulation. Shows specificity for GRIA1, GRIA4 and the long isoform of GRIA2. Thought to stabilize the calcium channel in an inactivated (closed) state (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250}. SUBUNIT: The L-type calcium channel is composed of five subunits: alpha-1, alpha-2/delta, beta and gamma. Acts as an auxiliary subunit for AMPA-selective glutamate receptors (AMPARs). Found in a complex with GRIA1, GRIA2, GRIA3, GRIA4, CNIH2, CNIH3, CACNG2, CACNG3, CACNG4, CACNG7 and CACNG8. Interacts with GRIA1, GRIA2, GRIA3 and GRIA4 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Brain. Enriched in Bergman glia, as well as a variety of neuronal populations including locus coeruleus, olfactory bulb, lateral septal nucleus, interpeduncular nucleus,and the CA2 and rostral/medial CA1 regions of hippocampus. {ECO:0000269|PubMed:18817736}. +Q8CE72 CPLN1_MOUSE Ciliogenesis and planar polarity effector 1 (Protein C5orf42 homolog) (Protein JBTS17) 3214 358,550 Chain (1); Erroneous initiation (1); Natural variant (1); Sequence caution (1); Sequence conflict (1); Transmembrane (2) TRANSMEM 593 613 Helical. {ECO:0000255}.; TRANSMEM 632 652 Helical. {ECO:0000255}. FUNCTION: Involved in ciliogenesis. Involved in the establishment of cell polarity required for directional cell migration (PubMed:25877302). Proposed to act in association with the CPLANE (ciliogenesis and planar polarity effectors) complex. Involved in recruitment of peripheral IFT-A proteins to basal bodies (PubMed:27158779). {ECO:0000269|PubMed:25877302, ECO:0000305|PubMed:27158779}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cell projection, cilium {ECO:0000269|PubMed:25877302}. Note=Localizes to the ciliary transition zone. {ECO:0000269|PubMed:25877302}. SUBUNIT: Interacts with FUZ; INTU and WDPCP; the interactors are proposed to form the core CPLANE (ciliogenesis and planar polarity effectors) complex (PubMed:27158779). DISEASE: Note=Defects in Jbts17 are the cause of the Hug (Heart under glass) phenotype which is a model of Joubert syndrome. Hug mice die prenatally and show skelatal dysplasia, craniofacial defects, polydactyly, cystic kidney, cerebellar hypoplasia and congenital heart defects of varying degrees. Most severely affected mutants die at mid-gestation with a transparent chest wall due to complete failure to form the rib cage. The phenotype is consistent with the spectrum of MKS-BBS-Joubert syndrome phenotypes. {ECO:0000269|PubMed:25877302}. +Q5ND19 CQ047_MOUSE Uncharacterized protein C17orf47 homolog 536 59,211 Chain (1); Compositional bias (2) +Q32P12 CQ053_MOUSE Uncharacterized protein C17orf53 homolog 615 66,063 Alternative sequence (1); Chain (1); Modified residue (1); Sequence conflict (2) +O88543 CSN3_MOUSE COP9 signalosome complex subunit 3 (SGN3) (Signalosome subunit 3) (JAB1-containing signalosome subunit 3) 423 47,832 Chain (1); Domain (1); Initiator methionine (1); Modified residue (4) FUNCTION: Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. Essential to maintain the survival of epiblast cells and thus the development of the postimplantation embryo. {ECO:0000269|PubMed:12972600}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Component of the CSN complex, composed of COPS1/GPS1, COPS2, COPS3, COPS4, COPS5, COPS6, COPS7 (COPS7A or COPS7B), COPS8 and COPS9 (PubMed:9707402). In the complex, it probably interacts directly with COPS1, COPS4, COPS8 and COPS9. Interacts with CK2 and PKD. Interacts with the translation initiation factor EIF3S6 and IKBKG (By similarity). {ECO:0000250|UniProtKB:Q9UNS2, ECO:0000269|PubMed:9707402}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12972600}. +O35864 CSN5_MOUSE COP9 signalosome complex subunit 5 (SGN5) (Signalosome subunit 5) (EC 3.4.-.-) (Jun activation domain-binding protein 1) (Kip1 C-terminus-interacting protein 2) 334 37,549 Chain (1); Domain (1); Initiator methionine (1); Metal binding (3); Modified residue (1); Motif (1); Mutagenesis (1) FUNCTION: Probable protease subunit of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of the SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. Promotes the proteasomal degradation of BRSK2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. In the complex, it probably acts as the catalytic center that mediates the cleavage of Nedd8 from cullins. It however has no metalloprotease activity by itself and requires the other subunits of the CSN complex. Interacts directly with a large number of proteins that are regulated by the CSN complex, confirming a key role in the complex. {ECO:0000250|UniProtKB:Q92905}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10721695}. Nucleus {ECO:0000269|PubMed:10721695}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q92905}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250|UniProtKB:Q92905}. Note=Nuclear localization is diminished in the presence of IFIT3. {ECO:0000250|UniProtKB:Q92905}. SUBUNIT: Component of the CSN complex, composed of COPS1/GPS1, COPS2, COPS3, COPS4, COPS5, COPS6, COPS7 (COPS7A or COPS7B), COPS8 and COPS9. In the complex, it probably interacts directly with COPS1, COPS2, COPS4, COPS6 and COPS7 (COPS7A or COPS7B) and COPS9. The CSN complex interacts with the BRISC complex. Also exists as monomeric form. Interacts with TP53, MIF, JUN, UCHL1, NCOA1, BCL3, GFER, PGR, LHCGR, SMAD4, SMAD7, ITGB2 and TOP2A. Part of a complex consisting of RANBP9, RAN, DYRK1B and COPS5. Interacts with CDKN1B, HIF1A, ID1 and ID3. Interacts with IFIT3. Interacts with BRSK2 (By similarity). Interacts with ZDHHC16 (By similarity). Interacts with MINDY3 (By similarity). Interacts with FANK1; regulates the phosphorylation of JUN and the transcriptional activity of AP-1 (By similarity). {ECO:0000250|UniProtKB:Q92905}. DOMAIN: The JAMM motif is essential for the protease activity of the CSN complex resulting in deneddylation of cullins. It constitutes the catalytic center of the complex. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10721695}. +Q8VHY0 CSPG4_MOUSE Chondroitin sulfate proteoglycan 4 (Chondroitin sulfate proteoglycan NG2) (Proteoglycan AN2) 2327 252,309 Alternative sequence (3); Chain (1); Compositional bias (1); Disulfide bond (2); Domain (2); Frameshift (1); Glycosylation (16); Modified residue (1); Motif (1); Mutagenesis (5); Region (6); Repeat (15); Sequence conflict (11); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 2230 2250 Helical. {ECO:0000255}. TOPO_DOM 30 2229 Extracellular. {ECO:0000250|UniProtKB:Q00657}.; TOPO_DOM 2251 2327 Cytoplasmic. {ECO:0000250|UniProtKB:Q00657}. FUNCTION: Proteoglycan playing a role in cell proliferation and migration which stimulates endothelial cells motility during microvascular morphogenesis. May also inhibit neurite outgrowth and growth cone collapse during axon regeneration. Cell surface receptor for collagen alpha 2(VI) which may confer cells ability to migrate on that substrate. Binds through its extracellular N-terminus growth factors, extracellular matrix proteases modulating their activity. May regulate MPP16-dependent degradation and invasion of type I collagen participating in melanoma cells invasion properties. May modulate the plasminogen system by enhancing plasminogen activation and inhibiting angiostatin. Functions also as a signal transducing protein by binding through its cytoplasmic C-terminus scaffolding and signaling proteins. May promote retraction fiber formation and cell polarization through Rho GTPase activation. May stimulate alpha-4, beta-1 integrin-mediated adhesion and spreading by recruiting and activating a signaling cascade through CDC42, ACK1 and BCAR1. May activate FAK and ERK1/ERK2 signaling cascades. {ECO:0000269|PubMed:10036240, ECO:0000269|PubMed:15181153}. PTM: O-glycosylated; contains glycosaminoglycan chondroitin sulfate which are required for proper localization and function in stress fiber formation. Involved in interaction with MMP16 and ITGA4 (By similarity). {ECO:0000250}.; PTM: Phosphorylation by PRKCA regulates its subcellular location and function in cell motility. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12458226}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q00657}; Extracellular side {ECO:0000250|UniProtKB:Q00657}. Apical cell membrane {ECO:0000250|UniProtKB:Q00657}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q00657}; Extracellular side {ECO:0000250|UniProtKB:Q00657}. Cell projection, lamellipodium membrane {ECO:0000250|UniProtKB:Q00657}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q00657}; Extracellular side {ECO:0000250|UniProtKB:Q00657}. Cell surface {ECO:0000250|UniProtKB:Q00657}. Note=Localized at the apical plasma membrane it relocalizes to the lamellipodia of astrocytoma upon phosphorylation by PRKCA. Localizes to the retraction fibers. A fraction may undergo cell surface proteolysis and secretion (By similarity). Localizes to the plasma membrane of oligodendrocytes (PubMed:12458226). {ECO:0000250|UniProtKB:Q00657, ECO:0000269|PubMed:12458226}. SUBUNIT: Interacts with ITGA4 through its chondroitin sulfate glycosaminoglycan. Interacts with BCAR1, CDC42 and ACK1. Interacts with MMP16. Interacts with the first PDZ domain of MPDZ. Interacts with PRKCA. Interacts with LGALS3 and the integrin composed of ITGB1 and ITGA3. Binds TNC, laminin-1, COL5A1 and COL6A2. Interacts with PLG and angiostatin. Binds FGF2 and PDGFA (By similarity). Interacts with GRIP1, GRIP2 and GRIA2. Forms a ternary complex with GRIP1 and GRIA2. {ECO:0000250, ECO:0000269|PubMed:12458226}. TISSUE SPECIFICITY: Expressed in microcascular pericytes and not endothelial cells. {ECO:0000269|PubMed:15181153}. +B2RQR8 ECE2_MOUSE Endothelin-converting enzyme 2 (ECE-2) (EC 3.4.24.71) 763 86,231 Active site (2); Alternative sequence (1); Chain (1); Glycosylation (9); Metal binding (3); Modified residue (1); Topological domain (2); Transmembrane (1) TRANSMEM 61 81 Helical; Signal-anchor for type II membrane protein. {ECO:0000305}. TOPO_DOM 1 60 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 82 763 Lumenal. {ECO:0000305}. FUNCTION: Converts big endothelin-1 to endothelin-1. Also involved in the processing of various neuroendocrine peptides, including neurotensin, angiotensin I, substance P, proenkephalin-derived peptides, and prodynorphin-derived peptides (By similarity). May play a role in amyloid-beta processing (PubMed:12464614). {ECO:0000250|UniProtKB:P0DPD6, ECO:0000269|PubMed:12464614}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:F1N476}; Single-pass type II membrane protein {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:F1N476}. +Q9JMI0 ECEL1_MOUSE Endothelin-converting enzyme-like 1 (EC 3.4.24.-) (Damage-induced neuronal endopeptidase) (Xce protein) 775 87,993 Active site (1); Chain (1); Glycosylation (3); Metal binding (3); Sequence conflict (5); Topological domain (2); Transmembrane (1) TRANSMEM 62 82 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 61 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 83 775 Lumenal. {ECO:0000255}. FUNCTION: May contribute to the degradation of peptide hormones and be involved in the inactivation of neuronal peptides. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. +Q99JY0 ECHB_MOUSE Trifunctional enzyme subunit beta, mitochondrial (TP-beta) [Includes: 3-ketoacyl-CoA thiolase (EC 2.3.1.16) (Acetyl-CoA acyltransferase) (Beta-ketothiolase)] 475 51,386 Active site (3); Chain (1); Modified residue (15); Sequence conflict (4); Transit peptide (1) Lipid metabolism; fatty acid beta-oxidation. PTM: Acetylation of Lys-202 is observed in liver mitochondria from fasted mice but not from fed mice. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Mitochondrion inner membrane {ECO:0000250}. Mitochondrion outer membrane {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. SUBUNIT: Octamer of 4 alpha (HADHA) and 4 beta (HADHB) subunits. Interacts with RSAD2/viperin. {ECO:0000250}. +Q9D9V3 ECHD1_MOUSE Ethylmalonyl-CoA decarboxylase (EC 4.1.1.94) (Enoyl-CoA hydratase domain-containing protein 1) (Methylmalonyl-CoA decarboxylase) (MMCD) (EC 7.2.4.3) 322 35,467 Alternative sequence (1); Chain (1); Modified residue (3); Sequence conflict (4) FUNCTION: Decarboxylases ethylmalonyl-CoA decarboxylase, a potentially toxic metabolite, to form butyryl-CoA, suggesting it might be involved in metabolite proofreading. Also has methylmalonyl-CoA decarboxylase activity at lower level. {ECO:0000269|PubMed:22016388}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305|PubMed:22016388}. +P59054 CSRN1_MOUSE Cysteine/serine-rich nuclear protein 1 (CSRNP-1) (Axin-1 up-regulated gene 1 protein) (TGF-beta-induced apoptosis protein 3) (TAIP-3) 583 62,525 Chain (1); Compositional bias (2); Sequence conflict (2) FUNCTION: Binds to the consensus sequence 5'-AGAGTG-3' and has transcriptional activator activity. May have a tumor-suppressor function. May play a role in apoptosis. {ECO:0000269|PubMed:17726538}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17726538}. TISSUE SPECIFICITY: Widely expressed with highest levels in thymus and lung. Low levels detected in naive T-cells. {ECO:0000269|PubMed:17726538}. +P59055 CSRN3_MOUSE Cysteine/serine-rich nuclear protein 3 (CSRNP-3) (Protein FAM130A2) (TGF-beta-induced apoptosis protein 2) (TAIP-2) 597 66,121 Alternative sequence (1); Chain (1); Compositional bias (3); Erroneous initiation (2); Sequence conflict (2) FUNCTION: Binds to the consensus sequence 5'-AGAGTG-3' and has transcriptional activator activity. Plays a role in apoptosis. {ECO:0000269|PubMed:17726538, ECO:0000269|PubMed:18291095}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17726538, ECO:0000269|PubMed:18291095}. TISSUE SPECIFICITY: Detected only in the brain of E15, E18, newborn and P6 mice (at protein level). {ECO:0000269|PubMed:17726538, ECO:0000269|PubMed:18291095}. +P42125 ECI1_MOUSE Enoyl-CoA delta isomerase 1, mitochondrial (EC 5.3.3.8) (3,2-trans-enoyl-CoA isomerase) (Delta(3),Delta(2)-enoyl-CoA isomerase) (D3,D2-enoyl-CoA isomerase) (Dodecenoyl-CoA isomerase) 289 32,250 Binding site (2); Chain (1); Modified residue (15); Region (1); Sequence conflict (4); Site (1); Transit peptide (1) Lipid metabolism; fatty acid beta-oxidation. FUNCTION: Able to isomerize both 3-cis and 3-trans double bonds into the 2-trans form in a range of enoyl-CoA species. SUBCELLULAR LOCATION: Mitochondrion matrix. SUBUNIT: Homotrimer. {ECO:0000250}. +Q9WUR2 ECI2_MOUSE Enoyl-CoA delta isomerase 2, mitochondrial (EC 5.3.3.8) (Delta(3),delta(2)-enoyl-CoA isomerase) (D3,D2-enoyl-CoA isomerase) (Dodecenoyl-CoA isomerase) (Peroxisomal 3,2-trans-enoyl-CoA isomerase) (pECI) 391 43,268 Alternative sequence (1); Binding site (2); Chain (1); Domain (1); Erroneous initiation (1); Modified residue (15); Motif (1); Region (3); Sequence conflict (3); Site (1); Transit peptide (1) FUNCTION: Able to isomerize both 3-cis and 3-trans double bonds into the 2-trans form in a range of enoyl-CoA species (PubMed:24344334). Has a preference for 3-trans substrates (By similarity). {ECO:0000250|UniProtKB:Q5XIC0, ECO:0000269|PubMed:24344334}. PTM: Acetylation of Lys-60 is observed in liver mitochondria from fasted mice but not from fed mice. SUBCELLULAR LOCATION: Isoform 1: Mitochondrion {ECO:0000269|PubMed:24344334}.; SUBCELLULAR LOCATION: Isoform 2: Peroxisome matrix {ECO:0000269|PubMed:24344334}. TISSUE SPECIFICITY: Expressed in liver and kidney (at protein level). {ECO:0000269|PubMed:24344334}. +Q6PDI5 ECM29_MOUSE Proteasome adapter and scaffold protein ECM29 (Proteasome-associated protein ECM29 homolog) 1840 203,703 Alternative sequence (1); Chain (1); Cross-link (1); Modified residue (2); Repeat (25); Sequence caution (1); Sequence conflict (3) FUNCTION: Adapter/scaffolding protein that binds to the 26S proteasome, motor proteins and other compartment specific proteins. May couple the proteasome to different compartments including endosome, endoplasmic reticulum and centrosome. May play a role in ERAD and other enhanced proteolyis (By similarity). Promotes proteasome dissociation under oxidative stress (PubMed:26802743). {ECO:0000250|UniProtKB:Q5VYK3, ECO:0000269|PubMed:26802743}. SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:Q5VYK3}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250|UniProtKB:Q5VYK3}. Endosome {ECO:0000250|UniProtKB:Q5VYK3}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q5VYK3}. Nucleus {ECO:0000250|UniProtKB:Q5VYK3}. Endosome, multivesicular body {ECO:0000250|UniProtKB:Q5VYK3}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q5VYK3}. SUBUNIT: Non-stoichiometric component of the proteasome; associates with the 26S proteasome. Interacts (via N-terminus) with VPS11, VPS26A, VPS36, RAB11FIP4 and RABEP1. Interacts (via C-terminus) with DCTN1, DCTN2, KIF5B, MYH7, MYH10, MYO10 and ARF6. {ECO:0000250|UniProtKB:Q5VYK3}. TISSUE SPECIFICITY: Widely expressed (at protein level). {ECO:0000269|PubMed:15496406, ECO:0000269|PubMed:26802743}. +Q5FW85 ECM2_MOUSE Extracellular matrix protein 2 (Tenonectin) 670 76,676 Chain (1); Compositional bias (1); Domain (2); Glycosylation (3); Motif (1); Repeat (13); Signal peptide (1) FUNCTION: Promotes matrix assembly and cell adhesiveness. {ECO:0000269|PubMed:18757743}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:18757743}. SUBUNIT: Interacts with numerous extracellular matrix proteins. {ECO:0000269|PubMed:18757743}. +Q8BIQ5 CSTF2_MOUSE Cleavage stimulation factor subunit 2 (CF-1 64 kDa subunit) (Cleavage stimulation factor 64 kDa subunit) (CSTF 64 kDa subunit) (CstF-64) 580 61,341 Alternative sequence (2); Chain (1); Compositional bias (2); Cross-link (1); Domain (1); Modified residue (6); Region (3); Repeat (12); Sequence conflict (1) FUNCTION: One of the multiple factors required for polyadenylation and 3'-end cleavage of mammalian pre-mRNAs. This subunit is directly involved in the binding to pre-mRNAs (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14681198}. Note=Localized with DDX1 in cleavage bodies. {ECO:0000250}. SUBUNIT: The CSTF complex is composed of CSTF1 (50 kDa subunit), CSTF2 (64 kDa subunit) and CSTF3 (77 kDa subunit). CSTF2 directly interacts with CSTF3, SYMPK and RPO2TC1. Interacts with HSF1 in heat-stressed cells (By similarity). Interacts with CPSF2, CPSF3 and FIP1L1. Interacts with DDX1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in most somatic cell types (at protein level). Highly expressed in testis, except in meiotic spermatocytes. {ECO:0000269|PubMed:11369601, ECO:0000269|PubMed:14681198}. +Q99LI7 CSTF3_MOUSE Cleavage stimulation factor subunit 3 (CF-1 77 kDa subunit) (Cleavage stimulation factor 77 kDa subunit) (CSTF 77 kDa subunit) (CstF-77) 717 82,877 Beta strand (3); Chain (1); Compositional bias (1); Helix (29); Initiator methionine (1); Modified residue (2); Repeat (9); Turn (6) FUNCTION: One of the multiple factors required for polyadenylation and 3'-end cleavage of mammalian pre-mRNAs. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Homodimer. The CSTF complex is composed of CSTF1 (50 kDa subunit), CSTF2 (64 kDa subunit) and CSTF3 (77 kDa subunit). CSTF3 directly interacts with CSTF1 and CSTF2. Interacts with FIP1L1 (By similarity). {ECO:0000250}. +Q8C7E9 CSTFT_MOUSE Cleavage stimulation factor subunit 2 tau variant (CF-1 64 kDa subunit tau variant) (Cleavage stimulation factor 64 kDa subunit tau variant) (CSTF 64 kDa subunit tau variant) (TauCstF-64) 632 65,862 Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (1); Frameshift (1); Modified residue (1); Region (2); Repeat (20); Sequence conflict (4) FUNCTION: May play a significant role in AAUAAA-independent mRNA polyadenylation in germ cells. Directly involved in the binding to pre-mRNAs. {ECO:0000269|PubMed:11113135}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14681198}. TISSUE SPECIFICITY: Expressed in testes, where it is restricted to pachytene spermatocytes and spermatids, and in the brain (at protein level). {ECO:0000269|PubMed:14681198}. +Q9ER65 CSTN2_MOUSE Calsyntenin-2 (Alcadein-gamma) (Alc-gamma) 966 107,887 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (2); Erroneous initiation (1); Glycosylation (6); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 836 856 Helical. {ECO:0000255}. TOPO_DOM 21 835 Extracellular. {ECO:0000255}.; TOPO_DOM 857 966 Cytoplasmic. {ECO:0000255}. FUNCTION: May modulate calcium-mediated postsynaptic signals. {ECO:0000250}. PTM: Proteolytically processed under normal cellular conditions. A primary zeta-cleavage generates a large extracellular (soluble) N-terminal domain (sAlc) and a short C-terminal transmembrane fragment (CTF1). A secondary cleavage catalyzed by gamma-secretase within the transmembrane domain releases the beta-Alc-gamma chain in the extracellular milieu and produces an intracellular fragment (AlcICD). This processing is strongly suppressed in the tripartite complex formed with APBA2 and APP, which seems to prevent the association with PSEN1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:12498782}. Golgi apparatus membrane {ECO:0000269|PubMed:12498782}. Note=Most prominent in the postsynaptic specializations of asymmetric (type I) synapses with both axodendritic and axospinous localization. DOMAIN: Binds synaptic Ca(2+) with its cytoplasmic domain. {ECO:0000250}. TISSUE SPECIFICITY: Restricted to the brain. In the cerebral cortex, found in the somas and neuropil of all layers. Expressed at highest levels in neurons of cortical layers 5 and 6 and, at lower levels, in neurons of the upper layers. Highly expressed in Purkinje cells. Also found in a few scattered interneurons throughout the granule cell layer and occasionally in neurons in the molecular layer (at protein level). Present throughout all cortical layers, highest levels in GABAergic neurons (based on morphology and distribution pattern). {ECO:0000269|PubMed:12498782}. +Q99JH7 CSTN3_MOUSE Calsyntenin-3 (Alcadein-beta) (Alc-beta) 956 105,872 Chain (1); Domain (2); Glycosylation (5); Mutagenesis (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 848 868 Helical. {ECO:0000255}. TOPO_DOM 20 847 Extracellular. {ECO:0000255}.; TOPO_DOM 869 956 Cytoplasmic. {ECO:0000255}. FUNCTION: May modulate calcium-mediated postsynaptic signals. Complex formation with APBA2 and APP, stabilizes APP metabolism and enhances APBA2-mediated suppression of beta-APP40 secretion, due to the retardation of intracellular APP maturation. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:12498782}. Golgi apparatus membrane {ECO:0000269|PubMed:12498782}. Note=Most prominent in the postsynaptic specializations of asymmetric (type I) synapses with both axodendritic and axospinous localization. SUBUNIT: Directly interacts with APBA2. Forms a tripartite complex with APBA2 and APP (By similarity). Interacts with low affinity with KLC1. {ECO:0000250, ECO:0000269|PubMed:16760430}. DOMAIN: Binds synaptic Ca(2+) with its cytoplasmic domain. {ECO:0000250}. TISSUE SPECIFICITY: Restricted to the brain. In the cerebral cortex, found in the somas and neuropil of all layers. Expressed at highest levels in neurons of cortical layer 5 and, at lower levels, in neurons of the upper layers. Highly expressed in Purkinje cells. Also found in a few scattered interneurons throughout the granule cell layer and occasionally in neurons in the molecular layer (at protein level). In all layers, high levels in a subpopulation of presumptive GABAergic neurons (based on morphology). {ECO:0000269|PubMed:12498782}. +Q9Z0H6 CST9_MOUSE Cystatin-9 (Testatin) 137 16,094 Chain (1); Disulfide bond (2); Glycosylation (2); Signal peptide (1) FUNCTION: May be involved in testis development (PubMed:9826679). May play a role in hematopoietic differentiation or inflammation (By similarity). Has immunomodulatory and antimicrobial functions against Francisella tularensis, a Gram-negative bacteria (PubMed:23922243). {ECO:0000250|UniProtKB:Q5W186, ECO:0000269|PubMed:23922243, ECO:0000305|PubMed:9826679}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Expression is restricted to fetal gonads and adult testis. {ECO:0000269|PubMed:9826679}. +A0A140LIA7 CT204_MOUSE Uncharacterized protein C20orf204 homolog 188 20,635 Chain (1); Glycosylation (1); Signal peptide (1) +P97425 ECP2_MOUSE Eosinophil cationic protein 2 (ECP 2) (EC 3.1.27.-) (Eosinophil secondary granule ribonuclease 2) (EAR-2) (Ribonuclease 3-2) (RNase 3-2) 156 17,620 Active site (2); Chain (1); Disulfide bond (4); Glycosylation (3); Region (1); Signal peptide (1) FUNCTION: Cytotoxin and helminthotoxin with ribonuclease activity. Selectively chemotactic for dendritic cells. Possesses a wide variety of biological activities. SUBCELLULAR LOCATION: Cytoplasmic granule {ECO:0000250}. Note=Matrix of eosinophil's large specific granule. {ECO:0000250}. DOMAIN: The N-terminal region is necessary for mediating chemotactic activity. +O35290 ECP3_MOUSE Eosinophil cationic-type ribonuclease 3 (MR-3) 156 17,745 Active site (2); Chain (1); Disulfide bond (4); Glycosylation (4); Region (1); Signal peptide (1) +Q99LJ0 CT2NL_MOUSE CTTNBP2 N-terminal-like protein 638 69,841 Chain (1); Coiled coil (1); Erroneous initiation (1); Modified residue (11); Sequence conflict (1) SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, stress fiber {ECO:0000269|PubMed:23015759}. SUBUNIT: May form homomers (By similarity). May interact with MOB4, PPP2R1A, PPP2CB, STK24, STK25, STK26, STRN4, STRIP1 and STRIP2 (By similarity). Interacts with CTTN/cortactin; this interaction may redistribute CTTN to stress fibers. {ECO:0000250, ECO:0000269|PubMed:23015759}. TISSUE SPECIFICITY: Predominantly expressed in skin, also detectable in spleen and lung (at protein level). Very low levels, if any, in brain (at protein level). +O88712 CTBP1_MOUSE C-terminal-binding protein 1 (CtBP1) (EC 1.1.1.-) 441 47,745 Active site (3); Alternative sequence (2); Binding site (3); Chain (1); Cross-link (1); Erroneous initiation (1); Modified residue (2); Nucleotide binding (4); Region (2); Sequence conflict (5) FUNCTION: Corepressor targeting diverse transcription regulators such as GLIS2 or BCL6. Has dehydrogenase activity. Involved in controlling the equilibrium between tubular and stacked structures in the Golgi complex. Functions in brown adipose tissue (BAT) differentiation. {ECO:0000269|PubMed:10369679, ECO:0000269|PubMed:10567582, ECO:0000269|PubMed:16326862, ECO:0000269|PubMed:18483224, ECO:0000269|PubMed:19103759}. PTM: ADP-ribosylated; when cells are exposed to brefeldin A. {ECO:0000250}.; PTM: The level of phosphorylation appears to be regulated during the cell cycle. Phosphorylation by HIPK2 on Ser-423 induces proteasomal degradation (By similarity). {ECO:0000250}.; PTM: Sumoylation on Lys-429 is promoted by the E3 SUMO-protein ligase CBX4. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13363}. Nucleus {ECO:0000250|UniProtKB:Q13363}. SUBUNIT: Homo- or heterodimer. Heterodimer with CTBP2. Interacts with ELK3 (via its PXDLS motif). Interacts with RBBP8 (via its PXDLS motif). Interacts with PNN, MECOM and ZFHX1B. Interacts with ZNF366 (via PXDLS motif) (By similarity). Interaction with SATB1 (non-acetylated form); the interaction stabilizes its attachment to DNA and promotes transcription repression. Interacts with PRDM16; the interaction represses white adipose tissue (WAT)-specific genes expression. Interacts with GLIS2, HIPK2, FOXP1, FOXP2, HDAC4, HDAC5, HDAC9, NRIP1, WIZ and ZNF217. Interacts with BCL6; the interaction is required for BCL6 transcriptional autoinhibition and inhibition of some BCL6 target genes. Interacts with IKZF4. Interacts with MCRIP1 (unphosphorylated form, via the PXDLS motif); competitively inhibiting CTBP-ZEB1 interaction (By similarity). {ECO:0000250|UniProtKB:Q13363, ECO:0000269|PubMed:11022042, ECO:0000269|PubMed:14567915, ECO:0000269|PubMed:14701752, ECO:0000269|PubMed:14736873, ECO:0000269|PubMed:16326862, ECO:0000269|PubMed:16702210, ECO:0000269|PubMed:18483224, ECO:0000269|PubMed:19103759, ECO:0000269|PubMed:19696312}. TISSUE SPECIFICITY: Expressed in a wide range of adult tissues. {ECO:0000269|PubMed:10567582}. +Q7TSG2 CTDP1_MOUSE RNA polymerase II subunit A C-terminal domain phosphatase (EC 3.1.3.16) (TFIIF-associating CTD phosphatase) 960 104,554 Alternative sequence (2); Chain (1); Compositional bias (3); Domain (2); Modified residue (8); Sequence conflict (2) FUNCTION: Processively dephosphorylates 'Ser-2' and 'Ser-5' of the heptad repeats YSPTSPS in the C-terminal domain of the largest RNA polymerase II subunit. This promotes the activity of RNA polymerase II. Plays a role in the exit from mitosis by dephosphorylating crucial mitotic substrates (USP44, CDC20 and WEE1) that are required for M-phase-promoting factor (MPF)/CDK1 inactivation (By similarity). {ECO:0000250}. PTM: Phosphorylated. In the presence of TFIIF, the phosphorylated form has an increased CTD phosphatase activity. The phosphorylation is required for the physical interaction with GTF2F1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. Midbody {ECO:0000250}. Note=Found at centrosomes in prometaphase, at spindle and spindle poles in metaphase and at spindle midzone and midbody in anaphase and telophase-G1 respectively. {ECO:0000250}. SUBUNIT: Homodimer. Interacts with GTF2F1 (By similarity). Interacts with WDR77, SNRPB and SNRNP70 (By similarity). {ECO:0000250}. +P58466 CTDS1_MOUSE Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 1 (EC 3.1.3.16) (Golli-interacting protein) (GIP) (Nuclear LIM interactor-interacting factor 3) (NLI-interacting factor 3) (Small C-terminal domain phosphatase 1) (SCP1) (Small CTD phosphatase 1) 261 29,266 Active site (2); Chain (1); Domain (1); Metal binding (3); Modified residue (1); Mutagenesis (2); Site (2) FUNCTION: Preferentially catalyzes the dephosphorylation of 'Ser-5' within the tandem 7 residue repeats in the C-terminal domain (CTD) of the largest RNA polymerase II subunit POLR2A. Negatively regulates RNA polymerase II transcription, possibly by controlling the transition from initiation/capping to processive transcript elongation (By similarity). Recruited by REST to neuronal genes that contain RE-1 elements, leading to neuronal gene silencing in non-neuronal cells. {ECO:0000250, ECO:0000269|PubMed:15681389}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Monomer. Interacts with REST. {ECO:0000250}. TISSUE SPECIFICITY: Expression is restricted to non-neuronal tissues. {ECO:0000269|PubMed:15681389}. +Q8BX07 CTDS2_MOUSE Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 2 (EC 3.1.3.16) (Small C-terminal domain phosphatase 2) (Small CTD phosphatase 2) (SCP2) 270 30,546 Active site (2); Chain (1); Domain (1); Metal binding (3); Modified residue (1); Site (2) FUNCTION: Preferentially catalyzes the dephosphorylation of 'Ser-5' within the tandem 7 residue repeats in the C-terminal domain (CTD) of the largest RNA polymerase II subunit POLR2A. Negatively regulates RNA polymerase II transcription, possibly by controlling the transition from initiation/capping to processive transcript elongation. Recruited by REST to neuronal genes that contain RE-1 elements, leading to neuronal gene silencing in non-neuronal cells (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Monomer. Interacts with REST. {ECO:0000250}. TISSUE SPECIFICITY: Expression is restricted to non-neuronal tissues. {ECO:0000269|PubMed:15681389}. +Q8BIW9 CTF18_MOUSE Chromosome transmission fidelity protein 18 homolog 969 108,137 Chain (1); Modified residue (2); Nucleotide binding (1); Sequence conflict (3) FUNCTION: Chromosome cohesion factor involved in sister chromatid cohesion and fidelity of chromosome transmission. Component of one of the cell nuclear antigen loader complexes, CTF18-replication factor C (CTF18-RFC), which consists of CTF18, CTF8, DCC1, RFC2, RFC3, RFC4 and RFC5. The CTF18-RFC complex binds to single-stranded and primed DNAs and has weak ATPase activity that is stimulated by the presence of primed DNA, replication protein A (RPA) and by proliferating cell nuclear antigen (PCNA). The CTF18-RFC complex catalyzes the ATP-dependent loading of PCNA onto primed and gapped DNA. It also interacts with and stimulates DNA polymerase POLH (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Note=Associates with chromatin during S phase. {ECO:0000250}. SUBUNIT: Component of the CTF18-RFC complex, which consists of CTF18, CTF8, DCC1, RFC2, RFC3, RFC4 and RFC5. During assembly of the CTF18-RFC complex, CTF18 may first assemble into a subcomplex with RFC2, RFC3, RFC4 and RFC5. CTF18 then interacts directly with CTF8, which in turn interacts with DCC1. The CTF18-RFC complex associates with PCNA and with DNA polymerase POLH. The CTF18-RFC complex does not interact with the Rad9/Rad1/Hus1 complex. CTF18 interacts with SMC1A and RAD21. Interacts with DDX11. {ECO:0000250|UniProtKB:Q8WVB6}. +P83714 CTF2_MOUSE Cardiotrophin-2 (CT-2) (Neuropoietin) (Np) 204 22,000 Chain (1); Glycosylation (1); Signal peptide (1) FUNCTION: Increases the platelet count associated with splenomegaly. May have an important role in neuronal precursor development and maturation. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Binds to tripartite CNTF receptor complex consisting of CNTF alpha chain, LIFR and IL6ST (in vitro). TISSUE SPECIFICITY: Not detected in adult tissues. +P12399 CTL2A_MOUSE Protein CTLA-2-alpha (Cytotoxic T-lymphocyte-associated protein 2-alpha) 137 15,883 Chain (1); Erroneous initiation (1); Region (1); Repeat (2); Signal peptide (1) FUNCTION: Not known, expressed in activated T-cell. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +P00015 CYC2_MOUSE Cytochrome c, testis-specific 105 11,714 Beta strand (1); Binding site (2); Chain (1); Helix (5); Initiator methionine (1); Metal binding (2); Modified residue (1); Turn (1) FUNCTION: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.; FUNCTION: Plays a role in apoptosis. Suppression of the anti-apoptotic members or activation of the pro-apoptotic members of the Bcl-2 family leads to altered mitochondrial membrane permeability resulting in release of cytochrome c into the cytosol. Binding of cytochrome c to Apaf-1 triggers the activation of caspase-9, which then accelerates apoptosis by activating other caspases (By similarity). {ECO:0000250}. PTM: Binds 1 heme group per subunit.; PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the turnover in the reaction with cytochrome c oxidase, down-regulating mitochondrial respiration. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely associated with the inner membrane. TISSUE SPECIFICITY: This is one of two isocytochromes C found in the testis. The other is identical with the form found in other mouse tissues. These cytochromes are assumed to be located in the sperm. +Q99LD9 EI2BB_MOUSE Translation initiation factor eIF-2B subunit beta (eIF-2B GDP-GTP exchange factor subunit beta) 351 38,898 Chain (1) FUNCTION: Catalyzes the exchange of eukaryotic initiation factor 2-bound GDP for GTP. {ECO:0000250}. SUBUNIT: Complex of five different subunits; alpha, beta, gamma, delta and epsilon. {ECO:0000250}. +Q8VIH7 CYYR1_MOUSE Cysteine and tyrosine-rich protein 1 (Proline-rich domain-containing protein) 165 18,044 Chain (1); Compositional bias (1); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 62 82 Helical. {ECO:0000255}. TOPO_DOM 30 61 Extracellular. {ECO:0000255}.; TOPO_DOM 83 165 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q8CIM3 D2HDH_MOUSE D-2-hydroxyglutarate dehydrogenase, mitochondrial (EC 1.1.99.-) 535 58,576 Chain (1); Domain (1); Modified residue (1); Sequence conflict (6); Transit peptide (1) FUNCTION: Catalyzes the oxidation of D-2-hydroxyglutarate to alpha-ketoglutarate. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. +Q64505 CP7A1_MOUSE Cholesterol 7-alpha-monooxygenase (EC 1.14.14.23) (CYPVII) (Cholesterol 7-alpha-hydroxylase) (Cytochrome P450 7A1) 503 57,262 Chain (1); Metal binding (1); Sequence conflict (3) Lipid metabolism; bile acid biosynthesis. FUNCTION: Catalyzes a rate-limiting step in cholesterol catabolism and bile acid biosynthesis by introducing a hydrophilic moiety at position 7 of cholesterol. Important for cholesterol homeostasis. {ECO:0000269|PubMed:14522988}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. +Q8BMD2 DZIP1_MOUSE Zinc finger protein DZIP1 (DAZ-interacting protein 1 homolog) 852 97,263 Alternative sequence (4); Chain (1); Coiled coil (3); Erroneous initiation (1); Sequence conflict (2); Zinc finger (1) FUNCTION: May participate in spermatogenesis via its interaction with DAZL. Has a role in primary cilium formation. {ECO:0000250|UniProtKB:Q86YF9}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15081113}. Cytoplasm {ECO:0000269|PubMed:15081113}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q86YF9}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q86YF9}. Note=In primary and secondary spermatocytes, it is predominantly cytoplasmic. Colocalizes with DAZL in primordial germ cells. In spermatocytes, it localizes to a unique U-shaped pattern in cytoplasm. {ECO:0000269|PubMed:15081113}. SUBUNIT: Probably interacts with DAZL. May participate in an RNA-binding complex that functions in both ES cells and germ cells (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in testis and undifferentiated ES cells. {ECO:0000269|PubMed:15081113}. +Q8C166 CPNE1_MOUSE Copine-1 (Copine I) 536 58,887 Chain (1); Domain (3); Modified residue (1); Sequence conflict (2) FUNCTION: Calcium-dependent phospholipid-binding protein that plays a role in calcium-mediated intracellular processes. Involved in the TNF-alpha receptor signaling pathway in a calcium-dependent manner. Exhibits calcium-dependent phospholipid binding properties. Plays a role in neuronal progenitor cell differentiation; induces neurite outgrowth via a AKT-dependent signaling cascade and calcium-independent manner. May recruit target proteins to the cell membrane in a calcium-dependent manner. May function in membrane trafficking. Involved in TNF-alpha-induced NF-kappa-B transcriptional repression by inducing endoprotease processing of the transcription factor NF-kappa-B p65/RELA subunit. Also induces endoprotease processing of NF-kappa-B p50/NFKB1, p52/NFKB2, RELB and REL. {ECO:0000250|UniProtKB:Q99829}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q99829}. Cytoplasm {ECO:0000250|UniProtKB:Q99829}. Cell membrane {ECO:0000250|UniProtKB:Q99829}. Note=Translocates to the cell membrane in a calcium-dependent manner. {ECO:0000250|UniProtKB:Q99829}. SUBUNIT: Homodimer; homodimerizes via its C2 domains. Interacts with p65/RELA (via N-terminus); this interaction induces proteolytic cleavage of p65/RELA subunit and inhibition of NF-kappa-B transcriptional activity. Interacts (via VWFA domain) with ACTB, CCDC22, MYCBP2, PPP5C, RDX and UBE2O. {ECO:0000250|UniProtKB:Q99829}. DOMAIN: C2 domains are necessary for calcium-dependent cell membrane association. C2 domains are necessary for neuronal progenitor cell differentiation in a calcium-independent manner. {ECO:0000250|UniProtKB:Q99829}. +O88962 CP8B1_MOUSE 7-alpha-hydroxycholest-4-en-3-one 12-alpha-hydroxylase (EC 1.14.18.8) (7-alpha-hydroxy-4-cholesten-3-one 12-alpha-hydroxylase) (CYPVIIIB1) (Cytochrome P450 8B1) (Sterol 12-alpha-hydroxylase) 500 57,706 Chain (1); Metal binding (1); Modified residue (1); Natural variant (1); Transmembrane (1) TRANSMEM 4 24 Helical. {ECO:0000255}. FUNCTION: Involved in bile acid synthesis and is responsible for the conversion of 7 alpha-hydroxy-4-cholesten-3-one into 7 alpha, 12 alpha-dihydroxy-4-cholesten-3-one. Responsible for the balance between formation of cholic acid and chenodeoxycholic acid. Has a rather broad substrate specificity including a number of 7-alpha-hydroxylated C27 steroids. {ECO:0000250|UniProtKB:O02766}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. Microsome membrane; Single-pass membrane protein. TISSUE SPECIFICITY: Expressed in liver. +Q3UZA1 CPZIP_MOUSE CapZ-interacting protein (Protein kinase substrate CapZIP) 412 44,114 Alternative sequence (1); Chain (1); Modified residue (21); Sequence conflict (15) FUNCTION: Stress-induced phosphorylation of CAPZIP may regulate the ability of F-actin-capping protein to remodel actin filament assembly. {ECO:0000250}. PTM: Dephosphorylation results in its dissociation from CAPZA2. {ECO:0000250}. SUBUNIT: Interacts with CAPZA2 and CAPZB. {ECO:0000250}. +Q9DC53 CPNE8_MOUSE Copine-8 (Copine VIII) 577 64,667 Chain (1); Domain (3); Modified residue (1) FUNCTION: Probable calcium-dependent phospholipid-binding protein that may play a role in calcium-mediated intracellular processes. {ECO:0000250|UniProtKB:Q99829}. +Q9D2L5 CPXM2_MOUSE Inactive carboxypeptidase-like protein X2 764 86,963 Chain (1); Compositional bias (1); Disulfide bond (1); Domain (1); Glycosylation (5); Sequence conflict (7); Signal peptide (1) FUNCTION: May be involved in cell-cell interactions. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Highly expressed in lung and kidney. Moderate expression in liver and brain, including the cerebral cortex, piriform cortex, nucleus of the lateral olfactory tract, hippocampus, habenular nucleus, and choroid plexus. {ECO:0000269|PubMed:9809751}. +Q3THF9 CQ10B_MOUSE Coenzyme Q-binding protein COQ10 homolog B, mitochondrial 240 27,269 Alternative sequence (1); Chain (1); Erroneous initiation (4); Sequence conflict (3); Transit peptide (1) FUNCTION: Required for the function of coenzyme Q in the respiratory chain. May serve as a chaperone or may be involved in the transport of Q6 from its site of synthesis to the catalytic sites of the respiratory complexes (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Matrix side {ECO:0000250}. SUBUNIT: Interacts with coenzyme Q. {ECO:0000250}. +Q5XFZ0 CR021_MOUSE UPF0711 protein C18orf21 homolog 217 24,123 Chain (1); Frameshift (1); Modified residue (3); Sequence conflict (1) +Q8R555 CRAC1_MOUSE Cartilage acidic protein 1 (68 kDa chondrocyte-expressed protein) (CEP-68) (ASPIC) (Protein CRTAC1-B) 646 70,325 Chain (1); Compositional bias (1); Disulfide bond (3); Domain (1); Erroneous initiation (1); Repeat (4); Sequence conflict (3); Signal peptide (1) SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. +Q8WTY4 CPIN1_MOUSE Anamorsin (Cytokine-induced apoptosis inhibitor 1) (Fe-S cluster assembly protein DRE2 homolog) 309 33,429 Chain (1); Metal binding (8); Modified residue (6); Motif (2); Region (5) FUNCTION: Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the scaffold complex NUBP1-NUBP2. Electrons are transferred to CIAPIN1 from NADPH via the FAD- and FMN-containing protein NDOR1. NDOR1-CIAPIN1 are also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit (By similarity). Has anti-apoptotic effects in the cell. Involved in negative control of cell death upon cytokine withdrawal. Promotes development of hematopoietic cells (PubMed:14970183). {ECO:0000255|HAMAP-Rule:MF_03115, ECO:0000269|PubMed:14970183}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03115}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03115}. Mitochondrion intermembrane space {ECO:0000255|HAMAP-Rule:MF_03115}. SUBUNIT: Monomer. Interacts with NDOR1. Interacts with CHCHD4. {ECO:0000255|HAMAP-Rule:MF_03115}. DOMAIN: The twin Cx2C motifs are involved in the recognition by the mitochondrial CHCHD4/MIA40-GFER/ERV1 disulfide relay system. The formation of 2 disulfide bonds in the Cx2C motifs through dithiol/disulfide exchange reactions effectively traps the protein in the mitochondrial intermembrane space. {ECO:0000255|HAMAP-Rule:MF_03115}.; DOMAIN: The C-terminal domain binds 2 Fe-S clusters but is otherwise mostly in an intrinsically disordered conformation. {ECO:0000255|HAMAP-Rule:MF_03115}.; DOMAIN: The N-terminal domain has structural similarity with S-adenosyl-L-methionine-dependent methyltransferases, but does not bind S-adenosyl-L-methionine. It is required for correct assembly of the 2 Fe-S clusters. {ECO:0000255|HAMAP-Rule:MF_03115}. +Q9Z2R9 E2AK1_MOUSE Eukaryotic translation initiation factor 2-alpha kinase 1 (EC 2.7.11.1) (Heme-controlled repressor) (HCR) (Heme-regulated eukaryotic initiation factor eIF-2-alpha kinase) (Heme-regulated inhibitor) (Hemin-sensitive initiation factor 2-alpha kinase) 619 69,702 Active site (1); Binding site (1); Chain (1); Domain (1); Erroneous initiation (1); Modified residue (4); Mutagenesis (7); Nucleotide binding (1); Repeat (2); Sequence conflict (7); Site (1) FUNCTION: Inhibits protein synthesis at the translation initiation level, in response to various stress conditions, including oxidative stress, heme deficiency, osmotic shock and heat shock. Exerts its function through the phosphorylation of EIF2S1 at 'Ser-48' and 'Ser-51', thus preventing its recycling. Binds hemin forming a 1:1 complex through a cysteine thiolate and histidine nitrogenous coordination. This binding occurs with moderate affinity, allowing it to sense the heme concentration within the cell. Thanks to this unique heme-sensing capacity, plays a crucial role to shut off protein synthesis during acute heme-deficient conditions. In red blood cells (RBCs), controls hemoglobin synthesis ensuring a coordinated regulation of the synthesis of its heme and globin moieties. Thus plays an essential protective role for RBC survival in anemias of iron deficiency. Similarly, in hepatocytes, involved in heme-mediated translational control of CYP2B and CYP3A and possibly other hepatic P450 cytochromes. May also contain ER stress during acute heme-deficient conditions. {ECO:0000269|PubMed:11726526, ECO:0000269|PubMed:16893190, ECO:0000269|PubMed:20071449}. PTM: Activated by autophosphorylation; phosphorylated predominantly on serine and threonine residues, but also on tyrosine residues. Autophosphorylation at Thr-485 is required for kinase activation. The active autophosphorylated form apparently is largely refractory to cellular heme fluctuations. {ECO:0000269|PubMed:12767237}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17932563}. SUBUNIT: Synthesized in an inactive form that binds to the N-terminal domain of CDC37. Has to be associated with a multiprotein complex containing Hsp90, CDC37 and PPP5C for maturation and activation by autophosphorylation. The phosphatase PPP5C modulates this activation (By similarity). Forms oligomers. Has been reported as a homodimer, as well as a hexamer in the absence of hemin. Converted to an inactive disulfide linked homodimer in the presence of hemin. {ECO:0000250}. TISSUE SPECIFICITY: Expressed predominantly in erythroid cells, mature reticulocytes, as well as fetal liver nucleated erythroid cells. At much lower levels, expressed in hepatocytes and bone marrow-derived macrophages (at protein level). {ECO:0000269|PubMed:11689689, ECO:0000269|PubMed:17932563, ECO:0000269|PubMed:20071449}. DISEASE: Note=Defects in Eif2ak1 are a cause of hyperchromic anemia in animals suffering from iron deficiency. The number of red blood cells is decreased due to increased apoptosis of erythroid precursor cells, probably because globins misfold and aggregate in the absence of heme. +Q8BW22 CREST_MOUSE Calcium-responsive transactivator (SS18-like protein 1) 402 43,729 Chain (1); Compositional bias (1); Motif (4); Region (5); Sequence conflict (2) FUNCTION: Transcriptional activator which is required for calcium-dependent dendritic growth and branching in cortical neurons. Recruits CREB-binding protein (CREBBP) to nuclear bodies. Component of the CREST-BRG1 complex, a multiprotein complex that regulates promoter activation by orchestrating a calcium-dependent release of a repressor complex and a recruitment of an activator complex. In resting neurons, transcription of the c-FOS promoter is inhibited by BRG1-dependent recruitment of a phospho-RB1-HDAC1 repressor complex. Upon calcium influx, RB1 is dephosphorylated by calcineurin, which leads to release of the repressor complex. At the same time, there is increased recruitment of CREBBP to the promoter by a CREST-dependent mechanism, which leads to transcriptional activation. The CREST-BRG1 complex also binds to the NR2B promoter, and activity-dependent induction of NR2B expression involves a release of HDAC1 and recruitment of CREBBP. {ECO:0000269|PubMed:14716005, ECO:0000269|PubMed:19081374}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Note=Localizes to nuclear bodies. Colocalizes with SGO1 at kinetochore (By similarity). {ECO:0000250}. SUBUNIT: Homodimer. Dimerization may be necessary for its function in neuronal dendritic development. Interacts (via C-terminus) with CREBBP (via N-terminus), EP300 and SMARCA4/BRG1. Interacts with the nBAF complex. Association with CREBBP facilitates transcription while the association with SMARCA4/BRG1 suppresses CREST-mediated transcription in resting neurons (By similarity). {ECO:0000250}. DOMAIN: The MFD (multi-functional domain) domain is involved in transcription transactivation, nuclear body targeting and dimerization. {ECO:0000250}. +Q61502 E2F5_MOUSE Transcription factor E2F5 (E2F-5) 335 36,555 Chain (1); Compositional bias (1); DNA binding (1); Motif (1); Region (4); Sequence conflict (1) FUNCTION: Transcriptional activator that binds to E2F sites, these sites are present in the promoter of many genes whose products are involved in cell proliferation. May mediate growth factor-initiated signal transduction. It is likely involved in the early responses of resting cells to growth factor stimulation. Specifically required for multiciliate cell differentiation: together with MCIDAS and E2F5, binds and activate genes required for centriole biogenesis. {ECO:0000250|UniProtKB:Q6DE14}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Component of the DRTF1/E2F transcription factor complex. Binds cooperatively with DP-1 to E2F sites. Interaction with retinoblastoma protein RB1 or proteins RBL1 and RBL2 inhibits the E2F transactivation domain. Component of the DREAM complex (also named LINC complex) at least composed of E2F4, E2F5, LIN9, LIN37, LIN52, LIN54, MYBL1, MYBL2, RBL1, RBL2, RBBP4, TFDP1 and TFDP2. The complex exists in quiescent cells where it represses cell cycle-dependent genes. It dissociates in S phase when LIN9, LIN37, LIN52 and LIN54 form a subcomplex that binds to MYBL2 (By similarity). {ECO:0000250}. +P04344 CRGB_MOUSE Gamma-crystallin B (Gamma-B-crystallin) (Gamma-crystallin 3) 175 21,086 Chain (1); Domain (4); Region (1); Sequence conflict (3) FUNCTION: Crystallins are the dominant structural components of the vertebrate eye lens. DOMAIN: Has a two-domain beta-structure, folded into four very similar Greek key motifs. +Q8CIT0 CRF_MOUSE Corticoliberin (Corticotropin-releasing factor) (CRF) (Corticotropin-releasing hormone) 187 20,778 Modified residue (1); Peptide (1); Propeptide (1); Signal peptide (1) FUNCTION: Hormone regulating the release of corticotropin from pituitary gland. Induces NLRP6 in intestinal epithelial cells, hence may influence gut microbiota profile (PubMed:23470617). {ECO:0000250|UniProtKB:P06296, ECO:0000269|PubMed:23470617}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P06296}. SUBUNIT: Interacts (via C-terminus) with CRFR1 (via N-terminal extracellular domain). {ECO:0000250|UniProtKB:P06850}. TISSUE SPECIFICITY: Expressed in parvocellular paraventricular nucleus of the hypothalamus and in medial accessory olivary nucleus. {ECO:0000269|PubMed:19912808}. +P04342 CRGD_MOUSE Gamma-crystallin D (Gamma-D-crystallin) (Gamma-crystallin 1) 174 21,118 Chain (1); Domain (4); Region (1); Sequence conflict (6) FUNCTION: Crystallins are the dominant structural components of the vertebrate eye lens. DOMAIN: Has a two-domain beta-structure, folded into four very similar Greek key motifs. TISSUE SPECIFICITY: Detected in the superior olivary complex of the auditory hindbrain. {ECO:0000269|PubMed:27517863}. +Q03740 CRGE_MOUSE Gamma-crystallin E (Gamma-E-crystallin) 174 21,196 Chain (1); Domain (4); Region (1); Sequence conflict (5) FUNCTION: Crystallins are the dominant structural components of the vertebrate eye lens. DOMAIN: Has a two-domain beta-structure, folded into four very similar Greek key motifs. TISSUE SPECIFICITY: Detected in the superior olivary complex of the auditory hindbrain. {ECO:0000269|PubMed:27517863}. +Q6S7F2 E2F7_MOUSE Transcription factor E2F7 (E2F-7) 904 99,535 Alternative sequence (2); Chain (1); DNA binding (2); Frameshift (1); Modified residue (3); Sequence conflict (6) FUNCTION: Atypical E2F transcription factor that participates in various processes such as angiogenesis, polyploidization of specialized cells and DNA damage response. Mainly acts as a transcription repressor that binds DNA independently of DP proteins and specifically recognizes the E2 recognition site 5'-TTTC[CG]CGC-3'. Directly represses transcription of classical E2F transcription factors such as E2F1. Acts as a regulator of S-phase by recognizing and binding the E2-related site 5'-TTCCCGCC-3' and mediating repression of G1/S-regulated genes. Plays a key role in polyploidization of cells in placenta and liver by regulating the endocycle, probably by repressing genes promoting cytokinesis and antagonizing action of classical E2F proteins (E2F1, E2F2 and/or E2F3). Required for placental development by promoting polyploidization of trophoblast giant cells. Also involved in DNA damage response: up-regulated by p53/TP53 following genotoxic stress and acts as a downstream effector of p53/TP53-dependent repression by mediating repression of indirect p53/TP53 target genes involved in DNA replication. Acts as a promoter of sprouting angiogenesis, possibly by acting as a transcription activator: associates with HIF1A, recognizes and binds the VEGFA promoter, which is different from canonical E2 recognition site, and activates expression of the VEGFA gene. Acts as a negative regulator of keratinocyte differentiation. {ECO:0000269|PubMed:12893818, ECO:0000269|PubMed:18194653, ECO:0000269|PubMed:22180533, ECO:0000269|PubMed:22516201, ECO:0000269|PubMed:22802529, ECO:0000269|PubMed:22903062, ECO:0000269|PubMed:23064264, ECO:0000269|PubMed:23064266}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12893818}. SUBUNIT: Interacts with HIF1A (By similarity). Homodimer and heterodimer: mainly forms homodimers and, to a lesser extent, heterodimers with E2F8. Dimerization is important for DNA-binding. {ECO:0000250}. DOMAIN: In contrast to classical members of the E2F transcription factor, atypical members contain 2 DNA-binding domains and regulate transcription in a DP-independent manner. Both DNA-binding domains are required for DNA-binding and are proposed to form an intramolecular structure that is similar to the winged helix structure of the E2F-DP heterodimer (PubMed:12893818). {ECO:0000269|PubMed:12893818}. TISSUE SPECIFICITY: Widely expressed with highest levels in skin and thymus and very low levels in brain, muscle and stomach. Expressed in trophoblast giant cells throughout placenta development (at protein level). {ECO:0000269|PubMed:12893818, ECO:0000269|PubMed:22516201, ECO:0000269|PubMed:23064266}. +Q03401 CRIS1_MOUSE Cysteine-rich secretory protein 1 (CRISP-1) (Acidic epididymal glycoprotein 1) (Sperm-coating glycoprotein 1) (SCP 1) 244 27,680 Chain (1); Disulfide bond (5); Domain (2); Glycosylation (1); Signal peptide (1) FUNCTION: This protein is supposed to help spermatozoa undergo functional maturation while they move from the testis to the ductus deferens. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle. Note=Stored in secretory granules of granular convoluted tubules cells. TISSUE SPECIFICITY: Mainly found in the cauda epididymis where it is synthesized by the principal cells and secreted into the lumen. Binds to the heads of spermatozoa. Also expressed in the submandibular gland. +P16563 CRIS2_MOUSE Cysteine-rich secretory protein 2 (CRISP-2) (Testis-specific protein TPX-1) 243 27,605 Beta strand (1); Chain (1); Disulfide bond (5); Domain (2); Helix (3); Signal peptide (1) FUNCTION: May regulate some ion channels' activity and therebye regulate calcium fluxes during sperm capacitation. {ECO:0000269|PubMed:16339766}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. SUBUNIT: Interacts with NSUN4 isoform 3. {ECO:0000269|PubMed:19686095}. TISSUE SPECIFICITY: Testis. +Q9Z2H5 E41L1_MOUSE Band 4.1-like protein 1 (Neuronal protein 4.1) (4.1N) 879 98,315 Alternative sequence (2); Chain (1); Domain (1); Erroneous initiation (1); Modified residue (30); Region (3); Sequence conflict (11) FUNCTION: May function to confer stability and plasticity to neuronal membrane via multiple interactions, including the spectrin-actin-based cytoskeleton, integral membrane channels and membrane-associated guanylate kinases. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SUBUNIT: Interacts with AGAP2. {ECO:0000250}. TISSUE SPECIFICITY: Highest expression in brain, also present in kidney, olfactory epithelium, retina, sensory ganglia, gastrointestinal tract (only enteric neurons) and lung. +P52963 E41LA_MOUSE Band 4.1-like protein 4A (Protein NBL4) 686 78,533 Chain (1); Domain (1); Modified residue (4); Sequence conflict (1) SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. TISSUE SPECIFICITY: Brain, heart, lung, liver and spleen. Not detected in thymus and kidney. +P14847 CRP_MOUSE C-reactive protein 225 25,360 Chain (1); Disulfide bond (1); Domain (1); Metal binding (7); Sequence conflict (3); Signal peptide (1) FUNCTION: Displays several functions associated with host defense: it promotes agglutination, bacterial capsular swelling, phagocytosis and complement fixation through its calcium-dependent binding to phosphorylcholine. Can interact with DNA and histones and may scavenge nuclear material released from damaged circulating cells. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Homopentamer. Pentraxin (or pentaxin) have a discoid arrangement of 5 non-covalently bound subunits. Interacts with FCN1; may regulate monocyte activation by FCN1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Found in plasma. +Q9CYD3 CRTAP_MOUSE Cartilage-associated protein 400 46,169 Chain (1); Glycosylation (2); Sequence conflict (5); Signal peptide (1) FUNCTION: Necessary for efficient 3-hydroxylation of fibrillar collagen prolyl residues. {ECO:0000269|PubMed:17055431}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. TISSUE SPECIFICITY: Found in articular chondrocytes. Expressed in a variety of tissues. {ECO:0000269|PubMed:17055431}. DISEASE: Note=Defects in Crtap are a cause of osteochondrodysplasia characterized by severe osteoporosis and decreased osteoid production. {ECO:0000269|PubMed:17055431}. +Q8VHS2 CRUM1_MOUSE Protein crumbs homolog 1 1405 153,350 Alternative sequence (7); Chain (1); Disulfide bond (59); Domain (22); Glycosylation (11); Sequence conflict (24); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1340 1360 Helical. {ECO:0000255}. TOPO_DOM 28 1339 Extracellular. {ECO:0000255}.; TOPO_DOM 1361 1405 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a role in photoreceptor morphogenesis in the retina. May maintain cell polarization and adhesion. Isoform 3 could play a role in epidermal tissue morphogenesis. May function in cell attachment for stratified epithelial organization. {ECO:0000269|PubMed:12915475, ECO:0000269|PubMed:14684155, ECO:0000269|PubMed:15316081}. PTM: Glycosylated. {ECO:0000305}. SUBCELLULAR LOCATION: Isoform 1: Membrane; Single-pass type I membrane protein. Note=In the retina, localizes to the Mueller cell radial processes in the inner nuclear layer and in apical processes sclerad to the external limiting membrane. Localizes to the subapical region, adjacent to the adherens junction of photoreceptors. Isoform 3 which is secreted is found in the cytoplasmic area of undifferentiated keratinocytes and associates with the plasma membrane at the site of cell-cell contacts and focal adhesion upon keratinocytes differentiation. SUBUNIT: In photoreceptor cells, forms a complex with MPDZ, MPP4 and MPP5. TISSUE SPECIFICITY: Expressed exclusively in brain and proliferative retinoblasts of the eye. In the brain, expressed in the granular layer of the cerebellum, the hippocampal dentate gyrus, the olfactory bulbs, the subventricular region lining the telencephalic ventricles and the rostral migratory stream. Isoform 3 is ubiquitously expressed. {ECO:0000269|PubMed:11744384, ECO:0000269|PubMed:14684155}. DISEASE: Note=Defects in Crb1 are a cause of focal retinal dysplasia and degeneration associated with a shortening of inner and outer segments. Affected mice produce a secreted truncated protein that lacks the single transmembrane and the intracellular domain, and develop irregularities at the outer limiting membrane and loss of photoreceptor cells. {ECO:0000269|PubMed:12915475}. +Q9DAZ5 CS024_MOUSE Uncharacterized membrane protein C19orf24 homolog 108 12,374 Chain (1); Glycosylation (1); Modified residue (2); Sequence conflict (1); Signal peptide (1); Transmembrane (1) TRANSMEM 47 69 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q8R3Y5 CS047_MOUSE Uncharacterized protein C19orf47 homolog 413 44,410 Alternative sequence (4); Chain (1); Cross-link (1); Frameshift (1); Modified residue (5); Sequence conflict (14) +Q8CF25 CS067_MOUSE UPF0575 protein C19orf67 homolog 301 33,638 Chain (1); Frameshift (1); Sequence conflict (5) +A6H6Q4 CS071_MOUSE Uncharacterized protein C19orf71 homolog 206 23,954 Chain (1); Sequence conflict (1) +Q8CFG8 CS1B_MOUSE Complement C1s-B subcomponent (EC 3.4.21.42) (C1 esterase) (Complement component 1 subcomponent s-B) [Cleaved into: Complement C1s-B subcomponent heavy chain; Complement C1s-B subcomponent light chain] 688 76,700 Active site (3); Chain (3); Disulfide bond (13); Domain (6); Glycosylation (1); Metal binding (9); Modified residue (1); Signal peptide (1) FUNCTION: C1s B chain is a serine protease that combines with C1q and C1r to form C1, the first component of the classical pathway of the complement system. C1r activates C1s so that it can, in turn, activate C2 and C4 (By similarity). {ECO:0000250}. PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}. SUBUNIT: C1 is a calcium-dependent trimolecular complex of C1q, C1r and C1s in the molar ration of 1:2:2. Activated C1s is an disulfide-linked heterodimer of a heavy chain and a light chain (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Specifically expressed in male reproductive tissues. {ECO:0000269|PubMed:12513694}. +O54983 CRYM_MOUSE Ketimine reductase mu-crystallin (EC 1.5.1.25) (NADP-regulated thyroid-hormone-binding protein) 313 33,523 Beta strand (14); Binding site (2); Chain (1); Helix (14); Nucleotide binding (1); Turn (2) FUNCTION: Specifically catalyzes the reduction of imine bonds in brain substrates that may include cystathionine ketimine (CysK) and lanthionine ketimine (LK). Binds thyroid hormone which is a strong reversible inhibitor. Presumably involved in the regulation of the free intracellular concentration of triiodothyronine and access to its nuclear receptors (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +Q9R194 CRY2_MOUSE Cryptochrome-2 592 66,850 Beta strand (10); Binding site (3); Chain (1); Compositional bias (1); Cross-link (6); Domain (1); Helix (28); Modified residue (5); Mutagenesis (13); Nucleotide binding (1); Region (1); Sequence conflict (3); Turn (6) FUNCTION: Transcriptional repressor which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, ARNTL/BMAL1, ARNTL2/BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and ARNTL/BMAL1 or ARNTL2/BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-ARNTL/BMAL1|ARNTL2/BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress ARNTL/BMAL1 transcription, respectively. CRY1 and CRY2 have redundant functions but also differential and selective contributions at least in defining the pace of the SCN circadian clock and its circadian transcriptional outputs. Less potent transcriptional repressor in cerebellum and liver than CRY1, though less effective in lengthening the period of the SCN oscillator. Seems to play a critical role in tuning SCN circadian period by opposing the action of CRY1. With CRY1, dispensable for circadian rhythm generation but necessary for the development of intercellular networks for rhythm synchrony. May mediate circadian regulation of cAMP signaling and gluconeogenesis by blocking glucagon-mediated increases in intracellular cAMP concentrations and in CREB1 phosphorylation. Besides its role in the maintenance of the circadian clock, is also involved in the regulation of other processes. Plays a key role in glucose and lipid metabolism modulation, in part, through the transcriptional regulation of genes involved in these pathways, such as LEP or ACSL4. Represses glucocorticoid receptor NR3C1/GR-induced transcriptional activity by binding to glucocorticoid response elements (GREs). Represses the CLOCK-ARNTL/BMAL1 induced transcription of BHLHE40/DEC1 and NAMPT. {ECO:0000269|PubMed:10428031, ECO:0000269|PubMed:16628007, ECO:0000269|PubMed:17310242, ECO:0000269|PubMed:19299583, ECO:0000269|PubMed:20852621, ECO:0000269|PubMed:22170608, ECO:0000269|PubMed:23531614, ECO:0000269|PubMed:23575670, ECO:0000269|PubMed:23616524, ECO:0000269|PubMed:24154698}. PTM: Phosphorylation on Ser-265 by MAPK is important for the inhibition of CLOCK-ARNTL-mediated transcriptional activity. Phosphorylation by CSKNE requires interaction with PER1 or PER2. Phosphorylated in a circadian manner at Ser-553 and Ser-557 in the suprachiasmatic nucleus (SCN) and liver. Phosphorylation at Ser-557 by DYRK1A promotes subsequent phosphorylation at Ser-553 by GSK3-beta: the two-step phosphorylation at the neighboring Ser residues leads to its proteasomal degradation. {ECO:0000269|PubMed:11875063, ECO:0000269|PubMed:15298678, ECO:0000269|PubMed:15980066, ECO:0000269|PubMed:20123978}.; PTM: Ubiquitinated by the SCF(FBXL3) and SCF(FBXL21) complexes, regulating the balance between degradation and stabilization. The SCF(FBXL3) complex is mainly nuclear and mediates ubiquitination and subsequent degradation of CRY2. In contrast, cytoplasmic SCF(FBXL21) complex-mediated ubiquitination leads to stabilize CRY2 and counteract the activity of the SCF(FBXL3) complex. The SCF(FBXL3) and SCF(FBXL21) complexes probably mediate ubiquitination at different Lys residues. The SCF(FBXL3) complex recognizes and binds CRY2 phosphorylated at Ser-553 and Ser-557. Ubiquitination may be inhibited by PER2. {ECO:0000269|PubMed:15298678, ECO:0000269|PubMed:15980066, ECO:0000269|PubMed:17462724, ECO:0000269|PubMed:20123978, ECO:0000269|PubMed:23452855, ECO:0000269|PubMed:23452856}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Translocated to the nucleus through interaction with other Clock proteins such as PER2 or ARNTL. SUBUNIT: Component of the circadian core oscillator, which includes the CRY proteins, CLOCK or NPAS2, ARNTL/BMAL1 or ARNTL2/BMAL2, CSNK1D and/or CSNK1E, TIMELESS, and the PER proteins. Interacts directly with PER1 and PER2 C-terminal domains. Interaction with PER2 inhibits its ubiquitination and vice versa. Interacts with NFIL3. Interacts with FBXL3 and FBXL21. FBXL3, PER2 and the cofactor FAD compete for overlapping binding sites. FBXL3 cannot bind CRY2 that interacts already with PER2 or that contains bound FAD. Interacts with PPP5C (via TPR repeats); the interaction downregulates the PPP5C phosphatase activity on CSNK1E. AR, NR1D1, NR3C1/GR, RORA and RORC; the interaction, at least, with NR3C1/GR is ligand dependent. Interacts with PRKDC and CIART. {ECO:0000269|PubMed:10428031, ECO:0000269|PubMed:11875063, ECO:0000269|PubMed:14701732, ECO:0000269|PubMed:16628007, ECO:0000269|PubMed:16717091, ECO:0000269|PubMed:17274955, ECO:0000269|PubMed:17462724, ECO:0000269|PubMed:19917250, ECO:0000269|PubMed:20840750, ECO:0000269|PubMed:22170608, ECO:0000269|PubMed:23452855, ECO:0000269|PubMed:23452856, ECO:0000269|PubMed:23503662, ECO:0000269|PubMed:24080726, ECO:0000269|PubMed:24154698, ECO:0000269|PubMed:24158435, ECO:0000269|PubMed:24736997}. TISSUE SPECIFICITY: Expressed in all tissues examined including heart, brain, spleen, lung, liver, skeletal muscle, kidney and testis. Weak expression in spleen. {ECO:0000269|PubMed:10521578, ECO:0000269|PubMed:24154698, ECO:0000269|PubMed:9801304}. +Q8CBX0 CSC1_MOUSE Calcium permeable stress-gated cation channel 1 (Transmembrane protein 63C) 802 93,011 Chain (1); Modified residue (2); Transmembrane (10) TRANSMEM 33 53 Helical. {ECO:0000255}.; TRANSMEM 135 155 Helical. {ECO:0000255}.; TRANSMEM 182 202 Helical. {ECO:0000255}.; TRANSMEM 409 429 Helical. {ECO:0000255}.; TRANSMEM 455 475 Helical. {ECO:0000255}.; TRANSMEM 494 514 Helical. {ECO:0000255}.; TRANSMEM 540 560 Helical. {ECO:0000255}.; TRANSMEM 604 624 Helical. {ECO:0000255}.; TRANSMEM 655 675 Helical. {ECO:0000255}.; TRANSMEM 685 705 Helical. {ECO:0000255}. FUNCTION: Acts as an osmosensitive calcium-permeable cation channel. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +P43006 EAA2_MOUSE Excitatory amino acid transporter 2 (GLT-1) (Sodium-dependent glutamate/aspartate transporter 2) (Solute carrier family 1 member 2) 572 62,030 Alternative sequence (2); Binding site (3); Chain (1); Glycosylation (2); Intramembrane (2); Lipidation (1); Metal binding (5); Modified residue (12); Mutagenesis (1); Region (2); Sequence conflict (6); Topological domain (1); Transmembrane (8) INTRAMEM 344 374 Discontinuously helical. {ECO:0000250|UniProtKB:P43003}.; INTRAMEM 424 457 Discontinuously helical. {ECO:0000250|UniProtKB:P43003}. TRANSMEM 45 64 Helical. {ECO:0000255}.; TRANSMEM 88 108 Helical. {ECO:0000255}.; TRANSMEM 121 142 Helical. {ECO:0000255}.; TRANSMEM 235 258 Helical; Name=4. {ECO:0000250|UniProtKB:P43003}.; TRANSMEM 268 295 Helical; Name=5. {ECO:0000250|UniProtKB:P43003}.; TRANSMEM 317 338 Helical; Name=6. {ECO:0000250|UniProtKB:P43003}.; TRANSMEM 384 410 Helical; Name=7. {ECO:0000250|UniProtKB:P43003}.; TRANSMEM 471 492 Helical; Name=8. {ECO:0000250|UniProtKB:P43003}. TOPO_DOM 1 44 Cytoplasmic. {ECO:0000255}. FUNCTION: Sodium-dependent, high-affinity amino acid transporter that mediates the uptake of L-glutamate and also L-aspartate and D-aspartate (PubMed:7698742, PubMed:7557442, PubMed:9373176). Functions as a symporter that transports one amino acid molecule together with two or three Na(+) ions and one proton, in parallel with the counter-transport of one K(+) ion. Mediates Cl(-) flux that is not coupled to amino acid transport; this avoids the accumulation of negative charges due to aspartate and Na(+) symport (By similarity). Essential for the rapid removal of released glutamate from the synaptic cleft, and for terminating the postsynaptic action of glutamate (PubMed:9180080). {ECO:0000250|UniProtKB:P43004, ECO:0000269|PubMed:7557442, ECO:0000269|PubMed:7698742, ECO:0000269|PubMed:9180080, ECO:0000269|PubMed:9373176}. PTM: Glycosylated. {ECO:0000250|UniProtKB:P43004}.; PTM: Palmitoylation at Cys-38 is not required for correct subcellular localization, but is important for glutamate uptake activity. {ECO:0000269|PubMed:20685337}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7557442, ECO:0000269|PubMed:7698742, ECO:0000269|PubMed:9373176}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P43004}. SUBUNIT: Homotrimer (By similarity). Interacts with AJUBA (By similarity). {ECO:0000250|UniProtKB:P31596, ECO:0000250|UniProtKB:P43004}. DOMAIN: Contains eight transmembrane regions plus two helical hairpins that dip into the membrane. These helical hairpin structures play an important role in the transport process. The first enters the membrane from the cytoplasmic side, the second one from the extracellular side. During the transport cycle, the regions involved in amino acid transport, and especially the helical hairpins, move vertically by about 15-18 Angstroms, alternating between exposure to the aqueous phase and reinsertion in the lipid bilayer. In contrast, the regions involved in trimerization do not move. {ECO:0000250|UniProtKB:P43003}. TISSUE SPECIFICITY: Detected in brain (PubMed:9180080). Detected in embryonic forebrain, especially in globus pallidus, perirhinal cortex, lateral hypothalamus, hippocampus, and on fimbria and axonal pathways connecting the neocortex, basal ganglia and thalamus (at protein level) (PubMed:16880397). Isoform GLT1 is expressed in the brain (PubMed:7698742, PubMed:7557442, PubMed:9373176, PubMed:9180080). Isoforms GLT-1A and GLT-1B are expressed in the liver (PubMed:9373176). {ECO:0000269|PubMed:16880397, ECO:0000269|PubMed:7557442, ECO:0000269|PubMed:7698742, ECO:0000269|PubMed:9180080, ECO:0000269|PubMed:9373176}. +O35544 EAA4_MOUSE Excitatory amino acid transporter 4 (High-affinity neuronal glutamate transporter) (Sodium-dependent glutamate/aspartate transporter) (Solute carrier family 1 member 6) 561 60,784 Binding site (3); Chain (1); Glycosylation (3); Intramembrane (2); Metal binding (5); Modified residue (1); Region (2); Topological domain (1); Transmembrane (8) INTRAMEM 368 398 Discontinuously helical. {ECO:0000250|UniProtKB:P43003}.; INTRAMEM 448 481 Discontinuously helical. {ECO:0000250|UniProtKB:P43003}. TRANSMEM 53 73 Helical. {ECO:0000255}.; TRANSMEM 96 116 Helical. {ECO:0000255}.; TRANSMEM 130 150 Helical. {ECO:0000255}.; TRANSMEM 259 282 Helical; Name=4. {ECO:0000250|UniProtKB:P43003}.; TRANSMEM 292 319 Helical; Name=5. {ECO:0000250|UniProtKB:P43003}.; TRANSMEM 341 362 Helical; Name=6. {ECO:0000250|UniProtKB:P43003}.; TRANSMEM 408 434 Helical; Name=7. {ECO:0000250|UniProtKB:P43003}.; TRANSMEM 495 516 Helical; Name=8. {ECO:0000250|UniProtKB:P43003}. TOPO_DOM 1 52 Cytoplasmic. {ECO:0000255}. FUNCTION: Sodium-dependent, high-affinity amino acid transporter that mediates the uptake of L-glutamate and also L-aspartate and D-aspartate (PubMed:9379843). Functions as a symporter that transports one amino acid molecule together with two or three Na(+) ions and one proton, in parallel with the counter-transport of one K(+) ion. Mediates Cl(-) flux that is not coupled to amino acid transport; this avoids the accumulation of negative charges due to aspartate and Na(+) symport (By similarity). Plays a redundant role in the rapid removal of released glutamate from the synaptic cleft, which is essential for terminating the postsynaptic action of glutamate (Probable). {ECO:0000250|UniProtKB:O35921, ECO:0000269|PubMed:9379843, ECO:0000305}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9379843}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Homotrimer. {ECO:0000305}. DOMAIN: Contains eight transmembrane regions plus two helical hairpins that dip into the membrane. These helical hairpin structures play an important role in the transport process. The first enters the membrane from the cytoplasmic side, the second one from the extracellular side. During the transport cycle, the regions involved in amino acid transport, and especially the helical hairpins, move vertically by about 15-18 Angstroms, alternating between exposure to the aqueous phase and reinsertion in the lipid bilayer. In contrast, the regions involved in trimerization do not move. {ECO:0000250|UniProtKB:P43003}. TISSUE SPECIFICITY: Brain specific. {ECO:0000269|PubMed:9379843}. +Q6P9K8 CSKI1_MOUSE Caskin-1 (CASK-interacting protein 1) 1431 150,495 Alternative sequence (4); Chain (1); Compositional bias (2); Domain (3); Modified residue (19); Region (1); Repeat (6); Sequence conflict (3) FUNCTION: May link the scaffolding protein CASK to downstream intracellular effectors. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Binds the CaM kinase domain of CASK. Forms a ternary complex with CASK and LIN7A, LIN7B or LIN7C. Competes with APBA1 that forms a similar complex with CASK and LIN7 proteins. The tripartite complex CASKIN1/CASK/LIN7(A/B/C) binds the cytoplasmic tail of NRXN1. Polymerizes, via the tandem SAM domains, to form long, 8 nM wide fibers, upon which other proteins can assemble (By similarity). {ECO:0000250}. +O54833 CSK22_MOUSE Casein kinase II subunit alpha' (CK II alpha') (EC 2.7.11.1) 350 41,215 Active site (1); Binding site (1); Chain (1); Domain (1); Modified residue (5); Nucleotide binding (1) FUNCTION: Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response. During mitosis, functions as a component of the p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in response to spindle damage. Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation. Can also negatively regulate apoptosis. Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3. Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8. Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV. Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, SRF, MAX, JUN, FOS, MYC and MYB. Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function. Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1. Acts as an ectokinase that phosphorylates several extracellular proteins (By similarity). {ECO:0000250}. SUBUNIT: Heterotetramer composed of two catalytic subunits (alpha chain and/or alpha' chain) and two regulatory subunits (beta chains). The tetramer can exist as a combination of 2 alpha/2 beta, 2 alpha'/2 beta or 1 alpha/1 alpha'/2 beta subunits. Also part of a CK2-SPT16-SSRP1 complex composed of SSRP1, SUPT16H, CSNK2A1, CSNK2A2 and CSNK2B, which forms following UV irradiation. Interacts with RNPS1 (By similarity). Interacts with CSNKA2IP (via C-terminus) (PubMed:19273531). {ECO:0000250|UniProtKB:P19784, ECO:0000269|PubMed:19273531}. TISSUE SPECIFICITY: Highly expressed in brain, testis and mature epididymal spermatozoa. Weakly expressed in kidney, liver, lung, spleen and thymus (at protein level). {ECO:0000269|PubMed:10471512}. +Q9QUK0 CDKL2_MOUSE Cyclin-dependent kinase-like 2 (EC 2.7.11.22) (Serine/threonine-protein kinase KKIAMRE) 568 64,056 Active site (1); Alternative sequence (2); Binding site (1); Chain (1); Domain (1); Erroneous initiation (1); Motif (1); Nucleotide binding (1); Sequence conflict (4) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. DOMAIN: The [NKR]KIAxRE motif seems to be a cyclin-binding region. TISSUE SPECIFICITY: Expressed in testis, kidney, lung and brain. {ECO:0000269|PubMed:14605869}. +Q8BLF2 CDKL3_MOUSE Cyclin-dependent kinase-like 3 (EC 2.7.11.22) 595 67,739 Active site (1); Alternative sequence (9); Binding site (1); Chain (1); Domain (1); Modified residue (2); Motif (1); Nucleotide binding (1); Sequence conflict (4) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. DOMAIN: The [NKR]KIAxRE motif seems to be a cyclin-binding region. +O35161 CELR1_MOUSE Cadherin EGF LAG seven-pass G-type receptor 1 3034 330,471 Chain (1); Compositional bias (1); Disulfide bond (27); Domain (21); Glycosylation (23); Modified residue (6); Sequence conflict (5); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 2485 2505 Helical; Name=1. {ECO:0000255}.; TRANSMEM 2517 2537 Helical; Name=2. {ECO:0000255}.; TRANSMEM 2543 2563 Helical; Name=3. {ECO:0000255}.; TRANSMEM 2588 2608 Helical; Name=4. {ECO:0000255}.; TRANSMEM 2626 2646 Helical; Name=5. {ECO:0000255}.; TRANSMEM 2671 2691 Helical; Name=6. {ECO:0000255}.; TRANSMEM 2695 2715 Helical; Name=7. {ECO:0000255}. TOPO_DOM 30 2484 Extracellular. {ECO:0000255}.; TOPO_DOM 2506 2516 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 2538 2542 Extracellular. {ECO:0000255}.; TOPO_DOM 2564 2587 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 2609 2625 Extracellular. {ECO:0000255}.; TOPO_DOM 2647 2670 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 2692 2694 Extracellular. {ECO:0000255}.; TOPO_DOM 2716 3034 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor that may have an important role in cell/cell signaling during nervous system formation. PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed in the brain, where it is localized principally in the ependymal cell layer, choroid plexus and the area postrema. Also found in spinal chord and in the eye. {ECO:0000269|PubMed:9339365}. +P53568 CEBPG_MOUSE CCAAT/enhancer-binding protein gamma (C/EBP gamma) (Granulocyte colony-stimulating factor promoter element 1-binding protein) (GPE1-BP) (GPE1-binding protein) (Immunoglobulin enhancer-binding protein 1) (IG/EBP-1) 150 16,400 Chain (1); Cross-link (1); Domain (1); Erroneous initiation (1); Region (2) FUNCTION: Transcription factor that binds to the promoter and the enhancer regions of target genes (PubMed:21602272). Binds to the promoter and the enhancer of the immunoglobulin heavy chain (PubMed:2121606). Binds to GPE1, a cis-acting element in the G-CSF gene promoter (PubMed:1709121). Binds to the enhancer element PRE-I (positive regulatory element-I) of the IL-4 gene (By similarity). Binds to the promoter and the enhancer of the alpha-1-fetoprotein gene (By similarity). {ECO:0000250|UniProtKB:P26801, ECO:0000250|UniProtKB:P53567, ECO:0000269|PubMed:1709121, ECO:0000269|PubMed:2121606, ECO:0000269|PubMed:21602272}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:1709121, ECO:0000305|PubMed:2121606}. SUBUNIT: Binds DNA as a dimer and can form stable heterodimers with CEBPA (PubMed:2121606). Can form stable heterodimers with CEBPB (By similarity). Interacts with ZNF638; this interaction increases transcriptional activation (PubMed:21602272). {ECO:0000250|UniProtKB:P26801, ECO:0000269|PubMed:21602272}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:1709121, ECO:0000269|PubMed:2121606}. +P27790 CENPB_MOUSE Major centromere autoantigen B (Centromere protein B) (CENP-B) 599 65,381 Chain (1); Compositional bias (2); Cross-link (1); DNA binding (2); Domain (2); Initiator methionine (1); Modified residue (4); Region (1); Sequence conflict (2) FUNCTION: Interacts with centromeric heterochromatin in chromosomes and binds to a specific 17 bp subset of alphoid satellite DNA, called the CENP-B box. May organize arrays of centromere satellite DNA into a higher-order structure which then directs centromere formation and kinetochore assembly in mammalian chromosomes. {ECO:0000250|UniProtKB:P07199}. PTM: Poly-ADP-ribosylated by PARP1. {ECO:0000269|PubMed:12011073}.; PTM: N-terminally methylated by METTL11A/NTM1. Alpha-N-methylation is stimulated in response to extracellular stimuli, including increased cell density and heat shock, and seems to facilitate binding to CENP-B boxes. Chromatin-bound CENP-B is primarily trimethylated. {ECO:0000250|UniProtKB:P07199}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07199}. Chromosome, centromere {ECO:0000250|UniProtKB:P07199}. SUBUNIT: Antiparallel homodimer. Interacts with CENPT. Identified in a centromere complex containing histones H2A, H2B and H4, and at least CENPA, CENPB, CENPC, CENPT, CENPN, HJURP, SUPT16H, SSRP1 and RSF1. {ECO:0000250|UniProtKB:P07199}. +P49452 CENPC_MOUSE Centromere protein C (CENP-C) (Centromere autoantigen C) (Centromere protein C 1) (CENP-C 1) 906 102,154 Chain (1); Cross-link (10); Modified residue (12); Motif (4); Region (2); Sequence conflict (5) FUNCTION: Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. CENPC recruits DNA methylation and DNMT3B to both centromeric and pericentromeric satellite repeats and regulates the histone code in these regions. {ECO:0000250|UniProtKB:Q03188}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q03188}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q03188}. Chromosome, centromere {ECO:0000250|UniProtKB:Q03188}. Note=Localizes exclusively in the kinetochore domain of centromeres. {ECO:0000250|UniProtKB:Q03188}. SUBUNIT: Oligomer. Component of the CENPA-NAC complex, at least composed of CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and CENPU. The CENPA-NAC complex interacts with the CENPA-CAD complex, composed of CENPI, CENPK, CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS. Binds to DAXX. Interacts with DNMT3B. Interacts directly with CENPA. Identified in a centromere complex containing histones H2A, H2B and H4, and at least CENPA, CENPB, CENPC, CENPT, CENPN, HJURP, SUPT16H, SSRP1 and RSF1 (By similarity). Interacts with MEIKIN (PubMed:25533956). {ECO:0000250|UniProtKB:Q03188, ECO:0000269|PubMed:25533956}. DOMAIN: The MIF2 homology domain II targets centromeres and binds the alpha satellite DNA in vivo. The MIF2 homology domain III can induce CENPC dimerization/oligomerization. {ECO:0000250|UniProtKB:Q03188}. +Q64285 CEL_MOUSE Bile salt-activated lipase (BAL) (EC 3.1.1.13) (EC 3.1.1.3) (Bile salt-stimulated lipase) (BSSL) (Carboxyl ester lipase) (Cholesterol esterase) (Pancreatic lysophospholipase) (Sterol esterase) 599 65,813 Active site (3); Chain (1); Disulfide bond (2); Glycosylation (2); Region (1); Repeat (3); Signal peptide (1) FUNCTION: Catalyzes fat and vitamin absorption. Acts in concert with pancreatic lipase and colipase for the complete digestion of dietary triglycerides (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Interacts with CLC. {ECO:0000269|PubMed:11834744}. TISSUE SPECIFICITY: EXpressed by eosinophils. {ECO:0000269|PubMed:11834744}. +Q8BT07 CEP55_MOUSE Centrosomal protein of 55 kDa (Cep55) 462 53,930 Alternative sequence (1); Chain (1); Coiled coil (1); Modified residue (6); Natural variant (1); Region (3); Sequence conflict (7) FUNCTION: Plays a role in mitotic exit and cytokinesis. Recruits PDCD6IP and TSG101 to midbody during cytokinesis. Required for successful completion of cytokinesis. Not required for microtubule nucleation. Plays a role in the development of the brain and kidney. {ECO:0000250|UniProtKB:Q53EZ4}. PTM: There is a hierachy of phosphorylation, where both Ser-423 and Ser-426 are phosphorylated at the onset of mitosis, prior to Ser-434. Phosphorylation at Ser-423 and Ser-426 is required for dissociation from the centrosome at the G2/M boundary. Phosphorylation at the 3 sites, Ser-423, Ser-426 and Ser-434, is required for protein function at the final stages of cell division to complete cytokinesis successfully (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q53EZ4}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q53EZ4}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q53EZ4}. Cleavage furrow {ECO:0000250|UniProtKB:Q53EZ4}. Midbody, Midbody ring {ECO:0000250|UniProtKB:Q53EZ4}. Note=Present at the centrosomes at interphase. A small portion is associated preferentially with the mother centriole, whereas the majority localizes to the pericentriolar material. During mitosis, loses affinity for the centrosome at the onset of prophase and diffuses throughout the cell. This dissociation from the centrosome is phosphorylation-dependent. May remain localized at the centrosome during mitosis in certain cell types. Appears at the cleavage furrow in late anaphase and in the midbody in cytokinesis. {ECO:0000250|UniProtKB:Q53EZ4}. SUBUNIT: Homodimer. Interacts (phosphorylated on Ser-423 and Ser-426) with PLK1. Interacts with AKAP9/CG-NAP; the interaction occurs in interphase and is lost upon mitotic entry. Interacts with PCNT/Kendrin; the interaction occurs in interphase and is lost upon mitotic entry. Directly interacts with PDCD6IP; this interaction is required for PDCD6IP targeting to the midbody; CEP55 binds PDCD6IP in a 2:1 stoichiometry; PDCD6IP competes with TSG101 for the same binding site. Interacts with TSG101; TSG101 competes with PDCD6IP for the same binding site; interaction is required for cytokinesis. Interacts with MVB12A, VPS37B, VPS37C and VPS28 (By similarity). {ECO:0000250|UniProtKB:Q53EZ4}. +Q8C172 CERS6_MOUSE Ceramide synthase 6 (CerS6) (LAG1 longevity assurance homolog 6) 384 44,813 Chain (1); DNA binding (1); Domain (1); Glycosylation (1); Helix (3); Site (1); Topological domain (6); Transmembrane (5) TRANSMEM 35 55 Helical. {ECO:0000255}.; TRANSMEM 174 194 Helical. {ECO:0000255}.; TRANSMEM 205 225 Helical. {ECO:0000255}.; TRANSMEM 263 283 Helical. {ECO:0000255}.; TRANSMEM 303 323 Helical. {ECO:0000255}. TOPO_DOM 1 34 Lumenal. {ECO:0000255}.; TOPO_DOM 56 173 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 195 204 Lumenal. {ECO:0000255}.; TOPO_DOM 226 262 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 284 302 Lumenal. {ECO:0000255}.; TOPO_DOM 324 384 Cytoplasmic. {ECO:0000255}. FUNCTION: May be involved in sphingolipid synthesis or its regulation. {ECO:0000269|PubMed:15823095}. PTM: Glycosylation on Asn-18 is not necessary for function. {ECO:0000269|PubMed:15823095}. SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000255|PROSITE-ProRule:PRU00108}; Multi-pass membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:15823095}; Multi-pass membrane protein {ECO:0000269|PubMed:15823095}. TISSUE SPECIFICITY: Broadly expressed, with highest levels in kidney and brain. {ECO:0000269|PubMed:15823095}. +Q9DAY5 CF120_MOUSE UPF0669 protein C6orf120 homolog 185 20,945 Chain (1); Erroneous initiation (3); Frameshift (1); Glycosylation (1); Signal peptide (1) FUNCTION: May be involved in induction of apoptosis in CD4(+) T-cells, but not CD8(+) T-cells or hepatocytes. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Secreted by hepatocytes. {ECO:0000250}. +Q6IQY5 CEP70_MOUSE Centrosomal protein of 70 kDa (Cep70) 616 71,065 Alternative sequence (2); Chain (1); Coiled coil (2); Frameshift (1); Repeat (1); Sequence conflict (5) FUNCTION: Plays a role in the organization of both preexisting and nascent microtubules in interphase cells. During mitosis, required for the organization and orientation of the mitotic spindle (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. SUBUNIT: Directly interacts with tubulin-gamma; this interaction determines centrosomal localization. {ECO:0000250}. DOMAIN: The coiled-coil domains may be important for tubulin-gamma-binding and hence for centrosomal localization. {ECO:0000250}. +E9Q7R9 CFA43_MOUSE Cilia- and flagella-associated protein 43 1682 193,426 Chain (1); Coiled coil (2); Repeat (6) FUNCTION: Flagellar protein involved in sperm flagellum axoneme organization and function. {ECO:0000269|PubMed:28552195, ECO:0000269|PubMed:29449551}. SUBCELLULAR LOCATION: Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q57WH1}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:Q57WH1}. TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:28552195}. +Q497N7 CF201_MOUSE Uncharacterized protein C6orf201 homolog 227 26,076 Chain (1); Frameshift (2); Sequence conflict (3) +Q810M1 CF299_MOUSE Cilia- and flagella-associated protein 299 233 26,938 Chain (1) +Q6PE87 CF206_MOUSE Cilia- and flagella-associated protein 206 622 70,946 Alternative sequence (2); Chain (1); Erroneous gene model prediction (1); Erroneous initiation (2) FUNCTION: May regulate cilium motility through its role in the assembly of the axonemal radial spokes. {ECO:0000250|UniProtKB:Q23H79}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q23H79}. +Q5F201 CFA52_MOUSE Cilia- and flagella-associated protein 52 (WD repeat-containing protein 16) 620 68,240 Alternative sequence (2); Chain (1); Repeat (11); Sequence conflict (1) FUNCTION: May play a role in cell growth and/or survival. {ECO:0000250|UniProtKB:Q8N1V2}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8N1V2}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:A8ILK1}. SUBUNIT: Interacts with BRCA2. Interacts with the CCT chaperonin complex. Interacts with HSP70. {ECO:0000250|UniProtKB:Q8N1V2}. +Q8VCN5 CGL_MOUSE Cystathionine gamma-lyase (EC 4.4.1.1) (Cysteine-protein sulfhydrase) (Gamma-cystathionase) 398 43,567 Binding site (4); Chain (1); Modified residue (1) Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-homocysteine and L-serine: step 2/2. FUNCTION: Catalyzes the last step in the trans-sulfuration pathway from methionine to cysteine. Has broad substrate specificity. Converts cystathionine to cysteine, ammonia and 2-oxobutanoate. Converts two cysteine molecules to lanthionine and hydrogen sulfide. Can also accept homocysteine as substrate. Specificity depends on the levels of the endogenous substrates. Generates the endogenous signaling molecule hydrogen sulfide (H2S), and so contributes to the regulation of blood pressure. Acts as a cysteine-protein sulfhydrase by mediating sulfhydration of target proteins: sulfhydration consists of converting -SH groups into -SSH on specific cysteine residues of target proteins such as GAPDH, PTPN1 and NF-kappa-B subunit RELA, thereby regulating their function. {ECO:0000269|PubMed:18948540, ECO:0000269|PubMed:19903941, ECO:0000269|PubMed:22244329}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homotetramer (By similarity). Interacts with CALM in a calcium-dependent manner. {ECO:0000250, ECO:0000269|PubMed:18948540}. TISSUE SPECIFICITY: Detected in liver and kidney, and at lower levels in small intestine (at protein level). Highly expressed in liver and kidney. detected at lower levels in stomach, small intestine and adipose tissue. {ECO:0000269|PubMed:15038791}. +Q3U6N9 CH033_MOUSE UPF0488 protein C8orf33 homolog 222 24,465 Alternative sequence (2); Chain (1); Compositional bias (1); Initiator methionine (1); Modified residue (3) +Q61129 CFAI_MOUSE Complement factor I (EC 3.4.21.45) (C3B/C4B inactivator) [Cleaved into: Complement factor I heavy chain; Complement factor I light chain] 603 67,261 Active site (3); Calcium binding (2); Chain (3); Disulfide bond (21); Domain (5); Glycosylation (7); Sequence conflict (3); Signal peptide (1) FUNCTION: Trypsin-like serine protease that plays an essential role in regulating the immune response by controlling all complement pathways. Inhibits these pathways by cleaving three peptide bonds in the alpha-chain of C3b and two bonds in the alpha-chain of C4b thereby inactivating these proteins. Essential cofactors for these reactions include factor H and C4BP in the fluid phase and membrane cofactor protein/CD46 and CR1 on cell surfaces. The presence of these cofactors on healthy cells allows degradation of deposited C3b by CFI in order to prevent undesired complement activation, while in apoptotic cells or microbes, the absence of such cofactors leads to C3b-mediated complement activation and subsequent opsonization. {ECO:0000250|UniProtKB:P05156}. SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250|UniProtKB:P05156}. SUBUNIT: Heterodimer of a light and heavy chains; disulfide-linked. The fully processed and mature protein circulates as a zymogen, and is allosterically activated by substrate-induced remodeling of the active site. Interacts with C3b. Interacts with complement factor H. {ECO:0000250|UniProtKB:P05156}. TISSUE SPECIFICITY: Expressed in the liver by hepatocytes. Also present in other cells such as monocytes, fibroblasts or keratinocytes. {ECO:0000250|UniProtKB:P05156}. +Q9CXL3 CG050_MOUSE Uncharacterized protein C7orf50 homolog 195 22,168 Chain (1); Frameshift (1); Modified residue (4); Sequence conflict (3) +Q99LJ5 CKLF3_MOUSE CKLF-like MARVEL transmembrane domain-containing protein 3 (Chemokine-like factor superfamily member 3) 184 20,247 Chain (1); Domain (1); Frameshift (1); Sequence conflict (1); Transmembrane (3) TRANSMEM 64 84 Helical. {ECO:0000255}.; TRANSMEM 96 116 Helical. {ECO:0000255}.; TRANSMEM 131 151 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. +Q9CZ69 CKLF6_MOUSE CKLF-like MARVEL transmembrane domain-containing protein 6 (Chemokine-like factor superfamily member 6) 183 19,824 Chain (1); Domain (1); Modified residue (2); Sequence conflict (1); Topological domain (5); Transmembrane (4) TRANSMEM 46 66 Helical. {ECO:0000255}.; TRANSMEM 68 88 Helical. {ECO:0000255}.; TRANSMEM 107 127 Helical. {ECO:0000255}.; TRANSMEM 135 155 Helical. {ECO:0000255}. TOPO_DOM 1 45 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 67 67 Extracellular. {ECO:0000305}.; TOPO_DOM 89 106 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 128 134 Extracellular. {ECO:0000305}.; TOPO_DOM 156 183 Cytoplasmic. {ECO:0000305}. FUNCTION: Master regulator of recycling and plasma membrane expression of PD-L1/CD274, an immune inhibitory ligand critical for immune tolerance to self and antitumor immunity. Associates with both constitutive and IFNG-induced PD-L1/CD274 at recycling endosomes, where it protects PD-L1/CD274 from being targeted for lysosomal degradation, likely by preventing its ubiquitination. May stabilize PD-L1/CD274 expression on antigen presenting cells and potentiates inhibitory signaling by PDCD1/CD279, its receptor on T-cells, ultimately triggering T-cell anergy. {ECO:0000250|UniProtKB:Q9NX76}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9NX76}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:Q9NX76}; Multi-pass membrane protein {ECO:0000255}. Recycling endosome membrane {ECO:0000250|UniProtKB:Q9NX76}. Note=Co-localizes with PD-L1/CD274 in the plasma membrane and in recycling endosomes. {ECO:0000250|UniProtKB:Q9NX76}. SUBUNIT: Interacts with PD-L1/CD274 (via transmembrane domain); the interaction is direct. Interacts with CMTM4. Interacts with CD58, ARG1, ENO1 and TMPO. {ECO:0000250|UniProtKB:Q9NX76}. +Q9ESD6 CKLF7_MOUSE CKLF-like MARVEL transmembrane domain-containing protein 7 (Chemokine-like factor superfamily member 7) (LNV) 167 18,105 Alternative sequence (1); Chain (1); Domain (1); Transmembrane (4) TRANSMEM 35 55 Helical. {ECO:0000255}.; TRANSMEM 69 89 Helical. {ECO:0000255}.; TRANSMEM 102 122 Helical. {ECO:0000255}.; TRANSMEM 132 152 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. +Q9CR63 COX16_MOUSE Cytochrome c oxidase assembly protein COX16 homolog, mitochondrial 106 12,266 Alternative sequence (1); Chain (1); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 16 33 Helical. {ECO:0000255}. TOPO_DOM 1 15 Mitochondrial matrix. {ECO:0000250|UniProtKB:Q9P0S2}.; TOPO_DOM 34 106 Mitochondrial intermembrane. {ECO:0000250|UniProtKB:Q9P0S2}. FUNCTION: Required for the assembly of the mitochondrial respiratory chain complex IV (CIV), also known as cytochrome c oxidase. Promotes the insertion of copper into the active site of cytochrome c oxidase subunit II (MT-CO2/COX2). Interacts specifically with newly synthesized MT-CO2/COX and its copper center-forming metallochaperones SCO1, SCO2 and COA6. Probably facilitates MT-CO2/COX2 association with the MITRAC assembly intermediate containing MT-CO1/COX1, thereby participating in merging the MT-CO1/COX1 and MT-CO2/COX2 assembly lines. {ECO:0000250|UniProtKB:Q9P0S2}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9P0S2}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9P0S2}. SUBUNIT: Associates with the MITRAC complex. Interacts with MT-CO2/COX; specifically interacts with newly synthesized MT-CO2/COX. Interacts with SCO1, SCO2 and COA6. {ECO:0000250|UniProtKB:Q9P0S2}. +Q148W8 DUS27_MOUSE Inactive dual specificity phosphatase 27 1138 128,575 Chain (1); Compositional bias (2); Domain (1); Modified residue (9); Sequence conflict (2) FUNCTION: May be required for myofiber maturation. {ECO:0000250|UniProtKB:F1QWM2}. SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere {ECO:0000250|UniProtKB:F1QWM2}. +Q8BTR5 DUS28_MOUSE Dual specificity phosphatase 28 (EC 3.1.3.16) (EC 3.1.3.48) 163 17,505 Active site (1); Beta strand (6); Chain (1); Domain (1); Helix (6) FUNCTION: Has phosphatase activity with the synthetic substrate 6,8-difluoro-4-methylumbelliferyl phosphate (in vitro). Has almost no detectable activity with phosphotyrosine, even less activity with phosphothreonine and displays complete lack of activity with phosphoserine. The poor activity with phosphotyrosine may be due to steric hindrance by bulky amino acid sidechains that obstruct access to the active site. {ECO:0000250|UniProtKB:Q4G0W2}. SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q4G0W2}. +Q8CFY5 COX10_MOUSE Protoheme IX farnesyltransferase, mitochondrial (EC 2.5.1.141) (Heme O synthase) 443 48,884 Chain (1); Transit peptide (1); Transmembrane (7) TRANSMEM 174 194 Helical. {ECO:0000255}.; TRANSMEM 230 250 Helical. {ECO:0000255}.; TRANSMEM 252 272 Helical. {ECO:0000255}.; TRANSMEM 286 306 Helical. {ECO:0000255}.; TRANSMEM 308 328 Helical. {ECO:0000255}.; TRANSMEM 363 383 Helical. {ECO:0000255}.; TRANSMEM 410 430 Helical. {ECO:0000255}. FUNCTION: Converts protoheme IX and farnesyl diphosphate to heme O. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q9D7B1 DUS2L_MOUSE tRNA-dihydrouridine(20) synthase [NAD(P)+]-like (EC 1.3.1.-) (Dihydrouridine synthase 2) (tRNA-dihydrouridine synthase 2-like) 493 55,325 Active site (1); Beta strand (7); Binding site (3); Chain (1); Domain (1); Helix (3); Modified residue (1); Nucleotide binding (3); Turn (1) FUNCTION: Dihydrouridine synthase. Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs (By similarity). Negatively regulates the activation of EIF2AK2/PKR (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Note=Mainly at the endoplasmic reticulum. {ECO:0000250}. SUBUNIT: Interacts with EPRS. Interacts (via DRBM domain) with PRKRA and EIF2AK2/PKR (via DRBM 1 domain). {ECO:0000250}. +Q05922 DUS2_MOUSE Dual specificity protein phosphatase 2 (EC 3.1.3.16) (EC 3.1.3.48) (Dual specificity protein phosphatase PAC-1) 318 34,576 Active site (1); Alternative sequence (2); Chain (1); Domain (2); Sequence conflict (7) FUNCTION: Regulates mitogenic signal transduction by dephosphorylating both Thr and Tyr residues on MAP kinases ERK1 and ERK2. SUBCELLULAR LOCATION: Nucleus. TISSUE SPECIFICITY: In hematopoietic tissues such as spleen and thymus. +Q6P8I6 COX11_MOUSE Cytochrome c oxidase assembly protein COX11, mitochondrial 275 30,849 Chain (1); Topological domain (2); Transit peptide (1); Transmembrane (1) TRANSMEM 95 113 Helical. {ECO:0000255}. TOPO_DOM ? 94 Mitochondrial matrix. {ECO:0000250|UniProtKB:Q9Y6N1}.; TOPO_DOM 114 275 Mitochondrial intermembrane. {ECO:0000250|UniProtKB:Q9Y6N1}. FUNCTION: Exerts its effect at some terminal stage of cytochrome c oxidase synthesis, probably by being involved in the insertion of the copper B into subunit I. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9Y6N1}; Single-pass membrane protein {ECO:0000255}; Intermembrane side {ECO:0000250|UniProtKB:Q9Y6N1}. SUBUNIT: Interacts with CNNM4/ACDP4. {ECO:0000250}. +Q8BH51 COX14_MOUSE Cytochrome c oxidase assembly protein COX14 57 6,380 Chain (1); Transmembrane (1) TRANSMEM 15 37 Helical. {ECO:0000255}. FUNCTION: Core component of the MITRAC (mitochondrial translation regulation assembly intermediate of cytochrome c oxidase complex) complex, that regulates cytochrome c oxidase assembly. Requires for coordination of the early steps of cytochrome c oxidase assembly with the synthesis of MT-CO1. {ECO:0000250|UniProtKB:Q96I36}. SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. SUBUNIT: Along with COA3, core component of the MITRAC (mitochondrial translation regulation assembly intermediate of cytochrome c oxidase complex) complex. {ECO:0000250|UniProtKB:Q96I36}. +Q9D7X3 DUS3_MOUSE Dual specificity protein phosphatase 3 (EC 3.1.3.16) (EC 3.1.3.48) (T-DSP11) (Vaccinia H1-related phosphatase) (VHR) 185 20,472 Active site (1); Chain (1); Domain (1) FUNCTION: Shows activity both for tyrosine-protein phosphate and serine-protein phosphate, but displays a strong preference toward phosphotyrosines. Specifically dephosphorylates and inactivates ERK1 and ERK2 (By similarity). {ECO:0000250, ECO:0000269|PubMed:16845380}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16845380}. SUBUNIT: Interacts with VRK3, which seems to activate it's phosphatase activity. {ECO:0000269|PubMed:16845380}. +Q32M08 DUS4L_MOUSE tRNA-dihydrouridine(20a/20b) synthase [NAD(P)+]-like (EC 1.3.1.-) (tRNA-dihydrouridine synthase 4-like) 324 36,620 Active site (1); Binding site (3); Chain (1); Nucleotide binding (3); Sequence conflict (1) FUNCTION: Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs. {ECO:0000250}. +Q8BFV3 DUS4_MOUSE Dual specificity protein phosphatase 4 (EC 3.1.3.16) (EC 3.1.3.48) 398 43,372 Active site (1); Chain (1); Domain (2); Initiator methionine (1); Modified residue (3) FUNCTION: Regulates mitogenic signal transduction by dephosphorylating both Thr and Tyr residues on MAP kinases ERK1 and ERK2. {ECO:0000250|UniProtKB:Q13115}. PTM: Phosphorylation in the C-terminus by ERK1/2 inhibits proteasomal degradation and stabilizes the protein. {ECO:0000250|UniProtKB:Q13115}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13115}. SUBUNIT: Hollow spherical complex composed of 24 subunits with pseudooctahedral symmetry, has a tetramer as the basic unit. {ECO:0000250|UniProtKB:Q13115}. +P00397 COX1_MOUSE Cytochrome c oxidase subunit 1 (EC 1.9.3.1) (Cytochrome c oxidase polypeptide I) 514 56,910 Chain (1); Cross-link (1); Metal binding (7); Sequence conflict (6); Transmembrane (12) TRANSMEM 17 37 Helical. {ECO:0000255}.; TRANSMEM 56 76 Helical. {ECO:0000255}.; TRANSMEM 102 122 Helical. {ECO:0000255}.; TRANSMEM 145 165 Helical. {ECO:0000255}.; TRANSMEM 183 203 Helical. {ECO:0000255}.; TRANSMEM 234 254 Helical. {ECO:0000255}.; TRANSMEM 268 288 Helical. {ECO:0000255}.; TRANSMEM 310 330 Helical. {ECO:0000255}.; TRANSMEM 338 358 Helical. {ECO:0000255}.; TRANSMEM 380 400 Helical. {ECO:0000255}.; TRANSMEM 414 434 Helical. {ECO:0000255}.; TRANSMEM 456 476 Helical. {ECO:0000255}. Energy metabolism; oxidative phosphorylation. FUNCTION: Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SUBUNIT: As a newly synthesized protein, rapidly incorporates into a multi-subunit assembly intermediate in the inner membrane, called MITRAC (mitochondrial translation regulation assembly intermediate of cytochrome c oxidase) complex, whose core components are COA3/MITRAC12 and COX14. Within the MITRAC complex, interacts with COA3 and with SMIM20/MITRAC7; the interaction with SMIM20 stabilizes the newly synthesized MT-CO1 and prevents its premature turnover. Interacts with TMEM177 in a COX20-dependent manner. {ECO:0000250|UniProtKB:P00395}. +Q14AM7 CP072_MOUSE UPF0472 protein C16orf72 homolog 275 30,940 Chain (1); Frameshift (1); Modified residue (2); Sequence conflict (1) +P28649 CP19A_MOUSE Aromatase (EC 1.14.14.14) (CYPXIX) (Cytochrome P-450AROM) (Cytochrome P450 19A1) (Estrogen synthase) 503 58,015 Binding site (2); Chain (1); Metal binding (1) FUNCTION: Catalyzes the formation of aromatic C18 estrogens from C19 androgens. SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein. +Q80VN0 CP100_MOUSE Cilia- and flagella-associated protein 100 (Coiled-coil domain-containing protein 37) 613 72,033 Chain (1); Coiled coil (4); Erroneous initiation (2); Sequence caution (2); Sequence conflict (1) FUNCTION: May play a role in ciliary/flagellar motility by regulating the assembly and the activity of axonemal inner dynein arm. {ECO:0000250|UniProtKB:A8I4E9}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:A8I4E9}. +O54750 CP2J6_MOUSE Cytochrome P450 2J6 (EC 1.14.14.1) (Arachidonic acid epoxygenase) (CYPIIJ6) 501 57,792 Chain (1); Metal binding (1); Sequence conflict (1) SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. +Q6P5D4 CP135_MOUSE Centrosomal protein of 135 kDa (Cep135) (Centrosomal protein 4) 1140 133,345 Chain (1); Coiled coil (4); Modified residue (5) FUNCTION: Centrosomal protein involved in centriole biogenesis. Acts as a scaffolding protein during early centriole biogenesis. Required for the targeting of centriole satellite proteins to centrosomes such as of PCM1, SSX2IP and CEP290 and recruitment of WRAP73 to centrioles. Also required for centriole-centriole cohesion during interphase by acting as a platform protein for CEP250 at the centriole. Required for the recruitment of CEP295 to the proximal end of new-born centrioles at the centriolar microtubule wall during early S phase in a PLK4-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q66GS9}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:11781336}. Note=During centriole biogenesis, it is concentrated within the proximal lumen of both parental centrioles and procentrioles. {ECO:0000250|UniProtKB:Q66GS9}. SUBUNIT: Interacts with CEP250 (By similarity). Interacts with DCTN2. {ECO:0000250|UniProtKB:Q66GS9, ECO:0000269|PubMed:14983524}. +Q9EP75 CP4FE_MOUSE Leukotriene-B4 omega-hydroxylase 3 (EC 1.14.14.94) (Cyp4f-14) (Cytochrome P450 4F14) (Cytochrome P450-LTB-omega) (Leukotriene-B4 20-monooxygenase 3) 524 59,800 Binding site (1); Chain (1); Metal binding (1) Lipid metabolism; leukotriene B4 degradation. FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. Catalyzes the omega-hydroxylation of LTB4 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Microsome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. +Q64441 CP24A_MOUSE 1,25-dihydroxyvitamin D(3) 24-hydroxylase, mitochondrial (24-OHase) (Vitamin D(3) 24-hydroxylase) (EC 1.14.15.16) (Cytochrome P450 24A1) (Cytochrome P450-CC24) 514 59,453 Chain (1); Metal binding (1); Transit peptide (1) FUNCTION: Has a role in maintaining calcium homeostasis. Catalyzes the adrenodoxin-dependent 24-hydroxylation of calcidiol (25-hydroxyvitamin D(3)) and calcitriol (1-alpha,25-dihydroxyvitamin D(3)). The enzyme can perform up to 6 rounds of hydroxylation of calcitriol leading to calcitroic acid. {ECO:0000250|UniProtKB:Q09128}. SUBCELLULAR LOCATION: Mitochondrion. +P24457 CP2DB_MOUSE Cytochrome P450 2D11 (EC 1.14.14.1) (CYPIID11) (Cytochrome P450-16-alpha) (Cytochrome P450CC) (Testosterone 16-alpha hydroxylase) 504 56,988 Chain (1); Metal binding (1); Sequence conflict (16) FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. +Q9D816 CP255_MOUSE Cytochrome P450 2C55 (EC 1.14.14.1) (CYPIIC55) 490 56,096 Chain (1); Metal binding (1) FUNCTION: Metabolizes arachidonic acid mainly to 19-hydroxyeicosatetraenoic acid (HETE). {ECO:0000269|PubMed:15102943}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. TISSUE SPECIFICITY: Highest level in colon. Low levels in liver and small intestine. {ECO:0000269|PubMed:15102943}. +Q8C008 DZAN1_MOUSE Double zinc ribbon and ankyrin repeat-containing protein 1 778 85,025 Chain (1); Frameshift (1); Modified residue (3); Repeat (2); Sequence caution (1); Sequence conflict (3); Zinc finger (2) +Q6NVF9 CPSF6_MOUSE Cleavage and polyadenylation specificity factor subunit 6 551 59,153 Chain (1); Compositional bias (2); Domain (1); Modified residue (2); Motif (1); Region (8); Sequence conflict (3) FUNCTION: Component of the cleavage factor Im (CFIm) complex that functions as an activator of the pre-mRNA 3'-end cleavage and polyadenylation processing required for the maturation of pre-mRNA into functional mRNAs. CFIm contributes to the recruitment of multiprotein complexes on specific sequences on the pre-mRNA 3'-end, so called cleavage and polyadenylation signals (pA signals). Most pre-mRNAs contain multiple pA signals, resulting in alternative cleavage and polyadenylation (APA) producing mRNAs with variable 3'-end formation. The CFIm complex acts as a key regulator of cleavage and polyadenylation site choice during APA through its binding to 5'-UGUA-3' elements localized in the 3'-untranslated region (UTR) for a huge number of pre-mRNAs. CPSF6 enhances NUDT21/CPSF5 binding to 5'-UGUA-3' elements localized upstream of pA signals and promotes RNA looping, and hence activates directly the mRNA 3'-processing machinery. Plays a role in mRNA export. {ECO:0000250|UniProtKB:Q16630}. PTM: Phosphorylated. Phosphorylated in the Arg/Ser-rich domain by SRPK1, in vitro. {ECO:0000250|UniProtKB:Q16630}.; PTM: Symmetrically dimethylated on arginine residues by PRMT5 in a WDR77- and CLNS1A-dependent manner. Asymmetrically dimethylated on arginine residues by PRMT1. {ECO:0000250|UniProtKB:Q16630}.; PTM: Symmetrically dimethylated on arginine residues in the GAR motif by PRMT5 in a WDR77- and CLNS1A-dependent manner. Asymmetrically dimethylated on arginine residues in the GAR motif by PRMT1. {ECO:0000250|UniProtKB:Q16630}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18032416}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q16630}. Nucleus speckle {ECO:0000250|UniProtKB:Q16630}. Cytoplasm {ECO:0000250|UniProtKB:Q16630}. Note=Shuttles between the nucleus and the cytoplasm in a transcription- and XPO1/CRM1-independent manner, most probably in complex with the cleavage factor Im complex (CFIm). Colocalizes with PSPC1 in punctate subnuclear structures often located adjacent to nuclear speckles, called paraspeckles, and corresponding to interchromatin granules-associated zones (IGAZs). Distribution in speckles and paraspeckles varies during the cell cycle. Associates at sites of active transcription on nascent perichromatin fibrils (PFs) and perichromatin granules. {ECO:0000250|UniProtKB:Q16630}. SUBUNIT: Component of the cleavage factor Im (CFIm) complex which is an heterotetramer composed of two subunits of NUDT21/CPSF5 and two subunits of CPSF6 or CPSF7 or an heterodimer of CPSF6 and CPSF7. The cleavage factor Im (CFIm) complex associates with the CPSF and CSTF complexes to promote the assembly of the core mRNA 3'-processing machinery. Associates with the exon junction complex (EJC). Associates with the 80S ribosome particle. Interacts (via the RRM domain) with NUDT21/CPSF5; this interaction is direct and enhances binding to RNA. Interacts (via Arg/Ser-rich domain) with FIP1L1 (preferentially via unphosphorylated form and Arg/Glu/Asp-rich region); this interaction mediates, at least in part, the interaction between the CFIm and CPSF complexes and may be inhibited by CPSF6 hyper-phosphorylation. Interacts (via N-terminus) with NXF1; this interaction is direct. Interacts with SRSF3. Interacts with SRSF7. Interacts with SNRNP70. Interacts with TRA2B/SFRS10. Interacts with UPF1. Interacts with UPF3B. Interacts with VIRMA. {ECO:0000250|UniProtKB:Q16630}. DOMAIN: Contains an Arg/Ser-rich domain composed of arginine-serine dipeptide repeats within the C-terminal region that is necessary and sufficient for activating mRNA 3'-processing and alternative polyadenylation (APA). {ECO:0000250|UniProtKB:Q16630}. TISSUE SPECIFICITY: Expressed in testis (PubMed:18032416). Expressed in male germ cells (at protein level) (PubMed:18032416). {ECO:0000269|PubMed:18032416}. +Q9Z140 CPNE6_MOUSE Copine-6 (Copine VI) (Neuronal-copine) (N-copine) 557 61,781 Chain (1); Domain (3); Mutagenesis (20); Region (1) FUNCTION: Calcium-dependent phospholipid-binding protein that plays a role in calcium-mediated intracellular processes. Binds phospholipid membranes in a calcium-dependent manner (PubMed:9886090). Plays a role in dendrite formation by melanocytes (By similarity). {ECO:0000250|UniProtKB:O95741, ECO:0000269|PubMed:9886090}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21087455, ECO:0000269|PubMed:9886090}. Cell membrane {ECO:0000269|PubMed:21087455, ECO:0000269|PubMed:26175110}. Endosome {ECO:0000269|PubMed:21087455}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:21087455}. Perikaryon {ECO:0000269|PubMed:9886090}. Cell projection, dendrite {ECO:0000269|PubMed:9886090}. Note=Mainly cytoplasmic in absence of calcium. Associated predominantly with membranes in presence of calcium (PubMed:9886090). Translocates to the cell membrane in a calcium-dependent manner (PubMed:21087455, PubMed:26175110). Colocalized with transferrin in intracellular clathrin-coated membrane vesicles in a calcium-dependent manner (PubMed:21087455). {ECO:0000269|PubMed:21087455, ECO:0000269|PubMed:26175110, ECO:0000269|PubMed:9886090}. SUBUNIT: Interacts (via second C2 domain) with OS9 (via C-terminus); this interaction occurs in a calcium-dependent manner in vitro (PubMed:10403379). May interact with NECAB1 (By similarity). {ECO:0000250|UniProtKB:O95741, ECO:0000269|PubMed:10403379}. DOMAIN: The C2 domain 1 binds phospholipids in a calcium-independent manner and is not necessary for calcium-mediated translocation and association to the plasma membrane (PubMed:9886090, PubMed:26175110). The C2 domain 2 binds phospholipids in a calcium-dependent manner and is necessary for calcium-mediated translocation and association to the plasma membrane (PubMed:9886090, PubMed:26175110). The linker region contributes to the calcium-dependent translocation and association to the plasma membrane (PubMed:21087455, PubMed:26175110). The VWFA domain is necessary for association with intracellular clathrin-coated vesicles in a calcium-dependent manner (PubMed:21087455). {ECO:0000269|PubMed:21087455, ECO:0000269|PubMed:26175110, ECO:0000269|PubMed:9886090}. TISSUE SPECIFICITY: Expressed in the brain (PubMed:9645480). Expressed in pyramidal cells, granule cells, and neurons in the dentate gyrus of the hippocampus and in granule cells of the olfactory bulb (at protein level). Expressed in pyramidal cells of the CA1-CA3 regions, in granule cells of the dentate gyrus, in granule cells of the olfactory bulbs, in the mitral cell layer and in neurons of the cerebral cortex layer II, brainstem and spinal cord (PubMed:9886090). Not detected in glial cells (PubMed:9645480, PubMed:9886090). {ECO:0000269|PubMed:9645480, ECO:0000269|PubMed:9886090}. +P84086 CPLX2_MOUSE Complexin-2 (921-L) (Complexin II) (CPX II) (Synaphin-1) 134 15,394 Chain (1); Coiled coil (1); Modified residue (1); Region (1) FUNCTION: Negatively regulates the formation of synaptic vesicle clustering at active zone to the presynaptic membrane in postmitotic neurons. Positively regulates a late step in exocytosis of various cytoplasmic vesicles, such as synaptic vesicles and other secretory vesicles (PubMed:11163241, PubMed:23345244). Also involved in mast cell exocytosis (PubMed:11163241). Although not essential for development, seems critical for the acquisition of higher cognitive functions in the adult brain (PubMed:12915444). {ECO:0000269|PubMed:11163241, ECO:0000269|PubMed:12915444, ECO:0000269|PubMed:20346398, ECO:0000269|PubMed:23345244}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:7635198}. Note=Enriched at synaptic-releasing sites in mature neurons. SUBUNIT: Binds to the SNARE core complex containing SNAP25, VAMP2 and STX1A. {ECO:0000250}. TISSUE SPECIFICITY: Nervous system. Expressed predominantly in brain, where it is present in many regions, including hippocampus and cerebellum. In the retina, present at conventional amacrine cell synapses (at protein level). {ECO:0000269|PubMed:15911881, ECO:0000269|PubMed:7635198}. +Q8BGJ3 CQ100_MOUSE Uncharacterized protein C17orf100 homolog 129 14,539 Chain (1); Sequence conflict (1) +Q0PHV7 DACT3_MOUSE Dapper homolog 3 (Dapper antagonist of catenin 3) 610 63,287 Chain (1); Coiled coil (1); Compositional bias (2); Modified residue (6); Motif (1) FUNCTION: May be involved in regulation of intracellular signaling pathways during development. Specifically thought to play a role in canonical and/or non-canonical Wnt signaling pathways through interaction with DSH (Dishevelled) family proteins (By similarity). {ECO:0000250}. SUBUNIT: Can form homodimers and heterodimers with DACT1 or DACT3. Interacts with CSNK1D, PKA catalytic subunit, PKC-type kinase, DVL1, DVL2, DVL3, VANGL1, VANGL2 and CTNND1. {ECO:0000269|PubMed:21718540}. DOMAIN: The C-terminal PDZ-binding motif may mediate interaction with the PDZ domains of DSH (Dishevelled) family proteins. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain and uterus. {ECO:0000269|PubMed:16881060}. +Q61475 DAF1_MOUSE Complement decay-accelerating factor, GPI-anchored (DAF-GPI) (CD antigen CD55) 390 42,618 Chain (1); Compositional bias (1); Disulfide bond (8); Domain (4); Glycosylation (2); Lipidation (1); Propeptide (1); Sequence conflict (16); Signal peptide (1) FUNCTION: This protein recognizes C4b and C3b fragments that condense with cell-surface hydroxyl or amino groups when nascent C4b and C3b are locally generated during C4 and c3 activation. Interaction of daf with cell-associated C4b and C3b polypeptides interferes with their ability to catalyze the conversion of C2 and factor B to enzymatically active C2a and Bb and thereby prevents the formation of C4b2a and C3bBb, the amplification convertases of the complement cascade. Inhibits complement activation by destabilizing and preventing the formation of C3 and C5 convertases, which prevents complement damage. {ECO:0000250|UniProtKB:P08174}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. DOMAIN: The first Sushi domain (SCR1) is not necessary for function. SCR2 and SCR4 provide the proper conformation for the active site on SCR3 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Brain, secretory epithelia, skeletal muscle, liver, testes, thymus, spleen and lymph node. +Q9QXT1 DAPP1_MOUSE Dual adapter for phosphotyrosine and 3-phosphotyrosine and 3-phosphoinositide (mDAPP1) (B lymphocyte adapter protein Bam32) (B-cell adapter molecule of 32 kDa) 280 32,167 Chain (1); Domain (2); Modified residue (2); Sequence conflict (1) FUNCTION: May act as a B-cell-associated adapter that regulates B-cell antigen receptor (BCR)-signaling downstream of PI3K. PTM: Phosphorylated on tyrosine residues. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Membrane-associated after cell stimulation leading to its translocation. {ECO:0000250}. SUBUNIT: Interacts with PtdIns(3,4,5)P3 and PLCG2. {ECO:0000250}. +Q80YE7 DAPK1_MOUSE Death-associated protein kinase 1 (DAP kinase 1) (EC 2.7.11.1) 1442 161,442 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Domain (3); Erroneous initiation (1); Modified residue (7); Nucleotide binding (1); Region (2); Repeat (10); Sequence conflict (9) FUNCTION: Calcium/calmodulin-dependent serine/threonine kinase involved in multiple cellular signaling pathways that trigger cell survival, apoptosis, and autophagy. Regulates both type I apoptotic and type II autophagic cell deaths signal, depending on the cellular setting. The former is caspase-dependent, while the latter is caspase-independent and is characterized by the accumulation of autophagic vesicles. Phosphorylates PIN1 resulting in inhibition of its catalytic activity, nuclear localization, and cellular function. Phosphorylates TPM1, enhancing stress fiber formation in endothelial cells. Phosphorylates STX1A and significantly decreases its binding to STXBP1. Phosphorylates PRKD1 and regulates JNK signaling by binding and activating PRKD1 under oxidative stress. Phosphorylates BECN1, reducing its interaction with BCL2 and BCL2L1 and promoting the induction of autophagy. Phosphorylates TSC2, disrupting the TSC1-TSC2 complex and stimulating mTORC1 activity in a growth factor-dependent pathway. Phosphorylates RPS6, MYL9 and DAPK3 (By similarity). Acts as a signaling amplifier of NMDA receptors at extrasynaptic sites for mediating brain damage in stroke. Cerebral ischemia recruits DAPK1 into the NMDA receptor complex and it phosphorylates GRINB at Ser-1303 inducing injurious Ca(2+) influx through NMDA receptor channels, resulting in an irreversible neuronal death. Required together with DAPK3 for phosphorylation of RPL13A upon interferon-gamma activation which is causing RPL13A involvement in transcript-selective translation inhibition. {ECO:0000250, ECO:0000269|PubMed:11485996, ECO:0000269|PubMed:18806755, ECO:0000269|PubMed:20141836, ECO:0000269|PubMed:23071094}. PTM: Ubiquitinated by the BCR(KLHL20) E3 ubiquitin ligase complex, leading to its degradation by the proteasome. {ECO:0000250}.; PTM: In response to mitogenic stimulation (PMA or EGF), phosphorylated at Ser-289; phosphorylation suppresses DAPK1 pro-apoptotic function. Autophosphorylation at Ser-308 inhibits its catalytic activity. Phosphorylation at Ser-734 by MAPK1 increases its catalytic activity and promotes cytoplasmic retention of MAPK1. Endoplasmic-stress can cause dephosphorylation at Ser-308. {ECO:0000269|PubMed:15729359, ECO:0000269|PubMed:20141836}. SUBUNIT: Interacts with KLHL20. Interacts (via death domain) with MAPK1 and MAPK3. Interacts with MAP1B (via N-terminus). Interacts with PRKD1 in an oxidative stress-regulated manner. Interacts with PIN1, PDCD6, BECN1, TSC2 and STX1A (By similarity). Interacts (via death domain) with UNC5B (via death domain). Interacts with GRINB. {ECO:0000250, ECO:0000269|PubMed:15729359, ECO:0000269|PubMed:20141836}. DOMAIN: The autoinhibitory domain sterically blocks the substrate peptide-binding site by making both hydrophobic and electrostatic contacts with the kinase core. TISSUE SPECIFICITY: High levels in bladder, uterus, vas deferens, lung, liver and kidney. {ECO:0000269|PubMed:11485996}. +A2AKB9 DCA10_MOUSE DDB1- and CUL4-associated factor 10 (WD repeat-containing protein 32) 566 61,558 Alternative sequence (3); Chain (1); Compositional bias (1); Erroneous gene model prediction (1); Erroneous initiation (3); Modified residue (8); Repeat (7); Sequence conflict (3) Protein modification; protein ubiquitination. FUNCTION: May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex. {ECO:0000250}. SUBUNIT: Interacts with DDB1. {ECO:0000250}. +Q6PFH3 DCA15_MOUSE DDB1- and CUL4-associated factor 15 600 66,643 Alternative sequence (1); Chain (1); Modified residue (2); Sequence conflict (1) Protein modification; protein ubiquitination. FUNCTION: May be involved in ubiquitination and degradation through a DBB1-CUL4 E3 protein-ubiquitin ligase. {ECO:0000250}. SUBUNIT: Interacts with DDB1 and CUL4A. {ECO:0000250}. +Q91ZV3 DCBD2_MOUSE Discoidin, CUB and LCCL domain-containing protein 2 (Endothelial and smooth muscle cell-derived neuropilin-like protein) 769 83,774 Chain (1); Compositional bias (1); Disulfide bond (4); Domain (3); Glycosylation (5); Modified residue (1); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 524 544 Helical. {ECO:0000255}. TOPO_DOM 64 523 Extracellular. {ECO:0000255}.; TOPO_DOM 545 769 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. +P70211 DCC_MOUSE Netrin receptor DCC (Tumor suppressor protein DCC) 1447 158,341 Alternative sequence (2); Beta strand (13); Chain (1); Disulfide bond (4); Domain (10); Glycosylation (7); Helix (2); Modified residue (3); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1098 1122 Helical. {ECO:0000255}. TOPO_DOM 26 1097 Extracellular. {ECO:0000255}.; TOPO_DOM 1123 1447 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for netrin required for axon guidance. Mediates axon attraction of neuronal growth cones in the developing nervous system upon ligand binding. Its association with UNC5 proteins may trigger signaling for axon repulsion. It also acts as a dependence receptor required for apoptosis induction when not associated with netrin ligand. Implicated as a tumor suppressor gene. PTM: Ubiquitinated; mediated by SIAH1 or SIAH2 and leading to its subsequent proteasomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Interacts with the cytoplasmic part of UNC5A, UNC5B, UNC5C and probably UNC5D. Interacts with MAPK1. Interacts with NTN1 (By similarity). Interacts with DSCAM. Interacts with PTK2/FAK1. Interacts with MYO10. Interacts with CBLN4; this interaction can be competed by NTN1. {ECO:0000250, ECO:0000269|PubMed:15494734, ECO:0000269|PubMed:18585357, ECO:0000269|PubMed:21321230, ECO:0000269|PubMed:22220752}. TISSUE SPECIFICITY: In the embryo, expressed at high levels in the developing brain and neural tube. In the embryo, expressed in developing neurons of the telencephalic cortical plate and in developing brainstem nuclei (PubMed:28250456). In adult, highly expressed in brain with very low levels found in testis, heart and thymus. Isoform C is expressed only in the embryo. {ECO:0000269|PubMed:28250456}. +Q8K0V2 DCNL3_MOUSE DCN1-like protein 3 (DCUN1 domain-containing protein 3) (Defective in cullin neddylation protein 1-like protein 3) 304 34,439 Chain (1); Domain (1); Initiator methionine (1); Lipidation (1) FUNCTION: Antagonizes DCUN1D1-mediated CUL1 neddylation by sequestering CUL1 at the cell membrane. {ECO:0000250|UniProtKB:Q8IWE4}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8IWE4}. SUBUNIT: Interacts with CAND1, CUL1, CUL3 and RBX1 through the DCUN1 domain. Does not interact with UBE2M in vivo. {ECO:0000250|UniProtKB:Q8IWE4}. DOMAIN: The DCUN1 domain, also known as PONY domain, mediates recognition of the N-terminally acetylated NEDD8-conjugating E2 enzyme. This domain is also involved in CAND1-, CUL1-, CUL3- and RBX1-binding. {ECO:0000250|UniProtKB:Q8IWE4}. +Q8K2D6 DCTD_MOUSE Deoxycytidylate deaminase (EC 3.5.4.12) (dCMP deaminase) 178 20,059 Active site (1); Chain (1); Domain (1); Metal binding (3); Modified residue (1); Sequence conflict (1) FUNCTION: Supplies the nucleotide substrate for thymidylate synthetase. {ECO:0000250}. SUBUNIT: Homohexamer. {ECO:0000250}. +Q9DAR7 DCPS_MOUSE m7GpppX diphosphatase (EC 3.6.1.59) (DCS-1) (Decapping scavenger enzyme) (Hint-related 7meGMP-directed hydrolase) (Histidine triad nucleotide-binding protein 5) (Histidine triad protein member 5) (HINT-5) (Scavenger mRNA-decapping enzyme DcpS) 338 38,988 Active site (1); Beta strand (17); Binding site (4); Chain (1); Helix (13); Initiator methionine (1); Modified residue (5); Motif (3); Region (1); Sequence conflict (1); Turn (3) FUNCTION: Decapping scavenger enzyme that catalyzes the cleavage of a residual cap structure following the degradation of mRNAs by the 3'->5' exosome-mediated mRNA decay pathway. Hydrolyzes cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG) with up to 10 nucleotide substrates (small capped oligoribonucleotides) and specifically releases 5'-phosphorylated RNA fragments and 7-methylguanosine monophosphate (m7GMP). Cleaves cap analog structures like tri-methyl guanosine nucleoside triphosphate (m3(2,2,7)GpppG) with very poor efficiency. Does not hydrolyze unmethylated cap analog (GpppG) and shows no decapping activity on intact m7GpppG-capped mRNA molecules longer than 25 nucleotides. Does not hydrolyze 7-methylguanosine diphosphate (m7GDP) to m7GMP. May also play a role in the 5'->3 mRNA decay pathway; m7GDP, the downstream product released by the 5'->3' mRNA mediated decapping activity, may be also converted by DCPS to m7GMP. Binds to m7GpppG and strongly to m7GDP. Plays a role in first intron splicing of pre-mRNAs. Inhibits activation-induced cell death. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Predominantly localized in the nucleus. Nucleocytoplasmic shuttling protein that can transiently enter the cytoplasm in mammalian cells in a XPO1/CRM1-dependent manner. {ECO:0000250}. SUBUNIT: Homodimer. Associates with components of the exosome multienzyme ribonuclease complex, such as EXOSC3 and EXOSC4. Interacts with NDOR1. {ECO:0000250}. DOMAIN: The C-terminal histidine triad (HIT) motif and the N-terminal domain are required for the decapping activity. The N-terminus is necessary but not sufficient for binding cap structures. {ECO:0000250}. +Q8CBY8 DCTN4_MOUSE Dynactin subunit 4 (Dynactin subunit p62) 467 53,057 Alternative sequence (1); Chain (1); Coiled coil (1); Cross-link (1); Initiator methionine (1); Modified residue (3) FUNCTION: Could have a dual role in dynein targeting and in ACTR1A/Arp1 subunit of dynactin pointed-end capping. Could be involved in ACTR1A pointed-end binding and in additional roles in linking dynein and dynactin to the cortical cytoskeleton. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9UJW0}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9UJW0}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:Q9QUR2}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q9QUR2}. Cytoplasm, myofibril, sarcomere {ECO:0000269|PubMed:19109891}. Note=Has a punctate cytoplasmic distribution as well as centrosomal distribution typical of dynactin (By similarity). Overexpression in cultured mammalian cells revealed colocalization with cortical actin, stress fibers, and focal adhesion sites, sites of potential interaction between microtubules and the cell cortex (By similarity). In skeletal muscles, costamere localization requires the presence of ANK2 (PubMed:19109891). {ECO:0000250|UniProtKB:Q9QUR2, ECO:0000250|UniProtKB:Q9UJW0, ECO:0000269|PubMed:19109891}. SUBUNIT: Member of the pointed-end complex of the dynactin shoulder complex which contains DCTN4, DCTN5 and DCTN6 subunits and ACTR10 (By similarity). Binds directly to the ACTR1A subunit of dynactin (By similarity). Interacts with ATP7B, but not ATP7A, in a copper-dependent manner (By similarity). Interacts with ANK2; this interaction is required for localization at costameres. {ECO:0000250, ECO:0000269|PubMed:19109891}. +Q9QZB9 DCTN5_MOUSE Dynactin subunit 5 (Dynactin subunit p25) 182 20,141 Chain (1); Modified residue (1); Sequence conflict (2) SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. SUBUNIT: Member of the pointed-end complex of the dynactin shoulder complex which contains DCTN4, DCTN5 and DCTN6 subunits and ACTR10. Within the complex DCTN6 forms a heterodimer with DCTN5. {ECO:0000269|PubMed:10525537}. +Q9QY93 DCTP1_MOUSE dCTP pyrophosphatase 1 (EC 3.6.1.12) (Deoxycytidine-triphosphatase 1) (dCTPase 1) (RS21-C6) 170 18,795 Beta strand (1); Binding site (3); Chain (1); Helix (6); Initiator methionine (1); Metal binding (4); Modified residue (2); Mutagenesis (8); Region (1); Turn (2) FUNCTION: Hydrolyzes deoxynucleoside triphosphates (dNTPs) to the corresponding nucleoside monophosphates. Has a strong preference for dCTP and its analogs including 5-iodo-dCTP and 5-methyl-dCTP for which it may even have a higher efficiency. May protect DNA or RNA against the incorporation of these genotoxic nucleotide analogs through their catabolism. {ECO:0000269|PubMed:17320107, ECO:0000269|PubMed:19220460}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:19220460}. Note=Not detected in mitochondrion and nucleus. {ECO:0000269|PubMed:19220460}. SUBUNIT: Homotetramer. {ECO:0000269|PubMed:17320107, ECO:0000269|Ref.6}. TISSUE SPECIFICITY: Ubiquitous. Highly expressed in heart, liver, skeletal muscle, cerebellum, brain, and salivary gland. {ECO:0000269|PubMed:19220460}. +Q9DAF3 DDI1_MOUSE Protein DDI1 homolog 1 (EC 3.4.23.-) 408 45,713 Active site (1); Beta strand (6); Chain (1); Compositional bias (1); Domain (1); Helix (3); Turn (1) FUNCTION: Probable aspartic protease. {ECO:0000250|UniProtKB:I7HUG0}. +Q80YA3 DDHD1_MOUSE Phospholipase DDHD1 (EC 3.1.1.-) (DDHD domain-containing protein 1) (Phosphatidic acid-preferring phospholipase A1 homolog) (PA-PLA1) 547 61,823 Active site (1); Alternative sequence (1); Chain (1); Domain (1); Modified residue (1) FUNCTION: Phospholipase that hydrolyzes phosphatidic acid, including 1,2-dioleoyl-sn-phosphatidic acid. The different isoforms may change the substrate specificity (By similarity). Required for the organization of the endoplasmic reticulum exit sites (ERES), also known as transitional endoplasmic reticulum (tER) (By similarity). {ECO:0000250|UniProtKB:Q8NEL9}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8NEL9}. SUBUNIT: Forms homooligomers and, to a much smaller extent, heterooligomers with DDHD2. Interacts with SEC23A and SEC24C. {ECO:0000250|UniProtKB:Q8NEL9}. +Q6NZG4 DDIAS_MOUSE DNA damage-induced apoptosis suppressor protein (Nitric oxide-inducible gene protein) 898 99,945 Chain (1); Compositional bias (1); Sequence conflict (3) FUNCTION: May be an anti-apoptotic protein involved in DNA repair or cell survival. {ECO:0000269|PubMed:17515607}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17515607}. Nucleus {ECO:0000269|PubMed:17515607}. Note=Accumulates in the nucleus in response to stress. TISSUE SPECIFICITY: Highly expressed in the testis, spleen and heart. Expressed at high levels in the primary spermatocytes and to a lesser extent in the round spermatids. Also found in the bone marrow, brain, lung, kidney and liver. {ECO:0000269|PubMed:17515607}. +Q3U1J4 DDB1_MOUSE DNA damage-binding protein 1 (DDB p127 subunit) (Damage-specific DNA-binding protein 1) (UV-damaged DNA-binding factor) 1140 126,853 Chain (1); Cross-link (1); Initiator methionine (1); Modified residue (3); Region (5); Sequence conflict (9) Protein modification; protein ubiquitination. FUNCTION: Required for DNA repair. Binds to DDB2 to form the UV-damaged DNA-binding protein complex (the UV-DDB complex). The UV-DDB complex may recognize UV-induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair. The UV-DDB complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and short mismatches. Also appears to function as a component of numerous distinct DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The functional specificity of the DCX E3 ubiquitin-protein ligase complex is determined by the variable substrate recognition component recruited by DDB1. DCX(DDB2) (also known as DDB1-CUL4-ROC1, CUL4-DDB-ROC1 and CUL4-DDB-RBX1) may ubiquitinate histone H2A, histone H3 and histone H4 at sites of UV-induced DNA damage. The ubiquitination of histones may facilitate their removal from the nucleosome and promote subsequent DNA repair. DCX(DDB2) also ubiquitinates XPC, which may enhance DNA-binding by XPC and promote NER. DCX(DTL) plays a role in PCNA-dependent polyubiquitination of CDT1 and MDM2-dependent ubiquitination of TP53 in response to radiation-induced DNA damage and during DNA replication. DCX(ERCC8) (the CSA complex) plays a role in transcription-coupled repair (TCR). May also play a role in ubiquitination of CDKN1B/p27kip when associated with CUL4 and SKP2 (By similarity). {ECO:0000250, ECO:0000269|PubMed:12107171}. PTM: Phosphorylated by ABL1. {ECO:0000269|PubMed:12107171}.; PTM: Ubiquitinated by CUL4A. Subsequently degraded by ubiquitin-dependent proteolysis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Primarily cytoplasmic. Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage (By similarity). {ECO:0000250}. SUBUNIT: Component of the UV-DDB complex which includes DDB1 and DDB2; the heterodimer dimerizes to give rise to a heterotetramer when bound to damaged DNA. The UV-DDB complex interacts with monoubiquitinated histone H2A and binds to XPC via the DDB2 subunit. Component of numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which consist of a core of DDB1, CUL4A or CUL4B and RBX1. DDB1 may recruit specific substrate targeting subunits to the DCX complex. These substrate targeting subunits are generally known as DCAF (DDB1- and CUL4-associated factor) or CDW (CUL4-DDB1-associated WD40-repeat) proteins. Interacts with AMBRA1, ATG16L1, BTRC, CRBN, DCAF1, DCAF4, DCAF5, DCAF6, DCAF7, DCAF8, DCAF9, DCAF10, DCAF11, DCAF12, DCAF15, DCAF16, DCAF17, DDA1, DET1, DTL, ERCC8, FBXW5, FBXW8, GRWD1, KATNB1, NLE1, NUP43, PAFAH1B1, PHIP, PWP1, RBBP4, RBBP5, RBBP7, COP1, SNRNP40, DCAF1, WDR5, WDR5B, WDR12, WDR26, WDR39, WDR42, WDR53, WDR59, WDR61, WSB1, WSB2, LRWD1 and WDTC1. DCX complexes may associate with the COP9 signalosome, and this inhibits the E3 ubiquitin-protein ligase activity of the complex. Interacts with NF2, TSC1 and TSC2. Interacts with AGO1 and AGO2. Associates with the E3 ligase complex containing DYRK2, EDD/UBR5, DDB1 and DCAF1 proteins (EDVP complex). Interacts directly with DYRK2 (By similarity). Interacts with TRPC4AP (By similarity). {ECO:0000250|UniProtKB:Q16531}. DOMAIN: The core of the protein consists of three WD40 beta-propeller domains. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed. Expressed in pregnant, lactating and involuting mammary gland. {ECO:0000269|PubMed:10574459}. +Q03146 DDR1_MOUSE Epithelial discoidin domain-containing receptor 1 (Epithelial discoidin domain receptor 1) (EC 2.7.10.1) (CD167 antigen-like family member A) (Cell adhesion kinase) (Discoidin receptor tyrosine kinase) (Protein-tyrosine kinase MPK-6) (Tyrosine kinase DDR) (Tyrosine-protein kinase CAK) (CD antigen CD167a) 911 101,161 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Compositional bias (2); Disulfide bond (3); Domain (2); Glycosylation (4); Metal binding (9); Modified residue (7); Motif (1); Nucleotide binding (1); Region (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 416 436 Helical. {ECO:0000255}. TOPO_DOM 22 415 Extracellular. {ECO:0000255}.; TOPO_DOM 437 911 Cytoplasmic. {ECO:0000255}. FUNCTION: Tyrosine kinase that functions as cell surface receptor for fibrillar collagen and regulates cell attachment to the extracellular matrix, remodeling of the extracellular matrix, cell migration, differentiation, survival and cell proliferation. Collagen binding triggers a signaling pathway that involves SRC and leads to the activation of MAP kinases. Regulates remodeling of the extracellular matrix by up-regulation of the matrix metalloproteinases MMP2, MMP7 and MMP9, and thereby facilitates cell migration and wound healing, but also tumor cell invasion. Promotes smooth muscle cell migration, and thereby contributes to arterial wound healing. Phosphorylates PTPN11 (By similarity). Required for normal blastocyst implantation during pregnancy, for normal mammary gland differentiation and normal lactation. Required for normal ear morphology and normal hearing. {ECO:0000250, ECO:0000269|PubMed:12065315}. PTM: Autophosphorylated in response to fibrillar collagen binding. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SUBUNIT: Homodimer. Interacts (via PPxY motif) with WWC1 (via WW domains) in a collagen-regulated manner. Forms a tripartite complex with WWC1 and PRKCZ, but predominantly in the absence of collagen. Interacts (tyrosine phosphorylated) with SHC1. Interacts with SRC. Interacts with MYH9. Interacts with CDH1. Interacts with PTPN11. Interacts with NCK2 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Detected in the cochlea and the organ of Corti in the inner ear. Isoform 1 is predominant and is expressed in developing embryo and adult brain. Isoform 2 is expressed in various epithelial cells. {ECO:0000269|PubMed:18026164}. +Q9ESV0 DDX24_MOUSE ATP-dependent RNA helicase DDX24 (EC 3.6.4.13) (DEAD box protein 24) 857 96,429 Chain (1); Compositional bias (2); Cross-link (2); Domain (2); Modified residue (5); Motif (2); Nucleotide binding (1); Sequence conflict (4) FUNCTION: ATP-dependent RNA helicase. {ECO:0000305}. +P54823 DDX6_MOUSE Probable ATP-dependent RNA helicase DDX6 (EC 3.6.4.13) (ATP-dependent RNA helicase p54) (DEAD box protein 6) (Oncogene RCK homolog) 483 54,192 Chain (1); Domain (2); Modified residue (1); Motif (2); Nucleotide binding (1); Sequence conflict (8) FUNCTION: In the process of mRNA degradation, plays a role in mRNA decapping (By similarity). Blocks autophagy in nutrient-rich conditions by repressing the expression of ATG-related genes through degration of their transcripts (PubMed:26098573). {ECO:0000250|UniProtKB:P26196, ECO:0000269|PubMed:26098573}. PTM: Sumoylated. {ECO:0000250|UniProtKB:P26196}. SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000250|UniProtKB:P26196}. Cytoplasm {ECO:0000250|UniProtKB:P26196}. Nucleus {ECO:0000250|UniProtKB:P26196}. Note=Upon cellular stress, relocalizes to stress granules. {ECO:0000250|UniProtKB:P26196}. SUBUNIT: Forms a complex with DCP1A, DCP2, EDC3 and EDC4/HEDLS (By similarity). Interacts with LIMD1, WTIP and AJUBA (By similarity). Interacts with APOBEC3G in an RNA-dependent manner (By similarity). Interacts with RC3H1 (PubMed:20639877). Interacts with ATXN2L (By similarity). Interacts with MCRIP1 (By similarity). Interacts with MCRIP2 (By similarity). Interacts with NUFIP2 (By similarity). Interacts with TRIM71 (via NHL repeats) in an RNA-dependent manner (By similarity). {ECO:0000250|UniProtKB:P26196, ECO:0000269|PubMed:20639877}. +P63034 CYH2_MOUSE Cytohesin-2 (ARF nucleotide-binding site opener) (Protein ARNO) (PH, SEC7 and coiled-coil domain-containing protein 2) (CLM2) (SEC7 homolog B) (mSec7-2) 400 46,585 Alternative sequence (2); Beta strand (10); Binding site (6); Chain (1); Coiled coil (1); Domain (2); Helix (1); Mutagenesis (8); Region (2); Sequence conflict (7) FUNCTION: Acts as a guanine-nucleotide exchange factor (GEF). Promotes guanine-nucleotide exchange on ARF1, ARF3 and ARF6. Activates ARF factors through replacement of GDP with GTP (PubMed:18042453). The cell membrane form, in association with ARL4 proteins, recruits ARF6 to the plasma membrane (By similarity). Involved in neurite growth (PubMed:25326380). {ECO:0000250|UniProtKB:Q99418, ECO:0000269|PubMed:18042453, ECO:0000269|PubMed:25326380}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q99418}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q99418}. Cytoplasm {ECO:0000269|PubMed:25326380}. Cell projection {ECO:0000269|PubMed:25326380}. Cell projection, growth cone {ECO:0000269|PubMed:25326380}. Cell junction, tight junction {ECO:0000269|PubMed:20080746}. Cell junction, adherens junction {ECO:0000269|PubMed:20080746}. Note=Recruited to the cell membrane through its association with ARL4A, ARL4C and ARL4D. Requires also interaction with phosphoinositides for targeting to plasma membrane (By similarity). In differentiating neuroblastoma cells, colocalizes with CCDC120 in both neurite shaft and growth cone areas. {ECO:0000250, ECO:0000269|PubMed:25326380}. SUBUNIT: Heteromer. Composed of GRASP, CYTH2 and at least one GRM1. Interacts with ARRB1. Interacts with ARL4D; the interaction is direct (By similarity). Directly interacts with CCDC120 through the coiled coil domain; this interaction stabilizes CCDC120, possibly by preventing its ubiquitination, and is required for neurite growth in a neuroblastoma cell line (PubMed:25326380). Interacts with FRMD4A (PubMed:20080746). Interacts (via N-terminal domain) with INAVA (via N-terminal domain) (By similarity). {ECO:0000250|UniProtKB:Q99418, ECO:0000269|PubMed:20080746, ECO:0000269|PubMed:25326380}. DOMAIN: Binds via its PH domain to the inositol head group of phosphatidylinositol 1,4,5-trisphosphate. The PH domain is necessary and sufficient for plasma membrane relocalization (By similarity). {ECO:0000250}.; DOMAIN: Autoinhibited by its C-terminal basic region. {ECO:0000250}.; DOMAIN: The coiled coil domain is involved in interaction with CCDC120. {ECO:0000269|PubMed:25326380}. TISSUE SPECIFICITY: Present in all tissues tested, with highest protein levels in brain and adrenal. +P35173 CYT3_MOUSE Stefin-3 103 11,640 Chain (1); Motif (1); Site (1) FUNCTION: This is an intracellular thiol proteinase inhibitor. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +Q64368 DAZL_MOUSE Deleted in azoospermia-like (DAZ-like autosomal) (Deleted in azoospermia-like 1) 298 33,313 Beta strand (5); Chain (1); Compositional bias (1); Domain (2); Helix (3); Modified residue (1); Mutagenesis (4); Region (1) FUNCTION: RNA-binding protein, which is essential for gametogenesis in both males and females. Plays a central role during spermatogenesis. Acts by binding to the 3'-UTR of mRNA, specifically recognizing GUU triplets, and thereby regulating the translation of key transcripts. {ECO:0000269|PubMed:22021443, ECO:0000269|PubMed:9288969}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9288969}. SUBUNIT: Homodimer and heterodimer. Forms a heterodimer with DAZ. Interacts with BOLL, DAZAP1 and DAZAP2. Interacts with PUM2 (By similarity). Multiple DAZL RRMs can bind to a single RNA containing multiple GUU triplets. {ECO:0000250, ECO:0000269|PubMed:10903443, ECO:0000269|PubMed:22021443}. DOMAIN: The DAZ-like domain mediates the interaction with DAZAP1 and DAZAP2. {ECO:0000250}. TISSUE SPECIFICITY: Expressed predominantly in testis with lower levels in ovary. In testis, it is expressed in pachytene spermatocytes and at lower level in type-B spermatogonia, preleptotene and zygotene spermatocytes. In ovary, it is expressed in maturing follicles. In embryonic and prepuberal ovary, it is expressed in the oocyte and follicular cells. {ECO:0000269|PubMed:9288969}. +P23738 DCHS_MOUSE Histidine decarboxylase (HDC) (EC 4.1.1.22) 662 74,045 Binding site (2); Chain (1); Modified residue (1); Sequence conflict (2) Amine and polyamine biosynthesis; histamine biosynthesis; histamine from L-histidine: step 1/1. FUNCTION: Catalyzes the biosynthesis of histamine from histidine. {ECO:0000250}. SUBUNIT: Homodimer. +Q9QZ73 DCNL1_MOUSE DCN1-like protein 1 (DCUN1 domain-containing protein 1) (Defective in cullin neddylation protein 1-like protein 1) (Testis-specific protein 3) 259 30,097 Chain (1); Domain (2); Erroneous initiation (1); Modified residue (1); Sequence conflict (3); Site (1) FUNCTION: Part of an E3 ubiquitin ligase complex for neddylation. Promotes neddylation of cullin components of E3 cullin-RING ubiquitin ligase complexes. Acts by binding to cullin-RBX1 complexes in the cytoplasm and promoting their nuclear translocation, enhancing recruitment of E2-NEDD8 (UBE2M-NEDD8) thioester to the complex, and optimizing the orientation of proteins in the complex to allow efficient transfer of NEDD8 from the E2 to the cullin substrates. Involved in the release of inhibitory effets of CAND1 on cullin-RING ligase E3 complex assembly and activity (By similarity). Acts also as an oncogene facilitating malignant transformation and carcinogenic in vivo (PubMed:20563250). {ECO:0000250|UniProtKB:Q96GG9, ECO:0000269|PubMed:20563250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96GG9}. SUBUNIT: Part of an E3 complex for neddylation composed of cullins, RBX1, UBE2M and CAND1. Interacts (via the C-terminus 50 AA) with CUL1, CUL2, CUL3, CUL4 and CUL5. Binds neddylated CUL1. Interacts (via the C-terminus 50 AA) directly with RBX1. Interacts (via DCUN1 domain) with UBE2M (acetylated at N-terminal methionine). Interacts preferentially with UBE2M-NEDD8 thioester (via N-terminus 1-26 AA) than with free UBE2M. UBE2M N-terminal acetylation increases the affinity of this interaction by about 2 orders of magnitude. Interacts with CAND1 when in complex with CUL1-RBX1. {ECO:0000250|UniProtKB:Q96GG9}. DOMAIN: The DCUN1 domain, also known as PONY domain mediates its interaction with N-terminally acetylated UBE2M. {ECO:0000250|UniProtKB:Q96GG9}. TISSUE SPECIFICITY: Highly expressed in testis. Also expressed in brain, heart, liver, skeletal muscle and kidney. In brain, preferentially expressed in the telencephalon ventricular and subventricular zones, albeit at low levels. In adult testis, expressed in cells above seminiferous tubules, but only weakly in spermatogonia. {ECO:0000269|PubMed:10777668, ECO:0000269|PubMed:10831844}. +Q9Z0Y1 DCTN3_MOUSE Dynactin subunit 3 (Dynactin light chain p24) 186 20,978 Chain (1); Coiled coil (1); Initiator methionine (1); Modified residue (1); Sequence conflict (2) FUNCTION: Together with dynein may be involved in spindle assembly and cytokinesis. {ECO:0000250|UniProtKB:O75935}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Cleavage furrow {ECO:0000250}. Midbody {ECO:0000250}. Note=Localizes to punctate cytoplasmic structures and to the centrosome during interphase, and to kinetochores and to spindle poles throughout mitosis. Colocalizes with dynein to the cleavage furrow and to midbody of dividing cells (By similarity). {ECO:0000250}. SUBUNIT: Subunit of dynactin, a multiprotein complex associated with dynein. +Q61655 DD19A_MOUSE ATP-dependent RNA helicase DDX19A (EC 3.6.4.13) (DEAD box RNA helicase DEAD5) (mDEAD5) (DEAD box protein 19A) (Eukaryotic translation initiation factor 4A-related sequence 1) 478 53,933 Binding site (3); Chain (1); Compositional bias (1); Cross-link (2); Domain (2); Initiator methionine (1); Modified residue (2); Motif (2); Nucleotide binding (1); Region (3); Sequence conflict (2) FUNCTION: ATP-dependent RNA helicase involved in mRNA export from the nucleus. Rather than unwinding RNA duplexes, DDX19 functions as a remodeler of ribonucleoprotein particles, whereby proteins bound to nuclear mRNA are dissociated and replaced by cytoplasmic mRNA binding proteins (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, nuclear pore complex. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Nuclear pore complex cytoplasmic fibrils. DOMAIN: The N-terminal extension helix acts as an autoinhibitory domain, preventing ATP hydrolysis, unless the N-terminus of the protein is displaced by RNA binding, allowing cleft closure to bring key side chains into position for catalysis. {ECO:0000250}. TISSUE SPECIFICITY: Found in testis, heart, brain, liver, skeletal muscle, and kidney. +A2ADY9 DDI2_MOUSE Protein DDI1 homolog 2 (EC 3.4.23.-) 399 44,591 Active site (1); Chain (1); Domain (1); Modified residue (5); Motif (1) FUNCTION: Aspartic protease that mediates the cleavage of NFE2L1/NRF1 at 'Leu-104', thereby promoting release of NFE2L1/NRF1 from the endoplasmic reticulum membrane. Ubiquitination of NFE2L1/NRF1 is a prerequisite for cleavage, suggesting that DDI2 specifically recognizes and binds ubiquitinated NFE2L1/NRF1. {ECO:0000250|UniProtKB:Q5TDH0}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q5TDH0}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q5TDH0}. +P35174 CYT2_MOUSE Stefin-2 103 11,842 Alternative sequence (1); Chain (1); Motif (1); Sequence conflict (1); Site (1) FUNCTION: This is an intracellular thiol proteinase inhibitor. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +Q9DCP9 DAZP2_MOUSE DAZ-associated protein 2 (Deleted in azoospermia-associated protein 2) (Proline-rich protein expressed in brain) 168 17,289 Chain (1); Compositional bias (1); Sequence conflict (1) PTM: Ubiquitinated by SMURF2, leading to proteasomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Predominantly nuclear in macrophages, stimulation of IL17RB with its ligand IL17E induces accumulation in the cytoplasm. {ECO:0000250}. SUBUNIT: Interacts with DAZ and DAZL (By similarity). Interacts with IL17RB (By similarity). May interact with FAM168B (By similarity). Interacts with SOX6 (PubMed:14530442). Interacts with INCA1 (By similarity). {ECO:0000250|UniProtKB:Q15038, ECO:0000269|PubMed:14530442}. TISSUE SPECIFICITY: Widely expressed. Highly expressed in brain. {ECO:0000269|PubMed:10373015, ECO:0000269|PubMed:14530442}. +Q64263 DAR10_MOUSE Alpha-defensin-related sequence 10 (CRS4C-4) (Cryptdin-related protein 4C-4) (Defensin-related cryptdin-related sequence 10) 91 9,777 Peptide (1); Propeptide (1); Region (1); Repeat (7); Signal peptide (1) FUNCTION: Apparent precursor of a secreted, cationic, proline- and cysteine-rich peptide that contains Cys-Pro-Xaa repeats. Unlike cryptdin, the proposed mature peptide region lacks the structural motif characteristic of defensins. It may have microbicidal activities (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Paneth cells of the small bowel. +Q9JIQ3 DBLOH_MOUSE Diablo homolog, mitochondrial (Direct IAP-binding protein with low pI) (Second mitochondria-derived activator of caspase) (Smac) 237 26,820 Chain (1); Modified residue (1); Motif (1); Sequence conflict (1); Transit peptide (1) FUNCTION: Promotes apoptosis by activating caspases in the cytochrome c/Apaf-1/caspase-9 pathway. Acts by opposing the inhibitory activity of inhibitor of apoptosis proteins (IAP). Inhibits the activity of BIRC6/bruce by inhibiting its binding to caspases (By similarity). {ECO:0000250, ECO:0000269|PubMed:10929712}. PTM: Ubiquitinated by BIRC7/livin. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:10929712}. Note=Released into the cytosol when cells undergo apoptosis. SUBUNIT: Homodimer. Interacts with BIRC2/c-IAP1, BIRC3/c-IAP2, XIAP/BIRC4, BIRC6/bruce and BIRC7/livin. Interacts with the monomeric and dimeric form of BIRC5/survivin (By similarity). Interacts with BEX3. {ECO:0000250, ECO:0000269|PubMed:15178455}. DOMAIN: The mature N-terminus mediates interaction with XIAP/BIRC4. {ECO:0000250}. TISSUE SPECIFICITY: Highest expression found in heart, liver, kidney and testis. {ECO:0000269|PubMed:10929712}. +Q9CZ00 DBND1_MOUSE Dysbindin domain-containing protein 1 160 17,479 Alternative sequence (1); Chain (1); Compositional bias (1); Modified residue (3); Sequence conflict (1) +Q8VDF3 DAPK2_MOUSE Death-associated protein kinase 2 (DAP kinase 2) (EC 2.7.11.1) (DAP-kinase-related protein 1) (DRP-1) 370 42,778 Active site (1); Alternative sequence (1); Beta strand (10); Binding site (1); Chain (1); Domain (1); Helix (14); Modified residue (4); Nucleotide binding (1); Region (2); Sequence conflict (4); Turn (3) FUNCTION: Calcium/calmodulin-dependent serine/threonine kinase involved in multiple cellular signaling pathways that trigger cell survival, apoptosis, and autophagy. Capable of regulating both type I apoptotic and type II autophagic cell death signals. The former involves caspase activation, chromatin and mitochondrial condensation while the latter involves caspase-independent cell death in conjunction with accumulation of mature autophagic vesicles, plasma membrane blebs, and nuclear condensation without DNA degradation. Mediator of anoikis and a suppressor of beta-catenin-dependent anchorage-independent growth of malignant epithelial cells. May play a role in granulocytic maturation (By similarity). Regulates granulocytes motility by controlling cell spreading and polarization (PubMed:24163421). {ECO:0000250|UniProtKB:Q9UIK4, ECO:0000269|PubMed:24163421}. PTM: Autophosphorylation at Ser-318 inhibits its catalytic activity. Dephosphorylated at Ser-318 in response to activated Fas and TNF-alpha receptors. {ECO:0000250|UniProtKB:Q9UIK4}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasmic vesicle, autophagosome lumen {ECO:0000250}. SUBUNIT: Homodimer in its autoinhibited state. Active as monomer. Interacts with 14-3-3 proteins YWHAB, YWHAE, YWHAG, YWHAH, YWHAQ, YWHAZ and SFN; the interaction requires DAPK2 phosphorylation at Thr-369 and suppresses DAPK2 kinase activity and DAPK2-induced apoptosis. {ECO:0000269|PubMed:21497605, ECO:0000269|PubMed:26047703}. DOMAIN: The autoinhibitory domain sterically blocks the substrate peptide-binding site by making both hydrophobic and electrostatic contacts with the kinase core. TISSUE SPECIFICITY: Expressed in peritubular interstitial cells of the renal cortex (PubMed:24906443). Isoform 1 is found in the adult brain while isoform 2 is expressed in brains of embryos and young mice (at protein level) (PubMed:21408167). {ECO:0000269|PubMed:21408167, ECO:0000269|PubMed:24906443}. +Q60925 DBP_MOUSE D site-binding protein (Albumin D box-binding protein) (Albumin D-element-binding protein) 325 34,380 Chain (1); Compositional bias (3); Domain (1); Modified residue (1); Region (2); Sequence conflict (2) FUNCTION: This transcriptional activator recognizes and binds to the sequence 5'-RTTAYGTAAY-3' found in the promoter of genes such as albumin, CYP2A4 and CYP2A5. It is not essential for circadian rhythm generation, but modulates important clock output genes. May be a direct target for regulation by the circadian pacemaker component clock. May affect circadian period and sleep regulation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Binds DNA as a homodimer or a heterodimer. Can form a heterodimer with TEF (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the suprachiasmatic nuclei (SCN) and in most peripheral tissues, with a strong circadian rhythmicity. +Q923B1 DBR1_MOUSE Lariat debranching enzyme (EC 3.1.-.-) 550 62,289 Chain (1); Frameshift (1); Modified residue (11); Sequence conflict (9) FUNCTION: Cleaves the 2'-5' phosphodiester linkage at the branch point of lariat intron pre-mRNAs after splicing and converts them into linear molecules that are subsequently degraded. It thereby facilitates ribonucleotide turnover. It may also participate in retrovirus replication via an RNA lariat intermediate in cDNA synthesis (By similarity). {ECO:0000250, ECO:0000269|PubMed:11355701}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +P52950 DBX1_MOUSE Homeobox protein DBX1 (Developing brain homeobox protein 1) 335 36,334 Chain (1); Compositional bias (1); DNA binding (1) FUNCTION: Could have a role in patterning the central nervous system during embryogenesis. Has a key role in regulating the distinct phenotypic features that distinguish two major classes of ventral interneurons, V0 and V1 neurons. Regulates the transcription factor profile, neurotransmitter phenotype, intraspinal migratory path and axonal trajectory of V0 neurons, features that differentiate them from an adjacent set of V1 neurons. {ECO:0000269|PubMed:11239429}. SUBCELLULAR LOCATION: Nucleus. +Q6PDL0 DC1L2_MOUSE Cytoplasmic dynein 1 light intermediate chain 2 (Dynein light intermediate chain 2, cytosolic) 492 54,218 Chain (1); Modified residue (7); Nucleotide binding (1); Sequence conflict (1) FUNCTION: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in binding dynein to membranous organelles or chromosomes (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. SUBUNIT: Homodimer (By similarity). The cytoplasmic dynein 1 complex consists of two catalytic heavy chains (HCs) and a number of non-catalytic subunits presented by intermediate chains (ICs), light intermediate chains (LICs) and light chains (LCs); the composition seems to vary in respect to the IC, LIC and LC composition. The heavy chain homodimer serves as a scaffold for the probable homodimeric assembly of the respective non-catalytic subunits. The ICs and LICs bind directly to the HC dimer and the LCs assemble on the IC dimer. Self-associates. Interacts with DYNC1H1; DYNC1LI1 and DYNC1LI2 bind mutually exclusive to DYNC1H1 (By similarity). {ECO:0000250}. +Q91YD3 DCP1A_MOUSE mRNA-decapping enzyme 1A (EC 3.-.-.-) (MAD homolog 4-interacting transcription coactivator 1) (Smad4-interacting transcriptional co-activator) (Transcription factor SMIF) 602 65,219 Chain (1); Modified residue (16); Natural variant (1) FUNCTION: Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Contributes to the transactivation of target genes after stimulation by TGFB1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:19861488}. Nucleus {ECO:0000250|UniProtKB:Q9NPI6}. Note=Predominantly cytoplasmic, in processing bodies (PB). Nuclear, after TGFB1 treatment. Translocation to the nucleus depends on interaction with SMAD4 (By similarity). Colocalizes with NANOS3 in the processing bodies (PubMed:19861488). {ECO:0000250|UniProtKB:Q9NPI6, ECO:0000269|PubMed:19861488}. SUBUNIT: Forms a complex with EDC3, DCP2, DDX6 and EDC4/HEDLS, within this complex directly interacts with EDC3. Part of a cytoplasmic complex containing proteins involved in mRNA decay, including XRN1 and LSM1. Interacts with DCP1B. Interacts with DCP2. Interacts with DDX17 in an RNA-independent manner. Interacts with PNRC2. Interacts with SMAD4. Interacts with UPF1. Interacts with ZC3HAV1. Interacts with ZFP36L1. Interacts with NBDY. {ECO:0000250|UniProtKB:Q9NPI6}. +Q9JLM8 DCLK1_MOUSE Serine/threonine-protein kinase DCLK1 (EC 2.7.11.1) (Doublecortin-like and CAM kinase-like 1) (Doublecortin-like kinase 1) 756 84,153 Active site (1); Alternative sequence (2); Binding site (1); Chain (1); Compositional bias (1); Domain (3); Modified residue (23); Nucleotide binding (1) FUNCTION: Probable kinase that may be involved in a calcium-signaling pathway controlling neuronal migration in the developing brain. May also participate in functions of the mature nervous system (By similarity). {ECO:0000250}. +O08788 DCTN1_MOUSE Dynactin subunit 1 (150 kDa dynein-associated polypeptide) (DAP-150) (DP-150) (p150-glued) 1281 141,676 Alternative sequence (1); Chain (1); Coiled coil (3); Compositional bias (1); Domain (1); Modified residue (6); Region (1); Sequence conflict (4) FUNCTION: Plays a key role in dynein-mediated retrograde transport of vesicles and organelles along microtubules by recruiting and tethering dynein to microtubules. Binds to both dynein and microtubules providing a link between specific cargos, microtubules and dynein. Essential for targeting dynein to microtubule plus ends, recruiting dynein to membranous cargos and enhancing dynein processivity (the ability to move along a microtubule for a long distance without falling off the track). Can also act as a brake to slow the dynein motor during motility along the microtubule. Can regulate microtubule stability by promoting microtubule formation, nucleation and polymerization and by inhibiting microtubule catastrophe in neurons. Inhibits microtubule catastrophe by binding both to microtubules and to tubulin, leading to enhanced microtubule stability along the axon. Plays a role in metaphase spindle orientation. Plays a role in centriole cohesion and subdistal appendage organization and function. Its recruitement to the centriole in a KIF3A-dependent manner is essential for the maintenance of centriole cohesion and the formation of subdistal appendage. Also required for microtubule anchoring at the mother centriole. Plays a role in primary cilia formation. {ECO:0000250|UniProtKB:Q14203}. PTM: Ubiquitinated by a SCF complex containing FBXL5, leading to its degradation by the proteasome. {ECO:0000250|UniProtKB:Q14203}.; PTM: Phosphorylation by SLK at Thr-145, Thr-146 and Thr-147 targets DCTN1 to the centrosome. It is uncertain if SLK phosphorylates all three threonines or one or two of them. PLK1-mediated phosphorylation at Ser-179 is essential for its localization in the nuclear envelope and promotes its dissociation from microtubules during early mitosis and positively regulates nuclear envelope breakdown during prophase. {ECO:0000250|UniProtKB:Q14203}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14203}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16954346}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q14203}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:23386061}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q14203}. Nucleus envelope {ECO:0000250|UniProtKB:Q14203}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q14203}. Note=Localizes to microtubule plus ends. Localizes preferentially to the ends of tyrosinated microtubules (PubMed:16954346). Localization at centrosome is regulated by SLK-dependent phosphorylation. Localizes to centrosome in a PARKDA-dependent manner. PLK1-mediated phosphorylation at Ser-179 is essential for its localization in the nuclear envelope (By similarity). Localizes to the subdistal appendage region of the centriole in a KIF3A-dependent manner (PubMed:23386061). {ECO:0000250|UniProtKB:Q14203, ECO:0000269|PubMed:16954346, ECO:0000269|PubMed:23386061}. SUBUNIT: Monomer and homodimer. Dynactin is a large macromolecular complex of at least 10 components; p150(glued) binds directly to microtubules and to cytoplasmic dynein. Interacts with the C-terminus of MAPRE1, MAPRE2 and MAPRE3. Interacts with FBXL5. Interacts with ECPAS. Interacts with CLIP1. Interacts with CLN3 and DYNAP. Interacts with MISP; this interaction regulates its distribution at the cell cortex. Interacts with CEP131. Interacts with CEP126. Interacts with dynein intermediate chain and dynein heavy chain. Interacts with PLK1 (via POLO-box domain). Interacts with TBCB and PARD6A (By similarity). Binds preferentially to tyrosinated microtubules than to detyrosinated microtubules (PubMed:16954346). Interacts with KIF3A (PubMed:23386061). Interacts with HPS6 (PubMed:25189619). Interacts with SNX6 (PubMed:19935774). Interacts with BICD2 (PubMed:22956769). Interacts with DST (isoform 1) (PubMed:14581450). Identified in a complex with MREG and RILP (PubMed:22275436). Interacts with BCCIP. Interacts with DCDC1 (By similarity). {ECO:0000250|UniProtKB:Q14203, ECO:0000269|PubMed:14581450, ECO:0000269|PubMed:16954346, ECO:0000269|PubMed:19935774, ECO:0000269|PubMed:22275436, ECO:0000269|PubMed:22956769, ECO:0000269|PubMed:23386061, ECO:0000269|PubMed:25189619}. DOMAIN: The CAP-Gly domain is essential for interactions with microtubules and its binding partners and for its motion along the microtubules. Essential for its preferential binding to tyrosinated microtubules and for promoting the sustained interaction of the dynein motor with microtubules. {ECO:0000250|UniProtKB:Q14203}. +Q059Y8 DCST1_MOUSE E3 ubiquitin-protein ligase DCST1 (EC 2.3.2.27) (DC-STAMP domain-containing protein 1) (RING-type E3 ubiquitin transferase) 732 84,332 Chain (1); Glycosylation (5); Topological domain (7); Transmembrane (6); Zinc finger (1) TRANSMEM 47 67 Helical. {ECO:0000255}.; TRANSMEM 77 97 Helical. {ECO:0000255}.; TRANSMEM 108 128 Helical. {ECO:0000255}.; TRANSMEM 395 415 Helical. {ECO:0000255}.; TRANSMEM 490 510 Helical. {ECO:0000255}.; TRANSMEM 577 597 Helical. {ECO:0000255}. TOPO_DOM 1 46 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 68 76 Extracellular. {ECO:0000255}.; TOPO_DOM 98 107 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 129 394 Extracellular. {ECO:0000255}.; TOPO_DOM 416 489 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 511 576 Extracellular. {ECO:0000255}.; TOPO_DOM 598 732 Cytoplasmic. {ECO:0000255}. Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase which mediates 'Lys-48'-linked ubiquitination of STAT2 and induces its proteosomal degradation thereby negatively regulating type-I-interferon signaling. {ECO:0000250|UniProtKB:Q5T197}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q5T197}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Interacts with STAT2; the interaction results in STAT2 'Lys-48'-linked ubiquitination leading to its proteasomal degradation. {ECO:0000250|UniProtKB:Q5T197}. DOMAIN: The RING-type zinc finger domain is responsible for E3 ubiquitin ligase activity. {ECO:0000250|UniProtKB:Q5T197}. +Q99KJ8 DCTN2_MOUSE Dynactin subunit 2 (50 kDa dynein-associated polypeptide) (Dynactin complex 50 kDa subunit) (DCTN-50) (Growth cone membrane protein 23-48K) (GMP23-48K) (p50 dynamitin) 402 44,117 Chain (1); Coiled coil (2); Initiator methionine (1); Modified residue (6) FUNCTION: Modulates cytoplasmic dynein binding to an organelle, and plays a role in prometaphase chromosome alignment and spindle organization during mitosis. Involved in anchoring microtubules to centrosomes. May play a role in synapse formation during brain development. {ECO:0000269|PubMed:14983524}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14983524, ECO:0000269|PubMed:9144527}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. SUBUNIT: Subunit of dynactin, a multiprotein complex associated with dynein. Interacts with ECPAS, DYNAP and MAPRE1 (By similarity). Interacts with BICD2 (PubMed:11483508, PubMed:22956769). Interacts with CEP135 (PubMed:14983524). {ECO:0000250|UniProtKB:Q13561, ECO:0000269|PubMed:11483508, ECO:0000269|PubMed:14983524, ECO:0000269|PubMed:22956769}. +P36368 EGFB2_MOUSE Epidermal growth factor-binding protein type B (EGF-BP B) (EC 3.4.21.119) (Glandular kallikrein K13) (mGK-13) (Prorenin-converting enzyme 1) (PRECE-1) (Tissue kallikrein 13) 261 28,689 Active site (3); Beta strand (14); Chain (1); Disulfide bond (5); Domain (1); Glycosylation (1); Helix (4); Propeptide (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Cleaves REN2 at a dibasic site to yield mature renin. +Q8BHZ5 CYREN_MOUSE Cell cycle regulator of non-homologous end joining (Cell cycle regulator of NHEJ) (Modulator of retrovirus infection homolog) 157 17,287 Alternative sequence (1); Chain (1); Modified residue (1); Motif (1); Sequence conflict (2) FUNCTION: Cell-cycle-specific inhibitor of classical non-homologous end joining (NHEJ) of DNA double-strand break (DSB) repair during the S and G2 phases. Acts as a regulator of DNA repair pathway choice by specifically inhibiting classical NHEJ during the S and G2 phases, thereby promoting error-free repair by homologous recombination during cell cycle phases when sister chromatids are present. Preferentially protects single-stranded overhangs at break sites by inhibiting classical NHEJ, thereby creating a local environment that favors homologous recombination. Acts via interaction with XRCC5/Ku80 and XRCC6/Ku70, interaction restricted during the S and G2 phases only. Molecular mechanisms governing classical NHEJ inhibition via interaction with XRCC5/Ku80 and XRCC6/Ku70 are unknown (By similarity). May act as a regulator of proteasome (By similarity). {ECO:0000250|UniProtKB:Q09HN1, ECO:0000250|UniProtKB:Q9BWK5}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BWK5}. Nucleus {ECO:0000250|UniProtKB:Q9BWK5}. Note=Nuclear localization may depend upon interaction with XRCC5/Ku80 and XRCC6/Ku70 heterodimer. {ECO:0000250|UniProtKB:Q9BWK5}. SUBUNIT: Interacts (via KBM motif) with XRCC5/Ku80 and XRCC6/Ku70 heterodimer; interaction is restricted during the S and G2 phases. {ECO:0000250|UniProtKB:Q9BWK5}. DOMAIN: The KBM (Ku-binding motif) mediates interaction with XRCC5/Ku80 and XRCC6/Ku70. {ECO:0000250|UniProtKB:Q9BWK5}. +O70273 EHF_MOUSE ETS homologous factor (ETS domain-containing transcription factor) 300 34,903 Alternative sequence (3); Chain (1); DNA binding (1); Domain (1) FUNCTION: Transcriptional activator that may play a role in regulating epithelial cell differentiation and proliferation. May act as a repressor for a specific subset of ETS/AP-1-responsive genes, and as a modulator of the nuclear response to mitogen-activated protein kinase signaling cascades. Binds to DNA sequences containing the consensus nucleotide core sequence GGAA. Involved in regulation of TNFRSF10B/DR5 expression through Ets-binding sequences on the TNFRSF10B/DR5 promoter (By similarity). {ECO:0000250|UniProtKB:Q9NZC4, ECO:0000269|PubMed:16704374}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NZC4, ECO:0000255|PROSITE-ProRule:PRU00237}. DOMAIN: The PNT domain acts as a transcriptional activator. {ECO:0000269|PubMed:16704374}. TISSUE SPECIFICITY: Highly expressed in kidney and lung, weakly in skeletal muscle, heart, and liver, and not detected in brain, spleen or testis. {ECO:0000269|PubMed:9600089}. +Q9Z148 EHMT2_MOUSE Histone-lysine N-methyltransferase EHMT2 (EC 2.1.1.-) (EC 2.1.1.43) (Euchromatic histone-lysine N-methyltransferase 2) (HLA-B-associated transcript 8) (Histone H3-K9 methyltransferase 3) (H3-K9-HMTase 3) (Protein G9a) 1263 138,039 Alternative sequence (3); Binding site (2); Chain (1); Compositional bias (1); Cross-link (3); Domain (3); Erroneous gene model prediction (2); Erroneous initiation (2); Metal binding (16); Modified residue (16); Mutagenesis (7); Region (5); Repeat (7) FUNCTION: Histone methyltransferase that specifically mono- and dimethylates 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin. H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting HP1 proteins to methylated histones. Also mediates monomethylation of 'Lys-56' of histone H3 (H3K56me1) in G1 phase, leading to promote interaction between histone H3 and PCNA and regulating DNA replication. Also weakly methylates 'Lys-27' of histone H3 (H3K27me). Also required for DNA methylation, the histone methyltransferase activity is not required for DNA methylation, suggesting that these 2 activities function independently. Probably targeted to histone H3 by different DNA-binding proteins like E2F6, MGA, MAX and/or DP1. May also methylate histone H1. In addition to the histone methyltransferase activity, also methylates non-histone proteins: mediates dimethylation of 'Lys-373' of p53/TP53. Also methylates CDYL, WIZ, ACIN1, DNMT1, HDAC1, ERCC6, KLF12 and itself. {ECO:0000269|PubMed:12130538, ECO:0000269|PubMed:15774718, ECO:0000269|PubMed:18818694, ECO:0000269|PubMed:22387026}. PTM: Methylated at Lys-239; automethylated. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Chromosome {ECO:0000305}. Note=Almost excluded form nucleoli. Associates with euchromatic regions. Does not associate with heterochromatin. Part of a complex composed of TRIM28, HDAC1, HDAC2 and EHMT2 (By similarity). Interacts with CDYL. Interacts with REST only in the presence of CDYL. Part of a complex containing at least CDYL, REST, WIZ, SETB1, EHMT1 and EHMT2 (By similarity). Interacts with UHRF1. {ECO:0000250}. SUBUNIT: Part of the E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EHMT1, RING1, RNF2, MBLR, GFI1B, L3MBTL2 and YAF2 (By similarity). Heterodimer; heterodimerizes with EHMT1. Interacts with WIZ. {ECO:0000250, ECO:0000269|PubMed:15774718, ECO:0000269|PubMed:16702210, ECO:0000269|PubMed:19056828}. DOMAIN: The ANK repeats bind H3K9me1 and H3K9me2. {ECO:0000250}.; DOMAIN: The SET domain mediates interaction with WIZ.; DOMAIN: In the pre-SET domain, Cys residues bind 3 zinc ions that are arranged in a triangular cluster; some of these Cys residues contribute to the binding of two zinc ions within the cluster. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15774718}. +P56567 CYTA_MOUSE Cystatin-A (Cystatin-A1) (Stefin-A) 97 10,929 Chain (1); Modified residue (1); Motif (1); Site (1) FUNCTION: This is an intracellular thiol proteinase inhibitor. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +Q3UYV8 DAAF3_MOUSE Dynein assembly factor 3, axonemal 586 64,613 Chain (1); Compositional bias (1) FUNCTION: Required for the assembly of axonemal inner and outer dynein arms. Involved in preassembly of dyneins into complexes before their transport into cilia (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +Q9CRD4 DBND2_MOUSE Dysbindin domain-containing protein 2 158 17,194 Chain (1); Modified residue (4) FUNCTION: May modulate the activity of casein kinase-1. Inhibits CSNK1D autophosphorylation (in vitro) (By similarity). {ECO:0000250}. SUBUNIT: Monomer. Interacts with CSNK1D and CSNK1E (By similarity). {ECO:0000250}. +Q8BHC4 DCAKD_MOUSE Dephospho-CoA kinase domain-containing protein 231 26,476 Chain (1); Domain (1); Nucleotide binding (1) +Q9D4J3 DCBD1_MOUSE Discoidin, CUB and LCCL domain-containing protein 1 503 54,518 Alternative sequence (1); Chain (1); Disulfide bond (4); Domain (2); Erroneous initiation (1); Glycosylation (2); Modified residue (2); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 251 271 Helical. {ECO:0000255}. TOPO_DOM 26 250 Extracellular. {ECO:0000255}.; TOPO_DOM 272 503 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q8R1Q8 DC1L1_MOUSE Cytoplasmic dynein 1 light intermediate chain 1 (Dynein light chain A) (DLC-A) (Dynein light intermediate chain 1, cytosolic) 523 56,614 Chain (1); Modified residue (15); Nucleotide binding (1) FUNCTION: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in binding dynein to membranous organelles or chromosomes. Probably involved in the microtubule-dependent transport of pericentrin. Is required for progress through the spindle assembly checkpoint. The phosphorylated form appears to be involved in the selective removal of MAD1L1 and MAD1L2 but not BUB1B from kinetochores (By similarity). {ECO:0000250}. PTM: Phosphorylated during mitosis but not in interphase. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. SUBUNIT: Homodimer (By similarity). The cytoplasmic dynein 1 complex consists of two catalytic heavy chains (HCs) and a number of non-catalytic subunits presented by intermediate chains (ICs), light intermediate chains (LICs) and light chains (LCs); the composition seems to vary in respect to the IC, LIC and LC composition. The heavy chain homodimer serves as a scaffold for the probable homodimeric assembly of the respective non-catalytic subunits. The ICs and LICs bind directly to the HC dimer and the LCs assemble on the IC dimer. Self-associates. Interacts with DYNC1H1; DYNC1LI1 and DYNC1LI2 bind mutually exclusive to DYNC1H1. Interacts with PCNT (By similarity). {ECO:0000250}. +Q8BZJ7 DCNL2_MOUSE DCN1-like protein 2 (DCUN1 domain-containing protein 2) (Defective in cullin neddylation protein 1-like protein 2) 259 30,068 Alternative sequence (2); Chain (1); Domain (2); Frameshift (1); Modified residue (1) FUNCTION: Potently stimulates the neddylation of cullin components of SCF-type E3 ubiquitin ligase complexes from the NEDD8-conjugating E2 enzyme UBC12. Neddylation of cullins play an essential role in the regulation of SCF-type complexes activity (By similarity). {ECO:0000250}. DOMAIN: The DCUN1 domain, also known as PONY domain mediates recognition of the N-terminally acetylated NEDD8-conjugating E2 enzyme. {ECO:0000250}. +Q9CX80 CYGB_MOUSE Cytoglobin (Histoglobin) (HGb) 190 21,466 Chain (1); Metal binding (2); Region (1) FUNCTION: May have a protective function during conditions of oxidative stress. May be involved in intracellular oxygen storage or transfer. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +Q9JJZ5 EGFL6_MOUSE Epidermal growth factor-like protein 6 (EGF-like protein 6) (MAM and EGF domains-containing gene protein) (Protein W80) 550 61,520 Chain (1); Coiled coil (1); Disulfide bond (11); Domain (6); Glycosylation (1); Mutagenesis (1); Signal peptide (1) FUNCTION: May bind integrin alpha-8/beta-1 and play a role in hair follicle morphogenesis. Promotes matrix assembly. {ECO:0000269|PubMed:15572035, ECO:0000269|PubMed:18757743}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000269|PubMed:18757743}. TISSUE SPECIFICITY: Expressed at basement membrane of pelage follicles (at protein level). {ECO:0000269|PubMed:15572035}. +Q6GUQ1 EGFL8_MOUSE Epidermal growth factor-like protein 8 (EGF-like protein 8) 293 32,066 Alternative sequence (1); Chain (1); Coiled coil (1); Disulfide bond (9); Domain (3); Glycosylation (1); Sequence conflict (2); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Ubiquitously expressed in brain, kidney, thymus and lung. {ECO:0000269|PubMed:15162510}. +Q9QXY6 EHD3_MOUSE EH domain-containing protein 3 535 60,821 Binding site (2); Calcium binding (1); Chain (1); Coiled coil (1); Cross-link (2); Domain (3); Modified residue (3); Mutagenesis (1); Nucleotide binding (1); Region (5); Sequence conflict (2) FUNCTION: ATP- and membrane-binding protein that controls membrane reorganization/tubulation upon ATP hydrolysis. In vitro causes tubulation of endocytic membranes (By similarity). Binding to phosphatidic acid induces its membrane tubulation activity (PubMed:26896729). Plays a role in endocytic transport. Involved in early endosome to recycling endosome compartment (ERC), retrograde early endosome to Golgi, and endosome to plasma membrane (rapid recycling) protein transport. Involved in the regulation of Golgi maintenance and morphology (By similarity). Involved in the recycling of internalized D1 dopamine receptor (By similarity). Plays a role in cardiac protein trafficking probably implicating ANK2. Involved in the ventricular membrane targeting of SLC8A1 and CACNA1C and probably the atrial membrane localization of CACNA1GG and CACNA1H implicated in the regulation of atrial myocyte excitability and cardiac conduction (PubMed:20489164, PubMed:24759929, PubMed:25825486). In conjunction with EHD4 may be involved in endocytic trafficking of KDR/VEGFR2 implicated in control of glomerular function (PubMed:21408024). Involved in the rapid recycling of integrin beta-3 implicated in cell adhesion maintenance (By similarity). Involved in the unidirectional retrograde dendritic transport of endocytosed BACE1 and in efficient sorting of BACE1 to axons implicating a function in neuronal APP processing. Plays a role in the formation of the ciliary vesicle, an early step in cilium biogenesis; possibly sharing redundant functions with Ehd1 (PubMed:25686250). {ECO:0000250|UniProtKB:Q9NZN3, ECO:0000269|PubMed:20489164, ECO:0000269|PubMed:21408024, ECO:0000269|PubMed:24373286, ECO:0000269|PubMed:24759929, ECO:0000269|PubMed:25686250, ECO:0000269|PubMed:25825486, ECO:0000269|PubMed:26896729}. SUBCELLULAR LOCATION: Recycling endosome membrane {ECO:0000250|UniProtKB:Q9NZN3, ECO:0000305|PubMed:12121420}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell membrane {ECO:0000250|UniProtKB:Q9NZN3}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell projection, cilium membrane {ECO:0000250|UniProtKB:Q9NZN3}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle {ECO:0000269|PubMed:12121420, ECO:0000269|PubMed:24373286}. Note=Localizes to the ciliary pocket from where the cilium protrudes (By similarity). Colocalizes with RAB8A and MYO5B to a cytoplasmic tubular network devoid of RAB11A (PubMed:17507647). Colocalizes with ANK2 in myocyte perinuclear region (PubMed:25825486). Colocalizes with BACE1 in tubulovesicular cytoplasmic membranes. Colocalizes with BACE1 and APP amyloid beta proteins in hippocampal mossy fiber terminals (PubMed:24373286). {ECO:0000250|UniProtKB:Q9NZN3, ECO:0000269|PubMed:17507647, ECO:0000269|PubMed:24373286, ECO:0000269|PubMed:25825486}. SUBUNIT: Homooligomer. Heterooligomer with EHD1 (PubMed:12121420). Heterooligomer with EHD2 and EHD4; ATP-binding is required for heterooligomerization (By similarity). Interacts with PACSIN1 (PubMed:15930129). Interacts with PACSIN2 (PubMed:15930129). Interacts (via EH domain) with MICALL1 (By similarity). Interacts (via EH domain) with RAB11FIP2 (By similarity). Interacts with ANK2 (By similarity). Interacts with CACNA1GG and CACNA1H (PubMed:25825486). {ECO:0000250|UniProtKB:Q9NZN3, ECO:0000269|PubMed:12121420, ECO:0000269|PubMed:15930129, ECO:0000269|PubMed:25825486}. DOMAIN: The EH domain interacts with Asn-Pro-Phe (NPF) motifs of target proteins. {ECO:0000250|UniProtKB:Q9WVK4}. TISSUE SPECIFICITY: Strong expression seen in the kidney, brain and liver. In the kidney, expressed exclusively by glomerular endothelial cells; at protein level. Expressed in skeletal muscle neuromuscular junction perisynaptic region; at protein level. {ECO:0000269|PubMed:17251388, ECO:0000269|PubMed:21408024, ECO:0000269|PubMed:22974368}. +Q6PJN8 DALD3_MOUSE DALR anticodon-binding domain-containing protein 3 538 58,733 Alternative sequence (1); Chain (1); Sequence conflict (1) +Q76LW6 DAND5_MOUSE DAN domain family member 5 (Cerberus-like protein 2) (Cerl-2) 185 19,772 Chain (1); Disulfide bond (4); Domain (1); Glycosylation (1); Signal peptide (1) FUNCTION: Seems to play a role in the correct specification of the left-right axis. May antagonize NODAL and BMP4 signaling. Cystine knot-containing proteins play important roles during development, organogenesis, and tissue growth and differentiation. {ECO:0000269|PubMed:15466485}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q80U19 DAAM2_MOUSE Disheveled-associated activator of morphogenesis 2 1115 128,370 Alternative sequence (2); Chain (1); Coiled coil (1); Compositional bias (1); Domain (4); Erroneous initiation (1); Sequence caution (1); Sequence conflict (2) FUNCTION: Key regulator of the Wnt signaling pathway, which is required for various processes during development, such as dorsal patterning, determination of left/right symmetry or myelination in the central nervous system (PubMed:22227309, PubMed:24091014, PubMed:25754822). Acts downstream of Wnt ligands and upstream of beta-catenin (CTNNB1) (PubMed:22227309, PubMed:25754822). Required for canonical Wnt signaling pathway during patterning in the dorsal spinal cord by promoting the aggregation of Disheveled (Dvl) complexes, thereby clustering and formation of Wnt receptor signalosomes and potentiating Wnt activity (PubMed:22227309). During dorsal patterning of the spinal cord, inhibits oligodendrocytes differentiation via interaction with PIP5K1A (PubMed:25754822). Also regulates non-canonical Wnt signaling pathway (PubMed:24091014). Acts downstream of PITX2 in the developing gut and is required for left/right asymmetry within dorsal mesentery: affects mesenchymal condensation by lengthening cadherin-based junctions through WNT5A and non-canonical Wnt signaling, inducing polarized condensation in the left dorsal mesentery necessary to initiate gut rotation (PubMed:24091014). Together with DAAM1, required for myocardial maturation and sarcomere assembly (PubMed:26526197). {ECO:0000269|PubMed:22227309, ECO:0000269|PubMed:24091014, ECO:0000269|PubMed:25754822, ECO:0000269|PubMed:26526197}. SUBUNIT: Interacts with DVL3. {ECO:0000269|PubMed:22227309}. DOMAIN: The DAD domain regulates activation via by an autoinhibitory interaction with the GBD/FH3 domain. This autoinhibition is released upon competitive binding of an activated GTPase. The release of DAD allows the FH2 domain to then nucleate and elongate nonbranched actin filaments (By similarity). {ECO:0000250|UniProtKB:O08808}. TISSUE SPECIFICITY: In early embryogenesis, expression is confined to embryonic ectoderm. Highly dynamic expression in later stages of gastrulation. In early somite stages, detected in posterior node and persists until 9-10 somites have developed when expression is concentrated in the chordoneural hinge. During organogenesis, expressed in the CNS, PNS, liver primordia, limb buds and genital tubercle. {ECO:0000269|PubMed:15464228, ECO:0000269|PubMed:15533824}. +O08967 CYH3_MOUSE Cytohesin-3 (ARF nucleotide-binding site opener 3) (Protein ARNO3) (General receptor of phosphoinositides 1) (Grp1) (PH, SEC7 and coiled-coil domain-containing protein 3) (CLM3) (SEC7 homolog C) (mSec7-3) 399 46,280 Beta strand (12); Binding site (4); Chain (1); Coiled coil (1); Domain (2); Helix (12); Mutagenesis (13); Region (2); Turn (2) FUNCTION: Promotes guanine-nucleotide exchange on ARF1. Promotes the activation of ARF factors through replacement of GDP with GTP (PubMed:18042453). Play a role in the epithelial polarization (PubMed:20080746). {ECO:0000269|PubMed:18042453, ECO:0000269|PubMed:20080746}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:18042453}; Peripheral membrane protein {ECO:0000269|PubMed:18042453}. Cell junction, adherens junction {ECO:0000269|PubMed:20080746}. Cell junction, tight junction {ECO:0000269|PubMed:20080746}. Note=Translocates from the cytosol to membranes enriched in phosphatidylinositol 3,4,5-trisphosphate. SUBUNIT: Interacts with GRASP. Interacts with FRMD4A (PubMed:20080746). Interacts with FRMD4B (PubMed:20080746). {ECO:0000269|PubMed:10828067, ECO:0000269|PubMed:10983984, ECO:0000269|PubMed:10983985, ECO:0000269|PubMed:15359279, ECO:0000269|PubMed:18042453, ECO:0000269|PubMed:20080746}. DOMAIN: Binds via its PH domain to the inositol head group of phosphatidylinositol 3,4,5-trisphosphate.; DOMAIN: Autoinhibited by its C-terminal basic region. +Q9QXA1 CYHR1_MOUSE Cysteine and histidine-rich protein 1 311 35,757 Alternative sequence (4); Chain (1); Erroneous initiation (1); Zinc finger (2) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10745073}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10745073}. Note=Shows a prominent perinuclear and cytoplasmic localization. SUBUNIT: Interacts with LGALS3. {ECO:0000269|PubMed:10745073, ECO:0000269|PubMed:12765788}. TISSUE SPECIFICITY: Expressed in heart, brain, liver, testis and kidney. {ECO:0000269|PubMed:10745073}. +Q8C088 EGFEM_MOUSE EGF-like and EMI domain-containing protein 1 590 65,021 Alternative sequence (1); Chain (1); Disulfide bond (14); Domain (6); Sequence conflict (1); Signal peptide (1) +P18406 CYR61_MOUSE Protein CYR61 (3CH61) (CCN family member 1) (Cysteine-rich angiogenic inducer 61) (Insulin-like growth factor-binding protein 10) (IBP-10) (IGF-binding protein 10) (IGFBP-10) 379 41,709 Chain (1); Disulfide bond (5); Domain (4); Modified residue (1); Region (1); Signal peptide (1) FUNCTION: Promotes cell proliferation, chemotaxis, angiogenesis and cell adhesion. Appears to play a role in wound healing by up-regulating, in skin fibroblasts, the expression of a number of genes involved in angiogenesis, inflammation and matrix remodeling including VEGA-A, VEGA-C, MMP1, MMP3, TIMP1, uPA, PAI-1 and integrins alpha-3 and alpha-5 (By similarity). CYR61-mediated gene regulation is dependent on heparin-binding (By similarity). Down-regulates the expression of alpha-1 and alpha-2 subunits of collagen type-1 (By similarity). Promotes cell adhesion and adhesive signaling through integrin alpha-6/beta-1, cell migration through integrin alpha-1/beta-5 and cell proliferation through integrin alpha-v/beta-3 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Interaction with integrins is heparin- and cell-type-dependent and promotes cell adhesion. {ECO:0000250}. TISSUE SPECIFICITY: Low in kidney, adrenal gland, testes, brain, and ovary, moderate in heart, uterus, and skeletal muscle, highest in lung. +Q9D2H9 DAAF1_MOUSE Dynein assembly factor 1, axonemal (Leucine-rich repeat-containing protein 50) 634 69,704 Chain (1); Compositional bias (1); Domain (1); Modified residue (4); Repeat (6) FUNCTION: Cilium-specific protein required for the stability of the ciliary architecture. Plays a role in cytoplasmic preassembly of dynein arms (By similarity). Involved in regulation of microtubule-based cilia and actin-based brush border microvilli (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000250}. +A6X919 D19L1_MOUSE Probable C-mannosyltransferase DPY19L1 (EC 2.4.1.-) (Dpy-19-like protein 1) (Protein dpy-19 homolog 1) 746 84,187 Alternative sequence (3); Chain (1); Frameshift (1); Modified residue (2); Sequence conflict (1); Transmembrane (11) TRANSMEM 137 159 Helical. {ECO:0000255}.; TRANSMEM 227 247 Helical. {ECO:0000255}.; TRANSMEM 257 279 Helical. {ECO:0000255}.; TRANSMEM 307 325 Helical. {ECO:0000255}.; TRANSMEM 331 350 Helical. {ECO:0000255}.; TRANSMEM 357 374 Helical. {ECO:0000255}.; TRANSMEM 380 396 Helical. {ECO:0000255}.; TRANSMEM 405 425 Helical. {ECO:0000255}.; TRANSMEM 481 501 Helical. {ECO:0000255}.; TRANSMEM 520 540 Helical. {ECO:0000255}.; TRANSMEM 562 582 Helical. {ECO:0000255}. FUNCTION: Probable C-mannosyltransferase that mediates C-mannosylation of tryptophan residues on target proteins. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q91XC8 DAP1_MOUSE Death-associated protein 1 (DAP-1) 102 11,155 Chain (1); Initiator methionine (1); Modified residue (6) FUNCTION: Negative regulator of autophagy. Involved in mediating interferon-gamma-induced cell death (By similarity). {ECO:0000250}. PTM: Phosphorylated. Phosphorylation by MTOR inhibits the suppressive activity of DAP toward autophagy (By similarity). {ECO:0000250}. +Q9D757 DAPL1_MOUSE Death-associated protein-like 1 (Early epithelial differentiation-associated protein) 107 11,813 Chain (1) FUNCTION: May play a role in the early stages of epithelial differentiation or in apoptosis. {ECO:0000269|PubMed:15920738}. TISSUE SPECIFICITY: Expressed in hair follicle, corneal epithelium, epidermis and footpad epithelium (at protein level). {ECO:0000269|PubMed:15920738}. +Q80YW0 CYH4_MOUSE Cytohesin-4 (PH, SEC7 and coiled-coil domain-containing protein 4) 393 45,285 Binding site (3); Chain (1); Coiled coil (1); Domain (2); Region (2) FUNCTION: Promotes guanine-nucleotide exchange on ARF1 and ARF5. Promotes the activation of ARF factors through replacement of GDP with GTP (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. DOMAIN: Binds via its PH domain to the inositol head group of phosphatidylinositol 3,4,5-trisphosphate. {ECO:0000250}.; DOMAIN: Autoinhibited by its C-terminal basic region. {ECO:0000250}. +Q8CH20 CYPT1_MOUSE Cysteine-rich perinuclear theca protein 1 168 18,957 Alternative sequence (1); Chain (1); Compositional bias (2); Sequence conflict (7) SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, perinuclear theca {ECO:0000269|PubMed:15286030}. Note=Found in the postacrosomal region of the perinuclear theca. {ECO:0000269|PubMed:15286030}. TISSUE SPECIFICITY: Specifically expressed in spermatozoa (at protein level). Detected from the elongated spermatid stage onwards; not found in immature germ cells or somatic cells (at protein level). {ECO:0000269|PubMed:15286030}. +Q5DW34 EHMT1_MOUSE Histone-lysine N-methyltransferase EHMT1 (EC 2.1.1.-) (EC 2.1.1.43) (Euchromatic histone-lysine N-methyltransferase 1) (Eu-HMTase1) (G9a-like protein 1) (GLP) (GLP1) (Lysine N-methyltransferase 1D) 1296 141,999 Alternative sequence (3); Binding site (3); Chain (1); Compositional bias (2); Cross-link (12); Domain (2); Erroneous initiation (1); Initiator methionine (1); Metal binding (16); Modified residue (4); Mutagenesis (4); Region (5); Repeat (8); Sequence conflict (1) FUNCTION: Histone methyltransferase that specifically mono- and dimethylates 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin. H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting HP1 proteins to methylated histones. Also weakly methylates 'Lys-27' of histone H3 (H3K27me). Also required for DNA methylation, the histone methyltransferase activity is not required for DNA methylation, suggesting that these 2 activities function independently. Probably targeted to histone H3 by different DNA-binding proteins like E2F6, MGA, MAX and/or DP1. During G0 phase, it probably contributes to silencing of MYC- and E2F-responsive genes, suggesting a role in G0/G1 transition in cell cycle. In addition to the histone methyltransferase activity, also methylates non-histone proteins: mediates dimethylation of 'Lys-373' of p53/TP53. {ECO:0000269|PubMed:15774718, ECO:0000269|PubMed:18818694}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15774718}. Chromosome {ECO:0000269|PubMed:15774718}. Note=Associates with euchromatic regions. SUBUNIT: Interacts with WIZ. Part of the E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EHMT1, RING1, RNF2, MBLR, L3MBTL2 and YAF2. Interacts with MPHOSPH8 (By similarity). Interacts with CDYL. Interacts with REST only in the presence of CDYL. Part of a complex containing at least CDYL, REST, WIZ, SETB1, EHMT1 and EHMT2 (By similarity). Heterodimer; heterodimerizes with EHMT2. Interacts (via ANK repeats) with RELA (when monomethylated at 'Lys-310'). {ECO:0000250, ECO:0000269|PubMed:15774718, ECO:0000269|PubMed:21131967}. DOMAIN: The ANK repeats specifically recognize and bind H3K9me1 and H3K9me2 (By similarity). They also specifically recognize and bind RELA subunit of NF-kappa-B, when RELA is monomethylated at 'Lys-310'. {ECO:0000250, ECO:0000269|PubMed:21131967}.; DOMAIN: The SET domain mediates interaction with WIZ. {ECO:0000250}.; DOMAIN: In the pre-SET domain, Cys residues bind 3 zinc ions that are arranged in a triangular cluster; some of these Cys residues contribute to the binding of two zinc ions within the cluster. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15774718}. +Q62426 CYTB_MOUSE Cystatin-B (Stefin-B) 98 11,046 Chain (1); Modified residue (1); Motif (1); Site (1) FUNCTION: This is an intracellular thiol proteinase inhibitor. SUBCELLULAR LOCATION: Cytoplasm. TISSUE SPECIFICITY: Widely expressed. Highest expression in heart, liver and kidney. Lower levels in brain, lung and skeletal muscle. Lowest levels in spleen and testis. +O89098 CYTF_MOUSE Cystatin-F (Cystatin-7) (Cystatin-like metastasis-associated protein) (CMAP) (Leukocystatin) 144 16,380 Chain (1); Disulfide bond (2); Glycosylation (1); Motif (1); Signal peptide (1); Site (1) FUNCTION: Inhibits papain and cathepsin L but with affinities lower than other cystatins. May play a role in immune regulation through inhibition of a unique target in the hematopoietic system. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +P0CW70 D19L2_MOUSE Probable C-mannosyltransferase DPY19L2 (EC 2.4.1.-) (Dpy-19-like protein 2) (Protein dpy-19 homolog 2) 773 89,882 Chain (1); Transmembrane (9) TRANSMEM 123 143 Helical. {ECO:0000255}.; TRANSMEM 210 230 Helical. {ECO:0000255}.; TRANSMEM 257 277 Helical. {ECO:0000255}.; TRANSMEM 312 332 Helical. {ECO:0000255}.; TRANSMEM 345 367 Helical. {ECO:0000255}.; TRANSMEM 387 407 Helical. {ECO:0000255}.; TRANSMEM 438 458 Helical. {ECO:0000255}.; TRANSMEM 508 528 Helical. {ECO:0000255}.; TRANSMEM 549 569 Helical. {ECO:0000255}. FUNCTION: Probable C-mannosyltransferase that mediates C-mannosylation of tryptophan residues on target proteins. Required during spermatogenesis for sperm head elongation and acrosome formation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Predominantly expressed in testis. Present in testis but absent from epididymal sperm (at protein level). {ECO:0000269|PubMed:21397064}. +A2AJQ3 D19L4_MOUSE Probable C-mannosyltransferase DPY19L4 (EC 2.4.1.-) (Dpy-19-like protein 4) (Protein dpy-19 homolog 4) 722 83,604 Alternative sequence (1); Chain (1); Initiator methionine (1); Modified residue (1); Transmembrane (12) TRANSMEM 51 71 Helical. {ECO:0000255}.; TRANSMEM 160 177 Helical. {ECO:0000255}.; TRANSMEM 183 201 Helical. {ECO:0000255}.; TRANSMEM 246 262 Helical. {ECO:0000255}.; TRANSMEM 268 284 Helical. {ECO:0000255}.; TRANSMEM 291 307 Helical. {ECO:0000255}.; TRANSMEM 313 331 Helical. {ECO:0000255}.; TRANSMEM 351 369 Helical. {ECO:0000255}.; TRANSMEM 420 440 Helical. {ECO:0000255}.; TRANSMEM 465 485 Helical. {ECO:0000255}.; TRANSMEM 487 507 Helical. {ECO:0000255}.; TRANSMEM 521 541 Helical. {ECO:0000255}. FUNCTION: Probable C-mannosyltransferase that mediates C-mannosylation of tryptophan residues on target proteins. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q925Q8 DACH2_MOUSE Dachshund homolog 2 (Dach2) 634 68,588 Alternative sequence (5); Chain (1); Coiled coil (1); Compositional bias (1); Region (2); Sequence conflict (1) FUNCTION: Transcription factor that is involved in regulation of organogenesis. Seems to be a regulator for SIX1 and SIX6. Seems to act as a corepressor of SIX6 in regulating proliferation by directly repressing cyclin-dependent kinase inhibitors, including the p27Kip1 promoter. Is recruited with SIX6 to the p27Kip1 promoter in embryonal retina. SIX6 corepression seems also to involve NCOR1, TBL1, HDAC1 and HDAC3. May be involved together with PAX3, SIX1, and EYA2 in regulation of myogenesis. In the developing somite, expression of DACH2 and PAX3 is regulated by the overlying ectoderm, and DACH2 and PAX3 positively regulate each other's expression. Probably binds to DNA via its DACHbox-N domain. {ECO:0000269|PubMed:12112464, ECO:0000269|PubMed:12130660}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Interacts with SIX6. Interacts with EYA2 (By similarity). {ECO:0000250}. DOMAIN: The DACHbox-N domain forms a structure containing a DNA binding motif similar to that of the forkhead/winged helix domain. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in embryo, and at lower levels in the newborn. {ECO:0000269|PubMed:11287190}. +Q8R4A3 DACT1_MOUSE Dapper homolog 1 (Dapper antagonist of catenin 1) (Frodo homolog) (MDpr1) (Thymus-expressed novel gene 3 protein) 778 84,306 Chain (1); Coiled coil (1); Erroneous initiation (1); Frameshift (1); Modified residue (1); Motif (3); Region (1); Sequence conflict (7) FUNCTION: Involved in regulation of intracellular signaling pathways during development. Specifically thought to play a role in canonical and/or non-canonical Wnt signaling pathways through interaction with DSH (Dishevelled) family proteins. The activation/inhibition of Wnt signaling may depend on the phosphorylation status. Proposed to regulate the degradation of CTNNB1/beta-catenin, thereby modulating the transcriptional activation of target genes of the Wnt signaling pathway. Its function in stabilizing CTNNB1 may involve inhibition of GSK3B activity. Promotes the membrane localization of CTNNB1. The cytoplasmic form can induce DVL2 degradation via a lysosome-dependent mechanism; the function is inhibited by PKA-induced binding to 14-3-3 proteins, such as YWHAB (By similarity). Seems to be involved in morphogenesis at the primitive streak by regulating VANGL2 and DVL2; the function seems to be independent of canonical Wnt signaling and rather involves the non-canonical Wnt/planar cell polarity (PCP) pathway. The nuclear form may prevent the formation of LEF1:CTNNB1 complex and recruit HDAC1 to LEF1 at target gene promoters to repress transcription thus antagonizing Wnt signaling (By similarity). May be involved in positive regulation of fat cell differentiation. During neuronal differentiation may be involved in excitatory synapse organization, and dendrite formation and establishment of spines. {ECO:0000250, ECO:0000269|PubMed:17197390, ECO:0000269|PubMed:19073771, ECO:0000269|PubMed:19701191, ECO:0000269|PubMed:20145239, ECO:0000269|PubMed:20335472}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cell junction, synapse {ECO:0000269|PubMed:20335472}. Note=Shuttles between the nucleus and the cytoplasm. Seems to be nuclear in the absence of Wnt signaling and to translocate to the cytoplasm in its presence (By similarity). {ECO:0000250}. SUBUNIT: Can form homodimers and heterodimers with DACT2 or DACT3. Interacts with CSNK1D, PKA catalytic subunit, PKC-type kinase, CSNK2A1, CSNK2B, DVL1, DLV2, DVAL3, VANGL1, VANGL2, CTNND1 and HDAC1. Interacts with GSK3B; the interaction is indicative for an association of DACT1 with the beta-catenin destruction complex. Interacts with GSK3A. Interacts with YWHAB; the interaction is enhanced by PKA phosphorylating DACT1 at Ser-769. Interacts with CTNNB1 (By similarity). {ECO:0000250}. DOMAIN: The C-terminal PDZ-binding motif mediates interaction with the PDZ domains of DSH (Dishevelled) family proteins. {ECO:0000269|PubMed:14636582}. TISSUE SPECIFICITY: Expressed in multiple tissues including brain, heart, kidney, liver and testis. {ECO:0000269|PubMed:11970895, ECO:0000269|PubMed:16881060}. +Q7TN08 DACT2_MOUSE Dapper homolog 2 (mDpr2) (Dapper antagonist of catenin 2) 757 81,668 Chain (1); Coiled coil (1); Frameshift (1); Motif (1); Region (1); Sequence conflict (3) FUNCTION: Involved in regulation of intracellular signaling pathways during development. Negatively regulates the Nodal signaling pathway, possibly by promoting the lysosomal degradation of Nodal receptors, such as TGFBR1. May be involved in control of the morphogenetic behavior of kidney ureteric bud cells by keeping cells epithelial and restraining their mesenchymal character. May play an inhibitory role in the re-epithelialization of skin wounds by attenuating TGF-beta signaling. {ECO:0000269|PubMed:17197390, ECO:0000269|PubMed:18716284, ECO:0000269|PubMed:20685821}. SUBUNIT: Can form homodimers and heterodimers with DACT1 or DACT3. Interacts with CSNK1D, PKA catalytic subunit, PKC-type kinase, CSNK2B, DVL1, DVL2, DVL3, VANGL1, VANGL2, TGFBR1, CTNNB1, CTNND2, CTNND1, LEF1, TCF7, TCF7L1 and HDAC1. {ECO:0000269|PubMed:17197390, ECO:0000269|PubMed:21718540}. DOMAIN: The C-terminal PDZ-binding motif may mediate interaction with the PDZ domains of DSH (Dishevelled) family proteins. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in kidney (inner medullary collecting duct). Expressed in epidermal keratinocytes and hair follicles. {ECO:0000269|PubMed:18716284, ECO:0000269|PubMed:20685821}. +Q62165 DAG1_MOUSE Dystroglycan (Dystrophin-associated glycoprotein 1) [Cleaved into: Alpha-dystroglycan (Alpha-DG); Beta-dystroglycan (Beta-DG)] 893 96,905 Beta strand (13); Chain (2); Compositional bias (2); Disulfide bond (2); Domain (1); Glycosylation (7); Helix (7); Modified residue (2); Motif (2); Mutagenesis (3); Region (6); Sequence conflict (4); Signal peptide (1); Site (2); Topological domain (2); Transmembrane (1); Turn (2) TRANSMEM 752 772 Helical. {ECO:0000255}. TOPO_DOM 652 751 Extracellular. {ECO:0000255}.; TOPO_DOM 773 893 Cytoplasmic. {ECO:0000255}. FUNCTION: The dystroglycan complex is involved in a number of processes including laminin and basement membrane assembly, sacrolemmal stability, cell survival, peripheral nerve myelination, nodal structure, cell migration, and epithelial polarization.; FUNCTION: Alpha-dystroglycan is an extracellular peripheral glycoprotein that acts as a receptor for both extracellular matrix proteins containing laminin-G domains, and for certain adenoviruses. Receptor for laminin-2 (LAMA2) and agrin in peripheral nerve Schwann cells. Also receptor for lymphocytic choriomeningitis virus, Old World Lassa fever virus, and clade C New World arenaviruses.; FUNCTION: Beta-dystroglycan is a transmembrane protein that plays important roles in connecting the extracellular matrix to the cytoskeleton. Acts as a cell adhesion receptor in both muscle and non-muscle tissues. Receptor for both DMD and UTRN and, through these interactions, scaffolds axin to the cytoskeleton. Also functions in cell adhesion-mediated signaling and implicated in cell polarity (By similarity). {ECO:0000250, ECO:0000269|PubMed:12797959, ECO:0000269|PubMed:12843252, ECO:0000269|PubMed:9175728}. PTM: O- and N-glycosylated (By similarity). POMGNT1 catalyzes the initial addition of N-acetylglucosamine, giving rise to the GlcNAc(beta1-2)Man(alpha1-)O-Ser/Thr moiety and thus providing the necessary basis for the addition of further carbohydrate moieties. Alpha-dystroglycan is heavily O-glycosylated comprising of up to two thirds of its mass and the carbohydrate composition differs depending on tissue type. Mucin-type O-glycosylation is important for ligand binding activity. O-mannosylation of alpha-DAG1 is found in high abundance in both brain and muscle where the most abundant glycan is Sia-alpha-2-3-Gal-beta-1-4-Glc-NAc-beta-1-2-Man. In muscle, glycosylation on Thr-315, Thr-317, Thr-379 by a phosphorylated O-mannosyl glycan with the structure 2-(N-acetylamido)-2-deoxygalactosyl-beta-1,3-2-(N-acetylamido)-2-deoxyglucosyl-beta-1,4-6-phosphomannose is mediated by like-acetylglucosaminyltransferase (LARGE1) protein amd is required for laminin binding. O-glycosylated in the N-terminal region with a core 1 or possibly core 8 glycan. The beta subunit is N-glycosylated (By similarity). {ECO:0000250|UniProtKB:Q14118, ECO:0000269|PubMed:20044576}.; PTM: Autolytic cleavage produces the alpha and beta subunits. In cutaneous cells, as well as in certain pathological conditions, shedding of beta-dystroglcan can occur releasing a peptide of about 30 kDa (By similarity). {ECO:0000250}.; PTM: SRC-mediated phosphorylation of the PPXY motif of the beta subunit recruits SH2 domain-containing proteins, but inhibits binding to WWW domain-containing proteins, DMD and UTRN. This phosphorylation also inhibits nuclear entry (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Alpha-dystroglycan: Secreted, extracellular space {ECO:0000250}.; SUBCELLULAR LOCATION: Beta-dystroglycan: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton. Nucleus, nucleoplasm. Cell membrane, sarcolemma. Cell junction, synapse, postsynaptic cell membrane. Note=The monomeric form translocates to the nucleus via the action of importins and depends on RAN. Nuclear transport is inhibited by Tyr-892 phosphorylation. In skeletal muscle, this phosphorylated form locates to a vesicular internal membrane compartment. In muscle cells, sarcolemma localization requires the presence of ANK2, while localization to costameres requires the presence of ANK3. Localizes to neuromuscular junctions (NMJs). In adult muscle, NMJ localization depends upon ANK2 presence, but not in newborn animals. In peripheral nerves, localizes to the Schwann cell membrane. Colocalizes with ERM proteins in Schwann-cell microvilli. SUBUNIT: Monomer. Heterodimer of alpha- and beta-dystroglycan subunits which are the central components of the dystrophin-glycoprotein complex. This complex then can form a dystrophin-associated glycoprotein complex (DGC) which is composed of three subcomplexes: a cytoplasmic complex comprised of DMD (or UTRN), DTNA and a number of syntrophins, such as SNTB1, SNTB2, SNTG1 and SNTG2, the transmembrane dystroglycan complex, and the sarcoglycan-sarcospan complex. Interacts (via the N-terminal of alphaDAG1) with LARGE1; the interaction enhances laminin binding (By similarity). Interacts with SGCD. Interacts with AGR2 and AGR3. Interacts (betaDAG1) with DMD; the interaction is inhibited by phosphorylation on the PPXY motif. Interacts (betaDAG1, via its PPXY motif) with UTRN (via its WWW and ZZ domains); the interaction is inhibited by phosphorylation on the PPXY motif. Interacts (betaDAG1, via its phosphorylated PPXY motif) with the SH2 domain-containing proteins, FYN, CSK, NCK and SHC. Interacts (betaDAG1) with CAV3 (via a central WW-like domain); the interaction disrupts the binding of DMD. BetaDAG1 directly interacts with ANK3, but not with ANK2; this interaction does not interfere with DMD-binding and is required for retention at costameres (By similarity). Identified in a dystroglycan complex that contains at least PRX, DRP2, UTRN, DMD and DAG1 (PubMed:11430802). Interacts with POMGNT1 (By similarity). {ECO:0000250|UniProtKB:Q14118, ECO:0000250|UniProtKB:Q28685, ECO:0000269|PubMed:11430802, ECO:0000269|PubMed:11495720, ECO:0000269|PubMed:15326183, ECO:0000269|PubMed:19109891, ECO:0000269|PubMed:9864373}. TISSUE SPECIFICITY: Detected in sciatic nerve (at protein level) (PubMed:11430802). Expressed in a variety of tissues. In brain, expressed in the hippocampal formation, the olfactory bulb, the cerebellum and the thalamus. In the peripheral nerve system, expressed in Schwann cells. {ECO:0000269|PubMed:11430802, ECO:0000269|PubMed:12843252, ECO:0000269|PubMed:7833916, ECO:0000269|PubMed:9175728}. +A6PWD2 FHAD1_MOUSE Forkhead-associated domain-containing protein 1 (FHA domain-containing protein 1) 1420 163,728 Alternative sequence (8); Chain (1); Coiled coil (5); Compositional bias (1); Domain (1); Sequence conflict (1) +Q9ERZ6 FIGN_MOUSE Fidgetin 759 82,098 Alternative sequence (1); Binding site (1); Chain (1); Compositional bias (1); Modified residue (1); Nucleotide binding (1); Sequence conflict (3) FUNCTION: ATP-dependent microtubule severing protein. Severs microtubules along their length and depolymerizes their ends, primarily the minus-end, suppressing microtubule growth from and attachment to centrosomes. Microtubule severing may promote rapid reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. Microtubule release from the mitotic spindle poles may allow depolymerization of the microtubule end proximal to the spindle pole, leading to poleward microtubule flux and poleward motion of chromosome (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000269|PubMed:16751186}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Note=Localizes to centrosomes throughout mitosis and to the spindle midzone during telophase. {ECO:0000250}. SUBUNIT: Interacts with AKAP8 (via C-terminus). {ECO:0000269|PubMed:16751186}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11017077}. DISEASE: Note=Defects in Fign are characterized by a side-to-side head-shaking and circling behavior, due to reduced or absent semicircular canals. Diseased mice also have small eyes, associated with cell-cycle delay and insufficient growth of the retinal neural epithelium, and lower penetrance skeletal abnormalities, including pelvic girdle dysgenesis, skull bone fusions and polydactyly. {ECO:0000269|PubMed:11017077}. +A2AJL3 FGGY_MOUSE FGGY carbohydrate kinase domain-containing protein (EC 2.7.1.-) 552 60,336 Alternative sequence (2); Chain (1); Erroneous initiation (1); Frameshift (1); Sequence conflict (1) +Q9JHE6 HES6_MOUSE Transcription cofactor HES-6 (Hairy and enhancer of split 6) 224 24,454 Chain (1); Domain (2); Motif (1) FUNCTION: Does not bind DNA itself but suppresses both HES1-mediated N box-dependent transcriptional repression and binding of HES1 to E box sequences. Also suppresses HES1-mediated inhibition of the heterodimer formed by ASCL1/MASH1 and TCF3/E47, allowing ASCL1 and TCF3 to up-regulate transcription in its presence. Promotes cell differentiation. {ECO:0000269|PubMed:10851137}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Transcription repression requires formation of a complex with a corepressor protein of the Groucho/TLE family (By similarity). Interacts with HES1. {ECO:0000250, ECO:0000269|PubMed:10851137}. DOMAIN: The C-terminal WRPW motif is a transcriptional repression domain necessary for the interaction with Groucho/TLE family members, transcriptional corepressors recruited to specific target DNA by Hairy-related proteins. {ECO:0000250}.; DOMAIN: Has a particular type of basic domain (presence of a helix-interrupting proline) that binds to the N-box (CACNAG), rather than the canonical E-box (CANNTG). TISSUE SPECIFICITY: Expressed in both undifferentiated and differentiated cells. High levels of expression are observed in several embryonic tissues including the nervous system, muscle and thymus. In the nervous system, initially expressed in the closing neural tube, then in the spinal cord, cranial and dorsal root ganglia, and brain neuroepithelium. Also expressed in epithelial cells of the embryonic respiratory, urinary and digestive systems. In the limb buds, expressed in skeletal muscle and presumptive tendons. {ECO:0000269|PubMed:10906477, ECO:0000269|PubMed:11044617}. +Q9WTJ4 FIZ1_MOUSE Flt3-interacting zinc finger protein 1 500 52,685 Chain (1); Modified residue (1); Sequence conflict (1); Zinc finger (11) FUNCTION: May be a transcriptional repressor of NRL function in photoreceptors. Does not repress CRX-mediated transactivation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409713}. Nucleus {ECO:0000269|PubMed:10409713}. SUBUNIT: Interacts with FLT3 cytoplasmic catalytic domain, following receptor stimulation, in a kinase-independent manner. Does not interact with other structurally related receptor tyrosine kinases, including KIT, CSF1R and PDGFR. Interacts with NRL (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. In the retina, highest expression in the ganglion cell layer. {ECO:0000269|PubMed:10409713, ECO:0000269|PubMed:12566383}. +Q8BQB4 FJX1_MOUSE Four-jointed box protein 1 (Four-jointed protein x1) (Four-jointed protein homolog) 450 50,396 Chain (1); Compositional bias (1); Frameshift (1); Glycosylation (2); Sequence conflict (1); Signal peptide (1) FUNCTION: Acts as an inhibitor of dendrite extension and branching. {ECO:0000269|PubMed:18028897}. PTM: Glycosylated. {ECO:0000269|PubMed:16145673}.; PTM: Undergoes proteolytic cleavage. {ECO:0000269|PubMed:16145673}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16145673}. TISSUE SPECIFICITY: Expressed in brain, kidney and lung. In the telencephalon, expressed in the piriform cortex, hippocampus and olfactory bulb. In the diencephalon, expressed in the dorsal thalamus. Expressed in Purkinje cells of the cerebellum and in numerous medullary nuclei. {ECO:0000269|PubMed:10072791, ECO:0000269|PubMed:16059920, ECO:0000269|PubMed:16145673}. +Q9D1M7 FKB11_MOUSE Peptidyl-prolyl cis-trans isomerase FKBP11 (PPIase FKBP11) (EC 5.2.1.8) (19 kDa FK506-binding protein) (19 kDa FKBP) (FKBP-19) (FK506-binding protein 11) (FKBP-11) (Rotamase) 201 22,137 Chain (1); Domain (1); Sequence conflict (2); Signal peptide (1); Transmembrane (1) TRANSMEM 156 176 Helical. {ECO:0000255}. FUNCTION: PPIases accelerate the folding of proteins during protein synthesis. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. SUBUNIT: Interacts with IFITM5. {ECO:0000269|PubMed:20838829}. +Q9CS72 FLIP1_MOUSE Filamin-A-interacting protein 1 (FILIP) 1211 137,599 Chain (1); Coiled coil (2); Erroneous initiation (1); Modified residue (2) FUNCTION: By acting through a filamin-A/F-actin axis, it controls the start of neocortical cell migration from the ventricular zone. May be able to induce the degradation of filamin-A. {ECO:0000250|UniProtKB:Q8K4T4}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q7Z7B0, ECO:0000250|UniProtKB:Q8K4T4}. SUBUNIT: Interacts with FLNA. Interacts with RHOD (in GTP-bound form). {ECO:0000269|PubMed:15794127}. +P50285 FMO1_MOUSE Dimethylaniline monooxygenase [N-oxide-forming] 1 (EC 1.14.13.8) (Dimethylaniline oxidase 1) (Hepatic flavin-containing monooxygenase 1) (FMO 1) 532 59,915 Binding site (1); Chain (1); Nucleotide binding (5); Site (1); Transmembrane (1) TRANSMEM 511 531 Helical. {ECO:0000255}. FUNCTION: This protein is involved in the oxidative metabolism of a variety of xenobiotics such as drugs and pesticides. Form I catalyzes the N-oxygenation of secondary and tertiary amines. SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250|UniProtKB:Q95LA2}; Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q95LA2}; Single-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Liver. +Q8C0T1 FM1AB_MOUSE Protein fem-1 homolog A-B (FEM1a-B) (FEM1-alpha-B) 654 72,210 Chain (1); Erroneous initiation (1); Repeat (11) Protein modification; protein ubiquitination. FUNCTION: Probable component of an E3 ubiquitin-protein ligase complex, in which it may act as a substrate recognition subunit. May participate in antiinflammatory signaling via its interaction with PTGER4 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Component of some E3 ubiquitin-protein ligase complex. Interacts with PTGER4 (By similarity). {ECO:0000250}. +Q8K2I3 FMO2_MOUSE Dimethylaniline monooxygenase [N-oxide-forming] 2 (EC 1.14.13.8) (Dimethylaniline oxidase 2) (Pulmonary flavin-containing monooxygenase 2) (FMO 2) 535 60,974 Binding site (1); Chain (1); Initiator methionine (1); Modified residue (1); Nucleotide binding (5); Sequence conflict (1); Transmembrane (1) TRANSMEM 510 530 Helical. {ECO:0000255}. FUNCTION: This protein is involved in the oxidative metabolism of a variety of xenobiotics such as drugs and pesticides. Shows catalytic activity towards methimazole, thiourea, trimethylamine, and the insecticide phorate. SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250|UniProtKB:P17635}; Single-pass membrane protein {ECO:0000250|UniProtKB:P17635}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17635}; Single-pass membrane protein {ECO:0000250|UniProtKB:P17635}. +Q9JL26 FMNL1_MOUSE Formin-like protein 1 (Formin-related protein) 1094 122,060 Alternative sequence (3); Chain (1); Compositional bias (1); Domain (3); Initiator methionine (1); Lipidation (1); Modified residue (4); Sequence conflict (7) FUNCTION: Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the cortical actin filament dynamics and cell shape. May play a role in the control of cell motility and survival of macrophages. {ECO:0000269|PubMed:10958683, ECO:0000269|PubMed:21148482}. PTM: Myristoylation mediates membrane localization. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane; Lipid-anchor. Cytoplasmic vesicle, phagosome. Note=Recruited to actin-rich phagosomes during phagocytosis. Translocates to the plasma membrane upon activation by RAC1. SUBUNIT: Interacts with RAC1, PFN1 and PFN2. Interacts (activated by RAC1) with SRGAP2 (via SH3 domain); regulates the actin filament severing activity of FMNL1. {ECO:0000269|PubMed:10958683, ECO:0000269|PubMed:21148482}. DOMAIN: The DAD domain regulates activation via by an autoinhibitory interaction with the N-terminus. This autoinhibition is released upon competitive binding of an activated GTPase. The release of DAD allows the FH2 domain to then nucleate and elongate nonbranched actin filaments (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in the spleen, lymph node and bone marrow cells. {ECO:0000269|PubMed:10958683}. +Q61060 FOXD3_MOUSE Forkhead box protein D3 (HNF3/FH transcription factor genesis) (Hepatocyte nuclear factor 3 forkhead homolog 2) (HFH-2) 465 46,345 Chain (1); Compositional bias (2); DNA binding (1); Frameshift (1) FUNCTION: Binds to the consensus sequence 5'-A[AT]T[AG]TTTGTTT-3' and acts as a transcriptional repressor. Also acts as a transcriptional activator. Promotes development of neural crest cells from neural tube progenitors. Restricts neural progenitor cells to the neural crest lineage while suppressing interneuron differentiation. Required for maintenance of pluripotent cells in the pre-implantation and peri-implantation stages of embryogenesis. {ECO:0000269|PubMed:12381664, ECO:0000269|PubMed:8798505}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Interacts with POU5F1. {ECO:0000250|UniProtKB:Q9UJU5}. TISSUE SPECIFICITY: Expressed in premigratory and migrating neural crest cells in the early embryo and in motorneuron and interneuron progenitors in the developing spinal cord. {ECO:0000269|PubMed:11684651, ECO:0000269|PubMed:9767163}. +Q60688 FOXD4_MOUSE Forkhead box protein D4 (Forkhead-related protein FKHL9) (Forkhead-related transcription factor 5) (FREAC-5) (Transcription factor FKH-2) 444 48,047 Chain (1); Compositional bias (2); DNA binding (1); Sequence conflict (1) SUBCELLULAR LOCATION: Nucleus. DOMAIN: Contains two potential transactivation domains A and B. TISSUE SPECIFICITY: Not detected in any adult tissues tested. +Q9ES18 FOXJ2_MOUSE Forkhead box protein J2 (Fork head homologous X) 565 61,570 Chain (1); Compositional bias (3); DNA binding (1); Initiator methionine (1); Modified residue (6) FUNCTION: Transcriptional activator. Able to bind to two different type of DNA binding sites. {ECO:0000269|PubMed:11025217}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: In embryos, both cell layers of the blastocyst: the trophectoderm (TE) and the inner cell mass (ICM) show expression. Expressed in adult brain, heart skeletal muscle, lung, kidney and gonads. Liver, small intestine, and spleen also show expression but at lower levels. In the testis, expressed from pachytene spermatocytes to round spermatids, but not in spermatogonia. In addition to the germ lineage, also expressed in Sertoli cells of the testis. In the ovary, only granulosa cells of the follicles show expression. In the brain, expressed in the piriform cortex, hippocampus, habenula and in the granula cell layer in the cerebellum. {ECO:0000269|PubMed:11025217, ECO:0000269|PubMed:16376864}. +O54743 FOXF2_MOUSE Forkhead box protein F2 (Protein LUN) 446 46,383 Chain (1); Compositional bias (6); DNA binding (1); Sequence conflict (2) FUNCTION: Probable transcription activator for a number of lung-specific genes. {ECO:0000269|PubMed:9676429}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089}. SUBUNIT: Interacts with the transcription factors TBP and TFIIB. {ECO:0000250}. DOMAIN: Two activation domains, AD1 and AD2, C-terminal of (and distinct from) the forkhead domains are necessary for transcriptional activation. {ECO:0000250}. TISSUE SPECIFICITY: Uniquely expressed in the bronchiolar epithelium and in type II pneumocytes. {ECO:0000269|PubMed:9676429}. +Q64733 FOXB2_MOUSE Forkhead box protein B2 (Transcription factor FKH-4) 428 45,170 Chain (1); Compositional bias (7); DNA binding (1) FUNCTION: Transcription factor. {ECO:0000305}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +P42128 FOXK1_MOUSE Forkhead box protein K1 (Myocyte nuclear factor) (MNF) 719 74,920 Beta strand (6); Chain (1); Compositional bias (2); DNA binding (1); Domain (1); Erroneous initiation (1); Frameshift (2); Helix (4); Initiator methionine (1); Modified residue (22); Mutagenesis (2); Region (2); Sequence conflict (5) FUNCTION: Transcriptional regulator that binds to the upstream enhancer region (CCAC box) of myoglobin gene (PubMed:8007964). Important regulatory factor of the myogenic progenitor cell population (PubMed:9271401). Involved in the cell cycle process, promotes proliferation by repressing Foxo4 transcriptional activity and the cyclin-dependent kinase inhibitor, p21CIP, in the myogenic progenitor cells (PubMed:12446708). Represses myogenic differentiation by inhibiting MEFC acitivity (PubMed:22956541). Has a role in remodeling processes of adult muscles that occur in response to physiological stimuli (PubMed:9271401, PubMed:22956541). Required to correct temporal orchestration of molecular and cellular events necessary for muscle repair (PubMed:10792059). Positively regulates Wnt/beta-catenin signaling by translocating DVL into the nucleus (By similarity). Reduces virus replication, probably by binding the interferon stimulated response element (ISRE) to promote antiviral gene expression (By similarity). {ECO:0000250|UniProtKB:P85037, ECO:0000269|PubMed:10792059, ECO:0000269|PubMed:12446708, ECO:0000269|PubMed:22956541, ECO:0000269|PubMed:8007964, ECO:0000269|PubMed:9271401}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P85037, ECO:0000305}. Cytoplasm {ECO:0000250|UniProtKB:P85037}. Note=Accumulates in the nucleus upon viral infection. {ECO:0000250|UniProtKB:P85037}. SUBUNIT: Interacts with SIN3A and SIN3B (via PAH2) to form a complex which represses transcription (PubMed:10620510). Interacts with FOXO4 and MEF2C; both interactions inhibit FOXO4 and MEF2C transactivation activity (PubMed:22956541). Interacts with DVL2 and DVL3; the interaction induces DVL2 nuclear translocation (By similarity). {ECO:0000250|UniProtKB:P85037, ECO:0000269|PubMed:10620510, ECO:0000269|PubMed:22956541}. TISSUE SPECIFICITY: Expressed in tissues and cells in which the myoglobin gene is transcriptionally active including cardiac and skeletal myocytes, brain and kidney. In the adult brain, expressed in the piriform cortex and the indusium griseum. In the hippocampus, expression is localized to the dentate gyrus and CA3 area. In the cerebellum, expression is confined to the Purkinje cell layer. {ECO:0000269|PubMed:16376864, ECO:0000269|PubMed:8007964, ECO:0000269|PubMed:9271401}. +Q3UCQ1 FOXK2_MOUSE Forkhead box protein K2 (Cellular transcription factor ILF-1) (Interleukin enhancer-binding factor 1) 651 68,446 Alternative sequence (1); Chain (1); Cross-link (4); DNA binding (1); Domain (1); Metal binding (4); Modified residue (8); Region (4); Sequence conflict (1) FUNCTION: Transcriptional regulator that recognizes the core sequence 5'-TAAACA-3'. Binds to NFAT-like motifs (purine-rich) in the IL2 promoter. Positively regulates WNT/beta-catenin signaling by translocating DVL proteins into the nucleus. {ECO:0000250|UniProtKB:Q01167}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089, ECO:0000269|PubMed:16376864}. SUBUNIT: Interacts with DVL1, DVL2 (when phosphorylated) and DVL3; the interaction induces DVL2 nuclear translocation. Interacts with SUDS3. {ECO:0000250|UniProtKB:Q01167}. DOMAIN: The C-terminal part of the DNA-binding domain may contribute to DNA recognition specificity. {ECO:0000250|UniProtKB:Q01167}. TISSUE SPECIFICITY: Expressed in a wide range of adult brain regions, namely the piriform cortex, the major islands of Calleja and cells lining the lateral ventricles, the bed nucleus of stria terminalis, the paraventricular thalamic nucleus, habenula and all structures of the hippocampus. Also present in the hypothalamus, cerebral cortex and in the Purkinje cell layer in the cerebellum. Additionally expressed in dopamine neurons of the substantia and more sparsely in the ventral tegmental area. {ECO:0000269|PubMed:16376864}. +Q99JB6 FOXP3_MOUSE Forkhead box protein P3 (Scurfin) [Cleaved into: Forkhead box protein P3, C-terminally processed; Forkhead box protein P3 41 kDa form] 429 47,346 Chain (3); Cross-link (5); DNA binding (1); Helix (1); Modified residue (6); Motif (4); Mutagenesis (10); Propeptide (1); Region (4); Site (2); Turn (1); Zinc finger (1) FUNCTION: Transcriptional regulator which is crucial for the development and inhibitory function of regulatory T-cells (Treg). Plays an essential role in maintaining homeostasis of the immune system by allowing the acquisition of full suppressive function and stability of the Treg lineage, and by directly modulating the expansion and function of conventional T-cells. Can act either as a transcriptional repressor or a transcriptional activator depending on its interactions with other transcription factors, histone acetylases and deacetylases. The suppressive activity of Treg involves the coordinate activation of many genes, including CTLA4 and TNFRSF18 by FOXP3 along with repression of genes encoding cytokines such as interleukin-2 (IL2) and interferon-gamma (IFNG). Inhibits cytokine production and T-cell effector function by repressing the activity of two key transcription factors, RELA and NFATC2 (PubMed:15790681). Mediates transcriptional repression of IL2 via its association with histone acetylase KAT5 and histone deacetylase HDAC7 (By similarity). Can activate the expression of TNFRSF18, IL2RA and CTLA4 and repress the expression of IL2 and IFNG via its association with transcription factor RUNX1 (PubMed:17377532). Inhibits the differentiation of IL17 producing helper T-cells (Th17) by antagonizing RORC function, leading to down-regulation of IL17 expression, favoring Treg development (PubMed:18368049). Inhibits the transcriptional activator activity of RORA (By similarity). Can repress the expression of IL2 and IFNG via its association with transcription factor IKZF4 (PubMed:19696312). {ECO:0000250|UniProtKB:Q9BZS1, ECO:0000269|PubMed:15790681, ECO:0000269|PubMed:17377532, ECO:0000269|PubMed:18368049, ECO:0000269|PubMed:19696312}. PTM: Acetylation on lysine residues stabilizes FOXP3 and promotes differentiation of T-cells into induced regulatory T-cells (iTregs) associated with suppressive functions. Deacetylated by SIRT1. {ECO:0000269|PubMed:22312127}.; PTM: Polyubiquitinated, leading to its proteasomal degradation in regulatory T-cells (Treg) which is mediated by STUB1 in a HSPA1A/B-dependent manner. Deubiquitinated by USP7 leading to increase in protein stability. {ECO:0000269|PubMed:23973222, ECO:0000269|PubMed:23973223}.; PTM: Phosphorylation at Ser-418 regulates its transcriptional repressor activity and consequently, regulatory T-cells (Treg) suppressive function (By similarity). Phosphorylation by CDK2 negatively regulates its transcriptional activity and protein stability. {ECO:0000250|UniProtKB:Q9BZS1, ECO:0000269|PubMed:23853094}.; PTM: Undergoes proteolytic cleavage in activated regulatory T-cells (Treg), and can be cleaved at either the N- or C-terminal site, or at both sites. Treg expressing the form cleaved at C-terminal site or both N- and C-terminal sites exhibit an increased induction of IL10 and an increased capacity to suppress proliferation of conventional T-cells in vitro. Treg expressing the form cleaved at only the C-terminal site are highly effective at preventing experimental colitis in an in vivo model of inflammatory bowel disease. {ECO:0000269|PubMed:19117830}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089, ECO:0000269|PubMed:17377532, ECO:0000269|PubMed:18368049}. Cytoplasm {ECO:0000250|UniProtKB:Q9BZS1}. Note=Predominantly expressed in the cytoplasm in activated conventional T-cells whereas predominantly expressed in the nucleus in regulatory T-cells (Treg) (By similarity). The 41 kDa form derived by proteolytic processing is found exclusively in the chromatin fraction of activated Treg cells. {ECO:0000250|UniProtKB:Q9BZS1, ECO:0000269|PubMed:19117830}. SUBUNIT: Homodimer. Dimerization is essential for its transcriptional regulator activity. Interacts with IKZF3 (By similarity). Interacts (via LXXLL motif) with isoform 4 of RORA (via AF-2 motif) (By similarity). Interacts with STUB1 and HSPA1A/B. Interacts with IKZF4, HDAC7 and KAT5. Interacts with RUNX1, RUNX2, RUNX3 and NFATC2. Interacts with RORC. Interacts with HDAC9 in the absence of T-cell stimulation (By similarity). Interacts with RELA, PPP1CA, PPP1CB, PPP1CG, HSPA8 and USP7 (By similarity). {ECO:0000250|UniProtKB:Q9BZS1, ECO:0000269|PubMed:16769892, ECO:0000269|PubMed:17377532, ECO:0000269|PubMed:18368049, ECO:0000269|PubMed:19696312, ECO:0000269|PubMed:23973223}. DOMAIN: The fork-head DNA-binding domain is essential for its dimerization and interaction with NFATC2. {ECO:0000250|UniProtKB:Q9BZS1}. TISSUE SPECIFICITY: High level of expression in thymus and spleen. DISEASE: Note=Defects in Foxp3 are the cause of the scurfy phenotype (sf). It results in a lethal disorder of immunoregulation, characterized by infections, diarrhea, anemia, thrombocytopenia, hypogonadism, gastrointestinal bleeding, lymphadenopathy and leukocytosis. +Q3UTB7 FOXR1_MOUSE Forkhead box protein R1 (Forkhead box protein N5) 268 30,579 Alternative sequence (2); Chain (1); DNA binding (1) SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +A2AD83 FRMD7_MOUSE FERM domain-containing protein 7 703 80,330 Chain (1); Coiled coil (1); Domain (1); Erroneous initiation (3) FUNCTION: Plays a role in neurite development, may be through the activation of the GTPase RAC1. Plays a role in the control of eye movement and gaze stability. {ECO:0000250|UniProtKB:Q6ZUT3, ECO:0000269|PubMed:19892780}. SUBCELLULAR LOCATION: Cell projection {ECO:0000269|PubMed:19892780}. Cell projection, growth cone {ECO:0000269|PubMed:19892780}. Note=In undifferentiated neurons, located in the actin-rich regions of the cell body. In differentiated neurons, located in the actin-rich regions of the cell body and primary neurite processes but is almost absent from secondary extensions arising from the primary neurite. Also found at the actin-rich distal end of growth cones. {ECO:0000269|PubMed:19892780}. TISSUE SPECIFICITY: In the developing cerebral cortex, strong expression is observed in the ventricular and intermediate zones at E13 and E17. At E17 and P0, expression appears to be restricted to the cortical plate. In neonates, highly expressed in cortex, hippocampus, cerebellum, olfactory bulb and eye with little or no expression in liver, kidney, skeletal muscle or heart muscle (at protein level). {ECO:0000269|PubMed:19892780}. +P09528 FRIH_MOUSE Ferritin heavy chain (Ferritin H subunit) (EC 1.16.3.1) [Cleaved into: Ferritin heavy chain, N-terminally processed] 182 21,067 Chain (2); Domain (1); Helix (6); Initiator methionine (1); Metal binding (6); Modified residue (2); Sequence conflict (4); Turn (2) FUNCTION: Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney. {ECO:0000269|PubMed:19154717}. SUBUNIT: Oligomer of 24 subunits. There are two types of subunits: L (light) chain and H (heavy) chain. The major chain can be light or heavy, depending on the species and tissue type. The functional molecule forms a roughly spherical shell with a diameter of 12 nm and contains a central cavity into which the insoluble mineral iron core is deposited. +Q9EQC7 FSTL3_MOUSE Follistatin-related protein 3 (Follistatin-like protein 3) (Follistatin-related gene protein) 256 27,271 Chain (1); Disulfide bond (11); Domain (5); Glycosylation (2); Signal peptide (1) FUNCTION: The secreted form is a binding and antagonizing protein for members of the TGF-beta family, such us activin, BMP2 and MSTN. Inhibits activin A-, activin B-, BMP2- and MSDT-induced cellular signaling; more effective on activin A than on activin B. Involved in bone formation; inhibits osteoclast differentiation. Involved in hematopoiesis; involved in differentiation of hemopoietic progenitor cells, increases hematopoietic cell adhesion to fibronectin and seems to contribute to the adhesion of hematopoietic precursor cells to the bone marrow stroma. The nuclear form is probably involved in transcriptional regulation via interaction with MLLT10 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Interacts with INHBA and INHBB. Interacts with FN1. Interacts with ADAM12. Interacts with MLLT10; the interaction enhances MLLT10 in vitro transcriptional activity and self-association. Interacts with MSTN (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Abundantly expressed in heart, lung, kidney and testis. Continuously expressed in embryonic heart. {ECO:0000269|PubMed:17878677}. +Q91XD4 FTCD_MOUSE Formimidoyltransferase-cyclodeaminase (Formiminotransferase-cyclodeaminase) (FTCD) [Includes: Glutamate formimidoyltransferase (EC 2.1.2.5) (Glutamate formiminotransferase) (Glutamate formyltransferase); Formimidoyltetrahydrofolate cyclodeaminase (EC 4.3.1.4) (Formiminotetrahydrofolate cyclodeaminase)] 541 58,939 Active site (2); Chain (1); Modified residue (1); Region (5) Amino-acid degradation; L-histidine degradation into L-glutamate; L-glutamate from N-formimidoyl-L-glutamate (transferase route): step 1/1. One-carbon metabolism; tetrahydrofolate interconversion. FUNCTION: Folate-dependent enzyme, that displays both transferase and deaminase activity. Serves to channel one-carbon units from formiminoglutamate to the folate pool (By similarity). {ECO:0000250}.; FUNCTION: Binds and promotes bundling of vimentin filaments originating from the Golgi. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250}. Golgi apparatus {ECO:0000250}. Note=More abundantly located around the mother centriole. {ECO:0000250}. SUBUNIT: Homooctamer, including four polyglutamate binding sites. The subunits are arranged as a tetramer of dimers, and form a planar ring-shaped structure (By similarity). {ECO:0000250}. +Q9QXC1 FETUB_MOUSE Fetuin-B (Fetuin-like protein IRL685) 388 42,713 Chain (1); Disulfide bond (5); Domain (2); Glycosylation (4); Modified residue (1); Signal peptide (1) FUNCTION: Protease inhibitor required for egg fertilization. Required to prevent premature zona pellucida hardening before fertilization, probably by inhibiting the protease activity of ASTL, a protease that mediates the cleavage of ZP2 and triggers zona pellucida hardening. {ECO:0000269|PubMed:23562279}. SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:23562279}. TISSUE SPECIFICITY: Liver, lung and tongue. +Q3UFD7 FFAR3_MOUSE Free fatty acid receptor 3 (G-protein coupled receptor 41) 319 36,501 Chain (1); Compositional bias (1); Disulfide bond (1); Glycosylation (2); Mutagenesis (1); Topological domain (8); Transmembrane (7) TRANSMEM 16 36 Helical; Name=1. {ECO:0000255}.; TRANSMEM 44 64 Helical; Name=2. {ECO:0000255}.; TRANSMEM 99 119 Helical; Name=3. {ECO:0000255}.; TRANSMEM 128 148 Helical; Name=4. {ECO:0000255}.; TRANSMEM 184 206 Helical; Name=5. {ECO:0000255}.; TRANSMEM 219 239 Helical; Name=6. {ECO:0000255}.; TRANSMEM 255 275 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 15 Extracellular. {ECO:0000255}.; TOPO_DOM 37 43 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 65 98 Extracellular. {ECO:0000255}.; TOPO_DOM 120 127 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 149 183 Extracellular. {ECO:0000255}.; TOPO_DOM 207 218 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 240 254 Extracellular. {ECO:0000255}.; TOPO_DOM 276 319 Cytoplasmic. {ECO:0000255}. FUNCTION: G protein-coupled receptor that is activated by a major product of dietary fiber digestion, the short chain fatty acids (SCFAs), and that plays a role in the regulation of whole-body energy homeostasis and in intestinal immunity. In omnivorous mammals, the short chain fatty acids acetate, propionate and butyrate are produced primarily by the gut microbiome that metabolizes dietary fibers. SCFAs serve as a source of energy but also act as signaling molecules. That G protein-coupled receptor is probably coupled to the pertussis toxin-sensitive, G(i/o)-alpha family of G proteins. Its activation results in the formation of inositol 1,4,5-trisphosphate, the mobilization of intracellular calcium, the phosphorylation of the MAPK3/ERK1 and MAPK1/ERK2 kinases and the inhibition of intracellular cAMP accumulation. Activated by SCFAs and by beta-hydroxybutyrate, a ketone body produced by the liver upon starvation, it inhibits N-type calcium channels and modulates the activity of sympathetic neurons through a signaling cascade involving the beta and gamma subunits of its coupled G protein, phospholipase C and MAP kinases. Thereby, it may regulate energy expenditure through the control of the sympathetic nervous system that controls for instance heart rate (PubMed:21518883, PubMed:22673524). Upon activation by SCFAs accumulating in the intestine, it may also signal to the brain via neural circuits which in turn would regulate intestinal gluconeogenesis. May also control the production of hormones involved in whole-body energy homeostasis. May for instance, regulate blood pressure through renin secretion (PubMed:23401498). May also regulate secretion of the PYY peptide by enteroendocrine cells and control gut motility, intestinal transit rate, and the harvesting of energy from SCFAs produced by gut microbiota (PubMed:18931303). May also indirectly regulate the production of LEP/Leptin, a hormone acting on the CNS to inhibit food intake, in response to the presence of short-chain fatty acids in the intestine (PubMed:14722361, PubMed:20399779). Finally, may also play a role in glucose homeostasis (PubMed:22190648, PubMed:24748202). Besides its role in energy homeostasis, may play a role in intestinal immunity. May mediate the activation of the inflammatory and immune response by SCFAs in the gut, regulating the rapid production of chemokines and cytokines by intestinal epithelial cells (PubMed:23665276). Exhibits an SCFA-independent constitutive G protein-coupled receptor activity (PubMed:23066016). {ECO:0000269|PubMed:14722361, ECO:0000269|PubMed:18931303, ECO:0000269|PubMed:20399779, ECO:0000269|PubMed:21518883, ECO:0000269|PubMed:22190648, ECO:0000269|PubMed:22673524, ECO:0000269|PubMed:23066016, ECO:0000269|PubMed:23401498, ECO:0000269|PubMed:23665276, ECO:0000269|PubMed:24748202}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed in white adipose tissue and skeletal muscle (at protein level). Abundantly expressed in sympathetic ganglia such as the superior cervical ganglion. Also expressed by intestinal endocrine cells. {ECO:0000269|PubMed:14722361, ECO:0000269|PubMed:18931303, ECO:0000269|PubMed:21518883, ECO:0000269|PubMed:22190648, ECO:0000269|PubMed:24748202}. +Q9ESS2 FGF22_MOUSE Fibroblast growth factor 22 (FGF-22) 162 18,927 Chain (1); Signal peptide (1) FUNCTION: Plays a role in the fasting response, glucose homeostasis, lipolysis and lipogenesis. Can stimulate cell proliferation (in vitro). May be involved in hair development. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. SUBUNIT: Interacts with FGFR1 and FGFR2. Interacts with FGFBP1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Preferentially expressed in skin; low expression in brain. Expressed in the inner root sheath of the hair follicle. +Q91V87 FGRL1_MOUSE Fibroblast growth factor receptor-like 1 (FGF receptor-like protein 1) (Fibroblast growth factor receptor 5) (FGFR-5) 529 57,013 Alternative sequence (1); Chain (1); Disulfide bond (3); Domain (3); Glycosylation (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 375 395 Helical. {ECO:0000255}. TOPO_DOM 21 374 Extracellular. {ECO:0000255}.; TOPO_DOM 396 529 Cytoplasmic. {ECO:0000255}. FUNCTION: Has a negative effect on cell proliferation. {ECO:0000250, ECO:0000269|PubMed:12813049}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. SUBUNIT: Interacts with FGF2 with a low affinity. {ECO:0000269|PubMed:11418238}. TISSUE SPECIFICITY: Highly expressed in the kidney, brain and lung. Weakly expressed in the muscle, thymus, lymph node, stomach, intestine, colon and liver. Expressed in fetal cartilaginous structures like the nasal cartilage, the ribs and the sternum as well as in the cartilaginous rudiments of developing bones such as the vertebrae and the pelvic bone. High expression is found in the muscles of the tongue and the diaphragm. {ECO:0000269|PubMed:11418238, ECO:0000269|PubMed:12813049}. +Q4U2R1 HERC2_MOUSE E3 ubiquitin-protein ligase HERC2 (EC 2.3.2.26) (HECT domain and RCC1-like domain-containing protein 2) (HECT-type E3 ubiquitin transferase HERC2) 4836 527,456 Active site (1); Alternative sequence (1); Chain (1); Coiled coil (1); Domain (4); Modified residue (11); Repeat (21); Sequence conflict (26); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that regulates ubiquitin-dependent retention of repair proteins on damaged chromosomes. Recruited to sites of DNA damage in response to ionizing radiation (IR) and facilitates the assembly of UBE2N and RNF8 promoting DNA damage-induced formation of 'Lys-63'-linked ubiquitin chains. Acts as a mediator of binding specificity between UBE2N and RNF8. Involved in the maintenance of RNF168 levels. E3 ubiquitin-protein ligase that promotes the ubiquitination and proteasomal degradation of XPA which influences the circadian oscillation of DNA excision repair activity. By controlling the steady-state expression of the IGF1R receptor, indirectly regulates the insulin-like growth factor receptor signaling pathway. {ECO:0000250|UniProtKB:O95714}. PTM: Phosphorylation at Thr-4829 is required for interaction with RNF8.; PTM: Sumoylated with SUMO1 by PIAS4 in response to double-strand breaks (DSBs), promoting the interaction with RNF8. {ECO:0000250|UniProtKB:O95714}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O95714}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:O95714}. Nucleus {ECO:0000250|UniProtKB:O95714}. Note=Recruited to sites of DNA damage in response to ionising radiation (IR) via its interaction with RNF8. May loose association with centrosomes during mitosis. {ECO:0000250|UniProtKB:O95714}. SUBUNIT: Interacts (when phosphorylated at Thr-4829 and sumoylated) with RNF8 (via FHA domain); this interaction increases after ionising radiation (IR) treatment. Interacts with XPA. Interacts with NEURL4. Via its interaction with NEURL4, may indirectly interact with CCP110 and CEP97. {ECO:0000250|UniProtKB:O95714}. DOMAIN: The ZZ-type zinc finger mediates binding to SUMO1, and at low level SUMO2. {ECO:0000250|UniProtKB:O95714}.; DOMAIN: The RCC1 repeats are grouped into three seven-bladed beta-propeller regions. {ECO:0000250|UniProtKB:O95714}. TISSUE SPECIFICITY: Highest levels are found in brain and testis with lower levels in heart, lung, liver, skeletal muscle and kidney. Little expression detected in spleen. {ECO:0000269|PubMed:9689098}. DISEASE: Note=Defects in Herc2 are the cause of the runty, jerky, sterile phenotype (rjs), also known as the juvenile development and fertility phenotype (jfd2), which is characterized by reduced size, jerky gait, fertility problems including spermatocyte and oocyte abnormalities, defective maternal behavior and reduced lifespan with juvenile lethality. {ECO:0000269|PubMed:10441737, ECO:0000269|PubMed:9689098, ECO:0000269|PubMed:9949213}. +F2Z461 HERC6_MOUSE E3 ISG15--protein ligase Herc6 (EC 2.3.2.-) 1003 112,928 Active site (1); Chain (1); Domain (1); Repeat (5); Sequence conflict (1) FUNCTION: Major E3 ligase for ISG15 conjugation. Acts as a positive regulator of innate antiviral response in cells induced by interferon. {ECO:0000269|PubMed:22272257}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:22272257}. Note=Exclusively cytoplasmic. +Q9JJK5 HERP1_MOUSE Homocysteine-responsive endoplasmic reticulum-resident ubiquitin-like domain member 1 protein 391 43,907 Chain (1); Domain (1); Modified residue (2); Region (1); Topological domain (3); Transmembrane (2) TRANSMEM 264 284 Helical. {ECO:0000255}.; TRANSMEM 290 310 Helical. {ECO:0000255}. TOPO_DOM 1 263 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 285 289 Lumenal. {ECO:0000255}.; TOPO_DOM 311 391 Cytoplasmic. {ECO:0000255}. FUNCTION: Component of the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. Binds to ubiquilins and this interaction is required for efficient degradation of CD3D via the ERAD pathway. {ECO:0000250|UniProtKB:Q15011}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with PSEN1 and PSEN2. Interacts with SYVN1 and UBXN6. Interacts with UBQLN1, UBQLN2 and UBQLN4. {ECO:0000250|UniProtKB:Q15011}. +Q61851 FGFR3_MOUSE Fibroblast growth factor receptor 3 (FGFR-3) (EC 2.7.10.1) (Heparin-binding growth factor receptor) (CD antigen CD333) 801 87,758 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Disulfide bond (3); Domain (4); Glycosylation (6); Modified residue (6); Mutagenesis (1); Nucleotide binding (1); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 370 390 Helical. {ECO:0000255}. TOPO_DOM 21 369 Extracellular. {ECO:0000255}.; TOPO_DOM 391 801 Cytoplasmic. {ECO:0000255}. FUNCTION: Tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of cell proliferation, differentiation and apoptosis. Plays an essential role in the regulation of chondrocyte differentiation, proliferation and apoptosis, and is required for normal skeleton development. Regulates both osteogenesis and postnatal bone mineralization by osteoblasts. Promotes apoptosis in chondrocytes, but can also promote cancer cell proliferation. Required for normal development of the inner ear. Phosphorylates PLCG1, CBL and FRS2. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Plays a role in the regulation of vitamin D metabolism. Mutations that lead to constitutive kinase activation or impair normal FGFR3 maturation, internalization and degradation lead to aberrant signaling. Over-expressed or constitutively activated FGFR3 promotes activation of STAT1, STAT5A and STAT5B. Plays a role in postnatal lung development. {ECO:0000269|PubMed:14699054, ECO:0000269|PubMed:21561999, ECO:0000269|PubMed:8601314, ECO:0000269|PubMed:8630492, ECO:0000269|PubMed:8663044, ECO:0000269|PubMed:9716527}. PTM: Autophosphorylated. Binding of FGF family members together with heparan sulfate proteoglycan or heparin promotes receptor dimerization and autophosphorylation on tyrosine residues. Autophosphorylation occurs in trans between the two FGFR molecules present in the dimer. Phosphorylation at Tyr-719 is essential for stimulation of cell proliferation and activation of PIK3R1, STAT1 and MAP kinase signaling. Phosphorylation at Tyr-755 is required for interaction with PIK3R1 and PLCG1 (By similarity). {ECO:0000250}.; PTM: Ubiquitinated. Is rapidly ubiquitinated after ligand binding and autophosphorylation, leading to receptor internalization and degradation. Subject to both proteasomal and lysosomal degradation (By similarity). {ECO:0000250}.; PTM: N-glycosylated in the endoplasmic reticulum. The N-glycan chains undergo further maturation to an Endo H-resistant form in the Golgi apparatus (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Cytoplasmic vesicle {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Note=The activated receptor is rapidly internalized and degraded. Detected in intracellular vesicles after internalization of the autophosphorylated receptor (By similarity). {ECO:0000250}. SUBUNIT: Monomer. Homodimer after ligand binding. Interacts with FGF1, FGF2, FGF4, FGF6; FGF8, FGF9, FGF10, FGF17, FGF18, FGF19, FGF20 and FGF23 (in vitro). Interacts with KLB. Affinity for fibroblast growth factors (FGFs) is increased by heparan sulfate glycosaminoglycans that function as coreceptors. Likewise, KLB increases the affinity for FGF19 and FGF21. Interacts with PIK3R1, PLCG1, SOCS1 and SOCS3 (By similarity). {ECO:0000250}. DOMAIN: The second and third Ig-like domains directly interact with fibroblast growth factors (FGF) and heparan sulfate proteoglycans. {ECO:0000250}. TISSUE SPECIFICITY: In embryo, expressed in heart, lung, kidney, skin, head and liver but not in muscle. In adult, highest levels in brain. Also expressed in liver, lung, kidney, testis, ovary and uterus. Very low levels in heart, thymus, spleen and muscle. +Q6RKD8 FLRT1_MOUSE Leucine-rich repeat transmembrane protein FLRT1 (Fibronectin leucine rich transmembrane protein 1) 674 74,151 Chain (1); Disulfide bond (3); Domain (3); Glycosylation (1); Modified residue (3); Mutagenesis (3); Repeat (10); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 553 573 Helical. {ECO:0000255}. TOPO_DOM 21 552 Extracellular. {ECO:0000305}.; TOPO_DOM 574 674 Cytoplasmic. {ECO:0000305}. FUNCTION: Plays a role in fibroblast growth factor-mediated signaling cascades that lead to the activation of MAP kinases (PubMed:16872596, PubMed:20421966). Promotes neurite outgrowth via FGFR1-mediated activation of downstream MAP kinases. Promotes an increase both in neurite number and in neurite length (PubMed:20421966). May play a role in cell-cell adhesion and cell guidance via its interaction with ADGRL1/LPHN1 and ADGRL3 (PubMed:22405201). {ECO:0000269|PubMed:16872596, ECO:0000269|PubMed:20421966, ECO:0000305|PubMed:22405201}. PTM: Phosphorylated in response to FGFR1 signaling, but is not a direct substrate of FGFR1 or SRC. A mutant where the Tyr phosphorylation sites have been replaced by Phe displays constitutive FGFR1-dependent activation of downstream MAP kinases. {ECO:0000269|PubMed:20421966}.; PTM: N-glycosylated. {ECO:0000269|PubMed:16872596, ECO:0000269|PubMed:21673655}.; PTM: Proteolytic cleavage in the juxtamembrane region gives rise to a soluble ectodomain. {ECO:0000269|PubMed:21673655}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16872596, ECO:0000269|PubMed:20421966, ECO:0000269|PubMed:22405201}; Single-pass membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000305|PubMed:16872596, ECO:0000305|PubMed:20421966}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:16872596, ECO:0000269|PubMed:20421966}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16872596, ECO:0000269|PubMed:20421966}. Cell junction, focal adhesion {ECO:0000269|PubMed:16872596}. Secreted {ECO:0000269|PubMed:21673655}. Cell projection {ECO:0000269|PubMed:20421966}. Cell junction {ECO:0000269|PubMed:20421966}. Note=In addition to its location at the cell membrane, colocalizes with FGFR1 in punctate perinuclear cytoplasmic vesicles (PubMed:16872596, PubMed:20421966). Detected along neurites and at contacts between neurite termini and other cells (PubMed:20421966). Proteolytic cleavage gives rise to a shedded ectodomain (PubMed:21673655). {ECO:0000269|PubMed:16872596, ECO:0000269|PubMed:20421966, ECO:0000269|PubMed:21673655}. SUBUNIT: Interacts with FGFR1 (PubMed:16872596). Interacts (via extracellular domain) with ADGRL1/LPHN1 and ADGRL3 (via olfactomedin-like domain) (PubMed:22405201). {ECO:0000269|PubMed:16872596, ECO:0000269|PubMed:22405201}. TISSUE SPECIFICITY: Detected in brain (at protein level). {ECO:0000269|PubMed:21673655}. +Q8BGT1 FLRT3_MOUSE Leucine-rich repeat transmembrane protein FLRT3 (Fibronectin leucine rich transmembrane protein 3) 649 72,879 Beta strand (22); Chain (1); Disulfide bond (3); Domain (3); Erroneous initiation (1); Glycosylation (1); Helix (4); Mutagenesis (4); Region (1); Repeat (10); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (7) TRANSMEM 529 549 Helical. {ECO:0000255}. TOPO_DOM 29 528 Extracellular. {ECO:0000305}.; TOPO_DOM 550 649 Cytoplasmic. {ECO:0000305}. FUNCTION: Functions in cell-cell adhesion, cell migration and axon guidance, exerting an attractive or repulsive role depending on its interaction partners (PubMed:19056886, PubMed:25374360). Plays a role in the spatial organization of brain neurons (PubMed:25374360). Plays a role in vascular development in the retina (PubMed:25374360). Plays a role in cell-cell adhesion via its interaction with ADGRL3 and probably also other latrophilins that are expressed at the surface of adjacent cells (PubMed:22405201, PubMed:25374360). Interaction with the intracellular domain of ROBO1 mediates axon attraction towards cells expressing NTN1 (PubMed:24560577). Mediates axon growth cone collapse and plays a repulsive role in neuron guidance via its interaction with UNC5B, and possibly also other UNC-5 family members (PubMed:21673655, PubMed:25374360). Promotes neurite outgrowth (in vitro) (By similarity). Mediates cell-cell contacts that promote an increase both in neurite number and in neurite length (By similarity). Plays a role in the regulation of the density of glutamaergic synapses (PubMed:22405201). Plays a role in fibroblast growth factor-mediated signaling cascades (PubMed:16872596). Required for normal morphogenesis during embryonic development, but not for normal embryonic patterning (PubMed:19056886). Required for normal ventral closure, headfold fusion and definitive endoderm migration during embryonic development (PubMed:18448090). Required for the formation of a normal basement membrane and the maintenance of a normal anterior visceral endoderm during embryonic development (PubMed:19056886). {ECO:0000250|UniProtKB:B1H234, ECO:0000269|PubMed:16872596, ECO:0000269|PubMed:18448090, ECO:0000269|PubMed:19056886, ECO:0000269|PubMed:21673655, ECO:0000269|PubMed:22405201, ECO:0000269|PubMed:24560577, ECO:0000269|PubMed:25374360}. PTM: N-glycosylated. {ECO:0000269|PubMed:16872596, ECO:0000269|PubMed:21673655}.; PTM: Proteolytic cleavage in the juxtamembrane region gives rise to a soluble ectodomain. Cleavage is probably effected by a metalloprotease. {ECO:0000269|PubMed:21673655}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16872596, ECO:0000269|PubMed:21673655, ECO:0000269|PubMed:22405201, ECO:0000269|PubMed:24560577, ECO:0000269|PubMed:25374360}; Single-pass membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000305|PubMed:16872596}. Cell junction, focal adhesion {ECO:0000269|PubMed:16872596}. Secreted {ECO:0000269|PubMed:21673655}. Cell projection, axon {ECO:0000269|PubMed:24560577}. Note=Detected at neuronal growth cones (PubMed:24560577). Detected on dendritic punctae that colocalize in part with glutamaergic synapses, but not with GABAergic synapses. Detected on axons and at axon termini (By similarity). Proteolytic cleavage in the juxtamembrane region gives rise to a shedded ectodomain (PubMed:21673655). {ECO:0000250|UniProtKB:B1H234, ECO:0000269|PubMed:21673655, ECO:0000269|PubMed:24560577}. SUBUNIT: Monomer and homodimer (By similarity). Self-associates (via leucine-rich repeats), giving rise to homooligomers (PubMed:25374360). Interacts with FGFR1 (PubMed:16872596). Interacts (via extracellular domain) with ADGRL1/LPHN1 and LPHN2 (via olfactomedin-like domain) (PubMed:22405201). Interacts (via extracellular domain) with ADGRL3 (via olfactomedin-like domain) (PubMed:24739570, PubMed:22405201, PubMed:26235031). Interacts (via extracellular domain) with UNC5B (via Ig domain) (PubMed:19492039, PubMed:21673655, PubMed:22405201, PubMed:25374360). May also interact (via extracellular domain) with UNC5A and UNC5C (PubMed:22405201). Interacts (via extracellular domain) with UNC5D (via extracellular domain) (PubMed:19492039). Identified in complexes composed of FLRT3, ADGRL3 and UNC5B, respectively FLRT3, ADGRL3 and UNC5D (By similarity). Interacts (via cytoplasmic domain) with ROBO1 (PubMed:24560577). {ECO:0000250|UniProtKB:Q9NZU0, ECO:0000269|PubMed:16872596, ECO:0000269|PubMed:21673655, ECO:0000269|PubMed:22405201, ECO:0000269|PubMed:24560577, ECO:0000269|PubMed:24739570, ECO:0000269|PubMed:25374360, ECO:0000269|PubMed:26235031}. TISSUE SPECIFICITY: Detected in adult brain (PubMed:21350012). Detected in embryonic rostral thalamus neurons (at protein level) (PubMed:24560577). Detected in embryonic rostral thalamus neurons (PubMed:24560577). Detected in neonate eye, in the inner plexiform layer and the outer nuclear layer (PubMed:25374360). {ECO:0000269|PubMed:21350012, ECO:0000269|PubMed:24560577}. +Q61239 FNTA_MOUSE Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha (EC 2.5.1.58) (EC 2.5.1.59) (CAAX farnesyltransferase subunit alpha) (FTase-alpha) (Ras proteins prenyltransferase subunit alpha) (Type I protein geranyl-geranyltransferase subunit alpha) (GGTase-I-alpha) 377 44,013 Chain (1); Compositional bias (1); Initiator methionine (1); Modified residue (1); Repeat (5); Sequence conflict (1) FUNCTION: Essential subunit of both the farnesyltransferase and the geranylgeranyltransferase complex. Contributes to the transfer of a farnesyl or geranylgeranyl moiety from farnesyl or geranylgeranyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. May positively regulate neuromuscular junction development downstream of MUSK via its function in RAC1 prenylation and activation. {ECO:0000269|PubMed:14622576}. PTM: Phosphorylated. Phosphorylation is mediated by MUSK upon AGRIN stimulation and results in the activation of FNTA. {ECO:0000269|PubMed:14622576}. SUBUNIT: Heterodimer of FNTA and FNTB (farnesyltransferase). Heterodimer of FNTA and PGGT1B (geranylgeranyltransferase). Interacts with MUSK; the interaction is direct and mediates AGRIN-induced phosphorylation of FNTA. {ECO:0000269|PubMed:14622576}. +A2A9Q0 FND10_MOUSE Fibronectin type III domain-containing protein 10 223 24,417 Chain (1); Domain (1); Frameshift (1); Glycosylation (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 180 200 Helical. {ECO:0000255}. TOPO_DOM 20 179 Extracellular. {ECO:0000255}.; TOPO_DOM 201 223 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +O35615 FOG1_MOUSE Zinc finger protein ZFPM1 (Friend of GATA protein 1) (FOG-1) (Friend of GATA 1) (Zinc finger protein multitype 1) 995 105,984 Beta strand (7); Chain (1); Helix (3); Modified residue (12); Mutagenesis (45); Region (2); Turn (1); Zinc finger (9) FUNCTION: Transcription regulator that plays an essential role in erythroid and megakaryocytic cell differentiation. Essential cofactor that acts via the formation of a heterodimer with transcription factors of the GATA family GATA1, GATA2 and GATA3. Such heterodimer can both activate or repress transcriptional activity, depending on the cell and promoter context. The heterodimer formed with GATA proteins is essential to activate expression of genes such as NFE2, ITGA2B, alpha- and beta-globin, while it represses expression of KLF1. May be involved in regulation of some genes in gonads. May also be involved in cardiac development, in a non-redundant way with ZFPM2/FOG2. {ECO:0000269|PubMed:10078204, ECO:0000269|PubMed:10329627, ECO:0000269|PubMed:11940669, ECO:0000269|PubMed:12356738, ECO:0000269|PubMed:14614148, ECO:0000269|PubMed:9230307, ECO:0000269|PubMed:9553047}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9230307}. SUBUNIT: Interacts with the N-terminal zinc-finger of GATA1, GATA2 and GATA3. Interacts with corepressor CTBP2; this interaction is however not essential for corepressor activity in erythropoiesis. Interacts with TACC3. {ECO:0000269|PubMed:10329627, ECO:0000269|PubMed:11940669, ECO:0000269|PubMed:15234987, ECO:0000269|PubMed:9230307, ECO:0000269|PubMed:9837943}. DOMAIN: The CCHC FOG-type zinc fingers 1, 2, 3 and 5 bind directly to GATA-type zinc fingers. The Tyr residue adjacent to the last Cys of the CCHC FOG-type zinc finger is essential for the interaction with GATA-type zinc fingers. TISSUE SPECIFICITY: Mainly expressed in hematopoietic tissues. Expressed in the spleen, a primary site of hematopoiesis in the adult mouse, as well as in the liver and testis, but not in the heart, brain, lung, kidney, or skeletal muscle. Among hematopoietic cell lines, it is strongly expressed in erythroid and megakaryocytic cell lines. Expressed at low level in several lymphoid and early myeloid cell lines. Not expressed in mast cell and macrophage lines. Expressed in the heart, where it colocalizes with GATA4, GATA5 and GATA6. {ECO:0000269|PubMed:14614148, ECO:0000269|PubMed:9230307}. +P48760 FOLC_MOUSE Folylpolyglutamate synthase, mitochondrial (EC 6.3.2.17) (Folylpoly-gamma-glutamate synthetase) (FPGS) (Tetrahydrofolylpolyglutamate synthase) (Tetrahydrofolate synthase) 587 64,955 Alternative sequence (4); Binding site (2); Chain (1); Erroneous initiation (1); Metal binding (3); Modified residue (1); Nucleotide binding (1); Sequence conflict (13); Transit peptide (1) Cofactor biosynthesis; tetrahydrofolylpolyglutamate biosynthesis. FUNCTION: Catalyzes conversion of folates to polyglutamate derivatives allowing concentration of folate compounds in the cell and the intracellular retention of these cofactors, which are important substrates for most of the folate-dependent enzymes that are involved in one-carbon transfer reactions involved in purine, pyrimidine and amino acid synthesis. Dihydrofolate, tetrahydrofolate, 5,10-methylenetetrahydrofolate, 10-formyltetrahydrofolate and 5-formyltetrahydrofolate are the best substrates. Folic acid and 5-methyltetrahydrofolate can also act as substrates. {ECO:0000269|PubMed:11772020, ECO:0000269|PubMed:6548641}. SUBCELLULAR LOCATION: Isoform 1: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q05932}. Mitochondrion matrix {ECO:0000250|UniProtKB:Q05932}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm {ECO:0000250|UniProtKB:Q05932}. SUBUNIT: Monomer. {ECO:0000250}. TISSUE SPECIFICITY: With non-specific probe, highest content in kidney and liver and lowest in spleen, lung and small intestine, and readily detectable in all of the tumors except hepatoma. Isoform 1 and isoform 2 expressed in leukemic cells and isoform 4 and isoform 5 in liver cells. Isoform 1 and isoform 2 exclusively expressed in hepatoma and Lewis lung carcinoma. Isoform 1 and isoform 2 also expressed in bone marrow, small intestine and spleen. Kidney expresses isoform 1, isoform 2, isoform 4 and isoform 5. {ECO:0000269|PubMed:10626793, ECO:0000269|PubMed:17998333, ECO:0000269|PubMed:9038166}. +Q9QY14 FOXE3_MOUSE Forkhead box protein E3 288 30,541 Chain (1); Compositional bias (1); DNA binding (1); Natural variant (2) FUNCTION: Transcription factor that controls lens epithelial cell growth through regulation of proliferation, apoptosis and cell cycle (PubMed:10652278, PubMed:10890982). During lens development, controls the ratio of the lens fiber cells to the cells of the anterior lens epithelium by regulating the rate of proliferation and differentiation (PubMed:16199865). Controls lens vesicle closure and subsequent separation of the lens vesicle from ectoderm (PubMed:10652278). Is required for morphogenesis and differentiation of the anterior segment of the eye (PubMed:17064680). Controls the expression of DNAJB1 in a pathway that is crucial for the development of the anterior segment of the eye (By similarity). {ECO:0000250|UniProtKB:Q13461, ECO:0000269|PubMed:10652278, ECO:0000269|PubMed:10890982, ECO:0000269|PubMed:16199865, ECO:0000269|PubMed:17064680}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17064680}. TISSUE SPECIFICITY: Expressed in the embryonic lens. {ECO:0000269|PubMed:10652278, ECO:0000269|PubMed:10890982, ECO:0000269|PubMed:27218149}. DISEASE: Note=Defects in Foxe3 are the cause of the dysgenetic lens (dyl) phenotype. In mouse mutant dyl the lens vesicle fails to separate from the ectoderm, causing a fusion between the lens and the cornea. Lack of a proliferating anterior lens epithelium leads to absence of secondary lens fibers and a dysplastic, cataractous lens. {ECO:0000269|PubMed:10652278, ECO:0000269|PubMed:10890982}. +Q91W97 HKDC1_MOUSE Putative hexokinase HKDC1 (EC 2.7.1.1) (Hexokinase domain-containing protein 1) 915 102,259 Binding site (1); Chain (1); Domain (2); Nucleotide binding (2); Region (6); Sequence conflict (2) Carbohydrate metabolism; hexose metabolism. +O35943 FRDA_MOUSE Frataxin, mitochondrial (Fxn) (EC 1.16.3.1) [Cleaved into: Frataxin intermediate form; Frataxin mature form] 207 22,924 Chain (2); Transit peptide (1) FUNCTION: Promotes the biosynthesis of heme and assembly and repair of iron-sulfur clusters by delivering Fe(2+) to proteins involved in these pathways. May play a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+); the oligomeric form but not the monomeric form has in vitro ferroxidase activity. May be able to store large amounts of iron in the form of a ferrihydrite mineral by oligomerization. Modulates the RNA-binding activity of ACO1 (By similarity). {ECO:0000250, ECO:0000269|PubMed:19805308}. PTM: Processed in two steps by mitochondrial processing peptidase (MPP). MPP first cleaves the precursor to intermediate form and subsequently converts the intermediate to yield frataxin mature form (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q16595}. Mitochondrion {ECO:0000269|PubMed:17597094, ECO:0000269|PubMed:9241270}. Note=PubMed:17597094 describes localization exclusively in mitochondria. SUBUNIT: Monomer (probable predominant form). Oligomer (PubMed:11823441). Interacts with LYRM4 and HSPA9. Interacts with ACO1. Interacts with ISCU. Interacts with FECH; one iron-bound FXN monomer seems to interact with a FECH homodimer. Interacts with SDHA and SDHB. Interacts with ACO2; the interaction is dependent on citrate (By similarity). {ECO:0000250|UniProtKB:D3ZYW7, ECO:0000250|UniProtKB:Q16595, ECO:0000269|PubMed:11823441}. TISSUE SPECIFICITY: Heart, liver, skeletal muscle, kidney, spleen and thymus. Weakly expressed in the brain and lung. {ECO:0000269|PubMed:9241270}. +Q61575 FOXN1_MOUSE Forkhead box protein N1 (Hepatocyte nuclear factor 3 forkhead homolog 11) (HFH-11) (HNF-3/forkhead homolog 11) (Winged-helix transcription factor nude) 648 69,245 Chain (1); Compositional bias (1); DNA binding (1) FUNCTION: Transcriptional regulator which regulates the development, differentiation, and function of thymic epithelial cells (TECs) both in the prenatal and postnatal thymus. Acts as a master regulator of the TECs lineage development and is required from the onset of differentiation in progenitor TECs in the developing fetus to the final differentiation steps through which TECs mature to acquire their full functionality. Regulates, either directly or indirectly the expression of a variety of genes that mediate diverse aspects of thymus development and function, including MHC Class II, DLL4, CCL25, CTSL, CD40 and PAX1. Regulates the differentiation of the immature TECs into functional cortical TECs (cTECs) and medullary TECs (mTECs) (PubMed:22072979). Essential for maintenance of mTECs population in the postnatal thymus (PubMed:19955175). Involved in the morphogenesis and maintenance of the three-dimensional thymic microstructure which is necessary for a fully functional thymus (PubMed:21109991). Plays an important role in the maintenance of hematopoiesis and particularly T lineage progenitors within the bone marrow niche with age (PubMed:24184560). Essential for the vascularization of the thymus anlage (PubMed:19853842). Promotes the terminal differentiation of epithelial cells in the epidermis and hair follicles, partly by negatively regulating the activity of protein kinase C (PubMed:17459087). {ECO:0000269|PubMed:17459087, ECO:0000269|PubMed:19853842, ECO:0000269|PubMed:19955175, ECO:0000269|PubMed:21109991, ECO:0000269|PubMed:22072979, ECO:0000269|PubMed:24184560}. SUBCELLULAR LOCATION: Nucleus. TISSUE SPECIFICITY: Bone marrow (at protein level). Expressed in thymus and skin. {ECO:0000269|PubMed:24184560}. DISEASE: Note=Defects in FOXN1 are the cause of the nude/severe combined immunodeficiency (SCID) phenotype which is characterized by athymia and hairlessness. Mice develop largely normal hair follicles and produce hair shafts. However, presumably because of a lack of certain hair keratins, the hair shafts that are generated twist and coil in the hair follicle infundibulum, which becomes dilated. Since hair shafts fail to penetrate the epidermis, macroscopic nudity results and generates the grossly misleading impression that nude mice are hairless. {ECO:0000269|PubMed:2288204, ECO:0000269|PubMed:7969402}. +O08790 FPRS1_MOUSE Formyl peptide receptor-related sequence 1 (FMLP-related receptor I) (FMLP-R-I) (Formyl peptide receptor related sequence 1) (Formyl peptide receptor-like 1) (Lipoxin A4 receptor) (LXA4 receptor) (N-formyl peptide receptor 2) (N-formyl peptide receptor 3) 351 39,523 Chain (1); Disulfide bond (1); Glycosylation (2); Sequence conflict (9); Topological domain (8); Transmembrane (7) TRANSMEM 28 50 Helical; Name=1. {ECO:0000255}.; TRANSMEM 62 83 Helical; Name=2. {ECO:0000255}.; TRANSMEM 101 121 Helical; Name=3. {ECO:0000255}.; TRANSMEM 141 162 Helical; Name=4. {ECO:0000255}.; TRANSMEM 206 226 Helical; Name=5. {ECO:0000255}.; TRANSMEM 243 266 Helical; Name=6. {ECO:0000255}.; TRANSMEM 287 306 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 27 Extracellular. {ECO:0000255}.; TOPO_DOM 51 61 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 84 100 Extracellular. {ECO:0000255}.; TOPO_DOM 122 140 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 163 205 Extracellular. {ECO:0000255}.; TOPO_DOM 227 242 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 267 286 Extracellular. {ECO:0000255}.; TOPO_DOM 307 351 Cytoplasmic. {ECO:0000255}. FUNCTION: Low affinity receptor for N-formyl-methionyl peptides. Receptor for lipoxin A4. May have an olfactory function associated with the identification of pathogens or of pathogenic states. {ECO:0000269|PubMed:19387439}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed exclusively in vomeronasal neurons (PubMed:19387439 and PubMed:19497865). Expressed in 0.6 % of a subset of sensory neurons located in the basal layer of the vomeronasal organ. Each neuron appears to express only one receptor gene. Expressed mostly in neutrophils, followed by spleen and lung and expressed at very low levels in heart and liver (PubMed:19387439). {ECO:0000269|PubMed:19387439, ECO:0000269|PubMed:19497865, ECO:0000269|PubMed:9151906, ECO:0000269|PubMed:9722950}. +Q3SXG2 FPRS6_MOUSE Formyl peptide receptor-related sequence 6 339 38,154 Chain (1); Disulfide bond (1); Glycosylation (2); Sequence conflict (6); Topological domain (8); Transmembrane (7) TRANSMEM 24 44 Helical; Name=1. {ECO:0000255}.; TRANSMEM 63 85 Helical; Name=2. {ECO:0000255}.; TRANSMEM 100 120 Helical; Name=3. {ECO:0000255}.; TRANSMEM 145 165 Helical; Name=4. {ECO:0000255}.; TRANSMEM 199 219 Helical; Name=5. {ECO:0000255}.; TRANSMEM 242 262 Helical; Name=6. {ECO:0000255}.; TRANSMEM 281 301 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 23 Extracellular. {ECO:0000255}.; TOPO_DOM 45 62 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 86 99 Extracellular. {ECO:0000255}.; TOPO_DOM 121 144 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 166 198 Extracellular. {ECO:0000255}.; TOPO_DOM 220 241 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 263 280 Extracellular. {ECO:0000255}.; TOPO_DOM 302 339 Cytoplasmic. {ECO:0000255}. FUNCTION: May have an olfactory function associated with the identification of pathogens or of pathogenic states. {ECO:0000269|PubMed:19387439}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed exclusively in vomeronasal tissue (PubMed:19387439 and PubMed:19497865). Expressed in 1.2 % of a subset of sensory neurons located in the apical layer of the vomeronasal organ. Each neuron appears to express only one receptor gene. Expressed in brain, spleen, skeletal muscle and at high level in testis (PubMed:12459252). {ECO:0000269|PubMed:12459252, ECO:0000269|PubMed:19387439, ECO:0000269|PubMed:19497865}. +B1AXV0 FRS1L_MOUSE DOMON domain-containing protein FRRS1L (Ferric-chelate reductase 1-like protein) 293 32,507 Chain (1); Domain (1); Erroneous initiation (1); Signal peptide (1); Transmembrane (1) TRANSMEM 271 291 Helical. {ECO:0000255}. FUNCTION: Important modulator of glutamate signaling pathway. {ECO:0000250|UniProtKB:Q9P0K9}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:22632720}. Cell junction, synapse {ECO:0000305|PubMed:22632720}. SUBUNIT: Component of the outer core of AMPAR complex. AMPAR complex consists of an inner core made of 4 pore-forming GluA/GRIA proteins (GRIA1, GRIA2, GRIA3 and GRIA4) and 4 major auxiliary subunits arranged in a twofold symmetry. One of the two pairs of distinct binding sites is occupied either by CNIH2, CNIH3 or CACNG2, CACNG3. The other harbors CACNG2, CACNG3, CACNG4, CACNG8 or GSG1L. This inner core of AMPAR complex is complemented by outer core constituents binding directly to the GluA/GRIA proteins at sites distinct from the interaction sites of the inner core constituents. Outer core constituents include at least PRRT1, PRRT2, CKAMP44/SHISA9, FRRS1L and NRN1. The proteins of the inner and outer core serve as a platform for other, more peripherally associated AMPAR constituents. Alone or in combination, these auxiliary subunits control the gating and pharmacology of the AMPAR complex and profoundly impact their biogenesis and protein processing. {ECO:0000269|PubMed:22632720}. TISSUE SPECIFICITY: Expressed in the brain (at protein level) (PubMed:22632720). In embryos expression is evident in the ventral forebrain, but a lower level is seen in the remainder of the embryos. In the adult brain, expressed in the cortex, cerebellum, hippocampus and basal ganglia (PubMed:27236917). {ECO:0000269|PubMed:22632720, ECO:0000269|PubMed:27236917}. +Q8K3Q3 FOXN4_MOUSE Forkhead box protein N4 521 56,121 Chain (1); DNA binding (1); Sequence conflict (6) FUNCTION: Transcription factor essential for neural and some non-neural tissues development, such as retina and lung respectively. Binds to an 11-bp consensus sequence containing the invariant tetranucleotide 5'-ACGC-3'. During development of the central nervous system, is required to specify the amacrine and horizontal cell fates from multipotent retinal progenitors while suppressing the alternative photoreceptor cell fates through activating DLL4-NOTCH signaling. Also acts synergistically with ASCL1/MASH1 to activate DLL4-NOTCH signaling and drive commitment of p2 progenitors to the V2b interneuron fates during spinal cord neurogenesis. In development of non-neural tissues, plays an essential role in the specification of the atrioventricular canal and is indirectly required for patterning the distal airway during lung development. {ECO:0000269|PubMed:15363391, ECO:0000269|PubMed:16020526, ECO:0000269|PubMed:17728344, ECO:0000269|PubMed:21438071, ECO:0000269|PubMed:22323600, ECO:0000269|PubMed:23652001}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089, ECO:0000269|PubMed:22323600}. TISSUE SPECIFICITY: Mainly expressed in proliferator progenitor cells in brain and retina rather than differentiated cells. In contrast, is expressed only in postmitotic epithelial cells rather than in proliferative progenitors in the proximal airway. {ECO:0000269|PubMed:15363391, ECO:0000269|PubMed:16020526, ECO:0000269|PubMed:21438071}. +Q8K385 FRRS1_MOUSE Ferric-chelate reductase 1 (EC 1.-.-.-) (Stromal cell-derived receptor 2) (SDR-2) 592 66,047 Chain (1); Domain (3); Glycosylation (4); Metal binding (4); Sequence conflict (11); Transmembrane (7) TRANSMEM 2 22 Helical; Name=1. {ECO:0000255}.; TRANSMEM 372 392 Helical; Name=2. {ECO:0000255}.; TRANSMEM 415 435 Helical; Name=3. {ECO:0000255}.; TRANSMEM 446 466 Helical; Name=4. {ECO:0000255}.; TRANSMEM 477 499 Helical; Name=5. {ECO:0000255}.; TRANSMEM 515 535 Helical; Name=6. {ECO:0000255}.; TRANSMEM 569 589 Helical; Name=7. {ECO:0000255}. FUNCTION: Ferric-chelate reductases reduce Fe(3+) to Fe(2+) before its transport from the endosome to the cytoplasm. {ECO:0000269|PubMed:14499595}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in spleen, liver and kidney with low expression in brain. Localizes in adult brain to the choroid plexus of the fourth, third, and lateral ventricles and to ependymal cells that line the ventricles. {ECO:0000269|PubMed:14499595, ECO:0000269|PubMed:8938438}. +Q61553 FSCN1_MOUSE Fascin (Singed-like protein) 493 54,508 Chain (1); Cross-link (1); Initiator methionine (1); Modified residue (8); Sequence conflict (12) FUNCTION: Organizes filamentous actin into bundles with a minimum of 4.1:1 actin/fascin ratio. Plays a role in the organization of actin filament bundles and the formation of microspikes, membrane ruffles, and stress fibers. Important for the formation of a diverse set of cell protrusions, such as filopodia, and for cell motility and migration (By similarity). {ECO:0000250}. PTM: Phosphorylation on Ser-39 inhibits the actin-binding ability of fascin. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q16658}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q16658}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:Q16658}. Cell projection, growth cone {ECO:0000269|PubMed:24720729}. Cell projection, filopodium {ECO:0000269|PubMed:24720729}. Cell projection, invadopodium {ECO:0000269|PubMed:24720729}. Cell projection, microvillus {ECO:0000250|UniProtKB:Q16658}. Cell junction {ECO:0000250|UniProtKB:Q16658}. Note=Colocalized with RUFY3 and F-actin at filipodia of the axonal growth cone (PubMed:24720729). Colocalized with DBN1 and F-actin at the transitional domain of the axonal growth cone (PubMed:24720729). {ECO:0000250|UniProtKB:Q16658, ECO:0000269|PubMed:24720729}. SUBUNIT: Interacts with RUFY3 (via N-terminus); the interaction induces neuron axon development (PubMed:24720729). Associates with beta-catenin (PubMed:8794867). Interacts with PLXNB3 (PubMed:21706053). {ECO:0000269|PubMed:21706053, ECO:0000269|PubMed:24720729, ECO:0000269|PubMed:8794867}. DOMAIN: Composed of four beta-trefoil domains. {ECO:0000250}. TISSUE SPECIFICITY: Most abundant in brain. Found in other tissues including uterus, small intestine and spleen. +Q32M02 FSCN2_MOUSE Fascin-2 (Retinal fascin) 492 55,073 Chain (1); Natural variant (1); Sequence conflict (1) FUNCTION: Acts as an actin bundling protein. May play a pivotal role in photoreceptor cell-specific events, such as disk morphogenesis. Important for maintaining functional hair-cell bundless in the inner ear. May stiffen the longer stereocilia of hair-cell bundles in the inner ear enabling better force transmission to tip links. {ECO:0000269|PubMed:20660251}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:20660251}. Cell projection, stereocilium {ECO:0000269|PubMed:20660251}. Note=Found mostly in longer hair-cell stereocilia and, in all stereocilia, present in gradient with the highest concentration at stereocilia tips. TISSUE SPECIFICITY: Expressed in the inner ear. DISEASE: Note=Defects in Fscn2 lead to hair-cell degeneration in the inner ear and are a key contributor to the early-onset, age-related hearing loss (prebycusis) phenotype when in combination with waltzer cadherin 23 mutant. {ECO:0000269|PubMed:20660251}. +Q922K9 FRK_MOUSE Tyrosine-protein kinase FRK (EC 2.7.10.2) (Beta-cell Src-homology tyrosine kinase) (BSK) (FYN-related kinase) (Intestine tyrosine kinase) 512 58,844 Active site (1); Beta strand (16); Binding site (1); Chain (1); Domain (3); Helix (3); Modified residue (2); Nucleotide binding (1); Sequence conflict (6); Turn (1) FUNCTION: Non-receptor tyrosine-protein kinase that negatively regulates cell proliferation. Positively regulates PTEN protein stability through phosphorylation of PTEN on 'Tyr-336', which in turn prevents its ubiquitination and degradation, possibly by reducing its binding to NEDD4. May function as a tumor suppressor (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Predominantly found in the nucleus, with a small fraction found in the cell periphery. {ECO:0000250}. SUBUNIT: Interacts (via the SH3-domain) with PTEN. Interacts with RB1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in intestinal tract, fetal and adult islets of Langerhans, kidney, liver and lung. {ECO:0000269|PubMed:7733928, ECO:0000269|PubMed:7835707}. +Q62356 FSTL1_MOUSE Follistatin-related protein 1 (Follistatin-like protein 1) (TGF-beta-inducible protein TSC-36) 306 34,554 Chain (1); Disulfide bond (3); Domain (5); Glycosylation (3); Modified residue (1); Sequence conflict (1); Signal peptide (1) FUNCTION: May modulate the action of some growth factors on cell proliferation and differentiation. Binds heparin (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. SUBUNIT: Interacts with SCN10A. +Q8BYC4 GPR20_MOUSE G-protein coupled receptor 20 358 39,432 Chain (1); Glycosylation (2); Topological domain (8); Transmembrane (7) TRANSMEM 47 67 Helical; Name=1. {ECO:0000255}.; TRANSMEM 85 105 Helical; Name=2. {ECO:0000255}.; TRANSMEM 124 144 Helical; Name=3. {ECO:0000255}.; TRANSMEM 167 188 Helical; Name=4. {ECO:0000255}.; TRANSMEM 196 216 Helical; Name=5. {ECO:0000255}.; TRANSMEM 238 258 Helical; Name=6. {ECO:0000255}.; TRANSMEM 275 295 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 46 Extracellular. {ECO:0000255}.; TOPO_DOM 68 84 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 106 123 Extracellular. {ECO:0000255}.; TOPO_DOM 145 166 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 189 195 Extracellular. {ECO:0000255}.; TOPO_DOM 217 237 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 259 274 Extracellular. {ECO:0000255}.; TOPO_DOM 296 358 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan receptor with constitutive G(i) signaling activity that activate cyclic AMP. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous expressed with abundant expression in intestinal tissues. {ECO:0000269|PubMed:18347022}. +Q8BZL4 GPR22_MOUSE G-protein coupled receptor 22 432 49,019 Chain (1); Glycosylation (2); Topological domain (8); Transmembrane (7) TRANSMEM 46 66 Helical; Name=1. {ECO:0000255}.; TRANSMEM 86 106 Helical; Name=2. {ECO:0000255}.; TRANSMEM 116 136 Helical; Name=3. {ECO:0000255}.; TRANSMEM 157 177 Helical; Name=4. {ECO:0000255}.; TRANSMEM 209 229 Helical; Name=5. {ECO:0000255}.; TRANSMEM 315 335 Helical; Name=6. {ECO:0000255}.; TRANSMEM 349 369 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 45 Extracellular. {ECO:0000305}.; TOPO_DOM 67 85 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 107 115 Extracellular. {ECO:0000305}.; TOPO_DOM 137 156 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 178 208 Extracellular. {ECO:0000305}.; TOPO_DOM 230 314 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 336 348 Extracellular. {ECO:0000305}.; TOPO_DOM 370 432 Cytoplasmic. {ECO:0000305}. FUNCTION: Orphan G-protein coupled receptor. Seems to act through a G(i)/G(o) mediated pathway (By similarity). May be involved in ciliogenesis (By similarity). {ECO:0000250|UniProtKB:A0A2R9YJI3, ECO:0000250|UniProtKB:Q99680}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:D4A3U0}; Multi-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Abundant levels detected in the brain and heart and no detectable expression in other peripheral tissues. {ECO:0000269|PubMed:18539757}. +F8VQN3 GPR31_MOUSE 12-(S)-hydroxy-5,8,10,14-eicosatetraenoic acid receptor (12-(S)-HETE receptor) (12-HETER) (G-protein coupled receptor 31) 319 35,642 Chain (1); Glycosylation (1); Sequence conflict (11); Topological domain (8); Transmembrane (7) TRANSMEM 17 37 Helical; Name=1. {ECO:0000255}.; TRANSMEM 53 73 Helical; Name=2. {ECO:0000255}.; TRANSMEM 92 110 Helical; Name=3. {ECO:0000255}.; TRANSMEM 132 152 Helical; Name=4. {ECO:0000255}.; TRANSMEM 181 201 Helical; Name=5. {ECO:0000255}.; TRANSMEM 220 240 Helical; Name=6. {ECO:0000255}.; TRANSMEM 266 284 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 16 Extracellular. {ECO:0000255}.; TOPO_DOM 38 52 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 74 91 Extracellular. {ECO:0000255}.; TOPO_DOM 111 131 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 153 180 Extracellular. {ECO:0000255}.; TOPO_DOM 202 219 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 241 265 Extracellular. {ECO:0000255}.; TOPO_DOM 285 319 Cytoplasmic. {ECO:0000255}. FUNCTION: High-affinity receptor for 12-(S)-hydroxy-5,8,10,14-eicosatetraenoic acid (12-S-HETE). 12-(S)-HETE is an arachidonic acid metabolite secreted by platelets and tumor cells, and known to induce endothelial cells retraction allowing invasive cell access to the subendothelial matrix, which is a critical step for extravasation or metastasis. Ligand-binding lead to activation of ERK1/2 (MAPK3/MAPK1), MEK, and NF-kappa-B (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q9R1K6 GPR34_MOUSE Probable G-protein coupled receptor 34 375 43,173 Chain (1); Disulfide bond (1); Glycosylation (5); Topological domain (8); Transmembrane (7) TRANSMEM 55 75 Helical; Name=1. {ECO:0000255}.; TRANSMEM 82 102 Helical; Name=2. {ECO:0000255}.; TRANSMEM 122 142 Helical; Name=3. {ECO:0000255}.; TRANSMEM 165 185 Helical; Name=4. {ECO:0000255}.; TRANSMEM 210 230 Helical; Name=5. {ECO:0000255}.; TRANSMEM 263 283 Helical; Name=6. {ECO:0000255}.; TRANSMEM 304 324 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 54 Extracellular. {ECO:0000255}.; TOPO_DOM 76 81 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 103 121 Extracellular. {ECO:0000255}.; TOPO_DOM 143 164 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 186 209 Extracellular. {ECO:0000255}.; TOPO_DOM 231 262 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 284 303 Extracellular. {ECO:0000255}.; TOPO_DOM 325 375 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan receptor. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Broadly expressed. +Q8K2I9 FBH1_MOUSE F-box DNA helicase 1 (EC 3.6.4.12) (F-box only protein 18) 1042 118,298 Alternative sequence (2); Chain (1); Domain (2); Motif (2); Nucleotide binding (1); Sequence conflict (3) Protein modification; protein ubiquitination. FUNCTION: 3'-5' DNA helicase and substrate-recognition component of the SCF(FBH1) E3 ubiquitin ligase complex that plays a key role in response to stalled/damaged replication forks (By similarity). Involved in genome maintenance by acting as an anti-recombinogenic helicase and preventing extensive strand exchange during homologous recombination: promotes RAD51 filament dissolution from stalled forks, thereby inhibiting homologous recombination and preventing excessive recombination (PubMed:24108124). Also promotes cell death and DNA double-strand breakage in response to replication stress: together with MUS81, promotes the endonucleolytic DNA cleavage following prolonged replication stress via its helicase activity, possibly to eliminate cells with excessive replication stress. Plays a major role in remodeling of stalled DNA forks by catalyzing fork regression, in which the fork reverses and the two nascent DNA strands anneal. In addition to the helicase activity, also acts as the substrate-recognition component of the SCF(FBH1) E3 ubiquitin ligase complex, a complex that mediates ubiquitination of RAD51, leading to regulate RAD51 subcellular location (By similarity). {ECO:0000250|UniProtKB:Q8NFZ0, ECO:0000269|PubMed:24108124}. PTM: Ubiquitinated. Ubiquitination by the DCX(DTL) complex, also named CRL4(CDT2), leading to its degradation: ubiquitination takes place after its localization to DNA damage sites, possibly to facilitate the translesion synthesis (TLS) pathway. {ECO:0000250|UniProtKB:Q8NFZ0}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8NFZ0}. Chromosome {ECO:0000250|UniProtKB:Q8NFZ0}. Note=Accumulates at sites of DNA damage or replication stress. PCNA is required for localization to DNA damage sites. Localizes to the nucleoplasm in absence of DNA damage. {ECO:0000250|UniProtKB:Q8NFZ0}. SUBUNIT: Part of the SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase complex SCF(FBH1) composed of CUL1, SKP1, RBX1 and FBH1 (By similarity). Interacts with RPA2 (By similarity). Interacts with RAD51 (PubMed:24108124). Interacts (via PIP-box and RanBP2-type zinc finger) with PCNA (By similarity). {ECO:0000250|UniProtKB:Q8NFZ0, ECO:0000269|PubMed:24108124}. DOMAIN: The PIP-box mediates the interaction with PCNA. {ECO:0000250|UniProtKB:Q8NFZ0}. +P37889 FBLN2_MOUSE Fibulin-2 (FIBL-2) 1221 131,834 Alternative sequence (1); Chain (1); Disulfide bond (35); Domain (14); Glycosylation (4); Motif (1); Region (4); Sequence conflict (6); Signal peptide (1) FUNCTION: Its binding to fibronectin and some other ligands is calcium dependent. May act as an adapter that mediates the interaction between FBN1 and ELN. {ECO:0000250|UniProtKB:P98095}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SUBUNIT: Homotrimer; disulfide-linked. Interacts with LAMA2 (PubMed:10022829). Interacts with FBN1 (via N-terminal domain). Forms a ternary complex with ELN and FBN1 (By similarity). {ECO:0000250|UniProtKB:P98095, ECO:0000269|PubMed:10022829}. TISSUE SPECIFICITY: Component of both basement membranes and other connective tissues. +Q7TPD1 FBX11_MOUSE F-box only protein 11 930 103,728 Alternative sequence (2); Chain (1); Domain (1); Mutagenesis (2); Repeat (19); Sequence conflict (2); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as DTL/CDT2, BCL6 and PRDM1/BLIMP1. The SCF(FBXO11) complex mediates ubiquitination and degradation of BCL6, thereby playing a role in the germinal center B-cells terminal differentiation toward memory B-cells and plasma cells. The SCF(FBXO11) complex also mediates ubiquitination and degradation of DTL, an important step for the regulation of TGF-beta signaling, cell migration and the timing of the cell-cycle progression and exit. Binds to and neddylates phosphorylated p53/TP53, inhibiting its transcriptional activity. SCF(FBXO11) does not seem to direct ubiquitination of p53/TP53. {ECO:0000250|UniProtKB:Q86XK2}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}. SUBUNIT: Component of the SCF(FBXO11) complex consisting of CUL1, RBX1, SKP1 and FBXO11. Interacts with p53/TP53, BCL6 and DTL (when not phosphorylated). Interacts with PRMD1. {ECO:0000250|UniProtKB:Q86XK2}. TISSUE SPECIFICITY: At E9.5 and E10.5, expression is restricted to developing heart tissue. By E11.5 and E12.5, detected in liver and subsequently in muscle by E13.5. At E14.5, still detected in heart, liver and muscle and also in the developing secondary palate including the nasal, medial and oral epithelia of the palatal shelves. At E15.5 and E16.5, expressed in lung, kidney, heart, liver, muscle and adrenal gland. At this time, fusion of the palate shelves has occurred, with expression confined to the nasal and oral epithelia. At E17.5, expression in the lung is confined to bronchial epithelial cells and is evident in bone marrow, skin, tissue macrophages, osteoblasts, kidney, liver and spleen. At E18.5, expressed in bone marrow, liver, kidney and muscle but decreases in heart and lung. At this time, first detected in the middle ear epithelium. At the newborn stage, expression is strong in the middle ear where it is confined to mucin-secreting cells, as well as persisting in bone marrow, kidney and liver. Middle ear expression persists in postnatal head tissue at 4 and 13 days after birth and has declined by 21 days after birth. In the adult, expression is seen in alveolar macrophages of the lung, glomeruli and collecting tubules of the kidney, midbrain, heart and muscle. {ECO:0000269|PubMed:17035249}. +Q9QZM8 FBX17_MOUSE F-box only protein 17 (F-box only protein 26) 286 32,500 Alternative sequence (2); Chain (1); Domain (2) FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. Able to recognize and bind denatured glycoproteins, which are modified with complex-type oligosaccharides. Also recognizes sulfated glycans. Does not bind high-mannose glycoproteins (By similarity). {ECO:0000250}. SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex. Interacts with SKP1 and CUL1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed primarily in the brain. {ECO:0000269|PubMed:18203720}. +Q8VE08 FBX33_MOUSE F-box only protein 33 (AIG30-12-1) 562 63,363 Chain (1); Compositional bias (1); Domain (1); Sequence conflict (1) Protein modification; protein ubiquitination. FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Probably recognizes and binds to phosphorylated target proteins. Recognizes YBX1. {ECO:0000269|PubMed:16797541}. SUBUNIT: Part of the SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase complex SCF(FBXO33) formed of CUL1, SKP1, RBX1 and FBXO33. Interacts via its N-terminus with YBX1 CSD domain. Directly interacts with SKP1 and CUL1 (By similarity). {ECO:0000250}. +Q80XI1 FBX34_MOUSE F-box only protein 34 695 77,138 Alternative sequence (1); Chain (1); Domain (1); Sequence conflict (3) FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. {ECO:0000250}. SUBUNIT: Directly interacts with SKP1 and CUL1. {ECO:0000250}. +Q8BIG4 FBX28_MOUSE F-box only protein 28 368 40,978 Chain (1); Domain (1); Erroneous initiation (1); Modified residue (4); Sequence conflict (1) FUNCTION: Probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q9NVF7}. SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex. {ECO:0000250}. +Q6NS60 FBX41_MOUSE F-box only protein 41 873 94,331 Chain (1); Coiled coil (1); Compositional bias (3); Domain (1); Modified residue (4) FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. {ECO:0000250}. SUBUNIT: Directly interacts with SKP1 and CUL1. {ECO:0000250}. +Q3ULA2 FBW1A_MOUSE F-box/WD repeat-containing protein 1A (Beta-TrCP protein E3RS-IkappaB) (Beta-transducin repeat-containing protein) (Beta-TrCP) (E3RSIkappaB) (mE3RS-IkappaB) (F-box and WD repeats protein beta-TrCP) (HOS) (Ubiquitin ligase FWD1) (pIkappaB-E3 receptor subunit) 605 68,923 Alternative sequence (1); Chain (1); Domain (1); Erroneous initiation (1); Region (2); Repeat (7); Sequence conflict (7) Protein modification; protein ubiquitination. FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Recognizes and binds to phosphorylated target proteins (PubMed:10097128, PubMed:16371461, PubMed:18782782, PubMed:9859996, PubMed:9990853, PubMed:21911472). SCF(BTRC) mediates the ubiquitination of phosphorylated NFKB, ATF4, CDC25A, DLG1, FBXO5, PER1, SMAD3, SMAD4, SNAI1 and probably NFKB2. SCF(BTRC) mediates the ubiquitination of CTNNB1 and participates in Wnt signaling (By similarity). SCF(BTRC) mediates the ubiquitination of NFKBIA, NFKBIB and NFKBIE; the degradation frees the associated NFKB1 to translocate into the nucleus and to activate transcription (PubMed:9859996, PubMed:10097128). Ubiquitination of NFKBIA occurs at 'Lys-21' and 'Lys-22' (PubMed:9859996, PubMed:10097128). SCF(BTRC) mediates the ubiquitination of CEP68; this is required for centriole separation during mitosis (By similarity). SCF(BTRC) mediates the ubiquitination and subsequent degradation of nuclear NFE2L1 (PubMed:21911472). Has an essential role in the control of the clock-dependent transcription via degradation of phosphorylated PER1 and PER2 (PubMed:18782782). May be involved in ubiquitination and subsequent proteasomal degradation through a DBB1-CUL4 E3 ubiquitin-protein ligase (By similarity). Required for activation of NFKB-mediated transcription by IL1B, MAP3K14, MAP3K1, IKBKB and TNF (By similarity). Required for proteolytic processing of GLI3 (PubMed:16371461). {ECO:0000250|UniProtKB:Q9Y297, ECO:0000269|PubMed:10097128, ECO:0000269|PubMed:16371461, ECO:0000269|PubMed:18782782, ECO:0000269|PubMed:21911472, ECO:0000269|PubMed:9859996, ECO:0000269|PubMed:9990853}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11735228}. Nucleus {ECO:0000269|PubMed:11735228}. SUBUNIT: Homodimer. Self-associates. Component of the SCF(BTRC) complex, composed of SKP1, CUL1 and BTRC. Direct interaction with SKP1 with SKP1 occurs via the F-box domain. Interacts with phosphorylated ubiquitination substrates SMAD3 and SMAD4. Interacts with phosphorylated ubiquitination substrates CTNNB1, NFKBIA, NFKBIB, NFKBIE, NFKB1/nuclear factor NF-kappa-B p105 subunit, ATF4, CDC25A, DLG1, FBXO5 and SNAI1; the interaction requires the phosphorylation of the 2 serine residues in the substrate destruction motif D-S-G-X(2,3,4)-S. Binds UBQLN1. Interacts with CDC34 and UBE2R2. Interacts with FBXW11. Interacts with CUL4A and DDB1. Part of a SCF(BTRC)-like complex lacking CUL1, which is associated with phosphorylated NKBIA and RELA; RELA interacts directly with NFKBIA. Interacts with the phosphorylated form of GLI3. Interacts with CLU. Interacts with PER1 (phosphorylated), PER2 (phosphorylated) and PER3. Interacts with phosphorylated ubiquitination substrate CEP68 (By similarity). Interacts with ZC3H12A; this interaction occurs when ZC3H12A is phosphorylated in a IKBKB/IKKB-dependent manner (PubMed:22037600). Interacts with HSF1; this interaction occurs during mitosis and induces HSF1 ubiquitin-dependent degradation, a process inhibited by CDC20 (By similarity). Interacts with NFE2L1 (PubMed:21911472). Interacts with INAVA (By similarity). Interacts with IL10RA; this interaction leads to IL10RA ubiquitination and subsequent degradation (By similarity). {ECO:0000250|UniProtKB:Q9Y297, ECO:0000269|PubMed:10097128, ECO:0000269|PubMed:11735228, ECO:0000269|PubMed:15917222, ECO:0000269|PubMed:16371461, ECO:0000269|PubMed:18782782, ECO:0000269|PubMed:21911472, ECO:0000269|PubMed:22037600, ECO:0000269|PubMed:9859996, ECO:0000269|PubMed:9990853}. DOMAIN: The N-terminal D domain mediates homodimerization. {ECO:0000250|UniProtKB:Q9Y297}. TISSUE SPECIFICITY: Expressed in heart, brain, liver, skeletal muscle and, most strongly, in testis. {ECO:0000269|PubMed:11735228}. +P20693 FCER2_MOUSE Low affinity immunoglobulin epsilon Fc receptor (Fc-epsilon-RII) (Lymphocyte IgE receptor) (CD antigen CD23) 331 37,648 Alternative sequence (2); Chain (1); Disulfide bond (4); Domain (1); Glycosylation (2); Lipidation (2); Metal binding (3); Repeat (3); Topological domain (2); Transmembrane (1) TRANSMEM 24 49 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 23 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 50 331 Extracellular. {ECO:0000255}. FUNCTION: Low-affinity receptor for immunoglobulin E (IgE) and CR2/CD21. Has essential roles in the regulation of IgE production and in the differentiation of B-cells (it is a B-cell-specific antigen). PTM: N- and O-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. +A0A0B4J1G0 FCGR4_MOUSE Low affinity immunoglobulin gamma Fc region receptor IV (CD16-2) (FcgammaRIV) 249 28,398 Chain (1); Disulfide bond (2); Domain (2); Glycosylation (3); Modified residue (1); Mutagenesis (1); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 204 224 Helical. {ECO:0000255}. TOPO_DOM 21 203 Extracellular. {ECO:0000305}.; TOPO_DOM 225 249 Cytoplasmic. {ECO:0000305}. FUNCTION: Receptor for the Fc region of immunoglobulin gamma (PubMed:16039578). Also acts as a receptor for the Fc region of immunoglobulin epsilon (PubMed:17558411, PubMed:18949059). Binds with intermediate affinity to both IgG2a and IgG2b (PubMed:16039578, PubMed:17558411, PubMed:19795417). Can bind to IgG2a and IgG2b monomers (PubMed:18949059). Does not display binding to IgG1 or IgG3 (PubMed:16039578). Mediates neutrophil activation by IgG complexes redundantly with Fcgr3 (PubMed:18097064). Plays a role in promoting bone resorption by enhancing osteoclast differentiation following binding to IgG2a (PubMed:25824719). Binds with low affinity to both the a and b allotypes of IgE (PubMed:18949059). Has also been shown to bind to IgE allotype a only but not to allotype b (PubMed:17558411). Binds aggregated IgE but not the monomeric form and bound monomeric IgG is readily displaced by IgE complexes (PubMed:18949059). Binding to IgE promotes macrophage-mediated phagocytosis, antigen presentation to T cells, production of proinflammatory cytokines and the late phase of cutaneous allergic reactions (PubMed:17558411, PubMed:18949059). {ECO:0000269|PubMed:16039578, ECO:0000269|PubMed:17558411, ECO:0000269|PubMed:18097064, ECO:0000269|PubMed:18949059, ECO:0000269|PubMed:19795417, ECO:0000269|PubMed:25824719}. PTM: N-glycosylated. {ECO:0000269|PubMed:16039578, ECO:0000269|PubMed:18949059}.; PTM: Phosphorylated following receptor ligation. {ECO:0000269|PubMed:17558411}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16039578, ECO:0000269|PubMed:17558411}; Single-pass type I membrane protein {ECO:0000255}. Note=Cell surface expression is dependent on the presence of the Fc receptor gamma chain Fcerg. {ECO:0000269|PubMed:16039578, ECO:0000269|PubMed:17558411}. SUBUNIT: Interacts with the Fc receptor gamma chain Fcerg; Fcerg is required for the cell surface expression of Fcrg4. {ECO:0000269|PubMed:16039578, ECO:0000269|PubMed:17558411}. TISSUE SPECIFICITY: Detected on myeloid cells, peripheral blood monocytes, splenic and bone marrow dendritic cells, and thioglycollate-elicited macrophages and neutrophils but absent from lymphoid populations with no expression observed on T cells, B cells, NK cells or other granulocytes (at protein level) (PubMed:16039578, PubMed:19795417). Expressed in peripheral blood leukocytes, spleen, liver, thymus and small intestine (PubMed:12389094, PubMed:17558411). {ECO:0000269|PubMed:12389094, ECO:0000269|PubMed:16039578, ECO:0000269|PubMed:17558411, ECO:0000269|PubMed:19795417}. +Q8CHQ0 FBX4_MOUSE F-box only protein 4 385 43,777 Chain (1); Domain (1); Modified residue (2); Sequence conflict (2) Protein modification; protein ubiquitination. FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes ubiquitination of CCND1 and its subsequent proteasomal degradation. Recognizes TERF1 and promotes its ubiquitination together with UBE2D1 (By similarity). {ECO:0000250, ECO:0000269|PubMed:17081987, ECO:0000269|PubMed:18598945, ECO:0000269|PubMed:19767775}. PTM: Phosphorylation at Ser-11 varies during the cell cycle. It is low in resting cells and high in the S phase and the G2/M phase of the cell cycle. Phosphorylation is decreased during late G1 phase. Phosphorylation at Ser-11 is important for homodimerization and for optimal ubiquitin ligase activity towards CCND1. {ECO:0000269|PubMed:18598945}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17081987}. SUBUNIT: Homodimer. Directly interacts with SKP1 and CUL1. Part of the SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase complex SCF(FBXO4) formed of CUL1, SKP1, RBX1 and FBXO4. Interacts with TERF1; this interaction is prevented in the presence of GNL3L. Identified in a complex with CRYAB and CCND1 (By similarity). {ECO:0000250}. +P16879 FES_MOUSE Tyrosine-protein kinase Fes/Fps (EC 2.7.10.2) (Proto-oncogene c-Fes) 822 93,779 Active site (1); Binding site (1); Chain (1); Coiled coil (2); Domain (3); Modified residue (7); Nucleotide binding (1); Region (1); Sequence conflict (14) FUNCTION: Tyrosine-protein kinase that acts downstream of cell surface receptors and plays a role in the regulation of the actin cytoskeleton, microtubule assembly, cell attachment and cell spreading. Plays a role in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Acts down-stream of the activated FCER1 receptor and the mast/stem cell growth factor receptor KIT. Plays a role in the regulation of mast cell degranulation. Plays a role in the regulation of cell differentiation and promotes neurite outgrowth in response to NGF signaling. Plays a role in cell scattering and cell migration in response to HGF-induced activation of EZR. Phosphorylates BCR and down-regulates BCR kinase activity. Phosphorylates HCLS1/HS1, PECAM1, STAT3 and TRIM28. {ECO:0000269|PubMed:16731527, ECO:0000269|PubMed:17595334, ECO:0000269|PubMed:19892014}. PTM: Autophosphorylated on Tyr-713 in response to FGF2. Phosphorylated by LYN in response to FCER1 activation. Phosphorylated by HCK (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Golgi apparatus {ECO:0000250}. Cell junction, focal adhesion {ECO:0000250}. Note=Distributed throughout the cytosol when the kinase is not activated. Association with microtubules requires activation of the kinase activity. Shuttles between focal adhesions and cell-cell contacts in epithelial cells. Recruited to the lateral cell membrane in polarized epithelial cells by interaction with phosphorylated EZR. Detected at tubular membrane structures in the cytoplasm and at the cell periphery (By similarity). {ECO:0000250}. SUBUNIT: Homooligomer. Interacts with BCR. Interacts (when activated, via coiled coil domain) with TRIM28. Interacts (via SH2 domain) with phosphorylated EZR, MS4A2/FCER1B and HCLS1/HS1. Interacts with phosphorylated KIT. Interacts with FLT3. Interacts (via F-BAR domain) with soluble tubulin. Interacts (via SH2 domain) with microtubules (By similarity). {ECO:0000250}. DOMAIN: The coiled coil domains are important for regulating the kinase activity. They mediate homooligomerization and probably also interaction with other proteins (By similarity). {ECO:0000250}.; DOMAIN: The N-terminal region including the first coiled coil domain mediates interaction with phosphoinositide-containing membranes. {ECO:0000250}. +Q9ERZ0 HEMGN_MOUSE Hemogen (Hemopoietic gene protein) (Negative differentiation regulator protein) (mNDR) 503 55,043 Chain (1); Modified residue (14); Region (1); Sequence conflict (1) FUNCTION: Regulates the proliferation and differentiation of hematopoietic cells. Overexpression block the TPA-induced megakaryocytic differentiation in the K562 cell model. May also prevent cell apoptosis through the activation of the nuclear factor-kappa B (NF-kB) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11404085}. TISSUE SPECIFICITY: Expressed in hematopoietic precursor cells. Highly expressed in bone marrow, the red pulp of the spleen and round spermatids. Weakly expressed in peripheral blood cells. {ECO:0000269|PubMed:11404085, ECO:0000269|PubMed:14648837}. +P29699 FETUA_MOUSE Alpha-2-HS-glycoprotein (Countertrypin) (Fetuin-A) 345 37,326 Chain (1); Disulfide bond (6); Domain (2); Glycosylation (3); Modified residue (7); Sequence conflict (1); Signal peptide (1) FUNCTION: Probably involved in differentiation. PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000250|UniProtKB:P02765}. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Liver is the major site of synthesis, but fetuin is also expressed in limb buds and other extrahepatic tissues during development. +Q7TMA4 FFAR4_MOUSE Free fatty acid receptor 4 (G-protein coupled receptor 120) (G-protein coupled receptor GT01) (Omega-3 fatty acid receptor 1) 361 40,813 Chain (1); Compositional bias (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 46 66 Helical; Name=1. {ECO:0000255}.; TRANSMEM 78 98 Helical; Name=2. {ECO:0000255}.; TRANSMEM 104 124 Helical; Name=3. {ECO:0000255}.; TRANSMEM 157 177 Helical; Name=4. {ECO:0000255}.; TRANSMEM 205 225 Helical; Name=5. {ECO:0000255}.; TRANSMEM 269 289 Helical; Name=6. {ECO:0000255}.; TRANSMEM 296 316 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 45 Extracellular. {ECO:0000255}.; TOPO_DOM 67 77 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 99 103 Extracellular. {ECO:0000255}.; TOPO_DOM 125 156 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 178 204 Extracellular. {ECO:0000255}.; TOPO_DOM 226 268 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 290 295 Extracellular. {ECO:0000255}.; TOPO_DOM 317 361 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for medium and long-chain free fatty acids (FFAs). Signals via a G(q)/G(11)-coupled pathway. Acts as a receptor for omega-3 fatty acids and mediates robust anti-inflammatory effects, particularly in macrophages and fat cells. The anti-inflammatory effects involve inhibition of TAK1 through a beta-arrestin 2 (ARRB2)/TAB1-dependent effect, but independent of the G(q)/G(11)-coupled pathway. Mediates potent insulin sensitizing and antidiabetic effects by repressing macrophage-induced tissue inflammation. Mediates the taste of fatty acids. Mediates FFA-induced inhibition of apoptosis in enteroendocrine cells. May play a role in the regulation of adipocyte development and differentiation. {ECO:0000269|PubMed:15619630, ECO:0000269|PubMed:15774482, ECO:0000269|PubMed:17250804, ECO:0000269|PubMed:20573884, ECO:0000269|PubMed:20813258}. PTM: Phosphorylated. FFA stimulation facilitates phosphorylation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20813258}; Multi-pass membrane protein {ECO:0000269|PubMed:20813258}. Note=Colocalized with ARRB2 following DHA treatment. SUBUNIT: Interacts with ARRB2 following docosahexaenoic acid (DHA) stimulation. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the taste buds of the circumvallate and fungiform papillae, mainly in type II cells (at protein level). Abundant expression in the intestinal tract. Highly expressed in adipose tissue, including subcutaneous, perineral, mesentric and epididymal adipose tissue. Expressed in proinflammatory CD11c+ macrophages, mature adipocytes, RAW 264.7 cells and enteroendocrine L cells. Expressed in the epithelium of circumvallate papillae containing taste buds but not in the nonsensory lingual epithelium. High expression detected also in pituitary gland, lung and spleen. Negligible expression in muscle, liver, brain, heart, kidney and stomach. {ECO:0000269|PubMed:15619630, ECO:0000269|PubMed:17250804, ECO:0000269|PubMed:19071193, ECO:0000269|PubMed:20573884, ECO:0000269|PubMed:20813258}. +Q0VDQ9 FEZF1_MOUSE Fez family zinc finger protein 1 475 52,006 Chain (1); Compositional bias (1); Motif (1); Sequence conflict (1); Zinc finger (6) FUNCTION: Transcription repressor. Involved in the axonal projection and proper termination of olfactory sensory neurons (OSN). Plays a role in rostro-caudal patterning of the diencephalon and in prethalamic formation. Expression is required in OSN to cell-autonomously regulate OSN axon projections. Regulates non-cell-autonomously the layer formation of the olfactory bulb development and the interneurons. May be required for correct rostral migration of the interneuron progenitors. {ECO:0000269|PubMed:16540508, ECO:0000269|PubMed:16971467}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q9ESP5 FEZF2_MOUSE Fez family zinc finger protein 2 (Forebrain embryonic zinc finger-like protein 2) (Zinc finger protein 312) (Zinc finger protein Fez-like) 455 48,931 Chain (1); Compositional bias (1); Motif (1); Sequence conflict (1); Zinc finger (6) FUNCTION: Transcription repressor. Required for the specification of corticospinal motor neurons and other subcerebral projection neurons. May play a role in layer and neuronal subtype-specific patterning of subcortical projections and axonal fasciculation. Controls the development of dendritic arborization and spines of large layer V pyramidal neurons. Plays a role in rostro-caudal patterning of the diencephalon and in prethalamic formation. {ECO:0000269|PubMed:16157277, ECO:0000269|PubMed:16314561, ECO:0000269|PubMed:16540508, ECO:0000269|PubMed:16971467}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16314561}. TISSUE SPECIFICITY: Highly expressed in neocortical layer V, moderately expressed in layer VI. Expressed in subcortically projecting neurons. {ECO:0000269|PubMed:16157277, ECO:0000269|PubMed:16314561}. +P70379 FGF14_MOUSE Fibroblast growth factor 14 (FGF-14) (Fibroblast growth factor homologous factor 4) (FHF-4) 247 27,764 Alternative sequence (1); Chain (1); Sequence conflict (1) FUNCTION: Probably involved in nervous system development and function. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Interacts with SCN8A. {ECO:0000250|UniProtKB:Q92915}. TISSUE SPECIFICITY: Brain and testis; widely distributed in the developing nervous system. In adult, high levels in the granular layer of the cerebellum, less in hippocampus and olfactory bulb. +O35622 FGF15_MOUSE Fibroblast growth factor 15 (FGF-15) 218 25,236 Chain (1); Signal peptide (1) FUNCTION: Involved in the suppression of bile acid biosynthesis through down-regulation of CYP7A1 expression. {ECO:0000269|PubMed:16213224, ECO:0000269|PubMed:23747249}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Interacts with MALRD1. {ECO:0000269|PubMed:23747249}. TISSUE SPECIFICITY: Expressed in the developing brain. +Q80UZ0 FGD5_MOUSE FYVE, RhoGEF and PH domain-containing protein 5 1219 134,719 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (3); Modified residue (1); Zinc finger (1) FUNCTION: Activates CDC42, a member of the Ras-like family of Rho- and Rac proteins, by exchanging bound GDP for free GTP. Mediates VEGF-induced CDC42 activation. May regulate proangiogenic action of VEGF in vascular endothelial cells, including network formation, directional movement and proliferation. May play a role in regulating the actin cytoskeleton and cell shape (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell projection, ruffle membrane {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Golgi apparatus {ECO:0000250}. Early endosome {ECO:0000250}. Note=In peripheral membrane ruffles, colocolizes with F-actin. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in highly vascularized tissues, such as lung, kidney and ovary. {ECO:0000269|PubMed:22328776}. +Q6P9Q4 FHOD1_MOUSE FH1/FH2 domain-containing protein 1 (Formin homolog overexpressed in spleen 1) (FHOS) (Formin homology 2 domain-containing protein 1) 1197 129,600 Chain (1); Compositional bias (2); Domain (4); Modified residue (7); Region (1); Sequence conflict (3) FUNCTION: Required for the assembly of F-actin structures, such as stress fibers. Depends on the Rho-ROCK cascade for its activity. Contributes to the coordination of microtubules with actin fibers and plays a role in cell elongation. Acts synergistically with ROCK1 to promote SRC-dependent non-apoptotic plasma membrane blebbing (By similarity). {ECO:0000250}. PTM: Phosphorylated by ROCK1. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell projection, bleb {ECO:0000250}. Note=Predominantly cytoplasmic. {ECO:0000250}. SUBUNIT: Self-associates via the FH2 domain. Binds to F-actin via its N-terminus. Binds to the cytoplasmic domain of CD21 via its C-terminus (By similarity). Interacts with ROCK1 in a Src-dependent manner (By similarity). {ECO:0000250}. DOMAIN: Regulated by intramolecular binding to a C-terminal auto-inhibitory domain. Effector binding abolishes this interaction and activates the protein (By similarity). {ECO:0000250}.; DOMAIN: The DAD domain regulates activation via by an autoinhibitory interaction with the GBD/FH3 domain. This autoinhibition is released upon competitive binding of an activated GTPase. The release of DAD allows the FH2 domain to then nucleate and elongate nonbranched actin filaments (By similarity). {ECO:0000250}. +O89106 FHIT_MOUSE Bis(5'-adenosyl)-triphosphatase (EC 3.6.1.29) (AP3A hydrolase) (AP3Aase) (Diadenosine 5',5'''-P1,P3-triphosphate hydrolase) (Dinucleosidetriphosphatase) (Fragile histidine triad protein) 150 17,235 Active site (1); Binding site (4); Chain (1); Domain (1); Modified residue (2); Motif (1); Nucleotide binding (1); Sequence conflict (1); Site (1) FUNCTION: Cleaves P(1)-P(3)-bis(5'-adenosyl) triphosphate (Ap3A) to yield AMP and ADP. Can also hydrolyze P(1)-P(4)-bis(5'-adenosyl) tetraphosphate (Ap4A), but has extremely low activity with ATP. Modulates transcriptional activation by CTNNB1 and thereby contributes to regulate the expression of genes essential for cell proliferation and survival, such as CCND1 and BIRC5. Plays a role in the induction of apoptosis via SRC and AKT1 signaling pathways. Inhibits MDM2-mediated proteasomal degradation of p53/TP53 and thereby plays a role in p53/TP53-mediated apoptosis. Induction of apoptosis depends on the ability of FHIT to bind P(1)-P(3)-bis(5'-adenosyl) triphosphate or related compounds, but does not require its catalytic activity (By similarity). Functions as tumor suppressor. {ECO:0000250, ECO:0000269|PubMed:10758156, ECO:0000269|PubMed:11517343}. PTM: Phosphorylation at Tyr-114 by SRC is required for induction of apoptosis. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9699672}. SUBUNIT: Homodimer. Interacts with UBE2I. Interacts with MDM2. Interacts with CTNNB1. Identified in a complex with CTNNB1 and LEF1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in heart, brain, lung and skeletal muscle. Particularly strong expression in liver, testis and kidney, where it is confined to the tubular epithelium. {ECO:0000269|PubMed:9671749, ECO:0000269|PubMed:9699672}. +Q8BPY9 FIGL1_MOUSE Fidgetin-like protein 1 (EC 3.6.4.-) 683 74,850 Binding site (1); Chain (1); Modified residue (1); Nucleotide binding (1); Sequence conflict (3) FUNCTION: Involved in DNA double-strand break (DBS) repair via homologous recombination (HR). Recruited at DSB sites independently of BRCA2, RAD51 and RAD51 paralogs in a H2AX-dependent manner. May regulate osteoblast proliferation and differentiation (PubMed:17352653). May play a role in the control of male meiosis dynamic (PubMed:22110678). {ECO:0000250|UniProtKB:Q6PIW4, ECO:0000269|PubMed:17352653, ECO:0000269|PubMed:22110678}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6PIW4}. Cytoplasm {ECO:0000269|PubMed:22110678}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:22110678}. Note=Together with RAD51 and a subset of H2A histone proteins, redistributed in discrete nuclear DNA damage-induced foci after ionizing radiation (IR) treatment. {ECO:0000250|UniProtKB:Q6PIW4}. SUBUNIT: Hexamer. Interacts (via N-terminal one-half region) with RAD51; the interaction is direct. Interacts (via N-terminal one-half region) with SPIDR (via the C-terminal region); the interaction is direct (By similarity). {ECO:0000250|UniProtKB:Q6PIW4}. DOMAIN: The N-terminus is necessary for its recruitment to DNA damage sites. {ECO:0000250|UniProtKB:Q6PIW4}. TISSUE SPECIFICITY: Expressed at high level in the testis (PubMed:22110678). Detected in pachytene spermatocytes and in metaphase spermatocytes (at protein level). {ECO:0000269|PubMed:22110678}. +Q99MX2 FHL17_MOUSE Ferritin heavy polypeptide-like 17 176 20,491 Chain (1); Domain (1); Metal binding (3); Sequence conflict (2) TISSUE SPECIFICITY: Testis specific. +Q9CR13 FMC1_MOUSE Protein FMC1 homolog (Formation of mitochondrial complex V assembly factor 1) 113 12,695 Chain (1) FUNCTION: Plays a role in the assembly/stability of the mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V). {ECO:0000250|UniProtKB:Q96HJ9}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q96HJ9}. SUBUNIT: Interacts with ATPAF2. {ECO:0000250|UniProtKB:Q96HJ9}. +Q9JL04 FMN2_MOUSE Formin-2 1578 167,387 Chain (1); Coiled coil (2); Compositional bias (20); Domain (2); Modified residue (4); Mutagenesis (1); Region (2); Repeat (12); Sequence conflict (8) FUNCTION: Actin-binding protein that is involved in actin cytoskeleton assembly and reorganization (PubMed:18848445, PubMed:21620703). Acts as an actin nucleation factor and promotes assembly of actin filaments together with SPIRE1 and SPIRE2 (PubMed:18848445, PubMed:21620703). Involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport (PubMed:21983562). Required for asymmetric spindle positioning, asymmetric oocyte division and polar body extrusion during female germ cell meiosis (PubMed:12447394, PubMed:18848445, PubMed:19062278, PubMed:21620703). Plays a role in responses to DNA damage, cellular stress and hypoxia by protecting CDKN1A against degradation, and thereby plays a role in stress-induced cell cycle arrest (By similarity). Also acts in the nucleus: together with SPIRE1 and SPIRE2, promotes assembly of nuclear actin filaments in response to DNA damage in order to facilitate movement of chromatin and repair factors after DNA damage (By similarity). Protects cells against apoptosis by protecting CDKN1A against degradation (By similarity). {ECO:0000250|UniProtKB:Q9NZ56, ECO:0000269|PubMed:12447394, ECO:0000269|PubMed:18848445, ECO:0000269|PubMed:19062278, ECO:0000269|PubMed:21620703, ECO:0000269|PubMed:21983562}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19062278, ECO:0000269|PubMed:21620703}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9NZ56}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:21620703}. Nucleus {ECO:0000250|UniProtKB:Q9NZ56}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9NZ56}. Cell membrane {ECO:0000269|PubMed:21705804}; Peripheral membrane protein {ECO:0000269|PubMed:21705804}; Cytoplasmic side {ECO:0000269|PubMed:21705804}. Cytoplasm, cell cortex {ECO:0000269|PubMed:21983562}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:21983562}; Peripheral membrane protein {ECO:0000269|PubMed:21983562}; Cytoplasmic side {ECO:0000269|PubMed:21983562}. Note=Colocalizes with the actin cytoskeleton (PubMed:21705804). Recruited to the membranes via its interaction with SPIRE1 (PubMed:21705804). Detected at the cleavage furrow during asymmetric oocyte division and polar body extrusion (PubMed:21620703). Accumulates in the nucleus following DNA damage (By similarity). {ECO:0000250|UniProtKB:Q9NZ56, ECO:0000269|PubMed:21620703, ECO:0000269|PubMed:21705804}. SUBUNIT: Interacts with SPIRE1 (PubMed:21705804). Binds actin (PubMed:21705804). Interacts with CDKN1A (By similarity). {ECO:0000250|UniProtKB:Q9NZ56, ECO:0000269|PubMed:21705804}. TISSUE SPECIFICITY: Detected in brain and in oocytes (at protein level) (PubMed:12447394, PubMed:19062278). Expressed almost exclusively in the developing and mature central nervous system (PubMed:10781961). Detected in oocytes (PubMed:12447394, PubMed:19062278). {ECO:0000269|PubMed:10781961, ECO:0000269|PubMed:12447394, ECO:0000269|PubMed:19062278}. +Q91X85 FLVC2_MOUSE Feline leukemia virus subgroup C receptor-related protein 2 (Calcium-chelate transporter) (CCT) 551 60,107 Chain (1); Compositional bias (1); Modified residue (1); Region (1); Repeat (8); Sequence conflict (2); Transmembrane (12) TRANSMEM 108 128 Helical. {ECO:0000255}.; TRANSMEM 148 168 Helical. {ECO:0000255}.; TRANSMEM 175 195 Helical. {ECO:0000255}.; TRANSMEM 199 219 Helical. {ECO:0000255}.; TRANSMEM 240 260 Helical. {ECO:0000255}.; TRANSMEM 275 295 Helical. {ECO:0000255}.; TRANSMEM 333 353 Helical. {ECO:0000255}.; TRANSMEM 372 392 Helical. {ECO:0000255}.; TRANSMEM 401 421 Helical. {ECO:0000255}.; TRANSMEM 424 444 Helical. {ECO:0000255}.; TRANSMEM 459 479 Helical. {ECO:0000255}.; TRANSMEM 490 510 Helical. {ECO:0000255}. FUNCTION: Acts as an importer of heme. Also acts as a transporter for a calcium-chelator complex, important for growth and calcium metabolism (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Found in the kidney and in cells implicated in rapid calcium exchange, namely the CNS, the eye, cardiomyocytes and placenta in late term. +Q3TR08 FNDC4_MOUSE Fibronectin type III domain-containing protein 4 (Fibronectin type III repeat-containing protein 1) 231 24,933 Chain (1); Domain (1); Erroneous initiation (1); Glycosylation (2); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 164 184 Helical. {ECO:0000255}. TOPO_DOM 41 163 Extracellular. {ECO:0000255}.; TOPO_DOM 185 231 Cytoplasmic. {ECO:0000255}. FUNCTION: Acts as an anti-inflammatory factor in the intestine and colon. Binds to and acts on macrophages to downregulate pro-inflammatory gene expression. Affects key macrophage functions, including phagocytosis, by downregulating many key pathways for macrophage activation, partly via by STAT3 activation and signaling. May be required to dampen the immunological response in colitis. {ECO:0000269|PubMed:27066907}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Secreted {ECO:0000269|PubMed:27066907}. Note=The N-terminus is probably cleaved to release a secreted extracellular portion of the protein. {ECO:0000269|PubMed:27066907}. TISSUE SPECIFICITY: Highly expressed in adult liver and brain tissues. {ECO:0000269|PubMed:12384288}. +Q80TY0 FNBP1_MOUSE Formin-binding protein 1 (Formin-binding protein 17) 616 71,344 Alternative sequence (7); Chain (1); Coiled coil (2); Compositional bias (1); Domain (3); Erroneous initiation (2); Modified residue (9); Region (10); Site (1) FUNCTION: Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during the late stage of clathrin-mediated endocytosis. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also enhances actin polymerization via the recruitment of WASL/N-WASP, which in turn activates the Arp2/3 complex. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. May act as a link between RND2 signaling and regulation of the actin cytoskeleton. May be required for the lysosomal retention of FASLG/FASL (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Lysosome {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Membrane, clathrin-coated pit {ECO:0000250}. Note=Enriched in cortical regions coincident with F-actin. Also localizes to endocytic vesicles and lysosomes. {ECO:0000250}. SUBUNIT: Homodimerizes, the dimers can polymerize end-to-end to form filamentous structures. Interacts specifically with GTP-bound RND2 and CDC42. Interacts with AKAP9, ARHGAP17, DAAM1, DIAPH1, DIAPH2, DNM1, DNM2, DNM3, FASLG/FASL, microtubules, PDE6G, SNX2 and WASL/N-WASP. May interact with TNKS (By similarity). {ECO:0000250}. DOMAIN: The F-BAR domain binds the phospholipid membrane with its concave surface. The end-to-end polymerization of dimers of these domains provides a curved surface that fits best membranes with around 600 A diameter, and may drive tubulation (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain and testis. {ECO:0000269|PubMed:15252009}. +Q8CCH7 FOG2_MOUSE Zinc finger protein ZFPM2 (Friend of GATA protein 2) (FOG-2) (Friend of GATA 2) (mFOG-2) (Zinc finger protein multitype 2) 1151 127,692 Alternative sequence (3); Chain (1); Cross-link (5); Modified residue (4); Motif (1); Region (1); Zinc finger (8) FUNCTION: Transcription regulator that plays a central role in heart morphogenesis and development of coronary vessels from epicardium, by regulating genes that are essential during cardiogenesis. Essential cofactor that acts via the formation of a heterodimer with transcription factors of the GATA family GATA4, GATA5 and GATA6. Such heterodimer can both activate or repress transcriptional activity, depending on the cell and promoter context. Also required in gonadal differentiation, possibly be regulating expression of SRY. Probably acts a corepressor of NR2F2. {ECO:0000269|PubMed:10330188, ECO:0000269|PubMed:10888889, ECO:0000269|PubMed:10892744, ECO:0000269|PubMed:12223418, ECO:0000269|PubMed:9927674, ECO:0000269|PubMed:9927675}. PTM: Sumoylation reduces transcriptional repression activity. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10330188, ECO:0000269|PubMed:9927674, ECO:0000269|PubMed:9927675}. SUBUNIT: Interacts with the N-terminal zinc-finger of GATA4, GATA5 and probably GATA6. Interacts with retinoid nuclear receptor RXRA when ligand bound. Interacts with corepressor CTBP2; this interaction is however not essential for corepressor activity. Interacts with NR2F2 and NR2F6. Interacts with ATOH8; mediates indirect interaction with GATA4. {ECO:0000269|PubMed:10330188, ECO:0000269|PubMed:10801815, ECO:0000269|PubMed:10999851, ECO:0000269|PubMed:11382775, ECO:0000269|PubMed:23836893, ECO:0000269|PubMed:9927674, ECO:0000269|PubMed:9927675}. DOMAIN: The CCHC FOG-type zinc fingers 1, 2, 3 and 5 directly bind to GATA-type zinc fingers. The Tyr residue adjacent to the last Cys of the CCHC FOG-type zinc finger is probably essential for the interaction with GATA-type zinc fingers. {ECO:0000269|PubMed:10329627}. TISSUE SPECIFICITY: Expressed in heart, brain and testis. Weakly expressed in lung and liver. First expressed at approximately E8.5 in the developing ventral heart tube and septum transversum. Cardiac expression persists throughout the remainder of embryonic development in the atria as well as in all layers of the ventricles (endocardium, myocardium, and pericardium). Expressed in the neuroepithelium of the developing midbrain and hindbrain from E11.5 and increased in intensity between E12 and E16.5. Also expressed in the urogenital ridge beginning at E11.5 and subsequently localized to the gonads by E16.5. Colocalizes with GATA4 GATA5 and GATA6 in the developing heart, GATA3 in the brain, and GATA4 in the gonads. {ECO:0000269|PubMed:10330188, ECO:0000269|PubMed:9927674, ECO:0000269|PubMed:9927675}. +O70165 FCN1_MOUSE Ficolin-1 (Collagen/fibrinogen domain-containing protein 1) (Ficolin-A) (Ficolin-alpha) (M-ficolin) 334 36,298 Chain (1); Disulfide bond (3); Domain (2); Glycosylation (1); Metal binding (2); Region (4); Signal peptide (1); Site (1) FUNCTION: Extracellular lectin functioning as a pattern-recognition receptor in innate immunity. Binds the sugar moieties of pathogen-associated molecular patterns (PAMPs) displayed on microbes and activates the lectin pathway of the complement system. May also activate monocytes through a G protein-coupled receptor, FFAR2, inducing the secretion of interleukin-8/IL-8. Binds preferentially to 9-O-acetylated 2-6-linked sialic acid derivatives and to various glycans containing sialic acid engaged in a 2-3 linkage (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O00602}. Cell membrane {ECO:0000250|UniProtKB:O00602}; Peripheral membrane protein {ECO:0000250|UniProtKB:O00602}; Extracellular side {ECO:0000250|UniProtKB:O00602}. Note=Found on the monocyte and granulocyte surface. {ECO:0000250|UniProtKB:O00602}. SUBUNIT: Homotrimer. Interacts with elastin/ELN. Interacts (via Fibrinogen C-terminal domain) with FFAR2. Interacts with CRP; may regulate monocyte activation by FCN1. {ECO:0000250|UniProtKB:O00602}. DOMAIN: The fibrinogen C-terminal domain mediates calcium-dependent binding to carbohydrates and tethering to the cell surface in monocytes and granulocytes. The domain undergoes a conformational switch at pH under 6.2, and looses its carbohydrate-binding ability. {ECO:0000250|UniProtKB:O00602}. TISSUE SPECIFICITY: Highly expressed in liver and spleen. +Q3U7U3 FBX7_MOUSE F-box only protein 7 523 57,649 Chain (1); Compositional bias (1); Domain (1); Modified residue (3); Motif (1); Region (5); Sequence conflict (3) Protein modification; protein ubiquitination. FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Recognizes BIRC2 and DLGAP5. Plays a role downstream of PINK1 in the clearance of damaged mitochondria via selective autophagy (mitophagy) by targeting PRKN to dysfunctional depolarized mitochondria. Promotes MFN1 ubiquitination (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Mitochondrion {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Note=Predominantly cytoplasmic. A minor proportion is detected in the nucleus. Relocates from the cytosol to depolarized mitochondria (By similarity). {ECO:0000250}. SUBUNIT: Part of the SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase complex SCF(FBXO7) formed of CUL1, SKP1, RBX1 and FBXO7. Interacts via its C-terminal proline-rich region with DLGAP5. Interacts with BIRC2. Interacts with CDK6 and promotes its interaction with D-type cyclin. Interacts (via the N-terminal Ubl domain) with PRKN. Interacts (via N-terminal region) with PINK1. Interacts with PSMF1 (By similarity). {ECO:0000250}. DOMAIN: The ubiquitin-like region mediates interaction with PRKN. {ECO:0000250}.; DOMAIN: The proline-rich region is important for protein-protein interactions. {ECO:0000250}. +Q9QZN3 FBX8_MOUSE F-box only protein 8 319 36,970 Chain (1); Domain (2); Sequence conflict (1) FUNCTION: May promote guanine-nucleotide exchange on an ARF. Promotes the activation of ARF through replacement of GDP with GTP (Potential). {ECO:0000305}. TISSUE SPECIFICITY: High expression in brain, heart, kidney, liver, lung, skeletal muscle, testis, and day-7 embryos. +Q61559 FCGRN_MOUSE IgG receptor FcRn large subunit p51 (FcRn) (IgG Fc fragment receptor transporter alpha chain) (Neonatal Fc receptor) 365 40,093 Chain (1); Disulfide bond (2); Domain (1); Glycosylation (4); Modified residue (1); Natural variant (2); Region (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 298 321 Helical. {ECO:0000255}. TOPO_DOM 22 297 Extracellular. {ECO:0000255}.; TOPO_DOM 322 365 Cytoplasmic. {ECO:0000255}. FUNCTION: Binds to the Fc region of monomeric immunoglobulins gamma (PubMed:7504013). Mediates the selective uptake of IgG from milk and helps newborn animals to acquire passive immunity. IgG in the milk is bound at the apical surface of the intestinal epithelium. The resultant FcRn-IgG complexes are transcytosed across the intestinal epithelium and IgG is released from FcRn into blood or tissue fluids (By similarity). Possible role in transfer of immunoglobulin G from mother to fetus (By similarity). {ECO:0000250|UniProtKB:P13599, ECO:0000250|UniProtKB:P55899, ECO:0000269|PubMed:7504013}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P13599}; Single-pass type I membrane protein {ECO:0000255}. SUBUNIT: FcRn complex consist of two subunits: p51, and p14 which is equivalent to beta-2-microglobulin. It forms an MHC class I-like heterodimer. {ECO:0000250|UniProtKB:P13599}. TISSUE SPECIFICITY: Intestinal epithelium of suckling rodents. Expressed in neonatal intestine and fetal yolk sac. {ECO:0000269|PubMed:7504013}. +P20491 FCERG_MOUSE High affinity immunoglobulin epsilon receptor subunit gamma (Fc receptor gamma-chain) (FcRgamma) (Fc-epsilon RI-gamma) (IgE Fc receptor subunit gamma) (FceRI gamma) 86 9,652 Chain (1); Disulfide bond (1); Domain (1); Modified residue (3); Mutagenesis (5); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 24 44 Helical. {ECO:0000255}. TOPO_DOM 19 23 Extracellular. {ECO:0000255}.; TOPO_DOM 45 86 Cytoplasmic. {ECO:0000255}. FUNCTION: Adapter protein containing an immunoreceptor tyrosine-based activation motif (ITAM) that transduces activation signals from various immunoreceptors. As a component of the high-affinity immunoglobulin E (IgE) receptor, mediates allergic inflammatory signaling in mast cells (PubMed:14764707). As a constitutive component of interleukin-3 receptor complex, selectively mediates interleukin 4/IL4 production by basophils, priming T-cells toward effector T-helper 2 subset (PubMed:19098920). Associates with pattern recognition receptors CLEC4D and CLEC4E to form a functional signaling complex in myeloid cells. Binding of mycobacterial trehalose 6,6'-dimycolate (TDM) to this receptor complex leads to phosphorylation of ITAM, triggering activation of SYK, CARD9 and NF-kappa-B, consequently driving maturation of antigen-presenting cells and shaping antigen-specific priming of T-cells toward effector T-helper 1 and T-helper 17 cell subtypes (PubMed:23602766) (Probable). May function cooperatively with other activating receptors. Functionally linked to integrin beta-2/ITGB2-mediated neutrophil activation (PubMed:17086186). Also involved in integrin alpha-2/ITGA2-mediated platelet activation (PubMed:9171347). {ECO:0000269|PubMed:14764707, ECO:0000269|PubMed:17086186, ECO:0000269|PubMed:19098920, ECO:0000269|PubMed:23602766, ECO:0000269|PubMed:9171347, ECO:0000305}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: IgE Fc receptor is a tetramer of an alpha chain, a beta chain, and two disulfide linked gamma chains. Associates with FCGR1A; forms a functional signaling complex (By similarity). Associates with CLEC6A (PubMed:17050534). Interacts with CLEC4E (PubMed:23602766, PubMed:18776906). Interacts (via ITAM domain) with SYK (via SH2 domains); activates SYK, enabling integrin-mediated activation of neutrophils and macrophages (PubMed:17086186). Interacts with CSF2RB and recruits SYK in response to IL3 stimulation; this interaction is direct (PubMed:19098920). Interacts with CD300LH; the interaction may be indirect (PubMed:20817736). Interacts with CD300LD (PubMed:20817736). Interacts with TARM1 (By similarity). {ECO:0000250|UniProtKB:P30273, ECO:0000269|PubMed:17050534, ECO:0000269|PubMed:17086186, ECO:0000269|PubMed:18776906, ECO:0000269|PubMed:19098920, ECO:0000269|PubMed:20817736, ECO:0000269|PubMed:23602766}. TISSUE SPECIFICITY: Expressed in mast cells (at protein level) (PubMed:14764707). Expressed in basophils (at protein level) (PubMed:19098920). {ECO:0000269|PubMed:14764707, ECO:0000269|PubMed:19098920}. +Q8BH70 FBXL4_MOUSE F-box/LRR-repeat protein 4 (F-box and leucine-rich repeat protein 4) 621 70,269 Chain (1); Domain (1); Modified residue (1); Repeat (9) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Mitochondrion {ECO:0000250}. SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex. {ECO:0000250}. +P23591 FCL_MOUSE GDP-L-fucose synthase (EC 1.1.1.271) (GDP-4-keto-6-deoxy-D-mannose-3,5-epimerase-4-reductase) (Protein FX) (Red cell NADP(H)-binding protein) (Transplantation antigen P35B) (Tum-P35B antigen) 321 35,878 Active site (1); Binding site (6); Chain (1); Natural variant (1); Nucleotide binding (2); Site (3) Nucleotide-sugar biosynthesis; GDP-L-fucose biosynthesis via de novo pathway; GDP-L-fucose from GDP-alpha-D-mannose: step 2/2. FUNCTION: Catalyzes the two-step NADP-dependent conversion of GDP-4-dehydro-6-deoxy-D-mannose to GDP-fucose, involving an epimerase and a reductase reaction. {ECO:0000250|UniProtKB:Q13630}. SUBUNIT: Homodimer. {ECO:0000250}. +Q9JMJ2 FBXW4_MOUSE F-box/WD repeat-containing protein 4 (F-box and WD-40 domain-containing protein 4) (Protein hagoromo) 410 46,142 Chain (1); Domain (1); Frameshift (1); Repeat (4); Sequence conflict (9) FUNCTION: Probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. Likely to be involved in key signaling pathways crucial for normal limb development. May participate in Wnt signaling. SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex (Probable). Interacts with POUF51 (PubMed:29153991). {ECO:0000269|PubMed:29153991, ECO:0000305}. +Q6PAV2 HERC4_MOUSE Probable E3 ubiquitin-protein ligase HERC4 (EC 2.3.2.26) (HECT domain and RCC1-like domain-containing protein 4) (HECT-type E3 ubiquitin transferase HERC4) 1057 118,412 Active site (1); Alternative sequence (3); Chain (1); Domain (1); Repeat (7); Sequence conflict (3) Protein modification; protein ubiquitination. FUNCTION: Probable E3 ubiquitin-protein ligase involved in either protein trafficking or in the distribution of cellular structures. Required for spermatozoon maturation and fertility, and for the removal of the cytoplasmic droplet of the spermatozoon. E3 ubiquitin-protein ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer it to targeted substrates. {ECO:0000269|PubMed:17967448}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q5GLZ8}. TISSUE SPECIFICITY: Ubiquitously expressed, highest expression is found in testis during spermiogenesis. It is specifically found in spermatogonia, spermatocytes, and spermatids with little or no expression detectable in the spermatozoa, or interstitial cells. {ECO:0000269|PubMed:17967448}. +P97447 FHL1_MOUSE Four and a half LIM domains protein 1 (FHL-1) (KyoT) (RBP-associated molecule 14-1) (RAM14-1) (Skeletal muscle LIM-protein 1) (SLIM) (SLIM-1) 280 31,889 Alternative sequence (2); Beta strand (1); Chain (1); Cross-link (1); Domain (4); Erroneous initiation (1); Initiator methionine (1); Modified residue (2); Sequence conflict (1); Zinc finger (1) FUNCTION: May have an involvement in muscle development or hypertrophy. Isoform 2 binds to RBP-J and plays a negative regulatory role in the RBP-J-mediated transcription in mammalian systems. SUBCELLULAR LOCATION: Isoform 1: Cytoplasm.; SUBCELLULAR LOCATION: Isoform 2: Nucleus. TISSUE SPECIFICITY: Isoform 1 seems to be most abundant in each tissue and isoform 2 much less abundant. Isoform 1 is highly expressed in skeletal muscle and lung, and to a lesser extent in heart, brain and kidney. Isoform 2 was found in brain, lung kidney and genital organs. {ECO:0000269|PubMed:10906474}. +Q8BKT2 HES7_MOUSE Transcription factor HES-7 (mHes7) (Hairy and enhancer of split 7) (bHLH factor Hes7) 225 24,890 Chain (1); Compositional bias (1); Domain (2); Motif (1); Mutagenesis (10); Sequence conflict (3) FUNCTION: Transcriptional repressor. Represses transcription from both N box- and E box-containing promoters. May with HES1, cooperatively regulate somite formation in the presomitic mesoderm (PSM). May function as a segmentation clock, which is essential for coordinated somite segmentation. {ECO:0000269|PubMed:11260262, ECO:0000269|PubMed:15170214, ECO:0000269|PubMed:18775957}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Transcription repression requires formation of a complex with a corepressor protein of the Groucho/TLE family. {ECO:0000250}. DOMAIN: Has a particular type of basic domain which includes a helix-interrupting proline.; DOMAIN: The C-terminal WRPW motif is a transcriptional repression motif which is necessary for interaction with Groucho/TLE family members, transcriptional corepressors recruited to specific target DNA by Hairy-related proteins. {ECO:0000250}. +P59024 FKB14_MOUSE Peptidyl-prolyl cis-trans isomerase FKBP14 (PPIase FKBP14) (EC 5.2.1.8) (FK506-binding protein 14) (FKBP-14) (Rotamase) 211 24,252 Calcium binding (2); Chain (1); Disulfide bond (1); Domain (3); Glycosylation (1); Motif (1); Signal peptide (1) FUNCTION: PPIase which accelerates the folding of proteins during protein synthesis. Has a preference for substrates containing 4-hydroxylproline modifications, including type III collagen. May also target type VI and type X collagens. {ECO:0000250|UniProtKB:Q9NWM8}. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138}. SUBUNIT: Monomer. Homodimer. Interacts with type III, type IV and type X collagens. {ECO:0000250|UniProtKB:Q9NWM8}. +Q64378 FKBP5_MOUSE Peptidyl-prolyl cis-trans isomerase FKBP5 (PPIase FKBP5) (EC 5.2.1.8) (51 kDa FK506-binding protein) (51 kDa FKBP) (FKBP-51) (FK506-binding protein 5) (FKBP-5) (Rotamase) 456 50,966 Chain (1); Domain (2); Modified residue (2); Repeat (3) FUNCTION: Immunophilin protein with PPIase and co-chaperone activities. Component of unligated steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). Plays a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors maintaining the complex into the cytoplasm when unliganded. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11751894}. Nucleus {ECO:0000269|PubMed:11751894}. SUBUNIT: Part of a heteromultimeric cytoplasmic complex with HSP90AA1, HSPA1A/HSPA1B and steroid receptors. Upon ligand binding dissociates from the complex and FKBP4 takes its place. Interacts with functionally mature heterooligomeric progesterone receptor complexes along with HSP90 and TEBP. {ECO:0000269|PubMed:11751894, ECO:0000269|PubMed:21994940}. TISSUE SPECIFICITY: Widely expressed, highest levels found in the liver, skeletal muscle, kidney and thymus. Expression is regulated during adipocyte differentiation. +O54998 FKBP7_MOUSE Peptidyl-prolyl cis-trans isomerase FKBP7 (PPIase FKBP7) (EC 5.2.1.8) (23 kDa FK506-binding protein) (23 kDa FKBP) (FKBP-23) (FK506-binding protein 7) (FKBP-7) (Rotamase) 218 24,913 Calcium binding (2); Chain (1); Domain (3); Glycosylation (2); Motif (1); Signal peptide (1) FUNCTION: PPIases accelerate the folding of proteins during protein synthesis. PTM: Glycosylated. {ECO:0000269|PubMed:9806833}. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138, ECO:0000269|PubMed:9806833}. TISSUE SPECIFICITY: Expressed at highest levels in heart, lung and testis. Weakly expressed in kidney and lymph node. Little or no expression detected in brain, thymus, spleen and liver. {ECO:0000269|PubMed:9806833}. +O35465 FKBP8_MOUSE Peptidyl-prolyl cis-trans isomerase FKBP8 (PPIase FKBP8) (EC 5.2.1.8) (38 kDa FK506-binding protein) (38 kDa FKBP) (FKBP-38) (mFKBP38) (FK506-binding protein 8) (FKBP-8) (FKBPR38) (Rotamase) 402 43,529 Alternative sequence (1); Chain (1); Compositional bias (1); Cross-link (11); Domain (1); Erroneous gene model prediction (1); Erroneous initiation (8); Modified residue (1); Repeat (3); Sequence conflict (10); Transmembrane (1) TRANSMEM 380 400 Helical. {ECO:0000255}. FUNCTION: Constitutively inactive PPiase, which becomes active when bound to calmodulin and calcium. Seems to act as a chaperone for BCL2, targets it to the mitochondria and modulates its phosphorylation state. The BCL2/FKBP8/calmodulin/calcium complex probably interferes with the binding of BCL2 to its targets. The active form of FKBP8 may therefore play a role in the regulation of apoptosis (By similarity). Required for normal embryonic development. {ECO:0000250}. PTM: Ubiquitinated by PRKN during mitophagy, leading to its degradation and enhancement of mitophagy. Deubiquitinated by USP30. {ECO:0000250|UniProtKB:Q14318}. SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000269|PubMed:15105374}; Single-pass membrane protein {ECO:0000269|PubMed:15105374}; Cytoplasmic side {ECO:0000269|PubMed:15105374}. SUBUNIT: Homomultimers or heteromultimers (Potential). Forms heterodimer with calmodulin. When activated by calmodulin and calcium, interacts with the BH4 domain of BCL2 and weakly with BCLX isoform Bcl-X(L). Does not bind and inhibit calcineurin (By similarity). Interacts with ZFYVE27; may negatively regulate ZFYVE27 phosphorylation (By similarity). {ECO:0000250, ECO:0000305}. TISSUE SPECIFICITY: Detected throughout the embryonic body, in caudal neural tube, limbs and head. Detected in adult retina, brain, heart, kidney, liver, pancreas, lung, testis and urinary bladder (at protein level). Detected in adult brain, kidney, liver, testis and trigeminal nerve, and in embryo. Detected at lower levels in lung, spleen, heart and ovary. Widely expressed in forebrain. Detected in the Purkinje cell layer in the cerebellum and in hippocampus neurons. {ECO:0000269|PubMed:10197430, ECO:0000269|PubMed:14667822, ECO:0000269|PubMed:15105374}. +P45878 FKBP2_MOUSE Peptidyl-prolyl cis-trans isomerase FKBP2 (PPIase FKBP2) (EC 5.2.1.8) (13 kDa FK506-binding protein) (13 kDa FKBP) (FKBP-13) (FK506-binding protein 2) (FKBP-2) (Immunophilin FKBP13) (Rotamase) 140 15,344 Chain (1); Domain (1); Motif (1); Signal peptide (1) FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. SUBUNIT: Interacts with ARFGEF1/BIG1 and the C-terminal of EPB41L2. {ECO:0000269|PubMed:9531554}. +Q00342 FLT3_MOUSE Receptor-type tyrosine-protein kinase FLT3 (EC 2.7.10.1) (FL cytokine receptor) (Fetal liver kinase 2) (FLK-2) (Fms-like tyrosine kinase 3) (FLT-3) (Tyrosine-protein kinase receptor flk-2) (CD antigen CD135) 1000 113,496 Active site (1); Binding site (1); Chain (1); Disulfide bond (6); Domain (2); Glycosylation (10); Modified residue (13); Mutagenesis (1); Nucleotide binding (1); Region (1); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 545 564 Helical. {ECO:0000255}. TOPO_DOM 28 544 Extracellular. {ECO:0000255}.; TOPO_DOM 565 992 Cytoplasmic. {ECO:0000255}. FUNCTION: Tyrosine-protein kinase that acts as cell-surface receptor for the cytokine FLT3LG and regulates differentiation, proliferation and survival of hematopoietic progenitor cells and of dendritic cells. Promotes phosphorylation of SHC1 and AKT1, and activation of the downstream effector MTOR. Promotes activation of RAS signaling and phosphorylation of downstream kinases, including MAPK1/ERK2 and/or MAPK3/ERK1. Promotes phosphorylation of FES, FER, PTPN6/SHP, PTPN11/SHP-2, PLCG1, and STAT5A and/or STAT5B. Activation of wild-type FLT3 causes only marginal activation of STAT5A or STAT5B. Mutations that cause constitutive kinase activity promote cell proliferation and resistance to apoptosis via the activation of multiple signaling pathways. {ECO:0000269|PubMed:18469816, ECO:0000269|PubMed:19286519, ECO:0000269|PubMed:20457904, ECO:0000269|PubMed:21516120, ECO:0000269|PubMed:8920882}. PTM: N-glycosylated, contains complex N-glycans with sialic acid. {ECO:0000250}.; PTM: Autophosphorylated on several tyrosine residues in response to FLT3LG binding. FLT3LG binding also increases phosphorylation of mutant kinases that are constitutively activated. Dephosphorylated by PTPRJ/DEP-1, PTPN1, PTPN6/SHP-1, and to a lesser degree by PTPN12. Dephosphorylation is important for export from the endoplasmic reticulum and location at the cell membrane (By similarity). {ECO:0000250}.; PTM: Rapidly ubiquitinated by UBE2L6 and the E3 ubiquitin-protein ligase SIAH1 after autophosphorylation, leading to its proteasomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. Endoplasmic reticulum lumen {ECO:0000250}. Note=Constitutively activated mutant forms with internal tandem duplications are less efficiently transported to the cell surface and a significant proportion is retained in an immature form in the endoplasmic reticulum lumen. The activated kinase is rapidly targeted for degradation (By similarity). {ECO:0000250}. SUBUNIT: Monomer in the absence of bound FLT3LG. Homodimer in the presence of bound FLT3LG. Interacts with FIZ1 following ligand activation. Interacts with FES, FER, LYN, FGR, HCK, SRC and GRB2. Interacts with PTPRJ/DEP-1 and PTPN11/SHP2 (By similarity). Interacts with RNF115 and RNF126. {ECO:0000250|UniProtKB:P36888, ECO:0000269|PubMed:23418353}. DOMAIN: The juxtamembrane autoregulatory region is important for normal regulation of the kinase activity and for maintaining the kinase in an inactive state in the absence of bound ligand. Upon tyrosine phosphorylation, it mediates interaction with the SH2 domains of numerous signaling partners. In-frame internal tandem duplications (ITDs) result in constitutive activation of the kinase. The activity of the mutant kinase can be stimulated further by FLT3LG binding (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Hematopoietic stem and progenitor cell-enriched populations. Found in brain, placenta and testis. +P97501 FMO3_MOUSE Dimethylaniline monooxygenase [N-oxide-forming] 3 (EC 1.14.13.8) (Dimethylaniline oxidase 3) (Hepatic flavin-containing monooxygenase 3) (FMO 3) (Trimethylamine monooxygenase) (EC 1.14.13.148) 534 60,516 Binding site (1); Chain (1); Modified residue (1); Nucleotide binding (5); Transmembrane (1) TRANSMEM 514 534 Helical. {ECO:0000255}. FUNCTION: Involved in the oxidative metabolism of a variety of xenobiotics such as drugs and pesticides. It N-oxygenates primary aliphatic alkylamines as well as secondary and tertiary amines. Acts on TMA to produce TMA-N-oxide. {ECO:0000269|PubMed:23177478}. SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250|UniProtKB:P32417}; Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P32417}; Single-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Liver. +P35922 FMR1_MOUSE Synaptic functional regulator FMR1 (Fragile X mental retardation protein 1 homolog) (FMRP) (Protein FMR-1) (mFmr1p) 614 68,989 Alternative sequence (9); Chain (1); Domain (4); Modified residue (12); Motif (3); Mutagenesis (4); Region (5) FUNCTION: Multifunctional polyribosome-associated RNA-binding protein that plays a central role in neuronal development and synaptic plasticity through the regulation of alternative mRNA splicing, mRNA stability, mRNA dendritic transport and postsynaptic local protein synthesis of a subset of mRNAs (PubMed:11438589, PubMed:12032354, PubMed:15475576, PubMed:16631377, PubMed:16790844, PubMed:17417632, PubMed:17548835, PubMed:18539120, PubMed:18653529, PubMed:19640847, PubMed:19166269, PubMed:20159450, PubMed:21784246, PubMed:23235829, PubMed:24813610). Plays a role in the alternative splicing of its own mRNA (PubMed:18653529). Plays a role in mRNA nuclear export (PubMed:16790844). Together with export factor NXF2, is involved in the regulation of the NXF1 mRNA stability in neurons (PubMed:17548835). Stabilizes the scaffolding postsynaptic density protein DLG4/PSD-95 and the myelin basic protein MBP mRNAs in hippocampal neurons and glial cells, respectively; this stabilization is further increased in response to metabotropic glutamate receptor (mGluR) stimulation (PubMed:17417632). Plays a role in selective delivery of a subset of dendritic mRNAs to synaptic sites in response to mGluR activation in a kinesin-dependent manner (PubMed:18539120). Plays a role as a repressor of mRNA translation during the transport of dendritic mRNAs to postnyaptic dendritic spines (PubMed:11376146, PubMed:12581522, PubMed:14570712, PubMed:12927206, PubMed:15475576, PubMed:16908410, PubMed:18805096, PubMed:19640847, PubMed:21784246, PubMed:23235829). Component of the CYFIP1-EIF4E-FMR1 complex which blocks cap-dependent mRNA translation initiation (PubMed:18805096). Represses mRNA translation by stalling ribosomal translocation during elongation (PubMed:21784246). Reports are contradictory with regards to its ability to mediate translation inhibition of (MBP) mRNA in oligodendrocytes (PubMed:14613971, PubMed:23891804). Also involved in the recruitment of the RNA helicase MOV10 to a subset of mRNAs and hence regulates microRNA (miRNA)-mediated translational repression by AGO2 (PubMed:20159450, PubMed:25464849). Facilitates the assembly of miRNAs on specific target mRNAs (By similarity). Plays also a role as an activator of mRNA translation of a subset of dendritic mRNAs at synapses (PubMed:14614133, PubMed:14613971, PubMed:15548614, PubMed:19640847, PubMed:19166269, PubMed:21490210). In response to mGluR stimulation, FMR1-target mRNAs are rapidly derepressed, allowing for local translation at synapses (PubMed:16908410, PubMed:17507556, PubMed:19640847). Binds to a large subset of dendritic mRNAs that encode a myriad of proteins involved in pre- and postsynaptic functions (PubMed:11719188, PubMed:11376146, PubMed:14613971, PubMed:17507556, PubMed:21784246, PubMed:21490210, PubMed:24349419). Binds to 5'-ACU[GU]-3' and/or 5'-[AU]GGA-3' RNA consensus sequences within mRNA targets, mainly at coding sequence (CDS) and 3'-untranslated region (UTR) and less frequently at 5'-UTR (By similarity). Binds to intramolecular G-quadruplex structures in the 5'- or 3'-UTRs of mRNA targets (PubMed:25692235). Binds to G-quadruplex structures in the 3'-UTR of its own mRNA (By similarity). Binds also to RNA ligands harboring a kissing complex (kc) structure; this binding may mediate the association of FMR1 with polyribosomes (By similarity). Binds mRNAs containing U-rich target sequences (By similarity). Binds to a triple stem-loop RNA structure, called Sod1 stem loop interacting with FMRP (SoSLIP), in the 5'-UTR region of superoxide dismutase SOD1 mRNA (PubMed:19166269). Binds to the dendritic, small non-coding brain cytoplasmic RNA 1 (BC1); which may increase the association of the CYFIP1-EIF4E-FMR1 complex to FMR1 target mRNAs at synapses (PubMed:12581522, PubMed:18805096). Associates with export factor NXF1 mRNA-containing ribonucleoprotein particles (mRNPs) in a NXF2-dependent manner (PubMed:17548835). Binds to a subset of miRNAs in the brain (PubMed:20159450). May associate with nascent transcripts in a nuclear protein NXF1-dependent manner (By similarity). In vitro, binds to RNA homopolymer; preferentially on poly(G) and to a lesser extent on poly(U), but not on poly(A) or poly(C) (By similarity). Moreover, plays a role in the modulation of the sodium-activated potassium channel KCNT1 gating activity (PubMed:20512134). Negatively regulates the voltage-dependent calcium channel current density in soma and presynaptic terminals of dorsal root ganglion (DRG) neurons, and hence regulates synaptic vesicle exocytosis (By similarity). Modulates the voltage-dependent calcium channel CACNA1B expression at the plasma membrane by targeting the channels for proteosomal degradation (PubMed:24709664). Plays a role in regulation of MAP1B-dependent microtubule dynamics during neuronal development (PubMed:15475576). Recently, has been shown to play a translation-independent role in the modulation of presynaptic action potential (AP) duration and neurotransmitter release via large-conductance calcium-activated potassium (BK) channels in hippocampal and cortical excitatory neurons (PubMed:25561520). Finally, FMR1 may be involved in the control of DNA damage response (DDR) mechanisms through the regulation of ATR-dependent signaling pathways such as histone H2AFX/H2A.x and BRCA1 phosphorylations (PubMed:24813610). {ECO:0000250|UniProtKB:Q06787, ECO:0000250|UniProtKB:Q80WE1, ECO:0000269|PubMed:11376146, ECO:0000269|PubMed:11438589, ECO:0000269|PubMed:11719188, ECO:0000269|PubMed:12032354, ECO:0000269|PubMed:12581522, ECO:0000269|PubMed:12927206, ECO:0000269|PubMed:14570712, ECO:0000269|PubMed:14613971, ECO:0000269|PubMed:14614133, ECO:0000269|PubMed:15475576, ECO:0000269|PubMed:15548614, ECO:0000269|PubMed:16631377, ECO:0000269|PubMed:16790844, ECO:0000269|PubMed:16908410, ECO:0000269|PubMed:17417632, ECO:0000269|PubMed:17507556, ECO:0000269|PubMed:17548835, ECO:0000269|PubMed:18539120, ECO:0000269|PubMed:18653529, ECO:0000269|PubMed:18805096, ECO:0000269|PubMed:19166269, ECO:0000269|PubMed:19640847, ECO:0000269|PubMed:20159450, ECO:0000269|PubMed:20512134, ECO:0000269|PubMed:21490210, ECO:0000269|PubMed:21784246, ECO:0000269|PubMed:23235829, ECO:0000269|PubMed:23891804, ECO:0000269|PubMed:24349419, ECO:0000269|PubMed:24709664, ECO:0000269|PubMed:24813610, ECO:0000269|PubMed:25561520, ECO:0000269|PubMed:25692235}. PTM: Phosphorylated on several serine residues (PubMed:14570712). Phosphorylation at Ser-499 is required for phosphorylation of other nearby serine residues (PubMed:14570712). Phosphorylation has no effect on the binding of individual mRNA species, but may affect the association with polyribosome (PubMed:14570712). Unphosphorylated FMR1 is associated with actively translating polyribosome, whereas a fraction of phosphorylated FMR1 is associated with apparently stalled polyribosome (PubMed:14570712). Dephosphorylation by an activated phosphatase may release the FMR1-mediated translational repression and allow synthesis of a locally required protein at snypases (PubMed:14570712). {ECO:0000269|PubMed:14570712}.; PTM: Monoubiquitinated (PubMed:16908410). Polyubiquitinated (PubMed:16908410). Ubiquitinated and targeted for proteasomal degradation after activation of metabotropic glutamate receptor (mGluR) (PubMed:16908410). {ECO:0000269|PubMed:16908410}.; PTM: Methylated; methylation is necessary for heterodimerization with FXR1, association with polyribosomes, recruitment into stress granules and translation of FMR1 target mRNAs. Methylated by PRMT1, PRMT3 and PRMT4, in vitro. {ECO:0000250|UniProtKB:Q06787}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16908410, ECO:0000269|PubMed:8842725, ECO:0000269|PubMed:8895584}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q06787}. Chromosome, centromere {ECO:0000269|PubMed:24813610}. Chromosome {ECO:0000269|PubMed:24813610}. Cytoplasm {ECO:0000269|PubMed:11438699, ECO:0000269|PubMed:14570712, ECO:0000269|PubMed:15317853, ECO:0000269|PubMed:16790844, ECO:0000269|PubMed:24709664, ECO:0000269|PubMed:8895584}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:11438699, ECO:0000269|PubMed:16790844, ECO:0000269|PubMed:8842725, ECO:0000269|PubMed:9285783}. Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000269|PubMed:15028757, ECO:0000269|PubMed:15312650, ECO:0000269|PubMed:15329415, ECO:0000269|PubMed:16098134, ECO:0000269|PubMed:18539120, ECO:0000269|PubMed:8842725, ECO:0000269|PubMed:9285783}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q06787}. Perikaryon {ECO:0000269|PubMed:14613971, ECO:0000269|PubMed:16908410, ECO:0000269|PubMed:18805096, ECO:0000269|PubMed:19193898}. Cell projection {ECO:0000250|UniProtKB:Q06787}. Cell projection, axon {ECO:0000269|PubMed:16631377, ECO:0000269|PubMed:19193898}. Cell projection, dendrite {ECO:0000269|PubMed:15028757, ECO:0000269|PubMed:16631377, ECO:0000269|PubMed:16908410, ECO:0000269|PubMed:18539120, ECO:0000269|PubMed:18805096, ECO:0000269|PubMed:19193898}. Cell projection, dendritic spine {ECO:0000269|PubMed:15028757, ECO:0000269|PubMed:16631377}. Cell junction, synapse, synaptosome {ECO:0000269|PubMed:18805096}. Cell projection, filopodium {ECO:0000269|PubMed:16631377}. Cell projection, growth cone {ECO:0000269|PubMed:16631377}. Cell projection, filopodium tip {ECO:0000269|PubMed:16631377}. Cell junction, synapse {ECO:0000269|PubMed:16631377}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000269|PubMed:19193898}. Cell junction, synapse, presynaptic cell membrane {ECO:0000269|PubMed:19193898}. Cell membrane {ECO:0000269|PubMed:24709664}. Note=Colocalizes with H2AFX/H2A.x in pericentromeric heterochromatin in response to DNA damaging agents (PubMed:24813610). Localizes on meiotic pachytene-stage chromosomes (PubMed:24813610). Forms nuclear foci representing sites of ongoing DNA replication in response to DNA damaging agents (PubMed:24813610). Shuttles between nucleus and cytoplasm in a XPO1/CRM1-dependent manner (PubMed:8895584, PubMed:8842725). Localizes to cytoplasmic granules, also referred to as messenger ribonucleoprotein particles or mRNPs, along dendrites and dendritic spines (PubMed:15028757, PubMed:16631377). FMR1-containing cytoplasmic granules colocalize to F-actin-rich structures, including filopodium, spines and growth cone during the development of hippocampal neurons (By similarity). FMR1-containing cytoplasmic granules are transported out of the soma along axon and dendrite to synaptic contacts in a microtubule- and kinesin-dependent manner (PubMed:15312650, PubMed:16098134, PubMed:18539120). Colocalizes with CACNA1B in the cytoplasm and at the cell membrane of neurons (PubMed:24709664). Colocalizes with CYFIP1, CYFIP2, NXF2 and ribosomes in the perinuclear region (PubMed:11438699, PubMed:16790844). Colocalizes with CYFIP1 and EIF4E in dendrites and probably at synapses (PubMed:18805096). Colocalizes with FXR1, kinesin, 60S acidic ribosomal protein RPLP0 and SMN in cytoplasmic granules in the soma and neurite cell processes (By similarity). Colocalizes with FXR1 and FXR2 in discrete granules, called fragile X granules (FXGs), along axon and presynaptic compartments (PubMed:19193898). Colocalizes with TDRD3 in cytoplasmic stress granules (SGs) in response to various cellular stress (By similarity). Interacts with SND1 (By similarity). {ECO:0000250|UniProtKB:Q06787, ECO:0000250|UniProtKB:Q80WE1, ECO:0000269|PubMed:11438699, ECO:0000269|PubMed:15028757, ECO:0000269|PubMed:15312650, ECO:0000269|PubMed:16098134, ECO:0000269|PubMed:16631377, ECO:0000269|PubMed:16790844, ECO:0000269|PubMed:18539120, ECO:0000269|PubMed:18805096, ECO:0000269|PubMed:19193898, ECO:0000269|PubMed:24709664, ECO:0000269|PubMed:24813610, ECO:0000269|PubMed:8842725, ECO:0000269|PubMed:8895584}.; SUBCELLULAR LOCATION: Isoform 4: Nucleus {ECO:0000269|PubMed:8842725}. Nucleus, nucleoplasm {ECO:0000269|PubMed:8842725}. SUBUNIT: Homodimer (By similarity). Forms heterodimer with FXR1; heterodimerization occurs in a methylation-dependent manner (By similarity). Forms heterodimer with FXR2 (By similarity). Homooligomer (By similarity). Component of the CYFIP1-EIF4E-FMR1 complex at least composed of CYFIP, EIF4E and FMR1; this mRNA cap binding complex formation increases in presence of the brain cytoplasmic RNA BC1 and is dynamically regulated in an activity-dependent manner to repress and then possibly release dendritic mRNAs for translation in response to mGluR stimulation (PubMed:18805096). Associates with the SMN core complex that contains SMN, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8 and STRAP/UNRIP (PubMed:18093976). Part of a ribonucleoprotein complex with AGO2/EIF2C2 and miRNAs (By similarity). Interacts with AGO2/EIF2C2 (By similarity). Interacts (via C-terminus) with CACNA1B; this interaction induces a deacrease in the number of presynaptic functional CACNA1B channels at the cell surface (PubMed:24709664). Interacts with CYFIP1; this interaction recruits CYFIP1 to capped mRNA (PubMed:11438699, PubMed:18805096). Interacts with CYFIP2 (PubMed:11438699). Interacts with EIF5; this interaction occurs in a RNA-dependent manner (By similarity). Interacts with dynein (PubMed:18539120). Interacts with FXR1 and FXR2 (PubMed:10567518). Interacts with methylated histone H3 (By similarity). Interacts with IGF2BP1; this interaction allows to recruit IGF2BP1 to mRNA in a FMR1-dependent manner (By similarity). Interacts (via N-terminus) with KCNMB4 (PubMed:25561520). Interacts with KCNT1 (via C-terminus); this interaction alters gating properties of KCNT1 (PubMed:20512134). Interacts (via C-terminus) with KIF5A; this interaction is increased in a mGluR-dependent manner (PubMed:18539120). Interacts (via phosphorylated form) with MCRS1 (via N-terminus) (By similarity). Interacts with MOV10; this interaction is direct, occurs in an RNA-dependent manner on polysomes and induces association of MOV10 with RNAs (PubMed:25464849). Interacts with MYO5A and PURA; these interactions occur in association with polyribosome (PubMed:12147688). Interacts with NCL (PubMed:10567518). Interacts with NUFIP1 (PubMed:10556305). Interacts (via N-terminus) with NUFIP2 (By similarity). Interacts with NXF1; this interaction occurs in a mRNA-dependent and polyribosome-independent manner in the nucleus (By similarity). Interacts with NXF2 (via N-terminus); this interaction is direct and occurs in a NXF1 mRNA-containing mRNP complexes (PubMed:16790844, PubMed:17548835). Interacts with RANBP9; this interaction is direct and inhibits binding of FMR1 to RNA homopolymer (PubMed:15381419). Interacts with RPLP0 (PubMed:21784246). Interacts (via C-terminus) with SMN (via C-terminus); this interaction is direct and occurs in a RNA-independent manner (By similarity). Interacts with TDRD3 (via C-terminus); this interaction is direct (By similarity). Interacts with YBX1; this interaction occurs in association with polyribosome (PubMed:11162447). Interacts with nucleosome (By similarity). Associates with polyribosome; this association occurs in a mRNA-dependent manner (PubMed:8842725, PubMed:9285783, PubMed:12581522, PubMed:12575950, PubMed:14613971, PubMed:15317853, PubMed:15805463, PubMed:21784246). Associates with messenger ribonucleoprotein particles (mRNPs) (PubMed:8842725, PubMed:9285783, PubMed:11719188, PubMed:12581522, PubMed:12575950, PubMed:15329415, PubMed:18805096). Associates with microtubules in a kinesin- and dynein-dependent manner (PubMed:18539120). Interacts with HABP4 (By similarity). {ECO:0000250|UniProtKB:Q06787, ECO:0000269|PubMed:10556305, ECO:0000269|PubMed:10567518, ECO:0000269|PubMed:11162447, ECO:0000269|PubMed:11438699, ECO:0000269|PubMed:11719188, ECO:0000269|PubMed:12147688, ECO:0000269|PubMed:12575950, ECO:0000269|PubMed:12581522, ECO:0000269|PubMed:14613971, ECO:0000269|PubMed:15317853, ECO:0000269|PubMed:15329415, ECO:0000269|PubMed:15381419, ECO:0000269|PubMed:15805463, ECO:0000269|PubMed:16790844, ECO:0000269|PubMed:17548835, ECO:0000269|PubMed:18093976, ECO:0000269|PubMed:18539120, ECO:0000269|PubMed:18805096, ECO:0000269|PubMed:20512134, ECO:0000269|PubMed:21784246, ECO:0000269|PubMed:24709664, ECO:0000269|PubMed:25464849, ECO:0000269|PubMed:25561520, ECO:0000269|PubMed:8842725, ECO:0000269|PubMed:9285783}. DOMAIN: The N-terminal 134 amino acids are necessary for homodimerization and RNA-binding. The N-terminal 298 amino acids are sufficient to interact with KCNMB4 and to regulate presynaptic action potential (AP) duration in neurons. The two agenet-like domains are necessary for binding to histone H3 in a methylation-dependent manner. The KH domains are necessary for mediating miRNA annealing to specific RNA targets. The KH 2 domain is necessary for binding to kissing complex (kc) RNA ligands. The RGG box domain is necessary for binding to mRNA targets that contain G-quadruplex structures. The RGG-box domain is necessary for binding to a triple stem-loop RNA structure, called Sod1 stem loop interacting with FMRP (SoSLIP), in the superoxide dismutase SOD1 mRNA. The RGG box domain is necessary for binding to its own mRNA. The RGG-box domain is necessary for binding to homopolymer poly(G). {ECO:0000250|UniProtKB:Q06787}. TISSUE SPECIFICITY: Expressed in brain (PubMed:8033209). Strongly expressed in the neonatal hippocampus (PubMed:15475576). Expressed in the brainstem (PubMed:14613971). Expressed in the cerebellum (PubMed:19193898). Expressed in neurons of hippocampal area CA3 (PubMed:17548835, PubMed:19193898). Expressed in neurons of the olfactory bulb including the granule, mitral, tufted and juxtaglomerular cells (PubMed:19193898). Expressed in both mature and immature olfactory sensory neurons (OSNs) (PubMed:19193898). Expressed in neurons in all layers and in all regions of cerebral cortex (PubMed:19193898). Expressed in mature oligodendrocytes (OLGs) (PubMed:23891804). Expressed in spermatogonia (at protein level) (PubMed:16790844). Expressed predominantly in the brain (PubMed:16000371). Expressed in testis (PubMed:8033209). {ECO:0000269|PubMed:14613971, ECO:0000269|PubMed:15475576, ECO:0000269|PubMed:16000371, ECO:0000269|PubMed:16790844, ECO:0000269|PubMed:17548835, ECO:0000269|PubMed:19193898, ECO:0000269|PubMed:23891804, ECO:0000269|PubMed:8033209}. +Q9D2H8 FNDC8_MOUSE Fibronectin type III domain-containing protein 8 321 35,619 Alternative sequence (1); Chain (1); Domain (1); Sequence conflict (1) +Q9ER35 FN3K_MOUSE Fructosamine-3-kinase (EC 2.7.1.-) 309 35,032 Chain (1); Frameshift (1); Modified residue (1) FUNCTION: May initiate a process leading to the deglycation of fructoselysine and of glycated proteins. May play a role in the phosphorylation of 1-deoxy-1-morpholinofructose (DMF), fructoselysine, fructoseglycine, fructose and glycated lysozyme (By similarity). {ECO:0000250}. +Q8K2I1 FNTB_MOUSE Protein farnesyltransferase subunit beta (FTase-beta) (EC 2.5.1.58) (CAAX farnesyltransferase subunit beta) (Ras proteins prenyltransferase subunit beta) 437 48,820 Beta strand (4); Chain (1); Helix (22); Metal binding (3); Modified residue (2); Region (3); Repeat (5); Site (1); Turn (3) FUNCTION: Essential subunit of the farnesyltransferase complex. Catalyzes the transfer of a farnesyl moiety from farnesyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. {ECO:0000269|PubMed:21520375}. SUBUNIT: Heterodimer of FNTA and FNTB. {ECO:0000269|PubMed:21520375}. +A2AKG8 FOCAD_MOUSE Focadhesin 1798 198,950 Alternative sequence (3); Chain (1); Compositional bias (1); Erroneous initiation (2); Modified residue (1); Sequence conflict (7); Transmembrane (2) TRANSMEM 441 461 Helical. {ECO:0000255}.; TRANSMEM 1033 1053 Helical. {ECO:0000255}. FUNCTION: Potential tumor suppressor in gliomas. {ECO:0000269|PubMed:22427331}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cell junction, focal adhesion. Note=Colocalizes with VCL in astrocytes. {ECO:0000250}. SUBUNIT: Interacts with VCL. {ECO:0000250}. TISSUE SPECIFICITY: Expressed by glial and neuronal cells in brain. {ECO:0000269|PubMed:22427331}. +Q9QZ59 DMRT1_MOUSE Doublesex- and mab-3-related transcription factor 1 374 39,444 Alternative sequence (3); Chain (1); Compositional bias (1); DNA binding (1); Modified residue (1); Sequence conflict (3) FUNCTION: Transcription factor that plays a key role in male sex determination and differentiation by controlling testis development and male germ cell proliferation. Plays a central role in spermatogonia by inhibiting meiosis in undifferentiated spermatogonia and promoting mitosis, leading to spermatogonial development and allowing abundant and continuous production of sperm. Acts both as a transcription repressor and activator: prevents meiosis by restricting retinoic acid (RA)-dependent transcription and repressing STRA8 expression and promotes spermatogonial development by activating spermatogonial differentiation genes, such as SOHLH1. Also plays a key role in postnatal sex maintenance by maintaining testis determination and preventing feminization: represses transcription of female promoting genes such as FOXL2 and activates male-specific genes. May act as a tumor suppressor. May also play a minor role in oogenesis. {ECO:0000269|PubMed:11040213, ECO:0000269|PubMed:17540358, ECO:0000269|PubMed:20007774, ECO:0000269|PubMed:20616082, ECO:0000269|PubMed:20951351, ECO:0000269|PubMed:21621532, ECO:0000269|PubMed:21775990}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00070, ECO:0000269|PubMed:11040213}. TISSUE SPECIFICITY: Testis-specific. In adult testis, expressed in Sertoli cells in all regions of the seminiferous tubules. Expressed dynamically in premeiotic germ cells (spermatogonia), with high expression only in regions of the seminiferous tubule that are early in the spermatogenic cycle (at protein level). Expressed in all mitotic spermatogonia. Expression decreases with the onset of spermatogonial differentiation and disappears at the initiation of meiosis. {ECO:0000269|PubMed:11040213, ECO:0000269|PubMed:20951351}. +Q9JI44 DMAP1_MOUSE DNA methyltransferase 1-associated protein 1 (DNMAP1) (DNMT1-associated protein 1) (MAT1-mediated transcriptional repressor) 468 53,130 Alternative sequence (2); Chain (1); Coiled coil (1); Compositional bias (2); Cross-link (2); Domain (1); Modified residue (2) FUNCTION: Involved in transcription repression and activation. Its interaction with HDAC2 may provide a mechanism for histone deacetylation in heterochromatin following replication of DNA at late firing origins. Can also repress transcription independently of histone deacetylase activity. May specifically potentiate DAXX-mediated repression of glucocorticoid receptor-dependent transcription. Component of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Participates in the nuclear localization of URI1 and increases its transcriptional corepressor activity (By similarity). {ECO:0000250, ECO:0000269|PubMed:14978102}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm {ECO:0000250}. Note=Targeted to replication foci throughout S phase by DNMT1. SUBUNIT: Component of the NuA4 histone acetyltransferase complex which contains the catalytic subunit KAT5/TIP60 and the subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6. Component of a NuA4-related complex which contains EP400, TRRAP/PAF400, SRCAP, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, actin, ACTL6A/BAF53A, VPS72 and YEATS4/GAS41. DMAP1 also forms a complex with DNMT1 and HDAC2. Throughout S phase it interacts directly with the N-terminus of DNMT1, which serves to recruit DMAP1 to replication foci. DMAP1 interacts with ING1, a component of the mSIN3A transcription repressor complex, although this interaction is not required for recruitment of ING1 to heterochromatin. Interacts directly with the transcriptional corepressor TSG101. Interacts with URI1 (By similarity). Interacts with the pro-apoptotic protein DAXX. {ECO:0000250, ECO:0000269|PubMed:14978102}. +O55188 DMP1_MOUSE Dentin matrix acidic phosphoprotein 1 (DMP-1) (Dentin matrix protein 1) (AG1) 503 53,965 Chain (1); Compositional bias (1); Glycosylation (3); Motif (1); Sequence conflict (27); Signal peptide (1) FUNCTION: May have a dual function during osteoblast differentiation. In the nucleus of undifferentiated osteoblasts, unphosphorylated form acts as a transcriptional component for activation of osteoblast-specific genes like osteocalcin. During the osteoblast to osteocyte transition phase it is phosphorylated and exported into the extracellular matrix, where it regulates nucleation of hydroxyapatite (By similarity). {ECO:0000250}. PTM: Phosphorylated in the cytosol and extracellular matrix and unphosphorylated in the nucleus. Phosphorylation is necessary for nucleocytoplasmic transport and may be catalyzed by a nuclear isoform of CK2 and can be augmented by calcium. Phosphorylated (in vitro) by FAM20C in the extracellular medium at sites within the S-x-E/pS motif (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Secreted, extracellular space, extracellular matrix {ECO:0000250}. Note=In proliferating preosteoblasts it is nuclear, during early maturation stage is cytoplasmic and in mature osteoblast localizes in the mineralized matrix. Export from the nucleus of differentiating osteoblast is triggered by the release of calcium from intracellular stores followed by a massive influx of this pool of calcium into the nucleus (By similarity). {ECO:0000250}. SUBUNIT: Interacts with importin alpha. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in tooth particularly in odontoblast, ameloblast and cementoblast. Also expressed in bone particularly in osteoblast. +Q8BG36 DMRT2_MOUSE Doublesex- and mab-3-related transcription factor 2 (Doublesex-like 2 protein) (Terra) 561 61,641 Chain (1); Compositional bias (1); DNA binding (1); Erroneous initiation (1); Frameshift (2); Sequence caution (1); Sequence conflict (10) FUNCTION: Transcriptional activator that directly regulates early activation of the myogenic determination gene MYF5 by binding in a sequence-specific manner to the early epaxial enhancer element of it. Involved in somitogenesis during embryogenesis and somite development and differentiation into sclerotome and dermomyotome. Required for the initiation and/or maintenance of proper organization of the sclerotome, dermomyotome and myotome. Is not required for sex determination and/or differentiation in embryonic development. Also not involved in symmetric somite formation and hence does not regulate the laterality pathway that controls left-right asymmetric organ positioning. {ECO:0000269|PubMed:10021344, ECO:0000269|PubMed:16387292, ECO:0000269|PubMed:17605809, ECO:0000269|PubMed:20368965, ECO:0000269|PubMed:21203428}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00070, ECO:0000269|PubMed:17605809}. SUBUNIT: Homodimer. {ECO:0000269|PubMed:17605809}. TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:12609607, ECO:0000269|PubMed:20368965}. +Q922Y0 DYRK3_MOUSE Dual specificity tyrosine-phosphorylation-regulated kinase 3 (EC 2.7.12.1) 586 65,572 Active site (1); Binding site (1); Chain (1); Domain (1); Modified residue (1); Motif (1); Mutagenesis (5); Nucleotide binding (2); Region (1) FUNCTION: Dual-specificity protein kinase that promotes disassembly of several types of membraneless organelles during mitosis, such as stress granules, nuclear speckles and pericentriolar material (By similarity). Dual-specificity tyrosine-regulated kinases (DYRKs) autophosphorylate a critical tyrosine residue in their activation loop and phosphorylate their substrate on serine and threonine residues (PubMed:12356771). Acts as a central dissolvase of membraneless organelles during the G2-to-M transition, after the nuclear-envelope breakdown: acts by mediating phosphorylation of multiple serine and threonine residues in unstructured domains of proteins, such as SRRM1 and PCM1 (By similarity). Does not mediate disassembly of all membraneless organelles: disassembly of P-body and nucleolus is not regulated by DYRK3 (By similarity). Dissolution of membraneless organelles at the onset of mitosis is also required to release mitotic regulators, such as ZNF207, from liquid-unmixed organelles where they are sequestered and keep them dissolved during mitosis (By similarity). Regulates mTORC1 by mediating the dissolution of stress granules: during stressful conditions, DYRK3 partitions from the cytosol to the stress granule, together with mTORC1 components, which prevents mTORC1 signaling (By similarity). When stress signals are gone, the kinase activity of DYRK3 is required for the dissolution of stress granule and mTORC1 relocation to the cytosol: acts by mediating the phosphorylation of the mTORC1 inhibitor AKT1S1, allowing full reactivation of mTORC1 signaling (By similarity). Also acts as a negative regulator of EPO-dependent erythropoiesis: may place an upper limit on red cell production during stress erythropoiesis (By similarity). Inhibits cell death due to cytokine withdrawal in hematopoietic progenitor cells (By similarity). Promotes cell survival upon genotoxic stress through phosphorylation of SIRT1: this in turn inhibits p53/TP53 activity and apoptosis (PubMed:20167603). {ECO:0000250|UniProtKB:O43781, ECO:0000269|PubMed:12356771, ECO:0000269|PubMed:20167603}. PTM: Ubiquitinated at anaphase by the anaphase-promoting complex (APC/C), leading to its degradation by the proteasome. {ECO:0000250|UniProtKB:O43781}.; PTM: Protein kinase activity is activated following autophosphorylation at Tyr-368. {ECO:0000269|PubMed:12356771}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O43781}. Cytoplasm {ECO:0000250|UniProtKB:O43781}. Nucleus speckle {ECO:0000250|UniProtKB:O43781}. Cytoplasmic granule {ECO:0000250|UniProtKB:O43781}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:O43781}. Note=Associates with membraneless organelles in the cytoplasm and nucleus. Shuttles between cytoplasm and stress granules. Localized predominantly on distinct speckles distributed throughout the cytoplasm of the cell. At low concentration, showns a homogeneous distribution throughout the cytoplasm and does not condense in speckles. During oxidative and osmotic stress, localizes to stress granules. {ECO:0000250|UniProtKB:O43781}. SUBUNIT: Interacts with SIRT1. {ECO:0000269|PubMed:20167603}. DOMAIN: The N-terminal domain, which is intrinsically disordered, is required for stress granule localization. {ECO:0000250|UniProtKB:O43781}. +Q8BI55 DYRK4_MOUSE Dual specificity tyrosine-phosphorylation-regulated kinase 4 (EC 2.7.12.1) 632 72,561 Active site (1); Alternative sequence (2); Binding site (1); Chain (1); Domain (1); Modified residue (1); Nucleotide binding (2); Sequence conflict (1) FUNCTION: Possible non-essential role in spermiogenesis. {ECO:0000269|PubMed:17292540}. PTM: Autophosphorylation on Tyr-379 in the activation loop is required for kinase activity. {ECO:0000250|UniProtKB:Q9NR20}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NR20}. TISSUE SPECIFICITY: Highly expressed in testes. {ECO:0000269|PubMed:17292540}. +P62880 GBB2_MOUSE Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-2 (G protein subunit beta-2) (Transducin beta chain 2) 340 37,331 Chain (1); Initiator methionine (1); Modified residue (2); Repeat (7); Sequence conflict (2) FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}. SUBUNIT: G proteins are composed of 3 units, alpha, beta and gamma. Interacts with ARHGEF18 and RASD2. Interacts with ATXN10. Interacts with SCN8A. {ECO:0000250|UniProtKB:P62879}. +P39054 DYN2_MOUSE Dynamin-2 (EC 3.6.5.5) (Dynamin UDNM) 870 98,145 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (3); Modified residue (6); Mutagenesis (1); Nucleotide binding (3); Region (5); Sequence conflict (2) FUNCTION: Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP. Plays a role in the regulation of neuron morphology, axon growth and formation of neuronal growth cones (By similarity). Plays an important role in vesicular trafficking processes, in particular endocytosis. Involved in cytokinesis (PubMed:18923138). Regulates maturation of apoptotic cell corpse-containing phagosomes by recruiting PIK3C3 to the phagosome membrane (PubMed:18425118). {ECO:0000250|UniProtKB:P39052, ECO:0000269|PubMed:18425118, ECO:0000269|PubMed:18923138}. PTM: Phosphorylation at Ser-764 by CDK1 is greatly increased upon mitotic entry. It regulates cytokinesis downstream of calcineurin, and does not affect clathrin-mediated endocytosis. Dephosphorylated by calcineurin/PP2 (By similarity). Phosphorylated on tyrosine residues after activation of SRC (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P39052}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P50570}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P50570}. Cell junction {ECO:0000250|UniProtKB:P39052}. Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:P39052}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250|UniProtKB:P50570}. Cell junction, synapse {ECO:0000250|UniProtKB:P50570}. Midbody {ECO:0000250|UniProtKB:P50570}. Cell projection, phagocytic cup {ECO:0000269|PubMed:18425118}. Cytoplasmic vesicle, phagosome membrane {ECO:0000269|PubMed:18425118}; Peripheral membrane protein {ECO:0000269|PubMed:18425118}. Note=Colocalizes with CTTN at the basis of filopodia in hippocampus neuron growth zones. Microtubule-associated. Also found in the postsynaptic density of neuronal cells (By similarity). Co-localizes with PIK3C3 and RAB5A to the nascent phagosome (PubMed:18425118). {ECO:0000250|UniProtKB:P39052, ECO:0000250|UniProtKB:P50570, ECO:0000269|PubMed:18425118}. SUBUNIT: Interacts with SHANK1, SHANK2 and NOSTRIN. Interacts with SNX9. Interacts with SNX33 (via SH3 domain). Interacts with MYO1E (via SH3 domain). Interacts with CTTN and ACTN1 (By similarity). Interacts with MYOF and SH3BP4 (PubMed:17702744, PubMed:16325581). Interacts with PSTPIP1. Interacts with CTNND2 (By similarity). May interact with PIK3C3 (PubMed:18425118). May be a component of a complex composed of RAB5A (in GDP-bound form), DYN2 and PIK3C3 (PubMed:18425118). Interacts with BIN1 (By similarity). {ECO:0000250|UniProtKB:P39052, ECO:0000250|UniProtKB:P50570, ECO:0000269|PubMed:16325581, ECO:0000269|PubMed:17702744, ECO:0000305|PubMed:18425118}. TISSUE SPECIFICITY: Expressed in most tissues during embryonic development, including the peripheral nervous system although no expression is evident in skeletal muscle or heart. {ECO:0000269|PubMed:23092955}. +Q61211 EIF2D_MOUSE Eukaryotic translation initiation factor 2D (eIF2D) (Ligatin) 570 62,830 Alternative sequence (1); Chain (1); Domain (2); Frameshift (1); Modified residue (4); Sequence conflict (10) FUNCTION: Translation initiation factor that is able to deliver tRNA to the P-site of the eukaryotic ribosome in a GTP-independent manner. The binding of Met-tRNA(I) occurs after the AUG codon finds its position in the P-site of 40S ribosomes, the situation that takes place during initiation complex formation on some specific RNAs. Its activity in tRNA binding with 40S subunits does not require the presence of the aminoacyl moiety. Possesses the unique ability to deliver non-Met (elongator) tRNAs into the P-site of the 40S subunit. In addition to its role in initiation, can promote release of deacylated tRNA and mRNA from recycled 40S subunits following ABCE1-mediated dissociation of post-termination ribosomal complexes into subunits (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +Q9D4V0 EKI1_MOUSE Ethanolamine kinase 1 (EKI 1) (EC 2.7.1.82) 363 41,984 Chain (1); Sequence conflict (2) Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from ethanolamine: step 1/3. FUNCTION: Highly specific for ethanolamine phosphorylation. May be a rate-controlling step in phosphatidylathanolamine biosynthesis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +O08856 ELL_MOUSE RNA polymerase II elongation factor ELL (Eleven-nineteen lysine-rich leukemia protein) 602 67,146 Chain (1); Initiator methionine (1); Modified residue (4); Sequence conflict (3) FUNCTION: Elongation factor component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. Specifically required for stimulating the elongation step of RNA polymerase II- and III-dependent snRNA gene transcription. ELL also plays an early role before its assembly into in the SEC complex by stabilizing RNA polymerase II recruitment/initiation and entry into the pause site. Required to stabilize the pre-initiation complex and early elongation. Specifically required for stimulating the elongation step of RNA polymerase II- and III-dependent snRNA gene transcription (By similarity). Elongation factor component of the little elongation complex (LEC), a complex required to regulate small nuclear RNA (snRNA) gene transcription by RNA polymerase II and III (PubMed:22195968). {ECO:0000250, ECO:0000269|PubMed:22195968}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P55199}. Nucleus speckle {ECO:0000250|UniProtKB:P55199}. Nucleus, Cajal body {ECO:0000250|UniProtKB:P55199}. Note=Colocalizes with EAF2 to nuclear speckles. Colocalizes with coilin in subnuclear cajal and histone locus bodies. Translocates in the LEC complex to cajal and histone locus bodies at snRNA genes in a ICE1-dependent manner. Associates to transcriptionally active chromatin at snRNA genes (By similarity). {ECO:0000250|UniProtKB:P55199}. SUBUNIT: Component of the super elongation complex (SEC), at least composed of EAF1, EAF2, CDK9, MLLT3/AF9, AFF (AFF1 or AFF4), the P-TEFb complex and ELL (ELL, ELL2 or ELL3). Component of the little elongation complex (LEC), at least composed of ELL (ELL, ELL2 or ELL3), ZC3H8, ICE1 and ICE2. Interacts with ICE1 (via N-terminus domain). Interacts with ICE2. Interacts with AFF4; the interaction is direct. Interacts with EAF1 and EAF2 (By similarity). Interacts with USPL1 (By similarity). {ECO:0000250|UniProtKB:P55199}. +Q9CZX0 ELP3_MOUSE Elongator complex protein 3 (EC 2.3.1.48) 547 62,385 Alternative sequence (1); Chain (1); Domain (1); Metal binding (3); Modified residue (2) FUNCTION: Catalytic histone acetyltransferase subunit of the RNA polymerase II elongator complex, which is a component of the RNA polymerase II (Pol II) holoenzyme and is involved in transcriptional elongation. Elongator may play a role in chromatin remodeling and is involved in acetylation of histones H3 and probably H4. Involved in acetylation of alpha-tubulin (By similarity). May also have a methyltransferase activity. Involved in cell migration. Involved in neurogenesis. Regulates the migration and branching of projection neurons in the developing cerebral cortex, through a process depending on alpha-tubulin acetylation (PubMed:19185337). {ECO:0000250|UniProtKB:Q9H9T3, ECO:0000269|PubMed:19185337, ECO:0000269|PubMed:22854966}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19185337}. Nucleus {ECO:0000250|UniProtKB:Q9H9T3}. SUBUNIT: Component of the RNA polymerase II elongator complex (Elongator), which consists of ELP1, STIP1/ELP2, ELP3, ELP4, ELP5 and ELP6. ELP1, STIP1/ELP2 and ELP3 form the Elongator core complex. Elongator associates with the C-terminal domain (CTD) of Pol II largest subunit. Interacts with ELP1 (By similarity). Interacts with alpha-tubulin (By similarity). {ECO:0000250|UniProtKB:Q9H9T3}. +P62869 ELOB_MOUSE Elongin-B (EloB) (Elongin 18 kDa subunit) (RNA polymerase II transcription factor SIII subunit B) (SIII p18) (Transcription elongation factor B polypeptide 2) 118 13,170 Beta strand (4); Chain (1); Domain (1); Helix (4); Modified residue (4); Turn (1) Protein modification; protein ubiquitination. FUNCTION: SIII, also known as elongin, is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. Subunit A is transcriptionally active and its transcription activity is strongly enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex) (By similarity). In embryonic stem cells, the elongin BC complex is recruited by EPOP to Polycomb group (PcG) target genes in order generate genomic region that display both active and repressive chromatin properties, an important feature of pluripotent stem cells (PubMed:27863225, PubMed:27863226). {ECO:0000250|UniProtKB:Q15370, ECO:0000269|PubMed:27863225, ECO:0000269|PubMed:27863226}.; FUNCTION: The elongin BC complex seems to be involved as an adapter protein in the proteasomal degradation of target proteins via different E3 ubiquitin ligase complexes, including the von Hippel-Lindau ubiquitination complex CBC(VHL). By binding to BC-box motifs it seems to link target recruitment subunits, like VHL and members of the SOCS box family, to Cullin/RBX1 modules that activate E2 ubiquitination enzymes. {ECO:0000250|UniProtKB:Q15370}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Heterotrimer of an A (ELOA, ELOA2 or ELOA3), ELOB and ELOC subunit (PubMed:16498413). The elongin BC complex interacts with EPOP; leading to recruit the elongin BC complex to Polycomb group (PcG) target genes, thereby restricting excessive activity of the PRC2/EED-EZH2 complex (PubMed:27863225, PubMed:27863226). Part of E3 ubiquitin ligase complexes with CUL5 or CUL2, RBX1 and a substrate adapter protein that can be either SOCS1, SOCS5, ELOA, VHL or WSB1. Interacts with VHL. Found in a complex composed of LIMD1, VHL, EGLN1/PHD2, ELOB and CUL2. Interacts with SPSB1. Interacts with KLHDC10; which may be an E3 ubiquitin ligase complex substrate recognition component. {ECO:0000269|PubMed:10051596, ECO:0000269|PubMed:11384984, ECO:0000269|PubMed:16498413, ECO:0000269|PubMed:27863225, ECO:0000269|PubMed:27863226}. +Q8BGF6 ELMD2_MOUSE ELMO domain-containing protein 2 293 34,747 Chain (1); Domain (1); Sequence conflict (2) FUNCTION: Acts as a GTPase-activating protein (GAP) toward guanine nucleotide exchange factors like ARL2, ARL3, ARF1 and ARF6, but not for GTPases outside the Arf family. +P21995 EMB_MOUSE Embigin (Teratocarcinoma glycoprotein Gp-70) 330 37,064 Chain (1); Disulfide bond (2); Domain (2); Glycosylation (9); Modified residue (1); Sequence conflict (5); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 255 283 Helical. {ECO:0000255}. TOPO_DOM 34 254 Extracellular. {ECO:0000255}.; TOPO_DOM 284 330 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a role in targeting the monocarboxylate transporters SLC16A1 and SLC16A7 to the cell membrane (By similarity). Plays a role in the outgrowth of motoneurons and in the formation of neuromuscular junctions. Following muscle denervation, promotes nerve terminal sprouting and the formation of additional acetylcholine receptor clusters at synaptic sites without affecting terminal Schwann cell number or morphology. Delays the retraction of terminal sprouts following re-innervation of denervated endplates. {ECO:0000250, ECO:0000269|PubMed:19164284}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O88775}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:O88775}. Cell junction, synapse {ECO:0000269|PubMed:19164284}. Note=Localizes to the neuromuscular junctions. {ECO:0000269|PubMed:19164284}. SUBUNIT: Interacts with SLC16A1 and SLC16A7. {ECO:0000250}. TISSUE SPECIFICITY: Only member of the immunoglobulin superfamily to be expressed in embryonal carcinoma cells, which resemble multipotential cells of early embryos. {ECO:0000269|PubMed:2963822}. +Q8C2S5 FBXL5_MOUSE F-box/LRR-repeat protein 5 (F-box and leucine-rich repeat protein 5) 690 77,894 Alternative sequence (5); Chain (1); Domain (1); Metal binding (9); Region (1); Repeat (7); Sequence conflict (2) Protein modification; protein ubiquitination. FUNCTION: Component of some SCF (SKP1-cullin-F-box) protein ligase complex that plays a central role in iron homeostasis by promoting the ubiquitination and subsequent degradation of IREB2/IRP2. Upon high iron and oxygen level, it specifically recognizes and binds IREB2/IRP2, promoting its ubiquitination and degradation by the proteasome. Promotes ubiquitination and subsequent degradation of DCTN1/p150-glued (By similarity). {ECO:0000250}. PTM: Ubiquitinated upon iron and oxygen depletion, leading to its degradation by the proteasome. Ubiquitination is regulated by the hemerythrin-like region that acts as an oxygen and iron sensor (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}. SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex. Interacts with ACO1, IREB2/IRP2; the interaction depends on the 4Fe-4S cluster. Interacts with DCTN1/p150-glued (By similarity). {ECO:0000250}. DOMAIN: The hemerythrin-like region acts as an oxygen and iron sensor by binding oxygen through a diiron metal-center. In absence of oxygen and iron, the protein is ubiquitinated and degraded (By similarity). {ECO:0000250}. +Q923Z4 FER3L_MOUSE Fer3-like protein (Basic helix-loop-helix protein N-twist) (Nephew of atonal 3) (Neuronal twist) 168 19,463 Chain (1); Compositional bias (1); Domain (1) FUNCTION: Transcription factor that binds to the E-box and functions as inhibitor of transcription. DNA binding requires dimerization with an E protein. Inhibits transcription activation by ASCL1/MASH1 by sequestering E proteins. {ECO:0000269|PubMed:12217327}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Heterodimer with TCF3/E12. Interacts with the bHLH domain of TCF3/E12. {ECO:0000269|PubMed:12217327}. TISSUE SPECIFICITY: Detected in the developing central nervous system, in particular in embryonic ventral neural tube, brain, and spinal cord. Detected in embryonic intestine. Detected in embryonic and adult thalamus, hypothalamus, midbrain, pons and medulla. {ECO:0000269|PubMed:11472856, ECO:0000269|PubMed:12217327}. +P30416 FKBP4_MOUSE Peptidyl-prolyl cis-trans isomerase FKBP4 (PPIase FKBP4) (EC 5.2.1.8) (52 kDa FK506-binding protein) (52 kDa FKBP) (FKBP-52) (59 kDa immunophilin) (p59) (FK506-binding protein 4) (FKBP-4) (FKBP59) (HSP-binding immunophilin) (HBI) (Immunophilin FKBP52) (Rotamase) [Cleaved into: Peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processed] 458 51,572 Chain (2); Cross-link (1); Domain (2); Erroneous initiation (1); Frameshift (1); Initiator methionine (1); Modified residue (8); Region (1); Repeat (3); Sequence conflict (7) FUNCTION: Immunophilin protein with PPIase and co-chaperone activities. Component of steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). May play a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors between cytoplasm and nuclear compartments. The isomerase activity controls neuronal growth cones via regulation of TRPC1 channel opening. Acts also as a regulator of microtubule dynamics by inhibiting MAPT/TAU ability to promote microtubule assembly. May have a protective role against oxidative stress in mitochondria. {ECO:0000269|PubMed:11278753, ECO:0000269|PubMed:11751894, ECO:0000269|PubMed:8341706}. PTM: Phosphorylation by CK2 results in loss of HSP90 binding activity. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:11751894}. Mitochondrion {ECO:0000250|UniProtKB:Q02790}. Nucleus {ECO:0000269|PubMed:11751894, ECO:0000269|PubMed:8341706}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Shuttles from mitochondria to nucleus; co-localizes in mitochondria with the glucocorticoid receptor. Colocalized with MAPT/TAU in the distal part of the primary cortical neurons. {ECO:0000250|UniProtKB:Q02790, ECO:0000250|UniProtKB:Q9QVC8}. SUBUNIT: Homodimer (By similarity). Interacts with GLMN (By similarity). Associates with HSP90AA1 and HSPA1A/HSPA1B in steroid hormone receptor complexes. Also interacts with peroxisomal phytanoyl-CoA alpha-hydroxylase (PHYH). Interacts with NR3C1 and dynein. Interacts with HSF1 in the HSP90 complex. Associates with tubulin. Interacts with MAPT/TAU (By similarity). Interacts (via TPR domain) with S100A1, S100A2 and S100A6; the interaction is Ca(2+) dependent. Interaction with S100A1 and S100A2 (but not with S100A6) leads to inhibition of FKBP4-HSP90 interaction. Interacts with dynein; contributes to NR3C1 transport to the nucleus. {ECO:0000250, ECO:0000250|UniProtKB:Q02790, ECO:0000250|UniProtKB:Q9QVC8, ECO:0000269|PubMed:11278753, ECO:0000269|PubMed:11751894, ECO:0000269|PubMed:9195923}. DOMAIN: The PPIase activity is mainly due to the first PPIase FKBP-type domain (1-138 AA). {ECO:0000250}.; DOMAIN: The C-terminal region (AA 375-458) is required to prevent tubulin polymerization. {ECO:0000250}.; DOMAIN: The chaperone activity resides in the C-terminal region, mainly between amino acids 264 and 400. {ECO:0000250}.; DOMAIN: The TPR repeats mediate mitochondrial localization. {ECO:0000250}. +Q6P9Q6 FKB15_MOUSE FK506-binding protein 15 (FKBP-15) (133 kDa FK506-binding protein) (133 kDa FKBP) (FKBP-133) (WASP and FKBP-like) (WAFL) 1216 132,961 Alternative sequence (1); Chain (1); Coiled coil (2); Compositional bias (3); Domain (1); Modified residue (20); Region (1); Sequence conflict (1) FUNCTION: Involved in the transport of early endosomes at the level of transition between microfilament-based and microtubule-based movement (By similarity). May be involved in the cytoskeletal organization of neuronal growth cones. Seems to be inactive as a PPIase. {ECO:0000250, ECO:0000269|PubMed:16756961}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16756961}. Cell projection, axon {ECO:0000269|PubMed:16756961}. Early endosome {ECO:0000269|PubMed:16756961}. Note=Present in axons and neuronal growth cones. {ECO:0000269|PubMed:16756961}. SUBUNIT: Interacts with WIP and actin (By similarity). Interacts with TBC1D23 (PubMed:29084197). {ECO:0000250|UniProtKB:Q5T1M5, ECO:0000269|PubMed:29084197}. DOMAIN: The PPIase FKBP-type domain seems to be inactive both for FK506-binding and enzymatic activity.; DOMAIN: The central coiled-coil region is responsible for association with early endosomes. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain, with highest levels in the granular cell layer of cerebellum and in the granule cell layer of dentate gyrus. {ECO:0000269|PubMed:16756961}. +Q8R507 FKTN_MOUSE Fukutin (EC 2.4.2.-) (Fukuyama-type congenital muscular dystrophy protein) (Ribitol-5-phosphate transferase) 461 53,579 Chain (1); Glycosylation (1); Region (1); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 8 28 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 7 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 29 461 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Catalyzes the transfer of CDP-ribitol to the distal N-acetylgalactosamine of the phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-3-N-acetylglucosamine-beta-4-(phosphate-6-)mannose), a carbohydrate structure present in alpha-dystroglycan (DAG1) (PubMed:12471058). This constitutes the first step in the formation of the ribitol 5-phosphate tandem repeat which links the phosphorylated O-mannosyl trisaccharide to the ligand binding moiety composed of repeats of 3-xylosyl-alpha-1,3-glucuronic acid-beta-1 (By similarity). Required for normal location of POMGNT1 in Golgi membranes, and for normal POMGNT1 activity (PubMed:19017726). May interact with and reinforce a large complex encompassing the outside and inside of muscle membranes (PubMed:19017726, PubMed:22922256). Could be involved in brain development (Probable). {ECO:0000250|UniProtKB:O75072, ECO:0000269|PubMed:12471058, ECO:0000269|PubMed:19017726, ECO:0000269|PubMed:22922256, ECO:0000305|PubMed:12670716}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:12471058}; Single-pass type II membrane protein {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:29416295}. Nucleus {ECO:0000269|PubMed:29416295}. Endoplasmic reticulum {ECO:0000305|PubMed:29416295}. Note=In retinal tissue, does not localize with the Golgi apparatus. {ECO:0000269|PubMed:29416295}. SUBUNIT: Forms a complex composed of FKTN/fukutin, FKRP and RXYLT1/TMEM5 (By similarity). Interacts (via transmembrane domain) with POMGNT1; the interaction is direct and is required for normal POMGNT1 location in Golgi membranes (By similarity). {ECO:0000250|UniProtKB:O75072}. TISSUE SPECIFICITY: Expressed in the retina, with highest levels found in the inner segments of photoreceptors and the outer plexiform layer (at protein level) (PubMed:29416295). Expressed at lower levels in the inner and outer nuclear layers, the inner plexiform layers, and the ganglion cell layers of the retina (at protein level) (PubMed:29416295). Expressed in the heart, brain, spleen, lung, liver, skeletal muscle, kidney and testis (PubMed:12471058, PubMed:12408965). {ECO:0000269|PubMed:12408965, ECO:0000269|PubMed:12471058, ECO:0000269|PubMed:29416295}. +Q8BLU0 FLRT2_MOUSE Leucine-rich repeat transmembrane protein FLRT2 (Fibronectin leucine rich transmembrane protein 2) 660 73,948 Beta strand (16); Chain (1); Disulfide bond (4); Domain (3); Glycosylation (1); Helix (7); Mutagenesis (5); Repeat (10); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (8) TRANSMEM 541 561 Helical. {ECO:0000255}. TOPO_DOM 36 540 Extracellular. {ECO:0000305}.; TOPO_DOM 562 660 Cytoplasmic. {ECO:0000305}. FUNCTION: Functions in cell-cell adhesion, cell migration and axon guidance. Mediates cell-cell adhesion via its interactions with ADGRL3 and probably also other latrophilins that are expressed at the surface of adjacent cells (PubMed:21350012, PubMed:25728924 PubMed:25374360). May play a role in the migration of cortical neurons during brain development via its interaction with UNC5D (PubMed:21673655). Mediates axon growth cone collapse and plays a repulsive role in neuron guidance via its interaction with UNC5D, and possibly also other UNC-5 family members (PubMed:21673655, PubMed:25728924). Plays a role in fibroblast growth factor-mediated signaling cascades (PubMed:16872596). Required for normal organization of the cardiac basement membrane during embryogenesis, and for normal embryonic epicardium and heart morphogenesis (PubMed:21350012). {ECO:0000269|PubMed:16872596, ECO:0000269|PubMed:21350012, ECO:0000269|PubMed:21673655, ECO:0000269|PubMed:25374360, ECO:0000269|PubMed:25728924}. PTM: N-glycosylated. {ECO:0000269|PubMed:16872596, ECO:0000269|PubMed:21673655}.; PTM: Proteolytic cleavage in the juxtamembrane region gives rise to a soluble ectodomain. Cleavage is probably effected by a metalloprotease. {ECO:0000269|PubMed:21673655}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16872596, ECO:0000269|PubMed:22405201, ECO:0000269|PubMed:24585683, ECO:0000269|PubMed:25374360}; Single-pass membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000305|PubMed:16872596, ECO:0000305|PubMed:24585683}. Cell junction, focal adhesion {ECO:0000269|PubMed:16872596}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:24585683}. Cell junction, synapse, synaptosome {ECO:0000250|UniProtKB:D3ZTV3}. Microsome membrane {ECO:0000269|PubMed:24585683}. Secreted {ECO:0000269|PubMed:21673655}. Note=Proteolytic cleavage gives rise to a shedded ectodomain. {ECO:0000269|PubMed:21673655}. SUBUNIT: Self-associates (via leucine-rich repeats), giving rise to homooligomers (PubMed:25374360). Interacts with FGFR1 (PubMed:16872596). Interacts with FGFR2 (PubMed:21765038). Interacts (via extracellular domain) with ADGRL1/LPHN1 (PubMed:22405201). Interacts (via extracellular domain) with ADGRL3 (via olfactomedin-like domain)(PubMed:22405201, PubMed:25728924). Interacts (via extracellular domain) with UNC5D (via the first Ig-like domain) (PubMed:21673655, PubMed:25374360). Can also interact (via extracellular domain) with UNC5B, but with much lower affinity (PubMed:21673655). Interacts (via extracellular domain) with FN1 (PubMed:24585683). {ECO:0000269|PubMed:16872596, ECO:0000269|PubMed:21673655, ECO:0000269|PubMed:21765038, ECO:0000269|PubMed:22405201, ECO:0000269|PubMed:24585683, ECO:0000269|PubMed:25374360, ECO:0000269|PubMed:25728924}. TISSUE SPECIFICITY: Detected in adult brain (at protein level). {ECO:0000269|PubMed:21350012}. +Q6ZPF4 FMNL3_MOUSE Formin-like protein 3 1028 117,169 Alternative sequence (2); Beta strand (3); Chain (1); Compositional bias (1); Domain (3); Erroneous initiation (1); Helix (16); Initiator methionine (1); Lipidation (1); Modified residue (3); Turn (4) FUNCTION: Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration. Required for developmental angiogenesis. In this process, required for microtubule reorganization and for efficient endothelial cell elongation. In quiescent endothelial cells, triggers rearrangement of the actin cytoskeleton, but does not alter microtubule alignement. {ECO:0000250|UniProtKB:Q6NXC0, ECO:0000250|UniProtKB:Q8IVF7}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8IVF7}. Cell membrane {ECO:0000250|UniProtKB:Q8IVF7}; Lipid-anchor {ECO:0000255}. Note=Enriched in lamellipodia. {ECO:0000250|UniProtKB:Q8IVF7}. SUBUNIT: Interacts with SRGAP2 (via SH3 domain). {ECO:0000269|PubMed:21148482}. DOMAIN: The DAD domain regulates activation via by an autoinhibitory interaction with the GBD/FH3 domain. This autoinhibition is released upon competitive binding of an activated GTPase. The release of DAD allows the FH2 domain to then nucleate and elongate nonbranched actin filaments (By similarity). {ECO:0000250}. +Q6P8X9 FLTOP_MOUSE Protein Flattop (Cilia- and flagella-associated protein 126) 189 20,550 Chain (1); Frameshift (1) FUNCTION: Acts as a regulator of cilium basal body docking and positioning in mono- and multiciliated cells. Regulates basal body docking and cilia formation in multiciliated lung cells. Regulates kinocilium positioning and stereocilia bundle morphogenesis in the inner ear. {ECO:0000269|PubMed:25296022}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:25296022}. Cell projection, cilium {ECO:0000269|PubMed:25296022}. Apical cell membrane {ECO:0000269|PubMed:25296022}. Note=Localizes to the apical cell membrane, the basal body and the primary cilium in monociliated node cells. {ECO:0000269|PubMed:25296022}. SUBUNIT: Interacts with DLG3. {ECO:0000269|PubMed:25296022}. TISSUE SPECIFICITY: Expressed in mono- and multiciliated tissues during planar cell polarity acquisition. {ECO:0000269|PubMed:22153975, ECO:0000269|PubMed:25296022}. +B2RXV4 FLVC1_MOUSE Feline leukemia virus subgroup C receptor-related protein 1 (Feline leukemia virus subgroup C receptor) (Major facilitator superfamily domain containing 7B) (Mfsd7b) 560 60,469 Alternative sequence (1); Chain (1); Glycosylation (1); Modified residue (1); Topological domain (13); Transmembrane (12) TRANSMEM 101 121 Helical. {ECO:0000255}.; TRANSMEM 141 161 Helical. {ECO:0000255}.; TRANSMEM 168 188 Helical. {ECO:0000255}.; TRANSMEM 193 213 Helical. {ECO:0000255}.; TRANSMEM 234 254 Helical. {ECO:0000255}.; TRANSMEM 281 301 Helical. {ECO:0000255}.; TRANSMEM 337 357 Helical. {ECO:0000255}.; TRANSMEM 378 398 Helical. {ECO:0000255}.; TRANSMEM 407 427 Helical. {ECO:0000255}.; TRANSMEM 430 450 Helical. {ECO:0000255}.; TRANSMEM 465 485 Helical. {ECO:0000255}.; TRANSMEM 497 517 Helical. {ECO:0000255}. TOPO_DOM 1 100 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 122 140 Extracellular. {ECO:0000255}.; TOPO_DOM 162 167 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 189 192 Extracellular. {ECO:0000255}.; TOPO_DOM 214 233 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 255 280 Extracellular. {ECO:0000255}.; TOPO_DOM 302 336 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 358 377 Extracellular. {ECO:0000255}.; TOPO_DOM 399 406 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 428 429 Extracellular. {ECO:0000255}.; TOPO_DOM 451 464 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 486 496 Extracellular. {ECO:0000255}.; TOPO_DOM 518 560 Cytoplasmic. {ECO:0000255}. FUNCTION: Isoform 1: Heme transporter that exports cytoplasmic heme. It can also export coproporphyrin and protoporphyrin IX, which are both intermediate products in the heme biosynthetic pathway. Does not export bilirubin. Heme export depends on the presence of HPX and is required to maintain intracellular free heme balance, protecting cells from heme toxicity. Heme export provides protection from heme or ferrous iron toxicities in liver, brain, sensory neurons and during erythtopoiesis, a process in which heme synthesis intensifies. Causes susceptibility to FeLV-C in vitro. {ECO:0000250|UniProtKB:Q9Y5Y0, ECO:0000269|PubMed:18258918}.; FUNCTION: Isoform 2: Heme transporter that promotes heme efflux from the mitochondrion to the cytoplasm. Essential for erythroid differentiation. PTM: N-Glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Isoform 1: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 2: Mitochondrion membrane {ECO:0000269|PubMed:23187127}; Multi-pass membrane protein {ECO:0000269|PubMed:23187127}. SUBUNIT: Interacts with HPX. {ECO:0000250}. +A2AED3 FNDC7_MOUSE Fibronectin type III domain-containing protein 7 737 78,141 Alternative sequence (4); Chain (1); Domain (8); Erroneous gene model prediction (2); Frameshift (1); Glycosylation (2); Sequence conflict (4); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q8BJN4 FNDC9_MOUSE Fibronectin type III domain-containing protein 9 226 25,656 Chain (1); Domain (1); Transmembrane (1) TRANSMEM 113 133 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q68FD7 FNIP1_MOUSE Folliculin-interacting protein 1 1165 130,126 Chain (1); Compositional bias (1); Domain (3); Erroneous initiation (2); Modified residue (9); Region (1) FUNCTION: Acts as a co-chaperone of HSP90AA1. Inhibits the ATPase activity of HSP90AA1 leading to reduction in its chaperone activity. Facilitates the binding of client protein FLCN to HSP90AA1. Competes with the activating co-chaperone AHSA1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins. May be involved in energy and/or nutrient sensing through the AMPK and mTOR signaling pathways. May regulate phosphorylation of RPS6KB1. {ECO:0000250|UniProtKB:Q8TF40}. PTM: Phosphorylated by AMPK. {ECO:0000250|UniProtKB:Q8TF40}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8TF40}. Note=Colocalizes with FLCN in the cytoplasm. {ECO:0000250|UniProtKB:Q8TF40}. SUBUNIT: Homodimer and homomultimer. Heterodimer and heteromultimer with FNIP2. Interacts with FLCN (via C-terminus). Interacts with HSPCA and with the PRKAA1, PRKAB1 and PRKAG1 subunits of 5'-AMP-activated protein kinase (AMPK). Phosphorylated FLCN and AMPK are preferentially bound. Interacts with HSP70, STIP1, PTGES3, CDC37, BRAF, GCR and CDK4. Interacts with HSP90AA1; the interaction inhibits HSP90AA1 ATPase activity. {ECO:0000250|UniProtKB:Q8TF40}. +P35846 FOLR1_MOUSE Folate receptor alpha (FR-alpha) (Folate receptor 1) (Folate-binding protein 1) 255 29,449 Binding site (3); Chain (1); Disulfide bond (8); Glycosylation (3); Lipidation (1); Propeptide (1); Region (2); Sequence conflict (1); Signal peptide (1) FUNCTION: Binds to folate and reduced folic acid derivatives and mediates delivery of 5-methyltetrahydrofolate and folate analogs into the interior of cells. Has high affinity for folate and folic acid analogs at neutral pH. Exposure to slightly acidic pH after receptor endocytosis triggers a conformation change that strongly reduces its affinity for folates and mediates their release. Required for normal embryonic development and normal cell proliferation. Required for renal folate reabsorption. {ECO:0000269|PubMed:10508523, ECO:0000269|PubMed:12854656, ECO:0000269|PubMed:15259034, ECO:0000269|PubMed:15703271, ECO:0000269|PubMed:17286298, ECO:0000269|PubMed:1894617}. PTM: The secreted form is derived from the membrane-bound form either by cleavage of the GPI anchor, or/and by proteolysis catalyzed by a metalloprotease. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. Secreted {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250}. Endosome {ECO:0000250}. Apical cell membrane. Note=Endocytosed into cytoplasmic vesicles and then recycled to the cell membrane (By similarity). Detected at proximal tubule apical membranes. {ECO:0000250}. TISSUE SPECIFICITY: Detected in kidney proximal tubules (at protein level). {ECO:0000269|PubMed:15703271}. +Q61572 FOXC1_MOUSE Forkhead box protein C1 (Forkhead-related protein FKHL7) (Forkhead-related transcription factor 3) (FREAC-3) (Mesoderm/mesenchyme forkhead 1) (MF-1) (Transcription factor FKH-1) 553 56,940 Chain (1); Compositional bias (8); DNA binding (1); Modified residue (5); Motif (2); Mutagenesis (8); Region (3); Sequence conflict (2) FUNCTION: DNA-binding transcriptional factor that plays a role in a broad range of cellular and developmental processes such as eye, bones, cardiovascular, kidney and skin development (PubMed:9635428, PubMed:9106663, PubMed:10479458, PubMed:10395790, PubMed:11562355, PubMed:18187037, PubMed:19668217, PubMed:22493429, PubMed:24590069, PubMed:25808752, PubMed:28223138). Acts either as a transcriptional activator or repressor (PubMed:28223138). Binds to the consensus binding site 5'-[G/C][A/T]AAA[T/C]AA[A/C]-3' in promoter of target genes (PubMed:25808752). Upon DNA-binding, promotes DNA bending. Acts as a transcriptional coactivator (PubMed:25808752). Stimulates Indian hedgehog (Ihh)-induced target gene expression mediated by the transcription factor GLI2, and hence regulates endochondral ossification (PubMed:25808752). Acts also as a transcriptional coregulator by increasing DNA-binding capacity of GLI2 in breast cancer cells. Regulates FOXO1 through binding to a conserved element, 5'-GTAAACAAA-3' in its promoter region, implicating FOXC1 as an important regulator of cell viability and resistance to oxidative stress in the eye (By similarity). Cooperates with transcription factor FOXC2 in regulating expression of genes that maintain podocyte integrity (PubMed:28223138). Promotes cell growth inhibition by stopping the cell cycle in the G1 phase through TGFB1-mediated signals. Involved in epithelial-mesenchymal transition (EMT) induction by increasing cell proliferation, migration and invasion (By similarity). Involved in chemokine CXCL12-induced endothelial cell migration through the control of CXCR4 expression (PubMed:18187037). Plays a role in the gene regulatory network essential for epidermal keratinocyte terminal differentiation (By similarity). Essential developmental transcriptional factor required for mesoderm-derived tissues formation, such as the somites, skin, bone and cartilage (PubMed:9106663, PubMed:10479458, PubMed:10395790, PubMed:10704385, PubMed:11562355, PubMed:15196959). Positively regulates CXCL12 and stem cell factor expression in bone marrow mesenchymal progenitor cells, and hence plays a role in the development and maintenance of mesenchymal niches for haematopoietic stem and progenitor cells (HSPC) (PubMed:24590069). Plays a role in corneal transparency by preventing both blood vessel and lymphatic vessel growth during embryonic development in a VEGF-dependent manner (PubMed:22171010). May function as a tumor suppressor (By similarity). {ECO:0000250|UniProtKB:Q12948, ECO:0000269|PubMed:10395790, ECO:0000269|PubMed:10479458, ECO:0000269|PubMed:10704385, ECO:0000269|PubMed:11562355, ECO:0000269|PubMed:15196959, ECO:0000269|PubMed:18187037, ECO:0000269|PubMed:19668217, ECO:0000269|PubMed:22171010, ECO:0000269|PubMed:22493429, ECO:0000269|PubMed:24590069, ECO:0000269|PubMed:25808752, ECO:0000269|PubMed:28223138, ECO:0000269|PubMed:9106663, ECO:0000269|PubMed:9635428}. PTM: Phosphorylated (PubMed:22493429). Phosphorylated on Ser-274 in response to epidermal growth factor (EGF) in a ERK1/2 MAPK-dependent signaling pathway; phosphorylation contributes to its protein stability and transcriptional regulatory activity (By similarity). {ECO:0000250|UniProtKB:Q12948, ECO:0000269|PubMed:22493429}.; PTM: Sumoylated preferentially with SUMO2 or SUMO3. Desumoylated by SENP2. {ECO:0000269|PubMed:22493429}.; PTM: Ubiquitinated, leading to its proteasomal degradation. {ECO:0000250|UniProtKB:Q12948}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11562355, ECO:0000269|PubMed:22493429, ECO:0000269|PubMed:25808752}. Note=Colocalizes with PITX2 in the nucleus at subnuclear chromatin regions. Colocalizes with CBX5 to a heterochromatin-rich region of the nucleus (By similarity). Colocalizes with GLI2 in the nucleus (PubMed:25808752). {ECO:0000250|UniProtKB:Q12948, ECO:0000269|PubMed:25808752}. SUBUNIT: Monomer. Interacts with C1QBP (By similarity). Interacts (via N-terminus) with GLI2 (via C-terminal internal region); this interaction is direct and increases GLI2 DNA-binding and transcriptional activity through a smoothened (SMO)-independent Hedgehog (Hh) signaling pathway (PubMed:26565916, PubMed:25808752). Interacts (via C-terminus domain) with PITX2 (via homeobox domain) (By similarity). Interacts with FLNA and PBX1 (By similarity). {ECO:0000250|UniProtKB:Q12948, ECO:0000269|PubMed:25808752, ECO:0000269|PubMed:26565916}. TISSUE SPECIFICITY: Expressed in glomerular epithelial cells, the podocytes (PubMed:28223138). Expressed in a population of adipo-osteogenic progenitor cells, termed CXCL12-abundant reticular (CAR) cells (at protein level) (PubMed:24590069). Expressed in many embryonic tissues, including prechondrogenic mesenchyme, periocular mesenchyme, meninges, endothelial cells and kidney (PubMed:9767123). Detected in adult brain, heart, kidney, adrenal gland, lung and testis, with lower levels in stomach, spleen and thymus (PubMed:9767123). Expressed in endothelial cells (PubMed:18187037). Expressed in the mesenchyme adjacent to the developing cerebellum (PubMed:19668217). Expressed in the sternum and rib cartilage (PubMed:25808752). Expressed in growth plate chondrocytes (PubMed:25808752). {ECO:0000269|PubMed:18187037, ECO:0000269|PubMed:19668217, ECO:0000269|PubMed:24590069, ECO:0000269|PubMed:25808752, ECO:0000269|PubMed:28223138, ECO:0000269|PubMed:9767123}. +Q66JX5 FR1OP_MOUSE FGFR1 oncogene partner 399 42,758 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (1); Modified residue (7); Natural variant (1) FUNCTION: Required for anchoring microtubules to the centrosomes. Required for ciliation. {ECO:0000250|UniProtKB:O95684}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:O95684}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:O95684}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:O95684}. Note=Associated with gamma-tubulin. Localizes on both mother and daughter centrioles. Localizes to an axial position on the mother centriole. Localizes to the distal end of the centriole partly to the subdistal appendage region. {ECO:0000250|UniProtKB:O95684}. SUBUNIT: Homodimer. Part of a ternary complex that contains CEP350, FGFR1OP and MAPRE1. Interacts directly with CEP350 and MAPRE1. Interacts with CEP19. Interacts (via N-terminus) with CEP350 (via C-terminus). {ECO:0000250|UniProtKB:O95684}. +Q80T14 FRAS1_MOUSE Extracellular matrix protein FRAS1 4010 442,369 Chain (1); Domain (11); Erroneous termination (1); Frameshift (1); Glycosylation (16); Modified residue (1); Repeat (26); Sequence conflict (24); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 3904 3924 Helical. {ECO:0000255}. TOPO_DOM 26 3903 Extracellular. {ECO:0000255}.; TOPO_DOM 3925 4010 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}; Extracellular side {ECO:0000305}. DOMAIN: The Calx-beta domains bind calcium with high affinity and undergo a major conformational shift upon binding. {ECO:0000250}. TISSUE SPECIFICITY: Found in a linear fashion underlying the epidermis and the basal surface of other epithelia in embryos. {ECO:0000269|PubMed:12766770}. DISEASE: Note=Defects in Fras1 are the cause of blebbed (bl) phenotype, which is characterized by blister formation, syndactyly, eyelid fusion and renal agenesis. Subepidermal blisters are predominantly formed in the head region around the eyes and at the distal part of the limbs. As development proceeds blisters that are initially transparent gradually become hemorrhagic and embryos die between E14.5 and E16.5. {ECO:0000269|PubMed:12766769, ECO:0000269|PubMed:12766770}. +Q8C180 FRS2_MOUSE Fibroblast growth factor receptor substrate 2 (FGFR substrate 2) (FGFR-signaling adaptor SNT) (FRS2-alpha) (Suc1-associated neurotrophic factor target 1) (SNT-1) 508 56,794 Chain (1); Domain (1); Initiator methionine (1); Lipidation (1); Modified residue (10); Mutagenesis (6) FUNCTION: Adapter protein that links activated FGR and NGF receptors to downstream signaling pathways. Plays an important role in the activation of MAP kinases and in the phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, in response to ligand-mediated activation of FGFR1. Modulates signaling via SHC1 by competing for a common binding site on NTRK1. {ECO:0000269|PubMed:11353842, ECO:0000269|PubMed:11390647, ECO:0000269|PubMed:12181353, ECO:0000269|PubMed:9182757, ECO:0000269|PubMed:9632781}. PTM: Phosphorylated on tyrosine residues upon stimulation by FGF2 or NGFB. Phosphorylated by ULK2 (in vitro). Phosphorylated on tyrosine residues by activated ALK and FGFR1. Phosphorylated on tyrosine residues upon activation of FGFR2 and FGFR3. Phosphorylated on threonine residues by MAP kinases; this inhibits tyrosine phosphorylation, and thereby down-regulates FRS2-mediated activation of MAP kinases.; PTM: Ubiquitinated when tyrosine phosphorylated and in a complex with GRB2. The unphosphorylated form is not subject to ubiquitination. {ECO:0000269|PubMed:11997436}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:8780727}; Lipid-anchor {ECO:0000269|PubMed:8780727}. SUBUNIT: Part of a complex containing FRS2, GRB2, GAB1, PIK3R1 and SOS1. Part of a complex containing GRB2 and CBL. Binds ALK, CKS2, FGFR1, RET, MAPK1/ERK2, MAPK3/ERK1 and SRC. The tyrosine-phosphorylated protein binds the SH2 domains of GRB2 and PTPN11. Interacts with NTRK1, NTRK2 and NTRK3 (phosphorylated upon ligand-binding) (By similarity). Identified in a complex containing FGFR4, NCAM1, CDH2, PLCG1, FRS2, SRC, SHC1, GAP43 and CTTN. {ECO:0000250, ECO:0000269|PubMed:10629055, ECO:0000269|PubMed:11353842, ECO:0000269|PubMed:11390647, ECO:0000269|PubMed:11433297, ECO:0000269|PubMed:11997436, ECO:0000269|PubMed:12181353, ECO:0000269|PubMed:8780727, ECO:0000269|PubMed:9182757, ECO:0000269|PubMed:9632781}. TISSUE SPECIFICITY: Ubiquitous. Expression is highest in brain, kidney, lung and testis. {ECO:0000269|PubMed:9182757}. +Q6P5H6 FRMD5_MOUSE FERM domain-containing protein 5 517 58,583 Alternative sequence (4); Chain (1); Domain (1); Modified residue (1); Region (1) FUNCTION: May be involved in regulation of cell migration. May regulate cell-matrix interactions via its interaction with ITGB5 and modifying ITGB5 cytoplasmic tail interactions such as with FERMT2 and TLN1. May regulate ROCK1 kinase activity possibly involved in regulation of actin stress fiber formation. {ECO:0000250|UniProtKB:Q7Z6J6}. SUBCELLULAR LOCATION: Cell junction, adherens junction {ECO:0000250|UniProtKB:Q7Z6J6}. SUBUNIT: Interacts with CTNND1, ITGB5 (via cytoplasmic domain) and ROCK1. {ECO:0000250|UniProtKB:Q7Z6J6}. +P35378 FSHR_MOUSE Follicle-stimulating hormone receptor (FSH-R) (Follitropin receptor) 692 77,769 Chain (1); Disulfide bond (7); Domain (1); Glycosylation (3); Modified residue (1); Repeat (9); Sequence conflict (1); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 366 386 Helical; Name=1. {ECO:0000255}.; TRANSMEM 398 420 Helical; Name=2. {ECO:0000255}.; TRANSMEM 443 464 Helical; Name=3. {ECO:0000255}.; TRANSMEM 485 507 Helical; Name=4. {ECO:0000255}.; TRANSMEM 528 549 Helical; Name=5. {ECO:0000255}.; TRANSMEM 573 596 Helical; Name=6. {ECO:0000255}.; TRANSMEM 608 629 Helical; Name=7. {ECO:0000255}. TOPO_DOM 18 365 Extracellular. {ECO:0000255}.; TOPO_DOM 387 397 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 421 442 Extracellular. {ECO:0000255}.; TOPO_DOM 465 484 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 508 527 Extracellular. {ECO:0000255}.; TOPO_DOM 550 572 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 597 607 Extracellular. {ECO:0000255}.; TOPO_DOM 630 692 Cytoplasmic. {ECO:0000255}. FUNCTION: G protein-coupled receptor for follitropin, the follicle-stimulating hormone. Through cAMP production activates the downstream PI3K-AKT and ERK1/ERK2 signaling pathways. {ECO:0000250|UniProtKB:P23945}. PTM: N-glycosylated; indirectly required for FSH-binding, possibly via a conformational change that allows high affinity binding of hormone. {ECO:0000250|UniProtKB:P20395}.; PTM: Sulfated. {ECO:0000250|UniProtKB:P23945}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P23945}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P23945}. SUBUNIT: Homotrimer. Functions as a homotrimer binding the FSH hormone heterodimer composed of CGA and FSHB (By similarity). Interacts with ARRB2 (By similarity). {ECO:0000250|UniProtKB:P20395, ECO:0000250|UniProtKB:P23945}. +Q78JE5 FBX22_MOUSE F-box only protein 22 402 44,203 Chain (1); Domain (1); Erroneous initiation (1); Modified residue (2) FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. Promotes the proteasome-dependent degradation of key sarcomeric proteins, such as alpha-actinin (ACTN2) and filamin-C (FLNC), essential for maintenance of normal contractile function. {ECO:0000269|PubMed:22972877}. SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:22972877}. SUBUNIT: Directly interacts with SKP1 and CUL1. {ECO:0000250}. +Q9D2Y6 FBX25_MOUSE F-box only protein 25 357 41,826 Chain (1); Domain (1); Region (1); Sequence conflict (1) Protein modification; protein ubiquitination. FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. May play a role in accumulation of expanded polyglutamine (polyQ) protein huntingtin (HTT). {ECO:0000269|PubMed:16714087, ECO:0000269|PubMed:18287534}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16714087, ECO:0000269|PubMed:18287534}. Note=In the nucleus, associates with a specific and novel subnuclear dot-like structure. Colocalized with SKP1. SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex consisting of FBXO25, SKP1, CUL1 and RBX1. Interacts directly with SKP1 and CUL1. Interacts (via C-terminus) with beta-actin (via N-terminus) (By similarity). {ECO:0000250}. DOMAIN: The F-box is necessary for the interaction with SKP1. TISSUE SPECIFICITY: Expressed in all tissues tested, except striated muscle (at protein level). Expressed predominantly in the cerebral cortex, the hippocampus and the Purkinje cell layer of the brain. Intestine and kidney show also significant levels. {ECO:0000269|PubMed:16278047, ECO:0000269|PubMed:16714087, ECO:0000269|PubMed:18287534}. +Q8BMI0 FBX38_MOUSE F-box only protein 38 (Modulator of KLF7 activity) (MoKA) 1194 133,928 Chain (1); Compositional bias (1); Domain (1); Modified residue (6); Region (1); Sequence conflict (6) FUNCTION: Probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. May coactivate KLF7, but does not seem to promote KLF7 ubiquitination. {ECO:0000269|PubMed:14729953}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14729953}. Nucleus {ECO:0000269|PubMed:14729953}. SUBUNIT: Interacts with KLF7. Part of a SCF (SKP1-cullin-F-box) protein ligase complex (By similarity). {ECO:0000250}. DOMAIN: The N-terminal region aa 1-349 seems to be involved in cytoplasmic localization.; DOMAIN: The C-terminal region aa 473-1194 seems to be involved in nuclear localization. TISSUE SPECIFICITY: Expressed at high levels in embryo (developing brain, spinal chord, branchial arms and limbs). Widely expressed at low levels in adult tissues, with highest expression in testis. Expressed in postmeiotic spermatids. {ECO:0000269|PubMed:14729953}. +P08508 FCGR3_MOUSE Low affinity immunoglobulin gamma Fc region receptor III (IgG Fc receptor III) (Fc-gamma RIII) (FcRIII) (CD antigen CD16) 261 30,036 Chain (1); Disulfide bond (2); Domain (2); Glycosylation (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 216 235 Helical. {ECO:0000255}. TOPO_DOM 31 215 Extracellular. {ECO:0000255}.; TOPO_DOM 236 261 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for the Fc region of complexed immunoglobulins gamma. Low affinity receptor which binds to IgG1, IgG2a and IgG2b (PubMed:17558411). Mediates neutrophil activation by IgG complexes redundantly with Fcgr4 (PubMed:18097064). {ECO:0000269|PubMed:17558411, ECO:0000269|PubMed:18097064}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17558411}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Interacts with INPP5D/SHIP1. {ECO:0000269|PubMed:12393695}. +Q8BK26 FBX44_MOUSE F-box only protein 44 (F-box only protein 6a) 255 29,723 Alternative sequence (2); Chain (1); Domain (2) FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. {ECO:0000250}. SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex. Interacts with SKP1 and CUL1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain, liver, pancreas and adipose tissue (at protein level). Widely expressed. {ECO:0000269|PubMed:18203720}. +A2A6H3 FBX47_MOUSE F-box only protein 47 451 51,374 Chain (1); Domain (1) FUNCTION: Probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. {ECO:0000250}. SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex. {ECO:0000250}. +Q8CEF1 FEM1C_MOUSE Protein fem-1 homolog C (FEM1c) (FEM1-gamma) 617 68,578 Chain (1); Modified residue (1); Repeat (11); Sequence conflict (3) Protein modification; protein ubiquitination. FUNCTION: Probable component of an E3 ubiquitin-protein ligase complex, in which it may act as a substrate recognition subunit. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Component of some E3 ubiquitin-protein ligase complex. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in testis. {ECO:0000269|PubMed:14527725}. +P39749 FEN1_MOUSE Flap endonuclease 1 (FEN-1) (EC 3.1.-.-) (Flap structure-specific endonuclease 1) 378 42,315 Binding site (5); Chain (1); Metal binding (7); Modified residue (14); Region (3) FUNCTION: Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a genome stabilization factor that prevents flaps from equilibrating into structurs that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA, and exhibits RNase H activity. Also involved in replication and repair of rDNA and in repairing mitochondrial DNA. {ECO:0000255|HAMAP-Rule:MF_03140, ECO:0000269|PubMed:7926735}. PTM: Acetylated by EP300. Acetylation inhibits both endonuclease and exonuclease activity. Acetylation also reduces DNA-binding activity but does not affect interaction with PCNA or EP300. {ECO:0000255|HAMAP-Rule:MF_03140}.; PTM: Phosphorylation upon DNA damage induces relocalization to the nuclear plasma. Phosphorylation at Ser-185 by CDK2 occurs during late S-phase and results in dissociation from PCNA. {ECO:0000255|HAMAP-Rule:MF_03140}.; PTM: Methylation at Arg-190 by PRMT5 impedes Ser-185 phosphorylation and increases interaction with PCNA. {ECO:0000255|HAMAP-Rule:MF_03140}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000255|HAMAP-Rule:MF_03140}. Nucleus, nucleoplasm {ECO:0000255|HAMAP-Rule:MF_03140}. Mitochondrion. Note=Resides mostly in the nucleoli and relocalizes to the nucleoplasm upon DNA damage. {ECO:0000255|HAMAP-Rule:MF_03140}. SUBUNIT: Three molecules of FEN1 bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity. The C-terminal domain binds EP300; can bind simultaneously to both PCNA and EP300. Interacts with PCNA; can bind simultaneously to both PCNA and EP300. Interacts with DDX11; this interaction is direct and increases flap endonuclease activity of FEN1. {ECO:0000250|UniProtKB:P39748, ECO:0000255|HAMAP-Rule:MF_03140}. +Q9CRA9 FGOP2_MOUSE FGFR1 oncogene partner 2 homolog 253 29,374 Alternative sequence (1); Chain (1); Coiled coil (2); Modified residue (1); Sequence conflict (2) FUNCTION: May be involved in wound healing pathway. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +Q91ZT5 FGD4_MOUSE FYVE, RhoGEF and PH domain-containing protein 4 (Actin filament-binding protein frabin) (FGD1-related F-actin-binding protein) 766 86,541 Alternative sequence (5); Chain (1); Domain (3); Modified residue (2); Region (1); Sequence conflict (3); Zinc finger (1) FUNCTION: Activates CDC42, a member of the Ras-like family of Rho- and Rac proteins, by exchanging bound GDP for free GTP. Activates MAPK8 (By similarity). Plays a role in regulating the actin cytoskeleton and cell shape. Promotes the formation of lamellipodia. {ECO:0000250, ECO:0000269|PubMed:10871857, ECO:0000269|PubMed:11527409}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell projection, filopodium {ECO:0000250}. Note=Concentrated in filopodia and poorly detected at lamellipodia. Binds along the sides of actin fibers (By similarity). {ECO:0000250}. SUBUNIT: Homooligomer. {ECO:0000250}. DOMAIN: The part of the protein spanning the actin filament-binding domain together with the DH domain and the first PH domain is necessary and sufficient for microspike formation. Activation of MAPK8 requires the presence of all domains with the exception of the actin filament-binding domain (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Detected in thymus, lung, heart, skeletal muscle, small intestine, liver, kidney, spleen and testis. Expressed in all parts of the brain and in the spinal cord at embryonic, postnatal, and adult stages. Levels of expression are lower in postnatal and adult tissues than in embryonic tissues. {ECO:0000269|PubMed:11527409, ECO:0000269|PubMed:17564959}. +P11403 FGF4_MOUSE Fibroblast growth factor 4 (FGF-4) (Heparin-binding growth factor 4) (HBGF-4) (K-fibroblast growth factor) 202 21,919 Chain (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Plays an important role in the regulation of embryonic development, cell proliferation, and cell differentiation. Is essential for survival of the postimplantation mouse embryo. Required for normal limb and cardiac valve development during embryogenesis. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. SUBUNIT: Interacts with FGFR1, FGFR2, FGFR3 and FGFR4. Affinity between fibroblast growth factors (FGFs) and their receptors is increased by heparan sulfate glycosaminoglycans that function as coreceptors (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the blastocyst inner cell mass and later in distinct embryonic tissues. +Q9JI19 FIBP_MOUSE Acidic fibroblast growth factor intracellular-binding protein (aFGF intracellular-binding protein) (FGF-1 intracellular-binding protein) 357 41,204 Chain (1); Initiator methionine (1); Modified residue (1) FUNCTION: May be involved in mitogenic function of FGF1 (By similarity). May mediate with IER2 FGF-signaling in the establishment of laterality in the embryo (By similarity). {ECO:0000250|UniProtKB:O43427, ECO:0000250|UniProtKB:Q6T938}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O43427}. Endomembrane system {ECO:0000250|UniProtKB:O43427}; Peripheral membrane protein {ECO:0000250}. Note=Also associated with cytoplasmic membranes, particularly of mitochondria. {ECO:0000250|UniProtKB:O43427}. SUBUNIT: Binds to internalized FGF1; this interaction is increased in the presence of CSNKB, suggesting a possible cooperative interaction between CSNKB and FIBP in binding to FGF1. {ECO:0000250|UniProtKB:O43427}. +Q9JJC9 HERP2_MOUSE Homocysteine-responsive endoplasmic reticulum-resident ubiquitin-like domain member 2 protein 404 44,501 Chain (1); Compositional bias (1); Domain (1); Sequence conflict (3); Transmembrane (1) TRANSMEM 301 321 Helical. {ECO:0000255}. FUNCTION: Could be involved in the unfolded protein response (UPR) pathway. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +P37237 FGF8_MOUSE Fibroblast growth factor 8 (FGF-8) (Androgen-induced growth factor) (AIGF) (Heparin-binding growth factor 8) (HBGF-8) 268 30,420 Alternative sequence (2); Chain (1); Glycosylation (2); Modified residue (1); Signal peptide (1) FUNCTION: Plays an important role in the regulation of embryonic development, cell proliferation, cell differentiation and cell migration. Required for normal brain, eye, ear and limb development during embryogenesis. Required for normal development of the gonadotropin-releasing hormone (GnRH) neuronal system. Plays a role in neurite outgrowth in hippocampal cells (By similarity). Cooperates with Wnt-1 in mouse mammary tumor virus-induced murine mammary tumorigenesis (PubMed:7884899). {ECO:0000250|UniProtKB:P55075, ECO:0000269|PubMed:7884899}. PTM: The N-terminus is blocked. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Monomer. Homodimer. Interacts with FGFR1, FGFR2, FGFR3 and FGFR4. Affinity between fibroblast growth factors (FGFs) and their receptors is increased by heparan sulfate glycosaminoglycans that function as coreceptors (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Absent in normal mammary glands and detected only in adult testis and ovary and in midgestational embryos. +Q8VCM7 FIBG_MOUSE Fibrinogen gamma chain 436 49,391 Chain (1); Cross-link (2); Disulfide bond (8); Domain (1); Glycosylation (1); Metal binding (3); Modified residue (1); Mutagenesis (1); Signal peptide (1) FUNCTION: Together with fibrinogen alpha (FGA) and fibrinogen beta (FGB), polymerizes to form an insoluble fibrin matrix (By similarity). Fibrin has a major function in hemostasis as one of the primary components of blood clots (By similarity). In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization (By similarity). Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo (By similarity). Enhances expression of SELP in activated platelets via an ITGB3-dependent pathway (PubMed:19332769). Maternal fibrinogen is essential for successful pregnancy (By similarity). Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage (By similarity). May also facilitate the immune response via both innate and T-cell mediated pathways (By similarity). {ECO:0000250|UniProtKB:E9PV24, ECO:0000269|PubMed:19332769}. PTM: Conversion of fibrinogen to fibrin is triggered by thrombin, which cleaves fibrinopeptides A and B from alpha and beta chains, and thus exposes the N-terminal polymerization sites responsible for the formation of the soft clot. The soft clot is converted into the hard clot by factor XIIIA which catalyzes the epsilon-(gamma-glutamyl)lysine cross-linking between gamma chains (stronger) and between alpha chains (weaker) of different monomers (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02679}. SUBUNIT: Heterohexamer; disulfide linked. Contains 2 sets of 3 non-identical chains (alpha, beta and gamma). The 2 heterotrimers are in head to head conformation with the N-termini in a small central domain (By similarity). {ECO:0000250|UniProtKB:P02679}. DOMAIN: A long coiled coil structure formed by 3 polypeptide chains connects the central nodule to the C-terminal domains (distal nodules). The long C-terminal ends of the alpha chains fold back, contributing a fourth strand to the coiled coil structure. {ECO:0000250|UniProtKB:P02679}. +Q71KU9 FGL1_MOUSE Fibrinogen-like protein 1 (Mouse fibrinogen-related protein 1) (MFIRE-1) 314 36,439 Chain (1); Coiled coil (1); Disulfide bond (3); Domain (1); Sequence conflict (2); Signal peptide (1) FUNCTION: Has hepatocyte mitogenic activity. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Homodimer. {ECO:0000305}. TISSUE SPECIFICITY: Liver specific. {ECO:0000269|PubMed:12528893}. +P11088 FILA_MOUSE Filaggrin (Fragment) 336 35,678 Chain (1); Non-terminal residue (1) FUNCTION: Aggregates keratin intermediate filaments and promotes disulfide-bond formation among the intermediate filaments during terminal differentiation of mammalian epidermis. PTM: Filaggrin is initially synthesized as a large, insoluble, highly phosphorylated precursor containing many tandem copies of 248 AA, which are not separated by large linker sequences. During terminal differentiation it is dephosphorylated and proteolytically cleaved. SUBCELLULAR LOCATION: Cytoplasmic granule {ECO:0000269|PubMed:3680218}. Note=In the stratum granulosum of the epidermis, localized within keratohyalin granules. In granular keratinocytes and in lower corneocytes, colocalizes with calpain-1/CAPN1 (By similarity). {ECO:0000250|UniProtKB:P20930}. TISSUE SPECIFICITY: Expressed in the granular layer of the epidermis. {ECO:0000269|PubMed:3680218, ECO:0000269|PubMed:6174530}. +Q9CQ92 FIS1_MOUSE Mitochondrial fission 1 protein (FIS1 homolog) (Tetratricopeptide repeat protein 11) (TPR repeat protein 11) 152 17,009 Beta strand (1); Chain (1); Helix (7); Modified residue (2); Repeat (1); Topological domain (2); Transmembrane (1) TRANSMEM 123 143 Helical. {ECO:0000255}. TOPO_DOM 1 122 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 144 152 Mitochondrial intermembrane. {ECO:0000255}. FUNCTION: Involved in the fragmentation of the mitochondrial network and its perinuclear clustering. Plays a minor role in the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface and mitochondrial fission. May be not essential for the assembly of functional fission complexes and the subsequent membrane scission event. Can induce cytochrome c release from the mitochondrion to the cytosol, ultimately leading to apoptosis. Also mediates peroxisomal fission. {ECO:0000269|PubMed:23283981}. PTM: Ubiquitinated by MARCH5. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass membrane protein. Peroxisome membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with DNM1L/DLP1 through the TPR region. Interacts with MARCH5. Interacts with MIEF1. Interacts with PEX11A, PEX11B and PEX11G. {ECO:0000250|UniProtKB:Q9Y3D6}. DOMAIN: The C-terminus is required for mitochondrial or peroxisomal localization, while the N-terminus is necessary for mitochondrial or peroxisomal fission, localization and regulation of the interaction with DNM1L. {ECO:0000250}. +Q91XW8 FKBP6_MOUSE Inactive peptidyl-prolyl cis-trans isomerase FKBP6 (Inactive PPIase FKBP6) (36 kDa FK506-binding protein) (36 kDa FKBP) (FKBP-36) (FK506-binding protein 6) (FKBP-6) (Immunophilin FKBP36) 327 37,125 Alternative sequence (2); Chain (1); Domain (1); Mutagenesis (1); Repeat (3); Sequence conflict (1) FUNCTION: Co-chaperone required during spermatogenesis to repress transposable elements and prevent their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and govern the methylation and subsequent repression of transposons. Acts as a co-chaperone via its interaction with HSP90 and is required for the piRNA amplification process, the secondary piRNA biogenesis. May be required together with HSP90 in removal of 16 nucleotide ping-pong by-products from Piwi complexes, possibly facilitating turnover of Piwi complexes. {ECO:0000269|PubMed:12764197, ECO:0000269|PubMed:18408354, ECO:0000269|PubMed:22902560}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12764197, ECO:0000269|PubMed:22902560}. Nucleus {ECO:0000269|PubMed:12764197}. Chromosome {ECO:0000269|PubMed:12764197}. Note=Does not localize to pi-bodies. Localizes to meiotic chromosome cores and regions of homologous chromosome synapsis. {ECO:0000269|PubMed:12764197, ECO:0000269|PubMed:22902560}. SUBUNIT: Interacts with HSP72/HSPA2 and CLTC. Interacts with GAPDH; leading to inhibit GAPDH catalytic activity (By similarity). Interacts (via TPR repeats) with HSP90. {ECO:0000250, ECO:0000269|PubMed:22902560}. TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:12764197}. +P26323 FLI1_MOUSE Friend leukemia integration 1 transcription factor (Retroviral integration site protein Fli-1) 452 51,002 Chain (1); DNA binding (1); Domain (1); Modified residue (1) FUNCTION: Sequence-specific transcriptional activator. Recognizes the DNA sequence 5'-C[CA]GGAAGT-3'. {ECO:0000250|UniProtKB:Q01543}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q01543}. SUBUNIT: Can form homodimers or heterodimers with ETV6/TEL1. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in both hematopoietic and nonhematopoietic tissues. DISEASE: Note=Involved in erythroleukemia induction by Friend murine leukemia virus (F-MULV). {ECO:0000269|PubMed:2044959}. +Q9Z2G1 FM1AA_MOUSE Protein fem-1 homolog A-A (FEM1a-A) (FEM1-alpha-A) 654 72,089 Chain (1); Frameshift (1); Repeat (11); Sequence conflict (4) Protein modification; protein ubiquitination. FUNCTION: Probable component of an E3 ubiquitin-protein ligase complex, in which it may act as a substrate recognition subunit. May participate in antiinflammatory signaling via its interaction with PTGER4 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Component of some E3 ubiquitin-protein ligase complex. Interacts with PTGER4 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in adult heart and skeletal muscle. {ECO:0000269|PubMed:9828124}. +Q60634 FLOT2_MOUSE Flotillin-2 (Epidermal surface antigen) (ESA) (Membrane component chromosome 17 surface marker 1 homolog) 428 47,038 Alternative sequence (2); Beta strand (7); Chain (1); Helix (5); Initiator methionine (1); Lipidation (4); Modified residue (1); Sequence conflict (1); Turn (1) FUNCTION: May act as a scaffolding protein within caveolar membranes, functionally participating in formation of caveolae or caveolae-like vesicles. May be involved in epidermal cell adhesion and epidermal structure and function. PTM: ZDHHC5-catalyzed palmitoylation may be required for the formation of higher-order complexes and for neurite outgrowth in cultured neural stem cells. {ECO:0000269|PubMed:22081607}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Membrane, caveola {ECO:0000250}; Peripheral membrane protein {ECO:0000269|PubMed:9153235}. Endosome {ECO:0000250}. Membrane {ECO:0000250|UniProtKB:Q14254}; Lipid-anchor {ECO:0000250|UniProtKB:Q14254}. Note=Membrane-associated protein of caveolae. {ECO:0000250}. SUBUNIT: Heterooligomeric complex of flotillin-1 and flotillin-2 and caveolin-1 and caveolin-2. Interacts with ECPAS (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in many tissues, including suprabasal epidermis, hair follicles, heart, lung, thymus, spleen, liver, kidney and brain. Not expressed in skeletal muscle. +Q05860 FMN1_MOUSE Formin-1 (Limb deformity protein) 1466 163,581 Alternative sequence (8); Chain (1); Coiled coil (1); Compositional bias (1); Domain (2); Region (2); Sequence conflict (7) FUNCTION: Plays a role in the formation of adherens junction and the polymerization of linear actin cables. {ECO:0000269|PubMed:14647292, ECO:0000269|PubMed:15198975}. PTM: Phosphorylated on serine and possibly threonine residues. {ECO:0000269|PubMed:8516300}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cell junction, adherens junction. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Note=Localization to the adherens junctions is alpha-catenin-dependent. Also localizes to F-actin bundles originating from adherens junctions.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm, cytoskeleton. Note=Isoform 2 localizes to microtubules. SUBUNIT: Interacts with alpha-catenin and may interact with tubulin. {ECO:0000269|PubMed:14647292, ECO:0000269|PubMed:16480715}. TISSUE SPECIFICITY: It is present in the adult kidney, testis, limb, ovary, brain, small intestine, salivary gland and harderian gland. Isoforms 1, 2 and 5 are detected in skin and keratinocytes. Isoform 5 is found throughout the embryo. {ECO:0000269|PubMed:14647292, ECO:0000269|PubMed:2392150}. +P97872 FMO5_MOUSE Dimethylaniline monooxygenase [N-oxide-forming] 5 (EC 1.14.13.8) (Dimethylaniline oxidase 5) (Hepatic flavin-containing monooxygenase 5) (FMO 5) 533 60,001 Binding site (1); Chain (1); Modified residue (8); Nucleotide binding (4); Sequence conflict (2); Transmembrane (1) TRANSMEM 513 533 Helical. {ECO:0000255}. FUNCTION: In contrast with other forms of FMO it does not seem to be a drug-metabolizing enzyme. {ECO:0000250}. SUBCELLULAR LOCATION: Microsome membrane. Endoplasmic reticulum membrane {ECO:0000250}. +O35565 FGF10_MOUSE Fibroblast growth factor 10 (FGF-10) (Keratinocyte growth factor 2) 209 23,597 Chain (1); Compositional bias (1); Glycosylation (2); Signal peptide (1) FUNCTION: Plays an important role in the regulation of embryonic development, cell proliferation and cell differentiation. Required for normal branching morphogenesis. May play a role in wound healing. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. SUBUNIT: Interacts with FGFR1 and FGFR2. Interacts with FGFBP1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed abundantly in embryos and the lung, and at much lower levels in brain and heart. +P70451 FER_MOUSE Tyrosine-protein kinase Fer (EC 2.7.10.2) (Proto-oncogene c-Fer) (p94-Fer) 823 94,579 Active site (1); Alternative sequence (6); Binding site (1); Chain (1); Coiled coil (2); Domain (3); Modified residue (4); Mutagenesis (8); Nucleotide binding (1); Region (1); Sequence conflict (4) FUNCTION: Tyrosine-protein kinase that acts downstream of cell surface receptors for growth factors and plays a role in the regulation of the actin cytoskeleton, microtubule assembly, lamellipodia formation, cell adhesion, cell migration and chemotaxis. Acts downstream of EGFR, KIT, PDGFRA and PDGFRB. Acts downstream of EGFR to promote activation of NF-kappa-B and cell proliferation. May play a role in the regulation of the mitotic cell cycle. Plays a role in the insulin receptor signaling pathway and in activation of phosphatidylinositol 3-kinase. Acts downstream of the activated FCER1 receptor and plays a role in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Plays a role in the regulation of mast cell degranulation. Plays a role in leukocyte recruitment and diapedesis in response to bacterial lipopolysaccharide (LPS). Phosphorylates CTTN, CTNND1, PTK2/FAK1, GAB1, PECAM1 and PTPN11. May phosphorylate JUP and PTPN1. Can phosphorylate STAT3 according to PubMed:10878010 and PubMed:19159681, but clearly plays a redundant role in STAT3 phosphorylation. According to PubMed:11134346, cells where wild type FER has been replaced by a kinase-dead mutant show no reduction in STAT3 phosphorylation. Phosphorylates TMF1. Isoform 3 lacks kinase activity. {ECO:0000269|PubMed:10878010, ECO:0000269|PubMed:11006284, ECO:0000269|PubMed:11994443, ECO:0000269|PubMed:15226396, ECO:0000269|PubMed:16176974, ECO:0000269|PubMed:16731527, ECO:0000269|PubMed:16732323, ECO:0000269|PubMed:17606629, ECO:0000269|PubMed:19159681, ECO:0000269|PubMed:20133938, ECO:0000269|PubMed:7623846, ECO:0000269|PubMed:9742951}. PTM: Autophosphorylated. {ECO:0000269|PubMed:10074905, ECO:0000269|PubMed:16176974, ECO:0000269|PubMed:16731527, ECO:0000269|PubMed:19159681}.; PTM: Polyubiquitinated; this leads to proteasomal degradation. {ECO:0000269|PubMed:19159681}. SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell projection {ECO:0000250}. Cell junction {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus. Cytoplasm, cell cortex {ECO:0000250}. Note=Detected on microtubules in polarized and motile vascular endothelial cells. Colocalizes with F-actin at the cell cortex. Colocalizes with PECAM1 and CTNND1 at nascent cell-cell contacts (By similarity). Not detected in the nucleus, but detected in the nuclear area surrounding the chromosomes after breakdown of the nuclear envelope during mitosis (PubMed:11339827). {ECO:0000250, ECO:0000269|PubMed:11339827}.; SUBCELLULAR LOCATION: Isoform 4: Nucleus. SUBUNIT: Homotrimer. Isoform 4 is a monomer, due to the absence of the N-terminal coiled coil domains. Interacts with CTNND1, EGFR, FLT3, PECAM1 and PDGFR. Interacts (via SH2 domain) with CTTN. Component of a complex that contains at least FER, CTTN and PTK2/FAK1 (By similarity). Interacts with IRS1 and PIK3R1. Interacts with STAT3. Interacts with PPP1CA and regulates its phosphorylation at 'Thr-320'. Interacts with JAK1. Interacts with HSP90; this stabilizes phosphorylated FER and protects FER against proteasomal degradation. Interacts with ARHGDIA, NRP1, PLEC and TMF1. {ECO:0000250, ECO:0000269|PubMed:10391941, ECO:0000269|PubMed:10878010, ECO:0000269|PubMed:11006284, ECO:0000269|PubMed:12200133, ECO:0000269|PubMed:12738762, ECO:0000269|PubMed:15467733, ECO:0000269|PubMed:16732323, ECO:0000269|PubMed:19159681, ECO:0000269|PubMed:20133938, ECO:0000269|PubMed:7623846}. DOMAIN: The coiled coil domains mediate homooligomerization and are required for location at microtubules. {ECO:0000250}.; DOMAIN: The N-terminal region including the first coiled coil domain mediates interaction with phosphoinositide-containing membranes. {ECO:0000250}. TISSUE SPECIFICITY: Detected in liver and testis. Isoform 4 is detected only in testis (at protein level). Widely expressed. {ECO:0000269|PubMed:10391941, ECO:0000269|PubMed:11134346, ECO:0000269|PubMed:2294399}. +Q6TYB5 FEZ2_MOUSE Fasciculation and elongation protein zeta-2 (Zygin II) (Zygin-2) 348 39,101 Chain (1); Coiled coil (1); Compositional bias (1); Disulfide bond (1); Modified residue (3) FUNCTION: Involved in axonal outgrowth and fasciculation. {ECO:0000250}. SUBUNIT: Homodimer; disulfide-linked. May form heterodimers with FEZ1. Interacts with synaptotagmin (By similarity). {ECO:0000250}. +Q9Z0Z4 HEPH_MOUSE Hephaestin (EC 1.-.-.-) 1157 129,666 Alternative sequence (1); Chain (1); Disulfide bond (5); Domain (6); Erroneous initiation (1); Glycosylation (8); Metal binding (19); Modified residue (3); Sequence conflict (6); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1110 1130 Helical. {ECO:0000255}. TOPO_DOM 19 1109 Extracellular. {ECO:0000255}.; TOPO_DOM 1131 1157 Cytoplasmic. {ECO:0000255}. FUNCTION: May function as a ferroxidase for ferrous (II) to ferric ion (III) conversion and may be involved in copper transport and homeostasis. Implicated in iron homeostasis and may mediate iron efflux associated to ferroportin 1. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. DISEASE: Note=Defects in Heph are a cause of the sex-linked anemia (sla) that is characterized by moderate to severe microcytic hypochronic anemia. +P70377 FGF13_MOUSE Fibroblast growth factor 13 (FGF-13) (Fibroblast growth factor homologous factor 2) (FHF-2) 245 27,588 Alternative sequence (2); Chain (1); Modified residue (1); Region (3); Sequence conflict (3) FUNCTION: Microtubule-binding protein which directly binds tubulin and is involved in both polymerization and stabilization of microtubules. Through its action on microtubules, may participate to the refinement of axons by negatively regulating axonal and leading processes branching. Plays a crucial role in neuron polarization and migration in the cerebral cortex and the hippocampus.; FUNCTION: Isoform 1 seems not to be involved in neuroblast polarization and migration but regulates axon branching.; FUNCTION: May regulate voltage-gated sodium channels transport and function.; FUNCTION: May also play a role in MAPK signaling. PTM: May be phosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cell projection, filopodium. Cell projection, growth cone. Cell projection, dendrite. Nucleus. Cytoplasm. Note=Not secreted. Localizes to the lateral membrane and intercalated disks of myocytes.; SUBCELLULAR LOCATION: Isoform 1: Nucleus.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. SUBUNIT: Interacts with SCN8A; may regulate SCN8A activity (By similarity). Interacts with SCN1A; may regulate SCN1A activity (By similarity). Interacts with SCN5A; the interaction is direct and may regulate SNC5A density at membranes and function. Interacts with MAPK8IP2; may regulate the MAPK8IP2 scaffolding activity. {ECO:0000250, ECO:0000269|PubMed:11378392, ECO:0000269|PubMed:21817159}. TISSUE SPECIFICITY: Detected in brain, eye and heart. In brain, the different isoforms display different patterns of expression. Expressed in brain and heart (at protein level). Isoform 3 is highly expressed in cardiac myocytes while isoform 1 is the most abundant in brain. {ECO:0000269|PubMed:10644718, ECO:0000269|PubMed:21817159, ECO:0000269|PubMed:9232594}. +O88842 FGD3_MOUSE FYVE, RhoGEF and PH domain-containing protein 3 733 80,624 Alternative sequence (2); Chain (1); Domain (3); Modified residue (2); Sequence conflict (2); Zinc finger (1) FUNCTION: Promotes the formation of filopodia. May activate CDC42, a member of the Ras-like family of Rho- and Rac proteins, by exchanging bound GDP for free GTP. Plays a role in regulating the actin cytoskeleton and cell shape. {ECO:0000269|PubMed:10721717}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Cytoplasm, cytoskeleton {ECO:0000305}. TISSUE SPECIFICITY: Detected in adult brain, spleen, lung and skeletal muscle. Detected in embryos from E7 to E17. {ECO:0000269|PubMed:10721717}. +Q9ESL8 FGF16_MOUSE Fibroblast growth factor 16 (FGF-16) 207 23,778 Chain (1); Glycosylation (1); Modified residue (1); Sequence conflict (2) FUNCTION: Plays an important role in the regulation of embryonic development, cell proliferation and cell differentiation, and is required for normal cardiomyocyte proliferation and heart development. {ECO:0000250|UniProtKB:O43320}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O54769}. SUBUNIT: Interacts with FGFR1 and FGFR2. {ECO:0000250|UniProtKB:O43320}. +Q9CQS3 FIBIN_MOUSE Fin bud initiation factor homolog 217 24,760 Chain (1); Disulfide bond (2); Glycosylation (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Golgi apparatus {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. SUBUNIT: Homodimer; disulfide-linked. Seems to also exist as monomers (By similarity). {ECO:0000250}. +P61148 FGF1_MOUSE Fibroblast growth factor 1 (FGF-1) (Acidic fibroblast growth factor) (aFGF) (Heparin-binding growth factor 1) (HBGF-1) 155 17,418 Binding site (1); Chain (1); Initiator methionine (1); Modified residue (1); Propeptide (1); Region (1) FUNCTION: Plays an important role in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration. Functions as potent mitogen in vitro. Acts as a ligand for FGFR1 and integrins. Binds to FGFR1 in the presence of heparin leading to FGFR1 dimerization and activation via sequential autophosphorylation on tyrosine residues which act as docking sites for interacting proteins, leading to the activation of several signaling cascades. Binds to integrin ITGAV:ITGB3. Its binding to integrin, subsequent ternary complex formation with integrin and FGFR1, and the recruitment of PTPN11 to the complex are essential for FGF1 signaling. Induces the phosphorylation and activation of FGFR1, FRS2, MAPK3/ERK1, MAPK1/ERK2 and AKT1. Can induce angiogenesis. {ECO:0000250|UniProtKB:P05230}. PTM: In the nucleus, phosphorylated by PKC/PRKCD. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. Cytoplasm {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Nucleus {ECO:0000250}. Note=Lacks a cleavable signal sequence. Within the cytoplasm, it is transported to the cell membrane and then secreted by a non-classical pathway that requires Cu(2+) ions and S100A13. Secreted in a complex with SYT1. Binding of exogenous FGF1 to FGFR facilitates endocytosis followed by translocation of FGF1 across endosomal membrane into the cytosol. Nuclear import from the cytosol requires the classical nuclear import machinery, involving proteins KPNA1 and KPNB1, as well as LRRC59 (By similarity). {ECO:0000250}. SUBUNIT: Monomer. Homodimer. Interacts with FGFR1, FGFR2, FGFR3 and FGFR4. Affinity between fibroblast growth factors (FGFs) and their receptors is increased by heparan sulfate glycosaminoglycans that function as coreceptors. Found in a complex with FGFBP1, FGF1 and FGF2. Interacts with FGFBP1. Part of a Cu(2+)-dependent multiprotein aggregate containing FGF1, S100A13 and SYT1. Interacts with SYT1. Interacts with S100A13 (By similarity). Interacts with LRRC59 (By similarity). Interacts with CSNKA, CSNKB and FIBP (By similarity). While binding with LRRC59, CSNKA and FIBP seem mutually exclusive, CSNKB and FIBP may cooperatively interact with FGF1. Forms a ternary complex with FGFR1 and ITGAV:ITGB3 and induces the recruitment of PTPN11 to the complex (By similarity). {ECO:0000250|UniProtKB:P05230}. +P54130 FGF9_MOUSE Fibroblast growth factor 9 (FGF-9) (Glia-activating factor) (GAF) (HBGF-9) 208 23,414 Chain (1); Glycosylation (1); Propeptide (1); Sequence conflict (2) FUNCTION: Plays an important role in the regulation of embryonic development, cell proliferation, cell differentiation and cell migration. May have a role in glial cell growth and differentiation during development, gliosis during repair and regeneration of brain tissue after damage, differentiation and survival of neuronal cells, and growth stimulation of glial tumors. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Monomer. Homodimer. Interacts with FGFR1, FGFR2, FGFR3 and FGFR4. Affinity between fibroblast growth factors (FGFs) and their receptors is increased by heparan sulfate glycosaminoglycans that function as coreceptors (By similarity). {ECO:0000250}. +Q8BIX9 FICD_MOUSE Protein adenylyltransferase FICD (EC 2.7.7.n1) (AMPylator FICD) (De-AMPylase FICD) (EC 3.1.4.-) (FIC domain-containing protein) 458 51,754 Active site (1); Alternative sequence (1); Binding site (2); Chain (1); Domain (1); Glycosylation (1); Modified residue (2); Motif (1); Nucleotide binding (3); Repeat (2); Sequence conflict (2); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 24 44 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 23 Cytoplasmic. {ECO:0000250|UniProtKB:Q9BVA6}.; TOPO_DOM 45 458 Lumenal. {ECO:0000250|UniProtKB:Q9BVA6}. FUNCTION: Protein that can both mediate the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context (By similarity). The side chain of Glu-231 determines which of the two opposing activities (AMPylase or de-AMPylase) will take place (By similarity). Acts as a key regulator of the ERN1/IRE1-mediated unfolded protein response (UPR) by mediating AMPylation or de-AMPylation of HSPA5/BiP (By similarity). In unstressed cells, acts as an adenylyltransferase by mediating AMPylation of HSPA5/BiP at 'Thr-518', thereby inactivating it (By similarity). In response to endoplasmic reticulum stress, acts as a phosphodiesterase by mediating removal of ATP (de-AMPylation) from HSPA5/BiP at 'Thr-518', leading to restore HSPA5/BiP activity (By similarity). Although it is able to AMPylate RhoA, Rac and Cdc42 Rho GTPases in vitro, Rho GTPases do not constitute physiological substrates (By similarity). {ECO:0000250|UniProtKB:A0A061I403, ECO:0000250|UniProtKB:Q9BVA6}. PTM: Auto-AMPylated in vitro. {ECO:0000250|UniProtKB:Q9BVA6}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9BVA6}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9BVA6}. SUBUNIT: Homodimer. Interacts with HD. {ECO:0000250|UniProtKB:Q9BVA6}. DOMAIN: The fido domain mediates the adenylyltransferase activity. {ECO:0000250|UniProtKB:Q9BVA6}. +P70120 HES5_MOUSE Transcription factor HES-5 (Hairy and enhancer of split 5) 167 18,425 Chain (1); Compositional bias (4); Domain (2); Motif (1); Sequence conflict (2) FUNCTION: Transcriptional repressor of genes that require a bHLH protein for their transcription. Plays an important role as neurogenesis negative regulator. {ECO:0000269|PubMed:23160044}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Transcription repression requires formation of a complex with a corepressor protein of the Groucho/TLE family. {ECO:0000250}. DOMAIN: Has a particular type of basic domain (presence of a helix-interrupting proline) that binds to the N-box (CACNAG), rather than the canonical E-box (CANNTG).; DOMAIN: The C-terminal WRPW motif is a transcriptional repression domain necessary for the interaction with Groucho/TLE family members, transcriptional corepressors recruited to specific target DNA by Hairy-related proteins. {ECO:0000250}. +Q91V79 FITM1_MOUSE Fat storage-inducing transmembrane protein 1 (Fat-inducing protein 1) 292 32,280 Chain (1); Erroneous initiation (1); Topological domain (7); Transmembrane (6) TRANSMEM 19 39 Helical. {ECO:0000255}.; TRANSMEM 55 75 Helical. {ECO:0000255}.; TRANSMEM 95 115 Helical. {ECO:0000255}.; TRANSMEM 188 208 Helical. {ECO:0000255}.; TRANSMEM 221 241 Helical. {ECO:0000255}.; TRANSMEM 250 270 Helical. {ECO:0000255}. TOPO_DOM 1 18 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 40 54 Extracellular. {ECO:0000255}.; TOPO_DOM 76 94 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 116 187 Extracellular. {ECO:0000255}.; TOPO_DOM 209 220 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 242 249 Extracellular. {ECO:0000255}.; TOPO_DOM 271 292 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays an important role in lipid droplet accumulation. {ECO:0000269|PubMed:18160536}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18160536}; Multi-pass membrane protein {ECO:0000269|PubMed:18160536}. TISSUE SPECIFICITY: Predominantly expressed in skeletal muscle and at lower levels in the heart (at protein level). In the heart, mRNA expression levels do not correlate well with protein levels, suggesting post-transcriptional regulation in this organ. {ECO:0000269|PubMed:18160536}. +Q6NWW9 FND3B_MOUSE Fibronectin type III domain-containing protein 3B (Factor for adipocyte differentiation 104) (HCV NS5A-binding protein 37) 1207 132,764 Chain (1); Compositional bias (2); Domain (9); Modified residue (3); Sequence conflict (8); Transmembrane (1) TRANSMEM 1185 1205 Helical. {ECO:0000255}. FUNCTION: May be positive regulator of adipogenesis. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. +Q8K4Z2 FNDC5_MOUSE Fibronectin type III domain-containing protein 5 (Fibronectin type III repeat-containing protein 2) (Peroxisomal protein) (PeP) [Cleaved into: Irisin] 209 23,321 Chain (2); Domain (1); Glycosylation (2); Motif (1); Sequence conflict (6); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 150 170 Helical. {ECO:0000255}. TOPO_DOM 29 149 Extracellular. {ECO:0000255}.; TOPO_DOM 171 209 Cytoplasmic. {ECO:0000255}. FUNCTION: Irisin: mediates beneficial effects of muscular exercise. Induces browning of white adipose tissue by stimulating UCP1 expression, at least in part, via the nuclear receptor PPARA. {ECO:0000269|PubMed:22237023}. PTM: The extracellular domain is cleaved and released from the cell membrane.; PTM: N-Glycosylated. {ECO:0000269|PubMed:22237023}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Peroxisome membrane; Single-pass type I membrane protein. Secreted. Note=Imported in peroxisomes through the PEX5 receptor pathway.; SUBCELLULAR LOCATION: Irisin: Secreted. Note=Detected in the blood of individuals subjected to endurance exercise. TISSUE SPECIFICITY: In adult, it is highly expressed in skeletal muscle, heart and brain. {ECO:0000269|PubMed:12112469, ECO:0000269|PubMed:12384288}. +Q05685 FOLR2_MOUSE Folate receptor beta (FR-beta) (Folate receptor 2) (Folate-binding protein 2) 251 28,821 Binding site (3); Chain (1); Disulfide bond (8); Glycosylation (2); Lipidation (1); Propeptide (1); Region (2); Signal peptide (1) FUNCTION: Binds to folate and reduced folic acid derivatives and mediates delivery of 5-methyltetrahydrofolate and folate analogs into the interior of cells. Has high affinity for folate and folic acid analogs at neutral pH. Exposure to slightly acidic pH after receptor endocytosis triggers a conformation change that strongly reduces its affinity for folates and mediates their release (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. +P13346 FOSB_MOUSE Protein fosB 338 35,977 Chain (1); Domain (1); Region (2) FUNCTION: FosB interacts with Jun proteins enhancing their DNA binding activity. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Heterodimer. {ECO:0000250}. +G5E8F4 FPGT_MOUSE Fucose-1-phosphate guanylyltransferase (EC 2.7.7.30) (GDP-L-fucose diphosphorylase) (GDP-L-fucose pyrophosphorylase) 590 65,362 Chain (1); Frameshift (1); Sequence conflict (8) FUNCTION: Catalyzes the formation of GDP-L-fucose from GTP and L-fucose-1-phosphate (PubMed:14686921). Functions as a salvage pathway to reutilize L-fucose arising from the turnover of glycoproteins and glycolipids (Probable). {ECO:0000269|PubMed:14686921, ECO:0000305|PubMed:14686921}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:14686921}. TISSUE SPECIFICITY: Expressed at highest levels in brain, moderately in testis, ovary and kidney, and weakly in liver, spleen, heart and lung. {ECO:0000269|PubMed:14686921}. +Q3UQN2 FCHO2_MOUSE F-BAR domain only protein 2 809 88,734 Alternative sequence (4); Chain (1); Coiled coil (1); Compositional bias (2); Cross-link (1); Disulfide bond (2); Domain (2); Erroneous initiation (3); Frameshift (1); Modified residue (13); Mutagenesis (7); Region (2); Sequence conflict (1) FUNCTION: Functions in an early step of clathrin-mediated endocytosis. Has both a membrane binding/bending activity and the ability to recruit proteins essential to the formation of functional clathrin-coated pits. Has a lipid-binding activity with a preference for membranes enriched in phosphatidylserine and phosphoinositides (Pi(4,5) biphosphate) like the plasma membrane. Its membrane-bending activity might be important for the subsequent action of clathrin and adaptors in the formation of clathrin-coated vesicles. Involved in adaptor protein complex AP-2-dependent endocytosis of the transferrin receptor, it also functions in the AP-2-independent endocytosis of the LDL receptor. {ECO:0000269|PubMed:21762413, ECO:0000269|PubMed:21883765}. PTM: Ubiquitinated. Mainly undergoes monoubiquitination but also polyubiquitination. {ECO:0000269|PubMed:21762413}. SUBCELLULAR LOCATION: Membrane, clathrin-coated pit {ECO:0000305|PubMed:20448150, ECO:0000305|PubMed:21762413}; Peripheral membrane protein {ECO:0000305|PubMed:20448150, ECO:0000305|PubMed:21762413}; Cytoplasmic side {ECO:0000305|PubMed:20448150, ECO:0000305|PubMed:21762413}. Note=Associated with forming but not mature clathrin-coated vesicles. The recruitment to coated-pits precede the one of clathrin and the adaptor protein complex AP-2. SUBUNIT: Homodimer; disulfide-linked (By similarity). May form homotetramer. Interacts with AP2A1. Interacts with EPS15, EPS15R, ITSN1 and ITSN2; recruit those scaffolding proteins which in turn may interact with the adaptor protein complex AP-2 at the plasma membrane. Interacts with DAB2 (via DPF motifs); mediates LDL receptor/LDLR endocytosis. {ECO:0000250, ECO:0000269|PubMed:20448150, ECO:0000269|PubMed:21762413, ECO:0000269|PubMed:22323290}. TISSUE SPECIFICITY: Ubiquitously expressed (at protein level). {ECO:0000269|PubMed:21762413}. +P35428 HES1_MOUSE Transcription factor HES-1 (Hairy and enhancer of split 1) 282 29,749 Chain (1); Compositional bias (2); Domain (2); Motif (1) FUNCTION: Transcriptional repressor of genes that require a bHLH protein for their transcription. May act as a negative regulator of myogenesis by inhibiting the functions of MYOD1 and ASH1 (By similarity). Binds DNA on N-box motifs: 5'-CACNAG-3' with high affinity and on E-box motifs: 5'-CANNTG-3' with low affinity. May play a role in a functional FA core complex response to DNA cross-link damage, being required for the stability and nuclear localization of FA core complex proteins, as well as for FANCD2 monoubiquitination in response to DNA damage (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with SIRT1 (By similarity). Transcription repression requires formation of a complex with a corepressor protein of the Groucho/TLE family. Interacts (via WPRW motif) with TLE1, and more weakly with TLE2. Interacts with HES6. Interacts with an FA complex, composed of FANCA, FANCF, FANCG and FANCL, but not of FANCC, nor FANCE (By similarity). {ECO:0000250}. DOMAIN: Has a particular type of basic domain (presence of a helix-interrupting proline) that binds to the N-box (CACNAG), rather than the canonical E-box (CANNTG).; DOMAIN: The C-terminal WRPW motif is a transcriptional repression domain necessary for the interaction with Groucho/TLE family members, transcriptional corepressors recruited to specific target DNA by Hairy-related proteins.; DOMAIN: The bHLH, as well as cooperation between the central Orange domain and the C-terminal WRPW motif, is required for transcriptional repressor activity. {ECO:0000250}. TISSUE SPECIFICITY: Expressed at high levels in undifferentiated neural precursor cells, but the level of expression decreases as neural differentiation proceeds. +Q3ULZ2 FHDC1_MOUSE FH2 domain-containing protein 1 (Inverted formin-1) 1149 125,367 Chain (1); Domain (1); Erroneous initiation (1); Modified residue (3); Region (1); Sequence conflict (3) FUNCTION: Microtubule-associated formin which regulates both actin and microtubule dynamics. Induces microtubule acetylation and stabilization and actin stress fiber formation (PubMed:18815276). Regulates Golgi ribbon formation (PubMed:26564798). Required for normal cilia assembly. Early in cilia assembly, may assist in the maturation and positioning of the centrosome/basal body, and once cilia assembly has initiated, may also promote cilia elongation by inhibiting disassembly (PubMed:29742020). {ECO:0000269|PubMed:18815276, ECO:0000269|PubMed:26564798, ECO:0000269|PubMed:29742020}. SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:26564798}. Cell projection, cilium {ECO:0000250|UniProtKB:Q9C0D6}. Note=Associates with microtubules. {ECO:0000269|PubMed:18815276, ECO:0000269|PubMed:26564798, ECO:0000269|PubMed:29742020}. SUBUNIT: Interacts with CEP170. {ECO:0000269|PubMed:29742020}. DOMAIN: The FH2 and MBD domains are essential for its function in regulating Golgi ribbon formation. {ECO:0000250|UniProtKB:Q9C0D6}. TISSUE SPECIFICITY: Brain, heart and lung (at protein level). {ECO:0000269|PubMed:18815276}. +P59266 FITM2_MOUSE Fat storage-inducing transmembrane protein 2 (Fat-inducing protein 2) 262 30,016 Chain (1); Topological domain (7); Transmembrane (6) TRANSMEM 24 44 Helical. {ECO:0000255}.; TRANSMEM 58 78 Helical. {ECO:0000255}.; TRANSMEM 94 114 Helical. {ECO:0000255}.; TRANSMEM 146 166 Helical. {ECO:0000255}.; TRANSMEM 191 211 Helical. {ECO:0000255}.; TRANSMEM 219 239 Helical. {ECO:0000255}. TOPO_DOM 1 23 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 45 57 Extracellular. {ECO:0000255}.; TOPO_DOM 79 93 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 115 145 Extracellular. {ECO:0000255}.; TOPO_DOM 167 190 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 212 218 Extracellular. {ECO:0000255}.; TOPO_DOM 240 262 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays an important role in lipid droplet accumulation. Plays a role in the regulation of cell morphology and cytoskeletal organization. {ECO:0000269|PubMed:18160536}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18160536}; Multi-pass membrane protein {ECO:0000269|PubMed:18160536}. TISSUE SPECIFICITY: Widely expressed, with highest levels in white and brown adipose tissues (at protein level). In the heart, mRNA expression levels do not correlate well with protein levels, suggesting post-transcriptional regulation in this organ. {ECO:0000269|PubMed:18160536}. +P26883 FKB1A_MOUSE Peptidyl-prolyl cis-trans isomerase FKBP1A (PPIase FKBP1A) (EC 5.2.1.8) (12 kDa FK506-binding protein) (12 kDa FKBP) (FKBP-12) (Calstabin-1) (FK506-binding protein 1A) (FKBP-1A) (Immunophilin FKBP12) (Rotamase) 108 11,923 Chain (1); Domain (1); Modified residue (2) FUNCTION: Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. Recruits SMAD7 to ACVR1B which prevents the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. May modulate the RYR1 calcium channel activity. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P62942}. Sarcoplasmic reticulum membrane {ECO:0000250|UniProtKB:P62943}; Peripheral membrane protein {ECO:0000250|UniProtKB:P62943}; Cytoplasmic side {ECO:0000250|UniProtKB:P62943}. SUBUNIT: Interacts with TGFBR1; prevents TGFBR1 phosphorylation by TGFBR2 and stabilizes it in the inactive conformation (By similarity). Interacts with ACVR1B and SMAD7 (By similarity). Identified in a complex composed of RYR1, PDE4D, PKA, FKBP1A and protein phosphatase 1 (PP1) (PubMed:18268335). Interacts directly with RYR2 and RYR3 (By similarity). Interacts directly with RYR1 (By similarity). Interacts with GLMN; rapamycin and FK506 abolish the interaction with GLMN in a dose dependent manner (By similarity). {ECO:0000250|UniProtKB:P62942, ECO:0000250|UniProtKB:P62943, ECO:0000250|UniProtKB:Q62658, ECO:0000269|PubMed:18268335}. +Q8CG64 FKRP_MOUSE Fukutin-related protein (EC 2.4.2.-) (Ribitol-5-phosphate transferase) 494 54,852 Chain (1); Disulfide bond (1); Erroneous initiation (1); Glycosylation (2); Mutagenesis (6); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 7 29 Helical. {ECO:0000255}. TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 30 494 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Catalyzes the transfer of CDP-ribitol to ribitol 5-phosphate previously attached by FKTN/fukutin of to the phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-3-N-acetylglucosamine-beta-4-(phosphate-6-)mannose), a carbohydrate structure present in alpha-dystroglycan (DAG1) (By similarity). This constitutes the second step in the formation of the ribose 5-phosphate tandem repeat which links the phosphorylated O-mannosyl trisaccharide to the ligand binding moiety composed of repeats of 3-xylosyl-alpha-1,3-glucuronic acid-beta-1 (By similarity). {ECO:0000250|UniProtKB:Q9H9S5}. PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:12471058, ECO:0000269|PubMed:17554798}; Single-pass type II membrane protein {ECO:0000305}. Secreted {ECO:0000269|PubMed:19900540}. Cell membrane, sarcolemma {ECO:0000269|PubMed:17452335}. Rough endoplasmic reticulum {ECO:0000250|UniProtKB:Q9H9S5}. Cytoplasm {ECO:0000269|PubMed:29416295}. Note=The N-terminal hydrophobic domain is cleaved after translocation to the Golgi apparatus and the protein is secreted (PubMed:19900540). Localization at the cell membrane may require the presence of dystroglycan (PubMed:17452335). At the Golgi apparatus localizes to the middle-to-trans-cisternae (PubMed:12471058, PubMed:17554798). Detected in rough endoplasmic reticulum in myocytes (By similarity). {ECO:0000250|UniProtKB:Q9H9S5, ECO:0000269|PubMed:12471058, ECO:0000269|PubMed:17452335, ECO:0000269|PubMed:17554798, ECO:0000269|PubMed:19900540}. SUBUNIT: Homodimer; disulfide-linked (By similarity). Forms a complex composed of FKRP, FKTN/fukutin, and RXYLT1/TMEM5 (By similarity). Exists also as large multimeric protein complexes (By similarity). May interact with the dystrophin-glycoprotein complex (DGC) (PubMed:17452335). {ECO:0000250|UniProtKB:Q9H9S5, ECO:0000269|PubMed:17452335}. TISSUE SPECIFICITY: Expressed in the retina, specifically in the inner segments of the photoreceptors, the outer plexiform layers, inner nuclear layers, and ganglion cell layers (at protein level) (PubMed:29416295). Expressed at highest levels in brain, lung, heart, kidney and liver (PubMed:12471058). {ECO:0000269|PubMed:12471058, ECO:0000269|PubMed:29416295}. +Q9Z2I2 FKB1B_MOUSE Peptidyl-prolyl cis-trans isomerase FKBP1B (PPIase FKBP1B) (EC 5.2.1.8) (12.6 kDa FK506-binding protein) (12.6 kDa FKBP) (FKBP-12.6) (FK506-binding protein 1B) (FKBP-1B) (Immunophilin FKBP12.6) (Rotamase) 108 11,798 Chain (1); Domain (1) FUNCTION: Has the potential to contribute to the immunosuppressive and toxic effects of FK506 and rapamycin. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Sarcoplasmic reticulum {ECO:0000250}. SUBUNIT: Identified in a complex composed of RYR2, FKBP1B, PKA catalytic subunit, PRKAR2A, AKAP6, and the protein phosphatases PP2A and PP1. Interacts directly with RYR2 (By similarity). {ECO:0000250}. +Q8QZS3 FLCN_MOUSE Folliculin 579 64,327 Chain (1); Coiled coil (1); Domain (3); Frameshift (1); Modified residue (4); Sequence conflict (4) FUNCTION: May be a tumor suppressor. May be involved in energy and/or nutrient sensing through the AMPK and mTOR signaling pathways. May regulate phosphorylation of RPS6KB1. {ECO:0000250|UniProtKB:Q8NFG4}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8NFG4}. Nucleus {ECO:0000250|UniProtKB:Q8NFG4}. Note=Mainly localized in the nucleus. Colocalizes with FNIP1 and FNIP2 in the cytoplasm. {ECO:0000250|UniProtKB:Q8NFG4}. SUBUNIT: Interacts (via C-terminus) with FNIP1 and FNIP2 (via C-terminus). This mediates indirect interaction with the PRKAA1, PRKAB1 and PRKAG1 subunits of 5'-AMP-activated protein kinase. Interacts with HSP90AA1 in the presence of FNIP1. Interacts with HSP70, STUB1, CDC37, AHSA1, CCT2, STIP1, PTGES3 and PPP5C. {ECO:0000250|UniProtKB:Q8NFG4}. +Q62446 FKBP3_MOUSE Peptidyl-prolyl cis-trans isomerase FKBP3 (PPIase FKBP3) (EC 5.2.1.8) (25 kDa FK506-binding protein) (25 kDa FKBP) (FKBP-25) (FK506-binding protein 3) (FKBP-3) (Immunophilin FKBP25) (Rapamycin-selective 25 kDa immunophilin) (Rotamase) 224 25,148 Beta strand (8); Chain (1); Domain (1); Helix (3); Initiator methionine (1); Modified residue (5); Sequence conflict (1); Turn (1) FUNCTION: FK506- and rapamycin-binding proteins (FKBPs) constitute a family of receptors for the two immunosuppressants which inhibit T-cell proliferation by arresting two distinct cytoplasmic signal transmission pathways. PPIases accelerate the folding of proteins (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +Q8VHG0 FMO4_MOUSE Dimethylaniline monooxygenase [N-oxide-forming] 4 (EC 1.14.13.8) (Dimethylaniline oxidase 4) (Hepatic flavin-containing monooxygenase 4) (FMO 4) 560 63,792 Binding site (1); Chain (1); Nucleotide binding (4); Transmembrane (1) TRANSMEM 510 530 Helical. {ECO:0000255}. FUNCTION: This protein is involved in the oxidative metabolism of a variety of xenobiotics such as drugs and pesticides. {ECO:0000250}. SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250|UniProtKB:Q8K4B7}; Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8K4B7}; Single-pass membrane protein {ECO:0000255}. +Q8BG21 FLOWR_MOUSE Calcium channel flower homolog (Calcium channel flower domain-containing protein 1) 171 18,343 Alternative sequence (3); Chain (1); Transmembrane (3) TRANSMEM 32 52 Helical. {ECO:0000255}.; TRANSMEM 57 77 Helical. {ECO:0000255}.; TRANSMEM 102 122 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q80TD3 FNIP2_MOUSE Folliculin-interacting protein 2 (FNIP1-like protein) (O6-methylguanine-induced apoptosis 1 protein) 1108 122,520 Chain (1); Compositional bias (2); Domain (3); Modified residue (5); Region (1) FUNCTION: Acts as a co-chaperone of HSP90AA1. Inhibits the ATPase activity of HSP90AA1 leading to reduction in its chaperone activity. Facilitates the binding of client protein FLCN to HSP90AA1. May be involved in energy and/or nutrient sensing through the AMPK and mTOR signaling pathways. May regulate phosphorylation of RPS6KB1 (By similarity). May play a role in the signal transduction pathway of apoptosis induced by O6-methylguanine-mispaired lesions (PubMed:19137017). {ECO:0000250|UniProtKB:Q9P278, ECO:0000269|PubMed:19137017}. PTM: Phosphorylated by AMPK. {ECO:0000250|UniProtKB:Q9P278}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19137017}. Note=Colocalizes with FLCN in the cytoplasm. {ECO:0000250|UniProtKB:Q9P278}. SUBUNIT: Homodimer and homomultimer. Heterodimer and heteromultimer with FNIP1. Interacts (via C-terminus) with FLCN (via C-terminus). Phosphorylated FLCN is preferentially bound. Interacts with PRKAA1, PRKAB1 and PRKAG1 subunits of 5'-AMP-activated protein kinase. Interacts with HSP70, HSP90AA1, STIP1, PTGES3, CDC37, BRAF, GCR and CDK4. {ECO:0000250|UniProtKB:Q9P278}. +Q6ZQ03 FNBP4_MOUSE Formin-binding protein 4 (Formin-binding protein 30) 1031 111,245 Alternative sequence (4); Chain (1); Compositional bias (2); Cross-link (6); Domain (2); Erroneous initiation (3); Frameshift (1); Modified residue (17); Sequence conflict (7) SUBUNIT: Binds FMN1. Interacts with the Arg/Gly-rich-flanked Pro-rich regions of KHDRBS1/SAM68. Arginine methylation in these regions has no effect on this binding (By similarity). {ECO:0000250}. DOMAIN: These WW domains interact with Arg/Gly-rich-flanked Pro-rich domains found in several WW domain-binding proteins (WBPs). The N-terminal WW domain has the greater ligand-binding ability (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. Highest levels in spleen and thymus. {ECO:0000269|PubMed:10510470, ECO:0000269|PubMed:10744724}. +Q922I5 FOXI1_MOUSE Forkhead box protein I1 372 40,798 Chain (1); Compositional bias (1); DNA binding (1); Sequence conflict (1) FUNCTION: Transcriptional activator required for the development of normal hearing, sense of balance and kidney function. Required for the expression of SLC26A4/PDS, JAG1 and COCH in a subset of epithelial cells and the development of the endolymphatic system in the inner ear. Also required for the expression of SLC4A1/AE1, SLC4A9/AE4, ATP6V1B1 and the differentiation of intercalated cells in the epithelium of distal renal tubules. {ECO:0000269|PubMed:12642503, ECO:0000269|PubMed:15173882}. SUBCELLULAR LOCATION: Nucleus. TISSUE SPECIFICITY: Expressed in intercalated cells of the epithelium of the distal renal tubule. {ECO:0000269|PubMed:15173882}. +Q9CRB3 HIUH_MOUSE 5-hydroxyisourate hydrolase (HIU hydrolase) (HIUHase) (EC 3.5.2.17) (Transthyretin-related protein) 118 13,559 Binding site (3); Chain (1); Mutagenesis (6) Purine metabolism; urate degradation; (S)-allantoin from urate: step 2/3. FUNCTION: Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU). SUBCELLULAR LOCATION: Peroxisome {ECO:0000305}. SUBUNIT: Homotetramer. {ECO:0000250}. +Q9WVH3 FOXO4_MOUSE Forkhead box protein O4 (Afxh) (Fork head domain transcription factor AFX1) 505 53,649 Chain (1); DNA binding (1); Modified residue (3); Region (1) FUNCTION: Transcription factor involved in the regulation of the insulin signaling pathway. Binds to insulin-response elements (IREs) and can activate transcription of IGFBP1. Down-regulates expression of HIF1A and suppresses hypoxia-induced transcriptional activation of HIF1A-modulated genes. Also involved in negative regulation of the cell cycle. Involved in increased proteasome activity in embryonic stem cells (ESCs) by activating expression of PSMD11 in ESCs, leading to enhanced assembly of the 26S proteasome, followed by higher proteasome activity (By similarity). Represses smooth muscle cell differentiation by inhibiting the transcriptional coactivator activity of myocardin. {ECO:0000250|UniProtKB:P98177, ECO:0000269|PubMed:16054032}. PTM: Acetylation by CREBBP/CBP is induced by oxidative stress and inhibits transcriptional activity. Deacetylation by SIRT1 is NAD-dependent and stimulates transcriptional activity (By similarity). {ECO:0000250|UniProtKB:P98177}.; PTM: Phosphorylation by PKB/AKT1 inhibits transcriptional activity and is responsible for cytoplasmic localization. May be phosphorylated at multiple sites by NLK (By similarity). {ECO:0000250|UniProtKB:P98177}.; PTM: Monoubiquitinated; monoubiquitination is induced by oxidative stress and reduced by deacetylase inhibitors; results in its relocalization to the nucleus and its increased transcriptional activity. Deubiquitinated by USP7; deubiquitination is induced by oxidative stress; enhances its interaction with USP7 and consequently, deubiquitination; increases its translocation to the cytoplasm and inhibits its transcriptional activity. Hydrogene-peroxide-induced ubiquitination and USP7-mediated deubiquitination have no major effect on its protein stability (By similarity). {ECO:0000250|UniProtKB:P98177}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=When phosphorylated, translocated from nucleus to cytoplasm. Dephosphorylation triggers nuclear translocation. Monoubiquitination increases nuclear localization. When deubiquitinated, translocated from nucleus to cytoplasm (By similarity). {ECO:0000250|UniProtKB:P98177}. SUBUNIT: Interacts with CREBBP/CBP, MYOCD, SIRT1, SRF and YWHAZ. Acetylated by CREBBP/CBP and deacetylated by SIRT1. Binding of YWHAZ inhibits DNA-binding. Interacts with USP7; the interaction is enhanced in presence of hydrogen peroxide and occurs independently of TP53. Interacts with NLK, and this inhibits monoubiquitination and transcriptional activity (By similarity). Interacts with FOXK1; the interaction inhibits MEF2C transactivation activity (PubMed:22956541). {ECO:0000250|UniProtKB:P98177, ECO:0000269|PubMed:22956541}. TISSUE SPECIFICITY: Strongly expressed in brown adipose tissue and weakly in white adipose tissue (at protein level). Expressed in skeletal muscle. {ECO:0000269|PubMed:11353388, ECO:0000269|PubMed:22510882}. +Q8BUR3 FOXJ3_MOUSE Forkhead box protein J3 623 68,954 Alternative sequence (1); Chain (1); DNA binding (1); Erroneous initiation (1); Modified residue (3) FUNCTION: Transcriptional activator of MEF2C involved in the regulation of adult muscle fiber type identity and skeletal muscle regeneration (PubMed:19914232). {ECO:0000269|PubMed:19914232}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089}. +P0DM40 FR1L5_MOUSE Fer-1-like protein 5 2038 235,837 Chain (1); Domain (6); Mutagenesis (2); Sequence conflict (9); Transmembrane (1) TRANSMEM 1961 1981 Helical. {ECO:0000255}. FUNCTION: Plays a role in myoblast fusion; probable mediator of endocytic recycling for membrane trafficking events during myotube formation. {ECO:0000269|PubMed:21177873}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21177873}. Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Note=Colocalizes with EHD1 and EHD2 at the plasma membrane in myoblasts and myotubes. Localizes into foci at the plasma membrane. SUBUNIT: Interacts (via second C2 domain) with EHD1 and EHD2. {ECO:0000269|PubMed:21177873}. TISSUE SPECIFICITY: Expressed in differentiating myoblasts and myotubes. {ECO:0000269|PubMed:21177873}. +Q8K025 FRAT2_MOUSE GSK-3-binding protein FRAT2 (Frequently rearranged in advanced T-cell lymphomas 2) (FRAT-2) 231 23,914 Chain (1); Compositional bias (2); Region (1) FUNCTION: Positively regulates the Wnt signaling pathway by stabilizing beta-catenin through the association with GSK-3. SUBUNIT: Binds GSK-3 and prevents GSK-3-dependent phosphorylation. +Q9WV91 FPRP_MOUSE Prostaglandin F2 receptor negative regulator (Prostaglandin F2-alpha receptor regulatory protein) (Prostaglandin F2-alpha receptor-associated protein) (CD antigen CD315) 879 98,722 Chain (1); Disulfide bond (6); Domain (6); Glycosylation (8); Modified residue (1); Motif (3); Sequence conflict (6); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 833 853 Helical. {ECO:0000255}. TOPO_DOM 22 832 Extracellular. {ECO:0000255}.; TOPO_DOM 854 879 Cytoplasmic. {ECO:0000255}. FUNCTION: Inhibits the binding of prostaglandin F2-alpha (PGF2-alpha) to its specific FP receptor, by decreasing the receptor number rather than the affinity constant. Functional coupling with the prostaglandin F2-alpha receptor seems to occur (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Interacts with CD9 and CD81. Also seems to interact with CD63, CD82 and CD151 (By similarity). {ECO:0000250}. +A4FUQ5 FPRS4_MOUSE Formyl peptide receptor-related sequence 4 (N-formylpeptide receptor-like 4) 323 36,294 Chain (1); Disulfide bond (1); Glycosylation (3); Sequence conflict (5); Topological domain (8); Transmembrane (7) TRANSMEM 30 50 Helical; Name=1. {ECO:0000255}.; TRANSMEM 67 87 Helical; Name=2. {ECO:0000255}.; TRANSMEM 100 120 Helical; Name=3. {ECO:0000255}.; TRANSMEM 145 165 Helical; Name=4. {ECO:0000255}.; TRANSMEM 203 223 Helical; Name=5. {ECO:0000255}.; TRANSMEM 242 262 Helical; Name=6. {ECO:0000255}.; TRANSMEM 281 301 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 29 Extracellular. {ECO:0000255}.; TOPO_DOM 51 66 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 88 99 Extracellular. {ECO:0000255}.; TOPO_DOM 121 144 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 166 202 Extracellular. {ECO:0000255}.; TOPO_DOM 224 241 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 263 280 Extracellular. {ECO:0000255}.; TOPO_DOM 302 323 Cytoplasmic. {ECO:0000255}. FUNCTION: May have an olfactory function associated with the identification of pathogens or of pathogenic states. {ECO:0000269|PubMed:19387439}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed in 0.6 % of a subset of sensory neurons located in the apical layer of the vomeronasal organ. Each neuron appears to express only one receptor gene. {ECO:0000269|PubMed:19387439, ECO:0000269|PubMed:19497865}. +Q499D0 FOXN3_MOUSE Forkhead box protein N3 (Checkpoint suppressor 1) 457 50,345 Chain (1); Compositional bias (1); DNA binding (1); Modified residue (4) FUNCTION: Acts as a transcriptional repressor. May be involved in DNA damage-inducible cell cycle arrests (checkpoints) (By similarity). {ECO:0000250|UniProtKB:O00409}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Interacts through its C-terminus with the C-terminus of SNW1/SKIP. {ECO:0000250|UniProtKB:O00409}. +Q76JU9 FFAR1_MOUSE Free fatty acid receptor 1 (G-protein coupled receptor 40) 300 31,804 Binding site (3); Chain (1); Disulfide bond (1); Glycosylation (1); Region (1); Sequence conflict (1); Site (2); Topological domain (8); Transmembrane (7) TRANSMEM 9 31 Helical; Name=1. {ECO:0000250|UniProtKB:O14842, ECO:0000255}.; TRANSMEM 42 64 Helical; Name=2. {ECO:0000250|UniProtKB:O14842, ECO:0000255}.; TRANSMEM 80 101 Helical; Name=3. {ECO:0000250|UniProtKB:O14842, ECO:0000255}.; TRANSMEM 122 142 Helical; Name=4. {ECO:0000250|UniProtKB:O14842, ECO:0000255}.; TRANSMEM 179 200 Helical; Name=5. {ECO:0000250|UniProtKB:O14842, ECO:0000255}.; TRANSMEM 224 248 Helical; Name=6. {ECO:0000250|UniProtKB:O14842, ECO:0000255}.; TRANSMEM 257 279 Helical; Name=7. {ECO:0000250|UniProtKB:O14842, ECO:0000255}. TOPO_DOM 1 8 Extracellular. {ECO:0000250|UniProtKB:O14842, ECO:0000255}.; TOPO_DOM 32 41 Cytoplasmic. {ECO:0000250|UniProtKB:O14842, ECO:0000255}.; TOPO_DOM 65 79 Extracellular. {ECO:0000250|UniProtKB:O14842, ECO:0000255}.; TOPO_DOM 102 121 Cytoplasmic. {ECO:0000250|UniProtKB:O14842, ECO:0000255}.; TOPO_DOM 143 178 Extracellular. {ECO:0000250|UniProtKB:O14842, ECO:0000255}.; TOPO_DOM 201 223 Cytoplasmic. {ECO:0000250|UniProtKB:O14842, ECO:0000255}.; TOPO_DOM 249 256 Extracellular. {ECO:0000250|UniProtKB:O14842, ECO:0000255}.; TOPO_DOM 280 300 Cytoplasmic. {ECO:0000250|UniProtKB:O14842, ECO:0000255}. FUNCTION: G-protein coupled receptor for medium and long chain saturated and unsaturated fatty acids that plays an important role in glucose homeostasis. Fatty acid binding increases glucose-stimulated insulin secretion, and may also enhance the secretion of glucagon-like peptide 1 (GLP-1). May also play a role in bone homeostasis; receptor signaling activates pathways that inhibit osteoclast differentiation (PubMed:23335512). Ligand binding leads to a conformation change that triggers signaling via G-proteins that activate phospholipase C, leading to an increase of the intracellular calcium concentration. Seems to act through a G(q) and G(i)-mediated pathway. {ECO:0000269|PubMed:12629551, ECO:0000269|PubMed:16044321, ECO:0000269|PubMed:17395749, ECO:0000269|PubMed:18559658, ECO:0000269|PubMed:23335512, ECO:0000269|PubMed:23403053, ECO:0000269|PubMed:24130766}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16044321, ECO:0000269|PubMed:24130766}; Multi-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Expressed in pancreatic islet beta cells (at protein level) (PubMed:16044321). Expressed in pancreatic islet beta cells. {ECO:0000269|PubMed:12496284, ECO:0000269|PubMed:16044321}. +Q8QZW2 FEV_MOUSE Protein FEV (PC12 ETS domain-containing transcription factor 1) (PC12 ETS factor 1) (Pet-1) (mPet-1) 237 24,991 Chain (1); Compositional bias (1); DNA binding (1); Region (1) FUNCTION: Functions as a transcriptional regulator. May function as a transcriptional repressor. Functions in the differentiation and the maintenance of the central serotonergic neurons. May play a role in cell growth. {ECO:0000269|PubMed:12546819, ECO:0000269|PubMed:14602809, ECO:0000269|PubMed:17656160}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00237, ECO:0000269|PubMed:11875656}. TISSUE SPECIFICITY: Expressed in central serotonergic neurons. {ECO:0000269|PubMed:11875656}. +Q9JJN1 FGF21_MOUSE Fibroblast growth factor 21 (FGF-21) 210 23,237 Chain (1); Signal peptide (1) FUNCTION: Stimulates glucose uptake in differentiated adipocytes via the induction of glucose transporter SLC2A1/GLUT1 expression (but not SLC2A4/GLUT4 expression). Activity probably requires the presence of KLB. {ECO:0000269|PubMed:15902306}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. SUBUNIT: Interacts (via C-terminus) with KLB; this interaction is direct. Interacts with FGFR4 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Most abundantly expressed in the liver, also expressed in the thymus at lower levels. {ECO:0000269|PubMed:10858549}. +O70514 FGFP1_MOUSE Fibroblast growth factor-binding protein 1 (FGF-BP) (FGF-BP1) (FGF-binding protein 1) (FGFBP-1) 251 28,294 Chain (1); Disulfide bond (5); Glycosylation (1); Region (1); Sequence conflict (3); Signal peptide (1) FUNCTION: Acts as a carrier protein that releases fibroblast-binding factors (FGFs) from the extracellular matrix (EM) storage and thus enhances the mitogenic activity of FGFs. Enhances FGF2 signaling during tissue repair, angiogenesis and in tumor growth (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250|UniProtKB:Q14512}. Cell membrane {ECO:0000250|UniProtKB:Q14512}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q14512}. Note=Extracellular and plasma membrane-associated. {ECO:0000250|UniProtKB:Q14512}. SUBUNIT: Found in a complex with FGFBP1, FGF1 and FGF2. Interacts with FGF1, FGF7, FGF10, FGF22 and HSPG2 (By similarity). Interacts with FGF2. {ECO:0000250, ECO:0000269|PubMed:9178765}. TISSUE SPECIFICITY: Expressed in intestine, ovary, lung, placenta and normal and wounded skin. {ECO:0000269|PubMed:15806171, ECO:0000269|PubMed:9178765}. +O35453 HEPS_MOUSE Serine protease hepsin (EC 3.4.21.106) [Cleaved into: Serine protease hepsin non-catalytic chain; Serine protease hepsin catalytic chain] 436 46,821 Active site (3); Alternative sequence (1); Chain (2); Disulfide bond (8); Domain (2); Frameshift (1); Glycosylation (1); Mutagenesis (1); Sequence conflict (6); Topological domain (2); Transmembrane (1) TRANSMEM 39 59 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 38 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 60 436 Extracellular. {ECO:0000255}. FUNCTION: Serine protease that cleaves extracellular substrates, and contributes to the proteolytic processing of growth factors, such as HGF and MST1/HGFL. Plays a role in cell growth and maintenance of cell morphology. Plays a role in the proteolytic processing of ACE2 (By similarity). Mediates the proteolytic cleavage of urinary UMOD that is required for UMOD polymerization (PubMed:26673890). {ECO:0000250|UniProtKB:P05981, ECO:0000269|PubMed:26673890}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:26673890}; Single-pass type II membrane protein {ECO:0000305}. Cell membrane {ECO:0000250|UniProtKB:P05981}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P05981}.; SUBCELLULAR LOCATION: Isoform 2: Secreted {ECO:0000269|PubMed:9395459}. TISSUE SPECIFICITY: Detected in kidney, in thick ascending tubule epithelial cells (at protein level) (PubMed:26673890). Detected in kidney and liver (PubMed:9395459, PubMed:9435303). {ECO:0000269|PubMed:9395459, ECO:0000269|PubMed:9435303}. +P63075 FGF17_MOUSE Fibroblast growth factor 17 (FGF-17) 216 24,924 Chain (1); Glycosylation (1); Signal peptide (1) FUNCTION: Plays an important role in the regulation of embryonic development and as signaling molecule in the induction and patterning of the embryonic brain. Required for normal brain development. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Interacts with FGFR3 and FGFR4. {ECO:0000250}. +P14234 FGR_MOUSE Tyrosine-protein kinase Fgr (EC 2.7.10.2) (Proto-oncogene c-Fgr) (p55-Fgr) 517 58,867 Active site (1); Binding site (1); Chain (1); Domain (3); Initiator methionine (1); Lipidation (3); Modified residue (7); Mutagenesis (2); Nucleotide binding (1); Sequence conflict (4) FUNCTION: Non-receptor tyrosine-protein kinase that transmits signals from cell surface receptors devoid of kinase activity and contributes to the regulation of immune responses, including neutrophil, monocyte, macrophage and mast cell functions, cytoskeleton remodeling in response to extracellular stimuli, phagocytosis, cell adhesion and migration. Promotes mast cell degranulation, release of inflammatory cytokines and IgE-mediated anaphylaxis. Acts downstream of receptors that bind the Fc region of immunoglobulins, such as MS4A2/FCER1B, FCER1G and FCGR2. Acts downstream of ITGB1 and ITGB2, and regulates actin cytoskeleton reorganization, cell spreading and adhesion. Depending on the context, activates or inhibits cellular responses. Functions as negative regulator of ITGB2 signaling, phagocytosis and SYK activity in monocytes (PubMed:11672534). Required for normal ITGB1 and ITGB2 signaling, normal cell spreading and adhesion in neutrophils and macrophages (PubMed:8666673 and PubMed:9687507). Functions as positive regulator of cell migration and regulates cytoskeleton reorganization via RAC1 activation (PubMed:15561106). Phosphorylates SYK (in vitro) and promotes SYK-dependent activation of AKT1 and MAP kinase signaling (PubMed:21746961). Phosphorylates PLD2 in antigen-stimulated mast cells, leading to PLD2 activation and the production of the signaling molecules lysophosphatidic acid and diacylglycerol. Promotes activation of PIK3R1. Phosphorylates FASLG, and thereby regulates its ubiquitination and subsequent internalization. Phosphorylates ABL1. Promotes phosphorylation of CBL, CTTN, PIK3R1, PTK2/FAK1, PTK2B/PYK2 and VAV2. Phosphorylates HCLS1 that has already been phosphorylated by SYK, but not unphosphorylated HCLS1. {ECO:0000269|PubMed:10662797, ECO:0000269|PubMed:11672534, ECO:0000269|PubMed:15561106, ECO:0000269|PubMed:19903482, ECO:0000269|PubMed:21746961, ECO:0000269|PubMed:8125254, ECO:0000269|PubMed:8666673, ECO:0000269|PubMed:9687507}. PTM: Ubiquitinated. Becomes ubiquitinated in response to ITGB2 signaling; this does not lead to degradation (By similarity). {ECO:0000250}.; PTM: Phosphorylated. Autophosphorylated on tyrosine residues. Becomes phosphorylated in response to FCGR2 engagement, cell adhesion and signaling by ITGB2. Prior phosphorylation at Tyr-511 by SRC inhibits ulterior autophosphorylation at Tyr-400 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:15561106}; Lipid-anchor {ECO:0000305|PubMed:15561106}; Cytoplasmic side {ECO:0000305|PubMed:15561106}. Cell membrane {ECO:0000269|PubMed:15561106}; Peripheral membrane protein {ECO:0000269|PubMed:15561106}; Cytoplasmic side {ECO:0000269|PubMed:15561106}. Cell projection, ruffle membrane {ECO:0000269|PubMed:15561106}. Cytoplasm, cytosol {ECO:0000269|PubMed:15561106}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15561106}. Mitochondrion inner membrane {ECO:0000250}. Mitochondrion intermembrane space {ECO:0000250}. Note=Detected in mitochondrial intermembrane space and at inner membranes (By similarity). Colocalizes with actin fibers at membrane ruffles. Detected at plasma membrane lipid rafts. {ECO:0000250}. SUBUNIT: Interacts with ITGB1, ITGB2, MS4A2/FCER1B, FCER1G and FCGR2. Interacts (via SH2 domain) with SYK (tyrosine phosphorylated). Interacts (via SH2 domain) with FLT3 (tyrosine phosphorylated). Interacts with PTK2/FAK1. Interacts (via SH2 domain) with HCLS1 (tyrosine phosphorylated by SYK). Interacts with SIRPA and PTPNS1. Interacts (not phosphorylated on tyrosine residues) with CBL; FGR tyrosine phosphorylation promotes dissociation (By similarity). {ECO:0000250}. +P15656 FGF5_MOUSE Fibroblast growth factor 5 (FGF-5) (Heparin-binding growth factor 5) (HBGF-5) 264 29,103 Alternative sequence (2); Chain (1); Compositional bias (1); Glycosylation (1); Signal peptide (1) FUNCTION: Plays an important role in the regulation of cell proliferation and cell differentiation. Required for normal regulation of the hair growth cycle. Functions as an inhibitor of hair elongation by promoting progression from anagen, the growth phase of the hair follicle, into catagen the apoptosis-induced regression phase (By similarity). {ECO:0000250|UniProtKB:Q20FD0}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. SUBUNIT: Interacts with FGFR1 and FGFR2. Affinity between fibroblast growth factors (FGFs) and their receptors is increased by heparan sulfate glycosaminoglycans that function as coreceptors (By similarity). {ECO:0000250}. +P21803 FGFR2_MOUSE Fibroblast growth factor receptor 2 (FGFR-2) (EC 2.7.10.1) (Keratinocyte growth factor receptor) (KGFR) (CD antigen CD332) 821 91,984 Active site (1); Alternative sequence (3); Beta strand (8); Binding site (2); Chain (1); Disulfide bond (3); Domain (4); Glycosylation (9); Helix (1); Modified residue (7); Mutagenesis (1); Nucleotide binding (2); Region (1); Sequence conflict (14); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 378 398 Helical. {ECO:0000255}. TOPO_DOM 22 377 Extracellular. {ECO:0000255}.; TOPO_DOM 399 821 Cytoplasmic. {ECO:0000255}. FUNCTION: Tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of cell proliferation, differentiation, migration and apoptosis, and in the regulation of embryonic development. Required for normal embryonic patterning, trophoblast function, limb bud development, lung morphogenesis, osteogenesis and skin development. Plays an essential role in the regulation of osteoblast differentiation, proliferation and apoptosis, and is required for normal skeleton development. Promotes cell proliferation in keratinocytes and immature osteoblasts, but promotes apoptosis in differentiated osteoblasts. Phosphorylates PLCG1, FRS2 and PAK4. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. FGFR2 signaling is down-regulated by ubiquitination, internalization and degradation. Mutations that lead to constitutive kinase activation or impair normal FGFR2 maturation, internalization and degradation lead to aberrant signaling. Over-expressed FGFR2 promotes activation of STAT1. {ECO:0000269|PubMed:10851026, ECO:0000269|PubMed:15629145, ECO:0000269|PubMed:8393815, ECO:0000269|PubMed:8663044}. PTM: Autophosphorylated. Binding of FGF family members together with heparan sulfate proteoglycan or heparin promotes receptor dimerization and autophosphorylation on tyrosine residues. Autophosphorylation occurs in trans between the two FGFR molecules present in the dimer (By similarity). {ECO:0000250}.; PTM: N-glycosylated in the endoplasmic reticulum. The N-glycan chains undergo further maturation to an Endo H-resistant form in the Golgi apparatus (By similarity). {ECO:0000250}.; PTM: Ubiquitinated. FGFR2 is rapidly ubiquitinated after autophosphorylation, leading to internalization and degradation. Subject to degradation both in lysosomes and by the proteasome (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Golgi apparatus {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Note=Detected on osteoblast plasma membrane lipid rafts. After ligand binding, the activated receptor is rapidly internalized and degraded (By similarity). {ECO:0000250}. SUBUNIT: Monomer. Homodimer after ligand binding. Interacts predominantly with FGF1 and FGF2, but can also interact with FGF3, FGF4, FGF6, FGF7, FGF8, FGF9, FGF10, FGF17, FGF18 and FGF22 (in vitro) (PubMed:8663044). Ligand specificity is determined by tissue-specific expression of isoforms, and differences in the third Ig-like domain are crucial for ligand specificity. Affinity for fibroblast growth factors (FGFs) is increased by heparan sulfate glycosaminoglycans that function as coreceptors. Likewise, KLB increases the affinity for FGF19 and FGF21. Interacts with PLCG1 (PubMed:15629145). Interacts with GRB2 and PAK4 (By similarity). Interacts with FLRT2 (PubMed:21765038). {ECO:0000250|UniProtKB:P21802, ECO:0000269|PubMed:15629145, ECO:0000269|PubMed:21765038, ECO:0000269|PubMed:8663044}. DOMAIN: The second and third Ig-like domains directly interact with fibroblast growth factors (FGF) and heparan sulfate proteoglycans. Alternative splicing events affecting the third Ig-like domain are crucial for ligand selectivity (By similarity). {ECO:0000250}. +Q91WF7 FIG4_MOUSE Polyphosphoinositide phosphatase (EC 3.1.3.-) (Phosphatidylinositol 3,5-bisphosphate 5-phosphatase) (SAC domain-containing protein 3) 907 103,447 Chain (1); Domain (1) FUNCTION: The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). In vitro, hydrolyzes all three D5-phosphorylated polyphosphoinositide substrates in the order PtdIns(4,5)P2 > PtdIns(3,5)P2 > PtdIns(3,4,5)P3. Plays a role in the biogenesis of endosome carrier vesicles (ECV) / multivesicular bodies (MVB) transport intermediates from early endosomes. {ECO:0000269|PubMed:17572665, ECO:0000269|PubMed:19037259}. SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:19037259}. Note=Localization requires VAC14 and PIKFYVE. SUBUNIT: Component of the PI(3,5)P2 regulatory complex/PAS complex, at least composed of PIKFYVE, FIG4 and WIPI1. VAC14 nucleates the assembly of the complex and serves as a scaffold. {ECO:0000269|PubMed:19037259}. TISSUE SPECIFICITY: Wide-spread. {ECO:0000269|PubMed:17572665}. "DISEASE: Note=Defects in Fig4 are the cause of the pale tremor phenotype which is a multi-organ disorder with neuronal degeneration in the central nervous system, peripheral neuronopathy and diluted pigmentation. At postnatal day three (P3), affected homozygotes have diluted pigmentation and reduced size. Intentional tremor develops during the second week after birth, and abnormal limb postures are evident by the third week. There is impaired motor coordination, muscle weakness and ""swimming"" gait. There is progressive loss of mobility, reduction in body weight and juvenile lethality. {ECO:0000269|PubMed:17572665}." +Q03142 FGFR4_MOUSE Fibroblast growth factor receptor 4 (FGFR-4) (EC 2.7.10.1) (Protein-tyrosine kinase receptor MPK-11) (CD antigen CD334) 799 88,661 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Disulfide bond (3); Domain (4); Glycosylation (5); Modified residue (4); Mutagenesis (1); Nucleotide binding (1); Sequence conflict (8); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 367 387 Helical. {ECO:0000255}. TOPO_DOM 17 366 Extracellular. {ECO:0000255}.; TOPO_DOM 388 799 Cytoplasmic. {ECO:0000255}. FUNCTION: Tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays a role in the regulation of cell proliferation, differentiation and migration, and in regulation of lipid metabolism, bile acid biosynthesis, glucose uptake, vitamin D metabolism and phosphate homeostasis. Required for normal down-regulation of the expression of CYP7A1, the rate-limiting enzyme in bile acid synthesis, in response to FGF19. Phosphorylates PLCG1 and FRS2. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Promotes SRC-dependent phosphorylation of the matrix protease MMP14 and its lysosomal degradation. FGFR4 signaling is down-regulated by receptor internalization and degradation; MMP14 promotes internalization and degradation of FGFR4. Plays a role in postnatal lung development. May be involved in the development of skeletal muscle cell lineages. {ECO:0000269|PubMed:10809780, ECO:0000269|PubMed:17664243, ECO:0000269|PubMed:19237543, ECO:0000269|PubMed:21561999, ECO:0000269|PubMed:9716527}. PTM: N-glycosylated. Isoform 1 and isoform 2 are glycosylated. Full maturation of the glycan chains in the Golgi is essential for high affinity interaction with FGF19 (By similarity). {ECO:0000250}.; PTM: Ubiquitinated. Subject to proteasomal degradation when not fully glycosylated (By similarity). {ECO:0000250}.; PTM: Autophosphorylated. Binding of FGF family members together with heparan sulfate proteoglycan or heparin promotes receptor dimerization and autophosphorylation on tyrosine residues. Autophosphorylation occurs in trans between the two FGFR molecules present in the dimer. Isoform 1 and isoform 2 are phosphorylated on tyrosine residues (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18186042}; Single-pass type I membrane protein {ECO:0000269|PubMed:18186042}. Endosome {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Note=Internalized from the cell membrane to recycling endosomes, and from there back to the cell membrane. {ECO:0000250}. SUBUNIT: Monomer. Homodimer after ligand binding. Interacts with FGF1, FGF2, FGF4, FGF6, FGF8, FGF9, FGF16, FGF17, FGF18, FGF19, FGF21 and FGF23 (in vitro). Binding affinity for FGF family members is enhanced by interactions between FGFs and heparan sulfate proteoglycans. Interacts with KLB; this strongly increases the affinity for FGF19 and FGF23. Affinity for FGF19 is strongly increased by KLB and sulfated glycosaminoglycans. KLB and KL both interact with the core-glycosylated FGFR4 in the endoplasmic reticulum and promote its degradation, so that only FGFR4 with fully mature N-glycans is expressed at the cell surface. Identified in a complex with NCAM1, CDH2, PLCG1, FRS2, SRC, SHC1, GAP43 and CTTN. Interacts with MMP14 and HIP1. Interacts with STAT3 (By similarity). {ECO:0000250|UniProtKB:P22455}. TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in lung and proliferating myoblasts and myotubes of primary myogenic cells (at protein level). Isoform 1 and isoform 2 are expressed in liver, muscle, spleen, heart, lung, kidney and in primary myogenic cells. {ECO:0000269|PubMed:1723680, ECO:0000269|PubMed:18186042}. +O55208 FIGLA_MOUSE Factor in the germline alpha (FIGalpha) (Transcription factor FIGa) 194 21,529 Chain (1); Domain (1) FUNCTION: Germ-line specific transcription factor implicated in postnatal oocyte-specific gene expression. Plays a key regulatory role in the expression of multiple oocyte-specific genes, including those that initiate folliculogenesis and those that encode the zona pellucida (ZP1, ZP2 and ZP3) required for fertilization and early embryonic survival. Essential for oocytes to survive and form primordial follicles. The persistence of FIGLA in adult females suggests that it may regulate additional pathways that are essential for normal ovarian development. Binds to the E-box (5'-CANNTG-3') of the ZPs (ZP1, ZP2, ZP3) promoters. {ECO:0000269|PubMed:11023867}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Heterodimer with TCF3/isoform E12. TISSUE SPECIFICITY: Expressed only in the oocytes within the ovary and at lower level in the testis. Found in the resting oocytes of the primordial follicle cells, at the periphery of the ovary and in the hilar region. Also detected in growing oocytes, but at lower levels. +O70433 FHL2_MOUSE Four and a half LIM domains protein 2 (FHL-2) (Skeletal muscle LIM-protein 3) (SLIM-3) 279 32,073 Chain (1); Cross-link (3); Domain (4); Modified residue (1); Zinc finger (1) FUNCTION: May function as a molecular transmitter linking various signaling pathways to transcriptional regulation. Negatively regulates the transcriptional repressor E4F1 and may function in cell growth. Inhibits the transcriptional activity of FOXO1 and its apoptotic function by enhancing the interaction of FOXO1 with SIRT1 and FOXO1 deacetylation (By similarity). Negatively regulates the calcineurin/NFAT signaling pathway in cardiomyocytes (PubMed:22851699). {ECO:0000250|UniProtKB:Q14192, ECO:0000269|PubMed:22851699}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:22851699}. SUBUNIT: Interacts with ZNF638 and TTN/titin. Interacts with E4F1. Interacts with GRB7. Interacts with SIRT1 and FOXO1. Interacts with CEFIP (By similarity). Interacts with calcineurin (PubMed:22851699). {ECO:0000250|UniProtKB:Q14192, ECO:0000269|PubMed:22851699}. DOMAIN: The third LIM zinc-binding mediates interaction with E4F1. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in heart but also detectable in brain and skeletal muscle. {ECO:0000269|PubMed:10906474}. +P11276 FINC_MOUSE Fibronectin (FN) [Cleaved into: Anastellin] 2477 272,538 Beta strand (15); Chain (2); Cross-link (3); DNA binding (1); Disulfide bond (30); Domain (31); Glycosylation (8); Modified residue (7); Motif (2); Mutagenesis (5); Region (6); Sequence conflict (3); Signal peptide (1) FUNCTION: Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape healing, and maintenance of cell shape. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization. Participates in the regulation of type I collagen deposition by osteoblasts. {ECO:0000269|PubMed:21768292}.; FUNCTION: Anastellin binds fibronectin and induces fibril formation. This fibronectin polymer, named superfibronectin, exhibits enhanced adhesive properties. Both anastellin and superfibronectin inhibit tumor growth, angiogenesis and metastasis. Anastellin activates p38 MAPK and inhibits lysophospholipid signaling (By similarity). {ECO:0000250}. PTM: Sulfated. {ECO:0000250}.; PTM: Forms covalent cross-links mediated by a transglutaminase, such as F13A or TGM2, between a glutamine and the epsilon-amino group of a lysine residue, forming homopolymers and heteropolymers (e.g. fibrinogen-fibronectin, collagen-fibronectin heteropolymers). {ECO:0000269|PubMed:9312106}.; PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000250|UniProtKB:P02751}.; PTM: Proteolytic processing produces the C-terminal NC1 peptide, anastellin. {ECO:0000250}.; PTM: Some lysine residues are oxidized to allysine by LOXL3, promoting fibronectin activation and matrix formation. {ECO:0000269|PubMed:26954549}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SUBUNIT: Mostly heterodimers or multimers of alternatively spliced variants, connected by 2 disulfide bonds near the carboxyl ends; to a lesser extent homodimers. Interacts with FBLN1, AMBP, LGALS3BP and COL13A1 and COMP (By similarity). Interacts with TNR; interaction mediates inhibition of cell adhesion and neurite outgrowth. Interacts with FBLN7. Interacts with FST3 and MYOC (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Plasma FN (soluble dimeric form) is secreted by hepatocytes. Cellular FN (dimeric or cross-linked multimeric forms), made by fibroblasts, epithelial and other cell types, is deposited as fibrils in the extracellular matrix. +Q9Z247 FKBP9_MOUSE Peptidyl-prolyl cis-trans isomerase FKBP9 (PPIase FKBP9) (EC 5.2.1.8) (63 kDa FK506-binding protein) (63 kDa FKBP) (FKBP-63) (FK506-binding protein 9) (FKBP-9) (FKBP65RS) (Rotamase) 570 62,995 Calcium binding (2); Chain (1); Domain (6); Glycosylation (4); Motif (1); Sequence conflict (13); Signal peptide (1) FUNCTION: PPIases accelerate the folding of proteins during protein synthesis. PTM: Phosphorylated. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138, ECO:0000269|PubMed:10524204}. TISSUE SPECIFICITY: Predominantly expressed in heart, skeletal muscle, lung, liver and kidney. Lower levels found in brain, spleen and testis. {ECO:0000269|PubMed:10524204, ECO:0000269|PubMed:11710534}. +O35450 FKBPL_MOUSE FK506-binding protein-like (WAF-1/CIP1 stabilizing protein 39) (WISp39) 347 38,302 Chain (1); Modified residue (1); Repeat (3); Sequence conflict (2) FUNCTION: May be involved in response to X-ray. Regulates p21 protein stability by binding to Hsp90 and p21. {ECO:0000250}. SUBUNIT: Forms a ternary complex with CDKN1A/p21 and HSP90AB1/Hsp90. {ECO:0000250}. +Q9JJ28 FLII_MOUSE Protein flightless-1 homolog 1271 144,803 Chain (1); Compositional bias (1); Modified residue (5); Region (2); Repeat (20); Sequence caution (1); Sequence conflict (2) FUNCTION: May play a role as coactivator in transcriptional activation by hormone-activated nuclear receptors (NR) and acts in cooperation with NCOA2 and CARM1. Involved in estrogen hormone signaling (By similarity). Essential for early embryonic development. May play a role in regulation of cytoskeletal rearrangements involved in cytokinesis and cell migration, by inhibiting Rac1-dependent paxillin phosphorylation. {ECO:0000250, ECO:0000269|PubMed:11171324, ECO:0000269|PubMed:11971982, ECO:0000269|PubMed:21430700, ECO:0000269|PubMed:22581781}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cell junction, focal adhesion. Note=Colocalizes to actin-rich structures in blastocysts and, together with HRAS, RHOA and CDC42, in migrating fibroblasts. Localizes to centrosomes. SUBUNIT: Interacts with actin, ACTL6A, NCOA2 and MYD88 (By similarity). Interacts with LRRFIP1 and LRRFIP2. Upon LPS stimulation, LRRFIP2 competes for MYD88-binding. LRRFIP1 constitutively blocks the interaction with MyD88, even in the absence of LPS (By similarity). Interacts with the nuclear receptors ESR1 and THRB (By similarity). Interacts with CARM1. Interacts with SGK3. {ECO:0000250, ECO:0000269|PubMed:14966289}. TISSUE SPECIFICITY: Expressed in blastocyst. {ECO:0000269|PubMed:10947868}. +Q7TSA3 BTLA_MOUSE B- and T-lymphocyte attenuator (B- and T-lymphocyte-associated protein) (CD antigen CD272) 306 34,337 Alternative sequence (2); Beta strand (11); Chain (1); Disulfide bond (3); Domain (1); Glycosylation (6); Helix (1); Mutagenesis (7); Natural variant (9); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 184 204 Helical. {ECO:0000255}. TOPO_DOM 30 183 Extracellular. {ECO:0000255}.; TOPO_DOM 205 306 Cytoplasmic. {ECO:0000255}. FUNCTION: Inhibitory receptor on lymphocytes that negatively regulates antigen receptor signaling via PTPN6/SHP-1 and PTPN11/SHP-2 (PubMed:12796776, PubMed:14652006). May interact in cis (on the same cell) or in trans (on other cells) with TNFRSF14 (PubMed:19915044). In cis interactions, appears to play an immune regulatory role inhibiting in trans interactions in naive T cells to maintain a resting state. In trans interactions, can predominate during adaptive immune response to provide survival signals to effector T cells (PubMed:19915044). {ECO:0000269|PubMed:12796776, ECO:0000269|PubMed:14652006, ECO:0000269|PubMed:19915044}. PTM: Phosphorylated on Tyr residues by TNFRSF14 and by antigen receptors cross-linking, both inducing association with PTPN6 and PTPN11. {ECO:0000269|PubMed:15568026}.; PTM: N-glycosylated. {ECO:0000269|PubMed:12796776}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12796776}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Interacts with tyrosine phosphatases PTPN6/SHP-1 and PTPN11/SHP-2 (PubMed:12796776, PubMed:14652006). Interacts with TNFRSF14/HVEM (via cysteine-rich domain 1) (PubMed:19915044). {ECO:0000269|PubMed:12796776, ECO:0000269|PubMed:14652006, ECO:0000269|PubMed:15568026, ECO:0000269|PubMed:18178834, ECO:0000269|PubMed:19915044}. TISSUE SPECIFICITY: Expressed in splenic T- and B-cells as well as lymph node tissues but very weakly in somatic tissues. Also expressed in macrophages, NK cells and dendritic cells. A polymorphic tissue distribution between several strains is seen. {ECO:0000269|PubMed:12796776, ECO:0000269|PubMed:15749870}. +Q8R149 BUD13_MOUSE BUD13 homolog 637 72,139 Alternative sequence (1); Chain (1); Coiled coil (1); Compositional bias (1); Cross-link (1); Modified residue (31); Sequence conflict (2) FUNCTION: Involved in pre-mRNA splicing as component of the activated spliceosome. {ECO:0000250|UniProtKB:Q9BRD0}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BRD0}. SUBUNIT: Part of the activated spliceosome B/catalytic step 1 spliceosome, one of the forms of the spliceosome which has a well-formed active site but still cannot catalyze the branching reaction and is composed of at least 52 proteins, the U2, U5 and U6 snRNAs and the pre-mRNA. {ECO:0000250|UniProtKB:Q9BRD0}. +P14106 C1QB_MOUSE Complement C1q subcomponent subunit B 253 26,717 Chain (1); Disulfide bond (1); Domain (2); Modified residue (16); Sequence conflict (1); Signal peptide (1) FUNCTION: C1q associates with the proenzymes C1r and C1s to yield C1, the first component of the serum complement system. The collagen-like regions of C1q interact with the Ca(2+)-dependent C1r(2)C1s(2) proenzyme complex, and efficient activation of C1 takes place on interaction of the globular heads of C1q with the Fc regions of IgG or IgM antibody present in immune complexes. PTM: Hydroxylated on lysine and proline residues. Hydroxylated lysine residues can be glycosylated. Mouse C1Q contains up to 64.0 hydroxylysine-galactosylglucose residues. Total percentage hydroxylysine residues glycosylated is 95.1%. Contains no hydroxylysine-monosaccharides. {ECO:0000269|PubMed:6286235}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: C1 is a calcium-dependent trimolecular complex of C1q, R and S in the molar ration of 1:2:2. C1q subcomponent is composed of nine subunits, six of which are disulfide-linked dimers of the A and B chains, and three of which are disulfide-linked dimers of the C chain. TISSUE SPECIFICITY: Highest expression in thioglycolate-activated peritoneal macrophages. Also found in spleen, thymus and heart. Very weak expression liver, kidney, lung and intestine. {ECO:0000269|PubMed:2591537}. +Q02105 C1QC_MOUSE Complement C1q subcomponent subunit C 246 25,992 Chain (1); Disulfide bond (1); Domain (2); Modified residue (10); Sequence conflict (10); Signal peptide (1) FUNCTION: C1q associates with the proenzymes C1r and C1s to yield C1, the first component of the serum complement system. The collagen-like regions of C1q interact with the Ca(2+)-dependent C1r(2)C1s(2) proenzyme complex, and efficient activation of C1 takes place on interaction of the globular heads of C1q with the Fc regions of IgG or IgM antibody present in immune complexes. PTM: Hydroxylation on proline residues within the sequence motif, GXPG, is most likely to be 4-hydroxy as this fits the requirement for 4-hydroxylation in vertebrates. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: C1 is a calcium-dependent trimolecular complex of C1q, R and S in the molar ration of 1:2:2. C1q subcomponent is composed of nine subunits, six of which are disulfide-linked dimers of the A and B chains, and three of which are disulfide-linked dimers of the C chain. +Q4ZJM9 C1QL4_MOUSE Complement C1q-like protein 4 (C1q and tumor necrosis factor-related protein 11) (C1q/TNF-related protein 11) (C1qTNF11) (CTRP11) 238 24,928 Chain (1); Domain (2); Mutagenesis (2); Signal peptide (1) FUNCTION: May regulate the number of excitatory synapses that are formed on hippocampus neurons. Has no effect on inhibitory synapses. May inhibit adipocyte differentiation at an early stage of the process. {ECO:0000269|PubMed:21262840, ECO:0000269|PubMed:23449976}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23449976}. SUBUNIT: Forms homooligomers, predominantly dimers or trimers. Forms heterooligomers with C1QL1, C1QL2 and C1QL3, when proteins are coexpressed; this interaction does not occur after secretion (PubMed:23449976). Interacts with ADGRB3 (PubMed:21262840). {ECO:0000269|PubMed:21262840, ECO:0000269|PubMed:23449976}. TISSUE SPECIFICITY: Highly expressed in testis and adipose tissue, brown adipose tissue expressing higher levels than subcutaneous and visceral white adipose tissue. In gonadal fat pad, expressed at lower levels in adipocytes than in the stromal vascular fraction (VSP), which contains preadipocytes, fibroblasts, endothelial cells and occasional immune cells. Expression exhibits sexually dimorphism, with higher levels in females than in males. {ECO:0000269|PubMed:23449976}. +Q91ZX1 C209A_MOUSE CD209 antigen-like protein A (Dendritic cell-specific ICAM-3-grabbing non-integrin) (DC-SIGN) (CD antigen CD209) 238 27,149 Alternative sequence (1); Chain (1); Disulfide bond (3); Domain (1); Glycosylation (2); Metal binding (6); Topological domain (2); Transmembrane (1) TRANSMEM 52 72 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 51 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 73 238 Extracellular. {ECO:0000255}. FUNCTION: Probable pathogen-recognition receptor. May mediate the endocytosis of pathogens which are subsequently degraded in lysosomal compartments. May recognize in a calcium-dependent manner high mannose N-linked oligosaccharides in a variety of pathogen antigens. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Predominantly expressed in dendritic cells. Detected at very low levels in lung, spleen, lymph nodes and bone marrow. {ECO:0000269|PubMed:11581173, ECO:0000269|PubMed:11684292}. +Q91ZW9 C209C_MOUSE CD209 antigen-like protein C (DC-SIGN-related protein 2) (DC-SIGNR2) (CD antigen CD209) 178 21,245 Chain (1); Disulfide bond (3); Domain (1); Glycosylation (1); Metal binding (5) FUNCTION: Probable pathogen-recognition receptor. May recognize in a calcium-dependent manner high mannose N-linked oligosaccharides in a variety of pathogen antigens. +Q9QXP7 C1QT1_MOUSE Complement C1q tumor necrosis factor-related protein 1 (Putative secreted protein ZSIG37) 281 32,009 Chain (1); Domain (2); Glycosylation (1); Sequence conflict (2); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q9D8U4 C1QT2_MOUSE Complement C1q tumor necrosis factor-related protein 2 (mCTRP2) 294 30,865 Chain (1); Domain (2); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. SUBUNIT: May interact with ERFE. +Q9ES30 C1QT3_MOUSE Complement C1q tumor necrosis factor-related protein 3 (Collagenous repeat-containing sequence 26 kDa protein) (CORS26) (Secretory protein CORS26) 246 26,828 Chain (1); Domain (2); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q8BGH7 C42S2_MOUSE CDC42 small effector protein 2 84 9,223 Chain (1); Compositional bias (1); Domain (1); Lipidation (2); Modified residue (2); Sequence conflict (1) FUNCTION: Probably involved in the organization of the actin cytoskeleton by acting downstream of CDC42, inducing actin filament assembly. Alters CDC42-induced cell shape changes. In activated T-cells, may play a role in CDC42-mediated F-actin accumulation at the immunological synapse. May play a role in early contractile events in phagocytosis in macrophages (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Cell projection, phagocytic cup {ECO:0000250}. Note=Recruited to the activated TCR prior actin polymerization. Localizes at the phagocytic cup of macrophages. {ECO:0000250}. SUBUNIT: Interacts with CDC42 (in GTP-bound form). Interacts weakly with RAC1 and not at all with RHOA (By similarity). {ECO:0000250}. DOMAIN: The CRIB domain mediates interaction with CDC42. {ECO:0000250}. TISSUE SPECIFICITY: Detected in spleen, thymus and lung (at protein level). {ECO:0000269|PubMed:15840583}. +Q8CG16 C1RA_MOUSE Complement C1r-A subcomponent (EC 3.4.21.41) (Complement component 1 subcomponent r-A) [Cleaved into: Complement C1r-A subcomponent heavy chain; Complement C1r-A subcomponent light chain] 707 80,073 Active site (3); Chain (3); Disulfide bond (13); Domain (6); Glycosylation (3); Modified residue (2); Sequence conflict (2); Signal peptide (1) FUNCTION: C1r B chain is a serine protease that combines with C1q and C1s to form C1, the first component of the classical pathway of the complement system. PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}. SUBUNIT: C1 is a calcium-dependent trimolecular complex of C1q, C1r and C1s in the molar ration of 1:2:2. C1r is a dimer of identical chains, each of which is activated by cleavage into two chains, A and B, connected by disulfide bonds (By similarity). {ECO:0000250}. +Q06138 CAB39_MOUSE Calcium-binding protein 39 (MO25alpha) (Protein Mo25) 341 39,843 Chain (1); Sequence conflict (1) FUNCTION: Component of a complex that binds and activates STK11/LKB1. In the complex, required to stabilize the interaction between CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta) and STK11/LKB1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. SUBUNIT: Component of a trimeric complex composed of STK11/LKB1, STRAD (STRADA or STRADB) and CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta): the complex tethers STK11/LKB1 in the cytoplasm and stimulates its catalytic activity. {ECO:0000250}. +Q8VDY9 CAAP1_MOUSE Caspase activity and apoptosis inhibitor 1 (Conserved anti-apoptotic protein) (CAAP) 356 37,825 Chain (1); Coiled coil (1); Compositional bias (1); Cross-link (1); Modified residue (5); Sequence conflict (4) FUNCTION: Anti-apoptotic protein that modulates a caspase-10 dependent mitochondrial caspase-3/9 feedback amplification loop. {ECO:0000250}. +Q9ESJ1 CABL1_MOUSE CDK5 and ABL1 enzyme substrate 1 (Interactor with CDK3 1) (Ik3-1) 568 61,429 Chain (1); Compositional bias (1); Modified residue (3); Mutagenesis (2); Region (2); Sequence conflict (5) FUNCTION: Cyclin-dependent kinase binding protein. Enhances cyclin-dependent kinase tyrosine phosphorylation by nonreceptor tyrosine kinases, such as that of CDK5 by activated ABL1, which leads to increased CDK5 activity and is critical for neuronal development, and that of CDK2 by WEE1, which leads to decreased CDK2 activity and growth inhibition. Positively affects neuronal outgrowth. Plays a role as a regulator for p53/p73-induced cell death (By similarity). {ECO:0000250, ECO:0000269|PubMed:11706030}. PTM: Phosphorylated on Ser-274 by CCNE1/CDK3. Phosphorylated on serine/threonine residues by CDK5 and on tyrosine residues by ABL1. Also phosphorylated in vitro by CCNA1/CDK2, CCNE1/CDK2, CCNA1/CDK3 and CCNE1/CDK3. {ECO:0000269|PubMed:10896159, ECO:0000269|PubMed:11733001}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cell projection, growth cone. Note=Located in the cell body and proximal region of the developing axonal shaft of immature neurons. Located in axonal growth cone, but not in the distal part of the axon shaft or in dendritic growth cone of mature neurons. SUBUNIT: Found in a complex with p53/TP53 (By similarity). Found in a number of complexes with CDK2, CDK3, CDK5, ABL1, TDRD7, CDK17, CCNA1, CCNE1 and TP73. Interacts with CDK2, CDK3, CDK5, ABL1 and TDRD7. {ECO:0000250, ECO:0000269|PubMed:10873625, ECO:0000269|PubMed:10896159, ECO:0000269|PubMed:11527406, ECO:0000269|PubMed:11585773, ECO:0000269|PubMed:11706030}. TISSUE SPECIFICITY: Ubiquitous. Expressed in postnatal day 1 (P1), in postmitotic neurons of the subplate, cortex (V/VI) and marginal zone; in postnatal day 7 (P7), in all layers of the cerebral cortex and in the CA1 and CA2 regions of the hippocampus (at protein level). Highly expressed in brain, kidney, liver and lung. {ECO:0000269|PubMed:10873625, ECO:0000269|PubMed:10896159}. +Q8K3M5 CABL2_MOUSE CDK5 and ABL1 enzyme substrate 2 (Interactor with CDK3 2) (Ik3-2) 476 52,082 Chain (1); Compositional bias (2); Erroneous initiation (1); Modified residue (2) FUNCTION: Unknown. Probably involved in G1-S cell cycle transition. SUBUNIT: Binds to CDK3, CDK5 and ABL1. The C-terminal cyclin-box-like region binds to CDK5. {ECO:0000269|PubMed:11955625}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11955625}. +P54285 CACB3_MOUSE Voltage-dependent L-type calcium channel subunit beta-3 (CAB3) (Calcium channel voltage-dependent subunit beta 3) (CCHB3) 484 54,572 Chain (1); Domain (1); Modified residue (2); Region (1); Sequence conflict (7) FUNCTION: Regulatory subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents (PubMed:24751537). Increases CACNA1B peak calcium current and shifts the voltage dependencies of channel activation and inactivation (By similarity). Increases CACNA1C peak calcium current and shifts the voltage dependencies of channel activation and inactivation (By similarity). {ECO:0000250|UniProtKB:P54287, ECO:0000250|UniProtKB:Q9MZL3, ECO:0000269|PubMed:24751537}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:21831364}. SUBUNIT: Component of a calcium channel complex consisting of a pore-forming alpha subunit (CACNA1C) and the ancillary subunits CACNB3 and CACNA2D1. The channel complex contains alpha, beta, gamma and delta subunits in a 1:1:1:1 ratio. Interacts with CACNA2D4. Interacts with FASLG (By similarity). Interacts with CBARP; prevents the interaction of CACNB3 with the alpha subunit CACNA1C thereby negatively regulating the activity of the corresponding calcium channel (PubMed:24751537). {ECO:0000250|UniProtKB:P54284, ECO:0000269|PubMed:24751537}. TISSUE SPECIFICITY: Detected in the inner plexiform layer in the retina (at protein level). {ECO:0000269|PubMed:21831364}. +Q8BM92 CADH7_MOUSE Cadherin-7 785 87,202 Beta strand (18); Chain (1); Domain (5); Glycosylation (2); Helix (1); Propeptide (1); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (7) TRANSMEM 608 628 Helical. {ECO:0000255}. TOPO_DOM 28 607 Extracellular. {ECO:0000255}.; TOPO_DOM 629 785 Cytoplasmic. {ECO:0000255}. FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. DOMAIN: Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain. {ECO:0000250}. +Q01815 CAC1C_MOUSE Voltage-dependent L-type calcium channel subunit alpha-1C (Calcium channel, L type, alpha-1 polypeptide, isoform 1, cardiac muscle) (MELC-CC) (Mouse brain class C) (MBC) (Voltage-gated calcium channel subunit alpha Cav1.2) 2139 240,138 Alternative sequence (6); Calcium binding (1); Chain (1); Compositional bias (3); Disulfide bond (4); Glycosylation (4); Intramembrane (4); Metal binding (3); Modified residue (9); Motif (4); Mutagenesis (4); Region (10); Repeat (4); Sequence conflict (24); Site (4); Topological domain (29); Transmembrane (24) INTRAMEM 351 372 Pore-forming. {ECO:0000250|UniProtKB:P07293}.; INTRAMEM 694 715 Pore-forming. {ECO:0000250|UniProtKB:P07293}.; INTRAMEM 1102 1122 Pore-forming. {ECO:0000250|UniProtKB:P07293}.; INTRAMEM 1405 1423 Pore-forming. {ECO:0000250|UniProtKB:P07293}. TRANSMEM 125 143 Helical; Name=S1 of repeat I. {ECO:0000250|UniProtKB:P07293}.; TRANSMEM 159 179 Helical; Name=S2 of repeat I. {ECO:0000250|UniProtKB:P07293}.; TRANSMEM 189 209 Helical; Name=S3 of repeat I. {ECO:0000250|UniProtKB:P07293}.; TRANSMEM 233 251 Helical; Name=S4 of repeat I. {ECO:0000250|UniProtKB:P07293}.; TRANSMEM 269 290 Helical; Name=S5 of repeat I. {ECO:0000250|UniProtKB:P07293}.; TRANSMEM 381 401 Helical; Name=S6 of repeat I. {ECO:0000250|UniProtKB:P07293}.; TRANSMEM 525 543 Helical; Name=S1 of repeat II. {ECO:0000250|UniProtKB:P07293}.; TRANSMEM 555 575 Helical; Name=S2 of repeat II. {ECO:0000250|UniProtKB:P07293}.; TRANSMEM 587 606 Helical; Name=S3 of repeat II. {ECO:0000250|UniProtKB:P07293}.; TRANSMEM 616 634 Helical; Name=S4 of repeat II. {ECO:0000250|UniProtKB:P07293}.; TRANSMEM 654 673 Helical; Name=S5 of repeat II. {ECO:0000250|UniProtKB:P07293}.; TRANSMEM 726 745 Helical; Name=S6 of repeat II. {ECO:0000250|UniProtKB:P07293}.; TRANSMEM 901 919 Helical; Name=S1 of repeat III. {ECO:0000250|UniProtKB:P07293}.; TRANSMEM 932 951 Helical; Name=S2 of repeat III. {ECO:0000250|UniProtKB:P07293}.; TRANSMEM 968 986 Helical; Name=S3 of repeat III. {ECO:0000250|UniProtKB:P07293}.; TRANSMEM 994 1012 Helical; Name=S4 of repeat III. {ECO:0000250|UniProtKB:P07293}.; TRANSMEM 1032 1051 Helical; Name=S5 of repeat III. {ECO:0000250|UniProtKB:P07293}.; TRANSMEM 1140 1161 Helical; Name=S6 of repeat III. {ECO:0000250|UniProtKB:P07293}.; TRANSMEM 1220 1241 Helical; Name=S1 of repeat IV. {ECO:0000250|UniProtKB:P07293}.; TRANSMEM 1250 1271 Helical; Name=S2 of repeat IV. {ECO:0000250|UniProtKB:P07293}.; TRANSMEM 1282 1301 Helical; Name=S3 of repeat IV. {ECO:0000250|UniProtKB:P07293}.; TRANSMEM 1325 1343 Helical; Name=S4 of repeat IV. {ECO:0000250|UniProtKB:P07293}.; TRANSMEM 1362 1382 Helical; Name=S5 of repeat IV. {ECO:0000250|UniProtKB:P07293}.; TRANSMEM 1452 1476 Helical; Name=S6 of repeat IV. {ECO:0000250|UniProtKB:P07293}. TOPO_DOM 1 124 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 144 158 Extracellular. {ECO:0000305}.; TOPO_DOM 180 188 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 210 232 Extracellular. {ECO:0000305}.; TOPO_DOM 252 268 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 291 350 Extracellular. {ECO:0000305}.; TOPO_DOM 373 380 Extracellular. {ECO:0000305}.; TOPO_DOM 402 524 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 544 554 Extracellular. {ECO:0000305}.; TOPO_DOM 576 586 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 607 615 Extracellular. {ECO:0000305}.; TOPO_DOM 635 653 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 674 693 Extracellular. {ECO:0000305}.; TOPO_DOM 716 725 Extracellular. {ECO:0000305}.; TOPO_DOM 746 900 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 920 931 Extracellular. {ECO:0000305}.; TOPO_DOM 952 967 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 987 993 Extracellular. {ECO:0000305}.; TOPO_DOM 1013 1031 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1052 1101 Extracellular. {ECO:0000305}.; TOPO_DOM 1123 1139 Extracellular. {ECO:0000305}.; TOPO_DOM 1162 1219 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1242 1249 Extracellular. {ECO:0000305}.; TOPO_DOM 1272 1281 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1302 1324 Extracellular. {ECO:0000305}.; TOPO_DOM 1344 1361 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1383 1404 Extracellular. {ECO:0000305}.; TOPO_DOM 1424 1451 Extracellular. {ECO:0000305}.; TOPO_DOM 1477 2139 Cytoplasmic. {ECO:0000305}. FUNCTION: Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents (PubMed:14609949, PubMed:18586882, PubMed:21216955, PubMed:25368181, PubMed:28119464). Mediates influx of calcium ions into the cytoplasm, and thereby triggers calcium release from the sarcoplasm (By similarity). Plays an important role in excitation-contraction coupling in the heart. Required for normal heart development and normal regulation of heart rhythm (PubMed:21216955). Required for normal contraction of smooth muscle cells in blood vessels and in the intestine. Essential for normal blood pressure regulation via its role in the contraction of arterial smooth muscle cells (PubMed:14609949, PubMed:28119464). Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group (Probable). {ECO:0000250|UniProtKB:P15381, ECO:0000269|PubMed:14609949, ECO:0000269|PubMed:18586882, ECO:0000269|PubMed:21216955, ECO:0000269|PubMed:25368181, ECO:0000269|PubMed:28119464, ECO:0000305}. PTM: Phosphorylation by PKA activates the channel. Elevated levels of blood glucose lead to increased phosphorylation by PKA. {ECO:0000269|PubMed:28119464}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14609949, ECO:0000269|PubMed:18586882, ECO:0000269|PubMed:21216955}; Multi-pass membrane protein {ECO:0000305}. Cell membrane, sarcolemma {ECO:0000269|PubMed:25368181, ECO:0000269|PubMed:28119464}; Multi-pass membrane protein {ECO:0000305}. Perikaryon {ECO:0000250|UniProtKB:P22002}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250|UniProtKB:P22002}. Cell projection, dendrite {ECO:0000250|UniProtKB:P22002}. Cell membrane, sarcolemma, T-tubule {ECO:0000269|PubMed:22355118}. Note=Colocalizes with ryanodine receptors in distinct clusters at the junctional membrane, where the sarcolemma and the sarcoplasmic reticulum are in close contact. The interaction between RRAD and CACNB2 promotes the expression of CACNA1C at the cell membrane. Localized in T-tubules, as shown in SERCA2-knockout cardiomyocytes (PubMed:22355118). {ECO:0000250|UniProtKB:P15381, ECO:0000269|PubMed:22355118}. SUBUNIT: Component of a calcium channel complex consisting of a pore-forming alpha subunit (CACNA1C) and ancillary beta, gamma and delta subunits. The channel complex contains alpha, beta, gamma and delta subunits in a 1:1:1:1 ratio, i.e. it contains only one of each type of subunit. CACNA1C channel activity is modulated by ancillary subunits, such as CACNB1, CACNB2, CACNB3, CACNA2D1 and CACNA2D4 (By similarity). Intereracts with the gamma subunits CACNG4, CACNG6, CACNG7 and CACNG8 (By similarity). Interacts with CACNB1 (By similarity). Interacts with CACNB2. Identified in a complex with CACNA2D4 and CACNB3. Interacts with CACNB3. Interacts with CACNA2D1. Interacts with CACNA2D4. Interacts with CALM1. Interacts (via the N-terminus and the C-terminal C and IQ motifs) with CABP1; this inhibits Ca(2+)-dependent channel inactivation. The binding via the C motif is calcium independent whereas the binding via IQ requires the presence of calcium and is mutually exclusive with calmodulin binding (By similarity). The binding to the cytoplasmic N-terminal domain is calcium independent but is essential for the channel modulation (By similarity). Interacts (via C-terminal CDB motif) with CABP5; in a calcium-dependent manner (PubMed:18586882). Interacts with CIB1; the interaction increases upon cardiomyocytes hypertrophy (PubMed:20639889). Interacts with STAC2 and STAC3; this inhibits channel inactivation (By similarity). {ECO:0000250|UniProtKB:P15381, ECO:0000250|UniProtKB:Q13936, ECO:0000269|PubMed:18586882, ECO:0000269|PubMed:20639889}. DOMAIN: Each of the four internal repeats contains five hydrophobic transmembrane segments (S1, S2, S3, S5, S6) and one positively charged transmembrane segment (S4). S4 segments probably represent the voltage-sensor and are characterized by a series of positively charged amino acids at every third position.; DOMAIN: Binding of intracellular calcium through the EF-hand motif inhibits the opening of the channel. {ECO:0000250|UniProtKB:P15381}. TISSUE SPECIFICITY: Detected in embryonic heart (PubMed:10973973, PubMed:21216955). Detected in retina in rod bipolar cells (PubMed:18586882). Detected in tibialis artery (at protein level) (PubMed:14609949). Detected in smooth muscle cells from tibialis artery and in mesenteric artery (PubMed:14609949). High expression in heart, followed by brain and spinal cord (PubMed:1385406). {ECO:0000269|PubMed:10973973, ECO:0000269|PubMed:1385406, ECO:0000269|PubMed:14609949, ECO:0000269|PubMed:18586882, ECO:0000269|PubMed:21216955}. +Q99246 CAC1D_MOUSE Voltage-dependent L-type calcium channel subunit alpha-1D (Calcium channel, L type, alpha-1 polypeptide isoform 2) (Voltage-gated calcium channel subunit alpha Cav1.3) 2179 247,061 Alternative sequence (3); Calcium binding (1); Chain (1); Coiled coil (1); Compositional bias (3); Modified residue (1); Region (4); Repeat (4); Sequence conflict (7); Site (4); Topological domain (25); Transmembrane (24) TRANSMEM 127 145 Helical; Name=S1 of repeat I. {ECO:0000255}.; TRANSMEM 164 183 Helical; Name=S2 of repeat I. {ECO:0000255}.; TRANSMEM 196 214 Helical; Name=S3 of repeat I. {ECO:0000255}.; TRANSMEM 236 254 Helical; Name=S4 of repeat I. {ECO:0000255}.; TRANSMEM 274 293 Helical; Name=S5 of repeat I. {ECO:0000255}.; TRANSMEM 382 406 Helical; Name=S6 of repeat I. {ECO:0000255}.; TRANSMEM 544 563 Helical; Name=S1 of repeat II. {ECO:0000255}.; TRANSMEM 579 597 Helical; Name=S2 of repeat II. {ECO:0000255}.; TRANSMEM 606 624 Helical; Name=S3 of repeat II. {ECO:0000255}.; TRANSMEM 635 653 Helical; Name=S4 of repeat II. {ECO:0000255}.; TRANSMEM 673 693 Helical; Name=S5 of repeat II. {ECO:0000255}.; TRANSMEM 748 772 Helical; Name=S6 of repeat II. {ECO:0000255}.; TRANSMEM 907 925 Helical; Name=S1 of repeat III. {ECO:0000255}.; TRANSMEM 942 961 Helical; Name=S2 of repeat III. {ECO:0000255}.; TRANSMEM 974 992 Helical; Name=S3 of repeat III. {ECO:0000255}.; TRANSMEM 999 1018 Helical; Name=S4 of repeat III. {ECO:0000255}.; TRANSMEM 1038 1057 Helical; Name=S5 of repeat III. {ECO:0000255}.; TRANSMEM 1148 1168 Helical; Name=S6 of repeat III. {ECO:0000255}.; TRANSMEM 1226 1244 Helical; Name=S1 of repeat IV. {ECO:0000255}.; TRANSMEM 1260 1279 Helical; Name=S2 of repeat IV. {ECO:0000255}.; TRANSMEM 1287 1308 Helical; Name=S3 of repeat IV. {ECO:0000255}.; TRANSMEM 1334 1353 Helical; Name=S4 of repeat IV. {ECO:0000255}.; TRANSMEM 1373 1392 Helical; Name=S5 of repeat IV. {ECO:0000255}.; TRANSMEM 1460 1484 Helical; Name=S6 of repeat IV. {ECO:0000255}. TOPO_DOM 1 126 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 146 163 Extracellular. {ECO:0000255}.; TOPO_DOM 184 195 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 215 235 Extracellular. {ECO:0000255}.; TOPO_DOM 255 273 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 294 381 Extracellular. {ECO:0000255}.; TOPO_DOM 407 543 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 564 578 Extracellular. {ECO:0000255}.; TOPO_DOM 598 605 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 625 634 Extracellular. {ECO:0000255}.; TOPO_DOM 654 672 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 694 747 Extracellular. {ECO:0000255}.; TOPO_DOM 773 906 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 926 941 Extracellular. {ECO:0000255}.; TOPO_DOM 962 973 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 993 998 Extracellular. {ECO:0000255}.; TOPO_DOM 1019 1037 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1058 1147 Extracellular. {ECO:0000255}.; TOPO_DOM 1169 1225 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1245 1259 Extracellular. {ECO:0000255}.; TOPO_DOM 1280 1286 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1309 1333 Extracellular. {ECO:0000255}.; TOPO_DOM 1354 1372 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1393 1459 Extracellular. {ECO:0000255}.; TOPO_DOM 1485 2179 Cytoplasmic. {ECO:0000255}. FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1D gives rise to L-type calcium currents. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group. They are blocked by dihydropyridines (DHP), phenylalkylamines, and by benzothiazepines. {ECO:0000269|PubMed:16354915}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SUBUNIT: Voltage-dependent calcium channels are multisubunit complexes, consisting of alpha-1, alpha-2, beta and delta subunits in a 1:1:1:1 ratio. The channel activity is directed by the pore-forming and voltage-sensitive alpha-1 subunit. In many cases, this subunit is sufficient to generate voltage-sensitive calcium channel activity. The auxiliary subunits beta and alpha-2/delta linked by a disulfide bridge regulate the channel activity. Interacts (via IQ domain) with CABP1 and CABP4 in a calcium independent manner. Interacts with RIMBP2 (By similarity). {ECO:0000250}. DOMAIN: Each of the four internal repeats contains five hydrophobic transmembrane segments (S1, S2, S3, S5, S6) and one positively charged transmembrane segment (S4). S4 segments probably represent the voltage-sensor and are characterized by a series of positively charged amino acids at every third position. TISSUE SPECIFICITY: Expressed in the inner hair cells (IHC) of the cochlea. {ECO:0000269|PubMed:16354915}. +Q9WTR5 CAD13_MOUSE Cadherin-13 (Heart cadherin) (H-cadherin) (Truncated cadherin) (T-cad) (T-cadherin) 714 78,186 Beta strand (18); Chain (1); Domain (5); Glycosylation (7); Helix (3); Lipidation (1); Mutagenesis (1); Propeptide (2); Sequence conflict (3); Signal peptide (1); Turn (5) FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. May act as a negative regulator of neural cell growth. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. SUBUNIT: By contrast to classical cadherins, homodimerization in trans is not mediated by cadherin EC1 domain strand-swapping, but instead through a homophilic adhesive interface which joins two elongated EC1-EC2 domains through a region near their Ca2+-binding sites to form a tetrahedral, X-like shape. {ECO:0000269|PubMed:20190755}. DOMAIN: Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain. {ECO:0000250}. +Q8VHB5 CAH9_MOUSE Carbonic anhydrase 9 (EC 4.2.1.1) (Carbonate dehydratase IX) (Carbonic anhydrase IX) (CA-IX) (CAIX) (Membrane antigen MN homolog) 437 47,265 Active site (1); Alternative sequence (2); Chain (1); Disulfide bond (2); Domain (1); Glycosylation (2); Metal binding (3); Modified residue (1); Region (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 391 411 Helical. {ECO:0000255}. TOPO_DOM 32 390 Extracellular. {ECO:0000255}.; TOPO_DOM 412 437 Cytoplasmic. {ECO:0000255}. FUNCTION: Reversible hydration of carbon dioxide. Participates in pH regulation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cell projection, microvillus membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Forms oligomers linked by disulfide bonds. {ECO:0000250}. +Q02789 CAC1S_MOUSE Voltage-dependent L-type calcium channel subunit alpha-1S (Calcium channel, L type, alpha-1 polypeptide, isoform 3, skeletal muscle) (Dihydropyridine receptor) (DHPR) (Voltage-gated calcium channel subunit alpha Cav1.1) 1880 213,260 Alternative sequence (1); Calcium binding (1); Chain (1); Compositional bias (1); Disulfide bond (4); Glycosylation (3); Helix (1); Intramembrane (4); Metal binding (3); Modified residue (7); Motif (4); Region (6); Repeat (4); Sequence conflict (2); Topological domain (29); Transmembrane (24) INTRAMEM 280 301 Pore-forming. {ECO:0000250|UniProtKB:P07293}.; INTRAMEM 602 623 Pore-forming. {ECO:0000250|UniProtKB:P07293}.; INTRAMEM 1001 1021 Pore-forming. {ECO:0000250|UniProtKB:P07293}.; INTRAMEM 1312 1330 Pore-forming. {ECO:0000250|UniProtKB:P07293}. TRANSMEM 52 70 Helical; Name=S1 of repeat I. {ECO:0000250|UniProtKB:P07293}.; TRANSMEM 86 106 Helical; Name=S2 of repeat I. {ECO:0000250|UniProtKB:P07293}.; TRANSMEM 116 136 Helical; Name=S3 of repeat I. {ECO:0000250|UniProtKB:P07293}.; TRANSMEM 161 179 Helical; Name=S4 of repeat I. {ECO:0000250|UniProtKB:P07293}.; TRANSMEM 197 218 Helical; Name=S5 of repeat I. {ECO:0000250|UniProtKB:P07293}.; TRANSMEM 310 330 Helical; Name=S6 of repeat I. {ECO:0000250|UniProtKB:P07293}.; TRANSMEM 433 451 Helical; Name=S1 of repeat II. {ECO:0000250|UniProtKB:P07293}.; TRANSMEM 463 483 Helical; Name=S2 of repeat II. {ECO:0000250|UniProtKB:P07293}.; TRANSMEM 495 514 Helical; Name=S3 of repeat II. {ECO:0000250|UniProtKB:P07293}.; TRANSMEM 524 542 Helical; Name=S4 of repeat II. {ECO:0000250|UniProtKB:P07293}.; TRANSMEM 562 581 Helical; Name=S5 of repeat II. {ECO:0000250|UniProtKB:P07293}.; TRANSMEM 634 653 Helical; Name=S6 of repeat II. {ECO:0000250|UniProtKB:P07293}.; TRANSMEM 800 818 Helical; Name=S1 of repeat III. {ECO:0000250|UniProtKB:P07293}.; TRANSMEM 831 850 Helical; Name=S2 of repeat III. {ECO:0000250|UniProtKB:P07293}.; TRANSMEM 867 885 Helical; Name=S3 of repeat III. {ECO:0000250|UniProtKB:P07293}.; TRANSMEM 893 911 Helical; Name=S4 of repeat III. {ECO:0000250|UniProtKB:P07293}.; TRANSMEM 931 950 Helical; Name=S5 of repeat III. {ECO:0000250|UniProtKB:P07293}.; TRANSMEM 1039 1060 Helical; Name=S6 of repeat III. {ECO:0000250|UniProtKB:P07293}.; TRANSMEM 1119 1140 Helical; Name=S1 of repeat IV. {ECO:0000250|UniProtKB:P07293}.; TRANSMEM 1149 1170 Helical; Name=S2 of repeat IV. {ECO:0000250|UniProtKB:P07293}.; TRANSMEM 1181 1200 Helical; Name=S3 of repeat IV. {ECO:0000250|UniProtKB:P07293}.; TRANSMEM 1232 1250 Helical; Name=S4 of repeat IV. {ECO:0000250|UniProtKB:P07293}.; TRANSMEM 1269 1289 Helical; Name=S5 of repeat IV. {ECO:0000250|UniProtKB:P07293}.; TRANSMEM 1357 1381 Helical; Name=S6 of repeat IV. {ECO:0000250|UniProtKB:P07293}. TOPO_DOM 1 51 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 71 85 Extracellular. {ECO:0000305}.; TOPO_DOM 107 115 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 137 160 Extracellular. {ECO:0000305}.; TOPO_DOM 180 196 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 219 279 Extracellular. {ECO:0000305}.; TOPO_DOM 302 309 Extracellular. {ECO:0000305}.; TOPO_DOM 331 432 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 452 462 Extracellular. {ECO:0000305}.; TOPO_DOM 484 494 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 515 523 Extracellular. {ECO:0000305}.; TOPO_DOM 543 561 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 582 601 Extracellular. {ECO:0000305}.; TOPO_DOM 624 633 Extracellular. {ECO:0000305}.; TOPO_DOM 654 799 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 819 830 Extracellular. {ECO:0000305}.; TOPO_DOM 851 866 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 886 892 Extracellular. {ECO:0000305}.; TOPO_DOM 912 930 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 951 1000 Extracellular. {ECO:0000305}.; TOPO_DOM 1022 1038 Extracellular. {ECO:0000305}.; TOPO_DOM 1061 1118 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1141 1148 Extracellular. {ECO:0000305}.; TOPO_DOM 1171 1180 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1201 1231 Extracellular. {ECO:0000305}.; TOPO_DOM 1251 1268 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1290 1311 Extracellular. {ECO:0000305}.; TOPO_DOM 1331 1356 Extracellular. {ECO:0000305}.; TOPO_DOM 1382 1880 Cytoplasmic. {ECO:0000305}. FUNCTION: Pore-forming, alpha-1S subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents in skeletal muscle. Calcium channels containing the alpha-1S subunit play an important role in excitation-contraction coupling in skeletal muscle via their interaction with RYR1, which triggers Ca(2+) release from the sarcplasmic reticulum and ultimately results in muscle contraction. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group. {ECO:0000250|UniProtKB:P07293}. PTM: The alpha-1S subunit is found in two isoforms in the skeletal muscle: a minor form of 212 kDa containing the complete amino acid sequence, and a major form of 190 kDa derived from the full-length form by post-translational proteolysis close to Phe-1690. {ECO:0000250|UniProtKB:P07293}.; PTM: Both the minor and major forms are phosphorylated in vitro by PKA. Phosphorylation by PKA activates the calcium channel. {ECO:0000250|UniProtKB:P07293}. SUBCELLULAR LOCATION: Cell membrane, sarcolemma, T-tubule {ECO:0000250|UniProtKB:P07293}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P07293}. SUBUNIT: Component of a calcium channel complex consisting of a pore-forming alpha subunit (CACNA1S) and the ancillary subunits CACNB1 or CACNB2, CACNG1 and CACNA2D1 (PubMed:28351836). The channel complex contains alpha, beta, gamma and delta subunits in a 1:1:1:1 ratio, i.e. it contains either CACNB1 or CACNB2 (By similarity). CACNA1S channel activity is modulated by the auxiliary subunits (CACNB1 or CACNB2, CACNG1 and CACNA2D1). Interacts with DYSF and JSRP1 (PubMed:12871958, PubMed:16550931, PubMed:16638807). Interacts with RYR1 (By similarity). Interacts with STAC, STAC2 and STAC3 (via their SH3 domains) (PubMed:29467163). Interacts with CALM (By similarity). {ECO:0000250|UniProtKB:P07293, ECO:0000250|UniProtKB:Q13698, ECO:0000269|PubMed:12871958, ECO:0000269|PubMed:16550931, ECO:0000269|PubMed:16638807, ECO:0000269|PubMed:28351836, ECO:0000269|PubMed:29467163}. DOMAIN: Each of the four internal repeats contains five hydrophobic transmembrane segments (S1, S2, S3, S5, S6) and one positively charged transmembrane segment (S4). S4 segments probably represent the voltage-sensor and are characterized by a series of positively charged amino acids at every third position. {ECO:0000250|UniProtKB:P07293}.; DOMAIN: The loop between repeats II and III interacts with the ryanodine receptor, and is therefore important for calcium release from the endoplasmic reticulum necessary for muscle contraction. {ECO:0000250|UniProtKB:P07293}. DISEASE: Note=Defects in Cacna1s are the cause of muscular dysgenesis (MDG), a lethal autosomal recessive disorder in which there is total lack of excitation-contraction coupling in homozygotes, and which results in complete skeletal muscle paralysis. A single nucleotide deletion yields a protein with an altered and truncated C-terminus. {ECO:0000269|PubMed:1281468}. +Q9D9Q6 CALR3_MOUSE Calreticulin-3 (Calreticulin-2) (Calsperin) 380 44,232 Binding site (5); Chain (1); Disulfide bond (1); Glycosylation (2); Motif (1); Region (5); Repeat (7); Sequence conflict (1); Signal peptide (1) FUNCTION: CALR3 capacity for calcium-binding may be absent or much lower than that of CALR (By similarity). During spermatogenesis, may act as a lectin-independent chaperone for specific client proteins such as ADAM3. Required for sperm fertility. {ECO:0000250, ECO:0000269|PubMed:21131354}. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250}. SUBUNIT: Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5. {ECO:0000269|PubMed:16931514}. TISSUE SPECIFICITY: Testis specific, absent in mature sperm. {ECO:0000269|PubMed:12384296, ECO:0000269|PubMed:21131354}. +Q99JA0 CALCA_MOUSE Calcitonin gene-related peptide 1 (Alpha-type CGRP) (Calcitonin gene-related peptide I) (CGRP-I) 128 14,065 Disulfide bond (1); Modified residue (1); Peptide (1); Propeptide (2); Signal peptide (1) FUNCTION: CGRP induces vasodilation. It dilates a variety of vessels including the coronary, cerebral and systemic vasculature. Its abundance in the CNS also points toward a neurotransmitter or neuromodulator role. It also elevates platelet cAMP (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Detected in nerve cells of cerebrum, hippocampus and pons/midbrain in newborns, and only in nerve cells of pons/midbrain in adult. {ECO:0000269|PubMed:18544925}. +A2AHC3 CAMP1_MOUSE Calmodulin-regulated spectrin-associated protein 1 1581 175,887 Alternative sequence (3); Chain (1); Coiled coil (3); Domain (2); Erroneous initiation (1); Modified residue (20); Region (2); Sequence conflict (2) FUNCTION: Key microtubule-organizing protein that specifically binds the minus-end of non-centrosomal microtubules and regulates their dynamics and organization. Specifically recognizes growing microtubule minus-ends and stabilizes microtubules. Acts on free microtubule minus-ends that are not capped by microtubule-nucleating proteins or other factors and protects microtubule minus-ends from depolymerization. In contrast to CAMSAP2 and CAMSAP3, tracks along the growing tips of minus-end microtubules without significantly affecting the polymerization rate: binds at the very tip of the microtubules minus-end and acts as a minus-end tracking protein (-TIP) that dissociates from microtubules after allowing tubulin incorporation. Through interaction with spectrin may regulate neurite outgrowth. {ECO:0000250|UniProtKB:Q5T5Y3}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q5T5Y3}. Note=Associates with the minus-end of microtubules. In contrast to CAMSAP2 and CAMSAP3, does not form stretches of decorated microtubule minus-ends. {ECO:0000250|UniProtKB:Q5T5Y3}. SUBUNIT: Interacts with spectrin via SPTBN1; the interaction is direct. Interacts with calmodulin; calcium-dependent it prevents interaction with spectrin. {ECO:0000250|UniProtKB:Q5T5Y3}. DOMAIN: The CKK domain binds microtubules. {ECO:0000255|PROSITE-ProRule:PRU00841}. +Q6P2L7 CASC4_MOUSE Protein CASC4 (Cancer susceptibility candidate gene 4 protein homolog) 435 49,409 Alternative sequence (3); Chain (1); Coiled coil (1); Frameshift (1); Modified residue (3); Topological domain (2); Transmembrane (1) TRANSMEM 15 35 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 14 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 36 435 Lumenal. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. +P48320 DCE2_MOUSE Glutamate decarboxylase 2 (EC 4.1.1.15) (65 kDa glutamic acid decarboxylase) (GAD-65) (Glutamate decarboxylase 65 kDa isoform) 585 65,224 Binding site (1); Chain (1); Lipidation (2); Modified residue (5); Region (1); Sequence conflict (4) FUNCTION: Catalyzes the production of GABA. PTM: Phosphorylated; which does not affect kinetic parameters or subcellular location. {ECO:0000250}.; PTM: Palmitoylated; which is required for presynaptic clustering. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Cell junction, synapse, presynaptic cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Associated to cytoplasmic vesicles. In neurons, cytosolic leaflet of Golgi membranes and presynaptic clusters (By similarity). {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +P10605 CATB_MOUSE Cathepsin B (EC 3.4.22.1) (Cathepsin B1) [Cleaved into: Cathepsin B light chain; Cathepsin B heavy chain] 339 37,280 Active site (3); Chain (3); Disulfide bond (6); Glycosylation (1); Modified residue (1); Propeptide (2); Sequence conflict (4); Signal peptide (1) FUNCTION: Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Cleaves matrix extracellular phosphoglycoprotein MEPE. Has also been implicated in tumor invasion and metastasis. {ECO:0000250|UniProtKB:P07858}. SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:P07858}. Melanosome {ECO:0000250|UniProtKB:P07858}. Secreted, extracellular space {ECO:0000250|UniProtKB:A1E295}. SUBUNIT: Dimer of a heavy chain and a light chain cross-linked by a disulfide bond. Interacts with SRPX2. Directly interacts with SHKBP1. {ECO:0000250|UniProtKB:P07858}. +Q91ZF2 CAT7_MOUSE Cathepsin 7 (EC 3.4.22.-) (Cathepsin 1) 331 37,725 Active site (3); Chain (1); Disulfide bond (3); Glycosylation (1); Motif (1); Propeptide (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Involved in trophoblast cell proliferation and differentiation probably by affecting mitotic cell cycle progression. Proteolytic activity and nuclear localization are essential for its role in cell cycle progression. {ECO:0000269|PubMed:18776147}. SUBCELLULAR LOCATION: Endosome {ECO:0000269|PubMed:18776147, ECO:0000305}. Lysosome {ECO:0000269|PubMed:18776147, ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:18776147}. Golgi apparatus {ECO:0000269|PubMed:18776147, ECO:0000305}. Nucleus {ECO:0000269|PubMed:18776147}. Secreted, extracellular space {ECO:0000269|PubMed:18776147}. TISSUE SPECIFICITY: Expressed in placenta. Expressed in parietal and spiral artery-associated trophoblast giant cells, most abundantly during the phase of trophoblast invasion. From E14.5 onwards, expressed at lower levels in labyrinth trophoblast cells. Expressed in trophoblast stem cells. Expressed in heart, liver and testis. {ECO:0000269|PubMed:10885754, ECO:0000269|PubMed:11829493, ECO:0000269|PubMed:18776147}. +P28293 CATG_MOUSE Cathepsin G (EC 3.4.21.20) (Vimentin-specific protease) (VSP) 261 29,096 Active site (3); Chain (1); Disulfide bond (3); Domain (1); Glycosylation (1); Propeptide (1); Sequence conflict (3); Signal peptide (1) FUNCTION: This vimentin-specific protease may regulate the reorganization of vimentin filaments, occurring during cell differentiation, movement and mitosis. SUBCELLULAR LOCATION: Membrane. Note=Strongly associated with membranes. +B9EKE5 CATIP_MOUSE Ciliogenesis-associated TTC17-interacting protein 520 59,301 Alternative sequence (2); Chain (1); Compositional bias (2) FUNCTION: Plays a role in primary ciliogenesis by modulating actin polymerization. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Colocalized with TTC17 at F-actin rich zones and at dynamic plasma membrane protrusions. {ECO:0000250}. SUBUNIT: Interacts with TTC17. {ECO:0000250}. +P51637 CAV3_MOUSE Caveolin-3 (M-caveolin) 151 17,358 Chain (1); Cross-link (1); Intramembrane (1); Mutagenesis (2); Region (1); Topological domain (2) INTRAMEM 84 104 Helical. {ECO:0000255}. TOPO_DOM 1 83 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 105 151 Cytoplasmic. {ECO:0000255}. FUNCTION: May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity. May also regulate voltage-gated potassium channels. Plays a role in the sarcolemma repair mechanism of both skeletal muscle and cardiomyocytes that permits rapid resealing of membranes disrupted by mechanical stress (PubMed:19380584). Mediates the recruitment of CAVIN2 and CAVIN3 proteins to the caveolae (By similarity). {ECO:0000250|UniProtKB:P56539, ECO:0000269|PubMed:19380584}. PTM: Sumoylation with SUMO3 by PIAS4 may reduce agonist-induced internalization and desensitization of adrenergic receptor ABRD2. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:26497963}; Peripheral membrane protein {ECO:0000250}. Membrane, caveola {ECO:0000269|PubMed:24066022}; Peripheral membrane protein {ECO:0000250}. Cell membrane, sarcolemma {ECO:0000269|PubMed:24066022}. Note=Potential hairpin-like structure in the membrane. Membrane protein of caveolae (By similarity). {ECO:0000250}. SUBUNIT: Homooligomer. Interacts with DYSF. Interacts with DLG1 and KCNA5; forms a ternary complex. Interacts with DAG1 (via its C-terminal); the interaction prevents binding of DAG1 with DMD (By similarity). Interacts with TRIM72 (PubMed:19380584). Interacts with MUSK; may regulate MUSK signaling (PubMed:19940021). Interacts with BVES (PubMed:24066022). Interacts with CAVIN1, CAVIN2 and CAVIN4 (By similarity). {ECO:0000250|UniProtKB:P51638, ECO:0000250|UniProtKB:P56539, ECO:0000269|PubMed:19380584, ECO:0000269|PubMed:19940021, ECO:0000269|PubMed:24066022}. TISSUE SPECIFICITY: Expressed predominantly in muscle. {ECO:0000269|PubMed:8521953}. +Q9WVJ3 CBPQ_MOUSE Carboxypeptidase Q (EC 3.4.17.-) (Hematopoietic lineage switch 2) (Plasma glutamate carboxypeptidase) 470 51,813 Active site (1); Chain (1); Frameshift (1); Glycosylation (3); Metal binding (6); Propeptide (1); Sequence caution (1); Sequence conflict (2); Signal peptide (1) FUNCTION: Carboxypeptidase that may play an important role in the hydrolysis of circulating peptides. Catalyzes the hydrolysis of dipeptides with unsubstituted terminals into amino acids. May play a role in the liberation of thyroxine hormone from its thyroglobulin (Tg) precursor (By similarity). {ECO:0000250}. PTM: N-glycosylated. The secreted form is modified by hybrid or complex type oligosaccharide chains. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250}. Golgi apparatus {ECO:0000250}. Lysosome {ECO:0000250}. Secreted {ECO:0000250}. Note=Secretion is stimulated by TSH/thyroid-stimulating hormone, INS/insulin and SST/somatostatin. {ECO:0000250}. SUBUNIT: Homodimer. The monomeric form is inactive while the homodimer is active (By similarity). {ECO:0000250}. +Q8BGK9 CC018_MOUSE Uncharacterized protein C3orf18 homolog 164 17,721 Chain (1); Coiled coil (1); Sequence conflict (3); Transmembrane (1) TRANSMEM 64 84 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q8CHW5 BICL2_MOUSE BICD family-like cargo adapter 2 (Bicaudal D-related protein 2) (BICD-related protein 2) (BICDR-2) (Coiled-coil domain-containing protein 64B) 507 57,527 Chain (1); Coiled coil (2); Erroneous initiation (1) SUBUNIT: Interacts with RAB13. {ECO:0000269|PubMed:20360680}. +Q62210 BIRC2_MOUSE Baculoviral IAP repeat-containing protein 2 (EC 2.3.2.27) (Cellular inhibitor of apoptosis 1) (C-IAP1) (Inhibitor of apoptosis protein 2) (mIAP2) (RING-type E3 ubiquitin transferase BIRC2) 612 69,676 Chain (1); Domain (1); Metal binding (4); Modified residue (2); Repeat (3); Sequence conflict (1); Zinc finger (1) FUNCTION: Multi-functional protein which regulates not only caspases and apoptosis, but also modulates inflammatory signaling and immunity, mitogenic kinase signaling, and cell proliferation, as well as cell invasion and metastasis. Acts as an E3 ubiquitin-protein ligase regulating NF-kappa-B signaling and regulates both canonical and non-canonical NF-kappa-B signaling by acting in opposite directions: acts as a positive regulator of the canonical pathway and suppresses constitutive activation of non-canonical NF-kappa-B signaling. The target proteins for its E3 ubiquitin-protein ligase activity include: RIPK1, RIPK2, RIPK3, RIPK4, CASP3, CASP7, CASP8, TRAF2, DIABLO/SMAC, MAP3K14/NIK, MAP3K5/ASK1, IKBKG/NEMO, IKBKE and MXD1/MAD1. Can also function as an E3 ubiquitin-protein ligase of the NEDD8 conjugation pathway, targeting effector caspases for neddylation and inactivation. Acts as an important regulator of innate immune signaling via regulation of Toll-like receptors (TLRs), Nodlike receptors (NLRs) and RIG-I like receptors (RLRs), collectively referred to as pattern recognition receptors (PRRs). Protects cells from spontaneous formation of the ripoptosome, a large multi-protein complex that has the capability to kill cancer cells in a caspase-dependent and caspase-independent manner. Suppresses ripoptosome formation by ubiquitinating RIPK1 and CASP8. Can stimulate the transcriptional activity of E2F1. Plays a role in the modulation of the cell cycle. {ECO:0000269|PubMed:18621737}. PTM: Auto-ubiquitinated and degraded by the proteasome in apoptotic cells. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Agents that induce either the extrinsic or intrinsic apoptotic pathways promote its redistribution from the nuclear compartment to the cytoplasmic compartment. Associated with the midbody in telophase cells, and found diffusely in the nucleus of interphase cells (By similarity). {ECO:0000250}. SUBUNIT: Interacts with DIABLO/SMAC and with PRSS25; these interactions inhibit apoptotic suppressor activity. Interacts with CASP9. Interacts (via BIR domains) with TRAF2; the interaction is required for IKBKE ubiquitination. Interacts with E2F1, RIPK1, RIPK2, RIPK3, RIPK4, BIRC5/survivin and USP19 (By similarity). Interacts with HSP90AB1 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q13490}. DOMAIN: The BIR domains mediate nuclear localization. {ECO:0000250}.; DOMAIN: The CARD domain is necessary to stabilize the protein and inhibit the activation of E3 ubiquitin-protein ligase activity of BIRC2/c-IAP1 by preventing RING domain dimerization and E2 ubiquitin donor binding and activation. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in heart, brain, spleen, lung, liver, skeletal muscle, kidney and testis. +O08863 BIRC3_MOUSE Baculoviral IAP repeat-containing protein 3 (EC 2.3.2.27) (Cellular inhibitor of apoptosis 2) (C-IAP2) (Inhibitor of apoptosis protein 1) (mIAP1) (RING-type E3 ubiquitin transferase BIRC3) 600 67,228 Chain (1); Domain (1); Metal binding (4); Modified residue (1); Repeat (3); Sequence conflict (1); Zinc finger (1) FUNCTION: Multi-functional protein which regulates not only caspases and apoptosis, but also modulates inflammatory signaling and immunity, mitogenic kinase signaling and cell proliferation, as well as cell invasion and metastasis. Acts as an E3 ubiquitin-protein ligase regulating NF-kappa-B signaling and regulates both canonical and non-canonical NF-kappa-B signaling by acting in opposite directions: acts as a positive regulator of the canonical pathway and suppresses constitutive activation of non-canonical NF-kappa-B signaling. The target proteins for its E3 ubiquitin-protein ligase activity include: RIPK1, RIPK2, RIPK3, RIPK4, CASP3, CASP7, CASP8, IKBKE, TRAF1, and BCL10. Acts as an important regulator of innate immune signaling via regulation of Toll-like receptors (TLRs), Nodlike receptors (NLRs) and RIG-I like receptors (RLRs), collectively referred to as pattern recognition receptors (PRRs). Protects cells from spontaneous formation of the ripoptosome, a large multi-protein complex that has the capability to kill cancer cells in a caspase-dependent and caspase-independent manner. Suppresses ripoptosome formation by ubiquitinating RIPK1 and CASP8. {ECO:0000269|PubMed:18621737}. PTM: Auto-ubiquitinated and degraded by the proteasome in apoptotic cells. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Interacts with DIABLO/SMAC and with PRSS25; these interactions inhibit apoptotic suppressor activity. The BIR motifs region interacts with TNF receptor associated factors 1 and 2 (TRAF1 and TRAF2) to form a heteromeric complex, which is then recruited to the tumor necrosis factor receptor 2 (TNFR2). Interaction with TRAF2 is required for ubiquitination of IKBKE, degradation of NFKBIA and activation of NF-kappa-B. Interacts with RIP1, RIP2, RIP3, RIP4 and USP19 (By similarity). {ECO:0000250}. +P16277 BLK_MOUSE Tyrosine-protein kinase Blk (EC 2.7.10.2) (B lymphocyte kinase) (p55-Blk) 499 56,674 Active site (1); Beta strand (9); Binding site (1); Chain (1); Domain (3); Helix (2); Initiator methionine (1); Lipidation (1); Modified residue (1); Mutagenesis (2); Nucleotide binding (1); Sequence conflict (1); Turn (2) FUNCTION: Non-receptor tyrosine kinase involved in B-lymphocyte development, differentiation and signaling. B-cell receptor (BCR) signaling requires a tight regulation of several protein tyrosine kinases and phosphatases, and associated coreceptors (PubMed:2404338, PubMed:7690139, PubMed:7608542, PubMed:9636152, PubMed:14662906, PubMed:12563261). Binding of antigen to the B-cell antigen receptor (BCR) triggers signaling that ultimately leads to B-cell activation (PubMed:2404338, PubMed:7690139, PubMed:7608542, PubMed:14662906, PubMed:12563261). Signaling through BLK plays an important role in transmitting signals through surface immunoglobulins and supports the pro-B to pre-B transition, as well as the signaling for growth arrest and apoptosis downstream of B-cell receptor (PubMed:2404338, PubMed:7690139, PubMed:7608542, PubMed:14662906, PubMed:12563261). Specifically binds and phosphorylates CD79A at 'Tyr-188'and 'Tyr-199', as well as CD79B at 'Tyr-196' and 'Tyr-207' (PubMed:7592958, PubMed:9177269). Phosphorylates also the immunoglobulin G receptor FCGR2 (By similarity). With FYN and LYN, plays an essential role in pre-B-cell receptor (pre-BCR)-mediated NF-kappa-B activation (PubMed:14662906, PubMed:12563261). Contributes also to BTK activation by indirectly stimulating BTK intramolecular autophosphorylation (PubMed:7565679). In pancreatic islets, acts as a modulator of beta-cells function through the up-regulation of PDX1 and NKX6-1 and consequent stimulation of insulin secretion in response to glucose (By similarity). Phosphorylates CGAS, promoting retention of CGAS in the cytosol (By similarity). {ECO:0000250|UniProtKB:P51451, ECO:0000269|PubMed:12563261, ECO:0000269|PubMed:14662906, ECO:0000269|PubMed:2404338, ECO:0000269|PubMed:7565679, ECO:0000269|PubMed:7592958, ECO:0000269|PubMed:7608542, ECO:0000269|PubMed:7690139, ECO:0000269|PubMed:9177269, ECO:0000269|PubMed:9636152}. PTM: Phosphorylated on tyrosine residues after antibody-mediated surface engagement of the B-cell antigen receptor (BCR).; PTM: Ubiquitination of activated BLK by the UBE3A ubiquitin protein ligase leads to its degradation by the ubiquitin-proteasome pathway. {ECO:0000269|PubMed:10449731}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Note=Present and active in lipid rafts (By similarity). Membrane location is required for the phosphorylation of CD79A and CD79B. {ECO:0000250, ECO:0000269|PubMed:7592958}. SUBUNIT: Interacts with CBL (via SH2 domain) (By similarity). Interacts with CD79A and CD79B (via SH2 domain). {ECO:0000250, ECO:0000269|PubMed:1506682, ECO:0000269|PubMed:7592958}. TISSUE SPECIFICITY: Specifically expressed in the B-cell lineage. {ECO:0000269|PubMed:1537861, ECO:0000269|PubMed:2404338}. +P36898 BMR1B_MOUSE Bone morphogenetic protein receptor type-1B (BMP type-1B receptor) (BMPR-1B) (EC 2.7.11.30) (Activin receptor-like kinase 6) (ALK-6) (Serine/threonine-protein kinase receptor R6) (SKR6) (CD antigen CDw293) 502 56,944 Active site (1); Beta strand (5); Binding site (1); Chain (1); Disulfide bond (5); Domain (2); Helix (2); Nucleotide binding (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 127 148 Helical. {ECO:0000255}. TOPO_DOM 14 126 Extracellular. {ECO:0000255}.; TOPO_DOM 149 502 Cytoplasmic. {ECO:0000255}. FUNCTION: On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for BMP7/OP-1. Receptor for GDF5 (PubMed:26105076, PubMed:19229295). Positively regulates chondrocyte differentiation through GDF5 interaction (PubMed:24098149). {ECO:0000269|PubMed:19229295, ECO:0000269|PubMed:24098149, ECO:0000269|PubMed:26105076}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24129431, ECO:0000269|PubMed:26105076}. Membrane; Single-pass type I membrane protein. SUBUNIT: Interacts with high affinity with GDF5; positively regulates chondrocyte differentiation. {ECO:0000250|UniProtKB:O00238}. +Q9D8S9 BOLA1_MOUSE BolA-like protein 1 137 14,379 Beta strand (5); Chain (1); Helix (4); Modified residue (1); Turn (2) FUNCTION: Acts as a mitochondrial iron-sulfur (Fe-S) cluster assembly factor that facilitates (Fe-S) cluster insertion into a subset of mitochondrial proteins (By similarity). Probably acts together with the monothiol glutaredoxin GLRX5. May protect cells against oxidative stress (By similarity). {ECO:0000250|UniProtKB:Q3E793, ECO:0000250|UniProtKB:Q9Y3E2}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9Y3E2}. SUBUNIT: Interacts with GLRX5. {ECO:0000250|UniProtKB:Q9Y3E2}. +Q9Z2F7 BNI3L_MOUSE BCL2/adenovirus E1B 19 kDa protein-interacting protein 3-like (NIP3-like protein X) (NIP3L) 218 23,766 Chain (1); Modified residue (5); Motif (1); Transmembrane (1) TRANSMEM 187 207 Helical. {ECO:0000255}. FUNCTION: Induces apoptosis. Interacts with viral and cellular anti-apoptosis proteins. Can overcome the suppressors BCL-2 and BCL-XL, although high levels of BCL-XL expression will inhibit apoptosis. Inhibits apoptosis induced by BNIP3. Involved in mitochondrial quality control via its interaction with SPATA18/MIEAP: in response to mitochondrial damage, participates in mitochondrial protein catabolic process (also named MALM) leading to the degradation of damaged proteins inside mitochondria. The physical interaction of SPATA18/MIEAP, BNIP3 and BNIP3L/NIX at the mitochondrial outer membrane regulates the opening of a pore in the mitochondrial double membrane in order to mediate the translocation of lysosomal proteins from the cytoplasm to the mitochondrial matrix (By similarity). May function as a tumor suppressor (By similarity). {ECO:0000250}. PTM: Undergoes progressive proteolysis to an 11 kDa C-terminal fragment, which is blocked by the proteasome inhibitor lactacystin. SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Mitochondrion outer membrane {ECO:0000250}. Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Note=Colocalizes with SPATA18 at the mitochondrion outer membrane. {ECO:0000250}. SUBUNIT: Self-associates. Interacts with BNIP3 and STEAP3. Interacts (via BH3 domain) with SPATA18 (via coiled-coil domains) (By similarity). {ECO:0000250}. +Q80ZU7 BPIB3_MOUSE BPI fold-containing family B member 3 (Ligand-binding protein RYA3) (Long palate, lung and nasal epithelium carcinoma-associated protein 3) 473 49,885 Chain (1); Disulfide bond (1); Glycosylation (1); Signal peptide (1) FUNCTION: May have the capacity to recognize and bind specific classes of odorants. May act as a carrier molecule, transporting odorants across the mucus layer to access receptor sites. May serve as a primary defense mechanism by recognizing and removing potentially harmful odorants or pathogenic microorganisms from the mucosa or clearing excess odorant from mucus to enable new odorant stimuli to be received (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +Q9ESU6 BRD4_MOUSE Bromodomain-containing protein 4 (Mitotic chromosome-associated protein) (MCAP) 1400 155,895 Alternative sequence (2); Binding site (4); Chain (1); Compositional bias (7); Cross-link (8); Domain (3); Helix (22); Modified residue (14); Mutagenesis (4); Region (3); Sequence conflict (3); Turn (2) FUNCTION: Chromatin reader protein that recognizes and binds acetylated histones and plays a key role in transmission of epigenetic memory across cell divisions and transcription regulation. Remains associated with acetylated chromatin throughout the entire cell cycle and provides epigenetic memory for postmitotic G1 gene transcription by preserving acetylated chromatin status and maintaining high-order chromatin structure. During interphase, plays a key role in regulating the transcription of signal-inducible genes by associating with the P-TEFb complex and recruiting it to promoters: BRD4 is required to form the transcriptionally active P-TEFb complex by displacing negative regulators such as HEXIM1 and 7SKsnRNA complex from P-TEFb, thereby transforming it into an active form that can then phosphorylate the C-terminal domain (CTD) of RNA polymerase II. Promotes phosphorylation of 'Ser-2' of the C-terminal domain (CTD) of RNA polymerase II. In addition to acetylated histones, also recognizes and binds acetylated RELA, leading to further recruitment of the P-TEFb complex and subsequent activation of NF-kappa-B. Also acts as a regulator of p53/TP53-mediated transcription: following phosphorylation by CK2, recruited to p53/TP53 specific target promoters. {ECO:0000269|PubMed:10938129, ECO:0000269|PubMed:16109376}. PTM: Phosphorylation by CK2 disrupt the intramolecular binding between the bromo domain 2 and the NPS region and promotes binding between the NPS and the BID regions, leading to activate the protein and promote binding to acetylated histones. In absence of phosphorylation, BRD4 does not localize to p53/TP53 target gene promoters, phosphorylation promoting recruitment to p53/TP53 target promoters (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Associates with acetylated chromatin. Released from chromatin upon deacetylation of histones that can be triggered by different signals such as activation of the JNK pathway or nocodazole treatment. Preferentially localizes to mitotic chromosomes, while it does not localizes to meiotic chromosomes. SUBUNIT: Interacts with p53/TP53; the interaction is direct. Interacts with RELA (when acetylated at 'Lys-310'). Interacts (via NET domain) with WHSC1L1, JMJD6, CHD4, BICRA and ATAD5. The interaction with BICRA bridges BRD4 to the GBAF complex (By similarity). Interacts (via CTD region) with CDK9 and CCNT1, acting as an associated component of P-TEFb complex (PubMed:16109376). {ECO:0000250|UniProtKB:O60885, ECO:0000269|PubMed:16109376}. DOMAIN: The 2 bromo domains mediate specific binding to acetylated histones via Asn-140 and Asn-434, respectively (PubMed:19828451). The exact combination of modified histone tails required to recruit BRD4 to target genes is still unclear. The first bromo domain has high affinity for acetylated histone H4 tail, whereas the second bromo domain recognizes multiply acetylated marks in histone H3 (By similarity). {ECO:0000250, ECO:0000269|PubMed:19828451}.; DOMAIN: The NET domain mediates interaction with a number of chromatin proteins involved in transcription regulation (WHSC1L1, JMJD6, CHD4, GLTSCR1 and ATAD5). {ECO:0000250}.; DOMAIN: The C-terminal (CTD) region mediates interaction and recruitment of CDK9 and CCNT1 subunits of the P-TEFb complex. It is also required for maintenance of higher-order chromatin structure (By similarity). {ECO:0000250}. +Q3URV1 BROMI_MOUSE Protein broad-minded (TBC1 domain family member 32) 1296 148,061 Alternative sequence (1); Chain (1); Domain (1); Erroneous initiation (1) FUNCTION: Required for high-level Shh responses in the developing neural tube. Together with CDK20, controls the structure of the primary cilium by coordinating assembly of the ciliary membrane and axoneme, allowing GLI2 to be properly activated in response to Shh signaling. {ECO:0000269|PubMed:20159594}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20159594}. Cell projection, cilium {ECO:0000269|PubMed:20159594}. SUBUNIT: Interacts with CDK20, which promotes CDK20 stability and function. {ECO:0000269|PubMed:20159594}. +Q0Q236 BSPH2_MOUSE Binder of sperm protein homolog 2 131 15,641 Chain (1); Disulfide bond (4); Domain (2); Signal peptide (1) FUNCTION: Binds sperm in vitro but has no effect on sperm capacitation. Also binds gelatin and heparin, but not chondroitin sulfate B or phospholipid liposomes. {ECO:0000269|PubMed:24307707}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Epididymis. {ECO:0000269|Ref.2}. +Q8R2Q8 BST2_MOUSE Bone marrow stromal antigen 2 (BST-2) (HM1.24 antigen) (CD antigen CD317) 172 19,152 Chain (1); Coiled coil (1); Disulfide bond (3); Glycosylation (3); Helix (1); Lipidation (1); Propeptide (1); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 31 51 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 30 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 52 152 Extracellular. {ECO:0000255}. FUNCTION: IFN-induced antiviral host restriction factor which efficiently blocks the release of diverse mammalian enveloped viruses by directly tethering nascent virions to the membranes of infected cells. Acts as a direct physical tether, holding virions to the cell membrane and linking virions to each other. The tethered virions can be internalized by endocytosis and subsequently degraded or they can remain on the cell surface. In either case, their spread as cell-free virions is restricted. Its target viruses belong to diverse families, including retroviridae: human immunodeficiency virus type 1 (HIV-1), mouse mammary tumor virus (MMTV) and murine leukemia virus (MLV), filoviridae: ebola virus (EBOV), arenaviridae: lassa virus (LASV), and rhabdoviridae: vesicular stomatitis virus (VSV). Can inhibit cell surface proteolytic activity of MMP14 causing decreased activation of MMP15 which results in inhibition of cell growth and migration. Can stimulate signaling by LILRA4/ILT7 and consequently provide negative feedback to the production of IFN by plasmacytoid dendritic cells in response to viral infection. Plays a role in the organization of the subapical actin cytoskeleton in polarized epithelial cells. {ECO:0000269|PubMed:16920966, ECO:0000269|PubMed:19179289, ECO:0000269|PubMed:20686043, ECO:0000269|PubMed:20702620, ECO:0000269|PubMed:21919738, ECO:0000269|PubMed:22025715, ECO:0000269|PubMed:22284121, ECO:0000269|PubMed:22327075}. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network. Cell membrane; Single-pass type II membrane protein. Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. Late endosome {ECO:0000250}. Membrane raft {ECO:0000250}. Cytoplasm {ECO:0000250}. Apical cell membrane {ECO:0000250}. Note=Shuttles between the cell membrane, where it is present predominantly in membrane/lipid rafts, and the trans-Golgi network. Forms a complex with MMP14 and localizes to the cytoplasm (By similarity). {ECO:0000250}. SUBUNIT: Parallel homodimer; disulfide-linked. May form homotetramers under reducing conditions. Dimerization is essential for its antiviral activity. Interacts (via cytoplasmic domain) with ARHGAP44 (By similarity). Interacts with MMP14 (via C-terminal cytoplasmic tail) (By similarity). Interacts with LILRA4/ILT7 (By similarity). {ECO:0000250}. DOMAIN: The extracellular coiled coil domain forms an extended 170 A long semi-flexible rod-like structure important for virion retention at the cell surface and prevention of virus spreading. {ECO:0000250}. TISSUE SPECIFICITY: In naive mice, specifically expressed on type I interferon-producing cells (at protein level). {ECO:0000269|PubMed:16920966}. +Q8CFE5 BTBD7_MOUSE BTB/POZ domain-containing protein 7 (Function-unkown protein 1) 1130 126,243 Alternative sequence (4); Chain (1); Compositional bias (2); Domain (3); Erroneous initiation (1); Initiator methionine (1); Lipidation (1); Modified residue (2) FUNCTION: Acts as a mediator of epithelial dynamics and organ branching by promoting cleft progression. Induced following accumulation of fibronectin in forming clefts, leading to local expression of the cell-scattering SNAIL2 and suppression of E-cadherin levels, thereby altering cell morphology and reducing cell-cell adhesion. This stimulates cell separation at the base of forming clefts by local, dynamic intercellular gap formation and promotes cleft progression. {ECO:0000269|PubMed:20671187}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11527404}. TISSUE SPECIFICITY: Specifically expressed in embryonic epithelia. {ECO:0000269|PubMed:20671187}. +D3YUB6 BTBD8_MOUSE BTB/POZ domain-containing protein 8 377 41,583 Chain (1); Domain (2) SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Localized to nucleus in fetal cells. {ECO:0000250}. +Q9WVA3 BUB3_MOUSE Mitotic checkpoint protein BUB3 (WD repeat type I transmembrane protein A72.5) 326 36,955 Chain (1); Cross-link (1); Frameshift (1); Modified residue (2); Repeat (5); Sequence conflict (3) FUNCTION: Has a dual function in spindle-assembly checkpoint signaling and in promoting the establishment of correct kinetochore-microtubule (K-MT) attachments. Promotes the formation of stable end-on bipolar attachments. Necessary for kinetochore localization of BUB1. The BUB1/BUB3 complex plays a role in the inhibition of anaphase-promoting complex or cyclosome (APC/C) when spindle-assembly checkpoint is activated and inhibits the ubiquitin ligase activity of APC/C by phosphorylating its activator CDC20. This complex can also phosphorylate MAD1L1 (By similarity). Regulates chromosome segregation during oocyte meiosis. {ECO:0000250, ECO:0000269|PubMed:19888327}. PTM: Poly-ADP-ribosylated by PARP1. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:19888327}. Note=Starts to localize at kinetochores in prometaphase I (Pro-MI) stage and maintains the localization until the metaphase I-anaphase I (MI-AI) transition. {ECO:0000250}. SUBUNIT: Interacts with BUB1 and BUBR1. The BUB1/BUB3 complex interacts with MAD1L1. Interacts with ZNF207/BuGZ; leading to promote stability and kinetochore loading of BUB3 (By similarity). {ECO:0000250}. +P30993 C5AR1_MOUSE C5a anaphylatoxin chemotactic receptor 1 (C5a anaphylatoxin chemotactic receptor) (C5a-R) (C5aR) (CD antigen CD88) 351 39,023 Chain (1); Disulfide bond (1); Glycosylation (1); Modified residue (8); Sequence conflict (3); Topological domain (8); Transmembrane (7) TRANSMEM 38 64 Helical; Name=1. {ECO:0000250|UniProtKB:P21730}.; TRANSMEM 70 93 Helical; Name=2. {ECO:0000250|UniProtKB:P21730}.; TRANSMEM 111 132 Helical; Name=3. {ECO:0000250|UniProtKB:P21730}.; TRANSMEM 154 174 Helical; Name=4. {ECO:0000250|UniProtKB:P21730}.; TRANSMEM 202 227 Helical; Name=5. {ECO:0000250|UniProtKB:P21730}.; TRANSMEM 244 266 Helical; Name=6. {ECO:0000250|UniProtKB:P21730}.; TRANSMEM 284 304 Helical; Name=7. {ECO:0000250|UniProtKB:P21730}. TOPO_DOM 1 37 Extracellular. {ECO:0000305}.; TOPO_DOM 65 69 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 94 110 Extracellular. {ECO:0000305}.; TOPO_DOM 133 153 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 175 201 Extracellular. {ECO:0000305}.; TOPO_DOM 228 243 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 267 283 Extracellular. {ECO:0000305}.; TOPO_DOM 305 351 Cytoplasmic. {ECO:0000305}. FUNCTION: Receptor for the chemotactic and inflammatory peptide anaphylatoxin C5a. The ligand interacts with at least two sites on the receptor: a high-affinity site on the extracellular N-terminus, and a second site in the transmembrane region which activates downstream signaling events. Receptor activation stimulates chemotaxis, granule enzyme release, intracellular calcium release and superoxide anion production. {ECO:0000250|UniProtKB:P21730}. PTM: Sulfation plays a critical role in the association of C5aR with C5a, but no significant role in the ability of the receptor to transduce a signal and mobilize calcium in response to a small peptide agonist. {ECO:0000250|UniProtKB:P21730}.; PTM: Phosphorylated on serine residues in response to C5a binding, resulting in internalization of the receptor and short-term desensitization to C5a. {ECO:0000250|UniProtKB:P21730}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P21730}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P21730}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:P21730}. Note=Phosphorylated C5aR colocalizes with ARRB1 and ARRB2 in cytoplasmic vesicles. {ECO:0000250|UniProtKB:P21730}. SUBUNIT: Homodimer. May also form higher-order oligomers. Interacts (when phosphorylated) with ARRB1 and ARRB2; the interaction is associated with internalization of C5aR. {ECO:0000250|UniProtKB:P21730}. +Q8K207 CA021_MOUSE Uncharacterized protein C1orf21 homolog 121 13,882 Chain (1); Modified residue (2) +Q3U7U4 CA162_MOUSE Transmembrane protein C1orf162 homolog 132 14,354 Chain (1); Modified residue (1); Transmembrane (1) TRANSMEM 36 56 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q6PHS9 CA2D2_MOUSE Voltage-dependent calcium channel subunit alpha-2/delta-2 (Protein ducky) (Voltage-gated calcium channel subunit alpha-2/delta-2) [Cleaved into: Voltage-dependent calcium channel subunit alpha-2-2; Voltage-dependent calcium channel subunit delta-2] 1154 130,385 Alternative sequence (3); Chain (3); Disulfide bond (1); Domain (2); Frameshift (1); Glycosylation (7); Metal binding (3); Motif (1); Mutagenesis (4); Natural variant (1); Sequence conflict (9); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1117 1137 Helical. {ECO:0000255}. TOPO_DOM 19 1116 Extracellular. {ECO:0000255}.; TOPO_DOM 1138 1154 Cytoplasmic. {ECO:0000255}. FUNCTION: The alpha-2/delta subunit of voltage-dependent calcium channels regulates calcium current density and activation/inactivation kinetics of the calcium channel. Acts as a regulatory subunit for P/Q-type calcium channel (CACNA1A), N-type (CACNA1B), L-type (CACNA1C OR CACNA1D) and possibly T-type (CACNA1G). {ECO:0000269|PubMed:15331424}. PTM: N-glycosylated. {ECO:0000269|PubMed:11306709, ECO:0000269|PubMed:17052222}.; PTM: May be proteolytically processed into subunits alpha-2-2 and delta-2 that are disulfide-linked. It is however unclear whether such cleavage really takes place in vivo and has a functional role. According to PubMed:11306709, it is processed, at least in vitro, while according to PubMed:17052222, it is only poorly processed in vivo. {ECO:0000269|PubMed:11306709}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Colocalizes with CACNA1A in lipid raft fractions. {ECO:0000269|PubMed:11756448, ECO:0000269|PubMed:16928863}. SUBUNIT: Dimer formed of alpha-2-2 and delta-2 chains; disulfide-linked. Voltage-dependent calcium channels are multisubunit complexes, consisting of alpha-1 (CACNA1), alpha-2 (CACNA2D), beta (CACNB) and delta (CACNA2D) subunits in a 1:1:1:1 ratio (Probable). {ECO:0000305|PubMed:11306709}. DOMAIN: The MIDAS-like motif in the VWFA domain binds divalent metal cations and is required to promote trafficking of the alpha-1 (CACNA1) subunit to the plasma membrane by an integrin-like switch. TISSUE SPECIFICITY: Predominantly expressed in brain in a restricted pattern. Also expressed at lower level in kidney and testis Not expressed in lung at any moment of development. In brain, it localizes to sections of P21 brain. Expressed at high level in the cerebellum, with moderate levels in medulla, pons, and striatum. Also expressed in cortex, hippocampus, habenula and nucleus reticularis thalami (nRT). Strongly expressed in cerebellar Purkinje cells. {ECO:0000269|PubMed:10762351}. DISEASE: Note=Defects in Cacna2d2 are the cause of ducky phenotype (du). Du mice have spike-wave seizures characteristic of absence epilepsy and ataxia, with accompanying decreased calcium channel current in cerebellar Purkinje cells. {ECO:0000269|PubMed:11487633, ECO:0000269|PubMed:11756448, ECO:0000269|PubMed:14660671, ECO:0000269|PubMed:17135419}. +Q6PGH1 BUD31_MOUSE Protein BUD31 homolog (Protein G10 homolog) 144 17,000 Alternative sequence (1); Chain (1); Modified residue (1); Motif (1); Region (1) FUNCTION: Involved in the pre-mRNA splicing process. May play a role as regulator of AR transcriptional activity; may increase AR transcriptional activity. {ECO:0000250|UniProtKB:P41223}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P41223}. Note=Detected in chromatin at the promoter of AR target genes. {ECO:0000250|UniProtKB:P41223}. SUBUNIT: Identified in the spliceosome C complex. May interact with AR. {ECO:0000250|UniProtKB:P41223}. DOMAIN: Contains a short sequence motif (Phe-Xaa-Xaa-Phe-Tyr) that can bind to AR and may modulate AR activity. {ECO:0000250|UniProtKB:P41223}. +P28662 BRI3_MOUSE Brain protein I3 125 13,643 Chain (1); Compositional bias (1); Sequence conflict (1); Transmembrane (2) TRANSMEM 71 91 Helical. {ECO:0000255}.; TRANSMEM 92 112 Helical. {ECO:0000255}. FUNCTION: Participates in tumor necrosis factor-alpha (TNF)-induced cell death (Ref.4). May be a target of Wnt/beta-catenin signaling in the liver (By similarity). {ECO:0000250|UniProtKB:O95415, ECO:0000269|Ref.4}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:O95415}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Interacts with BRI3BP. {ECO:0000250|UniProtKB:O95415}. TISSUE SPECIFICITY: High expression in cerebral cortex, and in cerebellar cortex. +O35127 C10_MOUSE Protein C10 126 13,194 Chain (1); Initiator methionine (1); Modified residue (1) FUNCTION: In brain, may be required for corpus callusum development. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed, with higher expression in lung. {ECO:0000269|PubMed:23453665}. +P00920 CAH2_MOUSE Carbonic anhydrase 2 (EC 4.2.1.1) (Carbonate dehydratase II) (Carbonic anhydrase II) (CA-II) 260 29,033 Active site (3); Chain (1); Domain (1); Initiator methionine (1); Metal binding (3); Modified residue (4); Region (1); Sequence conflict (5) FUNCTION: Essential for bone resorption and osteoclast differentiation. Reversible hydration of carbon dioxide. Contributes to intracellular pH regulation in the duodenal upper villous epithelium during proton-coupled peptide absorption. Stimulates the chloride-bicarbonate exchange activity of SLC26A6. {ECO:0000269|PubMed:20150244}. SUBCELLULAR LOCATION: Cytoplasm. Cell membrane {ECO:0000250}. Note=Colocalized with SLC26A6 at the surface of the cell membrane in order to form a bicarbonate transport metabolon. Displaced from the cytosolic surface of the cell membrane by PKC in phorbol myristate acetate (PMA)-induced cells (By similarity). {ECO:0000250}. SUBUNIT: Interacts with SLC4A4. Interaction with SLC4A7 regulates SLC4A7 transporter activity. Interacts with SLC26A6 (By similarity). {ECO:0000250}. +Q5IR70 CAGE1_MOUSE Cancer-associated gene 1 protein homolog (CAGE-1) (Cancer/testis antigen 3 homolog) (CT3 homolog) 849 97,035 Alternative sequence (3); Chain (1); Coiled coil (1); Modified residue (1); Sequence conflict (2) TISSUE SPECIFICITY: Expressed in spermatids and spermatozoa. Localized to the acrosomal matrix and acrosomal granule. Predominantly expressed during postmeiotic stages of spermatogenesis. {ECO:0000269|PubMed:15819420}. +P15116 CADH2_MOUSE Cadherin-2 (Neural cadherin) (N-cadherin) (CD antigen CD325) 906 99,796 Beta strand (54); Chain (1); Compositional bias (1); Domain (5); Glycosylation (7); Helix (5); Metal binding (15); Mutagenesis (8); Propeptide (1); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (13) TRANSMEM 725 745 Helical. {ECO:0000255}. TOPO_DOM 160 724 Extracellular. {ECO:0000255}.; TOPO_DOM 746 906 Cytoplasmic. {ECO:0000255}. FUNCTION: Calcium-dependent cell adhesion protein; preferentially mediates homotypic cell-cell adhesion by dimerization with a CDH2 chain from another cell (PubMed:2762814, PubMed:11433297, PubMed:17988630, PubMed:9655503, PubMed:25253890). Cadherins may thus contribute to the sorting of heterogeneous cell types. Acts as a regulator of neural stem cells quiescence by mediating anchorage of neural stem cells to ependymocytes in the adult subependymal zone: upon cleavage by MMP24, CDH2-mediated anchorage is affected, leading to modulate neural stem cell quiescence (PubMed:24952463). CDH2 may be involved in neuronal recognition mechanism. In hippocampal neurons, may regulate dendritic spine density. {ECO:0000269|PubMed:11433297, ECO:0000269|PubMed:17988630, ECO:0000269|PubMed:24952463, ECO:0000269|PubMed:25253890, ECO:0000269|PubMed:2762814, ECO:0000269|PubMed:9655503}. PTM: Cleaved by MMP24. Ectodomain cleavage leads to the generation of a soluble 90 kDa amino-terminal soluble fragment and a 45 kDa membrane-bound carboxy-terminal fragment 1 (CTF1), which is further cleaved by gamma-secretase into a 35 kDa. Cleavage in neural stem cells by MMP24 affects CDH2-mediated anchorage of neural stem cells to ependymocytes in the adult subependymal zone, leading to modulate neural stem cell quiescence. {ECO:0000269|PubMed:19805319, ECO:0000269|PubMed:24952463}.; PTM: May be phosphorylated by OBSCN. {ECO:0000269|PubMed:23392350}.; PTM: O-glycosylated on Ser and Thr residues. {ECO:0000269|PubMed:21300292}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17988630, ECO:0000269|PubMed:26403541, ECO:0000269|PubMed:9655503}; Single-pass type I membrane protein {ECO:0000255}. Cell membrane, sarcolemma {ECO:0000269|PubMed:23392350}. Cell junction {ECO:0000250|UniProtKB:P19022}. Cell surface {ECO:0000269|PubMed:25232112, ECO:0000269|PubMed:9655503}. Note=Colocalizes with TMEM65 at the intercalated disk in cardiomyocytes (PubMed:26403541). Colocalizes with OBSCN at the intercalated disk and sarcolemma in cardiomyocytes (PubMed:23392350). {ECO:0000269|PubMed:23392350, ECO:0000269|PubMed:26403541}. SUBUNIT: Homodimer (via extracellular region) (PubMed:21300292, PubMed:25253890). Can also form heterodimers with other cadherins (via extracellular region) (PubMed:25253890). Dimerization occurs in trans, i.e. with a cadherin chain from another cell (PubMed:21300292, PubMed:25253890). Interacts with CDCP1 (By similarity). Interacts with PCDH8; this complex may also include TAOK2 (By similarity). The interaction with PCDH8 may lead to internalization through TAOK2/p38 MAPK pathway (By similarity). Identified in a complex containing FGFR4, NCAM1, CDH2, PLCG1, FRS2, SRC, SHC1, GAP43 and CTTN (PubMed:11433297). May interact with OBSCN (via protein kinase domain 2) (PubMed:23392350). {ECO:0000250|UniProtKB:P19022, ECO:0000250|UniProtKB:Q9Z1Y3, ECO:0000269|PubMed:11433297, ECO:0000269|PubMed:21300292, ECO:0000269|PubMed:23392350, ECO:0000269|PubMed:25253890}. DOMAIN: Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain. Calcium-binding sites are occupied sequentially in the order of site 3, then site 2 and site 1. {ECO:0000269|PubMed:21300292, ECO:0000269|PubMed:21366346}. TISSUE SPECIFICITY: Expressed in cardiac muscle (at protein level). {ECO:0000269|PubMed:23392350}. +Q8CE93 CAHM4_MOUSE Calcium homeostasis modulator protein 4 (Protein FAM26D) 315 35,429 Chain (1); Erroneous initiation (1); Transmembrane (4) TRANSMEM 12 34 Helical. {ECO:0000255}.; TRANSMEM 49 71 Helical. {ECO:0000255}.; TRANSMEM 108 130 Helical. {ECO:0000255}.; TRANSMEM 188 207 Helical. {ECO:0000255}. FUNCTION: Pore-forming subunit of a voltage-gated ion channel. {ECO:0000250|UniProtKB:Q8IU99}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +P18761 CAH6_MOUSE Carbonic anhydrase 6 (EC 4.2.1.1) (Carbonate dehydratase VI) (Carbonic anhydrase VI) (CA-VI) (Salivary carbonic anhydrase) (Secreted carbonic anhydrase) 317 36,495 Active site (2); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (1); Metal binding (3); Region (1); Sequence conflict (8); Signal peptide (1) FUNCTION: Reversible hydration of carbon dioxide. Its role in saliva is unknown. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Major constituent of saliva. +P55284 CADH5_MOUSE Cadherin-5 (Vascular endothelial cadherin) (VE-cadherin) (CD antigen CD144) 784 87,903 Beta strand (2); Chain (1); Compositional bias (1); Domain (5); Glycosylation (5); Metal binding (17); Mutagenesis (2); Propeptide (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 600 620 Helical. {ECO:0000255}. TOPO_DOM 46 599 Extracellular. {ECO:0000255}.; TOPO_DOM 621 784 Cytoplasmic. {ECO:0000255}. FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. This cadherin may play an important role in endothelial cell biology through control of the cohesion and organization of the intercellular junctions. Acts in concert with KRIT1 to establish and maintain correct endothelial cell polarity and vascular lumen. These effects are mediated by recruitment and activation of the Par polarity complex and RAP1B. Required for activation of PRKCZ and for localization of phosphorylated PRKCZ, PARD3, TIAM1 and RAP1B to the cell junction. {ECO:0000269|PubMed:20332120, ECO:0000269|PubMed:9220534}. PTM: Phosphorylated on tyrosine residues by KDR/VEGFR-2. Dephosphorylated by PTPRB. {ECO:0000269|PubMed:12234928}.; PTM: O-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction {ECO:0000269|PubMed:19635461}. Cell membrane {ECO:0000269|PubMed:19635461}; Single-pass type I membrane protein {ECO:0000269|PubMed:19635461}. Note=Found at cell-cell boundaries and probably at cell-matrix boundaries. KRIT1 and CDH5 reciprocally regulate their localization to endothelial cell-cell junctions (By similarity). {ECO:0000250|UniProtKB:P33151}. SUBUNIT: Interacts (via cadherin 5 domain) with PTPRB. Interacts with TRPC4. Interacts with KRIT1 (By similarity). Interacts with PARD3. {ECO:0000250, ECO:0000269|PubMed:12234928, ECO:0000269|PubMed:20047332}. DOMAIN: Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain. {ECO:0000250}. +Q8R3Z5 CACB1_MOUSE Voltage-dependent L-type calcium channel subunit beta-1 (CAB1) (Calcium channel voltage-dependent subunit beta 1) 597 65,486 Alternative sequence (4); Beta strand (10); Chain (1); Domain (1); Helix (14); Modified residue (11); Sequence conflict (2); Turn (2) FUNCTION: Regulatory subunit of L-type calcium channels. Regulates the activity of L-type calcium channels that contain CACNA1A as pore-forming subunit (By similarity). Regulates the activity of L-type calcium channels that contain CACNA1C as pore-forming subunit and increases the presence of the channel complex at the cell membrane. Required for functional expression L-type calcium channels that contain CACNA1D as pore-forming subunit. Regulates the activity of L-type calcium channels that contain CACNA1B as pore-forming subunit (By similarity). {ECO:0000250|UniProtKB:P19517, ECO:0000250|UniProtKB:Q02641}. SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P19517}; Peripheral membrane protein {ECO:0000250|UniProtKB:P19517}; Cytoplasmic side {ECO:0000250|UniProtKB:P19517}. Cell membrane {ECO:0000305|PubMed:21831364}; Peripheral membrane protein {ECO:0000250|UniProtKB:P19517}. SUBUNIT: Regulatory subunit of L-type calcium channels that consist of a pore-forming alpha subunit and auxiliary beta, gamma and delta subunits. Interacts with CACNA1A, CACNA1B, CACNA1C and CACNA1S. Component of a calcium channel complex consisting of a pore-forming alpha subunit (CACNA1S) and the ancillary subunits CACNB1 or CACNB2, CACNG1 and CACNA2D1 (By similarity). Interacts with CACNA1S (PubMed:28351836). Identified in a complex with CACNA1C. Identified in a complex with the L-type calcium channel subunits CACNA1C, CACNA2D1, CACNB1 and one of the gamma subunits (CACNG4, CACNG6, CACNG7, or CACNG8) (By similarity). Part of a L-type calcium channel complex that contains CACNA1D, CACNA2D1 and CACNB1. Part of a L-type calcium channel complex that contains CACNA1B, CACNA2D1 and CACNB1 (By similarity). Interacts with JSRP1 (PubMed:16638807). Interacts with RYR1 (PubMed:21320436). Interacts with CBARP (PubMed:24751537). {ECO:0000250|UniProtKB:P19517, ECO:0000250|UniProtKB:Q02641, ECO:0000269|PubMed:16638807, ECO:0000269|PubMed:21320436, ECO:0000269|PubMed:24751537, ECO:0000269|PubMed:28351836}. TISSUE SPECIFICITY: Detected in the inner nuclear layer in the retina (at protein level) (PubMed:21831364). Detected in skeletal muscle, brain, heart and spleen (PubMed:1385409). {ECO:0000269|PubMed:1385409, ECO:0000269|PubMed:21831364}. +P0DP26 CALM1_MOUSE Calmodulin-1 149 16,838 Beta strand (6); Calcium binding (4); Chain (1); Cross-link (2); Domain (4); Helix (9); Initiator methionine (1); Modified residue (11); Region (1); Sequence conflict (8) FUNCTION: Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis. Mediates calcium-dependent inactivation of CACNA1C. Positively regulates calcium-activated potassium channel activity of KCNN2. {ECO:0000250|UniProtKB:P62158}. PTM: Ubiquitination results in a strongly decreased activity. {ECO:0000250}.; PTM: Phosphorylation results in a decreased activity. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, spindle pole. Note=Distributed throughout the cell during interphase, but during mitosis becomes dramatically localized to the spindle poles and the spindle microtubules. {ECO:0000250}. SUBUNIT: Interacts with CEP97, CCP110, MYO1C, TTN/titin and SRY. Interacts with MYO10. Interacts with RRAD (By similarity). Interacts with USP6; the interaction is calcium dependent (By similarity). Interacts with CDK5RAP2. Interacts with SCN5A (By similarity). Interacts with FCHO1. Interacts with MIP in a 1:2 stoichiometry; the interaction with the cytoplasmic domains from two MIP subunits promotes MIP water channel closure. Interacts with ORAI1; this may play a role in the regulation of ORAI1-mediated calcium transport (By similarity). Interacts with RYR1 (PubMed:18650434). Interacts with MYO5A (PubMed:17151196). Interacts with IQCF1 (PubMed:25380116). Interacts with SYT7 (PubMed:24569478). Interacts with CEACAM1 (via cytoplasmic domain); this interaction is in a calcium dependent manner and reduces homophilic cell adhesion through dissociation of dimer (By similarity). Interacts with RYR2; regulates RYR2 calcium-release channel activity (PubMed:18650434). Interacts with PCP4; regulates calmodulin calcium-binding (By similarity). Interacts with the heterotetrameric KCNQ2 and KCNQ3 channel; the interaction is calcium-independent, constitutive and participates to the proper assembly of a functional heterotetrameric M channel (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P0DP23, ECO:0000250|UniProtKB:P62161, ECO:0000269|PubMed:17151196, ECO:0000269|PubMed:18650434, ECO:0000269|PubMed:24569478, ECO:0000269|PubMed:25380116}. +Q3UW68 CAN13_MOUSE Calpain-13 (EC 3.4.22.-) (Calcium-activated neutral proteinase 13) (CANP 13) 665 76,049 Active site (3); Chain (1); Domain (3) FUNCTION: Probable non-lysosomal thiol-protease. {ECO:0000250}. +Q9JLG8 CAN15_MOUSE Calpain-15 (EC 3.4.22.-) (Small optic lobes homolog) 1095 118,719 Active site (3); Alternative sequence (3); Chain (1); Compositional bias (1); Domain (1); Modified residue (4); Zinc finger (5) TISSUE SPECIFICITY: Expressed in olfactory bulbs (at protein level). {ECO:0000269|PubMed:10708520}. +Q91VA3 CAN8_MOUSE Calpain-8 (EC 3.4.22.53) (New calpain 2) (nCL-2) (Stomach-specific M-type calpain) 703 79,335 Active site (3); Alternative sequence (2); Calcium binding (2); Chain (1); Domain (5); Mutagenesis (1); Region (3); Sequence conflict (5) FUNCTION: Calcium-regulated non-lysosomal thiol-protease (By similarity). Involved in membrane trafficking in the gastric surface mucus cells (pit cells) and may involve the membrane trafficking of mucus cells via interactions with coat protein. Proteolytically cleaves the beta-subunit of coatomer complex. {ECO:0000250, ECO:0000269|PubMed:16476741}. PTM: Undergoes autolytic cleavage between Ala-5 and Ala-6 which gives rise to fragments extending from Ala-6 to the C-terminus, Ala-6 to the EF-hand 2 domain and from Ala-6 to the beginning of domain III. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus {ECO:0000269|PubMed:16476741}. SUBUNIT: Monomer and homooligomer. Interacts with COPS1/GPS1, COPB1, EYA2, NME2, NME4 and TOMM70. {ECO:0000269|PubMed:16476741, ECO:0000269|PubMed:17646163}. DOMAIN: The domain III mediates oligomerization. {ECO:0000269|PubMed:17646163}. TISSUE SPECIFICITY: Predominantly expressed in the stomach. Localizes strictly to the surface mucus cells in the gastric epithelium and the mucus-secreting goblet cells in the duodenum. {ECO:0000269|PubMed:11523006, ECO:0000269|PubMed:16476741}. +Q63810 CANB1_MOUSE Calcineurin subunit B type 1 (Protein phosphatase 2B regulatory subunit 1) (Protein phosphatase 3 regulatory subunit B alpha isoform 1) 170 19,300 Alternative sequence (1); Beta strand (3); Calcium binding (4); Chain (1); Domain (4); Helix (12); Initiator methionine (1); Lipidation (1); Modified residue (1); Region (1); Sequence conflict (1); Site (2) FUNCTION: Regulatory subunit of calcineurin, a calcium-dependent, calmodulin stimulated protein phosphatase. Confers calcium sensitivity. {ECO:0000269|PubMed:26794871}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:20639889}. Cell membrane {ECO:0000269|PubMed:20639889}. Cell membrane, sarcolemma {ECO:0000269|PubMed:20639889}. Cell membrane {ECO:0000250|UniProtKB:P63098}; Lipid-anchor {ECO:0000250|UniProtKB:P63098}. Note=Translocates from the cytosol to the sarcolemma in a CIB1-dependent manner during cardiomyocyte hypertrophy. {ECO:0000269|PubMed:20639889}. SUBUNIT: Forms a complex composed of a calmodulin-dependent catalytic subunit (also known as calcineurin A) and a regulatory Ca(2+)-binding subunit (also known as calcineurin B) (PubMed:26794871). There are three catalytic subunits, each encoded by a separate gene (PPP3CA, PPP3CB, and PPP3CC) and two regulatory subunits which are also encoded by separate genes (PPP3R1 and PPP3R2). The regulatory subunit confers calcium sensitivity. Interacts with catalytic subunit PPP3CA/calcineurin A (PubMed:26794871). Interacts with catalytic subunit PPP3CB/calcineurin A (By similarity). Isoform 1 and isoform 2 interact with CIB1 (via C-terminal region); the interaction increases upon cardiomyocyte hypertrophy (PubMed:20639889). {ECO:0000250|UniProtKB:P63098, ECO:0000269|PubMed:20639889, ECO:0000269|PubMed:26794871}. TISSUE SPECIFICITY: Brain specific. +Q6P8Y1 CAPSL_MOUSE Calcyphosin-like protein 208 24,115 Calcium binding (2); Chain (1); Domain (4); Erroneous initiation (2) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. +A2AIV8 CARD9_MOUSE Caspase recruitment domain-containing protein 9 536 62,462 Chain (1); Coiled coil (2); Domain (1); Modified residue (11) FUNCTION: Adapter protein that plays a key role in innate immune response to a number of intracellular pathogens, such as C.albicans and L.monocytogenes. Is at the crossroads of ITAM-tyrosine kinase and the Toll-like receptors (TLR) and NOD2 signaling pathways (PubMed:17514206). Probably controls various innate immune response pathways depending on the intracellular pathogen. Controls CLEC7A (dectin-1)-mediated myeloid cell activation induced by the yeast cell wall component zymosan, leading to cytokine production and innate anti-fungal immunity: acts by regulating BCL10-MALT1-mediated NF-kappa-B activation pathway. Activates NF-kappa-B via BCL10 (PubMed:16862125). In response to the hyphal form of C.albicans, mediates CLEC6A (dectin-2)-induced I-kappa-B kinase ubiquitination, leading to NF-kappa-B activation via interaction with BCL10 (PubMed:20538615). In response to L.monocytogenes infection, acts by connecting NOD2 recognition of peptidoglycan to downstream activation of MAP kinases (MAPK) without activating NF-kappa-B (PubMed:17187069). In response to fungal infection, may be required for the development and subsequent differentiation of interleukin 17-producing T helper (TH-17) cells (PubMed:17450144). Also involved in activation of myeloid cells via classical ITAM-associated receptors and TLR: required for TLR-mediated activation of MAPK, while it is not required for TLR-induced activation of NF-kappa-B (PubMed:17486093). {ECO:0000269|PubMed:16862125, ECO:0000269|PubMed:17187069, ECO:0000269|PubMed:17450144, ECO:0000269|PubMed:17486093, ECO:0000269|PubMed:17514206, ECO:0000269|PubMed:20538615}. PTM: Phosphorylated at Thr-531 and Thr-531 by CK2 following interaction with VHL, leading to inhibit the ability to activate NF-kappa-B. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with VHL; without leading to protein degradation (By similarity). Self-associates. Interacts (via CARD domain) with BCL10 (via CARD domain) (By similarity). Interacts with NOD2 (via NACHT domain)(PubMed:17187069, PubMed:24960071). Interacts with RIPK2 (PubMed:17187069). {ECO:0000250|UniProtKB:Q9EPY0, ECO:0000250|UniProtKB:Q9H257, ECO:0000269|PubMed:17187069, ECO:0000269|PubMed:24960071}. TISSUE SPECIFICITY: Expressed in myeloid cells. Not expressed in non-lymphoid organs. {ECO:0000269|PubMed:16862125, ECO:0000269|PubMed:17187069}. +P10598 CASB_MOUSE Beta-casein 231 25,337 Chain (1); Modified residue (5); Sequence conflict (11); Signal peptide (1) FUNCTION: Important role in determination of the surface properties of the casein micelles. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Mammary gland specific. Secreted in milk. +Q810S2 CB074_MOUSE Uncharacterized protein C2orf74 homolog 196 22,381 Chain (1); Erroneous initiation (1); Erroneous termination (1); Sequence conflict (5); Transmembrane (1) TRANSMEM 26 46 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q09LZ8 CBPC6_MOUSE Cytosolic carboxypeptidase 6 (EC 3.4.17.-) (ATP/GTP-binding protein-like 4) 540 62,210 Active site (1); Alternative sequence (2); Chain (1); Erroneous gene model prediction (8); Metal binding (3); Mutagenesis (2) FUNCTION: Metallocarboxypeptidase that mediates deglutamylation of target proteins (PubMed:17244818, PubMed:21074048, PubMed:25103237, PubMed:26829768). Catalyzes the deglutamylation of polyglutamate side chains generated by post-translational polyglutamylation in proteins such as tubulins (PubMed:17244818). Also removes polyglutamates from the carboxy-terminus of target proteins such as MYLK (PubMed:21074048). Mediates deglutamylation of CGAS, regulating the antiviral activity of CGAS (PubMed:26829768). Acts as a long-chain deglutamylase and specifically shortens long polyglutamate chains, while it is not able to remove the branching point glutamate, a process catalyzed by AGBL5/CCP5 (PubMed:25103237). {ECO:0000269|PubMed:17244818, ECO:0000269|PubMed:21074048, ECO:0000269|PubMed:25103237, ECO:0000269|PubMed:26829768}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:17244818}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q5VU57}. Golgi apparatus {ECO:0000250|UniProtKB:Q5VU57}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q5VU57}. Note=Colocalizes with gamma-tubulin in the centrioles at interphase and dividing cells and with glutamylated tubulin in basal bodies of ciliated cells. {ECO:0000250|UniProtKB:Q5VU57}. SUBUNIT: Interacts with MYLK. {ECO:0000269|PubMed:21074048}. TISSUE SPECIFICITY: Widely expressed. Expressed abundantly in testis, pituitary and brain and to a lower extent in eye, stomach, adrenal and kidney. In brain, expressed at low level in cerebellum as compared to cortex. {ECO:0000269|PubMed:17244818, ECO:0000269|PubMed:21074048, ECO:0000269|PubMed:25103237}. +Q8BXX9 CC169_MOUSE Coiled-coil domain-containing protein 169 214 24,754 Alternative sequence (1); Chain (1); Coiled coil (1) +Q80X53 CC116_MOUSE Coiled-coil domain-containing protein 116 541 59,879 Chain (1); Coiled coil (1); Modified residue (1); Sequence conflict (2) SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q8IYX3}. +Q6PB51 CC117_MOUSE Coiled-coil domain-containing protein 117 277 30,427 Chain (1); Coiled coil (1); Modified residue (2); Sequence conflict (2) +Q3U155 CC174_MOUSE Coiled-coil domain-containing protein 174 467 53,942 Chain (1); Coiled coil (2); Compositional bias (2); Modified residue (1); Sequence conflict (1) FUNCTION: Probably involved in neuronal development. {ECO:0000250|UniProtKB:Q6PII3}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6PII3}. +E9PVB3 CC175_MOUSE Coiled-coil domain-containing protein 175 822 97,122 Chain (1); Coiled coil (3) +Q8CDV0 CC178_MOUSE Coiled-coil domain-containing protein 178 866 103,041 Chain (1); Coiled coil (6); Sequence conflict (3) +Q6RUT8 CC154_MOUSE Coiled-coil domain-containing protein 154 (Golgin-160-like protein) 657 74,611 Alternative sequence (4); Chain (1); Coiled coil (4); Sequence conflict (5) SUBCELLULAR LOCATION: Early endosome {ECO:0000269|PubMed:22895184}. TISSUE SPECIFICITY: Expressed in brain, heart, lung, liver, spleen, kidney, testis, muscle, intestine and thymus. {ECO:0000269|PubMed:22895184}. +Q9QXV1 CBX8_MOUSE Chromobox protein homolog 8 (Polycomb 3 homolog) (Pc3) (mPc3) 362 39,860 Beta strand (2); Chain (1); Domain (1); Helix (1); Modified residue (8); Turn (1) FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility (By similarity). {ECO:0000250|UniProtKB:Q9HC52}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16537902}. Chromosome {ECO:0000269|PubMed:16537902}. Note=Localizes to the inactivated X chromosome in females. {ECO:0000269|PubMed:16537902}. SUBUNIT: Component of a PRC1-like complex (PubMed:16359901). Interacts with RING1, RNF2, PCGF1, PCGF2, PCGF3, BMI1, PCGF5, PCGF6 and PHC2 (PubMed:16359901). Interacts with histone H3 (By similarity). Interacts with MLLT3 (Ref.8). Interacts with PHC2 (By similarity). Interacts (via chromodomain) with single-stranded RNA (PubMed:16537902). {ECO:0000250|UniProtKB:Q9HC52, ECO:0000269|PubMed:11439343, ECO:0000269|PubMed:16359901, ECO:0000269|PubMed:16537902}. +Q8K2Q7 BROX_MOUSE BRO1 domain-containing protein BROX (BRO1 domain- and CAAX motif-containing protein) 411 46,202 Alternative sequence (2); Chain (1); Domain (1); Lipidation (1); Modified residue (1); Propeptide (1); Sequence conflict (1) SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. SUBUNIT: Interacts with CHMP4B. {ECO:0000250}. +Q9DCA5 BRX1_MOUSE Ribosome biogenesis protein BRX1 homolog (Brix domain-containing protein 2) 353 41,241 Chain (1); Cross-link (3); Domain (1); Erroneous initiation (2); Modified residue (2); Sequence conflict (3) FUNCTION: Required for biogenesis of the 60S ribosomal subunit. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. +Q9Z1S0 BUB1B_MOUSE Mitotic checkpoint serine/threonine-protein kinase BUB1 beta (EC 2.7.11.1) (MAD3/BUB1-related protein kinase) (BubR1) (Mitotic checkpoint kinase MAD3L) 1052 118,392 Active site (1); Binding site (1); Chain (1); Compositional bias (2); Domain (2); Modified residue (11); Motif (2); Nucleotide binding (1); Region (1); Sequence conflict (4); Site (2) FUNCTION: Essential component of the mitotic checkpoint. Required for normal mitosis progression and tumor suppression. The mitotic checkpoint delays anaphase until all chromosomes are properly attached to the mitotic spindle. One of its checkpoint functions is to inhibit the activity of the anaphase-promoting complex/cyclosome (APC/C) by blocking the binding of CDC20 to APC/C, independently of its kinase activity. The other is to monitor kinetochore activities that depend on the kinetochore motor CENPE. Required for kinetochore localization of CENPE. Negatively regulates PLK1 activity in interphase cells and suppresses centrosome amplification. Also implicated in triggering apoptosis in polyploid cells that exit aberrantly from mitotic arrest. Essential for tumor suppression. May play a role in regulating aging and fertility (By similarity). {ECO:0000250, ECO:0000269|PubMed:14744753, ECO:0000269|PubMed:15208629}. PTM: Proteolytically cleaved by caspase-3 in a cell cycle specific manner. The cleavage might be involved in the durability of the cell cycle delay. {ECO:0000250}.; PTM: Acetylation at Lys-243 regulates its degradation and timing in anaphase entry. {ECO:0000250}.; PTM: Ubiquitinated. Degraded by the proteasome (By similarity). {ECO:0000250}.; PTM: Sumoylated with SUMO2 and SUMO3. The sumoylation mediates the association with CENPE at the kinetochore (By similarity). {ECO:0000250}.; PTM: Autophosphorylated in vitro. Intramolecular autophosphorylation stimulated by CENPE. Phosphorylated during mitosis and hyperphosphorylated in mitotically arrested cells. Phosphorylation at Ser-659 and Ser-1033 occurs at kinetochores upon mitotic entry with dephosphorylation at the onset of anaphase. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:12925705, ECO:0000269|PubMed:17925231}. Note=Cytoplasmic in interphase cells (By similarity). Associates with the kinetochores in early prophase. Kinetochore localization requires BUB1, PLK1 and KNL1 (By similarity). {ECO:0000250}. SUBUNIT: Interacts with CENPE (PubMed:12925705). Interacts with CENPF, mitosin, PLK1 and BUB3. Part of a complex containing BUB3, CDC20 and BUB1B. Interacts with anaphase-promoting complex/cyclosome (APC/C). Interacts with KNL1. Interacts with RIPK3 (By similarity). {ECO:0000250|UniProtKB:O60566, ECO:0000269|PubMed:12925705}. DOMAIN: The D-box targets the protein for rapid degradation by ubiquitin-dependent proteolysis during the transition from mitosis to interphase. {ECO:0000305}.; DOMAIN: The BUB1 N-terminal domain directs kinetochore localization and binding to BUB3. TISSUE SPECIFICITY: Highly expressed in thymus followed by spleen. DISEASE: Note=Defects in Bub1b are involved in the development of lung and intestinal adenocarcinomas after exposure to a carcinogen. +Q91ZW8 C209D_MOUSE CD209 antigen-like protein D (DC-SIGN-related protein 3) (DC-SIGNR3) (CD antigen CD209) 237 26,925 Alternative sequence (1); Chain (1); Disulfide bond (3); Domain (1); Glycosylation (2); Metal binding (5); Topological domain (2); Transmembrane (1) TRANSMEM 55 75 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 54 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 76 237 Extracellular. {ECO:0000255}. FUNCTION: Probable pathogen-recognition receptor. May mediate the endocytosis of pathogens which are subsequently degraded in lysosomal compartments. May recognize in a calcium-dependent manner high mannose N-linked oligosaccharides in a variety of pathogen antigens. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. +Q91ZW7 C209E_MOUSE CD209 antigen-like protein E (DC-SIGN-related protein 4) (DC-SIGNR4) (CD antigen CD209) 208 24,389 Chain (1); Disulfide bond (3); Domain (1); Topological domain (2); Transmembrane (1) TRANSMEM 17 37 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 16 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 38 208 Extracellular. {ECO:0000255}. FUNCTION: Putative pathogen-recognition receptor. May mediate the endocytosis of pathogens which are subsequently degraded in lysosomal compartments. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. +Q8R066 C1QT4_MOUSE Complement C1q tumor necrosis factor-related protein 4 (C1q/TNF-related protein 4) 326 35,058 Chain (1); Domain (2); Frameshift (2); Sequence conflict (2); Signal peptide (1) FUNCTION: May be involved in the regulation of the inflammatory network. The role as pro- or anti-inflammatory seems to be context dependent (By similarity). Seems to have some role in regulating food intake and energy balance when administered in the brain. This effect is sustained over a two-day period, and it is accompanied by decreased expression of orexigenic neuropeptides in the hypothalamus 3 h post-injection (Probable). {ECO:0000250|UniProtKB:Q9BXJ3, ECO:0000269|PubMed:24366864}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24366864, ECO:0000269|PubMed:27086950}. SUBUNIT: Homomultimer. Forms trimers, hexamers and high molecular weight oligomers. {ECO:0000269|PubMed:24366864}. TISSUE SPECIFICITY: High expression in testis, kidney, and brain. Expressed in brain and kidney (at protein level). Within the brain, highly expressed in cerebellum, cortex, hippocampus and hippothalamus, and lower expression in hindbrain (at protein level). Serum levels were increased in leptin-deficient ob/ob mice (a genetic model of hyperphagia and morbid obesity) relative to age-matched lean controls. No difference in serum levels were detected between mice fed a low-fat versus high-fat diet for 14 weeks (PubMed:24366864). {ECO:0000269|PubMed:24366864}. +Q8CFG9 C1RB_MOUSE Complement C1r-B subcomponent (EC 3.4.21.41) (Complement component 1 subcomponent r-B) [Cleaved into: Complement C1r-B subcomponent heavy chain; Complement C1r-B subcomponent light chain] 706 79,936 Active site (3); Chain (3); Disulfide bond (13); Domain (6); Glycosylation (3); Modified residue (2); Signal peptide (1) FUNCTION: C1r B chain is a serine protease that combines with C1q and C1s to form C1, the first component of the classical pathway of the complement system. {ECO:0000250}. PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}. SUBUNIT: C1 is a calcium-dependent trimolecular complex of C1q, C1r and C1s in the molar ration of 1:2:2. C1r is a dimer of identical chains, each of which is activated by cleavage into two chains, A and B, connected by disulfide bonds (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Specifically expressed in male reproductive tissues. {ECO:0000269|PubMed:12513694}. +Q8CFW7 C2D2A_MOUSE Coiled-coil and C2 domain-containing protein 2A 1633 187,530 Alternative sequence (1); Chain (1); Coiled coil (2); Compositional bias (1); Domain (1); Sequence conflict (1) FUNCTION: Component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. Required for ciliogenesis and sonic hedgehog/SHH signaling. {ECO:0000269|PubMed:21725307, ECO:0000269|PubMed:22179047}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21725307}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:21725307}. Note=Localizes at the transition zone, a region between the basal body and the ciliary axoneme. SUBUNIT: Part of the tectonic-like complex (also named B9 complex). {ECO:0000269|PubMed:21725307, ECO:0000269|PubMed:22179047}. +Q9CPZ3 CA185_MOUSE Uncharacterized protein C1orf185 homolog 230 25,707 Alternative sequence (1); Chain (1); Glycosylation (1); Transmembrane (1) TRANSMEM 17 37 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q9CWU4 CA052_MOUSE UPF0690 protein C1orf52 homolog 180 20,101 Chain (1); Erroneous initiation (1); Modified residue (3) +Q8R2K8 CA054_MOUSE Uncharacterized protein C1orf54 homolog (Protein L259) 148 16,823 Alternative sequence (1); Chain (1); Glycosylation (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +B1ARW8 CA122_MOUSE Uncharacterized protein C1orf122 homolog 110 11,319 Chain (1); Coiled coil (1) +P97291 CADH8_MOUSE Cadherin-8 799 88,215 Beta strand (9); Chain (1); Domain (5); Glycosylation (4); Helix (1); Modified residue (1); Propeptide (1); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (4) TRANSMEM 622 642 Helical. {ECO:0000255}. TOPO_DOM 62 621 Extracellular. {ECO:0000255}.; TOPO_DOM 643 799 Cytoplasmic. {ECO:0000255}. FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. DOMAIN: Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain. {ECO:0000250}. +Q6PFX6 CAD24_MOUSE Cadherin-24 781 84,104 Chain (1); Domain (5); Glycosylation (3); Propeptide (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 604 624 Helical. {ECO:0000255}. TOPO_DOM 45 603 Extracellular. {ECO:0000255}.; TOPO_DOM 625 781 Cytoplasmic. {ECO:0000255}. FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. Cadherin-24 mediate strong cell-cell adhesion (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Associates with alpha-, beta- and delta-catenins. {ECO:0000250}. DOMAIN: Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain. {ECO:0000250}. +P55288 CAD11_MOUSE Cadherin-11 (OSF-4) (Osteoblast cadherin) (OB-cadherin) 796 88,112 Beta strand (19); Chain (1); Domain (5); Glycosylation (2); Helix (1); Modified residue (2); Propeptide (1); Sequence conflict (6); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (8) TRANSMEM 618 640 Helical. {ECO:0000255}. TOPO_DOM 54 617 Extracellular. {ECO:0000255}.; TOPO_DOM 641 796 Cytoplasmic. {ECO:0000255}. FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SUBUNIT: Interacts with PCDH8. {ECO:0000250}. DOMAIN: Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain. {ECO:0000250}. TISSUE SPECIFICITY: Selectively expressed in osteoblastic cell lines, precursor cell lines of osteoblasts, and primary osteoblastic cells from calvaria, as well as in lung, testis, and brain tissues at low levels. +Q5RJH3 CAD12_MOUSE Cadherin-12 794 88,468 Chain (1); Domain (5); Glycosylation (4); Modified residue (1); Propeptide (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 610 637 Helical. {ECO:0000255}. TOPO_DOM 55 609 Extracellular. {ECO:0000255}.; TOPO_DOM 638 794 Cytoplasmic. {ECO:0000255}. FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. DOMAIN: Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain. {ECO:0000250}. +Q9ERQ8 CAH7_MOUSE Carbonic anhydrase 7 (EC 4.2.1.1) (Carbonate dehydratase VII) (Carbonic anhydrase VII) (CA-VII) 264 29,915 Active site (2); Chain (1); Domain (1); Metal binding (3); Region (1) FUNCTION: Reversible hydration of carbon dioxide. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. +Q08331 CALB2_MOUSE Calretinin (CR) 271 31,373 Calcium binding (6); Chain (1); Domain (6); Modified residue (1) FUNCTION: Calretinin is a calcium-binding protein which is abundant in auditory neurons. +Q8BLQ9 CADM2_MOUSE Cell adhesion molecule 2 (Immunoglobulin superfamily member 4D) (IgSF4D) (Nectin-like protein 3) (NECL-3) (Synaptic cell adhesion molecule 2) (SynCAM 2) 435 47,559 Alternative sequence (2); Beta strand (8); Chain (1); Compositional bias (1); Disulfide bond (3); Domain (3); Glycosylation (3); Helix (1); Modified residue (1); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 368 388 Helical. {ECO:0000255}. TOPO_DOM 25 367 Extracellular. {ECO:0000255}.; TOPO_DOM 389 435 Cytoplasmic. {ECO:0000255}. FUNCTION: Adhesion molecule that engages in homo- and heterophilic interactions with the other nectin-like family members, leading to cell aggregation. Important for synapse organization, providing regulated trans-synaptic adhesion. Preferentially binds to oligodendrocytes (By similarity). {ECO:0000250}. PTM: Glycosylation at Asn-51 reduces adhesive binding. {ECO:0000269|PubMed:20739279}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein. Cell junction, synapse {ECO:0000250}. Cell projection, axon {ECO:0000250}. Note=Found in the axoplasm of myelinated axons. {ECO:0000250}. +Q99MP3 CALCB_MOUSE Calcitonin gene-related peptide 2 (Beta-type CGRP) (Calcitonin gene-related peptide II) (CGRP-II) 130 14,623 Disulfide bond (1); Modified residue (1); Peptide (1); Propeptide (2); Signal peptide (1) FUNCTION: CGRP induces vasodilation. It dilates a variety of vessels including the coronary, cerebral and systemic vasculature. Its abundance in the CNS also points toward a neurotransmitter or neuromodulator role (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Detected in nerve cells of cerebrum, hippocampus and pons/midbrain in newborns, and only in nerve cells of pons/midbrain in adult. {ECO:0000269|PubMed:18544925}. +Q63811 CANB2_MOUSE Calcineurin subunit B type 2 (Protein phosphatase 2B regulatory subunit 2) (Protein phosphatase 3 regulatory subunit B beta isoform) 179 20,659 Calcium binding (4); Chain (1); Domain (4); Initiator methionine (1); Lipidation (1); Region (1); Site (2) FUNCTION: Regulatory subunit of calcineurin, a calcium-dependent, calmodulin stimulated protein phosphatase. Confers calcium sensitivity. {ECO:0000250|UniProtKB:Q63810}. SUBUNIT: Forms a complex composed of a calmodulin-dependent catalytic subunit (also known as calcineurin A) and a regulatory Ca(2+)-binding subunit (also known as calcineurin B). There are three catalytic subunits, each encoded by a separate gene (PPP3CA, PPP3CB, and PPP3CC) and two regulatory subunits which are also encoded by separate genes (PPP3R1 and PPP3R2). {ECO:0000250|UniProtKB:Q63810}. TISSUE SPECIFICITY: Testis specific. {ECO:0000269|PubMed:1325794}. +P0DP27 CALM2_MOUSE Calmodulin-2 149 16,838 Calcium binding (4); Chain (1); Cross-link (2); Domain (4); Initiator methionine (1); Modified residue (11); Region (1) FUNCTION: Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis. Mediates calcium-dependent inactivation of CACNA1C. Positively regulates calcium-activated potassium channel activity of KCNN2. {ECO:0000250|UniProtKB:P62158}. PTM: Ubiquitination results in a strongly decreased activity. {ECO:0000250}.; PTM: Phosphorylation results in a decreased activity. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, spindle pole. Note=Distributed throughout the cell during interphase, but during mitosis becomes dramatically localized to the spindle poles and the spindle microtubules. {ECO:0000250}. SUBUNIT: Interacts with CEP97, CCP110, MYO1C, TTN/titin and SRY. Interacts with MYO10. Interacts with RRAD (By similarity). Interacts with USP6; the interaction is calcium dependent (By similarity). Interacts with CDK5RAP2. Interacts with SCN5A (By similarity). Interacts with FCHO1. Interacts with MIP in a 1:2 stoichiometry; the interaction with the cytoplasmic domains from two MIP subunits promotes MIP water channel closure. Interacts with ORAI1; this may play a role in the regulation of ORAI1-mediated calcium transport (By similarity). Interacts with RYR1 (PubMed:18650434). Interacts with MYO5A (By similarity). Interacts with IQCF1 (PubMed:25380116). Interacts with SYT7 (PubMed:24569478). Interacts with CEACAM1 (via cytoplasmic domain); this interaction is in a calcium dependent manner and reduces homophilic cell adhesion through dissociation of dimer (By similarity). Interacts with RYR2; regulates RYR2 calcium-release channel activity (PubMed:18650434). Interacts with PCP4; regulates calmodulin calcium-binding (By similarity). Interacts with the heterotetrameric KCNQ2 and KCNQ3 channel; the interaction is calcium-independent, constitutive and participates to the proper assembly of a functional heterotetrameric M channel (By similarity). {ECO:0000250|UniProtKB:P0DP24, ECO:0000250|UniProtKB:P0DP26, ECO:0000250|UniProtKB:P62161, ECO:0000269|PubMed:18650434, ECO:0000269|PubMed:24569478, ECO:0000269|PubMed:25380116}. +P40124 CAP1_MOUSE Adenylyl cyclase-associated protein 1 (CAP 1) 474 51,565 Beta strand (15); Chain (1); Compositional bias (2); Cross-link (1); Domain (1); Helix (1); Initiator methionine (1); Modified residue (11); Sequence conflict (3) FUNCTION: Directly regulates filament dynamics and has been implicated in a number of complex developmental and morphological processes, including mRNA localization and the establishment of cell polarity. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. SUBUNIT: Homodimer. Binds actin monomers (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. +Q3UHL1 CAMKV_MOUSE CaM kinase-like vesicle-associated protein 512 54,819 Chain (1); Compositional bias (1); Domain (1); Modified residue (3); Sequence conflict (1) FUNCTION: Does not appear to have detectable kinase activity. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Predominantly observed in association with the plasma membrane of soma and in neurites, both axons and dendrites. May be associated with vesicular structures (By similarity). {ECO:0000250}. SUBUNIT: Interacts with calmodulin, in the presence of calcium. {ECO:0000250}. DOMAIN: The protein kinase domain is predicted to be catalytically inactive. +Q6ZQ73 CAND2_MOUSE Cullin-associated NEDD8-dissociated protein 2 (Cullin-associated and neddylation-dissociated protein 2) (TBP-interacting protein of 120 kDa B) (TBP-interacting protein 120B) (p120 CAND2) 1235 135,633 Chain (1); Compositional bias (2); Erroneous initiation (1); Initiator methionine (1); Modified residue (1); Repeat (26); Sequence conflict (1) FUNCTION: Probable assembly factor of SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes that promotes the exchange of the substrate-recognition F-box subunit in SCF complexes, thereby playing a key role in the cellular repertoire of SCF complexes. {ECO:0000250}. PTM: Ubiquitinated and targeted for proteasomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Binds TBP, CNOT3 and UBE3C. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in embryonic limb buds. {ECO:0000269|PubMed:12207886}. +Q8C1B1 CAMP2_MOUSE Calmodulin-regulated spectrin-associated protein 2 (Calmodulin-regulated spectrin-associated protein 1-like protein 1) 1461 164,333 Alternative sequence (1); Chain (1); Coiled coil (3); Domain (2); Modified residue (22); Region (1); Sequence conflict (2) FUNCTION: Key microtubule-organizing protein that specifically binds the minus-end of non-centrosomal microtubules and regulates their dynamics and organization (PubMed:23169647). Specifically recognizes growing microtubule minus-ends and autonomously decorates and stabilizes microtubule lattice formed by microtubule minus-end polymerization (By similarity). Acts on free microtubule minus-ends that are not capped by microtubule-nucleating proteins or other factors and protects microtubule minus-ends from depolymerization (By similarity). In addition, it also reduces the velocity of microtubule polymerization (By similarity). Through the microtubule cytoskeleton, also regulates the organization of cellular organelles including the Golgi and the early endosomes (By similarity). Essential for the tethering, but not for nucleation of non-centrosomal microtubules at the Golgi: together with Golgi-associated proteins AKAP9 and PDE4DIP, required to tether non-centrosomal minus-end microtubules to the Golgi, an important step for polarized cell movement (By similarity). Also acts as a regulator of neuronal polarity and development: localizes to non-centrosomal microtubule minus-ends in neurons and stabilizes non-centrosomal microtubules, which is required for neuronal polarity, axon specification and dendritic branch formation (By similarity). Through the microtubule cytoskeleton, regulates the autophagosome transport (By similarity). {ECO:0000250|UniProtKB:Q08AD1}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q08AD1}. Golgi apparatus {ECO:0000250|UniProtKB:Q08AD1}. Note=Associated with the minus-end of microtubules and also detected at the centrosomes. Decorates the minus-end of microtubules by decreasing the rate of tubulin incorporation and remaining bound. The length of CAMSAP2-decorated stretches on the minus-end of microtubules is dependent on MAPRE1/EB1 and MAPRE3/EB3, which promote elongation of CAMSAP2-decorated microtubule stretches. Recruited to the Golgi apparatus by AKAP9 and PDE4DIP isoform 2/MMG8/SMYLE. In neurons, localizes to the minus-end of microtubules in axon and dendrites. {ECO:0000250|UniProtKB:Q08AD1}. SUBUNIT: Interacts with CAMSAP3 (PubMed:23169647). Interacts with KATNA1 and KATNB1; leading to regulate the length of CAMSAP2-decorated microtubule stretches (By similarity). Interacts with a complex formed by AKAP9 and PDE4DIP isoform 2/MMG8/SMYLE, which recruits CAMSAP2 to the Golgi (By similarity). Interacts with MAPRE1/EB1 (By similarity). {ECO:0000250|UniProtKB:Q08AD1, ECO:0000269|PubMed:23169647}. DOMAIN: The CKK domain binds microtubules and specifically recognizes the minus-end of microtubules. {ECO:0000250|UniProtKB:Q08AD1, ECO:0000255|PROSITE-ProRule:PRU00841}.; DOMAIN: The MBD (microtubule-binding domain) region can recognize some features of the microtubule lattice, which might contribute to the specific decoration of growing microtubule minus-ends by CAMSAP2. {ECO:0000250|UniProtKB:Q08AD1}. +P47757 CAPZB_MOUSE F-actin-capping protein subunit beta (CapZ beta) 277 31,345 Alternative sequence (2); Chain (1); Initiator methionine (1); Modified residue (4) FUNCTION: F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. Isoform 3 may play a role in spermatogenesis. Alternatively, may play a role in later maturation steps such as capacitation and fertilization which involve changes of membrane domains. Plays a role in the regulation of cell morphology and cytoskeletal organization (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 1: Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250}. Cytoplasm, myofibril, sarcomere {ECO:0000250}. Note=In cardiac muscle, isoform 1 is located at Z-disks of sarcomeres while isoform 2 is enriched at intercalated disks. {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 3: Cytoplasm, cytoskeleton, perinuclear theca, calyx {ECO:0000250}. Note=Isoform 3 is located to sperm head cytoskeletal structure tightly associated to the nucleus (By similarity). Isoform 3 colocalizes with the alpha subunit in testicular sperm and to the acrosome in elongating and condensing spermatids. {ECO:0000250}. SUBUNIT: Heterodimer of an alpha and a beta subunit. Interacts with ARHGAP17 and RCSD1/CAPZIP. Component of the WASH complex, composed of F-actin-capping protein subunit alpha (CAPZA1, CAPZA2 or CAPZA3), F-actin-capping protein subunit beta (CAPZB), WASHC1, WASHC2, WASHC3, WASHC4 and WASHC5. Isoform 2 also is a component of dynactin complex from brain, which contains the actin-related protein ARP1. Interacts with ACTG1. {ECO:0000250|UniProtKB:P47756}. TISSUE SPECIFICITY: Isoform 3 is testis-specific and is present in round spermatids, but not in pachytene spermatocytes or Sertoli cells. {ECO:0000269|PubMed:19341723}. +Q99KF0 CAR14_MOUSE Caspase recruitment domain-containing protein 14 (Bcl10-interacting MAGUK protein 2) (Bimp2) 999 113,497 Chain (1); Coiled coil (1); Domain (3); Modified residue (1); Region (1); Sequence conflict (1) FUNCTION: Acts as a scaffolding protein that can activate the inflammatory transcription factor NF-kappa-B and p38/JNK MAP kinase signaling pathways. Forms a signaling complex with BCL10 and MALT1, and activates MALT1 proteolytic activity and inflammatory gene expression. MALT1 is indispensable for CARD14-induced activation of NF-kappa-B and p38/JNK MAP kinases. May play a role in signaling mediated by TRAF2, TRAF3 and TRAF6 and protects cells against apoptosis. {ECO:0000250|UniProtKB:Q9BXL6}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BXL6}. SUBUNIT: Interacts (via CARD domain) with BCL10 (via CARD domain). Forms a complex with MALT1 and BCL10; resulting in the formation of a CBM (CARD14-BLC10-MALT1) complex. Interacts with TRAF2, TRAF3 and TRAF6. {ECO:0000250|UniProtKB:Q9BXL6}. DOMAIN: A linker region between the coiled-coil and PDZ region holds the protein in an inactive state. {ECO:0000250|UniProtKB:Q9BXL6}. +Q9D1I2 CAR19_MOUSE Caspase recruitment domain-containing protein 19 (Bcl10-interacting CARD protein) (BinCARD) 183 20,936 Chain (1); Disulfide bond (1); Domain (1); Transmembrane (1) TRANSMEM 122 142 Helical. {ECO:0000255}. FUNCTION: Plays a role in inhibiting the effects of BCL10-induced activation of NF-kappa-B. {ECO:0000250|UniProtKB:Q96LW7}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Mitochondrion membrane {ECO:0000250}; Single-pass membrane protein. SUBUNIT: Associates with BCL10 by CARD-CARD interaction. {ECO:0000250|UniProtKB:Q96LW7}. +Q6EDY6 CARL1_MOUSE F-actin-uncapping protein LRRC16A (CARMIL homolog) (Capping protein regulator and myosin 1 linker protein 1) (Capping protein, Arp2/3 and myosin-I linker homolog 1) (Capping protein, Arp2/3 and myosin-I linker protein 1) (CARML1) (Leucine-rich repeat-containing protein 16A) 1374 151,860 Alternative sequence (4); Beta strand (30); Chain (1); Coiled coil (1); Compositional bias (2); Erroneous initiation (2); Helix (30); Modified residue (14); Mutagenesis (3); Region (2); Repeat (11); Sequence conflict (6); Turn (4) FUNCTION: Cell membrane-cytoskeleton-associated protein that plays a role in the regulation of actin polymerization at the barbed end of actin filaments. Prevents F-actin heterodimeric capping protein (CP) activity at the leading edges of migrating cells, and hence generates uncapped barbed ends and enhances actin polymerization, however, seems unable to nucleate filaments (PubMed:16054028). Plays a role in lamellipodial protrusion formations and cell migration (PubMed:16054028). {ECO:0000269|PubMed:16054028}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16054028}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16054028}. Cell membrane {ECO:0000250|UniProtKB:Q5VZK9}. Cell projection, lamellipodium {ECO:0000269|PubMed:16054028}. Note=Found on macropinosomes (By similarity). Colocalized with heterodimeric capping protein (CP) and F-actin in lamellipodia but not with F-actin in stress fibers (PubMed:16054028). {ECO:0000250|UniProtKB:Q5VZK9, ECO:0000269|PubMed:16054028}. SUBUNIT: Homodimer (By similarity). Interacts (via C-terminus) with heterodimeric capping protein (CP); this interaction uncaps barbed ends capped by CP, enhances barbed-end actin polymerization and promotes lamellipodial formation and cell migration (PubMed:16054028). Interacts with MYO1E (By similarity). Interacts with TRIO (By similarity). {ECO:0000250|UniProtKB:Q5VZK9, ECO:0000269|PubMed:16054028}. DOMAIN: The C-terminus is necessary for localization to the cell membrane. {ECO:0000250|UniProtKB:Q5VZK9}. +Q3UFQ8 CARL3_MOUSE Capping protein, Arp2/3 and myosin-I linker protein 3 (Capping protein regulator and myosin 1 linker protein 3) (Leucine-rich repeat-containing protein 16B) 1375 150,416 Chain (1); Compositional bias (2); Repeat (10); Sequence caution (1) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8ND23}. Cell membrane {ECO:0000250|UniProtKB:Q8ND23}. DOMAIN: The C-terminus is necessary for localization to the cell membrane. {ECO:0000250|UniProtKB:Q8ND23}. +Q9JI81 CAT8_MOUSE Cathepsin 8 (EC 3.4.22.-) (Cathepsin 2) 333 37,803 Active site (3); Chain (1); Disulfide bond (3); Glycosylation (2); Propeptide (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Probable protease (By similarity). In placenta, plays a role in promoting giant cell differentiation (PubMed:18776147). Also plays a role in placental spiral artery remodeling by direct degradation of smooth muscle alpha-actin (PubMed:18776147). {ECO:0000250|UniProtKB:O60911, ECO:0000269|PubMed:18776147}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18776147}. Lysosome {ECO:0000269|PubMed:18776147}. Endosome {ECO:0000269|PubMed:18776147}. Note=Localizes to the cytoplasm with a punctate staining pattern indicative of a predominant lysosomal and endosomal localization. {ECO:0000269|PubMed:18776147}. TISSUE SPECIFICITY: Expressed in placenta (PubMed:11829493, PubMed:10885754, PubMed:18776147). Highly expressed in a subset of trophoblast giant cells in the parietal yolk sac and at the outside of the ectoplacental cone (PubMed:10885754). Expressed at highest level in liver with lesser amounts in testis, kidney, heart, lung and brain (PubMed:10885754). Not detected in spleen and skeletal muscle (PubMed:10885754, PubMed:11829493). Not detected in blood, heart, brain, testis, liver, lung, kidney, thymus or uterus (PubMed:11829493). {ECO:0000269|PubMed:10885754, ECO:0000269|PubMed:11829493, ECO:0000269|PubMed:18776147}. +P24270 CATA_MOUSE Catalase (EC 1.11.1.6) 527 59,795 Active site (2); Chain (1); Initiator methionine (1); Metal binding (1); Modified residue (21); Mutagenesis (1); Sequence conflict (7) FUNCTION: Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. Promotes growth of cells. SUBCELLULAR LOCATION: Peroxisome. SUBUNIT: Homotetramer. +O09165 CASQ1_MOUSE Calsequestrin-1 (Calmitine) (Calsequestrin, skeletal muscle isoform) 405 46,378 Chain (1); Compositional bias (1); Erroneous initiation (1); Glycosylation (1); Modified residue (4); Signal peptide (1) FUNCTION: Calsequestrin is a high-capacity, moderate affinity, calcium-binding protein and thus acts as an internal calcium store in muscle. Calcium ions are bound by clusters of acidic residues at the protein surface, often at the interface between subunits. Can bind around 80 Ca(2+) ions (By similarity). Regulates the release of lumenal Ca(2+) via the calcium release channel RYR1; this plays an important role in triggering muscle contraction. Negatively regulates store-operated Ca(2+) entry (SOCE) activity (By similarity). {ECO:0000250|UniProtKB:P31415, ECO:0000269|PubMed:17627988, ECO:0000269|PubMed:22049211, ECO:0000269|PubMed:7945294}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:P07221}. SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:P31415}. Sarcoplasmic reticulum {ECO:0000250|UniProtKB:P31415}. Sarcoplasmic reticulum lumen {ECO:0000269|PubMed:22049211, ECO:0000269|PubMed:7945294}. Sarcoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P07221}. Mitochondrion matrix {ECO:0000269|PubMed:7945294}. Note=This isoform of calsequestrin occurs in the sarcoplasmic reticulum's terminal cisternae luminal spaces of fast skeletal muscle cells (PubMed:22049211). Preferentially forms linear and round aggregates in the endoplasmic reticulum (ER) of resting cells. In a minority of cells, homogeneously detected in the ER lumen. Colocalizes with STIM1 at endoplasmic reticulum in response to a depletion of intracellular calcium (By similarity). {ECO:0000250|UniProtKB:P31415, ECO:0000269|PubMed:22049211}. SUBUNIT: Monomer; increases in response to a depletion of intracellular calcium. Homodimer. homotetramer and homopolymer. Can form linear homooligomers. Ca(2+) ions promote oligomerization. Interacts (via C-terminal end and preferentially with the monomeric form) with STIM1; this interaction increases in response to a depletion of intracellular calcium, decreases both STIM1 aggregation and clustering, interaction of STIM1 with ORAI1 and store-operated Ca(2+) entry (SOCE) activity. Interacts with ASPH and TRDN. {ECO:0000250|UniProtKB:P07221, ECO:0000250|UniProtKB:P31415}. TISSUE SPECIFICITY: Detected in skeletal muscle (at protein level). Detected in skeletal muscle. {ECO:0000269|PubMed:17627988, ECO:0000269|PubMed:22049211, ECO:0000269|PubMed:7945294, ECO:0000269|PubMed:9795116}. +Q920P3 BRNP1_MOUSE BMP/retinoic acid-inducible neural-specific protein 1 (Deleted in bladder cancer protein 1 homolog) 760 88,641 Alternative sequence (2); Chain (1); Domain (1); Glycosylation (7); Sequence conflict (4); Signal peptide (1) FUNCTION: Inhibits cell proliferation by negative regulation of the G1/S transition. Mediates cell death which is not of the classical apoptotic type and regulates expression of components of the plasminogen pathway. {ECO:0000269|PubMed:20025061}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain. Weakly expressed in embryonic stem (ES) cells and in ES-derived neural stem cells (NSCs). {ECO:0000269|PubMed:15193423, ECO:0000269|PubMed:20025061}. +Q3UW26 BSPH1_MOUSE Binder of sperm protein homolog 1 (Bovine seminal plasma protein homolog 1) (Bovine seminal plasma protein-like 1) 133 16,014 Chain (1); Disulfide bond (4); Domain (2); Glycosylation (1); Signal peptide (1) FUNCTION: Binds sperm in vitro and promotes sperm capacitation (PubMed:22539676, PubMed:24307707). Specifically promotes capacitation induced by high density lipoproteins (HDLs) (PubMed:25602034). Also binds heparin, phospholipid liposomes, and weakly to gelatin (PubMed:22539676). Does not bind chondroitin sulfate B (PubMed:22539676). {ECO:0000269|PubMed:22539676, ECO:0000269|PubMed:24307707, ECO:0000269|PubMed:25602034}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Expressed only in the epididymis. {ECO:0000269|PubMed:17085770}. +P35991 BTK_MOUSE Tyrosine-protein kinase BTK (EC 2.7.10.2) (Agammaglobulinemia tyrosine kinase) (ATK) (B-cell progenitor kinase) (BPK) (Bruton tyrosine kinase) (Kinase EMB) 659 76,437 Active site (1); Beta strand (18); Binding site (11); Chain (1); Domain (4); Helix (17); Initiator methionine (1); Metal binding (4); Modified residue (15); Motif (1); Mutagenesis (3); Natural variant (1); Nucleotide binding (1); Region (2); Sequence conflict (4); Turn (4); Zinc finger (1) FUNCTION: Non-receptor tyrosine kinase indispensable for B lymphocyte development, differentiation and signaling. Binding of antigen to the B-cell antigen receptor (BCR) triggers signaling that ultimately leads to B-cell activation. After BCR engagement and activation at the plasma membrane, phosphorylates PLCG2 at several sites, igniting the downstream signaling pathway through calcium mobilization, followed by activation of the protein kinase C (PKC) family members. PLCG2 phosphorylation is performed in close cooperation with the adapter protein B-cell linker protein BLNK. BTK acts as a platform to bring together a diverse array of signaling proteins and is implicated in cytokine receptor signaling pathways. Plays an important role in the function of immune cells of innate as well as adaptive immunity, as a component of the Toll-like receptors (TLR) pathway. The TLR pathway acts as a primary surveillance system for the detection of pathogens and are crucial to the activation of host defense. Especially, is a critical molecule in regulating TLR9 activation in splenic B-cells. Within the TLR pathway, induces tyrosine phosphorylation of TIRAP which leads to TIRAP degradation. BTK plays also a critical role in transcription regulation. Induces the activity of NF-kappa-B, which is involved in regulating the expression of hundreds of genes. BTK is involved on the signaling pathway linking TLR8 and TLR9 to NF-kappa-B. Transiently phosphorylates transcription factor GTF2I on tyrosine residues in response to BCR. GTF2I then translocates to the nucleus to bind regulatory enhancer elements to modulate gene expression. ARID3A and NFAT are other transcriptional target of BTK. BTK is required for the formation of functional ARID3A DNA-binding complexes. There is however no evidence that BTK itself binds directly to DNA. BTK has a dual role in the regulation of apoptosis. {ECO:0000269|PubMed:10852954, ECO:0000269|PubMed:11120822, ECO:0000269|PubMed:16738337, ECO:0000269|PubMed:17725607, ECO:0000269|PubMed:7538439, ECO:0000269|PubMed:8629002}. PTM: Following B-cell receptor (BCR) engagement, translocates to the plasma membrane where it gets phosphorylated at Tyr-551 by LYN and SYK. Phosphorylation at Tyr-551 is followed by autophosphorylation of Tyr-223 which may create a docking site for a SH2 containing protein. Phosphorylation at Ser-180 by PRKCB, leads in translocation of BTK back to the cytoplasmic fraction. Phosphorylation at Ser-21 and Ser-115 creates a binding site for PIN1 at these Ser-Pro motifs, and promotes it's recruitment (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11120822}. Cell membrane {ECO:0000269|PubMed:11120822}; Peripheral membrane protein {ECO:0000269|PubMed:11120822}. Nucleus {ECO:0000269|PubMed:11120822}. Note=In steady state, BTK is predominantly cytosolic. Following B-cell receptor (BCR) engagement by antigen, translocates to the plasma membrane through its PH domain. Plasma membrane localization is a critical step in the activation of BTK. A fraction of BTK also shuttles between the nucleus and the cytoplasm, and nuclear export is mediated by the nuclear export receptor CRM1. {ECO:0000250}. SUBUNIT: Binds GTF2I through the PH domain. Interacts with SH3BP5 via the SH3 domain. Interacts with IBTK via its PH domain (By similarity). Interacts with ARID3A. Interacts with CAV1, FASLG, PIN1, TLR8 and TLR9 (By similarity). {ECO:0000250}. DOMAIN: The PH domain mediates the binding to inositol polyphosphate and phosphoinositides, leading to its targeting to the plasma membrane. It is extended in the BTK kinase family by a region designated the TH (Tec homology) domain, which consists of about 80 residues preceding the SH3 domain. {ECO:0000269|PubMed:9240435}. DISEASE: Note=Defects in Btk are the cause of murine X-linked immunodeficiency (XID). +Q9CQH7 BT3L4_MOUSE Transcription factor BTF3 homolog 4 (Basic transcription factor 3-like 4) 158 17,271 Chain (1); Domain (1); Modified residue (2) +Q9D6W7 C16L2_MOUSE CD164 sialomucin-like 2 protein 172 18,220 Chain (1); Glycosylation (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 138 158 Helical. {ECO:0000255}. TOPO_DOM 30 137 Extracellular. {ECO:0000255}.; TOPO_DOM 159 172 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q8BG79 C19L2_MOUSE CWF19-like protein 2 887 103,173 Alternative sequence (2); Chain (1); Coiled coil (3); Compositional bias (2); Cross-link (2); Erroneous initiation (2); Modified residue (5); Sequence conflict (3) +Q9D211 C2AIL_MOUSE CDKN2AIP N-terminal-like protein (CDKN2A-interacting protein N-terminal-like protein) 116 13,209 Chain (1); Domain (1); Modified residue (1) SUBUNIT: Interacts with XRN2; the interaction is direct. {ECO:0000250|UniProtKB:Q96HQ2}. +Q922D8 C1TC_MOUSE C-1-tetrahydrofolate synthase, cytoplasmic (C1-THF synthase) [Cleaved into: C-1-tetrahydrofolate synthase, cytoplasmic, N-terminally processed] [Includes: Methylenetetrahydrofolate dehydrogenase (EC 1.5.1.5); Methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9); Formyltetrahydrofolate synthetase (EC 6.3.4.3)] 935 101,200 Binding site (1); Chain (2); Initiator methionine (1); Modified residue (4); Nucleotide binding (2); Region (5); Sequence conflict (2) One-carbon metabolism; tetrahydrofolate interconversion. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. DOMAIN: This trifunctional enzyme consists of two major domains: an N-terminal part containing the methylene-THF dehydrogenase and cyclohydrolase activities and a larger C-terminal part containing formyl-THF synthetase activity. +E9Q3C1 C2CD2_MOUSE C2 domain-containing protein 2 696 76,536 Chain (1); Domain (2); Erroneous initiation (1); Modified residue (4); Sequence conflict (6); Transmembrane (1) TRANSMEM 8 28 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q52KB6 C2CD3_MOUSE C2 domain-containing protein 3 (Protein hearty) 2323 255,346 Alternative sequence (4); Chain (1); Domain (2); Erroneous initiation (1); Modified residue (3); Sequence conflict (2) FUNCTION: Component of the centrioles that acts as a positive regulator of centriole elongation (PubMed:24997988). Promotes assembly of centriolar distal appendage, a structure at the distal end of the mother centriole that acts as an anchor of the cilium, and is required for recruitment of centriolar distal appendages proteins CEP83, SCLT1, CEP89, FBF1 and CEP164. Not required for centriolar satellite integrity or RAB8 activation (PubMed:24469809). Required for primary cilium formation. Required for sonic hedgehog/SHH signaling and for proteolytic processing of GLI3 (PubMed:19004860). {ECO:0000269|PubMed:19004860, ECO:0000269|PubMed:24469809, ECO:0000269|PubMed:24997988}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Note=Localizes to centrioles and procentrioles both in interphase and mitosis. Localizes to centriolar satellites, localization is dependent on PCM1 and dynein-mediated retrograde transport. Also localizes to the distal ends of the mother and daughter centrioles (PubMed:24469809). {ECO:0000269|PubMed:24469809}. SUBUNIT: Interacts with OFD1; OFD1 may act as a negative regulator of C2CD3. Associates with the BBSome complex (By similarity). Interacts with IFT88, BBS4 and PCM1. {ECO:0000250, ECO:0000269|PubMed:24469809}. +Q8R092 CA043_MOUSE Uncharacterized protein C1orf43 homolog 253 28,691 Alternative sequence (3); Chain (1); Sequence conflict (5); Transmembrane (1) TRANSMEM 11 31 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q5EBG8 CA050_MOUSE Uncharacterized protein C1orf50 homolog 199 21,863 Chain (1); Coiled coil (1) +Q9DAA7 CA100_MOUSE Uncharacterized protein C1orf100 homolog 145 16,975 Chain (1) +P97445 CAC1A_MOUSE Voltage-dependent P/Q-type calcium channel subunit alpha-1A (Brain calcium channel I) (BI) (Calcium channel, L type, alpha-1 polypeptide isoform 4) (Voltage-gated calcium channel subunit alpha Cav2.1) 2368 267,647 Calcium binding (1); Chain (1); Compositional bias (2); Glycosylation (2); Modified residue (16); Natural variant (1); Region (1); Repeat (4); Sequence conflict (8); Site (5); Topological domain (25); Transmembrane (24) TRANSMEM 101 119 Helical; Name=S1 of repeat I. {ECO:0000255}.; TRANSMEM 139 156 Helical; Name=S2 of repeat I. {ECO:0000255}.; TRANSMEM 169 184 Helical; Name=S3 of repeat I. {ECO:0000255}.; TRANSMEM 193 211 Helical; Name=S4 of repeat I. {ECO:0000255}.; TRANSMEM 231 250 Helical; Name=S5 of repeat I. {ECO:0000255}.; TRANSMEM 338 362 Helical; Name=S6 of repeat I. {ECO:0000255}.; TRANSMEM 490 509 Helical; Name=S1 of repeat II. {ECO:0000255}.; TRANSMEM 524 543 Helical; Name=S2 of repeat II. {ECO:0000255}.; TRANSMEM 552 570 Helical; Name=S3 of repeat II. {ECO:0000255}.; TRANSMEM 581 599 Helical; Name=S4 of repeat II. {ECO:0000255}.; TRANSMEM 619 638 Helical; Name=S5 of repeat II. {ECO:0000255}.; TRANSMEM 692 716 Helical; Name=S6 of repeat II. {ECO:0000255}.; TRANSMEM 1191 1214 Helical; Name=S1 of repeat III. {ECO:0000255}.; TRANSMEM 1232 1251 Helical; Name=S2 of repeat III. {ECO:0000255}.; TRANSMEM 1259 1282 Helical; Name=S3 of repeat III. {ECO:0000255}.; TRANSMEM 1294 1311 Helical; Name=S4 of repeat III. {ECO:0000255}.; TRANSMEM 1331 1350 Helical; Name=S5 of repeat III. {ECO:0000255}.; TRANSMEM 1438 1462 Helical; Name=S6 of repeat III. {ECO:0000255}.; TRANSMEM 1519 1537 Helical; Name=S1 of repeat IV. {ECO:0000255}.; TRANSMEM 1552 1573 Helical; Name=S2 of repeat IV. {ECO:0000255}.; TRANSMEM 1581 1600 Helical; Name=S3 of repeat IV. {ECO:0000255}.; TRANSMEM 1608 1626 Helical; Name=S4 of repeat IV. {ECO:0000255}.; TRANSMEM 1646 1665 Helical; Name=S5 of repeat IV. {ECO:0000255}.; TRANSMEM 1738 1763 Helical; Name=S6 of repeat IV. {ECO:0000255}. TOPO_DOM 1 100 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 120 138 Extracellular. {ECO:0000255}.; TOPO_DOM 157 168 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 185 192 Extracellular. {ECO:0000255}.; TOPO_DOM 212 230 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 251 337 Extracellular. {ECO:0000255}.; TOPO_DOM 363 489 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 510 523 Extracellular. {ECO:0000255}.; TOPO_DOM 544 551 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 571 580 Extracellular. {ECO:0000255}.; TOPO_DOM 600 618 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 639 691 Extracellular. {ECO:0000255}.; TOPO_DOM 717 1190 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1215 1231 Extracellular. {ECO:0000255}.; TOPO_DOM 1252 1258 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1283 1293 Extracellular. {ECO:0000255}.; TOPO_DOM 1312 1330 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1351 1437 Extracellular. {ECO:0000255}.; TOPO_DOM 1463 1518 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1538 1551 Extracellular. {ECO:0000255}.; TOPO_DOM 1574 1580 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1601 1607 Extracellular. {ECO:0000255}.; TOPO_DOM 1627 1645 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1666 1737 Extracellular. {ECO:0000255}.; TOPO_DOM 1764 2368 Cytoplasmic. {ECO:0000255}. FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1A gives rise to P and/or Q-type calcium currents. P/Q-type calcium channels belong to the 'high-voltage activated' (HVA) group and are specifically blocked by the spider omega-agatoxin-IVA (AC P54282) (By similarity). They are however insensitive to dihydropyridines (DHP). {ECO:0000250|UniProtKB:O00555, ECO:0000250|UniProtKB:P54282}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O00555}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Voltage-dependent calcium channels are multisubunit complexes, consisting of alpha-1, alpha-2, beta and delta subunits in a 1:1:1:1 ratio. The channel activity is directed by the pore-forming and voltage-sensitive alpha-1 subunit. In many cases, this subunit is sufficient to generate voltage-sensitive calcium channel activity. The auxiliary subunits beta and alpha-2/delta linked by a disulfide bridge regulate the channel activity. Interacts with CABP1 (By similarity).Interacts with the spider omega-agatoxin-IVA (AC P30288) (By similarity). {ECO:0000250|UniProtKB:O00555, ECO:0000250|UniProtKB:P54282}. DOMAIN: Each of the four internal repeats contains five hydrophobic transmembrane segments (S1, S2, S3, S5, S6) and one positively charged transmembrane segment (S4). S4 segments probably represent the voltage-sensor and are characterized by a series of positively charged amino acids at every third position. TISSUE SPECIFICITY: Brain specific; mainly found in the cerebellum, olfactory bulb, cerebral cortex, hippocampus, and inferior colliculus. In the hippocampus, expression occurs in pyramidal and granule neurons, as well as in interneurons. Purkinje cells contain predominantly P-type VSCC, the Q-type being a prominent calcium current in cerebellar granule cells. DISEASE: Note=Defects in Cacna1a are the cause of a delayed-onset, recessive neurological disorder seen in tottering (tg) mutants, resulting in ataxia, motor seizures and behavioral absence seizures resembling petit mal epilepsy (or absence epilepsy) in humans. There are two more alleles, leaner (tg(lA)), that is characterized by severe ataxia and frequent death past weaning, but no motor seizures; and rolling Nagoya (tg(rol)), that presents an intermediary phenotype, the ataxia being somewhat more severe that with tg, but without motors seizures. Selective degeneration of cerebellar Purkinje cells has been shown for all these types of mutants. Selective degeneration of cerebellar Purkinje cells has been shown for all these types of mutants. {ECO:0000269|PubMed:8929530}. +Q8R0S4 CACB4_MOUSE Voltage-dependent L-type calcium channel subunit beta-4 (CAB4) (Calcium channel voltage-dependent subunit beta 4) 519 57,950 Alternative sequence (2); Chain (1); Domain (1); Modified residue (6); Sequence conflict (1) FUNCTION: The beta subunit of voltage-dependent calcium channels contributes to the function of the calcium channel by increasing peak calcium current, shifting the voltage dependencies of activation and inactivation, modulating G protein inhibition and controlling the alpha-1 subunit membrane targeting. {ECO:0000250|UniProtKB:O00305}. SUBUNIT: The L-type calcium channel is composed of four subunits: alpha-1, alpha-2, beta and gamma. Interacts with FASLG (By similarity). Interacts with CBARP (PubMed:24751537). {ECO:0000250|UniProtKB:O00305, ECO:0000269|PubMed:24751537}. +O55017 CAC1B_MOUSE Voltage-dependent N-type calcium channel subunit alpha-1B (Brain calcium channel III) (BIII) (Calcium channel, L type, alpha-1 polypeptide isoform 5) (Voltage-gated calcium channel subunit alpha Cav2.2) 2327 261,481 Alternative sequence (1); Calcium binding (1); Chain (1); Compositional bias (2); Domain (1); Frameshift (1); Glycosylation (3); Modified residue (11); Natural variant (1); Nucleotide binding (1); Region (1); Repeat (4); Sequence conflict (26); Site (4); Topological domain (25); Transmembrane (24) TRANSMEM 96 114 Helical; Name=S1 of repeat I. {ECO:0000255}.; TRANSMEM 134 151 Helical; Name=S2 of repeat I. {ECO:0000255}.; TRANSMEM 165 179 Helical; Name=S3 of repeat I. {ECO:0000255}.; TRANSMEM 187 205 Helical; Name=S4 of repeat I. {ECO:0000255}.; TRANSMEM 226 245 Helical; Name=S5 of repeat I. {ECO:0000255}.; TRANSMEM 332 356 Helical; Name=S6 of repeat I. {ECO:0000255}.; TRANSMEM 483 502 Helical; Name=S1 of repeat II. {ECO:0000255}.; TRANSMEM 517 536 Helical; Name=S2 of repeat II. {ECO:0000255}.; TRANSMEM 545 563 Helical; Name=S3 of repeat II. {ECO:0000255}.; TRANSMEM 575 592 Helical; Name=S4 of repeat II. {ECO:0000255}.; TRANSMEM 612 631 Helical; Name=S5 of repeat II. {ECO:0000255}.; TRANSMEM 685 709 Helical; Name=S6 of repeat II. {ECO:0000255}.; TRANSMEM 1135 1158 Helical; Name=S1 of repeat III. {ECO:0000255}.; TRANSMEM 1176 1195 Helical; Name=S2 of repeat III. {ECO:0000255}.; TRANSMEM 1204 1226 Helical; Name=S3 of repeat III. {ECO:0000255}.; TRANSMEM 1242 1256 Helical; Name=S4 of repeat III. {ECO:0000255}.; TRANSMEM 1278 1297 Helical; Name=S5 of repeat III. {ECO:0000255}.; TRANSMEM 1384 1408 Helical; Name=S6 of repeat III. {ECO:0000255}.; TRANSMEM 1466 1484 Helical; Name=S1 of repeat IV. {ECO:0000255}.; TRANSMEM 1499 1518 Helical; Name=S2 of repeat IV. {ECO:0000255}.; TRANSMEM 1528 1546 Helical; Name=S3 of repeat IV. {ECO:0000255}.; TRANSMEM 1555 1573 Helical; Name=S4 of repeat IV. {ECO:0000255}.; TRANSMEM 1593 1612 Helical; Name=S5 of repeat IV. {ECO:0000255}.; TRANSMEM 1675 1694 Helical; Name=S6 of repeat IV. {ECO:0000255}. TOPO_DOM 1 95 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 115 133 Extracellular. {ECO:0000255}.; TOPO_DOM 152 164 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 180 186 Extracellular. {ECO:0000255}.; TOPO_DOM 206 225 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 246 331 Extracellular. {ECO:0000255}.; TOPO_DOM 357 482 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 503 516 Extracellular. {ECO:0000255}.; TOPO_DOM 537 544 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 564 574 Extracellular. {ECO:0000255}.; TOPO_DOM 593 611 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 632 684 Extracellular. {ECO:0000255}.; TOPO_DOM 710 1134 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1159 1175 Extracellular. {ECO:0000255}.; TOPO_DOM 1196 1203 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1227 1241 Extracellular. {ECO:0000255}.; TOPO_DOM 1257 1277 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1298 1383 Extracellular. {ECO:0000255}.; TOPO_DOM 1409 1465 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1485 1498 Extracellular. {ECO:0000255}.; TOPO_DOM 1519 1527 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1547 1554 Extracellular. {ECO:0000255}.; TOPO_DOM 1574 1592 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1613 1674 Extracellular. {ECO:0000255}.; TOPO_DOM 1695 2327 Cytoplasmic. {ECO:0000255}. FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1B gives rise to N-type calcium currents. N-type calcium channels belong to the 'high-voltage activated' (HVA) group and are specifically blocked by omega-conotoxin-GVIA (AC P01522) (By similarity). They are however insensitive to dihydropyridines (DHP). Calcium channels containing alpha-1B subunit may play a role in directed migration of immature neurons. {ECO:0000250|UniProtKB:Q02294}. PTM: Phosphorylated in vitro by CaM-kinase II, PKA, PKC and CGPK. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SUBUNIT: Multisubunit complex consisting of alpha-1, alpha-2, beta and delta subunits in a 1:1:1:1 ratio. The channel activity is directed by the pore-forming and voltage-sensitive alpha-1 subunit. In many cases, this subunit is sufficient to generate voltage-sensitive calcium channel activity. The auxiliary subunits beta and alpha-2/delta linked by a disulfide bridge regulate the channel activity. Interacts with RIMS1 (PubMed:11438518). Interacts with FMR1 (via C-terminus); this interaction induces a deacrease in the number of presynaptic functional CACNA1B channels at the cell surface (PubMed:24709664). Interacts with the omega-conotoxin-GVIA (AC P01522) (By similarity). {ECO:0000250|UniProtKB:Q02294, ECO:0000269|PubMed:11438518, ECO:0000269|PubMed:24709664}. DOMAIN: Each of the four internal repeats contains five hydrophobic transmembrane segments (S1, S2, S3, S5, S6) and one positively charged transmembrane segment (S4). S4 segments probably represent the voltage-sensor and are characterized by a series of positively charged amino acids at every third position. TISSUE SPECIFICITY: Widespread expression throughout the brain. Highest levels in pyramidal cell layers C1, C2 and C3 of the hippocampus, in the dentate gyrus, in the cortex layers 2 et 4, in the subiculum and the habenula. +Q8R0X2 CACL1_MOUSE CDK2-associated and cullin domain-containing protein 1 377 42,106 Alternative sequence (2); Chain (1); Compositional bias (2) FUNCTION: Cell cycle associated protein capable of promoting cell proliferation through the activation of CDK2 at the G1/S phase transition. {ECO:0000250}. SUBUNIT: Interacts with CDK2. {ECO:0000250}. +Q9JJG7 CABP8_MOUSE Calcium-binding protein 8 (CaBP8) (Calneuron I) (Calneuron-1) 219 24,823 Calcium binding (2); Chain (1); Domain (2); Topological domain (2); Transmembrane (1) TRANSMEM 193 213 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 1 192 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 214 219 Extracellular. {ECO:0000255}. FUNCTION: Negatively regulates Golgi-to-plasma membrane trafficking by interacting with PI4KB and inhibiting its activity (By similarity). May play a role in the physiology of neurons and is potentially important in memory and learning. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. SUBUNIT: Interacts with PI4KB. This binding competes with FREQ/NCS1 binding in a calcium-dependent manner (By similarity). {ECO:0000250}. DOMAIN: The C-terminal transmembrane domain (TMD) is necessary and sufficient for membrane targeting. {ECO:0000250}. TISSUE SPECIFICITY: Brain-specific. High expression in the cerebellum, hippocampus, and cortex. +Q8CGU1 CACO1_MOUSE Calcium-binding and coiled-coil domain-containing protein 1 (Coiled-coil coactivator protein) 691 77,280 Chain (1); Coiled coil (3); Erroneous initiation (1); Modified residue (1); Mutagenesis (3); Region (4); Sequence conflict (2) FUNCTION: Functions as a coactivator for aryl hydrocarbon and nuclear receptors (NR). Recruited to promoters through its contact with the N-terminal basic helix-loop-helix-Per-Arnt-Sim (PAS) domain of transcription factors or coactivators, such as NCOA2. During ER-activation acts synergistically in combination with other NCOA2-binding proteins, such as EP300, CREBBP and CARM1. Involved in the transcriptional activation of target genes in the Wnt/CTNNB1 pathway. Functions as a secondary coactivator in LEF1-mediated transcriptional activation via its interaction with CTNNB1. Coactivator function for nuclear receptors and LEF1/CTNNB1 involves differential utilization of two different activation regions. In association with CCAR1 enhances GATA1- and MED1-mediated transcriptional activation from the gamma-globin promoter during erythroid differentiation of K562 erythroleukemia cells (PubMed:24245781). {ECO:0000269|PubMed:14690606, ECO:0000269|PubMed:16931570, ECO:0000269|PubMed:24245781}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16931570}. Nucleus {ECO:0000269|PubMed:16931570}. Note=Shuttles between nucleus and cytoplasm. SUBUNIT: Part of a calphoglin complex consisting of CALCOCO1, PPA1 and PGM (By similarity). Interacts with the bHLH-PAS domains of GRIP1, AHR and ARNT. Interacts with CTNNB1 via both its N- and C-terminal regions. Interacts with EP300. Interacts with CCAR1 (via N-terminus) and GATA1. {ECO:0000250|UniProtKB:Q9P1Z2, ECO:0000269|PubMed:14690606, ECO:0000269|PubMed:15383530, ECO:0000269|PubMed:16344550, ECO:0000269|PubMed:16931570, ECO:0000269|PubMed:24245781}. DOMAIN: The C-terminal activation region (AD) is used for downstream signaling. Seems to be essential for coactivator function with nuclear receptors and with the aryl hydrocarbon receptor.; DOMAIN: The N-terminal activation region (AD) is necessary and sufficient for synergistic activation of LEF1-mediated transcription by CTNNB1. Contains a EP3000 binding region which is important for synergistic cooperation.; DOMAIN: Recruitment by nuclear receptors is accomplished by the interaction of the coiled-coiled domain with p160 coactivators. TISSUE SPECIFICITY: Expressed in all tissues examined except spleen, with high levels of expression in the heart and kidney. {ECO:0000269|PubMed:14690606, ECO:0000269|PubMed:15522220}. +Q99PF4 CAD23_MOUSE Cadherin-23 (Otocadherin) 3354 369,623 Alternative sequence (4); Beta strand (110); Chain (1); Domain (27); Glycosylation (42); Helix (21); Mutagenesis (3); Natural variant (12); Sequence conflict (10); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (24) TRANSMEM 3065 3085 Helical. {ECO:0000255}. TOPO_DOM 24 3064 Extracellular. {ECO:0000255}.; TOPO_DOM 3086 3354 Cytoplasmic. {ECO:0000255}. FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells. CDH23 is required for establishing and/or maintaining the proper organization of the stereocilia bundle of hair cells in the cochlea and the vestibule during late embryonic/early postnatal development. It is part of the functional network formed by USH1C, USH1G, CDH23 and MYO7A that mediates mechanotransduction in cochlear hair cells. Required for normal hearing. {ECO:0000269|PubMed:11138008}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000255}. SUBUNIT: Interacts with USH1C and USH1G (By similarity). antiparallel heterodimer with PCDH15. Isoform C1: Interacts with CAMSAP3; leading to inhibit CAMSAP3 ability to induce microtubule bundle formation (PubMed:27349180). {ECO:0000250|UniProtKB:Q9H251, ECO:0000269|PubMed:17805295, ECO:0000269|PubMed:20399731, ECO:0000269|PubMed:20498078, ECO:0000269|PubMed:23135401, ECO:0000269|PubMed:27349180}. DOMAIN: Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain. {ECO:0000250|UniProtKB:P12830}.; DOMAIN: Cadherin repeats 1 and 2 mediate calcium-dependent heterophilic interaction with PCDH15. {ECO:0000269|PubMed:23135401}. TISSUE SPECIFICITY: In adult animals relatively high levels of expression are found in testis, skeletal muscle, heart, eye and thymus, and lower expression in kidney, lung and brain. Found in the sensory hair cells of the inner ear. {ECO:0000269|PubMed:11138008}. DISEASE: Note=Defects in Cdh23 are the cause of waltzer (v) phenotype. Waltzer mice are characterized by deafness and vestibular dysfunction due to degeneration of the neuroepithelium within the inner ear. {ECO:0000269|PubMed:11138008, ECO:0000269|PubMed:11750125}. +Q9QWF0 CAF1A_MOUSE Chromatin assembly factor 1 subunit A (CAF-1 subunit A) (Chromatin assembly factor I p150 subunit) (CAF-I 150 kDa subunit) (CAF-I p150) 911 101,936 Beta strand (1); Chain (1); Compositional bias (3); Modified residue (5); Motif (1); Mutagenesis (2); Region (4); Turn (1) FUNCTION: Core component of the CAF-1 complex, a complex thought to mediate chromatin assembly in DNA replication and DNA repair. Assembles histone octamers onto replicating DNA in vitro. CAF-1 performs the first step of the nucleosome assembly process, bringing newly synthesized histones H3 and H4 to replicating DNA; histones H2A/H2B can bind to this chromatin precursor subsequent to DNA replication to complete the histone octamer. CHAF1A binds to histones H3 and H4. It may play a role in heterochromatin maintenance in proliferating cells by bringing newly synthesized cbx proteins to heterochromatic DNA replication foci. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Note=DNA replication foci. SUBUNIT: Homodimer (By similarity). Subunit of the CAF-1 complex that contains RBBP4, CHAF1B and CHAF1A. CHAF1A binds directly to CHAF1B. Only minor amounts of RBBP4 are complexed with CHAF1A and CHAF1B in G1 phase. CHAF1A binds directly to PCNA and to CBX1, CBX3 and CBX5. Binds MBD1. Interacts directly with CBX5 via the PxVxL motif. During DNA replication, it forms a S phase-specific complex that facilitates DNA methylation and histone H3 'Lys-9' methylation during replication-coupled chromatin assembly and is at least composed of the CHAF1A, MBD1 and SETDB1. Interacts with CBX5 (By similarity). {ECO:0000250}. DOMAIN: Contains one Pro-Xaa-Val-Xaa-Leu (PxVxL) motif, which is required for interaction with chromoshadow domains. This motif requires additional residues -7, -6, +4 and +5 of the central Val which contact the chromoshadow domain. +P59862 CAD26_MOUSE Cadherin-like protein 26 763 85,084 Chain (1); Compositional bias (1); Domain (4); Glycosylation (5); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 591 611 Helical. {ECO:0000255}. TOPO_DOM 21 590 Extracellular. {ECO:0000255}.; TOPO_DOM 612 763 Cytoplasmic. {ECO:0000255}. FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. Ligand for integrins alpha-E/beta-7, ITGAE:ITGAB7, alpha-4/beta-7, ITGA4:ITGAB7 and alpha-4/beta-1, ITGA4:ITGAB1 through which modulates CD4(+) T cells activation. {ECO:0000250|UniProtKB:Q8IXH8}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q8IXH8}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8IXH8}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q8IXH8}. SUBUNIT: Homodimer. Component of a cadherin:catenin adhesion complex composed of at least of CDH26, beta-catenin/CTNNB1, alpha-catenin/CTNNA1 and p120 catenin/CTNND1. {ECO:0000250|UniProtKB:Q8IXH8}. DOMAIN: Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain. {ECO:0000250}. +Q61290 CAC1E_MOUSE Voltage-dependent R-type calcium channel subunit alpha-1E (Brain calcium channel II) (BII) (Calcium channel, L type, alpha-1 polypeptide, isoform 6) (Voltage-gated calcium channel subunit alpha Cav2.3) 2272 257,236 Calcium binding (2); Chain (1); Compositional bias (7); Domain (1); Glycosylation (3); Modified residue (14); Region (1); Repeat (4); Site (4); Topological domain (25); Transmembrane (24) TRANSMEM 91 109 Helical; Name=S1 of repeat I. {ECO:0000255}.; TRANSMEM 129 147 Helical; Name=S2 of repeat I. {ECO:0000255}.; TRANSMEM 160 174 Helical; Name=S3 of repeat I. {ECO:0000255}.; TRANSMEM 187 206 Helical; Name=S4 of repeat I. {ECO:0000255}.; TRANSMEM 225 245 Helical; Name=S5 of repeat I. {ECO:0000255}.; TRANSMEM 328 351 Helical; Name=S6 of repeat I. {ECO:0000255}.; TRANSMEM 478 497 Helical; Name=S1 of repeat II. {ECO:0000255}.; TRANSMEM 511 530 Helical; Name=S2 of repeat II. {ECO:0000255}.; TRANSMEM 540 558 Helical; Name=S3 of repeat II. {ECO:0000255}.; TRANSMEM 569 587 Helical; Name=S4 of repeat II. {ECO:0000255}.; TRANSMEM 607 626 Helical; Name=S5 of repeat II. {ECO:0000255}.; TRANSMEM 680 704 Helical; Name=S6 of repeat II. {ECO:0000255}.; TRANSMEM 1151 1167 Helical; Name=S1 of repeat III. {ECO:0000255}.; TRANSMEM 1192 1211 Helical; Name=S2 of repeat III. {ECO:0000255}.; TRANSMEM 1220 1242 Helical; Name=S3 of repeat III. {ECO:0000255}.; TRANSMEM 1257 1274 Helical; Name=S4 of repeat III. {ECO:0000255}.; TRANSMEM 1294 1313 Helical; Name=S5 of repeat III. {ECO:0000255}.; TRANSMEM 1401 1424 Helical; Name=S6 of repeat III. {ECO:0000255}.; TRANSMEM 1482 1500 Helical; Name=S1 of repeat IV. {ECO:0000255}.; TRANSMEM 1516 1535 Helical; Name=S2 of repeat IV. {ECO:0000255}.; TRANSMEM 1544 1562 Helical; Name=S3 of repeat IV. {ECO:0000255}.; TRANSMEM 1574 1592 Helical; Name=S4 of repeat IV. {ECO:0000255}.; TRANSMEM 1612 1631 Helical; Name=S5 of repeat IV. {ECO:0000255}.; TRANSMEM 1701 1726 Helical; Name=S6 of repeat IV. {ECO:0000255}. TOPO_DOM 1 90 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 110 128 Extracellular. {ECO:0000255}.; TOPO_DOM 148 159 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 175 186 Extracellular. {ECO:0000255}.; TOPO_DOM 207 224 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 246 327 Extracellular. {ECO:0000255}.; TOPO_DOM 352 477 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 498 510 Extracellular. {ECO:0000255}.; TOPO_DOM 531 539 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 559 568 Extracellular. {ECO:0000255}.; TOPO_DOM 588 606 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 627 679 Extracellular. {ECO:0000255}.; TOPO_DOM 705 1150 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1168 1191 Extracellular. {ECO:0000255}.; TOPO_DOM 1212 1219 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1243 1256 Extracellular. {ECO:0000255}.; TOPO_DOM 1275 1293 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1314 1400 Extracellular. {ECO:0000255}.; TOPO_DOM 1425 1481 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1501 1515 Extracellular. {ECO:0000255}.; TOPO_DOM 1536 1543 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1563 1573 Extracellular. {ECO:0000255}.; TOPO_DOM 1593 1611 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1632 1700 Extracellular. {ECO:0000255}.; TOPO_DOM 1727 2272 Cytoplasmic. {ECO:0000255}. FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1E gives rise to R-type calcium currents. R-type calcium channels belong to the 'high-voltage activated' (HVA) group and are blocked by nickel. They are however insensitive to dihydropyridines (DHP). Calcium channels containing alpha-1E subunit could be involved in the modulation of firing patterns of neurons which is important for information processing. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SUBUNIT: Interacts with EFHC1. Voltage-dependent calcium channels are multisubunit complexes, consisting of alpha-1, alpha-2, beta and delta subunits in a 1:1:1:1 ratio. The channel activity is directed by the pore-forming and voltage-sensitive alpha-1 subunit. In many cases, this subunit is sufficient to generate voltage-sensitive calcium channel activity. The auxiliary subunits beta and alpha-2/delta linked by a disulfide bridge regulate the channel activity. DOMAIN: Each of the four internal repeats contains five hydrophobic transmembrane segments (S1, S2, S3, S5, S6) and one positively charged transmembrane segment (S4). S4 segments probably represent the voltage-sensor and are characterized by a series of positively charged amino acids at every third position. TISSUE SPECIFICITY: Expressed in neuronal tissues, retina, spleen, and pancreatic islet cells. +Q8C9E8 CAHM6_MOUSE Calcium homeostasis modulator protein 6 (Protein FAM26F) 313 34,956 Chain (1); Transmembrane (4) TRANSMEM 19 39 Helical. {ECO:0000255}.; TRANSMEM 52 72 Helical. {ECO:0000255}.; TRANSMEM 95 115 Helical. {ECO:0000255}.; TRANSMEM 174 194 Helical. {ECO:0000255}. FUNCTION: Pore-forming subunit of a voltage-gated ion channel. {ECO:0000250|UniProtKB:Q8IU99}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +P70407 CADH9_MOUSE Cadherin-9 (T1-cadherin) 786 88,301 Chain (1); Domain (5); Glycosylation (4); Modified residue (1); Propeptide (1); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 615 635 Helical. {ECO:0000255}. TOPO_DOM 22 614 Extracellular. {ECO:0000255}.; TOPO_DOM 636 786 Cytoplasmic. {ECO:0000255}. FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. DOMAIN: Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain. {ECO:0000250}. +D3Z291 CAHM1_MOUSE Calcium homeostasis modulator protein 1 348 38,827 Chain (1); Glycosylation (1); Topological domain (5); Transmembrane (4) TRANSMEM 17 37 Helical. {ECO:0000255}.; TRANSMEM 49 69 Helical. {ECO:0000255}.; TRANSMEM 108 128 Helical. {ECO:0000255}.; TRANSMEM 181 201 Helical. {ECO:0000255}. TOPO_DOM 1 16 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 38 48 Extracellular. {ECO:0000255}.; TOPO_DOM 70 107 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 129 180 Extracellular. {ECO:0000255}.; TOPO_DOM 202 348 Cytoplasmic. {ECO:0000255}. FUNCTION: Pore-forming subunit of a voltage-gated ion channel required for sensory perception of sweet, bitter and umami tastes. Specifically present in type II taste bud cells, where it plays a central role in sweet, bitter and umami taste perception by inducing ATP release from the cell, ATP acting as a neurotransmitter to activate afferent neural gustatory pathways. Acts both as a voltage-gated and calcium-activated ion channel: mediates neuronal excitability in response to changes in extracellular Ca(2+) concentration. Has poor ion selectivity and forms a wide pore (around 14 Angstroms) that mediates permeation of Ca(2+), Na(+) and K(+), as well as permeation of monovalent anions. Acts as an activator of the ERK1 and ERK2 cascade. Triggers endoplasmic reticulum stress by reducing the calcium content of the endoplasmic reticulum. May indirectly control amyloid precursor protein (APP) proteolysis and aggregated amyloid-beta (Abeta) peptides levels in a Ca(2+) dependent manner. {ECO:0000269|PubMed:22711817, ECO:0000269|PubMed:23467090}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8IU99}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8IU99}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Homohexamer. {ECO:0000250|UniProtKB:Q8IU99}. TISSUE SPECIFICITY: Specifically expressed in type II taste bud cells. Not expressed in brain. {ECO:0000269|PubMed:22711817, ECO:0000269|PubMed:22723178, ECO:0000269|PubMed:23467090}. +Q8VEC4 CAHM2_MOUSE Calcium homeostasis modulator protein 2 (Protein FAM26B) 323 35,823 Chain (1); Frameshift (1); Sequence conflict (3); Transmembrane (4) TRANSMEM 21 41 Helical. {ECO:0000255}.; TRANSMEM 55 75 Helical. {ECO:0000255}.; TRANSMEM 100 120 Helical. {ECO:0000255}.; TRANSMEM 185 205 Helical. {ECO:0000255}. FUNCTION: Pore-forming subunit of a voltage-gated ion channel. {ECO:0000250|UniProtKB:Q8IU99}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q99N28 CADM3_MOUSE Cell adhesion molecule 3 (Immunoglobulin superfamily member 4B) (IgSF4B) (Nectin-like protein 1) (NECL-1) (Synaptic cell adhesion molecule 3) (TSLC1-like protein 1) 396 42,964 Chain (1); Disulfide bond (3); Domain (3); Erroneous initiation (1); Glycosylation (1); Modified residue (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 329 349 Helical. {ECO:0000255}. TOPO_DOM 23 328 Extracellular. {ECO:0000255}.; TOPO_DOM 350 396 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in the cell-cell adhesion. Has both calcium-independent homophilic cell-cell adhesion activity and calcium-independent heterophilic cell-cell adhesion activity with IGSF4, NECTIN1 and NECTIN3. Interaction with EPB41L1 may regulate structure or function of cell-cell junctions. {ECO:0000269|PubMed:15741237, ECO:0000269|PubMed:15893517}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14659875, ECO:0000269|PubMed:15741237, ECO:0000269|PubMed:15893517}; Single-pass type I membrane protein {ECO:0000269|PubMed:15893517}. Cell junction {ECO:0000269|PubMed:14659875, ECO:0000269|PubMed:15741237, ECO:0000269|PubMed:15893517}. SUBUNIT: Homodimer. Can form trans-heterodimers with NECTIN3. Interacts with EPB41L1, DLG3, MPP6 and CASK. {ECO:0000269|PubMed:15741237, ECO:0000269|PubMed:15893517}. DOMAIN: The cytoplasmic region mediates interaction with EPB41L1, DLG3, MPP6 and CASK. TISSUE SPECIFICITY: Mainly expressed in brain, in neuronal cell bodies of cerebellum, cortex, hippocampus, hypothalamus and spinal cord. In spinal cord predominantly expressed in motor neurons. Expressed in axons, presynaptic nerve terminals, glia cell processes. {ECO:0000269|PubMed:14659875, ECO:0000269|PubMed:15741237, ECO:0000269|PubMed:15893517}. +Q9JM83 CALM4_MOUSE Calmodulin-4 (Calcium-binding protein Dd112) 148 16,767 Calcium binding (3); Chain (1); Domain (4); Sequence conflict (3) FUNCTION: Implicated in the early stage of ectopic ossification. +Q9R1W5 CALRL_MOUSE Calcitonin gene-related peptide type 1 receptor (CGRP type 1 receptor) (Calcitonin receptor-like receptor) 463 53,265 Chain (1); Disulfide bond (3); Glycosylation (6); Modified residue (2); Sequence conflict (2); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 146 165 Helical; Name=1. {ECO:0000255}.; TRANSMEM 173 192 Helical; Name=2. {ECO:0000255}.; TRANSMEM 213 235 Helical; Name=3. {ECO:0000255}.; TRANSMEM 253 272 Helical; Name=4. {ECO:0000255}.; TRANSMEM 289 312 Helical; Name=5. {ECO:0000255}.; TRANSMEM 336 353 Helical; Name=6. {ECO:0000255}.; TRANSMEM 366 387 Helical; Name=7. {ECO:0000255}. TOPO_DOM 23 145 Extracellular. {ECO:0000255}.; TOPO_DOM 166 172 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 193 212 Extracellular. {ECO:0000255}.; TOPO_DOM 236 252 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 273 288 Extracellular. {ECO:0000255}.; TOPO_DOM 313 335 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 354 365 Extracellular. {ECO:0000255}.; TOPO_DOM 388 463 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for calcitonin-gene-related peptide (CGRP) together with RAMP1 and receptor for adrenomedullin together with RAMP2 or RAMP3. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBUNIT: Heterodimer of CALCRL and RAMP1, RAMP2 or RAMP3. TISSUE SPECIFICITY: Expressed predominantly in the lung, thymus, heart and brain. {ECO:0000269|PubMed:10777702, ECO:0000269|PubMed:12147211}. +Q9CYT6 CAP2_MOUSE Adenylyl cyclase-associated protein 2 (CAP 2) 476 52,862 Chain (1); Domain (1); Modified residue (2); Sequence conflict (1) FUNCTION: May have a regulatory bifunctional role. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. +Q6ZQ38 CAND1_MOUSE Cullin-associated NEDD8-dissociated protein 1 (Cullin-associated and neddylation-dissociated protein 1) (p120 CAND1) 1230 136,332 Chain (1); Compositional bias (1); Erroneous initiation (3); Initiator methionine (1); Modified residue (4); Repeat (27) FUNCTION: Key assembly factor of SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes that promotes the exchange of the substrate-recognition F-box subunit in SCF complexes, thereby playing a key role in the cellular repertoire of SCF complexes. Acts as a F-box protein exchange factor. The exchange activity of CAND1 is coupled with cycles of neddylation conjugation: in the deneddylated state, cullin-binding CAND1 binds CUL1-RBX1, increasing dissociation of the SCF complex and promoting exchange of the F-box protein. Probably plays a similar role in other cullin-RING E3 ubiquitin ligase complexes (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Predominantly cytoplasmic. {ECO:0000250}. SUBUNIT: Interacts with TBP (By similarity). Part of a complex that contains CUL1 and RBX1. Interacts with unneddylated cullins: interacts with CUL1, CUL2, CUL3, CUL4A, CUL4B and CUL5. Does not bind neddylated CUL1. Interaction with cullins is abolished in presence of COMMD1, which antagonizes with CAND1 for interacting with cullins (By similarity). Interacts with DCUN1D3 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q86VP6}. +Q9ESK3 CAN10_MOUSE Calpain-10 (EC 3.4.22.-) (Calcium-activated neutral proteinase 10) (CANP 10) 666 74,596 Active site (3); Chain (1); Domain (1); Region (2); Sequence conflict (4) FUNCTION: Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. May play a role in insulin-stimulated glucose uptake (By similarity). {ECO:0000250}. +Q9ER56 CAN12_MOUSE Calpain-12 (EC 3.4.22.-) (Calcium-activated neutral proteinase 12) (CANP 12) 720 80,588 Active site (3); Alternative sequence (6); Calcium binding (1); Chain (1); Domain (2); Region (2) FUNCTION: Calcium-regulated non-lysosomal thiol-protease. {ECO:0000250}. TISSUE SPECIFICITY: Expression localized to the cortex of the hair follicle during the anagen phase of hair cycle. +O35646 CAN6_MOUSE Calpain-6 641 74,543 Chain (1); Domain (2); Region (1); Sequence conflict (1) FUNCTION: Microtubule-stabilizing protein that may be involved in the regulation of microtubule dynamics and cytoskeletal organization. May act as a regulator of RAC1 activity through interaction with ARHGEF2 to control lamellipodial formation and cell mobility. Does not seem to have protease activity as it has lost the active site residues. {ECO:0000269|PubMed:17210638, ECO:0000269|PubMed:21406564}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:17210638, ECO:0000269|PubMed:20814968}. SUBUNIT: Interacts (via domain III) with microtubules. Interacts (via domain II) with ARHGEF2 (via the N-terminal zinc finger). {ECO:0000269|PubMed:17210638, ECO:0000269|PubMed:21406564}. +Q8BYR5 CAPS2_MOUSE Calcium-dependent secretion activator 2 (Calcium-dependent activator protein for secretion 2) (CAPS-2) 1297 147,841 Alternative sequence (9); Chain (1); Domain (3); Erroneous initiation (1); Frameshift (2); Modified residue (2); Region (1); Sequence conflict (12) FUNCTION: Calcium-binding protein involved in exocytosis of vesicles filled with neurotransmitters and neuropeptides. Probably acts upstream of fusion in the biogenesis or maintenance of mature secretory vesicles. Regulates neurotrophin release from granule cells leading to regulate cell differentiation and survival during cerebellar development. May specifically mediate the Ca(2+)-dependent exocytosis of large dense-core vesicles (DCVs) and other dense-core vesicles. SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell junction, synapse {ECO:0000269|PubMed:14530279, ECO:0000269|PubMed:15820695}. Note=Membrane-associated to vesicles. Strongly enriched in synaptic fractions. Probably localizes to different vesicles compared to CADPS. Enriched on vesicular structures in the parallel fiber terminal of granule cells that are distinct from synaptic vesicles. SUBUNIT: Homodimer. Interacts with the dopamine receptor DRD2 (By similarity). {ECO:0000250}. DOMAIN: The PH domain is essential for regulated exocytosis and binds phospholipids. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in cerebellum. Also expressed in non-neuronal tissues such as lung, spleen, testis, uterus and ovary. Highly expressed in brain. In brain, it is highly expressed in cerebellum, cortex, olfactory bulb, CA1/CA2 regions of the hippocampus, and dentate gyrus, and weakly or not expressed in the CA3 regions of the hippocampus, striatum, thalamus, superior and inferior colliculi, and brain stem. Not present in adult adrenal glands. Isoform 4, but not isoform 3, is highly expressed in postnatal and adult stages of cerebellum. {ECO:0000269|PubMed:14530279, ECO:0000269|PubMed:15820695}. +P58660 CAR10_MOUSE Caspase recruitment domain-containing protein 10 (Bcl10-interacting MAGUK protein 1) (Bimp1) 1021 114,414 Chain (1); Coiled coil (1); Compositional bias (1); Domain (1); Modified residue (1) FUNCTION: Activates NF-kappa-B via BCL10 and IKK. SUBUNIT: CARD10 and BCL10 bind to each other by CARD-CARD interaction. They both participate in a complex with MALT1, where MALT1 binds to BCL10. TISSUE SPECIFICITY: Highly expressed in kidney, heart followed by brain, lung, liver, skeletal muscle and testis. +Q80UY1 CARME_MOUSE Carnosine N-methyltransferase (EC 2.1.1.22) 400 46,339 Chain (1); Sequence conflict (2) FUNCTION: N-methyltransferase that mediates the formation of anserine (beta-alanyl-N(Pi)-methyl-L-histidine) from carnosine. Anserine, a methylated derivative of carnosine (beta-alanyl-L-histidine), is an abundant constituent of vertebrate skeletal muscles. Also methylates other L-histidine-containing di- and tripeptides such as Gly-Gly-His, Gly-His and homocarnosine (GABA-His). {ECO:0000250|UniProtKB:Q5BJZ6}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q5BJZ6}. Nucleus {ECO:0000250|UniProtKB:Q5BJZ6}. +P49817 CAV1_MOUSE Caveolin-1 178 20,539 Alternative sequence (1); Chain (1); Cross-link (6); Initiator methionine (1); Intramembrane (1); Lipidation (3); Modified residue (7); Region (2); Sequence conflict (1); Topological domain (2) INTRAMEM 105 125 Helical. {ECO:0000255}. TOPO_DOM 2 104 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 126 178 Cytoplasmic. {ECO:0000255}. FUNCTION: May act as a scaffolding protein within caveolar membranes (By similarity). Forms a stable heterooligomeric complex with CAV2 that targets to lipid rafts and drives caveolae formation. Mediates the recruitment of CAVIN proteins (CAVIN1/2/3/4) to the caveolae (PubMed:19546242). Interacts directly with G-protein alpha subunits and can functionally regulate their activity (By similarity). Involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Its binding to DPP4 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner (By similarity). Recruits CTNNB1 to caveolar membranes and may regulate CTNNB1-mediated signaling through the Wnt pathway (PubMed:10816572). Negatively regulates TGFB1-mediated activation of SMAD2/3 by mediating the internalization of TGFBR1 from membrane rafts leading to its subsequent degradation (By similarity). {ECO:0000250|UniProtKB:Q03135, ECO:0000269|PubMed:10816572, ECO:0000269|PubMed:19546242}. PTM: The N-terminus of both isoforms are blocked.; PTM: Phosphorylated at Tyr-14 by ABL1 in response to oxidative stress. {ECO:0000269|PubMed:12036959, ECO:0000269|PubMed:12531427}.; PTM: Ubiquitinated. Undergo monoubiquitination and multi- and/or polyubiquitination. Monoubiquitination of N-terminal lysines promotes integration in a ternary complex with UBXN6 and VCP which promotes oligomeric CAV1 targeting to lysosomes for degradation. {ECO:0000250|UniProtKB:Q03135}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Membrane, caveola {ECO:0000269|PubMed:19546242, ECO:0000269|PubMed:21610094}; Peripheral membrane protein {ECO:0000269|PubMed:21610094}. Membrane raft {ECO:0000250|UniProtKB:Q03135}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:P33724}. Note=Colocalized with DPP4 in membrane rafts. Potential hairpin-like structure in the membrane. Membrane protein of caveolae (By similarity). {ECO:0000250}. SUBUNIT: Homooligomer. Interacts (via the N-terminus) with DPP4; the interaction is direct. Forms a stable heterooligomeric complex with CAV2 that targets to lipid rafts and drives caveolae formation. Interacts with BMX, BTK, CTNNB1, CDH1, GLIPR2, JUP, NOSTRIN, SNAP25 and STX1A. Interacts with SLC7A9. Interacts with TGFBR1 (By similarity). Interacts with PACSIN2 (PubMed:21610094). Interacts with CAVIN3 (via leucine-zipper domain) in a cholesterol-sensitive manner. Interacts with EHD2 in a cholesterol-dependent manner (By similarity). Interacts with CAVIN1 (PubMed:19546242). Forms a ternary complex with UBXN6 and VCP; mediates CAV1 targeting to lysosomes for degradation (By similarity). {ECO:0000250|UniProtKB:P41350, ECO:0000250|UniProtKB:Q03135, ECO:0000269|PubMed:19546242, ECO:0000269|PubMed:21610094}. TISSUE SPECIFICITY: Adipose tissue, lung, heart, skeletal muscle, stomach, small bowel, kidney, spleen and testis (at protein level). {ECO:0000269|PubMed:19546242}. +Q149G0 CB068_MOUSE UPF0561 protein C2orf68 homolog 166 18,643 Chain (1); Compositional bias (1); Frameshift (1) +Q9D9H8 CB069_MOUSE UPF0565 protein C2orf69 homolog 365 41,689 Chain (1); Frameshift (1); Glycosylation (2); Sequence conflict (2); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q9CQX3 BPIA5_MOUSE BPI fold-containing family A member 5 (BPI fold-containing family A member Pluncl) (Palate lung and nasal carcinoma-like protein) (Short palate lung and nasal clone protein 5) (Tongue plunc-like protein) (TPL) 270 29,175 Chain (1); Disulfide bond (1); Sequence conflict (6); Signal peptide (1) FUNCTION: May play a role in innate immunity in the oral cavity. {ECO:0000269|PubMed:15028288}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Expressed in interpapillar epithelium of the anterior part of the tongue. {ECO:0000269|PubMed:15028288}. +Q7TMB8 CYFP1_MOUSE Cytoplasmic FMR1-interacting protein 1 (Specifically Rac1-associated protein 1) (Sra-1) 1253 145,241 Alternative sequence (1); Chain (1); Erroneous initiation (1); Modified residue (2); Mutagenesis (6); Region (1); Sequence conflict (11) FUNCTION: Component of the CYFIP1-EIF4E-FMR1 complex which binds to the mRNA cap and mediates translational repression. In the CYFIP1-EIF4E-FMR1 complex this subunit is an adapter between EIF4E and FMR1. Promotes the translation repression activity of FMR1 in brain probably by mediating its association with EIF4E and mRNA (By similarity). Regulates formation of membrane ruffles and lamellipodia. Plays a role in axon outgrowth. Binds to F-actin but not to RNA. Part of the WAVE complex that regulates actin filament reorganization via its interaction with the Arp2/3 complex. Actin remodeling activity is regulated by RAC1. Regulator of epithelial morphogenesis. May act as an invasion suppressor in cancers. As component of the WAVE1 complex, required for BDNF-NTRK2 endocytic trafficking and signaling from early endosomes (PubMed:27605705). {ECO:0000250|UniProtKB:Q7L576, ECO:0000269|PubMed:11438699, ECO:0000269|PubMed:14765121, ECO:0000269|PubMed:18805096, ECO:0000269|PubMed:19524508, ECO:0000269|PubMed:27605705}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11438699, ECO:0000269|PubMed:14765121}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:11438699}. Cell projection, lamellipodium {ECO:0000269|PubMed:14765121}. Cell projection, ruffle {ECO:0000269|PubMed:14765121}. Cell junction, synapse, synaptosome {ECO:0000269|PubMed:11438699}. Note=Highly expressed in the perinuclear region (PubMed:11438699). Enriched in synaptosomes (PubMed:11438699). Also enriched in membrane ruffles and at the tips of lamellipodia (PubMed:14765121). {ECO:0000269|PubMed:11438699, ECO:0000269|PubMed:14765121}. SUBUNIT: Component of the WAVE1 complex composed of ABI2, CYFIP1 or CYFIP2, BRK1, NCKAP1 and WASF1/WAVE1. Within the complex, a heterodimer containing NCKAP1 and CYFIP1 interacts with a heterotrimer formed by WAVE1, ABI2 and BRK1. Component of the CYFIP1-EIF4E-FMR1 complex which is composed of CYFIP, EIF4E and FMR1. Interacts with FMR1 but does not bind to related proteins FXR1 or FXR2. Interaction with EIF4E stimulates FMR1 binding. Component of the WAVE2 complex composed of ABI1, CYFIP1/SRA1, NCKAP1/NAP1 (NCKAP1L/HEM1 in hematopoietic cells) and WASF2/WAVE2. Interacts with the active GTP-bound form of RAC1. Interacts through its C-terminus with the C-terminus of DPYSL2/CRMP2 which is necessary for DPYSL2-induced axon outgrowth. Interacts with NYAP1, NYAP2 and MYO16. Interacts with TMEM108 (via N-terminus); the interaction associates TMEM108 with the WAVE1 complex (PubMed:27605705). {ECO:0000250|UniProtKB:Q7L576, ECO:0000269|PubMed:11438699, ECO:0000269|PubMed:18805096, ECO:0000269|PubMed:21946561, ECO:0000269|PubMed:27605705}. TISSUE SPECIFICITY: Highly expressed in embryonic and adult developing nervous system. {ECO:0000269|PubMed:9756361}. +Q99N20 BRMS1_MOUSE Breast cancer metastasis-suppressor 1 homolog 246 28,210 Chain (1); Coiled coil (1); Cross-link (2) FUNCTION: Transcriptional repressor. Down-regulates transcription activation by NF-kappa-B by promoting the deacetylation of RELA at 'Lys-310'. Promotes HDAC1 binding to promoter regions. Down-regulates expression of anti-apoptotic genes that are controlled by NF-kappa-B. Promotes apoptosis in cells that have inadequate adherence to a substrate, a process called anoikis, and may thereby inhibit metastasis (By similarity). {ECO:0000250}. PTM: Ubiquitinated by a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex containing SPOP, leading to proteasomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Predominantly nuclear. {ECO:0000250}. SUBUNIT: Homohexamer (Potential). Interacts with SNX6, HDAC1 and RELA. Interacts with ARID4A. Identified in mSin3A corepressor complexes together with SIN3A, SIN3B, RBBP4, RBBP7, SAP30, SUDS3, ARID4A, HDAC1 and HDAC2. Interacts with SPOP; this recruits the protein to a ubiquitin ligase complex containing SPOP and CUL3 (By similarity). {ECO:0000250, ECO:0000305}. DOMAIN: Contains an N-terminal anti-parallel coiled coil formed by two BRMS1 chains; this region can form homohexamers. {ECO:0000250}. +Q8VIM4 BSND_MOUSE Barttin 307 33,813 Chain (1); Lipidation (2); Modified residue (5); Sequence conflict (3); Topological domain (3); Transmembrane (2) TRANSMEM 6 26 Helical. {ECO:0000255}.; TRANSMEM 33 53 Helical. {ECO:0000255}. TOPO_DOM 1 5 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 27 32 Extracellular. {ECO:0000255}.; TOPO_DOM 54 307 Cytoplasmic. {ECO:0000255}. FUNCTION: Functions as a beta-subunit for CLCNKA and CLCNKB chloride channels. In the kidney CLCNK/BSND heteromers mediate chloride reabsorption by facilitating its basolateral efflux. In the stria, CLCNK/BSND channels drive potassium secretion by recycling chloride for the basolateral SLC12A2 cotransporter. PTM: Palmitoylation is necessary for activation of plasma membrane-inserted CLC-K/barttin channels. {ECO:0000250|UniProtKB:Q8WZ55}. SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000269|PubMed:11734858}; Multi-pass membrane protein {ECO:0000269|PubMed:11734858}. Note=Staining in membranes of the renal tubule is basolateral. Also detected in basolateral membranes of intercalated cells of the collecting duct, which are known to express CLCNKB as well. Both acid-secreting alpha-intercalated cells and base-secreting beta-intercalated cells express this protein basolaterally, but intervening AQP2-expressing principal cells appear devoid of protein expression. In the inner ear, colocalizes with CLCNK in K(+)-secreting marginal cells of the stria vascularis. The basolateral staining contrasts with the apical localization of the KCNQ1 K(+) channel. Also found in K(+)-secreting vestibular dark cells, where it colocalized in basolateral membranes with CLCNK below apical membranes that expressed KCNQ1. SUBUNIT: Interacts with CLCNK channels. Forms probably heteromers with CLCNKA in the thin ascending limb of Henle and with CLCNKB in the thick ascending limb and more distal segments. {ECO:0000269|PubMed:11734858}. TISSUE SPECIFICITY: Expression is evident in inner and outer stripes of the outer medulla of the kidney, most probably representing thin limbs of Henle's loop together with some collecting duct coursing through the outer stripe. In situ hybridization in fetal kidney at 18.5 dpc revealed a clear continuity between hybridization signals from the thin limb of Henle's loop and the distal convoluted tubule, suggesting that part of the expression pattern may result from expression in the thick ascending limb of Henle's loop. In addition, strong signals are present in a subset of cortical tubules, representing distal convoluted tubules or cortical collecting duct. Strong expression is also observed in the inner medulla of the kidney. This expression does not extend all the way to the tip of the papilla. Thus this signal most probably represents cells of the thin ascending limbs. In the inner ear, strong and exclusive expression is detected in marginal cells of the stria vascularis. In addition to cochlear signal, expression is observed in dark cells localized at the base of the crista ampullaris of the vestibular organ. {ECO:0000269|PubMed:11687798, ECO:0000269|PubMed:11734858}. +P48754 BRCA1_MOUSE Breast cancer type 1 susceptibility protein homolog (EC 2.3.2.27) (RING-type E3 ubiquitin transferase BRCA1) 1812 198,795 Chain (1); Compositional bias (1); Cross-link (7); Domain (2); Modified residue (22); Region (1); Sequence conflict (32); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. It is unclear whether it also mediates the formation of other types of polyubiquitin chains. The E3 ubiquitin-protein ligase activity is required for its tumor suppressor function. The BRCA1-BARD1 heterodimer coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability. Regulates centrosomal microtubule nucleation. Required for normal cell cycle progression from G2 to mitosis. Required for appropriate cell cycle arrests after ionizing irradiation in both the S-phase and the G2 phase of the cell cycle. Involved in transcriptional regulation of P21 in response to DNA damage. Required for FANCD2 targeting to sites of DNA damage. May function as a transcriptional regulator. Contributes to homologous recombination repair (HRR) via its direct interaction with PALB2, fine-tunes recombinational repair partly through its modulatory role in the PALB2-dependent loading of BRCA2-RAD51 repair machinery at DNA breaks. Component of the BRCA1-RBBP8 complex which regulates CHEK1 activation and controls cell cycle G2/M checkpoints on DNA damage via BRCA1-mediated ubiquitination of RBBP8. Acts as a transcriptional activator (By similarity). Inhibits lipid synthesis by binding to inactive phosphorylated ACACA and preventing its dephosphorylation. {ECO:0000250|UniProtKB:P38398, ECO:0000269|PubMed:12360400}. PTM: Phosphorylated in response to IR, UV, and various stimuli that cause checkpoint activation, probably by ATM or ATR. Phosphorylation at Ser-971 by CHEK2 regulates mitotic spindle assembly. {ECO:0000250|UniProtKB:P38398}.; PTM: Autoubiquitinated, undergoes 'Lys-6'-linked polyubiquitination. 'Lys-6'-linked polyubiquitination does not promote degradation. {ECO:0000250|UniProtKB:P38398}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P38398}. Chromosome {ECO:0000269|PubMed:22549958, ECO:0000269|PubMed:23039116}. Cytoplasm {ECO:0000250|UniProtKB:P38398}. Note=Localizes at sites of DNA damage at double-strand breaks (DSBs); recruitment to DNA damage sites is mediated by the BRCA1-A complex. Translocated to the cytoplasm during UV-induced apoptosis. {ECO:0000250|UniProtKB:P38398}. SUBUNIT: Heterodimer with BARD1. Part of the BRCA1-associated genome surveillance complex (BASC), which contains BRCA1, MSH2, MSH6, MLH1, ATM, BLM, PMS2 and the MRE11-RAD50-NBN protein (MRN) complex. This association could be a dynamic process changing throughout the cell cycle and within subnuclear domains. Component of the BRCA1-A complex, at least composed of BRCA1, BARD1, UIMC1/RAP80, ABRAXAS1, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1. Interacts (via the BRCT domains) with ABRAXAS1 (phosphorylated form); this is important for recruitment to sites of DNA damage. Can form a heterotetramer with two molecules of ABRAXAS1 (phosphorylated form). Component of the BRCA1-RBBP8 complex. Interacts (via the BRCT domains) with RBBP8 ('Ser-327' phosphorylated form); the interaction ubiquitinates RBBP8, regulates CHEK1 activation, and involves RBBP8 in BRCA1-dependent G2/M checkpoint control on DNA damage. Associates with RNA polymerase II holoenzyme. Interacts with SMC1A, NELFB, DCLRE1C, CLSPN. CHEK1, CHEK2, BAP1, BRCC3, AURKA, UBXN1 and PCLAF. Interacts (via BRCT domains) with BRIP1 (phosphorylated form). Interacts with FANCD2 (ubiquitinated form). Interacts with H2AFX (phosphorylated on 'Ser-140'). Interacts (via the BRCT domains) with ACACA (phosphorylated form); the interaction prevents dephosphorylation of ACACA. Part of a BRCA complex containing BRCA1, BRCA2 and PALB2. Interacts directly with PALB2; the interaction is essential for its function in HRR. Interacts directly with BRCA2; the interaction occurs only in the presence of PALB2 which serves as the bridging protein. Interacts (via the BRCT domains) with LMO4; the interaction represses the transcriptional activity of BRCA1. Interacts (via the BRCT domains) with CCAR2 (via N-terminus); the interaction represses the transcriptional activator activity of BRCA1 (By similarity). Interacts with EXD2 (By similarity). Interacts (via C-terminus) with DHX9; this interaction is direct and links BRCA1 to the RNA polymerase II holoenzyme (By similarity). {ECO:0000250|UniProtKB:P38398, ECO:0000269|PubMed:12360400}. DOMAIN: The BRCT domains recognize and bind phosphorylated pSXXF motif on proteins. The interaction with the phosphorylated pSXXF motif of ABRAXAS1, recruits BRCA1 at DNA damage sites. {ECO:0000250|UniProtKB:P38398}.; DOMAIN: The RING-type zinc finger domain interacts with BAP1. {ECO:0000250|UniProtKB:P38398}. TISSUE SPECIFICITY: In the embryo, expressed in otic vesicles at day 9.5. At day 10.5, this expression decreases and high levels are found in the neuroectoderm. At days 11-12.5, high levels in differentiating keratinocytes and whisker pad primordia. At days 14-17, expression also observed in kidney epithelial cells. In the adult, highest levels found in spleen, thymus, lymph nodes, epithelial organs, and alveolar and ductal epithelial cells of the mammary gland. Very low levels in brain, kidney, and skin. No expression in heart, liver or lung. +P58544 BTBD1_MOUSE BTB/POZ domain-containing protein 1 (Glucose signal-repressing protein) 488 53,233 Chain (1); Compositional bias (1); Domain (2); Erroneous initiation (1); Modified residue (1); Mutagenesis (1); Sequence conflict (2) Protein modification; protein ubiquitination. FUNCTION: Probable substrate-specific adapter of an E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). Seems to regulate expression levels and/or subnuclear distribution of TOP1, via an unknown mechanism (PubMed:15486563, PubMed:17462629). May play a role in mesenchymal differentiation where it promotes myogenic differentiation and suppresses adipogenesis (PubMed:15486563, PubMed:17462629). {ECO:0000250|UniProtKB:Q9H0C5, ECO:0000269|PubMed:15486563, ECO:0000269|PubMed:17462629}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15486563}. Note=Localizes to punctate or elongated cytoplasmic bodies. {ECO:0000250|UniProtKB:Q9H0C5}. SUBUNIT: Interacts (via C-terminus) with TOP1. Interacts with TRIM5 isoform Delta. Interacts with CUL3. {ECO:0000250|UniProtKB:Q9H0C5}. TISSUE SPECIFICITY: Strongly expressed in heart and skeletal muscle. Weakly expressed in myoblast C2C12 cells, but strongly up-regulated upon their differentiation into myotubes. {ECO:0000269|PubMed:15486563}. +Q04211 BTG2_MOUSE Protein BTG2 (BTG family member 2) (NGF-inducible protein TIS21) 158 17,682 Beta strand (4); Chain (1); Helix (5); Modified residue (2); Turn (1) FUNCTION: Anti-proliferative protein; the function is mediated by association with deadenylase subunits of the CCR4-NOT complex. Activates mRNA deadenylation in a CNOT6 and CNOT7-dependent manner. In vitro can inhibit deadenylase activity of CNOT7 and CNOT8. Involved in cell cycle regulation. Could be involved in the growth arrest and differentiation of the neuronal precursors. Modulates transcription regulation mediated by ESR1. Involved in mitochondrial depolarization and neurite outgrowth (By similarity). {ECO:0000250}. PTM: Phosphorylated at Ser-147 by MAPK1/ERK2 and MAPK3/ERK1, and at Ser-149 by MAPK14, leading to PIN1-binding and mitochondrial depolarization. {ECO:0000250}. SUBUNIT: Interacts with PRKCABP. Interacts with CNOT7 and CNOT8; indicative for an association with the CCR4-NOT complex. Interacts with PIN1, inducing mitochondrial depolarization (By similarity). {ECO:0000250}. +Q8CI33 C19L1_MOUSE CWF19-like protein 1 537 60,193 Alternative sequence (1); Chain (1); Sequence caution (1); Sequence conflict (2) +Q80X80 C2C2L_MOUSE Phospholipid transfer protein C2CD2L (C2 domain-containing protein 2-like) (Transmembrane protein 24) 706 76,329 Chain (1); Domain (2); Modified residue (18); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 10 30 Helical. {ECO:0000255}. TOPO_DOM 1 9 Lumenal. {ECO:0000305}.; TOPO_DOM 31 706 Cytoplasmic. {ECO:0000305}. FUNCTION: Lipid-binding protein that transports phosphatidylinositol, the precursor of phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), from its site of synthesis in the endoplasmic reticulum to the cell membrane (By similarity). It thereby maintains the pool of cell membrane phosphoinositides, which are degraded during phospholipase C (PLC) signaling (By similarity). Plays a key role in the coordination of Ca(2+) and phosphoinositide signaling: localizes to sites of contact between the endoplasmic reticulum and the cell membrane, where it tethers the two bilayers (By similarity). In response to elevation of cytosolic Ca(2+), it is phosphorylated at its C-terminus and dissociates from the cell membrane, abolishing phosphatidylinositol transport to the cell membrane (By similarity). Positively regulates insulin secretion in response to glucose (PubMed:24012759). Phosphatidylinositol transfer to the cell membrane allows replenishment of PI(4,5)P2 pools and calcium channel opening, priming a new population of insulin granules (By similarity). {ECO:0000250|UniProtKB:O14523, ECO:0000269|PubMed:24012759}. PTM: Phosphorylation at the C-terminus acidifies the protein and leads to disassociation from the acidic cell membrane. Reassociates with the cell membrane upon dephosphorylation. {ECO:0000250|UniProtKB:O14523}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O14523}; Single-pass membrane protein {ECO:0000250|UniProtKB:O14523}. Cell membrane {ECO:0000250|UniProtKB:O14523}; Peripheral membrane protein {ECO:0000250|UniProtKB:O14523}. Note=Localizes to sites of contact between the endoplasmic reticulum and the cell membrane. Embedded into the endoplamic reticulum membrane via its N-terminal transmembrane domain and associates with cell membrane via its C-terminus. In response to elevation of cytosolic Ca(2+), it is phosphorylated at its C-terminus and dissociates from the cell membrane and localizes to the reticular endoplamic reticulum. Reassociates with cell membrane upon dephosphorylation. {ECO:0000250|UniProtKB:O14523}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O14523}. DOMAIN: The SMP-LBD domain is a lipid transport module, which binds glycerolipids with a preference for phosphatidylinositol (PI). {ECO:0000250|UniProtKB:O14523}. +Q8CIL4 CA131_MOUSE Uncharacterized protein C1orf131 homolog 281 31,344 Chain (1); Compositional bias (1); Modified residue (4); Sequence conflict (4) SUBCELLULAR LOCATION: Chromosome {ECO:0000250|UniProtKB:Q8NDD1}. +Q499E6 CA109_MOUSE Uncharacterized protein C1orf109 homolog 217 24,442 Alternative sequence (2); Chain (1); Sequence conflict (1) PTM: Phosphorylated on serines by CK2 kinase. {ECO:0000250|UniProtKB:Q9NX04}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NX04}. Cytoplasm {ECO:0000250|UniProtKB:Q9NX04}. +Q9JLK4 CABP2_MOUSE Calcium-binding protein 2 (CaBP2) 216 24,223 Alternative sequence (1); Calcium binding (3); Chain (1); Domain (4); Initiator methionine (1); Lipidation (1) FUNCTION: Required for sound encoding at inner hair cells (IHCs) synapses, likely via inhibition of the inactivation of voltage-gated calcium channel of type 1.3 (Cav1.3) in the IHCs (PubMed:28183797). Required for the normal transfer of light signals through the retina (PubMed:27822497). {ECO:0000269|PubMed:27822497, ECO:0000269|PubMed:28183797}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Golgi apparatus {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the inner hair cells (IHCs), outer hair cells,(OHCs) and vestibular hair cells within the ear and in the retina (at protein level) (PubMed:28183797, PubMed:17947313). Expressed in the retinal cone type 6 ON-bipolar cells and type 1 OFF-bipolar cells (at protein level) (PubMed:27822497). Expressed in the organ of Corti and spiral ganglion neurons in the cochlea (at protein level) (PubMed:26809054). {ECO:0000269|PubMed:17947313, ECO:0000269|PubMed:26809054, ECO:0000269|PubMed:27822497, ECO:0000269|PubMed:28183797}. +Q8VHC5 CABP4_MOUSE Calcium-binding protein 4 (CaBP4) 271 30,268 Beta strand (2); Calcium binding (3); Chain (1); Domain (4); Helix (9); Modified residue (1); Mutagenesis (7); Turn (2) FUNCTION: Involved in normal synaptic function through regulation of Ca(2+) influx and neurotransmitter release in photoreceptor synaptic terminals and in auditory transmission. Modulator of CACNA1D and CACNA1F, suppressing the calcium-dependent inactivation and shifting the activation range to more hyperpolarized voltages. {ECO:0000269|PubMed:15452577, ECO:0000269|PubMed:16249514, ECO:0000269|PubMed:17050707, ECO:0000269|PubMed:17947313}. PTM: Phosphorylated. Phosphorylation levels change with the light conditions and regulate the activity, but has no effect on calcium binding. {ECO:0000269|PubMed:18003854}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Found in rod spherules and cone pedicles of the presynapses from both types of photoreceptors. {ECO:0000269|PubMed:15452577}. SUBUNIT: Interacts with CACNA1F and CACNA1D (via IQ domain) in a calcium independent manner. Interacts (via N-terminus) with UNC119. {ECO:0000269|PubMed:15452577, ECO:0000269|PubMed:17050707, ECO:0000269|PubMed:17947313, ECO:0000269|PubMed:18296658}. TISSUE SPECIFICITY: Expressed in retina and in the inner hair cells (IHC) of the cochlea. {ECO:0000269|PubMed:15452577, ECO:0000269|PubMed:16249514, ECO:0000269|PubMed:17050707, ECO:0000269|PubMed:17947313}. +Q9WTP5 CAD22_MOUSE Cadherin-22 (Pituitary and brain cadherin) (PB-cadherin) 813 87,953 Beta strand (15); Chain (1); Domain (5); Glycosylation (3); Helix (1); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (7) TRANSMEM 622 642 Helical. {ECO:0000255}. TOPO_DOM 34 621 Extracellular. {ECO:0000255}.; TOPO_DOM 643 813 Cytoplasmic. {ECO:0000255}. FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. PB-cadherins may have a role in the morphological organization of pituitary gland and brain tissues. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. DOMAIN: Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain. {ECO:0000250}. TISSUE SPECIFICITY: Predominantly expressed in brain. Abundant in olfactory bulb, cerebrum, and cerebellum, less in pons, medulla, and spinal cord. Low expression in heart. No expression in lung, liver, spleen, kidney, testis, stomach, intestine, colon, and placenta. +P09803 CADH1_MOUSE Cadherin-1 (ARC-1) (Epithelial cadherin) (E-cadherin) (Uvomorulin) (CD antigen CD324) [Cleaved into: E-Cad/CTF1; E-Cad/CTF2; E-Cad/CTF3] 884 98,256 Beta strand (48); Chain (4); Compositional bias (1); Domain (5); Glycosylation (11); Helix (6); Metal binding (3); Modified residue (8); Mutagenesis (2); Propeptide (1); Region (2); Sequence conflict (2); Signal peptide (1); Site (3); Topological domain (2); Transmembrane (1); Turn (14) TRANSMEM 710 733 Helical. {ECO:0000255}. TOPO_DOM 157 709 Extracellular. {ECO:0000255}.; TOPO_DOM 734 884 Cytoplasmic. {ECO:0000255}. FUNCTION: Cadherins are calcium-dependent cell adhesion proteins (PubMed:11976333). They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. CDH1 is involved in mechanisms regulating cell-cell adhesions, mobility and proliferation of epithelial cells (PubMed:11976333). Has a potent invasive suppressor role. It is a ligand for integrin alpha-E/beta-7 (By similarity). {ECO:0000250|UniProtKB:P12830, ECO:0000269|PubMed:11976333}.; FUNCTION: E-Cad/CTF2 promotes non-amyloidogenic degradation of Abeta precursors. Has a strong inhibitory effect on APP C99 and C83 production (By similarity). {ECO:0000250|UniProtKB:P12830}.; FUNCTION: (Microbial infection) Does not function as a receptor for L.monocytogenes internalin A (InlA); mutating a single surface-exposed residue confers receptor activity to this protein and promotes uptake of the bacteria. {ECO:0000269|PubMed:10406800}. PTM: O-glycosylated. O-manosylated by TMTC1, TMTC2, TMTC3 or TMTC4. Ser-287 and Thr-511 are O-manosylated by TMTC2 or TMTC4 but not TMTC1 or TMTC3. {ECO:0000269|PubMed:28973932}.; PTM: N-glycosylation at Asn-639 is essential for expression, folding and trafficking. Addition of bisecting N-acetylglucosamine by MGAT3 modulates its cell membrane location (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P12830}.; PTM: Ubiquitinated by a SCF complex containing SKP2, which requires prior phosphorylation by CK1/CSNK1A1. Ubiquitinated by CBLL1/HAKAI, requires prior phosphorylation at Tyr-756 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction {ECO:0000250|UniProtKB:P12830}. Cell membrane; Single-pass type I membrane protein. Endosome {ECO:0000250}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Note=Colocalizes with DLGAP5 at sites of cell-cell contact in intestinal epithelial cells. Anchored to actin microfilaments through association with alpha-, beta- and gamma-catenin. Sequential proteolysis induced by apoptosis or calcium influx, results in translocation from sites of cell-cell contact to the cytoplasm. Colocalizes with RAB11A endosomes during its transport from the Golgi apparatus to the plasma membrane (By similarity). {ECO:0000250}. SUBUNIT: Homodimer; disulfide-linked (By similarity). Component of an E-cadherin/ catenin adhesion complex composed of at least E-cadherin/CDH1, beta-catenin/CTNNB1 or gamma-catenin/JUP, and potentially alpha-catenin/CTNNA1; the complex is located to adherens junctions (PubMed:7982500, PubMed:19759396). Interacts with the TRPV4 and CTNNB1 complex (PubMed:20413591, PubMed:11348595). Interacts with CTNND1 (By similarity). The stable association of CTNNA1 is controversial as CTNNA1 was shown not to bind to F-actin when assembled in the complex (PubMed:16325582). Alternatively, the CTNNA1-containing complex may be linked to F-actin by other proteins such as LIMA1 (PubMed:18093941). Interaction with PSEN1, cleaves CDH1 resulting in the disassociation of cadherin-based adherens junctions (CAJs) (By similarity). Interacts with AJAP1 and DLGAP5 (By similarity). Interacts with TBC1D2 (By similarity). Interacts with LIMA1 (By similarity). Interacts with CAV1 (By similarity). Interacts with PIP5K1C (By similarity). Interacts with RAB8B (By similarity). Interacts with DDR1; this stabilizes CDH1 at the cell surface and inhibits its internalization (By similarity). Interacts with RAPGEF2 (By similarity). Interacts with KLRG1 (By similarity). {ECO:0000250|UniProtKB:P12830, ECO:0000250|UniProtKB:Q9R0T4, ECO:0000269|PubMed:11348595, ECO:0000269|PubMed:16325582, ECO:0000269|PubMed:18093941, ECO:0000269|PubMed:19759396, ECO:0000269|PubMed:20413591, ECO:0000269|PubMed:7982500}. DOMAIN: Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain. TISSUE SPECIFICITY: Non-neural epithelial tissues. +A2A6M5 CACO2_MOUSE Calcium-binding and coiled-coil domain-containing protein 2 (Nuclear domain 10 protein NDP52) (Nuclear domain 10 protein 52) 331 40,136 Alternative sequence (4); Chain (1); Coiled coil (1); Frameshift (1); Motif (2); Region (1) FUNCTION: Xenophagy-specific receptor required for autophagy-mediated intracellular bacteria degradation (By similarity). Acts as an effector protein of galectin-sensed membrane damage that restricts the proliferation of infecting pathogens upon entry into the cytosol by targeting LGALS8-associated bacteria for autophagy (By similarity). Initially orchestrates bacteria targeting to autophagosomes and subsequently ensures pathogen degradation by regulating pathogen-containing autophagosome maturation (By similarity). Bacteria targeting to autophagosomes relies on its interaction with MAP1LC3A, MAP1LC3B and/or GABARAPL2, whereas regulation of pathogen-containing autophagosome maturation requires the interaction with MAP3LC3C (By similarity). May play a role in ruffle formation and actin cytoskeleton organization and seems to negatively regulate constitutive secretion (By similarity). {ECO:0000250|UniProtKB:Q13137}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q13137}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q13137}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:Q13137}; Peripheral membrane protein {ECO:0000305}. SUBUNIT: Dimer. Part of a complex consisting of CALCOCO2, TAX1BP1 and MYO6. Interacts with GEMIN4. Interacts with ATG8 family members MAP1LC3A, MAP1LC3B, GABARAP, GABARAPL1 and GABARAPL2. Interacts with ATG8 family member MAP1LC3C. Interacts with LGALS8. {ECO:0000250|UniProtKB:Q13137}. DOMAIN: The LGALS8-binding domain is essential for the recruitment to cytosol-exposed infecting bacteria. {ECO:0000250|UniProtKB:Q13137}.; DOMAIN: The CLIR (LC3C-interacting region) motif is required for interaction with MAP1LC3C, but dispensable for CALCOCO2-mediated autophagosome maturation. {ECO:0000250|UniProtKB:Q13137}.; DOMAIN: The LIR-like motif is required for interaction with MAP1LC3A, MAP1LC3B and GABARAPL2, as well as for CALCOCO2-mediated autophagosome maturation. {ECO:0000250|UniProtKB:Q13137}. +Q9JIS7 CAC1F_MOUSE Voltage-dependent L-type calcium channel subunit alpha-1F (Voltage-gated calcium channel subunit alpha Cav1.4) 1985 221,926 Calcium binding (1); Chain (1); Compositional bias (5); Glycosylation (1); Region (4); Repeat (4); Site (4); Topological domain (25); Transmembrane (24) TRANSMEM 93 111 Helical; Name=S1 of repeat I. {ECO:0000255}.; TRANSMEM 130 149 Helical; Name=S2 of repeat I. {ECO:0000255}.; TRANSMEM 162 180 Helical; Name=S3 of repeat I. {ECO:0000255}.; TRANSMEM 202 220 Helical; Name=S4 of repeat I. {ECO:0000255}.; TRANSMEM 240 259 Helical; Name=S5 of repeat I. {ECO:0000255}.; TRANSMEM 348 372 Helical; Name=S6 of repeat I. {ECO:0000255}.; TRANSMEM 530 549 Helical; Name=S1 of repeat II. {ECO:0000255}.; TRANSMEM 565 583 Helical; Name=S2 of repeat II. {ECO:0000255}.; TRANSMEM 592 610 Helical; Name=S3 of repeat II. {ECO:0000255}.; TRANSMEM 621 639 Helical; Name=S4 of repeat II. {ECO:0000255}.; TRANSMEM 659 679 Helical; Name=S5 of repeat II. {ECO:0000255}.; TRANSMEM 734 758 Helical; Name=S6 of repeat II. {ECO:0000255}.; TRANSMEM 877 895 Helical; Name=S1 of repeat III. {ECO:0000255}.; TRANSMEM 912 931 Helical; Name=S2 of repeat III. {ECO:0000255}.; TRANSMEM 944 962 Helical; Name=S3 of repeat III. {ECO:0000255}.; TRANSMEM 969 988 Helical; Name=S4 of repeat III. {ECO:0000255}.; TRANSMEM 1008 1027 Helical; Name=S5 of repeat III. {ECO:0000255}.; TRANSMEM 1118 1138 Helical; Name=S6 of repeat III. {ECO:0000255}.; TRANSMEM 1196 1214 Helical; Name=S1 of repeat IV. {ECO:0000255}.; TRANSMEM 1230 1249 Helical; Name=S2 of repeat IV. {ECO:0000255}.; TRANSMEM 1257 1278 Helical; Name=S3 of repeat IV. {ECO:0000255}.; TRANSMEM 1296 1315 Helical; Name=S4 of repeat IV. {ECO:0000255}.; TRANSMEM 1335 1354 Helical; Name=S5 of repeat IV. {ECO:0000255}.; TRANSMEM 1422 1446 Helical; Name=S6 of repeat IV. {ECO:0000255}. TOPO_DOM 1 92 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 112 129 Extracellular. {ECO:0000255}.; TOPO_DOM 150 161 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 181 201 Extracellular. {ECO:0000255}.; TOPO_DOM 221 239 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 260 347 Extracellular. {ECO:0000255}.; TOPO_DOM 373 529 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 550 564 Extracellular. {ECO:0000255}.; TOPO_DOM 584 591 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 611 620 Extracellular. {ECO:0000255}.; TOPO_DOM 640 658 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 680 733 Extracellular. {ECO:0000255}.; TOPO_DOM 759 876 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 896 911 Extracellular. {ECO:0000255}.; TOPO_DOM 932 943 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 963 968 Extracellular. {ECO:0000255}.; TOPO_DOM 989 1007 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1028 1117 Extracellular. {ECO:0000255}.; TOPO_DOM 1139 1195 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1215 1229 Extracellular. {ECO:0000255}.; TOPO_DOM 1250 1256 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1279 1295 Extracellular. {ECO:0000255}.; TOPO_DOM 1316 1334 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1355 1421 Extracellular. {ECO:0000255}.; TOPO_DOM 1447 1982 Cytoplasmic. {ECO:0000255}. FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1F gives rise to L-type calcium currents. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group. They are blocked by dihydropyridines (DHP), phenylalkylamines, and by benzothiazepines (By similarity). Activates at more negative voltages and does not undergo calcium-dependent inactivation (CDI), due to incoming calcium ions, during depolarization. {ECO:0000250|UniProtKB:O60840}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SUBUNIT: Voltage-dependent calcium channels are multisubunit complexes, consisting of alpha-1, alpha-2, beta and delta subunits in a 1:1:1:1 ratio. The channel activity is directed by the pore-forming and voltage-sensitive alpha-1 subunit. In many cases, this subunit is sufficient to generate voltage-sensitive calcium channel activity. The auxiliary subunits beta and alpha-2/delta linked by a disulfide bridge regulate the channel activity (By similarity). Interacts (via IQ domain) with CABP4; in a calcium independent manner. {ECO:0000250, ECO:0000269|PubMed:15452577}. DOMAIN: Each of the four internal repeats contains five hydrophobic transmembrane segments (S1, S2, S3, S5, S6) and one positively charged transmembrane segment (S4). S4 segments probably represent the voltage-sensor and are characterized by a series of positively charged amino acids at every third position. TISSUE SPECIFICITY: Expressed in the inner and outer nuclear layers and the genglion cell layer of the retina. {ECO:0000269|PubMed:10873387}. +Q05A80 CAPR2_MOUSE Caprin-2 (C1q domain-containing protein 1) (Cytoplasmic activation/proliferation-associated protein 2) (RNA granule protein 140) 1031 114,491 Alternative sequence (1); Chain (1); Domain (1); Erroneous initiation (1); Metal binding (2); Modified residue (2); Sequence conflict (1) FUNCTION: Promotes phosphorylation of the Wnt coreceptor LRP6, leading to increased activity of the canonical Wnt signaling pathway (By similarity). Faciliates constitutive LRP6 phosphorylation by CDK14/CCNY during G2/M stage of the cell cycle, which may potentiate cells for Wnt signaling (By similarity). May regulate the transport and translation of mRNAs, modulating for instance the expression of proteins involved in synaptic plasticity in neurons (PubMed:20516077). Involved in regulation of growth as erythroblasts shift from a highly proliferative state towards their terminal phase of differentiation (By similarity). May be involved in apoptosis (By similarity). {ECO:0000250|UniProtKB:Q6IMN6, ECO:0000269|PubMed:20516077}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6IMN6}. Cell membrane; Peripheral membrane protein {ECO:0000250|UniProtKB:Q6IMN6}. SUBUNIT: Homotrimer; via C1q domain. Found in a complex with LRP6, CCNY and CDK14 during G2/M stage; CAPRIN2 functions as a scaffold for the complex by binding to CCNY via its N terminus and to CDK14 via its C terminus. Interacts with LRP5. Interacts with LRP6. {ECO:0000250|UniProtKB:Q6IMN6}. DOMAIN: The C1q domain is essential for the function in Wnt signaling. {ECO:0000250|UniProtKB:Q6IMN6}. TISSUE SPECIFICITY: Specifically expressed in brain (at protein level). {ECO:0000269|PubMed:20516077}. +Q9WVG6 CARM1_MOUSE Histone-arginine methyltransferase CARM1 (EC 2.1.1.319) (Coactivator-associated arginine methyltransferase 1) (Protein arginine N-methyltransferase 4) 608 65,854 Alternative sequence (1); Beta strand (16); Binding site (6); Chain (1); Domain (1); Helix (15); Modified residue (2); Mutagenesis (10); Region (1); Sequence conflict (1); Turn (9) FUNCTION: Methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in several proteins involved in DNA packaging, transcription regulation, pre-mRNA splicing, and mRNA stability. Recruited to promoters upon gene activation together with histone acetyltransferases from EP300/P300 and p160 families, methylates histone H3 at 'Arg-17' (H3R17me), forming mainly asymmetric dimethylarginine (H3R17me2a), leading to activates transcription via chromatin remodeling. During nuclear hormone receptor activation and TCF7L2/TCF4 activation, acts synergically with EP300/P300 and either one of the p160 histone acetyltransferases NCOA1/SRC1, NCOA2/GRIP1 and NCOA3/ACTR or CTNNB1/beta-catenin to activate transcription. During myogenic transcriptional activation, acts together with NCOA3/ACTR as a coactivator for MEF2C. During monocyte inflammatory stimulation, acts together with EP300/P300 as a coactivator for NF-kappa-B. Acts as coactivator for PPARG, promotes adipocyte differentiation and the accumulation of brown fat tissue. Plays a role in the regulation of pre-mRNA alternative splicing by methylation of splicing factors. Also seems to be involved in p53/TP53 transcriptional activation. Methylates EP300/P300, both at 'Arg-2142', which may loosen its interaction with NCOA2/GRIP1, and at 'Arg-580' and 'Arg-604' in the KIX domain, which impairs its interaction with CREB and inhibits CREB-dependent transcriptional activation. Also methylates arginine residues in RNA-binding proteins PABPC1, ELAVL1 and ELAV4, which may affect their mRNA-stabilizing properties and the half-life of their target mRNAs. {ECO:0000269|PubMed:10381882, ECO:0000269|PubMed:11341840, ECO:0000269|PubMed:11701890, ECO:0000269|PubMed:11713257, ECO:0000269|PubMed:11983685, ECO:0000269|PubMed:11997499, ECO:0000269|PubMed:12756295, ECO:0000269|PubMed:14966289, ECO:0000269|PubMed:15186775, ECO:0000269|PubMed:15616592, ECO:0000269|PubMed:16322096, ECO:0000269|PubMed:17218272, ECO:0000269|PubMed:17882261, ECO:0000269|PubMed:18188184, ECO:0000269|PubMed:19843527, ECO:0000269|PubMed:19897492, ECO:0000269|PubMed:21138967}. PTM: Phosphorylation at Ser-217 is strongly increased during mitosis, and decreases rapidly to a very low, basal level after entry into the G1 phase of the cell cycle (By similarity). Phosphorylation at Ser-217 interferes with S-adenosyl-L-methionine binding and strongly reduces methyltransferase activity. Phosphorylation at Ser-217 may promote cytosolic location. {ECO:0000250, ECO:0000269|PubMed:19843527}.; PTM: Auto-methylated on Arg-551. Methylation enhances transcription coactivator activity. Methylation is required for its role in the regulation of pre-mRNA alternative splicing. {ECO:0000269|PubMed:10381882, ECO:0000269|PubMed:11701890, ECO:0000269|PubMed:11747826, ECO:0000269|PubMed:11751582, ECO:0000269|PubMed:11850402, ECO:0000269|PubMed:12237300, ECO:0000269|PubMed:12498683, ECO:0000269|PubMed:12756295, ECO:0000269|PubMed:15339660, ECO:0000269|PubMed:15616592, ECO:0000269|PubMed:21138967}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Mainly nuclear during the G1, S and G2 phases of the cell cycle. Cytoplasmic during mitosis, after breakup of the nuclear membrane (By similarity). {ECO:0000250}. SUBUNIT: Homodimer. Interacts with NR1H4. Interacts with SNRPC (By similarity). Interacts with the C-terminus of NCOA2/GRIP1, NCO3/ACTR and NCOA1/SRC1. Part of a complex consisting of CARM1, EP300/P300 and NCOA2/GRIP1. Interacts with FLII, TP53, myogenic factor MEF2, EP300/P300, TRIM24, CREBBP and CTNNB1. Interacts with RELA. Identified in a complex containing CARM1, TRIM24 and NCOA2/GRIP1. Interacts with NCOA3/SRC3. {ECO:0000250, ECO:0000269|PubMed:10381882, ECO:0000269|PubMed:11701890, ECO:0000269|PubMed:11713257, ECO:0000269|PubMed:11983685, ECO:0000269|PubMed:11997499, ECO:0000269|PubMed:14966289, ECO:0000269|PubMed:15186775, ECO:0000269|PubMed:15616592, ECO:0000269|PubMed:16322096, ECO:0000269|PubMed:17882261, ECO:0000269|PubMed:19843527, ECO:0000269|PubMed:19897492}. TISSUE SPECIFICITY: Ubiquitously expressed. Within the brain, present in proliferating cells from lateral ventricular zone and dentate gyrus (at protein level). {ECO:0000269|PubMed:10381882, ECO:0000269|PubMed:16508003}. +Q8R1Y2 CP045_MOUSE Uncharacterized protein C16orf45 homolog 203 23,465 Chain (1); Domain (1) +A2A5R2 BIG2_MOUSE Brefeldin A-inhibited guanine nucleotide-exchange protein 2 (Brefeldin A-inhibited GEP 2) (ADP-ribosylation factor guanine nucleotide-exchange factor 2) 1792 202,240 Chain (1); Domain (1); Modified residue (19); Region (2) FUNCTION: Promotes guanine-nucleotide exchange on ARF1 and ARF3 and to a lower extent on ARF5 and ARF6. Promotes the activation of ARF1/ARF5/ARF6 through replacement of GDP with GTP. Involved in the regulation of Golgi vesicular transport. Required for the integrity of the endosomal compartment. Involved in trafficking from the trans-Golgi network (TGN) to endosomes and is required for membrane association of the AP-1 complex and GGA1. Seems to be involved in recycling of the transferrin receptor from recycling endosomes to the plasma membrane. Probably is involved in the exit of GABA(A) receptors from the endoplasmic reticulum. Involved in constitutive release of tumor necrosis factor receptor 1 via exosome-like vesicles; the function seems to involve PKA and specifically PRKAR2B. Proposed to act as A kinase-anchoring protein (AKAP) and may mediate crosstalk between Arf and PKA pathways (By similarity). {ECO:0000250}. PTM: In vitro phosphorylated by PKA reducing its GEF activity and dephosphorylated by phosphatase PP1. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}. Golgi apparatus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Endosome {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Cell junction, synapse {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Translocates from cytoplasm to membranes upon cAMP treatment. Localized in recycling endosomes (By similarity). {ECO:0000250}. SUBUNIT: Homodimer. Interacts with ARFGEF1/BIG1; both proteins are probably part of the same or very similar macromolecular complexes. Interacts with PRKAR1A, PRKAR2A, PRKAR1B, PRKAR2B, PPP1CC, PDE3A, TNFRSF1A, MYCBP and EXOC7. Interacts with GABRB1, GABRB2 and GABRB3 (By similarity). {ECO:0000250}. +Q9QYC3 BHA15_MOUSE Class A basic helix-loop-helix protein 15 (bHLHa15) (Class B basic helix-loop-helix protein 8) (bHLHb8) (Muscle, intestine and stomach expression 1) (MIST-1) 197 22,150 Chain (1); Compositional bias (1); Domain (1); Modified residue (2); Sequence conflict (2) FUNCTION: Plays a role in controlling the transcriptional activity of MyoD, ensuring that expanding myoblast populations remain undifferentiated (PubMed:17612490). Repression may occur through muscle-specific E-box occupancy by homodimers. May also negatively regulate bHLH-mediated transcription through an N-terminal repressor domain. Serves as a key regulator of acinar cell function, stability, and identity. Also required for normal organelle localization in exocrine cells and for mitochondrial calcium ion transport. May function as a unique regulator of gene expression in several different embryonic and postnatal cell lineages. Binds to the E-box consensus sequence 5'-CANNTG-3'. {ECO:0000269|PubMed:15003629, ECO:0000269|PubMed:15665001, ECO:0000269|PubMed:17612490, ECO:0000269|PubMed:9482738}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Forms homodimers or heterodimers with TCF3 gene products E12 and E47. These dimers bind to the E-box site, however, heterodimer with MYOD1 does not bind target DNA. DOMAIN: Lacks a classic transcription activation domain and instead possesses an N-terminal region capable of inhibiting heterologous activators. TISSUE SPECIFICITY: Expressed in pancreatic tissue only in acinar cells. There is a complete absence of expression in intra- or interlobular pancreatic ducts and in all islet cells. {ECO:0000269|PubMed:11696558}. +O70337 BIK_MOUSE Bcl-2-interacting killer (Apoptosis inducer NBK) (Bik-like killer protein) 150 16,901 Chain (1); Motif (1); Region (1); Site (1); Transmembrane (1) TRANSMEM 127 147 Helical. {ECO:0000255}. FUNCTION: Accelerates programmed cell death. Binding to the apoptosis repressors Bcl-X(L), BHRF1 or Bcl-2 suppresses this death-promoting activity. {ECO:0000269|PubMed:9525867}. PTM: Proteolytically cleaved by RHBDL4/RHBDD1. RHBDL4/RHBDD1-induced cleavage is a necessary step prior its degradation by the proteosome-dependent mechanism (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Mitochondrion membrane {ECO:0000269|PubMed:9525867}; Single-pass membrane protein {ECO:0000269|PubMed:9525867}. Note=Around the nuclear envelope, and in cytoplasmic membranes. {ECO:0000250}. DOMAIN: Intact BH3 motif is required by BIK, BID, BAK, BAD and BAX for their pro-apoptotic activity and for their interaction with anti-apoptotic members of the Bcl-2 family. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in testis, kidney, liver, lung and heart. {ECO:0000269|PubMed:9525867}. +Q9CY64 BIEA_MOUSE Biliverdin reductase A (BVR A) (EC 1.3.1.24) (Biliverdin-IX alpha-reductase) 295 33,525 Binding site (1); Chain (1); Compositional bias (1); Metal binding (4); Modified residue (6); Nucleotide binding (2); Propeptide (1); Sequence conflict (2) Porphyrin-containing compound metabolism; protoheme degradation. FUNCTION: Reduces the gamma-methene bridge of the open tetrapyrrole, biliverdin IX alpha, to bilirubin with the concomitant oxidation of a NADH or NADPH cofactor. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. +Q9D6W8 BORC6_MOUSE BLOC-1-related complex subunit 6 360 38,011 Chain (1); Compositional bias (1); Modified residue (5); Sequence conflict (2) FUNCTION: As part of the BORC complex may play a role in lysosomes movement and localization at the cell periphery. Associated with the cytosolic face of lysosomes, the BORC complex may recruit ARL8B and couple lysosomes to microtubule plus-end-directed kinesin motor. {ECO:0000250|UniProtKB:Q96GS4}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q96GS4}. SUBUNIT: Component of the BLOC-one-related complex (BORC) which is composed of BLOC1S1, BLOC1S2, BORCS5, BORCS6, BORCS7, BORCS8, KXD1 and SNAPIN. {ECO:0000250|UniProtKB:Q96GS4}. +Q810B3 BSH_MOUSE Brain-specific homeobox protein homolog 232 25,862 Alternative sequence (2); Chain (1); Compositional bias (1); DNA binding (1); Mutagenesis (2) FUNCTION: DNA binding protein that function as transcriptional activator. Is essential for normal postnatal growth and nursing. Is an essential factor for neuronal neuropeptide Y and agouti-related peptide function and locomotory behavior in the control of energy balance. {ECO:0000269|PubMed:17353277, ECO:0000269|PubMed:17485440, ECO:0000269|PubMed:17550780}. SUBCELLULAR LOCATION: Isoform 1: Nucleus {ECO:0000269|PubMed:17353277}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm {ECO:0000269|PubMed:17353277}. TISSUE SPECIFICITY: Expressed in brain. In brain, it is restricted to a few specific developing brain structures such as pineal gland, telencephalic septum, hypothalamic pre-mammillary body and arcuate nucleus. {ECO:0000269|PubMed:14678827}. +Q8CIF4 BTD_MOUSE Biotinidase (Biotinase) (EC 3.5.1.12) 520 58,154 Active site (3); Chain (1); Domain (1); Erroneous initiation (3); Glycosylation (6); Sequence conflict (1); Signal peptide (1) FUNCTION: Catalytic release of biotin from biocytin, the product of biotin-dependent carboxylases degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250}. +Q80Y55 BSDC1_MOUSE BSD domain-containing protein 1 427 46,953 Chain (1); Domain (1); Erroneous initiation (1); Modified residue (6); Sequence conflict (2) +Q3UQU0 BRD9_MOUSE Bromodomain-containing protein 9 596 66,840 Binding site (2); Chain (1); Cross-link (1); Domain (1); Modified residue (4); Region (1); Sequence conflict (1) FUNCTION: Plays a role in chromatin remodeling and regulation of transcription. Acts as a chromatin reader that recognizes and binds acylated histones: binds histones that are acetylated and/or butyrylated. Component of SWI/SNF chromatin remodeling subcomplex GBAF that carries out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. {ECO:0000250|UniProtKB:Q9H8M2}. SUBUNIT: Binds acetylated histones H3 and H4. Binds butyrylated histone H4 (By similarity). Component of the multiprotein chromatin-remodeling subcomplex SWI/SNF called GBAF, which includes at least BICRA or BICRAL (mutually exclusive), BRD9, SS18, the core BAF subunits, SMARCA2/BRM, SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, SMARCC1/BAF155, and SMARCD1/BAF60A (PubMed:29374058). {ECO:0000250|UniProtKB:Q9H8M2, ECO:0000269|PubMed:29374058}. DOMAIN: The Bromo domain mediates interaction with histones that have acetylated lysine residues at specific positions. Also recognizes and binds histones that are butyrylated. {ECO:0000250|UniProtKB:Q9H8M2}. +E9Q173 BTBDG_MOUSE BTB/POZ domain-containing protein 16 522 60,279 Chain (1); Domain (1) +A0A0A6YY25 BTBDI_MOUSE BTB/POZ domain-containing protein 18 723 79,464 Chain (1); Domain (1); Modified residue (3) FUNCTION: Specifically required during spermatogenesis to promote expression of piRNA precursors. The piRNA metabolic process mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons, which is essential for the germline integrity. Acts by facilitating transcription elongation at piRNA loci during pachytene. {ECO:0000269|PubMed:28292424}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28292424}. TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:28292424}. +Q8VC97 BUP1_MOUSE Beta-ureidopropionase (EC 3.5.1.6) (Beta-alanine synthase) (N-carbamoyl-beta-alanine amidohydrolase) 393 43,937 Active site (3); Chain (1); Domain (1); Modified residue (1) Amino-acid biosynthesis; beta-alanine biosynthesis. FUNCTION: Catalyzes a late step in pyrimidine degradation. Converts N-carbamoyl-beta-alanine (3-ureidopropanoate) into beta-alanine, ammonia and carbon dioxide. Likewise, converts N-carbamoyl-beta-aminoisobutyrate (3-ureidoisobutyrate) into beta-aminoisobutyrate, ammonia and carbon dioxide. {ECO:0000250|UniProtKB:Q9UBR1}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homodimer, homotetramer, homooctamer; can also form higher homooligomers. {ECO:0000250|UniProtKB:Q9UBR1}. +Q2VLH6 C163A_MOUSE Scavenger receptor cysteine-rich type 1 protein M130 (CD antigen CD163) [Cleaved into: Soluble CD163 (sCD163)] 1121 120,921 Alternative sequence (1); Chain (2); Disulfide bond (26); Domain (9); Glycosylation (2); Motif (1); Sequence conflict (5); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1046 1066 Helical. {ECO:0000255}. TOPO_DOM 39 1045 Extracellular. {ECO:0000255}.; TOPO_DOM 1067 1121 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in clearance and endocytosis of hemoglobin/haptoglobin complexes by macrophages and may thereby protect tissues from free hemoglobin-mediated oxidative damage. May play a role in the uptake and recycling of iron, via endocytosis of hemoglobin/haptoglobin and subsequent breakdown of heme. Binds hemoglobin/haptoglobin complexes in a calcium-dependent and pH-dependent manner. Induces a cascade of intracellular signals that involves tyrosine kinase-dependent calcium mobilization, inositol triphosphate production and secretion of IL6 and CSF1 (By similarity). {ECO:0000250}.; FUNCTION: After shedding, the soluble form (sCD163) may play an anti-inflammatory role. {ECO:0000250}. PTM: A soluble form (sCD163) is produced by proteolytic shedding which can be induced by lipopolysaccharide, phorbol ester and Fc region of immunoglobulin gamma. This cleavage is dependent on protein kinase C and tyrosine kinases and can be blocked by protease inhibitors. The shedding is inhibited by the tissue inhibitor of metalloproteinase TIMP3, and thus probably induced by membrane-bound metalloproteinases ADAMs (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Soluble CD163: Secreted {ECO:0000250|UniProtKB:Q86VB7}.; SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q86VB7}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q86VB7}. SUBUNIT: Interacts with CSNK2B. {ECO:0000250}. DOMAIN: The SRCR domain 3 mediates calcium-sensitive interaction with hemoglobin/haptoglobin complexes. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in monocytes and mature macrophages such as Kupffer cells in the liver, red pulp macrophages in the spleen and mesenteric lymph nodes. {ECO:0000269|PubMed:11345593}. +Q8CFR0 C1QL2_MOUSE Complement C1q-like protein 2 (C1q and tumor necrosis factor-related protein 10) (C1q/TNF-related protein 10) (C1qTNF10) (CTRP10) 287 29,292 Beta strand (11); Chain (1); Domain (2); Mutagenesis (2); Signal peptide (1); Turn (1) FUNCTION: May regulate the number of excitatory synapses that are formed on hippocampus neurons. Has no effect on inhibitory synapses. {ECO:0000269|PubMed:21262840}. PTM: Glycosylated, but not with N-linked glycans. {ECO:0000269|PubMed:18783346}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18783346}. SUBUNIT: Forms homotrimers which can further assemble to form higher-order oligomeric complexes. Interacts with ADGRB3. May interact with ERFE. Forms heterooligomers with C1QL3 and C1QL4, when proteins are coexpressed; this interaction does not occur after secretion. {ECO:0000269|PubMed:18783346, ECO:0000269|PubMed:21262840, ECO:0000269|PubMed:21378161, ECO:0000269|PubMed:22351773, ECO:0000269|PubMed:23449976}. TISSUE SPECIFICITY: Highest expression in eye, followed by placenta and brain, intermediate expression in adipose tissue and lowest expression in lymph node and testis. {ECO:0000269|PubMed:18783346}. +Q9CQC6 BZW1_MOUSE Basic leucine zipper and W2 domain-containing protein 1 419 48,043 Chain (1); Cross-link (1); Domain (1); Modified residue (4); Sequence conflict (1) FUNCTION: Enhances histone H4 gene transcription but does not seem to bind DNA directly. {ECO:0000250}. TISSUE SPECIFICITY: Broadly expressed, with highest levels in testis. {ECO:0000269|PubMed:16690031}. +Q9WVT6 CAH14_MOUSE Carbonic anhydrase 14 (EC 4.2.1.1) (Carbonate dehydratase XIV) (Carbonic anhydrase XIV) (CA-XIV) 337 37,505 Active site (2); Beta strand (14); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (1); Helix (7); Metal binding (3); Modified residue (1); Region (1); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (4) TRANSMEM 291 311 Helical. {ECO:0000255}. TOPO_DOM 16 290 Extracellular. {ECO:0000255}.; TOPO_DOM 312 337 Cytoplasmic. {ECO:0000255}. FUNCTION: Reversible hydration of carbon dioxide. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Most abundant in the kidney and heart, followed by the skeletal muscle, brain, lung and liver. +O88338 CAD16_MOUSE Cadherin-16 (Kidney-specific cadherin) (Ksp-cadherin) 830 89,860 Chain (1); Domain (6); Glycosylation (3); Modified residue (1); Region (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 789 809 Helical. {ECO:0000255}. TOPO_DOM 22 788 Extracellular. {ECO:0000255}.; TOPO_DOM 810 830 Cytoplasmic. {ECO:0000255}. FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. DOMAIN: Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain. {ECO:0000250}. TISSUE SPECIFICITY: Kidney specific. +Q9QZA0 CAH5B_MOUSE Carbonic anhydrase 5B, mitochondrial (EC 4.2.1.1) (Carbonate dehydratase VB) (Carbonic anhydrase VB) (CA-VB) 317 36,623 Chain (1); Domain (1); Metal binding (3); Region (1); Sequence conflict (2); Transit peptide (1) FUNCTION: Reversible hydration of carbon dioxide. SUBCELLULAR LOCATION: Mitochondrion. +A2AWP0 BIRC7_MOUSE Baculoviral IAP repeat-containing protein 7 (EC 2.3.2.27) (Livin) (RING-type E3 ubiquitin transferase BIRC7) [Cleaved into: Baculoviral IAP repeat-containing protein 7 30 kDa subunit (Truncated livin) (p30-Livin) (tLivin)] 285 31,992 Chain (2); Compositional bias (1); Erroneous initiation (2); Metal binding (4); Repeat (1); Site (1); Zinc finger (1) FUNCTION: Apoptotic regulator capable of exerting proapoptotic and anti-apoptotic activities and plays crucial roles in apoptosis, cell proliferation, and cell cycle control. Its anti-apoptotic activity is mediated through the inhibition of caspase-3, -7, and -9, as well as by its E3 ubiquitin-protein ligase activity. As it is a weak caspase inhibitor, its anti-apoptotic activity is thought to be due to its ability to ubiquitinate DIABLO/SMAC targeting it for degradation thereby promoting cell survival. May contribute to caspase inhibition, by blocking the ability of DIABLO/SMAC to disrupt XIAP/BIRC4-caspase interactions. Protects against apoptosis induced by TNF or by chemical agents such as adriamycin, etoposide or staurosporine. Suppression of apoptosis is mediated by activation of MAPK8/JNK1, and possibly also of MAPK9/JNK2. This activation depends on TAB1 and NR2C2/TAK1. {ECO:0000250|UniProtKB:Q96CA5}. PTM: Autoubiquitinated and undergoes proteasome-mediated degradation. {ECO:0000250|UniProtKB:Q96CA5}.; PTM: The truncated protein (tLivin) not only loses its anti-apoptotic effect but also acquires a pro-apoptotic effect. {ECO:0000250|UniProtKB:Q96CA5}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96CA5}. Cytoplasm {ECO:0000250|UniProtKB:Q96CA5}. Golgi apparatus {ECO:0000250|UniProtKB:Q96CA5}. Note=Nuclear, and in a filamentous pattern throughout the cytoplasm. Full-length livin is detected exclusively cytoplasm, whereas the truncated form (tLivin) is found in the peri-nuclear region with marked localization to the Golgi apparatus; the accumulation of tLivin in the nucleus shows positive correlation with the increase in apoptosis. {ECO:0000250|UniProtKB:Q96CA5}. SUBUNIT: Binds to caspase-9. Interaction with DIABLO/SMAC via the BIR domain disrupts binding to caspase-9 and apoptotic suppressor activity. Interacts with TAB1. In vitro, interacts with caspase-3 and caspase-7 via its BIR domain. {ECO:0000250|UniProtKB:Q96CA5}. DOMAIN: The RING domain is essential for autoubiquitination. {ECO:0000250|UniProtKB:Q96CA5}. +P20029 BIP_MOUSE Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein) 655 72,422 Binding site (1); Chain (1); Cross-link (2); Modified residue (18); Motif (1); Nucleotide binding (4); Region (3); Sequence conflict (7); Signal peptide (1) FUNCTION: Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (PubMed:12411443, PubMed:12475965). Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate (PubMed:12411443). Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR) (By similarity). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to disrupt the dimerization of ERN1/IRE1, thereby inactivating ERN1/IRE1 (By similarity). Accumulation of misfolded protein in the endoplasmic reticulum causes release of HSPA5/BiP from ERN1/IRE1, allowing homodimerization and subsequent activation of ERN1/IRE1 (By similarity). Plays an auxiliary role in post-translational transport of small presecretory proteins across endoplasmic reticulum (ER). May function as an allosteric modulator for SEC61 channel-forming translocon complex, likely cooperating with SEC62 to enable the productive insertion of these precursors into SEC61 channel. Appears to specifically regulate translocation of precursors having inhibitory residues in their mature region that weaken channel gating. {ECO:0000250|UniProtKB:G3I8R9, ECO:0000250|UniProtKB:P11021, ECO:0000269|PubMed:12411443, ECO:0000269|PubMed:12475965}. PTM: In unstressed cells, AMPylation at Thr-519 by FICD inactivates the chaperome activity: AMPylated form is locked in a relatively inert state and only weakly stimulated by J domain-containing proteins. In response to endoplasmic reticulum stress, de-AMPylation by the same protein, FICD, restores the chaperone activity. {ECO:0000250|UniProtKB:G3I8R9}. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138, ECO:0000269|PubMed:21992152}. Cytoplasm {ECO:0000269|PubMed:21992152}. SUBUNIT: Monomer and homooligomer; homooligomerization via the interdomain linker inactivates the chaperone activity and acts as a storage of HSPA5/BiP molecules (By similarity). Interacts with DNAJC1 (via J domain) (PubMed:12065409). Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5 (PubMed:16931514). Part of a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX (PubMed:12475965). Interacts with TMEM132A and TRIM21 (By similarity). May form a complex with ERLEC1, OS9, SEL1L and SYVN1 (By similarity). Interacts with DNAJC10 (PubMed:12411443). Interacts with DNAJB9/ERdj4; leading to recruit HSPA5/BiP to ERN1/IRE1 (PubMed:11836248). Interacts with ERN1/IRE1; interaction takes place following interaction with DNAJB9/ERdj4 and leads to inactivate ERN1/IRE1 (By similarity). Interacts with MX1 (PubMed:21992152). Interacts with METTL23 (By similarity). Interacts with CEMIP; the interaction induces calcium leakage from the endoplasmic reticulum and cell migration (By similarity). Interacts with PCSK4 form; the interaction takes place in the endoplasmic reticulum (By similarity). Interacts with CIPC (By similarity). Interacts with CCDC88B (via C-terminus); the interaction opposes ERN1-mediated JNK activation, protecting against apoptosis (By similarity). Interacts with INPP5K; necessary for INPP5K localization at the endoplasmic reticulum (By similarity). Interacts with MANF; the interaction is direct (By similarity). Interacts with LOXL2; leading to activate the ERN1/IRE1-XBP1 pathway of the unfolded protein response (By similarity). {ECO:0000250|UniProtKB:G3I8R9, ECO:0000250|UniProtKB:P11021, ECO:0000269|PubMed:11836248, ECO:0000269|PubMed:12065409, ECO:0000269|PubMed:12411443, ECO:0000269|PubMed:12475965, ECO:0000269|PubMed:16931514, ECO:0000269|PubMed:21992152}. DOMAIN: The interdomain linker regulates the chaperone activity by mediating the formation of homooligomers. Homooligomers are formed by engagement of the interdomain linker of one HSPA5/BiP molecule as a typical substrate of an adjacent HSPA5/BiP molecule. HSPA5/BiP oligomerization inactivates participating HSPA5/BiP protomers. HSPA5/BiP oligomers probably act as reservoirs to store HSPA5/BiP molecules when they are not needed by the cell. When the levels of unfolded proteins rise, cells can rapidly break up these oligomers to make active monomers. {ECO:0000250|UniProtKB:G3I8R9}. +Q8R016 BLMH_MOUSE Bleomycin hydrolase (BH) (BLM hydrolase) (BMH) (EC 3.4.22.40) 455 52,511 Active site (3); Chain (1); Modified residue (2); Sequence conflict (3) FUNCTION: The normal physiological role of BLM hydrolase is unknown, but it catalyzes the inactivation of the antitumor drug BLM (a glycopeptide) by hydrolyzing the carboxamide bond of its B-aminoalaninamide moiety thus protecting normal and malignant cells from BLM toxicity. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homohexamer. {ECO:0000250}. +Q8CBX9 BIVM_MOUSE Basic immunoglobulin-like variable motif-containing protein 502 56,622 Chain (1); Sequence conflict (3) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. +Q9JIB6 BIR1F_MOUSE Baculoviral IAP repeat-containing protein 1f (Neuronal apoptosis inhibitory protein 6) 1403 159,866 Chain (1); Domain (1); Metal binding (4); Nucleotide binding (1); Repeat (3); Sequence conflict (1) FUNCTION: Sensor component of the NLRC4 inflammasome that specifically recognizes and binds flagellin from pathogenic bacteria. Association of pathogenic bacteria proteins drives in turn drive assembly and activation of the NLRC4 inflammasome, promoting caspase-1 activation, cytokine production and macrophage pyroptosis. The NLRC4 inflammasome is activated as part of the innate immune response to a range of intracellular bacteria (PubMed:21874021). The NLRC4 inflammasome senses Gram-negative bacteria such as L.pneumophila and P.aeruginosa, enteric pathogens S.typhimurium (Salmonella) and S.flexneri. May contribute to prevent motor-neuron apoptosis induced by a variety of signals (By similarity). {ECO:0000250|UniProtKB:Q13075, ECO:0000269|PubMed:21874021}. SUBUNIT: Component of the NLRC4 inflammasome, at least composed of NLRC4, caspase-1 (CASP1) and some NAIP protein. {ECO:0000269|PubMed:21874021}.; SUBUNIT: (Microbial infection) Interacts with S.typhimurium (Salmonella) flagellin. {ECO:0000269|PubMed:21874021}. +Q9JIB3 BIR1G_MOUSE Baculoviral IAP repeat-containing protein 1g (Neuronal apoptosis inhibitory protein 7) 1402 159,664 Binding site (1); Chain (1); Domain (1); Metal binding (4); Repeat (3) FUNCTION: Prevents motor-neuron apoptosis induced by a variety of signals. +P25916 BMI1_MOUSE Polycomb complex protein BMI-1 (Polycomb group RING finger protein 4) 324 36,708 Beta strand (4); Chain (1); Compositional bias (1); Helix (6); Motif (1); Region (2); Turn (3); Zinc finger (1) FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. The complex composed of RNF2, UB2D3 and BMI1 binds nucleosomes, and has activity only with nucleosomal histone H2A. In the PRC1-like complex, regulates the E3 ubiquitin-protein ligase activity of RNF2/RING2 (By similarity). {ECO:0000250|UniProtKB:P35226, ECO:0000269|PubMed:16710298}. PTM: May be polyubiquitinated; which does not lead to proteasomal degradation (By similarity). Monoubiquitinated. {ECO:0000250, ECO:0000269|PubMed:16710298}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P35226}. Cytoplasm {ECO:0000250|UniProtKB:P35226}. SUBUNIT: Component of a PRC1-like complex (PubMed:16359901). Identified in a PRC1-like HPRC-H complex with CBX2, CBX4, CBX8, PHC1, PHC2, PHC3, RING1 and RNF2 (By similarity). Interacts with RNF2/RING2 (PubMed:16359901, PubMed:16710298). Interacts with RING1 (PubMed:16359901, PubMed:16710298). Part of a complex that contains RNF2, UB2D3 and BMI1, where RNF2 and BMI1 form a tight heterodimer, and UB2D3 interacts only with RNF2. The complex composed of RNF2, UB2D3 and BMI1 binds nucleosomes, and has activity only with nucleosomal histone H2A. Interacts with CBX7 and CBX8 (PubMed:16359901). Interacts with SPOP. Part of a complex consisting of BMI1, CUL3 and SPOP. Interacts with E4F1 (By similarity). Interacts with PHC2 (PubMed:16359901). {ECO:0000250|UniProtKB:P35226, ECO:0000269|PubMed:16359901, ECO:0000269|PubMed:16710298}. TISSUE SPECIFICITY: Detected in most organs with high expression levels in thymus, heart, brain and testis. +Q9QUN3 BLNK_MOUSE B-cell linker protein (B-cell adapter containing a SH2 domain protein) (B-cell adapter containing a Src homology 2 domain protein) (Cytoplasmic adapter protein) (Lymphocyte antigen 57) (Src homology 2 domain-containing leukocyte protein of 65 kDa) (Slp-65) 457 50,671 Beta strand (7); Chain (1); Compositional bias (1); Domain (1); Helix (3); Modified residue (5); Mutagenesis (3); Sequence conflict (4); Turn (2) FUNCTION: Functions as a central linker protein, downstream of the B-cell receptor (BCR), bridging the SYK kinase to a multitude of signaling pathways and regulating biological outcomes of B-cell function and development. Plays a role in the activation of ERK/EPHB2, MAP kinase p38 and JNK. Modulates AP1 activation. Important for the activation of NF-kappa-B and NFAT. Plays an important role in BCR-mediated PLCG1 and PLCG2 activation and Ca(2+) mobilization and is required for trafficking of the BCR to late endosomes. However, does not seem to be required for pre-BCR-mediated activation of MAP kinase and phosphatidyl-inositol 3 (PI3) kinase signaling. May be required for the RAC1-JNK pathway. Plays a critical role in orchestrating the pro-B cell to pre-B cell transition. May play an important role in BCR-induced B-cell apoptosis. {ECO:0000269|PubMed:12761551, ECO:0000269|PubMed:18369315, ECO:0000269|PubMed:9705962}. PTM: Following BCR activation, phosphorylated on tyrosine residues by SYK and LYN. When phosphorylated, serves as a scaffold to assemble downstream targets of antigen activation, including PLCG1, VAV1, GRB2 and NCK1. Phosphorylation of Tyr-84, Tyr-178 and Tyr-189 facilitates PLCG1 binding. Phosphorylation of Tyr-72 facilitates VAV1 and NCK1 binding. Phosphorylation is required for both Ca(2+) and MAPK signaling pathways (By similarity). Phosphorylation of Tyr-96 is required for the binding of BTK. {ECO:0000250, ECO:0000269|PubMed:9705962}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=BCR activation results in the translocation to membrane fraction. {ECO:0000250}. SUBUNIT: Associates with PLCG1, VAV1 and NCK1 in a B-cell antigen receptor-dependent fashion. Interacts with VAV3, PLCG2 and GRB2 (By similarity). Interacts through its SH2 domain with CD79A. Interacts (via SH2 domain) with SYK; phosphorylated and activated by SYK. Interacts with SCIMP. {ECO:0000250, ECO:0000269|PubMed:11449366, ECO:0000269|PubMed:11859098, ECO:0000269|PubMed:11909947, ECO:0000269|PubMed:18369315, ECO:0000269|PubMed:21930792, ECO:0000269|PubMed:9705962}. TISSUE SPECIFICITY: Expressed in the spleen and weakly in thymus, no expression was seen in liver, testis, or brain. Expressed in B-cell lines representing different developmental stages from the pre-B to the plasma cell stage, but not in a T-cell or a fibroblast cell line. {ECO:0000269|PubMed:9705962}. +Q6AZB0 BOC_MOUSE Brother of CDO (Protein BOC) 1110 121,331 Alternative sequence (4); Beta strand (15); Chain (1); Disulfide bond (4); Domain (7); Frameshift (1); Glycosylation (8); Helix (1); Natural variant (1); Sequence conflict (9); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 851 871 Helical. {ECO:0000255}. TOPO_DOM 26 850 Extracellular. {ECO:0000255}.; TOPO_DOM 872 1110 Cytoplasmic. {ECO:0000255}. FUNCTION: Component of a cell-surface receptor complex that mediates cell-cell interactions between muscle precursor cells. Promotes differentiation of myogenic cells. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Part of a complex that contains BOC, CDON, NEO1, cadherins and CTNNB1. Interacts with SHH, DHH and IHH. Interacts with NTN3 (By similarity). Interacts with CDH2 and CTNNB1. Interacts with CDH15 only during the early stages of myoblast differentiation. {ECO:0000250, ECO:0000269|PubMed:12634428}. TISSUE SPECIFICITY: Highly expressed in embryonic somites, limb buds, dermomyotomes and in the neural tube. {ECO:0000269|PubMed:11782431}. +Q924Y0 BODG_MOUSE Gamma-butyrobetaine dioxygenase (EC 1.14.11.1) (Gamma-butyrobetaine hydroxylase) (Gamma-BBH) (Gamma-butyrobetaine,2-oxoglutarate dioxygenase) 387 44,699 Chain (1); Metal binding (7); Modified residue (1) Amine and polyamine biosynthesis; carnitine biosynthesis. FUNCTION: Catalyzes the formation of L-carnitine from gamma-butyrobetaine. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +Q8CJ69 BMPER_MOUSE BMP-binding endothelial regulator protein (Bone morphogenetic protein-binding endothelial cell precursor-derived regulator) (Protein crossveinless-2) (mCV2) 685 76,148 Chain (1); Domain (7); Glycosylation (5); Sequence conflict (3); Signal peptide (1) FUNCTION: Inhibitor of bone morphogenetic protein (BMP) function, it may regulate BMP responsiveness of osteoblasts and chondrocytes. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14516682}. SUBUNIT: Interacts with BMP4. {ECO:0000269|PubMed:12897139}. +Q9WTL8 BMAL1_MOUSE Aryl hydrocarbon receptor nuclear translocator-like protein 1 (Arnt3) (Brain and muscle ARNT-like 1) 632 69,452 Alternative sequence (5); Beta strand (11); Chain (1); Cross-link (3); Domain (4); Helix (14); Modified residue (5); Motif (3); Mutagenesis (15); Region (1); Sequence conflict (2); Site (5); Turn (2) FUNCTION: Transcriptional activator which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, ARNTL/BMAL1, ARNTL2/BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and ARNTL/BMAL1 or ARNTL2/BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-ARNTL/BMAL1|ARNTL2/BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress ARNTL/BMAL1 transcription, respectively. ARNTL/BMAL1 positively regulates myogenesis and negatively regulates adipogenesis via the transcriptional control of the genes of the canonical Wnt signaling pathway. Plays a role in normal pancreatic beta-cell function; regulates glucose-stimulated insulin secretion via the regulation of antioxidant genes NFE2L2/NRF2 and its targets SESN2, PRDX3, CCLC and CCLM. Negatively regulates the mTORC1 signaling pathway; regulates the expression of MTOR and DEPTOR. Controls diurnal oscillations of Ly6C inflammatory monocytes; rhythmic recruitment of the PRC2 complex imparts diurnal variation to chemokine expression that is necessary to sustain Ly6C monocyte rhythms. Regulates the expression of HSD3B2, STAR, PTGS2, CYP11A1, CYP19A1 and LHCGR in the ovary and also the genes involved in hair growth. Plays an important role in adult hippocampal neurogenesis by regulating the timely entry of neural stem/progenitor cells (NSPCs) into the cell cycle and the number of cell divisions that take place prior to cell-cycle exit. Regulates the circadian expression of CIART and KLF11. The CLOCK-ARNTL/BMAL1 heterodimer regulates the circadian expression of SERPINE1/PAI1, VWF, B3, CCRN4L/NOC, NAMPT, DBP, MYOD1, PPARGC1A, PPARGC1B, SIRT1, GYS2, F7, NGFR, GNRHR, BHLHE40/DEC1, ATF4, MTA1, KLF10 and also genes implicated in glucose and lipid metabolism. Promotes rhythmic chromatin opening, regulating the DNA accessibility of other transcription factors. May play a role in spermatogenesis; contributes to the chromatoid body assembly and physiology. The NPAS2-ARNTL/BMAL1 heterodimer positively regulates the expression of MAOA, F7 and LDHA and modulates the circadian rhythm of daytime contrast sensitivity by regulating the rhythmic expression of adenylate cyclase type 1 (ADCY1) in the retina. The preferred binding motif for the CLOCK-ARNTL/BMAL1 heterodimer is 5'-CACGTGA-3', which contains a flanking Ala residue in addition to the canonical 6-nucleotide E-box sequence (By similarity). CLOCK specifically binds to the half-site 5'-CAC-3', while ARNTL binds to the half-site 5'-GTGA-3' (By similarity). The CLOCK-ARNTL/BMAL1 heterodimer also recognizes the non-canonical E-box motifs 5'-AACGTGA-3' and 5'-CATGTGA-3' (By similarity). Essential for the rhythmic interaction of CLOCK with ASS1 and plays a critical role in positively regulating CLOCK-mediated acetylation of ASS1 (PubMed:28985504). {ECO:0000250|UniProtKB:O00327, ECO:0000269|PubMed:14672706, ECO:0000269|PubMed:18258755, ECO:0000269|PubMed:18316400, ECO:0000269|PubMed:19141540, ECO:0000269|PubMed:19286518, ECO:0000269|PubMed:19299583, ECO:0000269|PubMed:19605937, ECO:0000269|PubMed:20153195, ECO:0000269|PubMed:20385766, ECO:0000269|PubMed:20430893, ECO:0000269|PubMed:20562852, ECO:0000269|PubMed:20658528, ECO:0000269|PubMed:20840750, ECO:0000269|PubMed:20956306, ECO:0000269|PubMed:21768648, ECO:0000269|PubMed:21966465, ECO:0000269|PubMed:22045262, ECO:0000269|PubMed:22101268, ECO:0000269|PubMed:22611086, ECO:0000269|PubMed:22653727, ECO:0000269|PubMed:22900038, ECO:0000269|PubMed:22981862, ECO:0000269|PubMed:23291174, ECO:0000269|PubMed:23525013, ECO:0000269|PubMed:23547261, ECO:0000269|PubMed:23750248, ECO:0000269|PubMed:23955654, ECO:0000269|PubMed:23970558, ECO:0000269|PubMed:24048828, ECO:0000269|PubMed:24089055, ECO:0000269|PubMed:24268780, ECO:0000269|PubMed:24270424, ECO:0000269|PubMed:24378737, ECO:0000269|PubMed:24385426, ECO:0000269|PubMed:24395244, ECO:0000269|PubMed:24442997, ECO:0000269|PubMed:24481314, ECO:0000269|PubMed:24736997, ECO:0000269|PubMed:28985504}. PTM: Ubiquitinated, leading to its proteasomal degradation (PubMed:16980631, PubMed:18644859, PubMed:23185022). Deubiquitinated by USP9X (PubMed:29626158). {ECO:0000269|PubMed:16980631, ECO:0000269|PubMed:18644859, ECO:0000269|PubMed:23185022, ECO:0000269|PubMed:29626158}.; PTM: O-glycosylated; contains O-GlcNAc. O-glycosylation by OGT prevents protein degradation by inhibiting ubiquitination. It also stabilizes the CLOCK-ARNTL/BMAL1 heterodimer thereby increasing CLOCK-ARNTL/BMAL1-mediated transcription of genes in the negative loop of the circadian clock such as PER1/2/3 and CRY1/2. {ECO:0000269|PubMed:23337503, ECO:0000269|PubMed:23395176}.; PTM: Acetylated on Lys-544 upon dimerization with CLOCK. Acetylation facilitates CRY1-mediated repression. Deacetylated by SIRT1, which may result in decreased protein stability. {ECO:0000269|PubMed:18075593, ECO:0000269|PubMed:18662547}.; PTM: Phosphorylated upon dimerization with CLOCK. Phosphorylation enhances the transcriptional activity, alters the subcellular localization and decreases the stability of the CLOCK-ARNTL/BMAL1 heterodimer by promoting its degradation. Phosphorylation shows circadian variations in the liver with a peak between CT10 to CT14. Phosphorylation at Ser-97 by CK2 is essential for its nuclear localization, its interaction with CLOCK and controls CLOCK nuclear entry. Dephosphorylation at Ser-85 is important for dimerization with CLOCK and transcriptional activity (By similarity). {ECO:0000250|UniProtKB:O00327, ECO:0000269|PubMed:11779462, ECO:0000269|PubMed:12897057, ECO:0000269|PubMed:19330005, ECO:0000269|PubMed:19414601, ECO:0000269|PubMed:19946213, ECO:0000269|PubMed:20049328}.; PTM: Sumoylated on Lys-266 upon dimerization with CLOCK. Predominantly conjugated to poly-SUMO2/3 rather than SUMO1 and the level of these conjugates undergo rhythmic variation, peaking at CT9-CT12. Sumoylation localizes it exclusively to the PML body and promotes its ubiquitination in the PML body, ubiquitin-dependent proteasomal degradation and the transcriptional activity of the CLOCK-ARNTL/BMAL1 heterodimer. {ECO:0000269|PubMed:16109848, ECO:0000269|PubMed:18644859}.; PTM: Undergoes lysosome-mediated degradation in a time-dependent manner in the liver. {ECO:0000269|PubMed:29937374}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16980631, ECO:0000269|PubMed:22208286}. Cytoplasm {ECO:0000269|PubMed:16980631}. Nucleus, PML body {ECO:0000269|PubMed:18644859}. Note=Shuttles between the nucleus and the cytoplasm and this nucleocytoplasmic shuttling is essential for the nuclear accumulation of CLOCK, target gene transcription and the degradation of the CLOCK-ARNTL/BMAL1 heterodimer. The sumoylated form localizes in the PML body. Sequestered to the cytoplasm in the presence of ID2. {ECO:0000269|PubMed:16980631, ECO:0000269|PubMed:18644859, ECO:0000269|PubMed:20861012}. SUBUNIT: Component of the circadian clock oscillator which includes the CRY1/2 proteins, CLOCK or NPAS2, ARNTL/BMAL1 or ARNTL2/BMAL2, CSNK1D and/or CSNK1E, TIMELESS and the PER1/2/3 proteins (PubMed:11779462). Forms a heterodimer with CLOCK (PubMed:9616112, PubMed:16717091, PubMed:16980631, PubMed:18662546, PubMed:19946213, PubMed:19330005, PubMed:21613214, PubMed:23970558, PubMed:22653727). The CLOCK-ARNTL/BMAL1 heterodimer is required for E-box-dependent transactivation, for CLOCK nuclear translocation and degradation, and, for phosphorylation of both CLOCK and ARNTL/BMAL1 (PubMed:11779462). Part of a nuclear complex which also includes RACK1 and PRKCA; RACK1 and PRKCA are recruited to the complex in a circadian manner (PubMed:20093473). Interacts with NPAS2 (PubMed:16628007). Interacts with EZH2 (PubMed:16717091, PubMed:23970558). Interacts with SUMO3 (PubMed:18644859). Interacts with SIRT1 (PubMed:18662546, PubMed:18662547, PubMed:19299583). Interacts with AHR (PubMed:20106950). Interacts with ID1, ID2 and ID3 (PubMed:20861012). Interacts with DDX4 (PubMed:22900038). Interacts with OGT (PubMed:23337503). Interacts with EED and SUZ12 (PubMed:23970558). Interacts with MTA1 (PubMed:24089055). Interacts with CIART (PubMed:24385426, PubMed:24736997). Interacts with HSP90 (By similarity). Interacts with KAT2B and EP300 (By similarity). Interacts with BHLHE40/DEC1 and BHLHE41/DEC2 (PubMed:12397359). Interacts with RELB and the interaction is enhanced in the presence of CLOCK (PubMed:22894897). Interacts with PER1, PER2, CRY1 and CRY2 and this interaction requires a translocation to the nucleus (PubMed:18430226, PubMed:19605937, PubMed:20840750, PubMed:21613214, PubMed:24154698). Interaction of the CLOCK-ARNTL/BMAL1 heterodimer with PER or CRY inhibits transcription activation (PubMed:21613214). Interaction of the CLOCK-ARNTL/BMAL1 with CRY1 is independent of DNA but with PER2 is off DNA (PubMed:21613214). The CLOCK-ARNTL/BMAL1 heterodimer interacts with GSK3B (PubMed:19946213, PubMed:20049328). Interacts with KDM5A (PubMed:21960634). Interacts with KMT2A; in a circadian manner (PubMed:21113167). Interacts with UBE3A (By similarity). Interacts with PRKCG (PubMed:23185022). Interacts with MAGEL2 (PubMed:22208286). Interacts with NCOA2 (PubMed:24529706). Interacts with THRAP3 (PubMed:24043798). The CLOCK-ARNTL/BMAL1 heterodimer interacts with PASD1 (By similarity). Interacts with PASD1 (By similarity). Interacts with USP9X (PubMed:29626158). {ECO:0000250|UniProtKB:O00327, ECO:0000269|PubMed:12397359, ECO:0000269|PubMed:16628007, ECO:0000269|PubMed:16717091, ECO:0000269|PubMed:16980631, ECO:0000269|PubMed:18430226, ECO:0000269|PubMed:18644859, ECO:0000269|PubMed:18662546, ECO:0000269|PubMed:18662547, ECO:0000269|PubMed:19299583, ECO:0000269|PubMed:19330005, ECO:0000269|PubMed:19605937, ECO:0000269|PubMed:19946213, ECO:0000269|PubMed:20049328, ECO:0000269|PubMed:20093473, ECO:0000269|PubMed:20106950, ECO:0000269|PubMed:20840750, ECO:0000269|PubMed:20861012, ECO:0000269|PubMed:21113167, ECO:0000269|PubMed:21613214, ECO:0000269|PubMed:21960634, ECO:0000269|PubMed:22208286, ECO:0000269|PubMed:22653727, ECO:0000269|PubMed:22894897, ECO:0000269|PubMed:22900038, ECO:0000269|PubMed:23185022, ECO:0000269|PubMed:23337503, ECO:0000269|PubMed:23970558, ECO:0000269|PubMed:24043798, ECO:0000269|PubMed:24089055, ECO:0000269|PubMed:24154698, ECO:0000269|PubMed:24385426, ECO:0000269|PubMed:24529706, ECO:0000269|PubMed:24736997, ECO:0000269|PubMed:29626158, ECO:0000269|PubMed:9616112}. TISSUE SPECIFICITY: Expressed in liver and testis (at protein level). Expressed in the suprachiasmatic nucleus (SCN) in a circadian manner (PubMed:29138967). {ECO:0000269|PubMed:16790549, ECO:0000269|PubMed:22900038, ECO:0000269|PubMed:23531614, ECO:0000269|PubMed:24154698, ECO:0000269|PubMed:24603368, ECO:0000269|PubMed:29138967}. +P21274 BMP2_MOUSE Bone morphogenetic protein 2 (BMP-2) (Bone morphogenetic protein 2A) (BMP-2A) 394 44,525 Chain (1); Disulfide bond (4); Glycosylation (4); Modified residue (1); Propeptide (1); Sequence conflict (3); Signal peptide (1) FUNCTION: Induces cartilage and bone formation. Stimulates the differentiation of myoblasts into osteoblasts via the EIF2AK3-EIF2A- ATF4 pathway. BMP2 activation of EIF2AK3 stimulates phosphorylation of EIF2A which leads to increased expression of ATF4 which plays a central role in osteoblast differentiation. In addition stimulates TMEM119, which upregulates the expression of ATF4. {ECO:0000250|UniProtKB:P12643}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Homodimer; disulfide-linked (By similarity). Interacts with SOSTDC1, GREM2, RGMA, RGMB and RGMC. Interacts with ASPN. Interacts with MFAP5. Interacts with FBN1 (via N-terminal domain) and FBN2 (By similarity). {ECO:0000250|UniProtKB:P12643, ECO:0000269|PubMed:14623234, ECO:0000269|PubMed:15039429, ECO:0000269|PubMed:15671031, ECO:0000269|PubMed:15975920, ECO:0000269|PubMed:16604073, ECO:0000269|PubMed:17472960, ECO:0000269|PubMed:17522060, ECO:0000269|PubMed:23963447}. +Q8BHX3 BOREA_MOUSE Borealin (Cell division cycle-associated protein 8) (MESrg) 289 32,214 Alternative sequence (3); Chain (1); Compositional bias (2); Cross-link (1); Modified residue (11); Region (5); Sequence conflict (4) FUNCTION: Component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. In the complex, it may be required to direct the CPC to centromeric DNA. Major effector of the TTK kinase in the control of attachment-error-correction and chromosome alignment (By similarity). {ECO:0000250|UniProtKB:Q53HL2}. PTM: Phosphorylated by TTK, essentially at Thr-94. Phosphorylation (probably by CDK1) promotes targeting of the CPC to centromeric DNA. {ECO:0000250|UniProtKB:Q53HL2}.; PTM: Sumoylated by UBE2I and RANBP2. Desumoylated by SENP3 through the removal of SUMO2 and SUMO3 (By similarity). {ECO:0000250|UniProtKB:Q53HL2}.; PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q53HL2}. Cytoplasm {ECO:0000250|UniProtKB:Q53HL2}. Chromosome, centromere {ECO:0000250|UniProtKB:Q53HL2}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q53HL2}. Note=Localizes on chromosome arms and inner centromeres from prophase through metaphase and then transferring to the spindle midzone and midbody from anaphase through cytokinesis. Colocalizes with SENP3 in the nucleolus in interphase cells. {ECO:0000250|UniProtKB:Q53HL2}. SUBUNIT: May form homooligomers and homodimers. Component of the chromosomal passenger complex (CPC) composed of at least BIRC5/survivin, CDCA8/borealin, INCENP, AURKB or AURKC; in the complex forms a triple-helix bundle-based subcomplex with INCENP and BIRC5 (By similarity). Interacts with SENP3, UBE2I and RANBP2. Interacts (phosphorylated) with SGO1 and SGO2; the association is dependent on CDK1 (By similarity). {ECO:0000250|UniProtKB:Q53HL2}. DOMAIN: The C-terminal region (aa 216-289) represents the dimerization motif. {ECO:0000250}. +Q67E05 BPI_MOUSE Bactericidal permeability-increasing protein (BPI) 483 53,940 Alternative sequence (2); Chain (1); Disulfide bond (1); Glycosylation (2); Region (6); Signal peptide (1) FUNCTION: The cytotoxic action of BPI is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope. {ECO:0000269|PubMed:15590754}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P17213}. Cytoplasmic granule membrane {ECO:0000269|PubMed:15590754}. Note=Membrane-associated in polymorphonuclear Leukocytes (PMN) granules. {ECO:0000269|PubMed:15590754}. SUBUNIT: Monomer. Homodimer; disulfide-linked (By similarity). {ECO:0000250}. DOMAIN: The N-terminal region may be exposed to the interior of the granule, whereas the C-terminal portion may be embedded in the membrane. During phagocytosis and degranulation, proteases may be released and activated and cleave BPI at the junction of the N- and C-terminal portions of the molecule, providing controlled release of the N-terminal antibacterial fragment when bacteria are ingested (By similarity). {ECO:0000250}.; DOMAIN: The N- and C-terminal barrels adopt an identical fold despite having only 13% of conserved residues. {ECO:0000250|UniProtKB:P17213}. TISSUE SPECIFICITY: Expressed in testis, epididymis, and bone marrow, as well as in Sertoli and promyelocytic cell lines. Upon stimulation with different TLR ligands, it is strongly expressed in granulocytes and in bone marrow-derived dendritic cells. {ECO:0000269|PubMed:15590754, ECO:0000269|PubMed:16365446}. +P49003 BMP5_MOUSE Bone morphogenetic protein 5 (BMP-5) 452 51,512 Alternative sequence (1); Chain (1); Disulfide bond (4); Glycosylation (4); Propeptide (1); Signal peptide (1) FUNCTION: Induces cartilage and bone formation. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}. +Q5SQX6 CYFP2_MOUSE Cytoplasmic FMR1-interacting protein 2 (p53-inducible protein 121) 1253 145,659 Chain (1); Erroneous initiation (1); Modified residue (1); Natural variant (1); Sequence conflict (5) FUNCTION: Part of the WAVE1 complex that regulates actin filament reorganization via its interaction with the Arp2/3 complex (By similarity). Involved in T-cell adhesion and p53-dependent induction of apoptosis (By similarity). Does not bind RNA. As component of the WAVE1 complex, required for BDNF-NTRK2 endocytic trafficking and signaling from early endosomes (PubMed:27605705). {ECO:0000250|UniProtKB:Q96F07, ECO:0000269|PubMed:11438699, ECO:0000269|PubMed:27605705}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11438699}. Nucleus {ECO:0000250|UniProtKB:Q96F07}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:11438699}. Cell junction, synapse, synaptosome {ECO:0000269|PubMed:11438699}. Note=Highly expressed in the perinuclear region and enriched in synaptosomes (PubMed:11438699). {ECO:0000269|PubMed:11438699}. SUBUNIT: Component of the WAVE1 complex composed of ABI2, CYFIP1 or CYFIP2, BRK1, NCKAP1 and WASF1/WAVE1. Interacts with FMR1, FXR1 and FXR2 (PubMed:11438699). Interacts with FMR1; the interaction occurs in a RNA-dependent manner (By similarity). Interacts with RAC1 (activated form) which causes the complex to dissociate, releasing activated WASF1 (By similarity). The complex can also be activated by NCK1 (By similarity). Interacts with SHANK3; the interaction mediates the association of SHANK3 with the WAVE1 complex (PubMed:24153177). Interacts with TMEM108 (via N-terminus); the interaction associates TMEM108 with the WAVE1 complex (PubMed:27605705). {ECO:0000250|UniProtKB:Q96F07, ECO:0000269|PubMed:11438699, ECO:0000269|PubMed:24153177, ECO:0000269|PubMed:27605705}. TISSUE SPECIFICITY: Expressed in hippocampus (at protein level). {ECO:0000269|PubMed:24153177}. +Q7JJ13 BRD2_MOUSE Bromodomain-containing protein 2 (Female sterile homeotic-related protein 1) (Fsrg-1) (Protein RING3) 798 88,067 Alternative sequence (1); Chain (1); Compositional bias (7); Domain (3); Erroneous initiation (1); Modified residue (7); Motif (1); Sequence conflict (4) FUNCTION: Binds hyperacetylated chromatin and plays a role in the regulation of transcription, probably by chromatin remodeling. Regulates transcription of the CCND1 gene. Plays a role in nucleosome assembly (By similarity). May play a role in spermatogenesis or folliculogenesis. {ECO:0000250, ECO:0000269|PubMed:9693039, ECO:0000269|PubMed:9811568}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9693039, ECO:0000269|PubMed:9811568}. Note=Detected on chromatin and nucleosomes. {ECO:0000250}. SUBUNIT: Homodimer. Interacts with E2F1 and with histone H4 acetylated at 'Lys-13' (By similarity). {ECO:0000250}. DOMAIN: One bromodomain is sufficient for a partial interaction with histone H4 acetylated at 'Lys-13'. {ECO:0000250}. TISSUE SPECIFICITY: Predominantly expressed in the testis, followed by ovary, placenta, embryo and to a lower extent in somatic tissues. {ECO:0000269|PubMed:9693039, ECO:0000269|PubMed:9811568}. +Q69Z98 BRSK2_MOUSE Serine/threonine-protein kinase BRSK2 (EC 2.7.11.1) (EC 2.7.11.26) (Brain-specific serine/threonine-protein kinase 2) (BR serine/threonine-protein kinase 2) (Serine/threonine-protein kinase SAD-A) 735 81,733 Active site (1); Alternative sequence (4); Beta strand (17); Binding site (1); Chain (1); Compositional bias (1); Domain (2); Helix (19); Modified residue (16); Motif (1); Mutagenesis (2); Nucleotide binding (1); Sequence conflict (1); Turn (4) FUNCTION: Serine/threonine-protein kinase that plays a key role in polarization of neurons and axonogenesis, cell cycle progress and insulin secretion. Phosphorylates CDK16, CDC25C, MAPT/TAU, PAK1 and WEE1. Following phosphorylation and activation by STK11/LKB1, acts as a key regulator of polarization of cortical neurons, probably by mediating phosphorylation of microtubule-associated proteins such as MAPT/TAU at 'Thr-504' and 'Ser-554'. Also regulates neuron polarization by mediating phosphorylation of WEE1 at 'Ser-642' in post-mitotic neurons, leading to down-regulate WEE1 activity in polarized neurons. Plays a role in the regulation of the mitotic cell cycle progress and the onset of mitosis. Plays a role in the regulation of insulin secretion in response to elevated glucose levels, probably via phosphorylation of CDK16 and PAK1. While BRSK2 phosphorylated at Thr-175 can inhibit insulin secretion (PubMed:22798068), BRSK2 phosphorylated at Thr-261 can promote insulin secretion (PubMed:22669945). Regulates reorganization of the actin cytoskeleton. May play a role in the apoptotic response triggered by endoplasmic reticulum (ER) stress. {ECO:0000269|PubMed:15705853, ECO:0000269|PubMed:17482548, ECO:0000269|PubMed:20026642, ECO:0000269|PubMed:22669945, ECO:0000269|PubMed:22798068}. PTM: May be phosphorylated at Thr-261 by PKA (By similarity). Phosphorylated at Thr-175 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. Not phosphorylated at Thr-175 by CaMKK2. In contrast, it is phosphorylated and activated by CaMKK1. May be inactivated via dephosphorylation of Thr-175 by PP2C. {ECO:0000250, ECO:0000269|PubMed:17482548}.; PTM: Polyubiquitinated by the APC complex in conjunction with FZR1, leading to its proteasomal degradation. Targeted for proteasomal degradation by interaction with COPS5. BRSK2 levels change during the cell cycle. BRSK2 levels are low at the G1/S boundary and gradually increase as cells progress into G2 phase. BRSK2 levels decrease rapidly at the end of mitosis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Note=Detected at centrosomes during mitosis. Localizes to the endoplasmic reticulum in response to stress caused by tunicamycin (By similarity). {ECO:0000250}. SUBUNIT: Interacts with FZR1, a regulatory subunit of the APC ubiquitin ligase complex. Interacts with COPS5. Interacts with PAK1 (By similarity). {ECO:0000250}. DOMAIN: The KEN box motif is required for interaction with FZR1/CDH1 and essential for APC(CDH1)-mediated ubiquitination. {ECO:0000250}. TISSUE SPECIFICITY: Detected in pancreas islets and in brain (at protein level). Detected in brain and pancreas. {ECO:0000269|PubMed:22798068}. +Q921C3 BRWD1_MOUSE Bromodomain and WD repeat-containing protein 1 (WD repeat-containing protein 9) 2304 259,228 Alternative sequence (2); Chain (1); Compositional bias (4); Domain (2); Modified residue (28); Repeat (8); Sequence conflict (20) FUNCTION: May be a transcriptional activator. May be involved in chromatin remodeling. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape. {ECO:0000269|PubMed:12889071}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12889071}. Nucleus {ECO:0000269|PubMed:12889071}. SUBUNIT: Interacts with SMARCA4. {ECO:0000269|PubMed:12889071}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:12359327}. +O88665 BRD7_MOUSE Bromodomain-containing protein 7 (75 kDa bromodomain protein) 651 74,000 Chain (1); Coiled coil (1); Compositional bias (1); Cross-link (10); Domain (1); Erroneous initiation (1); Modified residue (8); Motif (1); Sequence conflict (1) FUNCTION: Acts both as coactivator and as corepressor. May play a role in chromatin remodeling. Transcriptional corepressor that down-regulates the expression of target genes. Binds to target promoters, leading to increased histone H3 acetylation at 'Lys-9' (H3K9ac). Binds to the ESR1 promoter. Recruits BRCA1 and POU2F1 to the ESR1 promoter. Coactivator for TP53-mediated activation of transcription of a set of target genes. Required for TP53-mediated cell-cycle arrest in response to oncogene activation. Promotes acetylation of TP53 at 'Lys-382', and thereby promotes efficient recruitment of TP53 to target promoters. Inhibits cell cycle progression from G1 to S phase (By similarity). Activator of the Wnt signaling pathway in a DVL1-dependent manner by negatively regulating the GSK3B phosphotransferase activity. Induces dephosphorylation of GSK3B at 'Tyr-216'. Down-regulates TRIM24-mediated activation of transcriptional activation by AR. {ECO:0000250, ECO:0000269|PubMed:12941796, ECO:0000269|PubMed:18809673, ECO:0000269|PubMed:19909775}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10526152, ECO:0000269|PubMed:19909775}. SUBUNIT: Interacts with IRF2 and HNRPUL1 (By similarity). Interacts (via N-terminus) with TP53. Interacts (via C-terminus) with EP300. Interacts with BRCA1. Interacts (via bromo domain) with histone H3 (via N-terminus) acetylated at 'Lys-14' (H3K14ac). Has low affinity for histone H3 acetylated at 'Lys-9' (H3K9ac). Has the highest affinity for histone H3 that is acetylated both at 'Lys-9' (H3K9ac) and at 'Lys-14' (H3K14ac). Has very low affinity for non-acetylated histone H3. Interacts (via bromo domain) with histone H4 (via N-terminus) acetylated at 'Lys-8' (H3K8ac) (in vitro) (By similarity). Interacts with TRIM24, PTPN13 and DVL1. Identified in a complex with SMARCA4/BRG1, SMARCC1/BAF155, SMARCE1/BAF57, DPF2/BAF45D and ARID2, subunits of the SWI/SNF-B (PBAF) chromatin remodeling complex. {ECO:0000250, ECO:0000269|PubMed:10526152, ECO:0000269|PubMed:12941796, ECO:0000269|PubMed:18809673, ECO:0000269|PubMed:19909775}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10526152}. +B2RRD7 BRPF1_MOUSE Peregrin (Bromodomain and PHD finger-containing protein 1) 1212 137,310 Chain (1); Domain (2); Modified residue (13); Region (3); Zinc finger (4) FUNCTION: Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. Preferentially mediates histone H3-K23 acetylation (PubMed:27939640). Positively regulates the transcription of RUNX1 and RUNX2 (By similarity). {ECO:0000250|UniProtKB:P55201, ECO:0000269|PubMed:27939640}. PTM: Acetylated by KAT6A. {ECO:0000250|UniProtKB:P55201}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P55201}. Cytoplasm {ECO:0000250|UniProtKB:P55201}. Note=Localization to the nucleus depends on KAT6A, ING5 and MEAF6. {ECO:0000250|UniProtKB:P55201}. SUBUNIT: Component of the MOZ/MORF complex composed at least of ING5, KAT6A, KAT6B, MEAF6 and one of BRPF1, BRD1/BRPF2 and BRPF3. Interacts with trimethylated 'Lys-36' of histone H3 (H3K36me3). May interact with KAT7. {ECO:0000250|UniProtKB:P55201}. +P62325 BTG1_MOUSE Protein BTG1 (B-cell translocation gene 1 protein) 171 19,209 Chain (1); Modified residue (1) FUNCTION: Anti-proliferative protein. {ECO:0000250}. SUBUNIT: Interacts with CNOT7 and CNOT8. {ECO:0000250}. +Q499E0 BRNP3_MOUSE BMP/retinoic acid-inducible neural-specific protein 3 766 88,483 Chain (1); Domain (1); Glycosylation (6); Sequence conflict (1); Signal peptide (1) FUNCTION: Inhibits neuronal cell proliferation by negative regulation of the cell cycle transition. Promotes pituitary gonadotrope cell proliferation, migration and invasion, when overexpressed. May play a role in cell pituitary tumor development. {ECO:0000269|PubMed:20025061}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Mitochondrion {ECO:0000269|PubMed:17138656}. TISSUE SPECIFICITY: Expressed in the brain. Weakly expressed in embryonic stem (ES) cells. Expressed in ES-derived neural stem cells (NSCs) and neuronal cells. {ECO:0000269|PubMed:17138656, ECO:0000269|PubMed:20025061}. +P58545 BTBD3_MOUSE BTB/POZ domain-containing protein 3 530 58,802 Chain (1); Compositional bias (1); Domain (2); Sequence conflict (1) FUNCTION: Acts as a key regulator of dendritic field orientation during development of sensory cortex. Also directs dendrites toward active axon terminals when ectopically expressed. {ECO:0000269|PubMed:24179155}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:24179155}. Nucleus {ECO:0000269|PubMed:24179155}. Note=Translocates from the cytosol to the nucleus in response to neuronal activity. TISSUE SPECIFICITY: In the somatosensory cortex, specifically expressed in spiny stellate neurons during barrel formation. Also expressed in the olfactory bulb, piriform cortex and hippocampus. {ECO:0000269|PubMed:24179155}. +O70355 BTNL2_MOUSE Butyrophilin-like protein 2 454 50,894 Alternative sequence (1); Chain (1); Disulfide bond (4); Domain (4); Glycosylation (4); Topological domain (2); Transmembrane (1) TRANSMEM 7 23 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 24 454 Extracellular. {ECO:0000255}. FUNCTION: Negative regulator of T-cell proliferation. {ECO:0000269|PubMed:16751379, ECO:0000269|PubMed:17237401}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in intestine and at reduced levels in lung and stomach. Also expressed in thymus, spleen, lymph nodes, T-cells, B-cells, and macrophages. {ECO:0000269|PubMed:16751379, ECO:0000269|PubMed:17237401}. +Q8BJE2 BTNL9_MOUSE Butyrophilin-like protein 9 536 60,549 Alternative sequence (3); Chain (1); Disulfide bond (2); Domain (3); Erroneous gene model prediction (1); Glycosylation (3); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 258 278 Helical. {ECO:0000255}. TOPO_DOM 36 257 Extracellular. {ECO:0000255}.; TOPO_DOM 279 536 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. +Q8C726 BTBD9_MOUSE BTB/POZ domain-containing protein 9 612 69,148 Chain (1); Domain (2) TISSUE SPECIFICITY: Expressed in the brain (at protein level). {ECO:0000269|PubMed:22658601}. +Q3TMW1 C102A_MOUSE Coiled-coil domain-containing protein 102A 549 62,624 Chain (1); Coiled coil (3); Compositional bias (1); Modified residue (4); Sequence conflict (2) +Q9JJ06 C1GLT_MOUSE Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1 (EC 2.4.1.122) (Core 1 O-glycan T-synthase) (T-syn) (Core 1 UDP-galactose:N-acetylgalactosamine-alpha-R beta 1,3-galactosyltransferase 1) (Core 1 beta1,3-galactosyltransferase 1) (C1GalT1) (Core 1 beta3-Gal-T1) 363 42,304 Chain (1); Modified residue (1); Mutagenesis (1); Sequence conflict (3); Topological domain (2); Transmembrane (1) TRANSMEM 9 29 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 8 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 30 363 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Glycosyltransferase that generates the core 1 O-glycan Gal-beta1-3GalNAc-alpha1-Ser/Thr (T antigen), which is a precursor for many extended O-glycans in glycoproteins. Plays a central role in many processes, such as angiogenesis, thrombopoiesis and kidney homeostasis development. {ECO:0000269|PubMed:14745002, ECO:0000269|PubMed:17062753}. SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. SUBUNIT: Homodimer; disulfide-linked. Interacts with the C1GALT1C1 chaperone; required for galactosyltransferase activity (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Primarily expressed in endothelial, hematopoietic and epithelial cells during development. {ECO:0000269|PubMed:14745002}. +Q91VK1 BZW2_MOUSE Basic leucine zipper and W2 domain-containing protein 2 419 48,063 Chain (1); Domain (1); Modified residue (4); Sequence conflict (2) FUNCTION: May be involved in neuronal differentiation. {ECO:0000250}. +O89103 C1QR1_MOUSE Complement component C1q receptor (C1q/MBL/SPA receptor) (C1qR(p)) (C1qRp) (Cell surface antigen AA4) (Complement component 1 q subcomponent receptor 1) (Lymphocyte antigen 68) (Ly-68) (CD antigen CD93) 644 69,354 Chain (1); Disulfide bond (16); Domain (6); Glycosylation (2); Modified residue (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 573 593 Helical. {ECO:0000255}. TOPO_DOM 23 572 Extracellular. {ECO:0000255}.; TOPO_DOM 594 644 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor (or element of a larger receptor complex) for C1q, mannose-binding lectin (MBL2) and pulmonary surfactant protein A (SPA). May mediate the enhancement of phagocytosis in monocytes and macrophages upon interaction with soluble defense collagens. May play a role in intercellular adhesion. Marker for early multipotent hematopoietic precursor cells. May play a role in cell-cell interactions during hematopoietic and vascular development. PTM: N- and O-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Interacts with C1QBP; the association may represent a cell surface C1q receptor. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in lung, heart and bone marrow. Expressed at lower level in ovary, whole embryo and fetal liver. Not detected in brain, adult liver or thymus. Highly expressed in peritoneal cavity and bone marrow macrophages. Not detected in epithelial cells. +Q6IR41 C1QT6_MOUSE Complement C1q tumor necrosis factor-related protein 6 264 29,081 Chain (1); Domain (2); Glycosylation (1); Sequence conflict (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q4ZJN1 C1QT9_MOUSE Complement C1q and tumor necrosis factor-related protein 9 333 34,566 Alternative sequence (1); Chain (1); Domain (4); Glycosylation (2); Modified residue (13); Mutagenesis (1); Signal peptide (1) FUNCTION: Probable adipokine. Activates AMPK, AKT, and p44/42 MAPK signaling pathways. {ECO:0000269|PubMed:18787108}. PTM: The isomeric forms of the hydroxylated amino acids could not be determined in the mass-spectrometric methods reported in PubMed:18787108 but are assumed on the basis of their occurrence in collagen-like domains. {ECO:0000269|PubMed:18787108}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18787108}. SUBUNIT: Multimers (predominantly trimers). Interacts with ADIPOQ via the C1q domain to form a heterotrimeric complex. {ECO:0000269|PubMed:18787108}. TISSUE SPECIFICITY: Expressed predominantly in adipose tissue. Females express higher levels than males. {ECO:0000269|PubMed:18787108}. +Q99N23 CAH15_MOUSE Carbonic anhydrase 15 (EC 4.2.1.1) (Carbonate dehydratase XV) (Carbonic anhydrase XV) (CA-XV) 324 35,482 Active site (2); Chain (1); Domain (1); Glycosylation (3); Metal binding (3); Region (1); Signal peptide (1) FUNCTION: Reversible hydration of carbon dioxide. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +P28651 CAH8_MOUSE Carbonic anhydrase-related protein (CARP) (Carbonic anhydrase VIII) (CA-VIII) 291 33,081 Active site (1); Chain (1); Compositional bias (1); Domain (1); Metal binding (2); Modified residue (1); Mutagenesis (1); Sequence conflict (3); Site (1) FUNCTION: Does not have a carbonic anhydrase catalytic activity. TISSUE SPECIFICITY: Expressed only in Purkinje cells. +Q8CDE2 CALI_MOUSE Calicin 588 66,750 Chain (1); Domain (2); Modified residue (1); Repeat (6) FUNCTION: Possible morphogenetic cytoskeletal element in spermiogenic differentiation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, perinuclear theca, calyx {ECO:0000250}. Note=Sperm head cytoskeletal structure tightly associated to the nucleus. {ECO:0000250}. +Q8R5M8 CADM1_MOUSE Cell adhesion molecule 1 (Immunoglobulin superfamily member 4) (IgSF4) (Nectin-like protein 2) (NECL-2) (Spermatogenic immunoglobulin superfamily) (SgIgSF) (Synaptic cell adhesion molecule) (SynCAM) (Tumor suppressor in lung cancer 1) (TSLC-1) 456 49,788 Alternative sequence (8); Chain (1); Disulfide bond (3); Domain (3); Frameshift (1); Glycosylation (6); Modified residue (2); Sequence conflict (11); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 389 409 Helical. {ECO:0000255}. TOPO_DOM 48 388 Extracellular. {ECO:0000255}.; TOPO_DOM 410 456 Cytoplasmic. {ECO:0000255}. FUNCTION: Mediates homophilic cell-cell adhesion in a Ca(2+)-independent manner. Also mediates heterophilic cell-cell adhesion with CADM3 and NECTIN3 in a Ca(2+)-independent manner. Acts as a tumor suppressor in non-small-cell lung cancer (NSCLC) cells. Interaction with CRTAM promotes natural killer (NK) cell cytotoxicity and interferon-gamma (IFN-gamma) secretion by CD8+ cells in vitro as well as NK cell-mediated rejection of tumors expressing CADM3 in vivo. May contribute to the less invasive phenotypes of lepidic growth tumor cells. In mast cells, may mediate attachment to and promote communication with nerves. CADM1, together with MITF, is essential for development and survival of mast cells in vivo. Acts as a synaptic cell adhesion molecule and plays a role in the formation of dendritic spines and in synapse assembly. May be involved in neuronal migration, axon growth, pathfinding, and fasciculation on the axons of differentiating neurons. May play diverse roles in the spermatogenesis including in the adhesion of spermatocytes and spermatids to Sertoli cells and for their normal differentiation into mature spermatozoa. {ECO:0000269|PubMed:12202822, ECO:0000269|PubMed:12606335, ECO:0000269|PubMed:12799182, ECO:0000269|PubMed:12826663, ECO:0000269|PubMed:15158462, ECO:0000269|PubMed:15707673, ECO:0000269|PubMed:15811952, ECO:0000269|PubMed:16605125, ECO:0000269|PubMed:16612000, ECO:0000269|PubMed:23209303}. PTM: N-glycosylated. {ECO:0000269|PubMed:12606335, ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:19656770, ECO:0000269|PubMed:20739279}.; PTM: Glycosylation at Asn-70 and Asn-104 promotes adhesive binding and synapse induction. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12826663, ECO:0000269|PubMed:20739279}; Single-pass type I membrane protein {ECO:0000269|PubMed:12826663, ECO:0000269|PubMed:20739279}. Cell junction, synapse {ECO:0000269|PubMed:20739279, ECO:0000269|PubMed:23209303}. Note=Localized to the basolateral plasma membrane of epithelial cells in gall bladder. {ECO:0000269|PubMed:12826663}. SUBUNIT: Homodimer. Interacts with CRTAM. Interacts (via C-terminus) with EPB41L3/DAL1. The interaction with EPB41L3/DAL1 may act to anchor CADM1 to the actin cytoskeleton. Interacts via its C-terminus with the PDZ domain of MPP2, MPP3 and MPP6. Interacts with FARP1. {ECO:0000250|UniProtKB:Q6AYP5, ECO:0000269|PubMed:12826663, ECO:0000269|PubMed:15781451, ECO:0000269|PubMed:15811952, ECO:0000269|PubMed:23209303}. DOMAIN: The cytoplasmic domain appears to play a critical role in proapoptosis and tumor suppressor activity in NSCLC. {ECO:0000250|UniProtKB:Q9BY67}. TISSUE SPECIFICITY: Expressed in brain, lung, kidney, testis, heart, spleen and liver, but not expressed in skeletal muscle. In brain, enriched in the synaptic plasma membrane. Expressed dominantly in epithelial cells but not expressed in fibroblast cells (at protein level). {ECO:0000269|PubMed:12202822, ECO:0000269|PubMed:12242005, ECO:0000269|PubMed:12606335, ECO:0000269|PubMed:12826663}. +Q6DFY8 BRNP2_MOUSE BMP/retinoic acid-inducible neural-specific protein 2 783 89,228 Chain (1); Domain (1); Erroneous initiation (1); Glycosylation (6); Sequence conflict (2); Signal peptide (1) FUNCTION: Inhibits neuronal cell proliferation by negative regulation of the cell cycle transition. {ECO:0000269|PubMed:20025061}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Weakly expressed in embryonic stem (ES) cells. Strongly expressed in ES-derived neural stem cells (NSCs). {ECO:0000269|PubMed:20025061}. +Q80YW5 BSPRY_MOUSE B box and SPRY domain-containing protein 473 52,751 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (1); Sequence conflict (3); Zinc finger (1) FUNCTION: May regulate epithelial calcium transport by inhibiting TRPV5 activity. {ECO:0000269|PubMed:16380433}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16380433}. Membrane {ECO:0000269|PubMed:16380433}; Peripheral membrane protein {ECO:0000269|PubMed:16380433}. Note=Apical domain of kidney distal tubular cells. SUBUNIT: Interacts with YWHAZ/14-3-3 protein zeta (By similarity). Interacts with TRPV5 and TRPV6. {ECO:0000250, ECO:0000269|PubMed:16380433}. TISSUE SPECIFICITY: According to PubMed:10978534, testis-specific. According to PubMed:16371431, broadly expressed. {ECO:0000269|PubMed:10978534, ECO:0000269|PubMed:16380433}. +Q05928 BTC_MOUSE Probetacellulin [Cleaved into: Betacellulin (BTC)] 177 19,664 Chain (2); Compositional bias (1); Disulfide bond (3); Domain (1); Glycosylation (3); Propeptide (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 119 139 Helical. {ECO:0000255}. TOPO_DOM 32 118 Extracellular. {ECO:0000255}.; TOPO_DOM 140 177 Cytoplasmic. {ECO:0000255}. FUNCTION: Growth factor that binds to EGFR, ERBB4 and other EGF receptor family members. Potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. {ECO:0000269|PubMed:21897861}. SUBCELLULAR LOCATION: Betacellulin: Secreted, extracellular space.; SUBCELLULAR LOCATION: Probetacellulin: Cell membrane; Single-pass type I membrane protein. SUBUNIT: Monomer. Interacts with EGFR and ERBB4. TISSUE SPECIFICITY: Found in several mouse tissues including kidney, uterus and liver, as well as in beta tumor cell line and MCF-7 cells. It is not detected in the brain. +O35473 C1D_MOUSE Nuclear nucleic acid-binding protein C1D (mC1D) (Small unique nuclear receptor corepressor) (Sun-CoR) (SunCoR) 141 15,945 Chain (1); Cross-link (3); Region (3); Sequence conflict (2) FUNCTION: Plays a role in the recruitment of the RNA exosome complex to pre-rRNA to mediate the 3'-5' end processing of the 5.8S rRNA; this function may include MPHOSPH6. Can activate PRKDC not only in the presence of linear DNA but also in the presence of supercoiled DNA. Can induce apoptosis in a p53/TP53 dependent manner. May regulate the TRAX/TSN complex formation. Potentiates transcriptional repression by NR1D1 and THRB (By similarity). {ECO:0000250, ECO:0000269|PubMed:10362552, ECO:0000269|PubMed:9405624}. PTM: Phosphorylated by PRKDC. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9405624}. Cytoplasm {ECO:0000250|UniProtKB:Q13901}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q13901}. Note=EXOSC10 is required for nucleolar localization. Colocalizes with TSNAX in the nucleus. {ECO:0000250|UniProtKB:Q13901}. SUBUNIT: Monomer and homodimer. Interacts with EXOSC10; the interaction probably mediates the association with the nuclear form of the RNA exosome. The homodimeric form interacts with TSNAX following gamma-radiation. Interacts with RAC3 (By similarity). Interacts with NR1D1, THRA, THRB, NCOR1 and NCOR2. {ECO:0000250, ECO:0000269|PubMed:9405624, ECO:0000269|PubMed:9469821}. TISSUE SPECIFICITY: Kidney, heart, brain, spleen, lung, testis, liver and small intestine. {ECO:0000269|PubMed:9405624}. +O09047 C3AR_MOUSE C3a anaphylatoxin chemotactic receptor (C3AR) (C3a-R) (Complement component 3a receptor 1) 477 53,576 Chain (1); Disulfide bond (1); Glycosylation (4); Modified residue (5); Sequence conflict (7); Topological domain (8); Transmembrane (7) TRANSMEM 24 46 Helical; Name=1. {ECO:0000255}.; TRANSMEM 58 80 Helical; Name=2. {ECO:0000255}.; TRANSMEM 97 118 Helical; Name=3. {ECO:0000255}.; TRANSMEM 140 160 Helical; Name=4. {ECO:0000255}.; TRANSMEM 334 353 Helical; Name=5. {ECO:0000255}.; TRANSMEM 371 393 Helical; Name=6. {ECO:0000255}.; TRANSMEM 411 431 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 23 Extracellular. {ECO:0000255}.; TOPO_DOM 47 57 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 81 96 Extracellular. {ECO:0000255}.; TOPO_DOM 119 139 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 161 333 Extracellular. {ECO:0000255}.; TOPO_DOM 354 370 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 394 410 Extracellular. {ECO:0000255}.; TOPO_DOM 432 477 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for the chemotactic and inflammatory peptide anaphylatoxin C3a. This receptor stimulates chemotaxis, granule enzyme release and superoxide anion production. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Detected in varying levels in all tissues examined except the spleen. Especially abundant in heart and lung. +Q9CZB0 C560_MOUSE Succinate dehydrogenase cytochrome b560 subunit, mitochondrial (Integral membrane protein CII-3) (QPs-1) (QPs1) 169 18,382 Chain (1); Metal binding (1); Sequence conflict (4); Topological domain (4); Transit peptide (1); Transmembrane (3) TRANSMEM 63 92 Helical. {ECO:0000250}.; TRANSMEM 113 137 Helical. {ECO:0000250}.; TRANSMEM 145 166 Helical. {ECO:0000250}. TOPO_DOM 30 62 Mitochondrial matrix. {ECO:0000250}.; TOPO_DOM 93 112 Mitochondrial intermembrane. {ECO:0000250}.; TOPO_DOM 138 144 Mitochondrial matrix. {ECO:0000250}.; TOPO_DOM 167 169 Mitochondrial intermembrane. {ECO:0000250}. Carbohydrate metabolism; tricarboxylic acid cycle. FUNCTION: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Component of complex II composed of four subunits: the flavoprotein (FP) SDHA, iron-sulfur protein (IP) SDHB, and a cytochrome b560 composed of SDHC and SDHD. {ECO:0000250}. +P79621 C2TA_MOUSE MHC class II transactivator (CIITA) (EC 2.3.1.-) (EC 2.7.11.1) 1155 127,528 Alternative sequence (3); Chain (1); Compositional bias (1); Domain (1); Nucleotide binding (1); Region (1); Repeat (4); Sequence conflict (1) FUNCTION: Essential for transcriptional activity of the HLA class II promoter; activation is via the proximal promoter. No DNA binding of in vitro translated CIITA was detected. May act in a coactivator-like fashion through protein-protein interactions by contacting factors binding to the proximal MHC class II promoter, to elements of the transcription machinery, or both. Alternatively it may activate HLA class II transcription by modifying proteins that bind to the MHC class II promoter. Also mediates enhanced MHC class I transcription, the promoter element requirements for CIITA-mediated transcription are distinct from those of constitutive MHC class I transcription, and CIITA can functionally replace TAF1 at these genes. Exhibits intrinsic GTP-stimulated acetyltransferase activity. Exhibits serine/threonine protein kinase activity: phosphorylates the TFIID component TAF7, the RAP74 subunit of the general transcription factor TFIIF, histone H2B at 'Ser-37' and other histones (By similarity). {ECO:0000250}. PTM: Autophosphorylated, affecting interaction with TAF7. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Nucleus, PML body {ECO:0000250}. Note=Recruited to PML body by PML. {ECO:0000250}. SUBUNIT: Interacts with ZXDB and ZXDC. Interacts with PML. {ECO:0000250}. DOMAIN: The acetyltransferase domain is necessary for activation of both class I and class II transcription. {ECO:0000250}.; DOMAIN: The GTP-binding motif doesn't confer GTPase activity but promotes nuclear localization. {ECO:0000250}. TISSUE SPECIFICITY: Isoform 1 is expressed at very high levels in dendritic cells, at very low levels in spleen and thymus and is not detected in other tissues. Isoform 2 is detected at high levels in spleen and tonsil as well as in a number of B-lymphocyte cell lines, and at very low levels in dendritic cells. {ECO:0000269|PubMed:9184229}. +Q9WUF3 C8AP2_MOUSE CASP8-associated protein 2 (FLICE-associated huge protein) 1962 219,091 Chain (1); Initiator methionine (1); Modified residue (7); Motif (1); Region (1); Sequence conflict (3) FUNCTION: Participates in TNF-alpha-induced blockade of glucocorticoid receptor (GR) transactivation at the nuclear receptor coactivator level, upstream and independently of NF-kappa-B. Suppresses both NCOA2- and NCOA3-induced enhancement of GR transactivation (By similarity). Required for histone gene transcription and progression through S phase (By similarity). Required for histone gene transcription and S phase progression (By similarity). Involved in TNF-alpha-induced activation of NF-kappa-B via a TRAF2-dependent pathway. Acts as a downstream mediator for CASP8-induced activation of NF-kappa-B. Required for the activation of CASP8 in FAS-mediated apoptosis. {ECO:0000250, ECO:0000269|PubMed:11340079, ECO:0000269|PubMed:15592525}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000269|PubMed:17003125}. Nucleus, PML body {ECO:0000250}. Mitochondrion {ECO:0000250}. Note=Exported from the nucleus to the mitochondria upon FAS activation. {ECO:0000250}. SUBUNIT: Self-associates. Interacts with NPAT (By similarity). Interacts with SRRT (By similarity). Interacts (via SIM domains) with SUMO1 and SUMO2 (By similarity). Interacts with SP100; may negatively regulate CASP8AP2 export from the nucleus to the cytoplasm (By similarity). Interacts with NCOA2 and NCOA3 (By similarity). Component of the death-inducing signaling complex (DISC) with CASP8, FADD and FAS. Interacts with TRAF2. {ECO:0000250, ECO:0000269|PubMed:10235259, ECO:0000269|PubMed:11340079, ECO:0000269|PubMed:17245429}. TISSUE SPECIFICITY: Highly expressed in heart, brain, thymus, lung, testis and spleen. {ECO:0000269|PubMed:10235259}. +Q9DAD0 CA194_MOUSE Uncharacterized protein C1orf194 homolog 168 18,931 Chain (1) +Q9D5Q8 CA141_MOUSE Uncharacterized protein C1orf141 homolog 446 51,672 Alternative sequence (3); Chain (1); Sequence conflict (6) +Q3KQP7 CA146_MOUSE Uncharacterized protein C1orf146 homolog 184 20,929 Alternative sequence (2); Chain (1); Erroneous initiation (2); Frameshift (1) +Q9CQM1 CA210_MOUSE Type III endosome membrane protein TEMP (TEMP) 111 11,532 Chain (1); Glycosylation (1); Topological domain (2); Transmembrane (1) TRANSMEM 28 48 Helical; Signal-anchor for type III membrane protein. {ECO:0000255}. TOPO_DOM 1 27 Extracellular. {ECO:0000303|PubMed:24710541}.; TOPO_DOM 49 111 Cytoplasmic. {ECO:0000255}. FUNCTION: May be involved in membrane trafficking between endosomes and plasma membrane. {ECO:0000303|PubMed:24710541}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type III membrane protein {ECO:0000305}. Early endosome {ECO:0000269|PubMed:24710541}. Recycling endosome {ECO:0000269|PubMed:24710541}. Cell membrane {ECO:0000303|PubMed:24710541}. Note=Also localizes to tubular endosome structures. {ECO:0000269|PubMed:24710541}. TISSUE SPECIFICITY: Expressed in stomach, kidney, large and small intestine and kidney. {ECO:0000269|PubMed:24710541}. +P97326 CADH6_MOUSE Cadherin-6 (Kidney cadherin) (K-cadherin) 790 88,355 Beta strand (17); Chain (1); Domain (5); Glycosylation (5); Helix (1); Modified residue (2); Propeptide (1); Sequence conflict (13); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (8) TRANSMEM 616 636 Helical. {ECO:0000255}. TOPO_DOM 54 615 Extracellular. {ECO:0000255}.; TOPO_DOM 637 790 Cytoplasmic. {ECO:0000255}. FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. DOMAIN: Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain. {ECO:0000250}. +Q9Z0M3 CAD20_MOUSE Cadherin-20 (Cadherin-7) 801 88,998 Chain (1); Domain (5); Glycosylation (4); Propeptide (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 620 640 Helical. {ECO:0000255}. TOPO_DOM 60 619 Extracellular. {ECO:0000255}.; TOPO_DOM 641 801 Cytoplasmic. {ECO:0000255}. FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. DOMAIN: Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain. Highest level of expression in the retina. In embryo it is synthesized by the forebrain, anterior neural ridge, developing visual system, primitive external granular layer of the cerebellum and a subset of neural crest cells likely to develop into melanoblasts. {ECO:0000269|PubMed:10433813, ECO:0000269|PubMed:15273735}. +Q8C633 CABS1_MOUSE Calcium-binding and spermatid-specific protein 1 391 42,302 Chain (1); Modified residue (7); Sequence conflict (2) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Mitochondrion {ECO:0000250}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:19208547}. Note=Detected in mitochondria of step 17 to 18 spermatids. Associated with the mitochondrial inner membrane in step 18 spermatids (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Detected only in testis. Expressed from stages X to VIII of the seminiferous epithelial cycle. Expressed from step 13 to step 16 of spermatid development (at protein level). {ECO:0000269|PubMed:19208547}. +Q9D424 CABYR_MOUSE Calcium-binding tyrosine phosphorylation-regulated protein (Calcium-binding protein 86) (Testis-specific calcium-binding protein CBP86) 453 48,333 Alternative sequence (4); Chain (1); Domain (1); Sequence conflict (2) FUNCTION: May function as a regulator of both motility- and head-associated functions such as capacitation and the acrosome reaction. May bind calcium in vitro (By similarity). {ECO:0000250}. PTM: Phosphorylated on tyrosine residues during in vitro capacitation. Dephosphorylation affects its ability to bind calcium (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12801634}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12801634}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:12801634}. Note=Localizes to fibrous sheath including the surface of the longitudinal columns and ribs of the principal piece of sperm flagella. SUBUNIT: Interacts with FSCB. {ECO:0000269|PubMed:17855365}. TISSUE SPECIFICITY: Expressed in spermatozoa. {ECO:0000269|PubMed:12801634}. +Q9D0N7 CAF1B_MOUSE Chromatin assembly factor 1 subunit B (CAF-1 subunit B) (Chromatin assembly factor I p60 subunit) (CAF-I 60 kDa subunit) (CAF-I p60) 572 63,132 Chain (1); Modified residue (10); Repeat (7) FUNCTION: Complex that is thought to mediate chromatin assembly in DNA replication and DNA repair. Assembles histone octamers onto replicating DNA in vitro. CAF-1 performs the first step of the nucleosome assembly process, bringing newly synthesized histones H3 and H4 to replicating DNA; histones H2A/H2B can bind to this chromatin precursor subsequent to DNA replication to complete the histone octamer (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=DNA replication foci. {ECO:0000250}. SUBUNIT: Subunit of the CAF-1 complex that contains RBBP4, CHAF1B and CHAF1A. CHAF1A binds directly to CHAF1B (By similarity). {ECO:0000250}. +P70408 CAD10_MOUSE Cadherin-10 (T2-cadherin) 788 88,312 Beta strand (16); Chain (1); Domain (5); Glycosylation (3); Modified residue (1); Propeptide (1); Sequence conflict (10); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (8) TRANSMEM 614 634 Helical. {ECO:0000255}. TOPO_DOM 23 613 Extracellular. {ECO:0000255}.; TOPO_DOM 635 788 Cytoplasmic. {ECO:0000255}. FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. DOMAIN: Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain. {ECO:0000250}. +O70354 CAH11_MOUSE Carbonic anhydrase-related protein 11 (CA-RP XI) (CA-XI) (CARP XI) (Carbonic anhydrase-related protein 2) (CA-RP II) (CARP-2) 328 36,051 Chain (1); Domain (1); Glycosylation (1); Signal peptide (1) FUNCTION: Does not have a catalytic activity. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +P16015 CAH3_MOUSE Carbonic anhydrase 3 (EC 4.2.1.1) (Carbonate dehydratase III) (Carbonic anhydrase III) (CA-III) 260 29,366 Active site (1); Chain (1); Domain (1); Initiator methionine (1); Metal binding (3); Modified residue (14); Region (2); Sequence conflict (4) FUNCTION: Reversible hydration of carbon dioxide. PTM: S-glutathionylated in hepatocytes under oxidative stress. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. TISSUE SPECIFICITY: Expressed at lower levels in adipose tissue from animals that were either genetically obese or had experimentally induced obesity. {ECO:0000269|PubMed:1922100}. +P10287 CADH3_MOUSE Cadherin-3 (Placental cadherin) (P-cadherin) 822 90,612 Beta strand (17); Chain (1); Compositional bias (1); Domain (5); Glycosylation (2); Helix (2); Propeptide (1); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (5) TRANSMEM 648 670 Helical. {ECO:0000255}. TOPO_DOM 100 647 Extracellular. {ECO:0000255}.; TOPO_DOM 671 822 Cytoplasmic. {ECO:0000255}. FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SUBUNIT: Interacts with CDCP1 and CTNNB1. {ECO:0000250}. DOMAIN: Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain. {ECO:0000250}. +O88427 CAC1H_MOUSE Voltage-dependent T-type calcium channel subunit alpha-1H (Voltage-gated calcium channel subunit alpha Cav3.2) 2365 262,030 Alternative sequence (1); Chain (1); Compositional bias (2); Glycosylation (3); Metal binding (3); Repeat (4); Sequence conflict (23); Site (4); Topological domain (25); Transmembrane (24) TRANSMEM 101 119 Helical; Name=S1 of repeat I. {ECO:0000255}.; TRANSMEM 142 160 Helical; Name=S2 of repeat I. {ECO:0000255}.; TRANSMEM 170 184 Helical; Name=S3 of repeat I. {ECO:0000255}.; TRANSMEM 194 212 Helical; Name=S4 of repeat I. {ECO:0000255}.; TRANSMEM 233 253 Helical; Name=S5 of repeat I. {ECO:0000255}.; TRANSMEM 395 419 Helical; Name=S6 of repeat I. {ECO:0000255}.; TRANSMEM 791 811 Helical; Name=S1 of repeat II. {ECO:0000255}.; TRANSMEM 825 846 Helical; Name=S2 of repeat II. {ECO:0000255}.; TRANSMEM 853 871 Helical; Name=S3 of repeat II. {ECO:0000255}.; TRANSMEM 880 903 Helical; Name=S4 of repeat II. {ECO:0000255}.; TRANSMEM 915 935 Helical; Name=S5 of repeat II. {ECO:0000255}.; TRANSMEM 988 1012 Helical; Name=S6 of repeat II. {ECO:0000255}.; TRANSMEM 1302 1324 Helical; Name=S1 of repeat III. {ECO:0000255}.; TRANSMEM 1343 1363 Helical; Name=S2 of repeat III. {ECO:0000255}.; TRANSMEM 1374 1393 Helical; Name=S3 of repeat III. {ECO:0000255}.; TRANSMEM 1408 1429 Helical; Name=S4 of repeat III. {ECO:0000255}.; TRANSMEM 1440 1463 Helical; Name=S5 of repeat III. {ECO:0000255}.; TRANSMEM 1541 1566 Helical; Name=S6 of repeat III. {ECO:0000255}.; TRANSMEM 1628 1648 Helical; Name=S1 of repeat IV. {ECO:0000255}.; TRANSMEM 1663 1684 Helical; Name=S2 of repeat IV. {ECO:0000255}.; TRANSMEM 1692 1710 Helical; Name=S3 of repeat IV. {ECO:0000255}.; TRANSMEM 1725 1748 Helical; Name=S4 of repeat IV. {ECO:0000255}.; TRANSMEM 1763 1783 Helical; Name=S5 of repeat IV. {ECO:0000255}.; TRANSMEM 1847 1874 Helical; Name=S6 of repeat IV. {ECO:0000255}. TOPO_DOM 1 100 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 120 141 Extracellular. {ECO:0000255}.; TOPO_DOM 161 169 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 185 193 Extracellular. {ECO:0000255}.; TOPO_DOM 213 232 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 254 394 Extracellular. {ECO:0000255}.; TOPO_DOM 420 790 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 812 824 Extracellular. {ECO:0000255}.; TOPO_DOM 847 852 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 872 879 Extracellular. {ECO:0000255}.; TOPO_DOM 904 914 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 936 987 Extracellular. {ECO:0000255}.; TOPO_DOM 1013 1301 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1325 1342 Extracellular. {ECO:0000255}.; TOPO_DOM 1364 1373 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1394 1407 Extracellular. {ECO:0000255}.; TOPO_DOM 1430 1439 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1464 1540 Extracellular. {ECO:0000255}.; TOPO_DOM 1567 1627 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1649 1662 Extracellular. {ECO:0000255}.; TOPO_DOM 1685 1691 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1711 1724 Extracellular. {ECO:0000255}.; TOPO_DOM 1749 1762 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1784 1846 Extracellular. {ECO:0000255}.; TOPO_DOM 1875 2365 Cytoplasmic. {ECO:0000255}. "FUNCTION: Voltage-sensitive calcium channel that gives rise to T-type calcium currents. T-type calcium channels belong to the ""low-voltage activated (LVA)"" group. A particularity of this type of channel is an opening at quite negative potentials, and a voltage-dependent inactivation. T-type channels serve pacemaking functions in both central neurons and cardiac nodal cells and support calcium signaling in secretory cells and vascular smooth muscle. They may also be involved in the modulation of firing patterns of neurons. In the adrenal zona glomerulosa, participates in the signaling pathway leading to aldosterone production in response to either AGT/angiotensin II, or hyperkalemia. {ECO:0000250|UniProtKB:O95180}." PTM: In response to raising of intracellular calcium, the T-type channels are activated by CaM-kinase II. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O95180}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O95180}. Note=Interaction with STAC increases expression at the cell membrane. {ECO:0000250|UniProtKB:O95180}. SUBUNIT: Interacts (via N-terminal cytoplasmic domain) with STAC. {ECO:0000269|PubMed:27149520}. DOMAIN: Each of the four internal repeats contains five hydrophobic transmembrane segments (S1, S2, S3, S5, S6) and one positively charged transmembrane segment (S4). S4 segments probably represent the voltage-sensor and are characterized by a series of positively charged amino acids at every third position. +Q6PDJ1 CAHD1_MOUSE VWFA and cache domain-containing protein 1 (Cache domain-containing protein 1) 1288 143,812 Alternative sequence (1); Chain (1); Compositional bias (2); Domain (3); Erroneous gene model prediction (2); Glycosylation (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1110 1130 Helical. {ECO:0000255}. TOPO_DOM 50 1109 Extracellular. {ECO:0000255}.; TOPO_DOM 1131 1288 Cytoplasmic. {ECO:0000255}. FUNCTION: May regulate voltage-dependent calcium channels. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +P12658 CALB1_MOUSE Calbindin (Calbindin D28) (D-28K) (PCD-29) (Spot 35 protein) (Vitamin D-dependent calcium-binding protein, avian-type) 261 29,994 Calcium binding (4); Chain (1); Domain (5); Initiator methionine (1); Modified residue (1); Region (1) FUNCTION: Buffers cytosolic calcium. May stimulate a membrane Ca(2+)-ATPase and a 3',5'-cyclic nucleotide phosphodiesterase. SUBUNIT: Interacts with RANBP9. {ECO:0000250|UniProtKB:P05937}. DOMAIN: This protein has four functional calcium-binding sites; potential sites II and VI have lost affinity for calcium. {ECO:0000250|UniProtKB:P05937}. +P24452 CAPG_MOUSE Macrophage-capping protein (Actin regulatory protein CAP-G) (Actin-capping protein GCAP39) (Myc basic motif homolog 1) 352 39,240 Chain (1); Modified residue (2); Motif (1); Repeat (3); Sequence conflict (10) FUNCTION: Calcium-sensitive protein which reversibly blocks the barbed ends of actin filaments but does not sever preformed actin filaments. May play an important role in macrophage function. May play a role in regulating cytoplasmic and/or nuclear structures through potential interactions with actin. May bind DNA. Uncapping occurs either when Ca(2+) falls or when the concentration of polyphosphoinositide rises, both at low and high Ca(2+). PTM: Phosphorylated. Nuclear GCAP39 is more highly phosphorylated than cytoplasmic GCAP39. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8293478}. Cytoplasm {ECO:0000269|PubMed:8293478}. Melanosome {ECO:0000250|UniProtKB:P40121}. Cell projection, lamellipodium. Cell projection, ruffle. Note=In macrophages, may be predominantly cytoplasmic. Nuclear localization was observed in fibroblasts. In macrophages, present at the membrane-cytoplasm interface. In activated macrophages, concentrated in the ruffles of the leading lamellipodia. {ECO:0000269|PubMed:8293478}. SUBUNIT: Interacts with NUP62. Interacts with NUTF2 and RAN; involved in CAPG nuclear import. {ECO:0000250|UniProtKB:P40121}. TISSUE SPECIFICITY: Present in a large variety of tissues and is particularly abundant in kidney and lung. Highly expressed in macrophages (at protein level) (PubMed:8293478). {ECO:0000269|PubMed:8293478}. +P49070 CAMLG_MOUSE Calcium signal-modulating cyclophilin ligand (CAML) 294 32,542 Chain (1); Modified residue (1); Sequence conflict (1); Topological domain (3); Transmembrane (2) TRANSMEM 188 208 Helical. {ECO:0000255}.; TRANSMEM 239 255 Helical. {ECO:0000255}. TOPO_DOM 1 187 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 209 238 Extracellular. {ECO:0000255}.; TOPO_DOM 256 294 Cytoplasmic. {ECO:0000255}. FUNCTION: Likely involved in the mobilization of calcium as a result of the TCR/CD3 complex interaction. Binds to cyclophilin B. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SUBUNIT: The N-terminal domain binds to TNFRSF13B/TACI. {ECO:0000250}. +P51437 CAMP_MOUSE Cathelicidin antimicrobial peptide (Cathelin-like protein) (CLP) [Cleaved into: Cathelin-related antimicrobial peptide (Cramp)] 172 19,453 Disulfide bond (2); Peptide (1); Propeptide (1); Sequence conflict (5); Signal peptide (1) FUNCTION: Acts as a potent antimicrobial peptide. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Expressed in testis, spleen, stomach, and intestine. Very low expression found in heart, lung and skeletal muscle. No expression in brain, kidney or liver. +O35350 CAN1_MOUSE Calpain-1 catalytic subunit (EC 3.4.22.52) (Calcium-activated neutral proteinase 1) (CANP 1) (Calpain mu-type) (Calpain-1 large subunit) (Micromolar-calpain) (muCANP) 713 82,106 Active site (3); Calcium binding (4); Chain (1); Domain (5); Modified residue (1); Region (3); Sequence conflict (2); Site (2) FUNCTION: Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. {ECO:0000250|UniProtKB:P07384}. PTM: Undergoes calcium-induced successive autoproteolytic cleavages that generate a membrane-bound 78 kDa active form and an intracellular 75 kDa active form. Calpastatin reduces with high efficiency the transition from 78 kDa to 75 kDa calpain forms (By similarity). {ECO:0000250|UniProtKB:P07384}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P07384}. Cell membrane {ECO:0000250|UniProtKB:P07384}. Note=Translocates to the plasma membrane upon Ca(2+) binding. {ECO:0000250|UniProtKB:P07384}. SUBUNIT: Forms a heterodimer with a small (regulatory) subunit CAPNS1. {ECO:0000250|UniProtKB:P97571}. +Q9R1S8 CAN7_MOUSE Calpain-7 (EC 3.4.22.-) (PalB homolog) (PalBH) 813 92,564 Active site (3); Chain (1); Domain (1); Erroneous initiation (1); Modified residue (2); Region (2) FUNCTION: Calcium-regulated non-lysosomal thiol-protease. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. +Q60865 CAPR1_MOUSE Caprin-1 (Cytoplasmic activation- and proliferation-associated protein 1) (GPI-anchored membrane protein 1) (GPI-anchored protein p137) (GPI-p137) (p137GPI) (Membrane component chromosome 11 surface marker 1) (RNA granule protein 105) 707 78,169 Chain (1); Coiled coil (2); Erroneous gene model prediction (1); Erroneous initiation (1); Frameshift (1); Initiator methionine (1); Modified residue (11); Region (1); Sequence conflict (8) FUNCTION: May regulate the transport and translation of mRNAs of proteins involved in synaptic plasticity in neurons and cell proliferation and migration in multiple cell types (PubMed:20516077). Binds directly and selectively to MYC and CCND2 RNAs. In neuronal cells, directly binds to several mRNAs associated with RNA granules, including BDNF, CAMK2A, CREB1, MAP2, NTRK2 mRNAs, as well as to GRIN1 and KPNB1 mRNAs, but not to rRNAs (By similarity). {ECO:0000250|UniProtKB:Q14444, ECO:0000269|PubMed:20516077}. PTM: O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell projection, dendrite. Note=Associated with RNA granules. {ECO:0000250}. SUBUNIT: May form homomultimers (PubMed:14764709). Interacts with G3BP1; interaction is direct and takes place in cytoplasmic RNA granules. Interacts with PQBP1 (By similarity). {ECO:0000250|UniProtKB:Q14444, ECO:0000269|PubMed:14764709}. TISSUE SPECIFICITY: Highest expression in thymus, spleen and brain (at protein level). Lower levels in kidney, muscle and liver (at protein level). {ECO:0000269|PubMed:14764709, ECO:0000269|PubMed:20516077}. +O88875 BY55_MOUSE CD160 antigen (Natural killer cell receptor BY55) (CD antigen CD160) [Cleaved into: CD160 antigen, soluble form] 185 20,570 Chain (2); Disulfide bond (2); Domain (1); Glycosylation (2); Lipidation (1); Propeptide (1); Sequence conflict (1); Signal peptide (1) FUNCTION: CD160 antigen: Receptor on immune cells capable to deliver stimulatory or inhibitory signals that regulate cell activation and differentiation. Exists as a GPI-anchored and as a transmembrane form, each likely initiating distinct signaling pathways via phosphoinositol 3-kinase in activated NK cells and via LCK and CD247/CD3 zeta chain in activated T cells (By similarity). Receptor for both classical and non-classical MHC class I molecules (PubMed:16177084). Receptor or ligand for TNF superfamily member TNFRSF14, participating in bidirectional cell-cell contact signaling between antigen presenting cells and lymphocytes. Upon ligation of TNFRSF14, provides stimulatory signal to NK cells enhancing IFNG production and anti-tumor immune response (PubMed:25711213). On activated CD4+ T cells, interacts with TNFRSF14 and downregulates CD28 costimulatory signaling, restricting memory and alloantigen-specific immune response (By similarity). In the context of bacterial infection, acts as a ligand for TNFRSF14 on epithelial cells, triggering the production of antimicrobial proteins and proinflammatory cytokines (PubMed:22801499). {ECO:0000250|UniProtKB:O95971, ECO:0000269|PubMed:16177084, ECO:0000269|PubMed:22801499, ECO:0000269|PubMed:25711213}.; FUNCTION: CD160 antigen, soluble form: The soluble GPI-cleaved form, usually released by activated lymphocytes, might play an immune regulatory role by limiting lymphocyte effector functions. {ECO:0000250|UniProtKB:O95971}. SUBCELLULAR LOCATION: CD160 antigen: Cell membrane {ECO:0000269|PubMed:22801499, ECO:0000269|PubMed:25711213}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:O95971}.; SUBCELLULAR LOCATION: CD160 antigen, soluble form: Secreted {ECO:0000250|UniProtKB:O95971, ECO:0000305|PubMed:16177084}. Note=Released from the cell membrane by GPI cleavage. {ECO:0000250|UniProtKB:O95971, ECO:0000305|PubMed:16177084}. SUBUNIT: Homomultimer; disulfide-linked (By similarity). Interacts with classical and non-classical MHC class I molecules (PubMed:16177084). Interacts with TNFRSF14 (via cysteine-rich domain 1); this interaction is direct (PubMed:18193050). Interacts with LCK and CD247/CD3 zeta chain (By similarity). {ECO:0000250|UniProtKB:O95971, ECO:0000269|PubMed:16177084, ECO:0000269|PubMed:18193050}. TISSUE SPECIFICITY: Expressed in resting and activated NK cell subsets (at protein level) (PubMed:25711213, PubMed:16177084). Expressed in resting NKT cells (at protein level) (PubMed:16177084). Expressed in activated CD8+ T cells (at protein level). Highly expressed in intraepithelial lymphocyte (IEL) subsets, particularly in innate-like CD8A-positive IELs (at protein level) (PubMed:22801499). {ECO:0000269|PubMed:16177084, ECO:0000269|PubMed:22801499, ECO:0000269|PubMed:25711213}. +Q3V3R1 C1TM_MOUSE Monofunctional C1-tetrahydrofolate synthase, mitochondrial (EC 6.3.4.3) (Formyltetrahydrofolate synthetase) 977 105,729 Beta strand (1); Chain (1); Erroneous initiation (1); Helix (3); Modified residue (4); Nucleotide binding (1); Region (2); Sequence conflict (10); Transit peptide (1); Turn (1) One-carbon metabolism; tetrahydrofolate interconversion. FUNCTION: May provide the missing metabolic reaction required to link the mitochondria and the cytoplasm in the mammalian model of one-carbon folate metabolism in embryonic an transformed cells complementing thus the enzymatic activities of MTHFD2. {ECO:0000269|PubMed:15611115}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. DOMAIN: This monofunctional enzyme consists of two major domains: an N-terminal inactive methylene-THF dehydrogenase and cyclohydrolase domain and an active larger formyl-THF synthetase C-terminal domain. +Q8BHL7 C42S1_MOUSE CDC42 small effector protein 1 80 9,076 Chain (1); Domain (1); Lipidation (2) FUNCTION: Probably involved in the organization of the actin cytoskeleton by acting downstream of CDC42, inducing actin filament assembly. Alters CDC42-induced cell shape changes. In activated T-cells, may play a role in CDC42-mediated F-actin accumulation at the immunological synapse. May play a role in early contractile events in phagocytosis in macrophages (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. SUBUNIT: Interacts with CDC42 (in GTP-bound form). Interacts weakly with RAC1 and not at all with RHOA (By similarity). {ECO:0000250}. DOMAIN: The CRIB domain mediates interaction with CDC42. {ECO:0000250}. +Q8K479 C1QT5_MOUSE Complement C1q tumor necrosis factor-related protein 5 243 25,437 Chain (1); Domain (2); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. SUBUNIT: Homotrimer (via collagen-like domain). May form higher order oligomers by supercoiling of the trimers (By similarity). May interact with ERFE. {ECO:0000250}. +A2AE42 C56D1_MOUSE Cytochrome b561 domain-containing protein 1 229 25,519 Chain (1); Domain (1); Metal binding (4); Topological domain (2); Transmembrane (6) TRANSMEM 25 45 Helical. {ECO:0000255}.; TRANSMEM 54 74 Helical. {ECO:0000255}.; TRANSMEM 92 112 Helical. {ECO:0000255}.; TRANSMEM 129 149 Helical. {ECO:0000255}.; TRANSMEM 170 190 Helical. {ECO:0000255}.; TRANSMEM 194 214 Helical. {ECO:0000255}. TOPO_DOM 1 24 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 215 229 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9WUE3 C56D2_MOUSE Cytochrome b561 domain-containing protein 2 (EC 7.2.1.3) (Putative tumor suppressor protein 101F6) (Transmembrane ascorbate ferrireductase) 222 24,187 Chain (1); Domain (1); Initiator methionine (1); Metal binding (4); Mutagenesis (2); Topological domain (1); Transmembrane (6) TRANSMEM 18 38 Helical. {ECO:0000255}.; TRANSMEM 47 67 Helical. {ECO:0000255}.; TRANSMEM 86 106 Helical. {ECO:0000255}.; TRANSMEM 123 143 Helical. {ECO:0000255}.; TRANSMEM 163 183 Helical. {ECO:0000255}.; TRANSMEM 187 207 Helical. {ECO:0000255}. TOPO_DOM 2 17 Cytoplasmic. {ECO:0000305}. FUNCTION: Two-heme-containing cytochrome that catalyzes ascorbate-dependent trans-membrane ferric-chelate reduction. {ECO:0000269|PubMed:17938141, ECO:0000269|PubMed:19943161}. SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:17938141}; Multi-pass membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:17938141}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Highly expressed in the brain, lung, liver, and kidney (PubMed:17938141). Moderately expressed in the heart, placenta, skeletal muscle, and pancreas (PubMed:17938141). {ECO:0000269|PubMed:17938141}. +Q9DAE8 CA074_MOUSE UPF0739 protein C1orf74 homolog 263 28,921 Chain (1) +G3UW36 C97D2_MOUSE Uncharacterized protein CFAP97D2 (CFAP97 domain-containing protein 2) 98 11,800 Chain (1) +Q8BIF0 C99L2_MOUSE CD99 antigen-like protein 2 (MIC2-like protein 1) (CD antigen CD99) 237 25,463 Alternative sequence (1); Chain (1); Compositional bias (3); Erroneous gene model prediction (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 162 182 Helical. {ECO:0000255}. TOPO_DOM 26 161 Extracellular. {ECO:0000255}.; TOPO_DOM 183 237 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a role in a late step of leukocyte extravasation helping cells to overcome the endothelial basement membrane. Acts at the same site as, but independently of, PECAM1. Homophilic adhesion molecule, but these interactions may not be required for cell aggregation. {ECO:0000269|PubMed:17344467, ECO:0000269|PubMed:18163232, ECO:0000269|PubMed:20479283}. PTM: O-glycosylated. {ECO:0000269|PubMed:17344467}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}; Extracellular side {ECO:0000250}. Cell junction {ECO:0000269|PubMed:17344467}. Note=Concentrated at cell-cell contacts in cultured endothelial cells. TISSUE SPECIFICITY: Highly expressed in the nervous system, including brain, dentate nucleus of hippocampus, granular and Purkinje cells of cerebellum, brain stem nucleus and choroid plexus. Expressed in peripheral blood T- and B-cells and neutrophils (at protein level). Almost undetectable in bone marrow-derived neutrophils (at protein level). Also expressed in thymocytes (at protein level) with higher expression in cortical thymocytes than in medullary thymocytes. Expressed at high levels in testis (mostly in germ cells and Sertoli cells) and ovary (mostly in granulosa cells). Expressed in lung, heart, kidney and liver (at protein level); however, expression in heart, kidney and liver seems restricted to endothelial cells (at protein level). Highly expressed in endothelial cells and to a lower level in vascular smooth muscle cells (at protein level). Low expression in spleen. {ECO:0000269|PubMed:12706889, ECO:0000269|PubMed:17344467, ECO:0000269|PubMed:18163232}. +Q5RJF7 CA2D4_MOUSE Voltage-dependent calcium channel subunit alpha-2/delta-4 (Voltage-gated calcium channel subunit alpha-2/delta-4) [Cleaved into: Voltage-dependent calcium channel subunit alpha-2-4; Voltage-dependent calcium channel subunit delta-4] 1116 125,991 Alternative sequence (1); Chain (3); Disulfide bond (1); Domain (2); Glycosylation (3); Metal binding (3); Motif (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1095 1115 Helical. {ECO:0000255}. TOPO_DOM 48 1094 Extracellular. {ECO:0000255}.; TOPO_DOM 1116 1116 Cytoplasmic. {ECO:0000255}. FUNCTION: The alpha-2/delta subunit of voltage-dependent calcium channels regulates calcium current density and activation/inactivation kinetics of the calcium channel. {ECO:0000250}. PTM: May be proteolytically processed into subunits alpha-2-4 and delta-4 that are disulfide-linked. It is however unclear whether such cleavage really takes place in vivo and has a functional role (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Dimer formed of alpha-2-2 and delta-2 chains; disulfide-linked. Voltage-dependent calcium channels are multisubunit complexes, consisting of alpha-1 (CACNA1), alpha-2 (CACNA2D), beta (CACNB) and delta (CACNA2D) subunits in a 1:1:1:1 ratio (Probable). Interacts with CACNA1C and CACNB3 (By similarity). {ECO:0000250, ECO:0000305}. DOMAIN: The MIDAS-like motif in the VWFA domain binds divalent metal cations and is required to promote trafficking of the alpha-1 (CACNA1) subunit to the plasma membrane by an integrin-like switch. {ECO:0000250}. DISEASE: Note=Defects in Cacna2d4 are a cause of cone-rod dysfunction. Mice display affected retinal ribbon-type synapses. The retinopathy is accompanied by a substantial loss in the activities of the second-order neurons. Rod photoreceptor responses are maintained with reduced amplitude, whereas cone activities are absent. {ECO:0000269|PubMed:16877424}. +Q61112 CAB45_MOUSE 45 kDa calcium-binding protein (Cab45) (Stromal cell-derived factor 4) (SDF-4) 361 42,064 Alternative sequence (2); Calcium binding (6); Chain (1); Domain (6); Glycosylation (1); Modified residue (5); Natural variant (1); Region (1); Signal peptide (1) FUNCTION: May regulate calcium-dependent activities in the endoplasmic reticulum lumen or post-ER compartment. SUBCELLULAR LOCATION: Golgi apparatus lumen {ECO:0000269|PubMed:16608874}. DOMAIN: Binds calcium, probably via its EF-hands. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:8609160}. +Q4KKZ1 CA158_MOUSE Uncharacterized protein C1orf158 homolog 196 23,026 Chain (1); Erroneous initiation (3) +O08532 CA2D1_MOUSE Voltage-dependent calcium channel subunit alpha-2/delta-1 (Voltage-gated calcium channel subunit alpha-2/delta-1) [Cleaved into: Voltage-dependent calcium channel subunit alpha-2-1; Voltage-dependent calcium channel subunit delta-1] 1103 124,630 Alternative sequence (3); Chain (3); Disulfide bond (1); Domain (2); Glycosylation (8); Metal binding (3); Modified residue (1); Motif (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1074 1094 Helical. {ECO:0000255}. TOPO_DOM 25 1073 Extracellular. {ECO:0000255}.; TOPO_DOM 1095 1103 Cytoplasmic. {ECO:0000255}. FUNCTION: The alpha-2/delta subunit of voltage-dependent calcium channels regulates calcium current density and activation/inactivation kinetics of the calcium channel. Plays an important role in excitation-contraction coupling (By similarity). {ECO:0000250}. PTM: Proteolytically processed into subunits alpha-2-1 and delta-1 that are disulfide-linked. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Dimer formed of alpha-2-1 and delta-1 chains; disulfide-linked. Voltage-dependent calcium channels are multisubunit complexes, consisting of alpha-1 (CACNA1), alpha-2 (CACNA2D), beta (CACNB) and delta (CACNA2D) subunits in a 1:1:1:1 ratio (By similarity). {ECO:0000250}. DOMAIN: The MIDAS-like motif in the VWFA domain binds divalent metal cations and is required to promote trafficking of the alpha-1 (CACNA1) subunit to the plasma membrane by an integrin-like switch. {ECO:0000250}. TISSUE SPECIFICITY: Isoform 2A is expressed in skeletal muscle and aorta. Isoform 2B is expressed in brain. Isoform 2C is expressed in heart. Isoform 2D is expressed in heart and smooth muscle. Isoform 2E is expressed in smooth muscle. All five isoforms are expressed in the cardiovascular system. +Q9JLK7 CABP1_MOUSE Calcium-binding protein 1 (CaBP1) 227 25,943 Alternative sequence (1); Calcium binding (3); Chain (1); Domain (4); Initiator methionine (2); Lipidation (4); Metal binding (17); Modified residue (1) FUNCTION: Modulates calcium-dependent activity of inositol 1,4,5-triphosphate receptors (ITPRs). Inhibits agonist-induced intracellular calcium signaling. Enhances inactivation and does not support calcium-dependent facilitation of voltage-dependent P/Q-type calcium channels (By similarity). Causes calcium-dependent facilitation and inhibits inactivation of L-type calcium channels by binding to the same sites as calmodulin in the C-terminal domain of CACNA1C, but has an opposite effect on channel function. Suppresses the calcium-dependent inactivation of CACNA1D (PubMed:17050707, PubMed:17947313). Inhibits TRPC5 channels. Prevents NMDA receptor-induced cellular degeneration (By similarity). Required for the normal transfer of light signals through the retina (PubMed:27822497). {ECO:0000250|UniProtKB:Q9NZU7, ECO:0000269|PubMed:17050707, ECO:0000269|PubMed:17947313, ECO:0000269|PubMed:27822497}. PTM: Phosphorylated. The phosphorylation regulates the activity (By similarity). {ECO:0000250}. SUBUNIT: Homodimer; when bound to calcium or magnesium. Interacts (via C-terminus) with ITPR1, ITPR2 and ITPR3. This binding is calcium dependent and the interaction correlates with calcium concentration. An additional calcium-independent interaction with the N-terminus of ITPR1 results in a decreased InsP(3) binding to the receptor (By similarity). Interacts with CACNA1A (via C-terminal CDB motif) in the pre- and postsynaptic membranes (By similarity). Interacts with CACNA1D and CACNA1C (via C-terminal C and IQ motifs). The binding to the C motif is calcium independent whereas the binding to IQ requires the presence of calcium and is mutually exclusive with calmodulin binding (By similarity). Interacts with TRPC5 (via C-terminus). Interacts (via EF-hands 1 and 2) at microtubules with MAP1LC3B (By similarity). Interacts with MYO1C. Interacts (via EF-hands 1 and 2) with NSMF (via the central NLS-containing motif region), the interaction occurs in a calcium dependent manner after synaptic NMDA receptor stimulation and prevents nuclear import of NSMF. Interacts with SPACA9 homolog. {ECO:0000250|UniProtKB:Q9NZU7, ECO:0000269|PubMed:15895247, ECO:0000269|PubMed:17050707, ECO:0000269|PubMed:17947313, ECO:0000269|PubMed:17994197, ECO:0000269|PubMed:24256100}. DOMAIN: EF-1 binds magnesium constitutively under physiological conditions, EF-3 and EF-4 bind calcium cooperatively and EF-2 binds neither calcium nor magnesium. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the inner retina, specifically in amacrine cells and in cone OFF-bipolar cells (at protein level) (PubMed:27822497). {ECO:0000269|PubMed:27822497}. +Q9JLK3 CABP5_MOUSE Calcium-binding protein 5 (CaBP5) 173 19,730 Calcium binding (3); Chain (1); Domain (4) FUNCTION: Inhibits calcium-dependent inactivation of L-type calcium channel and shifts voltage dependence of activation to more depolarized membrane potentials. Involved in the transmission of light signals. {ECO:0000269|PubMed:18586882}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with CACNA1C (via C-terminal CDB motif) in a calcium-dependent manner. {ECO:0000269|PubMed:18586882}. TISSUE SPECIFICITY: Expressed in retina and in the inner hair cells (IHC) of the cochlea. {ECO:0000269|PubMed:17947313, ECO:0000269|PubMed:18586882}. +Q64444 CAH4_MOUSE Carbonic anhydrase 4 (EC 4.2.1.1) (Carbonate dehydratase IV) (Carbonic anhydrase IV) (CA-IV) 305 34,351 Active site (1); Beta strand (17); Chain (1); Disulfide bond (2); Domain (1); Glycosylation (2); Helix (10); Lipidation (1); Metal binding (3); Propeptide (1); Region (1); Signal peptide (1) FUNCTION: Reversible hydration of carbon dioxide. May stimulate the sodium/bicarbonate transporter activity of SLC4A4 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. SUBUNIT: Interacts with SLC4A4. {ECO:0000269|PubMed:14567693, ECO:0000269|PubMed:9541386}. +P33146 CAD15_MOUSE Cadherin-15 (Cadherin-14) (Muscle cadherin) (M-cadherin) 784 85,644 Chain (1); Compositional bias (1); Domain (5); Glycosylation (5); Propeptide (1); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 606 625 Helical. {ECO:0000255}. TOPO_DOM 60 605 Extracellular. {ECO:0000255}.; TOPO_DOM 626 784 Cytoplasmic. {ECO:0000255}. FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. M-cadherin is part of the myogenic program and may provide a trigger for terminal muscle differentiation. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. DOMAIN: Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain. {ECO:0000250}. TISSUE SPECIFICITY: Skeletal muscle. +P13634 CAH1_MOUSE Carbonic anhydrase 1 (EC 4.2.1.1) (Carbonate dehydratase I) (Carbonic anhydrase I) (CA-I) 261 28,331 Active site (2); Binding site (1); Chain (1); Domain (1); Initiator methionine (1); Metal binding (6); Modified residue (1); Region (1); Sequence conflict (2) FUNCTION: Reversible hydration of carbon dioxide. SUBCELLULAR LOCATION: Cytoplasm. +P0DP28 CALM3_MOUSE Calmodulin-3 149 16,838 Calcium binding (4); Chain (1); Cross-link (2); Domain (4); Erroneous translation (1); Initiator methionine (1); Modified residue (11); Region (1); Sequence conflict (1) FUNCTION: Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis. Mediates calcium-dependent inactivation of CACNA1C. Positively regulates calcium-activated potassium channel activity of KCNN2. {ECO:0000250|UniProtKB:P62158}. PTM: Ubiquitination results in a strongly decreased activity. {ECO:0000250}.; PTM: Phosphorylation results in a decreased activity. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, spindle pole. Note=Distributed throughout the cell during interphase, but during mitosis becomes dramatically localized to the spindle poles and the spindle microtubules. {ECO:0000250}. SUBUNIT: Interacts with CEP97, CCP110, MYO1C, TTN/titin and SRY. Interacts with MYO10. Interacts with RRAD (By similarity). Interacts with USP6; the interaction is calcium dependent (By similarity). Interacts with CDK5RAP2. Interacts with SCN5A (By similarity). Interacts with FCHO1. Interacts with MIP in a 1:2 stoichiometry; the interaction with the cytoplasmic domains from two MIP subunits promotes MIP water channel closure. Interacts with ORAI1; this may play a role in the regulation of ORAI1-mediated calcium transport (By similarity). Interacts with RYR1 (PubMed:18650434). Interacts with MYO5A (By similarity). Interacts with IQCF1 (PubMed:25380116). Interacts with SYT7 (PubMed:24569478). Interacts with CEACAM1 (via cytoplasmic domain); this interaction is in a calcium dependent manner and reduces homophilic cell adhesion through dissociation of dimer (By similarity). Interacts with RYR2; regulates RYR2 calcium-release channel activity (PubMed:18650434). Interacts with PCP4; regulates calmodulin calcium-binding (By similarity). Interacts with the heterotetrameric KCNQ2 and KCNQ3 channel; the interaction is calcium-independent, constitutive and participates to the proper assembly of a functional heterotetrameric M channel (By similarity). {ECO:0000250|UniProtKB:P0DP25, ECO:0000250|UniProtKB:P0DP26, ECO:0000250|UniProtKB:P62161, ECO:0000269|PubMed:18650434, ECO:0000269|PubMed:24569478, ECO:0000269|PubMed:25380116}. +Q91WQ9 CALL4_MOUSE Calmodulin-like protein 4 (Calmodulin-related) (CALM-Rel) 153 17,671 Alternative sequence (2); Chain (1); Domain (4); Sequence conflict (1) +Q8R464 CADM4_MOUSE Cell adhesion molecule 4 (Immunoglobulin superfamily member 4C) (IgSF4C) (Nectin-like protein 4) (NECL-4) (TSLC1-like protein 2) 388 42,723 Chain (1); Disulfide bond (3); Domain (3); Glycosylation (3); Modified residue (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 325 345 Helical. {ECO:0000255}. TOPO_DOM 25 324 Extracellular. {ECO:0000255}.; TOPO_DOM 346 388 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in the cell-cell adhesion. Has calcium- and magnesium-independent cell-cell adhesion activity. May have tumor-suppressor activity. {ECO:0000269|PubMed:14659875}. PTM: N-glycosylated. {ECO:0000269|PubMed:16261159}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Monomer and homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the brain and several organs including the kidney and liver. {ECO:0000269|PubMed:14659875}. +Q60755 CALCR_MOUSE Calcitonin receptor (CT-R) 533 62,469 Alternative sequence (1); Chain (1); Disulfide bond (3); Erroneous initiation (1); Glycosylation (4); Sequence conflict (2); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 171 190 Helical; Name=1. {ECO:0000255}.; TRANSMEM 198 217 Helical; Name=2. {ECO:0000255}.; TRANSMEM 275 297 Helical; Name=3. {ECO:0000255}.; TRANSMEM 315 334 Helical; Name=4. {ECO:0000255}.; TRANSMEM 351 374 Helical; Name=5. {ECO:0000255}.; TRANSMEM 398 415 Helical; Name=6. {ECO:0000255}.; TRANSMEM 428 449 Helical; Name=7. {ECO:0000255}. TOPO_DOM 42 170 Extracellular. {ECO:0000255}.; TOPO_DOM 191 197 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 218 274 Extracellular. {ECO:0000255}.; TOPO_DOM 298 314 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 335 350 Extracellular. {ECO:0000255}.; TOPO_DOM 375 397 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 416 427 Extracellular. {ECO:0000255}.; TOPO_DOM 450 533 Cytoplasmic. {ECO:0000255}. FUNCTION: This is a receptor for calcitonin. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. The calcitonin receptor is thought to couple to the heterotrimeric guanosine triphosphate-binding protein that is sensitive to cholera toxin. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBUNIT: Interacts with GPRASP2. {ECO:0000250}. +Q9DCA7 CALY_MOUSE Neuron-specific vesicular protein calcyon 226 24,580 Chain (1); Compositional bias (1); Topological domain (2); Transmembrane (1) TRANSMEM 89 109 Helical. {ECO:0000255}. TOPO_DOM 1 88 Extracellular. {ECO:0000255}.; TOPO_DOM 110 226 Cytoplasmic. {ECO:0000255}. FUNCTION: Interacts with clathrin light chain A and stimulates clathrin self-assembly and clathrin-mediated endocytosis. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with CLTA. {ECO:0000250}. TISSUE SPECIFICITY: Most abundant in brain. Also expressed in testis and ovary and, at much lower levels, in kidney and heart. {ECO:0000269|PubMed:12853145}. +Q8R2K1 FUCM_MOUSE Fucose mutarotase (EC 5.1.3.29) 153 16,805 Active site (3); Alternative sequence (4); Beta strand (7); Binding site (5); Chain (1); Erroneous initiation (1); Helix (7) FUNCTION: Involved in the interconversion between alpha- and beta-L-fucoses. L-Fucose (6-deoxy-L-galactose) exists as alpha-L-fucose (29.5%) and beta-L-fucose (70.5%), the beta-form is metabolized through the salvage pathway. GDP-L-fucose formed either by the de novo or salvage pathways is transported into the endoplasmic reticulum, where it serves as a substrate for N- and O-glycosylations by fucosyltransferases. Fucosylated structures expressed on cell surfaces or secreted in biological fluids are believed to play a critical role in cell-cell adhesion and recognition processes. {ECO:0000269|PubMed:17602138}. SUBUNIT: Mainly homodimer, but exists also as homotetramer, homooctamer, and homodecamer. The homodimeric form seems catalytically inactive. {ECO:0000269|PubMed:19524593}. TISSUE SPECIFICITY: Widely expressed in various tissues and cell lines, including kidney, liver, and pancreas, marginally in muscle and testis. {ECO:0000269|PubMed:17602138}. +Q9WV18 GABR1_MOUSE Gamma-aminobutyric acid type B receptor subunit 1 (GABA-B receptor 1) (GABA-B-R1) (GABA-BR1) (GABABR1) (Gb1) 960 108,216 Alternative sequence (1); Binding site (6); Chain (1); Coiled coil (1); Disulfide bond (4); Domain (2); Glycosylation (7); Modified residue (2); Region (1); Sequence conflict (10); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 591 611 Helical; Name=1. {ECO:0000255}.; TRANSMEM 631 651 Helical; Name=2. {ECO:0000255}.; TRANSMEM 667 687 Helical; Name=3. {ECO:0000255}.; TRANSMEM 710 730 Helical; Name=4. {ECO:0000255}.; TRANSMEM 768 788 Helical; Name=5. {ECO:0000255}.; TRANSMEM 804 824 Helical; Name=6. {ECO:0000255}.; TRANSMEM 833 853 Helical; Name=7. {ECO:0000255}. TOPO_DOM 17 590 Extracellular. {ECO:0000255}.; TOPO_DOM 612 630 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 652 666 Extracellular. {ECO:0000255}.; TOPO_DOM 688 709 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 731 767 Extracellular. {ECO:0000255}.; TOPO_DOM 789 803 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 825 832 Extracellular. {ECO:0000255}.; TOPO_DOM 854 960 Cytoplasmic. {ECO:0000255}. FUNCTION: Component of a heterodimeric G-protein coupled receptor for GABA, formed by GABBR1 and GABBR2 (PubMed:10773016, PubMed:10075644). Within the heterodimeric GABA receptor, only GABBR1 seems to bind agonists, while GABBR2 mediates coupling to G proteins (By similarity). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase (PubMed:10773016, PubMed:10075644). Signaling inhibits adenylate cyclase, stimulates phospholipase A2, activates potassium channels, inactivates voltage-dependent calcium-channels and modulates inositol phospholipid hydrolysis (PubMed:10075644). Calcium is required for high affinity binding to GABA (By similarity). Plays a critical role in the fine-tuning of inhibitory synaptic transmission (By similarity). Pre-synaptic GABA receptor inhibits neurotransmitter release by down-regulating high-voltage activated calcium channels, whereas postsynaptic GABA receptor decreases neuronal excitability by activating a prominent inwardly rectifying potassium (Kir) conductance that underlies the late inhibitory postsynaptic potentials (PubMed:10075644). Not only implicated in synaptic inhibition but also in hippocampal long-term potentiation, slow wave sleep, muscle relaxation and antinociception (By similarity). {ECO:0000250|UniProtKB:Q9UBS5, ECO:0000250|UniProtKB:Q9Z0U4, ECO:0000269|PubMed:10075644, ECO:0000269|PubMed:10773016}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Note=Coexpression of GABBR1 and GABBR2 is required for GABBR1 maturation and transport to the plasma membrane. Colocalizes with ATF4 in hippocampal neuron dendritic membranes (By similarity). {ECO:0000250}. SUBUNIT: Heterodimer of GABBR1 and GABBR2 (PubMed:10773016, PubMed:10075644, PubMed:9872744). Homodimers may form, but are inactive (By similarity). Interacts (via C-terminus) with ATF4 (via leucine zipper domain) (By similarity). Interacts with JAKMIP1 (PubMed:14718537). {ECO:0000250|UniProtKB:Q9Z0U4, ECO:0000269|PubMed:10075644, ECO:0000269|PubMed:10773016, ECO:0000269|PubMed:14718537, ECO:0000269|PubMed:9872744}. DOMAIN: Alpha-helical parts of the C-terminal intracellular region mediate heterodimeric interaction with GABBR2. The linker region between the transmembrane domain 3 (TM3) and the transmembrane domain 4 (TM4) probably plays a role in the specificity for G-protein coupling. TISSUE SPECIFICITY: Expressed in neuronal tissue including cortex, cerebellum and spinal cord. Not detected in non-neuronal tissues including heart, liver, spleen and kidney. {ECO:0000269|PubMed:11306808}. +Q99PR8 HSPB2_MOUSE Heat shock protein beta-2 (HspB2) 182 20,375 Alternative sequence (1); Chain (1); Domain (1); Sequence conflict (1) FUNCTION: May regulate the kinase DMPK. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Localizes to nuclear foci. {ECO:0000250}. SUBUNIT: Interacts with DMPK; may enhance its kinase activity. {ECO:0000250}. +Q9QZ57 HSPB3_MOUSE Heat shock protein beta-3 (HspB3) 154 17,230 Chain (1); Domain (1) FUNCTION: Inhibitor of actin polymerization. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Translocates to nuclear foci during heat shock. {ECO:0000250}. +P35385 HSPB7_MOUSE Heat shock protein beta-7 (HspB7) (Cardiovascular heat shock protein) (cvHsp) (Heat shock protein 25 kDa 2) (Protein p19/6.8) 169 18,635 Chain (1); Compositional bias (1); Domain (1); Region (1); Sequence conflict (5) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Nucleus, Cajal body {ECO:0000250}. Note=Resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles. {ECO:0000250}. SUBUNIT: Interacts with C-terminal domain of actin-binding protein 280. TISSUE SPECIFICITY: Found in both cardiac and slow skeletal (soleus) muscle. +Q9DAM3 HSPB9_MOUSE Heat shock protein beta-9 (HspB9) 168 18,493 Chain (1); Domain (1) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Translocates to nuclear foci during heat shock. {ECO:0000250}. TISSUE SPECIFICITY: Testis specific. {ECO:0000269|PubMed:11470154}. +Q9Z2G9 HTAI2_MOUSE Oxidoreductase HTATIP2 (EC 1.1.1.-) 242 26,870 Active site (2); Alternative sequence (2); Beta strand (9); Binding site (1); Chain (1); Helix (9); Initiator methionine (1); Modified residue (1); Nucleotide binding (1); Sequence conflict (7) FUNCTION: Oxidoreductase required for tumor suppression. NAPDH-bound form inhibits nuclear import by competing with nuclear import substrates for binding to a subset of nuclear transport receptors. May act as a redox sensor linked to transcription through regulation of nuclear import. {ECO:0000269|PubMed:14695192}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus envelope {ECO:0000250}. SUBUNIT: Monomer. Binds nuclear transport receptors XPO4, IPO5/RANBP5, IPO7, IPO9 and KPNB1 as well as GCN1L1/GCN1 and LRPPRC probably through their HEAT repeats. Binds NCOA5/CIA (By similarity). {ECO:0000250}. +Q5PRF0 HTR5A_MOUSE HEAT repeat-containing protein 5A 2038 219,893 Alternative sequence (1); Chain (1); Frameshift (2); Modified residue (1); Repeat (2); Sequence conflict (5) +Q8C547 HTR5B_MOUSE HEAT repeat-containing protein 5B 2070 224,319 Alternative sequence (4); Chain (1); Erroneous initiation (1); Erroneous translation (1); Frameshift (2); Modified residue (1); Repeat (3); Sequence conflict (3) +Q9R118 HTRA1_MOUSE Serine protease HTRA1 (EC 3.4.21.-) (High-temperature requirement A serine peptidase 1) (Serine protease 11) 480 51,214 Active site (3); Chain (1); Disulfide bond (2); Domain (3); Mutagenesis (2); Region (1); Sequence conflict (8); Signal peptide (1); Site (3) FUNCTION: Serine protease with a variety of targets, including extracellular matrix proteins such as fibronectin. HTRA1-generated fibronectin fragments further induce synovial cells to up-regulate MMP1 and MMP3 production. May also degrade proteoglycans, such as aggrecan, decorin and fibromodulin. Through cleavage of proteoglycans, may release soluble FGF-glycosaminoglycan complexes that promote the range and intensity of FGF signals in the extracellular space. Regulates the availability of insulin-like growth factors (IGFs) by cleaving IGF-binding proteins. Inhibits signaling mediated by TGF-beta family members. This activity requires the integrity of the catalytic site, but it is unclear whether it leads to the proteolytic degradation of TGF-beta proteins themselves (PubMed:18551132) or not (PubMed:14973287). By acting on TGF-beta signaling, may regulate many physiological processes, including retinal angiogenesis and neuronal survival and maturation during development. Intracellularly, degrades TSC2, leading to the activation of TSC2 downstream targets. {ECO:0000269|PubMed:14973287, ECO:0000269|PubMed:15993670, ECO:0000269|PubMed:18551132, ECO:0000269|PubMed:22049084}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q92743}. Secreted {ECO:0000250|UniProtKB:Q92743}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q92743}. Note=Predominantly secreted. Also found associated with the plasma membrane. {ECO:0000250|UniProtKB:Q92743}. SUBUNIT: Forms homotrimers. In the presence of substrate, may form higher-order multimers in a PDZ-independent manner (By similarity). Interacts with TGF-beta family members, including BMP4, TGFB1, TGFB2, activin A and GDF5. {ECO:0000250, ECO:0000269|PubMed:14973287}. DOMAIN: The IGFBP N-terminal domain mediates interaction with TSC2 substrate. {ECO:0000250}. TISSUE SPECIFICITY: In the brain, mainly expressed in cortical areas both in glial cells and neurons (at protein level). In bones, deposited in the matrix, with higher level in newly formed bone compared to fully calcified bone (at protein level). Also expressed in the tendons (at protein level). In the articular cartilage, detected only in the deepest zone of the joint cartilage. Not detected in the chondrocytes of the growth plate (at protein level). In an experimental arthritis model, at early disease stages, up-regulated in articular chondrocytes in the deep layers of the cartilage (at protein level). As arthritis progresses, chondrocyte expression expands toward the surface. {ECO:0000269|PubMed:14973287, ECO:0000269|PubMed:15993670, ECO:0000269|PubMed:18551132}. +Q9JIY5 HTRA2_MOUSE Serine protease HTRA2, mitochondrial (EC 3.4.21.108) (High temperature requirement protein A2) (HtrA2) (Omi stress-regulated endoprotease) (Serine protease 25) (Serine proteinase OMI) 458 49,348 Active site (3); Chain (1); Domain (1); Motif (1); Mutagenesis (3); Propeptide (1); Region (1); Sequence conflict (1); Transit peptide (1); Transmembrane (1) TRANSMEM 105 125 Helical. {ECO:0000255}. FUNCTION: Serine protease that shows proteolytic activity against a non-specific substrate beta-casein. Promotes or induces cell death either by direct binding to and inhibition of BIRC proteins (also called inhibitor of apoptosis proteins, IAPs), leading to an increase in caspase activity, or by a BIRC inhibition-independent, caspase-independent and serine protease activity-dependent mechanism. Cleaves THAP5 and promotes its degradation during apoptosis (By similarity). {ECO:0000250, ECO:0000269|PubMed:11604410}. PTM: Autoproteolytically activated. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Mitochondrion membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Note=Predominantly present in the intermembrane space. Released into the cytosol following apoptotic stimuli, such as UV treatment, and stimulation of mitochondria with BID. SUBUNIT: Homotrimer. Interacts with MXI2. Interacts with THAP5 under apoptotic conditions (By similarity). The mature protein, but not the precursor, binds to BIRC2/c-IAP1, BIRC3/c-IAP2 and XIAP/BIRC4 (By similarity). Interacts with BIRC6/bruce (By similarity). {ECO:0000250}. DOMAIN: The mature N-terminus is involved in the interaction with XIAP.; DOMAIN: The PDZ domain mediates interaction with MXI2. +Q9D236 HTRA3_MOUSE Serine protease HTRA3 (EC 3.4.21.-) (High-temperature requirement factor A3) (Pregnancy-related serine protease) (Toll-associated serine protease) 459 49,149 Active site (3); Alternative sequence (3); Chain (1); Disulfide bond (2); Domain (3); Mutagenesis (1); Region (1); Sequence conflict (2); Signal peptide (1) FUNCTION: Serine protease that cleaves beta-casein/CSN2 as well as several extracellular matrix (ECM) proteoglycans such as decorin/DCN, biglycan/BGN and fibronectin/FN1. Inhibits signaling mediated by TGF-beta family proteins possibly indirectly by degradation of these ECM proteoglycans (PubMed:15206957). May act as a tumor suppressor. Negatively regulates, in vitro, trophoblast invasion during placental development and may be involved in the development of the placenta in vivo. May also have a role in ovarian development, granulosa cell differentiation and luteinization (By similarity). {ECO:0000250|UniProtKB:P83110, ECO:0000269|PubMed:15206957}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P83110}. Note=Secretion increased during decidualization of endometrial stromal cells. {ECO:0000250|UniProtKB:P83110}. SUBUNIT: Homotrimer (By similarity). Interacts with MYH9 (By similarity). Interacts with TGFB1; the interaction inhibits TGFB-mediated signaling. Interacts with BMP4; the interaction inhibits BMP4-mediated signaling. Interacts with TGFB2 and GDF5. {ECO:0000250|UniProtKB:P83110, ECO:0000269|PubMed:15206957}. TISSUE SPECIFICITY: Highest level of isoform 1 in maternal part of the placenta, moderate level in heart, testis and ovary, low level in muscle and lung. High expression found in granulosa cells of the ovary. Expressed in bone matrix, particularly in articular chondrocytes. Very low level of isoform 2 expressed in placenta. Expressed in the bone matrix, particularly in articular chondrocytes. {ECO:0000269|PubMed:15206957, ECO:0000269|PubMed:15951015, ECO:0000269|Ref.2}. +A2RT60 HTRA4_MOUSE Serine protease HTRA4 (EC 3.4.21.-) (High-temperature requirement factor A4) 483 51,988 Active site (3); Chain (1); Domain (2); Region (1); Signal peptide (1) FUNCTION: Serine protease. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +Q8VI64 HUMMR_MOUSE Protein MGARP (Corneal endothelium-specific protein 1) (CESP-1) (Hypoxia up-regulated mitochondrial movement regulator protein) (Mitochondria-localized glutamic acid-rich protein) (Ovary-specific acidic protein) 283 29,925 Chain (1); Compositional bias (1); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 42 64 Helical; Anchor for type IV membrane protein. TOPO_DOM 1 41 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 65 283 Mitochondrial intermembrane. {ECO:0000255}. FUNCTION: Plays a role in the trafficking of mitochondria along microtubules. Regulates the kinesin-mediated axonal transport of mitochondria to nerve terminals along microtubules during hypoxia. Participates in the translocation of TRAK2/GRIF1 from the cytoplasm to the mitochondrion. Also plays a role in steroidogenesis through maintenance of mitochondrial abundance and morphology. {ECO:0000269|PubMed:19325000, ECO:0000269|PubMed:19528298}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:19325000, ECO:0000269|PubMed:19528298, ECO:0000269|PubMed:20107910, ECO:0000269|PubMed:21447634}. Mitochondrion outer membrane {ECO:0000269|PubMed:19325000, ECO:0000269|PubMed:19528298, ECO:0000269|PubMed:20107910, ECO:0000269|PubMed:21447634}; Single-pass type IV membrane protein {ECO:0000269|PubMed:19325000, ECO:0000269|PubMed:19528298, ECO:0000269|PubMed:20107910, ECO:0000269|PubMed:21447634}; Cytoplasmic side {ECO:0000269|PubMed:19325000, ECO:0000269|PubMed:19528298, ECO:0000269|PubMed:20107910, ECO:0000269|PubMed:21447634}. Note=Colocalizes with RHOT1, RHOT2, TRAK1 and TRAK2 at the mitochondrion (PubMed:19528298). SUBUNIT: Interacts with RHOT1/Miro-1, RHOT2/Miro-2, TRAK1/OIP106 and TRAK2/GRIF1. {ECO:0000269|PubMed:19528298}. TISSUE SPECIFICITY: Expressed in the ovary, testis, brain, adrenal glands and the compartments of the visual nervous system. Expressed in corneal endothelium (CE) (at protein level). Expressed in steroidogenic tissues with the highest level of expression observed in the adrenal gland. Weakly expressed in placenta. Weakly expressed in astrocytes and neurons under normoxia. Strongly expressed in astrocytes and neurons under hypoxia. Expressed in each layer of the retina, with particularly higher staining in the inner segment of the photoreceptor (IS), the outer plexiform layer (OPL) and the ganglion cell layer (GCL). {ECO:0000269|PubMed:16565373, ECO:0000269|PubMed:19325000, ECO:0000269|PubMed:19528298, ECO:0000269|PubMed:20107910, ECO:0000269|PubMed:21447634}. +Q9JL27 FUT2_MOUSE Galactoside 2-alpha-L-fucosyltransferase 2 (EC 2.4.1.344) (EC 2.4.1.69) (Alpha(1,2)FT 2) (Fucosyltransferase 2) (GDP-L-fucose:beta-D-galactoside 2-alpha-L-fucosyltransferase 2) (Secretory blood group protein 2) 347 39,243 Chain (1); Glycosylation (4); Topological domain (2); Transmembrane (1) TRANSMEM 6 26 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 5 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 27 347 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Mediates the transfer of fucose to the terminal galactose on glycan chains of cell surface glycoproteins and glycolipids (PubMed:11323419, PubMed:27161092). The resulting epitope plays a role in cell-cell interaction including host-microbe interaction (PubMed:19706747, PubMed:27161092). Mediates interaction with intestinal microbiota influencing its composition (PubMed:19706747, PubMed:27161092). Creates a soluble precursor oligosaccharide FuC-alpha ((1,2)Galbeta-) called the H antigen, which is an essential substrate for the final step in the blood group antigen synthesis pathway (PubMed:11323419). {ECO:0000269|PubMed:11323419, ECO:0000269|PubMed:19706747, ECO:0000269|PubMed:27161092}. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Membrane-bound form in trans cisternae of Golgi. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in stomach, colon, ovary and uterus, specifically in luminal uterine epithelium. {ECO:0000269|PubMed:11323419}. +Q3V0G7 GARL3_MOUSE GTPase-activating Rap/Ran-GAP domain-like protein 3 1038 115,437 Alternative sequence (2); Chain (1); Domain (2); Erroneous initiation (1); Modified residue (5); Sequence conflict (1) +Q8BVW0 GANC_MOUSE Neutral alpha-glucosidase C (EC 3.2.1.20) 898 102,008 Active site (3); Alternative sequence (3); Chain (1); Erroneous initiation (1) FUNCTION: Has alpha-glucosidase activity. {ECO:0000250}. +Q9CZD3 GARS_MOUSE Glycine--tRNA ligase (EC 3.6.1.17) (EC 6.1.1.14) (Diadenosine tetraphosphate synthetase) (AP-4-A synthetase) (Glycyl-tRNA synthetase) (GlyRS) 729 81,878 Binding site (4); Chain (1); Domain (1); Modified residue (5); Natural variant (1); Nucleotide binding (4); Region (2); Sequence conflict (4) FUNCTION: Catalyzes the ligation of glycine to the 3'-end of its cognate tRNA. Is also able produce diadenosine tetraphosphate (Ap4A), a universal pleiotropic signaling molecule needed for cell regulation pathways, by direct condensation of 2 ATPs (By similarity). {ECO:0000250|UniProtKB:P41250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P41250}. Cell projection, axon {ECO:0000250|UniProtKB:P41250}. Secreted {ECO:0000269|PubMed:26503042}. Secreted, exosome {ECO:0000305|PubMed:26503042}. Note=Associated with granules in cultured neuron cells (By similarity). Secreted by motor neuron and differentiated myotube cell lines, but not by undifferentiated myoblasts, possibly through the exosome pathway (PubMed:26503042). {ECO:0000250|UniProtKB:P41250, ECO:0000269|PubMed:26503042}. SUBUNIT: Homodimer. {ECO:0000250}. DISEASE: Note=Mice (Nmf249) heterozygous for the P278YK variant are used a model for human Charcot-Marie-Tooth 2D (CMT2D), which is caused by dominant GARS mutations. They exhibit reduced amplitudes of muscle compound action potentials and a large reduction in sciatic nerve conduction velocity in the absence of demyelination or remyelination, resulting from an age-related decrease in the number of large myelinated motor and sensory axons. The loss of myelinated axons is length-dependent, and there is a length- and time-dependent decrease in motor innervation of distal versus proximal muscles. Most of the axonal loss occurs by 1 month of age and mice that survive this period can be long-lived. At the molecular level, the P278YK mutation creates a neomorphic binding activity leading to the interaction of the variant with NRP1. This interaction competes out VEGFA binding and inhibits VEGFA-NRP1 signling which is essential for motor neuron survival. VEGFA, but not GDNF treatment significantly ameliorates the loss of motor function in mutant mice. {ECO:0000269|PubMed:16982418}. +Q5U4C1 GASP1_MOUSE G-protein coupled receptor-associated sorting protein 1 (GASP-1) 1347 151,745 Alternative sequence (1); Chain (1); Compositional bias (1); Erroneous initiation (1); Modified residue (5); Sequence conflict (2) FUNCTION: Modulates lysosomal sorting and functional down-regulation of a variety of G-protein coupled receptors. Targets receptors for degradation in lysosomes via its interaction with BECN2. {ECO:0000269|PubMed:23954414}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with cytoplasmic tails of a variety of G-protein coupled receptors such as delta opioid receptor/OPRD1, beta-2 adrenergic receptor/ADRB2 and D4 dopamine receptor/DRD4 as well as D2 dopamine receptor/DRD2. Interacts with PER1 (By similarity). Interacts with BECN2; the interaction is direct. {ECO:0000250, ECO:0000269|PubMed:23954414}. TISSUE SPECIFICITY: Expressed in the brain, with higher expression in the hippocampus, hypothalamus and olfactory bulb. {ECO:0000269|PubMed:15086532}. +P17679 GATA1_MOUSE Erythroid transcription factor (Eryf1) (GATA-binding factor 1) (GATA-1) (GF-1) (NF-E1 DNA-binding protein) 413 42,674 Alternative sequence (1); Chain (1); Cross-link (1); Helix (3); Modified residue (16); Mutagenesis (28); Region (3); Sequence conflict (2); Turn (2); Zinc finger (2) FUNCTION: Transcriptional activator or repressor which probably serves as a general switch factor for erythroid development. It binds to DNA sites with the consensus sequence 5'-[AT]GATA[AG]-3' within regulatory regions of globin genes and of other genes expressed in erythroid cells. Activates the transcription of genes involved in erythroid differentiation of K562 erythroleukemia cells, including HBB, HBG1/2, ALAS2 and HMBS (By similarity). {ECO:0000250|UniProtKB:P15976, ECO:0000269|PubMed:15173587, ECO:0000269|PubMed:16888089, ECO:0000269|PubMed:2276623, ECO:0000269|PubMed:8206977, ECO:0000269|PubMed:8524811}. PTM: Highly phosphorylated on serine residues. Phosphorylation on Ser-310 is enhanced on erythroid differentiation. Phosphorylation on Ser-142 promotes sumoylation on Lys-137 (By similarity). {ECO:0000250}.; PTM: Sumoylation on Lys-137 is enhanced by phosphorylation on Ser-142 and by interaction with PIAS4. Sumoylation with SUMO1 has no effect on transcriptional activity. {ECO:0000269|PubMed:15173587, ECO:0000269|PubMed:8206977}.; PTM: Acetylated on Lys-233, Lys-245 Lys-246 by EP300 (By similarity). Acetylated on Lys-246, Lys-252 and Lys-312 by CREBBP in vitro. Acetylation does not affect DNA-binding in vitro but is essential to induce erythroid differentiation and for binding chromatin in vivo. {ECO:0000250, ECO:0000269|PubMed:10207073, ECO:0000269|PubMed:21536911}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16888089}. SUBUNIT: May form homodimers or heterodimers with other isoforms. Interacts (via the N-terminal zinc finger) with ZFPM1 (By similarity). Interacts with GFI1B. Interacts with PIAS4; the interaction enhances sumoylation and represses the transactivational activity in a sumoylation-independent manner. Interacts with LMCD1. Interacts with CREBBP; the interaction stimulates acetylation and transcriptional activity in vivo. Interacts with BRD3. Interacts with MED1, CCAR1 and CALCOCO1. Interacts with EP300 (By similarity). Interacts with CEBPE (By similarity). {ECO:0000250|UniProtKB:P15976, ECO:0000269|PubMed:10207073, ECO:0000269|PubMed:15173587, ECO:0000269|PubMed:15920471, ECO:0000269|PubMed:16199866, ECO:0000269|PubMed:21536911, ECO:0000269|PubMed:21555453, ECO:0000269|PubMed:24245781, ECO:0000269|PubMed:8524811}. DOMAIN: The two fingers are functionally distinct and cooperate to achieve specific, stable DNA binding. The first finger is necessary only for full specificity and stability of binding, whereas the second one is required for binding. TISSUE SPECIFICITY: Erythrocytes. Expressed (at protein level) in liver. {ECO:0000269|PubMed:2725678, ECO:0000269|PubMed:8524811}. +O09100 GATA2_MOUSE Endothelial transcription factor GATA-2 (GATA-binding protein 2) 480 50,468 Chain (1); Cross-link (1); Modified residue (3); Zinc finger (2) FUNCTION: Transcriptional activator which regulates endothelin-1 gene expression in endothelial cells. Binds to the consensus sequence 5'-AGATAG-3'. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with BRD3. Interacts with AR and CCAR1 (By similarity). {ECO:0000250|UniProtKB:P23769, ECO:0000269|PubMed:21536911}. +Q61316 HSP74_MOUSE Heat shock 70 kDa protein 4 (Heat shock 70-related protein APG-2) 841 94,133 Chain (1); Modified residue (13) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. SUBUNIT: Interacts with TJP1/ZO-1. {ECO:0000250}. +Q9CZN8 GATA_MOUSE Glutamyl-tRNA(Gln) amidotransferase subunit A, mitochondrial (Glu-AdT subunit A) (EC 6.3.5.7) (Glutaminyl-tRNA synthase-like protein 1) 525 56,783 Active site (3); Chain (1); Sequence conflict (2) FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). {ECO:0000255|HAMAP-Rule:MF_03150}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03150}. SUBUNIT: Subunit of the heterotrimeric GatCAB amidotransferase (AdT) complex, composed of A (QRSL1), B (GATB) and C (GATC) subunits. {ECO:0000255|HAMAP-Rule:MF_03150}. +Q9JK92 HSPB8_MOUSE Heat shock protein beta-8 (HspB8) (Alpha-crystallin C chain) (Small stress protein-like protein HSP22) 196 21,533 Chain (1); Domain (1); Modified residue (6) FUNCTION: Displays temperature-dependent chaperone activity. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UJY1}. Nucleus {ECO:0000250|UniProtKB:Q9UJY1}. Note=Translocates to nuclear foci during heat shock. {ECO:0000250|UniProtKB:Q9UJY1}. SUBUNIT: Monomer. Interacts with HSPB1 (By similarity). Interacts with DNAJB6 (By similarity). Interacts with BAG3 (By similarity). {ECO:0000250|UniProtKB:Q9UJY1}. TISSUE SPECIFICITY: Highly expressed in skeletal muscle, heart, uterus, liver, lung and ovary. Low levels found in stomach and brain. Not detected in small intestine, large intestine, kidney, spleen and testis. In the ovary, expression is concentrated in the endometrium and in the connective tissue between the circular and longitudinal muscles of the myometrium. {ECO:0000269|PubMed:11133685}. +Q9Z0E6 GBP2_MOUSE Guanylate-binding protein 2 (EC 3.6.5.-) (GTP-binding protein 2) (GBP-2) (mGBP-2) (mGBP2) (Guanine nucleotide-binding protein 2) (Interferon-induced guanylate-binding protein 2) 589 66,739 Chain (1); Domain (1); Lipidation (1); Modified residue (1); Nucleotide binding (3); Propeptide (1); Region (1); Sequence conflict (5) FUNCTION: Hydrolyzes GTP to GMP in 2 consecutive cleavage reactions, but the major reaction product is GDP (By similarity). Exhibits antiviral activity against influenza virus. Promote oxidative killing and deliver antimicrobial peptides to autophagolysosomes, providing broad host protection against different pathogen classes (By similarity). {ECO:0000250|UniProtKB:P32455, ECO:0000250|UniProtKB:P32456}. PTM: Isoprenylation is required for proper subcellular location. {ECO:0000250|UniProtKB:P32456}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P32456}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P32456}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P32456}. Membrane {ECO:0000250|UniProtKB:P32456}; Lipid-anchor {ECO:0000250|UniProtKB:P32456}. Note=GBP2-GBP5 dimers localize to the Golgi apparatus. {ECO:0000250|UniProtKB:P32456}. SUBUNIT: Homodimer; homodimerization occurs upon GTP-binding and is required for the association with membranous structures. Heterodimer with other family members, including GBP1, GBP3, GBP4 and GBP5. {ECO:0000250|UniProtKB:P32456}. +P56475 GBRR1_MOUSE Gamma-aminobutyric acid receptor subunit rho-1 (GABA(A) receptor subunit rho-1) (GABA(C) receptor) 480 55,488 Chain (1); Disulfide bond (1); Erroneous initiation (2); Glycosylation (3); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (4) TRANSMEM 283 306 Helical. {ECO:0000305}.; TRANSMEM 310 332 Helical. {ECO:0000305}.; TRANSMEM 344 366 Helical. {ECO:0000305}.; TRANSMEM 459 480 Helical. {ECO:0000305}. TOPO_DOM 22 282 Extracellular. {ECO:0000305}.; TOPO_DOM 367 458 Cytoplasmic. {ECO:0000305}. FUNCTION: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel. Rho-1 GABA receptor could play a role in retinal neurotransmission (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Generally pentameric. There are five types of GABA(A) receptor chains: alpha, beta, gamma, delta, and rho. Interacts with SQSTM1 (By similarity). {ECO:0000250}. +Q9DC63 FBX3_MOUSE F-box only protein 3 480 55,227 Alternative sequence (3); Chain (1); Compositional bias (3); Domain (2); Sequence conflict (8) FUNCTION: Substrate recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. Mediates the ubiquitination of HIPK2 and probably that of EP300, leading to rapid degradation by the proteasome. In the presence of PML, HIPK2 ubiquitination still occurs, but degradation is prevented. PML, HIPK2 and FBXO3 may act synergically to activate p53/TP53-dependent transactivation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Colocalizes with PML at the peripheries of nuclear bodies. {ECO:0000250}. SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex consisting of FBXO3, SKP1, CUL1 and RBX1. Interacts with PML, interaction is direct and takes place either alone or within the SCF complex (By similarity). {ECO:0000250}. +Q2TB54 FCAMR_MOUSE High affinity immunoglobulin alpha and immunoglobulin mu Fc receptor (Fc alpha/mu receptor) (mFcamR) (CD antigen CD351) 535 57,823 Alternative sequence (1); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (1); Mutagenesis (2); Region (1); Sequence conflict (28); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 456 476 Helical. {ECO:0000255}. TOPO_DOM 36 455 Extracellular. {ECO:0000255}.; TOPO_DOM 477 535 Cytoplasmic. {ECO:0000255}. FUNCTION: Functions as a receptor for the Fc fragment of IgA and IgM. Binds IgA and IgM with high affinity and mediates their endocytosis. May function in the immune response to microbes mediated by IgA and IgM. {ECO:0000269|PubMed:11062505}. PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11062505}; Single-pass type I membrane protein {ECO:0000269|PubMed:11062505}. TISSUE SPECIFICITY: Expressed in several tissues including thymus, spleen, liver, kidney, small and large intestine, testis and placenta. Expressed by oligodendrocytes, B-cells and macrophages but not granulocytes, T-cells or NK cells (at protein level). {ECO:0000269|PubMed:11062505, ECO:0000269|PubMed:12527391}. +Q8BK06 FBX9_MOUSE F-box only protein 9 437 50,760 Alternative sequence (3); Chain (1); Domain (1); Frameshift (1); Initiator methionine (2); Modified residue (5); Repeat (1); Sequence conflict (1) Protein modification; protein ubiquitination. FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of TTI1 and TELO2 in a CK2-dependent manner, thereby directly regulating mTOR signaling. SCF(FBXO9) recognizes and binds mTORC1-bound TTI1 and TELO2 when they are phosphorylated by CK2 following growth factor deprivation, leading to their degradation. In contrast, the SCF(FBXO9) does not mediate ubiquitination of TTI1 and TELO2 when they are part of the mTORC2 complex. As a consequence, mTORC1 is inactivated to restrain cell growth and protein translation, while mTORC2 is activated due to the relief of feedback inhibition by mTORC1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Part of the SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase complex SCF(FBXO9) composed of CUL1, SKP1, RBX1 and FBXO9. Interacts with TTI1 and TELO2; when TTI1 and TELO2 are phosphorylated by CK2 (By similarity). {ECO:0000250}. +Q8BG80 FBX46_MOUSE F-box only protein 46 (F-box only protein 34-like) 603 65,294 Chain (1); Domain (1); Modified residue (1) FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. {ECO:0000250}. SUBUNIT: Interacts with SKP1 and CUL1. {ECO:0000250}. +A1YIY0 FCRL6_MOUSE Fc receptor-like protein 6 (FcR-like protein 6) (FcRL6) 268 30,237 Alternative sequence (2); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (2); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 216 236 Helical. {ECO:0000255}. TOPO_DOM 17 215 Extracellular. {ECO:0000255}.; TOPO_DOM 237 268 Cytoplasmic. {ECO:0000255}. FUNCTION: Acts as a MHC class II receptor. When stimulated on its own, does not play a role in cytokine production or the release of cytotoxic granules by NK cells and cytotoxic CD8(+) T cells. Does not act as an Fc receptor. {ECO:0000250|UniProtKB:Q6DN72}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6DN72}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Interacts with class II MHC. {ECO:0000250|UniProtKB:Q6DN72}. +Q920A9 FCRLA_MOUSE Fc receptor-like A (Fc receptor homolog expressed in B-cells) (Fc receptor-like and mucin-like protein 1) (Fc receptor-like protein) (Fc receptor-related protein X) (FcRX) 352 38,348 Alternative sequence (1); Chain (1); Compositional bias (1); Disulfide bond (2); Domain (2); Sequence conflict (7); Signal peptide (1) FUNCTION: May be implicated in B-cell differentiation and lymphomagenesis. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q7L513}. Note=Seems not to be secreted. {ECO:0000250|UniProtKB:Q7L513}. SUBUNIT: Monomer or homodimer; disulfide-linked. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in spleen. Expressed in immature B-cell and B-cell lines. {ECO:0000269|PubMed:12202404}. +Q5BJ29 FBXL7_MOUSE F-box/LRR-repeat protein 7 (F-box and leucine-rich repeat protein 7) 491 54,646 Chain (1); Domain (1); Erroneous initiation (1); Repeat (10) Protein modification; protein ubiquitination. FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of AURKA during mitosis, causing mitotic arrest. {ECO:0000269|PubMed:22306998}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:22306998}. Note=Localizes to the centrosome during spindle formation. SUBUNIT: Part of the SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase complex SCF(FBXL7) composed of CUL1, SKP1, RBX1 and FBXL7. Interacts with AURKA; interaction takes place during mitosis but not in interphase. {ECO:0000269|PubMed:22306998}. +Q5DRQ8 FCRLB_MOUSE Fc receptor-like B (Fc receptor homolog expressed in B-cells protein 2) (FREB-2) (Fc receptor-like and mucin-like protein 2) (Fc receptor-like protein 2) (Fc receptor-related protein Y) (FcRY) 427 47,502 Chain (1); Disulfide bond (2); Domain (2); Glycosylation (1); Sequence conflict (4); Signal peptide (1) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6BAA4}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q6BAA4}. Note=Seems not to be secreted. {ECO:0000250|UniProtKB:Q6BAA4}. TISSUE SPECIFICITY: Expressed at low levels. Expressed in B-lymphocytes. Detected in spleen, lymph node, kidney, lung and brain. {ECO:0000269|PubMed:15815692, ECO:0000269|PubMed:16263223}. +P59113 FERM1_MOUSE Fermitin family homolog 1 (Kindlin-1) (Unc-112-related protein 1) 677 76,941 Beta strand (13); Chain (1); Compositional bias (1); Domain (2); Erroneous initiation (1); Helix (5); Modified residue (2); Sequence conflict (2); Turn (2) FUNCTION: Involved in cell adhesion. Contributes to integrin activation. When coexpressed with talin, potentiates activation of ITGA2B. Required for normal keratinocyte proliferation. Required for normal polarization of basal keratinocytes in skin, and for normal cell shape. Required for normal adhesion of keratinocytes to fibronectin and laminin, and for normal keratinocyte migration to wound sites (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell junction, focal adhesion {ECO:0000250}. Cell projection, ruffle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Colocalizes with filamentous actin. Constituent of focal adhesions (By similarity). Localized at the basal aspect of skin keratinocytes, close to the cell membrane (By similarity). Upon TGFB1 treatment, it localizes to membrane ruffles (By similarity). {ECO:0000250}. SUBUNIT: Interacts with the cytoplasmic domain of integrins ITGB1 and ITGB3. {ECO:0000250}. DOMAIN: The FERM domain is not correctly detected by PROSITE or Pfam techniques because it contains the insertion of a PH domain. The FERM domain contains the subdomains F1, F2 and F3. It is preceded by a F0 domain with a ubiquitin-like fold. The F0 domain is required for integrin activation and for localization at focal adhesions (By similarity). {ECO:0000250}. +Q80ZA7 FMR1N_MOUSE Fragile X mental retardation 1 neighbor protein (Protein mNY-SAR-35) 238 27,018 Alternative sequence (1); Chain (1); Domain (1); Sequence conflict (1); Topological domain (3); Transmembrane (2) TRANSMEM 80 100 Helical. {ECO:0000255}.; TRANSMEM 179 199 Helical. {ECO:0000255}. TOPO_DOM 1 79 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 101 178 Extracellular. {ECO:0000255}.; TOPO_DOM 200 238 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +P50608 FMOD_MOUSE Fibromodulin (FM) (Collagen-binding 59 kDa protein) (Keratan sulfate proteoglycan fibromodulin) (KSPG fibromodulin) 376 43,055 Chain (1); Compositional bias (2); Disulfide bond (1); Domain (1); Glycosylation (5); Modified residue (7); Repeat (11); Signal peptide (1) FUNCTION: Affects the rate of fibrils formation. May have a primary role in collagen fibrillogenesis. PTM: Binds keratan sulfate chains. {ECO:0000250}.; PTM: Sulfated on tyrosine residue(s). {ECO:0000305}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SUBUNIT: Binds to type I and type II collagen. TISSUE SPECIFICITY: Highest levels observed in knee epiphysis, in calvarial and diaphyseal bone, in nasal and costal cartilage, in the eye, and in bladder. In mature knee joint it is mostly present in the proliferating zone of growth plate. It is also observed in ligaments, especially at insertion sites, in the junction between meniscus and joint capsule, in the perimysium of skeletal muscle and in the periosteum. +Q9D799 FMT_MOUSE Methionyl-tRNA formyltransferase, mitochondrial (MtFMT) (EC 2.1.2.9) 386 43,092 Chain (1); Sequence conflict (2); Transit peptide (1) FUNCTION: Formylates methionyl-tRNA in mitochondria. A single tRNA(Met) gene gives rise to both an initiator and an elongator species via an unknown mechanism (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. DOMAIN: Composed of an N- and a C-terminal domain. The N-terminal domain carries the tetrahydrofolate (THF)-binding site and the C-terminal domain is presumably involved in positioning the Met-tRNA substrate for the formylation reaction. +Q80WB0 FND11_MOUSE Fibronectin type III domain-containing protein 11 326 37,356 Chain (1); Domain (1) +Q8BX90 FND3A_MOUSE Fibronectin type-III domain-containing protein 3A 1198 131,958 Chain (1); Compositional bias (1); Domain (9); Modified residue (4); Sequence conflict (4); Transmembrane (1) TRANSMEM 1177 1197 Helical. {ECO:0000255}. FUNCTION: Mediates spermatid-Sertoli adhesion during spermatogenesis. {ECO:0000269|PubMed:16904100}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Testis. Localizes to the acrosome of spermatids, as well as to Leydig cells. Can be detected on the acrosome beginning at steps 2-3 and continuing until step 12 of spermiogenesis. {ECO:0000269|PubMed:16904100}. +P01101 FOS_MOUSE Proto-oncogene c-Fos (Cellular oncogene fos) 380 40,838 Chain (1); Cross-link (4); Domain (1); Helix (1); Modified residue (7); Mutagenesis (13); Region (2) FUNCTION: Nuclear phosphoprotein which forms a tight but non-covalently linked complex with the JUN/AP-1 transcription factor. On TGF-beta activation, forms a multimeric SMAD3/SMAD4/JUN/FOS complex, at the AP1/SMAD-binding site to regulate TGF-beta-mediated signaling (By similarity). Has a critical function in regulating the development of cells destined to form and maintain the skeleton. It is thought to have an important role in signal transduction, cell proliferation and differentiation. In growing cells, activates phospholipid synthesis, possibly by activating CDS1 and PI4K2A. This activity requires Tyr-dephosphorylation and association with the endoplasmic reticulum. {ECO:0000250, ECO:0000269|PubMed:12134156, ECO:0000269|PubMed:12972619, ECO:0000269|PubMed:15719069, ECO:0000269|PubMed:21998197, ECO:0000269|PubMed:22105363}. PTM: Phosphorylated in the C-terminal upon stimulation by nerve growth factor (NGF) and epidermal growth factor (EGF). Phosphorylated, in vitro, by MAPK and RSK1. Phosphorylation on both Ser-362 and Ser-374 by MAPK1/2 and RSK1/2 leads to protein stabilization with phosphorylation on Ser-374 being the major site for protein stabilization on NGF stimulation. Phosphorylation on Ser-362 and Ser-374 primes further phosphorylations on Thr-325 and Thr-331 through promoting docking of MAPK to the DEF domain. Phosphorylation on Thr-232, induced by HA-RAS, activates the transcriptional activity and antagonizes sumoylation. Phosphorylation on Ser-362 by RSK2 in osteoblasts contributes to osteoblast transformation (By similarity). {ECO:0000250}.; PTM: Constitutively sumoylated with SUMO1, SUMO2 and SUMO3. Desumoylated by SENP2. Sumoylation requires heterodimerization with JUN and is enhanced by mitogen stimulation. Sumoylation inhibits the AP-1 transcriptional activity and is, itself, inhibited by Ras-activated phosphorylation on Thr-232 (By similarity). {ECO:0000250}.; PTM: In quiescent cells, the small amount of FOS present is phosphorylated at Tyr-10 and Tyr-30 by SRC. This Tyr-phosphorylated form is cytosolic. In growing cells, dephosphorylated by PTPN2. Dephosphorylation leads to the association with endoplasmic reticulum membranes and activation of phospholipid synthesis. {ECO:0000269|PubMed:12134156, ECO:0000269|PubMed:12972619, ECO:0000269|PubMed:15719069}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}. Endoplasmic reticulum {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Note=In quiescent cells, present in very small amounts in the cytosol. Following induction of cell growth, first localizes to the endoplasmic reticulum and only later to the nucleus. Localization at the endoplasmic reticulum requires dephosphorylation at Tyr-10 and Tyr-30 (By similarity). {ECO:0000250}. SUBUNIT: Heterodimer; with JUN (By similarity). Interacts with MAFB. Component of the SMAD3/SMAD4/JUN/FOS complex required for synergistic TGF-beta-mediated transcription at the AP1 promoter site. Interacts with SMAD3; the interaction is weak even on TGF-beta activation. Interacts with MAFB (By similarity). Interacts with DSIPI; this interaction inhibits the binding of active AP1 to its target DNA. Interacts with CDS1 and PI4K2A, but not with CDIPT, nor PI4K2B. {ECO:0000250, ECO:0000269|PubMed:11397794, ECO:0000269|PubMed:22105363}. +Q64732 FOXB1_MOUSE Forkhead box protein B1 (Transcription factor FKH-5) 325 35,008 Chain (1); DNA binding (1); Sequence conflict (2) SUBCELLULAR LOCATION: Nucleus. +O88621 FOXH1_MOUSE Forkhead box protein H1 (Forkhead activin signal transducer 1) (Fast-1) (Forkhead activin signal transducer 2) (Fast-2) 401 44,001 Alternative sequence (1); Chain (1); Compositional bias (2); DNA binding (1); Motif (3); Region (1); Sequence conflict (10) FUNCTION: Transcriptional activator. Recognizes and binds to the DNA sequence 5'-TGT[GT][GT]ATT-3'. Required for induction of the goosecoid (GSC) promoter by TGF-beta or activin signaling. Forms a transcriptionally active complex containing FOXH1/SMAD2/SMAD4 on a site on the GSC promoter called TARE (TGF-beta/activin response element). {ECO:0000269|PubMed:10349617, ECO:0000269|PubMed:9702197, ECO:0000269|PubMed:9858566, ECO:0000269|Ref.4}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with the MH2 domains of SMAD2 and SMAD3. {ECO:0000269|PubMed:10349617}. DOMAIN: The FM region is required for binding SMAD2/SMAD4 complexes. FM2 is more effective than FM1 and only interacts with phosphorylated SMAD2 that is in an activated SMAD complex (By similarity). {ECO:0000250}. +A3KGK3 FR1L4_MOUSE Fer-1-like protein 4 1992 223,891 Alternative sequence (2); Chain (1); Compositional bias (3); Domain (5); Erroneous gene model prediction (1); Erroneous termination (1); Topological domain (2); Transmembrane (1) TRANSMEM 1953 1973 Helical. {ECO:0000255}. TOPO_DOM 1 1952 Extracellular. {ECO:0000255}.; TOPO_DOM 1974 1992 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +P29391 FRIL1_MOUSE Ferritin light chain 1 (Ferritin L subunit 1) 183 20,802 Chain (1); Domain (1); Helix (6); Metal binding (5); Sequence conflict (2); Turn (1) FUNCTION: Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney. {ECO:0000269|PubMed:19154717}. SUBUNIT: Oligomer of 24 subunits. There are two types of subunits: L (light) chain and H (heavy) chain. The major chain can be light or heavy, depending on the species and tissue type. The functional molecule forms a roughly spherical shell with a diameter of 12 nm and contains a central cavity into which the insoluble mineral iron core is deposited. +P49945 FRIL2_MOUSE Ferritin light chain 2 (Ferritin L subunit 2) (Ferritin subunit LG) 183 20,843 Chain (1); Domain (1); Metal binding (5) FUNCTION: Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney. {ECO:0000269|PubMed:19154717}. SUBUNIT: Oligomer of 24 subunits. There are two types of subunits: L (light) chain and H (heavy) chain. The major chain can be light or heavy, depending on the species and tissue type. The functional molecule forms a roughly spherical shell with a diameter of 12 nm and contains a central cavity into which the insoluble mineral iron core is deposited. +Q9R1E0 FOXO1_MOUSE Forkhead box protein O1 (Forkhead box protein O1A) (Forkhead in rhabdomyosarcoma) 652 69,518 Chain (1); Compositional bias (3); DNA binding (1); Modified residue (21); Motif (2); Mutagenesis (37); Region (4); Sequence conflict (1); Site (3) FUNCTION: Transcription factor that is the main target of insulin signaling and regulates metabolic homeostasis in response to oxidative stress. Binds to the insulin response element (IRE) with consensus sequence 5'-TT[G/A]TTTTG-3' and the related Daf-16 family binding element (DBE) with consensus sequence 5'-TT[G/A]TTTAC-3'. Activity suppressed by insulin. Main regulator of redox balance and osteoblast numbers and controls bone mass. Orchestrates the endocrine function of the skeleton in regulating glucose metabolism. Acts synergistically with ATF4 to suppress osteocalcin/BGLAP activity, increasing glucose levels and triggering glucose intolerance and insulin insensitivity. Also suppresses the transcriptional activity of RUNX2, an upstream activator of osteocalcin/BGLAP. In hepatocytes, promotes gluconeogenesis by acting together with PPARGC1A and CEBPA to activate the expression of genes such as IGFBP1, G6PC and PCK1. Important regulator of cell death acting downstream of CDK1, PKB/AKT1 and STK4/MST1. Promotes neural cell death. Mediates insulin action on adipose tissue. Regulates the expression of adipogenic genes such as PPARG during preadipocyte differentiation and, adipocyte size and adipose tissue-specific gene expression in response to excessive calorie intake. Regulates the transcriptional activity of GADD45A and repair of nitric oxide-damaged DNA in beta-cells. Required for the autophagic cell death induction in response to starvation or oxidative stress in a transcription-independent manner. Mediates the function of MLIP in cardiomyocytes hypertrophy and cardiac remodeling (By similarity). {ECO:0000250|UniProtKB:G3V7R4, ECO:0000269|PubMed:12754525, ECO:0000269|PubMed:15184386, ECO:0000269|PubMed:15220471, ECO:0000269|PubMed:16917544, ECO:0000269|PubMed:17090532, ECO:0000269|PubMed:17627282, ECO:0000269|PubMed:17681146, ECO:0000269|PubMed:20519497, ECO:0000269|PubMed:20668652, ECO:0000269|PubMed:21196578, ECO:0000269|PubMed:21335550, ECO:0000269|PubMed:21471200, ECO:0000269|PubMed:22298775, ECO:0000269|PubMed:22417654, ECO:0000269|PubMed:22510882}. PTM: Phosphorylation by NLK promotes nuclear export and inhibits the transcriptional activity. In response to growth factors, phosphorylation on Thr-24, Ser-253 and Ser-319 by PKB/AKT1 promotes nuclear export and inactivation of transactivational activity. Phosphorylation on Thr-24 is required for binding 14-3-3 proteins. Phosphorylation of Ser-253 decreases DNA-binding activity and promotes the phosphorylation of Thr-24 and Ser-316, permitting phosphorylation of Ser-319 and Ser-322, probably by CDK1, leading to nuclear exclusion and loss of function. Stress signals, such as response to oxygen or nitric oxide, attenuate the PKB/AKT1-mediated phosphorylation leading to nuclear retention. Phosphorylation of Ser-326 is independent of IGF1 and leads to reduced function. Dephosphorylated on Thr-24 and Ser-253 by PP2A in beta-cells under oxidative stress leading to nuclear retention (By similarity). Phosphorylation of Ser-246 by CDK1 disrupts binding of 14-3-3 proteins leading to nuclear accumulation and has no effect on DNA-binding nor transcriptional activity. Phosphorylation by STK4/MST1 on Ser-209, upon oxidative stress, inhibits binding to 14-3-3 proteins and nuclear export. {ECO:0000250, ECO:0000269|PubMed:10347145, ECO:0000269|PubMed:16076959, ECO:0000269|PubMed:19965929, ECO:0000269|PubMed:20519497}.; PTM: Ubiquitinated by SRT2. Ubiquitination leads to proteasomal degradation (By similarity). {ECO:0000250}.; PTM: Methylation inhibits PKB/AKT1-mediated phosphorylation at Ser-253, promoting nuclear retention and increasing the transcriptional activity and cell death. Methylation increased by oxidative stress. {ECO:0000269|PubMed:10347145, ECO:0000269|PubMed:16076959, ECO:0000269|PubMed:18951090, ECO:0000269|PubMed:19965929, ECO:0000269|PubMed:20519497}.; PTM: Acetylation at Lys-259 and Lys-271 are necessary for autophagic cell death induction. Deacetylated by SIRT2 in response to oxidative stress or serum deprivation, thereby negatively regulating FOXO1-mediated autophagic cell death (By similarity). Once in the nucleus, acetylated by CREBBP/EP300. Acetylation diminishes the interaction with target DNA and attenuates the transcriptional activity. It increases the phosphorylation at Ser-253, and is required for the transcriptional inhibition by FCOR. Deacetylation by SIRT1 results in reactivation of the transcriptional activity (PubMed:17090532). Acetylation of FOXO1 diminishes its binding to PPARG in adipocytes. Deacetylated by SIRT2; deacetylation of FOXO1 directly increases its repressive binding to PPARG and inhibits adipocyte differentiation. Oxidative stress by hydrogen peroxide treatment appears to promote deacetylation and uncoupling of insulin-induced phosphorylation. By contrast, resveratrol acts independently of acetylation. {ECO:0000250, ECO:0000269|PubMed:10347145, ECO:0000269|PubMed:15220471, ECO:0000269|PubMed:16076959, ECO:0000269|PubMed:17090532, ECO:0000269|PubMed:17681146, ECO:0000269|PubMed:19037106, ECO:0000269|PubMed:19965929, ECO:0000269|PubMed:20519497, ECO:0000269|PubMed:21196578}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18388859, ECO:0000269|PubMed:21317886}. Nucleus {ECO:0000269|PubMed:17627282, ECO:0000269|PubMed:18388859, ECO:0000269|PubMed:21317886}. Note=Shuttles between the cytoplasm and nucleus. Largely nuclear in unstimulated cells. In osteoblasts, colocalizes with ATF4 and RUNX2 in the nucleus (By similarity). Insulin-induced phosphorylation at Ser-253 by PKB/AKT1 leads, via stimulation of Thr-24 phosphorylation, to binding of 14-3-3 proteins and nuclear export to the cytoplasm where it is degraded by the ubiquitin-proteosomal pathway. Phosphorylation at Ser-249 by CDK1 disrupts binding of 14-3-3 proteins and promotes nuclear accumulation. Phosphorylation by NLK results in nuclear export. Translocates to the nucleus upon oxidative stress-induced phosphorylation at Ser-212 by STK4/MST1. SGK1-mediated phosphorylation also results in nuclear translocation. Retained in the nucleus under stress stimuli including oxidative stress, nutrient deprivation or nitric oxide. Methylated form is nuclear. {ECO:0000250}. SUBUNIT: Interacts with EP300 and CREBBP; the interactions acetylate FOXO1. Interacts with the 14-3-3 proteins, YWHAG and YWHAZ; the interactions require insulin-stimulated phosphorylation on Thr-24, promote nuclear exit and loss of transcriptional activity. Interacts with SKP2; the interaction ubiquitinates FOXO1 leading to its proteosomal degradation. Interacts with PMRT1; methylates FOXO1, prevents PKB/AKT1 phosphorylation and retains FOXO1 in the nucleus (By similarity). Interacts (via an N-terminal domain) with FCOR; the interaction is direct, occurs in a forskolin-independent manner and prevents SIRT1 binding to FOXO1. Interacts (via the C-terminal half) with ATF4 (via its DNA-binding domain); the interaction occurs in osteoblasts, regulates glucose homeostasis via suppression of beta-cell proliferation and subsequent decrease in insulin production. Interacts with RUNX2; the interaction inhibits RUNX2 transcriptional activity and mediates the IGF1/insulin-dependent BGLAP expression in osteoblasts. Interacts with PPP2R1A; the interaction regulates the dephosphorylation of FOXO1 at Thr-24 and Ser-253 leading to its nuclear import. Binds to CDK1. Interacts with LRPPRC. Interacts with RUNX2; the interaction inhibits RUNX2 transcriptional activity and mediates the IGF1/insulin-dependent BGLAP expression in osteoblasts. Interacts with NLK. Interacts with SIRT1; the interaction results in the deacetylation of FOXO1 leading to activation of FOXO1-mediated transcription of genes involved in DNA repair and stress resistance. The interaction requires the presence of KRIT1 and is inhibited by FCOR. Interacts with SIRT2; the interaction is disrupted in response to oxidative stress or serum deprivation, leading to increased level of acetylated FOXO1, which promotes stress-induced autophagy by stimulating E1-like activating enzyme ATG7. Interacts (acetylated form) with ATG7; the interaction is increased in response to oxidative stress or serum deprivation and promotes the autophagic process leading to cell death. Interacts (acetylated form) with PPARG (PubMed:12754525, PubMed:15220471, PubMed:16917544, PubMed:17050673, PubMed:17681146, PubMed:19037106, PubMed:20061393, PubMed:20668652, PubMed:21471200, PubMed:22298775, PubMed:22417654, PubMed:22510882). Interacts with XBP1 isoform 2; this interaction is direct and leads to FOXO1 ubiquitination and degradation via the proteasome pathway (PubMed:21317886). Interacts (via the Fork-head domain) with CEBPA; the interaction increases when FOXO1 is deacetylated (PubMed:17090532, PubMed:17627282). Interacts with WDFY2 (PubMed:18388859). Forms a complex with WDFY2 and AKT1 (PubMed:18388859). {ECO:0000250|UniProtKB:Q12778, ECO:0000269|PubMed:12754525, ECO:0000269|PubMed:15220471, ECO:0000269|PubMed:16917544, ECO:0000269|PubMed:17050673, ECO:0000269|PubMed:17090532, ECO:0000269|PubMed:17627282, ECO:0000269|PubMed:17681146, ECO:0000269|PubMed:18388859, ECO:0000269|PubMed:19037106, ECO:0000269|PubMed:20061393, ECO:0000269|PubMed:20668652, ECO:0000269|PubMed:21317886, ECO:0000269|PubMed:21471200, ECO:0000269|PubMed:22298775, ECO:0000269|PubMed:22417654, ECO:0000269|PubMed:22510882}. TISSUE SPECIFICITY: Expressed in liver, white and brown adipose tissues (at protein level). {ECO:0000269|PubMed:17627282, ECO:0000269|PubMed:22510882}. +Q60687 FSHB_MOUSE Follitropin subunit beta (Follicle-stimulating hormone beta subunit) (FSH-B) (FSH-beta) (Follitropin beta chain) 130 14,919 Chain (1); Disulfide bond (6); Glycosylation (2); Signal peptide (1) FUNCTION: Together with the alpha chain CGA constitutes follitropin, the follicle-stimulating hormone, and provides its biological specificity to the hormone heterodimer. Binds FSHR, a G protein-coupled receptor, on target cells to activate downstream signaling pathways (By similarity). Follitropin is involved in follicle development and spermatogenesis in reproductive organs (PubMed:9020850, PubMed:11416011). {ECO:0000250|UniProtKB:P01225, ECO:0000269|PubMed:11416011, ECO:0000269|PubMed:9020850}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01225}. Note=Efficient secretion requires dimerization with CGA. {ECO:0000250|UniProtKB:P01225}. SUBUNIT: Heterodimer. The active follitropin is a heterodimer composed of an alpha chain/CGA shared with other hormones and a unique beta chain/FSHB shown here. {ECO:0000250|UniProtKB:P01225}. +P52927 HMGA2_MOUSE High mobility group protein HMGI-C (High mobility group AT-hook protein 2) 108 11,819 Chain (1); DNA binding (3); Initiator methionine (1); Modified residue (5); Region (1) FUNCTION: Functions as a transcriptional regulator. Functions in cell cycle regulation through CCNA2. Plays an important role in chromosome condensation during the meiotic G2/M transition of spermatocytes. Plays a role in postnatal myogenesis, is involved in satellite cell activation (PubMed:27446912). {ECO:0000269|PubMed:14668482, ECO:0000269|PubMed:27446912}. PTM: Regulated by cell cycle-dependent phosphorylation which alters its DNA binding affinity. Phosphorylated by NEK2. {ECO:0000269|PubMed:14668482}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14668482}. SUBUNIT: Interacts with E4F1 (By similarity). Interacts with NEK2 (PubMed:14668482). {ECO:0000250|UniProtKB:P52926, ECO:0000269|PubMed:14668482}. TISSUE SPECIFICITY: Expressed in mitotic spermatogonia, meiotic spermatocytes, and postmeiotic round spermatids (at protein level) (PubMed:14668482). Expressed in embryonic myogenic progenitor cells (PubMed:27446912). {ECO:0000269|PubMed:14668482, ECO:0000269|PubMed:27446912}. +Q99KR8 FUCO2_MOUSE Plasma alpha-L-fucosidase (EC 3.2.1.51) (Alpha-L-fucoside fucohydrolase 2) (Alpha-L-fucosidase 2) 461 53,645 Chain (1); Glycosylation (3); Modified residue (1); Sequence conflict (3); Signal peptide (1); Site (1) FUNCTION: Alpha-L-fucosidase is responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. SUBUNIT: Homotetramer. {ECO:0000250}. +Q6DIA9 FBX27_MOUSE F-box only protein 27 280 31,633 Alternative sequence (1); Chain (1); Domain (2) FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. Able to recognize and bind complex-type oligosaccharides. {ECO:0000250}. SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex. Interacts with SKP1 and CUL1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Detected in brain, heart and muscle. {ECO:0000269|PubMed:18203720}. +O70497 FCN2_MOUSE Ficolin-2 (Collagen/fibrinogen domain-containing protein 2) (Ficolin-B) (Ficolin-beta) (L-ficolin) 314 33,984 Chain (1); Disulfide bond (3); Domain (2); Glycosylation (1); Metal binding (4); Sequence conflict (1); Signal peptide (1) FUNCTION: May function in innate immunity through activation of the lectin complement pathway. Calcium-dependent and GlcNAc-binding lectin (By similarity). {ECO:0000250|UniProtKB:Q15485}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Homotrimer. Interacts with elastin. Interacts with MASP1 and MASP2. {ECO:0000250|UniProtKB:Q15485}. DOMAIN: The fibrinogen-like domain (FBG) contains calcium-binding sites that may be involved in carbohydrate binding. {ECO:0000250|UniProtKB:Q15485}. +Q5SUS0 FBW10_MOUSE F-box/WD repeat-containing protein 10 (F-box and WD-40 domain-containing protein 10) 1030 117,691 Alternative sequence (2); Chain (1); Coiled coil (1); Domain (1); Repeat (5); Sequence conflict (1) FUNCTION: Probable substrate-recognition component of a SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Overexpression is leading to degradation of CBX5 and CBX1 (By similarity). {ECO:0000250}. +Q9CPU7 FBX32_MOUSE F-box only protein 32 (Atrogin-1) (Muscle atrophy F-box protein) (MAFbx) 355 41,504 Chain (1); Domain (1); Motif (3) Protein modification; protein ubiquitination. FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Probably recognizes and binds to phosphorylated target proteins during skeletal muscle atrophy. Recognizes TERF1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q969P5}. Nucleus {ECO:0000250|UniProtKB:Q969P5}. Note=Shuttles between cytoplasm and the nucleus. {ECO:0000250|UniProtKB:Q969P5}. SUBUNIT: Part of the SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase complex SCF(FBXO32) formed of CUL1, SKP1, RBX1 and FBXO32. {ECO:0000250|UniProtKB:Q969P5}. TISSUE SPECIFICITY: Specifically expressed in cardiac and skeletal muscle. +Q6PDJ6 FBX42_MOUSE F-box only protein 42 717 77,777 Chain (1); Compositional bias (1); Domain (1); Modified residue (4); Repeat (4); Sequence conflict (3) FUNCTION: Substrate-recognition component of some SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. Specifically recognizes p53/TP53, promoting its ubiquitination and degradation (By similarity). {ECO:0000250}. SUBUNIT: Component of some SCF complex, composed of CUL1, SKP1, RBX1 and FBXO42. Interacts (via the kelch domain) with p53/TP53; interaction is direct (By similarity). {ECO:0000250}. +P20489 FCERA_MOUSE High affinity immunoglobulin epsilon receptor subunit alpha (Fc-epsilon RI-alpha) (FcERI) (IgE Fc receptor subunit alpha) 250 28,657 Chain (1); Disulfide bond (2); Domain (2); Glycosylation (6); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 205 223 Helical. {ECO:0000255}. TOPO_DOM 24 204 Extracellular. {ECO:0000255}.; TOPO_DOM 224 250 Cytoplasmic. {ECO:0000255}. FUNCTION: Binds to the Fc region of immunoglobulins epsilon. High affinity receptor. Responsible for initiating the allergic response. Binding of allergen to receptor-bound IgE leads to cell activation and the release of mediators (such as histamine) responsible for the manifestations of allergy. The same receptor also induces the secretion of important lymphokines. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SUBUNIT: Tetramer of an alpha chain, a beta chain, and two disulfide linked gamma chains. TISSUE SPECIFICITY: Expressed in bone marrow mast cells, as well as in the pineal gland at night. {ECO:0000269|PubMed:17728245}. +Q8R4Y0 FCRL1_MOUSE Fc receptor-like protein 1 (FcR-like protein 1) (FcRL1) (BXMAS1-like protein 1) (mBXMH1) (Fc receptor homolog 1) (FcRH1) (moFcRH1) (IFGP family protein 1) (mIFGP1) (CD antigen CD307a) 343 37,277 Alternative sequence (4); Chain (1); Disulfide bond (1); Domain (2); Glycosylation (2); Motif (5); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 220 240 Helical. {ECO:0000255}. TOPO_DOM 17 219 Extracellular. {ECO:0000255}.; TOPO_DOM 241 343 Cytoplasmic. {ECO:0000255}. FUNCTION: May function as an activating coreceptor in B-cells. May function in B-cells activation and differentiation (By similarity). {ECO:0000250}. PTM: Phosphorylated on tyrosines upon activation. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. Expressed in B-cells at the various stages of differentiation. {ECO:0000269|PubMed:12037601, ECO:0000269|PubMed:15302849}. +Q9CTH6 FCF1_MOUSE rRNA-processing protein FCF1 homolog 198 23,341 Chain (1); Domain (1); Erroneous termination (1) FUNCTION: Essential protein involved in pre-rRNA processing and 40S ribosomal subunit assembly. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. +Q68SN8 FCRL5_MOUSE Fc receptor-like protein 5 (FcR-like protein 5) (FcRL5) (BXMAS1-like protein 2) (mBXMH2) (Fc receptor homolog 3) (FcRH3) (moFcRH3) (CD antigen CD307e) 596 66,779 Alternative sequence (1); Chain (1); Disulfide bond (5); Domain (5); Erroneous initiation (1); Glycosylation (2); Sequence conflict (21); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 497 517 Helical. {ECO:0000255}. TOPO_DOM 27 496 Extracellular. {ECO:0000255}.; TOPO_DOM 518 596 Cytoplasmic. {ECO:0000255}. PTM: Phosphorylated on cytoplasmic tyrosines; required for interaction with protein tyrosine phosphatases and protein tyrosine kinases. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Interacts with PTPN6, PTPN11, SYK and ZAP70. {ECO:0000250}. TISSUE SPECIFICITY: Preferentially expressed in marginal zone B cells. {ECO:0000269|PubMed:15302849}. +Q9QXW0 FBXL6_MOUSE F-box/LRR-repeat protein 6 (F-box and leucine-rich repeat protein 6) (F-box protein FBL6) 535 59,268 Alternative sequence (2); Chain (1); Domain (1); Frameshift (1); Repeat (10) FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. {ECO:0000250}. SUBUNIT: Directly interacts with SKP1 and CUL1. {ECO:0000250}. +Q7TSG3 FBX5_MOUSE F-box only protein 5 (Early mitotic inhibitor 1) 421 47,508 Chain (1); Domain (1); Modified residue (1); Mutagenesis (4); Region (7); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: Regulator of APC activity during mitotic and meiotic cell cycle (PubMed:17190794, PubMed:15526037, PubMed:16809773). During mitotic cell cycle plays a role as both substrate and inhibitor of APC-FZR1 complex (PubMed:16809773). During G1 phase, plays a role as substrate of APC-FZR1 complex E3 ligase. Then switches as an inhibitor of APC-FZR1 complex during S and G2 leading to cell-cycle commitment. As APC inhibitor, prevents the degradation of APC substrates at multiple levels: by interacting with APC and blocking access of APC substrates to the D-box co-receptor, formed by FZR1 and ANAPC10; by suppressing ubiquitin ligation and chain elongation by APC by preventing the UBE2C and UBE2S activities. Plays a role in genome integrity preservation by coordinating DNA replication with mitosis through APC inhibition in interphase to stabilize CCNA2 and GMNN in order to promote mitosis and prevent rereplication and DNA damage-induced cellular senescence (By similarity). During oocyte maturation, plays a role in meiosis through inactivation of APC-FZR1 complex. Inhibits APC through RPS6KA2 interaction that increases FBXO5 affiniy for CDC20 leading to the metaphase arrest of the second meiotic division before fertilization (PubMed:15526037). Controls entry into the first meiotic division through inactivation of APC-FZR1 complex (PubMed:17190794). Promotes migration and osteogenic differentiation of mesenchymal stem cells (By similarity). {ECO:0000250|UniProtKB:Q9UKT4, ECO:0000269|PubMed:15526037, ECO:0000269|PubMed:16809773, ECO:0000269|PubMed:17190794}. PTM: Phosphorylation by CDK2 and subsequently by PLK1 triggers degradation during early mitosis through ubiquitin-mediated proteolysis by the SCF ubiquitin ligase complex containing the F-box protein BTRC. This degradation is necessary for the activation of APC in late mitosis and subsequent mitotic progression (By similarity). Phosphorylated by RPS6KA2; increases and stabilizes interaction with CDC20 (PubMed:15526037). {ECO:0000250|UniProtKB:Q9UKT4, ECO:0000269|PubMed:15526037}.; PTM: Ubiquitinated by the SCF(BTRC) complex following phosphorylation by PLK1. Undergoes both 'Lys-11' and 'Lys-48'-linked polyubiquitination by APC-FZR1 complex leading to degradation during G1 phase by the proteasome (By similarity). Degraded through the SCF(BTRC) complex; degradation occurs during oocyte maturation, between germinal vesicle breakdown (GVBD) and meiosis I, and is required for the meiosis I-meiosis II transition (PubMed:17190794). {ECO:0000250|UniProtKB:Q9UKT4, ECO:0000269|PubMed:17190794}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UKT4}. Cytoplasm {ECO:0000269|PubMed:15526037}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:15526037}. Note=In interphase, localizes in a punctate manner in the nucleus and cytoplasm with some perinuclear concentration. In mitotic cells, localizes throughout the cell, particularly at the spindle. {ECO:0000250|UniProtKB:Q9UKT4}. SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex. Interacts with BTRC; mediates proteolysis by the SCF ubiquitin ligase complex leading to activation of APC in late mitosis and subsequent mitotic progression. Interacts with FZR1/CDH1 and the N-terminal substrate-binding domain of CDC20; prevents APC activation. Also interacts with EVI5 which blocks its phosphorylation by PLK1 and prevents its subsequent binding to BTRC and degradation. Interacts simultaneously with anaphase promoting complex (APC), through at least ANAPC2, CDC23, CDC27, the APC substrate GMNN and the APC activator FZR1. Interacts with UBE2S; interferes with the activity of UBE2S mainly by disrupting the dynamic electrostatic association between the C-terminal tail of UBE2S and ANAPC2 (By similarity). Interacts with RPS6KA2; cooperates to induce the metaphase arrest of early blastomeres; increases and stabilizes interaction of FBXO5 with CDC20 (PubMed:15526037). {ECO:0000250|UniProtKB:Q9UKT4, ECO:0000269|PubMed:15526037}. TISSUE SPECIFICITY: Expressed in oocytes and granulosa cells (PubMed:15526037, PubMed:17190794). Expressed in proliferating cells compartments in hair follicle and skin epidermis, spermatogonia, and intestinal crypts (PubMed:17875940). {ECO:0000269|PubMed:15526037, ECO:0000269|PubMed:17190794, ECO:0000269|PubMed:17875940}. +Q9QZN4 FBX6_MOUSE F-box only protein 6 (F-box only protein 6b) (F-box protein that recognizes sugar chains 2) (F-box/G-domain protein 2) 295 34,493 Chain (1); Domain (2); Erroneous gene model prediction (3); Modified residue (3); Sequence conflict (8) Protein modification; protein ubiquitination. FUNCTION: Substrate-recognition component of some SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complexes. Involved in DNA damage response by specifically recognizing activated CHEK1 (phosphorylated on 'Ser-345'), promoting its ubiquitination and degradation. Ubiquitination of CHEK1 is required to insure that activated CHEK1 does not accumulate as cells progress through S phase, or when replication forks encounter transient impediments during normal DNA replication (By similarity). Involved in endoplasmic reticulum-associated degradation pathway (ERAD) for misfolded lumenal proteins by recognizing and binding sugar chains on unfolded glycoproteins that are retrotranslocated into the cytosol and promoting their ubiquitination and subsequent degradation. Able to recognize and bind denatured glycoproteins, which are modified with not only high-mannose but also complex-type oligosaccharides. Also recognizes sulfated glycans. {ECO:0000250, ECO:0000269|PubMed:12939278, ECO:0000269|PubMed:15723043}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with CHEK1 and CUL1 (By similarity). Part of a SCF (SKP1-cullin-F-box) protein ligase complex. Interacts with VCP. {ECO:0000250, ECO:0000269|PubMed:12939278, ECO:0000269|PubMed:15723043}. TISSUE SPECIFICITY: Present in liver and kidney (at protein level). Widely expressed. {ECO:0000269|PubMed:12939278, ECO:0000269|PubMed:18203720}. +Q8VBV4 FBXW7_MOUSE F-box/WD repeat-containing protein 7 (F-box and WD-40 domain-containing protein 7) (F-box protein FBW7) (F-box protein Fbxw6) (F-box-WD40 repeat protein 6) (SEL-10) 710 79,848 Alternative sequence (1); Chain (1); Domain (1); Modified residue (2); Repeat (7); Sequence conflict (4) FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:21953459, PubMed:22748924). Recognizes and binds phosphorylated sites/phosphodegrons within target proteins and thereafter bring them to the SCF complex for ubiquitination (PubMed:22748924). Mediates ubiquitination and subsequent degradation of CCNE1 and MYC (PubMed:22748924). Identified substrates include cyclin-E (CCNE1 or CCNE2), DISC1, JUN, MYC, NOTCH1 released notch intracellular domain (NICD), NOTCH2, MCL1 and probably PSEN1 (By similarity). Acts as a negative regulator of JNK signaling by binding to phosphorylated JUN and promoting its ubiquitination and subsequent degradation (By similarity). SCF(FBXW7) complex mediates the ubiquitination and subsequent degradation of NFE2L1 (PubMed:21953459). Involved in bone homeostasis and negative regulation of osteoclast differentiation (PubMed:29149593). {ECO:0000250|UniProtKB:Q969H0, ECO:0000269|PubMed:16141072, ECO:0000269|PubMed:21953459, ECO:0000269|PubMed:22748924, ECO:0000269|PubMed:29149593}. PTM: Phosphorylation at Thr-208 promotes interaction with PIN1, leading to disrupt FBXW7 dimerization and promoting FBXW7 autoubiquitination and degradation. {ECO:0000250|UniProtKB:Q969H0}.; PTM: Ubiquitinated: autoubiquitinates following phosphorylation at Thr-208 and subsequent interaction with PIN1 (By similarity). Ubiquitination leads to its proteasomal degradation (PubMed:22748924). {ECO:0000250|UniProtKB:Q969H0, ECO:0000269|PubMed:22748924}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:11461910}. SUBUNIT: Homodimer; homodimerization plays a role in substrate binding and/or ubiquitination and degradation (By similarity). Component of the SCF(FBXW7) complex consisting of CUL1, RBX1, SKP1 and FBXW7 (PubMed:11735228). Interacts (via F-box domain) with SKP1 (PubMed:11735228). Interacts (via F-box domain) with pseudophosphatase STYX; the interaction is direct and prevents FBXW7 interaction with SKP1 (By similarity). Interacts with cyclin-E (CCNE1 or CCNE2) (By similarity). Interacts with PSEN1 (By similarity). Forms a trimeric complex with NOTCH1 and SGK1 (By similarity). Interacts with NOTCH1 intracellular domain/NICD and NOTCH4 intracellular domain/NICD (PubMed:11425854, PubMed:11461910). Interacts with NOTCH2 intracellular domain (N2ICD) (By similarity). Interacts with MYC (when phosphorylated) (By similarity). Interacts with USP28, leading to counteract ubiquitination of MYC (By similarity). Interacts (when phosphorylated at Thr-127) with PIN1, leading to disrupt FBXW7 dimerization and promoting FBXW7 autoubiquitination and degradation (By similarity). Interacts with UBE2QL1 (By similarity). Interacts with FAM83D; promotes FBXW7 degradation (By similarity). Interacts with MYCN; FBXW7 competes with AURKA for binding to unphosphorylated MYCN but not for binding to phosphorylated MYCN (By similarity). Interacts with JUN (By similarity). Found in a complex with JUN and PRR7 (By similarity). Interacts with JUN and PRR7; the interaction inhibits ubiquitination-mediated JUN degradation promoting its phosphorylation and transcriptional activity (By similarity). Interacts with NFE2L1 (PubMed:21953459). {ECO:0000250|UniProtKB:Q969H0, ECO:0000269|PubMed:11425854, ECO:0000269|PubMed:11461910, ECO:0000269|PubMed:11735228, ECO:0000269|PubMed:21953459}. DOMAIN: The WD repeats mediate interaction with substrates of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex. {ECO:0000250|UniProtKB:Q969H0}.; DOMAIN: The F-box domain mediates interaction with SKP1. {ECO:0000250|UniProtKB:Q969H0}. TISSUE SPECIFICITY: Widely expressed with highest levels in brain, heart and testis. {ECO:0000269|PubMed:11735228}. +Q8BIA4 FBXW8_MOUSE F-box/WD repeat-containing protein 8 (F-box and WD-40 domain-containing protein 8) 598 67,956 Alternative sequence (1); Chain (1); Domain (1); Modified residue (3); Repeat (5); Sequence conflict (4) Protein modification; protein ubiquitination. FUNCTION: Substrate-recognition component of a Cul7-RING ubiquitin-protein ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. The Cul7-RING(FBXW8) complex mediates ubiquitination and consequent degradation of GORASP1, acting as a component of the ubiquitin ligase pathway that regulates Golgi morphogenesis and dendrite patterning in brain. The Cul7-RING(FBXW8) complex also mediates ubiquitination of MAP4K1/HPK1: recognizes and binds autophosphorylated MAP4K1/HPK1, leading to its degradation, thereby affecting cell proliferation and differentiation. Associated component of the 3M complex, suggesting that it mediates some of 3M complex functions (By similarity). {ECO:0000250|UniProtKB:Q8N3Y1}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P0DL28}. Golgi apparatus {ECO:0000250|UniProtKB:P0DL28}. Note=Colocalizes with CUL7 at the Golgi apparatus in neurons. {ECO:0000250|UniProtKB:P0DL28}. SUBUNIT: Part of a SCF-like complex consisting of CUL7, RBX1, SKP1, FBXW8 and GLMN. Interacts with OBSL1, CUL1, CUL2, SKP1, CCT6B, PFDN5, CCT2, CCT3, CCT6A, CCT7, VBP1, CCDC8, ARF1, TRIP13, PDCD5 and GORASP1. Interacts with MAP4K1/HPK1 (when autophosphorylated). Associated component of the 3M complex (By similarity). Interacts with CUL7. Interacts with POUF51 (when phosphorylated on 'Ser-347') (PubMed:29153991). {ECO:0000250, ECO:0000269|PubMed:16880526, ECO:0000269|PubMed:29153991}. TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in skeletal muscle, cartilage and lung. {ECO:0000269|PubMed:17998335}. +P49772 FLT3L_MOUSE Fms-related tyrosine kinase 3 ligand (Flt3 ligand) (Flt3L) (SL cytokine) 232 26,141 Alternative sequence (4); Chain (1); Disulfide bond (3); Glycosylation (2); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 190 210 Helical. {ECO:0000255}. TOPO_DOM 27 189 Extracellular. {ECO:0000255}.; TOPO_DOM 211 232 Cytoplasmic. {ECO:0000255}. FUNCTION: Stimulates the proliferation of early hematopoietic cells by activating FLT3. Synergizes well with a number of other colony stimulating factors and interleukins. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Isoform 3: Secreted. Note=Biologically active.; SUBCELLULAR LOCATION: Isoform 4: Secreted. Note=Inactive. SUBUNIT: Homodimer (soluble isoform). {ECO:0000250}. +Q8CF02 FM25C_MOUSE Protein FAM25C 89 9,235 Chain (1) +A2APV2 FMNL2_MOUSE Formin-like protein 2 (Protein Man) 1086 123,101 Alternative sequence (4); Chain (1); Compositional bias (1); Domain (3); Erroneous gene model prediction (1); Erroneous initiation (1); Initiator methionine (1); Lipidation (1); Modified residue (1); Sequence conflict (1) FUNCTION: Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the cortical actin filament dynamics (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. DOMAIN: The DAD domain regulates activation via by an autoinhibitory interaction with the GBD/FH3 domain. This autoinhibition is released upon competitive binding of an activated GTPase. The release of DAD allows the FH2 domain to then nucleate and elongate nonbranched actin filaments (By similarity). {ECO:0000250}. +Q61345 FOXD1_MOUSE Forkhead box protein D1 (Brain factor 2) (BF-2) (Forkhead-related protein FKHL8) (Forkhead-related transcription factor 4) (FREAC-4) (HFH-BF-2) 456 45,371 Chain (1); Compositional bias (10); DNA binding (1); Sequence conflict (1) FUNCTION: Transcription factor involved in regulation of gene expression in a variety of processes including formation of positional identity in the developing retina, regionalization of the optic chiasm, morphogenesis of the kidney, and neuralization of ectodermal cells (PubMed:15509772, PubMed:15634693, PubMed:9811586). Involved in transcriptional activation of PGF and C3 genes (By similarity). {ECO:0000250|UniProtKB:Q16676, ECO:0000269|PubMed:15509772, ECO:0000269|PubMed:15634693, ECO:0000269|PubMed:9811586}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089}. TISSUE SPECIFICITY: Predominantly expressed in the CNS and temporal half of the retina. Also expressed in the condensed head mesenchyme, metanephric blastema of the developing kidney, cortex of the adrenal gland, condensed mesenchyme at the base of the follicles of vibrassae and cartilage perichondrium of the developing vertebrate. +Q9D6K8 FUND2_MOUSE FUN14 domain-containing protein 2 (Hepatitis C virus core-binding protein 6) 151 16,564 Chain (1); Sequence conflict (2) +Q8CI03 FWCH1_MOUSE FLYWCH-type zinc finger-containing protein 1 673 77,096 Alternative sequence (2); Chain (1); Compositional bias (1); Cross-link (2); Frameshift (1); Modified residue (3); Sequence conflict (4); Zinc finger (5) SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q9WVR4 FXR2_MOUSE Fragile X mental retardation syndrome-related protein 2 673 73,743 Chain (1); Compositional bias (4); Domain (4); Modified residue (12) FUNCTION: RNA-binding protein. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with FMR1 (By similarity). Interacts with FXR1 (By similarity). Interacts with TDRD3 (By similarity). Interacts with HABP4 (By similarity). Interacts with CYFIP2 but not with CYFIP1 (PubMed:11438699). {ECO:0000250|UniProtKB:P51116, ECO:0000269|PubMed:11438699}. DOMAIN: The tandem Agenet-like domains preferentially recognize trimethylated histone peptides. {ECO:0000250}. +Q00422 GABPA_MOUSE GA-binding protein alpha chain (GABP subunit alpha) 454 51,344 Beta strand (8); Chain (1); DNA binding (1); Domain (1); Helix (16); Modified residue (1); Sequence conflict (1); Turn (4) FUNCTION: Transcription factor capable of interacting with purine rich repeats (GA repeats). SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Heterotetramer of two alpha and two beta subunits. TISSUE SPECIFICITY: Ubiquitous. +P58463 FOXP2_MOUSE Forkhead box protein P2 714 79,819 Alternative sequence (1); Chain (1); Compositional bias (1); DNA binding (1); Mutagenesis (5); Region (2); Sequence conflict (4); Zinc finger (1) FUNCTION: Transcriptional repressor that may play a role in the specification and differentiation of lung epithelium. May also play a role in developing neural, gastrointestinal and cardiovascular tissues. Can act with CTBP1 to synergistically repress transcription but CTPBP1 is not essential. Plays a role in synapse formation by regulating SRPX2 levels. {ECO:0000269|PubMed:14701752, ECO:0000269|PubMed:24179158}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Forms homodimers and heterodimers with FOXP1 and FOXP4. Dimerization is required for DNA-binding (By similarity). Interacts with CTBP1 (PubMed:14701752). Interacts with FOXP1 (By similarity). {ECO:0000250|UniProtKB:O15409, ECO:0000269|PubMed:14701752}. DOMAIN: The leucine-zipper is required for dimerization and transcriptional repression. {ECO:0000269|PubMed:14701752}. TISSUE SPECIFICITY: Highest expression in lung. Lower expression in spleen, skeletal muscle, brain, kidney and small intestine. +Q9DBY0 FOXP4_MOUSE Forkhead box protein P4 (Fork head-related protein-like A) (mFKHLA) 795 85,981 Alternative sequence (3); Chain (1); Compositional bias (2); Cross-link (2); DNA binding (1); Modified residue (3); Mutagenesis (1); Region (1); Sequence conflict (3); Zinc finger (1) FUNCTION: Transcriptional repressor that represses lung-specific expression. {ECO:0000269|PubMed:14701752}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255, ECO:0000305}. SUBUNIT: Forms homodimers and heterodimers with FOXP1 and FOXP2. Dimerization is required for DNA-binding. {ECO:0000269|PubMed:14701752}. DOMAIN: The leucine-zipper is required for dimerization and transcriptional repression. {ECO:0000269|PubMed:14701752}. TISSUE SPECIFICITY: Expressed in the adult heart, brain, spleen lung, liver, kidney and testes. {ECO:0000269|PubMed:12818433, ECO:0000269|PubMed:14516685}. +Q3UM89 FOXR2_MOUSE Forkhead box protein R2 (Forkhead box protein N6) 302 35,036 Chain (1); DNA binding (1) SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089}. +Q61574 FOXS1_MOUSE Forkhead box protein S1 (Forkhead-like 18 protein) (Forkhead-related transcription factor 10) (FREAC-10) (Transcription factor FKH-3) 329 35,567 Chain (1); DNA binding (1) FUNCTION: Transcriptional repressor that suppresses transcription from the FASLG, FOXO3 and FOXO4 promoters. May have a role in the organization of the testicular vasculature. {ECO:0000269|PubMed:18288644}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089, ECO:0000269|PubMed:18288644}. +A2ACJ2 FP100_MOUSE Fanconi anemia core complex-associated protein 100 (Fanconi anemia-associated protein of 100 kDa) 879 94,281 Chain (1); Erroneous initiation (2); Frameshift (1); Sequence conflict (2) FUNCTION: Plays a role in Fanconi anemia-associated DNA damage response network. Regulates FANCD2 monoubiquitination and the stability of the FA core complex. Induces chromosomal instability as well as hypersensitivity to DNA cross-linking agents, when repressed (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Belongs to the multisubunit FA complex composed of FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL/PHF9, FANCM, FAAP24 and FAAP100. Forms a subcomplex with FANCB and FANCL (By similarity). {ECO:0000250}. +Q684R7 FREM1_MOUSE FRAS1-related extracellular matrix protein 1 (Protein QBRICK) 2191 244,544 Alternative sequence (3); Chain (1); Disulfide bond (1); Domain (2); Erroneous initiation (1); Frameshift (1); Glycosylation (6); Motif (1); Mutagenesis (1); Repeat (12); Signal peptide (1) FUNCTION: Extracellular matrix protein that plays a role in epidermal differentiation and is required for epidermal adhesion during embryonic development. {ECO:0000269|PubMed:15345741}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000269|PubMed:15878328}. Note=Localizes at the basement membrane zone of embryonic epidermis and hair follicles. DOMAIN: The Calx-beta domain binds calcium with high affinity and undergo a major conformational shift upon binding. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in epidermis and hair follicles. Expressed in many developing epidermal appendages, including the whisker and sensory vibrissae, cranial and trunk hair follicles, meibomian glands, teeth, footpads, eyelash primordia and invaginating mammary glands. Limb expression localizes to sheets of dermal cells on the apical and basal surfaces of the digits but, unlike FRAS1, is excluded from the apical ectodermal ridge. Usually expressed at higher level in dermal cells underlying the differentiating epithelial components, especially underlying the epidermis of the head, limbs, and eyelids. Expression in the eyelid dermis is apparent as early as 13 dpc. Postnatal expression in the skin is limited to the dermal papillae. In the kidney, it is expressed from 12.5 dpc in the mesenchyme surrounding the branching ureteric tree, with a strong expression in the more proximal regions of these tubules rather than at the proliferating and branching ends of the ureteric buds. In hair follicle, it is selectively expressed in the vibrissal hair primordia during development. Preferentially expressed in the whisker pad epithelia of E12.5 embryos, in both the epithelial and mesenchymal cells of developing hair follicles. In the early stages of hair follicle development (i.e. stages 0-1), it is expressed in both hair placodes and dermal condensations. In stage 2, it is detected in dermal condensations and adjacent epithelia, but not in the upper region of the hair follicles. Expressed at the tip of developing hair follicles in the later stages (i.e. stages 3-5). {ECO:0000269|PubMed:15345741, ECO:0000269|PubMed:15878328}. DISEASE: Note=Defects in Frem1 are the cause of head blebs (heb) which is a spontaneous mutation that is characterized by absent or malformed eyes, which are often open at birth. Cryptophthalmos is noted in all heb homozygous animals, as is occasional hindlimb polydactyly. {ECO:0000269|PubMed:15345741}. +A2AKB4 FRPD1_MOUSE FERM and PDZ domain-containing protein 1 1549 169,208 Chain (1); Domain (2); Region (1); Sequence conflict (14) FUNCTION: Stabilizes membrane-bound GPSM1, and thereby promotes its interaction with GNAI1. {ECO:0000250|UniProtKB:Q5SYB0}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q5SYB0}. Cell membrane {ECO:0000250|UniProtKB:Q5SYB0}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q5SYB0}; Cytoplasmic side {ECO:0000250|UniProtKB:Q5SYB0}. Note=Found both in the cytoplasm and associated with the cell membrane. {ECO:0000250|UniProtKB:Q5SYB0}. SUBUNIT: Interacts with GPSM1 (By similarity). Interacts with GPSM2 (PubMed:23318951). {ECO:0000250|UniProtKB:Q5SYB0, ECO:0000269|PubMed:23318951}. +Q8C456 FRITZ_MOUSE WD repeat-containing and planar cell polarity effector protein fritz homolog (mFrtz) (Homolog-13) (WD repeat-containing and planar cell polarity effector protein) 722 81,731 Alternative sequence (1); Chain (1); Compositional bias (1); Repeat (2); Sequence conflict (1) FUNCTION: Probable effector of the planar cell polarity signaling pathway which regulates the septin cytoskeleton in both ciliogenesis and collective cell movements. Together with FUZ and WDPCP proposed to function as core component of the CPLANE (ciliogenesis and planar polarity effectors) complex involved in the recruitment of peripheral IFT-A proteins to basal bodies (PubMed:27158779). {ECO:0000250|UniProtKB:Q32NR9, ECO:0000305|PubMed:27158779}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q32NR9}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q32NR9}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q32NR9}. SUBUNIT: Interacts with CPLANE1. Interacts with INTU and FUZ; FUZ, INTU and WDPCP probably form the core CPLANE (ciliogenesis and planar polarity effectors) complex. {ECO:0000269|PubMed:27158779}. +Q8C0V9 FRMD6_MOUSE FERM domain-containing protein 6 622 71,652 Alternative sequence (5); Chain (1); Compositional bias (2); Domain (1); Modified residue (5); Sequence conflict (2) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Can colocalize with actin. {ECO:0000250}. +P63158 HMGB1_MOUSE High mobility group protein B1 (High mobility group protein 1) (HMG-1) 215 24,894 Chain (1); Compositional bias (1); DNA binding (2); Disulfide bond (1); Helix (6); Modified residue (26); Motif (2); Region (8); Sequence conflict (2); Site (2) FUNCTION: Multifunctional redox sensitive protein with various roles in different cellular compartments. In the nucleus is one of the major chromatin-associated non-histone proteins and acts as a DNA chaperone involved in replication, transcription, chromatin remodeling, V(D)J recombination, DNA repair and genome stability. Proposed to be an universal biosensor for nucleic acids. Promotes host inflammatory response to sterile and infectious signals and is involved in the coordination and integration of innate and adaptive immune responses. In the cytoplasm functions as sensor and/or chaperone for immunogenic nucleic acids implicating the activation of TLR9-mediated immune responses, and mediates autophagy. Acts as danger associated molecular pattern (DAMP) molecule that amplifies immune responses during tissue injury. Released to the extracellular environment can bind DNA, nucleosomes, IL-1 beta, CXCL12, AGER isoform 2/sRAGE, lipopolysaccharide (LPS) and lipoteichoic acid (LTA), and activates cells through engagement of multiple surface receptors. In the extracellular compartment fully reduced HMGB1 (released by necrosis) acts as a chemokine, disulfide HMGB1 (actively secreted) as a cytokine, and sulfonyl HMGB1 (released from apoptotic cells) promotes immunological tolerance (PubMed:23519706, PubMed:23446148, PubMed:23994764, PubMed:25048472). Has proangiogenic activity (PubMed:16365390). May be involved in platelet activation. Binds to phosphatidylserine and phosphatidylethanolamide. Bound to RAGE mediates signaling for neuronal outgrowth. May play a role in accumulation of expanded polyglutamine (polyQ) proteins (By similarity). {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P10103, ECO:0000250|UniProtKB:P12682, ECO:0000250|UniProtKB:P63159, ECO:0000269|PubMed:16365390, ECO:0000305|PubMed:23446148, ECO:0000305|PubMed:23519706, ECO:0000305|PubMed:23994764, ECO:0000305|PubMed:25048472}.; FUNCTION: Nuclear functions are attributed to fully reduced HGMB1. Associates with chromatin and binds DNA with a preference to non-canonical DNA structures such as single-stranded DNA, DNA-containing cruciforms or bent structures, supercoiled DNA and ZDNA. Can bent DNA and enhance DNA flexibility by looping thus providing a mechanism to promote activities on various gene promoters by enhancing transcription factor binding and/or bringing distant regulatory sequences into close proximity. May be involved in nucleotide excision repair (NER), mismatch repair (MMR) and base excision repair (BER) pathways, and double strand break repair such as non-homologous end joining (NHEJ) (PubMed:17803946, PubMed:18650382). Involved in V(D)J recombination by acting as a cofactor of the RAG complex: acts by stimulating cleavage and RAG protein binding at the 23 bp spacer of conserved recombination signal sequences (RSS). In vitro can displace histone H1 from highly bent DNA. Can restructure the canonical nucleosome leading to relaxation of structural constraints for transcription factor-binding (By similarity). Enhances binding of sterol regulatory element-binding proteins (SREBPs) such as SREBF1 to their cognate DNA sequences and increases their transcriptional activities (PubMed:16040616). Facilitates binding of TP53 to DNA (By similarity). Proposed to be involved in mitochondrial quality control and autophagy in a transcription-dependent fashion implicating HSPB1; however, this function has been questioned (PubMed:21641551, PubMed:24606906). Can modulate the activity of the telomerase complex and may be involved in telomere maintenance (PubMed:22544226). {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P10103, ECO:0000250|UniProtKB:P63159, ECO:0000269|PubMed:16040616, ECO:0000269|PubMed:17803946, ECO:0000269|PubMed:18650382, ECO:0000269|PubMed:21641551, ECO:0000269|PubMed:22544226, ECO:0000269|PubMed:24606906}.; FUNCTION: In the cytoplasm proposed to dissociate the BECN1:BCL2 complex via competitive interaction with BECN1 leading to autophagy activation (PubMed:21395369). Can protect BECN1 and ATG5 from calpain-mediated cleavage and thus proposed to control their proautophagic and proapoptotic functions and to regulate the extent and severity of inflammation-associated cellular injury (PubMed:25642769). In myeloid cells has a protective role against endotoxemia and bacterial infection by promoting autophagy (PubMed:24302768). Involved in endosomal translocation and activation of TLR9 in response to CpG-DNA in macrophages (PubMed:17548579). {ECO:0000250|UniProtKB:P09429, ECO:0000269|PubMed:17548579, ECO:0000269|PubMed:20819940, ECO:0000269|PubMed:21395369, ECO:0000269|PubMed:24302768, ECO:0000269|PubMed:25642769}.; FUNCTION: In the extracellular compartment (following either active secretion or passive release) involved in regulation of the inflammatory response. Fully reduced HGMB1 (which subsequently gets oxidized after release) in association with CXCL12 mediates the recruitment of inflammatory cells during the initial phase of tissue injury; the CXCL12:HMGB1 complex triggers CXCR4 homodimerization (PubMed:22370717). Induces the migration of monocyte-derived immature dendritic cells and seems to regulate adhesive and migratory functions of neutrophils implicating AGER/RAGE and ITGAM (PubMed:17268551). Can bind to various types of DNA and RNA including microbial unmethylated CpG-DNA to enhance the innate immune response to nucleic acids. Proposed to act in promiscuous DNA/RNA sensing which cooperates with subsequent discriminative sensing by specific pattern recognition receptors (PubMed:19890330). Promotes extracellular DNA-induced AIM2 inflammasome activation implicating AGER/RAGE. Disulfide HMGB1 binds to transmembrane receptors, such as AGER/RAGE, TLR2, TLR4 and probably TREM1, thus activating their signal transduction pathways (PubMed:17568691, PubMed:19264983, PubMed:21419643). Mediates the release of cytokines/chemokines such as TNF, IL-1, IL-6, IL-8, CCL2, CCL3, CCL4 and CXCL10 (PubMed:12110890, PubMed:17548579). Promotes secretion of interferon-gamma by macrophage-stimulated natural killer (NK) cells in concert with other cytokines like IL-2 or IL-12. TLR4 is proposed to be the primary receptor promoting macrophage activation and signaling through TLR4 seems to implicate LY96/MD-2. In bacterial LPS- or LTA-mediated inflammatory responses binds to the endotoxins and transfers them to CD14 for signaling to the respective TLR4:LY96 and TLR2 complexes (By similarity). Contributes to tumor proliferation by association with ACER/RAGE (By similarity). Can bind to IL1-beta and signals through the IL1R1:IL1RAP receptor complex (By similarity). Binding to class A CpG activates cytokine production in plasmacytoid dendritic cells implicating TLR9, MYD88 and AGER/RAGE and can activate autoreactive B cells. Via HMGB1-containing chromatin immune complexes may also promote B cell responses to endogenous TLR9 ligands through a B-cell receptor (BCR)-dependent and ACER/RAGE-independent mechanism (By similarity). Inhibits phagocytosis of apoptotic cells by macrophages; the function is dependent on poly-ADP-ribosylation and involves binding to phosphatidylserine on the cell surface of apoptotic cells (PubMed:22204001, PubMed:18768881). In adaptive immunity may be involved in enhancing immunity through activation of effector T-cells and suppression of regulatory T (TReg) cells (PubMed:21419643). In contrast, without implicating effector or regulatory T-cells, required for tumor infiltration and activation of T-cells expressing the lymphotoxin LTA:LTB heterotrimer thus promoting tumor malignant progression (PubMed:23108142). Also reported to limit proliferation of T-cells (By similarity). Released HMGB1:nucleosome complexes formed during apoptosis can signal through TLR2 to induce cytokine production (By similarity). Involved in induction of immunological tolerance by apoptotic cells; its pro-inflammatory activities when released by apoptotic cells are neutralized by reactive oxygen species (ROS)-dependent oxidation specifically on Cys-106 (By similarity). During macrophage activation by activated lymphocyte-derived self apoptotic DNA (ALD-DNA) promotes recruitment of ALD-DNA to endosomes (PubMed:25660970). {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P10103, ECO:0000250|UniProtKB:P63159, ECO:0000269|PubMed:12110890, ECO:0000269|PubMed:17268551, ECO:0000269|PubMed:17568691, ECO:0000269|PubMed:18768881, ECO:0000269|PubMed:19264983, ECO:0000269|PubMed:21419643, ECO:0000269|PubMed:22204001, ECO:0000269|PubMed:22370717, ECO:0000269|PubMed:23108142, ECO:0000269|PubMed:25660970, ECO:0000305|PubMed:19890330}. PTM: Acetylated on multiple sites upon stimulation with LPS (By similarity). Acetylation on lysine residues in the nuclear localization signals (NLS 1 and NLS 2) leads to cytoplasmic localization and subsequent secretion. Acetylation on Lys-3 results in preferential binding to DNA ends and impairs DNA bending activity (By similarity). {ECO:0000250|UniProtKB:P10103, ECO:0000250|UniProtKB:P63159}.; PTM: Phosphorylated at serine residues (PubMed:17114460). Phosphorylation in both NLS regions is required for cytoplasmic translocation followed by secretion (By similarity). {ECO:0000250|UniProtKB:P09429, ECO:0000269|PubMed:17114460}.; PTM: Reduction/oxidation of cysteine residues Cys-23, Cys-45 and Cys-106 and a possible intramolecular disulfide bond involving Cys-23 and Cys-45 give rise to different redox forms with specific functional activities in various cellular compartments: 1- Fully reduced HGMB1 (HMGB1C23hC45hC106h), 2- Disulfide HMGB1 (HMGB1C23-C45C106h) and 3- Sulfonyl HMGB1 (HMGB1C23soC45soC106so). {ECO:0000269|PubMed:22105604}.; PTM: Poly-ADP-ribosylated by PARP1 when secreted following stimulation with LPS (PubMed:18768881, PubMed:22204001). {ECO:0000269|PubMed:18768881, ECO:0000269|PubMed:22204001}.; PTM: In vitro cleavage by CASP1 is liberating a HMG box 1-containing peptide which may mediate immunogenic activity; the peptide antagonizes apoptosis-induced immune tolerance (By similarity). Can be proteolytically cleaved by a thrombin:thrombomodulin complex; reduces binding to heparin and proinflammatory activities. {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P10103}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17114460, ECO:0000269|PubMed:20819940}. Cytoplasm {ECO:0000269|PubMed:17114460, ECO:0000269|PubMed:20819940}. Secreted {ECO:0000269|PubMed:22105604}. Chromosome {ECO:0000269|PubMed:12110890}. Cell membrane {ECO:0000269|PubMed:2461949}; Peripheral membrane protein {ECO:0000269|PubMed:2461949}; Extracellular side {ECO:0000269|PubMed:2461949}. Endosome {ECO:0000269|PubMed:19890330}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000305|PubMed:17548579}. Note=In basal state predominantly nuclear. Shuttles between the cytoplasm and the nucleus (PubMed:17114460). Translocates from the nucleus to the cytoplasm upon autophagy stimulation (PubMed:20819940). Release from macrophages in the extracellular milieu requires the activation of NLRC4 or NLRP3 inflammasomes (PubMed:20802146). Passively released to the extracellular milieu from necrotic cells by diffusion, involving the fully reduced form which subsequently gets oxidized (PubMed:12110890). Also released from apoptotic cells (PubMed:25660970). Actively secreted from a variety of immune and non-immune cells such as macrophages, monocytes, neutrophils, dendritic cells and natural killer cells in response to various stimuli, involving a nonconventional secretory process via secretory lysosomes (PubMed:17548579). Secreted by plasma cells in response to LPS (PubMed:21319304). Associated with the plasma membrane of filipodia in process-growing cells, and also deposited into the substrate-attached material (By similarity). Colocalizes with DDX58 on endosomal membranes (PubMed:19890330). {ECO:0000250|UniProtKB:P09429, ECO:0000269|PubMed:12110890, ECO:0000269|PubMed:17114460, ECO:0000269|PubMed:17548579, ECO:0000269|PubMed:19890330, ECO:0000269|PubMed:20802146, ECO:0000269|PubMed:20819940, ECO:0000269|PubMed:21319304, ECO:0000269|PubMed:22105604, ECO:0000269|PubMed:2461949, ECO:0000269|PubMed:25660970}. SUBUNIT: Interacts (fully reduced HMGB1) with CXCL12; probably in a 1:2 ratio involving two molecules of CXCL12, each interacting with one HMG box of HMGB1; inhibited by glycyrrhizin (PubMed:22370717). Associates with the TLR4:LY96 receptor complex (By similarity). Component of the RAG complex composed of core components RAG1 and RAG2, and associated component HMGB1 or HMGB2 (PubMed:9184213). Interacts (in cytoplasm upon starvation) with BECN1; inhibits the interaction of BECN1 and BCL2 leading to promotion of autophagy (PubMed:20819940). Interacts with KPNA1; involved in nuclear import (PubMed:17114460). Interacts with SREBF1, TLR2, TLR4, TLR9, APEX1, FEN1, POLB, TERT (PubMed:16040616, PubMed:16267105, PubMed:17548579, PubMed:17803946, PubMed:22544226). Interacts with AGER, PTPRZ1, IL1B, MSH2, XPA, XPC, HNF1A, TP53 (By similarity). Interacts with CD24; the probable CD24:SIGLEC10 complex is proposed to inhibit HGMB1-mediated tissue damage immune response (PubMed:19264983). Interacts with THBD; prevents HGMB1 interaction with ACER/RAGE and inhibits HGMB1 proinflammatory activity (By similarity). Interacts with HAVCR2; impairs HMGB1 binding to B-DNA and likely HMGB1-mediated innate immume response (PubMed:22842346). Interacts with XPO1; mediating nuclear export (By similarity). {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P10103, ECO:0000250|UniProtKB:P63159, ECO:0000269|PubMed:16040616, ECO:0000269|PubMed:16267105, ECO:0000269|PubMed:17114460, ECO:0000269|PubMed:17548579, ECO:0000269|PubMed:17803946, ECO:0000269|PubMed:19264983, ECO:0000269|PubMed:20819940, ECO:0000269|PubMed:22370717, ECO:0000269|PubMed:22544226, ECO:0000269|PubMed:22842346, ECO:0000269|PubMed:9184213}. DOMAIN: HMG box 2 mediates proinflammatory cytokine-stimulating activity and binding to TLR4. However, not involved in mediating immunogenic activity in the context of apoptosis-induced immune tolerance. {ECO:0000250|UniProtKB:P09429}.; DOMAIN: The acidic C-terminal domain forms a flexible structure which can reversibly interact intramolecularily with the HMG boxes and modulate binding to DNA and other proteins. {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P63159}. TISSUE SPECIFICITY: Serum levels are found elevated in mice with modeled systemic lupus erythematosus (SLE) and are correlated with SLE disease activity (PubMed:26078984). {ECO:0000269|PubMed:26078984}. +Q9QZN1 FXL17_MOUSE F-box/LRR-repeat protein 17 (F-box and leucine-rich repeat protein 17) (F-box only protein 13) 701 75,683 Alternative sequence (2); Chain (1); Compositional bias (5); Domain (1) FUNCTION: Substrate-recognition component of the SCF(FBXL17) E3 ubiquitin ligase complex, a key component of a quality control pathway required to ensure functional dimerization of BTB domain-containing proteins (dimerization quality control, DQC). FBXL17 specifically recognizes and binds a conserved degron of non-consecutive residues present at the interface of BTB dimers of aberrant composition: aberrant BTB dimer are then ubiquitinated by the SCF(FBXL17) complex and degraded by the proteaseome (By similarity). The ability of the SCF(FBXL17) complex to eliminate compromised BTB dimers is required for the differentiation and survival of neural crest and neuronal cells (By similarity). The SCF(FBXL17) complex mediates ubiquitination and degradation of BACH1 (By similarity). The SCF(FBXL17) complex is also involved in the regulation of the hedgehog/smoothened (Hh) signaling pathway by mediating the ubiquitination and degradation of SUFU, allowing the release of GLI1 from SUFU for proper Hh signal transduction (PubMed:27234298). The SCF(FBXL17) complex mediates ubiquitination and degradation of PRMT1 (PubMed:28883095). {ECO:0000250|UniProtKB:B1H1X1, ECO:0000250|UniProtKB:Q9UF56, ECO:0000269|PubMed:27234298, ECO:0000269|PubMed:28883095}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UF56}. Nucleus {ECO:0000250|UniProtKB:Q9UF56}. Note=Present in the cytoplasm and nucleus; more abundant in the cytoplasm. {ECO:0000250|UniProtKB:Q9UF56}. SUBUNIT: Part of the SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase complex SCF(FBXL17) composed of CUL1, SKP1, RBX1 and FBXL17. Interacts with BTB domain-containing proteins such as KLHL12, BCL6 and BACH1; specifically recognizes and binds a conserved degron of non-consecutive residues present at the interface of BTB dimers of aberrant composition. Interacts with SUFU (By similarity). Interacts with PRMT1 (PubMed:28883095). {ECO:0000250|UniProtKB:Q9UF56, ECO:0000269|PubMed:28883095}. +Q3TQB2 FXRD1_MOUSE FAD-dependent oxidoreductase domain-containing protein 1 (EC 1.-.-.-) 487 54,178 Alternative sequence (1); Chain (1); Compositional bias (1); Transmembrane (1) TRANSMEM 62 82 Helical. {ECO:0000255}. FUNCTION: Required for the assembly of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I). Involved in mid-late stages of complex I assembly. {ECO:0000250|UniProtKB:Q96CU9}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q96CU9}; Single-pass membrane protein {ECO:0000255}. SUBUNIT: Associates with components of the mitochondrial respiratory chain complex I. {ECO:0000250|UniProtKB:Q96CU9}. +Q3USW5 FXRD2_MOUSE FAD-dependent oxidoreductase domain-containing protein 2 665 76,004 Chain (1); Frameshift (1); Glycosylation (1); Motif (1); Sequence conflict (2); Signal peptide (1) FUNCTION: Probable flavoprotein which may function in endoplasmic reticulum associated degradation (ERAD). May bind non-native proteins in the endoplasmic reticulum and target them to the ubiquitination machinery for subsequent degradation (By similarity). {ECO:0000250}. PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138}. SUBUNIT: Interacts with SEL1L. May interact with OS9 and DNAJC10. Interacts with TXNDC16. {ECO:0000250|UniProtKB:Q8IWF2}. +Q61835 FXYD3_MOUSE FXYD domain-containing ion transport regulator 3 (Chloride conductance inducer protein Mat-8) (Mammary tumor 8 kDa protein) (Phospholemman-like) (Sodium/potassium-transporting ATPase subunit FXYD3) 88 9,526 Chain (1); Mutagenesis (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 39 59 Helical. {ECO:0000255}. TOPO_DOM 1 38 Extracellular. {ECO:0000255}.; TOPO_DOM 60 88 Cytoplasmic. {ECO:0000255}. FUNCTION: Associates with and regulates the activity of the sodium/potassium-transporting ATPase (NKA) which transports Na(+) out of the cell and K(+) into the cell (PubMed:15743908). Reduces glutathionylation of the NKA beta-1 subunit ATP1B1, thus reversing glutathionylation-mediated inhibition of ATP1B1 (By similarity). Induces a hyperpolarization-activated chloride current when expressed in Xenopus oocytes (By similarity). {ECO:0000250|UniProtKB:Q14802, ECO:0000269|PubMed:15743908}. PTM: Glutathionylated. {ECO:0000250|UniProtKB:Q14802}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000255}. SUBUNIT: Regulatory subunit of the sodium/potassium-transporting ATPase which is composed of a catalytic alpha subunit, a non-catalytic beta subunit and an additional regulatory subunit (PubMed:15743908). Interacts with catalytic alpha subunit ATP1A1 (PubMed:15743908). Also interacts with non-catalytic beta subunit ATP1B1 (PubMed:15743908). Interacts with the ATP1A1-ATP1B1, ATP1A2-ATP1B1 and ATP1A3-ATP1B1 NKA isozymes (By similarity). {ECO:0000250|UniProtKB:Q14802, ECO:0000269|PubMed:15743908}. TISSUE SPECIFICITY: Expressed at high levels in heart, skeletal muscle and liver with low levels of expression in breast, brain, lung, stomach and colon (PubMed:7836447). In the gastric gland, mainly expressed in the mucus cells forming the upper part of the gland and is absent from the parietal cells (PubMed:15743908). {ECO:0000269|PubMed:15743908, ECO:0000269|PubMed:7836447}. +P59648 FXYD7_MOUSE FXYD domain-containing ion transport regulator 7 80 8,487 Chain (1); Modified residue (1); Transmembrane (1) TRANSMEM 23 45 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q7TMC8 FUK_MOUSE L-fucose kinase (Fucokinase) (EC 2.7.1.52) 1090 119,267 Alternative sequence (1); Chain (1); Erroneous initiation (1); Nucleotide binding (1) FUNCTION: Takes part in the salvage pathway for reutilization of fucose from the degradation of oligosaccharides. {ECO:0000305|PubMed:14686921}.; FUNCTION: Isoform 1: Has strong fucokinase activity. {ECO:0000269|PubMed:14686921}.; FUNCTION: Isoform 2: Has very weak fucokinase activity. {ECO:0000269|PubMed:14686921}. TISSUE SPECIFICITY: Isoform 1: Expressed strongly in brain, ovary and testis, moderately in kidney and liver, and weakly in lung, spleen and heart. Isoform 2: Expressed very strongly in brain, strongly in ovary, testis and kidney, moderately in lung and liver, and weakly in heart and spleen. {ECO:0000269|PubMed:14686921}. +Q5F2L2 FUT10_MOUSE Alpha-(1,3)-fucosyltransferase 10 (EC 2.4.1.-) (Fucosyltransferase X) (Fuc-TX) (FucT-X) (Galactoside 3-L-fucosyltransferase 10) (Fucosyltransferase 10) 481 55,707 Alternative sequence (3); Chain (1); Glycosylation (4); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 9 31 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 8 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 32 481 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Probable fucosyltransferase. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed, with a higher expression in liver and thymus. {ECO:0000269|PubMed:12370785}. +Q9Z1T6 FYV1_MOUSE 1-phosphatidylinositol 3-phosphate 5-kinase (Phosphatidylinositol 3-phosphate 5-kinase) (EC 2.7.1.150) (FYVE finger-containing phosphoinositide kinase) (PIKfyve) (Phosphatidylinositol 3-phosphate 5-kinase type III) (PIPkin-III) (Type III PIP kinase) (p235) 2097 236,877 Alternative sequence (4); Chain (1); Compositional bias (1); Domain (2); Erroneous initiation (2); Frameshift (1); Initiator methionine (1); Modified residue (12); Region (1); Sequence conflict (7); Zinc finger (1) FUNCTION: The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Catalyzes the phosphorylation of phosphatidylinositol 3-phosphate on the fifth hydroxyl of the myo-inositol ring, to form phosphatidylinositol 3,5-bisphosphate. Required for endocytic-vacuolar pathway and nuclear migration. The product of the reaction it catalyzes functions as an important regulator of vacuole homeostasis perhaps by controlling membrane flux to and/or from the vacuole. {ECO:0000269|PubMed:19037259}. PTM: Phosphorylated in response to insulin at Ser-318 in a protein kinase B (PKB)-dependent manner. {ECO:0000269|PubMed:20513353}. SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:19037259}; Peripheral membrane protein {ECO:0000269|PubMed:19037259}. Endosome membrane {ECO:0000250}. Note=Associated with vesicle structures. Displays a peripheral vesicular punctate pattern. Mainly associated with membranes of the late endocytic pathway (By similarity). {ECO:0000250}. SUBUNIT: Component of the PI(3,5)P2 regulatory complex/PAS complex, at least composed of PIKFYVE, FIG4 and VAC14. VAC14 nucleates the assembly of the complex and serves as a scaffold. {ECO:0000269|PubMed:19037259}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:17956977}. +Q810H5 GALP_MOUSE Galanin-like peptide 117 12,773 Alternative sequence (1); Chain (1); Propeptide (1); Signal peptide (1) FUNCTION: Isoform 1: Hypothalamic neuropeptide which binds to the G-protein-coupled galanin receptors (GALR1, GALR2 and GALR3). Involved in a large number of putative physiological functions in CNS homeostatic processes, including the regulation of gonadotropin-releasing hormone secretion.; FUNCTION: Isoform 2: Exhibits antimicrobial activity against Gram-negative bacterias, inducing bacterial membrane blebbing (By similarity). Exhibits potent and dose-dependent vasoconstrictor and anti-edema activity in the cutaneous microvasculature, a physiologic effects which does not appear to be mediated via GALR1 or GALR2. {ECO:0000250, ECO:0000269|PubMed:12746327, ECO:0000269|PubMed:17535903}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. TISSUE SPECIFICITY: Isoform 2 is found in brain, thymus and skin. Isoform 2 is found in the skin, in pericytes covering microvascular arterioles and venules on their abluminal surfaces. In larger vessels, isoform 2 is expressed in layers of smooth muscle cells. Isoform 2 is not detected in endothelial cells. +Q8C102 GALT5_MOUSE Polypeptide N-acetylgalactosaminyltransferase 5 (EC 2.4.1.41) (Polypeptide GalNAc transferase 5) (GalNAc-T5) (pp-GaNTase 5) (Protein-UDP acetylgalactosaminyltransferase 5) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 5) 930 105,780 Binding site (6); Chain (1); Disulfide bond (5); Domain (1); Glycosylation (12); Metal binding (3); Modified residue (1); Region (2); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 13 35 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 12 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 36 930 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has activity toward EA2 peptide substrate, but has a weak activity toward Muc2 or Muc1b substrates (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. SUBUNIT: Interacts with EXT2. Does not interact with EXT1, EXTL1 or EXTL3 (By similarity). {ECO:0000250}. DOMAIN: There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding. {ECO:0000250}.; DOMAIN: The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity. {ECO:0000250}. TISSUE SPECIFICITY: Expressed at low level. Not expressed before E7.5 during embryogenesis. Expressed in dental mesenchyme and tongue. Accumulates in a subset of mesenchymal cells at the ventral-most portions of the E12.5 maxilla and mandible underlying the dental lamina. {ECO:0000269|PubMed:11159923}. +P61922 GABT_MOUSE 4-aminobutyrate aminotransferase, mitochondrial (EC 2.6.1.19) ((S)-3-amino-2-methylpropionate transaminase) (EC 2.6.1.22) (GABA aminotransferase) (GABA-AT) (Gamma-amino-N-butyrate transaminase) (GABA transaminase) (GABA-T) (L-AIBAT) 500 56,452 Alternative sequence (1); Binding site (2); Chain (1); Disulfide bond (1); Metal binding (2); Modified residue (10); Region (1); Transit peptide (1) FUNCTION: Catalyzes the conversion of gamma-aminobutyrate and L-beta-aminoisobutyrate to succinate semialdehyde and methylmalonate semialdehyde, respectively. Can also convert delta-aminovalerate and beta-alanine (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}. +Q9WVH4 FOXO3_MOUSE Forkhead box protein O3 672 71,064 Chain (1); Compositional bias (1); DNA binding (1); Modified residue (28); Motif (1); Mutagenesis (1); Region (2); Sequence caution (1) FUNCTION: Transcriptional activator (PubMed:23805378). Triggers apoptosis in the absence of survival factors, including neuronal cell death upon oxidative stress (By similarity). Recognizes and binds to the DNA sequence 5'-[AG]TAAA[TC]A-3' (By similarity). Participates in post-transcriptional regulation of MYC: following phosphorylation by MAPKAPK5, promotes induction of miR-34b and miR-34c expression, 2 post-transcriptional regulators of MYC that bind to the 3'UTR of MYC transcript and prevent its translation (By similarity). In response to metabolic stress, translocates into the mitochondria where it promotes mtDNA transcription (PubMed:23283301). {ECO:0000250|UniProtKB:O43524, ECO:0000269|PubMed:23283301, ECO:0000269|PubMed:23805378}. PTM: Deacetylation by SIRT1 or SIRT2 stimulates interaction of FOXO3 with SKP2 and facilitates SCF(SKP2)-mediated FOXO3 ubiquitination and proteasomal degradation (By similarity). Deacetylation by SIRT2 stimulates FOXO3-mediated transcriptional activity in response to oxidative stress (PubMed:17521387). Deacetylated by SIRT3 (By similarity). Deacetylation by SIRT3 stimulates FOXO3-mediated mtDNA transcriptional activity in response to metabolic stress (By similarity). {ECO:0000250|UniProtKB:O43524, ECO:0000269|PubMed:17521387}.; PTM: In the presence of survival factors such as IGF-1, phosphorylated on Thr-32 and Ser-252 by AKT1/PKB. This phosphorylated form then interacts with 14-3-3 proteins and is retained in the cytoplasm. Survival factor withdrawal induces dephosphorylation and promotes translocation to the nucleus where the dephosphorylated protein induces transcription of target genes and triggers apoptosis. Although AKT1/PKB doesn't appear to phosphorylate Ser-314 directly, it may activate other kinases that trigger phosphorylation at this residue. Phosphorylated by STK4/MST1 on Ser-208 upon oxidative stress, which leads to dissociation from YWHAB/14-3-3-beta and nuclear translocation. Phosphorylated by PIM1. Phosphorylation by AMPK leads to the activation of transcriptional activity without affecting subcellular localization. Phosphorylated by AMPK on Ser-30 in response to metabolic stress which mediates FOXO3 mitochondrial translocation (By similarity). Phosphorylation by MAPKAPK5 promotes nuclear localization and DNA-binding, leading to induction of miR-34b and miR-34c expression, 2 post-transcriptional regulators of MYC that bind to the 3'UTR of MYC transcript and prevent its translation. Phosphorylated by CHUK/IKKA and IKBKB/IKKB. TNF-induced inactivation of FOXO3 requires its phosphorylation at Ser-643 by IKBKB/IKKB which promotes FOXO3 retention in the cytoplasm, polyubiquitination and ubiquitin-mediated proteasomal degradation (By similarity). May be dephosphorylated by calcineurin A on Ser-298 which abolishes FOXO3 transcriptional activity (PubMed:23805378). {ECO:0000250|UniProtKB:O43524, ECO:0000269|PubMed:23805378}.; PTM: Heavily methylated by SET9 which decreases stability, while moderately increasing transcriptional activity. The main methylation site is Lys-270. Methylation doesn't affect subcellular location. {ECO:0000250|UniProtKB:O43524}.; PTM: Polyubiquitinated. Ubiquitinated by a SCF complex containing SKP2, leading to proteasomal degradation. {ECO:0000250|UniProtKB:O43524}.; PTM: The N-terminus is cleaved following import into the mitochondrion. {ECO:0000269|PubMed:29445193}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:23283301}. Nucleus {ECO:0000269|PubMed:23283301}. Mitochondrion matrix {ECO:0000269|PubMed:23283301, ECO:0000269|PubMed:29445193}. Mitochondrion outer membrane {ECO:0000269|PubMed:29445193}; Peripheral membrane protein {ECO:0000269|PubMed:29445193}; Cytoplasmic side {ECO:0000269|PubMed:29445193}. Note=Retention in the cytoplasm contributes to its inactivation (By similarity). Translocates to the nucleus upon oxidative stress and in the absence of survival factors (By similarity). Translocates in a AMPK-dependent manner into the mitochondrion in response to metabolic stress (PubMed:23283301, PubMed:29445193). {ECO:0000250|UniProtKB:O43524, ECO:0000269|PubMed:23283301, ECO:0000269|PubMed:29445193}. SUBUNIT: Upon metabolic stress, forms a complex composed of FOXO3, SIRT3 and mitochondrial RNA polymerase POLRMT; the complex is recruited to mtDNA in a SIRT3-dependent manner (PubMed:23283301). Also forms a complex composed of FOXO3, SIRT3, TFAM and POLRMT (By similarity). Interacts with SIRT2; the interaction occurs independently of SIRT2 deacetylase activity (PubMed:17521387). Interacts with YWHAB/14-3-3-beta and YWHAZ/14-3-3-zeta, which are required for cytosolic sequestration. Upon oxidative stress, interacts with STK4/MST1, which disrupts interaction with YWHAB/14-3-3-beta and leads to nuclear translocation. Interacts with PIM1. Interacts with DDIT3/CHOP. Interacts (deacetylated form) with SKP2. Interacts with CHUK and IKBKB (By similarity). Interacts with CAMK2A, CAMK2B and calcineurin A (PubMed:23805378). {ECO:0000250|UniProtKB:O43524, ECO:0000269|PubMed:17521387, ECO:0000269|PubMed:23283301, ECO:0000269|PubMed:23805378}. TISSUE SPECIFICITY: Expressed in white and brown adipose tissues (at protein level) (PubMed:22510882). Expressed in liver, kidney, lung and colon (at protein level) (PubMed:29445193). Expressed in skeletal muscles (at protein level) (PubMed:23283301). {ECO:0000269|PubMed:22510882, ECO:0000269|PubMed:23283301, ECO:0000269|PubMed:29445193}. +Q70KY4 FOXO6_MOUSE Forkhead box protein O6 559 57,595 Chain (1); Compositional bias (4); DNA binding (1); Modified residue (1); Mutagenesis (2) FUNCTION: Transcriptional activator. {ECO:0000269|PubMed:12857750}. PTM: Phosphorylation of Ser-184 is be important in regulating the transacriptional activity. {ECO:0000269|PubMed:12857750}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12857750}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089, ECO:0000269|PubMed:12857750}. Note=When phosphorylated, translocated from nucleus to cytoplasm. High nuclear localization after stimulation with growth factors. TISSUE SPECIFICITY: Expressed in brain in areas of the nucleus accumbens, cingulate cortex, parts of the amygdala and in the hippocampus. {ECO:0000269|PubMed:12857750}. +Q6PG16 HJURP_MOUSE Holliday junction recognition protein (Fetal liver expressing gene 1 protein homolog) (mFleg1) 667 74,199 Alternative sequence (2); Chain (1); Cross-link (1); Modified residue (9); Sequence conflict (33) FUNCTION: Centromeric protein that plays a central role in the incorporation and maintenance of histone H3-like variant CENPA at centromeres. Acts as a specific chaperone for CENPA and is required for the incorporation of newly synthesized CENPA molecules into nucleosomes at replicated centromeres. Prevents CENPA-H4 tetramerization and prevents premature DNA binding by the CENPA-H4 tetramer. Directly binds Holliday junctions. {ECO:0000250|UniProtKB:Q8NCD3}. SUBCELLULAR LOCATION: Nucleus, nucleolus. Chromosome, centromere. Note=Localizes in centromeres during late telophase and early G1, when CENPA nucleosomes are assembled. Localizes to nucleolus during S phase, nucleolus site being often related to storage (By similarity). {ECO:0000250}. SUBUNIT: Interacts with CENPA (via CATD domain); the interaction is direct and specific for CENPA since it does not interact with H3.1- or H3.3-containing nucleosomes. Heterotrimer composed of HJURP, CENPA and histone H4, where HJURP interacts with the dimer formed by CENPA and histone H4 and prevents tetramerization of CENPA and H4. Identified in a centromere complex containing histones H2A, H2B and H4, and at least CENPA, CENPB, CENPC, CENPT, CENPN, HJURP, SUPT16H, SSRP1 and RSF1. Interacts with 14-3-3 family members in a phosphorylation-dependent manner. Interacts with MSH5 and NBN. {ECO:0000250|UniProtKB:Q8NCD3}. +P58462 FOXP1_MOUSE Forkhead box protein P1 (Forkhead-related transcription factor 1) 705 78,833 Alternative sequence (4); Chain (1); Compositional bias (1); Cross-link (4); DNA binding (1); Modified residue (3); Mutagenesis (2); Region (2); Sequence conflict (6); Zinc finger (1) FUNCTION: Transcriptional repressor. Can act with CTBP1 to synergistically repress transcription but CTPBP1 is not essential (PubMed:11358962, PubMed:14701752). Plays an important role in the specification and differentiation of lung epithelium. Acts cooperatively with FOXP4 to regulate lung secretory epithelial cell fate and regeneration by restricting the goblet cell lineage program; the function may involve regulation of AGR2 (PubMed:11358962, PubMed:22675208). Essential transcriptional regulator of B-cell development (PubMed:16819554). Involved in regulation of cardiac muscle cell proliferation (PubMed:20713518). Involved in the columnar organization of spinal motor neurons. Promotes the formation of the lateral motor neuron column (LMC) and the preganglionic motor column (PGC) and is required for respective appropriate motor axon projections. The segment-appropriate generation of spinal chord motor columns requires cooperation with other Hox proteins (PubMed:18667151, PubMed:18662545). Can regulate PITX3 promoter activity; may promote midbrain identity in embryonic stem cell-derived dopamine neurons by regulating PITX3 (PubMed:20175877). Negatively regulates the differentiation of T follicular helper cells T(FH)s (PubMed:24859450). Involved in maintenance of hair follicle stem cell quiescence; the function probably involves regulation of FGF18 (PubMed:23946441). Represses transcription of various pro-apoptotic genes and cooperates with NF-kappa B-signaling in promoting B-cell expansion by inhibition of caspase-dependent apoptosis. Binds to CSF1R promoter elements and is involved in regulation of monocyte differentiation and macrophage functions; repression of CSF1R in monocytes seems to involve NCOR2 as corepressor. Involved in endothelial cell proliferation, tube formation and migration indicative for a role in angiogenesis; the role in neovascularization seems to implicate suppression of SEMA5B. Can negatively regulate androgen receptor signaling (By similarity). {ECO:0000250|UniProtKB:Q9H334, ECO:0000269|PubMed:14701752, ECO:0000269|PubMed:16819554, ECO:0000269|PubMed:18662545, ECO:0000269|PubMed:18667151, ECO:0000269|PubMed:20175877, ECO:0000269|PubMed:20713518, ECO:0000269|PubMed:22675208, ECO:0000269|PubMed:23946441, ECO:0000269|PubMed:24859450, ECO:0000305|PubMed:20175877, ECO:0000305|PubMed:22675208, ECO:0000305|PubMed:23946441}.; FUNCTION: Isoform 5: Involved in transcriptional regulation in embryonic stem cells (ESCs). Stimulates expression of transcription factors that are required for pluripotency and decreases expression of differentiation-associated genes. Has distinct DNA-binding specifities as compared to the canonical form and preferentially binds DNA with the sequence 5'-CGATACAA-3' (or closely related sequences) (By similarity). Promotes ESC self-renewal and pluripotency (PubMed:21924763). {ECO:0000250|UniProtKB:Q9H334, ECO:0000269|PubMed:21924763}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H334}. Note=Not found in the nucleolus. {ECO:0000250|UniProtKB:Q9H334}. SUBUNIT: Forms homodimers and heterodimers with FOXP2 and FOXP4. Dimerization is required for DNA-binding. Self-associates (By similarity). Interacts with CTBP1 (PubMed:14701752). Interacts with NCOR2 and AR. Interacts with FOXP2 (By similarity). {ECO:0000250|UniProtKB:Q9H334, ECO:0000269|PubMed:14701752}. DOMAIN: The leucine-zipper is required for dimerization and transcriptional repression. {ECO:0000269|PubMed:14701752}. TISSUE SPECIFICITY: Isoform 5 is specifically expressed in embryonic stem cells (PubMed:21924763). Highest expression in the lung, brain, and spleen. Lower expression in heart, skeletal muscle, kidney, small intestine (isoform 3 not present) and liver. {ECO:0000269|PubMed:21924763}. +Q8BKE5 FSBP_MOUSE Fibrinogen silencer-binding protein 299 34,403 Alternative sequence (1); Chain (1); Cross-link (1) FUNCTION: Transcriptional repressor that down-regulates the expression of the fibrinogen gamma chain. Represses transcription of GSK3B gene promoter via its interaction with APBA1. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with APBA1 (via PDZ 1 and 2 domains). {ECO:0000250}. +A1EGX6 FSCB_MOUSE Fibrous sheath CABYR-binding protein (PKA-phosphorylated calcium and CABYR-binding protein) 1074 114,979 Chain (1); Compositional bias (1); Modified residue (6) FUNCTION: May be involved in the later stages of fibrous sheath biogenesis and spermatozoa capacitation. Inhibits ROPN1 and ROPN1L SUMOylation. Binds calcium. {ECO:0000269|PubMed:17855365, ECO:0000269|PubMed:27398160}. PTM: Phosphorylated by PKA upon spermatozoa capacitation conditions. {ECO:0000269|PubMed:17855365, ECO:0000269|PubMed:21871179, ECO:0000269|PubMed:27398160}. SUBCELLULAR LOCATION: Cell projection, cilium, flagellum {ECO:0000269|PubMed:17855365}. Note=Localizes to cortex of the fibrous sheath including the surface of the longitudinal columns and ribs of the principal piece of sperm flagella. {ECO:0000269|PubMed:17855365}. SUBUNIT: Interacts with CABYR (PubMed:17855365). Interacts with ROPN1 and ROPN1L; the interaction increases upon spermatozoa capacitation conditions (PubMed:27398160). {ECO:0000269|PubMed:17855365, ECO:0000269|PubMed:27398160}. TISSUE SPECIFICITY: Expression is restricted to testis and epididymis, expressed by spermatozoa. {ECO:0000269|PubMed:17855365, ECO:0000269|PubMed:27398160}. +P17095 HMGA1_MOUSE High mobility group protein HMG-I/HMG-Y (HMG-I(Y)) (High mobility group AT-hook protein 1) (High mobility group protein A1) 107 11,614 Alternative sequence (1); Chain (1); Compositional bias (1); Cross-link (1); DNA binding (3); Initiator methionine (1); Modified residue (21); Region (1); Sequence conflict (2) FUNCTION: HMG-I/Y bind preferentially to the minor groove of A+T rich regions in double-stranded DNA. It is suggested that these proteins could function in nucleosome phasing and in the 3'-end processing of mRNA transcripts. They are also involved in the transcription regulation of genes containing, or in close proximity to A+T-rich regions. PTM: Isoforms HMG-I and HMG-Y can be phosphorylated by HIPK2. Phosphorylation may modulate DNA-binding affinity (By similarity). {ECO:0000250}.; PTM: Methylation at Arg-58 is mutually exclusive with methylation at Arg-60. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Chromosome. SUBUNIT: Interacts with HIPK2. {ECO:0000269|PubMed:11593421}. +Q6P8W9 HMGB4_MOUSE High mobility group protein B4 181 21,604 Chain (1); DNA binding (2); Sequence conflict (1) SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}. Chromosome {ECO:0000250}. +Q9DB70 FUND1_MOUSE FUN14 domain-containing protein 1 155 17,159 Chain (1); Modified residue (2); Motif (1); Topological domain (4); Transmembrane (3) TRANSMEM 48 68 Helical. {ECO:0000255}.; TRANSMEM 75 95 Helical. {ECO:0000255}.; TRANSMEM 134 154 Helical. {ECO:0000255}. TOPO_DOM 1 47 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 69 74 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 96 133 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 155 155 Mitochondrial intermembrane. {ECO:0000255}. FUNCTION: Acts as an activator of hypoxia-induced mitophagy, an important mechanism for mitochondrial quality control. {ECO:0000250}. PTM: Phosphorylation at Tyr-18 by SRC inhibits activation of mitophagy. Following hypoxia, dephosphorylated at Tyr-18, leading to interaction with MAP1 LC3 family proteins and triggering mitophagy (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts (via YXXL motif) with MAP1 LC3 family proteins MAP1LC3A, MAP1LC3B and GABARAP. {ECO:0000250}. DOMAIN: The YXXL motif mediates the interaction with MAP1 LC3 family proteins MAP1LC3A, MAP1LC3B and GABARAP. {ECO:0000250}. +Q9EPX5 FXL12_MOUSE F-box/LRR-repeat protein 12 (F-box and leucine-rich repeat protein 12) (F-box protein FBL12) 326 37,231 Chain (1); Domain (1); Frameshift (1); Repeat (8) Protein modification; protein ubiquitination. FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. Mediates the polyubiquitination and proteasomal degradation of CAMK1 leading to disruption of cyclin D1/CDK4 complex assembly which results in G1 cell cycle arrest in lung epithelia (By similarity). {ECO:0000250}. SUBUNIT: Interacts with SKP1 and CUL1. {ECO:0000250}. +Q91W61 FXL15_MOUSE F-box/LRR-repeat protein 15 (F-box only protein 37) 300 33,125 Chain (1); Domain (1); Frameshift (1); Modified residue (1); Region (1); Repeat (5); Sequence conflict (2) Protein modification; protein ubiquitination. FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of SMURF1, thereby acting as a positive regulator of the BMP signaling pathway. Required for dorsal/ventral pattern formation and bone mass maintenance. Also mediates ubiquitination of SMURF2 and WWP2 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Part of the SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase complex SCF(FBXL15) composed of CUL1, SKP1, RBX1 and FBXL15. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in heart, liver, spleen, bone, muscle, brain and kidney (at protein level). {ECO:0000269|PubMed:21572392}. +Q11131 FUT7_MOUSE Alpha-(1,3)-fucosyltransferase 7 (EC 2.4.1.-) (Fucosyltransferase 7) (Fucosyltransferase VII) (Fuc-TVII) (FucT-VII) (Galactoside 3-L-fucosyltransferase) 389 44,495 Alternative sequence (1); Chain (1); Disulfide bond (3); Glycosylation (2); Topological domain (2); Transmembrane (1) TRANSMEM 56 78 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 55 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 79 389 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Catalyzes alpha-1,3 glycosidic linkages involved in the expression of sialyl Lewis X antigens. {ECO:0000250|UniProtKB:Q11130}. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. Note=Membrane-bound form in trans cisternae of Golgi. TISSUE SPECIFICITY: Highly expressed in lung and bone marrow and to a much lesser extent in spleen, salivary gland and skeletal muscle. {ECO:0000269|PubMed:8626519}. +P97808 FXYD5_MOUSE FXYD domain-containing ion transport regulator 5 (EF-8) (Ion channel homolog RIC) (Oncoprotein-induced protein 2) 178 19,454 Chain (1); Compositional bias (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 146 166 Helical. {ECO:0000255}. TOPO_DOM 22 145 Extracellular. {ECO:0000255}.; TOPO_DOM 167 178 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in down-regulation of E-cadherin which results in reduced cell adhesion. Promotes metastasis (By similarity). {ECO:0000250}. PTM: Glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Spleen, lung, skeletal muscle, and testis. +Q9WTS2 FUT8_MOUSE Alpha-(1,6)-fucosyltransferase (Alpha1-6FucT) (EC 2.4.1.68) (Fucosyltransferase 8) (GDP-L-Fuc:N-acetyl-beta-D-glucosaminide alpha1,6-fucosyltransferase) (GDP-fucose--glycoprotein fucosyltransferase) (Glycoprotein 6-alpha-L-fucosyltransferase) 575 66,557 Chain (1); Disulfide bond (4); Domain (2); Modified residue (1); Motif (1); Region (1); Sequence conflict (3); Topological domain (2); Transmembrane (1) TRANSMEM 10 30 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 9 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 31 575 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Catalyzes the addition of fucose in alpha 1-6 linkage to the first GlcNAc residue, next to the peptide chains in N-glycans. {ECO:0000250}. PTM: Tyrosine phosphorylated by PKDCC/VLK. {ECO:0000250|UniProtKB:Q9BYC5}. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Membrane-bound form in trans cisternae of Golgi. {ECO:0000250}. +Q9CYL5 GAPR1_MOUSE Golgi-associated plant pathogenesis-related protein 1 (GAPR-1) (Golgi-associated PR-1 protein) (Glioma pathogenesis-related protein 2) (GliPR 2) 154 17,090 Chain (1); Coiled coil (1); Domain (1); Initiator methionine (1); Lipidation (1); Region (1); Sequence conflict (2) SUBCELLULAR LOCATION: Golgi apparatus membrane; Lipid-anchor. Note=Binds lipid-enriched microdomains of Golgi membranes not only by ionic interactions but also through the myristate. {ECO:0000250|UniProtKB:Q9H4G4}. SUBUNIT: Homodimer. Interacts with CAV1 (By similarity). {ECO:0000250}. +O88854 GALR2_MOUSE Galanin receptor type 2 (GAL2-R) (GALR-2) 371 40,516 Chain (1); Disulfide bond (1); Glycosylation (1); Sequence conflict (5); Topological domain (8); Transmembrane (7) TRANSMEM 28 48 Helical; Name=1. {ECO:0000255}.; TRANSMEM 60 80 Helical; Name=2. {ECO:0000255}.; TRANSMEM 99 120 Helical; Name=3. {ECO:0000255}.; TRANSMEM 141 161 Helical; Name=4. {ECO:0000255}.; TRANSMEM 187 207 Helical; Name=5. {ECO:0000255}.; TRANSMEM 237 257 Helical; Name=6. {ECO:0000255}.; TRANSMEM 260 280 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 27 Extracellular. {ECO:0000255}.; TOPO_DOM 49 59 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 81 98 Extracellular. {ECO:0000255}.; TOPO_DOM 121 140 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 162 186 Extracellular. {ECO:0000255}.; TOPO_DOM 208 236 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 258 259 Extracellular. {ECO:0000255}.; TOPO_DOM 281 371 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for the hormone galanin, GALP and spexin-1. The activity of this receptor is mediated by G proteins that activate the phospholipase C/protein kinase C pathway (via G(q)) and that inhibit adenylyl cyclase (via G(i)). {ECO:0000250|UniProtKB:O43603, ECO:0000269|PubMed:9832122}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +P63017 HSP7C_MOUSE Heat shock cognate 71 kDa protein (Heat shock 70 kDa protein 8) 646 70,871 Beta strand (17); Binding site (1); Chain (1); Cross-link (2); Frameshift (1); Helix (15); Initiator methionine (1); Modified residue (20); Nucleotide binding (4); Region (3); Sequence conflict (14); Turn (7) FUNCTION: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The co-chaperones have been shown to not only regulate different steps of the ATPase cycle of HSP70, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation. The affinity of HSP70 for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. HSP70 goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The HSP70-associated co-chaperones are of three types: J-domain co-chaperones HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1. Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion. Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co-chaperones and the E3 ligase STUB1. {ECO:0000250|UniProtKB:P11142}. PTM: Acetylated. {ECO:0000250|UniProtKB:P11142}.; PTM: ISGylated. {ECO:0000269|PubMed:16139798}.; PTM: Trimethylation at Lys-561 reduces fibrillar SNCA binding. {ECO:0000250|UniProtKB:P11142}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Melanosome {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Translocates rapidly from the cytoplasm to the nuclei, and especially to the nucleoli, upon heat shock (By similarity). {ECO:0000250}. SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with PACRG. Interacts with DNAJC7. Interacts with DNAJB12 (via J domain). Interacts with DNAJB14 (via J domain). Interacts (via C-terminus) with the E3 ligase STUB1 forming a 210 kDa complex of one STUB1 and two HSPA8 molecules. Interacts with CITED1 (via N-terminus); the interaction suppresses the association of CITED1 to p300/CBP and Smad-mediated transcription transactivation. Component of the PRP19-CDC5L splicing complex composed of a core complex comprising a homotetramer of PRPF19, CDC5L, PLRG1 and BCAS2, and at least three less stably associated proteins CTNNBL1, CWC15 and HSPA8. Interacts with IRAK1BP1 and HSPH1/HSP105 (PubMed:9675148, PubMed:15292236, PubMed:17233114). Interacts with TRIM5. Part of a complex composed at least of ASCL2, EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; this complex may have a histone H3-specific methyltransferase activity. Following LPS binding, may form a complex with CXCR4, GDF5 and HSP90AA1. Interacts with PRKN. Interacts with FOXP3. Interacts with DNAJC9 (via J domain). Interacts with MLLT11. Interacts with RNF207. Interacts with DNAJC21. Interacts with DNAJB2. Interacts with TTC1 (via TPR repeats). Interacts with SGTA (via TPR repeats). Interacts with HSF1 (via transactivation domain). Interacts with HOPX, STUB1, HSP40, HSP90, BAG2 and BAG3 (By similarity). Interacts with DNAJC12 (By similarity). Interacts with HSPC138 (By similarity). Interacts with ZMYND10 (By similarity). {ECO:0000250|UniProtKB:P11142, ECO:0000250|UniProtKB:P63018, ECO:0000269|PubMed:15292236, ECO:0000269|PubMed:17233114, ECO:0000269|PubMed:9675148}. DOMAIN: The N-terminal nucleotide binding domain (NBD) (also known as the ATPase domain) is responsible for binding and hydrolyzing ATP. The C-terminal substrate-binding domain (SBD) (also known as peptide-binding domain) binds to the client/substrate proteins. The two domains are allosterically coupled so that, when ATP is bound to the NBD, the SBD binds relatively weakly to clients. When ADP is bound in the NBD, a conformational change enhances the affinity of the SBD for client proteins. {ECO:0000250|UniProtKB:P11142}. TISSUE SPECIFICITY: Ubiquitous. +Q99M31 HSP7E_MOUSE Heat shock 70 kDa protein 14 (NST-1) (hsr.1) 509 54,650 Alternative sequence (1); Chain (1); Sequence conflict (3) FUNCTION: Component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding-competent state. In the RAC complex, binds to the nascent polypeptide chain, while DNAJC2 stimulates its ATPase activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. SUBUNIT: Component of ribosome-associated complex (RAC), a heterodimer composed of Hsp70/DnaK-type chaperone HSPA14 and Hsp40/DnaJ-type chaperone DNAJC2. {ECO:0000250}. +P14602 HSPB1_MOUSE Heat shock protein beta-1 (HspB1) (Growth-related 25 kDa protein) (Heat shock 25 kDa protein) (HSP 25) (Heat shock 27 kDa protein) (HSP 27) (p25) 209 23,014 Alternative sequence (2); Chain (1); Domain (1); Modified residue (12); Region (1); Sequence conflict (12) FUNCTION: Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding-competent state. Plays a role in stress resistance and actin organization (PubMed:17661394). Through its molecular chaperone activity may regulate numerous biological processes including the phosphorylation and the axonal transport of neurofilament proteins (By similarity). {ECO:0000250|UniProtKB:P04792, ECO:0000269|PubMed:17661394}. PTM: Phosphorylated upon exposure to protein kinase C activators and heat shock (By similarity). Phosphorylation by MAPKAPK2 and MAPKAPK3 in response to stress dissociates HSPB1 from large small heat-shock protein (sHsps) oligomers and impairs its chaperone activity and ability to protect against oxidative stress effectively. Phosphorylation by MAPKAPK5 in response to PKA stimulation induces F-actin rearrangement (PubMed:1332886, PubMed:1860870, PubMed:21575178, PubMed:8093612). {ECO:0000250|UniProtKB:P04792, ECO:0000269|PubMed:1332886, ECO:0000269|PubMed:1860870, ECO:0000269|PubMed:21575178, ECO:0000269|PubMed:8093612}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P04792}. Nucleus {ECO:0000250|UniProtKB:P04792}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P04792}. Note=Cytoplasmic in interphase cells. Colocalizes with mitotic spindles in mitotic cells. Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles. {ECO:0000250|UniProtKB:P04792}. SUBUNIT: Homooligomer. Homodimer; becomes monomeric upon activation. Heterooligomer; with HSPB6. Associates with alpha- and beta-tubulin (By similarity). Interacts with TGFB1I1 (PubMed:11546764). Interacts with CRYAB (By similarity). Interacts with HSPB8 (PubMed:11342557). Interacts with HSPBAP1 (PubMed:10751411). {ECO:0000250|UniProtKB:P04792, ECO:0000269|PubMed:10751411, ECO:0000269|PubMed:11342557, ECO:0000269|PubMed:11546764}. +Q1HCM0 FGFP3_MOUSE Fibroblast growth factor-binding protein 3 (FGF-BP3) (FGF-binding protein 3) (FGFBP-3) 245 26,217 Chain (1); Disulfide bond (3); Erroneous initiation (1); Signal peptide (1) FUNCTION: Heparin-binding protein which binds to FGF2, prevents binding of FGF2 to heparin and probably inhibits immobilization of FGF2 on extracellular matrix glycosaminoglycans, allowing its release and subsequent activation of FGFR signaling which leads to increased vascular permeability. {ECO:0000250|UniProtKB:Q8TAT2}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8TAT2}. SUBUNIT: Interacts with FGF2. {ECO:0000269|PubMed:20851768}. TISSUE SPECIFICITY: In the adult, highly expressed in brain with lower levels in ovary. In the embryo, highest levels are found in the brain and spinal cord at E14 and expression is almost completely restricted to the brain by E18. In the adult and post-natal brain, highly expressed in the orbitofrontal cortex where it is concentrated primarily in differentiated neurons. {ECO:0000269|PubMed:20851768}. +P15655 FGF2_MOUSE Fibroblast growth factor 2 (FGF-2) (Basic fibroblast growth factor) (bFGF) (Heparin-binding growth factor 2) (HBGF-2) 154 17,153 Binding site (1); Chain (1); Cross-link (1); Modified residue (1); Propeptide (1); Region (1); Site (3) FUNCTION: Acts as a ligand for FGFR1, FGFR2, FGFR3 and FGFR4. Also acts as an integrin ligand which is required for FGF2 signaling. Binds to integrin ITGAV:ITGB3. Plays an important role in the regulation of cell survival, cell division, cell differentiation and cell migration. Functions as a potent mitogen in vitro. Can induce angiogenesis. {ECO:0000250|UniProtKB:P09038}. PTM: Phosphorylation at Tyr-81 regulates FGF2 unconventional secretion. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Nucleus {ECO:0000250}. Note=Exported from cells by an endoplasmic reticulum (ER)/Golgi-independent mechanism. Unconventional secretion of FGF2 occurs by direct translocation across the plasma membrane (By similarity). Binding of exogenous FGF2 to FGFR facilitates endocytosis followed by translocation of FGF2 across endosomal membrane into the cytosol. Nuclear import from the cytosol requires the classical nuclear import machinery, involving proteins KPNA1 and KPNB1, as well as CEP57 (By similarity). {ECO:0000250}. SUBUNIT: Monomer. Homodimer. Interacts with FGFR1, FGFR2, FGFR3 and FGFR4. Affinity between fibroblast growth factors (FGFs) and their receptors is increased by heparan sulfate glycosaminoglycans that function as coreceptors. Interacts with CSPG4, FGFBP1 and TEC. Found in a complex with FGFBP1, FGF1 and FGF2 (By similarity). Interacts with FGFBP3 (PubMed:20851768). Interacts with integrin ITGAV:ITGB3; the interaction is required for FGF2 signaling (By similarity). Interacts with SNORC (via the extracellular domain) (PubMed:28323137). Interacts with glypican GPC3 (By similarity). {ECO:0000250|UniProtKB:P09038, ECO:0000250|UniProtKB:P13109, ECO:0000269|PubMed:20851768, ECO:0000269|PubMed:28323137, ECO:0000269|PubMed:9178765}. +Q6DFV6 FN3C1_MOUSE Fibronectin type III domain containing protein 3C1 1356 149,712 Chain (1); Compositional bias (2); Domain (8); Topological domain (1); Transmembrane (1) TRANSMEM 1330 1350 Helical. {ECO:0000255}. TOPO_DOM 1351 1356 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. +Q3I5G5 FOXI2_MOUSE Forkhead box protein I2 311 32,784 Chain (1); DNA binding (1); Erroneous initiation (2) FUNCTION: Possible transcriptional activator. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. +O35392 FOXD2_MOUSE Forkhead box protein D2 (Mesoderm/mesenchyme forkhead 2) (MF-2) 492 48,937 Chain (1); Compositional bias (3); DNA binding (1); Modified residue (1) FUNCTION: Probable transcription factor involved in embryogenesis and somatogenesis. {ECO:0000269|PubMed:9510020}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: Expressed at high levels in the ventral region of newly formed somites, in sclerotomal derivatives, in lateral plate and cephalic mesoderm and in the first and second branchial arches. Other regions of mesodermal expression include the developing tongue, meninges, nose, whiskers, kidney, genital tubercule and limb joints. In the nervous system it is transcribed in restricted regions of the mid- and forebrain. {ECO:0000269|PubMed:9510020}. +P35582 FOXA1_MOUSE Hepatocyte nuclear factor 3-alpha (HNF-3-alpha) (HNF-3A) (Forkhead box protein A1) 468 48,854 Chain (1); DNA binding (1); Modified residue (2); Region (1); Sequence conflict (3) FUNCTION: Transcription factor that is involved in embryonic development, establishment of tissue-specific gene expression and regulation of gene expression in differentiated tissues. Is thought to act as a 'pioneer' factor opening the compacted chromatin for other proteins through interactions with nucleosomal core histones and thereby replacing linker histones at target enhancer and/or promoter sites. Binds DNA with the consensus sequence 5'-[AC]A[AT]T[AG]TT[GT][AG][CT]T[CT]-3' (By similarity). Proposed to play a role in translating the epigenetic signatures into cell type-specific enhancer-driven transcriptional programs. Involved in the development of multiple endoderm-derived organ systems such as the liver, pancreas, lungs and prostate; FOXA1 and FOXA2 seem to have at least in part redundant roles. Plays a role in prostate morphogenesis and epithelial cell differentiation. FOXA1 and FOXA2 are essential for hepatic specification. FOXA1 and FOXA2 are required for morphogenesis and cell differentiation during formation of the lung. FOXA1 and FOXA2 are involved in bile duct formation; they positively regulate the binding of glucocorticoid receptor/NR3C1 to the IL6 promoter. FOXA1 and FOXA2 regulate multiple phases of midbrain dopaminergic neuron development; they regulate expression of NEUROG2 at the beginning of mDA neurogenesis and of NR4A2 and EN1 in immature mDA neurons. Modulates the transcriptional activity of nuclear hormone receptors. Is involved in ESR1-mediated transcription. Inhibits NKX2-1-mediated transcription from the SFTPC promoter in lung epithel independently from DNA-binding. Involved in regulation of apoptosis. Involved in cell cycle regulation. Originally described as a transcription activator for a number of liver genes such as AFP, albumin, tyrosine aminotransferase, PEPCK, etc. Interacts with the cis-acting regulatory regions of these genes. Involved in glucose homeostasis; activates the GCG promoter. {ECO:0000250, ECO:0000269|PubMed:10049364, ECO:0000269|PubMed:11864602, ECO:0000269|PubMed:15668254, ECO:0000269|PubMed:15748903, ECO:0000269|PubMed:15959514, ECO:0000269|PubMed:15987773, ECO:0000269|PubMed:17596284, ECO:0000269|PubMed:19141476, ECO:0000269|PubMed:19436110}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089, ECO:0000269|PubMed:15987773}. SUBUNIT: Binds DNA as a monomer. Interacts with FOXA2. Interacts with NKX2-1. Interacts with HDAC7. Interacts with the histone H3-H4 heterodimer. Associates with nucleosomes containing histone H2A. Interacts with AR. Interacts with NR0B2 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Restricted mainly to endoderm-derived tissues (lung, liver, stomach, and small intestine). Expressed in the prostate. {ECO:0000269|PubMed:15987773}. +P35583 FOXA2_MOUSE Hepatocyte nuclear factor 3-beta (HNF-3-beta) (HNF-3B) (Forkhead box protein A2) 459 48,498 Chain (1); DNA binding (1); Modified residue (10); Motif (1); Region (2); Sequence conflict (2) FUNCTION: Transcription factor that is involved in embryonic development, establishment of tissue-specific gene expression and regulation of gene expression in differentiated tissues. Is thought to act as a 'pioneer' factor opening the compacted chromatin for other proteins through interactions with nucleosomal core histones and thereby replacing linker histones at target enhancer and/or promoter sites. Binds DNA with the consensus sequence 5'-[AC]A[AT]T[AG]TT[GT][AG][CT]T[CT]-3' (By similarity). In embryonic development is required for notochord formation. Involved in the development of multiple endoderm-derived organ systems such as the liver, pancreas and lungs; Foxa1 and Foxa2 seem to have at least in part redundant roles. FOXA1 and FOXA2 are essential for hepatic specification. FOXA1 and FOXA2 are required for morphogenesis and cell differentiation during formation of the lung. FOXA1 and FOXA2 are involved in bile duct formation; they positively regulate the binding glucocorticoid receptor/NR3C1 to the IL6 promoter. FOXA1 and FOXA2 regulate multiple phases of midbrain dopaminergic neuron development; they regulate expression of NEUROG2 at the beginning of mDA neurogenesis and of NR4A2 and EN1 in immature mDA neurons. Modulates the transcriptional activity of nuclear hormone receptors; inhibits AR-mediated transcription from the LCN5 promoter. Binds to fibrinogen beta promoter and is involved in IL6-induced fibrinogen beta transcriptional activation. Originally described as a transcription activator for a number of liver genes such as AFP, albumin, tyrosine aminotransferase, PEPCK, etc. Interacts with the cis-acting regulatory regions of these genes. Involved in glucose homeostasis; regulates the expression of genes important for glucose sensing in pancreatic beta-cells and glucose homeostasis. In pancreatic beta cells activates transcription of potassium channel subunits KCNJ11 and ABCC8. Involved in regulation of fat metabolism; activates transcriptional programs of lipid metabolism and ketogenesis at low insulin state. Involved in transcriptional regulation of MUC2 in the intestine. {ECO:0000250, ECO:0000269|PubMed:11445544, ECO:0000269|PubMed:11875061, ECO:0000269|PubMed:15616563, ECO:0000269|PubMed:15668254, ECO:0000269|PubMed:15959514, ECO:0000269|PubMed:16740652, ECO:0000269|PubMed:17596284, ECO:0000269|PubMed:18336786, ECO:0000269|PubMed:19141476, ECO:0000269|PubMed:19436110, ECO:0000269|PubMed:8069909}. PTM: Phosphorylation on Thr-156 abolishes binding to target promoters and subsequent transcription activation upon insulin stimulation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089, ECO:0000269|PubMed:15616563}. Cytoplasm {ECO:0000269|PubMed:15616563}. Note=Shuttles between the nucleus and cytoplasm in a CRM1-dependent manner; in response to insulin signaling via AKT1 is exported from the nucleus. SUBUNIT: Binds DNA as a monomer. Binds TLE1. Interacts with FOXA1 and FOXA3. Interacts with PRKDC (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Restricted mainly to endoderm-derived tissues (lung, liver, stomach, and small intestine). Expressed in epididymis with region-specific expression pattern: no expression is observed in initial segment, low expression in proximal caput, gradiently higher levels of expression in middle and distal caput and highest level in corpus and cauda (at protein level). {ECO:0000269|PubMed:16740652}. +O09160 FUT1_MOUSE Galactoside 2-alpha-L-fucosyltransferase 1 (EC 2.4.1.344) (Alpha(1,2)FT 1) (Fucosyltransferase 1) (GDP-L-fucose:beta-D-galactoside 2-alpha-L-fucosyltransferase 1) 376 42,255 Chain (1); Glycosylation (2); Topological domain (2); Transmembrane (1) TRANSMEM 9 26 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 8 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 27 376 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Creates a soluble precursor oligosaccharide FuC-alpha ((1,2)Gal-beta-) called the H antigen which is an essential substrate for the final step in the soluble A and B antigen synthesis pathway. {ECO:0000250|UniProtKB:P19526}. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. Note=Membrane-bound form in trans cisternae of Golgi. TISSUE SPECIFICITY: In the adult, highly expressed in pancreas, testis and epididymis and to a lesser extent in thymus, lung, stomach, small intestine, colon, spleen and uterus. Not expressed in brain, heart, skeletal muscle, kidney, liver and bone marrow. +Q8BID8 FXL14_MOUSE F-box/LRR-repeat protein 14 (F-box and leucine-rich repeat protein 14) 400 43,864 Chain (1); Domain (1); Region (1); Repeat (5); Sequence conflict (1) FUNCTION: Substrate-recognition component of some (SKP1-CUL1-F-box protein)-type E3 ubiquitin-protein ligase complexes. The SCF(FBXL14) complex acts by mediating ubiquitination and subsequent degradation of SNAI1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Part of a SCF (SKP1-cullin-F-box) ubiquitin-protein ligase complex. Interacts with SKP1 and CUL1. Interacts with SNAI1; the interaction requires the phosphorylation of the two serine residues in the substrate destruction motif D-S-G-X(2,3,4)-S (By similarity). {ECO:0000250}. +Q9D2W0 FXYD4_MOUSE FXYD domain-containing ion transport regulator 4 (Channel-inducing factor) (CHIF) 88 9,269 Chain (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 39 59 Helical. {ECO:0000255}. TOPO_DOM 21 38 Extracellular. {ECO:0000255}.; TOPO_DOM 60 88 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +P47930 FOSL2_MOUSE Fos-related antigen 2 (FRA-2) 326 35,298 Alternative sequence (1); Chain (1); Cross-link (5); Domain (1); Modified residue (7); Region (2); Sequence conflict (2) FUNCTION: Controls osteoclast survival and size. As a dimer with JUN, activates LIF transcription. Activates CEBPB transcription in PGE2-activated osteoblasts (By similarity). {ECO:0000250, ECO:0000269|PubMed:18548006}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Heterodimer; with JUN. +Q8R2I0 FOXE1_MOUSE Forkhead box protein E1 (Thyroid transcription factor 2) (TTF-2) 371 37,768 Chain (1); Compositional bias (3); DNA binding (1) FUNCTION: Transcription factor that binds consensus sites on a variety of gene promoters and activate their transcription. Involved in proper palate formation, most probably through the expression of MSX1 and TGFB3 genes which are direct targets of this transcription factor (PubMed:21177256). Also implicated in thyroid gland morphogenesis (PubMed:9697704). May indirectly play a role in cell growth and migration through the regulation of WNT5A expression (By similarity). {ECO:0000250|UniProtKB:O00358, ECO:0000269|PubMed:21177256, ECO:0000269|PubMed:9697704}. PTM: Phosphorylated. {ECO:0000269|PubMed:12203737}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O00358}. TISSUE SPECIFICITY: Expressed in Rathke pouch, in thyroid, and in the epithelium of the pharyngeal wall and arches, whereas it is absent in the epithelium of the pharyngeal pouches. {ECO:0000269|PubMed:12203737}. +Q64731 FOXL1_MOUSE Forkhead box protein L1 (Forkhead-related protein FKHL11) (Transcription factor FKH-6) 336 35,793 Chain (1); DNA binding (1); Frameshift (1); Sequence conflict (2) FUNCTION: Transcription factor required for proper proliferation and differentiation in the gastrointestinal epithelium. Target gene of the hedgehog (Hh) signaling pathway via GLI2 AND GLI3 transcription factors. {ECO:0000269|PubMed:19049965, ECO:0000269|PubMed:9203584}. SUBCELLULAR LOCATION: Nucleus. +O88536 FPR2_MOUSE Formyl peptide receptor 2 (Formylpeptide receptor-related sequence 2) (Lipoxin A4 receptor-like protein) (N-formylpeptide receptor-like 2) 351 39,422 Chain (1); Disulfide bond (1); Glycosylation (2); Topological domain (8); Transmembrane (7) TRANSMEM 30 50 Helical; Name=1. {ECO:0000255}.; TRANSMEM 62 82 Helical; Name=2. {ECO:0000255}.; TRANSMEM 100 120 Helical; Name=3. {ECO:0000255}.; TRANSMEM 145 165 Helical; Name=4. {ECO:0000255}.; TRANSMEM 206 226 Helical; Name=5. {ECO:0000255}.; TRANSMEM 242 262 Helical; Name=6. {ECO:0000255}.; TRANSMEM 283 305 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 29 Extracellular. {ECO:0000255}.; TOPO_DOM 51 61 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 83 99 Extracellular. {ECO:0000255}.; TOPO_DOM 121 144 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 166 205 Extracellular. {ECO:0000255}.; TOPO_DOM 227 241 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 263 282 Extracellular. {ECO:0000255}.; TOPO_DOM 306 351 Cytoplasmic. {ECO:0000255}. FUNCTION: High affinity receptor for N-formyl-methionyl peptides (FMLP), which are powerful neutrophil chemotactic factors (PubMed:12218158, PubMed:10477558, PubMed:19387439). Stimulates chemotaxis in immune cells to site of infection or tissue damage upon recognition of several ligands, such as FMLP, or ligand involved in cell damage, disease or inflammation (PubMed:10477558, PubMed:19497865). Receptor for the chemokine-like protein FAM19A5, mediating FAM19A5-stimulated macrophage chemotaxis and the inhibitory effect on TNFSF11/RANKL-induced osteoclast differentiation (PubMed:29138422). {ECO:0000269|PubMed:10477558, ECO:0000269|PubMed:12218158, ECO:0000269|PubMed:19387439, ECO:0000269|PubMed:19497865, ECO:0000269|PubMed:29138422}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P25090}; Multi-pass membrane protein {ECO:0000305}. Note=Associates with Amyloid-beta protein 42, product of APP, at the cell surface and the complex is then rapidly internalized. {ECO:0000250|UniProtKB:P25090}. SUBUNIT: Interacts with Amyloid-beta protein 42, product of APP; the interaction takes place at the cell surface and the complex is then rapidly internalized. {ECO:0000250|UniProtKB:P25090}. TISSUE SPECIFICITY: Primarily expressed in neutrophils. Not detected in vomeronasal neurons. {ECO:0000269|PubMed:10477558, ECO:0000269|PubMed:15879124, ECO:0000269|PubMed:17237393, ECO:0000269|PubMed:19387439, ECO:0000269|PubMed:19497865}. +O88537 FPRS3_MOUSE Formyl peptide receptor-related sequence 3 343 38,064 Chain (1); Disulfide bond (1); Glycosylation (2); Sequence conflict (2); Topological domain (8); Transmembrane (7) TRANSMEM 30 50 Helical; Name=1. {ECO:0000255}.; TRANSMEM 67 87 Helical; Name=2. {ECO:0000255}.; TRANSMEM 100 120 Helical; Name=3. {ECO:0000255}.; TRANSMEM 145 165 Helical; Name=4. {ECO:0000255}.; TRANSMEM 203 223 Helical; Name=5. {ECO:0000255}.; TRANSMEM 242 262 Helical; Name=6. {ECO:0000255}.; TRANSMEM 281 301 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 29 Extracellular. {ECO:0000255}.; TOPO_DOM 51 66 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 88 99 Extracellular. {ECO:0000255}.; TOPO_DOM 121 144 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 166 202 Extracellular. {ECO:0000255}.; TOPO_DOM 224 241 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 263 280 Extracellular. {ECO:0000255}.; TOPO_DOM 302 343 Cytoplasmic. {ECO:0000255}. FUNCTION: May have an olfactory function associated with the identification of pathogens or of pathogenic states. {ECO:0000269|PubMed:19387439}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed exclusively in vomeronasal neurons (PubMed:19387439 and PubMed:19497865). Expressed in 0.8 % of a subset of sensory neurons located in the apical layer of the vomeronasal organ. Localized in sensory somata as well as dendritic cells. Each neuron appears to express only one receptor gene. {ECO:0000269|PubMed:19387439, ECO:0000269|PubMed:19497865}. +Q71MR7 FPRS7_MOUSE Formyl peptide receptor-related sequence 7 338 38,141 Chain (1); Disulfide bond (1); Glycosylation (3); Sequence conflict (1); Topological domain (8); Transmembrane (7) TRANSMEM 24 44 Helical; Name=1. {ECO:0000255}.; TRANSMEM 63 85 Helical; Name=2. {ECO:0000255}.; TRANSMEM 100 120 Helical; Name=3. {ECO:0000255}.; TRANSMEM 145 165 Helical; Name=4. {ECO:0000255}.; TRANSMEM 199 219 Helical; Name=5. {ECO:0000255}.; TRANSMEM 242 262 Helical; Name=6. {ECO:0000255}.; TRANSMEM 281 301 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 23 Extracellular. {ECO:0000255}.; TOPO_DOM 45 62 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 86 99 Extracellular. {ECO:0000255}.; TOPO_DOM 121 144 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 166 198 Extracellular. {ECO:0000255}.; TOPO_DOM 220 241 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 263 280 Extracellular. {ECO:0000255}.; TOPO_DOM 302 338 Cytoplasmic. {ECO:0000255}. FUNCTION: May have an olfactory function associated with the identification of pathogens or of pathogenic states. {ECO:0000269|PubMed:19387439}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed exclusively in vomeronasal organ (PubMed:19387439, PubMed:19497865). Expressed in 0.8 % of a subset of sensory neurons located in the apical layer of the vomeronasal organ. Each neuron appears to express only one receptor gene. Expressed in heart, liver, lung, spleen smooth muscle and pancreas (PubMed:12459252). {ECO:0000269|PubMed:12459252, ECO:0000269|PubMed:19387439, ECO:0000269|PubMed:19497865}. +Q11127 FUT4_MOUSE Alpha-(1,3)-fucosyltransferase 4 (EC 2.4.1.-) (Fucosyltransferase 4) (Fucosyltransferase IV) (Fuc-TIV) (FucT-IV) (Galactoside 3-L-fucosyltransferase) 433 49,481 Alternative sequence (1); Chain (1); Glycosylation (2); Sequence conflict (4); Topological domain (2); Transmembrane (1) TRANSMEM 53 74 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 52 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 75 433 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: May catalyze alpha-1,3 glycosidic linkages involved in the expression of Lewis X/SSEA-1 and VIM-2 antigens. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. Note=Membrane-bound form in trans cisternae of Golgi. TISSUE SPECIFICITY: Highest expression in stomach and colon. It is also expressed in the lung, testis, uterus, small intestine and to a lesser extent in spleen, and ovary. Present in trace amounts in brain, thymus, heart, smooth muscle, kidney and bone marrow. Not found in liver, salivary gland and pancreas. +A2RT62 FXL16_MOUSE F-box/LRR-repeat protein 16 (F-box and leucine-rich repeat protein 16) 479 51,878 Chain (1); Domain (1); Modified residue (1); Repeat (6) FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. {ECO:0000250}. SUBUNIT: Interacts with SKP1 and CUL1. {ECO:0000250}. +Q8R059 GALE_MOUSE UDP-glucose 4-epimerase (EC 5.1.3.2) (Galactowaldenase) (UDP-N-acetylglucosamine 4-epimerase) (UDP-GlcNAc 4-epimerase) (EC 5.1.3.7) (UDP-galactosamine 4-epimerase) (UDP-GalNAc 4-epimerase) (UDP-galactose 4-epimerase) 347 38,225 Active site (1); Binding site (5); Chain (1); Nucleotide binding (3); Region (5) Carbohydrate metabolism; galactose metabolism. FUNCTION: Catalyzes two distinct but analogous reactions: the reversible epimerization of UDP-glucose to UDP-galactose and the reversible epimerization of UDP-N-acetylglucosamine to UDP-N-acetylgalactosamine. The reaction with UDP-Gal plays a critical role in the Leloir pathway of galactose catabolism in which galactose is converted to the glycolytic intermediate glucose 6-phosphate. It contributes to the catabolism of dietary galactose and enables the endogenous biosynthesis of both UDP-Gal and UDP-GalNAc when exogenous sources are limited. Both UDP-sugar interconversions are important in the synthesis of glycoproteins and glycolipids. {ECO:0000250|UniProtKB:Q14376}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q14376}. +Q8R070 G6PT2_MOUSE Glucose-6-phosphate exchanger SLC37A1 (Solute carrier family 37 member 1) 531 57,355 Chain (1); Sequence conflict (1); Transmembrane (12) TRANSMEM 18 38 Helical. {ECO:0000255}.; TRANSMEM 100 120 Helical. {ECO:0000255}.; TRANSMEM 129 149 Helical. {ECO:0000255}.; TRANSMEM 157 177 Helical. {ECO:0000255}.; TRANSMEM 192 214 Helical. {ECO:0000255}.; TRANSMEM 222 242 Helical. {ECO:0000255}.; TRANSMEM 332 352 Helical. {ECO:0000255}.; TRANSMEM 364 384 Helical. {ECO:0000255}.; TRANSMEM 392 412 Helical. {ECO:0000255}.; TRANSMEM 419 439 Helical. {ECO:0000255}.; TRANSMEM 464 484 Helical. {ECO:0000255}.; TRANSMEM 488 508 Helical. {ECO:0000255}. FUNCTION: Inorganic phosphate and glucose-6-phosphate antiporter. May transport cytoplasmic glucose-6-phosphate into the lumen of the endoplasmic reticulum and translocate inorganic phosphate into the opposite direction. Independent of a lumenal glucose-6-phosphatase. May not play a role in homeostatic regulation of blood glucose levels. {ECO:0000250|UniProtKB:P57057}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P57057}; Multi-pass membrane protein {ECO:0000255}. +Q6PAR5 GAPD1_MOUSE GTPase-activating protein and VPS9 domain-containing protein 1 (GAPex-5) (Rab5-activating protein 6) 1458 162,402 Alternative sequence (6); Chain (1); Domain (2); Erroneous gene model prediction (6); Erroneous initiation (5); Frameshift (1); Modified residue (20); Sequence caution (2); Sequence conflict (4) FUNCTION: Acts both as a GTPase-activating protein (GAP) and a guanine nucleotide exchange factor (GEF), and participates in various processes such as endocytosis, insulin receptor internalization or LC2A4/GLUT4 trafficking. Acts as a GEF for the Ras-related protein RAB31 by exchanging bound GDP for free GTP, leading to regulate LC2A4/GLUT4 trafficking. In the absence of insulin, it maintains RAB31 in an active state and promotes a futile cycle between LC2A4/GLUT4 storage vesicles and early endosomes, retaining LC2A4/GLUT4 inside the cells. Upon insulin stimulation, it is translocated to the plasma membrane, releasing LC2A4/GLUT4 from intracellular storage vesicles. Also involved in EGFR trafficking and degradation, possibly by promoting EGFR ubiquitination and subsequent degradation by the proteasome. Has GEF activity for Rab5 and GAP activity for Ras. {ECO:0000269|PubMed:16880210, ECO:0000269|PubMed:17189207, ECO:0000269|PubMed:17545148}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:17189207}; Peripheral membrane protein {ECO:0000269|PubMed:17189207}. Endosome {ECO:0000250}. Note=Recruited to the plasma membrane by TRIP10/CIP4 in response to insulin. SUBUNIT: Interacts with RAB5A (By similarity). Interacts with TRIP10/CIP4. {ECO:0000250, ECO:0000269|PubMed:17189207}. TISSUE SPECIFICITY: Present in adipocytes and fibroblasts (at protein level). Ubiquitously expressed. {ECO:0000269|PubMed:17189207}. +P11862 GAS2_MOUSE Growth arrest-specific protein 2 (GAS-2) 314 34,901 Beta strand (6); Chain (1); Domain (2); Helix (3); Modified residue (2); Mutagenesis (1); Site (1); Turn (1) FUNCTION: May play a role in apoptosis by acting as a cell death substrate for caspases. Is cleaved during apoptosis and the cleaved form induces dramatic rearrangements of the actin cytoskeleton and potent changes in the shape of the affected cells. May play a role in chondrocyte proliferation and differentiation, and in limb myogenesis. May be involved in the regulation of the apoptosis in the interdigital tissues of the developing hindlimb. May be involved in the membrane ruffling process. {ECO:0000269|PubMed:10049561}. PTM: Cleaved, during apoptosis, on a specific aspartic residue by caspases. {ECO:0000250}.; PTM: Phosphorylated on serine residues during the G0-G1 transition phase. {ECO:0000269|PubMed:8120096}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, stress fiber {ECO:0000269|PubMed:8120096}. Membrane {ECO:0000269|PubMed:8120096}; Peripheral membrane protein {ECO:0000269|PubMed:8120096}. Note=Component of the microfilament system (PubMed:1607387). Colocalizes with actin fibers at the cell border and along the stress fibers in growth-arrested fibroblasts (PubMed:8120096). Mainly membrane-associated (PubMed:8120096). When hyperphosphorylated, accumulates at membrane ruffles (PubMed:8120096). {ECO:0000269|PubMed:1607387, ECO:0000269|PubMed:8120096}. TISSUE SPECIFICITY: Expressed in most tissues. Highest levels in liver, lung and kidney. In the embryo strongly expressed in regions that undergo extensive apoptosis, such as the intervertebral tissues, the cranofacial mesenchyme and the cartilage of the limbs. +L7N1X6 FBW15_MOUSE F-box/WD repeat-containing protein 15 466 53,586 Alternative sequence (1); Chain (1); Domain (1); Repeat (5); Sequence conflict (2) Protein modification; protein ubiquitination. FUNCTION: Substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. Promotes KAT7 ubiquitination and subsequent degradation in collaboration with MAP2K1 kinase, leading to reduced histone H3K14 acetylation and increased cell proliferation. {ECO:0000269|PubMed:23319590}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:18094359, ECO:0000269|PubMed:23319590}. Endoplasmic reticulum {ECO:0000269|PubMed:18094359}. Nucleus {ECO:0000269|PubMed:23319590}. SUBUNIT: Part of an SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex. Interacts with KAT7 and SKP1. {ECO:0000269|PubMed:23319590}. TISSUE SPECIFICITY: Specifically expressed in oocytes from follicles of the medullary region of the ovary. {ECO:0000269|PubMed:18094359}. +Q8BH16 FBXL2_MOUSE F-box/LRR-repeat protein 2 (F-box and leucine-rich repeat protein 2) 423 46,890 Chain (1); Domain (1); Lipidation (1); Motif (1); Region (1); Repeat (13); Sequence conflict (1) FUNCTION: Calcium-activated substrate recognition component of the SCF (SKP1-cullin-F-box protein) E3 ubiquitin-protein ligase complex, SCF(FBXL2), which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Unlike many F-box proteins, FBXL2 does not seem to target phosphodegron within its substrates but rather calmodulin-binding motifs and is thereby antagonized by calmodulin. This is the case for the cyclins CCND2 and CCND3 which polyubiquitination and subsequent degradation are inhibited by calmodulin. Through CCND2 and CCND3 degradation induces cell-cycle arrest in G(0). SCF(FBXL2) also mediates PIK3R2 ubiquitination and proteasomal degradation thereby regulating phosphatidylinositol 3-kinase signaling and autophagy (By similarity). PCYT1A monoubiquitination by SCF(FBXL2) and subsequent degradation regulates synthesis of phosphatidylcholine, which is utilized for formation of membranes and of pulmonary surfactant (PubMed:21343341). {ECO:0000250|UniProtKB:Q9UKC9, ECO:0000269|PubMed:21343341}. SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9UKC9}; Lipid-anchor {ECO:0000250|UniProtKB:Q9UKC9}. SUBUNIT: Part of the SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase complex SCF(FBXL2) composed of CUL1, SKP1, RBX1 and FBXL2 (By similarity). Interacts with PCYT1A (PubMed:21343341). Interacts with calmodulin; may antagonize substrate ubiquitination by SCF(FBXL2) (PubMed:21343341). Interacts with CCND2 and CCND3. Interacts with PIK3R2; PIK3R2 is a substrate ubiquitinated by the SCF(FBXL2) complex. May interact with PIK3R1. Interacts with PTPN13 (By similarity). {ECO:0000250|UniProtKB:Q9UKC9, ECO:0000269|PubMed:21343341}. DOMAIN: The CAAX motif is a signal for the geranylgeranylation of FBXL2 and is required for its association with cell membranes and the recruitment of substrates to the active SCF(FBXL2) complex. {ECO:0000250|UniProtKB:Q9UKC9}. +Q8C4V4 FBXL3_MOUSE F-box/LRR-repeat protein 3 (F-box and leucine-rich repeat protein 3A) (F-box/LRR-repeat protein 3A) (Protein after-hours) (Protein overtime) 428 48,682 Alternative sequence (1); Chain (1); Domain (1); Erroneous initiation (3); Mutagenesis (4); Repeat (7); Sequence conflict (1) Protein modification; protein ubiquitination. FUNCTION: Substrate-recognition component of the SCF(FBXL3) E3 ubiquitin ligase complex involved in circadian rhythm function. Plays a key role in the maintenance of both the speed and the robustness of the circadian clock oscillation. The SCF(FBXL3) complex mainly acts in the nucleus and mediates ubiquitination and subsequent degradation of CRY1 and CRY2. Activity of the SCF(FBXL3) complex is counteracted by the SCF(FBXL21) complex. {ECO:0000269|PubMed:17462724, ECO:0000269|PubMed:17463252, ECO:0000269|PubMed:18953409, ECO:0000269|PubMed:23452855, ECO:0000269|PubMed:23452856, ECO:0000269|PubMed:23616524}. PTM: Undergoes autophagy-mediated degradation in the liver in a time-dependent manner. {ECO:0000269|PubMed:29937374}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Predominantly nuclear. SUBUNIT: Part of the SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase complex SCF(FBXL3) composed of CUL1, SKP1, RBX1 and FBXL3. Interacts with CRY1 and CRY2 (phosphorylated). {ECO:0000269|PubMed:17462724, ECO:0000269|PubMed:18953409, ECO:0000269|PubMed:23452855, ECO:0000269|PubMed:23452856}. TISSUE SPECIFICITY: Ubiquitously expressed but enriched in brain. Diffusely expressed in the suprachiasmatic nucleus, SCN. {ECO:0000269|PubMed:17462724, ECO:0000269|PubMed:18953409}. +Q8CIG9 FBXL8_MOUSE F-box/LRR-repeat protein 8 (F-box and leucine-rich repeat protein 8) (F-box protein FBL8) 374 41,145 Chain (1); Domain (1); Sequence conflict (2) FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. {ECO:0000250}. SUBUNIT: Directly interacts with SKP1 and CUL1. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed during embryogenesis and in adult tissues. {ECO:0000269|PubMed:10531037}. +Q6PFY1 FCSD1_MOUSE F-BAR and double SH3 domains protein 1 688 76,256 Alternative sequence (1); Chain (1); Coiled coil (1); Compositional bias (1); Domain (3); Modified residue (1) +Q8CIB5 FERM2_MOUSE Fermitin family homolog 2 (Kindlin-2) (Pleckstrin homology domain-containing family C member 1) 680 77,800 Beta strand (18); Binding site (1); Chain (1); Domain (2); Erroneous initiation (1); Helix (19); Modified residue (5); Mutagenesis (1); Region (1); Sequence conflict (1); Turn (9) FUNCTION: Scaffolding protein that enhances integrin activation mediated by TLN1 and/or TLN2, but activates integrins only weakly by itself. Binds to membranes enriched in phosphoinositides. Enhances integrin-mediated cell adhesion onto the extracellular matrix and cell spreading; this requires both its ability to interact with integrins and with phospholipid membranes. Required for the assembly of focal adhesions. Participates in the connection between extracellular matrix adhesion sites and the actin cytoskeleton and also in the orchestration of actin assembly and cell shape modulation. Recruits FBLIM1 to focal adhesions. Plays a role in the TGFB1 and integrin signaling pathways. Stabilizes active CTNNB1 and plays a role in the regulation of transcription mediated by CTNNB1 and TCF7L2/TCF4 and in Wnt signaling. {ECO:0000269|PubMed:18174465, ECO:0000269|PubMed:18483218, ECO:0000269|PubMed:21378273}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000250}. Cell junction, focal adhesion {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell projection, lamellipodium membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, myofibril, sarcomere, I band. Cell surface. Note=Colocalizes with actin stress fibers at cell-ECM focal adhesion sites. Colocalizes with ITGB3 at lamellipodia at the leading edge of spreading cells. Binds to membranes that contain phosphatidylinositides (By similarity). {ECO:0000250}. SUBUNIT: Interacts with ITGB1; the interaction is inhibited in presence of ITGB1BP1. Interacts with FBLIM1. Interacts with active, unphosphorylated CTNNB1. Identified in a complex with CTNNB1 and TCF7L2/TCF4 (By similarity). Interacts with ILK, ITGB1 and ITGB3. {ECO:0000250, ECO:0000269|PubMed:18483218}. DOMAIN: The FERM domain is not correctly detected by PROSITE or Pfam techniques because it contains the insertion of a PH domain.; DOMAIN: The PH domain binds phospholipids. Binds preferentially phosphatidylinositol-3,4,5-trisphosphate, and has lower affinity for phosphatidylinositol-4,5-bisphosphate (By similarity). {ECO:0000250}.; DOMAIN: The N-terminal region displays a ubiquitin-type fold and mediates interaction with membranes containing negatively charged phosphatidylinositol phosphate via a surface enriched in positively charged residues. {ECO:0000250}. TISSUE SPECIFICITY: Detected in adult heart muscle (at protein level). Detected in heart, skeletal muscle and testis. {ECO:0000269|PubMed:18174465}. +P02772 FETA_MOUSE Alpha-fetoprotein (Alpha-1-fetoprotein) (Alpha-fetoglobulin) 605 67,337 Chain (1); Disulfide bond (15); Domain (3); Glycosylation (2); Modified residue (5); Sequence conflict (1); Signal peptide (1) FUNCTION: Binds estrogens, fatty acids and metals. PTM: Glycosylated; contains two glycans.; PTM: Sulfated. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Plasma. +P70378 FGF11_MOUSE Fibroblast growth factor 11 (FGF-11) (Fibroblast growth factor homologous factor 3) (FHF-3) 225 25,178 Chain (1) FUNCTION: Probably involved in nervous system development and function. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: Brain and eye, and in a segmental pattern of the embryonic body wall. In adult olfactory bulb, hippocampus and most concentrated in Purkinje cell layer of the cerebellum. +Q8K0X8 FEZ1_MOUSE Fasciculation and elongation protein zeta-1 (Zygin I) (Zygin-1) 392 45,215 Chain (1); Coiled coil (1); Compositional bias (1); Modified residue (3); Sequence conflict (3) FUNCTION: May be involved in axonal outgrowth as component of the network of molecules that regulate cellular morphology and axon guidance machinery. May participate in the transport of mitochondria and other cargos along microtubules (By similarity). {ECO:0000250}. PTM: Phosphorylated by protein kinase C zeta; which enhances interaction with UBE4B and polyubiquitination. {ECO:0000250}.; PTM: Polyubiquitinated in a UBE4B-dependent manner; which does not lead to proteasomal degradation and may be important for neurogenic activity. Polyubiquitin linkage seems to be mainly through Lys-26 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Colocalizes with both, alpha- and gamma-tubulin. Translocated from the plasma membrane to the cytoplasm by activation of the PKC zeta (By similarity). {ECO:0000250}. SUBUNIT: Homodimer. Interacts with the NH2-terminal variable region (V1) of PKC zeta and weakly with that of PKC epsilon. Interacts with UBE4B and SAP30L (By similarity). Interacts with SCOC and ULK1; SCOC interferes with ULK1-binding to FEZ1 (By similarity). Directly interacts with SCOC and UVRAG. Stabilizes the interaction between SCOC and UVRAG during amino acid starvation (By similarity). {ECO:0000250}. +Q9EPC2 FGF23_MOUSE Fibroblast growth factor 23 (FGF-23) 251 27,758 Chain (1); Disulfide bond (1); Glycosylation (1); Signal peptide (1) FUNCTION: Regulator of phosphate homeostasis (By similarity). Inhibits renal tubular phosphate transport by reducing SLC34A1 levels (By similarity). Acts directly on the parathyroid to decrease PTH secretion (By similarity). Regulator of vitamin-D metabolism (By similarity). Negatively regulates osteoblasts differentiation and matrix mineralization (By similarity). Upregulates EGR1 expression in the presence of KL. {ECO:0000250, ECO:0000269|PubMed:17086194}. PTM: Following secretion this protein is inactivated by cleavage into a N-terminal fragment and a C-terminal fragment. The processing is effected by proprotein convertases (By similarity). {ECO:0000250}.; PTM: O-glycosylated by GALT3. Glycosylation is necessary for secretion; it blocks processing by proprotein convertases when the O-glycan is alpha 2,6-sialylated. Competition between proprotein convertase cleavage and block of cleavage by O-glycosylation determines the level of secreted active FGF23 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Secretion is dependent on O-glycosylation. {ECO:0000250}. SUBUNIT: Interacts with FGFR1, FGFR2, FGFR3 and FGFR4. Affinity between fibroblast growth factors (FGFs) and their receptors is increased by KL and heparan sulfate glycosaminoglycans that function as coreceptors (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Mainly expressed in the brain and thymus at low levels. In brain; preferentially expressed in the ventrolateral thalamic nucleus. +P52734 FGD1_MOUSE FYVE, RhoGEF and PH domain-containing protein 1 (Faciogenital dysplasia 1 protein homolog) (Rho/Rac guanine nucleotide exchange factor FGD1) (Rho/Rac GEF) (Zinc finger FYVE domain-containing protein 3) 960 106,365 Chain (1); Compositional bias (1); Domain (3); Modified residue (4); Motif (1); Mutagenesis (3); Sequence conflict (2); Zinc finger (1) FUNCTION: Activates CDC42, a member of the Ras-like family of Rho- and Rac proteins, by exchanging bound GDP for free GTP. Plays a role in regulating the actin cytoskeleton and cell shape. {ECO:0000269|PubMed:12913069}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12913069}. Cell projection, lamellipodium {ECO:0000269|PubMed:12913069}. Cell projection, ruffle {ECO:0000269|PubMed:12913069}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12913069}. Note=Associated with membrane ruffles and lamellipodia. SUBUNIT: Interacts with DBNL/ABP1 and CTTN. Binds CDC42 (By similarity). May interact with CCPG1. {ECO:0000250, ECO:0000269|PubMed:12913069}. DOMAIN: The DH domain is involved in interaction with CCPG1. +Q69ZL1 FGD6_MOUSE FYVE, RhoGEF and PH domain-containing protein 6 1399 155,169 Alternative sequence (1); Beta strand (7); Chain (1); Compositional bias (1); Domain (3); Erroneous initiation (1); Helix (1); Modified residue (6); Sequence conflict (11); Zinc finger (1) FUNCTION: May activate CDC42, a member of the Ras-like family of Rho- and Rac proteins, by exchanging bound GDP for free GTP. May play a role in regulating the actin cytoskeleton and cell shape (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Cytoplasm, cytoskeleton {ECO:0000305}. +P16092 FGFR1_MOUSE Fibroblast growth factor receptor 1 (FGFR-1) (bFGF-R-1) (EC 2.7.10.1) (Basic fibroblast growth factor receptor 1) (MFR) (Proto-oncogene c-Fgr) (CD antigen CD331) 822 91,981 Active site (1); Alternative sequence (7); Beta strand (8); Binding site (4); Chain (1); Disulfide bond (3); Domain (4); Glycosylation (8); Helix (1); Modified residue (7); Nucleotide binding (2); Region (1); Sequence caution (1); Sequence conflict (15); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 377 397 Helical. {ECO:0000255}. TOPO_DOM 22 376 Extracellular. {ECO:0000255}.; TOPO_DOM 398 822 Cytoplasmic. {ECO:0000255}. FUNCTION: Tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of embryonic development, cell proliferation, differentiation and migration. Required for normal mesoderm patterning and correct axial organization during embryonic development, normal skeletogenesis and normal development of the gonadotropin-releasing hormone (GnRH) neuronal system. Phosphorylates PLCG1, FRS2, GAB1 and SHB. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Promotes phosphorylation of SHC1, STAT1 and PTPN11/SHP2. In the nucleus, enhances RPS6KA1 and CREB1 activity and contributes to the regulation of transcription. FGFR1 signaling is down-regulated by IL17RD/SEF, and by FGFR1 ubiquitination, internalization and degradation (By similarity). {ECO:0000250|UniProtKB:P11362, ECO:0000269|PubMed:10821861, ECO:0000269|PubMed:10896947, ECO:0000269|PubMed:1309590, ECO:0000269|PubMed:17086194, ECO:0000269|PubMed:8001822, ECO:0000269|PubMed:8001823}. PTM: Autophosphorylated. Binding of FGF family members together with heparan sulfate proteoglycan or heparin promotes receptor dimerization and autophosphorylation on tyrosine residues. Autophosphorylation occurs in trans between the two FGFR molecules present in the dimer and proceeds in a highly ordered manner. Initial autophosphorylation at Tyr-653 increases the kinase activity by a factor of 50 to 100. After this, Tyr-583 becomes phosphorylated, followed by phosphorylation of Tyr-463, Tyr-766, Tyr-583 and Tyr-585. In a third stage, Tyr-654 is autophosphorylated, resulting in a further tenfold increase of kinase activity. Phosphotyrosine residues provide docking sites for interacting proteins and so are crucial for FGFR1 function and its regulation (By similarity). {ECO:0000250|UniProtKB:P11362}.; PTM: Ubiquitinated. FGFR1 is rapidly ubiquitinated by NEDD4 after autophosphorylation, leading to internalization and lysosomal degradation. CBL is recruited to activated FGFR1 via FRS2 and GRB2, and mediates ubiquitination and subsequent degradation of FGFR1 (By similarity). {ECO:0000250|UniProtKB:P11362}.; PTM: N-glycosylated in the endoplasmic reticulum. The N-glycan chains undergo further maturation to an Endo H-resistant form in the Golgi apparatus. {ECO:0000269|PubMed:10821861, ECO:0000269|PubMed:19349973}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Nucleus. Cytoplasm, cytosol. Cytoplasmic vesicle. Note=After ligand binding, both receptor and ligand are rapidly internalized. Can translocate to the nucleus after internalization, or by translocation from the endoplasmic reticulum or Golgi apparatus to the cytosol, and from there to the nucleus.; SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Isoform 5: Cell membrane; Single-pass type I membrane protein. SUBUNIT: Monomer. Homodimer after ligand binding. Interacts predominantly with FGF1 and FGF2, but can also interact with FGF3, FGF4, FGF5, FGF6, FGF8, FGF10, FGF19, FGF21, FGF22 and FGF23 (in vitro) (PubMed:10821861, PubMed:1309590, PubMed:17086194). Ligand specificity is determined by tissue-specific expression of isoforms, and differences in the third Ig-like domain are crucial for ligand specificity. Affinity for fibroblast growth factors (FGFs) is increased by heparan sulfate glycosaminoglycans that function as coreceptors. Likewise, KLB increases the affinity for FGF19, FGF21 and FGF23. Interacts (phosphorylated on Tyr-766) with PLCG1 (via SH2 domains). Interacts with FRS2. Interacts with RPS6KA1. Interacts (via C-terminus) with NEDD4 (via WW3 domain). Interacts with KL (PubMed:17086194). Interacts with SHB (via SH2 domain) (PubMed:12181353). Interacts with GRB10 (By similarity). Interacts with ANOS1; this interaction does not interfere with FGF2-binding to FGFR1, but prevents binding of heparin-bound FGF2 (By similarity). Interacts with SOX2 and SOX3 (PubMed:17728342). Interacts with FLRT1, FLRT2 and FLRT3 (PubMed:16872596). Found in a ternary complex with FGF1 and ITGAV:ITGB3 (By similarity). {ECO:0000250|UniProtKB:P11362, ECO:0000269|PubMed:10821861, ECO:0000269|PubMed:12181353, ECO:0000269|PubMed:1309590, ECO:0000269|PubMed:16872596, ECO:0000269|PubMed:17086194, ECO:0000269|PubMed:17452648, ECO:0000269|PubMed:17728342, ECO:0000269|PubMed:8663044}. DOMAIN: The second and third Ig-like domains directly interact with fibroblast growth factors (FGF) and heparan sulfate proteoglycans. Isoforms lacking the first Ig-like domain have higher affinity for fibroblast growth factors (FGF) and heparan sulfate proteoglycans than isoforms with all three Ig-like domains (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10821861}. +P21658 FGF6_MOUSE Fibroblast growth factor 6 (FGF-6) (Heparin secretory-transforming protein 2) (HST-2) (HSTF-2) (Heparin-binding growth factor 6) (HBGF-6) 208 22,798 Chain (1); Disulfide bond (1); Glycosylation (1); Signal peptide (1) FUNCTION: Plays an important role in the regulation of cell proliferation, cell differentiation, angiogenesis and myogenesis, and is required for normal muscle regeneration. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space. SUBUNIT: Interacts with FGFR1, FGFR2 and FGFR4. Affinity between fibroblast growth factors (FGFs) and their receptors is increased by heparan sulfate glycosaminoglycans that function as coreceptors (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Embryos, adult muscles and adult testis. +P36363 FGF7_MOUSE Fibroblast growth factor 7 (FGF-7) (Heparin-binding growth factor 7) (HBGF-7) (Keratinocyte growth factor) (KGF) 194 22,347 Chain (1); Glycosylation (1); Signal peptide (1) FUNCTION: Plays an important role in the regulation of embryonic development, cell proliferation and cell differentiation. Required for normal branching morphogenesis. Growth factor active on keratinocytes. Possible major paracrine effector of normal epithelial cell proliferation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Interacts with FGFBP1. Interacts with FGFR2. Affinity between fibroblast growth factors (FGFs) and their receptors is increased by heparan sulfate glycosaminoglycans that function as coreceptors (By similarity). {ECO:0000250}. +Q76LL6 FHOD3_MOUSE FH1/FH2 domain-containing protein 3 (Formin homolog overexpressed in spleen 2) (mFHOS2) 1578 175,655 Alternative sequence (3); Chain (1); Coiled coil (1); Compositional bias (3); Domain (4); Modified residue (5); Sequence conflict (3) FUNCTION: May play a role in actin filament polymerization in cardiomyocytes (By similarity). Actin-organizing protein that may cause stress fiber formation together with cell elongation. {ECO:0000250, ECO:0000269|PubMed:15966898}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:21149568}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:21149568}. Note=Main part of the protein localizes to actin fibers and the remaining part displays filamentous staining. {ECO:0000250}. SUBUNIT: Interacts with nestin/NES-based interfilament (IF). Interacts with SQSTM1. {ECO:0000250}. DOMAIN: The DAD domain regulates activation via by an autoinhibitory interaction with the GBD/FH3 domain. This autoinhibition is released upon competitive binding of an activated GTPase. The release of DAD allows the FH2 domain to then nucleate and elongate nonbranched actin filaments (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the heart, including left ventricle, kidney, brain and skeletal muscle, including soleus and tibialis anterior (at protein level). {ECO:0000269|PubMed:15966898, ECO:0000269|PubMed:21149568}. +Q8K0E8 FIBB_MOUSE Fibrinogen beta chain [Cleaved into: Fibrinopeptide B; Fibrinogen beta chain] 481 54,753 Chain (1); Coiled coil (1); Disulfide bond (5); Domain (1); Glycosylation (1); Peptide (1); Region (1); Signal peptide (1); Site (1) FUNCTION: Cleaved by the protease thrombin to yield monomers which, together with fibrinogen alpha (FGA) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets via an ITGB3-dependent pathway. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the immune response via both innate and T-cell mediated pathways. {ECO:0000250|UniProtKB:E9PV24}. PTM: Conversion of fibrinogen to fibrin is triggered by thrombin, which cleaves fibrinopeptides A and B from alpha and beta chains, and thus exposes the N-terminal polymerization sites responsible for the formation of the soft clot. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02675}. SUBUNIT: Heterohexamer; disulfide linked. Contains 2 sets of 3 non-identical chains (alpha, beta and gamma). The 2 heterotrimers are in head to head conformation with the N-termini in a small central domain (By similarity). {ECO:0000250|UniProtKB:P02675}. DOMAIN: A long coiled coil structure formed by 3 polypeptide chains connects the central nodule to the C-terminal domains (distal nodules). The long C-terminal ends of the alpha chains fold back, contributing a fourth strand to the coiled coil structure (By similarity). {ECO:0000250|UniProtKB:P02675}. +O54792 HES2_MOUSE Transcription factor HES-2 (Hairy and enhancer of split 2) 157 17,259 Chain (1); Compositional bias (1); Domain (2); Motif (1); Sequence conflict (1) FUNCTION: Transcriptional repressor of genes that require a bHLH protein for their transcription. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Transcription repression requires formation of a complex with a corepressor protein of the Groucho/TLE family. {ECO:0000250}. DOMAIN: Has a particular type of basic domain (presence of a helix-interrupting proline) that binds to the N-box (CACNAG), rather than the canonical E-box (CANNTG).; DOMAIN: The C-terminal WRPW motif is a transcriptional repression domain necessary for the interaction with Groucho/TLE family members, transcriptional corepressors recruited to specific target DNA by Hairy-related proteins. {ECO:0000250}. +Q61658 HESX1_MOUSE Homeobox expressed in ES cells 1 (Anterior-restricted homeobox protein) (Homeobox protein ANF) (Rathke pouch homeo box) 185 21,504 Chain (1); DNA binding (1); Sequence conflict (5) FUNCTION: Required for the normal development of the forebrain, eyes and other anterior structures such as the olfactory placodes and pituitary gland. Possible transcriptional repressor. Binds to the palindromic PIII sequence, 5'-AGCTTGAGTCTAATTGAATTAACTGTAC-3'. HESX1 and PROP1 bind as heterodimers on this palindromic site, and, in vitro, HESX1 can antagonize PROP1 activation. {ECO:0000269|PubMed:9620767}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Can form heterodimers with PROP1 in binding to DNA Interacts with TLE1. {ECO:0000250}. TISSUE SPECIFICITY: High levels found in the embryonic liver, lower level expression seen in the viscera, amnion and yolk sac. +E9PV24 FIBA_MOUSE Fibrinogen alpha chain [Cleaved into: Fibrinopeptide A; Fibrinogen alpha chain] 789 87,429 Alternative sequence (2); Chain (1); Coiled coil (1); Compositional bias (1); Disulfide bond (8); Domain (1); Glycosylation (1); Metal binding (4); Modified residue (3); Peptide (1); Signal peptide (1); Site (4) FUNCTION: Cleaved by the protease thrombin to yield monomers which, together with fibrinogen beta (FGB) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots (PubMed:7649481). In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization (PubMed:11389004). Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood (PubMed:7649481). However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo (PubMed:10930441). Enhances expression of SELP in activated platelets via an ITGB3-dependent pathway (PubMed:19332769). Maternal fibrinogen is essential for successful pregnancy (PubMed:7649481). Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage (PubMed:12629066). May also facilitate the immune response via both innate and T-cell mediated pathways (PubMed:23487423). {ECO:0000250|UniProtKB:P02671, ECO:0000269|PubMed:10930441, ECO:0000269|PubMed:11389004, ECO:0000269|PubMed:12629066, ECO:0000269|PubMed:15972474, ECO:0000269|PubMed:19332769, ECO:0000269|PubMed:23487423, ECO:0000269|PubMed:7649481}. PTM: Conversion of fibrinogen to fibrin is triggered by thrombin, which cleaves fibrinopeptides A and B from alpha and beta chains, and thus exposes the N-terminal polymerization sites responsible for the formation of the soft clot. The soft clot is converted into the hard clot by factor XIIIA which catalyzes the epsilon-(gamma-glutamyl)lysine cross-linking between gamma chains (stronger) and between alpha chains (weaker) of different monomers. {ECO:0000250|UniProtKB:P02671}.; PTM: Forms F13A-mediated cross-links between a glutamine and the epsilon-amino group of a lysine residue, forming fibronectin-fibrinogen heteropolymers. {ECO:0000250|UniProtKB:P02671}.; PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000250|UniProtKB:P02671}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7649481}. SUBUNIT: Heterohexamer; disulfide linked. Contains 2 sets of 3 non-identical chains (alpha, beta and gamma). The 2 heterotrimers are in head to head conformation with the N-termini in a small central domain. {ECO:0000250|UniProtKB:P02671}. DOMAIN: A long coiled coil structure formed by 3 polypeptide chains connects the central nodule to the C-terminal domains (distal nodules). The long C-terminal ends of the alpha chains fold back, contributing a fourth strand to the coiled coil structure. {ECO:0000250|UniProtKB:P02671}. TISSUE SPECIFICITY: Expressed in liver. {ECO:0000269|PubMed:7649481}. +Q9D824 FIP1_MOUSE Pre-mRNA 3'-end-processing factor FIP1 (FIP1-like 1 protein) 581 64,959 Alternative sequence (4); Chain (1); Compositional bias (3); Modified residue (10); Region (6) FUNCTION: Component of the cleavage and polyadenylation specificity factor (CPSF) complex that plays a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. FIP1L1 contributes to poly(A) site recognition and stimulates poly(A) addition. Binds to U-rich RNA sequence elements surrounding the poly(A) site. May act to tether poly(A) polymerase to the CPSF complex (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the cleavage and polyadenylation specificity factor (CPSF) complex, composed of CPSF1, CPSF2, CPSF3, CPSF4 and FIP1L1. Found in a complex with CPSF1, FIP1L1 and PAPOLA. Interacts with CPSF1, CPSF4, CSTF2 and CSTF3 (By similarity). Interacts with AHCYL1 (when phosphorylated); the interaction is direct and associates AHCYL1 with the CPSF complex and RNA (PubMed:19224921). Interacts with PAPOLA; the interaction seems to be increased by the interaction with AHCYL1 (PubMed:19224921). Interacts with NUDT21/CPSF5; this interaction occurs in a RNA sequence-specific manner. Interacts (preferentially via unphosphorylated form and Arg/Glu/Asp-rich domain) with CPSF6 (via Arg/Ser-rich domain); this interaction mediates, at least in part, the interaction between the CFIm and CPSF complexes and may be inhibited by CPSF6 hyper-phosphorylation. Interacts (preferentially via unphosphorylated form and Arg/Asp/Glu-rich domain) with CPSF7 (via Arg/Ser-rich domain); this interaction mediates, at least in part, the interaction between the CFIm and CPSF complexes and may be inhibited by CPSF7 hyper-phosphorylation (By similarity). {ECO:0000250|UniProtKB:Q6UN15, ECO:0000269|PubMed:19224921}. +Q61576 FKB10_MOUSE Peptidyl-prolyl cis-trans isomerase FKBP10 (PPIase FKBP10) (EC 5.2.1.8) (65 kDa FK506-binding protein) (65 kDa FKBP) (FKBP-65) (FK506-binding protein 10) (FKBP-10) (Immunophilin FKBP65) (Rotamase) 581 64,697 Calcium binding (2); Chain (1); Domain (6); Glycosylation (7); Motif (1); Sequence conflict (2); Signal peptide (1) FUNCTION: PPIases accelerate the folding of proteins during protein synthesis. PTM: Glycosylated and phosphorylated. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138, ECO:0000269|PubMed:11071917}. TISSUE SPECIFICITY: Expressed in aorta, brain, kidney, and lung. {ECO:0000269|PubMed:11071917}. +Q9ER69 FL2D_MOUSE Pre-mRNA-splicing regulator WTAP (Female-lethal(2)D homolog) (WT1-associated protein) (Wilms tumor 1-associating protein) 396 44,177 Alternative sequence (2); Chain (1); Modified residue (8) FUNCTION: Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing (PubMed:29535189, PubMed:29547716). Acts as a key regulator of m6A methylation by promoting m6A methylation of mRNAs at the 3'-UTR (PubMed:29547716). Required for accumulation of METTL3 and METTL14 to nuclear speckle (By similarity). Acts as a mRNA splicing regulator (By similarity). Regulates G2/M cell-cycle transition by binding to the 3' UTR of CCNA2, which enhances its stability (By similarity). Impairs WT1 DNA-binding ability and inhibits expression of WT1 target genes (By similarity). {ECO:0000250|UniProtKB:Q15007, ECO:0000269|PubMed:29535189, ECO:0000269|PubMed:29547716}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q15007}. Nucleus, nucleoplasm {ECO:0000269|PubMed:29547716}. Cytoplasm {ECO:0000269|PubMed:29547716}. Note=Mainly nuclear with some fraction located in the cytoplasm (PubMed:29547716). ZC3H13 is required to anchor component of the MACOM subcomplex, such as VIRMA, in the nucleus (PubMed:29547716). {ECO:0000269|PubMed:29547716}. SUBUNIT: Component of the WMM complex, a N6-methyltransferase complex composed of a catalytic subcomplex, named MAC, and of an associated subcomplex, named MACOM (PubMed:29535189, PubMed:29547716). The MAC subcomplex is composed of METTL3 and METTL14 (PubMed:29535189, PubMed:29547716). The MACOM subcomplex is composed of WTAP, ZC3H13, CBLL1/HAKAI, VIRMA, and, in some cases of RBM15 (RBM15 or RBM15B) (PubMed:29535189, PubMed:29547716). Interacts with WT1 (By similarity). Also component of a MACOM-like complex, named WTAP complex, composed of WTAP, ZC3H13, CBLL1, VIRMA, RBM15, BCLAF1 and THRAP3 (By similarity). Interacts with CPNE4 (via VWFA domain) (PubMed:12522145). {ECO:0000250|UniProtKB:Q15007, ECO:0000269|PubMed:12522145, ECO:0000269|PubMed:29535189, ECO:0000269|PubMed:29547716}. +Q60987 FOXG1_MOUSE Forkhead box protein G1 (FoxG1) (Brain factor 1) (BF-1) (BF1) (Forkhead-related protein FKHL1) 481 51,625 Chain (1); Compositional bias (3); DNA binding (1); Region (1) FUNCTION: Transcription repression factor which plays an important role in the establishment of the regional subdivision of the developing brain and in the development of the telencephalon. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with KDM5B. {ECO:0000250}. TISSUE SPECIFICITY: CNS, and nasal half of the retina. +P33766 FPR1_MOUSE fMet-Leu-Phe receptor (fMLP receptor) (N-formyl peptide receptor) (FPR) (N-formylpeptide chemoattractant receptor) 364 40,327 Chain (1); Disulfide bond (1); Glycosylation (3); Topological domain (8); Transmembrane (7) TRANSMEM 36 58 Helical; Name=1. {ECO:0000255}.; TRANSMEM 70 91 Helical; Name=2. {ECO:0000255}.; TRANSMEM 109 129 Helical; Name=3. {ECO:0000255}.; TRANSMEM 149 170 Helical; Name=4. {ECO:0000255}.; TRANSMEM 217 237 Helical; Name=5. {ECO:0000255}.; TRANSMEM 254 277 Helical; Name=6. {ECO:0000255}.; TRANSMEM 297 316 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 35 Extracellular. {ECO:0000255}.; TOPO_DOM 59 69 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 92 108 Extracellular. {ECO:0000255}.; TOPO_DOM 130 148 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 171 216 Extracellular. {ECO:0000255}.; TOPO_DOM 238 253 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 278 296 Extracellular. {ECO:0000255}.; TOPO_DOM 317 364 Cytoplasmic. {ECO:0000255}. FUNCTION: High affinity receptor for N-formyl-methionyl peptides (fMLP), which are powerful neutrophil chemotactic factors. Binding of fMLP to the receptor stimulates intracellular calcium mobilization and superoxide anion release. This response is mediated via a G-protein that activates a phosphatidylinositol-calcium second messenger system. {ECO:0000269|PubMed:8244972}. PTM: Phosphorylated; which is necessary for desensitization. {ECO:0000250|UniProtKB:P21462}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8244972}; Multi-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Expressed in neutrophils, dendritic cells, microglia, spleen, lung and liver. Low level of expression in the vomeronasal organ. {ECO:0000269|PubMed:19497865}. +O88470 FOXL2_MOUSE Forkhead box protein L2 (Pituitary forkhead factor) (P-Frk) 375 38,887 Chain (1); Compositional bias (3); Cross-link (1); DNA binding (1); Modified residue (1) FUNCTION: Transcriptional regulator. Critical factor essential for ovary differentiation and maintenance, and repression of the genetic program for somatic testis determination. Prevents trans-differentiation of ovary to testis through transcriptional repression of the Sertoli cell-promoting gene SOX9. Has apoptotic activity in ovarian cells. Suppresses ESR1-mediated transcription of PTGS2/COX2 stimulated by tamoxifen. Activates SIRT1 transcription under cellular stress conditions. Activates transcription of OSR2. Is a regulator of CYP19 expression. Is a transcriptional repressor of STAR. Participates in SMAD3-dependent transcription of FST via the intronic SMAD-binding element. {ECO:0000269|PubMed:15059956, ECO:0000269|PubMed:15944199, ECO:0000269|PubMed:19106105, ECO:0000269|PubMed:19797124, ECO:0000269|PubMed:20005806}. PTM: Sumoylated with SUMO1; sumoylation is required for transcriptional repression activity. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089, ECO:0000269|PubMed:19797124}. SUBUNIT: Interacts with ESR1. Interacts with UBE2I/UBC9 (By similarity). Interacts with SMAD3. Interacts with DDX20. {ECO:0000250, ECO:0000269|PubMed:16153597, ECO:0000269|PubMed:19106105, ECO:0000269|PubMed:19797124, ECO:0000269|PubMed:20005806}. TISSUE SPECIFICITY: Expressed in the mesenchyme of developing eyelids. Expressed in ovaries throughout development and adulthood, localized to the undifferentiated granulosa cells in small and medium follicles as well as cumulus cells of preovulatory follicles. Expressed in the pituitary. {ECO:0000269|PubMed:15059956, ECO:0000269|PubMed:19106105}. +P70339 FRAT1_MOUSE Proto-oncogene FRAT1 (Frequently rearranged in advanced T-cell lymphomas 1) (FRAT-1) 274 28,875 Chain (1); Compositional bias (4); Modified residue (2); Region (1) FUNCTION: Positively regulates the Wnt signaling pathway by stabilizing beta-catenin through the association with GSK-3. May play a role in tumor progression and collaborate with PIM1 and MYC in lymphomagenesis. {ECO:0000269|PubMed:15073180}. PTM: Phosphorylated. {ECO:0000269|PubMed:15073180}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15073180}. SUBUNIT: Binds DVL1. Binds GSK-3 and prevent GSK-3-dependent phosphorylation. TISSUE SPECIFICITY: Highly expressed in testis. Lower level of expression in spleen, thymus and brain. DISEASE: Note=Activation contributes to progression of mouse T-cell lymphomas (PubMed:9034327). {ECO:0000269|PubMed:9034327}. +O70220 FOXQ1_MOUSE Forkhead box protein Q1 (HFH-1l) (HNF-3/forkhead-like protein 1) (HFH-1) (Hepatocyte nuclear factor 3 forkhead homolog 1) 400 41,368 Chain (1); DNA binding (1); Sequence conflict (1) FUNCTION: Plays a role in hair follicle differentiation. {ECO:0000269|PubMed:16835220}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089}. TISSUE SPECIFICITY: Expressed in kidney and stomach. Expression in the outer medulla of the kidney and the transitional epithelium. Expressed in the hair follicle medulla. {ECO:0000269|PubMed:16835220, ECO:0000269|PubMed:9726250}. DISEASE: Note=Defects in Foxq1 are the cause of the satin (sa) phenotype and results in a silky coat with high sheen arising from structurally abnormal medulla cells and defects in differentiation of the hair shaft. {ECO:0000269|PubMed:11309849}. +Q91WJ0 FRS3_MOUSE Fibroblast growth factor receptor substrate 3 (FGFR substrate 3) (FRS2-beta) 492 53,976 Chain (1); Domain (1); Initiator methionine (1); Lipidation (1) FUNCTION: Adapter protein that links FGF and NGF receptors to downstream signaling pathways. Involved in the activation of MAP kinases. Down-regulates ERK2 signaling by interfering with the phosphorylation and nuclear translocation of ERK2. PTM: Phosphorylated on tyrosine residues upon stimulation by BFGF or NGFB. Phosphorylated by ULK2 in vitro. {ECO:0000269|PubMed:16887332}. SUBCELLULAR LOCATION: Membrane; Lipid-anchor. SUBUNIT: Binds NGFR, GRB2, PTPN11 and ERK2 (By similarity). Binds FGFR1 and NTRK1. {ECO:0000250}. +E9Q8I9 FRY_MOUSE Protein furry homolog 3020 339,093 Alternative sequence (5); Chain (1); Erroneous initiation (1); Modified residue (10); Mutagenesis (2); Sequence conflict (5) FUNCTION: Plays a crucial role in the structural integrity of mitotic centrosomes and in the maintenance of spindle bipolarity by promoting PLK1 activity at the spindle poles in early mitosis. May function as a scaffold promoting the interaction between AURKA and PLK1, thereby enhancing AURKA-mediated PLK1 phosphorylation. {ECO:0000269|PubMed:22753416}. PTM: Phosphorylated by AURKA, CDK1 and PLK1. {ECO:0000269|PubMed:22753416}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. Note=Distributed diffusely throughout the cytoplasm in interphase. Localizes to the separating centrosomes in prophase, to the spindle poles and spindle microtubules in prometaphase to metaphase, to spindle microtubules in anaphase and to the distal sections of the midbody in cytokinesis. Colocalizes with PLK1 to separating centrosomes and spindle poles from prophase to metaphase in mitosis, but not in other stages of the cell cycle (By similarity). {ECO:0000250}. SUBUNIT: When phosphorylated by CDK1, interacts with PLK1; this interaction occurs in mitotic cells, but not in interphase cells, and leads to further FRY phosphorylation by PLK1. {ECO:0000269|PubMed:22753416}. +Q8BIE6 FRM4A_MOUSE FERM domain-containing protein 4A 1020 113,879 Alternative sequence (2); Chain (1); Coiled coil (1); Compositional bias (2); Domain (1); Erroneous gene model prediction (2); Erroneous initiation (1); Modified residue (8); Region (2); Sequence conflict (1) FUNCTION: Scaffolding protein that regulates epithelial cell polarity by connecting ARF6 activation with the PAR3 complex (PubMed:20080746). Plays a redundant role with FRMD4B in epithelial polarization (PubMed:20080746). May regulate MAPT secretion by activating ARF6-signaling (By similarity). {ECO:0000250|UniProtKB:Q9P2Q2, ECO:0000269|PubMed:20080746}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell junction, adherens junction {ECO:0000269|PubMed:20080746}. Cell junction, tight junction {ECO:0000269|PubMed:20080746}. Note=Colocalized with CYTH1 at adherens junction and tight junction (PubMed:20080746). Colocalized with PARD3 during the process of epithelial polarization (PubMed:20080746). {ECO:0000269|PubMed:20080746}. SUBUNIT: Interacts (via coiled-coil domain) with CYTH1 (via coiled-coil domain) (PubMed:20080746). Interacts with PARD3 (via coiled-coil domain) (PubMed:20080746). Found in a complex with PARD3, CYTH1 and FRMD4A (PubMed:20080746). Interacts with CYTH2 (PubMed:20080746). Interacts with CYTH3 (PubMed:20080746). {ECO:0000269|PubMed:20080746}. +Q5H8B9 FREM3_MOUSE FRAS1-related extracellular matrix protein 3 (NV domain-containing protein 2) 2123 234,999 Chain (1); Domain (3); Glycosylation (5); Repeat (12); Signal peptide (1) FUNCTION: Extracellular matrix protein which may play a role in cell adhesion. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. DOMAIN: The Calx-beta domains bind calcium with high affinity and undergo a major conformational shift upon binding. {ECO:0000250}. +A2AFR3 FRPD4_MOUSE FERM and PDZ domain-containing protein 4 (PDZ domain-containing protein 10) (PSD-95-interacting regulator of spine morphogenesis) (Preso) 1320 144,978 Alternative sequence (2); Chain (1); Domain (3); Erroneous translation (1) FUNCTION: Positive regulator of dendritic spine morphogenesis and density. Required for the maintenance of excitatory synaptic transmission. Binds phosphatidylinositol 4,5-bisphosphate. {ECO:0000250|UniProtKB:Q14CM0}. SUBCELLULAR LOCATION: Cell projection, dendritic spine {ECO:0000250|UniProtKB:Q14CM0}. SUBUNIT: Interacts (via C-terminus) with DLG1, DLG2, DLG3 and DLG4/PSD95. Interacts (via N-terminus) with ARHGEF7; the interaction is mediated by the PDZ domain. Interacts with GPSM2 (via TPR repeat region). {ECO:0000250|UniProtKB:Q14CM0}. DOMAIN: The FERM domain mediates the interaction with phosphatidylinositol 4,5-bisphosphate. {ECO:0000250|UniProtKB:Q14CM0}. TISSUE SPECIFICITY: Expressed in various regions of the brain, including cortex, hippocampus, cerebellum, olfactory bulb and medial habenular nucleus. {ECO:0000269|PubMed:19118189}. +Q9D3V5 FSIP1_MOUSE Fibrous sheath-interacting protein 1 435 48,968 Alternative sequence (2); Chain (1); Coiled coil (1); Modified residue (2); Sequence conflict (8) SUBUNIT: May interact with AKAP4. {ECO:0000305}. TISSUE SPECIFICITY: Detected in male germ cells and testis. {ECO:0000269|PubMed:12606363}. +A2ARZ3 FSIP2_MOUSE Fibrous sheath-interacting protein 2 6995 784,857 Chain (1); Coiled coil (1); Erroneous gene model prediction (2); Modified residue (1) SUBUNIT: May interact with AKAP4. {ECO:0000305}. +Q91WJ8 FUBP1_MOUSE Far upstream element-binding protein 1 (FBP) (FUSE-binding protein 1) 651 68,540 Alternative sequence (1); Beta strand (8); Chain (1); Compositional bias (3); Domain (4); Helix (6); Initiator methionine (1); Modified residue (12); Sequence conflict (1); Turn (1) FUNCTION: Regulates MYC expression by binding to a single-stranded far-upstream element (FUSE) upstream of the MYC promoter. May act both as activator and repressor of transcription (By similarity). {ECO:0000250}. PTM: Ubiquitinated. This targets the protein for proteasome-mediated degradation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Found in a complex with PUF60 and far upstream element (FUSE) DNA segment. Interacts with PUF60 and JTV1 (By similarity). {ECO:0000250}. +Q8C7B6 FXL22_MOUSE F-box and leucine-rich protein 22 236 26,320 Chain (1); Domain (1); Repeat (6) Protein modification; protein ubiquitination. FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. Promotes ubiquitination of sarcomeric proteins alpha-actinin-2 (ACTN2) and filamin-C (FLNC) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:22972877}. SUBUNIT: Directly interacts with SKP1 and CUL1. TISSUE SPECIFICITY: Enriched in cardiac muscle (at protein level). {ECO:0000269|PubMed:22972877}. +Q8CB93 GAPT_MOUSE Protein GAPT (Growth factor receptor-bound protein 2-binding adapter protein, transmembrane) 157 17,601 Chain (1); Compositional bias (1); Transmembrane (1) TRANSMEM 10 30 Helical. {ECO:0000255}. FUNCTION: Negatively regulates B-cell proliferation following stimulation through the B-cell receptor. May play an important role in maintenance of marginal zone (MZ) B-cells. {ECO:0000269|PubMed:18559951}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with GRB2. {ECO:0000250}. TISSUE SPECIFICITY: Expressed primarily in B220+ splenocytes and total bone marrow cells. Expressed at lower levels in mast cells and dendritic cells. Not detected in T-cells and macrophages (at protein level). {ECO:0000269|PubMed:18559951}. +P56479 GALR1_MOUSE Galanin receptor type 1 (GAL1-R) (GALR-1) 348 39,114 Chain (1); Disulfide bond (1); Glycosylation (3); Lipidation (1); Topological domain (8); Transmembrane (7) TRANSMEM 35 55 Helical; Name=1. {ECO:0000255}.; TRANSMEM 71 91 Helical; Name=2. {ECO:0000255}.; TRANSMEM 110 131 Helical; Name=3. {ECO:0000255}.; TRANSMEM 152 172 Helical; Name=4. {ECO:0000255}.; TRANSMEM 198 218 Helical; Name=5. {ECO:0000255}.; TRANSMEM 248 268 Helical; Name=6. {ECO:0000255}.; TRANSMEM 271 291 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 34 Extracellular. {ECO:0000255}.; TOPO_DOM 56 70 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 92 109 Extracellular. {ECO:0000255}.; TOPO_DOM 132 151 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 173 197 Extracellular. {ECO:0000255}.; TOPO_DOM 219 247 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 269 270 Extracellular. {ECO:0000255}.; TOPO_DOM 292 348 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for the hormone galanin. The activity of this receptor is mediated by G proteins that inhibit adenylate cyclase activity. {ECO:0000250|UniProtKB:P47211, ECO:0000269|PubMed:9271210}. PTM: Three cysteine residues are found in the C-terminus, at least one of which may be palmitoylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expression is detected in brain, spinal cord, heart and skeletal muscle. {ECO:0000269|PubMed:9271210}. +Q03249 GALT_MOUSE Galactose-1-phosphate uridylyltransferase (Gal-1-P uridylyltransferase) (EC 2.7.7.12) (UDP-glucose--hexose-1-phosphate uridylyltransferase) 379 43,232 Active site (1); Binding site (3); Chain (1); Erroneous initiation (2); Frameshift (1); Metal binding (6); Region (3); Sequence conflict (10) Carbohydrate metabolism; galactose metabolism. FUNCTION: Plays an important role in galactose metabolism. {ECO:0000250|UniProtKB:P07902}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P07902}. +P17156 HSP72_MOUSE Heat shock-related 70 kDa protein 2 (Heat shock protein 70.2) 633 69,642 Binding site (1); Chain (1); Modified residue (4); Nucleotide binding (4); Region (2); Sequence conflict (2) FUNCTION: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release (By similarity). Plays a role in spermatogenesis (PubMed:24557841). In association with SHCBP1L may participate in the maintenance of spindle integrity during meiosis in male germ cells (PubMed:24557841). {ECO:0000250|UniProtKB:P54652, ECO:0000269|PubMed:24557841}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:24557841}. Note=Colocalizes with SHCBP1L at spindle during the meiosis process (PubMed:24557841). {ECO:0000269|PubMed:24557841}. SUBUNIT: Interacts with FKBP6 (By similarity). Interacts with ZNF541 (PubMed:18849567). Component of the CatSper complex (PubMed:21224844). Interacts with RABL2/RABL2A; binds preferentially to GTP-bound RABL2 (PubMed:23055941). Interacts with SHCBP1L; this interaction may promote the recruitment of HSPA2 to the spindle (PubMed:24557841). Interacts with MOV10L1 (PubMed:20547853). {ECO:0000250|UniProtKB:P54652, ECO:0000269|PubMed:18849567, ECO:0000269|PubMed:20547853, ECO:0000269|PubMed:21224844, ECO:0000269|PubMed:23055941, ECO:0000269|PubMed:24557841}. DOMAIN: The N-terminal nucleotide binding domain (NBD) (also known as the ATPase domain) is responsible for binding and hydrolyzing ATP. The C-terminal substrate-binding domain (SBD) (also known as peptide-binding domain) binds to the client/substrate proteins. The two domains are allosterically coupled so that, when ATP is bound to the NBD, the SBD binds relatively weakly to clients. When ADP is bound in the NBD, a conformational change enhances the affinity of the SBD for client proteins. {ECO:0000250|UniProtKB:P54652}. TISSUE SPECIFICITY: Expressed in male germ cells (at protein level) (PubMed:24557841, PubMed:23055941, PubMed:3405224). {ECO:0000269|PubMed:23055941, ECO:0000269|PubMed:24557841, ECO:0000269|PubMed:3405224}. +O88853 GALR3_MOUSE Galanin receptor type 3 (GAL3-R) (GALR-3) 370 40,420 Chain (1); Compositional bias (2); Disulfide bond (1); Glycosylation (1); Lipidation (1); Sequence conflict (3); Topological domain (8); Transmembrane (7) TRANSMEM 21 41 Helical; Name=1. {ECO:0000255}.; TRANSMEM 58 78 Helical; Name=2. {ECO:0000255}.; TRANSMEM 97 118 Helical; Name=3. {ECO:0000255}.; TRANSMEM 139 159 Helical; Name=4. {ECO:0000255}.; TRANSMEM 185 205 Helical; Name=5. {ECO:0000255}.; TRANSMEM 237 257 Helical; Name=6. {ECO:0000255}.; TRANSMEM 260 280 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 20 Extracellular. {ECO:0000255}.; TOPO_DOM 42 57 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 79 96 Extracellular. {ECO:0000255}.; TOPO_DOM 119 138 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 160 184 Extracellular. {ECO:0000255}.; TOPO_DOM 206 236 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 258 259 Extracellular. {ECO:0000255}.; TOPO_DOM 281 370 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for the hormone galanin and spexin-1. {ECO:0000250|UniProtKB:O60755}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +E9Q7D5 ARHG5_MOUSE Rho guanine nucleotide exchange factor 5 1581 176,664 Chain (1); Compositional bias (2); Domain (3); Modified residue (5) FUNCTION: Guanine nucleotide exchange factor which activates Rho GTPases (PubMed:19713215, PubMed:21525037). Strongly activates RHOA (PubMed:19713215, PubMed:21525037). Also strongly activates RHOB, weakly activates RHOC and RHOG and shows no effect on RHOD, RHOV, RHOQ or RAC1 (PubMed:19713215). Involved in regulation of cell shape and actin cytoskeletal organization (PubMed:21525037). Plays a role in actin organization by generating a loss of actin stress fibers and the formation of membrane ruffles and filopodia (By similarity). Required for SRC-induced podosome formation (PubMed:21525037). Involved in positive regulation of immature dendritic cell migration (PubMed:19713215). {ECO:0000250|UniProtKB:Q12774, ECO:0000269|PubMed:19713215, ECO:0000269|PubMed:21525037}. PTM: Activation of SRC induces tyrosine phosphorylation of ARHGEF5. {ECO:0000269|PubMed:21525037}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q12774}. Cytoplasm {ECO:0000250|UniProtKB:Q12774}. Cell projection, podosome {ECO:0000269|PubMed:21525037}. SUBUNIT: Interacts with SRC (PubMed:21525037). Forms a ternary complex with SRC and the PI3K 85 kDa subunit (PubMed:21525037). Interacts with and is activated by the heterodimer formed by GNB1 and GNG2 (PubMed:19713215). Interacts with ODAM (via C-terminus) (By similarity). Interacts with RHOA (PubMed:19713215). {ECO:0000250|UniProtKB:Q12774, ECO:0000269|PubMed:19713215, ECO:0000269|PubMed:21525037}. DOMAIN: The PH domain binds to phosphoinositides and is essential for podosome formation. {ECO:0000269|PubMed:21525037}. +Q8K4I3 ARHG6_MOUSE Rho guanine nucleotide exchange factor 6 (Alpha-PIX) (Rac/Cdc42 guanine nucleotide exchange factor 6) 771 87,051 Beta strand (10); Chain (1); Domain (4); Helix (1); Modified residue (6); Turn (3) FUNCTION: Acts as a RAC1 guanine nucleotide exchange factor (GEF). {ECO:0000250}. SUBCELLULAR LOCATION: Cell projection, lamellipodium {ECO:0000269|PubMed:18325335}. SUBUNIT: Interacts with PAK kinases through the SH3 domain. Interacts with GIT1. Component of cytoplasmic complexes, which also contain PXN, GIT1 and PAK1. Interacts with BIN2. Identified in a complex with BIN2 and GIT2 (By similarity). Interacts with PARVB. {ECO:0000250, ECO:0000269|PubMed:18325335}. TISSUE SPECIFICITY: Detected in adult heart, spleen, lung, skeletal muscle, kidney and testis. Detected throughout embryogenesis. {ECO:0000269|PubMed:12063400}. +P61211 ARL1_MOUSE ADP-ribosylation factor-like protein 1 181 20,412 Binding site (1); Chain (1); Initiator methionine (1); Lipidation (1); Metal binding (2); Nucleotide binding (5) FUNCTION: GTP-binding protein. Can activate phospholipase D with very low efficiency. Important for normal function of the Golgi apparatus (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Membrane {ECO:0000250|UniProtKB:P40616}; Lipid-anchor {ECO:0000250|UniProtKB:P40616}. SUBUNIT: The GTP-bound form interacts with GOLGA1, GOLGA4 and RGPD8. The GTP-bound form directly interacts with ARFIP2; this interaction leads to an increase in the amount of bound GTP at steady state level. Binds to SCOC, preferentially in its GTP-bound form. May interact with UNC119 (By similarity). {ECO:0000250}. +E9Q7E2 ARID2_MOUSE AT-rich interactive domain-containing protein 2 (ARID domain-containing protein 2) (BRG1-associated factor 200) (BAF200) (Zinc finger protein with activation potential) (Zipzap/p200) 1828 195,988 Chain (1); Cross-link (7); DNA binding (1); Domain (1); Initiator methionine (1); Modified residue (10); Motif (1); Zinc finger (1) FUNCTION: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Required for the stability of the SWI/SNF chromatin remodeling complex SWI/SNF-B (PBAF). May be involved in targeting the complex to different genes. May be involved in regulating transcriptional activation of cardiac genes. {ECO:0000250|UniProtKB:Q68CP9, ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355, ECO:0000255|PROSITE-ProRule:PRU00858}. SUBUNIT: Component of the SWI/SNF-B (PBAF) chromatin remodeling complex, at least composed of SMARCA4/BRG1, SMARCB1/BAF47/SNF5, ACTL6A/BAF53A or ACTL6B/BAF53B, SMARCE1/BAF57, SMARCD1/BAF60A, SMARCD2/BAF60B, perhaps SMARCD3/BAF60C, SMARCC1/BAF155, SMARCC2/BAF170, PBRM1/BAF180, ARID2/BAF200 and actin. Interacts with SRF. Forms complexes with SRF and SRF cofactors MYOCD, NKX2-5 and SRFBP1. {ECO:0000250|UniProtKB:Q68CP9, ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}. TISSUE SPECIFICITY: Highly expressed in testis, expressed in heart, liver and kidney. {ECO:0000269|PubMed:16782067}. +Q8C142 ARH_MOUSE Low density lipoprotein receptor adapter protein 1 (Autosomal recessive hypercholesterolemia protein homolog) 308 33,975 Chain (1); Domain (1); Erroneous initiation (1); Modified residue (4); Motif (2); Region (1); Sequence conflict (3) FUNCTION: Adapter protein (clathrin-associated sorting protein (CLASP)) required for efficient endocytosis of the LDL receptor (LDLR) in polarized cells such as hepatocytes and lymphocytes, but not in non-polarized cells (fibroblasts). May be required for LDL binding and internalization but not for receptor clustering in coated pits. May facilitate the endocytocis of LDLR and LDLR-LDL complexes from coated pits by stabilizing the interaction between the receptor and the structural components of the pits. May also be involved in the internalization of other LDLR family members. Binds to phosphoinositides, which regulate clathrin bud assembly at the cell surface. Required for trafficking of LRP2 to the endocytic recycling compartment which is necessary for LRP2 proteolysis, releasing a tail fragment which translocates to the nucleus and mediates transcriptional repression (By similarity). {ECO:0000250|UniProtKB:D3ZAR1, ECO:0000269|PubMed:12746448, ECO:0000269|PubMed:15166224}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15166224}. SUBUNIT: Interacts (via PID domain) with LDLR (via NPXY motif). Binds to soluble clathrin trimers. Interacts with AP2B1; the interaction mediates the association with the AP-2 complex (By similarity). Interacts with VLDLR (PubMed:12746448). Interacts with LRP2 (By similarity). {ECO:0000250|UniProtKB:D3ZAR1, ECO:0000250|UniProtKB:Q5SW96, ECO:0000269|PubMed:12746448}. DOMAIN: The [DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif mediates interaction the AP-2 complex subunit AP2B1. {ECO:0000250|UniProtKB:Q5SW96}.; DOMAIN: The PID domain mediates interaction with the NPXY internalization motif of LDLR. {ECO:0000250|UniProtKB:D3ZAR1}. +Q9WUL7 ARL3_MOUSE ADP-ribosylation factor-like protein 3 182 20,487 Beta strand (9); Binding site (2); Chain (1); Helix (12); Initiator methionine (1); Lipidation (1); Metal binding (2); Modified residue (1); Mutagenesis (7); Nucleotide binding (4); Turn (2) FUNCTION: Small GTP-binding protein which cycles between an inactive GDP-bound and an active GTP-bound form, and the rate of cycling is regulated by guanine nucleotide exchange factors (GEF) and GTPase-activating proteins (GAP) (PubMed:18376416). Required for normal cytokinesis and cilia signaling. Required for targeting proteins to the cilium, including myristoylated NPHP3 and prenylated INPP5E. Targets NPHP3 to the ciliary membrane by releasing myristoylated NPHP3 from UNC119B cargo adapter into the cilium (By similarity). Requires assistance from GTPase-activating proteins (GAPs) like RP2 and PDE6D, in order to cycle between inactive GDP-bound and active GTP-bound forms (PubMed:15979089). Required for PKD1:PKD2 complex targeting from the trans-Golgi network to the cilium (PubMed:25405894). {ECO:0000250|UniProtKB:P36405, ECO:0000269|PubMed:15979089, ECO:0000269|PubMed:18376416, ECO:0000269|PubMed:25405894}. SUBCELLULAR LOCATION: Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton, spindle. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell projection, cilium {ECO:0000250|UniProtKB:P36405}. Note=Detected predominantly in the photoreceptor connecting cilium. Centrosome-associated throughout the cell cycle. Not detected to interphase microtubules (By similarity). Present on the mitotic spindle. {ECO:0000250}. SUBUNIT: Found in a complex with ARL3, RP2 and UNC119 (or UNC119B); RP2 induces hydrolysis of GTP ARL3 in the complex, leading to the release of UNC119 (or UNC119B). Interacts with RP2; interaction is direct and stimulated with the activated GTP-bound form of ARL3. Interacts with SYS1. Interacts with ARL2BP; the GTP-bound form interacts with ARL2BP. Microtubule-associated protein. Does not interact with TBCC (By similarity). Interacts with RP2 (PubMed:18376416). Interacts with PDE6D; the interaction occurs specifically with the GTP-bound form of ARL3 (PubMed:10518933, PubMed:15979089). Interacts with GGA1; the interaction recruits PKD1:PKD2 complex to trans-Golgi network and is required for ciliary targeting of PKD1:PKD2 complex (PubMed:25405894). {ECO:0000250|UniProtKB:P36405, ECO:0000269|PubMed:10518933, ECO:0000269|PubMed:15979089, ECO:0000269|PubMed:18376416, ECO:0000269|PubMed:25405894}. +Q5FWH6 ARHGF_MOUSE Rho guanine nucleotide exchange factor 15 (Ephexin-5) (E5) 849 92,946 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (1); Modified residue (3); Mutagenesis (5) FUNCTION: Specific GEF for RhoA activation. Does not activate RAC1 or CDC42. Regulates vascular smooth muscle contractility. Negatively regulates excitatory synapse development by suppressing the synapse-promoting activity of EPHB2. {ECO:0000269|PubMed:21029865}. PTM: Phosphorylated on tyrosine residues upon EFNA1 stimulation. EPHB2-dependent phosphorylation at Tyr-361 triggers UBE3A-mediated ubiquitination. {ECO:0000269|PubMed:21029865}.; PTM: Ubiquitinated; UBE3A-mediated ubiquitination and degradation by the proteasome promotes EFNB1-dependent synapse formation. {ECO:0000269|PubMed:21029865}. SUBCELLULAR LOCATION: Cell projection, dendrite {ECO:0000269|PubMed:21029865}. Note=Expressed exclusively in dendrites of the developing hippocampus. SUBUNIT: Interacts with EPHA4 (By similarity). Interacts with EPHB2. {ECO:0000250, ECO:0000269|PubMed:21029865}. TISSUE SPECIFICITY: At P12, expressed is detected in the CA1 region and the dentate gyrus of the hippocampus. {ECO:0000269|PubMed:21029865}. +Q8CG76 ARK72_MOUSE Aflatoxin B1 aldehyde reductase member 2 (EC 1.1.1.n11) (Succinic semialdehyde reductase) (SSA reductase) 367 40,612 Active site (1); Beta strand (9); Binding site (7); Chain (1); Erroneous initiation (3); Helix (18); Modified residue (4); Nucleotide binding (3); Sequence conflict (8); Site (1); Turn (3) FUNCTION: Catalyzes the NADPH-dependent reduction of succinic semialdehyde to gamma-hydroxybutyrate. May have an important role in producing the neuromodulator gamma-hydroxybutyrate (GHB). Has broad substrate specificity. Can reduce the dialdehyde protein-binding form of aflatoxin B1 (AFB1) to the non-binding AFB1 dialcohol. May be involved in protection of liver against the toxic and carcinogenic effects of AFB1, a potent hepatocarcinogen (By similarity). {ECO:0000250, ECO:0000269|PubMed:16460003}. SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250}. Cytoplasm {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000269|PubMed:16460003}. TISSUE SPECIFICITY: Expressed in liver, kidney, testis and brain with low levels in skeletal muscle, spleen, heart and lung. {ECO:0000269|PubMed:12123834}. +Q80U35 ARHGH_MOUSE Rho guanine nucleotide exchange factor 17 2057 221,671 Alternative sequence (2); Chain (1); Compositional bias (7); Domain (1); Erroneous initiation (1); Modified residue (22); Sequence conflict (2) FUNCTION: Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPases. {ECO:0000250}. +P61213 ARL4A_MOUSE ADP-ribosylation factor-like protein 4A 200 22,588 Chain (1); Initiator methionine (1); Lipidation (1); Nucleotide binding (3) FUNCTION: Small GTP-binding protein which cycles between an inactive GDP-bound and an active GTP-bound form, and the rate of cycling is regulated by guanine nucleotide exchange factors (GEF) and GTPase-activating proteins (GAP). GTP-binding protein that does not act as an allosteric activator of the cholera toxin catalytic subunit. Recruits CYTH1, CYTH2, CYTH3 and CYTH4 to the plasma membrane in GDP-bound form (By similarity). {ECO:0000250}. PTM: Myristoylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Cytoplasm {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Note=Localization in the nucleolus is dependent by nucleotide binding. {ECO:0000250}. SUBUNIT: Interacts with CYTH2. Interacts with KPNA2; the interaction is direct. Does not interacts with ARL4A (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed strongly in testis and liver. Expressed slightly in heart, spleen, lung and kidney. {ECO:0000269|PubMed:10980193}. +Q8BWA8 ARHGJ_MOUSE Rho guanine nucleotide exchange factor 19 (Ephexin-2) (Weakly similar to Rho GEF 5) 802 88,851 Chain (1); Domain (3); Sequence conflict (1) FUNCTION: Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPase. {ECO:0000269|PubMed:15485661}. TISSUE SPECIFICITY: Highly expressed in intestine, and at lower levels in liver, heart and kidney. {ECO:0000269|PubMed:15485661}. +P61208 ARL4C_MOUSE ADP-ribosylation factor-like protein 4C (ADP-ribosylation factor-like 7) 192 21,487 Chain (1); Initiator methionine (1); Lipidation (1); Nucleotide binding (3) FUNCTION: Small GTP-binding protein which cycles between an inactive GDP-bound and an active GTP-bound form, and the rate of cycling is regulated by guanine nucleotide exchange factors (GEF) and GTPase-activating proteins (GAP). GTP-binding protein that does not act as an allosteric activator of the cholera toxin catalytic subunit. May be involved in transport between a perinuclear compartment and the plasma membrane, apparently linked to the ABCA1-mediated cholesterol secretion pathway. Recruits CYTH1, CYTH2, CYTH3 and CYTH4 to the plasma membrane in the GDP-bound form. Regulates the microtubule-dependent intracellular vesicular transport from early endosome to recycling endosome process (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell projection, filopodium {ECO:0000250}. Cell membrane {ECO:0000250}. Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with CYTH2. Interacts with alpha tubulin; interaction is independent on the ARL4C GTP or GDP binding status (By similarity). {ECO:0000250}. +Q99PE9 ARL4D_MOUSE ADP-ribosylation factor-like protein 4D (ADP-ribosylation factor-like protein 4L) (ADP-ribosylation factor-like protein 5) 201 22,270 Chain (1); Initiator methionine (1); Lipidation (1); Nucleotide binding (3); Sequence conflict (7) FUNCTION: Small GTP-binding protein which cycles between an inactive GDP-bound and an active GTP-bound form, and the rate of cycling is regulated by guanine nucleotide exchange factors (GEF) and GTPase-activating proteins (GAP). GTP-binding protein that does not act as an allosteric activator of the cholera toxin catalytic subunit. Recruits CYTH1, CYTH2, CYTH3 and CYTH4 to the plasma membrane in GDP-bound form (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:12414990}. Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with CYTH2; the interaction is direct and ARL4D GTP-dependent. Does not interact with ARL4D (By similarity). {ECO:0000250}. +O88848 ARL6_MOUSE ADP-ribosylation factor-like protein 6 186 20,959 Alternative sequence (1); Binding site (3); Chain (1); Initiator methionine (1); Lipidation (1); Metal binding (1); Nucleotide binding (3) FUNCTION: Involved in membrane protein trafficking at the base of the ciliary organelle (By similarity). Mediates recruitment onto plasma membrane of the BBSome complex which would constitute a coat complex required for sorting of specific membrane proteins to the primary cilia (By similarity). Together with BBS1, is necessary for correct trafficking of PKD1 to primary cilia (PubMed:24939912). Together with the BBSome complex and LTZL1, controls SMO ciliary trafficking and contributes to the sonic hedgehog (SHH) pathway regulation (By similarity). May regulate cilia assembly and disassembly and subsequent ciliary signaling events such as the Wnt signaling cascade (By similarity). Isoform 2 may be required for proper retinal function and organization (PubMed:20333246). {ECO:0000250|UniProtKB:Q9H0F7, ECO:0000269|PubMed:20333246, ECO:0000269|PubMed:24939912}. SUBCELLULAR LOCATION: Cell projection, cilium membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250}. Note=Appears in a pattern of punctae flanking the microtubule axoneme that likely correspond to small membrane-associated patches. Localizes to the so-called ciliary gate where vesicles carrying ciliary cargo fuse with the membrane (By similarity). {ECO:0000250}. SUBUNIT: Interacts with SEC61B, ARL6IP1, ARL6IP2, ARL6IP3, ARL6IP4 ARL6IP5 and ARL6IP6. Interacts (GTP-bound form) with the BBSome a complex that contains BBS1, BBS2, BBS4, BBS5, BBS7, BBS8/TTC8, BBS9 and BBIP10. Interacts (GTP-free form) with IFT27. {ECO:0000250|UniProtKB:Q9H0F7}. TISSUE SPECIFICITY: Most abundant in brain and kidney. Expressed in heart and eye. Isoform 2 is expressed only in the retina. {ECO:0000269|PubMed:20333246}. +A6PWV5 ARI3C_MOUSE AT-rich interactive domain-containing protein 3C (ARID domain-containing protein 3C) 409 43,633 Chain (1); Compositional bias (2); Domain (2); Erroneous gene model prediction (1) SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +A2CG63 ARI4B_MOUSE AT-rich interactive domain-containing protein 4B (ARID domain-containing protein 4B) (180 kDa Sin3-associated polypeptide) (Sin3-associated polypeptide p180) (Histone deacetylase complex subunit SAP180) 1314 147,643 Alternative sequence (1); Chain (1); Coiled coil (1); Compositional bias (4); Cross-link (3); Domain (1); Erroneous gene model prediction (1); Modified residue (19) FUNCTION: Acts as a transcriptional repressor. May function in the assembly and/or enzymatic activity of the Sin3A corepressor complex or in mediating interactions between the complex and other regulatory complexes (By similarity). Plays a role in the regulation of epigenetic modifications at the PWS/AS imprinting center near the SNRPN promoter, where it might function as part of a complex with RB1 and ARID4A (PubMed:17043311). Involved in spermatogenesis, together with ARID4A, where it functions as a transcriptional coactivator for AR (androgen receptor) and enhances expression of genes required for sperm maturation. Regulates expression of the tight junction protein CLDN3 in the testis, which is important for integrity of the blood-testis barrier (PubMed:23487765). Plays a role in myeloid homeostasis where it regulates the histone methylation state of bone marrow cells and expression of various genes involved in hematopoiesis. May function as a leukemia suppressor (PubMed:18728284). {ECO:0000250|UniProtKB:Q4LE39, ECO:0000269|PubMed:17043311, ECO:0000269|PubMed:18728284, ECO:0000269|PubMed:23487765}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355}. SUBUNIT: Component of a Sin3A corepressor complex consisting of SIN3A, SAP130, SUDS3/SAP45, SAP180, HDAC1 and HDAC2 (By similarity). Interacts with ARID4A (PubMed:17043311). Interacts with AR (PubMed:23487765). {ECO:0000250|UniProtKB:Q4LE39, ECO:0000269|PubMed:17043311, ECO:0000269|PubMed:23487765}. DOMAIN: The C-terminus mediates interaction with mSin3A corepressor complex. {ECO:0000250|UniProtKB:Q4LE39}.; DOMAIN: The N-terminus is involved in transcriptional repression by HDAC-independent mechanisms. {ECO:0000250|UniProtKB:Q4LE39}.; DOMAIN: The ARID domain is involved in stabilizing the mSin3A corepressor complex on DNA. {ECO:0000250|UniProtKB:Q4LE39}. TISSUE SPECIFICITY: Expressed in Sertoli cells of the testis. {ECO:0000269|PubMed:23487765}. +Q3U108 ARI5A_MOUSE AT-rich interactive domain-containing protein 5A (ARID domain-containing protein 5A) 590 63,898 Alternative sequence (5); Chain (1); Cross-link (2); Domain (1); Modified residue (5); Mutagenesis (4); Region (1); Sequence conflict (4) FUNCTION: DNA-binding protein that may regulate transcription and act as a repressor by binding to AT-rich stretches in the promoter region of target genes (By similarity). May positively regulate chondrocyte-specific transcription such as of COL2A1 in collaboration with SOX9 and positively regulate histone H3 acetylation at chondrocyte-specific genes. May stimulate early-stage chondrocyte differentiation and inhibit later stage differention (PubMed:21346191). Can repress ESR1-mediated transcriptional activation; proposed to act as corepressor for selective nuclear hormone receptors (By similarity). As RNA-binding protein involved in the regulation of inflammatory response by stabilizing selective inflammation-related mRNAs, such as IL6, STAT3 and TBX21. Binds to stem loop structures located in the 3'UTRs of IL6, STAT3 and TBX21 mRNAs; at least for STAT3 prevents binding of ZC3H12A to the mRNA stem loop structure thus inhibiting its degradation activity. Contributes to elevated IL6 levels possibly implicated in autoimmunity processes. IL6-dependent stabilization of STAT3 mRNA may promote differentiation of naive CD4+ T-cells into T-helper Th17 cells (PubMed:23676272, PubMed:27022145). In CD4+ T-cells may also inhibit RORC-induced Th17 cell differentiation independently of IL6 signaling (PubMed:24782182). Stabilization of TBX21 mRNA contributes to elevated interferon-gamma secretion in Th1 cells possibly implicated in the establishment of septic shock (PubMed:27671645). {ECO:0000250|UniProtKB:Q03989, ECO:0000269|PubMed:21346191, ECO:0000269|PubMed:23676272, ECO:0000269|PubMed:24782182, ECO:0000269|PubMed:27022145, ECO:0000269|PubMed:27671645}. PTM: Phosphorylated by MAPK14 on serine residues involving a TLR4 signaling pathway upon lipopolysaccharide (LPS) stimulation leading to its ubiquitination and proteasomal degradation. {ECO:0000269|PubMed:28168301}.; PTM: Ubiquitinated leading to proteasomal degradation; involving WWP1 linked to MAPK14-mediated phosphorylation upon LPS stimulation. {ECO:0000269|PubMed:28168301}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355, ECO:0000269|PubMed:21346191}. SUBUNIT: Interacts with SOX9 (PubMed:21346191). Interacts with ESR1 (By similarity). Interacts with RORC (PubMed:24782182). {ECO:0000250|UniProtKB:Q03989, ECO:0000269|PubMed:21346191, ECO:0000269|PubMed:24782182}. TISSUE SPECIFICITY: Expressed at high levels in cartilage, heart, testis and bone. {ECO:0000269|PubMed:21346191}. +O55226 CHAD_MOUSE Chondroadherin (Cartilage leucine-rich protein) 358 40,349 Chain (1); Disulfide bond (3); Domain (2); Glycosylation (1); Repeat (10); Signal peptide (1) FUNCTION: Promotes attachment of chondrocytes, fibroblasts, and osteoblasts. This binding is mediated (at least for chondrocytes and fibroblasts) by the integrin alpha(2)beta(1). May play an important role in the regulation of chondrocyte growth and proliferation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. SUBUNIT: Mostly monomeric. Interacts with collagen type II (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Cartilage. +Q8CBW7 CHIC1_MOUSE Cysteine-rich hydrophobic domain-containing protein 1 (Brain X-linked protein) 227 25,791 Chain (1); Coiled coil (1); Compositional bias (4); Frameshift (2); Sequence conflict (1) PTM: Palmitoylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Note=Also present at a Golgi-like vesicular compartment and at scattered vesicles. {ECO:0000250}. TISSUE SPECIFICITY: Expressed moderately in the brain. {ECO:0000269|PubMed:9321471}. +Q9D9G3 CHIC2_MOUSE Cysteine-rich hydrophobic domain-containing protein 2 165 19,282 Chain (1); Coiled coil (1); Compositional bias (1); Motif (1); Sequence conflict (1) PTM: Palmitoylation in the CHIC motif is required for membrane association. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Golgi apparatus {ECO:0000250}. Note=Associated and found in vesicular structures of Golgi complex. {ECO:0000250}. +Q91V57 CHIN_MOUSE N-chimaerin (A-chimaerin) (Alpha-chimerin) (N-chimerin) (NC) (Rho GTPase-activating protein 2) 459 53,193 Alternative sequence (2); Chain (1); Domain (2); Initiator methionine (1); Modified residue (3); Sequence conflict (3); Zinc finger (1) FUNCTION: GTPase-activating protein for p21-rac and a phorbol ester receptor. May play an important role in neuronal signal-transduction mechanisms (By similarity). Involved in the assembly of neuronal locomotor circuits as a direct effector of EPHA4 in axon guidance. {ECO:0000250, ECO:0000269|PubMed:17785183}. PTM: Phosphorylated. Phosphorylation is EPHA4 kinase activity-dependent. {ECO:0000269|PubMed:17785183}. SUBUNIT: Interacts with EPHA4; effector of EPHA4 in axon guidance linking EPHA4 activation to RAC1 regulation. May also interact with EPHB1 and EPHB2. {ECO:0000269|PubMed:17719550, ECO:0000269|PubMed:17785183}. +Q80XD1 CHIO_MOUSE Beta-chimaerin (Beta-chimerin) (Rho GTPase-activating protein 3) 332 38,218 Alternative sequence (4); Chain (1); Domain (1); Frameshift (1); Sequence conflict (1); Zinc finger (1) FUNCTION: GTPase-activating protein for p21-rac. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. +Q9WUD1 CHIP_MOUSE STIP1 homology and U box-containing protein 1 (EC 2.3.2.27) (Carboxy terminus of Hsp70-interacting protein) (E3 ubiquitin-protein ligase CHIP) (RING-type E3 ubiquitin transferase CHIP) 304 34,909 Beta strand (2); Chain (1); Compositional bias (1); Cross-link (4); Domain (1); Helix (15); Modified residue (5); Mutagenesis (5); Repeat (3); Sequence conflict (1); Turn (4) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase which targets misfolded chaperone substrates towards proteasomal degradation. Collaborates with ATXN3 in the degradation of misfolded chaperone substrates: ATXN3 restricting the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension. Ubiquitinates NOS1 in concert with Hsp70 and Hsp40. Modulates the activity of several chaperone complexes, including Hsp70, Hsc70 and Hsp90. Mediates transfer of non-canonical short ubiquitin chains to HSPA8 that have no effect on HSPA8 degradation. Mediates polyubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base-excision repair: catalyzes polyubiquitination by amplifying the HUWE1/ARF-BP1-dependent monoubiquitination and leading to POLB-degradation by the proteasome. Mediates polyubiquitination of CYP3A4. Ubiquitinates EPHA2 and may regulate the receptor stability and activity through proteasomal degradation. Negatively regulates the suppressive function of regulatory T-cells (Treg) during inflammation by mediating the ubiquitination and degradation of FOXP3 in a HSPA1A/B-dependent manner (PubMed:23973223). Acts as a co-chaperone for HSPA1A and HSPA1B chaperone proteins and promotes ubiquitin-mediated protein degradation. Likely mediates polyubiquitination and downregulates plasma membrane expression of PD-L1/CD274, an immune inhibitory ligand critical for immune tolerance to self and antitumor immunity. Negatively regulates TGF-beta signaling by modulating the basal level of SMAD3 via ubiquitin-mediated degradation (By similarity). May regulate myosin assembly in striated muscles together with UBE4B and VCP/p97 by targeting myosin chaperone UNC45B for proteasomal degradation (By similarity). Mediates ubiquitination of RIPK3 leading to its subsequent proteasome-dependent degradation (By similarity). {ECO:0000250|UniProtKB:Q9UNE7, ECO:0000269|PubMed:11435423, ECO:0000269|PubMed:21855799, ECO:0000269|PubMed:23973223}. PTM: Auto-ubiquitinated; mediated by UBE2D1 and UBE2D2. Monoubiquitinated at Lys-2 following cell stress by UBE2W, promoting the interaction with ATXN3. {ECO:0000269|PubMed:21855799}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11435423}. Nucleus {ECO:0000250|UniProtKB:Q9UNE7}. Note=Translocates to the nucleus in response to inflammatory signals in regulatory T-cells (Treg). {ECO:0000250|UniProtKB:Q9UNE7}. SUBUNIT: Homodimer (PubMed:16307917). Interacts with BAG2, and with the E2 ubiquitin conjugating enzymes UBE2D1, UBE2D2 and UBE2D3. Detected in a ternary complex containing STUB1, HSPA1A and HSPBP1. Interacts with MKKS. Interacts with DNAAF4 and POLB (By similarity). Interacts (via the U-box domain) with the UBE2V2-UBE2N heterodimer; the complex has a specific 'Lys-63'-linked polyubiquitination activity (PubMed:16307917). Interacts (when monoubiquitinated) with ATXN3 (PubMed:21855799). Interacts with UBE2W (PubMed:21855799). Interacts with DNAJB6 (By similarity). Interacts with FOXP3 (PubMed:23973223). Interacts with FLCN and HSP90AA1. Interacts with HSP90. Interacts with UBE2N and UBE2V1. Interacts (via TPR repeats) with the C-terminal domains of HSPA8 and HSPA1A. Interacts with the non-acetylated form of HSPA1A and HSPA1B. Interacts with SMAD3 and HSP90AB1 (By similarity). Interacts with UBE4B (By similarity). Interacts with RIPK3 (By similarity). {ECO:0000250|UniProtKB:Q9UNE7, ECO:0000269|PubMed:16307917, ECO:0000269|PubMed:21855799, ECO:0000269|PubMed:23973223}. DOMAIN: The U-box domain is required for the ubiquitin protein ligase activity. {ECO:0000269|PubMed:11435423}.; DOMAIN: The TPR domain is essential for ubiquitination mediated by UBE2D1. {ECO:0000250|UniProtKB:Q9UNE7}. +Q61548 AP180_MOUSE Clathrin coat assembly protein AP180 (91 kDa synaptosomal-associated protein) (Clathrin coat-associated protein AP180) (Phosphoprotein F1-20) 901 91,851 Alternative sequence (2); Chain (1); Compositional bias (5); Domain (1); Glycosylation (1); Modified residue (12) FUNCTION: Adaptins are components of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. Binding of AP180 to clathrin triskelia induces their assembly into 60-70 nm coats. PTM: Thr-310 can be modified by the addition of N-acetylglucosamine which can be further phosphorylated. There is no evidence for direct Thr-310 phosphorylation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane. Membrane, coated pit; Peripheral membrane protein; Cytoplasmic side. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles in the plasma membrane. SUBUNIT: Binds AP2A2. Interacts with AP2B1; clathrin competes with SNAP91 (By similarity). {ECO:0000250}. DOMAIN: Possesses a three domain structure: the N-terminal 300 residues harbor a clathrin binding site, an acidic middle domain 450 residues, interrupted by an Ala-rich segment, and the C-terminal domain (166 residues). TISSUE SPECIFICITY: Brain. Associated with the synapses. +Q7TN05 AP1S3_MOUSE AP-1 complex subunit sigma-3 (Adaptor protein complex AP-1 subunit sigma-1C) (Adaptor-related protein complex 1 subunit sigma-1C) (Clathrin assembly protein complex 1 sigma-1C small chain) (Golgi adaptor HA1/AP1 adaptin sigma-1C subunit) (Sigma 1C subunit of AP-1 clathrin) (Sigma-adaptin 1C) (Sigma1C-adaptin) 154 18,440 Chain (1) FUNCTION: Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules (By similarity). Involved in TLR3 trafficking (By similarity). {ECO:0000250|UniProtKB:Q96PC3}. SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Membrane, clathrin-coated pit {ECO:0000250}. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex. {ECO:0000250}. SUBUNIT: Adaptor protein complex 1 (AP-1) is a heterotetramer composed of two large adaptins (gamma-type subunit AP1G1 and beta-type subunit AP1B1), a medium adaptin (mu-type subunit AP1M1 or AP1M2) and a small adaptin (sigma-type subunit AP1S1 or AP1S2 or AP1S3). {ECO:0000250}. +P84091 AP2M1_MOUSE AP-2 complex subunit mu (AP-2 mu chain) (Adaptor protein complex AP-2 subunit mu) (Adaptor-related protein complex 2 subunit mu) (Clathrin assembly protein complex 2 mu medium chain) (Clathrin coat assembly protein AP50) (Clathrin coat-associated protein AP50) (Mu2-adaptin) (Plasma membrane adaptor AP-2 50 kDa protein) 435 49,655 Binding site (5); Chain (1); Domain (1); Modified residue (2) FUNCTION: Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. The AP-2 mu subunit binds to transmembrane cargo proteins; it recognizes the Y-X-X-Phi motifs. The surface region interacting with to the Y-X-X-Phi motif is inaccessible in cytosolic AP-2, but becomes accessible through a conformational change following phosphorylation of AP-2 mu subunit at 'Tyr-156' in membrane-associated AP-2. The membrane-specific phosphorylation event appears to involve assembled clathrin which activates the AP-2 mu kinase AAK1 (By similarity). Plays a role in endocytosis of frizzled family members upon Wnt signaling (By similarity). {ECO:0000250, ECO:0000269|PubMed:14745134, ECO:0000269|PubMed:15473838}. PTM: Phosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane. Membrane, coated pit; Peripheral membrane protein; Cytoplasmic side. Note=AP-2 appears to be excluded from internalizing CCVs and to disengage from sites of endocytosis seconds before internalization of the nascent CCV. {ECO:0000250}. SUBUNIT: Adaptor protein complex 2 (AP-2) is a heterotetramer composed of two large adaptins (alpha-type subunit AP2A1 or AP2A2 and beta-type subunit AP2B1), a medium adaptin (mu-type subunit AP2M1) and a small adaptin (sigma-type subunit AP2S1) (By similarity). Interacts with ATP6V1H and MEGF10 (By similarity). Interacts with EGFR and TTGN1 (By similarity). Interacts with F2R (By similarity). Interacts with PIP5K1C isoform 1; tyrosine phosphorylation of PIP5K1C weakens the interaction. Does not interact with PIP5K1C isoform 3 (PubMed:16707488). Interacts with KIAA0319; required for clathrin-mediated endocytosis of KIAA0319 (By similarity). Interacts with DVL2 (via DEP domain) (By similarity). Interacts with KCNQ1; mediates estrogen-induced internalization via clathrin-coated vesicles (By similarity). Interacts with P2RX4 (via internalization motif) (By similarity). {ECO:0000250|UniProtKB:P84092, ECO:0000250|UniProtKB:Q96CW1, ECO:0000269|PubMed:16707488}. TISSUE SPECIFICITY: Detected in spleen. +P08226 APOE_MOUSE Apolipoprotein E (Apo-E) 311 35,867 Chain (1); Helix (7); Modified residue (2); Region (7); Repeat (8); Sequence conflict (1); Signal peptide (1); Turn (1) FUNCTION: APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apoliproteins are amphipathic molecules that interact both with lipids of the lipoprotein particle core and the aqueous environment of the plasma. As such, APOE associates with chylomicrons, chylomicron remnants, very low density lipoproteins (VLDL) and intermediate density lipoproteins (IDL) but shows a preferential binding to high-density lipoproteins (HDL). It also binds a wide range of cellular receptors including the LDL receptor/LDLR and the very low-density lipoprotein receptor/VLDLR that mediate the cellular uptake of the APOE-containing lipoprotein particles (By similarity). Finally, APOE has also a heparin-binding activity and binds heparan-sulfate proteoglycans on the surface of cells, a property that supports the capture and the receptor-mediated uptake of APOE-containing lipoproteins by cells (PubMed:23676495). {ECO:0000250|UniProtKB:P02649, ECO:0000269|PubMed:23676495}. PTM: APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific. {ECO:0000269|PubMed:29516132}.; PTM: Glycated in plasma VLDL. {ECO:0000250|UniProtKB:P02649}.; PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000250|UniProtKB:P02649}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P02649}. Note=In the plasma, APOE is associated with chylomicrons, chylomicrons remnants, VLDL, LDL and HDL lipoproteins. Lipid poor oligomeric APOE is associated with the extracellular matrix in a calcium- and heparan-sulfate proteoglycans-dependent manner. Lipidation induces the release from the extracellular matrix. {ECO:0000250|UniProtKB:P02649}. SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P02649}. +Q9JJJ3 AQP9_MOUSE Aquaporin-9 (AQP-9) (Aquaglyceroporin-9) 295 31,764 Chain (1); Motif (2); Topological domain (7); Transmembrane (6) TRANSMEM 30 50 Helical. {ECO:0000255}.; TRANSMEM 55 75 Helical. {ECO:0000255}.; TRANSMEM 111 131 Helical. {ECO:0000255}.; TRANSMEM 159 179 Helical. {ECO:0000255}.; TRANSMEM 190 210 Helical. {ECO:0000255}.; TRANSMEM 246 266 Helical. {ECO:0000255}. TOPO_DOM 1 29 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 51 54 Extracellular. {ECO:0000255}.; TOPO_DOM 76 110 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 132 158 Extracellular. {ECO:0000255}.; TOPO_DOM 180 189 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 211 245 Extracellular. {ECO:0000255}.; TOPO_DOM 267 295 Cytoplasmic. {ECO:0000255}. FUNCTION: Forms a channel with a broad specificity. Mediates passage of a wide variety of non-charged solutes including carbamides, polyols, purines, and pyrimidines in a phloretin- and mercury-sensitive manner, whereas amino acids, cyclic sugars, Na(+), K(+), Cl(-), and deprotonated monocarboxylates are excluded. Also permeable to urea and glycerol (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. DOMAIN: Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA). +Q66JY6 ARG39_MOUSE Rho guanine nucleotide exchange factor 39 344 39,106 Alternative sequence (1); Chain (1); Domain (2); Sequence conflict (1) FUNCTION: Promotes cell proliferation. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. +Q8VEH3 ARL8A_MOUSE ADP-ribosylation factor-like protein 8A (ADP-ribosylation factor-like protein 10B) (Novel small G protein indispensable for equal chromosome segregation 2) 186 21,390 Chain (1); Intramembrane (1); Nucleotide binding (3) INTRAMEM 1 19 Note=Mediates targeting to membranes. {ECO:0000250}. FUNCTION: May play a role in lysosomes motility. Alternatively, may play a role in chromosome segregation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250}. Lysosome membrane {ECO:0000250}. +E9Q7T7 CHADL_MOUSE Chondroadherin-like protein 748 81,361 Chain (1); Disulfide bond (3); Domain (4); Glycosylation (2); Repeat (19); Signal peptide (1) FUNCTION: Potential negative modulator of chondrocyte differentiation. Inhibits collagen fibrillogenesis in vitro. May influence chondrocyte's differentiation by acting on its cellular collagenous microenvironment. {ECO:0000269|PubMed:25451920}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:25451920}. SUBUNIT: Associates with collagen and binds to collagen fibrils. {ECO:0000250|UniProtKB:Q6NUI6}. TISSUE SPECIFICITY: Expressed in cartilage, including articular knee cartilage, where it localizes to the extracellular space in the area immediately surrounding the chondrocytes, not detected in any other tissues (at protein level). {ECO:0000269|PubMed:25451920}. +Q5EBP3 ARMC5_MOUSE Armadillo repeat-containing protein 5 926 96,728 Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (2); Modified residue (1); Repeat (7) FUNCTION: Involved in fetal development, T-cell function and adrenal gland growth homeostasis (PubMed:28169274). Negatively regulates adrenal cells survival. Plays a role in steroidogenesis, modulates steroidogenic enzymes expression and cortisol production (By similarity). {ECO:0000250|UniProtKB:Q96C12, ECO:0000269|PubMed:28169274}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28169274}. TISSUE SPECIFICITY: Expression is high in the thymus, stomach, bone marrow and lymphatic tissues (including lymph nodes and intestinal wall). Also expressed in the adrenal gland, skin and in brain structures, with noticeable levels found in the cerebellum. {ECO:0000269|PubMed:28169274}. +Q8BNU0 ARMC6_MOUSE Armadillo repeat-containing protein 6 468 50,683 Alternative sequence (2); Chain (1); Frameshift (1); Modified residue (1); Repeat (4); Sequence conflict (1) +A6H630 ARMT1_MOUSE Protein-glutamate O-methyltransferase (EC 2.1.1.-) (Acidic residue methyltransferase 1) 439 50,549 Alternative sequence (7); Binding site (2); Chain (1); Initiator methionine (1); Modified residue (3) FUNCTION: O-methyltransferase that methylates glutamate residues of target proteins to form gamma-glutamyl methyl ester residues. Methylates PCNA, suggesting it is involved in the DNA damage response. {ECO:0000250|UniProtKB:Q9H993}. PTM: Automethylated. {ECO:0000250|UniProtKB:Q9H993}. +Q9DBR3 ARMC8_MOUSE Armadillo repeat-containing protein 8 673 75,364 Alternative sequence (3); Chain (1); Initiator methionine (1); Modified residue (3); Repeat (14) FUNCTION: Component of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1. {ECO:0000250|UniProtKB:Q8IUR7}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8IUR7}. Cytoplasm {ECO:0000250|UniProtKB:Q8IUR7}. SUBUNIT: Identified in the CTLH complex that contains GID4, RANBP9 and/or RANBP10, MKLN1, MAEA, RMND5A (or alternatively its paralog RMND5B), GID8, ARMC8, WDR26 and YPEL5. Within this complex, MAEA, RMND5A (or alternatively its paralog RMND5B), GID8, WDR26, and RANBP9 and/or RANBP10 form the catalytic core, while GID4, MKLN1, ARMC8 and YPEL5 have ancillary roles. {ECO:0000250|UniProtKB:Q8IUR7}. +Q6PD19 ARMD3_MOUSE Armadillo-like helical domain-containing protein 3 689 78,632 Alternative sequence (3); Chain (1); Sequence caution (1); Transmembrane (1) TRANSMEM 520 538 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. SUBUNIT: Interacts with PI4KB. {ECO:0000250|UniProtKB:Q5T2E6}. +Q8BHS6 ARMX3_MOUSE Armadillo repeat-containing X-linked protein 3 379 42,620 Chain (1); Modified residue (4); Region (3); Repeat (3); Sequence conflict (4); Topological domain (2); Transmembrane (1) TRANSMEM 7 29 Helical; Signal-anchor. {ECO:0000255}. TOPO_DOM 1 6 Mitochondrial intermembrane. {ECO:0000305|PubMed:19304657}.; TOPO_DOM 30 379 Cytoplasmic. {ECO:0000269|PubMed:19304657}. FUNCTION: Regulates mitochondrial aggregation and transport in axons in living neurons (PubMed:22569362, PubMed:23844091). May link mitochondria to the Trak2-kinesin motor complex via its interaction with Miro and Trak2 (PubMed:22569362). Mitochondrial distribution and dynamics is regulated through Armcx3 protein degradation, which is promoted by PCK and negatively regulated by Wnt1 (PubMed:23844091). Enhances the Sox10-mediated transactivation of the neuronal acetylcholine receptor subunit alpha-3 and beta-4 subunit gene promoters (PubMed:19304657). {ECO:0000269|PubMed:19304657, ECO:0000269|PubMed:22569362, ECO:0000269|PubMed:23844091}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:19304657, ECO:0000269|PubMed:22569362}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:22569362}. Nucleus {ECO:0000269|PubMed:22569362}. SUBUNIT: Interacts (via ARM domain) with MIRO1, MIRO2 and TRAK2. The interaction with Miro is calcium-dependent (PubMed:22569362). Interacts with Sox10 (PubMed:19304657). {ECO:0000269|PubMed:19304657, ECO:0000269|PubMed:22569362}. TISSUE SPECIFICITY: Highly expressed in the developing neural tissues, neural crest derivatives and hind limbs. Also widely expressed in the adult nervous tissue, especially in the forebrain, including the cerebral cortex, hippocampus and thalamus. {ECO:0000269|PubMed:22569362}. +E9PZM4 CHD2_MOUSE Chromodomain-helicase-DNA-binding protein 2 (CHD-2) (EC 3.6.4.12) (ATP-dependent helicase CHD2) 1827 210,804 Chain (1); Compositional bias (6); Domain (4); Modified residue (9); Motif (1); Nucleotide binding (1) FUNCTION: DNA-binding helicase that specifically binds to the promoter of target genes, leading to chromatin remodeling, possibly by promoting deposition of histone H3.3. Involved in myogenesis via interaction with MYOD1: binds to myogenic gene regulatory sequences and mediates incorporation of histone H3.3 prior to the onset of myogenic gene expression, promoting their expression. {ECO:0000269|PubMed:22569126}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22569126}. Note=Binds to myogenic gene promoters. SUBUNIT: Interacts with MYOD1. Interacts with histone H3.3. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:16810678}. +A2AJK6 CHD7_MOUSE Chromodomain-helicase-DNA-binding protein 7 (CHD-7) (EC 3.6.4.12) (ATP-dependent helicase CHD7) 2986 334,061 Alternative sequence (3); Chain (1); Coiled coil (1); Compositional bias (8); Domain (4); Erroneous initiation (1); Frameshift (1); Modified residue (21); Motif (1); Nucleotide binding (1); Sequence conflict (4) FUNCTION: Probable transcription regulator. Maybe involved in the in 45S precursor rRNA production (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9P2D1}. SUBUNIT: May interact with CTCF. Interacts with CHD8. Interacts with FAM124B. Found in a complex composed of AGO2, CHD7 and FAM172A (PubMed:29311329). {ECO:0000250|UniProtKB:Q9P2D1, ECO:0000269|PubMed:29311329}. TISSUE SPECIFICITY: Expressed in the outflow tract of the heart, optic vesicle, facio-acoustic preganglion complex, brain, olfactory pit, and mandibular component of the first branchial arch. {ECO:0000269|PubMed:16400610}. +Q8BYH8 CHD9_MOUSE Chromodomain-helicase-DNA-binding protein 9 (CHD-9) (EC 3.6.4.12) (ATP-dependent helicase CHD9) (PPAR-alpha-interacting complex protein 320 kDa) (Peroxisomal proliferator-activated receptor A-interacting complex 320 kDa protein) 2885 323,860 Alternative sequence (1); Chain (1); Cross-link (11); Domain (4); Erroneous initiation (1); Modified residue (10); Motif (6); Nucleotide binding (1); Region (2); Sequence conflict (2) FUNCTION: Acts as a transcriptional coactivator for PPARA and possibly other nuclear receptors. Proposed to be a ATP-dependent chromatin remodeling protein. Has DNA-dependent ATPase activity and binds to A/T-rich DNA (By similarity). Associates with A/T-rich regulatory regions in promoters of genes that participate in the differentiation of progenitors during osteogenesis. {ECO:0000250}. PTM: Phosphorylated on serine and tyrosine residues. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Interacts with PPARA. Probably interacts with ESR1 and NR1I3 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in osteoprogenitor cells during development and in mature bone (at protein level). {ECO:0000269|PubMed:16419031}. +Q8BJ64 CHDH_MOUSE Choline dehydrogenase, mitochondrial (CDH) (CHD) (EC 1.1.99.1) 596 66,415 Active site (1); Chain (1); Modified residue (6); Nucleotide binding (1); Sequence conflict (4); Transit peptide (1) Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine aldehyde from choline (cytochrome c reductase route): step 1/1. PTM: Acetylation of Lys-498 is observed in liver mitochondria from fasted mice but not from fed mice. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:20371614}. +Q61324 ARNT2_MOUSE Aryl hydrocarbon receptor nuclear translocator 2 (ARNT protein 2) 712 77,902 Alternative sequence (1); Chain (1); Compositional bias (3); Domain (4); Erroneous initiation (1); Modified residue (1); Mutagenesis (8); Sequence conflict (2) FUNCTION: Transcription factor that plays a role in the development of the hypothalamo-pituitary axis, postnatal brain growth, and visual and renal function. Specifically recognizes the xenobiotic response element (XRE). {ECO:0000250|UniProtKB:Q9HBZ2}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9HBZ2, ECO:0000255|PROSITE-ProRule:PRU00981}. SUBUNIT: Efficient DNA binding requires dimerization with another bHLH protein (By similarity). Heterodimer with NPAS4 or SIM1 (PubMed:27782878). Heterodimer with the aryl hydrocarbon receptor (AHR) or the SIM1 protein (By similarity). Interacts with TACC3 (PubMed:11025203). {ECO:0000250|UniProtKB:Q9HBZ2, ECO:0000269|PubMed:11025203, ECO:0000269|PubMed:27782878}. TISSUE SPECIFICITY: Restricted to adult brain and kidney. +O35643 AP1B1_MOUSE AP-1 complex subunit beta-1 (Adaptor protein complex AP-1 subunit beta-1) (Adaptor-related protein complex 1 subunit beta-1) (Beta-1-adaptin) (Beta-adaptin 1) (Clathrin assembly protein complex 1 beta large chain) (Golgi adaptor HA1/AP1 adaptin beta subunit) 943 103,935 Chain (1); Compositional bias (1); Modified residue (2); Sequence conflict (2) FUNCTION: Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Golgi apparatus {ECO:0000250}. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex. {ECO:0000250}. SUBUNIT: Adaptor protein complex 1 (AP-1) is a heterotetramer composed of two large adaptins (gamma-type subunit AP1G1 and beta-type subunit AP1B1), a medium adaptin (mu-type subunit AP1M1 or AP1M2) and a small adaptin (sigma-type subunit AP1S1 or AP1S2 or AP1S3). TISSUE SPECIFICITY: Widely expressed. +Q3TAP4 AP5B1_MOUSE AP-5 complex subunit beta-1 (Adaptor-related protein complex 5 beta subunit) (Beta5) 876 94,679 Chain (1); Compositional bias (1) FUNCTION: As part of AP-5, a probable fifth adaptor protein complex it may be involved in endosomal transport. {ECO:0000250}. SUBUNIT: Probably part of the adaptor protein complex 5 (AP-5), a tetramer composed of AP5B1, AP5M1, AP5S1 and AP5Z1. Interacts with ZFYVE26 and SPG11 (By similarity). {ECO:0000250}. +Q9CPX9 APC11_MOUSE Anaphase-promoting complex subunit 11 (APC11) (Cyclosome subunit 11) 84 9,818 Chain (1); Metal binding (12); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: Together with the cullin protein ANAPC2, constitutes the catalytic component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. May recruit the E2 ubiquitin-conjugating enzymes to the complex (By similarity). {ECO:0000250|UniProtKB:Q9NYG5}. PTM: Auto-ubiquitinated. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: The mammalian APC/C is composed at least of 14 distinct subunits ANAPC1, ANAPC2, CDC27/APC3, ANAPC4, ANAPC5, CDC16/APC6, ANAPC7, CDC23/APC8, ANAPC10, ANAPC11, CDC26/APC12, ANAPC13, ANAPC15 and ANAPC16 that assemble into a complex of at least 19 chains with a combined molecular mass of around 1.2 MDa; APC/C interacts with FZR1 and FBXO5. Interacts with the cullin domain of ANAPC2. Interacts with UBE2D2. {ECO:0000250|UniProtKB:Q9NYG5}. DOMAIN: The RING-type zinc finger domain coordinates an additional third zinc ion. {ECO:0000250}. +P33622 APOC3_MOUSE Apolipoprotein C-III (Apo-CIII) (ApoC-III) (Apolipoprotein C3) 99 10,982 Chain (1); Glycosylation (1); Mass spectrometry (2); Modified residue (1); Region (1); Sequence conflict (3); Signal peptide (1); Site (1) FUNCTION: Component of triglyceride-rich very low density lipoproteins (VLDL) and high density lipoproteins (HDL) in plasma. Plays a multifaceted role in triglyceride homeostasis. Intracellularly, promotes hepatic very low density lipoprotein 1 (VLDL1) assembly and secretion; extracellularly, attenuates hydrolysis and clearance of triglyceride-rich lipoproteins (TRLs). Impairs the lipolysis of TRLs by inhibiting lipoprotein lipase and the hepatic uptake of TRLs by remnant receptors. Formed of several curved helices connected via semiflexible hinges, so that it can wrap tightly around the curved micelle surface and easily adapt to the different diameters of its natural binding partners. {ECO:0000250|UniProtKB:P02656}. PTM: The most abundant glycoforms are characterized by an O-linked disaccharide galactose linked to N-acetylgalactosamine (Gal-GalNAc), further modified with up to 3 sialic acid residues. Less abundant glycoforms are characterized by more complex and fucosylated glycan moieties. O-glycosylated on Thr-94 with a core 1 or possibly core 8 glycan. {ECO:0000250|UniProtKB:P02656}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02656}. +Q8CFQ3 AQR_MOUSE RNA helicase aquarius (EC 3.6.4.13) (Intron-binding protein of 160 kDa) 1481 170,294 Binding site (2); Chain (1); Erroneous initiation (1); Frameshift (1); Modified residue (1); Nucleotide binding (1); Region (2); Sequence conflict (2) FUNCTION: Involved in pre-mRNA splicing as component of the spliceosome. Intron-binding spliceosomal protein required to link pre-mRNA splicing and snoRNP (small nucleolar ribonucleoprotein) biogenesis. Plays a key role in position-dependent assembly of intron-encoded box C/D small snoRNP, splicing being required for snoRNP assembly. May act by helping the folding of the snoRNA sequence. Binds to intron of pre-mRNAs in a sequence-independent manner, contacting the region between snoRNA and the branchpoint of introns (40 nucleotides upstream of the branchpoint) during the late stages of splicing. Has ATP-dependent RNA helicase activity and can unwind double-stranded RNA molecules with a 3' overhang (in vitro). {ECO:0000250|UniProtKB:O60306}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O60306}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:O60306}. Note=Localizes to speckle-like regions of the nucleoplasm. {ECO:0000250|UniProtKB:O60306}. SUBUNIT: Identified in the spliceosome C complex. Component of the XAB2 complex, a multimeric protein complex composed of XAB2, PRPF19, AQR, ZNF830, ISY1, and PPIE. Identified in a pentameric intron-binding (IB) complex composed of AQR, XAB2, ISY1, ZNF830 and PPIE that is incorporated into the spliceosome as a preassembled complex. The IB complex does not contain PRPF19. Within the spliceosome, interacts with SNRPA1, SF3B1, SF3B3, SF3A1 and SF3A2. {ECO:0000250|UniProtKB:O60306}. DOMAIN: Contains an N-terminal domain with structural similarity to ARM repeat regions; this domain functions as scaffold for protein-protein interactions, but is not required for RNA binding or for ATP-dependent RNA helicase activity. {ECO:0000250|UniProtKB:O60306}. +Q8BZ05 ARAP2_MOUSE Arf-GAP with Rho-GAP domain, ANK repeat and PH domain-containing protein 2 (Centaurin-delta-1) (Cnt-d1) 1703 193,398 Alternative sequence (2); Chain (1); Domain (9); Modified residue (2); Zinc finger (1) FUNCTION: Phosphatidylinositol 3,4,5-trisphosphate-dependent GTPase-activating protein that modulates actin cytoskeleton remodeling by regulating ARF and RHO family members. Is activated by phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) binding. Can be activated by phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4,5)P2) binding, albeit with lower efficiency (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +P61205 ARF3_MOUSE ADP-ribosylation factor 3 181 20,601 Chain (1); Initiator methionine (1); Lipidation (1); Nucleotide binding (3) FUNCTION: GTP-binding protein that functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. Involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus. SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. SUBUNIT: Interacts with PRKCABP. Interacts with PI4KB and NCS1/FREQ at the Golgi complex. {ECO:0000250}. +Q8BW86 ARG33_MOUSE Rho guanine nucleotide exchange factor 33 850 94,758 Alternative sequence (1); Chain (1); Coiled coil (1); Compositional bias (3); Domain (1); Modified residue (1); Sequence conflict (1) +Q9EPJ9 ARFG1_MOUSE ADP-ribosylation factor GTPase-activating protein 1 (ARF GAP 1) (ADP-ribosylation factor 1 GTPase-activating protein) (ARF1 GAP) (ARF1-directed GTPase-activating protein) 414 45,288 Alternative sequence (1); Chain (1); Domain (1); Modified residue (12); Sequence conflict (2); Zinc finger (1) FUNCTION: GTPase-activating protein (GAP) for the ADP ribosylation factor 1 (ARF1). Involved in membrane trafficking and /or vesicle transport. Promotes hydrolysis of the ARF1-bound GTP and thus, is required for the dissociation of coat proteins from Golgi-derived membranes and vesicles, a prerequisite for vesicle's fusion with target compartment. Probably regulates ARF1-mediated transport via its interaction with the KDELR proteins and TMED2. Overexpression induces the redistribution of the entire Golgi complex to the endoplasmic reticulum, as when ARF1 is deactivated. Its activity is stimulated by phosphoinosides and inhibited by phosphatidylcholine (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus {ECO:0000250}. Note=Associates with the Golgi complex. {ECO:0000250}. SUBUNIT: Interacts with ARF1. Interacts with the COPI coat proteins, KDELR1 and TMED2. It is probably a component of the COPI coat protein complex. The interaction with TMED2 inhibits the GAP activity (By similarity). {ECO:0000250}. DOMAIN: The region downstream of Arf-GAP domain is essential to GAP activity in vivo. This region may be required for its targeting to Golgi membranes (By similarity). {ECO:0000250}. +B2RY50 ARMC4_MOUSE Armadillo repeat-containing protein 4 1037 115,266 Chain (1); Modified residue (1); Mutagenesis (1); Repeat (10) FUNCTION: Ciliary protein that may be involved in a late step of axonemal outer dynein arm assembly. {ECO:0000269|PubMed:23849778}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in testis. In males, also detected at lower levels in lung, brain, liver and muscle. In females, detected in ovary. {ECO:0000269|PubMed:24055424}. +Q80X86 ARM12_MOUSE Armadillo repeat-containing protein 12 340 38,530 Chain (1); Repeat (3); Sequence conflict (2) +Q9D7A8 ARMC1_MOUSE Armadillo repeat-containing protein 1 282 31,247 Chain (1); Modified residue (6); Repeat (1); Sequence conflict (1) +Q3URY6 ARMC2_MOUSE Armadillo repeat-containing protein 2 854 95,311 Alternative sequence (2); Chain (1); Repeat (12) +Q8BT18 ARMD4_MOUSE Armadillo-like helical domain-containing protein 4 775 83,774 Chain (1); Compositional bias (1); Glycosylation (2); Modified residue (2); Sequence conflict (23); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 716 736 Helical. {ECO:0000255}. TOPO_DOM 48 715 Extracellular. {ECO:0000255}.; TOPO_DOM 737 775 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q3UZB0 ARMX5_MOUSE Armadillo repeat-containing X-linked protein 5 606 67,895 Chain (1); Repeat (4) TISSUE SPECIFICITY: Highly expressed in the developing neural tissues, neural crest derivatives and hind limbs. {ECO:0000269|PubMed:22569362}. +Q9CQA6 CHCH1_MOUSE Coiled-coil-helix-coiled-coil-helix domain-containing protein 1 (28S ribosomal protein S37, mitochondrial) (MRP-S37) 118 13,608 Chain (1); Disulfide bond (2); Domain (1); Motif (2) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q96BP2}. Nucleus {ECO:0000250|UniProtKB:Q96BP2}. SUBUNIT: Component of the mitochondrial ribosome small subunit (28S) which comprises a 12S rRNA and about 30 distinct proteins. {ECO:0000250}. +P40201 CHD1_MOUSE Chromodomain-helicase-DNA-binding protein 1 (CHD-1) (EC 3.6.4.12) (ATP-dependent helicase CHD1) 1711 196,385 Chain (1); Compositional bias (2); Domain (4); Modified residue (24); Motif (1); Nucleotide binding (1); Region (1); Repeat (3); Sequence conflict (1) FUNCTION: ATP-dependent chromatin-remodeling factor which functions as substrate recognition component of the transcription regulatory histone acetylation (HAT) complex SAGA. Regulates polymerase II transcription. Also required for efficient transcription by RNA polymerase I, and more specifically the polymerase I transcription termination step. Regulates negatively DNA replication. Not only involved in transcription-related chromatin-remodeling, but also required to maintain a specific chromatin configuration across the genome. Required for the bridging of SNF2, the FACT complex, the PAF complex as well as the U2 snRNP complex to H3K4me3. Functions to modulate the efficiency of pre-mRNA splicing in part through physical bridging of spliceosomal components to H3K4me3 (By similarity). Required for maintaining open chromatin and pluripotency in embryonic stem cells (PubMed:19587682). Is also associated with histone deacetylase (HDAC) activity (PubMed:12890497). {ECO:0000250|UniProtKB:O14646, ECO:0000269|PubMed:12890497, ECO:0000269|PubMed:19587682}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10199952, ECO:0000269|PubMed:7739555}. Cytoplasm {ECO:0000269|PubMed:7739555}. Note=Is released into the cytoplasm when cells enter mitosis and is reincorporated into chromatin during telophase-cytokinesis (PubMed:7739555). SUBUNIT: Component of the SAGA complex (By similarity). Specifically interacts with methylated H3K4me2 and H3K4me3. Interacts with the FACT complex, the PAF complex and the U2 snRNP. Interacts directly with PAF1, SFA3A1, SFA3A2, SFA3A3, SNF2 and SSRP1 (By similarity). Interacts with BCLAF1, NCoR, SRP20 and SAFB. {ECO:0000250, ECO:0000269|PubMed:10199952, ECO:0000269|PubMed:12890497, ECO:0000269|PubMed:19587682}. DOMAIN: The 2 chromodomains are involved in the binding to the histone H3 methyllysine at position 4 (H3K4me3). {ECO:0000250}. TISSUE SPECIFICITY: Abundance is higher in cells representing early stages of the B-lymphoid lineage such as pre-B and B-cells, than in cells representing mature plasmacytes or other cell lineages such as fibroblasts. +Q6PDQ2 CHD4_MOUSE Chromodomain-helicase-DNA-binding protein 4 (CHD-4) (EC 3.6.4.12) 1915 217,751 Chain (1); Compositional bias (3); Cross-link (27); Domain (4); Modified residue (28); Motif (1); Nucleotide binding (1); Region (1); Zinc finger (2) FUNCTION: Component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. {ECO:0000269|PubMed:17938210}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Note=Associates with centrosomes in interphase. {ECO:0000250}. SUBUNIT: Central component of the nucleosome remodeling and histone deacetylase (NuRD) repressor complex (PubMed:11003653). Interacts with KLF1; the interaction depends on sumoylation of KLF1, and leads to its transcriptional repression (PubMed:17938210). Interacts with ZGPAT; the interaction is direct. Interacts with BCL6, BRD4 and PCNT. Interacts directly with IKFZ1 in the NuRD complex. Interacts with TRIM27. Part of a complex containing ATR and HDAC2. Interacts with SETX (By similarity). Interacts with HDAC1 (By similarity). {ECO:0000250|UniProtKB:Q14839, ECO:0000269|PubMed:11003653, ECO:0000269|PubMed:17938210}. +A2A8L1 CHD5_MOUSE Chromodomain-helicase-DNA-binding protein 5 (CHD-5) (EC 3.6.4.12) (ATP-dependent helicase CHD5) 1946 222,515 Chain (1); Compositional bias (1); Domain (4); Modified residue (2); Motif (1); Mutagenesis (6); Nucleotide binding (1); Region (1); Zinc finger (2) FUNCTION: Chromatin-remodeling protein that binds DNA through histones and regulates gene transcription. May specifically recognize and bind trimethylated 'Lys-27' (H3K27me3) and non-methylated 'Lys-4' of histone H3. Plays a role in the development of the nervous system by activating the expression of genes promoting neuron terminal differentiation. In parallel, it may also positively regulate the trimethylation of histone H3 at 'Lys-27' thereby specifically repressing genes that promote the differentiation into non-neuronal cell lineages. Tumor suppressor, it regulates the expression of genes involved in cell proliferation and differentiation. Downstream activated genes may include CDKN2A that positively regulates the p53/TP53 pathway, which in turn, prevents cell proliferation. In spermatogenesis, it probably regulates histone hyperacetylation and the replacement of histones by transition proteins in chromatin, a crucial step in the condensation of spermatid chromatin and the production of functional spermatozoa. {ECO:0000269|PubMed:17289567, ECO:0000269|PubMed:23318260, ECO:0000269|PubMed:23948251, ECO:0000269|PubMed:24252660}. PTM: Methylated at Gln-1392 by N6AMT1. {ECO:0000250|UniProtKB:Q8TDI0}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23318260, ECO:0000269|PubMed:23948251}. Note=Associates with heterochromatin. SUBUNIT: May be part of a nucleosome remodeling and histone deacetylation, NuRD-like, complex composed at least of GATAD2B, HDAC1, HDAC2 and MTA3. {ECO:0000269|PubMed:21931736}. DOMAIN: The PHD domains mediate specific binding to histone H3 unmethylated at 'Lys-4' and may preferentially recruit the protein to transcriptionally inactive genes. {ECO:0000269|PubMed:23318260}.; DOMAIN: The chromo domains mediate specific binding to histone H3 trimethylated at 'Lys-27' (H3K27me3) and may be required in neuron differentiation for proper gene regulation. {ECO:0000269|PubMed:23948251}. TISSUE SPECIFICITY: Specifically expressed by neurons in brain, retina and adrenal gland (at protein level). Also detected in testis. {ECO:0000269|PubMed:21931736, ECO:0000269|PubMed:23948251, ECO:0000269|PubMed:24252660}. +A3KFM7 CHD6_MOUSE Chromodomain-helicase-DNA-binding protein 6 (CHD-6) (EC 3.6.4.12) (ATP-dependent helicase CHD6) 2711 305,397 Alternative sequence (1); Chain (1); Domain (5); Erroneous initiation (1); Modified residue (1); Motif (1); Nucleotide binding (1); Region (1); Sequence caution (1); Sequence conflict (3) FUNCTION: DNA-dependent ATPase that plays a role in chromatin remodeling. Regulates transcription by disrupting nucleosomes in a largely non-sliding manner which strongly increases the accessibility of chromatin. Activates transcription of specific genes in response to oxidative stress through interaction with NFE2L2. {ECO:0000250|UniProtKB:Q8TD26}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q8TD26}. Note=Enriched at sites of mRNA synthesis. {ECO:0000250|UniProtKB:Q8TD26}. SUBUNIT: Interacts with NFE2L2; involved in activation of the transcription. {ECO:0000250|UniProtKB:Q8TD26}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:17027977}. +O70423 AOC3_MOUSE Membrane primary amine oxidase (EC 1.4.3.21) (Copper amine oxidase) (Semicarbazide-sensitive amine oxidase) (SSAO) (Vascular adhesion protein 1) (VAP-1) 765 84,534 Active site (2); Alternative sequence (1); Chain (1); Disulfide bond (4); Glycosylation (7); Metal binding (11); Modified residue (1); Region (3); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 7 27 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 28 765 Extracellular. {ECO:0000255}. FUNCTION: Cell adhesion protein that participates in lymphocyte recirculation by mediating the binding of lymphocytes to peripheral lymph node vascular endothelial cells in an L-selectin-independent fashion. Has a monoamine oxidase activity. May play a role in adipogenesis (By similarity). {ECO:0000250}. PTM: N- and O-glycosylated. {ECO:0000250}.; PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue. {ECO:0000250|UniProtKB:P12807}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. SUBUNIT: Homodimer; disulfide-linked (By similarity). Forms a heterodimer with AOC2 (By similarity). {ECO:0000250|UniProtKB:P19801, ECO:0000250|UniProtKB:Q16853}. +Q9WV06 ANKR2_MOUSE Ankyrin repeat domain-containing protein 2 (Skeletal muscle ankyrin repeat protein) (mArpp) 328 36,707 Chain (1); Erroneous initiation (3); Modified residue (2); Repeat (5) FUNCTION: Functions as a negative regulator of myocyte differentiation. May interact with both sarcoplasmic structural proteins and nuclear proteins to regulate gene expression during muscle development and in response to muscle stress. {ECO:0000269|PubMed:21737686, ECO:0000269|PubMed:23824195}. PTM: Phosphorylation at Ser-68 by PKB/AKT2 in response to oxidative stress induces translocation to the nucleus and negatively regulates myoblast differentiation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, I band. Cytoplasm, cytosol. Nucleus. Nucleus, PML body {ECO:0000250}. Note=In the sarcoplasm of differentiated striated muscle cells, where it is cytosolic and enriched in the I band. In nucleus and PML bodies of proliferating and undifferentiated myoblasts. Associates with the euchromatin in the nucleus of myocytes upon muscle stress. SUBUNIT: Interacts with ID3; both proteins cooperate in myoblast differentiation. Interacts with TTN/titin (By similarity). Interacts (via ANK repeats) with TCAP; the interaction is direct (By similarity). Interacts with TJP1 (via PDZ domains) (By similarity). Interacts with PML; the interaction is direct (By similarity). Interacts with p53/TP53 (By similarity). Interacts with YBX1 (By similarity). Interacts with AKT2. {ECO:0000250, ECO:0000269|PubMed:21737686, ECO:0000269|PubMed:23824195}. TISSUE SPECIFICITY: Expressed by myoblasts (at protein level). Expressed in skeletal and cardiac muscles. {ECO:0000269|PubMed:10873377}. +Q9CZ52 ANTR1_MOUSE Anthrax toxin receptor 1 (Tumor endothelial marker 8) 562 62,308 Alternative sequence (1); Chain (1); Compositional bias (2); Disulfide bond (1); Domain (1); Erroneous initiation (1); Glycosylation (3); Metal binding (3); Modified residue (1); Region (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 320 340 Helical. {ECO:0000255}. TOPO_DOM 31 319 Extracellular. {ECO:0000255}.; TOPO_DOM 341 562 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a role in cell attachment and migration. Interacts with extracellular matrix proteins and with the actin cytoskeleton. Mediates adhesion of cells to type 1 collagen and gelatin, reorganization of the actin cytoskeleton and promotes cell spreading. Plays a role in the angiogenic response of cultured umbilical vein endothelial cells (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cell projection, lamellipodium membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cell projection, filopodium membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=At the membrane of lamellipodia and at the tip of actin-enriched filopodia. Colocalizes with actin at the base of lamellipodia (By similarity). {ECO:0000250}. SUBUNIT: Interacts with gelatin and type 1 collagen. Interacts with the actin cytoskeleton. Binds to the protective antigen (PA) of Bacillus anthracis. Binding does not occur in the presence of calcium (By similarity). {ECO:0000250}. DOMAIN: Binding to PA occurs through the VWA domain. {ECO:0000250}. +Q9JKC7 AP4M1_MOUSE AP-4 complex subunit mu-1 (AP-4 adaptor complex mu subunit) (Adaptor-related protein complex 4 subunit mu-1) (Mu subunit of AP-4) (Mu-adaptin-related protein 2) (mu-ARP2) (Mu4-adaptin) (mu4) 449 49,509 Chain (1); Domain (1) FUNCTION: Component of the adaptor protein complex 4 (AP-4). Adaptor protein complexes are vesicle coat components involved both in vesicle formation and cargo selection. They control the vesicular transport of proteins in different trafficking pathways. AP-4 forms a non clathrin-associated coat on vesicles departing the trans-Golgi network (TGN) and may be involved in the targeting of proteins from the trans-Golgi network (TGN) to the endosomal-lysosomal system (By similarity). It is also involved in protein sorting to the basolateral membrane in epithelial cells and the proper asymmetric localization of somatodendritic proteins in neurons (PubMed:18341993). Within AP-4, the mu-type subunit AP4M1 is directly involved in the recognition and binding of tyrosine-based sorting signals found in the cytoplasmic part of cargos. The adaptor protein complex 4 (AP-4) may also recognize other types of sorting signal (By similarity). {ECO:0000250|UniProtKB:O00189, ECO:0000269|PubMed:18341993}. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:O00189}; Peripheral membrane protein {ECO:0000250|UniProtKB:O00189}. Early endosome {ECO:0000250|UniProtKB:O00189}. Note=Found in soma and dendritic shafts of neuronal cells. {ECO:0000250|UniProtKB:Q2PWT8}. SUBUNIT: Adaptor protein complex 4 (AP-4) is a heterotetramer composed of two large adaptins (epsilon-type subunit AP4E1 and beta-type subunit AP4B1), a medium adaptin (mu-type subunit AP4M1) and a small adaptin (sigma-type AP4S1). Interacts with tyrosine-based sorting signals on the cytoplasmic tail of cargo proteins such as APP, LAMP2 and NAGPA. Interacts with the C-terminal domain of GRID2 (By similarity). Interacts with GRIA1 and GRIA2; the interaction is indirect via CACNG3 (PubMed:18341993). Interacts with CACNG3; CACNG3 associates GRIA1 and GRIA2 with the adaptor protein complex 4 (AP-4) to target them to the somatodendritic compartment of neurons (PubMed:18341993). {ECO:0000250|UniProtKB:O00189, ECO:0000269|PubMed:18341993}. +Q6PAK3 ANM8_MOUSE Protein arginine N-methyltransferase 8 (EC 2.1.1.319) (EC 2.1.1.321) (Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 4) 394 45,276 Active site (2); Binding site (5); Chain (1); Domain (1); Erroneous initiation (1); Initiator methionine (1); Lipidation (1); Modified residue (2); Motif (2); Region (1) FUNCTION: S-adenosyl-L-methionine-dependent and membrane-associated arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and asymmetrical dimethylarginine (aDMA) in proteins such as NIFK, myelin basic protein, histone H4, H2A and H2A/H2B dimer. Able to mono- and dimethylate EWS protein; however its precise role toward EWS remains unclear as it still interacts with fully methylated EWS. {ECO:0000250|UniProtKB:Q9NR22}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9NR22}; Lipid-anchor {ECO:0000250|UniProtKB:Q9NR22}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9NR22}. SUBUNIT: Homodimer. Tetramer; individual homodimers associates to form a homotetramer. Homooctamer; individual homodimers associates to form a homooctamer and homooligomerization is required for proper localization to the cell membrane. Heterodimer with PRMT1; heterodimerization may recruit PRMT1 activity to the plasma membrane. Interacts with PRMT2 (via the SH3 domain). Interacts with FYN (via the SH3 domain). Interacts with EWS; independently of EWS methylation status. {ECO:0000250|UniProtKB:Q9NR22}. DOMAIN: The SH3-binding motifs mediate the interaction with SH3 domain-containing proteins such as PRMT2 and FYN, possibly leading to displace the N-terminal domain and activate the protein. {ECO:0000250|UniProtKB:Q9NR22}.; DOMAIN: The N-terminal region (1-60) inhibits the arginine N-methyltransferase activity. {ECO:0000250|UniProtKB:Q9NR22}. TISSUE SPECIFICITY: Brain-specific. Only expressed in neurons, especially in the somatosensory and limbic systems, and a part of motor system. Highly expressed in all of the regions related to general somatosensory system. Expressed in most of the relay nuclei intervening the special somatosensory system, such as the auditory, visual and vestibular systems. Also present in forebrain limbic areas and thalamic nuclei relevant to limbic areas and in areas related to the motor system, such as the caudate putamen, Purkinje cells, inferior olivary nucleus and cerebellar nuclei. {ECO:0000269|PubMed:17512914}. +Q9WVL1 AP4S1_MOUSE AP-4 complex subunit sigma-1 (AP-4 adaptor complex subunit sigma-1) (Adaptor-related protein complex 4 subunit sigma-1) (Sigma-1 subunit of AP-4) (Sigma-4-adaptin) (Sigma4-adaptin) 144 16,818 Chain (1) FUNCTION: Component of the adaptor protein complex 4 (AP-4). Adaptor protein complexes are vesicle coat components involved both in vesicle formation and cargo selection. They control the vesicular transport of proteins in different trafficking pathways. AP-4 forms a non clathrin-associated coat on vesicles departing the trans-Golgi network (TGN) and may be involved in the targeting of proteins from the trans-Golgi network (TGN) to the endosomal-lysosomal system. It is also involved in protein sorting to the basolateral membrane in epithelial cells and the proper asymmetric localization of somatodendritic proteins in neurons. AP-4 is involved in the recognition and binding of tyrosine-based sorting signals found in the cytoplasmic part of cargos, but may also recognize other types of sorting signal. {ECO:0000250|UniProtKB:Q9Y587}. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q9Y587}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9Y587}. SUBUNIT: Adaptor protein complex 4 (AP-4) is a heterotetramer composed of two large adaptins (epsilon-type subunit AP4E1 and beta-type subunit AP4B1), a medium adaptin (mu-type subunit AP4M1) and a small adaptin (sigma-type AP4S1). {ECO:0000250|UniProtKB:Q9Y587}. +Q9WV08 APJ_MOUSE Apelin receptor (Angiotensin receptor-like 1) (G-protein coupled receptor APJ) (MSR) 377 42,266 Chain (1); Glycosylation (2); Topological domain (8); Transmembrane (7) TRANSMEM 25 49 Helical; Name=1. {ECO:0000255}.; TRANSMEM 65 89 Helical; Name=2. {ECO:0000255}.; TRANSMEM 99 123 Helical; Name=3. {ECO:0000255}.; TRANSMEM 143 164 Helical; Name=4. {ECO:0000255}.; TRANSMEM 199 219 Helical; Name=5. {ECO:0000255}.; TRANSMEM 243 269 Helical; Name=6. {ECO:0000255}.; TRANSMEM 283 306 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 24 Extracellular. {ECO:0000255}.; TOPO_DOM 50 64 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 90 98 Extracellular. {ECO:0000255}.; TOPO_DOM 124 142 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 165 198 Extracellular. {ECO:0000255}.; TOPO_DOM 220 242 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 270 282 Extracellular. {ECO:0000255}.; TOPO_DOM 307 377 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for apelin receptor early endogenous ligand (APELA) and apelin (APLN) hormones coupled to G proteins that inhibit adenylate cyclase activity. Plays a key role in early development such as gastrulation, blood vessels formation and heart morphogenesis by acting as a receptor for APELA hormone (PubMed:28854362, PubMed:28890073, PubMed:28663440). May promote angioblast migration toward the embryonic midline, i.e. the position of the future vessel formation, during vasculogenesis (By similarity). Promotes sinus venosus (SV)-derived endothelial cells migration into the developing heart to promote coronary blood vessel development (PubMed:28890073). Plays also a role in various processes in adults such as regulation of blood vessel formation, blood pressure, heart contractility and heart failure (PubMed:28371822). {ECO:0000250|UniProtKB:P79960, ECO:0000250|UniProtKB:Q7SZP9, ECO:0000269|PubMed:28371822, ECO:0000269|PubMed:28663440, ECO:0000269|PubMed:28854362, ECO:0000269|PubMed:28890073}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P35414}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P79960}. Note=After exposure to apelin (APLN) or apelin receptor early endogenous ligand (APELA), internalized from the cell surface into an endosomal recycling compartment, from where it is recycled to the cell membrane. {ECO:0000250|UniProtKB:P35414, ECO:0000250|UniProtKB:Q9JHG3}. TISSUE SPECIFICITY: Expressed in coronary endothelial cells (at protein level) (PubMed:28890073). Expressed in the embryo, allantoic and endothelial precursor cells of the yolk sac at 8 days post-coitum (dpc) (PubMed:28663440). Expressed in the secondary heart field and somite at 8.25 dpc (PubMed:28854362). Expressed in fetal allantoic endothelial cells at 9 dpc (PubMed:28663440). Expressed in the allantoid and the invading fetal vasculature of the placenta at 9.5 dpc (PubMed:28854362). Expressed in endothelial cells adjacent to syncytiotrophoblast cells at 10.5 dpc (PubMed:28663440). Expressed weakly in the embryonic heart at 11.5 dpc (PubMed:26611206). Expressed in the adult heart (PubMed:26611206). Expressed in endothelial cells and cardiomyocytes and weakly expressed in fibroblasts (PubMed:10473142, PubMed:26611206). {ECO:0000269|PubMed:10473142, ECO:0000269|PubMed:26611206, ECO:0000269|PubMed:28663440, ECO:0000269|PubMed:28854362, ECO:0000269|PubMed:28890073}. +Q6VUP9 AP2E_MOUSE Transcription factor AP-2-epsilon (AP2-epsilon) (Activating enhancer-binding protein 2-epsilon) 442 46,283 Chain (1); Compositional bias (1); Modified residue (1); Motif (1); Region (1); Sequence conflict (1) FUNCTION: Sequence-specific DNA-binding protein that interacts with inducible viral and cellular enhancer elements to regulate transcription of selected genes. AP-2 factors bind to the consensus sequence 5'-GCCNNNGGC-3' and activate genes involved in a large spectrum of important biological functions including proper eye, face, body wall, limb and neural tube development. They also suppress a number of genes including MCAM/MUC18, C/EBP alpha and MYC. AP-2-epsilon may play a role in the development of the CNS and in cartilage differentiation. {ECO:0000269|PubMed:14572467, ECO:0000269|PubMed:14636996, ECO:0000269|PubMed:16684505}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16684505}. SUBUNIT: Binds DNA as a dimer. Can form homodimers or heterodimers with other AP-2 family members (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed most prominently in the mitral cell layer of the developing olfactory bulb and to a lesser extent in the granule cell layer. Also expressed in skin, articular cartilage, primary chondrocytes, and chondrosarcoma cell line SW1353. {ECO:0000269|PubMed:14572467, ECO:0000269|PubMed:14636996, ECO:0000269|PubMed:16684505}. +Q9Z1R3 APOM_MOUSE Apolipoprotein M (Apo-M) (ApoM) 190 21,273 Beta strand (8); Binding site (2); Chain (1); Disulfide bond (3); Helix (4); Signal peptide (1) FUNCTION: Probably involved in lipid transport. Can bind sphingosine-1-phosphate, myristic acid, palmitic acid and stearic acid, retinol, all-trans-retinoic acid and 9-cis-retinoic acid (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. SUBUNIT: Interacts with LRP2; LRP2 mediates APOM renal uptake and subsequent lysosomal degradation. {ECO:0000269|PubMed:16099815}. TISSUE SPECIFICITY: Expressed by the liver; secreted in plasma. +Q09PK2 APRV1_MOUSE Retroviral-like aspartic protease 1 (EC 3.4.23.-) (Skin-specific retroviral-like aspartic protease) (SASPase) (Skin aspartic protease) (TPA-inducible aspartic proteinase-like protein) 339 37,174 Active site (1); Chain (1); Domain (1); Erroneous initiation (1); Glycosylation (2); Mutagenesis (1); Propeptide (2); Sequence conflict (1); Transmembrane (1) TRANSMEM 55 75 Helical. {ECO:0000255}. PTM: Undergoes autocleavage which is necessary for activation of the protein. {ECO:0000269|PubMed:16837463}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. SUBUNIT: Homodimer. {ECO:0000269|PubMed:16837463, ECO:0000305}. TISSUE SPECIFICITY: Highly expressed in stratified epithelia in skin, tongue, esophagus, forestomach and vagina. Also expressed in trachea, urinary bladder and thymus. Undetectable in simple epithelia. Within the epidermis, expressed exclusively in the granular layer (at protein level). Levels are elevated in benign skin tumors but are down-regulated in squamous cell carcinomas. {ECO:0000269|PubMed:16565508, ECO:0000269|PubMed:16837463}. +Q8CHJ2 AQP12_MOUSE Aquaporin-12 (AQP-12) 290 31,290 Chain (1); Motif (2); Transmembrane (6) TRANSMEM 1 21 Helical; Name=1. {ECO:0000255}.; TRANSMEM 67 87 Helical; Name=2. {ECO:0000255}.; TRANSMEM 112 138 Helical; Name=3. {ECO:0000255}.; TRANSMEM 158 178 Helical; Name=4. {ECO:0000255}.; TRANSMEM 191 211 Helical; Name=5. {ECO:0000255}.; TRANSMEM 228 248 Helical; Name=6. {ECO:0000255}. FUNCTION: Aquaporins facilitate the transport of water and small neutral solutes across cell membranes. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. DOMAIN: Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA). TISSUE SPECIFICITY: Restricted to pancreatic acinar cells. {ECO:0000269|PubMed:15809071}. +O54794 AQP7_MOUSE Aquaporin-7 (AQP-7) (Aquaglyceroporin-7) 303 32,667 Chain (1); Modified residue (1); Motif (2); Sequence conflict (2); Topological domain (7); Transmembrane (6) TRANSMEM 26 46 Helical. {ECO:0000255}.; TRANSMEM 53 73 Helical. {ECO:0000255}.; TRANSMEM 99 119 Helical. {ECO:0000255}.; TRANSMEM 156 176 Helical. {ECO:0000255}.; TRANSMEM 190 210 Helical. {ECO:0000255}.; TRANSMEM 241 261 Helical. {ECO:0000255}. TOPO_DOM 1 25 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 47 52 Extracellular. {ECO:0000255}.; TOPO_DOM 74 98 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 120 155 Extracellular. {ECO:0000255}.; TOPO_DOM 177 189 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 211 240 Extracellular. {ECO:0000255}.; TOPO_DOM 262 303 Cytoplasmic. {ECO:0000255}. FUNCTION: Forms a channel for water and glycerol. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. DOMAIN: Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro/Ala-Ala/Ser (NPA). +P56404 AQP8_MOUSE Aquaporin-8 (AQP-8) 261 27,797 Chain (1); Glycosylation (1); Motif (2); Sequence conflict (1); Topological domain (7); Transmembrane (6) TRANSMEM 37 57 Helical. {ECO:0000255}.; TRANSMEM 85 105 Helical. {ECO:0000255}.; TRANSMEM 108 128 Helical. {ECO:0000255}.; TRANSMEM 157 177 Helical. {ECO:0000255}.; TRANSMEM 184 204 Helical. {ECO:0000255}.; TRANSMEM 229 249 Helical. {ECO:0000255}. TOPO_DOM 1 36 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 58 84 Extracellular. {ECO:0000255}.; TOPO_DOM 106 107 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 129 156 Extracellular. {ECO:0000255}.; TOPO_DOM 178 183 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 205 228 Extracellular. {ECO:0000255}.; TOPO_DOM 250 261 Cytoplasmic. {ECO:0000255}. FUNCTION: Forms a water-specific channel; mercury-sensitive. Also permeable to urea but not to glycerol. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. DOMAIN: Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA). TISSUE SPECIFICITY: Colon, liver, heart and placenta. +P04627 ARAF_MOUSE Serine/threonine-protein kinase A-Raf (EC 2.7.11.1) (Proto-oncogene A-Raf) 604 67,581 Active site (1); Binding site (1); Chain (1); Domain (2); Metal binding (8); Modified residue (7); Nucleotide binding (1); Sequence conflict (4); Zinc finger (1) FUNCTION: Involved in the transduction of mitogenic signals from the cell membrane to the nucleus. May also regulate the TOR signaling cascade (By similarity). {ECO:0000250}. SUBUNIT: Interacts with TH1L/NELFD. {ECO:0000250}. +Q9D8S3 ARFG3_MOUSE ADP-ribosylation factor GTPase-activating protein 3 (ARF GAP 3) 523 57,456 Chain (1); Compositional bias (1); Domain (1); Modified residue (12); Sequence conflict (4); Zinc finger (1) FUNCTION: GTPase-activating protein (GAP) for ADP ribosylation factor 1 (ARF1). Hydrolysis of ARF1-bound GTP may lead to dissociation of coatomer from Golgi-derived membranes to allow fusion with target membranes (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Also found on peripheral punctate structures likely to be endoplasmic reticulum-Golgi intermediate compartment. {ECO:0000250}. +O08691 ARGI2_MOUSE Arginase-2, mitochondrial (EC 3.5.3.1) (Arginase II) (Kidney-type arginase) (Non-hepatic arginase) (Type II arginase) 354 38,878 Binding site (3); Chain (1); Metal binding (8); Mutagenesis (1); Region (2); Transit peptide (1) Nitrogen metabolism; urea cycle; L-ornithine and urea from L-arginine: step 1/1. FUNCTION: May play a role in the regulation of extra-urea cycle arginine metabolism and also in down-regulation of nitric oxide synthesis. Extrahepatic arginase functions to regulate L-arginine bioavailability to nitric oxid synthase (NOS). Arginine metabolism is a critical regulator of innate and adaptive immune responses. Seems to be involved in negative regulation of the survival capacity of activated CD4(+) and CD8(+) T cells (PubMed:27745970, PubMed:25009204). May suppress inflammation-related signaling in asthmatic airway epithelium (PubMed:27214549). May contribute to the immune evasion of H.pylori by restricting M1 macrophage activation and polyamine metabolism (PubMed:27074721). May play a role in promoting prenatal immune suppression (By similarity). Regulates RPS6KB1 signaling, which promotes endothelial cell senescence and inflammation and implicates NOS3/eNOS dysfunction (PubMed:22928666). Can inhibit endothelial autophagy independently of its enzymatic activity implicating mTORC2 signaling (PubMed:25484082). Involved in vascular smooth muscle cell senescence and apoptosis independently of its enzymatic activity (By similarity). {ECO:0000250|UniProtKB:P78540, ECO:0000269|PubMed:22928666, ECO:0000269|PubMed:25009204, ECO:0000269|PubMed:25484082, ECO:0000269|PubMed:27074721, ECO:0000269|PubMed:27214549, ECO:0000269|PubMed:27745970}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25009204}. SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:P78540}. +Q8CG72 ARHL2_MOUSE ADP-ribose glycohydrolase ARH3 (ADP-ribosylhydrolase 3) (O-acetyl-ADP-ribose deacetylase ARH3) (EC 3.5.1.-) (Poly(ADP-ribose) glycohydrolase ARH3) (EC 3.2.1.143) ([Protein ADP-ribosylarginine] hydrolase-like protein 2) ([Protein ADP-ribosylserine] hydrolase) (EC 3.2.2.-) 370 39,414 Alternative sequence (1); Beta strand (1); Binding site (4); Chain (1); Compositional bias (2); Helix (23); Metal binding (8); Modified residue (1); Region (1); Sequence conflict (1); Site (1); Turn (2) FUNCTION: ADP-ribose glycohydrolase that preferentially hydrolyzes the scissile alpha-O-linkage attached to the anomeric C1'' position of ADP-ribose and acts on different substrates, such as proteins ADP-ribosylated on serine, free poly(ADP-ribose) and O-acetyl-ADP-D-ribose (By similarity). Specifically acts as a serine mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to serine residues on proteins, thereby playing a key role in DNA damage response (By similarity). Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage (By similarity). Does not hydrolyze ADP-ribosyl-arginine, -cysteine, -diphthamide, or -asparagine bonds (By similarity). Also able to degrade protein free poly(ADP-ribose), which is synthesized in response to DNA damage: free poly(ADP-ribose) acts as a potent cell death signal and its degradation by ADPRHL2 protects cells from poly(ADP-ribose)-dependent cell death, a process named parthanatos (PubMed:24191052). Also hydrolyzes free poly(ADP-ribose) in mitochondria (By similarity). Specifically digests O-acetyl-ADP-D-ribose, a product of deacetylation reactions catalyzed by sirtuins (By similarity). Specifically degrades 1''-O-acetyl-ADP-D-ribose isomer, rather than 2''-O-acetyl-ADP-D-ribose or 3''-O-acetyl-ADP-D-ribose isomers (By similarity). {ECO:0000250|UniProtKB:Q9NX46, ECO:0000269|PubMed:24191052}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16278211, ECO:0000269|PubMed:24191052}. Cytoplasm {ECO:0000269|PubMed:16278211}. Chromosome {ECO:0000250|UniProtKB:Q9NX46}. Mitochondrion matrix {ECO:0000269|PubMed:24191052}. Note=Recruited to DNA lesion regions following DNA damage; ADP-D-ribose-recognition is required for recruitment to DNA damage sites. {ECO:0000250|UniProtKB:Q9NX46}. SUBUNIT: Monomer. {ECO:0000269|PubMed:18323597}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:16278211}. +Q7TNR9 ARHG4_MOUSE Rho guanine nucleotide exchange factor 4 (APC-stimulated guanine nucleotide exchange factor) (Asef) 484 56,679 Chain (1); Domain (3); Frameshift (1) FUNCTION: Acts as guanine nucleotide exchange factor (GEF) for RHOA, RAC1 and CDC42 GTPases. Binding of APC may activate RAC1 GEF activity. The APC-ARHGEF4 complex seems to be involved in cell migration as well as in E-cadherin-mediated cell-cell adhesion (By similarity). Required for MMP9 up-regulation via the JNK signaling pathway in colorectal tumor cells. Involved in tumor angiogenesis and may play a role in intestinal adenoma formation and tumor progression. {ECO:0000250, ECO:0000269|PubMed:19893577}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10947987}. Note=Colocalized with APC in the synapse of olfactory glomerulus. SUBUNIT: Interacts with RHOA and RAC1, and APC. Found in a complex consisting of ARHGEF4, APC and CTNNB1 (By similarity). {ECO:0000250}. DOMAIN: In an autoinhibited form the SH3 domain binds intramolecularly to the DH domain, thus blocking the Rac-binding site. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in colon epithelial cells. Highly expressed in CNS, including hippocampus, olfactory bulb and cerebellum. Expression is aberrantly enhanced in most colorectal tumors. {ECO:0000269|PubMed:10947987, ECO:0000269|PubMed:19893577}. +Q80VK6 ARH38_MOUSE Rho guanine nucleotide exchange factor 38 770 87,679 Alternative sequence (3); Chain (1); Compositional bias (1); Domain (4); Modified residue (1); Sequence conflict (3) FUNCTION: May act as a guanine-nucleotide releasing factor. {ECO:0000250}. +Q9ES28 ARHG7_MOUSE Rho guanine nucleotide exchange factor 7 (Beta-Pix) (PAK-interacting exchange factor beta) (p85SPR) 862 97,056 Alternative sequence (9); Beta strand (5); Chain (1); Coiled coil (1); Domain (4); Erroneous initiation (8); Helix (1); Modified residue (8); Sequence conflict (19) FUNCTION: Acts as a RAC1 guanine nucleotide exchange factor (GEF) and can induce membrane ruffling. May function as a positive regulator of apoptosis. Functions in cell migration, attachment and cell spreading. Promotes targeting of RAC1 to focal adhesions. Downstream of NMDA receptors and CaMKK-CaMK1 signaling cascade, promotes the formation of spines and synapses in hippocampal neurons (By similarity). {ECO:0000250, ECO:0000269|PubMed:17093062}. PTM: Phosphorylated on Ser-673 by CaMK1; enhancement of GEF activity and downstream activation of RAC1 (By similarity). Phosphorylated by PTK2/FAK1; this promotes interaction with RAC1. {ECO:0000250, ECO:0000269|PubMed:17093062}. SUBCELLULAR LOCATION: Cell junction, focal adhesion. Cell projection, ruffle. Cytoplasm, cell cortex. Cell projection, lamellipodium. Note=Detected at cell adhesions. A small proportion is detected at focal adhesions. SUBUNIT: Interacts with PAK kinases through the SH3 domain. Interacts with unphosphorylated PAK1. Interacts with ITCH. Interacts with SCRIB; interaction is direct and may play a role in regulation of apoptosis (By similarity). Interacts with GIT1 and TGFB1I1. Interacts with FRMPD4 (via N-terminus). Interacts with CaMK1. Interacts with BIN2 (By similarity). Interacts with PTK2/FAK1 and RAC1. Interacts with PARVB. {ECO:0000250, ECO:0000269|PubMed:10428811, ECO:0000269|PubMed:12153727, ECO:0000269|PubMed:17093062, ECO:0000269|PubMed:18325335}. TISSUE SPECIFICITY: Seems to be expressed in the central nervous system. Isoform B, isoform C and isoform E are expressed with highest levels in brain and testis. {ECO:0000269|PubMed:10860822, ECO:0000269|PubMed:11266127}. +Q8C033 ARHGA_MOUSE Rho guanine nucleotide exchange factor 10 1345 147,946 Alternative sequence (1); Chain (1); Coiled coil (1); Domain (1); Erroneous initiation (4); Modified residue (4); Sequence conflict (7) FUNCTION: May play a role in developmental myelination of peripheral nerves. {ECO:0000269|PubMed:14508709}. PTM: Methylated at Gln-1314 by N6AMT1. {ECO:0000250|UniProtKB:O15013}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:14508709}. +A2BH40 ARI1A_MOUSE AT-rich interactive domain-containing protein 1A (ARID domain-containing protein 1A) (BRG1-associated factor 250) (BAF250) (BRG1-associated factor 250a) (BAF250A) (Osa homolog 1) (SWI-like protein) (SWI/SNF complex protein p270) (SWI/SNF-related, matrix-associated, actin-dependent regulator of chromatin subfamily F member 1) 2283 242,092 Alternative sequence (4); Chain (1); Compositional bias (10); Domain (1); Initiator methionine (1); Modified residue (26); Motif (5); Sequence conflict (15) FUNCTION: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. Binds DNA non-specifically (PubMed:22952240, PubMed:26601204). Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (PubMed:17640523). {ECO:0000250|UniProtKB:O14497, ECO:0000269|PubMed:17640523, ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355}. SUBUNIT: Component of SWI/SNF chromatin remodeling complexes, in some of which it can be mutually exclusive with ARID1B/BAF250B. The canonical complex contains a catalytic subunit (either SMARCA4/BRG1/BAF190A or SMARCA2/BRM/BAF190B) and at least SMARCE1, ACTL6A/BAF53, SMARCC1/BAF155, SMARCC2/BAF170, and SMARCB1/SNF5/BAF47. Other subunits specific to each of the complexes may also be present permitting several possible combinations developmentally and tissue specific. Component of the BAF (SWI/SNF-A) complex, which includes at least actin (ACTB), ARID1A/BAF250A, ARID1B/BAF250B, SMARCA2/BRM, SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57, SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C (By similarity). In muscle cells, the BAF complex also contains DPF3. Component of neural progenitors-specific chromatin remodeling complex (npBAF complex) composed of at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, PHF10/BAF45A, ACTL6A/BAF53A and actin. Component of neuron-specific chromatin remodeling complex (nBAF complex) composed of at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, DPF1/BAF45B, DPF3/BAF45C, ACTL6B/BAF53B and actin (PubMed:17640523). Component of a SWI/SNF-like EBAFa complex, at least composed of SMARCA4/BRG1/BAF190A, SMARCB1/BAF47/SNF5, ACTL6A/BAF53A, SMARCE1/BAF57, SMARCD1/BAF60A, SMARCC1/BAF155, SMARCC2/BAF170, BAF250A and MLLT1/ENL. Interacts through its C-terminus with SMARCA2/BRM/BAF190B and SMARCA4/BRG1/BAF190A. Interacts with SMARCC1/BAF155 (By similarity). {ECO:0000250|UniProtKB:O14497, ECO:0000269|PubMed:17640523, ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}. TISSUE SPECIFICITY: Widely expressed. Expressed at high levels in the testis. {ECO:0000269|PubMed:11318604}. +Q80ZU0 ARL5A_MOUSE ADP-ribosylation factor-like protein 5A 179 20,724 Binding site (1); Chain (1); Initiator methionine (1); Lipidation (1); Nucleotide binding (3) FUNCTION: Lacks ADP-ribosylation enhancing activity. {ECO:0000250}. +Q8BGK2 ARHL1_MOUSE [Protein ADP-ribosylarginine] hydrolase-like protein 1 (EC 3.2.-.-) (ADP-ribosylhydrolase 2) 353 39,885 Chain (1); Erroneous initiation (1); Modified residue (1) FUNCTION: Seems not to catalyse the hydrolysis of O-acetyl-ADP-ribose. {ECO:0000269|PubMed:17075046}. +P31955 AREG_MOUSE Amphiregulin (AR) (Schwannoma-derived growth factor) (SDGF) 248 27,549 Chain (1); Disulfide bond (3); Domain (1); Glycosylation (2); Propeptide (1); Signal peptide (1); Transmembrane (1) TRANSMEM 192 215 Helical. {ECO:0000255}. FUNCTION: Ligand of the EGF receptor/EGFR. Autocrine growth factor as well as a mitogen for a broad range of target cells including astrocytes, Schwann cells and fibroblasts. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SUBUNIT: The immature precursor interacts with CNIH. {ECO:0000250}. +Q8K221 ARFP2_MOUSE Arfaptin-2 (ADP-ribosylation factor-interacting protein 2) 341 37,773 Chain (1); Domain (1); Modified residue (1); Sequence conflict (1) FUNCTION: Putative target protein of ADP-ribosylation factor. Involved in membrane ruffling (By similarity). {ECO:0000250}. SUBUNIT: Interacts with RAC1 by binding directly to it. Specifically binds to GTP-bound ARF1 and ARF6, but binds to RAC1.GTP and RAC1.GDP with similar affinities (By similarity). Directly interacts with ARL1 GTP-bound form; this interaction leads to an increase in the amount of bound GTP at steady state level (By similarity). {ECO:0000250}. +Q60875 ARHG2_MOUSE Rho guanine nucleotide exchange factor 2 (Guanine nucleotide exchange factor H1) (GEF-H1) (LBC'S first cousin) (Lymphoid blast crisis-like 1) (Oncogene LFC) (Rhobin) 985 111,974 Alternative sequence (6); Beta strand (2); Chain (1); Coiled coil (2); Compositional bias (1); Domain (2); Erroneous initiation (1); Helix (1); Modified residue (31); Region (1); Sequence conflict (7); Zinc finger (1) FUNCTION: Activates Rho-GTPases by promoting the exchange of GDP for GTP. May be involved in epithelial barrier permeability, cell motility and polarization, dendritic spine morphology, antigen presentation, leukemic cell differentiation, cell cycle regulation, innate immune response, and cancer. Binds Rac-GTPases, but does not seem to promote nucleotide exchange activity toward Rac-GTPases. May stimulate instead the cortical activity of Rac. Inactive toward CDC42, TC10, or Ras-GTPases. Forms an intracellular sensing system along with NOD1 for the detection of microbial effectors during cell invasion by pathogens. Involved in innate immune signaling transduction pathway promoting cytokine IL6/interleukin-6 and TNF-alpha secretion in macrophage upon stimulation by bacterial peptidoglycans; acts as a signaling intermediate between NOD2 receptor and RIPK2 kinase. Contributes to the tyrosine phosphorylation of RIPK2 through Src tyrosine kinase leading to NF-kappaB activation by NOD2. Overexpression activates Rho-, but not Rac-GTPases, and increases paracellular permeability (By similarity). Involved in neuronal progenitor cell division and differentiation (PubMed:28453519). Involved in the migration of precerebellar neurons (PubMed:28453519). {ECO:0000250|UniProtKB:Q865S3, ECO:0000250|UniProtKB:Q92974, ECO:0000269|PubMed:28453519}. PTM: Phosphorylation of Ser-885 by PAK1 induces binding to protein YWHAZ, promoting its relocation to microtubules and the inhibition of its activity. Phosphorylated by AURKA and CDK1 during mitosis, which negatively regulates its activity. Phosphorylation by MAPK1 or MAPK3 increases nucleotide exchange activity. Phosphorylation by PAK4 releases GEF-H1 from the microtubules. Phosphorylated on serine, threonine and tyrosine residues in a RIPK2-dependent manner (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q865S3, ECO:0000250|UniProtKB:Q92974}. Cytoplasm {ECO:0000250|UniProtKB:Q865S3, ECO:0000250|UniProtKB:Q92974}. Cell junction, tight junction {ECO:0000269|PubMed:12604587}. Golgi apparatus {ECO:0000250|UniProtKB:Q92974}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q865S3, ECO:0000250|UniProtKB:Q92974}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q92974}. Note=Localizes to the tips of cortical microtubules of the mitotic spindle during cell division, and is further released upon microtubule depolymerization (By similarity). Colocalized with NOD2 and RIPK2 in vesicles and with the cytoskeleton (By similarity). Associated with apical intercellular junctions in the trophectoderm of the blastocyst (PubMed:12604587). {ECO:0000250|UniProtKB:Q92974, ECO:0000269|PubMed:12604587}. SUBUNIT: Found in a complex composed at least of ARHGEF2, NOD2 and RIPK2. Interacts with RIPK2; the interaction mediates tyrosine phosphorylation of RIPK2 by Src kinase CSK. Interacts with RIPK1 and RIPK3. Interacts with YWHAZ/14-3-3 zeta; when phosphorylated at Ser-885. Interacts with the kinases PAK4, AURKA and MAPK1. Interacts with RHOA and RAC1. Interacts with NOD1 (By similarity). Interacts (via the N- terminal zinc finger) with CAPN6 (via domain II). Interacts with DYNLT1. {ECO:0000250, ECO:0000250|UniProtKB:Q865S3, ECO:0000269|PubMed:21406564}. DOMAIN: The DH (DBL-homology) domain promotes tyrosine phosphorylation of RIPK2 (By similarity). The DH (DBL-homology) domain interacts with and promotes loading of GTP on RhoA. {ECO:0000250}.; DOMAIN: The PH domain has no affinity for phosphoinositides suggesting that it does not interact directly with membranes. {ECO:0000250|UniProtKB:Q92974}.; DOMAIN: The phorbol-ester/DAG-type zinc-finger and the C-terminal coiled-coil domains (606-986) are both important for association with microtubules. {ECO:0000250|UniProtKB:Q92974}. TISSUE SPECIFICITY: Ubiquitous, with the exception of liver tissue. Levels are high in hemopoietic tissues (thymus, spleen, bone marrow) as well as in kidney and lung. Expressed in the germinal zones of both the neocortex and the cerebellum and in the pontine gray nuclei (PubMed:28453519). {ECO:0000269|PubMed:28453519}. +A1IGU4 ARH37_MOUSE Rho guanine nucleotide exchange factor 37 676 76,524 Alternative sequence (1); Chain (1); Domain (4) FUNCTION: May act as a guanine nucleotide exchange factor (GEF). {ECO:0000250}. +Q3UPH7 ARH40_MOUSE Rho guanine nucleotide exchange factor 40 (Protein SOLO) 1517 165,132 Alternative sequence (3); Chain (1); Coiled coil (1); Compositional bias (3); Domain (2); Erroneous initiation (2); Modified residue (10); Sequence caution (2); Sequence conflict (7) FUNCTION: May act as a guanine nucleotide exchange factor (GEF). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Concentrated in the perinuclear region. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed but enriched in brain. In brain, it is expressed at higher level in olfactory bulb and cerebellum and peaks perinatally (from E16 to P0.5). {ECO:0000269|PubMed:16143467}. +Q61210 ARHG1_MOUSE Rho guanine nucleotide exchange factor 1 (Lbc's second cousin) (Lymphoid blast crisis-like 2) 920 102,805 Alternative sequence (6); Chain (1); Coiled coil (1); Domain (3); Modified residue (9); Sequence conflict (3) FUNCTION: Seems to play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13) subunits. Acts as GTPase-activating protein (GAP) for GNA12 and GNA13, and as guanine nucleotide exchange factor (GEF) for RhoA GTPase. Activated G alpha 13/GNA13 stimulates the RhoGEF activity through interaction with the RGS-like domain. This GEF activity is inhibited by binding to activated GNA12. Mediates angiotensin-2-induced RhoA activation. Isoform 3 and isoform 4 do not homooligomerize and show an enhanced RhoGEF activity. {ECO:0000269|PubMed:20098430, ECO:0000269|PubMed:8910315}. PTM: Phosphorylated by PKCA (By similarity). Angiotensin-2 induced Tyr-737 phosphorylation is mediated by JAK2. Isoform 5 is phosphorylated at 'Ser-390'. {ECO:0000250, ECO:0000269|PubMed:20098430}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}. Note=Translocated to the membrane by activated GNA13 or LPA stimulation. {ECO:0000250}. SUBUNIT: Interacts with RHOA, GNA12 and GNA13 (By similarity). Homooligomerizes through the coiled coil region. Interacts with CTNNAL1 (By similarity). May interact with CCPG1. {ECO:0000250, ECO:0000269|PubMed:12773540, ECO:0000269|PubMed:8910315}. DOMAIN: The RGSL domain, also known as rgRGS domain, is necessary but not sufficient for full GAP activity. {ECO:0000250}.; DOMAIN: The DH domain is involved in interaction with CCPG1. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:8702517}. +Q9Z206 ARHG8_MOUSE Neuroepithelial cell-transforming gene 1 protein (Rho guanine nucleotide exchange factor 8) 595 67,734 Alternative sequence (2); Chain (1); Domain (2); Modified residue (6); Motif (2); Mutagenesis (4); Region (1); Sequence conflict (5) FUNCTION: Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPase. May be involved in activation of the SAPK/JNK pathway. Stimulates genotoxic stress-induced RHOB activity in breast cancer cells leading to their cell death. {ECO:0000269|PubMed:9670022}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11839749}. Nucleus {ECO:0000269|PubMed:11839749}. SUBUNIT: Interacts with RHOA in its GTP- and GDP-bound states, and with CDC42 in its GTP-bound state. Interacts with the PDZ 1 domain of BAIAP1. {ECO:0000269|PubMed:11350080, ECO:0000269|PubMed:9535835}. DOMAIN: The PH domain is sufficient for the nuclear export of the oncogenic N-terminal truncated form. The relocalization is not affected by the Leu-492 mutation. +Q9D0J4 ARL2_MOUSE ADP-ribosylation factor-like protein 2 184 20,864 Beta strand (6); Binding site (1); Chain (1); Cross-link (1); Helix (10); Initiator methionine (1); Lipidation (1); Modified residue (1); Mutagenesis (2); Nucleotide binding (3); Sequence conflict (1); Turn (1) FUNCTION: Small GTP-binding protein which cycles between an inactive GDP-bound and an active GTP-bound form, and the rate of cycling is regulated by guanine nucleotide exchange factors (GEF) and GTPase-activating proteins (GAP). GTP-binding protein that does not act as an allosteric activator of the cholera toxin catalytic subunit. Regulates formation of new microtubules and centrosome integrity. Prevents the TBCD-induced microtubule destruction. Participates in association with TBCD, in the disassembly of the apical junction complexes. Antagonizes the effect of TBCD on epithelial cell detachment and tight and adherens junctions disassembly. Together with ARL2, plays a role in the nuclear translocation, retention and transcriptional activity of STAT3. Component of a regulated secretory pathway involved in Ca(2+)-dependent release of acetylcholine. Required for normal progress through the cell cycle. PTM: Not N-myristoylated. SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Nucleus. Cytoplasm. Note=The complex formed with ARL2BP, ARL2 and SLC25A6 is expressed in mitochondria. Not detected in the Golgi, nucleus and on the mitotic spindle. Centrosome-associated throughout the cell cycle. Not detected to interphase microtubules (By similarity). The complex formed with ARL2BP, ARL2 and SLC25A4 is expressed in mitochondria. {ECO:0000250}. SUBUNIT: Found in a complex with ARL2, ARL2BP and SLC25A6. Found in a complex with at least ARL2, PPP2CB, PPP2R1A, PPP2R2A, PPP2R5E and TBCD. Interacts with ELMOD2. The GTP-bound form interacts with ARL2BP. Interacts with TBCD; the GDP-bound form interacts preferentially with TBCD. Interacts with UNC119 (By similarity). Found in a complex with ARL2, ARL2BP and SLC25A4. The GTP-bound form interacts with PDE6D. {ECO:0000250, ECO:0000269|PubMed:11809823, ECO:0000269|PubMed:11980706, ECO:0000269|PubMed:15979089}. TISSUE SPECIFICITY: Expressed in brain, lung, cerebellum, liver, kidney, hippocampus, spleen, cortex and heart (at protein level). {ECO:0000269|PubMed:11809823}. +Q8R4H2 ARHGC_MOUSE Rho guanine nucleotide exchange factor 12 (Leukemia-associated RhoGEF) 1543 172,349 Chain (1); Coiled coil (2); Domain (4); Erroneous initiation (1); Initiator methionine (1); Modified residue (11); Sequence conflict (4) FUNCTION: May play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13). Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPase and may act as GTPase-activating protein (GAP) for GNA12 and GNA13 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Membrane {ECO:0000305}. Note=Translocated to the membrane upon stimulation. {ECO:0000305}. SUBUNIT: Interacts with GNA12 and GNA13, probably through the RGS-like domain, with RHOA, PLXNB1 and PLXNB2, and through its PDZ domain with IGF1R beta subunit. Interacts with GCSAM. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain, predominantly in neuronal cell bodies. {ECO:0000269|PubMed:12492428}. +E9Q4N7 ARI1B_MOUSE AT-rich interactive domain-containing protein 1B (ARID domain-containing protein 1B) (BRG1-associated factor 250b) (BAF250B) 2244 237,795 Chain (1); Compositional bias (7); Domain (1); Modified residue (10); Motif (3) FUNCTION: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (PubMed:17640523). Binds DNA non-specifically. {ECO:0000250|UniProtKB:Q8NFD5, ECO:0000269|PubMed:17640523, ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8NFD5, ECO:0000255|PROSITE-ProRule:PRU00355}. SUBUNIT: Component of SWI/SNF chromatin remodeling complexes, in some of which it can be mutually exclusive with ARID1B/BAF250B. The canonical complex contains a catalytic subunit (either SMARCA4/BRG1/BAF190A or SMARCA2/BRM/BAF190B), and at least SMARCE1, ACTL6A/BAF53, SMARCC1/BAF155, SMARCC2/BAF170, and SMARCB1/SNF5/BAF47. Other subunits specific to each of the complexes may also be present permitting several possible combinations developmentally and tissue specific. Component of the BAF (SWI/SNF-A) complex, which includes at least actin (ACTB), ARID1A/BAF250A, ARID1B/BAF250B, SMARCA2/BRM, SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57, SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C (By similarity). In muscle cells, the BAF complex also contains DPF3. Component of neural progenitors-specific chromatin remodeling complex (npBAF complex) composed of at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, PHF10/BAF45A, ACTL6A/BAF53A and actin. Component of neuron-specific chromatin remodeling complex (nBAF complex) composed of at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, DPF1/BAF45B, DPF3/BAF45C, ACTL6B/BAF53B and actin (PubMed:17640523). Component of a SWI/SNF-like EBAFb complex, at least composed of SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, ACTL6A/BAF53A, SMARCE1/BAF57, SMARCD1/BAF60A, SMARCD2/BAF60B, SMARCC1/BAF155, SMARCC2/BAF170, ARID1B/BAF250B, MLLT1/ENL and actin. Interacts through its C-terminus with SMARCA2/BRM/BAF190B and SMARCA4/BRG1/BAF190A. Interacts with SMARCC1/BAF155 (By similarity). {ECO:0000250|UniProtKB:Q8NFD5, ECO:0000269|PubMed:17640523, ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}. +Q3SXC5 ARL14_MOUSE ADP-ribosylation factor-like protein 14 (ADP-ribosylation factor 7) 192 21,835 Chain (1); Initiator methionine (1); Lipidation (1); Nucleotide binding (3) FUNCTION: GTPase that recruits MYO1E to MHC class II-containing vesicles via the effector protein ARL14EP and hence controls the movement of these vesicles along the actin cytoskeleton in dendritic cells. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasmic vesicle. Note=Colocalizes with MHC II-containing cytoplasmic vesicles. {ECO:0000250}. SUBUNIT: Interacts with ARL14EP. {ECO:0000250}. +Q8BGR6 ARL15_MOUSE ADP-ribosylation factor-like protein 15 (ADP-ribosylation factor-related protein 2) (ARF-related protein 2) 204 22,905 Chain (1); Nucleotide binding (3) +Q9Z1K6 ARI2_MOUSE E3 ubiquitin-protein ligase ARIH2 (ARI-2) (Protein ariadne-2 homolog) (EC 2.3.2.31) (RING-type E3 ubiquitin transferase ARIH2) (Triad1 protein) (UbcM4-interacting protein 48) 492 57,697 Active site (1); Chain (1); Metal binding (24); Modified residue (1); Region (3); Zinc finger (3) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase, which catalyzes ubiquitination of target proteins together with ubiquitin-conjugating enzyme E2 UBE2L3 (By similarity). Acts as an atypical E3 ubiquitin-protein ligase by working together with cullin-5-RING ubiquitin ligase complex (ECS complex, also named CRL5 complex) and initiating ubiquitination of ECS substrates: associates with ECS complex and specifically mediates addition of the first ubiquitin on ECS targets (By similarity). The initial ubiquitin is then elongated (By similarity). E3 ubiquitin-protein ligase activity is activated upon binding to neddylated form of the ECS complex. Mediates 'Lys-6', 'Lys-48'-and 'Lys-63'-linked polyubiquitination. May play a role in myelopoiesis (By similarity). {ECO:0000250|UniProtKB:O95376, ECO:0000250|UniProtKB:Q9Y4X5}. PTM: Ubiquitinated. Ubiquitination promotes proteasomal degradation. {ECO:0000250|UniProtKB:O95376}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O95376}. Cytoplasm {ECO:0000250|UniProtKB:O95376}. SUBUNIT: Interacts (via RING-type zinc finger 1) with UBE2L3. Interacts (via RING-type zinc finger 2) with UBE2N. Interacts with neddylated CUL5. Interacts (via RING-type 2) with GFI1B. Interacts with GFI1; prevents its ubiquitination and proteasomal degradation. {ECO:0000250|UniProtKB:O95376}. DOMAIN: Members of the RBR family are atypical E3 ligases. They interact with the E2 conjugating enzyme UBE2L3 and function like HECT-type E3 enzymes: they bind E2s via the first RING-type zinc finger, but require an obligate trans-thiolation step during the ubiquitin transfer, requiring a conserved active site Cys residue in the second RING-type zinc finger. The active site probably forms a thioester intermediate with ubiquitin taken from the active-site cysteine of the E2 before ultimately transferring it to a Lys residue on the substrate. {ECO:0000250|UniProtKB:Q9Y4X5}.; DOMAIN: The Ariadne domain inhibits activity by masking the second RING-type zinc finger that contains the active site. {ECO:0000250|UniProtKB:Q9Y4X5}. +Q9Z1N7 ARI3B_MOUSE AT-rich interactive domain-containing protein 3B (ARID domain-containing protein 3B) (Bright and dead ringer protein) (Bright-like protein) 568 61,015 Alternative sequence (4); Chain (1); Compositional bias (4); Domain (2); Modified residue (4); Region (2); Sequence conflict (1) FUNCTION: Transcription factor involved in the production of cranial mesenchymal tissues. Favors nuclear targeting of ARID3A. {ECO:0000269|PubMed:16530748}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355}. SUBUNIT: Heterodimer with ARID3A. Interacts with unphosphorylated RB1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed at high levels in testis. Also expressed in prostate, thyroid and thymus. {ECO:0000269|PubMed:16530748}. +Q8K327 CHAP1_MOUSE Chromosome alignment-maintaining phosphoprotein 1 (Zinc finger protein 828) 802 87,561 Chain (1); Compositional bias (1); Cross-link (5); Erroneous initiation (1); Modified residue (45); Region (3); Sequence conflict (5); Zinc finger (1) FUNCTION: Required for proper alignment of chromosomes at metaphase and their accurate segregation during mitosis. Involved in the maintenance of spindle microtubules attachment to the kinetochore during sister chromatid biorientation. May recruit CENPE and CENPF to the kinetochore (By similarity). {ECO:0000250}. PTM: Phosphorylated by CDK1. Mitotic phosphorylation is required for the attachment of spindle microtubules to the kinetochore (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. SUBUNIT: Interacts with MAD2L2. Interacts with POGZ, CBX1, CBX3 and CBX5 (By similarity). {ECO:0000250}. +Q61767 3BHS4_MOUSE NADPH-dependent 3-keto-steroid reductase Hsd3b4 (3 beta-hydroxysteroid dehydrogenase type 4) (3 beta-hydroxysteroid dehydrogenase type IV) (3 beta-HSD IV) (EC 1.1.1.270) (Dihydrotestosterone 3-ketoreductase) (EC 1.1.1.210) 373 41,766 Active site (1); Binding site (2); Chain (1); Modified residue (1); Nucleotide binding (1); Transmembrane (1) TRANSMEM 288 308 Helical. {ECO:0000255}. Steroid metabolism. FUNCTION: Responsible for the reduction of the oxo group on the C-3 of 5alpha-androstane steroids. Catalyzes the conversion of dihydrotestosterone to its inactive form 5alpha-androstanediol, that does not bind androgen receptor/AR. Does not function as an isomerase. {ECO:0000269|PubMed:8145763}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. Mitochondrion membrane; Single-pass membrane protein. TISSUE SPECIFICITY: Kidney (at protein level); found only in the cortex, appears to be associated with the proximal tubules; and a minor expression in testis. {ECO:0000269|PubMed:8145763}. +Q99L13 3HIDH_MOUSE 3-hydroxyisobutyrate dehydrogenase, mitochondrial (HIBADH) (EC 1.1.1.31) 335 35,440 Active site (1); Binding site (3); Chain (1); Modified residue (19); Nucleotide binding (2); Sequence conflict (1); Transit peptide (1) Amino-acid degradation; L-valine degradation. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +P12961 7B2_MOUSE Neuroendocrine protein 7B2 (Secretogranin V) (Secretogranin-5) (Secretory granule endocrine protein I) [Cleaved into: N-terminal peptide; C-terminal peptide] 212 23,866 Chain (2); Disulfide bond (1); Modified residue (2); Mutagenesis (2); Peptide (1); Sequence conflict (4); Signal peptide (1) FUNCTION: Acts as a molecular chaperone for PCSK2/PC2, preventing its premature activation in the regulated secretory pathway. Binds to inactive PCSK2 in the endoplasmic reticulum and facilitates its transport from there to later compartments of the secretory pathway where it is proteolytically matured and activated. Also required for cleavage of PCSK2 but does not appear to be involved in its folding. Plays a role in regulating pituitary hormone secretion. The C-terminal peptide inhibits PCSK2 in vitro. {ECO:0000269|PubMed:10089884, ECO:0000269|PubMed:9348280}. PTM: Proteolytically cleaved in the Golgi by a furin-like convertase to generate bioactive peptides. {ECO:0000269|PubMed:8034690}.; PTM: Sulfated on tyrosine residues. {ECO:0000269|PubMed:8034690}. SUBCELLULAR LOCATION: Secreted. Note=Neuroendocrine and endocrine secretory granules. SUBUNIT: Interacts with PCSK2/PC2 early in the secretory pathway. Dissociation occurs at later stages (By similarity). {ECO:0000250}. +P07361 A1AG2_MOUSE Alpha-1-acid glycoprotein 2 (AGP 2) (Orosomucoid-2) (OMD 2) 207 23,843 Chain (1); Disulfide bond (1); Glycosylation (5); Modified residue (1); Signal peptide (1) FUNCTION: Functions as transport protein in the blood stream. Binds various ligands in the interior of its beta-barrel domain (By similarity). Appears to function in modulating the activity of the immune system during the acute-phase reaction. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. DOMAIN: Contains a beta-barrel that binds various ligands in its interior. {ECO:0000250}. TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma. +Q14BT6 A4GCT_MOUSE Alpha-1,4-N-acetylglucosaminyltransferase (Alpha4GnT) (EC 2.4.1.-) 341 39,276 Chain (1); Glycosylation (1); Motif (1); Topological domain (2); Transmembrane (1) TRANSMEM 5 25 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 4 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 26 341 Lumenal. {ECO:0000305}. Protein modification; protein glycosylation. FUNCTION: Catalyzes the transfer of N-acetylglucosamine (GlcNAc) to core 2 branched O-glycans. Necessary for the synthesis of type III mucin which is specifically produced in the stomach, duodenum, and pancreatic duct. May protect against inflammation-associated gastric adenocarcinoma. {ECO:0000269|PubMed:22307328}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. DOMAIN: The conserved DXD motif is involved in enzyme activity. {ECO:0000250|UniProtKB:Q9JI93}. +Q9DCQ7 A1AT6_MOUSE Alpha-1-antitrypsin 1-6 (Alpha-1 protease inhibitor 6) (Alpha-1-antiproteinase) (Serine protease inhibitor 1-6) (Serine protease inhibitor A1f) (Serpin A1f) 411 46,337 Alternative sequence (1); Chain (1); Glycosylation (4); Sequence conflict (12); Signal peptide (1); Site (1) FUNCTION: Inhibitor of serine proteases. {ECO:0000250|UniProtKB:P07758}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P07758}. DOMAIN: The reactive center loop (RCL) extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site within the RCL, establishing a covalent linkage between the carboxyl group of the serpin reactive site and the serine hydroxyl of the protease. The resulting inactive serpin-protease complex is highly stable. Variability within the reactive center loop (RCL) sequences of Serpina1-related genes may determine target protease specificity (By similarity). {ECO:0000250|UniProtKB:P01009, ECO:0000250|UniProtKB:P07758}. TISSUE SPECIFICITY: Expressed predominantly in epididymis where it is found in the epithelial cells of the caput, corpus and cauda epididymis. {ECO:0000269|PubMed:16707773}. +Q7TSV6 AATC2_MOUSE Putative aspartate aminotransferase, cytoplasmic 2 (EC 2.6.1.1) (Glutamate oxaloacetate transaminase 1-like protein 1) (Transaminase A-like protein 1) 404 45,458 Alternative sequence (1); Chain (1); Modified residue (1) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +O54950 AAKG1_MOUSE 5'-AMP-activated protein kinase subunit gamma-1 (AMPK gamma1) (AMPK subunit gamma-1) (AMPKg) 330 37,520 Binding site (9); Chain (1); Domain (4); Modified residue (3); Motif (1); Nucleotide binding (6); Sequence conflict (4) FUNCTION: AMP/ATP-binding subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (PRKAA1 or PRKAA2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits. ADP also stimulates phosphorylation, without stimulating already phosphorylated catalytic subunit. ATP promotes dephosphorylation of catalytic subunit, rendering the AMPK enzyme inactive (By similarity). {ECO:0000250}. PTM: Phosphorylated by ULK1 and ULK2; leading to negatively regulate AMPK activity and suggesting the existence of a regulatory feedback loop between ULK1, ULK2 and AMPK. {ECO:0000269|PubMed:21460634}. SUBUNIT: AMPK is a heterotrimer of an alpha catalytic subunit (PRKAA1 or PRKAA2), a beta (PRKAB1 or PRKAB2) and a gamma non-catalytic subunits (PRKAG1, PRKAG2 or PRKAG3). Interacts with FNIP1 and FNIP2 (By similarity). {ECO:0000250}. DOMAIN: The AMPK pseudosubstrate motif resembles the sequence around sites phosphorylated on target proteins of AMPK, except the presence of a non-phosphorylatable residue in place of Ser. In the absence of AMP this pseudosubstrate sequence may bind to the active site groove on the alpha subunit (PRKAA1 or PRKAA2), preventing phosphorylation by the upstream activating kinase STK11/LKB1 (By similarity). {ECO:0000250}.; DOMAIN: The 4 CBS domains mediate binding to nucleotides. Of the 4 potential nucleotide-binding sites, 3 are occupied, designated as sites 1, 3, and 4 based on the CBS modules that provide the acidic residue for coordination with the 2'- and 3'-hydroxyl groups of the ribose of AMP. Of these, site 4 appears to be a structural site that retains a tightly held AMP molecule (AMP 3). The 2 remaining sites, 1 and 3, can bind either AMP, ADP or ATP. Site 1 (AMP, ADP or ATP 1) is the high-affinity binding site and likely accommodates AMP or ADP. Site 3 (AMP, ADP or ATP 2) is the weakest nucleotide-binding site on the gamma subunit, yet it is exquisitely sensitive to changes in nucleotide levels and this allows AMPK to respond rapidly to changes in cellular energy status. Site 3 is likely to be responsible for protection of a conserved threonine in the activation loop of the alpha catalytic subunit through conformational changes induced by binding of AMP or ADP. {ECO:0000250|UniProtKB:P80385}. +Q8BL65 ABLM2_MOUSE Actin-binding LIM protein 2 (abLIM-2) (Actin-binding LIM protein family member 2) 612 68,107 Alternative sequence (5); Chain (1); Compositional bias (1); Domain (5); Metal binding (16); Modified residue (10); Sequence conflict (2) FUNCTION: May act as scaffold protein. May stimulate ABRA activity and ABRA-dependent SRF transcriptional activity. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17194709}. Note=In skeletal muscle, sarcomeric or cosarcomeric localization. SUBUNIT: Interacts with F-actin and ABRA. {ECO:0000269|PubMed:17194709}. TISSUE SPECIFICITY: Expressed in brain. Highly expressed in caudate/putamen, moderately expressed in the olfactory bulb. In the hippocampus, expressed in the CA1, CA2 and CA3 fields. In the cerebellum, expressed in Purkinje cells. {ECO:0000269|PubMed:17194709}. +Q9Z1Q2 ABHGA_MOUSE Protein ABHD16A (EC 3.-.-.-) (Alpha/beta hydrolase domain-containing protein 16A) (Abhydrolase domain-containing protein 16A) (HLA-B-associated transcript 5) 558 63,086 Active site (3); Chain (1); Domain (1); Transmembrane (2) TRANSMEM 60 80 Helical. {ECO:0000255}.; TRANSMEM 93 113 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q5EG47 AAPK1_MOUSE 5'-AMP-activated protein kinase catalytic subunit alpha-1 (AMPK subunit alpha-1) (EC 2.7.11.1) (Acetyl-CoA carboxylase kinase) (ACACA kinase) (EC 2.7.11.27) (Hydroxymethylglutaryl-CoA reductase kinase) (HMGCR kinase) (EC 2.7.11.31) (Tau-protein kinase PRKAA1) (EC 2.7.11.26) 559 63,929 Active site (1); Beta strand (8); Binding site (1); Chain (1); Domain (1); Helix (8); Modified residue (16); Mutagenesis (1); Nucleotide binding (1); Region (1); Sequence conflict (1); Turn (5) FUNCTION: Catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Regulates lipid synthesis by phosphorylating and inactivating lipid metabolic enzymes such as ACACA, ACACB, GYS1, HMGCR and LIPE; regulates fatty acid and cholesterol synthesis by phosphorylating acetyl-CoA carboxylase (ACACA and ACACB) and hormone-sensitive lipase (LIPE) enzymes, respectively. Regulates insulin-signaling and glycolysis by phosphorylating IRS1, PFKFB2 and PFKFB3. AMPK stimulates glucose uptake in muscle by increasing the translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane, possibly by mediating phosphorylation of TBC1D4/AS160. Regulates transcription and chromatin structure by phosphorylating transcription regulators involved in energy metabolism such as CRTC2/TORC2, FOXO3, histone H2B, HDAC5, MEF2C, MLXIPL/ChREBP, EP300, HNF4A, p53/TP53, SREBF1, SREBF2 and PPARGC1A. Acts as a key regulator of glucose homeostasis in liver by phosphorylating CRTC2/TORC2, leading to CRTC2/TORC2 sequestration in the cytoplasm. In response to stress, phosphorylates 'Ser-36' of histone H2B (H2BS36ph), leading to promote transcription. Acts as a key regulator of cell growth and proliferation by phosphorylating TSC2, RPTOR and ATG1/ULK1: in response to nutrient limitation, negatively regulates the mTORC1 complex by phosphorylating RPTOR component of the mTORC1 complex and by phosphorylating and activating TSC2. In response to nutrient limitation, promotes autophagy by phosphorylating and activating ATG1/ULK1. In that process also activates WDR45. In response to nutrient limitation, phosphorylates transcription factor FOXO3 promoting FOXO3 mitochondrial import (PubMed:23283301). AMPK also acts as a regulator of circadian rhythm by mediating phosphorylation of CRY1, leading to destabilize it. May regulate the Wnt signaling pathway by phosphorylating CTNNB1, leading to stabilize it. Also has tau-protein kinase activity: in response to amyloid beta A4 protein (APP) exposure, activated by CAMKK2, leading to phosphorylation of MAPT/TAU; however the relevance of such data remains unclear in vivo. Also phosphorylates CFTR, EEF2K, KLC1, NOS3 and SLC12A1. {ECO:0000269|PubMed:15878856, ECO:0000269|PubMed:16148943, ECO:0000269|PubMed:16308421, ECO:0000269|PubMed:16804075, ECO:0000269|PubMed:16804077, ECO:0000269|PubMed:18439900, ECO:0000269|PubMed:19833968, ECO:0000269|PubMed:20361929, ECO:0000269|PubMed:20647423, ECO:0000269|PubMed:21205641, ECO:0000269|PubMed:21258367, ECO:0000269|PubMed:21459323, ECO:0000269|PubMed:23283301}. PTM: Phosphorylated at Thr-183 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. Also phosphorylated at Thr-183 by CAMKK2; triggered by a rise in intracellular calcium ions, without detectable changes in the AMP/ATP ratio. CAMKK1 can also phosphorylate Thr-183, but at a much lower level. Dephosphorylated by protein phosphatase 2A and 2C (PP2A and PP2C). Phosphorylated by ULK1 and ULK2; leading to negatively regulate AMPK activity and suggesting the existence of a regulatory feedback loop between ULK1, ULK2 and AMPK. Dephosphorylated by PPM1A and PPM1B (By similarity). {ECO:0000250}.; PTM: Ubiquitinated. {ECO:0000269|PubMed:18254724}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000269|PubMed:19833968}. Note=In response to stress, recruited by p53/TP53 to specific promoters. SUBUNIT: AMPK is a heterotrimer of an alpha catalytic subunit (PRKAA1 or PRKAA2), a beta (PRKAB1 or PRKAB2) and a gamma non-catalytic subunits (PRKAG1, PRKAG2 or PRKAG3). Interacts with FNIP1 and FNIP2. DOMAIN: The AIS (autoinhibitory sequence) region shows some sequence similarity with the ubiquitin-associated domains and represses kinase activity. {ECO:0000250}. +Q9DBM0 ABCG8_MOUSE ATP-binding cassette sub-family G member 8 (Sterolin-2) 673 75,996 Alternative sequence (1); Chain (1); Domain (2); Glycosylation (1); Mutagenesis (8); Sequence conflict (1); Topological domain (7); Transmembrane (6) TRANSMEM 417 437 Helical; Name=1. {ECO:0000250|UniProtKB:Q9H221}.; TRANSMEM 448 468 Helical; Name=2. {ECO:0000250|UniProtKB:Q9H221}.; TRANSMEM 498 518 Helical; Name=3. {ECO:0000250|UniProtKB:Q9H221}.; TRANSMEM 528 548 Helical; Name=4. {ECO:0000250|UniProtKB:Q9H221}.; TRANSMEM 556 576 Helical; Name=5. {ECO:0000250|UniProtKB:Q9H221}.; TRANSMEM 640 660 Helical; Name=6. {ECO:0000250|UniProtKB:Q9H221}. TOPO_DOM 1 416 Cytoplasmic. {ECO:0000250|UniProtKB:Q9H221}.; TOPO_DOM 438 447 Extracellular. {ECO:0000250|UniProtKB:Q9H221}.; TOPO_DOM 469 497 Cytoplasmic. {ECO:0000250|UniProtKB:Q9H221}.; TOPO_DOM 519 527 Extracellular. {ECO:0000250|UniProtKB:Q9H221}.; TOPO_DOM 549 555 Cytoplasmic. {ECO:0000250|UniProtKB:Q9H221}.; TOPO_DOM 577 639 Extracellular. {ECO:0000250|UniProtKB:Q9H221}.; TOPO_DOM 661 673 Cytoplasmic. {ECO:0000250|UniProtKB:Q9H221}. FUNCTION: ABCG5 and ABCG8 form an obligate heterodimer that mediates Mg(2+)- and ATP-dependent sterol transport across the cell membrane (PubMed:16352607, PubMed:16867993, PubMed:18402465). Plays an essential role in the selective transport of the dietary cholesterol in and out of the enterocytes and in the selective sterol excretion by the liver into bile (PubMed:12444248, PubMed:14504269, PubMed:14657202, PubMed:25378657). Plays an important role in preventing the accumulation of dietary plant sterols in the body (PubMed:12444248, PubMed:14657202). Required for normal sterol homeostasis (PubMed:12444248, PubMed:14657202). The heterodimer with ABCG5 has ATPase activity (PubMed:16352607, PubMed:16867993). {ECO:0000269|PubMed:12444248, ECO:0000269|PubMed:14504269, ECO:0000269|PubMed:14657202, ECO:0000269|PubMed:16352607, ECO:0000269|PubMed:16867993, ECO:0000269|PubMed:18402465, ECO:0000269|PubMed:25378657}. PTM: N-glycosylated (PubMed:12208867, PubMed:12444248, PubMed:16867993, PubMed:15054092, PubMed:18402465). N-glycosylation is important for efficient export out of the endoplasmic reticulum (PubMed:15054092). {ECO:0000269|PubMed:12208867, ECO:0000269|PubMed:12444248, ECO:0000269|PubMed:15054092, ECO:0000269|PubMed:16867993, ECO:0000269|PubMed:18402465}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12208867, ECO:0000269|PubMed:18402465, ECO:0000305|PubMed:16352607}; Multi-pass membrane protein {ECO:0000305}. Apical cell membrane {ECO:0000269|PubMed:12208867, ECO:0000269|PubMed:14504269, ECO:0000269|PubMed:16867993, ECO:0000269|PubMed:18402465}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Heterodimer with ABCG5. {ECO:0000269|PubMed:12208867, ECO:0000269|PubMed:14504269, ECO:0000269|PubMed:15054092, ECO:0000269|PubMed:16352607, ECO:0000269|PubMed:16867993, ECO:0000269|PubMed:18402465}. DOMAIN: A functional Walker motif (consensus sequence G-X-X-G-X-G-K-[ST]-T) is expected to bind ATP. The essential Lys in this region is not conserved in ABCG8 (G-S-S-G-C-R-A-S) and is not required for transport activity mediated by the heterodimer with ABCG5. {ECO:0000269|PubMed:16352607}. TISSUE SPECIFICITY: Detected in liver and jejunum (at protein level) (PubMed:12444248, PubMed:18402465, PubMed:25378657). Expressed in jejunum and ileum and, at lower level, in the liver (PubMed:11907139, PubMed:11099417, PubMed:12444248, PubMed:15040800, PubMed:25378657). {ECO:0000269|PubMed:11099417, ECO:0000269|PubMed:11907139, ECO:0000269|PubMed:12444248, ECO:0000269|PubMed:15040800, ECO:0000269|PubMed:18402465, ECO:0000269|PubMed:25378657}. +P48410 ABCD1_MOUSE ATP-binding cassette sub-family D member 1 (Adrenoleukodystrophy protein) (ALDP) 736 81,859 Chain (1); Domain (2); Glycosylation (1); Nucleotide binding (1); Region (3); Transmembrane (5) TRANSMEM 92 112 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 131 151 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 238 258 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 338 358 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 473 493 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}. FUNCTION: Plays a role in the transport of free very-long-chain fatty acids (VLCFAs) as well as their CoA-esters across the peroxisomal membrane by acting as an ATP-specific binding subunit releasing ADP after ATP hydrolysis (By similarity). Thus, plays a role in regulation of VLCFAs and energy metabolism namely, in the degradation and biosynthesis of fatty acids by beta-oxidation, mitochondrial function and microsomal fatty acid elongation (PubMed:25255441, PubMed:9418970, PubMed:9126326, PubMed:9256488, PubMed:18854420, PubMed:23123468, PubMed:26108493, PubMed:23604518, PubMed:25583114). Involved in several processes; namely, controls the active myelination phase by negatively regulating the microsomal fatty acid elongation activity and may also play a role in axon and myelin maintenance (PubMed:11875044, PubMed:26108493, PubMed:15489218). Controls also the cellular response to oxidative stress by regulating mitochondrial function like, mitochondrial oxidative phosphorylation and depolarization (PubMed:25583114, PubMed:23604518, PubMed:18344354, PubMed:22521832). And finally controls the inflammatory response by positively regulating peroxisomal beta-oxidation of VLCFAs (PubMed:18723473). {ECO:0000250|UniProtKB:D3ZHR2, ECO:0000250|UniProtKB:P33897, ECO:0000269|PubMed:11875044, ECO:0000269|PubMed:15489218, ECO:0000269|PubMed:18344354, ECO:0000269|PubMed:18723473, ECO:0000269|PubMed:18854420, ECO:0000269|PubMed:22521832, ECO:0000269|PubMed:23123468, ECO:0000269|PubMed:23604518, ECO:0000269|PubMed:25255441, ECO:0000269|PubMed:25583114, ECO:0000269|PubMed:26108493, ECO:0000269|PubMed:9126326, ECO:0000269|PubMed:9256488, ECO:0000269|PubMed:9418970}. PTM: Tyrosine-phosphorylated. {ECO:0000250|UniProtKB:D3ZHR2}. SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000250|UniProtKB:P33897}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000250|UniProtKB:P33897}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P33897}. Lysosome membrane {ECO:0000250|UniProtKB:P33897}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P33897}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P33897}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P33897}. SUBUNIT: Can form homooligomers, homodimers and heterodimers with ABCD2/ALDR and ABCD3/PMP70 (PubMed:15276650). Dimerization is necessary to form an active transporter. Interacts with PEX19; facilitates ABCD1 insertion into the peroxisome membrane (By similarity). {ECO:0000250|UniProtKB:P33897, ECO:0000269|PubMed:15276650}. DOMAIN: The NH2-terminal transmembrane domaine (TMD) is involved in the recognition of substrates, and undergoes a conformational change upon ATP binding to the COOH-terminal nucleotide binding domain (NBD). {ECO:0000250|UniProtKB:P33897}. TISSUE SPECIFICITY: Widely expressed at low levels with higher levels in heart, lung, intestine and spleen than in skeletal muscle, brain, liver and kidney. {ECO:0000269|PubMed:10504404}. +Q61102 ABCB7_MOUSE ATP-binding cassette sub-family B member 7, mitochondrial (ATP-binding cassette transporter 7) (ABC transporter 7 protein) 752 82,581 Binding site (1); Chain (1); Compositional bias (1); Domain (2); Modified residue (6); Nucleotide binding (1); Sequence conflict (3); Transmembrane (6) TRANSMEM 141 161 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 186 206 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 260 280 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 291 311 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 383 403 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 410 430 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}. FUNCTION: Could be involved in the transport of heme from the mitochondria to the cytosol. Plays a central role in the maturation of cytosolic iron-sulfur (Fe/S) cluster-containing proteins (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. SUBUNIT: Homodimer or heterodimer. {ECO:0000305}. +P56485 ACKR3_MOUSE Atypical chemokine receptor 3 (C-X-C chemokine receptor type 7) (CXC-R7) (CXCR-7) (Chemokine orphan receptor 1) (G-protein coupled receptor RDC1 homolog) (RDC-1) 362 41,636 Chain (1); Disulfide bond (1); Glycosylation (2); Modified residue (3); Region (1); Sequence conflict (2); Topological domain (8); Transmembrane (7) TRANSMEM 48 68 Helical; Name=1. {ECO:0000255}.; TRANSMEM 82 102 Helical; Name=2. {ECO:0000255}.; TRANSMEM 119 139 Helical; Name=3. {ECO:0000255}.; TRANSMEM 163 183 Helical; Name=4. {ECO:0000255}.; TRANSMEM 214 234 Helical; Name=5. {ECO:0000255}.; TRANSMEM 253 273 Helical; Name=6. {ECO:0000255}.; TRANSMEM 297 319 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 47 Extracellular. {ECO:0000255}.; TOPO_DOM 69 81 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 103 118 Extracellular. {ECO:0000255}.; TOPO_DOM 140 162 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 184 213 Extracellular. {ECO:0000255}.; TOPO_DOM 235 252 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 274 296 Extracellular. {ECO:0000255}.; TOPO_DOM 320 362 Cytoplasmic. {ECO:0000255}. FUNCTION: Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing receptor) or chemokine-scavenging receptor or chemokine decoy receptor. Acts as a receptor for chemokines CXCL11 and CXCL12/SDF1. Chemokine binding does not activate G-protein-mediated signal transduction but instead induces beta-arrestin recruitment, leading to ligand internalization and activation of MAPK signaling pathway. Required for regulation of CXCR4 protein levels in migrating interneurons, thereby adapting their chemokine responsiveness. In glioma cells, transduces signals via MEK/ERK pathway, mediating resistance to apoptosis. Promotes cell growth and survival. Not involved in cell migration, adhesion or proliferation of normal hematopoietic progenitors but activated by CXCL11 in malignant hemapoietic cells, leading to phosphorylation of ERK1/2 (MAPK3/MAPK1) and enhanced cell adhesion and migration. Plays a regulatory role in CXCR4-mediated activation of cell surface integrins by CXCL12. Required for heart valve development. {ECO:0000269|PubMed:17804806, ECO:0000269|PubMed:18442043, ECO:0000269|PubMed:20161793, ECO:0000269|PubMed:21220100, ECO:0000269|PubMed:21246655}. PTM: The Ser/Thr residues in the C-terminal cytoplasmic tail may be phosphorylated. {ECO:0000250}.; PTM: Ubiquitinated at the Lys residues in its C-terminal cytoplasmic tail and is essential for correct trafficking from and to the cell membrane. Deubiquitinated by CXCL12-stimulation in a reversible manner (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21220100}; Multi-pass membrane protein {ECO:0000269|PubMed:21220100}. Cytoplasm, perinuclear region {ECO:0000250}. Early endosome {ECO:0000250}. Recycling endosome {ECO:0000269|PubMed:21220100}. Note=Predominantly localizes to endocytic vesicles, and upon stimulation by the ligand is internalized via clathrin-coated pits in a beta-arrestin -dependent manner. Once internalized, the ligand dissociates from the receptor, and is targeted to degradation while the receptor is recycled back to the cell membrane (By similarity). {ECO:0000250}. SUBUNIT: Homodimer. Can form heterodimers with CXCR4; heterodimerization may regulate CXCR4 signaling activity (By similarity).Interacts with ARRB1 and ARRB2 (By similarity). {ECO:0000250}. DOMAIN: The C-terminal cytoplasmic tail, plays a key role in: correct trafficking to the cell membrane, recruitment of beta-arrestin, ubiquitination, and in chemokine scavenging and signaling functions. The Ser/Thr residues and the Lys residues in the C-terminal cytoplasmic tail are essential for beta-arrestin recruitment and ubiquitination respectively (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Not detected in blood, liver, lung and heart, but high expression detected in several tumor cell lines (at protein level). Expressed in heart, spleen, kidney, lung, ovary, brain, testis, astrocytes, neutrophils and B-lymphocytes. {ECO:0000269|PubMed:16940167, ECO:0000269|PubMed:17804806, ECO:0000269|PubMed:9510554}. +Q8BX37 ACP7_MOUSE Acid phosphatase type 7 (EC 3.1.3.2) (Purple acid phosphatase long form) 438 50,663 Chain (1); Erroneous initiation (3); Glycosylation (3); Metal binding (8); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q9CQJ0 ACO15_MOUSE Acyl-coenzyme A thioesterase THEM5 (Acyl-CoA thioesterase THEM5) (EC 3.1.2.2) (Acyl-coenzyme A thioesterase 15) (Thioesterase superfamily member 5) 248 27,865 Active site (1); Alternative sequence (1); Chain (1) FUNCTION: Has acyl-CoA thioesterase activity towards long-chain (C16 and C18) fatty acyl-CoA substrates, with a preference for linoleoyl-CoA and other unsaturated long-chain fatty acid-CoA esters. Plays an important role in mitochondrial fatty acid metabolism, and in remodeling of the mitochondrial lipid cardiolipin. Required for normal mitochondrial function. {ECO:0000269|PubMed:22586271}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +Q9R182 ANGL3_MOUSE Angiopoietin-related protein 3 (Angiopoietin-like protein 3) [Cleaved into: ANGPTL3(17-224)] 455 52,543 Chain (2); Coiled coil (1); Disulfide bond (2); Domain (1); Glycosylation (5); Mutagenesis (2); Region (3); Signal peptide (1) FUNCTION: Acts in part as a hepatokine that is involved in regulation of lipid and glucose metabolism (PubMed:11788823, PubMed:12671033). Proposed to play a role in the trafficking of energy substrates to either storage or oxidative tissues in response to food intake (PubMed:26305978). Has a stimulatory effect on plasma triglycerides (TG), which is achieved by suppressing plasma TG clearance via inhibition of LPL activity; the function seems to be specific for the feeding conditions. The inhibition of LPL activity appears to be an indirect mechanism involving recruitment of proprotein convertases PCSK6 and FURIN to LPL leading to cleavage and dissociation of LPL from the cell surface; the function does not require ANGPTL3 proteolytic cleavage but seems to be mediated by the N-terminal domain, and is not inhibited by GPIHBP1 (PubMed:12909640, PubMed:16081640, PubMed:20581395). Can inhibit endothelial lipase, causing increased plasma levels of high density lipoprotein (HDL) cholesterol and phospholipids; the cleaved N-terminal domain is more efficient than the uncleaved proprotein (PubMed:17681148). Can bind to adipocytes to activate lipolysis, releasing free fatty acids and glycerol (By similarity). Suppresses LPL specifically in oxidative tissues which is required to route very low density lipoprotein (VLDL)-TG to white adipose tissue (WAT) for storage in response to food; the function may involve cooperation with circulating, liver-derived ANGPTL8 and ANGPTL4 expression in WAT (PubMed:26305978). Contributes to lower plasma levels of low density lipoprotein (LDL)-cholesterol by a mechanism that is independent of the canonical pathway implicating APOE and LDLR (PubMed:25954050). May stimulate hypothalamic LPL activity (PubMed:25338813). {ECO:0000250|UniProtKB:Q9Y5C1, ECO:0000269|PubMed:11788823, ECO:0000269|PubMed:12671033, ECO:0000269|PubMed:16081640, ECO:0000269|PubMed:17681148, ECO:0000269|PubMed:20581395, ECO:0000269|PubMed:25338813, ECO:0000269|PubMed:25954050, ECO:0000269|PubMed:26305978}.; FUNCTION: Involved in angiogenesis (PubMed:11877390). Binds to endothelial cells via integrin alpha-V/beta-3 (ITGAV:ITGB3), activates FAK, MAPK and Akt signaling pathways and induces cell adhesion and cell migration (By similarity). May increase the motility of podocytes. Secreted from podocytes, may modulate properties of glomerular endothelial cells involving integrin alpha-V/beta-3 and Akt signaling (By similarity). May induce actin filament rearrangements in podocytes implicating integrin alpha-V/beta-3 and Rac1 activation (PubMed:20633534, PubMed:24294595, PubMed:25710887). Binds to hematopoietic stem cells (HSC) and is involved in the regulation of HSC activity probably implicating down-regulation of IKZF1/IKAROS (PubMed:20959605). {ECO:0000250|UniProtKB:Q9Y5C1, ECO:0000269|PubMed:11877390, ECO:0000269|PubMed:20633534, ECO:0000269|PubMed:20959605, ECO:0000269|PubMed:24294595, ECO:0000269|PubMed:25710887}. PTM: In part proteolytically cleaved by proprotein convertases; proposed to be involved in activation. In primary hepatocytes is intracellularily predominantly processed by FURIN and extracellularily by FURIN and PCSK6/PACE4. In E18.5 embryos 75% of protein is found to be processed compared to 25 % in adults. {ECO:0000269|PubMed:17681148, ECO:0000269|PubMed:23918928}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23918928}. Cell projection, lamellipodium {ECO:0000269|PubMed:25710887}. Note=Colocalized with HSPG2 and activated ITGB3 on podocytes. {ECO:0000269|PubMed:20424482, ECO:0000269|PubMed:25710887}. SUBUNIT: Interacts with ANGPTL8 (By similarity). Interacts with ITGB3. {ECO:0000250|UniProtKB:Q9Y5C1, ECO:0000269|PubMed:25710887}. DOMAIN: The fibrinogen C-terminal domain is sufficient to mediate endothelial cell adhesion. {ECO:0000250|UniProtKB:Q9Y5C1}. TISSUE SPECIFICITY: Predominantly expressed in liver, weakly expressed in kidney and lung. Expressed in podocytes (at protein level). Expressed in hypothalamic neurons (at protein level). Expressed in bone marrow sinusoidal endothelial cells (at protein level). {ECO:0000269|PubMed:10644446, ECO:0000269|PubMed:20959605, ECO:0000269|PubMed:25338813, ECO:0000269|PubMed:25710887}. +Q400C8 AMZ2_MOUSE Archaemetzincin-2 (EC 3.4.-.-) (Archeobacterial metalloproteinase-like protein 2) 359 41,341 Active site (1); Alternative sequence (2); Chain (1); Erroneous initiation (3); Frameshift (1); Metal binding (7) FUNCTION: Zinc metalloprotease. Exhibits activity against angiotensin-3 in vitro. Does not hydrolyze neurogranin nor angiotensin-2 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Predominantly expressed in testis. {ECO:0000269|PubMed:17074343}. +Q80UP5 AN13A_MOUSE Ankyrin repeat domain-containing protein 13A 588 67,177 Chain (1); Domain (4); Erroneous initiation (1); Modified residue (2); Repeat (2) FUNCTION: Ubiquitin-binding protein that specifically recognizes and binds 'Lys-63'-linked ubiquitin. Does not bind 'Lys-48'-linked ubiquitin. Positively regulates the internalization of ligand-activated EGFR by binding to the Ub moiety of ubiquitinated EGFR at the cell membrane (By similarity). {ECO:0000250}. PTM: Monoubiquitinated, inhibits interaction with ubiquitinated EGFR. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane. Late endosome. Note=Interaction with EGFR may enhance association with the cell membrane. {ECO:0000250}. SUBUNIT: Interacts (via the UIM 3 and 4 repeats) with EGFR (ubiquitinated); the interaction is direct, inhibited by ANKRD13A monoubiquitination and may regulate EGFR internalization. {ECO:0000250}. DOMAIN: The UIM repeats 3 and 4 are required for binding to ubiquitinated EGFR and 'Lys-63'-linked ubiquitin. {ECO:0000250}. +P00687 AMY1_MOUSE Alpha-amylase 1 (EC 3.2.1.1) (1,4-alpha-D-glucan glucanohydrolase 1) (Salivary and hepatic alpha-amylase) 511 57,644 Active site (2); Binding site (3); Chain (1); Disulfide bond (5); Metal binding (4); Modified residue (1); Sequence conflict (11); Signal peptide (1); Site (1) SUBCELLULAR LOCATION: Secreted. SUBUNIT: Monomer. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in liver and saliva. +O08538 ANGP1_MOUSE Angiopoietin-1 (ANG-1) 498 57,519 Chain (1); Coiled coil (2); Disulfide bond (2); Domain (1); Glycosylation (5); Sequence conflict (1); Signal peptide (1) FUNCTION: Binds and activates TEK/TIE2 receptor by inducing its dimerization and tyrosine phosphorylation. Plays an important role in the regulation of angiogenesis, endothelial cell survival, proliferation, migration, adhesion and cell spreading, reorganization of the actin cytoskeleton, but also maintenance of vascular quiescence. Required for normal angiogenesis and heart development during embryogenesis. After birth, activates or inhibits angiogenesis, depending on the context. Inhibits angiogenesis and promotes vascular stability in quiescent vessels, where endothelial cells have tight contacts. In quiescent vessels, ANGPT1 oligomers recruit TEK to cell-cell contacts, forming complexes with TEK molecules from adjoining cells, and this leads to preferential activation of phosphatidylinositol 3-kinase and the AKT1 signaling cascades. In migrating endothelial cells that lack cell-cell adhesions, ANGT1 recruits TEK to contacts with the extracellular matrix, leading to the formation of focal adhesion complexes, activation of PTK2/FAK and of the downstream kinases MAPK1/ERK2 and MAPK3/ERK1, and ultimately to the stimulation of sprouting angiogenesis. Mediates blood vessel maturation/stability. Implicated in endothelial developmental processes later and distinct from that of VEGF. Appears to play a crucial role in mediating reciprocal interactions between the endothelium and surrounding matrix and mesenchyme (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Homooligomer. Interacts with TEK/TIE2 (By similarity). {ECO:0000250}. +Q3U0L2 AN33B_MOUSE Ankyrin repeat domain-containing protein 33B 486 53,203 Alternative sequence (5); Chain (1); Coiled coil (1); Modified residue (1); Repeat (5); Sequence conflict (1) +A8VU90 ANKL1_MOUSE Ankyrin repeat and LEM domain-containing protein 1 (EC 3.1.-.-) (Ankyrin repeat domain-containing protein 41) (LEM-domain containing protein 3) 534 58,441 Alternative sequence (1); Chain (1); Domain (2); Erroneous initiation (1); Frameshift (1); Motif (1); Repeat (4); Sequence caution (1); Sequence conflict (3) FUNCTION: Endonuclease that probably plays a role in the DNA damage response and DNA repair. {ECO:0000250|UniProtKB:Q8NAG6}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8NAG6}. Nucleus {ECO:0000250|UniProtKB:Q8NAG6}. Note=At the steady state, predominantly localizes in the cytoplasm. {ECO:0000250|UniProtKB:Q8NAG6}. SUBUNIT: Interacts (via LEM domain) with BANF1; the interaction may favor BANF1 dimerization. {ECO:0000250|UniProtKB:Q8NAG6}. DOMAIN: The LEM domain is required for GIY-YIG domain-mediated DNA cleavage and induction of DNA damage response. {ECO:0000250|UniProtKB:Q8NAG6}. TISSUE SPECIFICITY: Predominantly expressed in bone marrow, spleen, thymus, colon and ovary. Expressed also to a lesser extent in lymph nodes, liver and testis. {ECO:0000269|PubMed:27010503}. +Q810B6 ANFY1_MOUSE Rabankyrin-5 (Rank-5) (Ankyrin repeat and FYVE domain-containing protein 1) (Ankyrin repeats hooked to a zinc finger motif) 1169 128,653 Alternative sequence (2); Chain (1); Domain (1); Initiator methionine (1); Modified residue (2); Motif (1); Region (1); Repeat (21); Sequence conflict (10); Zinc finger (1) FUNCTION: Proposed effector of Rab5. Binds to phosphatidylinositol 3-phosphate (PI(3)P). Involved in homotypic early endosome fusion and to a lesser extent in heterotypic fusion of chlathrin-coated vesicles with early endosomes. Required for correct endosomal localization. Involved in the internalization and trafficking of activated tyrosine kinase receptors such as PDGFRB. Regulates the subcellular localization of the retromer complex in a EHD1-dependent manner. Involved in endosome-to-Golgi transport and biosynthetic transport to late endosomes and lysosomes indicative for a regulation of retromer complex-mediated retrograde transport (By similarity). Involved in macropinocytosis; the function is dependent on Rab5-GTP. {ECO:0000250|UniProtKB:Q9P2R3, ECO:0000269|PubMed:15328530}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10092534}. Endosome membrane {ECO:0000269|PubMed:10092534}; Peripheral membrane protein {ECO:0000269|PubMed:10092534}. Cytoplasmic vesicle {ECO:0000269|PubMed:15328530}. Note=Also associated with endosomal membranes. Localizes to macropinosomes. In kidney proximal tubule cells localizes to vesicle-like structures underneath the apical brush border. {ECO:0000269|PubMed:15328530}. SUBUNIT: Interacts with RAB5A (in GTP-bound form). Interacts with RHOD (independent of GTP-loaded status). Interacts with EHD1. Interacts with VPS26A; the interaction is indepenedent of EHD1 and is indicative for an association with the cargo recognition subcomplex of the retromer complex. {ECO:0000250|UniProtKB:Q9P2R3}. TISSUE SPECIFICITY: Expressed in kidney proximal tubule epithelial cells; at protein level. {ECO:0000269|PubMed:15328530}. +Q9DBG3 AP2B1_MOUSE AP-2 complex subunit beta (AP105B) (Adaptor protein complex AP-2 subunit beta) (Adaptor-related protein complex 2 subunit beta) (Beta-2-adaptin) (Beta-adaptin) (Clathrin assembly protein complex 2 beta large chain) (Plasma membrane adaptor HA2/AP2 adaptin beta subunit) 937 104,583 Alternative sequence (1); Chain (1); Compositional bias (1); Initiator methionine (1); Modified residue (5) FUNCTION: Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. The AP-2 beta subunit acts via its C-terminal appendage domain as a scaffolding platform for endocytic accessory proteins; at least some clathrin-associated sorting proteins (CLASPs) are recognized by their [DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif. The AP-2 beta subunit binds to clathrin heavy chain, promoting clathrin lattice assembly; clathrin displaces at least some CLASPs from AP2B1 which probably then can be positioned for further coat assembly (By similarity). {ECO:0000250, ECO:0000269|PubMed:14745134, ECO:0000269|PubMed:15473838}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Membrane, coated pit {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=AP-2 appears to be excluded from internalizing CCVs and to disengage from sites of endocytosis seconds before internalization of the nascent CCV. {ECO:0000250}. SUBUNIT: Adaptor protein complex 2 (AP-2) is a heterotetramer composed of two large adaptins (alpha-type subunit AP2A1 or AP2A2 and beta-type subunit AP2B1), a medium adaptin (mu-type subunit AP2M1) and a small adaptin (sigma-type subunit AP2S1). Interacts with EPN1. Interacts with EPS15; clathrin competes with EPS15. Interacts with SNAP91; clathrin competes with SNAP91. Interacts with CLTC; clathrin competes with EPS15, SNAP91 and PIP5K1C. Interacts with LDLRAP1. Interacts with AMPH and BIN1. Interacts with ARF6 (GDP-bound). Interacts (dephosphorylated at Tyr-737) with ARRB1; phosphorylation of AP2B1 at Tyr-737 disrupts the interaction. Interacts with SLC2A8. Interacts with SCYL1 and SCYL2. Interacts with TGFBR1 and TGFBR2. Interacts with PIP5K1C; clathrin competes with PIP5K1C. Interacts with DENND1B. Interacts with FCHO1. Interacts with RFTN1. Interacts with KIAA1107 (PubMed:29262337). {ECO:0000250|UniProtKB:P62944, ECO:0000250|UniProtKB:P63010, ECO:0000269|PubMed:29262337}. +Q9DB50 AP1S2_MOUSE AP-1 complex subunit sigma-2 (Adaptor protein complex AP-1 subunit sigma-1B) (Adaptor-related protein complex 1 subunit sigma-1B) (Clathrin assembly protein complex 1 sigma-1B small chain) (Golgi adaptor HA1/AP1 adaptin sigma-1B subunit) (Sigma 1B subunit of AP-1 clathrin) (Sigma-adaptin 1B) (Sigma1B-adaptin) 160 18,929 Chain (1) FUNCTION: Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Membrane, clathrin-coated pit {ECO:0000250}. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex. {ECO:0000250}. SUBUNIT: Adaptor protein complex 1 (AP-1) is a heterotetramer composed of two large adaptins (gamma-type subunit AP1G1 and beta-type subunit AP1B1), a medium adaptin (mu-type subunit AP1M1 or AP1M2) and a small adaptin (sigma-type subunit AP1S1 or AP1S2 or AP1S3). Binds to MUC1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. +Q75UR0 ANO5_MOUSE Anoctamin-5 (Gnathodiaphyseal dysplasia 1 protein homolog) (Transmembrane protein 16E) 904 106,214 Alternative sequence (6); Chain (1); Compositional bias (1); Glycosylation (6); Topological domain (9); Transmembrane (8) TRANSMEM 291 311 Helical. {ECO:0000255}.; TRANSMEM 372 392 Helical. {ECO:0000255}.; TRANSMEM 454 474 Helical. {ECO:0000255}.; TRANSMEM 503 523 Helical. {ECO:0000255}.; TRANSMEM 549 569 Helical. {ECO:0000255}.; TRANSMEM 668 688 Helical. {ECO:0000255}.; TRANSMEM 724 744 Helical. {ECO:0000255}.; TRANSMEM 826 846 Helical. {ECO:0000255}. TOPO_DOM 1 290 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 312 371 Extracellular. {ECO:0000255}.; TOPO_DOM 393 453 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 475 502 Extracellular. {ECO:0000255}.; TOPO_DOM 524 548 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 570 667 Extracellular. {ECO:0000255}.; TOPO_DOM 689 723 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 745 825 Extracellular. {ECO:0000255}.; TOPO_DOM 847 904 Cytoplasmic. {ECO:0000255}. FUNCTION: Does not exhibit calcium-activated chloride channel (CaCC) activity. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:17418107}; Multi-pass membrane protein {ECO:0000269|PubMed:17418107}. Cell membrane {ECO:0000269|PubMed:17418107}; Multi-pass membrane protein {ECO:0000255}. Note=Colocalized with CALR/calreticulin. Shows an intracellular localization. {ECO:0000250|UniProtKB:Q75V66}. TISSUE SPECIFICITY: Highly expressed in skeletal muscle, bone tissues and thyroid gland. {ECO:0000269|PubMed:15124103, ECO:0000269|PubMed:15882990, ECO:0000269|PubMed:17418107, ECO:0000269|PubMed:20056604}. +Q9DAX9 APBP2_MOUSE Amyloid protein-binding protein 2 (Amyloid beta precursor protein-binding protein 2) (APP-BP2) 585 66,855 Chain (1); Repeat (8) FUNCTION: May play a role in intracellular protein transport. May be involved in the translocation of APP along microtubules toward the cell surface (By similarity). {ECO:0000250}. PTM: Rapidly degraded by the proteasome upon overexpression of a C-terminal fragment of APP. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=Associated with membranes and microtubules. {ECO:0000250}. SUBUNIT: Binds APP. {ECO:0000250}. +P09813 APOA2_MOUSE Apolipoprotein A-II (Apo-AII) (ApoA-II) (Apolipoprotein A2) [Cleaved into: Proapolipoprotein A-II (ProapoA-II)] 102 11,309 Chain (2); Mass spectrometry (7); Modified residue (1); Natural variant (1); Sequence conflict (12); Signal peptide (1) FUNCTION: May stabilize HDL (high density lipoprotein) structure by its association with lipids, and affect the HDL metabolism. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02652}. SUBUNIT: Monomer. Interacts with APOA1BP and NDRG1 (By similarity). {ECO:0000250|UniProtKB:P02652}. TISSUE SPECIFICITY: Plasma. DISEASE: Note=Defects in Apoa2 are the cause of senescence accelerated mouse (SAM), the senile amyloid is a mutated apolipoprotein A-II. {ECO:0000269|PubMed:2426658, ECO:0000269|PubMed:2514123}. +Q8C7N7 APH1B_MOUSE Gamma-secretase subunit APH-1B (APH-1b) (Aph-1beta) 257 28,703 Alternative sequence (2); Chain (1); Transmembrane (7) TRANSMEM 5 25 Helical; Name=1. {ECO:0000255}.; TRANSMEM 32 52 Helical; Name=2. {ECO:0000255}.; TRANSMEM 66 86 Helical; Name=3. {ECO:0000255}.; TRANSMEM 115 135 Helical; Name=4. {ECO:0000255}.; TRANSMEM 160 180 Helical; Name=5. {ECO:0000255}.; TRANSMEM 186 206 Helical; Name=6. {ECO:0000255}.; TRANSMEM 213 233 Helical; Name=7. {ECO:0000255}. FUNCTION: Probable subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral proteins such as Notch receptors and APP (amyloid-beta precursor protein). It probably represents a stabilizing cofactor for the presenilin homodimer that promotes the formation of a stable complex. Probably present in a minority of gamma-secretase complexes compared to APH1A (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Probable component of the gamma-secretase complex, a complex composed of a presenilin homodimer (PSEN1 or PSEN2), nicastrin (NCSTN), APH1 (APH1A or APH1B) and PEN2. Such minimal complex is sufficient for secretase activity, although other components may exist (By similarity). Interacts with PSEN1 and PSEN2 (By similarity). {ECO:0000250}. +P62331 ARF6_MOUSE ADP-ribosylation factor 6 175 20,082 Beta strand (6); Chain (1); Helix (6); Initiator methionine (1); Lipidation (1); Mutagenesis (4); Nucleotide binding (5); Turn (2) FUNCTION: GTP-binding protein involved in protein trafficking that regulates endocytic recycling and cytoskeleton remodeling (PubMed:11950392). Required for normal completion of mitotic cytokinesis. Involved in the regulation of dendritic spine development, contributing to the regulation of dendritic branching and filopodia extension. Plays an important role in membrane trafficking, during junctional remodeling and epithelial polarization. Regulates surface levels of adherens junction proteins such as CDH1 (PubMed:29420262, PubMed:20080746). Required for NTRK1 sorting to the recycling pathway from early endosomes (By similarity). {ECO:0000250|UniProtKB:P62332, ECO:0000269|PubMed:11950392, ECO:0000269|PubMed:16325184, ECO:0000269|PubMed:20080746, ECO:0000269|PubMed:22522702, ECO:0000269|PubMed:23572513, ECO:0000269|PubMed:29420262}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P62330}. Cell membrane {ECO:0000269|PubMed:29420262}; Lipid-anchor {ECO:0000250|UniProtKB:P62330}. Endosome membrane; Lipid-anchor {ECO:0000250|UniProtKB:P62330}. Recycling endosome membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Cell projection, filopodium membrane; Lipid-anchor. Cell projection, ruffle {ECO:0000250|UniProtKB:P62330}. Cleavage furrow {ECO:0000250|UniProtKB:P62330}. Midbody, Midbody ring {ECO:0000269|PubMed:22522702}. Early endosome membrane {ECO:0000269|PubMed:11950392}; Lipid-anchor {ECO:0000305}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:11950392}; Lipid-anchor {ECO:0000305}. Note=Distributed uniformly on the plasma membrane, as well as throughout the cytoplasm during metaphase. Subsequently concentrated at patches in the equatorial region at the onset of cytokinesis, and becomes distributed in the equatorial region concurrent with cleavage furrow ingression. In late stages of cytokinesis, concentrates at the midbody ring/Flemming body. Recruitement to the midbody ring requires both activation by PSD/EFA6A and interaction with KIF23/MKLP1. After abscission of the intercellular bridge, incorporated into one of the daughter cells as a midbody remnant and localizes to punctate structures beneath the plasma membrane (PubMed:22522702). Recruited to the cell membrane in association with CYTH2 and ARL4C. Colocalizes with DAB2IP at the plasma membrane and endocytic vesicles. Myristoylation is required for proper localization to membranes (By similarity). {ECO:0000250|UniProtKB:P62330, ECO:0000269|PubMed:22522702}. SUBUNIT: Interacts (when activated) with GGA1, GGA2 and GGA3; the interaction is required for proper subcellular location of GGA1, GGA2 and GGA3 (PubMed:11950392, PubMed:22522702). Interacts with ARHGAP21, ASAP2, HERC1, PIP5K1C and UACA. Interacts with NCS1/FREQ at the plasma membrane. Interacts with RAB11FIP3. Interacts with USP6 (via Rab-GAP TBC domain). Interacts with ECPAS. Interacts with TBC1D24. Interacts with MICALL1. Interacts with CYTH3 (By similarity). Interacts with KIF23, forming heterodimers and heterotetramers. Interacts with SPAG9 and RAB11FIP4 (PubMed:22522702). Interacts with C9orf72 (PubMed:27723745). {ECO:0000250|UniProtKB:P62330, ECO:0000250|UniProtKB:P62332, ECO:0000269|PubMed:11950392, ECO:0000269|PubMed:22522702, ECO:0000269|PubMed:27723745}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:8947846}. +Q3UL36 ARGL1_MOUSE Arginine and glutamate-rich protein 1 271 32,887 Alternative sequence (2); Chain (1); Compositional bias (2); Modified residue (6); Sequence caution (1) +Q8BLD6 ANR55_MOUSE Ankyrin repeat domain-containing protein 55 626 68,524 Chain (1); Modified residue (1); Repeat (9); Sequence conflict (2) +Q6NZB1 ANM6_MOUSE Protein arginine N-methyltransferase 6 (EC 2.1.1.319) (Histone-arginine N-methyltransferase PRMT6) 378 41,866 Active site (2); Beta strand (15); Binding site (5); Chain (1); Domain (1); Erroneous initiation (2); Helix (11); Modified residue (1); Sequence conflict (3); Turn (3) FUNCTION: Arginine methyltransferase that can catalyze the formation of both omega-N monomethylarginine (MMA) and asymmetrical dimethylarginine (aDMA), with a strong preference for the formation of aDMA (PubMed:22904064, PubMed:26070566). Preferentially methylates arginyl residues present in a glycine and arginine-rich domain and displays preference for monomethylated substrates (By similarity). Specifically mediates the asymmetric dimethylation of histone H3 'Arg-2' to form H3R2me2a (By similarity). H3R2me2a represents a specific tag for epigenetic transcriptional repression and is mutually exclusive with methylation on histone H3 'Lys-4' (H3K4me2 and H3K4me3) (By similarity). Acts as a transcriptional repressor of various genes such as HOXA2, THBS1 and TP53 (PubMed:22904064). Repression of TP53 blocks cellular senescence (PubMed:22904064). Also methylates histone H2A and H4 'Arg-3' (H2AR3me and H4R3me, respectively). Acts as a regulator of DNA base excision during DNA repair by mediating the methylation of DNA polymerase beta (POLB), leading to the stimulation of its polymerase activity by enhancing DNA binding and processivity. Methylates HMGA1. Regulates alternative splicing events. Acts as a transcriptional coactivator of a number of steroid hormone receptors including ESR1, ESR2, PGR and NR3C1. Promotes fasting-induced transcriptional activation of the gluconeogenic program through methylation of the CRTC2 transcription coactivator (PubMed:24570487). Methylates GPS2, protecting GPS2 from ubiquitination and degradation (PubMed:26070566). {ECO:0000250|UniProtKB:Q96LA8, ECO:0000269|PubMed:22904064, ECO:0000269|PubMed:24570487, ECO:0000269|PubMed:26070566}. PTM: Automethylation enhances its stability. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96LA8}. SUBUNIT: Interacts with (and methylates) HIV-1 Tat, Rev and Nucleocapsid protein p7 (NC). Interacts with EPB41L3 and NCOA1. {ECO:0000250|UniProtKB:Q96LA8}. +Q9QXJ1 APBB1_MOUSE Amyloid-beta A4 precursor protein-binding family B member 1 (Protein Fe65) 710 77,384 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (3); Modified residue (4); Mutagenesis (2); Sequence conflict (5) FUNCTION: Adapter protein that forms a transcriptionally active complex with the gamma-secretase-derived amyloid precursor protein (APP) intracellular domain. Plays a central role in the response to DNA damage by translocating to the nucleus and inducing apoptosis. May act by specifically recognizing and binding histone H2AX phosphorylated on 'Tyr-142' (H2AXY142ph) at double-strand breaks (DSBs), recruiting other pro-apoptosis factors such as MAPK8/JNK1. Required for histone H4 acetylation at double-strand breaks (DSBs). Its ability to specifically bind modified histones and chromatin modifying enzymes such as KAT5/TIP60, probably explains its transcription activation activity. Function in association with TSHZ3, SET and HDAC factors as a transcriptional repressor, that inhibits the expression of CASP4. Associates with chromatin in a region surrounding the CASP4 transcriptional start site(s). {ECO:0000269|PubMed:17121854, ECO:0000269|PubMed:25342469}. PTM: Polyubiquitination by RNF157 leads to degradation by the proteasome (PubMed:25342469). {ECO:0000269|PubMed:25342469}.; PTM: Phosphorylated following nuclear translocation. Phosphorylation at Tyr-546 enhances the transcription activation activity and reduces the affinity with RASD1/DEXRAS1. Phosphorylation at Ser-610 by SGK1 promotes its localization to the nucleus (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17121854}. Cytoplasm {ECO:0000269|PubMed:17121854}. Nucleus {ECO:0000269|PubMed:17121854}. Cell projection, growth cone {ECO:0000250}. Nucleus speckle {ECO:0000250}. Note=Colocalizes with TSHZ3 in the nucleus and in axonal growth cone. Colocalizes with NEK6 at the nuclear speckles (By similarity). In normal conditions, it mainly localizes to the cytoplasm, while a small fraction is tethered to the cell membrane via its interaction with APP. Following exposure to DNA damaging agents, it is released from cell membrane and translocates to the nucleus. Nuclear translocation is under the regulation of APP. Phosphorylation at Ser-610 by SGK1 promotes its localization to the nucleus (By similarity). {ECO:0000250}. SUBUNIT: Interacts with SET. Found in a trimeric complex with HDAC1 and TSHZ3; the interaction between HDAC1 and APBB1 is mediated by TSHZ3 (By similarity). Component of a complex, at least composed of APBB1, RASD1/DEXRAS1 and APP. Interacts (via PID domain 2) with APP (with the intracellular domain of the amyloid-beta precursor protein). Interacts (via PID domain 2) with RASD1/DEXRAS1; impairs the transcription activation activity. Interacts (via PID domain 1) with KAT5/TIP60. Interacts (via the WW domain) with histone H2AX (when phosphorylated on 'Tyr-142'). Interacts with MAPK8 (By similarity). Interacts (via the WW domain) with proline-rich regions of APBB1IP and ENAH. Interacts (via PID domain 1) with TSHZ3 (via homeobox domain). Interacts with TSHZ1 and TSHZ2. Interacts (via WWW domain) with NEK6. Interacts (via WWW domain) with ABL1 (By similarity). Interacts with RNF157 (PubMed:25342469). {ECO:0000250|UniProtKB:O00213, ECO:0000269|PubMed:25342469}. +Q9R0R4 APEL_MOUSE Apelin (APJ endogenous ligand) [Cleaved into: Apelin-36; Apelin-31; Apelin-28; Apelin-13] 77 8,658 Peptide (4); Propeptide (1); Signal peptide (1) FUNCTION: Endogenous ligand for the apelin receptor (APLNR). Drives internalization of APLNR (By similarity). Apelin-36 dissociates more hardly than (pyroglu)apelin-13 from APLNR (By similarity). Hormone involved in the regulation of cardiac precursor cell movements during gastrulation and heart morphogenesis (By similarity). Has an inhibitory effect on cytokine production in response to T-cell receptor/CD3 cross-linking; the oral intake of apelin in the colostrum and the milk might therefore modulate immune responses in neonates (PubMed:10525157). Plays a role in early coronary blood vessels formation (PubMed:28890073). Mediates myocardial contractility in an ERK1/2-dependent manner (By similarity). May also have a role in the central control of body fluid homeostasis by influencing vasopressin release and drinking behavior (PubMed:11359874). {ECO:0000250|UniProtKB:Q4TTN8, ECO:0000250|UniProtKB:Q9R0R3, ECO:0000269|PubMed:10525157, ECO:0000269|PubMed:11359874, ECO:0000269|PubMed:28890073}. PTM: Several active peptides may be produced by proteolytic processing of the peptide precursor. {ECO:0000250|UniProtKB:Q9TUI9}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9TUI9}. Secreted, extracellular space {ECO:0000250|UniProtKB:Q9TUI9}. Note=Abundantly secreted in the colostrum. Lower level in milk. Decreases rapidly within several days after parturition in milk, but is still detectable even in commercial milk. {ECO:0000250|UniProtKB:Q9TUI9}. TISSUE SPECIFICITY: Expressed in extraembryonic visceral endoderm and in the primitive streak at 6.5 and 7.5 dpc (PubMed:28854362). Expressed in the anterior visceral yolk sac at 8.25 dpc (PubMed:28854362). Expressed weakly in the embryonic heart at 11.5 dpc (PubMed:26611206). Expressed in the adult heart (PubMed:26611206). Expressed in endothelial cells and cardiomyocytes and weakly expressed in fibroblasts (PubMed:26611206). {ECO:0000269|PubMed:26611206, ECO:0000269|PubMed:28854362}. +Q569N2 ANR37_MOUSE Ankyrin repeat domain-containing protein 37 159 17,262 Chain (1); Repeat (3) SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. +Q9JKW0 AR6P1_MOUSE ADP-ribosylation factor-like protein 6-interacting protein 1 (ARL-6-interacting protein 1) (Aip-1) (Protein TBX2) 203 23,437 Chain (1); Erroneous initiation (1); Frameshift (1); Topological domain (4); Transmembrane (3) TRANSMEM 42 62 Helical. {ECO:0000255}.; TRANSMEM 66 86 Helical. {ECO:0000255}.; TRANSMEM 134 175 Helical. {ECO:0000255}. TOPO_DOM 1 41 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 63 65 Lumenal. {ECO:0000255}.; TOPO_DOM 87 133 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 176 203 Lumenal. {ECO:0000255}. FUNCTION: Positively regulates SLC1A1/EAAC1-mediated glutamate transport by increasing its affinity for glutamate in a PKC activity-dependent manner. Promotes the catalytic efficiency of SLC1A1/EAAC1 probably by reducing its interaction with ARL6IP5, a negative regulator of SLC1A1/EAAC1-mediated glutamate transport (PubMed:18684713). Plays a role in the formation and stabilization of endoplasmic reticulum tubules. Negatively regulates apoptosis, possibly by modulating the activity of caspase-9 (CASP9). Inhibits cleavage of CASP9-dependent substrates and downstream markers of apoptosis but not CASP9 itself. May be involved in protein transport, membrane trafficking, or cell signaling during hematopoietic maturation (By similarity). {ECO:0000250|UniProtKB:Q15041, ECO:0000269|PubMed:18684713}. SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250|UniProtKB:Q15041}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q15041}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum {ECO:0000269|PubMed:18684713}. Note=Predominantly localized to intracytoplasmic membranes. Preferentially localizes at the ER tubules and the edge of the ER sheets, both of which are characterized by a high membrane curvature. {ECO:0000250|UniProtKB:Q15041}. SUBUNIT: Homooligomer (By similarity). Heterodimer with ARL6IP5 (PubMed:18684713). Interacts with ARL6 (PubMed:10508919). Interacts with TMEM33. Interacts with ATL1 (By similarity). {ECO:0000250|UniProtKB:Q15041, ECO:0000269|PubMed:10508919, ECO:0000269|PubMed:18684713}. DOMAIN: The transmembrane domains are required for its ability to shape the endoplasmic reticulum membrane into tubules. {ECO:0000250|UniProtKB:Q15041}. TISSUE SPECIFICITY: Expressed in the cerebral cortex, cerebellum, hippocampus, olfactory bulbs, medulla oblongate and limbic system (at protein level). Ubiquitous (PubMed:18684713). Expressed in all hematopoietic cell lineages, with highest levels in early myeloid progenitor cells. {ECO:0000269|PubMed:10995579, ECO:0000269|PubMed:18684713}. +Q8BH07 AR6P6_MOUSE ADP-ribosylation factor-like protein 6-interacting protein 6 (ARL-6-interacting protein 6) (Aip-6) 226 24,909 Chain (1); Frameshift (1); Modified residue (5); Sequence caution (1); Sequence conflict (6); Transmembrane (3) TRANSMEM 111 131 Helical. {ECO:0000255}.; TRANSMEM 150 170 Helical. {ECO:0000255}.; TRANSMEM 205 225 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9WV32 ARC1B_MOUSE Actin-related protein 2/3 complex subunit 1B (Arp2/3 complex 41 kDa subunit) (p41-ARC) 372 41,064 Chain (1); Repeat (6); Sequence conflict (1) FUNCTION: Component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility. In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA. The Arp2/3 complex promotes homologous recombination (HR) repair in response to DNA damage by promoting nuclear actin polymerization, leading to drive motility of double-strand breaks (DSBs). {ECO:0000250|UniProtKB:O15143}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O15143}. Nucleus {ECO:0000250|UniProtKB:O15143}. SUBUNIT: Component of the Arp2/3 complex composed of ACTR2/ARP2, ACTR3/ARP3, ARPC1B/p41-ARC, ARPC2/p34-ARC, ARPC3/p21-ARC, ARPC4/p20-ARC and ARPC5/p16-ARC. {ECO:0000250|UniProtKB:O15143}. +Q8CHG5 AREL1_MOUSE Apoptosis-resistant E3 ubiquitin protein ligase 1 (EC 2.3.2.26) (Apoptosis-resistant HECT-type E3 ubiquitin transferase 1) 823 94,199 Active site (1); Chain (1); Domain (1); Erroneous initiation (1); Repeat (1); Sequence conflict (1) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Inhibits apoptosis by ubiquitinating and targeting for degradation a number of proapoptotic proteins including DIABLO/SMAC, HTRA2 and SEPT4/ARTS which are released from the mitochondrion into the cytosol following apoptotic stimulation. {ECO:0000250|UniProtKB:O15033}. PTM: Autoubiquitinated in vitro in the presence of E2 enzyme UBE2D1/UBCH5A. {ECO:0000250|UniProtKB:O15033}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:O15033}. TISSUE SPECIFICITY: Detected in brain, testis, heart, liver, lung and kidney with very low levels in skeletal muscle and spleen. {ECO:0000269|PubMed:23479728}. +Q8BXL7 ARFRP_MOUSE ADP-ribosylation factor-related protein 1 (ARF-related protein 1) 201 22,659 Chain (1); Modified residue (1); Nucleotide binding (3); Sequence conflict (1) FUNCTION: Trans-Golgi-associated GTPase that regulates protein sorting. Controls the targeting of ARL1 and its effector to the trans-Golgi. Required for the lipidation of chylomicrons in the intestine and required for VLDL lipidation in the liver. {ECO:0000269|PubMed:22505585, ECO:0000269|PubMed:23033902, ECO:0000269|PubMed:24186947}. SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:17127620}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:17127620}. Note=Located in the trans-Golgi in the GTP-bound active state. {ECO:0000269|PubMed:17127620}. SUBUNIT: Interacts with SYS1. {ECO:0000250|UniProtKB:Q13795}. +P84084 ARF5_MOUSE ADP-ribosylation factor 5 180 20,530 Chain (1); Initiator methionine (1); Lipidation (1); Nucleotide binding (3) FUNCTION: GTP-binding protein involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus. {ECO:0000269|PubMed:11950392}. SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P84085}. Membrane {ECO:0000250|UniProtKB:P84085}; Lipid-anchor {ECO:0000250|UniProtKB:P84085}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:11950392}; Lipid-anchor {ECO:0000305}. SUBUNIT: Interacts (when activated) with GGA1, GGA2 and GGA3; the interaction is required for proper subcellular location of GGA1, GGA2 and GGA3 (PubMed:11950392). Binds ASAP2 (By similarity). Interacts with NCS1/FREQ at the Golgi complex. Interacts with RAB11FIP3 and RAB11FIP4 (By similarity). {ECO:0000250|UniProtKB:P84085, ECO:0000269|PubMed:11950392}. TISSUE SPECIFICITY: Ubiquitous. +P63277 AMELX_MOUSE Amelogenin, X isoform (Leucine-rich amelogenin peptide) (LRAP) 210 23,483 Alternative sequence (3); Chain (1); Modified residue (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Plays a role in the biomineralization of teeth. Seems to regulate the formation of crystallites during the secretory stage of tooth enamel development. Thought to play a major role in the structural organization and mineralization of developing enamel. PTM: Several forms are produced by C-terminal processing.; PTM: Phosphorylated by FAM20C in vitro. {ECO:0000250|UniProtKB:Q99217}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. +Q8BXQ6 AMPO_MOUSE Aminopeptidase O (AP-O) (EC 3.4.11.-) 817 92,955 Active site (1); Alternative sequence (6); Chain (1); Erroneous initiation (1); Metal binding (3); Site (1) FUNCTION: Aminopeptidases catalyze the hydrolysis of amino acid residues from the N-terminus of peptide or protein substrates. Able to cleave angiotensin III to generate angiotensin IV, a bioactive peptide of the renin-angiotensin pathway. Not able to cleave angiotensin I and angiotensin II. May play a role in the proteolytic processing of bioactive peptides in tissues such as testis and heart (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:15687497}. +Q3TYQ9 AOXD_MOUSE Aldehyde oxidase 4 (EC 1.2.3.1) (Aldehyde oxidase homolog 2) (Azaheterocycle hydroxylase 4) (EC 1.17.3.-) (Retinal oxidase) 1336 148,279 Active site (1); Binding site (10); Chain (1); Domain (2); Metal binding (8); Nucleotide binding (1); Region (2); Sequence conflict (1) FUNCTION: Aldehyde oxidase able to catalyze the oxidation of retinaldehyde into retinoate. Is responsible for the major all-trans-retinaldehyde-metabolizing activity in the Harderian gland, and contributes a significant amount of the same activity in the skin. Is devoid of pyridoxal-oxidizing activity, in contrast to the other aldehyde oxidases. Acts as a negative modulator of the epidermal trophism. May be able to oxidize a wide variety of aldehydes into their corresponding carboxylates and to hydroxylate azaheterocycles. {ECO:0000269|PubMed:18981221}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18981221}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:G3X982}. TISSUE SPECIFICITY: Highly expressed in Harderian glands and sebaceous glands with detectable levels in the epidermis and other keratinized epithelia (at protein level). Detected in testis. The expression is 3 times greater in females than in males. {ECO:0000269|PubMed:18981221, ECO:0000269|PubMed:23263164}. +Q8BHY3 ANO1_MOUSE Anoctamin-1 (Transmembrane protein 16A) 960 110,916 Alternative sequence (1); Chain (1); Erroneous initiation (3); Erroneous translation (1); Glycosylation (1); Modified residue (1); Mutagenesis (7); Topological domain (9); Transmembrane (8) TRANSMEM 334 354 Helical. {ECO:0000255}.; TRANSMEM 403 423 Helical. {ECO:0000255}.; TRANSMEM 494 514 Helical. {ECO:0000255}.; TRANSMEM 540 560 Helical. {ECO:0000255}.; TRANSMEM 582 602 Helical. {ECO:0000255}.; TRANSMEM 706 726 Helical. {ECO:0000255}.; TRANSMEM 766 786 Helical. {ECO:0000255}.; TRANSMEM 857 877 Helical. {ECO:0000255}. TOPO_DOM 1 333 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 355 402 Extracellular. {ECO:0000255}.; TOPO_DOM 424 493 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 515 539 Extracellular. {ECO:0000255}.; TOPO_DOM 561 581 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 603 705 Extracellular. {ECO:0000255}.; TOPO_DOM 727 765 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 787 856 Extracellular. {ECO:0000255}.; TOPO_DOM 878 960 Cytoplasmic. {ECO:0000255}. FUNCTION: Calcium-activated chloride channel (CaCC) which plays an important role in transepithelial anion transport and smooth muscle contraction. Required for the normal functioning of the interstitial cells of Cajal (ICCs) which generate electrical pacemaker activity in gastrointestinal smooth muscles. Acts as a major contributor to basal and stimulated chloride conductance in airway epithelial cells and plays an important role in tracheal cartilage development. {ECO:0000269|PubMed:18585372, ECO:0000269|PubMed:18724360, ECO:0000269|PubMed:21908539, ECO:0000269|PubMed:22002868, ECO:0000269|PubMed:22075693}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18585372, ECO:0000269|PubMed:22075693}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:Q5XXA6}. Note=Cytoplasmic localization seen in neoplastic cells of head and neck squamous cell carcinoma (HNSCC) tumors. {ECO:0000250|UniProtKB:Q5XXA6}. SUBUNIT: Homodimer. Interacts with CFTR (By similarity). Interacts with TRPV4 (PubMed:24509911). {ECO:0000250|UniProtKB:Q5XXA6, ECO:0000269|PubMed:24509911}. DOMAIN: The region spanning the fifth and sixth transmembrane domains probably forms the pore-forming region. TISSUE SPECIFICITY: Highly expressed in pulmonary bronchiole epithelial cells, pancreatic and submandibular gland acinar cells, kidney proximal tubule, all retinal cell layers, most sensory cells of dorsal root ganglia, Leydig cells and spermatocytes (at protein level). Expressed at high levels in the thyroid gland and gastrointestinal muscles. {ECO:0000269|PubMed:18585372, ECO:0000269|PubMed:18724360, ECO:0000269|PubMed:20056604}. +Q9JKC8 AP3M1_MOUSE AP-3 complex subunit mu-1 (AP-3 adaptor complex mu3A subunit) (Adaptor-related protein complex 3 subunit mu-1) (Mu-adaptin 3A) (Mu3A-adaptin) 418 46,936 Chain (1); Domain (1) FUNCTION: Part of the AP-3 complex, an adaptor-related complex which is not clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to lysosomes. In concert with the BLOC-1 complex, AP-3 is required to target cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. {ECO:0000269|PubMed:21998198}. SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex. {ECO:0000250}. SUBUNIT: Adaptor protein complex 3 (AP-3) is a heterotetramer composed of two large adaptins (delta-type subunit AP3D1 and beta-type subunit AP3B1 or AP3B2), a medium adaptin (mu-type subunit AP3M1 or AP3M2) and a small adaptin (sigma-type subunit APS1 or AP3S2). Interacts with AGAP1. AP-3 associates with the BLOC-1 complex. {ECO:0000269|PubMed:12967569}. +Q5SGK3 AOXB_MOUSE Aldehyde oxidase 2 (EC 1.2.3.1) (Aldehyde oxidase homolog 3) (Azaheterocycle hydroxylase 2) (EC 1.17.3.-) 1345 147,913 Active site (1); Binding site (9); Chain (1); Domain (2); Metal binding (8); Nucleotide binding (1); Region (2); Sequence conflict (1) FUNCTION: Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as phthalazine, as well as aldehydes, such as benzaldehyde and retinal. Cannot use hypoxanthine as substrate. {ECO:0000269|PubMed:15383531}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15383531}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O54754}. TISSUE SPECIFICITY: Expressed in olfactory mucosa epithelium (at protein level). Detected in skin. {ECO:0000269|PubMed:15383531, ECO:0000269|PubMed:23263164}. +Q8BTZ4 APC5_MOUSE Anaphase-promoting complex subunit 5 (APC5) (Cyclosome subunit 5) 740 83,098 Alternative sequence (1); Chain (1); Frameshift (1); Modified residue (2); Repeat (13); Sequence conflict (10) Protein modification; protein ubiquitination. FUNCTION: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By similarity). {ECO:0000250}. SUBUNIT: The mammalian APC/C is composed at least of 14 distinct subunits ANAPC1, ANAPC2, CDC27/APC3, ANAPC4, ANAPC5, CDC16/APC6, ANAPC7, CDC23/APC8, ANAPC10, ANAPC11, CDC26/APC12, ANAPC13, ANAPC15 and ANAPC16 that assemble into a complex of at least 19 chains with a combined molecular mass of around 1.2 MDa; APC/C interacts with FZR1 and FBXO5. {ECO:0000250|UniProtKB:Q9UJX4}. +Q9WVM3 APC7_MOUSE Anaphase-promoting complex subunit 7 (APC7) (Cyclosome subunit 7) (Prediabetic NOD sera-reactive autoantigen) 565 63,021 Chain (1); Modified residue (1); Repeat (10); Sequence conflict (4) Protein modification; protein ubiquitination. FUNCTION: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By similarity). {ECO:0000250}. SUBUNIT: V-shaped homodimer. The mammalian APC/C is composed at least of 14 distinct subunits ANAPC1, ANAPC2, CDC27/APC3, ANAPC4, ANAPC5, CDC16/APC6, ANAPC7, CDC23/APC8, ANAPC10, ANAPC11, CDC26/APC12, ANAPC13, ANAPC15 and ANAPC16 that assemble into a complex of at least 19 chains with a combined molecular mass of around 1.2 MDa; APC/C interacts with FZR1 and FBXO5. {ECO:0000250|UniProtKB:Q9UJX3}. +P17426 AP2A1_MOUSE AP-2 complex subunit alpha-1 (100 kDa coated vesicle protein A) (Adaptor protein complex AP-2 subunit alpha-1) (Adaptor-related protein complex 2 subunit alpha-1) (Alpha-adaptin A) (Alpha1-adaptin) (Clathrin assembly protein complex 2 alpha-A large chain) (Plasma membrane adaptor HA2/AP2 adaptin alpha A subunit) 977 107,664 Alternative sequence (1); Chain (1); Modified residue (4) FUNCTION: Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. The AP-2 alpha subunit binds polyphosphoinositide-containing lipids, positioning AP-2 on the membrane. The AP-2 alpha subunit acts via its C-terminal appendage domain as a scaffolding platform for endocytic accessory proteins. The AP-2 alpha and AP-2 sigma subunits are thought to contribute to the recognition of the [ED]-X-X-X-L-[LI] motif (By similarity). {ECO:0000250, ECO:0000269|PubMed:14745134, ECO:0000269|PubMed:15473838}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Membrane, coated pit {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=AP-2 appears to be excluded from internalizing CCVs and to disengage from sites of endocytosis seconds before internalization of the nascent CCV. {ECO:0000250}. SUBUNIT: Adaptor protein complex 2 (AP-2) is a heterotetramer composed of two large adaptins (alpha-type subunit AP2A1 or AP2A2 and beta-type subunit AP2B1), a medium adaptin (mu-type subunit AP2M1) and a small adaptin (sigma-type subunit AP2S1). Interacts with HIP1 and RAB11FIP2 (By similarity). Interacts with SLC12A5 (PubMed:18625303). Interacts with clathrin (PubMed:7559550). Interacts with SGIP1 (PubMed:17626015). Interacts with RFTN1 (By similarity). Interacts with KIAA1107 (PubMed:29262337). {ECO:0000250|UniProtKB:O95782, ECO:0000269|PubMed:17626015, ECO:0000269|PubMed:18625303, ECO:0000269|PubMed:29262337, ECO:0000269|PubMed:7559550}. TISSUE SPECIFICITY: Isoform A is expressed only in neuronal tissue and skeletal muscle. Isoform B is widely expressed. +Q02013 AQP1_MOUSE Aquaporin-1 (AQP-1) (Aquaporin-CHIP) (Delayed early response protein 2) (DER2) (Water channel protein for red blood cells and kidney proximal tubule) 269 28,793 Chain (1); Compositional bias (1); Glycosylation (1); Intramembrane (4); Modified residue (3); Motif (2); Sequence conflict (1); Site (4); Topological domain (9); Transmembrane (6) INTRAMEM 71 76 {ECO:0000250}.; INTRAMEM 77 84 Helical; Name=Helix B. {ECO:0000250}.; INTRAMEM 187 192 {ECO:0000250}.; INTRAMEM 193 200 Helical; Name=Helix E. {ECO:0000250}. TRANSMEM 8 36 Helical; Name=Helix 1. {ECO:0000250}.; TRANSMEM 49 66 Helical; Name=Helix 2. {ECO:0000250}.; TRANSMEM 95 115 Helical; Name=Helix 3. {ECO:0000250}.; TRANSMEM 137 155 Helical; Name=Helix 4. {ECO:0000250}.; TRANSMEM 167 183 Helical; Name=Helix 5. {ECO:0000250}.; TRANSMEM 208 228 Helical; Name=Helix 6. {ECO:0000250}. TOPO_DOM 1 7 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 37 48 Extracellular. {ECO:0000250}.; TOPO_DOM 67 70 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 85 94 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 116 136 Extracellular. {ECO:0000250}.; TOPO_DOM 156 166 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 184 186 Extracellular. {ECO:0000250}.; TOPO_DOM 201 207 Extracellular. {ECO:0000250}.; TOPO_DOM 229 269 Cytoplasmic. {ECO:0000250}. FUNCTION: Forms a water-specific channel that provides the plasma membranes of red cells and kidney proximal tubules with high permeability to water, thereby permitting water to move in the direction of an osmotic gradient. {ECO:0000269|PubMed:12133842}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12133842}; Multi-pass membrane protein {ECO:0000269|PubMed:12133842}. SUBUNIT: Homotetramer. Identified in a complex with STOM (By similarity). Interacts with EPHB2; involved in endolymph production in the inner ear. {ECO:0000250, ECO:0000269|PubMed:10839360}. DOMAIN: Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA). TISSUE SPECIFICITY: Detected in erythrocytes (at protein level). Erythrocytes and renal tubules. {ECO:0000269|PubMed:12133842}. +Q9R0Q6 ARC1A_MOUSE Actin-related protein 2/3 complex subunit 1A (SOP2-like protein) (Sid 329) 370 41,626 Chain (1); Repeat (6) FUNCTION: Probably functions as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks (By similarity). In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA (By similarity). {ECO:0000250|UniProtKB:Q8AVT9, ECO:0000250|UniProtKB:Q92747}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q92747}. Nucleus {ECO:0000250|UniProtKB:Q8AVT9}. SUBUNIT: Probable component of the Arp2/3 complex in which it may replace ARPC1B. {ECO:0000250|UniProtKB:Q92747}. +Q9WV31 ARC_MOUSE Activity-regulated cytoskeleton-associated protein (mArc) (Activity-regulated gene 3.1 protein) (ARC/ARG3.1) (Arg3.1) 396 45,321 Chain (1); Coiled coil (1); Mutagenesis (1); Region (2) FUNCTION: Master regulator of synaptic plasticity that self-assembles into virion-like capsids that encapsulate RNAs and mediate intercellular RNA transfer in the nervous system (By similarity). ARC protein is released from neurons in extracellular vesicles that mediate the transfer of ARC mRNA into new target cells, where ARC mRNA can undergo activity-dependent translation (By similarity). ARC capsids are endocytosed and are able to transfer ARC mRNA into the cytoplasm of neurons (By similarity). Acts as a key regulator of synaptic plasticity: required for protein synthesis-dependent forms of long-term potentiation (LTP) and depression (LTD) and for the formation of long-term memory (PubMed:29264923, PubMed:24094104). Regulates synaptic plasticity by promoting endocytosis of AMPA receptors (AMPARs) in response to synaptic activity: this endocytic pathway maintains levels of surface AMPARs in response to chronic changes in neuronal activity through synaptic scaling, thereby contributing to neuronal homeostasis (PubMed:17088213, PubMed:20211139, PubMed:20228806). Acts as a postsynaptic mediator of activity-dependent synapse elimination in the developing cerebellum by mediating elimination of surplus climbing fiber synapses (PubMed:23791196). Accumulates at weaker synapses, probably to prevent their undesired enhancement (By similarity). This suggests that ARC-containing virion-like capsids may be required to eliminate synaptic material (By similarity). Required to transduce experience into long-lasting changes in visual cortex plasticity and for long-term memory (PubMed:17088210, PubMed:20228806). Involved in postsynaptic trafficking and processing of amyloid-beta A4 (APP) via interaction with PSEN1 (PubMed:22036569). In addition to its role in synapses, also involved in the regulation of the immune system: specifically expressed in skin-migratory dendritic cells and regulates fast dendritic cell migration, thereby regulating T-cell activation (PubMed:28783680). {ECO:0000250|UniProtKB:Q63053, ECO:0000269|PubMed:17088210, ECO:0000269|PubMed:17088213, ECO:0000269|PubMed:20211139, ECO:0000269|PubMed:20228806, ECO:0000269|PubMed:22036569, ECO:0000269|PubMed:24094104, ECO:0000269|PubMed:28783680, ECO:0000269|PubMed:29264923}. PTM: Ubiquitinated by UBE3A, leading to its degradation by the proteasome, thereby promoting AMPA receptors (AMPARs) expression at synapses. {ECO:0000269|PubMed:20211139}.; PTM: Palmitoylation anchors the protein into the membrane by allowing direct insertion into the hydrophobic core of the lipid bilayer. {ECO:0000305|PubMed:29264923}. SUBCELLULAR LOCATION: Extracellular vesicle membrane {ECO:0000250|UniProtKB:Q63053}; Lipid-anchor {ECO:0000269|PubMed:29264923}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000269|PubMed:22036569}; Lipid-anchor {ECO:0000269|PubMed:29264923}. Cell junction, synapse {ECO:0000250|UniProtKB:Q63053}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250|UniProtKB:Q63053}. Early endosome membrane {ECO:0000250|UniProtKB:Q63053}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q63053}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q63053}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q63053}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:Q63053}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:12493697}. Note=Forms virion-like extracellular vesicles that are released from neurons (By similarity). Enriched in postsynaptic density of dendritic spines (By similarity). Targeted to inactive synapses following interaction with CAMK2B in the kinase inactive state (By similarity). Accumulation at weaker synapses may be required to prevent their undesired enhancement (By similarity). Associated with the cell cortex of neuronal soma and dendrites (By similarity). Associated with the sperm tail (PubMed:12493697). {ECO:0000250|UniProtKB:Q63053, ECO:0000269|PubMed:12493697}. SUBUNIT: Homooligomer; homooligomerizes into virion-like capsids (By similarity). Interacts with SH3GL1/endophilin-2, SH3GL3/endophilin-3 and DNM2/DYN2 (By similarity). Interacts with CAMK2B (in the kinase inactive state); leading to target ARC to inactive synapses (By similarity). Interacts with PSEN1 (PubMed:22036569). {ECO:0000250|UniProtKB:Q63053, ECO:0000269|PubMed:22036569}. TISSUE SPECIFICITY: Expressed in brain and testis (PubMed:12493697). In primary visual cortex, detected in all cortical layers with the exception of layer 5: present at highest level in layers 2/3 and 4, the predominant sites of ocular dominance plasticity (at protein level) (PubMed:20228806). Also expressed in skin-migratory dendritic cells (PubMed:28783680). {ECO:0000269|PubMed:12493697, ECO:0000269|PubMed:20228806, ECO:0000269|PubMed:28783680}. +P97822 AN32E_MOUSE Acidic leucine-rich nuclear phosphoprotein 32 family member E (Cerebellar postnatal development protein 1) (LANP-like protein) (LANP-L) 260 29,622 Alternative sequence (2); Chain (1); Compositional bias (1); Cross-link (1); Domain (1); Modified residue (1); Region (1); Repeat (4); Sequence conflict (3) FUNCTION: Histone chaperone that specifically mediates the genome-wide removal of histone H2A.Z/H2AFZ from the nucleosome: removes H2A.Z/H2AFZ from its normal sites of deposition, especially from enhancer and insulator regions. Not involved in deposition of H2A.Z/H2AFZ in the nucleosome. May stabilize the evicted H2A.Z/H2AFZ-H2B dimer, thus shifting the equilibrium towards dissociation and the off-chromatin state (PubMed:24463511). Inhibits activity of protein phosphatase 2A (PP2A). Does not inhibit protein phosphatase 1. May play a role in cerebellar development and synaptogenesis. {ECO:0000269|PubMed:11430900, ECO:0000269|PubMed:14964690, ECO:0000269|PubMed:16420440, ECO:0000269|PubMed:24463511}. PTM: Phosphorylated. The phosphorylation is nuclear localization signal (NLS)-dependent (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. SUBUNIT: Component of a SWR1-like complex, composed of EP400, KAT5/TIP60, TRRAP, BRD8, RUVBL1, RUVBL2, ING3 and ANP32E; the complex does not contain SRCAP. Interacts with H2A.Z/H2AFZ (By similarity). Interacts with the importin alpha KPNA1 and KPNA2. {ECO:0000250, ECO:0000269|PubMed:10692581}. DOMAIN: The H2A.Z-interacting domain (ZID) mediates a direct interaction with H2A.Z/H2AFZ. {ECO:0000250}. TISSUE SPECIFICITY: Expressed at highest levels in cerebellum and spleen. In the cerebellum, expressed mainly in granule cells and, to a lesser extent, in Purkinje cells. {ECO:0000269|PubMed:11430900}. +Q61839 ANFC_MOUSE C-type natriuretic peptide [Cleaved into: CNP-22; CNP-29; CNP-53] 126 13,320 Disulfide bond (1); Peptide (3); Propeptide (1); Signal peptide (1) FUNCTION: Hormone which plays a role in endochondral ossification through regulation of cartilaginous growth plate chondrocytes proliferation and differentiation. May also be vasoactive and natriuretic. Specifically binds and stimulates the cGMP production of the NPR2 receptor. Binds the clearance receptor NPR3. {ECO:0000269|PubMed:11259675, ECO:0000269|PubMed:12890708}. SUBCELLULAR LOCATION: Secreted. +Q8CIG8 ANM5_MOUSE Protein arginine N-methyltransferase 5 (EC 2.1.1.320) (Histone-arginine N-methyltransferase PRMT5) (Jak-binding protein 1) (Shk1 kinase-binding protein 1 homolog) (SKB1 homolog) 637 72,680 Active site (2); Binding site (4); Chain (1); Domain (1); Initiator methionine (1); Modified residue (1); Region (5); Sequence conflict (3); Site (1) FUNCTION: Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA (PubMed:15485929, PubMed:19584108, PubMed:19858291, PubMed:21917714, PubMed:23133559). Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Methylates SUPT5H and may regulate its transcriptional elongation properties. Mono- and dimethylates arginine residues of myelin basic protein (MBP) in vitro. May play a role in cytokine-activated transduction pathways. Negatively regulates cyclin E1 promoter activity and cellular proliferation (By similarity). Methylates histone H2A and H4 'Arg-3' during germ cell development. Methylates histone H3 'Arg-8', which may repress transcription (PubMed:15485929). Methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the interaction with Tudor domain-containing proteins and subsequent localization to the meiotic nuage (PubMed:19584108). Methylates RPS10 (By similarity). Attenuates EGF signaling through the MAPK1/MAPK3 pathway acting at 2 levels. First, monomethylates EGFR; this enhances EGFR 'Tyr-1197' phosphorylation and PTPN6 recruitment, eventually leading to reduced SOS1 phosphorylation. Second, methylates RAF1 and probably BRAF, hence destabilizing these 2 signaling proteins and reducing their catalytic activity (PubMed:21917714). Required for induction of E-selectin and VCAM-1, on the endothelial cells surface at sites of inflammation. Methylates HOXA9. Methylates and regulates SRGAP2 which is involved in cell migration and differentiation (By similarity). Acts as a transcriptional corepressor in CRY1-mediated repression of the core circadian component PER1 by regulating the H4R3 dimethylation at the PER1 promoter (PubMed:23133559). Methylates GM130/GOLGA2, regulating Golgi ribbon formation. Methylates H4R3 in genes involved in glioblastomagenesis in a CHTOP- and/or TET1-dependent manner (By similarity). Symmetrically methylates POLR2A, a modification that allows the recruitment to POLR2A of proteins including SMN1/SMN2 and SETX. This is required for resolving RNA-DNA hybrids created by RNA polymerase II, that form R-loop in transcription terminal regions, an important step in proper transcription termination (By similarity). Along with LYAR, binds the promoter of gamma-globin HBG1/HBG2 and represses its expression (By similarity). Symmetrically methylates NCL (By similarity). {ECO:0000250|UniProtKB:O14744, ECO:0000269|PubMed:15485929, ECO:0000269|PubMed:19584108, ECO:0000269|PubMed:19858291, ECO:0000269|PubMed:21917714, ECO:0000269|PubMed:23133559}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O14744}. Nucleus {ECO:0000269|PubMed:22872859}. Golgi apparatus {ECO:0000250|UniProtKB:O14744}. SUBUNIT: Forms, at least, homodimers and homotetramers. Component of the methylosome complex, composed of PRMT5, WDR77 and CLNS1A (By similarity). Found in a complex composed of PRMT5, WDR77 and RIOK1 (By similarity). RIOK1 and CLNS1A associate with PRMT5 in a mutually exclusive fashion, which allows the recruitment of distinct methylation substrates, such as nucleolin/NCL and Sm proteins, respectively (By similarity). Interacts with PRDM1 (PubMed:16699504). Identified in a complex composed of methylosome and PRMT1 and ERH. Component of a high molecular weight E2F-pocket protein complex, CERC (cyclin E1 repressor complex). Also interacts with Sm proteins, JAK2 and SSTR1. Associates with SWI/SNF remodeling complexes containing SMARCA2 and SMARCA4. Interacts with LSM11, PRMT7 and SNRPD3. Interacts with COPRS; promoting its recruitment on histone H4 (By similarity). Interacts with PRDM1. Interacts with RPS10. Interacts with EGFR; methylates EGFR and stimulates EGFR-mediated ERK activation (By similarity). Interacts with BRAF and with active RAF1 (By similarity). Interacts with HOXA9 (By similarity). Interacts with SRGAP2. Interacts with EPB41L3; this modulates methylation of target proteins (By similarity). Found in a complex with COPRS, RUNX1 and CBFB (PubMed:22193545). Interacts with CHTOP; the interaction symmetrically methylates CHTOP, but seems to require the presence of PRMT1 (PubMed:19858291, PubMed:22872859). Interacts with IWS1 (By similarity). Interacts with CRY1 (PubMed:23133559). Interacts with POLR2A (By similarity). Interacts with SMN1/SMN2 (By similarity). Interacts with LYAR; this interaction is direct (By similarity). {ECO:0000250|UniProtKB:O14744, ECO:0000269|PubMed:16699504, ECO:0000269|PubMed:19858291, ECO:0000269|PubMed:22193545, ECO:0000269|PubMed:22872859, ECO:0000269|PubMed:23133559}. +Q9QZ10 ANX10_MOUSE Annexin A10 (Annexin-10) 324 37,290 Chain (1); Repeat (4); Sequence conflict (4) +Q8K1C0 ANGE2_MOUSE Protein angel homolog 2 544 62,413 Alternative sequence (5); Chain (1) +Q99JG3 ANX13_MOUSE Annexin A13 (Annexin XIII) (Annexin-13) 317 35,922 Chain (1); Initiator methionine (1); Lipidation (1); Repeat (4) SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Note=Associated with the plasma membrane of undifferentiated, proliferating crypt epithelial cells as well as differentiated villus enterocytes. {ECO:0000250}. DOMAIN: A pair of annexin repeats may form one binding site for calcium and phospholipid. +Q9CQM6 ANR61_MOUSE Ankyrin repeat domain-containing protein 61 421 46,588 Alternative sequence (1); Chain (1); Repeat (8) +Q99NH0 ANR17_MOUSE Ankyrin repeat domain-containing protein 17 (Ankyrin repeat domain-containing protein FOE) (Gene trap ankyrin repeat protein) 2603 274,213 Alternative sequence (6); Chain (1); Coiled coil (1); Compositional bias (6); Cross-link (1); Domain (1); Erroneous initiation (1); Modified residue (19); Repeat (25); Sequence caution (1); Sequence conflict (3) FUNCTION: Could play pivotal roles in cell cycle and DNA regulation. Involved in innate immune defense against viruse by positively regulating the viral dsRNA receptors DDX58 and IFIH1 signaling pathways. Involves in NOD2- and NOD1-mediated responses to bacteria suggesting a role in innate antibacterial immune pathways too. Could play a central role for the formation and/or maintenance of the blood vessels of the circulation system (PubMed:19619540). {ECO:0000250|UniProtKB:O75179, ECO:0000269|PubMed:19619540}. PTM: Phosphorylated by CDK2. {ECO:0000250|UniProtKB:O75179}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O75179}. Nucleus {ECO:0000250|UniProtKB:O75179}. Note=Detected around the nucleolus. {ECO:0000250|UniProtKB:O75179}. SUBUNIT: Interacts (via N-terminus) with NOD2. Interacts with CDK2, MCM3, MCM5, MCM7, CDC6 and PCNA. Interacts with MAVS and IFIH1. Interacts (via the second ankyrin repeat cluster) with DDX58. {ECO:0000250|UniProtKB:O75179}. TISSUE SPECIFICITY: Highly expressed in fetal liver. Detected in adult liver cells, ovarian oocytes, seminiferous tubules of the testes and pelvic region of the kidney. It was not detected in heart, gut, lung, spleen and skeletal muscle. Earliest specific in situ marker of hepatic differentiation during embryogenesis, useful for characterization of inductive events involved in hepatic specification. {ECO:0000269|PubMed:11165478, ECO:0000269|PubMed:11740861, ECO:0000269|PubMed:19619540}. +O88879 APAF_MOUSE Apoptotic protease-activating factor 1 (APAF-1) 1249 141,003 Alternative sequence (1); Beta strand (65); Binding site (1); Chain (1); Domain (2); Helix (29); Mutagenesis (1); Nucleotide binding (1); Region (1); Repeat (15); Sequence conflict (3); Turn (16) FUNCTION: Oligomeric Apaf-1 mediates the cytochrome c-dependent autocatalytic activation of pro-caspase-9 (Apaf-3), leading to the activation of caspase-3 and apoptosis. This activation requires ATP (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Monomer. Oligomerizes to a heptameric ring, known as the apoptosome, upon binding of cytochrome c and dATP. Oligomeric Apaf-1 and pro-caspase-9 bind to each other via their respective NH2-terminal CARD domains and consecutively mature caspase-9 is released from the complex (By similarity). Interacts with UACA. It may also interact with Bcl-XL. Interacts with APIP. Interacts (via CARD and NACHT domains) with NAIP/BIRC1 (via NACHT domain) (By similarity). Interacts with CIAO2A (By similarity). {ECO:0000250|UniProtKB:O14727}. DOMAIN: The CARD domain mediates interaction with APIP. {ECO:0000269|PubMed:15262985}.; DOMAIN: The monomeric form is autoinhibited in a closed conformation through a bound ADP at the nucleotide binding site. Exchange of ADP for ATP and binding of cytochrome c trigger a large conformational change where the first WD repeat region swings out, allowing the NB-ARC domain to rotate and expose the contact areas for oligomerization. {ECO:0000269|PubMed:15262985}. TISSUE SPECIFICITY: Highly expressed in lung and spleen, weakly in brain and kidney and not detectable in liver. +A2AHL1 ANO3_MOUSE Anoctamin-3 (Transmembrane protein 16C) 981 114,568 Alternative sequence (2); Chain (1); Glycosylation (4); Topological domain (9); Transmembrane (8) TRANSMEM 404 424 Helical. {ECO:0000255}.; TRANSMEM 470 490 Helical. {ECO:0000255}.; TRANSMEM 551 571 Helical. {ECO:0000255}.; TRANSMEM 593 613 Helical. {ECO:0000255}.; TRANSMEM 641 661 Helical. {ECO:0000255}.; TRANSMEM 762 782 Helical. {ECO:0000255}.; TRANSMEM 811 831 Helical. {ECO:0000255}.; TRANSMEM 915 935 Helical. {ECO:0000255}. TOPO_DOM 1 403 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 425 469 Extracellular. {ECO:0000255}.; TOPO_DOM 491 550 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 572 592 Extracellular. {ECO:0000255}.; TOPO_DOM 614 640 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 662 761 Extracellular. {ECO:0000255}.; TOPO_DOM 783 810 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 832 914 Extracellular. {ECO:0000255}.; TOPO_DOM 936 981 Cytoplasmic. {ECO:0000255}. FUNCTION: Has calcium-dependent phospholipid scramblase activity; scrambles phosphatidylcholine and galactosylceramide. Does not exhibit calcium-activated chloride channel (CaCC) activity. Seems to act as potassium channel regulator and may inhibit pain signaling; can facilitate KCNT1/Slack channel activity by promoting its full single-channel conductance at very low sodium concentrations and by increasing its sodium sensitivity. {ECO:0000269|PubMed:23532839, ECO:0000269|PubMed:23872594}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. Note=Shows an intracellular localization. {ECO:0000250}. SUBUNIT: Interacts with KCNT1/Slack. {ECO:0000269|PubMed:23872594}. TISSUE SPECIFICITY: Predominantly expressed in neuronal tissues. Expressed in brain. {ECO:0000269|PubMed:20056604, ECO:0000269|PubMed:23532839}. +Q91W96 APC4_MOUSE Anaphase-promoting complex subunit 4 (APC4) (Cyclosome subunit 4) 807 91,708 Chain (1); Cross-link (2); Erroneous initiation (1); Modified residue (5) Protein modification; protein ubiquitination. FUNCTION: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By similarity). {ECO:0000250}. SUBUNIT: The mammalian APC/C is composed at least of 14 distinct subunits ANAPC1, ANAPC2, CDC27/APC3, ANAPC4, ANAPC5, CDC16/APC6, ANAPC7, CDC23/APC8, ANAPC10, ANAPC11, CDC26/APC12, ANAPC13, ANAPC15 and ANAPC16 that assemble into a complex of at least 19 chains with a combined molecular mass of around 1.2 MDa; APC/C interacts with FZR1 and FBXO5. In the context of the APC/C complex, directly interacts with UBE2S. {ECO:0000250|UniProtKB:Q9UJX5}. +P07356 ANXA2_MOUSE Annexin A2 (Annexin II) (Annexin-2) (Calpactin I heavy chain) (Calpactin-1 heavy chain) (Chromobindin-8) (Lipocortin II) (Placental anticoagulant protein IV) (PAP-IV) (Protein I) (p36) 339 38,676 Beta strand (2); Chain (1); Cross-link (2); Helix (21); Initiator methionine (1); Modified residue (8); Region (1); Repeat (4); Turn (1) FUNCTION: Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity. May be involved in heat-stress response (By similarity). Inhibits PCSK9-enhanced LDLR degradation, probably reduces PCSK9 protein levels via a translational mechanism but also competes with LDLR for binding with PCSK9 (PubMed:22848640). {ECO:0000250|UniProtKB:P07355, ECO:0000269|PubMed:22848640}. PTM: ISGylated. {ECO:0000269|PubMed:16139798}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane. Melanosome {ECO:0000250}. Note=In the lamina beneath the plasma membrane. SUBUNIT: Heterotetramer containing 2 light chains of S100A10/p11 and 2 heavy chains of ANXA2/p36 (By similarity). Interacts with ATP1B1 (By similarity). Interacts with DYSF (PubMed:14506282). Interacts with COCH. Interacts (via repeat Annexin 1) with PCSK9 (via the C-terminal domain); the interaction inhibits the degradation of LDLR. Interacts with CEACAM1 (via the cytoplasmic domain); this interaction is regulated by phosphorylation of CEACAM1 (By similarity). {ECO:0000250|UniProtKB:A2SW69, ECO:0000250|UniProtKB:P07355, ECO:0000250|UniProtKB:Q6TEQ7, ECO:0000269|PubMed:14506282}. DOMAIN: A pair of annexin repeats may form one binding site for calcium and phospholipid. +Q8K2H6 APC10_MOUSE Anaphase-promoting complex subunit 10 (APC10) (Cyclosome subunit 10) 185 21,266 Chain (1); Domain (1); Initiator methionine (1); Modified residue (2) Protein modification; protein ubiquitination. FUNCTION: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By similarity). {ECO:0000250|UniProtKB:Q9UM13}. SUBUNIT: The mammalian APC/C is composed at least of 14 distinct subunits ANAPC1, ANAPC2, CDC27/APC3, ANAPC4, ANAPC5, CDC16/APC6, ANAPC7, CDC23/APC8, ANAPC10, ANAPC11, CDC26/APC12, ANAPC13, ANAPC15 and ANAPC16 that assemble into a complex of at least 19 chains with a combined molecular mass of around 1.2 MDa; APC/C interacts with FZR1 and FBXO5. The C-terminus of APC10 binds to CDC27/APC3 (By similarity). Interacts with PIWIL1; interaction only takes place when PIWIL1 binds piRNA (PubMed:23328397). {ECO:0000250|UniProtKB:Q9UM13, ECO:0000269|PubMed:23328397}. +P97429 ANXA4_MOUSE Annexin A4 (Annexin IV) (Annexin-4) 319 35,916 Chain (1); Modified residue (5); Repeat (4); Sequence conflict (2) FUNCTION: Calcium/phospholipid-binding protein which promotes membrane fusion and is involved in exocytosis. {ECO:0000250}. DOMAIN: A pair of annexin repeats may form one binding site for calcium and phospholipid. +Q5SUE8 ANR40_MOUSE Ankyrin repeat domain-containing protein 40 363 40,560 Alternative sequence (4); Chain (1); Compositional bias (2); Modified residue (2); Repeat (2); Sequence conflict (3) +Q9D842 APLF_MOUSE Aprataxin and PNK-like factor (EC 4.2.99.18) (Apurinic-apyrimidinic endonuclease APLF) 499 54,968 Alternative sequence (3); Binding site (7); Chain (1); Compositional bias (2); Domain (1); Modified residue (2); Region (1); Sequence conflict (2); Zinc finger (2) FUNCTION: Nuclease involved in single-strand and double-strand DNA break repair. Recruited to sites of DNA damage through interaction with poly(ADP-ribose), a polymeric post-translational modification synthesized transiently at sites of chromosomal damage to accelerate DNA strand break repair reactions. Displays apurinic-apyrimidinic (AP) endonuclease and 3'-5' exonuclease activities in vitro. Also able to introduce nicks at hydroxyuracil and other types of pyrimidine base damage. Together with PARP3, promotes the retention of the LIG4-XRCC4 complex on chromatin and accelerate DNA ligation during non-homologous end-joining (NHEJ). {ECO:0000250|UniProtKB:Q8IW19}. PTM: Poly-ADP-ribosylated. In addition to binding non covalently poly(ADP-ribose) via its PBZ-type zinc fingers, the protein is also covalently poly-ADP-ribosylated by PARP1. {ECO:0000250|UniProtKB:Q8IW19}.; PTM: Phosphorylated in an ATM-dependent manner upon double-strand DNA break. {ECO:0000250|UniProtKB:Q8IW19}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8IW19}. Chromosome {ECO:0000250|UniProtKB:Q8IW19}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8IW19}. Note=Localizes to DNA damage sites. Accumulates at single-strand breaks and double-strand breaks via the PBZ-type zinc fingers. {ECO:0000250|UniProtKB:Q8IW19}. SUBUNIT: Interacts with LIG4, PARP1, XRCC1, XRCC4 and XRCC5. {ECO:0000250|UniProtKB:Q8IW19}. DOMAIN: The PBZ-type zinc fingers (also named CYR) mediate non-covalent poly(ADP-ribose)-binding. Poly(ADP-ribose)-binding is dependent on the presence of zinc and promotes its recruitment to DNA damage sites. {ECO:0000250|UniProtKB:Q8IW19}.; DOMAIN: The FHA-like domain mediates interaction with XRCC1 and XRCC4. {ECO:0000250|UniProtKB:Q8IW19}. +Q8VE42 ANR49_MOUSE Ankyrin repeat domain-containing protein 49 (Fetal globin-increasing factor) (Fetal globin-inducing factor) 238 27,111 Chain (1); Modified residue (1); Repeat (4); Sequence conflict (1) FUNCTION: May have a role in spermatogenesis where it promotes autophagy in response to serum starvation, via the NF-kappaB pathway. {ECO:0000269|PubMed:26043108}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26043108}. TISSUE SPECIFICITY: Expressed in spermatogonia, spermatocytes and round spermatids. {ECO:0000269|PubMed:26043108}. +Q9CQW7 APOP1_MOUSE Apoptogenic protein 1, mitochondrial (APOP-1) 192 22,715 Alternative sequence (1); Chain (1); Transit peptide (1) FUNCTION: Plays a role in the regulation of apoptosis. Mediates mitochondria-induced cell death in vascular smooth muscle cells through the release of cytochrome c from mitochondria, followed by the activation of the caspase cascade. {ECO:0000269|PubMed:16782708, ECO:0000269|PubMed:18977203}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16782708, ECO:0000269|PubMed:18977203}. TISSUE SPECIFICITY: Expressed in atherosclerotic smooth muscle cells (at protein level). Expressed in aorta, brain, heart, kidney, liver, lung and spleen. Isoform 1 is strongly expressed in Kidney. Isoform 2 is strongly expressed in brain. {ECO:0000269|PubMed:16782708}. +Q9JM54 APR_MOUSE Phorbol-12-myristate-13-acetate-induced protein 1 (Protein Noxa) 103 11,566 Chain (1); Helix (2); Motif (2); Mutagenesis (2); Region (1) FUNCTION: Promotes activation of caspases and apoptosis. Promotes mitochondrial membrane changes and efflux of apoptogenic proteins from the mitochondria. Contributes to p53/TP53-dependent apoptosis after radiation exposure. Promotes proteasomal degradation of MCL1. Competes with BIM/BCL2L11 for binding to MCL1 and can displace BIM/BCL2L11 from its binding site on MCL1 (By similarity). Competes with BAK1 for binding to MCL1 and can displace BAK1 from its binding site on MCL1. {ECO:0000250, ECO:0000269|PubMed:10807576, ECO:0000269|PubMed:15694340, ECO:0000269|PubMed:15901672, ECO:0000269|PubMed:16822983, ECO:0000269|PubMed:17389404}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:10807576}. SUBUNIT: Interacts with MCL1, BCL2A1 and BAX. {ECO:0000250}. DOMAIN: The BH3 motif is essential for pro-apoptotic activity. TISSUE SPECIFICITY: Detected in thymocytes after irradiation with X-rays. Not detectable in untreated thymocytes (at protein level). Detected in embryonic neural precursor cells of the telencephalon Constitutively expressed at low levels in adult brain, testis, thymus, spleen, lung and kidney. {ECO:0000269|PubMed:16822983}. +O35409 FOLH1_MOUSE Glutamate carboxypeptidase 2 (EC 3.4.17.21) (Folate hydrolase 1) (Folylpoly-gamma-glutamate carboxypeptidase) (FGCP) (Glutamate carboxypeptidase II) (GCPII) (Membrane glutamate carboxypeptidase) (mGCP) (N-acetylated-alpha-linked acidic dipeptidase I) (NAALADase I) (Prostate-specific membrane antigen homolog) (Pteroylpoly-gamma-glutamate carboxypeptidase) 752 84,574 Active site (4); Binding site (5); Chain (1); Glycosylation (9); Metal binding (10); Modified residue (1); Region (5); Sequence conflict (9); Topological domain (2); Transmembrane (1) TRANSMEM 23 44 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 22 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 45 752 Extracellular. {ECO:0000255}. FUNCTION: Has both folate hydrolase and N-acetylated-alpha-linked-acidic dipeptidase (NAALADase) activity. Has a preference for tri-alpha-glutamate peptides (By similarity). In the intestine, required for the uptake of folate. In the brain, modulates excitatory neurotransmission through the hydrolysis of the neuropeptide, N-aceylaspartylglutamate (NAAG), thereby releasing glutamate. {ECO:0000250}.; FUNCTION: Also exhibits a dipeptidyl-peptidase IV type activity. In vitro, cleaves Gly-Pro-AMC. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q04609}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q04609}. SUBUNIT: Homodimer. {ECO:0000250}. DOMAIN: The NAALADase activity is found in the central region, the dipeptidyl peptidase IV type activity in the C-terminal. TISSUE SPECIFICITY: Expressed predominantly in the hippocampal region of the brain and in kidney. Lower levels in the ovary, testis and mandibular gland. +Q8BHD4 FRMD3_MOUSE FERM domain-containing protein 3 595 68,448 Alternative sequence (3); Chain (1); Domain (1); Sequence conflict (1); Transmembrane (1) TRANSMEM 529 549 Helical. {ECO:0000255}. FUNCTION: Putative tumor suppressor gene that may be implicated in the origin and progression of lung cancer. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q8BZ52 FSD2_MOUSE Fibronectin type III and SPRY domain-containing protein 2 (Minispryn) (SPRY domain-containing protein 1) 716 81,473 Chain (1); Coiled coil (1); Domain (3); Erroneous initiation (1); Sequence conflict (2) SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:H0UZ81}. Sarcoplasmic reticulum {ECO:0000250|UniProtKB:H0UZ81}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:H0UZ81}. Note=In skeletal muscles and striated muscles flanks Z-disks. Partially colocalizes with RYR2 in the sarcoplasmic reticulum. {ECO:0000250|UniProtKB:H0UZ81}. SUBUNIT: Interacts with CMYA5 (PubMed:28740084). In cardiac muscles, identified in a complex composed of FSD2, CMYA5 and RYR2 (PubMed:28740084). {ECO:0000269|PubMed:28740084}. TISSUE SPECIFICITY: Expressed predominantly in heart and skeletal muscle (at protein level). {ECO:0000269|PubMed:28740084}. +Q5STE3 FSTL4_MOUSE Follistatin-related protein 4 (Follistatin-like protein 4) (m-D/Bsp120I 1-1) 841 92,579 Calcium binding (2); Chain (1); Disulfide bond (5); Domain (5); Glycosylation (1); Sequence conflict (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q8BFR2 FSTL5_MOUSE Follistatin-related protein 5 (Follistatin-like protein 5) (m-D/Bsp120I 1-2) 847 95,816 Calcium binding (2); Chain (1); Disulfide bond (5); Domain (5); Glycosylation (2); Sequence conflict (3); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +P30681 HMGB2_MOUSE High mobility group protein B2 (High mobility group protein 2) (HMG-2) 210 24,162 Chain (1); Compositional bias (1); DNA binding (2); Disulfide bond (1); Modified residue (11); Region (1); Sequence conflict (19) FUNCTION: Multifunctional protein with various roles in different cellular compartments. May act in a redox sensitive manner. In the nucleus is an abundant chromatin-associated non-histone protein involved in transcription, chromatin remodeling and V(D)J recombination and probably other processes. Binds DNA with a preference to non-canonical DNA structures such as single-stranded DNA. Can bent DNA and enhance DNA flexibility by looping thus providing a mechanism to promote activities on various gene promoters by enhancing transcription factor binding and/or bringing distant regulatory sequences into close proximity (By similarity). Involved in V(D)J recombination by acting as a cofactor of the RAG complex: acts by stimulating cleavage and RAG protein binding at the 23 bp spacer of conserved recombination signal sequences (RSS) (PubMed:9184213). Proposed to be involved in the innate immune response to nucleic acids by acting as a cytoplasmic promiscuous immunogenic DNA/RNA sensor which cooperates with subsequent discriminative sensing by specific pattern recognition receptors (PubMed:19890330). In the extracellular compartment acts as a chemokine. Promotes proliferation and migration of endothelial cells implicating AGER/RAGE (By similarity). Has antimicrobial activity in gastrointestinal epithelial tissues (By similarity). Involved in inflammatory response to antigenic stimulus coupled with proinflammatory activity (PubMed:25306442). May play a role in germ cell differentiation (PubMed:11262228). Involved in modulation of neurogenesis probably by regulation of neural stem proliferation (PubMed:24391977). Involved in articular cartilage surface maintenance implicating LEF1 and the Wnt/beta-catenin pathway (PubMed:19805379). {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P26583, ECO:0000269|PubMed:19805379, ECO:0000269|PubMed:19890330, ECO:0000269|PubMed:23495099, ECO:0000269|PubMed:24391977, ECO:0000269|PubMed:25306442, ECO:0000269|PubMed:9184213, ECO:0000305|PubMed:11262228}. PTM: Reduction/oxidation of cysteine residues Cys-23, Cys-45 and Cys-106 and a possible intramolecular disulfide bond involving Cys-23 and Cys-45 give rise to different redox forms with specific functional activities in various cellular compartments: 1- fully reduced HMGB2 (HMGB2C23hC45hC106h), 2- disulfide HMGB2 (HMGB2C23-C45C106h) and 3- sulfonyl HMGB2 (HMGB2C23soC45soC106so). {ECO:0000250|UniProtKB:P09429}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P09429}. Chromosome {ECO:0000250|UniProtKB:P26583}. Cytoplasm {ECO:0000269|PubMed:19890330}. Secreted {ECO:0000250|UniProtKB:P26583}. SUBUNIT: Interacts with POU2F2, POU2F1 and POU3F1 (PubMed:7720710). Component of the RAG complex composed of core components RAG1 and RAG2, and associated component HMGB1 or HMGB2 (PubMed:9184213). Component of the SET complex, composed of at least ANP32A, APEX1, HMGB2, NME1, SET and TREX1. Directly interacts with SET (By similarity). Interacts with LEF1 (PubMed:19805379). {ECO:0000250|UniProtKB:P26583, ECO:0000269|PubMed:19805379, ECO:0000269|PubMed:7720710, ECO:0000269|PubMed:9184213}. DOMAIN: Both, HMG box 1 and HMG box 2, show antimicrobial activity. {ECO:0000250|UniProtKB:P26583}. TISSUE SPECIFICITY: Widely expressed in embryo. In adult mainly expressed in lymphoid organs and testes (PubMed:11262228). Expressed in primary spermatocytes. Expressed in the superficial zone of articular cartilage (PubMed:19805379). {ECO:0000269|PubMed:11262228, ECO:0000269|PubMed:19805379}. +Q8CG73 FTM_MOUSE Protein fantom (Nephrocystin-8) (RPGR-interacting protein 1-like protein) (RPGRIP1-like protein) 1264 145,000 Chain (1); Coiled coil (4); Domain (2); Sequence conflict (2) FUNCTION: Negatively regulates signaling through the G-protein coupled thromboxane A2 receptor (TBXA2R) (By similarity). May be involved in mechanisms like programmed cell death, craniofacial development, patterning of the limbs, and formation of the left-right axis. Involved in the organization of apical junctions; the function is proposed to implicate a NPHP1-4-8 module. Does not seem to be strictly required for ciliogenesis (By similarity). Involved in establishment of planar cell polarity such as in cochlear sensory epithelium and is proposed to implicate stabilization of disheveled proteins (PubMed:22927466). Involved in regulation of proteasomal activity at the primary cilium probably implicating association with PSDM2 (PubMed:26150391). {ECO:0000250|UniProtKB:Q68CZ1, ECO:0000269|PubMed:10501967, ECO:0000269|PubMed:11956760, ECO:0000269|PubMed:21565611, ECO:0000269|PubMed:22927466, ECO:0000269|PubMed:26150391}. SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:21565611}. Cytoplasm, cytoskeleton, cilium axoneme. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:26150391}. Cell junction, tight junction {ECO:0000269|PubMed:21565611}. Note=In cultured renal cells, it localizes diffusely in the cytoplasm but, as cells approach confluence, it accumulates to basolateral tight junctions. Localizes to the ciliary transition zone. {ECO:0000269|PubMed:21565611, ECO:0000269|PubMed:22927466, ECO:0000269|PubMed:26150391}. SUBUNIT: Interacts with NPHP4 and NPHP1; NPHP1, NPHP4 and RPGRIP1L are proposed to form a functional NPHP1-4-8 module localized to cell-cell contacts and the ciliary transition zone; NPHP4 mediates the interaction between NPHP1 and RPGRIP1L. Interacts with IQCB1; the interaction likely requires additional interactors (PubMed:21565611). Interacts with TBXA2R (via C-terminus), RPGR, NEK4. Interacts with NPHP4, INVS and DVL2; proposed to form a complex involved in DVL2 stabilization (By similarity). Interacts with PSMD2 (PubMed:26150391). {ECO:0000250|UniProtKB:Q68CZ1, ECO:0000269|PubMed:21565611, ECO:0000269|PubMed:26150391}. TISSUE SPECIFICITY: Ubiquitously expressed. Not found in heart and skin. {ECO:0000269|PubMed:10501967}. +O54879 HMGB3_MOUSE High mobility group protein B3 (High mobility group protein 2a) (HMG-2a) (High mobility group protein 4) (HMG-4) 200 23,010 Chain (1); Compositional bias (1); DNA binding (2); Disulfide bond (1); Modified residue (9) FUNCTION: Multifunctional protein with various roles in different cellular compartments. May act in a redox sensitive manner. Associates with chromatin and binds DNA with a preference to non-canonical DNA structures such as single-stranded DNA. Can bent DNA and enhance DNA flexibility by looping thus providing a mechanism to promote activities on various gene promoters (By similarity). Proposed to be involved in the innate immune response to nucleic acids by acting as a cytoplasmic promiscuous immunogenic DNA/RNA sensor (PubMed:19890330). Negatively regulates B-cell and myeloid cell differentiation. In hematopoietic stem cells may regulate the balance between self-renewal and differentiation. Involved in negative regulation of canonical Wnt signaling (PubMed:12714519, PubMed:15358624, PubMed:16945912). {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P40618, ECO:0000269|PubMed:12714519, ECO:0000269|PubMed:15358624, ECO:0000269|PubMed:16945912, ECO:0000269|PubMed:19890330}. PTM: Reduction/oxidation of cysteine residues Cys-23, Cys-45 and Cys-104 and a possible intramolecular disulfide bond involving Cys-23 and Cys-45 give rise to different redox forms with specific functional activities in various cellular compartments: 1- fully reduced HMGB3 (HMGB3C23hC45hC104h), 2- disulfide HMGB3 (HMGB3C23-C45C104h) and 3- sulfonyl HMGB3 (HMGB3C23soC45soC104so). {ECO:0000250|UniProtKB:P09429}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P40618, ECO:0000255|PROSITE-ProRule:PRU00267}. Chromosome {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:19890330}. TISSUE SPECIFICITY: Expressed in bone marrow cells, specifically in primitive Lin-, c-kit+, Sca-1+, IL-7Ralpha- cells, and Ter119+ erythroid cells (PubMed:12714519). {ECO:0000269|PubMed:12714519}. +Q9CZV8 FXL20_MOUSE F-box/LRR-repeat protein 20 (F-box and leucine-rich repeat protein 20) (F-box/LRR-repeat protein 2-like) 436 48,396 Alternative sequence (2); Chain (1); Domain (1); Erroneous initiation (1); Modified residue (2); Repeat (13); Sequence caution (1); Sequence conflict (2) FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. Isoform 3 regulates neural transmission by binding and ubiquitinating RIMS1, a modulator of presynaptic plasticity. {ECO:0000269|PubMed:17803915}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17803915}. Note=Isoform 3 is present at the presynaptic membrane. SUBUNIT: Interacts with SKP1 and CUL1. {ECO:0000269|PubMed:17803915}. TISSUE SPECIFICITY: Highly expressed in brain. {ECO:0000269|PubMed:17803915}. +Q9R0N0 GALK1_MOUSE Galactokinase (EC 2.7.1.6) (Galactose kinase) 392 42,295 Active site (1); Binding site (1); Chain (1); Modified residue (1); Nucleotide binding (1); Region (2); Sequence conflict (1); Site (1) Carbohydrate metabolism; galactose metabolism. FUNCTION: Major enzyme for galactose metabolism. SUBUNIT: Homodimer. {ECO:0000250}. +Q60780 GAS7_MOUSE Growth arrest-specific protein 7 (GAS-7) 421 48,174 Alternative sequence (2); Chain (1); Coiled coil (1); Domain (2); Modified residue (2) FUNCTION: May play a role in promoting maturation and morphological differentiation of cerebellar neurons. SUBCELLULAR LOCATION: Cytoplasm. TISSUE SPECIFICITY: Expressed abundantly in brain with lower levels in heart and testis. In the brain, expressed prominently in the Purkinje layer of the cerebellum, moderately in hippocampus, and less extensively in cerebral cortex and caudate putamen. {ECO:0000269|PubMed:10552931}. +Q3UFT3 GARE1_MOUSE GRB2-associated and regulator of MAPK protein (GRB2-associated and regulator of MAPK1) 876 97,250 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (1); Modified residue (4); Region (2); Sequence conflict (3) FUNCTION: Acts as an adapter protein that plays a role in intracellular signaling cascades triggered either by the cell surface activated epidermal growth factor receptor and/or cytoplasmic protein tyrosine kinases. Promotes activation of the MAPK/ERK signaling pathway. Plays a role in the regulation of cell proliferation (By similarity). {ECO:0000250}. PTM: On EGF stimulation, phosphorylated on Tyr-105 and Tyr-453. {ECO:0000250}. SUBUNIT: Interacts with EGFR. Interacts (via proline-rich domain and phosphorylated at Tyr-105 and Tyr-453) with GRB2 (via SH3 domains); the interaction occurs upon EGF stimulation. Interacts (phosphorylated at Tyr-453) with PTPN11; the interaction increases MAPK/ERK activity and does not affect the GRB2/SOS complex formation (By similarity). {ECO:0000250}. +Q01721 GAS1_MOUSE Growth arrest-specific protein 1 (GAS-1) 343 35,694 Chain (1); Compositional bias (4); Erroneous initiation (1); Glycosylation (2); Lipidation (1); Propeptide (1); Signal peptide (1) FUNCTION: Specific growth arrest protein involved in growth suppression. Blocks entry to S phase. Prevents cycling of normal and transformed cells. {ECO:0000269|PubMed:1505026}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. +P56481 GASR_MOUSE Gastrin/cholecystokinin type B receptor (CCK-B receptor) (CCK-BR) (Cholecystokinin-2 receptor) (CCK2-R) 453 49,172 Chain (1); Disulfide bond (1); Glycosylation (3); Lipidation (1); Topological domain (8); Transmembrane (7) TRANSMEM 58 79 Helical; Name=1. {ECO:0000255}.; TRANSMEM 88 109 Helical; Name=2. {ECO:0000255}.; TRANSMEM 132 150 Helical; Name=3. {ECO:0000255}.; TRANSMEM 171 189 Helical; Name=4. {ECO:0000255}.; TRANSMEM 220 242 Helical; Name=5. {ECO:0000255}.; TRANSMEM 340 361 Helical; Name=6. {ECO:0000255}.; TRANSMEM 380 400 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 57 Extracellular. {ECO:0000255}.; TOPO_DOM 80 87 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 110 131 Extracellular. {ECO:0000255}.; TOPO_DOM 151 170 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 190 219 Extracellular. {ECO:0000255}.; TOPO_DOM 243 339 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 362 379 Extracellular. {ECO:0000255}.; TOPO_DOM 401 453 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for gastrin and cholecystokinin. The CCK-B receptors occur throughout the central nervous system where they modulate anxiety, analgesia, arousal, and neuroleptic activity. This receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q8VI38 GBGT1_MOUSE Globoside alpha-1,3-N-acetylgalactosaminyltransferase 1 (EC 2.4.1.88) (Forssman glycolipid synthase) 347 40,502 Active site (1); Chain (1); Glycosylation (1); Metal binding (2); Region (3); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 7 27 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 28 347 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Catalyzes the formation of Forssman glycolipid via the addition of N-acetylgalactosamine (GalNAc) in alpha-1,3-linkage to GalNAcb-1,3Gala-1,4Galb-1,4GlcCer (Gb4Cer). Forssman glycolipid (also called Forssman antigen; FG) probably serves for adherence of some pathogens. Conversely, it diminishes Shiga toxins susceptibility. {ECO:0000269|PubMed:14573676}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. DOMAIN: The conserved DXD motif is involved in cofactor binding. The manganese ion interacts with the beta-phosphate group of UDP and may also have a role in catalysis (By similarity). {ECO:0000250}. +Q9JMF3 GBG13_MOUSE Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-13 67 7,979 Chain (1); Lipidation (1); Modified residue (1); Propeptide (1) FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. SUBUNIT: G proteins are composed of 3 units, alpha, beta and gamma. +P97737 GDF10_MOUSE Growth/differentiation factor 10 (GDF-10) (Bone morphogenetic protein 3B) (BMP-3B) 476 52,575 Chain (1); Disulfide bond (4); Glycosylation (4); Propeptide (1); Sequence conflict (2); Signal peptide (1) FUNCTION: Growth factor involved in osteogenesis and adipogenesis. Plays an inhibitory role in the process of osteoblast differentiation via SMAD2/3 pathway (PubMed:22155034). Plays an inhibitory role in the process of adipogenesis (PubMed:21712809). {ECO:0000269|PubMed:21712809, ECO:0000269|PubMed:22155034}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21712809}. SUBUNIT: Homodimer or heterodimer. Can form a non-covalent complex of the mature region and the pro-region (PubMed:21712809). {ECO:0000269|PubMed:21712809, ECO:0000305}. TISSUE SPECIFICITY: Highly expressed in epididymal adipose tissue, brain, bone and aorta and to a lesser extent in liver and spleen. Expressed at higher levels in preadipocytes than in mature adipocytes (PubMed:21712809). Strongly expressed in glial cells of the cerebellum (PubMed:24963847). {ECO:0000269|PubMed:10419686, ECO:0000269|PubMed:22155034, ECO:0000269|PubMed:24963847, ECO:0000269|PubMed:8679252}. +Q9Z1W4 GDF11_MOUSE Growth/differentiation factor 11 (GDF-11) (Bone morphogenetic protein 11) (BMP-11) 405 44,947 Chain (1); Compositional bias (2); Disulfide bond (5); Glycosylation (1); Mutagenesis (1); Propeptide (1); Sequence conflict (2); Signal peptide (1); Site (1) FUNCTION: Secreted signal that acts globally to specify positional identity along the anterior/posterior axis during development (PubMed:10391213). May play critical roles in patterning both mesodermal and neural tissues and in establishing the skeletal pattern. Signals through activin receptors type-2, ACVR2A and ACVR2B, and activin receptors type-1, ACVR1B, ACVR1C and TGFBR1 leading to the phosphorylation of SMAD2 and SMAD3 (PubMed:16845371, PubMed:12414726). {ECO:0000250|UniProtKB:O95390, ECO:0000269|PubMed:10391213, ECO:0000269|PubMed:12414726, ECO:0000269|PubMed:16845371}. PTM: Synthesized as large precursor molecule that undergoes proteolytic cleavage. The mature C-terminal portion of the molecule is bound non-covalently to its N-terminal propeptide rendering it inactive. Ligand activation requires additional cleavage of the prodomain by a tolloid-like metalloproteinase. {ECO:0000269|PubMed:15988002}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. SUBUNIT: Homodimer; disulfide-linked (By similarity). Interacts directly with ACVR2B (PubMed:16845371, PubMed:12414726). Interacts directly with ACVR2A (PubMed:12414726). Interacts with ACVR1B, TGFBR1 and ACVR1C in an ACVR2B-dependent manner (PubMed:16845371). Interacts with FST isoform 2/FS288 (By similarity). {ECO:0000250|UniProtKB:O95390, ECO:0000269|PubMed:12414726, ECO:0000269|PubMed:16845371}. TISSUE SPECIFICITY: Highly expressed in the developing limb bud, initially detected in the distal mesenchyme, and later localizing to regions around the developing bones. Is also expressed in adult dental pulp and brain. +Q9Z0J7 GDF15_MOUSE Growth/differentiation factor 15 (GDF-15) (Macrophage inhibitory cytokine 1) (MIC-1) 303 33,225 Chain (1); Disulfide bond (5); Glycosylation (1); Propeptide (1); Sequence conflict (8); Signal peptide (1) FUNCTION: Regulates food intake, energy expenditure and body weight in response to metabolic and toxin-induced stresses. Binds to its receptor, GFRAL, and activates GFRAL-expressing neurons localized in the area postrema and nucleus tractus solitarius of the brainstem. It then triggers the activation of neurons localized within the parabrachial nucleus and central amygdala, which contitutes part of the 'emergency circuit' that shapes feeding responses to stressful conditions (PubMed:28953886, PubMed:28846097, PubMed:28846099, PubMed:28572090, PubMed:23468844, PubMed:29046435). On hepatocytes, inhibits growth hormone signaling (PubMed:28572090). {ECO:0000269|PubMed:23468844, ECO:0000269|PubMed:28572090, ECO:0000269|PubMed:28846097, ECO:0000269|PubMed:28846099, ECO:0000269|PubMed:28953886, ECO:0000269|PubMed:29046435}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28572090, ECO:0000269|PubMed:29046435}. SUBUNIT: Homodimer; disulfide-linked (By similarity). Interacts with GFRAL; ligand of GFRAL which mediates GDF15 internalization and cellular signaling through interaction with RET (PubMed:28846098, PubMed:28846099). {ECO:0000250|UniProtKB:Q99988, ECO:0000269|PubMed:28846098, ECO:0000269|PubMed:28846099}. TISSUE SPECIFICITY: Highly expressed in liver (PubMed:10779363, PubMed:28572090, PubMed:29046435). Detected in plasma (at protein level) (PubMed:28572090, PubMed:29046435). Expressed by cardiomyocytes, expression is highly increased in heart diseases (PubMed:28572090). Also detected in subcutaneous fat (PubMed:28572090, PubMed:29046435). {ECO:0000269|PubMed:10779363, ECO:0000269|PubMed:28572090, ECO:0000269|PubMed:29046435}. +P20863 GDF1_MOUSE Embryonic growth/differentiation factor 1 (GDF-1) 357 38,660 Chain (1); Disulfide bond (4); Glycosylation (1); Propeptide (1); Sequence conflict (1); Signal peptide (1) FUNCTION: May mediate cell differentiation events during embryonic development. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}. TISSUE SPECIFICITY: Expressed almost exclusively in the nervous system. +Q9WV56 GDF2_MOUSE Growth/differentiation factor 2 (GDF-2) (Bone morphogenetic protein 9) (BMP-9) 428 47,703 Beta strand (12); Chain (1); Disulfide bond (5); Glycosylation (3); Helix (4); Propeptide (1); Region (1); Sequence conflict (2); Signal peptide (1); Turn (2) FUNCTION: Potent circulating inhibitor of angiogenesis (By similarity). Signals through the type I activin receptor ACVRL1 but not other Alks (PubMed:25751889). Signaling through SMAD1 in endothelial cells requires TGF-beta coreceptor endoglin/ENG (PubMed:23300529). {ECO:0000250|UniProtKB:Q9UK05, ECO:0000269|PubMed:23300529, ECO:0000269|PubMed:25751889}. PTM: A reversible disulfide bond can be formed between the two subunits in the homodimer; this has no effect on GDF2 activity. {ECO:0000250|UniProtKB:Q9UK05}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9UK05}. SUBUNIT: Homodimer; disulfide-linked. Detected in extracellular fluid as mature homodimer, and in complex with its propeptide (By similarity). Interacts with ACVRL1, BMPR2 and ACVR2B with high affinity (in vitro) (PubMed:25751889). Identified in a complex with ACVRL1 and ACVR2B (By similarity). Has ten times lower affinity for ACVR2A (in vitro) (PubMed:25751889). Interacts with ENG, forming a heterotetramer with a 2:2 stoichiometry. Can form a heteromeric complex with ENG and ACVRL1 (By similarity). {ECO:0000250|UniProtKB:Q9UK05, ECO:0000269|PubMed:25751889}. +Q07104 GDF3_MOUSE Growth/differentiation factor 3 (GDF-3) (VG-1-related protein 2) 366 41,586 Chain (1); Disulfide bond (3); Glycosylation (2); Propeptide (1); Sequence conflict (5); Signal peptide (1) FUNCTION: Growth factor involved in early embryonic development and adipose-tissue homeostasis. During embryogenesis controls formation of anterior visceral endoderm and mesoderm and the establishment of anterior-posterior identity through a receptor complex comprising the receptor ACVR1B and the coreceptor TDGF1/Cripto (PubMed:16368929, PubMed:17936261). Regulates adipose-tissue homeostasis and energy balance under nutrient overload in part by signaling through the receptor complex based on ACVR1C and TDGF1/Cripto. {ECO:0000269|PubMed:16368929, ECO:0000269|PubMed:17936261, ECO:0000269|PubMed:18480259}. PTM: Synthesized as large precursor molecule that undergo proteolytic cleavage, releasing the pro-domain from the active, receptor binding, C-terminal region of the molecule. {ECO:0000250|UniProtKB:Q9NR23}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9NR23}. Cytoplasm {ECO:0000250|UniProtKB:Q9NR23}. Note=Mainly accumulated in the cytoplasm. {ECO:0000250|UniProtKB:Q9NR23}. SUBUNIT: Homodimer. Heterodimer (Potential). But, in contrast to other members of this family, cannot be disulfide-linked. {ECO:0000305}. TISSUE SPECIFICITY: Primarily in adult bone marrow, spleen, thymus and adipose tissue. {ECO:0000269|PubMed:1480182, ECO:0000269|PubMed:18480259, ECO:0000269|PubMed:8429021}. +P43027 GDF5_MOUSE Growth/differentiation factor 5 (GDF-5) (Bone morphogenetic protein 14) (BMP-14) 495 54,895 Chain (1); Disulfide bond (4); Glycosylation (1); Natural variant (1); Propeptide (1); Signal peptide (1) FUNCTION: Growth factor involved in bone and cartilage formation. During cartilage development regulates differentiation of chondrogenic tissue through two pathways. Firstly, positively regulates differentiation of chondrogenic tissue through its binding of high affinity with BMPR1B and of less affinity with BMPR1A, leading to induction of SMAD1-SMAD5-SMAD8 complex phosphorylation and then SMAD protein signaling transduction (By similarity). Secondly, negatively regulates chondrogenic differentiation through its interaction with NOG (By similarity). Required to prevent excessive muscle loss upon denervation. This function requires SMAD4 and is mediated by phosphorylated SMAD1/5/8 (PubMed:24076600). Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes (By similarity). {ECO:0000250|UniProtKB:P43026, ECO:0000269|PubMed:24076600}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P43026}. Cell membrane {ECO:0000250|UniProtKB:P43026}. SUBUNIT: Homodimer; disulfide-linked (By similarity). Interacts with serine proteases, HTRA1 and HTRA3 (PubMed:15206957, PubMed:14973287). Following LPS binding, may form a complex with CXCR4, HSP90AA1 and HSPA8 (By similarity). Interacts with high affinity with NOG; inhibits chondrogenesis (By similarity). Interacts with high affinity with BMPR1B and lower affinity with BMPR1A; positively regulates chondrocyte differentiation and induces SMAD-dependent signaling. Interacts with FBN1 (via N-terminal domain) and FBN2 (By similarity). {ECO:0000250|UniProtKB:P43026, ECO:0000269|PubMed:14973287, ECO:0000269|PubMed:15206957}. DISEASE: Note=Defects in Gdf5 are the cause of brachypodism (bp) which alters the length and numbers of bones in the limbs but spares the axial skeleton. {ECO:0000269|PubMed:8145850}. +P43028 GDF6_MOUSE Growth/differentiation factor 6 (GDF-6) (Bone morphogenetic protein 13) (BMP-13) (Growth/differentiation factor 16) 454 50,942 Chain (1); Compositional bias (2); Disulfide bond (4); Glycosylation (1); Propeptide (1); Signal peptide (1) FUNCTION: Growth factor that controls proliferation and cellular differentiation in the retina and bone formation. Plays a key role in regulating apoptosis during retinal development. Establishes dorsal-ventral positional information in the retina and controls the formation of the retinotectal map (PubMed:23307924). Required for normal formation of bones and joints in the limbs, skull, digits and axial skeleton. Plays a key role in establishing boundaries between skeletal elements during development. Regulation of GDF6 expression seems to be a mechanism for evolving species-specific changes in skeletal structures (PubMed:26774823). Seems to positively regulate differentiation of chondrogenic tissue through the growth factor receptors subunits BMPR1A, BMPR1B, BMPR2 and ACVR2A, leading to the activation of SMAD1-SMAD5-SMAD8 complex. The regulation of chondrogenic differentiation is inhibited by NOG (PubMed:12606286, PubMed:16049014). Also involved in the induction of adipogenesis from mesenchymal stem cells. This mechanism acts through the growth factor receptors subunits BMPR1A, BMPR2 and ACVR2A and the activation of SMAD1-SMAD5-SMAD8 complex and MAPK14/p38 (PubMed:23527555). {ECO:0000269|PubMed:12606286, ECO:0000269|PubMed:16049014, ECO:0000269|PubMed:23307924, ECO:0000269|PubMed:23527555, ECO:0000269|PubMed:26774823}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q6KF10}. SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250|UniProtKB:P39905}. TISSUE SPECIFICITY: Expressed in different subsets of developing joints. {ECO:0000269|PubMed:12606286}. +P43029 GDF7_MOUSE Growth/differentiation factor 7 (GDF-7) 461 47,891 Alternative sequence (1); Chain (1); Compositional bias (2); Disulfide bond (4); Glycosylation (1); Propeptide (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}. +O70237 GFI1B_MOUSE Zinc finger protein Gfi-1b (Growth factor independent protein 1B) 330 37,443 Chain (1); Modified residue (1); Mutagenesis (1); Region (3); Sequence conflict (1); Zinc finger (6) FUNCTION: Essential proto-oncogenic transcriptional regulator necessary for development and differentiation of erythroid and megakaryocytic lineages. Component of a RCOR-GFI-KDM1A-HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development and controls hematopoietic differentiation. Transcriptional repressor or activator depending on both promoter and cell type context; represses promoter activity of SOCS1 and SOCS3 and thus, may regulate cytokine signaling pathways. Cooperates with GATA1 to repress target gene transcription, such as the apoptosis regulator BCL2L1; GFI1B silencing in leukemic cell lines markedly increase apoptosis rate. Inhibits down-regulation of MYC and MYB as well as the cyclin-dependent kinase inhibitor CDKN1A/P21WAF1 in IL6-treated myelomonocytic cells. Represses expression of GATA3 in T-cell lymphomas and inhibits GATA1-mediated transcription; as GATA1 also mediates erythroid GFI1B transcription, both GATA1 and GFI1B participate in a feedback regulatory pathway controlling the expression of GFI1B gene in erythroid cells. Suppresses GATA1-mediated stimulation of GFI1B promoter through protein interaction. Binds to gamma-satellite DNA and to its own promoter, auto-repressing its own expression. Alters histone methylation by recruiting histone methyltransferase to target genes promoters. Plays a role in heterochromatin formation. {ECO:0000269|PubMed:11696536, ECO:0000269|PubMed:12351384, ECO:0000269|PubMed:12594258, ECO:0000269|PubMed:15718298, ECO:0000269|PubMed:17707228, ECO:0000269|PubMed:9566867}. PTM: Methylation at Lys-8 in the SNAG domain seems required for the recruitment of the corepressor complex. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12594258}. Note=Localized at foci of pericentric heterochromatin. SUBUNIT: Interacts with histone methyltransferases EHMT2 and SUV39H1. Interacts with ARIH2 (via RING-type 2) and with RUNX1T1 (By similarity). Forms a complex with GATA1. Component of a RCOR-GFI-KDM1A-HDAC complex. Interacts directly with RCOR1, KDM1A and HDAC2. {ECO:0000250, ECO:0000269|PubMed:15920471, ECO:0000269|PubMed:17707228}. DOMAIN: The zinc finger domain is essential for erythroid expansion and acts as an activation domain whereas non finger domain serves as repression domain. {ECO:0000269|PubMed:12351384}.; DOMAIN: The SNAG domain of GFIs is required for nuclear location and for interaction with some corepressors. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in bone marrow and in spleen. Detected in hematopoietic stem cells, erythroblasts, and megakaryocytes. Expressed in thymocytes. {ECO:0000269|PubMed:12351384, ECO:0000269|PubMed:12594258, ECO:0000269|PubMed:17095621, ECO:0000269|PubMed:9566867}. +Q9D1H0 RITA1_MOUSE RBPJ-interacting and tubulin-associated protein 1 (RBPJ-interacting and tubulin-associated protein) 253 27,071 Chain (1); Motif (1); Region (2) FUNCTION: Tubulin-binding protein that acts as a negative regulator of Notch signaling pathway. Shuttles between the cytoplasm and the nucleus and mediates the nuclear export of RBPJ/RBPSUH, thereby preventing the interaction between RBPJ/RBPSUH and NICD product of Notch proteins (Notch intracellular domain), leading to down-regulate Notch-mediated transcription. May play a role in neurogenesis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Note=Shuttles rapidly between the cytoplasm and the nucleus. The function of centrosome localization is still unclear (By similarity). {ECO:0000250}. SUBUNIT: Interacts with RBPJ/RBPSUH. {ECO:0000250}. +P62830 RL23_MOUSE 60S ribosomal protein L23 140 14,865 Chain (1); Modified residue (2); Sequence conflict (2) +P62843 RS15_MOUSE 40S ribosomal protein S15 (RIG protein) 145 17,040 Chain (1); Cross-link (1); Initiator methionine (1); Modified residue (1) +P62702 RS4X_MOUSE 40S ribosomal protein S4, X isoform 263 29,598 Chain (1); Cross-link (1); Domain (1); Modified residue (1); Sequence conflict (1) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. {ECO:0000250}. SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. {ECO:0000250}. +P83882 RL36A_MOUSE 60S ribosomal protein L36a (60S ribosomal protein L44) 106 12,441 Chain (1) SUBCELLULAR LOCATION: Cytoplasm. +P97461 RS5_MOUSE 40S ribosomal protein S5 [Cleaved into: 40S ribosomal protein S5, N-terminally processed] 204 22,889 Chain (2); Cross-link (1); Initiator methionine (1); Modified residue (5); Sequence conflict (1) +Q8CI94 PYGB_MOUSE Glycogen phosphorylase, brain form (EC 2.4.1.1) 843 96,730 Binding site (4); Chain (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (6); Region (1); Site (4) FUNCTION: Glycogen phosphorylase that regulates glycogen mobilization. Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties. {ECO:0000250|UniProtKB:P11216}. PTM: Phosphorylation of Ser-15 converts phosphorylase B (unphosphorylated) to phosphorylase A. {ECO:0000250|UniProtKB:P11217}. SUBUNIT: Homodimer. Dimers associate into a tetramer to form the enzymatically active phosphorylase A (By similarity). {ECO:0000250|UniProtKB:P11216}. +Q8K459 PXT1_MOUSE Peroxisomal testis-specific protein 1 (Small testis-specific peroxisomal protein) 51 5,934 Chain (1); Motif (1); Mutagenesis (1) SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:18160785}. TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:18160785}. +Q05920 PYC_MOUSE Pyruvate carboxylase, mitochondrial (EC 6.4.1.1) (Pyruvic carboxylase) (PCB) 1178 129,685 Active site (1); Binding site (5); Chain (1); Domain (4); Metal binding (4); Modified residue (28); Mutagenesis (3); Region (1); Transit peptide (1) Carbohydrate biosynthesis; gluconeogenesis. FUNCTION: Pyruvate carboxylase catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second. Catalyzes in a tissue specific manner, the initial reactions of glucose (liver, kidney) and lipid (adipose tissue, liver, brain) synthesis from pyruvate. PTM: Acetylation of Lys-316 is observed in liver mitochondria from fasted mice but not from fed mice (PubMed:23576753). Acetylation of Lys-748 might play a role in catalytic activity regulation (PubMed:23438705). {ECO:0000269|PubMed:23438705}. SUBCELLULAR LOCATION: Mitochondrion matrix. SUBUNIT: Homotetramer (By similarity). Interacts (via the biotin carboxylation domain) with SIRT4 (PubMed:23438705). {ECO:0000250|UniProtKB:P11498, ECO:0000269|PubMed:23438705}. TISSUE SPECIFICITY: Liver, kidney, adipose tissue, liver and brain. +P47964 RL36_MOUSE 60S ribosomal protein L36 105 12,216 Chain (1); Modified residue (1) FUNCTION: Component of the large ribosomal subunit. {ECO:0000250|UniProtKB:Q9Y3U8}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9Y3U8}. Cytoplasm {ECO:0000250|UniProtKB:Q9Y3U8}. Note=Detected on cytosolic polysomes. {ECO:0000250|UniProtKB:Q2YGT9, ECO:0000250|UniProtKB:Q9Y3U8}. SUBUNIT: Component of the large ribosomal subunit. {ECO:0000250|UniProtKB:Q9Y3U8}. +Q8BSI6 R3HC1_MOUSE R3H and coiled-coil domain-containing protein 1 488 54,163 Chain (1); Coiled coil (1); Domain (1); Erroneous initiation (2); Modified residue (1) +Q8VDV3 R3GEF_MOUSE Guanine nucleotide exchange factor for Rab-3A (Rab-3A-interacting-like protein 1) (Rab3A-interacting-like protein 1) (Rabin3-like 1) 383 42,713 Alternative sequence (1); Chain (1); Coiled coil (1); Modified residue (2) FUNCTION: Guanine nucleotide exchange factor (GEF) which may activate RAB3A, a GTPase that regulates synaptic vesicle exocytosis. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. May also activates RAB8A and RAB8B (By similarity). {ECO:0000250}. SUBUNIT: Interacts with RAB3A and IHPK1 through the coiled-coil domain. This interaction is competitive. IHPK1 kinase activity is not required for this interaction (By similarity). {ECO:0000250}. +Q8K386 RAB15_MOUSE Ras-related protein Rab-15 212 24,318 Chain (1); Lipidation (2); Modified residue (1); Nucleotide binding (3) FUNCTION: May act in concert with RAB3A in regulating aspects of synaptic vesicle membrane flow within the nerve terminal. EHBP1L1. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. SUBUNIT: The GTP bound form of RAB15 interacts with REP15. Interacts (GTP-bound form) with MICAL1, MICAL3, MICALCL, EHBP1 and EHBP1L1. {ECO:0000250}. +P61027 RAB10_MOUSE Ras-related protein Rab-10 200 22,541 Chain (1); Lipidation (2); Modified residue (1); Motif (1); Mutagenesis (1); Nucleotide binding (6); Sequence conflict (1) FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (By similarity). That Rab is mainly involved in the biosynthetic transport of proteins from the Golgi to the plasma membrane. Regulates, for instance, SLC2A4/GLUT4 glucose transporter-enriched vesicles delivery to the plasma membrane. In parallel, it regulates the transport of TLR4, a toll-like receptor to the plasma membrane and therefore may be important for innate immune response. Plays also a specific role in asymmetric protein transport to the plasma membrane within the polarized neuron and epithelial cells. In neurons, it is involved in axonogenesis through regulation of vesicular membrane trafficking toward the axonal plasma membrane while in epithelial cells, it regulates transport from the Golgi to the basolateral membrane. Moreover, may play a role in the basolateral recycling pathway and in phagosome maturation. Finally, may play a role in endoplasmic reticulum dynamics and morphology controlling tubulation along microtubules and tubules fusion. {ECO:0000250|UniProtKB:P61026, ECO:0000269|PubMed:17403373, ECO:0000269|PubMed:20643919, ECO:0000269|PubMed:22908308, ECO:0000269|PubMed:27354378}. SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000305}; Lipid-anchor {ECO:0000305|PubMed:20576682}; Cytoplasmic side {ECO:0000305|PubMed:20576682}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:P24409}. Endosome membrane {ECO:0000250|UniProtKB:P61026}. Recycling endosome membrane {ECO:0000250|UniProtKB:P24409}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:P24409}. Cell projection, cilium {ECO:0000269|PubMed:20576682}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:20576682}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:27354378}. Note=Associates with SLC2A4/GLUT4 storage vesicles (PubMed:27354378). Localizes to the base of the cilium (PubMed:20576682). Transiently associates with phagosomes (By similarity). Localizes to the endoplasmic reticulum at domains of new tubule growth (By similarity). {ECO:0000250|UniProtKB:P24409, ECO:0000250|UniProtKB:P61026, ECO:0000269|PubMed:20576682, ECO:0000269|PubMed:27354378}. SUBUNIT: Interacts with MYO5A; mediates the transport to the plasma membrane of SLC2A4/GLUT4 storage vesicles (PubMed:22908308). Interacts with GDI1 and maybe with GDI2; negatively regulates RAB10 association with membranes and activation (PubMed:19570034). Interacts (GDP-bound form) with LLGL1; the interaction is direct and promotes RAB10 association with membranes and activation through competition with the Rab inhibitor GDI1 (By similarity). Interacts with EXOC4; probably associates with the exocyst (By similarity). Interacts (GTP-bound form) with MICALCL, MICAL1, MICAL3, EHBP1 and EHBP1L1; at least in case of MICAL1 two molecules of RAB10 can bind to one molecule of MICAL1 (By similarity). Interacts with TBC1D13 (PubMed:22762500). Interacts with SEC16A (PubMed:27354378). {ECO:0000250|UniProtKB:P24409, ECO:0000250|UniProtKB:P35281, ECO:0000250|UniProtKB:P61026, ECO:0000269|PubMed:19570034, ECO:0000269|PubMed:22762500, ECO:0000269|PubMed:22908308, ECO:0000269|PubMed:27354378}. +Q9JKM7 RAB37_MOUSE Ras-related protein Rab-37 223 24,656 Chain (1); Initiator methionine (1); Lipidation (2); Modified residue (2); Motif (1); Nucleotide binding (3); Propeptide (1); Sequence conflict (1) SUBCELLULAR LOCATION: Cytoplasmic vesicle. Note=Secretory granules. SUBUNIT: Interacts with RIMS1. {ECO:0000269|PubMed:12578829}. TISSUE SPECIFICITY: Specifically expressed in the bone marrow mast cells. +Q8QZZ8 RAB38_MOUSE Ras-related protein Rab-38 211 23,776 Chain (1); Lipidation (2); Motif (1); Mutagenesis (2); Natural variant (1); Nucleotide binding (3); Sequence conflict (3) FUNCTION: Plays a role in the maturation of phagosomes that engulf pathogens, such as S.aureus and Mycobacterium (By similarity). May be involved in melanosomal transport and docking. Involved in the proper sorting of TYRP1. Involved in peripheral melanosomal distribution of TYRP1 in melanocytes; the function, which probably is implicating vesicle-trafficking, includes cooperation with ANKRD27 and VAMP7 (PubMed:21187289). Plays an important role in the control of melanin production and melanosome biogenesis (By similarity). In concert with RAB32, regulates the proper trafficking of melanogenic enzymes TYR, TYRP1 and DCT/TYRP2 to melanosomes in melanocytes (PubMed:26620560). {ECO:0000250|UniProtKB:P57729, ECO:0000269|PubMed:21187289, ECO:0000269|PubMed:26620560}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle, phagosome {ECO:0000250|UniProtKB:P57729}. Cytoplasmic vesicle, phagosome membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Melanosome {ECO:0000269|PubMed:26620560}. Melanosome membrane {ECO:0000250|UniProtKB:P57729}. Note=Recruited to phagosomes containing S.aureus or M.tuberculosis. The BLOC-3 complex, a heterodimer of HPS1 and HPS4 promotes its membrane localization. {ECO:0000250|UniProtKB:P57729}. SUBUNIT: Interacts with ANKRD27 (By similarity). {ECO:0000250|UniProtKB:P57729}. DISEASE: Note=Defects in Rab38 are the cause of a form of oculocutaneous albinism known as the chocolate (cht) phenotype. Mice exhibit a brown coat similar in color to mice with a mutation in tyrosinase-related protein 1 (TYRP1). The targeting of TYRP1 protein to the melanosome is impaired in Rab38(cht)/Rab38(cht) melanocytes. {ECO:0000269|PubMed:11917121}. +P62823 RAB3C_MOUSE Ras-related protein Rab-3C 227 25,872 Chain (1); Lipidation (2); Modified residue (4); Motif (1); Nucleotide binding (5) FUNCTION: Protein transport. Probably involved in vesicular traffic (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. SUBUNIT: Interacts with RIMS1, RIMS2, RPH3A and RPH3AL. {ECO:0000269|PubMed:12578829}. +P35293 RAB18_MOUSE Ras-related protein Rab-18 206 23,035 Chain (1); Lipidation (2); Modified residue (3); Motif (1); Nucleotide binding (4); Propeptide (1) FUNCTION: Plays a role in apical endocytosis/recycling. May be implicated in transport between the plasma membrane and early endosomes. Plays a key role in eye and brain development and neurodegeneration (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Basal cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Note=Highly enriched on apical endocytic structures in polarized epithelial cells of kidney proximal tubules. Detected on both the apical and basolateral domains in epithelial cells of the intestine. TISSUE SPECIFICITY: Expression is high in the brain, moderate in the pituitary, and low in the liver. Detected in all tissues. +P35294 RAB19_MOUSE Ras-related protein Rab-19 217 24,398 Chain (1); Lipidation (2); Modified residue (1); Motif (1); Nucleotide binding (3); Sequence conflict (1) SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. TISSUE SPECIFICITY: Expressed in a tissue-specific manner. Detected at high levels in intestine, lung and spleen, and at a lower level in kidney. +P56371 RAB4A_MOUSE Ras-related protein Rab-4A 218 24,409 Chain (1); Erroneous initiation (1); Lipidation (2); Modified residue (3); Motif (1); Nucleotide binding (4); Sequence conflict (1) FUNCTION: Protein transport. Probably involved in vesicular traffic (By similarity). {ECO:0000250}. PTM: Phosphorylated by CDK1 kinase during mitosis. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P20338}; Peripheral membrane protein {ECO:0000250|UniProtKB:P20338}. Cytoplasm {ECO:0000250|UniProtKB:P20338}. Early endosome membrane {ECO:0000250|UniProtKB:P05714}; Peripheral membrane protein {ECO:0000250|UniProtKB:P05714}. Recycling endosome membrane {ECO:0000250|UniProtKB:P05714}; Peripheral membrane protein {ECO:0000250|UniProtKB:P05714}. Note=Generally associated with membranes. Cytoplasmic when phosphorylated by CDK1. {ECO:0000250|UniProtKB:P20338}. SUBUNIT: Interacts (membrane-bound form) with NDRG1; the interaction involves NDRG1 in vesicular recycling of E-cadherin. Interacts with RAB11FIP1, RABEP1 and ZFYVE20. Interacts with RABEP1 and RBSN (By similarity). Interacts (in GTP-bound form) with GRIPAP1 (via N-terminus) (By similarity). Interacts with RUFY1 (PubMed:11172003). Interacts with SGSM1, SGSM2 and SGSM3 (PubMed:17509819). Does not interact with HPS4 (PubMed:20048159). {ECO:0000250|UniProtKB:P05714, ECO:0000250|UniProtKB:P20338, ECO:0000269|PubMed:11172003, ECO:0000269|PubMed:17509819, ECO:0000269|PubMed:20048159}. TISSUE SPECIFICITY: Expressed in the central nervous system, including cortex, cerebellum, midbrain and spinal cord, and in the kidney, lung, liver and spleen. {ECO:0000269|PubMed:20098723}. +P58069 RASA2_MOUSE Ras GTPase-activating protein 2 (GAP1m) 847 96,401 Chain (1); Compositional bias (1); Domain (4); Initiator methionine (1); Modified residue (2); Mutagenesis (2); Sequence conflict (1); Zinc finger (1) FUNCTION: Inhibitory regulator of the Ras-cyclic AMP pathway. Binds inositol tetrakisphosphate (IP4) and phospholipids. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}. +Q60790 RASA3_MOUSE Ras GTPase-activating protein 3 (GAP1(IP4BP)) (GapIII) (Ins P4-binding protein) 834 95,987 Chain (1); Domain (4); Initiator methionine (1); Modified residue (6); Sequence conflict (1); Zinc finger (1) FUNCTION: Inhibitory regulator of the Ras-cyclic AMP pathway. May bind inositol tetrakisphosphate (IP4). TISSUE SPECIFICITY: High levels in brain, lower in spleen and lung. +O35626 RASD1_MOUSE Dexamethasone-induced Ras-related protein 1 280 31,684 Chain (1); Lipidation (1); Modified residue (2); Motif (1); Nucleotide binding (3); Propeptide (1) FUNCTION: Small GTPase. Negatively regulates the transcription regulation activity of the APBB1/FE65-APP complex via its interaction with APBB1/FE65 (By similarity). {ECO:0000250}. PTM: S-nitrosylation stimulates guanine-nucleotide exchange activity. {ECO:0000269|PubMed:11086993}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Component of a complex, at least composed of APBB1, RASD1/DEXRAS1 and APP. Interacts with APBB1/FE65 (By similarity). Forms a ternary complex with CAPON and NOS1. {ECO:0000250, ECO:0000269|PubMed:11086993}. TISSUE SPECIFICITY: Expressed in brain, heart, kidney and liver. {ECO:0000269|PubMed:9452419}. +Q6PFQ7 RASL2_MOUSE Ras GTPase-activating protein 4 (Calcium-promoted Ras inactivator) (Ras p21 protein activator 4) (RasGAP-activating-like protein 2) 802 90,060 Alternative sequence (1); Chain (1); Domain (4); Erroneous initiation (1); Sequence conflict (3); Zinc finger (1) FUNCTION: Ca(2+)-dependent Ras GTPase-activating protein, that switches off the Ras-MAPK pathway following a stimulus that elevates intracellular calcium. Functions as an adaptor for Cdc42 and Rac1 during FcR-mediated phagocytosis. Isoform 2 activates the Ras pathway and promotes RANKL shedding by modulating the expression of MMP14. {ECO:0000269|PubMed:16041389, ECO:0000269|PubMed:16234249}. SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell membrane; Peripheral membrane protein. Note=Localized to the cytosol as a result of its lack of phosphoinositide binding activity. Upon agonist-stimulated calcium mobilization, utilizes the C2A and C2B domains to associate with the plasma membrane. DOMAIN: The PH domain does not bind phosphatidylinositol 4,5-bisphosphate or phosphatidylinositol 3,4,5-trisphosphate. This lack of binding activity is due to Leu-591, compared to Arg found in other family members (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Isoform 2 is expressed in osteoblasts. {ECO:0000269|PubMed:16234249}. +Q5RI75 RASEF_MOUSE Ras and EF-hand domain-containing protein homolog 627 70,752 Alternative sequence (1); Chain (1); Coiled coil (1); Modified residue (2); Nucleotide binding (3) FUNCTION: Binds predominantly GDP, and also GTP. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +Q7TN89 RASE_MOUSE GTPase ERas (E-Ras) (Embryonic stem cell-expressed Ras) 227 24,321 Chain (1); Lipidation (3); Modified residue (1); Motif (1); Nucleotide binding (3); Propeptide (1) FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. Plays an important role in the tumor-like growth properties of embryonic stem cells. {ECO:0000269|PubMed:12774123}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. SUBUNIT: Interacts with PIK3CD. {ECO:0000269|PubMed:12774123}. TISSUE SPECIFICITY: Expressed in several undifferentiated mouse embryonic stem cell lines. {ECO:0000269|PubMed:12774123}. +Q08AT1 RASLC_MOUSE Ras-like protein family member 12 266 29,555 Chain (1); Nucleotide binding (3); Sequence conflict (1) +Q8BMS9 RASF2_MOUSE Ras association domain-containing protein 2 326 37,973 Chain (1); Domain (2); Erroneous initiation (1) FUNCTION: Potential tumor suppressor. Acts as a KRAS-specific effector protein. May promote apoptosis and cell cycle arrest. Stabilizes STK3/MST2 by protecting it from proteasomal degradation (By similarity). {ECO:0000250}. PTM: Phosphorylated by STK3/MST2 and STK4/MST1. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P50749}. Cytoplasm {ECO:0000250|UniProtKB:P50749}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:P50749}. Note=Translocates to the cytoplasm in the presence of STK3/MST2 AND STK4/MST1. {ECO:0000250|UniProtKB:P50749}. SUBUNIT: Interacts directly with activated KRAS in a GTP-dependent manner. Interacts (via SARAH domain) with STK3/MST2 AND STK4/MST1. {ECO:0000250}. +Q9CW46 RAVR1_MOUSE Ribonucleoprotein PTB-binding 1 (Protein raver-1) 748 79,382 Alternative sequence (2); Beta strand (6); Chain (1); Compositional bias (1); Domain (3); Erroneous initiation (1); Helix (2); Initiator methionine (1); Modified residue (10); Motif (2); Region (1); Sequence conflict (2); Turn (2) FUNCTION: Cooperates with PTBP1 to modulate regulated alternative splicing events. Promotes exon skipping. Cooperates with PTBP1 to modulate switching between mutually exclusive exons during maturation of the TPM1 pre-mRNA. {ECO:0000269|PubMed:14633994}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11724819}. Cytoplasm {ECO:0000269|PubMed:11724819}. Note=Nuclear, in perinucleolar structures. Shuttles between nucleus and cytoplasm. Cytoplasm, at focal contacts and cell-cell contacts. Associated with myotubes during muscle differentiation. SUBUNIT: Interacts with PTBP1, RAVER2, VCL and ACTN1. Part of a complex containing RAVER1, VCL and ACTN1. {ECO:0000269|PubMed:11724819, ECO:0000269|PubMed:16051233}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11724819, ECO:0000269|PubMed:16051233}. +Q8CJ96 RASF8_MOUSE Ras association domain-containing protein 8 (Carcinoma-associated protein HOJ-1 homolog) 419 48,103 Chain (1); Compositional bias (1); Domain (1); Modified residue (4); Sequence conflict (1) +Q9ERI2 RB27A_MOUSE Ras-related protein Rab-27A 221 25,017 Beta strand (7); Chain (1); Disulfide bond (1); Helix (8); Initiator methionine (1); Lipidation (2); Modified residue (3); Motif (1); Mutagenesis (1); Nucleotide binding (4); Turn (2) FUNCTION: Plays a role in cytotoxic granule exocytosis in lymphocytes. Required for both granule maturation and granule docking and priming at the immunologic synapse (By similarity). {ECO:0000250|UniProtKB:P51159}. SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P51159}; Lipid-anchor {ECO:0000250|UniProtKB:P51159}. Melanosome {ECO:0000250|UniProtKB:P51159}. Late endosome {ECO:0000250|UniProtKB:P51159}. Lysosome {ECO:0000250|UniProtKB:P51159}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Localizes to endosomal exocytic vesicles. {ECO:0000250|UniProtKB:P51159}. SUBUNIT: Binds SYTL1, SYTL2, SLAC2B, MYRIP, SYTL3, SYTL4, SYTL5 and MLPH. Interacts with UNC13D. Interacts with RPH3A and RPH3A. Does not interact with the BLOC-3 complex (heterodimer of HPS1 and HPS4) (By similarity). {ECO:0000250|UniProtKB:P51159, ECO:0000269|PubMed:11773082, ECO:0000269|PubMed:11887186, ECO:0000269|PubMed:12051743, ECO:0000269|PubMed:12578829, ECO:0000269|PubMed:16716193, ECO:0000269|PubMed:18266782, ECO:0000269|PubMed:18354201, ECO:0000269|PubMed:18940603}. TISSUE SPECIFICITY: Detected in melanocytes. Expressed abundantly in the stomach and is predominantly localized at the apical region of gastric-surface mucus cells. Also expressed in the thymus and lung. {ECO:0000269|PubMed:16716193}. +P97868 RBBP6_MOUSE E3 ubiquitin-protein ligase RBBP6 (EC 2.3.2.27) (Proliferation potential-related protein) (Protein P2P-R) (RING-type E3 ubiquitin transferase RBBP6) (Retinoblastoma-binding protein 6) (p53-associated cellular protein of testis) 1790 199,587 Alternative sequence (3); Chain (1); Cross-link (2); Domain (1); Frameshift (1); Modified residue (26); Region (2); Sequence conflict (28); Zinc finger (2) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase which promotes ubiquitination of YBX1, leading to its degradation by the proteasome (By similarity). May play a role as a scaffold protein to promote the assembly of the p53/TP53-MDM2 complex, resulting in increase of MDM2-mediated ubiquitination and degradation of p53/TP53; may function as negative regulator of p53/TP53, leading to both apoptosis and cell growth retardation (PubMed:17470788). Regulates DNA-replication and common fragile sites (CFS) stability in a ZBTB38- and MCM10-dependent manner. Controls ZBTB38 protein stability and abundance via ubiquitination and proteasomal degradation, and ZBTB38 in turn negatively regulates the expression of MCM10 which plays an important role in DNA-replication (PubMed:24726359). {ECO:0000250|UniProtKB:Q7Z6E9, ECO:0000269|PubMed:17470788, ECO:0000269|PubMed:24726359}. PTM: Phosphorylated by NEK6. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus. Chromosome. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Note=Colocalizes with mitotic chromosomes. Co-localizes with NEK6 in the centrosome (By similarity). {ECO:0000250}. SUBUNIT: Interacts with MDM2 and YBX1 (By similarity). Interacts also with p53/TP53 and RB1. Interacts with NEK6 (By similarity). Interacts with ZBTB38 (By similarity). {ECO:0000250|UniProtKB:Q7Z6E9, ECO:0000269|PubMed:14566974, ECO:0000269|PubMed:9010216, ECO:0000269|PubMed:9037032}. TISSUE SPECIFICITY: Highly expressed in testis. Expressed at lower levels in brain, heart, kidney, liver, lung, skeletal muscle, spleen, thymus and tongue. {ECO:0000269|PubMed:9010216, ECO:0000269|PubMed:9037032}. +Q8BHD0 RB39A_MOUSE Ras-related protein Rab-39A (Rab-39) 217 24,978 Chain (1); Lipidation (2); Modified residue (1); Motif (1); Nucleotide binding (3) FUNCTION: Plays a role in the maturation and acidification of phagosomes that engulf pathogens, such as S.aureus and M.tuberculosis. Plays a role in vesicular trafficking. Plays a role in the fusion of phagosomes with lysosomes. Negatively regulates LPS-induced autophagosome formation in macrophages possibly by implicating PI3K (By similarity). May be involved in multiple neurite formation (PubMed:23624502). {ECO:0000250|UniProtKB:Q14964, ECO:0000269|PubMed:23624502}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle, phagosome {ECO:0000250}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Lysosome {ECO:0000250|UniProtKB:Q14964}. Note=Recruited to phagosomes containing S.aureus or Mycobacterium. {ECO:0000250}. SUBUNIT: Interacts with BECN1. Probably associates with the PI3K (PI3KC3/PI3K-III/class III phosphatidylinositol 3-kinase) complex (By similarity). Interacts with UACA. {ECO:0000250|UniProtKB:Q14964, ECO:0000269|PubMed:23624502}. +A2AWA9 RBGP1_MOUSE Rab GTPase-activating protein 1 (GAP and centrosome-associated protein) (Rab6 GTPase-activating protein GAPCenA) 1064 120,798 Alternative sequence (6); Chain (1); Coiled coil (1); Domain (2); Erroneous initiation (4); Modified residue (3); Sequence conflict (1); Site (2) FUNCTION: May act as a GTPase-activating protein of RAB6A. May play a role in microtubule nucleation by centrosome. May participate in a RAB6A-mediated pathway involved in the metaphase-anaphase transition (By similarity). {ECO:0000250|UniProtKB:Q9Y3P9}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9Y3P9}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9Y3P9}. Note=Predominantly cytosolic but also associated with the centrosome. {ECO:0000250|UniProtKB:Q9Y3P9}. SUBUNIT: Interacts with RAB6A and tubulin gamma. {ECO:0000250|UniProtKB:Q9Y3P9}. DOMAIN: The arginine and glutamine fingers are critical for the GTPase-activating mechanism, they pull out Rab's 'switch 2' glutamine and insert in Rab's active site. {ECO:0000250}. +Q9WV02 RBMX_MOUSE RNA-binding motif protein, X chromosome (Heterogeneous nuclear ribonucleoprotein G) (hnRNP G) [Cleaved into: RNA-binding motif protein, X chromosome, N-terminally processed] 391 42,301 Alternative sequence (1); Chain (2); Compositional bias (2); Cross-link (3); Domain (1); Initiator methionine (1); Modified residue (18) FUNCTION: RNA-binding protein that plays several role in the regulation of pre- and post-transcriptional processes. Implicated in tissue-specific regulation of gene transcription and alternative splicing of several pre-mRNAs. Binds to and stimulates transcription from the tumor suppressor TXNIP gene promoter; may thus be involved in tumor suppression. When associated with SAFB, binds to and stimulates transcription from the SREBF1 promoter. Associates with nascent mRNAs transcribed by RNA polymerase II. Component of the supraspliceosome complex that regulates pre-mRNA alternative splice site selection. Can either activate or suppress exon inclusion; acts additively with TRA2B to promote exon 7 inclusion of the survival motor neuron SMN2. Represses the splicing of MAPT/Tau exon 10. Binds preferentially to single-stranded 5'-CC[A/C]-rich RNA sequence motifs localized in a single-stranded conformation; probably binds RNA as a homodimer. Binds non-specifically to pre-mRNAs. Plays also a role in the cytoplasmic TNFR1 trafficking pathways; promotes both the IL-1-beta-mediated inducible proteolytic cleavage of TNFR1 ectodomains and the release of TNFR1 exosome-like vesicles to the extracellular compartment. {ECO:0000269|PubMed:17188681, ECO:0000269|PubMed:19403048}. PTM: O-glycosylated. {ECO:0000250}.; PTM: Arg-182 is dimethylated, probably to asymmetric dimethylarginine. SUBCELLULAR LOCATION: Nucleus. Note=Localizes in numerous small granules in the nucleus (By similarity). Component of ribonucleosomes. {ECO:0000250}. SUBUNIT: Homomultimer. Found in the supraspliceosome complex. Identified in the spliceosome C complex. Interacts with KHDRBS3. Forms a complex with ILF2, ILF3, YLPM1, KHDRBS1, NCOA5 and PPP1CA Interacts with CLK2, KHDRBS2, SAFB, TRA2B and YTHDC1. Interacts with ERAP1; the interaction is RNA-independent (By similarity). Interacts with SAFB/SAFB1. {ECO:0000250, ECO:0000269|PubMed:19403048}. DOMAIN: The RRM domain is necessary for RNA-binding, but not for splice site selection, indicating that its splicing activity does not require direct binding to RNA. {ECO:0000250}. TISSUE SPECIFICITY: Both isoforms are widely expressed. {ECO:0000269|PubMed:10391207}. +Q62172 RBP1_MOUSE RalA-binding protein 1 (RalBP1) (Dinitrophenyl S-glutathione ATPase) (DNP-SG ATPase) (Ral-interacting protein 1) 648 75,043 Chain (1); Compositional bias (1); Domain (1); Initiator methionine (1); Modified residue (12); Region (1); Sequence conflict (3) FUNCTION: Can activate specifically hydrolysis of GTP bound to RAC1 and CDC42, but not RALA. Mediates ATP-dependent transport of S-(2,4-dinitrophenyl)-glutathione (DNP-SG) and doxorubicin (DOX) and is the major ATP-dependent transporter of glutathione conjugates of electrophiles (GS-E) and DOX in erythrocytes. Can catalyze transport of glutathione conjugates and xenobiotics, and may contribute to the multidrug resistance phenomenon. Serves as a scaffold protein that brings together proteins forming an endocytotic complex during interphase and also with CDK1 to switch off endocytosis, One of its substrates would be EPN1/Epsin (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. SUBUNIT: Interacts with the GTP-bound form of RALA, RALB, CDC42 and RAC1. Interacts with REPS1 and REPS2 and this does not affect the Ral-binding activity. Interacts with DAB2IP. Interacts with catalytically active CCNB1 and CDK1 during mitosis. Interacts with EPN1, NUMB and TFAP2A during interphase and mitosis (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. The highest level of expression was observed in ovaries and skeletal muscle, whereas the lowest was found in spleen, liver and peripheral blood leukocytes. +Q62176 RBM38_MOUSE RNA-binding protein 38 (RNA-binding motif protein 38) (RNA-binding region-containing protein 1) (ssDNA-binding protein SEB4) 237 25,364 Chain (1); Domain (1); Sequence conflict (2) FUNCTION: RNA-binding protein that specifically bind the 3'-UTR of CDKN1A transcripts, leading to maintain the stability of CDKN1A transcripts, thereby acting as a mediator of the p53/TP53 family to regulate CDKN1A. CDKN1A is a cyclin-dependent kinase inhibitor transcriptionally regulated by the p53/TP53 family to induce cell cycle arrest. Has the ability to induce cell cycle arrest in G1 and maintain the stability of CDKN1A transcripts induced by p53/TP53. Also acts as a mRNA splicing factor. Specifically regulates the expression of FGFR2-IIIb, an epithelial cell-specific isoform of FGFR2 (By similarity). Plays a role in myogenic differentiation. {ECO:0000250, ECO:0000269|PubMed:19817877}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Nucleus {ECO:0000250}. TISSUE SPECIFICITY: Expressed in cardiac and skeletal muscle tissues. {ECO:0000269|PubMed:19817877}. +Q8R4X3 RBM12_MOUSE RNA-binding protein 12 (RNA-binding motif protein 12) (SH3/WW domain anchor protein in the nucleus) (SWAN) 992 102,796 Beta strand (5); Chain (1); Compositional bias (2); Domain (3); Erroneous initiation (1); Helix (2); Modified residue (6); Sequence conflict (35); Turn (3) SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +Q9D8M4 RL7L_MOUSE 60S ribosomal protein L7-like 1 246 28,544 Chain (1); Modified residue (1) +Q9JHG6 RCAN1_MOUSE Calcipressin-1 (Down syndrome critical region protein 1 homolog) (Myocyte-enriched calcineurin-interacting protein 1) (MCIP1) (Regulator of calcineurin 1) 251 28,137 Alternative sequence (3); Beta strand (5); Chain (1); Compositional bias (1); Erroneous initiation (1); Helix (3); Modified residue (3); Sequence conflict (4); Turn (2) FUNCTION: Inhibits calcineurin-dependent transcriptional responses by binding to the catalytic domain of calcineurin A. Could play a role during central nervous system development (PubMed:11231093). {ECO:0000269|PubMed:11231093}. PTM: Phosphorylation increases its ability to inhibit calcineurin and decreases protein half-life. {ECO:0000250|UniProtKB:P53805}. SUBUNIT: Interacts with RAF1 and PPP3R1 (By similarity). Interacts with PPP3CA (PubMed:12809556). {ECO:0000250|UniProtKB:P53805, ECO:0000269|PubMed:12809556}. TISSUE SPECIFICITY: Highly expressed in heart and skeletal muscle. Also expressed in all other tissues. {ECO:0000269|PubMed:11231093, ECO:0000269|PubMed:12809556}. +Q8BK67 RCC2_MOUSE Protein RCC2 520 55,983 Chain (1); Modified residue (13); Region (1); Repeat (7) FUNCTION: Multifunctional protein that may effect its functions by regulating the activity of small GTPases, such as RAC1 and RALA. Required for normal progress through the cell cycle, both during interphase and during mitosis. Required for the presence of normal levels of MAD2L1, AURKB and BIRC5 on inner centromeres during mitosis, and for normal attachment of kinetochores to mitotic spindles. Required for normal organization of the microtubule cytoskeleton in interphase cells. Functions as guanine nucleotide exchange factor (GEF) for RALA. Interferes with the activation of RAC1 by guanine nucleotide exchange factors (By similarity). Prevents accumulation of active, GTP-bound RAC1, and suppresses RAC1-mediated reorganization of the actin cytoskeleton and formation of membrane protrusions (PubMed:25074804). Required for normal cellular responses to contacts with the extracellular matrix of adjacent cells, and for directional cell migration in response to a fibronectin gradient (in vitro) (By similarity). {ECO:0000250|UniProtKB:Q9P258, ECO:0000269|PubMed:25074804}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9P258}. Nucleus {ECO:0000250|UniProtKB:Q9P258}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9P258}. Chromosome, centromere {ECO:0000250|UniProtKB:Q9P258}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9P258}. Chromosome {ECO:0000250|UniProtKB:Q9P258}. Midbody {ECO:0000250|UniProtKB:Q9P258}. Cell membrane {ECO:0000250|UniProtKB:Q9P258}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9P258}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9P258}. Note=Appears in the nucleus at G2, then concentrates at the inner centromere region of chromosomes during prophase. Redistributes to the midzone of the mitotic spindle during anaphase. Here, the protein covers the entire equatorial diameter from cortex to cortex. Colocalizes with cytoplasmic microtubules in interphase cells. Colocalizes with RAC1 at the cell membrane. {ECO:0000250|UniProtKB:Q9P258}. SUBUNIT: Interacts with RAC1 (PubMed:25074804). Interacts with nucleotide-free and with GDP and GTP-bound forms of RAC1, with a slight preference for GDP-bound RAC1. Binds preferentially to the nucleotide-free form of RAC1. Interacts with CORO1C. Interacts with microtubules (By similarity). {ECO:0000250|UniProtKB:Q9P258, ECO:0000269|PubMed:25074804}. +Q6NXM2 RCBT1_MOUSE RCC1 and BTB domain-containing protein 1 (Regulator of chromosome condensation and BTB domain-containing protein 1) 531 58,379 Chain (1); Domain (2); Repeat (6); Sequence conflict (3) FUNCTION: May be involved in cell cycle regulation by chromatin remodeling. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: In the retina, mainly expressed in the inner retina with strong signals reaching up to the outer plexiform layer (at protein level). {ECO:0000269|PubMed:27486781}. +Q9WTZ1 RBX2_MOUSE RING-box protein 2 (Rbx2) (RING finger protein 7) (Sensitive to apoptosis gene protein) 113 12,707 Chain (1); Initiator methionine (1); Metal binding (12); Modified residue (1); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: Probable component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins involved in cell cycle progression, signal transduction and transcription (By similarity). CRLs complexes and ARIH1 collaborate in tandem to mediate ubiquitination of target proteins, ARIH1 mediating addition of the first ubiquitin on CRLs targets (By similarity). Through the RING-type zinc finger, seems to recruit the E2 ubiquitination enzyme to the complex and brings it into close proximity to the substrate. Promotes the neddylation of CUL5 via its interaction with UBE2F. May play a role in protecting cells from apoptosis induced by redox agents (By similarity). {ECO:0000250|UniProtKB:P62877, ECO:0000250|UniProtKB:Q9UBF6}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Probable part of SCF complexes, which consist of SKP1, CUL1, RNF7/RBX2 and a F-box protein. Interacts (preferentially) with CUL5. Also interacts (with lower preference) with CUL1, CUL2, CUL3, CUL4A and CUL4B. Interacts with UBE2F (By similarity). {ECO:0000250}. DOMAIN: The RING-type zinc finger domain is essential for ubiquitin ligase activity. It coordinates an additional third zinc ion. +Q05186 RCN1_MOUSE Reticulocalbin-1 325 38,113 Calcium binding (6); Chain (1); Domain (6); Glycosylation (1); Modified residue (2); Motif (1); Sequence conflict (3); Signal peptide (1) FUNCTION: May regulate calcium-dependent activities in the endoplasmic reticulum lumen or post-ER compartment. PTM: O-glycosylated. O-mannosylated by POMT1 and POMT2 and elongated by POMGNT1. {ECO:0000250|UniProtKB:Q15293}. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. +P54728 RD23B_MOUSE UV excision repair protein RAD23 homolog B (HR23B) (mHR23B) (XP-C repair-complementing complex 58 kDa protein) (p58) 416 43,513 Chain (1); Compositional bias (3); Domain (4); Helix (6); Modified residue (6); Sequence conflict (8) FUNCTION: Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Binds to polyubiquitin chains. Proposed to be capable to bind simultaneously to the 26S proteasome and to polyubiquitinated substrates and to deliver ubiquitinated proteins to the proteasome. May play a role in endoplasmic reticulum-associated degradation (ERAD) of misfolded glycoproteins by association with PNGase and delivering deglycosylated proteins to the proteasome. {ECO:0000269|PubMed:12815074, ECO:0000269|PubMed:15336624, ECO:0000269|PubMed:16709668}.; FUNCTION: Involved in global genome nucleotide excision repair (GG-NER) by acting as component of the XPC complex. Cooperatively with Cetn2 appears to stabilize Xpc. May protect Xpc from proteasomal degradation (By similarity). {ECO:0000250}.; FUNCTION: The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, Xpa, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. In vitro, the Xpc:Rad23b dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts. Xpc:Rad23b contacts DNA both 5' and 3' of a cisplatin lesion with a preference for the 5' side. Xpc:Rad23bB induces a bend in DNA upon binding. Xpc:Rad23b stimulates the activity of DNA glycosylases Tdg and Smug1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15336624}. Cytoplasm {ECO:0000269|PubMed:15336624}. SUBUNIT: Component of the XPC complex composed of XPC, RAD23B and CETN2. Interacts with NGLY1 and PSMC1. Interacts with ATXN3 (By similarity). Interacts with AMFR. Interacts with VCP; the interaction is indirect and mediated by NGLY1. {ECO:0000250, ECO:0000269|PubMed:11562482, ECO:0000269|PubMed:15358861, ECO:0000269|PubMed:16249333, ECO:0000269|PubMed:16500903, ECO:0000269|PubMed:16709668}. +Q8CE46 PUS7L_MOUSE Pseudouridylate synthase 7 homolog-like protein (EC 5.4.99.-) 702 79,197 Active site (1); Chain (1); Domain (1); Modified residue (1); Sequence caution (1); Sequence conflict (3) FUNCTION: Pseudouridylate synthase that catalyzes pseudouridylation of RNAs. {ECO:0000250|UniProtKB:Q96PZ0}. +P35288 RAB23_MOUSE Ras-related protein Rab-23 (Protein open brain) (Rab-15) 237 26,678 Beta strand (7); Chain (1); Helix (8); Lipidation (1); Modified residue (3); Motif (1); Nucleotide binding (3); Propeptide (1); Turn (1) FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (By similarity). Plays a role in autophagic vacuole assembly, and mediates defense against pathogens, such as S.aureus, by promoting their capture by autophagosomes that then merge with lysosomes (By similarity). Together with SUFU, prevents nuclear import of GLI1, and thereby inhibits GLI1 transcription factor activity. Regulates GLI1 in differentiating chondrocytes. Likewise, regulates GLI3 proteolytic processing and modulates GLI2 and GLI3 transcription factor activity. {ECO:0000250, ECO:0000269|PubMed:11071781, ECO:0000269|PubMed:11449277, ECO:0000269|PubMed:16364285, ECO:0000269|PubMed:18218620, ECO:0000269|PubMed:7720556}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14617350}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000269|PubMed:14617350}. Cytoplasm {ECO:0000269|PubMed:14617350}. Endosome membrane {ECO:0000269|PubMed:14617350}. Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:Q9ULC3}. Cytoplasmic vesicle, phagosome {ECO:0000305}. Cytoplasmic vesicle, phagosome membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Recruited to phagosomes containing S.aureus or Mycobacterium. {ECO:0000250|UniProtKB:Q9ULC3}. SUBUNIT: Interacts with SUFU. {ECO:0000250}. TISSUE SPECIFICITY: Detected in brain neurons (at protein level). Forebrain and midbrain. {ECO:0000269|PubMed:14617350, ECO:0000269|PubMed:16463280}. DISEASE: Note=Defects in Rab23 are the cause of the open brain phenotype. Mice suffer from exencephaly and severe malformations of the spinal cord and the dorsal root ganglia, leading to complete embryonic lethality. In addition, mice display poorly developed eyes and polydactyly. +P61514 RL37A_MOUSE 60S ribosomal protein L37a 92 10,275 Chain (1); Zinc finger (1) +Q504M8 RAB26_MOUSE Ras-related protein Rab-26 260 28,619 Chain (1); Lipidation (2); Motif (1); Nucleotide binding (4) FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. Mediates transport of ADRA2A and ADRA2B from the Golgi to the cell membrane. Plays a role in the maturation of zymogenic granules and in pepsinogen secretion in the stomach (By similarity). Plays a role in the secretion of amylase from acinar granules in the parotid gland. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000305|PubMed:20038531}; Lipid-anchor {ECO:0000305|PubMed:20038531}; Cytoplasmic side {ECO:0000305|PubMed:20038531}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9ULW5}; Lipid-anchor {ECO:0000250|UniProtKB:Q9ULW5}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9ULW5}. Note=Not localized at the plasma membrane (By similarity). Inhibition of S-geranylgeranyl cysteine formation abolishes membrane location. {ECO:0000250|UniProtKB:P51156}. SUBUNIT: Interacts with ADRA2B (By similarity). Interacts with RIMS1. {ECO:0000250, ECO:0000269|PubMed:12578829}. TISSUE SPECIFICITY: Detected in zymogenic cells in the stomach. {ECO:0000269|PubMed:20038531}. +P35283 RAB12_MOUSE Ras-related protein Rab-12 (Rab-13) 243 27,329 Chain (1); Lipidation (2); Modified residue (5); Motif (1); Mutagenesis (1); Nucleotide binding (4); Sequence conflict (3) FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (By similarity). That Rab may play a role in protein transport from recycling endosomes to lysosomes regulating, for instance, the degradation of the transferrin receptor. Involved in autophagy. {ECO:0000250, ECO:0000269|PubMed:21718402, ECO:0000269|PubMed:23357852}. SUBCELLULAR LOCATION: Recycling endosome membrane {ECO:0000269|PubMed:21718402}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Lysosome membrane {ECO:0000269|PubMed:21718402}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P51152}. Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:23357852}. SUBUNIT: Interacts with RABIF and OPTN. {ECO:0000269|PubMed:23357852}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:21718402}. +Q8CAM5 RAB36_MOUSE Ras-related protein Rab-36 267 29,776 Chain (1); Lipidation (2); Motif (1); Nucleotide binding (3) FUNCTION: Protein transport. Probably involved in vesicular traffic (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane; Lipid-anchor. +Q923S9 RAB30_MOUSE Ras-related protein Rab-30 203 23,058 Chain (1); Lipidation (2); Modified residue (1); Motif (1); Nucleotide binding (3); Propeptide (1); Sequence conflict (1) FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (By similarity). Required for maintaining the structural integrity of the Golgi apparatus, possibly by mediating interactions with cytoplasmic scaffolding proteins (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Cytoplasm {ECO:0000250}. Golgi apparatus {ECO:0000250}. +P63011 RAB3A_MOUSE Ras-related protein Rab-3A 220 24,970 Chain (1); Lipidation (2); Modified residue (3); Motif (1); Nucleotide binding (5) FUNCTION: Involved in exocytosis by regulating a late step in synaptic vesicle fusion. Could play a role in neurotransmitter release by regulating membrane flow in the nerve terminal (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. SUBUNIT: Heterodimer with RIMS2. Part of a ternary complex involving PCLO and EPAC2. Interacts with RPH3A and RPH3AL. Interacts with the exocyst complex through SEC15. Binds SYTL4, RIMS1 and RIMS2. Interacts with RAB3IP. Interacts with SGSM1 and SGSM3. {ECO:0000269|PubMed:11056535, ECO:0000269|PubMed:11431472, ECO:0000269|PubMed:12401793, ECO:0000269|PubMed:12578829, ECO:0000269|PubMed:12590134, ECO:0000269|PubMed:17509819}. +P61021 RAB5B_MOUSE Ras-related protein Rab-5B 215 23,707 Chain (1); Initiator methionine (1); Lipidation (2); Modified residue (1); Motif (1); Nucleotide binding (5); Sequence conflict (1) FUNCTION: Protein transport. Probably involved in vesicular traffic (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. Early endosome membrane; Lipid-anchor. Melanosome {ECO:0000250}. SUBUNIT: Binds EEA1. Interacts with RIN2 and RIN3, which probably regulate its pathway, possibly by acting as GEFs (By similarity). {ECO:0000250}. +Q9CQT9 RAB5I_MOUSE Uncharacterized protein RAB5IF homolog (Rab5-interacting protein) (RIP5) 129 14,825 Chain (1) +Q9D4V7 RABL3_MOUSE Rab-like protein 3 236 26,298 Alternative sequence (1); Chain (1); Nucleotide binding (3); Region (1); Sequence conflict (1) +Q9CQD1 RAB5A_MOUSE Ras-related protein Rab-5A 215 23,599 Chain (1); Lipidation (2); Motif (1); Mutagenesis (2); Nucleotide binding (5); Sequence conflict (2) FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. RAB5A is required for the fusion of plasma membranes and early endosomes. Contributes to the regulation of filopodia extension. Required for the exosomal release of SDCBP, CD63, PDCD6IP and syndecan (By similarity). Regulates maturation of apoptotic cell-containing phagosomes, probably downstream of DYN2 and PIK3C3 (PubMed:18425118). {ECO:0000250|UniProtKB:P18066, ECO:0000250|UniProtKB:P20339, ECO:0000269|PubMed:18425118}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P20339}; Lipid-anchor {ECO:0000250|UniProtKB:P20339}; Cytoplasmic side {ECO:0000250|UniProtKB:P18066}. Early endosome membrane {ECO:0000250|UniProtKB:P20339}; Lipid-anchor {ECO:0000250|UniProtKB:P20339}. Melanosome {ECO:0000269|PubMed:25869668}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:P20339}. Cell projection, ruffle {ECO:0000250|UniProtKB:P18066}. Membrane {ECO:0000250|UniProtKB:P20339}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P20339}. Cytoplasmic vesicle, phagosome membrane {ECO:0000269|PubMed:18425118}. Endosome membrane {ECO:0000250|UniProtKB:P20339}. Note=Enriched in stage I melanosomes. Alternates between membrane-bound and cytosolic forms. {ECO:0000250|UniProtKB:P20339}. SUBUNIT: Interacts with GDI1; this promotes dissociation from membranes. Interacts with EEA1. Interacts with RIN1 and GAPVD1, which regulate its pathway, probably by acting as a GEF. Interacts with RINL. Interacts with ALS2CL, SUN2, ZFYVE20 and RUFY1. Interacts with RABEP1; one RABEP1 homodimer binds two RAB5A chains, but at opposite sides of the dimer (By similarity). Interacts with SGSM1 and SGSM3 (PubMed:17509819). Interacts with PIK3CB (PubMed:21059846). Interacts with OCRL and INPP5F (PubMed:25869668). May be a component of a complex composed of RAB5A, DYN2 and PIK3C3 (PubMed:18425118). Does not interact with BLOC-3 complex (heterodimer of HPS1 and HPS4). Interacts with CLN5 (By similarity). {ECO:0000250|UniProtKB:P18066, ECO:0000250|UniProtKB:P20339, ECO:0000269|PubMed:17509819, ECO:0000269|PubMed:21059846, ECO:0000269|PubMed:25869668, ECO:0000305|PubMed:18425118}. +P62965 RABP1_MOUSE Cellular retinoic acid-binding protein 1 (Cellular retinoic acid-binding protein I) (CRABP-I) 137 15,592 Beta strand (10); Chain (1); Helix (2); Motif (1); Region (1) FUNCTION: Cytosolic CRABPs may regulate the access of retinoic acid to the nuclear retinoic acid receptors. SUBCELLULAR LOCATION: Cytoplasm. DOMAIN: Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior. +P35295 RAB20_MOUSE Ras-related protein Rab-20 233 25,989 Chain (1); Lipidation (2); Motif (1); Nucleotide binding (3) FUNCTION: Plays a role in apical endocytosis/recycling. Plays a role in the maturation and acidification of phagosomes that engulf pathogens, such as S.aureus and Mycobacterium. Plays a role in the fusion of phagosomes with lysosomes (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, phagosome {ECO:0000250|UniProtKB:Q9NX57}. Cytoplasmic vesicle, phagosome membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Golgi apparatus {ECO:0000250|UniProtKB:Q9NX57}. Note=Recruited to phagosomes containing S.aureus or Mycobacterium (By similarity). Highly enriched on apical endocytic structures in polarized epithelial cells of kidney proximal tubules (PubMed:7706395). {ECO:0000250|UniProtKB:Q9NX57, ECO:0000269|PubMed:7706395}. TISSUE SPECIFICITY: Present in a variety of tissues, but not in brain. +P62892 RL39_MOUSE 60S ribosomal protein L39 51 6,407 Chain (1) SUBUNIT: Interacts with IMPACT (PubMed:22404850). {ECO:0000269|PubMed:22404850}. +P68040 RACK1_MOUSE Receptor of activated protein C kinase 1 (12-3) (Guanine nucleotide-binding protein subunit beta-2-like 1) (Receptor for activated C kinase) (Receptor of activated protein kinase C 1) (p205) [Cleaved into: Receptor of activated protein C kinase 1, N-terminally processed (Guanine nucleotide-binding protein subunit beta-2-like 1, N-terminally processed)] 317 35,077 Chain (2); Frameshift (1); Initiator methionine (1); Modified residue (14); Repeat (7); Sequence conflict (8) FUNCTION: Scaffolding protein involved in the recruitment, assembly and/or regulation of a variety of signaling molecules. Interacts with a wide variety of proteins and plays a role in many cellular processes. Component of the 40S ribosomal subunit involved in translational repression. Involved in the initiation of the ribosome quality control (RQC), a pathway that takes place when a ribosome has stalled during translation, by promoting ubiquitination of a subset of 40S ribosomal subunits (By similarity). Binds to and stabilizes activated protein kinase C (PKC), increasing PKC-mediated phosphorylation. May recruit activated PKC to the ribosome, leading to phosphorylation of EIF6. Inhibits the activity of SRC kinases including SRC, LCK and YES1. Inhibits cell growth by prolonging the G0/G1 phase of the cell cycle. Enhances phosphorylation of BMAL1 by PRKCA and inhibits transcriptional activity of the BMAL1-CLOCK heterodimer. Facilitates ligand-independent nuclear translocation of AR following PKC activation, represses AR transactivation activity and is required for phosphorylation of AR by SRC. Modulates IGF1R-dependent integrin signaling and promotes cell spreading and contact with the extracellular matrix. Involved in PKC-dependent translocation of ADAM12 to the cell membrane. Promotes the ubiquitination and proteasome-mediated degradation of proteins such as CLEC1B and HIF1A. Required for VANGL2 membrane localization, inhibits Wnt signaling, and regulates cellular polarization and oriented cell division during gastrulation. Required for PTK2/FAK1 phosphorylation and dephosphorylation. Regulates internalization of the muscarinic receptor CHRM2. Promotes apoptosis by increasing oligomerization of BAX and disrupting the interaction of BAX with the anti-apoptotic factor BCL2L. Inhibits TRPM6 channel activity. Regulates cell surface expression of some GPCRs such as TBXA2R. Plays a role in regulation of FLT1-mediated cell migration. Involved in the transport of ABCB4 from the Golgi to the apical bile canalicular membrane (By similarity). {ECO:0000250|UniProtKB:P63244, ECO:0000269|PubMed:18258429, ECO:0000269|PubMed:20093473, ECO:0000269|PubMed:7968370}. PTM: Phosphorylated on Tyr-228 and/or Tyr-246 by SRC. This is required for binding to SRC (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P63244}; Peripheral membrane protein {ECO:0000250|UniProtKB:P63244}. Cytoplasm {ECO:0000269|PubMed:20093473}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P63244}. Nucleus {ECO:0000269|PubMed:20093473}. Perikaryon {ECO:0000269|PubMed:16414032}. Cell projection, dendrite {ECO:0000269|PubMed:16414032}. Note=Recruited to the plasma membrane through interaction with KRT1 which binds to membrane-bound ITGB1. PKC activation induces translocation from the perinuclear region to the cell periphery (By similarity). In the brain, detected mainly in cell bodies and dendrites with little expression in axonal fibers or nuclei (PubMed:16414032). {ECO:0000250|UniProtKB:P63244, ECO:0000269|PubMed:16414032}. SUBUNIT: Monomer; also forms homodimers and homooligomers (By similarity). Interacts with CPNE3 (By similarity). May interact with ABCB4 (By similarity). Component of the small (40S) ribosomal subunit. Interacts with LARP4B. Interacts with LARP4. Interacts with PKD2L1 (By similarity). Binds SLC9A3R1. Forms a ternary complex with TRIM63 and PRKCE. Interacts with HABP4, KRT1 and OTUB1. Interacts with SRC (via SH2 domain); the interaction is enhanced by tyrosine phosphorylation of RACK1. Recruited in a circadian manner into a nuclear complex which also includes BMAL1 and PRKCA. Interacts with AR. Interacts with IGF1R but not with INSR. Interacts with ADAM12. Interacts with CLEC1B (via N-terminal region) and with HIF1A; the interaction promotes their degradation. Interacts with RHOA; this enhances RHOA activation and promotes cell migration. Interacts with CHRM2; the interaction regulates CHRM2 internalization. Interacts with TRPM6 (via kinase domain). Interacts with PTK2/FAK1; required for PTK2/FAK1 phosphorylation and dephosphorylation. Interacts with FLT1. Interacts with HRAS. {ECO:0000250, ECO:0000250|UniProtKB:P63244, ECO:0000269|PubMed:18258429, ECO:0000269|PubMed:20093473, ECO:0000269|PubMed:21262816}. DOMAIN: The 7 WD repeats mediate protein-protein interactions with binding partners. {ECO:0000250|UniProtKB:P63244}. TISSUE SPECIFICITY: Strongly and ubiquitously expressed in the embryonic and early postnatal brain. At E11.5, expressed in a high-dorsal to low-ventral gradient throughout the brain. At E13.5, most abundant in the telecephalon. At E18.5, expressed most abundantly in layers 1-4 of the cortex, striatum, hippocampus, dentate gyrus, and specific thalamic nuclei. This expression decreases during postnatal development and is localized in the dentate gyrus, habenula, piriform cortex, paraventricular nucleus of the hypothalamus and supraoptic nucleus of the adult brain. {ECO:0000269|PubMed:16414032, ECO:0000269|PubMed:7968370}. +Q62151 RAGE_MOUSE Advanced glycosylation end product-specific receptor (Receptor for advanced glycosylation end products) 402 42,654 Alternative sequence (20); Chain (1); Disulfide bond (4); Domain (3); Glycosylation (2); Modified residue (2); Sequence conflict (7); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 341 361 Helical. {ECO:0000255}. TOPO_DOM 23 340 Extracellular. {ECO:0000255}.; TOPO_DOM 362 402 Cytoplasmic. {ECO:0000255}. FUNCTION: Mediates interactions of advanced glycosylation end products (AGE). These are nonenzymatically glycosylated proteins which accumulate in vascular tissue in aging and at an accelerated rate in diabetes. Acts as a mediator of both acute and chronic vascular inflammation in conditions such as atherosclerosis and in particular as a complication of diabetes. AGE/RAGE signaling plays an important role in regulating the production/expression of TNF-alpha, oxidative stress, and endothelial dysfunction in type 2 diabetes. Interaction with S100A12 on endothelium, mononuclear phagocytes, and lymphocytes triggers cellular activation, with generation of key proinflammatory mediators. Interaction with S100B after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling. Can also bind oligonucleotides. Receptor for amyloid beta peptide. Contributes to the translocation of amyloid-beta peptide (ABPP) across the cell membrane from the extracellular to the intracellular space in cortical neurons. ABPP-initiated RAGE signaling, especially stimulation of p38 mitogen-activated protein kinase (MAPK), has the capacity to drive a transport system delivering ABPP as a complex with RAGE to the intraneuronal space. RAGE-dependent signaling in microglia contributes to neuroinflammation, amyloid accumulation, and impaired learning/memory in a mouse model of Alzheimer disease. {ECO:0000269|PubMed:10399917, ECO:0000269|PubMed:18539754, ECO:0000269|PubMed:19901339, ECO:0000269|PubMed:19906677}.; FUNCTION: Isoform 2: Is able to advanced glycosylation end product (AGE)-induce nuclear factor NF-kappa-B activation. {ECO:0000269|PubMed:16503878}.; FUNCTION: Isoform 10: Down-regulates receptor for advanced glycosylation end products (RAGE)-ligand induced signaling through various MAPK pathways including ERK1/2, p38 and SAPK/JNK. Significantly affects tumor cell properties through decreasing cell migration, invasion, adhesion and proliferation, and increasing cellular apoptosis. Exhibits drastic inhibition on tumorigenesis in vitro. {ECO:0000269|PubMed:24260107}. SUBCELLULAR LOCATION: Isoform 1: Membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Isoform 2: Secreted {ECO:0000269|PubMed:16503878}.; SUBCELLULAR LOCATION: Isoform 10: Cell membrane {ECO:0000269|PubMed:24260107}; Single-pass membrane protein {ECO:0000255}. SUBUNIT: Interacts with S100B, S100A1 and S100A14. Constitutive homodimer; disulfide-linked (By similarity). Interacts with S100A12 and APP. {ECO:0000250, ECO:0000269|PubMed:10399917, ECO:0000269|PubMed:19901339}. TISSUE SPECIFICITY: Isoform 1: Expressed at higher levels in the coronary arterioles in type 2 diabetic mice (at protein level). Endothelial cells (PubMed:18539754). Expressed in lung, kidney, brain and heart. Most prevalent isoform with the highest level in heart (PubMed:19164451). Isoform 2: Expressed in brain, lung, kidney and small intestine with the highest level in lung. Expressed in brain, lung, kidney and small intestine with the highest level in small intestine (at protein level). Detected in neurons of the cerebrum, bronchial epithelium, endothelial cells, tubular cells of kidney and epithelial cells of small intestine (at protein level). Expression is increased in the kidney of diabetic wild-type mice (at protein level), but not in the other tissues (PubMed:16503878). Expressed only in kidney. Expression is increased in the kidney of diabetic mice (PubMed:19164451). Isoform 3: Expressed in lung, kidney and heart. The second most prevalent isoform with the highest level in lung. Not expressed in brain (PubMed:19164451). Isoform 4: Expressed at very low level in lung only (PubMed:19164451). Isoform 5: Expressed at very low level in lung only (PubMed:19164451). Isoform 6: Expressed at very low level in lung only (PubMed:19164451). Isoform 7: Expressed at very low level in heart only (PubMed:19164451). Isoform 8: Expressed at very low level in lung only (PubMed:19164451). Isoform 9: Expressed at very low level in heart only (PubMed:19164451). Isoform 10: Expressed in lung, brain, heart and kidney with a very high level in kidney (PubMed:24260107). Isoform 11: Expressed in brain, kidney and heart. Not expressed in lung (PubMed:19164451). Isoform 12: Expressed at very low level in lung and kidney (PubMed:19164451). Isoform 13: Expressed at very low level in lung only (PubMed:19164451). {ECO:0000269|PubMed:16503878, ECO:0000269|PubMed:18539754, ECO:0000269|PubMed:19164451, ECO:0000269|PubMed:24260107}. +Q9JIW9 RALB_MOUSE Ras-related protein Ral-B 206 23,349 Chain (1); Lipidation (1); Modified residue (1); Motif (1); Nucleotide binding (4); Propeptide (1) FUNCTION: Multifunctional GTPase involved in a variety of cellular processes including gene expression, cell migration, cell proliferation, oncogenic transformation and membrane trafficking. Accomplishes its multiple functions by interacting with distinct downstream effectors. Acts as a GTP sensor for GTP-dependent exocytosis of dense core vesicles (By similarity). Required both to stabilize the assembly of the exocyst complex and to localize functional exocyst complexes to the leading edge of migrating cells (By similarity). Required for suppression of apoptosis (By similarity). In late stages of cytokinesis, upon completion of the bridge formation between dividing cells, mediates exocyst recruitment to the midbody to drive abscission (By similarity). {ECO:0000250|UniProtKB:P11234, ECO:0000250|UniProtKB:P36860}. PTM: Prenylation is essential for membrane localization. {ECO:0000250|UniProtKB:P11234}.; PTM: The farnesylated form confers resistance to the proapoptotic and anti-anchorage-dependent growth effects of some geranylgeranyltransferase I inhibitors. {ECO:0000250|UniProtKB:P11234}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P11234}; Lipid-anchor {ECO:0000250|UniProtKB:P11234}; Cytoplasmic side {ECO:0000250|UniProtKB:P11234}. Midbody {ECO:0000250|UniProtKB:P11234}. Note=During late cytokinesis, enriched at the midbody. {ECO:0000250|UniProtKB:P11234}. SUBUNIT: Interacts with EXOC2/Sec5 and EXOC8/Exo84 (By similarity). Interacts (via effector domain) with RALBP1 (By similarity). {ECO:0000250|UniProtKB:P11234}. +P46061 RAGP1_MOUSE Ran GTPase-activating protein 1 (RanGAP1) 589 63,531 Chain (1); Compositional bias (1); Cross-link (9); Helix (10); Initiator methionine (1); Modified residue (11); Motif (1); Mutagenesis (23); Region (1); Repeat (6); Sequence conflict (2); Site (2) FUNCTION: GTPase activator for RAN. Converts cytoplasmic GTP-bound RAN to GDP-bound RAN, which is essential for RAN-mediated nuclear import and export (PubMed:18305100). Mediates dissociation of cargo from nuclear export complexes containing XPO1, RAN and RANBP2 after nuclear export (By similarity). Required for postimplantation embryonic development (PubMed:8314081). {ECO:0000250|UniProtKB:P46060, ECO:0000269|PubMed:18305100, ECO:0000269|PubMed:8314081}. PTM: Phosphorylation occurs before nuclear envelope breakdown and continues throughout mitosis. Phosphorylated by the M-phase kinase cyclin B/Cdk1, in vitro. Differential timimg of dephosphorylation occurs during phases of mitosis. The phosphorylated form remains associated with RANBP2/NUP358 and the SUMO E2-conjugating enzyme, UBE2I, on nuclear pore complex (NPC) diassembly and during mitosis. {ECO:0000269|PubMed:15037602}.; PTM: Sumoylated (PubMed:26506250, PubMed:11853669). Sumoylation is necessary for targeting to the nuclear envelope (NE) (PubMed:16469311). Sumoylation is necessary for association with mitotic spindles and kinetochores during mitosis (By similarity). Also required for interaction with RANBP2 and is mediated by UBE2I (PubMed:9456312, PubMed:11853669). {ECO:0000250|UniProtKB:P46060, ECO:0000269|PubMed:11853669, ECO:0000269|PubMed:16469311, ECO:0000269|PubMed:26506250, ECO:0000269|PubMed:9456312}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:26506250, ECO:0000269|PubMed:9442102, ECO:0000269|PubMed:9456312}. Nucleus, nucleoplasm {ECO:0000269|PubMed:26506250}. Nucleus envelope {ECO:0000269|PubMed:16469311, ECO:0000269|PubMed:18305100, ECO:0000269|PubMed:26506250, ECO:0000269|PubMed:9442102, ECO:0000269|PubMed:9456312}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:P46060}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P46060}. Note=Cytoplasmic during interphase (PubMed:26506250). Detected at the nuclear envelope during interphase (PubMed:9442102, PubMed:9456312, PubMed:26506250). Shuttles between nucleus and cytoplasm (PubMed:26506250). Targeted to the nuclear pores after sumoylation. During mitosis, associates with mitotic spindles, but is essentially not detected at the spindle poles. Association with kinetochores appears soon after nuclear envelope breakdown and persists until late anaphase. Mitotic location also requires sumoylation (By similarity). {ECO:0000250|UniProtKB:P46060, ECO:0000269|PubMed:26506250, ECO:0000269|PubMed:9442102, ECO:0000269|PubMed:9456312}. SUBUNIT: Homodimer (PubMed:7891706). Interacts with RAN (PubMed:7891706). Forms a complex with RANBP2/NUP358, NXF1 and NXT1 (By similarity). Forms a tight complex in association with RANBP2 and UBE2I/UBC9, the ubiquitin-conjugating enzyme E2 (PubMed:11853669). Interacts with UBE2I; the interaction conjugates SUMO1 to RANGAP1, and subsequently stabilizes interactions of sumoylated RANGAP1 with RANBP2 (PubMed:9456312, PubMed:18305100, PubMed:11853669). The complex composed of RANBP2, SUMO1, RANGAP1 and UBE2I associates with nuclear pore complexes (By similarity). Identified in a complex composed of RAN, RANBP2, sumoylated RANGAP1, UBE2I and XPO1 (By similarity). Interacts with TRAF6 (By similarity). Interacts with SUMO1 and SENP1 (By similarity). Interacts (when sumoylated) with MYCBP2; interaction inhibits MYCBP2 E3 ubiquitin-protein ligase activity and promotes MYCBP2 translocation to the nucleus (PubMed:26304119). {ECO:0000250|UniProtKB:P46060, ECO:0000269|PubMed:11853669, ECO:0000269|PubMed:18305100, ECO:0000269|PubMed:26304119, ECO:0000269|PubMed:9456312, ECO:0000305|PubMed:7891706}. TISSUE SPECIFICITY: Detected in adult brain, liver, kidney, intestine, uterus and ovary. {ECO:0000269|PubMed:8314081}. +Q64012 RALY_MOUSE RNA-binding protein Raly (Maternally-expressed hnRNP C-related protein) (hnRNP associated with lethal yellow protein) 312 33,188 Alternative sequence (1); Chain (1); Coiled coil (1); Cross-link (7); Domain (1); Initiator methionine (1); Modified residue (11); Sequence conflict (4) FUNCTION: RNA-binding protein that acts as a transcriptional cofactor for cholesterol biosynthetic genes in the liver (PubMed:27251289). Binds the lipid-responsive non-coding RNA LeXis and is required for LeXis-mediated effect on cholesterogenesis (PubMed:27251289). May be a heterogeneous nuclear ribonucleoprotein (hnRNP) (By similarity). {ECO:0000250|UniProtKB:Q9UKM9, ECO:0000269|PubMed:27251289}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27251289}. SUBUNIT: Identified in the spliceosome C complex. Interacts (through its RNA-binding domain) with FUS (through its RNA-binding domain); both are components of the same RNPs. {ECO:0000250|UniProtKB:Q9UKM9}. TISSUE SPECIFICITY: Widely expressed. Expressed in brain, testis, lung, spleen and kidney. Weakly expressed in liver. {ECO:0000269|PubMed:8319910}. DISEASE: Note=Defects in Raly are the cause of lethal yellow mutation (A(y)), a dominant allele that cause embryonic lethality when homozygous, and pleiotropic effects when heterozygous, including yellow pelage, obesity, non-insulin dependent diabetes and increased tumor susceptibility. A(y) is due to a 170 kb deletion that removes all but the promoter and non-coding first exon of Raly and links them to the ASIP/Agouti gene. {ECO:0000269|PubMed:8050375, ECO:0000269|PubMed:8319910}. +Q9EP71 RAI14_MOUSE Ankycorbin (Ankyrin repeat and coiled-coil structure-containing protein) (Novel retinal pigment epithelial cell protein) (Retinoic acid-induced protein 14) (p125) 979 108,852 Chain (1); Coiled coil (2); Erroneous initiation (1); Modified residue (21); Motif (1); Repeat (7); Sequence conflict (1) FUNCTION: Plays a role in actin regulation at the ectoplasmic specialization, a type of cell junction specific to testis. Important for establishment of sperm polarity and normal spermatid adhesion. May also promote integrity of Sertoli cell tight junctions at the blood-testis barrier. {ECO:0000250|UniProtKB:Q5U312}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11168586}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000269|PubMed:11168586}. Cytoplasm, cell cortex {ECO:0000269|PubMed:11168586}. Cell junction {ECO:0000250|UniProtKB:Q5U312}. Nucleus {ECO:0000250|UniProtKB:Q9P0K7}. Note=Associated with the cortical actin cytoskeleton structures in terminal web and cell-cell adhesion sites (PubMed:11168586). Highly expressed at the ectoplasmic specialization, an actin-rich cell junction specific to the testis (By similarity). Predominantly nuclear in nonconfluent cells (By similarity). {ECO:0000250|UniProtKB:Q5U312, ECO:0000250|UniProtKB:Q9P0K7, ECO:0000269|PubMed:11168586}. SUBUNIT: Interacts with PALLD (By similarity). Associates with actin (PubMed:11168586). However, does not bind F-actin directly (PubMed:11168586). {ECO:0000250|UniProtKB:Q5U312, ECO:0000269|PubMed:11168586}. TISSUE SPECIFICITY: Highly expressed in testis, where it localizes to seminiferous tubules (at protein level) (PubMed:11042181, PubMed:16806700). Expressed in ganglion cell layer and in Muller cell fibers of the retina (at protein level) (PubMed:11042181, PubMed:16806700). In small intestine highly expressed at the apical and lateral borders of absorptive epithelia (at protein level) (PubMed:11168586). In liver highly expressed along the bile canaliculi (at protein level) (PubMed:11168586). {ECO:0000269|PubMed:11042181, ECO:0000269|PubMed:11168586, ECO:0000269|PubMed:16806700}. +Q9CT10 RANB3_MOUSE Ran-binding protein 3 (RanBP3) 491 52,573 Chain (1); Domain (1); Initiator methionine (1); Modified residue (14); Sequence conflict (4) FUNCTION: Acts as a cofactor for XPO1/CRM1-mediated nuclear export, perhaps as export complex scaffolding protein. Bound to XPO1/CRM1, stabilizes the XPO1/CRM1-cargo interaction. In the absence of Ran-bound GTP prevents binding of XPO1/CRM1 to the nuclear pore complex. Binds to CHC1/RCC1 and increases the guanine nucleotide exchange activity of CHC1/RCC1. Recruits XPO1/CRM1 to CHC1/RCC1 in a Ran-dependent manner. Negative regulator of TGF-beta signaling through interaction with the R-SMAD proteins, SMAD2 and SMAD3, and mediating their nuclear export (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Interacts with CHC1 in a Ran-stimulated manner. Interacts with XPO1. Interacts (via its C-terminal R domain) with SMAD2 (dephosphorylated form via its MH1 and MH2 domains); the interaction results in the nuclear export of SMAD2 and termination of the TGF-beta signaling. Interacts (via its C-terminal R domain) with SMAD3 (dephosphorylated form via its MH1 domain); the interaction results in the nuclear export of SMAD3 and termination of the TGF-beta signaling (By similarity). {ECO:0000250}. +P34022 RANG_MOUSE Ran-specific GTPase-activating protein (HpaII tiny fragments locus 9a protein) (Ran-binding protein 1) (RANBP1) 203 23,596 Chain (1); Domain (1); Initiator methionine (1); Modified residue (8); Sequence conflict (9) FUNCTION: Plays a role in RAN-dependent nucleocytoplasmic transport. Alleviates the TNPO1-dependent inhibition of RAN GTPase activity and mediates the dissociation of RAN from proteins involved in transport into the nucleus (PubMed:9428644). Induces a conformation change in the complex formed by XPO1 and RAN that triggers the release of the nuclear export signal of cargo proteins (By similarity). Promotes the disassembly of the complex formed by RAN and importin beta. Promotes dissociation of RAN from a complex with KPNA2 and CSE1L (PubMed:9428644). Required for normal mitotic spindle assembly and normal progress through mitosis via its effect on RAN (By similarity). Does not increase the RAN GTPase activity by itself, but increases GTP hydrolysis mediated by RANGAP1 (PubMed:9428644). Inhibits RCC1-dependent exchange of RAN-bound GDP by GTP (By similarity). {ECO:0000250|UniProtKB:P43487, ECO:0000269|PubMed:9428644}. SUBUNIT: Interacts with RAN (via C-terminus of GTP-bound form) but not with GDP-bound RAN (PubMed:8255297, PubMed:7891706, PubMed:8896452). Identified in a complex composed of RAN, RANGAP1 and RANBP1 (By similarity). Identified in a complex that contains TNPO1, RAN and RANBP1 (PubMed:9428644). Identified in a complex that contains CSE1L, KPNA2, RAN and RANBP1 (PubMed:9428644). Identified in a complex with nucleotide-free RAN and RCC1 (By similarity). {ECO:0000250|UniProtKB:P43487, ECO:0000269|PubMed:7891706, ECO:0000269|PubMed:8255297, ECO:0000269|PubMed:8896452, ECO:0000269|PubMed:9428644}. +Q9WUP1 RAMP3_MOUSE Receptor activity-modifying protein 3 147 16,779 Chain (1); Disulfide bond (2); Glycosylation (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 118 137 Helical. {ECO:0000255}. TOPO_DOM 23 117 Extracellular. {ECO:0000255}.; TOPO_DOM 138 147 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a role in cardioprotection by reducing cardiac hypertrophy and perivascular fibrosis in a GPER1-dependent manner. Transports the calcitonin gene-related peptide type 1 receptor (CALCRL) to the plasma membrane. Acts as a receptor for adrenomedullin (AM) together with CALCRL. {ECO:0000269|PubMed:10854696, ECO:0000269|PubMed:23674134}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23674134}; Single-pass type I membrane protein {ECO:0000269|PubMed:23674134}. Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Interacts with GPER1 (By similarity). Heterodimer of CALCRL and RAMP3. {ECO:0000250}. TISSUE SPECIFICITY: Expressed predominantly in the testis, embryonic and adult brain and in kidney. {ECO:0000269|PubMed:10777702, ECO:0000269|PubMed:10854696}. +Q61820 RANT_MOUSE GTP-binding nuclear protein Ran, testis-specific isoform 216 24,452 Chain (1); Cross-link (2); Erroneous initiation (1); Initiator methionine (1); Modified residue (8); Nucleotide binding (3); Sequence conflict (1) FUNCTION: GTP-binding protein involved in nucleocytoplasmic transport. Required for the import of protein into the nucleus and also for RNA export. Involved in chromatin condensation and control of cell cycle (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. TISSUE SPECIFICITY: Testis specific. +P62835 RAP1A_MOUSE Ras-related protein Rap-1A (Ras-related protein Krev-1) 184 20,987 Chain (1); Lipidation (1); Modified residue (1); Motif (1); Nucleotide binding (3); Propeptide (1) FUNCTION: Induces morphological reversion of a cell line transformed by a Ras oncogene. Counteracts the mitogenic function of Ras, at least partly because it can interact with Ras GAPs and RAF in a competitive manner. Together with ITGB1BP1, regulates KRIT1 localization to microtubules and membranes (By similarity). Plays a role in nerve growth factor (NGF)-induced neurite outgrowth. Plays a role in the regulation of embryonic blood vessel formation. Involved in the establishment of basal endothelial barrier function. May be involved in the regulation of the vascular endothelial growth factor receptor KDR expression at endothelial cell-cell junctions. {ECO:0000250, ECO:0000269|PubMed:19635461}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Cell junction {ECO:0000269|PubMed:19635461}. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Early endosome {ECO:0000250}. Late endosome {ECO:0000250}. Note=Recruited from early endosome to late endosome compartment after nerve growth factor (NGF) stimulation. Colocalized with RAPGEF2 in the perinuclear region (By similarity). Localized with RAPGEF2 at cell-cell junctions. {ECO:0000250}. SUBUNIT: Found in a complex, at least composed of ITGB1BP1, KRIT1 and RAP1A. Interacts (active GTP-bound form preferentially) with KRIT1 (via C-terminus FERM domain); the interaction does not induce the opening conformation of KRIT1. In its GTP-bound form interacts with PLCE1 and RADIL. Interacts with SGSM1, SGSM2 and SGSM3. Interacts (via GTP-bound active form) with RAPGEF2 (via Ras-associating domain) (By similarity). {ECO:0000250}. +Q99JI6 RAP1B_MOUSE Ras-related protein Rap-1b (GTP-binding protein smg p21B) 184 20,825 Chain (1); Lipidation (1); Modified residue (3); Motif (1); Nucleotide binding (4); Propeptide (1); Region (1); Sequence conflict (2) FUNCTION: GTP-binding protein that possesses intrinsic GTPase activity. Contributes to the polarizing activity of KRIT1 and CDH5 in the establishment and maintenance of correct endothelial cell polarity and vascular lumen. Required for the localization of phosphorylated PRKCZ, PARD3 and TIAM1 to the cell junction. Plays a role in the establishment of basal endothelial barrier function (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Cell junction {ECO:0000250}. Note=May shuttle between plasma membrane and cytosol. Presence of KRIT1 and CDH5 is required for its localization to the cell junction (By similarity). {ECO:0000250}. SUBUNIT: Interacts with SGSM1, SGSM2 and SGSM3. Interacts with KRIT1 (By similarity). {ECO:0000250}. +Q7TPD6 RAVR2_MOUSE Ribonucleoprotein PTB-binding 2 (Protein raver-2) 673 72,031 Chain (1); Compositional bias (1); Domain (3) FUNCTION: May bind single-stranded nucleic acids. {ECO:0000305}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16051233}. Cytoplasm {ECO:0000269|PubMed:16051233}. Note=May shuttle between the nucleus and the cytoplasm. SUBUNIT: Interacts with PTBP1 and RAVER1. {ECO:0000269|PubMed:16051233}. TISSUE SPECIFICITY: Expressed throughout embryogenesis. Detected at low levels in adult lung, brain and kidney, but not in the other tissues tested. {ECO:0000269|PubMed:16051233}. +Q61411 RASH_MOUSE GTPase HRas (H-Ras-1) (Transforming protein p21) (c-H-ras) (p21ras) [Cleaved into: GTPase HRas, N-terminally processed] 189 21,298 Alternative sequence (1); Chain (2); Erroneous initiation (1); Initiator methionine (1); Lipidation (4); Modified residue (4); Motif (1); Mutagenesis (1); Nucleotide binding (3); Propeptide (1); Region (1); Sequence conflict (2) FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. PTM: Palmitoylated by the ZDHHC9-GOLGA7 complex. A continuous cycle of de- and re-palmitoylation regulates rapid exchange between plasma membrane and Golgi. {ECO:0000250|UniProtKB:P01112}.; PTM: S-nitrosylated; critical for redox regulation. Important for stimulating guanine nucleotide exchange. No structural perturbation on nitrosylation. {ECO:0000250|UniProtKB:P01112}.; PTM: The covalent modification of cysteine by 15-deoxy-Delta12,14-prostaglandin-J2 is autocatalytic and reversible. It may occur as an alternative to other cysteine modifications, such as S-nitrosylation and S-palmitoylation. {ECO:0000250|UniProtKB:P01112}.; PTM: Acetylation at Lys-104 prevents interaction with guanine nucleotide exchange factors (GEFs). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Golgi apparatus {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Note=Shuttles between the plasma membrane and the Golgi apparatus. The active GTP-bound form is localized most strongly to membranes than the inactive GDP-bound form (By similarity). {ECO:0000250}. SUBUNIT: Forms a signaling complex with RASGRP1 and DGKZ (By similarity). In its GTP-bound form interacts with PLCE1 (By similarity). Interacts with TBC1D10C and RASSF5 (By similarity). Interacts with PDE6D (By similarity). Interacts with IKZF3 (By similarity). Found in a complex with at least BRAF, HRAS, MAP2K1, MAPK3 and RGS14 (By similarity). Interacts (active GTP-bound form) with RGS14 (via RBD 1 domain) (By similarity). Interacts with RACK1 (By similarity). Interacts with RAPGEF2 (By similarity). Interacts with RGL3 (PubMed:10869344). Interacts with HSPD1 (PubMed:1347942). Interacts with PIK3CG; the interaction is required for membrane recruitment and beta-gamma G protein dimer-dependent activation of the PI3K gamma complex PIK3CG:PIK3R6 (PubMed:19906996). Interacts (in GTP-bound form) with Oog1 (PubMed:16580637). {ECO:0000250|UniProtKB:P01112, ECO:0000250|UniProtKB:P20171, ECO:0000269|PubMed:10869344, ECO:0000269|PubMed:1347942, ECO:0000269|PubMed:16580637, ECO:0000269|PubMed:19906996}. +Q8R3C6 RBM19_MOUSE Probable RNA-binding protein 19 (RNA-binding motif protein 19) 952 106,083 Alternative sequence (2); Beta strand (21); Chain (1); Compositional bias (3); Cross-link (1); Domain (6); Helix (10); Modified residue (6); Turn (3) FUNCTION: Plays a role in embryo pre-implantation development. {ECO:0000269|PubMed:19087264}. SUBCELLULAR LOCATION: Nucleus, nucleolus. Nucleus, nucleoplasm. Cytoplasm. Chromosome. Note=Colocalizes with NPM1 during interphase. By late prophase, metaphase, anaphase and telophase, associates with the chromosome periphery. By telophase localizes to nucleolar precursor body (NPB) (By similarity). In discrete foci distributed throughout the cytoplasm and nucleoplasm during the 4 to 8 cell stages and the morula stage, but not in the periphery of the NPB. During blastocyst development, becomes increasingly localized to the nucleolus and less to the cytoplasm. At the late blastocyst stage, localized predominantly in the nucleolus. Localized in the nucleolus during interphase and to the perichromosomal sheath during mitosis. Does not colocalize in the cytoplasm with GW182 in P-bodies. May translocate to the nucleolus upon early embryonic development. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the crypts of Lieberkuhn of the intestine (at protein level). {ECO:0000269|PubMed:16027046}. +Q8BHN5 RBM45_MOUSE RNA-binding protein 45 (Developmentally-regulated RNA-binding protein 1) (RB-1) (RNA-binding motif protein 45) 476 53,324 Chain (1); Cross-link (1); Domain (3); Frameshift (1); Modified residue (2); Sequence conflict (2) FUNCTION: RNA-binding protein with binding specificity for poly(C). May play an important role in neural development (By similarity). {ECO:0000250|UniProtKB:Q8CFD1, ECO:0000250|UniProtKB:Q8IUH3}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Predominantly cytoplasmic. May shuttle between cytoplasm and nucleus. {ECO:0000250}. +Q8VCH7 RDH10_MOUSE Retinol dehydrogenase 10 (EC 1.1.1.300) 341 38,075 Active site (1); Binding site (1); Chain (1); Nucleotide binding (1); Transmembrane (1) TRANSMEM 3 23 Helical; Signal-anchor. {ECO:0000255}. Cofactor metabolism; retinol metabolism. FUNCTION: Retinol dehydrogenase with a clear preference for NADP. Converts all-trans-retinol to all-trans-retinal. Has no detectable activity towards 11-cis-retinol, 9-cis-retinol and 13-cis-retinol (By similarity). Required for normal embryonic development. {ECO:0000250, ECO:0000269|PubMed:17473173}. SUBCELLULAR LOCATION: Microsome membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Detected in retinal pigment epithelium (at protein level). {ECO:0000269|PubMed:12407145, ECO:0000269|PubMed:15505029}. +Q8BQZ4 RLGPB_MOUSE Ral GTPase-activating protein subunit beta (p170) 1484 165,200 Alternative sequence (2); Chain (1); Domain (1); Erroneous initiation (1); Modified residue (7); Sequence conflict (1) FUNCTION: Non-catalytic subunit of the heterodimeric RalGAP1 and RalGAP2 complexes which act as GTPase activators for the Ras-like small GTPases RALA and RALB. {ECO:0000250}. SUBUNIT: Component of the heterodimeric RalGAP1 complex with RALGAPA1 and of the heterodimeric RalGAP2 complex with RALGAPA2. Heterodimerization is required for activity (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Abundantly expressed in testis, pancreas, lung, thymus, brown fat, and white fat. Expressed at lower levels in the brain. {ECO:0000269|PubMed:16490346}. +Q5SVL6 RPGP2_MOUSE Rap1 GTPase-activating protein 2 (Rap1GAP2) (GTPase-activating Rap/Ran-GAP domain-like protein 4) 712 78,254 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (1); Modified residue (9); Sequence caution (1) FUNCTION: GTPase activator for the nuclear Ras-related regulatory protein RAP-1A (KREV-1), converting it to the putatively inactive GDP-bound state. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +Q9CYP7 SESN3_MOUSE Sestrin-3 492 57,021 Binding site (2); Chain (1); Region (2) FUNCTION: May function as an intracellular leucine sensor that negatively regulates the TORC1 signaling pathway (PubMed:25259925). May also regulate the insulin-receptor signaling pathway through activation of TORC2 (PubMed:25377878). This metabolic regulator may also play a role in protection against oxidative and genotoxic stresses (By similarity). {ECO:0000250|UniProtKB:P58004, ECO:0000269|PubMed:25259925, ECO:0000269|PubMed:25377878}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25377878}. SUBUNIT: Interacts with the GATOR2 complex which is composed of MIOS, SEC13, SEH1L, WDR24 and WDR59; the interaction is not regulated by leucine (By similarity). Interacts with RRAGA, RRAGB, RRAGC and RRAGD; may function as a guanine nucleotide dissociation inhibitor for RRAGs and regulate them (PubMed:25259925). Interacts with the TORC2 complex; through RICTOR (PubMed:25377878). {ECO:0000250|UniProtKB:P58005, ECO:0000269|PubMed:25259925, ECO:0000269|PubMed:25377878}. DOMAIN: The C-terminal domain may mediate interaction with GATOR2 and regulation of TORC1 signaling. {ECO:0000250|UniProtKB:P58004}. TISSUE SPECIFICITY: Detected in liver and skeletal muscles. {ECO:0000269|PubMed:25259925}. +Q9WUV2 SIA7C_MOUSE Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 3 (EC 2.4.99.7) (GalNAc alpha-2,6-sialyltransferase III) (ST6GalNAc III) (ST6GalNAcIII) (STY) (Sialyltransferase 7C) (SIAT7-C) 305 35,414 Chain (1); Disulfide bond (1); Glycosylation (2); Topological domain (2); Transmembrane (1) TRANSMEM 9 28 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 8 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 29 305 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Involved in the biosynthesis of ganglioside GD1A from GM1B. Transfers CMP-NeuAc with an alpha-2,6-linkage to GalNAc residue on NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc of glycoproteins and glycolipids. ST6GalNAcIII prefers glycolipids to glycoproteins. {ECO:0000269|PubMed:10207017}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. TISSUE SPECIFICITY: High expression in brain, lung and heart and to a lesser extent in kidney, mammary gland, spleen, testis and thymus. {ECO:0000269|PubMed:10207017}. +Q9QYJ1 SIA7E_MOUSE Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 5 (EC 2.4.99.-) (GD1 alpha synthase) (GalNAc alpha-2,6-sialyltransferase V) (ST6GalNAc V) (ST6GalNAcV) (Sialyltransferase 7E) (SIAT7-E) 336 38,430 Chain (1); Compositional bias (1); Disulfide bond (1); Glycosylation (2); Natural variant (2); Topological domain (2); Transmembrane (1) TRANSMEM 9 29 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 8 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 30 336 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Involved in the biosynthesis of ganglioside GD1a from GM1b. It exhibits higher activity with glycolipids than with glycoproteins. {ECO:0000269|PubMed:10521438, ECO:0000269|PubMed:10601645}. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein. TISSUE SPECIFICITY: High expression in forebrain and to a lesser extent in cerebellum. No expression in salivary gland, intestine, liver, kidney, heart, lung, thymus and spleen. {ECO:0000269|PubMed:10521438, ECO:0000269|PubMed:10601645}. +Q9JM95 SIA7F_MOUSE Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 6 (EC 2.4.99.-) (GalNAc alpha-2,6-sialyltransferase VI) (ST6GalNAc VI) (ST6GalNAcVI) (Sialyltransferase 7F) (SIAT7-F) 333 38,167 Alternative sequence (3); Chain (1); Compositional bias (1); Disulfide bond (1); Erroneous gene model prediction (5); Glycosylation (1); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 44 64 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 43 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 65 333 Lumenal. {ECO:0000255}. FUNCTION: Alpha-2,6-sialyltransferase involved in the synthesis of alpha-series gangliosides. Has activity toward GD1a, GT1b and GM1b. Has no activity toward glycoproteins. Responsible for the biosynthesis of DSGG (disialylgalactosylgloboside) from MSGG (monosialylgalactosylgloboside) in kidney. {ECO:0000269|PubMed:10702226}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10702226}. +Q64687 SIA8A_MOUSE Alpha-N-acetylneuraminide alpha-2,8-sialyltransferase (EC 2.4.99.8) (Alpha-2,8-sialyltransferase 8A) (Ganglioside GD3 synthase) (Ganglioside GT3 synthase) (Sialyltransferase 8A) (SIAT8-A) (Sialyltransferase St8Sia I) (ST8SiaI) 355 40,324 Active site (1); Binding site (1); Chain (1); Disulfide bond (2); Glycosylation (4); Region (2); Sequence conflict (4); Topological domain (2); Transmembrane (1) TRANSMEM 29 47 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 28 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 48 355 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. Lipid metabolism; sphingolipid metabolism. FUNCTION: Involved in the production of gangliosides GD3 and GT3 from GM3; gangliosides are a subfamily of complex glycosphinglolipds that contain one or more residues of sialic acid. {ECO:0000269|PubMed:8910600}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. +O35696 SIA8B_MOUSE Alpha-2,8-sialyltransferase 8B (EC 2.4.99.-) (Polysialic acid synthase) (Sialyltransferase 8B) (SIAT8-B) (Sialyltransferase St8Sia II) (ST8SiaII) (Sialyltransferase X) (STX) 375 42,411 Active site (1); Binding site (1); Chain (1); Disulfide bond (2); Glycosylation (6); Region (3); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 7 23 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 24 375 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: May transfer sialic acid through alpha-2,8-linkages to the alpha-2,3-linked and alpha-2,6-linked sialic acid of N-linked oligosaccharides of glycoproteins and may be involved in PSA (polysialic acid) expression. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. +Q64689 SIA8C_MOUSE Sia-alpha-2,3-Gal-beta-1,4-GlcNAc-R:alpha 2,8-sialyltransferase (EC 2.4.99.-) (Alpha-2,8-sialyltransferase 8C) (Alpha-2,8-sialyltransferase III) (ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 3) (Sialyltransferase 8C) (SIAT8-C) (Sialyltransferase St8Sia III) (ST8SiaIII) 380 43,942 Active site (1); Binding site (1); Chain (1); Disulfide bond (2); Glycosylation (3); Region (3); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 18 33 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 17 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 34 380 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Catalyzes the transfer of sialic acid from a CMP-linked sialic acid donor onto the terminal sialic acid of an acceptor through alpha-2,8-linkages. Is active with alpha-2,3-linked, alpha-2,6-linked and alpha-2,8-linked sialic acid of N-linked oligosaccharides of glycoproteins and glycolipids. Displays preference for substrates with alpha-2,3-linked terminal sialic acid. It can form polysialic acid in vitro directly on alpha-2,3-, alpha-2,6-, or alpha-2,8-linked sialic acid. {ECO:0000269|PubMed:7782326}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O43173}. TISSUE SPECIFICITY: Expressed in brain and testes. {ECO:0000269|PubMed:7782326}. +Q64692 SIA8D_MOUSE CMP-N-acetylneuraminate-poly-alpha-2,8-sialyltransferase (EC 2.4.99.-) (Alpha-2,8-sialyltransferase 8D) (Polysialyltransferase-1) (Sialyltransferase 8D) (SIAT8-D) (Sialyltransferase St8Sia IV) (ST8SiaIV) 359 41,256 Active site (1); Binding site (1); Chain (1); Disulfide bond (2); Glycosylation (5); Region (3); Topological domain (2); Transmembrane (1) TRANSMEM 8 20 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 7 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 21 359 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Catalyzes the polycondensation of alpha-2,8-linked sialic acid required for the synthesis of polysialic acid (PSA), which is present on the embryonic neural cell adhesion molecule (N-CAM), necessary for plasticity of neural cells. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Strongly expressed in lung, heart and spleen and weakly in brain. +P70126 SIA8E_MOUSE Alpha-2,8-sialyltransferase 8E (EC 2.4.99.-) (Sialyltransferase 8E) (SIAT8-E) (Sialyltransferase St8Sia V) (ST8SiaV) 412 47,829 Active site (1); Alternative sequence (2); Binding site (1); Chain (1); Disulfide bond (2); Glycosylation (5); Region (2); Sequence conflict (9); Topological domain (2); Transmembrane (1) TRANSMEM 17 37 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 16 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 38 412 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: May be involved in the synthesis of gangliosides GD1c, GT1a, GQ1b and GT3 from GD1a, GT1b, GM1b and GD3 respectively. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Highly expressed in brain. Expressed at low levels in other tissues, including liver, testis, lung, placenta and spleen. +Q8K4T1 SIA8F_MOUSE Alpha-2,8-sialyltransferase 8F (EC 2.4.99.-) (Sialyltransferase 8F) (SIAT8-F) (Sialyltransferase St8Sia VI) (ST8SiaVI) 398 45,428 Active site (1); Binding site (1); Chain (1); Disulfide bond (2); Glycosylation (4); Region (2); Topological domain (2); Transmembrane (1) TRANSMEM 4 24 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 3 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 25 398 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Prefers O-glycans to N-glycans or glycolipids as acceptor substrates. The minimal acceptor substrate is the NeuAc-alpha-2,3(6)-Gal sequence at the non-reducing end of their carbohydrate groups. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. +P70665 SIAE_MOUSE Sialate O-acetylesterase (EC 3.1.1.53) (Sialic acid-specific 9-O-acetylesterase) (Yolk sac protein 2) [Cleaved into: Sialate O-acetylesterase small subunit; Sialate O-acetylesterase large subunit] 541 60,775 Alternative sequence (3); Chain (2); Erroneous initiation (1); Glycosylation (8); Sequence conflict (6); Signal peptide (1) FUNCTION: Catalyzes the removal of O-acetyl ester groups from position 9 of the parent sialic acid, N-acetylneuraminic acid. PTM: The two subunits are derived from a single precursor by proteolytic cleavage. {ECO:0000250}.; PTM: The lysosomal isoform is glycosylated. SUBCELLULAR LOCATION: Isoform 1: Lysosome.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. SUBUNIT: Disulfide-linked heterodimer of a small subunit and a large subunit. {ECO:0000250}. TISSUE SPECIFICITY: Isoform 1 is widely expressed. Isoform 2 shows a more restricted distribution with highest expression in brain and ovary and lower levels in liver and thymus. +Q06986 SIAH2_MOUSE E3 ubiquitin-protein ligase SIAH2 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase SIAH2) (Seven in absentia homolog 2) (Siah-2) (mSiah2) 325 34,758 Chain (1); Metal binding (8); Modified residue (6); Region (1); Sequence conflict (1); Zinc finger (2) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:11257006, PubMed:14645235, PubMed:14645526, PubMed:17003045, PubMed:9637679, PubMed:26070566). E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates (PubMed:11257006, PubMed:14645235, PubMed:14645526, PubMed:17003045, PubMed:9637679, PubMed:26070566). Mediates E3 ubiquitin ligase activity either through direct binding to substrates or by functioning as the essential RING domain subunit of larger E3 complexes. Mediates ubiquitination and proteasomal degradation of DYRK2 in response to hypoxia. Promotes monoubiquitination of SNCA (By similarity). Triggers the ubiquitin-mediated degradation of many substrates, including proteins involved in transcription regulation (GPS2, POU2AF1, PML, NCOR1), a cell surface receptor (DCC), an antiapoptotic protein (BAG1), and a protein involved in synaptic vesicle function in neurons (SYP) (PubMed:11257006, PubMed:14645235, PubMed:14645526, PubMed:17003045, PubMed:9637679, PubMed:26070566). It is thereby involved in apoptosis, tumor suppression, cell cycle, transcription and signaling processes. Has some overlapping function with SIAH1. Triggers the ubiquitin-mediated degradation of TRAF2, whereas SIAH1 does not. Regulates cellular clock function via ubiquitination of the circadian transcriptional repressors NR1D1 and NR1D2 leading to their proteasomal degradation. Plays an important role in mediating the rhythmic degradation/clearance of NR1D1 and NR1D2 contributing to their circadian profile of protein abundance (PubMed:26392558). {ECO:0000250|UniProtKB:O43255, ECO:0000269|PubMed:11257006, ECO:0000269|PubMed:14645235, ECO:0000269|PubMed:14645526, ECO:0000269|PubMed:17003045, ECO:0000269|PubMed:26070566, ECO:0000269|PubMed:26392558, ECO:0000269|PubMed:9637679}. PTM: Phosphorylated at Ser-29 by DYRK2; this increases the ubiquitin ligase activity and promotes degradation of EGLN3 (By similarity). Phosphorylated at Thr-24 and Ser-29 by MAPK14, which mediates the degradation by the proteasome of EGLN3. {ECO:0000250|UniProtKB:O43255, ECO:0000269|PubMed:17003045}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O43255}. Nucleus {ECO:0000250|UniProtKB:O43255}. Note=Predominantly cytoplasmic. Partially nuclear. {ECO:0000250|UniProtKB:O43255}. SUBUNIT: Homodimer (By similarity). Interacts with UBE2E2 (By similarity). Interacts with VAV1, without mediating its ubiquitin-mediated degradation (By similarity). Interacts with CACYBP/SIP (By similarity). Probable component of some large E3 complex possibly composed of UBE2D1, SIAH2, CACYBP/SIP, SKP1, APC and TBL1X (By similarity). Interacts with UBE2I (By similarity). Interacts with PEG10, which may inhibit its activity (By similarity). Interacts with EGLN2 and SNCAIP (By similarity). Interacts with DYRK2 (By similarity). Interacts with PEG3 (PubMed:10681424). Interacts with NR1D1 and NR1D2 (By similarity). {ECO:0000250|UniProtKB:O43255, ECO:0000269|PubMed:10681424}. DOMAIN: The RING-type zinc finger domain is essential for ubiquitin ligase activity.; DOMAIN: The SBD domain (substrate-binding domain) mediates the homodimerization and the interaction with substrate proteins. It is related to the TRAF family. {ECO:0000250|UniProtKB:P61092}. TISSUE SPECIFICITY: Widely expressed at low level in embryos and adults. Expressed in a specific population of germ cells within both the mouse ovary and testis. Absent in primordial oocytes but expressed in all growing oocytes, coincident with their recruitment from the pool of quiescent cells. Its level of expression increases as the oocytes mature. Expressed in Graafian follicles and in fertilized zygotes up until the two cell stage, a time of extensive maternal transcript degradation and zygotic gene activation. Expressed in the testis from postmeiotic spermatids. {ECO:0000269|PubMed:7895278, ECO:0000269|PubMed:8404535}. +Q61711 SIAL_MOUSE Bone sialoprotein 2 (Bone sialoprotein II) (BSP II) (Cell-binding sialoprotein) (Integrin-binding sialoprotein) 324 35,734 Chain (1); Compositional bias (3); Glycosylation (4); Modified residue (8); Motif (1); Sequence conflict (4); Signal peptide (1) FUNCTION: Binds tightly to hydroxyapatite. Appears to form an integral part of the mineralized matrix. Probably important to cell-matrix interaction. Promotes Arg-Gly-Asp-dependent cell attachment (By similarity). {ECO:0000250}. PTM: N-glycosylated; glycans consist of sialylated and core-fucosylated bi-, tri- and tetraantennary chains. {ECO:0000250}.; PTM: Sulfated on either Tyr-320 or Tyr-321. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. +Q99J77 SIAS_MOUSE Sialic acid synthase (N-acetylneuraminate-9-phosphate synthase) (EC 2.5.1.57) (N-acetylneuraminic acid phosphate synthase) 359 40,024 Chain (1); Domain (1); Modified residue (5); Sequence conflict (1) FUNCTION: Produces N-acetylneuraminate-9-phosphate (Neu5Ac-9-P) from N-acetylmannosamine 6-phosphate. Has no detectable activity towards N-acetylmannosamine or mannose 6-phosphate. {ECO:0000269|PubMed:10873658}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10873658}. TISSUE SPECIFICITY: Ubiquitious. {ECO:0000269|PubMed:10873658}. +Q64685 SIAT1_MOUSE Beta-galactoside alpha-2,6-sialyltransferase 1 (Alpha 2,6-ST 1) (EC 2.4.99.1) (CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,6-sialyltransferase 1) (ST6Gal I) (ST6GalI) (Sialyltransferase 1) 403 46,586 Binding site (9); Chain (1); Disulfide bond (3); Glycosylation (2); Modified residue (1); Mutagenesis (3); Region (1); Sequence conflict (5); Topological domain (2); Transmembrane (1) TRANSMEM 10 26 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 9 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 27 403 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Transfers sialic acid from CMP-sialic acid to galactose-containing acceptor substrates. {ECO:0000269|PubMed:22039275}. PTM: The soluble form derives from the membrane form by proteolytic processing. {ECO:0000250|UniProtKB:P13721}.; PTM: N-glycosylated. {ECO:0000250|UniProtKB:P13721}. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:P15907}; Single-pass type II membrane protein. Secreted. Note=Membrane-bound form in trans cisternae of Golgi. Secreted into the body fluid. SUBUNIT: Monomer and homodimer. {ECO:0000250|UniProtKB:P15907}. +Q76K27 SIAT2_MOUSE Beta-galactoside alpha-2,6-sialyltransferase 2 (Alpha 2,6-ST 2) (EC 2.4.99.1) (CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,6-sialyltransferase 2) (ST6Gal II) (ST6GalII) (Sialyltransferase 2) 524 60,192 Alternative sequence (2); Chain (1); Compositional bias (1); Disulfide bond (3); Erroneous initiation (1); Glycosylation (3); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 12 32 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 11 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 33 524 Lumenal. {ECO:0000255}. FUNCTION: Transfers sialic acid from the donor of substrate CMP-sialic acid to galactose containing acceptor substrates. Has alpha-2,6-sialyltransferase activity toward oligosaccharides that have the Gal-beta-1,4-GlcNAc sequence at the non-reducing end of their carbohydrate groups, but it has weak or no activities toward glycoproteins and glycolipids. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Mainly expressed in brain and embryo. Very low expression is also detected in spleen, oviduct, lung and skeletal muscle. {ECO:0000269|PubMed:12966079}. +P97325 SIAT6_MOUSE CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3-sialyltransferase (EC 2.4.99.6) (Beta-galactoside alpha-2,3-sialyltransferase 3) (Alpha 2,3-ST 3) (Gal beta-1,3(4) GlcNAc alpha-2,3 sialyltransferase) (N-acetyllactosaminide alpha-2,3-sialyltransferase) (ST3Gal III) (ST3GalIII) (ST3N) (Sialyltransferase 6) 374 42,132 Chain (1); Disulfide bond (1); Glycosylation (2); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 9 28 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 8 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 29 374 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Catalyzes the formation of the NeuAc-alpha-2,3-Gal-beta-1,4-GlcNAc-, NeuAc-alpha-2,3-Gal-beta-1,3-GlcNAc- and NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc- sequences found in terminal carbohydrate groups of glycoproteins and glycolipids. The highest activity is toward Gal-beta-1,3-GlcNAc and the lowest toward Gal-beta-1,3-GalNAc. {ECO:0000269|PubMed:9184827}. SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. TISSUE SPECIFICITY: Found in all tissues tested. High expression found in brain, liver, kidney, colon, heart and spleen. {ECO:0000269|PubMed:9184827}. +O88829 SIAT9_MOUSE Lactosylceramide alpha-2,3-sialyltransferase (EC 2.4.99.9) (CMP-NeuAc:lactosylceramide alpha-2,3-sialyltransferase) (Ganglioside GM3 synthase) (ST3Gal V) (ST3GalV) (Sialyltransferase 9) 414 47,360 Alternative sequence (1); Chain (1); Disulfide bond (1); Erroneous gene model prediction (1); Erroneous initiation (7); Glycosylation (3); Sequence conflict (4); Topological domain (2); Transmembrane (1) TRANSMEM 66 86 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 65 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 87 414 Lumenal. {ECO:0000255}. FUNCTION: Catalyzes the formation of ganglioside GM3 (alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1, 4-beta-D-glucosylceramide), which is a precursor for most of the complex ganglioside species. {ECO:0000269|PubMed:12629211}.; FUNCTION: (Microbial infection) Gangliosides GD1b and GT1b (derived from GM3) may serve as receptors for some C.botulinum neurotoxins (minimally types BoNT/A, B, C) (PubMed:16115873). {ECO:0000305|PubMed:16115873}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. +Q6AXF6 SIDT1_MOUSE SID1 transmembrane family member 1 827 93,896 Alternative sequence (1); Chain (1); Glycosylation (7); Mutagenesis (2); Signal peptide (1); Topological domain (12); Transmembrane (11) TRANSMEM 310 330 Helical. {ECO:0000255}.; TRANSMEM 443 463 Helical. {ECO:0000255}.; TRANSMEM 495 515 Helical. {ECO:0000255}.; TRANSMEM 542 562 Helical. {ECO:0000255}.; TRANSMEM 573 590 Helical. {ECO:0000255}.; TRANSMEM 601 621 Helical. {ECO:0000255}.; TRANSMEM 627 647 Helical. {ECO:0000255}.; TRANSMEM 684 704 Helical. {ECO:0000255}.; TRANSMEM 711 731 Helical. {ECO:0000255}.; TRANSMEM 742 762 Helical. {ECO:0000255}.; TRANSMEM 792 812 Helical. {ECO:0000255}. TOPO_DOM 20 309 Extracellular. {ECO:0000255}.; TOPO_DOM 331 442 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 464 494 Extracellular. {ECO:0000255}.; TOPO_DOM 516 541 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 563 572 Extracellular. {ECO:0000255}.; TOPO_DOM 591 600 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 622 626 Extracellular. {ECO:0000255}.; TOPO_DOM 648 683 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 705 710 Extracellular. {ECO:0000255}.; TOPO_DOM 732 741 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 763 791 Extracellular. {ECO:0000255}.; TOPO_DOM 813 827 Cytoplasmic. {ECO:0000255}. FUNCTION: In vitro binds long double-stranded RNA (dsRNA) (500 and 700 base pairs), but not dsRNA shorter than 300 bp (PubMed:26067272). Not involved in RNA autophagy, a process in which RNA is directly imported into lysosomes in an ATP-dependent manner, and degraded (PubMed:27046251). {ECO:0000269|PubMed:26067272, ECO:0000269|PubMed:27046251}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8CIF6 SIDT2_MOUSE SID1 transmembrane family member 2 832 94,501 Alternative sequence (1); Chain (1); Compositional bias (1); Glycosylation (10); Modified residue (3); Mutagenesis (6); Signal peptide (1); Topological domain (11); Transmembrane (10) TRANSMEM 294 314 Helical. {ECO:0000255}.; TRANSMEM 448 468 Helical. {ECO:0000255}.; TRANSMEM 500 520 Helical. {ECO:0000255}.; TRANSMEM 547 567 Helical. {ECO:0000255}.; TRANSMEM 606 626 Helical. {ECO:0000255}.; TRANSMEM 632 652 Helical. {ECO:0000255}.; TRANSMEM 689 709 Helical. {ECO:0000255}.; TRANSMEM 716 736 Helical. {ECO:0000255}.; TRANSMEM 747 767 Helical. {ECO:0000255}.; TRANSMEM 797 817 Helical. {ECO:0000255}. TOPO_DOM 19 293 Extracellular. {ECO:0000255}.; TOPO_DOM 315 447 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 469 499 Extracellular. {ECO:0000255}.; TOPO_DOM 521 546 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 568 605 Extracellular. {ECO:0000255}.; TOPO_DOM 627 631 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 653 688 Extracellular. {ECO:0000255}.; TOPO_DOM 710 715 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 737 746 Extracellular. {ECO:0000255}.; TOPO_DOM 768 796 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 818 832 Extracellular. {ECO:0000255}. FUNCTION: Mediates the translocation of RNA and DNA across the lysosomal membrane during RNA and DNA autophagy (RDA), a process in which RNA and DNA is directly imported into lysosomes in an ATP-dependent manner, and degraded (PubMed:27046251, PubMed:27846365, PubMed:28724756). Involved in the uptake of single-stranded oligonucleotides by living cells, a process called gymnosis (PubMed:28277980). In vitro, mediates the uptake of linear DNA more efficiently than that of circular DNA, but exhibits similar uptake efficacy toward RNA and DNA (PubMed:27846365). Binds long double-stranded RNA (dsRNA) (500 - 700 base pairs), but not dsRNA shorter than 100 bp (PubMed:26067272). {ECO:0000269|PubMed:26067272, ECO:0000269|PubMed:27046251, ECO:0000269|PubMed:27846365, ECO:0000269|PubMed:28277980, ECO:0000269|PubMed:28724756}. PTM: Glycosylated. {ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:20965152}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:20965152, ECO:0000269|PubMed:27046251, ECO:0000269|PubMed:28724756}; Multi-pass membrane protein {ECO:0000269|PubMed:20965152}. Cell membrane {ECO:0000250|UniProtKB:Q8NBJ9}. Note=Mainly localizes to lysosomes and only partly to the plasma membrane (By similarity). Lysosomal localization is required for SIDT2-mediated intracellular degradation of endogenous RNA (PubMed:28724756). {ECO:0000250|UniProtKB:Q8NBJ9, ECO:0000269|PubMed:28724756}. SUBUNIT: Interacts with adapter protein complex 1 (AP-1) and AP-2, but not AP-3 and AP-4 (PubMed:28724756). Interacts with LAMP2 (PubMed:27046251). {ECO:0000269|PubMed:27046251, ECO:0000269|PubMed:28724756}. TISSUE SPECIFICITY: Widely expressed, including in the liver, brain and kidney (at protein level). {ECO:0000269|PubMed:20965152, ECO:0000269|PubMed:23776622, ECO:0000269|PubMed:27987306}. +Q9CPR7 SIKE1_MOUSE Suppressor of IKBKE 1 (Suppressor of IKK-epsilon) 207 23,522 Chain (1); Coiled coil (2); Sequence conflict (1) FUNCTION: Physiological suppressor of IKK-epsilon and TBK1 that plays an inhibitory role in virus- and TLR3-triggered IRF3. Inhibits TLR3-mediated activation of interferon-stimulated response elements (ISRE) and the IFN-beta promoter. May act by disrupting the interactions of IKBKE or TBK1 with TICAM1/TRIF, IRF3 and DDX58/RIG-I. Does not inhibit NF-kappa-B activation pathways (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with IKBKE and TBK1 via its coiled coil region. Interaction with TBK1 is disrupted upon viral infection or TLR3 stimulation. Interacts with CDC42BPB. {ECO:0000250|UniProtKB:Q9BRV8}. +G3X9R7 RN148_MOUSE RING finger protein 148 (Goliath-related E3 ubiquitin-protein ligase 3) 316 35,463 Chain (1); Domain (1); Glycosylation (1); Sequence conflict (2); Signal peptide (1); Transmembrane (2); Zinc finger (1) TRANSMEM 173 193 Helical. {ECO:0000255}.; TRANSMEM 204 224 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q99ML9 RN111_MOUSE E3 ubiquitin-protein ligase Arkadia (EC 2.3.2.27) (RING finger protein 111) (RING-type E3 ubiquitin transferase Arkadia) 989 107,896 Alternative sequence (1); Chain (1); Compositional bias (4); Cross-link (13); Metal binding (4); Motif (3); Mutagenesis (4); Region (3); Sequence conflict (4); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase required for mesoderm patterning during embryonic development (PubMed:11298452). Acts as an enhancer of the transcriptional responses of the SMAD2/SMAD3 effectors, which are activated downstream of BMP (PubMed:14657019). Acts by mediating ubiquitination and degradation of SMAD inhibitors such as SMAD7, inducing their proteasomal degradation and thereby enhancing the transcriptional activity of TGF-beta and BMP (PubMed:14657019). In addition to enhance transcription of SMAD2/SMAD3 effectors, also regulates their turnover by mediating their ubiquitination and subsequent degradation, coupling their activation with degradation, thereby ensuring that only effectors 'in use' are degraded (By similarity). Activates SMAD3/SMAD4-dependent transcription by triggering signal-induced degradation of SNON isoform of SKIL (By similarity). Associates with UBE2D2 as an E2 enzyme (By similarity). Specifically binds polysumoylated chains via SUMO interaction motifs (SIMs) and mediates ubiquitination of sumoylated substrates (PubMed:23530056). Catalyzes 'Lys-63'-linked ubiquitination of sumoylated XPC in response to UV irradiation, promoting nucleotide excision repair (By similarity). Mediates ubiquitination and degradation of sumoylated PML (PubMed:23530056). The regulation of the BMP-SMAD signaling is however independent of sumoylation and is not dependent of SUMO interaction motifs (SIMs) (PubMed:23530056). {ECO:0000250|UniProtKB:Q6ZNA4, ECO:0000269|PubMed:11298452, ECO:0000269|PubMed:14657019, ECO:0000269|PubMed:17341133, ECO:0000269|PubMed:23530056}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14657019}. Cytoplasm {ECO:0000250|UniProtKB:Q6ZNA4}. Nucleus, PML body {ECO:0000269|PubMed:23530056}. Note=Upon TGF-beta treatment, translocates from nucleus to cytosol. {ECO:0000250|UniProtKB:Q6ZNA4}. SUBUNIT: Monomer (By similarity). Interacts with SMAD6, SMAD7, AXIN1, AXIN2 and SKIL isoform SNON (PubMed:14657019). Interacts with (phosphorylated) SMAD2 and SMAD3 (PubMed:17341133). Part of a complex containing RNF111, AXIN1 and SMAD7 (By similarity). Interacts (via SIM domains) with SUMO1 and SUMO2 (PubMed:23530056). {ECO:0000250|UniProtKB:Q6ZNA4, ECO:0000269|PubMed:14657019, ECO:0000269|PubMed:17341133, ECO:0000269|PubMed:23530056}. DOMAIN: The SUMO interaction motifs (SIMs) mediates the binding to polysumoylated substrate. {ECO:0000269|PubMed:23530056}.; DOMAIN: The RING-type zinc finger mediates the E3 ubiquitin-protein ligase activity and binds directly to free ubiquitin. Non-covalent ubiquitin-binding stabilizes the ubiquitin-conjugating enzyme E2 (donor ubiquitin) in the 'closed' conformation and stimulates ubiquitin transfer. {ECO:0000250|UniProtKB:Q6ZSG1}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:11298452}. +Q9CWS1 RN135_MOUSE E3 ubiquitin-protein ligase RNF135 (EC 2.3.2.27) (RING finger protein 135) (RING-type E3 ubiquitin transferase RNF135) 417 46,462 Alternative sequence (1); Chain (1); Coiled coil (2); Domain (1); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: Acts as an E2-dependent E3 ubiquitin-protein ligase, involved in innate immune defense against viruses. Ubiquitinates DDX58 and is required for full activation of the DDX58 signaling resulting in interferon beta production. {ECO:0000250|UniProtKB:Q8IUD6}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8IUD6}. SUBUNIT: Interacts with DDX58. Interacts with PCBP2. {ECO:0000250|UniProtKB:Q8IUD6}. +Q96DY5 RN112_MOUSE RING finger protein 112 (EC 2.3.2.27) (Brain finger protein) (Neurolastin) (Zinc finger protein 179) 654 71,275 Alternative sequence (2); Chain (1); Domain (1); Frameshift (1); Mutagenesis (2); Nucleotide binding (1); Region (1); Sequence conflict (4); Transmembrane (2); Zinc finger (1) TRANSMEM 570 590 Helical. {ECO:0000255}.; TRANSMEM 603 623 Helical. {ECO:0000255}. Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that plays an important role in neuronal differentiation, including neurogenesis and gliogenesis, during brain development. During embryonic development initiates neuronal differentiation by inducing cell cycle arrest at the G0/G1 phase through up-regulation of cell-cycle regulatory proteins (PubMed:21566658, PubMed:28684796). Plays a role not only in the fetal period during the development of the nervous system, but also in the adult brain, where it is involved in the maintenance of neural functions and protection of the nervous tissue cells from oxidative stress-induced damage (PubMed:27918959, PubMed:26792191, PubMed:26951452). Exhibits GTPase and E3 ubiquitin-protein ligase activities. Regulates dendritic spine density and synaptic neurotransmission; its ability to hydrolyze GTP is involved in the maintenance of dendritic spine density (PubMed:26212327). {ECO:0000269|PubMed:21566658, ECO:0000269|PubMed:26212327, ECO:0000269|PubMed:26792191, ECO:0000269|PubMed:26951452, ECO:0000269|PubMed:27918959, ECO:0000269|PubMed:28684796}. PTM: Auto-ubiquitinated. {ECO:0000269|PubMed:26212327}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:26212327}; Multi-pass membrane protein {ECO:0000255}. Membrane {ECO:0000269|PubMed:26212327}; Peripheral membrane protein {ECO:0000269|PubMed:26212327}. Cytoplasm {ECO:0000269|PubMed:24359566, ECO:0000269|PubMed:27918959, ECO:0000269|PubMed:9806830}. Nucleus {ECO:0000269|PubMed:24359566, ECO:0000269|PubMed:26951452, ECO:0000269|PubMed:27918959, ECO:0000269|PubMed:9806830}. Nucleus, Nuclear body {ECO:0000269|PubMed:24359566}. Nucleus, nucleoplasm {ECO:0000269|PubMed:24359566}. Endosome {ECO:0000269|PubMed:26212327}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000269|PubMed:26212327}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000269|PubMed:26212327}. Note=Predominantly in the nucleus, but some amounts were also found in the cytoplasm (PubMed:9806830, PubMed:24359566). Oxidative stress stimulates its shuttling from the cytoplasm into the nucleus (PubMed:27918959). Recruited to nuclear bodies via its interaction with ZBTB16 (PubMed:24359566). Localizes to the cell soma and neuritis and only slightly to the nucleus in the neurons of most brain areas (PubMed:26951452). {ECO:0000269|PubMed:24359566, ECO:0000269|PubMed:26951452, ECO:0000269|PubMed:27918959, ECO:0000269|PubMed:9806830}. SUBUNIT: Self-associates (PubMed:26212327). Interacts with SP1 in an oxidative stress-regulated manner (PubMed:27918959). Interacts with SIGMAR1 in an oxidative stress-regulated manner (PubMed:26792191). Interacts with ZBTB16 (via C2H2-type zinc finger domains 1 and 2) (PubMed:24359566). {ECO:0000269|PubMed:24359566, ECO:0000269|PubMed:26212327, ECO:0000269|PubMed:26792191, ECO:0000269|PubMed:27918959}. TISSUE SPECIFICITY: Expressed in most of the brain areas, including cortex, striatum, hippocampus, thalamus, and cerebellum (at protein level). Expressed in lateral amygdaloid nucleus, and ventromedial hypothalamus. Also expressed strongly in the marginal zone of brain vesicles, optic stalk, and cartilage primordium. {ECO:0000269|PubMed:21566658, ECO:0000269|PubMed:26951452, ECO:0000269|PubMed:9806830}. +P00683 RNAS1_MOUSE Ribonuclease pancreatic (EC 3.1.27.5) (RNase 1) (RNase A) 149 16,820 Active site (2); Beta strand (7); Binding site (3); Chain (1); Disulfide bond (4); Helix (4); Region (1); Signal peptide (1); Turn (1) FUNCTION: Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single-stranded and double-stranded RNA (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Monomer. Interacts with and forms tight 1:1 complexes with RNH1. Dimerization of two such complexes may occur. Interaction with RNH1 inhibits this protein (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Pancreas. +D3YYI7 RN217_MOUSE Probable E3 ubiquitin-protein ligase RNF217 (EC 2.3.2.31) (IBR domain-containing protein 1) (RING finger protein 217) 515 56,036 Active site (1); Chain (1); Compositional bias (2); Metal binding (16); Region (1); Transmembrane (1); Zinc finger (3) TRANSMEM 476 496 Helical. {ECO:0000255}. Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. DOMAIN: Members of the RBR family are atypical E3 ligases. They interact with the E2 conjugating enzyme UBE2L3 and function like HECT-type E3 enzymes: they bind E2s via the first RING domain, but require an obligate trans-thiolation step during the ubiquitin transfer, requiring a conserved cysteine residue in the second RING domain. {ECO:0000250|UniProtKB:O60260}. +E9QAU8 RN165_MOUSE E3 ubiquitin-protein ligase RNF165 (EC 2.3.2.27) (Arkadia-like protein 2C) (Ark2C) (RING finger protein 165) 347 39,736 Chain (1); Metal binding (4); Region (2); Zinc finger (1) FUNCTION: E3 ubiquitin-protein ligase that acts as a regulator of motor axon elongation (PubMed:23610558). Required for efficient motor axon extension in the dorsal forelimb by enhancing the transcriptional responses of the SMAD1/SMAD5/SMAD8 effectors, which are activated downstream of BMP (PubMed:23610558). Acts by mediating ubiquitination and degradation of SMAD inhibitors such as SMAD6, SMAD7, SKI and SNON isoform of SKIL (PubMed:23610558). {ECO:0000269|PubMed:23610558}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23610558}. SUBUNIT: Monomer; binding to the ubiquitin-conjugating enzyme E2 does not trigger homodimerization. {ECO:0000250|UniProtKB:Q6ZSG1}. DOMAIN: The RING-type zinc finger mediates the E3 ubiquitin-protein ligase activity and binds directly to free ubiquitin. Non-covalent ubiquitin-binding stabilizes the ubiquitin-conjugating enzyme E2 (donor ubiquitin) in the 'closed' conformation and stimulates ubiquitin transfer. {ECO:0000250|UniProtKB:Q6ZSG1}. TISSUE SPECIFICITY: Expressed in neurons of the nervous system. {ECO:0000269|PubMed:23610558}. +Q91XF4 RN167_MOUSE E3 ubiquitin-protein ligase RNF167 (EC 2.3.2.27) (RING finger protein 167) (RING-type E3 ubiquitin transferase RNF167) 347 38,014 Chain (1); Domain (1); Glycosylation (1); Sequence conflict (1); Signal peptide (1); Transmembrane (1); Zinc finger (1) TRANSMEM 174 194 Helical. {ECO:0000255}. Protein modification; protein ubiquitination. FUNCTION: May act as an E3 ubiquitin-protein ligase, or as part of the E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, such as UBE2E1, and then transfers it to substrates, such as SLC22A18. May play a role in growth regulation involved in G1/S transition. {ECO:0000250}. PTM: Auto-ubiquitinated in vitro in the presence of UBE2D1 and UBE2E1. {ECO:0000250}. SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=Targeted to cytoplasmic membranes. {ECO:0000250}. SUBUNIT: Interacts with SLC22A18. {ECO:0000250}. +Q3UIW8 RN224_MOUSE RING finger protein 224 156 17,382 Chain (1); Zinc finger (1) +Q9D7D1 RN225_MOUSE RING finger protein 225 332 35,839 Chain (1); Compositional bias (1); Transmembrane (1); Zinc finger (1) TRANSMEM 205 225 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. +Q9DCB3 RN227_MOUSE RING finger protein 227 190 20,820 Chain (1); Erroneous initiation (2); Sequence conflict (2); Zinc finger (1) +Q9JI90 RNF14_MOUSE E3 ubiquitin-protein ligase RNF14 (EC 2.3.2.31) (Androgen receptor-associated protein 54) (Protein Triad2) (RING finger protein 14) 485 54,926 Active site (1); Alternative sequence (2); Chain (1); Compositional bias (2); Domain (1); Metal binding (24); Modified residue (1); Motif (1); Region (1); Sequence conflict (5); Zinc finger (3) FUNCTION: Might act as an E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes and then transfers it to substrates, which could be nuclear proteins. Could play a role as a coactivator for androgen- and, to a lesser extent, progesterone-dependent transcription (By similarity). {ECO:0000250}. PTM: RING-type zinc finger-dependent and UBE2E2-dependent autoubiquitination. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Interacts with the ubiquitin-conjugating enzymes UBE2E1 and UBE2E2. Interacts with AR/androgen receptor; testosterone- and RNF6-regulated it promotes AR transcriptional activity. {ECO:0000250}. DOMAIN: The N-terminal destruction box (D-box) could act as a recognition signal for degradation via the ubiquitin-proteasome pathway. {ECO:0000250}.; DOMAIN: The RING-type zinc finger is essential for the interaction with UBE2E2. {ECO:0000250}.; DOMAIN: Members of the RBR family are atypical E3 ligases. They interact with the E2 conjugating enzyme UBE2L3 and function like HECT-type E3 enzymes: they bind E2s via the first RING domain, but require an obligate trans-thiolation step during the ubiquitin transfer, requiring a conserved cysteine residue in the second RING domain. {ECO:0000250|UniProtKB:O60260}. +Q8BLR7 RND1_MOUSE Rho-related GTP-binding protein Rho6 (Rho family GTPase 1) (Rnd1) 232 26,034 Alternative sequence (2); Chain (1); Lipidation (1); Modified residue (1); Motif (1); Nucleotide binding (5); Propeptide (1) FUNCTION: Lacks intrinsic GTPase activity. Has a low affinity for GDP, and constitutively binds GTP. Controls rearrangements of the actin cytoskeleton. Induces the Rac-dependent neuritic process formation in part by disruption of the cortical actin filaments. Causes the formation of many neuritic processes from the cell body with disruption of the cortical actin filaments (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. SUBUNIT: Binds GRB7 and PLXNB1. Interacts with PLXNA2. Interacts with UBXD5 (By similarity). {ECO:0000250}. +Q924T7 RNF31_MOUSE E3 ubiquitin-protein ligase RNF31 (EC 2.3.2.31) (HOIL-1-interacting protein) (HOIP) (Putative Ariadne-like ubiquitin ligase) (PAUL) (RING finger protein 31) (RING-type E3 ubiquitin transferase RNF31) 1066 119,314 Active site (1); Alternative sequence (1); Chain (1); Domain (2); Helix (9); Metal binding (20); Modified residue (1); Region (4); Site (1); Turn (2); Zinc finger (6) FUNCTION: E3 ubiquitin-protein ligase component of the LUBAC complex which conjugates linear ('Met-1'-linked) polyubiquitin chains to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation (PubMed:28701375). LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways (By similarity). Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation (PubMed:28701375). Recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex (By similarity). Together with OTULIN, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis (By similarity). Binds polyubiquitin of different linkage types (By similarity). {ECO:0000250|UniProtKB:Q96EP0, ECO:0000269|PubMed:28701375}. PTM: Autoubiquitinated (PubMed:29950720). Interaction with OTULIN is required to suppress formation of 'Met-1'-linked polyubiquitin chains and prevent subsequent inactivation of the LUBAC complex (PubMed:29950720). {ECO:0000269|PubMed:29950720}.; PTM: Cleaved by caspase during apoptosis. {ECO:0000250|UniProtKB:Q96EP0}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14678832}. SUBUNIT: Component of the LUBAC complex (linear ubiquitin chain assembly complex) which consists of SHARPIN, RBCK1 and RNF31 (By similarity). LUBAC has a MW of approximately 600 kDa suggesting a heteromultimeric assembly of its subunits (By similarity). Associates with the TNF-R1 signaling complex (TNF-RSC) in a stimulation-dependent manner (By similarity). Interacts (via the PUB domain) with OTULIN (via the PIM motif); the interaction is direct (PubMed:23708998). Interacts (via the PUB domain) with VCP (via the PIM motif) (By similarity). Interacts (via the PUB domain) with SPATA2 (via the PIM motif); interaction is direct and bridges RNF31 and CYLD (By similarity). Interacts with CYLD; the interaction is indirect and is mediated via SPATA2 (By similarity). Interacts with MUSK (PubMed:14678832). {ECO:0000250|UniProtKB:Q96EP0, ECO:0000269|PubMed:14678832, ECO:0000269|PubMed:23708998}. DOMAIN: The PUB domain mediates interaction with the PIM motifs of VCP and RNF31, with a strong preference for RNF31. {ECO:0000250|UniProtKB:Q96EP0}.; DOMAIN: The RanBP2-type zinc fingers mediate the specific interaction with ubiquitin. {ECO:0000250|UniProtKB:Q96EP0}.; DOMAIN: The UBA domain mediates association with RBCK1/HOIL1 via interaction with its UBL domain. {ECO:0000250|UniProtKB:Q96EP0}.; DOMAIN: RING 1 and IBR zinc-fingers catalyze the first step transfer of ubiquitin from the E2 onto RING 2, to transiently form a HECT-like covalent thioester intermediate. {ECO:0000250|UniProtKB:Q96EP0}.; DOMAIN: The linear ubiquitin chain determining domain (LDD) mediates the final transfer of ubiquitin from RING 2 onto the N-terminus of a target ubiquitin. {ECO:0000250|UniProtKB:Q96EP0}. TISSUE SPECIFICITY: Widely expressed (at protein level). Not expressed in heart. {ECO:0000269|PubMed:14678832}. +P61588 RND3_MOUSE Rho-related GTP-binding protein RhoE (Rho family GTPase 3) (Rnd3) 244 27,368 Beta strand (5); Chain (1); Helix (9); Lipidation (1); Modified residue (1); Motif (1); Nucleotide binding (3); Propeptide (1); Turn (3) FUNCTION: Binds GTP but lacks intrinsic GTPase activity and is resistant to Rho-specific GTPase-activating proteins. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:12773565}; Peripheral membrane protein {ECO:0000269|PubMed:12773565}. SUBUNIT: Interacts with UBXD5 (By similarity). Binds ROCK1. {ECO:0000250, ECO:0000269|PubMed:12773565}. TISSUE SPECIFICITY: Ubiquitous. +Q5NCP0 RNF43_MOUSE E3 ubiquitin-protein ligase RNF43 (EC 2.3.2.27) (RING finger protein 43) (RING-type E3 ubiquitin transferase RNF43) 784 86,304 Alternative sequence (3); Chain (1); Compositional bias (3); Disulfide bond (1); Glycosylation (2); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1); Zinc finger (1) TRANSMEM 198 218 Helical. {ECO:0000255}. TOPO_DOM 24 197 Extracellular. {ECO:0000255}.; TOPO_DOM 219 784 Cytoplasmic. {ECO:0000255}. Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that acts as a negative regulator of the Wnt signaling pathway by mediating the ubiquitination, endocytosis and subsequent degradation of Wnt receptor complex components Frizzled. Acts on both canonical and non-canonical Wnt signaling pathway (PubMed:22895187). Along with RSPO2 and ZNRF3, constitutes a master switch that governs limb specification (By similarity). {ECO:0000250|UniProtKB:P0DPR2, ECO:0000269|PubMed:22895187}. PTM: Autoubiquitinated. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Nucleus envelope {ECO:0000250}. Note=May be secreted. {ECO:0000250}. SUBUNIT: Interacts with AKAP8L, NONO and SFPQ. Interacts with FZD5 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in crypt base columnar cells of small intestinal epithelium. Crypt base columnar cells are small cycling cells residing between the terminally differentiated Paneth cells at crypt bottoms. Colocalizes with Lgr5-positive stem cells. {ECO:0000269|PubMed:22895187}. +Q3UHJ8 RNF44_MOUSE RING finger protein 44 407 45,497 Alternative sequence (2); Chain (1); Compositional bias (1); Erroneous initiation (2); Frameshift (1); Zinc finger (1) +Q9QZS2 RNF4_MOUSE E3 ubiquitin-protein ligase RNF4 (EC 2.3.2.27) (RING finger protein 4) (RING-type E3 ubiquitin transferase RNF4) 194 21,911 Chain (1); Modified residue (2); Motif (4); Mutagenesis (5); Region (2); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase which binds polysumoylated chains covalently attached to proteins and mediates 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination of those substrates and their subsequent targeting to the proteasome for degradation. Regulates the degradation of several proteins including PML and the transcriptional activator PEA3. Involved in chromosome alignment and spindle assembly, it regulates the kinetochore CENPH-CENPI-CENPK complex by targeting polysumoylated CENPI to proteasomal degradation. Regulates the cellular responses to hypoxia and heat shock through degradation of respectively EPAS1 and PARP1. Alternatively, it may also bind DNA/nucleosomes and have a more direct role in the regulation of transcription for instance enhancing basal transcription and steroid receptor-mediated transcriptional activation. {ECO:0000269|PubMed:20681948}. PTM: Sumoylated; conjugated by one or two SUMO1 moieties. {ECO:0000250}.; PTM: Autoubiquitinated. {ECO:0000269|PubMed:20681948}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Nucleus, PML body {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. SUBUNIT: Homodimer (via RING-type zinc finger domain). Interacts with AR/the androgen receptor and TBP (By similarity). Interacts with PATZ1 (By similarity). Interacts with PML; SUMO1-dependent. Interacts with PML; SUMO2-dependent (By similarity). Interacts with TRPS1; negatively regulates the TRPS1 transcriptional repressor activity. Interacts with GSC2. Interacts with TCF20. Interacts with PARP1. Interacts with PML (By similarity). {ECO:0000250}. DOMAIN: The SUMO interaction motifs (SIMs) mediates the binding to polysumoylated substrate. {ECO:0000250|UniProtKB:P78317}.; DOMAIN: The RING-type zinc finger domain is required for the ubiquitination of polysumoylated substrates. {ECO:0000250|UniProtKB:O88846}. TISSUE SPECIFICITY: In the embryo, expressed primarily in the developing nervous system with strong expression in the dorsal root ganglia and gonads. Ubiquitously expressed in the adult. +O70338 RNH1_MOUSE Ribonuclease H1 (RNase H1) (EC 3.1.26.4) 285 31,805 Chain (1); Domain (1); Metal binding (5); Sequence conflict (1) FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. Plays a role in RNA polymerase II (RNAp II) transcription termination by degrading R-loop RNA-DNA hybrid formation at G-rich pause sites located downstream of the poly(A) site and behind the elongating RNAp II. {ECO:0000250|UniProtKB:O60930}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. SUBUNIT: Monomer. {ECO:0000250}. +Q9DCN7 RNFT1_MOUSE E3 ubiquitin-protein ligase RNFT1 (EC 2.3.2.27) (RING finger and transmembrane domain-containing protein 1) 395 45,277 Chain (1); Region (1); Sequence conflict (2); Transmembrane (6); Zinc finger (1) TRANSMEM 118 138 Helical. {ECO:0000255}.; TRANSMEM 165 185 Helical. {ECO:0000255}.; TRANSMEM 193 213 Helical. {ECO:0000255}.; TRANSMEM 216 236 Helical. {ECO:0000255}.; TRANSMEM 258 278 Helical. {ECO:0000255}.; TRANSMEM 283 303 Helical. {ECO:0000255}. Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that acts in the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway, which targets misfolded proteins that accumulate in the endoplasmic reticulum (ER) for ubiquitination and subsequent proteasome-mediated degradation. Protects cells from ER stress-induced apoptosis. {ECO:0000250|UniProtKB:Q5M7Z0}. SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000250|UniProtKB:Q5M7Z0}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Predominantly expressed in testis. {ECO:0000269|PubMed:17074343, ECO:0000269|PubMed:27485036}. +Q80ZV0 RNH2B_MOUSE Ribonuclease H2 subunit B (RNase H2 subunit B) (Deleted in lymphocytic leukemia 8 homolog) (Ribonuclease HI subunit B) 308 34,729 Beta strand (7); Chain (1); Helix (9); Initiator methionine (1); Modified residue (3); Sequence conflict (1); Turn (7) FUNCTION: Non catalytic subunit of RNase H2, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging-strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA:RNA duplexes. {ECO:0000269|PubMed:19923215}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: The RNase H2 complex is a heterotrimer composed of the catalytic subunit RNASEH2A and the non-catalytic subunits RNASEH2B and RNASEH2C. {ECO:0000269|PubMed:19923215}. +Q9D706 RPAP3_MOUSE RNA polymerase II-associated protein 3 660 74,096 Chain (1); Compositional bias (1); Cross-link (1); Initiator methionine (1); Modified residue (6); Repeat (7) FUNCTION: Forms an interface between the RNA polymerase II enzyme and chaperone/scaffolding protein, suggesting that it is required to connect RNA polymerase II to regulators of protein complex formation. {ECO:0000250}. SUBUNIT: Tightly associated with the RNA polymerase II complex. Component of the R2TP complex composed at least of PIHD1, RUVBL1, RUVBL2 and RPAP3. Interacts with PIH1D1. {ECO:0000250|UniProtKB:Q9H6T3}. +Q99JH1 RP25L_MOUSE Ribonuclease P protein subunit p25-like protein (RNase P protein subunit-like p25) (Rpp25-like protein) 163 17,675 Chain (1); Sequence conflict (1) FUNCTION: May be a component of ribonuclease P or MRP. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +P97760 RPB3_MOUSE DNA-directed RNA polymerase II subunit RPB3 (RNA polymerase II subunit 3) (RNA polymerase II subunit B3) (DNA-directed RNA polymerase II 33 kDa polypeptide) (RPB33) (DNA-directed RNA polymerase II subunit C) (RPB31) 275 31,443 Chain (1); Compositional bias (1); Modified residue (2); Sequence conflict (6) FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB3 is part of the core element with the central large cleft and the clamp element that moves to open and close the cleft (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the RNA polymerase II (Pol II) complex consisting of 12 subunits. RPB11/POLR2J and RPB3/POLR2C subunits interact with each other. +P52432 RPAC1_MOUSE DNA-directed RNA polymerases I and III subunit RPAC1 (DNA-directed RNA polymerase I subunit C) (RNA polymerases I and III subunit AC1) (AC40) (DNA-directed RNA polymerases I and III 40 kDa polypeptide) (RPA40) (RPC40) 346 39,107 Chain (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (1); Mutagenesis (2); Sequence conflict (2) FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I and III which synthesize ribosomal RNA precursors and small RNAs, such as 5S rRNA and tRNAs, respectively. RPAC1 is part of the Pol core element with the central large cleft and probably a clamp element that moves to open and close the cleft (By similarity). {ECO:0000250|UniProtKB:O15160, ECO:0000250|UniProtKB:P07703}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O15160}. SUBUNIT: Component of the RNA polymerase I (Pol I) and RNA polymerase III (Pol III) complexes consisting of at least 13 and 17 subunits, respectively. {ECO:0000250|UniProtKB:O15160}. +Q9D7M8 RPB4_MOUSE DNA-directed RNA polymerase II subunit RPB4 (RNA polymerase II subunit B4) (DNA-directed RNA polymerase II subunit D) 142 16,311 Chain (1); Erroneous initiation (1) FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB4 is part of a subcomplex with RPB7 that binds to a pocket formed by RPB1, RPB2 and RPB6 at the base of the clamp element. The RBP4-RPB7 subcomplex seems to lock the clamp via RPB7 in the closed conformation thus preventing double-stranded DNA to enter the active site cleft. The RPB4-RPB7 subcomplex binds single-stranded DNA and RNA (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the RNA polymerase II (Pol II) complex consisting of 12 subunits. RPB4 and RPB7 form a subcomplex that protrudes from the 10-subunit Pol II core complex (By similarity). {ECO:0000250}. +P08775 RPB1_MOUSE DNA-directed RNA polymerase II subunit RPB1 (RNA polymerase II subunit B1) (EC 2.7.7.6) (DNA-directed RNA polymerase II subunit A) (DNA-directed RNA polymerase III largest subunit) 1970 217,176 Chain (1); Metal binding (13); Modified residue (69); Mutagenesis (16); Region (2); Repeat (52); Sequence conflict (2) FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Forms the polymerase active center together with the second largest subunit. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB1 is part of the core element with the central large cleft, the clamp element that moves to open and close the cleft and the jaws that are thought to grab the incoming DNA template. At the start of transcription, a single-stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol II. A bridging helix emanates from RPB1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol II by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition. During transcription elongation, Pol II moves on the template as the transcript elongates (By similarity). Elongation is influenced by the phosphorylation status of the C-terminal domain (CTD) of Pol II largest subunit (RPB1), which serves as a platform for assembly of factors that regulate transcription initiation, elongation, termination and mRNA processing (By similarity). Regulation of gene expression levels depends on the balance between methylation and acetylation levels of tha CTD-lysines (PubMed:26687004). Initiation or early elongation steps of transcription of growth-factors-induced immediate early genes are regulated by the acetylation status of the CTD (PubMed:24207025). Methylation and dimethylation have a repressive effect on target genes expression (PubMed:26687004). {ECO:0000250|UniProtKB:P24928, ECO:0000269|PubMed:24207025, ECO:0000269|PubMed:26687004}. PTM: The tandem heptapeptide repeats in the C-terminal domain (CTD) can be highly phosphorylated. The phosphorylation activates Pol II. Phosphorylation occurs mainly at residues 'Ser-2' and 'Ser-5' of the heptapeptide repeat and is mediated, at least, by CDK7 and CDK9. CDK7 phosphorylation of POLR2A associated with DNA promotes transcription initiation by triggering dissociation from DNA. Phosphorylation also takes place at 'Ser-7' of the heptapeptide repeat, which is required for efficient transcription of snRNA genes and processing of the transcripts. The phosphorylation state is believed to result from the balanced action of site-specific CTD kinases and phosphatases, and a 'CTD code' that specifies the position of Pol II within the transcription cycle has been proposed. Dephosphorylated by the protein phosphatase CTDSP1. {ECO:0000250|UniProtKB:P24928}.; PTM: Among tandem heptapeptide repeats of the C-terminal domain (CTD) some do not match the Y-S-P-T-S-P-S consensus, the seventh serine residue 'Ser-7' being replaced by a lysine. 'Lys-7' in these non-consensus heptapeptide repeats can be alternatively acetylated, methylated and dimethylated. EP300 is one of the enzyme able to acetylate 'Lys-7'. Acetylation at 'Lys-7' of non-consensus heptapeptide repeats is associated with 'Ser-2' phosphorylation and active transcription. It may regulate initiation or early elongation steps of transcription specially for inducible genes. {ECO:0000269|PubMed:24207025, ECO:0000269|PubMed:26687004}.; PTM: Ubiquitinated by WWP2 leading to proteasomal degradation (PubMed:17526739). Following UV treatment, the elongating form of RNA polymerase II (RNA pol IIo) is ubiquitinated on UV damage sites without leading to degradation: ubiquitination is facilitated by KIAA1530/UVSSA and promotes RNA pol IIo backtracking to allow access to the nucleotide excision repair machinery (By similarity). {ECO:0000250|UniProtKB:P24928, ECO:0000269|PubMed:17526739}.; PTM: Methylated at Arg-1810 prior to transcription initiation when the CTD is hypophosphorylated, phosphorylation at Ser-1805 and Ser-1808 preventing this methylation. Symmetrically or asymmetrically dimethylated at Arg-1810 by PRMT5 and CARM1 respectively. Symmetric or asymmetric dimethylation modulates interactions with CTD-binding proteins like SMN1/SMN2 and TDRD3. SMN1/SMN2 interacts preferentially with the symmetrically dimethylated form while TDRD3 interacts with the asymmetric form. Through the recruitment of SMN1/SMN2, symmetric dimethylation is required for resolving RNA-DNA hybrids created by RNA polymerase II, that form R-loop in transcription terminal regions, an important step in proper transcription termination. CTD dimethylation may also facilitate the expression of select RNAs. Among tandem heptapeptide repeats of the C-terminal domain (CTD) some do not match the Y-S-P-T-S-P-S consensus, the seventh serine residue 'Ser-7' being replaced by a lysine. 'Lys-7' in these non-consensus heptapeptide repeats can be alternatively acetylated, methylated, dimethylated and trimethylated. Methylation occurs in the earliest transcription stages and precedes or is concomitant to 'Ser-5' and 'Ser-7' phosphorylation. Dimethylation and trimehtylation at 'Lys-7' of non-consensus heptapeptide repeats are exclusively associated with phosphorylated CTD. {ECO:0000250|UniProtKB:P24928, ECO:0000269|PubMed:26687004}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24207025, ECO:0000269|PubMed:26687004}. Cytoplasm {ECO:0000250|UniProtKB:P24928}. Note=Hypophosphorylated form is mainly found in the cytoplasm, while the hyperphosphorylated and active form is nuclear. {ECO:0000250|UniProtKB:P24928}. SUBUNIT: Component of the RNA polymerase II (Pol II) complex consisting of 12 subunits. Component of a complex which is at least composed of HTATSF1/Tat-SF1, the P-TEFb complex components CDK9 and CCNT1, RNA polymerase II, SUPT5H, and NCL/nucleolin. The large PER complex involved in the repression of transcriptional termination is composed of at least PER2, CDK9, DDX5, DHX9, NCBP1 and POLR2A (active). Interacts (via the C-terminal domain (CTD)) with U2AF2; recruits PRPF19 and the Prp19 complex to the pre-mRNA and may couple transcription to pre-mRNA splicing. Interacts (via the C-terminal domain (CTD)) with SMN1/SMN2; recruits SMN1/SMN2 to RNA Pol II elongation complexes. Interacts via the phosphorylated C-terminal domain with WDR82 and with SETD1A and SETD1B only in the presence of WDR82. When phosphorylated at 'Ser-5', interacts with MEN1; the unphosphorylated form, or phosphorylated at 'Ser-2' does not interact. When phosphorylated at 'Ser-2', interacts with SUPT6H (via SH2 domain). Interacts with RECQL5 and TCEA1; binding of RECQL5 prevents TCEA1 binding. The phosphorylated C-terminal domain interacts with FNBP3 and SYNCRIP. Interacts with ATF7IP. Interacts with DDX5. Interacts with WWP2. Interacts with SETX. Interacts (phosphorylated) with PIH1D1. Interacts (via the C-terminal domain (CTD)) with TDRD3. Interacts with PRMT5. Interacts with XRN2. Interacts with SAFB/SAFB1. Interacts with CCNL1. Interacts with CCNL2, MYO1C, PAF1 and SFRS19. Interacts (via C-terminus) with CMTR1, CTDSP1 and SCAF8. Interacts (via the C-terminal domain (CTD)) with CCNT2 (By similarity). Interacts with FUS (By similarity). {ECO:0000250|UniProtKB:P24928, ECO:0000269|PubMed:11030652, ECO:0000269|PubMed:17526739, ECO:0000269|PubMed:19141475, ECO:0000269|PubMed:22767893, ECO:0000269|PubMed:8692929}. DOMAIN: The C-terminal domain (CTD) serves as a platform for assembly of factors that regulate transcription initiation, elongation, termination and mRNA processing. {ECO:0000305}. +Q9R0X5 RPGR_MOUSE X-linked retinitis pigmentosa GTPase regulator (mRpgr) 1001 111,801 Alternative sequence (6); Chain (1); Compositional bias (1); Erroneous initiation (3); Lipidation (1); Modified residue (2); Propeptide (1); Repeat (6); Sequence conflict (5) FUNCTION: Could be a guanine-nucleotide releasing factor (By similarity). Plays a role in ciliogenesis (By similarity). Probably regulates cilia formation by regulating actin stress filaments and cell contractility (By similarity). May be involved in microtubule organization and regulation of transport in primary cilia (By similarity). Plays an important role in photoreceptor integrity. Isoform 5 may play a critical role in spermatogenesis and in intraflagellar transport processes. {ECO:0000250, ECO:0000269|PubMed:18579752, ECO:0000269|PubMed:22563472}. PTM: Prenylated. {ECO:0000269|PubMed:9677393}. SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:15772089, ECO:0000269|PubMed:16043481, ECO:0000269|PubMed:20007830, ECO:0000269|PubMed:9677393}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 5: Cytoplasm, cytoskeleton, cilium basal body. Cytoplasm, cytoskeleton, cilium axoneme. Cytoplasm, cytoskeleton, flagellum axoneme. SUBUNIT: Interacts with PDE6D, RPGRIP1 and RPGRIP1L; PDE6D, RPGRIP1 and RPGRIP1L may compete for the same binding sites (By similarity). Interacts with NPM1 (By similarity). Interacts with PDE6D. Isoform 5 interacts (via N-terminus) with SMC1A and SMC3. Isoform 5 interacts with CEP290. Interacts with WHRN. {ECO:0000250|UniProtKB:Q92834, ECO:0000269|PubMed:16043481, ECO:0000269|PubMed:22323458, ECO:0000269|PubMed:9990021}. DOMAIN: The RCC1 repeat region mediates interactions with RPGRIP1. {ECO:0000250|UniProtKB:Q92834}. TISSUE SPECIFICITY: Colocalizes with either CEP290, WHRN or RPGRIP1 in the photoreceptor connecting cilium, a thin bridge linking the cell body and the light-sensing outer segment. Expressed in kidney. Isoforms 1 and 5 expressed in retina (at protein level). Widely expressed with highest levels in brain and testis and low levels in eye. {ECO:0000269|PubMed:10401007, ECO:0000269|PubMed:12140192, ECO:0000269|PubMed:16632484, ECO:0000269|PubMed:18579752, ECO:0000269|PubMed:20007830, ECO:0000269|PubMed:20805823, ECO:0000269|PubMed:21546531, ECO:0000269|PubMed:22323458, ECO:0000269|PubMed:9677393}. +Q8BPX9 S15A3_MOUSE Solute carrier family 15 member 3 (Peptide transporter 3) (Peptide/histidine transporter 2) (cAMP-inducible gene 1 protein) 578 64,051 Chain (1); Compositional bias (2); Glycosylation (3); Sequence conflict (1); Transmembrane (12) TRANSMEM 33 53 Helical. {ECO:0000255}.; TRANSMEM 77 97 Helical. {ECO:0000255}.; TRANSMEM 102 122 Helical. {ECO:0000255}.; TRANSMEM 155 175 Helical. {ECO:0000255}.; TRANSMEM 201 221 Helical. {ECO:0000255}.; TRANSMEM 232 252 Helical. {ECO:0000255}.; TRANSMEM 308 328 Helical. {ECO:0000255}.; TRANSMEM 367 387 Helical. {ECO:0000255}.; TRANSMEM 405 425 Helical. {ECO:0000255}.; TRANSMEM 462 481 Helical. {ECO:0000255}.; TRANSMEM 494 514 Helical. {ECO:0000255}.; TRANSMEM 538 558 Helical. {ECO:0000255}. FUNCTION: Proton oligopeptide cotransporter. Transports free histidine and certain di- and tripeptides (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Expressed highly in bone marrow derived macrophages, and weakly in spleen and lung. {ECO:0000269|PubMed:11004510}. +Q9CQF0 RM11_MOUSE 39S ribosomal protein L11, mitochondrial (L11mt) (MRP-L11) 192 20,680 Chain (1); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11279069}. SUBUNIT: Component of the mitochondrial ribosome large subunit (39S) which comprises a 16S rRNA and about 50 distinct proteins. {ECO:0000250|UniProtKB:Q9Y3B7}. +Q99N89 RM43_MOUSE 39S ribosomal protein L43, mitochondrial (L43mt) (MRP-L43) (Mitochondrial ribosomal protein bMRP36a) 183 20,203 Chain (1); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11279069}. SUBUNIT: Component of the mitochondrial ribosome large subunit (39S) which comprises a 16S rRNA and about 50 distinct proteins. {ECO:0000250|UniProtKB:Q8N983}. TISSUE SPECIFICITY: Ubiquitous with the highest levels in the liver, heart and kidneys. The skeletal muscle, brain and testis showed lower but detectable expression. Expression is coregulated with TWNK. {ECO:0000269|PubMed:15509589}. +Q9D1B9 RM28_MOUSE 39S ribosomal protein L28, mitochondrial (L28mt) (MRP-L28) 257 30,170 Chain (1); Erroneous initiation (7); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q13084}. SUBUNIT: Component of the mitochondrial ribosome large subunit (39S) which comprises a 16S rRNA and about 50 distinct proteins. Interacts with OXA1L. {ECO:0000250|UniProtKB:Q13084, ECO:0000250|UniProtKB:Q2HJJ1}. +Q921S7 RM37_MOUSE 39S ribosomal protein L37, mitochondrial (L37mt) (MRP-L37) 423 48,341 Chain (1); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9BZE1}. SUBUNIT: Component of the mitochondrial ribosome large subunit (39S) which comprises a 16S rRNA and about 50 distinct proteins. {ECO:0000250|UniProtKB:Q9BZE1}. +Q8BYR8 S41A2_MOUSE Solute carrier family 41 member 2 573 62,305 Chain (1); Modified residue (2); Topological domain (12); Transmembrane (11) TRANSMEM 163 183 Helical. {ECO:0000255}.; TRANSMEM 196 216 Helical. {ECO:0000255}.; TRANSMEM 246 266 Helical. {ECO:0000255}.; TRANSMEM 283 303 Helical. {ECO:0000255}.; TRANSMEM 314 334 Helical. {ECO:0000255}.; TRANSMEM 348 368 Helical. {ECO:0000255}.; TRANSMEM 377 397 Helical. {ECO:0000255}.; TRANSMEM 407 427 Helical. {ECO:0000255}.; TRANSMEM 470 490 Helical. {ECO:0000255}.; TRANSMEM 499 519 Helical. {ECO:0000255}.; TRANSMEM 544 564 Helical. {ECO:0000255}. TOPO_DOM 1 162 Extracellular. {ECO:0000255}.; TOPO_DOM 184 195 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 217 245 Extracellular. {ECO:0000250}.; TOPO_DOM 267 282 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 304 313 Extracellular. {ECO:0000250}.; TOPO_DOM 335 347 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 369 376 Extracellular. {ECO:0000250}.; TOPO_DOM 398 406 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 428 469 Extracellular. {ECO:0000250}.; TOPO_DOM 491 498 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 520 543 Extracellular. {ECO:0000250}.; TOPO_DOM 565 573 Cytoplasmic. {ECO:0000250}. FUNCTION: Acts as a plasma-membrane magnesium transporter. {ECO:0000250, ECO:0000269|PubMed:15809054}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +P58355 S45A2_MOUSE Membrane-associated transporter protein (Melanoma antigen AIM1) (Protein AIM-1) (Protein underwhite) (Solute carrier family 45 member 2) 530 57,961 Chain (1); Glycosylation (1); Natural variant (2); Topological domain (13); Transmembrane (12) TRANSMEM 46 66 Helical; Name=1. {ECO:0000255}.; TRANSMEM 69 89 Helical; Name=2. {ECO:0000255}.; TRANSMEM 106 126 Helical; Name=3. {ECO:0000255}.; TRANSMEM 139 159 Helical; Name=4. {ECO:0000255}.; TRANSMEM 185 205 Helical; Name=5. {ECO:0000255}.; TRANSMEM 217 237 Helical; Name=6. {ECO:0000255}.; TRANSMEM 319 339 Helical; Name=7. {ECO:0000255}.; TRANSMEM 367 387 Helical; Name=8. {ECO:0000255}.; TRANSMEM 399 419 Helical; Name=9. {ECO:0000255}.; TRANSMEM 426 446 Helical; Name=10. {ECO:0000255}.; TRANSMEM 478 498 Helical; Name=11. {ECO:0000255}.; TRANSMEM 505 525 Helical; Name=12. {ECO:0000255}. TOPO_DOM 1 45 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 67 68 Extracellular. {ECO:0000255}.; TOPO_DOM 90 105 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 127 138 Extracellular. {ECO:0000255}.; TOPO_DOM 160 184 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 206 216 Extracellular. {ECO:0000255}.; TOPO_DOM 238 318 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 340 366 Extracellular. {ECO:0000255}.; TOPO_DOM 388 398 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 420 425 Extracellular. {ECO:0000255}.; TOPO_DOM 447 477 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 499 504 Extracellular. {ECO:0000255}.; TOPO_DOM 526 530 Cytoplasmic. {ECO:0000255}. FUNCTION: Melanocyte differentiation antigen. May transport substances required for melanin biosynthesis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Melanosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Melanocytes, eyes, kidney and uterus. DISEASE: Note=Defects in Slc45a2 are the cause of the UW-dbr phenotype that results in loss of nearly all pigmentation in the homozygous state. {ECO:0000269|PubMed:11574907}. +Q8K0H7 S45A3_MOUSE Solute carrier family 45 member 3 (Prostate cancer-associated protein 6) (Prostein) 553 59,742 Chain (1); Transmembrane (11) TRANSMEM 19 39 Helical; Name=1. {ECO:0000255}.; TRANSMEM 52 72 Helical; Name=2. {ECO:0000255}.; TRANSMEM 88 108 Helical; Name=3. {ECO:0000255}.; TRANSMEM 120 140 Helical; Name=4. {ECO:0000255}.; TRANSMEM 161 181 Helical; Name=5. {ECO:0000255}.; TRANSMEM 198 218 Helical; Name=6. {ECO:0000255}.; TRANSMEM 275 295 Helical; Name=7. {ECO:0000255}.; TRANSMEM 323 343 Helical; Name=8. {ECO:0000255}.; TRANSMEM 353 373 Helical; Name=9. {ECO:0000255}.; TRANSMEM 382 402 Helical; Name=10. {ECO:0000255}.; TRANSMEM 522 542 Helical; Name=11. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in the epididymis. {ECO:0000269|PubMed:14561649}. +Q8BFX1 RN187_MOUSE E3 ubiquitin-protein ligase RNF187 (EC 2.3.2.27) (RING domain AP1 coactivator 1) (RACO-1) (RING finger protein 187) (RING-type E3 ubiquitin transferase RNF187) 236 26,313 Chain (1); Cross-link (3); Erroneous initiation (4); Modified residue (3); Sequence caution (4); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that acts as a coactivator of JUN-mediated gene activation in response to growth factor signaling via the MAP3K1 pathway, independently from MAPK8. {ECO:0000250|UniProtKB:Q5TA31}. PTM: Ubiquitinated; undergoes 'Lys-48'-linked autoubiquitination in the absence of growth factors and MAP3K1-induced 'Lys-63'-linked polyubiquitination. 'Lys-48'-autoubiquitination leads to degradation by the proteasome, while MAP3K1-induced 'Lys-63'-linked polyubiquitination results in the stabilization of the protein. 'Lys-48'- and 'Lys-63'-linked polyubiquitinations occur most probably on the same 3 C-terminal lysine residues (Lys-195, Lys-224 and Lys-225) and are thus mutually exclusive. Other sites of ubiquitination are not excluded. 'Lys-63'-linked polyubiquitination by TRIM7 in response to growth factor signaling via the MEK/ERK pathway enhances protein stability. {ECO:0000250|UniProtKB:Q5TA31}.; PTM: Arginine methylation by PRMT1 stabilizes RNF187 by facilitating K63-linked ubiquitin chain formation, and enables dimerization, c-Jun interaction and subsequent AP1 target gene expression. {ECO:0000250|UniProtKB:Q5TA31}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q5TA31}. Nucleus {ECO:0000250|UniProtKB:Q5TA31}. Note=Shuttles between the cytoplasm and the nucleus. {ECO:0000250|UniProtKB:Q5TA31}. SUBUNIT: Homodimer (By similarity). Interacts with JUN, independently of JUN phosphorylation (PubMed:20852630). Interacts (via C-terminus) with TRIM7 (By similarity). {ECO:0000250|UniProtKB:Q5TA31, ECO:0000269|PubMed:20852630}. DOMAIN: The RING-type zinc finger domain is required for E3 ligase activity. {ECO:0000250}. +P50636 RN19A_MOUSE E3 ubiquitin-protein ligase RNF19A (EC 2.3.2.31) (Double ring-finger protein) (Dorfin) (Gametogenesis-expressed protein GEG-154) (RING finger protein 19A) (UBCM4-interacting protein 117) (UIP117) (XY body protein) (XYbp) 840 90,632 Active site (1); Chain (1); Frameshift (1); Metal binding (24); Modified residue (1); Region (2); Sequence conflict (2); Transmembrane (2); Zinc finger (3) TRANSMEM 368 388 Helical. {ECO:0000255}.; TRANSMEM 424 444 Helical. {ECO:0000255}. Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates, such as SNCAIP or CASR. {ECO:0000250, ECO:0000269|PubMed:10431818}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:10585566}. Note=Expressed primarily in the XY body of pachytene spermatocytes and in the centrosome of somatic and germ cells in all phases of the cell cycle. SUBUNIT: Interacts with UBE2L3 and UBE2L6. Also interacts with transcription factor Sp1. Interacts with SNCAIP and CASR (By similarity). Interacts with VCP. {ECO:0000250, ECO:0000269|PubMed:15456787}. DOMAIN: Members of the RBR family are atypical E3 ligases. They interact with the E2 conjugating enzyme UBE2L3 and function like HECT-type E3 enzymes: they bind E2s via the first RING domain, but require an obligate trans-thiolation step during the ubiquitin transfer, requiring a conserved cysteine residue in the second RING domain. {ECO:0000250|UniProtKB:O60260}. +Q9D244 RNAS6_MOUSE Ribonuclease K6 (RNase K6) (EC 3.1.27.-) 153 17,675 Active site (2); Binding site (1); Chain (1); Disulfide bond (4); Glycosylation (2); Region (1); Sequence conflict (1); Signal peptide (1); Site (2) FUNCTION: Ribonuclease which shows a preference for the pyrimidines uridine and cytosine (PubMed:15693621). Has potent antibacterial activity against a range of Gram-positive and Gram-negative bacteria, including P.aeruginosa, A.baumanii, M.luteus, S.aureus, E.faecalis, E.faecium, S.saprophyticus and E.coli (PubMed:15693621, PubMed:25075772). Causes loss of bacterial membrane integrity, and also promotes agglutination of Gram-negative bacteria (By similarity). Probably contributes to urinary tract sterility (PubMed:25075772). Bactericidal activity is independent of RNase activity (By similarity). {ECO:0000250|UniProtKB:Q93091, ECO:0000269|PubMed:15693621, ECO:0000269|PubMed:25075772}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25075772}. Lysosome {ECO:0000305|PubMed:25075772}. Cytoplasmic granule {ECO:0000269|PubMed:25075772}. SUBUNIT: Interacts (via N-terminus) with bacterial lipopolysaccharide (LPS). {ECO:0000250|UniProtKB:Q93091}. TISSUE SPECIFICITY: Highly expressed in spleen (at protein level) (PubMed:15693621, PubMed:25075772). Has little or no expression in healthy kidneys (at protein level) (PubMed:25075772). Detected at high levels in infected kidneys (at protein level) (PubMed:25075772). Expressed at low levels in bladder (PubMed:15693621, PubMed:25075772). Also detected in skeletal muscle, heart and bone marrow (PubMed:15693621). {ECO:0000269|PubMed:15693621}. +F6TQD1 RN212_MOUSE Probable E3 SUMO-protein ligase RNF212 (EC 2.3.2.-) (Probable E3 SUMO-protein transferase RNF212) (RING finger protein 212) 307 33,898 Alternative sequence (2); Chain (1); Coiled coil (1); Zinc finger (1) Protein modification; protein sumoylation. FUNCTION: SUMO E3 ligase that acts as a regulator of crossing-over during meiosis: required to couple chromosome synapsis to the formation of crossover-specific recombination complexes. Localizes to recombination sites and stabilizes meiosis-specific recombination factors, such as MutS-gamma complex proteins (MSH4 and MSH5) and TEX11. May mediate sumoylation of target proteins MSH4 and/or MSH5, leading to enhance their binding to recombination sites. Acts as a limiting factor for crossover designation and/or reinforcement and plays an antagonist role with CCNB1IP1/HEI10 in the regulation of meiotic recombination. {ECO:0000269|PubMed:23396135, ECO:0000269|PubMed:24390283}. SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Associates to the synaptonemal complex. Localizes to a minority of double-strand breaks (DSBs) sites. Marks crossover sites during midpachynema. TISSUE SPECIFICITY: Specifically expressed in meiocytes of the gonads. {ECO:0000269|PubMed:23396135}. +Q9D5A9 RNS10_MOUSE Inactive ribonuclease-like protein 10 (Protein Train A) 208 23,407 Chain (1); Erroneous initiation (1); Glycosylation (2); Sequence conflict (6); Signal peptide (1) FUNCTION: Secreted proximal epididymal protein required for post-testicular sperm maturation and male fertility. May be involved in sperm adhesion to the egg zona pellucida. Does not have ribonuclease activity. {ECO:0000269|PubMed:22750516}. PTM: The N-terminus is blocked. Glycosylated (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. TISSUE SPECIFICITY: Male-specific expression in proximal caput of the epididymis (at protein level). {ECO:0000269|PubMed:12920233, ECO:0000269|PubMed:14561640, ECO:0000269|PubMed:22750516}. +Q9D1M0 SEC13_MOUSE Protein SEC13 homolog (GATOR complex protein SEC13) (SEC13-like protein 1) (SEC13-related protein) 322 35,566 Chain (1); Initiator methionine (1); Modified residue (3); Repeat (6); Sequence conflict (2) FUNCTION: Functions as a component of the nuclear pore complex (NPC) and the COPII coat. At the endoplasmic reticulum, SEC13 is involved in the biogenesis of COPII-coated vesicles (By similarity). Required for the exit of adipsin (CFD/ADN), an adipocyte-secreted protein from the endoplasmic reticulum (PubMed:27354378). {ECO:0000250|UniProtKB:P55735, ECO:0000269|PubMed:27354378}.; FUNCTION: As a component of the GATOR subcomplex GATOR2, functions within the amino acid-sensing branch of the TORC1 signaling pathway. Indirectly activates mTORC1 and the TORC1 signaling pathway through the inhibition of the GATOR1 subcomplex. It is negatively regulated by the upstream amino acid sensors SESN2 and CASTOR1. {ECO:0000250|UniProtKB:P55735}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250|UniProtKB:P55735}; Peripheral membrane protein {ECO:0000250|UniProtKB:P55735}; Cytoplasmic side {ECO:0000250|UniProtKB:P55735}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P55735}; Peripheral membrane protein {ECO:0000250|UniProtKB:P55735}; Cytoplasmic side {ECO:0000250|UniProtKB:P55735}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P55735}. Lysosome membrane {ECO:0000250|UniProtKB:P55735}. Note=In interphase, localizes at both sides of the NPC. {ECO:0000250|UniProtKB:P55735}. SUBUNIT: At the nuclear pore: component of the Y-shaped Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex includes NUP160, NUP133, NUP107, NUP98, NUP85, NUP43, NUP37, SEH1 and SEC13. At the COPII coat complex: interacts with SEC31A and SEC31B. Within the GATOR complex, component of the GATOR2 subcomplex, made of MIOS, SEC13, SEH1L, WDR24 and WDR59. The GATOR complex strongly interacts with RRAGA/RRAGC and RRAGB/RRAGC heterodimers. The GATOR2 complex interacts with CASTOR2 and CASTOR1; the interaction is negatively regulated by arginine. The GATOR2 complex interacts with SESN1, SESN2 and SESN3; the interaction is negatively regulated by amino acids. Interacts with SEC16A. Interacts with SEC16B. {ECO:0000250|UniProtKB:P55735}. +Q8CFI7 RPB2_MOUSE DNA-directed RNA polymerase II subunit RPB2 (EC 2.7.7.6) (DNA-directed RNA polymerase II 140 kDa polypeptide) (DNA-directed RNA polymerase II subunit B) (RNA polymerase II subunit 2) (RNA polymerase II subunit B2) 1174 133,911 Chain (1); Erroneous initiation (1); Metal binding (5); Modified residue (2); Zinc finger (1) FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Second largest component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB2 is part of the core element with the central large cleft, the clamp element that moves to open and close the cleft and the jaws that are thought to grab the incoming DNA template (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the RNA polymerase II (Pol II) complex consisting of 12 subunits. Interacts with WDR82 (By similarity). Interacts with MEN1 (By similarity). {ECO:0000250}. +O35427 RPC9_MOUSE DNA-directed RNA polymerase III subunit RPC9 (RNA polymerase III subunit C9) (Calcitonin gene-related peptide-receptor component protein) (CGRP-RCP) (CGRP-receptor component protein) (CGRPRCP) 148 16,683 Chain (1) FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts induce type I interferon and NF- Kappa-B through the RIG-I pathway (By similarity). {ECO:0000250}.; FUNCTION: Accessory protein for the calcitonin gene-related peptide (CGRP) receptor. It modulates CGRP responsiveness in a variety of tissues. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:10903324}; Peripheral membrane protein {ECO:0000269|PubMed:10903324}; Cytoplasmic side {ECO:0000269|PubMed:10903324}. SUBUNIT: Component of the RNA polymerase III (Pol III) complex consisting of 17 subunits. Interacts with POLR3H/RPC8. POLR3H/RPC8 and CRCP/RPC9 probably form a Pol III subcomplex (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. Most prevalent in testis. {ECO:0000269|PubMed:10067875}. +Q9D483 RPC3_MOUSE DNA-directed RNA polymerase III subunit RPC3 (RNA polymerase III subunit C3) (DNA-directed RNA polymerase III subunit C) 533 60,706 Alternative sequence (2); Chain (1); Modified residue (1); Sequence conflict (1) FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. May direct with other members of the subcomplex RNA Pol III binding to the TFIIIB-DNA complex via the interactions between TFIIIB and POLR3F. May be involved either in the recruitment and stabilization of the subcomplex within RNA polymerase III, or in stimulating catalytic functions of other subunits during initiation. Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts induce type I interferon and NF-Kappa-B through the RIG-I pathway. Preferentially binds single-stranded DNA (ssDNA) in a sequence-independent manner. {ECO:0000250|UniProtKB:Q9BUI4}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Component of the RNA polymerase III (Pol III) complex consisting of 17 subunits (By similarity). RPC3/POLR3C, RPC6/POLR3F and RPC7/POLR3G form a Pol III subcomplex (By similarity). Directly interacts with POLR3G and POLR3GL. Directly interacts with POLR3F/RPC39. Interacts with GTF3C4. {ECO:0000250|UniProtKB:Q9BUI4}. +P97762 RP9_MOUSE Retinitis pigmentosa 9 protein homolog (Pim-1-associated protein) (PAP-1) 213 25,262 Chain (1); Compositional bias (2); Cross-link (1); Modified residue (2); Region (1); Zinc finger (1) FUNCTION: Is thought to be a target protein for the PIM1 kinase. May play some roles in B-cell proliferation in association with PIM1. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Binds to PIM1. Binds to ZNHIT4. TISSUE SPECIFICITY: Highly expressed in the testis, moderately in the kidney, liver and spleen, and weakly in the skeletal muscle and heart. +Q91WD1 RPC4_MOUSE DNA-directed RNA polymerase III subunit RPC4 (RNA polymerase III subunit C4) (DNA-directed RNA polymerase III subunit D) 398 44,357 Chain (1); Cross-link (12); Initiator methionine (1); Modified residue (5); Sequence conflict (1) FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts induce type I interferon and NF- Kappa-B through the RIG-I pathway (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the RNA polymerase III (Pol III) complex consisting of 17 subunits. Interacts with POLR3E/RPC5 (By similarity). {ECO:0000250}. +Q80TE0 RPAP1_MOUSE RNA polymerase II-associated protein 1 1409 155,270 Alternative sequence (2); Chain (1); Compositional bias (1); Erroneous initiation (1); Modified residue (1); Sequence conflict (48) FUNCTION: Forms an interface between the RNA polymerase II enzyme and chaperone/scaffolding protein, suggesting that it is required to connect RNA polymerase II to regulators of protein complex formation. Required for interaction of the RNA polymerase II complex with acetylated histone H3 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Part of an RNA polymerase II complex that contains POLR2A, POLR2B, POLR2C, POLR2D, POLR2E, POLR2F, POLR2G, POLR2H, POLR2I, POLR2J, POLR2K, POLR2L, RPAP1, FCP1 plus the general transcription factors TFIIB and TFIIF. {ECO:0000250}. +P51410 RL9_MOUSE 60S ribosomal protein L9 192 21,881 Chain (1); Modified residue (1); Natural variant (1) +Q9EQI8 RM46_MOUSE 39S ribosomal protein L46, mitochondrial (L46mt) (MRP-L46) 283 32,132 Chain (1); Modified residue (3); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9H2W6}. SUBUNIT: Component of the mitochondrial ribosome large subunit (39S) which comprises a 16S rRNA and about 50 distinct proteins. {ECO:0000250|UniProtKB:Q9H2W6}. +Q99N90 RM36_MOUSE 39S ribosomal protein L36, mitochondrial (L36mt) (MRP-L36) 102 11,545 Chain (1); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9P0J6}. SUBUNIT: Component of the mitochondrial ribosome large subunit (39S) which comprises a 16S rRNA and about 50 distinct proteins. {ECO:0000250|UniProtKB:Q9P0J6}. +Q3TLD5 RMP_MOUSE Unconventional prefoldin RPB5 interactor (Protein NNX3) (Protein phosphatase 1 regulatory subunit 19) (RNA polymerase II subunit 5-mediating protein) (RPB5-mediating protein) 531 59,084 Alternative sequence (1); Chain (1); Modified residue (3); Sequence conflict (5) FUNCTION: Involved in gene transcription regulation. Acts as a transcriptional repressor in concert with the corepressor UXT to regulate androgen receptor (AR) transcription. May act as a tumor suppressor to repress AR-mediated gene transcription and to inhibit anchorage-independent growth in prostate cancer cells. Required for cell survival in ovarian cancer cells. Together with UXT, associates with chromatin to the NKX3-1 promoter region (By similarity). {ECO:0000250}.; FUNCTION: Plays a central role in maintaining S6K1 signaling and BAD phosphorylation under normal growth conditions thereby protecting cells from potential deleterious effects of sustained S6K1 signaling. The URI1-PPP1CC complex acts as a central component of a negative feedback mechanism that counteracts excessive S6K1 survival signaling to BAD in response to growth factors. Mediates inhibition of PPP1CC phosphatase activity in mitochondria. Coordinates the regulation of nutrient-sensitive gene expression availability in a mTOR-dependent manner. Seems to be a scaffolding protein able to assemble a prefoldin-like complex that contains PFDs and proteins with roles in transcription and ubiquitination (By similarity). {ECO:0000250}. PTM: Phosphorylation occurs in response to androgen treatment in prostate cancer cells in a mTOR-dependent manner. Phosphorylated; hyperhosphorylated in mitochondria in a mTORC-dependent signaling pathway. Phosphorylated at Ser-369 by RPS6KB1 in a growth factor- and rapamycin-dependent manner. S6K1-mediated mitochondrial phosphorylation at Ser-369 disrupts the URI1-PPP1CC complex in the mitochondrion, relieves PPP1CC phosphatase inhibition activity and hence engages a negative feedback diminishing RPS6KB1 kinase activity, preventing sustained S6K1-dependent signaling (By similarity). Phosphorylated. Phosphorylation occurs essentially on serine residues. {ECO:0000250, ECO:0000269|PubMed:9878255}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9878255}. Cytoplasm {ECO:0000269|PubMed:9878255}. Mitochondrion {ECO:0000269|PubMed:9878255}. Cell projection, dendrite {ECO:0000250}. Note=Colocalizes with PFDN2, PFDN4, PPP1CC, RPS6KB1 and STAP1 in mitochondrion. SUBUNIT: Homodimer. Component of the URI complex that contains PFDN2, POLR2E/RPB5, RUVBL2, RUVBL1 and URI1. Interacts with PPP1CC; the interaction is phosphorylation-dependent and occurs in a growth factor-dependent manner. Interacts with PFDN2, PFDN4 and STAP1; the interactions are phosphorylation-dependent and occur in a growth-dependent manner in the mitochondrion. Interacts (via the middle C-terminal region) with GTF2F1 and GTF2F2. Interacts with DMAP1, POLR2E/RPB5 and UXT (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the spinal cord, ganglia, choroid plexus and olfactors epithelium of the developing brain. Expressed in skin, lung, kidney, testis and muscles (at protein level). Expressed strongly in brain and kidney. Expressed weakly in skeletal muscle, lung and liver. {ECO:0000269|PubMed:9878255}. +Q9CY62 RN181_MOUSE E3 ubiquitin-protein ligase RNF181 (EC 2.3.2.27) (RING finger protein 181) (RING-type E3 ubiquitin transferase RNF181) 165 19,101 Alternative sequence (2); Chain (1); Modified residue (1); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. {ECO:0000250|UniProtKB:Q9P0P0}. PTM: Auto-ubiquitinated as part of the enzymatic reaction. {ECO:0000250|UniProtKB:Q9P0P0}. SUBUNIT: Directly interacts with ITGA2B and, as a result, with integrin ITGA2B/ITGB3. There is no evidence that integrin ITGA2B/ITGB3 is an endogenous substrate for RNF181-directed ubiquitination. {ECO:0000250|UniProtKB:Q9P0P0}. +Q8BFU3 RN214_MOUSE RING finger protein 214 668 73,625 Alternative sequence (4); Chain (1); Coiled coil (1); Compositional bias (1); Erroneous initiation (3); Initiator methionine (1); Modified residue (9); Sequence caution (1); Sequence conflict (3); Zinc finger (1) +Q5SPX3 RN215_MOUSE RING finger protein 215 379 41,610 Chain (1); Compositional bias (1); Erroneous gene model prediction (2); Glycosylation (1); Sequence conflict (1); Topological domain (3); Transmembrane (2); Zinc finger (1) TRANSMEM 25 45 Helical. {ECO:0000255}.; TRANSMEM 253 273 Helical. {ECO:0000255}. TOPO_DOM 1 24 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 46 252 Extracellular. {ECO:0000255}.; TOPO_DOM 274 379 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q7TMV1 RN139_MOUSE E3 ubiquitin-protein ligase RNF139 (EC 2.3.2.27) (RING finger protein 139) (RING-type E3 ubiquitin transferase RNF139) (Translocation in renal carcinoma on chromosome 8 protein) 668 76,185 Chain (1); Initiator methionine (1); Modified residue (4); Sequence conflict (1); Transmembrane (11); Zinc finger (1) TRANSMEM 51 71 Helical. {ECO:0000255}.; TRANSMEM 85 105 Helical. {ECO:0000255}.; TRANSMEM 125 145 Helical. {ECO:0000255}.; TRANSMEM 154 174 Helical. {ECO:0000255}.; TRANSMEM 178 198 Helical. {ECO:0000255}.; TRANSMEM 293 313 Helical. {ECO:0000255}.; TRANSMEM 323 343 Helical. {ECO:0000255}.; TRANSMEM 356 376 Helical. {ECO:0000255}.; TRANSMEM 390 410 Helical. {ECO:0000255}.; TRANSMEM 420 440 Helical. {ECO:0000255}.; TRANSMEM 470 490 Helical. {ECO:0000255}. Protein modification; protein ubiquitination. FUNCTION: E3-ubiquitin ligase; acts as a negative regulator of the cell proliferation through mechanisms involving G2/M arrest and cell death. Required for MHC class I ubiquitination in cells expressing the cytomegalovirus protein US2 before dislocation from the endoplasmic reticulum (ER). Affects SREBP processing by hindering the SREBP/SCAP complex translocation from the ER to the Golgi, thereby reducing SREBF2 target gene expression. Required for INSIG1 ubiquitination. May be required for EIF3 complex ubiquitination. May function as a signaling receptor. {ECO:0000250|UniProtKB:Q8WU17}. PTM: Autoubiquitinated. Ubiquitination is induced by sterol and leads to ist degradation via the ubiquitin-proteasome pathway. {ECO:0000250|UniProtKB:Q8WU17}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SUBUNIT: Interacts with VHL. Interacts with MHC class I and HM13. Component of SCAP/SREBP complex composed of SREBF2, SCAP and RNF139; the complex hampers the interaction between SCAP and SEC24B, thereby reducing SREBF2 proteolytic processing. Interacts with SREBF2 (via C-terminal domain). Interacts with SCAP; the interaction inhibits the interaction of SCAP with SEC24B and hampering the ER to Golgi transport of the SCAP/SREBP complex. Interacts with SEC24B. Interacts with INSIG1 and INSIG2. Interacts with EIF3F and EIF3H; the interaction leads to protein translation inhibitions in a ubiquitination-dependent manner. Interacts with XBP1 isoform 1; the interaction induces ubiquitination and degradation of XBP1 isoform 1. {ECO:0000250|UniProtKB:Q8WU17}. DOMAIN: The RING-type zinc finger domain may be essential for ubiquitin ligase activity. {ECO:0000250|UniProtKB:O75485}. +Q8K2Y0 RN219_MOUSE RING finger protein 219 722 79,958 Alternative sequence (4); Chain (1); Coiled coil (2); Erroneous initiation (1); Modified residue (8); Zinc finger (1) +Q8K0W3 RN208_MOUSE RING finger protein 208 265 28,390 Chain (1); Erroneous initiation (1); Modified residue (1); Zinc finger (1) +Q8BIV3 RNBP6_MOUSE Ran-binding protein 6 (RanBP6) 1105 124,587 Chain (1); Erroneous initiation (2); Initiator methionine (1); Modified residue (1); Repeat (7); Sequence conflict (1) FUNCTION: May function in nuclear protein import as nuclear transport receptor. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. +Q5HZJ0 RNC_MOUSE Ribonuclease 3 (EC 3.1.26.3) (Protein Drosha) (Ribonuclease III) (RNase III) 1373 158,828 Chain (1); Compositional bias (2); Domain (3); Metal binding (14); Modified residue (2); Region (1); Site (1) FUNCTION: Ribonuclease III double-stranded (ds) RNA-specific endoribonuclease that is involved in the initial step of microRNA (miRNA) biogenesis. Component of the microprocessor complex that is required to process primary miRNA transcripts (pri-miRNAs) to release precursor miRNA (pre-miRNA) in the nucleus. Within the microprocessor complex, DROSHA cleaves the 3' and 5' strands of a stem-loop in pri-miRNAs (processing center 11 bp from the dsRNA-ssRNA junction) to release hairpin-shaped pre-miRNAs that are subsequently cut by the cytoplasmic DICER to generate mature miRNAs. Involved also in pre-rRNA processing. Cleaves double-strand RNA and does not cleave single-strand RNA. Involved in the formation of GW bodies. {ECO:0000250|UniProtKB:Q9NRR4}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NRR4}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9NRR4}. Note=A fraction is translocated to the nucleolus during the S phase of the cell cycle. Localized in GW bodies (GWBs), also known as P-bodies. {ECO:0000250|UniProtKB:Q9NRR4}. SUBUNIT: Component of the microprocessor complex, or pri-miRNA processing protein complex, which is composed of DROSHA and DGCR8. The microprocessor complex is a heterotrimer; each of the two DROSHA RNase III domains binds one DGCR8 (via C-terminal region). Interacts with SP1 and SNIP1 (By similarity). Interacts with SRRT/ARS2 (PubMed:19632182). {ECO:0000250|UniProtKB:Q9NRR4, ECO:0000269|PubMed:19632182}. DOMAIN: The 2 RNase III domains form an intramolecular dimer where the domain 1 cuts the 3'strand while the domain 2 cleaves the 5'strand of pri-miRNAs, independently of each other. {ECO:0000250|UniProtKB:Q9NRR4}. +Q99KR6 RNF34_MOUSE E3 ubiquitin-protein ligase RNF34 (EC 2.3.2.27) (Phafin-1) (RING finger protein 34) (RING-type E3 ubiquitin transferase RNF34) 376 42,030 Chain (1); Compositional bias (1); Domain (2); Modified residue (3); Site (1); Zinc finger (2) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that regulates several biological processes through the ubiquitin-mediated proteasomal degradation of various target proteins. Ubiquitinates the caspases CASP8 and CASP10, promoting their proteasomal degradation, to negatively regulate cell death downstream of death domain receptors in the extrinsic pathway of apoptosis. May mediate 'Lys-48'-linked polyubiquitination of RIPK1 and its subsequent proteasomal degradation thereby indirectly regulating the tumor necrosis factor-mediated signaling pathway. Negatively regulates p53/TP53 through its direct ubiquitination and targeting to proteasomal degradation. Indirectly, may also negatively regulate p53/TP53 through ubiquitination and degradation of SFN. Mediates PPARGC1A proteasomal degradation probably through ubiquitination thereby indirectly regulating the metabolism of brown fat cells (PubMed:22064484). Possibly involved in innate immunity, through 'Lys-48'-linked polyubiquitination of NOD1 and its subsequent proteasomal degradation. {ECO:0000250|UniProtKB:Q969K3, ECO:0000269|PubMed:22064484}. PTM: Autoubiquitinated (in vitro). {ECO:0000250|UniProtKB:Q6AYH3}.; PTM: Proteolytically cleaved by caspases upon induction of apoptosis by TNF. {ECO:0000250|UniProtKB:Q969K3}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q969K3}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q969K3}. Endomembrane system {ECO:0000250|UniProtKB:Q6AYH3}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q6AYH3}. Nucleus {ECO:0000250|UniProtKB:Q969K3}. Nucleus speckle {ECO:0000250|UniProtKB:Q969K3}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q969K3}. SUBUNIT: Interacts with CASP8 and CASP10. Interacts with p53/TP53; involved in p53/TP53 ubiquitination. Interacts (via RING-type zinc finger) with MDM2; the interaction stabilizes MDM2. Interacts (via RING-type zinc finger) with PPARGC1A. Interacts with NOD1. {ECO:0000250|UniProtKB:Q969K3}. DOMAIN: The RING-type zinc finger is required for the ubiquitination of target proteins. {ECO:0000250|UniProtKB:Q969K3}.; DOMAIN: The FYVE-type zinc finger domain is required for localization and may confer affinity for cellular compartments enriched in phosphatidylinositol 5-phosphate and phosphatidylinositol 3-phosphate phospholipids. {ECO:0000250|UniProtKB:Q969K3}. +Q8CIT9 SBSN_MOUSE Suprabasin 700 72,334 Alternative sequence (1); Chain (1); Coiled coil (1); Compositional bias (1); Sequence conflict (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15256262}. TISSUE SPECIFICITY: Detected in epidermis, in suprabasal keratinocytes. Detected in suprabasal layers of embryonic epidermis and in stratified layers of embryonic tongue and palate. Detected in adult stomach. {ECO:0000269|PubMed:12228223, ECO:0000269|PubMed:15256262}. +Q9WTV7 RNF12_MOUSE E3 ubiquitin-protein ligase RLIM (EC 2.3.2.27) (LIM domain-interacting RING finger protein) (RING finger LIM domain-binding protein) (R-LIM) (RING finger protein 12) (RING-type E3 ubiquitin transferase RLIM) 600 66,377 Chain (1); Compositional bias (2); Modified residue (6); Motif (1); Sequence conflict (11); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that acts as a negative coregulator for LIM homeodomain transcription factors by mediating the ubiquitination and subsequent degradation of LIM cofactors LDB1 and LDB2 and by mediating the recruitment the SIN3a/histone deacetylase corepressor complex. Ubiquitination and degradation of LIM cofactors LDB1 and LDB2 allows DNA-bound LIM homeodomain transcription factors to interact with other protein partners such as RLIM. Plays a role in telomere length-mediated growth suppression by mediating the ubiquitination and degradation of TERF1. By targeting ZFP42 for degradation, acts as an activator of random inactivation of X chromosome in the embryo, a stochastic process in which one X chromosome is inactivated to minimize sex-related dosage differences of X-encoded genes in somatic cells of female placental mammals. {ECO:0000269|PubMed:10431247, ECO:0000269|PubMed:11882901, ECO:0000269|PubMed:19945382, ECO:0000269|PubMed:22596162}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19945382}. SUBUNIT: Interacts (via N-terminus) with TERF1. Interacts (via C-terminus) with ESR1 (By similarity). Interacts with LIM/homeobox factors such as LHX3. Interacts with LDB1, LDB2 and SIN3A. Interacts with LIMK1. {ECO:0000250, ECO:0000269|PubMed:11882901, ECO:0000269|PubMed:16204183}. +Q8VC56 RNF8_MOUSE E3 ubiquitin-protein ligase RNF8 (EC 2.3.2.27) (ActA-interacting protein 37) (AIP37) (LaXp180) (RING finger protein 8) (RING-type E3 ubiquitin transferase RNF8) 488 55,517 Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (1); Frameshift (1); Modified residue (1); Mutagenesis (1); Region (1); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that plays a key role in DNA damage signaling via 2 distinct roles: by mediating the 'Lys-63'-linked ubiquitination of histones H2A and H2AX and promoting the recruitment of DNA repair proteins at double-strand breaks (DSBs) sites, and by catalyzing 'Lys-48'-linked ubiquitination to remove target proteins from DNA damage sites. Following DNA DSBs, it is recruited to the sites of damage by ATM-phosphorylated MDC1 and catalyzes the 'Lys-63'-linked ubiquitination of histones H2A and H2AX, thereby promoting the formation of TP53BP1 and BRCA1 ionizing radiation-induced foci (IRIF). Also controls the recruitment of UIMC1-BRCC3 (RAP80-BRCC36) and PAXIP1/PTIP to DNA damage sites. Also recruited at DNA interstrand cross-links (ICLs) sites and catalyzes 'Lys-63'-linked ubiquitination of histones H2A and H2AX, leading to recruitment of FAAP20 and Fanconi anemia (FA) complex, followed by interstrand cross-link repair. H2A ubiquitination also mediates the ATM-dependent transcriptional silencing at regions flanking DSBs in cis, a mechanism to avoid collision between transcription and repair intermediates. Promotes the formation of 'Lys-63'-linked polyubiquitin chains via interactions with the specific ubiquitin-conjugating UBE2N/UBC13 and ubiquitinates non-histone substrates such as PCNA. Substrates that are polyubiquitinated at 'Lys-63' are usually not targeted for degradation. Also catalyzes the formation of 'Lys-48'-linked polyubiquitin chains via interaction with the ubiquitin-conjugating UBE2L6/UBCH8, leading to degradation of substrate proteins such as CHEK2, JMJD2A/KDM4A and KU80/XRCC5: it is still unclear how the preference toward 'Lys-48'- versus 'Lys-63'-linked ubiquitination is regulated but it could be due to RNF8 ability to interact with specific E2 specific ligases. For instance, interaction with phosphorylated HERC2 promotes the association between RNF8 and UBE2N/UBC13 and favors the specific formation of 'Lys-63'-linked ubiquitin chains. Promotes non-homologous end joining (NHEJ) by promoting the 'Lys-48'-linked ubiquitination and degradation the of KU80/XRCC5. Following DNA damage, mediates the ubiquitination and degradation of JMJD2A/KDM4A in collaboration with RNF168, leading to unmask H4K20me2 mark and promote the recruitment of TP53BP1 at DNA damage sites. Following DNA damage, mediates the ubiquitination and degradation of POLD4/p12, a subunit of DNA polymerase delta. In the absence of POLD4, DNA polymerase delta complex exhibits higher proofreading activity. In addition to its function in damage signaling, also plays a role in higher-order chromatin structure by mediating extensive chromatin decondensation. Involved in the activation of ATM by promoting histone H2B ubiquitination, which indirectly triggers histone H4 'Lys-16' acetylation (H4K16ac), establishing a chromatin environment that promotes efficient activation of ATM kinase. Required in the testis, where it plays a role in the replacement of histones during spermatogenesis (PubMed:20153262, PubMed:28552346). At uncapped telomeres, promotes the joining of deprotected chromosome ends by inducing H2A ubiquitination and TP53BP1 recruitment, suggesting that it may enhance cancer development by aggravating telomere-induced genome instability in case of telomeric crisis. Promotes the assembly of RAD51 at DNA DSBs in the absence of BRCA1 and TP53BP1 Also involved in class switch recombination in immune system, via its role in regulation of DSBs repair. May be required for proper exit from mitosis after spindle checkpoint activation and may regulate cytokinesis. May play a role in the regulation of RXRA-mediated transcriptional activity. Not involved in RXRA ubiquitination by UBE2E2. {ECO:0000255|HAMAP-Rule:MF_03067, ECO:0000269|PubMed:20080757, ECO:0000269|PubMed:20153262, ECO:0000269|PubMed:21706008, ECO:0000269|PubMed:21857671, ECO:0000269|PubMed:22266820, ECO:0000269|PubMed:24953653, ECO:0000269|PubMed:28552346}. PTM: Autoubiquitinated through 'Lys-48' and 'Lys-63' of ubiquitin. 'Lys-63' polyubiquitination is mediated by UBE2N. 'Lys-29'-type polyubiquitination is also observed, but it doesn't require its own functional RING-type zinc finger. {ECO:0000255|HAMAP-Rule:MF_03067}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03067, ECO:0000269|PubMed:28552346}. Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03067, ECO:0000269|PubMed:28552346}. Midbody {ECO:0000255|HAMAP-Rule:MF_03067}. Chromosome, telomere {ECO:0000255|HAMAP-Rule:MF_03067, ECO:0000269|PubMed:21857671, ECO:0000269|PubMed:22101936}. Note=Recruited at uncapped telomeres (PubMed:21857671, PubMed:22101936). Following DNA double-strand breaks, recruited to the sites of damage. During prophase, concomitant with nuclear envelope breakdown, localizes throughout the cell, with a dotted pattern. In telophase, again in the nucleus and also with a discrete dotted pattern in the cytoplasm. In late telophase and during cytokinesis, localizes in the midbody of the tubulin bridge joining the daughter cells. Does not seem to be associated with condensed chromosomes at any time during the cell cycle (By similarity). During spermatogenesis, sequestered in the cytoplasm by PIWIL1: RNF8 is released following ubiquitination and degradation of PIWIL1 (PubMed:28552346). {ECO:0000255|HAMAP-Rule:MF_03067, ECO:0000269|PubMed:21857671, ECO:0000269|PubMed:22101936, ECO:0000269|PubMed:28552346}. SUBUNIT: Homodimer. Forms a E2-E3 ubiquitin ligase complex composed of the RNF8 homodimer and a E2 heterodimer of UBE2N and UBE2V2. Interacts with class III E2s, including UBE2E1, UBE2E2, and UBE2E3 and with UBE2N. Interacts with RXRA. Interacts (via FHA domain) with ATM-phosphorylated MDC1. Interacts (via FHA domain) with 'Thr-4829' phosphorylated HERC2 (via C-terminus) (By similarity). Interacts with PIWIL1; leading to sequester RNF8 in the cytoplasm (PubMed:28552346). Interacts with WRAP53/TCAB1 (By similarity). {ECO:0000255|HAMAP-Rule:MF_03067, ECO:0000269|PubMed:28552346}.; SUBUNIT: (Microbial infection) May interact with the L.monocytogenes protein actA; however, given these errors in the sequence (AJ242721), the relevance of the interaction with actA remains to be confirmed. {ECO:0000269|PubMed:11207567}. DOMAIN: The FHA domain specifically recognizes and binds ATM-phosphorylated MDC1 and phosphorylated HERC2 (By similarity). This domain is also required for proper recruitment to DNA damage sites after UV irradiation, ionizing radiation, or treatment with an alkylating agent (By similarity). {ECO:0000250|UniProtKB:O76064, ECO:0000255|HAMAP-Rule:MF_03067}. +C0HKG6 RNT2B_MOUSE Ribonuclease T2-B (EC 3.1.27.-) (Ribonuclease 6-B) 259 29,609 Active site (3); Chain (1); Disulfide bond (4); Glycosylation (3); Signal peptide (1) FUNCTION: Has ribonuclease activity, with higher activity at acidic pH. May play a role in cellular RNA catabolism. Probably is involved in lysosomal degradation of ribosomal RNA. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Endoplasmic reticulum lumen {ECO:0000250}. Lysosome lumen {ECO:0000250}. +Q6NXY9 RPC7_MOUSE DNA-directed RNA polymerase III subunit RPC7 (RNA polymerase III subunit C7) (DNA-directed RNA polymerase III subunit G) 223 25,947 Alternative sequence (2); Chain (1); Modified residue (2) FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. May direct with other members of the RPC3/POLR3C-RPC6/POLR3F-RPC7/POLR3G subcomplex RNA Pol III binding to the TFIIIB-DNA complex via the interactions between TFIIIB and POLR3F. May be involved either in the recruitment and stabilization of the subcomplex within RNA polymerase III, or in stimulating catalytic functions of other subunits during initiation. Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts induce type I interferon and NF- Kappa-B through the RIG-I pathway. {ECO:0000250|UniProtKB:O15318}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21898682}. Cytoplasm {ECO:0000269|PubMed:21898682}. Note=In zygotes and the 2-cell stage embryos, mainly in the cytoplasm. Starts to localize to the nucleus in the 8-16 cell stage embryo and early blastocysts. {ECO:0000269|PubMed:21898682}. SUBUNIT: Component of the RNA polymerase III (Pol III) complex consisting of 17 subunits. RPC3/POLR3C, RPC6/POLR3F and RPC7/POLR3G form a Pol III subcomplex. Directly interacts with POLR3C/RPC62. Also found a trimeric complex with POLR3C and POLR3GL. {ECO:0000250|UniProtKB:O15318}. TISSUE SPECIFICITY: Expressed at low levels in the liver. {ECO:0000269|PubMed:24107381}. +Q8VEE0 RPE_MOUSE Ribulose-phosphate 3-epimerase (EC 5.1.3.1) (Ribulose-5-phosphate-epimerase) 228 24,945 Active site (2); Binding site (3); Chain (1); Erroneous termination (1); Initiator methionine (1); Metal binding (4); Modified residue (1); Region (2); Sequence caution (1) FUNCTION: Catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate. {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +A2ALS5 RPGP1_MOUSE Rap1 GTPase-activating protein 1 (Rap1GAP) (Rap1GAP1) (ARPP-90) 663 73,433 Alternative sequence (3); Chain (1); Compositional bias (2); Domain (2); Erroneous initiation (2); Modified residue (9); Sequence conflict (1) FUNCTION: GTPase activator for the nuclear Ras-related regulatory protein RAP-1A (KREV-1), converting it to the putatively inactive GDP-bound state. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. SUBUNIT: Homodimer and heterodimer with RAP1B. {ECO:0000250}. TISSUE SPECIFICITY: Detected in brain cortex and striatum (at protein level). Detected in brain cortex and striatum. {ECO:0000269|PubMed:19218462}. +P19324 SERPH_MOUSE Serpin H1 (47 kDa heat shock protein) (Collagen-binding protein) (Colligin) (Serine protease inhibitor J6) 417 46,534 Chain (1); Glycosylation (3); Modified residue (5); Motif (1); Sequence conflict (7); Signal peptide (1); Site (1) FUNCTION: Binds specifically to collagen. Could be involved as a chaperone in the biosynthetic pathway of collagen. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. +Q80YQ8 RMD5A_MOUSE E3 ubiquitin-protein ligase RMND5A (EC 2.3.2.27) (Protein RMD5 homolog A) 391 43,993 Chain (1); Domain (2); Erroneous initiation (1); Modified residue (1); Sequence conflict (2); Zinc finger (1) FUNCTION: Core component of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1. MAEA and RMND5A are both required for catalytic activity of the CTLH E3 ubiquitin-protein ligase complex. Catalytic activity of the complex is required for normal cell proliferation. The CTLH E3 ubiquitin-protein ligase complex is not required for the degradation of enzymes involved in gluconeogenesis, such as FBP1. {ECO:0000250|UniProtKB:Q9H871}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9H871}. Cytoplasm {ECO:0000250|UniProtKB:Q9H871}. SUBUNIT: Identified in the CTLH complex that contains GID4, RANBP9 and/or RANBP10, MKLN1, MAEA, RMND5A (or alternatively its paralog RMND5B), GID8, ARMC8, WDR26 and YPEL5. Within this complex, MAEA, RMND5A (or alternatively its paralog RMND5B), GID8, WDR26, and RANBP9 and/or RANBP10 form the catalytic core, while GID4, MKLN1, ARMC8 and YPEL5 have ancillary roles. {ECO:0000250|UniProtKB:Q9H871}. +Q9D1I6 RM14_MOUSE 39S ribosomal protein L14, mitochondrial (L14mt) (MRP-L14) 145 15,874 Chain (1); Sequence conflict (2); Transit peptide (1) FUNCTION: May form part of 2 intersubunit bridges in the assembled ribosome. Upon binding to MALSU1, intersubunit bridge formation is blocked, preventing ribosome formation and repressing translation. {ECO:0000250|UniProtKB:Q6P1L8}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q6P1L8}. SUBUNIT: Component of the mitochondrial ribosome large subunit (39S) which comprises a 16S rRNA and about 50 distinct proteins. Interacts with MALSU1. {ECO:0000250|UniProtKB:Q6P1L8}. +Q8VC42 RMC1_MOUSE Regulator of MON1-CCZ1 complex (Colon cancer-associated protein Mic1) (Mic-1) 657 74,922 Chain (1); Domain (1); Erroneous initiation (1) FUNCTION: Componement of the CCZ1-MON1 RAB7A guanine exchange factor (GEF). Acts as a positive regulator of CCZ1-MON1A/B function necessary for endosomal/autophagic flux and efficient RAB7A localization. {ECO:0000250|UniProtKB:Q96DM3}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q96DM3}. Late endosome membrane {ECO:0000250|UniProtKB:Q96DM3}. SUBUNIT: Found in a complex with RMC1, CCZ1, MON1A and MON1B. {ECO:0000250|UniProtKB:Q96DM3}. TISSUE SPECIFICITY: Highly expressed in heart, brain, spleen, lung, liver, skeletal muscle, kidney and testis. {ECO:0000269|PubMed:9211850}. +Q9CQP0 RM33_MOUSE 39S ribosomal protein L33, mitochondrial (L33mt) (MRP-L33) 65 7,416 Chain (1); Sequence conflict (1); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:O75394}. SUBUNIT: Component of the mitochondrial ribosome large subunit (39S) which comprises a 16S rRNA and about 50 distinct proteins. {ECO:0000250|UniProtKB:O75394}. +Q9D0C1 RN115_MOUSE E3 ubiquitin-protein ligase RNF115 (EC 2.3.2.27) (RING finger protein 115) (RING-type E3 ubiquitin transferase RNF115) (Rabring 7) (Zinc finger protein 364) 305 33,859 Chain (1); Initiator methionine (1); Modified residue (1); Mutagenesis (3); Sequence conflict (2); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that mediates E2-dependent, 'Lys-48'- and/or 'Lys-63'-linked polyubiquitination of substrates and may play a role in diverse biological processes. Through their polyubiquitination, may play a role in the endosomal trafficking and degradation of membrane receptors including EGFR, FLT3, MET and CXCR4. {ECO:0000269|PubMed:17462600, ECO:0000303|PubMed:23418353}. PTM: RING-type zinc finger-dependent and E2-dependent autoubiquitination. {ECO:0000269|PubMed:17462600}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12972561}. Note=The GTP-bound form of RAB7A recruits RNF115 from the cytosol onto late endosomes/lysosomes. {ECO:0000269|PubMed:12972561}. SUBUNIT: Interacts with RAB7A. Interacts with EGFR and FLT3. {ECO:0000269|PubMed:12972561, ECO:0000269|PubMed:23418353}. +Q8R1Z9 RN121_MOUSE RING finger protein 121 327 37,987 Alternative sequence (2); Chain (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (1); Sequence conflict (7); Transmembrane (6); Zinc finger (1) TRANSMEM 50 70 Helical. {ECO:0000255}.; TRANSMEM 79 99 Helical. {ECO:0000255}.; TRANSMEM 100 120 Helical. {ECO:0000255}.; TRANSMEM 148 168 Helical. {ECO:0000255}.; TRANSMEM 172 192 Helical. {ECO:0000255}.; TRANSMEM 306 326 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9Z2Q5 RM40_MOUSE 39S ribosomal protein L40, mitochondrial (L40mt) (MRP-L40) (Nuclear localization signal-containing protein deleted in velocardiofacial syndrome homolog) 206 24,301 Chain (1); Natural variant (1); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9NQ50}. SUBUNIT: Component of the mitochondrial ribosome large subunit (39S) which comprises a 16S rRNA and about 50 distinct proteins. {ECO:0000250|UniProtKB:Q9NQ50}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9790763}. +Q5XPI3 RN123_MOUSE E3 ubiquitin-protein ligase RNF123 (EC 2.3.2.27) (Kip1 ubiquitination-promoting complex protein 1) (RING finger protein 123) (RING-type E3 ubiquitin transferase RNF123) 1314 148,652 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (1); Initiator methionine (1); Modified residue (3); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: Catalytic subunit of the KPC complex that acts as E3 ubiquitin-protein ligase. Required for poly-ubiquitination and proteasome-mediated degradation of CDKN1B during G1 phase of the cell cycle. {ECO:0000250|UniProtKB:Q5XPI4}. PTM: Ubiquitinated, leading to its degradation. Deubiquitinated by USP19, thereby stimulating CDKN1B ubiquitin-dependent degradation. {ECO:0000250|UniProtKB:D3ZXK7}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q5XPI4}. SUBUNIT: Component of the KPC complex composed of RNF123/KPC1 and UBAC1/KPC2. Interacts with UBAC1 and CDKN1B via its N-terminal domain. {ECO:0000250|UniProtKB:Q5XPI4}. +Q99N93 RM16_MOUSE 39S ribosomal protein L16, mitochondrial (L16mt) (MRP-L16) 251 28,804 Chain (1); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9NX20}. SUBUNIT: Component of the mitochondrial ribosome large subunit (39S) which comprises a 16S rRNA and about 50 distinct proteins. {ECO:0000250|UniProtKB:Q9NX20}. +Q3UJU9 RMD3_MOUSE Regulator of microtubule dynamics protein 3 (RMD-3) (mRMD-3) (Protein FAM82A2) (Protein FAM82C) 470 52,029 Chain (1); Coiled coil (1); Erroneous initiation (2); Modified residue (8); Sequence caution (1); Sequence conflict (5); Transmembrane (1) TRANSMEM 13 35 Helical. {ECO:0000255}. FUNCTION: Involved in cellular calcium homeostasis regulation (By similarity). May participate in differentiation and apoptosis of keratinocytes. Overexpression induces apoptosis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Mitochondrion outer membrane {ECO:0000250}. Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. Note=In interphase localizes in the cytoplasm, and during mitosis localizes to the spindle microtubules and spindle poles. {ECO:0000250}. SUBUNIT: Interacts with PTPN2. Interacts with microtubules. Interacts with VAPB. {ECO:0000250}. DOMAIN: The transmembrane region is required for mitochondrial localization. {ECO:0000250}. +Q9D1N9 RM21_MOUSE 39S ribosomal protein L21, mitochondrial (L21mt) (MRP-L21) 209 23,366 Alternative sequence (1); Chain (1); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q7Z2W9}. SUBUNIT: Component of the mitochondrial ribosome large subunit (39S) which comprises a 16S rRNA and about 50 distinct proteins. {ECO:0000250|UniProtKB:Q7Z2W9}. +Q9CZW6 RN146_MOUSE E3 ubiquitin-protein ligase RNF146 (EC 2.3.2.27) (Iduna) (RING finger protein 146) (RING-type E3 ubiquitin transferase RNF146) 359 38,934 Beta strand (10); Binding site (7); Chain (1); Cross-link (4); Domain (1); Helix (3); Modified residue (2); Mutagenesis (4); Region (1); Sequence conflict (2); Turn (6); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that specifically binds poly-ADP-ribosylated (PARsylated) proteins and mediates their ubiquitination and subsequent degradation. May regulate many important biological processes, such as cell survival and DNA damage response. Acts as an activator of the Wnt signaling pathway by mediating the ubiquitination of PARsylated AXIN1 and AXIN2, 2 key components of the beta-catenin destruction complex. Acts in cooperation with tankyrase proteins (TNKS and TNKS2), which mediate PARsylation of target proteins AXIN1, AXIN2, BLZF1, CASC3, TNKS and TNKS2. Recognizes and binds tankyrase-dependent PARsylated proteins via its WWE domain and mediates their ubiquitination (By similarity). May regulate TNKS and TNKS2 subcellular location, preventing aggregation at a centrosomal location. Neuroprotective protein. Protects the brain against N-methyl-D-aspartate (NMDA) receptor-mediated glutamate excitotoxicity and ischemia, by interfering with PAR-induced cell death, called parthanatos. Prevents nuclear translocation of AIFM1 in a PAR-binding dependent manner. Does not affect PARP1 activation (By similarity). Protects against cell death induced by DNA damaging agents, such as N-methyl-N-nitro-N-nitrosoguanidine (MNNG) and rescues cells from G1 arrest. Promotes cell survival after gamma-irradiation. Facilitates DNA repair. Neuroprotective protein. Protects the brain against N-methyl-D-aspartate (NMDA) receptor-mediated glutamate excitotoxicity and ischemia, by interfering with PAR-induced cell death, called parthanatos. Prevents nuclear translocation of AIFM1 in a PAR-binding dependent manner. Does not affect PARP1 activation. {ECO:0000250, ECO:0000269|PubMed:21602803, ECO:0000269|PubMed:21825151}. PTM: Ubiquitinated; autoubiquitinated. Autoubiquitination is enhanced upon PAR-binding (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:21602803}. Nucleus {ECO:0000250}. Note=Translocates to the nucleus after DNA damage, such as laser-induced DNA breaks, and concentrates at DNA breaks. This translocation requires PARP1 activation and PAR-binding (By similarity). {ECO:0000250}. SUBUNIT: Can form homooligomers. Interacts with PARsylated AXIN1, AXIN2, BLZF1, CASC3, HIST1H1C, IPO7, LIG3, NCL, PARP1, XRCC1, XRCC5 and XRCC6. Interacts with DDB1, DHX15, IQGAP1, LRPPRC, PARP2, PRKDC, RUVBL2, TNKS1 and TNKS2. Binding often leads to interactor ubiquitination, in the presence of the appropriate E1 and E2 enzymes, and proteasomal degradation. {ECO:0000250}. DOMAIN: The WWE domain mediates non-covalent PAR-binding. TISSUE SPECIFICITY: Expressed at relatively high levels in the brain. Also present in spleen, heart, kidney, testis and liver. In the brain, expressed in the cerebellum, hippocampus, striatum, cortex, frontal cortex and, at lowest levels, in olfactory bulb (at protein level). Predominantly expressed in neurons. {ECO:0000269|PubMed:15813938, ECO:0000269|PubMed:21602803}. +Q14B02 RN133_MOUSE E3 ubiquitin-protein ligase RNF133 (EC 2.3.2.27) (Goliath-related E3 ubiquitin-protein ligase 2) (RING finger protein 133) (RING-type E3 ubiquitin transferase RNF133) 382 43,102 Alternative sequence (1); Chain (1); Domain (1); Sequence conflict (1); Transmembrane (1); Zinc finger (1) TRANSMEM 190 210 Helical. {ECO:0000255}. Protein modification; protein ubiquitination. FUNCTION: Has E3 ubiquitin-protein ligase activity. {ECO:0000269|PubMed:18574499}. PTM: Auto-ubiquitinated. {ECO:0000269|PubMed:18574499}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305|PubMed:18574499}; Single-pass membrane protein {ECO:0000305|PubMed:18574499}. TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:18574499}. +Q3U2C5 RN149_MOUSE E3 ubiquitin-protein ligase RNF149 (EC 2.3.2.27) (Goliath-related E3 ubiquitin-protein ligase 4) (RING finger protein 149) (RING-type E3 ubiquitin transferase RNF149) 394 42,553 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (1); Glycosylation (3); Modified residue (3); Sequence conflict (2); Signal peptide (1); Transmembrane (1); Zinc finger (1) TRANSMEM 197 217 Helical. {ECO:0000255}. Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase. Ubiquitinates BRAF, inducing its proteasomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. DOMAIN: The RING-type zinc finger domain mediates binding to an E2 ubiquitin-conjugating enzyme. {ECO:0000250}. +Q5DTZ6 RN150_MOUSE RING finger protein 150 437 48,013 Alternative sequence (3); Chain (1); Domain (1); Erroneous initiation (1); Glycosylation (4); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1); Zinc finger (1) TRANSMEM 208 228 Helical. {ECO:0000255}. TOPO_DOM 35 207 Extracellular. {ECO:0000255}.; TOPO_DOM 229 437 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q9CQ29 RN151_MOUSE RING finger protein 151 239 27,175 Chain (1); Zinc finger (2) FUNCTION: May be involved in acrosome formation of spermatids. {ECO:0000269|PubMed:17577571}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17577571}. Nucleus {ECO:0000269|PubMed:17577571}. SUBUNIT: Interacts with DTNBP1. {ECO:0000269|PubMed:17577571}. TISSUE SPECIFICITY: Expressed in testis. Expressed in round spermatids of the stages VII-VIII semniniferous tubules. Expressed in elongating spermatids of stages VIII-IX seminiferous tubules (at protein level). {ECO:0000269|PubMed:17577571}. +Q99MB7 RN141_MOUSE RING finger protein 141 (Zinc finger protein 230) 230 25,529 Chain (1); Initiator methionine (1); Lipidation (1); Sequence conflict (3); Zinc finger (1) FUNCTION: May be involved in spermatogenesis. {ECO:0000269|PubMed:12804569}. SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q8WVD5}; Lipid-anchor {ECO:0000250|UniProtKB:Q8WVD5}. TISSUE SPECIFICITY: Isoform 1 is testis-specific. Isoform 2 is expressed in heart, brain, skeletal muscle, kidney, pancreas, lung, liver and testis. Isoform 3 is expressed in heart, liver, and kidney. {ECO:0000269|PubMed:12804569}. +Q62191 RO52_MOUSE E3 ubiquitin-protein ligase TRIM21 (EC 2.3.2.27) (52 kDa Ro protein) (52 kDa ribonucleoprotein autoantigen Ro/SS-A) (RING-type E3 ubiquitin transferase TRIM21) (Ro(SS-A)) (Sjoegren syndrome type A antigen) (SS-A) (Tripartite motif-containing protein 21) 470 54,175 Beta strand (15); Chain (1); Coiled coil (1); Domain (1); Helix (1); Turn (3); Zinc finger (2) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase whose activity is dependent on E2 enzymes, UBE2D1, UBE2D2, UBE2E1 and UBE2E2. Forms a ubiquitin ligase complex in cooperation with the E2 UBE2D2 that is used not only for the ubiquitination of USP4 and IKBKB but also for its self-ubiquitination. Component of cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes such as SCF(SKP2)-like complexes. A TRIM21-containing SCF(SKP2)-like complex is shown to mediate ubiquitination of CDKN1B ('Thr-187' phosphorylated-form), thereby promoting its degradation by the proteasome. Monoubiquitinates IKBKB that will negatively regulates Tax-induced NF-kappa-B signaling. Negatively regulates IFN-beta production post-pathogen recognition by polyubiquitin-mediated degradation of IRF3. Mediates the ubiquitin-mediated proteasomal degradation of IgG1 heavy chain, which is linked to the VCP-mediated ER-associated degradation (ERAD) pathway. Promotes IRF8 ubiquitination, which enhanced the ability of IRF8 to stimulate cytokine genes transcription in macrophages. Plays a role in the regulation of the cell cycle progression. Enhances the decapping activity of DCP2. Exists as a ribonucleoprotein particle present in all mammalian cells studied and composed of a single polypeptide and one of four small RNA molecules. At least two isoforms are present in nucleated and red blood cells, and tissue specific differences in RO/SSA proteins have been identified. The common feature of these proteins is their ability to bind HY RNAs.2. Involved in the regulation of innate immunity and the inflammatory response in response to IFNG/IFN-gamma. Organizes autophagic machinery by serving as a platform for the assembly of ULK1, Beclin 1/BECN1 and ATG8 family members and recognizes specific autophagy targets, thus coordinating target recognition with assembly of the autophagic apparatus and initiation of autophagy. Acts as an autophagy receptor for the degradation of IRF3, hence attenuating type I interferon (IFN)-dependent immune responses (By similarity). {ECO:0000250|UniProtKB:P19474, ECO:0000269|PubMed:17579016}. PTM: Autoubiquitinated; does not lead to its proteasomal degradation. Deubiquitinated by USP4; leading to its stabilization (By similarity). Autoubiquitinated. {ECO:0000250, ECO:0000269|PubMed:17579016}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17579016}. Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:O15553}. Nucleus {ECO:0000269|PubMed:17579016}. Cytoplasm, P-body {ECO:0000250}. Note=Enters the nucleus upon exposure to nitric oxide. Localizes to small dot- or rod-like structures in the cytoplasm, called processing bodies (P-bodies) that are located underneath the plasma membrane and also diffusely in the cytoplasm. They are located along the microtubules and are highly motile in cells. Colocalizes with DCP2 in P-bodies. {ECO:0000250|UniProtKB:P19474}. SUBUNIT: Homotrimer (By similarity). Component of a SCF(SKP2)-like complex containing CUL1, SKP1, TRIM21 and SKP2. Interacts with CALR, CUL1, FBXW11, HSPA5, IKBKB, IRF3, SKP1 and VCP. Interacts with SKP2; the interaction with SKP2 does not depend on an intact F-box domain. Interacts (via N-terminus and C-terminus) with DCP2 (via N-terminus and C-terminus) (By similarity). Interacts (via C-terminus) with IRF8 (via C-terminus). Interacts with ULK1, BECN1 and with ATG8 family members, including GABARAP, GABARAPL1, GABARAPL2 and MAP1LC3C/LC3C. Interacts with TRIM21 and SQSTM1/sequestosome 1. Interacts with IRF3 (By similarity). {ECO:0000250|UniProtKB:P19474, ECO:0000269|PubMed:17579016}. DOMAIN: The coiled-coil is necessary for the cytoplasmic localization. The B30.2/SPRY domain is necessary for the cytoplasmic localization, the interaction with IRF3 and for the IRF3-driven interferon beta promoter activity. The RING-type zinc finger is necessary for ubiquitination and for the IRF3-driven interferon beta promoter activity. Interacts with SKP2 and CUL1 in a RING finger-independent manner (By similarity). {ECO:0000250}. +P32958 ROM1_MOUSE Rod outer segment membrane protein 1 (ROSP1) 351 37,265 Chain (1); Topological domain (5); Transmembrane (4) TRANSMEM 20 44 Helical. {ECO:0000255}.; TRANSMEM 65 84 Helical. {ECO:0000255}.; TRANSMEM 103 125 Helical. {ECO:0000255}.; TRANSMEM 264 286 Helical. {ECO:0000255}. TOPO_DOM 1 19 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 45 64 Lumenal. {ECO:0000255}.; TOPO_DOM 85 102 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 126 263 Lumenal. {ECO:0000255}.; TOPO_DOM 287 351 Cytoplasmic. {ECO:0000255}. FUNCTION: May function as an adhesion molecule involved in stabilization and compaction of outer segment disks or in the maintenance of the curvature of the rim. It is essential for disk morphogenesis. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SUBUNIT: Homodimer; disulfide-linked. Probably forms a complex with a PRPH2 homodimer. Other proteins could associate with this complex in rods. TISSUE SPECIFICITY: Retina (photoreceptor). In rim region of ROS (rod outer segment) disks. +P97353 SEC1_MOUSE Galactoside 2-alpha-L-fucosyltransferase 3 (EC 2.4.1.69) (Alpha(1,2)FT 3) (Fucosyltransferase 10) (GDP-L-fucose:beta-D-galactoside 2-alpha-L-fucosyltransferase 3) (Secretory blood group protein 1) 368 41,464 Chain (1); Glycosylation (3); Natural variant (5); Topological domain (2); Transmembrane (1) TRANSMEM 21 41 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 20 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 42 368 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Membrane-bound form in trans cisternae of Golgi. {ECO:0000250}. +Q99020 ROAA_MOUSE Heterogeneous nuclear ribonucleoprotein A/B (hnRNP A/B) (CArG-binding factor-A) (CBF-A) 285 30,831 Chain (1); Compositional bias (2); Cross-link (2); Domain (2); Modified residue (11); Sequence conflict (2) FUNCTION: Transcriptional repressor. Binds to CArG box motifs, single-stranded and double-stranded DNA, and RNA. It may be that repression by CBF-A is a result of competitive binding of CBF, a putative positive factor, and CBF-A to the same or overlapping motifs around the CArG boxes. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Cytoplasm {ECO:0000250}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. {ECO:0000250}. SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with APOBEC1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. +Q8C0Q9 RPGF5_MOUSE Rap guanine nucleotide exchange factor 5 (Guanine nucleotide exchange factor for Rap1) (M-Ras-regulated Rap GEF) (MR-GEF) 814 93,725 Alternative sequence (4); Chain (1); Domain (3); Erroneous initiation (1); Sequence conflict (3) FUNCTION: Guanine nucleotide exchange factor (GEF) for RAP1A, RAP2A and MRAS/M-Ras-GTP. Its association with MRAS inhibits Rap1 activation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +P62488 RPB7_MOUSE DNA-directed RNA polymerase II subunit RPB7 (RNA polymerase II subunit B7) (DNA-directed RNA polymerase II subunit G) 172 19,294 Chain (1) FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB7 is part of a subcomplex with RPB4 that binds to a pocket formed by RPB1, RPB2 and RPB6 at the base of the clamp element. The RBP4-RPB7 subcomplex seems to lock the clamp via RPB7 in the closed conformation thus preventing double-stranded DNA to enter the active site cleft. The RPB4-RPB7 subcomplex binds single-stranded DNA and RNA. Binds RNA (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the RNA polymerase II (Pol II) complex consisting of 12 subunits. RPB4 and RPB7 form a subcomplex that protrudes from the 10-subunit Pol II core complex. +Q768S4 RPH3L_MOUSE Rab effector Noc2 (No C2 domains protein) (Rabphilin-3A-like protein) 302 33,259 Alternative sequence (2); Chain (1); Domain (1); Modified residue (1); Mutagenesis (1); Zinc finger (1) FUNCTION: Rab GTPase effector involved in the late steps of regulated exocytosis, both in endocrine and exocrine cells. Regulates the exocytosis of dense-core vesicles in neuroendocrine cells through interaction with RAB27A. Acts as a potential RAB3B effector protein in epithelial cells. {ECO:0000269|PubMed:14722103, ECO:0000269|PubMed:15159548}. SUBCELLULAR LOCATION: Cytoplasm. Cytoplasmic vesicle, secretory vesicle membrane. Note=Recruited to the exocytic secretory vesicles by RAB27A. SUBUNIT: Recruited to dense-core vesicles through specific interaction with RAB27A in endocrine cells. Interacts with RAB3A, RAB3B, RAB3C and RAB3D. Interacts with ZYX (By similarity). {ECO:0000250}. DOMAIN: The N-terminus of the RabBD domain is necessary and sufficient for interaction with RAB27A. {ECO:0000269|PubMed:14722103}. TISSUE SPECIFICITY: Highly expressed in pancreatic islets. High to moderate expression in adrenal gland, pituitary gland and ovary. {ECO:0000269|PubMed:16835753}. +Q9Z1W5 SERP1_MOUSE Stress-associated endoplasmic reticulum protein 1 (Ribosome-attached membrane protein 4) 66 7,374 Chain (1); Topological domain (2); Transmembrane (1) TRANSMEM 39 59 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 1 38 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 60 66 Extracellular. {ECO:0000255}. FUNCTION: Interacts with target proteins during their translocation into the lumen of the endoplasmic reticulum. Protects unfolded target proteins against degradation during ER stress. May facilitate glycosylation of target proteins after termination of ER stress. May modulate the use of N-glycosylation sites on target proteins (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Single-pass type IV membrane protein. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. SUBUNIT: Interacts with SEC61B, SEC61A1 and the SEC61 complex. Interacts with CANX (By similarity). {ECO:0000250}. +P58043 SESN2_MOUSE Sestrin-2 (EC 1.11.1.15) 480 54,377 Active site (1); Binding site (2); Chain (1); Modified residue (2); Mutagenesis (3); Region (3) FUNCTION: Functions as an intracellular leucine sensor that negatively regulates the TORC1 signaling pathway through the GATOR complex. In absence of leucine, binds the GATOR subcomplex GATOR2 and prevents TORC1 signaling. Binding of leucine to SESN2 disrupts its interaction with GATOR2 thereby activating the TORC1 signaling pathway (PubMed:18692468, PubMed:25259925). This stress-inducible metabolic regulator also plays a role in protection against oxidative and genotoxic stresses. May negatively regulate protein translation in response to endoplasmic reticulum stress, via TORC1 (PubMed:24947615). May positively regulate the transcription by NFE2L2 of genes involved in the response to oxidative stress by facilitating the SQSTM1-mediated autophagic degradation of KEAP1 (PubMed:23274085). May also mediate TP53 inhibition of TORC1 signaling upon genotoxic stress (PubMed:18692468). Has an alkylhydroperoxide reductase activity born by the N-terminal domain of the protein (By similarity). Was originally reported to contribute to oxidative stress resistance by reducing PRDX1 (By similarity). However, this could not be confirmed (By similarity). {ECO:0000250|UniProtKB:P58004, ECO:0000269|PubMed:18692468, ECO:0000269|PubMed:23274085, ECO:0000269|PubMed:24947615, ECO:0000269|PubMed:25259925}. PTM: Phosphorylated by ULK1 at multiple sites. {ECO:0000250|UniProtKB:P58004}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P58004}. SUBUNIT: Interacts with the GATOR2 complex which is composed of MIOS, SEC13, SEH1L, WDR24 and WDR59; the interaction is negatively regulated by leucine (By similarity). Interacts with RRAGA, RRAGB, RRAGC and RRAGD; may function as a guanine nucleotide dissociation inhibitor for RRAGs and regulate them (PubMed:25259925). May interact with the TORC2 complex (PubMed:25377878). Interacts with KEAP1, RBX1, SQSTM and ULK1; to regulate the degradation of KEAP1 (PubMed:25040165). May also associate with the complex composed of TSC1, TSC2 and the AMP-responsive protein kinase/AMPK to regulate TORC1 signaling (PubMed:18692468). May interact with PRDX1 (By similarity). {ECO:0000250|UniProtKB:P58004, ECO:0000269|PubMed:18692468, ECO:0000269|PubMed:25040165, ECO:0000269|PubMed:25259925, ECO:0000269|PubMed:25377878}. DOMAIN: Composed of an N-terminal domain that has an alkylhydroperoxide reductase activity and a C-terminal domain that mediates interaction with GATOR2 through which it regulates TORC1 signaling. {ECO:0000250|UniProtKB:P58004}. TISSUE SPECIFICITY: Detected in heart, liver and skeletal muscles (at protein level). {ECO:0000269|PubMed:25259925}. +P62918 RL8_MOUSE 60S ribosomal protein L8 257 28,025 Chain (1); Cross-link (4); Modified residue (1) FUNCTION: Component of the large ribosomal subunit. {ECO:0000250|UniProtKB:P62917}. PTM: Hydroxylated on His-216 by RIOX1. The modification is impaired by hypoxia. {ECO:0000250|UniProtKB:P62917}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P62917}. SUBUNIT: Component of the large ribosomal subunit (By similarity). Interacts with CRY1 (PubMed:19129230). {ECO:0000250|UniProtKB:P62917, ECO:0000269|PubMed:19129230}. +P14869 RLA0_MOUSE 60S acidic ribosomal protein P0 (60S ribosomal protein L10E) 317 34,216 Chain (1); Cross-link (2); Modified residue (4); Sequence conflict (3) FUNCTION: Ribosomal protein P0 is the functional equivalent of E.coli protein L10. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P05388}. Cytoplasm {ECO:0000250|UniProtKB:P05388}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. {ECO:0000250|UniProtKB:P05388}. SUBUNIT: P0 forms a pentameric complex by interaction with dimers of P1 and P2. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with APEX1. Interacts with FMR1. {ECO:0000250|UniProtKB:P05388}. +Q99L28 RLP24_MOUSE Probable ribosome biogenesis protein RLP24 (Ribosomal L24 domain-containing protein 1) (Ribosomal protein L24-like) 163 19,611 Chain (1) FUNCTION: Involved in the biogenesis of the 60S ribosomal subunit. Ensures the docking of GTPBP4/NOG1 to pre-60S particles (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. SUBUNIT: Associated with nucleolar and cytoplasmic pre-60S particles. At the end of biogenesis it dissociates from cytoplasmic pre-60S particles and is likely to be exchanged for its ribosomal homolog, RPL24 (By similarity). {ECO:0000250}. +Q5NCM1 S17A4_MOUSE Probable small intestine urate exporter (Solute carrier family 17 member 4) 492 53,668 Chain (1); Erroneous gene model prediction (1); Glycosylation (6); Transmembrane (11) TRANSMEM 112 132 Helical. {ECO:0000255}.; TRANSMEM 134 154 Helical. {ECO:0000255}.; TRANSMEM 156 176 Helical. {ECO:0000255}.; TRANSMEM 198 218 Helical. {ECO:0000255}.; TRANSMEM 225 245 Helical. {ECO:0000255}.; TRANSMEM 287 307 Helical. {ECO:0000255}.; TRANSMEM 327 347 Helical. {ECO:0000255}.; TRANSMEM 363 383 Helical. {ECO:0000255}.; TRANSMEM 393 413 Helical. {ECO:0000255}.; TRANSMEM 426 446 Helical. {ECO:0000255}.; TRANSMEM 456 476 Helical. {ECO:0000255}. FUNCTION: Acts as a membrane potential-dependent organic anion transporter, the transport requires a low concentration of chloride ions. May be involved in urate extrusion from the intestinal duct. May recognize hydrophilic anionic drugs such as aspirin, salicylate, and ibuprofen as substrates. Able to actively transport inorganic phosphate into cells via Na(+) cotransport (in vitro) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Multi-pass membrane protein. Note=Apical in the intestinal brush border. {ECO:0000250}. +Q9D773 RM02_MOUSE 39S ribosomal protein L2, mitochondrial (L2mt) (MRP-L2) 306 33,341 Chain (1); Compositional bias (1); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q5T653}. SUBUNIT: Component of the mitochondrial ribosome large subunit (39S) which comprises a 16S rRNA and about 50 distinct proteins. {ECO:0000250|UniProtKB:Q5T653}. +Q80VA5 S3TC2_MOUSE SH3 domain and tetratricopeptide repeat-containing protein 2 1289 145,144 Alternative sequence (6); Chain (1); Domain (2); Repeat (8) +Q9CZ83 RM55_MOUSE 39S ribosomal protein L55, mitochondrial (L55mt) (MRP-L55) 127 15,122 Alternative sequence (1); Chain (1); Modified residue (1); Sequence conflict (1); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P0C2B8}. SUBUNIT: Component of the mitochondrial ribosome large subunit (39S) which comprises a 16S rRNA and about 50 distinct proteins. {ECO:0000250|UniProtKB:P0C2B8}. +Q91YQ7 RMD5B_MOUSE E3 ubiquitin-protein transferase RMND5B (EC 2.3.2.27) (Protein RMD5 homolog B) 393 44,421 Chain (1); Domain (2); Modified residue (1); Zinc finger (1) FUNCTION: Core component of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1. MAEA and RMND5A are both required for catalytic activity of the CTLH E3 ubiquitin-protein ligase complex. Catalytic activity of the complex is required for normal cell proliferation. The CTLH E3 ubiquitin-protein ligase complex is not required for the degradation of enzymes involved in gluconeogenesis, such as FBP1. {ECO:0000250|UniProtKB:Q96G75}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q96G75}. SUBUNIT: Identified in the CTLH complex that contains GID4, RANBP9 and/or RANBP10, MKLN1, MAEA, RMND5A (or alternatively its paralog RMND5B), GID8, ARMC8, WDR26 and YPEL5. Within this complex, MAEA, RMND5A (or alternatively its paralog RMND5B), GID8, WDR26, and RANBP9 and/or RANBP10 form the catalytic core, while GID4, MKLN1, ARMC8 and YPEL5 have ancillary roles. {ECO:0000250|UniProtKB:Q96G75}. +A2AVZ9 S43A3_MOUSE Solute carrier family 43 member 3 (Embryonic epithelia gene 1 protein) 502 56,034 Alternative sequence (1); Chain (1); Compositional bias (1); Frameshift (1); Glycosylation (2); Sequence conflict (2); Transmembrane (12) TRANSMEM 17 37 Helical. {ECO:0000255}.; TRANSMEM 72 92 Helical. {ECO:0000255}.; TRANSMEM 97 117 Helical. {ECO:0000255}.; TRANSMEM 122 142 Helical. {ECO:0000255}.; TRANSMEM 156 176 Helical. {ECO:0000255}.; TRANSMEM 189 209 Helical. {ECO:0000255}.; TRANSMEM 294 314 Helical. {ECO:0000255}.; TRANSMEM 335 355 Helical. {ECO:0000255}.; TRANSMEM 381 401 Helical. {ECO:0000255}.; TRANSMEM 419 439 Helical. {ECO:0000255}.; TRANSMEM 442 462 Helical. {ECO:0000255}.; TRANSMEM 468 488 Helical. {ECO:0000255}. FUNCTION: Putative transporter. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: High expression in the heart, followed by the lung, liver, spleen and kidney. {ECO:0000269|PubMed:11704567}. +Q6PDX6 RN220_MOUSE E3 ubiquitin-protein ligase Rnf220 (EC 2.3.2.27) (RING finger protein 220) (RING-type E3 ubiquitin transferase Rnf220) 566 62,693 Alternative sequence (6); Chain (1); Coiled coil (1); Cross-link (1); Modified residue (1); Region (1); Sequence conflict (1); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that promotes the ubiquitination and proteasomal degradation of SIN3B (PubMed:20170641). Independently of its E3 ligase activity, acts as a CTNNB1 stabilizer through USP7-mediated deubiquitination of CTNNB1 and promotes Wnt signaling (By similarity). {ECO:0000250|UniProtKB:Q5VTB9, ECO:0000269|PubMed:20170641}. PTM: Auto-ubiquitinated; leads to proteasomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20170641}. SUBUNIT: Interacts with SIN3B (PubMed:20170641). Interacts with CTNNB1 (via Armadillo repeats 2-8) (By similarity). Interacts with USP7 (via MATH domain) (By similarity). {ECO:0000250|UniProtKB:Q5VTB9, ECO:0000269|PubMed:20170641}. +Q9JJH1 RNAS4_MOUSE Ribonuclease 4 (RNase 4) (EC 3.1.27.-) 148 17,025 Active site (2); Binding site (3); Chain (1); Disulfide bond (4); Modified residue (1); Region (1); Signal peptide (1) FUNCTION: This RNase has marked specificity towards the 3' side of uridine nucleotides. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. +Q3UIW5 RNF10_MOUSE RING finger protein 10 (Sid 2705) 804 88,345 Alternative sequence (3); Chain (1); Compositional bias (2); Erroneous initiation (1); Modified residue (3); Sequence conflict (2); Zinc finger (1) FUNCTION: Transcriptional factor involved in the regulation of MAG (Myelin-associated glycoprotein) expression and myelin formation in Schwann cells. {ECO:0000250|UniProtKB:Q5XI59}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8N5U6}. Nucleus {ECO:0000250|UniProtKB:Q5XI59}. SUBUNIT: Interacts with MEOX2. {ECO:0000250|UniProtKB:Q8N5U6}. +Q80Y81 RNZ2_MOUSE Zinc phosphodiesterase ELAC protein 2 (EC 3.1.26.11) (ElaC homolog protein 2) (Ribonuclease Z 2) (RNase Z 2) (tRNA 3 endonuclease 2) (tRNase Z 2) 831 92,719 Alternative sequence (1); Chain (1); Modified residue (8); Sequence conflict (5); Transit peptide (1) FUNCTION: Zinc phosphodiesterase, which displays mitochondrial tRNA 3'-processing endonuclease activity. Involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Nucleus {ECO:0000250}. Note=Mainly mitochondrial. {ECO:0000250}. SUBUNIT: Homodimer. Interacts with PTCD1. {ECO:0000250}. +Q6QD59 SEC20_MOUSE Vesicle transport protein SEC20 228 26,175 Chain (1); Coiled coil (1); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 200 220 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 1 199 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 221 228 Lumenal. {ECO:0000255}. FUNCTION: As part of a SNARE complex may be involved in endoplasmic reticulum membranes fusion and be required for the maintenance of endoplasmic reticulum organization. Plays also a role in apoptosis. It is for instance required for endoplasmic reticulum stress-induced apoptosis. As a substrate of RNF185 interacting with SQSTM1, might also be involved in mitochondrial autophagy. {ECO:0000250|UniProtKB:Q12981}. PTM: Polyubiquitinated. 'Lys-63'-linked polyubiquitination by RNF185 increases the interaction with the autophagy receptor SQSTM1. Undergoes 'Lys-29'- and 'Lys-63'-linked polyubiquitination by RNF186 that may regulate BNIP1 localization to the mitochondrion. {ECO:0000250|UniProtKB:Q12981}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q12981}; Single-pass type IV membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q12981}; Single-pass type IV membrane protein {ECO:0000255}. Note=Localization to the mitochondrion is regulated by RNF186. {ECO:0000250|UniProtKB:Q12981}. SUBUNIT: Component of a SNARE complex consisting of STX18, USE1L, BNIP1/SEC20L and SEC22B. Interacts directly with STX18, RINT1/TIP20L and NAPA. Interacts with ZW10 through RINT1. Interacts with BCL2. Interacts with RNF186. Interacts with RNF185. Interacts with SQSTM1; increased by 'Lys-63'-linked polyubiquitination of BNIP1. {ECO:0000250|UniProtKB:Q12981}. +Q8VC34 RPAP2_MOUSE Putative RNA polymerase II subunit B1 CTD phosphatase Rpap2 (EC 3.1.3.16) (RNA polymerase II-associated protein 2) 614 68,530 Alternative sequence (6); Chain (1); Coiled coil (1); Initiator methionine (1); Metal binding (4); Modified residue (4); Sequence conflict (4); Zinc finger (1) FUNCTION: Protein phosphatase that displays CTD phosphatase activity and regulates transcription of snRNA genes. Recognizes and binds phosphorylated 'Ser-7' of the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit POLR2A, and mediates dephosphorylation of 'Ser-5' of the CTD, thereby promoting transcription of snRNA genes. {ECO:0000250|UniProtKB:Q8IXW5}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Shuttles between the cytoplasm and the nucleus in a CRM1-dependent manner. {ECO:0000250}. SUBUNIT: Associates with the RNA polymerase II complex. Interacts with transcribing RNA polymerase II phosphorylated on 'Ser-7' on CTD (By similarity). {ECO:0000250}. +P56716 RP1_MOUSE Oxygen-regulated protein 1 (Retinitis pigmentosa RP1 protein homolog) 2095 234,388 Chain (1); Compositional bias (1); Domain (2) FUNCTION: Microtubule-associated protein regulating the stability and length of the microtubule-based axoneme of photoreceptors. Required for the differentiation of photoreceptor cells, it plays a role in the organization of the outer segment of rod and cone photoreceptors ensuring the correct orientation and higher-order stacking of outer segment disks along the photoreceptor axoneme. {ECO:0000269|PubMed:14507858, ECO:0000269|PubMed:15269252}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme. Cell projection, cilium, photoreceptor outer segment. Note=Specifically localized in the connecting cilia of rod and cone photoreceptors. SUBUNIT: Interacts (via the doublecortin domains) with microtubules. Interacts with RP1L1. Interacts with MAK. {ECO:0000269|PubMed:15269252, ECO:0000269|PubMed:19657028, ECO:0000269|PubMed:21148103}. DOMAIN: The doublecortin domains, which mediate interaction with microtubules, are required for regulation of microtubule polymerization and function in photoreceptor differentiation. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the cell bodies and inner segments of photoreceptors. Not found in liver, spleen, kidney, brain, thymus, muscle, heart, lung and testis. +Q76KJ5 RPA34_MOUSE DNA-directed RNA polymerase I subunit RPA34 (A34.5) (Anti-sense to ERCC-1 protein) (ASE-1) (CD3-epsilon-associated protein) (CD3E-associated protein) (RNA polymerase I-associated factor PAF49) 399 43,082 Chain (1); Compositional bias (1); Modified residue (6); Sequence conflict (4) FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I which synthesizes ribosomal RNA precursors. Involved in UBTF-activated transcription, presumably at a step following PIC formation. {ECO:0000269|PubMed:15226435}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:15226435}. Note=Accumulates in the nucleolus of exponentially growing cells. SUBUNIT: Component of the RNA polymerase I (Pol I) complex consisting of at least 13 subunits. Interacts with TAF1A thereby associates with the SL1 complex. Interacts with UBTF (By similarity). Interacts with POLR1E/PRAF1 through its N-terminal region. {ECO:0000250, ECO:0000269|PubMed:15226435}. +O08740 RPB11_MOUSE DNA-directed RNA polymerase II subunit RPB11 (RNA polymerase II subunit B11) (DNA-directed RNA polymerase II subunit J) (RNA polymerase II 13.3 kDa subunit) (RPB14) 117 13,251 Chain (1); Modified residue (1) FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB11 is part of the core element with the central large cleft (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the RNA polymerase II (Pol II) complex consisting of 12 subunits. Interacts with AATF (By similarity). {ECO:0000250}. +Q9JJ80 RPF2_MOUSE Ribosome production factor 2 homolog (Brix domain-containing protein 1) (Ribosome biogenesis protein RPF2 homolog) 306 35,364 Chain (1); Domain (1); Sequence conflict (2) FUNCTION: Involved in ribosomal large subunit assembly. May regulate the localization of the 5S RNP/5S ribonucleoprotein particle to the nucleolus. {ECO:0000250|UniProtKB:Q9H7B2}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9H7B2}. Note=Associated with the nucleolus in an RNA-dependent manner. {ECO:0000250|UniProtKB:Q9H7B2}. +Q9EQZ6 RPGF4_MOUSE Rap guanine nucleotide exchange factor 4 (Exchange factor directly activated by cAMP 2) (Exchange protein directly activated by cAMP 2) (EPAC 2) (cAMP-dependent Rap1 guanine-nucleotide exchange factor) (cAMP-regulated guanine nucleotide exchange factor II) (cAMP-GEFII) 1011 115,491 Alternative sequence (2); Beta strand (35); Chain (1); Domain (3); Helix (48); Mutagenesis (4); Nucleotide binding (2); Sequence conflict (2); Turn (7) FUNCTION: Guanine nucleotide exchange factor (GEF) for RAP1A, RAP1B and RAP2A small GTPases that is activated by binding cAMP. Seems not to activate RAB3A. Involved in cAMP-dependent, PKA-independent exocytosis through interaction with RIMS2. {ECO:0000269|PubMed:11056535}. SUBCELLULAR LOCATION: Cytoplasm. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. SUBUNIT: Interacts with RAP1B, RIMS1 and RIMS2. Probably part of a complex with RIMS2 and GTP-activated RAB3A. {ECO:0000269|PubMed:11056535, ECO:0000269|PubMed:18660803}. DOMAIN: The N-terminal nucleotide phosphate binding region cAMP 1 has a much lower affinity for cAMP as compared to cAMP 2. {ECO:0000250}.; DOMAIN: The DEP domain is involved in membrane localization independent from regulation by cAMP. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in cerebellum, pituitary, adrenal gland and liver. {ECO:0000269|PubMed:11056535}. +Q62193 RFA2_MOUSE Replication protein A 32 kDa subunit (RP-A p32) (Replication factor A protein 2) (RF-A protein 2) (Replication protein A 34 kDa subunit) (RP-A p34) 270 29,718 Chain (1); Cross-link (2); DNA binding (1); Modified residue (7); Region (1) FUNCTION: As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates, that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage. In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation. Through recruitment of ATRIP activates the ATR kinase a master regulator of the DNA damage response. It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin in response to DNA damage. Also recruits to sites of DNA damage proteins like XPA and XPG that are involved in nucleotide excision repair and is required for this mechanism of DNA repair. Plays also a role in base excision repair (BER) probably through interaction with UNG. Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. May also play a role in telomere maintenance. {ECO:0000250|UniProtKB:P15927}. PTM: Differentially phosphorylated throughout the cell cycle, becoming phosphorylated at the G1-S transition and dephosphorylated in late mitosis. Mainly phosphorylated at Ser-23 and Ser-29, by cyclin A-CDK2 and cyclin B-CDK1, respectively during DNA replication and mitosis. Dephosphorylation may require the serine/threonine-protein phosphatase 4. Phosphorylation at Ser-23 and Ser-29 is a prerequisite for further phosphorylation. Becomes hyperphosphorylated on additional residues including Ser-4, Ser-8, Thr-21 and Ser-33 in response to DNA damage. Hyperphosphorylation is mediated by ATM, ATR and PRKDC. Primarily recruited to DNA repair nuclear foci as a hypophosphorylated form it undergoes subsequent hyperphosphorylation, catalyzed by ATR. Hyperphosphorylation is required for RAD51 recruitment to chromatin and efficient DNA repair. Phosphorylation at Thr-21 depends upon RFWD3 presence. {ECO:0000250|UniProtKB:P15927}.; PTM: DNA damage-induced 'Lys-63'-linked polyubiquitination by PRPF19 mediates ATRIP recruitment to the RPA complex at sites of DNA damage and activation of ATR. Ubiquitinated by RFWD3 at stalled replication forks in response to DNA damage: ubiquitination by RFWD3 does not lead to degradation by the proteasome and promotes removal of the RPA complex from stalled replication forks, promoting homologous recombination. {ECO:0000250|UniProtKB:P15927}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P15927}. Nucleus, PML body {ECO:0000250|UniProtKB:P15927}. Note=Redistributes to discrete nuclear foci upon DNA damage in an ATR-dependent manner. {ECO:0000250|UniProtKB:P15927, ECO:0000269|PubMed:17141802}. SUBUNIT: Component of the replication protein A complex (RPA/RP-A), a heterotrimeric complex composed of RPA1, RPA2 and RPA3. Interacts with PRPF19; the PRP19-CDC5L complex is recruited to the sites of DNA repair where it ubiquitinates the replication protein A complex (RPA) (By similarity). Interacts with SERTAD3. Interacts with TIPIN (PubMed:17141802). Interacts with TIMELESS (PubMed:17141802). Interacts with PPP4R2; the interaction is direct, DNA damage-dependent and mediates the recruitment of the PP4 catalytic subunit PPP4C (By similarity). Interacts (hyperphosphorylated) with RAD51 (By similarity). Interacts with SMARCAL1; the interaction is direct and mediates the recruitment to the RPA complex of SMARCAL1 (By similarity). Interacts with RAD52 and XPA; those interactions are direct and associate RAD52 and XPA to the RPA complex (By similarity). Interacts with FBH1 (By similarity). Interacts with ETAA1; the interaction is direct and promotes ETAA1 recruitment at stalled replication forks (By similarity). {ECO:0000250|UniProtKB:P15927}. +Q3UYI5 RGL3_MOUSE Ral guanine nucleotide dissociation stimulator-like 3 (RalGDS-like 3) (RalGDS-related effector protein of M-Ras) (Ras pathway modulator) (RPM) 709 77,945 Alternative sequence (4); Chain (1); Compositional bias (2); Domain (3); Frameshift (1); Modified residue (7); Region (1); Sequence conflict (5) FUNCTION: Guanine nucleotide exchange factor (GEF) for Ral-A. Potential effector of GTPase HRas and Ras-related protein M-Ras. Negatively regulates Elk-1-dependent gene induction downstream of HRas and MEKK1. {ECO:0000269|PubMed:10869344, ECO:0000269|PubMed:11313946}. SUBUNIT: Interacts with GTP-bound forms of RIT1, HRAS and MRAS. {ECO:0000269|PubMed:10869344, ECO:0000269|PubMed:11313946}. DOMAIN: The Ras-associating domain plays a central role in the activation of Ral-A GDP/GTP exchange activity. {ECO:0000269|PubMed:10869344}. TISSUE SPECIFICITY: Widely expressed. Expressed at high levels in the liver and kidney. {ECO:0000269|PubMed:10869344, ECO:0000269|PubMed:11313946}. +P70425 RIT2_MOUSE GTP-binding protein Rit2 (Ras-like protein expressed in neurons) (Ras-like without CAAX protein 2) 217 24,802 Chain (1); Erroneous initiation (1); Mutagenesis (3); Nucleotide binding (3); Sequence conflict (4) FUNCTION: Binds and exchanges GTP and GDP. Binds and modulates the activation of POU4F1 as gene expression regulator. {ECO:0000269|PubMed:12934100}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23805044}. Cell membrane {ECO:0000269|PubMed:23805044}. Note=Colocalizes with PLXNB3 at the plasma membrane. {ECO:0000250|UniProtKB:Q99578}. SUBUNIT: Interacts with PLXNB3 (By similarity). Interacts with AFDN, the C-terminal domain of RALGDS and RLF, but not with RIN1 and PIK3CA. RLF binds exclusively to the active GTP-bound form. Binds calmodulin. Interacts with POU4F1 (via N-terminus); the interaction controls POU4F1 transactivation activity on some neuronal target genes (PubMed:12934100). {ECO:0000250|UniProtKB:Q99578, ECO:0000269|PubMed:10545207, ECO:0000269|PubMed:12934100}. TISSUE SPECIFICITY: Expressed in ganglion cell layer (GCL), inner plexiform layer (IPL) and inner nuclear layer (INL) of the retina. Expressed in retinal ganglion cells (RGCs). Expressed in horizontal, bipolar and amacrine cells, but not Mueller glia, of the INL (at protein level). Neuron-specific (PubMed:8824319). Expressed in ganglion cell layer (GCL) and inner plexiform layer (IPL) (PubMed:23805044). {ECO:0000269|PubMed:23805044, ECO:0000269|PubMed:8824319}. +P61255 RL26_MOUSE 60S ribosomal protein L26 (Silica-induced gene 20 protein) (SIG-20) 145 17,258 Chain (1); Cross-link (1); Modified residue (1) FUNCTION: Component of the large ribosomal subunit. {ECO:0000305|PubMed:26100019}. SUBUNIT: Component of the large ribosomal subunit (Probable). Interacts with DHX33 (PubMed:26100019). {ECO:0000269|PubMed:26100019, ECO:0000305|PubMed:26100019}. +P47915 RL29_MOUSE 60S ribosomal protein L29 160 17,587 Chain (1); Modified residue (5); Region (1); Repeat (2) FUNCTION: Component of the large ribosomal subunit. {ECO:0000250|UniProtKB:P47914}. SUBUNIT: Component of the large ribosomal subunit. {ECO:0000250|UniProtKB:P47914}. +Q9D8E6 RL4_MOUSE 60S ribosomal protein L4 419 47,154 Chain (1); Compositional bias (1); Cross-link (3); Initiator methionine (1); Modified residue (13); Sequence conflict (1) PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}. SUBUNIT: May bind IPO9 with low affinity. Interacts with RBM3 (By similarity). {ECO:0000250}. +P62862 RS30_MOUSE 40S ribosomal protein S30 59 6,648 Chain (1); Erroneous initiation (8); Modified residue (1) +P97351 RS3A_MOUSE 40S ribosomal protein S3a (Protein TU-11) 264 29,885 Chain (1); Cross-link (2); Modified residue (6) FUNCTION: May play a role during erythropoiesis through regulation of transcription factor DDIT3. {ECO:0000255|HAMAP-Rule:MF_03122, ECO:0000269|PubMed:10713066}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03122, ECO:0000269|PubMed:10713066}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03122, ECO:0000269|PubMed:10713066}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. {ECO:0000255|HAMAP-Rule:MF_03122}. SUBUNIT: Component of the small ribosomal subunit. Mature ribosomes consist of a small (40S) and a large (60S) subunit. The 40S subunit contains about 33 different proteins and 1 molecule of RNA (18S). The 60S subunit contains about 49 different proteins and 3 molecules of RNA (28S, 5.8S and 5S). Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Binds with high affinity to IPO4. Interacts with DDIT3. {ECO:0000255|HAMAP-Rule:MF_03122, ECO:0000269|PubMed:10713066, ECO:0000269|PubMed:11823430}. +P62908 RS3_MOUSE 40S ribosomal protein S3 (EC 4.2.99.18) 243 26,674 Chain (1); Cross-link (5); Domain (1); Initiator methionine (1); Modified residue (16) FUNCTION: Involved in translation as a component of the 40S small ribosomal subunit (By similarity). Has endonuclease activity and plays a role in repair of damaged DNA (PubMed:7775413). Cleaves phosphodiester bonds of DNAs containing altered bases with broad specificity and cleaves supercoiled DNA more efficiently than relaxed DNA (By similarity). Displays high binding affinity for 7,8-dihydro-8-oxoguanine (8-oxoG), a common DNA lesion caused by reactive oxygen species (ROS) (By similarity). Has also been shown to bind with similar affinity to intact and damaged DNA (By similarity). Stimulates the N-glycosylase activity of the base excision protein OGG1 (By similarity). Enhances the uracil excision activity of UNG1 (By similarity). Also stimulates the cleavage of the phosphodiester backbone by APEX1 (By similarity). When located in the mitochondrion, reduces cellular ROS levels and mitochondrial DNA damage (By similarity). Has also been shown to negatively regulate DNA repair in cells exposed to hydrogen peroxide (By similarity). Plays a role in regulating transcription as part of the NF-kappa-B p65-p50 complex where it binds to the RELA/p65 subunit, enhances binding of the complex to DNA and promotes transcription of target genes (By similarity). Represses its own translation by binding to its cognate mRNA (By similarity). Binds to and protects TP53/p53 from MDM2-mediated ubiquitination (By similarity). Involved in spindle formation and chromosome movement during mitosis by regulating microtubule polymerization (By similarity). Involved in induction of apoptosis through its role in activation of CASP8 (PubMed:14988002). Induces neuronal apoptosis by interacting with the E2F1 transcription factor and acting synergistically with it to up-regulate pro-apoptotic proteins BCL2L11/BIM and HRK/Dp5 (By similarity). Interacts with TRADD following exposure to UV radiation and induces apoptosis by caspase-dependent JNK activation (By similarity). {ECO:0000250|UniProtKB:P23396, ECO:0000269|PubMed:14988002, ECO:0000269|PubMed:7775413}. PTM: Methylation by PRMT1 is required for import into the nucleolus and for ribosome assembly. {ECO:0000250|UniProtKB:P23396}.; PTM: Sumoylation by SUMO1 enhances protein stability through increased resistance to proteolysis. Sumoylation occurs at one or more of the three consensus sites, Lys-18, Lys-214 and Lys-230. {ECO:0000250|UniProtKB:P23396}.; PTM: Phosphorylation at Thr-221 by CDK1 occurs mainly in G2/M phase. Phosphorylation by PRKCD occurs on a non-ribosomal-associated form which results in translocation of RPS3 to the nucleus and enhances its endonuclease activity. Phosphorylated on Ser-209 by IKKB in response to activation of the NF-kappa-B p65-p50 complex which enhances the association of RPS3 with importin-alpha and mediates the nuclear translocation of RPS3. Phosphorylation by MAPK is required for translocation to the nucleus following exposure of cells to DNA damaging agents such as hydrogen peroxide. Phosphorylation by PKB/AKT mediates RPS3 nuclear translocation, enhances RPS3 endonuclease activity and suppresses RPS3-induced neuronal apoptosis. {ECO:0000250|UniProtKB:P23396}.; PTM: Ubiquitinated. This is prevented by interaction with HSP90 which stabilizes the protein. Monoubiquitinated at Lys-214 by ZNF598 when a ribosome has stalled during translation of poly(A) sequences, leading to preclude synthesis of a long poly-lysine tail and initiate the ribosome quality control (RQC) pathway to degrade the potentially detrimental aberrant nascent polypeptide. {ECO:0000250|UniProtKB:P23396}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14988002}. Nucleus {ECO:0000269|PubMed:14988002}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P23396}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:P23396}; Peripheral membrane protein {ECO:0000250|UniProtKB:P23396}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P23396}. Note=In normal cells, located mainly in the cytoplasm with small amounts in the nucleus but translocates to the nucleus in cells undergoing apoptosis. Nuclear translocation is also induced by DNA damaging agents such as hydrogen peroxide (By similarity). Accumulates in the mitochondrion in response to increased ROS levels (By similarity). Localizes to the spindle during mitosis (By similarity). Localized in cytoplasmic mRNP granules containing untranslated mRNAs (By similarity). {ECO:0000250|UniProtKB:P23396, ECO:0000269|PubMed:14988002}. SUBUNIT: Component of the 40S small ribosomal subunit. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with HNRPD. Interacts with PRMT1; the interaction methylates RPS3. Interacts with SUMO1; the interaction sumoylates RPS3. Interacts with UBC9. Interacts with CDK1; the interaction phosphorylates RPS3. Interacts with PRKCD; the interaction phosphorylates RPS3. Interacts with PKB/AKT; the interaction phosphorylates RPS3. Interacts with E2F1; the interaction occurs in the absence of nerve growth factor and increases transcription of pro-apoptotic proteins BCL2L11/BIM and HRK/Dp5. Interacts with the base excision repair proteins APEX1 and OGG1; interaction with OGG1 increases OGG1 N-glycosylase activity. Interacts with UNG; the interaction increases the uracil excision activity of UNG1. Interacts with HSP90; the interaction prevents the ubiquitination and proteasome-dependent degradation of RPS3 and is suppressed by increased ROS levels. Interacts with TOM70; the interaction promotes translocation of RPS3 to the mitochondrion. Interacts (via N-terminus) with RELA (via N-terminus); the interaction enhances the DNA-binding activity of the NF-kappa-B p65-p50 complex. Interacts with NFKBIA; the interaction is direct and may bridge the interaction between RPS3 and RELA. Interacts with IKKB; the interaction phosphorylates RPS3 and enhances its translocation to the nucleus. Interacts (via KH domain) with MDM2 and TP53. Interacts with TRADD. Interacts with CRY1. {ECO:0000250|UniProtKB:P23396, ECO:0000269|PubMed:19129230}. +P86048 RL10L_MOUSE 60S ribosomal protein L10-like 214 24,558 Chain (1) +P53026 RL10A_MOUSE 60S ribosomal protein L10a (CSA-19) (Neural precursor cell expressed developmentally down-regulated protein 6) (NEDD-6) 217 24,916 Chain (1); Cross-link (3); Frameshift (1); Initiator methionine (1); Modified residue (5) FUNCTION: Component of the large ribosomal subunit. {ECO:0000250|UniProtKB:P62906}. SUBUNIT: Component of the large ribosomal subunit. {ECO:0000250|UniProtKB:P62906}. +Q9D6S7 RRFM_MOUSE Ribosome-recycling factor, mitochondrial (RRF) (Ribosome-releasing factor, mitochondrial) 262 29,051 Beta strand (6); Chain (1); Helix (2); Transit peptide (1); Turn (1) FUNCTION: Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. +Q8BVY0 RL1D1_MOUSE Ribosomal L1 domain-containing protein 1 452 50,421 Chain (1); Coiled coil (1); Compositional bias (1); Cross-link (2); Frameshift (1); Modified residue (9) FUNCTION: Regulates cellular senescence through inhibition of PTEN translation. Acts as a pro-apoptotic regulator in response to DNA damage. {ECO:0000250|UniProtKB:O76021}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:O76021}. SUBUNIT: Interacts with ING1. {ECO:0000250|UniProtKB:O76021}. +Q8BP67 RL24_MOUSE 60S ribosomal protein L24 157 17,779 Chain (1); Cross-link (4); Erroneous initiation (1); Modified residue (7); Sequence conflict (1) +Q9QXU7 PROK2_MOUSE Prokineticin-2 (PK2) (Protein Bv8 homolog) 128 14,185 Alternative sequence (2); Chain (1); Disulfide bond (5); Signal peptide (1) FUNCTION: May function as an output molecule from the suprachiasmatic nucleus (SCN) that transmits behavioral circadian rhythm. May also function locally within the SCN to synchronize output. Potently contracts gastrointestinal (GI) smooth muscle (By similarity). {ECO:0000250, ECO:0000269|PubMed:12024206}. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Expressed in the SCN and among a few other discrete brain areas, including the islands of Calleja, media l preoptic area of the hypothalamus and the shell of the nucleus accumbens. Highly expressed in testis. In the SCN, expression subjected to high amplitude of circadian oscillation. +Q8CCF0 PRP31_MOUSE U4/U6 small nuclear ribonucleoprotein Prp31 (Pre-mRNA-processing factor 31) (U4/U6 snRNP 61 kDa protein) (Protein 61K) 499 55,430 Alternative sequence (3); Chain (1); Coiled coil (2); Compositional bias (2); Cross-link (2); Domain (1); Erroneous translation (1); Frameshift (2); Modified residue (8); Motif (1); Sequence caution (1); Sequence conflict (10); Site (5) FUNCTION: Involved in pre-mRNA splicing as component of the spliceosome. Required for the assembly of the U4/U5/U6 tri-snRNP complex, one of the building blocks of the spliceosome. {ECO:0000250|UniProtKB:Q8WWY3}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8WWY3}. Nucleus speckle {ECO:0000250|UniProtKB:Q8WWY3}. Nucleus, Cajal body {ECO:0000250|UniProtKB:Q8WWY3}. Note=Predominantly found in speckles and in Cajal bodies. {ECO:0000250|UniProtKB:Q8WWY3}. SUBUNIT: Identified in the spliceosome B complex. Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39. Interacts with a complex formed by SNU13 and U4 snRNA, but not with SNU13 or U4 snRNA alone. The complex formed by SNU13 and PRPF31 binds also U4atac snRNA, a characteristic component of specific, less abundant spliceosomal complexes. Interacts with PRPF6/U5 snRNP-associated 102 kDa protein. Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, KAT8/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Interacts (via its NLS) with CTNNBL1. {ECO:0000250|UniProtKB:Q8WWY3}. DOMAIN: Interacts with the snRNP via the Nop domain. {ECO:0000250|UniProtKB:Q8WWY3}.; DOMAIN: The coiled coil domain is formed by two non-contiguous helices. {ECO:0000250|UniProtKB:Q8WWY3}. +P11680 PROP_MOUSE Properdin (Complement factor P) 464 50,327 Chain (1); Disulfide bond (20); Domain (7); Glycosylation (1); Sequence conflict (3); Signal peptide (1) FUNCTION: A positive regulator of the alternate pathway of complement. It binds to and stabilizes the C3- and C5-convertase enzyme complexes. SUBCELLULAR LOCATION: Secreted. SUBUNIT: In plasma, properdin exists as dimers, trimers or tetramers in the relative proportions of 26:54:20. {ECO:0000250}. DOMAIN: TSP type-1 domains 0 and 6 bind to each other and mediate multimerization. {ECO:0000250}. +A6H6T1 PRS40_MOUSE Serine protease 40 (EC 3.4.21.-) (Testicular serine protease 2) 365 40,146 Active site (3); Chain (1); Disulfide bond (4); Domain (1); Glycosylation (1); Sequence conflict (10); Signal peptide (1) FUNCTION: May play an important role in the sperm/egg interaction; released during the acrosome reaction. {ECO:0000269|PubMed:9588171}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:9588171}. Secreted {ECO:0000269|PubMed:9588171}. TISSUE SPECIFICITY: Expressed in testis. More specifically, abundantly expressed in the haploid round spermatid. {ECO:0000269|PubMed:9588171}. +P63013 PRRX1_MOUSE Paired mesoderm homeobox protein 1 (Homeobox protein K-2) (Homeobox protein mHox) (Paired-related homeobox protein 1) (PRX-1) 245 27,269 Alternative sequence (1); Chain (1); DNA binding (1); Modified residue (3); Motif (1) FUNCTION: Acts as a transcriptional regulator of muscle creatine kinase (MCK) and so has a role in the establishment of diverse mesodermal muscle types. The protein binds to an A/T-rich element in the muscle creatine enhancer. SUBCELLULAR LOCATION: Nucleus. TISSUE SPECIFICITY: Expressed exclusively in mesodermally derived cell types. During embryogenesis, highest levels of expression are found in the mesenchyme and precartilage elements of the face and hind limbs. In the adult, expression is restricted to skeletal muscle, heart and uterus. +Q3UPH1 PRRC1_MOUSE Protein PRRC1 (Proline-rich and coiled-coil-containing protein 1) 443 46,298 Chain (1); Compositional bias (1); Erroneous initiation (1); Modified residue (1) SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250}. +P14685 PSMD3_MOUSE 26S proteasome non-ATPase regulatory subunit 3 (26S proteasome regulatory subunit RPN3) (26S proteasome regulatory subunit S3) (Proteasome subunit p58) (Transplantation antigen P91A) (Tum-P91A antigen) 530 60,718 Chain (1); Compositional bias (1); Cross-link (2); Domain (1); Modified residue (2); Sequence conflict (2) FUNCTION: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. {ECO:0000250|UniProtKB:O43242}. SUBUNIT: Component of the 19S proteasome regulatory particle complex. The 26S proteasome consists of a 20S core particle (CP) and two 19S regulatory subunits (RP). The regulatory particle is made of a lid composed of 9 subunits including PSMD3, a base containing 6 ATPases and few additional components. Interacts with UBQLN1 (via ubiquitin-like domain). {ECO:0000250|UniProtKB:O43242, ECO:0000269|PubMed:16857966}. +Q8BJY1 PSMD5_MOUSE 26S proteasome non-ATPase regulatory subunit 5 (26S protease subunit S5 basic) (26S proteasome subunit S5B) 504 55,972 Chain (1); Initiator methionine (1); Modified residue (1); Sequence conflict (3) FUNCTION: Acts as a chaperone during the assembly of the 26S proteasome, specifically of the base subcomplex of the PA700/19S regulatory complex (RC). In the initial step of the base subcomplex assembly is part of an intermediate PSMD5:PSMC2:PSMC1:PSMD2 module which probably assembles with a PSMD10:PSMC4:PSMC5:PAAF1 module followed by dissociation of PSMD5 (By similarity). {ECO:0000250}. SUBUNIT: Interacts with PSMC1, PSMC2, PSMD1 and PSMD6. Part of transient complex containing PSMD5, PSMC2, PSMC1 and PSMD2 formed during the assembly of the 26S proteasome. {ECO:0000269|PubMed:16857966}. DOMAIN: Rich in dileucine repeats, which have been implicated in trafficking of a variety of transmembrane proteins. +Q9JM51 PTGES_MOUSE Prostaglandin E synthase (mPGES-1) (EC 5.3.99.3) (Microsomal prostaglandin E synthase 1) 153 17,286 Binding site (4); Chain (1); Region (3); Topological domain (4); Transmembrane (4) TRANSMEM 14 42 Helical. {ECO:0000250}.; TRANSMEM 62 91 Helical. {ECO:0000250}.; TRANSMEM 97 120 Helical. {ECO:0000250}.; TRANSMEM 125 153 Helical. {ECO:0000250}. TOPO_DOM 1 13 Lumenal. {ECO:0000250}.; TOPO_DOM 43 61 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 92 96 Lumenal. {ECO:0000250}.; TOPO_DOM 121 124 Cytoplasmic. {ECO:0000250}. FUNCTION: Catalyzes the oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Homotrimer. {ECO:0000250}. +O35074 PTGIS_MOUSE Prostacyclin synthase (EC 5.3.99.4) (Prostaglandin I2 synthase) 501 57,047 Binding site (4); Chain (1); Metal binding (1); Region (1); Transmembrane (1) TRANSMEM 1 21 Helical. {ECO:0000255}. FUNCTION: Catalyzes the isomerization of prostaglandin H2 to prostacyclin (= prostaglandin I2). {ECO:0000250|UniProtKB:Q16647}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q29626}; Single-pass membrane protein {ECO:0000255}. +Q64434 PTK6_MOUSE Protein-tyrosine kinase 6 (EC 2.7.10.2) (SRC-related intestinal kinase) 451 51,972 Active site (1); Binding site (1); Chain (1); Domain (3); Modified residue (7); Mutagenesis (1); Nucleotide binding (1); Region (1) FUNCTION: Non-receptor tyrosine-protein kinase implicated in the regulation of a variety of signaling pathways that control the differentiation and maintenance of normal epithelia, as well as tumor growth. Function seems to be context dependent and differ depending on cell type, as well as its intracellular localization. A number of potential nuclear and cytoplasmic substrates have been identified. These include the RNA-binding proteins: KHDRBS1/SAM68, KHDRBS2/SLM1, KHDRBS3/SLM2 and SFPQ/PSF; transcription factors: STAT3 and STAT5A/B and a variety of signaling molecules: ARHGAP35/p190RhoGAP, PXN/paxillin, BTK/ATK, STAP2/BKS. Associates also with a variety of proteins that are likely upstream of PTK6 in various signaling pathways, or for which PTK6 may play an adapter-like role. These proteins include ADAM15, EGFR, ERBB2, ERBB3 and IRS4. In normal or non-tumorigenic tissues, PTK6 promotes cellular differentiation and apoptosis. In tumors PTK6 contributes to cancer progression by sensitizing cells to mitogenic signals and enhancing proliferation, anchorage-independent survival and migration/invasion. Association with EGFR, ERBB2, ERBB3 may contribute to mammary tumor development and growth through enhancement of EGF-induced signaling via BTK/AKT and PI3 kinase. Contributes to migration and proliferation by contributing to EGF-mediated phosphorylation of ARHGAP35/p190RhoGAP, which promotes association with RASA1/p120RasGAP, inactivating RhoA while activating RAS. EGF stimulation resulted in phosphorylation of PNX/Paxillin by PTK6 and activation of RAC1 via CRK/CrKII, thereby promoting migration and invasion. PTK6 activates STAT3 and STAT5B to promote proliferation. Nuclear PTK6 may be important for regulating growth in normal epithelia, while cytoplasmic PTK6 might activate oncogenic signaling pathways. {ECO:0000269|PubMed:10913193, ECO:0000269|PubMed:15471878, ECO:0000269|PubMed:19501589}. PTM: Autophosphorylated. Autophosphorylation of Tyr-342 leads to an increase of kinase activity. Tyr-447 binds to the SH2 domain when phosphorylated and negatively regulates kinase activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Membrane. Cell projection, ruffle {ECO:0000250}. Note=Also found to be membrane-associated. Colocalizes with KHDRBS1, within the nucleus. SUBUNIT: Interacts with KHDRBS1. Interacts with phosphorylated IRS4 (By similarity). Interacts with GAP-A.p65. Interacts with ADAM15 (By similarity). Interacts (via SH3 and SH2 domains) with phosphorylated IRS4 (By similarity). Interacts (via SH3 domain) with SFPQ (By similarity). Interacts with EGFR and ERBB2 (By similarity). Interacts with STAP2 (By similarity). Interacts with PNX (By similarity). Interacts with SFPQ (By similarity). Interacts with PTK/ATK (By similarity). Interacts with CTNNB1 (By similarity). {ECO:0000250}. DOMAIN: The SH3 domain plays a major role in substrate interactions. The SH2 domain of PTK6 plays a role in protein-protein interactions, but is likely more important for the regulation of catalytic activity (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed only in epithelial tissues, including the skin and lining of the alimentary canal. Restricted to the cell layers immediately above the proliferative cell zone in these epithelia. {ECO:0000269|PubMed:15471878}. +Q8R2Y8 PTH2_MOUSE Peptidyl-tRNA hydrolase 2, mitochondrial (PTH 2) (EC 3.1.1.29) 181 19,527 Chain (1); Cross-link (6); Erroneous initiation (1); Sequence conflict (1); Transit peptide (1) FUNCTION: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis. {ECO:0000250}. PTM: Ubiquitinated by PRKN during mitophagy, leading to its degradation and enhancement of mitophagy. Deubiquitinated by USP30. {ECO:0000250|UniProtKB:Q9Y3E5}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. +P26350 PTMA_MOUSE Prothymosin alpha [Cleaved into: Prothymosin alpha, N-terminally processed; Thymosin alpha] 111 12,254 Chain (2); Compositional bias (1); Cross-link (1); Initiator methionine (1); Modified residue (13); Peptide (1); Sequence conflict (1); Turn (1) FUNCTION: Prothymosin alpha may mediate immune function by conferring resistance to certain opportunistic infections. PTM: Covalently linked to a small RNA of about 20 nucleotides. SUBCELLULAR LOCATION: Nucleus. +Q9CWJ9 PUR9_MOUSE Bifunctional purine biosynthesis protein PURH [Includes: Phosphoribosylaminoimidazolecarboxamide formyltransferase (EC 2.1.2.3) (5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase) (AICAR transformylase); IMP cyclohydrolase (EC 3.5.4.10) (ATIC) (IMP synthase) (Inosinicase)] 592 64,217 Active site (2); Binding site (6); Chain (1); Domain (1); Frameshift (1); Modified residue (2); Nucleotide binding (5); Region (1); Sequence conflict (4); Site (1) Purine metabolism; IMP biosynthesis via de novo pathway; 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): step 1/1. Purine metabolism; IMP biosynthesis via de novo pathway; IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide: step 1/1. FUNCTION: Bifunctional enzyme that catalyzes 2 steps in purine biosynthesis. {ECO:0000250}.; FUNCTION: Promotes insulin receptor/INSR autophosphorylation and is involved in INSR internalization. {ECO:0000250|UniProtKB:P31939}. SUBUNIT: Homodimer (By similarity). Associates with internalized INSR complexes on Golgi/endosomal membranes. Interacts with INSR; ATIC together with PRKAA2/AMPK2 and HACD3/PTPLAD1 is proposed to be part of a signaling network regulating INSR autophosphorylation and endocytosis (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O35567}. DOMAIN: The IMP cyclohydrolase activity resides in the N-terminal region. +Q8BHA9 PXYP1_MOUSE 2-phosphoxylose phosphatase 1 (EC 3.1.3.-) (Acid phosphatase-like protein 2) 480 54,937 Active site (2); Chain (1); Glycosylation (3); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 7 27 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 28 480 Lumenal. {ECO:0000255}. FUNCTION: Responsible for the 2-O-dephosphorylation of xylose in the glycosaminoglycan-protein linkage region of proteoglycans thereby regulating the amount of mature glycosaminoglycan (GAG) chains. Sulfated glycosaminoglycans (GAGs), including heparan sulfate and chondroitin sulfate, are synthesized on the so-called common GAG-protein linkage region (GlcUAbeta1-3Galbeta1-3Galbeta1-4Xylbeta1-O-Ser) of core proteins, which is formed by the stepwise addition of monosaccharide residues by the respective specific glycosyltransferases. Xylose 2-O-dephosphorylation during completion of linkage region formation is a prerequisite for the initiation and efficient elongation of the repeating disaccharide region of GAG chains. {ECO:0000250|UniProtKB:Q8TE99}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q8TE99}; Single-pass type II membrane protein {ECO:0000255}. Note=Colocalizes to Golgi apparatus in a B3GAT3-dependent manner. {ECO:0000250|UniProtKB:Q8TE99}. SUBUNIT: Interacts with B3GAT3; the interaction increases the 2-phosphoxylose phosphatase activity of PXYLP1 during completion of linkage region formation in a B3GAT3-mediated manner. {ECO:0000250|UniProtKB:Q8TE99}. +P82343 RENBP_MOUSE N-acylglucosamine 2-epimerase (AGE) (EC 5.1.3.8) (GlcNAc 2-epimerase) (N-acetyl-D-glucosamine 2-epimerase) (Renin-binding protein) (RnBP) 430 49,771 Alternative sequence (1); Chain (1); Erroneous initiation (3); Modified residue (1); Region (1); Sequence conflict (1) Amino-sugar metabolism; N-acetylneuraminate degradation. FUNCTION: Catalyzes the interconversion of N-acetylglucosamine to N-acetylmannosamine. Binds to renin forming a protein complex called high molecular weight (HMW) renin and inhibits renin activity. Involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway. {ECO:0000269|PubMed:22692205}. SUBUNIT: Homodimer. {ECO:0000250}. +Q04863 RELB_MOUSE Transcription factor RelB 558 60,305 Beta strand (28); Chain (1); Domain (1); Helix (5); Modified residue (3); Motif (2); Mutagenesis (1); Region (1); Sequence conflict (2); Turn (4) FUNCTION: NF-kappa-B is a pleiotropic transcription factor which is present in almost all cell types and is involved in many biological processed such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. NF-kappa-B heterodimeric RelB-p50 and RelB-p52 complexes are transcriptional activators. RELB neither associates with DNA nor with RELA/p65 or REL. Stimulates promoter activity in the presence of NFKB2/p49 (By similarity). As a member of the NUPR1/RELB/IER3 survival pathway, may allow the development of pancreatic intraepithelial neoplasias. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer in a CRY1/CRY2 independent manner. Increased repression of the heterodimer is seen in the presence of NFKB2/p52. Is required for both T and B lymphocyte maturation and function (By similarity). {ECO:0000250|UniProtKB:Q01201, ECO:0000269|PubMed:22565310, ECO:0000269|PubMed:22894897}. PTM: Phosphorylation at 'Thr-103' and 'Ser-573' is followed by proteasomal degradation. {ECO:0000269|PubMed:11781828}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Note=Colocalizes with NEK6 in the centrosome. {ECO:0000250}. SUBUNIT: Component of the NF-kappa-B RelB-p50 complex. Component of the NF-kappa-B RelB-p52 complex (By similarity). Self-associates; the interaction seems to be transient and may prevent degradation allowing for heterodimer formation p50 or p52. Interacts with NFKB1/p50, NFKB2/p52 and NFKB2/p100. Interacts with NFKBID. Interacts with ARNTL/BMAL1 and the interaction is enhanced in the presence of CLOCK. {ECO:0000250, ECO:0000269|PubMed:11931770, ECO:0000269|PubMed:12874295, ECO:0000269|PubMed:17869269, ECO:0000269|PubMed:22894897}. DOMAIN: Both N- and C-terminal domains are required for transcriptional activation. TISSUE SPECIFICITY: Expressed in intestine, thymus and spleen. Undetectable in liver, bome marrow, kidney and testis. +O35929 REM1_MOUSE GTP-binding protein REM 1 (Rad and Gem-like GTP-binding protein 1) 297 32,909 Chain (1); Compositional bias (1); Modified residue (1); Nucleotide binding (2); Region (1) FUNCTION: Promotes endothelial cell sprouting and actin cytoskeletal reorganization (By similarity). May be involved in angiogenesis. May function in Ca(2+) signaling. {ECO:0000250}. SUBUNIT: In vitro, interacts with calmodulin in a calcium-dependent manner (By similarity). Interacts 14-3-3 family members including YWHAE, YWHAH, YWHAQ, YWHAZ in a phosphorylation-dependent manner. {ECO:0000250, ECO:0000269|PubMed:10441394}. TISSUE SPECIFICITY: High expression in cardiac muscle. Moderate expression in lung, skeletal muscle and kidney. Low levels in spleen and brain. +Q8VCG9 RFXAP_MOUSE Regulatory factor X-associated protein (RFX-associated protein) 231 24,787 Chain (1); Cross-link (1); Motif (1) FUNCTION: Part of the RFX complex that binds to the X-box of MHC II promoters. {ECO:0000250}. PTM: Phosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: RFX consists of at least 3 different subunits; RFXAP, RFX5 and RFX-B/RFXANK; with each subunit representing a separate complementation group. RFX forms cooperative DNA binding complexes with X2BP and CBF/NF-Y. RFX associates with CIITA to form an active transcriptional complex (By similarity). {ECO:0000250}. +Q9D620 RFIP1_MOUSE Rab11 family-interacting protein 1 (Rab11-FIP1) (Rab-coupling protein) 645 70,684 Chain (1); Compositional bias (1); Domain (2); Modified residue (14); Region (1); Sequence conflict (4) FUNCTION: A Rab11 effector protein involved in the endosomal recycling process. Also involved in controlling membrane trafficking along the phagocytic pathway and phagocytosis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Recycling endosome {ECO:0000250}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250}. Note=Membrane-bound. RAB11A rather than RAB4A mediates RAB11FIP1 localization in the endocytic recycling compartment (ERC). Colocalizes with RAB11A at phagosomes (By similarity). {ECO:0000250}. SUBUNIT: Homooligomer. Interacts with RAB4A, RAB11A, RAB11B and RAB25 (By similarity). {ECO:0000250}. +Q6ZWV3 RL10_MOUSE 60S ribosomal protein L10 (Protein QM homolog) (Ribosomal protein L10) 214 24,604 Chain (1); Cross-link (2); Modified residue (1); Sequence conflict (1) FUNCTION: Component of the large ribosomal subunit. Plays a role in the formation of actively translating ribosomes. May play a role in the embryonic brain development. {ECO:0000250|UniProtKB:P27635}. PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}. SUBUNIT: Component of the large ribosomal subunit. Mature ribosomes consist of a small (40S) and a large (60S) subunit. The 40S subunit contains about 33 different proteins and 1 molecule of RNA (18S). The 60S subunit contains about 49 different proteins and 3 molecules of RNA (28S, 5.8S and 5S). {ECO:0000250|UniProtKB:P27635}. +P35980 RL18_MOUSE 60S ribosomal protein L18 188 21,645 Chain (1); Cross-link (2); Modified residue (2); Sequence conflict (8) FUNCTION: Component of the large ribosomal subunit. {ECO:0000250|UniProtKB:Q07020}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q07020}. Cytoplasm {ECO:0000250|UniProtKB:Q07020}. Rough endoplasmic reticulum {ECO:0000250|UniProtKB:Q95342}. Note=Detected on cytosolic polysomes (By similarity). Detected in ribosomes that are associated with the rough endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:Q07020, ECO:0000250|UniProtKB:Q95342}. SUBUNIT: Component of the large ribosomal subunit. {ECO:0000250|UniProtKB:Q07020}. +Q9CR57 RL14_MOUSE 60S ribosomal protein L14 217 23,564 Chain (1); Cross-link (1); Modified residue (5); Region (2); Repeat (6); Sequence conflict (1) FUNCTION: Component of the large ribosomal subunit. {ECO:0000250|UniProtKB:P50914}. SUBUNIT: Component of the large ribosomal subunit. {ECO:0000250|UniProtKB:P50914}. +P61358 RL27_MOUSE 60S ribosomal protein L27 136 15,798 Chain (1); Domain (1); Modified residue (2) FUNCTION: Component of the large ribosomal subunit (By similarity). Required for proper rRNA processing and maturation of 28S and 5.8S rRNAs (By similarity). {ECO:0000250|UniProtKB:A1XQU5, ECO:0000250|UniProtKB:P61353}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P61353}. Cytoplasm {ECO:0000250|UniProtKB:P61353}. Rough endoplasmic reticulum {ECO:0000250|UniProtKB:A1XQU5}. Note=Detected on cytosolic polysomes (By similarity). Detected in ribosomes that are associated with the rough endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:A1XQU5, ECO:0000250|UniProtKB:P61353}. SUBUNIT: Component of the large ribosomal subunit (By similarity). Interacts with RRP1B (By similarity). Interacts with DHX33 (PubMed:26100019). {ECO:0000250|UniProtKB:A1XQU5, ECO:0000250|UniProtKB:P61353, ECO:0000269|PubMed:26100019}. +P19253 RL13A_MOUSE 60S ribosomal protein L13a (Transplantation antigen P198) (Tum-P198 antigen) 203 23,464 Chain (1); Initiator methionine (1); Modified residue (5); Mutagenesis (1); Natural variant (1) FUNCTION: Associated with ribosomes but is not required for canonical ribosome function and has extra-ribosomal functions (By similarity). Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma activation and subsequent phosphorylation dissociates from the ribosome and assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation. In the GAIT complex interacts with m7G cap-bound eIF4G at or near the eIF3-binding site and blocks the recruitment of the 43S ribosomal complex. {ECO:0000250, ECO:0000269|PubMed:23071094}. PTM: Phosphorylation at Ser-77 upon interferon-gamma treatment in macrophages involves a DAPK1-DAPK3 kinase cascade and is causing release from the ribosome, association with the GAIT complex and subsequent involvement in transcript-selective translation inhibition. {ECO:0000269|PubMed:23071094}.; PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}. SUBUNIT: Component of the 60S ribosome. Component of the GAIT complex. Interacts with EIF4G1 (By similarity). {ECO:0000250}. +P84099 RL19_MOUSE 60S ribosomal protein L19 196 23,466 Chain (1); Cross-link (1); Modified residue (6); Sequence conflict (1) PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}. +P47963 RL13_MOUSE 60S ribosomal protein L13 (A52) 211 24,305 Chain (1); Cross-link (5); Modified residue (5); Sequence conflict (3) +P62245 RS15A_MOUSE 40S ribosomal protein S15a 130 14,840 Chain (1); Erroneous initiation (1); Modified residue (1); Sequence conflict (1) +P41105 RL28_MOUSE 60S ribosomal protein L28 137 15,733 Chain (1); Cross-link (2); Initiator methionine (1); Modified residue (2) FUNCTION: Component of the large ribosomal subunit. {ECO:0000250|UniProtKB:P46779}. SUBUNIT: Component of the large ribosomal subunit. {ECO:0000250|UniProtKB:P46779}. +Q9CXE0 PRDM5_MOUSE PR domain zinc finger protein 5 (EC 2.1.1.-) (PR domain-containing protein 5) 599 69,550 Chain (1); Compositional bias (1); Domain (1); Sequence conflict (1); Zinc finger (15) FUNCTION: Sequence-specific DNA-binding transcription factor. Represses transcription at least in part by recruitment of the histone methyltransferase EHMT2/G9A and histone deacetylases such as HDAC1. Regulates hematopoiesis-associated protein-coding and microRNA (miRNA) genes (By similarity). May regulate the expression of proteins involved in extracellular matrix development and maintenance, connective tissue components and molecules regulating cell migration and adhesion. May caused G2/M arrest and apoptosis in cancer cells (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with EHMT2/G9A, GFI1 and HDAC1. {ECO:0000250}. +Q9CRB5 PR7C1_MOUSE Prolactin-7C1 (Placental prolactin-like protein O) (PLP-O) (PRL-like protein O) 251 29,258 Chain (1); Disulfide bond (2); Glycosylation (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000250}. TISSUE SPECIFICITY: Expressed exclusively in the placenta. Expressed in spongiotrophoblast cells and trophoblast giant cells of the junctional zone and in labyrinthine trophoblast. {ECO:0000269|PubMed:12488360}. +P04769 PR7D1_MOUSE Prolactin-7D1 (Proliferin-related protein) (PRP) 244 27,952 Chain (1); Disulfide bond (2); Signal peptide (1) SUBCELLULAR LOCATION: Secreted. +Q9DAY2 PR8A6_MOUSE Prolactin-8A6 (Placental prolactin-like protein C1) (PLP-C1) (PRL-like protein C1) (Prolactin-like protein C-alpha) (PLP C-alpha) (Prolactin-like protein C) 240 27,274 Alternative sequence (2); Chain (1); Disulfide bond (3); Glycosylation (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000250}. TISSUE SPECIFICITY: Expressed specifically in the spongiotrophoblast and trophoblast giant cells from the junctional zone of the chorioallantoic placenta. {ECO:0000269|PubMed:9832456}. +Q8BZ97 PRDM8_MOUSE PR domain zinc finger protein 8 (EC 2.1.1.-) (PR domain-containing protein 8) 687 70,886 Chain (1); Compositional bias (4); Domain (1); Zinc finger (2) FUNCTION: Probable histone methyltransferase, preferentially acting on 'Lys-9' of histone H3 (PubMed:19646955). Histone methyltransferase activity has not been confirmed in other species. Involved in the control of steroidogenesis through transcriptional repression of steroidogenesis marker genes such as CYP17A1 and LHCGR (PubMed:19646955). Forms with BHLHE22 a transcriptional repressor complex controlling genes involved in neural development and neuronal differentiation (PubMed:22284184). In the retina, it is required for rod bipolar and type 2 OFF-cone bipolar cell survival (PubMed:26023183). {ECO:0000269|PubMed:19646955, ECO:0000269|PubMed:22284184, ECO:0000269|PubMed:26023183}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19646955}. SUBUNIT: Interacts with BHLHE22 (PubMed:22284184). Interacts with EPM2A and NHLRC1. This interaction sequesters EPM2A and NHLRC1 to the nucleus (By similarity). {ECO:0000250|UniProtKB:Q9NQV8, ECO:0000269|PubMed:22284184}. TISSUE SPECIFICITY: Expressed in brain, heart, liver, testes, retina (PubMed:19646955, PubMed:22284184). Highest expression is observed in the retina and hippocampus; moderately expressed in the cortex and cerebellum. In the retina, it is expressed in bipolar and amacrine cells (PubMed:26023183). {ECO:0000269|PubMed:19646955, ECO:0000269|PubMed:22284184, ECO:0000269|PubMed:26023183}. +Q80SY5 PR38B_MOUSE Pre-mRNA-splicing factor 38B 542 63,753 Chain (1); Coiled coil (1); Compositional bias (1); Initiator methionine (1); Modified residue (14); Sequence conflict (1) FUNCTION: May be required for pre-mRNA splicing. {ECO:0000305}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +A2AGX3 PRD11_MOUSE PR domain-containing protein 11 (EC 2.1.1.-) 565 63,383 Chain (1); Cross-link (5); Domain (1); Erroneous gene model prediction (2); Modified residue (1) FUNCTION: May be involved in transcription regulation. {ECO:0000250|UniProtKB:Q9NQV5}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NQV5}. Cytoplasm {ECO:0000250|UniProtKB:Q9NQV5}. TISSUE SPECIFICITY: Widely expressed, with the highest levels in spleen, lung, mesenteric lymph node and kidney. Among splenocytes, predominantly expressed by B-cells (at protein level). {ECO:0000269|PubMed:25499759}. +Q9R1C7 PR40A_MOUSE Pre-mRNA-processing factor 40 homolog A (Formin-binding protein 11) (FBP-11) (Formin-binding protein 3) 953 108,481 Alternative sequence (1); Chain (1); Cross-link (4); Domain (8); Modified residue (15); Sequence conflict (2) FUNCTION: Binds to WASL/N-WASP and suppresses its translocation from the nucleus to the cytoplasm, thereby inhibiting its cytoplasmic function. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration. May play a role in cytokinesis. May be involved in pre-mRNA splicing. {ECO:0000269|PubMed:14697212}. SUBCELLULAR LOCATION: Nucleus speckle. Nucleus matrix. Note=Colocalizes with AKAP8L in the nuclear matrix. SUBUNIT: Interacts with the N-terminus of HTT and with the phosphorylated C-terminal domain of POLR2A (By similarity). Interacts with AKAP8L, SF1, SRPK1, CARD8, ATBF1 and MECP2. Interacts through the WW domains with formin proline-rich regions and with WASL/N-WASP. {ECO:0000250, ECO:0000269|PubMed:14697212, ECO:0000269|PubMed:16391387, ECO:0000269|PubMed:8605874, ECO:0000269|PubMed:9171351}. DOMAIN: The WW domains are essential for localization to nuclear speckles. +E9PZZ1 PRD13_MOUSE PR domain zinc finger protein 13 (EC 2.1.1.-) (PR domain-containing protein 13) 754 78,705 Alternative sequence (1); Chain (1); Compositional bias (5); Domain (1); Zinc finger (4) FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +O35256 PR4A1_MOUSE Prolactin-4A1 (Placental prolactin-like protein A) (PLP-A) (PRL-like protein A) 227 26,336 Chain (1); Disulfide bond (2); Glycosylation (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000250}. TISSUE SPECIFICITY: Expressed specifically in placenta. Expressed in both trophoblast giant cells and spongiotrophoblast cells. {ECO:0000269|PubMed:9389542, ECO:0000269|PubMed:9472921}. +Q80XD8 PRAP1_MOUSE Proline-rich acidic protein 1 (Pregnancy-specific uterine protein) (Uterine-specific proline-rich acidic protein) 149 16,798 Chain (1); Sequence conflict (1); Signal peptide (1) FUNCTION: May play an important role in maintaining normal growth homeostasis in epithelial cells. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. TISSUE SPECIFICITY: Abundantly expressed in the uterus during late pregnancy by uterus epithelial cells. After birth expression rapidly decreases and is no longer found in the uterus by the third day. Also highly expressed in the small intestine where it shows a proximal-distal graded expression. {ECO:0000269|PubMed:10899595, ECO:0000269|PubMed:9065197}. +Q61878 PRG2_MOUSE Bone marrow proteoglycan (BMPG) (Proteoglycan 2) [Cleaved into: Eosinophil granule major basic protein (EMBP) (MBP)] 223 24,255 Chain (2); Disulfide bond (2); Domain (1); Propeptide (1); Signal peptide (1) FUNCTION: Cytotoxin and helminthotoxin. MBP also induces non-cytolytic histamine release from basophils. It is involved in antiparasitic defense mechanisms and immune hypersensitivity reactions (By similarity). {ECO:0000250}. PTM: Nitrated. {ECO:0000269|PubMed:18694936}. SUBCELLULAR LOCATION: Cytoplasmic granule {ECO:0000250}. Note=Matrix of eosinophil's large specific granule (crystalloid core). {ECO:0000250}. +Q9JL95 PRG3_MOUSE Proteoglycan 3 (Eosinophil major basic protein 2) 222 25,204 Alternative sequence (1); Chain (1); Disulfide bond (2); Domain (1); Frameshift (1); Signal peptide (1) FUNCTION: Possesses similar cytotoxic and cytostimulatory activities to PRG2/MBP. {ECO:0000250}. SUBCELLULAR LOCATION: Note=Localized to the eosinophil secondary granule. {ECO:0000269|PubMed:10770291}. TISSUE SPECIFICITY: Expressed in bone marrow, spleen, and thymus. Not detected in heart, liver or lung. {ECO:0000269|PubMed:10770291}. +Q9JM99 PRG4_MOUSE Proteoglycan 4 (Lubricin) (Megakaryocyte-stimulating factor) (Superficial zone proteoglycan) [Cleaved into: Proteoglycan 4 C-terminal part] 1054 115,996 Alternative sequence (3); Chain (2); Compositional bias (3); Disulfide bond (15); Domain (2); Glycosylation (60); Mutagenesis (8); Region (1); Repeat (39); Sequence conflict (4); Signal peptide (1); Site (1) FUNCTION: Plays a role in boundary lubrication within articulating joints. Prevents protein deposition onto cartilage from synovial fluid by controlling adhesion-dependent synovial growth and inhibiting the adhesion of synovial cells to the cartilage surface. {ECO:0000269|PubMed:15719068}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q92954}.; PTM: O-glycosylated; contains glycosaminoglycan chondroitin sulfate and keratan sulfate. O-glycosylated with sialylated oligosaccharides which are predominantly represented by the monosialylated core type I structure, NeuNAcalpha2-3Galbeta1-3GalNAc, with smaller amounts of disialylated O-glycans. {ECO:0000250|UniProtKB:Q92954}.; PTM: The disulfide bond between Cys-795 and Cys-1053 is essential for protein cleavage. {ECO:0000269|PubMed:16000300}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:16000300}. TISSUE SPECIFICITY: Highly expressed in cartilage, bone and liver and weakly expressed in heart, brain and muscle. Expressed in the surface chondrocytes and in synovial intimal cells. Isoform B is expressed in bone, small intestine, muscle, testis, heart, liver and lung. Isoform C and isoform D are widely expressed. {ECO:0000269|PubMed:11124536, ECO:0000269|PubMed:15719068}. +Q80V63 PRDM4_MOUSE PR domain zinc finger protein 4 (EC 2.1.1.-) (PR domain-containing protein 4) 803 88,145 Chain (1); Compositional bias (3); Domain (1); Erroneous initiation (1); Zinc finger (6) FUNCTION: May function as a transcription factor involved in cell differentiation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +O70343 PRGC1_MOUSE Peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PGC-1-alpha) (PPAR-gamma coactivator 1-alpha) (PPARGC-1-alpha) 797 90,588 Alternative sequence (7); Chain (1); Compositional bias (2); Domain (1); Helix (1); Modified residue (15); Motif (1); Mutagenesis (3); Region (2); Sequence conflict (2) FUNCTION: Transcriptional coactivator for steroid receptors and nuclear receptors. Greatly increases the transcriptional activity of PPARG and thyroid hormone receptor on the uncoupling protein promoter. Can regulate key mitochondrial genes that contribute to the program of adaptive thermogenesis. Plays an essential role in metabolic reprogramming in response to dietary availability through coordination of the expression of a wide array of genes involved in glucose and fatty acid metabolism. Induces the expression of PERM1 in the skeletal muscle in an ESRRA-dependent manner. Also involved in the integration of the circadian rhythms and energy metabolism. Required for oscillatory expression of clock genes, such as ARNTL/BMAL1 and NR1D1, through the coactivation of RORA and RORC, and metabolic genes, such as PDK4 and PEPCK. Isoform 4 specifically activates the expression of IGF1 and suppresses myostatin expression in skeletal muscle leading to muscle fiber hypertrophy. {ECO:0000269|PubMed:15744310, ECO:0000269|PubMed:17476214, ECO:0000269|PubMed:23217713, ECO:0000269|PubMed:9529258}. PTM: Phosphorylation by AMPK in skeletal muscle increases activation of its own promoter. Phosphorylated by CLK2. {ECO:0000269|PubMed:17609368, ECO:0000269|PubMed:20074525}.; PTM: Heavily acetylated by GCN5 and biologically inactive under conditions of high nutrients. Deacetylated by SIRT1 in low nutrients/high NAD conditions. {ECO:0000269|PubMed:15744310}.; PTM: Ubiquitinated. Ubiquitination by RNF34 induces proteasomal degradation. {ECO:0000250|UniProtKB:Q9UBK2}. SUBCELLULAR LOCATION: Nucleus. Nucleus, PML body. SUBUNIT: Homooligomer (By similarity). Interacts with MYBBP1A; inhibits MYBBP1A transcriptional activation. Interacts with PRDM16, LPIN1 and PML. Interacts (via LXXLL motif) with RORA and RORC (via AF-2 motif); activates RORA and RORC transcriptional activation. Interacts with LRPPRC (By similarity). Interacts with RNF34 (via RING-type zinc finger) (By similarity). {ECO:0000250|UniProtKB:Q9UBK2, ECO:0000269|PubMed:14744933, ECO:0000269|PubMed:16950137, ECO:0000269|PubMed:17476214, ECO:0000269|PubMed:17618855, ECO:0000269|PubMed:18483224, ECO:0000269|PubMed:22886304}. TISSUE SPECIFICITY: White quadriceps and red tibialis anterior (TA) muscles, liver, kidney and brown adipose tissue (at protein level). Skeletal muscle, brown adipose tissue, heart, kidney and brain. {ECO:0000269|PubMed:17476214, ECO:0000269|PubMed:23217713, ECO:0000269|PubMed:9529258}. +P99029 PRDX5_MOUSE Peroxiredoxin-5, mitochondrial (EC 1.11.1.15) (Antioxidant enzyme B166) (AOEB166) (Liver tissue 2D-page spot 2D-0014IV) (PLP) (Peroxiredoxin V) (Prx-V) (Peroxisomal antioxidant enzyme) (Thioredoxin peroxidase PMP20) 210 21,897 Active site (1); Alternative sequence (1); Chain (1); Disulfide bond (1); Domain (1); Modified residue (8); Motif (1); Sequence conflict (2); Transit peptide (1) FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. {ECO:0000269|PubMed:10679306}. SUBCELLULAR LOCATION: Isoform Mitochondrial: Mitochondrion {ECO:0000250|UniProtKB:P30044}.; SUBCELLULAR LOCATION: Isoform Cytoplasmic+peroxisomal: Cytoplasm {ECO:0000250|UniProtKB:P30044}. Peroxisome matrix {ECO:0000250|UniProtKB:P30044}. SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P30044}. TISSUE SPECIFICITY: Widely expressed. +O08709 PRDX6_MOUSE Peroxiredoxin-6 (EC 1.11.1.15) (1-Cys peroxiredoxin) (1-Cys PRX) (Acidic calcium-independent phospholipase A2) (aiPLA2) (EC 3.1.1.4) (Antioxidant protein 2) (Non-selenium glutathione peroxidase) (NSGPx) 224 24,871 Active site (2); Chain (1); Domain (1); Initiator methionine (1); Modified residue (7); Natural variant (1); Region (1); Sequence conflict (2); Site (1) FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. Also has phospholipase activity, and can therefore either reduce the oxidized sn-2 fatty acyl grup of phospholipids (peroxidase activity) or hydrolyze the sn-2 ester bond of phospholipids (phospholipase activity). These activities are dependent on binding to phospholipids at acidic pH and to oxidized phospholipds at cytosolic pH. Plays a role in cell protection against oxidative stress by detoxifying peroxides and in phospholipid homeostasis. {ECO:0000250|UniProtKB:P30041}. PTM: Irreversibly inactivated by overoxidation of Cys-47 to sulfinic acid (Cys-SO(2)H) and sulfonic acid (Cys-SO(3)H) forms upon oxidative stress. {ECO:0000250|UniProtKB:P30041}.; PTM: Phosphorylation at Thr-177 by MAP kinases increases the phospholipase activity of the enzyme. {ECO:0000250|UniProtKB:O35244}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O35244}. Lysosome {ECO:0000250|UniProtKB:O35244}. Note=Also found in lung secretory organelles (lamellar bodies). {ECO:0000250|UniProtKB:O35244}. SUBUNIT: Homodimer (By similarity). Interacts with GSTP1; mediates PRDX6 glutathionylation and regeneration (By similarity). Interacts with APEX1. Interacts with STH. May interact with FAM168B (By similarity). May interact with HTR2A (PubMed:14988405). {ECO:0000250|UniProtKB:O77834, ECO:0000250|UniProtKB:P30041, ECO:0000269|PubMed:14988405}. TISSUE SPECIFICITY: Highly expressed in heart, kidney and liver. Moderate expression in brain and stomach. Very low levels in intestine. +Q11011 PSA_MOUSE Puromycin-sensitive aminopeptidase (PSA) (EC 3.4.11.14) (Cytosol alanyl aminopeptidase) (AAP-S) 920 103,325 Active site (1); Binding site (1); Chain (1); Metal binding (3); Modified residue (1); Motif (1); Region (1); Sequence conflict (1); Site (1) FUNCTION: Aminopeptidase with broad substrate specificity for several peptides. Involved in proteolytic events essential for cell growth and viability. May act as regulator of neuropeptide activity. Plays a role in the antigen-processing pathway for MHC class I molecules. Involved in the N-terminal trimming of cytotoxic T-cell epitope precursors. Digests the poly-Q peptides found in many cellular proteins. {ECO:0000269|PubMed:7592939}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:7592939}. Nucleus {ECO:0000269|PubMed:7592939}. SUBUNIT: Monomer. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. Highest expression in brain, particularly the striatum and hippocampus. Expressed in Sertoli cells. {ECO:0000269|PubMed:10407043, ECO:0000269|PubMed:11376114, ECO:0000269|PubMed:7592939}. +Q99JI4 PSMD6_MOUSE 26S proteasome non-ATPase regulatory subunit 6 (26S proteasome regulatory subunit RPN7) (26S proteasome regulatory subunit S10) (p42A) 389 45,536 Chain (1); Domain (1); Sequence conflict (1) FUNCTION: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. {ECO:0000250|UniProtKB:Q15008}. SUBUNIT: Component of the 19S proteasome regulatory particle complex. The 26S proteasome consists of a 20S core particle (CP) and two 19S regulatory subunits (RP). The regulatory particle is made of a lid composed of 9 subunits including PSMD6, a base containing 6 ATPases and few additional components. {ECO:0000250|UniProtKB:Q15008, ECO:0000269|PubMed:16857966}. +Q9CX56 PSMD8_MOUSE 26S proteasome non-ATPase regulatory subunit 8 (26S proteasome regulatory subunit RPN12) (26S proteasome regulatory subunit S14) 353 39,930 Chain (1); Cross-link (1); Domain (1); Erroneous initiation (1) FUNCTION: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. {ECO:0000250|UniProtKB:P48556}. SUBUNIT: Component of the 19S proteasome regulatory particle complex. The 26S proteasome consists of a 20S core particle (CP) and two 19S regulatory subunits (RP). The regulatory particle is made of a lid composed of 9 subunits including PSMD8, a base containing 6 ATPases and few additional components. {ECO:0000250|UniProtKB:P48556}. +P0C7N9 PSMG4_MOUSE Proteasome assembly chaperone 4 (PAC-4) (mPAC4) 123 13,974 Chain (1) FUNCTION: Chaperone protein which promotes assembly of the 20S proteasome. {ECO:0000269|PubMed:17707236}. SUBUNIT: Interacts with PSMG3. Associates with alpha subunits of the 20S proteasome. {ECO:0000269|PubMed:17707236}. +Q9D3U0 PUS10_MOUSE Putative tRNA pseudouridine synthase Pus10 (EC 5.4.99.25) (Coiled-coil domain-containing protein 139) (tRNA pseudouridine 55 synthase) (Psi55 synthase) (tRNA pseudouridylate synthase) (tRNA-uridine isomerase) 527 59,710 Active site (1); Binding site (2); Chain (1); Coiled coil (1); Modified residue (1); Region (2); Sequence conflict (12) FUNCTION: Pseudouridylate synthases catalyze pseudouridination of structural RNAs, including transfer, ribosomal, and splicing RNAs. PUS10 catalyzes the formation of the universal psi55 in the GC loop of transfer RNAs (Probable). Modulator of TRAIL-induced cell death via activation of procaspase 8 and BID cleavage. Required for the progression of the apoptotic signal through intrinsic mitochondrial cell death (By similarity). {ECO:0000250, ECO:0000305}. PTM: Proteolytically cleaved during TRAIL-induced cell death. Cleaved, in vitro, either by caspase-3 or caspase-8 (By similarity). {ECO:0000250}. +P13405 RB_MOUSE Retinoblastoma-associated protein (pRb) (Rb) (pp105) 921 105,367 Chain (1); Compositional bias (2); Initiator methionine (1); Modified residue (25); Motif (1); Mutagenesis (3); Region (6); Sequence conflict (1) FUNCTION: Key regulator of entry into cell division that acts as a tumor suppressor. Promotes G0-G1 transition when phosphorylated by CDK3/cyclin-C. Acts as a transcription repressor of E2F1 target genes. The underphosphorylated, active form of RB1 interacts with E2F1 and represses its transcription activity, leading to cell cycle arrest. Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation. Recruits and targets histone methyltransferases SUV39H1, KMT5B and KMT5C, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-20' trimethylation. Inhibits the intrinsic kinase activity of TAF1. Mediates transcriptional repression by SMARCA4/BRG1 by recruiting a histone deacetylase (HDAC) complex to the c-FOS promoter. In resting neurons, transcription of the c-FOS promoter is inhibited by BRG1-dependent recruitment of a phospho-RB1-HDAC1 repressor complex. Upon calcium influx, RB1 is dephosphorylated by calcineurin, which leads to release of the repressor complex (By similarity). {ECO:0000250, ECO:0000269|PubMed:15750587, ECO:0000269|PubMed:16612004}. PTM: Phosphorylated by CDK6 and CDK4, and subsequently by CDK2 at Ser-561 in G1, thereby releasing E2F1 which is then able to activate cell growth. Dephosphorylated at the late M phase. Phosphorylation of threonine residues in domain C promotes interaction between the C-terminal domain C and the Pocket domain, and thereby inhibits interactions with heterodimeric E2F/DP transcription factor complexes. Dephosphorylated at Ser-788 by calcineruin upon calcium stimulation. CDK3/cyclin-C-mediated phosphorylation at Ser-800 and Ser-804 is required for G0-G1 transition (By similarity). Phosphorylated by CDK1 and CDK2 upon TGFB1-mediated apoptosis (By similarity). {ECO:0000250}.; PTM: Monomethylation at Lys-803 by SMYD2 enhances phosphorylation at Ser-800 and Ser-804, and promotes cell cycle progression. Monomethylation at Lys-853 by SMYD2 promotes interaction with L3MBTL1 (By similarity). N-terminus is methylated by METTL11A/NTM1. {ECO:0000250, ECO:0000269|PubMed:20668449}.; PTM: Acetylation at Lys-866 and Lys-867 regulates subcellular localization, at least during keratinocytes differentiation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: The hypophosphorylated form interacts with and sequesters the E2F1 transcription factor. Interacts with heterodimeric E2F/DP transcription factor complexes containing TFDP1 and either E2F1, E2F3, E2F4 or E2F5, or TFDP2 and E2F4. The unphosphorylated form interacts with EID1, ARID3B, KDM5A, SUV39H1, MJD2A/JHDM3A and THOC1. Interacts with the N-terminal domain of TAF1. Interacts with SNW1, ATAD5, AATF, DNMT1, LIN9, LMNA, KMT5B, KMT5C, PELP1, UHRF2, TMPO-alpha and USP4. May interact with NDC80. Interacts with GRIP1 and UBR4. Interacts with ARID4A and KDM5B. Interacts with E4F1 and LIMD1. Interacts with SMARCA4/BRG1 and HDAC1. Interacts with USP4. Interacts (when methylated at Lys-853) with L3MBTL1. Binds to CDK1 and CDK2. Interacts with CHEK2; phosphorylates RB1 (By similarity). Interacts with PRMT2. Interacts with CEBPA. P-TEFB complex interacts with RB1; promotes phosphorylation of RB1 (By similarity). {ECO:0000250|UniProtKB:P06400, ECO:0000250|UniProtKB:P33568, ECO:0000269|PubMed:10869426, ECO:0000269|PubMed:10888886, ECO:0000269|PubMed:11571651, ECO:0000269|PubMed:15750587, ECO:0000269|PubMed:15983387, ECO:0000269|PubMed:16612004, ECO:0000269|PubMed:16616919}. TISSUE SPECIFICITY: Expressed in the cell nuclei of renal tubules, hepatocytes and skeletal muscles. Colocalizes with RB1CC1 in various tissues. {ECO:0000269|PubMed:12095676}. +Q9CWH4 RE114_MOUSE Meiotic recombination protein REC114 259 28,211 Chain (1); Compositional bias (1) FUNCTION: Required for DNA double-strand breaks (DSBs) formation in unsynapsed regions during meiotic recombination (PubMed:20551173, PubMed:27723721). Probably acts by forming a complex with IHO1/CCDC36 and MEI4, which activates DSBs formation in unsynapsed regions, an essential step to ensure completion of synapsis (PubMed:27723721). {ECO:0000269|PubMed:20551173, ECO:0000269|PubMed:27723721}. SUBUNIT: Interacts with MEI4 (PubMed:20551173). Interacts with IHO1/CCDC36 (PubMed:27723721). Part of the MCD recombinosome complex, at least composed of IHO1/CCDC36, REC114 and MEI4 (PubMed:27723721). {ECO:0000269|PubMed:20551173, ECO:0000269|PubMed:27723721}. TISSUE SPECIFICITY: Expressed in adult testis and embryonic ovary. Also expressed at low levels in liver. {ECO:0000269|PubMed:20551173}. +Q9D8T3 REBL1_MOUSE GTPase RhebL1 (Ras homolog enriched in brain-like protein 1) (Rheb-like protein 1) 184 20,934 Binding site (1); Chain (1); Lipidation (1); Metal binding (1); Modified residue (1); Motif (1); Nucleotide binding (4); Propeptide (1) FUNCTION: Binds GTP and exhibits intrinsic GTPase activity. May activate NF-kappa-B-mediated gene transcription. Promotes signal transduction through MTOR, activates RPS6KB1, and is a downstream target of the small GTPase-activating proteins TSC1 and TSC2 (By similarity). {ECO:0000250|UniProtKB:Q8TAI7}. SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250|UniProtKB:Q8TAI7}; Lipid-anchor {ECO:0000250|UniProtKB:Q8TAI7}; Cytoplasmic side {ECO:0000250|UniProtKB:Q8TAI7}. Cytoplasm {ECO:0000250|UniProtKB:Q8TAI7}. SUBUNIT: Interacts with MTOR. {ECO:0000250|UniProtKB:Q8TAI7}. +O88451 RDH7_MOUSE Retinol dehydrogenase 7 (EC 1.1.1.105) (Cis-retinol/3alpha-hydroxysterol short-chain dehydrogenase isozyme 2) (Cis-retinol/androgen dehydrogenase type 2) (CRAD-2) 316 35,660 Active site (1); Binding site (1); Chain (1); Nucleotide binding (1) Cofactor metabolism; retinol metabolism. FUNCTION: Acts on androgens and retinols, i.e. has steroid 3-alpha- and 17-beta-dehydrogenase and cis/trans-retinol catalytic activities. {ECO:0000269|PubMed:9651397}. SUBCELLULAR LOCATION: Microsome {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in liver. Also expressed in lung, eye, kidney, and brain. {ECO:0000269|PubMed:9651397}. +Q5U4E2 REPI1_MOUSE Replication initiator 1 (Zinc finger protein 464) (Zfp-464) 545 61,830 Chain (1); Frameshift (1); Modified residue (3); Sequence conflict (2); Zinc finger (15) FUNCTION: Sequence-specific double-stranded DNA-binding protein required for initiation of chromosomal DNA replication. Binds on 5'-ATT-3' reiterated sequences downstream of the origin of bidirectional replication (OBR) and a second, homologous ATT sequence of opposite orientation situated within the OBR zone. Facilitates DNA bending (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Homodimers and homomultimers. Found in a complex with RIP60 and RIP100 (By similarity). {ECO:0000250}. +Q9CQV4 RETR3_MOUSE Reticulophagy regulator 3 466 51,638 Alternative sequence (1); Chain (1); Modified residue (15); Motif (1); Sequence conflict (2); Transmembrane (3) TRANSMEM 81 101 Helical. {ECO:0000255}.; TRANSMEM 169 186 Helical. {ECO:0000255}.; TRANSMEM 187 207 Helical. {ECO:0000255}. FUNCTION: Mediates NRF1-enhanced neurite outgrowth. {ECO:0000250|UniProtKB:Q86VR2}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Interacts with ATG8 family modifier proteins MAP1LC3A, MAP1LC3B, GABARAP and GABARAPL1. {ECO:0000250|UniProtKB:Q86VR2}. DOMAIN: The LIR motif interacts with ATG8 family proteins. {ECO:0000250|UniProtKB:Q86VR2}. TISSUE SPECIFICITY: Mainly expressed in the central nervous system and in parenchymatous organs including liver, lung and kidney. {ECO:0000269|PubMed:19838196}. +Q8BP71 RFOX2_MOUSE RNA binding protein fox-1 homolog 2 (Fox-1 homolog B) (Fox-1 homolog Fxh) (Hexaribonucleotide-binding protein 2) (RNA-binding motif protein 9) (RNA-binding protein 9) 449 47,330 Alternative sequence (9); Chain (1); Compositional bias (1); Domain (1); Modified residue (21); Sequence conflict (3); Site (8) FUNCTION: RNA-binding protein that regulates alternative splicing events by binding to 5'-UGCAUGU-3' elements. Prevents binding of U2AF2 to the 3'-splice site. Regulates alternative splicing of tissue-specific exons and of differentially spliced exons during erythropoiesis. Seems to act as a coregulatory factor of ER-alpha (By similarity). {ECO:0000250, ECO:0000269|PubMed:15824060, ECO:0000269|PubMed:16260614, ECO:0000269|PubMed:16449636, ECO:0000269|PubMed:16537540, ECO:0000269|PubMed:17101796, ECO:0000269|PubMed:17715393}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. SUBUNIT: Interacts with ER-alpha N-terminal activation domain. {ECO:0000250}. TISSUE SPECIFICITY: Detected in brain neurons (at protein level). Detected in heart, brain, embryo, lung, liver, kidney and ovary. {ECO:0000269|PubMed:11401487, ECO:0000269|PubMed:16260614}. +Q6PEE3 RIR2B_MOUSE Ribonucleoside-diphosphate reductase subunit M2 B (EC 1.17.4.1) (TP53-inducible ribonucleotide reductase M2 B) (p53-inducible ribonucleotide reductase small subunit 2-like protein) (p53R2) 351 40,804 Active site (1); Chain (1); Metal binding (7) Genetic information processing; DNA replication. FUNCTION: Plays a pivotal role in cell survival by repairing damaged DNA in a p53/TP53-dependent manner. Supplies deoxyribonucleotides for DNA repair in cells arrested at G1 or G2. Contains an iron-tyrosyl free radical center required for catalysis. Forms an active ribonucleotide reductase (RNR) complex with RRM1 which is expressed both in resting and proliferating cells in response to DNA damage. {ECO:0000269|PubMed:11517226, ECO:0000269|PubMed:12858174}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Translocates from cytoplasm to nucleus in response to DNA damage. {ECO:0000250}. SUBUNIT: Heterotetramer with large (RRM1) subunit. Interacts with p53/TP53. Interacts with RRM1 in response to DNA damage (By similarity). {ECO:0000250}. +Q920A5 RISC_MOUSE Retinoid-inducible serine carboxypeptidase (EC 3.4.16.-) (Serine carboxypeptidase 1) 452 50,965 Active site (3); Chain (1); Glycosylation (5); Sequence conflict (1); Signal peptide (1) FUNCTION: May be involved in vascular wall and kidney homeostasis. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q9QY40 PLXB3_MOUSE Plexin-B3 (Plexin-6) 1902 208,366 Chain (1); Disulfide bond (10); Domain (8); Erroneous gene model prediction (1); Glycosylation (10); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1246 1266 Helical. {ECO:0000255}. TOPO_DOM 37 1245 Extracellular. {ECO:0000255}.; TOPO_DOM 1267 1902 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for SEMA5A that plays a role in axon guidance, invasive growth and cell migration. Stimulates neurite outgrowth and mediates Ca(2+)/Mg(2+)-dependent cell aggregation. In glioma cells, SEMA5A stimulation of PLXNB3 results in the disassembly of F-actin stress fibers, disruption of focal adhesions and cellular collapse as well as inhibition of cell migration and invasion through ARHGDIA-mediated inactivation of RAC1 (By similarity). Seem to be non-essential for normal development and function of the central nervous system. {ECO:0000250, ECO:0000269|PubMed:15218527, ECO:0000269|PubMed:20696765}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Colocalizes with RIT2/RIN at the plasma membrane. {ECO:0000250}. SUBUNIT: Binds MET and MST1R. Interacts with RIT2/RIN. May form homodimers (via Sema domain) (By similarity). Interacts (via cytoplasmic domain) with FSCN1, ARHGDIA and RAC1. {ECO:0000250, ECO:0000269|PubMed:20696765, ECO:0000269|PubMed:21706053}. TISSUE SPECIFICITY: Expressed in brain (at protein level). In cerebellum, strongest expression detected in Purkinje and granular cells. Detected at very low levels in several fetal tissues, including dorsal root ganglia (DRG), heart, lung, optic bulb, brain and liver. {ECO:0000269|PubMed:15218527, ECO:0000269|PubMed:16122393}. +P55065 PLTP_MOUSE Phospholipid transfer protein (Lipid transfer protein II) 493 54,453 Chain (1); Disulfide bond (1); Glycosylation (7); Sequence conflict (9); Signal peptide (1) FUNCTION: Facilitates the transfer of a spectrum of different lipid molecules, including diacylglycerol, phosphatidic acid, sphingomyelin, phosphatidylcholine, phosphatidylglycerol, cerebroside and phosphatidyl ethanolamine. Essential for the transfer of excess surface lipids from triglyceride-rich lipoproteins to HDL, thereby facilitating the formation of smaller lipoprotein remnants, contributing to the formation of LDL, and assisting in the maturation of HDL particles. PLTP also plays a key role in the uptake of cholesterol from peripheral cells and tissues that is subsequently transported to the liver for degradation and excretion. Two distinct forms of PLTP exist in plasma: an active form that can transfer PC from phospholipid vesicles to high-density lipoproteins (HDL), and an inactive form that lacks this capability (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Highest in lung, adipose tissue, brain, and heart. +Q8JZW8 PNMA3_MOUSE Paraneoplastic antigen Ma3 homolog 466 54,041 Chain (1); Compositional bias (2); Zinc finger (1) SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the cerebrum and cerebellum. {ECO:0000269|PubMed:19366867}. +A3KGS3 RGPA2_MOUSE Ral GTPase-activating protein subunit alpha-2 (250 kDa substrate of Akt) (AS250) (P220) 1872 210,288 Alternative sequence (2); Chain (1); Domain (1); Erroneous gene model prediction (3); Erroneous initiation (1); Modified residue (9); Sequence caution (1); Sequence conflict (4) FUNCTION: Catalytic subunit of the heterodimeric RalGAP2 complex which acts as a GTPase activator for the Ras-like small GTPases RALA and RALB. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Component of the heterodimeric RalGAP2 complex with RALGAPB. Heterodimerization is required for activity (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Abundantly expressed in testis, pancreas, lung, thymus, brown fat, and white fat. {ECO:0000269|PubMed:16490346}. +P31361 PO3F3_MOUSE POU domain, class 3, transcription factor 3 (Brain-specific homeobox/POU domain protein 1) (Brain-1) (Brn-1) (Octamer-binding protein 8) (Oct-8) (Octamer-binding transcription factor 8) (OTF-8) 497 50,200 Chain (1); Compositional bias (4); DNA binding (1); Domain (1); Sequence conflict (2) FUNCTION: Transcription factor that acts synergistically with SOX11 and SOX4 (By similarity). Plays a role in neuronal development. Is implicated in an enhancer activity at the embryonic met-mesencephalic junction; the enhancer element contains the octamer motif (5'-ATTTGCAT-3'). {ECO:0000250, ECO:0000269|PubMed:10473120, ECO:0000269|PubMed:12130536, ECO:0000269|PubMed:19527706}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-ProRule:PRU00530, ECO:0000269|PubMed:10473120}. TISSUE SPECIFICITY: Brain. +P17208 PO4F1_MOUSE POU domain, class 4, transcription factor 1 (Brain-specific homeobox/POU domain protein 3A) (Brain-3A) (Brn-3A) (Brn-3.0) 421 42,767 Alternative sequence (1); Chain (1); Compositional bias (3); DNA binding (1); Domain (1); Motif (1); Mutagenesis (1); Sequence conflict (1) FUNCTION: Multifunctional transcription factor with different regions mediating its different effects (PubMed:10640682, PubMed:8621561, PubMed:9694219, PubMed:9722627). Acts by binding (via its C-terminal domain) to sequences related to the consensus octamer motif 5'-ATGCAAAT-3' in the regulatory regions of its target genes (PubMed:8621561, PubMed:17668438). Regulates the expression of specific genes involved in differentiation and survival within a subset of neuronal lineages. It has been shown that activation of some of these genes requires its N-terminal domain, maybe through a neuronal-specific cofactor (PubMed:12934100). Ativates BCL2 expression and protects neuronal cells from apoptosis (via the N-terminal domain) (PubMed:9722627). Induces neuronal process outgrowth and the coordinate expression of genes encoding synaptic proteins (PubMed:8972215). Exerts its major developmental effects in somatosensory neurons and in brainstem nuclei involved in motor control. Stimulates the binding affinity of the nuclear estrogene receptor ESR1 to DNA estrogen response element (ERE), and hence modulates ESR1-induced transcriptional activity (PubMed:9448000). May positively regulate POU4F2 and POU4F3 (PubMed:8876243). Regulates dorsal root ganglion sensory neuron specification and axonal projection into the spinal cord (PubMed:22326227). Plays a role in TNFSF11-mediated terminal osteoclast differentiation (PubMed:17668438). Negatively regulates its own expression interacting directly with a highly conserved autoregulatory domain surrounding the transcription initiation site (PubMed:12441296). {ECO:0000269|PubMed:10640682, ECO:0000269|PubMed:12441296, ECO:0000269|PubMed:12934100, ECO:0000269|PubMed:17668438, ECO:0000269|PubMed:22326227, ECO:0000269|PubMed:8621561, ECO:0000269|PubMed:8876243, ECO:0000269|PubMed:8972215, ECO:0000269|PubMed:9448000, ECO:0000269|PubMed:9694219, ECO:0000269|PubMed:9722627}.; FUNCTION: Isoform 2: Able to act as transcription factor, cannot regulate the expression of the same subset of genes than isoform 1 (PubMed:12934100). Does not have antiapoptotic effect on neuronal cells (PubMed:9722627). {ECO:0000269|PubMed:12934100, ECO:0000269|PubMed:9722627}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17668438}. Cytoplasm {ECO:0000269|PubMed:17668438}. SUBUNIT: Interacts (via N-terminus) with RIT2; the interaction controls POU4F1 transactivation activity on some neuronal target genes (PubMed:12934100). Isoform 1 interacts with POU4F2 isoform 2; this interaction inhibits both POU4F1 DNA-binding and transcriptional activities (PubMed:8537352). Isoform 1 interacts (C-terminus) with ESR1 (via DNA-binding domain); this interaction decreases the estrogen receptor ESR1 transcriptional activity in a DNA- and ligand 17-beta-estradiol-independent manner (PubMed:9448000). {ECO:0000269|PubMed:12934100, ECO:0000269|PubMed:8537352, ECO:0000269|PubMed:9448000}. DOMAIN: The C-terminal domain is able to act as both DNA-binding domain and a transcriptional activator. The N-terminal domain is also required for transactivation activity on some target genes acting as a discrete activation domain (PubMed:8621561, PubMed:9722627). Neurite outgrowth and expression of genes required for synapse formation are primarily dependent on the C-terminal domain, however the N-terminal domain is required for maximal induction (PubMed:8972215). {ECO:0000269|PubMed:8621561, ECO:0000269|PubMed:8972215, ECO:0000269|PubMed:9722627}. TISSUE SPECIFICITY: Expressed in mature osteoclasts (at protein level) (PubMed:17668438). Brain, peripheral sensory nervous system and retina (PubMed:8162704). In the adult nervous system, predominates in the medial habenula, superficial gray of the superior colliculus, red nucleus, mesencephalic nucleus of the trigeminal ganglion, nucleus ambiguus, inferior olivary nucleus, and peripheral sensory ganglia (PubMed:8290353). {ECO:0000269|PubMed:17668438, ECO:0000269|PubMed:8162704, ECO:0000269|PubMed:8290353}. +Q9QZH3 PPIE_MOUSE Peptidyl-prolyl cis-trans isomerase E (PPIase E) (EC 5.2.1.8) (Cyclophilin E) (Cyclophilin-33) (Rotamase E) 301 33,449 Chain (1); Domain (2); Modified residue (2); Sequence conflict (2) FUNCTION: Involved in pre-mRNA splicing as component of the spliceosome. Combines RNA-binding and PPIase activities. Binds mRNA and has a preference for single-stranded RNA molecules with poly-A and poly-U stretches, suggesting it binds to the poly(A)-region in the 3'-UTR of mRNA molecules. Catalyzes the cis-trans isomerization of proline imidic peptide bonds in proteins. Inhibits KMT2A activity; this requires proline isomerase activity. {ECO:0000250|UniProtKB:Q9UNP9}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UNP9}. SUBUNIT: Identified in the spliceosome C complex. Component of the XAB2 complex, a multimeric protein complex composed of XAB2, PRPF19, AQR, ZNF830, ISY1, and PPIE. Identified in a pentameric intron-binding (IB) complex composed of AQR, XAB2, ISY1, ZNF830 and PPIE that is incorporated into the spliceosome as a preassembled complex. The IB complex does not contain PRPF19. Interacts (via RNA-binding domain) with KMT2A (via the third PHD-type zinc-finger). {ECO:0000250|UniProtKB:Q9UNP9}. DOMAIN: The RRM domain mediates both interaction with RNA and with KMT2A (via the third PHD-type zinc-finger), but has much higher affinity for the KMT2A PHD-type zinc-finger. {ECO:0000250|UniProtKB:Q9UNP9}. +Q99KR7 PPIF_MOUSE Peptidyl-prolyl cis-trans isomerase F, mitochondrial (PPIase F) (EC 5.2.1.8) (Cyclophilin D) (CyP-D) (CypD) (Cyclophilin F) (Rotamase F) 206 21,737 Chain (1); Domain (1); Modified residue (7); Transit peptide (1) FUNCTION: PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. Involved in regulation of the mitochondrial permeability transition pore (mPTP). It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probability of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated. In cooperation with mitochondrial TP53 is involved in activating oxidative stress-induced necrosis. Involved in modulation of mitochondrial membrane F(1)F(0) ATP synthase activity and regulation of mitochondrial matrix adenine nucleotide levels. Has anti-apoptotic activity independently of mPTP and in cooperation with BCL2 inhibits cytochrome c-dependent apoptosis. {ECO:0000269|PubMed:15800626, ECO:0000269|PubMed:15800627, ECO:0000269|PubMed:16103352, ECO:0000269|PubMed:18684715, ECO:0000269|PubMed:19801635, ECO:0000269|PubMed:21281446, ECO:0000269|PubMed:22726440}. PTM: Deacteylated at Lys-166 by SIRT3. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. SUBUNIT: Associates with the mitochondrial membrane ATP synthase F(1)F(0) ATP synthase; the association is increased by inorganic phosphate (Pi) and decreased by cyclosporin A (CsA). Interacts with ATP5F1B; ATP5PD and ATP5PO. Interacts with SLC25A3; the interaction is impaired by CsA. Interacts with BCL2; the interaction is impaired by CsA. Interacts with TP53; the association implicates preferentially tetrameric TP53, is induced by oxidative stress and is impaired by CsA. Interacts with C1QBP. Interacts with MCUR1. Component of the mitochondrial permeability transition pore complex (mPTPC), at least composed of SPG7, VDAC1 and PPIF. Interacts with SPG7 (By similarity). {ECO:0000250|UniProtKB:P30405, ECO:0000269|PubMed:20950273, ECO:0000269|PubMed:21212461, ECO:0000269|PubMed:21281446, ECO:0000269|PubMed:22726440}. +Q9D6D8 PPIL6_MOUSE Probable inactive peptidyl-prolyl cis-trans isomerase-like 6 (PPIase) (Cyclophilin-like protein PPIL6) 278 31,869 Chain (1); Domain (1) FUNCTION: Probable inactive PPIase with no peptidyl-prolyl cis-trans isomerase activity. {ECO:0000250|UniProtKB:Q8IXY8}. +Q99M15 PPIP2_MOUSE Proline-serine-threonine phosphatase-interacting protein 2 (PEST phosphatase-interacting protein 2) (Macrophage actin-associated tyrosine-phosphorylated protein) (pp37) 334 38,948 Chain (1); Coiled coil (1); Domain (1); Initiator methionine (1); Modified residue (2); Sequence conflict (1) FUNCTION: Binds to F-actin. May be involved in regulation of the actin cytoskeleton. PTM: Phosphorylated on tyrosine. SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein. TISSUE SPECIFICITY: Expressed in macrophage-containing tissues, including bone marrow, spleen, liver, kidney, intestine and brain. +Q9D787 PPIL2_MOUSE RING-type E3 ubiquitin-protein ligase PPIL2 (EC 2.3.2.27) (CYC4) (Probable inactive peptidyl-prolyl cis-trans isomerase-like 2) (PPIase) 521 59,065 Chain (1); Coiled coil (1); Cross-link (1); Domain (2); Modified residue (1); Sequence conflict (1) Protein modification; protein ubiquitination. FUNCTION: Has a ubiquitin-protein ligase activity acting as an E3 ubiquitin protein ligase or as an ubiquitin-ubiquitin ligase promoting elongation of ubiquitin chains on substrates. By mediating 'Lys-48'-linked polyubiquitination of proteins could target them for proteasomal degradation. May also function as a chaperone, playing a role in transport to the cell membrane of BSG/Basigin for instance. Probable inactive PPIase with no peptidyl-prolyl cis-trans isomerase activity. {ECO:0000250|UniProtKB:Q13356}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13356}. SUBUNIT: Interacts with BSG. Interacts (via the PPIase cyclophilin-type domain) with CRNKL1; they may form a trimeric complex with HSP90. {ECO:0000250|UniProtKB:Q13356, ECO:0000269|PubMed:15189447}. +P61014 PPLA_MOUSE Cardiac phospholamban (PLB) 52 6,095 Chain (1); Lipidation (1); Modified residue (3); Mutagenesis (7); Topological domain (1); Transmembrane (1); Turn (1) TRANSMEM 32 52 Helical. {ECO:0000255}. TOPO_DOM 1 31 Cytoplasmic. {ECO:0000255}. FUNCTION: Reversibly inhibits the activity of ATP2A2 in cardiac sarcoplasmic reticulum by decreasing the apparent affinity of the ATPase for Ca(2+). Modulates the contractility of the heart muscle in response to physiological stimuli via its effects on ATP2A2. Modulates calcium re-uptake during muscle relaxation and plays an important role in calcium homeostasis in the heart muscle. The degree of ATP2A2 inhibition depends on the oligomeric state of PLN. ATP2A2 inhibition is alleviated by PLN phosphorylation. {ECO:0000269|PubMed:22971924, ECO:0000269|PubMed:26816378}. PTM: Phosphorylated at Thr-17 by CaMK2, and in response to beta-adrenergic stimulation. Phosphorylation by DMPK may stimulate sarcoplasmic reticulum calcium uptake in cardiomyocytes (By similarity). Phosphorylation by PKA abolishes the inhibition of ATP2A2-mediated calcium uptake. {ECO:0000250|UniProtKB:P26678, ECO:0000269|PubMed:20890288, ECO:0000269|PubMed:22971924}.; PTM: Palmitoylated by ZDHHC16, promoting formation of the homopentamer. {ECO:0000269|PubMed:26644582}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:26816378}; Single-pass membrane protein {ECO:0000255}. Sarcoplasmic reticulum membrane {ECO:0000250|UniProtKB:P26678}; Single-pass membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000250|UniProtKB:A4IFH6}; Single-pass membrane protein {ECO:0000255}. Membrane {ECO:0000269|PubMed:20890288}; Single-pass membrane protein {ECO:0000255}. Note=Colocalizes with HAX1 at the endoplasmic reticulum. Colocalizes with DMPK a the sarcoplasmic reticulum. {ECO:0000250|UniProtKB:P26678}. SUBUNIT: Homopentamer (PubMed:26644582). Interacts with HAX1 and ATP2A2 (By similarity). {ECO:0000250|UniProtKB:P26678, ECO:0000269|PubMed:26644582}. +Q80TL0 PPM1E_MOUSE Protein phosphatase 1E (EC 3.1.3.16) (Ca(2+)/calmodulin-dependent protein kinase phosphatase N) (CaMKP-N) (CaMKP-nucleus) (CaMKN) (Partner of PIX 1) (Partner of PIX-alpha) (Partner of PIXA) 749 83,419 Chain (1); Compositional bias (2); Domain (1); Metal binding (5); Modified residue (2); Region (1); Repeat (7); Sequence conflict (1) FUNCTION: Protein phosphatase that inactivates multifunctional CaM kinases such as CAMK4 and CAMK2. Dephosphorylates and inactivates PAK. May play a role in the inhibition of actin fiber stress breakdown and in morphological changes driven by TNK2/CDC42 (By similarity). Dephosphorylates PRKAA2. {ECO:0000250, ECO:0000269|PubMed:23088624}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8WY54}. Cytoplasm {ECO:0000250|UniProtKB:Q8WY54}. Note=A truncated form, major form, with the C-terminal part missing, is mostly found in the cytoplasm and a little in the nucleus. The full-length, minor form, is found in the nucleus. {ECO:0000250|UniProtKB:Q8WY54}. SUBUNIT: Heterotrimer. Interacts with PAX1 and ARHGEF6 (or ARHGEF7) (By similarity). {ECO:0000250}. +Q61074 PPM1G_MOUSE Protein phosphatase 1G (EC 3.1.3.16) (Fibroblast growth factor-inducible protein 13) (FIN13) (Protein phosphatase 1C) (Protein phosphatase 2C isoform gamma) (PP2C-gamma) (Protein phosphatase magnesium-dependent 1 gamma) 542 58,728 Chain (1); Compositional bias (1); Domain (1); Initiator methionine (1); Lipidation (1); Metal binding (5); Modified residue (4); Sequence conflict (1) FUNCTION: May be involved in regulation of cell cycle. {ECO:0000269|PubMed:9271424}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9271424}. Membrane {ECO:0000250|UniProtKB:O15355}; Lipid-anchor {ECO:0000250|UniProtKB:O15355}. SUBUNIT: Interacts with NOL3; may dephosphorylate NOL3. {ECO:0000250|UniProtKB:F1LNI5}. TISSUE SPECIFICITY: Highly expressed in testis. Low level of expression in kidney. Also expressed in a number of tissues undergoing proliferation including embryo, uterus at pregnancy, placenta, and ovaries. +Q149T7 PPM1J_MOUSE Protein phosphatase 1J (EC 3.1.3.16) (Protein phosphatase 2C isoform zeta) (PP2C-zeta) 507 55,550 Chain (1); Domain (1); Erroneous initiation (1); Modified residue (3); Sequence conflict (3) SUBUNIT: Interacts with UBE2I/UBC9. {ECO:0000269|PubMed:12633878}. TISSUE SPECIFICITY: Specifically expressed in the testicular germ cells. {ECO:0000269|PubMed:12633878}. +Q8BHN0 PPM1L_MOUSE Protein phosphatase 1L (EC 3.1.3.16) (Protein phosphatase 1-like) (Protein phosphatase 2C isoform epsilon) (PP2C-epsilon) 360 41,049 Alternative sequence (2); Chain (1); Domain (1); Erroneous initiation (1); Metal binding (5); Mutagenesis (5); Sequence conflict (6); Topological domain (2); Transmembrane (1) TRANSMEM 26 42 Helical. {ECO:0000255}. TOPO_DOM 1 25 Extracellular. {ECO:0000255}.; TOPO_DOM 43 360 Cytoplasmic. {ECO:0000255}. FUNCTION: Acts as a suppressor of the SAPK signaling pathways by associating with and dephosphorylating MAP3K7/TAK1 and MAP3K5, and by attenuating the association between MAP3K7/TAK1 and MAP2K4 or MAP2K6. {ECO:0000269|PubMed:12556533}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Interacts with MAP3K7/TAK1 and MAP3K5. {ECO:0000269|PubMed:12556533, ECO:0000269|PubMed:17456047}. TISSUE SPECIFICITY: Expressed in brain, heart, testis, liver, lung and skeletal muscle. {ECO:0000269|PubMed:12556533}. +Q7TPM1 PRC2B_MOUSE Protein PRRC2B (HLA-B-associated transcript 2-like 1) (Proline-rich coiled-coil protein 2B) 1486 160,913 Alternative sequence (2); Chain (1); Coiled coil (2); Compositional bias (2); Cross-link (2); Modified residue (15); Sequence conflict (1) +O54830 PR7A1_MOUSE Prolactin-7A1 (Placental prolactin-like protein E) (PLP-E) (PRL-like protein E) (Placental prolactin-like protein G) (PLP-G) (PRL-like protein G) 266 29,828 Alternative sequence (1); Chain (1); Disulfide bond (2); Glycosylation (5); Sequence conflict (2); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000250}. TISSUE SPECIFICITY: Expressed specifically in the placenta. Detected only in the trophoblast giant cells. +Q9CQ58 PR8A9_MOUSE Prolactin-8A9 (Placental prolactin-like protein C2) (PLP-C2) (PRL-like protein C2) (Prolactin-like protein C-beta) (PLP C-beta) 241 27,697 Chain (1); Disulfide bond (3); Glycosylation (2); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000250}. TISSUE SPECIFICITY: Detected only in placenta. Localized to spongiotrophoblasts and trophoblast giant cells of the placenta. {ECO:0000269|PubMed:10965907}. +O55103 PRAX_MOUSE Periaxin 1391 147,688 Alternative sequence (2); Chain (1); Compositional bias (3); Domain (1); Modified residue (12); Motif (2); Region (1); Repeat (45) FUNCTION: Scaffolding protein that functions as part of a dystroglycan complex in Schwann cells, and as part of EZR and AHNAK-containing complexes in eye lens fiber cells (PubMed:11430802, PubMed:21745462, PubMed:22764250). Required for the maintenance of the peripheral myelin sheath that is essential for normal transmission of nerve impulses and normal perception of sensory stimuli (PubMed:10839370). Required for normal transport of MBP mRNA from the perinuclear to the paranodal regions (PubMed:15356632). Required for normal remyelination after nerve injury (PubMed:10839370). Required for normal elongation of Schwann cells and normal length of the internodes between the nodes of Ranvier. The demyelinated nodes of Ranvier permit saltatory transmission of nerve impulses; shorter internodes cause slower transmission of nerve impulses (PubMed:15356632, PubMed:23022068). Required for the formation of appositions between the abaxonal surface of the myelin sheath and the Schwann cell plasma membrane; the Schwann cell cytoplasm is restricted to regions between these appositions (PubMed:15356632, PubMed:23022068). Required for the formation of Cajal bands and of Schmidt-Lanterman incisures that correspond to short, cytoplasm-filled regions on myelinated nerves (PubMed:23022068, PubMed:22764250). Recruits DRP2 to the Schwann cell plasma membrane (PubMed:11430802, PubMed:23022068, PubMed:22764250). Required for normal protein composition of the eye lens fiber cell plasma membrane and normal eye lens fiber cell morphology (PubMed:21745462). {ECO:0000269|PubMed:10839370, ECO:0000269|PubMed:11430802, ECO:0000269|PubMed:15356632, ECO:0000269|PubMed:22764250, ECO:0000269|PubMed:23022068}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21745462}. Cell junction {ECO:0000269|PubMed:21745462}. Note=Colocalizes with ACTB at tricellular junctions between eye lens fiber cells. {ECO:0000269|PubMed:21745462}.; SUBCELLULAR LOCATION: Isoform 1: Cell membrane {ECO:0000269|PubMed:9488714}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Nucleus {ECO:0000269|PubMed:10671475}. Cytoplasm {ECO:0000250|UniProtKB:Q9BXM0}. Note=Detected in the Schwann cell nucleus prior to the onset of myelination (PubMed:10671475). Detected in Schwann cells at periaxonal myelin membranes. Associated with the cell membrane during myelination (PubMed:9488714). {ECO:0000269|PubMed:10671475, ECO:0000269|PubMed:9488714}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm {ECO:0000269|PubMed:10671475, ECO:0000269|PubMed:9488714}. SUBUNIT: Homodimer (via PDZ domain) (By similarity). Interacts with SCN10A. Found in a complex with SCN10A (By similarity). Interacts with DRP2 (PubMed:22764250). Identified in a dystroglycan complex that contains at least PRX, DRP2, UTRN, DMD and DAG1 (PubMed:11430802). Detected in a complex composed of at least EZR, AHNAK, PPL and PRX (By similarity). Identified in a complex with EZR, AHNAK, BFSP1, BFSP2, ANK2, PLEC, VIM and spectrin (PubMed:21745462). {ECO:0000250|UniProtKB:E1BM58, ECO:0000250|UniProtKB:Q63425, ECO:0000250|UniProtKB:Q9BXM0, ECO:0000269|PubMed:11430802, ECO:0000269|PubMed:21745462, ECO:0000269|PubMed:22764250}. DOMAIN: Has a remarkable domain of repetitive pentameric units sometimes followed by a tripeptide spacer, it may separate two functional basic and acidic domains. {ECO:0000305}.; DOMAIN: The PDZ domain contains the signal for export from the nucleus (By similarity). The N-terminal region including the PDZ domain is required for the formation of Cajal bands on myelinated nerves. {ECO:0000250|UniProtKB:Q9BXM0, ECO:0000269|PubMed:23022068}.; DOMAIN: The Arg/Lys-rich basic domain functions as a tripartite nuclear localization signal. {ECO:0000250|UniProtKB:Q63425}. TISSUE SPECIFICITY: Detected in myelinating Schwann cells in intramuscular nerves in triangularis sterni (PubMed:18205176). Detected in sciatic nerve (PubMed:11430802). Detected in eye lens fiber cells (PubMed:21745462). Isoform 1 is detected in myelinating Schwann cells in sciatic nerve (PubMed:9488714, PubMed:10671475, PubMed:10839370). Isoform 2 is detected in myelinating Schwann cells in sciatic nerve (at protein level) (PubMed:9488714, PubMed:10839370). Detected in sciatic nerve (PubMed:9488714, PubMed:10839370). {ECO:0000269|PubMed:10671475, ECO:0000269|PubMed:10839370, ECO:0000269|PubMed:11430802, ECO:0000269|PubMed:18205176, ECO:0000269|PubMed:21745462, ECO:0000269|PubMed:9488714}. +Q69ZK0 PREX1_MOUSE Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 1 protein (P-Rex1) (PtdIns(3,4,5)-dependent Rac exchanger 1) 1650 184,935 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (5); Erroneous initiation (1); Modified residue (4); Sequence conflict (1) FUNCTION: Functions as a RAC guanine nucleotide exchange factor (GEF), which activates the Rac proteins by exchanging bound GDP for free GTP. Its activity is synergistically activated by phosphatidylinositol 3,4,5-trisphosphate and the beta gamma subunits of heterotrimeric G protein. May function downstream of heterotrimeric G proteins in neutrophils (By similarity). {ECO:0000250, ECO:0000269|PubMed:16243036}. SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell membrane. Note=Mainly cytosolic. Some amount is apparently associated to the plasma membrane (By similarity). {ECO:0000250}. SUBUNIT: Interacts preferentially with RAC2 (PubMed:16243036). Interacts with RAC1 (PubMed:16243036). Interacts with AUTS2 (PubMed:25533347). {ECO:0000269|PubMed:16243036, ECO:0000269|PubMed:25533347}. +Q0VBB0 PRLD2_MOUSE PRELI domain-containing protein 2 177 20,420 Chain (1); Domain (1) +P06879 PRL_MOUSE Prolactin (PRL) 226 25,496 Chain (1); Disulfide bond (3); Modified residue (2); Sequence conflict (1); Signal peptide (1) FUNCTION: Prolactin acts primarily on the mammary gland by promoting lactation. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Interacts with PRLR. {ECO:0000250|UniProtKB:P01236}. +Q91VI7 RINI_MOUSE Ribonuclease inhibitor (Ribonuclease/angiogenin inhibitor 1) 456 49,816 Beta strand (18); Chain (1); Helix (22); Modified residue (2); Repeat (15); Sequence conflict (5) FUNCTION: Ribonuclease inhibitor which inhibits RNASE1, RNASE2 and ANG. May play a role in redox homeostasis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Forms high-affinity heterodimers with RNASE1, ANG and RNASE2. {ECO:0000250}. DOMAIN: The LRR domain forms a horseshoe-shaped structure that interacts tightly with target RNases via a large protein interaction surface on its interior side. {ECO:0000250}. +P04925 PRIO_MOUSE Major prion protein (PrP) (PrP27-30) (PrP33-35C) (CD antigen CD230) 254 27,977 Beta strand (4); Chain (1); Disulfide bond (1); Glycosylation (2); Helix (5); Lipidation (1); Metal binding (12); Modified residue (1); Mutagenesis (2); Natural variant (2); Propeptide (1); Region (3); Repeat (5); Sequence conflict (2); Signal peptide (1); Turn (3) FUNCTION: Its primary physiological function is unclear. May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May promote myelin homeostasis through acting as an agonist for ADGRG6 receptor. May play a role in iron uptake and iron homeostasis. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro) (By similarity). Association with GPC1 (via its heparan sulfate chains) targets PRNP to lipid rafts. Also provides Cu(2+) or ZN(2+) for the ascorbate-mediated GPC1 deaminase degradation of its heparan sulfate side chains (PubMed:12732622, PubMed:16492732, PubMed:19242475, PubMed:19568430). {ECO:0000250|UniProtKB:P04156, ECO:0000269|PubMed:12732622, ECO:0000269|PubMed:16492732, ECO:0000269|PubMed:19242475, ECO:0000269|PubMed:19568430}. PTM: N-glycosylated. {ECO:0000269|PubMed:16492732, ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:19568430}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11571277, ECO:0000269|PubMed:9837873}; Lipid-anchor, GPI-anchor. Golgi apparatus {ECO:0000269|PubMed:11756421}. Note=Targeted to lipid rafts via association with the heparan sulfate chains of GPC1. Colocates, in the presence of Cu(2+), to. vesicles in para- and perinuclear regions, where both proteins undergo internalization. Heparin displaces PRNP from lipid rafts and promotes endocytosis. {ECO:0000269|PubMed:11571277, ECO:0000269|PubMed:12732622, ECO:0000269|PubMed:16923158, ECO:0000269|PubMed:9837873}. SUBUNIT: Monomer and homodimer. Has a tendency to aggregate into amyloid fibrils containing a cross-beta spine, formed by a steric zipper of superposed beta-strands. Soluble oligomers may represent an intermediate stage on the path to fibril formation. Copper binding may promote oligomerization. Interacts with GRB2, APP, ERI3/PRNPIP and SYN1 (PubMed:11571277). Mislocalized cytosolically exposed PrP interacts with MGRN1; this interaction alters MGRN1 subcellular location and causes lysosomal enlargement (By similarity). Interacts with APP. Interacts with KIAA1191 (By similarity). Interacts with ADGRG6 (PubMed:27501152). {ECO:0000250|UniProtKB:P04156, ECO:0000269|PubMed:11571277, ECO:0000269|PubMed:27501152}. DOMAIN: The normal, monomeric form has a mainly alpha-helical structure. The disease-associated, protease-resistant form forms amyloid fibrils containing a cross-beta spine, formed by a steric zipper of superposed beta-strands. Disease mutations may favor intermolecular contacts via short beta strands, and may thereby trigger oligomerization. {ECO:0000250|UniProtKB:P04156}.; DOMAIN: Contains an N-terminal region composed of octamer repeats. At low copper concentrations, the sidechains of His residues from three or four repeats contribute to the binding of a single copper ion. Alternatively, a copper ion can be bound by interaction with the sidechain and backbone amide nitrogen of a single His residue. The observed copper binding stoichiometry suggests that two repeat regions cooperate to stabilize the binding of a single copper ion. At higher copper concentrations, each octamer can bind one copper ion by interactions with the His sidechain and Gly backbone atoms. A mixture of binding types may occur, especially in the case of octamer repeat expansion. Copper binding may stabilize the conformation of this region and may promote oligomerization. {ECO:0000250|UniProtKB:P04156}. TISSUE SPECIFICITY: Highly expressed in the brain, lung, kidney and heart. Expressed at low levels in the liver and spleen. {ECO:0000269|PubMed:16492732, ECO:0000269|PubMed:19568430}. DISEASE: Note=Found in high quantity in the brain of humans and animals infected with degenerative neurological diseases such as kuru, Creutzfeldt-Jakob disease (CJD), Gerstmann-Straussler syndrome (GSS), scrapie, bovine spongiform encephalopathy (BSE), transmissible mink encephalopathy (TME), etc. {ECO:0000305}. +Q6P1E7 PRIPO_MOUSE DNA-directed primase/polymerase protein (EC 2.7.7.-) (Coiled-coil domain-containing protein 111) 537 61,330 Active site (2); Alternative sequence (2); Chain (1); Coiled coil (1); Motif (1); Region (1); Sequence conflict (2) FUNCTION: DNA primase and DNA polymerase able to initiate de novo DNA synthesis using dNTPs. Shows a high capacity to tolerate DNA damage lesions such as 8oxoG and abasic sites in DNA. Involved in translesion synthesis via its primase activity by mediating uninterrupted fork progression after programmed or damage-induced fork arrest and by reinitiating DNA synthesis after dNTP depletion. Required for mitochondrial DNA (mtDNA) synthesis, suggesting it may be involved in DNA tolerance during the replication of mitochondrial DNA. Has non-overlapping function with POLH (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Mitochondrion matrix {ECO:0000250}. Note=Present in the nucleus, but a larger fraction is localized inside mitochondria. {ECO:0000250}. SUBUNIT: Interacts with RPA1. {ECO:0000250}. +Q8CD15 RIOX2_MOUSE Ribosomal oxygenase 2 (Bifunctional lysine-specific demethylase and histidyl-hydroxylase MINA) (EC 1.14.11.-) (Histone lysine demethylase MINA) (MYC-induced nuclear antigen) 465 53,517 Chain (1); Domain (1); Metal binding (3); Modified residue (1); Sequence conflict (5) FUNCTION: Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase. Is involved in the demethylation of trimethylated 'Lys-9' on histone H3 (H3K9me3), leading to an increase in ribosomal RNA expression. Also catalyzes the hydroxylation of 60S ribosomal protein L27a on 'His-39' (By similarity). May play an important role in cell growth and survival. May be involved in ribosome biogenesis, most likely during the assembly process of pre-ribosomal particles. {ECO:0000250, ECO:0000269|PubMed:16533354}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16533354}. Nucleus, nucleolus {ECO:0000269|PubMed:16533354}. TISSUE SPECIFICITY: Predominantly expressed in testis. Expressed at high levels in spleen, thymus, and colon, but barely detectable in brain, skeletal muscle, and seminal vesicle (at protein level). {ECO:0000269|PubMed:16533354}. +Q9QZL0 RIPK3_MOUSE Receptor-interacting serine/threonine-protein kinase 3 (EC 2.7.11.1) (RIP-like protein kinase 3) (Receptor-interacting protein 3) (RIP-3) (mRIP3) 486 53,322 Active site (1); Beta strand (10); Binding site (1); Chain (1); Compositional bias (1); Domain (1); Helix (16); Modified residue (15); Motif (1); Mutagenesis (8); Nucleotide binding (1); Sequence conflict (7); Turn (2) FUNCTION: Essential for necroptosis, a programmed cell death process in response to death-inducing TNF-alpha family members. Upon induction of necrosis, RIPK3 interacts with, and phosphorylates RIPK1 and MLKL to form a necrosis-inducing complex. RIPK3 binds to and enhances the activity of three metabolic enzymes: GLUL, GLUD1, and PYGL. These metabolic enzymes may eventually stimulate the tricarboxylic acid cycle and oxidative phosphorylation, which could result in enhanced ROS production. {ECO:0000269|PubMed:19590578, ECO:0000269|PubMed:24012422, ECO:0000269|PubMed:24019532, ECO:0000269|PubMed:24095729}. PTM: RIPK1 and RIPK3 undergo reciprocal auto- and trans-phosphorylation. Phosphorylation of Ser-204 plays a role in the necroptotic function of RIPK3. Phosphorylation at Ser-232 is required for binding MLKL (PubMed:23612963). Phosphorylation at Thr-187 is important for its kinase activity, interaction with PELI1 and for its ability to mediate TNF-induced necroptosis (By similarity). {ECO:0000250|UniProtKB:Q9Y572, ECO:0000269|PubMed:23612963}.; PTM: Polyubiquitinated with 'Lys-48' and 'Lys-63'-linked chains by BIRC2/c-IAP1 and BIRC3/c-IAP2, leading to activation of NF-kappa-B. Ubiquitinated by STUB1 leading to its subsequent proteasome-dependent degradation. {ECO:0000250|UniProtKB:Q9Y572}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305}. Cell membrane. Mitochondrion {ECO:0000305}. SUBUNIT: Interacts (via RIP homotypic interaction motif) with RIPK1 (via RIP homotypic interaction motif); this interaction induces RIPK1 phosphorylation and formation of a RIPK1-RIPK3 necroptosis-inducing complex. Upon TNF-induced necrosis, the RIPK1-RIPK3 dimer further interacts with PGAM5 and MLKL; the formation of this complex leads to PGAM5 phosphorylation and increase in PGAM5 phosphatase activity (By similarity). Binds TRAF2 and is recruited to the TNFR-1 signaling complex (By similarity). Interacts with MLKL; the interaction is direct (PubMed:24012422). Interacts with PYGL, GLUL and GLUD1; these interactions result in activation of these metabolic enzymes. Interacts with BIRC2/c-IAP1, BIRC3/c-IAP2 and XIAP/BIRC4 (By similarity). Interacts with ARHGEF2 (By similarity). Interacts with ZBP1 (PubMed:19590578). Interacts with PELI1 (via atypical FHA domain) (PubMed:29883609). The phosphorylated form at Thr-187 binds preferentially to PELI1 (By similarity). Interacts with BUB1B, TRAF2 and STUB1 (By similarity). {ECO:0000250|UniProtKB:Q9Y572, ECO:0000269|PubMed:19590578, ECO:0000269|PubMed:24012422, ECO:0000269|PubMed:29883609}.; SUBUNIT: (Microbial infection) Interacts (via RIP homotypic interaction motif) with murid herpesvirus 1 viral inhibitor of RIP activation; this interaction disrupts RIP3-RIP1 interactions characteristic of TNF-alpha induced necroptosis, thereby suppressing this death pathway. {ECO:0000269|PubMed:18442983}. TISSUE SPECIFICITY: Expressed in embryo and in adult spleen, liver, testis, heart, brain and lung. +Q9JJC6 RIPL1_MOUSE RILP-like protein 1 (Rab-interacting lysosomal-like protein 1) 406 47,323 Chain (1); Coiled coil (1); Domain (2); Modified residue (3) FUNCTION: Neuroprotective protein, which acts by sequestring GAPDH in the cytosol and prevent the apoptotic function of GAPDH in the nucleus. Competes with SIAH1 for binding GAPDH. Does not regulate lysosomal morphology and distribution (By similarity). Plays a role in the regulation of cell shape and polarity. Plays a role in cellular protein transport, including protein transport away from primary cilia. {ECO:0000250, ECO:0000269|PubMed:23264467}. PTM: S-nitrosylation is required for the interaction with GAPDH. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Cell projection, cilium {ECO:0000269|PubMed:23264467}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:23264467}. SUBUNIT: Interacts (when S-nitrosylated) with GAPDH. {ECO:0000250}. +P97458 PROP1_MOUSE Homeobox protein prophet of Pit-1 (PROP-1) (Pituitary-specific homeodomain factor) 223 25,025 Chain (1); DNA binding (1); Mutagenesis (2) FUNCTION: Possibly involved in the ontogenesis of pituitary gonadotropes, as well as somatotropes, lactotropes and caudomedial thyrotropes. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. +Q80U16 RIPR2_MOUSE Rho family-interacting cell polarization regulator 2 1078 118,970 Alternative sequence (11); Chain (1); Coiled coil (1); Erroneous initiation (1); Modified residue (4); Mutagenesis (1); Region (1); Sequence conflict (1) FUNCTION: Acts as an inhibitor of the small GTPase RHOA and plays several roles in the regulation of myoblast and hair cell differentiation, lymphocyte T proliferation and neutrophil polarization (PubMed:25588844, PubMed:27269051). Plays a role in fetal mononuclear myoblast differentiation by promoting filopodia and myotube formation (PubMed:17150207). Maintains naive T lymphocytes in a quiescent state and prevents chemokine-induced T lymphocyte responses, such as cell adhesion, polarization and migration (By similarity). Involved also in the regulation of neutrophil polarization, chemotaxis and adhesion (PubMed:25588844). Required for normal development of inner and outer hair cell stereocilia within the cochlea of the inner ear (PubMed:27269051). Plays a role for maintaining the structural organization of the basal domain of stereocilia (PubMed:27269051). Involved in mechanosensory hair cell function (PubMed:27269051). Required for normal hearing (PubMed:27269051). {ECO:0000250|UniProtKB:Q9Y4F9, ECO:0000269|PubMed:17150207, ECO:0000269|PubMed:25588844, ECO:0000269|PubMed:27269051}. PTM: Phosphorylated. Chemokine-induced phosphorylation in neutrophils occurs in a PKC- and AKT-dependent manner, resulting in RIPOR2 interaction with YWHAB and stabilization. Phosphorylated by PKCA, AKT1 and MAPKAPK1A; in vitro. {ECO:0000250|UniProtKB:Q9Y4F9}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y4F9}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9Y4F9}. Cell projection, filopodium {ECO:0000250|UniProtKB:Q9Y4F9}. Cell projection, stereocilium {ECO:0000269|PubMed:27269051}. Cell projection, stereocilium membrane {ECO:0000250|UniProtKB:Q7TP54}. Apical cell membrane {ECO:0000250|UniProtKB:Q7TP54}. Note=Localized in the cytoplasm in cells undergoing mitosis (By similarity). Colocalized with F-actin (By similarity). Accumulates at the leading edge of polarized neutrophils in a chemokine-dependent manner (By similarity). Localized with RHOC within the basal domain of hair cell stereocilia, near the taper region (PubMed:27269051). Detected in punctate pattern forming a circumferential ring at the stereocilia base (PubMed:27269051). Localized to the apical stereocilia of inner and outer hair cells (By similarity). Not detected as a membrane-associated protein in stereocilia (PubMed:27269051). {ECO:0000250|UniProtKB:Q9Y4F9, ECO:0000269|PubMed:27269051}. SUBUNIT: Homooligomer; homooligomerization is regulated by RHOC and leads to the formation of concatemers through the association of N- and C-termini (PubMed:27269051). Interacts (phosphorylated form) with 14-3-3 proteins; these interactions occur during myogenic cell differentiation and also induces T cell proliferation arrest (By similarity). Interacts (phosphorylated form) with HDAC6; this interaction occurs during early myogenic differentiation, prevents HDAC6 to deacetylate tubulin and also induces T cell proliferation arrest (By similarity). Interacts with DYSF; this interaction occurs during early myogenic differentiation (PubMed:24687993). Interacts with MYOF (By similarity). Interacts (via active GTP- or inactive GDP-bound forms) with RHOA; this interaction is direct, blocks the loading of GTP to RHOA and decreases upon chemokine CCL19 stimulation in primary T lymphocytes (PubMed:27269051). Interacts with RHOC (PubMed:27269051). Interacts (via phosphorylated form) with YWHAB; this interaction occurs in a chemokine-dependent manner and does not compete for binding of RIPOR2 with RHOA nor blocks inhibition of RIPOR2-mediated RHOA activity (By similarity). Interacts with YWHAE (By similarity). Interacts with YWHAQ (By similarity). {ECO:0000250|UniProtKB:Q9Y4F9, ECO:0000269|PubMed:24687993, ECO:0000269|PubMed:27269051}. TISSUE SPECIFICITY: Expressed in the cochlea (PubMed:24958875). Expressed in inner hair cells and outer hair cells and Hensen's cells (at protein level) (PubMed:27269051). Expressed in the brain, cerebellum, spinal cord, retina, heart, spleen liver, kidney, bladder, muscle and lung ((PubMed:24958875), PubMed:27269051). Expressed in the cochlea of the inner ear ((PubMed:24958875), PubMed:27269051). {ECO:0000269|PubMed:24958875, ECO:0000269|PubMed:27269051}. +O70169 PRS39_MOUSE Inactive serine protease 39 (Inactive testicular serine protease 1) 367 40,766 Chain (1); Disulfide bond (4); Domain (1); Signal peptide (1) FUNCTION: May play an important role in the sperm/egg interaction; released during the acrosome reaction. {ECO:0000269|PubMed:9588171}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:9588171}. Secreted {ECO:0000269|PubMed:9588171}. TISSUE SPECIFICITY: Expressed in testis. More specifically, abundantly expressed in the haploid round spermatid. {ECO:0000269|PubMed:9588171}. +A1L3T7 RIPR3_MOUSE RIPOR family member 3 938 104,161 Chain (1); Modified residue (6) +Q5M8S2 PRS46_MOUSE Serine protease 46 (EC 3.4.21.-) 314 35,185 Active site (3); Alternative sequence (1); Chain (1); Disulfide bond (4); Domain (1); Frameshift (1); Transmembrane (1) TRANSMEM 293 313 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q06348 PRRX2_MOUSE Paired mesoderm homeobox protein 2 (PRX-2) (Homeobox protein S8) 247 26,427 Chain (1); Compositional bias (1); DNA binding (1); Motif (1) SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-ProRule:PRU00138}. TISSUE SPECIFICITY: In the embryo, expressed in craniofacial mesenchyme, limb, heart, somites and sclerotomes. Absent from central and peripheral nervous systems, splanchnopleure and ectodermal derivatives. +Q7M756 PRS54_MOUSE Inactive serine protease 54 (Plasma kallikrein-like protein 4) 383 42,758 Chain (1); Disulfide bond (3); Domain (1); Glycosylation (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q8BJR6 PRS27_MOUSE Serine protease 27 (EC 3.4.21.-) (Marapsin) (Pancreasin) 328 35,789 Active site (3); Chain (1); Disulfide bond (4); Domain (1); Glycosylation (1); Propeptide (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +Q14B24 PRS57_MOUSE Serine protease 57 (EC 3.4.21.-) (Neutrophil serine protease 4) (NSP4) (Serine protease 1-like protein 1) 284 30,341 Active site (3); Chain (1); Disulfide bond (4); Domain (1); Glycosylation (1); Signal peptide (1) FUNCTION: Serine protease that cleaves preferentially after Arg residues. Can also cleave after citrulline (deimidated arginine) and methylarginine residues. {ECO:0000250|UniProtKB:Q6UWY2}. PTM: After cleavage of the signal peptide, the N-terminus is probably further processed by CTSC. Processing by CTSC is probably required for accumulation in cytoplasmic granules; in the absence of CTSC the protein does not accumulate. {ECO:0000250|UniProtKB:Q6UWY2}.; PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q6UWY2}. SUBCELLULAR LOCATION: Cytoplasmic granule lumen {ECO:0000250|UniProtKB:Q6UWY2}. Secreted {ECO:0000250|UniProtKB:Q6UWY2}. Note=Stored in cytoplasmic granules and secreted as active enzyme in response to stimulation of neutrophils. {ECO:0000250|UniProtKB:Q6UWY2}. +O88685 PRS6A_MOUSE 26S proteasome regulatory subunit 6A (26S proteasome AAA-ATPase subunit RPT5) (Proteasome 26S subunit ATPase 3) (Tat-binding protein 1) (TBP-1) 442 49,549 Chain (1); Modified residue (2); Nucleotide binding (1); Sequence conflict (6) FUNCTION: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. PSMC3 belongs to the heterohexameric ring of AAA (ATPases associated with diverse cellular activities) proteins that unfolds ubiquitinated target proteins that are concurrently translocated into a proteolytic chamber and degraded into peptides. {ECO:0000250|UniProtKB:P17980}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}. Note=Colocalizes with TRIM5 in cytoplasmic bodies. {ECO:0000269|PubMed:22078707}. SUBUNIT: Component of the 19S proteasome regulatory particle complex. The 26S proteasome consists of a 20S core particle (CP) and two 19S regulatory subunits (RP). The regulatory particle is made of a lid composed of 9 subunits, a base containing 6 ATPases including PSMC3 and few additional components. Interacts with PAAF1. {ECO:0000250|UniProtKB:P17980}. +Q8C5R2 PRSR2_MOUSE Proline and serine-rich protein 2 471 50,421 Chain (1); Compositional bias (2); Erroneous initiation (1); Modified residue (9); Sequence conflict (5) +Q8K0G7 PHGR1_MOUSE Proline, histidine and glycine-rich protein 1 91 8,681 Alternative sequence (1); Chain (1); Compositional bias (1); Sequence caution (2) +Q8K0S0 PHYIP_MOUSE Phytanoyl-CoA hydroxylase-interacting protein (Phytanoyl-CoA hydroxylase-associated protein 1) (PAHX-AP1) (PAHXAP1) 330 37,555 Chain (1); Domain (1); Erroneous initiation (1); Glycosylation (2) FUNCTION: Its interaction with PHYH suggests a role in the development of the central system. SUBUNIT: Interacts with PHYH and ADGRB1. {ECO:0000269|PubMed:10686344, ECO:0000269|PubMed:11245925}. TISSUE SPECIFICITY: Highly expressed in the brain. {ECO:0000269|PubMed:10686344}. +Q9QZ09 PHTF1_MOUSE Putative homeodomain transcription factor 1 761 86,779 Chain (1); Modified residue (5); Sequence conflict (3) FUNCTION: May play a role in transcription regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Interacts with FEM1B. {ECO:0000269|PubMed:15601915}. TISSUE SPECIFICITY: Widely expressed with highest levels in testis. {ECO:0000269|PubMed:10729229}. +Q9CWW6 PIN4_MOUSE Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4 (EC 5.2.1.8) (Parvulin-14) (Par14) (Peptidyl-prolyl cis-trans isomerase Pin4) (PPIase Pin4) (Rotamase Pin4) 131 13,815 Chain (1); Domain (1); Modified residue (1); Region (2) FUNCTION: Involved as a ribosomal RNA processing factor in ribosome biogenesis. Binds to tightly bent AT-rich stretches of double-stranded DNA (By similarity). {ECO:0000250}. PTM: Phosphorylated. Phosphorylation occurs both in the nucleus and the cytoplasm. Phosphorylation at Ser-19 does not affect its PPIase activity but is required for nuclear localization, and the dephosphorylation is a prerequisite for the binding to DNA. The unphosphorylated form associates with the pre-rRNP complexes in the nucleus (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Colocalizes in the nucleolus during interphase and on the spindle apparatus during mitosis with NPM1. {ECO:0000250}. SUBUNIT: Found in pre-ribosomal ribonucleoprotein (pre-rRNP) complexes. {ECO:0000269|PubMed:11960984}. +P97474 PITX2_MOUSE Pituitary homeobox 2 (ALL1-responsive protein ARP1) (BRX1 homeoprotein) (Homeobox protein PITX2) (Orthodenticle-like homeobox 2) (Paired-like homeodomain transcription factor 2) (Paired-like homeodomain transcription factor Munc 30) (Solurshin) 317 35,321 Alternative sequence (4); Chain (1); DNA binding (1); Erroneous initiation (1); Modified residue (1); Motif (2); Sequence conflict (2) FUNCTION: Controls cell proliferation in a tissue-specific manner and is involved in morphogenesis. During embryonic development, exerts a role in the expansion of muscle progenitors. May play a role in the proper localization of asymmetric organs such as the heart and stomach. Isoform Ptx2c is involved in left-right asymmetry the developing embryo. {ECO:0000269|PubMed:20019746}. PTM: Phosphorylation at Thr-90 impairs its association with the CCND1 mRNA-stabilizing complex thus shortening the half-life of CCND1. {ECO:0000269|PubMed:20019746}. SUBCELLULAR LOCATION: Nucleus. TISSUE SPECIFICITY: In day-11 embryos, expressed in the periocular mesenchyme, maxillary and mandibular epithelia, umbilicus, Rathke pouch, vitelline vessels and limb mesenchyme. In adult tissues, expressed in pituitary gland, brain, kidney, eye, lung, testis and tongue. +Q00286 PIT1_MOUSE Pituitary-specific positive transcription factor 1 (PIT-1) (Growth hormone factor 1) (GHF-1) 291 32,885 Alternative sequence (2); Chain (1); DNA binding (1); Domain (1); Natural variant (1) FUNCTION: Transcription factor involved in the specification of the lactotrope, somatotrope, and thyrotrope phenotypes in the developing anterior pituitary. Activates growth hormone and prolactin genes. Specifically binds to the consensus sequence 5'-TAAAT-3'. {ECO:0000250|UniProtKB:P28069}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P28069}. SUBUNIT: Interacts with PITX1. Interacts with LHX3. Interacts with ELK1. {ECO:0000250|UniProtKB:P28069}. DISEASE: Note=Defects in Pou1f1 are the cause of the dwarf (dw) phenotype which interrupts the normal development of the anterior pituitary gland, resulting in the loss of expression of growth hormone, prolactin and thyroid-stimulating hormone, and hypoplasia of their respective cell types. {ECO:0000269|PubMed:1977085}. +Q8C115 PKHH2_MOUSE Pleckstrin homology domain-containing family H member 2 1491 167,733 Alternative sequence (3); Chain (1); Coiled coil (1); Compositional bias (3); Domain (4); Erroneous initiation (1); Sequence conflict (3) FUNCTION: In the kidney glomerulus may play a role in linking podocyte foot processes to the glomerular basement membrane. May be involved in stabilization of F-actin by attenuating its depolymerization. Can recruit TGFB1I1 from focal adhesions to podocyte lamellipodia. {ECO:0000269|PubMed:22832517}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17251388}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Note=Localizes to the slit diaphragm and foot process of podocytes. Localization to peripheral regions of lamellipodia seems to be dependent on PI3K (By similarity). {ECO:0000250}. SUBUNIT: Self-associates. Interacts with TGFB1I1. {ECO:0000269|PubMed:22832517}. TISSUE SPECIFICITY: Expressed in the kidney and testis. Expressed in the kidney exclusively by glomerular podocytes. {ECO:0000269|PubMed:17251388}. +Q8VC98 PKHA4_MOUSE Pleckstrin homology domain-containing family A member 4 (PH domain-containing family A member 4) (Phosphoinositol 3-phosphate-binding protein 1) (PEPP-1) 588 64,839 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (1); Modified residue (2); Sequence conflict (1) FUNCTION: Binds specifically to phosphatidylinositol 3-phosphate (PtdIns3P), but not to other phosphoinositides. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. +Q7TQG1 PKHA6_MOUSE Pleckstrin homology domain-containing family A member 6 (PH domain-containing family A member 6) (Phosphoinositol 3-phosphate-binding protein 3) (PEPP-3) 1173 131,427 Chain (1); Compositional bias (1); Domain (1); Modified residue (24) +Q9QZC7 PKHB2_MOUSE Pleckstrin homology domain-containing family B member 2 (PH domain-containing family B member 2) (Evectin-2) 221 24,574 Alternative sequence (2); Beta strand (7); Binding site (1); Chain (1); Domain (1); Helix (2); Sequence conflict (2); Turn (2) FUNCTION: Involved in retrograde transport of recycling endosomes. {ECO:0000250}. SUBCELLULAR LOCATION: Recycling endosome membrane {ECO:0000250}; Peripheral membrane protein. Note=Specifically detected in tubulovesicular structures, and colocalizes with TFNR. {ECO:0000250}. DOMAIN: The PH domain specifically binds phosphatidylserine, which is enriched in recycling endosome membranes, it doesn't recognize PIPs. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in brain, retina, heart and kidney. Detected at lower levels in lung, muscle and nerve. {ECO:0000269|PubMed:10200314}. +Q3TB82 PKHF1_MOUSE Pleckstrin homology domain-containing family F member 1 (PH domain-containing family F member 1) (Lysosome-associated apoptosis-inducing protein containing PH and FYVE domains) 279 31,158 Chain (1); Domain (1); Sequence conflict (3); Zinc finger (1) FUNCTION: May induce apoptosis through the lysosomal-mitochondrial pathway. Translocates to the lysosome initiating the permeabilization of lysosomal membrane (LMP) and resulting in the release of CTSD and CTSL to the cytoplasm. Triggers the caspase-independent apoptosis by altering mitochondrial membrane permeabilization (MMP) resulting in the release of PDCD8 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16188880}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16188880}. Lysosome {ECO:0000269|PubMed:16188880}. Note=Translocates to lysosome during apoptosis. DOMAIN: PH and FYVE-type zinc finger domains are required for lysosomal location. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:16188880}. +Q8BTI9 PK3CB_MOUSE Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform (PI3-kinase subunit beta) (PI3K-beta) (PI3Kbeta) (PtdIns-3-kinase subunit beta) (EC 2.7.1.153) (Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit beta) (PtdIns-3-kinase subunit p110-beta) (p110beta) 1064 121,711 Beta strand (35); Chain (1); Domain (5); Helix (47); Modified residue (2); Motif (1); Sequence conflict (1); Turn (10) Phospholipid metabolism; phosphatidylinositol phosphate biosynthesis. FUNCTION: Phosphoinositide-3-kinase (PI3K) that phosphorylates PtdIns (Phosphatidylinositol), PtdIns4P (Phosphatidylinositol 4-phosphate) and PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Involved in the activation of AKT1 upon stimulation by G-protein coupled receptors (GPCRs) ligands such as CXCL12, sphingosine 1-phosphate, and lysophosphatidic acid. May also act downstream receptor tyrosine kinases. Required in different signaling pathways for stable platelet adhesion and aggregation. Plays a role in platelet activation signaling triggered by GPCRs, alpha-IIb/beta-3 integrins (ITGA2B/ ITGB3) and ITAM (immunoreceptor tyrosine-based activation motif)-bearing receptors such as GP6. Regulates the strength of adhesion of ITGA2B/ ITGB3 activated receptors necessary for the cellular transmission of contractile forces. Required for platelet aggregation induced by F2 (thrombin) and thromboxane A2 (TXA2). Has a role in cell survival. May have a role in cell migration. Involved in the early stage of autophagosome formation. Modulates the intracellular level of PtdIns3P (Phosphatidylinositol 3-phosphate) and activates PIK3C3 kinase activity. May act as a scaffold, independently of its lipid kinase activity to positively regulate autophagy. May have a role in insulin signaling as scaffolding protein in which the lipid kinase activity is not required. May have a kinase-independent function in regulating cell proliferation and in clathrin-mediated endocytosis. Mediator of oncogenic signal in cell lines lacking PTEN. The lipid kinase activity is necessary for its role in oncogenic transformation. Required for the growth of ERBB2 and RAS driven tumors. {ECO:0000269|PubMed:18544649, ECO:0000269|PubMed:18594509, ECO:0000269|PubMed:19515725, ECO:0000269|PubMed:19940148, ECO:0000269|PubMed:20065293, ECO:0000269|PubMed:21059846}. PTM: Phosphorylation at Ser-1064 down-regulates lipid kinase activity. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Interaction with PIK3R2 is required for nuclear localization and export. SUBUNIT: Heterodimer of a catalytic subunit PIK3CB and a p85 regulatory subunit (PIK3R1, PIK3R2 or PIK3R3). Interaction with PIK3R2 is required for nuclear localization and nuclear export (By similarity). Part of a complex with PIK3R1 and PTEN (By similarity). Binding to PTEN may antagonize the lipid kinase activity under normal growth conditions (By similarity). Part of a complex involved in autophagosome formation composed of PIK3C3 and PIK3R4. Interacts with BECN1, ATG14 and RAB5A. {ECO:0000250, ECO:0000269|PubMed:21059846}. DOMAIN: The inhibitory interactions with PIK3R1 are mediated by the PI3K-ABD domain and the C2 PI3K-type domain with the iSH2 (inter-SH2) region of PIK3R1; the C2 PI3K-type domain, the PI3K helical domain, and the PI3K/PI4K kinase domain with the nSH2 (N-terminal SH2) region of PIK3R1; and the PI3K/PI4K kinase domain with the cSH2 (C-terminal SH2) region of PIK3R1. The inhibitory interaction between the PI3K-ABD domain and the C2 PI3K-type domain with the iSH2 (inter-SH2) region of PIK3R1 is weak. The nuclear localization signal (NLS) is required for its function in cell survival (By similarity). {ECO:0000250}. +Q9Z280 PLD1_MOUSE Phospholipase D1 (PLD 1) (mPLD1) (EC 3.1.4.4) (Choline phosphatase 1) (Phosphatidylcholine-hydrolyzing phospholipase D1) 1074 123,969 Alternative sequence (1); Chain (1); Domain (4); Lipidation (2); Modified residue (3); Region (1); Sequence conflict (7) FUNCTION: Implicated as a critical step in numerous cellular pathways, including signal transduction, membrane trafficking, and the regulation of mitosis. May be involved in the regulation of perinuclear intravesicular membrane traffic. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:9395408}. Endoplasmic reticulum membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Golgi apparatus membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Late endosome membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. SUBUNIT: Interacts with PIP5K1B. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in kidney, lung, and at a much lower levels, in brain, liver, heart, testis and spleen. DISEASE: Note=Defects in Pld1 may result in coa which is associated with coat color dilution and white spotting. It is also associated with platelet-storage pool deficiency characterized by decreased levels in serotonin and dense granules. +Q8CGN5 PLIN1_MOUSE Perilipin-1 (Lipid droplet-associated protein) (Perilipin A) 517 55,596 Alternative sequence (6); Chain (1); Compositional bias (1); Modified residue (19); Region (1); Sequence conflict (2) FUNCTION: Modulator of adipocyte lipid metabolism. Coats lipid storage droplets to protect them from breakdown by hormone-sensitive lipase (HSL). Its absence may result in leanness (By similarity). Plays a role in unilocular lipid droplet formation by activating CIDEC. Their interaction promotes lipid droplet enlargement and directional net neutral lipid transfer. May modulate lipolysis and triglyceride levels. {ECO:0000250, ECO:0000269|PubMed:23481402}. PTM: Major cAMP-dependent protein kinase-substrate in adipocytes, also dephosphorylated by PP1. When phosphorylated, may be maximally sensitive to HSL and when unphosphorylated, may play a role in the inhibition of lipolysis, by acting as a barrier in lipid droplet (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:O60240}. Lipid droplet {ECO:0000269|PubMed:23481402, ECO:0000269|PubMed:24945349}. Note=Lipid droplet surface-associated. {ECO:0000250|UniProtKB:O60240}. SUBUNIT: Interacts with ABHD5. Interacts with CIDEC. {ECO:0000269|PubMed:15292255, ECO:0000269|PubMed:23481402}. +Q8K4X7 PLCD_MOUSE 1-acyl-sn-glycerol-3-phosphate acyltransferase delta (EC 2.3.1.51) (1-acylglycerol-3-phosphate O-acyltransferase 4) (1-AGP acyltransferase 4) (1-AGPAT 4) (Lysophosphatidic acid acyltransferase delta) (LPAAT-delta) 378 43,810 Chain (1); Motif (1); Transmembrane (4) TRANSMEM 11 31 Helical. {ECO:0000255}.; TRANSMEM 125 145 Helical. {ECO:0000255}.; TRANSMEM 311 331 Helical. {ECO:0000255}.; TRANSMEM 338 358 Helical. {ECO:0000255}. Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3. FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone. {ECO:0000269|PubMed:15367102}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. DOMAIN: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate. {ECO:0000250}. TISSUE SPECIFICITY: Expressed at a high levels in the brain, at intermediate or low levels in skeletal muscles, gut, kidney, spleen and lung. Barely detectable in heart and liver. {ECO:0000269|PubMed:15367102}. +Q8VE85 PLD3A_MOUSE PRELI domain containing protein 3A (Protein slowmo homolog 1) 172 19,026 Chain (1); Domain (1); Site (2) FUNCTION: In vitro, the TRIAP1:PRELID3A complex mediates the transfer of phosphatidic acid (PA) between liposomes and probably functions as a PA transporter across the mitochondrion intermembrane space. Phosphatidic acid import is required for cardiolipin (CL) synthesis in the mitochondrial inner membrane. {ECO:0000250|UniProtKB:Q96N28}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q96N28}. SUBUNIT: Interacts with TRIAP1. {ECO:0000250|UniProtKB:Q96N28}. +Q9D7R2 PMEPA_MOUSE Protein TMEPAI (NEDD4 WW domain-binding protein 4) (Prostate transmembrane protein androgen induced 1) (Transmembrane prostate androgen-induced protein) 260 28,716 Chain (1); Motif (3); Mutagenesis (2); Topological domain (2); Transmembrane (1) TRANSMEM 21 43 Helical. {ECO:0000255}. TOPO_DOM 1 20 Lumenal. {ECO:0000255}.; TOPO_DOM 44 260 Cytoplasmic. {ECO:0000255}. FUNCTION: Functions as a negative regulator of TGF-beta signaling and thereby probably plays a role in cell proliferation, differentiation, apoptosis, motility, extracellular matrix production and immunosuppression. In the canonical TGF-beta pathway, ZFYVE9/SARA recruits the intracellular signal transducer and transcriptional modulators SMAD2 and SMAD3 to the TGF-beta receptor. Phosphorylated by the receptor, SMAD2 and SMAD3 then form a heteromeric complex with SMAD4 that translocates to the nucleus to regulate transcription. Through interaction with SMAD2 and SMAD3, LDLRAD4 may compete with ZFYVE9 and SMAD4 and prevent propagation of the intracellular signal (PubMed:20129061). Also involved in down-regulation of the androgen receptor (AR), enhancing ubiquitination and proteasome-mediated degradation of AR, probably by recruiting NEDD4. {ECO:0000269|PubMed:20129061}. SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with AR. Interacts with LDLRAD4. Interacts (via the SMAD interaction motif) with SMAD2 and SMAD3 (By similarity). Interacts with NEDD4 (via PPxY motifs). {ECO:0000250, ECO:0000269|PubMed:11042109}. DOMAIN: The PPxY motifs mediate interaction with NEDD4. {ECO:0000269|PubMed:11042109}.; DOMAIN: The SMAD interaction motif is required for interaction with SMAD2 and SMAD3 and the negative regulation of TGF-beta signaling. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain, heart, kidney, bladder, ovary and adrenal gland. {ECO:0000269|PubMed:24627487}. +Q3UH93 PLXD1_MOUSE Plexin-D1 1925 211,608 Beta strand (15); Chain (1); Disulfide bond (9); Domain (4); Glycosylation (5); Helix (27); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (7) TRANSMEM 1272 1292 Helical. {ECO:0000255}. TOPO_DOM 49 1271 Extracellular. {ECO:0000255}.; TOPO_DOM 1293 1925 Cytoplasmic. {ECO:0000255}. FUNCTION: Cell surface receptor for SEMA4A and for class 3 semaphorins, such as SEMA3A, SEMA3C and SEMA3E. Plays an important role in cell-cell signaling, and in regulating the migration of a wide spectrum of cell types. Regulates the migration of thymocytes in the medulla. Regulates endothelial cell migration. Plays an important role in ensuring the specificity of synapse formation. Mediates anti-angiogenic signaling in response to SEMA3E. Required for normal development of the heart and vasculature. {ECO:0000269|PubMed:15239958, ECO:0000269|PubMed:17318185, ECO:0000269|PubMed:18992737, ECO:0000269|PubMed:19027330, ECO:0000269|PubMed:19421194, ECO:0000269|PubMed:22179111}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17318185, ECO:0000269|PubMed:19027330}; Single-pass membrane protein {ECO:0000269|PubMed:17318185, ECO:0000269|PubMed:19027330}. Cell projection, lamellipodium membrane {ECO:0000250|UniProtKB:Q9Y4D7}. SUBUNIT: Interacts with NRP1 and SEMA4A (PubMed:15239958, PubMed:17318185). Interacts with SH3BP1; they dissociate upon SEMA3E binding to PLXND1 allowing SH3BP1 to transduce downstream signal through RAC1 inactivation (By similarity). {ECO:0000250|UniProtKB:Q9Y4D7, ECO:0000269|PubMed:15239958, ECO:0000269|PubMed:17318185}. TISSUE SPECIFICITY: Detected in embryonic heart and vascular endothelium, brain, dorsal root ganglia, adrenal gland, lung mesenchyme, small intestine and in the ossification centers of vertebral bodies. {ECO:0000269|PubMed:18992737}. +Q8K4L4 POF1B_MOUSE Protein POF1B 587 67,785 Chain (1); Coiled coil (1); Sequence conflict (1) FUNCTION: Plays a key role in the organization of epithelial monolayers by regulating the actin cytoskeleton. May be involved in ovary development (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000250}. SUBUNIT: Interacts with nonmuscle actin. {ECO:0000250}. TISSUE SPECIFICITY: Expression absent in adult ovary. {ECO:0000269|PubMed:15459172}. +P10400 POL1_MOUSE Retrovirus-related Pol polyprotein [Includes: Reverse transcriptase (EC 2.7.7.49); Endonuclease] (Fragment) 120 13,302 Chain (1); Non-terminal residue (1) +Q9CQT5 POMP_MOUSE Proteasome maturation protein (Proteassemblin) (Protein UMP1 homolog) (mUMP1) 141 15,766 Chain (1); Cross-link (1); Sequence conflict (2) FUNCTION: Molecular chaperone essential for the assembly of standard proteasomes and immunoproteasomes. Degraded after completion of proteasome maturation (By similarity). Mediates the association of 20S preproteasome with the endoplasmic reticulum (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Nucleus {ECO:0000250}. Microsome membrane {ECO:0000250}. SUBUNIT: Constituent of preproteasomes, but not of mature 20S proteasomes. Within the preproteasome, may directly interact with PSMB1/beta6, PSMB4/beta7, PSMB5/beta5, PSMB6/beta1 and PSMB9/beta1i. Interaction with PSMB8/beta5i is controversial. Forms tetramers (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10891394}. +Q9JJJ7 PORCN_MOUSE Protein-serine O-palmitoleoyltransferase porcupine (mPORC) (EC 2.3.1.-) 461 52,508 Active site (1); Alternative sequence (5); Chain (1); Mutagenesis (13); Topological domain (9); Transmembrane (8) TRANSMEM 18 38 Helical. {ECO:0000255}.; TRANSMEM 67 87 Helical. {ECO:0000255}.; TRANSMEM 96 116 Helical. {ECO:0000255}.; TRANSMEM 153 173 Helical. {ECO:0000255}.; TRANSMEM 199 219 Helical. {ECO:0000255}.; TRANSMEM 253 273 Helical. {ECO:0000255}.; TRANSMEM 338 358 Helical. {ECO:0000255}.; TRANSMEM 397 417 Helical. {ECO:0000255}. TOPO_DOM 1 17 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 39 66 Extracellular. {ECO:0000255}.; TOPO_DOM 88 95 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 117 152 Extracellular. {ECO:0000255}.; TOPO_DOM 174 198 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 220 252 Extracellular. {ECO:0000255}.; TOPO_DOM 274 337 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 359 396 Extracellular. {ECO:0000255}.; TOPO_DOM 418 461 Cytoplasmic. {ECO:0000255}. FUNCTION: Protein-serine O-palmitoleoyltransferase that acts as a key regulator of the Wnt signaling pathway by mediating the attachment of palmitoleate, a 16-carbon monounsaturated fatty acid (C16:1), to Wnt proteins. Serine palmitoleylation of WNT proteins is required for efficient binding to frizzled receptors. {ECO:0000269|PubMed:10866835, ECO:0000269|PubMed:17141155, ECO:0000269|PubMed:22046319, ECO:0000269|PubMed:24055053, ECO:0000269|PubMed:24798332}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10866835, ECO:0000269|PubMed:24798332}; Multi-pass membrane protein {ECO:0000269|PubMed:10866835}. SUBUNIT: Interacts with WNT1, WNT3, WNT3A, WNT4, WNT5A, WNT5B, WNT6, WNT7A and WNT7B. {ECO:0000269|PubMed:10866835, ECO:0000269|PubMed:24798332}. TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver, lung, muscle, spleen and testis. Isoform 4 is strongly expressed in kidney, liver, lung, spleen and testis. Isoform 1 is strongly expressed in brain, heart and muscle and poorly in kidney, liver, lung, spleen and testis. {ECO:0000269|PubMed:10866835}. +Q8BVM9 PH11A_MOUSE PHD finger protein 11A (PHD finger protein 11) (PHD finger protein 11-like) 293 32,673 Chain (1); Zinc finger (2) SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +Q8BYB9 PGLT1_MOUSE Protein O-glucosyltransferase 1 (EC 2.4.1.-) (CAP10-like 46 kDa protein) (KTEL motif-containing protein 1) (O-glucosyltransferase Rumi homolog) (Rumi) (Protein O-xylosyltransferase POGLUT1) (EC 2.4.2.26) (Wing-shaped neural plate protein) (Wsnp) 392 46,379 Active site (1); Binding site (3); Chain (1); Disulfide bond (4); Glycosylation (3); Motif (1); Mutagenesis (1); Region (3); Sequence conflict (1); Signal peptide (1); Site (2) Protein modification; protein glycosylation. FUNCTION: Dual specificity glycosyltransferase that catalyzes the transfer of glucose and xylose from UDP-glucose and UDP-xylose, respectively, to a serine residue found in the consensus sequence of C-X-S-X-P-C (PubMed:21949356, PubMed:26496195). Specifically targets extracellular EGF repeats of protein such as CRB2, F7, F9 and NOTCH2 (PubMed:21949356, PubMed:26496195). Acts as a positive regulator of Notch signaling by mediating O-glucosylation of Notch, leading to regulate muscle development (By similarity). Notch glucosylation does not affect Notch ligand binding (By similarity). Required during early development to promote gastrulation: acts by mediating O-glucosylation of CRB2, which is required for CRB2 localization to the cell membrane (PubMed:26496195). {ECO:0000250|UniProtKB:Q8NBL1, ECO:0000269|PubMed:21949356, ECO:0000269|PubMed:26496195}. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:Q8NBL1}. TISSUE SPECIFICITY: Widely expressed in newborn and adult tissues (at protein level). {ECO:0000269|PubMed:21490058, ECO:0000269|PubMed:26496195}. +Q9Z1B8 PHF1_MOUSE PHD finger protein 1 (Protein PHF1) (Polycomb-like protein 1) (mPCl1) (T-complex testis-expressed 3) 559 61,140 Beta strand (15); Chain (1); Domain (1); Helix (12); Sequence conflict (5); Turn (9); Zinc finger (2) FUNCTION: Polycomb group (PcG) that specifically binds histone H3 trimethylated at 'Lys-36' (H3K36me3) and recruits the PRC2 complex. Involved in DNA damage response and is recruited at double-strand breaks (DSBs). Acts by binding to H3K36me3, a mark for transcriptional activation, and recruiting the PRC2 complex: it is however unclear whether recruitment of the PRC2 complex to H3K36me3 leads to enhance or inhibit H3K27me3 methylation mediated by the PRC2 complex. According to some reports, PRC2 recruitment by PHF1 promotes H3K27me3 and subsequent gene silencing by inducing spreading of PRC2 and H3K27me3 into H3K36me3 loci (PubMed:18086877). According to other reports, PHF1 recruits the PRC2 complex at double-strand breaks (DSBs) and inhibits the activity of PRC2. Regulates p53/TP53 stability and prolonges its turnover: may act by specifically binding to a methylated from of p53/TP53. {ECO:0000269|PubMed:18086877}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18086877}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Note=Localizes specifically to the promoters of numerous target genes. Localizes to double-strand breaks (DSBs) sites following DNA damage. Colocalizes with NEK6 in the centrosome (By similarity). {ECO:0000250}. SUBUNIT: Associated component of the PRC2 complex. Interacts with p53/TP53 (By similarity). Interacts with CHMP1. {ECO:0000250, ECO:0000269|PubMed:11559747}. DOMAIN: The Tudor domain recognizes and binds H3K36me3. {ECO:0000269|PubMed:23104054}. TISSUE SPECIFICITY: Testis-specific. +Q8K1N2 PHLB2_MOUSE Pleckstrin homology-like domain family B member 2 (Protein LL5-beta) 1249 141,486 Alternative sequence (1); Chain (1); Coiled coil (3); Compositional bias (1); Domain (1); Modified residue (20); Sequence conflict (7) FUNCTION: Seems to be involved in the assembly of the postsynaptic apparatus. May play a role in acetyl-choline receptor (AChR) aggregation in the postsynaptic membrane. {ECO:0000269|PubMed:15851520}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Translocates to the plasma membrane at high levels of PtdIns(3,4,5)P3. At low levels of PtdIns(3,4,5)P3 is translocated to vesicular compartments (By similarity). {ECO:0000250}. SUBUNIT: Interacts with FLNC. {ECO:0000250}. DOMAIN: The PH domain mediates the binding to phosphoinositides. {ECO:0000250}. TISSUE SPECIFICITY: Expressed at postsynaptic membranes of skeletal neuromuscular junctions (at protein level). {ECO:0000269|PubMed:15851520}. +P83870 PHF5A_MOUSE PHD finger-like domain-containing protein 5A (PHD finger-like domain protein 5A) (Splicing factor 3B-associated 14 kDa protein) (SF3b14b) 110 12,405 Chain (1); Initiator methionine (1); Metal binding (12); Modified residue (3); Region (2); Site (2) FUNCTION: Involved with the PAF1 complex (PAF1C) in transcriptional elongation by RNA polymerase II, and in regulation of development and maintenance of embryonic stem cell (ESC) pluripotency. Required for maintenance of ESCs self-renewal and cellular reprogramming of stem cells. Maintains pluripotency by recruiting and stabilizing PAF1C on pluripotency genes loci, and by regulating the expression of the pluripotency genes. Regulates the deposition of elongation-associated histone modifications, including dimethylated histone H3 'Lys-79' (H3K79me2) and trimethylated histone H3 'Lys-36' (H3K36me3), on PAF1C targets, self-renewal and pluripotency genes. Regulates RNA polymerase II promoter-proximal pause release of the PAF1C targets and self-renewal genes, and the levels of elongating ('Ser-2' phosphorylated) RNA polymerase II in their gene bodies. Regulates muscle specification in adult stem cells by stabilizing PAF1C in chromatin to promote myogenic differentiation (PubMed:27749823). Involved in pre-mRNA splicing as a component of the splicing factor SF3B complex. SF3B complex is required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA (By similarity). Acts as a transcriptional regulator by binding to the GJA1/Cx43 promoter and enhancing its up-regulation by ESR1/ER-alpha (By similarity). {ECO:0000250|UniProtKB:P83871, ECO:0000250|UniProtKB:Q7RTV0, ECO:0000269|PubMed:27749823}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12054543, ECO:0000269|PubMed:18758164, ECO:0000269|PubMed:27749823}. Nucleus speckle {ECO:0000269|PubMed:18758164}. SUBUNIT: Interacts (via N-terminus) with U2AF1 and SRSF5; acts to bridge the two. Interacts (via C-terminus) with EP400 and DDX1; acts to bridge the two (PubMed:18758164). Component of splicing factor SF3B complex which is composed of at least eight subunits; SF3B1, SF3B2, SF3B3, SF3B4, SF3B5, SF3B6, PHF5A and DDX42. Within the SF3B complex interacts directly with SF3B1 and SF3B3. The SF3B complex composed of SF3B1, SF3B2, SF3B3, SF3B4, SF3B5, SF3B6 and PHF5A interacts with U2AF2. SF3B associates with the splicing factor SF3A and a 12S RNA unit to form the U2 small nuclear ribonucleoproteins complex (U2 snRNP). Component of the U11/U12 snRNPs that are part of the U12-type spliceosome (By similarity). Interacts with the PAF1 complex (PAF1C) composed of CDC73, PAF1, LEO1, CTR9, RTF1 and WDR61. Within the PAF1C interacts directly with CDC73 and WDR61. Interacts with RNA polymerase II (PubMed:27749823). {ECO:0000250|UniProtKB:Q7RTV0, ECO:0000269|PubMed:18758164, ECO:0000269|PubMed:27749823}. TISSUE SPECIFICITY: Expressed in primary spermatocytes (at protein level) (PubMed:18758164). Ubiquitously expressed in pre- and postnatal tissues (PubMed:12054543). Highly expressed in pluripotent embryonic stem cells (ESCs) (at protein level) and induced pluripotent stem cells (iPSCs) (PubMed:27749823). {ECO:0000269|PubMed:12054543, ECO:0000269|PubMed:18758164, ECO:0000269|PubMed:27749823}. +Q5SPL2 PHF12_MOUSE PHD finger protein 12 (PHD factor 1) (Pf1) 1003 109,509 Alternative sequence (2); Chain (1); Compositional bias (2); Cross-link (5); Domain (1); Erroneous initiation (1); Modified residue (6); Zinc finger (2) FUNCTION: Acts as a transcriptional repressor. Involved in recruitment of functional SIN3A complexes to DNA. Represses transcription at least in part through the activity of an associated histone deacetylase (HDAC). May also repress transcription in a SIN3A-independent manner through recruitment of functional AES complexes to DNA (By similarity). {ECO:0000250|UniProtKB:Q96QT6}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Interacts with SIN3A in a complex composed of HDAC1, SAP30 and SIN3A. Interacts with AES (By similarity). {ECO:0000250|UniProtKB:Q96QT6}. TISSUE SPECIFICITY: Expressed mainly in heart, brain, lung, liver and testis. {ECO:0000269|PubMed:11390640}. +P06803 PIM1_MOUSE Serine/threonine-protein kinase pim-1 (EC 2.7.11.1) 313 35,451 Active site (1); Alternative sequence (1); Binding site (3); Chain (1); Domain (1); Modified residue (4); Mutagenesis (1); Nucleotide binding (1); Sequence conflict (1) FUNCTION: Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation and thus providing a selective advantage in tumorigenesis. Exerts its oncogenic activity through: the regulation of MYC transcriptional activity, the regulation of cell cycle progression and by phosphorylation and inhibition of proapoptotic proteins (BAD, MAP3K5, FOXO3). Phosphorylation of MYC leads to an increase of MYC protein stability and thereby an increase of transcriptional activity. The stabilization of MYC exerted by PIM1 might explain partly the strong synergism between these two oncogenes in tumorigenesis. Mediates survival signaling through phosphorylation of BAD, which induces release of the anti-apoptotic protein Bcl-X(L)/BCL2L1. Phosphorylation of MAP3K5, an other proapoptotic protein, by PIM1, significantly decreases MAP3K5 kinase activity and inhibits MAP3K5-mediated phosphorylation of JNK and JNK/p38MAPK subsequently reducing caspase-3 activation and cell apoptosis. Stimulates cell cycle progression at the G1-S and G2-M transitions by phosphorylation of CDC25A and CDC25C. Phosphorylation of CDKN1A, a regulator of cell cycle progression at G1, results in the relocation of CDKN1A to the cytoplasm and enhanced CDKN1A protein stability. Promote cell cycle progression and tumorigenesis by down-regulating expression of a regulator of cell cycle progression, CDKN1B, at both transcriptional and post-translational levels. Phosphorylation of CDKN1B,induces 14-3-3 binding, nuclear export and proteasome-dependent degradation. May affect the structure or silencing of chromatin by phosphorylating HP1 gamma/CBX3. Acts also as a regulator of homing and migration of bone marrow cells involving functional interaction with the CXCL12-CXCR4 signaling axis (By similarity). {ECO:0000250|UniProtKB:P11309, ECO:0000269|PubMed:15199164, ECO:0000269|PubMed:15280015, ECO:0000269|PubMed:1825810, ECO:0000269|PubMed:18438430, ECO:0000269|PubMed:19687226}. PTM: Autophosphorylated on both serine/threonine and tyrosine residues. Phosphorylated. Interaction with PPP2CA promotes dephosphorylation (By similarity). {ECO:0000250|UniProtKB:P11309}.; PTM: Ubiquitinated, leading to proteasomal degradation. {ECO:0000250|UniProtKB:P11309}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1825810}. Nucleus {ECO:0000269|PubMed:1825810}. Cell membrane {ECO:0000269|PubMed:1825810}. Note=Mainly located in the cytoplasm. SUBUNIT: Isoform 1 is isolated as a monomer whereas isoform 2 complexes with other proteins (PubMed:1825810). Isoform 2, but not isoform 1, binds BMX (By similarity). Binds to RP9 (PubMed:10931201). Interacts with CDKN1B and FOXO3 (By similarity). Interacts with BAD (PubMed:15280015). Interacts with PPP2CA; this interaction promotes dephosphorylation of PIM1, ubiquitination and proteasomal degradation (By similarity). Interacts with HSP90AA1, this interaction stabilizes PIM1 protein levels (By similarity). Interacts (ubiquitinated form) with HSP70 and promotes its proteosomal degradation (By similarity). Interacts with CDKN1A (By similarity). Interacts with CDC25C (By similarity). Interacts (via N-terminal 96 residues) with CDC25A (By similarity). Interacts with MAP3K5 (By similarity). Interacts with MYC (PubMed:18438430). Interacts with CBX3 (By similarity). {ECO:0000250|UniProtKB:P11309, ECO:0000269|PubMed:10931201, ECO:0000269|PubMed:15280015, ECO:0000269|PubMed:1825810, ECO:0000269|PubMed:18438430}. DISEASE: Note=Frequently activated by provirus insertion in murine leukemia virus-induced T-cell lymphomas. +Q64374 RGN_MOUSE Regucalcin (RC) (Gluconolactonase) (GNL) (EC 3.1.1.17) (Senescence marker protein 30) (SMP-30) 299 33,407 Active site (1); Beta strand (23); Binding site (3); Chain (1); Helix (4); Metal binding (3); Modified residue (3); Sequence conflict (2); Turn (8) Cofactor biosynthesis; L-ascorbate biosynthesis via UDP-alpha-D-glucuronate pathway; L-ascorbate from UDP-alpha-D-glucuronate: step 3/4. FUNCTION: Gluconolactonase with low activity towards other sugar lactones, including gulonolactone and galactonolactone. Catalyzes a key step in ascorbic acid (vitamin C) biosynthesis. Can also hydrolyze diisopropyl phosphorofluoridate and phenylacetate (in vitro). Calcium-binding protein. Modulates Ca(2+) signaling, and Ca(2+)-dependent cellular processes and enzyme activities (By similarity). {ECO:0000250, ECO:0000269|PubMed:16585534, ECO:0000269|PubMed:23349732}. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Monomer. {ECO:0000269|PubMed:23349732}. TISSUE SPECIFICITY: Mainly present in the liver. Weak expression was found in the brain, lung and kidney. {ECO:0000269|PubMed:8765750, ECO:0000269|PubMed:9278263}. +Q5DTT8 PNMA5_MOUSE Paraneoplastic antigen-like protein 5 618 69,137 Chain (1); Erroneous initiation (1) TISSUE SPECIFICITY: Restricted to testis, where expression is low. Not detected in the brain. {ECO:0000269|PubMed:19366867}. +Q9CPS7 PNO1_MOUSE RNA-binding protein PNO1 248 27,454 Chain (1); Domain (1) FUNCTION: Positively regulates dimethylation of two adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 18S rRNA. {ECO:0000250|UniProtKB:Q9NRX1}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9NRX1}. +Q9ERD6 RGPS2_MOUSE Ras-specific guanine nucleotide-releasing factor RalGPS2 (Ral GEF with PH domain and SH3-binding motif 2) (RalA exchange factor RalGPS2) 590 65,530 Alternative sequence (4); Chain (1); Domain (2); Modified residue (9); Motif (1); Region (1); Sequence conflict (3) FUNCTION: Guanine nucleotide exchange factor for the small GTPase RALA. May be involved in cytoskeletal organization. May also be involved in the stimulation of transcription in a Ras-independent fashion. {ECO:0000269|PubMed:17462626}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17462626}. Cell membrane {ECO:0000269|PubMed:17462626}. Note=Associates with membranes through the PH domain. SUBUNIT: Interacts with RALA (By similarity). Interacts with the SH3 domains of GRB2 and PLCG1. {ECO:0000250, ECO:0000269|PubMed:17462626}. DOMAIN: The PH domain m1ediates binding to phosphatidylinositol 4,5-bisphosphate. {ECO:0000269|PubMed:17462626}. TISSUE SPECIFICITY: Abundant in brain and testis. {ECO:0000269|PubMed:17462626}. +P62515 PO3F4_MOUSE POU domain, class 3, transcription factor 4 (Brain-specific homeobox/POU domain protein 4) (Brain-4) (Brn-4) (Octamer-binding protein 9) (Oct-9) (Octamer-binding transcription factor 9) (OTF-9) 361 39,417 Chain (1); DNA binding (1); Domain (1); Modified residue (1) FUNCTION: Probable transcription factor which exert its primary action widely during early neural development and in a very limited set of neurons in the mature brain. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with HNRNPU. {ECO:0000250|UniProtKB:P49335}. TISSUE SPECIFICITY: Brain specific. +Q63955 PO4F3_MOUSE POU domain, class 4, transcription factor 3 (Brain-specific homeobox/POU domain protein 3C) (Brain-3C) (Brn-3C) (Brn-3.1) 338 37,016 Chain (1); DNA binding (1); Domain (1); Motif (1); Sequence conflict (5) FUNCTION: Acts as a transcriptional activator (PubMed:8290353, PubMed:7935408). Acts by binding to sequences related to the consensus octamer motif 5'-ATGCAAAT-3' in the regulatory regions of its target genes (PubMed:7935408). Involved in the auditory system development, required for terminal differentiation of hair cells in the inner ear (PubMed:8637595). {ECO:0000269|PubMed:7935408, ECO:0000269|PubMed:8290353, ECO:0000269|PubMed:8637595}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15319}. Cytoplasm {ECO:0000250|UniProtKB:Q15319}. Note=Preferentially localized in the nucleus. {ECO:0000250|UniProtKB:Q15319}. SUBUNIT: Interacts with ISL1 (PubMed:24643061). TISSUE SPECIFICITY: Brain. +Q9JJN0 POLH_MOUSE DNA polymerase eta (EC 2.7.7.7) (RAD30 homolog A) (Xeroderma pigmentosum variant type protein homolog) 694 76,167 Chain (1); Cross-link (4); Domain (1); Metal binding (2) FUNCTION: DNA polymerase specifically involved in the DNA repair by translesion synthesis (TLS) (PubMed:10871396). Due to low processivity on both damaged and normal DNA, cooperates with the heterotetrameric (REV3L, REV7, POLD2 and POLD3) POLZ complex for complete bypass of DNA lesions. Inserts one or 2 nucleotide(s) opposite the lesion, the primer is further extended by the tetrameric POLZ complex. In the case of 1,2-intrastrand d(GpG)-cisplatin cross-link, inserts dCTP opposite the 3' guanine (By similarity). Particularly important for the repair of UV-induced pyrimidine dimers (PubMed:10871396). Although inserts the correct base, may cause base transitions and transversions depending upon the context. May play a role in hypermutation at immunoglobulin genes. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but does not have any lyase activity, preventing the release of the 5'-deoxyribose phosphate (5'-dRP) residue. This covalent trapping of the enzyme by the 5'-dRP residue inhibits its DNA synthetic activity during base excision repair, thereby avoiding high incidence of mutagenesis. Targets POLI to replication foci (By similarity). {ECO:0000250|UniProtKB:Q9Y253, ECO:0000269|PubMed:10871396}. PTM: Monoubiquitinated by RCHY1/PIRH2; ubiquitination inhibits the ability of PolH to interact with PCNA and to bypass UV-induced lesions. {ECO:0000250|UniProtKB:Q9Y253}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y253}. Note=Accumulates at replication forks after DNA damage. After UV irradiation, recruited to DNA damage sites within 1 hour, to a maximum of about 80%; this recruitment may not be not restricted to cells active in DNA replication. {ECO:0000250|UniProtKB:Q9Y253}. SUBUNIT: Interacts with REV1 (PubMed:14657033). Interacts with monoubiquitinated PCNA, but not unmodified PCNA. Interacts with POLI; this interaction targets POLI to the replication machinery. Interacts with PALB2 and BRCA2; the interactions are direct and are required to sustain the recruitment of POLH at blocked replication forks and to stimulate POLH-dependent DNA synthesis on D loop substrates (By similarity). {ECO:0000250|UniProtKB:Q9Y253, ECO:0000269|PubMed:14657033}. DOMAIN: The catalytic core consists of fingers, palm and thumb subdomains, but the fingers and thumb subdomains are much smaller than in high-fidelity polymerases; residues from five sequence motifs of the Y-family cluster around an active site cleft that can accommodate DNA and nucleotide substrates with relaxed geometric constraints, with consequently higher rates of misincorporation and low processivity. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10871396}. +B1AUE5 PEX10_MOUSE Peroxisome biogenesis factor 10 (Peroxin-10) (Peroxisomal biogenesis factor 10) (Peroxisome assembly protein 10) 324 37,157 Chain (1); Zinc finger (1) FUNCTION: Somewhat implicated in the biogenesis of peroxisomes. {ECO:0000250}. SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. SUBUNIT: Interacts with PEX19. {ECO:0000250}. +Q8C437 PEX5R_MOUSE PEX5-related protein (PEX2-related protein) (PEX5-like protein) (Peroxin-5-related protein) (Tetratricopeptide repeat-containing Rab8b-interacting protein) (Pex5Rp) (TRIP8b) 567 63,135 Alternative sequence (2); Chain (1); Erroneous initiation (1); Helix (17); Modified residue (6); Repeat (6); Sequence conflict (2); Turn (2) FUNCTION: Accessory subunit of hyperpolarization-activated cyclic nucleotide-gated (HCN) channels, regulating their cell-surface expression and cyclic nucleotide dependence. {ECO:0000269|PubMed:22550182, ECO:0000269|Ref.5}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Some fraction is membrane associated via its interaction with RAB8B. {ECO:0000250}. SUBUNIT: Interacts with RAB8B (By similarity). Forms an obligate 4:4 complex with HCN2 (PubMed:22550182). Interacts with HCN3 (Ref.5). {ECO:0000250|UniProtKB:Q8IYB4, ECO:0000250|UniProtKB:Q925N3, ECO:0000269|PubMed:22550182, ECO:0000269|Ref.5}. +Q8C966 PF21B_MOUSE PHD finger protein 21B 487 53,002 Chain (1); Coiled coil (1); Zinc finger (1) +Q03958 PFD6_MOUSE Prefoldin subunit 6 (Protein Ke2) 127 14,455 Chain (1); Cross-link (2); Initiator methionine (1); Modified residue (3) FUNCTION: Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Heterohexamer of two PFD-alpha type and four PFD-beta type subunits. {ECO:0000250}. +Q9EPR2 PG12A_MOUSE Group XIIA secretory phospholipase A2 (GXII sPLA2) (sPLA2-XII) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase 12A) 192 21,319 Active site (2); Alternative sequence (1); Chain (1); Metal binding (4); Sequence conflict (2); Signal peptide (1) FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Does not exhibit detectable activity toward sn-2-arachidonoyl- or linoleoyl-phosphatidylcholine or -phosphatidylethanolamine (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. Cytoplasm {ECO:0000250}. +P09041 PGK2_MOUSE Phosphoglycerate kinase 2 (EC 2.7.2.3) (Phosphoglycerate kinase, testis specific) 417 44,853 Beta strand (21); Binding site (6); Chain (1); Helix (21); Modified residue (12); Nucleotide binding (1); Region (2); Sequence conflict (3); Turn (5) Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5. FUNCTION: Essential for sperm motility and male fertility but is not required for the completion of spermatogenesis (PubMed:19759366). {ECO:0000269|PubMed:19759366}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000269|PubMed:18004764}. TISSUE SPECIFICITY: Testis and sperm. Localized on the principle piece in the sperm (at protein level). Testis-specific. {ECO:0000269|PubMed:19759366, ECO:0000269|PubMed:3453121}. +Q9WUA3 PFKAP_MOUSE ATP-dependent 6-phosphofructokinase, platelet type (ATP-PFK) (PFK-P) (EC 2.7.1.11) (6-phosphofructokinase type C) (Phosphofructo-1-kinase isozyme C) (PFK-C) (Phosphohexokinase) 784 85,455 Active site (1); Alternative sequence (2); Binding site (9); Chain (1); Glycosylation (1); Metal binding (1); Modified residue (9); Natural variant (11); Nucleotide binding (2); Region (9) Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. PTM: GlcNAcylation decreases enzyme activity. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184}. SUBUNIT: Homo- and heterotetramers (By similarity). Phosphofructokinase (PFK) enzyme functions as a tetramer composed of different combinations of 3 types of subunits, called PFKM (M), PFKL (L) and PFKP (P). The composition of the PFK tetramer differs according to the tissue type it is present in. The kinetic and regulatory properties of the tetrameric enzyme are dependent on the subunit composition, hence can vary across tissues (Probable). {ECO:0000255|HAMAP-Rule:MF_03184, ECO:0000305}. TISSUE SPECIFICITY: Expression is constant during tumor growth and markedly decreases when cell proliferation stops. {ECO:0000269|PubMed:10814514}. +Q8CHP8 PGP_MOUSE Glycerol-3-phosphate phosphatase (G3PP) (EC 3.1.3.21) (Aspartate-based ubiquitous Mg(2+)-dependent phosphatase) (AUM) (EC 3.1.3.48) (Phosphoglycolate phosphatase) (PGP) 321 34,541 Active site (2); Beta strand (7); Chain (1); Helix (4); Metal binding (3); Mutagenesis (9); Site (1) FUNCTION: Glycerol-3-phosphate phosphatase hydrolyzing glycerol-3-phosphate into glycerol. Thereby, regulates the cellular levels of glycerol-3-phosphate a metabolic intermediate of glucose, lipid and energy metabolism (PubMed:26755581). Was also shown to have a 2-phosphoglycolate phosphatase activity and a tyrosine-protein phosphatase activity. However, their physiological relevance is unclear (PubMed:26755581, PubMed:24338473). In vitro, has also a phosphatase activity toward ADP, ATP, GDP and GTP (PubMed:24338473). {ECO:0000269|PubMed:24338473, ECO:0000269|PubMed:26755581}. SUBUNIT: Homodimer. {ECO:0000269|PubMed:24338473}. TISSUE SPECIFICITY: Ubiquitously expressed with higher expression in testis, heart, skeletal muscle and islet tissue (at protein level). {ECO:0000269|PubMed:24338473, ECO:0000269|PubMed:26755581}. +Q8VCS0 PGRP2_MOUSE N-acetylmuramoyl-L-alanine amidase (EC 3.5.1.28) (Peptidoglycan recognition protein 2) (Peptidoglycan recognition protein long) (PGRP-L) (TagL) 530 57,707 Alternative sequence (3); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (5); Metal binding (3); Modified residue (1); Sequence conflict (2); Signal peptide (1); Site (1) FUNCTION: May play a scavenger role by digesting biologically active peptidoglycan (PGN) into biologically inactive fragments. Has no direct bacteriolytic activity. SUBCELLULAR LOCATION: Secreted. Membrane. TISSUE SPECIFICITY: Strongly expressed in liver and fetal liver. +Q8BHF7 PGPS1_MOUSE CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase, mitochondrial (EC 2.7.8.5) (Phosphatidylglycerophosphate synthase 1) (PGP synthase 1) (Silencer-associated factor) 553 62,489 Active site (3); Chain (1); Domain (2); Erroneous initiation (1); Modified residue (1); Nucleotide binding (1); Sequence caution (1); Sequence conflict (1); Transit peptide (1) Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 1/2. FUNCTION: Functions in the biosynthesis of the anionic phospholipids phosphatidylglycerol and cardiolipin. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed with higher expression in testis, liver and brain. {ECO:0000269|PubMed:9880566}. +Q9JJT9 PHAX_MOUSE Phosphorylated adapter RNA export protein (RNA U small nuclear RNA export adapter protein) 385 43,247 Chain (1); Initiator methionine (1); Modified residue (9); Motif (3); Mutagenesis (11); Region (3); Sequence conflict (1) FUNCTION: A phosphoprotein adapter involved in the XPO1-mediated U snRNA export from the nucleus. Bridge components required for U snRNA export, the cap binding complex (CBC)-bound snRNA on the one hand and the GTPase Ran in its active GTP-bound form together with the export receptor XPO1 on the other. Its phosphorylation in the nucleus is required for U snRNA export complex assembly and export, while its dephosphorylation in the cytoplasm causes export complex disassembly. It is recycled back to the nucleus via the importin alpha/beta heterodimeric import receptor. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Its compartmentalized phosphorylation cycle may also contribute to the directionality of export. Binds strongly to m7G-capped U1 and U5 small nuclear RNAs (snRNAs) in a sequence-unspecific manner and phosphorylation-independent manner. Plays also a role in the biogenesis of U3 small nucleolar RNA (snoRNA). Involved in the U3 snoRNA transport from nucleoplasm to Cajal bodies. Binds strongly to m7G-capped U3, U8 and U13 precursor snoRNAs and weakly to trimethylated (TMG)-capped U3, U8 and U13 snoRNAs. Binds also to telomerase RNA (By similarity). {ECO:0000250, ECO:0000269|PubMed:10786834, ECO:0000269|PubMed:11333016}. PTM: Phosphorylated in the nucleus. Dephosphorylated in the cytoplasm. {ECO:0000269|PubMed:10786834}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H814}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9H814}. Nucleus, Cajal body {ECO:0000250|UniProtKB:Q9H814}. Cytoplasm {ECO:0000269|PubMed:10786834}. Note=Shuttles between the nucleus and the cytoplasm. Shuttles between the nucleoplasm and Cajal bodies. {ECO:0000250|UniProtKB:Q9H814}. SUBUNIT: Found in a U snRNA export complex with PHAX/RNUXA, NCBP1/CBP80, NCBP2/CBP20, RAN, XPO1 and m7G-capped RNA. Part of a precomplex with PHAX/RNUXA, NCBP1/CBP80, NCBP2/CBP20 and m7G-capped RNA. Interacts with NCBP1/CBP80. Found in a complex with snoRNA. Interacts with NCBP2/CBP20 (By similarity). {ECO:0000250|UniProtKB:Q9H814, ECO:0000269|PubMed:10786834, ECO:0000269|PubMed:11333016}. +Q9CXG9 PHF19_MOUSE PHD finger protein 19 (Polycomb-like protein 3) 578 65,236 Binding site (2); Chain (1); Domain (1); Modified residue (2); Mutagenesis (6); Region (1); Zinc finger (2) FUNCTION: Polycomb group (PcG) that specifically binds histone H3 trimethylated at 'Lys-36' (H3K36me3) and recruits the PRC2 complex. Probably involved in the transition from an active state to a repressed state in embryonic stem cells: acts by binding to H3K36me3, a mark for transcriptional activation, and recruiting H3K36me3 histone demethylases RIOX1 or KDM2B, leading to demethylation of H3K36 and recruitment of the PRC2 complex that mediates H3K27me3 methylation, followed by de novo silencing. Recruits the PRC2 complex to CpG islands and contributes to embryonic stem cell self-renewal. Also binds dimethylated at 'Lys-36' (H3K36me2). {ECO:0000269|PubMed:22438827, ECO:0000269|PubMed:23104054, ECO:0000269|PubMed:23160351, ECO:0000269|PubMed:23273982}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5T6S3}. SUBUNIT: Interacts with SUZ12. Interacts with RIOX1 (By similarity). Associated component of the PRC2 complex. Interacts with EZH2 (via its Tudor domain). {ECO:0000250|UniProtKB:Q5T6S3}. DOMAIN: The Tudor domain recognizes and binds H3K36me3. {ECO:0000269|PubMed:23104054}. +Q8CHP6 PHC3_MOUSE Polyhomeotic-like protein 3 981 105,353 Alternative sequence (4); Chain (1); Compositional bias (4); Cross-link (3); Domain (1); Modified residue (9); Motif (1); Sequence conflict (5); Zinc finger (1) FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of a PRC1-like complex. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous expression. {ECO:0000269|PubMed:12384788}. +Q80TL4 PHF24_MOUSE PHD finger protein 24 400 45,223 Alternative sequence (1); Chain (1); Erroneous initiation (1); Initiator methionine (1); Lipidation (1); Modified residue (5); Zinc finger (1) +Q9D8M7 PHF10_MOUSE PHD finger protein 10 (BRG1-associated factor 45a) (BAF45a) 497 55,840 Alternative sequence (1); Chain (1); Cross-link (2); Erroneous initiation (2); Modified residue (8); Region (3); Sequence conflict (5); Zinc finger (2) FUNCTION: Involved in transcription activity regulation by chromatin remodeling. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and is required for the proliferation of neural progenitors. During neural development a switch from a stem/progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth. {ECO:0000269|PubMed:17640523}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of neural progenitors-specific chromatin remodeling complex (npBAF complex) composed of at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, PHF10/BAF45A, ACTL6A/BAF53A and actin. Interacts with ACTL6A/BAF53A, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A and PBRM1/BAF180. {ECO:0000269|PubMed:17640523}. TISSUE SPECIFICITY: Widely expressed. Expressed selectively in neural stem and progenitor cells (at protein level). {ECO:0000269|PubMed:17640523}. +Q9QZC2 PLXC1_MOUSE Plexin-C1 (Virus-encoded semaphorin protein receptor) (CD antigen CD232) 1574 176,474 Chain (1); Disulfide bond (7); Domain (1); Glycosylation (9); Modified residue (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 951 971 Helical. {ECO:0000255}. TOPO_DOM 35 950 Extracellular. {ECO:0000255}.; TOPO_DOM 972 1574 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for SEMA7A, for vaccinia virus semaphorin A39R and for herpesvirus Sema protein. Binding of semaphorins triggers cellular responses leading to the rearrangement of the cytoskeleton and to secretion of IL6 and IL8 (By similarity). {ECO:0000250, ECO:0000269|PubMed:15611227}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Monomer. Homodimer. Interacts with SEMA7A (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Detected on dendritic cells, skin Langerhans cells and neutrophils (at protein level). {ECO:0000269|PubMed:15611227}. +Q9D1G2 PMVK_MOUSE Phosphomevalonate kinase (PMKase) (EC 2.7.4.2) 192 21,916 Alternative sequence (3); Binding site (4); Chain (1); Nucleotide binding (1); Sequence conflict (1) Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate: step 2/3. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q15126}. +Q8CC86 PNCB_MOUSE Nicotinate phosphoribosyltransferase (NAPRTase) (EC 6.3.4.21) (Nicotinate phosphoribosyltransferase domain-containing protein 1) 538 58,265 Binding site (4); Chain (1); Erroneous initiation (1); Erroneous termination (1); Modified residue (1); Sequence conflict (1) Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-ribonucleotide from nicotinate: step 1/1. FUNCTION: Catalyzes the first step in the biosynthesis of NAD from nicotinic acid, the ATP-dependent synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate. Helps prevent cellular oxidative stress via its role in NAD biosynthesis. {ECO:0000250|UniProtKB:Q6XQN6}. PTM: Transiently phosphorylated on a His residue during the reaction cycle. Phosphorylation strongly increases the affinity for substrates and increases the rate of nicotinate D-ribonucleotide production. Dephosphorylation regenerates the low-affinity form of the enzyme, leading to product release. {ECO:0000250|UniProtKB:P22253}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q6XQN6}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q6XQN6}. TISSUE SPECIFICITY: Abundantly expressed in the small intestine, liver and kidney. {ECO:0000269|PubMed:17604275}. +Q9Z2B3 RGR_MOUSE RPE-retinal G protein-coupled receptor 291 32,127 Chain (1); Disulfide bond (1); Modified residue (1); Topological domain (8); Transmembrane (7) TRANSMEM 16 36 Helical; Name=1. {ECO:0000255}.; TRANSMEM 53 73 Helical; Name=2. {ECO:0000255}.; TRANSMEM 92 112 Helical; Name=3. {ECO:0000255}.; TRANSMEM 131 151 Helical; Name=4. {ECO:0000255}.; TRANSMEM 176 196 Helical; Name=5. {ECO:0000255}.; TRANSMEM 220 240 Helical; Name=6. {ECO:0000255}.; TRANSMEM 248 268 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 15 Extracellular. {ECO:0000255}.; TOPO_DOM 37 52 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 74 91 Extracellular. {ECO:0000255}.; TOPO_DOM 113 130 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 152 175 Extracellular. {ECO:0000255}.; TOPO_DOM 197 219 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 241 247 Extracellular. {ECO:0000255}.; TOPO_DOM 269 291 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for all-trans- and 11-cis-retinal. Binds preferentially to the former and may catalyze the isomerization of the chromophore by a retinochrome-like mechanism (By similarity). {ECO:0000250}. PTM: Covalently binds all-trans- and 11-cis-retinal. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. +Q8CGE9 RGS12_MOUSE Regulator of G-protein signaling 12 (RGS12) 1381 149,637 Chain (1); Compositional bias (1); Cross-link (1); Domain (6); Modified residue (9); Sequence conflict (2) FUNCTION: Regulates G protein-coupled receptor signaling cascades. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. {ECO:0000250|UniProtKB:O08774}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O08774}. Cytoplasm {ECO:0000250|UniProtKB:O08774}. Cell projection, dendrite {ECO:0000250|UniProtKB:O08774}. Cell junction, synapse {ECO:0000250|UniProtKB:O08774}. SUBUNIT: Interacts with GNAI1, GNAI2 and GNAI3; the interactions are GDP-dependent. {ECO:0000250|UniProtKB:O08774}. DOMAIN: The GoLoco domain is necessary for interaction with GNAI1, GNAI2 and GNAI3. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain. {ECO:0000269|PubMed:15525537}. +P31360 PO3F2_MOUSE POU domain, class 3, transcription factor 2 (Brain-specific homeobox/POU domain protein 2) (Brain-2) (Brn-2) (Nervous system-specific octamer-binding transcription factor N-Oct-3) (Octamer-binding protein 7) (Oct-7) (Octamer-binding transcription factor 7) (OTF-7) 445 47,149 Chain (1); Compositional bias (2); DNA binding (1); Domain (1); Modified residue (1) FUNCTION: Transcription factor that plays a key role in neuronal differentiation (PubMed:24243019). Binds preferentially to the recognition sequence which consists of two distinct half-sites, ('GCAT') and ('TAAT'), separated by a non-conserved spacer region of 0, 2, or 3 nucleotides (By similarity). The combination of three transcription factors, ASCL1, POU3F2/BRN2 and MYT1L, is sufficient to reprogram fibroblasts and other somatic cells into induced neuronal (iN) cells in vitro (PubMed:20107439, PubMed:24243019, PubMed:27281220). Acts downstream of ASCL1, accessing chromatin that has been opened by ASCL1, and promotes transcription of neuronal genes (PubMed:24243019). {ECO:0000250|UniProtKB:P56222, ECO:0000269|PubMed:20107439, ECO:0000269|PubMed:24243019, ECO:0000269|PubMed:27281220}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with PQBP1 (By similarity). Interaction with ISL1 (PubMed:24643061). {ECO:0000250|UniProtKB:P20265, ECO:0000269|PubMed:24643061}. TISSUE SPECIFICITY: Expressed specifically in the neuroectodermal cell lineage. +Q9CR73 PNRC2_MOUSE Proline-rich nuclear receptor coactivator 2 140 15,401 Chain (1); Erroneous gene model prediction (1); Motif (1); Sequence conflict (1) FUNCTION: Involved in nonsense-mediated mRNA decay (NMD) by acting as a bridge between the mRNA decapping complex and the NMD machinery (By similarity). May act by targeting the NMD machinery to the P-body and recruiting the decapping machinery to aberrant mRNAs (By similarity). Required for UPF1/RENT1 localization to the P-body (By similarity). Plays a role in glucocorticoid receptor-mediated mRNA degradation by interacting with the glucocorticoid receptor NR3C1 in a ligand-dependent manner when it is bound to the 5' UTR of target mRNAs and recruiting the RNA helicase UPF1 and the mRNA-decapping enzyme DCP1A, leading to RNA decay (By similarity). Also acts as a nuclear receptor coactivator. May play a role in controlling the energy balance between energy storage and energy expenditure (PubMed:17971453). {ECO:0000250|UniProtKB:Q9NPJ4, ECO:0000269|PubMed:17971453}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, P-body {ECO:0000250}. SUBUNIT: Interacts with UPF1/RENT1; preferentially interacts with hyperphosphorylated form. Interacts with DCP1A. Interacts with many nuclear receptors including ESR1, ESRRA, ESRRG, NR3C1/GR, NR5A1, PGR, TR, RAR and RXR. {ECO:0000250|UniProtKB:Q9NPJ4}. DOMAIN: The interaction between PNRC2 and nuclear receptors is dependent on the SH3 binding motif. {ECO:0000250}. TISSUE SPECIFICITY: Strong expression is detected in lung, spleen, ovary, thymus, and colon. {ECO:0000269|PubMed:16181749}. +Q9JK95 PERP_MOUSE p53 apoptosis effector related to PMP-22 (Keratinocyte-associated protein 1) (KCP-1) 193 21,567 Chain (1); Transmembrane (4) TRANSMEM 12 32 Helical. {ECO:0000255}.; TRANSMEM 81 101 Helical. {ECO:0000255}.; TRANSMEM 110 130 Helical. {ECO:0000255}.; TRANSMEM 151 171 Helical. {ECO:0000255}. FUNCTION: Component of intercellular desmosome junctions. Plays a role in stratified epithelial integrity and cell-cell adhesion by promoting desmosome assembly. Plays a role as an effector in the TP53-dependent apoptotic pathway. {ECO:0000269|PubMed:10733530, ECO:0000269|PubMed:15797384}. SUBCELLULAR LOCATION: Cell junction, desmosome {ECO:0000269|PubMed:15797384}. Cell membrane {ECO:0000269|PubMed:15797384}; Multi-pass membrane protein {ECO:0000255}. Note=Associated with desmosomes. {ECO:0000269|PubMed:15797384}. TISSUE SPECIFICITY: Expressed in the stratified squamous skin epithelium of the skin and the tongue, but not in simple epithelia (at protein level). Expressed in apoptotic cells. {ECO:0000269|PubMed:10733530, ECO:0000269|PubMed:15797384}. +P61759 PFD3_MOUSE Prefoldin subunit 3 (von Hippel-Lindau-binding protein 1) (VBP-1) (VHL-binding protein 1) 196 22,436 Chain (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (2) FUNCTION: Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=In complex with VHL can translocate to the nucleus. SUBUNIT: Heterohexamer of two PFD-alpha type and four PFD-beta type subunits. Binds to the C-terminal part of VHL. +Q3TQR0 PGAP2_MOUSE Post-GPI attachment to proteins factor 2 (FGF receptor-activating protein 1) 254 29,446 Alternative sequence (2); Chain (1); Erroneous initiation (1); Sequence conflict (5); Topological domain (6); Transmembrane (5) TRANSMEM 24 44 Helical. {ECO:0000255}.; TRANSMEM 115 135 Helical. {ECO:0000255}.; TRANSMEM 144 164 Helical. {ECO:0000255}.; TRANSMEM 186 206 Helical. {ECO:0000255}.; TRANSMEM 210 230 Helical. {ECO:0000255}. TOPO_DOM 1 23 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 45 114 Lumenal. {ECO:0000255}.; TOPO_DOM 136 143 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 165 185 Lumenal. {ECO:0000255}.; TOPO_DOM 207 209 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 231 254 Lumenal. {ECO:0000255}. FUNCTION: Involved in the lipid remodeling steps of GPI-anchor maturation. Required for stable expression of GPI-anchored proteins at the cell surface (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with PGAP2IP. {ECO:0000269|PubMed:17761529}. +D3YZI9 PGBD5_MOUSE PiggyBac transposable element-derived protein 5 (EC 3.1.-.-) (PiggyBac transposase 5) 523 58,300 Alternative sequence (1); Chain (1); Modified residue (1); Sequence caution (1) FUNCTION: Transposase that mediates sequence-specific genomic rearrangements. {ECO:0000250|UniProtKB:Q8N414}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24180413}. TISSUE SPECIFICITY: Expressed in the brain (at protein level). {ECO:0000269|PubMed:24180413}. +Q8VC52 RBPS2_MOUSE RNA-binding protein with multiple splicing 2 206 22,463 Chain (1); Domain (1); Initiator methionine (1); Modified residue (1); Region (1) FUNCTION: Contributes to the regulation of smooth muscle cell differentiation and proliferation in the gastrointestinal system. Binds NOG mRNA. Mediates an increase of NOG mRNA levels, and thereby contributes to the negative regulation of the BMP signaling pathway. This promotes reversible dedifferentiation of smooth muscle cells and promotes smooth muscle cell proliferation. {ECO:0000250|UniProtKB:Q9W6I1}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6ZRY4}. SUBUNIT: Homodimer. Interacts with EEF2. {ECO:0000250|UniProtKB:Q6ZRY4}. +P26618 PGFRA_MOUSE Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor) (CD140 antigen-like family member A) (Platelet-derived growth factor alpha receptor) (CD antigen CD140a) 1089 122,683 Active site (1); Alternative sequence (2); Binding site (1); Chain (1); Disulfide bond (4); Domain (6); Glycosylation (10); Modified residue (11); Nucleotide binding (1); Sequence conflict (16); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 529 549 Helical. {ECO:0000255}. TOPO_DOM 25 528 Extracellular. {ECO:0000255}.; TOPO_DOM 550 1089 Cytoplasmic. {ECO:0000255}. FUNCTION: Tyrosine-protein kinase that acts as a cell-surface receptor for PDGFA, PDGFB and PDGFC and plays an essential role in the regulation of embryonic development, cell proliferation, survival and chemotaxis. Depending on the context, promotes or inhibits cell proliferation and cell migration. Plays an important role in the differentiation of bone marrow-derived mesenchymal stem cells. Required for normal skeleton development and cephalic closure during embryonic development. Required for normal development of the mucosa lining the gastrointestinal tract, and for recruitment of mesenchymal cells and normal development of intestinal villi. Plays a role in cell migration and chemotaxis in wound healing. Plays a role in platelet activation, secretion of agonists from platelet granules, and in thrombin-induced platelet aggregation. Binding of its cognate ligands - homodimeric PDGFA, homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or homodimeric PDGFC -leads to the activation of several signaling cascades; the response depends on the nature of the bound ligand and is modulated by the formation of heterodimers between PDGFRA and PDGFRB. Phosphorylates PIK3R1, PLCG1, and PTPN11. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate, mobilization of cytosolic Ca(2+) and the activation of protein kinase C. Phosphorylates PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, and thereby mediates activation of the AKT1 signaling pathway. Mediates activation of HRAS and of the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. Promotes activation of STAT family members STAT1, STAT3 and STAT5A and/or STAT5B. Receptor signaling is down-regulated by protein phosphatases that dephosphorylate the receptor and its down-stream effectors, and by rapid internalization of the activated receptor. {ECO:0000269|PubMed:10903171, ECO:0000269|PubMed:19030102, ECO:0000269|PubMed:20110689, ECO:0000269|PubMed:9226440}. PTM: Ubiquitinated, leading to its internalization and degradation. {ECO:0000269|PubMed:29237719}.; PTM: Autophosphorylated on tyrosine residues upon ligand binding. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Phosphorylation at Tyr-731 and Tyr-742 is important for interaction with PIK3R1. Phosphorylation at Tyr-720 and Tyr-754 is important for interaction with PTPN11. Phosphorylation at Tyr-762 is important for interaction with CRK. Phosphorylation at Tyr-572 and Tyr-574 is important for interaction with SRC and SRC family members. Phosphorylation at Tyr-988 and Tyr-1018 is important for interaction with PLCG1 (By similarity). {ECO:0000250|UniProtKB:P16234}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P16234}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P16234}. Cell projection, cilium {ECO:0000269|PubMed:29237719}. Golgi apparatus {ECO:0000269|PubMed:29237719}. SUBUNIT: Interacts with homodimeric PDGFA, PDGFB and PDGFC, and with heterodimers formed by PDGFA and PDGFB. Monomer in the absence of bound ligand. Interaction with dimeric PDGFA, PDGFB and/or PDGFC leads to receptor dimerization, where both PDGFRA homodimers and heterodimers with PDGFRB are observed. Interacts (tyrosine phosphorylated) with SHB (via SH2 domain). Interacts (tyrosine phosphorylated) with SHF (via SH2 domain). Interacts (tyrosine phosphorylated) with SRC (via SH2 domain). Interacts (tyrosine phosphorylated) with PIK3R1. Interacts (tyrosine phosphorylated) with PLCG1 (via SH2 domain). Interacts (tyrosine phosphorylated) with CRK, GRB2 and GRB7 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Focally expressed in cortical interstitial cells and highly expressed in the interstitium of the papillary region. Also expressed by adventitial cells in arterial vessels. Up-regulated in areas of renal fibrosis. In mice with unilateral ureteral obstruction, expression in cortical interstitial cells becomes prominent at day 4 which increases progressively until day 14. {ECO:0000269|PubMed:14514732}. +Q8BZF8 PGM5_MOUSE Phosphoglucomutase-like protein 5 567 62,220 Active site (1); Binding site (4); Chain (1); Compositional bias (1); Erroneous initiation (1); Metal binding (4); Modified residue (2); Region (3) FUNCTION: Component of adherens-type cell-cell and cell-matrix junctions. Lacks phosphoglucomutase activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, adherens junction. Cytoplasm, cytoskeleton. Note=Adherens-type cellular junctions. Concentrated in focal contacts at the ends of actin bundles, and associated with actin filaments (By similarity). {ECO:0000250}. SUBUNIT: Interacts with cytoskeletal proteins dystrophin and utrophin. {ECO:0000250}. +O55022 PGRC1_MOUSE Membrane-associated progesterone receptor component 1 (mPR) 195 21,694 Chain (1); Domain (1); Modified residue (4); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 25 43 Helical. {ECO:0000255}. TOPO_DOM 1 24 Lumenal. {ECO:0000255}.; TOPO_DOM 44 195 Cytoplasmic. {ECO:0000255}. FUNCTION: Component of a progesterone-binding protein complex. Binds progesterone. Has many reported cellular functions (heme homeostasis, interaction with CYPs). {ECO:0000250|UniProtKB:O00264}. SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250|UniProtKB:Q95250}; Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O00264}; Single-pass membrane protein {ECO:0000255}. SUBUNIT: Homodimer. Forms stable homodimer through hydrophobic heme-heme stacking interactions. {ECO:0000250|UniProtKB:O00264}. DOMAIN: The cytochrome b5 heme-binding domain lacks the conserved iron-binding His residues at positions 107 and 131. {ECO:0000250}. +O88593 PGRP1_MOUSE Peptidoglycan recognition protein 1 (Cytokine tag7) (Peptidoglycan recognition protein short) (PGRP-S) 182 20,489 Chain (1); Disulfide bond (3); Domain (1); Frameshift (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Pattern receptor that binds to murein peptidoglycans (PGN) of Gram-positive bacteria. Has bactericidal activity towards Gram-positive bacteria. May kill Gram-positive bacteria by interfering with peptidoglycan biosynthesis. Binds also to Gram-negative bacteria. Involved in innate immunity. May function in intracellular killing of bacteria. The soluble form triggers apoptosis in vitro. {ECO:0000269|PubMed:12649138, ECO:0000269|PubMed:9660837, ECO:0000269|PubMed:9707603}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9660837}. Secreted {ECO:0000269|PubMed:9660837}. Note=Exists in both soluble and membrane-associated forms. SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}. TISSUE SPECIFICITY: Strongly expressed in spleen and lung. Also detected in brain and thymus. In the lung, expressed in the intraalveolar space, in the brain, expressed in the Purkinje cells of the cerebellum and in certain layers of neurons in the hippocampus. Also detected in cells filling the space within the intestinal villus. {ECO:0000269|PubMed:9707603}. +Q2YFS2 PILRB_MOUSE Paired immunoglobulin-like type 2 receptor beta (Activating receptor PILR-beta) (Cell surface receptor FDFACT) 224 25,200 Chain (1); Erroneous initiation (1); Glycosylation (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 196 216 Helical. {ECO:0000255}. TOPO_DOM 29 195 Extracellular. {ECO:0000255}.; TOPO_DOM 217 224 Cytoplasmic. {ECO:0000255}. FUNCTION: Paired receptors consist of highly related activating and inhibitory receptors and are widely involved in the regulation of the immune system. PILRB is thought to act as a cellular signaling activating receptor that associates with ITAM-bearing adapter molecules on the cell surface. Seems to associate with DAP12 and is a receptor for CD99. May be involved in target cell recognition by natural killer cells and in activation of dendritic cells. {ECO:0000269|PubMed:14970179}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Interacts with CD99. Probably associates with DAP12. {ECO:0000269|PubMed:14970179}. TISSUE SPECIFICITY: Widely expressed with highest levels in spleen, liver and lung. Predominantly expressed by natural killer cells, macrophages, and granulocytes and dendritic cells (BM-DC). {ECO:0000269|PubMed:14970179}. +Q8BSF4 PISD_MOUSE Phosphatidylserine decarboxylase proenzyme, mitochondrial (EC 4.1.1.65) [Cleaved into: Phosphatidylserine decarboxylase beta chain; Phosphatidylserine decarboxylase alpha chain] 406 45,927 Active site (4); Chain (3); Modified residue (1); Sequence conflict (1); Site (1); Topological domain (2); Transit peptide (1); Transmembrane (1) TRANSMEM 61 79 Helical. {ECO:0000255|HAMAP-Rule:MF_03208}. TOPO_DOM 50 60 Mitochondrial matrix. {ECO:0000255|HAMAP-Rule:MF_03208}.; TOPO_DOM 80 406 Mitochondrial intermembrane. {ECO:0000255|HAMAP-Rule:MF_03208}. FUNCTION: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine. {ECO:0000255|HAMAP-Rule:MF_03208}. PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The autoendoproteolytic cleavage occurs by a canonical serine protease mechanism, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain. During this reaction, the Ser that is part of the protease active site of the proenzyme becomes the pyruvoyl prosthetic group, which constitutes an essential element of the active site of the mature decarboxylase. {ECO:0000255|HAMAP-Rule:MF_03208}. SUBCELLULAR LOCATION: Phosphatidylserine decarboxylase beta chain: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:6862014}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03208}; Intermembrane side {ECO:0000255|HAMAP-Rule:MF_03208}.; SUBCELLULAR LOCATION: Phosphatidylserine decarboxylase alpha chain: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:6862014}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03208}; Intermembrane side {ECO:0000255|HAMAP-Rule:MF_03208}. Note=Anchored to the mitochondrial inner membrane through its interaction with the integral membrane beta chain. {ECO:0000255|HAMAP-Rule:MF_03208}. SUBUNIT: Heterodimer of a large membrane-associated beta subunit and a small pyruvoyl-containing alpha subunit. {ECO:0000255|HAMAP-Rule:MF_03208}. TISSUE SPECIFICITY: Widely expressed, with highest levels in testis, including Sertoli cells, followed by liver. {ECO:0000269|PubMed:16192276}. +Q8R0J1 PKHG6_MOUSE Pleckstrin homology domain-containing family G member 6 (PH domain-containing family G member 6) 787 89,148 Chain (1); Domain (2); Sequence conflict (5) FUNCTION: Guanine nucleotide exchange factor activating the small GTPase RHOA, which, in turn, induces myosin filament formation. Also activates RHOG. Does not activate RAC1, or to a much lower extent than RHOA and RHOG. Part of a functional unit, involving PLEKHG6, MYH10 and RHOA, at the cleavage furrow to advance furrow ingression during cytokinesis. In epithelial cells, required for the formation of microvilli and membrane ruffles on the apical pole. Along with EZR, required for normal macropinocytosis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell projection, microvillus {ECO:0000250|UniProtKB:Q3KR16}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q3KR16}. Cleavage furrow {ECO:0000250|UniProtKB:Q3KR16}. Note=During mitosis, localizes to the spindle pole, central spindle and cleavage furrow. In epithelial cells, recruited to the apical membrane by EZR where it participates in macropinocytosis. {ECO:0000250|UniProtKB:Q3KR16}. SUBUNIT: Interacts with MYH10. Interacts with ELMO1 and EZR (in an open conformation). Interacts with CSPP1 (By similarity). {ECO:0000250}. +Q80TI1 PKHH1_MOUSE Pleckstrin homology domain-containing family H member 1 (PH domain-containing family H member 1) 1356 150,909 Alternative sequence (2); Chain (1); Coiled coil (2); Domain (4); Erroneous initiation (1); Modified residue (2); Sequence conflict (9) +Q9ERS5 PKHA2_MOUSE Pleckstrin homology domain-containing family A member 2 (PH domain-containing family A member 2) (PH domain-containing adaptor PHAD47) (Tandem PH domain-containing protein 2) (TAPP-2) 425 47,380 Beta strand (7); Chain (1); Cross-link (1); Domain (2); Helix (1); Modified residue (3); Sequence conflict (1); Turn (5) FUNCTION: Binds specifically to phosphatidylinositol 3,4-diphosphate (PtdIns3,4P2), but not to other phosphoinositides. May recruit other proteins to the plasma membrane. {ECO:0000269|PubMed:12101241, ECO:0000269|PubMed:14516276}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12101241}. Cell membrane {ECO:0000269|PubMed:12101241}; Peripheral membrane protein {ECO:0000269|PubMed:12101241}. Nucleus {ECO:0000269|PubMed:12101241}. Note=Locates to the plasma membrane after treatments that stimulate the production of PtdIns3,4P2. SUBUNIT: Binds MPDZ and PTPN13. +Q80W71 PKHA8_MOUSE Pleckstrin homology domain-containing family A member 8 (PH domain-containing family A member 8) (Phosphatidylinositol-four-phosphate adapter protein 2) (FAPP-2) (Phosphoinositol 4-phosphate adapter protein 2) 519 57,962 Alternative sequence (1); Chain (1); Domain (1); Modified residue (3); Region (1) FUNCTION: Cargo transport protein that is required for apical transport from the trans-Golgi network (TGN). Transports AQP2 from the trans-Golgi network (TGN) to sites of AQP2 phosphorylation. Mediates the non-vesicular transport of glucosylceramide (GlcCer) from the trans-Golgi network (TGN) to the plasma membrane and plays a pivotal role in the synthesis of complex glycosphingolipids. Binding of both phosphatidylinositol 4-phosphate (PIP) and ARF1 are essential for the GlcCer transfer ability. Also required for primary cilium formation, possibly by being involved in the transport of raft lipids to the apical membrane, and for membrane tubulation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q96JA3}. Membrane {ECO:0000250|UniProtKB:Q96JA3}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q96JA3}. Note=Binds through its PH domain to PtdIns(4)P and ARF1, and subsequently localizes to TGN exit sites. {ECO:0000250|UniProtKB:Q96JA3}. SUBUNIT: Homodimer. Interacts with ARF1; the interaction together with phosphatidylinositol 4-phosphate binding is required for FAPP2 GlcCer transfer ability. {ECO:0000250}. DOMAIN: The PH domain of FAPPS binds the small GTPase ARF1 and phosphatidylinositol-4-phosphate (PtdIns4P) with high selectivity, and is required for recruitment of FAPPs to the trans-Golgi network (TGN). {ECO:0000250}. +Q8BM47 PKHM3_MOUSE Pleckstrin homology domain-containing family M member 3 (PH domain-containing family M member 3) (Differentiation-associated protein) 761 86,553 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (2); Modified residue (1); Sequence conflict (1); Zinc finger (1) FUNCTION: Involved in skeletal muscle differentiation (PubMed:19028694). May act as a scaffold protein for AKT1 during muscle differentiation (PubMed:19028694). {ECO:0000269|PubMed:19028694}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19028694}. Golgi apparatus {ECO:0000269|PubMed:19028694}. Cell membrane {ECO:0000269|PubMed:19028694}. Note=Before differentiation of muscle cells, localized to the cytosol. During muscle differentiation shuttles to the plasma membrane. {ECO:0000269|PubMed:19028694}. SUBUNIT: Interacts with AKT1. {ECO:0000269|PubMed:19028694}. TISSUE SPECIFICITY: Widely expressed (PubMed:19028694). Expressed in C2C12 cells (at protein level) (PubMed:19028694). {ECO:0000269|PubMed:19028694}. +Q8K124 PKHO2_MOUSE Pleckstrin homology domain-containing family O member 2 (PH domain-containing family O member 2) (Pleckstrin homology domain-containing family Q member 1) (PH domain-containing family Q member 1) 495 53,872 Chain (1); Coiled coil (1); Domain (1); Modified residue (10); Sequence conflict (5) +Q6KAU7 PKHG2_MOUSE Pleckstrin homology domain-containing family G member 2 (PH domain-containing family G member 2) (Common site lymphoma/leukemia guanine nucleotide exchange factor) (Common site lymphoma/leukemia GEF) 1340 143,376 Alternative sequence (2); Chain (1); Compositional bias (2); Domain (2); Erroneous initiation (3); Modified residue (6); Sequence conflict (5) FUNCTION: May be a transforming oncogene with exchange activity for CDC42. May be a guanine-nucleotide exchange factor (GEF) for RAC1 and CDC42 (PubMed:11839748). Activated by the binding to subunits beta and gamma of the heterotrimeric guanine nucleotide-binding protein (G protein) (By similarity). Involved in the regulation of actin polymerization (By similarity). {ECO:0000250|UniProtKB:Q9H7P9, ECO:0000269|PubMed:11839748}. TISSUE SPECIFICITY: Expressed in thymus, skeletal muscle, lung, testis, uterus, pancreas and heart and also expressed during embryogenesis. {ECO:0000269|PubMed:11839748}. +A2A259 PK2L1_MOUSE Polycystic kidney disease 2-like 1 protein (Polycystin-2 homolog) 760 87,234 Beta strand (8); Calcium binding (1); Chain (1); Coiled coil (2); Disulfide bond (1); Domain (1); Glycosylation (4); Helix (13); Intramembrane (1); Lipidation (1); Mutagenesis (10); Region (1); Sequence conflict (8); Topological domain (8); Transmembrane (6); Turn (4) INTRAMEM 512 526 Pore-forming. {ECO:0000305|PubMed:29567962}. TRANSMEM 104 124 Helical. {ECO:0000305|PubMed:29567962}.; TRANSMEM 357 376 Helical. {ECO:0000305|PubMed:29567962}.; TRANSMEM 385 405 Helical. {ECO:0000305|PubMed:29567962}.; TRANSMEM 434 454 Helical. {ECO:0000305|PubMed:29567962}.; TRANSMEM 480 499 Helical. {ECO:0000305|PubMed:29567962}.; TRANSMEM 537 557 Helical. {ECO:0000305|PubMed:29567962}. TOPO_DOM 1 103 Cytoplasmic. {ECO:0000305|PubMed:29567962}.; TOPO_DOM 125 356 Extracellular. {ECO:0000305|PubMed:29567962}.; TOPO_DOM 377 384 Cytoplasmic. {ECO:0000305|PubMed:29567962}.; TOPO_DOM 406 433 Extracellular. {ECO:0000305|PubMed:29567962}.; TOPO_DOM 455 479 Cytoplasmic. {ECO:0000305|PubMed:29567962}.; TOPO_DOM 500 511 Extracellular. {ECO:0000305|PubMed:29567962}.; TOPO_DOM 527 536 Extracellular. {ECO:0000305|PubMed:29567962}.; TOPO_DOM 558 760 Cytoplasmic. {ECO:0000305|PubMed:29567962}. FUNCTION: Pore-forming subunit of a heteromeric, non-selective cation channel that is permeable to Ca(2+) (PubMed:16891422, PubMed:15548533, PubMed:19464260, PubMed:20538909, PubMed:21185261, PubMed:22420714, PubMed:25820328, PubMed:28904867, PubMed:29567962). Pore-forming subunit of a calcium-permeant ion channel formed by PKD1L2 and PKD1L1 in primary cilia, where it controls cilium calcium concentration, but does not affect cytoplasmic calcium concentration (PubMed:24336288, PubMed:24336289). The channel formed by PKD1L2 and PKD1L1 in primary cilia regulates sonic hedgehog/SHH signaling and GLI2 transcription (PubMed:24336288). Pore-forming subunit of a channel formed by PKD1L2 and PKD1L3 that contributes to sour taste perception in gustatory cells (PubMed:16891422, PubMed:16929298, PubMed:20406802, PubMed:21098668, PubMed:21625513). The heteromeric channel formed by PKD1L2 and PKD1L3 is activated by low pH, but opens only when the extracellular pH rises again (PubMed:18535624, PubMed:19464260, PubMed:20538909, PubMed:20406802, PubMed:22420714, PubMed:28904867, PubMed:29567962). May play a role in the perception of carbonation taste (PubMed:19833970). May play a role in the sensory perception of water, via a mechanism that activates the channel in response to dilution of salivary bicarbonate and changes in salivary pH (PubMed:28553944). {ECO:0000269|PubMed:15548533, ECO:0000269|PubMed:16891422, ECO:0000269|PubMed:16929298, ECO:0000269|PubMed:18535624, ECO:0000269|PubMed:19464260, ECO:0000269|PubMed:19833970, ECO:0000269|PubMed:20406802, ECO:0000269|PubMed:20538909, ECO:0000269|PubMed:21098668, ECO:0000269|PubMed:21185261, ECO:0000269|PubMed:21625513, ECO:0000269|PubMed:22420714, ECO:0000269|PubMed:24336288, ECO:0000269|PubMed:24336289, ECO:0000269|PubMed:25820328, ECO:0000269|PubMed:28553944, ECO:0000269|PubMed:28904867, ECO:0000269|PubMed:29567962}. PTM: Palmitoylation is important for expression at the cell membrane and for channel activity. {ECO:0000250|UniProtKB:Q9P0L9}. SUBCELLULAR LOCATION: Cell projection, cilium membrane {ECO:0000269|PubMed:24336288, ECO:0000269|PubMed:24336289}; Multi-pass membrane protein {ECO:0000269|PubMed:29567962}. Cell membrane {ECO:0000269|PubMed:15548533, ECO:0000269|PubMed:16891422, ECO:0000269|PubMed:18535624, ECO:0000269|PubMed:19464260, ECO:0000269|PubMed:20406802, ECO:0000269|PubMed:20538909, ECO:0000269|PubMed:21185261, ECO:0000269|PubMed:22420714, ECO:0000269|PubMed:25820328}; Multi-pass membrane protein {ECO:0000269|PubMed:29567962}. Cytoplasmic vesicle {ECO:0000305|PubMed:20538909}. Note=Interaction with PKD1 or PKD1L3 is required for localization to the cell membrane. {ECO:0000269|PubMed:15548533, ECO:0000269|PubMed:16891422, ECO:0000269|PubMed:20538909, ECO:0000269|PubMed:21185261}. SUBUNIT: Homotetramer (PubMed:25820328, PubMed:29567962). Heterotetramer with either PKD1L1, PKD1L3 or PKD1; the heterotetrameric complex probably contains 3 PKD1L2 chains plus one chain from another family member (PubMed:16891422, PubMed:15548533, PubMed:25820328, PubMed:29567962). Interacts with PKD1L1, forming a ciliary calcium channel (PubMed:24336289). Interacts with PKD1L3, forming a cation channel that is activated by low extracellular pH (PubMed:16891422, PubMed:18535624, PubMed:19464260, PubMed:20538909, PubMed:20406802, PubMed:22420714, PubMed:25820328, PubMed:29567962). Interacts with PKD1 (PubMed:15548533). Interacts with RACK1; inhibits the channel activity possibly by impairing localization to the cell membrane (By similarity). {ECO:0000250|UniProtKB:Q9P0L9, ECO:0000269|PubMed:15548533, ECO:0000269|PubMed:16891422, ECO:0000269|PubMed:18535624, ECO:0000269|PubMed:19464260, ECO:0000269|PubMed:20406802, ECO:0000269|PubMed:20538909, ECO:0000269|PubMed:22420714, ECO:0000269|PubMed:24336289, ECO:0000269|PubMed:25820328, ECO:0000269|PubMed:29567962}. DOMAIN: The EF-hand domain probably mediates calcium-binding. It is not required for channel activation. {ECO:0000250|UniProtKB:Q9P0L9}.; DOMAIN: Interaction of the cytoplasmic N- and C-terminal domains is important for channel activity. {ECO:0000250|UniProtKB:Q9P0L9}. TISSUE SPECIFICITY: Detected in kidney, testis and brain, (PubMed:25820328). Expressed in all 4 taste areas in taste buds. Detected in the taste pore region of circumvallate papillae, foliate papillae, fungiform papillae and palate (PubMed:16891422, PubMed:16929298, PubMed:20538909, PubMed:21625513). Expressed in cells distinct from those mediating sweet, umami and bitter taste (at protein level) (PubMed:16891422). Expressed in type III taste cells (at protein level) (PubMed:18156604). Ubiquitous (PubMed:15548533). Detected in circumvallate, foliate, fungiform and palate taste buds, in cells distinct from those mediating sweet, umami and bitter taste (PubMed:16929298, PubMed:21625513). Detected in taste tissues and testis (PubMed:16891422). {ECO:0000269|PubMed:15548533, ECO:0000269|PubMed:16891422, ECO:0000269|PubMed:16929298, ECO:0000269|PubMed:18156604, ECO:0000269|PubMed:20538909, ECO:0000269|PubMed:21625513, ECO:0000269|PubMed:25820328}. +Q3TCN2 PLBL2_MOUSE Putative phospholipase B-like 2 (EC 3.1.1.-) (66.3 kDa protein) (76 kDa protein) (p76) (LAMA-like protein 2) (Lamina ancestor homolog 2) (Phospholipase B domain-containing protein 2) [Cleaved into: Putative phospholipase B-like 2 28 kDa form; Putative phospholipase B-like 2 40 kDa form; Putative phospholipase B-like 2 15 kDa form] 594 66,289 Alternative sequence (2); Beta strand (25); Chain (4); Disulfide bond (2); Erroneous initiation (1); Glycosylation (5); Helix (24); Sequence conflict (12); Signal peptide (1); Turn (7) FUNCTION: Putative phospholipase. {ECO:0000250}. PTM: The p76 protein is synthesized as a 76 kDa precursor which is then processed into a N-terminal 28 kDa form and a C-terminal 40 kDa form. The C-terminal peptide is further processed into a 15 kDa form.; PTM: Glycosylated; contains mannose 6-phosphate sugars. {ECO:0000250}. SUBCELLULAR LOCATION: Lysosome lumen {ECO:0000269|PubMed:17007843, ECO:0000269|PubMed:17105447}. SUBUNIT: Interacts with IGF2R. {ECO:0000250}. TISSUE SPECIFICITY: Present at highest levels in spleen, lung and brain (at protein level). {ECO:0000269|PubMed:17007843}. +Q8R3B1 PLCD1_MOUSE 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1 (EC 3.1.4.11) (Phosphoinositide phospholipase C-delta-1) (Phospholipase C-delta-1) (PLC-delta-1) 756 85,873 Active site (2); Binding site (4); Calcium binding (2); Chain (1); Domain (6); Glycosylation (2); Metal binding (10); Modified residue (2); Region (1); Sequence conflict (1) FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. Essential for trophoblast and placental development. {ECO:0000269|PubMed:16314520}. TISSUE SPECIFICITY: Highly expressed in brain, heart, lung, epididymis and testis. Detected at lower levels in kidney and skeletal muscle. {ECO:0000269|PubMed:10425196}. +Q91VC4 PLVAP_MOUSE Plasmalemma vesicle-associated protein (MECA-32 antigen) (Plasmalemma vesicle protein 1) (PV-1) 438 49,933 Chain (1); Coiled coil (3); Compositional bias (1); Glycosylation (4); Sequence conflict (10); Topological domain (2); Transmembrane (1) TRANSMEM 27 47 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 26 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 48 438 Extracellular. {ECO:0000255}. FUNCTION: Involved in the formation of stomatal and fenestral diaphragms of caveolae. May function in microvascular permeability (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9WV78}; Single-pass type II membrane protein {ECO:0000255}. Membrane, caveola {ECO:0000250|UniProtKB:Q9WV78}; Single-pass type II membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9WV78}. Note=Membrane-associated protein of caveolae. Found in fenestral and stomatal diaphragms in fenestrated endothelia and transendothelial channels. Also colocalized with CAV1 in perinuclear region. {ECO:0000250|UniProtKB:Q9WV78}. SUBUNIT: Homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in lung, kidney, spleen, heart, muscle, eye, pancreas, thyroid, thymus, submaxillary gland, prostate, epididymis, uterus and liver. {ECO:0000269|PubMed:11401446, ECO:0000269|PubMed:7626790}. +Q9Z210 PX11B_MOUSE Peroxisomal membrane protein 11B (Peroxin-11B) (Peroxisomal biogenesis factor 11B) (Protein PEX11 homolog beta) (PEX11-beta) 259 28,710 Chain (1); Modified residue (1); Region (1); Sequence conflict (3); Transmembrane (1) TRANSMEM 234 254 Helical. {ECO:0000255}. FUNCTION: Involved in peroxisomal proliferation. May regulate peroxisome division by recruiting the dynamin-related GTPase DNM1L to the peroxisomal membrane. Promotes membrane protrusion and elongation on the peroxisomal surface. {ECO:0000250|UniProtKB:O96011, ECO:0000269|PubMed:11839773, ECO:0000269|PubMed:12024045}. SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000250|UniProtKB:O96011}; Single-pass membrane protein {ECO:0000250|UniProtKB:O96011}. SUBUNIT: Homodimer. Heterodimer with PEX11G. Interacts with PEX19. Interacts with FIS1. {ECO:0000250|UniProtKB:O96011}. +Q8JZU6 PXDC1_MOUSE PX domain-containing protein 1 231 26,448 Alternative sequence (3); Chain (1); Domain (1) +Q3UQ28 PXDN_MOUSE Peroxidasin homolog (EC 1.11.1.7) 1475 165,103 Active site (1); Binding site (2); Chain (1); Disulfide bond (10); Domain (7); Glycosylation (7); Metal binding (6); Modified residue (2); Repeat (4); Sequence conflict (2); Signal peptide (1); Site (1) FUNCTION: Displays low peroxidase activity and is likely to participate in H(2)O(2) metabolism and peroxidative reactions in the cardiovascular system (By similarity). Plays a role in extracellular matrix formation. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:19590037}. Note=Enriched in the peritubular space of fibrotic kidneys. TISSUE SPECIFICITY: Highly expressed in the cardiovascular system. In the embryo, expressed in the corneal epithelial layer. In the adult eyes, expressed in the corneal and lens epithelium. {ECO:0000269|PubMed:18929642, ECO:0000269|PubMed:21907015}. +P35419 PERT_MOUSE Thyroid peroxidase (TPO) (EC 1.11.1.8) 914 101,342 Active site (1); Binding site (2); Chain (1); Disulfide bond (10); Domain (2); Glycosylation (5); Metal binding (6); Sequence conflict (1); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 835 859 Helical. {ECO:0000255}. TOPO_DOM 32 834 Extracellular. {ECO:0000255}.; TOPO_DOM 860 914 Cytoplasmic. {ECO:0000255}. Hormone biosynthesis; thyroid hormone biosynthesis. FUNCTION: Iodination and coupling of the hormonogenic tyrosines in thyroglobulin to yield the thyroid hormones T(3) and T(4). {ECO:0000250|UniProtKB:P09933}. PTM: Heme is covalently bound through a H(2)O(2)-dependent autocatalytic process. Heme insertion is important for the delivery of protein at the cell surface (By similarity). {ECO:0000250}.; PTM: Cleaved in its N-terminal part. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Interacts with DUOX1, DUOX2 and CYBA. {ECO:0000250}. +O70361 PER3_MOUSE Period circadian protein homolog 3 (mPER3) (Circadian clock protein PERIOD 3) 1113 120,911 Beta strand (15); Chain (1); Compositional bias (1); Domain (3); Helix (12); Modified residue (1); Motif (4); Mutagenesis (3); Region (2); Sequence conflict (2); Turn (5) FUNCTION: Originally described as a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, ARNTL/BMAL1, ARNTL2/BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and ARNTL/BMAL1 or ARNTL2/BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-ARNTL/BMAL1|ARNTL2/BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1, NR1D2, RORA, RORB and RORG, which form a second feedback loop and which activate and repress ARNTL/BMAL1 transcription, respectively. Has a redundant role with the other PER proteins PER1 and PER2 and is not essential for the circadian rhythms maintenance. In contrast, plays an important role in sleep-wake timing and sleep homeostasis probably through the transcriptional regulation of sleep homeostasis-related genes, without influencing circadian parameters. Can bind heme. {ECO:0000269|PubMed:11395012, ECO:0000269|PubMed:21957163, ECO:0000269|PubMed:22331899}. PTM: Phosphorylation by CSNK1E is weak and appears to require association with PER1 and translocation to the nucleus. {ECO:0000269|PubMed:11865049, ECO:0000269|PubMed:14701732}.; PTM: Ubiquitinated. {ECO:0000269|PubMed:11865049}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10428031, ECO:0000269|PubMed:11591712, ECO:0000269|PubMed:11865049, ECO:0000269|PubMed:14701732}. Nucleus {ECO:0000269|PubMed:10428031, ECO:0000269|PubMed:11591712, ECO:0000269|PubMed:11865049, ECO:0000269|PubMed:14701732}. Note=Mainly cytoplasmic. Translocates to the nucleus through binding PER1, PER2, CRY1 or CRY2, but not TIMELESS. {ECO:0000269|PubMed:10428031, ECO:0000269|PubMed:11591712, ECO:0000269|PubMed:11865049, ECO:0000269|PubMed:14701732}. SUBUNIT: Homodimer. Component of the circadian core oscillator, which includes the CRY proteins, CLOCK or NPAS2, ARTNL/BMAL1 or ARTNL2/BMAL2, CSNK1D and/or CSNK1E, TIMELESS and the PER proteins. Interacts directly with PER1, PER2, CRY1, CRY2, and TIMELESS; interaction with CRY1 and CRY2 is weak and not rhythmic. Interacts with FBXW11 and BTRC. {ECO:0000269|PubMed:10428031, ECO:0000269|PubMed:11865049, ECO:0000269|PubMed:14564007, ECO:0000269|PubMed:14701732, ECO:0000269|PubMed:15917222, ECO:0000269|PubMed:22331899}. TISSUE SPECIFICITY: Widely expressed. Expressed in heart, brain, lung, liver, skeletal muscle, testis, and at low level in the spleen and kidney. In brain, mainly found in the SCN, hippocampus, piriform cortex, and cerebellum. Lower level of expression in the neocortex. Expression exhibits synchronous oscillations in liver, skeletal muscle and testis. {ECO:0000269|PubMed:14701732, ECO:0000269|PubMed:9655499}. +A2A559 PGAP3_MOUSE Post-GPI attachment to proteins factor 3 (PER1-like domain-containing protein 1) 320 36,528 Alternative sequence (1); Chain (1); Glycosylation (1); Sequence conflict (2); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 99 119 Helical. {ECO:0000255}.; TRANSMEM 136 156 Helical. {ECO:0000255}.; TRANSMEM 170 190 Helical. {ECO:0000255}.; TRANSMEM 199 219 Helical. {ECO:0000255}.; TRANSMEM 224 244 Helical. {ECO:0000255}.; TRANSMEM 258 278 Helical. {ECO:0000255}.; TRANSMEM 280 299 Helical. {ECO:0000255}. TOPO_DOM 24 98 Lumenal. {ECO:0000255}.; TOPO_DOM 120 135 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 157 169 Lumenal. {ECO:0000255}.; TOPO_DOM 191 198 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 220 223 Lumenal. {ECO:0000255}.; TOPO_DOM 245 257 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 279 279 Lumenal. {ECO:0000255}.; TOPO_DOM 300 320 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in the lipid remodeling steps of GPI-anchor maturation. Lipid remodeling steps consist in the generation of 2 saturated fatty chains at the sn-2 position of GPI-anchors proteins. Required for phospholipase A2 activity that removes an acyl-chain at the sn-2 position of GPI-anchors during the remodeling of GPI (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Mainly localizes to Golgi apparatus. {ECO:0000250}. +Q9WVB0 RBPMS_MOUSE RNA-binding protein with multiple splicing (RBP-MS) (Heart and RRM expressed sequence) (Hermes) 197 21,816 Alternative sequence (1); Chain (1); Domain (1); Modified residue (3); Region (1); Sequence conflict (2); Site (2) FUNCTION: Acts as a coactivator of transcriptional activity. Required to increase TGFB1/Smad-mediated transactivation. Acts through SMAD2, SMAD3 and SMAD4 to increase transcriptional activity. Increases phosphorylation of SMAD2 and SMAD3 on their C-terminal SSXS motif, possibly through recruitment of TGFBR1. Promotes the nuclear accumulation of SMAD2, SMAD3 and SMAD4 proteins. Binds to poly(A) RNA. {ECO:0000250|UniProtKB:Q93062}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q93062}. Cytoplasm {ECO:0000250|UniProtKB:Q93062}. Cytoplasm, P-body {ECO:0000250|UniProtKB:Q93062}. Note=Translocates into cytoplasmic stress granules that probably correspond to P-bodies in response to oxidative stress. {ECO:0000250|UniProtKB:Q93062}. SUBUNIT: Homodimer; each protein chain binds one RNA molecule via the external surface of the homodimer. Interacts with SMAD2, SMAD3 and SMAD4; the interactions are direct. {ECO:0000250|UniProtKB:Q93062}. DOMAIN: The RRM domain is necessary for interaction with SMAD4. Both the RRM domain and the C-terminus are required for TGFB1/Smad-mediated transactivation activity (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: mRNA expressed in developing heart, with significantly higher expression in the atria relative to the ventricles. {ECO:0000269|PubMed:10096065}. +Q05793 PGBM_MOUSE Basement membrane-specific heparan sulfate proteoglycan core protein (HSPG) [Cleaved into: Endorepellin; LG3 peptide] 3707 398,294 Beta strand (8); Chain (3); Disulfide bond (69); Domain (41); Glycosylation (13); Helix (2); Metal binding (4); Region (1); Sequence conflict (2); Signal peptide (1); Site (1) FUNCTION: Integral component of basement membranes. Component of the glomerular basement membrane (GBM), responsible for the fixed negative electrostatic membrane charge, and which provides a barrier which is both size- and charge-selective. It serves as an attachment substrate for cells. Plays essential roles in vascularization. Critical for normal heart development and for regulating the vascular response to injury. Also required for avascular cartilage development (By similarity). {ECO:0000250}.; FUNCTION: Endorepellin in an anti-angiogenic and anti-tumor peptide that inhibits endothelial cell migration, collagen-induced endothelial tube morphogenesis and blood vessel growth in the chorioallantoic membrane. Blocks endothelial cell adhesion to fibronectin and type I collagen. Anti-tumor agent in neovascularization. Interaction with its ligand, integrin alpha2/beta1, is required for the anti-angiogenic properties. Evokes a reduction in phosphorylation of receptor tyrosine kinases via alpha2/beta1 integrin-mediated activation of the tyrosine phosphatase, PTPN6 (By similarity). {ECO:0000250}.; FUNCTION: The LG3 peptide has anti-angiogenic properties that require binding of calcium ions for full activity. {ECO:0000250}. PTM: Proteolytic processing produces the C-terminal angiogenic peptide, endorepellin. This peptide can be further processed to produce the LG3 peptide (By similarity). {ECO:0000250}.; PTM: N- and O-glycosylated; contains 3 heparan sulfate chains. The LG3 peptide contains at least three and up to five potential O-glycosylation sites and no N-glycosylation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane. SUBUNIT: Purified perlecan has a strong tendency to aggregate in dimers or stellate structures. It interacts with other basement membrane components such as laminin, prolargin and collagen type IV. Interacts with COL13A1, FGFBP1 and VWA1. Interacts (via C-terminus) with ECM1 (via C-terminus) (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Found in the basement membranes. +P05622 PGFRB_MOUSE Platelet-derived growth factor receptor beta (PDGF-R-beta) (PDGFR-beta) (EC 2.7.10.1) (Beta platelet-derived growth factor receptor) (Beta-type platelet-derived growth factor receptor) (CD140 antigen-like family member B) (Platelet-derived growth factor receptor 1) (PDGFR-1) (CD antigen CD140b) 1098 122,806 Active site (1); Binding site (1); Chain (1); Disulfide bond (4); Domain (6); Glycosylation (11); Modified residue (16); Mutagenesis (8); Nucleotide binding (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 532 552 Helical. {ECO:0000255}. TOPO_DOM 32 531 Extracellular. {ECO:0000255}.; TOPO_DOM 553 1098 Cytoplasmic. {ECO:0000255}. FUNCTION: Tyrosine-protein kinase that acts as cell-surface receptor for homodimeric PDGFB and PDGFD and for heterodimers formed by PDGFA and PDGFB, and plays an essential role in the regulation of embryonic development, cell proliferation, survival, differentiation, chemotaxis and migration. Plays an essential role in blood vessel development by promoting proliferation, migration and recruitment of pericytes and smooth muscle cells to endothelial cells. Plays a role in the migration of vascular smooth muscle cells and the formation of neointima at vascular injury sites. Required for normal development of the cardiovascular system. Required for normal recruitment of pericytes (mesangial cells) in the kidney glomerulus, and for normal formation of a branched network of capillaries in kidney glomeruli. Promotes rearrangement of the actin cytoskeleton and the formation of membrane ruffles. Binding of its cognate ligands - homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or homodimeric PDGFD -leads to the activation of several signaling cascades; the response depends on the nature of the bound ligand and is modulated by the formation of heterodimers between PDGFRA and PDGFRB. Phosphorylates PLCG1, PIK3R1, PTPN11, RASA1/GAP, CBL, SHC1 and NCK1. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate, mobilization of cytosolic Ca(2+) and the activation of protein kinase C. Phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, leads to the activation of the AKT1 signaling pathway. Phosphorylation of SHC1, or of the C-terminus of PTPN11, creates a binding site for GRB2, resulting in the activation of HRAS, RAF1 and down-stream MAP kinases, including MAPK1/ERK2 and/or MAPK3/ERK1. Promotes phosphorylation and activation of SRC family kinases. Promotes phosphorylation of PDCD6IP/ALIX and STAM (By similarity). Receptor signaling is down-regulated by protein phosphatases that dephosphorylate the receptor and its down-stream effectors, and by rapid internalization of the activated receptor. {ECO:0000250, ECO:0000269|PubMed:14624252, ECO:0000269|PubMed:14993293, ECO:0000269|PubMed:15284236, ECO:0000269|PubMed:17620338, ECO:0000269|PubMed:18948621, ECO:0000269|PubMed:19030102, ECO:0000269|PubMed:19742316, ECO:0000269|PubMed:21664579, ECO:0000269|PubMed:8440729}. PTM: Autophosphorylated on tyrosine residues upon ligand binding. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Phosphorylation at Tyr-578, and to a lesser degree, Tyr-580 is important for interaction with SRC. Phosphorylation at Tyr-715 is important for interaction with GRB2. Phosphorylation at Tyr-739 and Tyr-750 is important for interaction with PIK3R1. Phosphorylation at Tyr-750 is important for interaction with NCK1. Phosphorylation at Tyr-770 and Tyr-856 is important for interaction with RASA1/GAP. Phosphorylation at Tyr-856 is important for efficient phosphorylation of PLCG1 and PTPN11, resulting in increased phosphorylation of AKT1, MAPK1/ERK2 and/or MAPK3/ERK1, PDCD6IP/ALIX and STAM, and in increased cell proliferation. Phosphorylation at Tyr-1008 is important for interaction with PTPN11. Phosphorylation at Tyr-1008 and Tyr-1020 is important for interaction with PLCG1. Dephosphorylated by PTPRJ at Tyr-750, Tyr-856, Tyr-1008 and Tyr-1020 (By similarity). Dephosphorylated by PTPN2 at Tyr-578 and Tyr-1020. {ECO:0000250}.; PTM: N-glycosylated. {ECO:0000250}.; PTM: Ubiquitinated. After autophosphorylation, the receptor is polyubiquitinated, leading to its degradation. {ECO:0000269|PubMed:15753096}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Cytoplasmic vesicle {ECO:0000250}. Lysosome lumen {ECO:0000250}. Note=After ligand binding, the autophosphorylated receptor is ubiquitinated and internalized, leading to its degradation. SUBUNIT: Interacts with homodimeric PDGFB and PDGFD, and with heterodimers formed by PDGFA and PDGFB. May also interact with homodimeric PDGFC. Monomer in the absence of bound ligand. Interaction with homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or homodimeric PDGFD, leads to receptor dimerization, where both PDGFRA homodimers and heterodimers with PDGFRB are observed. Interacts with SH2B2/APS. Interacts directly (tyrosine phosphorylated) with SHB. Interacts (tyrosine phosphorylated) with PIK3R1 and RASA1. Interacts (tyrosine phosphorylated) with CBL. Interacts (tyrosine phosphorylated) with SRC and SRC family kinases. Interacts (tyrosine phosphorylated) with PIK3C2B, maybe indirectly. Interacts (tyrosine phosphorylated) with SHC1, GRB7, GRB10 and NCK1. Interaction with GRB2 is mediated by SHC1. Interacts (via C-terminus) with SLC9A3R1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Weakly expressed in glomerular mesangial cells and interstitial cells. Up-regulated in areas of renal fibrosis. In mice with unilateral ureteral obstruction, increased expression in interstitial cells at day 4 and expression is markedly elevated at day 7 and is maximal at day 14. {ECO:0000269|PubMed:14514732}. +Q6PE55 PGFRL_MOUSE Platelet-derived growth factor receptor-like protein (PDGFR-like protein) 375 41,928 Chain (1); Disulfide bond (2); Domain (2); Glycosylation (1); Sequence conflict (3); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. SUBUNIT: Forms a complex composed of PDGFRL, TNK2 and GRB2. {ECO:0000250}. +P53612 PGTB2_MOUSE Geranylgeranyl transferase type-2 subunit beta (EC 2.5.1.60) (Geranylgeranyl transferase type II subunit beta) (GGTase-II-beta) (Rab geranyl-geranyltransferase subunit beta) (Rab GG transferase beta) (Rab GGTase beta) (Rab geranylgeranyltransferase subunit beta) (Type II protein geranyl-geranyltransferase subunit beta) 339 37,803 Beta strand (3); Chain (1); Helix (20); Metal binding (3); Modified residue (1); Region (3); Repeat (6); Sequence conflict (4); Turn (2) FUNCTION: Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of Rab proteins with the C-terminal sequence -XXCC, -XCXC and -CCXX, such as RAB1A, RAB3A, RAB5A and RAB7A. {ECO:0000269|PubMed:21520375}. SUBUNIT: Heterotrimer composed of RABGGTA, RABGGTB and CHM; within this trimer, RABGGTA and RABGGTB form the catalytic component B, while CHM (component A) mediates peptide substrate binding. The Rab GGTase dimer (RGGT) interacts with CHM (component A) prior to Rab protein binding; the association is stabilized by geranylgeranyl pyrophosphate (GGpp). The CHM:RGGT:Rab complex is destabilized by GGpp. Interaction of RABGGTB with prenylated PTP4A2 precludes its association with RABGGTA and inhibits enzyme activity (By similarity). Interacts with CHODL. {ECO:0000250|UniProtKB:P53611, ECO:0000250|UniProtKB:Q08603, ECO:0000269|PubMed:18161010}. TISSUE SPECIFICITY: Ubiquitous. Detected in all the major organs in adult animals. {ECO:0000269|PubMed:9031634}. +Q80UU9 PGRC2_MOUSE Membrane-associated progesterone receptor component 2 217 23,334 Chain (1); Domain (1); Modified residue (5); Transmembrane (1) TRANSMEM 40 62 Helical. {ECO:0000255}. FUNCTION: Receptor for steroids. {ECO:0000305}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. DOMAIN: The cytochrome b5 heme-binding domain lacks the conserved iron-binding His residues at positions 131 and 155. {ECO:0000250}. +P16331 PH4H_MOUSE Phenylalanine-4-hydroxylase (PAH) (EC 1.14.16.1) (Phe-4-monooxygenase) 453 51,900 Chain (1); Domain (1); Initiator methionine (1); Metal binding (3); Modified residue (2); Natural variant (2); Sequence conflict (2) Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 1/6. FUNCTION: Catalyzes the hydroxylation of L-phenylalanine to L-tyrosine. {ECO:0000250|UniProtKB:P00439}. PTM: Phosphorylation at Ser-16 increases basal activity and facilitates activation by the substrate phenylalanine. {ECO:0000250|UniProtKB:P00439}. SUBUNIT: Homodimer and homotetramer. {ECO:0000250|UniProtKB:P04176}. DISEASE: Note=Mouse strains deficient in phenylalanine hydroxylase (Pah) were created as models of phenylketonuria (PKU). {ECO:0000269|PubMed:9119379}. +Q8CHE4 PHLP1_MOUSE PH domain leucine-rich repeat-containing protein phosphatase 1 (EC 3.1.3.16) (Pleckstrin homology domain-containing family E member 1) (PH domain-containing family E member 1) (Suprachiasmatic nucleus circadian oscillatory protein) 1687 182,367 Alternative sequence (1); Chain (1); Compositional bias (8); Domain (2); Frameshift (1); Metal binding (5); Modified residue (3); Motif (1); Repeat (21); Sequence conflict (2) FUNCTION: Protein phosphatase involved in regulation of Akt and PKC signaling. Mediates dephosphorylation in the C-terminal domain hydrophobic motif of members of the AGC Ser/Thr protein kinase family; specifically acts on 'Ser-473' of AKT2 and AKT3, 'Ser-660' of PRKCB and 'Ser-657' of PRKCA (By similarity). Isoform 2 seems to have a major role in regulating Akt signaling in hippocampal neurons (By similarity). Akt regulates the balance between cell survival and apoptosis through a cascade that primarily alters the function of transcription factors that regulate pro- and antiapoptotic genes. Dephosphorylation of 'Ser-473' of Akt triggers apoptosis and suppression of tumor growth. Dephosphorylation of PRKCA and PRKCB leads to their destabilization and degradation. Dephosphorylates STK4 on 'Thr-387' leading to STK4 activation and apoptosis. Dephosphorylates RPS6KB1 and is involved in regulation of cap-dependent translation. Inhibits cancer cell proliferation and may act as a tumor suppressor. Dephosphorylates RAF1 inhibiting its kinase activity. May act as a negative regulator of K-Ras signaling in membrane rafts (By similarity). Involved in the hippocampus-dependent long-term memory formation (PubMed:17382888). Involved in circadian control by regulating the consolidation of circadian periodicity after resetting (PubMed:20080691). Involved in development and function of regulatory T-cells (PubMed:21498666). {ECO:0000250|UniProtKB:O60346, ECO:0000250|UniProtKB:Q9WTR8, ECO:0000269|PubMed:17382888, ECO:0000269|PubMed:20080691, ECO:0000269|PubMed:21498666}. SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein. Nucleus {ECO:0000250}. SUBUNIT: Interacts with the nucleotide free form of K-Ras (KRAS) via its LRR repeats (By similarity). Interacts with AKT2, AKT3 and PRKCB. Interacts with WDR48 and USP12 (By similarity). {ECO:0000250|UniProtKB:O60346, ECO:0000250|UniProtKB:Q9WTR8}. DOMAIN: The PH domain is required for interaction with PRKCB and its dephosphorylation. {ECO:0000250}. TISSUE SPECIFICITY: Isoforms 1 and 2 are expressed in the retina (PubMed:20089132). {ECO:0000269|PubMed:20089132}. +Q9Z1B3 PLCB1_MOUSE 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1 (EC 3.1.4.11) (PLC-154) (Phosphoinositide phospholipase C-beta-1) (Phospholipase C-beta-1) (PLC-beta-1) 1216 138,396 Active site (2); Alternative sequence (2); Chain (1); Compositional bias (1); Domain (3); Modified residue (11); Sequence conflict (33) FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:18802028}. Cytoplasm {ECO:0000250}. Note=Colocalizes with the adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane of cardiac myocytes. {ECO:0000250}. SUBUNIT: Interacts with DGKQ. {ECO:0000250}. +Q5RJI4 PKDCC_MOUSE Extracellular tyrosine-protein kinase PKDCC (EC 2.7.10.2) (Protein kinase domain-containing protein, cytoplasmic) (Protein kinase-like protein SgK493) (Sugen kinase 493) (Vertebrate lonesome kinase) 492 53,841 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Compositional bias (1); Domain (1); Frameshift (1); Glycosylation (5); Modified residue (2); Mutagenesis (4); Nucleotide binding (1); Signal peptide (1) FUNCTION: Secreted tyrosine-protein kinase that mediates phosphorylation of extracellular proteins and endogenous proteins in the secretory pathway, which is essential for patterning at organogenesis stages. Mediates phosphorylation of MMP1, MMP13, MMP14, MMP19 and ERP29 (PubMed:25171405). May also have serine/threonine protein kinase activity (PubMed:25171405). Required for longitudinal bone growth through regulation of chondrocyte differentiation (PubMed:19097194, PubMed:23792766). May be indirectly involved in protein transport from the Golgi apparatus to the plasma membrane (PubMed:19465597). Probably plays a role in platelets: rapidly and quantitatively secreted from platelets in response to stimulation of platelet degranulation (PubMed:25171405). {ECO:0000269|PubMed:19097194, ECO:0000269|PubMed:19465597, ECO:0000269|PubMed:23792766, ECO:0000269|PubMed:25171405}. PTM: Phosphorylated on tyrosines; probably via autophosphorylation. {ECO:0000269|PubMed:25171405}.; PTM: N-glycosylated. {ECO:0000269|PubMed:25171405}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25171405}. Golgi apparatus {ECO:0000269|PubMed:19465597}. Note=Both secreted and present in the Golgi apparatus. {ECO:0000269|PubMed:19465597, ECO:0000269|PubMed:25171405}. TISSUE SPECIFICITY: Strongly expressed in adult heart, liver and testis with weak expression in brain, spleen, lung and thymus. In the humerus, strongly expressed in early flat proliferative chondrocytes. In the embryo, expressed in the anterior visceral endoderm and anterior primitive streak at E6.5. At E7.5, expressed in the anterior definitive endoderm (ADE) and anterior mesoderm but not in the notochord. At E8.0, expressed in the ADE and anterior embryonic mesoderm. At E8.5, expressed more broadly in anterior tissues and at the midline of the neural plate in the midbrain region as well as the lateral margins of the neural plate posterior to the metencephalic region. Also weakly expressed in the anterior mesenchyme. At E9.5, strongest expression in branchial arches and limb buds. During mid-gestation, expression continues in mesenchymal cells, particularly in areas where these cells condense. {ECO:0000269|PubMed:19097194, ECO:0000269|PubMed:19465597}. +Q3UNN8 PLD5_MOUSE Inactive phospholipase D5 (Inactive PLD 5) (Inactive choline phosphatase 5) (Inactive phosphatidylcholine-hydrolyzing phospholipase D5) 536 61,066 Alternative sequence (2); Chain (1); Domain (2); Erroneous termination (1); Glycosylation (2); Topological domain (2); Transmembrane (1) TRANSMEM 69 89 Helical. {ECO:0000255}. TOPO_DOM 1 68 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 90 536 Extracellular. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +P16646 PMP22_MOUSE Peripheral myelin protein 22 (PMP-22) (Growth arrest-specific protein 3) (GAS-3) 161 18,023 Chain (1); Glycosylation (1); Natural variant (2); Sequence conflict (1); Topological domain (5); Transmembrane (4) TRANSMEM 2 31 Helical. {ECO:0000250}.; TRANSMEM 65 91 Helical. {ECO:0000250}.; TRANSMEM 96 119 Helical. {ECO:0000250}.; TRANSMEM 134 156 Helical. {ECO:0000250}. TOPO_DOM 1 1 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 32 64 Extracellular. {ECO:0000255}.; TOPO_DOM 92 95 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 120 133 Extracellular. {ECO:0000255}.; TOPO_DOM 157 160 Cytoplasmic. {ECO:0000255}. FUNCTION: Might be involved in growth regulation, and in myelinization in the peripheral nervous system. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Schwann cells of the peripheral nervous system. DISEASE: Note=A defect in Pmp-22 is the cause of trembler (tr) phenotype. Trembler mice show a Schwann cells defect characterized by severe hypomyelination and continuing Schwann cells proliferation throughout life. {ECO:0000269|PubMed:1374899, ECO:0000269|PubMed:1552943}. +Q9CZG9 PDZ11_MOUSE PDZ domain-containing protein 11 140 16,182 Beta strand (6); Chain (1); Domain (1); Helix (2) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q5EBL8}. SUBUNIT: Interacts with ATP2B1, ATP2B2, ATP2B3, ATP2B4 and ATP7A. {ECO:0000250}. +Q08481 PECA1_MOUSE Platelet endothelial cell adhesion molecule (PECAM-1) (CD antigen CD31) 727 81,263 Alternative sequence (3); Chain (1); Disulfide bond (6); Domain (6); Glycosylation (7); Lipidation (1); Modified residue (4); Motif (2); Mutagenesis (3); Region (2); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 591 609 Helical. {ECO:0000255}. TOPO_DOM 18 590 Extracellular. {ECO:0000255}.; TOPO_DOM 610 727 Cytoplasmic. {ECO:0000255}. FUNCTION: Cell adhesion molecule which is required for leukocyte transendothelial migration (TEM) under most inflammatory conditions (By similarity). Tyr-679 plays a critical role in TEM and is required for efficient trafficking of PECAM1 to and from the lateral border recycling compartment (LBRC) and is also essential for the LBRC membrane to be targeted around migrating leukocytes (By similarity). Trans-homophilic interaction may play a role in endothelial cell-cell adhesion via cell junctions (By similarity). Heterophilic interaction with CD177 plays a role in transendothelial migration of neutrophils (By similarity). Homophilic ligation of PECAM1 prevents macrophage-mediated phagocytosis of neighboring viable leukocytes by transmitting a detachment signal (By similarity). Promotes macrophage-mediated phagocytosis of apoptotic leukocytes by tethering them to the phagocytic cells; PECAM1-mediated detachment signal appears to be disabled in apoptotic leukocytes (By similarity). Modulates bradykinin receptor BDKRB2 activation (By similarity). Regulates bradykinin- and hyperosmotic shock-induced ERK1/2 activation in endothelial cells (By similarity). Induces susceptibility to atherosclerosis (PubMed:19048083). {ECO:0000250|UniProtKB:P16284, ECO:0000269|PubMed:19048083}. PTM: Phosphorylated on Ser and Tyr residues by src kinases after cellular activation (PubMed:16731527). Upon activation, phosphorylated on Ser-718 which probably initiates the dissociation of the membrane-interaction segment (residues 698-718) from the cell membrane allowing the sequential phosphorylation of Tyr-702 and Tyr-679 (By similarity). Constitutively phosphorylated on Ser-723 in resting platelets (By similarity). Phosphorylated on tyrosine residues by FER and FES in response to FCER1 activation (PubMed:16731527). In endothelial cells Fyn mediates mechanical-force (stretch or pull) induced tyrosine phosphorylation (By similarity). {ECO:0000250|UniProtKB:P16284, ECO:0000269|PubMed:16731527}.; PTM: Palmitoylation by ZDHHC21 is necessary for cell surface expression in endothelial cells and enrichment in membrane rafts. {ECO:0000250|UniProtKB:P16284}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P16284}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P16284}. Membrane raft {ECO:0000250|UniProtKB:P16284}. Cell junction {ECO:0000250|UniProtKB:P16284}. Note=Localizes to the lateral border recycling compartment (LBRC) and recycles from the LBRC to the junction in resting endothelial cells. Cell surface expression on neutrophils is down-regulated upon fMLP or CXCL8/IL8-mediated stimulation. {ECO:0000250|UniProtKB:P16284}. SUBUNIT: Trans-homodimer (via Ig-like C2-type 1 and Ig-like C2-type 2 domains); trans-homodimerization is required for cell-cell interaction. Forms a complex with BDKRB2 and GNAQ. Interacts with BDKRB2 and GNAQ. Interacts with PTPN11; Tyr-702 is critical for PTPN11 recruitment. Interacts with FER. Interacts with CD177; the interaction is Ca(2+)-dependent; the interaction is direct. {ECO:0000250|UniProtKB:P16284, ECO:0000250|UniProtKB:P51866}. DOMAIN: The Ig-like C2-type domains 2 and 3 contribute to formation of the complex with BDKRB2 and in regulation of its activity. {ECO:0000250}. TISSUE SPECIFICITY: Isoform 1 and isoform 3 are expressed in lung and platelets. {ECO:0000269|PubMed:18388311}. +Q08024 PEBB_MOUSE Core-binding factor subunit beta (CBF-beta) (Polyomavirus enhancer-binding protein 2 beta subunit) (PEA2-beta) (PEBP2-beta) (SL3-3 enhancer factor 1 subunit beta) (SL3/AKV core-binding factor beta subunit) 187 22,030 Alternative sequence (3); Beta strand (7); Chain (1); Helix (4); Modified residue (2); Mutagenesis (3); Sequence conflict (3); Turn (4) FUNCTION: Forms the heterodimeric complex core-binding factor (CBF) with RUNX family proteins (RUNX1, RUNX2, and RUNX3). RUNX members modulate the transcription of their target genes through recognizing the core consensus binding sequence 5'-TGTGGT-3', or very rarely, 5'-TGCGGT-3', within their regulatory regions via their runt domain, while CBFB is a non-DNA-binding regulatory subunit that allosterically enhances the sequence-specific DNA-binding capacity of RUNX. The heterodimers bind to the core site of a number of enhancers and promoters, including murine leukemia virus, polyomavirus enhancer, T-cell receptor enhancers, LCK, IL3 and GM-CSF promoters (Probable). CBF complexes repress ZBTB7B transcription factor during cytotoxic (CD8+) T cell development. They bind to RUNX-binding sequence within the ZBTB7B locus acting as transcriptional silencer and allowing for cytotoxic T cell differentiation (PubMed:18258917). {ECO:0000269|PubMed:18258917, ECO:0000305|PubMed:11257229, ECO:0000305|PubMed:8386878, ECO:0000305|PubMed:8497254}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Heterodimer with RUNX1, RUNX2 and RUNX3 (Probable). Interacts with COPRS. Found in a complex with PRMT5 and RUNX1 (PubMed:22193545). {ECO:0000269|PubMed:22193545, ECO:0000305|PubMed:11257229}. TISSUE SPECIFICITY: Expressed in all tissues tested. Highest level in thymus, but also abundantly expressed in muscle, lung and brain. +Q80X73 PELO_MOUSE Protein pelota homolog (EC 3.1.-.-) 385 43,349 Chain (1); Cross-link (1); Modified residue (4); Sequence conflict (11) FUNCTION: Required for normal chromosome segregation during cell division and genomic stability. May function in recognizing stalled ribosomes and triggering endonucleolytic cleavage of the mRNA, a mechanism to release non-functional ribosomes and degrade damaged mRNAs. May have ribonuclease activity (Potential). {ECO:0000305}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Cytoplasm {ECO:0000250}. DOMAIN: The N-terminal domain has the RNA-binding Sm fold. It may harbor the endoribonuclease activity (Potential). {ECO:0000305}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:12438745}. +P15331 PERI_MOUSE Peripherin 475 54,268 Alternative sequence (2); Chain (1); Domain (1); Modified residue (5); Region (7) FUNCTION: Class-III neuronal intermediate filament protein. +Q8BP56 PGGHG_MOUSE Protein-glucosylgalactosylhydroxylysine glucosidase (EC 3.2.1.107) (Acid trehalase-like protein 1) 690 76,488 Active site (1); Alternative sequence (4); Chain (1); Compositional bias (1); Erroneous initiation (1); Region (2); Sequence conflict (2) FUNCTION: Catalyzes the hydrolysis of glucose from the disaccharide unit linked to hydroxylysine residues of collagen and collagen-like proteins. {ECO:0000250|UniProtKB:Q32M88}. +Q8VCC1 PGDH_MOUSE 15-hydroxyprostaglandin dehydrogenase [NAD(+)] (15-PGDH) (EC 1.1.1.141) (Prostaglandin dehydrogenase 1) 269 29,181 Active site (1); Binding site (3); Chain (1); Frameshift (1); Nucleotide binding (5); Sequence conflict (8) FUNCTION: Prostaglandin inactivation. Contributes to the regulation of events that are under the control of prostaglandin levels. Catalyzes the NAD-dependent dehydrogenation of lipoxin A4 to form 15-oxo-lipoxin A4 (By similarity). {ECO:0000250, ECO:0000269|PubMed:8950170}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in proximal convoluted tubules of the kidney, where it colocalizes with the prostaglandin transporter SLC22A22 (at protein level) (PubMed:20448048). Expressed in lung, intestine, stomach and liver (PubMed:8950170). {ECO:0000269|PubMed:20448048, ECO:0000269|PubMed:8950170}. +Q8BWM0 PGES2_MOUSE Prostaglandin E synthase 2 (EC 5.3.99.3) (GATE-binding factor 1) (GBF-1) (Microsomal prostaglandin E synthase 2) (mPGES-2) [Cleaved into: Prostaglandin E synthase 2 truncated form] 384 43,324 Binding site (1); Chain (2); Domain (2); Region (1); Sequence conflict (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 57 73 Helical. {ECO:0000255}. TOPO_DOM 1 56 Lumenal. {ECO:0000255}.; TOPO_DOM 74 384 Cytoplasmic. {ECO:0000255}. Lipid metabolism; prostaglandin biosynthesis. FUNCTION: Isomerase that catalyzes the conversion of PGH2 into the more stable prostaglandin E2 (PGE2) (By similarity). May also have transactivation activity toward IFN-gamma (IFNG), possibly via an interaction with CEBPB; however, the relevance of transcription activation activity remains unclear. {ECO:0000250|UniProtKB:Q9H7Z7, ECO:0000303|PubMed:12050152}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9H7Z7}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9H7Z7}. Nucleus {ECO:0000269|PubMed:12050152}. Note=According to PubMed:12050152, some fraction may be nuclear. {ECO:0000269|PubMed:12050152}.; SUBCELLULAR LOCATION: Prostaglandin E synthase 2 truncated form: Cytoplasm {ECO:0000250|UniProtKB:Q9H7Z7}. Note=Synthesized as a Golgi membrane-bound protein, which is further cleaved into the predominant soluble truncated form. {ECO:0000250|UniProtKB:Q9H7Z7}. SUBUNIT: Homodimer. Interacts with EXOSC10 (By similarity). May interact with CEBPB. {ECO:0000250|UniProtKB:Q66LN0, ECO:0000250|UniProtKB:Q9H7Z7, ECO:0000269|PubMed:15879117}. TISSUE SPECIFICITY: Widely expressed. Expressed in brain, heart, liver, colon and lung. {ECO:0000269|PubMed:12050152, ECO:0000269|PubMed:12835322}. +P28654 PGS2_MOUSE Decorin (Bone proteoglycan II) (PG-S2) (PG40) 354 39,809 Chain (1); Compositional bias (1); Disulfide bond (3); Glycosylation (5); Propeptide (1); Repeat (12); Signal peptide (1) FUNCTION: May affect the rate of fibrils formation. PTM: The attached glycosaminoglycan chain can be either chondroitin sulfate or dermatan sulfate depending upon the tissue of origin. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SUBUNIT: Binds to type I and type II collagen, fibronectin and TGF-beta. Forms a ternary complex with MFAP2 and ELN. Interacts with DPT (By similarity). {ECO:0000250}. +Q6PEB6 PHOCN_MOUSE MOB-like protein phocein (Class II mMOB1) (Mob1 homolog 3) (Mob3) (Mps one binder kinase activator-like 3) (Preimplantation protein 3) 225 26,032 Chain (1); Metal binding (4); Sequence conflict (1) FUNCTION: May play a role in membrane trafficking, specifically in membrane budding reactions. PTM: Phosphorylated on serine residues. {ECO:0000269|PubMed:11319234}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:11319234}. Membrane {ECO:0000269|PubMed:11319234}; Peripheral membrane protein {ECO:0000269|PubMed:11319234}. Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:11319234}; Peripheral membrane protein {ECO:0000269|PubMed:11319234}. Note=In a perinuclear punctate pattern. Associated with membranes and the Golgi stacks. SUBUNIT: Binds STRN4 (By similarity). Interacts with DNM1 and EPS15 (By similarity). Interacts with nucleoside diphosphate kinase (By similarity). Binds STRN and STRN3. Part of a ternary complex containing MOB4/PHOCN, STRN and/or STRN3 and PPA2. Interacts with CTTNBP2 and CTTNBP2NL (By similarity). {ECO:0000250}. +Q9CZL5 PHS2_MOUSE Pterin-4-alpha-carbinolamine dehydratase 2 (PHS 2) (EC 4.2.1.96) (4-alpha-hydroxy-tetrahydropterin dehydratase 2) (DcoH-like protein DCoHm) (Dimerization cofactor of hepatocyte nuclear factor 1 from muscle) (HNF-1-alpha dimerization cofactor) 136 14,830 Beta strand (4); Chain (1); Compositional bias (1); Erroneous initiation (2); Helix (3); Modified residue (6); Turn (1) FUNCTION: Involved in tetrahydrobiopterin biosynthesis. Seems to both prevent the formation of 7-pterins and accelerate the formation of quinonoid-BH2 (By similarity). {ECO:0000250}.; FUNCTION: Regulates the dimerization of homeodomain protein HNF-1-alpha and enhances its transcriptional activity. {ECO:0000269|PubMed:15182178}. SUBUNIT: Homotetramer. Interacts with DYRK1B (By similarity). {ECO:0000250}. +P61458 PHS_MOUSE Pterin-4-alpha-carbinolamine dehydratase (PHS) (EC 4.2.1.96) (4-alpha-hydroxy-tetrahydropterin dehydratase) (Dimerization cofactor of hepatocyte nuclear factor 1-alpha) (DCoH) (Dimerization cofactor of HNF1) (Phenylalanine hydroxylase-stimulating protein) (Pterin carbinolamine dehydratase) (PCD) 104 11,986 Chain (1); Initiator methionine (1); Modified residue (1); Region (2) FUNCTION: Involved in tetrahydrobiopterin biosynthesis. Seems to both prevent the formation of 7-pterins and accelerate the formation of quinonoid-BH2. Coactivator for HNF1A-dependent transcription. Regulates the dimerization of homeodomain protein HNF1A and enhances its transcriptional activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Cytoplasmic and/or nuclear. SUBUNIT: Homotetramer and homodimer. Heterotetramer with HNF1A; formed by a dimer of dimers (By similarity). {ECO:0000250}. +Q9QUR7 PIN1_MOUSE Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (EC 5.2.1.8) (Peptidyl-prolyl cis-trans isomerase Pin1) (PPIase Pin1) 165 18,370 Chain (1); Domain (2); Modified residue (3) FUNCTION: Peptidyl-prolyl cis/trans isomerase (PPIase) that binds to and isomerizes specific phosphorylated Ser/Thr-Pro (pSer/Thr-Pro) motifs. By inducing conformational changes in a subset of phosphorylated proteins, acts as a molecular switch in multiple cellular processes. Displays a preference for an acidic residue N-terminal to the isomerized proline bond. Regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Down-regulates kinase activity of BTK. Can transactivate multiple oncogenes and induce centrosome amplification, chromosome instability and cell transformation. Required for the efficient dephosphorylation and recycling of RAF1 after mitogen activation (By similarity). Binds and targets PML and BCL6 for degradation in a phosphorylation-dependent manner (PubMed:17828269). Acts as a regulator of JNK cascade by binding to phosphorylated FBXW7, disrupting FBXW7 dimerization and promoting FBXW7 autoubiquitination and degradation: degradation of FBXW7 leads to subsequent stabilization of JUN (By similarity). May facilitate the ubiquitination and proteasomal degradation of RBBP8/CtIP through CUL3/KLHL15 E3 ubiquitin-protein ligase complex, hence favors DNA double-strand repair through error-prone non-homologous end joining (NHEJ) over error-free, RBBP8-mediated homologous recombination (HR) (By similarity). {ECO:0000250|UniProtKB:Q13526, ECO:0000269|PubMed:17828269}. PTM: Phosphorylation at Ser-73 by DAPK1 results in inhibition of its catalytic activity, nuclear localization, and its ability to induce centrosome amplification, chromosome instability and cell transformation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13526}. Nucleus speckle {ECO:0000250|UniProtKB:Q13526}. Cytoplasm {ECO:0000250|UniProtKB:Q13526}. Note=Colocalizes with NEK6 in the nucleus. Mainly localized in the nucleus but phosphorylation at Ser-73 by DAPK1 results in inhibition of its nuclear localization. {ECO:0000250|UniProtKB:Q13526}. SUBUNIT: Interacts with STIL (PubMed:16024801). Interacts with KIF20B. Interacts with NEK6. Interacts (via WW domain) with PRKX (PubMed:19367327). Interacts with BTK. Interacts (via PpiC domain) with DAPK1. Interacts with the phosphorylated form of RAF1. Interacts (via WW domain) with ATCAY; upon NGF stimulation. Interacts with PML and BCL-6. Interacts with FBXW7, disrupting FBXW7 dimerization and promoting FBXW7 autoubiquitination and degradation (By similarity). Directly interacts with RBBP8/CtIP; this interaction depends upon RBBP8 phosphorylation (By similarity). {ECO:0000250|UniProtKB:Q13526, ECO:0000269|PubMed:16024801, ECO:0000269|PubMed:19367327}. DOMAIN: The WW domain is required for the interaction with STIL and KIF20B. +Q2YFS1 PILB2_MOUSE Paired immunoglobulin-like type 2 receptor beta-2 (Activating receptor PILR-beta-2) 225 25,513 Chain (1); Glycosylation (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 196 216 Helical. {ECO:0000255}. TOPO_DOM 32 195 Extracellular. {ECO:0000255}.; TOPO_DOM 217 225 Cytoplasmic. {ECO:0000255}. FUNCTION: Paired receptors consist of highly related activating and inhibitory receptors and are widely involved in the regulation of the immune system. PILRB2 is probably a cellular signaling activating receptor that associates with ITAM-bearing adapter molecules on the cell surface. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q8BUL6 PKHA1_MOUSE Pleckstrin homology domain-containing family A member 1 (PH domain-containing family A member 1) (Tandem PH domain-containing protein 1) (TAPP-1) 383 43,371 Alternative sequence (2); Chain (1); Domain (2); Modified residue (1) FUNCTION: Binds specifically to phosphatidylinositol 3,4-diphosphate (PtdIns3,4P2), but not to other phosphoinositides. May recruit other proteins to the plasma membrane (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9HB21}. Cell membrane {ECO:0000250|UniProtKB:Q9HB21}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9HB21}. Nucleus {ECO:0000250|UniProtKB:Q9HB21}. Note=Locates to the plasma membrane after treatments that stimulate the production of PtdIns3,4P2. {ECO:0000250|UniProtKB:Q9HB21}. SUBUNIT: Interacts with MPDZ and PTPN13. {ECO:0000250}. DOMAIN: Binds to membranes enriched in PtdIns3,4P2 via the C-terminal PH domain. +Q8VCE9 PKHH3_MOUSE Pleckstrin homology domain-containing family H member 3 (PH domain-containing family H member 3) 796 85,842 Alternative sequence (3); Chain (1); Domain (3); Glycosylation (1); Modified residue (2); Signal peptide (1) +Q3UIL6 PKHA7_MOUSE Pleckstrin homology domain-containing family A member 7 (PH domain-containing family A member 7) (Heart adapter protein 1) 1118 126,742 Alternative sequence (6); Chain (1); Coiled coil (2); Compositional bias (2); Domain (3); Erroneous initiation (1); Frameshift (1); Modified residue (16); Region (1) FUNCTION: Required for zonula adherens biogenesis and maintenance. Acts via its interaction with KIAA1543/Nezha, which anchors microtubules at their minus-ends to zonula adherens, leading to the recruitment of KIFC3 kinesin to the junctional site (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, adherens junction {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Note=Localizes to zonula adherens, recruited via its interaction with CTNND1. {ECO:0000250}. SUBUNIT: Interacts with KIAA1543/Nezha and CTNND1. {ECO:0000250}. +O09049 REG3G_MOUSE Regenerating islet-derived protein 3-gamma (REG-3-gamma) (Pancreatitis-associated protein 3) (Regenerating islet-derived protein III-gamma) (Reg III-gamma) [Cleaved into: Regenerating islet-derived protein 3-gamma 16.5 kDa form; Regenerating islet-derived protein 3-gamma 15 kDa form] 174 19,307 Chain (2); Disulfide bond (3); Domain (1); Motif (1); Propeptide (1); Signal peptide (1) FUNCTION: Bactericidal C-type lectin which acts exclusively against Gram-positive bacteria and mediates bacterial killing by binding to surface-exposed carbohydrate moieties of peptidoglycan. Restricts bacterial colonization of the intestinal epithelial surface and consequently limits activation of adaptive immune responses by the microbiota. The uncleaved form has bacteriostatic activity, whereas the cleaved form has bactericidal activity against L.monocytogenes and methicillin-resistant S.aureus. Regulates keratinocyte proliferation and differentiation after skin injury. {ECO:0000269|PubMed:16504538, ECO:0000269|PubMed:16931762, ECO:0000269|PubMed:17635956, ECO:0000269|PubMed:19095652, ECO:0000269|PubMed:21998396, ECO:0000269|PubMed:22727489, ECO:0000269|PubMed:23401489}. PTM: Proteolytic processing by trypsin removes an inhibitory N-terminal propeptide and is essential for peptidoglycan binding and antibacterial activity. {ECO:0000269|PubMed:19095652}. SUBCELLULAR LOCATION: Secreted. Cytoplasm {ECO:0000250}. DOMAIN: The EPN motif is essential for recognition of the peptidoglycan carbohydrate backbone and for efficient bacterial killing with Glu-114 playing a key role in peptidoglycan binding and bactericidal activity. {ECO:0000250}. TISSUE SPECIFICITY: Predominantly expressed in the small intestine, including Paneth cells (at protein level). Hardly detectable in the colon (at protein level). Highly expressed in the lung epithelium during methicillin-resistant S.aureus infection (at protein level). Skin injury increases its epidermal expression. Also expressed in the pancreas. {ECO:0000269|PubMed:16504538, ECO:0000269|PubMed:16931762, ECO:0000269|PubMed:17635956, ECO:0000269|PubMed:21998396, ECO:0000269|PubMed:22727489, ECO:0000269|PubMed:23401489, ECO:0000269|PubMed:9055810}. +Q91WB4 PKHF2_MOUSE Pleckstrin homology domain-containing family F member 2 (PH domain-containing family F member 2) 249 27,755 Chain (1); Domain (1); Modified residue (4); Zinc finger (1) FUNCTION: May play a role in early endosome fusion upstream of RAB5, hence regulating receptor trafficking and fluid-phase transport (By similarity). Enhances cellular sensitivity to TNF-induced apoptosis. {ECO:0000250, ECO:0000269|PubMed:18288467}. SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000250|UniProtKB:Q9H8W4}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9H8W4}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9H8W4}. Note=Colocalizes with EEA1 and RAB5 at endosomal membrane fusion hot spots. May translocate to the endoplasmic reticulum in the early phase of apoptosis. {ECO:0000250|UniProtKB:Q9H8W4}. SUBUNIT: May interact with EEA1. {ECO:0000250}. DOMAIN: The PH and FYVE domains may be important for TNF-induced localization to the endoplasmic reticulum and for enhanced cellular sensitivity to TNF-induced apoptosis. The FYVE domain is important for binding to the endosomal membrane (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain, stomach and thymus, as well as in kidney, spleen, and skeletal muscle. Also expressed in peripheral blood mononuclear cells and dendritic cells. {ECO:0000269|PubMed:18288467}. +Q8BW88 PKHS1_MOUSE Pleckstrin homology domain-containing family S member 1 (PH domain-containing family S member 1) 474 53,077 Alternative sequence (5); Chain (1); Domain (1); Erroneous initiation (1); Sequence conflict (3) +Q8CGT6 PIWL4_MOUSE Piwi-like protein 4 (mAgo5) 848 95,773 Alternative sequence (2); Chain (1); Domain (2); Erroneous gene model prediction (2); Frameshift (1); Mutagenesis (1); Sequence conflict (2) FUNCTION: Plays a central role during spermatogenesis by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity (PubMed:17395546, PubMed:18381894, PubMed:18922463, PubMed:26669262, PubMed:22020280). Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons (PubMed:17395546, PubMed:18381894, PubMed:18922463, PubMed:26669262, PubMed:22020280). Directly binds piRNAs, a class of 24 to 30 nucleotide RNAs that are generated by a Dicer-independent mechanism and are primarily derived from transposons and other repeated sequence elements. Associates with secondary piRNAs antisense and PIWIL2/MILI is required for such association (PubMed:17395546, PubMed:18381894, PubMed:18922463, PubMed:26669262, PubMed:22020280). The piRNA process acts upstream of known mediators of DNA methylation (PubMed:17395546, PubMed:18381894, PubMed:18922463, PubMed:26669262, PubMed:22020280). Does not show endonuclease activity (PubMed:22020280). Plays a key role in the piRNA amplification loop, also named ping-pong amplification cycle, by acting as a 'slicer-incompetent' component that loads cleaved piRNAs from the 'slicer-competent' component PIWIL2 and target them on genomic transposon loci in the nucleus (PubMed:22020280). In addition to its role in germline, PIWIL4 also plays a role in the regualtion of somatic cells activities. Plays a role in pancreatic beta cell function and insulin secretion (By similarity). Involved in maintaining cell morphology and functional integrity of retinal epithelial through Akt/GSK3alpha/beta signaling pathway (By similarity). {ECO:0000250|UniProtKB:Q4G033, ECO:0000250|UniProtKB:Q7Z3Z4, ECO:0000269|PubMed:17395546, ECO:0000269|PubMed:18381894, ECO:0000269|PubMed:18922463, ECO:0000269|PubMed:22020280, ECO:0000269|PubMed:26669262}. PTM: Arginine methylation by PRMT5 is required for the interaction with Tudor domain-containing protein (TDRD1, TDRKH/TDRD2 and TDRD9) and subsequent localization to the meiotic nuage, also named P granule. {ECO:0000269|PubMed:19584108}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18922463}. Cytoplasm {ECO:0000269|PubMed:18922463, ECO:0000269|PubMed:19465913, ECO:0000269|PubMed:19584108}. Note=Probable component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis. PIWIL2/MILI is required for nuclear localization. {ECO:0000269|PubMed:18922463, ECO:0000269|PubMed:19465913, ECO:0000269|PubMed:19584108}. SUBUNIT: Interacts with PRMT5 and WDR77 (PubMed:19584108). Interacts (when methylated on arginine residues) with TDRD1, TDRKH/TDRD2 and TDRD9 (PubMed:19584108, PubMed:23714778). Interacts with MOV10L1 (PubMed:20534472, PubMed:20547853). {ECO:0000269|PubMed:19584108, ECO:0000269|PubMed:20534472, ECO:0000269|PubMed:20547853, ECO:0000269|PubMed:23714778}. TISSUE SPECIFICITY: Detected in male germ cells beginning around 14.5-15.5 dpc but is absent from female germ cells (PubMed:18922463, PubMed:25038252). From 15.5 dpc and until birth, it is present in male germ cells. Not detected in somatic cells of the embryonic gonad. Expression declines soon after birth, reaching undetectable levels in 4 day-old mice (at protein level). {ECO:0000269|PubMed:18922463, ECO:0000269|PubMed:25038252}. +Q9JLG4 PK2L2_MOUSE Polycystic kidney disease 2-like 2 protein (Polycystin-2L2) (Polycystin-L2) 621 73,683 Chain (1); Coiled coil (1); Glycosylation (2); Sequence conflict (2); Topological domain (7); Transmembrane (6) TRANSMEM 32 52 Helical. {ECO:0000255}.; TRANSMEM 278 298 Helical. {ECO:0000255}.; TRANSMEM 315 335 Helical. {ECO:0000255}.; TRANSMEM 361 381 Helical. {ECO:0000255}.; TRANSMEM 407 427 Helical. {ECO:0000255}.; TRANSMEM 469 489 Helical. {ECO:0000255}. TOPO_DOM 1 31 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 53 277 Extracellular. {ECO:0000255}.; TOPO_DOM 299 314 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 336 360 Extracellular. {ECO:0000255}.; TOPO_DOM 382 406 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 428 468 Extracellular. {ECO:0000255}.; TOPO_DOM 490 621 Cytoplasmic. {ECO:0000255}. FUNCTION: May function as a subunit of a cation channel and play a role in fertilization. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed only in testis and heart. +Q0ZLH2 PJVK_MOUSE Pejvakin (Autosomal recessive deafness type 59 protein homolog) 352 39,858 Chain (1); Mutagenesis (1) FUNCTION: Essential in the activity of auditory pathway neurons. TISSUE SPECIFICITY: In ear, it is detected in the organ of Corti and the spiral ganglion within the cochlea in the sensory areas of the vestibule (cristae ampullares of the semicircular ducts, and maculae of the saccule and utricle) and in the first 3 relays (cochlear nuclei, superior olivary complex and inferior colliculus) of the afferent auditory pathway. In the afferent auditory pathway, it is present in the cell bodies of neurons but not in fiber bundles such as the trapezoid body in the brainstem. Also detected in spiral ganglion cells, which form the auditory nerve and project to the cochlear nuclei in the brainstem. Also present in the cochlear nuclei, the superior olive and the inferior colliculus (at protein level). Expressed in all the adult organs tested: brain, eye, inner ear, heart, lung, kidney, liver, intestine, testis and weakly in skeletal muscle. {ECO:0000269|PubMed:16804542}. +Q5SWZ9 PLD6_MOUSE Mitochondrial cardiolipin hydrolase (EC 3.1.-.-) (Choline phosphatase 6) (Mitochondrial phospholipase) (MitoPLD) (Phosphatidylcholine-hydrolyzing phospholipase D6) (Phospholipase D6) (PLD 6) (Protein zucchini homolog) (mZuc) 221 25,041 Active site (3); Alternative sequence (2); Beta strand (9); Chain (1); Domain (1); Helix (5); Mutagenesis (1); Region (1); Topological domain (2); Transmembrane (1); Turn (2); Zinc finger (1) TRANSMEM 5 27 Helical. {ECO:0000255}. TOPO_DOM 1 4 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 28 221 Cytoplasmic. {ECO:0000255}. FUNCTION: Endonuclease that plays a critical role in PIWI-interacting RNA (piRNA) biogenesis during spermatogenesis. piRNAs provide essential protection against the activity of mobile genetic elements. piRNA-mediated transposon silencing is thus critical for maintaining genome stability, in particular in germline cells when transposons are mobilized as a consequence of wide-spread genomic demethylation (PubMed:23064227, PubMed:23064230). Has been proposed to act as a cardiolipin hydrolase to generate phosphatidic acid at mitochondrial surface (PubMed:21397847, PubMed:21397848). Although it cannot be excluded that it can act as a phospholipase in some circumstances, it should be noted that cardiolipin hydrolase activity is either undetectable in vitro, or very low. In addition, cardiolipin is almost exclusively found on the inner mitochondrial membrane, while PLD6 localizes to the outer mitochondrial membrane, facing the cytosol. Has been shown to be a backbone-non-specific, single strand-specific nuclease, cleaving either RNA or DNA substrates with similar affinity (PubMed:23064227, PubMed:23064230). Produces 5' phosphate and 3' hydroxyl termini, suggesting it could directly participate in the processing of primary piRNA transcripts (PubMed:23064230). Also acts as a regulator of mitochondrial shape through facilitating mitochondrial fusion (By similarity). {ECO:0000250|UniProtKB:Q8N2A8, ECO:0000269|PubMed:21397847, ECO:0000269|PubMed:21397848, ECO:0000269|PubMed:23064227, ECO:0000269|PubMed:23064230}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:21397847}; Single-pass membrane protein {ECO:0000269|PubMed:21397847}. SUBUNIT: Homodimer (PubMed:23064227). Interacts with MOV10L1 (PubMed:25762440). Interacts with MIGA1 and MIGA2; possibly facilitating homodimer formation (By similarity). {ECO:0000250|UniProtKB:Q8N2A8, ECO:0000269|PubMed:23064227, ECO:0000269|PubMed:25762440}. DOMAIN: In contrast to other members of the phospholipase D family, contains only one PLD phosphodiesterase domain, suggesting that it has a single half-catalytic and requires homodimerization to form a complete active site. {ECO:0000250|UniProtKB:Q8N2A8}. TISSUE SPECIFICITY: Predominantly expressed in testis (at protein level). Also expressed at high levels in growing ovary. {ECO:0000269|PubMed:21397847}. +Q8K3R3 PLCD4_MOUSE 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-4 (EC 3.1.4.11) (Phosphoinositide phospholipase C-delta-4) (Phospholipase C-delta-4) (PLC-delta-4) 807 92,694 Active site (2); Alternative sequence (4); Binding site (4); Calcium binding (2); Chain (1); Compositional bias (1); Domain (7); Metal binding (8); Motif (1); Region (1); Sequence conflict (7) FUNCTION: Hydrolyzes the phosphatidylinositol 4,5-bisphosphate (PIP2) to generate 2 second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). DAG mediates the activation of protein kinase C (PKC), while IP3 releases Ca(2+) from intracellular stores. Required for acrosome reaction in sperm during fertilization, probably by acting as an important enzyme for intracellular Ca(2+) mobilization in the zona pellucida-induced acrosome reaction. May play a role in cell growth. Modulates the liver regeneration in cooperation with nuclear PKC. Overexpression up-regulates the Erk signaling pathway and proliferation. {ECO:0000269|PubMed:11340203, ECO:0000269|PubMed:12695499, ECO:0000269|PubMed:16998201}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Note=Localizes primarily to intracellular membranes mostly to the endoplasmic reticulum. {ECO:0000250}. SUBUNIT: Interacts with GRIP1. {ECO:0000269|PubMed:16272139}. DOMAIN: The PDZ-binding motif mediates the interaction with GRIP1.; DOMAIN: The C2 domain mediates pre-localization to the membrane prior to Ca(2+) import and non-selective Ca(2+)-mediated targeting to various cellular membranes. {ECO:0000250}.; DOMAIN: The PH domain is not a critical determinant of the membrane localization. {ECO:0000250}. +O35245 PKD2_MOUSE Polycystin-2 (Polycystic kidney disease 2 protein homolog) (Transient receptor potential cation channel subfamily P member 2) 966 108,982 Alternative sequence (6); Calcium binding (1); Chain (1); Coiled coil (1); Compositional bias (2); Disulfide bond (1); Domain (1); Glycosylation (5); Intramembrane (1); Metal binding (5); Modified residue (7); Motif (1); Mutagenesis (4); Region (2); Sequence conflict (10); Topological domain (8); Transmembrane (6) INTRAMEM 630 644 Pore-forming. {ECO:0000250|UniProtKB:Q13563}. TRANSMEM 218 239 Helical; Name=S1. {ECO:0000250|UniProtKB:Q13563}.; TRANSMEM 467 487 Helical; Name=S2. {ECO:0000250|UniProtKB:Q13563}.; TRANSMEM 504 524 Helical; Name=S3. {ECO:0000250|UniProtKB:Q13563}.; TRANSMEM 551 571 Helical; Name=S4. {ECO:0000250|UniProtKB:Q13563}.; TRANSMEM 596 617 Helical; Name=5. {ECO:0000250|UniProtKB:Q13563}.; TRANSMEM 653 673 Helical; Name=S6. {ECO:0000250|UniProtKB:Q13563}. TOPO_DOM 1 217 Cytoplasmic. {ECO:0000250|UniProtKB:Q13563}.; TOPO_DOM 240 466 Extracellular. {ECO:0000250|UniProtKB:Q13563}.; TOPO_DOM 488 503 Cytoplasmic. {ECO:0000250|UniProtKB:Q13563}.; TOPO_DOM 525 550 Extracellular. {ECO:0000250|UniProtKB:Q13563}.; TOPO_DOM 572 595 Cytoplasmic. {ECO:0000250|UniProtKB:Q13563}.; TOPO_DOM 618 629 Extracellular. {ECO:0000250|UniProtKB:Q13563}.; TOPO_DOM 645 652 Extracellular. {ECO:0000250|UniProtKB:Q13563}.; TOPO_DOM 674 966 Cytoplasmic. {ECO:0000250|UniProtKB:Q13563}. FUNCTION: Component of a heteromeric calcium-permeable ion channel formed by PKD1 and PKD2 that is activated by interaction between PKD1 and a Wnt family member, such as WNT3A and WNT9B. Can also form a functional, homotetrameric ion channel (PubMed:27214281). Functions as a cation channel involved in fluid-flow mechanosensation by the primary cilium in renal epithelium (PubMed:12514735, PubMed:18695040, PubMed:27760766). Functions as outward-rectifying K(+) channel, but is also permeable to Ca(2+), and to a much lesser degree also to Na(+) (PubMed:27760766). May contribute to the release of Ca(2+) stores from the endoplasmic reticulum (By similarity). Together with TRPV4, forms mechano- and thermosensitive channels in cilium (PubMed:18695040). PKD1 and PKD2 may function through a common signaling pathway that is necessary to maintain the normal, differentiated state of renal tubule cells (PubMed:9568711, PubMed:10615132). Acts as a regulator of cilium length, together with PKD1. The dynamic control of cilium length is essential in the regulation of mechanotransductive signaling. The cilium length response creates a negative feedback loop whereby fluid shear-mediated deflection of the primary cilium, which decreases intracellular cAMP, leads to cilium shortening and thus decreases flow-induced signaling (PubMed:20096584). Also involved in left-right axis specification via its role in sensing nodal flow; forms a complex with PKD1L1 in cilia to facilitate flow detection in left-right patterning (PubMed:21307093, PubMed:22983710). Detection of asymmetric nodal flow gives rise to a Ca(2+) signal that is required for normal, asymmetric expression of genes involved in the specification of body left-right laterality (PubMed:12062060, PubMed:21307093, PubMed:22983710). {ECO:0000250|UniProtKB:Q13563, ECO:0000269|PubMed:12062060, ECO:0000269|PubMed:12514735, ECO:0000269|PubMed:18695040, ECO:0000269|PubMed:20096584, ECO:0000269|PubMed:21307093, ECO:0000269|PubMed:22983710, ECO:0000269|PubMed:27214281, ECO:0000269|PubMed:27760766, ECO:0000305|PubMed:10615132, ECO:0000305|PubMed:9568711}. PTM: N-glycosylated (PubMed:11854751). The four subunits in a tetramer probably differ in the extent of glycosylation; simultaneous glycosylation of all experimentally validated sites would probably create steric hindrance (By similarity). {ECO:0000250|UniProtKB:Q13563, ECO:0000269|PubMed:11854751}.; PTM: Phosphorylated (PubMed:16551655). Phosphorylation is important for protein function; a mutant that lacks the N-terminal phosphorylation sites cannot complement a zebrafish pkd2-deficient mutant. PKD-mediated phosphorylation at the C-terminus regulates its function in the release of Ca(2+) stores from the endoplasmic reticulum. PKA-mediated phosphorylation at a C-terminal site strongly increases the open probability of the channel, but does not increase single channel conductance. {ECO:0000250|UniProtKB:Q13563, ECO:0000269|PubMed:16551655}. SUBCELLULAR LOCATION: Cell projection, cilium membrane {ECO:0000269|PubMed:12514735, ECO:0000269|PubMed:18695040, ECO:0000269|PubMed:21307093, ECO:0000269|PubMed:22983710, ECO:0000269|PubMed:25405894, ECO:0000269|PubMed:27760766}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q13563}. Cell membrane {ECO:0000269|PubMed:16551655, ECO:0000269|PubMed:27214281}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q13563}. Basolateral cell membrane {ECO:0000269|PubMed:10770959, ECO:0000269|PubMed:9568711}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q13563}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:10770959, ECO:0000269|PubMed:16551655, ECO:0000269|PubMed:9568711}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:11854751, ECO:0000269|PubMed:25405894, ECO:0000305|PubMed:10913159}. Golgi apparatus {ECO:0000269|PubMed:25405894}. Note=PKD2 localization to the plasma and ciliary membranes requires PKD1. PKD1:PKD2 interaction is required to reach the Golgi apparatus form endoplasmic reticulum and then traffic to the cilia (PubMed:25405894). Detected on kidney tubule basolateral membranes and basal cytoplasmic vesicles (PubMed:9568711, PubMed:10770959). Retained in the endoplasmic reticulum by interaction with PACS1 and PACS2. Cilium localization requires GANAB (By similarity). {ECO:0000250|UniProtKB:Q13563, ECO:0000269|PubMed:10770959, ECO:0000269|PubMed:25405894, ECO:0000269|PubMed:9568711}. SUBUNIT: Homotetramer. Heterotetramer with PKD1, giving rise to a complex formed by one PKD1 chain and three PKD2 chains (By similarity). Interaction with PKD1 is required for ciliary localization (PubMed:25405894). Isoform 1 interacts with PKD1 while isoform 3 does not (PubMed:16192288). Interacts with PKD1L1 (PubMed:21307093, PubMed:22983710). PKD1 requires the presence of PKD2 for stable expression (PubMed:16192288). Interacts with CD2AP (PubMed:10913159). Interacts with HAX1 (PubMed:10760273). Interacts with NEK8 (PubMed:18235101). Part of a complex containing AKAP5, ADCY5, ADCY6 and PDE4C (PubMed:21670265). Interacts (via C-terminus) with TRPV4 (via C-terminus) (PubMed:18695040). Interacts (via C-terminal acidic region) with PACS1 and PACS2; these interactions retain the protein in the endoplasmic reticulum and prevent trafficking to the cell membrane (PubMed:15692563). {ECO:0000250|UniProtKB:Q13563, ECO:0000269|PubMed:10760273, ECO:0000269|PubMed:10913159, ECO:0000269|PubMed:15692563, ECO:0000269|PubMed:16192288, ECO:0000269|PubMed:18235101, ECO:0000269|PubMed:18695040, ECO:0000269|PubMed:21307093, ECO:0000269|PubMed:21670265, ECO:0000269|PubMed:25405894}. DOMAIN: The C-terminal coiled-coil domain is involved in oligomerization and the interaction with PKD1. The isolated coiled-coil domain forms a homotrimer in vitro; the homotrimer interacts with a single PKD1 chain. The coiled-coil domain binds calcium and undergoes a calcium-induced conformation change (in vitro). {ECO:0000250|UniProtKB:Q13563}. TISSUE SPECIFICITY: Detected in kidney epithelium (at protein level) (PubMed:9568711, PubMed:10770959, PubMed:11854751). Highly expressed on basolateral membranes in distal convoluted tubules and medullary thick ascending limbs of Henle (PubMed:9568711). Detected at much lower levels in cortical and medullary collecting tubules, and not detected in the glomerular tuft, in thin limbs of Henle, interstitium and blood vessels (at protein level) (PubMed:9568711). Expressed in mesenchymally derived structures in the developing embryo at day 12.5. Isoform 1 is predominantly expressed in kidney at all developmental stages with high levels also detected in lung. Isoform 3 shows highest expression in brain with lower expression in kidney and lung, low levels in thymus and is hardly detectable in liver. {ECO:0000269|PubMed:10770959, ECO:0000269|PubMed:11854751, ECO:0000269|PubMed:16192288, ECO:0000269|PubMed:21307093, ECO:0000269|PubMed:9568711, ECO:0000269|PubMed:9716661}. +O88492 PLIN4_MOUSE Perilipin-4 (Adipocyte protein S3-12) 1403 139,415 Alternative sequence (2); Chain (1); Erroneous initiation (2); Modified residue (4); Region (1); Repeat (29); Sequence conflict (3) FUNCTION: May play a role in triacylglycerol packaging into adipocytes. May function as a coat protein involved in the biogenesis of lipid droplets. {ECO:0000269|PubMed:12840023, ECO:0000269|PubMed:15731108}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9624692}. Cytoplasm {ECO:0000269|PubMed:12840023, ECO:0000269|PubMed:15731108}. Lipid droplet {ECO:0000269|PubMed:12840023, ECO:0000269|PubMed:15731108}. Note=Nascent lipid droplet surface-associated; association with lipid droplets is triacylglycerol synthesis-dependent. {ECO:0000269|PubMed:12840023, ECO:0000269|PubMed:15731108}. TISSUE SPECIFICITY: Specifically expressed in white adipose tissue and also weakly detected in heart and skeletal muscle (at protein level). {ECO:0000269|PubMed:12840023, ECO:0000269|PubMed:15111493, ECO:0000269|PubMed:9624692}. +Q9CYY7 PLD3B_MOUSE PRELI domain containing protein 3B (Protein slowmo homolog 2) 195 21,492 Chain (1); Domain (1); Modified residue (2); Sequence conflict (1) +Q9D517 PLCC_MOUSE 1-acyl-sn-glycerol-3-phosphate acyltransferase gamma (EC 2.3.1.51) (1-acylglycerol-3-phosphate O-acyltransferase 3) (1-AGP acyltransferase 3) (1-AGPAT 3) (Lysophosphatidic acid acyltransferase gamma) (LPAAT-gamma) 376 43,296 Chain (1); Erroneous initiation (1); Motif (1); Mutagenesis (3); Sequence conflict (3); Topological domain (3); Transmembrane (2) TRANSMEM 125 145 Helical. {ECO:0000255}.; TRANSMEM 317 339 Helical. {ECO:0000255}. TOPO_DOM 1 124 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 146 316 Lumenal. {ECO:0000255}.; TOPO_DOM 340 376 Cytoplasmic. {ECO:0000255}. Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3. FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone (PubMed:15367102). Acts on LPA containing saturated or unsaturated fatty acids C16:0-C20:4 at the sn-1 position using C18:1, C20:4 or C18:2-CoA as the acyl donor. Also acts on lysophosphatidylcholine, lysophosphatidylinositol and lysophosphatidylserine using C18:1 or C20:4-CoA (By similarity). Has a preference for arachidonoyl-CoA as a donor (PubMed:19114731). Has also a modest lysophosphatidylinositol acyltransferase (LPIAT) activity, converts lysophosphatidylinositol (LPI) into phosphatidylinositol (PubMed:19114731). {ECO:0000250|UniProtKB:Q9NRZ7, ECO:0000269|PubMed:15367102, ECO:0000269|PubMed:19114731}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19114731}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9NRZ7}. Nucleus envelope {ECO:0000250}. DOMAIN: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate. {ECO:0000305|PubMed:19114731}. TISSUE SPECIFICITY: Widely expressed. Mainly expressed in testis, kidney and liver (at protein level). {ECO:0000269|PubMed:19114731}. +Q91ZV7 PLDX1_MOUSE Plexin domain-containing protein 1 (Tumor endothelial marker 7) 500 55,635 Alternative sequence (1); Chain (1); Glycosylation (6); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 427 447 Helical. {ECO:0000255}. TOPO_DOM 20 426 Extracellular. {ECO:0000255}.; TOPO_DOM 448 500 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a critical role in endothelial cell capillary morphogenesis. {ECO:0000269|PubMed:16202431}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Cell junction, tight junction {ECO:0000250}. Note=Localized predominantly at the tight junctions of vascular endothelial cells and to a lesser extent at the luminal surface of vascular endothelial cells. {ECO:0000250}. SUBUNIT: Interacts with NID1. May interact with CTTN. {ECO:0000269|PubMed:15574754, ECO:0000269|PubMed:16574105}. TISSUE SPECIFICITY: Detected in brain. Highly expressed in Purkinje cells of the cerebellum. {ECO:0000269|PubMed:11559528}. +Q9Z239 PLM_MOUSE Phospholemman (FXYD domain-containing ion transport regulator 1) (Sodium/potassium-transporting ATPase subunit FXYD1) 92 10,323 Chain (1); Lipidation (2); Modified residue (5); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 36 56 Helical. {ECO:0000255}. TOPO_DOM 21 35 Extracellular. {ECO:0000255}.; TOPO_DOM 57 92 Cytoplasmic. {ECO:0000255}. FUNCTION: Associates with and regulates the activity of the sodium/potassium-transporting ATPase (NKA) which transports Na(+) out of the cell and K(+) into the cell (PubMed:15563542, PubMed:18065526). Inhibits NKA activity in its unphosphorylated state and stimulates activity when phosphorylated (By similarity). Reduces glutathionylation of the NKA beta-1 subunit ATP1B1, thus reversing glutathionylation-mediated inhibition of ATP1B1 (PubMed:21454534). Contributes to female sexual development by maintaining the excitability of neurons which secrete gonadotropin-releasing hormone (PubMed:19187398). {ECO:0000250|UniProtKB:O08589, ECO:0000250|UniProtKB:P56513, ECO:0000269|PubMed:19187398, ECO:0000269|PubMed:21454534}. PTM: Major plasma membrane substrate for cAMP-dependent protein kinase (PKA) and protein kinase C (PKC) in several different tissues. Phosphorylated in response to insulin and adrenergic stimulation. Phosphorylation at Ser-88 stimulates sodium/potassium-transporting ATPase activity while the unphosphorylated form inhibits sodium/potassium-transporting ATPase activity. Phosphorylation increases tetramerization, decreases binding to ATP1A1 and reduces inhibition of ATP1A1 activity. Phosphorylation at Ser-83 leads to greatly reduced interaction with ATP1A1, ATP1A2 and ATP1A3. May be phosphorylated by DMPK. {ECO:0000250|UniProtKB:O00168, ECO:0000250|UniProtKB:O08589, ECO:0000250|UniProtKB:P56513}.; PTM: Palmitoylation increases half-life and stability and is enhanced upon phosphorylation at Ser-88 by PKA. {ECO:0000250|UniProtKB:O00168}. SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P56513}; Single-pass type I membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:O08589}; Single-pass type I membrane protein {ECO:0000255}. Membrane, caveola {ECO:0000250|UniProtKB:O08589}. Cell membrane, sarcolemma, T-tubule {ECO:0000250|UniProtKB:O08589}. Note=Detected in the apical cell membrane in brain. In myocytes, localizes to sarcolemma, t-tubules and intercalated disks. {ECO:0000250|UniProtKB:O08589}. SUBUNIT: Homotetramer (By similarity). Monomer (By similarity). Regulatory subunit of the sodium/potassium-transporting ATPase (NKA) which is composed of a catalytic alpha subunit, a non-catalytic beta subunit and an additional regulatory subunit (By similarity). The monomeric form associates with NKA while the oligomeric form does not (PubMed:23532852). Interacts with the catalytic alpha-1 subunit ATP1A1 (PubMed:17283221). Also interacts with the catalytic alpha-2 and alpha-3 subunits ATP1A2 and ATP1A3 (By similarity). Very little interaction with the catalytic alpha subunits ATP1A1, ATP1A2 or ATP1A3 when phosphorylated at Ser-83 (By similarity). Interacts with the non-catalytic beta-1 subunit ATP1B1 (By similarity). Oxidative stress decreases interaction with ATP1A1 but increases interaction with ATP1B1 (By similarity). {ECO:0000250|UniProtKB:O00168, ECO:0000250|UniProtKB:O08589, ECO:0000250|UniProtKB:Q3SZX0, ECO:0000269|PubMed:17283221, ECO:0000269|PubMed:23532852}. DOMAIN: The cytoplasmic domain is sufficient to regulate sodium/potassium-transporting ATPase activity. {ECO:0000250|UniProtKB:O08589}. +B2RXA1 PLCX2_MOUSE PI-PLC X domain-containing protein 2 340 38,618 Active site (2); Chain (1); Domain (1) SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q0VAA5}. TISSUE SPECIFICITY: Expressed at highest levels in brain, followed by stomach and small intestine. Detected at low levels in kidney, ey, thymus and slkeletal muscle. {ECO:0000269|PubMed:22732399}. +Q9R0E1 PLOD3_MOUSE Multifunctional procollagen lysine hydroxylase and glycosyltransferase LH3 [Includes: Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3 (EC 1.14.11.4) (Lysyl hydroxylase 3) (LH3); Procollagen glycosyltransferase (EC 2.4.1.50) (EC 2.4.1.66) (Galactosylhydroxylysine-glucosyltransferase) (Procollagen galactosyltransferase) (Procollagen glucosyltransferase)] 741 84,922 Binding site (4); Chain (1); Disulfide bond (3); Domain (1); Glycosylation (3); Metal binding (6); Mutagenesis (1); Region (6); Sequence conflict (1); Signal peptide (1) FUNCTION: Multifunctional enzyme that catalyzes a series of post-translational modifications on Lys residues in procollagen (PubMed:16447251). Plays a redundant role in catalyzing the formation of hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens (PubMed:16447251). Plays a redundant role in catalyzing the transfer of galactose onto hydroxylysine groups, giving rise to galactosyl 5-hydroxylysine (By similarity). Has an essential role by catalyzing the subsequent transfer of glucose moieties, giving rise to 1,2-glucosylgalactosyl-5-hydroxylysine residues (PubMed:16447251, PubMed:16467571, PubMed:21220425). Catalyzes hydroxylation and glycosylation of Lys residues in the MBL1 collagen-like domain, giving rise to hydroxylysine and 1,2-glucosylgalactosyl-5-hydroxylysine residues (PubMed:25419660). Catalyzes hydroxylation and glycosylation of Lys residues in the ADIPOQ collagen-like domain, giving rise to hydroxylysine and 1,2-glucosylgalactosyl-5-hydroxylysine residues (PubMed:23209641). Essential for normal biosynthesis and secretion of type IV collagens (PubMed:15377789, PubMed:16467571, PubMed:17873278). Essential for normal formation of basement membranes (PubMed:15377789, PubMed:16467571). {ECO:0000250|UniProtKB:O60568, ECO:0000269|PubMed:15377789, ECO:0000269|PubMed:16447251, ECO:0000269|PubMed:16467571, ECO:0000269|PubMed:17873278, ECO:0000269|PubMed:21220425, ECO:0000269|PubMed:23209641, ECO:0000269|PubMed:25419660}. PTM: N-glycosylated. {ECO:0000269|PubMed:16447251}. SUBCELLULAR LOCATION: Rough endoplasmic reticulum {ECO:0000250|UniProtKB:O60568}. Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:O60568}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:16447251}; Peripheral membrane protein {ECO:0000305|PubMed:16447251}; Lumenal side {ECO:0000305|PubMed:16447251}. Secreted {ECO:0000269|PubMed:21465473}. Secreted, extracellular space {ECO:0000269|PubMed:16447251}. Note=The majority of the secreted protein is associated with the extracellular matrix. {ECO:0000269|PubMed:16447251}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O60568}. DOMAIN: The N-terminal domain mediates glycosyltransferase activity. {ECO:0000250|UniProtKB:O60568}.; DOMAIN: The C-terminal domain that mediates lysyl hydroxylase activity is also important for homodimerization. {ECO:0000250|UniProtKB:O60568}. TISSUE SPECIFICITY: Detected in blood serum, heart, brain, liver, kidney, lung, spleen, muscle and testis (at protein level) (PubMed:16447251). Highly expressed in the heart, lung, liver and testis (PubMed:10429951). Detected in the walls of blood vessels in placenta and embryos. Detected in chondrocytes in embryos at 14.5 dpc and in adults, in adult kidney mesangium and vascular poles of kidney glomeruli (PubMed:15377789). Detected around nerves and in the adrenal gland (PubMed:15377789). {ECO:0000269|PubMed:10429951, ECO:0000269|PubMed:15377789, ECO:0000269|PubMed:16447251}. +Q2M3X8 PHAR1_MOUSE Phosphatase and actin regulator 1 580 66,286 Alternative sequence (2); Chain (1); Compositional bias (1); Erroneous initiation (3); Helix (8); Modified residue (5); Motif (1); Mutagenesis (9); Repeat (4); Turn (1) FUNCTION: Binds actin monomers (G actin) and plays a role in the reorganization of the actin cytoskeleton and in formation of actin stress fibers. Plays a role in the formation of tubules by endothelial cells. Regulates PPP1CA activity. Required for normal cell survival (By similarity). Plays a role in cell motility. {ECO:0000250, ECO:0000269|PubMed:22976292, ECO:0000269|PubMed:23041370}. SUBCELLULAR LOCATION: Cytoplasm. Cell junction, synapse {ECO:0000250}. Nucleus. Note=Enriched at synapses (By similarity). Cytoplasmic in resting cells, and is imported into the nucleus upon serum stimulation. Interaction with actin prevents nuclear import. {ECO:0000250}. SUBUNIT: Interacts (via RPEL repeats) with ACTA1 and PPP1CA; ACTA1 and PPP1CA compete for the same binding site. {ECO:0000269|PubMed:22976292, ECO:0000269|PubMed:23041370}. DOMAIN: Binds three actin monomers via the three C-terminal RPEL repeats. {ECO:0000269|PubMed:23041370}. +Q64028 PHC1_MOUSE Polyhomeotic-like protein 1 (mPH1) (Early development regulatory protein 1) (RAE-28) 1012 106,317 Alternative sequence (4); Chain (1); Compositional bias (1); Cross-link (1); Domain (1); Modified residue (3); Sequence conflict (5); Zinc finger (1) FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. Required for proper control of cellular levels of GMNN expression (By similarity). {ECO:0000250, ECO:0000269|PubMed:9367423}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Homodimer. Component of a PRC1-like complex (By similarity). Interacts with the SAM domain of SCMH1 via its SAM domain in vitro (PubMed:10653359). Interacts with RNF2 and CBX7 (PubMed:22226355). Interacts with PHC2 (PubMed:16024804). Interacts with BMI1 (PubMed:9009205). {ECO:0000250|UniProtKB:P78364, ECO:0000269|PubMed:10653359, ECO:0000269|PubMed:16024804, ECO:0000269|PubMed:22226355, ECO:0000269|PubMed:9009205}. TISSUE SPECIFICITY: Highly expressed in testis with lower levels in most other tissues. Expressed in embryonic stem cells (PubMed:22226355). {ECO:0000269|PubMed:22226355}. +Q9WV95 PHLA3_MOUSE Pleckstrin homology-like domain family A member 3 (TDAG51/Ipl homolog 1) 125 13,719 Chain (1); Domain (1); Mutagenesis (2) FUNCTION: p53/TP53-regulated repressor of Akt/AKT1 signaling. Represses AKT1 by preventing AKT1-binding to membrane lipids, thereby inhibiting AKT1 translocation to the cellular membrane and activation. Contributes to p53/TP53-dependent apoptosis by repressing AKT1 activity. Its direct transcription regulation by p53/TP53 may explain how p53/TP53 can negatively regulate AKT1. May act as a tumor suppressor (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12374806}. Membrane {ECO:0000269|PubMed:12374806}; Peripheral membrane protein {ECO:0000269|PubMed:12374806}. DOMAIN: The PH domain binds phosphoinositides with a broad specificity. It competes with the PH domain of AKT1 and directly interferes with AKT1 binding to phosphatidylinositol 4,5-bisphosphate (PIP2) and phosphatidylinositol 3,4,5-trisphosphate (PIP3), preventing AKT1 association to membrane lipids and subsequent activation of AKT1 signaling (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed in fetal tissues, with the exception of liver. Strongly expressed in adult skeletal muscle and lung. Widely expressed at lower levels in other adult tissues, with weakest expression in liver and spleen. {ECO:0000269|PubMed:10594239}. +Q9D9M5 PHOP2_MOUSE Pyridoxal phosphate phosphatase PHOSPHO2 (EC 3.1.3.74) 241 27,563 Active site (2); Binding site (2); Chain (1); Metal binding (3); Sequence conflict (1) FUNCTION: Phosphatase that has high activity toward pyridoxal 5'-phosphate (PLP). Also active at much lower level toward pyrophosphate, phosphoethanolamine (PEA), phosphocholine (PCho), phospho-l-tyrosine, fructose-6-phosphate, p-nitrophenyl phosphate, and h-glycerophosphate (By similarity). {ECO:0000250}. +A6H619 PHRF1_MOUSE PHD and RING finger domain-containing protein 1 1682 184,081 Alternative sequence (2); Chain (1); Coiled coil (1); Compositional bias (2); Modified residue (15); Sequence caution (1); Zinc finger (2) SUBUNIT: Interacts with POLR2A (via the C-terminal domain). {ECO:0000250|UniProtKB:Q63625}. +Q8CB19 PHTF2_MOUSE Putative homeodomain transcription factor 2 747 84,105 Chain (1); Sequence conflict (4) FUNCTION: May play a role in transcription regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q62066 PHX2A_MOUSE Paired mesoderm homeobox protein 2A (Aristaless homeobox protein homolog) (PHOX2A homeodomain protein) (Paired-like homeobox 2A) 280 29,417 Chain (1); Compositional bias (2); DNA binding (1) FUNCTION: May be involved in regulating the specificity of expression of the catecholamine biosynthetic genes. Acts as a transcription activator/factor. Could maintain the noradrenergic phenotype (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. +Q9DB26 PHYD1_MOUSE Phytanoyl-CoA dioxygenase domain-containing protein 1 (EC 1.-.-.-) 291 32,517 Binding site (5); Chain (1); Erroneous initiation (4); Metal binding (3); Modified residue (1); Region (1) FUNCTION: Has alpha-ketoglutarate-dependent dioxygenase activity. Does not show detectable activity towards fatty acid CoA thioesters. Is not expected to be active with phytanoyl CoA (By similarity). {ECO:0000250}. +Q8BFY7 PIMRE_MOUSE Protein PIMREG (CALM-interactor expressed in thymus and spleen homolog) (PICALM-interacting mitotic regulator) (Regulator of chromosome segregation protein 1) 231 25,686 Alternative sequence (1); Chain (1); Modified residue (6); Motif (2); Sequence conflict (2) FUNCTION: During mitosis, may play a role in the metaphase-to-anaphase transition. {ECO:0000250|UniProtKB:Q9BSJ6}. PTM: Ubiquitinated by the anaphase-promoting complex/cyclosome (APC/C) complex in the presence of FZR1, leading to its degradation by the proteasome during mitotic exit. However, degradation is not essential for normal mitotic progression within a single cell cycle (By similarity). {ECO:0000250|UniProtKB:Q9BSJ6}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BSJ6}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9BSJ6}. Note=Partially localizes to the nucleolus. {ECO:0000250|UniProtKB:Q9BSJ6}. SUBUNIT: Interacts with PICALM; this interaction may target PICALM to the nucleus. During mitosis, associates with HDAC2 and MTA2 subunits of the chromatin-remodeling NuRD complex; this association is strongest at prometaphase and decreases as the cell progresses through metaphase and anaphase. {ECO:0000250|UniProtKB:Q9BSJ6}. DOMAIN: The N-terminal destruction box 2 (D-box 2) is required for APC/C ubiquitination and proteasomal degradation. {ECO:0000250|UniProtKB:Q9BSJ6}. TISSUE SPECIFICITY: Mainly expressed in thymus and ovary. Expressed in all T-cell subpopulations isolated from the thymus, macrophages, pro-erythrocytes, granulocytes, mast cells and progenitor cells. {ECO:0000269|PubMed:19383357}. +P23506 PIMT_MOUSE Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PIMT) (EC 2.1.1.77) (L-isoaspartyl protein carboxyl methyltransferase) (Protein L-isoaspartyl/D-aspartyl methyltransferase) (Protein-beta-aspartate methyltransferase) 227 24,634 Active site (1); Alternative sequence (1); Chain (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (1) FUNCTION: Catalyzes the methyl esterification of L-isoaspartyl and D-aspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins. Acts on EIF4EBP2, microtubule-associated protein 2, calreticulin, clathrin light chains a and b, Ubiquitin carboxyl-terminal hydrolase isozyme L1, phosphatidylethanolamine-binding protein 1, stathmin, beta-synuclein and alpha-synuclein. {ECO:0000269|PubMed:16923807, ECO:0000269|PubMed:20424163}. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Monomer. +Q2YFS3 PILRA_MOUSE Paired immunoglobulin-like type 2 receptor alpha (Cell surface receptor FDF03) (Inhibitory receptor PILR-alpha) 302 33,064 Alternative sequence (1); Chain (1); Glycosylation (2); Motif (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 199 219 Helical. {ECO:0000255}. TOPO_DOM 32 198 Extracellular. {ECO:0000255}.; TOPO_DOM 220 302 Cytoplasmic. {ECO:0000255}. FUNCTION: Paired receptors consist of highly related activating and inhibitory receptors and are widely involved in the regulation of the immune system. Receptor for CD99 and PIANP. {ECO:0000269|PubMed:21241660}. PTM: Phosphorylated on tyrosine residues. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Interacts with CD99. {ECO:0000269|PubMed:14970179}. DOMAIN: Contains 2 copies of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is involved in modulation of cellular responses. The phosphorylated ITIM motif can bind the SH2 domain of several SH2-containing phosphatases. PTPN6 seems to bind predominantly to the first ITIM motif (By similarity). {ECO:0000250}. +Q4VAC9 PKHG3_MOUSE Pleckstrin homology domain-containing family G member 3 (PH domain-containing family G member 3) 1341 148,519 Alternative sequence (8); Chain (1); Compositional bias (1); Domain (2); Erroneous initiation (1); Modified residue (21); Sequence conflict (5) +Q9DCE5 PK1IP_MOUSE p21-activated protein kinase-interacting protein 1 (PAK1-interacting protein 1) (Putative PAK inhibitor Skb15) 382 42,116 Chain (1); Repeat (5); Sequence conflict (3) FUNCTION: Negatively regulates the PAK1 kinase. PAK1 is a member of the PAK kinase family, which has been shown to play a positive role in the regulation of signaling pathways involving MAPK8 and RELA. PAK1 exists as an inactive homodimer, which is activated by binding of small GTPases such as CDC42 to an N-terminal regulatory domain. PAK1IP1 also binds to the N-terminus of PAK1, and inhibits the specific activation of PAK1 by CDC42. May be involved in ribosomal large subunit assembly. {ECO:0000250|UniProtKB:Q9NWT1}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9NWT1}. SUBUNIT: Interacts with PAK1. {ECO:0000250|UniProtKB:Q9NWT1}. +Q9D240 PKHJ1_MOUSE Pleckstrin homology domain-containing family J member 1 (PH domain-containing family J member 1) (Guanine nucleotide-releasing protein x) 164 19,029 Chain (1); Domain (1); Frameshift (1) +Q8C886 PKHN1_MOUSE Probable pleckstrin homology domain-containing family N member 1 (PH domain-containing family N member 1) (Cardiolipin and phosphatidic acid-binding protein) 610 66,826 Alternative sequence (5); Chain (1); Domain (2); Initiator methionine (1); Lipidation (1); Modified residue (2); Region (1); Sequence conflict (1) FUNCTION: Controls the stability of the leptin mRNA harboring an AU-rich element (ARE) in its 3' UTR, in cooperation with the RNA stabilizer ELAVL1. Decreases the stability of the leptin mRNA by antagonizing the function of ELAVL1 by inducing its atypical recruitment from the nucleus to the cytosol (PubMed:27616329). Binds to cardiolipin (CL), phosphatidic acid (PA), phosphatidylinositol 4-phosphate (PtdIns(4)P) and phosphatidylserine (PS) (By similarity). {ECO:0000250|UniProtKB:Q494U1, ECO:0000269|PubMed:27616329}. PTM: Phosphorylation is essential for its mitochondrial localization and regulates its interaction with C1QBP. {ECO:0000250|UniProtKB:Q494U1}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q494U1}; Lipid-anchor {ECO:0000250|UniProtKB:Q494U1}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q494U1}. Mitochondrion {ECO:0000269|PubMed:27616329}. Note=Interaction with C1QBP and phosphorylation is essential for its mitochondrial localization. Localizes on the microtubule in the form of small granules. {ECO:0000250|UniProtKB:Q494U1}. SUBUNIT: Found in a complex with cytochrome c mRNA and various ribosomal proteins. Interacts with C1QBP, ELAVL1 and BID. {ECO:0000250|UniProtKB:Q494U1}. DOMAIN: Both PH domains are essential for its mitochondrial localization. {ECO:0000250|UniProtKB:Q494U1}. TISSUE SPECIFICITY: Testis and adipose tissue (at protein level). Ubiquitous. {ECO:0000269|PubMed:27616329}. +O35954 PITM1_MOUSE Membrane-associated phosphatidylinositol transfer protein 1 (Drosophila retinal degeneration B homolog 1) (RdgB1) (Mpt-1) (Phosphatidylinositol transfer protein, membrane-associated 1) (PITPnm 1) (Pyk2 N-terminal domain-interacting receptor 2) (NIR-2) 1243 134,940 Chain (1); Compositional bias (1); Domain (1); Modified residue (20) FUNCTION: Regulates RHOA activity, and plays a role in cytoskeleton remodeling. Necessary for normal completion of cytokinesis. Plays a role in maintaining normal diacylglycerol levels in the Golgi apparatus. Binds phosphatidyl inositol phosphates (in vitro). May catalyze the transfer of phosphatidylinositol and phosphatidylcholine between membranes (By similarity). Necessary for maintaining the normal structure of the endoplasmic reticulum and the Golgi apparatus. Required for protein export from the endoplasmic reticulum and the Golgi. Binds calcium ions (By similarity). {ECO:0000250, ECO:0000269|PubMed:10400687}. PTM: Phosphorylated on multiple sites by CDK1 at the onset of mitosis. Phosphorylation facilitates dissociation from the Golgi complex and is required for interaction with PLK1 (By similarity). {ECO:0000250}.; PTM: Phosphorylated on threonine residues upon treatment with oleic acid. {ECO:0000250}.; PTM: Phosphorylated on tyrosine residues by PTK2B. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O00562}. Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:O00562}; Peripheral membrane protein {ECO:0000250|UniProtKB:O00562}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O00562}; Peripheral membrane protein {ECO:0000250|UniProtKB:O00562}. Lipid droplet {ECO:0000250|UniProtKB:O00562}. Cleavage furrow {ECO:0000250|UniProtKB:O00562}. Midbody {ECO:0000250|UniProtKB:O00562}. Note=Peripheral membrane protein associated with Golgi stacks in interphase cells. A minor proportion is associated with the endoplasmic reticulum. Associated with lipid droplets. Dissociates from the Golgi early on in mitosis and localizes to the cleavage furrow and midbody during cytokinesis. {ECO:0000250|UniProtKB:O00562}. SUBUNIT: Interacts with PTK2B via its C-terminus. Interacts with RHOA. Has higher affinity for the inactive, GDP-bound form of RHOA. The CDK1-phosphorylated form interacts with PLK1. Interacts with VAPB and PIK4CA (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Detected at high levels in brain, and at lower levels in lung, kidney, spleen and liver (at protein level). Ubiquitous. Highly expressed in embryonic retina and the central nervous system. {ECO:0000269|PubMed:9245688, ECO:0000269|PubMed:9680295}. +Q9D8G5 REG4_MOUSE Regenerating islet-derived protein 4 (REG-4) 157 18,398 Chain (1); Disulfide bond (3); Domain (1); Glycosylation (2); Region (2); Sequence conflict (1); Signal peptide (1) FUNCTION: Calcium-independent lectin displaying mannose-binding specificity and able to maintain carbohydrate recognition activity in an acidic environment. May be involved in inflammatory and metaplastic responses of the gastrointestinal epithelium (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +P42337 PK3CA_MOUSE Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform (PI3-kinase subunit alpha) (PI3K-alpha) (PI3Kalpha) (PtdIns-3-kinase subunit alpha) (EC 2.7.1.153) (Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit alpha) (PtdIns-3-kinase subunit p110-alpha) (p110alpha) (Phosphoinositide-3-kinase catalytic alpha polypeptide) (Serine/threonine protein kinase PIK3CA) (EC 2.7.11.1) 1068 124,412 Beta strand (37); Chain (1); Domain (5); Helix (46); Mutagenesis (3); Sequence conflict (1); Turn (10) FUNCTION: Phosphoinositide-3-kinase (PI3K) that phosphorylates PtdIns (Phosphatidylinositol), PtdIns4P (Phosphatidylinositol 4-phosphate) and PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Participates in cellular signaling in response to various growth factors. Involved in the activation of AKT1 upon stimulation by receptor tyrosine kinases ligands such as EGF, insulin, IGF1, VEGFA and PDGF. Involved in signaling via insulin-receptor substrate (IRS) proteins. Essential in endothelial cell migration during vascular development through VEGFA signaling, possibly by regulating RhoA activity. Required for lymphatic vasculature development, possibly by binding to RAS and by activation by EGF and FGF2, but not by PDGF. Regulates invadopodia formation through the PDPK1-AKT1 pathway. Participates in cardiomyogenesis in embryonic stem cells through a AKT1 pathway. Participates in vasculogenesis in embryonic stem cells through PDK1 and protein kinase C pathway. Also has serine-protein kinase activity: phosphorylates PIK3R1 (p85alpha regulatory subunit), EIF4EBP1 and HRAS. Plays a role in the positive regulation of phagocytosis and pinocytosis (PubMed:19604150). {ECO:0000269|PubMed:16625210, ECO:0000269|PubMed:16647110, ECO:0000269|PubMed:17060635, ECO:0000269|PubMed:17540175, ECO:0000269|PubMed:18449193, ECO:0000269|PubMed:19604150, ECO:0000269|PubMed:21540297}. SUBUNIT: Heterodimer of a catalytic subunit PIK3CA and a p85 regulatory subunit (PIK3R1, PIK3R2 or PIK3R3) (PubMed:8139567). Interacts with IRS1 in nuclear extracts (PubMed:15197263). Interacts with RUFY3. Interacts with RASD2. Interacts with APPL1 (By similarity). Interacts with HRAS and KRAS (PubMed:17540175). Interaction with HRAS/KRAS is required for PI3K pathway signaling and cell proliferation stimulated by EGF and FGF2 (PubMed:17540175). Interacts with FAM83B; activates the PI3K/AKT signaling cascade (By similarity). {ECO:0000250|UniProtKB:P42336, ECO:0000269|PubMed:15197263, ECO:0000269|PubMed:17540175, ECO:0000269|PubMed:8139567}. DOMAIN: The PI3K-ABD domain and the PI3K-RBD domain interact with the PI3K/PI4K kinase domain. The C2 PI3K-type domain may facilitate the recruitment to the plasma membrane. The inhibitory interactions with PIK3R1 are mediated by the PI3K-ABD domain and the C2 PI3K-type domain with the iSH2 (inter-SH2) region of PIK3R1, and the C2 PI3K-type domain, the PI3K helical domain, and the PI3K/PI4K kinase domain with the nSH2 (N-terminal SH2) region of PIK3R1. {ECO:0000250|UniProtKB:P42336}. +Q8CDG1 PIWL2_MOUSE Piwi-like protein 2 (EC 3.1.26.-) 971 109,488 Active site (4); Chain (1); Domain (2); Erroneous initiation (1); Modified residue (13); Mutagenesis (5); Sequence conflict (4) FUNCTION: Endoribonuclease that plays a central role during spermatogenesis by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity (PubMed:11578866, PubMed:14736746, PubMed:17446352, PubMed:18381894, PubMed:18922463, PubMed:26669262). Plays an essential role in meiotic differentiation of spermatocytes, germ cell differentiation and in self-renewal of spermatogonial stem cells (PubMed:11578866, PubMed:14736746, PubMed:17446352, PubMed:18381894, PubMed:18922463, PubMed:26669262). Its presence in oocytes suggests that it may participate in similar functions during oogenesis in females (PubMed:11578866, PubMed:14736746, PubMed:17446352, PubMed:18381894, PubMed:18922463, PubMed:26669262). Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and govern the methylation and subsequent repression of transposons (PubMed:11578866, PubMed:14736746, PubMed:17446352, PubMed:18381894, PubMed:18922463, PubMed:26669262). During piRNA biosynthesis, plays a key role in the piRNA amplification loop, also named ping-pong amplification cycle, by acting as a 'slicer-competent' piRNA endoribonuclease that cleaves primary piRNAs, which are then loaded onto 'slicer-incompetent' PIWIL4 (PubMed:22020280, PubMed:23706823, PubMed:26669262). PIWIL2 slicing produces a pre-miRNA intermediate, which is then processed in mature piRNAs, and as well as a 16 nucleotide by-product that is degraded (PubMed:28633017). Required for PIWIL4/MIWI2 nuclear localization and association with secondary piRNAs antisense (PubMed:18381894, PubMed:18922463, PubMed:26669262). Besides their function in transposable elements repression, piRNAs are probably involved in other processes during meiosis such as translation regulation (PubMed:19114715). Indirectly modulates expression of genes such as PDGFRB, SLC2A1, ITGA6, GJA7, THY1, CD9 and STRA8 (PubMed:16261612). {ECO:0000269|PubMed:11578866, ECO:0000269|PubMed:14736746, ECO:0000269|PubMed:16261612, ECO:0000269|PubMed:17446352, ECO:0000269|PubMed:18381894, ECO:0000269|PubMed:18922463, ECO:0000269|PubMed:19114715, ECO:0000269|PubMed:22020280, ECO:0000269|PubMed:23706823, ECO:0000269|PubMed:26669262, ECO:0000269|PubMed:28633017}. PTM: Arginine methylation by PRMT5 is required for the interaction with Tudor domain-containing protein TDRD1 and subsequent localization to the meiotic nuage, also named P granule. {ECO:0000269|PubMed:19377467, ECO:0000269|PubMed:19465913, ECO:0000269|PubMed:19584108, ECO:0000269|PubMed:19918066, ECO:0000269|PubMed:22996915}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11578866, ECO:0000269|PubMed:18922463, ECO:0000269|PubMed:19114715, ECO:0000269|PubMed:19465913, ECO:0000269|PubMed:19584108, ECO:0000269|PubMed:20439430}. Note=Present in chromatoid body. Probable component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis (PubMed:20439430). {ECO:0000269|PubMed:20439430}. SUBUNIT: Interacts with DDX4, MAEL, EIF3A, EIF4E, EIF4G, PRMT5 and WDR77. Associates with EIF4E- and EIF4G-containing m7G cap-binding complexes. Interacts (when methylated on arginine residues) with TDRD1 and TDRKH/TDRD2. Interacts with TDRD12 (PubMed:24067652). Component of the PET complex, at least composed of EXD1, PIWIL2, TDRD12 and piRNAs (PubMed:26669262). Interacts with MOV10L1 (PubMed:20534472, PubMed:20547853). Interacts with GPAT2 (PubMed:23611983). Interacts with Tex19.1 and, probably, Tex19.2 (PubMed:28254886). {ECO:0000269|PubMed:14736746, ECO:0000269|PubMed:16787967, ECO:0000269|PubMed:19114715, ECO:0000269|PubMed:19345100, ECO:0000269|PubMed:19465913, ECO:0000269|PubMed:19584108, ECO:0000269|PubMed:19918066, ECO:0000269|PubMed:20534472, ECO:0000269|PubMed:20547853, ECO:0000269|PubMed:22996915, ECO:0000269|PubMed:23611983, ECO:0000269|PubMed:24067652, ECO:0000269|PubMed:26669262, ECO:0000269|PubMed:28254886}. TISSUE SPECIFICITY: Expressed in adult testis, specifically in spermatocytes and in spermatogonia (PubMed:11279525, PubMed:11578866, PubMed:12906857, PubMed:18404146, PubMed:18922463, PubMed:19114715, PubMed:19377467). Only detected in primordial germ cells of both sexes. Widely expressed in tumors. Also present at early stages of oocyte growth. Expressed in brain (at protein level). Present in the mitotic spermatogonia (PubMed:23706823). Not detected in the first stages of meiosis (preleptotene and leptotene) (PubMed:23706823). Detected at the late zygotene stage and increases throughout pachytene, declining from this stage onward until expression stops at the early round spermatid stage (at protein level) (PubMed:23706823). {ECO:0000269|PubMed:11279525, ECO:0000269|PubMed:11578866, ECO:0000269|PubMed:12906857, ECO:0000269|PubMed:18404146, ECO:0000269|PubMed:18922463, ECO:0000269|PubMed:19114715, ECO:0000269|PubMed:19377467, ECO:0000269|PubMed:23706823}. +O55176 PJA1_MOUSE E3 ubiquitin-protein ligase Praja-1 (Praja1) (EC 2.3.2.27) (RING-type E3 ubiquitin transferase Praja-1) 578 63,906 Alternative sequence (4); Chain (1); Compositional bias (2); Modified residue (3); Mutagenesis (2); Sequence conflict (4); Zinc finger (1) FUNCTION: Has E2-dependent E3 ubiquitin-protein ligase activity. Ubiquitinates MAGED1 antigen leading to its subsequent degradation by proteasome. May be involved in protein sorting. {ECO:0000269|PubMed:10500182, ECO:0000269|PubMed:12036302}. PTM: Substrate for E2-dependent ubiquitination. SUBUNIT: Binds ubiquitin-conjugating enzymes (E2s). Binds, in vitro and in vivo, the MAGE conserved domain of MAGED1. Binds weakly Necdin, in vitro. Interacts with UBE2D2. {ECO:0000269|PubMed:11959851, ECO:0000269|PubMed:12036302}. DOMAIN: The RING-type zinc finger domain interacts with an ubiquitin-conjugating enzyme (E2) and facilitates ubiquitination. TISSUE SPECIFICITY: Expressed in brain, liver, kidney. Highest levels in brain where it is found in many regions including cortical and subcortical areas and in neurons of the amygdala. Weak expression also found in testis. Also expressed in developing embryo. +Q8K4D7 PLCZ1_MOUSE 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase zeta-1 (EC 3.1.4.11) (Phosphoinositide phospholipase C-zeta-1) (Phospholipase C-zeta-1) (PLC-zeta-1) 647 74,614 Active site (2); Alternative sequence (1); Chain (1); Domain (4); Mutagenesis (8); Sequence conflict (2) FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. In vitro, hydrolyzes PtdIns(4,5)P2 in a Ca(2+)-dependent manner. Triggers intracellular Ca(2+) oscillations in oocytes solely during M phase and is involved in inducing oocyte activation and initiating embryonic development up to the blastocyst stage. Is therefore a strong candidate for the egg-activating soluble sperm factor that is transferred from the sperm into the egg cytoplasm following gamete membrane fusion. May exert an inhibitory effect on phospholipase-C-coupled processes that depend on calcium ions and protein kinase C, including CFTR trafficking and function. {ECO:0000250|UniProtKB:Q86YW0, ECO:0000269|PubMed:12117804, ECO:0000269|PubMed:14701816, ECO:0000269|PubMed:15159452, ECO:0000269|PubMed:15385165, ECO:0000269|PubMed:15790568, ECO:0000269|PubMed:16854985, ECO:0000269|PubMed:17933795, ECO:0000269|PubMed:18028898, ECO:0000269|PubMed:18322275, ECO:0000305}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14701816, ECO:0000269|PubMed:15159452, ECO:0000269|PubMed:15385165, ECO:0000269|PubMed:15809052, ECO:0000269|PubMed:18322275}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:14701816, ECO:0000269|PubMed:15159452, ECO:0000269|PubMed:15385165, ECO:0000269|PubMed:15809052, ECO:0000269|PubMed:18322275}. Note=Exhibits alternative cytoplasmic/nuclear localization during development. Translocates from the pronucleus into cytoplasm upon nuclear envelope breakdown for mitosis and localizes again to the pronuclei at interphase following meiosis and mitosis. {ECO:0000269|PubMed:14701816, ECO:0000269|PubMed:15159452, ECO:0000269|PubMed:15385165, ECO:0000269|PubMed:15809052, ECO:0000269|PubMed:18322275}. SUBUNIT: Interacts via its C2 domain with PtdIns(3)P and, to a lesser extent, PtdIns(5)P in vitro. {ECO:0000269|PubMed:15790568}. DOMAIN: The EF-hand and C2 domains are essential for triggering Ca(2+) oscillating activity and the regulation of PLCZ1 enzyme activity. {ECO:0000269|PubMed:15790568, ECO:0000269|PubMed:16000311, ECO:0000269|PubMed:16854985, ECO:0000269|PubMed:18028898}.; DOMAIN: The X-Y linker region between PI-PLC X-box and Y-box domains may be a target for proteolysis and may play an important regulatory role during fertilization. {ECO:0000269|PubMed:15790568, ECO:0000269|PubMed:16000311, ECO:0000269|PubMed:16854985, ECO:0000269|PubMed:18028898}. TISSUE SPECIFICITY: Highly expressed in postpuberal testis, where expression is sperm cell-specific. Also expressed in brain of both sexes. {ECO:0000269|PubMed:12117804}. +O35083 PLCA_MOUSE 1-acyl-sn-glycerol-3-phosphate acyltransferase alpha (EC 2.3.1.51) (1-acylglycerol-3-phosphate O-acyltransferase 1) (1-AGP acyltransferase 1) (1-AGPAT 1) (Lysophosphatidic acid acyltransferase alpha) (LPAAT-alpha) 285 31,709 Chain (1); Motif (2); Sequence conflict (1); Signal peptide (1); Transmembrane (3) TRANSMEM 35 55 Helical. {ECO:0000255}.; TRANSMEM 125 145 Helical. {ECO:0000255}.; TRANSMEM 190 210 Helical. {ECO:0000255}. Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3. FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. DOMAIN: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15367102}. +P97813 PLD2_MOUSE Phospholipase D2 (PLD 2) (mPLD2) (EC 3.1.4.4) (Choline phosphatase 2) (PLD1C) (Phosphatidylcholine-hydrolyzing phospholipase D2) 933 106,168 Chain (1); Domain (4); Modified residue (1); Mutagenesis (1); Region (1) FUNCTION: May have a role in signal-induced cytoskeletal regulation and/or endocytosis. PTM: Phosphorylated by FGR (By similarity). Phosphorylated on Tyr-11; most likely by EGFR. {ECO:0000250, ECO:0000269|PubMed:9837959}. SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein. SUBUNIT: Interacts with PIP5K1B (By similarity). Interacts with EGFR. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. Highest levels in brain and lung. {ECO:0000269|PubMed:9307024}. +A3KGF7 PLCB2_MOUSE 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2 (EC 3.1.4.11) (Phosphoinositide phospholipase C-beta-2) (Phospholipase C-beta-2) (PLC-beta-2) 1181 134,546 Active site (2); Alternative sequence (6); Chain (1); Coiled coil (3); Compositional bias (1); Domain (3); Metal binding (4); Modified residue (1) FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. This protein may be involved in the transduction of bitter taste stimuli (By similarity). {ECO:0000250}. SUBUNIT: Interacts with RAC1 (By similarity). Forms a complex composed of at least WDR26, a G-beta:gamma unit, and PLCB2 (By similarity). {ECO:0000250|UniProtKB:Q00722}. +P51432 PLCB3_MOUSE 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3 (EC 3.1.4.11) (Phosphoinositide phospholipase C-beta-3) (Phospholipase C-beta-3) (PLC-beta-3) 1234 139,487 Active site (2); Chain (1); Domain (3); Initiator methionine (1); Modified residue (7); Region (1); Sequence conflict (3) FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9714794}. SUBUNIT: Interacts with SHANK2 and LPAR2. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in kidney, skeletal muscle, liver, lung, heart and brain. +Q8K4S1 PLCE1_MOUSE 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase epsilon-1 (EC 3.1.4.11) (Phosphoinositide phospholipase C-epsilon-1) (Phospholipase C-epsilon-1) (PLC-epsilon-1) 2282 255,047 Active site (2); Chain (1); Domain (6); Modified residue (1); Region (1); Sequence caution (1); Sequence conflict (10) FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. PLCE1 is a bifunctional enzyme which also regulates small GTPases of the Ras superfamily through its Ras guanine-exchange factor (RasGEF) activity. As an effector of heterotrimeric and small G-protein, it may play a role in cell survival, cell growth, actin organization and T-cell activation. {ECO:0000269|PubMed:12721365, ECO:0000269|PubMed:15604236, ECO:0000269|PubMed:15743817, ECO:0000269|PubMed:16293787}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Cell membrane {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}. Note=Recruited to plasma membrane by activated HRAS and RAP2. Recruited to perinuclear membrane by activated RAP1A. Associates with Golgi membranes (By similarity). {ECO:0000250}. SUBUNIT: Interacts with GTP-bound HRAS, RAP1A, RAP2A, RAP2B and RHOA (By similarity). Interacts with IQGAP1. {ECO:0000250, ECO:0000269|PubMed:17086182}. DOMAIN: The Ras-associating domain 1 is degenerated and may not bind HRAS. The Ras-associating domain 2 mediates interaction with GTP-bound HRAS, RAP1A, RAP2A and RAP2B and recruitment of HRAS to the cell membrane (By similarity). {ECO:0000250}.; DOMAIN: The Ras-GEF domain has a GEF activity towards HRAS and RAP1A. Mediates activation of the mitogen-activated protein kinase pathway (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in neurons and to a lower extent in skin, skeletal muscle and heart (at protein level). Expressed in the epidermis. {ECO:0000269|PubMed:15604236, ECO:0000269|PubMed:15743817}. +O35405 PLD3_MOUSE Phospholipase D3 (PLD 3) (EC 3.1.4.4) (Choline phosphatase 3) (Phosphatidylcholine-hydrolyzing phospholipase D3) (Schwannoma-associated protein 9) (SAM-9) 488 54,389 Active site (3); Chain (1); Domain (2); Glycosylation (1); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 39 59 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 38 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 60 488 Lumenal. {ECO:0000255}. FUNCTION: May be involved in APP processing. {ECO:0000250}. PTM: Glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. SUBUNIT: Interacts with APP. {ECO:0000250}. TISSUE SPECIFICITY: Expressed at higher level in brain than in non-nervous tissue. Probably highly expressed in neurons. Expressed in mature neurons of the forebrain and appears to be turned on at late stages of neurogenesis. Expressed during late neuronal development in the forebrain. {ECO:0000269|PubMed:9813063}. +Q8K3K7 PLCB_MOUSE 1-acyl-sn-glycerol-3-phosphate acyltransferase beta (EC 2.3.1.51) (1-acylglycerol-3-phosphate O-acyltransferase 2) (1-AGP acyltransferase 2) (1-AGPAT 2) (Lysophosphatidic acid acyltransferase beta) (LPAAT-beta) 278 31,011 Chain (1); Motif (2); Signal peptide (1); Transmembrane (3) TRANSMEM 30 50 Helical. {ECO:0000255}.; TRANSMEM 122 142 Helical. {ECO:0000255}.; TRANSMEM 187 207 Helical. {ECO:0000255}. Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3. FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone. {ECO:0000269|PubMed:15367102}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. DOMAIN: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate. {ECO:0000250}. TISSUE SPECIFICITY: Expressed at high levels in the liver, at intermediate levels in the kidney, gut, heart and skeletal muscles. Undetectable in brain and spleen. {ECO:0000269|PubMed:15367102}. +Q8CIH5 PLCG2_MOUSE 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2 (EC 3.1.4.11) (Phosphoinositide phospholipase C-gamma-2) (Phospholipase C-gamma-2) (PLC-gamma-2) 1265 147,592 Active site (2); Beta strand (13); Chain (1); Domain (7); Helix (5); Modified residue (5); Sequence conflict (1); Turn (2) FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. It is a crucial enzyme in transmembrane signaling (By similarity). {ECO:0000250}. PTM: Phosphorylated on tyrosine residues by BTK and SYK; upon ligand-induced activation of a variety of growth factor receptors and immune system receptors. Phosphorylation leads to increased phospholipase activity (By similarity). Phosphorylated on tyrosine residues by CSF1R. {ECO:0000250, ECO:0000269|PubMed:9312046}. SUBUNIT: Interacts (via SH2 domain) with CSF1R (tyrosine phosphorylated). {ECO:0000269|PubMed:9312046}. +P70206 PLXA1_MOUSE Plexin-A1 (Plex 1) (Plexin-1) 1894 211,099 Beta strand (29); Chain (1); Coiled coil (1); Disulfide bond (10); Domain (5); Glycosylation (7); Helix (4); Mutagenesis (1); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 1243 1263 Helical. {ECO:0000255}. TOPO_DOM 28 1242 Extracellular. {ECO:0000255}.; TOPO_DOM 1264 1894 Cytoplasmic. {ECO:0000255}. FUNCTION: Coreceptor for SEMA3A, SEMA3C, SEMA3F and SEMA6D. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance, invasive growth and cell migration. Class 3 semaphorins bind to a complex composed of a neuropilin and a plexin. The plexin modulates the affinity of the complex for specific semaphorins, and its cytoplasmic domain is required for the activation of down-stream signaling events in the cytoplasm. {ECO:0000269|PubMed:10520994, ECO:0000269|PubMed:10781943}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SUBUNIT: Interacts directly with NRP1 and NRP2. Interacts with FARP2, RND1 and KDR/VEGFR2. Binding of SEMA3A leads to dissociation of FARP2. Interacts with CRMP1, DPYSL2/CRMP2, DPYSL3/CRMP3 and DPYSL4/CRMP4. {ECO:0000269|PubMed:10520994, ECO:0000269|PubMed:10781943, ECO:0000269|PubMed:12559962, ECO:0000269|PubMed:14685275, ECO:0000269|PubMed:14977921, ECO:0000269|PubMed:16286926}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12559962, ECO:0000269|PubMed:8806667}. +P15327 PMGE_MOUSE Bisphosphoglycerate mutase (BPGM) (EC 5.4.2.4) (2,3-bisphosphoglycerate mutase, erythrocyte) (2,3-bisphosphoglycerate synthase) (EC 5.4.2.11) (BPG-dependent PGAM) 259 29,978 Active site (2); Binding site (2); Chain (1); Initiator methionine (1); Modified residue (2); Region (5); Site (1) FUNCTION: Plays a major role in regulating hemoglobin oxygen affinity by controlling the levels of its allosteric effector 2,3-bisphosphoglycerate (2,3-BPG). Also exhibits mutase (EC 5.4.2.11) activity. {ECO:0000250|UniProtKB:P07738}. SUBUNIT: Homodimer. TISSUE SPECIFICITY: Expressed in red blood cells. Expressed in placenta (labyrinthine trophoblasts). {ECO:0000269|PubMed:19733906, ECO:0000269|PubMed:2847721}. +O70362 PHLD_MOUSE Phosphatidylinositol-glycan-specific phospholipase D (PI-G PLD) (EC 3.1.4.50) (Glycoprotein phospholipase D) (Glycosyl-phosphatidylinositol-specific phospholipase D) (GPI-PLD) (GPI-specific phospholipase D) 837 93,255 Chain (1); Glycosylation (10); Repeat (7); Signal peptide (1) FUNCTION: This protein hydrolyzes the inositol phosphate linkage in proteins anchored by phosphatidylinositol glycans (GPI-anchor) thus releasing these proteins from the membrane. {ECO:0000269|PubMed:9716655}. SUBCELLULAR LOCATION: Secreted. Note=Associated with the High-Density Lipoproteins (HDL). {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000305}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9716655}. +Q9QW08 PHOS_MOUSE Phosducin (PHD) (33 kDa phototransducing protein) (Rod photoreceptor 1) (RPR-1) 244 28,016 Chain (1); Modified residue (1); Region (1) FUNCTION: Inhibits the transcriptional activation activity of the cone-rod homeobox CRX (By similarity). May participate in the regulation of visual phototransduction or in the integration of photoreceptor metabolism. {ECO:0000250}. PTM: Light-induced changes in cyclic nucleotide levels modulate the phosphorylation of this protein by cAMP kinase. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P20941}. Nucleus {ECO:0000250|UniProtKB:P20941}. Cell projection, cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:P19632}. Photoreceptor inner segment {ECO:0000250|UniProtKB:P19632}. SUBUNIT: Interacts with CRX (By similarity). Forms a complex with the beta and gamma subunits of the GTP-binding protein, transducin. {ECO:0000250}. +Q9DAK9 PHP14_MOUSE 14 kDa phosphohistidine phosphatase (EC 3.9.1.3) (Phosphohistidine phosphatase 1) (PHPT1) (Protein histidine phosphatase) (PHP) 124 13,997 Active site (1); Binding site (1); Chain (1); Region (1) FUNCTION: Exhibits phosphohistidine phosphatase activity. {ECO:0000250|UniProtKB:Q9NRX4}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9NRX4}. +Q66T02 PKHG5_MOUSE Pleckstrin homology domain-containing family G member 5 (PH domain-containing family G member 5) (Synectin-binding RhoA exchange factor) (SYX) 1073 118,924 Alternative sequence (1); Chain (1); Compositional bias (3); Domain (2); Erroneous gene model prediction (1); Modified residue (6) FUNCTION: Guanine nucleotide exchange factor that activates RHOA and maybe the NF-kappa-B signaling pathway. Involved in the control of neuronal cell differentiation. Plays a role in angiogenesis through regulation of endothelial cells chemotaxis. {ECO:0000269|PubMed:16467373, ECO:0000269|PubMed:21543326}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16467373}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16467373}. Cell membrane {ECO:0000269|PubMed:16467373}. Cell junction {ECO:0000269|PubMed:21543326}. Cell projection, lamellipodium {ECO:0000269|PubMed:21543326}. Note=Predominantly cytoplasmic, however when endothelial cells are stimulated with lysophosphatidic acid, PLEKHG5 is found in perinuclear regions and at the cell membrane (PubMed:16467373). Localizes at cell-cell junctions in quiescent endothelial cells, and relocalizes to cytoplasmic vesicle and the leading edge of lamellipodia in migrating endothelial cells (PubMed:21543326). {ECO:0000269|PubMed:16467373, ECO:0000269|PubMed:21543326}. SUBUNIT: Interacts with GIPC1/synectin and RHOA. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in neurons and glial cells of the peripheral nervous system, with highest levels of expression in the brain and sciatic nerve endoneurium. Isoform 2 is expressed at detectable levels only in malignant cells. {ECO:0000269|PubMed:16467373, ECO:0000269|PubMed:23777631}. +Q80TQ5 PKHM2_MOUSE Pleckstrin homology domain-containing family M member 2 (PH domain-containing family M member 2) 1018 112,734 Alternative sequence (3); Chain (1); Compositional bias (4); Domain (2); Erroneous initiation (1); Modified residue (2); Region (1); Sequence conflict (5) FUNCTION: May play a role in the regulation of conventional kinesin activity. Required for maintenance of the Golgi apparatus organization. May play a role in membrane tubulation. May play a role in lysosomes movement and localization at the cell periphery. {ECO:0000250|UniProtKB:Q8IWE5}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8IWE5}. SUBUNIT: Interacts with KIF5B (By similarity). Interacts with BORCS5 (By similarity). {ECO:0000250|UniProtKB:Q8IWE5}. +Q8BWR2 PITH1_MOUSE PITH domain-containing protein 1 211 24,192 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (1); Modified residue (1) +Q9JMB7 PIWL1_MOUSE Piwi-like protein 1 (EC 3.1.26.-) 862 98,574 Active site (4); Alternative sequence (1); Beta strand (14); Chain (1); Domain (2); Helix (11); Modified residue (6); Motif (1); Mutagenesis (6); Region (2); Sequence caution (1); Sequence conflict (2); Site (1); Turn (1) FUNCTION: Endoribonuclease that plays a central role in postnatal germ cells by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity (PubMed:11578866, PubMed:22121019, PubMed:21237665). Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons (PubMed:11578866, PubMed:22121019, PubMed:21237665). Directly binds methylated piRNAs, a class of 24 to 30 nucleotide RNAs that are generated by a Dicer-independent mechanism and are primarily derived from transposons and other repeated sequence elements (PubMed:11578866, PubMed:22121019, PubMed:21237665). Strongly prefers a uridine in the first position of their guide (g1U preference, also named 1U-bias) (PubMed:24757166). Not involved in the piRNA amplification loop, also named ping-pong amplification cycle (PubMed:22121019). Acts as an endoribonuclease that cleaves transposon messenger RNAs (PubMed:22121019). Besides their function in transposable elements repression, piRNAs are probably involved in other processes during meiosis such as translation regulation (PubMed:16938833). Probable component of some RISC complex, which mediates RNA cleavage and translational silencing (PubMed:16938833). Also plays a role in the formation of chromatoid bodies and is required for some miRNAs stability (PubMed:16787948). Required to sequester RNF8 in the cytoplasm until late spermatogenesis; RNF8 being released upon ubiquitination and degradation of PIWIL1 (PubMed:28552346). {ECO:0000269|PubMed:11578866, ECO:0000269|PubMed:16787948, ECO:0000269|PubMed:16938833, ECO:0000269|PubMed:21237665, ECO:0000269|PubMed:22121019, ECO:0000269|PubMed:24757166, ECO:0000269|PubMed:28552346}. PTM: Ubiquitinated by the anaphase promoting complex/cyclosome (APC/C) in late spermatids, leading to its degradation (PubMed:23328397). Ubiquitination only takes place following piRNA-binding in adult testis (PubMed:23328397). Ubiquitination and degradation in late spermatogenesis by APC/C is probably required to release RNF8 from the cytoplasm and promote histone to protamine exchange by RNF8 (PubMed:28552346). {ECO:0000269|PubMed:23328397, ECO:0000269|PubMed:28552346}.; PTM: Arginine methylation by PRMT5 is required for the interaction with Tudor domain-containing protein (TDRD1, TDRKH/TDRD2, RNF17/TDRD4, TDRD6, TDRD7 and TDRD9) and subsequent localization to the meiotic nuage, also named P granule. {ECO:0000269|PubMed:19377467, ECO:0000269|PubMed:19465913, ECO:0000269|PubMed:19584108, ECO:0000269|PubMed:19918066, ECO:0000269|PubMed:19926723}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11578866, ECO:0000269|PubMed:12062093, ECO:0000269|PubMed:16787948, ECO:0000269|PubMed:16938833, ECO:0000269|PubMed:19020299, ECO:0000269|PubMed:19584108}. Note=Component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis. Also present in chromatoid body. SUBUNIT: Interacts (via Piwi domain) with DICER1, suggesting that it forms ribonucleoprotein RISC complexes; this interaction is regulated by HSP90AB1 activity (PubMed:16938833). Interacts with MAEL, KIF17, PABPC1, PRMT5 and WDR77 (PubMed:16787948, PubMed:16787967, PubMed:19020299, PubMed:19584108). Interacts (when methylated on arginine residues) with TDRD1, TDRKH/TDRD2, RNF17/TDRD4, TDRD6, TDRD7 and TDRD9 (PubMed:19584108, PubMed:19918066, PubMed:19926723, PubMed:23714778). Interacts with CLOCK (PubMed:22900038). Interacts with MOV10L1 (PubMed:20534472). Interacts with ANAPC10; interaction oly takes place following piRNA-binding (PubMed:23328397). Interacts with RNF8; leading to sequester RNF8 in the cytoplasm (PubMed:28552346). Interacts with Tex19.1 and, probably, Tex19.2 (PubMed:28254886). {ECO:0000269|PubMed:16787948, ECO:0000269|PubMed:16787967, ECO:0000269|PubMed:16938833, ECO:0000269|PubMed:19020299, ECO:0000269|PubMed:19584108, ECO:0000269|PubMed:19918066, ECO:0000269|PubMed:19926723, ECO:0000269|PubMed:20534472, ECO:0000269|PubMed:22900038, ECO:0000269|PubMed:23328397, ECO:0000269|PubMed:23714778, ECO:0000269|PubMed:28254886, ECO:0000269|PubMed:28552346}. DOMAIN: The D-box (destruction box) acts as a recognition signal for association with the APC/C complex, ubiquitination and degradation (PubMed:23328397). {ECO:0000269|PubMed:23328397}.; DOMAIN: The PAZ domain specifically recognizes binds the 2'-O-methylated 3'-end of piRNAs (PubMed:21237665). The MID region is required for recognition of uridine in the first position of piRNAs (g1U preference, also named 1U-bias) (PubMed:24757166). {ECO:0000269|PubMed:21237665, ECO:0000269|PubMed:24757166}. TISSUE SPECIFICITY: Expressed in brain. Expressed in testis, specifically in spermatocytes (at protein level). Only detected in germ lineage cells of adult testis. Expressed in male gonads 2 weeks after birth at the initiation of spermatogenesis, but not expressed in female gonads. {ECO:0000269|PubMed:11578866, ECO:0000269|PubMed:12062093, ECO:0000269|PubMed:19377467, ECO:0000269|PubMed:19926723}. +Q3UHE1 PITM3_MOUSE Membrane-associated phosphatidylinositol transfer protein 3 (Phosphatidylinositol transfer protein, membrane-associated 3) (PITPnm 3) (Pyk2 N-terminal domain-interacting receptor 1) (NIR-1) 974 106,462 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (1); Modified residue (12); Sequence conflict (1) FUNCTION: Catalyzes the transfer of phosphatidylinositol and phosphatidylcholine between membranes (in vitro). Binds calcium ions (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endomembrane system {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. SUBUNIT: Interacts with PTK2B via its C-terminus. {ECO:0000250}. +P70314 PITX1_MOUSE Pituitary homeobox 1 (Hindlimb-expressed homeobox protein backfoot) (Homeobox protein P-OTX) (Homeobox protein PITX1) (Paired-like homeodomain transcription factor 1) (Pituitary OTX-related factor) 315 34,075 Chain (1); DNA binding (1); Modified residue (3); Motif (2); Region (1); Sequence conflict (1) FUNCTION: Sequence-specific transcription factor that binds gene promoters and activates their transcription. May play a role in the development of anterior structures, and in particular, the brain and facies and in specifying the identity or structure of hindlimb. Can independently activate and synergize with PIT-1 on pituitary-specific target gene promoters, thus may subserve functions in generating both precursor and specific cell phenotypes in the anterior pituitary gland and in several other organs. Can activate pituitary transcription of the proopiomelanocortin gene. {ECO:0000250|UniProtKB:P56673, ECO:0000269|PubMed:8675014, ECO:0000269|PubMed:8755540}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with POU1F1. {ECO:0000250|UniProtKB:P78337}. TISSUE SPECIFICITY: Expressed in primordial Rathke pouch, oral epithelium, first branchial arch, duodenum, and hindlimb. +Q6PF93 PK3C3_MOUSE Phosphatidylinositol 3-kinase catalytic subunit type 3 (PI3-kinase type 3) (PI3K type 3) (PtdIns-3-kinase type 3) (EC 2.7.1.137) (Phosphoinositide-3-kinase class 3) 887 101,487 Alternative sequence (2); Chain (1); Domain (3); Modified residue (5); Mutagenesis (2); Sequence conflict (2) FUNCTION: Catalytic subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate; different complex forms are believed to play a role in multiple membrane trafficking pathways: PI3KC3-C1 is involved in initiation of autophagosomes and PI3KC3-C2 in maturation of autophagosomes and endocytosis. Involved in regulation of degradative endocytic trafficking and required for the abcission step in cytokinesis, probably in the context of PI3KC3-C2. Involved in the transport of lysosomal enzyme precursors to lysosomes. Required for transport from early to late endosomes (By similarity). {ECO:0000250|UniProtKB:O88763, ECO:0000250|UniProtKB:Q8NEB9}. SUBCELLULAR LOCATION: Midbody {ECO:0000250|UniProtKB:Q8NEB9}. Late endosome {ECO:0000250|UniProtKB:Q8NEB9}. Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:Q8NEB9}. Note=As component of the PI3K complex I localized to pre-autophagosome structures. As component of the PI3K complex II localized predominantly to endosomes (By similarity). Localizes also to discrete punctae along the ciliary axoneme and to the base of the ciliary axoneme (PubMed:24089209). {ECO:0000250|UniProtKB:Q8NEB9, ECO:0000269|PubMed:24089209}. SUBUNIT: Component of the PI3K (PI3KC3/PI3K-III/class III phosphatidylinositol 3-kinase) complex the core of which is composed of the catalytic subunit PIK3C3, the regulatory subunit PIK3R4 and BECN1 associating with additional regulatory/auxilliary subunits to form alternative complex forms. Alternative complex forms containing a forth regulatory subunit in a mutually exclusive manner are: the PI3K complex I (PI3KC3-C1) containing ATG14, and the PI3K complex II (PI3KC3-C2) containing UVRAG. PI3KC3-C1 displays a V-shaped architecture with PIK3R4 serving as a bridge between PIK3C3 and the ATG14:BECN1 subcomplex (By similarity). Both, PI3KC3-C1 and PI3KC3-C2, can associate with further regulatory subunits such as RUBCN, SH3GLB1/Bif-1 and AMBRA1 (PubMed:17589504). PI3KC3-C1 probably associates with PIK3CB (PubMed:21059846). Interacts with RAB7A in the presence of PIK3R4 (By similarity). Interacts with AMBRA1 (PubMed:17589504). Interacts with BECN1P1/BECN2 (By similarity). Interacts with SLAMF1 (PubMed:22493499). May be a component of a complex composed of RAB5A (in GDP-bound form), DYN2 and PIK3C3 (By similarity). Interacts with NCKAP1L (By similarity). {ECO:0000250|UniProtKB:Q8NEB9, ECO:0000250|UniProtKB:Q9TXI7, ECO:0000269|PubMed:17589504, ECO:0000269|PubMed:21059846, ECO:0000269|PubMed:23332761}. +Q80U04 PJA2_MOUSE E3 ubiquitin-protein ligase Praja-2 (Praja2) (EC 2.3.2.27) (RING finger protein 131) (RING-type E3 ubiquitin transferase Praja-2) 707 77,958 Alternative sequence (1); Chain (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (6); Region (1); Sequence conflict (1); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: Has E2-dependent E3 ubiquitin-protein ligase activity. Responsible for ubiquitination of cAMP-dependent protein kinase type I and type II-alpha/beta regulatory subunits and for targeting them for proteasomal degradation. Essential for PKA-mediated long-term memory processes. Through the ubiquitination of MFHAS1, positively regulates the TLR2 signaling pathway that leads to the activation of the downstream p38 and JNK MAP kinases and promotes the polarization of macrophages toward the pro-inflammatory M1 phenotype. {ECO:0000250|UniProtKB:O43164, ECO:0000269|PubMed:12036302}. SUBCELLULAR LOCATION: Cytoplasm. Cell membrane {ECO:0000250}. Endoplasmic reticulum membrane; Peripheral membrane protein. Golgi apparatus membrane; Peripheral membrane protein. Cell junction, synapse {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250}. Note=Localizes at the cytoplasmic side of endoplasmic reticulum and Golgi apparatus. Expressed in the postsynaptic density region of synapses. Co-localizes with PRKAR2A and PRKAR2B in the cytoplasm and the cell membrane (By similarity). {ECO:0000250}. SUBUNIT: Binds ubiquitin-conjugating enzymes (E2s). In vitro, interacts with the ubiquitin-conjugating enzyme, UBE2D2. The phosphorylated form interacts with PRKAR1A, PRKAR2A and PRKAR2B. Binds the catalytic subunits of cAMP-dependent protein kinase. Interacts with MFHAS1. {ECO:0000250|UniProtKB:O43164}. +Q9JHG7 PK3CG_MOUSE Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform (PI3-kinase subunit gamma) (PI3K-gamma) (PI3Kgamma) (PtdIns-3-kinase subunit gamma) (EC 2.7.1.153) (Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit gamma) (PtdIns-3-kinase subunit p110-gamma) (p110gamma) (Phosphoinositide-3-kinase catalytic gamma polypeptide) (Serine/threonine protein kinase PIK3CG) (EC 2.7.11.1) (p120-PI3K) 1102 126,400 Chain (1); Compositional bias (1); Domain (5); Modified residue (2); Nucleotide binding (3); Sequence conflict (4) Phospholipid metabolism; phosphatidylinositol phosphate biosynthesis. FUNCTION: Phosphoinositide-3-kinase (PI3K) that phosphorylates PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Links G-protein coupled receptor activation to PIP3 production. Involved in immune, inflammatory and allergic responses. Modulates leukocyte chemotaxis to inflammatory sites and in response to chemoattractant agents. May control leukocyte polarization and migration by regulating the spatial accumulation of PIP3 and by regulating the organization of F-actin formation and integrin-based adhesion at the leading edge. Controls motility of dendritic cells. Together with PIK3CD is involved in natural killer (NK) cell development and migration towards the sites of inflammation. Participates in T-lymphocyte migration. Regulates T-lymphocyte proliferation and cytokine production. Together with PIK3CD participates in T-lymphocyte development. Required for B-lymphocyte development and signaling. Together with PIK3CD participates in neutrophil respiratory burst. Together with PIK3CD is involved in neutrophil chemotaxis and extravasation. Together with PIK3CB promotes platelet aggregation and thrombosis. Regulates alpha-IIb/beta-3 integrins (ITGA2B/ ITGB3) adhesive function in platelets downstream of P2Y12 through a lipid kinase activity-independent mechanism. May have also a lipid kinase activity-dependent function in platelet aggregation. Involved in endothelial progenitor cell migration. Negative regulator of cardiac contractility. Modulates cardiac contractility by anchoring protein kinase A (PKA) and PDE3B activation, reducing cAMP levels. Regulates cardiac contractility also by promoting beta-adrenergic receptor internalization by binding to GRK2 and by non-muscle tropomyosin phosphorylation. Also has serine/threonine protein kinase activity: both lipid and protein kinase activities are required for beta-adrenergic receptor endocytosis. May also have a scaffolding role in modulating cardiac contractility. Contribute to cardiac hypertrophy under pathological stress. Through simultaneous binding of PDE3B to RAPGEF3 and PIK3R6 is assembled in a signaling complex in which the PI3K gamma complex is activated by RAPGEF3 and which is involved in angiogenesis (By similarity). {ECO:0000250, ECO:0000269|PubMed:10669416, ECO:0000269|PubMed:10669418, ECO:0000269|PubMed:12297047, ECO:0000269|PubMed:15294162, ECO:0000269|PubMed:15318168, ECO:0000269|PubMed:16116162, ECO:0000269|PubMed:16127437, ECO:0000269|PubMed:17673465, ECO:0000269|PubMed:19297623, ECO:0000269|PubMed:21474070}. PTM: Phosphorylated at Thr-1024 by PKA. Phosphorylation inhibits lipid kinase activity. {ECO:0000269|PubMed:21474070}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. SUBUNIT: Heterodimer of a catalytic subunit PIK3CG and a PIK3R5 or PIK3R6 regulatory subunit. Interacts with GRK2 through the PIK helical domain (By similarity). Interaction with GRK2 is required for targeting to agonist-occupied receptor. Interacts with PDE3B. Interacts with TPM2 (By similarity). Interacts with EPHA8; regulates integrin-mediated cell adhesion to substrate. Interacts with HRAS; the interaction is required for membrane recruitment and beta-gamma G protein dimer-dependent activation of the PI3K gamma complex PIK3CG:PIK3R6. {ECO:0000250, ECO:0000269|PubMed:11416136, ECO:0000269|PubMed:15294162, ECO:0000269|PubMed:19906996}. +O08852 PKD1_MOUSE Polycystin-1 (Autosomal dominant polycystic kidney disease 1 protein homolog) 4293 466,577 Chain (1); Coiled coil (1); Compositional bias (2); Disulfide bond (4); Domain (24); Glycosylation (63); Modified residue (1); Repeat (2); Sequence conflict (13); Signal peptide (1); Site (1); Topological domain (12); Transmembrane (11) TRANSMEM 3067 3087 Helical. {ECO:0000250|UniProtKB:P98161}.; TRANSMEM 3270 3290 Helical. {ECO:0000250|UniProtKB:P98161}.; TRANSMEM 3316 3336 Helical. {ECO:0000250|UniProtKB:P98161}.; TRANSMEM 3550 3570 Helical. {ECO:0000250|UniProtKB:P98161}.; TRANSMEM 3573 3593 Helical. {ECO:0000250|UniProtKB:P98161}.; TRANSMEM 3656 3676 Helical. {ECO:0000250|UniProtKB:P98161}.; TRANSMEM 3892 3912 Helical. {ECO:0000250|UniProtKB:P98161}.; TRANSMEM 3926 3946 Helical. {ECO:0000250|UniProtKB:P98161}.; TRANSMEM 3975 3995 Helical. {ECO:0000250|UniProtKB:P98161}.; TRANSMEM 4018 4038 Helical. {ECO:0000250|UniProtKB:P98161}.; TRANSMEM 4081 4100 Helical. {ECO:0000250|UniProtKB:P98161}. TOPO_DOM 24 3066 Extracellular. {ECO:0000305}.; TOPO_DOM 3088 3269 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 3291 3315 Extracellular. {ECO:0000305}.; TOPO_DOM 3337 3549 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 3571 3572 Extracellular. {ECO:0000305}.; TOPO_DOM 3594 3655 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 3677 3891 Extracellular. {ECO:0000305}.; TOPO_DOM 3913 3925 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 3947 3974 Extracellular. {ECO:0000305}.; TOPO_DOM 3996 4017 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 4039 4080 Extracellular. {ECO:0000305}.; TOPO_DOM 4101 4293 Cytoplasmic. {ECO:0000305}. FUNCTION: Component of a heteromeric calcium-permeable ion channel formed by PKD1 and PKD2 that is activated by interaction between PKD1 and a Wnt family member, such as WNT3A and WNT9B. Both PKD1 and PKD2 are required for channel activity (By similarity). Involved in renal tubulogenesis (PubMed:24939912). Involved in fluid-flow mechanosensation by the primary cilium in renal epithelium (PubMed:12514735). Acts as a regulator of cilium length, together with PKD2 (PubMed:20096584). The dynamic control of cilium length is essential in the regulation of mechanotransductive signaling. The cilium length response creates a negative feedback loop whereby fluid shear-mediated deflection of the primary cilium, which decreases intracellular cAMP, leads to cilium shortening and thus decreases flow-induced signaling. May be an ion-channel regulator. Involved in adhesive protein-protein and protein-carbohydrate. {ECO:0000250|UniProtKB:P98161, ECO:0000269|PubMed:12514735, ECO:0000269|PubMed:20096584, ECO:0000269|PubMed:24939912}. PTM: After synthesis, undergoes autoproteolytic cleavage between Leu-3040 and Thr-3041 in the GPS domain (PubMed:25405894). Cleavage at the GPS domain occurs through a cis-autoproteolytic mechanism involving an ester-intermediate via N-O acyl rearrangement (By similarity). This process takes place in the early secretory pathway, depends on initial N-glycosylation, and requires the REJ domain (By similarity). PKD1 is ubiquitously and incompletely cleaved in wild-type mice, so that uncleaved and cleaved PKD1 molecules coexist. The differential patterns of cleavage during embryonic development, as well as in adult mice, suggest different functions of uncleaved and cleaved molecules (PubMed:18003909). {ECO:0000250|UniProtKB:P98161, ECO:0000269|PubMed:18003909, ECO:0000269|PubMed:25405894}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P98161}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P98161}. Cell projection, cilium {ECO:0000269|PubMed:12514735, ECO:0000269|PubMed:24939912, ECO:0000269|PubMed:25405894}. Endoplasmic reticulum {ECO:0000269|PubMed:25405894}. Golgi apparatus {ECO:0000269|PubMed:25405894}. Note=PKD1 localization to the plasma and ciliary membranes requires PKD2, is independent of PKD2 channel activity, and involves stimulation of PKD1 autocatalytic cleavage at the GPS domain (PubMed:12514735, PubMed:25405894). PKD1:PKD2 interaction is required to reach the Golgi apparatus from endoplasmic reticulum and then traffic to the cilia (PubMed:25405894). Ciliary localization of PKD1 requires BBS1 and ARL6/BBS3 (PubMed:24939912). Cell surface localization requires GANAB (By similarity). {ECO:0000250|UniProtKB:P98161, ECO:0000269|PubMed:12514735, ECO:0000269|PubMed:24939912, ECO:0000269|PubMed:25405894}. SUBUNIT: Interacts with PKD2; the interaction is required for ciliary localization (PubMed:25405894). Component of a heterotetrameric channel complex with PKD2; the tetramer contains one PKD1 chain and three PKD2 chains (By similarity). Interacts with PKD2L1 (PubMed:15548533). Interacts with PRKX; involved in differentiation and controlled morphogenesis of the kidney. Interacts (via extracellular domain) with WNT3A, WNT4 and WNT9B (By similarity). Interacts with WNT5A, DVL1 and DVL2 (PubMed:27214281). Interacts with NPHP1 (via SH3 domain) (PubMed:20856870). Interacts with BBS1, BBS4, BBS5 and TTC8. Interacts with RGS7 (By similarity). Interacts (via C-terminal domain) with RABEP1; the interaction connects PKD1:PKD2 to GGA1 and ARL3 that mediate the ciliary targeting (PubMed:25405894). {ECO:0000250|UniProtKB:P98161, ECO:0000269|PubMed:15548533, ECO:0000269|PubMed:20856870, ECO:0000269|PubMed:25405894, ECO:0000269|PubMed:27214281}. DOMAIN: The LDL-receptor class A domain is atypical; the potential calcium-binding site is missing. +Q8CHK2 REL3_MOUSE Relaxin-3 (Insulin-like peptide INSL7) (Insulin-like peptide 7) (Prorelaxin M3) [Cleaved into: Relaxin-3 B chain; Relaxin-3 A chain] 141 14,926 Disulfide bond (3); Peptide (2); Propeptide (1); Signal peptide (1) FUNCTION: May play a role in neuropeptide signaling processes. Ligand for LGR7, relaxin-3 receptor-1 and relaxin-3 receptor-2 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Heterodimer of a B chain and an A chain linked by two disulfide bonds. TISSUE SPECIFICITY: High expression in the brain localized to the pons/medulla with highest levels in pars ventromedialis of the dorsal tegmental nucleus. Significant expression is also detected in the spleen, thymus, lung, testis and ovary. {ECO:0000269|PubMed:11689565}. +Q8VCI0 PLBL1_MOUSE Phospholipase B-like 1 (EC 3.1.1.-) (LAMA-like protein 1) (Lamina ancestor homolog 1) (Phospholipase B domain-containing protein 1) [Cleaved into: Phospholipase B-like 1 chain A; Phospholipase B-like 1 chain B; Phospholipase B-like 1 chain C] 550 62,998 Chain (4); Disulfide bond (2); Frameshift (1); Glycosylation (9); Propeptide (1); Sequence conflict (2); Signal peptide (1) FUNCTION: Exhibits weak phospholipase activity, acting on various phospholipids, including phosphatidylcholine, phosphatidylinositol, phosphatidylethanolamine and lysophospholipids. However, in view of the small size of the putative binding pocket, it has been proposed that it may act rather as an amidase or a peptidase (By similarity). {ECO:0000250}. PTM: The maturation cleavages that produces chains A and B are required to open the putative substrate binding pocket. Both chains A and B remain associated in the mature protein (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Lysosome {ECO:0000250}. SUBUNIT: May form a homodimer, each monomer is composed of a chain A and a chain B. {ECO:0000250}. +Q8K2J0 PLCD3_MOUSE 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-3 (EC 3.1.4.11) (Phosphoinositide phospholipase C-delta-3) (Phospholipase C-delta-3) (PLC-delta-3) 785 88,607 Active site (2); Binding site (4); Calcium binding (2); Chain (1); Domain (7); Erroneous gene model prediction (1); Erroneous initiation (1); Metal binding (10); Modified residue (3); Region (1); Sequence caution (1); Sequence conflict (6) FUNCTION: Hydrolyzes the phosphatidylinositol 4,5-bisphosphate (PIP2) to generate 2 second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). DAG mediates the activation of protein kinase C (PKC), while IP3 releases Ca(2+) from intracellular stores. Essential for trophoblast and placental development. May participate in cytokinesis by hydrolyzing PIP2 at the cleavage furrow. {ECO:0000269|PubMed:16314520}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Cleavage furrow. Note=Localizes at the cleavage furrow during cytokinesis. DOMAIN: The C2 domain is a Ca(2+)-dependent membrane-targeting module. {ECO:0000250}.; DOMAIN: The PH domain mediates interaction with the surface membrane by binding to PIP2. {ECO:0000250}. +P43883 PLIN2_MOUSE Perilipin-2 (Adipophilin) (Adipose differentiation-related protein) (ADRP) 425 46,646 Chain (1); Initiator methionine (1); Modified residue (2); Sequence conflict (2) FUNCTION: May be involved in development and maintenance of adipose tissue. {ECO:0000305|PubMed:1518805}. SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:1518805}; Peripheral membrane protein {ECO:0000305|PubMed:1518805}. Lipid droplet {ECO:0000269|PubMed:9392423}. TISSUE SPECIFICITY: Adipose tissue specific. Expressed abundantly and preferentially in fat pads. {ECO:0000269|PubMed:1518805}. +Q9DBG5 PLIN3_MOUSE Perilipin-3 (Cargo selection protein TIP47) (Mannose-6-phosphate receptor-binding protein 1) 437 47,262 Beta strand (3); Chain (1); Coiled coil (2); Cross-link (1); Frameshift (1); Helix (9); Initiator methionine (1); Modified residue (8); Turn (1) FUNCTION: Required for the transport of mannose 6-phosphate receptors (MPR) from endosomes to the trans-Golgi network. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Lipid droplet {ECO:0000250}. Note=Membrane associated on endosomes. Detected in the envelope and the core of lipid bodies and in lipid sails (By similarity). {ECO:0000250}. SUBUNIT: Homooligomer. Interacts with M6PR (via the cytoplasmic domain). Interacts with IGF2R (via the cytoplasmic domain) (By similarity). {ECO:0000250}. +Q9Z0T6 PKDRE_MOUSE Polycystic kidney disease and receptor for egg jelly-related protein (PKD and REJ homolog) 2126 241,390 Chain (1); Domain (2); Glycosylation (18); Signal peptide (1); Topological domain (12); Transmembrane (11) TRANSMEM 1069 1089 Helical. {ECO:0000255}.; TRANSMEM 1274 1294 Helical. {ECO:0000255}.; TRANSMEM 1312 1332 Helical. {ECO:0000255}.; TRANSMEM 1450 1470 Helical. {ECO:0000255}.; TRANSMEM 1484 1504 Helical. {ECO:0000255}.; TRANSMEM 1581 1601 Helical. {ECO:0000255}.; TRANSMEM 1839 1859 Helical. {ECO:0000255}.; TRANSMEM 1876 1896 Helical. {ECO:0000255}.; TRANSMEM 1919 1939 Helical. {ECO:0000255}.; TRANSMEM 1965 1985 Helical. {ECO:0000255}.; TRANSMEM 2020 2040 Helical. {ECO:0000255}. TOPO_DOM 19 1068 Extracellular. {ECO:0000255}.; TOPO_DOM 1090 1273 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1295 1311 Extracellular. {ECO:0000255}.; TOPO_DOM 1333 1449 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1471 1483 Extracellular. {ECO:0000255}.; TOPO_DOM 1505 1580 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1602 1838 Extracellular. {ECO:0000255}.; TOPO_DOM 1860 1875 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1897 1918 Extracellular. {ECO:0000255}.; TOPO_DOM 1940 1964 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1986 2019 Extracellular. {ECO:0000255}.; TOPO_DOM 2041 2126 Cytoplasmic. {ECO:0000255}. FUNCTION: May have a central role in fertilization. May generate a Ca(2+) transporting channel directly involved in initiating the acrosome reaction of the sperm. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: May form homomultimers or heteromultimers in combination with an as yet unidentified subunits. +Q9D1E8 PLCE_MOUSE 1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon (EC 2.3.1.51) (1-acylglycerol-3-phosphate O-acyltransferase 5) (1-AGP acyltransferase 5) (1-AGPAT 5) (Lysophosphatidic acid acyltransferase epsilon) (LPAAT-epsilon) 365 42,202 Chain (1); Motif (1); Sequence conflict (2); Transmembrane (2) TRANSMEM 15 35 Helical. {ECO:0000255}.; TRANSMEM 345 365 Helical. {ECO:0000255}. Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3. FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone. Acts on LPA containing saturated or unsaturated fatty acids C15:0-C20:4 at the sn-1 position using C18:1-CoA as the acyl donor. Also acts on lysophosphatidylethanolamine using oleoyl-CoA, but not arachidonoyl-CoA, and lysophosphatidylinositol using arachidonoyl-CoA, but not oleoyl-CoA. Activity toward lysophosphatidylglycerol not detectable. {ECO:0000269|PubMed:15367102}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Nucleus envelope {ECO:0000250}. Mitochondrion {ECO:0000250}. DOMAIN: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15367102}. +Q62077 PLCG1_MOUSE 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 (EC 3.1.4.11) (Phosphoinositide phospholipase C-gamma-1) (Phospholipase C-gamma-1) (PLC-gamma-1) 1302 149,668 Active site (2); Calcium binding (1); Chain (1); Domain (10); Initiator methionine (1); Modified residue (12); Sequence conflict (2) FUNCTION: Mediates the production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). Plays an important role in the regulation of intracellular signaling cascades. Becomes activated in response to ligand-mediated activation of receptor-type tyrosine kinases, such as PDGFRA, PDGFRB, FGFR1, FGFR2, FGFR3 and FGFR4. Plays a role in actin reorganization and cell migration. {ECO:0000269|PubMed:15308098}. PTM: Tyrosine phosphorylated in response to signaling via activated FLT3, KIT and PDGFRA (By similarity). Tyrosine phosphorylated by activated FGFR1, FGFR2, FGFR3 and FGFR4. Tyrosine phosphorylated by activated FLT1 and KDR. Tyrosine phosphorylated by activated PDGFRB. The receptor-mediated activation of PLCG1 involves its phosphorylation by tyrosine kinases in response to ligation of a variety of growth factor receptors and immune system receptors. For instance, SYK phosphorylates and activates PLCG1 in response to ligation of the B-cell receptor. Phosphorylated by ITK and TXK on Tyr-783 upon TCR activation in T-cells. May be dephosphorylated by PTPRJ (By similarity). {ECO:0000250}.; PTM: Ubiquitinated by CBLB in activated T-cells. {ECO:0000269|PubMed:15308098}. SUBCELLULAR LOCATION: Cell projection, lamellipodium {ECO:0000250}. Cell projection, ruffle {ECO:0000250}. Note=Rapidly redistributed to ruffles and lamellipodia structures in response to epidermal growth factor (EGF) treatment. {ECO:0000250}. SUBUNIT: Interacts (via SH2 domain) with FGFR1, FGFR2, FGFR3 and FGFR4 (phosphorylated). Interacts with RALGPS1. Interacts (via SH2 domains) with VIL1 (phosphorylated at C-terminus tyrosine phosphorylation sites). Interacts (via SH2 domain) with RET (By similarity). Interacts with AGAP2 via its SH3 domain. Interacts with LAT (phosphorylated) upon TCR activation. Interacts (via SH3 domain) with the Pro-rich domain of TNK1. Associates with BLNK, VAV1, GRB2 and NCK1 in a B-cell antigen receptor-dependent fashion. Interacts with CBLB in activated T-cells; which inhibits phosphorylation. Interacts with SHB. Interacts (via SH3 domain) with the Arg/Gly-rich-flanked Pro-rich domains of KHDRBS1/SAM68. This interaction is selectively regulated by arginine methylation of KHDRBS1/SAM68. Interacts with INPP5D/SHIP1, THEMIS and CLNK. Interacts with FLT4 and KIT. Interacts with AXL (By similarity). Interacts with SYK; activates PLCG1 (By similarity). Interacts with FLT1 (tyrosine-phosphorylated). Interacts (via SH2 domain) with PDGFRA and PDGFRB (tyrosine phosphorylated). Interacts with PIP5K1C. Interacts with NTRK1 and NTRK2 (phosphorylated upon ligand-binding). Interacts with TESPA1 (By similarity). Interacts with GRB2, LAT and THEMIS upon TCR activation in thymocytes; the association is weaker in the absence of TESPA1. {ECO:0000250, ECO:0000269|PubMed:10646608, ECO:0000269|PubMed:10748127, ECO:0000269|PubMed:11463797, ECO:0000269|PubMed:12367511, ECO:0000269|PubMed:15629145, ECO:0000269|PubMed:16000869, ECO:0000269|PubMed:1646396, ECO:0000269|PubMed:1714377, ECO:0000269|PubMed:17620338, ECO:0000269|PubMed:17635937, ECO:0000269|PubMed:19597499, ECO:0000269|PubMed:22561606, ECO:0000269|PubMed:8943348, ECO:0000269|PubMed:9299537}. DOMAIN: The SH3 domain mediates interaction with RALGPS1 (By similarity). The SH3 domain also mediates interaction with CLNK. {ECO:0000250, ECO:0000269|PubMed:11463797}. +P20918 PLMN_MOUSE Plasminogen (EC 3.4.21.7) [Cleaved into: Plasmin heavy chain A; Activation peptide; Angiostatin; Plasmin heavy chain A, short form; Plasmin light chain B] 812 90,808 Active site (3); Chain (5); Disulfide bond (24); Domain (7); Modified residue (2); Peptide (1); Sequence conflict (5); Signal peptide (1) FUNCTION: Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation. In ovulation, weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1 and C5. Cleavage of fibronectin and laminin leads to cell detachment and apoptosis. Also cleaves fibrin, thrombospondin and von Willebrand factor. Its role in tissue remodeling and tumor invasion may be modulated by CSPG4. Binds to cells (By similarity). {ECO:0000250}.; FUNCTION: Angiostatin is an angiogenesis inhibitor that blocks neovascularization and growth of experimental primary and metastatic tumors in vivo. PTM: In the presence of the inhibitor, the activation involves only cleavage after Arg-581, yielding two chains held together by two disulfide bonds. In the absence of the inhibitor, the activation involves additionally the removal of the activation peptide (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Locates to the cell surface where it is proteolytically cleaved to produce the active plasmin. Interaction with HRG tethers it to the cell surface (By similarity). {ECO:0000250}. SUBUNIT: Interacts (both mature PLG and the angiostatin peptide) with AMOT and CSPG4. Interacts (via the Kringle domains) with HRG; the interaction tethers PLG to the cell surface and enhances its activation. Interacts (via Kringle 4 domain) with ADA; the interaction stimulates PLG activation when in complex with DPP4. Angiostatin: Interacts with ATP5F1A; the interaction inhibits most of the angiogenic effects of angiostatin. {ECO:0000250|UniProtKB:P00747}. DOMAIN: Kringle domains mediate interaction with CSPG4. {ECO:0000250}. +Q4KWH5 PLCH1_MOUSE 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase eta-1 (EC 3.1.4.11) (Phosphoinositide phospholipase C-eta-1) (Phospholipase C-eta-1) (PLC-eta-1) (Phospholipase C-like protein 3) (PLC-L3) 1682 187,743 Active site (2); Alternative sequence (9); Binding site (4); Calcium binding (1); Chain (1); Compositional bias (2); Domain (6); Metal binding (10); Sequence conflict (2) FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by calcium-activated phosphatidylinositol-specific phospholipase C enzymes. {ECO:0000269|PubMed:15702972}. SUBCELLULAR LOCATION: Cytoplasm. Membrane {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain and to a lower extent in lung. In brain, it is found in cerebrum, cerebellum and spinal cord. {ECO:0000269|PubMed:15702972}. +A2AP18 PLCH2_MOUSE 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase eta-2 (EC 3.1.4.11) (Phosphoinositide phospholipase C-eta-2) (Phosphoinositide phospholipase C-like 4) (PLC-L4) (Phospholipase C-like protein 4) (Phospholipase C-eta-2) (PLC-eta2) 1501 164,297 Active site (2); Alternative sequence (9); Binding site (4); Calcium binding (1); Chain (1); Compositional bias (1); Domain (6); Erroneous gene model prediction (2); Erroneous initiation (1); Erroneous termination (1); Metal binding (10); Modified residue (4); Mutagenesis (1); Region (1); Sequence caution (1); Sequence conflict (5) FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. This phospholipase activity is very sensitive to calcium. May be important for formation and maintenance of the neuronal network in the postnatal brain. {ECO:0000269|PubMed:15899900, ECO:0000269|PubMed:16107206}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15899900}. Cell membrane {ECO:0000269|PubMed:15899900}. Note=Localized predominantly at the plasma membrane. TISSUE SPECIFICITY: Specifically detected in the brain, with higher level in cerebral cortex, olfactory bulb and hippocampus (at protein level). Expressed in the pyramidal cells of the hippocampus, but also in eye and lung. {ECO:0000269|PubMed:15899900, ECO:0000269|PubMed:16107206}. +Q3USB7 PLCL1_MOUSE Inactive phospholipase C-like protein 1 (PLC-L1) (Phospholipase C-related but catalytically inactive protein) (PRIP) 1096 122,673 Chain (1); Coiled coil (1); Domain (4); Modified residue (8); Mutagenesis (2); Region (2); Sequence conflict (2) FUNCTION: Involved in an inositol phospholipid-based intracellular signaling cascade. Shows no PLC activity to phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol. Component in the phospho-dependent endocytosis process of GABA A receptor. Acts as a inhibitor of PPP1C (By similarity). Involved in the assembly and/or the trafficking of gamma-2 subunit-containing GABA A receptors. {ECO:0000250, ECO:0000269|PubMed:16854455, ECO:0000269|PubMed:17301177}. PTM: Phosphorylated by the catalytic subunit of PKA. Phosphorylation of Thr-94 resulted in dissociation of PPP1C from PRIP1. {ECO:0000269|PubMed:15306641}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with PPP2CA, Ins(1,4,5)P3, Ins(1,4,5,6)P4 GABARAP, GABA receptor beta subunits, GABA receptor gamma-2 subunits and PPP1C (By similarity). May form a ternary complex with GABA receptor beta subunit and GABARAP. The formation of a ternary complex with GABA receptor beta subunit and GABARAP could be the key step for facilitating the association of GABARAP with the GABA receptor gamma-2 subunit and to allow it to be transported at the right destination. {ECO:0000250}. +Q8K394 PLCL2_MOUSE Inactive phospholipase C-like protein 2 (PLC-L(2)) (PLC-L2) (Phospholipase C-L2) (Phospholipase C-epsilon-2) (PLC-epsilon-2) 1128 125,772 Chain (1); Compositional bias (1); Domain (4); Initiator methionine (1); Modified residue (5); Sequence conflict (6) FUNCTION: May play an role in the regulation of Ins(1,4,5)P3 around the endoplasmic reticulum. {ECO:0000269|PubMed:10581172}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10581172}. Note=Predominantly localized to perinuclear areas in both myoblast and myotube C2C12 cells. TISSUE SPECIFICITY: Ubiquitously expressed, with a strong expression in skeletal muscle. {ECO:0000269|PubMed:10581172}. +Q8CHS4 PLCX1_MOUSE PI-PLC X domain-containing protein 1 345 38,718 Chain (1); Domain (1); Sequence conflict (1) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NUJ7}. TISSUE SPECIFICITY: Expressed at highest levels in brain and kidney. Also detected in stomach, thymus and skeletal muscle. {ECO:0000269|PubMed:22732399}. +Q9R0E2 PLOD1_MOUSE Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1 (EC 1.14.11.4) (Lysyl hydroxylase 1) (LH1) 728 83,595 Active site (1); Chain (1); Domain (1); Glycosylation (3); Metal binding (3); Signal peptide (1) FUNCTION: Part of a complex composed of PLOD1, P3H3 and P3H4 that catalyzes hydroxylation of lysine residues in collagen alpha chains and is required for normal assembly and cross-linkling of collagen fibrils (PubMed:27119146). Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens (By similarity). These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links (PubMed:27119146). {ECO:0000250|UniProtKB:P24802, ECO:0000269|PubMed:27119146}. SUBCELLULAR LOCATION: Rough endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side. SUBUNIT: Homodimer (By similarity). Identified in a complex with P3H3 and P3H4 (PubMed:27119146). {ECO:0000250|UniProtKB:P24802, ECO:0000269|PubMed:27119146}. TISSUE SPECIFICITY: Highly expressed in the liver, heart, lung, skeletal muscle and kidney. {ECO:0000269|PubMed:10429951}. +Q9R0B9 PLOD2_MOUSE Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2 (EC 1.14.11.4) (Lysyl hydroxylase 2) (LH2) 737 84,488 Active site (1); Chain (1); Domain (1); Glycosylation (6); Metal binding (3); Modified residue (3); Sequence conflict (4); Signal peptide (1) FUNCTION: Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links. {ECO:0000250|UniProtKB:P24802}. SUBCELLULAR LOCATION: Rough endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P24802}. TISSUE SPECIFICITY: Is highly expressed in the heart, lung, kidney, eye, ovary and placenta. {ECO:0000269|PubMed:10429951}. +P70207 PLXA2_MOUSE Plexin-A2 (Plex 2) (Plexin-2) 1894 211,535 Beta strand (54); Chain (1); Coiled coil (1); Disulfide bond (10); Domain (5); Erroneous initiation (2); Glycosylation (9); Helix (15); Modified residue (1); Mutagenesis (3); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (14) TRANSMEM 1238 1258 Helical. {ECO:0000255}. TOPO_DOM 35 1237 Extracellular. {ECO:0000255}.; TOPO_DOM 1259 1894 Cytoplasmic. {ECO:0000255}. FUNCTION: Coreceptor for SEMA3A and SEMA6A. Necessary for signaling by SEMA6A and class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance, invasive growth and cell migration. Class 3 semaphorins bind to a complex composed of a neuropilin and a plexin. The plexin modulates the affinity of the complex for specific semaphorins, and its cytoplasmic domain is required for the activation of down-stream signaling events in the cytoplasm. {ECO:0000269|PubMed:10520994, ECO:0000269|PubMed:10781943, ECO:0000269|PubMed:20877282}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20877282, ECO:0000269|PubMed:20881961}; Single-pass type I membrane protein {ECO:0000269|PubMed:20877282, ECO:0000269|PubMed:20881961}. SUBUNIT: Homodimer. Interacts with RND1 (By similarity). Interacts directly with NRP1 and NRP2. The PLXNA2 homodimer interacts with a SEMA6A homodimer, giving rise to a heterotetramer. {ECO:0000250, ECO:0000269|PubMed:10520994, ECO:0000269|PubMed:10781943, ECO:0000269|PubMed:20877282, ECO:0000269|PubMed:20881961}. +P70208 PLXA3_MOUSE Plexin-A3 1872 207,958 Alternative sequence (1); Beta strand (8); Chain (1); Coiled coil (1); Disulfide bond (10); Domain (5); Glycosylation (3); Helix (29); Modified residue (1); Mutagenesis (8); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (9) TRANSMEM 1221 1241 Helical. {ECO:0000255}. TOPO_DOM 20 1220 Extracellular. {ECO:0000255}.; TOPO_DOM 1242 1872 Cytoplasmic. {ECO:0000255}. FUNCTION: Coreceptor for SEMA3A and SEMA3F. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance in the developing nervous system. Regulates the migration of sympathetic neurons, but not of neural crest precursors. Required for normal dendrite spine morphology in pyramidal neurons. May play a role in regulating semaphorin-mediated programmed cell death in the developing nervous system. Class 3 semaphorins bind to a complex composed of a neuropilin and a plexin. The plexin modulates the affinity of the complex for specific semaphorins, and its cytoplasmic domain is required for the activation of down-stream signaling events in the cytoplasm. {ECO:0000269|PubMed:11683995, ECO:0000269|PubMed:18262512, ECO:0000269|PubMed:18804103, ECO:0000269|PubMed:19020035, ECO:0000269|PubMed:19717441, ECO:0000269|PubMed:20010807}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. TISSUE SPECIFICITY: Detected in embryonic hindbrain, spinal cord, dorsal root ganglion, trigeminal ganglion and superior cervical ganglion. In newborns, detected throughout all layers of the hippocampus. {ECO:0000269|PubMed:11683995, ECO:0000269|PubMed:18804103, ECO:0000269|PubMed:8806646}. +Q60696 PMEL_MOUSE Melanocyte protein PMEL (Melanocyte protein Pmel 17) (Premelanosome protein) (Silver locus protein) [Cleaved into: M-alpha; M-beta] 626 65,980 Chain (3); Domain (1); Glycosylation (4); Natural variant (5); Region (1); Repeat (7); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 563 583 Helical. {ECO:0000255}. TOPO_DOM 437 562 Lumenal. {ECO:0000255}.; TOPO_DOM 584 626 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a central role in the biogenesis of melanosomes. Involved in the maturation of melanosomes from stage I to II. The transition from stage I melanosomes to stage II melanosomes involves an elongation of the vesicle, and the appearance within of distinct fibrillar structures (By similarity). {ECO:0000250}. PTM: A small amount of P1/P100 (major form) undergoes glycosylation to yield P2/P120 (minor form). P2 is cleaved by a furin-like proprotein convertase (PC) in a pH-dependent manner in a post-Golgi, prelysosomal compartment into two disulfide-linked subunits: a large lumenal subunit, M-alpha/ME20-S, and an integral membrane subunit, M-beta. Despite cleavage, only a small fraction of M-alpha is secreted, whereas most M-alpha and M-beta remain associated with each other intracellularly. M-alpha is further processed to M-alpha N and M-alpha C. M-alpha C further undergoes processing to yield M-alpha C1 and M-alpha C3 (M-alpha C2 in the case of PMEL17-is or PMEL17-ls). Formation of intralumenal fibrils in the melanosomes requires the formation of M-alpha that becomes incorporated into the fibrils. Stage II melanosomes harbor only Golgi-modified Pmel17 fragments that are derived from M-alpha and that bear sialylated O-linked oligosaccharides (By similarity). {ECO:0000250}.; PTM: N-glycosylated. O-glycosylated; contains sialic acid (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Golgi apparatus {ECO:0000250}. Melanosome {ECO:0000250}. Endosome, multivesicular body {ECO:0000250}. Note=Localizes predominantly to intralumenal vesicles (ILVs) within multivesicular bodies. Associates with ILVs found within the lumen of premelanosomes and melanosomes and particularly in compartments that serve as precursors to the striated stage II premelanosomes (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: M-alpha: Secreted {ECO:0000250}. SUBUNIT: Heterooligomer; disulfide-linked heterooligomers of M-alpha and M-beta. Interacts with MLANA. Interacts (via luminal domain) with CD63; this is important for normal sorting of the luminal domain after proteolytic processing (By similarity). {ECO:0000250}. DOMAIN: The RPT domain is essential for the generation of the fibrillar matrix of melanosomes. {ECO:0000250}.; DOMAIN: The lumenal domain is necessary for correct processing and trafficking to melanosomes. {ECO:0000250}. TISSUE SPECIFICITY: Preferentially expressed in melanocytes. DISEASE: Note=Defects in Silv are the cause of the silver coat color which seems to be due to premature death of pigment cells during the hair cycle. +B2RXS4 PLXB2_MOUSE Plexin-B2 1842 206,230 Beta strand (9); Chain (1); Disulfide bond (10); Domain (4); Glycosylation (8); Helix (24); Modified residue (3); Sequence conflict (1); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1); Turn (7) TRANSMEM 1202 1222 Helical. {ECO:0000255}. TOPO_DOM 20 1201 Extracellular. {ECO:0000255}.; TOPO_DOM 1223 1842 Cytoplasmic. {ECO:0000255}. FUNCTION: Cell surface receptor for SEMA4C, SEMA4D and SEMA4G that plays an important role in cell-cell signaling. Binding to class 4 semaphorins promotes downstream activation of RHOA and phosphorylation of ERBB2 at 'Tyr-1248'. Required for normal differentiation and migration of neuronal cells during brain corticogenesis and for normal embryonic brain development. Regulates the migration of cerebellar granule cells in the developing brain. Plays a role in RHOA activation and subsequent changes of the actin cytoskeleton. Plays a role in axon guidance, invasive growth and cell migration. May modulate the activity of RAC1 and CDC42. Down-regulates macrophage migration in wound-healing assays (in vitro). {ECO:0000269|PubMed:17554007, ECO:0000269|PubMed:19948886, ECO:0000269|PubMed:21122816, ECO:0000269|PubMed:21966369}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21966369}; Single-pass type I membrane protein {ECO:0000269|PubMed:21966369}. SUBUNIT: Monomer, and heterodimer with PLXNB1. Binds MET, ARHGEF11 and ARHGEF12. May also interact with MST1R (By similarity). Interacts with SEMA4C, SEMA4D and SEMA4G. {ECO:0000250, ECO:0000269|PubMed:17554007, ECO:0000269|PubMed:21122816}. TISSUE SPECIFICITY: Detected in macrophages from spleen and bone marrow (at protein level). Detected in granule cells in the developing cerebellum, dentate gyrus and olfactory bulb. {ECO:0000269|PubMed:17554007, ECO:0000269|PubMed:21966369}. +Q69ZP3 PNKD_MOUSE Probable hydrolase PNKD (EC 3.-.-.-) (Myofibrillogenesis regulator 1) (MR-1) (Paroxysmal nonkinesiogenic dyskinesia protein) 385 43,017 Alternative sequence (4); Chain (1); Erroneous initiation (2); Metal binding (8); Modified residue (1); Region (2); Sequence conflict (1) FUNCTION: Probable hydrolase that plays an aggravative role in the development of cardiac hypertrophy via activation of the NF-kappa-B signaling pathway. {ECO:0000269|PubMed:17420335}. SUBCELLULAR LOCATION: Isoform 1: Membrane; Peripheral membrane protein.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Nucleus.; SUBCELLULAR LOCATION: Isoform 4: Mitochondrion {ECO:0000250}. SUBUNIT: Isoform 2 interacts with the sarcomeric proteins, MRLC2, MYOM1 and ENO3. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in many discrete areas of the brain. {ECO:0000269|PubMed:15496428}. +A2AR50 RGPS1_MOUSE Ras-specific guanine nucleotide-releasing factor RalGPS1 (Ral GEF with PH domain and SH3-binding motif 1) (Ral guanine nucleotide exchange factor 2) (RalGEF 2) (RalA exchange factor RalGPS1) 585 65,475 Alternative sequence (5); Beta strand (7); Chain (1); Compositional bias (1); Domain (2); Erroneous gene model prediction (2); Erroneous initiation (1); Erroneous termination (1); Frameshift (1); Helix (2); Motif (1); Region (1); Sequence conflict (13) FUNCTION: Guanine nucleotide exchange factor for the small GTPase RALA. May be involved in cytoskeleton organization. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Associates with membranes through the PH domain. {ECO:0000250}. SUBUNIT: Interacts with the SH3 domains of GRB2, NCK1, PLCG1 and SRC. {ECO:0000250}. DOMAIN: The PH domain mediates binding to membranes. It is required for efficient GEF activity. {ECO:0000250}. +Q9JLV6 PNKP_MOUSE Bifunctional polynucleotide phosphatase/kinase (DNA 5'-kinase/3'-phosphatase) (Polynucleotide kinase-3'-phosphatase) [Includes: Polynucleotide 3'-phosphatase (EC 3.1.3.32) (2'(3')-polynucleotidase); Polynucleotide 5'-hydroxyl-kinase (EC 2.7.1.78)] 522 57,223 Alternative sequence (1); Beta strand (30); Chain (1); Domain (1); Helix (17); Modified residue (3); Mutagenesis (3); Nucleotide binding (1); Region (2); Sequence conflict (2); Turn (4) FUNCTION: Plays a key role in the repair of DNA damage, functioning as part of both the non-homologous end-joining (NHEJ) and base excision repair (BER) pathways. Through its two catalytic activities, PNK ensures that DNA termini are compatible with extension and ligation by either removing 3'-phosphates from, or by phosphorylating 5'-hydroxyl groups on, the ribose sugar of the DNA backbone. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000269|PubMed:15749016}. DOMAIN: The FHA domain binds threonine-phosphorylated peptides from XRCC1/4, and is responsible for the recruitment of PNKP to the sites of DNA repair. The affinity is ten times greater if peptides are also phosphorylated on the serine preceeding the phosphothreonine. {ECO:0000269|PubMed:15749016}. +P27671 RGRF1_MOUSE Ras-specific guanine nucleotide-releasing factor 1 (Ras-GRF1) (CDC25Mm) (Guanine nucleotide-releasing protein) (GNRP) (Ras-specific nucleotide exchange factor CDC25) 1262 144,102 Chain (1); Domain (6); Helix (14); Modified residue (5); Mutagenesis (2); Sequence conflict (1) FUNCTION: Promotes the exchange of Ras-bound GDP by GTP. {ECO:0000269|PubMed:10373510}. PTM: Phosphorylated by PLK2, leading to ubiquitination and degradation by the proteasome. {ECO:0000250}.; PTM: Ubiquitinated and degraded following phosphorylation by PLK2. {ECO:0000305|PubMed:11500497}.; PTM: Phosphorylated by SRC and LCK. Phosphorylation by LCK increases its capacity to stimulate the GDP/GTP exchange on Ras, whereas its phosphorylation by SRC seems not to have an effect on stimulation activity (By similarity). {ECO:0000250}. SUBUNIT: Homooligomer and heterooligomer with RASGRF2. Interacts with USP8, thereby regulating its stability. {ECO:0000269|PubMed:10373510, ECO:0000269|PubMed:11500497}. DOMAIN: The DH (DBL-homology) domain mediates interaction with RASGRF2. TISSUE SPECIFICITY: Brain. +P70392 RGRF2_MOUSE Ras-specific guanine nucleotide-releasing factor 2 (Ras-GRF2) (Ras guanine nucleotide exchange factor 2) 1189 135,668 Chain (1); Coiled coil (1); Domain (6); Modified residue (8); Mutagenesis (2); Region (2); Sequence conflict (4) FUNCTION: Functions as a calcium-regulated nucleotide exchange factor activating both Ras and RAC1 through the exchange of bound GDP for GTP. Preferentially activates HRAS in vivo compared to RRAS based on their different types of prenylation. Functions in synaptic plasticity by contributing to the induction of long term potentiation. {ECO:0000269|PubMed:10733575, ECO:0000269|PubMed:11500499, ECO:0000269|PubMed:14749369, ECO:0000269|PubMed:15029245, ECO:0000269|PubMed:16407208, ECO:0000269|PubMed:16467520, ECO:0000269|PubMed:9032266, ECO:0000269|PubMed:9707409}. PTM: Phosphorylated by CDK5; down-regulates RASGRF2-mediated RAC1 activation. {ECO:0000269|PubMed:11238945, ECO:0000269|PubMed:15128856}.; PTM: Ubiquitinated upon interaction with Ras. Ubiquitination leads to degradation through the 26S proteasome. {ECO:0000269|PubMed:11238945}. SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Peripheral membrane protein. Note=Translocates to membranes when activated. Found both at cell periphery and along the axon of neurons (By similarity). {ECO:0000250}. SUBUNIT: Homooligomer and heterooligomer with RASGRF1. Interacts with Ras and RAC1. Interacts in a calcium-dependent manner with calmodulin. Interacts with EPB49 and probably CDK5R1. Interacts with the AMPA receptor through GRIA1. Interacts with microtubules. {ECO:0000269|PubMed:10373510, ECO:0000269|PubMed:11856323, ECO:0000269|PubMed:16407208, ECO:0000269|PubMed:16649990, ECO:0000269|PubMed:9032266, ECO:0000269|PubMed:9707409}. DOMAIN: The Ras-GEF domain and the N-terminal Ras-GEF domain form a Ras-binding site and mediate Ras activation. {ECO:0000250}.; DOMAIN: The IQ domain mediates the calcium-dependent interaction with calmodulin but is dispensable for the Ras-GEF activity.; DOMAIN: The DH (DBL-homology) domain mediates interaction with RASGRF1 and probably EPB49 and is required for RAC1 activation. TISSUE SPECIFICITY: Expressed in brain in the nucleus of the solitary tract. Not observed in the hippocampus (at protein level). {ECO:0000269|PubMed:11909944}. +Q99MZ7 PECR_MOUSE Peroxisomal trans-2-enoyl-CoA reductase (TERP) (EC 1.3.1.38) 303 32,410 Active site (1); Chain (1); Initiator methionine (1); Modified residue (9); Motif (1); Nucleotide binding (1); Sequence conflict (4) Lipid metabolism; fatty acid biosynthesis. FUNCTION: Participates in chain elongation of fatty acids. Has no 2,4-dienoyl-CoA reductase activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}. SUBUNIT: Interacts with PEX5, probably required to target it into peroxisomes. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in liver and kidney. Expressed at lowe level in heart and skeletal muscle. Expressed at weak level in other tissues. {ECO:0000269|PubMed:10811639}. +Q9D7R7 PEPC_MOUSE Gastricsin (EC 3.4.23.3) (Pepsinogen C) 392 42,849 Active site (2); Chain (1); Disulfide bond (3); Domain (1); Frameshift (1); Propeptide (1); Signal peptide (1) FUNCTION: Hydrolyzes a variety of proteins. SUBCELLULAR LOCATION: Secreted. +O54943 PER2_MOUSE Period circadian protein homolog 2 (mPER2) (Circadian clock protein PERIOD 2) 1257 135,881 Beta strand (14); Chain (1); Compositional bias (2); Domain (3); Helix (15); Modified residue (17); Motif (6); Mutagenesis (10); Region (4); Sequence conflict (2); Turn (8) FUNCTION: Transcriptional repressor which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, ARNTL/BMAL1, ARNTL2/BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndrome and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and ARNTL/BMAL1 or ARNTL2/BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-ARNTL/BMAL1|ARNTL2/BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress ARNTL/BMAL1 transcription, respectively. PER1 and PER2 proteins transport CRY1 and CRY2 into the nucleus with appropriate circadian timing, but also contribute directly to repression of clock-controlled target genes through interaction with several classes of RNA-binding proteins, helicases and others transcriptional repressors. PER appears to regulate circadian control of transcription by at least three different modes. First, interacts directly with the CLOCK-ARTNL/BMAL1 at the tail end of the nascent transcript peak to recruit complexes containing the SIN3-HDAC that remodel chromatin to repress transcription. Second, brings H3K9 methyltransferases such as SUV39H1 and SUV39H2 to the E-box elements of the circadian target genes, like PER2 itself or PER1. The recruitment of each repressive modifier to the DNA seems to be very precisely temporally orchestrated by the large PER complex, the deacetylases acting before than the methyltransferases. Additionally, large PER complexes are also recruited to the target genes 3' termination site through interactions with RNA-binding proteins and helicases that may play a role in transcription termination to regulate transcription independently of CLOCK-ARTNL/BMAL1 interactions. Recruitment of large PER complexes to the elongating polymerase at PER and CRY termination sites inhibited SETX action, impeding RNA polymerase II release and thereby repressing transcriptional reinitiation. May propagate clock information to metabolic pathways via the interaction with nuclear receptors. Coactivator of PPARA and corepressor of NR1D1, binds rhythmically at the promoter of nuclear receptors target genes like ARNTL or G6PC. Directly and specifically represses PPARG proadipogenic activity by blocking PPARG recruitment to target promoters and thereby transcriptional activation. Required for fatty acid and lipid metabolism, is involved as well in the regulation of circulating insulin levels. Plays an important role in the maintenance of cardiovascular functions through the regulation of NO and vasodilatatory prostaglandins production in aortas. Controls circadian glutamate uptake in synaptic vesicles through the regulation of VGLUT1 expression. May also be involved in the regulation of inflammatory processes. Represses the CLOCK-ARNTL/BMAL1 induced transcription of BHLHE40/DEC1 and ATF4. Negatively regulates the formation of the TIMELESS-CRY1 complex by competing with TIMELESS for binding to CRY1. {ECO:0000269|PubMed:10428031, ECO:0000269|PubMed:11395012, ECO:0000269|PubMed:16595674, ECO:0000269|PubMed:17310242, ECO:0000269|PubMed:17404161, ECO:0000269|PubMed:19605937, ECO:0000269|PubMed:19917250, ECO:0000269|PubMed:20159955, ECO:0000269|PubMed:21035761, ECO:0000269|PubMed:21680841, ECO:0000269|PubMed:21768648, ECO:0000269|PubMed:21930935, ECO:0000269|PubMed:22504074, ECO:0000269|PubMed:22767893, ECO:0000269|PubMed:23418588, ECO:0000269|PubMed:23977055, ECO:0000269|PubMed:24413057}. PTM: Acetylated. Deacetylated by SIRT1, resulting in decreased protein stability. {ECO:0000269|PubMed:18662546}.; PTM: Phosphorylated by CSNK1E and CSNK1D. Phosphorylation results in PER2 protein degradation. May be dephosphorylated by PP1. {ECO:0000269|PubMed:11865049, ECO:0000269|PubMed:14701732, ECO:0000269|PubMed:16097765, ECO:0000269|PubMed:19414593, ECO:0000269|PubMed:21930935}.; PTM: Ubiquitinated, leading to its proteasomal degradation. Ubiquitination may be inhibited by CRY1. {ECO:0000269|PubMed:11889036}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22208286}. Cytoplasm {ECO:0000269|PubMed:22208286}. Cytoplasm, perinuclear region. Note=Nucleocytoplasmic shuttling is effected by interaction with other circadian core oscillator proteins and/or by phosphorylation. Translocate to the nucleus after phosphorylation by CSNK1D or CSNK1E. Also translocated to the nucleus by CRY1 or CRY2. PML regulates its nuclear localization. SUBUNIT: Homodimer. Component of the circadian core oscillator, which includes the CRY proteins, CLOCK or NPAS2, ARTNL/BMAL1 or ARTNL2/BMAL2, CSNK1D and/or CSNK1E, TIMELESS, and the PER proteins. Interacts with CLOCK-ARNTL/BMAL1 (off DNA). Interacts with ARNTL2/BMAL2. Interacts directly with PER1 and PER3, and through a C-terminal domain, with CRY1 and CRY2. Interacts, via its second PAS domain, with TIMELESS in vitro. Interacts with NFIL3. Different large complexes have been identified with different repressive functions. The core of PER complexes is composed of at least PER1, PER2, PER3, CRY1, CRY2, CSNK1D and/or CSNK1E. The large PER complex involved in the repression of transcriptional termination is composed of at least PER2, CDK9, DDX5, DHX9, NCBP1 and POLR2A (active). The large PER complex involved in the histone deacetylation is composed of at least HDAC1, PER2, SFPQ and SIN3A. The large PER complex involved in the histone methylation is composed of at least PER2, CBX3, TRIM28, SUV39H1 and/or SUV39H2; CBX3 mediates the formation of the complex. Interacts with SETX; the interaction inhibits termination of circadian target genes. Interacts with the nuclear receptors HNF4A, NR1D1, NR4A2, RORA, PPARA, PPARG and THRA; the interaction with at least PPARG is ligand dependent. Interacts with PML. Interacts (phosphorylated) with BTRC and FBXW11; the interactions trigger proteasomal degradation. Interacts with NONO and SFPQ. Interacts with SIRT1. Interacts with CAVIN3. Interacts with MAGEL2. Interacts with MAP1LC3B (PubMed:29937374). {ECO:0000269|PubMed:10428031, ECO:0000269|PubMed:10848614, ECO:0000269|PubMed:11889036, ECO:0000269|PubMed:14701732, ECO:0000269|PubMed:16478995, ECO:0000269|PubMed:17274955, ECO:0000269|PubMed:18662546, ECO:0000269|PubMed:18782782, ECO:0000269|PubMed:19402751, ECO:0000269|PubMed:19605937, ECO:0000269|PubMed:19917250, ECO:0000269|PubMed:20159955, ECO:0000269|PubMed:20840750, ECO:0000269|PubMed:21035761, ECO:0000269|PubMed:21613214, ECO:0000269|PubMed:21680841, ECO:0000269|PubMed:22208286, ECO:0000269|PubMed:22274616, ECO:0000269|PubMed:22767893, ECO:0000269|PubMed:22966205, ECO:0000269|PubMed:23079727, ECO:0000269|PubMed:23418588, ECO:0000269|PubMed:24385426, ECO:0000269|PubMed:24413057, ECO:0000269|PubMed:29937374, ECO:0000269|PubMed:9856465}. TISSUE SPECIFICITY: In the brain, high expression in SCN during the subjective day. Constitutive expression in the cornu ammonis and in the dentate gyrus of the hyppocampus. Also expressed in the piriform cortex and the glomeruli of the olfactory bulb, and at a lower extent in the cerebral cortex. Not expressed in the pars tuberalis and the Purkinje neurons. Also expressed in adipose tissue (white and brown), heart, kidney, bladder, lumbar spinal cord, skeletal muscle, spleen, lung, pancreas and liver with highest levels in skeletal muscle and liver and lowest levels in spleen. {ECO:0000269|PubMed:15860628, ECO:0000269|PubMed:21035761, ECO:0000269|PubMed:23531614, ECO:0000269|PubMed:24154698, ECO:0000269|PubMed:24603368, ECO:0000269|PubMed:9427249, ECO:0000269|PubMed:9428527}. +P10820 PERF_MOUSE Perforin-1 (P1) (Cytolysin) (Lymphocyte pore-forming protein) 554 62,081 Beta strand (25); Chain (1); Disulfide bond (9); Domain (3); Glycosylation (3); Helix (15); Metal binding (6); Mutagenesis (4); Sequence conflict (6); Signal peptide (1); Site (2); Turn (8) FUNCTION: Plays a key role in secretory granule-dependent cell death, and in defense against virus-infected or neoplastic cells. Can insert into the membrane of target cells in its calcium-bound form, oligomerize and form large pores. Promotes cytolysis and apoptosis of target cells by facilitating the uptake of cytotoxic granzymes. {ECO:0000269|PubMed:19446473, ECO:0000269|PubMed:21037563, ECO:0000269|PubMed:3261391, ECO:0000269|PubMed:7526382, ECO:0000269|PubMed:8164737}. PTM: N-glycosylated. The glycosylation sites are facing the interior of the pore. {ECO:0000269|PubMed:21037563}. SUBCELLULAR LOCATION: Cytoplasmic granule lumen. Secreted. Cell membrane; Multi-pass membrane protein. Endosome lumen {ECO:0000250}. Note=Stored in cytoplasmic granules of cytolytic T-lymphocytes and secreted into the cleft between T-lymphocyte and target cell. May be taken up via endocytosis involving clathrin-coated vesicles and accumulate in a first time in large early endosomes (By similarity). Inserts into the cell membrane of target cells and forms pores. Membrane insertion and pore formation requires a major conformation change. {ECO:0000250}. SUBUNIT: Monomer, as soluble protein. Homooligomer. Oligomerization is required for pore formation. {ECO:0000269|PubMed:19446473, ECO:0000269|PubMed:21037563}. DOMAIN: The C2 domain mediates calcium-dependent binding to lipid membranes. A subsequent conformation change leads to membrane insertion of beta-hairpin structures and pore formation. The pore is formed by transmembrane beta-strands. TISSUE SPECIFICITY: Detected in cytotoxic T-lymphocytes and natural killer cells. {ECO:0000269|PubMed:2040805, ECO:0000269|PubMed:2783486, ECO:0000269|PubMed:3261391}. +Q149B8 PERM1_MOUSE PGC-1 and ERR-induced regulator in muscle protein 1 (PPARGC1 and ESRR-induced regulator in muscle 1) (Peroxisome proliferator-activated receptor gamma coactivator 1 and estrogen-related receptor-induced regulator in muscle 1) 807 85,157 Chain (1); Erroneous termination (1); Frameshift (1); Modified residue (3); Sequence conflict (12) FUNCTION: Regulates the expression of selective PPARGC1A/B and ESRRA/B/G target genes with roles in glucose and lipid metabolism, energy transfer, contractile function, muscle mitochondrial biogenesis and oxidative capacity. Required for the efficient induction of MT-CO2, MT-CO3, COX4I1, TFB1M, TFB2M, POLRMT and SIRT3 by PPARGC1A. Positively regulates the PPARGC1A/ESRRG-induced expression of CKMT2, TNNI3 and SLC2A4 and negatively regulates the PPARGC1A/ESRRG-induced expression of PDK4. {ECO:0000269|PubMed:23836911}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23836911}. Nucleus {ECO:0000269|PubMed:23836911}. Note=Shows a nuclear localization in the presence of PPARGC1A. TISSUE SPECIFICITY: Highly expressed in skeletal muscles and heart with lower levels in brown adipose tissue (at protein level). Muscle-specific expression is increased by endurance exercise. {ECO:0000269|PubMed:23836911}. +Q6ZPK0 PF21A_MOUSE PHD finger protein 21A (BHC80a) (BRAF35-HDAC complex protein BHC80) (mBHC80) 659 72,521 Alternative sequence (6); Chain (1); Coiled coil (1); Compositional bias (1); Cross-link (1); DNA binding (1); Erroneous initiation (1); Modified residue (2); Sequence conflict (2); Zinc finger (1) FUNCTION: Component of the BHC complex, a corepressor complex that represses transcription of neuron-specific genes in non-neuronal cells. The BHC complex is recruited at RE1/NRSE sites by REST and acts by deacetylating and demethylating specific sites on histones, thereby acting as a chromatin modifier. In the BHC complex, it may act as a scaffold. Inhibits KDM1A-mediated demethylation of 'Lys-4' of histone H3 in vitro, suggesting a role in demethylation regulation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15325272}. SUBUNIT: Component of a BHC histone deacetylase complex that contains HDAC1, HDAC2, HMG20B/BRAF35, KDM1A, RCOR1/CoREST and PHF21A/BHC80. The BHC complex may also contain ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I. In the complex, it interacts directly with HDAC1, HDAC2, HMG20B/BRAF35, KDM1A and RCOR1/CoREST (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the brain and testis. Weakly or not expressed in other tissues tested. Localized throughout the central nervous system (CNS) in brain, including the cerebellum, hippocampus, and cortex. Notably present in neuronal cells of granular cell layer and dentate gyrus in cerebellum and hippocampus, respectively. In the seminiferous tubules, the signals it is present strongly in spermatocytes, and weakly in spermatogonia and round spermatids. In some cases, it is also observed solely in spermatocytes (at protein level). {ECO:0000269|PubMed:15325272}. +Q8BGI5 PEX26_MOUSE Peroxisome assembly protein 26 (Peroxin-26) 305 34,016 Alternative sequence (1); Chain (1); Topological domain (2); Transmembrane (1) TRANSMEM 247 267 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 246 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 268 305 Peroxisomal matrix. {ECO:0000255}. FUNCTION: Probably required for protein import into peroxisomes. Anchors PEX1 and PEX6 to peroxisome membranes, possibly to form heteromeric AAA ATPase complexes required for the import of proteins into peroxisomes. Involved in the import of catalase and proteins containing a PTS2 target sequence, but not in import of proteins with a PTS1 target sequence (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. SUBUNIT: Interacts directly with PEX6 via its cytoplasmic domain. Interacts indirectly with PEX1, via its interaction with PEX6 (By similarity). {ECO:0000250}. +O70591 PFD2_MOUSE Prefoldin subunit 2 154 16,534 Chain (1); Sequence conflict (1) FUNCTION: Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Mitochondrion {ECO:0000250}. SUBUNIT: Interacts with URI1; the interaction is phosphorylation-dependent and occurs in a growth-dependent manner (By similarity). Heterohexamer of two PFD-alpha type and four PFD-beta type subunits. Binds to c-Myc; interacts with its N-terminal domain. {ECO:0000250}. +P55098 PEX2_MOUSE Peroxisome biogenesis factor 2 (Peroxin-2) (Peroxisomal membrane protein 3) (Peroxisome assembly factor 1) (PAF-1) 305 34,732 Chain (1); Sequence conflict (12); Transmembrane (2); Zinc finger (1) TRANSMEM 140 159 Helical. {ECO:0000255}.; TRANSMEM 195 213 Helical. {ECO:0000255}. FUNCTION: Somewhat implicated in the biogenesis of peroxisomes. SUBCELLULAR LOCATION: Peroxisome membrane; Multi-pass membrane protein. +Q9D4J7 PHF6_MOUSE PHD finger protein 6 364 41,139 Alternative sequence (1); Chain (1); Cross-link (2); Erroneous initiation (1); Frameshift (1); Initiator methionine (1); Modified residue (7); Motif (3); Region (2); Zinc finger (4) FUNCTION: Transcriptional regulator that associates with ribosomal RNA promoters and suppresses ribosomal RNA (rRNA) transcription. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q8IWS0}. Note=Nuclear, it particularly localizes to the nucleolus. {ECO:0000250}. SUBUNIT: Interacts with UBTF. Interacts with the NuRD complex component RBBP4 (via the nucleolar localization motif), the interaction mediates transcriptional repression activity (By similarity). {ECO:0000250}. DOMAIN: The PHD-type zinc finger 1 mediates both nucleolar localization and interaction with UBTF. {ECO:0000250}.; DOMAIN: The ePHD2 domain folds as an integrated structural module comprizing the C2HC pre-PHD-type 2 zinc finger and the PHD-type 2 zinc finger. It mediates non-specific binding to dsDNA, but doesn't bind histones in contrast to many PHD-type zinc fingers. {ECO:0000250|UniProtKB:Q8IWS0}. TISSUE SPECIFICITY: At 12.5 dpc it is highly expressed in the embryonic central nervous system and at lower levels in other tissues. Very low levels present throughout the adult brain. {ECO:0000269|PubMed:12415272}. +Q80TJ7 PHF8_MOUSE Histone lysine demethylase PHF8 (EC 1.14.11.27) (PHD finger protein 8) 1023 113,553 Alternative sequence (5); Beta strand (4); Binding site (2); Chain (1); Compositional bias (1); Domain (1); Erroneous gene model prediction (1); Helix (2); Metal binding (3); Modified residue (13); Region (1); Turn (2); Zinc finger (1) FUNCTION: Histone lysine demethylase with selectivity for the di- and monomethyl states that plays a key role cell cycle progression, rDNA transcription and brain development. Demethylates mono- and dimethylated histone H3 'Lys-9' residue (H3K9Me1 and H3K9Me2), dimethylated H3 'Lys-27' (H3K27Me2) and monomethylated histone H4 'Lys-20' residue (H4K20Me1). Acts as a transcription activator as H3K9Me1, H3K9Me2, H3K27Me2 and H4K20Me1 are epigenetic repressive marks. Involved in cell cycle progression by being required to control G1-S transition. Acts as a coactivator of rDNA transcription, by activating polymerase I (pol I) mediated transcription of rRNA genes. Required for brain development, probably by regulating expression of neuron-specific genes. Has activity toward H4K20Me1 only when nucleosome is used as a substrate and when not histone octamer is used as substrate. May also have weak activity toward dimethylated H3 'Lys-36' (H3K36Me2), however, the relevance of this result remains unsure in vivo. Specifically binds trimethylated 'Lys-4' of histone H3 (H3K4me3), affecting histone demethylase specificity: has weak activity toward H3K9Me2 in absence of H3K4me3, while it has high activity toward H3K9me2 when binding H3K4me3. {ECO:0000250|UniProtKB:Q9UPP1}. PTM: Phosphorylation at Ser-33 and Ser-84 are required for dissociation from chromatin and accumulation of H4K20Me1 levels during prophase. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Note=Recruited to H3K4me3 sites on chromatin during interphase. Dissociates from chromatin when cells enter mitosis (By similarity). {ECO:0000250}. SUBUNIT: Interacts with POLR1B, UBTF, SETD1A, HCFC1, E2F1 and ZNF711. {ECO:0000250}. DOMAIN: The PHD-type zinc finger mediates the binding to H3K4me3. Binding to H3K4me3 promotes its access to H3K9me2 (By similarity). {ECO:0000250}.; DOMAIN: The linker region is a critical determinant of demethylase specificity. It enables the active site of JmjC to reach the target H3K9me2 when the PHD-type zinc finger binds to H3K4me3 (By similarity). {ECO:0000250}. +Q8BXA7 PHLP2_MOUSE PH domain leucine-rich repeat-containing protein phosphatase 2 (EC 3.1.3.16) (PH domain leucine-rich repeat-containing protein phosphatase-like) (PHLPP-like) 1320 145,947 Chain (1); Compositional bias (3); Domain (2); Erroneous initiation (1); Metal binding (5); Modified residue (1); Repeat (22); Sequence conflict (1) FUNCTION: Protein phosphatase involved in regulation of Akt and PKC signaling. Mediates dephosphorylation in the C-terminal domain hydrophobic motif of members of the AGC Ser/Thr protein kinase family; specifically acts on 'Ser-473' of AKT1, 'Ser-660' of PRKCB isoform beta-II and 'Ser-657' of PRKCA. Akt regulates the balance between cell survival and apoptosis through a cascade that primarily alters the function of transcription factors that regulate pro- and antiapoptotic genes. Dephosphorylation of 'Ser-473' of Akt triggers apoptosis and decreases cell proliferation. Also controls the phosphorylation of AKT3. Dephosphorylates STK4 on 'Thr-387' leading to STK4 activation and apoptosis. Dephosphorylates RPS6KB1 and is involved in regulation of cap-dependent translation. Inhibits cancer cell proliferation and may act as a tumor suppressor. Dephosphorylation of PRKCA and PRKCB leads to their destabilization and degradation. Dephosphorylates RAF1 inhibiting its kinase activity (By similarity). {ECO:0000250|UniProtKB:Q6ZVD8}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6ZVD8}. Membrane; Peripheral membrane protein {ECO:0000250|UniProtKB:Q6ZVD8}. Nucleus {ECO:0000250|UniProtKB:Q6ZVD8}. SUBUNIT: Interacts with AKT1, AKT3 and PRKCB. Interacts with STK4, RPS6KB1, RAF1. Interacts with FKBP5; FKBP5 acts as a scaffold for PHLPP2 and Akt. Interacts with SLC9A3R1; SLC9A3R1 scaffolds a heterotrimeric complex with PTEN (By similarity). {ECO:0000250|UniProtKB:Q6ZVD8}. TISSUE SPECIFICITY: Expressed in the retina. {ECO:0000269|PubMed:20089132}. +O35690 PHX2B_MOUSE Paired mesoderm homeobox protein 2B (Neuroblastoma Phox) (NBPhox) (PHOX2B homeodomain protein) (Paired-like homeobox 2B) 314 31,621 Chain (1); Compositional bias (3); DNA binding (1) SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. SUBUNIT: Interacts with TRIM11. {ECO:0000269|PubMed:18275850}. +P15974 PHXR4_MOUSE Putative per-hexamer repeat protein 4 95 10,493 Chain (1) +P08399 PHXR5_MOUSE Putative per-hexamer repeat protein 5 672 57,923 Chain (1); Compositional bias (1) +Q8R526 PK1L1_MOUSE Polycystic kidney disease protein 1-like 1 (PC1-like 1 protein) (Polycystin-1L1) (Protein rikishi) 2615 290,844 Chain (1); Domain (5); Glycosylation (9); Mutagenesis (1); Sequence conflict (5); Topological domain (12); Transmembrane (11) TRANSMEM 1525 1545 Helical. {ECO:0000255}.; TRANSMEM 1733 1753 Helical. {ECO:0000255}.; TRANSMEM 1773 1793 Helical. {ECO:0000255}.; TRANSMEM 1906 1926 Helical. {ECO:0000255}.; TRANSMEM 1951 1971 Helical. {ECO:0000255}.; TRANSMEM 2058 2078 Helical. {ECO:0000255}.; TRANSMEM 2289 2309 Helical. {ECO:0000255}.; TRANSMEM 2333 2353 Helical. {ECO:0000255}.; TRANSMEM 2380 2400 Helical. {ECO:0000255}.; TRANSMEM 2406 2426 Helical. {ECO:0000255}.; TRANSMEM 2484 2504 Helical. {ECO:0000255}. TOPO_DOM 1 1524 Extracellular. {ECO:0000255}.; TOPO_DOM 1546 1732 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1754 1772 Extracellular. {ECO:0000255}.; TOPO_DOM 1794 1905 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1927 1950 Extracellular. {ECO:0000255}.; TOPO_DOM 1972 2057 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 2079 2288 Extracellular. {ECO:0000255}.; TOPO_DOM 2310 2332 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 2354 2379 Extracellular. {ECO:0000255}.; TOPO_DOM 2401 2405 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 2427 2483 Extracellular. {ECO:0000255}.; TOPO_DOM 2505 2615 Cytoplasmic. {ECO:0000255}. FUNCTION: Component of a ciliary calcium channel that controls calcium concentration within primary cilia without affecting cytoplasmic calcium concentration. Forms a heterodimer with PKD2L1 in primary cilia and forms a calcium-permeant ciliary channel that regulates sonic hedgehog/SHH signaling and GLI2 transcription. Does not constitute the pore-forming subunit. Also involved in left/right axis specification downstream of nodal flow: forms a complex with PKD2 in cilia to facilitate flow detection in left/right patterning. {ECO:0000269|PubMed:21307093, ECO:0000269|PubMed:24336289}. SUBCELLULAR LOCATION: Cell projection, cilium membrane {ECO:0000269|PubMed:21307093}; Multi-pass membrane protein {ECO:0000269|PubMed:21307093}. SUBUNIT: Heterodimer; heterodimerizes with PKD2 proteins to form a calcium channel. Interacts with PKD2L1; to form ciliary calcium channel. Interacts with PKD2. {ECO:0000269|PubMed:21307093}. TISSUE SPECIFICITY: In testis, strong expression in Leydig cells, low level in seminal ducts, myoid cells and tunica vaginalis. Other tissues, including adrenal gland and heart myocardium, also show low expression. In embryo, highly expressed in the node. {ECO:0000269|PubMed:21307093}. +O35160 PITX3_MOUSE Pituitary homeobox 3 (Homeobox protein PITX3) (Paired-like homeodomain transcription factor 3) 302 31,715 Chain (1); Compositional bias (1); DNA binding (1); Modified residue (2); Motif (2) FUNCTION: Transcriptional regulator which is important for the differentiation and maintenance of meso-diencephalic dopaminergic (mdDA) neurons during development. In addition to its importance during development, it also has roles in the long-term survival and maintenance of the mdDA neurons. Activates NR4A2/NURR1-mediated transcription of genes such as SLC6A3, SLC18A2, TH and DRD2 which are essential for development of mdDA neurons. Acts by decreasing the interaction of NR4A2/NURR1 with the corepressor NCOR2/SMRT which acts through histone deacetylases (HDACs) to keep promoters of NR4A2/NURR1 target genes in a repressed deacetylated state. Essential for the normal lens development and differentiation. Plays a critical role in the maintenance of mitotic activity of lens epithelial cells, fiber cell differentiation and in the control of the temporal and spatial activation of fiber cell-specific crystallins. Positively regulates FOXE3 expression and negatively regulates PROX1 in the anterior lens epithelium, preventing activation of CDKN1B/P27Kip1 and CDKN1C/P57Kip2 and thus maintains lens epithelial cells in cell cycle. {ECO:0000269|PubMed:15950611, ECO:0000269|PubMed:17184956, ECO:0000269|PubMed:19007884, ECO:0000269|PubMed:19144721, ECO:0000269|PubMed:19334279}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-ProRule:PRU00138, ECO:0000269|PubMed:17184956}. SUBUNIT: Interacts with SFPQ. {ECO:0000269|PubMed:19144721}. TISSUE SPECIFICITY: Highly expressed in developing eye lens. Expression is restricted to the substantia nigra and ventral tegmental area in the midbrain. {ECO:0000269|PubMed:15950611, ECO:0000269|PubMed:19007884}. DISEASE: Note=Mutations in Pitx3 appear to be the cause of the aphakia (ak) phenotype, a recessive homozygous disease characterized by small eyes and closed eyelids. {ECO:0000269|PubMed:19334279}. +Q8K4R4 PITC1_MOUSE Cytoplasmic phosphatidylinositol transfer protein 1 (Mammalian rdgB homolog beta) (M-rdgB beta) (MrdgBbeta) (mM-rdgBbeta) (Retinal degeneration B homolog beta) (RdgBbeta) 332 38,384 Alternative sequence (6); Chain (1); Erroneous gene model prediction (5); Modified residue (5) FUNCTION: Phosphatidylinositol transfer proteins mediate the monomeric transport of lipids by shielding a lipid from the aqueous environment and binding the lipid in a hydrophobic cavity. Able to transfer phosphatidylinositol in vitro. Isoform 2 specifically binds to phosphatidylinositol but not to other phospholipids and may play a role in the phosphoinositide-mediated signaling in the neural development. {ECO:0000269|PubMed:12562526}. SUBCELLULAR LOCATION: Isoform 1: Cytoplasm {ECO:0000269|PubMed:12562526}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm {ECO:0000269|PubMed:12562526}. Nucleus {ECO:0000269|PubMed:12562526}. TISSUE SPECIFICITY: Isoform 1 is widely expressed. Isoform 2 is weakly expressed. In brain, isoform 2 is weakly expressed and is rather confined to the embryonic stage. In contrast, isoform 1 is widely expressed in brain, with expression in the gray matters of pre- and postnatal brains. {ECO:0000269|PubMed:12562526}. +Q9QYE9 PKHB1_MOUSE Pleckstrin homology domain-containing family B member 1 (PH domain-containing family B member 1) (Evectin-1) (PH domain-containing protein in retina 1) (PHRET1) (Pleckstrin homology domain retinal protein 1) 243 27,340 Alternative sequence (2); Beta strand (8); Chain (1); Domain (1); Helix (2); Turn (3) SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:20301200}. Cytoplasm {ECO:0000269|PubMed:20301200}. Note=Membrane-associated. Highly expressed in the outer segments of photoreceptor cells, both in rods and cones (By similarity). Localizes to the apical juxta-nuclear Golgi region of the cytoplasm (PubMed:20301200). {ECO:0000250|UniProtKB:Q9UF11}. SUBUNIT: Binds transducins (By similarity). Homodimer. Interacts (via PH domain) with MYO1C. Interacts (via PH domain) with MYO7A. {ECO:0000250|UniProtKB:Q9UF11, ECO:0000269|PubMed:15976448}. TISSUE SPECIFICITY: Highly expressed in retina and brain. In retina, abundantly expressed in photoreceptors. Isoform 4 is the predominant isoform expressed in mature olfactory receptor neurons and vestibular and cochlear hair cells. Also expressed in cells with possible sensory function, including peripheral retinal ganglion cells, cochlear interdental cells, and neurons of the circumventricular organ (at protein level). {ECO:0000269|PubMed:10585447, ECO:0000269|PubMed:15456885, ECO:0000269|PubMed:20301200}. +O09037 REG3A_MOUSE Regenerating islet-derived protein 3-alpha (REG-3-alpha) (Islet of Langerhans regenerating protein 3) (Lithostathine 3) (Pancreatitis-associated protein 2) (Regenerating islet-derived protein III-alpha) (Reg III-alpha) [Cleaved into: Regenerating islet-derived protein 3-alpha 16.5 kDa form; Regenerating islet-derived protein 3-alpha 15 kDa form] 175 19,539 Chain (2); Disulfide bond (3); Domain (1); Propeptide (1); Signal peptide (1) FUNCTION: Bactericidal C-type lectin (By similarity). Regulates keratinocyte proliferation and differentiation after skin injury via activation of EXTL3-PI3K-AKT signaling pathway. {ECO:0000250, ECO:0000269|PubMed:22727489}. PTM: Proteolytic processing by trypsin removes an inhibitory N-terminal propeptide and is essential for its antimicrobial activity. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Interacts with EXTL3. {ECO:0000250}. DOMAIN: Lacks the EPN motif and the presence of Gln instead of Glu at amino-acid position 114 may explain its inability to bind peptidoglycan. TISSUE SPECIFICITY: Small intestine and pancreas. DISEASE: Note=Overexpressed during the acute phase of pancreatitis. +P35230 REG3B_MOUSE Regenerating islet-derived protein 3-beta (REG-3-beta) (Pancreatitis-associated protein 1) (Regenerating islet-derived protein III-beta) (Reg III-beta) [Cleaved into: Regenerating islet-derived protein 3-beta 16.5 kDa form; Regenerating islet-derived protein 3-beta 15 kDa form] 175 19,476 Chain (2); Disulfide bond (3); Domain (1); Motif (1); Propeptide (1); Signal peptide (1) FUNCTION: Bactericidal C-type lectin which acts against several intestinal Gram-positive and Gram-negative bacteria. Lacks antibacterial activity against S.typhimurium. May play a role in protection against infection with S.enteritidis by inhibiting its translocation from the gut lumen into intestinal tissues and further extraintestinal tissues. {ECO:0000269|PubMed:21694778, ECO:0000269|PubMed:22252863}. PTM: Proteolytic processing by trypsin removes an inhibitory N-terminal propeptide and is essential for peptidoglycan binding and antibacterial activity. {ECO:0000269|PubMed:21694778}. SUBCELLULAR LOCATION: Secreted. Note=Found in the apical region of pancreatic acinar cells. {ECO:0000250}. DOMAIN: The EPN motif is essential for recognition of the peptidoglycan carbohydrate backbone and for efficient bacterial killing with Glu-114 playing a key role in peptidoglycan binding and bactericidal activity. {ECO:0000250}. TISSUE SPECIFICITY: Constitutively expressed in the small intestine, moderately in colon and at an extremely low level in healthy pancreas. DISEASE: Note=Overexpressed during the acute phase of pancreatitis. +Q9JIY0 PKHO1_MOUSE Pleckstrin homology domain-containing family O member 1 (PH domain-containing family O member 1) 408 45,997 Binding site (2); Chain (1); Domain (1); Modified residue (3); Region (3); Sequence conflict (1); Site (2) FUNCTION: Plays a role in the regulation of the actin cytoskeleton through its interactions with actin capping protein (CP). May function to target CK2 to the plasma membrane thereby serving as an adapter to facilitate the phosphorylation of CP by protein kinase 2 (CK2). Appears to target ATM to the plasma membrane. Appears to also inhibit tumor cell growth by inhibiting AKT-mediated cell-survival. Also implicated in PI3K-regulated muscle differentiation, the regulation of AP-1 activity (plasma membrane bound AP-1 regulator that translocates to the nucleus) and the promotion of apoptosis induced by tumor necrosis factor TNF. When bound to PKB, it inhibits it probably by decreasing PKB level of phosphorylation (By similarity). {ECO:0000250, ECO:0000269|PubMed:17942896}. PTM: C-terminal fragments could be released during apoptosis via caspase-3-dependent cleavage. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q53GL0}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q53GL0}. Nucleus {ECO:0000250|UniProtKB:Q53GL0}. Cytoplasm {ECO:0000250|UniProtKB:Q53GL0}. Note=Predominantly localized to the plasma membrane through the binding to phosphatidylinositol 3-phosphate. In C2C12 cells, with the absence of growth factor, it is found in the nucleus. It rapidly translocates to the plasma membrane after insulin stimulation. In response to TNF, it translocates from the plasma membrane to the cytoplasm and then to the nucleus accompanied by cleavage by caspase-3. However, the subcellular location is highly dependent of the cell type, and this explains why it is found exclusively at the plasma membrane, in some type of cells. {ECO:0000250|UniProtKB:Q53GL0}. SUBUNIT: Heterodimer or homodimer. Interacts with CK2 and actin capping subunits (capping protein CP-alpha and CP-beta). CKIP1 and CK2 together inhibit the activity of actin capping protein at the barbed ends of actin filaments. Interacts with ATM, IFP35, JUN, JUND, NMI and PI3K. Interacts with AKT1, AKT2 and AKT3 (each isozyme of PKB), PtdIns(3,5)P2, PtdIns(4,5)P2 and PtdIns(3,4,5)P2 (By similarity). {ECO:0000250}. +Q6ZPQ6 PITM2_MOUSE Membrane-associated phosphatidylinositol transfer protein 2 (Drosophila retinal degeneration B homolog 2) (RdgB2) (Phosphatidylinositol transfer protein, membrane-associated 2) (PITPnm 2) (Pyk2 N-terminal domain-interacting receptor 3) (NIR-3) 1335 148,035 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (1); Modified residue (10) FUNCTION: Catalyzes the transfer of phosphatidylinositol and phosphatidylcholine between membranes (in vitro). Binds calcium ions (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000305|PubMed:10460238}. Note=May associate with the cytoskeleton. SUBUNIT: Interacts with CPNE4 (via VWFA domain) (PubMed:12522145). Interacts with PTK2B via its C-terminus (By similarity). {ECO:0000250|UniProtKB:Q9BZ72, ECO:0000269|PubMed:12522145}. TISSUE SPECIFICITY: Detected in retina and in the dentate gyrus of the cerebellum. {ECO:0000269|PubMed:10460238}. +O35292 RNS2B_MOUSE Ribonuclease 2B (EC 3.1.27.5) (Eosinophil cationic-type ribonuclease 5) (MR-5) 155 17,514 Active site (2); Chain (1); Disulfide bond (4); Glycosylation (1); Region (1); Sequence conflict (2); Signal peptide (1) FUNCTION: This is a non-secretory ribonuclease. It is a pyrimidine specific nuclease with a slight preference for U. Cytotoxin and helminthotoxin. Possesses a wide variety of biological activities. {ECO:0000250|UniProtKB:P10153}. +Q8R0C0 RPC7L_MOUSE DNA-directed RNA polymerase III subunit RPC7-like (RNA polymerase III subunit C7-like) (DNA-directed RNA polymerase III subunit G-like) 218 25,136 Chain (1); Compositional bias (1); Frameshift (1); Sequence conflict (4) FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. {ECO:0000250|UniProtKB:Q9BT43}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BT43}. SUBUNIT: Component of the RNA polymerase III (Pol III) complex consisting of 17 subunits (By similarity). Found a trimeric complex with POLR3C and POLR3G. Directly interacts with POLR3C (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9BT43}. TISSUE SPECIFICITY: Expressed in the liver. {ECO:0000269|PubMed:24107381}. +P70700 RPA2_MOUSE DNA-directed RNA polymerase I subunit RPA2 (RNA polymerase I subunit 2) (EC 2.7.7.6) (DNA-directed RNA polymerase I 135 kDa polypeptide) (RPA135) 1135 128,213 Chain (1); Modified residue (1); Sequence conflict (9); Zinc finger (1) FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Second largest core component of RNA polymerase I which synthesizes ribosomal RNA precursors. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol I is composed of mobile elements and RPA2 is part of the core element with the central large cleft and probably a clamp element that moves to open and close the cleft (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. SUBUNIT: Component of the RNA polymerase I (Pol I) complex consisting of at least 13 subunits. {ECO:0000250}. +P47708 RP3A_MOUSE Rabphilin-3A (Exophilin-1) 681 75,489 Beta strand (9); Chain (1); Compositional bias (1); Domain (3); Helix (2); Metal binding (20); Modified residue (4); Turn (2); Zinc finger (1) FUNCTION: Protein transport. Probably involved with Ras-related protein Rab-3A in synaptic vesicle traffic and/or synaptic vesicle fusion. Could play a role in neurotransmitter release by regulating membrane flow in the nerve terminal. SUBCELLULAR LOCATION: Cell junction, synapse {ECO:0000250}. Membrane {ECO:0000305|PubMed:18945677}; Peripheral membrane protein {ECO:0000305|PubMed:18945677}. SUBUNIT: Monomer. Interacts with RAB3A, RAB3B, RAB3C, RAB3D, RAB8A, RAB27A and RAB27B. {ECO:0000269|PubMed:12578829, ECO:0000269|PubMed:18945677}. DOMAIN: Binds calcium via the C2 domains. The calcium-bound C2 domains mediate interactions with phospholipid bilayers. TISSUE SPECIFICITY: Specifically expressed in brain. +Q80UW8 RPAB1_MOUSE DNA-directed RNA polymerases I, II, and III subunit RPABC1 (RNA polymerases I, II, and III subunit ABC1) (DNA-directed RNA polymerase II subunit E) (RPB5 homolog) 210 24,570 Chain (1); Cross-link (1); Modified residue (1) FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively. Pol II is the central component of the basal RNA polymerase II transcription machinery. Pols are composed of mobile elements that move relative to each other. In Pol II, POLR2E/RPB5 is part of the lower jaw surrounding the central large cleft and thought to grab the incoming DNA template. Seems to be the major component in this process (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the RNA polymerase I (Pol I), RNA polymerase II (Pol II) and RNA polymerase III (Pol III) complexes consisting of at least 13, 12 and 17 subunits, respectively. In RNA Pol II, this subunit is present in 2-fold molar excess over the other subunits. Interacts with URI1 (By similarity). {ECO:0000250}. +E9PYH6 SET1A_MOUSE Histone-lysine N-methyltransferase SETD1A (EC 2.1.1.43) (SET domain-containing protein 1A) 1716 186,060 Chain (1); Domain (3); Modified residue (5); Motif (1); Region (2) FUNCTION: Histone methyltransferase that specifically methylates 'Lys-4' of histone H3, when part of the SET1 histone methyltransferase (HMT) complex, but not if the neighboring 'Lys-9' residue is already methylated. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. The non-overlapping localization with SETD1B suggests that SETD1A and SETD1B make non-redundant contributions to the epigenetic control of chromatin structure and gene expression. {ECO:0000269|PubMed:29490266}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:O15047}. Chromosome {ECO:0000250|UniProtKB:O15047}. Note=Localizes to a largely non-overlapping set of euchromatic nuclear speckles with SETD1B, suggesting that SETD1A and SETD1B each bind to a unique set of target genes. {ECO:0000250|UniProtKB:O15047}. SUBUNIT: Component of the SET1 complex, at least composed of the catalytic subunit (SETD1A or SETD1B), WDR5, WDR82, RBBP5, ASH2L/ASH2, CXXC1/CFP1, HCFC1 and DPY30. Interacts with HCFC1. Interacts with ASH2/ASH2L, CXXC1/CFP1, WDR5 and RBBP5. Interacts (via the RRM domain) with WDR82. Interacts (via the RRM domain) with hyperphosphorylated C-terminal domain (CTD) of RNA polymerase II large subunit (POLR2A) only in the presence of WDR82. Binds specifically to CTD heptad repeats phosphorylated on 'Ser-5' of each heptad. Interacts with ZNF335. Interacts with SUPT6H (By similarity). Interacts with NAP1L1 (PubMed:29490266). {ECO:0000250|UniProtKB:O15047, ECO:0000269|PubMed:29490266}. +Q8VD37 SGIP1_MOUSE SH3-containing GRB2-like protein 3-interacting protein 1 (Endophilin-3-interacting protein) 806 86,063 Alternative sequence (8); Chain (1); Compositional bias (2); Domain (1); Modified residue (32); Region (5); Sequence conflict (3) FUNCTION: May function in clathrin-mediated endocytosis. Has both a membrane binding/tubulating activity and the ability to recruit proteins essential to the formation of functional clathrin-coated pits. Has a preference for membranes enriched in phosphatidylserine and phosphoinositides and is required for the endocytosis of the transferrin receptor. May also bind tubulin. May play a role in the regulation of energy homeostasis. {ECO:0000269|PubMed:17626015, ECO:0000269|PubMed:21747946}. SUBCELLULAR LOCATION: Membrane, clathrin-coated pit {ECO:0000305|PubMed:17626015}; Peripheral membrane protein {ECO:0000305|PubMed:17626015}; Cytoplasmic side {ECO:0000305|PubMed:17626015}. SUBUNIT: Interacts with proteins essential or regulating the formation of functional clathrin-coated pits (Probable). Interacts with CANX (PubMed:17626015, PubMed:21747946). Interacts with AP2A1 (PubMed:17626015). Interacts with EPS15 (PubMed:17626015). Interacts with SH3GL3 (By similarity). Interacts with AMPH (By similarity). Interacts with ITSN1 (via SH3 domains) (By similarity). Interacts with and REPS1 (By similarity). {ECO:0000250|UniProtKB:Q9BQI5, ECO:0000269|PubMed:17626015, ECO:0000269|PubMed:21747946, ECO:0000305}. TISSUE SPECIFICITY: Detected in brain, spinal cord and cerebellum. {ECO:0000269|PubMed:21747946}. +Q8BKJ9 SIR7_MOUSE NAD-dependent protein deacetylase sirtuin-7 (EC 3.5.1.-) (Regulatory protein SIR2 homolog 7) (SIR2-like protein 7) 402 45,146 Active site (1); Binding site (1); Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (2); Metal binding (4); Modified residue (1); Mutagenesis (1); Nucleotide binding (4); Sequence conflict (3) FUNCTION: NAD-dependent protein deacetylase that specifically mediates deacetylation of histone H3 at 'Lys-18' (H3K18Ac). In contrast to other histone deacetylases, displays selectivity for a single histone mark, H3K18Ac, directly linked to control of gene expression. H3K18Ac is mainly present around the transcription start site of genes and has been linked to activation of nuclear hormone receptors. SIRT7 thereby acts as a transcription repressor. Moreover, H3K18 hypoacetylation has been reported as a marker of malignancy in various cancers and seems to maintain the transformed phenotype of cancer cells. These data suggest that SIRT7 may play a key role in oncogenic transformation by suppresses expression of tumor suppressor genes by locus-specific deacetylation of H3K18Ac at promoter regions (By similarity). Required to restore the transcription of ribosomal RNA (rRNA) at the exit from mitosis. Promotes the association of RNA polymerase I with the rDNA promoter region and coding region. Stimulates transcription activity of the RNA polymerase I complex. May also deacetylate p53/TP53 and promotes cell survival, however such data need additional confirmation. {ECO:0000250, ECO:0000269|PubMed:16618798, ECO:0000269|PubMed:18239138}. PTM: Phosphorylated during mitosis. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, nucleolus {ECO:0000269|PubMed:16618798}. Note=Located close to the nuclear membrane when in the cytoplasm (By similarity). Associated with chromatin. Associated with rDNA promoter and transcribed region. Associated with nucleolar organizer regions during mitosis (By similarity). {ECO:0000250}. SUBUNIT: Interacts with UBTF and the RNA polymerase I complex. Interacts with components of the B-WICH complex, such as MYBBP1A, SMARCA5/SNF2H and BAZ1B/WSTF. Interacts with ELK4, leading to stabilization at target promoters for H3K18Ac deacetylation. Interacts with histone H2A and/or histone H2B (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Detected in liver, spleen and testis. Detected in embryos. {ECO:0000269|PubMed:16618798}. +P56183 RRP1_MOUSE Ribosomal RNA processing protein 1 homolog A (Novel nuclear protein 1) (NNP-1) (Nucleolar protein Nop52) (RRP1-like protein) 494 54,777 Alternative sequence (3); Chain (1); Compositional bias (1); Modified residue (3); Sequence conflict (1) FUNCTION: Plays a critical role in the generation of 28S rRNA. {ECO:0000250|UniProtKB:P56182}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:P56182}. SUBUNIT: Interacts with C1QBP. Interacts with RRP1B. {ECO:0000250|UniProtKB:P56182}. +Q8C503 SIT1_MOUSE Signaling threshold-regulating transmembrane adapter 1 (SHP2-interacting transmembrane adapter protein) (Suppression-inducing transmembrane adapter 1) 180 19,578 Chain (1); Disulfide bond (1); Glycosylation (1); Modified residue (10); Region (4); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 25 45 Helical; Signal-anchor for type III membrane protein. {ECO:0000255}. TOPO_DOM 1 24 Extracellular. {ECO:0000255}.; TOPO_DOM 46 180 Cytoplasmic. {ECO:0000255}. FUNCTION: Negatively regulates T-cell antigen receptor (TCR)-mediated signaling. Involved in positive selection of T-cells. {ECO:0000269|PubMed:16107703}. PTM: Phosphorylated on tyrosines upon TCR activation; which leads to the recruitment of PTPN11, GRB2 and CSK. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. SUBUNIT: Homodimer; disulfide-linked. When phosphorylated, interacts with PTPN11/SHP2, GRB2 and CSK (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in thymus and spleen, with highest levels in immature thymocytes (at protein level). {ECO:0000269|PubMed:16107703}. +Q9CSH3 RRP44_MOUSE Exosome complex exonuclease RRP44 (EC 3.1.13.-) (EC 3.1.26.-) (Protein DIS3 homolog) (Ribosomal RNA-processing protein 44) 958 108,838 Chain (1); Domain (1); Modified residue (3); Sequence caution (1); Sequence conflict (1) FUNCTION: Putative catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. DIS3 has both 3'-5' exonuclease and endonuclease activities. {ECO:0000250|UniProtKB:Q9Y2L1}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y2L1}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9Y2L1}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9Y2L1}. Nucleus {ECO:0000250|UniProtKB:Q9Y2L1}. Note=Predominantly located in the nucleus. According to, found in the nucleolus. According to, excluded from nucleolus supporting the existence of a nucleolar RNA exosome complex devoid of DIS3. {ECO:0000250|UniProtKB:Q9Y2L1}. SUBUNIT: Component of the RNA exosome complex. The catalytically inactive RNA exosome core (Exo-9) complex is believed to associate with catalytic subunits EXOSC10, and DIS3 or DIS3L in cytoplasmic- and nuclear-specific RNA exosome complex forms (By similarity). {ECO:0000250}. +Q3UND0 SKAP2_MOUSE Src kinase-associated phosphoprotein 2 (Pyk2/RAFTK-associated protein) (SKAP55 homolog) (SKAP-HOM) (Src family-associated phosphoprotein 2) (Src kinase-associated phosphoprotein 55-related protein) (Src-associated adapter protein with PH and SH3 domains) 358 40,712 Alternative sequence (1); Beta strand (9); Chain (1); Domain (2); Helix (8); Modified residue (12); Mutagenesis (1); Region (1); Sequence conflict (2); Turn (2) FUNCTION: May be involved in B-cell and macrophage adhesion processes. In B-cells, may act by coupling the B-cell receptor (BCR) to integrin activation. May play a role in src signaling pathway. {ECO:0000269|PubMed:11063873, ECO:0000269|PubMed:15894167, ECO:0000269|PubMed:16135797}. PTM: Dephosphorylated on Tyr-75 by PTPN22 (By similarity). Phosphorylated by FYN on Tyr-260. In case of infection with Y.pseudotuberculosis, dephosphorylated by bacterial phosphatase yopH. {ECO:0000250, ECO:0000269|PubMed:11063873, ECO:0000269|PubMed:11207596, ECO:0000269|PubMed:15894167}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11063873, ECO:0000269|PubMed:12893833, ECO:0000269|PubMed:19026786}. Note=Membrane ruffles of macrophages. Perikarya and dendrites from neurons. SUBUNIT: Interacts with LAT, GRB2, PTK2B and PRAM1 (By similarity). Homodimer. Interacts with FYB1, which is required for SKAP2 protein stability. Interacts with PTPNS1. Part of a complex consisting of SKAP2, FYB1 and PTPNS1. Part of a complex consisting of SKAP2, FYB1 and LILRB3. May interact with actin. May interact with FYN, HCK and LYN. Interacts with FASLG (By similarity). {ECO:0000250}. DOMAIN: The SH3 domain interacts with FYB1 and PTK2B. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in kidney, lung, liver, spleen, bone marrow and testis. Present in T-cells, B-cells, and all cells of the myelomonocytic lineage. Present in all brain regions, with highest levels in neurons from the Purkinje cell layer, hippocampal gyrus, cortex and substantia nigra (at protein level). {ECO:0000269|PubMed:11063873, ECO:0000269|PubMed:12893833, ECO:0000269|PubMed:15894167, ECO:0000269|PubMed:16135797}. +A2AQ25 SKT_MOUSE Sickle tail protein (Enhancer trap locus 4) 1946 213,037 Alternative sequence (11); Chain (1); Coiled coil (5); Compositional bias (3); Erroneous initiation (2); Glycosylation (1); Modified residue (18); Sequence conflict (4) FUNCTION: Required for normal development of intervertebral disks. {ECO:0000269|PubMed:16204209}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16204209}. SUBUNIT: Interacts with CPNE4 (via VWFA domain) (PubMed:12522145). {ECO:0000269|PubMed:12522145}. TISSUE SPECIFICITY: Expressed predominantly in the notochord and mesonephros during embryogenesis as well as in other areas such as the epithalamus sulcus, lens vesicle, inner retinal layer, heart, hepatic primordial surface, infundibulum, surface ectoderm, hind gut and limb bud mesenchyme. In adults, expressed in a range of tissues including the nucleus pulposus, corpus callosum, kidney, cardiac muscle, Sertoli cells and hair follicles. {ECO:0000269|PubMed:16204209}. +Q61165 SL9A1_MOUSE Sodium/hydrogen exchanger 1 (Na(+)/H(+) exchanger 1) (NHE-1) (Solute carrier family 9 member 1) 820 91,468 Chain (1); Glycosylation (1); Intramembrane (1); Modified residue (14); Region (1); Site (1); Topological domain (14); Transmembrane (12) INTRAMEM 386 406 Name=H10. {ECO:0000250}. TRANSMEM 13 33 Helical; Name=M1. {ECO:0000255}.; TRANSMEM 106 126 Helical; Name=M2. {ECO:0000255}.; TRANSMEM 134 153 Helical; Name=M3. {ECO:0000255}.; TRANSMEM 159 178 Helical; Name=M4. {ECO:0000255}.; TRANSMEM 196 215 Helical; Name=M5. {ECO:0000255}.; TRANSMEM 232 251 Helical; Name=M6. {ECO:0000255}.; TRANSMEM 261 280 Helical; Name=M7. {ECO:0000255}.; TRANSMEM 299 319 Helical; Name=M8. {ECO:0000255}.; TRANSMEM 343 362 Helical; Name=M9. {ECO:0000255}.; TRANSMEM 415 434 Helical; Name=M10. {ECO:0000255}.; TRANSMEM 453 474 Helical; Name=M11. {ECO:0000255}.; TRANSMEM 484 503 Helical; Name=M12. {ECO:0000255}. TOPO_DOM 1 12 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 34 105 Extracellular. {ECO:0000255}.; TOPO_DOM 127 133 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 154 158 Extracellular. {ECO:0000255}.; TOPO_DOM 179 195 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 216 231 Extracellular. {ECO:0000255}.; TOPO_DOM 252 260 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 281 298 Extracellular. {ECO:0000255}.; TOPO_DOM 320 342 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 363 385 Extracellular. {ECO:0000255}.; TOPO_DOM 407 414 Extracellular. {ECO:0000255}.; TOPO_DOM 435 452 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 475 483 Extracellular. {ECO:0000255}.; TOPO_DOM 504 820 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in pH regulation to eliminate acids generated by active metabolism or to counter adverse environmental conditions. Major proton extruding system driven by the inward sodium ion chemical gradient. Plays an important role in signal transduction. PTM: O-glycosylated. {ECO:0000250}.; PTM: Ubiquitinated, leading to its degradation by the proteasome. Ubiquitination is reduced by CHP1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane; Multi-pass membrane protein. Note=Colocalizes with CHP1 and CHP2 at the reticulum endoplasmic and plasma membrane. {ECO:0000250}. SUBUNIT: Oligomer. Interacts with calmodulin and TESC. Interacts (via the juxtamembrane region of the cytoplasmic C-terminal domain) with CHP1; the interaction occurs at the plasma membrane in a calcium-dependent manner. Interacts with CHP2; the interaction occurs in a calcium-dependent manner (By similarity). {ECO:0000250}. +Q8BUE1 SL9A4_MOUSE Sodium/hydrogen exchanger 4 (Na(+)/H(+) exchanger 4) (NHE-4) (Solute carrier family 9 member 4) 797 90,937 Chain (1); Glycosylation (1); Intramembrane (3); Topological domain (14); Transmembrane (10) INTRAMEM 14 28 Name=A/M1. {ECO:0000255}.; INTRAMEM 70 90 Name=B/M2. {ECO:0000255}.; INTRAMEM 421 441 Name=L. {ECO:0000255}. TRANSMEM 95 114 Helical; Name=C/M3. {ECO:0000255}.; TRANSMEM 128 148 Helical; Name=D/M4. {ECO:0000255}.; TRANSMEM 155 175 Helical; Name=E/M5. {ECO:0000255}.; TRANSMEM 195 215 Helical; Name=F/M5A. {ECO:0000255}.; TRANSMEM 227 247 Helical; Name=G/M5B. {ECO:0000255}.; TRANSMEM 271 291 Helical; Name=H/M6. {ECO:0000255}.; TRANSMEM 305 325 Helical; Name=I/M7. {ECO:0000255}.; TRANSMEM 353 373 Helical; Name=J/M8. {ECO:0000255}.; TRANSMEM 385 405 Helical; Name=K/M9. {ECO:0000255}.; TRANSMEM 451 471 Helical; Name=M/M10. {ECO:0000255}. TOPO_DOM 1 13 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 29 69 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 91 94 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 115 127 Extracellular. {ECO:0000255}.; TOPO_DOM 149 154 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 176 194 Extracellular. {ECO:0000255}.; TOPO_DOM 216 226 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 248 270 Extracellular. {ECO:0000255}.; TOPO_DOM 292 304 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 326 352 Extracellular. {ECO:0000255}.; TOPO_DOM 374 384 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 406 420 Extracellular. {ECO:0000255}.; TOPO_DOM 442 450 Extracellular. {ECO:0000255}.; TOPO_DOM 472 797 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in pH regulation to eliminate acids generated by active metabolism or to counter adverse environmental conditions. Major proton extruding system driven by the inward sodium ion chemical gradient. Plays an important role in signal transduction. May play a specialized role in the kidney in rectifying cell volume in response to extreme fluctuations of hyperosmolar-stimulated cell shrinkage. Is relatively amiloride and ethylisopropylamiloride (EIPA) insensitive. Can be activated under conditions of hyperosmolar-induced cell shrinkage in a sustained intracellular acidification-dependence manner. Activated by 4,4'-diisothiocyanostilbene-2,2'-disulfonic acid (DIDS) in a sustained intracellular acidification-dependence manner. Affects potassium/proton exchange as well as sodium/proton and lithium/proton exchange (By similarity). In basolateral cell membrane, participates in homeostatic control of intracellular pH, and may play a role in proton extrusion in order to achieve transepithelial HCO3(-) secretion. In apical cell membrane may be involved in mediating sodium absorption. Requires for normal levels of gastric acid secretion, secretory membrane development, parietal cell maturation and/or differentiation and at least secondarily for chief cell differentiation. {ECO:0000250, ECO:0000269|PubMed:12493726, ECO:0000269|PubMed:15684419}. PTM: May be phosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Apical cell membrane; Multi-pass membrane protein. Basolateral cell membrane; Multi-pass membrane protein. Cytoplasmic granule membrane; Multi-pass membrane protein. Note=Found in zymogen granule membranes. SUBUNIT: Interacts with CHP1 and CHP2. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in kidney. Expressed in uterus and endometrial epithelial cells. Expressed in the inner segments of inner medullary collecting ducts (IMCD) in kidney. {ECO:0000269|PubMed:9691122}. +Q8R4D1 SL9A8_MOUSE Sodium/hydrogen exchanger 8 (Na(+)/H(+) exchanger 8) (NHE-8) (Solute carrier family 9 member 8) 576 64,737 Alternative sequence (3); Chain (1); Modified residue (3); Sequence conflict (3); Transmembrane (12) TRANSMEM 55 75 Helical. {ECO:0000255}.; TRANSMEM 79 99 Helical. {ECO:0000255}.; TRANSMEM 118 138 Helical. {ECO:0000255}.; TRANSMEM 151 171 Helical. {ECO:0000255}.; TRANSMEM 186 206 Helical. {ECO:0000255}.; TRANSMEM 211 231 Helical. {ECO:0000255}.; TRANSMEM 256 276 Helical. {ECO:0000255}.; TRANSMEM 306 326 Helical. {ECO:0000255}.; TRANSMEM 349 369 Helical. {ECO:0000255}.; TRANSMEM 374 394 Helical. {ECO:0000255}.; TRANSMEM 412 432 Helical. {ECO:0000255}.; TRANSMEM 446 466 Helical. {ECO:0000255}. FUNCTION: Involved in pH regulation to eliminate acids generated by active metabolism or to counter adverse environmental conditions. Major proton extruding system driven by the inward sodium ion chemical gradient. Plays an important role in signal transduction (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed. Expressed in both renal cortex and medulla. In the cortex, present in the majority of cortical tubules. In the medulla, most highly expressed in the proximal tubules (S3) of the outer stripe of the outer medulla. {ECO:0000269|PubMed:12409279}. +Q6UJY2 SL9C1_MOUSE Sodium/hydrogen exchanger 10 (Na(+)/H(+) exchanger 10) (NHE-10) (Solute carrier family 10 member 10) (Solute carrier family 9 member C1) (Sperm-specific Na(+)/H(+) exchanger) (sNHE) 1175 135,545 Chain (1); Erroneous gene model prediction (1); Frameshift (1); Glycosylation (1); Nucleotide binding (1); Region (1); Sequence conflict (6); Transmembrane (14) TRANSMEM 37 57 Helical. {ECO:0000255}.; TRANSMEM 61 81 Helical. {ECO:0000255}.; TRANSMEM 100 120 Helical. {ECO:0000255}.; TRANSMEM 125 145 Helical. {ECO:0000255}.; TRANSMEM 160 180 Helical. {ECO:0000255}.; TRANSMEM 192 212 Helical. {ECO:0000255}.; TRANSMEM 240 260 Helical. {ECO:0000255}.; TRANSMEM 269 289 Helical. {ECO:0000255}.; TRANSMEM 314 334 Helical. {ECO:0000255}.; TRANSMEM 353 373 Helical. {ECO:0000255}.; TRANSMEM 420 440 Helical. {ECO:0000255}.; TRANSMEM 633 653 Helical. {ECO:0000255}.; TRANSMEM 666 686 Helical. {ECO:0000255}.; TRANSMEM 693 713 Helical. {ECO:0000255}. FUNCTION: Sperm-specific sodium/hydrogen exchanger involved in intracellular pH regulation of spermatozoa. Required for sperm motility and fertility. Involved in sperm cell hyperactivation, a step needed for sperm motility which is essential late in the preparation of sperm for fertilization. Required for the expression and bicarbonate regulation of the soluble adenylyl cyclase (sAC). {ECO:0000269|PubMed:14634667, ECO:0000269|PubMed:17517652}. SUBCELLULAR LOCATION: Cell projection, cilium, flagellum membrane {ECO:0000269|PubMed:14634667}; Multi-pass membrane protein {ECO:0000269|PubMed:14634667}. SUBUNIT: Interacts with soluble adenylyl cyclase (sAC). {ECO:0000269|PubMed:17517652}. DOMAIN: The ion transport-like region is related to the membrane segments of voltage-gated ion channels. Its function is unknown. TISSUE SPECIFICITY: Testis-specific. Specifically present in the principal piece of sperm tail (at protein level). {ECO:0000269|PubMed:14634667}. +Q18PI6 SLAF5_MOUSE SLAM family member 5 (Leukocyte differentiation antigen CD84) (Signaling lymphocytic activation molecule 5) (CD antigen CD84) 329 37,378 Alternative sequence (3); Chain (1); Disulfide bond (1); Domain (2); Glycosylation (1); Modified residue (3); Motif (2); Mutagenesis (2); Natural variant (1); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 222 242 Helical. {ECO:0000255}. TOPO_DOM 22 221 Extracellular. {ECO:0000255}.; TOPO_DOM 243 329 Cytoplasmic. {ECO:0000255}. FUNCTION: Self-ligand receptor of the signaling lymphocytic activation molecule (SLAM) family. SLAM receptors triggered by homo- or heterotypic cell-cell interactions are modulating the activation and differentiation of a wide variety of immune cells and thus are involved in the regulation and interconnection of both innate and adaptive immune response. Activities are controlled by presence or absence of small cytoplasmic adapter proteins, SH2D1A/SAP and/or SH2D1B/EAT-2 (PubMed:20962259). Can mediate natural killer (NK) cell cytotoxicity dependent on SH2D1A and SH2D1B (PubMed:20962259). Increases proliferative responses of activated T-cells and SH2D1A/SAP does not seen be required for this process. Homophilic interactions enhance interferon gamma/IFNG secretion in lymphocytes and induce platelet stimulation via a SH2D1A/SAP-dependent pathway. May serve as a marker for hematopoietic progenitor cells (By similarity). Required for a prolonged T-cell:B-cell contact, optimal T follicular helper function, and germinal center formation (PubMed:20153220). In germinal centers involved in maintaining B cell tolerance and in preventing autoimmunity (PubMed:25801429). In mast cells negatively regulates high affinity immunoglobulin epsilon receptor signaling; independent of SH2D1A and SH2D1B but implicating FES and PTPN6/SHP-1 (By similarity). In macrophages enhances LPS-induced MAPK phosphorylation and NF-kappaB activation and modulates LPS-induced cytokine secretion; involving ITSM 2 (PubMed:20628063). Positively regulates macroautophagy in primary dendritic cells via stabilization of IRF8; inhibits TRIM21-mediated proteasomal degradation of IRF8 (By similarity). {ECO:0000250|UniProtKB:Q9UIB8, ECO:0000269|PubMed:16037392, ECO:0000269|PubMed:20153220, ECO:0000269|PubMed:20628063, ECO:0000269|PubMed:20962259, ECO:0000269|PubMed:25801429, ECO:0000305}. PTM: Phosphorylated by tyrosine-protein kinase LCK on tyrosine residues following ligation induced by agonist monoclonal antibody. The association with SH2D1A/SAP is dependent of tyrosine phosphorylation of its cytoplasmic domain. Phosphorylated on Tyr-280 and Tyr-300 following platelet aggregation. Phosphorylated on tyrosine residues upon high affinity immunoglobulin epsilon receptor aggregation in mast cells. {ECO:0000250|UniProtKB:Q9UIB8}.; PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Homodimer; via its extracellular domain. Forms a head to tail dimer with a CD48 molecule from another cell. Interacts with SH2 domain-containing proteins SH2D1A/SAP and SH2D1B/EAT-2. Interacts with tyrosine-protein phosphatases PTPN6/SHP-1 and PTPN11/SHP-2 via its phosphorylated cytoplasmic domain, and this interaction is blocked by SH2D1A (By similarity). {ECO:0000250}. DOMAIN: The ITSMs (immunoreceptor tyrosine-based switch motifs) with the consensus sequence T-X-Y-X-X-[VI] present in SLAM family receptors have overlapping specificity for activating and inhibitory SH2 domain-containingbinding partners. Especially they mediate the interaction with the SH2 domain of SH2D1A and SH2D1B. A 'two-out-of-three-pronged' mechanism is proposed involving threonine (position -2), phosphorylated tyrosine (position 0) and valine/isoleucine (position +3). {ECO:0000250|UniProtKB:Q13291, ECO:0000250|UniProtKB:Q9UIB8}. TISSUE SPECIFICITY: Predominantly expressed in hematopoietic tissues such as lymph node, spleen, thymus, and bone marrow. Detected also in lung. +Q9ET39 SLAF6_MOUSE SLAM family member 6 (Lymphocyte antigen 108) (CD antigen CD352) 351 38,638 Alternative sequence (3); Chain (1); Disulfide bond (2); Domain (2); Glycosylation (9); Modified residue (1); Motif (2); Mutagenesis (9); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 240 262 Helical. {ECO:0000255}. TOPO_DOM 31 239 Extracellular. {ECO:0000255}.; TOPO_DOM 263 351 Cytoplasmic. {ECO:0000255}. FUNCTION: Self-ligand receptor of the signaling lymphocytic activation molecule (SLAM) family. SLAM receptors triggered by homo- or heterotypic cell-cell interactions are modulating the activation and differentiation of a wide variety of immune cells and thus are involved in the regulation and interconnection of both innate and adaptive immune response. Activities are controlled by presence or absence of small cytoplasmic adapter proteins, SH2D1A/SAP and/or SH2D1B/EAT-2 (PubMed:19648922). Triggers cytolytic activity only in natural killer cells (NK) expressing high surface densities of natural cytotoxicity receptors (By similarity). Positive signaling in NK cells implicates phosphorylation of VAV1. NK cell activation seems to depend on SH2D1B and not on SH2D1A (By similarity). In conjunction with SLAMF1 controls the transition between positive selection and the subsequent expansion and differentiation of the thymocytic natural killer T (NKT) cell lineage (PubMed:18031695). Promotes T cell differentiation into a helper T-cell Th17 phenotype leading to increased IL-17 secretion; the costimulatory activity requires SH2D1A (By similarity). Promotes recruitment of RORC to the IL-17 promoter (By similarity). In conjunction with SLAMF1 and CD84/SLAMF5 may be a negative regulator of the humoral immune response (PubMed:25926831). In the absence of SH2D1A/SAP can transmit negative signals to CD4(+) T-cells and NKT cells. Negatively regulates germinal center formation by inhibiting T-cell:B-cell adhesion; the function probably implicates increased association with PTPN6/SHP-1 via ITSMs in absence of SH2D1A/SAP (PubMed:22683125). However, reported to mediated T-cell adhesion, to participate in stable T-cell:B-cell interactions and to be involved in maintaining B-cell tolerance in germinal centers and in preventing autoimmunity (PubMed:20153220, PubMed:25801429). Involved in regulation of autoimmunity. Isoform 3 may be suppressor of pathogenic T-cell proliferation (PubMed:21422172). {ECO:0000250|UniProtKB:Q96DU3, ECO:0000269|PubMed:18031695, ECO:0000269|PubMed:19648922, ECO:0000269|PubMed:20153220, ECO:0000269|PubMed:21422172, ECO:0000269|PubMed:22683125, ECO:0000269|PubMed:25801429}. PTM: Phosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Homodimer. Interacts with PTN6 and, upon phosphorylation, with PTN11 and SH2D1A/SAP (By similarity). {ECO:0000250}. DOMAIN: The ITSMs (immunoreceptor tyrosine-based switch motifs) with the consensus sequence T-X-Y-X-X-[VI] present in SLAM family receptors have overlapping specificity for activating and inhibitory SH2 domain-containing binding partners. Especially they mediate the interaction with the SH2 domain of SH2D1A and SH2D1B. A 'two-out-of-three-pronged' mechanism is proposed involving threonine (position -2), phosphorylated tyrosine (position 0) and valine/isoleucine (position +3). {ECO:0000250|UniProtKB:Q13291}. TISSUE SPECIFICITY: Expressed on hematopoietic cells. Isoform 3 is expressed in thymocytes and B lymphocytes of C57Bl/6 strain. {ECO:0000269|PubMed:21422172}. +Q8BHK6 SLAF7_MOUSE SLAM family member 7 (Leukocyte cell-surface antigen) (Novel Ly9) (CD antigen CD319) 333 37,187 Alternative sequence (2); Chain (1); Disulfide bond (2); Domain (2); Frameshift (1); Glycosylation (5); Modified residue (2); Motif (1); Mutagenesis (3); Region (1); Sequence conflict (8); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 225 245 Helical. {ECO:0000255}. TOPO_DOM 23 224 Extracellular. {ECO:0000255}.; TOPO_DOM 246 333 Cytoplasmic. {ECO:0000255}. FUNCTION: Self-ligand receptor of the signaling lymphocytic activation molecule (SLAM) family. SLAM receptors triggered by homo- or heterotypic cell-cell interactions are modulating the activation and differentiation of a wide variety of immune cells and thus are involved in the regulation and interconnection of both innate and adaptive immune response. Activities are controlled by presence or absence of small cytoplasmic adapter proteins, SH2D1A/SAP and/or SH2D1B/EAT-2 (PubMed:19648922). Mediates natural killer (NK) cell activation through a SH2D1A-independent extracellular signal-regulated ERK-mediated pathway (By similarity). Positively regulates NK cell functions by a mechanism dependent on the adapter SH2D1B. In addition to heterotypic NK cells-target cells interactions also homotypic interactions between NK cells may contribute to activation. However, in the absence of SH2D1B, inhibits NK cell function. Acts also inhibitory in T-cells (PubMed:19151721). May play a role in lymphocyte adhesion (By similarity). In LPS-activated monocytes negatively regulates production of proinflammatory cytokines (By similarity). {ECO:0000250|UniProtKB:Q9NQ25, ECO:0000269|PubMed:19151721, ECO:0000269|PubMed:19648922}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Interacts (via ITSM phosphorylated on Tyr-302) with SH2D1B, PTPN6/SHP-1, PTPN11/SHP-2, INPP5D/SHIP1, CSK and FYN. {ECO:0000269|PubMed:19151721}. DOMAIN: The ITSMs (immunoreceptor tyrosine-based switch motifs) with the consensus sequence T-X-Y-X-X-[VI] present in SLAM family receptors have overlapping specificity for activating and inhibitory SH2 domain-containing binding partners. Especially they mediate the interaction with the SH2 domain of SH2D1A and SH2D1B. A 'three-pronged' mechanism is proposed involving threonine (position -2), phosphorylated tyrosine (position 0) and valine/isoleucine (position +3). {ECO:0000250|UniProtKB:Q13291}. TISSUE SPECIFICITY: Expressed in spleen, lymph node, bone marrow and testis. Lower levels detected in thymus. Expressed in NK cells, B-cells, natural killer cells and activated T-cells. {ECO:0000269|PubMed:12242590, ECO:0000269|PubMed:19151721}. +Q8R4L0 SLAP2_MOUSE Src-like-adapter 2 (Src-like adapter protein 2) (SLAP-2) 259 28,476 Alternative sequence (1); Chain (1); Domain (2); Erroneous initiation (1); Initiator methionine (1); Lipidation (1); Mutagenesis (4); Region (1); Sequence conflict (3) FUNCTION: Adapter protein, which negatively regulates T-cell receptor (TCR) signaling. Inhibits T-cell antigen-receptor induced activation of nuclear factor of activated T-cells. May act by linking signaling proteins such as ZAP70 with CBL, leading to a CBL dependent degradation of signaling proteins. {ECO:0000269|PubMed:11891219, ECO:0000269|PubMed:12024036}. PTM: Phosphorylated by CSF1R. {ECO:0000269|PubMed:12024036, ECO:0000269|PubMed:17353186}. SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Cytoplasmic vesicle. Late endosome. Note=Localized to the plasma membrane and intracellular vesicles, including late endosomal vesicles. SUBUNIT: Interacts (via its C-terminal domain) with CBL (phosphorylated). Interacts (via SH2 domain) with ZAP70 (phosphorylated) and CD3Z (phosphorylated). Interacts (via SH2 domain) with CSF1R (phosphorylated). {ECO:0000269|PubMed:11891219, ECO:0000269|PubMed:12024036, ECO:0000269|PubMed:17353186}. DOMAIN: The loss of the C-terminal domain partially abolishes the inhibitory function. TISSUE SPECIFICITY: Mainly expressed in immune system. Highly expressed in spleen and thymus and expressed at intermediate levels in lung. Not expressed in liver, heart and brain. Isoform 1 is predominant in lung and spleen, while isoform 2 is predominant in thymus. +P97440 SLBP_MOUSE Histone RNA hairpin-binding protein (Histone stem-loop-binding protein) 275 31,603 Chain (1); Cross-link (1); Modified residue (7); Motif (2); Region (1) FUNCTION: RNA-binding protein involved in the histone pre-mRNA processing. Binds the stem-loop structure of replication-dependent histone pre-mRNAs and contributes to efficient 3'-end processing by stabilizing the complex between histone pre-mRNA and U7 small nuclear ribonucleoprotein (snRNP), via the histone downstream element (HDE). Plays an important role in targeting mature histone mRNA from the nucleus to the cytoplasm and to the translation machinery. Stabilizes mature histone mRNA and could be involved in cell-cycle regulation of histone gene expression (By similarity). Involved in the mechanism by which growing oocytes accumulate histone proteins that support early embryogenesis. Binds to the 5' side of the stem-loop structure of histone pre-mRNAs. {ECO:0000250, ECO:0000269|PubMed:18036581, ECO:0000269|PubMed:19470752}. PTM: Phosphorylated on Thr-61 and Thr-62 in the S-phase. Phosphorylation of Thr-62 by CDK1 primes phosphorylation of Thr-61 by CK2. Phosphorylation of Thr-62 is required for its degradation at the end of the S phase. Its degradation is not required for histone mRNA degradation at the end of the S phase. All the phosphorylated forms detected are present in the cytoplasm. Both unphosphorylated and phosphorylated forms bind the stem-loop structure of histone mRNAs. Phosphorylation at Thr-171 increases affinity for histone mRNAs (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18036581}. Nucleus {ECO:0000269|PubMed:18036581}. Note=Localizes predominantly in the nucleus at the G1/G2 phases and the beginning of S phase. Through the S phase, partially redistributes to the cytoplasm. Binding to histone mRNA is necessary for cytoplasmic localization. Shuttles between the nucleus and the cytoplasm. Imported in the nucleus by the Importin alpha/Importin beta receptor (By similarity). Polyribosome-associated. {ECO:0000250}. SUBUNIT: Monomer. SLBP/pre-mRNA complex interacts with ZNF473. Interacts with the Importin alpha/Importin beta receptor, LSM1, MIF4GD, TNPO3 and UPF1. Interaction with LSM1 occurs when histone mRNA is being rapidly degraded during the S phase. Found in a ternary complex with ERI1 and the stem-loop structure of the 3' end of histone mRNA. Associates with polyribosomes (By similarity). Identified in a histone pre-mRNA complex, at least composed of ERI1, LSM11, SLBP, SNRPB, SYNCRIP and YBX1. Binds in a cooperative manner with ERI1 to the mature 3'-end of histone mRNAs. {ECO:0000250, ECO:0000269|PubMed:19470752}. DOMAIN: Amino acids 31-34, 96-99 and 246-249 are necessary for interaction with the Importin alpha/Importin beta receptor. The first 18 amino acids, amino acids 69-76 and 179-182 are necessary for interaction with TNPO3. Amino acids 31-34, 96-99 and 246-249 are necessary for nuclear localization (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. Expressed in growing primary but not non-growing oocytes, within the primordial follicles. Also detected in fully-grown oocytes in antral follicles (at protein level). {ECO:0000269|PubMed:18036581}. +Q8R3P9 SLF1_MOUSE SMC5-SMC6 complex localization factor protein 1 (Ankyrin repeat domain-containing protein 32) (BRCT domain-containing protein 1) (Protein BRCTx) 1054 121,004 Alternative sequence (2); Chain (1); Domain (2); Erroneous initiation (3); Repeat (3); Sequence conflict (2) FUNCTION: Plays a role in the DNA damage response (DDR) pathway by regulating postreplication repair of UV-damaged DNA and genomic stability maintenance. The SLF1-SLF2 complex acts to link RAD18 with the SMC5-SMC6 complex at replication-coupled interstrand cross-links (ICL) and DNA double-strand breaks (DSBs) sites on chromatin during DNA repair in response to stalled replication forks. Promotes the recruitment of SLF2 and the SMC5-SMC6 complex to DNA lesions. {ECO:0000250|UniProtKB:Q9BQI6}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15632077, ECO:0000269|PubMed:22036607}. Cytoplasm {ECO:0000269|PubMed:15632077}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:15632077}. Note=Relocalizes with RAD18 to nuclear foci in response to DNA damage (PubMed:22036607). Colocalizes with RAD18 in the nucleus and to centrosomes (PubMed:15632077). Associates with chromatin. Accumulates with RAD18 and the SMC5-SMC6 complex at replication-coupled DNA interstrand repair and DNA double-strand breaks (DSBs) sites on chromatin in a ubiquitin-dependent manner. {ECO:0000250|UniProtKB:Q9BQI6, ECO:0000269|PubMed:15632077, ECO:0000269|PubMed:22036607}. SUBUNIT: Interacts (via BRCT domains) with RAD18 (via C-terminus and phosphorylated form); this interaction is required for efficient repair of UV-induced DNA damage (PubMed:15632077, PubMed:22036607). Interacts (via N-terminus) with SLF2; this interaction links RAD18 to the SMC5-SMC6 complex. Interacts (via BRCT domains) with RAD18; this interaction occurs in a SLF2-independent manner. Interacts with SMC6. {ECO:0000250|UniProtKB:Q9BQI6, ECO:0000269|PubMed:15632077, ECO:0000269|PubMed:22036607}. DOMAIN: BRCT domains are necessary for its targeting to ionizing radiation-induced nuclear foci (PubMed:22036607). {ECO:0000269|PubMed:22036607}. TISSUE SPECIFICITY: Widely expressed (PubMed:15632077). Expressed in testis (PubMed:15632077). Expressed in spermatocytes (PubMed:15632077). {ECO:0000269|PubMed:15632077}. +Q6P9P0 SLF2_MOUSE SMC5-SMC6 complex localization factor protein 2 1278 143,970 Chain (1); Compositional bias (1); Erroneous initiation (1); Modified residue (4); Sequence conflict (5) FUNCTION: Plays a role in the DNA damage response (DDR) pathway by regulating postreplication repair of UV-damaged DNA and genomic stability maintenance. The SLF1-SLF2 complex acts to link RAD18 with the SMC5-SMC6 complex at replication-coupled interstrand cross-links (ICL) and DNA double-strand breaks (DSBs) sites on chromatin during DNA repair in response to stalled replication forks. Promotes the recruitment of the SMC5-SMC6 complex to DNA lesions. {ECO:0000250|UniProtKB:Q8IX21}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8IX21}. Note=Mainly localizes in the nucleus. Colocalizes with PCNA on replication sites. Associates with chromatin. Accumulates with RAD18 and the SMC5-SMC6 complex at replication-coupled DNA interstrand repair and DNA double-strand breaks (DSBs) sites on chromatin in a ubiquitin-dependent manner. {ECO:0000250|UniProtKB:Q8IX21}. SUBUNIT: Interacts with SLF1 (via N-terminus); this interaction links RAD18 to the SMC5-SMC6 complex. Interacts with RAD18; this interaction is increased in a SLF1-dependent manner. Interacts with SMC5 and SMC6. {ECO:0000250|UniProtKB:Q8IX21}. +Q8CBA2 SLFN5_MOUSE Schlafen family member 5 884 100,819 Chain (1); Nucleotide binding (1); Sequence conflict (8) FUNCTION: May have a role in hematopoietic cell differentiation. {ECO:0000269|PubMed:15351786}. +B1ARD8 SLFN8_MOUSE Schlafen family member 8 (EC 3.1.-.-) (Schlafen-8) (mSLFN8) 910 104,264 Active site (2); Chain (1); Metal binding (3); Nucleotide binding (1); Region (1); Sequence conflict (2) FUNCTION: Endoribonuclease that cleaves tRNAs and rRNAs (PubMed:29563550). Cleaves tRNAs 11 nucleotides from the 3'-terminus at the acceptor stem (PubMed:29563550). May be involved in immune system via regulation of inflammation (PubMed:29528433). {ECO:0000269|PubMed:29528433, ECO:0000269|PubMed:29563550}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q68D06}. DOMAIN: Shows a pseudo-dimeric U-pillow-shaped architecture of the SLFN13 N'-domain that may clamp base-paired RNAs. {ECO:0000250|UniProtKB:Q5U311}. TISSUE SPECIFICITY: In T-cells, expressed at relatively constant levels during development: expressed in immature CD3(-)CD4(-)CD8(-) T-cells (DN stage), in CD4(+)CD8(+) double-positive stage (DP) and mature CD4(+) or CD8(+) thymocytes. Expression is slightly reduced at the DP stage. {ECO:0000269|PubMed:15351786}. +B1ARD6 SLFN9_MOUSE Schlafen family member 9 (EC 3.1.-.-) (Schlafen-9) 910 103,992 Active site (2); Chain (1); Erroneous gene model prediction (1); Metal binding (3); Nucleotide binding (1); Region (1); Sequence conflict (22) FUNCTION: Endoribonuclease that cleaves tRNAs and rRNAs. {ECO:0000250|UniProtKB:Q5U311}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q68D06}. DOMAIN: Shows a pseudo-dimeric U-pillow-shaped architecture of the SLFN13 N'-domain that may clamp base-paired RNAs. {ECO:0000250|UniProtKB:Q5U311}. TISSUE SPECIFICITY: In T-cells, expressed at relatively constant levels during development: expressed in immature CD3(-)CD4(-)CD8(-) T-cells (DN stage), in CD4(+)CD8(+) double-positive stage (DP) and mature CD4(+) or CD8(+) thymocytes. Expression is slightly reduced at the DP stage. {ECO:0000269|PubMed:15351786}. +Q810B7 SLIK5_MOUSE SLIT and NTRK-like protein 5 957 107,165 Alternative sequence (3); Chain (1); Domain (3); Frameshift (1); Glycosylation (2); Repeat (12); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 665 685 Helical. {ECO:0000255}. TOPO_DOM 41 664 Extracellular. {ECO:0000255}.; TOPO_DOM 686 957 Cytoplasmic. {ECO:0000255}. FUNCTION: Suppresses neurite outgrowth. {ECO:0000269|PubMed:14550773}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. TISSUE SPECIFICITY: In the adult, significant expression is detected only in the brain. In the embryo, expressed in the subventricular zone, cortical plate, pyramidal layer of hippocampus, thalamus and hypothalamus. {ECO:0000269|PubMed:14550773}. +Q8C110 SLIK6_MOUSE SLIT and NTRK-like protein 6 840 95,056 Chain (1); Domain (4); Repeat (11); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 610 630 Helical. {ECO:0000255}. TOPO_DOM 23 609 Extracellular. {ECO:0000255}.; TOPO_DOM 631 840 Cytoplasmic. {ECO:0000255}. FUNCTION: Regulator of neurite outgrowth required for normal hearing and vision. {ECO:0000269|PubMed:14550773, ECO:0000269|PubMed:23543054}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. TISSUE SPECIFICITY: In the embryo, expressed in otic cyst, lateral trunk epidermis and underlying mesodermal tissue, limb bud, maxillary process, cochlea, retina, tongue, tooth primordium, central nervous system, and primordia of visceral organs including lung, gastrointestinal tract and pancreas. In the central nervous system, expressed primarily in dorsal thalamus, cerebellum and medulla. {ECO:0000269|PubMed:14643680}. +D3YWJ0 SLIP_MOUSE Nuclear GTPase SLIP-GC (EC 3.6.1.-) (Speckled-like pattern in the germinal center) 796 91,269 Chain (1); Coiled coil (2); Nucleotide binding (1) FUNCTION: Nuclear GTPase found in germinal center B-cells, where it may inhibit function of the activation-induced cytidine deaminase AICDA (By similarity). Reduces somatic hypermutation in B-cells which may enhance genome stability (PubMed:22833677). {ECO:0000250|UniProtKB:Q68CJ6, ECO:0000269|PubMed:22833677}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:22833677}. +Q9D8T7 SLIRP_MOUSE SRA stem-loop-interacting RNA-binding protein, mitochondrial 112 12,605 Alternative sequence (1); Chain (1); Domain (1); Frameshift (1); Modified residue (3); Sequence conflict (1); Transit peptide (1) FUNCTION: RNA-binding protein that acts as a nuclear receptor corepressor. Probably acts by binding the SRA RNA, and repressing the SRA-mediated nuclear receptor coactivation. Binds the STR7 loop of SRA RNA. Also able to repress glucocorticoid (GR), androgen (AR), thyroid (TR) and VDR-mediated transactivation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Nucleus {ECO:0000250}. Note=Predominantly mitochondrial. Some fraction is nuclear. In the nucleus, it is recruited to nuclear receptor target promoters (By similarity). {ECO:0000250}. +Q8BI21 RNF38_MOUSE E3 ubiquitin-protein ligase RNF38 (EC 2.3.2.27) (RING finger protein 38) (RING-type E3 ubiquitin transferase RNF38) 518 57,999 Alternative sequence (1); Chain (1); Compositional bias (1); Motif (2); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: Acts as an E3 ubiquitin-protein ligase able to ubiquitinate p53/TP53 which promotes its relocalization to discrete foci associated with PML nuclear bodies. Exhibits preference for UBE2D2 as a E2 enzyme. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +Q8BH75 RNF41_MOUSE E3 ubiquitin-protein ligase NRDP1 (EC 2.3.2.27) (RING finger protein 41) (RING-type E3 ubiquitin transferase NRDP1) 317 35,891 Alternative sequence (2); Beta strand (4); Chain (1); Erroneous initiation (1); Erroneous translation (2); Helix (8); Sequence conflict (5); Turn (2); Zinc finger (2) Protein modification; protein ubiquitination. FUNCTION: Acts as E3 ubiquitin-protein ligase and regulates the degradation of target proteins. Polyubiquitinates MYD88 (By similarity). Negatively regulates MYD88-dependent production of proinflammatory cytokines. Can promote TRIF-dependent production of type I interferon and inhibits infection with vesicular stomatitis virus. Promotes also activation of TBK1 and IRF3 (PubMed:19483718). Involved in the ubiquitination of erythropoietin (EPO) and interleukin-3 (IL-3) receptors. Thus, through maintaining basal levels of cytokine receptors, RNF41 is involved in the control of hematopoietic progenitor cell differentiation into myeloerythroid lineages (PubMed:18495327). Contributes to the maintenance of steady-state ERBB3 levels by mediating its growth factor-independent degradation. Involved in the degradation of the inhibitor of apoptosis BIRC6 and thus is an important regulator of cell death by promoting apoptosis. Acts also as a PRKN modifier that accelerates its degradation, resulting in a reduction of PRKN activity, influencing the balance of intracellular redox state. The RNF41-PRKN pathway regulates autophagosome-lysosome fusion during late mitophagy. Mitophagy is a selective form of autophagy necessary for mitochondrial quality control (PubMed:24949970). {ECO:0000250, ECO:0000269|PubMed:18495327, ECO:0000269|PubMed:19483718, ECO:0000269|PubMed:24949970}. PTM: Autoubiquitinated. Autoubiquitination leads to proteasomal degradation. Deubiquitinated by USP8 to get stabilized which induces apoptosis. {ECO:0000250}. SUBUNIT: Interacts with USP8, ERBB3, PRKN and BIRC6 (By similarity). Interacts with CSF2RB, EPOR, IL3RA, MYD88 and TBK1. Interacts with Clec16a (PubMed:24949970). {ECO:0000250, ECO:0000269|PubMed:17384230, ECO:0000269|PubMed:18495327, ECO:0000269|PubMed:19483718, ECO:0000269|PubMed:24949970}. +Q5GAM9 RNS11_MOUSE Putative inactive ribonuclease 11 (RNase 11) 192 20,883 Chain (1); Sequence conflict (3); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +C0HKG5 RNT2A_MOUSE Ribonuclease T2-A (EC 3.1.27.-) (Ribonuclease 6-A) 259 29,609 Active site (3); Chain (1); Disulfide bond (4); Glycosylation (3); Signal peptide (1) FUNCTION: Has ribonuclease activity, with higher activity at acidic pH. May play a role in cellular RNA catabolism. Probably is involved in lysosomal degradation of ribosomal RNA. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Endoplasmic reticulum lumen {ECO:0000250}. Lysosome lumen {ECO:0000250}. +G5E872 RNPL1_MOUSE Aminopeptidase RNPEPL1 (EC 3.4.11.-) (Methionyl aminopeptidase) (EC 3.4.11.18) 720 79,535 Active site (1); Chain (1); Metal binding (3); Region (1); Site (1) FUNCTION: Broad specificity aminopeptidase which preferentially hydrolyzes an N-terminal methionine, citrulline or glutamine. {ECO:0000250|UniProtKB:Q9HAU8}. +Q63871 RPAB4_MOUSE DNA-directed RNA polymerases I, II, and III subunit RPABC4 (RNA polymerases I, II, and III subunit ABC4) (DNA-directed RNA polymerase II subunit K) (Metallothionein-I gene transcription activator) (RPB10alpha) 58 6,974 Chain (1); Erroneous initiation (1); Metal binding (4); Zinc finger (1) FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and a small RNAs, such as 5S rRNA and tRNAs, respectively (By similarity). {ECO:0000250}.; FUNCTION: Factor that activates expression from a metal response element of the mouse metallothionein-I gene. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the RNA polymerase I (Pol I), RNA polymerase II (Pol II) and RNA polymerase III (Pol III) complexes consisting of at least 13, 12 and 17 subunits, respectively. {ECO:0000250}. +Q8VCC8 RPGF3_MOUSE Rap guanine nucleotide exchange factor 3 (Exchange factor directly activated by cAMP 1) (Exchange protein directly activated by cAMP 1) (EPAC 1) (cAMP-regulated guanine nucleotide exchange factor I) (cAMP-GEFI) 918 103,533 Alternative sequence (1); Chain (1); Domain (3); Erroneous initiation (1); Modified residue (3); Nucleotide binding (1); Region (2) FUNCTION: Guanine nucleotide exchange factor (GEF) for RAP1A and RAP2A small GTPases that is activated by binding cAMP. Through simultaneous binding of PDE3B to RAPGEF3 and PIK3R6 is assembled in a signaling complex in which it activates the PI3K gamma complex and which is involved in angiogenesis. Plays a role in the modulation of the cAMP-induced dynamic control of endothelial barrier function through a pathway that is independent on Rho-mediated signaling. Required for the actin rearrangement at cell-cell junctions, such as stress fibers and junctional actin (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. DOMAIN: The DEP domain is involved in membrane localization independent from regulation by cAMP. {ECO:0000250}. +Q68EF8 RPGFL_MOUSE Rap guanine nucleotide exchange factor-like 1 662 73,695 Chain (1); Compositional bias (1); Domain (1); Sequence caution (1) FUNCTION: Probable guanine nucleotide exchange factor (GEF). +P47968 RPIA_MOUSE Ribose-5-phosphate isomerase (EC 5.3.1.6) (Phosphoriboisomerase) 303 32,451 Chain (1); Erroneous initiation (2); Modified residue (2); Sequence conflict (1) Carbohydrate degradation; pentose phosphate pathway; D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step 1/1. TISSUE SPECIFICITY: Found in the spleen, kidney, thymus, heart, brain and lung. Higher levels are found in testis. {ECO:0000269|PubMed:7758956}. +Q14B98 SESQ2_MOUSE Sesquipedalian-2 (Ses2) (27 kDa inositol polyphosphate phosphatase interacting protein B) (IPIP27B) (PH domain-containing endocytic trafficking adaptor 2) 259 28,707 Chain (1); Coiled coil (1); Domain (1); Motif (1); Sequence conflict (1) FUNCTION: Plays a role in endocytic trafficking. Required for receptor recycling from endosomes, both to the trans-Golgi network and the plasma membrane. {ECO:0000250|UniProtKB:Q6ICB4}. SUBCELLULAR LOCATION: Early endosome {ECO:0000250|UniProtKB:Q6ICB4}. Recycling endosome {ECO:0000250|UniProtKB:Q6ICB4}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q6ICB4}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:Q6ICB4}. Note=Also found on macropinosomes. Not detected in late endosomes, nor in lysosomes. {ECO:0000250|UniProtKB:Q6ICB4}. SUBUNIT: Forms homodimers and heterodimers with PHETA1. Interacts with OCRL and INPP5B. {ECO:0000250|UniProtKB:Q6ICB4}. DOMAIN: The F&H motif, an approximately 12-13 amino-acid sequence centered around Phe and His residues, is essential for binding to OCRL and INPP5B. {ECO:0000250|UniProtKB:Q8N4B1}. +B2RS91 RRN3_MOUSE RNA polymerase I-specific transcription initiation factor RRN3 656 74,518 Chain (1); Modified residue (4); Region (2); Sequence conflict (1) FUNCTION: Required for efficient transcription initiation by RNA polymerase I. Required for the formation of the competent preinitiation complex (PIC). Dissociates from pol I as a consequence of transcription. In vitro, cannot activate transcription in a subsequent transcription reaction. {ECO:0000269|PubMed:12015311, ECO:0000269|PubMed:12646563}. PTM: Phosphorylated at Thr-198 by MAPK9/JNK2, which abrogates initiation complex formation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12015311}. SUBUNIT: Interacts with TAF1B. Interacts with TWISTNB, EIF3L and TAF1C (By similarity). {ECO:0000250}. +A7TZG1 SKI10_MOUSE Selection and upkeep of intraepithelial T-cells protein 10 (Skint-10) 354 40,861 Chain (1); Disulfide bond (1); Domain (1); Erroneous initiation (2); Glycosylation (1); Sequence conflict (6); Signal peptide (1); Topological domain (4); Transmembrane (3) TRANSMEM 159 179 Helical. {ECO:0000255}.; TRANSMEM 210 230 Helical. {ECO:0000255}.; TRANSMEM 253 273 Helical. {ECO:0000255}. TOPO_DOM 53 158 Extracellular. {ECO:0000255}.; TOPO_DOM 180 209 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 231 252 Extracellular. {ECO:0000255}.; TOPO_DOM 274 354 Cytoplasmic. {ECO:0000255}. FUNCTION: May act by engaging a cell surface molecule on immature T-cells in the embryonic thymus. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in skin and thymus. {ECO:0000269|PubMed:18408721}. +A7TZF0 SKIT3_MOUSE Selection and upkeep of intraepithelial T-cells protein 3 (Skint-3) 458 53,068 Alternative sequence (2); Chain (1); Disulfide bond (2); Domain (2); Glycosylation (1); Signal peptide (1); Topological domain (6); Transmembrane (5) TRANSMEM 238 258 Helical. {ECO:0000255}.; TRANSMEM 284 304 Helical. {ECO:0000255}.; TRANSMEM 325 345 Helical. {ECO:0000255}.; TRANSMEM 360 380 Helical. {ECO:0000255}.; TRANSMEM 415 435 Helical. {ECO:0000255}. TOPO_DOM 25 237 Extracellular. {ECO:0000255}.; TOPO_DOM 259 283 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 305 324 Extracellular. {ECO:0000255}.; TOPO_DOM 346 359 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 381 414 Extracellular. {ECO:0000255}.; TOPO_DOM 436 458 Cytoplasmic. {ECO:0000255}. FUNCTION: May act by engaging a cell surface molecule on immature T-cells in the embryonic thymus. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in skin and thymus. {ECO:0000269|PubMed:18408721}. +A7TZF3 SKIT4_MOUSE Selection and upkeep of intraepithelial T-cells protein 4 (Skint-4) 474 54,166 Alternative sequence (1); Chain (1); Disulfide bond (2); Domain (2); Glycosylation (2); Signal peptide (1); Topological domain (6); Transmembrane (5) TRANSMEM 242 262 Helical. {ECO:0000255}.; TRANSMEM 299 319 Helical. {ECO:0000255}.; TRANSMEM 342 362 Helical. {ECO:0000255}.; TRANSMEM 382 402 Helical. {ECO:0000255}.; TRANSMEM 421 441 Helical. {ECO:0000255}. TOPO_DOM 26 241 Extracellular. {ECO:0000255}.; TOPO_DOM 263 298 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 320 341 Extracellular. {ECO:0000255}.; TOPO_DOM 363 381 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 403 420 Extracellular. {ECO:0000255}.; TOPO_DOM 442 474 Cytoplasmic. {ECO:0000255}. FUNCTION: May act by engaging a cell surface molecule on immature T-cells in the embryonic thymus. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in skin, thymus and, to a lower extent, bladder and testis. {ECO:0000269|PubMed:18408721}. +A7XUY5 SKIT5_MOUSE Selection and upkeep of intraepithelial T-cells protein 5 (Skint-5) 1461 165,918 Alternative sequence (3); Chain (1); Compositional bias (1); Disulfide bond (2); Domain (2); Glycosylation (1); Signal peptide (1); Topological domain (5); Transmembrane (4) TRANSMEM 1307 1327 Helical. {ECO:0000255}.; TRANSMEM 1346 1366 Helical. {ECO:0000255}.; TRANSMEM 1388 1408 Helical. {ECO:0000255}.; TRANSMEM 1428 1448 Helical. {ECO:0000255}. TOPO_DOM 25 1306 Extracellular. {ECO:0000255}.; TOPO_DOM 1328 1345 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1367 1387 Extracellular. {ECO:0000255}.; TOPO_DOM 1409 1427 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1449 1461 Extracellular. {ECO:0000255}. FUNCTION: May act by engaging a cell surface molecule on immature T-cells in the embryonic thymus. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in skin and, to a lower extent, testis. {ECO:0000269|PubMed:18408721}. +A7XUZ6 SKIT6_MOUSE Selection and upkeep of intraepithelial T-cells protein 6 (Skint-6) 1240 141,567 Alternative sequence (2); Chain (1); Disulfide bond (2); Domain (2); Glycosylation (3); Signal peptide (1); Topological domain (5); Transmembrane (4) TRANSMEM 1087 1107 Helical. {ECO:0000255}.; TRANSMEM 1126 1146 Helical. {ECO:0000255}.; TRANSMEM 1168 1188 Helical. {ECO:0000255}.; TRANSMEM 1206 1226 Helical. {ECO:0000255}. TOPO_DOM 25 1086 Extracellular. {ECO:0000255}.; TOPO_DOM 1108 1125 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1147 1167 Extracellular. {ECO:0000255}.; TOPO_DOM 1189 1205 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1227 1240 Extracellular. {ECO:0000255}. FUNCTION: May act by engaging a cell surface molecule on immature T-cells in the embryonic thymus. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in skin. {ECO:0000269|PubMed:18408721}. +A7XV04 SKIT7_MOUSE Selection and upkeep of intraepithelial T-cells protein 7 (Skint-7) 395 45,215 Alternative sequence (4); Chain (1); Disulfide bond (2); Domain (2); Erroneous initiation (5); Glycosylation (2); Sequence conflict (9); Signal peptide (1); Topological domain (4); Transmembrane (3) TRANSMEM 249 269 Helical. {ECO:0000255}.; TRANSMEM 288 308 Helical. {ECO:0000255}.; TRANSMEM 330 350 Helical. {ECO:0000255}. TOPO_DOM 26 248 Extracellular. {ECO:0000255}.; TOPO_DOM 270 287 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 309 329 Extracellular. {ECO:0000255}.; TOPO_DOM 351 395 Cytoplasmic. {ECO:0000255}. FUNCTION: May act by engaging a cell surface molecule on immature T-cells in the embryonic thymus. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in skin, thymus, testis and, to a lower extent, bladder. {ECO:0000269|PubMed:18408721}. +Q8BLV3 SL9A7_MOUSE Sodium/hydrogen exchanger 7 (Na(+)/H(+) exchanger 7) (NHE-7) (Solute carrier family 9 member 7) 726 80,289 Alternative sequence (2); Chain (1); Modified residue (1); Sequence conflict (1); Transmembrane (13) TRANSMEM 71 91 Helical. {ECO:0000255}.; TRANSMEM 96 116 Helical. {ECO:0000255}.; TRANSMEM 176 196 Helical. {ECO:0000255}.; TRANSMEM 211 231 Helical. {ECO:0000255}.; TRANSMEM 252 272 Helical. {ECO:0000255}.; TRANSMEM 278 298 Helical. {ECO:0000255}.; TRANSMEM 324 344 Helical. {ECO:0000255}.; TRANSMEM 351 371 Helical. {ECO:0000255}.; TRANSMEM 373 393 Helical. {ECO:0000255}.; TRANSMEM 416 436 Helical. {ECO:0000255}.; TRANSMEM 444 464 Helical. {ECO:0000255}.; TRANSMEM 515 535 Helical. {ECO:0000255}.; TRANSMEM 613 633 Helical. {ECO:0000255}. FUNCTION: Mediates electroneutral exchange of protons for Na(+) and K(+) across endomembranes. May contribute to Golgi volume and cation homeostasis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Recycling endosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with SCAMP1, SCAMP2 and SCAMP5; may participate in its shuttling from trans-Golgi network to recycling endosomes. {ECO:0000250}. +Q8C0X2 SL9B1_MOUSE Sodium/hydrogen exchanger 9B1 (Na(+)/H(+) exchanger-like domain-containing protein 1) (NHE domain-containing protein 1) (Sodium/hydrogen exchanger-like domain-containing protein 1) (Solute carrier family 9 subfamily B member 1) (Testis specific sodium-hydrogen exchanger) (MtsNHE) 565 61,958 Alternative sequence (7); Chain (1); Compositional bias (1); Sequence conflict (3); Transmembrane (13) TRANSMEM 122 142 Helical. {ECO:0000255}.; TRANSMEM 146 166 Helical. {ECO:0000255}.; TRANSMEM 167 187 Helical. {ECO:0000255}.; TRANSMEM 206 223 Helical. {ECO:0000255}.; TRANSMEM 238 258 Helical. {ECO:0000255}.; TRANSMEM 266 286 Helical. {ECO:0000255}.; TRANSMEM 311 331 Helical. {ECO:0000255}.; TRANSMEM 341 361 Helical. {ECO:0000255}.; TRANSMEM 371 391 Helical. {ECO:0000255}.; TRANSMEM 419 439 Helical. {ECO:0000255}.; TRANSMEM 449 469 Helical. {ECO:0000255}.; TRANSMEM 482 502 Helical. {ECO:0000255}.; TRANSMEM 523 543 Helical. {ECO:0000255}. FUNCTION: Sperm-specific Na(+)/H(+) exchanger involved in intracellular pH regulation of spermatozoa (PubMed:20036903). Involved in sperm motility and fertility (PubMed:20036903, PubMed:27010853, PubMed:19409551). {ECO:0000269|PubMed:19409551, ECO:0000269|PubMed:20036903, ECO:0000269|PubMed:27010853}. SUBCELLULAR LOCATION: Cell projection, cilium, flagellum membrane {ECO:0000269|PubMed:19409551, ECO:0000269|PubMed:20036903, ECO:0000269|PubMed:27010853}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Testis-specific (PubMed:20036903). Expressed in the spermatids and spermatozoa (at protein level) (PubMed:20036903). Specifically present in the principal piece of sperm tail (at protein level) (PubMed:20036903, PubMed:27010853, PubMed:19409551). {ECO:0000269|PubMed:19409551, ECO:0000269|PubMed:20036903, ECO:0000269|PubMed:27010853}. +Q9D3G2 SLAF8_MOUSE SLAM family member 8 (B-lymphocyte activator macrophage expressed) (CD antigen CD353) 278 30,646 Chain (1); Disulfide bond (1); Domain (1); Glycosylation (2); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 232 252 Helical. {ECO:0000255}. TOPO_DOM 21 231 Extracellular. {ECO:0000255}.; TOPO_DOM 253 278 Cytoplasmic. {ECO:0000255}. FUNCTION: May play a role in B-lineage commitment and/or modulation of signaling through the B-cell receptor. {ECO:0000269|PubMed:11313408}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. +Q9D780 SLAF9_MOUSE SLAM family member 9 285 31,749 Chain (1); Compositional bias (1); Disulfide bond (1); Domain (2); Glycosylation (6); Sequence conflict (7); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 233 253 Helical. {ECO:0000255}. TOPO_DOM 18 232 Extracellular. {ECO:0000255}.; TOPO_DOM 254 285 Cytoplasmic. {ECO:0000255}. FUNCTION: May play a role in the immune response. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. +Q68FF7 SLAI1_MOUSE SLAIN motif-containing protein 1 579 61,307 Alternative sequence (1); Chain (1); Coiled coil (1); Compositional bias (1); Modified residue (3) FUNCTION: Microtubule plus-end tracking protein that might be involved in the regulation of cytoplasmic microtubule dynamics, microtubule organization and microtubule elongation. {ECO:0000269|PubMed:21646404}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:21646404}. Note=Colocalizes with microtubules. Detected at the plus end of growing microtubules. {ECO:0000269|PubMed:21646404}. SUBUNIT: Interacts with MAPRE1, MAPRE2, MAPRE3 and CKAP5 (PubMed:21646404). Interacts with ZDHHC17 (via ANK repeats) (By similarity). {ECO:0000250|UniProtKB:Q8ND83, ECO:0000269|PubMed:21646404}. TISSUE SPECIFICITY: Expressed in embryonic stem cells (PubMed:16546155). Expressed in adult bone marrow, brain, kidney, lung, testis and thymus (PubMed:16546155, PubMed:20563991). Expressed in colon (PubMed:20563991). Isoform 1 is highly expressed in brain (PubMed:20563991). Isoform 2 is more widely expressed in bone marrow, brain, colon, kidney, lung and thymus (PubMed:20563991). {ECO:0000269|PubMed:16546155, ECO:0000269|PubMed:20563991}. +Q8CI08 SLAI2_MOUSE SLAIN motif-containing protein 2 581 62,378 Alternative sequence (1); Chain (1); Coiled coil (1); Compositional bias (1); Erroneous initiation (3); Modified residue (23); Sequence caution (2); Sequence conflict (1); Site (1) FUNCTION: Binds to the plus end of microtubules and regulates microtubule dynamics and microtubule organization. Promotes cytoplasmic microtubule nucleation and elongation. Required for normal structure of the microtubule cytoskeleton during interphase. {ECO:0000269|PubMed:21646404}. PTM: Is highly phosphorylated during mitosis, but not during interphase. The highly phosphorylated form does not localize at microtubule plus ends and does not interact with MAPRE1 or CKAP5 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Note=Colocalizes with microtubules. Detected at the plus end of growing microtubules (By similarity). {ECO:0000250}. SUBUNIT: Interacts with CLIP1, CLIP2, CKAP5, CLASP1, MAPRE1 and MAPRE3. {ECO:0000250}. DOMAIN: The N-terminus forms a two-stranded coiled coil. {ECO:0000250}. +Q60898 SLAP1_MOUSE Src-like-adapter (Src-like-adapter protein 1) (SLAP-1) (mSLAP) 281 31,681 Alternative sequence (1); Chain (1); Domain (2); Initiator methionine (1); Lipidation (1); Modified residue (2); Mutagenesis (3); Region (1); Sequence conflict (2) FUNCTION: Adapter protein, which negatively regulates T-cell receptor (TCR) signaling. Inhibits T-cell antigen-receptor induced activation of nuclear factor of activated T-cells. Involved in the negative regulation of positive selection and mitosis of T-cells. May act by linking signaling proteins such as ZAP70 with CBL, leading to a CBL dependent degradation of signaling proteins. {ECO:0000269|PubMed:10662792, ECO:0000269|PubMed:10779329, ECO:0000269|PubMed:11567635}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10779329}. Endosome {ECO:0000269|PubMed:10779329}. Note=Colocalizes with endosomes. SUBUNIT: Homodimer. Interacts with phosphorylated CBL, SYK and LAT. Homodimerization and interaction with phosphorylated CBL occurs via its C-terminal domain (By similarity). Interacts with PDGFRB and EPHA2. Interacts with phosphorylated proteins ZAP70; CD3Z; VAV1 and LCP2 via its SH2 domain. {ECO:0000250, ECO:0000269|PubMed:10662792, ECO:0000269|PubMed:7543898, ECO:0000269|PubMed:9742401}. DOMAIN: The C-terminal domain is essential for the homodimerization and the interaction with CBL. While the interaction with CBL is apparently mediated via the hydrophobic region of this domain, the highly charged region is apparently required for the homodimerization (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Predominantly expressed in lymphoid tissues. Highly expressed in spleen, thymus and lymph nodes. Weakly expressed in lung and brain. Expressed in T-cells and at low level in B-cells. {ECO:0000269|PubMed:7543898}. +Q99LZ3 SLD5_MOUSE DNA replication complex GINS protein SLD5 (GINS complex subunit 4) [Cleaved into: DNA replication complex GINS protein SLD5, N-terminally processed] 223 25,961 Chain (2); Initiator methionine (1); Modified residue (4); Region (1) FUNCTION: The GINS complex plays an essential role in the initiation of DNA replication, and progression of DNA replication forks. GINS4 is important for GINS complex assembly. GINS complex seems to bind preferentially to single-stranded DNA (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16338220}. Nucleus {ECO:0000269|PubMed:16338220}. SUBUNIT: Component of the GINS complex which is a heterotetramer of GINS1, GINS2, GINS3 and GINS4. Forms a stable subcomplex with GINS1. GINS complex interacts with DNA primase in vitro. {ECO:0000250|UniProtKB:Q9BRT9}. TISSUE SPECIFICITY: Highly abundant in testis. Weakly expressed in thymus and bone marrow. {ECO:0000269|PubMed:16338220}. +Q99M28 RNPS1_MOUSE RNA-binding protein with serine-rich domain 1 305 34,208 Alternative sequence (1); Chain (1); Compositional bias (4); Cross-link (2); Domain (1); Modified residue (5); Region (6) FUNCTION: Part of pre- and post-splicing multiprotein mRNP complexes. Auxiliary component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Component of the ASAP and PSAP complexes which bind RNA in a sequence-independent manner and are proposed to be recruited to the EJC prior to or during the splicing process and to regulate specific excision of introns in specific transcription subsets. The ASAP complex can inhibit RNA processing during in vitro splicing reactions. The ASAP complex promotes apoptosis and is disassembled after induction of apoptosis. Enhances the formation of the ATP-dependent A complex of the spliceosome. Involved in both constitutive splicing and, in association with SRP54 and TRA2B/SFRS10, in distinctive modulation of alternative splicing in a substrate-dependent manner. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms such as Bcl-X(S); the activity is different from the established EJC assembly and function. Participates in mRNA 3'-end cleavage. Involved in UPF2-dependent nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. Also mediates increase of mRNA abundance and translational efficiency. Binds spliced mRNA 20-25 nt upstream of exon-exon junctions (By similarity). {ECO:0000250}. PTM: Phosphorylated on one or more of the four Ser/Thr residues (Ser-43, Thr-49, Ser-52 or Ser-53). Ser-53 phosphorylation site is important for splicing and translation stimulation activity in vitro (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus speckle {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Nucleocytoplasmic shuttling protein. Colocalizes with the core EJC, ALYREF/THOC4, NXF1 and UAP56 in the nucleus and nuclear speckles (By similarity). {ECO:0000250}. SUBUNIT: Found in mRNA splicing-dependent exon junction complexes (EJC). Found in a post-splicing complex with NXF1, RBM8A, UPF1, UPF2, UPF3A, UPF3B and RNPS1. Component of the heterotrimeric ASAP (apoptosis- and splicing-associated protein) and PSAP complexes consisting of RNPS1, SAP18 and either ACIN1 or PNN, respectively; the ASAP and PSAP complexes probably are formed mutually exclusive. Component of the active spliceosome. Associates with polysomes. Interacts with the cleaved p110 isoform of CDC2L1, CSNK2A1, PNN, SART3, SRP54, SRRM1 and TRA2B/SFRS10 (By similarity). {ECO:0000250}. DOMAIN: The RRM domain is required for the formation of the ASAP complex. {ECO:0000250}. +Q9CQZ7 RPC10_MOUSE DNA-directed RNA polymerase III subunit RPC10 (RNA polymerase III subunit C10) (DNA-directed RNA polymerase III subunit K) (RNA polymerase III subunit C11) (RPC11) 108 12,330 Chain (1); Sequence conflict (1); Zinc finger (2) FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts induce type I interferon and NF- Kappa-B through the RIG-I pathway (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:P32529}. SUBUNIT: Component of the RNA polymerase III (Pol III) complex consisting of 17 subunits. {ECO:0000250}. +P62876 RPAB5_MOUSE DNA-directed RNA polymerases I, II, and III subunit RPABC5 (RNA polymerases I, II, and III subunit ABC5) (DNA-directed RNA polymerase III subunit L) (RPB10 homolog) 67 7,645 Chain (1); Metal binding (4) FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and a small RNAs, such as 5S rRNA and tRNAs, respectively. Pol II is the central component of the basal RNA polymerase II transcription machinery. Pols are composed of mobile elements that move relative to each other. In Pol II, POLR2L/RBP10 is part of the core element with the central large cleft (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the RNA polymerase I (Pol I), RNA polymerase II (Pol II) and RNA polymerase III (Pol III) complexes consisting of at least 13, 12 and 17 subunits, respectively. {ECO:0000250}. +Q9CZT4 RPC5_MOUSE DNA-directed RNA polymerase III subunit RPC5 (RNA polymerase III subunit 5) (RNA polymerase III subunit C5) (Sex-lethal interactor homolog) (Sxl interactor) 710 79,854 Alternative sequence (1); Chain (1); Cross-link (5); Modified residue (5); Sequence conflict (2) FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific periphjeric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Essential for efficient transcription from both the type 2 VAI and type 3 U6 RNA polymerase III promoters. Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts induce type I interferon and NF- Kappa-B through the RIG-I pathway (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the RNA polymerase III (Pol III) complex consisting of 17 subunits. Interacts with RPC4 (By similarity). {ECO:0000250}. +O35134 RPA1_MOUSE DNA-directed RNA polymerase I subunit RPA1 (RNA polymerase I subunit A1) (EC 2.7.7.6) (DNA-directed RNA polymerase I largest subunit) (DNA-directed RNA polymerase I subunit A) (RNA polymerase I 194 kDa subunit) (RPA194) 1717 194,110 Chain (1); Metal binding (7); Modified residue (1); Region (1); Sequence conflict (2) FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic core component of RNA polymerase I which synthesizes ribosomal RNA precursors. Forms the polymerase active center together with the second largest subunit. A single stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol I. A bridging helix emanates from RPA1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol I by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition (By similarity). {ECO:0000250|UniProtKB:P10964}. PTM: Phosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. SUBUNIT: Component of the RNA polymerase I (Pol I) complex consisting of at least 13 subunits (By similarity). Interacts with MYO1C (PubMed:16514417). Interacts with ERBB2 (By similarity). Interacts with DDX11 (By similarity). {ECO:0000250|UniProtKB:O95602, ECO:0000269|PubMed:16514417}. +P61219 RPAB2_MOUSE DNA-directed RNA polymerases I, II, and III subunit RPABC2 (RNA polymerases I, II, and III subunit ABC2) (DNA-directed RNA polymerase II subunit F) (RPB6 homolog) 127 14,464 Chain (1); Initiator methionine (1); Modified residue (2) FUNCTION: DNA-dependent RNA polymerases catalyze the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively. Pol II is the central component of the basal RNA polymerase II transcription machinery. Pols are composed of mobile elements that move relative to each other. In Pol II, POLR2F/RPB6 is part of the clamp element and together with parts of RPB1 and RPB2 forms a pocket to which the RPB4-RPB7 subcomplex binds (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the RNA polymerase I (Pol I), RNA polymerase II (Pol II) and RNA polymerase III (Pol III) complexes consisting of at least 13, 12 and 17 subunits, respectively. {ECO:0000250}. +Q9DBG6 RPN2_MOUSE Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2 (Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 63 kDa subunit) (Ribophorin II) (RPN-II) (Ribophorin-2) 631 69,063 Chain (1); Cross-link (1); Glycosylation (1); Signal peptide (1); Topological domain (4); Transmembrane (3) TRANSMEM 541 561 Helical. {ECO:0000255}.; TRANSMEM 572 592 Helical. {ECO:0000255}.; TRANSMEM 597 617 Helical. {ECO:0000255}. TOPO_DOM 23 540 Lumenal. {ECO:0000255}.; TOPO_DOM 562 571 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 593 596 Lumenal. {ECO:0000255}.; TOPO_DOM 618 631 Cytoplasmic. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. {ECO:0000250|UniProtKB:F1PCT7}. SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:F1PCT7}. Endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Component of the oligosaccharyltransferase (OST) complex. OST exists in two different complex forms which contain common core subunits RPN1, RPN2, OST48, OST4, DAD1 and TMEM258, either STT3A or STT3B as catalytic subunits, and form-specific accessory subunits. STT3A complex assembly occurs through the formation of 3 subcomplexes. Subcomplex 1 contains RPN1 and TMEM258, subcomplex 2 contains the STT3A-specific subunits STT3A, DC2/OSTC, and KCP2 as well as the core subunit OST4, and subcomplex 3 contains RPN2, DAD1, and OST48. The STT3A complex can form stable complexes with the Sec61 complex or with both the Sec61 and TRAP complexes. {ECO:0000250|UniProtKB:F1PCT7}. +Q80UK0 SESD1_MOUSE SEC14 domain and spectrin repeat-containing protein 1 (Huntingtin-interacting protein-like protein) 696 79,376 Chain (1); Domain (1); Repeat (3); Sequence conflict (1) FUNCTION: May act as the primary docking protein directing membrane turnover and assembly of the transient receptor potential channels TRPC4 and TRPC5. Binds phospholipids such as phosphatidylinositol monophosphates, phosphatidylinositol diphosphates (PIP2s) and phosphatidic acid, but not less polar lipids including phosphatidylcholine, phosphatidylserine, and phosphatidylinositol. The binding to PIP2s is calcium dependent. Might be involved in the plasma membrane localization of CTNNB1 (By similarity). {ECO:0000250}. SUBUNIT: Interacts (via the spectrin 1 repeat) with TRPC4 and TRPC5 (via CIRB domain). Interacts with CTNNB1. {ECO:0000250}. +Q9WVC6 SGK1_MOUSE Serine/threonine-protein kinase Sgk1 (EC 2.7.11.1) (Serum/glucocorticoid-regulated kinase 1) 431 48,928 Active site (1); Alternative sequence (2); Binding site (1); Chain (1); Compositional bias (1); Disulfide bond (2); Domain (2); Erroneous initiation (1); Modified residue (7); Motif (1); Nucleotide binding (1); Region (1); Sequence conflict (3) FUNCTION: Serine/threonine-protein kinase which is involved in the regulation of a wide variety of ion channels, membrane transporters, cellular enzymes, transcription factors, neuronal excitability, cell growth, proliferation, survival, migration and apoptosis. Plays an important role in cellular stress response. Contributes to regulation of renal Na(+) retention, renal K(+) elimination, salt appetite, gastric acid secretion, intestinal Na(+)/H(+) exchange and nutrient transport, insulin-dependent salt sensitivity of blood pressure, salt sensitivity of peripheral glucose uptake, cardiac repolarization and memory consolidation. Up-regulates Na(+) channels: SCNN1A/ENAC, SCN5A and ASIC1/ACCN2, K(+) channels: KCNJ1/ROMK1, KCNA1-5, KCNQ1-5 and KCNE1, epithelial Ca(2+) channels: TRPV5 and TRPV6, chloride channels: BSND, CLCN2 and CFTR, glutamate transporters: SLC1A3/EAAT1, SLC1A2 /EAAT2, SLC1A1/EAAT3, SLC1A6/EAAT4 and SLC1A7/EAAT5, amino acid transporters: SLC1A5/ASCT2, SLC38A1/SN1 and SLC6A19, creatine transporter: SLC6A8, Na(+)/dicarboxylate cotransporter: SLC13A2/NADC1, Na(+)-dependent phosphate cotransporter: SLC34A2/NAPI-2B, glutamate receptor: GRIK2/GLUR6. Up-regulates carriers: SLC9A3/NHE3, SLC12A1/NKCC2, SLC12A3/NCC, SLC5A3/SMIT, SLC2A1/GLUT1, SLC5A1/SGLT1 and SLC15A2/PEPT2. Regulates enzymes: GSK3A/B, PMM2 and Na(+)/K(+) ATPase, and transcription factors: CTNNB1 and nuclear factor NF-kappa-B. Stimulates sodium transport into epithelial cells by enhancing the stability and expression of SCNN1A/ENAC. This is achieved by phosphorylating the NEDD4L ubiquitin E3 ligase, promoting its interaction with 14-3-3 proteins, thereby preventing it from binding to SCNN1A/ENAC and targeting it for degradation. Regulates store-operated Ca(+2) entry (SOCE) by stimulating ORAI1 and STIM1. Regulates KCNJ1/ROMK1 directly via its phosphorylation or indirectly via increased interaction with SLC9A3R2/NHERF2. Phosphorylates MDM2 and activates MDM2-dependent ubiquitination of p53/TP53. Phosphorylates MAPT/TAU and mediates microtubule depolymerization and neurite formation in hippocampal neurons. Phosphorylates SLC2A4/GLUT4 and up-regulates its activity. Phosphorylates APBB1/FE65 and promotes its localization to the nucleus. Phosphorylates MAPK1/ERK2 and activates it by enhancing its interaction with MAP2K1/MEK1 and MAP2K2/MEK2. Phosphorylates FBXW7 and plays an inhibitory role in the NOTCH1 signaling. Phosphorylates FOXO1 resulting in its relocalization from the nucleus to the cytoplasm. Phosphorylates FOXO3, promoting its exit from the nucleus and interference with FOXO3-dependent transcription. Phosphorylates BRAF and MAP3K3/MEKK3 and inhibits their activity. Phosphorylates SLC9A3/NHE3 in response to dexamethasone, resulting in its activation and increased localization at the cell membrane. Phosphorylates CREB1. Necessary for vascular remodeling during angiogenesis. {ECO:0000269|PubMed:12488318, ECO:0000269|PubMed:12684516, ECO:0000269|PubMed:15774535, ECO:0000269|PubMed:19756449, ECO:0000269|PubMed:19965929, ECO:0000269|PubMed:20568246, ECO:0000269|PubMed:21147854, ECO:0000269|PubMed:21385992, ECO:0000269|PubMed:21757730, ECO:0000269|PubMed:21865597}. PTM: Regulated by phosphorylation. Activated by phosphorylation on Ser-422 by mTORC2, transforming it into a substrate for PDPK1 which phosphorylates it on Thr-256. Phosphorylation on Ser-397 and Ser-401 are also essential for its activity. Phosphorylation on Ser-78 by MAPK7 is required for growth factor-induced cell cycle progression (By similarity). {ECO:0000250}.; PTM: Ubiquitinated by NEDD4L; which promotes proteasomal degradation. Ubiquitinated by SYVN1 at the endoplasmic reticulum; which promotes rapid proteasomal degradation and maintains a high turnover rate in resting cells (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}. Cell membrane {ECO:0000250}. Mitochondrion {ECO:0000250}. Note=The subcellular localization is controlled by the cell cycle, as well as by exposure to specific hormones and environmental stress stimuli. In proliferating cells, it shuttles between the nucleus and cytoplasm in synchrony with the cell cycle, and in serum/growth factor-stimulated cells it resides in the nucleus. In contrast, after exposure to environmental stress or treatment with glucocorticoids, it is detected in the cytoplasm and with certain stress conditions is associated with the mitochondria. In osmoregulation through the epithelial sodium channel, it can be localized to the cytoplasmic surface of the cell membrane. Nuclear, upon phosphorylation (By similarity). {ECO:0000250}. SUBUNIT: Homodimer; disulfide-linked. Interacts with MAPK3/ERK1, MAPK1/ERK2, MAP2K1/MEK1, MAP2K2/MEK2, NEDD4, NEDD4L, MAPT/TAU, MAPK7, CREB1, SLC9A3R2/NHERF2 and KCNJ1/ROMK1 (By similarity). Forms a trimeric complex with FBXW7 and NOTCH1 Associates with the mammalian target of rapamycin complex 2 (mTORC2) via an interaction with MAPKAP1/SIN1. {ECO:0000250, ECO:0000269|PubMed:21147854, ECO:0000269|PubMed:21757730}. +Q9CYX7 RRP15_MOUSE RRP15-like protein (Ribosomal RNA-processing protein 15) 281 31,058 Chain (1); Coiled coil (1); Cross-link (5); Initiator methionine (1); Modified residue (8); Sequence conflict (8) PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}. +O54926 SIVA_MOUSE Apoptosis regulatory protein Siva (CD27-binding protein) (CD27BP) 175 18,770 Alternative sequence (1); Chain (1); Modified residue (2); Region (1); Sequence conflict (3) FUNCTION: Induces CD27-mediated apoptosis. Inhibits BCL2L1 isoform Bcl-x(L) anti-apoptotic activity. Inhibits activation of NF-kappa-B and promotes T-cell receptor-mediated apoptosis (By similarity). {ECO:0000250, ECO:0000269|PubMed:9177220}. PTM: Phosphorylated by ABL2/ARG in response to oxidative stress. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}. Note=In the nucleus, accumulates in dot-like structures. {ECO:0000250}. SUBUNIT: Binds through its N-terminal region to the C-terminus of CD27 and to PXMP2/PMP22. Binds to the C-terminus of TNFRSF18/GITR. Isoform 1 binds to BCL2L1/BCLX isoform Bcl-x(L) but not to BAX. {ECO:0000269|PubMed:12478477}. TISSUE SPECIFICITY: Highly expressed in testis, heart, liver, lung, and muscle, and less in kidney, spleen and brain. +Q9DB85 RRP8_MOUSE Ribosomal RNA-processing protein 8 (EC 2.1.1.-) (Cerebral protein 1 homolog) 457 51,066 Binding site (6); Chain (1); Compositional bias (1); Frameshift (1); Modified residue (5); Sequence conflict (15) FUNCTION: Essential component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus. In the complex, RRP8 binds to H3K9me2 and probably acts as a methyltransferase. Its substrates are however unknown (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Note=Localizes at rDNA locus. {ECO:0000250}. SUBUNIT: Component of the eNoSC complex, composed of SIRT1, SUV39H1 and RRP8. {ECO:0000250}. +Q62233 SIX3_MOUSE Homeobox protein SIX3 (Sine oculis homeobox homolog 3) 333 35,593 Alternative sequence (2); Chain (1); Compositional bias (1); DNA binding (1); Erroneous initiation (1); Frameshift (1); Mutagenesis (2); Region (2); Sequence conflict (2) FUNCTION: Transcriptional regulator which can act as both a transcriptional repressor and activator by binding a ATTA homeodomain core recognition sequence on these target genes. During forebrain development represses WNT1 expression allowing zona limitans intrathalamica formation and thereby ensuring proper anterio-posterior patterning of the diencephalon and formation of the rostral diencephalon (PubMed:18094027). Acts as a direct upstream activator of SHH expression in the rostral diencephalon ventral midline and that in turn SHH maintains its expression (PubMed:18775421). In addition, Six3 activity is required for the formation of the telencephalon. During postnatal stages of brain development is necessary for ependymal cell maturation by promoting the maturation of radial glia into ependymal cells through regulation of neuroblast proliferation and migration (PubMed:22071110). Acts on the proliferation and differentiation of neural progenitor cells through activating transcription of CCND1 AND CCND2 (PubMed:17576749). During early lens formation plays a role in lens induction and specification by activating directly PAX6 in the presumptive lens ectoderm (PubMed:17066077). In turn PAX6 activates SIX3 resulting in activation of PDGFRA and CCND1 promoting cell proliferation (PubMed:12072567). Also is required for the neuroretina development by directly suppressing WNT8B expression in the anterior neural plate territory (PubMed:20890044). Its action during retina development and lens morphogenesis is AES and TLE4-dependent manner. Furthermore, during eye development regulates several genes expression. Before and during early lens development represses the CRYGF promoter by binding a SIX repressor element (PubMed:11139622). Directly activates RHO transcription, or cooperates with CRX or NRL (PubMed:17666527). Six3 functions also in the formation of the proximodistal axis of the optic cup (PubMed:12163408), and promotes the formation of optic vesicles-like structures (PubMed:11458394). During pituitary development, acts in parallel or alternatively with HESX1 to control cell proliferation through Wnt/beta-catenin pathway (PubMed:18694563). Plays a role in eye development by suppressing WNT1 expression and in dorsal-ventral patterning by repressing BMP signaling pathway (By similarity). {ECO:0000250|UniProtKB:O95343, ECO:0000269|PubMed:11139622, ECO:0000269|PubMed:11458394, ECO:0000269|PubMed:12050133, ECO:0000269|PubMed:12072567, ECO:0000269|PubMed:12163408, ECO:0000269|PubMed:12569128, ECO:0000269|PubMed:17066077, ECO:0000269|PubMed:17576749, ECO:0000269|PubMed:17666527, ECO:0000269|PubMed:18094027, ECO:0000269|PubMed:18694563, ECO:0000269|PubMed:18775421, ECO:0000269|PubMed:20682799, ECO:0000269|PubMed:20890044, ECO:0000269|PubMed:22071110}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:12050133}. SUBUNIT: Interacts with EYA4; translocates EYA4 from the cytoplasm to the nucleus and promotes activation of their target genes. Interacts with MTA1 and HDAC2; represses its own transcription. Interacts with MTA1; facilitates the binding of SIX3 to the core DNA motif of SIX3 promoter. Interacts with EYA1; promotes EYA1 translocation to the nucleus. Interacts with TLE1 and AES (via Q domain); can act in combination with either TLE1 and/or AES leading to transcriptional repression or activation, respectively (By similarity). Interacts (via homeobox) with NR4A3; differentially regulates the transcriptional activities NR4A3 (By similarity). Interacts with GMNN (By similarity). Interacts with TLE4. {ECO:0000250|UniProtKB:O95343, ECO:0000269|PubMed:12050133, ECO:0000269|PubMed:16024294, ECO:0000269|PubMed:17666527, ECO:0000269|PubMed:19606496}. TISSUE SPECIFICITY: Expressed in ependymal cells during the formation of the lateral wall. {ECO:0000269|PubMed:22071110}. +Q9QZ28 SIX6_MOUSE Homeobox protein SIX6 (Optic homeobox 2) (Sine oculis homeobox homolog 6) (Six9 protein) 246 27,741 Chain (1); DNA binding (1); Modified residue (5); Sequence conflict (2) FUNCTION: May be involved in eye development. {ECO:0000303|PubMed:10381575, ECO:0000303|PubMed:10473118, ECO:0000303|PubMed:9724757}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. SUBUNIT: Interacts with TLE4 and AES. {ECO:0000269|PubMed:12050133}. TISSUE SPECIFICITY: In the developing embryo, expressed mainly in the ventral optic stalk, optic chiasma, the neural retina and the primordial tissues that give rise to the pituitary/hypothalamus axis. Not expressed in the lens placode. {ECO:0000269|PubMed:10381575, ECO:0000269|PubMed:10473118}. +P63325 RS10_MOUSE 40S ribosomal protein S10 165 18,916 Chain (1); Cross-link (2); Modified residue (5) FUNCTION: Component of the 40S ribosomal subunit. {ECO:0000250}. PTM: Methylated by PRMT5. Methylation is necessary for its interaction with NPS1, its localization in the granular component (GC) region of the nucleolus, for the proper assembly of ribosomes, protein synthesis and optimal cell proliferation (By similarity). {ECO:0000250}.; PTM: Monoubiquitinated by ZNF598 when a ribosome has stalled during translation of poly(A) sequences, leading to preclude synthesis of a long poly-lysine tail and initiate the ribosome quality control (RQC) pathway to degrade the potentially detrimental aberrant nascent polypeptide. {ECO:0000250|UniProtKB:P46783}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Note=Localized in the granular component (GC) region of the nucleolus. Methylation is required for its localization in the GC region. Colocalizes with NPS1 in the GC region of the nucleolus (By similarity). {ECO:0000250}. SUBUNIT: Component of the small ribosomal subunit. Interacts with PRMT5. The methylated form interacts with NPM1 (By similarity). {ECO:0000250}. +Q8C263 SKA3_MOUSE Spindle and kinetochore-associated protein 3 411 45,370 Chain (1); Modified residue (6); Sequence conflict (1) FUNCTION: Component of the SKA1 complex, a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. The SKA1 complex is a direct component of the kinetochore-microtubule interface and directly associates with microtubules as oligomeric assemblies. The complex facilitates the processive movement of microspheres along a microtubule in a depolymerization-coupled manner. In the complex, it mediates the microtubule-stimulated oligomerization. Affinity for microtubules is synergistically enhanced in the presence of the ndc-80 complex and may allow the ndc-80 complex to track depolymerizing microtubules. {ECO:0000250|UniProtKB:Q8IX90}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q8IX90}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q8IX90}. Note=Localizes to the outer kinetochore and spindle microtubules during mitosis in a NDC80 complex-dependent manner. {ECO:0000250|UniProtKB:Q8IX90}. SUBUNIT: Component of the SKA1 complex, composed of SKA1, SKA2 and SKA3. The core SKA1 complex is composed of 2 SKA1-SKA2 heterodimers, each heterodimer interacting with a molecule of the SKA3 homodimer. The core SKA1 complex associates with microtubules and forms oligomeric assemblies. Interacts with SKA1; the interaction is direct. {ECO:0000250|UniProtKB:Q8IX90}. +Q6DIC0 SMCA2_MOUSE Probable global transcription activator SNF2L2 (EC 3.6.4.-) (ATP-dependent helicase SMARCA2) (BRG1-associated factor 190B) (BAF190B) (Protein brahma homolog) (SNF2-alpha) (SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2) 1577 180,253 Chain (1); Compositional bias (5); Cross-link (1); Domain (5); Modified residue (18); Motif (1); Nucleotide binding (1) FUNCTION: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. Binds DNA non-specifically (PubMed:22952240, PubMed:26601204). Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth. {ECO:0000250|UniProtKB:P51531, ECO:0000269|PubMed:17640523, ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00549}. SUBUNIT: Component of the multiprotein chromatin-remodeling complexes SWI/SNF: SWI/SNF-A (BAF), SWI/SNF-B (PBAF) and related complexes. The canonical complex contains a catalytic subunit (either SMARCA4/BRG1/BAF190A or SMARCA2/BRM/BAF190B) and at least SMARCE1, ACTL6A/BAF53, SMARCC1/BAF155, SMARCC2/BAF170, and SMARCB1/SNF5/BAF47. Other subunits specific to each of the complexes may also be present permitting several possible combinations developmentally and tissue specific (Probable). Component of the BAF complex, which includes at least actin (ACTB), ARID1A/BAF250A, ARID1B/BAF250B, SMARCA2/BRM, SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57, SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C (By similarity). In muscle cells, the BAF complex also contains DPF3 (By similarity). Component of neural progenitors-specific chromatin remodeling complex (npBAF complex) composed of at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, PHF10/BAF45A, ACTL6A/BAF53A and actin. Component of neuron-specific chromatin remodeling complex (nBAF complex) composed of at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, DPF1/BAF45B, DPF3/BAF45C, ACTL6B/BAF53B and actin (PubMed:17640523). Interacts with PHF10/BAF45A (By similarity). Interacts with CEBPB (when not methylated) (PubMed:20111005). Interacts with TOPBP1 (By similarity). Interacts with CEBPA (when phosphorylated) (PubMed:15107404). Interacts with DPF2 (By similarity). {ECO:0000250|UniProtKB:P51531, ECO:0000269|PubMed:15107404, ECO:0000269|PubMed:17640523, ECO:0000269|PubMed:20111005, ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}. TISSUE SPECIFICITY: Expressed in the cortex and the hippocampus. Expressed in the cortical plate in the embryo. {ECO:0000269|PubMed:22366787}. +Q9QZ39 SIA7A_MOUSE Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 1 (EC 2.4.99.3) (GalNAc alpha-2,6-sialyltransferase I) (ST6GalNAc I) (ST6GalNAcI) (Sialyltransferase 7A) (SIAT7-A) 526 60,734 Chain (1); Disulfide bond (1); Glycosylation (5); Sequence conflict (10); Topological domain (2); Transmembrane (1) TRANSMEM 13 33 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 12 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 34 526 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Transfers CMP-NeuAc with an alpha-2,6-linkage to the GalNAc residues of GalNAc-O-Ser/Thr, Gal-beta-1,3-GalNAc-O-Ser/Thr and NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc-O-Ser/Thr are substrates. Higher activity towards GalNAc-O-Ser/Thr. {ECO:0000269|PubMed:10788794}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Submaxillary gland, mammary gland, spleen and colon. +Q9R2B6 SIA7D_MOUSE Alpha-N-acetyl-neuraminyl-2,3-beta-galactosyl-1,3-N-acetyl-galactosaminide alpha-2,6-sialyltransferase (EC 2.4.99.7) (NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc-alpha-2,6-sialyltransferase) (ST6GalNAc IV) (ST6GalNAcIV) (Sialyltransferase 7D) (SIAT7-D) 360 40,773 Alternative sequence (2); Chain (1); Disulfide bond (1); Glycosylation (1); Topological domain (2); Transmembrane (1) TRANSMEM 72 94 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 71 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 95 360 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Involved in the biosynthesis of ganglioside GD1A from GM1B. Transfers CMP-NeuAc with an alpha-2,6-linkage to GalNAc residue on NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc of glycoproteins and glycolipids. Prefers glycoproteins to glycolipids. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. TISSUE SPECIFICITY: High expression in brain and colon and to a lesser extent in lung, heart, kidney, spleen and thymus. {ECO:0000269|PubMed:10207017}. +Q80ZE3 SIG10_MOUSE Sialic acid-binding Ig-like lectin 10 (Siglec-10) (Sialic acid-binding Ig-like lectin G) (Siglec-G) (mSiglec-G) 688 76,884 Binding site (1); Chain (1); Disulfide bond (5); Domain (4); Glycosylation (2); Modified residue (1); Motif (2); Mutagenesis (5); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 544 564 Helical. {ECO:0000255}. TOPO_DOM 18 543 Extracellular. {ECO:0000255}.; TOPO_DOM 565 688 Cytoplasmic. {ECO:0000255}. FUNCTION: Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,3- or alpha-2,6-linked sialic acid (PubMed:20038598). The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, seems to act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules (By similarity). Involved in negative regulation of B-cell antigen receptor signaling and specifically acts on B1 cells to inhibit Ca(2+) signaling, cellular expansion and antibody secretion (PubMed:17572677). The inhibition of B cell activation is dependent on PTPN6/SHP-1 (PubMed:23836061). In association with CD24 may be involved in the selective suppression of the immune response to danger-associated molecular patterns (DAMPs) such as HMGB1, HSP70 and HSP90 (PubMed:19264983). In association with CD24 may regulate the immune repsonse of natural killer (NK) cells (By similarity). Plays a role in the control of autoimmunity (PubMed:20200274). During initiation of adaptive immune responses by CD8-alpha(+) dendritic cells inhibits cross-presentation by impairing the formation of MHC class I-peptide complexes. The function seems to implicate recruitment of PTPN6/SHP-1, which dephosphorylates NCF1 of the NADPH oxidase complex consequently promoting phagosomal acidification (PubMed:27548433). {ECO:0000250|UniProtKB:Q96LC7, ECO:0000269|PubMed:17572677, ECO:0000269|PubMed:19264983, ECO:0000269|PubMed:20038598, ECO:0000269|PubMed:20200274, ECO:0000269|PubMed:27548433}.; FUNCTION: (Microbial infection) During infection by RNA viruses inhibits DDX58/RIG-I signaling in macrophages by promoting its CBL-dependent ubiquitination and degradation via PTPN11/SHP-2. {ECO:0000269|PubMed:23374343}. PTM: Phosphorylation of Tyr-659 is involved in binding to PTPN6. {ECO:0000250|UniProtKB:Q96LC7}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q96LC7}; Single-pass type I membrane protein. SUBUNIT: Interacts with PTPN6/SHP-1 upon phosphorylation. Interacts with NCF1 (PubMed:27548433). Interacts with CD24; the probable CD24:SIGLEC10 complex is proposed to inhibit HGMB1-mediated tissue damage immune response. Interacts with HMGB1; the interaction is dependent on CD24 (PubMed:19264983). Associates with membrane IgM on the B cell surface (PubMed:24790146). Interacts with DDX58, CBL and PTPN11 (PubMed:23374343). {ECO:0000250|UniProtKB:Q96LC7, ECO:0000269|PubMed:19264983, ECO:0000269|PubMed:23374343, ECO:0000269|PubMed:24790146, ECO:0000269|PubMed:27548433}. DOMAIN: Contains 1 copy of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is involved in modulation of cellular responses. The phosphorylated ITIM motif can bind the SH2 domain of several SH2-containing phosphatases. TISSUE SPECIFICITY: Expressed in B cells with high levels in pre-B cells and B1a cells of the peritoneal cavity. {ECO:0000269|PubMed:17572677}. +Q91Y57 SIG12_MOUSE Sialic acid-binding Ig-like lectin 12 (Siglec-12) (Myeloid inhibitory siglec) (MIS) (Sialic acid-binding Ig-like lectin 5) (Siglec-5) (Sialic acid-binding Ig-like lectin E) (Siglec-E) (mSiglec-E) (Sialic acid-binding Ig-like lectin-like 1) (Siglec-L1) 467 51,901 Binding site (1); Chain (1); Disulfide bond (4); Domain (3); Glycosylation (10); Modified residue (2); Motif (2); Mutagenesis (2); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 354 374 Helical. {ECO:0000255}. TOPO_DOM 19 353 Extracellular. {ECO:0000255}.; TOPO_DOM 375 467 Cytoplasmic. {ECO:0000255}. FUNCTION: Putative adhesion molecule that mediates sialic-acid dependent binding to cells. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules. PTM: Phosphorylation of Tyr-432 is required for binding to PTPN6 and PTPN11. Phosphorylation of Tyr-455 is involved in binding to PTPN6. Tyr-432 needs to be phosphorylated prior to Tyr-455. {ECO:0000269|PubMed:11171044, ECO:0000269|PubMed:11278955}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Homodimer; disulfide-linked. Interacts with PTPN6/SHP-1 and PTPN11/SHP-2 upon phosphorylation. {ECO:0000269|PubMed:11171044, ECO:0000269|PubMed:11278955}. DOMAIN: Contains 1 copy of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is involved in modulation of cellular responses. The phosphorylated ITIM motif can bind the SH2 domain of several SH2-containing phosphatases. TISSUE SPECIFICITY: Expressed by monocytic/myeloid lineage cells. Found at higher levels in spleen, liver and heart. Found at lower levels in kidney and lung. +Q9JLZ8 SIGIR_MOUSE Single Ig IL-1-related receptor (Single Ig IL-1R-related molecule) (Single immunoglobulin domain-containing IL1R-related protein) (Toll/interleukin-1 receptor 8) (TIR8) 409 46,159 Alternative sequence (1); Chain (1); Disulfide bond (1); Domain (2); Frameshift (1); Glycosylation (5); Modified residue (1); Sequence conflict (3); Topological domain (2); Transmembrane (1) TRANSMEM 118 138 Helical; Signal-anchor for type III membrane protein. {ECO:0000255}. TOPO_DOM 1 117 Extracellular. {ECO:0000255}.; TOPO_DOM 139 409 Cytoplasmic. {ECO:0000255}. FUNCTION: Acts as a negative regulator of the Toll-like and IL-1R receptor signaling pathways. Attenuates the recruitment of receptor-proximal signaling components to the TLR4 receptor, probably through an TIR-TIR domain interaction with TLR4. Through its extracellular domain interferes with the heterodimerization of Il1R1 and IL1RAP (By similarity). {ECO:0000250, ECO:0000269|PubMed:12925853}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type III membrane protein {ECO:0000305}. SUBUNIT: Interacts with IL1R1, IRAK1, TLR4, TLR5, TLR9 and TRAF6. Upon IL-1 stimulation found in a complex at least composed of IL1R1, SIGIRR, MYD88, IRAK1 and TRAF6. Upon stimulation with LPC found in a complex at least composed of TLR4, SIG1IR, MYD88, IRAK1 and TRAF6. Interacts with PALM3 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed at high levels in kidney, and at moderate levels in colon, small intestine, lung, spleen and liver. Not expressed in brain and muscle. Expressed at high levels in epithelial cells, at moderate levels in splenocytes, and at low or undetectable levels in fibroblasts or endothelial cells. Expressed in mucosal and dendritic cells. {ECO:0000269|PubMed:12925853, ECO:0000269|PubMed:14993616, ECO:0000269|PubMed:21077278}. +Q920G3 SIGL5_MOUSE Sialic acid-binding Ig-like lectin 5 (Siglec-5) (Sialic acid-binding Ig-like lectin F) (Siglec-F) (mSiglec-F) (CD antigen CD170) 569 61,476 Binding site (3); Chain (1); Disulfide bond (4); Domain (3); Glycosylation (7); Motif (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 440 460 Helical. {ECO:0000255}. TOPO_DOM 17 439 Extracellular. {ECO:0000255}.; TOPO_DOM 461 569 Cytoplasmic. {ECO:0000255}. FUNCTION: Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,3-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. DOMAIN: Contains 1 copy of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is involved in modulation of cellular responses. The phosphorylated ITIM motif can bind the SH2 domain of several SH2-containing phosphatases. TISSUE SPECIFICITY: Predominantly expressed by immature monocytic/myeloid lineage cells in bone marrow. Also found at lower levels in mature neutrophils and monocytes. +Q60670 SIK1_MOUSE Serine/threonine-protein kinase SIK1 (EC 2.7.11.1) (HRT-20) (Myocardial SNF1-like kinase) (Salt-inducible kinase 1) (SIK-1) (Serine/threonine-protein kinase SNF1-like kinase 1) (Serine/threonine-protein kinase SNF1LK) 779 85,115 Active site (1); Binding site (1); Chain (1); Domain (2); Modified residue (4); Mutagenesis (12); Nucleotide binding (1); Region (1); Sequence conflict (1) FUNCTION: Serine/threonine-protein kinase involved in various processes such as cell cycle regulation, gluconeogenesis and lipogenesis regulation, muscle growth and differentiation and tumor suppression. Phosphorylates HDAC4, HDAC5, PPME1, SREBF1, CRTC1/TORC1 and CRTC2/TORC2. Acts as a tumor suppressor and plays a key role in p53/TP53-dependent anoikis, a type of apoptosis triggered by cell detachment: required for phosphorylation of p53/TP53 in response to loss of adhesion and is able to suppress metastasis. Part of a sodium-sensing signaling network, probably by mediating phosphorylation of PPME1: following increases in intracellular sodium, SIK1 is activated by CaMK1 and phosphorylates PPME1 subunit of protein phosphatase 2A (PP2A), leading to dephosphorylation of sodium/potassium-transporting ATPase ATP1A1 and subsequent increase activity of ATP1A1. Acts as a regulator of muscle cells by phosphorylating and inhibiting class II histone deacetylases HDAC4 and HDAC5, leading to promote expression of MEF2 target genes in myocytes. Also required during cardiomyogenesis by regulating the exit of cardiomyoblasts from the cell cycle via down-regulation of CDKN1C/p57Kip2. Acts as a regulator of hepatic gluconeogenesis by phosphorylating and repressing the CREB-specific coactivators CRTC1/TORC1 and CRTC2/TORC2, leading to inhibit CREB activity. Also regulates hepatic lipogenesis by phosphorylating and inhibiting SREBF1. In concert with CRTC1/TORC1, regulates the light-induced entrainment of the circadian clock by attenuating PER1 induction; represses CREB-mediated transcription of PER1 by phosphorylating and deactivating CRTC1/TORC1. {ECO:0000269|PubMed:12200423, ECO:0000269|PubMed:15177563, ECO:0000269|PubMed:15511237, ECO:0000269|PubMed:16148943, ECO:0000269|PubMed:16817901, ECO:0000269|PubMed:17468767, ECO:0000269|PubMed:19244231, ECO:0000269|PubMed:19622832, ECO:0000269|PubMed:20140255, ECO:0000269|PubMed:23993098}. PTM: Phosphorylated at Thr-182 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39, leading to its activation. Phosphorylation at Thr-182 promotes autophosphorylation at Ser-186, which is required for sustained activity. Autophosphorylation at Ser-186 is maintained by sequential phosphorylation at Thr-182 by GSK3-beta. GSK3-beta cannot initiate phosphorylation at Thr-182, it can only maintain it. Phosphorylation at Ser-577 by PKA promotes translocation to the cytoplasm. Phosphorylation at Thr-322 by CaMK1 following intracellular sodium concentration leads to activation. {ECO:0000269|PubMed:12200423, ECO:0000269|PubMed:16817901, ECO:0000269|PubMed:17468767}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Following ACTH (adrenocorticotropic hormone) treatment and subsequent phosphorylation by PKA, translocates to the cytoplasm, where it binds to YWHAZ. SUBUNIT: Interacts (when phosphorylated on Thr-182 and Ser-186) with YWHAZ. Interacts with ATP1A1 (By similarity). {ECO:0000250}. DOMAIN: The RK-rich region determines the subcellular location. {ECO:0000269|PubMed:15511237}. TISSUE SPECIFICITY: Expressed in lung, skin, ovary, heart and stomach. No expression in brain, liver or adult skeletal muscle but is present in skeletal muscle progenitor cells of the somite beginning at 9.5 dpc. Present at 8.0 dpc in the monolayer of presumptive myocardial cells but rapidly down-regulated at 8.5 dpc upon primitive ventricle formation, although still present in myocardial cells that will populate the primitive atrium and bulbus cordis. At 9.5 dpc expression is down-regulated in the primitive atrium but observed in the sinus venosus and truncus arteriosus. {ECO:0000269|PubMed:15177563, ECO:0000269|PubMed:7893599}. +Q8CFH6 SIK2_MOUSE Serine/threonine-protein kinase SIK2 (EC 2.7.11.1) (Salt-inducible kinase 2) (SIK-2) (Serine/threonine-protein kinase SNF1-like kinase 2) 931 104,198 Active site (1); Binding site (1); Chain (1); Domain (2); Modified residue (8); Mutagenesis (8); Nucleotide binding (1); Region (1) FUNCTION: Phosphorylates 'Ser-789' of IRS1 in insulin-stimulated adipocytes, potentially modulating the efficiency of insulin signal transduction. Inhibits CREB activity by phosphorylating and inhibiting activity of TORCs, the CREB-specific coactivators, like CRTC2/TORC2 and CRTC3/TORC3 in response to cAMP signaling (PubMed:29211348). {ECO:0000269|PubMed:12624099, ECO:0000269|PubMed:16817901, ECO:0000269|PubMed:29211348}. PTM: Phosphorylated at Thr-175 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39 (By similarity). Phosphorylation at Ser-358, Thr-484 and/or Ser-587 following cAMP signaling is required for 14-3-3 interaction and thus inactivation (PubMed:29211348). {ECO:0000250|UniProtKB:Q9H0K1, ECO:0000269|PubMed:29211348}.; PTM: Acetylation at Lys-53 inhibits kinase activity. Deacetylated by HDAC6 (By similarity). {ECO:0000250|UniProtKB:Q9H0K1}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12624099}. SUBUNIT: Interacts with and phosphorylates TORC2/CRTC2 (PubMed:29211348). Interacts (when phosphorylated at Ser-343, Ser-358, Thr-484 and/or Ser-587) with 14-3-3 proteins; the interaction inhibits its kinase activity towards TORCs (PubMed:29211348). There is a cooperative effect of the phosphorylation sites in 14-3-3 binding as the interaction is stronger when more sites are modified. {ECO:0000269|PubMed:29211348}. DOMAIN: The RK-rich region is required for cAMP responsiveness. {ECO:0000269|PubMed:29211348}. TISSUE SPECIFICITY: Present in both white and brown adipose tissues with levels increasing during adipocyte differentiation. Lower levels observed in the testis. {ECO:0000269|PubMed:12624099}. +Q6P4S6 SIK3_MOUSE Serine/threonine-protein kinase SIK3 (EC 2.7.11.1) (Salt-inducible kinase 3) (SIK-3) (Serine/threonine-protein kinase QSK) 1311 145,784 Active site (1); Alternative sequence (2); Binding site (1); Chain (1); Compositional bias (1); Domain (2); Modified residue (11); Nucleotide binding (1); Sequence conflict (4) PTM: Phosphorylated at Thr-163 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Note=Locates to punctate structures within the cytoplasm on binding to YWHAZ. {ECO:0000250}. SUBUNIT: Binds to and is activated by YWHAZ when phosphorylated on Thr-163. {ECO:0000250}. +Q3UTD9 SIM15_MOUSE Small integral membrane protein 15 74 8,591 Chain (1); Coiled coil (1); Transmembrane (1) TRANSMEM 20 40 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q0VG18 SIM24_MOUSE Small integral membrane protein 24 120 13,547 Chain (1); Modified residue (2); Signal peptide (1); Transmembrane (1) TRANSMEM 31 51 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q8R043 SIM29_MOUSE Small integral membrane protein 29 (Uncharacterized protein SMIM29) 102 11,553 Chain (1); Glycosylation (1); Transmembrane (1) TRANSMEM 21 41 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. +Q61079 SIM2_MOUSE Single-minded homolog 2 (SIM transcription factor) (mSIM) 657 72,513 Chain (1); Domain (5); Frameshift (1); Motif (1); Sequence conflict (10) FUNCTION: Transcription factor that may be a master gene of CNS development in cooperation with Arnt. It may have pleiotropic effects in the tissues expressed during development. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00632, ECO:0000255|PROSITE-ProRule:PRU00981}. SUBUNIT: Efficient DNA binding requires dimerization with another bHLH protein. Heterodimer of SIM2 and ARNT. {ECO:0000269|PubMed:9020169}. TISSUE SPECIFICITY: Transcripts were detected in high levels in kidney followed by skeletal muscle and lung. Low levels were found in testis, brain and heart. In early fetal development it is found in CNS, developing kidney, tongue epithelium and cartilage primordia. +Q3V2G4 SIM31_MOUSE Small integral membrane protein 31 71 8,514 Chain (1); Glycosylation (1); Transmembrane (1) TRANSMEM 8 28 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. +E9Q2Z6 SIM35_MOUSE Small integral membrane protein 35 85 9,396 Chain (1); Transmembrane (1) TRANSMEM 7 27 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. +A0A1B0GRQ0 SIM36_MOUSE Small integral membrane protein 36 93 10,272 Chain (1); Sequence conflict (1); Transmembrane (1) TRANSMEM 14 34 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. +Q80X95 RRAGA_MOUSE Ras-related GTP-binding protein A (Rag A) (RagA) 313 36,566 Chain (1); Cross-link (4); Erroneous initiation (1); Frameshift (1); Modified residue (1); Nucleotide binding (3) FUNCTION: Guanine nucleotide-binding protein that plays a crucial role in the cellular response to amino acid availability through regulation of the mTORC1 signaling cascade. Forms heterodimeric Rag complexes with RRAGC or RRAGD and cycles between an inactive GDP-bound and an active GTP-bound form. In its active form participates in the relocalization of mTORC1 to the lysosomes and its subsequent activation by the GTPase RHEB. Involved in the RCC1/Ran-GTPase pathway. May play a direct role in a TNF-alpha signaling pathway leading to induction of cell death. {ECO:0000250|UniProtKB:Q7L523}. PTM: Ubiquitinated. 'Lys-68'-linked polyubiquitination of the GDP-bound inactive form of RRAGA at Lys-142, Lys-220, Lys-230 and Lys-244 by RNF152 is increased in response to amino acid starvation. Polyubiquitination promotes interaction with the GATOR1 complex. This does not affect RRAGA degradation. {ECO:0000250|UniProtKB:Q7L523}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Lysosome {ECO:0000250}. Note=Predominantly cytoplasmic. May shuttle between the cytoplasm and nucleus, depending on the bound nucleotide state (By similarity). {ECO:0000250}. SUBUNIT: Can occur as a homodimer or as a heterodimer with RRAGC or RRAGD in a sequence-independent manner; heterodimerization stabilizes proteins of the heterodimer. In complex with RRAGC, but not with RRAGB, interacts with RPTOR. The GTP-bound form of RRAGA interacts with NOL8. Interacts with SH3BP4; the interaction with this negative regulator is most probably direct, preferentially occurs with the inactive GDP-bound form of RRAGA and is negatively regulated by amino acids. The Rag heterodimer interacts with SLC38A9; the probable amino acid sensor. Interacts (inactive GDP-bound form) with RNF152; stimulated by amino acid starvation. Interacts (polyubiquitinated) with the GATOR1 complex; inactivates RRAGA. Interacts (polyubiquitinated) with TSC2 (By similarity). Interacts with SESN1, SESN2 AND SESN3 (PubMed:25259925). {ECO:0000250|UniProtKB:Q7L523, ECO:0000269|PubMed:25259925}. +Q7TT45 RRAGD_MOUSE Ras-related GTP-binding protein D (Rag D) (RagD) 449 51,232 Chain (1); Nucleotide binding (3); Sequence conflict (5) FUNCTION: Guanine nucleotide-binding protein forming heterodimeric Rag complexes required for the amino acid-induced relocalization of mTORC1 to the lysosomes and its subsequent activation by the GTPase RHEB. This is a crucial step in the activation of the TOR signaling cascade by amino acids (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NQL2}. Nucleus {ECO:0000250|UniProtKB:Q9NQL2}. Lysosome {ECO:0000250|UniProtKB:Q9NQL2}. Note=Predominantly cytoplasmic. May shuttle between the cytoplasm and nucleus, depending on the bound nucleotide state of associated RRAGA. {ECO:0000250|UniProtKB:Q9NQL2}. SUBUNIT: Forms a heterodimer with RRAGA in a sequence-independent manner and RRAGB. Heterodimerization stabilizes RRAG proteins. In complex with RRAGB, interacts with RPTOR; this interaction is particularly efficient with GTP-loaded RRAGB and GDP-loaded RRAGC. Interacts with NOL8. Interacts with SH3BP4; the interaction with this negative regulator is most probably direct, preferentially occurs with the inactive GDP-bound form of RRAGD and is negatively regulated by amino acids. The Rag heterodimer interacts with SLC38A9; the probable amino acid sensor (By similarity). Interacts with SESN1, SESN2 AND SESN3 (PubMed:25259925). {ECO:0000250|UniProtKB:Q9NQL2, ECO:0000269|PubMed:25259925}. +P62071 RRAS2_MOUSE Ras-related protein R-Ras2 204 23,400 Chain (1); Initiator methionine (1); Lipidation (2); Modified residue (3); Motif (1); Nucleotide binding (4); Propeptide (1); Sequence conflict (2) FUNCTION: It is a plasma membrane-associated GTP-binding protein with GTPase activity. Might transduce growth inhibitory signals across the cell membrane, exerting its effect through an effector shared with the Ras proteins but in an antagonistic fashion. PTM: May be post-translationally modified by both palmitoylation and polyisoprenylation. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Inner surface of plasma membrane possibly with attachment requiring acylation of the C-terminal cysteine (By similarity with RAS). +P10833 RRAS_MOUSE Ras-related protein R-Ras (p23) 218 23,764 Chain (1); Lipidation (1); Modified residue (1); Motif (1); Nucleotide binding (4); Propeptide (1) FUNCTION: Regulates the organization of the actin cytoskeleton. With OSPBL3, modulates integrin beta-1 (ITGB1) activity. {ECO:0000250|UniProtKB:P10301}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Inner surface of plasma membrane possibly with attachment requiring acylation of the C-terminal cysteine (By similarity with RAS). SUBUNIT: Interacts with PLCE1. Interacts (active GTP-bound form preferentially) with RGS14. Interacts with OSBPL3. {ECO:0000250|UniProtKB:D3Z8L7, ECO:0000250|UniProtKB:P10301}. +Q62141 SIN3B_MOUSE Paired amphipathic helix protein Sin3b (Histone deacetylase complex subunit Sin3b) (Transcriptional corepressor Sin3b) 1098 126,405 Alternative sequence (5); Beta strand (2); Chain (1); Domain (3); Erroneous initiation (1); Helix (10); Modified residue (2); Region (4); Sequence conflict (2); Turn (3) FUNCTION: Acts as a transcriptional repressor. Interacts with MXI1 to repress MYC responsive genes and antagonize MYC oncogenic activities. Interacts with MAD-MAX heterodimers by binding to MAD. The heterodimer then represses transcription by tethering SIN3B to DNA. Also forms a complex with FOXK1 which represses transcription. With FOXK1, regulates cell cycle progression probably by repressing cell cycle inhibitor genes expression (PubMed:22476904). {ECO:0000269|PubMed:10620510, ECO:0000269|PubMed:22476904, ECO:0000269|PubMed:7889570}. PTM: Ubiquitinated by RNF220 that leads to proteasomal degradation. {ECO:0000269|PubMed:20170641}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00810, ECO:0000269|PubMed:20170641, ECO:0000269|PubMed:7889570}. SUBUNIT: Interacts with FOXK1/MNF, MXI, MAD, NCOR1 and SAP30. Interaction with SUDS3 enhances the interaction with HDAC1 to form a complex. Interacts with CRY1, HCFC1, MAD3, MAD4, MAEL, REST, RNF220 and SETDB1. Interacts with MYT1L (PubMed:28379941). Interacts with C6orf89 (By similarity). {ECO:0000250|UniProtKB:O75182, ECO:0000269|PubMed:10620510, ECO:0000269|PubMed:11101889, ECO:0000269|PubMed:11909966, ECO:0000269|PubMed:12398767, ECO:0000269|PubMed:15226430, ECO:0000269|PubMed:16288918, ECO:0000269|PubMed:16787967, ECO:0000269|PubMed:20170641, ECO:0000269|PubMed:22476904, ECO:0000269|PubMed:28379941, ECO:0000269|PubMed:7889570, ECO:0000269|PubMed:8521822, ECO:0000269|PubMed:9139820, ECO:0000269|PubMed:9702189}. +Q8R2Q4 RRF2M_MOUSE Ribosome-releasing factor 2, mitochondrial (RRF2mt) (Elongation factor G 2, mitochondrial) (EF-G2mt) (mEF-G 2) 779 86,109 Alternative sequence (2); Chain (1); Domain (1); Nucleotide binding (3); Sequence conflict (3) FUNCTION: Mitochondrial GTPase that mediates the disassembly of ribosomes from messenger RNA at the termination of mitochondrial protein biosynthesis. Acts in collaboration with MRRF. GTP hydrolysis follows the ribosome disassembly and probably occurs on the ribosome large subunit. Not involved in the GTP-dependent ribosomal translocation step during translation elongation. {ECO:0000255|HAMAP-Rule:MF_03059}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03059}. +Q9CYH6 RRS1_MOUSE Ribosome biogenesis regulatory protein homolog 365 41,552 Chain (1); Compositional bias (1); Cross-link (3); Modified residue (2); Sequence conflict (3) FUNCTION: Involved in ribosomal large subunit assembly. May regulate the localization of the 5S RNP/5S ribonucleoprotein particle to the nucleolus. {ECO:0000250|UniProtKB:Q15050}. PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q15050}. +Q6NS46 RRP5_MOUSE Protein RRP5 homolog (Apoptosis-linked gene 4 protein) (Programmed cell death protein 11) 1862 207,779 Chain (1); Cross-link (1); Domain (13); Erroneous initiation (2); Initiator methionine (1); Modified residue (5); Repeat (4); Sequence caution (1); Sequence conflict (11) FUNCTION: Essential for the generation of mature 18S rRNA, specifically necessary for cleavages at sites A0, 1 and 2 of the 47S precursor. Directly interacts with U3 snoRNA (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. SUBUNIT: Interacts with NF-kappa-B p50/NFKB1 and NF-kappa-B p65/RELA. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10229231}. +Q9D1C9 RRP7A_MOUSE Ribosomal RNA-processing protein 7 homolog A (Gastric cancer antigen Zg14 homolog) 280 32,399 Chain (1); Domain (1); Modified residue (1); Sequence conflict (1) +Q62232 SIX2_MOUSE Homeobox protein SIX2 (Sine oculis homeobox homolog 2) 296 32,718 Chain (1); DNA binding (1); Erroneous initiation (1); Sequence conflict (2) FUNCTION: Transcription factor that plays an important role in the development of several organs, including kidney, skull and stomach. During kidney development, maintains cap mesenchyme multipotent nephron progenitor cells in an undifferentiated state by opposing the inductive signals emanating from the ureteric bud and cooperates with WNT9B to promote renewing progenitor cells proliferation. Acts through its interaction with TCF7L2 and OSR1 in a canonical Wnt signaling independent manner preventing transcription of differentiation genes in cap mesenchyme such as WNT4. Also acts independently of OSR1 to activate expression of many cap mesenchyme genes, including itself, GDNF and OSR1. During craniofacial development plays a role in growth and elongation of the cranial base through regulation of chondrocyte differentiation (PubMed:20515681). During stomach organogenesis, controls pyloric sphincter formation and mucosal growth through regulation of a gene network including NKX2-5, BMPR1B, BMP4, SOX9 and GREM1 (PubMed:19660448). During branchial arch development, acts to mediate HOXA2 control over the insulin-like growth factor pathway (PubMed:18321982). Also may be involved in limb tendon and ligament development (PubMed:7720577). Plays a role in cell proliferation and migration (By similarity). {ECO:0000250|UniProtKB:Q9NPC8, ECO:0000269|PubMed:17036046, ECO:0000269|PubMed:18321982, ECO:0000269|PubMed:18682239, ECO:0000269|PubMed:19660448, ECO:0000269|PubMed:20515681, ECO:0000269|PubMed:21350016, ECO:0000269|PubMed:22902740, ECO:0000269|PubMed:24598167, ECO:0000269|PubMed:7720577}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8814301}. SUBUNIT: Interacts with TCF7L2; in a canonical Wnt signaling independent manner; prevents transcription of differentiation genes in cap mesenchyme. Interacts with OSR1; form a strong repressor complex with TCF7L2, TLE2 and TLE3 to prevent the activation of Wnt/beta-catenin target genes in the cap mesenchyme. Interacts with HOXA11, EYA1 and EYA3. {ECO:0000269|PubMed:11734542, ECO:0000269|PubMed:12215533, ECO:0000269|PubMed:22902740, ECO:0000269|PubMed:24598167}. TISSUE SPECIFICITY: Expressed in phalangeal tendons, in smooth muscle and in head and body mesenchyme. +Q9CPV1 SKA1_MOUSE Spindle and kinetochore-associated protein 1 254 29,445 Chain (1); Coiled coil (1); Region (1); Sequence conflict (5) FUNCTION: Component of the SKA1 complex, a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. Required for timely anaphase onset during mitosis, when chromosomes undergo bipolar attachment on spindle microtubules leading to silencing of the spindle checkpoint. The SKA1 complex is a direct component of the kinetochore-microtubule interface and directly associates with microtubules as oligomeric assemblies. The complex facilitates the processive movement of microspheres along a microtubule in a depolymerization-coupled manner. Affinity for microtubules is synergistically enhanced in the presence of the ndc-80 complex and may allow the ndc-80 complex to track depolymerizing microtubules. In the complex, it mediates the interaction with microtubules. {ECO:0000250|UniProtKB:Q96BD8}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q96BD8}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q96BD8}. Note=Localizes to the outer kinetochore and spindle microtubules during mitosis in a NDC80 complex-dependent manner. Localizes to both the mitotic spindle and kinetochore-associated proteins. Associates with kinetochores following microtubule attachment from prometaphase, through mid-anaphase and then vanishes in telophase. {ECO:0000250|UniProtKB:Q96BD8}. SUBUNIT: Component of the SKA1 complex, composed of SKA1, SKA2 and SKA3. Forms a heterodimer with SKA2; the heterodimer interacting with SKA3. The core SKA1 complex is composed of 2 SKA1-SKA2 heterodimers, each heterodimer interacting with a molecule of the SKA3 homodimer. The core SKA1 complex associates with microtubules and forms oligomeric assemblies. Interacts with microtubules; the interaction is direct. Interacts with SKA2. Interacts with SKA3. {ECO:0000250|UniProtKB:Q96BD8}. +Q9CR46 SKA2_MOUSE Spindle and kinetochore-associated protein 2 (Protein FAM33A) 120 13,725 Chain (1) FUNCTION: Component of the SKA1 complex, a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. Required for timely anaphase onset during mitosis, when chromosomes undergo bipolar attachment on spindle microtubules leading to silencing of the spindle checkpoint. The SKA1 complex is a direct component of the kinetochore-microtubule interface and directly associates with microtubules as oligomeric assemblies. The complex facilitates the processive movement of microspheres along a microtubule in a depolymerization-coupled manner. In the complex, it is required for SKA1 localization. Affinity for microtubules is synergistically enhanced in the presence of the ndc-80 complex and may allow the ndc-80 complex to track depolymerizing microtubules. {ECO:0000250|UniProtKB:Q8WVK7}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q8WVK7}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q8WVK7}. Note=Localizes to the outer kinetochore and spindle microtubules during mitosis in a NDC80 complex-dependent manner. Localizes to both the mitotic spindle and kinetochore-associated proteins. {ECO:0000250|UniProtKB:Q8WVK7}. SUBUNIT: Component of the SKA1 complex, composed of SKA1, SKA2 and SKA3. Forms a heterodimer with SKA1; the heterodimer interacting with SKA3. The core SKA1 complex is composed of 2 SKA1-SKA2 heterodimers, each heterodimer interacting with a molecule of the SKA3 homodimer. The core SKA1 complex associates with microtubules and forms oligomeric assemblies. Interacts directly with SKA1. Binds directly to microtubules; but with a much lower affinity than SKA1 in vivo (By similarity). {ECO:0000250}. +Q3UUV5 SKAP1_MOUSE Src kinase-associated phosphoprotein 1 (Src family-associated phosphoprotein 1) 355 40,962 Alternative sequence (4); Chain (1); Compositional bias (2); Domain (2); Modified residue (4); Region (1); Sequence conflict (1) FUNCTION: Positively regulates T-cell receptor signaling by enhancing the MAP kinase pathway. Required for optimal conjugation between T-cells and antigen-presenting cells by promoting the clustering of integrin ITGAL on the surface of T-cells. May be involved in high affinity immunoglobulin epsilon receptor signaling in mast cells (By similarity). {ECO:0000250}. PTM: Phosphorylated on tyrosines. Phosphorylation by FYN on Tyr-268 is required for GRB2 interaction. Phosphorylation by FYN on Tyr-291 abolishes interaction with FYB1. Tyr-237 is dephosphorylated by PTPRC (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Upon T-cell stimulation, translocates to lipid rafts at the cell membrane. {ECO:0000250}. SUBUNIT: Homodimer. Interacts with FYN and PTPRC. Interacts with GRB2 when phosphorylated on Tyr-268. Interacts with FYB1, which is required for SKAP2 protein stability. Part of a complex consisting of SKAP1, FYB1 and CLNK. Interacts with RASGRP1. Interacts with FYB2. {ECO:0000250|UniProtKB:Q4V7G1, ECO:0000250|UniProtKB:Q86WV1}. DOMAIN: The SH3 domain interacts with FYB1. {ECO:0000250}. +Q80YR3 SKDA1_MOUSE SKI/DACH domain-containing protein 1 (Protein DLN-1) 822 90,309 Chain (1); Compositional bias (7); Cross-link (1); Erroneous gene model prediction (2); Sequence conflict (1) +P58006 SESN1_MOUSE Sestrin-1 (EC 1.11.1.15) 492 56,637 Active site (1); Binding site (2); Chain (1); Modified residue (2); Region (3); Sequence conflict (1) FUNCTION: Functions as an intracellular leucine sensor that negatively regulates the TORC1 signaling pathway through the GATOR complex. In absence of leucine, binds the GATOR subcomplex GATOR2 and prevents TORC1 signaling. Binding of leucine to SESN2 disrupts its interaction with GATOR2 thereby activating the TORC1 signaling pathway (PubMed:25259925). This stress-inducible metabolic regulator may also play a role in protection against oxidative and genotoxic stresses. May positively regulate the transcription by NFE2L2 of genes involved in the response to oxidative stress by facilitating the SQSTM1-mediated autophagic degradation of KEAP1. May have an alkylhydroperoxide reductase activity born by the N-terminal domain of the protein. Was originally reported to contribute to oxidative stress resistance by reducing PRDX1. However, this could not be confirmed (By similarity). {ECO:0000250|UniProtKB:P58004, ECO:0000269|PubMed:25259925}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y6P5}. Cytoplasm {ECO:0000250|UniProtKB:Q9Y6P5}. SUBUNIT: Interacts with the GATOR2 complex which is composed of MIOS, SEC13, SEH1L, WDR24 and WDR59; the interaction is negatively regulated by leucine (By similarity). Interacts with RRAGA, RRAGB, RRAGC and RRAGD; may function as a guanine nucleotide dissociation inhibitor for RRAGs and regulate them (PubMed:25259925). Interacts with KEAP1, RBX1 and SQSTM1; in the SQSTM1-dependent autophagic degradation of KEAP1. May interact with PRDX1 (By similarity). {ECO:0000250|UniProtKB:Q9Y6P5, ECO:0000269|PubMed:25259925}. DOMAIN: Composed of an N-terminal domain that has an alkylhydroperoxide reductase activity and a C-terminal domain that mediates interaction with GATOR2 through which it regulates TORC1 signaling. {ECO:0000250|UniProtKB:P58004}. TISSUE SPECIFICITY: Highly expressed in heart and also detected in liver and skeletal muscles (at protein level). {ECO:0000269|PubMed:25259925}. +P70277 SIA7B_MOUSE Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 2 (EC 2.4.99.3) (Gal-beta-1,3-GalNAc alpha-2,6-sialyltransferase) (GalNAc alpha-2,6-sialyltransferase II) (ST6GalNAc II) (ST6GalNAcII) (Sialyltransferase 7B) (SIAT7-B) 373 42,482 Binding site (4); Chain (1); Disulfide bond (2); Glycosylation (2); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 7 27 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 28 373 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Catalyzes the transfer of N-acetylneuraminyl groups onto glycan chains in glycoproteins. {ECO:0000269|PubMed:8662927}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Highly expressed in lactating mammary gland and adult testis. Lower levels in kidney. +Q9EPK6 SIL1_MOUSE Nucleotide exchange factor SIL1 465 52,430 Chain (1); Glycosylation (2); Region (1); Sequence conflict (2); Signal peptide (1) FUNCTION: Required for protein translocation and folding in the endoplasmic reticulum (ER). Functions as a nucleotide exchange factor for the ER lumenal chaperone HSPA5 (By similarity). {ECO:0000250}. PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000269|PubMed:16116427}. SUBUNIT: Interacts with HSPA5. {ECO:0000269|PubMed:16116427}. TISSUE SPECIFICITY: Expressed in several areas of the brain including the cerebellum, cerebral cortex, cortical neurons, glial cells of white matter, hippocampus, olfactory bulb, Purkinje cells, inferior olive and the choroids plexus. Also expressed in the eye and skeletal muscle. {ECO:0000269|PubMed:16116427, ECO:0000269|PubMed:16282977, ECO:0000269|PubMed:16282978}. +Q6NTA4 RRAGB_MOUSE Ras-related GTP-binding protein B (Rag B) (RagB) 374 43,191 Chain (1); Cross-link (4); Modified residue (1); Nucleotide binding (3) FUNCTION: Guanine nucleotide-binding protein that plays a crucial role in the cellular response to amino acid availability through regulation of the mTORC1 signaling cascade. Forms heterodimeric Rag complexes with RRAGC or RRAGD and cycles between an inactive GDP-bound and an active GTP-bound form. In its active form participates in the relocalization of mTORC1 to the lysosomes and its subsequent activation by the GTPase RHEB. Involved in the RCC1/Ran-GTPase pathway. {ECO:0000250|UniProtKB:Q5VZM2}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q5VZM2}. Lysosome {ECO:0000250|UniProtKB:Q5VZM2}. SUBUNIT: Interacts with RRAGC and RRAGD; heterodimerization stabilizes RRAG proteins. In complex with RRAGC, but not with RRAGA, interacts with RPTOR; this interaction is particularly efficient with GTP-loaded RRAGB and GDP-loaded RRAGC. Interacts with SH3BP4; the interaction with this negative regulator is most probably direct, preferentially occurs with the inactive GDP-bound form of RRAGB, is negatively regulated by amino acids and prevents interaction with RPTOR. Interacts with the GATOR1 complex; inactivates RRAGB. The Rag heterodimer interacts with SLC38A9; the probable amino acid sensor (By similarity). Interacts with SESN1, SESN2 AND SESN3 (PubMed:25259925). {ECO:0000250|UniProtKB:Q5VZM2, ECO:0000269|PubMed:25259925}. +Q8BKH7 SIN1_MOUSE Target of rapamycin complex 2 subunit MAPKAP1 (TORC2 subunit MAPKAP1) (Mitogen-activated protein kinase 2-associated protein 1) (Stress-activated map kinase-interacting protein 1) (SAPK-interacting protein 1) 522 59,009 Alternative sequence (2); Chain (1); Initiator methionine (1); Modified residue (3); Region (3); Sequence conflict (1) FUNCTION: Subunit of mTORC2, which regulates cell growth and survival in response to hormonal signals. mTORC2 is activated by growth factors, but, in contrast to mTORC1, seems to be nutrient-insensitive. mTORC2 seems to function upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors. mTORC2 promotes the serum-induced formation of stress-fibers or F-actin. mTORC2 plays a critical role in AKT1 'Ser-473' phosphorylation, which may facilitate the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1 which is a prerequisite for full activation. mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422'. mTORC2 also modulates the phosphorylation of PRKCA on 'Ser-657'. Within mTORC2, MAPKAP1 is required for complex formation and mTORC2 kinase activity. MAPKAP1 inhibits MAP3K2 by preventing its dimerization and autophosphorylation. Inhibits HRAS and KRAS signaling. Enhances osmotic stress-induced phosphorylation of ATF2 and ATF2-mediated transcription. Isoform 1 is involved in ciliogenesis, regulates cilia length through its interaction with CCDC28B independently of mTORC2 complex. {ECO:0000269|PubMed:16962653}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: All isoforms except isoform 4 can be incorporated into the mammalian target of rapamycin complex 2 (mTORC2) which contains MTOR, MLST8, PRR5, RICTOR, MAPKAP1 and DEPTOR. Contrary to mTORC1, mTORC2 does not bind to and is not sensitive to FKBP12-rapamycin. Interacts with ATF2, MAP3K2 and MAPK8. Interacts with GTP-bound HRAS and KRAS. Interacts with IFNAR2 and SGK1. Isoform 2 interacts with NBN. Isoform 1 interacts with CCDC28B. {ECO:0000269|PubMed:21757730}. TISSUE SPECIFICITY: Uniquitously expresseed, with highest levels in testis, kidney and liver. Present in renal tubule cells (at protein level). {ECO:0000269|PubMed:17054722}. +Q60520 SIN3A_MOUSE Paired amphipathic helix protein Sin3a (Histone deacetylase complex subunit Sin3a) (Transcriptional corepressor Sin3a) 1274 145,088 Alternative sequence (1); Beta strand (1); Chain (1); Coiled coil (1); Compositional bias (3); Cross-link (3); Domain (3); Erroneous initiation (1); Helix (21); Modified residue (11); Mutagenesis (7); Region (7); Sequence caution (3); Sequence conflict (13); Turn (5) FUNCTION: Acts as a transcriptional repressor. Corepressor for REST. Interacts with MXI1 to repress MYC responsive genes and antagonize MYC oncogenic activities. Also interacts with MXD1-MAX heterodimers to repress transcription by tethering SIN3A to DNA. Acts cooperatively with OGT to repress transcription in parallel with histone deacetylation. Involved in the control of the circadian rhythms. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex through histone deacetylation. Cooperates with FOXK1 to regulate cell cycle progression probably by repressing cell cycle inhibitor genes expression (PubMed:22476904). {ECO:0000269|PubMed:10734093, ECO:0000269|PubMed:21680841, ECO:0000269|PubMed:22476904, ECO:0000269|PubMed:7889570, ECO:0000269|PubMed:8649810}. PTM: SUMO1 sumoylated by TOPORS. Probably desumoylated by SENP2. {ECO:0000250|UniProtKB:Q96ST3}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21454521}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q96ST3}. Note=Recruited to the nucleolus by SAP30L. {ECO:0000250|UniProtKB:Q96ST3, ECO:0000269|PubMed:21454521}. SUBUNIT: Interacts with ARID4B, BRMS1L, HCFC1, HDAC1, HDAC2, MXI1, SAP30L, SAP130, SFPQ and TOPORS. Interacts with OGT (via TPRs 1-6); the interaction mediates transcriptional repression in parallel with histone deacetylase (By similarity). Interacts with BAZ2A, MXD3, MXD4, MBD2, DACH1, NCOR1, NR4A2, REST, RLIM, SAP30, SETDB1, SMYD2, and SUDS3. Interacts with PHF12 in a complex composed of HDAC1, PHF12 and SAP30. Interacts with TET1; the interaction recruits SIN3A to gene promoters. The large PER complex involved in the histone deacetylation is composed of at least HDAC1, PER2, SFPQ and SIN3A. Interacts with KLF11. Interacts with PPHLN1 (By similarity). Found in a complex with YY1, GON4L and HDAC1 (PubMed:21454521). Interacts (via PAH2) with FOXK1 (PubMed:22476904). Found in a complex composed of at least SINHCAF, SIN3A, HDAC1, SAP30, RBBP4, OGT and TET1. Interacts with SINHCAF (PubMed:28554894). {ECO:0000250|UniProtKB:Q96ST3, ECO:0000269|PubMed:10734093, ECO:0000269|PubMed:10950960, ECO:0000269|PubMed:11106735, ECO:0000269|PubMed:11390640, ECO:0000269|PubMed:11882901, ECO:0000269|PubMed:11909966, ECO:0000269|PubMed:12130660, ECO:0000269|PubMed:12198165, ECO:0000269|PubMed:12398767, ECO:0000269|PubMed:15774581, ECO:0000269|PubMed:16805913, ECO:0000269|PubMed:19144721, ECO:0000269|PubMed:21454521, ECO:0000269|PubMed:21490601, ECO:0000269|PubMed:21680841, ECO:0000269|PubMed:22476904, ECO:0000269|PubMed:28554894, ECO:0000269|PubMed:7889570, ECO:0000269|PubMed:8521822, ECO:0000269|PubMed:8649810, ECO:0000269|PubMed:9139820, ECO:0000269|PubMed:9702189}. TISSUE SPECIFICITY: Widely expressed. Highest levels in testis, lung and thymus. +P46062 SIPA1_MOUSE Signal-induced proliferation-associated protein 1 (Sipa-1) (GTPase-activating protein Spa-1) 1037 112,066 Chain (1); Coiled coil (1); Domain (2); Erroneous initiation (1); Frameshift (1); Modified residue (8); Sequence conflict (3) FUNCTION: GTPase activator for the nuclear Ras-related regulatory proteins Rap1, Rsr1 and Ran in vitro, converting them to the putatively inactive GDP-bound state. Affects cell cycle progression. {ECO:0000269|PubMed:7799964}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:7799964}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q96FS4}. Endomembrane system; Peripheral membrane protein {ECO:0000250|UniProtKB:Q96FS4}. Note=Mostly localized in the perinuclear membraneous region. {ECO:0000250|UniProtKB:Q96FS4}. SUBUNIT: Interacts with RRP1B; the interaction leads to inhibition of SIPA1 GTPase activity. {ECO:0000269|PubMed:18081427}. TISSUE SPECIFICITY: Preferentially expressed in both fetal and adult lymphohematopoietic tissues. +Q8R216 SIR4_MOUSE NAD-dependent protein lipoamidase sirtuin-4, mitochondrial (EC 3.5.1.-) (NAD-dependent ADP-ribosyltransferase sirtuin-4) (EC 2.4.2.-) (NAD-dependent protein deacetylase sirtuin-4) (EC 3.5.1.-) (Regulatory protein SIR2 homolog 4) (SIR2-like protein 4) 333 37,525 Active site (1); Binding site (1); Chain (1); Domain (1); Erroneous initiation (1); Metal binding (4); Nucleotide binding (4); Sequence conflict (1); Transit peptide (1) FUNCTION: Acts as NAD-dependent protein lipoamidase, ADP-ribosyl transferase and deacetylase (PubMed:19220062). Catalyzes more efficiently removal of lipoyl- and biotinyl- than acetyl-lysine modifications. Inhibits the pyruvate dehydrogenase complex (PDH) activity via the enzymatic hydrolysis of the lipoamide cofactor from the E2 component, DLAT, in a phosphorylation-independent manner (PubMed:25525879). Catalyzes the transfer of ADP-ribosyl groups onto target proteins, including mitochondrial GLUD1, inhibiting GLUD1 enzyme activity. Acts as a negative regulator of mitochondrial glutamine metabolism by mediating mono ADP-ribosylation of GLUD1: expressed in response to DNA damage and negatively regulates anaplerosis by inhibiting GLUD1, leading to block metabolism of glutamine into tricarboxylic acid cycle and promoting cell cycle arrest (PubMed:16959573). In response to mTORC1 signal, SIRT4 expression is repressed, promoting anaplerosis and cell proliferation (PubMed:23663782). Acts as a tumor suppressor (PubMed:23562301, PubMed:23663782). Also acts as a NAD-dependent protein deacetylase: mediates deacetylation of 'Lys-471' of MLYCD, inhibiting its activity, thereby acting as a regulator of lipid homeostasis (PubMed:23746352). Does not seem to deacetylate PC (PubMed:23438705). Controls fatty acid oxidation by inhibiting PPARA transcriptional activation. Impairs SIRT1:PPARA interaction probably through the regulation of NAD(+) levels (PubMed:24043310, PubMed:20685656). Down-regulates insulin secretion (By similarity). {ECO:0000255|HAMAP-Rule:MF_03161, ECO:0000269|PubMed:19220062, ECO:0000269|PubMed:20685656, ECO:0000269|PubMed:23438705, ECO:0000269|PubMed:23562301, ECO:0000269|PubMed:23663782, ECO:0000269|PubMed:23746352, ECO:0000269|PubMed:24043310, ECO:0000269|PubMed:25525879}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-Rule:MF_03161, ECO:0000269|PubMed:16959573, ECO:0000269|PubMed:23746352}. SUBUNIT: Interacts with IDE and SLC25A5 (By similarity). Interacts with GLUD1 (PubMed:16959573). Interacts with DLAT and PDHX (By similarity). Interacts with MCCC1 (via the biotin carboxylation domain) (PubMed:23438705). Interacts with PCCA and PC (PubMed:23438705). {ECO:0000250|UniProtKB:Q9Y6E7, ECO:0000269|PubMed:16959573, ECO:0000269|PubMed:23438705}. TISSUE SPECIFICITY: Detected in kidney, heart, brain, liver and pancreatic islets (at protein level). {ECO:0000269|PubMed:16959573}. +P59941 SIR6_MOUSE NAD-dependent protein deacetylase sirtuin-6 (EC 3.5.1.-) (Regulatory protein SIR2 homolog 6) (SIR2-like protein 6) 334 36,920 Active site (1); Binding site (1); Chain (1); Domain (1); Initiator methionine (1); Metal binding (4); Modified residue (2); Mutagenesis (2); Nucleotide binding (4) FUNCTION: NAD-dependent protein deacetylase. Has deacetylase activity towards histone H3K9Ac and H3K56Ac. Modulates acetylation of histone H3 in telomeric chromatin during the S-phase of the cell cycle. Deacetylates histone H3K9Ac at NF-kappa-B target promoters and may down-regulate the expression of a subset of NF-kappa-B target genes. Deacetylation of nucleosomes interferes with RELA binding to target DNA. May be required for the association of WRN with telomeres during S-phase and for normal telomere maintenance. On DNA damage, promotes DNA end resection via deacetylation of RBBP8. Has very weak deacetylase activity and can bind NAD(+) in the absence of acetylated substrate (By similarity). Acts as a corepressor of the transcription factor Hif1a to control the expression of multiple glycolytic genes to regulate glucose homeostasis. Required for genomic stability. Required for normal IGF1 serum levels and normal glucose homeostasis. Modulates cellular senescence and apoptosis. Regulates the production of TNF protein. Has a role in the regulation of life span in male mice, but not in female mice. {ECO:0000250, ECO:0000269|PubMed:16439206, ECO:0000269|PubMed:19135889, ECO:0000269|PubMed:19151729, ECO:0000269|PubMed:19220062, ECO:0000269|PubMed:19597350, ECO:0000269|PubMed:20141841, ECO:0000269|PubMed:22367546}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15795229, ECO:0000269|PubMed:16439206}. Note=Predominantly nuclear. Associated with chromatin. SUBUNIT: Interacts with RBBP8; the interaction deacetylates RBBP8 (By similarity). Interacts with RELA. {ECO:0000250, ECO:0000269|PubMed:19135889}. TISSUE SPECIFICITY: Highest levels are found in muscle, thymus, spleen, brain and heart (at protein level). {ECO:0000269|PubMed:15795229, ECO:0000269|PubMed:16439206}. +Q3UFY0 RRP36_MOUSE Ribosomal RNA processing protein 36 homolog 244 28,589 Chain (1); Coiled coil (1); Modified residue (2); Motif (1); Sequence conflict (3) FUNCTION: Involved in the early processing steps of the pre-rRNA in the maturation pathway leading to the 18S rRNA. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. +P63276 RS17_MOUSE 40S ribosomal protein S17 135 15,524 Chain (1); Cross-link (2); Modified residue (3) +Q9JIS3 SMCO4_MOUSE Single-pass membrane and coiled-coil domain-containing protein 4 (Protein FN5) 59 6,694 Chain (1); Coiled coil (1); Sequence conflict (2); Transmembrane (1) TRANSMEM 32 52 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q9D2C9 SNPC3_MOUSE snRNA-activating protein complex subunit 3 (SNAPc subunit 3) (Small nuclear RNA-activating complex polypeptide 3) 407 46,277 Chain (1); Modified residue (1); Sequence conflict (1) FUNCTION: Part of the SNAPc complex required for the transcription of both RNA polymerase II and III small-nuclear RNA genes. Binds to the proximal sequence element (PSE), a non-TATA-box basal promoter element common to these 2 types of genes. Recruits TBP and BRF2 to the U6 snRNA TATA box (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Part of the SNAPc complex composed of 5 subunits: SNAPC1, SNAPC2, SNAPC3, SNAPC4 and SNAPC5. SNAPC3 interacts with SNAPC1 (By similarity). {ECO:0000250}. +Q8BP86 SNPC4_MOUSE snRNA-activating protein complex subunit 4 (SNAPc subunit 4) (snRNA-activating protein complex 190 kDa subunit) (SNAPc 190 kDa subunit) 1333 147,413 Alternative sequence (2); Chain (1); Compositional bias (1); DNA binding (3); Domain (5); Modified residue (5); Region (2); Sequence conflict (1) FUNCTION: Part of the SNAPc complex required for the transcription of both RNA polymerase II and III small-nuclear RNA genes. Binds to the proximal sequence element (PSE), a non-TATA-box basal promoter element common to these 2 types of genes. Recruits TBP and BRF2 to the U6 snRNA TATA box (By similarity). {ECO:0000250|UniProtKB:Q5SXM2}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625}. SUBUNIT: Part of the SNAPc composed of 5 subunits: SNAPC1, SNAPC2, SNAPC3, SNAPC4 and SNAPC5. SNAPC4 interacts with SNAPC1, SNAPC2, SNAPC5, BRF2 and TBP (By similarity). {ECO:0000250}. +Q8R2K7 SNPC5_MOUSE snRNA-activating protein complex subunit 5 (SNAPc subunit 5) (Small nuclear RNA-activating complex polypeptide 5) (snRNA-activating protein complex 19 kDa subunit) (SNAPc 19 kDa subunit) 98 11,340 Chain (1); Compositional bias (1) FUNCTION: Part of the SNAPc complex required for the transcription of both RNA polymerase II and III small-nuclear RNA genes. Binds to the proximal sequence element (PSE), a non-TATA-box basal promoter element common to these 2 types of genes. Recruits TBP and BRF2 to the U6 snRNA TATA box (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Part of the SNAPc complex composed of 5 subunits: SNAPC1, SNAPC2, SNAPC3, SNAPC4 and SNAPC5. SNAPC5 interacts with SNAPC4 (By similarity). {ECO:0000250}. +Q8K194 SNR27_MOUSE U4/U6.U5 small nuclear ribonucleoprotein 27 kDa protein (U4/U6.U5 snRNP 27 kDa protein) (U4/U6.U5-27K) (U4/U6.U5 tri-snRNP-associated protein 3) 155 18,885 Alternative sequence (1); Chain (1); Compositional bias (1); Modified residue (5) FUNCTION: May play a role in mRNA splicing. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Part of a tri-snRNP complex. +Q61234 SNTA1_MOUSE Alpha-1-syntrophin (59 kDa dystrophin-associated protein A1 acidic component 1) (Syntrophin-1) 503 53,665 Beta strand (21); Chain (1); Domain (4); Helix (5); Modified residue (5); Region (1); Sequence conflict (3); Turn (3) FUNCTION: Adapter protein that binds to and probably organizes the subcellular localization of a variety of membrane proteins. May link various receptors to the actin cytoskeleton and the extracellular matrix via the dystrophin glycoprotein complex. Plays an important role in synapse formation and in the organization of UTRN and acetylcholine receptors at the neuromuscular synapse. Binds to phosphatidylinositol 4,5-bisphosphate. PTM: Phosphorylated by CaM-kinase II. Phosphorylation may inhibit the interaction with DMD. {ECO:0000269|PubMed:10525145}. SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000269|PubMed:9214383}; Peripheral membrane protein {ECO:0000269|PubMed:9214383}; Cytoplasmic side {ECO:0000269|PubMed:9214383}. Cell junction {ECO:0000269|PubMed:9214383}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9214383}. Note=In skeletal muscle, it localizes at the cytoplasmic side of the sarcolemmal membrane and at neuromuscular junctions. SUBUNIT: Monomer and homodimer. Interacts with MAPK12, TGFA, GA and F-actin (By similarity). Interacts with the other members of the syntrophin family: SNTB1 and SNTB2; with dystrophin protein DMD and related proteins DTNA and UTRN; SGCG and SGCA of the dystrophin glycoprotein complex; NOS1; GRB2; calmodulin and the sodium channel proteins SCN4A and SCN5A. Interacts with MYOC; regulates muscle hypertrophy. {ECO:0000250, ECO:0000269|PubMed:11551227, ECO:0000269|PubMed:22371502, ECO:0000269|PubMed:7547961, ECO:0000269|PubMed:8625413, ECO:0000269|PubMed:9063877, ECO:0000269|PubMed:9214383, ECO:0000269|PubMed:9412493}. DOMAIN: The PH 1 domain mediates the oligomerization in a calcium dependent manner, and the association with the phosphatidylinositol 4,5-bisphosphate.; DOMAIN: The PDZ domain binds to the last three or four amino acids of ion channels and receptor proteins. The association with dystrophin or related proteins probably leaves the PDZ domain available to recruit proteins to the membrane.; DOMAIN: The SU domain binds calmodulin in a calcium-dependent manner. TISSUE SPECIFICITY: High expression in skeletal muscle. Expressed at intermediate level in heart, kidney and brain, and at low level in intestine, liver, lung and testis. {ECO:0000269|PubMed:9214383}. +Q61235 SNTB2_MOUSE Beta-2-syntrophin (59 kDa dystrophin-associated protein A1 basic component 2) (Syntrophin-3) (SNT3) (Syntrophin-like) (SNTL) 520 56,382 Chain (1); Compositional bias (1); Domain (4); Modified residue (8); Region (1) FUNCTION: Adapter protein that binds to and probably organizes the subcellular localization of a variety of membrane proteins. May link various receptors to the actin cytoskeleton and the dystrophin glycoprotein complex. May play a role in the regulation of secretory granules via its interaction with PTPRN (By similarity). {ECO:0000250}. PTM: Phosphorylated. Partially dephosphorylated upon insulin stimulation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:9214383}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000269|PubMed:9214383}; Peripheral membrane protein {ECO:0000269|PubMed:9214383}. Cell junction {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9214383}. Note=Membrane-associated. In insulinoma cell line, it is enriched in secretory granules (By similarity). In muscle, it is exclusively localized at the neuromuscular junction. {ECO:0000250}. SUBUNIT: Monomer and homodimer (Probable). Interacts with the dystrophin protein DMD and related protein DTNA; and with the other members of the syntrophin family: SNTA1 and SNTB1. Interacts with the neuroregulin receptor ERBB4. Interacts with PTPRN when phosphorylated, protecting PTPRN from protein cleavage by CAPN1. Dephosphorylation upon insulin stimulation disrupts the interaction with PTPRN and results in the cleavage of PTPRN (By similarity). Interacts with the sodium channel proteins SCN4A and SCN5A. Interacts with SAST, MAST205, microtubules and microtubule-associated proteins. Interacts with the dystrophin related protein UTRN. {ECO:0000250, ECO:0000269|PubMed:10404183, ECO:0000269|PubMed:9214383, ECO:0000269|PubMed:9412493, ECO:0000305}. DOMAIN: The PH 1 domain mediates the oligomerization in a calcium dependent manner. {ECO:0000250}.; DOMAIN: The PDZ domain binds to the last three or four amino acids of ion channels and receptor proteins. The association with dystrophin or related proteins probably leaves the PDZ domain available to recruit proteins to the membrane (By similarity). {ECO:0000250}.; DOMAIN: The SU domain binds calmodulin in a calcium-dependent manner. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. Expressed at high levels in the testis. {ECO:0000269|PubMed:9214383}. +Q3TIX9 SNUT2_MOUSE U4/U6.U5 tri-snRNP-associated protein 2 (Inactive ubiquitin-specific peptidase 39) 564 65,146 Chain (1); Compositional bias (1); Cross-link (1); Domain (1); Modified residue (2); Sequence conflict (5); Zinc finger (1) FUNCTION: Plays a role in pre-mRNA splicing as a component of the U4/U6-U5 tri-snRNP, one of the building blocks of the precatalytic spliceosome. Regulates AURKB mRNA levels, and thereby plays a role in cytokinesis and in the spindle checkpoint. Does not have ubiquitin-specific peptidase activity. {ECO:0000250|UniProtKB:Q53GS9}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q53GS9}. SUBUNIT: The U4/U6-U5 tri-snRNP complex is a building block of the precatalytic spliceosome (spliceosome B complex). Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39, plus LSM2, LSM3, LSM4, LSM5, LSM6, LSM7 and LSM8. {ECO:0000250|UniProtKB:Q53GS9}. +Q9DA08 SGF29_MOUSE SAGA-associated factor 29 (Coiled-coil domain-containing protein 101) (SAGA complex-associated factor 29) 293 33,298 Binding site (2); Chain (1); Coiled coil (1); Domain (1); Modified residue (1); Region (3); Sequence conflict (1) FUNCTION: Chromatin reader component of some histone acetyltransferase (HAT) SAGA-type complexes like the TFTC-HAT, ATAC or STAGA complexes. SGF29 specifically recognizes and binds methylated 'Lys-4' of histone H3 (H3K4me), with a preference for trimethylated form (H3K4me3). In the SAGA-type complexes, SGF29 is required to recruit complexes to H3K4me. Involved in the response to endoplasmic reticulum (ER) stress by recruiting the SAGA complex to H3K4me, thereby promoting histone H3 acetylation and cell survival. {ECO:0000250|UniProtKB:Q96ES7}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P0C606}. SUBUNIT: Interacts with dimethylated and trimethylated 'Lys-4' of histone H3 (H3K4me2 and H3K4me3), with a preference for the trimethylated form (H3K4me3). Component of some SAGA-type complexes. Component of the ADA2A-containing complex (ATAC), composed of KAT14, KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1 (By similarity). Interacts with TADA3L, GCN5L2, SUPT3H and MYC (By similarity). {ECO:0000250|UniProtKB:P0C606, ECO:0000250|UniProtKB:Q96ES7}. DOMAIN: The SGF29 C-terminal (also named tudor-like) domain mediates binding to methylated 'Lys-4' of histone H3 (H3K4me). {ECO:0000255|PROSITE-ProRule:PRU00851}. +Q3UH06 RREB1_MOUSE Ras-responsive element-binding protein 1 (RREB-1) (RAS-responsive zinc finger transcription factor RREB) 1700 184,154 Alternative sequence (4); Chain (1); Compositional bias (4); Cross-link (12); Modified residue (19); Sequence conflict (3); Zinc finger (15) FUNCTION: Transcription factor that binds specifically to the RAS-responsive elements (RRE) of gene promoters. May be involved in Ras/Raf-mediated cell differentiation by enhancing calcitonin expression. Represses the angiotensinogen gene. Negatively regulates the transcriptional activity of AR. Potentiates the transcriptional activity of NEUROD1 (By similarity). Binds specifically to the allelic variant of the CDKN2A promoter present in Balb/c mice, which leads to a down-regulation of CDKN2A expression in this strain, and, as a consequence, to an elevated susceptibility to pristane-induced tumors. {ECO:0000250, ECO:0000269|PubMed:12700664}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}. SUBUNIT: Interacts with NEUROD1 and AR. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in splenic B-cells. {ECO:0000269|PubMed:12700664}. +Q99PL5 RRBP1_MOUSE Ribosome-binding protein 1 (Ribosome receptor protein) (RRp) (mRRp) 1605 172,879 Alternative sequence (13); Chain (1); Cross-link (2); Modified residue (8); Region (1); Repeat (61); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 8 28 Helical. {ECO:0000255}. TOPO_DOM 1 7 Lumenal. {ECO:0000255}.; TOPO_DOM 29 1605 Cytoplasmic. {ECO:0000255}. FUNCTION: Acts as a ribosome receptor and mediates interaction between the ribosome and the endoplasmic reticulum membrane. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11167022}. +Q8BHW9 SLNL1_MOUSE Schlafen-like protein 1 410 45,595 Alternative sequence (1); Chain (1); Coiled coil (1); Nucleotide binding (1) +Q9Z0K7 SLUR1_MOUSE Secreted Ly-6/uPAR-related protein 1 (SLURP-1) (ARS component B) 110 12,016 Chain (1); Disulfide bond (5); Domain (1); Signal peptide (1) FUNCTION: Has an antitumor activity. Was found to be a marker of late differentiation of the skin. Implicated in maintaining the physiological and structural integrity of the keratinocyte layers of the skin. In vitro down-regulates keratinocyte proliferation; the function may involve the proposed role as modulator of nicotinic acetylcholine receptors (nAChRs) activity. In vitro inhibits alpha-7-dependent nAChR currents in an allosteric manner (By similarity). In T cells may be involved in regulation of intracellular Ca(2+) signaling (PubMed:17286989). Seems to have a immunomodulatory function in the cornea. The function may implicate a possible role as a scavenger receptor for PLAU thereby blocking PLAU-dependent functions of PLAUR such as in cell migration and proliferation (PubMed:23139280, PubMed:25168896). {ECO:0000250|UniProtKB:P55000, ECO:0000269|PubMed:17286989, ECO:0000269|PubMed:23139280, ECO:0000269|PubMed:25168896}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P55000}. SUBUNIT: Homodimer (By similarity). Interacts with PLAU (PubMed:25168896). Interacts with CHRNA7. {ECO:0000250, ECO:0000250|UniProtKB:P55000, ECO:0000269|PubMed:25168896}. TISSUE SPECIFICITY: Expressed in skin, eye, whole lung, trachea, esophagus and stomach (PubMed:14721776). Widely expressed in various tissues including spleen and thymus but not pancreas. Expressed in macrophages, dendritic cells, T and B cells (PubMed:17286989). Expressed in lung specifically in ciliated bronchial epithelial cells (at protein level). Expression is decreased in lungs of asthmatic model mice(PubMed:19396877, PubMed:20621062). Expressed in the cornea (PubMed:23139280). {ECO:0000269|PubMed:14721776, ECO:0000269|PubMed:17286989, ECO:0000269|PubMed:19396877, ECO:0000269|PubMed:20621062, ECO:0000269|PubMed:23139280}. +P14131 RS16_MOUSE 40S ribosomal protein S16 146 16,445 Chain (1); Modified residue (2); Sequence conflict (2) +Q924W5 SMC6_MOUSE Structural maintenance of chromosomes protein 6 (SMC protein 6) (SMC-6) (mSMC6) 1097 127,198 Alternative sequence (2); Chain (1); Coiled coil (3); Compositional bias (1); Cross-link (2); Erroneous initiation (1); Modified residue (1); Nucleotide binding (1); Region (1); Sequence conflict (5) FUNCTION: Core component of the SMC5-SMC6 complex, a complex involved in repair of DNA double-strand breaks by homologous recombination. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The complex is required for telomere maintenance via recombination and mediates sumoylation of shelterin complex (telosome) components (By similarity). {ECO:0000250}. PTM: Phosphorylated. {ECO:0000250}.; PTM: Sumoylated by NSMCE2/MMS21. {ECO:0000250}.; PTM: Ubiquitinated. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11408570}. Nucleus speckle {ECO:0000250|UniProtKB:Q96SB8}. Chromosome {ECO:0000269|PubMed:11408570}. Nucleus, PML body {ECO:0000250|UniProtKB:Q96SB8}. Chromosome, telomere {ECO:0000250|UniProtKB:Q96SB8}. Note=Localizes to PML nuclear bodies in ALT cell lines. Associates with chromatin. Accumulates with RAD18 and the SLF1-SLF2 complex at replication-coupled DNA interstrand repair and DNA double-strand breaks (DSBs) sites on chromatin in a ubiquitin-dependent manner. Localizes in interchromatin granule clusters (By similarity). Colocalizes with SMC5 on the X-Y chromosome pair within the sex vesicle during late pachytene/diplotene (PubMed:11408570). {ECO:0000250|UniProtKB:Q96SB8, ECO:0000269|PubMed:11408570}. SUBUNIT: Forms a heterodimer with SMC5. Component of the SMC5-SMC6 complex which consists at least of SMC5, SMC6, NSMCE2, NSMCE1, NSMCE4A or EID3 and NSMCE3. Interacts with NSMCE1. Interacts with NSMCE2. Interacts with SLF1. Interacts with SLF2. Interacts with RAD18. {ECO:0000250|UniProtKB:Q96SB8}. DOMAIN: The flexible hinge domain, which separates the large intramolecular coiled coil regions, allows the heterotypic interaction with the corresponding domain of SMC5, forming a V-shaped heterodimer. {ECO:0000250}. +Q6PGB8 SMCA1_MOUSE Probable global transcription activator SNF2L1 (EC 3.6.4.-) (ATP-dependent helicase SMARCA1) (DNA-dependent ATPase SNF2L) (Nucleosome-remodeling factor subunit SNF2L) (SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 1) 1046 121,715 Alternative sequence (1); Chain (1); Coiled coil (1); Cross-link (3); Domain (4); Frameshift (1); Modified residue (3); Motif (1); Nucleotide binding (1); Sequence conflict (4) FUNCTION: Energy-transducing component of the NURF (nucleosome-remodeling factor) and CERF (CECR2-containing-remodeling factor) complexes, which facilitate the perturbation of chromatin structure in an ATP-dependent manner. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00624}. SUBUNIT: Part of the nucleosome-remodeling factor complex (NURF) which consists of SMARCA1; BPTF; RBBP4 and RBBP7. Part of the CECR2-containing-remodeling factor (CERF) complex which contains CECR2 and SMARCA1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Predominantly expressed in cortex, cerebellum, ovaries, testes, uterus and placenta. {ECO:0000269|PubMed:11359880, ECO:0000269|PubMed:14609955}. +Q9WU12 SNURF_MOUSE SNRPN upstream reading frame protein 71 8,407 Chain (1); Sequence conflict (1) SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10318933}. TISSUE SPECIFICITY: Expressed in brain and embryonic stem (ES) cells (at protein level). Expressed in the brain, ovary, testis, liver, heart, kidney and muscle. {ECO:0000269|PubMed:10318933, ECO:0000269|PubMed:16429232}. +Q9CZX8 RS19_MOUSE 40S ribosomal protein S19 145 16,085 Chain (1); Modified residue (5) FUNCTION: Required for pre-rRNA processing and maturation of 40S ribosomal subunits. {ECO:0000250}. SUBUNIT: Interacts with RPS19BP1. {ECO:0000269|PubMed:16289379}. +Q8VEB6 RNZ1_MOUSE Zinc phosphodiesterase ELAC protein 1 (EC 3.1.26.11) (ElaC homolog protein 1) (Ribonuclease Z 1) (RNase Z 1) (tRNA 3 endonuclease 1) (tRNase Z 1) 362 39,740 Active site (1); Alternative sequence (1); Chain (1); Metal binding (8); Sequence conflict (9) FUNCTION: Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Nucleus {ECO:0000250}. Note=Mainly cytosolic. {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +Q9Z2I4 ROBO3_MOUSE Roundabout homolog 3 (Retinoblastoma-inhibiting gene 1 protein) (Rig-1) 1366 146,054 Alternative sequence (2); Chain (1); Compositional bias (1); Disulfide bond (5); Domain (8); Glycosylation (12); Modified residue (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 892 912 Helical. {ECO:0000255}. TOPO_DOM 21 891 Extracellular. {ECO:0000255}.; TOPO_DOM 913 1366 Cytoplasmic. {ECO:0000255}. FUNCTION: Thought to be involved during neural development in axonal navigation at the ventral midline of the neural tube. In spinal chord development plays a role in guiding commissural axons probably by preventing premature sensitivity to Slit proteins thus inhibiting Slit signaling through ROBO1. Required for hindbrain axon midline crossing (By similarity). {ECO:0000250, ECO:0000269|PubMed:15084255}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10049565}; Single-pass type I membrane protein {ECO:0000269|PubMed:10049565}. SUBUNIT: Probably interacts with SLIT2. {ECO:0000269|PubMed:15084255}. TISSUE SPECIFICITY: Detected in embryonal spinal chord and hindbrain. {ECO:0000269|PubMed:10049565, ECO:0000269|PubMed:15084255}. +P59470 RPC2_MOUSE DNA-directed RNA polymerase III subunit RPC2 (RNA polymerase III subunit C2) (EC 2.7.7.6) (C128) (DNA-directed RNA polymerase III 127.6 kDa polypeptide) (DNA-directed RNA polymerase III subunit B) 1133 127,715 Chain (1); Erroneous initiation (1); Metal binding (4); Sequence conflict (1); Zinc finger (1) FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Second largest core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol III is composed of mobile elements and RPC2 is part of the core element with the central large cleft and probably a clamp element that moves to open and close the cleft. Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts induce type I interferon and NF- Kappa-B through the RIG-I pathway (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the RNA polymerase III (Pol III) complex consisting of 17 subunits. {ECO:0000250}. +Q8CGM2 RP1L1_MOUSE Retinitis pigmentosa 1-like 1 protein (Retinitis pigmentosa 1-like protein 1) 1859 199,686 Chain (1); Compositional bias (1); Domain (2); Erroneous initiation (1) FUNCTION: Required for the differentiation of photoreceptor cells. Plays a role in the organization of outer segment of rod and cone photoreceptors. {ECO:0000269|PubMed:19657028}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:19657028}. Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:19657028}. Note=Localized to the axoneme of outer segments and connecting cilia in rod photoreceptors. SUBUNIT: Interacts with RP1; has a synergistic effect with RP1 in photoreceptor differentiation. {ECO:0000269|PubMed:19657028}. TISSUE SPECIFICITY: Retinal-specific; expressed in photoreceptor. +Q9D2C6 RPC8_MOUSE DNA-directed RNA polymerase III subunit RPC8 (DNA-directed RNA polymerase III subunit H) (RNA polymerase III subunit C7) 204 22,948 Chain (1) FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNA. Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts induce type I interferon and NF- Kappa-B through the RIG-I pathway (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the RNA polymerase III (Pol III) complex consisting of 17 subunits. Interacts with RPC9 (By similarity). {ECO:0000250}. +Q791N7 RPA12_MOUSE DNA-directed RNA polymerase I subunit RPA12 (Zinc ribbon domain-containing protein 1) 123 13,650 Chain (1); Zinc finger (2) FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I which synthesizes ribosomal RNA precursors. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:P32529}. SUBUNIT: Component of the RNA polymerase I (Pol I) complex consisting of at least 13 subunits. {ECO:0000250}. +Q7TND5 RPF1_MOUSE Ribosome production factor 1 (Brix domain-containing protein 5) (Ribosome biogenesis protein RPF1) 349 40,037 Chain (1); Domain (1); Erroneous initiation (2); Region (1); Sequence caution (1); Sequence conflict (2) FUNCTION: May be required for ribosome biogenesis. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. +Q8R2S1 RPKL1_MOUSE Ribosomal protein S6 kinase-like 1 (EC 2.7.11.1) 544 60,193 Active site (1); Alternative sequence (4); Binding site (1); Chain (1); Domain (2); Nucleotide binding (1); Sequence conflict (1) +Q9QZS5 SGK2_MOUSE Serine/threonine-protein kinase Sgk2 (EC 2.7.11.1) (Serum/glucocorticoid-regulated kinase 2) 367 41,359 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Domain (2); Modified residue (3); Motif (1); Nucleotide binding (1); Sequence conflict (1) FUNCTION: Serine/threonine-protein kinase which is involved in the regulation of a wide variety of ion channels, membrane transporters, cell growth, survival and proliferation. Up-regulates Na(+) channels: SCNN1A/ENAC, K(+) channels: KCNA3/Kv1.3, KCNE1 and KCNQ1, amino acid transporter: SLC6A19, glutamate transporter: SLC1A6/EAAT4, glutamate receptors: GRIA1/GLUR1 and GRIK2/GLUR6, Na(+)/H(+) exchanger: SLC9A3/NHE3, and the Na(+)/K(+) ATPase. {ECO:0000269|PubMed:15774535, ECO:0000269|PubMed:15774536, ECO:0000269|PubMed:21865597}. PTM: Activated by phosphorylation on Ser-356 by an unknown kinase (may be mTORC2 but not confirmed), transforming it into a substrate for PDPK1 which then phosphorylates it on Thr-193. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. +Q6P5B0 RRP12_MOUSE RRP12-like protein 1295 143,131 Chain (1); Compositional bias (1); Cross-link (1); Modified residue (8); Sequence caution (1); Sequence conflict (4); Transmembrane (1) TRANSMEM 904 924 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. +Q91YK2 RRP1B_MOUSE Ribosomal RNA processing protein 1 homolog B (RRP1-like protein B) 724 80,582 Chain (1); Modified residue (12); Sequence conflict (2) FUNCTION: Positively regulates DNA damage-induced apoptosis by acting as a transcriptional coactivator of proapoptotic target genes of the transcriptional activator E2F1 (By similarity). Likely to play a role in ribosome biogenesis by targeting serine/threonine protein phosphatase PP1 to the nucleolus (By similarity). Involved in regulation of mRNA splicing (PubMed:23604122). Inhibits SIPA1 GTPase activity (PubMed:18081427). Involved in regulating expression of extracellular matrix genes (PubMed:18081427). Associates with chromatin and may play a role in modulating chromatin structure (By similarity). {ECO:0000250|UniProtKB:Q14684, ECO:0000269|PubMed:18081427, ECO:0000269|PubMed:23604122}. PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q14684}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q14684}. Chromosome {ECO:0000250|UniProtKB:Q14684}. Note=Predominantly located in the nucleolus with a small amount found in the nucleoplasm. Associates with the perichromatin region during metaphase and with cytoplasmic foci during telophase before reaccumulation in the nucleolus during G2. Associates with heterochromatin and euchromatin. {ECO:0000250|UniProtKB:Q14684}. SUBUNIT: Interacts with the transcriptional activator E2F1 (By similarity). Interacts with serine/threonine-protein phosphatase PP1 subunits PPP1CB and PPP1CC but not with PPP1CA (By similarity). Interacts with 60S ribosomal proteins RPL5 and RPL27, ribosomal processing protein RRP1/NNP1 and other nucleolar proteins including NOP2/NOL1 and FBL (By similarity). Also interacts with nucleolar protein NPM1/B23 (By similarity). Interacts with splicing factor SRSF1 and LUC7L3/CROP (By similarity). Interacts with GTPase activator SIPA1 (PubMed:18081427). Interacts with H1FX, NCL, PARP1, TRIM28 and YBX3 (By similarity). {ECO:0000250|UniProtKB:Q14684, ECO:0000269|PubMed:18081427}. +Q62231 SIX1_MOUSE Homeobox protein SIX1 (Sine oculis homeobox homolog 1) 284 32,210 Chain (1); DNA binding (1); Sequence conflict (1) FUNCTION: Transcription factor that is involved in the regulation of cell proliferation, apoptosis and embryonic development. Plays an important role in the development of several organs, including kidney, muscle and inner ear. Depending on context, functions as transcriptional repressor or activator. Lacks an activation domain, and requires interaction with EYA family members for transcription activation. Mediates nuclear translocation of EYA1 and EYA2. Binds the 5'-TCA[AG][AG]TTNC-3' motif present in the MEF3 element in the MYOG promoter. Regulates the expression of numerous genes, including MYC, CCNA1, CCND1 and EZR. Acts as activator of the IGFBP5 promoter, probably coactivated by EYA2. Repression of precursor cell proliferation in myoblasts is switched to activation through recruitment of EYA3 to the SIX1-DACH1 complex. During myogenesis, seems to act together with EYA2 and DACH2. {ECO:0000269|PubMed:11978764, ECO:0000269|PubMed:12215533, ECO:0000269|PubMed:12668636, ECO:0000269|PubMed:12783782, ECO:0000269|PubMed:12834866, ECO:0000269|PubMed:14628042, ECO:0000269|PubMed:14695375, ECO:0000269|PubMed:16488997}. PTM: Phosphorylated during interphase; becomes hyperphosphorylated during mitosis. Hyperphosphorylation impairs binding to promoter elements (By similarity). {ECO:0000250}.; PTM: Ubiquitinated by the anaphase promoting complex (APC), leading to its proteasomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15475}. Cytoplasm {ECO:0000250|UniProtKB:Q15475}. SUBUNIT: Interacts with EYA1. Interacts with CDC20 (By similarity). Interacts with DACH1, EYA2 and EYA3. Interacts with TBX18 (By similarity). {ECO:0000250|UniProtKB:Q15475, ECO:0000269|PubMed:11978764, ECO:0000269|PubMed:12215533, ECO:0000269|PubMed:14628042}. TISSUE SPECIFICITY: Expressed in phalangeal tendons and in skeletal muscle and in head and body mesenchyme. +Q05A13 S16C6_MOUSE Short-chain dehydrogenase/reductase family 16C member 6 (EC 1.1.1.-) 316 35,158 Active site (1); Binding site (1); Chain (1); Nucleotide binding (1) +Q8BN82 S17A5_MOUSE Sialin (H(+)/nitrate cotransporter) (H(+)/sialic acid cotransporter) (AST) (Solute carrier family 17 member 5) (Vesicular H(+)/Aspartate-glutamate cotransporter) 495 54,369 Alternative sequence (3); Chain (1); Glycosylation (3); Motif (1); Topological domain (13); Transmembrane (12) TRANSMEM 42 62 Helical. {ECO:0000255}.; TRANSMEM 110 130 Helical. {ECO:0000255}.; TRANSMEM 137 157 Helical. {ECO:0000255}.; TRANSMEM 159 179 Helical. {ECO:0000255}.; TRANSMEM 201 221 Helical. {ECO:0000255}.; TRANSMEM 228 248 Helical. {ECO:0000255}.; TRANSMEM 279 299 Helical. {ECO:0000255}.; TRANSMEM 329 349 Helical. {ECO:0000255}.; TRANSMEM 366 386 Helical. {ECO:0000255}.; TRANSMEM 392 412 Helical. {ECO:0000255}.; TRANSMEM 424 444 Helical. {ECO:0000255}.; TRANSMEM 458 478 Helical. {ECO:0000255}. TOPO_DOM 1 41 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 63 109 Lumenal. {ECO:0000255}.; TOPO_DOM 131 136 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 158 158 Lumenal. {ECO:0000255}.; TOPO_DOM 180 200 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 222 227 Lumenal. {ECO:0000255}.; TOPO_DOM 249 278 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 300 328 Lumenal. {ECO:0000255}.; TOPO_DOM 350 365 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 387 391 Lumenal. {ECO:0000255}.; TOPO_DOM 413 423 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 445 457 Lumenal. {ECO:0000255}.; TOPO_DOM 479 495 Cytoplasmic. {ECO:0000255}. FUNCTION: Transports glucuronic acid and free sialic acid out of the lysosome after it is cleaved from sialoglycoconjugates undergoing degradation, this is required for normal CNS myelination. Mediates aspartate and glutamate membrane potential-dependent uptake into synaptic vesicles and synaptic-like microvesicles. Also functions as an electrogenic 2NO(3)(-)/H(+) cotransporter in the plasma membrane of salivary gland acinar cells, mediating the physiological nitrate efflux, 25% of the circulating nitrate ions is typically removed and secreted in saliva (By similarity). {ECO:0000250, ECO:0000269|PubMed:20007460}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9NRA2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9NRA2}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q9NRA2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9NRA2}. Lysosome membrane {ECO:0000250|UniProtKB:Q9NRA2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9NRA2}. +Q9D174 S18L2_MOUSE SS18-like protein 2 77 8,873 Chain (1); Motif (1) +Q9CQ06 RM24_MOUSE 39S ribosomal protein L24, mitochondrial (L24mt) (MRP-L24) 216 24,945 Chain (1); Domain (1); Modified residue (1); Sequence conflict (10); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q96A35}. SUBUNIT: Component of the mitochondrial ribosome large subunit (39S) which comprises a 16S rRNA and about 50 distinct proteins. {ECO:0000250|UniProtKB:Q96A35}. +Q9DB15 RM12_MOUSE 39S ribosomal protein L12, mitochondrial (L12mt) (MRP-L12) 201 21,708 Chain (1); Modified residue (4); Sequence conflict (1); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion. SUBUNIT: Interacts with NOA1. {ECO:0000250}. +Q8BSE0 RMD2_MOUSE Regulator of microtubule dynamics protein 2 (RMD-2) (mRMD-2) (Protein FAM82A1) 410 47,016 Chain (1); Coiled coil (1); Erroneous initiation (1); Modified residue (6); Sequence conflict (2); Transmembrane (1) TRANSMEM 9 28 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Cytoplasm. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. Note=In interphase localizes in the cytoplasm, and during mitosis localizes to the spindle microtubules and spindle poles. Also detected as large dots in the perinuclear region (By similarity). {ECO:0000250}. SUBUNIT: Interacts with microtubules. {ECO:0000250}. +Q3UV31 RN223_MOUSE RING finger protein 223 285 30,532 Chain (1); Sequence conflict (1); Transmembrane (1); Zinc finger (1) TRANSMEM 230 250 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q3UPR9 SBSPO_MOUSE Somatomedin-B and thrombospondin type-1 domain-containing protein (RPE-spondin) 264 29,464 Chain (1); Disulfide bond (7); Domain (2); Glycosylation (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. +Q9QYK7 RNF11_MOUSE RING finger protein 11 (NEDD4 WW domain-binding protein 2) (Sid 1669) 154 17,458 Chain (1); Erroneous initiation (1); Initiator methionine (1); Lipidation (2); Modified residue (3); Motif (1); Mutagenesis (1); Zinc finger (1) FUNCTION: Essential component of a ubiquitin-editing protein complex, comprising also TNFAIP3, ITCH and TAX1BP1, that ensures the transient nature of inflammatory signaling pathways. Promotes the association of TNFAIP3 to RIPK1 after TNF stimulation. TNFAIP3 deubiquitinates 'Lys-63' polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-48'-polyubiquitin chains. This leads to RIPK1 proteasomal degradation and consequently termination of the TNF- or LPS-mediated activation of NF-kappa-B. Recruits STAMBP to the E3 ubiquitin-ligase SMURF2 for ubiquitination, leading to its degradation by the 26S proteasome. PTM: Ubiquitinated in the presence of ITCH, SMURF2 and UBE2D1, as well as WWP1. {ECO:0000250}.; PTM: Phosphorylation by PKB/AKT1 may accelerate degradation by the proteasome. {ECO:0000250}.; PTM: Acylation at both Gly-2 and Cys-4 is required for proper localization to the endosomes. {ECO:0000250}. SUBCELLULAR LOCATION: Early endosome {ECO:0000250}. Recycling endosome {ECO:0000250}. Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Predominantly cytoplasmic, when unphosphorylated, and nuclear, when phosphorylated by PKB/AKT1. {ECO:0000250}. SUBUNIT: Interacts (when phosphorylated) with 14-3-3. Interacts with the E3 ubiquitin-ligases NEDD4, ITCH, SMURF2 and WWP1 (By similarity). Also interacts with the E2 ubiquitin-conjugating enzymes UBE2D1 and UBE2N, but neither with CDC34, nor with UBE2L3. Interacts with ZNF350, EPS15 and STAMBP (By similarity). After TNF stimulation, interacts with TAX1BP1, TNFAIP3 and RIPK1; these interaction are transient and they are lost after 1 hour of stimulation with TNF. Interacts with GGA1 (By similarity). {ECO:0000250}. DOMAIN: The PPxY motif mediates interaction with NEDD4. {ECO:0000269|PubMed:11042109}. +O54965 RNF13_MOUSE E3 ubiquitin-protein ligase RNF13 (EC 2.3.2.27) (RING finger protein 13) (RING-type E3 ubiquitin transferase RNF13) 381 42,732 Alternative sequence (2); Chain (1); Domain (1); Glycosylation (1); Mutagenesis (1); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1); Zinc finger (1) TRANSMEM 183 203 Helical. {ECO:0000255}. TOPO_DOM 35 182 Lumenal. {ECO:0000255}.; TOPO_DOM 204 381 Cytoplasmic. {ECO:0000255}. Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that may play a role in controlling cell proliferation. {ECO:0000269|PubMed:19292867}. PTM: Auto-ubiquitinated. {ECO:0000269|PubMed:19292867}.; PTM: N-glycosylated and also modified with chondroitin sulfate. {ECO:0000269|PubMed:19292867}. SUBCELLULAR LOCATION: Late endosome membrane; Single-pass membrane protein. Lysosome membrane. Cytoplasm, cytosol. Nucleus inner membrane. Note=The mature protein is subjected to extensive proteolysis that leads to the shedding of the ectodomain into the lumen of vesicles and the release of the C-terminal fragment into the cytosol. Not detected in early endosomes. Treatment of the cells with either PMA or ionomycin stabilizes the full-length protein which relocalizes to recycling endosomes and to the inner nuclear membrane. DOMAIN: The RING-type zinc finger domain is required for E3 ligase activity. TISSUE SPECIFICITY: Expressed in the brain, heart, kidney, liver and spleen. Higher expression in adult tissues compared to the embryonic counterparts. {ECO:0000269|PubMed:19292867}. +Q3UF64 RNFT2_MOUSE RING finger and transmembrane domain-containing protein 2 (Transmembrane protein 118) 445 48,856 Alternative sequence (1); Chain (1); Compositional bias (1); Erroneous initiation (2); Frameshift (1); Sequence conflict (1); Topological domain (5); Transmembrane (4); Zinc finger (1) TRANSMEM 184 203 Helical. {ECO:0000255}.; TRANSMEM 216 236 Helical. {ECO:0000255}.; TRANSMEM 257 277 Helical. {ECO:0000255}.; TRANSMEM 331 351 Helical. {ECO:0000255}. TOPO_DOM 1 183 Extracellular. {ECO:0000255}.; TOPO_DOM 204 215 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 237 256 Extracellular. {ECO:0000255}.; TOPO_DOM 278 330 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 352 445 Extracellular. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8C310 ROBO4_MOUSE Roundabout homolog 4 1012 108,499 Alternative sequence (2); Chain (1); Disulfide bond (2); Domain (4); Erroneous initiation (5); Frameshift (1); Glycosylation (9); Modified residue (2); Signal peptide (1) FUNCTION: Receptor for Slit proteins, at least for SLIT2, and seems to be involved in angiogenesis and vascular patterning. May mediate the inhibition of primary endothelial cell migration by Slit proteins. {ECO:0000269|PubMed:12941633}. SUBUNIT: Interacts with SLIT2 and ENAH. {ECO:0000269|PubMed:12941633}. TISSUE SPECIFICITY: Expressed specifically in embryo and adult vascular endothelium. {ECO:0000269|PubMed:12941633}. +Q9CX86 ROA0_MOUSE Heterogeneous nuclear ribonucleoprotein A0 (hnRNP A0) 305 30,530 Chain (1); Compositional bias (1); Cross-link (9); Domain (2); Modified residue (9) FUNCTION: mRNA-binding component of ribonucleosomes. Specifically binds AU-rich element (ARE)-containing mRNAs. Involved in post-transcriptional regulation of cytokines mRNAs. {ECO:0000269|PubMed:12456657}. PTM: Phosphorylated at Ser-84 by MAPKAPK2 in response to LPS treatment, promoting stabilization of GADD45A mRNA. {ECO:0000269|PubMed:12456657}.; PTM: Arg-293 is dimethylated, probably to asymmetric dimethylarginine. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Component of ribonucleosomes. {ECO:0000250}. +Q3TDK6 ROGDI_MOUSE Protein rogdi homolog (Leucine-zipper-containing LZF) 287 32,100 Alternative sequence (2); Chain (1); Frameshift (1); Initiator methionine (1); Modified residue (1); Sequence conflict (3) SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000250|UniProtKB:Q9GZN7}. Cell junction, synapse, presynaptic cell membrane {ECO:0000250|UniProtKB:Q4V7D2}. Cell projection, axon {ECO:0000250|UniProtKB:Q4V7D2}. Perikaryon {ECO:0000250|UniProtKB:Q4V7D2}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q4V7D2}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250|UniProtKB:Q4V7D2}. Note=Detected primarily at presynaptic sites on axons, and to a lesser degree in soma and dendrites. Not detected at post-synaptic sites. {ECO:0000250|UniProtKB:Q4V7D2}. SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9GZN7}. TISSUE SPECIFICITY: Detected in brain, kidney and testis. {ECO:0000269|PubMed:11740862}. +O08848 RO60_MOUSE 60 kDa SS-A/Ro ribonucleoprotein (60 kDa Ro protein) (60 kDa ribonucleoprotein Ro) (RoRNP) (TROVE domain family member 2) 538 60,124 Chain (1); Domain (1); Metal binding (3); Modified residue (4); Region (2); Sequence conflict (3) FUNCTION: RNA-binding protein that binds to misfolded non-coding RNAs, pre-5S rRNA, and several small cytoplasmic RNA molecules known as Y RNAs. May stabilize some of these RNAs and protect them from degradation. {ECO:0000269|PubMed:21289087}.; FUNCTION: May play roles in cilia formation and/or maintenance. {ECO:0000269|PubMed:21289087}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. {ECO:0000250}. SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Found in a complex with PUF60 and Y5 RNA. Interacts with RIP11 (By similarity). {ECO:0000250}. DOMAIN: The horseshoe-shaped TROVE domain is built with 7 helical HEAT-like repeats, and is closed by the VWFA-like domain giving rise to a ring-shaped monomer. Single-stranded RNA is bound in the positively charged central cavity (By similarity). {ECO:0000250|UniProtKB:P42700}.; DOMAIN: The MIDAS-like motif in the VWFA-like domain binds divalent metal cations. {ECO:0000250|UniProtKB:P42700}. TISSUE SPECIFICITY: Highest in brain, followed by lung, muscle, kidney and heart. Lower levels are found in testis, liver and spleen. +P70335 ROCK1_MOUSE Rho-associated protein kinase 1 (EC 2.7.11.1) (Rho-associated, coiled-coil-containing protein kinase 1) (Rho-associated, coiled-coil-containing protein kinase I) (ROCK-I) (p160 ROCK-1) (p160ROCK) 1354 158,171 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Coiled coil (2); Compositional bias (1); Domain (5); Erroneous initiation (1); Initiator methionine (1); Modified residue (4); Nucleotide binding (1); Region (3); Sequence caution (1); Site (1); Zinc finger (1) FUNCTION: Protein kinase which is a key regulator of actin cytoskeleton and cell polarity. Involved in regulation of smooth muscle contraction, actin cytoskeleton organization, stress fiber and focal adhesion formation, neurite retraction, cell adhesion and motility via phosphorylation of DAPK3, GFAP, LIMK1, LIMK2, MYL9/MLC2, PFN1 and PPP1R12A. Phosphorylates FHOD1 and acts synergistically with it to promote SRC-dependent non-apoptotic plasma membrane blebbing. Required for centrosome positioning and centrosome-dependent exit from mitosis. Plays a role in terminal erythroid differentiation. Promotes keratinocyte terminal differentiation (By similarity). Phosphorylates JIP3 and regulates the recruitment of JNK to JIP3 upon UVB-induced stress. Acts as a suppressor of inflammatory cell migration by regulating PTEN phosphorylation and stability. Acts as a negative regulator of VEGF-induced angiogenic endothelial cell activation. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization. May regulate closure of the eyelids and ventral body wall by inducing the assembly of actomyosin bundles. {ECO:0000250, ECO:0000269|PubMed:15753128, ECO:0000269|PubMed:19036714, ECO:0000269|PubMed:19181962, ECO:0000269|PubMed:20008297, ECO:0000269|PubMed:21768292}. PTM: Autophosphorylated on serine and threonine residues.; PTM: Cleaved by caspase-3 during apoptosis. This leads to constitutive activation of the kinase and membrane blebbing (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16741948}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:16741948}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell projection, bleb {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16741948}. Cell membrane {ECO:0000269|PubMed:16741948}. Cell projection, lamellipodium {ECO:0000269|PubMed:16741948}. Cell projection, ruffle {ECO:0000269|PubMed:16741948}. Note=Associated with the mother centriole and an intercentriolar linker. A small proportion is associated with Golgi membranes (By similarity). Colocalizes with ITGB1BP1 and ITGB1 at the cell membrane predominantly in lamellipodia and membrane ruffles, but also in retraction fibers. Localizes at the cell membrane in an ITGB1BP1-dependent manner. {ECO:0000250}. SUBUNIT: Homodimer (By similarity). Interacts with RHOA (activated by GTP), RHOB, RHOC, GEM, MYLC2B, RHOE, PPP1R12A, LIMK1, LIMK2, TSG101, CHORDC1, DAPK3, PFN1 and JIP3 (By similarity). Interacts with FHOD1 in a Src-dependent manner (By similarity). Interacts with PTEN. Interacts with ITGB1BP1 (via N-terminus and PTB domain). {ECO:0000250, ECO:0000269|PubMed:16741948, ECO:0000269|PubMed:17654484, ECO:0000269|PubMed:20008297}. DOMAIN: The C-terminal auto-inhibitory domain interferes with kinase activity. RHOA binding leads to a conformation change and activation of the kinase. Truncated ROCK1 is constitutively activated. TISSUE SPECIFICITY: Highly expressed in brain, heart, lung, liver, stomach, spleen, kidney, testis, muscle, embryo and placenta. {ECO:0000269|PubMed:8772201}. +Q62190 RON_MOUSE Macrophage-stimulating protein receptor (MSP receptor) (EC 2.7.10.1) (Stem cell-derived tyrosine kinase) (p185-Ron) (CD antigen CD136) [Cleaved into: Macrophage-stimulating protein receptor alpha chain; Macrophage-stimulating protein receptor beta chain] 1378 150,519 Active site (1); Binding site (2); Chain (3); Compositional bias (1); Disulfide bond (11); Domain (5); Glycosylation (8); Modified residue (4); Nucleotide binding (2); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 961 981 Helical. {ECO:0000255}. TOPO_DOM 25 960 Extracellular. {ECO:0000255}.; TOPO_DOM 982 1378 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to MST1 ligand. Regulates many physiological processes including cell survival, migration and differentiation. Ligand binding at the cell surface induces autophosphorylation of RON on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with the PI3-kinase subunit PIK3R1, PLCG1 or the adapter GAB1. Recruitment of these downstream effectors by RON leads to the activation of several signaling cascades including the RAS-ERK, PI3 kinase-AKT, or PLCgamma-PKC. RON signaling activates the wound healing response by promoting epithelial cell migration, proliferation as well as survival at the wound site. Plays also a role in the innate immune response by regulating the migration and phagocytic activity of macrophages. Alternatively, RON can also promote signals such as cell migration and proliferation in response to growth factors other than MST1 ligand. PTM: Proteolytic processing yields the two subunits. {ECO:0000250}.; PTM: Autophosphorylated in response to ligand binding on Tyr-1215 and Tyr-1216 in the kinase domain leading to further phosphorylation of Tyr-1330 and Tyr-1337 in the C-terminal multifunctional docking site. {ECO:0000250}.; PTM: Ubiquitinated. Ubiquitination by CBL regulates the receptor stability and activity through proteasomal degradation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Heterodimer of an alpha chain and a beta chain which are disulfide linked. Binds PLXNB1. Associates with and is negatively regulated by HYAL2. Interacts when phosphorylated with downstream effectors including PIK3R1, PCLG1, GRB2 and GAB1. Interacts with integrin beta1/ITGB1 in a ligand-independent fashion. Isoform sf-Stk forms covalent heterodimers with friend spleen focus-forming virus (FSFFV) gp55. {ECO:0000269|PubMed:11483734}. TISSUE SPECIFICITY: Expressed in liver, skin, lung, brain, testis and kidney. {ECO:0000269|PubMed:8545120}. +P60898 RPB9_MOUSE DNA-directed RNA polymerase II subunit RPB9 (RNA polymerase II subunit B9) (DNA-directed RNA polymerase II subunit I) (RNA polymerase II 14.5 kDa subunit) (RPB14.5) 125 14,523 Chain (1); Metal binding (8); Modified residue (1); Zinc finger (2) FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB9 is part of the upper jaw surrounding the central large cleft and thought to grab the incoming DNA template (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:P32529}. SUBUNIT: Component of the RNA polymerase II (Pol II) complex consisting of 12 subunits. {ECO:0000250}. +O55242 SGMR1_MOUSE Sigma non-opioid intracellular receptor 1 (Sigma 1-type opioid receptor) (Sigma1-receptor) (Sigma1R) 223 25,250 Alternative sequence (1); Chain (1); Region (3); Sequence conflict (1); Site (2); Topological domain (2); Transmembrane (1) TRANSMEM 10 30 Helical. {ECO:0000250|UniProtKB:Q99720}. TOPO_DOM 1 9 Lumenal. {ECO:0000250|UniProtKB:Q99720}.; TOPO_DOM 31 223 Cytoplasmic. {ECO:0000250|UniProtKB:Q99720}. FUNCTION: Functions in lipid transport from the endoplasmic reticulum and is involved in a wide array of cellular functions probably through regulation of the biogenesis of lipid microdomains at the plasma membrane (PubMed:12730355). Involved in the regulation of different receptors it plays a role in BDNF signaling and EGF signaling. Also regulates ion channels like the potassium channel and could modulate neurotransmitter release. Plays a role in calcium signaling through modulation together with ANK2 of the ITP3R-dependent calcium efflux at the endoplasmic reticulum. Plays a role in several other cell functions including proliferation, survival and death. Originally identified for its ability to bind various psychoactive drugs it is involved in learning processes, memory and mood alteration (PubMed:11149946, PubMed:14622179, PubMed:15571673, PubMed:15777781, PubMed:23332758, PubMed:9425306, PubMed:9603192). Necessary for proper mitochondrial axonal transport in motor neurons, in particular the retrograde movement of mitochondria (PubMed:25678561). Plays a role in protecting cells against oxidative stress-induced cell death via its interaction with RNF112 (PubMed:26792191). {ECO:0000269|PubMed:11149946, ECO:0000269|PubMed:12730355, ECO:0000269|PubMed:14622179, ECO:0000269|PubMed:15571673, ECO:0000269|PubMed:15777781, ECO:0000269|PubMed:23332758, ECO:0000269|PubMed:25678561, ECO:0000269|PubMed:26792191, ECO:0000269|PubMed:9425306, ECO:0000269|PubMed:9603192}. SUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000250|UniProtKB:Q99720}. Nucleus outer membrane {ECO:0000250|UniProtKB:Q99720}. Nucleus envelope {ECO:0000269|PubMed:12730355}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q99720}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:12730355}. Membrane {ECO:0000250|UniProtKB:Q99720}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q99720}. Lipid droplet {ECO:0000269|PubMed:12730355}. Cell junction {ECO:0000250|UniProtKB:Q99720}. Cell membrane {ECO:0000250|UniProtKB:Q99720}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q99720}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000269|PubMed:20167253}. Note=During interphase, detected at the inner and outer nuclear membrane and the endoplasmic reticulum. Detected on cytoplasmic vesicles during mitosis (By similarity). Targeted to lipid droplets, cholesterol and galactosylceramide-enriched domains of the endoplasmic reticulum (PubMed:12730355). Enriched at cell-cell communication regions, growth cone and postsynaptic structures. Localization is modulated by ligand-binding. In motor neurons it is enriched at cholinergic postsynaptic densities (PubMed:20167253). {ECO:0000250|UniProtKB:Q99720, ECO:0000269|PubMed:12730355, ECO:0000269|PubMed:20167253}. SUBUNIT: Homotrimer (By similarity). Interacts with KCNA4 (By similarity). Interacts with KCNA2; cocaine consumption leads to increased interaction (PubMed:23332758). Forms a ternary complex with ANK2 and ITPR3. The complex is disrupted by agonists (PubMed:11149946). Interacts with RNF112 in an oxidative stress-regulated manner (PubMed:26792191). {ECO:0000250|UniProtKB:Q99720, ECO:0000250|UniProtKB:Q9R0C9, ECO:0000269|PubMed:11149946, ECO:0000269|PubMed:23332758, ECO:0000269|PubMed:26792191}. DOMAIN: The C-terminal helices form a flat, hydrophobic surface that is probably tightly associated with the cytosolic surface of the endoplasmic reticulum membrane. {ECO:0000250|UniProtKB:Q99720}. TISSUE SPECIFICITY: Widely expressed with higher expression in liver, brain, kidney and thymus. Expressed throughout the brain with higher expression within cerebral cortex, hippocampus and cerebellum. Within the hippocampus expressed in cornu ammonis pyramidal neurons, the granular cells of the dentate gyrus as well as interneurons. Within the cerebellum, expressed in Purkinje cell bodies (PubMed:11207432, PubMed:11476895, PubMed:11687279, PubMed:9603192). Highly expressed in the brainstem and motor neurons of the spinal cord (PubMed:20167253). Expressed by neural retina, retinal pigment epithelial cells and lens (PubMed:11207432, PubMed:11476895, PubMed:11687279, PubMed:9603192). {ECO:0000269|PubMed:11207432, ECO:0000269|PubMed:11476895, ECO:0000269|PubMed:11687279, ECO:0000269|PubMed:20167253, ECO:0000269|PubMed:9603192}. +Q99N95 RM03_MOUSE 39S ribosomal protein L3, mitochondrial (L3mt) (MRP-L3) 348 39,110 Chain (1); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P09001}. SUBUNIT: Component of the mitochondrial ribosome large subunit (39S) which comprises a 16S rRNA and about 50 distinct proteins. {ECO:0000250|UniProtKB:P09001}. +Q9QZR0 RNF25_MOUSE E3 ubiquitin-protein ligase RNF25 (EC 2.3.2.27) (RING finger protein 25) (RING finger protein AO7) (RING-type E3 ubiquitin transferase RNF25) 456 51,227 Chain (1); Domain (1); Mutagenesis (6); Sequence conflict (3); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of NKD2. Stimulates transcription mediated by NF-kappa-B (By similarity). {ECO:0000250, ECO:0000269|PubMed:10500182, ECO:0000269|PubMed:18757723}. PTM: Ubiquitinated. {ECO:0000250}. SUBUNIT: Interacts with UBE2D2, and may also interact with UBE2E1 and UBE2E3. Interacts with RELA (By similarity). Interacts with NKD2. {ECO:0000250, ECO:0000269|PubMed:10500182, ECO:0000269|PubMed:18757723}. DOMAIN: The RING-type zinc finger domain interacts with an ubiquitin-conjugating enzyme (E2) and facilitates ubiquitination. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10500182}. +O35445 RNF5_MOUSE E3 ubiquitin-protein ligase RNF5 (EC 2.3.2.27) (RING finger protein 5) (RING-type E3 ubiquitin transferase RNF5) 180 19,837 Chain (1); Initiator methionine (1); Modified residue (4); Transmembrane (2); Zinc finger (1) TRANSMEM 118 138 Helical. {ECO:0000255}.; TRANSMEM 160 180 Helical. {ECO:0000255}. Protein modification; protein ubiquitination. FUNCTION: Has E2-dependent E3 ubiquitin-protein ligase activity. May function together with E2 ubiquitin-conjugating enzymes UBE2D1/UBCH5A and UBE2D2/UBC4. Mediates ubiquitination of PXN/paxillin. May be involved in regulation of cell motility and localization of PXN/paxillin. Mediates the 'Lys-63'-linked polyubiquitination of JKAMP thereby regulating JKAMP function by decreasing its association with components of the proteasome and ERAD; the ubiquitination appears to involve E2 ubiquitin-conjugating enzyme UBE2N. Mediates the 'Lys-48'-linked polyubiquitination of TMEM173 at 'Lys-150 'leading to its proteasomal degradation; the ubiquitination occurs in mitochondria after viral transfection and regulates antiviral responses. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12861019}; Multi-pass membrane protein {ECO:0000269|PubMed:12861019}. Mitochondrion membrane {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}. Note=Predominantly located in the plasma membrane, with some localization occurring within cytoplasmic organelles. SUBUNIT: Interacts with PXN (By similarity). Interacts with JKAMP. Interacts with TMEM173; the interaction of endogenous proteins is dependent on viral infection (By similarity). {ECO:0000250}. +Q9DBU5 RNF6_MOUSE E3 ubiquitin-protein ligase RNF6 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase RNF6) (RLIM-like protein) 667 74,091 Chain (1); Compositional bias (1); Modified residue (1); Region (1); Sequence conflict (7); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase mediating 'Lys-48'-linked polyubiquitination of LIMK1 and its subsequent targeting to the proteasome for degradation. Negatively regulates axonal outgrowth through regulation of the LIMK1 turnover. Mediates 'Lys-6' and 'Lys-27'-linked polyubiquitination of AR/androgen receptor thereby modulating its transcriptional activity. May also bind DNA and function as a transcriptional regulator. {ECO:0000269|PubMed:11971979, ECO:0000269|PubMed:16204183}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cell projection, axon. Nucleus, PML body. Note=Localizes to the PML nuclear bodies in Sertoli cells. SUBUNIT: Interacts with AR (By similarity). Interacts with LIMK1. {ECO:0000250, ECO:0000269|PubMed:16204183}. TISSUE SPECIFICITY: Widely expressed with higher expression in the testis in both germ cells and Sertoli cells. {ECO:0000269|PubMed:11971979}. +Q9CWY8 RNH2A_MOUSE Ribonuclease H2 subunit A (RNase H2 subunit A) (EC 3.1.26.4) (Ribonuclease HI large subunit) (RNase HI large subunit) (Ribonuclease HI subunit A) 301 33,513 Beta strand (11); Chain (1); Helix (13); Metal binding (3); Modified residue (3); Mutagenesis (5); Sequence conflict (1); Turn (3) FUNCTION: Catalytic subunit of RNase HII, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging-strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA:RNA duplexes. {ECO:0000269|PubMed:19923215}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: The RNase H2 complex is a heterotrimer composed of the catalytic subunit RNASEH2A and the non-catalytic subunits RNASEH2B and RNASEH2C. {ECO:0000269|PubMed:19923215}. +Q9CQ18 RNH2C_MOUSE Ribonuclease H2 subunit C (RNase H2 subunit C) (Ribonuclease HI subunit C) 166 17,823 Beta strand (8); Chain (1); Helix (5); Modified residue (1); Sequence conflict (1); Turn (2) FUNCTION: Non catalytic subunit of RNase H2, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging-strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA:RNA duplexes. {ECO:0000269|PubMed:19923215}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: The RNase H2 complex is a heterotrimer composed of the catalytic subunit RNASEH2A and the non-catalytic subunits RNASEH2B and RNASEH2C. {ECO:0000269|PubMed:19923215}. +P49312 ROA1_MOUSE Heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1) (HDP-1) (Helix-destabilizing protein) (Single-strand-binding protein) (Topoisomerase-inhibitor suppressed) (hnRNP core protein A1) [Cleaved into: Heterogeneous nuclear ribonucleoprotein A1, N-terminally processed] 320 34,196 Alternative sequence (1); Chain (2); Compositional bias (2); Cross-link (7); Domain (2); Initiator methionine (1); Modified residue (33); Region (4) FUNCTION: Involved in the packaging of pre-mRNA into hnRNP particles, transport of poly(A) mRNA from the nucleus to the cytoplasm and may modulate splice site selection (By similarity). May bind to specific miRNA hairpins (By similarity). {ECO:0000250|UniProtKB:P09651}. PTM: Sumoylated. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P09651}. Cytoplasm {ECO:0000250|UniProtKB:P09651}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Shuttles continuously between the nucleus and the cytoplasm along with mRNA. Component of ribonucleosomes. {ECO:0000250|UniProtKB:P09651}. SUBUNIT: Identified in the spliceosome C complex. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with SEPT6. Interacts with C9orf72. Interacts with KHDRBS1. Interacts with UBQLN2. {ECO:0000250|UniProtKB:P09651}. +P60603 ROMO1_MOUSE Reactive oxygen species modulator 1 (ROS modulator 1) (Protein MGR2 homolog) 79 8,183 Chain (1); Region (1); Transmembrane (1) TRANSMEM 22 44 Helical. {ECO:0000255}. FUNCTION: Has antibacterial activity against a variety of bacteria including S.aureus, P.aeruginosa and M.tuberculosis. Acts by inducing bacterial membrane breakage (By similarity). {ECO:0000250}.; FUNCTION: Induces production of reactive oxygen species (ROS) which are necessary for cell proliferation. May play a role in inducing oxidative DNA damage and replicative senescence. May play a role in the coordination of mitochondrial morphology and cell proliferation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Detected in brain, liver and kidney. {ECO:0000269|PubMed:16842742}. +P70336 ROCK2_MOUSE Rho-associated protein kinase 2 (EC 2.7.11.1) (Rho-associated, coiled-coil-containing protein kinase 2) (Rho-associated, coiled-coil-containing protein kinase II) (ROCK-II) (p164 ROCK-2) 1388 160,586 Active site (1); Alternative sequence (2); Binding site (1); Chain (1); Coiled coil (1); Domain (5); Modified residue (6); Nucleotide binding (1); Region (3); Site (1); Zinc finger (1) FUNCTION: Protein kinase which is a key regulator of actin cytoskeleton and cell polarity. Involved in regulation of smooth muscle contraction, actin cytoskeleton organization, stress fiber and focal adhesion formation, neurite retraction, cell adhesion and motility via phosphorylation of ADD1, BRCA2, CNN1, EZR, DPYSL2, EP300, MSN, MYL9/MLC2, NPM1, RDX, PPP1R12A and VIM. Phosphorylates SORL1 and IRF4. Acts as a negative regulator of VEGF-induced angiogenic endothelial cell activation. Positively regulates the activation of p42/MAPK1-p44/MAPK3 and of p90RSK/RPS6KA1 during myogenic differentiation. Plays an important role in the timely initiation of centrosome duplication. Inhibits keratinocyte terminal differentiation. May regulate closure of the eyelids and ventral body wall through organization of actomyosin bundles. Plays a critical role in the regulation of spine and synaptic properties in the hippocampus. Plays a role in placental homeostasis during the perinatal period. Plays an important role in generating the circadian rhythm of the aortic myofilament Ca(2+) sensitivity and vascular contractility by modulating the myosin light chain phosphorylation. {ECO:0000269|PubMed:12832488, ECO:0000269|PubMed:18718479, ECO:0000269|PubMed:19181962, ECO:0000269|PubMed:20697158, ECO:0000269|PubMed:23172836}. PTM: Autophosphorylated. Phosphorylation at Tyr-722 reduces its binding to RHOA and is crucial for focal adhesion dynamics. Dephosphorylation by PTPN11 stimulates its RHOA binding activity (By similarity). {ECO:0000250}.; PTM: Cleaved by granzyme B during apoptosis. This leads to constitutive activation of the kinase and membrane blebbing. SUBCELLULAR LOCATION: Isoform 1: Cytoplasm. Cell membrane; Peripheral membrane protein. Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Note=Cytoplasmic, and associated with actin microfilaments and the plasma membrane. {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Cell membrane; Peripheral membrane protein. SUBUNIT: Homodimer. Interacts with RHOA (activated by GTP), CHORDC1, IRS1, RHOB, RHOC, PPP1R12A, SORL1, EP300 and BRCA2. Interacts with NPM1 and this interaction enhances its activity. Interacts with RAF1. {ECO:0000250}. DOMAIN: An interaction between Thr-414 and Asp-48 is essential for kinase activity and dimerization. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in brain, heart, lung, liver, stomach, spleen, kidney, testis, muscle, embryo and placenta. Isoform 2 is expressed predominantly in the skeletal muscle. {ECO:0000269|PubMed:17606625, ECO:0000269|PubMed:8772201}. +Q9ESG2 ROP1_MOUSE Ropporin-1 (Rhophilin-associated 'oppo' protein) (Rhophilin-associated protein 1) 212 24,003 Chain (1); Domain (1); Modified residue (1); Region (1) FUNCTION: Important for male fertility. With ROPN1L, involved in fibrous sheath integrity and sperm motility, plays a role in PKA-dependent signaling processes required for spermatozoa capacitation. {ECO:0000269|PubMed:23303679}. PTM: Sumoylated, sumoylation decreases upon spermatozoa capacitation conditions. {ECO:0000269|PubMed:27398160}. SUBCELLULAR LOCATION: Cell projection, cilium, flagellum {ECO:0000269|PubMed:11278869, ECO:0000269|PubMed:23303679}. Note=In the sperm tail, found in the principal piece and in the cytoplasmic droplet located at the distal end of the midpiece. Inner surface of the fibrous sheath. SUBUNIT: Homodimer. Interacts with AKAP3 (By similarity). May interact with SPA17 (By similarity). Interacts with RHPN1 (PubMed:10591629). Interacts with FSCB; the interaction increases upon spermatozoa capacitation conditions (PubMed:27398160). {ECO:0000250|UniProtKB:Q96C74, ECO:0000250|UniProtKB:Q9BZX4, ECO:0000269|PubMed:10591629, ECO:0000269|PubMed:27398160}. DOMAIN: The RIIa domain mediates interaction with AKAP3. {ECO:0000250}. TISSUE SPECIFICITY: Testis-specific. Present in the most inner parts of seminiferous tubules (at protein level). {ECO:0000269|PubMed:10591629, ECO:0000269|PubMed:23303679}. +Q62100 PRM3_MOUSE Protamine-3 (Sperm protamine P3) 101 11,166 Chain (1); Compositional bias (2); Modified residue (1); Sequence conflict (3) FUNCTION: Protamines substitute for histones in the chromatin of sperm during the haploid phase of spermatogenesis. They compact sperm DNA into a highly condensed, stable and inactive complex. SUBCELLULAR LOCATION: Nucleus. Chromosome. TISSUE SPECIFICITY: Testis. +Q80UW3 RINL_MOUSE Ras and Rab interactor-like protein 563 62,354 Alternative sequence (2); Chain (1); Domain (1); Erroneous initiation (2); Sequence conflict (1) FUNCTION: Guanine nucleotide exchange factor (GEF) for RAB5A and RAB22A that activates RAB5A and RAB22A by exchanging bound GDP for free GTP. Plays a role in endocytosis via its role in activating Rab family members. {ECO:0000269|PubMed:21419809}. SUBCELLULAR LOCATION: Cell projection, ruffle {ECO:0000269|PubMed:21419809}. Cytoplasmic vesicle {ECO:0000269|PubMed:21419809}. SUBUNIT: Interacts with RAB5A, RAB22A and MUSK. {ECO:0000269|PubMed:21419809}. TISSUE SPECIFICITY: Detected in thymus and spleen (at protein level). Detected in lung, liver, kidney, spleen, thymus and skeletal muscle. {ECO:0000269|PubMed:21419809}. +Q9ERK0 RIPK4_MOUSE Receptor-interacting serine/threonine-protein kinase 4 (EC 2.7.11.1) (Ankyrin repeat domain-containing protein 3) (PKC-associated protein kinase) (PKC-regulated protein kinase) 786 86,613 Active site (1); Beta strand (14); Binding site (1); Chain (1); Compositional bias (1); Cross-link (2); Domain (1); Helix (11); Nucleotide binding (1); Repeat (10); Sequence conflict (1); Site (2); Turn (4) FUNCTION: Involved in stratified epithelial development (By similarity). It is a direct transcriptional target of TP63. Plays a role in NF-kappa-B activation. {ECO:0000250, ECO:0000269|PubMed:12446564, ECO:0000269|PubMed:22197488}. PTM: May be phosphorylated by MAP3K2 and MAP3K3. {ECO:0000269|PubMed:11278382, ECO:0000269|PubMed:12676934}.; PTM: Proteolytically cleaved by during Fas-induced apoptosis. Cleavage at Asp-342 and Asp-380. {ECO:0000269|PubMed:12446564}.; PTM: Polyubiquitinated with 'Lys-48' and 'Lys-63'-linked chains by BIRC2/c-IAP1 and BIRC3/c-IAP2, leading to activation of NF-kappa-B. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein. Note=At steady state, a minor portion of this protein is membrane-associated. The major portion is cytoplasmic. SUBUNIT: Interacts with PRKCB. Interacts with TRAF1, TRAF2, TRAF3 and TRAF5. Interacts with BIRC2/c-IAP1, BIRC3/c-IAP2 and XIAP/BIRC4. {ECO:0000269|PubMed:11278382, ECO:0000269|PubMed:12446564}. TISSUE SPECIFICITY: Ubiquitously expressed, with an abundant expression in the thymus, bone marrow, pro-B, pre-B and immature B cells and a weak expression in the spleen. {ECO:0000269|PubMed:11278382}. +P33587 PROC_MOUSE Vitamin K-dependent protein C (EC 3.4.21.69) (Anticoagulant protein C) (Autoprothrombin IIA) (Blood coagulation factor XIV) [Cleaved into: Vitamin K-dependent protein C light chain; Vitamin K-dependent protein C heavy chain; Activation peptide] 460 51,818 Active site (3); Chain (3); Disulfide bond (12); Domain (4); Glycosylation (3); Modified residue (11); Natural variant (2); Peptide (1); Propeptide (1); Sequence conflict (1); Signal peptide (1); Site (1) FUNCTION: Protein C is a vitamin K-dependent serine protease that regulates blood coagulation by inactivating factors Va and VIIIa in the presence of calcium ions and phospholipids. Exerts a protective effect on the endothelial cell barrier function. {ECO:0000250|UniProtKB:P04070}. PTM: The vitamin K-dependent, enzymatic carboxylation of some Glu residues allows the modified protein to bind calcium.; PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P04070}. Golgi apparatus {ECO:0000250|UniProtKB:P04070}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P04070}. SUBUNIT: Synthesized as a single chain precursor, which is cleaved into a light chain and a heavy chain held together by a disulfide bond. The enzyme is then activated by thrombin, which cleaves a tetradecapeptide from the amino end of the heavy chain; this reaction, which occurs at the surface of endothelial cells, is strongly promoted by thrombomodulin. TISSUE SPECIFICITY: Plasma; synthesized in the liver. +Q2WG77 RIPP1_MOUSE Protein ripply1 201 21,804 Chain (1); Compositional bias (2); Motif (1); Region (1) FUNCTION: Plays a role in somitogenesis. Essential for transcriptional repression of the segmental patterning genes, thus terminating the segmentation program in the presomitic mesoderm, and also required for the maintenance of rostrocaudal polarity in somites (By similarity). {ECO:0000250|UniProtKB:Q2WG80}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q2WG80}. DOMAIN: The ripply homology domain is required for transcriptional repression. {ECO:0000250}.; DOMAIN: The WRPW motif is required for binding to TLE/GROUCHO proteins. {ECO:0000250|UniProtKB:Q2WG80}. TISSUE SPECIFICITY: Expressed in the anterior presomitic mesoderm and somites of stage E9.5 embryos. Also expressed in tongue, diaphragm and intercostal muscles at E16.5. {ECO:0000269|PubMed:16326386}. +Q2WG76 RIPP2_MOUSE Protein ripply2 128 14,305 Chain (1); Motif (1); Region (1); Sequence caution (1) FUNCTION: Plays a role in somitogenesis. Required for somite segregation and establishment of rostrocaudal polarity in somites. {ECO:0000269|PubMed:17360776, ECO:0000269|PubMed:17531978}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q2WG80}. DOMAIN: The ripply homology domain is required for transcriptional repression. {ECO:0000250}.; DOMAIN: The WRPW motif is required for binding to tle/groucho proteins. {ECO:0000250|UniProtKB:Q2WG80}. TISSUE SPECIFICITY: Expressed in the embryonic anterior presomitic mesoderm. First expressed in S-I at E8.5, where expression is maintained until E13.5, with an additional stripe of expression sometimes seen in the rostral part of S0 and S-I. {ECO:0000269|PubMed:16326386, ECO:0000269|PubMed:17531978}. +Q8BG41 PSB11_MOUSE Proteasome subunit beta type-11 (EC 3.4.25.1) (Proteasome subunit beta-5t) 302 33,220 Active site (1); Chain (1); Modified residue (1); Propeptide (1); Sequence conflict (2) FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. Incorporated instead of PSMB5 or PSMB8, this unit reduces the chymotrypsin-like activity of the proteasome. Plays a pivotal role in development of CD8-positive T-cells. {ECO:0000269|PubMed:17540904}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}. Nucleus {ECO:0000250}. SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel. Incorporated instead of PSMB5 and PSMB8. {ECO:0000269|PubMed:17540904}. TISSUE SPECIFICITY: Expressed exclusively in cortical thymic epithelial cells. {ECO:0000269|PubMed:17540904}. +Q3TXS7 PSMD1_MOUSE 26S proteasome non-ATPase regulatory subunit 1 (26S proteasome regulatory subunit RPN2) (26S proteasome regulatory subunit S1) 953 105,730 Chain (1); Compositional bias (1); Modified residue (9); Repeat (10) FUNCTION: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. {ECO:0000250|UniProtKB:Q99460}. SUBUNIT: Component of the 19S proteasome regulatory particle complex. The 26S proteasome consists of a 20S core particle (CP) and two 19S regulatory subunits (RP). The regulatory particle is made of a lid composed of 9 subunits, a base containing 6 ATPases and few additional components including PSMD1. Interacts with ADRM1. Interacts with ZFAND1 (By similarity). {ECO:0000250|UniProtKB:Q99460}. +P97372 PSME2_MOUSE Proteasome activator complex subunit 2 (11S regulator complex subunit beta) (REG-beta) (Activator of multicatalytic protease subunit 2) (Proteasome activator 28 subunit beta) (PA28b) (PA28beta) 239 27,057 Beta strand (1); Chain (1); Helix (7); Initiator methionine (1); Modified residue (2); Sequence conflict (1); Turn (1) FUNCTION: Implicated in immunoproteasome assembly and required for efficient antigen processing. The PA28 activator complex enhances the generation of class I binding peptides by altering the cleavage pattern of the proteasome. SUBUNIT: Heterodimer of PSME1 and PSME2, which forms a hexameric ring. +Q14B62 PTHD1_MOUSE Patched domain-containing protein 1 888 101,506 Alternative sequence (1); Chain (1); Domain (1); Glycosylation (10); Sequence conflict (2); Transmembrane (11) TRANSMEM 20 40 Helical. {ECO:0000255}.; TRANSMEM 273 293 Helical. {ECO:0000255}.; TRANSMEM 298 318 Helical. {ECO:0000255}.; TRANSMEM 328 348 Helical. {ECO:0000255}.; TRANSMEM 373 393 Helical. {ECO:0000255}.; TRANSMEM 407 427 Helical. {ECO:0000255}.; TRANSMEM 502 522 Helical. {ECO:0000255}.; TRANSMEM 707 727 Helical. {ECO:0000255}.; TRANSMEM 738 758 Helical. {ECO:0000255}.; TRANSMEM 795 815 Helical. {ECO:0000255}.; TRANSMEM 826 846 Helical. {ECO:0000255}. FUNCTION: Required for the development and function of the thalamic reticular nucleus (TRN), a part of the thalamus that is critical for thalamocortical transmission, generation of sleep rhythms, sensorimotor processing and attention. {ECO:0000269|PubMed:27007844}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q96NR3}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q96NR3}. TISSUE SPECIFICITY: Broadly expressed in the brain (PubMed:20844286). Selectively expressed in the thalamic reticular nucleus (TRN) in early development and continues to be enriched in this structure throughout adult life (PubMed:27007844). {ECO:0000269|PubMed:20844286, ECO:0000269|PubMed:27007844}. +Q99LE1 RIPL2_MOUSE RILP-like protein 2 (Rab-interacting lysosomal-like protein 2) 197 22,393 Alternative sequence (1); Chain (1); Coiled coil (1); Domain (2); Helix (5); Mutagenesis (3) FUNCTION: Involved in cell shape and neuronal morphogenesis, positively regulating the establishment and maintenance of dendritic spines. Plays a role in cellular protein transport, including protein transport away from primary cilia. May function via activation of RAC1 and PAK1. {ECO:0000269|PubMed:23264467}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:23264467}. Cell projection, cilium {ECO:0000269|PubMed:23264467}. SUBUNIT: Interacts with RAC1 (By similarity). Homodimer. Interacts (via N-terminus) with MYO5A, the interaction is required for its role in dendrite formation. {ECO:0000250, ECO:0000269|PubMed:23798443}. +Q91YR7 PRP6_MOUSE Pre-mRNA-processing factor 6 (PRP6 homolog) (U5 snRNP-associated 102 kDa protein) (U5-102 kDa protein) 941 106,722 Alternative sequence (2); Chain (1); Compositional bias (1); Modified residue (5); Repeat (9); Sequence conflict (2) FUNCTION: Involved in pre-mRNA splicing as component of the U4/U6-U5 tri-snRNP complex, one of the building blocks of the spliceosome. Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but does not affect estrogen-induced transactivation. {ECO:0000250|UniProtKB:O94906}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:O94906}. Nucleus speckle {ECO:0000250|UniProtKB:O94906}. Note=Localized in splicing speckles. {ECO:0000250|UniProtKB:O94906}. SUBUNIT: Identified in the spliceosome B complex. Identified in the spliceosome C complex. Associates with the U5 snRNP particle. Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39, LSm proteins LSm2-8 and Sm proteins. Interacts with ARAF1. Interacts with AR and NR3C1, but not ESR1, independently of the presence of hormones. {ECO:0000250|UniProtKB:O94906}. +Q9JJV2 PROF2_MOUSE Profilin-2 (Profilin II) 140 15,032 Alternative sequence (2); Beta strand (9); Chain (1); Helix (5); Initiator methionine (1); Modified residue (1); Sequence conflict (2); Turn (1) FUNCTION: Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SUBUNIT: Occurs in many kinds of cells as a complex with monomeric actin in a 1:1 ratio (By similarity). Interacts with PFN2 (PubMed:19403918). {ECO:0000250|UniProtKB:P35080, ECO:0000269|PubMed:19403918}. TISSUE SPECIFICITY: Isoform IIa is the main isoform and is abundant in brain. Isoform IIb is a minor isoform. +Q68FE6 RIPR1_MOUSE Rho family-interacting cell polarization regulator 1 1223 132,352 Chain (1); Coiled coil (1); Compositional bias (1); Erroneous initiation (4); Modified residue (10); Sequence conflict (2) FUNCTION: Downstream effector protein for Rho-type small GTPases that plays a role in cell polarity and directional migration. Acts as an adapter protein, linking active Rho proteins to STK24 and STK26 kinases, and hence positively regulates Golgi reorientation in polarized cell migration upon Rho activation. Involved in the subcellular relocation of STK26 from the Golgi to cytoplasm punctae in a Rho- and PDCD10-dependent manner upon serum stimulation. {ECO:0000250|UniProtKB:Q6ZS17}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17251388}. Golgi apparatus {ECO:0000250|UniProtKB:Q6ZS17}. Note=Localizes to the podocyte major processes and cell body (PubMed:17251388). Colocalized with STK26 in the Golgi of serum-starved cells and relocated to cytoplasmic punctae, probably vesicular compartments, along with STK26 upon serum stimulation in a Rho- and PDCD10-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q6ZS17, ECO:0000269|PubMed:17251388}. SUBUNIT: Interacts (via N-terminus) with RHOA (GTP-bound form); this interaction links active RHOA to STK24 and STK26 kinases. Interacts with RHOB. Interacts with RHOC. Interacts (via C-terminus) with PDCD10; this interaction occurs in a Rho-independent manner. Interacts (via C-terminus) with STK24; this interaction occurs in a PDCD10-dependent and Rho-independent manner. Interacts (via C-terminus) with STK26; this interaction occurs in a PDCD10-dependent and Rho-independent manner. Interacts (via N-terminus) with 14-3-3 proteins; these interactions occur in a Rho-dependent manner. {ECO:0000250|UniProtKB:Q6ZS17}. TISSUE SPECIFICITY: Expressed in the kidney exclusively by glomerular podocytes. {ECO:0000269|PubMed:17251388}. +Q9DC48 PRP17_MOUSE Pre-mRNA-processing factor 17 (Cell division cycle 40 homolog) (PRP17 homolog) 579 65,461 Chain (1); Repeat (7) FUNCTION: Associates with the spliceosome late in the splicing pathway and may function in the second step of pre-mRNA splicing. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Identified in the spliceosome C complex. {ECO:0000250}. +Q6PE13 PRRT3_MOUSE Proline-rich transmembrane protein 3 971 101,224 Chain (1); Compositional bias (1); Glycosylation (2); Modified residue (12); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 468 488 Helical. {ECO:0000255}.; TRANSMEM 492 512 Helical. {ECO:0000255}.; TRANSMEM 533 553 Helical. {ECO:0000255}.; TRANSMEM 561 581 Helical. {ECO:0000255}.; TRANSMEM 589 609 Helical. {ECO:0000255}.; TRANSMEM 629 649 Helical. {ECO:0000255}.; TRANSMEM 670 690 Helical. {ECO:0000255}. TOPO_DOM 28 467 Extracellular. {ECO:0000255}.; TOPO_DOM 489 491 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 513 532 Extracellular. {ECO:0000255}.; TOPO_DOM 554 560 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 582 588 Extracellular. {ECO:0000255}.; TOPO_DOM 610 628 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 650 669 Extracellular. {ECO:0000255}.; TOPO_DOM 691 971 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9CQJ5 PRR13_MOUSE Proline-rich protein 13 137 14,208 Chain (1); Compositional bias (2); Sequence conflict (1) FUNCTION: Negatively regulates TSP1 expression at the level of transcription. This down-regulation was shown to reduce taxane-induced apoptosis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +Q8BV84 PRR9_MOUSE Proline-rich protein 9 116 12,797 Chain (1); Compositional bias (1) +P54775 PRS6B_MOUSE 26S proteasome regulatory subunit 6B (26S proteasome AAA-ATPase subunit RPT3) (CIP21) (MB67-interacting protein) (MIP224) (Proteasome 26S subunit ATPase 4) (Tat-binding protein 7) (TBP-7) 418 47,408 Beta strand (1); Chain (1); Helix (5); Modified residue (6); Nucleotide binding (1); Sequence conflict (10) FUNCTION: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. PSMC4 belongs to the heterohexameric ring of AAA (ATPases associated with diverse cellular activities) proteins that unfolds ubiquitinated target proteins that are concurrently translocated into a proteolytic chamber and degraded into peptides. {ECO:0000250|UniProtKB:P43686}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P43686}. Nucleus {ECO:0000250|UniProtKB:P43686}. SUBUNIT: Component of the 19S proteasome regulatory particle complex. The 26S proteasome consists of a 20S core particle (CP) and two 19S regulatory subunits (RP). The regulatory particle is made of a lid composed of 9 subunits, a base containing 6 ATPases including PSMC4 and few additional components. Interacts with NR1I3. Interacts with PAAF1. Interacts with TRIM5. Interacts with ZFAND1 (By similarity). {ECO:0000250|UniProtKB:P43686}. +Q9D9B7 PRR30_MOUSE Proline-rich protein 30 401 43,406 Chain (1); Compositional bias (1); Sequence conflict (2) +Q9D6X6 PRS23_MOUSE Serine protease 23 (EC 3.4.21.-) 382 43,071 Active site (3); Chain (1); Disulfide bond (1); Glycosylation (2); Sequence conflict (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q8BW11 PRS58_MOUSE Putative inactive serine protease 58 (EC 3.4.21.4) (Trypsin-X3) 241 26,865 Active site (2); Chain (1); Disulfide bond (4); Domain (1); Glycosylation (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q8C0F9 PRS35_MOUSE Inactive serine protease 35 409 45,787 Chain (1); Compositional bias (1); Disulfide bond (1); Domain (1); Glycosylation (1); Sequence conflict (4); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: In ovary, it localizes to the theca cells of pre-antral follicles, the theca and granulosa cells of pre-ovulatory and ovulatory follicles, as well as to the developing corpus luteum. {ECO:0000269|PubMed:16870946}. +Q5PRE5 PRSR1_MOUSE Proline and serine-rich protein 1 913 91,978 Chain (1); Compositional bias (1); Erroneous initiation (1); Modified residue (1) +Q9CZM2 RL15_MOUSE 60S ribosomal protein L15 204 24,146 Chain (1); Cross-link (1); Initiator methionine (1); Lipidation (1); Modified residue (3); Sequence conflict (1) SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P61313}; Lipid-anchor {ECO:0000250|UniProtKB:P61313}. SUBUNIT: Interacts with IFIT1 (via TPR repeats 1-4). {ECO:0000250}. +Q9CPR4 RL17_MOUSE 60S ribosomal protein L17 184 21,423 Chain (1) FUNCTION: Component of the large ribosomal subunit. {ECO:0000250|UniProtKB:P18621}. SUBUNIT: Component of the large ribosomal subunit. {ECO:0000250|UniProtKB:P18621}. +Q922Q2 RIOK1_MOUSE Serine/threonine-protein kinase RIO1 (EC 2.7.11.1) (EC 3.6.3.-) (RIO kinase 1) 567 64,910 Active site (2); Binding site (3); Chain (1); Domain (1); Erroneous initiation (3); Frameshift (1); Metal binding (2); Modified residue (2); Sequence caution (1); Sequence conflict (3) FUNCTION: Involved in the final steps of cytoplasmic maturation of the 40S ribosomal subunit. Involved in processing of 18S-E pre-rRNA to the mature 18S rRNA. Required for the recycling of NOB1 and PNO1 from the late 40S precursor (By similarity). The association with the very late 40S subunit intermediate may involve a translation-like checkpoint point cycle preceeding the binding to the 60S ribosomal subunit (By similarity). Despite the protein kinase domain is proposed to act predominantly as an ATPase (By similarity). The catalytic activity regulates its dynamic association with the 40S subunit (By similarity). In addition to its role in ribosomal biogenesis acts as an adapter protein by recruiting NCL/nucleolin the to PRMT5 complex for its symmetrical methylation (By similarity). {ECO:0000250|UniProtKB:G0S3J5, ECO:0000250|UniProtKB:Q12196, ECO:0000250|UniProtKB:Q9BRS2}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9BRS2}. SUBUNIT: Associates with the precursor of the 40S ribosome subunit. Interacts (via its N-terminus) with PRMT5 (via its N-terminus). Interacts with WDR77 (By similarity). Found in a PRMT5 complex composed of PRMT5, WDR77 and RIOK1 (By similarity). Interacts (via its C-terminus) with NCL; this interaction targets NCL for PRTM5 methylation (By similarity). {ECO:0000250|UniProtKB:Q9BRS2}. +Q9CQS5 RIOK2_MOUSE Serine/threonine-protein kinase RIO2 (EC 2.7.11.1) (RIO kinase 2) 547 62,490 Active site (1); Binding site (1); Chain (1); Domain (1); Modified residue (11); Motif (1); Sequence conflict (3) FUNCTION: Serine/threonine-protein kinase involved in the final steps of cytoplasmic maturation of the 40S ribosomal subunit. Involved in export of the 40S pre-ribosome particles (pre-40S) from the nucleus to the cytoplasm. Its kinase activity is required for the release of NOB1, PNO1 and LTV1 from the late pre-40S and the processing of 18S-E pre-rRNA to the mature 18S rRNA. May regulate the timing of the metaphase-anaphase transition during mitotic progression, and its phosphorylation, may regulates this function. {ECO:0000250|UniProtKB:Q9BVS4}. PTM: Autophosphorylated (in vitro). Phosphorylation affects the timing of the metaphase-anaphase transition. {ECO:0000250|UniProtKB:Q9BVS4}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BVS4}. SUBUNIT: Associated with late 40S pre-ribosomal particles. Interacts with PLK1 (via its N-terminus). {ECO:0000250|UniProtKB:Q9BVS4}. +Q60855 RIPK1_MOUSE Receptor-interacting serine/threonine-protein kinase 1 (EC 2.7.11.1) (Cell death protein RIP) (Receptor-interacting protein 1) (RIP-1) 656 74,854 Active site (1); Binding site (1); Chain (1); Cross-link (1); Domain (2); Modified residue (9); Motif (1); Natural variant (1); Nucleotide binding (1); Region (1); Sequence conflict (1) FUNCTION: Serine-threonine kinase which transduces inflammatory and cell-death signals (programmed necrosis) following death receptors ligation, activation of pathogen recognition receptors (PRRs), and DNA damage (PubMed:12654725, PubMed:19590578). Upon activation of TNFR1 by the TNF-alpha family cytokines, TRADD and TRAF2 are recruited to the receptor (By similarity). Phosphorylates DAB2IP at 'Ser-728' in a TNF-alpha-dependent manner, and thereby activates the MAP3K5-JNK apoptotic cascade (By similarity). Ubiquitination by TRAF2 via 'Lys-63'-link chains acts as a critical enhancer of communication with downstream signal transducers in the mitogen-activated protein kinase pathway and the NF-kappa-B pathway, which in turn mediate downstream events including the activation of genes encoding inflammatory molecules (By similarity). Polyubiquitinated protein binds to IKBKG/NEMO, the regulatory subunit of the IKK complex, a critical event for NF-kappa-B activation (By similarity). Interaction with other cellular RHIM-containing adapters initiates gene activation and cell death (By similarity). RIPK1 and RIPK3 association, in particular, forms a necrosis-inducing complex (By similarity). {ECO:0000250|UniProtKB:Q13546, ECO:0000269|PubMed:12654725, ECO:0000269|PubMed:19590578}. PTM: Proteolytically cleaved by caspase-8 during TNF-induced apoptosis. Cleavage abolishes NF-kappa-B activation and enhances pro-apoptotic signaling through the TRADD-FADD interaction. {ECO:0000250|UniProtKB:Q13546}.; PTM: RIPK1 and RIPK3 undergo reciprocal auto- and trans-phosphorylation. Phosphorylation of Ser-161 by RIPK3 is necessary for the formation of the necroptosis-inducing complex. {ECO:0000250|UniProtKB:Q13546}.; PTM: Ubiquitinated by 'Lys-11'-, 'Lys-48'-, 'Lys-63'- and linear-linked type ubiquitin (By similarity). Polyubiquitination with 'Lys-63'-linked chains by TRAF2 induces association with the IKK complex (By similarity). Deubiquitination of 'Lys-63'-linked chains and polyubiquitination with 'Lys-48'-linked chains by TNFAIP3 leads to RIPK1 proteasomal degradation and consequently down-regulates TNF-alpha-induced NFkappa-B signaling (By similarity). 'Lys-48'-linked polyubiquitination by RFFL or RNF34 also promotes proteasomal degradation and negatively regulates TNF-alpha-induced NF-kappa-B signaling (By similarity). Linear polyubiquitinated; the head-to-tail linear polyubiquitination ('Met-1'-linked) is mediated by the LUBAC complex and decreases protein kinase activity (PubMed:28701375). Deubiquitination of linear polyubiquitin by CYLD promotes the kinase activity (PubMed:28701375). Also ubiquitinated with 'Lys-11'-linked chains (By similarity). Polyubiquitinated with 'Lys-48' and 'Lys-63'-linked chains by BIRC2/c-IAP1 and BIRC3/c-IAP2, leading to activation of NF-kappa-B (By similarity). Ubiquitinated with 'Lys-63'-linked chains by PELI1 (By similarity). {ECO:0000250|UniProtKB:Q13546, ECO:0000269|PubMed:28701375}. SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. SUBUNIT: Interacts (via RIP homotypic interaction motif) with RIPK3 (via RIP homotypic interaction motif) (By similarity). Upon TNF-induced necrosis, the RIPK1-RIPK3 dimer further interacts with PGAM5 and MLKL; the formation of this complex leads to PGAM5 phosphorylation and increase in PGAM5 phosphatase activity (By similarity). Interacts (via the death domain) with TNFRSF6 (via the death domain) and TRADD (via the death domain) (By similarity). Is recruited by TRADD to TNFRSF1A in a TNF-dependent process (By similarity). Binds RNF216, EGFR, IKBKG, TRAF1, TRAF2 and TRAF3 (By similarity). Interacts with BNLF1 (By similarity). Interacts with SQSTM1 upon TNF-alpha stimulation (By similarity). May interact with MAVS/IPS1 (By similarity). Interacts with ZFAND5 (By similarity). Interacts with RBCK1 (By similarity). Interacts with ZBP1 (PubMed:19590578). Interacts with BIRC2/c-IAP1, BIRC3/c-IAP2 and XIAP/BIRC4. Interacts (via kinase domain) with DAB2IP (via Ras-GAP domain); the interaction occurs in a TNF-alpha-dependent manner (By similarity). Interacts with ARHGEF2 (By similarity). Interacts (via protein kinase domain) with RFFL; involved in RIPK1 ubiquitination (By similarity). Interacts with RNF34; involved in RIPK1 ubiquitination (By similarity). Interacts with TICAM1 and this interaction is enhanced in the presence of WDFY1 (By similarity). Interacts with PELI1 (PubMed:29883609). Interacts (via Death domain) with CRADD (via Death domain); the interaction is direct (By similarity). {ECO:0000250|UniProtKB:Q13546, ECO:0000269|PubMed:19590578, ECO:0000269|PubMed:29883609}.; SUBUNIT: (Microbial infection) Interacts with Murid herpesvirus 1 protein RIR1. {ECO:0000269|PubMed:18442983}. DOMAIN: Contains a C-terminal death domain (DD) that engages other DD-containing proteins as well as a central (intermediate) region important for NF-kB activation and RHIM-dependent signaling. The Death domain mediates a direct interaction with the Death domain of CRADD. {ECO:0000250|UniProtKB:Q13546}. TISSUE SPECIFICITY: Found at low levels in all tissues. {ECO:0000269|PubMed:7538908}. +P58801 RIPK2_MOUSE Receptor-interacting serine/threonine-protein kinase 2 (EC 2.7.11.1) (Tyrosine-protein kinase RIPK2) (EC 2.7.10.2) 539 60,400 Active site (1); Binding site (1); Chain (1); Cross-link (1); Domain (2); Modified residue (8); Nucleotide binding (1) FUNCTION: Serine/threonine/tyrosine kinase that plays an essential role in modulation of innate and adaptive immune responses. Upon stimulation by bacterial peptidoglycans, NOD1 and NOD2 are activated, oligomerize and recruit RIPK2 through CARD-CARD domains. Once recruited, autophosphorylates and undergoes 'Lys-63'-linked polyubiquitination by E3 ubiquitin ligases XIAP, BIRC2 and BIRC3. The polyubiquitinated protein mediates the recruitment of MAP3K7/TAK1 to IKBKG/NEMO and induces 'Lys-63'-linked polyubiquitination of IKBKG/NEMO and subsequent activation of IKBKB/IKKB. In turn, NF-kappa-B is release from NF-kappa-B inhibitors and translocates into the nucleus where it activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis. Plays also a role during engagement of the T-cell receptor (TCR) in promoting BCL10 phosphorylation and subsequent NF-kappa-B activation. {ECO:0000269|PubMed:21469090}. PTM: Autophosphorylated. Autophosphorylation at Tyr-473 is necessary for effective NOD2 signaling. {ECO:0000250|UniProtKB:P51617}.; PTM: Ubiquitinated on Lys-209; undergoes 'Lys-63'-linked polyubiquitination catalyzed by ITCH. Polyubiquitinated with 'Lys-48' and 'Lys-63'-linked chains by BIRC2/c-IAP1 and BIRC3/c-IAP2, leading to activation of NF-kappa-B. Also undergoes 'Met-1'-linked polyubiquitination; the head-to-tail linear polyubiquitination is mediated by the LUBAC complex in response to NOD2 stimulation. Linear polyubiquitination is restricted by FAM105B/otulin, probably to limit NOD2-dependent proinflammatory signaling activation of NF-kappa-B (By similarity). {ECO:0000250|UniProtKB:P51617}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. SUBUNIT: Found in a signaling complex consisting of at least ARHGEF2, NOD2 and RIPK2. Interacts with ARHGEF2. Binds to CFLAR/CLARP and CASP1 via their CARD domains. Binds to BIRC3/c-IAP1 and BIRC2/c-IAP2, TRAF1, TRAF2, TRAF5 and TRAF6. May be a component of both the TNFRSF1A and TNRFSF5/CD40 receptor complex. Interacts with NOD1. Interacts (via CARD domain) with NOD2 (via CARD domain). Interacts with MAP3K4; this interaction sequesters RIPK2 from the NOD2 signaling pathway. Interacts with IKBKG/NEMO. The polyubiquitinated protein interacts with MAP3K7/TAK1. Interacts with XIAP/BIRC4. Interacts with NLRP10 (By similarity). Interacts with CARD9. Interacts with INAVA; the interaction takes place upon PRR stimulation (By similarity). {ECO:0000250|UniProtKB:P51617, ECO:0000269|PubMed:17187069}. DOMAIN: Contains an N-terminal kinase domain and a C-terminal caspase activation and recruitment domain (CARD) that mediates the recruitment of CARD-containing proteins. {ECO:0000250|UniProtKB:P51617}. +Q9D1T5 PRR15_MOUSE Proline-rich protein 15 122 13,655 Chain (1); Modified residue (1) FUNCTION: May have a role in proliferation and/or differentiation. {ECO:0000269|PubMed:12768423}. TISSUE SPECIFICITY: Exhibits a cell type specific expression pattern only in the small and large intestine and in the testis. Along the intestinal tract expression is restricted to the non-proliferating epithelial cells surrounding the villi and no expression is found in the intestinal crypts, where proliferation occurs. In the testis, it is detected only in post-mitotic secondary spermatocytes. {ECO:0000269|PubMed:12768423}. +Q9CWY9 RIP_MOUSE RPA-interacting protein 219 24,897 Chain (1); Modified residue (1); Region (1); Zinc finger (1) FUNCTION: Mediates the import of RPA complex into the nucleus, possibly via some interaction with importin beta. Sumoylation mediates the localization of RPA complex into the PML body of the nucleus, thereby participating in RPA function in DNA metabolism (By similarity). {ECO:0000250}. PTM: Sumoylated; required for localization in the nuclear PML body and transport of RPA complex in PML body. Upon UV irradiation and during S phase, it is desumoylated, releasing RPA complex that is translocated to sites of DNA damage. Sumoylation takes place at different Lys residues (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with the RPA1 subunit of RPA complex. {ECO:0000250}. +Q9R1P1 PSB3_MOUSE Proteasome subunit beta type-3 (EC 3.4.25.1) (Proteasome chain 13) (Proteasome component C10-II) (Proteasome theta chain) 205 22,965 Beta strand (13); Chain (1); Helix (4); Initiator methionine (1); Modified residue (2); Turn (3) FUNCTION: Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). {ECO:0000269|PubMed:16581775, ECO:0000269|PubMed:22341445}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P49720}. Nucleus {ECO:0000250|UniProtKB:P49720}. SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is a barrel-shaped complex made of 28 subunits that are arranged in four stacked rings. The two outer rings are each formed by seven alpha subunits, and the two inner rings are formed by seven beta subunits. The proteolytic activity is exerted by three beta-subunits PSMB5, PSMB6 and PSMB7. {ECO:0000269|PubMed:16857966, ECO:0000269|PubMed:22341445}. TISSUE SPECIFICITY: Detected in liver (at protein level). {ECO:0000269|PubMed:22341445}. +P28076 PSB9_MOUSE Proteasome subunit beta type-9 (EC 3.4.25.1) (LMP-2d) (Low molecular mass protein 2) (Macropain chain 7) (Multicatalytic endopeptidase complex chain 7) (Proteasome chain 7) (Proteasome subunit beta-1i) (Really interesting new gene 12 protein) 219 23,397 Active site (1); Beta strand (11); Chain (1); Frameshift (1); Helix (7); Modified residue (2); Natural variant (3); Propeptide (1); Site (1); Turn (2) FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processing to generate class I binding peptides. Contributes to NFKBIA degradation and subsequently NFKB1 generation. {ECO:0000269|PubMed:16222703, ECO:0000269|PubMed:22341445}. PTM: Autocleaved. The resulting N-terminal Thr residue of the mature subunit is responsible for the nucleophile proteolytic activity. {ECO:0000250|UniProtKB:O35955}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}. Nucleus {ECO:0000250}. SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel. Component of the immunoproteasome, where it displaces the equivalent housekeeping subunit PSMB6. Component of the spermatoproteasome, a form of the proteasome specifically found in testis. Interacts with NCOA1, NCOA2 and NCOA3. {ECO:0000269|PubMed:16857966, ECO:0000269|PubMed:22341445, ECO:0000269|PubMed:23706739}. TISSUE SPECIFICITY: Detected in liver (at protein level). Expressed at high levels in the thymus, spleen, lung, heart and liver. Expressed at moderate levels in the kidney. {ECO:0000269|PubMed:22341445, ECO:0000269|PubMed:8325639}. +Q9Z2X2 PSD10_MOUSE 26S proteasome non-ATPase regulatory subunit 10 (26S proteasome regulatory subunit p28) (Gankyrin) 231 25,084 Beta strand (1); Chain (1); Frameshift (1); Helix (15); Repeat (7); Sequence conflict (3) FUNCTION: Acts as a chaperone during the assembly of the 26S proteasome, specifically of the PA700/19S regulatory complex (RC). In the initial step of the base subcomplex assembly is part of an intermediate PSMD10:PSMC4:PSMC5:PAAF1 module which probably assembles with a PSMD5:PSMC2:PSMC1:PSMD2 module (By similarity). Independently of the proteasome, regulates EGF-induced AKT activation through inhibition of the RHOA/ROCK/PTEN pathway, leading to prolonged AKT activation. Plays an important role in RAS-induced tumorigenesis. {ECO:0000250, ECO:0000269|PubMed:20628200}.; FUNCTION: Acts as an oncoprotein by being involved in negative regulation of tumor suppressors RB1 and p53/TP53. Overexpression is leading to phosphorylation of RB1 and proteasomal degradation of RB1. Regulates CDK4-mediated phosphorylation of RB1 by competing with CDKN2A for binding with CDK4. Facilitates binding of MDM2 to p53/TP53 and the mono- and polyubiquitination of p53/TP53 by MDM2 suggesting a function in targeting the TP53:MDM2 complex to the 26S proteasome. Involved in p53-independent apoptosis. Involved in regulation of NF-kappa-B by retaining it in the cytoplasm. Binds to the NF-kappa-B component RELA and accelerates its XPO1/CRM1-mediated nuclear export (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Part of transient complex containing PSMD10, PSMC4, PSMC5 and PAAF1 formed during the assembly of the 26S proteasome. Stays associated throughout the assembly of the PA700/19S RC and is released upon association with the 20S core. Interacts with PSMC4. Interacts with RB1. Interacts with CDK4. Interacts with MDM2. Interacts with RELA. Associates with a CDK4:CCND2 serine/threonine kinase complex (By similarity). Interacts with ARHGDIA and increases the interaction between ARHGDIA and RHOA, hence promotes ARHGDIA inactivation of RHOA and ROCK (By similarity). {ECO:0000250}. +Q9WVJ2 PSD13_MOUSE 26S proteasome non-ATPase regulatory subunit 13 (26S proteasome regulatory subunit RPN9) (26S proteasome regulatory subunit S11) (26S proteasome regulatory subunit p40.5) 376 42,809 Chain (1); Domain (1); Modified residue (1); Sequence caution (1); Sequence conflict (1) FUNCTION: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. {ECO:0000250|UniProtKB:Q9UNM6}. SUBUNIT: Component of the 19S proteasome regulatory particle complex. The 26S proteasome consists of a 20S core particle (CP) and two 19S regulatory subunits (RP). The regulatory particle is made of a lid composed of 9 subunits including PSMD13, a base containing 6 ATPases and few additional components. {ECO:0000250|UniProtKB:Q9UNM6, ECO:0000269|PubMed:16857966}. +O35593 PSDE_MOUSE 26S proteasome non-ATPase regulatory subunit 14 (EC 3.4.19.-) (26S proteasome regulatory subunit RPN11) (MAD1) 310 34,577 Chain (1); Domain (1); Metal binding (3); Modified residue (3); Motif (1); Sequence conflict (1) FUNCTION: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. The PSMD14 subunit is a metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains within the complex. Plays a role in response to double-strand breaks (DSBs): acts as a regulator of non-homologous end joining (NHEJ) by cleaving 'Lys-63'-linked polyubiquitin, thereby promoting retention of JMJD2A/KDM4A on chromatin and restricting TP53BP1 accumulation. Also involved in homologous recombination repair by promoting RAD51 loading. {ECO:0000250|UniProtKB:O00487}. SUBUNIT: Component of the 19S proteasome regulatory particle complex. The 26S proteasome consists of a 20S core particle (CP) and two 19S regulatory subunits (RP). The regulatory particle is made of a lid composed of 9 subunits including PSMD4, a base containing 6 ATPases and few additional components. Within the complex, PSMD4 interacts with subunit PSMD7 through their respective MPN domain. Interacts with TXNL1. {ECO:0000250|UniProtKB:O00487}. +Q5DTT2 PSD1_MOUSE PH and SEC7 domain-containing protein 1 (Exchange factor for ADP-ribosylation factor guanine nucleotide factor 6) (Exchange factor for ARF6) (Exchange factor for ARF6 A) (Pleckstrin homology and SEC7 domain-containing protein 1) 1024 109,687 Alternative sequence (3); Chain (1); Coiled coil (2); Compositional bias (3); Domain (2); Modified residue (3); Mutagenesis (1) FUNCTION: Guanine nucleotide exchange factor for ARF6 (By similarity). Isoform 2 and isoform 3 induce cytoskeletal remodeling, but lead to distinct morphological changes in HeLa cells: isoform 2 induces cell elongation and formation of actin-rich protrusions, whereas isoform 3 promotes the formation of membrane ruffles and loss of stress fibers (PubMed:19494129). {ECO:0000250|UniProtKB:A5PKW4, ECO:0000269|PubMed:19494129}. SUBCELLULAR LOCATION: Isoform 1: Cell membrane {ECO:0000269|PubMed:15540117, ECO:0000269|PubMed:17298598}. Cell projection, ruffle {ECO:0000269|PubMed:15540117, ECO:0000269|PubMed:17298598}. Note=Colocalizes with ACTN1 in membrane ruffles and central reticular structures. {ECO:0000269|PubMed:15540117, ECO:0000269|PubMed:17298598}.; SUBCELLULAR LOCATION: Isoform 2: Cell membrane {ECO:0000269|PubMed:19494129}. Cell projection {ECO:0000269|PubMed:19494129}. Note=Accumulates in microvilli-like protrusions. {ECO:0000269|PubMed:19494129}.; SUBCELLULAR LOCATION: Isoform 3: Cell membrane {ECO:0000269|PubMed:15540117, ECO:0000269|PubMed:19494129}. Cell projection, ruffle {ECO:0000269|PubMed:15540117, ECO:0000269|PubMed:19494129}. Note=Colocalizes with F-actin in membrane ruffles. {ECO:0000269|PubMed:15540117, ECO:0000269|PubMed:19494129}.; SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:A5PKW4}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:A5PKW4}. Cleavage furrow {ECO:0000250|UniProtKB:A5PKW4}. Note=Distributed uniformly on the plasma membrane, as well as throughout the cytoplasm during metaphase. Subsequently concentrated at patches in the equatorial region at the onset of cytokinesis, and becomes distributed in the equatorial region concurrent with cleavage furrow ingression. In later cytokinesis phases, fades away from the cleavage furrow and becomes uniformly distributed throughout the plasma membrane. {ECO:0000250|UniProtKB:A5PKW4}. SUBUNIT: Interacts with ACTN1 (PubMed:17298598). Interacts (ARF6-bound form) with KCNK1; does not interact with KCNK1 in the absence of ARF6 (PubMed:15540117). {ECO:0000269|PubMed:15540117, ECO:0000269|PubMed:17298598}. TISSUE SPECIFICITY: Highest expression detected in brain and some expression detected also in uterus, stomach, ovary and intestine, with isoform 2 being expressed at the highest levels. In the brain, isoform 1 is highly expressed in the strata oriens, radiatum, lacunosum-moleculare of the hippocampal CA1-3 regions and the dentate molecular layer of the hippocampal formation, with lower levels detected in the neuronal cell layers and the stratum lucidum (at protein level). Not detected in tongue, thymus, spleen, lung, heart, liver and kidney. {ECO:0000269|PubMed:17298598, ECO:0000269|PubMed:19494129}. +Q6P1I6 PSD2_MOUSE PH and SEC7 domain-containing protein 2 (Exchange factor for ADP-ribosylation factor guanine nucleotide factor 6 C) (Exchange factor for ARF6 C) (Pleckstrin homology and SEC7 domain-containing protein 2) 770 84,299 Alternative sequence (2); Chain (1); Coiled coil (1); Domain (2); Modified residue (1); Transmembrane (1) TRANSMEM 619 636 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23603394}; Single-pass membrane protein {ECO:0000305}. Cell projection, ruffle membrane {ECO:0000269|PubMed:23603394}. Cleavage furrow {ECO:0000269|PubMed:23603394}. Note=In interphase associated with the plasma membrane, in particular with membrane ruffling regions. In cells undergoing cytokinesis, transiently found around the ingressing cleavage furrow. Not detected at the midbody ring/Flemming body. {ECO:0000269|PubMed:23603394}. +P62717 RL18A_MOUSE 60S ribosomal protein L18a 176 20,732 Chain (1); Cross-link (3); Modified residue (4) SUBUNIT: Binds IPO9 with high affinity. {ECO:0000250}. +Q9CY94 PSF3_MOUSE DNA replication complex GINS protein PSF3 (GINS complex subunit 3) 216 24,577 Chain (1); Region (1) FUNCTION: The GINS complex plays an essential role in the initiation of DNA replication, and progression of DNA replication forks. GINS complex seems to bind preferentially to single-stranded DNA (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the GINS complex which is a heterotetramer of GINS1, GINS2, GINS3 and GINS4. Forms a stable subcomplex with GINS2. GINS complex interacts with DNA primase in vitro. {ECO:0000250|UniProtKB:Q9BRX5}. +Q810J1 PSG22_MOUSE Pregnancy-specific glycoprotein 22 475 53,225 Chain (1); Disulfide bond (1); Domain (4); Glycosylation (3); Signal peptide (1) FUNCTION: May have an angiogenic function during early placental development. Binds to cell-surface heparan sulfate proteoglycans (HSPGs), and stimulates secretion of the proangiogenic factors VEGFA and TGFB from uterine dendritic cells and natural killer cells. Also induces endothelial tube formation in vitro. {ECO:0000269|PubMed:22423048}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q9Z0S9 PRAF1_MOUSE Prenylated Rab acceptor protein 1 (PRA1 family protein 1) (Prenylin) 185 20,619 Chain (1); Mutagenesis (9); Region (4); Topological domain (3); Transmembrane (4) TRANSMEM 79 94 Helical.; TRANSMEM 95 112 Helical.; TRANSMEM 132 148 Helical.; TRANSMEM 149 165 Helical. TOPO_DOM 1 78 Cytoplasmic. {ECO:0000269|PubMed:11535589}.; TOPO_DOM 113 131 Cytoplasmic. {ECO:0000269|PubMed:11535589}.; TOPO_DOM 166 185 Cytoplasmic. {ECO:0000269|PubMed:11535589}. FUNCTION: General Rab protein regulator required for vesicle formation from the Golgi complex. May control vesicle docking and fusion by mediating the action of Rab GTPases to the SNARE complexes. In addition it inhibits the removal of Rab GTPases from the membrane by GDI1 (By similarity). {ECO:0000250, ECO:0000269|PubMed:11335720}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O35394}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:O35394}. Golgi apparatus {ECO:0000250|UniProtKB:O35394}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250|UniProtKB:O35394}. Note=According to PubMed:11535589, it is an integral membrane protein, while other authors showed that it is cytoplasmic and membrane-associated to Golgi and synaptic vesicles. {ECO:0000250|UniProtKB:O35394}. SUBUNIT: Homodimer. Interacts with VAMP2 (synaptobrevin-2), GDI1, NRDG1 and PCLO (By similarity). Interacts with prenylated Rab proteins (including RAB5 and RAB6), and with the members of the Ras superfamily HRAS, RHOA, TC21, and RAP1A. {ECO:0000250, ECO:0000269|PubMed:11335720, ECO:0000269|PubMed:7782346}. +Q9JHK0 PR2A1_MOUSE Prolactin-2A1 (Placental prolactin-like protein M) (PLP-M) (PRL-like protein M) 228 25,554 Chain (1); Disulfide bond (2); Sequence conflict (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000250}. TISSUE SPECIFICITY: Expressed specifically in the placenta. Expression restricted to the junctional zone of the chorioallantoic placenta. {ECO:0000269|PubMed:10856884}. +Q9JIG8 PRAF2_MOUSE PRA1 family protein 2 178 19,478 Chain (1); Topological domain (5); Transmembrane (4) TRANSMEM 42 62 Helical. {ECO:0000255}.; TRANSMEM 65 85 Helical. {ECO:0000255}.; TRANSMEM 97 119 Helical. {ECO:0000255}.; TRANSMEM 123 140 Helical. {ECO:0000255}. TOPO_DOM 1 41 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 63 64 Extracellular. {ECO:0000255}.; TOPO_DOM 86 96 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 120 122 Extracellular. {ECO:0000255}.; TOPO_DOM 141 178 Cytoplasmic. {ECO:0000255}. FUNCTION: May be involved in ER/Golgi transport and vesicular traffic. Plays a proapoptotic role in cerulenin-induced neuroblastoma apoptosis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with CCR5 and GDE1. {ECO:0000250}. +Q9JLV9 PR2C5_MOUSE Prolactin-2C5 (Mitogen-regulated protein 4) 222 25,424 Alternative sequence (1); Chain (1); Disulfide bond (3); Glycosylation (1); Signal peptide (1) PTM: N-glycosylated and sialylated. {ECO:0000269|PubMed:10537154, ECO:0000269|PubMed:10803597}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10537154, ECO:0000269|PubMed:10803597}. TISSUE SPECIFICITY: Expressed in placenta (at protein level) (PubMed:10803597, PubMed:10537154, PubMed:16876275). Expressed in the tail hair follicle, with highest expression detected in the keratinocytes of the outer root sheath (PubMed:10803597). Expressed in ear skin with lesser amounts in small intestine (PubMed:10803597). Not detected in brain at 18 dpc, postnatal day 25 or postnatal day 55 (PubMed:16876275). {ECO:0000269|PubMed:10537154, ECO:0000269|PubMed:10803597, ECO:0000269|PubMed:16876275}. +Q8BFW3 PR15B_MOUSE Protein phosphatase 1 regulatory subunit 15B (Constitutive repressor of eIF2alpha phosphorylation) (CReP) 697 77,712 Alternative sequence (1); Chain (1); Modified residue (3) FUNCTION: Maintains low levels of EIF2S1 phosphorylation in unstressed cells by promoting its dephosphorylation by PP1. {ECO:0000269|PubMed:14638860, ECO:0000269|PubMed:19181853}. SUBUNIT: Interacts with PP1. Part of a complex containing PPP1R15B, PP1 and NCK1/2. {ECO:0000269|PubMed:14638860, ECO:0000269|PubMed:16835242}. +Q9JK53 PRELP_MOUSE Prolargin (Proline-arginine-rich end leucine-rich repeat protein) 378 43,293 Chain (1); Compositional bias (2); Disulfide bond (1); Glycosylation (4); Repeat (12); Signal peptide (1) FUNCTION: May anchor basement membranes to the underlying connective tissue. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SUBUNIT: Binds the basement membrane heparan sulfate proteoglycan perlecan and triple helical collagens type I and type II. {ECO:0000250}. DOMAIN: The basic N-terminal Arg/Pro-rich binds heparin and heparan sulfate. Binds collagens type I and type II through its leucine-rich repeat domain (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in cartilage throughout both fetal development and postnatal life. It is also expressed in the developing embryo prior to skeletogenesis. In adult, highest expression in lung, lower levels in cardiac and skeletal muscle. +Q80Y24 PRIC2_MOUSE Prickle-like protein 2 845 95,781 Chain (1); Compositional bias (3); Domain (4); Erroneous initiation (1); Lipidation (1); Modified residue (13); Propeptide (1); Sequence conflict (1) SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000305}. TISSUE SPECIFICITY: Expressed in the hippocampus and cerebral cortex. {ECO:0000269|PubMed:21276947}. +Q61136 PRP4B_MOUSE Serine/threonine-protein kinase PRP4 homolog (EC 2.7.11.1) (PRP4 pre-mRNA-processing factor 4 homolog) (Pre-mRNA protein kinase) 1007 116,976 Active site (1); Binding site (1); Chain (1); Compositional bias (2); Cross-link (8); Domain (1); Initiator methionine (1); Modified residue (40); Nucleotide binding (1); Sequence conflict (5) FUNCTION: Has a role in pre-mRNA splicing. Phosphorylates SF2/ASF. PTM: Phosphorylated by Clk1. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Identified in the spliceosome C complex (By similarity). Interacts with Clk1 C-terminus. {ECO:0000250}. +Q9CS42 PRPS2_MOUSE Ribose-phosphate pyrophosphokinase 2 (EC 2.7.6.1) (Phosphoribosyl pyrophosphate synthase II) (PRS-II) 318 34,786 Binding site (1); Chain (1); Metal binding (4); Nucleotide binding (1); Region (1) Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I): step 1/1. FUNCTION: Catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP) that is essential for nucleotide synthesis. SUBUNIT: Homodimer. The active form is probably a hexamer composed of 3 homodimers (By similarity). {ECO:0000250}. +P15499 PRPH2_MOUSE Peripherin-2 (Retinal degeneration slow protein) 346 39,260 Chain (1); Glycosylation (2); Region (1); Topological domain (5); Transmembrane (4) TRANSMEM 25 43 Helical. {ECO:0000255}.; TRANSMEM 62 80 Helical. {ECO:0000255}.; TRANSMEM 100 123 Helical. {ECO:0000255}.; TRANSMEM 265 290 Helical. {ECO:0000255}. TOPO_DOM 1 24 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 44 61 Lumenal. {ECO:0000255}.; TOPO_DOM 81 99 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 124 264 Lumenal. {ECO:0000255}.; TOPO_DOM 291 346 Cytoplasmic. {ECO:0000255}. FUNCTION: May function as an adhesion molecule involved in stabilization and compaction of outer segment disks or in the maintenance of the curvature of the rim. It is essential for disk morphogenesis. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SUBUNIT: Homodimer; disulfide-linked. Probably forms a complex with a ROM1 homodimer. Other proteins could associate with this complex in rods. Interacts with MREG. {ECO:0000269|PubMed:17260955}. TISSUE SPECIFICITY: Retina (photoreceptor). In rim region of ROS (rod outer segment) disks. DISEASE: Note=Responsible for retinal degeneration slow (Rds) (PubMed:8530028). {ECO:0000269|PubMed:8530028}. +E9PYL2 PRR12_MOUSE Proline-rich protein 12 2035 211,876 Chain (1); Compositional bias (4); DNA binding (2); Modified residue (16) SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26163108}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000269|PubMed:26163108}. Cell junction, synapse, synaptosome {ECO:0000269|PubMed:26163108}. Note=A smaller form of approximately 150 kDa has been found in perisynapse, synaptosomes and postsynaptic density in E15, P1 and adult brains. {ECO:0000269|PubMed:26163108}. TISSUE SPECIFICITY: Expressed in brain. {ECO:0000269|PubMed:26163108}. +B2RU40 PRRT4_MOUSE Proline-rich transmembrane protein 4 902 93,979 Chain (1); Compositional bias (4); Modified residue (1); Sequence conflict (2); Signal peptide (1); Transmembrane (5) TRANSMEM 371 391 Helical. {ECO:0000255}.; TRANSMEM 393 413 Helical. {ECO:0000255}.; TRANSMEM 432 452 Helical. {ECO:0000255}.; TRANSMEM 468 488 Helical. {ECO:0000255}.; TRANSMEM 501 521 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +A2AFE9 PRR32_MOUSE Proline-rich protein 32 284 30,901 Chain (1); Compositional bias (1); Erroneous initiation (1) +Q8C494 PRR33_MOUSE Proline-rich protein 33 260 28,520 Chain (1); Compositional bias (1) +O35449 PRRT1_MOUSE Proline-rich transmembrane protein 1 (Dispanin subfamily D member 1) (DSPD1) (Synapse differentiation-induced protein 4) 306 31,389 Chain (1); Compositional bias (5); Topological domain (3); Transmembrane (2) TRANSMEM 224 244 Helical. {ECO:0000255}.; TRANSMEM 276 296 Helical. {ECO:0000255}. TOPO_DOM 1 223 Extracellular. {ECO:0000255}.; TOPO_DOM 245 275 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 297 306 Extracellular. {ECO:0000255}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:22632720}; Multi-pass membrane protein {ECO:0000305|PubMed:22632720}. Cell junction, synapse {ECO:0000305|PubMed:22632720}. SUBUNIT: Component of the outer core of AMPAR complex. AMPAR complex consists of an inner core made of 4 pore-forming GluA/GRIA proteins (GRIA1, GRIA2, GRIA3 and GRIA4) and 4 major auxiliary subunits arranged in a twofold symmetry. One of the two pairs of distinct binding sites is occupied either by CNIH2, CNIH3 or CACNG2, CACNG3. The other harbors CACNG2, CACNG3, CACNG4, CACNG8 or GSG1L. This inner core of AMPAR complex is complemented by outer core constituents binding directly to the GluA/GRIA proteins at sites distinct from the interaction sites of the inner core constituents. Outer core constituents include at least PRRT1, PRRT2, CKAMP44/SHISA9, FRRS1L and NRN1. The proteins of the inner and outer core serve as a platform for other, more peripherally associated AMPAR constituents. Alone or in combination, these auxiliary subunits control the gating and pharmacology of the AMPAR complex and profoundly impact their biogenesis and protein processing. {ECO:0000269|PubMed:22632720}. TISSUE SPECIFICITY: Expressed in the brain (at protein level). {ECO:0000269|PubMed:22632720}. +Q9D9M0 PRS52_MOUSE Serine protease 52 (EC 3.4.21.-) (Testicular-specific serine protease 3) 321 35,883 Active site (3); Chain (1); Disulfide bond (4); Domain (1); Erroneous initiation (1); Glycosylation (1); Sequence conflict (1); Signal peptide (1); Transmembrane (1) TRANSMEM 300 320 Helical. {ECO:0000255}. FUNCTION: Probable serine protease. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q14BX2 PRS55_MOUSE Serine protease 55 (EC 3.4.21.-) 321 36,057 Active site (3); Chain (1); Disulfide bond (4); Domain (1); Glycosylation (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 294 314 Helical. {ECO:0000255}. TOPO_DOM 17 293 Extracellular. {ECO:0000255}.; TOPO_DOM 315 321 Cytoplasmic. {ECO:0000255}. FUNCTION: Probable serine protease. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q9QYZ9 PRS30_MOUSE Serine protease 30 (EC 3.4.21.-) (Distal intestinal serine protease) (Transmembrane serine protease 8) 310 33,707 Active site (3); Chain (1); Disulfide bond (4); Domain (1); Glycosylation (2); Lipidation (1); Propeptide (2); Sequence conflict (1); Signal peptide (1) FUNCTION: Selectively cleaves synthetic peptide substrates of trypsin. Activates the epithelial sodium channel ENaC (By similarity). {ECO:0000250|UniProtKB:P83748}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}. TISSUE SPECIFICITY: Expressed primarily in distal gut. {ECO:0000269|PubMed:10786627}. +Q3UKY7 PRS38_MOUSE Serine protease 38 (EC 3.4.21.-) (Marapsin-2) 322 35,698 Active site (3); Chain (1); Disulfide bond (4); Domain (1); Glycosylation (3); Propeptide (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q52KR3 PRUN2_MOUSE Protein prune homolog 2 (BNIP2 motif-containing molecule at the C-terminal region 1) 3084 339,516 Alternative sequence (6); Chain (1); Domain (1); Erroneous initiation (3); Modified residue (1); Motif (1); Sequence conflict (6) FUNCTION: May play an important role in regulating differentiation, survival and aggressiveness of the tumor cells. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +P32848 PRVA_MOUSE Parvalbumin alpha 110 11,931 Calcium binding (2); Chain (1); Domain (2); Initiator methionine (1); Mass spectrometry (1); Modified residue (4); Sequence conflict (2) FUNCTION: In muscle, parvalbumin is thought to be involved in relaxation after contraction. It binds two calcium ions. +Q9D600 PSF2_MOUSE DNA replication complex GINS protein PSF2 (GINS complex subunit 2) 185 21,236 Chain (1); Cross-link (1); Modified residue (3); Sequence conflict (2) FUNCTION: The GINS complex plays an essential role in the initiation of DNA replication, and progression of DNA replication forks. GINS complex seems to bind preferentially to single-stranded DNA (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the GINS complex which is a heterotetramer of GINS1, GINS2, GINS3 and GINS4. Forms a stable subcomplex with GINS3. GINS complex interacts with DNA primase in vitro (By similarity). {ECO:0000250}. +Q8BHL8 PSMF1_MOUSE Proteasome inhibitor PI31 subunit 271 29,664 Chain (1); Compositional bias (1); Initiator methionine (1); Modified residue (7); Region (1); Sequence conflict (1) FUNCTION: Plays an important role in control of proteasome function. Inhibits the hydrolysis of protein and peptide substrates by the 20S proteasome. Also inhibits the activation of the proteasome by the proteasome regulatory proteins PA700 and PA28 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. SUBUNIT: Monomer and homodimer. Interacts with FBXO7 (By similarity). {ECO:0000250}. +Q0EEE2 PTHD3_MOUSE Patched domain-containing protein 3 (RND-type protein RNDEu-3) 906 101,813 Alternative sequence (2); Chain (1); Domain (1); Glycosylation (2); Transmembrane (11) TRANSMEM 338 358 Helical. {ECO:0000255}.; TRANSMEM 370 390 Helical. {ECO:0000255}.; TRANSMEM 392 412 Helical. {ECO:0000255}.; TRANSMEM 442 462 Helical. {ECO:0000255}.; TRANSMEM 476 496 Helical. {ECO:0000255}.; TRANSMEM 559 579 Helical. {ECO:0000255}.; TRANSMEM 760 780 Helical. {ECO:0000255}.; TRANSMEM 782 802 Helical. {ECO:0000255}.; TRANSMEM 814 834 Helical. {ECO:0000255}.; TRANSMEM 848 868 Helical. {ECO:0000255}.; TRANSMEM 883 903 Helical. {ECO:0000255}. FUNCTION: May play a role in sperm development or sperm function. {ECO:0000269|PubMed:17904097}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=Localizes to the midpiece of the sperm tail. {ECO:0000269|PubMed:17904097}. TISSUE SPECIFICITY: Expressed in germ cells of the testis (at protein level). {ECO:0000269|PubMed:17904097}. +Q8BW00 PTH_MOUSE Probable peptidyl-tRNA hydrolase (PTH) (EC 3.1.1.29) 204 22,161 Chain (1) +Q6VMN6 PRLHR_MOUSE Prolactin-releasing peptide receptor (PrRP receptor) (PrRPR) (G-protein coupled receptor 10) 370 41,182 Chain (1); Disulfide bond (1); Glycosylation (2); Region (1); Sequence conflict (3); Topological domain (8); Transmembrane (7) TRANSMEM 63 83 Helical; Name=1. {ECO:0000255}.; TRANSMEM 102 122 Helical; Name=2. {ECO:0000255}.; TRANSMEM 127 147 Helical; Name=3. {ECO:0000255}.; TRANSMEM 176 196 Helical; Name=4. {ECO:0000255}.; TRANSMEM 224 244 Helical; Name=5. {ECO:0000255}.; TRANSMEM 277 297 Helical; Name=6. {ECO:0000255}.; TRANSMEM 318 338 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 62 Extracellular. {ECO:0000255}.; TOPO_DOM 84 101 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 123 126 Extracellular. {ECO:0000255}.; TOPO_DOM 148 175 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 197 223 Extracellular. {ECO:0000255}.; TOPO_DOM 245 276 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 298 317 Extracellular. {ECO:0000255}.; TOPO_DOM 339 370 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for prolactin-releasing peptide (PrRP). Implicated in lactation, regulation of food intake and pain-signal processing. {ECO:0000269|PubMed:14742914}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBUNIT: Interacts through its C-terminal region with the PDZ domain-containing proteins GRIP1, GRIP2 and PICK1. Interacts with PDZ domains 4 and 5 of GRIP1 and with the PDZ domain of PICK1 (By similarity). {ECO:0000250}. +O35730 RING1_MOUSE E3 ubiquitin-protein ligase RING1 (EC 2.3.2.27) (Polycomb complex protein RING1) (RING finger protein 1) (RING-type E3 ubiquitin transferase RING1) (Transcription repressor Ring1A) 406 42,631 Alternative sequence (3); Chain (1); Compositional bias (2); Erroneous initiation (1); Modified residue (10); Motif (1); Region (2); Sequence conflict (6); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: Constitutes one of the E3 ubiquitin-protein ligases that mediate monoubiquitination of 'Lys-119' of histone H2A, thereby playing a central role in histone code and gene regulation. H2A 'Lys-119' ubiquitination gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. Essential component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones, rendering chromatin heritably changed in its expressibility. Compared to RNF2/RING2, it does not have the main E3 ubiquitin ligase activity on histone H2A, and it may rather act as a modulator of RNF2/RING2 activity (By similarity). {ECO:0000250, ECO:0000269|PubMed:15525528, ECO:0000269|PubMed:16710298, ECO:0000269|PubMed:9312051}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}. SUBUNIT: Component of chromatin-associated Polycomb (PcG) complexes. Part of the E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1, RING1, RNF2/RING2 MBLR, L3MBTL2 and YAF2. Interacts with CBX2 and PCGF6. Component of a PRC1-like complex. Component of repressive BCOR complex containing Polycomb group subcomplex at least composed of RYBP, PCGF1, BCOR and RNF2/RING2. Interacts with PHC2, PCGF2, RNF2; CBX6, CBX7 and CBX8. Interacts with BMI1 (By similarity). {ECO:0000250}. +Q922R0 PRKX_MOUSE cAMP-dependent protein kinase catalytic subunit PRKX (PrKX) (Protein kinase X) (Protein kinase X-linked) (Serine/threonine-protein kinase PRKX) (EC 2.7.11.1) (PKA-related protein kinase) 355 40,467 Active site (1); Binding site (1); Chain (1); Domain (2); Modified residue (2); Nucleotide binding (1); Sequence conflict (2) FUNCTION: Serine/threonine protein kinase regulated by and mediating cAMP signaling in cells. Acts through phosphorylation of downstream targets that may include CREB, SMAD6 and PKD1 and has multiple functions in cellular differentiation and epithelial morphogenesis. Regulates myeloid cell differentiation through SMAD6 phosphorylation. Involved in nephrogenesis by stimulating renal epithelial cell migration and tubulogenesis. Also involved in angiogenesis through stimulation of endothelial cell proliferation, migration and vascular-like structure formation. {ECO:0000269|PubMed:16236808, ECO:0000269|PubMed:19367327, ECO:0000269|PubMed:21684272}. PTM: Phosphorylated; autophosphorylates in vitro. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=cAMP induces nuclear translocation. {ECO:0000250}. SUBUNIT: Like other cAMP-dependent protein kinases, the inactive holoenzyme is probably composed of 2 PRKX catalytic subunits and a dimer of regulatory subunits. Interacts (cAMP-dependent) specifically with the regulatory subunits PRKAR1A and PRKAR1B. Compared to other cAMP-dependent serine/threonine protein kinases, does not interact with the 2 other PKA regulatory subunits PRKAR2A and PRKAR2B. Interacts with PIN1 (via WW domain). Interacts with cAMP-dependent protein kinase inhibitor/PKI proteins; inhibits PRKX (By similarity). Interacts with GPKOW (By similarity). Interacts with SMAD6 (By similarity). Interacts with PKD1; involved in differentiation and controlled morphogenesis of the kidney (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10729225}. +Q9CQJ4 RING2_MOUSE E3 ubiquitin-protein ligase RING2 (EC 2.3.2.27) (RING finger protein 1B) (RING1b) (RING finger protein 2) (RING-type E3 ubiquitin transferase RING2) 336 37,623 Beta strand (4); Chain (1); Cross-link (3); Helix (5); Initiator methionine (1); Modified residue (4); Region (2); Sequence conflict (4); Turn (3); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that mediates monoubiquitination of 'Lys-119' of histone H2A (H2AK119Ub), thereby playing a central role in histone code and gene regulation (PubMed:15525528, PubMed:22325148, PubMed:28596365). H2AK119Ub gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals (PubMed:15525528, PubMed:28596365). May be involved in the initiation of both imprinted and random X inactivation (PubMed:15525528). Essential component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development (PubMed:22325148, PubMed:16710298). PcG PRC1 complex acts via chromatin remodeling and modification of histones, rendering chromatin heritably changed in its expressibility (PubMed:15525528, PubMed:22325148, PubMed:16710298). E3 ubiquitin-protein ligase activity is enhanced by BMI1/PCGF4 (PubMed:16710298). Acts as the main E3 ubiquitin ligase on histone H2A of the PRC1 complex, while RING1 may rather act as a modulator of RNF2/RING2 activity (PubMed:15525528, PubMed:16710298). Plays a role in the transcriptional repression of genes that are required for pluripotency in embryonic stem cells, thereby contributing to differentiation of the ectodermal and endodermal germ layers (PubMed:22226355). Association with the chromosomal DNA is cell-cycle dependent. In resting B- and T-lymphocytes, interaction with AURKB leads to block its activity, thereby maintaining transcription in resting lymphocytes (PubMed:24034696). {ECO:0000269|PubMed:12183370, ECO:0000269|PubMed:15525528, ECO:0000269|PubMed:16710298, ECO:0000269|PubMed:22226355, ECO:0000269|PubMed:22325148, ECO:0000269|PubMed:24034696, ECO:0000269|PubMed:28596365}. PTM: Polyubiquitinated in the presence of UBE2D3 (in vitro).; PTM: Monoubiquitinated, by auto-ubiquitination. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12183370, ECO:0000269|PubMed:22325148}. Chromosome {ECO:0000269|PubMed:12183370, ECO:0000269|PubMed:22325148}. Note=Enriched on inactive X chromosome (Xi) in female trophoblast stem (TS) cells as well as differentiating embryonic stem (ES) cells. The enrichment on Xi is transient during TS and ES cell differentiation. The association with Xi is mitotically stable in non-differentiated TS cells. {ECO:0000269|PubMed:12183370}. SUBUNIT: Component of chromatin-associated Polycomb (PcG) complexes (PubMed:22325148). Component of a number of PRC1-like complexes; these complexes contain either the polycomb group ring finger protein PCGF1, or PCGF2, or PCGF3, or BMI1, or PCGF5, or PCGF6 (PubMed:28596365, PubMed:16710298). Distinct PRC1-like complexes are composed of a RING1 subunit (RING1B or RING1A), one of the six PCGF proteins (PCGF1, PCGF2, PCGF3, BMI1, PCGF5 or PCGF6), one PHC protein (PHC1, PHC2 or PHC3) and one of the CBX proteins (CBX2, CBX4, CBX6, CBX7 or CBX8) (Probable). Part of a complex that contains RNF2, UB2D3 and BMI1; within that complex RNF2 and BMI1 form a tight heterodimer, where UB2D3 interacts only with RNF2. The complex composed of RNF2, UB2D3 and BMI1 binds nucleosomes, and has activity only with nucleosomal histone H2A (By similarity). Part of a complex that contains PCGF5, RNF2 and UBE2D3. Part of a complex that contains AUTS2, PCGF5, RNF2, CSNK2B AND RYBP (By similarity). Interacts with CBX6 and CBX8 (By similarity). Interacts with PHC1, PCGF2, RYBP, CBX7, CBX4, CBX2, RNF1/RING1, BMI1 and PHC2 (PubMed:12183370, PubMed:16024804, PubMed:16710298, PubMed:19170609, PubMed:9312051, PubMed:10369680, PubMed:22325148, PubMed:22226355). Interaction with RYBP and CBX7 is mutually exclusive; both compete for the same binding site on RNF2 (PubMed:22325148). Component of repressive BCOR complex containing a Polycomb group subcomplex at least composed of RYBP, PCGF1, BCOR and RING1 (By similarity). Interacts with CBX2 and PHC1 (PubMed:22226355). Interacts with CHTOP (PubMed:22872859). Interacts with AURKB (PubMed:24034696). Part of the E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1, RNF1/RING1, RNF2/RING2, MBLR, L3MBTL2 and YAF2 (By similarity). Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Interacts with RYBP, HIP2 and TFCP2 (By similarity). {ECO:0000250|UniProtKB:Q99496, ECO:0000269|PubMed:10369680, ECO:0000269|PubMed:12183370, ECO:0000269|PubMed:16024804, ECO:0000269|PubMed:16710298, ECO:0000269|PubMed:19170609, ECO:0000269|PubMed:22226355, ECO:0000269|PubMed:22325148, ECO:0000269|PubMed:22872859, ECO:0000269|PubMed:24034696, ECO:0000269|PubMed:28596365, ECO:0000269|PubMed:9312051, ECO:0000305}. TISSUE SPECIFICITY: Expressed in embryonic stem cells. {ECO:0000269|PubMed:22226355}. +Q8R107 PRLD1_MOUSE PRELI domain-containing protein 1, mitochondrial (Px19-like protein) 217 24,960 Chain (1); Domain (1); Sequence conflict (1); Transit peptide (1) FUNCTION: Involved in the modulation of the mitochondrial apoptotic pathway by ensuring the accumulation of cardiolipin (CL) in mitochondrial membranes. In vitro, the TRIAP1:PRELID1 complex mediates the transfer of phosphatidic acid (PA) between liposomes and probably functions as a PA transporter across the mitochondrion intermembrane space to provide PA for CL synthesis in the inner membrane. Regulates the mitochondrial apoptotic pathway in primary Th cells. Regulates Th cell differentiation by down-regulating STAT6 thereby reducing IL-4-induced Th2 cell number. May be important for the development of vital and immunocompetent organs (By similarity). {ECO:0000250|UniProtKB:Q9Y255, ECO:0000269|PubMed:21364629}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14640972}. Mitochondrion intermembrane space {ECO:0000250|UniProtKB:Q9Y255}. SUBUNIT: Forms a complex with TRIAP1 in the mitochondrion intermembrane space. Interacts with OPA1 and AIFM1 (By similarity). {ECO:0000250|UniProtKB:Q9Y255, ECO:0000269|PubMed:21364629}. TISSUE SPECIFICITY: Abundantly expressed in all tissues tested except testis with highest levels in thymus. {ECO:0000269|PubMed:14640972}. +Q8BZ36 RINT1_MOUSE RAD50-interacting protein 1 (RAD50 interactor 1) (RINT-1) 792 90,094 Alternative sequence (1); Chain (1); Coiled coil (1); Domain (1); Frameshift (1); Sequence conflict (3) FUNCTION: Involved in regulation of membrane traffic between the Golgi and the endoplasmic reticulum; the function is proposed to depend on its association in the NRZ complex which is believed to play a role in SNARE assembly at the ER. May play a role in cell cycle checkpoint control. Essential for telomere length control (By similarity). {ECO:0000250|UniProtKB:Q6NUQ1}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6NUQ1}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q6NUQ1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q6NUQ1}. SUBUNIT: Component of the NRZ complex composed of NBAS, ZW10 and RINT1/TIP20L; NRZ associates with SNAREs STX18, USE1L, BNIP1/SEC20L and SEC22B (the assembly has been described as syntaxin 18 complex). Interacts directly with BNIP1/SEC20L and ZW10. Interacts with RAD50 during late S and G2/M phases. Interacts with RBL2, preferentially with the active, hypophosphorylated form (By similarity). {ECO:0000250|UniProtKB:Q6NUQ1}. +Q9D6I3 PROF4_MOUSE Profilin-4 (Profilin IV) 129 14,416 Chain (1) FUNCTION: Binds to phosphatidylinositol 3-phosphate (PtdIns(3)P), phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), phosphatidylinositol 4-phosphate (PtdIns(4)P) and phosphatidic acid (PA). Does not bind to actin, contrary to other family members (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. TISSUE SPECIFICITY: Detected in testis (at protein level). {ECO:0000269|PubMed:15591451}. +Q99KP6 PRP19_MOUSE Pre-mRNA-processing factor 19 (EC 2.3.2.27) (Nuclear matrix protein 200) (PRP19/PSO4 homolog) (RING-type E3 ubiquitin transferase PRP19) (Senescence evasion factor) 504 55,239 Alternative sequence (2); Chain (1); Domain (1); Initiator methionine (1); Modified residue (5); Region (1); Repeat (7) Protein modification; protein ubiquitination. FUNCTION: Isoform 1: Ubiquitin-protein ligase which is a core component of several complexes mainly involved in pre-mRNA splicing and DNA repair. Core component of the PRP19C/Prp19 complex/NTC/Nineteen complex which is part of the spliceosome and participates in its assembly, its remodeling and is required for its activity. During assembly of the spliceosome, mediates 'Lys-63'-linked polyubiquitination of the U4 spliceosomal protein PRPF3. Ubiquitination of PRPF3 allows its recognition by the U5 component PRPF8 and stabilizes the U4/U5/U6 tri-snRNP spliceosomal complex. Recruited to RNA polymerase II C-terminal domain (CTD) and the pre-mRNA, it may also couple the transcriptional and spliceosomal machineries. The XAB2 complex, which contains PRPF19, is also involved in pre-mRNA splicing, transcription and transcription-coupled repair. Beside its role in pre-mRNA splicing PRPF19, as part of the PRP19-CDC5L complex, plays a role in the DNA damage response/DDR. It is recruited to the sites of DNA damage by the RPA complex where PRPF19 directly ubiquitinates RPA1 and RPA2. 'Lys-63'-linked polyubiquitination of the RPA complex allows the recruitment of the ATR-ATRIP complex and the activation of ATR, a master regulator of the DNA damage response. May also play a role in DNA double-strand break (DSB) repair by recruiting the repair factor SETMAR to altered DNA. As part of the PSO4 complex may also be involved in the DNA interstrand cross-links/ICLs repair process. In addition, may also mediate 'Lys-48'-linked polyubiquitination of substrates and play a role in proteasomal degradation (PubMed:17349974). May play a role in the biogenesis of lipid droplets (PubMed:17118936). May play a role in neural differentiation possibly through its function as part of the spliceosome (By similarity). {ECO:0000250|UniProtKB:Q9JMJ4, ECO:0000250|UniProtKB:Q9UMS4, ECO:0000269|PubMed:17118936, ECO:0000269|PubMed:17349974}.; FUNCTION: Isoform 2: Forced expression leads to suppression of neuronal differentiation, and on the contrary to stimulation of astroglial cell differentiation in retinoic acid-primed P19 cells (PubMed:16352598). {ECO:0000269|PubMed:16352598}. SUBCELLULAR LOCATION: Isoform 1: Nucleus {ECO:0000269|PubMed:16352598}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9UMS4}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9UMS4}. Cytoplasm {ECO:0000250|UniProtKB:Q9UMS4}. Lipid droplet {ECO:0000269|PubMed:17118936}. Note=Nucleoplasmic in interphase cells. Irregularly distributed in anaphase cells. In prophase cells, uniformly distributed, but not associated with condensing chromosomes. Found in extrachromosomal regions in metaphase cells. Mainly localized to the mitotic spindle apparatus when chromosomes segregate during anaphase. When nuclei reform during late telophase, uniformly distributed in daughter cells and displays no preferred association with decondensing chromatin. Recruited on damaged DNA at sites of double-strand break (By similarity). {ECO:0000250|UniProtKB:Q9UMS4}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm {ECO:0000269|PubMed:16352598}. Nucleus {ECO:0000269|PubMed:16352598}. SUBUNIT: Homotetramer. Component of the Prp19 complex/PRP19C/Nineteen complex/NTC and related complexes described as PRP19-CDC5L splicing complex and PSO4 complex. A homotetramer of PRPF19, CDC5L, PLRG1 and BCAS2 constitute the core of those complexes. The interaction with CDC5L, PLRG1 and BCAS2 is direct within this core complex. At least three less stably associated proteins CTNNBL1, CWC15 and HSPA8 are found in the Prp19 complex. The Prp19 complex associates with the spliceosome during its assembly and remodeling recruiting additional proteins. Component of the XAB2 complex, a multimeric protein complex composed of XAB2, PRPF19, AQR, ZNF830, ISY1, and PPIE. Interacts with CWC22 and EIF4A3 in an RNA-independent manner. Interacts with RPA1 and RPA2; the PRP19-CDC5L complex is recruited to the sites of DNA repair where it interacts with the replication protein A complex (RPA). Interacts with SETMAR; required for SETMAR recruitment to site of DNA damage. Interacts with U2AF2; the interaction is direct and recruits the Prp19 complex to RNA polymerase II C-terminal domain (CTD) and the pre-mRNA. Interacts with PRPF3. Interacts with APEX1, DNTT and PSMB4. Interacts with KNSTRN (By similarity). Interacts with PSMC5 (PubMed:17349974). Isoform 2 (via N-terminus) interacts with PPIA. Isoform 2 does not interact with CDC5L (PubMed:16352598). Interacts with KHDC4 (By similarity). {ECO:0000250|UniProtKB:Q9UMS4, ECO:0000269|PubMed:16352598, ECO:0000269|PubMed:17349974}. DOMAIN: The 7 WD repeats are necessary and sufficient to support interaction with the RPA complex. {ECO:0000250|UniProtKB:Q9UMS4}. TISSUE SPECIFICITY: Expressed in white and brown adipose tissues, brain and to a lower extent in liver, kidney, muscle, lung and spleen (at protein level). {ECO:0000269|PubMed:17118936}. +Q8BII1 PROX2_MOUSE Prospero homeobox protein 2 (Homeobox prospero-like protein PROX2) (PROX-2) 593 65,759 Chain (1); Domain (2); Region (1) FUNCTION: Transcription regulator. Does not seem to be essential for embryonic development and postnatal survival. {ECO:0000269|PubMed:16470382}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. DOMAIN: The Prospero-type homeodomain and the adjacent Prospero domain act as a single structural unit, the Homeo-Prospero domain. {ECO:0000255|PROSITE-ProRule:PRU01162}. TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:16470382}. +Q920S2 PRS41_MOUSE Serine protease 41 (EC 3.4.21.-) (Testis serine protease 1) (TESSP-1) 322 36,218 Active site (3); Alternative sequence (2); Chain (1); Disulfide bond (4); Domain (1); Glycosylation (1); Lipidation (1); Propeptide (2); Sequence conflict (1); Signal peptide (1) PTM: N-glycosylated. {ECO:0000269|PubMed:15515062}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15515062, ECO:0000269|PubMed:19798924}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:15515062, ECO:0000269|PubMed:19798924}. Note=Localized in the plasma membrane of spermatogonia. Localized in intracellular compartment in spermatocytes, probably in the Golgi apparatus. TISSUE SPECIFICITY: Testis-specific. Expressed in spermatogonia and spermatocytes. Expressed in Leydig and Sertoli cells (at protein level). Expressed 2 weeks after birth and remains highly expressed in the sexually mature testis. Expressed in the seminiferous tubules but not in the interstitial tissues. Expressed in type B spermatogonia and spermatocytes at stages between preleptotene and pachytene during the spermatogenesis cycle. {ECO:0000269|PubMed:15515062, ECO:0000269|PubMed:19798924}. +Q8VIF2 PRS42_MOUSE Serine protease 42 (EC 3.4.21.-) (Testis serine protease 2) 335 36,683 Active site (3); Chain (1); Compositional bias (1); Disulfide bond (4); Domain (1); Glycosylation (3); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|Ref.1}. +Q8K4I7 PRS45_MOUSE Inactive serine protease 45 (Inactive testis serine protease 5) (Trypsin-like protease p98) 317 35,723 Alternative sequence (1); Chain (1); Compositional bias (1); Disulfide bond (4); Domain (1); Glycosylation (3); Sequence conflict (3); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q99PW4 PRPK_MOUSE EKC/KEOPS complex subunit Tp53rk (EC 3.6.-.-) (Atypical serine/threonine protein kinase Tp53rk) (Nori-2) (TP53-regulating kinase) (EC 2.7.11.1) (p53-related protein kinase) 244 27,394 Active site (1); Binding site (1); Chain (1); Domain (1); Frameshift (1); Modified residue (1); Motif (1); Nucleotide binding (1); Sequence conflict (3) FUNCTION: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. TP53RK has ATPase activity in the context of the EKC/KEOPS complex and likely plays a supporting role to the catalytic subunit OSGEP (By similarity). Atypical protein kinase that phosphorylates 'Ser-15' of p53/TP53 protein and may therefore participate in its activation (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P53323, ECO:0000250|UniProtKB:Q96S44, ECO:0000250|UniProtKB:Q9UYB9}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96S44}. SUBUNIT: Component of the EKC/KEOPS complex composed of at least GON7, TP53RK, TPRKB, OSGEP and LAGE3; the whole complex dimerizes. {ECO:0000250|UniProtKB:Q96S44}. DOMAIN: This protein is considered an atypical serine/threonine kinase, because it lacks the conventional structural elements necessary for the substrate recognition as well as a lysine residue that in all other serine/threonine kinases participates in the catalytic event. TP53RK has protein kinase activity in vitro, but in the context of the EKC/KEOPS complex, the catalytic subunit OSGEP switches the activity of TP53RK from kinase into ATPase (By similarity). {ECO:0000250|UniProtKB:P53323, ECO:0000250|UniProtKB:Q9UYB9}. +Q14B25 PRS48_MOUSE Serine protease 48 (EC 3.4.21.-) (Epidermis-specific serine protease-like protein) 312 34,637 Active site (3); Chain (1); Disulfide bond (4); Domain (1); Glycosylation (2); Sequence conflict (4); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +P62192 PRS4_MOUSE 26S proteasome regulatory subunit 4 (P26s4) (26S proteasome AAA-ATPase subunit RPT2) (Proteasome 26S subunit ATPase 1) 440 49,185 Chain (1); Cross-link (1); Initiator methionine (1); Lipidation (1); Modified residue (5); Nucleotide binding (1) FUNCTION: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. PSMC1 belongs to the heterohexameric ring of AAA (ATPases associated with diverse cellular activities) proteins that unfolds ubiquitinated target proteins that are concurrently translocated into a proteolytic chamber and degraded into peptides. {ECO:0000250|UniProtKB:P62191}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Membrane {ECO:0000250|UniProtKB:P62191}; Lipid-anchor {ECO:0000250|UniProtKB:P62191}. SUBUNIT: Component of the 19S proteasome regulatory particle complex. The 26S proteasome consists of a 20S core particle (CP) and two 19S regulatory subunits (RP). The regulatory particle is made of a lid composed of 9 subunits, a base containing 6 ATPases including PSMC1 and few additional components. Interacts with SCA7. Interacts with NGLY1. Interacts with PAAF1. {ECO:0000250|UniProtKB:P62191, ECO:0000269|PubMed:11562482, ECO:0000269|PubMed:15358861, ECO:0000269|PubMed:16249333, ECO:0000269|PubMed:16709668, ECO:0000269|PubMed:16857966}. +Q571E5 PRS53_MOUSE Serine protease 53 (EC 3.4.21.-) (Polyserine protease 3) (Polyserase-3) 552 58,974 Active site (6); Chain (1); Disulfide bond (7); Domain (2); Erroneous initiation (2); Signal peptide (1) FUNCTION: In vitro can degrade the fibrinogen alpha chain of as well as pro-urokinase-type plasminogen activator. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +Q924N9 PRS28_MOUSE Serine protease 28 (EC 3.4.21.-) (Implantation serine proteinase 1) (ISP-1) (Strypsin) (Tryptase-like proteinase) 274 30,628 Active site (3); Chain (1); Disulfide bond (4); Domain (1); Glycosylation (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Involved in embryo hatching and implantation. {ECO:0000269|PubMed:11425330, ECO:0000269|PubMed:15293213, ECO:0000269|PubMed:17156484}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Note=Secretion into the glandular and uterine lumen may occur as a consequence of progesterone-induced epithelial differentiation. {ECO:0000269|PubMed:12112596, ECO:0000269|PubMed:15349836}. SUBUNIT: Homooligomer, heterodimer and heterotetramer. Able to form homo- and hetero- tetrameric structures. Heterotetramer is far more stable than the homotetramer. {ECO:0000269|PubMed:12112596, ECO:0000269|PubMed:15293213, ECO:0000269|PubMed:15349836, ECO:0000269|PubMed:17156484}. TISSUE SPECIFICITY: Expressed in embryos throughout the preimplantation period, during blastocyst hatching and embryo outgrowth. Found in uterus especially in glandular epithelium. {ECO:0000269|PubMed:11425330, ECO:0000269|PubMed:12112596, ECO:0000269|PubMed:15293213}. +Q9ESD1 PRSS8_MOUSE Prostasin (EC 3.4.21.-) (Channel-activating protease 1) (CAP1) (Serine protease 8) [Cleaved into: Prostasin light chain; Prostasin heavy chain] 342 36,729 Active site (3); Chain (3); Disulfide bond (5); Domain (1); Frameshift (1); Glycosylation (2); Propeptide (2); Signal peptide (1); Transmembrane (1) TRANSMEM 320 340 Helical. {ECO:0000255}. FUNCTION: Possesses a trypsin-like cleavage specificity with a preference for poly-basic substrates (By similarity). Stimulates epithelial sodium channel (ENaC) activity through activating cleavage of the gamma subunits (SCNN1G). {ECO:0000250, ECO:0000269|PubMed:10770960}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: Prostasin: Secreted, extracellular space {ECO:0000250}.; SUBCELLULAR LOCATION: Prostasin light chain: Secreted, extracellular space {ECO:0000250}. Note=Found in the seminal fluid. Secreted after cleavage of its C-terminus. {ECO:0000250}.; SUBCELLULAR LOCATION: Prostasin heavy chain: Secreted, extracellular space {ECO:0000250}. Note=Found in the seminal fluid. Secreted after cleavage of its C-terminus. {ECO:0000250}. SUBUNIT: Heterodimer of two chains, light and heavy, held by a disulfide bond. {ECO:0000250}. +P99026 PSB4_MOUSE Proteasome subunit beta type-4 (EC 3.4.25.1) (Low molecular mass protein 3) (Macropain beta chain) (Multicatalytic endopeptidase complex beta chain) (Proteasome beta chain) (Proteasome chain 3) 264 29,116 Beta strand (14); Chain (1); Helix (5); Modified residue (2); Propeptide (1); Sequence conflict (7); Turn (1) FUNCTION: Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). SMAD1/OAZ1/PSMB4 complex mediates the degradation of the CREBBP/EP300 repressor SNIP1. {ECO:0000269|PubMed:12874245, ECO:0000269|PubMed:16581775, ECO:0000269|PubMed:22341445}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P28070}. Nucleus {ECO:0000250|UniProtKB:P28070}. SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is a barrel-shaped complex made of 28 subunits that are arranged in four stacked rings. The two outer rings are each formed by seven alpha subunits, and the two inner rings are formed by seven beta subunits. The proteolytic activity is exerted by three beta-subunits PSMB5, PSMB6 and PSMB7 (PubMed:16857966, PubMed:22341445). Forms a ternary complex with SMAD1 and OAZ1 before PSMB4 is incorporated into the 20S proteasome (By similarity). Interacts with PRPF19 (By similarity). {ECO:0000250|UniProtKB:P28070, ECO:0000269|PubMed:16857966, ECO:0000269|PubMed:22341445}. TISSUE SPECIFICITY: Detected in liver (at protein level). {ECO:0000269|PubMed:22341445}. +Q9R1P3 PSB2_MOUSE Proteasome subunit beta type-2 (EC 3.4.25.1) (Macropain subunit C7-I) (Multicatalytic endopeptidase complex subunit C7-I) (Proteasome component C7-I) 201 22,906 Beta strand (14); Chain (1); Helix (4); Modified residue (1); Turn (1) FUNCTION: Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). {ECO:0000269|PubMed:16581775, ECO:0000269|PubMed:22341445}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P49721}. Nucleus {ECO:0000250|UniProtKB:P49721}. SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is a barrel-shaped complex made of 28 subunits that are arranged in four stacked rings. The two outer rings are each formed by seven alpha subunits, and the two inner rings are formed by seven beta subunits. The proteolytic activity is exerted by three beta-subunits PSMB5, PSMB6 and PSMB7. {ECO:0000269|PubMed:16857966, ECO:0000269|PubMed:22341445}. TISSUE SPECIFICITY: Detected in liver (at protein level). {ECO:0000269|PubMed:22341445}. +Q99JF8 PSIP1_MOUSE PC4 and SFRS1-interacting protein (Lens epithelium-derived growth factor) (mLEDGF) 528 59,697 Alternative sequence (2); Chain (1); Coiled coil (2); Cross-link (1); Domain (1); Modified residue (19); Motif (1); Sequence conflict (1) FUNCTION: Transcriptional coactivator involved in neuroepithelial stem cell differentiation and neurogenesis. Involved in particular in lens epithelial cell gene regulation and stress responses. May play an important role in lens epithelial to fiber cell terminal differentiation. May play a protective role during stress-induced apoptosis (By similarity). {ECO:0000250}. PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with IFRD1/PC4. Interacts POGZ and CDCA7L (By similarity). Murine leukemia virus (MLV) integrase does not interact with PSIP1. {ECO:0000250}. +P61290 PSME3_MOUSE Proteasome activator complex subunit 3 (11S regulator complex subunit gamma) (REG-gamma) (Activator of multicatalytic protease subunit 3) (Ki nuclear autoantigen) (Proteasome activator 28 subunit gamma) (PA28g) (PA28gamma) 254 29,506 Chain (1); Initiator methionine (1); Modified residue (5); Sequence conflict (6) FUNCTION: Subunit of the 11S REG-gamma (also called PA28-gamma) proteasome regulator, a doughnut-shaped homoheptamer which associates with the proteasome. 11S REG-gamma activates the trypsin-like catalytic subunit of the proteasome but inhibits the chymotrypsin-like and postglutamyl-preferring (PGPH) subunits. Facilitates the MDM2-p53/TP53 interaction which promotes ubiquitination- and MDM2-dependent proteasomal degradation of p53/TP53, limiting its accumulation and resulting in inhibited apoptosis after DNA damage. May also be involved in cell cycle regulation. Mediates CCAR2 and CHEK2-dependent SIRT1 inhibition (By similarity). {ECO:0000250|UniProtKB:P61289}. PTM: Phosphorylated by MAP3K3. Phosphorylation at Ser-247 promotes its association with CCAR2 (By similarity). {ECO:0000250|UniProtKB:P61289, ECO:0000269|PubMed:12650640}.; PTM: Acetylation at the major site Lys-195 is important for oligomerization and ability to degrade its target substrates. Deacetylated by SIRT1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12650640}. Cytoplasm {ECO:0000269|PubMed:12650640}. Note=Localizes to the cytoplasm during mitosis following nuclear envelope breakdown at this distinct stage of the cell cycle which allows its interaction with MAP3K3 kinase. SUBUNIT: Homoheptamer; the stability of the heptamer is essential for the specific activation of the trypsine-like subunit and inhibition of the chymotrypsin-like and postglutamyl-preferring (PGPH) subunits of the proteasome (By similarity). Interacts with p53/TP53 and MDM2 (By similarity). Interacts with MAP3K3 (PubMed:12650640). Associates with the proteasome (By similarity). Interacts with CCAR2 (By similarity). Interacts with FAM192A (via C-terminus); the interaction is direct and promotes the association of PSME3 with the 20S proteasome (By similarity). Interacts with COIL; the interaction is inhibited by FAM192A (By similarity). {ECO:0000250|UniProtKB:P61289, ECO:0000269|PubMed:12650640}. DOMAIN: The C-terminal sequences affect heptamer stability and proteasome affinity. {ECO:0000250}. +Q5SSW2 PSME4_MOUSE Proteasome activator complex subunit 4 (Proteasome activator PA200) (Protein TEMO) 1843 211,197 Alternative sequence (1); Chain (1); Erroneous initiation (1); Frameshift (1); Modified residue (3); Region (1); Repeat (6); Sequence conflict (25) FUNCTION: Associated component of the proteasome that specifically recognizes acetylated histones and promotes ATP- and ubiquitin-independent degradation of core histones during spermatogenesis and DNA damage response. Recognizes and binds acetylated histones via its bromodomain-like (BRDL) region and activates the proteasome by opening the gated channel for substrate entry. Binds to the core proteasome via its C-terminus, which occupies the same binding sites as the proteasomal ATPases, opening the closed structure of the proteasome via an active gating mechanism. Component of the spermatoproteasome, a form of the proteasome specifically found in testis: binds to acetylated histones and promotes degradation of histones, thereby participating actively to the exchange of histones during spermatogenesis. Also involved in DNA damage response in somatic cells, by promoting degradation of histones following DNA double-strand breaks. {ECO:0000269|PubMed:16581775, ECO:0000269|PubMed:23706739}. PTM: Phosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol. Nucleus. Nucleus speckle {ECO:0000250}. Note=Found in nuclear foci following treatment with ionizing radiation, but not with ultraviolet irradiation or H(2)O(2). {ECO:0000250}. SUBUNIT: Homodimer. Interacts with the 20S and 26S proteasomes. Component of the spermatoproteasome, a form of the proteasome specifically found in testis. {ECO:0000269|PubMed:23706739}. DOMAIN: The bromodomain-like (BRDL) region specifically recognizes and binds acetylated histones. {ECO:0000269|PubMed:23706739}. TISSUE SPECIFICITY: Broadly expressed. Present in heart (at protein level). {ECO:0000269|PubMed:12093752, ECO:0000269|PubMed:16857966}. +Q8R326 PSPC1_MOUSE Paraspeckle component 1 (Paraspeckle protein 1) (mPSP1) 523 58,758 Alternative sequence (2); Chain (1); Coiled coil (1); Compositional bias (1); Domain (2); Modified residue (6); Mutagenesis (4); Region (2); Sequence conflict (1) FUNCTION: Together with NONO, required for the formation of nuclear paraspeckles. Regulates, cooperatively with NONO and SFPQ, androgen receptor-mediated gene transcription activity in Sertoli cell line. Binds to poly(A), poly(G) and poly(U) RNA homopolymers. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer. Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway. {ECO:0000250|UniProtKB:Q8WXF1, ECO:0000269|PubMed:16641145, ECO:0000269|PubMed:22966205}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Note=In punctate subnuclear structures localized adjacent to nuclear splicing speckles, called paraspeckles. Colocalizes with NONO and SFPQ in paraspeckles and perinucleolar caps in an RNA-dependent manner. May cycle between paraspeckles and nucleolus. In telophase, when daughter nuclei form, localizes to perinucleolar caps. {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 1: Nucleus matrix. Cytoplasm. Nucleus speckle {ECO:0000250}. SUBUNIT: Forms heterodimers with NONO; this involves formation of a coiled coil domain by helices from both proteins (By similarity). Interaction with NONO is required for its targeting to paraspeckles and perinucleolar caps (By similarity). Found in a RNP complex with CAT2 transcribed nuclear RNA (CTN-RNA). Interacts with NONO and SFPQ. Part of the HDP-RNP complex composed of at least HEXIM1, PRKDC, XRCC5, XRCC6, paraspeckle proteins (SFPQ, NONO, PSPC1, RBM14, and MATR3) and NEAT1 RNA. {ECO:0000250|UniProtKB:Q8WXF1, ECO:0000269|PubMed:15140795, ECO:0000269|PubMed:16239143, ECO:0000269|PubMed:16641145}. TISSUE SPECIFICITY: Isoform 1 is strongly expressed in testis (leptoten spermatocytes, round spematids and Sertoli cells) and moderately in cerebrum, cerebellum, lung, spleen and ovary (at protein level). Isoform 2 is strongly expressed in kidney and moderately in salivary gland (at protein level). {ECO:0000269|PubMed:15140795, ECO:0000269|PubMed:16641145}. +Q91YR9 PTGR1_MOUSE Prostaglandin reductase 1 (PRG-1) (EC 1.3.1.-) (15-oxoprostaglandin 13-reductase) (EC 1.3.1.48) (NADP-dependent leukotriene B4 12-hydroxydehydrogenase) (EC 1.3.1.74) 329 35,560 Binding site (4); Chain (1); Modified residue (2); Nucleotide binding (3); Sequence conflict (2) FUNCTION: Functions as 15-oxo-prostaglandin 13-reductase and acts on 15-oxo-PGE1, 15-oxo-PGE2 and 15-oxo-PGE2-alpha. Has no activity towards PGE1, PGE2 and PGE2-alpha. Catalyzes the conversion of leukotriene B4 into its biologically less active metabolite, 12-oxo-leukotriene B4. This is an initial and key step of metabolic inactivation of leukotriene B4 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Monomer or homodimer. {ECO:0000250}. +Q14A28 PROK1_MOUSE Prokineticin-1 (Endocrine-gland-derived vascular endothelial growth factor) (EG-VEGF) 105 11,678 Alternative sequence (1); Chain (1); Disulfide bond (5); Signal peptide (1) FUNCTION: Potently contracts gastrointestinal (GI) smooth muscle. Induces proliferation, migration and fenestration (the formation of membrane discontinuities) in capillary endothelial cells. Induces proliferation and differentiation, but not migration, of enteric neural crest cells. Directly influences neuroblastoma progression by promoting the proliferation and migration of neuroblastoma cells. Positively regulates PTGS2 expression and prostaglandin synthesis. May play a role in placentation. May play a role in normal and pathological testis angiogenesis. {ECO:0000250|UniProtKB:P58294, ECO:0000269|PubMed:12746324, ECO:0000269|PubMed:17324478, ECO:0000269|PubMed:17531315}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P58294}. TISSUE SPECIFICITY: Highly expressed in liver and ovary and weakly expressed in testis and placenta. Expressed in mucosa and mesenchyme of embryonic gut during enteric nervous system development (at protein level). Predominantly expressed in kidney and liver. Also expressed in lung, ovary, placenta and testis. In fetal liver, is restricted to and highly expressed in hepatocytes. In adult kidney, expression is restricted to the endothelial tubule cells. In placenta, expressed throughout gestation. {ECO:0000269|PubMed:12746324, ECO:0000269|PubMed:17324478, ECO:0000269|PubMed:17531315}. +Q922U1 PRPF3_MOUSE U4/U6 small nuclear ribonucleoprotein Prp3 (Pre-mRNA-splicing factor 3) 683 77,455 Chain (1); Compositional bias (1); Cross-link (3); Domain (1); Modified residue (2); Region (1); Sequence conflict (1) FUNCTION: Plays role in pre-mRNA splicing as component of the U4/U6-U5 tri-snRNP complex that is involved in spliceosome assembly, and as component of the precatalytic spliceosome (spliceosome B complex). {ECO:0000250|UniProtKB:O43395}. PTM: Ubiquitinated. Undergoes 'Lys-63'-linked polyubiquitination by PRPF19 and deubiquitination by USP4. 'Lys-63'-linked ubiquitination increases the affinity for PRPF8 and may regulate the assembly of the U4/U6-U5 tri-snRNP complex. {ECO:0000250|UniProtKB:O43395}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O43395}. Nucleus speckle {ECO:0000255|PROSITE-ProRule:PRU00627}. SUBUNIT: Component of the precatalytic spliceosome (spliceosome B complex). Component of the U4/U6-U5 tri-snRNP complex, a building block of the precatalytic spliceosome (spliceosome B complex). The U4/U6-U5 tri-snRNP complex is composed of the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39, plus LSM2, LSM3, LSM4, LSM5, LSM6, LSM7 and LSM8. Interacts directly with PRPF4. Part of a heteromeric complex containing PPIH, PRPF3 and PRPF4 that is stable in the absence of RNA. Interacts with SART3; the interaction is direct and recruits the deubiquitinase USP4 to PRPF3. Interacts with PRPF19. Interacts ('Lys-63'-linked polyubiquitinated) with PRPF8 (via the MPN (JAB/Mov34) domain); may stabilize the U4/U6-U5 tri-snRNP complex. {ECO:0000250|UniProtKB:O43395}. +Q60692 PSB6_MOUSE Proteasome subunit beta type-6 (EC 3.4.25.1) (Low molecular mass protein 19) (Macropain delta chain) (Multicatalytic endopeptidase complex delta chain) (Proteasome delta chain) (Proteasome subunit Y) 238 25,379 Active site (1); Beta strand (12); Chain (1); Erroneous initiation (3); Frameshift (1); Helix (6); Initiator methionine (1); Modified residue (2); Natural variant (2); Propeptide (1); Sequence conflict (2); Turn (2) FUNCTION: Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). Within the 20S core complex, PSMB6 displays a peptidylglutamyl-hydrolyzing activity also termed postacidic or caspase-like activity, meaning that the peptides bond hydrolysis occurs directly after acidic residues. {ECO:0000269|PubMed:16581775, ECO:0000269|PubMed:22341445}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P28072}. Nucleus {ECO:0000250|UniProtKB:P28072}. SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is a barrel-shaped complex made of 28 subunits that are arranged in four stacked rings. The two outer rings are each formed by seven alpha subunits, and the two inner rings are formed by seven beta subunits. The proteolytic activity is exerted by three beta-subunits PSMB5, PSMB6 and PSMB7. {ECO:0000269|PubMed:16857966, ECO:0000269|PubMed:22341445}. +O09061 PSB1_MOUSE Proteasome subunit beta type-1 (EC 3.4.25.1) (Macropain subunit C5) (Multicatalytic endopeptidase complex subunit C5) (Proteasome component C5) (Proteasome gamma chain) 240 26,372 Beta strand (13); Chain (1); Erroneous initiation (1); Glycosylation (2); Helix (4); Modified residue (6); Propeptide (1); Turn (1) FUNCTION: Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). {ECO:0000269|PubMed:16581775, ECO:0000269|PubMed:22341445}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P20618}. Nucleus {ECO:0000250|UniProtKB:P20618}. SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is a barrel-shaped complex made of 28 subunits that are arranged in four stacked rings. The two outer rings are each formed by seven alpha subunits, and the two inner rings are formed by seven beta subunits. The proteolytic activity is exerted by three beta-subunits PSMB5, PSMB6 and PSMB7 (PubMed:16857966, PubMed:22341445). Interacts with SERPINB2 (By similarity). Interacts with RFPL4A (PubMed:12525704). {ECO:0000250|UniProtKB:P20618, ECO:0000269|PubMed:12525704, ECO:0000269|PubMed:16857966, ECO:0000269|PubMed:22341445}. TISSUE SPECIFICITY: Detected in liver (at protein level). {ECO:0000269|PubMed:22341445}. +P57096 PSCA_MOUSE Prostate stem cell antigen 123 13,478 Chain (1); Disulfide bond (5); Domain (1); Glycosylation (1); Lipidation (1); Propeptide (1); Sequence conflict (1); Signal peptide (1) FUNCTION: May be involved in the regulation of cell proliferation. {ECO:0000250}.; FUNCTION: May act as a modulator of nicotinic acetylcholine receptors (nAChRs) activity. In vitro inhibits nicotine-induced signaling probably implicating alpha-3:beta-2- or alpha-7-containing nAChRs. {ECO:0000250|UniProtKB:O43653}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O43653}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:O43653}. SUBUNIT: Interacts with CHRNA4. {ECO:0000250|UniProtKB:O43653}. TISSUE SPECIFICITY: Predominantly expressed in prostate. Also found in spleen, liver, lung, prostate, kidney and testis. Expressed in brain cortex; expression is increased in transgenic mouse model of Alzheimer disease (at protein level). {ECO:0000269|PubMed:25680266}. +Q8BG32 PSD11_MOUSE 26S proteasome non-ATPase regulatory subunit 11 (26S proteasome regulatory subunit RPN6) (26S proteasome regulatory subunit S9) (26S proteasome regulatory subunit p44.5) 422 47,437 Chain (1); Cross-link (1); Domain (1); Initiator methionine (1); Modified residue (3) FUNCTION: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. In the complex, PSMD11 is required for proteasome assembly. Plays a key role in increased proteasome activity in embryonic stem cells (ESCs): its high expression in ESCs promotes enhanced assembly of the 26S proteasome, followed by higher proteasome activity. {ECO:0000250|UniProtKB:O00231}. SUBUNIT: Component of the 19S proteasome regulatory particle complex. The 26S proteasome consists of a 20S core particle (CP) and two 19S regulatory subunits (RP). The regulatory particle is made of a lid composed of 9 subunits including PSMD11, a base containing 6 ATPases and few additional components. {ECO:0000250|UniProtKB:O00231, ECO:0000269|PubMed:16857966}. +Q2PFD7 PSD3_MOUSE PH and SEC7 domain-containing protein 3 (Exchange factor for ADP-ribosylation factor guanine nucleotide factor 6 D) (Exchange factor for ARF6 D) (Pleckstrin homology and SEC7 domain-containing protein 3) 1037 114,722 Alternative sequence (5); Chain (1); Coiled coil (1); Domain (2); Modified residue (7); Sequence conflict (1) FUNCTION: Guanine nucleotide exchange factor for ARF6. {ECO:0000269|PubMed:16707115}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23603394}. Cell projection, ruffle membrane {ECO:0000269|PubMed:23603394}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000269|PubMed:16707115}. Note=In interphase associated with the plasma membrane, in particular with membrane ruffling regions. {ECO:0000269|PubMed:23603394}. TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in liver. Present in brain, with highest levels in olfactory bulb, cortex, hippocampal pyramidal cell layer and cerebellar granule cell layer (at protein level). {ECO:0000269|PubMed:16707115}. +Q9D8W5 PSD12_MOUSE 26S proteasome non-ATPase regulatory subunit 12 (26S proteasome regulatory subunit RPN5) (26S proteasome regulatory subunit p55) 456 52,895 Chain (1); Cross-link (2); Domain (1); Initiator methionine (1); Modified residue (2); Sequence conflict (5) FUNCTION: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. {ECO:0000250|UniProtKB:O00232}. SUBUNIT: Component of the 19S proteasome regulatory particle complex. The 26S proteasome consists of a 20S core particle (CP) and two 19S regulatory subunits (RP). The regulatory particle is made of a lid composed of 9 subunits including PSMD12, a base containing 6 ATPases and few additional components. {ECO:0000250|UniProtKB:O00232, ECO:0000269|PubMed:16857966}. +Q9CWH6 PSMA8_MOUSE Proteasome subunit alpha-type 7-like (EC 3.4.25.1) 250 27,866 Chain (1) FUNCTION: Component of the spermatoproteasome, a form of the proteasome specifically found in testis that promotes degradation of histones, thereby participating actively to the exchange of histones during spermatogenesis. The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. {ECO:0000269|PubMed:23706739}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel (By similarity). Component of the spermatoproteasome, a form of the proteasome specifically found in testis. {ECO:0000250, ECO:0000269|PubMed:23706739}. +Q8BM39 PRP18_MOUSE Pre-mRNA-splicing factor 18 (PRP18 homolog) 342 39,890 Alternative sequence (2); Chain (1); Modified residue (1); Sequence caution (1); Sequence conflict (1) FUNCTION: Participates in the second step of pre-mRNA splicing. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}. Note=Colocalizes with spliceosomal snRNPs. {ECO:0000250}. SUBUNIT: Heterodimer with PPIH. Interacts with PRPF4 and with the spliceosome. Part of a complex containing U4/U6 snRNPs (By similarity). {ECO:0000250}. +Q9DAD6 PROF3_MOUSE Profilin-3 (Profilin III) 137 14,697 Chain (1) FUNCTION: Binds to actin and affects the structure of the cytoskeleton. Binds to poly-L-proline, phosphatidylinositol 3-phosphate (PtdIns(3)P), phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) and phosphatidylinositol 4-phosphate (PtdIns(4)P). Slightly reduces actin polymerization. May be involved in spermatogenesis. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Nucleus {ECO:0000269|PubMed:18692047}. SUBUNIT: Interacts with ACTRT3. {ECO:0000269|PubMed:18692047}. TISSUE SPECIFICITY: Testis specific. {ECO:0000269|PubMed:11867228}. +Q9WU79 PROD_MOUSE Proline dehydrogenase 1, mitochondrial (EC 1.5.5.2) (Proline oxidase) 599 68,036 Chain (1); Erroneous gene model prediction (1); Erroneous initiation (2); Modified residue (3); Sequence conflict (5); Transit peptide (1) Amino-acid degradation; L-proline degradation into L-glutamate; L-glutamate from L-proline: step 1/2. FUNCTION: Converts proline to delta-1-pyrroline-5-carboxylate. SUBCELLULAR LOCATION: Mitochondrion matrix. TISSUE SPECIFICITY: Expressed in liver, kidney, heart and to a lesser extent in brain, lung and muscle. DISEASE: Note=Pro/re mice that have a premature termination on Prodh are sluggish in their movement. +Q812A5 PRR5_MOUSE Proline-rich protein 5 (Protein observed with Rictor-1) (Protor-1) 387 42,523 Alternative sequence (1); Chain (1); Frameshift (1); Modified residue (2); Region (2); Sequence conflict (4) FUNCTION: Subunit of mTORC2, which regulates cell growth and survival in response to hormonal signals. mTORC2 is activated by growth factors, but, in contrast to mTORC1, seems to be nutrient-insensitive. mTORC2 seems to function upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors. mTORC2 promotes the serum-induced formation of stress-fibers or F-actin. mTORC2 plays a critical role in AKT1 'Ser-473' phosphorylation, which may facilitate the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1 which is a prerequisite for full activation. mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422'. mTORC2 also modulates the phosphorylation of PRKCA on 'Ser-657'. PRR5 plays an important role in regulation of PDGFRB expression and in modulation of platelet-derived growth factor signaling. May act as a tumor suppressor in breast cancer (By similarity). {ECO:0000250}. SUBUNIT: Part of the mammalian target of rapamycin complex 2 (mTORC2) which contains MTOR, MLST8, PRR5, RICTOR, MAPKAP1 and DEPTOR (By similarity). Contrary to mTORC1, mTORC2 does not bind to and is not sensitive to FKBP12-rapamycin. Binds directly to MTOR and RICTOR within the TORC2 complex (By similarity). Interacts with MTOR. {ECO:0000250, ECO:0000269|PubMed:20801936}. TISSUE SPECIFICITY: Ubiquitously expressed. Expressed at high levels in kidney. {ECO:0000269|PubMed:12559566}. +Q402U7 PRS44_MOUSE Serine protease 44 (EC 3.4.21.-) (Testis serine protease 4) (TESSP-4) (Testis-specific serine protease 4) 372 41,073 Active site (3); Alternative sequence (2); Chain (1); Disulfide bond (4); Domain (1); Glycosylation (1); Signal peptide (1); Topological domain (1); Transmembrane (1) TRANSMEM 352 372 Helical. {ECO:0000255}. TOPO_DOM 26 351 Extracellular. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +B1ARI9 PRR29_MOUSE Proline-rich protein 29 187 20,763 Alternative sequence (1); Chain (1); Compositional bias (1) +Q2EY15 PRTG_MOUSE Protogenin (Protein Shen-Dan) 1191 130,533 Chain (1); Disulfide bond (4); Domain (9); Erroneous initiation (1); Glycosylation (2); Sequence conflict (5); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 944 964 Helical. {ECO:0000255}. TOPO_DOM 24 943 Extracellular. {ECO:0000255}.; TOPO_DOM 965 1191 Cytoplasmic. {ECO:0000255}. FUNCTION: May play a role in anteroposterior axis elongation. {ECO:0000269|PubMed:16881056}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: From mid-gastrulation to early somite stages, restricted to posterior neural plate and mesoderm with an anterior limit at the level of the rhombencephalon. Posterior restriction is progressively lost during somitogenesis. Expression is maintained in the neural tube and paraxial mesoderm during this process. As development proceeds, further restricted to the dorsal parts of the spinal cord and somites. In parallel, expression progresses caudally during axis elongation. {ECO:0000269|PubMed:16881056}. +Q8BIW1 PRUN1_MOUSE Exopolyphosphatase PRUNE1 (EC 3.6.1.1) (PRUNEM1) 454 50,239 Chain (1); Metal binding (5); Modified residue (4); Motif (1); Region (1); Sequence conflict (2) FUNCTION: Phosphodiesterase (PDE) that has higher activity toward cAMP than cGMP, as substrate. Plays a role in cell proliferation, migration and differentiation, and acts as a negative regulator of NME1. Plays a role in the regulation of neurogenesis. Involved in the regulation of microtubule polymerization. {ECO:0000250|UniProtKB:Q86TP1}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cell junction, focal adhesion {ECO:0000250}. SUBUNIT: Homooligomer. Able to homodimerize via its C-terminal domain. Interacts with NME1. Interacts with GSK3; at focal adhesion complexes where paxillin and vinculin are colocalized. Interacts with alpha and beta tubulin. {ECO:0000250|UniProtKB:Q86TP1}. +Q7TSA6 PRSR3_MOUSE Proline and serine-rich protein 3 634 67,263 Alternative sequence (3); Chain (1); Compositional bias (2); Modified residue (1) +Q8BLR5 PSD4_MOUSE PH and SEC7 domain-containing protein 4 (Exchange factor for ADP-ribosylation factor guanine nucleotide factor 6 B) (Exchange factor for ARF6 B) (Pleckstrin homology and SEC7 domain-containing protein 4) 1005 112,733 Chain (1); Coiled coil (1); Domain (2); Erroneous initiation (1); Modified residue (7); Sequence conflict (1) FUNCTION: Guanine nucleotide exchange factor for ARF6 and ARL14/ARF7. Through ARL14 activation, controls the movement of MHC class II-containing vesicles along the actin cytoskeleton in dendritic cells. Involved in membrane recycling. Interacts with several phosphatidylinositol phosphate species, including phosphatidylinositol 3,4-bisphosphate, phosphatidylinositol 3,5-bisphosphate and phosphatidylinositol 4,5-bisphosphate (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8NDX1}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q8NDX1}. Note=In interphase associated with the plasma membrane, in particular with membrane ruffling regions. Accumulates in dynamic actin-rich membrane ruffles and microvilli-like structures. Recruited to membranes via phosphatidylinositol phosphate-binding. {ECO:0000250|UniProtKB:Q8NDX1}. +Q9CZ15 PSF1_MOUSE DNA replication complex GINS protein PSF1 (GINS complex subunit 1) 196 22,893 Chain (1) FUNCTION: Required for correct functioning of the GINS complex, a complex that plays an essential role in the initiation of DNA replication, and progression of DNA replication forks. GINS complex seems to bind preferentially to single-stranded DNA. {ECO:0000250|UniProtKB:Q14691}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the GINS complex which is a heterotetramer of GINS1, GINS2, GINS3 and GINS4. Forms a stable subcomplex with GINS4. GINS complex interacts with DNA primase in vitro. {ECO:0000250|UniProtKB:Q14691}. +Q8VDM4 PSMD2_MOUSE 26S proteasome non-ATPase regulatory subunit 2 (26S proteasome regulatory subunit RPN1) (26S proteasome regulatory subunit S2) (26S proteasome subunit p97) 908 100,203 Chain (1); Compositional bias (1); Modified residue (9); Repeat (7) FUNCTION: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. {ECO:0000250|UniProtKB:Q13200}.; FUNCTION: Binds to the intracellular domain of tumor necrosis factor type 1 receptor. The binding domain of TRAP1 and TRAP2 resides outside the death domain of TNFR1. {ECO:0000250|UniProtKB:Q13200}. SUBUNIT: Component of the 19S proteasome regulatory particle complex. The 26S proteasome consists of a 20S core particle (CP) and two 19S regulatory subunits (RP). The regulatory particle is made of a lid composed of 9 subunits, a base containing 6 ATPases and few additional components including PSMD2 (By similarity). Interacts with RPGRIP1L (PubMed:26150391). {ECO:0000250|UniProtKB:Q13200, ECO:0000269|PubMed:26150391}. +O70300 PSPN_MOUSE Persephin (PSP) 156 17,031 Chain (1); Disulfide bond (4); Signal peptide (1) FUNCTION: Exhibits neurotrophic activity on mesencephalic dopaminergic and motor neurons. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}. +Q9CR00 PSMD9_MOUSE 26S proteasome non-ATPase regulatory subunit 9 (26S proteasome regulatory subunit p27) 222 24,720 Chain (1); Domain (1); Modified residue (1) FUNCTION: Acts as a chaperone during the assembly of the 26S proteasome, specifically of the base subcomplex of the PA700/19S regulatory complex (RC). During the base subcomplex assembly is part of an intermediate PSMD9:PSMC6:PSMC3 module, also known as modulator trimer complex; PSMD9 is released during the further base assembly process (By similarity). {ECO:0000250}. SUBUNIT: Interacts with PSMC3. Part of a transient complex (modulator) containing PSMD9, PSMC6 and PSMC3 formed during the assembly of the 26S proteasome (By similarity). {ECO:0000250}. +P50405 PSPB_MOUSE Pulmonary surfactant-associated protein B (SP-B) (Pulmonary surfactant-associated proteolipid SPL(Phe)) 377 41,728 Chain (1); Disulfide bond (10); Domain (4); Glycosylation (1); Propeptide (2); Signal peptide (1) FUNCTION: Pulmonary surfactant-associated proteins promote alveolar stability by lowering the surface tension at the air-liquid interface in the peripheral air spaces. SP-B increases the collapse pressure of palmitic acid to nearly 70 millinewtons per meter. SUBCELLULAR LOCATION: Secreted, extracellular space, surface film. SUBUNIT: Homodimer; disulfide-linked. +Q9DAZ2 PR2B1_MOUSE Prolactin-2B1 (Placental prolactin-like protein K) (PLP-K) (PRL-like protein K) 228 25,879 Chain (1); Disulfide bond (2); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000250}. TISSUE SPECIFICITY: Expressed specifically in placenta. Expressed at high levels in trophoblast cells from both junctional and labyrinth zones of the chorioallantoic placenta the last week of gestation. {ECO:0000269|PubMed:12488360}. +P04768 PR2C3_MOUSE Prolactin-2C3 (Mitogen-regulated protein 2) (Mitogen-regulated protein 3) (Prolactin-2C4) (Proliferin-2) (Proliferin-3) 224 25,338 Chain (1); Disulfide bond (3); Glycosylation (4); Sequence conflict (3); Signal peptide (1) FUNCTION: May have a role in embryonic development. It is likely to provide a growth stimulus to target cells in maternal and fetal tissues during the development of the embryo at mid-gestation. May play a role during wound healing and in the hair follicle cycle as a growth factor and/or an angiogenesis factor. May play a role in microvilli formation and cell proliferation of neuroblastoma cells. {ECO:0000269|PubMed:11316781, ECO:0000269|PubMed:16876275}. PTM: N-glycosylated and sialylated. {ECO:0000269|PubMed:10537154}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10537154, ECO:0000269|PubMed:16876275}. Endoplasmic reticulum {ECO:0000269|PubMed:16876275}. TISSUE SPECIFICITY: Expressed in placenta and hair follicles, with highest expression levels detected in the outer root sheath and no expression detected in bulb (PubMed:11316781). Expressed in placenta, skin wounds, keratinocytes and weakly in embryonic fibroblasts (PubMed:10537154, PubMed:11316781, PubMed:16876275). Expressed in brain, cerebellum and in Neuro-2a cell line (PubMed:16876275). Not detected in liver, kidney, ovary, pituitary gland and brain (PubMed:3859868). {ECO:0000269|PubMed:10537154, ECO:0000269|PubMed:11316781, ECO:0000269|PubMed:16876275, ECO:0000269|PubMed:3859868}. +Q3UZD5 PRDM6_MOUSE Putative histone-lysine N-methyltransferase PRDM6 (EC 2.1.1.43) (PR domain zinc finger protein 6) (PR domain-containing protein 6) (PR domain-containing protein in smooth muscle) 596 64,503 Alternative sequence (3); Chain (1); Compositional bias (6); Domain (1); Mutagenesis (2); Zinc finger (4) FUNCTION: Putative histone methyltransferase that acts as a transcriptional repressor of smooth muscle gene expression (PubMed:16537907, PubMed:17662997). Promotes the transition from differentiated to proliferative smooth muscle by suppressing differentiation and maintaining the proliferative potential of vascular smooth muscle cells (PubMed:27181681, PubMed:16537907, PubMed:17662997). Also plays a role in endothelial cells by inhibiting endothelial cell proliferation, survival and differentiation. It is unclear whether it has histone methyltransferase activity in vivo. According to some authors, it does not act as a histone methyltransferase by itself and represses transcription by recruiting EHMT2/G9a (PubMed:16537907). According to others, it possesses histone methyltransferase activity when associated with other proteins and specifically methylates 'Lys-20' of histone H4 in vitro. 'Lys-20' methylation represents a specific tag for epigenetic transcriptional repression (PubMed:17662997). {ECO:0000269|PubMed:16537907, ECO:0000269|PubMed:17662997, ECO:0000269|PubMed:27181681}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16537907, ECO:0000269|PubMed:17662997, ECO:0000269|PubMed:27181681}. SUBUNIT: Interacts with HDAC1, HDAC2, HDAC3, CBX1 and EP300. {ECO:0000269|PubMed:16537907}. TISSUE SPECIFICITY: Expressed in a variety of smooth muscle-containing tissues and displays especially robust expression in the cardiac outflow tract and descending aorta during embryogenesis. Also enriched in vascular precursors during development. {ECO:0000269|PubMed:16537907, ECO:0000269|PubMed:17662997, ECO:0000269|PubMed:27181681}. +Q571I4 PRAG1_MOUSE Inactive tyrosine-protein kinase PRAG1 (Notch activation complex kinase) (PEAK1-related kinase-activating pseudokinase 1) (Sugen kinase 223) (Tyrosine-protein kinase SgK223) 1373 147,945 Chain (1); Compositional bias (2); Domain (1); Erroneous initiation (3); Modified residue (7); Region (2); Sequence conflict (11) FUNCTION: Catalytically inactive protein kinase that acts as a scaffold protein (By similarity). Functions as an effector of the small GTPase RND2, which stimulates RhoA activity and inhibits NGF-induced neurite outgrowth (By similarity). Promotes Src family kinase (SFK) signaling by regulating the subcellular localization of CSK, a negative regulator of these kinases, leading to the regulation of cell morphology and motility by a CSK-dependent mechanism (By similarity). Acts as a critical coactivator of Notch signaling (PubMed:25038227). {ECO:0000250|UniProtKB:D3ZMK9, ECO:0000269|PubMed:25038227}. PTM: Phosphorylated by CSK on Tyr-238, Tyr-343, and Tyr-391; Tyr-391 is a primary site of phosphorylation. {ECO:0000250|UniProtKB:D3ZMK9}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:D3ZMK9}. Nucleus {ECO:0000269|PubMed:25038227}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q86YV5}. Note=Colocalized with NOTCH1 in the nucleus (PubMed:25038227). SUBUNIT: Homodimer (By similarity). Dimerization leads to the catalytic activation of CSK (By similarity). Interacts (via C-terminus) with RND2 (By similarity). Interacts with CSK (via SH2 domain) in a Tyr-391 phosphorylation-dependent manner; this interaction potentiates kinase activity of CSK (By similarity). Interacts with NOTCH1 intracellular domain (N1ICD) (PubMed:25038227). Forms a complex with PRAG1, N1ICD and MAML1, in a MAML1-dependent manner (PubMed:25038227). {ECO:0000250|UniProtKB:D3ZMK9, ECO:0000269|PubMed:25038227}. DOMAIN: The dimerization region encompasses helices both from the N- and C-terminal of the protein kinase domain. {ECO:0000250|UniProtKB:D3ZMK9}. +Q96EQ9 PRDM9_MOUSE Histone-lysine N-methyltransferase PRDM9 (EC 2.1.1.43) (Hybrid sterility protein 1) (Meiosis-induced factor containing a PR/SET domain and zinc-finger motif) (PR domain zinc finger protein 9) (PR domain-containing protein 9) 843 97,365 Alternative sequence (5); Beta strand (10); Chain (1); Domain (2); Erroneous initiation (1); Helix (4); Mutagenesis (2); Turn (4); Zinc finger (13) FUNCTION: Histone methyltransferase that specifically trimethylates 'Lys-4' of histone H3 during meiotic prophase and is essential for proper meiotic progression. Does not have the ability to mono- and dimethylate 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Plays a central role in the transcriptional activation of genes during early meiotic prophase. {ECO:0000269|PubMed:16292313}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome {ECO:0000305}. TISSUE SPECIFICITY: Specifically expressed in germ cells entering meiotic prophase in female fetal gonads and in postnatal testis. {ECO:0000269|PubMed:16292313}. +Q9QUN5 PR3C1_MOUSE Prolactin-3C1 (Decidualin) (Placental prolactin-like protein J) (PLP-J) (PRL-like protein J) (Prolactin-like protein I) (PLP-I) (PRL-like protein I) 212 24,706 Chain (1); Disulfide bond (1); Erroneous initiation (1); Glycosylation (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000250}. TISSUE SPECIFICITY: Expressed exclusively in decidua. {ECO:0000269|PubMed:10537137}. +P18121 PR3D1_MOUSE Prolactin-3D1 (Chorionic somatomammotropin hormone 1) (Placental lactogen I) (PL-I) 224 25,524 Chain (1); Disulfide bond (2); Glycosylation (2); Signal peptide (1) SUBCELLULAR LOCATION: Secreted. +P97313 PRKDC_MOUSE DNA-dependent protein kinase catalytic subunit (DNA-PK catalytic subunit) (DNA-PKcs) (EC 2.7.11.1) (p460) 4128 471,471 Alternative sequence (2); Chain (1); Domain (3); Modified residue (23); Natural variant (3); Region (3); Repeat (6); Sequence conflict (6); Site (1) FUNCTION: Serine/threonine-protein kinase that acts as a molecular sensor for DNA damage. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break (DSB) repair and V(D)J recombination. Must be bound to DNA to express its catalytic properties. Promotes processing of hairpin DNA structures in V(D)J recombination by activation of the hairpin endonuclease artemis (DCLRE1C). The assembly of the DNA-PK complex at DNA ends is also required for the NHEJ ligation step. Required to protect and align broken ends of DNA. May also act as a scaffold protein to aid the localization of DNA repair proteins to the site of damage. Found at the ends of chromosomes, suggesting a further role in the maintenance of telomeric stability and the prevention of chromosomal end fusion. Also involved in modulation of transcription. Recognizes the substrate consensus sequence [ST]-Q. Phosphorylates 'Ser-139' of histone variant H2AX/H2AFX, thereby regulating DNA damage response mechanism. Phosphorylates DCLRE1C, C1D, c-Abl/ABL1, histone H1, HSPCA, c-jun/JUN, p53/TP53, PARP1, POU2F1, DHX9, SRF, XRCC1, XRCC4, XRCC5, XRCC6, WRN, MYC and RFA2. Can phosphorylate C1D not only in the presence of linear DNA but also in the presence of supercoiled DNA. Ability to phosphorylate p53/TP53 in the presence of supercoiled DNA is dependent on C1D. Contributes to the determination of the circadian period length by antagonizing phosphorylation of CRY1 'Ser-588' and increasing CRY1 protein stability, most likely through an indirect mechanism. Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway (By similarity). {ECO:0000250|UniProtKB:P78527, ECO:0000269|PubMed:12426399, ECO:0000269|PubMed:24158435}. PTM: Autophosphorylated on Ser-2053, Thr-2605, Thr-2634 and Thr-2643. Ser-2053 and Thr-2605 are DNA damage-inducible phosphorylation sites (inducible with ionizing radiation, IR) dephosphorylated by PPP5C. Autophosphorylation induces a conformational change that leads to remodeling of the DNA-PK complex, requisite for efficient end processing and DNA repair (By similarity). {ECO:0000250}.; PTM: S-nitrosylated by GAPDH. {ECO:0000269|PubMed:20972425}.; PTM: Polyubiquitinated by RNF144A, leading to proteasomal degradation. {ECO:0000250|UniProtKB:P78527}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P78527}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P78527}. SUBUNIT: DNA-PK is a heterotrimer of PRKDC and the Ku p70/YRCC6-p86/XRCC5 dimer. Formation of this complex may be promoted by interaction with ILF3. Associates with the DNA-bound Ku heterodimer, but it can also bind to and be activated by free DNA. The DNA-PK heterotrimer associates with the LIG4-XRCC4 complex to form the core of the non-homologous end joining (NHEJ) complex. Additional components of the NHEJ complex include NHEJ1/XLF and PAXX. Interacts with DNA-PKcs-interacting protein (KIP) with the region upstream the kinase domain. PRKDC alone also interacts with and phosphorylates DCLRE1C, thereby activating the latent endonuclease activity of this protein. Interacts with C1D. Interacts with TTI1 and TELO2. Interacts with CIB1. Interacts with SETX (By similarity). Interacts with CRY1 and CRY2; negatively regulates CRY1 phosphorylation (PubMed:24158435). Interacts with NR4A3; the DNA-dependent protein kinase complex DNA-PK phosphorylates and activates NR4A3 and prevents NR4A3 ubiquitination and degradation (By similarity). Part of the HDP-RNP complex composed of at least HEXIM1, PRKDC, XRCC5, XRCC6, paraspeckle proteins (SFPQ, NONO, PSPC1, RBM14, and MATR3) and NEAT1 RNA. {ECO:0000250|UniProtKB:P78527, ECO:0000269|PubMed:24158435}. DISEASE: Note=Defects in Prkdc are the cause of severe combined immune deficiency (SCID) which is characterized by a lack of mature functional lymphocytes and a high susceptibility to lethal opportunistic infections if not chronically treated with antibiotics. The lack of B- and T-cell immunity resembles severe combined immunodeficiency syndrome in human infants. {ECO:0000269|PubMed:9122213}. +Q80VL3 PRIC3_MOUSE Prickle planar cell polarity protein 3 (LIM domain only protein 6) (LMO-6) (Prickle-like protein 3) (Pk3) (Triple LIM domain protein 6) 624 69,727 Chain (1); Compositional bias (2); Domain (4); Modified residue (2); Sequence conflict (2) FUNCTION: Involved in the planar cell polarity (PCP) pathway that is essential for the polarization of epithelial cells during morphogenetic processes, including gastrulation and neurulation (By similarity). PCP is maintained by two molecular modules, the global and the core modules, PRICKLE3 being part of the core module (By similarity). Distinct complexes of the core module segregate to opposite sides of the cell, where they interact with the opposite complex in the neighboring cell at or near the adherents junctions (By similarity). Involved in the organization of the basal body (By similarity). Involved in cilia growth and positioning (By similarity). {ECO:0000250|UniProtKB:A8WH69}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A8WH69}. Cell membrane {ECO:0000250|UniProtKB:A8WH69}; Peripheral membrane protein {ECO:0000250|UniProtKB:A8WH69}; Cytoplasmic side {ECO:0000250|UniProtKB:A8WH69}. Note=Recruited by VANGL2 to anterior cell borders. This polarity is controlled by Wnt proteins (By similarity). WTIP is involved in the recruitment of PRICKLE3 to the basal body (By similarity). {ECO:0000250|UniProtKB:A8WH69}. SUBUNIT: Interacts with VANGL2 via its C-terminus (By similarity). The VANGL2-dependent membrane recruitment of PRICKLE3 is a prerequisite for its polarization (By similarity). Interacts with WTIP. WTIP is involved in the recruitment of PRICKLE3 to the basal body (By similarity). {ECO:0000250|UniProtKB:A8WH69}. +Q9WTX2 PRKRA_MOUSE Interferon-inducible double-stranded RNA-dependent protein kinase activator A (PKR-associated protein X) (PKR-associating protein X) (RAX) (Protein activator of the interferon-induced protein kinase) (Protein kinase, interferon-inducible double-stranded RNA-dependent activator) 313 34,371 Chain (1); Domain (3); Modified residue (4); Region (3); Sequence conflict (1) FUNCTION: Required for siRNA production by DICER1 and for subsequent siRNA-mediated post-transcriptional gene silencing. Does not seem to be required for processing of pre-miRNA to miRNA by DICER1 (By similarity). Activates EIF2AK2/PKR in the absence of double-stranded RNA (dsRNA), leading to phosphorylation of EIF2S1/EFI2-alpha and inhibition of translation and induction of apoptosis. Promotes UBC9-p53/TP53 association and sumoylation and phosphorylation of p53/TP53 at 'Lys-386' at 'Ser-392' respectively and enhances its activity in a EIF2AK2/PKR-dependent manner. {ECO:0000250, ECO:0000269|PubMed:10336432, ECO:0000269|PubMed:22214662}. PTM: Phosphorylated at Ser-246 in unstressed cells and at Ser-287 in stressed cells. Phosphorylation at Ser-246 appears to be a prerequisite for subsequent phosphorylation at Ser-287. Phosphorylation at Ser-246 and Ser-287 are necessary for activation of EIF2AK2/PKR under conditions of stress (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm {ECO:0000250}. SUBUNIT: Homodimer. Interacts with DICER1, AGO2 and TARBP2. Also able to interact with dsRNA (By similarity). Interacts with EIF2AK2/PKR through its DRBM domains. Interacts with DUS2L (via DRBM domain) (By similarity). Interacts with UBC9. Forms a complex with UBC9 and p53/TP53. {ECO:0000250, ECO:0000269|PubMed:10336432, ECO:0000269|PubMed:22214662}. DOMAIN: Self-association may occur via interactions between DRBM domains as follows: DRBM 1/DRBM 1, DRBM 1/DRBM 2, DRBM 2/DRBM 2 or DRBM 3/DRBM3. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver, lung, muscle, spleen and testis. {ECO:0000269|PubMed:10336432}. +Q08761 PROS_MOUSE Vitamin K-dependent protein S 675 74,934 Chain (1); Disulfide bond (15); Domain (7); Glycosylation (2); Modified residue (12); Propeptide (1); Region (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Anticoagulant plasma protein; it is a cofactor to activated protein C in the degradation of coagulation factors Va and VIIIa. It helps to prevent coagulation and stimulating fibrinolysis. PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Plasma. +P48437 PROX1_MOUSE Prospero homeobox protein 1 (Homeobox prospero-like protein PROX1) (PROX-1) 737 83,126 Chain (1); Compositional bias (1); Cross-link (1); Domain (2); Modified residue (8); Region (3); Sequence conflict (1) FUNCTION: Transcription factor involved in developmental processes such as cell fate determination, gene transcriptional regulation and progenitor cell regulation in a number of organs. Plays a critical role in embryonic development and functions as a key regulatory protein in neurogenesis and the development of the heart, eye lens, liver, pancreas and the lymphatic system. Involved in the regulation of the circadian rhythm. Represses: transcription of the retinoid-related orphan receptor RORG, transcriptional activator activity of RORA and RORG and the expression of RORA/G-target genes including core clock components: ARNTL/BMAL1, NPAS2 and CRY1 and metabolic genes: AVPR1A and ELOVL3. {ECO:0000269|PubMed:23723244, ECO:0000303|PubMed:22733308}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23723244}. Note=RORG promotes its nuclear localization. {ECO:0000269|PubMed:23723244}. SUBUNIT: Interacts with RORA and RORG (via AF-2 motif). {ECO:0000269|PubMed:23723244}. DOMAIN: The Prospero-type homeodomain and the adjacent Prospero domain act as a single structural unit, the Homeo-Prospero domain (Potential). The Prospero-type homeodomain is essential for repression of RORG transcriptional activator activity (PubMed:23723244). {ECO:0000255|PROSITE-ProRule:PRU01162, ECO:0000269|PubMed:23723244}. TISSUE SPECIFICITY: Expressed in the young neurons of the subventricular region of the CNS, developing eye lens and pancreas. It is also found in the developing liver, heart and skeletal muscle. In the eye, expressed in the lens and retina at postnatal day 10. In the retina, localized to the inner nuclear layer. In the lens, localized to epithelial and fiber cells. {ECO:0000269|PubMed:7908825, ECO:0000269|PubMed:9703987}. +Q811B5 PRR3_MOUSE Proline-rich protein 3 (MHC class I region proline-rich protein CAT56) 190 21,167 Chain (1); Compositional bias (1); Zinc finger (1) +A2AVJ5 PRR5L_MOUSE Proline-rich protein 5-like (Protein observed with Rictor-2) (Protor-2) 370 40,982 Chain (1); Erroneous initiation (3); Modified residue (1); Sequence conflict (2) FUNCTION: Associates with the mTORC2 complex that regulates cellular processes including survival and organization of the cytoskeleton (By similarity). Regulates the activity of the mTORC2 complex in a substrate-specific manner preventing for instance the specific phosphorylation of PKCs and thereby controlling cell migration (PubMed:22609986). Plays a role in the stimulation of ZFP36-mediated mRNA decay of several ZFP36-associated mRNAs, such as TNF-alpha and GM-CSF, in response to stress. Required for ZFP36 localization to cytoplasmic stress granule (SG) and P-body (PB) in response to stress. {ECO:0000250|UniProtKB:Q6MZQ0, ECO:0000269|PubMed:22609986}. PTM: Ubiquitinated. Ubiquitination by RFFL promotes proteasomal degradation of PRR5L thereby modifying the substrate-specific activity of the mTORC2 complex. Ubiquitination by RFFL is stimulated by LPA/lysophosphatidic acid (By similarity). {ECO:0000250}. SUBUNIT: Interacts with the mammalian target of rapamycin complex 2 (mTORC2) which contains MTOR, MLST8, PRR5, RICTOR, MAPKAP1 and DEPTOR. Interacts with RFFL. Interacts (via C-terminus) with ZFP36 (via C-terminus); this interaction may accelerate ZFP36-mediated mRNA decay during stress. Interacts with RICTOR. {ECO:0000250|UniProtKB:Q6MZQ0}. +Q3V0I2 PRR7_MOUSE Proline-rich protein 7 (Synaptic proline-rich membrane protein) 269 30,354 Chain (1); Compositional bias (1); Modified residue (1); Motif (1); Region (4); Topological domain (2); Transmembrane (1) TRANSMEM 10 30 Helical; Signal-anchor for type III membrane protein. {ECO:0000255}. TOPO_DOM 1 9 Extracellular. {ECO:0000255}.; TOPO_DOM 31 269 Cytoplasmic. {ECO:0000255}. FUNCTION: Acts as a synapse-to-nucleus messenger to promote NMDA receptor-mediated excitotoxicity in neurons in a JUN-dependent manner (By similarity). Inhibits ubiquitination-mediated degradation and promotes phosphorylation and transcriptional activity of transcription factor JUN (By similarity). Might play a redundant role in the regulation of T cell receptor signaling (PubMed:27657535). Might promote apoptosis in T cells (By similarity). {ECO:0000250|UniProtKB:P0C6T3, ECO:0000250|UniProtKB:Q8TB68, ECO:0000269|PubMed:27657535}. PTM: Palmitoylated. {ECO:0000250|UniProtKB:Q8TB68}.; PTM: Tyrosine phosphorylated, possibly by SRC. {ECO:0000250|UniProtKB:Q8TB68}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8TB68}; Single-pass type III membrane protein {ECO:0000305}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000250|UniProtKB:P0C6T3}; Single-pass type III membrane protein {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8TB68}. Cell junction, synapse {ECO:0000250|UniProtKB:P0C6T3}. Cell projection, dendrite {ECO:0000250|UniProtKB:P0C6T3}. Nucleus {ECO:0000250|UniProtKB:P0C6T3}. Note=Enriched in postsynaptic plasma membrane and postsynaptic densities (PSD). Accumulates in spines along with synapse maturation and colocalizes with DLG4 in a punctate pattern. Translocates from synapses to nuclei following NMDA receptor activity (By similarity). {ECO:0000250|UniProtKB:P0C6T3}. SUBUNIT: Forms a complex with NMDA receptor zeta subunit GRIN1 and epsilon subunit GRIN2B (By similarity). Interacts with GRIN2B (By similarity). Interacts with GRIN1; the interaction is reduced upon NMDA receptor activity (By similarity). Found in a postsynaptic membrane complex with DLG4 and GRIN1 (By similarity). Interacts with DLG4 (via PDZ3 domain and to lesser degree via PDZ2 domain) (By similarity). Interacts with JUN (PubMed:27458189). Found in a complex with JUN and FBXW7 (By similarity). Interacts with JUN and FBXW7; the interaction inhibits ubiquitination-mediated JUN degradation promoting its phosphorylation and transcriptional activity (By similarity). Interacts with SRC (By similarity). {ECO:0000250|UniProtKB:P0C6T3, ECO:0000250|UniProtKB:Q8TB68, ECO:0000269|PubMed:27458189}. TISSUE SPECIFICITY: Highly expressed in brain, moderately expressed in lymph nodes and T cells and low expression in thymus and spleen. Expressed in single positive progenitor thymocytes, particularly in CD8 single positive thymocytes. {ECO:0000269|PubMed:27657535}. +Q7TPN9 PRR14_MOUSE Proline-rich protein 14 612 67,811 Chain (1); Compositional bias (1); Modified residue (2); Region (4); Sequence caution (1) FUNCTION: Functions in tethering peripheral heterochromatin to the nuclear lamina during interphase, possibly through the interaction with heterochromatin protein CBX5/HP1 alpha (By similarity). Might play a role in reattaching heterochromatin to the nuclear lamina at mitotic exit (By similarity). Promotes myoblast differentiation during skeletal myogenesis, possibly by stimulating transcription factor MyoD activity via binding to CBX5/HP1 alpha (PubMed:25906157) (By similarity). Involved in the positive regulation of the PI3K-Akt-mTOR signaling pathway and in promoting cell proliferation, possibly via binding to GRB2 (By similarity). {ECO:0000250|UniProtKB:Q9BWN1, ECO:0000269|PubMed:25906157}. SUBCELLULAR LOCATION: Chromosome {ECO:0000250|UniProtKB:Q9BWN1}. Nucleus {ECO:0000250|UniProtKB:Q9BWN1}. Nucleus lamina {ECO:0000250|UniProtKB:Q9BWN1}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9BWN1}. Note=During interphase, associated with peripheral heterochromatin at the nuclear lamina. Released from the nuclear lamina in mitotic prophase and remains highly dispersed in metaphase. Associates with chromatin at the onset of anaphase and relocalizes to the nuclear lamina in telophase. {ECO:0000250|UniProtKB:Q9BWN1}. SUBUNIT: Interacts (via proline-rich region) with GRB2 (via SH3 domain 2). Interacts (via N-terminus) with CBX5. {ECO:0000250|UniProtKB:Q9BWN1}. +Q6PAN7 PRR18_MOUSE Proline-rich protein 18 307 32,214 Alternative sequence (1); Chain (1); Compositional bias (3); Erroneous initiation (1); Modified residue (4); Sequence conflict (4) +F2YMG0 PRS56_MOUSE Serine protease 56 (EC 3.4.21.-) 604 65,134 Active site (3); Chain (1); Disulfide bond (4); Domain (1); Frameshift (1); Glycosylation (1); Signal peptide (1) FUNCTION: Serine protease required during eye development. {ECO:0000269|PubMed:21532570}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21532570}; Peripheral membrane protein {ECO:0000269|PubMed:21532570}. TISSUE SPECIFICITY: Expressed in the eye: present in the retina and in the optic nerve. {ECO:0000269|PubMed:21397065, ECO:0000269|PubMed:21532570}. +Q99MS4 PRS29_MOUSE Serine protease 29 (EC 3.4.21.-) (Implantation serine proteinase 2) (ISP-2) (Strypsin-2) (Strypsin-related protein) (Tryptase-like proteinase) 279 30,986 Active site (3); Chain (1); Disulfide bond (4); Domain (1); Glycosylation (2); Sequence conflict (3); Signal peptide (1) FUNCTION: Involved in embryo hatching and implantation. {ECO:0000269|PubMed:11467974, ECO:0000269|PubMed:15304212, ECO:0000269|PubMed:17156484}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12112596, ECO:0000269|PubMed:15349836}. Note=Secretion into the glandular and uterine lumen may occur as a consequence of progesterone-induced epithelial differentiation. SUBUNIT: Homooligomer, heterodimer and heterotetramer. Able to form homo- and hetero- tetrameric structures. Heterotetramer is far more stable than the homotetramer. {ECO:0000269|PubMed:12112596, ECO:0000269|PubMed:15349836, ECO:0000269|PubMed:17156484}. TISSUE SPECIFICITY: Expressed in embryos and placenta. Found in uterus especially in glandular epithelium during zona lysis and implantation. {ECO:0000269|PubMed:11467974, ECO:0000269|PubMed:12112596}. +P46471 PRS7_MOUSE 26S proteasome regulatory subunit 7 (26S proteasome AAA-ATPase subunit RPT1) (Proteasome 26S subunit ATPase 2) (Protein MSS1) 433 48,648 Chain (1); Modified residue (2); Nucleotide binding (1); Sequence conflict (13) FUNCTION: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. PSMC2 belongs to the heterohexameric ring of AAA (ATPases associated with diverse cellular activities) proteins that unfolds ubiquitinated target proteins that are concurrently translocated into a proteolytic chamber and degraded into peptides. {ECO:0000250|UniProtKB:P35998}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P35998}. Note=Colocalizes with TRIM5 in cytoplasmic bodies. {ECO:0000250|UniProtKB:P35998}. SUBUNIT: Component of the 19S proteasome regulatory particle complex. The 26S proteasome consists of a 20S core particle (CP) and two 19S regulatory subunits (RP). The regulatory particle is made of a lid composed of 9 subunits, a base containing 6 ATPases including PSMC2 and few additional components. Interacts with NDC80 and SQSTM1. Interacts with PAAF1. Interacts with HIV-1 Tat. Interacts with TRIM5. {ECO:0000250|UniProtKB:P35998, ECO:0000269|PubMed:16857966, ECO:0000269|PubMed:22078707}. +Q80WM7 PRS33_MOUSE Serine protease 33 (EC 3.4.21.-) (Tryptase-6) (mT6) 277 29,888 Active site (3); Alternative sequence (1); Chain (1); Disulfide bond (4); Domain (1); Signal peptide (1) FUNCTION: Serine protease that has amidolytic activity, cleaving its substrates before Arg residues. {ECO:0000250}. PTM: Not glycosylated. {ECO:0000305}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14583634}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:14583634}. +Q9DAA4 PRS37_MOUSE Probable inactive serine protease 37 (Probable inactive trypsin-X2) 237 26,698 Chain (1); Disulfide bond (3); Domain (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Plays a role in male fertility (PubMed:23553430). May have a role in sperm migration or binding to zona-intact eggs (PubMed:23553430). Involved in the activation of the proacrosin/acrosin system (By similarity). {ECO:0000250|UniProtKB:A4D1T9, ECO:0000269|PubMed:23553430}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250|UniProtKB:A4D1T9}. Secreted {ECO:0000305}. TISSUE SPECIFICITY: Testis-specific (PubMed:23553430). Expressed in spermatids (PubMed:23553430). Weakly expressed in mature sperm (at protein level) (PubMed:23553430). {ECO:0000269|PubMed:23553430}. +P62196 PRS8_MOUSE 26S proteasome regulatory subunit 8 (26S proteasome AAA-ATPase subunit RPT6) (Proteasome 26S subunit ATPase 5) (Proteasome subunit p45) (p45/SUG) (mSUG1) 406 45,626 Chain (1); Initiator methionine (1); Modified residue (3); Nucleotide binding (1); Region (1); Sequence conflict (1) FUNCTION: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. PSMC5 belongs to the heterohexameric ring of AAA (ATPases associated with diverse cellular activities) proteins that unfolds ubiquitinated target proteins that are concurrently translocated into a proteolytic chamber and degraded into peptides. {ECO:0000250|UniProtKB:P62195}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P62195}. Nucleus {ECO:0000250|UniProtKB:P62195}. SUBUNIT: Component of the 19S proteasome regulatory particle complex. The 26S proteasome consists of a 20S core particle (CP) and two 19S regulatory subunits (RP). The regulatory particle is made of a lid composed of 9 subunits, a base containing 6 ATPases including PSMC5 and few additional components (By similarity). Component of a complex with USP49 and RUVBL1 (By similarity). Interacts with PRPF19 (PubMed:17349974). Interacts with TRIM5 (By similarity). Interacts with NDC80 (By similarity). Interacts with PAAF1 (By similarity). Interacts, in vitro, with the thyroid hormone receptor (in a thyroid hormone T3-dependent manner) and with retinoid X receptor (RXR) (PubMed:8598193). {ECO:0000250|UniProtKB:P62195, ECO:0000269|PubMed:17349974, ECO:0000269|PubMed:8598193}. +O55234 PSB5_MOUSE Proteasome subunit beta type-5 (EC 3.4.25.1) (Macropain epsilon chain) (Multicatalytic endopeptidase complex epsilon chain) (Proteasome chain 6) (Proteasome epsilon chain) (Proteasome subunit X) 264 28,532 Active site (1); Beta strand (13); Binding site (1); Chain (1); Helix (5); Propeptide (1); Sequence conflict (2); Turn (1) FUNCTION: Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). Within the 20S core complex, PSMB5 displays a chymotrypsin-like activity. {ECO:0000269|PubMed:16581775, ECO:0000269|PubMed:19183883, ECO:0000269|PubMed:22341445}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P28074}. Nucleus {ECO:0000250|UniProtKB:P28074}. SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is a barrel-shaped complex made of 28 subunits that are arranged in four stacked rings. The two outer rings are each formed by seven alpha subunits, and the two inner rings are formed by seven beta subunits. The proteolytic activity is exerted by three beta-subunits PSMB5, PSMB6 and PSMB7 (PubMed:16857966, PubMed:22341445). Directly interacts with POMP (By similarity). Interacts with ABCB1 and TAP1 (By similarity). {ECO:0000250|UniProtKB:P28074, ECO:0000269|PubMed:16857966, ECO:0000269|PubMed:22341445}. TISSUE SPECIFICITY: Expressed in uterus at the embryo implantation site. {ECO:0000269|PubMed:16434403, ECO:0000269|PubMed:22341445}. +Q8R5J9 PRAF3_MOUSE PRA1 family protein 3 (ADP-ribosylation factor-like protein 6-interacting protein 5) (ARL-6-interacting protein 5) (Aip-5) (Addicsin) (GTRAP3-18) (Glutamate transporter EAAC1-interacting protein) (Prenylated Rab acceptor protein 2) (Protein JWa) 188 21,558 Chain (1); Erroneous translation (1); Frameshift (1); Modified residue (1); Mutagenesis (2); Region (2); Sequence conflict (9); Topological domain (3); Transmembrane (4) TRANSMEM 40 60 Helical. {ECO:0000255}.; TRANSMEM 64 84 Helical. {ECO:0000255}.; TRANSMEM 93 113 Helical. {ECO:0000255}.; TRANSMEM 115 135 Helical. {ECO:0000255}. TOPO_DOM 1 39 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 85 92 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 136 188 Cytoplasmic. {ECO:0000250}. FUNCTION: Regulates intracellular concentrations of taurine and glutamate (By similarity). Negatively modulates SLC1A1/EAAC1 glutamate transport activity by decreasing its affinity for glutamate in a PKC activity-dependent manner (PubMed:12119102, PubMed:18684713). May be involved in membrane traffic (By similarity). {ECO:0000250|UniProtKB:Q9ES40, ECO:0000269|PubMed:12119102, ECO:0000269|PubMed:18684713}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12438930}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q9ES40}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:12438930}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12438930}. Note=Also exists as a soluble form in the cytoplasm. Associated with microtubules. {ECO:0000269|PubMed:12438930}. SUBUNIT: Homodimer. Heterodimer with ARL6IP1 (PubMed:18684713). Forms multimers. Interacts with prenylated RAB1A and RAB3A. Does not interact with VAMP1, VAMP2 or VAMP3 (By similarity). Interacts with ARL6 (PubMed:10508919). Interacts with SLC1A1/EAAC1 (PubMed:18684713, PubMed:12119102). {ECO:0000250|UniProtKB:Q9ES40, ECO:0000269|PubMed:10508919, ECO:0000269|PubMed:12119102, ECO:0000269|PubMed:18684713}. TISSUE SPECIFICITY: Expressed in the cerebral cortex, cerebellum, hippocampus, olfactory bulbs, medulla oblongate and limbic system (at protein level) (PubMed:18684713). Ubiquitous. {ECO:0000269|PubMed:12119102, ECO:0000269|PubMed:12438930, ECO:0000269|PubMed:18684713}. +Q9DAS4 PR8A8_MOUSE Prolactin-8A8 (Placental prolactin-like protein C3) (PLP-C3) (PRL-like protein C3) (Prolactin-like protein C-gamma) (PLP C-gamma) 241 28,089 Alternative sequence (1); Chain (1); Disulfide bond (3); Glycosylation (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000250}. TISSUE SPECIFICITY: Expressed specifically in the placenta. Predominantly expressed in spongiotrophoblast cells. +Q3UTQ7 PRD10_MOUSE PR domain zinc finger protein 10 (EC 2.1.1.-) (PR domain-containing protein 10) (Tristanin) 1184 133,746 Alternative sequence (2); Chain (1); Compositional bias (5); Cross-link (1); Domain (1); Modified residue (2); Sequence conflict (1); Zinc finger (9) FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12175877}. DOMAIN: The SET domain is degenerated, suggesting that it has lost methyltransferase activity. TISSUE SPECIFICITY: Present in brain, liver, kidney, spleen and thymus (at protein level). {ECO:0000269|PubMed:12175877}. +Q9WUQ2 PREB_MOUSE Prolactin regulatory element-binding protein (Mammalian guanine nucleotide exchange factor mSec12) 417 45,437 Chain (1); Modified residue (1); Repeat (3); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 389 409 Helical. {ECO:0000255}. TOPO_DOM 1 388 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 410 417 Lumenal. {ECO:0000255}. FUNCTION: Guanine nucleotide exchange factor that specifically activates the small GTPase SAR1B. Mediates the recruitement of SAR1B and other COPII coat components to endoplasmic reticulum membranes and is therefore required for the formation of COPII transport vesicles from the ER. {ECO:0000269|PubMed:11422940}.; FUNCTION: Was first identified based on its probable role in the regulation of pituitary gene transcription. Binds to the prolactin gene (PRL) promoter and seems to activate transcription. {ECO:0000250|UniProtKB:Q9WTV0}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9WTV0}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9WTV0}. Nucleus {ECO:0000250|UniProtKB:Q9WTV0}. Note=Concentrates at endoplasmic reticulum exit sites (ERES), also known as transitional endoplasmic reticulum (tER). {ECO:0000250|UniProtKB:Q9HCU5}. SUBUNIT: Interacts with SAR1B (GDP-bound form) (PubMed:11422940). Interacts with MIA2; recruits PREB to endoplasmic reticulum exit sites (By similarity). {ECO:0000250|UniProtKB:Q9HCU5, ECO:0000269|PubMed:11422940}. +Q8K411 PREP_MOUSE Presequence protease, mitochondrial (EC 3.4.24.-) (Pitrilysin metalloproteinase 1) 1036 117,372 Active site (1); Alternative sequence (2); Chain (1); Disulfide bond (1); Erroneous initiation (1); Metal binding (3); Modified residue (6); Natural variant (6); Sequence conflict (7); Transit peptide (1) FUNCTION: Metalloendopeptidase of the mitochondrial matrix that functions in peptide cleavage and degradation rather than in protein processing. Has an ATP-independent activity. Specifically cleaves peptides in the range of 5 to 65 residues. Shows a preference for cleavage after small polar residues and before basic residues, but without any positional preference. Degrades the transit peptides of mitochondrial proteins after their cleavage. Also degrades other unstructured peptides. It is also able to degrade amyloid-beta protein 40, one of the peptides produced by APP processing, when it accumulates in mitochondrion. It is a highly efficient protease, at least toward amyloid-beta protein 40. Cleaves that peptide at a specific position and is probably not processive, releasing digested peptides intermediates that can be further cleaved subsequently. {ECO:0000250|UniProtKB:Q5JRX3}. PTM: A disulfide bond locks the enzyme in the closed conformation preventing substrate entry into the catalytic chamber. {ECO:0000250|UniProtKB:Q5JRX3}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:Q5JRX3}. SUBUNIT: Monomer and homodimer; homodimerization is induced by binding of the substrate. {ECO:0000250|UniProtKB:Q5JRX3}. +A2A935 PRD16_MOUSE PR domain zinc finger protein 16 (PR domain-containing protein 16) (Transcription factor MEL1) (MDS1/EVI1-like gene 1) 1275 140,858 Alternative sequence (4); Chain (1); Compositional bias (1); Domain (1); Mutagenesis (2); Region (2); Sequence conflict (5); Zinc finger (10) FUNCTION: Binds DNA and functions as a transcriptional regulator. Functions in the differentiation of brown adipose tissue (BAT) which is specialized in dissipating chemical energy in the form of heat in response to cold or excess feeding while white adipose tissue (WAT) is specialized in the storage of excess energy and the control of systemic metabolism. Together with CEBPB, regulates the differentiation of myoblastic precursors into brown adipose cells. Functions also as a repressor of TGF-beta signaling. May regulate granulocytes differentiation. {ECO:0000269|PubMed:17618855, ECO:0000269|PubMed:18483224, ECO:0000269|PubMed:18719582, ECO:0000269|PubMed:19641492}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18483224}. SUBUNIT: Interacts with CEBPA, CEBPB and CEBPD; the interaction is direct (PubMed:19641492). Interacts with PPARG and PPARA; controls brown adipocytes (PubMed:18719582). Interacts with CTBP1 and CTBP2; represses the expression of WAT-specific genes (PubMed:18483224). Interacts with PPARGC1A and PPARGC1B; interaction with PPARGC1A or PPARGC1B activates the transcription of BAT-specific gene (PubMed:18483224, PubMed:17618855). Interacts with HDAC1, SKI and SMAD2; the interaction with SKI promotes the recruitment of SMAD3-HDAC1 complex on the promoter of TGF-beta target genes (Probable). Interacts with ZNF516; the interaction is direct and may play a role in the transcription of brown adipose tissue-specific gene (PubMed:25578880). {ECO:0000269|PubMed:17618855, ECO:0000269|PubMed:18483224, ECO:0000269|PubMed:18719582, ECO:0000269|PubMed:19641492, ECO:0000269|PubMed:25578880, ECO:0000305|PubMed:17467076}. TISSUE SPECIFICITY: Enriched in BAT compared to WAT. Detected in heart, lung, kidney and brain. Expressed in nuclei of cardiomyocytes. {ECO:0000269|PubMed:17618855, ECO:0000269|PubMed:23768516}. +Q7TSC1 PRC2A_MOUSE Protein PRRC2A (HLA-B-associated transcript 2) (Proline-rich and coiled-coil-containing protein 2A) 2158 229,203 Chain (1); Compositional bias (12); Modified residue (53); Region (3); Repeat (9); Sequence conflict (1) FUNCTION: May play a role in the regulation of pre-mRNA splicing. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. +P20108 PRDX3_MOUSE Thioredoxin-dependent peroxide reductase, mitochondrial (EC 1.11.1.15) (Antioxidant protein 1) (AOP-1) (PRX III) (Perioredoxin-3) (Protein MER5) 257 28,127 Active site (1); Chain (1); Disulfide bond (2); Domain (1); Modified residue (4); Transit peptide (1) FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. {ECO:0000250|UniProtKB:P30048}. PTM: Phosphorylated by LRRK2; phosphorylation reduces perodixase activity. {ECO:0000250|UniProtKB:P30048}.; PTM: The enzyme can be inactivated by further oxidation of the cysteine sulfenic acid (C(P)-SOH) to sulphinic acid (C(P)-SO2H) and sulphonic acid (C(P)-SO3H) instead of its condensation to a disulfide bond. {ECO:0000250|UniProtKB:P30048}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:9497357}. Cytoplasm {ECO:0000250|UniProtKB:P30048}. Early endosome {ECO:0000250|UniProtKB:P30048}. Note=Localizes to early endosomes in a RPS6KC1-dependent manner. {ECO:0000250|UniProtKB:P30048}. SUBUNIT: Homodimer; disulfide-linked, upon oxidation. 6 homodimers assemble to form a ring-like dodecamer. Interacts with NEK6. Interacts with LRRK2. Interacts with RPS6KC1 (via PX domain). {ECO:0000250|UniProtKB:P30048}. TISSUE SPECIFICITY: Housekeeping-type gene preferentially expressed in murine erythroleukemia (MEL) cells. +O08807 PRDX4_MOUSE Peroxiredoxin-4 (EC 1.11.1.15) (Antioxidant enzyme AOE372) (Peroxiredoxin IV) (Prx-IV) (Thioredoxin peroxidase AO372) (Thioredoxin-dependent peroxide reductase A0372) 274 31,053 Active site (1); Beta strand (8); Chain (1); Disulfide bond (2); Domain (1); Helix (7); Signal peptide (1); Turn (1) FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events (PubMed:11229364). Regulates the activation of NF-kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation (By similarity). {ECO:0000250|UniProtKB:Q13162, ECO:0000269|PubMed:11229364}. PTM: The enzyme can be inactivated by further oxidation of the cysteine sulfenic acid (C(P)-SOH) to sulphinic acid (C(P)-SO2H) and sulphonic acid (C(P)-SO3H) instead of its condensation to a disulfide bond. {ECO:0000250|UniProtKB:Q13162}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13162}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q13162}. Note=Not secreted. {ECO:0000269|PubMed:11229364}. SUBUNIT: Homodimer; disulfide-linked, upon oxidation. 5 homodimers assemble to form a ring-like decamer. {ECO:0000250|UniProtKB:Q13162}. +Q8VHJ7 PRGC2_MOUSE Peroxisome proliferator-activated receptor gamma coactivator 1-beta (PGC-1-beta) (PPAR-gamma coactivator 1-beta) (PPARGC-1-beta) (ERR ligand 1) 1014 112,075 Alternative sequence (1); Chain (1); Compositional bias (3); Domain (1); Modified residue (5); Motif (4); Region (1); Sequence conflict (2) FUNCTION: Plays a role of stimulator of transcription factors and nuclear receptors activities. Activates transcriptional activity of estrogen receptor alpha, nuclear respiratory factor 1 (NRF1) and glucocorticoid receptor in the presence of glucocorticoids. May play a role in constitutive non-adrenergic-mediated mitochondrial biogenesis as suggested by increased basal oxygen consumption and mitochondrial number when overexpressed. May be part of the pathways regulating the elevation of gluconeogenesis, beta-oxidation of fatty acids and ketogenesis during fasting. Stimulates SREBP-mediated lipogenic gene expression in the liver. Induces energy expenditure and antagonizes obesity when overexpressed. Induces also the expression of mitochondrial genes involved in oxidative metabolism. Induces the expression of PERM1 in the skeletal muscle in an ESRRA-dependent manner. {ECO:0000269|PubMed:11733490, ECO:0000269|PubMed:12678921, ECO:0000269|PubMed:14530391, ECO:0000269|PubMed:15680331}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with estrogen receptor alpha/ESR1 (By similarity). Interacts with hepatocyte nuclear factor 4-alpha/HNF4A, Sterol regulatory binding transcription factor 1/SREBF1, PPAR-alpha/PPARA, thyroid hormone receptor beta/THRB and host cell factor/HCFC1. Interacts with estrogen-related receptor gamma/ESRRG and alpha/ESRRA. Interacts with PRDM16. {ECO:0000250, ECO:0000269|PubMed:11733490, ECO:0000269|PubMed:12470660, ECO:0000269|PubMed:14530391, ECO:0000269|PubMed:15680331, ECO:0000269|PubMed:17618855, ECO:0000269|PubMed:18483224}. DOMAIN: Contains 3 Leu-Xaa-Xaa-Leu-Leu (LXXLL) motif, which are usually required for the association with nuclear receptors. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous with higher expression in heart, brown adipose tissue, brain and skeletal muscle. {ECO:0000269|PubMed:11733490, ECO:0000269|PubMed:12678921}. +Q00175 PRGR_MOUSE Progesterone receptor (PR) (Nuclear receptor subfamily 3 group C member 3) 926 98,981 Alternative sequence (1); Chain (1); Cross-link (4); DNA binding (1); Domain (1); Frameshift (1); Modified residue (10); Motif (3); Region (5); Sequence conflict (15); Zinc finger (2) FUNCTION: The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Depending on the isoform, progesterone receptor functions as transcriptional activator or repressor. {ECO:0000250|UniProtKB:P06401}.; FUNCTION: Isoform A: Ligand-dependent transdominant repressor of steroid hormone receptor transcriptional activity including repression of its isoform B, MR and ER. Transrepressional activity may involve recruitment of corepressor NCOR2. {ECO:0000250|UniProtKB:P06401}.; FUNCTION: Isoform B: Transcriptional activator of several progesteron-dependent promoters in a variety of cell types. Involved in activation of SRC-dependent MAPK signaling on hormone stimulation. {ECO:0000250|UniProtKB:P06401}. PTM: Phosphorylated on multiple serine sites. Several of these sites are hormone-dependent. Phosphorylation on Ser-294 is highly hormone-dependent and modulates ubiquitination and sumoylation on Lys-388. Phosphorylation on Ser-345 also requires induction by hormone. Basal phosphorylation on Ser-82, Ser-163, Ser-191 and Ser-400 is increased in response to progesterone and can be phosphorylated in vitro by the CDK2-A1 complex. Increased levels of phosphorylation on Ser-400 also in the presence of EGF, heregulin, IGF, PMA and FBS. Phosphorylation at this site by CDK2 is ligand-independent, and increases nuclear translocation and transcriptional activity. Phosphorylation at Ser-163 and Ser-294, but not at Ser-191, is impaired during the G(2)/M phase of the cell cycle. Phosphorylation on Ser-345 by ERK1/2 MAPK is required for interaction with SP1 (By similarity). {ECO:0000250}.; PTM: Sumoylation is hormone-dependent and represses transcriptional activity. Sumoylation on all three sites is enhanced by PIAS3. Desumoylated by SENP1. Sumoylation on Lys-388, the main site of sumoylation, is repressed by ubiquitination on the same site, and modulated by phosphorylation at Ser-294 (By similarity). {ECO:0000250}.; PTM: Ubiquitination is hormone-dependent and represses sumoylation on the same site. Promoted by MAPK-mediated phosphorylation on Ser-294 (By similarity). {ECO:0000250}.; PTM: Palmitoylated by ZDHHC7 and ZDHHC21. Palmitoylation is required for plasma membrane targeting and for rapid intracellular signaling via ERK and AKT kinases and cAMP generation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Nucleoplasmic shuttling is both hormone- and cell cycle-dependent. On hormone stimulation, retained in the cytoplasm in the G(1) and G(2)/M phases (By similarity). {ECO:0000250}. SUBUNIT: Interacts with SMARD1 and UNC45A. Interacts with CUEDC2; the interaction promotes ubiquitination, decreases sumoylation, and represses transcriptional activity. Interacts with PIAS3; the interaction promotes sumoylation of PR in a hormone-dependent manner, inhibits DNA-binding, and alters nuclear export. Interacts with SP1; the interaction requires ligand-induced phosphorylation on Ser-294 by ERK1/2 MAPK. Interacts with PRMT2 (By similarity). Isoform A interacts with NCOR2. Isoform B (but not isoform A) interacts with NCOA2 and NCOA1. Isoform B (but not isoform A) interacts with KLF9. {ECO:0000250|UniProtKB:P06401, ECO:0000269|PubMed:12672823}. DOMAIN: Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain. TISSUE SPECIFICITY: Expression of isoform A and isoform B in mammary epithelial cells is temporally and spatially separated during normal mammary gland development. Isoform A and isoform B are expressed in the pituitary. Isoform A and isoform B are differentially expressed in the ovary and oviduct, and the level of expression is dependent on both the cell type and estrous cycle stage. {ECO:0000269|PubMed:15044369, ECO:0000269|PubMed:15878961, ECO:0000269|PubMed:17003284}. +P05142 PRH1_MOUSE Proline-rich protein HaeIII subfamily 1 (Proline-rich protein MP-2) 261 26,090 Chain (1); Sequence conflict (8); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q9DBU3 RIOK3_MOUSE Serine/threonine-protein kinase RIO3 (EC 2.7.11.1) (RIO kinase 3) 519 58,704 Active site (1); Binding site (1); Chain (1); Domain (1); Modified residue (6); Nucleotide binding (1); Sequence conflict (2) FUNCTION: Involved in regulation of type I interferon (IFN)-dependent immune response which plays a critical role in the innate immune response against DNA and RNA viruses. May act as an adapter protein essential for the recruitment of TBK1 to IRF3. Phosphorylates IFIH1 on 'Ser-828' interfering with IFIH1 filament assembly on long dsRNA and resulting in attenuated IFIH1-signaling. Can inhibit CASP10 isoform 7-mediated activation of the NF-kappaB signaling pathway. May play a role in the biogenesis of the 40S ribosomal subunit. Involved in the processing of 21S pre-rRNA to the mature 18S rRNA. {ECO:0000250|UniProtKB:O14730}. PTM: Autophosphorylated (in vitro). {ECO:0000250|UniProtKB:O14730}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O14730}. SUBUNIT: Interacts with CASP10. Interacts with IRF3; RIOK3 probybly mediates the interaction of TBK1 with IRF3. Associated with 40S pre-ribosomal particles. {ECO:0000250|UniProtKB:O14730}. +Q9JJF3 RIOX1_MOUSE Ribosomal oxygenase 1 (Bifunctional lysine-specific demethylase and histidyl-hydroxylase NO66) (EC 1.14.11.-) (EC 1.14.11.27) (Histone lysine demethylase NO66) 603 67,557 Chain (1); Domain (1); Metal binding (3); Modified residue (4); Mutagenesis (2); Sequence conflict (1) FUNCTION: Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase Also catalyzes the hydroxylation of 60S ribosomal protein L8 on 'His-216'. Acts as a regulator of osteoblast differentiation via its interaction with SP7/OSX by demethylating H3K4me and H3K36me, thereby inhibiting SP7/OSX-mediated promoter activation. May also play a role in ribosome biogenesis and in the replication or remodeling of certain heterochromatic region. Participates in MYC-induced transcriptional activation (By similarity). Specifically demethylates 'Lys-4' (H3K4me) and 'Lys-36' (H3K36me) of histone H3, thereby playing a central role in histone code. Preferentially demethylates trimethylated H3 'Lys-4' (H3K4me3) and monomethylated H3 'Lys-4' (H3K4me1) residues, while it has weaker activity for dimethylated H3 'Lys-36' (H3K36me2). {ECO:0000250, ECO:0000269|PubMed:19927124}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000269|PubMed:14742713, ECO:0000269|PubMed:19927124}. SUBUNIT: Interacts with SP7/OSX; the interaction is direct. Interacts with PHF19; leading to its recruitment to H3K36me3 sites. Interacts with MYC (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Present in developing bones (at protein level). Widely but not ubiquitously expressed. +P62962 PROF1_MOUSE Profilin-1 (Profilin I) 140 14,957 Chain (1); Cross-link (2); Initiator methionine (1); Modified residue (6) FUNCTION: Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG. Inhibits androgen receptor (AR) and HTT aggregation and binding of G-actin is essential for its inhibition of AR (By similarity). {ECO:0000250}. PTM: Phosphorylation at Ser-138 reduces its affinity for G-actin and blocks its interaction with HTT, reducing its ability to inhibit androgen receptor (AR) and HTT aggregation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SUBUNIT: Interacts with VASP. Occurs in many kinds of cells as a complex with monomeric actin in a 1:1 ratio. Found in a complex with XPO6, Ran, ACTB and PFN1 (By similarity). Interacts with HTT (By similarity). {ECO:0000250}. +P05143 PRP2_MOUSE Proline-rich protein 2 (Proline-rich protein MP-3) 317 31,719 Alternative sequence (1); Chain (1); Compositional bias (1); Glycosylation (1); Sequence conflict (6); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q3UUY6 PROM2_MOUSE Prominin-2 (PROM-2) (Prominin-like protein 2) (mPROML2) 835 93,206 Alternative sequence (1); Chain (1); Coiled coil (1); Frameshift (1); Glycosylation (1); Modified residue (1); Sequence conflict (2); Signal peptide (1); Topological domain (6); Transmembrane (5) TRANSMEM 107 127 Helical. {ECO:0000255}.; TRANSMEM 154 174 Helical. {ECO:0000255}.; TRANSMEM 436 456 Helical. {ECO:0000255}.; TRANSMEM 479 499 Helical. {ECO:0000255}.; TRANSMEM 781 801 Helical. {ECO:0000255}. TOPO_DOM 28 106 Extracellular. {ECO:0000255}.; TOPO_DOM 128 153 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 175 435 Extracellular. {ECO:0000255}.; TOPO_DOM 457 478 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 500 780 Extracellular. {ECO:0000255}.; TOPO_DOM 802 835 Cytoplasmic. {ECO:0000255}. PTM: Glycosylated. {ECO:0000269|PubMed:17109118}. SUBCELLULAR LOCATION: Apical cell membrane; Multi-pass membrane protein. Basolateral cell membrane; Multi-pass membrane protein. Cell projection, microvillus membrane; Multi-pass membrane protein. Cell projection, cilium membrane; Multi-pass membrane protein. Note=Colocalizes with PROM1 (By similarity). Associates with membrane in a cholesterol-dependent manner. Localizes to the apical and basolateral membranes of epithelial cells. {ECO:0000250}. SUBUNIT: Binds cholesterol. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in kidney and testis. Present in urine within small membrane particles (at protein level). In the submandibular gland, expressed in seromucous acini. In the parotid gland, expressed in the serous acini and in all segments of the duct system. In the sublingual gland, expressed in large excretory ducts, but absent in intercalated ducts. In the extraorbital lacrimal gland, expressed in the serous acini. In the eyelid, expressed in the acini of the meibomian gland. {ECO:0000269|PubMed:12514187, ECO:0000269|PubMed:17109118, ECO:0000269|PubMed:17874118}. +Q9D7G0 PRPS1_MOUSE Ribose-phosphate pyrophosphokinase 1 (EC 2.7.6.1) (Phosphoribosyl pyrophosphate synthase I) (PRS-I) 318 34,834 Binding site (1); Chain (1); Metal binding (4); Nucleotide binding (1); Region (1); Sequence conflict (1) Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I): step 1/1. FUNCTION: Catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP) that is essential for nucleotide synthesis. SUBUNIT: Homodimer. The active form is probably a hexamer composed of 3 homodimers (By similarity). {ECO:0000250}. +P62334 PRS10_MOUSE 26S proteasome regulatory subunit 10B (26S proteasome AAA-ATPase subunit RPT4) (Proteasome 26S subunit ATPase 6) (Proteasome subunit p42) 389 44,173 Chain (1); Modified residue (3); Nucleotide binding (1); Sequence conflict (4) FUNCTION: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. PSMC6 belongs to the heterohexameric ring of AAA (ATPases associated with diverse cellular activities) proteins that unfolds ubiquitinated target proteins that are concurrently translocated into a proteolytic chamber and degraded into peptides. {ECO:0000250|UniProtKB:P62333}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Component of the 19S proteasome regulatory particle complex. The 26S proteasome consists of a 20S core particle (CP) and two 19S regulatory subunits (RP). The regulatory particle is made of a lid composed of 9 subunits, a base containing 6 ATPases including PSMC6 and few additional components. Interacts with PAAF1. {ECO:0000250|UniProtKB:P62333, ECO:0000269|PubMed:16857966}. +Q61096 PRTN3_MOUSE Myeloblastin (EC 3.4.21.76) (Proteinase 3) (PR-3) 254 27,626 Active site (3); Chain (1); Disulfide bond (4); Domain (1); Glycosylation (2); Propeptide (2); Sequence conflict (1); Signal peptide (1) FUNCTION: Serine protease that degrades elastin, fibronectin, laminin, vitronectin, and collagen types I, III, and IV (in vitro). By cleaving and activating receptor F2RL1/PAR-2, enhances endothelial cell barrier function and thus vascular integrity during neutrophil transendothelial migration. May play a role in neutrophil transendothelial migration, probably when associated with CD177. {ECO:0000250|UniProtKB:P24158}. SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:P24158}. Secreted {ECO:0000250|UniProtKB:P24158}. Cell membrane {ECO:0000250|UniProtKB:P24158}; Peripheral membrane protein {ECO:0000250|UniProtKB:P24158}; Extracellular side {ECO:0000250|UniProtKB:P24158}. Membrane raft {ECO:0000250|UniProtKB:P24158}; Peripheral membrane protein {ECO:0000250|UniProtKB:P24158}; Extracellular side {ECO:0000250|UniProtKB:P24158}. Note=Localizes predominantly to azurophil granules (primary secretory granules) in neutrophils. Secreted upon neutrophil stimulation by TNF-alpha, lipopolysaccharide (LPS), fMLP and CXCL8/IL8 or during neutrophil transmigration. Following secretion tethered to the cell membrane by CD177. {ECO:0000250|UniProtKB:P24158}. SUBUNIT: May form dimers. Interacts with CD177; the interaction tethers PRTN3 to the cell surface; the interaction is direct. {ECO:0000250|UniProtKB:P24158}. +O35955 PSB10_MOUSE Proteasome subunit beta type-10 (EC 3.4.25.1) (Low molecular mass protein 10) (Macropain subunit MECl-1) (Multicatalytic endopeptidase complex subunit MECl-1) (Proteasome MECl-1) (Proteasome subunit beta-2i) 273 29,063 Active site (1); Beta strand (14); Chain (1); Helix (4); Modified residue (1); Mutagenesis (1); Propeptide (1); Sequence conflict (3); Site (1); Turn (1) FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processing to generate class I binding peptides. Plays a role in determining the T-cell repertoire for an antiviral T-cell response. {ECO:0000269|PubMed:22341445}. PTM: Autocleaved. The resulting N-terminal Thr residue of the mature subunit is responsible for the nucleophile proteolytic activity. {ECO:0000305|PubMed:10413086}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}. Nucleus {ECO:0000250}. SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel. Component of the immunoproteasome, where it displaces the equivalent housekeeping subunit PSMB7. Component of the spermatoproteasome, a form of the proteasome specifically found in testis. {ECO:0000269|PubMed:16857966, ECO:0000269|PubMed:22341445, ECO:0000269|PubMed:23706739}. TISSUE SPECIFICITY: Detected in liver (at protein level). {ECO:0000269|PubMed:22341445}. +P99027 RLA2_MOUSE 60S acidic ribosomal protein P2 115 11,651 Chain (1); Modified residue (9); Sequence conflict (3) FUNCTION: Plays an important role in the elongation step of protein synthesis. SUBUNIT: Heterodimer with RPLP1 at the lateral ribosomal stalk of the large ribosomal subunit. {ECO:0000250}. +Q7TT28 REXO1_MOUSE RNA exonuclease 1 homolog (EC 3.1.-.-) (Transcription elongation factor B polypeptide 3-binding protein 1) 1213 130,790 Alternative sequence (3); Chain (1); Coiled coil (1); Compositional bias (2); Domain (1); Erroneous initiation (1); Modified residue (7); Sequence conflict (6) FUNCTION: Seems to have no detectable effect on transcription elongation in vitro. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with TCEA2 and ELOA. {ECO:0000250}. +Q00915 RET1_MOUSE Retinol-binding protein 1 (Cellular retinol-binding protein) (CRBP) (Cellular retinol-binding protein I) (CRBP-I) (mCRBPI) 135 15,846 Binding site (3); Chain (1); Region (1) FUNCTION: Cytoplasmic retinol-binding protein. Accepts retinol from the transport protein STRA6, and thereby contributes to retinol uptake, storage and retinoid homeostasis. {ECO:0000269|PubMed:10487743, ECO:0000269|PubMed:15632377, ECO:0000269|PubMed:22665496}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10487743}. Lipid droplet {ECO:0000269|PubMed:15632377}. SUBUNIT: Interacts (only as retinol-free apoprotein) with STRA6. {ECO:0000250|UniProtKB:P09455}. DOMAIN: Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior. {ECO:0000250|UniProtKB:P09455}. +Q9CYN9 RENR_MOUSE Renin receptor (ATPase H(+)-transporting lysosomal accessory protein 2) (ATPase H(+)-transporting lysosomal-interacting protein 2) (Renin/prorenin receptor) 350 39,092 Chain (1); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 303 323 Helical. {ECO:0000255}. TOPO_DOM 18 302 Extracellular. {ECO:0000255}.; TOPO_DOM 324 350 Cytoplasmic. {ECO:0000255}. FUNCTION: Functions as a renin and prorenin cellular receptor. May mediate renin-dependent cellular responses by activating ERK1 and ERK2. By increasing the catalytic efficiency of renin in AGT/angiotensinogen conversion to angiotensin I, it may also play a role in the renin-angiotensin system (RAS) (By similarity). {ECO:0000250}. PTM: Phosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Interacts with renin and the vacuolar proton-ATPase. {ECO:0000250}. +Q8K426 RETNG_MOUSE Resistin-like gamma (Resistin-like molecule gamma) (RELMgamma) (Ten-cysteine protein 1) (XCP1) 117 12,535 Chain (1); Disulfide bond (5); Erroneous initiation (3); Signal peptide (1) FUNCTION: Probable hormone (Probable). Promotes chemotaxis in myeloid cells (PubMed:15064728). {ECO:0000269|PubMed:15064728, ECO:0000305}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14733912, ECO:0000269|PubMed:15064728, ECO:0000269|PubMed:15834545}. SUBUNIT: Homodimer. Heterodimer with RETNLB. {ECO:0000269|PubMed:15834545}. TISSUE SPECIFICITY: Expressed in colon, lung, spleen, pancreas, ileum and bone marrow (at protein level) (PubMed:15834545). In colon, found throughout the crypt and surface epithelium, including goblet cells (at protein level) (PubMed:15834545). Highest expression is observed in bone marrow, spleen and lung, with lower levels in other tissues (PubMed:12782128, PubMed:14733912, PubMed:15064728, PubMed:15834545). Detected at low levels in granulocytes, but not found in monocytes or lymphocytes (PubMed:14733912). Has very weak expression in white adipose tissue (PubMed:12782128). {ECO:0000269|PubMed:12782128, ECO:0000269|PubMed:14733912, ECO:0000269|PubMed:15064728, ECO:0000269|PubMed:15834545}. +Q8VEL9 REM2_MOUSE GTP-binding protein REM 2 (Rad and Gem-like GTP-binding protein 2) 341 37,367 Alternative sequence (1); Beta strand (6); Chain (1); Erroneous initiation (2); Helix (7); Modified residue (2); Nucleotide binding (3); Sequence conflict (2); Turn (1) FUNCTION: Binds GTP saturably and exhibits a low intrinsic rate of GTP hydrolysis. {ECO:0000250|UniProtKB:Q9WTY2}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9WTY2}. +Q3UZ01 RNPC3_MOUSE RNA-binding region-containing protein 3 (RNA-binding motif protein 40) (RNA-binding protein 40) 514 57,972 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (2); Erroneous initiation (1); Modified residue (3); Sequence conflict (3) FUNCTION: Participates in pre-mRNA U12-dependent splicing, performed by the minor spliceosome which removes U12-type introns. U12-type introns comprises less than 1% of all non-coding sequences. Binds to the 3'-stem-loop of m(7)G-capped U12 snRNA (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the U11/U12 snRNPs that are part of the U12-type spliceosome. Found in a complex with m(7)G-capped U12 snRNA. Interacts with PDCD7 (By similarity). {ECO:0000250}. +Q9Z139 ROR1_MOUSE Inactive tyrosine-protein kinase transmembrane receptor ROR1 (mROR1) (Neurotrophic tyrosine kinase, receptor-related 1) 937 104,088 Binding site (1); Chain (1); Compositional bias (3); Disulfide bond (9); Domain (4); Glycosylation (4); Modified residue (1); Nucleotide binding (1); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 407 427 Helical. {ECO:0000255}. TOPO_DOM 30 406 Extracellular. {ECO:0000255}.; TOPO_DOM 428 937 Cytoplasmic. {ECO:0000255}. FUNCTION: Has very low kinase activity in vitro and is unlikely to function as a tyrosine kinase in vivo (By similarity). Receptor for ligand WNT5A which activate downstream NFkB signaling pathway and may result in the inhibition of WNT3A-mediated signaling (By similarity). In inner ear, crucial for spiral ganglion neurons to innervate auditory hair cells (PubMed:27162350). {ECO:0000250|UniProtKB:Q01973, ECO:0000269|PubMed:27162350}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:27162350}; Single-pass type I membrane protein. Cell projection, axon {ECO:0000269|PubMed:27162350}. TISSUE SPECIFICITY: At postnatal P0, expressed in heart, lung, liver, kidney, spleen and inner ear. {ECO:0000269|PubMed:27162350}. +Q9Z138 ROR2_MOUSE Tyrosine-protein kinase transmembrane receptor ROR2 (mROR2) (EC 2.7.10.1) (Neurotrophic tyrosine kinase, receptor-related 2) 944 105,005 Active site (1); Binding site (1); Chain (1); Compositional bias (3); Disulfide bond (9); Domain (4); Glycosylation (3); Modified residue (2); Nucleotide binding (1); Sequence conflict (6); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 404 424 Helical. {ECO:0000255}. TOPO_DOM 34 403 Extracellular. {ECO:0000255}.; TOPO_DOM 425 944 Cytoplasmic. {ECO:0000255}. FUNCTION: Tyrosine-protein kinase receptor which may be involved in the early formation of the chondrocytes. It seems to be required for cartilage and growth plate development (PubMed:10700181). Phosphorylates YWHAB, leading to induction of osteogenesis and bone formation. In contrast, has also been shown to have very little tyrosine kinase activity in vitro. May act as a receptor for wnt ligand WNT5A which may result in the inhibition of WNT3A-mediated signaling (By similarity). {ECO:0000250|UniProtKB:Q01974, ECO:0000269|PubMed:10700181}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19785987}; Single-pass type I membrane protein {ECO:0000269|PubMed:19785987}. SUBUNIT: Homodimer; promotes osteogenesis. Binds YWHAB (By similarity). Interacts with WTIP (PubMed:19785987). {ECO:0000250|UniProtKB:Q01974, ECO:0000269|PubMed:19785987}. +P51448 RORA_MOUSE Nuclear receptor ROR-alpha (Nuclear receptor RZR-alpha) (Nuclear receptor subfamily 1 group F member 1) (RAR-related orphan receptor A) (Retinoid-related orphan receptor-alpha) 523 58,845 Alternative sequence (1); Chain (1); Compositional bias (1); Cross-link (1); DNA binding (1); Domain (1); Erroneous initiation (2); Modified residue (2); Motif (1); Natural variant (1); Sequence conflict (13); Zinc finger (2) FUNCTION: Nuclear receptor that binds DNA as a monomer to ROR response elements (RORE) containing a single core motif half-site 5'-AGGTCA-3' preceded by a short A-T-rich sequence. Key regulator of embryonic development, cellular differentiation, immunity, circadian rhythm as well as lipid, steroid, xenobiotics and glucose metabolism. Considered to have intrinsic transcriptional activity, have some natural ligands like oxysterols that act as agonists (25-hydroxycholesterol) or inverse agonists (7-oxygenated sterols), enhancing or repressing the transcriptional activity, respectively. Recruits distinct combinations of cofactors to target genes regulatory regions to modulate their transcriptional expression, depending on the tissue, time and promoter contexts. Regulates genes involved in photoreceptor development including OPN1SW, OPN1SM and ARR3 and skeletal muscle development with MYOD1. Required for proper cerebellum development, regulates SHH gene expression, among others, to induce granule cells proliferation as well as expression of genes involved in calcium-mediated signal transduction. Regulates the circadian expression of several clock genes, including CLOCK, ARNTL/BMAL1, NPAS2 and CRY1. Competes with NR1D1 for binding to their shared DNA response element on some clock genes such as ARNTL/BMAL1, CRY1 and NR1D1 itself, resulting in NR1D1-mediated repression or RORA-mediated activation of clock genes expression, leading to the circadian pattern of clock genes expression. Therefore influences the period length and stability of the clock. Regulates genes involved in lipid metabolism such as apolipoproteins APOA1, APOA5, APOC3 and PPARG. In liver, has specific and redundant functions with RORC as positive or negative modulator of expression of genes encoding phase I and phase II proteins involved in the metabolism of lipids, steroids and xenobiotics, such as CYP7B1 and SULT2A1. Induces a rhythmic expression of some of these genes. In addition, interplays functionally with NR1H2 and NR1H3 for the regulation of genes involved in cholesterol metabolism. Also involved in the regulation of hepatic glucose metabolism through the modulation of G6PC and PCK1. In adipose tissue, plays a role as negative regulator of adipocyte differentiation, probably acting through dual mechanisms. May suppress CEBPB-dependent adipogenesis through direct interaction and PPARG-dependent adipogenesis through competition for DNA-binding. Downstream of IL6 and TGFB and synergistically with RORC isoform 2, is implicated in the lineage specification of uncommitted CD4(+) T-helper (T(H)) cells into T(H)17 cells, antagonizing the T(H)1 program. Probably regulates IL17 and IL17F expression on T(H) by binding to the essential enhancer conserved non-coding sequence 2 (CNS2) in the IL17-IL17F locus. Involved in hypoxia signaling by interacting with and activating the transcriptional activity of HIF1A. May inhibit cell growth in response to cellular stress. May exert an anti-inflammatory role by inducing CHUK expression and inhibiting NF-kappa-B signaling. {ECO:0000269|PubMed:11053433, ECO:0000269|PubMed:14687547, ECO:0000269|PubMed:15821743, ECO:0000269|PubMed:17666523, ECO:0000269|PubMed:18055760, ECO:0000269|PubMed:18164222, ECO:0000269|PubMed:18441015, ECO:0000269|PubMed:19014374, ECO:0000269|PubMed:19324970, ECO:0000269|PubMed:19965867, ECO:0000269|PubMed:21499262, ECO:0000269|PubMed:21628546, ECO:0000269|PubMed:22753030, ECO:0000269|PubMed:23172836, ECO:0000269|PubMed:23723244}. PTM: Phosphorylation by conventional PKCs in neurons inhibits transcriptional activity. Phosphorylated on Thr-183 by MAPK1/ERK1 in vitro. {ECO:0000250|UniProtKB:P35398}.; PTM: Sumoylated by SENP1 and SENP2. Sumoylation, promoted by PIAS2, PIAS3, PIAS4 but not PIAS1, enhances the transcriptional activity. Desumoylated by SENP1. {ECO:0000250|UniProtKB:P35398}.; PTM: Ubiquitinated, leading to its degradation by the proteasome. Proteasomal degradation is required for efficient transcriptional activity and is prevented by HR. {ECO:0000250|UniProtKB:P35398}.; PTM: Isoform 1: monomethylated at Lys-38 by EZH2, this creates a degron recognized by a DCX (DDB1-DCAF1/VPRBP-CUL4A-RBX1) E3 ubiquitin ligase complex. {ECO:0000250|UniProtKB:P35398}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407, ECO:0000269|PubMed:22753030, ECO:0000269|PubMed:23723244}. SUBUNIT: Monomer. Interacts (via the DNA-binding domain) with HIF1A; the interaction enhances HIF1A transcription under hypoxia through increasing protein stability. Interacts with CEBPB; the interaction disrupts the interaction CEBPB:EP300. Interacts with the coactivators NCOA2, PPARGC1A (via LXXLL motif), EP300 and MED1. Interacts with the corepressor NCOR1. Interacts with MAGED1 and CTNNB1. Interacts with CRY1 and PER2. Interacts (via AF-2 motif) with PROX1. Interacts with NRIP1. Isoform 4 interacts (via AF-2 motif) with isoform 1 of FOXP3 (via LXXLL motif) (By similarity). {ECO:0000250|UniProtKB:P35398, ECO:0000269|PubMed:14687547, ECO:0000269|PubMed:17476214, ECO:0000269|PubMed:19039140, ECO:0000269|PubMed:19324970, ECO:0000269|PubMed:20159955, ECO:0000269|PubMed:20300063, ECO:0000269|PubMed:21499262, ECO:0000269|PubMed:21628546, ECO:0000269|PubMed:22170608, ECO:0000269|PubMed:23723244}. DOMAIN: The AF-2 (activation function-2) motif is required for recruiting coregulators containing LXXLL motifs. {ECO:0000250|UniProtKB:P35398}. TISSUE SPECIFICITY: Expressed in cerebellum, heart, liver, lung, kidney, retina and brown and white adipose tissues. Expressed in the subset of mature Th17 cells. {ECO:0000269|PubMed:17666523, ECO:0000269|PubMed:18164222, ECO:0000269|PubMed:18441015, ECO:0000269|PubMed:22753030}. DISEASE: Note=Defects in Rora are the cause of the staggerer (SG) mutant phenotype which is characterized by disturbance of Purkinje cell development and immune system functioning. This phenotype exhibits lower body weight, reduced adiposity, decreased plasma cholesterol, triglyceride and apolipoprotein CIII levels, and is resistant to diet-induced obesity. Also has abnormal circadian rhythms. {ECO:0000269|PubMed:11053433, ECO:0000269|PubMed:14687547, ECO:0000269|PubMed:15821743, ECO:0000269|PubMed:17666523, ECO:0000269|PubMed:18055760, ECO:0000269|PubMed:18441015, ECO:0000269|PubMed:19014374, ECO:0000269|PubMed:9226375}. +Q8R1B8 RORB_MOUSE Nuclear receptor ROR-beta (Nuclear receptor RZR-beta) (Nuclear receptor subfamily 1 group F member 2) (Retinoid-related orphan receptor-beta) 470 53,118 Alternative sequence (1); Chain (1); DNA binding (1); Domain (1); Motif (1); Sequence caution (2); Sequence conflict (3); Zinc finger (2) FUNCTION: Nuclear receptor that binds DNA as a monomer to ROR response elements (RORE) containing a single core motif half-site 5'-AGGTCA-3' preceded by a short A-T-rich sequence. Considered to have intrinsic transcriptional activity, have some natural ligands such as all-trans retinoic acid (ATRA) and other retinoids which act as inverse agonists repressing the transcriptional activity. Required for normal postnatal development of rod and cone photoreceptor cells. Modulates rod photoreceptors differentiation at least by inducing the transcription factor NRL-mediated pathway. In cone photoreceptor cells, regulates transcription of OPN1SW. Involved in the regulation of the period length and stability of the circadian rhythm. May control cytoarchitectural patterning of neocortical neurons during development. May act in a dose-dependent manner to regulate barrel formation upon innervation of layer IV neurons by thalamocortical axons. May play a role in the suppression of osteoblastic differentiation through the inhibition of RUNX2 transcriptional activity.; FUNCTION: Isoform 1 is critical for hindlimb motor control and for the differentiation of amacrine and horizontal cells in the retina. Regulates the expression of PTF1A synergistically with FOXN4. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407, ECO:0000269|PubMed:16574740}. SUBUNIT: Monomer. Interacts with CRX. DOMAIN: AF-2 (activation function-2) motif is required for recruiting coregulators containing the LXXLL motif, such as NCOA1, and control the transactivational activity. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in inner and outer neuroblastic layer as well as in the ganglion cell layer of the developing retina. Expressed in bone marrow osteoprogenitor cells. {ECO:0000269|PubMed:16574740, ECO:0000269|PubMed:21799210, ECO:0000269|PubMed:22189870, ECO:0000269|PubMed:23652001, ECO:0000269|PubMed:9670004}. +P51450 RORG_MOUSE Nuclear receptor ROR-gamma (Nuclear receptor RZR-gamma) (Nuclear receptor subfamily 1 group F member 3) (RAR-related orphan receptor C) (Retinoid-related orphan receptor-gamma) (Thymus orphan receptor) (TOR) 516 58,117 Alternative sequence (4); Chain (1); Compositional bias (1); DNA binding (1); Domain (1); Motif (1); Mutagenesis (5); Region (1); Sequence conflict (9); Zinc finger (2) FUNCTION: Nuclear receptor that binds DNA as a monomer to ROR response elements (RORE) containing a single core motif half-site 5'-AGGTCA-3' preceded by a short A-T-rich sequence. Key regulator of cellular differentiation, immunity, peripheral circadian rhythm as well as lipid, steroid, xenobiotics and glucose metabolism. Considered to have intrinsic transcriptional activity, have some natural ligands like oxysterols that act as agonists (25-hydroxycholesterol) or inverse agonists (7-oxygenated sterols), enhancing or repressing the transcriptional activity, respectively. Recruits distinct combinations of cofactors to target gene regulatory regions to modulate their transcriptional expression, depending on the tissue, time and promoter contexts (PubMed:17666523, PubMed:19381306, PubMed:19965867, PubMed:21853531, PubMed:22789990, PubMed:23723244). Regulates the circadian expression of clock genes such as CRY1, ARNTL/BMAL1 and NR1D1 in peripheral tissues and in a tissue-selective manner (PubMed:22753030). Competes with NR1D1 for binding to their shared DNA response element on some clock genes such as ARNTL/BMAL1, CRY1 and NR1D1 itself, resulting in NR1D1-mediated repression or RORC-mediated activation of the expression, leading to the circadian pattern of clock genes expression. Therefore influences the period length and stability of the clock (PubMed:22753030). Involved in the regulation of the rhythmic expression of genes involved in glucose and lipid metabolism, including PLIN2 and AVPR1A. Negative regulator of adipocyte differentiation through the regulation of early phase genes expression, such as MMP3. Controls adipogenesis as well as adipocyte size and modulates insulin sensitivity in obesity. In liver, has specific and redundant functions with RORA as positive or negative modulator of expression of genes encoding phase I and Phase II proteins involved in the metabolism of lipids, steroids and xenobiotics, such as SULT1E1 (PubMed:21853531). Also plays also a role in the regulation of hepatocyte glucose metabolism through the regulation of G6PC and PCK1. Regulates the rhythmic expression of PROX1 and promotes its nuclear localization. {ECO:0000269|PubMed:17666523, ECO:0000269|PubMed:19381306, ECO:0000269|PubMed:19965867, ECO:0000269|PubMed:21853531, ECO:0000269|PubMed:22753030, ECO:0000269|PubMed:22789990, ECO:0000269|PubMed:23723244}.; FUNCTION: Isoform 2: Essential for thymopoiesis and the development of several secondary lymphoid tissues, including lymph nodes and Peyer's patches (PubMed:10602018, PubMed:14691482, PubMed:16148126). Required for the generation of LTi (lymphoid tissue inducer) cells. Regulates thymocyte survival through DNA-binding on ROREs of target gene promoter regions and recruitment of coactivaros via the AF-2. Also plays a key role, downstream of IL6 and TGFB and synergistically with RORA, for lineage specification of uncommitted CD4(+) T-helper (T(H)) cells into T(H)17 cells, antagonizing the T(H)1 program. Probably regulates IL17 and IL17F expression on T(H) by binding to the essential enhancer conserved non-coding sequence 2 (CNS2) in the IL17-IL17F locus (PubMed:16990136, PubMed:18164222, PubMed:26607793). May also play a role in the pre-TCR activation cascade leading to the maturation of alpha/beta T-cells and may participate in the regulation of DNA accessibility in the TCR-J(alpha) locus (PubMed:9881970, PubMed:10602018, PubMed:14691482, PubMed:16148126, PubMed:16990136, PubMed:18164222). Plays an indispensable role in the induction of IFN-gamma dependent anti-mycobacterial systemic immunity (By similarity). {ECO:0000250|UniProtKB:P51449, ECO:0000269|PubMed:10602018, ECO:0000269|PubMed:14691482, ECO:0000269|PubMed:16148126, ECO:0000269|PubMed:16990136, ECO:0000269|PubMed:18164222, ECO:0000269|PubMed:26607793, ECO:0000269|PubMed:9881970}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407, ECO:0000269|PubMed:18368049, ECO:0000269|PubMed:21853531, ECO:0000269|PubMed:22753030}. SUBUNIT: Interacts (via AF-2 motif) with the coactivators NCOA1, NCOA2 and PPARGC1A (via LXXLL motif). Interacts with the corepressor NCOR1. Interacts with CRY1. Interacts (via AF-2 motif) with PROX1. Interacts with FOXP3. {ECO:0000269|PubMed:16148126, ECO:0000269|PubMed:17476214, ECO:0000269|PubMed:18368049, ECO:0000269|PubMed:21499262, ECO:0000269|PubMed:22170608, ECO:0000269|PubMed:23723244}. DOMAIN: The AF-2 (activation function-2) motif is required for recruiting coregulators containing LXXLL motifs such as NCOA1 and NCOA2. {ECO:0000269|PubMed:16148126}. TISSUE SPECIFICITY: Isoform 1 is widely expressed with highest levels in muscle, kidney and liver. Isoform 2 is expressed primarily in immature thymocytes and the subset of mature T(H)17 cells. Neither isoform is expressed in spleen or bone marrow. {ECO:0000269|PubMed:10602018, ECO:0000269|PubMed:17666523, ECO:0000269|PubMed:22753030, ECO:0000269|PubMed:9881970}. +Q8C2Q3 RBM14_MOUSE RNA-binding protein 14 (RNA-binding motif protein 14) 669 69,449 Alternative sequence (1); Chain (1); Compositional bias (1); Cross-link (7); Domain (2); Modified residue (21); Region (1); Sequence conflict (3) FUNCTION: May function as a nuclear receptor coactivator, enhancing transcription through other coactivators such as NCOA6 and CITED1 (By similarity). Regulates centriole biogenesis by suppressing the formation of aberrant centriolar protein complexes in the cytoplasm and thus preserving mitotic spindle integrity (PubMed:25385835). Prevents the formation of the STIL-CENPJ complex (which can induce the formation of aberrant centriolar protein complexes) by interfering with the interaction of STIL with CENPJ (By similarity). Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway. {ECO:0000250|UniProtKB:Q96PK6, ECO:0000269|PubMed:25385835}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96PK6}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q96PK6}. Cytoplasm {ECO:0000250|UniProtKB:Q96PK6}. Note=In punctate subnuclear structures often located adjacent to splicing speckles, called paraspeckles. Cytoplasmic localization is crucial for its function in suppressing the formation of aberrant centriolar protein complexes. {ECO:0000250|UniProtKB:Q96PK6}. SUBUNIT: Interacts with NCOA6, CITED1 and XRCC5/KU86. Interacts with SS18. Interacts with STIL and interferes with its interaction with CENPJ. Interacts with gamma-tubulin. Part of the HDP-RNP complex composed of at least HEXIM1, PRKDC, XRCC5, XRCC6, paraspeckle proteins (SFPQ, NONO, PSPC1, RBM14, and MATR3) and NEAT1 RNA. {ECO:0000250|UniProtKB:Q96PK6}. +Q9CQT2 RBM7_MOUSE RNA-binding protein 7 (RNA-binding motif protein 7) 265 30,148 Chain (1); Domain (1); Initiator methionine (1); Modified residue (4); Region (2); Sequence conflict (1) FUNCTION: Subunit of the trimeric nuclear exosome targeting (NEXT) complex, a complex that directs a subset of non-coding short-lived RNAs for exosomal degradation. The RNA exosome is fundamental for the degradation of RNA in eukaryotic nuclei. Substrate targeting is facilitated by its cofactor MTREX, which links to RNA-binding protein adapters. Possible involved in germ cell RNA processing and meiosis. {ECO:0000250|UniProtKB:Q9Y580}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y580}. Note=Excluded from the nucleolus. {ECO:0000250|UniProtKB:Q9Y580}. SUBUNIT: Component of the nuclear exosome targeting (NEXT) complex composed of MTREX, ZCCHC8, and RBM7 that directs a subset of non-coding short-lived RNAs for exosomal degradation. Interacts with ZCCHC8 and SF3B2/SAP145. Binds to MTREX. {ECO:0000250|UniProtKB:Q9Y580}. +P86049 RBM46_MOUSE Probable RNA-binding protein 46 (RNA-binding motif protein 46) 533 60,077 Chain (1); Domain (3) +Q60990 RBY1B_MOUSE RNA-binding motif protein, Y chromosome, family 1 member B (RNA-binding motif protein 1) 380 43,143 Chain (1); Domain (1); Sequence conflict (3) FUNCTION: RNA-binding protein which may be involved in spermatogenesis. Required for sperm development, possibly by participating in pre-mRNA splicing in the testis. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with splicing factor proteins SFRS3/SRP20, TRA2B/SFRS10, KHDRBS1/SAM68 and KHDRBS3. TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:8817321}. +Q8BYK4 RDH12_MOUSE Retinol dehydrogenase 12 (EC 1.1.1.-) 316 35,292 Active site (1); Binding site (1); Chain (1); Nucleotide binding (1); Sequence conflict (2) FUNCTION: Exhibits an oxidoreductive catalytic activity towards retinoids. Most efficient as an NADPH-dependent retinal reductase. Displays high activity toward 9-cis and all-trans-retinol. Also involved in the metabolism of short-chain aldehydes. No steroid dehydrogenase activity detected. Might be the key enzyme in the formation of 11-cis-retinal from 11-cis-retinol during regeneration of the cone visual pigments (By similarity). {ECO:0000250}. +Q8CEE7 RDH13_MOUSE Retinol dehydrogenase 13 (EC 1.1.1.300) 334 36,464 Active site (1); Binding site (1); Chain (1); Initiator methionine (1); Modified residue (1); Nucleotide binding (1); Sequence conflict (1) Cofactor metabolism; retinol metabolism. FUNCTION: Retinol dehydrogenase with a clear preference for NADP. Oxidizes all-trans-retinol, but seems to reduce all-trans-retinal with much higher efficiency. Has no activity towards steroid. {ECO:0000250|UniProtKB:Q8NBN7}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q8NBN7}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8NBN7}. Note=Localized on the outer side of the inner mitochondrial membrane. {ECO:0000250|UniProtKB:Q8NBN7}. +P0C090 RC3H2_MOUSE Roquin-2 (EC 2.3.2.27) (Membrane-associated nucleic acid-binding protein) (RING finger and CCCH-type zinc finger domain-containing protein 2) (RING-type E3 ubiquitin transferase Roquin-2) 1187 131,295 Chain (1); Compositional bias (1); Metal binding (7); Modified residue (4); Region (3); Site (1); Zinc finger (2) Protein modification; protein ubiquitination. FUNCTION: Post-transcriptional repressor of mRNAs containing a conserved stem loop motif, called constitutive decay element (CDE), which is often located in the 3'-UTR, as in HMGXB3, ICOS, IER3, NFKBID, NFKBIZ, PPP1R10, TNF and in many more mRNAs. Binds to CDE and promotes mRNA deadenylation and degradation. This process does not involve miRNAs (PubMed:23663784). In follicular helper T (Tfh) cells, represses of ICOS and TNFRSF4 expression, thus preventing spontaneous Tfh cell differentiation, germinal center B-cell differentiation in the absence of immunization and autoimmunity. In resting or LPS-stimulated macrophages, controls inflammation by suppressing TNF expression. Also recognizes CDE in its own mRNA and in that of paralogous RC3H1, possibly leading to feedback loop regulation (PubMed:23583643, PubMed:23583642). Inhibits cooperatively with ZC3H12A the differentiation of helper T cells Th17 in lungs. They repress target mRNA encoding the Th17 cell-promoting factors IL6, ICOS, REL, IRF4, NFKBID and NFKBIZ. The cooperation requires RNA-binding by RC3H1 and the nuclease activity of ZC3H12A (PubMed:25282160). miRNA-binding protein that regulates microRNA homeostasis. Enhances DICER-mediated processing of pre-MIR146a but reduces mature MIR146a levels through an increase of 3' end uridylation. Both inhibits ICOS mRNA expression and they may act together to exert the suppression (PubMed:25697406). Acts as a ubiquitin E3 ligase. Pairs with E2 enzymes UBE2B, UBE2D2, UBE2E2, UBE2E3, UBE2G2, UBE2K and UBE2Q2 and produces polyubiquitin chains. Show the strongest activity when paired with UBE2N:UBE2V1 or UBE2N:UBE2V2 E2 complexes and generate both short and long polyubiquitin chains. Involved in the ubiquitination of MAP3K5 (By similarity). Able to interact with double-stranded RNA (dsRNA). {ECO:0000250|UniProtKB:Q9HBD1, ECO:0000269|PubMed:23583642, ECO:0000269|PubMed:23583643, ECO:0000269|PubMed:23663784, ECO:0000269|PubMed:25282160, ECO:0000269|PubMed:25697406}. PTM: Proteolytically cleaved by MALT1 in activated CD4(+) T cells; cleavage at Arg-509 is critical for promoting RC3H1 degradation in response to T-cell receptor (TCR) stimulation, and hence is necessary for prolonging the stability of a set of mRNAs controlling Th17 cell differentiation. {ECO:0000269|PubMed:25282160}. SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:23583642}. Note=During stress, such as that induced by arsenite, localizes to cytosolic stress granules. Localization to stress granules, but not to P-bodies, depends upon the RING-type zinc finger. SUBUNIT: Interacts with EDC4 (PubMed:23583643). Interacts with CCR4-NOT deadenylase complex (PubMed:23663784). Interacts with MAP3K5; the interaction is probably stimulus-dependent (By similarity). {ECO:0000250|UniProtKB:Q9HBD1, ECO:0000269|PubMed:23583643, ECO:0000269|PubMed:23663784}. DOMAIN: The RING-type zinc finger is required for proper localization to stress granules, but not to P-bodies. {ECO:0000269|PubMed:23583642}.; DOMAIN: The ROQ region is required for CDE RNA-binding. Has 2 separate RNA-binding sites, one for CDE RNA and the other for dsRNA (PubMed:23663784). It may also be involved in localization to stress granules (By similarity). {ECO:0000250|UniProtKB:Q4VGL6, ECO:0000269|PubMed:23663784}.; DOMAIN: HEPN (higher eukaryotes and prokaryotes nucleotide-binding) are observed in both N- and C-terminal sides of ROQ domain with 3D structure even if they are poredcted on the basis of sequence. {ECO:0000250|UniProtKB:Q9HBD1}. TISSUE SPECIFICITY: Highest levels in lymph node and thymus and slightly lesser amounts in brain, lung, and spleen (at protein level). Very weak expression in heart, muscle, and kidney (at protein level). Expressed in CD4(+) helper T-cells (at protein level). {ECO:0000269|PubMed:23583643}. +Q9Z0J1 RECK_MOUSE Reversion-inducing cysteine-rich protein with Kazal motifs (mRECK) 971 106,082 Chain (1); Disulfide bond (6); Domain (4); Glycosylation (5); Lipidation (1); Mutagenesis (5); Propeptide (1); Region (1); Repeat (5); Sequence conflict (8); Signal peptide (1) FUNCTION: Functions together with ADGRA2 to enable brain endothelial cells to selectively respond to Wnt7 signals (WNT7A or WNT7B) (PubMed:28803732). Plays a key role in Wnt7-specific responses: required for central nervous system (CNS) angiogenesis and blood-brain barrier regulation (PubMed:26658478, PubMed:28803732). Acts as a Wnt7-specific coactivator of canonical Wnt signaling by decoding Wnt ligands: acts by interacting specifically with the disordered linker region of Wnt7, thereby conferring ligand selectivity for Wnt7 (By similarity). ADGRA2 is then required to deliver RECK-bound Wnt7 to frizzled by assembling a higher-order RECK-ADGRA2-Fzd-LRP5-LRP6 complex (By similarity). Also acts as a serine protease inhibitor: negatively regulates matrix metalloproteinase-9 (MMP9) by suppressing MMP9 secretion and by direct inhibition of its enzymatic activity (PubMed:11747814). Also inhibits metalloproteinase activity of MMP2 and MMP14 (MT1-MMP) (PubMed:11747814). {ECO:0000250|UniProtKB:O95980, ECO:0000269|PubMed:11747814, ECO:0000269|PubMed:26658478, ECO:0000269|PubMed:28803732}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28803732}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:O95980}. SUBUNIT: Interacts (via knot repeats) with WNT7A (via disordered linker region); the interaction is direct (By similarity). Interacts (via knot repeats) with WNT7B (via disordered linker region); the interaction is direct (By similarity). Interacts with ADGRA2; the interaction is direct (PubMed:28803732). Interacts with MMP9 (By similarity). {ECO:0000250|UniProtKB:O95980, ECO:0000269|PubMed:28803732}. DOMAIN: The Kazal-like domains mediate the serine protease inhibitor activity. {ECO:0000250|UniProtKB:O95980}. +Q91ZS8 RED1_MOUSE Double-stranded RNA-specific editase 1 (EC 3.5.4.37) (RNA-editing deaminase 1) (RNA-editing enzyme 1) (dsRNA adenosine deaminase) 711 78,001 Active site (1); Alternative sequence (4); Beta strand (3); Binding site (8); Chain (1); Domain (3); Helix (2); Metal binding (3); Modified residue (1); Region (4); Sequence conflict (2) FUNCTION: Catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA) referred to as A-to-I RNA editing. This may affect gene expression and function in a number of ways that include mRNA translation by changing codons and hence the amino acid sequence of proteins; pre-mRNA splicing by altering splice site recognition sequences; RNA stability by changing sequences involved in nuclease recognition; genetic stability in the case of RNA virus genomes by changing sequences during viral RNA replication; and RNA structure-dependent activities such as microRNA production or targeting or protein-RNA interactions. Can edit both viral and cellular RNAs and can edit RNAs at multiple sites (hyper-editing) or at specific sites (site-specific editing). Its cellular RNA substrates include: bladder cancer-associated protein (BLCAP), neurotransmitter receptors for glutamate (GRIA2 and GRIK2) and serotonin (HTR2C), GABA receptor (GABRA3) and potassium voltage-gated channel (KCNA1). Site-specific RNA editing of transcripts encoding these proteins results in amino acid substitutions which consequently alter their functional activities. Edits GRIA2 at both the Q/R and R/G sites efficiently but converts the adenosine in hotspot1 much less efficiently. Can inhibit cell proliferation and migration and can stimulate exocytosis. {ECO:0000269|PubMed:17369310}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Note=Shuttles between nucleoli and the nucleoplasm. {ECO:0000250}. SUBUNIT: Homodimer. Homodimerization is essential for its catalytic activity. Can form heterodimers with isoform 5 of ADAR/ADAR1 (By similarity). {ECO:0000250}. +Q9JI20 RED2_MOUSE Double-stranded RNA-specific editase B2 (EC 3.5.-.-) (RNA-dependent adenosine deaminase 3) (RNA-editing deaminase 2) (RNA-editing enzyme 2) (dsRNA adenosine deaminase B2) 745 82,187 Active site (1); Chain (1); Domain (3); Metal binding (3); Region (1); Sequence conflict (5) FUNCTION: Lacks editing activity. It prevents the binding of other ADAR enzymes to targets in vitro, and decreases the efficiency of these enzymes. Capable of binding to dsRNA but also to ssRNA (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. TISSUE SPECIFICITY: Brain specific. +Q9Z1M8 RED_MOUSE Protein Red (Cytokine IK) (IK factor) (Protein RER) 557 65,616 Chain (1); Compositional bias (1); Cross-link (13); Modified residue (7); Region (1); Repeat (17); Sequence conflict (1) FUNCTION: Involved in pre-mRNA splicing as a component of the spliceosome. Auxiliary spliceosomal protein that regulates selection of alternative splice sites in a small set of target pre-mRNA species. Required for normal mitotic cell cycle progression. Recruits MAD1L1 and MAD2L1 to kinetochores, and is required to trigger the spindle assembly checkpoint. Required for normal accumulation of SMU1. {ECO:0000250|UniProtKB:Q13123}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13123}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q13123}. Chromosome {ECO:0000250|UniProtKB:Q13123}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q13123}. Note=Predominantly present throughout the nucleoplasm during prometaphase, metaphase and anaphase. Is also detected in nuclear foci that are not identical with Cajal bodies. Starts to accumulate at chromosomes during telophase, and is nearly exclusively associated with chromosomes in newly divided cells. Colocalizes with MAD1L1 at mitotic spindle poles during metaphase and anaphase. {ECO:0000250|UniProtKB:Q13123}. SUBUNIT: Component of the spliceosome B complex. Interacts with SMU1. Interacts with MAD1L1. May interact with DHX15. {ECO:0000250|UniProtKB:Q13123}. TISSUE SPECIFICITY: Ubiquitous. +Q8BGH4 REEP1_MOUSE Receptor expression-enhancing protein 1 201 22,285 Chain (1); Compositional bias (1); Modified residue (1); Transmembrane (2) TRANSMEM 1 21 Helical. {ECO:0000255}.; TRANSMEM 35 55 Helical. {ECO:0000255}. FUNCTION: Required for endoplasmic reticulum (ER) network formation, shaping and remodeling; it links ER tubules to the cytoskeleton. May also enhance the cell surface expression of odorant receptors (By similarity). {ECO:0000250, ECO:0000269|PubMed:15550249}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q9H902}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum {ECO:0000269|PubMed:24668814}. Note=A small proportion is detected at the cell surface. Localizes to endoplasmic reticulum tubular network. {ECO:0000269|PubMed:15550249, ECO:0000269|PubMed:24668814}. SUBUNIT: Interacts with OLFR992 (PubMed:15550249). Interacts with SPAST and ATL1. Interacts (via C-terminus) with microtubules (By similarity). Interacts with ZFYVE27 (PubMed:24668814). {ECO:0000250|UniProtKB:Q9H902, ECO:0000269|PubMed:15550249, ECO:0000269|PubMed:24668814}. TISSUE SPECIFICITY: Detected in olfactory sensory neurons of the olfactory epithelium, and in total brain. {ECO:0000269|PubMed:15550249}. +Q8VCD6 REEP2_MOUSE Receptor expression-enhancing protein 2 254 28,437 Chain (1); Modified residue (1); Transmembrane (2) TRANSMEM 1 21 Helical. {ECO:0000255}.; TRANSMEM 35 55 Helical. {ECO:0000255}. FUNCTION: Required for endoplasmic reticulum (ER) network formation, shaping and remodeling. May enhance the cell surface expression of odorant receptors (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with odorant receptor proteins. {ECO:0000250}. +Q99KK1 REEP3_MOUSE Receptor expression-enhancing protein 3 254 29,214 Chain (1); Erroneous termination (1); Modified residue (2); Sequence conflict (5); Transmembrane (3) TRANSMEM 1 21 Helical. {ECO:0000255}.; TRANSMEM 35 55 Helical. {ECO:0000255}.; TRANSMEM 59 79 Helical. {ECO:0000255}. FUNCTION: Microtubule-binding protein required to ensure proper cell division and nuclear envelope reassembly by sequestering the endoplasmic reticulum away from chromosomes during mitosis. Probably acts by clearing the endoplasmic reticulum membrane from metaphase chromosomes (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q8K072 REEP4_MOUSE Receptor expression-enhancing protein 4 257 29,691 Chain (1); Modified residue (5); Transmembrane (2) TRANSMEM 1 21 Helical. {ECO:0000255}.; TRANSMEM 42 62 Helical. {ECO:0000255}. FUNCTION: Microtubule-binding protein required to ensure proper cell division and nuclear envelope reassembly by sequestering the endoplasmic reticulum away from chromosomes during mitosis. Probably acts by clearing the endoplasmic reticulum membrane from metaphase chromosomes (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q60870 REEP5_MOUSE Receptor expression-enhancing protein 5 (GP106) (Polyposis locus protein 1 homolog) (Protein TB2 homolog) 185 21,051 Chain (1); Transmembrane (2) TRANSMEM 31 51 Helical. {ECO:0000255}.; TRANSMEM 86 106 Helical. {ECO:0000255}. FUNCTION: May promote functional cell surface expression of olfactory receptors. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum {ECO:0000269|PubMed:24668814}. Note=Localizes to endoplasmic reticulum tubular network. {ECO:0000269|PubMed:24668814}. SUBUNIT: Interacts with ATL1 and ATL2 (PubMed:19665976). Interacts with ZFYVE27 (PubMed:24668814). {ECO:0000269|PubMed:19665976, ECO:0000269|PubMed:24668814}. +Q9JM62 REEP6_MOUSE Receptor expression-enhancing protein 6 (Polyposis locus protein 1-like 1) (TB2 protein-like 1) 201 22,204 Alternative sequence (2); Chain (1); Transmembrane (3) TRANSMEM 36 56 Helical. {ECO:0000255}.; TRANSMEM 89 109 Helical. {ECO:0000255}.; TRANSMEM 117 137 Helical. {ECO:0000255}. FUNCTION: May play a role in intracellular protein transport from the endoplasmic reticulum to the cell surface (PubMed:24098485). Involved in retinal development (PubMed:24691551). Required for correct function and survival of retinal photoreceptors (By similarity). {ECO:0000250|UniProtKB:Q96HR9, ECO:0000269|PubMed:24098485, ECO:0000269|PubMed:24691551}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:24098485}; Multi-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Expressed in retinal rod photoreceptors and in liver, but not detected in brain, muscle, kidney, retinal cone photoreceptors or retinal ganglion cells (at protein level) (PubMed:24691551). Highly expressed in the ganglion cell layer of the retina and in liver, and also detected at low levels in kidney and testis (PubMed:15728532). Isoform 1 is expressed in the retina. Isoform 2 is expressed in liver. {ECO:0000269|PubMed:15728532, ECO:0000269|PubMed:24691551}. +Q8K2J7 RELL1_MOUSE RELT-like protein 1 272 29,351 Alternative sequence (1); Chain (1); Coiled coil (1); Modified residue (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 59 79 Helical. {ECO:0000255}. TOPO_DOM 24 58 Extracellular. {ECO:0000255}.; TOPO_DOM 80 272 Cytoplasmic. {ECO:0000255}. FUNCTION: Induces activation of MAPK14/p38 cascade, when overexpressed. Induces apoptosis, when overexpressed. {ECO:0000250|UniProtKB:Q8IUW5}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8IUW5}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q8IUW5}. SUBUNIT: Interacts with RELT, RELL2, OXSR1 and PLSCR1. {ECO:0000250|UniProtKB:Q8IUW5}. +Q8BRJ3 RELL2_MOUSE RELT-like protein 2 303 32,326 Chain (1); Modified residue (1); Transmembrane (1) TRANSMEM 15 35 Helical. {ECO:0000255}. FUNCTION: Induces activation of MAPK14/p38 cascade, when overexpressed. Induces apoptosis, when overexpressed. {ECO:0000250|UniProtKB:Q8NC24}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8NC24}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8NC24}. SUBUNIT: Interacts with RELT, RELL1, OXSR1, PLSCR1 AND TRAF2. {ECO:0000250|UniProtKB:Q8NC24}. +Q99J62 RFC4_MOUSE Replication factor C subunit 4 (Activator 1 subunit 4) 364 39,867 Chain (1); Modified residue (3); Nucleotide binding (1) FUNCTION: The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins proliferating cell nuclear antigen (PCNA) and activator 1. This subunit may be involved in the elongation of the multiprimed DNA template (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Heterotetramer of subunits RFC2, RFC3, RFC4 and RFC5 that can form a complex either with RFC1 or with RAD17. The former interacts with PCNA in the presence of ATP, while the latter has ATPase activity but is not stimulated by PCNA (By similarity). {ECO:0000250}. +P35601 RFC1_MOUSE Replication factor C subunit 1 (A1-P145) (Activator 1 140 kDa subunit) (A1 140 kDa subunit) (Activator 1 large subunit) (Activator 1 subunit 1) (Differentiation-specific element-binding protein) (ISRE-binding protein) (Replication factor C 140 kDa subunit) (RF-C 140 kDa subunit) (RFC140) (Replication factor C large subunit) 1131 125,985 Alternative sequence (1); Chain (1); Cross-link (1); Domain (1); Modified residue (20); Motif (1); Nucleotide binding (1); Region (1); Sequence conflict (7) FUNCTION: The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins PCNA and activator 1. This subunit binds to the primer-template junction. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Heterotetramer of subunits RFC2, RFC3, RFC4 and RFC5 that can form a complex either with RFC1 or with RAD17. The former interacts with PCNA in the presence of ATP, while the latter has ATPase activity but is not stimulated by PCNA (By similarity). {ECO:0000250}. +Q61193 RGL2_MOUSE Ral guanine nucleotide dissociation stimulator-like 2 (RalGDS-like 2) (RalGDS-like factor) (Ras-associated protein RAB2L) 778 83,826 Beta strand (11); Chain (1); Domain (3); Helix (25); Sequence conflict (2); Turn (6) FUNCTION: Probable guanine nucleotide exchange factor. Putative effector of Ras and/or Rap. Associates with the GTP-bound form of Rap 1A and H-Ras in vitro. SUBUNIT: Interacts with SAMD9. {ECO:0000250}. +O08849 RGS2_MOUSE Regulator of G-protein signaling 2 (RGS2) 211 24,294 Chain (1); Domain (1); Region (2); Sequence conflict (3) FUNCTION: Regulates G protein-coupled receptor signaling cascades. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form (By similarity). It is involved in the negative regulation of the angiotensin-activated signaling pathway (By similarity). Plays a role in the regulation of blood pressure in response to signaling via G protein-coupled receptors and GNAQ. Plays a role in regulating the constriction and relaxation of vascular smooth muscle (PubMed:14608379). Binds EIF2B5 and blocks its activity, thereby inhibiting the translation of mRNA into protein (By similarity). {ECO:0000250|UniProtKB:P41220, ECO:0000269|PubMed:14608379}. PTM: Phosphorylated by protein kinase C. Phosphorylation by PRKG1 leads to activation of RGS2 activity. {ECO:0000250|UniProtKB:P41220}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P41220}. Cytoplasm {ECO:0000250|UniProtKB:P41220}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P41220}. SUBUNIT: Interacts with GNAQ. Does not interact with GNAI1 and GNAI3. Interacts with EIF2B5. Interacts with PRKG1 (isoform alpha). {ECO:0000250|UniProtKB:P41220}. TISSUE SPECIFICITY: Expressed in a wide variety of tissues. {ECO:0000269|PubMed:9079700}. +Q8JZV4 RBM41_MOUSE RNA-binding protein 41 (RNA-binding motif protein 41) 413 47,515 Alternative sequence (5); Chain (1); Domain (1); Sequence conflict (1) FUNCTION: May bind RNA. {ECO:0000305}. +Q0VBL3 RBM15_MOUSE RNA-binding protein 15 (One-twenty two protein 1) (RNA-binding motif protein 15) 962 105,722 Alternative sequence (1); Chain (1); Compositional bias (6); Cross-link (5); Domain (4); Erroneous initiation (1); Modified residue (23); Sequence caution (1); Sequence conflict (4) FUNCTION: RNA-binding protein that acts as a key regulator of N6-methyladenosine (m6A) methylation of RNAs, thereby regulating different processes, such as hematopoietic cell homeostasis, alternative splicing of mRNAs and X chromosome inactivation mediated by Xist RNA (PubMed:29535189). Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing (PubMed:29535189). Plays a key role in m6A methylation, possibly by binding target RNAs and recruiting the WMM complex (PubMed:29535189). Involved in random X inactivation mediated by Xist RNA: acts by binding Xist RNA and recruiting the WMM complex, which mediates m6A methylation, leading to target YTHDC1 reader on Xist RNA and promoting transcription repression activity of Xist (By similarity). Required for the development of multiple tissues, such as the maintenance of the homeostasis of long-term hematopoietic stem cells and for megakaryocyte (MK) and B-cell differentiation (PubMed:17283045, PubMed:17376872, PubMed:18981216, PubMed:25468569). Regulates megakaryocyte differentiation by regulating alternative splicing of genes important for megakaryocyte differentiation; probably regulates alternative splicing via m6A regulation (By similarity). Required for placental vascular branching morphogenesis and embryonic development of the heart and spleen (PubMed:18981216). Acts as a regulator of thrombopoietin response in hematopoietic stem cells by regulating alternative splicing of MPL (PubMed:25468569). May also function as an mRNA export factor, stimulating export and expression of RTE-containing mRNAs which are present in many retrotransposons that require to be exported prior to splicing (By similarity). High affinity binding of pre-mRNA to RBM15 may allow targeting of the mRNP to the export helicase DBP5 in a manner that is independent of splicing-mediated NXF1 deposition, resulting in export prior to splicing (By similarity). May be implicated in HOX gene regulation (By similarity). {ECO:0000250|UniProtKB:Q96T37, ECO:0000269|PubMed:17283045, ECO:0000269|PubMed:17376872, ECO:0000269|PubMed:18981216, ECO:0000269|PubMed:25468569, ECO:0000269|PubMed:29535189}. PTM: Methylated at Arg-577 by PRMT1, leading to promote ubiquitination by CNOT4 and subsequent degradation by the proteasome. {ECO:0000250|UniProtKB:Q96T37}.; PTM: Ubiquitinated by CNOT4 following methylation at Arg-577 by PRMT1. {ECO:0000250|UniProtKB:Q96T37}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q96T37}. Nucleus, nucleoplasm {ECO:0000269|PubMed:17283045}. Nucleus envelope {ECO:0000250|UniProtKB:Q96T37}. Nucleus membrane {ECO:0000250|UniProtKB:Q96T37}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q96T37}. Note=Colocalizes at the nuclear pore with DBP5 and NXF1. {ECO:0000250|UniProtKB:Q96T37}. SUBUNIT: Component of the WMM complex, a N6-methyltransferase complex composed of a catalytic subcomplex, named MAC, and of an associated subcomplex, named MACOM (PubMed:29535189). The MAC subcomplex is composed of METTL3 and METTL14 (PubMed:29535189). The MACOM subcomplex is composed of WTAP, ZC3H13, CBLL1/HAKAI, VIRMA, and, in some cases of RBM15 (RBM15 or RBM15B) (PubMed:29535189). Also component of a MACOM-like complex, named WTAP complex, composed of WTAP, ZC3H13, CBLL1, VIRMA, RBM15, BCLAF1 and THRAP3 (By similarity). Interacts with RBPJ (PubMed:17283045). Interacts (via SPOC domain) with SETD1B (By similarity). Interacts with NXF1, the interaction is required to promote mRNA export (By similarity). Interacts with SF3B1 (By similarity). {ECO:0000250|UniProtKB:Q96T37, ECO:0000269|PubMed:17283045, ECO:0000269|PubMed:29535189}. +Q8R0F5 RBMX2_MOUSE RNA-binding motif protein, X-linked 2 326 37,536 Chain (1); Compositional bias (2); Cross-link (1); Domain (1); Modified residue (3) FUNCTION: Involved in pre-mRNA splicing as component of the activated spliceosome. {ECO:0000250|UniProtKB:Q9Y388}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y388}. SUBUNIT: Part of the activated spliceosome B/catalytic step 1 spliceosome, one of the forms of the spliceosome which has a well-formed active site but still cannot catalyze the branching reaction and is composed of at least 52 proteins, the U2, U5 and U6 snRNAs and the pre-mRNA. {ECO:0000250|UniProtKB:Q9Y388}. +Q9JHG2 RCAN2_MOUSE Calcipressin-2 (Calcineurin inhibitory protein ZAKI-4) (Down syndrome candidate region 1-like protein 1) (Myocyte-enriched calcineurin-interacting protein 2) (MCIP2) (Regulator of calcineurin 2) 197 22,025 Chain (1); Erroneous initiation (1); Modified residue (1); Sequence conflict (3) FUNCTION: Inhibits calcineurin-dependent transcriptional responses by binding to the catalytic domain of calcineurin A. Could play a role during central nervous system development. TISSUE SPECIFICITY: Highest expression in heart, skeletal muscle and brain. Lower expression in all other tissues. +Q8BH97 RCN3_MOUSE Reticulocalbin-3 328 38,002 Calcium binding (6); Chain (1); Domain (6); Glycosylation (1); Motif (1); Sequence conflict (2); Signal peptide (1) FUNCTION: Probable molecular chaperone assisting protein biosynthesis and transport in the endoplasmic reticulum (PubMed:26252542). Required for the proper biosynthesis and transport of pulmonary surfactant-associated protein A/SP-A, pulmonary surfactant-associated protein D/SP-D and the lipid transporter ABCA3 (PubMed:26252542). By regulating both the proper expression and the degradation through the endoplasmic reticulum-associated protein degradation pathway of these proteins plays a crucial role in pulmonary surfactant homeostasis (PubMed:26252542). Has an anti-fibrotic activity by negatively regulating the secretion of type I and type III collagens (By similarity). This calcium-binding protein also transiently associates with immature PCSK6 and regulates its secretion (By similarity). {ECO:0000250|UniProtKB:Q96D15, ECO:0000269|PubMed:26252542}. PTM: Degraded by PCSK6 and other endoproteases including FURIN and PCSK5. {ECO:0000250|UniProtKB:Q96D15}.; PTM: N-glycosylated. {ECO:0000250|UniProtKB:I6L9G5}. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000269|PubMed:26252542}. SUBUNIT: Interacts with PCSK6 (immature form including the propeptide); probably involved in the maturation and the secretion of PCSK6. {ECO:0000250|UniProtKB:Q96D15}. TISSUE SPECIFICITY: Highly expressed in lung and heart. Also detected in liver, spleen, kidney, skeletal muscle, intestine, stomach, and brain. {ECO:0000269|PubMed:26252542}. +Q9CYZ6 REX1B_MOUSE Required for excision 1-B domain-containing protein 169 18,706 Chain (1); Frameshift (1); Sequence conflict (2) +Q00724 RET4_MOUSE Retinol-binding protein 4 (Plasma retinol-binding protein) (PRBP) (RBP) 201 23,206 Binding site (1); Chain (1); Disulfide bond (3); Modified residue (1); Sequence conflict (2); Signal peptide (1) FUNCTION: Retinol-binding protein that mediates retinol transport in blood plasma. Delivers retinol from the liver stores to the peripheral tissues. Transfers the bound all-trans retinol to STRA6, that then facilitates retinol transport across the cell membrane. {ECO:0000250|UniProtKB:P02753}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02753}. SUBUNIT: Interacts with TTR. Interaction with TTR prevents its loss by filtration through the kidney glomeruli. Interacts with STRA6. {ECO:0000250|UniProtKB:P02753}. +Q920Q2 REV1_MOUSE DNA repair protein REV1 (EC 2.7.7.-) (Rev1-like terminal deoxycytidyl transferase) 1249 137,341 Beta strand (1); Binding site (3); Chain (1); Domain (2); Helix (4); Metal binding (4); Motif (1); Nucleotide binding (2); Region (4); Sequence conflict (5); Site (2) FUNCTION: Deoxycytidyl transferase involved in DNA repair. Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by physical and chemical agents. {ECO:0000269|PubMed:11711549}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Interacts with FAAP20 (By similarity). Monomer. Interacts with the DNA polymerase zeta which is composed of REV3L and MAD2L2; the interaction with MAD2L2 is direct and requires that REV3L is in its closed conformation. Interacts with POLH, POLI and POLK. {ECO:0000250, ECO:0000269|PubMed:11711549, ECO:0000269|PubMed:14657033}. DOMAIN: The C-terminal domain is necessary for protein interactions. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11711549}. +Q9JJ43 RFOX1_MOUSE RNA binding protein fox-1 homolog 1 (Ataxin-2-binding protein 1) (Fox-1 homolog A) 396 42,678 Alternative sequence (6); Chain (1); Domain (1); Modified residue (3); Sequence conflict (7); Site (8) FUNCTION: RNA-binding protein that regulates alternative splicing events by binding to 5'-UGCAUGU-3' elements. Prevents binding of U2AF2 to the 3'-splice site. Regulates alternative splicing of tissue-specific exons and of differentially spliced exons during erythropoiesis. {ECO:0000269|PubMed:12574126, ECO:0000269|PubMed:15824060, ECO:0000269|PubMed:16260614, ECO:0000269|PubMed:17101796}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Predominantly nuclear. SUBUNIT: Binds to the C-terminus of ATXN2. {ECO:0000250}. TISSUE SPECIFICITY: Detected in brain (at protein level). Detected in heart, brain, neurons, skeletal muscle and embryo. {ECO:0000269|PubMed:12574126, ECO:0000269|PubMed:15824060, ECO:0000269|PubMed:16260614}. +Q60695 RGL1_MOUSE Ral guanine nucleotide dissociation stimulator-like 1 (RalGDS-like 1) 768 86,324 Beta strand (5); Chain (1); Compositional bias (1); Domain (3); Helix (1); Modified residue (1); Sequence conflict (1); Turn (2) FUNCTION: Probable guanine nucleotide exchange factor. SUBUNIT: Interacts with Ras. +Q9D300 RGF1C_MOUSE Ras-GEF domain-containing family member 1C 466 52,723 Alternative sequence (1); Chain (1); Domain (2); Erroneous gene model prediction (2) FUNCTION: Guanine nucleotide exchange factor (GEF). {ECO:0000250}. +Q9JL25 RGS1_MOUSE Regulator of G-protein signaling 1 (RGS1) 209 24,107 Alternative sequence (1); Chain (1); Domain (1); Erroneous initiation (6); Sequence conflict (9) FUNCTION: Regulates G protein-coupled receptor signaling cascades, including signaling downstream of the N-formylpeptide chemoattractant receptors and leukotriene receptors. Inhibits B cell chemotaxis toward CXCL12 (PubMed:10779778). Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form (By similarity). {ECO:0000250|UniProtKB:Q08116, ECO:0000269|PubMed:10779778}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q08116}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q08116}; Cytoplasmic side {ECO:0000250|UniProtKB:Q08116}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q08116}. SUBUNIT: Interacts with GNAI1 and GNAQ. {ECO:0000250|UniProtKB:Q08116}. TISSUE SPECIFICITY: Detected in spleen, lymph node and intestine. {ECO:0000269|PubMed:10779778}. +G3UYX5 RGS22_MOUSE Regulator of G-protein signaling 22 1258 145,883 Chain (1); Domain (2) FUNCTION: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18703424}. Nucleus {ECO:0000269|PubMed:18703424}. Note=Expressed in the cytoplasm of spermatogonia and spermatocytes. In spermatids, also expressed in the nucleus. SUBUNIT: Interacts with GNA11, GNA12 AND GNA13. {ECO:0000250}. TISSUE SPECIFICITY: Expressed testis, including in Leydig cells and spermatogenic cells from the spermatogonia to spermatid stages (at protein level). {ECO:0000269|PubMed:18703424}. +Q8VH31 RFPLA_MOUSE Ret finger protein-like 4A 287 32,358 Chain (1); Domain (1); Sequence conflict (1); Zinc finger (1) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12525704}. Nucleus {ECO:0000269|PubMed:12525704}. SUBUNIT: Interacts with PSMB1, UBE2A and CCNB1. {ECO:0000269|PubMed:12525704}. TISSUE SPECIFICITY: Expressed in the ovaries and oocytes (at protein level) (PubMed:12525704, PubMed:11850190). Expression restricted to gonads. In testis, present at later stages of spermatogeneis and abundant in elongating spermatids. {ECO:0000269|PubMed:11850190, ECO:0000269|PubMed:12525704}. +Q8BQP8 RFIP4_MOUSE Rab11 family-interacting protein 4 (FIP4-Rab11) (Rab11-FIP4) (mRab11-FIP4A) 635 71,901 Calcium binding (1); Chain (1); Coiled coil (1); Domain (2); Region (1); Sequence conflict (1) FUNCTION: Acts as a regulator of endocytic traffic by participating in membrane delivery. Required for the abcission step in cytokinesis, possibly by acting as an 'address tag' delivering recycling endosome membranes to the cleavage furrow during late cytokinesis (By similarity). May play a role in differentiation during retinal development, in a Rab11-independent manner. {ECO:0000250, ECO:0000269|PubMed:17089410}. SUBCELLULAR LOCATION: Recycling endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cleavage furrow {ECO:0000250}. Midbody {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Note=Recruited to the cleavage furrow and the midbody during cytokinesis. {ECO:0000250}. SUBUNIT: Homodimer. Forms a complex with Rab11 (RAB11A or RAB11B) and ARF6. Interacts with RAB11A; the interaction is direct. Forms a heterooligomeric complex with RAB11FIP2, RAB11FIP3 and RAB11FIP5 (By similarity). Interacts with ECPAS (By similarity). {ECO:0000250}. DOMAIN: The RBD-FIP domain mediates the interaction with Rab11 (RAB11A or RAB11B). {ECO:0000250}. TISSUE SPECIFICITY: Strongly expressed in the developing retina. Expressed predominantly in neural tissues. {ECO:0000269|PubMed:17089410}. +Q8C3B8 RFT1_MOUSE Protein RFT1 homolog 541 60,303 Alternative sequence (2); Chain (1); Transmembrane (11) TRANSMEM 16 36 Helical. {ECO:0000255}.; TRANSMEM 45 62 Helical. {ECO:0000255}.; TRANSMEM 85 105 Helical. {ECO:0000255}.; TRANSMEM 123 143 Helical. {ECO:0000255}.; TRANSMEM 154 176 Helical. {ECO:0000255}.; TRANSMEM 187 207 Helical. {ECO:0000255}.; TRANSMEM 335 355 Helical. {ECO:0000255}.; TRANSMEM 376 396 Helical. {ECO:0000255}.; TRANSMEM 414 434 Helical. {ECO:0000255}.; TRANSMEM 470 490 Helical. {ECO:0000255}.; TRANSMEM 499 519 Helical. {ECO:0000255}. FUNCTION: May be involved in N-linked oligosaccharide assembly. May participate in the translocation of oligosaccharide from the cytoplasmic side to the lumenal side of the endoplasmic reticulum membrane (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q7TS73 RFLA_MOUSE Refilin-A (Regulator of filamin protein A) (RefilinA) 204 22,606 Chain (1); Modified residue (1); Sequence conflict (1) FUNCTION: Involved in the regulation of the perinuclear actin network and nuclear shape through interaction with filamins. Plays an essential role in the formation of cartilaginous skeletal elements. {ECO:0000269|PubMed:21709252, ECO:0000269|PubMed:24436304}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:21709252, ECO:0000269|PubMed:24436304}. Note=Colocalizes with FLNA along actin bundle-like structures. {ECO:0000269|PubMed:24436304}. SUBUNIT: Interacts with FLNA and FLNB. {ECO:0000269|PubMed:21709252, ECO:0000269|PubMed:24436304}. TISSUE SPECIFICITY: Detected in various tissues, with highest expression in lung, followed by spleen. {ECO:0000269|PubMed:24436304}. +Q9CR83 RBM18_MOUSE Probable RNA-binding protein 18 (RNA-binding motif protein 18) 190 21,649 Chain (1); Domain (1); Sequence conflict (2) +Q80Y56 RBNS5_MOUSE Rabenosyn-5 (FYVE finger-containing Rab5 effector protein rabenosyn-5) (RAB effector RBSN) (Zinc finger FYVE domain-containing protein 20) 783 88,491 Chain (1); Coiled coil (2); Compositional bias (3); Domain (1); Initiator methionine (1); Modified residue (7); Region (4); Sequence conflict (2); Zinc finger (2) FUNCTION: Rab4/Rab5 effector protein acting in early endocytic membrane fusion and membrane trafficking of recycling endosomes. Required for endosome fusion either homotypically or with clathrin coated vesicles. Plays a role in the lysosomal trafficking of CTSD/cathepsin D from the Golgi to lysosomes. Also promotes the recycling of transferrin directly from early endosomes to the plasma membrane. Binds phospholipid vesicles containing phosphatidylinositol 3-phosphate (PtdInsP3). Plays a role in the recycling of transferrin receptor to the plasma membrane (By similarity). {ECO:0000250|UniProtKB:Q9H1K0}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Early endosome membrane {ECO:0000250|UniProtKB:Q9H1K0}; Lipid-anchor {ECO:0000250}. Note=Enriched in endosomes that are in close proximity to clathrin-enriched regions at the cell surface (By similarity). {ECO:0000250|UniProtKB:Q9H1K0}. SUBUNIT: Interacts with EHD1, RAB4A, RAB5A, RAB22A, RAB24 and VPS45. Binds simultaneously to RAB4A and RAB5A in vitro. Interacts with RAB4A and RAB5A that has been activated by GTP binding (By similarity). {ECO:0000250}. +Q6NZN0 RBM26_MOUSE RNA-binding protein 26 (Protein expressed in male leptotene and zygotene spermatocytes 393) (MLZ-393) (RNA-binding motif protein 26) 1012 114,143 Alternative sequence (3); Chain (1); Coiled coil (3); Compositional bias (2); Cross-link (3); Domain (2); Erroneous initiation (3); Frameshift (3); Modified residue (5); Sequence conflict (5); Zinc finger (1) TISSUE SPECIFICITY: Expressed in testis and ovary. {ECO:0000269|PubMed:20339383}. +Q8C5L7 RBM34_MOUSE RNA-binding protein 34 (RNA-binding motif protein 34) 375 41,326 Chain (1); Cross-link (1); Domain (2); Modified residue (2) SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. +Q8BTU7 RCCD1_MOUSE RCC1 domain-containing protein 1 377 40,591 Alternative sequence (1); Chain (1); Modified residue (1); Region (1); Repeat (4); Sequence conflict (8) FUNCTION: Plays a role in transcriptional repression of satellite repeats, possibly by regulating H3K36 methylation levels in centromeric regions together with KDM8. Possibly together with KDM8, is involved in proper mitotic spindle organization and chromosome segregation. Plays a role in regulating alpha-tubulin deacetylation and cytoskeletal microtubule stability, thereby promoting cell migration and TGF-beta-induced epithelial to mesenchymal transition (EMT), potentially through the inhibition of KDM8. {ECO:0000250|UniProtKB:A6NED2}. PTM: Specifically hydroxylated (with R stereochemistry) at C-3 of ARG-141 by KDM8. {ECO:0000250|UniProtKB:A6NED2}. SUBCELLULAR LOCATION: Chromosome {ECO:0000250|UniProtKB:A6NED2}. Note=Colocalizes with trimethylated 'Lys-9' of histone H3 (H3K9me3). {ECO:0000250|UniProtKB:A6NED2}. SUBUNIT: Found in a complex with KDM8. Interacts (via N-terminus) with KDM8 (via N-terminus). {ECO:0000250|UniProtKB:A6NED2}. +Q9QYF1 RDH11_MOUSE Retinol dehydrogenase 11 (EC 1.1.1.300) (Androgen-regulated short-chain dehydrogenase/reductase 1) (Cell line MC/9.IL4-derived protein 1) (M42C60) (Prostate short-chain dehydrogenase/reductase 1) (Retinal reductase 1) (RalR1) (Short-chain aldehyde dehydrogenase) (SCALD) 316 35,148 Active site (1); Binding site (1); Chain (1); Frameshift (1); Modified residue (1); Nucleotide binding (1); Sequence conflict (2); Topological domain (1); Transmembrane (1) TRANSMEM 1 21 Helical; Signal-anchor for type II membrane protein. {ECO:0000269|PubMed:12807874}. TOPO_DOM 22 316 Cytoplasmic. {ECO:0000269|PubMed:12807874}. Cofactor metabolism; retinol metabolism. FUNCTION: Retinol dehydrogenase with a clear preference for NADP (PubMed:12807874, PubMed:29567832). Displays high activity towards 9-cis, 11-cis and all-trans-retinol, and to a lesser extent on 13-cis-retinol (By similarity) (PubMed:12807874). Exhibits also reductive activity towards toxic lipid peroxidation products such as medium-chain aldehydes trans-2-nonenal, nonanal, and cis-6-nonenal (PubMed:12807874). Has no dehydrogenase activity towards steroid (PubMed:12807874). Seems to be required for homeostasis of retinol in liver and testis (PubMed:29567832). {ECO:0000250|UniProtKB:Q8TC12, ECO:0000269|PubMed:12807874, ECO:0000269|PubMed:29567832}. PTM: Not glycosylated. {ECO:0000250|UniProtKB:Q8TC12}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12807874}; Single-pass type II membrane protein {ECO:0000269|PubMed:12807874}. TISSUE SPECIFICITY: Expressed at high level in liver and testis (PubMed:12807874, PubMed:15790565, PubMed:29567832). Expressed at lower levels in smooth muscle, thymus, submaxillary gland and epididymis. In testis, expression is restricted to pachytene spermatocytes. Also expressed in four layers of the retina, including the outer segment of rods and cones (PubMed:12807874, PubMed:15790565). {ECO:0000269|PubMed:12807874, ECO:0000269|PubMed:15790565, ECO:0000269|PubMed:29567832}. +Q4VGL6 RC3H1_MOUSE Roquin-1 (Roquin) (EC 2.3.2.27) (Protein Sanroque) (RING finger and C3H zinc finger protein 1) (RING finger and CCCH-type zinc finger domain-containing protein 1) 1130 125,378 Beta strand (8); Chain (1); Compositional bias (1); Erroneous initiation (1); Helix (18); Metal binding (7); Modified residue (6); Mutagenesis (24); Region (3); Site (2); Turn (5); Zinc finger (2) Protein modification; protein ubiquitination. FUNCTION: Post-transcriptional repressor of mRNAs containing a conserved stem loop motif, called constitutive decay element (CDE), which is often located in the 3'-UTR, as in HMGXB3, ICOS, IER3, NFKBID, NFKBIZ, PPP1R10, TNF, TNFRSF4 and in many more mRNAs (PubMed:23663784, PubMed:25026077, PubMed:18172933). Cleaves translationally inactive mRNAs harboring a stem-loop (SL), often located in their 3'-UTRs, during the early phase of inflammation in a helicase UPF1-independent manner (PubMed:26000482). Binds to CDE and promotes mRNA deadenylation and degradation. This process does not involve miRNAs (PubMed:20412057, PubMed:20639877). In follicular helper T (Tfh) cells, represses of ICOS and TNFRSF4/Ox40 expression, thus preventing spontaneous Tfh cell differentiation, germinal center B-cell differentiation in the absence of immunization and autoimmunity. In resting or LPS-stimulated macrophages, controls inflammation by suppressing TNF expression. Also recognizes CDE in its own mRNA and in that of paralogous RC3H2, possibly leading to feedback loop regulation (PubMed:23583642, PubMed:23583643, PubMed:15917799). Inhibits cooperatively with ZC3H12A the differentiation of helper T cells Th17 in lungs. They repress target mRNA encoding the Th17 cell-promoting factors IL6, ICOS, REL, IRF4, NFKBID and NFKBIZ. The cooperation requires RNA-binding by RC3H1 and the nuclease activity of ZC3H12A (PubMed:25282160). Recognizes and binds mRNAs containing an hexaloop stem-loop motif, called alternative decay element (ADE) (PubMed:27010430). Able to interact with double-stranded RNA (By similarity). miRNA-binding protein that regulates microRNA homeostasis. Enhances DICER-mediated processing of pre-MIR146a but reduces mature MIR146a levels through an increase of 3' end uridylation. Both inhibits ICOS mRNA expression and they may act together to exert the suppression (PubMed:25697406). Acts as a ubiquitin E3 ligase. Pairs with E2 enzymes UBE2A, UBE2B, UBE2D2, UBE2F, UBE2G1, UBE2G2 and UBE2L3 and produces polyubiquitin chains. Show the strongest activity when paired with UBE2N:UBE2V1 or UBE2N:UBE2V2 E2 complexes and generate both short and long polyubiquitin chains (By similarity). {ECO:0000250|UniProtKB:Q5TC82, ECO:0000269|PubMed:15917799, ECO:0000269|PubMed:18172933, ECO:0000269|PubMed:20412057, ECO:0000269|PubMed:20639877, ECO:0000269|PubMed:23583642, ECO:0000269|PubMed:23583643, ECO:0000269|PubMed:23663784, ECO:0000269|PubMed:25026077, ECO:0000269|PubMed:25282160, ECO:0000269|PubMed:25697406, ECO:0000269|PubMed:26000482, ECO:0000269|PubMed:27010430}. PTM: Proteolytically cleaved after Arg-510 and Arg-579 by MALT1 in activated CD4(+) T cells; cleavage at Arg-510 and Arg-579 is critical for promoting RC3H1 degradation in response to T-cell receptor (TCR) stimulation, and hence is necessary for prolonging the stability of a set of mRNAs controlling Th17 cell differentiation. {ECO:0000269|PubMed:25282160}. SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:15917799, ECO:0000269|PubMed:20412057, ECO:0000269|PubMed:20639877, ECO:0000269|PubMed:23583642, ECO:0000269|PubMed:26000482}. Cytoplasmic granule {ECO:0000269|PubMed:26000482}. Note=During stress, such as that induced by arsenite treatment, localizes to cytosolic stress granules (PubMed:26000482). Localization to stress granules, but not to P-bodies, depends upon the RING-type zinc finger. ICOS repression may correlate with the localization to P-bodies, not to stress granules (PubMed:20639877). {ECO:0000269|PubMed:20639877, ECO:0000269|PubMed:26000482}. SUBUNIT: Interacts with DDX6 and EDC4 (PubMed:20639877, PubMed:23583643). Interacts with CCR4-NOT deadenylase complex (PubMed:23663784). Interacts with RC3H1; the interaction is RNA independent (PubMed:25697406). {ECO:0000269|PubMed:20639877, ECO:0000269|PubMed:23583643, ECO:0000269|PubMed:23663784, ECO:0000269|PubMed:25697406}. DOMAIN: The ROQ region is required for CDE RNA-binding (PubMed:27010430, PubMed:25026077, PubMed:23663784). Has 2 separate RNA-binding sites, one for CDE RNA and the other for dsRNA, both sites are important for mRNA decay (By similarity). ADE RNA-binding involves an extended binding surface on the ROQ region with a number of additional residues compared with the CDE RNA (PubMed:27010430). It may also be involved in localization to stress granules (PubMed:20412057, PubMed:23583642). {ECO:0000250|UniProtKB:Q5TC82, ECO:0000269|PubMed:20412057, ECO:0000269|PubMed:23583642, ECO:0000269|PubMed:23663784, ECO:0000269|PubMed:25026077, ECO:0000269|PubMed:27010430}.; DOMAIN: The RING-type zinc finger may be required for proper localization to stress granules, but not to P-bodies. {ECO:0000269|PubMed:23583642}.; DOMAIN: HEPN (higher eukaryotes and prokaryotes nucleotide-binding) are observed in both N- and C-terminal sides of ROQ domain with 3D structure even if they are poredcted on the basis of sequence. {ECO:0000269|PubMed:25697406}. TISSUE SPECIFICITY: Widely expressed, with highest levels in lymph node and thymus and slightly lesser amounts in brain, lung, and spleen (at protein level). Very weak expression in heart, muscle, and kidney (at protein level). Expressed in CD4(+) helper T-cells (at protein level). {ECO:0000269|PubMed:15917799, ECO:0000269|PubMed:23583643}. +P34057 RECO_MOUSE Recoverin (23 kDa photoreceptor cell-specific protein) (Cancer-associated retinopathy protein) (Protein CAR) 202 23,407 Calcium binding (2); Chain (1); Domain (4); Initiator methionine (1); Lipidation (1) FUNCTION: Seems to be implicated in the pathway from retinal rod guanylate cyclase to rhodopsin. May be involved in the inhibition of the phosphorylation of rhodopsin in a calcium-dependent manner. The calcium-bound recoverin prolongs the photoresponse. TISSUE SPECIFICITY: Retina and pineal gland. +Q80XA6 REPS2_MOUSE RalBP1-associated Eps domain-containing protein 2 (Partner of RalBP1) (RalBP1-interacting protein 2) 521 57,750 Calcium binding (1); Chain (1); Coiled coil (1); Compositional bias (1); Domain (2); Modified residue (3); Mutagenesis (2); Region (2) FUNCTION: Involved in growth factor signaling through its influence on the Ral signaling pathway (By similarity). Interaction with ASAP1 may regulate cell migration. {ECO:0000250}. PTM: EGF stimulates phosphorylation on Tyr-residues and induces complex formation with EGF receptor through an adapter protein such as GRB2. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with RALBP1 and GRB2. Binding to RALBP1 does not affect the Ral-binding activity of the latter. It can form a ternary complex with activated Ral and RALBP1. Binds EPN1 (By similarity). Interacts with ASAP1 and this complex can bind paxillin. May form a ternary complex with RALBP1 and ASAP1. {ECO:0000250, ECO:0000269|PubMed:12149250}. +Q8VEE4 RFA1_MOUSE Replication protein A 70 kDa DNA-binding subunit (RP-A p70) (Replication factor A protein 1) (RF-A protein 1) 623 69,037 Chain (1); Cross-link (15); DNA binding (1); Modified residue (7); Natural variant (1) FUNCTION: As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates, that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage. In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation. Through recruitment of ATRIP activates the ATR kinase a master regulator of the DNA damage response. It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin in response to DNA damage. Also recruits to sites of DNA damage proteins like XPA and XPG that are involved in nucleotide excision repair and is required for this mechanism of DNA repair. Plays also a role in base excision repair (BER) probably through interaction with UNG. Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. May also play a role in telomere maintenance. {ECO:0000250|UniProtKB:P27694}. PTM: DNA damage-induced 'Lys-63'-linked polyubiquitination by PRPF19 mediates ATRIP recruitment to the RPA complex at sites of DNA damage and activation of ATR. Ubiquitinated by RFWD3 at stalled replication forks in response to DNA damage: ubiquitination by RFWD3 does not lead to degradation by the proteasome and promotes removal of the RPA complex from stalled replication forks, promoting homologous recombination. {ECO:0000250|UniProtKB:P27694}.; PTM: Sumoylated on lysine residues Lys-458 and Lys-586, with Lys-458 being the major site. Sumoylation promotes recruitment of RAD51 to the DNA damage foci to initiate DNA repair through homologous recombination. Desumoylated by SENP6 (By similarity). {ECO:0000250|UniProtKB:P27694}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P27694}. Nucleus, PML body {ECO:0000250|UniProtKB:P27694}. SUBUNIT: Component of the canonical replication protein A complex (RPA), a heterotrimer composed of RPA1, RPA2 and RPA3. The DNA-binding activity may reside exclusively on the RPA1 subunit. Interacts with PRPF19; the PRP19-CDC5L complex is recruited to the sites of DNA repair where it ubiquitinates the replication protein A complex (RPA). Interacts with RIPK1. Interacts with the polymerase alpha subunit POLA1/p180; this interaction stabilizes the replicative complex and reduces the misincorporation rate of DNA polymerase alpha by acting as a fidelity clamp. Interacts with RAD51 and SENP6 to regulate DNA repair. Interacts with HELB; this interaction promotes HELB recruitment to chromatin following DNA damage. Interacts with PRIMPOL. Interacts with XPA; the interaction is direct and associates XPA with the RPA complex. Interacts with ETAA1; the interaction is direct and promotes ETAA1 recruitment at stalled replication forks. {ECO:0000250|UniProtKB:P27694}. +Q8CHX7 RFTN2_MOUSE Raftlin-2 (Raft-linking protein 2) 500 54,972 Alternative sequence (2); Chain (1); Initiator methionine (1); Lipidation (2); Modified residue (3) FUNCTION: Upon bacterial lipopolysaccharide stimulation, mediates clathrin-dependent internalization of TLR4 in dendritic cells, resulting in activation of TICAM1-mediated signaling and subsequent IFNB1 production (PubMed:27022195). May regulate B-cell antigen receptor-mediated signaling. {ECO:0000269|PubMed:19414744, ECO:0000269|PubMed:27022195}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q14699}; Lipid-anchor {ECO:0000250|UniProtKB:Q14699}. TISSUE SPECIFICITY: Expressed in B-cells, heart, brain, spleen, large intestine and lung (PubMed:19414744). Expressed in dendritic cells and macrophages (PubMed:27022195). {ECO:0000269|PubMed:19414744, ECO:0000269|PubMed:27022195}. +Q9WUK4 RFC2_MOUSE Replication factor C subunit 2 (Activator 1 40 kDa subunit) (A1 40 kDa subunit) (Activator 1 subunit 2) (Replication factor C 40 kDa subunit) (RF-C 40 kDa subunit) (RFC40) 349 38,725 Chain (1); Modified residue (3); Nucleotide binding (1) FUNCTION: The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins proliferating cell nuclear antigen (PCNA) and activator 1. This subunit binds ATP (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Heterotetramer of subunits RFC2, RFC3, RFC4 and RFC5 that can form a complex either with RFC1 or with RAD17. The former interacts with PCNA in the presence of ATP, while the latter has ATPase activity but is not stimulated by PCNA. RFC2 also interacts with PRKAR1A; the complex may be involved in cell survival. Interacts with DDX11. {ECO:0000250|UniProtKB:P35250}. +P48379 RFX2_MOUSE DNA-binding protein RFX2 (Regulatory factor X 2) 717 79,190 Alternative sequence (1); Chain (1); DNA binding (1); Modified residue (2) FUNCTION: Transcription factor that acts as a key regulator of spermatogenesis (PubMed:26248850, PubMed:26162102, PubMed:26853561). Acts by regulating expression of genes required for the haploid phase during spermiogenesis, such as genes required for cilium assembly and function (PubMed:26162102, PubMed:26853561). Recognizes and binds the X-box, a regulatory motif with DNA sequence 5'-GTNRCC(0-3N)RGYAAC-3' present on promoters (PubMed:15229132, PubMed:26162102). Probably activates transcription of the testis-specific histone gene HIST1H1T (PubMed:15229132). {ECO:0000269|PubMed:15229132, ECO:0000269|PubMed:26162102, ECO:0000269|PubMed:26248850, ECO:0000269|PubMed:26853561}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:B2GV50, ECO:0000255|PROSITE-ProRule:PRU00858}. Cytoplasm {ECO:0000250|UniProtKB:B2GV50}. Note=Mainly expressed in the nucleus and at lower level in cytoplasm. {ECO:0000250|UniProtKB:B2GV50}. SUBUNIT: Homodimer; probably only forms homodimers in testis (PubMed:15229132). Heterodimer; heterodimerizes with RFX1 and RFX3 (PubMed:15229132). {ECO:0000269|PubMed:15229132}. +Q7TNK1 RFX4_MOUSE Transcription factor RFX4 (Regulatory factor X 4) 735 83,371 Alternative sequence (5); Chain (1); DNA binding (2); Erroneous initiation (1); Region (1); Sequence conflict (2) FUNCTION: Isoform 1: Transcription factor that plays a role in early brain development. May activate transcription by interacting directly with the X-box. May activate transcription from CX3CL1 promoter through the X-box during brain development. {ECO:0000269|PubMed:12925582, ECO:0000269|PubMed:16893423, ECO:0000269|PubMed:18218630}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00858, ECO:0000269|PubMed:14701801, ECO:0000269|PubMed:18218630}. SUBUNIT: Homodimer. Heterodimer with RFX2 and RFX3. Binds DNA (By similarity). Interacts with GPS2 (PubMed:18218630). {ECO:0000250|UniProtKB:Q33E94, ECO:0000269|PubMed:18218630}. TISSUE SPECIFICITY: Isoform 1: Brain-specific. Isoform 2: Testis-specific. Isoform 1: Highly expressed in the suprachiasmatic nucleus, the central pacemaker site of the circadian clock (at protein level). {ECO:0000269|PubMed:12925582, ECO:0000269|PubMed:14701801}. +Q6PCX7 RGMA_MOUSE Repulsive guidance molecule A (RGM domain family member A) 454 49,676 Alternative sequence (1); Chain (1); Compositional bias (1); Disulfide bond (2); Glycosylation (3); Lipidation (1); Propeptide (2); Sequence conflict (1); Signal peptide (1); Site (1) FUNCTION: Member of the repulsive guidance molecule (RGM) family that performs several functions in the developing and adult nervous system. Regulates cephalic neural tube closure, inhibits neurite outgrowth and cortical neuron branching, and the formation of mature synapses. Binding to its receptor NEO1/neogenin induces activation of RHOA-ROCK1/Rho-kinase signaling pathway through UNC5B-ARHGEF12/LARG-PTK2/FAK1 cascade, leading to collapse of the neuronal growth cone and neurite outgrowth inhibition. Furthermore, RGMA binding to NEO1/neogenin leads to HRAS inactivation by influencing HRAS-PTK2/FAK1-AKT1 pathway. It also functions as a bone morphogenetic protein (BMP) coreceptor that may signal through SMAD1, SMAD5, and SMAD8. {ECO:0000269|PubMed:14749425, ECO:0000269|PubMed:15084667, ECO:0000269|PubMed:15975920, ECO:0000269|PubMed:17389603, ECO:0000269|PubMed:17472960, ECO:0000269|PubMed:17953666, ECO:0000269|PubMed:18519029}. PTM: Autocatalytically cleaved at low pH; the two chains remain linked via two disulfide bonds. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. SUBUNIT: Interacts with NEO1, BMP2 and BMP4. {ECO:0000269|PubMed:15975920, ECO:0000269|PubMed:17389603, ECO:0000269|PubMed:17472960}. TISSUE SPECIFICITY: Expressed in gradient in periventricular layers of the developing nervous system. In adult, expressed in scattered cells throughout the brain. +Q7TQ33 RGMB_MOUSE RGM domain family member B (DRG11-responsive axonal guidance and outgrowth of neurite) (DRAGON) 436 47,181 Chain (1); Disulfide bond (2); Glycosylation (2); Lipidation (1); Propeptide (1); Sequence conflict (7); Signal peptide (1); Site (1) FUNCTION: Member of the repulsive guidance molecule (RGM) family that contributes to the patterning of the developing nervous system. Acts as a bone morphogenetic protein (BMP) coreceptor that potentiates BMP signaling. Promotes neuronal adhesion. May inhibit neurite outgrowth (By similarity). {ECO:0000250, ECO:0000269|PubMed:14985445, ECO:0000269|PubMed:15671031, ECO:0000269|PubMed:15890774}. PTM: GPI-anchored.; PTM: Autocatalytically cleaved at low pH; the two chains remain linked via two disulfide bonds. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15890774}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:15890774}. Membrane raft {ECO:0000269|PubMed:15890774}. SUBUNIT: Homooligomer. Interacts with DRGX. Interacts with BMP2 and BMP4. Interacts with the BMP type I receptors ACVR1, BMPR1A and BMPR1B and with the BMP type II receptor ACVR2B. The functional complex with its receptor NEO1/neogenin appears to be a heterotetramer with a 2:2 stoichiometry, RGM molecules acting as staples that brings two NEO1 receptors together without interacting themselves, this arrangement leads to activation of downstream signaling via RhoA. {ECO:0000269|PubMed:14985445, ECO:0000269|PubMed:15671031}. TISSUE SPECIFICITY: Detected in neonatal and adult dorsal root ganglion sensory neurons, spinal cord, and brain (at protein level). Also expressed at high levels in retinal ganglion cells of developing mouse, extending to the optic nerve (at protein level). Expressed in testis, epididymis, ovary, uterus, and pituitary. {ECO:0000269|PubMed:14985445, ECO:0000269|PubMed:15890774}. +Q7TQ32 RGMC_MOUSE Hemojuvelin (Hemochromatosis type 2 protein homolog) (Hemojuvelin BMP coreceptor) (RGM domain family member C) 420 44,848 Alternative sequence (1); Chain (1); Disulfide bond (2); Glycosylation (3); Lipidation (1); Modified residue (1); Propeptide (1); Sequence conflict (2); Signal peptide (1); Site (1) FUNCTION: Acts as a bone morphogenetic protein (BMP) coreceptor. Through enhancement of BMP signaling regulates hepcidin (HAMP) expression and regulates iron homeostasis. {ECO:0000269|PubMed:16604073}. PTM: Autocatalytically cleaved at low pH; the two chains remain linked via two disulfide bonds. Also proteolytically processed by TMPRSS6, several fragments being released in the extracellular space; regulates HJV activity in BMP signaling and thefore iron homeostasis. {ECO:0000250, ECO:0000250|UniProtKB:Q6ZVN8}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. Note=Also released in the extracellular space. {ECO:0000250|UniProtKB:Q6ZVN8}. SUBUNIT: Interacts with BMP2 and BMP4. Interacts with BMPR1B (By similarity). Interacts with TMPRSS6 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Muscle cell lineage. {ECO:0000269|PubMed:14678836}. +O08899 RGS4_MOUSE Regulator of G-protein signaling 4 (RGS4) 205 23,289 Chain (1); Domain (1); Lipidation (3); Sequence conflict (1) FUNCTION: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Activity on G(z)-alpha is inhibited by phosphorylation of the G-protein. Activity on G(z)-alpha and G(i)-alpha-1 is inhibited by palmitoylation of the G-protein (By similarity). {ECO:0000250}. PTM: Either Cys-2 or Cys-12 or both are palmitoylated. {ECO:0000250}.; PTM: Phosphorylated by cyclic GMP-dependent protein kinase. {ECO:0000250}. TISSUE SPECIFICITY: Expressed at high levels in brain, moderately low levels in heart, and very low levels in lung, liver, and skeletal muscle. +Q78DX7 ROS1_MOUSE Proto-oncogene tyrosine-protein kinase ROS (EC 2.7.10.1) (Proto-oncogene c-Ros) (Proto-oncogene c-Ros-1) (Receptor tyrosine kinase c-ros oncogene 1) (c-Ros receptor tyrosine kinase) 2340 261,967 Active site (1); Binding site (1); Chain (1); Domain (10); Glycosylation (7); Modified residue (2); Mutagenesis (1); Nucleotide binding (1); Sequence conflict (29); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1855 1875 Helical. {ECO:0000255}. TOPO_DOM 29 1854 Extracellular. {ECO:0000255}.; TOPO_DOM 1876 2340 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan receptor tyrosine kinase (RTK) that plays a role in epithelial cell differentiation and regionalization of the proximal epididymal epithelium. May activate several downstream signaling pathways related to cell differentiation, proliferation, growth and survival including the PI3 kinase-mTOR signaling pathway. Mediates the phosphorylation of PTPN11, an activator of this pathway. May also phosphorylate and activate the transcription factor STAT3 to control anchorage-independent cell growth. Mediates the phosphorylation and the activation of VAV3, a guanine nucleotide exchange factor regulating cell morphology. May activate other downstream signaling proteins including AKT1, MAPK1, MAPK3, IRS1, and PLCG2. {ECO:0000269|PubMed:11266449, ECO:0000269|PubMed:11799110, ECO:0000269|PubMed:8657124, ECO:0000269|PubMed:8675006, ECO:0000269|PubMed:9774423}. PTM: Phosphorylated. Probably autophosphorylates. Phosphorylation at Tyr-2267 and/or Tyr-2327 recruits PTPN11 (By similarity). Phosphorylation at Tyr-2267 is required for the interaction with PTPN6 that mediates ROS1 dephosphorylation. Phosphorylation at Tyr-2267 stimulates the kinase activity and the activation of the ERK1 signaling cascade. {ECO:0000250, ECO:0000269|PubMed:11266449}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Interacts with PTPN11; may activate the PI3 kinase-mTOR signaling pathway. Interacts with VAV3; constitutive interaction mediating VAV3 phosphorylation (By similarity). Interacts with PTPN6 (via SH2 1 domain); the interaction is direct and promotes ROS1 dephosphorylation. {ECO:0000250, ECO:0000269|PubMed:11266449}. TISSUE SPECIFICITY: Expressed by epithelial cells of the caput epididymis (at protein level). {ECO:0000269|PubMed:8675006}. +Q9CWZ3 RBM8A_MOUSE RNA-binding protein 8A (RNA-binding motif protein 8A) (Ribonucleoprotein RBM8A) 174 19,889 Alternative sequence (1); Chain (1); Cross-link (1); Domain (1); Initiator methionine (1); Modified residue (4); Sequence conflict (12) FUNCTION: Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). The MAGOH-RBM8A heterodimer inhibits the ATPase activity of EIF4A3, thereby trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The MAGOH-RBM8A heterodimer interacts with the EJC key regulator PYM1 leading to EJC disassembly in the cytoplasm and translation enhancement of EJC-bearing spliced mRNAs by recruiting them to the ribosomal 48S pre-initiation complex. Its removal from cytoplasmic mRNAs requires translation initiation from EJC-bearing spliced mRNAs. Associates preferentially with mRNAs produced by splicing. Does not interact with pre-mRNAs, introns, or mRNAs produced from intronless cDNAs. Associates with both nuclear mRNAs and newly exported cytoplasmic mRNAs. The MAGOH-RBM8A heterodimer is a component of the nonsense mediated decay (NMD) pathway. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms; the function is different from the established EJC assembly (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus speckle {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Nucleocytoplasmic shuttling protein. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. Colocalizes with the core EJC, ALYREF/THOC4, NXF1 and UAP56 in the nucleus and nuclear speckles (By similarity). {ECO:0000250}. SUBUNIT: Heterodimer with RBM8A. Part of the mRNA splicing-dependent exon junction complex (EJC) complex; the core complex contains CASC3, EIF4A3, MAGOH and RBM8A. Interacts with PYM1; the interaction is direct and dissociates the EJC from spliced mRNAs. Found in a post-splicing complex with NXF1, RBM8A, UPF1, UPF2, UPF3A, UPF3B and RNPS1. Interacts with BAT1, MAGOH, OVCA1, UPF3B, RNPS1, SRRM1 and ALYREF/THOC4. Interacts with IPO13; the interaction mediates the nuclear import of the MAGOH-RBM8A heterodimer. Identified in the spliceosome C complex. Associates with polysomes (By similarity). {ECO:0000250}. +Q8BHS3 RBM22_MOUSE Pre-mRNA-splicing factor RBM22 (RNA-binding motif protein 22) 420 46,896 Chain (1); Compositional bias (1); Cross-link (3); Domain (1); Initiator methionine (1); Modified residue (4); Sequence conflict (2); Zinc finger (1) FUNCTION: Involved in the first step of pre-mRNA splicing. Binds directly to the internal stem-loop (ISL) domain of the U6 snRNA and to the pre-mRNA intron near the 5' splice site during the activation and catalytic phases of the spliceosome cycle. Involved in both translocations of the nuclear SLU7 to the cytoplasm and the cytosolic calcium-binding protein PDCD6 to the nucleus upon cellular stress responses (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Mainly located in the nucleus. Translocated from the nucleus to the cytoplasm after heat shock cell treatment. May be shuttling between the nucleus and the cytosol (By similarity). {ECO:0000250}. SUBUNIT: Identified in the spliceosome C complex. Interacts with PDCD6; the interaction induces translocation of PDCD6 in the cytoplasm (By similarity). {ECO:0000250}. DOMAIN: The C-terminus RRM domain and the zinc finger motif are necessary for RNA-binding. {ECO:0000250}. +B2RY56 RBM25_MOUSE RNA-binding protein 25 (RNA-binding motif protein 25) 838 99,552 Chain (1); Compositional bias (2); Cross-link (8); Domain (2); Erroneous initiation (5); Modified residue (7); Region (1); Sequence caution (2); Sequence conflict (5) FUNCTION: RNA-binding protein that acts as a regulator of alternative pre-mRNA splicing. Involved in apoptotic cell death through the regulation of the apoptotic factor BCL2L1 isoform expression. Modulates the ratio of proapoptotic BCL2L1 isoform S to antiapoptotic BCL2L1 isoform L mRNA expression. When overexpressed, stimulates proapoptotic BCL2L1 isoform S 5'-splice site (5'-ss) selection, whereas its depletion caused the accumulation of antiapoptotic BCL2L1 isoform L. Promotes BCL2L1 isoform S 5'-ss usage through the 5'-CGGGCA-3' RNA sequence. Its association with LUC7L3 promotes U1 snRNP binding to a weak 5' ss in a 5'-CGGGCA-3'-dependent manner. Binds to the exonic splicing enhancer 5'-CGGGCA-3' RNA sequence located within exon 2 of the BCL2L1 pre-mRNA (By similarity). {ECO:0000250}. PTM: Sumoylated. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000255|PROSITE-ProRule:PRU00627}. Cytoplasm {ECO:0000250}. Note=Colocalizes predominantly, with SFRS2 and LUC7L3 splicing factors, in nuclear speckles. Cytoplasmic localization is faint (By similarity). {ECO:0000250}. SUBUNIT: Interacts with LUC7L3 and SRRM1 (By similarity). Specifically associates with functional splicing complexes, including Sm proteins and U1, U2, U4, U5 and U6 snRNAs (By similarity). Associates with exon junction complex (EJC) proteins, including APEX1, BAT1, NCBP1, RBM8A and RNPS1. Interaction with NCBP1 is RNA-dependent (By similarity). {ECO:0000250}. DOMAIN: The PWI domain binds nucleic acids with significant help from its N-terminal flanking basic region. It has an equal preference for binding to single- or double-stranded species, and it contributes to RBM25 role in modulation of alternative splicing, maybe by mediating RNA-dependent association with LUC7L3 (By similarity). {ECO:0000250}. +Q9D0V7 RCAS1_MOUSE Receptor-binding cancer antigen expressed on SiSo cells (Cancer-associated surface antigen RCAS1) (Estrogen receptor-binding fragment-associated gene 9 protein) 213 24,319 Chain (1); Coiled coil (1); Compositional bias (1); Modified residue (3); Sequence conflict (4); Topological domain (2); Transmembrane (1) TRANSMEM 8 27 Helical; Signal-anchor for type III membrane protein. {ECO:0000255}. TOPO_DOM 1 7 Extracellular. {ECO:0000255}.; TOPO_DOM 28 213 Cytoplasmic. {ECO:0000255}. FUNCTION: May participate in suppression of cell proliferation and induces apoptotic cell death through activation of interleukin-1-beta converting enzyme (ICE)-like proteases. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Note=Predominantly located in the Golgi. {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. DOMAIN: The coiled coil domain is necessary for the homodimerization. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. Expressed in heart, brain, spleen, liver, kidney and testis. {ECO:0000269|PubMed:11374862}. +P54726 RD23A_MOUSE UV excision repair protein RAD23 homolog A (HR23A) (mHR23A) 363 39,706 Chain (1); Cross-link (1); Domain (3); Modified residue (8); Sequence conflict (3) FUNCTION: Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Binds to 'Lys-48'-linked polyubiquitin chains in a length-dependent manner and with a lower affinity to 'Lys-63'-linked polyubiquitin chains. Proposed to be capable to bind simultaneously to the 26S proteasome and to polyubiquitinated substrates and to deliver ubiquitinated proteins to the proteasome (By similarity). {ECO:0000250}.; FUNCTION: Involved in nucleotide excision repair and is thought to be functional equivalent for Rad23b in global genome nucleotide excision repair (GG-NER) by association with Xpc. In vitro, the XPC:RAD23A dimer has NER activity. Can stabilize Xpc. Reported differences to Rad23b in regard to NER activity and Xpc stabilization are probably due to differences in expression levels with Rad23a being much less expressed than Rad23b. {ECO:0000269|PubMed:12815074, ECO:0000269|PubMed:15336624}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with XPC; the interaction is suggesting the existence of a functional equivalent variant XPC complex. Interacts with PSMD4 and PSMC5. Interacts with ATXN3. Interacts with UBQLN2 (By similarity). {ECO:0000250}. DOMAIN: The ubiquitin-like (UBL) and the UBA (ubiquitin-associated) domains interact intramolecularly in a highly dynamic manner, as each UBA domain competes for an overlapping UBL domain surface. Binding of ubiquitin or proteasome subunit Psmd4 disrupt the UBL-UBA domain interactions and drive Rad23a in to an open conformation (By similarity). {ECO:0000250}. +Q6PGA0 RCOR3_MOUSE REST corepressor 3 451 49,779 Alternative sequence (2); Chain (1); Coiled coil (1); Compositional bias (1); Cross-link (2); Domain (2); Erroneous initiation (1); Frameshift (1); Modified residue (4) FUNCTION: May act as a component of a corepressor complex that represses transcription. {ECO:0000305}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00512, ECO:0000255|PROSITE-ProRule:PRU00624}. +Q8VIG1 REST_MOUSE RE1-silencing transcription factor (Neural-restrictive silencer factor) 1082 117,784 Alternative sequence (4); Chain (1); Compositional bias (2); Modified residue (1); Region (3); Sequence caution (1); Sequence conflict (4); Zinc finger (9) FUNCTION: Transcriptional repressor which binds neuron-restrictive silencer element (NRSE) and represses neuronal gene transcription in non-neuronal cells. Restricts the expression of neuronal genes by associating with two distinct corepressors, mSin3 and CoREST, which in turn recruit histone deacetylase to the promoters of REST-regulated genes. Mediates repression by recruiting the BHC complex at RE1/NRSE sites which acts by deacetylating and demethylating specific sites on histones, thereby acting as a chromatin modifier. Transcriptional repression by REST-CDYL via the recruitment of histone methyltransferase EHMT2 may be important in transformation suppression. Key repressor of gene expression in hypoxia; represses genes in hypoxia by direct binding to an RE1/NRSE site on their promoter regions (By similarity). Represses the expression of SRRM4 in non-neural cells to prevent the activation of neural specific splicing events (PubMed:21884984). Acts as a regulator of osteoblast differentiation (PubMed:25727884). {ECO:0000250|UniProtKB:Q13127, ECO:0000269|PubMed:21884984, ECO:0000269|PubMed:25727884}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21284946}. Cytoplasm {ECO:0000250|UniProtKB:Q13127}. Note=Colocalizes with ZFP90 in the nucleus (PubMed:21284946). In response to hypoxia, there is a more pronounced increase in levels in the nucleus as compared to the cytoplasm (By similarity). {ECO:0000250|UniProtKB:Q13127, ECO:0000269|PubMed:21284946}. SUBUNIT: Interacts with SIN3A, SIN3B and RCOR1. Interacts with CDYL. Interacts with EHMT1 and EHMT2 only in the presence of CDYL. Part of a complex containing at least CDYL, REST, WIZ, SETB1, EHMT1 and EHMT2. Interacts (via zinc-finger DNA-binding domain) with ZFP90 (via N- and C-termini); the interaction inhibits REST repressor activity (PubMed:21284946). TISSUE SPECIFICITY: Expressed in many non-neuronal tissues including the heart and liver (PubMed:7871435). Abundantly expressed in osteoblastic lineage cells (PubMed:25727884). {ECO:0000269|PubMed:25727884, ECO:0000269|PubMed:7871435}. +P15307 REL_MOUSE Proto-oncogene c-Rel 587 64,960 Chain (1); Domain (1); Initiator methionine (1); Modified residue (2); Motif (1); Region (1); Sequence conflict (5) FUNCTION: Proto-oncogene that may play a role in differentiation and lymphopoiesis. NF-kappa-B is a pleiotropic transcription factor which is present in almost all cell types and is involved in many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. The NF-kappa-B heterodimer RELA/p65-c-Rel is a transcriptional activator (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Component of the NF-kappa-B p65-c-Rel complex. Component of the NF-kappa-B p50-c-Rel complex. Component of the NF-kappa-B p52-c-Rel complex. Homodimer; component of the NF-kappa-B c-Rel-c-Rel complex. Interacts with NKIRAS1. Interacts with NFKBIB. Interacts with NFKBIE (By similarity). {ECO:0000250}. +Q9Z205 RFXK_MOUSE DNA-binding protein RFXANK (Ankyrin repeat-containing adapter protein Tvl-1) (Regulatory factor X subunit B) (RFX-B) (Regulatory factor X-associated ankyrin-containing protein) 269 29,232 Alternative sequence (1); Chain (1); Repeat (5) FUNCTION: Activates transcription from class II MHC promoters. Activation requires the activity of the MHC class II transactivator/CIITA. May regulate other genes in the cell. RFX binds the X1 box of MHC-II promoters (By similarity). May also potentiate the activation of RAF1 (PubMed:10329666). {ECO:0000250|UniProtKB:O14593, ECO:0000269|PubMed:10329666}. PTM: Phosphorylated by RAF1. {ECO:0000269|PubMed:10329666}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10329666}. Nucleus {ECO:0000269|PubMed:10329666}. SUBUNIT: Forms homodimers (PubMed:10329666). The RFX heterotetrameric complex consists of 2 molecules of RFX5 and one each of RFXAP and RFX-B/RFXANK; with each subunit representing a separate complementation group. Interacts (via ankyrin repeats) with RFX5 (via PxLPxI/L motif); the interaction is direct. RFX forms cooperative DNA binding complexes with X2BP and CBF/NF-Y. RFX associates with CIITA to form an active transcriptional complex (By similarity). Interacts with RAF1 (PubMed:10329666). Interacts with RFX7 (By similarity). {ECO:0000250|UniProtKB:O14593, ECO:0000269|PubMed:10329666}. DOMAIN: Interacts with RAF-1 via its C-terminal ankyrin repeat domain. The same domain also mediates its homodimerization (PubMed:10329666). The third ankyrin repeat is required for association with the two other RFX subunits; RFX5 and RFXAP. The three central ANK repeats mediate binding to the PxLPxI/L motif of RFX5 (By similarity). {ECO:0000250|UniProtKB:O14593, ECO:0000269|PubMed:10329666}. TISSUE SPECIFICITY: Expressed primarily in thymus, lung and testis. +P48377 RFX1_MOUSE MHC class II regulatory factor RFX1 (Regulatory factor X 1) (Transcription factor RFX1) 963 103,707 Chain (1); DNA binding (1); Modified residue (3); Sequence conflict (1) FUNCTION: Regulatory factor essential for MHC class II genes expression. Binds to the X boxes of MHC class II genes (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00858}. SUBUNIT: Homodimer; binds DNA as a homodimer (By similarity). Heterodimer; heterodimerizes with RFX2 and RFX3 (PubMed:15229132). {ECO:0000250|UniProtKB:P22670, ECO:0000269|PubMed:15229132}. +Q8CHD8 RFIP3_MOUSE Rab11 family-interacting protein 3 (FIP3-Rab11) (Rab11-FIP3) 1047 118,535 Alternative sequence (2); Calcium binding (2); Chain (1); Coiled coil (1); Compositional bias (1); Domain (3); Modified residue (5); Region (1) FUNCTION: Acts as a regulator of endocytic traffic by participating in membrane delivery. Required for the abcission step in cytokinesis, possibly by acting as an 'address tag' delivering recycling endosome membranes to the cleavage furrow during late cytokinesis (By similarity). Also required for the structural integrity of the endosomal recycling compartment during interphase. Acts as an adapter protein linking the dynein motor complex to various cargos and converts dynein from a non-processive to a highly processive motor in the presence of dynactin. Facilitates the interaction between dynein and dynactin and activates dynein processivity (the ability to move along a microtubule for a long distance without falling off the track) (By similarity). {ECO:0000250|UniProtKB:O75154, ECO:0000269|PubMed:18685082}. SUBCELLULAR LOCATION: Recycling endosome membrane {ECO:0000250|UniProtKB:O75154}; Peripheral membrane protein {ECO:0000250|UniProtKB:O75154}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:O75154}. Cleavage furrow {ECO:0000250|UniProtKB:O75154}. Midbody {ECO:0000250|UniProtKB:O75154}. Note=In early mitosis remains diffuse and distributed through the cell. The onset of anaphase sequesters these vesicles to the centrosomes at the opposite poles of the cell. During telophase these vesicles move from the centrosomes, to the furrow, and then to the midbody to aid in abscission. Interaction with Rab11 mediates localization to endosomes. Interaction with ARF6 mediates localization to the midbody. {ECO:0000250|UniProtKB:O75154}. SUBUNIT: Homodimer. Forms a complex with Rab11 (RAB11A or RAB11B) and ARF6. Interacts with RAB11A; the interaction is direct. Interacts with RAB11B, RAB25 and RAB11FIP4. Interacts with ARF6. Interacts with RACGAP1/MgcRacGAP; interaction takes place during late stage of cytokinesis and is required for recruitment to the midbody. Interacts with EXOC7 (By similarity). Interacts with ASAP1 (PubMed:18685082). Interacts with dynein intermediate chain and dynactin (DCTN1) (By similarity). {ECO:0000250|UniProtKB:O75154, ECO:0000269|PubMed:18685082}. DOMAIN: The RBD-FIP domain mediates the interaction with Rab11 (RAB11A or RAB11B). {ECO:0000250|UniProtKB:O75154}. +Q8VE91 RETR1_MOUSE Reticulophagy regulator 1 (Reticulophagy receptor 1) 480 52,967 Alternative sequence (3); Chain (1); Modified residue (1); Motif (1); Region (1); Topological domain (5); Transmembrane (4) TRANSMEM 43 64 Helical. {ECO:0000255}.; TRANSMEM 76 93 Helical. {ECO:0000255}.; TRANSMEM 99 116 Helical. {ECO:0000255}.; TRANSMEM 192 212 Helical. {ECO:0000255}. TOPO_DOM 1 42 Cytoplasmic. {ECO:0000250|UniProtKB:Q9H6L5}.; TOPO_DOM 65 75 Lumenal. {ECO:0000305}.; TOPO_DOM 94 98 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 117 191 Lumenal. {ECO:0000305}.; TOPO_DOM 213 480 Cytoplasmic. {ECO:0000250|UniProtKB:Q9H6L5}. FUNCTION: Endoplasmic reticulum-anchored autophagy receptor that mediates ER delivery into lysosomes through sequestration into autophagosomes (PubMed:26040720). Promotes membrane remodeling and ER scission via its membrane bending capacity and targets the fragments into autophagosomes via interaction with ATG8 family proteins (PubMed:26040720). Required for long-term survival of nociceptive and autonomic ganglion neurons (PubMed:19838196, PubMed:26040720). {ECO:0000269|PubMed:19838196, ECO:0000269|PubMed:26040720}. SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:19838196}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9H6L5}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Interacts with ATG8 family modifier proteins MAP1LC3A, MAP1LC3B, GABARAP, GABARAPL1 and GABARAPL2. {ECO:0000250|UniProtKB:Q9H6L5}. DOMAIN: The LIR motif interacts with ATG8 family proteins and is necessary to target the ER fragments to autophagosomes for lysosomal degradation. {ECO:0000269|PubMed:26040720}.; DOMAIN: The reticulon homology domain provides capacity to bend the membrane and promotes ER scission (PubMed:26040720). This domain does not show relevant similarities with reticulon domains, preventing any domain predictions within the protein sequence. {ECO:0000269|PubMed:26040720, ECO:0000305}. TISSUE SPECIFICITY: Predominantly expressed in sensory and autonomic ganglia has demonstrated by in situ hybridizations of embryonic day 14.5 mouse embryo sections. Detected specifically in organelle-like intracellular structures of the small and large neurons of dorsal root ganglia (DRG) and in Neuro-2a cells, a tumor cell line that is related to autonomic ganglion neurons (at protein level). {ECO:0000269|PubMed:19838196}. +Q6PAQ4 REXO4_MOUSE RNA exonuclease 4 (EC 3.1.-.-) (Exonuclease XPMC2) (Prevents mitotic catastrophe 2 protein homolog) 432 47,599 Chain (1); Cross-link (1); Domain (1); Erroneous initiation (2); Modified residue (1); Sequence caution (1) FUNCTION: May function as an exonuclease. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. SUBUNIT: Can bind ESR1 and ESR2. This interaction is abrogated by estrogen and augmented by tamoxifen treatment (By similarity). {ECO:0000250}. +Q148V7 RELCH_MOUSE RAB11-binding protein RELCH (LisH domain and HEAT repeat-containing protein KIAA1468) (RAB11-binding protein containing LisH, coiled-coil, and HEAT repeats) 1216 134,587 Alternative sequence (4); Chain (1); Coiled coil (2); Domain (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (14); Region (1); Repeat (3); Sequence caution (1); Sequence conflict (3) FUNCTION: Regulates intracellular cholesterol distribution from recycling endosomes to the trans-Golgi network through interactions with RAB11 and OSBP. Functions in membrane tethering and promotes OSBP-mediated cholesterol transfer between RAB11-bound recycling endosomes and OSBP-bound Golgi-like membranes. {ECO:0000250|UniProtKB:Q9P260}. SUBCELLULAR LOCATION: Recycling endosome {ECO:0000269|PubMed:29514919}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q9P260}. Note=Colocalization with RAB11A in recycling endosomes (PubMed:29514919). Translocated to the trans-Golgi network area in an OSBP-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q9P260, ECO:0000269|PubMed:29514919}. SUBUNIT: Interacts with RAB11A (VIA-GTP form) (PubMed:29514919). Interacts with RAB11B (PubMed:29514919). Interacts (via the third HEAT repeat) with OSBP (via C-terminus) (PubMed:29514919). Found in a complex composed of RELCH, OSBP1 and RAB11A (PubMed:29514919). {ECO:0000269|PubMed:29514919}. +Q8R367 RERG_MOUSE Ras-related and estrogen-regulated growth inhibitor 199 22,580 Chain (1); Compositional bias (1); Nucleotide binding (3) FUNCTION: Binds GDP/GTP and possesses intrinsic GTPase activity. Has higher affinity for GDP than for GTP (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +Q99P86 RETNB_MOUSE Resistin-like beta (Cysteine-rich secreted protein A12-beta) (Cysteine-rich secreted protein FIZZ2) (RELMbeta) 105 11,278 Beta strand (6); Chain (1); Disulfide bond (6); Helix (2); Mutagenesis (1); Sequence conflict (2); Signal peptide (1); Turn (2) FUNCTION: Probable hormone. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11209052}. SUBUNIT: Homodimer; disulfide-linked (PubMed:11358969, PubMed:15834545, PubMed:15155948). Heterodimer with RETNLG (PubMed:15834545). {ECO:0000269|PubMed:11358969, ECO:0000269|PubMed:15155948, ECO:0000269|PubMed:15834545}. TISSUE SPECIFICITY: Strongly expressed in colon, and at lower levels in ileum (PubMed:15834545). In colon, found throughout the crypt and surface epithelium and in goblet cells (at protein level) (PubMed:15834545). Specific to the gastrointestinal tract; not detected in other tissues tested (PubMed:11209052, PubMed:15834545). {ECO:0000269|PubMed:11209052, ECO:0000269|PubMed:15834545}. +Q61103 REQU_MOUSE Zinc finger protein ubi-d4 (Apoptosis response zinc finger protein) (BRG1-associated factor 45D) (BAF45D) (D4, zinc and double PHD fingers family 2) (Protein requiem) 391 44,230 Chain (1); Cross-link (7); Erroneous initiation (2); Initiator methionine (1); Modified residue (7); Sequence conflict (2); Zinc finger (3) FUNCTION: Plays an active role in transcriptional regulation by binding modified histones H3 and H4. Is a negative regulator of myeloid differentiation of hematopoietic progenitor cells (By similarity). Might also have a role in the development and maturation of lymphoid cells (PubMed:7961935). Involved in the regulation of non-canonical NF-kappa-B pathway (By similarity). {ECO:0000250|UniProtKB:Q92785, ECO:0000269|PubMed:7961935}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92785}. Cytoplasm {ECO:0000250|UniProtKB:Q92785}. SUBUNIT: Interacts with the nucleosomes, in particular nucleosomes bearing histone H3 crotonylated at 'Lys-14' (H3K14cr) for which DPF2 has high affinity. Also interacts (via PHD-type zinc finger domains) with histone H3 butyrylated at 'Lys-14' (H3K14bu), histone H3 propionylated at 'Lys-14' (H3K14pr), and histone H3 acetylated at 'Lys-14' (H3K14ac). Interacts with histone H3 acetylated at 'Lys-9' (H3K9ac), histone H3 di-methylated at 'Lys-9' (H3K9me2), and histone H3 tri-methylated at 'Lys-9' (H3K9me3). Interacts with histone H4 acetylated at 'Lys-12' (H4K12ac). Interacts with histone H4 acetylated at 'Lys-16' (H4K16ac). Interacts with SWI/SNF complex components. Interacts with SMARCA2, SMARCA4, SMARCB1 and SMARCD1. Interacts with SMARCC1, SMARCC2 and ACTL6A. Interacts with RUNX1. {ECO:0000250|UniProtKB:Q92785}. TISSUE SPECIFICITY: In embryo, highest levels are seen in brain, eyes, thymus and olfactory epithelium in nose, whereas several other tissues, including the musculoskeletal system, show moderate expression. In adult, higher expression in testis, medium in thymus and spleen, lower in certain parts of the brain as the hippocampus. No expression in adult heart, lung, liver, duodenum and kidney. {ECO:0000269|PubMed:9680388}. +Q99P87 RETN_MOUSE Resistin (Adipose tissue-specific secretory factor) (ADSF) (Adipose-specific cysteine-rich secreted protein A12-alpha) (Cysteine-rich secreted protein FIZZ3) 114 12,492 Beta strand (5); Chain (1); Disulfide bond (6); Helix (1); Signal peptide (1); Turn (1) FUNCTION: Hormone that seems to suppress insulin ability to stimulate glucose uptake into adipose cells. Potentially links obesity to diabetes. {ECO:0000269|PubMed:11201732}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11201732}. SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:11358969, ECO:0000269|PubMed:15155948}. TISSUE SPECIFICITY: Expressed in white but not brown adipose tissue in a variety of organs. {ECO:0000269|PubMed:11201732}. +Q9EPU0 RENT1_MOUSE Regulator of nonsense transcripts 1 (EC 3.6.4.-) (ATP-dependent helicase RENT1) (Nonsense mRNA reducing factor 1) (NORF1) (Up-frameshift suppressor 1 homolog) (mUpf1) 1124 123,967 Alternative sequence (1); Binding site (4); Chain (1); Compositional bias (2); Modified residue (9); Motif (2); Nucleotide binding (1); Region (1); Sequence conflict (10); Zinc finger (1) FUNCTION: RNA-dependent helicase and ATPase required for nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. Is recruited to mRNAs upon translation termination and undergoes a cycle of phosphorylation and dephosphorylation; its phosphorylation appears to be a key step in NMD. Recruited by release factors to stalled ribosomes together with the SMG1C protein kinase complex to form the transient SURF (SMG1-UPF1-eRF1-eRF3) complex. In EJC-dependent NMD, the SURF complex associates with the exon junction complex (EJC) (located 50-55 or more nucleotides downstream from the termination codon) through UPF2 and allows the formation of an UPF1-UPF2-UPF3 surveillance complex which is believed to activate NMD. Phosphorylated UPF1 is recognized by EST1B/SMG5, SMG6 and SMG7 which are thought to provide a link to the mRNA degradation machinery involving exonucleolytic and endonucleolytic pathways, and to serve as adapters to protein phosphatase 2A (PP2A), thereby triggering UPF1 dephosphorylation. UPF1 can also activate NMD without UPF2 or UPF3, and in the absence of the NMD-enhancing downstream EJC indicative for alternative NMD pathways. Plays a role in replication-dependent histone mRNA degradation at the end of phase S; the function is independent of UPF2. For the recognition of premature termination codons (PTC) and initiation of NMD a competitive interaction between UPF1 and PABPC1 with the ribosome-bound release factors is proposed. The ATPase activity of UPF1 is required for disassembly of mRNPs undergoing NMD (By similarity). Essential for embryonic viability. {ECO:0000250}. PTM: Phosphorylated by SMG1; required for formation of mRNA surveillance complexes. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, P-body {ECO:0000250}. Nucleus {ECO:0000250}. Note=Hyperphosphorylated form is targeted to the P-body, while unphosphorylated protein is distributed throughout the cytoplasm. {ECO:0000250}. SUBUNIT: Found in a post-splicing messenger ribonucleoprotein (mRNP) complex. Associates with the exon junction complex (EJC). Associates with the SGM1C complex; is phosphorylated by the complex kinase component SGM1. Interacts with UPF2. Interacts with UPF3A and UPF3B. Interacts with EST1A. Interacts with SLBP. Interacts (when hyperphosphorylated) with PNRC2. Interacts with AGO1 and AGO2. Interacts with GSPT2. Interacts with isoform 1 and isoform 5 of ADAR/ADAR1. Interacts with SMG7. Interacts with ZC3H12A; this interaction occurs in a mRNA translationally active- and termination-dependent manner and is essential for ZC3H12A-mediated degradation of target mRNAs. Interacts with CPSF6. Interacts with MOV10; the interaction is direct and RNA-dependent (By similarity). {ECO:0000250|UniProtKB:Q92900}. DOMAIN: The [ST]-Q motif constitutes a recognition sequence for kinases from the PI3/PI4-kinase family. {ECO:0000250}. +Q64FW2 RETST_MOUSE All-trans-retinol 13,14-reductase (EC 1.3.99.23) (All-trans-13,14-dihydroretinol saturase) (RetSat) (PPAR-alpha-regulated and starvation-induced gene protein) 609 67,334 Chain (1); Erroneous initiation (1); Mutagenesis (3); Nucleotide binding (1); Sequence conflict (7); Signal peptide (1) FUNCTION: Catalyzes the saturation of all-trans-retinol to all-trans-13,14-dihydroretinol (PubMed:15358783, PubMed:17253779, PubMed:19139408). Does not exhibit any activity toward all-trans-retinoic acid, nor 9-cis, 11-cis or 13-cis-retinol isomers (PubMed:15358783). May play a role in the metabolism of vitamin A (PubMed:15358783, PubMed:17253779). Independently of retinol conversion, may regulate liver metabolism upstream of MLXIPL/ChREBP (PubMed:28855500). Required for adipocyte differentiation in a 3T3-L1 cell culture model (PubMed:19139408). This effect seems not to mimic the in vivo situation in which animals show increased adiposity in the absence of RETSAT (PubMed:19940255). {ECO:0000269|PubMed:15358783, ECO:0000269|PubMed:17253779, ECO:0000269|PubMed:19139408, ECO:0000269|PubMed:19940255, ECO:0000269|PubMed:28855500, ECO:0000305|PubMed:19940255}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15358783, ECO:0000269|PubMed:19139408}; Peripheral membrane protein {ECO:0000269|PubMed:15358783}. TISSUE SPECIFICITY: Predominantly expressed in the liver (at protein level) (PubMed:19940255). Also expressed at high levels in kidney, intestine, and white fat and brown fat (PubMed:15358783, PubMed:18289917, PubMed:19139408, PubMed:28855500). Weakly expressed in heart, skeletal muscle and testis and barely detected in the lung, brain and spleen (PubMed:15358783, PubMed:18289917, PubMed:28855500). Up-regulated in the liver of diet-induced obese mice, compared to lean animals (PubMed:28855500). Down-regulated in adipose tissue of obese mice; this decrease could be due to the impact of inflammatory cells on adipocytes (PubMed:19139408). {ECO:0000269|PubMed:15358783, ECO:0000269|PubMed:18289917, ECO:0000269|PubMed:19139408, ECO:0000269|PubMed:19940255, ECO:0000269|PubMed:28855500}. +Q61493 REV3L_MOUSE DNA polymerase zeta catalytic subunit (EC 2.7.7.7) (Protein reversionless 3-like) (REV3-like) (Seizure-related protein 4) 3122 350,711 Beta strand (1); Chain (1); Helix (3); Metal binding (8); Modified residue (3); Motif (1); Region (1); Sequence conflict (15); Zinc finger (1) FUNCTION: Catalytic subunit of the DNA polymerase zeta complex, an error-prone polymerase specialized in translesion DNA synthesis (TLS). Lacks an intrinsic 3'-5' exonuclease activity and thus has no proofreading function. {ECO:0000250|UniProtKB:O60673}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Heterodimer with MAD2L2. This dimer forms the minimal DNA polymerase zeta complex (Pol-zeta2), with REV3L bearing DNA polymerase catalytic activity, although its activity is very low in this context. Component of the tetrameric Pol-zeta complex (Pol-zeta4), which consists of REV3L, MAD2L2, POLD2 and POLD3; Pol-zeta4 is the fully active form of DNA polymerase zeta. {ECO:0000250|UniProtKB:O60673}. DOMAIN: The CysB motif binds 1 4Fe-4S cluster and is required for the formation of polymerase complexes. {ECO:0000250}. +Q8R323 RFC3_MOUSE Replication factor C subunit 3 (Activator 1 38 kDa subunit) (A1 38 kDa subunit) (Activator 1 subunit 3) (Replication factor C 38 kDa subunit) (RF-C 38 kDa subunit) (RFC38) 356 40,526 Chain (1); Modified residue (2) FUNCTION: The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins proliferating cell nuclear antigen (PCNA) and activator 1. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Heterotetramer of subunits RFC2, RFC3, RFC4 and RFC5 that can form a complex either with RFC1 or with RAD17. The former interacts with PCNA in the presence of ATP, while the latter has ATPase activity but is not stimulated by PCNA (By similarity). {ECO:0000250}. +Q9QZB1 RGS20_MOUSE Regulator of G-protein signaling 20 (RGS20) (Regulator of G-protein signaling Z1) 239 26,986 Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (1); Natural variant (1) FUNCTION: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds selectively to G(z)-alpha and G(alpha)-i2 subunits, accelerates their GTPase activity and regulates their signaling activities. The G(z)-alpha activity is inhibited by the phosphorylation and palmitoylation of the G-protein. Negatively regulates mu-opioid receptor-mediated activation of the G-proteins. {ECO:0000269|PubMed:14997173, ECO:0000269|PubMed:15827571, ECO:0000269|PubMed:16900103}. PTM: Fatty acylated. Heavily palmitoylated in the cysteine string motif (By similarity). {ECO:0000250}.; PTM: N- and O-glycosylated in synapsomal membranes. {ECO:0000269|PubMed:14997173}.; PTM: Serine phosphorylated in synapsomal membranes. {ECO:0000269|PubMed:16900103}.; PTM: Sumoylated with SUMO1, SUMO2 and SUMO3. Sumoylation increases binding to the G-proteins, G(alpha)-i2 and G(z), and interaction with mu-opioid receptors. {ECO:0000269|PubMed:16900103}. SUBCELLULAR LOCATION: Membrane; Lipid-anchor. Nucleus. Cytoplasm. Note=Shuttles between the cytoplasm/cell membrane and the nucleus Anchored to the membrane through palmitoylation. {ECO:0000250}. SUBUNIT: Forms a complex with G(alpha)z/i2 subunits and mu-opioid receptors; the formation of this complex results in mu-opioid receptor desensitization. Interacts with OPRM1 (By similarity). {ECO:0000250}. +G3XA57 RFIP2_MOUSE Rab11 family-interacting protein 2 (Rab11-FIP2) 512 58,207 Alternative sequence (1); Chain (1); Domain (2); Modified residue (2); Motif (3); Region (2) FUNCTION: A Rab11 effector binding preferentially phosphatidylinositol 3,4,5-trisphosphate (PtdInsP3) and phosphatidic acid (PA) and acting in the regulation of the transport of vesicles from the endosomal recycling compartment (ERC) to the plasma membrane. Involved in insulin granule exocytosis. Also involved in receptor-mediated endocytosis and membrane trafficking of recycling endosomes, probably originating from clathrin-coated vesicles. Required in a complex with MYO5B and RAB11 for the transport of NPC1L1 to the plasma membrane. Also acts as a regulator of cell polarity. {ECO:0000269|PubMed:19335615}. PTM: Phosphorylation at Ser-227 by MARK2 regulates epithelial cell polarity. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. Recycling endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Translocates with RAB11A from the vesicles of the endocytic recycling compartment (ERC) to the plasma membrane. {ECO:0000250}. SUBUNIT: Homooligomerizes in a Rab11-independent manner. Forms a heterooligomeric complex with RAB11FIP4. Interacts with AP2A1, MYO5B, RAB25 and REPS1. Interacts with RAB11A and RAB11B (activated GTP-bound form). Interacts with NPC1L1. Interacts (via NPF motifs) with EHD1 and EHD3 (By similarity). {ECO:0000250}. +Q9WVM1 RGAP1_MOUSE Rac GTPase-activating protein 1 (Male germ cell RacGap) (MgcRacGAP) 628 70,158 Chain (1); Coiled coil (1); Cross-link (2); Domain (1); Modified residue (18); Region (1); Sequence conflict (5); Zinc finger (1) FUNCTION: Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Required for proper attachment of the midbody to the cell membrane during cytokinesis. Plays key roles in controlling cell growth and differentiation of hematopoietic cells through mechanisms other than regulating Rac GTPase activity. Also involved in the regulation of growth-related processes in adipocytes and myoblasts. May be involved in regulating spermatogenesis and in the RACGAP1 pathway in neuronal proliferation. Shows strong GAP (GTPase activation) activity towards CDC42 and RAC1 and less towards RHOA. Essential for the early stages of embryogenesis. May play a role in regulating cortical activity through RHOA during cytokinesis. May participate in the regulation of sulfate transport in male germ cells. {ECO:0000269|PubMed:10235109, ECO:0000269|PubMed:10493933, ECO:0000269|PubMed:10979956, ECO:0000269|PubMed:11287179}. PTM: Phosphorylated at multiple sites in the midbody during cytokinesis. Phosphorylation by AURKB on Ser-388 at the midbody is, at least in part, responsible for exerting its latent GAP activity towards RhoA. Phosphorylation on multiple serine residues by PLK1 enhances its association with ECT2 and is critical for cleavage furrow formation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12590651}. Cytoplasm {ECO:0000269|PubMed:12590651}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:12590651}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:12590651}. Cleavage furrow {ECO:0000250|UniProtKB:Q9H0H5}. Midbody, Midbody ring {ECO:0000250|UniProtKB:Q9H0H5}. Cell membrane {ECO:0000250|UniProtKB:Q9H0H5}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9H0H5}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9H0H5}. Note=During interphase, localized to the nucleus and cytoplasm along with microtubules, in anaphase, is redistributed to the central spindle and, in telophase and cytokinesis, to the midbody ring, also called Flemming body. Colocalizes with RHOA at the myosin contractile ring during cytokinesis. Colocalizes with ECT2 to the mitotic spindles during anaphase/metaphase, the cleavage furrow during telophase and at the midbody at the end of cytokinesis. Colocalizes with Cdc42 to spindle microtubules from prometaphase to telophase (By similarity). Colocalizes with RND2 in Golgi-derived proacrosomal vesicles and the acrosome. {ECO:0000250|UniProtKB:Q9H0H5}. SUBUNIT: Heterotetramer of two molecules each of RACGAP1 and KIF23. Found in the centralspindlin complex composed of RACGAP1 and KIF23. Associates with alpha-, beta- and gamma-tubulin and microtubules. Interacts via its Rho-GAP domain with RND2. Associates with AURKB during M phase. Interacts via its Rho-GAP domain and basic region with PRC1. The interaction with PRC1 inhibits its GAP activity towards CDC42 in vitro, which may be required for maintaining normal spindle morphology. Interacts with SLC26A8 via its N-terminus. Interacts with RAB11FIP3. Interacts with ECT2; the interaction is direct, occurs at anaphase and during cytokinesis in a microtubule-dependent manner and is enhanced by phosphorylation by PLK1. Interacts with KIF23; the interaction is direct (By similarity). {ECO:0000250}. DOMAIN: The coiled coil region is indispensible for localization to the midbody during cytokinesis. {ECO:0000250|UniProtKB:Q9P2W2}.; DOMAIN: The phorbol-ester/DAG-type zinc finger domain mediates interaction with membranes enriched in phosphatidylinositol 3,4,5-trisphosphate and is required during mitotic cytokinesis for normal attachment of the midbody to the cell membrane. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in testis, thymus and spleen and weakly expressed in brain, heart, skeletal muscle and kidney. In testis, expression is restricted to germ cells with the highest levels of expression found in spermatocytes. Not detected in adult liver. Also expressed in fetal liver and in several hematopoietic cell lines. {ECO:0000269|PubMed:10493933, ECO:0000269|PubMed:10979956, ECO:0000269|PubMed:11287179}. +P48381 RFX3_MOUSE Transcription factor RFX3 (Regulatory factor X 3) 749 83,512 Alternative sequence (3); Chain (1); DNA binding (1); Sequence conflict (3) FUNCTION: Transcription factor required for ciliogenesis and islet cell differentiation during endocrine pancreas development. Essential for the differentiation of nodal monocilia and left-right asymmetry specification during embryogenesis. Required for the biogenesis of motile cilia by governing growth and beating efficiency of motile cells (PubMed:15121860, PubMed:19671664). Also required for ciliated ependymal cell differentiation (PubMed:16930429). Together with RFX6, participates in the differentiation of 4 of the 5 islet cell types during endocrine pancreas development, with the exception of pancreatic PP (polypeptide-producing) cells (PubMed:17229940). Regulates transcription by forming a heterodimer with another RFX protein and binding to the X-box in the promoter of target genes (By similarity). Regulates the expression of genes involved in ciliary assembly (DYNC2LI1, FOXJ1 and BBS4) and genes involved in ciliary motility (DNAH11, DNAH9 and DNAH5). Represses transcription of MAP1A in non-neuronal cells but not in neuronal cells. {ECO:0000250|UniProtKB:P48380, ECO:0000269|PubMed:15121860, ECO:0000269|PubMed:16930429, ECO:0000269|PubMed:17229940, ECO:0000269|PubMed:19671664}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00858, ECO:0000269|PubMed:19671664}. SUBUNIT: Heterodimer; heterodimerizes with RFX1 and RFX2, and RFX6. {ECO:0000250|UniProtKB:P48380, ECO:0000269|PubMed:15229132}. TISSUE SPECIFICITY: Expressed in ciliated cells of the node and in the ciliated ependymal cells of the subcommissural organ (SCO), choroid plexuses (CP) and ventricular walls during embryonic and postnatal development. Expressed in developing and mature pancreatic endocrine cells during embryogenesis and in adults (at protein level). {ECO:0000269|PubMed:15121860, ECO:0000269|PubMed:16930429, ECO:0000269|PubMed:17229940}. +Q9JL61 RFX5_MOUSE DNA-binding protein Rfx5 (Regulatory factor X 5) 658 69,735 Chain (1); DNA binding (1); Initiator methionine (1); Modified residue (3); Motif (1); Region (2); Sequence conflict (3) FUNCTION: Activates transcription from class II MHC promoters. Recognizes X-boxes. Mediates cooperative binding between RFX and NF-Y. RFX binds the X1 box of MHC-II promoters. {ECO:0000269|PubMed:10779326}. PTM: Phosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00858, ECO:0000269|PubMed:10779326}. SUBUNIT: Homodimer. The RFX heterotetrameric complex consists of 2 molecules of RFX5 and one each of RFXAP and RFX-B/RFXANK; with each subunit representing a separate complementation group (PubMed:10779326). Interacts (via PxLPxI/L motif) with RFXANK (via ankyrin repeats); the interaction is direct (By similarity). RFX forms cooperative DNA binding complexes with X2BP and CBF/NF-Y. RFX associates with CIITA to form an active transcriptional complex (PubMed:10779326). {ECO:0000250|UniProtKB:P48382, ECO:0000269|PubMed:10779326}. DOMAIN: The N-terminus is required for dimer formation, association with RFXANK and RFXAP, assembly of the RFX complex, and for binding of this complex to its X box target site in the MHC-II promoter. The C-terminus mediates cooperative binding between the RFX complex and NF-Y.; DOMAIN: The PxLPxI/L motif mediates interaction with ankyrin repeats of RFXANK. {ECO:0000250|UniProtKB:P48382}. +Q99NE5 RIMS1_MOUSE Regulating synaptic membrane exocytosis protein 1 (Rab-3-interacting molecule 1) (RIM 1) (Rab-3-interacting protein 1) 1463 163,161 Alternative sequence (9); Chain (1); Domain (4); Modified residue (21); Mutagenesis (1); Zinc finger (1) FUNCTION: Rab effector involved in exocytosis (PubMed:11797009). May act as scaffold protein that regulates neurotransmitter release at the active zone. Essential for maintaining normal probability of neurotransmitter release and for regulating release during short-term synaptic plasticity (PubMed:11797009). Plays a role in dendrite formation by melanocytes (By similarity). {ECO:0000250|UniProtKB:Q86UR5, ECO:0000269|PubMed:11797009}. PTM: Phosphorylated by BRSK1. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell junction, synapse {ECO:0000250}. Cell junction, synapse, presynaptic cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. SUBUNIT: Binds SNAP25, SYT1 and CACNA1B. Interaction with SYT1 is enhanced by calcium ions. Interaction with SNAP25 is weaker in the presence of calcium ions. Interacts with TSPOAP1 and RIMBP2; interacts with PPFIA3 and PPFIA4. Interacts with ERC1 (By similarity). Interacts with RAB3A, RAB3B and RAB3D that have been activated by GTP-binding. Interacts with RAB3C, RAB10, RAB26 AND RAB37. Binds UNC13A. {ECO:0000250, ECO:0000269|PubMed:11431472, ECO:0000269|PubMed:12578829}. +Q9EQZ7 RIMS2_MOUSE Regulating synaptic membrane exocytosis protein 2 (Rab-3-interacting molecule 2) (RIM 2) (Rab-3-interacting protein 2) 1530 172,863 Alternative sequence (4); Chain (1); Compositional bias (1); Domain (4); Modified residue (9); Zinc finger (1) FUNCTION: Rab effector involved in exocytosis. May act as scaffold protein. Plays a role in dendrite formation by melanocytes (By similarity). {ECO:0000250|UniProtKB:Q9UQ26}. SUBCELLULAR LOCATION: Cell junction, synapse, synaptosome. SUBUNIT: Interacts with TSPOAP1 and RIMBP2. Interacts with PPFIA3 and PPFIA4. Interacts via its zinc finger with the first C2 domain of UNC13A. Forms a complex consisting of UNC13A, RIMS2 and RAB3A (By similarity). Heterodimer with PCLO. Part of a ternary complex involving PCLO and EPAC2. Interacts with RAB3A and RAB3B that have been activated by GTP-binding. Interacts with RAB3C, RAB3D and RAB26. {ECO:0000250, ECO:0000269|PubMed:11056535, ECO:0000269|PubMed:12401793, ECO:0000269|PubMed:12578829}. TISSUE SPECIFICITY: Detected in testis, pituitary and an insulinoma cell line. Detected at low levels in cerebellar cortex. {ECO:0000269|PubMed:11056535}. +Q80U57 RIMS3_MOUSE Regulating synaptic membrane exocytosis protein 3 (Nim3) (RIM3 gamma) (Rab-3-interacting molecule 3) (RIM 3) 307 32,589 Chain (1); Domain (1); Modified residue (2) FUNCTION: Regulates synaptic membrane exocytosis. {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, synapse {ECO:0000250}. SUBUNIT: Binds PPFIA3 (By similarity). Does not bind RAB3. {ECO:0000250}. +P60191 RIMS4_MOUSE Regulating synaptic membrane exocytosis protein 4 (RIM4 gamma) (Rab3-interacting molecule 4) (RIM 4) 269 29,329 Chain (1); Domain (1); Modified residue (2) FUNCTION: Regulates synaptic membrane exocytosis. {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, synapse {ECO:0000250}. SUBUNIT: Binds PPFIA3 (By similarity). Does not bind RAB3. {ECO:0000250}. +Q921Q7 RIN1_MOUSE Ras and Rab interactor 1 (Ras interaction/interference protein 1) 763 83,014 Chain (1); Compositional bias (2); Domain (3); Modified residue (9) FUNCTION: Ras effector protein, which may serve as an inhibitory modulator of neuronal plasticity in aversive memory formation. Can affect Ras signaling at different levels. First, by competing with RAF1 protein for binding to activated Ras. Second, by enhancing signaling from ABL1 and ABL2, which regulate cytoskeletal remodeling. Third, by activating RAB5A, possibly by functioning as a guanine nucleotide exchange factor (GEF) for RAB5A, by exchanging bound GDP for free GTP, and facilitating Ras-activated receptor endocytosis (By similarity). {ECO:0000250, ECO:0000269|PubMed:12574403}. PTM: Phosphorylated on tyrosine residues by ABL1 and ABL2. Phosphorylation at Ser-340 by PRKD1 induces interaction with 14-3-3 proteins (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Some amount is membrane-associated. {ECO:0000250}. SUBUNIT: Interacts with the GTP-bound form of Ras proteins (NRAS, HRAS and KRAS). This interaction prevents the association between RAF1 and Ras. Interacts with 14-3-3 proteins YWHAB, YWHAE and YWHAZ when phosphorylated on Ser-340. Interacts with the SH3 domain of ABL1 and ABL2. Interacts with RAB5A. The interaction with Ras is probably regulated and antagonized by the interaction with 14-3-3 proteins. The interaction with 14-3-3 proteins is regulated by phosphorylation on Ser-340 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in brain. Weakly or no expressed in other tissues, except in testis, where it is expressed at intermediate level. In brain, it is mainly expressed in postnatal forebrain neurons in which it is localized in dendrites and colocalizes with Ras. {ECO:0000269|PubMed:12574403}. +Q9D684 RIN2_MOUSE Ras and Rab interactor 2 (Ras interaction/interference protein 2) 903 101,559 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (3); Erroneous initiation (3); Modified residue (3); Region (1); Sequence caution (4); Sequence conflict (11) FUNCTION: Ras effector protein. May function as an upstream activator and/or downstream effector for RAB5B in endocytic pathway. May function as a guanine nucleotide exchange (GEF) of RAB5B, required for activating the RAB5 proteins by exchanging bound GDP for free GTP (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homotetramer; probably composed of anti-parallel linkage of two parallel dimers. Interacts with Ras. Interacts with RAB5B, with a much higher affinity for GTP-bound activated RAB5B. Does not interact with other members of the Rab family (By similarity). {ECO:0000250}. +P59729 RIN3_MOUSE Ras and Rab interactor 3 (Ras interaction/interference protein 3) 980 107,220 Chain (1); Compositional bias (2); Domain (3); Region (1); Sequence conflict (4) FUNCTION: Ras effector protein that functions as a guanine nucleotide exchange (GEF) for RAB5B and RAB31, by exchanging bound GDP for free GTP. Required for normal RAB31 function (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8TB24}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q8TB24}. Early endosome {ECO:0000250|UniProtKB:Q8TB24}. Note=Activation of tyrosine phosphorylation signaling induces translocation to cytoplasmic vesicles. {ECO:0000250|UniProtKB:Q8TB24}. SUBUNIT: Interacts with CD2AP, RAB5B, RAB31 and BIN1. {ECO:0000250}. +P11157 RIR2_MOUSE Ribonucleoside-diphosphate reductase subunit M2 (EC 1.17.4.1) (Ribonucleotide reductase small chain) (Ribonucleotide reductase small subunit) 390 45,096 Active site (1); Beta strand (2); Chain (1); Helix (17); Metal binding (8); Modified residue (2); Turn (2) Genetic information processing; DNA replication. FUNCTION: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. Inhibits Wnt signaling (By similarity). {ECO:0000250}. PTM: Phosphorylation on Ser-20 relieves the inhibitory effect on Wnt signaling. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Heterodimer of a large and a small subunit. +P07742 RIR1_MOUSE Ribonucleoside-diphosphate reductase large subunit (EC 1.17.4.1) (Ribonucleoside-diphosphate reductase subunit M1) (Ribonucleotide reductase large subunit) 792 90,210 Active site (3); Binding site (4); Chain (1); Disulfide bond (1); Domain (1); Modified residue (3); Region (5); Sequence conflict (1); Site (8) Genetic information processing; DNA replication. FUNCTION: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Heterodimer of a large and a small subunit. Interacts with RRM2B. Interacts with AHCYL1 which inhibits its activity (By similarity). {ECO:0000250|UniProtKB:P23921}. +Q9WVL4 RK_MOUSE Rhodopsin kinase (RK) (EC 2.7.11.14) (G protein-coupled receptor kinase 1) 564 63,837 Active site (1); Binding site (1); Chain (1); Domain (3); Lipidation (1); Modified residue (6); Nucleotide binding (1); Propeptide (1); Region (2) FUNCTION: Retina-specific kinase involved in the signal turnoff via phosphorylation of rhodopsin (RHO), the G protein- coupled receptor that initiates the phototransduction cascade. This rapid desensitization is essential for scotopic vision and permits rapid adaptation to changes in illumination. {ECO:0000269|PubMed:10097103, ECO:0000269|PubMed:10704496}. PTM: Autophosphorylated, Ser-21 is a minor site of autophosphorylation compared to Ser-491 and Thr-492. Phosphorylation at Ser-21 is regulated by light and activated by cAMP. {ECO:0000250}.; PTM: Farnesylation is required for full activity. {ECO:0000250|UniProtKB:P28327}. SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P28327}; Lipid-anchor {ECO:0000250|UniProtKB:P28327}. SUBUNIT: Interacts (when prenylated) with PDE6D; this promotes release from membranes. {ECO:0000250|UniProtKB:P28327}. TISSUE SPECIFICITY: Primarily located in rod outer segments of retina photoreceptor cells. Also detected in cone photoreceptor cells (at protein level) (PubMed:10704496). Detected in retina (PubMed:10097103, PubMed:10704496). {ECO:0000269|PubMed:10097103, ECO:0000269|PubMed:10704496, ECO:0000269|PubMed:11717351, ECO:0000269|PubMed:21504899}. +P35979 RL12_MOUSE 60S ribosomal protein L12 165 17,805 Beta strand (4); Chain (1); Cross-link (1); Helix (2); Modified residue (3); Sequence conflict (1); Turn (2) FUNCTION: Binds directly to 26S ribosomal RNA. +Q8C796 RCOR2_MOUSE REST corepressor 2 (M-CoREST) 523 57,908 Chain (1); Coiled coil (1); Compositional bias (1); Cross-link (1); Domain (3); Erroneous initiation (1); Modified residue (6) FUNCTION: May act as a component of a corepressor complex that represses transcription. {ECO:0000305}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00512, ECO:0000255|PROSITE-ProRule:PRU00624}. TISSUE SPECIFICITY: Predominantly, but not exclusively, expressed in neural tissue. Strongly expressed in neural domains of the developing brain of the developing mouse CNS. {ECO:0000269|PubMed:11578870}. +Q7TQA3 RDHE2_MOUSE Epidermal retinol dehydrogenase 2 (EPHD-2) (RDH-E2) (EC 1.1.1.105) (Retinal short-chain dehydrogenase reductase 2) (retSDR2) (Short-chain dehydrogenase reductase 9) (Short-chain dehydrogenase/reductase family 16C member 5) 309 34,193 Active site (1); Binding site (1); Chain (1); Nucleotide binding (1); Transmembrane (2) TRANSMEM 11 31 Helical. {ECO:0000255}.; TRANSMEM 270 290 Helical. {ECO:0000255}. Cofactor metabolism; retinol metabolism. FUNCTION: Oxidoreductase with strong preference for NAD. Active in both the oxidative and reductive directions. Oxidizes all-trans-retinol in all-trans-retinaldehyde. No activity was detected with 11-cis-retinol or 11-cis-retinaldehyde as substrates with either NAD(+)/NADH or NADP(+)/NADPH (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q9CQU3 RER1_MOUSE Protein RER1 196 22,988 Chain (1); Initiator methionine (1); Modified residue (5); Transmembrane (3) TRANSMEM 41 61 Helical. {ECO:0000255}.; TRANSMEM 63 83 Helical. {ECO:0000255}.; TRANSMEM 140 160 Helical. {ECO:0000255}. FUNCTION: Involved in the retrieval of endoplasmic reticulum membrane proteins from the early Golgi compartment. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +O54916 REPS1_MOUSE RalBP1-associated Eps domain-containing protein 1 (RalBP1-interacting protein 1) 795 86,519 Alternative sequence (5); Beta strand (2); Calcium binding (1); Chain (1); Coiled coil (1); Compositional bias (1); Domain (3); Erroneous initiation (2); Helix (4); Modified residue (17); Region (1); Sequence conflict (3); Turn (1) FUNCTION: May coordinate the cellular actions of activated EGF receptors and Ral-GTPases. PTM: EGF stimulates phosphorylation on Tyr-residues. SUBCELLULAR LOCATION: Membrane, clathrin-coated pit {ECO:0000250}. Note=Colocalize with ITSN1 at the plasma membrane in structures that are most probably clathrin-coated pits. {ECO:0000250}. SUBUNIT: Homodimer (Potential). Interacts with RALBP1, CRK and GRB2. Binding to RALBP1 does not affect its Ral-binding activity. Forms a complex with the SH3 domains of CRK and GRB2 which may link it to an EGF-responsive tyrosine kinase. Interacts with RAB11FIP2 (By similarity). Interacts with AMPH, ITSN1 (via SH3 domains) and SGIP1; may be involved in clathrin-mediated endocytosis (By similarity). {ECO:0000250, ECO:0000305}. TISSUE SPECIFICITY: Expressed in all tissues examined. The highest level expression was found in the kidney and testis. +Q8BJU9 RF1ML_MOUSE Peptide chain release factor 1-like, mitochondrial (Mitochondrial translational release factor 1-like) 373 42,248 Chain (1); Coiled coil (1); Modified residue (1); Transit peptide (1) FUNCTION: Mitochondrial peptide chain release factor that directs the termination of translation in response to the peptide chain termination codons UAA and UAG. {ECO:0000250}. PTM: Methylation of glutamine in the GGQ triplet is conserved from bacteria to mammals. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. +Q9EP95 RETNA_MOUSE Resistin-like alpha (Cysteine-rich secreted protein A12-gamma) (Cysteine-rich secreted protein FIZZ1) (Hypoxia-induced mitogenic factor) (Parasite-induced macrophage novel gene 1 protein) (RELMalpha) 111 11,936 Chain (1); Disulfide bond (5); Erroneous initiation (1); Signal peptide (1) FUNCTION: Probable hormone. Plays a role in pulmonary vascular remodeling. {ECO:0000269|PubMed:20582166}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Monomer. {ECO:0000269|PubMed:11358969}. TISSUE SPECIFICITY: Highest levels in adipose tissue. +Q6ZQM0 RFFL_MOUSE E3 ubiquitin-protein ligase rififylin (EC 2.3.2.27) (RING finger and FYVE-like domain-containing protein 1) (Fring) (RING-type E3 ubiquitin transferase rififylin) 377 42,249 Alternative sequence (4); Chain (1); Domain (2); Modified residue (4); Sequence conflict (1); Zinc finger (2) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that regulates several biological processes through the ubiquitin-mediated proteasomal degradation of various target proteins. Mediates 'Lys-48'-linked polyubiquitination of PRR5L and its subsequent proteasomal degradation thereby indirectly regulating cell migration through the mTORC2 complex. Also ubiquitinates the caspases CASP8 and CASP10, promoting their proteasomal degradation, to negatively regulate apoptosis downstream of death domain receptors. Also negatively regulates the tumor necrosis factor-mediated signaling pathway through targeting of RIPK1 to ubiquitin-mediated proteasomal degradation. Negatively regulates p53/TP53 through its direct ubiquitination and targeting to proteasomal degradation. Indirectly, may also negatively regulate p53/TP53 through ubiquitination and degradation of SFN. May also play a role in endocytic recycling. {ECO:0000269|PubMed:15229288, ECO:0000269|PubMed:22609986}. PTM: Autoubiquitinated. {ECO:0000250}.; PTM: Palmitoylated. {ECO:0000250}.; PTM: Undergoes caspase-mediated cleavage upon death-receptor activation, by TNFSF10 for instance. May be mediated by the caspases CASP8 and CASP10 in a negative feedback loop (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:15229288}. Cell membrane {ECO:0000269|PubMed:15229288}; Peripheral membrane protein {ECO:0000269|PubMed:15229288}. Recycling endosome membrane {ECO:0000305|PubMed:15229288}; Peripheral membrane protein {ECO:0000305|PubMed:15229288}. Note=The FYVE-type zinc finger may mediate phosphatidylinositol phosphate-binding and control subcellular localization. SUBUNIT: Interacts with CASP8 and CASP10. Interacts with RIPK1 (via protein kinase domain); involved in RIPK1 ubiquitination. Interacts with PRR5L. Interacts (via RING-type zinc finger) with p53/TP53; involved in p53/TP53 ubiquitination. Interacts (via RING-type zinc finger) with MDM2; the interaction stabilizes MDM2. {ECO:0000250|UniProtKB:Q8WZ73}. DOMAIN: The FYVE-type zinc finger domain is required for localization to the recycling endosome membranes and the function in endocytic recycling. {ECO:0000269|PubMed:15229288}.; DOMAIN: The RING-type zinc finger is required for the ubiquitination of target proteins. {ECO:0000250|UniProtKB:Q8WZ73}. TISSUE SPECIFICITY: Ubiquitous. Detected in heart, brain, spleen, lung, liver, skeletal muscle, kidney, testis, thymus, whole embryo and embryonic stem cells. {ECO:0000269|PubMed:15229288}. +Q8BIF2 RFOX3_MOUSE RNA binding protein fox-1 homolog 3 (Fox-1 homolog C) (Hexaribonucleotide-binding protein 3) (Fox-3) (Neuronal nuclei antigen) (NeuN antigen) 374 40,610 Alternative sequence (3); Chain (1); Compositional bias (2); Domain (1); Modified residue (3); Sequence conflict (1); Site (8) FUNCTION: Pre-mRNA alternative splicing regulator. Regulates alternative splicing of RBFOX2 to enhance the production of mRNA species that are targeted for nonsense-mediated decay (NMD). {ECO:0000269|PubMed:19713214, ECO:0000269|PubMed:21747913}. PTM: Phosphorylated. {ECO:0000305|PubMed:15605376}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm.; SUBCELLULAR LOCATION: Isoform 1: Nucleus.; SUBCELLULAR LOCATION: Isoform 4: Cytoplasm.; SUBCELLULAR LOCATION: Isoform 5: Nucleus. TISSUE SPECIFICITY: Widely expressed in brain, including in cerebral cortex, hippocampus, thalamus, caudate/putamen, cerebellum, as well as in the spinal cord (at protein level). Not expressed in all neuronal cells within a region, in cerebellum, expression is absent in Purkinje cells (at protein level). Expressed in the retina in the ganglion cells and some cells in the inner nuclear layer, but absent from the photoreceptor cells and most cells in the inner nuclear layer (at protein level). {ECO:0000269|PubMed:1483388, ECO:0000269|PubMed:15605376, ECO:0000269|PubMed:19713214, ECO:0000269|PubMed:21747913}. +Q8CIK8 RFWD3_MOUSE E3 ubiquitin-protein ligase RFWD3 (EC 2.3.2.27) (RING finger and WD repeat domain-containing protein 3) (RING finger protein 201) 774 84,312 Chain (1); Coiled coil (1); Erroneous initiation (1); Modified residue (2); Repeat (3); Sequence conflict (6); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase required for the repair of DNA interstrand cross-links (ICL) in response to DNA damage. Plays a key role in RPA-mediated DNA damage signaling and repair. Acts by mediating ubiquitination of the RPA complex (RPA1, RPA2 and RPA3 subunits) and RAD51 at stalled replication forks, leading to remove them from DNA damage sites and promote homologous recombination. Also mediates the ubiquitination of p53/TP53 in the late response to DNA damage, and acts as a positive regulator of p53/TP53 stability, thereby regulating the G1/S DNA damage checkpoint. May act by catalyzing the formation of short polyubiquitin chains on p53/TP53 that are not targeted to the proteasome. In response to ionizing radiation, interacts with MDM2 and enhances p53/TP53 ubiquitination, possibly by restricting MDM2 from extending polyubiquitin chains on ubiquitinated p53/TP53. {ECO:0000250|UniProtKB:Q6PCD5}. PTM: Phosphorylated at Ser-59 and Ser-75 upon DNA damage by ATM or ATR. ATM phosphorylation occurs at early times upon DNA damage, while ATR is the major kinase at later times. Phosphorylation by ATM and ATR is required to stabilize p53/TP53. Part of the phosphorylation depends upon RPA2 presence. {ECO:0000250|UniProtKB:Q6PCD5}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6PCD5}. Nucleus, PML body {ECO:0000250|UniProtKB:Q6PCD5}. Cytoplasm {ECO:0000250|UniProtKB:Q6PCD5}. Note=In undamaged cells, found both in the cytoplasm and in the nucleus, partially associated with PML nuclear bodies. In response to replication block, such as that caused by hydroxyurea treatment, or to DNA damage caused by ionizing radiations or doxorubicin, recruited to the nucleus, to stalled replication forks or to sites of DNA repair. This recruitment depends upon RPA2. {ECO:0000250|UniProtKB:Q6PCD5}. SUBUNIT: Interacts with MDM2 and p53/TP53. Binds to the RPA complex via direct interaction with RPA2. Interacts with RAD51. {ECO:0000250|UniProtKB:Q6PCD5}. DOMAIN: The coiled coil domain may be involved in RPA2-binding. {ECO:0000250|UniProtKB:Q6PCD5}. +Q9DBX1 RGCC_MOUSE Regulator of cell cycle RGCC (Response gene to complement 32 protein) (RGC-32) 137 14,717 Chain (1); Compositional bias (2); Modified residue (7); Sequence conflict (2) FUNCTION: Modulates the activity of cell cycle-specific kinases. Enhances CDK1 activity. May contribute to the regulation of the cell cycle. May inhibit growth of glioma cells by promoting arrest of mitotic progression at the G2/M transition. Fibrogenic factor contributing to the pathogenesis of renal fibrosis through fibroblast activation. {ECO:0000269|PubMed:21990365}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Note=Cytoplasmic in unstimulated cells. Nuclear after activation by complement. Associated with the centrosome during prometaphase and metaphase (By similarity). {ECO:0000250}. SUBUNIT: Interacts with CDK1 and PLK1 (By similarity). Interacts with SMAD3. {ECO:0000250, ECO:0000269|PubMed:21990365}. +Q8C7R7 RFX6_MOUSE DNA-binding protein RFX6 (Regulatory factor X 6) (Regulatory factor X domain-containing protein 1) 927 102,566 Alternative sequence (3); Chain (1); DNA binding (1); Erroneous initiation (2) FUNCTION: Transcription factor required to direct islet cell differentiation during endocrine pancreas development. Specifically required for the differentiation of 4 of the 5 islet cell types and for the production of insulin. Not required for pancreatic PP (polypeptide-producing) cells differentiation. Acts downstream of NEUROG3 and regulates the transcription factors involved in beta-cell maturation and function, thereby restricting the expression of the beta-cell differentiation and specification genes, and thus the beta-cell fate choice. Activates transcription by forming a heterodimer with RFX3 and binding to the X-box in the promoter of target genes (PubMed:20148032). Involved in glucose-stimulated insulin secretion by promoting insulin and L-type calcium channel gene transcription (By similarity). {ECO:0000250|UniProtKB:Q8HWS3, ECO:0000269|PubMed:20148032}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20148032}. SUBUNIT: Interacts with RFX3 (PubMed:20148032). {ECO:0000269|PubMed:20148032}. TISSUE SPECIFICITY: In the adult pancreas, expression is restricted to the islets where it could be detected in all endocrine lineages. {ECO:0000269|PubMed:20040487, ECO:0000269|PubMed:20148032}. +Q9DC04 RGS3_MOUSE Regulator of G-protein signaling 3 (RGS3) (C2PA) 966 106,219 Alternative sequence (7); Beta strand (5); Chain (1); Compositional bias (1); Domain (2); Helix (2); Modified residue (5); Sequence conflict (2) FUNCTION: Down-regulates signaling from heterotrimeric G-proteins by increasing the GTPase activity of the alpha subunits, thereby driving them into their inactive GDP-bound form. Down-regulates G-protein-mediated release of inositol phosphates and activation of MAP kinases. {ECO:0000269|PubMed:11301003, ECO:0000269|PubMed:12210723}. PTM: Phosphorylated by cyclic GMP-dependent protein kinase. {ECO:0000250}.; PTM: ISGylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Cell membrane {ECO:0000250|UniProtKB:P49796}; Peripheral membrane protein {ECO:0000250|UniProtKB:P49796}; Cytoplasmic side {ECO:0000250|UniProtKB:P49796}. Note=Long isoforms are cytoplasmic and associated with the plasma membrane. Short isoforms are nuclear. {ECO:0000250|UniProtKB:P49796}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm {ECO:0000269|PubMed:11301003}.; SUBCELLULAR LOCATION: Isoform 3: Nucleus {ECO:0000269|PubMed:12210723}.; SUBCELLULAR LOCATION: Isoform 4: Nucleus {ECO:0000305}. SUBUNIT: Binds the GNB1-GNG2 heterodimer (By similarity). Binds EFNB1 and EFNB2. {ECO:0000250}. TISSUE SPECIFICITY: Detected in embryos from E8.5-16.5 in cortical ventricular zone, dorsal root ganglia and cerebellar primordia. Isoform 3 is detected in testis and in spermatocytes from newborn mice. Levels increase and reach a maximum after 21 days; after this they decrease again. Long isoforms are widely expressed. {ECO:0000269|PubMed:11034339}. +O08850 RGS5_MOUSE Regulator of G-protein signaling 5 (RGS5) 181 21,086 Chain (1); Domain (1); Sequence conflict (2) FUNCTION: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds to G(i)-alpha and G(o)-alpha, but not to G(s)-alpha. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O15539}. Membrane {ECO:0000250|UniProtKB:O15539}. TISSUE SPECIFICITY: Expressed in heart and muscle. +Q9Z2H2 RGS6_MOUSE Regulator of G-protein signaling 6 (RGS6) 472 54,531 Chain (1); Domain (3) FUNCTION: Regulates G protein-coupled receptor signaling cascades. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. The RGS6/GNB5 dimer enhances GNAO1 GTPase activity. {ECO:0000250|UniProtKB:P49758}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15897264}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P49758}. Membrane {ECO:0000250|UniProtKB:P49758}; Peripheral membrane protein {ECO:0000250|UniProtKB:P49758}. Nucleus {ECO:0000250|UniProtKB:P49758}. Cell membrane {ECO:0000269|PubMed:15897264}. Note=Interaction with GNB5 mediates translocation to the nucleus. {ECO:0000250|UniProtKB:P49758}. SUBUNIT: Interacts with GNB5 (By similarity). Interacts with RGS7BP, leading to regulate the subcellular location of the heterodimer formed with GNB5 (PubMed:15632198, PubMed:15897264). Interacts with GNAI1 (By similarity). {ECO:0000250|UniProtKB:P49758, ECO:0000269|PubMed:15632198, ECO:0000269|PubMed:15897264}. DOMAIN: The RGS domain interacts avidly with Galpha and mediates the acceleration of Galpha-mediated GTP hydrolysis. {ECO:0000250}. +O54829 RGS7_MOUSE Regulator of G-protein signaling 7 (RGS7) 469 54,792 Chain (1); Domain (3); Modified residue (4); Sequence conflict (1) FUNCTION: Regulates G protein-coupled receptor signaling cascades. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. The RGS7/GNB5 dimer enhances GNAO1 GTPase activity. May play a role in synaptic vesicle exocytosis. Modulates the activity of potassium channels that are activated by GNAO1 in response to muscarinic acetylcholine receptor M2/CHRM2 signaling. {ECO:0000250|UniProtKB:P49802}. PTM: Palmitoylated. {ECO:0000250|UniProtKB:O46470}.; PTM: Ubiquitinated, leading to rapid proteasomal degradation. {ECO:0000250|UniProtKB:P49802}.; PTM: Phosphorylation and subsequent interaction with 14-3-3 proteins inhibits GAP activity. {ECO:0000250|UniProtKB:P49802}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P49802}. Cytoplasm {ECO:0000250|UniProtKB:P49802}. Cell membrane {ECO:0000250|UniProtKB:P49802}. Membrane {ECO:0000250|UniProtKB:P49802}; Peripheral membrane protein {ECO:0000250|UniProtKB:P49802}; Cytoplasmic side {ECO:0000250|UniProtKB:P49802}. Note=Interaction with PKD1 promotes location at the cell membrane. Interaction with RGS7BP promotes location at the cell membrane. {ECO:0000250|UniProtKB:P49802}. SUBUNIT: Interacts with PKD1; this prevents rapid proteasomal degradation. Interacts with GNB5 (By similarity). Interacts with RGS7BP, leading to regulate the subcellular location of the heterodimer formed with GNB5 (PubMed:15632198, PubMed:15897264). Interacts (phosphorylated form) with 14-3-3 protein YWHAQ (PubMed:10862767). Interacts with SNAPIN. Interacts with GNAI1 (By similarity). Interacts with GNAO1, GNAI3 and GNAZ (By similarity). {ECO:0000250|UniProtKB:P49802, ECO:0000250|UniProtKB:P49803, ECO:0000269|PubMed:10862767, ECO:0000269|PubMed:15632198, ECO:0000269|PubMed:15897264}. TISSUE SPECIFICITY: Detected in brain (at protein level). {ECO:0000269|PubMed:10862767}. +Q8BXT1 RGS8_MOUSE Regulator of G-protein signaling 8 (RGS8) 180 20,963 Chain (1); Domain (1); Modified residue (1) FUNCTION: Regulates G protein-coupled receptor signaling cascades, including signaling via muscarinic acetylcholine receptor CHRM2 and dopamine receptor DRD2. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. Modulates the activity of potassium channels that are activated in response to DRD2 and CHRM2 signaling. {ECO:0000250|UniProtKB:P49804}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P49804}; Peripheral membrane protein {ECO:0000250|UniProtKB:P49804}; Cytoplasmic side {ECO:0000250|UniProtKB:P49804}. Membrane {ECO:0000250|UniProtKB:P49804}; Peripheral membrane protein {ECO:0000250|UniProtKB:P49804}; Cytoplasmic side {ECO:0000250|UniProtKB:P49804}. Perikaryon {ECO:0000250|UniProtKB:P49804}. Cell projection, dendrite {ECO:0000250|UniProtKB:P49804}. Nucleus {ECO:0000250|UniProtKB:P49804}. Note=Detected in Purkinje cell soma and dendrites. Associated with Purkinje cell membranes. Not detected in Purkinje cell nuclei. Detected in the nucleus after heterologous expression. Recruited to the cell membrane in the presence of GNAO1. {ECO:0000250|UniProtKB:P49804}. SUBUNIT: Interacts with GNAO1 and GNAI3. {ECO:0000250|UniProtKB:P49804}. +Q8K3C0 RNK_MOUSE Ribonuclease kappa (RNase K) (RNase kappa) (EC 3.1.-.-) 98 10,992 Chain (1); Sequence conflict (1); Transmembrane (2) TRANSMEM 13 33 Helical. {ECO:0000255}.; TRANSMEM 65 85 Helical. {ECO:0000255}. FUNCTION: Endoribonuclease which preferentially cleaves ApU and ApG phosphodiester bonds. Hydrolyzes UpU bonds at a lower rate (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +A7RDN6 RNLS_MOUSE Renalase (EC 1.6.3.5) (Monoamine oxidase-C) (MAO-C) (mMAO-C) 342 37,597 Alternative sequence (1); Binding site (2); Chain (1); Erroneous termination (1); Region (1); Sequence conflict (5); Signal peptide (1) FUNCTION: Catalyzes the oxidation of the less abundant 1,2-dihydro-beta-NAD(P) and 1,6-dihydro-beta-NAD(P) to form beta-NAD(P)(+). The enzyme hormone is secreted by the kidney, and circulates in blood and modulates cardiac function and systemic blood pressure. Lowers blood pressure in vivo by decreasing cardiac contractility and heart rate and preventing a compensatory increase in peripheral vascular tone, suggesting a causal link to the increased plasma catecholamine and heightened cardiovascular risk. High concentrations of catecholamines activate plasma renalase and promotes its secretion and synthesis. {ECO:0000250|UniProtKB:Q5VYX0}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17846919}. TISSUE SPECIFICITY: Expressed predominantly in kidney and testis with lower levels in liver, heart and embryo and weak expression in brain and skeletal muscle. {ECO:0000269|PubMed:17846919}. +P06281 RENI1_MOUSE Renin-1 (EC 3.4.23.15) (Angiotensinogenase) (Kidney renin) 402 44,343 Active site (2); Beta strand (22); Chain (1); Disulfide bond (2); Domain (1); Glycosylation (3); Helix (8); Natural variant (5); Propeptide (1); Sequence conflict (3); Signal peptide (1); Turn (2) FUNCTION: Renin is a highly specific endopeptidase, whose only known function is to generate angiotensin I from angiotensinogen in the plasma, initiating a cascade of reactions that produce an elevation of blood pressure and increased sodium retention by the kidney. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Membrane {ECO:0000250}. Note=Associated to membranes via binding to ATP6AP2. {ECO:0000250}. SUBUNIT: Interacts with ATP6AP2. {ECO:0000250}. TISSUE SPECIFICITY: Kidney. +P00796 RENI2_MOUSE Renin-2 (EC 3.4.23.15) (Angiotensinogenase) (Submandibular gland renin) [Cleaved into: Renin-2 heavy chain; Renin-2 light chain] 401 44,283 Active site (2); Beta strand (23); Chain (3); Disulfide bond (3); Domain (1); Helix (11); Propeptide (1); Sequence conflict (4); Signal peptide (1); Turn (5) FUNCTION: Renin is a highly specific endopeptidase, related to pepsin, whose only known function is to generate angiotensin I from angiotensinogen in the plasma, initiating a cascade of reactions that produce an elevation of blood pressure and increased sodium retention by the kidney. Its function in the salivary gland is not understood. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Dimer of a heavy chain and a light chain joined by a disulfide bond. TISSUE SPECIFICITY: Submandibular gland. +Q9EPC5 RET7_MOUSE Retinoid-binding protein 7 (Cellular retinoic acid-binding protein 4) (CRABP4) (CRBP4) (Cellular retinoic acid-binding protein IV) (CRABP-IV) 134 15,428 Chain (1) FUNCTION: Intracellular transport of retinol. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. DOMAIN: Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in white adipose tissue and mammary gland. +Q8JZL7 RGF1B_MOUSE Ras-GEF domain-containing family member 1B (GPI gamma-4) 473 55,273 Alternative sequence (3); Chain (1); Domain (2); Frameshift (1); Sequence conflict (2) FUNCTION: Guanine nucleotide exchange factor (GEF) with specificity for RAP2A, it doesn't seems to activate other Ras family proteins (in vitro). {ECO:0000269|PubMed:20090772}. SUBCELLULAR LOCATION: Early endosome {ECO:0000269|PubMed:20090772}. Late endosome {ECO:0000269|PubMed:20090772}. Midbody {ECO:0000250}. Note=Localizes to midbody at telophase (By similarity). May shuttle between early and late endosomes. Does not colocalize with lysosomal markers. {ECO:0000250}. SUBUNIT: Interacts with CCDC124 during cytokinesis (By similarity). Interacts with Ras family proteins. {ECO:0000250, ECO:0000269|PubMed:20090772}. TISSUE SPECIFICITY: Constitutively expressed in brain, intestine and testis. Low constitutive expression, if any, in heart, lung, lymph nodes and thymus. Up-regulated in heart, kidney, liver, lymph nodes, spleen and thymus at day 20 after infection with Trypanosoma cruzi. Not detected in muscle. {ECO:0000269|PubMed:12488504}. +Q8K2P6 RFESD_MOUSE Rieske domain-containing protein 157 17,966 Alternative sequence (2); Beta strand (12); Chain (1); Domain (2); Helix (3); Metal binding (4); Modified residue (2); Turn (3) +Q9D0F6 RFC5_MOUSE Replication factor C subunit 5 (Activator 1 36 kDa subunit) (A1 36 kDa subunit) (Activator 1 subunit 5) (Replication factor C 36 kDa subunit) (RF-C 36 kDa subunit) (RFC36) 339 38,096 Chain (1); Nucleotide binding (1) FUNCTION: The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins proliferating cell nuclear antigen (PCNA) and activator 1. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Heterotetramer of subunits RFC2, RFC3, RFC4 and RFC5 that can form a complex either with RFC1 or with RAD17. The former interacts with PCNA in the presence of ATP, while the latter has ATPase activity but is not stimulated by PCNA (By similarity). {ECO:0000250}. +Q8R361 RFIP5_MOUSE Rab11 family-interacting protein 5 (Rab11-FIP5) (Rab11-interacting protein Rip11) 645 69,553 Chain (1); Compositional bias (1); Domain (2); Modified residue (13) FUNCTION: Rab effector involved in protein trafficking from apical recycling endosomes to the apical plasma membrane. Involved in insulin granule exocytosis. May regulate V-ATPase intracellular transport in response to extracellular acidosis. {ECO:0000269|PubMed:19335615}. PTM: Phosphorylated on serine and threonine residues. Phosphorylation at Ser-357 is PKA-dependent. {ECO:0000269|PubMed:19335615}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Recycling endosome membrane {ECO:0000269|PubMed:19335615}; Peripheral membrane protein {ECO:0000269|PubMed:19335615}. Early endosome membrane {ECO:0000269|PubMed:19335615}; Peripheral membrane protein {ECO:0000269|PubMed:19335615}. Golgi apparatus membrane {ECO:0000269|PubMed:19335615}; Peripheral membrane protein {ECO:0000269|PubMed:19335615}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000269|PubMed:19335615}; Peripheral membrane protein {ECO:0000269|PubMed:19335615}. Mitochondrion membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. SUBUNIT: Forms a heterooligomeric complex with RAB11FIP4. Binds NAPG and TROVE2. Binds RAB11A that has been activated by GTP binding (By similarity). {ECO:0000250}. DOMAIN: Binds to vesicles enriched in neutral phospholipids via its C2 domain. The interaction is favored by Mg(2+) rather than Ca(2+) (By similarity). {ECO:0000250}. +Q5SVD0 RFLB_MOUSE Refilin-B (Regulator of filamin protein B) (RefilinB) 216 23,380 Chain (1); Modified residue (2); Sequence conflict (1) FUNCTION: Involved in the regulation of the perinuclear actin network and nuclear shape through interaction with filamins. Plays an essential role in the formation of cartilaginous skeletal elements. {ECO:0000269|PubMed:21709252, ECO:0000269|PubMed:24436304}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:21709252, ECO:0000269|PubMed:24436304}. Note=Colocalizes with FLNA along actin bundle-like structures. {ECO:0000269|PubMed:24436304}. SUBUNIT: Interacts with FLNA and FLNB. {ECO:0000269|PubMed:21709252, ECO:0000269|PubMed:24436304}. TISSUE SPECIFICITY: Detected in various tissues, with highest expression in lung, followed by spleen. {ECO:0000269|PubMed:24436304}. +O09009 RFNG_MOUSE Beta-1,3-N-acetylglucosaminyltransferase radical fringe (EC 2.4.1.222) (O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase) 332 36,926 Active site (1); Binding site (2); Chain (1); Disulfide bond (3); Glycosylation (1); Metal binding (2); Topological domain (2); Transmembrane (1) TRANSMEM 7 29 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 30 332 Lumenal. {ECO:0000255}. FUNCTION: Glycosyltransferase that initiates the elongation of O-linked fucose residues attached to EGF-like repeats in the extracellular domain of Notch molecules. Modulates NOTCH1 activity by modifying O-fucose residues at specific EGF-like domains resulting in enhancement of NOTCH1 activation by DLL1 and JAG1 (PubMed:28089369). May be involved in limb formation and in neurogenesis (By similarity). {ECO:0000250|UniProtKB:O12972, ECO:0000250|UniProtKB:Q9R1U9, ECO:0000269|PubMed:28089369}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Detected in all the examined tissues (12.5 dpc). High expression found in adult brain. +Q91V81 RBM42_MOUSE RNA-binding protein 42 (RNA-binding motif protein 42) 474 49,875 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (1); Initiator methionine (1); Modified residue (6); Region (1); Sequence conflict (3) FUNCTION: Binds (via the RRM domain) to the 3'-untranslated region (UTR) of CDKN1A mRNA. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19170760}. Cytoplasm {ECO:0000269|PubMed:19170760}. Note=Upon stress response, localizes with HNRNPK in cytoplasmic aggregates of stalled translational preinitiation complexes called stress granules. SUBUNIT: Interacts with HNRNPK. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in cell lines (at protein level). Expressed in heart, brain, spleen, lung, liver, skeletal muscle, kidney and testis. {ECO:0000269|PubMed:19170760}. +Q3V089 RBM44_MOUSE RNA-binding protein 44 (RNA-binding motif protein 44) 1013 112,281 Chain (1); Domain (1); Modified residue (5) FUNCTION: Component of intercellular bridges during meiosis. Intercellular bridges are evolutionarily conserved structures that connect differentiating germ cells. Not required for fertility. {ECO:0000269|PubMed:21364893}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21364893}. Note=Detected in the intercellular bridges. Localization to intercellular bridges is identified in all stages of tubules but dynamically increases from stage I pachytene spermatocytes to stage XII secondary spermatocytes and disappears after the formation of step 1 round spermatids (stage I). In addition, it is localized in the cytoplasm in pachytene spermatocytes to secondary spermatocytes. The cytoplasmic signals also increases dramatically in stages X-XII, decreases from step 1 to step 3 spermatids, and disappears in step 4 spermatids. SUBUNIT: Homodimer. Interacts with TEX14. {ECO:0000269|PubMed:21364893}. TISSUE SPECIFICITY: Highly expressed in testis. Also expressed in other tissues at lower level. {ECO:0000269|PubMed:21364893}. +Q99NF8 RBP17_MOUSE Ran-binding protein 17 1088 124,054 Chain (1); Initiator methionine (1); Modified residue (2); Sequence conflict (2) FUNCTION: May function as a nuclear transport receptor. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250}. SUBUNIT: Binds to nucleoporins and the GTP-bound form of Ran. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in primary spermatocytes and very weakly in pancreas. {ECO:0000269|PubMed:11071879}. +Q99KG3 RBM10_MOUSE RNA-binding protein 10 (RNA-binding motif protein 10) 930 103,494 Alternative sequence (2); Chain (1); Compositional bias (2); Domain (3); Erroneous initiation (1); Modified residue (12); Sequence conflict (3); Zinc finger (2) FUNCTION: Not known. Binds to RNA homopolymers, with a preference for poly(G) and poly(U) and little for poly(A) (By similarity). May bind to specific miRNA hairpins (By similarity). {ECO:0000250|UniProtKB:P70501, ECO:0000250|UniProtKB:P98175}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Associates with the spliceosome. Component of a large chromatin remodeling complex, at least composed of MYSM1, PCAF, RBM10 and KIF11/TRIP5 (By similarity). {ECO:0000250}. +Q924W9 RBTN1_MOUSE Rhombotin-1 (Cysteine-rich protein TTG-1) (LIM domain only protein 1) (LMO-1) (T-cell translocation protein 1) 156 17,805 Chain (1); Domain (2) FUNCTION: May be involved in gene regulation within neural lineage cells potentially by direct DNA binding or by binding to other transcription factors. {ECO:0000269|PubMed:1703797}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:1703797}. TISSUE SPECIFICITY: Expressed in the brain and not in the thymus. {ECO:0000269|PubMed:1703797}. +P62878 RBX1_MOUSE E3 ubiquitin-protein ligase RBX1 (EC 2.3.2.27) (EC 2.3.2.32) (E3 ubiquitin-protein transferase RBX1) (RING finger protein 75) (RING-box protein 1) (Rbx1) [Cleaved into: E3 ubiquitin-protein ligase RBX1, N-terminally processed] 108 12,274 Chain (2); Initiator methionine (1); Metal binding (11); Modified residue (3); Sequence conflict (1); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins, including proteins involved in cell cycle progression, signal transduction, transcription and transcription-coupled nucleotide excision repair (PubMed:22118460). CRLs complexes and ARIH1 collaborate in tandem to mediate ubiquitination of target proteins, ARIH1 mediating addition of the first ubiquitin on CRLs targets (By similarity). The functional specificity of the E3 ubiquitin-protein ligase complexes depends on the variable substrate recognition components (By similarity). As a component of the CSA complex promotes the ubiquitination of ERCC6 resulting in proteasomal degradation (By similarity). Through the RING-type zinc finger, seems to recruit the E2 ubiquitination enzyme, like CDC34, to the complex and brings it into close proximity to the substrate (By similarity). Probably also stimulates CDC34 autoubiquitination (By similarity). May be required for histone H3 and histone H4 ubiquitination in response to ultraviolet and for subsequent DNA repair (By similarity). Promotes the neddylation of CUL1, CUL2, CUL4 and CUL4 via its interaction with UBE2M (By similarity). Involved in the ubiquitination of KEAP1, ENC1 and KLHL41 (By similarity). In concert with ATF2 and CUL3, promotes degradation of KAT5 thereby attenuating its ability to acetylate and activate ATM (By similarity). {ECO:0000250|UniProtKB:P62877, ECO:0000269|PubMed:22118460}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P62877}. Nucleus {ECO:0000250|UniProtKB:P62877}. SUBUNIT: Interacts with COPS6. Component of the DCX DET1-COP1 ubiquitin ligase complex at least composed of RBX1, DET1, DDB1, CUL4A and COP1. Part of an E3 ligase complex composed of RBX1, DDB1, DDB2 and CUL4A or CUL4B (PubMed:22118460). Interacts with CAND1 (PubMed:22118460). Interacts with UBE2M (By similarity). Part of a SCF complex consisting of CUL1, RBX1, SKP1 and SKP2. Part of a SCF-like complex consisting of CUL7, RBX1, SKP1 and FBXW8. Part of CBC(VHL) complexes with elongin BC complex (ELOB and ELOC), CUL2 or CUL5 and VHL. Part of the CSA complex (DCX(ERCC8) complex), a DCX E3 ubiquitin-protein ligase complex containing ERCC8, RBX1, DDB1 and CUL4A; the CSA complex interacts with RNA polymerase II; upon UV irradiation it interacts with the COP9 signalosome and preferentially with the hyperphosphorylated form of RNA polymerase II (By similarity). Part of multisubunit E3 ubiquitin ligase complexes with elongin BC complex (ELOB and ELOC), CUL2 and MED8; elongin BC complex (ELOB and ELOC), CUL5 and MUF1. Part of multisubunit complexes with elongin BC complex (ELOB and ELOC), elongin A/ELOA or SOCS1 or WSB1 and CUL5. Interacts directly with CUL1 and probably also with CUL2, CUL3, CUL4A, CUL4B, CUL5 and CUL7. Interacts with CDC34. Interacts with GLMN. GLMN competes for the binding site of the E2 ubiquitin-conjugating enzyme CDC34 and disrupts CDC34 binding. Part of a SCF complex consisting of CUL1, RBX1, SKP1 and FBXO2. Part of a SCF complex consisting of CUL1, FBXO3, RBX1 and SKP1; this complex interacts with PML via FBXO3. Component of the SCF(Cyclin F) complex consisting of CUL1, RBX1, SKP1 and CCNF. Identified in a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex together with HINT1 and CDC34 (By similarity). Component of multiple BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes formed of CUL3, RBX1 and a variable BTB domain-containing protein. Part of the BCR(ENC1) complex containing ENC1. Part of the BCR(GAN) complex containing GAN. Part of the BCR(KLHL41) complex containing KLHL41. Part of the BCR(KEAP1) complex containing KEAP1 (By similarity). Interacts with DCUN1D3 (By similarity). Interacts with SESN1 and SESN2 (By similarity). Interacts with NOTCH2 (By similarity). Component of the BCR(KLHL22) E3 ubiquitin ligase complex, at least composed of CUL3, KLHL22 and RBX1 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P62877, ECO:0000269|PubMed:22118460}. DOMAIN: The RING-type zinc finger domain is essential for ubiquitin ligase activity (By similarity). It coordinates an additional third zinc ion (PubMed:22118460). {ECO:0000250|UniProtKB:P62877, ECO:0000269|PubMed:22118460}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10643962}. +A2AU37 RD21L_MOUSE Double-strand-break repair protein rad21-like protein 1 552 62,670 Chain (1); Compositional bias (1); Erroneous gene model prediction (1) FUNCTION: Meiosis-specific component of some cohesin complex required during the initial steps of prophase I in male meiosis. Probably required during early meiosis in males for separation of sister chromatids and homologous chromosomes. Replaces RAD21 in premeiotic S phase (during early stages of prophase I), while RAD21 reappears in later stages of prophase I. Involved in synaptonemal complex assembly, synapsis initiation and crossover recombination between homologous chromosomes during prophase I. Not required for meiosis in females in young mice, while it is required later as mice age. {ECO:0000269|PubMed:21242291, ECO:0000269|PubMed:21274006, ECO:0000269|PubMed:21527826, ECO:0000269|PubMed:21743440, ECO:0000269|PubMed:22711701}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21242291, ECO:0000269|PubMed:21274006, ECO:0000269|PubMed:21527826, ECO:0000269|PubMed:21743440}. Chromosome {ECO:0000269|PubMed:21242291, ECO:0000269|PubMed:21274006, ECO:0000269|PubMed:21527826, ECO:0000269|PubMed:21743440}. Note=In meiotic chromosomes, localized along axial elements in early meiosis: detectable on the axial elements in leptotene, and stays on the axial/lateral elements until mid pachytene. It then disappears and is replaced with RAD21. Compared to REC8, has mutually exclusive loading sites on the chromosomes: REC8 and RAD21L form distinct cohesin-enriched domains along the axial elements. {ECO:0000269|PubMed:21242291, ECO:0000269|PubMed:21274006, ECO:0000269|PubMed:21743440}. SUBUNIT: Component of some meiotic cohesin complex composed of the SMC1 (SMC1A or SMC1B) and SMC3 heterodimer attached via their hinge domain, RAD21L which link them, and STAG3. {ECO:0000269|PubMed:21242291, ECO:0000269|PubMed:21274006, ECO:0000269|PubMed:21527826}. TISSUE SPECIFICITY: Specifically expressed in male and female gonads (at protein level). {ECO:0000269|PubMed:21242291, ECO:0000269|PubMed:21274006, ECO:0000269|PubMed:21527826}. +Q8VE37 RCC1_MOUSE Regulator of chromosome condensation (Chromosome condensation protein 1) 421 44,931 Chain (1); Initiator methionine (1); Modified residue (3); Motif (1); Repeat (7); Sequence conflict (1) FUNCTION: Guanine-nucleotide releasing factor that promotes the exchange of Ran-bound GDP by GTP, and thereby plays an important role in RAN-mediated functions in nuclear import and mitosis. Contributes to the generation of high levels of chromosome-associated, GTP-bound RAN, which is important for mitotic spindle assembly and normal progress through mitosis. Via its role in maintaining high levels of GTP-bound RAN in the nucleus, contributes to the release of cargo proteins from importins after nuclear import. Involved in the regulation of onset of chromosome condensation in the S phase. Binds both to the nucleosomes and double-stranded DNA. {ECO:0000250|UniProtKB:P18754}. PTM: N-terminal methylation by METTL11A/NTM1 is required for binding double-stranded DNA and stable chromatin association. Dimethylation produces a permanent positive charge on the amino group, which facilitates electrostatic binding to the phosphate groups on DNA, while inhibiting histone-binding. Methylated tail helps retain RCC1 on chromosomes during nucleotide exchange on Ran. {ECO:0000250|UniProtKB:P18754}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P18754}. Chromosome {ECO:0000250|UniProtKB:P18754}. Cytoplasm {ECO:0000250|UniProtKB:P18754}. Note=Predominantly nuclear in interphase cells. Binds to mitotic chromosomes. {ECO:0000250|UniProtKB:P18754}. SUBUNIT: Interacts with RAN. Interacts (via N-terminus and RCC1 repeats) with KPNA4. Interacts with ARRB2; the interaction is detected in the nucleus upon OR1D2 stimulation. {ECO:0000250|UniProtKB:P18754}. +Q8BRE0 RD3_MOUSE Protein RD3 195 22,669 Chain (1); Coiled coil (1); Compositional bias (1); Erroneous initiation (1); Frameshift (1) TISSUE SPECIFICITY: Expressed in the retina and in particular in the inner nuclear layer, in the outer nuclear layer and in the ganglion cell layer. {ECO:0000269|PubMed:12914764}. +Q8C5S7 REC8_MOUSE Meiotic recombination protein REC8 homolog (Cohesin Rec8p) 591 67,425 Chain (1); Modified residue (3); Sequence conflict (1) FUNCTION: Required during meiosis for separation of sister chromatids and homologous chromosomes. Proteolytic cleavage of REC8 on chromosome arms by separin during anaphase I allows for homologous chromosome separation in meiosis I and cleavage of REC8 on centromeres during anaphase II allows for sister chromatid separation in meiosis II. {ECO:0000269|PubMed:12034751, ECO:0000269|PubMed:15515002, ECO:0000269|PubMed:15935783, ECO:0000269|PubMed:16855401}. PTM: Phosphorylated. {ECO:0000269|PubMed:12759374, ECO:0000269|PubMed:22346761}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12034751, ECO:0000269|PubMed:12759374, ECO:0000269|PubMed:16855401, ECO:0000269|PubMed:22346761}. Chromosome {ECO:0000269|PubMed:12034751, ECO:0000269|PubMed:12759374, ECO:0000269|PubMed:16855401, ECO:0000269|PubMed:22346761}. Chromosome, centromere {ECO:0000269|PubMed:12034751, ECO:0000269|PubMed:12759374, ECO:0000269|PubMed:16855401, ECO:0000269|PubMed:22346761}. Note=In meiotic chromosomes, localized along axial elements in prophase from the leptotene to diplotene stages. At later prophase stages, diakinesis and metaphase I, localized along interstitial axes of chromosomes including both centromere and arm regions. No longer detected in arm regions in anaphase I but persists on centromere regions until metaphase II. {ECO:0000269|PubMed:12034751, ECO:0000269|PubMed:12759374, ECO:0000269|PubMed:16855401, ECO:0000269|PubMed:22346761}. SUBUNIT: Interacts (phosphorylated and unphosphorylated form) with SMC3. Interacts with SYCP3. Interacts (phosphorylated and unphosphorylated form) with SMC1B. Does not interact with SMC1A. Interacts with RAD51. {ECO:0000269|PubMed:12759374}. TISSUE SPECIFICITY: Expressed primarily in the gonads. In the testis, expressed in pachytene spermatocytes and in spermatids. Not expressed in spermatogonia or somatic cells. In the ovary, expressed only in oocytes. Low levels also detected in a number of somatic tissues including thymus, lung, liver, kidney and small intestine. {ECO:0000269|PubMed:10207075, ECO:0000269|PubMed:12130806, ECO:0000269|PubMed:12759374, ECO:0000269|PubMed:15935783}. +Q60841 RELN_MOUSE Reelin (EC 3.4.21.-) (Reeler protein) 3461 387,495 Alternative sequence (2); Beta strand (93); Chain (1); Compositional bias (1); Disulfide bond (34); Domain (9); Erroneous initiation (1); Glycosylation (20); Helix (12); Metal binding (7); Mutagenesis (3); Repeat (16); Sequence conflict (13); Signal peptide (1); Turn (7) FUNCTION: Extracellular matrix serine protease that plays a role in layering of neurons in the cerebral cortex and cerebellum. Regulates microtubule function in neurons and neuronal migration. Affects migration of sympathetic preganglionic neurons in the spinal cord, where it seems to act as a barrier to neuronal migration. Enzymatic activity is important for the modulation of cell adhesion. Binding to the extracellular domains of lipoprotein receptors VLDLR and LRP8/APOER2 induces tyrosine phosphorylation of DAB1 and modulation of TAU phosphorylation. {ECO:0000269|PubMed:10880573}. PTM: N-glycosylated and to a lesser extent also O-glycosylated. {ECO:0000269|PubMed:17548821}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SUBUNIT: Oligomer of disulfide-linked homodimers. Binds to the ectodomains of VLDLR and LRP8/APOER2. {ECO:0000269|PubMed:16858396, ECO:0000269|PubMed:17548821, ECO:0000269|PubMed:21844191}. DOMAIN: The basic C-terminal region is essential for secretion. TISSUE SPECIFICITY: The major isoform 1 is neuron-specific. It is abundantly produced during brain ontogenesis by the Cajal-Retzius cells and other pioneer neurons located in the telencephalic marginal zone and by granule cells of the external granular layer of the cerebellum. Expression is located in deeper layers in the developing hippocampus and olfactory bulb, low levels of expression are also detected in the immature striatum. At early developmental stages, expressed also in hypothalamic differentiation fields, tectum and spinal cord. A moderate to low level of expression occurs in the septal area, striatal fields, habenular nuclei, some thalamic nuclei, particularly the lateral geniculate, the retina and some nuclei of the reticular formation in the central field of the medulla. Very low levels found in liver and kidney. No expression in radial glial cells, cortical plate, Purkinje cells and inferior olivary neurons. The minor isoform 2 is only expressed in non neuronal cells. The minor isoform 3 is found in the same cells as isoform 1, but is almost undetectable in retina and brain stem. {ECO:0000269|PubMed:10328932, ECO:0000269|PubMed:9182958}. DISEASE: Note=Defects in Reln are the cause of the autosomal recessive reeler (rl) phenotype which is characterized by impaired motor coordination, tremors and ataxia. Neurons in affected mice fail to reach their correct locations in the developing brain, disrupting the organization of the cerebellar and cerebral cortices and other laminated regions. {ECO:0000269|PubMed:7715726}. +Q08652 RET2_MOUSE Retinol-binding protein 2 (Cellular retinol-binding protein II) (CRBP-II) 134 15,610 Binding site (2); Chain (1); Sequence conflict (1) FUNCTION: Intracellular transport of retinol. SUBCELLULAR LOCATION: Cytoplasm. DOMAIN: Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in prenatal liver, intestine and lung, and in adult intestine. +P49194 RET3_MOUSE Retinol-binding protein 3 (Interphotoreceptor retinoid-binding protein) (IRBP) (Interstitial retinol-binding protein) 1234 134,451 Chain (1); Glycosylation (3); Region (1); Repeat (4); Sequence conflict (4); Signal peptide (1) FUNCTION: IRBP shuttles 11-cis and all trans retinoids between the retinol isomerase in the pigment epithelium and the visual pigments in the photoreceptor cells of the retina. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, interphotoreceptor matrix. Note=Interphotoreceptor matrix that permeates the space between the retina and the contiguous layer of pigment epithelium cells. TISSUE SPECIFICITY: Expressed in the photosensitive tissues; retina and pineal gland. {ECO:0000269|PubMed:1342928}. +Q8K126 RF1M_MOUSE Peptide chain release factor 1, mitochondrial (MRF-1) (MtRF-1) 446 52,458 Chain (1); Modified residue (1); Transit peptide (1) FUNCTION: Mitochondrial peptide chain release factor that directs the termination of translation in response to the peptide chain non-cognate termination stop codons AGG and AGA. {ECO:0000250}. PTM: Methylation of glutamine in the GGQ triplet is conserved from bacteria to mammals. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion. +Q6NS82 RETR2_MOUSE Reticulophagy regulator 2 541 57,542 Alternative sequence (2); Chain (1); Compositional bias (4); Frameshift (1); Modified residue (9); Motif (1); Sequence conflict (3); Transmembrane (3) TRANSMEM 10 30 Helical. {ECO:0000255}.; TRANSMEM 87 107 Helical. {ECO:0000255}.; TRANSMEM 199 219 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Interacts with ATG8 family modifier proteins MAP1LC3A, MAP1LC3B, GABARAP and GABARAPL1. {ECO:0000250|UniProtKB:Q8NC44}. DOMAIN: The LIR motif interacts with ATG8 family proteins. {ECO:0000250|UniProtKB:Q8NC44}. TISSUE SPECIFICITY: Mainly expressed in the central nervous system and in parenchymatous organs including liver, lung and kidney. {ECO:0000269|PubMed:19838196}. +Q8K2X2 RBM48_MOUSE RNA-binding protein 48 371 41,633 Alternative sequence (1); Chain (1); Domain (1); Sequence conflict (1) +Q5SFM8 RBM27_MOUSE RNA-binding protein 27 (Peri-implantation stem cell protein 1) (RNA-binding motif protein 27) 1060 118,552 Alternative sequence (2); Chain (1); Coiled coil (1); Compositional bias (2); Domain (1); Erroneous initiation (1); Frameshift (2); Modified residue (5); Sequence conflict (3); Zinc finger (1) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15741184}. Nucleus speckle {ECO:0000269|PubMed:15741184}. Note=Incorporated into the nuclear speckles and to speckles proximal to the nuclear periphery. Also localizes to punctate structures in the cytoplasm termed cytospeckles. DOMAIN: The RRM domain mediates integration into cytospeckles. +Q8CGC6 RBM28_MOUSE RNA-binding protein 28 (RNA-binding motif protein 28) 750 84,214 Beta strand (6); Chain (1); Compositional bias (1); Cross-link (1); Domain (4); Helix (2); Initiator methionine (1); Modified residue (5); Sequence conflict (9); Turn (1) FUNCTION: Nucleolar component of the spliceosomal ribonucleoprotein complexes. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. SUBUNIT: Interacts with U1, U2, U4, U5, and U6 spliceosomal small nuclear RNAs (snRNAs). {ECO:0000250}. +Q9CXK9 RBM33_MOUSE RNA-binding protein 33 (Proline-rich protein 8) (RNA-binding motif protein 33) 1231 137,325 Alternative sequence (2); Chain (1); Coiled coil (1); Compositional bias (4); Cross-link (1); Initiator methionine (1); Modified residue (11); Sequence conflict (1) +P12970 RL7A_MOUSE 60S ribosomal protein L7a (Surfeit locus protein 3) 266 29,977 Chain (1); Cross-link (7); Erroneous initiation (1); Modified residue (3) SUBUNIT: Interacts with CRY1 (PubMed:19129230). Interacts with DICER1, AGO2, TARBP2, MOV10 and EIF6; they form a large RNA-induced silencing complex (RISC) (By similarity). {ECO:0000250|UniProtKB:P62424, ECO:0000269|PubMed:19129230}. +Q80YT9 RBM11_MOUSE Splicing regulator RBM11 (RNA-binding motif protein 11) 238 26,945 Chain (1); Domain (1); Erroneous initiation (1); Motif (1) FUNCTION: Tissue-specific splicing factor with potential implication in the regulation of alternative splicing during neuron and germ cell differentiation. Antagonizes SRSF1-mediated BCL-X splicing. May affect the choice of alternative 5' splice sites by binding to specific sequences in exons and antagonizing the SR protein SRSF1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}. Nucleus speckle {ECO:0000250}. Note=Enriched in SRSF2-containing splicing speckles; shuttles between nucleoplasm and speckles. {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Selectively expressed in brain, cerebellum and testis, and to a lower extent in kidney. {ECO:0000269|PubMed:21984414}. +Q9CYF5 RCC1L_MOUSE RCC1-like G exchanging factor-like protein (RCC1-like) (Williams-Beuren syndrome chromosomal region 16 protein homolog) 461 49,995 Chain (1); Repeat (7); Transit peptide (1) FUNCTION: Guanine nucleotide exchange factor (GEF) for mitochondrial dynamin-related GTPase OPA1. Activates OPA1, by exchanging bound GDP for free GTP, and drives OPA1 and MFN1-dependent mitochondrial fusion (PubMed:28746876). Plays an essential role in mitochondrial ribosome biogenesis. As a component of a functional protein-RNA module, consisting of RCC1L, NGRN, RPUSD3, RPUSD4, TRUB2, FASTKD2 and 16S mitochondrial ribosomal RNA (16S mt-rRNA), controls 16S mt-rRNA abundance and is required for intra-mitochondrial translation of core subunits of the oxidative phosphorylation system (By similarity). {ECO:0000250|UniProtKB:Q96I51, ECO:0000269|PubMed:28746876}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:28746876}. SUBUNIT: Forms a regulatory protein-RNA complex, consisting of RCC1L, NGRN, RPUSD3, RPUSD4, TRUB2, FASTKD2 and 16S mt-rRNA. Interacts with 16S mt-rRNA; this interaction is direct (By similarity). Interacts with OPA1; this interaction is direct (PubMed:28746876). {ECO:0000250|UniProtKB:Q96I51, ECO:0000269|PubMed:28746876}. DOMAIN: The RCC1-like repeats assemble into a circular seven-bladed beta propeller structure. Each blade is composed of four antiparallel beta-strands with loops between each strand. {ECO:0000250|UniProtKB:Q96I51}. TISSUE SPECIFICITY: At E8.5, broadly expressed in yolk sac placenta, decidua, and embryo, with highest levels found in the trophoblast giant cells (TGCs) and ectoplacental cone (at protein level). {ECO:0000269|PubMed:28746876}. +Q9ERI6 RDH14_MOUSE Retinol dehydrogenase 14 (EC 1.1.1.300) (Alcohol dehydrogenase PAN2) 334 36,366 Active site (1); Binding site (1); Chain (1); Nucleotide binding (1) FUNCTION: Retinol dehydrogenase with a clear preference for NADP. Displays high activity towards 9-cis, 11-cis and all-trans-retinol. Shows a very weak activity towards 13-cis-retinol. Has no activity towards steroids. {ECO:0000269|PubMed:12226107}. +Q80TZ9 RERE_MOUSE Arginine-glutamic acid dipeptide repeats protein (Atrophin-2) 1558 171,755 Chain (1); Coiled coil (1); Compositional bias (5); Cross-link (2); Domain (3); Modified residue (20); Sequence conflict (2); Zinc finger (1) FUNCTION: Plays a role as a transcriptional repressor during development. May play a role in the control of cell survival. {ECO:0000269|PubMed:14645126}. SUBCELLULAR LOCATION: Nucleus, PML body {ECO:0000250}. Note=Localized in nuclear bodies of variables size. Colocalized with PML and BAX in nuclear PODs (By similarity). {ECO:0000250}. SUBUNIT: Interacts with HDAC1 and ATN1. Interaction with ATN1 is improved when the poly-Gln region of ATN1 is extended. Interacts with FAT1 (By similarity). {ECO:0000250}. DOMAIN: The interaction with ATN1 is mediated by the coiled domain. {ECO:0000250}. +P47939 RES18_MOUSE Regulated endocrine-specific protein 18 175 19,485 Chain (1); Signal peptide (1) FUNCTION: May play an important regulatory role in corticotrophs. SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:7988462}. Golgi apparatus {ECO:0000250|UniProtKB:P47940}. Cytoplasmic vesicle, secretory vesicle lumen {ECO:0000250|UniProtKB:P47940}. Note=Found in the lumen of secretory vesicles (dense core vesicles, DCV) (By similarity). However, seems to be retained intracellularly and not secreted (PubMed:7988462). {ECO:0000250|UniProtKB:P47940, ECO:0000269|PubMed:7988462}. TISSUE SPECIFICITY: Pituitary, hypothalamus and pancreas. Highest levels are found in somatotrophes, mammotrophes, and gonadotrophes, and lower levels are found in corticotrophs and thyrotropes. {ECO:0000269|PubMed:17951542}. +Q9CQ71 RFA3_MOUSE Replication protein A 14 kDa subunit (RP-A p14) (Replication factor A protein 3) (RF-A protein 3) 121 13,584 Chain (1); Cross-link (2) FUNCTION: As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates, that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage. In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation. Through recruitment of ATRIP activates the ATR kinase a master regulator of the DNA damage response. It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin, in response to DNA damage. Also recruits to sites of DNA damage proteins like XPA and XPG that are involved in nucleotide excision repair and is required for this mechanism of DNA repair. Plays also a role in base excision repair (BER), probably through interaction with UNG. Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. May also play a role in telomere maintenance. RPA3 has its own single-stranded DNA-binding activity and may be responsible for polarity of the binding of the complex to DNA. {ECO:0000250|UniProtKB:P35244}. PTM: Ubiquitinated by RFWD3 at stalled replication forks in response to DNA damage: ubiquitination by RFWD3 does not lead to degradation by the proteasome and promotes removal of the RPA complex from stalled replication forks, promoting homologous recombination. {ECO:0000250|UniProtKB:P35244}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the canonical replication protein A complex (RPA), a heterotrimer composed of RPA1, RPA2 and RPA3. Also component of the aRPA, the alternative replication protein A complex, a trimeric complex similar to the replication protein A complex/RPA but where RPA1 and RPA3 are associated with RPA4 instead of RPA2 (By similarity). {ECO:0000250}. +D3YU81 RFX8_MOUSE DNA-binding protein RFX8 (Regulatory factor X 8) 596 67,285 Chain (1); Compositional bias (2); DNA binding (1) FUNCTION: May be a transcription factor. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00858}. +Q6A0D4 RFTN1_MOUSE Raftlin (Raft-linking protein) 554 61,537 Chain (1); Erroneous initiation (2); Initiator methionine (1); Lipidation (2); Modified residue (4); Sequence conflict (3) FUNCTION: Involved in protein trafficking via association with clathrin and AP2 complex (By similarity). Upon bacterial lipopolysaccharide stimulation, mediates internalization of TLR4 to endosomes in dendritic cells and macrophages, and internalization of poly(I:C) to TLR3-positive endosomes in myeloid dendritic cells and epithelial cells; resulting in activation of TICAM1-mediated signaling and subsequent IFNB1 production (PubMed:27022195). Involved in T-cell antigen receptor-mediated signaling by regulating tyrosine kinase LCK localization, T-cell dependent antibody production and cytokine secretion (PubMed:19414744). May regulate B-cell antigen receptor-mediated signaling (By similarity). May play a pivotal role in the formation and/or maintenance of lipid rafts (By similarity). {ECO:0000250|UniProtKB:Q14699, ECO:0000269|PubMed:19414744, ECO:0000269|PubMed:27022195}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19414744}; Lipid-anchor {ECO:0000250|UniProtKB:Q14699}. Cytoplasm {ECO:0000250|UniProtKB:Q14699}. Membrane raft {ECO:0000250|UniProtKB:Q14699}. Endosome {ECO:0000250|UniProtKB:Q14699}. Early endosome {ECO:0000250|UniProtKB:Q14699}. Note=Translocates from cytoplasm to cell membrane where it colocalizes with poly (I:C) and then moves to endosomes where it colocalizes with TLR3. Translocates from cytoplasm to cell membrane where it colocalizes with TLR4 and then together with TLR4 moves to endosomes, upon lipopolysaccharide stimulation (PubMed:27022195). {ECO:0000250|UniProtKB:Q14699}. SUBUNIT: Interacts with TLR4; the interaction occurs in response to lipopolysaccharide stimulation. Interacts with CLTC; the interaction occurs in response to pathogens. Interacts with AP2A1 and AP2B1. {ECO:0000250|UniProtKB:Q14699}. TISSUE SPECIFICITY: Expressed in T-cells, B-cells, thymus and spleen (at protein level) (PubMed:19414744, PubMed:12805216). Expressed in dendritic cells, macrophages, heart, lung and small intestine (PubMed:19414744). {ECO:0000269|PubMed:12805216, ECO:0000269|PubMed:19414744}. +P47911 RL6_MOUSE 60S ribosomal protein L6 (TAX-responsive enhancer element-binding protein 107) (TAXREB107) 296 33,510 Chain (1); Cross-link (1); Erroneous initiation (1); Modified residue (4); Sequence conflict (3) FUNCTION: Component of the large ribosomal subunit. {ECO:0000250|UniProtKB:Q02878}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q02878}. Cytoplasm {ECO:0000250|UniProtKB:Q02878}. Rough endoplasmic reticulum {ECO:0000250|UniProtKB:Q2YGT9}. Note=Detected on cytosolic polysomes (By similarity). Detected in ribosomes that are associated with the rough endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:Q02878, ECO:0000250|UniProtKB:Q2YGT9}. SUBUNIT: Component of the large ribosomal subunit (By similarity). May bind IPO9 with low affinity (PubMed:11823430). {ECO:0000250|UniProtKB:Q02878, ECO:0000269|PubMed:11823430}. +Q99J08 S14L2_MOUSE SEC14-like protein 2 (Alpha-tocopherol-associated protein) (TAP) 403 46,300 Chain (1); Domain (2); Modified residue (5) FUNCTION: Carrier protein. Binds to some hydrophobic molecules and promotes their transfer between the different cellular sites. Binds with high affinity to alpha-tocopherol. Also binds with a weaker affinity to other tocopherols and to tocotrienols. May have a transcriptional activatory activity via its association with alpha-tocopherol. Probably recognizes and binds some squalene structure, suggesting that it may regulate cholesterol biosynthesis by increasing the transfer of squalene to a metabolic active pool in the cell (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Cytoplasmic in absence of alpha-tocopherol, and nuclear in presence of alpha-tocopherol. {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. +Q91W98 S15A4_MOUSE Solute carrier family 15 member 4 (Peptide transporter 4) (Peptide/histidine transporter 1) 574 62,256 Chain (1); Frameshift (1); Modified residue (2); Sequence conflict (9); Transmembrane (12) TRANSMEM 42 62 Helical. {ECO:0000255}.; TRANSMEM 69 89 Helical. {ECO:0000255}.; TRANSMEM 98 118 Helical. {ECO:0000255}.; TRANSMEM 161 181 Helical. {ECO:0000255}.; TRANSMEM 197 217 Helical. {ECO:0000255}.; TRANSMEM 225 245 Helical. {ECO:0000255}.; TRANSMEM 319 339 Helical. {ECO:0000255}.; TRANSMEM 364 384 Helical. {ECO:0000255}.; TRANSMEM 406 426 Helical. {ECO:0000255}.; TRANSMEM 460 480 Helical. {ECO:0000255}.; TRANSMEM 491 511 Helical. {ECO:0000255}.; TRANSMEM 536 556 Helical. {ECO:0000255}. FUNCTION: Proton oligopeptide cotransporter. Transports free histidine and certain di- and tripeptides (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8CBB2 S15A5_MOUSE Solute carrier family 15 member 5 566 62,622 Alternative sequence (1); Chain (1); Transmembrane (11) TRANSMEM 73 93 Helical. {ECO:0000255}.; TRANSMEM 103 123 Helical. {ECO:0000255}.; TRANSMEM 146 166 Helical. {ECO:0000255}.; TRANSMEM 184 204 Helical. {ECO:0000255}.; TRANSMEM 213 233 Helical. {ECO:0000255}.; TRANSMEM 299 319 Helical. {ECO:0000255}.; TRANSMEM 339 359 Helical. {ECO:0000255}.; TRANSMEM 379 399 Helical. {ECO:0000255}.; TRANSMEM 413 433 Helical. {ECO:0000255}.; TRANSMEM 453 473 Helical. {ECO:0000255}.; TRANSMEM 493 513 Helical. {ECO:0000255}. FUNCTION: Proton oligopeptide cotransporter. {ECO:0000305}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +D3Z5L6 S18B1_MOUSE MFS-type transporter SLC18B1 (Solute carrier family 18 member B1) 459 49,009 Chain (1); Modified residue (2); Topological domain (13); Transmembrane (12) TRANSMEM 34 54 Helical. {ECO:0000255}.; TRANSMEM 71 91 Helical. {ECO:0000255}.; TRANSMEM 101 121 Helical. {ECO:0000255}.; TRANSMEM 128 148 Helical. {ECO:0000255}.; TRANSMEM 168 188 Helical. {ECO:0000255}.; TRANSMEM 196 216 Helical. {ECO:0000255}.; TRANSMEM 236 256 Helical. {ECO:0000255}.; TRANSMEM 275 295 Helical. {ECO:0000255}.; TRANSMEM 307 327 Helical. {ECO:0000255}.; TRANSMEM 334 354 Helical. {ECO:0000255}.; TRANSMEM 380 400 Helical. {ECO:0000255}.; TRANSMEM 410 430 Helical. {ECO:0000255}. TOPO_DOM 1 33 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 55 70 Extracellular. {ECO:0000255}.; TOPO_DOM 92 100 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 122 127 Extracellular. {ECO:0000255}.; TOPO_DOM 149 167 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 189 195 Extracellular. {ECO:0000255}.; TOPO_DOM 217 235 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 257 274 Extracellular. {ECO:0000255}.; TOPO_DOM 296 306 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 328 333 Extracellular. {ECO:0000255}.; TOPO_DOM 355 379 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 401 409 Extracellular. {ECO:0000255}.; TOPO_DOM 431 459 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Widely expressed, with highest expression in the lung, pancreas and kidney. High expression in the CNS, particularly in the hypothalamus, the thalamus and the cerebellum. In the forebrain, abundantly expressed in the telencephalon, especially in the cerebral cortex layers, except layer 1, as well as in the induseum griseum, the piriform area, the taenia tecta, dorsal part and in the entorhinal area, lateral part. Lower levels in the bed anterior olfactory nucleus, posteroventral part and in layer two of the olfactory tubercle. In the amygdala, high levels observed in the intercalated nucleus and the medial nucleus. In the diencephalon, expressed in the nuclei in both the hypothalamus and thalamus. Among the hypothalamic areas, strongest expression in the arcuate nucleus and in the ventromedial nucleus, as well as in the suprachiasmatic nucleus, anterior nucleus, especially in its central part, and in the magnocellular division of the paraventricular nucleus. In the thalamus, highest levels in the medial habenula. Expression also observed in the paraventricular thalamic nucleus, parataenial nucleus, central medial nucleus, intermediodorsal nucleus and lateral dorsal nucleus. In the hindbrain, detected in the cerebellum and in the pons. In the midbrain and the medulla, expression levels were modest. In the midbrain, highest expression in the periaqueductal gray and all subdivisions of the interpeduncular nucleus, except for the caudal part. In the pons, the strongest labeling was seen in the nucleus incertus and in the tegmental nucleus. {ECO:0000269|PubMed:19697161}. +Q9DCU6 RM04_MOUSE 39S ribosomal protein L4, mitochondrial (L4mt) (MRP-L4) 294 33,073 Chain (1); Erroneous initiation (1); Frameshift (1); Modified residue (1); Sequence conflict (2) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9BYD3}. SUBUNIT: Component of the mitochondrial ribosome large subunit (39S) which comprises a 16S rRNA and about 50 distinct proteins. Interacts with MIEF1 upstream open reading frame protein. {ECO:0000250|UniProtKB:Q9BYD3}. +Q9CQL6 RM35_MOUSE 39S ribosomal protein L35, mitochondrial (L35mt) (MRP-L35) 188 21,501 Chain (1); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. +P70426 RIT1_MOUSE GTP-binding protein Rit1 (Ras-like protein expressed in many tissues) (Ras-like without CAAX protein 1) 219 25,169 Chain (1); Nucleotide binding (3) FUNCTION: Plays a crucial role in coupling NGF stimulation to the activation of both EPHB2 and MAPK14 signaling pathways and in NGF-dependent neuronal differentiation. Involved in ELK1 transactivation through the Ras-MAPK signaling cascade that mediates a wide variety of cellular functions, including cell proliferation, survival, and differentiation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane. SUBUNIT: Interacts with AFDN, the C-terminal domain of RALGDS and RLF, but not with RIN1 and PIK3CA. RLF binds exclusively to the active GTP-bound form. Strongly interacts with BRAF, but only weakly with RAF1. BARF and RAF1 association is dependent upon the GTP-bound state (By similarity). Interacts with RGL3. {ECO:0000250, ECO:0000269|PubMed:10869344}. TISSUE SPECIFICITY: Expressed in many tissues. +Q8R0F9 S14L4_MOUSE SEC14-like protein 4 403 46,053 Chain (1); Domain (2) FUNCTION: Probable hydrophobic ligand-binding protein; may play a role in the transport of hydrophobic ligands like tocopherol, squalene and phospholipids. {ECO:0000250}. +Q9JIP7 S15A1_MOUSE Solute carrier family 15 member 1 (Intestinal H(+)/peptide cotransporter) (Oligopeptide transporter, small intestine isoform) (Peptide transporter 1) (Proton-coupled dipeptide cotransporter) 709 78,560 Beta strand (19); Chain (1); Glycosylation (5); Helix (1); Sequence conflict (11); Topological domain (12); Transmembrane (12); Turn (1) TRANSMEM 1 21 Helical. {ECO:0000255}.; TRANSMEM 54 74 Helical. {ECO:0000255}.; TRANSMEM 83 103 Helical. {ECO:0000255}.; TRANSMEM 119 139 Helical. {ECO:0000255}.; TRANSMEM 162 182 Helical. {ECO:0000255}.; TRANSMEM 199 219 Helical. {ECO:0000255}.; TRANSMEM 277 297 Helical. {ECO:0000255}.; TRANSMEM 328 348 Helical. {ECO:0000255}.; TRANSMEM 362 382 Helical. {ECO:0000255}.; TRANSMEM 586 606 Helical. {ECO:0000255}.; TRANSMEM 621 641 Helical. {ECO:0000255}.; TRANSMEM 647 667 Helical. {ECO:0000255}. TOPO_DOM 22 53 Extracellular. {ECO:0000255}.; TOPO_DOM 75 82 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 104 118 Extracellular. {ECO:0000255}.; TOPO_DOM 140 161 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 183 198 Extracellular. {ECO:0000255}.; TOPO_DOM 220 276 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 298 327 Extracellular. {ECO:0000255}.; TOPO_DOM 349 361 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 383 585 Extracellular. {ECO:0000255}.; TOPO_DOM 607 620 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 642 646 Extracellular. {ECO:0000255}.; TOPO_DOM 668 709 Cytoplasmic. {ECO:0000255}. FUNCTION: Proton-coupled intake of oligopeptides of 2 to 4 amino acids with a preference for dipeptides. May constitute a major route for the absorption of protein digestion end-products (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. +Q9D8P4 RM17_MOUSE 39S ribosomal protein L17, mitochondrial (L17mt) (MRP-L17) 176 20,249 Alternative sequence (2); Chain (1); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9NRX2}. SUBUNIT: Component of the mitochondrial ribosome large subunit (39S) which comprises a 16S rRNA and about 50 distinct proteins. {ECO:0000250|UniProtKB:Q9NRX2}. +Q9D338 RM19_MOUSE 39S ribosomal protein L19, mitochondrial (L19mt) (MRP-L19) 292 33,578 Chain (1); Modified residue (1); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P49406}. SUBUNIT: Component of the mitochondrial ribosome large subunit (39S) which comprises a 16S rRNA and about 50 distinct proteins. {ECO:0000250|UniProtKB:P49406}. +Q9D0Y8 RM52_MOUSE 39S ribosomal protein L52, mitochondrial (L52mt) (MRP-L52) 121 13,658 Alternative sequence (1); Chain (1); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q86TS9}. SUBUNIT: Component of the mitochondrial ribosome large subunit (39S) which comprises a 16S rRNA and about 50 distinct proteins. {ECO:0000250|UniProtKB:Q86TS9}. +Q3TBW2 RM10_MOUSE 39S ribosomal protein L10, mitochondrial (L10mt) (MRP-L10) 262 29,396 Chain (1); Sequence conflict (2); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q7Z7H8}. SUBUNIT: Component of the mitochondrial ribosome large subunit (39S) which comprises a 16S rRNA and about 50 distinct proteins. {ECO:0000250|UniProtKB:Q7Z7H8}. +Q9CPW3 RM54_MOUSE 39S ribosomal protein L54, mitochondrial (L54mt) (MRP-L54) 135 15,422 Chain (1); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q6P161}. SUBUNIT: Component of the mitochondrial ribosome large subunit (39S) which comprises a 16S rRNA and about 50 distinct proteins. {ECO:0000250|UniProtKB:Q6P161}. +Q8VDT9 RM50_MOUSE 39S ribosomal protein L50, mitochondrial (L50mt) (MRP-L50) 159 18,213 Chain (1); Sequence conflict (2) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q8N5N7}. SUBUNIT: Component of the mitochondrial ribosome large subunit (39S) which comprises a 16S rRNA and about 50 distinct proteins. {ECO:0000250|UniProtKB:Q8N5N7}. +Q921R8 S41A3_MOUSE Solute carrier family 41 member 3 488 53,257 Alternative sequence (1); Chain (1); Transmembrane (9) TRANSMEM 63 83 Helical. {ECO:0000255}.; TRANSMEM 147 167 Helical. {ECO:0000255}.; TRANSMEM 189 209 Helical. {ECO:0000255}.; TRANSMEM 220 240 Helical. {ECO:0000255}.; TRANSMEM 251 271 Helical. {ECO:0000255}.; TRANSMEM 284 304 Helical. {ECO:0000255}.; TRANSMEM 377 397 Helical. {ECO:0000255}.; TRANSMEM 406 426 Helical. {ECO:0000255}.; TRANSMEM 450 470 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8K2M0 RM38_MOUSE 39S ribosomal protein L38, mitochondrial (L38mt) (MRP-L38) 380 45,030 Alternative sequence (1); Chain (1); Coiled coil (1); Erroneous initiation (3); Sequence conflict (4); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q96DV4}. SUBUNIT: Component of the mitochondrial ribosome large subunit (39S) which comprises a 16S rRNA and about 50 distinct proteins. {ECO:0000250|UniProtKB:Q96DV4}. +Q8BP31 RN122_MOUSE RING finger protein 122 155 17,448 Chain (1); Erroneous initiation (1); Sequence conflict (2); Transmembrane (1); Zinc finger (1) TRANSMEM 40 60 Helical. {ECO:0000255}. FUNCTION: May induce necrosis and apoptosis. May play a role in cell viability (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus. Endoplasmic reticulum {ECO:0000250}. Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q9CQN7 RM41_MOUSE 39S ribosomal protein L41, mitochondrial (L41mt) (MRP-L41) 135 15,262 Chain (1); Sequence conflict (2); Transit peptide (1) FUNCTION: Component of the mitochondrial ribosome large subunit. Also involved in apoptosis and cell cycle. Enhances p53/TP53 stability, thereby contributing to p53/TP53-induced apoptosis in response to growth-inhibitory condition. Enhances p53/TP53 translocation to the mitochondria. Has the ability to arrest the cell cycle at the G1 phase, possibly by stabilizing the CDKN1A and CDKN1B (p27Kip1) proteins. {ECO:0000250|UniProtKB:Q8IXM3}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q8IXM3}. SUBUNIT: Component of the mitochondrial ribosome large subunit (39S) which comprises a 16S rRNA and about 50 distinct proteins. Interacts with BCL2. {ECO:0000250|UniProtKB:Q8IXM3}. +Q9CPV3 RM42_MOUSE 39S ribosomal protein L42, mitochondrial (L42mt) (MRP-L42) (28S ribosomal protein S32, mitochondrial) (MRP-S32) (S32mt) (39S ribosomal protein L31, mitochondrial) (L31mt) (MRP-L31) 142 16,493 Chain (1); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9Y6G3}. SUBUNIT: Component of the mitochondrial ribosome large subunit (39S) which comprises a 16S rRNA and about 50 distinct proteins. Component of the mitochondrial ribosome small subunit (28S) which comprises a 12S rRNA and about 30 distinct proteins. {ECO:0000250|UniProtKB:Q9Y6G3}. +P58283 RN216_MOUSE E3 ubiquitin-protein ligase RNF216 (EC 2.3.2.27) (RING finger protein 216) (RING-type E3 ubiquitin transferase RNF216) (Triad domain-containing protein 3) (UbcM4-interacting protein 83) (Ubiquitin-conjugating enzyme 7-interacting protein 1) 853 97,682 Active site (1); Alternative sequence (3); Chain (1); Coiled coil (2); Cross-link (13); Metal binding (20); Modified residue (1); Region (1); Sequence conflict (4); Zinc finger (3) Protein modification; protein ubiquitination. FUNCTION: Acts as an E3 ubiquitin ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome. Promotes degradation of TRAF3, TLR4 and TLR9. Contributes to the regulation of antiviral responses. Down-regulates activation of NF-kappa-B, IRF3 activation and IFNB production. Promotes TNF and RIP mediated apoptosis. {ECO:0000250|UniProtKB:Q9NWF9}. PTM: Auto-ubiquitinated. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Interacts with UBE2L3 and to some extent with UBE2L6. Interacts with RIPK1, TRAF3, TLR3, TLR4, TLR5 and TLR9. {ECO:0000250}. +Q5SWK7 RN145_MOUSE RING finger protein 145 (EC 2.3.2.27) 663 74,648 Active site (1); Chain (1); Motif (1); Mutagenesis (2); Sequence conflict (6); Transmembrane (14); Zinc finger (1) TRANSMEM 53 73 Helical. {ECO:0000255}.; TRANSMEM 77 97 Helical. {ECO:0000255}.; TRANSMEM 123 143 Helical. {ECO:0000255}.; TRANSMEM 146 166 Helical. {ECO:0000255}.; TRANSMEM 168 188 Helical. {ECO:0000255}.; TRANSMEM 205 222 Helical. {ECO:0000255}.; TRANSMEM 225 245 Helical. {ECO:0000255}.; TRANSMEM 275 295 Helical. {ECO:0000255}.; TRANSMEM 316 336 Helical. {ECO:0000255}.; TRANSMEM 340 360 Helical. {ECO:0000255}.; TRANSMEM 384 404 Helical. {ECO:0000255}.; TRANSMEM 410 430 Helical. {ECO:0000255}.; TRANSMEM 460 480 Helical. {ECO:0000255}.; TRANSMEM 482 502 Helical. {ECO:0000255}. FUNCTION: E3 ubiquitin ligase that catalyzes the direct transfer of ubiquitin from E2 ubiquitin-conjugating enzyme to a specific substrate. In response to bacterial infection, negatively regulates the phagocyte oxidative burst by controlling the turnover of the NADPH oxidase complex subunits. Promotes monoubiquitination of CYBA and 'Lys-48'-linked polyubiquitination and degradation of CYBB NADPH oxidase catalytic subunits, both essential for the generation of antimicrobial reactive oxygen species (PubMed:26194095). Involved in the maintenance of cholesterol homeostasis. In response to high sterol concentrations ubiquitinates HMGCR, a rate-limiting enzyme in cholesterol biosynthesis, and targets it for degradation. The interaction with INSIG1 is required for this function (PubMed:29374057). In addition, triggers ubiquitination of SCAP, likely inhibiting its transport to the Golgi apparatus and the subsequent processing/maturation of SREBPF2, ultimately downregulating cholesterol biosynthesis (PubMed:29068315). {ECO:0000269|PubMed:26194095, ECO:0000269|PubMed:29068315, ECO:0000269|PubMed:29374057}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:26194095, ECO:0000269|PubMed:29068315, ECO:0000269|PubMed:29374057}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Interacts (via YLYF motif) with INSIG1 and INSIG2. {ECO:0000269|PubMed:29374057}. +Q3U9F6 RN166_MOUSE RING finger protein 166 237 26,064 Chain (1); Domain (1); Zinc finger (2) +P14115 RL27A_MOUSE 60S ribosomal protein L27a (L29) 148 16,605 Chain (1); Modified residue (5); Sequence conflict (3) PTM: Hydroxylated on His-39 by MINA. {ECO:0000250}. +Q8JZS9 RM48_MOUSE 39S ribosomal protein L48, mitochondrial (L48mt) (MRP-L48) 211 23,953 Chain (1); Compositional bias (1); Erroneous initiation (1); Modified residue (1); Sequence caution (1); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q96GC5}. SUBUNIT: Component of the mitochondrial ribosome large subunit (39S) which comprises a 16S rRNA and about 50 distinct proteins (By similarity). Interacts with OXA1L (By similarity). {ECO:0000250|UniProtKB:Q2YDI5, ECO:0000250|UniProtKB:Q96GC5}. +Q8K0H1 S47A1_MOUSE Multidrug and toxin extrusion protein 1 (MATE-1) (mMATE-1) (Solute carrier family 47 member 1) 567 61,642 Alternative sequence (2); Chain (1); Frameshift (1); Modified residue (2); Topological domain (14); Transmembrane (13) TRANSMEM 38 58 Helical. {ECO:0000255}.; TRANSMEM 73 93 Helical. {ECO:0000255}.; TRANSMEM 121 141 Helical. {ECO:0000255}.; TRANSMEM 153 173 Helical. {ECO:0000255}.; TRANSMEM 188 208 Helical. {ECO:0000255}.; TRANSMEM 217 237 Helical. {ECO:0000255}.; TRANSMEM 258 277 Helical. {ECO:0000255}.; TRANSMEM 296 316 Helical. {ECO:0000255}.; TRANSMEM 337 357 Helical. {ECO:0000255}.; TRANSMEM 371 391 Helical. {ECO:0000255}.; TRANSMEM 409 429 Helical. {ECO:0000255}.; TRANSMEM 438 458 Helical. {ECO:0000255}.; TRANSMEM 544 564 Helical. {ECO:0000255}. TOPO_DOM 1 37 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 59 72 Extracellular. {ECO:0000255}.; TOPO_DOM 94 120 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 142 152 Extracellular. {ECO:0000255}.; TOPO_DOM 174 187 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 209 216 Extracellular. {ECO:0000255}.; TOPO_DOM 238 257 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 278 295 Extracellular. {ECO:0000255}.; TOPO_DOM 317 336 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 358 370 Extracellular. {ECO:0000255}.; TOPO_DOM 392 408 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 430 437 Extracellular. {ECO:0000255}.; TOPO_DOM 459 543 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 565 567 Extracellular. {ECO:0000255}. FUNCTION: Solute transporter for tetraethylammonium (TEA), 1-methyl-4-phenylpyridinium (MPP), cimetidine, N-methylnicotinamide (NMN), metformin, creatinine, guanidine, procainamide, topotecan, estrone sulfate, acyclovir, ganciclovir and also the zwitterionic cephalosporin, cephalexin and cephradin. Seems to also play a role in the uptake of oxaliplatin (a new platinum anticancer agent). Able to transport paraquat (PQ or N,N-dimethyl-4-4'-bipiridinium); a widely used herbicid. Responsible for the secretion of cationic drugs across the brush border membranes (By similarity). {ECO:0000250, ECO:0000269|PubMed:16641166, ECO:0000269|PubMed:17715386}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16330770, ECO:0000269|PubMed:16641166, ECO:0000269|PubMed:17715386}; Multi-pass membrane protein {ECO:0000269|PubMed:16330770, ECO:0000269|PubMed:16641166, ECO:0000269|PubMed:17715386}. Note=Predominantly localized to the plasma membrane; at the brush border membranes of the proximal tubules (kidney) and at the bile caniculi (liver). TISSUE SPECIFICITY: Predominantly expressed in kidney and liver. Also expressed in various cells, including brain glia-like cells and capillaries, pancreatic duct cells, urinary bladder epithelium, adrenal gland cortex, heart, stomach, small intestine, thyroid gland, testes, alpha cells of the islets of Langerhans, Leydig cells, and vitamin A-storing Ito cells. Expressed in heart, stomach, small intestine, bladder, thyroid gland, adrenal gland and testes (at protein level). {ECO:0000269|PubMed:16330770}. +Q99N91 RM34_MOUSE 39S ribosomal protein L34, mitochondrial (L34mt) (MRP-L34) 92 10,531 Chain (1); Modified residue (1); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9BQ48}. SUBUNIT: Component of the mitochondrial ribosome large subunit (39S) which comprises a 16S rRNA and about 50 distinct proteins. {ECO:0000250|UniProtKB:Q9BQ48}. +Q9CXW4 RL11_MOUSE 60S ribosomal protein L11 178 20,252 Chain (1); Cross-link (3); Initiator methionine (1); Modified residue (5); Sequence conflict (1) FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. As part of the 5S RNP/5S ribonucleoprotein particle it is an essential component of the LSU, required for its formation and the maturation of rRNAs. It also couples ribosome biogenesis to p53/TP53 activation. As part of the 5S RNP it accumulates in the nucleoplasm and inhibits MDM2, when ribosome biogenesis is perturbed, mediating the stabilization and the activation of TP53 (PubMed:21804542). Promotes nucleolar location of PML (PubMed:15195100). {ECO:0000269|PubMed:15195100, ECO:0000269|PubMed:21804542}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:15195100, ECO:0000269|PubMed:21804542}. Cytoplasm {ECO:0000269|PubMed:21804542}. SUBUNIT: Component of the large ribosomal subunit (LSU). Part of a LSU subcomplex, the 5S RNP which is composed of the 5S RNA, RPL5 and RPL11 (By similarity). Interacts with PML (PubMed:15195100). Interacts with MDM2; negatively regulates MDM2-mediated TP53 ubiquitination and degradation (PubMed:15195100, PubMed:21804542). Interacts with NOP53; retains RPL11 into the nucleolus (PubMed:21804542). {ECO:0000250|UniProtKB:P62913, ECO:0000269|PubMed:15195100, ECO:0000269|PubMed:21804542}. +P14148 RL7_MOUSE 60S ribosomal protein L7 270 31,420 Chain (1); Modified residue (5); Region (1); Repeat (6); Sequence conflict (5) FUNCTION: Component of the large ribosomal subunit (By similarity). Binds to G-rich structures in 28S rRNA and in mRNAs. Plays a regulatory role in the translation apparatus; inhibits cell-free translation of mRNAs (By similarity). {ECO:0000250|UniProtKB:P18124}. SUBUNIT: Component of the large ribosomal subunit. Homodimer. Interacts with DHX33 (PubMed:26100019). {ECO:0000250|UniProtKB:P18124, ECO:0000269|PubMed:26100019}. +Q99N92 RM27_MOUSE 39S ribosomal protein L27, mitochondrial (L27mt) (MRP-L27) 148 15,945 Chain (1); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11279069}. SUBUNIT: Component of the mitochondrial ribosome large subunit (39S) which comprises a 16S rRNA and about 50 distinct proteins. {ECO:0000250|UniProtKB:Q9P0M9}. +Q9D1P0 RM13_MOUSE 39S ribosomal protein L13, mitochondrial (L13mt) (MRP-L13) 178 20,677 Chain (1); Initiator methionine (1); Modified residue (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9BYD1}. SUBUNIT: Component of the mitochondrial ribosome large subunit (39S) which comprises a 16S rRNA and about 50 distinct proteins (By similarity). Interacts with OXA1L (By similarity). {ECO:0000250|UniProtKB:Q3SYS1, ECO:0000250|UniProtKB:Q9BYD1}. +Q3UPE3 RMI2_MOUSE RecQ-mediated genome instability protein 2 149 15,838 Alternative sequence (1); Chain (1); DNA binding (1); Modified residue (1) FUNCTION: Essential component of the RMI complex, a complex that plays an important role in the processing of homologous recombination intermediates. It is required to regulate sister chromatid segregation and to limit DNA crossover. Essential for the stability, localization, and function of BLM, TOP3A, and complexes containing BLM. In the RMI complex, it is required to target BLM to chromatin and stress-induced nuclear foci and mitotic phosphorylation of BLM. {ECO:0000250|UniProtKB:Q96E14}. PTM: Phosphorylated during mitosis. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Colocalizes with BLM at nuclear DNA repair foci. {ECO:0000250}. SUBUNIT: Component of the RMI complex, containing at least TOP3A, RMI1 and RMI2. The RMI complex interacts with BLM (By similarity). {ECO:0000250}. +Q8BIV7 S45A1_MOUSE Proton-associated sugar transporter A (PAST-A) (Deleted in neuroblastoma 5 protein homolog) (DNb-5 homolog) (Solute carrier family 45 member 1) 751 81,474 Chain (1); Frameshift (1); Modified residue (1); Sequence conflict (2); Transmembrane (12) TRANSMEM 93 113 Helical. {ECO:0000255}.; TRANSMEM 123 143 Helical. {ECO:0000255}.; TRANSMEM 155 175 Helical. {ECO:0000255}.; TRANSMEM 191 211 Helical. {ECO:0000255}.; TRANSMEM 233 253 Helical. {ECO:0000255}.; TRANSMEM 268 288 Helical. {ECO:0000255}.; TRANSMEM 536 556 Helical. {ECO:0000255}.; TRANSMEM 576 596 Helical. {ECO:0000255}.; TRANSMEM 606 626 Helical. {ECO:0000255}.; TRANSMEM 630 650 Helical. {ECO:0000255}.; TRANSMEM 688 708 Helical. {ECO:0000255}.; TRANSMEM 710 730 Helical. {ECO:0000255}. FUNCTION: Proton-associated glucose transporter in the brain. {ECO:0000250|UniProtKB:Q8K4S3}. SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9Y2W3}; Multi-pass membrane protein {ECO:0000255}. +Q0P5V9 S45A4_MOUSE Solute carrier family 45 member 4 785 85,765 Alternative sequence (2); Chain (1); Modified residue (4); Sequence conflict (2); Transmembrane (12) TRANSMEM 64 84 Helical. {ECO:0000255}.; TRANSMEM 87 107 Helical. {ECO:0000255}.; TRANSMEM 124 144 Helical. {ECO:0000255}.; TRANSMEM 156 176 Helical. {ECO:0000255}.; TRANSMEM 197 217 Helical. {ECO:0000255}.; TRANSMEM 234 254 Helical. {ECO:0000255}.; TRANSMEM 525 545 Helical. {ECO:0000255}.; TRANSMEM 577 597 Helical. {ECO:0000255}.; TRANSMEM 609 629 Helical. {ECO:0000255}.; TRANSMEM 631 651 Helical. {ECO:0000255}.; TRANSMEM 683 703 Helical. {ECO:0000255}.; TRANSMEM 709 729 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9JKF7 RM39_MOUSE 39S ribosomal protein L39, mitochondrial (L39mt) (MRP-L39) 336 38,549 Chain (1); Erroneous initiation (3); Frameshift (1); Modified residue (1); Sequence conflict (5) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9NYK5}. SUBUNIT: Component of the mitochondrial ribosome large subunit (39S) which comprises a 16S rRNA and about 50 distinct proteins. {ECO:0000250|UniProtKB:Q9NYK5}. +Q9CQL4 RM20_MOUSE 39S ribosomal protein L20, mitochondrial (L20mt) (MRP-L20) 149 17,595 Chain (1); Sequence conflict (1); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q2TBR2}. SUBUNIT: Component of the mitochondrial ribosome large subunit (39S) which comprises a 16S rRNA and about 50 distinct proteins (By similarity). Interacts with OXA1L (By similarity). {ECO:0000250|UniProtKB:Q2TBR2, ECO:0000250|UniProtKB:Q9BYC9}. +Q91YL2 RN126_MOUSE E3 ubiquitin-protein ligase RNF126 (EC 2.3.2.27) (RING finger protein 126) 313 34,081 Beta strand (3); Chain (1); Compositional bias (1); Helix (1); Initiator methionine (1); Metal binding (4); Modified residue (2); Mutagenesis (3); Region (2); Turn (3); Zinc finger (2) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination oF target proteins (By similarity). Depending on the associated E2 ligase, mediates 'Lys-48'- and 'Lys-63'-linked polyubiquitination of substrates (PubMed:23418353). Part of a BAG6-dependent quality control process ensuring that proteins of the secretory pathway that are mislocalized to the cytosol are degraded by the proteasome (By similarity). Probably acts by providing the ubiquitin ligase activity associated with the BAG6 complex and be responsible for ubiquitination of the hydrophobic mislocalized proteins and their targeting to the proteasome (By similarity). May also play a role in the endosomal recycling of IGF2R, the cation-independent mannose-6-phosphate receptor (By similarity). May play a role in the endosomal sorting and degradation of several membrane receptors including EGFR, FLT3, MET and CXCR4, by mediating their ubiquitination (PubMed:23418353). By ubiquitinating CDKN1A/p21 and targeting it for degradation, may also promote cell proliferation (By similarity). May monoubiquitinate AICDA (By similarity). {ECO:0000250|UniProtKB:Q9BV68, ECO:0000269|PubMed:23418353}. PTM: Ubiquitinated. May undergo autoubiquitination. {ECO:0000250|UniProtKB:Q9BV68, ECO:0000303|PubMed:23418353}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BV68}. Nucleus {ECO:0000250|UniProtKB:Q9BV68}. SUBUNIT: Interacts with CCDC50, EGFR, FLT3 and SCAMP3 (PubMed:23418353). Interacts with BAG6 (via ubiquitin-like domain); required for BAG6-dependent ubiquitination of proteins mislocalized to the cytosol (By similarity). Interacts with CDKN1A (By similarity). Interacts with AICDA (By similarity). {ECO:0000250|UniProtKB:Q9BV68, ECO:0000269|PubMed:23418353}. DOMAIN: The C4-type zinc finger is required for interaction with BAG6. {ECO:0000250|UniProtKB:Q9BV68}. TISSUE SPECIFICITY: Detected in B-cells (at protein level). {ECO:0000269|PubMed:23277564}. +Q3U827 RN180_MOUSE E3 ubiquitin-protein ligase RNF180 (EC 2.3.2.27) (RING finger protein 180) (RING-type E3 ubiquitin transferase RNF180) 592 67,371 Alternative sequence (3); Chain (1); Modified residue (1); Region (1); Sequence conflict (7); Topological domain (2); Transmembrane (1); Zinc finger (1) TRANSMEM 565 585 Helical. {ECO:0000255}. TOPO_DOM 1 564 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 586 592 Extracellular. {ECO:0000255}. Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase which promotes polyubiquitination and degradation by the proteasome pathway of ZIC2. {ECO:0000269|PubMed:18363970}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18363970}; Single-pass membrane protein {ECO:0000269|PubMed:18363970}. Nucleus envelope {ECO:0000269|PubMed:18363970}. SUBUNIT: Interacts with ZIC2. {ECO:0000269|PubMed:18363970}. DOMAIN: The RING-type zinc finger domain mediates polyubiquitination of the interacting protein. {ECO:0000269|PubMed:18363970}. TISSUE SPECIFICITY: brain, kidney, testis and uterus. membrane protein. Nucleus envelope. {ECO:0000269|PubMed:18363970}. +O35972 RM23_MOUSE 39S ribosomal protein L23, mitochondrial (L23mt) (MRP-L23) (L23 mitochondrial-related protein) 146 17,122 Chain (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q16540}. SUBUNIT: Component of the mitochondrial ribosome large subunit (39S) which comprises a 16S rRNA and about 50 distinct proteins. {ECO:0000250|UniProtKB:Q16540}. +Q9CQE0 RN138_MOUSE E3 ubiquitin-protein ligase RNF138 (EC 2.3.2.27) (RING finger protein 138) (RING-type E3 ubiquitin transferase RNF138) 245 28,299 Alternative sequence (1); Chain (1); Domain (1); Modified residue (1); Sequence conflict (1); Zinc finger (4) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase involved in DNA damage response by promoting DNA resection and homologous recombination. Recruited to sites of double-strand breaks following DNA damage and specifically promotes double-strand break repair via homologous recombination. Two different, non-exclusive, mechanisms have been proposed. According to a report, regulates the choice of double-strand break repair by favoring homologous recombination over non-homologous end joining (NHEJ): acts by mediating ubiquitination of XRCC5/Ku80, leading to remove the Ku complex from DNA breaks, thereby promoting homologous recombination. According to another report, cooperates with UBE2Ds E2 ubiquitin ligases (UBE2D1, UBE2D2, UBE2D3 or UBE2D4) to promote homologous recombination by mediating ubiquitination of RBBP8/CtIP. Together with NLK, involved in the ubiquitination and degradation of TCF/LEF. Also exhibits auto-ubiquitination activity in combination with UBE2K. May act as a negative regulator in the Wnt/beta-catenin-mediated signaling pathway. {ECO:0000250|UniProtKB:Q8WVD3}. PTM: Auto-ubiquitinated. {ECO:0000250|UniProtKB:Q8WVD3}. SUBCELLULAR LOCATION: Chromosome {ECO:0000250|UniProtKB:Q8WVD3}. Note=Recruited at DNA damage sites. Localizes to sites of double-strand break: localization to double-strand break sites is mediated by the zinc fingers. {ECO:0000250|UniProtKB:Q8WVD3}. SUBUNIT: Interacts with NLK. Interacts with XRCC5/Ku80. Interacts with RBBP8/CtIP. {ECO:0000250|UniProtKB:Q8WVD3}. DOMAIN: The zinc finger domains (C2H2-type and C2HC-type zinc fingers) bind DNA and mediate recruitment to double-strand break sites. They show strong preference for DNA with 5'- or 3'-single-stranded overhangs, while they do not bind blunt-ended double-stranded DNA or poly(ADP-ribose) (PAR) polymers. {ECO:0000250|UniProtKB:Q8WVD3}. +Q91YT2 RN185_MOUSE E3 ubiquitin-protein ligase RNF185 (EC 2.3.2.27) (RING finger protein 185) (RING-type E3 ubiquitin transferase RNF185) 192 20,520 Alternative sequence (1); Chain (1); Region (1); Topological domain (2); Transmembrane (2); Zinc finger (1) TRANSMEM 131 151 Helical. {ECO:0000255}.; TRANSMEM 172 192 Helical. {ECO:0000255}. TOPO_DOM 1 130 Cytoplasmic.; TOPO_DOM 152 171 Mitochondrial intermembrane. Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that regulates selective mitochondrial autophagy by mediating 'Lys-63'-linked polyubiquitination of BNIP1. Acts in the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway, which targets misfolded proteins that accumulate in the endoplasmic reticulum (ER) for ubiquitination and subsequent proteasome-mediated degradation. Protects cells from ER stress-induced apoptosis. Responsible for the cotranslational ubiquitination and degradation of CFTR in the ERAD pathway. Preferentially associates with the E2 enzymes UBE2J1 and UBE2J2 (By similarity). {ECO:0000250|UniProtKB:Q96GF1}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q96GF1}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q96GF1}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q96GF1}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q96GF1}. SUBUNIT: Interacts with ATG5 and BNIP1. {ECO:0000250|UniProtKB:Q96GF1}. DOMAIN: The RING-type zinc finger domain is responsible for E3 ubiquitin ligase activity. {ECO:0000250|UniProtKB:Q96GF1}. TISSUE SPECIFICITY: Ubiquitously expressed with high expression in testis. {ECO:0000269|PubMed:27485036}. +Q3TEL6 RN157_MOUSE E3 ubiquitin ligase Rnf157 (EC 2.3.2.27) (RING finger protein 157) (RING-type E3 ubiquitin transferase Rnf157) 685 74,534 Alternative sequence (2); Chain (1); Compositional bias (1); Erroneous initiation (1); Initiator methionine (1); Lipidation (1); Motif (2); Zinc finger (1) FUNCTION: E3 ubiquitin ligase that ubiquitinates APBB1 for its degradation by the proteasome and thus prevents apoptosis and promotes survival of neurons (PubMed:25342469). Has a dual role in neurons as it is also required for dendrite growth and maintenance for which its ligase activity is not critical (PubMed:25342469). May act as a scaffold molecule to regulate this process (PubMed:25342469). Acts as a downstream effector of the interconnected PI3K and MAPK signaling pathways and thus participates in the regulation of the cell cycle (By similarity). {ECO:0000250|UniProtKB:Q96PX1, ECO:0000269|PubMed:25342469}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:M0R5D6}. SUBUNIT: Interacts with APBB1 (PubMed:25342469). Interacts with CHD1; CHD1-binding controls RNF157 stability (By similarity). Interacts also with ATRN, MEGF8, TECR, MSI2, PLRG1, BYSL, MTERF3, PSMA1, MRPS18B, PRPF4, FASTKD2, SLC25A1, SMU1, CNOT9, MRPS2, MAGT1, FXR2, EMD, PSMD8, HDAC1, RAN, HSD17B12, TXNDC5 AND MRPL19 (By similarity). {ECO:0000250|UniProtKB:Q96PX1, ECO:0000269|PubMed:25342469}. DOMAIN: The D-box motifs play a key role in RNF157 stabilization (By similarity). {ECO:0000250|UniProtKB:M0R5D6}. +Q8CEF8 RN222_MOUSE RING finger protein 222 211 23,003 Chain (1); Sequence conflict (1); Transmembrane (1); Zinc finger (1) TRANSMEM 187 207 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q3V3A7 RN207_MOUSE RING finger protein 207 635 70,759 Chain (1); Coiled coil (1); Compositional bias (1); Erroneous termination (1); Zinc finger (2) FUNCTION: Plays a role in cardiac repolarization possibly by stabilizing membrane expression of the potassium channel KCNH2/HERG, or by assisting its synthesis, folding or export from the endoplasmic reticulum, in a heat shock protein-dependent manner. {ECO:0000250|UniProtKB:Q6ZRF8}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6ZRF8}. Note=Probably located in the endoplasmic reticulum and/or possibly the cis-Golgi apparatus. {ECO:0000250|UniProtKB:Q6ZRF8}. SUBUNIT: Interacts with the core-glycosylated, but not the fully glycosylated form of KCNH2/HERG. Interacts with DNAJA1 and HSPA8. Interacts (via the C-terminus) with HSPA1A; this interaction additively increases KCNH2 expression. {ECO:0000250|UniProtKB:Q6ZRF8}. +Q6PDH4 RNB3L_MOUSE Ran-binding protein 3-like 491 54,492 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (1) FUNCTION: Nuclear export factor for BMP-specific SMAD1/5/8 that plays a critical role in terminating BMP signaling and regulating mesenchymal stem cell differentiation by blocking osteoblast differentiation to promote myogenic differention. Directly recognizes dephosphorylated SMAD1/5/8 and mediates their nuclear export in a Ran-dependent manner. {ECO:0000250|UniProtKB:Q86VV4, ECO:0000269|PubMed:25755279}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:25755279}. Cytoplasm {ECO:0000305|PubMed:25755279}. SUBUNIT: Interacts with SMAD1, SMAD5 and SMAD8. {ECO:0000250|UniProtKB:Q86VV4, ECO:0000269|PubMed:25755279}. +E9Q7F2 RN169_MOUSE E3 ubiquitin-protein ligase RNF169 (EC 2.3.2.27) (RING finger protein 169) (RING-type E3 ubiquitin transferase RNF169) 694 75,796 Chain (1); Cross-link (3); Modified residue (11); Motif (3); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: Probable E3 ubiquitin-protein ligase that acts as a negative regulator of double-strand breaks (DSBs) repair following DNA damage. Recruited to DSB repair sites by recognizing and binding ubiquitin catalyzed by RNF168 and competes with TP53BP1 and BRCA1 for association with RNF168-modified chromatin, thereby acting as a negative regulator of DSBs repair. E3 ubiquitin-protein ligase activity is not required for regulation of DSBs repair. {ECO:0000250|UniProtKB:Q8NCN4}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q8NCN4}. Note=Localizes to sites of double-strand breaks (DSBs) following DNA damage. Recruited to DSBs via recognition of RNF168-dependent ubiquitin products. {ECO:0000250|UniProtKB:Q8NCN4}. DOMAIN: The MIU motif (motif interacting with ubiquitin) mediates the interaction with both 'Lys-48'- and 'Lys-63'-linked ubiquitin chains. The UMI motif also mediates interaction with ubiquitin. The specificity for different types of ubiquitin is mediated by juxtaposition of ubiquitin-binding motifs (MIU and UMI motifs) with LR motifs (LRMs). {ECO:0000250|UniProtKB:Q8NCN4}. +Q9JIT1 RNF32_MOUSE RING finger protein 32 (Limb region protein 2) 368 42,139 Chain (1); Domain (1); Sequence conflict (5); Zinc finger (2) FUNCTION: May play a role in sperm formation. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +Q5GAM8 RNS12_MOUSE Probable inactive ribonuclease-like protein 12 145 16,936 Chain (1); Signal peptide (1) FUNCTION: Does not exhibit any ribonuclease activity. {ECO:0000305}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q99N94 RM09_MOUSE 39S ribosomal protein L9, mitochondrial (L9mt) (MRP-L9) 265 30,244 Chain (1); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9BYD2}. SUBUNIT: Component of the mitochondrial ribosome large subunit (39S) which comprises a 16S rRNA and about 50 distinct proteins. {ECO:0000250|UniProtKB:Q9BYD2}. +Q9D1H8 RM53_MOUSE 39S ribosomal protein L53, mitochondrial (L53mt) (MRP-L53) 118 12,738 Chain (1); Compositional bias (1); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q96EL3}. SUBUNIT: Component of the mitochondrial ribosome large subunit (39S) which comprises a 16S rRNA and about 50 distinct proteins. {ECO:0000250|UniProtKB:Q96EL3}. +Q9JHI9 S40A1_MOUSE Solute carrier family 40 member 1 (Ferroportin-1) (Iron-regulated transporter 1) (Metal transporter protein 1) (MTP1) 570 62,702 Chain (1); Glycosylation (4); Transmembrane (10) TRANSMEM 12 34 Helical. {ECO:0000255}.; TRANSMEM 58 80 Helical. {ECO:0000255}.; TRANSMEM 93 115 Helical. {ECO:0000255}.; TRANSMEM 125 147 Helical. {ECO:0000255}.; TRANSMEM 302 324 Helical. {ECO:0000255}.; TRANSMEM 339 361 Helical. {ECO:0000255}.; TRANSMEM 373 395 Helical. {ECO:0000255}.; TRANSMEM 449 471 Helical. {ECO:0000255}.; TRANSMEM 491 513 Helical. {ECO:0000255}.; TRANSMEM 518 540 Helical. {ECO:0000255}. FUNCTION: May be involved in iron export from duodenal epithelial cell and also in transfer of iron between maternal and fetal circulation. Mediates iron efflux in the presence of a ferroxidase (hephaestin and/or ceruloplasmin). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Note=Localized to the basolateral membrane of polarized epithelial cells. SUBUNIT: Identified in a complex with STOM. {ECO:0000250}. TISSUE SPECIFICITY: High expression in spleen, liver, kidney, heart and duodenum. +Q9D7N6 RM30_MOUSE 39S ribosomal protein L30, mitochondrial (L30mt) (MRP-L30) 160 18,342 Chain (1); Sequence conflict (1); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q8TCC3}. SUBUNIT: Component of the mitochondrial ribosome large subunit (39S) which comprises a 16S rRNA and about 50 distinct proteins. {ECO:0000250|UniProtKB:Q8TCC3}. +Q9ET26 RN114_MOUSE E3 ubiquitin-protein ligase RNF114 (EC 2.3.2.27) (RING finger protein 114) (RING-type E3 ubiquitin transferase RNF114) (Zinc finger protein 228) (Zinc finger protein 313) 229 25,745 Chain (1); Modified residue (2); Zinc finger (2) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase promoting the ubiquitination and degradation of the CDK inhibitor CDKN1A and probably also CDKN1B and CDKN1C. These activities stimulate cell cycle's G1-to-S phase transition and suppress cellular senescence. May play a role in spermatogenesis. {ECO:0000250|UniProtKB:Q9Y508}. PTM: Autoubiquitinated. Polyubiquitinated in the presence of E2 enzymes UBE2D1, UBE2D2 and UBE2D3, but only monoubiquitinated in the presence of UBE2E1. {ECO:0000250|UniProtKB:Q9Y508}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y508}. Nucleus {ECO:0000250|UniProtKB:Q9Y508}. SUBUNIT: Interacts with XAF1, the interaction increases XAF1 stability and proapoptotic effects, and may regulate IFN signaling. {ECO:0000250|UniProtKB:Q9Y508}. +Q9CPY1 RM51_MOUSE 39S ribosomal protein L51, mitochondrial (L51mt) (MRP-L51) (bMRP-64) (bMRP64) 128 15,103 Chain (1); Sequence conflict (2); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q4U2R6}. SUBUNIT: Component of the mitochondrial ribosome large subunit (39S) which comprises a 16S rRNA and about 50 distinct proteins (By similarity). Interacts with OXA1L (By similarity). {ECO:0000250|UniProtKB:P0C2B6, ECO:0000250|UniProtKB:Q4U2R6}. +Q91VM5 RMXL1_MOUSE RNA binding motif protein, X-linked-like-1 (Heterogeneous nuclear ribonucleoprotein G-like 1) (RNA binding motif protein, X chromosome retrogene) 388 42,162 Chain (1); Cross-link (1); Domain (1); Modified residue (1); Sequence conflict (5) FUNCTION: RNA-binding protein which may be involved in pre-mRNA splicing. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +Q9D9R0 RN125_MOUSE E3 ubiquitin-protein ligase RNF125 (EC 2.3.2.27) (RING finger protein 125) 233 26,362 Alternative sequence (1); Chain (1); Frameshift (1); Initiator methionine (1); Lipidation (1); Metal binding (12); Region (4); Sequence conflict (1); Zinc finger (2) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins, such as DDX58/RIG-I, MAVS/IPS1, IFIH1/MDA5, JAK1 and p53/TP53. Acts as a negative regulator of type I interferon production by mediating ubiquitination of DDX58/RIG-I at 'Lys-181', leading to DDX58/RIG-I degradation. Mediates ubiquitination and subsequent degradation of p53/TP53. Mediates ubiquitination and subsequent degradation of JAK1. Acts as a positive regulator of T-cell activation. {ECO:0000250|UniProtKB:Q96EQ8}. PTM: Autoubiquitinated, leading to its subsequent proteasomal degradation. {ECO:0000250|UniProtKB:Q96EQ8}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q96EQ8}; Lipid-anchor {ECO:0000250|UniProtKB:Q96EQ8}. Note=Shows a reticular staining pattern within the cell and is probably expressed at other intracellular membranes in addition to the Golgi membrane. Not detected at the plasma membrane. {ECO:0000250|UniProtKB:Q96EQ8}. SUBUNIT: Interacts with UBE2D1. Interacts with VCP/p97; leading to recruit RNF125 to DDX58/RIG-I and promote ubiquitination of DDX58/RIG-I. {ECO:0000250|UniProtKB:Q96EQ8}. DOMAIN: The C2HC RNF-type zinc finger and the linker region stabilize the RING-type zinc finger, leading to promote binding of the RING-type zinc finger to the ubiquitin-conjugating enzyme E2 (donor ubiquitin). {ECO:0000250|UniProtKB:Q96EQ8}. +A2A7Q9 RN19B_MOUSE E3 ubiquitin-protein ligase RNF19B (EC 2.3.2.31) (IBR domain-containing protein 3) (Natural killer lytic-associated molecule) (RING finger protein 19B) 732 78,127 Active site (1); Chain (1); Compositional bias (2); Erroneous initiation (2); Metal binding (20); Region (2); Sequence conflict (3); Transmembrane (2); Zinc finger (3) TRANSMEM 351 371 Helical. {ECO:0000255}.; TRANSMEM 412 432 Helical. {ECO:0000255}. Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates, such as UCKL1. Involved in the cytolytic activity of natural killer cells and cytotoxic T-cells. Protects against staurosporin-induced cell death (By similarity). {ECO:0000250|UniProtKB:Q6ZMZ0}. SUBCELLULAR LOCATION: Cytoplasmic granule membrane {ECO:0000250|UniProtKB:Q6ZMZ0}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q6ZMZ0}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q6ZMZ0}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q6ZMZ0}. SUBUNIT: Interacts with UBE2L3, UBE2L6 and UCKL1. {ECO:0000250|UniProtKB:Q6ZMZ0}. DOMAIN: The first IBR-type zinc finger is the most crucial for interaction with UBE2L3, UBE2L6 and UCKL1. {ECO:0000250|UniProtKB:Q6ZMZ0}.; DOMAIN: Members of the RBR family are atypical E3 ligases. They interact with the E2 conjugating enzyme UBE2L3 and function like HECT-type E3 enzymes: they bind E2s via the first RING domain, but require an obligate trans-thiolation step during the ubiquitin transfer, requiring a conserved cysteine residue in the second RING domain. {ECO:0000250|UniProtKB:O60260}. TISSUE SPECIFICITY: Expressed specifically in natural killer cells, activated macrophages and cytotoxic T-cells (PubMed:10912506). Present in macrophages (at protein level) (PubMed:10912506). Ubiquitously expressed with high expression in testis (PubMed:27485036). {ECO:0000269|PubMed:10912506, ECO:0000269|PubMed:27485036}. +P60154 RNAS9_MOUSE Inactive ribonuclease-like protein 9 184 21,378 Chain (1); Disulfide bond (3); Glycosylation (2); Signal peptide (1) FUNCTION: Does not exhibit any ribonuclease activity. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q80XJ2 RN168_MOUSE E3 ubiquitin-protein ligase RNF168 (EC 2.3.2.27) (RING finger protein 168) (RING-type E3 ubiquitin transferase RNF168) 565 64,779 Chain (1); Compositional bias (2); Cross-link (2); Erroneous initiation (1); Erroneous termination (1); Modified residue (6); Motif (5); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase required for accumulation of repair proteins to sites of DNA damage. Acts with UBE2N/UBC13 to amplify the RNF8-dependent histone ubiquitination. Recruited to sites of DNA damage at double-strand breaks (DSBs) by binding to ubiquitinated histone H2A and H2AX and amplifies the RNF8-dependent H2A ubiquitination, promoting the formation of 'Lys-63'-linked ubiquitin conjugates. This leads to concentrate ubiquitinated histones H2A and H2AX at DNA lesions to the threshold required for recruitment of TP53BP1 and BRCA1. Also recruited at DNA interstrand cross-links (ICLs) sites and promotes accumulation of 'Lys-63'-linked ubiquitination of histones H2A and H2AX, leading to recruitment of FAAP20 and Fanconi anemia (FA) complex, followed by interstrand cross-link repair. H2A ubiquitination also mediates the ATM-dependent transcriptional silencing at regions flanking DSBs in cis, a mechanism to avoid collision between transcription and repair intermediates. Also involved in class switch recombination in immune system, via its role in regulation of DSBs repair. Following DNA damage, promotes the ubiquitination and degradation of JMJD2A/KDM4A in collaboration with RNF8, leading to unmask H4K20me2 mark and promote the recruitment of TP53BP1 at DNA damage sites. Not able to initiate 'Lys-63'-linked ubiquitination in vitro; possibly due to partial occlusion of the UBE2N/UBC13-binding region. Catalyzes monoubiquitination of 'Lys-13' and 'Lys-15' of nucleosomal histone H2A (H2AK13Ub and H2AK15Ub, respectively). {ECO:0000255|HAMAP-Rule:MF_03066, ECO:0000269|PubMed:20080757}. PTM: Sumoylated with SUMO1 by PIAS4 in response to double-strand breaks (DSBs). {ECO:0000255|HAMAP-Rule:MF_03066}.; PTM: Ubiquitinated. {ECO:0000255|HAMAP-Rule:MF_03066}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03066}. Note=Localizes to double-strand breaks (DSBs) sites of DNA damage. {ECO:0000255|HAMAP-Rule:MF_03066}. SUBUNIT: Monomer. Interacts with UBE2N/UBC13. {ECO:0000255|HAMAP-Rule:MF_03066}. DOMAIN: The MIU motif (motif interacting with ubiquitin) mediates the interaction with both 'Lys-48'- and 'Lys-63'-linked ubiquitin chains. The UMI motif mediates interaction with ubiquitin with a preference for 'Lys-63'-linked ubiquitin. The specificity for different types of ubiquitin is mediated by juxtaposition of ubiquitin-binding motifs (MIU and UMI motifs) with LR motifs (LRMs). {ECO:0000255|HAMAP-Rule:MF_03066}. +Q925F4 RNF37_MOUSE RING finger protein 37 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase RNF37) (U-box domain-containing protein 5) (UbcM4-interacting protein 5) 539 58,732 Chain (1); Domain (1); Mutagenesis (2); Sequence conflict (1); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: May have a ubiquitin-protein ligase activity acting as an E3 ubiquitin-protein ligase or as a ubiquitin-ubiquitin ligase promoting elongation of ubiquitin chains on substrates. {ECO:0000269|PubMed:11435423}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11435423}. Note=Enriched in nuclear bodies. {ECO:0000250|UniProtKB:O94941}. SUBUNIT: Interacts with UBE2L3. Interacts with VCP. {ECO:0000269|PubMed:11274149, ECO:0000269|PubMed:15189447}. DOMAIN: The U-box domain mediates interaction with E2 ubiquitin ligases and is required for the ubiquitin-protein ligase activity. {ECO:0000250|UniProtKB:O94941, ECO:0000269|PubMed:11435423}. TISSUE SPECIFICITY: Expressed in testis and placenta. {ECO:0000269|PubMed:11274149}. +Q8BGI1 RNF24_MOUSE RING finger protein 24 148 17,254 Chain (1); Transmembrane (1); Zinc finger (1) TRANSMEM 24 44 Helical. {ECO:0000255}. FUNCTION: May play a role in TRPCs intracellular trafficking. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with TRPC1, TRPC3, TRPC4, TRPC5, TRPC6 and TRPC7. {ECO:0000250}. +Q8BUH7 RNF26_MOUSE E3 ubiquitin-protein ligase RNF26 (EC 2.3.2.27) (RING finger protein 26) 424 46,914 Alternative sequence (2); Chain (1); Sequence conflict (4); Transmembrane (5); Zinc finger (1) TRANSMEM 24 44 Helical. {ECO:0000255}.; TRANSMEM 60 80 Helical. {ECO:0000255}.; TRANSMEM 157 177 Helical. {ECO:0000255}.; TRANSMEM 183 203 Helical. {ECO:0000255}.; TRANSMEM 224 244 Helical. {ECO:0000255}. Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that plays a key role in endosome organization by retaining vesicles in the perinuclear cloud. Acts as a platform for perinuclear positioning of the endosomal system by mediating ubiquitination of SQSTM1. Ubiquitinated SQSTM1 attracts specific vesicle-associated adapters, forming a molecular bridge that restrains cognate vesicles in the perinuclear region and organizes the endosomal pathway for efficient cargo transport. Also acts as a regulator of type I interferon production in response to viral infection by mediating the formation of 'Lys-11'-linked polyubiquitin chains on TMEM173/STING, leading to stabilize TMEM173/STING. Also required to limit type I interferon response by promoting autophagic degradation of IRF3. {ECO:0000250|UniProtKB:Q9BY78}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9BY78}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Interacts with INCA1. {ECO:0000250|UniProtKB:Q9BY78}. +Q3U276 SDHF1_MOUSE Succinate dehydrogenase assembly factor 1, mitochondrial (SDH assembly factor 1) (SDHAF1) (LYR motif-containing protein 8) 118 13,142 Chain (1) FUNCTION: Plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Promotes maturation of the iron-sulfur protein subunit Sdhb of the SDH catalytic dimer, protecting it from the deleterious effects of oxidants. May act together with SDHAF3. {ECO:0000250|UniProtKB:A6NFY7}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:A6NFY7}. SUBUNIT: Interacts with Sdhb within an Sdha-Sdhb subcomplex. {ECO:0000250|UniProtKB:Q3E785}. +Q5GAM7 RNS13_MOUSE Probable inactive ribonuclease-like protein 13 153 17,592 Chain (1); Signal peptide (1) FUNCTION: Does not exhibit any ribonuclease activity. {ECO:0000305}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q7TPD3 ROBO2_MOUSE Roundabout homolog 2 1470 161,190 Alternative sequence (2); Chain (1); Disulfide bond (5); Domain (8); Glycosylation (6); Modified residue (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 864 884 Helical. {ECO:0000255}. TOPO_DOM 22 863 Extracellular. {ECO:0000255}.; TOPO_DOM 885 1470 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for SLIT2, and probably SLIT1, which are thought to act as molecular guidance cue in cellular migration, including axonal navigation at the ventral midline of the neural tube and projection of axons to different regions during neuronal development. {ECO:0000269|PubMed:15091338}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Interacts with SLIT2. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in embryonal spinal chord. {ECO:0000269|PubMed:15091338}. +Q9ES07 S15A2_MOUSE Solute carrier family 15 member 2 (Kidney H(+)/peptide cotransporter) (Oligopeptide transporter, kidney isoform) (Peptide transporter 2) 729 81,632 Chain (1); Glycosylation (4); Modified residue (3); Topological domain (13); Transmembrane (12) TRANSMEM 58 78 Helical. {ECO:0000255}.; TRANSMEM 88 108 Helical. {ECO:0000255}.; TRANSMEM 114 134 Helical. {ECO:0000255}.; TRANSMEM 140 160 Helical. {ECO:0000255}.; TRANSMEM 184 204 Helical. {ECO:0000255}.; TRANSMEM 218 238 Helical. {ECO:0000255}.; TRANSMEM 296 316 Helical. {ECO:0000255}.; TRANSMEM 344 364 Helical. {ECO:0000255}.; TRANSMEM 381 401 Helical. {ECO:0000255}.; TRANSMEM 612 632 Helical. {ECO:0000255}.; TRANSMEM 644 664 Helical. {ECO:0000255}.; TRANSMEM 675 695 Helical. {ECO:0000255}. TOPO_DOM 1 57 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 79 87 Extracellular. {ECO:0000305}.; TOPO_DOM 109 113 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 135 139 Extracellular. {ECO:0000305}.; TOPO_DOM 161 183 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 205 217 Extracellular. {ECO:0000305}.; TOPO_DOM 239 295 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 317 343 Extracellular. {ECO:0000305}.; TOPO_DOM 365 380 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 402 611 Extracellular. {ECO:0000305}.; TOPO_DOM 633 643 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 665 674 Extracellular. {ECO:0000305}.; TOPO_DOM 696 729 Cytoplasmic. {ECO:0000305}. FUNCTION: Proton-coupled intake of oligopeptides of 2 to 4 amino acids with a preference for dipeptides (PubMed:11027540). Transports the dipeptide-like aminopeptidase inhibitor bestatin (By similarity). Can also transport the aminocephalosporin antibiotic cefadroxil (By similarity). {ECO:0000250|UniProtKB:P46029, ECO:0000250|UniProtKB:Q63424, ECO:0000269|PubMed:11027540}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:11027540}; Multi-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Expressed in kidney brush border cells (at protein level). {ECO:0000269|PubMed:11027540}. +Q8VCL5 S17A9_MOUSE Solute carrier family 17 member 9 447 48,479 Chain (1); Transmembrane (11) TRANSMEM 40 60 Helical. {ECO:0000255}.; TRANSMEM 74 94 Helical. {ECO:0000255}.; TRANSMEM 103 123 Helical. {ECO:0000255}.; TRANSMEM 129 149 Helical. {ECO:0000255}.; TRANSMEM 169 189 Helical. {ECO:0000255}.; TRANSMEM 192 212 Helical. {ECO:0000255}.; TRANSMEM 252 272 Helical. {ECO:0000255}.; TRANSMEM 287 307 Helical. {ECO:0000255}.; TRANSMEM 327 347 Helical. {ECO:0000255}.; TRANSMEM 380 400 Helical. {ECO:0000255}.; TRANSMEM 413 433 Helical. {ECO:0000255}. FUNCTION: Involved in vesicular storage and exocytosis of ATP. May accumulate ATP and other nucleotides in secretory vesicles such as adrenal chromaffin granules and synaptic vesicles (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: In brain, specifically expressed in the medulla and is associated with chromaffin granules (at protein level). Predominantly expressed in adrenal gland, brain and thyroid. {ECO:0000269|PubMed:18375752}. +Q99N96 RM01_MOUSE 39S ribosomal protein L1, mitochondrial (L1mt) (MRP-L1) 336 37,597 Chain (1); Compositional bias (1); Erroneous initiation (3); Frameshift (1); Modified residue (1); Sequence conflict (6); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. +Q9CQL5 RM18_MOUSE 39S ribosomal protein L18, mitochondrial (L18mt) (MRP-L18) 180 20,677 Chain (1); Sequence conflict (1); Transit peptide (1) FUNCTION: Together with thiosulfate sulfurtransferase (TST), acts as a mitochondrial import factor for the cytosolic 5S rRNA. The precursor form shows RNA chaperone activity; is able to fold the 5S rRNA into an import-competent conformation that is recognized by rhodanese (TST). Both the cytoplasmic and mitochondrial forms are able to bind to the helix IV-loop D in the gamma domain of the 5S rRNA (By similarity). {ECO:0000250|UniProtKB:Q9H0U6}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9H0U6}. SUBUNIT: Component of the mitochondrial ribosome large subunit (39S) which comprises a 16S rRNA and about 50 distinct proteins. {ECO:0000250|UniProtKB:Q9H0U6}. +Q9CQ40 RM49_MOUSE 39S ribosomal protein L49, mitochondrial (L49mt) (MRP-L49) 166 19,133 Chain (1); Sequence conflict (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q13405}. SUBUNIT: Component of the mitochondrial ribosome large subunit (39S) which comprises a 16S rRNA and about 50 distinct proteins (By similarity). Interacts with OXA1L (By similarity). {ECO:0000250|UniProtKB:Q13405, ECO:0000250|UniProtKB:Q5EA71}. +Q9DCI9 RM32_MOUSE 39S ribosomal protein L32, mitochondrial (L32mt) (MRP-L32) (Heart-expressed gene 1 protein) 187 21,733 Chain (1); Erroneous initiation (1); Sequence conflict (1); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9BYC8}. SUBUNIT: Component of the mitochondrial ribosome large subunit (39S) which comprises a 16S rRNA and about 50 distinct proteins. {ECO:0000250|UniProtKB:Q9BYC8}. +Q9CPR5 RM15_MOUSE 39S ribosomal protein L15, mitochondrial (L15mt) (MRP-L15) 295 33,542 Alternative sequence (2); Chain (1); Compositional bias (1); Erroneous initiation (1); Sequence conflict (4); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9P015}. SUBUNIT: Component of the mitochondrial ribosome large subunit (39S) which comprises a 16S rRNA and about 50 distinct proteins. {ECO:0000250|UniProtKB:Q9P015}. +Q8CI78 RMND1_MOUSE Required for meiotic nuclear division protein 1 homolog 450 51,843 Chain (1); Sequence conflict (4); Transit peptide (1) FUNCTION: Required for mitochondrial translation, possibly by coordinating the assembly or maintenance of the mitochondrial ribosome. {ECO:0000250|UniProtKB:Q9NWS8}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9NWS8}. Note=May be localized in mitochondrial RNA granules. {ECO:0000250|UniProtKB:Q9NWS8}. SUBUNIT: Homooligomer. {ECO:0000250|UniProtKB:Q9NWS8}. +O35291 RNAS2_MOUSE Non-secretory ribonuclease (EC 3.1.27.5) (Eosinophil cationic-type ribonuclease 4) (MR-4) (Ribonuclease 2) (RNase 2) 155 17,723 Active site (2); Binding site (1); Chain (1); Disulfide bond (4); Glycosylation (4); Modified residue (1); Region (1); Signal peptide (1) FUNCTION: This is a non-secretory ribonuclease. It is a pyrimidine specific nuclease with a slight preference for U. Cytotoxin and helminthotoxin. Possesses a wide variety of biological activities. SUBCELLULAR LOCATION: Lysosome {ECO:0000305}. Cytoplasmic granule. Note=Matrix of eosinophil's large specific granule. SUBUNIT: Interacts with and forms a tight 1:1 complex with RNH1. Dimerization of two such complexes may occur (By similarity). {ECO:0000250}. +Q99MV7 RNF17_MOUSE RING finger protein 17 (Mad member-interacting protein 2) (Mmip-2) 1640 185,600 Alternative sequence (5); Chain (1); Domain (4); Frameshift (1); Modified residue (2); Sequence conflict (5); Zinc finger (1) FUNCTION: Seems to be involved in regulation of transcriptional activity of MYC. In vitro, inhibits DNA-binding activity of Mad-MAX heterodimers. Can recruit Mad transcriptional repressors (MXD1, MXD3, MXD4 and MXI1) to the cytoplasm. May be involved in spermiogenesis. {ECO:0000269|PubMed:10597267, ECO:0000269|PubMed:11420703}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Predominantly found in the cytoplasm. Component of a nuage in male germ cells (an electron-dense spherical cytoplasmic body present in late pachytene and diplotene spermatocytes and in elonging spermatids). SUBUNIT: Interacts with MXD1, MXD3, MXD4, MXI1 and PIWIL1. Self-associates. {ECO:0000269|PubMed:10597267, ECO:0000269|PubMed:19584108}. TISSUE SPECIFICITY: Expressed at high levels in adult testis. Expressed in male germ cells (at protein level). Expressed at lower levels in adult thyroid, submaxillary gland, ovary and epididymis. {ECO:0000269|PubMed:10597267, ECO:0000269|PubMed:16093322}. +Q9QYM5 RND2_MOUSE Rho-related GTP-binding protein RhoN (Rho family GTPase 2) (Rho-related GTP-binding protein Rho7) (Rnd2) 227 25,399 Chain (1); Lipidation (1); Modified residue (1); Motif (1); Nucleotide binding (3); Propeptide (1) FUNCTION: May be specifically involved in neuronal and hepatic functions. Is a C3 toxin-insensitive member of the Rho subfamily (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Colocalizes with RACGAP1 in Golgi-derived proacrosomal vesicles and the acrosome. {ECO:0000250|UniProtKB:P52198}. SUBUNIT: Interacts with the Rho-GAP domain of RACGAP1. Interacts with UBXD5. Interacts with PRAG1 (By similarity). {ECO:0000250|UniProtKB:P52198, ECO:0000250|UniProtKB:Q5HZE6}. TISSUE SPECIFICITY: Expressed specifically in neurons in the brain and spinal cord and also in hepatic stellate cells. {ECO:0000269|PubMed:10101234}. +Q9Z275 RLBP1_MOUSE Retinaldehyde-binding protein 1 (Cellular retinaldehyde-binding protein) 317 36,408 Binding site (2); Chain (1); Domain (1); Initiator methionine (1); Modified residue (1) FUNCTION: Soluble retinoid carrier essential the proper function of both rod and cone photoreceptors. Participates in the regeneration of active 11-cis-retinol and 11-cis-retinaldehyde, from the inactive 11-trans products of the rhodopsin photocycle and in the de novo synthesis of these retinoids from 11-trans metabolic precursors. The cycling of retinoids between photoreceptor and adjacent pigment epithelium cells is known as the 'visual cycle'. SUBCELLULAR LOCATION: Cytoplasm. TISSUE SPECIFICITY: Retina and pineal gland. +P47955 RLA1_MOUSE 60S acidic ribosomal protein P1 114 11,475 Chain (1); Initiator methionine (1); Modified residue (2) FUNCTION: Plays an important role in the elongation step of protein synthesis. SUBUNIT: Heterodimer with RPLP2 at the lateral ribosomal stalk of the large ribosomal subunit. {ECO:0000250}. +P41438 S19A1_MOUSE Folate transporter 1 (Intestinal folate carrier 1) (IFC-1) (Reduced folate carrier 1) (RFC-1) (RFC1) (Solute carrier family 19 member 1) 512 58,150 Alternative sequence (3); Chain (1); Glycosylation (1); Modified residue (4); Transmembrane (12) TRANSMEM 28 48 Helical. {ECO:0000255}.; TRANSMEM 65 85 Helical. {ECO:0000255}.; TRANSMEM 92 112 Helical. {ECO:0000255}.; TRANSMEM 122 142 Helical. {ECO:0000255}.; TRANSMEM 156 176 Helical. {ECO:0000255}.; TRANSMEM 181 201 Helical. {ECO:0000255}.; TRANSMEM 272 292 Helical. {ECO:0000255}.; TRANSMEM 305 325 Helical. {ECO:0000255}.; TRANSMEM 330 350 Helical. {ECO:0000255}.; TRANSMEM 355 375 Helical. {ECO:0000255}.; TRANSMEM 391 411 Helical. {ECO:0000255}.; TRANSMEM 427 447 Helical. {ECO:0000255}. FUNCTION: Transporter for the intake of folate, reduced folates and methotrexate. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9CY73 RM44_MOUSE 39S ribosomal protein L44, mitochondrial (L44mt) (MRP-L44) (EC 3.1.26.-) 333 37,527 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (2); Sequence conflict (2); Transit peptide (1) FUNCTION: Component of the 39S subunit of mitochondrial ribosome. May have a function in the assembly/stability of nascent mitochondrial polypeptides exiting the ribosome. {ECO:0000250|UniProtKB:Q9H9J2}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9H9J2}. SUBUNIT: Component of the mitochondrial ribosome large subunit (39S) which comprises a 16S rRNA and about 50 distinct proteins. {ECO:0000250|UniProtKB:Q9H9J2}. +Q9D0Q7 RM45_MOUSE 39S ribosomal protein L45, mitochondrial (L45mt) (MRP-L45) 306 35,411 Chain (1); Sequence conflict (1); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9BRJ2}. SUBUNIT: Component of the mitochondrial ribosome large subunit (39S) which comprises a 16S rRNA and about 50 distinct proteins. {ECO:0000250|UniProtKB:Q9BRJ2}. +Q8K2Y7 RM47_MOUSE 39S ribosomal protein L47, mitochondrial (L47mt) (MRP-L47) 252 29,726 Chain (1); Erroneous initiation (1); Modified residue (1); Sequence conflict (1); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9HD33}. SUBUNIT: Component of the mitochondrial ribosome large subunit (39S) which comprises a 16S rRNA and about 50 distinct proteins. {ECO:0000250|UniProtKB:Q9HD33}. +Q9D4G9 RMI1_MOUSE RecQ-mediated genome instability protein 1 616 68,465 Chain (1); Cross-link (2); Modified residue (3); Sequence conflict (5) FUNCTION: Essential component of the RMI complex, a complex that plays an important role in the processing of homologous recombination intermediates to limit DNA crossover formation in cells. Promotes TOP3A binding to double Holliday junctions (DHJ) and hence stimulates TOP3A-mediated dissolution. Required for BLM phosphorylation during mitosis. Within the BLM complex, required for BLM and TOP3A stability (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Forms foci in response to DNA damage. {ECO:0000250}. SUBUNIT: Component of the RMI complex, containing at least TOP3A, RMI1 and RMI2. The RMI complex interacts with BLM. Directly interacts with RMI2 and TOP3A. May bind DHJ. Interacts (via N-terminal region) with BLM; the interaction is direct (By similarity). {ECO:0000250}. +Q8BJA2 S41A1_MOUSE Solute carrier family 41 member 1 512 54,928 Chain (1); Transmembrane (10) TRANSMEM 101 121 Helical. {ECO:0000255}.; TRANSMEM 184 204 Helical. {ECO:0000255}.; TRANSMEM 221 241 Helical. {ECO:0000255}.; TRANSMEM 256 276 Helical. {ECO:0000255}.; TRANSMEM 285 305 Helical. {ECO:0000255}.; TRANSMEM 315 335 Helical. {ECO:0000255}.; TRANSMEM 345 365 Helical. {ECO:0000255}.; TRANSMEM 410 430 Helical. {ECO:0000255}.; TRANSMEM 438 458 Helical. {ECO:0000255}.; TRANSMEM 483 503 Helical. {ECO:0000255}. FUNCTION: Acts as a magnesium transporter that is responsive to magnesium balance. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9DCV4 RMD1_MOUSE Regulator of microtubule dynamics protein 1 (RMD-1) (mRMD-1) (Microtubule-associated protein) (Protein FAM82B) 305 35,000 Chain (1); Modified residue (2); Repeat (2); Sequence conflict (5) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. Note=In interphase localizes in the cytoplasm, and during mitosis localizes to the spindle microtubules and spindle poles. {ECO:0000250}. SUBUNIT: Interacts with microtubules. {ECO:0000250}. +Q9DC26 S46A3_MOUSE Solute carrier family 46 member 3 460 51,383 Chain (1); Glycosylation (3); Signal peptide (1); Topological domain (12); Transmembrane (11) TRANSMEM 74 94 Helical. {ECO:0000255}.; TRANSMEM 112 132 Helical. {ECO:0000255}.; TRANSMEM 136 156 Helical. {ECO:0000255}.; TRANSMEM 171 191 Helical. {ECO:0000255}.; TRANSMEM 196 216 Helical. {ECO:0000255}.; TRANSMEM 258 278 Helical. {ECO:0000255}.; TRANSMEM 302 322 Helical. {ECO:0000255}.; TRANSMEM 325 345 Helical. {ECO:0000255}.; TRANSMEM 348 368 Helical. {ECO:0000255}.; TRANSMEM 382 402 Helical. {ECO:0000255}.; TRANSMEM 411 431 Helical. {ECO:0000255}. TOPO_DOM 26 73 Extracellular. {ECO:0000255}.; TOPO_DOM 95 111 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 133 135 Extracellular. {ECO:0000255}.; TOPO_DOM 157 170 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 192 195 Extracellular. {ECO:0000255}.; TOPO_DOM 217 257 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 279 301 Extracellular. {ECO:0000255}.; TOPO_DOM 323 324 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 346 347 Extracellular. {ECO:0000255}.; TOPO_DOM 369 381 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 403 410 Extracellular. {ECO:0000255}.; TOPO_DOM 432 460 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8CBG9 RN170_MOUSE E3 ubiquitin-protein ligase RNF170 (EC 2.3.2.27) (RING finger protein 170) (RING-type E3 ubiquitin transferase RNF170) 286 33,414 Alternative sequence (7); Chain (1); Mutagenesis (2); Sequence conflict (1); Topological domain (4); Transmembrane (3); Zinc finger (1) TRANSMEM 53 73 Helical. {ECO:0000255}.; TRANSMEM 230 250 Helical. {ECO:0000255}.; TRANSMEM 252 272 Helical. {ECO:0000255}. TOPO_DOM 1 52 Lumenal. {ECO:0000255}.; TOPO_DOM 74 229 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 251 251 Lumenal. {ECO:0000255}.; TOPO_DOM 273 286 Cytoplasmic. {ECO:0000255}. Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that plays an essential role in stimulus-induced inositol 1,4,5-trisphosphate receptor type 1 (ITPR1) ubiquitination and degradation via the endoplasmic reticulum-associated degradation (ERAD) pathway. Also involved in ITPR1 turnover in resting cells. {ECO:0000269|PubMed:21610068}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21610068}; Multi-pass membrane protein {ECO:0000269|PubMed:21610068}. SUBUNIT: Constitutively associated with the ERLIN1/ERLIN 2 complex. Interacts with activated ITPR1. {ECO:0000269|PubMed:21610068}. +Q9D304 RN128_MOUSE E3 ubiquitin-protein ligase RNF128 (EC 2.3.2.27) (Gene related to anergy in lymphocytes protein) (Goliath-related E3 ubiquitin-protein ligase 1) (RING finger protein 128) (RING-type E3 ubiquitin transferase RNF128) 428 46,276 Chain (1); Domain (1); Glycosylation (3); Mutagenesis (2); Sequence conflict (4); Signal peptide (1); Transmembrane (1); Zinc finger (1) TRANSMEM 208 228 Helical. {ECO:0000255}. Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that catalyzes 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains formation. Functions as an inhibitor of cytokine gene transcription. Inhibits IL2 and IL4 transcription, thereby playing an important role in the induction of the anergic phenotype, a long-term stable state of T-lymphocyte unresponsiveness to antigenic stimulation associated with the blockade of interleukin production. Ubiquitinates ARPC5 with 'Lys-48' linkages and COR1A with 'Lys-63' linkages leading to their degradation, down-regulation of these cytosleletal components results in impaired lamellipodium formation and reduced accumulation of F-actin at the immunological synapse. Functions in the patterning of the dorsal ectoderm; sensitizes ectoderm to respond to neural-inducing signals (By similarity). {ECO:0000250, ECO:0000269|PubMed:12435366, ECO:0000269|PubMed:12705856}. PTM: Auto-ubiquitinated. Controls the development of T-cell clonal anergy by ubiquitination. {ECO:0000250|UniProtKB:Q8TEB7}. SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Localized in an asymmetric perinuclear punctate manner. Localizes to the internal pool of the transferrin recycling endosomal pathway. Partially colocalized with the endoplasmic reticulum resident HSPA5, with Golgi resident STX5, and with the late endosomal GTPase RAB7A. {ECO:0000250}. DOMAIN: Binding to E2 ubiquitin-conjugating enzyme requires an intact RING finger domain. {ECO:0000250|UniProtKB:Q8TEB7}. TISSUE SPECIFICITY: Expressed in brain, kidney, heart, liver, ovary, testis and thymus. Expression increased as early as 4 hours by 5- to 7-fold in anergized cultures as compared to resting or activated cells. {ECO:0000269|PubMed:12705856}. +Q8BU88 RM22_MOUSE 39S ribosomal protein L22, mitochondrial (L22mt) (MRP-L22) 206 23,805 Chain (1); Sequence conflict (1); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9NWU5}. SUBUNIT: Component of the mitochondrial ribosome large subunit (39S) which comprises a 16S rRNA and about 50 distinct proteins. {ECO:0000250|UniProtKB:Q9NWU5}. +Q9R1W3 RN103_MOUSE E3 ubiquitin-protein ligase RNF103 (EC 2.3.2.27) (KF-1) (mKF-1) (RING finger protein 103) (RING-type E3 ubiquitin transferase RNF103) (Zinc finger protein 103) (Zfp-103) 683 79,189 Chain (1); Sequence conflict (5); Transmembrane (4); Zinc finger (1) TRANSMEM 6 26 Helical. {ECO:0000255}.; TRANSMEM 326 346 Helical. {ECO:0000255}.; TRANSMEM 366 386 Helical. {ECO:0000255}.; TRANSMEM 411 431 Helical. {ECO:0000255}. Protein modification; protein ubiquitination. FUNCTION: Acts as an E2-dependent E3 ubiquitin-protein ligase, probably involved in the ER-associated protein degradation pathway. {ECO:0000250|UniProtKB:O00237}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O00237}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O00237}. SUBUNIT: Interacts with DERL1 and VCP. {ECO:0000250|UniProtKB:O00237}. TISSUE SPECIFICITY: Highly expressed in the normal cerebellum but not in the cerebral cortex. {ECO:0000269|PubMed:9070305}. +Q8C432 RN182_MOUSE E3 ubiquitin-protein ligase RNF182 (EC 2.3.2.27) (RING finger protein 182) (RING-type E3 ubiquitin transferase RNF182) 247 27,444 Chain (1); Transmembrane (2); Zinc finger (1) TRANSMEM 184 204 Helical. {ECO:0000255}.; TRANSMEM 211 231 Helical. {ECO:0000255}. Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that mediates the ubiquitination of ATP6V0C and targets it to degradation via the ubiquitin-proteasome pathway. {ECO:0000250|UniProtKB:Q8N6D2}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm {ECO:0000250|UniProtKB:Q8N6D2}. SUBUNIT: Interacts with ATP6V0C. {ECO:0000250|UniProtKB:Q8N6D2}. DOMAIN: The RING-type zinc finger domain is required for E3 ligase activity. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the cortex, hippocampus, cerebellum and spinal cord, but not in the heart, liver, kidney or skeletal muscle. {ECO:0000269|PubMed:18298843}. +Q8QZS5 RN183_MOUSE E3 ubiquitin-protein ligase RNF183 (EC 2.3.2.27) 190 21,625 Chain (1); Mutagenesis (2); Topological domain (2); Transmembrane (1); Zinc finger (1) TRANSMEM 160 180 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 1 159 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 181 190 Lumenal. {ECO:0000305}. Protein modification; protein ubiquitination. FUNCTION: Acts as a E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins (PubMed:29300766). Triggers apoptosis in response to prolonged ER stress by mediating the polyubiquitination and subsequent proteasomal degradation of BCL2L1 (By similarity). May collaborate with FATE1 to restrain BIK protein levels thus regulating apoptotic signaling (By similarity). {ECO:0000250|UniProtKB:Q96D59, ECO:0000269|PubMed:29300766}. PTM: Autoubiquitinated (in vitro). {ECO:0000269|PubMed:29300766}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:29300766}; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:Q96D59}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q96D59}. Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:29300766}. Lysosome membrane {ECO:0000269|PubMed:29300766}. SUBUNIT: Interacts with FATE1 (By similarity). Interacts with SEC16A (PubMed:29300766). Interacts with BCL2L1 (By similarity). {ECO:0000250|UniProtKB:Q96D59, ECO:0000269|PubMed:29300766}. TISSUE SPECIFICITY: Highly expressed in the kidney and testis. {ECO:0000269|PubMed:29300766, ECO:0000269|PubMed:29507230}. +Q9D241 RN186_MOUSE E3 ubiquitin-protein ligase RNF186 (EC 2.3.2.27) (RING finger protein 186) 226 24,704 Chain (1); Compositional bias (1); Erroneous initiation (1); Transmembrane (2); Zinc finger (1) TRANSMEM 157 177 Helical. {ECO:0000255}.; TRANSMEM 179 199 Helical. {ECO:0000255}. Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin protein ligase that is part of an apoptotic signaling pathway activated by endoplasmic reticulum stress. In that process, stimulates the expression of proteins specific of the unfolded protein response (UPR), ubiquitinates BNIP1 and regulates its localization to the mitochondrion and induces calcium release from the endoplasmic reticulum that ultimately leads to cell apoptosis. {ECO:0000250|UniProtKB:Q9NXI6}. PTM: Polyubiquitinated. 'Lys-29'-linked autoubiquitination leads to proteasomal degradation. {ECO:0000250|UniProtKB:Q9NXI6}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9NXI6}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Interacts with BNIP1. {ECO:0000250|UniProtKB:Q9NXI6}. DOMAIN: The RING-type domain is required for ubiquitination. {ECO:0000250|UniProtKB:Q9NXI6}. +Q8BG47 RN152_MOUSE E3 ubiquitin-protein ligase RNF152 (EC 2.3.2.27) (RING finger protein 152) (RING-type E3 ubiquitin transferase RNF152) 203 22,353 Chain (1); Region (1); Transmembrane (1); Zinc finger (1) TRANSMEM 167 187 Helical. {ECO:0000255}. Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase mediating 'Lys-63'-linked polyubiquitination of RRAGA in response to amino acid starvation. Thereby, regulates mTORC1 signaling and plays a role in the cellular response to amino acid availability (PubMed:25936802). Also mediates 'Lys-48'-linked polyubiquitination of target proteins and their subsequent targeting to the proteasome for degradation. Induces apoptosis when overexpressed (By similarity). {ECO:0000250|UniProtKB:Q8N8N0, ECO:0000269|PubMed:25936802}. PTM: Ubiquitinated. Autoubiquitinated in vitro, leading to its degradation by the proteasome. {ECO:0000250|UniProtKB:Q8N8N0}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q8N8N0}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8N8N0}. SUBUNIT: Interacts with RRAGA (inactive GDP-bound form); stimulated by amino acid starvation (By similarity). Interacts with SEC16A (PubMed:29300766). {ECO:0000250|UniProtKB:Q8N8N0, ECO:0000269|PubMed:29300766}. +Q05921 RN5A_MOUSE 2-5A-dependent ribonuclease (2-5A-dependent RNase) (EC 3.1.26.-) (Ribonuclease 4) (Ribonuclease L) (RNase L) 735 83,275 Chain (1); Domain (2); Region (3); Repeat (9); Zinc finger (1) FUNCTION: Endoribonuclease that functions in the interferon (IFN) antiviral response. In INF treated and virus infected cells, RNASEL probably mediates its antiviral effects through a combination of direct cleavage of single-stranded viral RNAs, inhibition of protein synthesis through the degradation of rRNA, induction of apoptosis, and induction of other antiviral genes. RNASEL mediated apoptosis is the result of a JNK-dependent stress-response pathway leading to cytochrome c release from mitochondria and caspase-dependent apoptosis. Therefore, activation of RNASEL could lead to elimination of virus infected cells under some circumstances. In the crosstalk between autophagy and apoptosis proposed to induce autophagy as an early stress response to small double-stranded RNA and at later stages of prolonged stress to activate caspase-dependent proteolytic cleavage of BECN1 to terminate autophagy and promote apoptosis. Might play a central role in the regulation of mRNA turnover (By similarity). Cleaves 3' of UpNp dimers, with preference for UU and UA sequences, to sets of discrete products ranging from between 4 and 22 nucleotides in length (By similarity). {ECO:0000250|UniProtKB:Q05823, ECO:0000269|PubMed:11585831}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11585831}. Mitochondrion {ECO:0000269|PubMed:11585831}. SUBUNIT: (Microbial infection) Interacts (via N-terminus) with TMEV leader protein; this interaction prevents RNASEL activation by its substrate 2'-5' oligoadenylates. {ECO:0000269|PubMed:23825954, ECO:0000269|PubMed:29652922}.; SUBUNIT: Monomer (inactive form) or homodimer. Interacts with ABCE1; this interaction inhibits the RNASEL (By similarity). {ECO:0000250}. DOMAIN: The nine ankyrin repeats also called 2-5A sensor constitute the N-terminus 2-5A binding domain.; DOMAIN: The protein kinase domain is predicted to be catalytically inactive. It allows the homodimerization.; DOMAIN: The ribonuclease domain is located in the C-terminus. A single active nuclease domain in a dimer is sufficient for ribonuclease activity. TISSUE SPECIFICITY: Expressed in spleen, thymus, lung, testis, kidney, liver and heart. +E9Q555 RN213_MOUSE E3 ubiquitin-protein ligase RNF213 (EC 2.3.2.27) (EC 3.6.4.-) (Mysterin) (RING finger protein 213) (RING-type E3 ubiquitin transferase RNF213) 5152 584,784 Chain (1); Coiled coil (1); Cross-link (1); Erroneous initiation (1); Modified residue (2); Mutagenesis (1); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase involved in angiogenesis. Involved in the non-canonical Wnt signaling pathway in vascular development: acts by mediating ubiquitination and degradation of FLNA and NFATC2 downstream of RSPO3, leading to inhibit the non-canonical Wnt signaling pathway and promoting vessel regression. Also has ATPase activity. {ECO:0000250|UniProtKB:Q63HN8}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q63HN8}. SUBUNIT: Homooligomer; probably forms homohexamers. {ECO:0000250|UniProtKB:Q63HN8}. +P50247 SAHH_MOUSE Adenosylhomocysteinase (AdoHcyase) (EC 3.3.1.1) (CUBP) (Liver copper-binding protein) (S-adenosyl-L-homocysteine hydrolase) 432 47,688 Beta strand (14); Binding site (5); Chain (1); Helix (23); Initiator methionine (1); Modified residue (3); Region (1); Sequence conflict (1); Turn (5) Amino-acid biosynthesis; L-homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1. FUNCTION: Adenosylhomocysteine is a competitive inhibitor of S-adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine. SUBCELLULAR LOCATION: Cytoplasm. Melanosome {ECO:0000250}. SUBUNIT: Homotetramer. {ECO:0000250}. +Q9CQH8 RPP14_MOUSE Ribonuclease P protein subunit p14 (EC 3.1.26.5) 122 13,565 Chain (1) FUNCTION: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: RNase P consists of an RNA moiety and at least 8 protein subunits; POP1, RPP14, RPP20/POP7, RPP25, RPP29/POP4, RPP30, RPP38 and RPP40. {ECO:0000250}. +Q8R040 RPP21_MOUSE Ribonuclease P protein subunit p21 (RNaseP protein p21) (EC 3.1.26.5) (Ribonucleoprotein V) 150 17,243 Chain (1); Initiator methionine (1); Metal binding (4); Modified residue (1); Sequence conflict (3) FUNCTION: Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. SUBUNIT: RNase P consists of an RNA moiety and at least 9 protein subunits; POP1, RPP14, RPP20/POP7, RPP21, RPP25, RPP29/POP4, RPP30, RPP38 and RPP40. {ECO:0000250}. +Q91WE3 RPP25_MOUSE Ribonuclease P protein subunit p25 (RNase P protein subunit p25) (EC 3.1.26.5) 199 21,038 Chain (1); Modified residue (1) FUNCTION: Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP. This subunit binds to RNA (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of nuclear RNase P and RNase MRP ribonucleoproteins. RNase P consists of an RNA moiety and at least 8 protein subunits; POP1, RPP14, RPP20/POP7, RPP25, RPP29/POP4, RPP30, RPP38 and RPP40. Interacts with the P3 domain of RNase MRP complex. RNase MRP consists of an RNA moiety and at least 9 protein subunits; POP1, RPP14, RPP20/POP7, RPP25, RPP29/POP4, RPP30, RPP38, RPP40, POP5 and RPP21 (By similarity). {ECO:0000250}. +Q9CR08 RPP29_MOUSE Ribonuclease P protein subunit p29 (EC 3.1.26.5) 221 25,637 Chain (1); Modified residue (1) FUNCTION: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. May function with RPP38 to coordinate the nucleolar targeting and/or assembly of RNase P (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. SUBUNIT: Component of nuclear RNase P and RNase MRP ribonucleoproteins. RNase P consists of an RNA moiety and at least 8 protein subunits; POP1, RPP14, RPP20/POP7, RPP25, RPP29/POP4, RPP30, RPP38 and RPP40. RNase MRP consists of an RNA moiety and at least 9 protein subunits; POP1, RPP14, RPP20/POP7, RPP25, RPP29/POP4, RPP30, RPP38, RPP40, POP5 and RPP21. Interacts with RPP25 and POP5 (By similarity). {ECO:0000250}. +O88796 RPP30_MOUSE Ribonuclease P protein subunit p30 (RNaseP protein p30) (EC 3.1.26.5) (RNase P subunit 2) 268 29,473 Chain (1); Initiator methionine (1); Modified residue (2) FUNCTION: Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000305}. +Q80UU2 RPP38_MOUSE Ribonuclease P protein subunit p38 (RNaseP protein p38) (EC 3.1.26.5) 280 31,129 Chain (1); Compositional bias (1); Initiator methionine (1); Modified residue (4); Sequence conflict (4) FUNCTION: Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. RPP38 may associate transiently with RNase P RNA as a factor involved in the transport of H1 RNA to the putative site of its assembly in the cell, the nucleolus (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000305}. SUBUNIT: RNase P consists of an RNA moiety and at least 8 protein subunits; POP1, RPP14, RPP20/POP7, RPP25, RPP29/POP4, RPP30, RPP38 and RPP40. RPP38 is probably a dimer (By similarity). {ECO:0000250}. +Q8R1F9 RPP40_MOUSE Ribonuclease P protein subunit p40 (RNaseP protein p40) (EC 3.1.26.5) 363 41,547 Chain (1); Erroneous initiation (3); Sequence conflict (1) FUNCTION: Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000305}. SUBUNIT: RNase P consists of an RNA moiety and at least 8 protein subunits; POP1, RPP14, RPP20/POP7, RPP25, RPP29/POP4, RPP30, RPP38 and RPP40. {ECO:0000250}. +Q8VDS4 RPR1A_MOUSE Regulation of nuclear pre-mRNA domain-containing protein 1A (Cyclin-dependent kinase inhibitor 2B-related protein) (p15INK4B-related protein) 312 35,701 Chain (1); Coiled coil (1); Domain (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (4) FUNCTION: Interacts with phosphorylated C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit POLR2A, and participates in dephosphorylation of the CTD by RPAP2. May act as a negative regulator of cyclin-D1 (CCND1) and cyclin-E (CCNE1) in the cell cycle. {ECO:0000250|UniProtKB:Q96P16}. SUBUNIT: May form a heterodimer with RPRD1B. Associates with the RNA polymerase II subunit POLR2A (via CTD phosphorylated at 'Ser-2' and 'Ser-7' of the heptad repeats). {ECO:0000250|UniProtKB:Q96P16}. +Q9CSU0 RPR1B_MOUSE Regulation of nuclear pre-mRNA domain-containing protein 1B (Cell cycle-related and expression-elevated protein in tumor) 326 36,884 Alternative sequence (4); Chain (1); Domain (1); Initiator methionine (1); Modified residue (6); Sequence conflict (14) FUNCTION: Interacts with phosphorylated C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit POLR2A, and participates in dephosphorylation of the CTD. Transcriptional regulator which enhances expression of CCND1. Promotes binding of RNA polymerase II to the CCDN1 promoter and to the termination region before the poly-A site but decreases its binding after the poly-A site. Prevents RNA polymerase II from reading through the 3' end termination site and may allow it to be recruited back to the promoter through promotion of the formation of a chromatin loop. Also enhances the transcription of a number of other cell cycle-related genes including CDK2, CDK4, CDK6 and cyclin-E but not CDKN1A, CDKN1B or cyclin-A. Promotes cell proliferation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Associates with the RNA polymerase II complex. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed in the adult with highest levels in liver, colon, prostate and uterus and lowest levels in heart and kidney. Not detected in rectum. {ECO:0000269|PubMed:22264791}. +Q6NXI6 RPRD2_MOUSE Regulation of nuclear pre-mRNA domain-containing protein 2 1469 156,586 Alternative sequence (1); Chain (1); Compositional bias (5); Domain (1); Initiator methionine (1); Modified residue (36); Sequence conflict (2) SUBUNIT: Associates with the RNA polymerase II complex. {ECO:0000250}. +Q3URD2 RPRML_MOUSE Reprimo-like protein 117 12,348 Chain (1); Modified residue (1); Transmembrane (1) TRANSMEM 64 84 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q9JJ72 RPRM_MOUSE Protein reprimo 109 11,820 Chain (1); Glycosylation (2); Modified residue (1); Sequence conflict (1); Transmembrane (1) TRANSMEM 56 76 Helical. {ECO:0000255}. FUNCTION: May be involved in the regulation of p53-dependent G2 arrest of the cell cycle. Seems to induce cell cycle arrest by inhibiting CDK1 activity and nuclear translocation of the CDC2 cyclin B1 complex. {ECO:0000269|PubMed:10930422}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10930422}. Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +P97347 RPTN_MOUSE Repetin 1118 128,619 Calcium binding (2); Chain (1); Domain (2); Region (3); Repeat (48); Sequence conflict (5) FUNCTION: Involved in the cornified cell envelope formation. Multifunctional epidermal matrix protein. PTM: Potential substrate of transglutaminase. Some arginines are probably converted to citrullines by peptidylarginine deimidase. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. DOMAIN: Can be divided into a N-terminal domain with significant homology to S100-like calcium-binding proteins, a central domain containing a series of short tandem repeats, and two flanking segments with low homology to the consensus sequences of the central repeats. {ECO:0000269|PubMed:9268637}. TISSUE SPECIFICITY: Detectable in the stratified internal epithelia of forestomach and tongue and to a lesser degree in normal skin epidermis, where it is restricted to the differentiated suprabasal cell layers. Overexpressed in skin tumors. {ECO:0000269|PubMed:9268637}. +Q8K4Q0 RPTOR_MOUSE Regulatory-associated protein of mTOR (Raptor) (p150 target of rapamycin (TOR)-scaffold protein) 1335 149,471 Alternative sequence (10); Chain (1); Frameshift (1); Modified residue (12); Mutagenesis (2); Repeat (7); Sequence conflict (3) FUNCTION: Involved in the control of the mammalian target of rapamycin complex 1 (mTORC1) activity which regulates cell growth and survival, and autophagy in response to nutrient and hormonal signals; functions as a scaffold for recruiting mTORC1 substrates. mTORC1 is activated in response to growth factors or amino acids. Growth factor-stimulated mTORC1 activation involves a AKT1-mediated phosphorylation of TSC1-TSC2, which leads to the activation of the RHEB GTPase that potently activates the protein kinase activity of mTORC1. Amino acid-signaling to mTORC1 requires its relocalization to the lysosomes mediated by the Ragulator complex and the Rag GTPases. Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. mTORC1 phosphorylates EIF4EBP1 and releases it from inhibiting the elongation initiation factor 4E (eiF4E). mTORC1 phosphorylates and activates S6K1 at 'Thr-389', which then promotes protein synthesis by phosphorylating PDCD4 and targeting it for degradation. Involved in ciliogenesis. {ECO:0000250|UniProtKB:Q8N122}. PTM: Insulin-stimulated phosphorylation at Ser-863 by MTOR and MAPK8 up-regulates mTORC1 activity. Osmotic stress also induces phosphorylation at Ser-696, Thr-706 and Ser-863 by MAPK8. Ser-863 phosphorylation is required for phosphorylation at Ser-855 and Ser-859 (By similarity). In response to nutrient limitation, phosphorylated by AMPK; phosphorylation promotes interaction with 14-3-3 proteins, leading to negative regulation of the mTORC1 complex. In response to growth factors, phosphorylated at Ser-719, Ser-721 and Ser-722 by RPS6KA1, which stimulates mTORC1 activity. {ECO:0000250|UniProtKB:Q8N122, ECO:0000269|PubMed:18439900, ECO:0000269|PubMed:19346248}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Lysosome {ECO:0000250}. Cytoplasmic granule {ECO:0000250|UniProtKB:Q8N122}. Note=Targeting to lysosomes depends on amino acid availability. In arsenite-stressed cells, accumulates in stress granules when associated with SPAG5 and association with lysosomes is drastically decreased. {ECO:0000250}. SUBUNIT: Part of the mammalian target of rapamycin complex 1 (mTORC1) which contains MTOR, MLST8, RPTOR, AKT1S1/PRAS40 and DEPTOR (PubMed:20801936). mTORC1 binds to and is inhibited by FKBP12-rapamycin. Binds directly to 4EBP1 and RPS6KB1 independently of its association with MTOR. Binds preferentially to poorly or non-phosphorylated forms of EIF4EBP1, and this binding is critical to the ability of MTOR to catalyze phosphorylation. Forms a complex with MTOR under both leucine-rich and -poor conditions. Interacts with ULK1 in a nutrient-dependent manner; the interaction is reduced during starvation. Interacts (when phosphorylated by AMPK) with 14-3-3 protein, leading to inhibition of its activity. Interacts with SPAG5; SPAG5 competes with MTOR for RPTOR-binding, resulting in decreased mTORC1 formation. Interacts with WAC; WAC positively regulates MTOR activity by promoting the assembly of the TTT complex composed of TELO2, TTI1 and TTI2 and the RUVBL complex composed of RUVBL1 and RUVBL2 into the TTT-RUVBL complex which leads to the dimerization of the mTORC1 complex and its subsequent activation. Interacts with G3BP1. The complex formed with G3BP1 AND SPAG5 is increased by oxidative stress. Interacts with HTR6. Interacts with PIH1D1. Interacts with LARP1. Interacts with BRAT1. {ECO:0000250|UniProtKB:Q8N122, ECO:0000269|PubMed:20801936}. +Q3UQS8 RBM20_MOUSE RNA-binding protein 20 (RNA-binding motif protein 20) 1199 130,124 Alternative sequence (1); Chain (1); Domain (1); Erroneous initiation (1); Modified residue (11); Sequence conflict (1) FUNCTION: RNA-binding protein that acts as a regulator of mRNA splicing of a subset of genes involved in cardiac development. Regulates splicing of TTN (Titin). {ECO:0000269|PubMed:22466703}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22466703}. TISSUE SPECIFICITY: Predominantly expressed in striated muscle, with highest expression in the heart. In differentiating myoblasts, expression correlates with sarcomere assembly: expression peaks when alpha-actinin is localized mainly in mature Z bodies within the nascent myofiber and expression declines as the sarcomeres continue to mature. +Q8VC70 RBMS2_MOUSE RNA-binding motif, single-stranded-interacting protein 2 383 40,724 Chain (1); Domain (2); Modified residue (3) SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q8BWL5 RBMS3_MOUSE RNA-binding motif, single-stranded-interacting protein 3 431 46,927 Alternative sequence (4); Chain (1); Domain (2); Erroneous initiation (1); Sequence conflict (3) FUNCTION: Binds poly(A) and poly(U) oligoribonucleotides. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +Q8C7Q4 RBM4_MOUSE RNA-binding protein 4 (Lark homolog) (mLark) (RNA-binding motif protein 4) (RNA-binding motif protein 4a) 361 40,046 Alternative sequence (2); Chain (1); Compositional bias (2); Cross-link (1); Domain (2); Frameshift (1); Modified residue (2); Region (1); Sequence conflict (4); Zinc finger (1) FUNCTION: RNA-binding factor involved in multiple aspects of cellular processes like alternative splicing of pre-mRNA and translation regulation. Modulates alternative 5'-splice site and exon selection. Acts as a muscle cell differentiation-promoting factor. Activates exon skipping of the PTB pre-mRNA during muscle cell differentiation. Antagonizes the activity of the splicing factor PTBP1 to modulate muscle cell-specific exon selection of alpha tropomyosin. Binds to intronic pyrimidine-rich sequence of the TPM1 and MAPT pre-mRNAs. Required for the translational activation of PER1 mRNA in response to circadian clock. Binds directly to the 3'-UTR of the PER1 mRNA. Exerts a suppressive activity on Cap-dependent translation via binding to CU-rich responsive elements within the 3'UTR of mRNAs, a process increased under stress conditions or during myocytes differentiation. Recruits EIF4A1 to stimulate IRES-dependent translation initiation in respons to cellular stress. Associates to internal ribosome entry segment (IRES) in target mRNA species under stress conditions. Plays a role for miRNA-guided RNA cleavage and translation suppression by promoting association of AGO2-containing miRNPs with their cognate target mRNAs. Associates with miRNAs during muscle cell differentiation. Binds preferentially to 5'-CGCGCG[GCA]-3' motif in vitro. {ECO:0000269|PubMed:17264215}. PTM: Phosphorylated. Phosphorylated in vitro on Ser-306 by SRPK1. Phosphorylation on Ser-306 is induced upon cell stress signaling, which alters its subcellular localization and may modulate its activity on IRES-mediated mRNA translation (By similarity). Phosphorylated. Phosphorylation on Ser-306 is induced upon cell muscle differentiation. {ECO:0000250, ECO:0000269|PubMed:19801630}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Nucleus speckle {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasmic granule {ECO:0000250}. Note=Undergoes continuous nucleocytoplasmic shuttling. Upon nuclear import colocalizes with SR proteins in nuclear speckles. Arsenite stress-induced phosphorylation increases its subcellular relocalization from the nucleus to the cytoplasm and to cytoplasmic stress granules (SG) via a p38 MAPK signaling pathway. Primarily localized in nucleus and nucleoli under cell growth conditions and accumulated in the cytoplasm and cytoplasm perinuclear granules upon muscle cell differentiation (By similarity). {ECO:0000250}. SUBUNIT: Interacts with TNPO3; the interaction mediates nuclear import of the protein and is disrupted by nuclear Ran bound to GTP. Interacts with EIF4G1 and WT1. Interacts with EIF4A1; the interaction is modulated under stress-induced conditions. Interacts with AGO1. Interacts with AGO2; the interaction occurs under both cell proliferation and differentiation conditions and in an RNA- and phosphorylation-independent manner. Interacts with DDX5; the interaction occurs in an RNA-independent manner (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the suprachiasmatic nucleus (SCN). Expressed in myocytes; expression gradually increases during muscle cell differentiation (at protein level). Expressed in the suprachiasmatic nucleus (SCN). {ECO:0000269|PubMed:17264215, ECO:0000269|PubMed:19801630, ECO:0000269|PubMed:21518792}. +Q9JJT0 RCL1_MOUSE RNA 3'-terminal phosphate cyclase-like protein 373 40,841 Chain (1) FUNCTION: Does not have cyclase activity. Plays a role in 40S-ribosomal-subunit biogenesis in the early pre-rRNA processing steps at sites A0, A1 and A2 that are required for proper maturation of the 18S RNA (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. +O55240 RDH1_MOUSE 11-cis retinol dehydrogenase (11-cis RDH) (11-cis RoDH) (EC 1.1.1.315) (9-cis retinol dehydrogenase) (Cis-retinol dehydrogenase) (Retinol dehydrogenase 5) 318 34,826 Active site (1); Binding site (1); Chain (1); Glycosylation (1); Nucleotide binding (1); Signal peptide (1) Cofactor metabolism; retinol metabolism. FUNCTION: Stereospecific 11-cis retinol dehydrogenase, which catalyzes the final step in the biosynthesis of 11-cis retinaldehyde, the universal chromophore of visual pigments. Also able to oxidize 9-cis-retinol and 13-cis-retinol, but not all-trans-retinol. Active in the presence of NAD as cofactor but not in the presence of NADP. {ECO:0000269|PubMed:10588954, ECO:0000269|PubMed:9539749}. SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q27979}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q27979}. Endoplasmic reticulum lumen {ECO:0000269|PubMed:10739682}. TISSUE SPECIFICITY: Expressed in eye, liver, kidney, brain, intestine, placenta, epididymus and submaxillary gland. In eye, strongly expressed in the retinal pigment epithelium, with lower expression levels detected in the inner segment of the photoreceptor cells and in the outer plexiform layer. In kidney, strong expression detected in the distal tubules and the transitional epithelium in the renal pelvis, with weaker expression detected in the epithelium of the outer stripe of the outer zone of the medulla. In liver, detected in hepatocytes in the centrilobular area. In lung, present in Clara cells in the epithelium of the bronchiole, in parenchyma and in cartilage surrounding the secondary bronchi. In skin, expressed in epidermis, hair follicles and mast cells in the dermis. Expressed in heart (PubMed:10588954 and PubMed:10739682). Not detected in heart (PubMed:9539749). Not detected in lung, spleen, skeletal muscle and testis. {ECO:0000269|PubMed:10588954, ECO:0000269|PubMed:10739682, ECO:0000269|PubMed:9539749, ECO:0000269|PubMed:9654122}. +Q9D7T1 REP15_MOUSE Rab15 effector protein 230 25,854 Chain (1); Frameshift (1); Initiator methionine (1); Lipidation (1); Sequence conflict (2) FUNCTION: Regulates transferrin receptor recycling from the endocytic recycling compartment. {ECO:0000250}. SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000250}. Note=Colocalizes with RAB11 and RAB15 to the endocytic recycling compartment. {ECO:0000250}. SUBUNIT: Interacts with the GTP-bound form of RAB15. {ECO:0000250}. +P35546 RET_MOUSE Proto-oncogene tyrosine-protein kinase receptor Ret (EC 2.7.10.1) (Proto-oncogene c-Ret) [Cleaved into: Soluble RET kinase fragment; Extracellular cell-membrane anchored RET cadherin 120 kDa fragment] 1115 123,874 Active site (1); Alternative sequence (1); Beta strand (1); Binding site (2); Chain (3); Disulfide bond (1); Domain (2); Glycosylation (12); Modified residue (10); Mutagenesis (1); Nucleotide binding (1); Region (1); Sequence conflict (1); Signal peptide (1); Site (2); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 638 659 Helical. {ECO:0000255}. TOPO_DOM 29 637 Extracellular. {ECO:0000255}.; TOPO_DOM 660 1115 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor tyrosine-protein kinase involved in numerous cellular mechanisms including cell proliferation, neuronal navigation, cell migration, and cell differentiation upon binding with glial cell derived neurotrophic factor family ligands. Phosphorylates PTK2/FAK1. Regulates both cell death/survival balance and positional information. Required for the molecular mechanisms orchestration during intestine organogenesis; involved in the development of enteric nervous system and renal organogenesis during embryonic life, and promotes the formation of Peyer's patch-like structures, a major component of the gut-associated lymphoid tissue. Modulates cell adhesion via its cleavage by caspase in sympathetic neurons and mediates cell migration in an integrin (e.g. ITGB1 and ITGB3)-dependent manner. Involved in the development of the neural crest. Active in the absence of ligand, triggering apoptosis through a mechanism that requires receptor intracellular caspase cleavage. Acts as a dependence receptor; in the presence of the ligand GDNF in somatotrophs (within pituitary), promotes survival and down regulates growth hormone (GH) production, but triggers apoptosis in absence of GDNF. Regulates nociceptor survival and size. Triggers the differentiation of rapidly adapting (RA) mechanoreceptors. Mediator of several diseases such as neuroendocrine cancers; these diseases are characterized by aberrant integrins-regulated cell migration. Mediates, through interaction with GDF15-receptor GFRAL, GDF15-induced cell-signaling in the brainstem which induces inhibition of food-intake. Activates MAPK- and AKT-signaling pathways (PubMed:28846099). {ECO:0000269|PubMed:17322904, ECO:0000269|PubMed:20237269, ECO:0000269|PubMed:28846099}. PTM: Autophosphorylated on C-terminal tyrosine residues upon ligand stimulation. Dephosphorylated by PTPRJ on Tyr-906, Tyr-1016 and Tyr-1063 (By similarity). {ECO:0000250|UniProtKB:P07949}.; PTM: Proteolytically cleaved by caspase-3. The soluble RET kinase fragment is able to induce cell death. The extracellular cell-membrane anchored RET cadherin fragment accelerates cell adhesion in sympathetic neurons (By similarity). {ECO:0000250|UniProtKB:P07949}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P07949}; Single-pass type I membrane protein. Endosome membrane {ECO:0000250|UniProtKB:P07949}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P07949}. SUBUNIT: Phosphorylated form interacts with the PBT domain of DOK2, DOK4 and DOK5 (PubMed:11470823). The phosphorylated form interacts with PLCG1 and GRB7 (PubMed:8631863). Interacts (not phosphorylated) with PTK2/FAK1 (via FERM domain) (By similarity). Extracellular cell-membrane anchored RET cadherin fragments form complex in neurons with reduced trophic status, preferentially at the contact sites between somas (By similarity). Interacts with AIP in the pituitary gland; this interaction prevents the formation of the AIP-survivin complex (By similarity). Binds to ARTN (PubMed:17322904). Interacts (inactive) with CBLC and CD2AP; dissociates upon activation by GDNF which increases CBLC:CD2AP interaction (PubMed:18753381). Interacts (via the extracellular domain) with GFRAL (via the extracellular domain); the interaction mediates cellular signaling upon interaction of GFRAL with its ligand GDF15 (PubMed:28846099). Interaction with GFRAL requires previous GDF15-binding to GFRAL (PubMed:28846099). {ECO:0000250|UniProtKB:P07949, ECO:0000269|PubMed:11470823, ECO:0000269|PubMed:17322904, ECO:0000269|PubMed:18753381, ECO:0000269|PubMed:28846099, ECO:0000269|PubMed:8631863}. TISSUE SPECIFICITY: Expressed in peripheral nerve cells, hematopoietic cells and podocytes (PubMed:18753381). Expressed in the brainstem, restricted to cells in the area postrema and the immediately adjacent region of the nucleus tractus solitarius (PubMed:28953886). {ECO:0000269|PubMed:18753381, ECO:0000269|PubMed:28953886}. +P20664 PRI1_MOUSE DNA primase small subunit (EC 2.7.7.-) (DNA primase 49 kDa subunit) (p49) 417 49,295 Active site (3); Chain (1); Modified residue (1); Motif (1); Sequence conflict (1) FUNCTION: DNA primase is the polymerase that synthesizes small RNA primers for the Okazaki fragments made during discontinuous DNA replication. SUBUNIT: Heterodimer of a small subunit and a large subunit. +O35181 NRG3_MOUSE Pro-neuregulin-3, membrane-bound isoform (Pro-NRG3) [Cleaved into: Neuregulin-3 (NRG-3)] 713 77,370 Chain (2); Compositional bias (7); Disulfide bond (3); Domain (1); Topological domain (2); Transmembrane (1) TRANSMEM 363 383 Helical; Note=Internal signal sequence. {ECO:0000255}. TOPO_DOM 1 362 Extracellular. {ECO:0000255}.; TOPO_DOM 384 713 Cytoplasmic. {ECO:0000255}. FUNCTION: Direct ligand for the ERBB4 tyrosine kinase receptor. Binding results in ligand-stimulated tyrosine phosphorylation and activation of the receptor. Does not bind to the EGF receptor, ERBB2 or ERBB3 receptors. {ECO:0000269|PubMed:9275162}. PTM: Proteolytic cleavage close to the plasma membrane on the external face leads to the release of the soluble growth factor form. {ECO:0000250}.; PTM: Extensive glycosylation precedes the proteolytic cleavage. {ECO:0000250}. SUBCELLULAR LOCATION: Pro-neuregulin-3, membrane-bound isoform: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Does not seem to be active. {ECO:0000250}.; SUBCELLULAR LOCATION: Neuregulin-3: Secreted {ECO:0000250}. SUBUNIT: Interacts with ERBB4. {ECO:0000269|PubMed:9275162}. DOMAIN: The cytoplasmic domain may be involved in the regulation of trafficking and proteolytic processing. Regulation of the proteolytic processing involves initial intracellular domain dimerization (By similarity). {ECO:0000250}.; DOMAIN: ERBB receptor binding is elicited entirely by the EGF-like domain. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in sympathetic, motor, and sensory neurons. +Q9WTX4 NRG4_MOUSE Pro-neuregulin-4, membrane-bound isoform (Pro-NRG4) [Cleaved into: Neuregulin-4 (NRG-4)] 115 12,744 Chain (2); Disulfide bond (3); Domain (1); Glycosylation (2); Topological domain (2); Transmembrane (1) TRANSMEM 63 83 Helical; Note=Internal signal sequence. {ECO:0000255}. TOPO_DOM 1 62 Extracellular. {ECO:0000255}.; TOPO_DOM 84 115 Cytoplasmic. {ECO:0000255}. FUNCTION: Low affinity ligand for the ERBB4 tyrosine kinase receptor. Concomitantly recruits ERBB1 and ERBB2 coreceptors, resulting in ligand-stimulated tyrosine phosphorylation and activation of the ERBB receptors. Does not bind to the ERBB1, ERBB2 and ERBB3 receptors. {ECO:0000269|PubMed:10348342}. PTM: Proteolytic cleavage close to the plasma membrane on the external face leads to the release of the soluble growth factor form. {ECO:0000250}.; PTM: Extensive glycosylation precedes the proteolytic cleavage. {ECO:0000250}. SUBCELLULAR LOCATION: Pro-neuregulin-4, membrane-bound isoform: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Does not seem to be active. {ECO:0000250}.; SUBCELLULAR LOCATION: Neuregulin-4: Secreted {ECO:0000250}. SUBUNIT: Interacts with ERBB4. {ECO:0000269|PubMed:10348342}. DOMAIN: The cytoplasmic domain may be involved in the regulation of trafficking and proteolytic processing. Regulation of the proteolytic processing involves initial intracellular domain dimerization (By similarity). {ECO:0000250}.; DOMAIN: ERBB receptor binding is elicited entirely by the EGF-like domain. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in pancreas; weakly expressed in muscle. +Q923B3 NRIF1_MOUSE Neurotrophin receptor-interacting factor 1 (Neurotrophin receptor-interacting factor) (Zinc finger protein 110) 828 93,650 Chain (1); Cross-link (1); Domain (3); Erroneous initiation (2); Mutagenesis (1); Sequence conflict (6); Zinc finger (5) FUNCTION: Transcription regulator involved in NGFR/p75(NTR)-mediated apoptosis. Essential component of the NGFR/p75(NTR) apoptotic pathway: upon ligand-binding and subsequent cleavage of NGFR/p75(NTR), binds to the intracellular domain (ICD) cleavage product of NGFR/p75(NTR), translocates to the nucleus and induces apoptosis, possibly by regulating expression of key regulators of apoptosis. Induces NGFR/p75(NTR)-mediated apoptosis in retina and sympathetic neurons. May also regulate expression of neuronal cholesterol biosynthesis genes. Probably acts as a transcription repressor: specifically binds to the 3'-end of zinc-finger coding genes and recruiting chromatin-modifying proteins such as SETDB1 and TRIM28/KAP1, leading to transcription repression. {ECO:0000269|PubMed:10545116, ECO:0000269|PubMed:15668238, ECO:0000269|PubMed:16630834, ECO:0000269|PubMed:18677445, ECO:0000269|PubMed:18815271}. PTM: Ubiquitinated by TRAF6 at Lys-15 through 'Lys-63'-linked polyubiquitination. 'Lys-63'-linked polyubiquitination occurs in response to NGFR/p75(NTR) cleavage by gamma-secretase and promotes binding with the ICD cleavage product of NGFR/p75(NTR), followed by translocation into the nucleus and subsequent apoptosis. {ECO:0000269|PubMed:16252010, ECO:0000269|PubMed:16630834}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Translocates into the nucleus following binding to TRAF6 and subsequent ubiquitination at Lys-15. SUBUNIT: Interacts with NGFR/p75(NTR). Interacts (via KRAB 1 domain) with TRAF6. Interacts (when ubiquitinated at Lys-15) with SQSTM1/p62. {ECO:0000269|PubMed:10545116, ECO:0000269|PubMed:14960584, ECO:0000269|PubMed:16252010, ECO:0000269|PubMed:16630834, ECO:0000269|PubMed:18815271}. TISSUE SPECIFICITY: Ubiquitously expressed at low level. Expressed at higher level in testis. +O35375 NRP2_MOUSE Neuropilin-2 (Vascular endothelial cell growth factor 165 receptor 2) 931 104,631 Alternative sequence (5); Chain (1); Compositional bias (1); Disulfide bond (6); Domain (5); Glycosylation (4); Metal binding (3); Sequence conflict (9); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 865 889 Helical. {ECO:0000255}. TOPO_DOM 21 864 Extracellular. {ECO:0000255}.; TOPO_DOM 890 931 Cytoplasmic. {ECO:0000255}. FUNCTION: High affinity receptor for semaphorins 3C, 3F, VEGF-165 and VEGF-145 isoforms of VEGF, and the PLGF-2 isoform of PGF. SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:O60462}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:O60462}. SUBUNIT: Heterodimer with NRP1. Binds PLXNB1 (By similarity). {ECO:0000250}. DOMAIN: The tandem CUB domains mediate binding to semaphorin, while the tandem F5/8 domains are responsible for heparin and VEGF binding. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in developing CNS, PNS and in some nonneural tissues including limb buds, developing bones, muscles, intestinal epithelium, kidney, lung and submandibular gland. +P97463 NRTN_MOUSE Neurturin 195 22,219 Chain (1); Disulfide bond (4); Propeptide (1); Signal peptide (1) FUNCTION: Supports the survival of sympathetic neurons in culture. May regulate the development and maintenance of the CNS. Might control the size of non-neuronal cell population such as haemopoietic cells. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Homodimer; disulfide-linked. TISSUE SPECIFICITY: Widespread distribution. +Q9CR47 NSA2_MOUSE Ribosome biogenesis protein NSA2 homolog (L-name-related protein 42) (LNR42) (TGF-beta-inducible nuclear protein 1) 260 30,036 Chain (1); Compositional bias (1); Cross-link (1); Frameshift (1); Modified residue (1); Motif (1); Sequence conflict (4) FUNCTION: Involved in the biogenesis of the 60S ribosomal subunit. May play a part in the quality control of pre-60S particles (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. SUBUNIT: Component of the pre-66S ribosomal particle. {ECO:0000250}. +Q91VT1 NSE2_MOUSE E3 SUMO-protein ligase NSE2 (EC 2.3.2.-) (E3 SUMO-protein transferase NSE2) (MMS21 homolog) (Non-structural maintenance of chromosomes element 2 homolog) (Non-SMC element 2 homolog) 247 28,231 Alternative sequence (1); Chain (1); Cross-link (4); Modified residue (2); Sequence conflict (1); Zinc finger (1) Protein modification; protein sumoylation. FUNCTION: E3 SUMO-protein ligase component of the SMC5-SMC6 complex, a complex involved in repair of DNA double-strand breaks by homologous recombination. Is not be required for the stability of the complex. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The complex is required for telomere maintenance via recombination and mediates sumoylation of shelterin complex (telosome) components. Acts as an E3 ligase mediating SUMO attachment to various proteins such as SMC6L1 and TRAX, the shelterin complex subunits TERF1, TERF2, TINF2 and TERF2IP, and maybe the cohesin components RAD21 and STAG2. Required for recruitment of telomeres to PML nuclear bodies. SUMO protein-ligase activity is required for the prevention of DNA damage-induced apoptosis by facilitating DNA repair. Required for sister chromatid cohesion during prometaphase and mitotic progression (By similarity). {ECO:0000250}. PTM: Sumoylated, possibly via autosumoylation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96MF7}. Chromosome, telomere {ECO:0000250|UniProtKB:Q96MF7}. SUBUNIT: Component of the SMC5-SMC6 complex which consists at least of SMC5, SMC6, NSMCE2, NSMCE1, NSMCE4A or EID3 and NSMCE3. {ECO:0000250}. +O88491 NSD1_MOUSE Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific (EC 2.1.1.43) (H3-K36-HMTase) (H4-K20-HMTase) (Nuclear receptor-binding SET domain-containing protein 1) (NR-binding SET domain-containing protein) 2588 284,084 Beta strand (6); Binding site (2); Chain (1); Compositional bias (2); Cross-link (3); Domain (4); Helix (1); Modified residue (8); Mutagenesis (5); Region (4); Turn (6); Zinc finger (4) FUNCTION: Histone methyltransferase. Preferentially methylates 'Lys-36' of histone H3 and 'Lys-20' of histone H4 (in vitro). Transcriptional intermediary factor capable of negatively influencing transcription. May also positively influence transcription. Essential for early post-implantation development. {ECO:0000269|PubMed:12805229, ECO:0000269|PubMed:9628876}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9628876}. Chromosome {ECO:0000305|PubMed:9628876}. SUBUNIT: Interacts with AR DNA- and ligand-binding domains (By similarity). Interacts with the ligand-binding domains of RARA and THRA in the absence of ligand; in the presence of ligand the interaction is severely disrupted but some binding still occurs. Interacts with the ligand-binding domains of RXRA and ESRRA only in the presence of ligand. Interacts with ZNF496. {ECO:0000250, ECO:0000269|PubMed:15169884, ECO:0000269|PubMed:9628876}. DOMAIN: Contains 2 adjacent but distinct nuclear receptor interaction domains (NID+L and NID-L) to which nuclear receptors bind differentially in the presence and absence of ligand respectively. TISSUE SPECIFICITY: Expressed in the embryo and the outer region of the uterine decidua at early post-implantation E5.5 stage. Uniformly expressed in embryonic and extraembryonic tissues during gastrulation stage E7.5. Expressed differentially after stage 14.5 with highest expression in proliferating cells. Enriched in the telencephalic region of the brain, spinal cord, intestinal crypt, tooth buds, thymus and salivary glands at stage E16.5. Also expressed in the ossification region of developing bones and in the periosteum. {ECO:0000269|PubMed:12805229}. +Q8BVE8 NSD2_MOUSE Histone-lysine N-methyltransferase NSD2 (EC 2.1.1.43) (Multiple myeloma SET domain-containing protein) (MMSET) (Nuclear SET domain-containing protein 2) (Wolf-Hirschhorn syndrome candidate 1 protein homolog) 1365 152,253 Alternative sequence (4); Chain (1); DNA binding (1); Domain (5); Erroneous initiation (1); Frameshift (1); Modified residue (6); Mutagenesis (2); Sequence caution (1); Sequence conflict (3); Zinc finger (4) FUNCTION: Histone methyltransferase with histone H3 'Lys-27' (H3K27me) methyltransferase activity. {ECO:0000269|PubMed:18172012}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}. Chromosome {ECO:0000250}. TISSUE SPECIFICITY: Expressed preferentially in rapidly growing embryonic tissues. {ECO:0000269|PubMed:9618163}. +Q9JIY8 NT8F3_MOUSE N-acetyltransferase family 8 member 3 (EC 2.3.1.48) (Camello-like protein 3) (N-acetyltransferase CML3) 226 25,956 Chain (1); Domain (1); Sequence conflict (6); Transmembrane (2) TRANSMEM 36 56 Helical. {ECO:0000255}.; TRANSMEM 58 78 Helical. {ECO:0000255}. FUNCTION: Has histone acetyltransferase activity in vitro, with specificity for histone H4. {ECO:0000269|PubMed:25123547}. SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000305|PubMed:25123547}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000305|PubMed:25123547}. Cytoplasm {ECO:0000305|PubMed:25123547}. Note=C-terminally tagged constructs localize to the nuclear membrane and perinuclear region. N-terminally tagged constructs show a punctate cytoplasmic distribution. {ECO:0000269|PubMed:25123547}. +P03903 NU4LM_MOUSE NADH-ubiquinone oxidoreductase chain 4L (EC 7.1.1.2) (NADH dehydrogenase subunit 4L) 98 10,607 Chain (1); Helix (6); Sequence conflict (2); Transmembrane (3); Turn (1) TRANSMEM 2 22 Helical. {ECO:0000255}.; TRANSMEM 26 46 Helical. {ECO:0000255}.; TRANSMEM 58 79 Helical. {ECO:0000255}. FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q4FZG9 NUA4L_MOUSE NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 4-like 2 87 10,046 Chain (1) +Q9Z2U1 PSA5_MOUSE Proteasome subunit alpha type-5 (EC 3.4.25.1) (Macropain zeta chain) (Multicatalytic endopeptidase complex zeta chain) (Proteasome zeta chain) 241 26,411 Beta strand (12); Chain (1); Glycosylation (1); Helix (7); Modified residue (5); Turn (2) FUNCTION: Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). {ECO:0000269|PubMed:16581775, ECO:0000269|PubMed:22341445}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P28066}. Nucleus {ECO:0000250|UniProtKB:P28066}. SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is a barrel-shaped complex made of 28 subunits that are arranged in four stacked rings. The two outer rings are each formed by seven alpha subunits, and the two inner rings are formed by seven beta subunits. The proteolytic activity is exerted by three beta-subunits PSMB5, PSMB6 and PSMB7 (PubMed:16857966, PubMed:22341445). PSMA5 interacts directly with the PSMG1-PSMG2 heterodimer which promotes 20S proteasome assembly (By similarity). {ECO:0000250|UniProtKB:P28066, ECO:0000269|PubMed:16857966, ECO:0000269|PubMed:22341445}. TISSUE SPECIFICITY: Detected in liver (at protein level). {ECO:0000269|PubMed:22341445}. +Q63850 NUP62_MOUSE Nuclear pore glycoprotein p62 (62 kDa nucleoporin) (Nucleoporin Nup62) 526 53,255 Chain (1); Coiled coil (1); Compositional bias (4); Disulfide bond (2); Glycosylation (2); Initiator methionine (1); Modified residue (3); Mutagenesis (2); Region (2); Repeat (5); Sequence conflict (2) FUNCTION: Essential component of the nuclear pore complex. The N-terminal is probably involved in nucleocytoplasmic transport. The C-terminal is involved in protein-protein interaction probably via coiled-coil formation, promotes its association with centrosomes and may function in anchorage of p62 to the pore complex. Plays a role in mitotic cell cycle progression by regulating centrosome segregation, centriole maturation and spindle orientation. It might be involved in protein recruitment to the centrosome after nuclear breakdown. {ECO:0000250|UniProtKB:P37198}. PTM: O-glycosylated. {ECO:0000303|PubMed:1915419}.; PTM: The inner channel of the NPC has a different redox environment from the cytoplasm and allows the formation of interchain disulfide bonds between some nucleoporins, the significant increase of these linkages upon oxidative stress reduces the permeability of the NPC. SUBCELLULAR LOCATION: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P37198}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:P37198}. Nucleus envelope {ECO:0000250|UniProtKB:P37198}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P37198}. Note=Central region of the nuclear pore, within the transporter. During mitotic cell division, it associates with the poles of the mitotic spindle. {ECO:0000250|UniProtKB:P37198}. SUBUNIT: Component of the p62 complex, a complex at least composed of NUP62, NUP54, and NUP58. Interacts with NUTF2. Interacts with HIKESHI. Interacts with OSBPL8. Interacts with CAPG. Interacts with SAS6 and TUBG1 at the centrosome. {ECO:0000250|UniProtKB:P17955, ECO:0000250|UniProtKB:P37198}. DOMAIN: Contains FG repeats. +Q9JIH2 NUP50_MOUSE Nuclear pore complex protein Nup50 (50 kDa nucleoporin) (Nuclear pore-associated protein 60 kDa-like) (Nucleoporin Nup50) 466 49,485 Chain (1); Compositional bias (2); Cross-link (1); Domain (1); Helix (1); Modified residue (10); Region (2); Repeat (5); Sequence conflict (8); Turn (1) FUNCTION: Component of the nuclear pore complex that has a direct role in nuclear protein import (PubMed:10811608). Actively displaces NLSs from importin-alpha, and facilitates disassembly of the importin-alpha:beta-cargo complex and importin recycling (PubMed:16222336). Interacts with regulatory proteins of cell cycle progression including CDKN1B (PubMed:10891500, PubMed:10811608). This interaction is required for correct intracellular transport and degradation of CDKN1B (PubMed:10811608). {ECO:0000269|PubMed:10811608, ECO:0000269|PubMed:10891500, ECO:0000269|PubMed:16222336}. SUBCELLULAR LOCATION: Nucleus, nuclear pore complex. Nucleus membrane {ECO:0000250|UniProtKB:O08587}; Peripheral membrane protein {ECO:0000250|UniProtKB:O08587}; Nucleoplasmic side {ECO:0000250|UniProtKB:O08587}. Note=Localizes to the nucleoplasmic fibrils of the nuclear pore complex. Dissociates from the NPC structure early during prophase of mitosis. Associates with the newly formed nuclear membrane during telophase. In the testis, the localization changes during germ cell differentiation from the nuclear surface in spermatocytes to the whole nucleus (interior) in spermatids and back to the nuclear surface in spermatozoa. {ECO:0000250|UniProtKB:O08587, ECO:0000250|UniProtKB:Q9UKX7}. SUBUNIT: Does not interact with TPR (By similarity). Interacts with Importin alpha-2, Importin beta, Importin beta-2, NUP153, Ran binding protein 7, CDKN1B and itself. {ECO:0000250, ECO:0000269|PubMed:16222336}. DOMAIN: Contains FG repeats. FG repeats are interaction sites for karyopherins (importins, exportins) and form probably an affinity gradient, guiding the transport proteins unidirectionally with their cargo through the NPC. FG repeat regions are highly flexible and lack ordered secondary structure. The overall conservation of FG repeats regarding exact sequence, spacing, and repeat unit length is limited. {ECO:0000305}. TISSUE SPECIFICITY: Widely expressed at low levels. Highest in the developing neural tube and adult testes. +Q9DC50 OCTC_MOUSE Peroxisomal carnitine O-octanoyltransferase (COT) (EC 2.3.1.137) 612 70,264 Active site (1); Beta strand (18); Binding site (4); Chain (1); Compositional bias (1); Helix (27); Modified residue (5); Motif (1); Mutagenesis (4); Region (1); Sequence conflict (1); Turn (5) Lipid metabolism; fatty acid beta-oxidation. FUNCTION: Beta-oxidation of fatty acids. The highest activity concerns the C6 to C10 chain length substrate. {ECO:0000269|PubMed:15492013}. SUBCELLULAR LOCATION: Peroxisome {ECO:0000305}. +Q8BZ09 ODC_MOUSE Mitochondrial 2-oxodicarboxylate carrier (Solute carrier family 25 member 21) 298 33,229 Chain (1); Repeat (3); Sequence conflict (1); Transmembrane (6) TRANSMEM 16 36 Helical; Name=1. {ECO:0000255}.; TRANSMEM 69 88 Helical; Name=2. {ECO:0000255}.; TRANSMEM 112 132 Helical; Name=3. {ECO:0000255}.; TRANSMEM 166 186 Helical; Name=4. {ECO:0000255}.; TRANSMEM 204 224 Helical; Name=5. {ECO:0000255}.; TRANSMEM 276 296 Helical; Name=6. {ECO:0000255}. FUNCTION: Transports C5-C7 oxodicarboxylates across the inner membranes of mitochondria. Can transport 2-oxoadipate, 2-oxoglutarate, adipate, glutarate, and to a lesser extent, pimelate, 2-oxopimelate, 2-aminoadipate, oxaloacetate, and citrate (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q810P2 OD3L1_MOUSE Outer dense fiber protein 3-like protein 1 275 31,064 Chain (1); Repeat (2) +Q3TZ65 OD3L2_MOUSE Outer dense fiber protein 3-like protein 2 277 29,757 Chain (1); Compositional bias (1); Repeat (3) +Q9D478 ODF2L_MOUSE Protein BCAP (Basal body centriole-associated protein) (Outer dense fiber protein 2-like) 642 74,151 Alternative sequence (2); Chain (1); Coiled coil (3); Sequence conflict (1) FUNCTION: Acts as a suppressor of ciliogenesis, specifically, the initiation of ciliogenesis. {ECO:0000269|PubMed:28775150}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9ULJ1}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q9ULJ1}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000250|UniProtKB:Q9ULJ1}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q9ULJ1}. Note=Localizes to centrioles in proliferative cells and basal bodies in ciliated cells. Disappears during ciliogenesis but reappears, albeit at a lower levels once ciliogenesis has completed. {ECO:0000250|UniProtKB:Q9ULJ1}. +Q61999 ODFP1_MOUSE Outer dense fiber protein 1 247 27,539 Chain (1); Modified residue (10); Region (2); Repeat (2) FUNCTION: Component of the outer dense fibers (ODF) of spermatozoa. ODF are filamentous structures located on the outside of the axoneme in the midpiece and principal piece of the mammalian sperm tail and may help to maintain the passive elastic structures and elastic recoil of the sperm tail. SUBUNIT: Interact (via leucine zipper motif) with TCP11 (By similarity). Interacts with SPAG4 (By similarity). Interacts with KLC3 (By similarity). {ECO:0000250|UniProtKB:P21769, ECO:0000250|UniProtKB:Q14990}. DOMAIN: The C-terminal contains many C-X-P repeats. +P18894 OXDA_MOUSE D-amino-acid oxidase (DAAO) (DAMOX) (DAO) (EC 1.4.3.3) 345 38,661 Binding site (8); Chain (1); Motif (1); Natural variant (1); Nucleotide binding (5); Sequence conflict (7) FUNCTION: Regulates the level of the neuromodulator D-serine in the brain. Has high activity towards D-DOPA and contributes to dopamine synthesis. Could act as a detoxifying agent which removes D-amino acids accumulated during aging. Acts on a variety of D-amino acids with a preference for those having small hydrophobic side chains followed by those bearing polar, aromatic, and basic groups. Does not act on acidic amino acids. SUBCELLULAR LOCATION: Peroxisome. SUBUNIT: Homodimer. {ECO:0000250}. +Q8C165 P20D1_MOUSE N-fatty-acyl-amino acid synthase/hydrolase PM20D1 (EC 3.5.1.-) (EC 4.3.-.-) (Peptidase M20 domain-containing protein 1) 503 55,663 Active site (2); Chain (1); Glycosylation (2); Metal binding (6); Mutagenesis (3); Sequence conflict (1); Signal peptide (1) FUNCTION: Bidirectional N-fatty-acyl amino acid synthase/hydrolase that regulates the production of N-fatty-acyl amino acids. These metabolites are endogenous chemical uncouplers of mitochondrial respiration. In an UCP1-independent manner, maybe through interaction with mitochondrial transporters, they promote proton leakage into the mitochondrial matrix. Thereby, this secreted protein may indirectly regulate the bodily dissipation of chemical energy as heat through thermogenic respiration. {ECO:0000269|PubMed:27374330}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:27374330}. TISSUE SPECIFICITY: Detected in blood (at protein level). Widely expressed with higher expression in kidney, liver and brown adipose tissues. {ECO:0000269|PubMed:27374330}. +Q9D2F7 P210L_MOUSE Nuclear pore membrane glycoprotein 210-like (Nucleoporin 210 kDa-like) (Nucleoporin Nup210-like) 1881 208,700 Chain (1); Domain (1); Frameshift (1); Glycosylation (4); Sequence conflict (2); Signal peptide (1); Transmembrane (1) TRANSMEM 1804 1824 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q8R143 PTTG_MOUSE Pituitary tumor-transforming gene 1 protein-interacting protein (Pituitary tumor-transforming gene protein-binding factor) (PBF) (PTTG-binding factor) 174 19,965 Chain (1); Coiled coil (1); Domain (1); Glycosylation (2); Modified residue (1); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 94 114 Helical. {ECO:0000255}. TOPO_DOM 30 93 Extracellular. {ECO:0000255}.; TOPO_DOM 115 174 Cytoplasmic. {ECO:0000255}. FUNCTION: May facilitate PTTG1 nuclear translocation. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=May be cytoplasmic and nuclear. {ECO:0000250}. SUBUNIT: Interacts with PTTG1. {ECO:0000250}. +Q6RUU0 PTX4_MOUSE Pentraxin-4 478 53,150 Alternative sequence (2); Chain (1); Disulfide bond (1); Domain (1); Frameshift (1); Glycosylation (1); Metal binding (7); Sequence conflict (11); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Expressed in liver (at protein level). Widely expressed at low levels with highest levels in liver. {ECO:0000269|PubMed:20357257}. +O54803 P2RX6_MOUSE P2X purinoceptor 6 (P2X6) (ATP receptor) (P2XM) (Purinergic receptor) (Purinergic receptor P2X-like 1) 389 43,099 Chain (1); Disulfide bond (5); Erroneous initiation (2); Glycosylation (3); Sequence conflict (1); Topological domain (3); Transmembrane (2) TRANSMEM 46 66 Helical; Name=1. {ECO:0000255}.; TRANSMEM 336 356 Helical; Name=2. {ECO:0000255}. TOPO_DOM 1 45 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 67 335 Extracellular. {ECO:0000255}.; TOPO_DOM 357 389 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for ATP that acts as a ligand-gated ion channel. {ECO:0000250}. PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SUBUNIT: Unlike most P2XRs, P2RX6 does not seem to form homotrimers or heterotrimers. {ECO:0000250}. TISSUE SPECIFICITY: Predominantly expressed in skeletal muscle. Also expressed in lung. +Q9CPV9 P2Y12_MOUSE P2Y purinoceptor 12 (P2Y12) 347 39,474 Binding site (7); Chain (1); Disulfide bond (2); Glycosylation (2); Modified residue (2); Nucleotide binding (3); Topological domain (8); Transmembrane (7) TRANSMEM 34 56 Helical; Name=1. {ECO:0000250}.; TRANSMEM 68 88 Helical; Name=2. {ECO:0000250}.; TRANSMEM 104 124 Helical; Name=3. {ECO:0000250}.; TRANSMEM 149 168 Helical; Name=4. {ECO:0000250}.; TRANSMEM 192 213 Helical; Name=5. {ECO:0000250}.; TRANSMEM 240 265 Helical; Name=6. {ECO:0000250}.; TRANSMEM 285 304 Helical; Name=7. {ECO:0000250}. TOPO_DOM 1 33 Extracellular. {ECO:0000250}.; TOPO_DOM 57 67 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 89 103 Extracellular. {ECO:0000250}.; TOPO_DOM 125 148 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 169 191 Extracellular. {ECO:0000250}.; TOPO_DOM 214 239 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 266 284 Extracellular. {ECO:0000250}.; TOPO_DOM 305 347 Cytoplasmic. {ECO:0000250}. FUNCTION: Receptor for ADP and ATP coupled to G-proteins that inhibit the adenylyl cyclase second messenger system. Required for normal platelet aggregation and blood coagulation. {ECO:0000269|PubMed:12897207}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. DOMAIN: The transmembrane domain is composed of seven transmembrane helices; most of these are not strictly perpendicular to the plane of the membrane, but are tilted and/or kinked. Agonist binding promotes a conformation change in the extracellular loops that leads to an inward movement of the transmembrane helices. Antagonists can bind to an overlapping site, but block the inward movement of the transmembrane helices (By similarity). {ECO:0000250}. +Q9Z1M0 P2RX7_MOUSE P2X purinoceptor 7 (P2X7) (ATP receptor) (P2Z receptor) (Purinergic receptor) 595 68,388 Chain (1); Disulfide bond (5); Glycosylation (5); Modified residue (3); Mutagenesis (2); Sequence conflict (3); Topological domain (3); Transmembrane (2) TRANSMEM 26 46 Helical; Name=1. {ECO:0000255}.; TRANSMEM 335 355 Helical; Name=2. {ECO:0000255}. TOPO_DOM 1 25 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 47 334 Extracellular. {ECO:0000255}.; TOPO_DOM 356 595 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for ATP that acts as a ligand-gated ion channel. Responsible for ATP-dependent lysis of macrophages through the formation of membrane pores permeable to large molecules. Could function in both fast synaptic transmission and the ATP-mediated lysis of antigen-presenting cells. In the absence of its natural ligand, ATP, functions as a scavenger receptor in the recognition and engulfment of apoptotic cells. {ECO:0000250|UniProtKB:Q99572}. PTM: Phosphorylation results in its inactivation. {ECO:0000250|UniProtKB:Q99572}.; PTM: ADP-ribosylation at Arg-125 is necessary and sufficient to activate P2RX7 and gate the channel.; PTM: Palmitoylation of several cysteines in the C-terminal cytoplasmic tail is required for efficient localization to cell surface. {ECO:0000250|UniProtKB:Q99572}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q99572}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Functional P2XRs are organized as homomeric and heteromeric trimers. Interacts with LAMA3, ITGB2, ACTB, ACTN4, SVIL, MPP3, HSPA1, HSPCB, HSPA8, PIK230 and PTPRB (By similarity). Interacts (via C-terminus) with EMP2 (By similarity). {ECO:0000250|UniProtKB:Q99572}. +O70167 P3C2G_MOUSE Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit gamma (PI3K-C2-gamma) (PtdIns-3-kinase C2 subunit gamma) (EC 2.7.1.154) (Phosphoinositide 3-kinase-C2-gamma) 1506 171,580 Alternative sequence (2); Chain (1); Domain (6) FUNCTION: Generates phosphatidylinositol 3-phosphate (PtdIns3P) and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) that act as second messengers. May play a role in SDF1A-stimulated chemotaxis. {ECO:0000269|PubMed:20536348, ECO:0000269|PubMed:9514948}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:9514948}; Peripheral membrane protein {ECO:0000269|PubMed:9514948}. TISSUE SPECIFICITY: Expressed predominantly in liver. Also found in kidney, lung and lymphoid tissue. Down-regulated in BeF3 cells expressing the BCR-ABL oncogene p185. {ECO:0000269|PubMed:20536348, ECO:0000269|PubMed:9514948}. +Q8CG71 P3H2_MOUSE Prolyl 3-hydroxylase 2 (EC 1.14.11.7) (Leprecan-like protein 1) 703 80,154 Active site (1); Chain (1); Domain (1); Glycosylation (2); Metal binding (3); Motif (1); Repeat (4); Sequence conflict (1); Signal peptide (1) FUNCTION: Prolyl 3-hydroxylase that catalyzes the post-translational formation of 3-hydroxyproline on collagens (PubMed:24368846, PubMed:25645914). Contributes to proline 3-hydroxylation of collagen COL4A1 and COL1A1 in tendons, the eye sclera and in the eye lens capsule (PubMed:25645914). Has high activity with the type IV collagen COL4A1, and lower activity with COL1A1. Catalyzes hydroxylation of the first Pro in Gly-Pro-Hyp sequences where Hyp is 4-hydroxyproline. Has no activity on substrates that have proline instead of 4-hydroxyproline in the third position (By similarity). {ECO:0000250|UniProtKB:Q8IVL5, ECO:0000269|PubMed:24368846, ECO:0000269|PubMed:25645914}. SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:Q8IVL5, ECO:0000255|PROSITE-ProRule:PRU10138}. Sarcoplasmic reticulum {ECO:0000250|UniProtKB:Q8IVL5}. Golgi apparatus {ECO:0000250|UniProtKB:Q8IVL5}. TISSUE SPECIFICITY: Detected in kidney (PubMed:25645914). Detected on kidney tubular cells, pancreas acinar cells, Schwann cells of the peripheral nerve in the pinna, and in tunica adventitia, the smooth muscle layer of the aortic wall (at protein level) (PubMed:18487197). Detected in lung, skeletal muscle and kidney (PubMed:18487197). Detected in kidney glomeruli and in prehypertrophic regions of long bone from neonates (PubMed:25645914). In the eye, detected in the epithelial layer of the cornea and at lower levels in the sclera at the posterior end of the eye (PubMed:25645914). {ECO:0000269|PubMed:18487197, ECO:0000269|PubMed:25645914}. +Q8CG70 P3H3_MOUSE Prolyl 3-hydroxylase 3 (EC 1.14.11.7) (Leprecan-like protein 2) (Protein B) 732 81,701 Active site (1); Chain (1); Coiled coil (1); Compositional bias (2); Domain (1); Glycosylation (2); Metal binding (3); Motif (1); Repeat (4); Signal peptide (1) FUNCTION: Part of a complex composed of PLOD1, P3H3 and P3H4 that catalyzes hydroxylation of lysine residues in collagen alpha chains and is required for normal assembly and cross-linkling of collagen fibrils (PubMed:27119146). Required for normal hydroxylation of lysine residues in type I collagen chains in skin, bone, tendon, aorta and cornea (PubMed:28115524). Required for normal skin stability via its role in hydroxylation of lysine residues in collagen alpha chains and in collagen fibril assembly (PubMed:27119146, PubMed:28115524). Apparently not required for normal prolyl 3-hydroxylation on collagen chains, possibly because it functions redundantly with other prolyl 3-hydroxylases (PubMed:28115524). {ECO:0000269|PubMed:27119146, ECO:0000269|PubMed:28115524}. SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000255|PROSITE-ProRule:PRU10138}. SUBUNIT: Identified in a complex with PLOD1 and P3H4. {ECO:0000269|PubMed:27119146}. TISSUE SPECIFICITY: Detected in kidney (at protein level). {ECO:0000269|PubMed:28115524}. +Q60715 P4HA1_MOUSE Prolyl 4-hydroxylase subunit alpha-1 (4-PH alpha-1) (EC 1.14.11.2) (Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-1) 534 60,910 Alternative sequence (1); Binding site (1); Chain (1); Domain (1); Glycosylation (2); Metal binding (3); Repeat (1); Sequence conflict (3); Signal peptide (1) FUNCTION: Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. SUBUNIT: Heterotetramer of two alpha-1 chains and two beta chains (the beta chain is the multi-functional PDI). +Q9DCC4 P5CR3_MOUSE Pyrroline-5-carboxylate reductase 3 (P5C reductase 3) (P5CR 3) (EC 1.5.1.2) (Pyrroline-5-carboxylate reductase-like protein) 274 28,721 Chain (1); Frameshift (1); Initiator methionine (1); Modified residue (1); Sequence conflict (11) Amino-acid biosynthesis; L-proline biosynthesis; L-proline from L-glutamate 5-semialdehyde: step 1/1. FUNCTION: Enzyme that catalyzes the last step in proline biosynthesis. Proline is synthesized from either glutamate or ornithine; both are converted to pyrroline-5-carboxylate (P5C), and then to proline via pyrroline-5-carboxylate reductases (PYCRs). PYCRL is exclusively linked to the conversion of ornithine to proline. {ECO:0000250|UniProtKB:Q53H96}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q53H96}. SUBUNIT: Homodecamer; composed of 5 homodimers. {ECO:0000250|UniProtKB:P32322}. +Q922R5 P4R3B_MOUSE Serine/threonine-protein phosphatase 4 regulatory subunit 3B (SMEK homolog 2) 820 93,934 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (1); Modified residue (3); Sequence conflict (10) FUNCTION: Regulatory subunit of serine/threonine-protein phosphatase 4 (PP4). May regulate the activity of PPP4C at centrosomal microtubule organizing centers (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Nucleus. Note=In interphase localized in the cytoplasm and (with higher levels) the nucleus. During metaphase located in pericentriolar regions. SUBUNIT: Serine/threonine-protein phosphatase 4 (PP4) occurs in different assemblies of the catalytic and one or more regulatory subunits. Component of the PP4 complex PPP4C-PPP4R2-PPP4R3B. +Q3UEB3 PUF60_MOUSE Poly(U)-binding-splicing factor PUF60 (60 kDa poly(U)-binding-splicing factor) 564 60,249 Alternative sequence (2); Chain (1); Compositional bias (1); Cross-link (4); Domain (3); Modified residue (6); Region (2); Sequence conflict (1) FUNCTION: DNA- and RNA-binding protein, involved in several nuclear processes such as pre-mRNA splicing, apoptosis and transcription regulation. In association with FUBP1 regulates MYC transcription at the P2 promoter through the core-TFIIH basal transcription factor. Acts as a transcriptional repressor through the core-TFIIH basal transcription factor. Represses FUBP1-induced transcriptional activation but not basal transcription. Decreases ERCC3 helicase activity. Is also involved in pre-mRNA splicing. Promotes splicing of an intron with weak 3'-splice site and pyrimidine tract in a cooperative manner with U2AF2. Involved in apoptosis induction when overexpressed in HeLa cells. Modulates alternative splicing of several mRNAs. Binds to relaxed DNA of active promoter regions. Binds to the pyrimidine tract and 3'-splice site regions of pre-mRNA; binding is enhanced in presence of U2AF2. Binds to Y5 RNA in association with TROVE2. Binds to poly(U) RNA (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Note=Colocalizes partially with TROVE2. {ECO:0000250}. SUBUNIT: Homodimer. Associates with the spliceosome. Found in a complex with TROVE2 and Y5 RNA. Found in a complex with FUBP1 and far upstream element (FUSE) DNA segment. Interacts directly with ERCC3. Interacts with CDK7, GTF2H1 and SFRS11 (By similarity). {ECO:0000250}. DOMAIN: The third RNA recognition motif, called PUMP domain, is atypical and may rather mediate homodimerization and/or protein-protein interactions. +O88898 P63_MOUSE Tumor protein 63 (p63) (Transformation-related protein 63) (TP63) (Tumor protein p73-like) (p73L) 680 76,789 Alternative sequence (4); Chain (1); Compositional bias (1); Cross-link (1); DNA binding (1); Domain (1); Helix (5); Metal binding (4); Mutagenesis (1); Region (4); Sequence caution (1) FUNCTION: Acts as a sequence specific DNA binding transcriptional activator or repressor. The isoforms contain a varying set of transactivation and auto-regulating transactivation inhibiting domains thus showing an isoform specific activity. May be required in conjunction with TP73/p73 for initiation of p53/TP53 dependent apoptosis in response to genotoxic insults and the presence of activated oncogenes. Involved in Notch signaling by probably inducing JAG1 and JAG2. Activates transcription of the p21 promoter (By similarity). Activates RIPK4 transcription. Plays a role in the regulation of epithelial morphogenesis. The ratio of DeltaN-type and TA*-type isoforms may govern the maintenance of epithelial stem cell compartments and regulate the initiation of epithelial stratification from the undifferentiated embryonal ectoderm. Required for limb formation from the apical ectodermal ridge. {ECO:0000250, ECO:0000269|PubMed:10227293, ECO:0000269|PubMed:10227294, ECO:0000269|PubMed:11932750, ECO:0000269|PubMed:14729569, ECO:0000269|PubMed:22197488}. PTM: May be sumoylated. {ECO:0000250}.; PTM: Ubiquitinated. Polyubiquitination involves WWP1 and leads to proteasomal degradation of this protein. {ECO:0000269|PubMed:18806757}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14729569}. SUBUNIT: Binds DNA as a homotetramer. Isoform composition of the tetramer may determine transactivation activity. Interacts with HIPK2. Interacts with SSRP1, leading to stimulate coactivator activity. Interacts with PDS5A. Interacts (via activation domain) with NOC2L (By similarity). Interacts with WWP1. {ECO:0000250, ECO:0000269|PubMed:18806757}. DOMAIN: The transactivation inhibitory domain (TID) can interact with, and inhibit the activity of the N-terminal transcriptional activation domain of TA*-type isoforms. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed, notably in thymus, prostate, placenta and skeletal muscle, although the precise isoform varies according to tissue type. Progenitor cell layers of skin, breast and prostate express high levels of DeltaN-type isoforms. {ECO:0000269|PubMed:9774969}. +Q8VHR5 P66B_MOUSE Transcriptional repressor p66-beta (GATA zinc finger domain-containing protein 2B) (p66/p68) 594 65,411 Alternative sequence (2); Chain (1); Coiled coil (2); Cross-link (10); Modified residue (11); Region (2); Zinc finger (1) FUNCTION: Transcriptional repressor. Enhances MBD2-mediated repression. Efficient repression requires the presence of GATAD2A (By similarity). Targets MBD3 to discrete loci in the nucleus (By similarity). Plays a role in synapse development (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}. Note=Speckled nuclear localization requires both CR1 and CR2 regions. {ECO:0000250}. SUBUNIT: Binds MBD2 and MBD3. Interaction with MBD2 is required for the enhancement of MBD2-mediated repression and for targeting to the chromatin (By similarity). Component of the MeCP1 histone deacetylase complex (By similarity). Interacts with histone tails, including that of histones H2A, H2B, H3 and H4 (By similarity). {ECO:0000250}. DOMAIN: Both CR1 and CR2 regions are required for speckled nuclear localization. {ECO:0000250}. +Q8BKS9 PUM3_MOUSE Pumilio homolog 3 647 72,800 Chain (1); Domain (1); Erroneous initiation (2); Frameshift (1); Modified residue (1); Motif (1); Repeat (11) FUNCTION: Inhibits the poly(ADP-ribosyl)ation activity of PARP1 and the degradation of PARP1 by CASP3 following genotoxic stress. Binds to double-stranded RNA or DNA without sequence specificity. Involved in development of the eye and of primordial germ cells. {ECO:0000250|UniProtKB:Q15397, ECO:0000250|UniProtKB:X1WGX5}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q15397}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q15397}. Chromosome {ECO:0000250|UniProtKB:Q15397}. Note=Localizes predominantly in the nucleolus with minor punctate signals in the nucleoplasm. {ECO:0000250|UniProtKB:Q15397}. SUBUNIT: Interacts with PARP1 (via catalytic domain). {ECO:0000250|UniProtKB:Q15397}. DOMAIN: A 90 degree bend between Pumilio repeats 3 and 4 gives rise to a L-shaped protein. {ECO:0000250|UniProtKB:Q15397}. TISSUE SPECIFICITY: In the adult eye, expressed primarily in retinal ganglion cells and, to a lesser extent, in the pigmented cells. {ECO:0000269|PubMed:19319195}. +Q61206 PA1B2_MOUSE Platelet-activating factor acetylhydrolase IB subunit beta (EC 3.1.1.47) (PAF acetylhydrolase 30 kDa subunit) (PAF-AH 30 kDa subunit) (PAF-AH subunit beta) (PAFAH subunit beta) 229 25,581 Active site (3); Chain (1); Initiator methionine (1); Modified residue (4); Sequence conflict (3) FUNCTION: Inactivates PAF by removing the acetyl group at the sn-2 position. This is a catalytic subunit. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Cytosolic PAF-AH IB is formed of three subunits of 45 kDa (alpha), 30 kDa (beta) and 29 kDa (gamma). The catalytic activity of the enzyme resides in the beta and gamma subunits, whereas the alpha subunit has regulatory activity. Trimer formation is not essential for the catalytic activity. +Q50L43 PA24D_MOUSE Cytosolic phospholipase A2 delta (cPLA2-delta) (EC 3.1.1.4) (Phospholipase A2 group IVD) 825 93,042 Active site (2); Chain (1); Domain (2); Region (1); Sequence conflict (4) FUNCTION: Calcium-dependent phospholipase A2 that selectively hydrolyzes glycerophospholipids in the sn-2 position. Compared to its human ortholog, may have no substrate specificity for the fatty acid found at the sn-2 position. {ECO:0000269|PubMed:15866882}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:15866882}. Membrane {ECO:0000305|PubMed:15866882}; Peripheral membrane protein {ECO:0000305|PubMed:15866882}; Cytoplasmic side {ECO:0000305|PubMed:15866882}. Note=Translocates to perinuclear membranes that may correspond to endoplasmic reticulum or Golgi in a calcium-dependent fashion. {ECO:0000269|PubMed:15866882}. DOMAIN: The N-terminal C2 domain mediates the association with lipid membranes upon calcium binding. An additional second C2 domain may stand in between the C2 domain and the PLA2c domain. {ECO:0000250|UniProtKB:Q86XP0}. TISSUE SPECIFICITY: Weakly or not expressed in most tissues. Detected in placenta of 17.5 dpc embryos. {ECO:0000269|PubMed:15866882}. +Q64737 PUR2_MOUSE Trifunctional purine biosynthetic protein adenosine-3 [Includes: Phosphoribosylamine--glycine ligase (EC 6.3.4.13) (Glycinamide ribonucleotide synthetase) (GARS) (Phosphoribosylglycinamide synthetase); Phosphoribosylformylglycinamidine cyclo-ligase (EC 6.3.3.1) (AIR synthase) (AIRS) (Phosphoribosyl-aminoimidazole synthetase); Phosphoribosylglycinamide formyltransferase (EC 2.1.2.2) (5'-phosphoribosylglycinamide transformylase) (GAR transformylase) (GART)] 1010 107,503 Active site (1); Alternative sequence (1); Binding site (2); Chain (1); Domain (1); Initiator methionine (1); Metal binding (2); Modified residue (6); Nucleotide binding (1); Region (6); Sequence conflict (9); Site (1) Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 2/2. Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/2. Purine metabolism; IMP biosynthesis via de novo pathway; N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (10-formyl THF route): step 1/1. TISSUE SPECIFICITY: Detected in liver, kidney and brain. {ECO:0000269|PubMed:7829519}. +Q3U0P1 PALB2_MOUSE Partner and localizer of BRCA2 1104 119,097 Alternative sequence (4); Chain (1); Coiled coil (1); Helix (1); Modified residue (3); Region (7); Repeat (7) FUNCTION: Plays a critical role in homologous recombination repair (HRR) through its ability to recruit BRCA2 and RAD51 to DNA breaks. Strongly stimulates the DNA strand-invasion activity of RAD51, stabilizes the nucleoprotein filament against a disruptive BRC3-BRC4 polypeptide and helps RAD51 to overcome the suppressive effect of replication protein A (RPA). Functionally cooperates with RAD51AP1 in promoting of D-loop formation by RAD51. Serves as the molecular scaffold in the formation of the BRCA1-PALB2-BRCA2 complex which is essential for homologous recombination. Via its WD repeats is proposed to scaffold a HR complex containing RAD51C and BRCA2 which is thought to play a role in HR-mediated DNA repair. Essential partner of BRCA2 that promotes the localization and stability of BRCA2. Also enables its recombinational repair and checkpoint functions of BRCA2. May act by promoting stable association of BRCA2 with nuclear structures, allowing BRCA2 to escape the effects of proteasome-mediated degradation. Binds DNA with high affinity for D loop, which comprises single-stranded, double-stranded and branched DNA structures. May play a role in the extension step after strand invasion at replication-dependent DNA double-strand breaks; together with BRCA2 is involved in both POLH localization at collapsed replication forks and DNA polymerization activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Note=Colocalizes with BRCA2 in nuclear foci. {ECO:0000250}. SUBUNIT: Homooligomer; dissociated upon DNA damage thus allowing association with BRCA1. Oligomerization is essential for its focal accumulation at DNA breaks. Part of a BRCA complex containing BRCA1, BRCA2 and PALB2. Interacts with BRCA1 and this interaction is essential for its function in HRR. Interacts with RAD51AP1 and MORF4L1/MRG15. Interacts with BRCA2, RAD51C, RAD51 and XRCC3; the interactions are direct and it may serve as a scaffold for a HR complex containing PALB2, BRCA2, RAD51C, RAD51 and XRCC3. Interacts with POLH; the interaction is direct (By similarity). {ECO:0000250}. DOMAIN: Interaction with BRCA2 occurs through a hydrophobic pocket at the crossover between WD repeats 4 and 5. {ECO:0000250}.; DOMAIN: The coiled coil domain mediates self-association.; DOMAIN: The chromatin-association motif (ChAM) mediates association with chromatin, probably through nucleosome core particles, independently from binding to D loop, ssDNA or dsDNA structures. +P70261 PALD_MOUSE Paladin 859 96,740 Chain (1); Compositional bias (1); Initiator methionine (1); Lipidation (1); Modified residue (1); Sequence conflict (5) SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. TISSUE SPECIFICITY: Vascular expression detected in the central nervous system, kidney, lung, heart, skeletal muscle, white adipose tissue (WAT), brown adipose tissue, liver, pancreas and spleen. Not expressed in all vessels: for instance, not expressed in capillaries in the brain, and expressed mainly in large vessels in the heart, WAT, liver, pancreas and kidney. Predominant nonvascular expression in myocardium and lung mesenchyme. In large vessels, primarily expressed by smooth muscle cells, but occasionally detected at low levels in the endothelium. Expressed in various cells of the hematopoietic lineage. {ECO:0000269|PubMed:22354871}. +Q9JHU2 PALMD_MOUSE Palmdelphin 551 62,700 Chain (1); Coiled coil (1); Cross-link (3); Modified residue (12); Sequence conflict (8) PTM: Phosphorylated. {ECO:0000269|PubMed:16323283}. SUBCELLULAR LOCATION: Cytoplasm. Cell projection, dendrite. Cell projection, dendritic spine {ECO:0000250}. SUBUNIT: Interacts with GLUL. {ECO:0000269|PubMed:16323283}. TISSUE SPECIFICITY: Ubiquitous. Expressed at highest levels in the heart and lung. {ECO:0000269|PubMed:11478809}. +Q8BU25 PAMR1_MOUSE Inactive serine protease PAMR1 (Peptidase domain-containing protein associated with muscle regeneration 1) (Regeneration-associated muscle protease homolog) 720 80,320 Chain (1); Compositional bias (1); Disulfide bond (11); Domain (5); Glycosylation (1); Sequence conflict (3); Signal peptide (1) FUNCTION: May play a role in regeneration of skeletal muscle. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Predominantly expressed in normal skeletal muscle and brain. Expression is enhanced in the regenerating area of injured skeletal muscle in mice. {ECO:0000269|PubMed:15111323}. +Q9DCL9 PUR6_MOUSE Multifunctional protein ADE2 [Includes: Phosphoribosylaminoimidazole-succinocarboxamide synthase (EC 6.3.2.6) (SAICAR synthetase); Phosphoribosylaminoimidazole carboxylase (EC 4.1.1.21) (AIR carboxylase) (AIRC)] 425 47,006 Active site (5); Chain (1); Initiator methionine (1); Modified residue (7); Region (4); Sequence conflict (1); Site (1) Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2. Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-phospho-D-ribosyl)imidazole (carboxylase route): step 1/1. SUBUNIT: Homooctamer. {ECO:0000250}. +Q78WZ7 RPA43_MOUSE DNA-directed RNA polymerase I subunit RPA43 (Twist neighbor protein) 330 36,721 Chain (1); Compositional bias (3); Frameshift (1); Modified residue (3); Sequence conflict (4) FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I which synthesizes ribosomal RNA precursors. Through its association with RRN3/TIF-IA may be involved in recruitment of Pol I to rDNA promoters. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. SUBUNIT: Component of the RNA polymerase I (Pol I) complex consisting of at least 13 subunits (By similarity). Interacts with RRN3/TIF-IA. {ECO:0000250, ECO:0000269|PubMed:12393749}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12438708}. +Q8CHG7 RPGF2_MOUSE Rap guanine nucleotide exchange factor 2 (Cyclic nucleotide ras GEF) (CNrasGEF) (Neural RAP guanine nucleotide exchange protein) (nRap GEP) (PDZ domain-containing guanine nucleotide exchange factor 1) (PDZ-GEF1) (RA-GEF-1) (Ras/Rap1-associating GEF-1) 1496 166,415 Chain (1); Compositional bias (2); Domain (4); Modified residue (13); Nucleotide binding (1) FUNCTION: Functions as a guanine nucleotide exchange factor (GEF), which activates Rap and Ras family of small GTPases by exchanging bound GDP for free GTP in a cAMP-dependent manner. Serves as a link between cell surface receptors and Rap/Ras GTPases in intracellular signaling cascades. Acts also as an effector for Rap1 by direct association with Rap1-GTP thereby leading to the amplification of Rap1-mediated signaling. Shows weak activity on HRAS. It is controversial whether RAPGEF2 binds cAMP and cGMP or not. Its binding to ligand-activated beta-1 adrenergic receptor ADRB1 leads to the Ras activation through the G(s)-alpha signaling pathway. Involved in the cAMP-induced Ras and Erk1/2 signaling pathway that leads to sustained inhibition of long term melanogenesis by reducing dendrite extension and melanin synthesis. Provides also inhibitory signals for cell proliferation of melanoma cells and promotes their apoptosis in a cAMP-independent nanner. Regulates cAMP-induced neuritogenesis by mediating the Rap1/B-Raf/ERK signaling through a pathway that is independent on both PKA and RAPGEF3/RAPGEF4. Involved in neuron migration and in the formation of the major forebrain fiber connections forming the corpus callosum, the anterior commissure and the hippocampal commissure during brain development. Involved in neuronal growth factor (NGF)-induced sustained activation of Rap1 at late endosomes and in brain-derived neurotrophic factor (BDNF)-induced axon outgrowth of hippocampal neurons. Plays a role in the regulation of embryonic blood vessel formation and in the establishment of basal junction integrity and endothelial barrier function. May be involved in the regulation of the vascular endothelial growth factor receptor KDR and cadherin CDH5 expression at allantois endothelial cell-cell junctions. {ECO:0000269|PubMed:16272156, ECO:0000269|PubMed:17826737, ECO:0000269|PubMed:19453629, ECO:0000269|PubMed:19635461, ECO:0000269|PubMed:21864586, ECO:0000269|PubMed:23800469}. PTM: Ubiquitinated by NEDD4, leading to proteasomal degradation. {ECO:0000250}.; PTM: Phosphorylation by PLK2 promotes its activity. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000250}. Late endosome {ECO:0000250}. Cell junction {ECO:0000250}. Note=Associated with the synaptic plasma membrane. Localized diffusely in the cytoplasm before neuronal growth factor (NGF) stimulation. Recruited to late endosomes after NGF stimulation. Colocalized with the high affinity nerve growth factor receptor NTRK1 at late endosomes. Translocated to the perinuclear region in a RAP1A-dependent manner. Translocated to the cell membrane. Colocalized with CTNNB1 at cell-cell contacts (By similarity). {ECO:0000250}. SUBUNIT: Found in a complex, at least composed of KIDINS220, MAGI2, NTRK1 and RAPGEF2; the complex is mainly formed at late endosomes in a neuronal growth factor (NGF)-dependent manner. Interacts (via C-terminal domain) with NEDD4 (via WW domains); this interaction leads to ubiquitination and degradation via the proteasome pathway in a cAMP-independent manner. Interacts with MAGI1 (via PDZ domain). Interacts with ADRB1 (via C-terminal PDZ motif); the interaction is direct. Interacts (via Ras-associating domain) with RAP1A (via GTP-bound active form). Interacts weakly with HRAS (via GDP- and GTP-bound forms). Interacts (via C-terminal domain) with MAGI2 (via PDZ and WW domains). Interacts with CDH1, CTNNB1 and TJP1 (By similarity). {ECO:0000250}. DOMAIN: The Ras-associating domain is necessary for the Rap guanine nucleotide exchange activity. The N-terminal regionis necessary for cAMP-binding. The PDZ domain is necessary for its targeting to the cell membrane (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in all layers of the cerebral cortex, hippocampus and cerebellum. Expressed in the cortical plate, cingulate cortex and the subventricular zone. Expressed in neurons and endocrine cells (at protein level). Expressed in melanoma cells. {ECO:0000269|PubMed:16272156, ECO:0000269|PubMed:19453629, ECO:0000269|PubMed:21864586, ECO:0000269|PubMed:23800469}. +P97304 RPAC2_MOUSE DNA-directed RNA polymerases I and III subunit RPAC2 (RNA polymerases I and III subunit AC2) (AC19) (DNA-directed RNA polymerase I subunit D) (RNA polymerase I 16 kDa subunit) (RPA16) 133 15,072 Chain (1); Modified residue (1) FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common core component of RNA polymerases I and III which synthesize ribosomal RNA precursors and small RNAs, such as 5S rRNA and tRNAs, respectively. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the RNA polymerase I (Pol I) and RNA polymerase III (Pol III) complexes consisting of at least 13 and 17 subunits, respectively. {ECO:0000250}. +Q6TAW2 SERP2_MOUSE Stress-associated endoplasmic reticulum protein 2 (Ribosome-associated membrane protein RAMP4-2) 65 7,431 Alternative sequence (2); Chain (1); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 38 58 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 1 37 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 59 65 Lumenal. {ECO:0000255}. FUNCTION: May interact with target proteins during translocation into the lumen of the endoplasmic reticulum. May protect unfolded target proteins against degradation and facilitate correct glycosylation (Potential). {ECO:0000305}. SUBCELLULAR LOCATION: Membrane; Single-pass type IV membrane protein. Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. +Q8BH49 SESQ1_MOUSE Sesquipedalian-1 (Ses1) (27 kDa inositol polyphosphate phosphatase interacting protein A) (IPIP27A) (PH domain-containing endocytic trafficking adaptor 1) 266 29,218 Chain (1); Domain (1); Modified residue (1); Motif (1) FUNCTION: Plays a role in endocytic trafficking. Required for receptor recycling from endosomes, both to the trans-Golgi network and the plasma membrane. {ECO:0000250|UniProtKB:Q8N4B1}. SUBCELLULAR LOCATION: Early endosome {ECO:0000250|UniProtKB:Q8N4B1}. Recycling endosome {ECO:0000250|UniProtKB:Q8N4B1}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q8N4B1}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:Q8N4B1}. Note=Interaction with OCRL may be crucial for targeting to endosome and to the trans-Golgi network. Also found on macropinosomes. Not detected in late endosomes, nor in lysosomes. {ECO:0000250|UniProtKB:Q8N4B1}. SUBUNIT: Forms homodimers and heterodimers with PHETA2. Interacts with OCRL and INPP5B (By similarity). Interaction with OCRL may be important for endosomal morphology and function (By similarity). {ECO:0000250|UniProtKB:D3ZL52, ECO:0000250|UniProtKB:Q8N4B1}. DOMAIN: The F&H motif, an approximately 12-13 amino-acid sequence centered around Phe and His residues, is essential for binding to OCRL and INPP5B. {ECO:0000250|UniProtKB:Q8N4B1}. +Q78RX3 SIM12_MOUSE Small integral membrane protein 12 92 10,796 Chain (1); Transmembrane (1) TRANSMEM 15 34 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +E9Q942 SIM13_MOUSE Small integral membrane protein 13 88 9,954 Chain (1); Modified residue (4); Transmembrane (1) TRANSMEM 10 30 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q91VT8 SIM14_MOUSE Small integral membrane protein 14 99 10,732 Chain (1); Topological domain (2); Transmembrane (1) TRANSMEM 50 70 Helical. {ECO:0000255}. TOPO_DOM 1 49 Lumenal. {ECO:0000255}.; TOPO_DOM 71 99 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:24499674}. +Q61045 SIM1_MOUSE Single-minded homolog 1 (mSIM1) 765 85,541 Chain (1); Domain (5); Erroneous termination (1); Motif (1); Sequence conflict (8) FUNCTION: Transcriptional factor that may have pleiotropic effects during embryogenesis and in the adult. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00632, ECO:0000255|PROSITE-ProRule:PRU00981}. SUBUNIT: Efficient DNA binding requires dimerization with another bHLH protein. Heterodimer; forms a heterodimer with ARNT, ARNT2. {ECO:0000269|PubMed:27782878, ECO:0000269|PubMed:9020169}. TISSUE SPECIFICITY: Detected in lung, skeletal muscle and kidney. During fetal development it is found in the CNS, developing kidney, mesodermal and endodermal tissues, including developing somites, mesonephric duct, and foregut. +Q9DAL0 SIM23_MOUSE Small integral membrane protein 23 136 15,821 Chain (1); Coiled coil (1); Topological domain (2); Transmembrane (1) TRANSMEM 32 52 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 31 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 53 136 Extracellular. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +A0A140LHV9 SIM27_MOUSE Small integral membrane protein 27 (TOPORS antisense RNA 1) 49 5,823 Chain (1); Transmembrane (1) TRANSMEM 11 31 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. +Q3TS39 SIM33_MOUSE Small integral membrane protein 33 127 13,926 Chain (1); Glycosylation (1); Transmembrane (1) TRANSMEM 38 58 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. +Q99K70 RRAGC_MOUSE Ras-related GTP-binding protein C (Rag C) (RagC) (GTPase-interacting protein 2) (TIB929) 398 44,121 Alternative sequence (2); Beta strand (5); Chain (1); Frameshift (1); Helix (4); Initiator methionine (1); Modified residue (4); Nucleotide binding (3); Sequence conflict (6); Turn (1) FUNCTION: Guanine nucleotide-binding protein forming heterodimeric Rag complexes required for the amino acid-induced relocalization of mTORC1 to the lysosomes and its subsequent activation by the GTPase RHEB. This is a crucial step in the activation of the TOR signaling cascade by amino acids (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9HB90}. Nucleus {ECO:0000250|UniProtKB:Q9HB90}. Lysosome {ECO:0000250|UniProtKB:Q9HB90}. Note=Predominantly cytoplasmic. May shuttle between the cytoplasm and nucleus, depending on the bound nucleotide state of associated RRAGA. {ECO:0000250|UniProtKB:Q9HB90}. SUBUNIT: Forms a heterodimer with RRAGA, in a sequence-independent manner, and RRAGB. Heterodimerization stabilizes proteins of the heterodimer. In complex with RRAGA or RRAGB, interacts with RPTOR; this interaction is particularly efficient with GTP-loaded RRAGB and GDP-loaded RRAGC. Interacts with NOL8. Interacts with SH3BP4; the interaction with this negative regulator is most probably direct, preferentially occurs with the inactive GDP-bound form of RRAGB, is negatively regulated by amino acids and prevents interaction with RPTOR. The Rag heterodimer interacts with SLC38A9; the probable amino acid sensor (By similarity). Interacts with SESN1, SESN2 AND SESN3 (PubMed:25259925). {ECO:0000250|UniProtKB:Q9HB90, ECO:0000269|PubMed:25259925}. TISSUE SPECIFICITY: Expressed most abundantly in kidney. Moderately expressed in brain, ovary, and testis, and detected at lower levels in heart, liver, and muscle. Not detected in lung, spleen, and small intestine. Widely expressed in tumor cells, with expression being specifically up-regulated in highly metastatic cells. {ECO:0000269|PubMed:10660099}. +Q8K2C6 SIR5_MOUSE NAD-dependent protein deacylase sirtuin-5, mitochondrial (EC 3.5.1.-) (Regulatory protein SIR2 homolog 5) (SIR2-like protein 5) 310 34,134 Active site (1); Binding site (3); Chain (1); Domain (1); Metal binding (4); Mutagenesis (1); Nucleotide binding (4); Transit peptide (1) FUNCTION: NAD-dependent lysine demalonylase, desuccinylase and deglutarylase that specifically removes malonyl, succinyl and glutaryl groups on target proteins (PubMed:23806337, PubMed:21908771, PubMed:22076378, PubMed:24315375, PubMed:24703693). Activates CPS1 and contributes to the regulation of blood ammonia levels during prolonged fasting: acts by mediating desuccinylation and deglutarylation of CPS1, thereby increasing CPS1 activity in response to elevated NAD levels during fasting (PubMed:19410549, PubMed:24703693). Activates SOD1 by mediating its desuccinylation, leading to reduced reactive oxygen species (By similarity). Activates SHMT2 by mediating its desuccinylation (By similarity). Modulates ketogenesis through the desuccinylation and activation of HMGCS2 (PubMed:24315375). Has weak NAD-dependent protein deacetylase activity; however this activity may not be physiologically relevant in vivo. Can deacetylate cytochrome c (CYCS) and a number of other proteins in vitro such as Uox (PubMed:23085393). {ECO:0000255|HAMAP-Rule:MF_03160, ECO:0000269|PubMed:19410549, ECO:0000269|PubMed:21908771, ECO:0000269|PubMed:22076378, ECO:0000269|PubMed:23085393, ECO:0000269|PubMed:23806337, ECO:0000269|PubMed:24315375, ECO:0000269|PubMed:24703693}. SUBCELLULAR LOCATION: Mitochondrion. Cytoplasm, cytosol. Nucleus. Note=Mainly mitochondrial. Also present extramitochondrially, with a fraction present in the cytosol and very small amounts also detected in the nucleus. SUBUNIT: Monomer. Homodimer (By similarity). Interacts with CPS1 (PubMed:19410549). Interacts with PCCA (PubMed:23438705). {ECO:0000250|UniProtKB:Q9NXA8, ECO:0000255|HAMAP-Rule:MF_03160, ECO:0000269|PubMed:19410549, ECO:0000269|PubMed:23438705}. DOMAIN: In contrast to class I sirtuins, class III sirtuins have only weak deacetylase activity. Difference in substrate specificity is probably due to a larger hydrophobic pocket with 2 residues (Tyr-102 and Arg-105) that bind to malonylated and succinylated substrates and define the specificity. {ECO:0000255|HAMAP-Rule:MF_03160}. TISSUE SPECIFICITY: Detected in brain, liver, heart, kidney, lung, thymus, spleen, skeletal muscle, intestine, pancreas and testis (at protein level). {ECO:0000269|PubMed:19410549}. +Q8BZG5 RRNAD_MOUSE Protein RRNAD1 475 53,303 Alternative sequence (3); Chain (1); Coiled coil (1); Sequence conflict (1); Transmembrane (1) TRANSMEM 406 426 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q61321 SIX4_MOUSE Homeobox protein SIX4 (Sine oculis homeobox homolog 4) (Skeletal muscle-specific ARE-binding protein AREC3) 775 82,263 Alternative sequence (4); Chain (1); Compositional bias (4); DNA binding (1); Initiator methionine (1); Modified residue (2); Region (1) FUNCTION: Transcriptional regulator which can act as both a transcriptional repressor and activator by binding a DNA sequence on these target genes and is involved in processes like cell differentiation, cell migration and cell survival. Transactivates gene expression by binding a 5'-[CAT]A[CT][CT][CTG]GA[GAT]-3' motif present in the Trex site and from a 5'-TCA[AG][AG]TTNC-3' motif present in the MEF3 site of the muscle-specific genes enhancer (PubMed:14966291). Acts cooperatively with EYA proteins to transactivate their target genes through interaction and nuclear translocation of EYA protein (PubMed:10490620). Acts synergistically with SIX1 to regulate target genes involved in formation of various organs, including muscle, kidney, gonad, ganglia, olfactory epithelium and cranial skeleton. Plays a role in several important steps of muscle development. Controls the genesis of hypaxial myogenic progenitors in the dermomyotome by transactivating PAX3 and the delamination and migration of the hypaxial precursors from the ventral lip to the limb buds through the transactivation of PAX3, MET and LBX1 (PubMed:15788460). Controls myoblast determination by transactivating MYF5, MYOD1 and MYF6 (PubMed:15788460, PubMed:17592144). Controls somitic differentiation in myocyte through MYOG transactivation (PubMed:15788460). Plays a role in synaptogenesis and sarcomere organization by participating in myofiber specialization during embryogenesis by activating fast muscle program in the primary myotome resulting in an up-regulation of fast muscle genes, including ATP2A1, MYL1 and TNNT3 (PubMed:19962975, PubMed:21884692). Simultaneously, is also able to activate inhibitors of slow muscle genes, such as SOX6, HRASLS, and HDAC4, thereby restricting the activation of the slow muscle genes (PubMed:21884692). During muscle regeneration, negatively regulates differentiation of muscle satellite cells through down-regulation of MYOG expression (PubMed:20696153). During kidney development regulates the early stages of metanephros development and ureteric bud formation through regulation of GDNF, SALL1, PAX8 and PAX2 expression (PubMed:17300925). Plays a role in gonad development by regulating both testis determination and size determination. In gonadal sex determination, transactivates ZFPM2 by binding a MEF3 consensus sequence, resulting in SRY up-regulation. In gonadal size determination, transactivates NR5A1 by binding a MEF3 consensus sequence resulting in gonadal precursor cell formation regulation (PubMed:23987514). During olfactory development mediates the specification and patterning of olfactory placode through fibroblast growth factor and BMP4 signaling pathways and also regulates epithelial cell proliferation during placode formation (PubMed:19027001). Promotes survival of sensory neurons during early trigeminal gangliogenesis (PubMed:16938278). In the developing dorsal root ganglia, up-regulates SLC12A2 transcription (PubMed:15955062). Regulates early thymus/parathyroid organogenesis through regulation of GCM2 and FOXN1 expression (PubMed:16530750). Forms gustatory papillae during development of the tongue (PubMed:21978088). Also plays a role during embryonic cranial skeleton morphogenesis (PubMed:20515681). {ECO:0000269|PubMed:10490620, ECO:0000269|PubMed:14966291, ECO:0000269|PubMed:15788460, ECO:0000269|PubMed:15955062, ECO:0000269|PubMed:16530750, ECO:0000269|PubMed:16938278, ECO:0000269|PubMed:17300925, ECO:0000269|PubMed:17592144, ECO:0000269|PubMed:19027001, ECO:0000269|PubMed:19962975, ECO:0000269|PubMed:20515681, ECO:0000269|PubMed:20696153, ECO:0000269|PubMed:21884692, ECO:0000269|PubMed:21978088, ECO:0000269|PubMed:23987514, ECO:0000303|PubMed:10490620}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8628654, ECO:0000269|PubMed:9990334}. Cytoplasm {ECO:0000269|PubMed:8628654, ECO:0000269|PubMed:9990334}. SUBUNIT: Interacts with EYA3; acts cooperatively with EYA3 to transactivate target genes through interaction and nuclear translocation of EYA3 protein (PubMed:12215533, PubMed:10490620). {ECO:0000269|PubMed:10490620, ECO:0000269|PubMed:12215533, ECO:0000303|PubMed:10490620}. TISSUE SPECIFICITY: Mainly expressed in the skeletal muscle (isoform 1 and isoform 2 but not isoform 3), and weakly in the heart. Also found in the retina and the distal tube of kidney. Expressed in skeletal muscle, nasal epithelium, cochlea, parathyroid and salivary gland (PubMed:11313460). Expressed in muscle satellite cells of normal and regenerating muscles (PubMed:20696153). {ECO:0000269|PubMed:11313460, ECO:0000269|PubMed:20696153}. +Q9D9Z1 SKAP_MOUSE Small kinetochore-associated protein (SKAP) (Kinetochore-localized astrin-binding protein) (Kinastrin) (Kinetochore-localized astrin/SPAG5-binding protein) (TRAF4-associated factor 1) 312 34,728 Chain (1); Coiled coil (2); Erroneous initiation (1); Region (1); Sequence conflict (1) FUNCTION: Essential component of the mitotic spindle required for faithful chromosome segregation and progression into anaphase. Promotes the metaphase-to-anaphase transition and is required for chromosome alignment, normal timing of sister chromatid segregation, and maintenance of spindle pole architecture. The astrin (SPAG5)-kinastrin (SKAP) complex promotes stable microtubule-kinetochore attachments. Required for kinetochore oscillations and dynamics of microtubule plus-ends during live cell mitosis, possibly by forming a link between spindle microtubule plus-ends and mitotic chromosomes to achieve faithful cell division. {ECO:0000250|UniProtKB:Q9Y448}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y448}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q9Y448}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q9Y448}. Note=Colocalizes with microtubules around centrosomes in prophase and with the mitotic spindle at prometaphase and metaphase. From late prometaphase to anaphase, is highly concentrated on kinetochores. Located at the kinetochore-microtubule interface. The astrin (SPAG5)-kinastrin (SKAP) complex localizes to the microtubule plus ends. {ECO:0000250|UniProtKB:Q9Y448}. SUBUNIT: Part of an astrin (SPAG5)-kinastrin (SKAP) complex containing KNSTRN, SPAG5, PLK1, DYNLL1 and SGO2. Interacts with SPAG5. Directly binds to microtubules, although at relatively low affinity. Interacts with CENPE; this interaction greatly favors microtubule-binding. Interacts with DSN1/MIS13; leading to localization to kinetochores. Interacts with MAPRE1/EB1; leading to localization to the microtubule plus ends. Interacts with PRPF19. {ECO:0000250|UniProtKB:Q9Y448}. DOMAIN: The coiled coil regions mediate binding to kinetochores. {ECO:0000250|UniProtKB:Q9Y448}. +A7XV14 SKI11_MOUSE Selection and upkeep of intraepithelial T-cells protein 11 (Skint-11) 364 42,262 Chain (1); Disulfide bond (1); Domain (1); Signal peptide (1); Topological domain (4); Transmembrane (3) TRANSMEM 139 159 Helical. {ECO:0000255}.; TRANSMEM 187 207 Helical. {ECO:0000255}.; TRANSMEM 231 251 Helical. {ECO:0000255}. TOPO_DOM 29 138 Extracellular. {ECO:0000255}.; TOPO_DOM 160 186 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 208 230 Extracellular. {ECO:0000255}.; TOPO_DOM 252 364 Cytoplasmic. {ECO:0000255}. FUNCTION: May act by engaging a cell surface molecule on immature T-cells in the embryonic thymus. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in skin and thymus. +Q60665 SKIL_MOUSE Ski-like protein (Ski-related oncogene) (Ski-related protein) 675 76,359 Alternative sequence (1); Chain (1); Coiled coil (1); Cross-link (4); Modified residue (1); Sequence conflict (13) FUNCTION: May have regulatory role in cell division or differentiation in response to extracellular signals. {ECO:0000250}. PTM: Ubiquitinated by RNF111 and RNF165, promoting proteasomal degradation, leading to enhance the BMP-Smad signaling. {ECO:0000269|PubMed:23610558}. SUBUNIT: Interacts with CPNE4 (via VWFA domain) (PubMed:12522145). Interacts with SMAD2, SMAD3 and RNF111. Interacts with WWP1 (By similarity). {ECO:0000250|UniProtKB:P12757, ECO:0000269|PubMed:12522145}. +A7TZE6 SKIT1_MOUSE Selection and upkeep of intraepithelial T-cells protein 1 (Skint-1) (Immunoglobulin-like and transmembrane domain-containing protein expressed in skin and thymus protein 1) 364 41,792 Alternative sequence (6); Beta strand (9); Chain (1); Disulfide bond (1); Domain (2); Glycosylation (1); Helix (2); Natural variant (1); Sequence conflict (28); Signal peptide (1); Topological domain (4); Transmembrane (3); Turn (2) TRANSMEM 247 267 Helical. {ECO:0000255}.; TRANSMEM 285 305 Helical. {ECO:0000255}.; TRANSMEM 326 346 Helical. {ECO:0000255}. TOPO_DOM 24 246 Extracellular. {ECO:0000255}.; TOPO_DOM 268 284 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 306 325 Extracellular. {ECO:0000255}.; TOPO_DOM 347 364 Cytoplasmic. {ECO:0000255}. FUNCTION: May act by engaging a cell surface molecule on immature T-cells in the embryonic thymus. Plays a central role in mediating key epithelial-immune interactions by being involved in the selection of Vgamma5(+)Vdelta1(+) T-cells, which constitute 90% of epidermal gammadelta T-cells. {ECO:0000269|PubMed:18408721}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in skin and thymus. {ECO:0000269|PubMed:18408721}. +A7XUX6 SKIT2_MOUSE Selection and upkeep of intraepithelial T-cells protein 2 (Skint-2) 400 45,644 Alternative sequence (3); Chain (1); Disulfide bond (2); Domain (2); Glycosylation (1); Sequence conflict (12); Signal peptide (1); Topological domain (4); Transmembrane (3) TRANSMEM 241 261 Helical. {ECO:0000255}.; TRANSMEM 281 301 Helical. {ECO:0000255}.; TRANSMEM 322 342 Helical. {ECO:0000255}. TOPO_DOM 22 240 Extracellular. {ECO:0000255}.; TOPO_DOM 262 280 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 302 321 Extracellular. {ECO:0000255}.; TOPO_DOM 343 400 Cytoplasmic. {ECO:0000255}. FUNCTION: May act by engaging a cell surface molecule on immature T-cells in the embryonic thymus. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in skin, thymus and mammary gland. {ECO:0000269|PubMed:18408721}. +A7XV07 SKIT8_MOUSE Selection and upkeep of intraepithelial T-cells protein 8 (Skint-8) 398 45,092 Alternative sequence (4); Chain (1); Disulfide bond (2); Domain (2); Erroneous initiation (4); Glycosylation (2); Sequence conflict (3); Signal peptide (1); Topological domain (4); Transmembrane (3) TRANSMEM 245 265 Helical. {ECO:0000255}.; TRANSMEM 289 309 Helical. {ECO:0000255}.; TRANSMEM 332 352 Helical. {ECO:0000255}. TOPO_DOM 26 244 Extracellular. {ECO:0000255}.; TOPO_DOM 266 288 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 310 331 Extracellular. {ECO:0000255}.; TOPO_DOM 353 398 Cytoplasmic. {ECO:0000255}. FUNCTION: May act by engaging a cell surface molecule on immature T-cells in the embryonic thymus. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in skin, thymus, testis and, to a lower extent, bladder, brain, heart, kidney, mammary gland, small intestine and uterus. {ECO:0000269|PubMed:18408721}. +A7TZG3 SKIT9_MOUSE Selection and upkeep of intraepithelial T-cells protein 9 (Skint-9) 319 36,119 Chain (1); Disulfide bond (1); Domain (1); Glycosylation (1); Signal peptide (1); Topological domain (4); Transmembrane (3) TRANSMEM 140 160 Helical. {ECO:0000255}.; TRANSMEM 184 204 Helical. {ECO:0000255}.; TRANSMEM 229 249 Helical. {ECO:0000255}. TOPO_DOM 27 139 Extracellular. {ECO:0000255}.; TOPO_DOM 161 183 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 205 228 Extracellular. {ECO:0000255}.; TOPO_DOM 250 319 Cytoplasmic. {ECO:0000255}. FUNCTION: May act by engaging a cell surface molecule on immature T-cells in the embryonic thymus. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in skin, thymus and testis. {ECO:0000269|PubMed:18408721}. +Q60698 SKI_MOUSE Ski oncogene (Proto-oncogene c-Ski) 725 80,119 Chain (1); Coiled coil (1); Modified residue (3) FUNCTION: May play a role in terminal differentiation of skeletal muscle cells but not in the determination of cells to the myogenic lineage. Functions as a repressor of TGF-beta signaling. PTM: Ubiquitinated by RNF165, promoting proteasomal degradation, leading to enhance the BMP-Smad signaling. {ECO:0000269|PubMed:23610558}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with SMAD2, SMAD3 and SMAD4. Interacts with HIPK2. Part of a complex with HIPK2 and SMAD1/2/3. Interacts with PRDM16 and SMAD3; the interaction with PRDM16 promotes the recruitment SMAD3-HDAC1 complex on the promoter of TGF-beta target genes (By similarity). {ECO:0000250}. +Q8BX46 SKOR1_MOUSE SKI family transcriptional corepressor 1 (Fussel-15 homolog) (Ladybird homeobox corepressor 1) (Lbx1 corepressor 1) (Transcriptional corepressor Corl1) 964 100,245 Alternative sequence (1); Chain (1); Coiled coil (1); Sequence conflict (2) FUNCTION: Inhibits BMP signaling (By similarity). Acts as a transcriptional corepressor of LBX1. {ECO:0000250, ECO:0000269|PubMed:15528197}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15528197}. SUBUNIT: Interacts with SMAD1, SMAD2 and SMAD3 (By similarity). Interacts with LBX1. {ECO:0000250, ECO:0000269|PubMed:15528197}. TISSUE SPECIFICITY: Expressed in brain with higher levels in embryo than adult. Expressed by migratory precursors of Purkinje cells in the postnatal brain. Also expressed in adult testis. {ECO:0000269|PubMed:15528197, ECO:0000269|PubMed:17292623}. +A7M7C7 SKOR2_MOUSE SKI family transcriptional corepressor 2 (Fussel-18 homolog) (LBX1 corepressor 1-like protein) (Ladybird homeobox corepressor 1-like protein) (Transcriptional corepressor Corl2) 1008 105,616 Chain (1); Compositional bias (6) FUNCTION: Acts as a TGF-beta antagonist in the nervous system (By similarity). Exhibits transcriptional repressor activity. {ECO:0000250, ECO:0000269|PubMed:18522874}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18522874}. Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with SMAD2 and SMAD3. {ECO:0000250}. TISSUE SPECIFICITY: Expression is restricted to adult and embryonic central nervous system. Expressed at high levels in the developing cerebellum, ventral metencephalon and myelencephalon at E12.5 (at protein level). In the adult cerebellum, expressed specifically in Purkinje cells. {ECO:0000269|PubMed:18522874}. +Q9WTX5 SKP1_MOUSE S-phase kinase-associated protein 1 (Cyclin-A/CDK2-associated protein p19) (S-phase kinase-associated protein 1A) (p19A) (p19skp1) 163 18,672 Chain (1); Cross-link (1); Modified residue (1); Region (1); Sequence conflict (1) Protein modification; protein ubiquitination. FUNCTION: Essential component of the SCF (SKP1-CUL1-F-box protein) ubiquitin ligase complex, which mediates the ubiquitination of proteins involved in cell cycle progression, signal transduction and transcription. In the SCF complex, serves as an adapter that links the F-box protein to CUL1. The functional specificity of the SCF complex depends on the F-box protein as substrate recognition component. SCF(BTRC) and SCF(FBXW11) direct ubiquitination of CTNNB1 and participate in Wnt signaling. SCF(FBXW11) directs ubiquitination of phosphorylated NFKBIA. SCF(BTRC) directs ubiquitination of NFKBIB, NFKBIE, ATF4, SMAD3, SMAD4, CDC25A, FBXO5, CEP68 and probably NFKB2. SCF(SKP2) directs ubiquitination of phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition. SCF(SKP2) directs ubiquitination of ORC1, CDT1, RBL2, ELF4, CDKN1A, RAG2, FOXO1A, and probably MYC and TAL1. SCF(FBXW7) directs ubiquitination of cyclin E, NOTCH1 released notch intracellular domain (NICD), and probably PSEN1. SCF(FBXW2) directs ubiquitination of GCM1. SCF(FBXO32) directs ubiquitination of MYOD1. SCF(FBXO7) directs ubiquitination of BIRC2 and DLGAP5. SCF(FBXO33) directs ubiquitination of YBX1. SCF(FBXO11) directs ubiquitination of BCL6 and DTL but does not seem to direct ubiquitination of TP53. SCF(BTRC) mediates the ubiquitination of NFKBIA at 'Lys-21' and 'Lys-22'; the degradation frees the associated NFKB1-RELA dimer to translocate into the nucleus and to activate transcription. SCF(CCNF) directs ubiquitination of CCP110. SCF(FBXL3) and SCF(FBXL21) direct ubiquitination of CRY1 and CRY2. SCF(FBXO9) directs ubiquitination of TTI1 and TELO2 (By similarity). {ECO:0000250|UniProtKB:P63208, ECO:0000269|PubMed:10097128, ECO:0000269|PubMed:12140560, ECO:0000269|PubMed:9990853}. PTM: Undergoes autophagy-mediated degradation in the liver in a time-dependent manner. {ECO:0000269|PubMed:29937374}. SUBUNIT: Component of multiple SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase complexes formed of CUL1, SKP1, RBX1 and a variable F-box domain-containing protein as substrate-specific subunit. Component of the SCF(FBXW11) complex containing FBXW11. Component of the SCF(SKP2) complex containing SKP2, in which it interacts directly with SKP1, SKP2 and RBX1. Component of the SCF(FBXW2) complex containing FBXw2. Component of the SCF(FBXO32) complex containing FBXO32. Component of the probable SCF(FBXO7) complex containing FBXO7. Component of the SCF(FBXO10) complex containing FBXO10. Component of the SCF(FBXO11) complex containing FBXO11. Component of the SCF(FBXO25) complex containing FBXO25. Component of the SCF(FBXO33) complex containing FBXO33. Component of the probable SCF(FBXO4) complex containing FBXO4. Component of the SCF(FBXO44) complex, composed of SKP1, CUL1 and FBXO44. Component of the SCF(BTRC) complex, composed of SKP1, CUL1 and BTRC. This complex binds phosphorylated NFKBIA. Part of a SCF complex consisting of CUL1, RBX1, SKP1 and FBXO2. Component of a SCF(SKP2)-like complex containing CUL1, SKP1, TRIM21 and SKP2. Component of the SCF(FBXO17) complex, composed of SKP1, CUL1 and FBXO17. Component of the SCF(FBXO27) complex, composed of SKP1, CUL1 and FBXO27. Component of the SCF(CCNF) complex consisting of CUL1, RBX1, SKP1 and CCNF. Component of the SCF(FBXL3) complex composed of CUL1, SKP1, RBX1 and FBXL3. Component of the SCF(FBXL21) complex composed of CUL1, SKP1, RBX1 and FBXL21. Component of the SCF(FBXO9) composed of CUL1, SKP1, RBX1 and FBXO9. Component of the SCF(FBXW7) composed of CUL1, SKP1, RBX1 and FBXW7. Component of the SCF(FBXW15) complex containing FBXW15 (PubMed:23319590). Interacts with CEP68 (By similarity). Interacts with FBXW15 (PubMed:23319590). Interacts with NOTCH2 (By similarity). {ECO:0000250|UniProtKB:P63208, ECO:0000269|PubMed:10097128, ECO:0000269|PubMed:11735228, ECO:0000269|PubMed:12140560, ECO:0000269|PubMed:19996097, ECO:0000269|PubMed:23319590, ECO:0000269|PubMed:9990853}. +P62281 RS11_MOUSE 40S ribosomal protein S11 158 18,431 Chain (1); Initiator methionine (1); Lipidation (1); Modified residue (8) PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}. +Q9Z0Z3 SKP2_MOUSE S-phase kinase-associated protein 2 (Cyclin-A/CDK2-associated protein p45) (F-box protein Skp2) (F-box/WD-40 protein 1) (FWD1) 424 47,766 Alternative sequence (2); Chain (1); Domain (1); Modified residue (5); Motif (1); Repeat (10); Sequence conflict (2) Protein modification; protein ubiquitination. FUNCTION: Substrate recognition component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins involved in cell cycle progression, signal transduction and transcription. The SCF complex provides substrate specificity and interacts with both, the E2 ubiquitin-conjugating enzyme and the substrate. Specifically recognizes phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition. Degradation of CDKN1B/p27kip also requires CKS1. Promotes ubiquitination and destruction of CDH1 in a CK1-Dependent Manner, thereby regulating cell migration (By similarity). {ECO:0000250, ECO:0000269|PubMed:10790373}.; FUNCTION: Through the ubiquitin-mediated proteasomal degradation of viral proteins may have an antiviral activity. {ECO:0000250|UniProtKB:Q13309}. PTM: Ubiquitinated by the APC/C complex, leading to its degradation by the proteasome. Deubiquitinated by USP13 (By similarity). {ECO:0000250}.; PTM: Acetylation at Lys-68 and Lys-71 increases stability through impairment of APC/C-mediated proteolysis and promotes cytoplasmic retention. Deacetylated by SIRT3 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Part of a SCF(SKP2) complex consisting of CUL1, RBX1, SKP1 and SKP2. Component of a SCF(SKP2)-like complex containing CUL1, SKP1, TRIM21 and SKP2. Interacts directly with CUL1 and SKP1. Interacts with CKS1. Interacts with the cyclin-A-CDK2 complex. Interacts with ORC1, phosphorylated CDT1, phosphorylated RBL2, ELF4, phosphorylated RAG2, FOXO1, UBP43, MYC, TOB1, TAL1 and KMT2A/MLL1. Interacts with TRIM21 (By similarity). {ECO:0000250}. +G3X939 SL9A3_MOUSE Sodium/hydrogen exchanger 3 829 93,104 Chain (1); Glycosylation (1); Intramembrane (3); Modified residue (7); Region (1); Topological domain (14); Transmembrane (10) INTRAMEM 12 23 Name=A/M1. {ECO:0000255}.; INTRAMEM 50 68 Name=B/M2. {ECO:0000255}.; INTRAMEM 401 421 Name=L. {ECO:0000255}. TRANSMEM 75 94 Helical; Name=C/M3. {ECO:0000255}.; TRANSMEM 108 128 Helical; Name=D/M4. {ECO:0000255}.; TRANSMEM 135 155 Helical; Name=E/M5. {ECO:0000255}.; TRANSMEM 176 197 Helical; Name=F/M5A. {ECO:0000255}.; TRANSMEM 206 227 Helical; Name=G/M5B. {ECO:0000255}.; TRANSMEM 248 269 Helical; Name=H/M6. {ECO:0000255}.; TRANSMEM 286 304 Helical; Name=I/M7. {ECO:0000255}.; TRANSMEM 336 357 Helical; Name=J/M8. {ECO:0000255}.; TRANSMEM 365 385 Helical; Name=K/M9. {ECO:0000255}.; TRANSMEM 431 451 Helical; Name=M/M10. {ECO:0000255}. TOPO_DOM 1 11 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 24 49 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 69 74 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 95 107 Extracellular. {ECO:0000305}.; TOPO_DOM 129 134 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 156 175 Extracellular. {ECO:0000305}.; TOPO_DOM 198 205 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 228 247 Extracellular. {ECO:0000305}.; TOPO_DOM 270 285 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 305 335 Extracellular. {ECO:0000305}.; TOPO_DOM 358 364 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 386 400 Extracellular. {ECO:0000305}.; TOPO_DOM 422 430 Extracellular. {ECO:0000305}.; TOPO_DOM 452 829 Cytoplasmic. {ECO:0000305}. FUNCTION: Involved in pH regulation to eliminate acids generated by active metabolism or to counter adverse environmental conditions. Major proton extruding system driven by the inward sodium ion chemical gradient. Plays an important role in signal transduction. {ECO:0000250|UniProtKB:P48764}. PTM: Phosphorylated by PKA, which inhibits activity. Phosphorylation at Ser-659 by SGK1 is associated with increased abundance at the cell membrane. {ECO:0000250|UniProtKB:P26432, ECO:0000250|UniProtKB:P26433}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:P26433, ECO:0000250|UniProtKB:P48764}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P48764}. Note=In intestinal epithelial cells, localizes to the ileal brush border. Phosphorylation at Ser-663 by SGK1 is associated with increased abundance at the cell membrane. Angiotensin-2 enhances apical expression (By similarity). {ECO:0000250|UniProtKB:P48764, ECO:0000250|UniProtKB:Q28362}. SUBUNIT: Binds SLC9A3R1 and SLC9A3R2. Interacts with CHP1, CHP2 and SHANK2. Interacts with PDZK1 (via C-terminal PDZ domain) (By similarity). Interacts with PDZD3 and interactions decrease in response to elevated calcium ion levels. Interacts with AHCYL1; the interaction is required for SLC9A3 activity (By similarity). {ECO:0000250|UniProtKB:P26432, ECO:0000250|UniProtKB:P26433, ECO:0000250|UniProtKB:P48764, ECO:0000250|UniProtKB:Q28362}. +Q8BZ00 SL9A9_MOUSE Sodium/hydrogen exchanger 9 (Na(+)/H(+) exchanger 9) (NHE-9) (Solute carrier family 9 member 9) 644 72,133 Chain (1); Transmembrane (12) TRANSMEM 21 41 Helical. {ECO:0000255}.; TRANSMEM 46 66 Helical. {ECO:0000255}.; TRANSMEM 127 147 Helical. {ECO:0000255}.; TRANSMEM 165 185 Helical. {ECO:0000255}.; TRANSMEM 204 224 Helical. {ECO:0000255}.; TRANSMEM 236 256 Helical. {ECO:0000255}.; TRANSMEM 278 298 Helical. {ECO:0000255}.; TRANSMEM 323 343 Helical. {ECO:0000255}.; TRANSMEM 365 385 Helical. {ECO:0000255}.; TRANSMEM 387 407 Helical. {ECO:0000255}.; TRANSMEM 430 450 Helical. {ECO:0000255}.; TRANSMEM 467 487 Helical. {ECO:0000255}. FUNCTION: May act in electroneutral exchange of protons for Na(+) across membranes. Involved in the effusion of Golgi luminal H(+) in exchange for cytosolic cations. Involved in organelle ion homeostasis by contributing to the maintenance of the unique acidic pH values of the Golgi and post-Golgi compartments in the cell (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q5BKR2 SL9B2_MOUSE Sodium/hydrogen exchanger 9B2 (NHA-oc) (Na(+)/H(+) exchanger NHA2) (Na(+)/H(+) exchanger-like domain-containing protein 2) (NHE domain-containing protein 2) (Soditlum/hydrogen exchanger-like domain-containing protein 2) (Solute carrier family 9 subfamily B member 2) 547 58,934 Alternative sequence (2); Chain (1); Modified residue (1); Sequence conflict (1); Site (2); Transmembrane (12) TRANSMEM 87 107 Helical. {ECO:0000255}.; TRANSMEM 115 135 Helical. {ECO:0000255}.; TRANSMEM 136 156 Helical. {ECO:0000255}.; TRANSMEM 207 227 Helical. {ECO:0000255}.; TRANSMEM 235 255 Helical. {ECO:0000255}.; TRANSMEM 266 286 Helical. {ECO:0000255}.; TRANSMEM 307 327 Helical. {ECO:0000255}.; TRANSMEM 340 360 Helical. {ECO:0000255}.; TRANSMEM 388 408 Helical. {ECO:0000255}.; TRANSMEM 425 445 Helical. {ECO:0000255}.; TRANSMEM 451 471 Helical. {ECO:0000255}.; TRANSMEM 493 513 Helical. {ECO:0000255}. FUNCTION: Na(+)/H(+) antiporter that extrudes Na(+) or Li(+) in exchange for external protons across the membrane (PubMed:18508966, PubMed:17988971). Contributes to the regulation of intracellular pH, sodium homeostasis, and cell volume. Plays an important role for insulin secretion and clathrin-mediated endocytosis in beta-cells (PubMed:23720317). Involved in sperm motility and fertility (PubMed:27010853). It is controversial whether SLC9B2 plays a role in osteoclast differentiation (PubMed:17988971) or not (PubMed:20441802, PubMed:22985540). {ECO:0000269|PubMed:17988971, ECO:0000269|PubMed:18508966, ECO:0000269|PubMed:20441802, ECO:0000269|PubMed:22985540, ECO:0000269|PubMed:23720317, ECO:0000269|PubMed:27010853}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18508966, ECO:0000269|PubMed:20441802}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000269|PubMed:17988971}; Multi-pass membrane protein {ECO:0000255}. Endosome membrane {ECO:0000269|PubMed:23720317}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:23720317}; Multi-pass membrane protein. Cell projection, cilium, flagellum membrane {ECO:0000269|PubMed:27010853}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000269|PubMed:20441802}; Multi-pass membrane protein {ECO:0000255}. Note=Strong colocalization with LAMP1 and TCIRG1 in osteoclasts (PubMed:20441802). In beta-cells colocalizes with RAB4A and SYP (PubMed:23720317). Localizes to the basolateral membrane of polarized osteoclasts (PubMed:20441802). On the contrary to (Ref.6) not detected at the mitochondrion membrane (PubMed:20441802, PubMed:23720317). {ECO:0000269|PubMed:17988971, ECO:0000269|PubMed:20441802, ECO:0000269|PubMed:23720317}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q86UD5}. TISSUE SPECIFICITY: Widely expressed (PubMed:18000046, PubMed:18508966, PubMed:17988971). However expression seems to be restricted to specific cell types within individual organs, e.g. osteoclasts in the bone, distal tubules of the kidney or beta-cells of Langerhans islets (PubMed:18508966, PubMed:17988971, PubMed:17698421, PubMed:23720317). In sperm specifically present in the principal piece of sperm tail (at protein level) (PubMed:27010853). {ECO:0000269|PubMed:17698421, ECO:0000269|PubMed:17988971, ECO:0000269|PubMed:18000046, ECO:0000269|PubMed:18508966, ECO:0000269|PubMed:23720317, ECO:0000269|PubMed:27010853}. +Q9QUM4 SLAF1_MOUSE Signaling lymphocytic activation molecule (SLAM family member 1) (CD antigen CD150) 343 38,094 Alternative sequence (1); Chain (1); Disulfide bond (2); Domain (2); Glycosylation (9); Modified residue (3); Motif (3); Mutagenesis (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 243 265 Helical. {ECO:0000255}. TOPO_DOM 25 242 Extracellular. {ECO:0000255}.; TOPO_DOM 266 343 Cytoplasmic. {ECO:0000255}. FUNCTION: Self-ligand receptor of the signaling lymphocytic activation molecule (SLAM) family. SLAM receptors triggered by homo- or heterotypic cell-cell interactions are modulating the activation and differentiation of a wide variety of immune cells and thus are involved in the regulation and interconnection of both innate and adaptive immune response. Activities are controlled by presence or absence of small cytoplasmic adapter proteins, SH2D1A/SAP and/or SH2D1B/EAT-2. SLAMF1-induced signal-transduction events in T-lymphocytes are different from those in B-cells. Two modes of SLAMF1 signaling seem to exist: one depending on SH2D1A (and perhaps SH2D1B) and another in which protein-tyrosine phosphatase 2C (PTPN11)-dependent signal transduction operates. Initially it has been proposed that association with SH2D1A prevents binding to inhibitory effectors including INPP5D/SHIP1 and PTPN11/SHP-2 (By similarity). However, signaling is also regulated by SH2D1A which can simultaneously interact with and recruit FYN which subsequently phosphorylates and activates SLAMF1 (By similarity). Mediates IL-2-independent proliferation of activated T-cells during immune responses and induces IFN-gamma production (PubMed:9126961, PubMed:12351401). Downstreaming signaling involves INPP5D, DOK1 and DOK2 leading to inhibited IFN-gamma production in T-cells, and PRKCQ, BCL10 and NFKB1 leading to increased T-cell activation and Th2 cytokine production (PubMed:11477403, PubMed:16847311, PubMed:15539155). Promotes T-cell receptor-induced IL-4 secretion by CD4(+) cells (PubMed:15123745). Inhibits antigen receptor-mediated production of IFN-gamma, but not IL-2, in CD4(-)/CD8(-) T-cells (PubMed:11477403). Required for IL-4 production by germinal centers T follicular helper (T(Fh))cells (PubMed:20525889). May inhibit CD40-induced signal transduction in monocyte-derived dendritic cells (By similarity). May play a role in allergic responses and may regulate allergen-induced Th2 cytokine and Th1 cytokine secretion (PubMed:16528012). In conjunction with SLAMF6 controls the transition between positive selection and the subsequent expansion and differentiation of the thymocytic natural killer T (NKT) cell lineage (PubMed:18031695). Involved in the peripheral differentiation of indifferent natural killer T (iNKT) cells toward a regulatory NKT2 type (PubMed:18606638). In macrophages involved in down-regulation of IL-12, TNF-alpha and nitric oxide in response to lipopolysaccharide (LPS) (PubMed:15123745). In B-cells activates the ERK signaling pathway independently of SH2D1A but implicating both, SYK and INPP5D, and activates Akt signaling dependent on SYK and SH2D1A (PubMed:15315965). In conjunction with CD84/SLAMF5 and SLAMF6 may be a negative regulator of the humoral immune response (PubMed:25926831). {ECO:0000250|UniProtKB:Q13291, ECO:0000269|PubMed:11477403, ECO:0000269|PubMed:15123745, ECO:0000269|PubMed:15315965, ECO:0000269|PubMed:15539155, ECO:0000269|PubMed:16528012, ECO:0000269|PubMed:16847311, ECO:0000269|PubMed:18031695, ECO:0000269|PubMed:18606638, ECO:0000269|PubMed:25926831, ECO:0000269|PubMed:9126961}.; FUNCTION: (Microbial infection) Involved in innate immune response against Gram-negative bacteria in macrophages; probably recognizes OmpC and/or OmpF on the bacterial surface, regulates phagosome maturation and recruitment of the PI3K complex II (PI3KC3-C2) leading to accumulated of PdtIns(3)P and NOX2 activity in the phagosomes (PubMed:20818396, PubMed:22493499). {ECO:0000269|PubMed:20818396, ECO:0000305|PubMed:22493499}. PTM: Phosphorylated on tyrosine residues by FYN (By similarity). {ECO:0000250|UniProtKB:Q13291, ECO:0000269|PubMed:11477403}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q13291}; Single-pass type I membrane protein. Note=Present on the surface of B-cells and T-cells. Located at the plasma membrane contacts between neighboring T cells. {ECO:0000250|UniProtKB:Q13291}. SUBUNIT: Interacts (via cytoplasmic domain) with SH2D1A and SH2D1B; SH2D1A mediates association with FYN; SH2D1A binds to phosphorylated and not phosphorylated ITSM 1 (PubMed:9774102, PubMed:16847311, PubMed:11477403.) Interacts (via cytoplasmic domain phosphorylated on tyrosine residues) with INPP5D and PTPN11; presence of SH2D1A facilitates binding to INPP5D (By similarity). Interacts with MAP4K1 (By similarity). Interacts with PIK3C3, BECN1 and UVRAG; indicative for an association with PI3K complex II (PI3KC3-C2) (PubMed:22493499). {ECO:0000250|UniProtKB:Q13291, ECO:0000269|PubMed:11477403, ECO:0000269|PubMed:11689425, ECO:0000269|PubMed:16847311, ECO:0000269|PubMed:20525889, ECO:0000269|PubMed:22493499, ECO:0000269|PubMed:9774102}. DOMAIN: The ITSMs (immunoreceptor tyrosine-based switch motifs) with the consensus sequence T-X-Y-X-X-[VI] present in SLAM family receptors have overlapping specificity for activating and inhibitory SH2 domain-containing binding partners. Especially they mediate the interaction with the SH2 domain of SH2D1A and SH2D1B. For SLAMF1 a 'two-out-of-three-pronged' mechanism is proposed involving threonine (position -2), phosphorylated tyrosine (position 0) and valine/isoleucine (position +3). Binding is mediated by either three 'prongs' (for high affinity binding involving ITSM 1) or a combination of any two also including non-phosphorylated Tyr-288 of ITSM 1 thus providing a positive feedback loop implicating SH2D1A-dependent recruitment of activating FYN. ITSM 2 needs to be phosphorylated on Tyr-335 for SH2D1A binding. {ECO:0000250|UniProtKB:Q13291}. +P63323 RS12_MOUSE 40S ribosomal protein S12 132 14,525 Chain (1); Initiator methionine (1); Modified residue (2) SUBCELLULAR LOCATION: Cytoplasm. +Q810B8 SLIK4_MOUSE SLIT and NTRK-like protein 4 837 94,538 Chain (1); Domain (3); Erroneous initiation (1); Glycosylation (3); Repeat (12); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 619 639 Helical. {ECO:0000255}. TOPO_DOM 19 618 Extracellular. {ECO:0000255}.; TOPO_DOM 640 837 Cytoplasmic. {ECO:0000255}. FUNCTION: It is involved in synaptogenesis and promotes synapse differentiation (By similarity). Suppresses neurite outgrowth (PubMed:14550773). {ECO:0000250|UniProtKB:Q8IW52, ECO:0000269|PubMed:14550773}. SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q8IW52}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q8IW52}. Cell membrane {ECO:0000250|UniProtKB:Q8IW52}. SUBUNIT: Interacts (via LRR 1 and 2 repeats) with PTPRD (via extracellular domain). TISSUE SPECIFICITY: In the adult, significant expression is detected only in the brain. Broadly expressed in embryonic brain with highest expression in subventricular zone, subplate, cortical plate, pyramidal cell layer of hippocampus, thalamus and hypothalamus. {ECO:0000269|PubMed:14550773}. +Q80TR4 SLIT1_MOUSE Slit homolog 1 protein (Slit-1) 1531 167,420 Chain (1); Disulfide bond (39); Domain (19); Erroneous initiation (1); Glycosylation (13); Repeat (20); Sequence conflict (5); Signal peptide (1) FUNCTION: Thought to act as molecular guidance cue in cellular migration, and function appears to be mediated by interaction with roundabout homolog receptors. During neural development involved in axonal navigation at the ventral midline of the neural tube and projection of axons to different regions (By similarity). SLIT1 and SLIT2 together seem to be essential for midline guidance in the forebrain by acting as repulsive signal preventing inappropriate midline crossing by axons projecting from the olfactory bulb. {ECO:0000250, ECO:0000269|PubMed:11804571, ECO:0000269|PubMed:12097499}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Interacts with GREM1 (By similarity) and ROBO1. {ECO:0000250, ECO:0000269|PubMed:10433822}. +Q9R1B9 SLIT2_MOUSE Slit homolog 2 protein (Slit-2) [Cleaved into: Slit homolog 2 protein N-product; Slit homolog 2 protein C-product] 1521 168,783 Chain (3); Disulfide bond (42); Domain (19); Glycosylation (12); Repeat (20); Sequence conflict (3); Signal peptide (1); Site (1) FUNCTION: Thought to act as molecular guidance cue in cellular migration, and function appears to be mediated by interaction with roundabout homolog receptors. During neural development involved in axonal navigation at the ventral midline of the neural tube and projection of axons to different regions. SLIT1 and SLIT2 seem to be essential for midline guidance in the forebrain by acting as repulsive signal preventing inappropriate midline crossing by axons projecting from the olfactory bulb. In spinal chord development, may play a role in guiding commissural axons once they reached the floor plate by modulating the response to netrin. In vitro, silences the attractive effect of NTN1 but not its growth-stimulatory effect and silencing requires the formation of a ROBO1-DCC complex. May be implicated in spinal chord midline post-crossing axon repulsion. In vitro, only commissural axons that crossed the midline responded to SLIT2. In the developing visual system, appears to function as repellent for retinal ganglion axons by providing a repulsion that directs these axons along their appropriate paths prior to, and after passage through, the optic chiasm. In vitro, collapses and repels retinal ganglion cell growth cones. Seems to play a role in branching and arborization of CNS sensory axons, and in neuronal cell migration. In vitro, Slit homolog 2 protein N-product, but not Slit homolog 2 protein C-product, repels olfactory bulb (OB) but not dorsal root ganglia (DRG) axons, induces OB growth cones collapse and induces branching of DRG axons. Seems to be involved in regulating leukocyte migration (By similarity). {ECO:0000250, ECO:0000269|PubMed:11804571, ECO:0000269|PubMed:12097499}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=The C-terminal cleavage protein is more diffusible than the larger N-terminal protein that is more tightly cell associated. {ECO:0000250}. SUBUNIT: Homodimer. Interacts with GREM1 (By similarity). Binds ROBO1 and ROBO2 with high affinity. {ECO:0000250}. DOMAIN: The leucine-rich repeat domain is sufficient for guiding both axon projection and neuronal migration, in vitro. TISSUE SPECIFICITY: Expressed in developing eye, in the optic stalk, and in the ventral diencephalon. {ECO:0000269|PubMed:10864954}. +Q9WVB4 SLIT3_MOUSE Slit homolog 3 protein (Slit-3) (Slit3) 1523 167,727 Chain (1); Disulfide bond (37); Domain (19); Glycosylation (12); Repeat (20); Sequence conflict (5); Signal peptide (1) FUNCTION: May act as molecular guidance cue in cellular migration, and function may be mediated by interaction with roundabout homolog receptors. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +O54988 SLK_MOUSE STE20-like serine/threonine-protein kinase (STE20-like kinase) (mSLK) (EC 2.7.11.1) (Etk4) (STE20-related kinase SMAK) (STE20-related serine/threonine-protein kinase) (STE20-related kinase) (Serine/threonine-protein kinase 2) 1233 141,457 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Coiled coil (2); Compositional bias (2); Domain (2); Erroneous initiation (1); Modified residue (21); Mutagenesis (1); Nucleotide binding (1); Sequence conflict (3); Site (1) FUNCTION: Mediates apoptosis and actin stress fiber dissolution. {ECO:0000269|PubMed:10611247}. PTM: Proteolytically cleaved by caspase-3. {ECO:0000269|PubMed:10611247}.; PTM: Autophosphorylated. {ECO:0000269|PubMed:9808774}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10611247, ECO:0000269|PubMed:9808774}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:10611247, ECO:0000269|PubMed:8346215, ECO:0000269|PubMed:9808774}. +Q3URD3 SLMAP_MOUSE Sarcolemmal membrane-associated protein (Sarcolemmal-associated protein) 845 96,933 Alternative sequence (5); Chain (1); Coiled coil (3); Domain (1); Erroneous initiation (2); Modified residue (3); Region (1); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 820 840 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 1 819 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 841 845 Extracellular. {ECO:0000255}. FUNCTION: May play a role during myoblast fusion. {ECO:0000269|PubMed:15086317}. SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Cytoplasm, myofibril, sarcomere, M line. Cytoplasm, myofibril, sarcomere, Z line. Note=Membrane-associated. Distributed in the transverse tubules and near the junctional sarcoplasmic reticulum (By similarity). Detected along the Z- and M-lines in cardiomyocytes (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 1: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Localizes to the centrosomes in a microtubule- dependent manner.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Localizes to the centrosomes in a microtubule- dependent manner. SUBUNIT: Homodimer. Interacts with myosin. {ECO:0000269|PubMed:15591093}. TISSUE SPECIFICITY: Expressed in proliferating myoblasts and differentiated myotubes (at protein level). Expressed in myoblasts, cardiac and skeletal muscles. {ECO:0000269|PubMed:10986292, ECO:0000269|PubMed:15086317}. +V9GXG1 SLN14_MOUSE Protein SLFN14 [Cleaved into: C-terminally truncated SLFN14 endoribonuclease (EC 3.1.-.-) (Schlafen family member 14)] 899 101,690 Chain (2); Region (2) FUNCTION: Protein SLFN14: Shows no ribosome-associated and endoribonuclease activities. {ECO:0000269|PubMed:25996083}.; FUNCTION: C-terminally truncated SLFN14 endoribonuclease: Displays polysome-associated endoribonuclease activity towards mRNAs and rRNAs (PubMed:25996083). May play a role in RNA surveillance pathways by recognizing stalled ribosomes and triggering endonucleolytic cleavage of aberrant mRNAs (Probable). Cleaves different types of rRNAs and mRNAs in a magnesium- and manganese-dependent and ATP-independent manner. Involved in correct maturation of megakaryocytes and especially important for proplatelet extension (By similarity). {ECO:0000250|UniProtKB:G1SRW8, ECO:0000250|UniProtKB:P0C7P3, ECO:0000269|PubMed:25996083, ECO:0000305|PubMed:25996083}. SUBCELLULAR LOCATION: Protein SLFN14: Nucleus {ECO:0000250|UniProtKB:P0C7P3}. SUBUNIT: C-terminally truncated SLFN14 endoribonuclease: Associates with ribosomes in an ATP-independent manner (PubMed:25996083). {ECO:0000269|PubMed:25996083}. TISSUE SPECIFICITY: Expressed in spleen (PubMed:19619625). {ECO:0000269|PubMed:19619625}. +P97430 SLPI_MOUSE Antileukoproteinase (ALP) (Secretory leukocyte protease inhibitor) 131 14,308 Chain (1); Disulfide bond (8); Domain (2); Mutagenesis (3); Region (1); Signal peptide (1); Site (1) FUNCTION: Acid-stable proteinase inhibitor with strong affinities for trypsin, chymotrypsin, elastase, and cathepsin G (PubMed:9126337). Modulates the innate immune response after bacterial infection (PubMed:12615907). Contributes to regulate the inflammatory and immune responses to the intracellular parasite L.major (PubMed:25030421). Down-regulates responses to bacterial lipopolysaccharide (LPS) (PubMed:9039268, PubMed:12615907, PubMed:25030421). Plays a role in regulating the activation of NF-kappa-B and inflammatory responses (PubMed:11017147, PubMed:12615907). Has antimicrobial activity against mycobacteria, but not against salmonella (PubMed:18322212). Contributes to normal resistance against infection by M.tuberculosis (PubMed:18322212). Required for normal resistance to L.major (PubMed:25030421). Required for normal wound healing, probably by preventing tissue damage by limiting protease activity (PubMed:11017147, PubMed:25030421). Together with ELANE, required for normal differentiation and proliferation of bone marrow myeloid cells (By similarity). {ECO:0000250|UniProtKB:P03973, ECO:0000269|PubMed:11017147, ECO:0000269|PubMed:12615907, ECO:0000269|PubMed:18322212, ECO:0000269|PubMed:25030421, ECO:0000269|PubMed:9039268, ECO:0000269|PubMed:9126337, ECO:0000269|PubMed:9351627, ECO:0000305}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18322212, ECO:0000269|PubMed:9126337}. TISSUE SPECIFICITY: Detected in bronchial epithelial cells (PubMed:18322212). Detected in bronchoalveolar fluid after infection with M.tuberculosis (at protein level) (PubMed:18322212). Highest expression in lung, spleen, intestine and epididymis with lower levels in liver and seminal vesicle. No expression in brain, heart, kidney and muscle. {ECO:0000269|PubMed:18322212, ECO:0000269|PubMed:9039268, ECO:0000269|PubMed:9126337, ECO:0000269|PubMed:9351627}. +Q9DCD2 SYF1_MOUSE Pre-mRNA-splicing factor SYF1 (XPA-binding protein 2) 855 99,988 Chain (1); Modified residue (2); Repeat (14); Sequence conflict (2) FUNCTION: Involved in pre-mRNA splicing as component of the spliceosome. Involved in transcription-coupled repair (TCR), transcription and pre-mRNA splicing. {ECO:0000250|UniProtKB:Q9HCS7}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q99PK0}. Note=Detected in the splicing complex carrying pre-mRNA. {ECO:0000250|UniProtKB:Q99PK0}. SUBUNIT: Associates with RNA polymerase II, the TCR-specific proteins CKN1/CSA and ERCC6/CSB, and XPA. Identified in the spliceosome C complex. Component of the XAB2 complex, a multimeric protein complex composed of XAB2, PRPF19, AQR, ZNF830, ISY1, and PPIE. Identified in a pentameric intron-binding (IB) complex composed of AQR, XAB2, ISY1, ZNF830 and PPIE that is incorporated into the spliceosome as a preassembled complex. The IB complex does not contain PRPF19. {ECO:0000250|UniProtKB:Q9HCS7}. +Q9D198 SYF2_MOUSE Pre-mRNA-splicing factor SYF2 (CCNDBP1-interactor) (mp29) (p29) 242 28,712 Chain (1); Coiled coil (1); Cross-link (2); Initiator methionine (1); Modified residue (1) FUNCTION: Involved in pre-mRNA splicing as component of the spliceosome. {ECO:0000250|UniProtKB:O95926}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12437976}. SUBUNIT: Identified in the spliceosome C complex. Interacts with CCNDBP1. {ECO:0000250|UniProtKB:O95926}. TISSUE SPECIFICITY: Abundantly expressed in the heart, liver and kidney. Expressed at lower level other tissues. {ECO:0000269|PubMed:12437976}. +Q6ZWN5 RS9_MOUSE 40S ribosomal protein S9 194 22,591 Chain (1); Cross-link (2); Domain (1); Modified residue (5); Sequence conflict (2) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. {ECO:0000250}. SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. {ECO:0000250}. +Q9ER99 RSCA1_MOUSE Regulatory solute carrier protein family 1 member 1 (Regulatory subunit of SGLT1) (Transporter regulator RS1) (mRS1) 582 61,251 Chain (1); Domain (1); Sequence conflict (7) FUNCTION: Mediates transcriptional and post-transcriptional regulation of SLC5A1. Inhibits a dynamin and PKC-dependent exocytotic pathway of SLC5A1. Also involved in transcriptional regulation of SLC22A2. Exhibits glucose-dependent, short-term inhibition of SLC5A1 and SLC22A2 by inhibiting the release of vesicles from the trans-Golgi network (By similarity). Regulates the expression of SLC5A1 in a tissue-specific manner and is specifically involved in its regulation in the small intestine. {ECO:0000250, ECO:0000269|PubMed:15601832}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15601832}. Nucleus {ECO:0000269|PubMed:15601832}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Note=Localizes at the inner side of the plasma membrane. SUBUNIT: Interacts with YRDC. {ECO:0000269|PubMed:16024787}. TISSUE SPECIFICITY: Expressed in epithelial and subepithelial cells of small intestine. {ECO:0000269|PubMed:15601832}. +Q3UFY4 RSH3A_MOUSE Radial spoke head protein 3 homolog A (A-kinase anchor protein RSPH3A) (Radial spoke head-like protein 2A) 516 58,786 Chain (1); Coiled coil (1); Compositional bias (1); Frameshift (1); Modified residue (1); Sequence conflict (1) FUNCTION: Functions as a protein kinase A-anchoring protein that scaffolds the cAMP-dependent protein kinase holoenzyme. May serve as a point of convergence for MAPK and PKA signaling in cilia (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:P12759}. SUBUNIT: Interacts with phosphorylated MAPK1. Interacts with MEK1. Interacts with PKA regulatory subunits PRKAR1A and PRKAR1B (By similarity). {ECO:0000250}. +Q9DA80 RSH3B_MOUSE Radial spoke head protein 3 homolog B (A-kinase anchor protein RSPH3B) (Radial spoke head-like protein 2B) 389 45,168 Chain (1); Coiled coil (1); Compositional bias (1); Modified residue (1) FUNCTION: Functions as a protein kinase A-anchoring protein that scaffolds the cAMP-dependent protein kinase holoenzyme. May serve as a point of convergence for MAPK and PKA signaling in cilia (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:P12759}. SUBUNIT: Interacts with phosphorylated MAPK1. Interacts with MEK1. Interacts with PKA regulatory subunits PRKAR1A and PRKAR1B (By similarity). {ECO:0000250}. +Q5SSG5 RSLAB_MOUSE Ras-like protein family member 10B 203 23,229 Chain (1); Lipidation (1); Modified residue (1); Motif (1); Nucleotide binding (3); Propeptide (1); Region (1) FUNCTION: May facilitate the release of atrial natriuretic peptide by cardiomyocytes and hence play a role in the regulation of arterial pressure. {ECO:0000269|PubMed:17984325}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. SUBUNIT: Interacts with CADPS. {ECO:0000269|PubMed:17984325}. TISSUE SPECIFICITY: Expressed in heart and brain. In the brain, expression restricted to neurons of the cortex, hippocampus and cerebellum. Sparse expression in the brainstem and almost absent in the hypothalamic region. In the heart, expressed in cardiomyocytes. Not detected in interstitial tissue or vascular cells. {ECO:0000269|PubMed:17984325}. +Q9WUA2 SYFB_MOUSE Phenylalanine--tRNA ligase beta subunit (EC 6.1.1.20) (Phenylalanyl-tRNA synthetase beta subunit) (PheRS) 589 65,697 Chain (1); Domain (1); Sequence conflict (2) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NSD9}. SUBUNIT: Heterotetramer; dimer of two heterodimers formed by FARSA and FARSB. {ECO:0000250|UniProtKB:Q9NSD9}. +Q99M01 SYFM_MOUSE Phenylalanine--tRNA ligase, mitochondrial (EC 6.1.1.20) (Phenylalanyl-tRNA synthetase) (PheRS) 451 52,337 Binding site (3); Chain (1); Domain (1); Modified residue (1); Region (3); Sequence conflict (4); Transit peptide (1) FUNCTION: Is responsible for the charging of tRNA(Phe) with phenylalanine in mitochondrial translation. To a lesser extent, also catalyzes direct attachment of m-Tyr (an oxidized version of Phe) to tRNA(Phe), thereby opening the way for delivery of the misacylated tRNA to the ribosome and incorporation of ROS-damaged amino acid into proteins (By similarity). {ECO:0000250|UniProtKB:O95363}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000305}. Mitochondrion {ECO:0000250|UniProtKB:Q6AYQ3}. SUBUNIT: Monomer. {ECO:0000250}. +A2AI08 TPRN_MOUSE Taperin 749 80,089 Chain (1); Compositional bias (2); Erroneous initiation (4); Frameshift (2); Modified residue (4); Sequence conflict (7) SUBCELLULAR LOCATION: Cell projection, stereocilium {ECO:0000269|PubMed:20170899}. Note=Localized prominently at the taper regions of hair cell stereocilia. TISSUE SPECIFICITY: Expressed in the sensory epithelia of the organ of Corti and vestibular end organs and, to a lesser extent, in Reisner's membrane and the spiral ligament (at protein level). At postnatal day 2, expression is detected in cochlea, liver, brain, kidney, heart and lung. {ECO:0000269|PubMed:20170898, ECO:0000269|PubMed:20170899}. +Q7M724 TR106_MOUSE Taste receptor type 2 member 106 (T2R106) (mT2R44) 308 35,498 Chain (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 8 28 Helical; Name=1. {ECO:0000255}.; TRANSMEM 42 62 Helical; Name=2. {ECO:0000255}.; TRANSMEM 79 99 Helical; Name=3. {ECO:0000255}.; TRANSMEM 125 145 Helical; Name=4. {ECO:0000255}.; TRANSMEM 180 200 Helical; Name=5. {ECO:0000255}.; TRANSMEM 228 248 Helical; Name=6. {ECO:0000255}.; TRANSMEM 258 278 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 7 Extracellular. {ECO:0000255}.; TOPO_DOM 29 41 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 63 78 Extracellular. {ECO:0000255}.; TOPO_DOM 100 124 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 146 179 Extracellular. {ECO:0000255}.; TOPO_DOM 201 227 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 249 257 Extracellular. {ECO:0000255}.; TOPO_DOM 279 308 Cytoplasmic. {ECO:0000255}. FUNCTION: Putative taste receptor which may play a role in the perception of bitterness. {ECO:0000305}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9CQ37 UBE2T_MOUSE Ubiquitin-conjugating enzyme E2 T (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme T) (Ubiquitin carrier protein T) (Ubiquitin-protein ligase T) 204 22,975 Active site (1); Chain (1); Cross-link (4); Modified residue (1) Protein modification; protein ubiquitination. FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes monoubiquitination. Involved in mitomycin-C (MMC)-induced DNA repair: acts as a specific E2 ubiquitin-conjugating enzyme for the Fanconi anemia complex by associating with E3 ubiquitin-protein ligase FANCL and catalyzing monoubiquitination of FANCD2, a key step in the DNA damage pathway. Also mediates monoubiquitination of FANCL and FANCI. May contribute to ubiquitination and degradation of BRCA1. In vitro able to promote polyubiquitination using all 7 ubiquitin Lys residues, but may prefer 'Lys-11'-, 'Lys-27'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination. {ECO:0000250|UniProtKB:Q9NPD8}. PTM: Auto-ubiquitinated. Effects of auto-monoubiquitination at Lys-91 and Lys-181 are unclear. {ECO:0000250|UniProtKB:Q9NPD8}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NPD8}. Note=Accumulates to chromatin. {ECO:0000250|UniProtKB:Q9NPD8}. SUBUNIT: Interacts with FANCL and BRCA1. {ECO:0000250|UniProtKB:Q9NPD8}. +Q3UE37 UBE2Z_MOUSE Ubiquitin-conjugating enzyme E2 Z (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme Z) (Uba6-specific E2 conjugating enzyme 1) (Use1) (Ubiquitin carrier protein Z) (Ubiquitin-protein ligase Z) 356 38,368 Active site (1); Chain (1); Erroneous initiation (2); Frameshift (1); Modified residue (1); Sequence conflict (7) Protein modification; protein ubiquitination. FUNCTION: Catalyzes the covalent attachment of ubiquitin to other proteins. Specific substrate for UBA6, not charged with ubiquitin by UBE1. May be involved in apoptosis regulation. {ECO:0000255|PROSITE-ProRule:PRU00388}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H832}. Nucleus {ECO:0000250|UniProtKB:Q9H832}. +Q9ES34 UBE3B_MOUSE Ubiquitin-protein ligase E3B (EC 2.3.2.26) (HECT-type ubiquitin transferase E3B) 1070 122,762 Active site (1); Chain (1); Domain (2); Erroneous initiation (1); Modified residue (2) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. High expression is observed in developing central nervous system. {ECO:0000269|PubMed:12837265, ECO:0000269|PubMed:23200864}. +P61089 UBE2N_MOUSE Ubiquitin-conjugating enzyme E2 N (EC 2.3.2.23) (Bendless-like ubiquitin-conjugating enzyme) (E2 ubiquitin-conjugating enzyme N) (Ubc13) (Ubiquitin carrier protein N) (Ubiquitin-protein ligase N) 152 17,138 Active site (1); Chain (1); Cross-link (1); Frameshift (1); Modified residue (1); Sequence conflict (1) Protein modification; protein ubiquitination. FUNCTION: The UBE2V1-UBE2N and UBE2V2-UBE2N heterodimers catalyze the synthesis of non-canonical 'Lys-63'-linked polyubiquitin chains (PubMed:22424771, PubMed:28039360). This type of polyubiquitination does not lead to protein degradation by the proteasome. Mediates transcriptional activation of target genes. Plays a role in the control of progress through the cell cycle and differentiation. Plays a role in the error-free DNA repair pathway and contributes to the survival of cells after DNA damage. Acts together with the E3 ligases, HLTF and SHPRH, in the 'Lys-63'-linked poly-ubiquitination of PCNA upon genotoxic stress, which is required for DNA repair. Appears to act together with E3 ligase RNF5 in the 'Lys-63'-linked polyubiquitination of JKAMP thereby regulating JKAMP function by decreasing its association with components of the proteasome and ERAD. Promotes TRIM5 capsid-specific restriction activity and the UBE2V1-UBE2N heterodimer acts in concert with TRIM5 to generate 'Lys-63'-linked polyubiquitin chains which activate the MAP3K7/TAK1 complex which in turn results in the induction and expression of NF-kappa-B and MAPK-responsive inflammatory genes. {ECO:0000250|UniProtKB:P61088, ECO:0000269|PubMed:22424771, ECO:0000269|PubMed:28039360}. PTM: Conjugation to ISG15 impairs formation of the thioester bond with ubiquitin but not interaction with UBE2V2. {ECO:0000250|UniProtKB:P61088}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P61088}. Cytoplasm {ECO:0000250|UniProtKB:P61088}. SUBUNIT: Heterodimer with UBE2V2 (By similarity). Interacts (UBE2V2-UBE2N heterodimer) with the E3 ligase STUB1 (via the U-box domain); the complex has a specific 'Lys-63'-linked polyubiquitination activity (By similarity). Interacts with RNF8 and RNF168 (By similarity). Interacts with RNF11 (By similarity). Interacts with the E3 ligases, HLTF and SHPRH; the interactions promote the 'Lys-63'-linked polyubiquitination of PCNA upon genotoxic stress and lead to DNA repair (By similarity). Interacts with ARIH2 (via RING-type 2) (By similarity). Interacts with OTUB1; leading to inhibit E2-conjugating activity (By similarity). Interacts with GPS2; leading to inhibit E2-conjugating activity (PubMed:22424771). {ECO:0000250|UniProtKB:P61088, ECO:0000269|PubMed:22424771}. +Q9Z2M6 UBL3_MOUSE Ubiquitin-like protein 3 (Membrane-anchored ubiquitin-fold protein) (MUB) (MmMUB) (Protein HCG-1) 117 13,180 Beta strand (8); Chain (1); Domain (1); Helix (1); Lipidation (2); Modified residue (1); Propeptide (1); Turn (2) SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. +Q9CQ84 UBL4B_MOUSE Ubiquitin-like protein 4B 188 20,518 Chain (1); Compositional bias (2); Domain (1); Frameshift (1) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16872915}. TISSUE SPECIFICITY: Expressed specifically in post-meiotic male germ cells of the testis. Abundantly expressed in stage 14-16 spermatids. {ECO:0000269|PubMed:16872915}. +Q9D9M2 UBP12_MOUSE Ubiquitin carboxyl-terminal hydrolase 12 (EC 3.4.19.12) (Deubiquitinating enzyme 12) (Ubiquitin thioesterase 12) (Ubiquitin-hydrolyzing enzyme 1) (Ubiquitin-specific-processing protease 12) 370 42,914 Active site (2); Alternative sequence (1); Chain (1); Domain (1); Metal binding (4) FUNCTION: Deubiquitinating enzyme. Has almost no deubiquitinating activity by itself and requires the interaction with WDR48 to have a high activity. Not involved in deubiquitination of monoubiquitinated FANCD2. {ECO:0000250|UniProtKB:O75317}. SUBUNIT: Interacts with WDR48. Interacts with WDR20. Component of the USP12/WDR20/WDR48 deubiquitinating complex. {ECO:0000250|UniProtKB:O75317}. +Q4G0F8 UBN1_MOUSE Ubinuclein-1 (Ubiquitously expressed nuclear protein) 1135 122,336 Alternative sequence (2); Chain (1); Coiled coil (1); Compositional bias (2); Erroneous gene model prediction (1); Modified residue (11); Sequence conflict (4) FUNCTION: Acts as a novel regulator of senescence. Involved in the formation of senescence-associated heterochromatin foci (SAHF), which represses expression of proliferation-promoting genes. Binds to proliferation-promoting genes. May be required for replication-independent chromatin assembly (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}. Nucleus, PML body {ECO:0000250}. Cell junction, tight junction {ECO:0000269|PubMed:18823282}. Note=Localized as a nuclear speckled-like pattern in proliferating primary fibroblasts. Colocalizes with HIRA, PML and SP100 in PML bodies of senescent cells. Colocalizes with CLDN1. Detected along the upper granular cell layer of epidermis. When overexpressed, accumulates in the nucleus in cells showing defective cytokinesis (By similarity). Colocalizes with TJP1. {ECO:0000250}. SUBUNIT: Component of a complex that includes at least ASF1A, CABIN1, HIRA, histone H3.3 and UBN1. Interacts with HIRA (via WD repeat domain); the interaction is direct. Interacts with ASF1A, CEBPA, TJP1, TJP2 and TJP3 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in bile canaliculi in liver, in bronchiolar epithelium in lung and in tubular structures of gland ducts inside the olfactory epithelium and tongue epithelium. {ECO:0000269|PubMed:18823282}. +Q80WC1 UBN2_MOUSE Ubinuclein-2 1314 141,740 Alternative sequence (7); Chain (1); Compositional bias (3); Cross-link (1); Erroneous initiation (1); Modified residue (12); Sequence conflict (2) +P52479 UBP10_MOUSE Ubiquitin carboxyl-terminal hydrolase 10 (EC 3.4.19.12) (Deubiquitinating enzyme 10) (Ubiquitin thioesterase 10) (Ubiquitin-specific-processing protease 10) 792 87,022 Active site (2); Alternative sequence (1); Chain (1); Domain (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (11); Region (1); Sequence conflict (7) FUNCTION: Hydrolase that can remove conjugated ubiquitin from target proteins such as p53/TP53, BECN1, SNX3 and CFTR. Acts as an essential regulator of p53/TP53 stability: in unstressed cells, specifically deubiquitinates p53/TP53 in the cytoplasm, leading to counteract MDM2 action and stabilize p53/TP53. Following DNA damage, translocates to the nucleus and deubiquitinates p53/TP53, leading to regulate the p53/TP53-dependent DNA damage response. Component of a regulatory loop that controls autophagy and p53/TP53 levels: mediates deubiquitination of BECN1, a key regulator of autophagy, leading to stabilize the PIK3C3/VPS34-containing complexes. In turn, PIK3C3/VPS34-containing complexes regulate USP10 stability, suggesting the existence of a regulatory system by which PIK3C3/VPS34-containing complexes regulate p53/TP53 protein levels via USP10 and USP13. Does not deubiquitinate MDM2. Deubiquitinates CFTR in early endosomes, enhancing its endocytic recycling. Involved in a TANK-dependent negative feedback response to attenuate NF-kappaB activation via deubiquitinating IKBKG or TRAF6 in response to interleukin-1-beta (IL1B) stimulation or upon DNA damage. Deubiquitinates TBX21 leading to its stabilization. {ECO:0000250|UniProtKB:Q14694}. PTM: Phosphorylated by ATM following DNA damage, leading to stablization and translocation it to the nucleus. {ECO:0000250}.; PTM: Ubiquitinated. Deubiquitinated by USP13 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14694}. Nucleus {ECO:0000250|UniProtKB:Q14694}. Early endosome {ECO:0000250|UniProtKB:Q14694}. Note=Cytoplasmic in normal conditions (By similarity). After DNA damage, translocates to the nucleus following phosphorylation by ATM (By similarity). {ECO:0000250|UniProtKB:Q14694}. SUBUNIT: Found in a deubiquitination complex with TANK, USP10 and ZC3H12A; this complex inhibits genotoxic stress- or interleukin-1-beta (IL1B)-mediated NF-kappaB activation by promoting IKBKG or TRAF6 deubiquitination. Interacts with IKBKG; this interaction increases in response to DNA damage. Interacts with TANK; this interaction increases in response to DNA damage. Interacts with TRAF6; this interaction increases in response to DNA damage. Interacts with ZC3H12A; this interaction increases in response to DNA damage. Interacts with G3BP, which may regulate its function. Interacts with p53/TP53, SNX3 and CFTR. Interacts with TBX21. {ECO:0000250|UniProtKB:Q14694}. +Q9QZL6 UBP21_MOUSE Ubiquitin carboxyl-terminal hydrolase 21 (EC 3.4.19.12) (Deubiquitinating enzyme 21) (Ubiquitin thioesterase 21) (Ubiquitin-specific-processing protease 21) 566 62,673 Active site (2); Chain (1); Domain (1); Metal binding (4); Motif (1); Mutagenesis (3); Sequence conflict (2) FUNCTION: Deubiquitinates histone H2A, a specific tag for epigenetic transcriptional repression, thereby acting as a coactivator. Deubiquitination of histone H2A releaves the repression of di- and trimethylation of histone H3 at 'Lys-4', resulting in regulation of transcriptional initiation. Regulates gene expression via histone H2A deubiquitination. Also capable of removing NEDD8 from NEDD8 conjugates but has no effect on Sentrin-1 conjugates. Deubiquitinates BAZ2A/TIP5 leading to its stabilization (By similarity). {ECO:0000250|UniProtKB:Q9UK80, ECO:0000269|PubMed:18172164}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Interacts with BEND3 and BAZ2A/TIP5. {ECO:0000250|UniProtKB:Q9UK80}. +O88623 UBP2_MOUSE Ubiquitin carboxyl-terminal hydrolase 2 (EC 3.4.19.12) (41 kDa ubiquitin-specific protease) (Deubiquitinating enzyme 2) (Ubiquitin thioesterase 2) (Ubiquitin-specific-processing protease 2) 613 68,845 Active site (2); Alternative sequence (5); Chain (1); Domain (1); Metal binding (4); Region (2); Sequence conflict (1) FUNCTION: Hydrolase that deubiquitinates polyubiquitinated target proteins such as MDM2, MDM4 and CCND1 (By similarity). Isoform 1 and isoform 2 possess both ubiquitin-specific peptidase and isopeptidase activities (By similarity). Deubiquitinates MDM2 without reversing MDM2-mediated p53/TP53 ubiquitination and thus indirectly promotes p53/TP53 degradation and limits p53 activity (By similarity). Has no deubiquitinase activity against p53/TP53 (By similarity). Prevents MDM2-mediated degradation of MDM4 (By similarity). Plays a role in the G1/S cell-cycle progression in normal and cancer cells (By similarity). Plays a role in the regulation of myogenic differentiation of embryonic muscle cells (By similarity). Regulates the circadian clock by modulating its intrinsic circadian rhythm and its capacity to respond to external cues (PubMed:23213472, PubMed:25238854, PubMed:26756164). Associates with clock proteins and deubiquitinates core clock component PER1 but does not affect its overall stability (PubMed:23213472). Regulates the nucleocytoplasmic shuttling and nuclear retention of PER1 and its repressive role on the clock transcription factors CLOCK and ARNTL/BMAL1 (PubMed:25238854). {ECO:0000250|UniProtKB:O75604, ECO:0000250|UniProtKB:Q5U349, ECO:0000269|PubMed:23213472, ECO:0000269|PubMed:25238854}.; FUNCTION: Isoform 2: Circadian clock output effector that regulates Ca(2+) absorption in the small intestine. Probably functions by regulating protein levels of the membrane scaffold protein PDZD3 in a rhythmic manner, and is therefore likely to control Ca(2+) membrane permeability mediated by the Ca(2+) channel TRPV6 in the intestine. {ECO:0000269|PubMed:26756164}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14686789}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:14686789}. Note=Localizes in the spermatid head in late-elongating spermatids in the thin area between the outer acrosomal membrane and the plasma membrane. {ECO:0000250|UniProtKB:Q5U349}.; SUBCELLULAR LOCATION: Isoform 2: Nucleus {ECO:0000250|UniProtKB:Q5U349}. Membrane {ECO:0000269|PubMed:26756164}; Peripheral membrane protein {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:26756164}. Note=Predominantly expressed at membranes. {ECO:0000269|PubMed:26756164}. SUBUNIT: Found in trimeric complex with MDM2 and MDM4 and USP2. Interacts with CCND1; the interaction is direct and promotes its stabilization by antagonizing ubiquitin-dependent degradation. Interacts (via N-terminus and C-terminus) with MDM2. Interacts with MDM4 and PER1 (By similarity). Homooligomer. Interacts with KCNQ1; counteracts the NEDD4L-specific down-regulation of I(Ks) and restores plasma membrane localization of KCNQ1 (By similarity). Isoform 2: Interacts with PDZD3 and CLTC (PubMed:26756164). {ECO:0000250|UniProtKB:O75604, ECO:0000250|UniProtKB:Q5U349, ECO:0000269|PubMed:14686789}. DOMAIN: The different N-terminus extensions of isoform 1 and isoform 2 determine their respective subcellular localization and differentiel effect on myoblast fusion and accumulation of muscle-specific proteins. The different N-terminus extensions of isoform 1 and isoform 4 are not essential for their catalytic activity. {ECO:0000250|UniProtKB:Q5U349}. TISSUE SPECIFICITY: Isoform 1: Expressed in heart, liver, kidney, pancreas and to a lower extent in skeletal muscle, brain and testis (at protein level) (PubMed:14686789). Expressed in testis, brain, heart and skeletal muscle (PubMed:14686789, PubMed:26756164). Not detected in the small intestine (PubMed:26756164). Isoform 2: Expressed in the small intestine (PubMed:26756164). {ECO:0000269|PubMed:14686789, ECO:0000269|PubMed:26756164}. +B1AY13 UBP24_MOUSE Ubiquitin carboxyl-terminal hydrolase 24 (EC 3.4.19.12) (Deubiquitinating enzyme 24) (Ubiquitin thioesterase 24) (Ubiquitin-specific-processing protease 24) 2617 294,001 Active site (2); Alternative sequence (2); Chain (1); Compositional bias (2); Domain (2); Modified residue (11) FUNCTION: Protease that can remove conjugated ubiquitin from target proteins and polyubiquitin chains. Deubiquitinates DDB2, preventing its proteasomal degradation (By similarity). {ECO:0000250}. +Q5I043 UBP28_MOUSE Ubiquitin carboxyl-terminal hydrolase 28 (EC 3.4.19.12) (Deubiquitinating enzyme 28) (Ubiquitin thioesterase 28) (Ubiquitin-specific-processing protease 28) 1051 119,318 Active site (2); Alternative sequence (1); Chain (1); Cross-link (1); Domain (2); Modified residue (5); Sequence conflict (2) FUNCTION: Deubiquitinase involved in DNA damage response checkpoint and MYC proto-oncogene stability. Involved in DNA damage induced apoptosis by specifically deubiquitinating proteins of the DNA damage pathway such as CLSPN. Also involved in G2 DNA damage checkpoint, by deubiquitinating CLSPN, and preventing its degradation by the anaphase promoting complex/cyclosome (APC/C). In contrast, it does not deubiquitinate PLK1. Specifically deubiquitinates MYC in the nucleoplasm, leading to prevent MYC degradation by the proteasome: acts by specifically interacting with FBXW7 (FBW7alpha) in the nucleoplasm and counteracting ubiquitination of MYC by the SCF(FBXW7) complex. Deubiquitinates ZNF304, hence preventing ZNF304 degradation by the proteasome and leading to the activated KRAS-mediated promoter hypermethylation and transcriptional silencing of tumor suppressor genes (TSGs) in a subset of colorectal cancers (CRC) cells. {ECO:0000250|UniProtKB:Q96RU2}. PTM: Degraded upon nickel ion level or hypoxia exposure. {ECO:0000250}.; PTM: Phosphorylated upon DNA damage at Ser-67 and Ser-720, by ATM or ATR. Phosphorylated by PRKD1. {ECO:0000250|UniProtKB:Q96RU2}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}. SUBUNIT: Interacts with ZNF304. Interacts with PRKD1. Interacts with TP53BP1. Interacts with FBXW7; following DNA damage, dissociates from FBXW7 leading to degradation of MYC. {ECO:0000250|UniProtKB:Q96RU2}. +Q8BUM9 UBP43_MOUSE Ubiquitin carboxyl-terminal hydrolase 43 (EC 3.4.19.12) (Deubiquitinating enzyme 43) (Ubiquitin thioesterase 43) (Ubiquitin-specific-processing protease 43) 1132 123,874 Active site (2); Alternative sequence (2); Chain (1); Domain (1); Erroneous initiation (2); Modified residue (2); Sequence conflict (3) FUNCTION: May recognize and hydrolyze the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins (By similarity). {ECO:0000250}. +P62069 UBP46_MOUSE Ubiquitin carboxyl-terminal hydrolase 46 (EC 3.4.19.12) (Deubiquitinating enzyme 46) (Ubiquitin thioesterase 46) (Ubiquitin-specific-processing protease 46) 366 42,442 Active site (2); Chain (1); Domain (1); Metal binding (4); Mutagenesis (1) FUNCTION: Deubiquitinating enzyme that plays a role in behavior, possibly by regulating GABA action. May act by mediating the deubiquitination of GAD1/GAD67 (PubMed:19465912). Has almost no deubiquitinating activity by itself and requires the interaction with WDR48 to have a high activity. Not involved in deubiquitination of monoubiquitinated FANCD2 (By similarity). {ECO:0000250|UniProtKB:P62068, ECO:0000269|PubMed:19465912}. SUBUNIT: Interacts with WDR48. Interacts with WDR20. {ECO:0000250|UniProtKB:P62068}. +Q8C0R0 UBP37_MOUSE Ubiquitin carboxyl-terminal hydrolase 37 (EC 3.4.19.12) (Deubiquitinating enzyme 37) (Ubiquitin thioesterase 37) (Ubiquitin-specific-processing protease 37) 979 110,063 Active site (2); Alternative sequence (1); Chain (1); Domain (4); Modified residue (5); Motif (6); Sequence conflict (1) FUNCTION: Deubiquitinase that antagonizes the anaphase-promoting complex (APC/C) during G1/S transition by mediating deubiquitination of cyclin-A (CCNA1 and CCNA2), thereby promoting S phase entry. Specifically mediates deubiquitination of 'Lys-11'-linked polyubiquitin chains, a specific ubiquitin-linkage type mediated by the APC/C complex. Also mediates deubiquitination of 'Lys-48'-linked polyubiquitin chains in vitro. Phosphorylation at Ser-628 during G1/S phase maximizes the deubiquitinase activity, leading to prevent degradation of cyclin-A (CCNA1 and CCNA2). Plays an important role in the regulation of DNA replication by stabilizing the licensing factor CDT1. {ECO:0000250|UniProtKB:Q86T82}. PTM: Polyubiquitinated via 'Lys-11'-linked ubiquitin by the APC(CDH1) complex during late mitosis, leading to its degradation. Able to mediate auto-deubiquitination. {ECO:0000250|UniProtKB:Q86T82}.; PTM: Phosphorylated at Ser-628 by CDK2 during G1/S phase but not during mitosis; phosphorylation at Ser-628 is required for deubiquitinase activity. Also polyubiquitinated during early G1 phase, without leading to degradation. {ECO:0000250|UniProtKB:Q86T82}. SUBUNIT: Interacts with FZR1/CDH1. Interacts with CDT1. {ECO:0000250|UniProtKB:Q86T82}. DOMAIN: The KEN box 3 is required for interaction with FZR1/CDH1 and is essential for APC(CDH1)-mediated ubiquitination. {ECO:0000250|UniProtKB:Q86T82}. +Q6WKZ8 UBR2_MOUSE E3 ubiquitin-protein ligase UBR2 (EC 2.3.2.27) (N-recognin-2) (RING-type E3 ubiquitin transferase UBR2) (Ubiquitin-protein ligase E3-alpha-2) (Ubiquitin-protein ligase E3-alpha-II) 1755 199,155 Alternative sequence (2); Chain (1); Coiled coil (1); Erroneous initiation (2); Initiator methionine (1); Modified residue (1); Sequence caution (1); Sequence conflict (11); Zinc finger (2) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. Plays a critical role in chromatin inactivation and chromosome-wide transcriptional silencing during meiosis via ubiquitination of histone H2A. Binds leucine and is a negative regulator of the leucine-mTOR signaling pathway, thereby controlling cell growth (By similarity). Required for spermatogenesis, promotes, with Tex19.1, SPO11-dependent recombination foci to accumulate and drive robust homologous chromosome synapsis (PubMed:28708824). Polyubiquitinates LINE-1 retrotransposon encoded, LIRE1, which induces degradation, inhibiting LINE-1 retranstoposon mobilization (PubMed:28806172). {ECO:0000250, ECO:0000269|PubMed:14585983, ECO:0000269|PubMed:20080676, ECO:0000269|PubMed:28708824, ECO:0000269|PubMed:28806172}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14585983, ECO:0000269|PubMed:20080676}. Note=Associated with chromatin during meiosis. SUBUNIT: Interacts with UBE2B; promotes the UBE2B-H2A interaction and the ubiquitination of histone H2A by UBE2B and UBR2 (PubMed:14585983, PubMed:20080676). Interacts with RECQL4 (By similarity). Interacts with Tex19.1 and Tex19.2; does not lead to Tex19.1 degradation and stabilizes it (PubMed:21103378). Interacts with L1RE1 (PubMed:28806172). Interacts with CASP8 (By similarity). {ECO:0000250|UniProtKB:Q8IWV8, ECO:0000269|PubMed:14585983, ECO:0000269|PubMed:20080676, ECO:0000269|PubMed:21103378, ECO:0000269|PubMed:28806172}. DOMAIN: The RING-H2 zinc finger is an atypical RING finger with a His ligand in place of the fourth Cys of the classical motif.; DOMAIN: The UBR-type zinc finger forms a pocket that mediates recognition of type 1 N-degrons. It exhibits preference for Arginine in first position, has poor affinity for histidine, and doesn't bind acetylated peptides (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in skeletal muscle. Also expressed in heart, kidney and testis. Expressed in acinar cells of the pancreas. In testes, expressed primarily in spermatocytes. Expressed in cerebellum (PubMed:28806172). {ECO:0000269|PubMed:14585983, ECO:0000269|PubMed:15548684, ECO:0000269|PubMed:16311597, ECO:0000269|PubMed:28806172}. +P15975 UBP53_MOUSE Inactive ubiquitin carboxyl-terminal hydrolase 53 (Inactive ubiquitin-specific peptidase 53) (Per-hexamer repeat protein 3) (Protein mambo) 1069 119,255 Alternative sequence (2); Chain (1); Domain (1); Mutagenesis (1); Sequence caution (1); Sequence conflict (1) FUNCTION: Tight junction-associated protein that is involved in the survival of auditory hair cells and hearing. Maybe by modulating the barrier properties and mechanical stability of tight junctions (PubMed:26609154). Has no peptidase activity (PubMed:26609154). {ECO:0000269|PubMed:26609154}. SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000269|PubMed:26609154}. SUBUNIT: Interacts (via the C-terminal region) with the heterodimer TJP1:TJP2. {ECO:0000269|PubMed:26609154}. TISSUE SPECIFICITY: Expressed in the cochlea. Isoform 1 expression levels are 10-fold higher than isoform 2 expression levels. {ECO:0000269|PubMed:26609154}. +Q922Y1 UBXN1_MOUSE UBX domain-containing protein 1 (Protein 2B28) (SAPK substrate protein 1) (UBA/UBX 33.3 kDa protein) (mY33K) 297 33,573 Chain (1); Domain (2); Helix (3); Initiator methionine (1); Modified residue (6); Region (1); Turn (1) FUNCTION: Ubiquitin-binding protein that plays a role in the modulation of innate immune response. Blocks both the RIG-I-like receptors (RLR) and NF-kappa-B pathways. Following viral infection, UBXN1 is induced and recruited to the RLR component MAVS. In turn, interferes with MAVS oligomerization, and disrupts the MAVS/TRAF3/TRAF6 signalosome. This function probably serves as a brake to prevent excessive RLR signaling. Interferes with the TNFalpha-triggered NF-kappa-B pathway by interacting with cellular inhibitors of apoptosis proteins (cIAPs) and thereby inhibiting their recruitment to TNFR1. Prevents also the activation of NF-kappa-B by associating with CUL1 and thus inhibiting NF-kappa-B inhibitor alpha/NFKBIA degradation that remains bound to NF-kappa-B. Interacts with the BRCA1-BARD1 heterodimer and regulates its activity. Specifically binds 'Lys-6'-linked polyubiquitin chains. Interaction with autoubiquitinated BRCA1 leads to the inhibition of the E3 ubiquitin-protein ligase activity of the BRCA1-BARD1 heterodimer. Component of a complex required to couple deglycosylation and proteasome-mediated degradation of misfolded proteins in the endoplasmic reticulum that are retrotranslocated in the cytosol. {ECO:0000250|UniProtKB:Q04323, ECO:0000269|PubMed:16709668}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15944415}. SUBUNIT: Interacts with MAVS; this interaction prevents MAVS oligomerization and thus disrupts the RLR signaling pathway. Interacts with CUL1; this interaction inhibits CUL1-mediated degradation of NF-kappa-B inhibitors. Interacts with BIRC2/c-IAP1; this interaction prevents TNFalpha-stimulated RIP1 ubiquitination and subsequent NF-kappa-B activation. Component of a complex required to couple retrotranslocation, ubiquitination and deglycosylation composed of NGLY1, SAKS1, AMFR, VCP and RAD23B (PubMed:11562482). Interacts with HOMER2 (PubMed:16709668). Interacts directly with VCP. Interacts with BRCA1 and BARD1; interaction takes place when BRCA1 is not autoubiquitinated but is strongly enhanced in the presence of autoubiquitinated BRCA1. {ECO:0000250|UniProtKB:Q04323, ECO:0000269|PubMed:11562482, ECO:0000269|PubMed:15944415, ECO:0000269|PubMed:16709668}. DOMAIN: The UBA domain specifically recognizes and binds 'Lys-6'-linked polyubiquitin chains. {ECO:0000250}. +Q9R0P9 UCHL1_MOUSE Ubiquitin carboxyl-terminal hydrolase isozyme L1 (UCH-L1) (EC 3.4.19.12) (EC 6.-.-.-) (Neuron cytoplasmic protein 9.5) (PGP 9.5) (PGP9.5) (Ubiquitin thioesterase L1) 223 24,838 Active site (2); Chain (1); Lipidation (1); Modified residue (1); Mutagenesis (2); Propeptide (1); Region (2); Sequence conflict (1); Site (1) FUNCTION: Ubiquitin-protein hydrolase involved both in the processing of ubiquitin precursors and of ubiquitinated proteins. This enzyme is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin. Also binds to free monoubiquitin and may prevent its degradation in lysosomes. The homodimer may have ATP-independent ubiquitin ligase activity. {ECO:0000269|PubMed:12913066}. PTM: O-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12913066}. Endoplasmic reticulum membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. SUBUNIT: Monomer. Homodimer. Interacts with COPS5 and SNCA (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain, where it is found in neurons but not in oligodendrocytes or astrocytes. Found in the ganglion cell layer and the inner nuclear layer of the retina (at protein level). Expressed in brain and testis. In the brain, expression is at its lowest in replaceable neurons of hippocampus and olfactory bulb. Highly expressed in senescent pituitary. {ECO:0000269|PubMed:10471497, ECO:0000269|PubMed:12559414, ECO:0000269|PubMed:12913066, ECO:0000269|PubMed:14695319, ECO:0000269|PubMed:15911766}. +Q8BGG7 UBS3B_MOUSE Ubiquitin-associated and SH3 domain-containing protein B (EC 3.1.3.48) (Cbl-interacting protein p70) (Suppressor of T-cell receptor signaling 1) (STS-1) (T-cell ubiquitin ligand 2) (TULA-2) (Tyrosine-protein phosphatase STS1/TULA2) 638 71,443 Active site (3); Alternative sequence (1); Beta strand (8); Chain (1); Compositional bias (1); Domain (2); Helix (14); Modified residue (2); Region (1); Sequence conflict (2); Turn (3) FUNCTION: Interferes with CBL-mediated down-regulation and degradation of receptor-type tyrosine kinases. Promotes accumulation of activated target receptors, such as T-cell receptors and EGFR, on the cell surface. Exhibits tyrosine phosphatase activity toward several substrates including EGFR, FAK, SYK, and ZAP70. Down-regulates proteins that are dually modified by both protein tyrosine phosphorylation and ubiquitination. {ECO:0000269|PubMed:14738763, ECO:0000269|PubMed:17679096, ECO:0000269|PubMed:19733910, ECO:0000269|PubMed:20585042}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000305}. SUBUNIT: Homodimer (PubMed:20516590, PubMed:17679096). Interacts with JAK2 (in vitro) (PubMed:12370296). Interacts with CBL. Part of a complex containing CBL and activated EGFR. Interacts with ubiquitin and with mono-ubiquitinated proteins (By similarity). Interacts with ZAP70 (ubiquitinated form) (PubMed:26903241). {ECO:0000250|UniProtKB:Q8TF42, ECO:0000269|PubMed:12370296, ECO:0000269|PubMed:17679096, ECO:0000269|PubMed:20516590, ECO:0000269|PubMed:26903241}. TISSUE SPECIFICITY: Detected in splenic T-cells and B-cells, total spleen, skeletal muscle, heart, lung, kidney, thymus, brain and liver (at protein level). Highly expressed in brain. Detected in heart, spleen, lung, liver, kidney and testis. {ECO:0000269|PubMed:12370296, ECO:0000269|PubMed:14738763}. +Q8C5U9 UBQL3_MOUSE Ubiquilin-3 658 70,753 Chain (1); Domain (3) TISSUE SPECIFICITY: Testis-specific (at protein level). {ECO:0000269|PubMed:25776854}. +Q9D2P4 URM1_MOUSE Ubiquitin-related modifier 1 101 11,323 Beta strand (6); Chain (1); Cross-link (1); Helix (4); Modified residue (1); Sequence conflict (1); Turn (4) tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis. FUNCTION: Acts as a sulfur carrier required for 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Serves as sulfur donor in tRNA 2-thiolation reaction by being thiocarboxylated (-COSH) at its C-terminus by MOCS3. The sulfur is then transferred to tRNA to form 2-thiolation of mcm(5)S(2)U. Also acts as a ubiquitin-like protein (UBL) that is covalently conjugated via an isopeptide bond to lysine residues of target proteins such as MOCS3, ATPBD3, CTU2, USP15 and CAS. The thiocarboxylated form serves as substrate for conjugation and oxidative stress specifically induces the formation of UBL-protein conjugates. {ECO:0000255|HAMAP-Rule:MF_03048}. PTM: C-terminal thiocarboxylation occurs in 2 steps, it is first acyl-adenylated (-COAMP) via the hesA/moeB/thiF part of MOCS3, then thiocarboxylated (-COSH) via the rhodanese domain of MOCS3. {ECO:0000255|HAMAP-Rule:MF_03048}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03048}. SUBUNIT: Component of a complex at least composed of URM1, CTU2/NCS2 and CTU1/ATPBD3. {ECO:0000255|HAMAP-Rule:MF_03048}. +P06869 UROK_MOUSE Urokinase-type plasminogen activator (U-plasminogen activator) (uPA) (EC 3.4.21.73) [Cleaved into: Urokinase-type plasminogen activator long chain A; Urokinase-type plasminogen activator short chain A; Urokinase-type plasminogen activator chain B] 433 48,268 Active site (3); Beta strand (27); Chain (4); Disulfide bond (12); Domain (3); Helix (9); Modified residue (1); Region (2); Signal peptide (1); Turn (3) FUNCTION: Specifically cleaves the zymogen plasminogen to form the active enzyme plasmin. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Found in high and low molecular mass forms. Each consists of two chains, A and B. The high molecular mass form contains a long chain A which is cleaved to yield a short chain A. Forms heterodimer with SERPINA5. Binds LRP1B; binding is followed by internalization and degradation. Interacts with MRC2. Interacts with PLAUR (By similarity). {ECO:0000250}. +Q640M1 UT14A_MOUSE U3 small nucleolar RNA-associated protein 14 homolog A (Juvenile spermatogonial depletion-like X-linked protein) (Jsd-like X-linked protein) 767 87,265 Alternative sequence (2); Chain (1); Coiled coil (1); Cross-link (3); Erroneous initiation (1); Frameshift (1); Modified residue (10); Sequence caution (1) FUNCTION: May be required for ribosome biogenesis. {ECO:0000250}. PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:15289605}. +Q6EJB6 UT14B_MOUSE U3 small nucleolar RNA-associated protein 14 homolog B (Juvenile spermatogonial depletion protein) 756 85,928 Chain (1); Coiled coil (3); Erroneous initiation (1); Modified residue (4); Sequence conflict (1) FUNCTION: Essential for spermatogenesis. May be required specifically for ribosome biogenesis and hence protein synthesis during male meiosis. {ECO:0000269|PubMed:15258580, ECO:0000269|PubMed:15289605}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. TISSUE SPECIFICITY: Expressed predominantly in germ cells of the testis; weakly expressed in brain. {ECO:0000269|PubMed:15258580, ECO:0000269|PubMed:15289605}. +Q80T11 USH1G_MOUSE Usher syndrome type-1G protein homolog (Jackson shaker protein) (Scaffold protein containing ankyrin repeats and SAM domain) 461 51,490 Chain (1); Domain (1); Repeat (3); Sequence conflict (1) FUNCTION: Required for normal development and maintenance of cochlear hair cell bundles. Anchoring/scaffolding protein that is a part of the functional network formed by USH1C, USH1G, CDH23 and MYO7A that mediates mechanotransduction in cochlear hair cells. Required for normal hearing. {ECO:0000269|PubMed:21436032, ECO:0000269|PubMed:21709241}. SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cytoplasm, cytoskeleton. Cell membrane; Peripheral membrane protein. Note=Detected at the tip of cochlear hair cell stereocilia. Recruited to the cell membrane via interaction with CDH23 or PCDH15. SUBUNIT: Interacts with USH1C (via the first PDZ domain). Interacts with PDZD7. Interacts with MYO7A (By similarity). Interacts with CDH23 and PCDH15; these interactions may recruit USH1G to the plasma membrane. {ECO:0000250, ECO:0000269|PubMed:12588794, ECO:0000269|PubMed:21436032}. TISSUE SPECIFICITY: Detected in stereocilia from cochlear hair cells (at protein level). Highly expressed in the cochlea, testis, cerebellum and eye, and low levels in brain, thymus and spleen. Significant signals detected in the neurosensory epithelium of inner ear cochlea and saccule, especially in inner and outer hair cells. {ECO:0000269|PubMed:12588793, ECO:0000269|PubMed:21436032, ECO:0000269|PubMed:21709241}. DISEASE: Note=Defects in Ush1g are the cause of the Jackson shaker phenotypes (js). Jackson shaker mice carry recessive mutations predicted to inactivate Ush1g by frameshift resulting in a truncated protein lacking the C-terminal SAM domain. The js phenotype is characterized by deafness, abnormal behavior (circling and/or head-tossing) and degeneration of inner ear neuroepithelia. Defects in the formation of protein complex including Ush1g may disrupt stereocilia bundle in js mice. {ECO:0000269|PubMed:12588793, ECO:0000269|PubMed:12588794, ECO:0000269|PubMed:21436032}. +Q2QI47 USH2A_MOUSE Usherin (Usher syndrome type IIa protein homolog) (Usher syndrome type-2A protein homolog) 5193 569,660 Alternative sequence (3); Chain (1); Disulfide bond (40); Domain (48); Glycosylation (68); Motif (1); Sequence conflict (8); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 5034 5054 Helical. {ECO:0000255}. TOPO_DOM 35 5033 Extracellular. {ECO:0000255}.; TOPO_DOM 5055 5193 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in hearing and vision as member of the USH2 complex (PubMed:20502675). In the inner ear, required for the maintenance of hair bundle ankle formation, which connects growing stereocilia in developing cochlear hair cells (PubMed:20502675, PubMed:24334608). In retina photoreceptors, the USH2 complex is required for the maintenance of periciliary membrane complex that seems to play a role in regulating intracellular protein transport (PubMed:20502675). {ECO:0000269|PubMed:20502675, ECO:0000269|PubMed:24334608}. SUBCELLULAR LOCATION: Cell projection, stereocilium membrane {ECO:0000269|PubMed:17567809, ECO:0000269|PubMed:20502675, ECO:0000269|PubMed:24334608}; Single-pass type I membrane protein. Photoreceptor inner segment {ECO:0000269|PubMed:20502675, ECO:0000269|PubMed:24334608}. Note=Component of the interstereocilia ankle links in the inner ear sensory cells (PubMed:20502675, PubMed:24334608). In photoreceptors, localizes at a plasma membrane microdomain in the apical inner segment taht surrounds the connecting cilia called periciliary membrane complex (PubMed:20502675, PubMed:24334608). {ECO:0000269|PubMed:20502675, ECO:0000269|PubMed:24334608}.; SUBCELLULAR LOCATION: Isoform 2: Secreted. SUBUNIT: Interacts with collagen IV and fibronectin via its laminin EGF-like domains. Interaction with collagen may be required for stable integration into the basement membrane. Interacts with NINL (By similarity). Interacts with USH1C (PubMed:16301217). Component of USH2 complex, composed of ADGRV1, PDZD7, USH2A and WHRN (PubMed:20502675, PubMed:25406310). Interacts with ADGRV1/MASS1 (via N-terminal PDZ domain) (PubMed:20502675). Interacts (via the cytoplasmic region) with WHRN (PubMed:16301217, PubMed:20502675, PubMed:23055499). Interacts (via the cytoplasmic region) with PDZD7 (PubMed:23055499). Interacts (via the cytoplasmic region) with VEZT and MYO7A (via MyTH4-FERM domains); the interaction associates VEZT with the USH2 complex at the stereocilia base (PubMed:17567809). {ECO:0000250|UniProtKB:O75445, ECO:0000269|PubMed:16301217, ECO:0000269|PubMed:17567809, ECO:0000269|PubMed:20502675, ECO:0000269|PubMed:23055499, ECO:0000269|PubMed:25406310}. DOMAIN: The PDZ-binding motif mediates the association with some of the PDZ domains of USH1C and WHRN. {ECO:0000269|PubMed:20502675}. TISSUE SPECIFICITY: Present in the testis, epididymis, oviduct, spleen, submaxillary gland, and small and large intestines. Not detected in the brain, skin, lung, skeletal muscle, cardiac muscle, liver or kidney. Expressed in smooth muscle of the colon and the epididymis. Also present in select vascular basement membranes. In the cochlea, it is present in virtually every basement membrane. It is particularly high in the strial capillary basement membranes (SCBMs). In the retina, it is again expressed in all of the basement membranes. It is also very prevalent in the lens capsule and the Bruch's layer between the retinal pigment epithelium and the choroid layer, which is very rich in basement membranes. At postnatal day 0 in it is widely expressed in the basement membranes of the cochlea. Present in the synaptic terminals of retinal photoreceptors (at protein level). {ECO:0000269|PubMed:11788194, ECO:0000269|PubMed:16301216, ECO:0000269|PubMed:17567809, ECO:0000269|PubMed:20502675}. +Q8VCY6 UTP6_MOUSE U3 small nucleolar RNA-associated protein 6 homolog (Multiple hat domains protein) 597 70,429 Chain (1); Repeat (5); Sequence conflict (1) FUNCTION: Involved in nucleolar processing of pre-18S ribosomal RNA. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. +Q9D1K2 VATF_MOUSE V-type proton ATPase subunit F (V-ATPase subunit F) (V-ATPase 14 kDa subunit) (Vacuolar proton pump subunit F) 119 13,370 Chain (1); Sequence conflict (1) FUNCTION: Subunit of the peripheral V1 complex of vacuolar ATPase essential for assembly or catalytic function. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'' and d). +Q3TYL0 YH010_MOUSE Putative IQ motif and ankyrin repeat domain-containing protein LOC642574 homolog 343 37,820 Chain (1); Domain (1); Repeat (2) +Q8BGW8 VGLL2_MOUSE Transcription cofactor vestigial-like protein 2 (Vgl-2) (Protein VITO1) 322 34,064 Chain (1); Sequence conflict (1) FUNCTION: May act as a specific coactivator for the mammalian TEFs. May play a role in the development of skeletal muscles. {ECO:0000269|PubMed:12376544}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12376544}. SUBUNIT: Interacts with TEFs. Binds to TEAD1/TEF1. {ECO:0000269|PubMed:12376544}. TISSUE SPECIFICITY: Skeletal muscle specific. {ECO:0000269|PubMed:12617818}. +P85442 VGLL3_MOUSE Transcription cofactor vestigial-like protein 3 (Vgl-3) 326 35,999 Chain (1); Compositional bias (2); Cross-link (2); Sequence conflict (1) FUNCTION: May act as a specific coactivator for the mammalian TEFs. {ECO:0000250|UniProtKB:Q8N8G2}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8N8G2}. +A2ARP1 VIP1_MOUSE Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1 (EC 2.7.4.21) (EC 2.7.4.24) (Diphosphoinositol pentakisphosphate kinase 1) (Histidine acid phosphatase domain-containing protein 2A) (InsP6 and PP-IP5 kinase 1) (VIP1 homolog) 1436 159,923 Alternative sequence (8); Binding site (8); Chain (1); Erroneous initiation (1); Frameshift (1); Modified residue (6); Nucleotide binding (3); Region (4); Sequence caution (1); Sequence conflict (5) FUNCTION: Bifunctional inositol kinase that acts in concert with the IP6K kinases IP6K1, IP6K2 and IP6K3 to synthesize the diphosphate group-containing inositol pyrophosphates diphosphoinositol pentakisphosphate, PP-InsP5, and bis-diphosphoinositol tetrakisphosphate, (PP)2-InsP4. PP-InsP5 and (PP)2-InsP4, also respectively called InsP7 and InsP8, regulate a variety of cellular processes, including apoptosis, vesicle trafficking, cytoskeletal dynamics, exocytosis, insulin signaling and neutrophil activation. Phosphorylates inositol hexakisphosphate (InsP6) at positions 1 or 3 to produce PP-InsP5 which is in turn phosphorylated by IP6Ks to produce (PP)2-InsP4. Alternatively, phosphorylates at position 1 or 3 PP-InsP5, produced by IP6Ks from InsP6, to produce (PP)2-InsP4. Activated when cells are exposed to hyperosmotic stress. {ECO:0000250|UniProtKB:Q6PFW1}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q6PFW1}. Cell membrane {ECO:0000250|UniProtKB:Q6PFW1}. Note=Relocalizes to the plasma membrane upon activation of the PtdIns 3-kinase pathway. {ECO:0000250|UniProtKB:Q6PFW1}. DOMAIN: The C-terminal acid phosphatase-like domain binds PtdIns(3,4,5)P3 and InsP6. Despite its similarity with the phosphatase domain of histidine acid phosphatases, it has no phosphatase activity. {ECO:0000250|UniProtKB:Q6PFW1}. +Q9CRC0 VKOR1_MOUSE Vitamin K epoxide reductase complex subunit 1 (EC 1.17.4.4) (Vitamin K1 2,3-epoxide reductase subunit 1) 161 17,768 Chain (1); Disulfide bond (1); Natural variant (2); Topological domain (4); Transmembrane (4) TRANSMEM 9 29 Helical. {ECO:0000255}.; TRANSMEM 79 97 Helical. {ECO:0000255}.; TRANSMEM 101 123 Helical. {ECO:0000255}.; TRANSMEM 127 149 Helical. {ECO:0000255}. TOPO_DOM 1 8 Lumenal. {ECO:0000255}.; TOPO_DOM 30 78 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 124 126 Lumenal. {ECO:0000255}.; TOPO_DOM 150 161 Cytoplasmic. {ECO:0000250}. FUNCTION: Involved in vitamin K metabolism. Catalytic subunit of the vitamin K epoxide reductase (VKOR) complex which reduces inactive vitamin K 2,3-epoxide to active vitamin K. Vitamin K is required for the gamma-carboxylation of various proteins, including clotting factors, and is required for normal blood coagulation, but also for normal bone development. {ECO:0000269|PubMed:15879509, ECO:0000269|PubMed:19492146}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. DOMAIN: The number of transmembrane domains and the membrane topology are controversial; supporting evidence is available both for models with three transmembrane domains and four transmembrane domains. {ECO:0000250}. TISSUE SPECIFICITY: Detected in liver. {ECO:0000269|PubMed:19492146}. +Q62471 VNS1_MOUSE Vomeronasal secretory protein 1 (Lipocalin-3) (Vomeronasal secretory protein I) (VNSP I) 182 20,626 Chain (1); Disulfide bond (1); Erroneous initiation (1); Glycosylation (1); Signal peptide (1) FUNCTION: Transport of lipophilic molecules, possible pheromone-carrier. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Specifically expressed in vomeronasal and posterior glands of the nasal septum, the ducts of which open into the lumen of the vomeronasal organ. +O08810 U5S1_MOUSE 116 kDa U5 small nuclear ribonucleoprotein component (Elongation factor Tu GTP-binding domain-containing protein 2) (U5 snRNP-specific protein, 116 kDa) (U5-116 kDa) 971 109,361 Chain (1); Cross-link (2); Domain (1); Modified residue (3); Nucleotide binding (3); Sequence caution (1) FUNCTION: Component of the U5 snRNP and the U4/U6-U5 tri-snRNP complex required for pre-mRNA splicing. Binds GTP (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39. Identified in the spliceosome C complex. Interacts with ERBB4 and PRPF8. Interacts with PIH1D1. {ECO:0000250|UniProtKB:Q15029}. +E9Q735 UBE4A_MOUSE Ubiquitin conjugation factor E4 A (EC 2.3.2.-) 1028 118,198 Chain (1); Domain (1); Modified residue (1) Protein modification; protein ubiquitination. FUNCTION: Ubiquitin-protein ligase that probably functions as an E3 ligase in conjunction with specific E1 and E2 ligases. May also function as an E4 ligase mediating the assembly of polyubiquitin chains on substrates ubiquitinated by another E3 ubiquitin ligase. Mediates 'Lys-48'-linked polyubiquitination of substrates. {ECO:0000250|UniProtKB:P54860, ECO:0000269|PubMed:11435423}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11435423}. DOMAIN: The U-box domain is required for the ubiquitin protein ligase activity. {ECO:0000250|UniProtKB:P54860, ECO:0000250|UniProtKB:Q9ES00}. TISSUE SPECIFICITY: Expressed in liver, heart, brain, kidney and testis. {ECO:0000269|PubMed:11435423}. +P68037 UB2L3_MOUSE Ubiquitin-conjugating enzyme E2 L3 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme L3) (UbcM4) (Ubiquitin carrier protein L3) (Ubiquitin-protein ligase L3) 154 17,862 Active site (1); Chain (1); Modified residue (1); Sequence conflict (1) Protein modification; protein ubiquitination. FUNCTION: Ubiquitin-conjugating enzyme E2 that specifically acts with HECT-type and RBR family E3 ubiquitin-protein ligases. Does not function with most RING-containing E3 ubiquitin-protein ligases because it lacks intrinsic E3-independent reactivity with lysine: in contrast, it has activity with the RBR family E3 enzymes, such as PRKN and ARIH1, that function like function like RING-HECT hybrids. Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'-linked polyubiquitination. Involved in the selective degradation of short-lived and abnormal proteins. Down-regulated during the S-phase it is involved in progression through the cell cycle. Regulates nuclear hormone receptors transcriptional activity. May play a role in myelopoiesis. {ECO:0000250|UniProtKB:P68036}. PTM: Ubiquitinated. The alteration of UBE2L3 protein levels during the S-phase of the cell cycle is due to ubiquitin-dependent proteasomal degradation. Autoubiquitinated in vitro. {ECO:0000250|UniProtKB:P68036}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P68036}. Cytoplasm {ECO:0000250|UniProtKB:P68036}. SUBUNIT: Interacts with PRKN; involved in ubiquitination and degradation of misfolded proteins. Interacts with UBE3A. Interacts with CCNB1IP1, CBL, ZAP70, RNF19A, RNF19B and RNF144B. Interacts with ARIH1. Interacts with ARIH2 (via RING-type 1). Interacts with NCOA1; they functionally interact to regulate progesterone receptor transcriptional activity. Interacts with NDFIP1 (via N-terminus); the interaction mediates recruitment of UBE2L3 to ITCH and causes MAP3K7 ubiquitination (PubMed:25632008). {ECO:0000250|UniProtKB:P68036, ECO:0000269|PubMed:25632008}. DOMAIN: In contrast to other ubiquitin-conjugating enzymes E2, residues essential for lysine reactivity are absent: Pro and a His residues are present instead of an Asp and an Asp residues in positions 88 and 119, respectively. {ECO:0000250|UniProtKB:P68036}. +P25976 UBF1_MOUSE Nucleolar transcription factor 1 (Upstream-binding factor 1) (UBF-1) 765 89,509 Alternative sequence (1); Beta strand (1); Chain (1); Compositional bias (1); DNA binding (6); Helix (12); Modified residue (14); Turn (4) FUNCTION: Recognizes the ribosomal RNA gene promoter and activates transcription mediated by RNA polymerase I through cooperative interactions with the transcription factor SL1/TIF-IB complex. It binds specifically to the upstream control element. {ECO:0000269|PubMed:20168301}. PTM: Phosphorylated and activated by PIK3CA. {ECO:0000269|PubMed:17182730}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:20168301}. SUBUNIT: Homodimer (By similarity). Interacts with TBP (By similarity). Interacts with TAF1A (By similarity). Interacts with RASL11A (PubMed:20168301). Binds to IRS1 and PIK3CA (PubMed:15197263). Interacts with DHX33 (PubMed:21930779). Interacts with PHF6 (By similarity). Interacts with CEBPA (isoform 1 and isoform 4) (By similarity). Interacts with DDX11 (By similarity). Interacts with NOP53 (By similarity). {ECO:0000250|UniProtKB:P17480, ECO:0000250|UniProtKB:P25977, ECO:0000269|PubMed:15197263, ECO:0000269|PubMed:20168301, ECO:0000269|PubMed:21930779}. +Q8CFI2 UB2R1_MOUSE Ubiquitin-conjugating enzyme E2 R1 (EC 2.3.2.23) ((E3-independent) E2 ubiquitin-conjugating enzyme R1) (EC 2.3.2.24) (E2 ubiquitin-conjugating enzyme R1) (Ubiquitin-conjugating enzyme E2-32 kDa complementing) (Ubiquitin-conjugating enzyme E2-CDC34) (Ubiquitin-protein ligase R1) 235 26,622 Active site (1); Chain (1); Compositional bias (1); Modified residue (5); Region (1) Protein modification; protein ubiquitination. FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination. Cooperates with the E2 UBCH5C and the SCF(FBXW11) E3 ligase complex for the polyubiquitination of NFKBIA leading to its subsequent proteasomal degradation. Performs ubiquitin chain elongation building ubiquitin chains from the UBE2D3-primed NFKBIA-linked ubiquitin. UBE2D3 acts as an initiator E2, priming the phosphorylated NFKBIA target at positions 'Lys-21' and/or 'Lys-22' with a monoubiquitin. Cooperates with the SCF(SKP2) E3 ligase complex to regulate cell proliferation through ubiquitination and degradation of MYBL2 and KIP1. Involved in ubiquitin conjugation and degradation of CREM isoform ICERIIgamma and ATF15 resulting in abrogation of ICERIIgamma- and ATF5-mediated repression of cAMP-induced transcription during both meiotic and mitotic cell cycles. Involved in the regulation of the cell cycle G2/M phase through its targeting of the WEE1 kinase for ubiquitination and degradation. Also involved in the degradation of beta-catenin. {ECO:0000250|UniProtKB:P49427, ECO:0000269|PubMed:10230406}. PTM: Phosphorylated by CK2. Phosphorylation of the C-terminal tail by CK2 controles the nuclear localization. {ECO:0000250|UniProtKB:P49427}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P49427}. Nucleus {ECO:0000250|UniProtKB:P49427}. Note=The phosphorylation of the C-terminal tail plays an important role in mediating nuclear localization. Colocalizes with beta-tubulin on mitotic spindles in anaphase. {ECO:0000250|UniProtKB:P49427}. SUBUNIT: Interacts with SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex. Identified in a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex together with HINT1 and RBX1. When cullin is neddylated, the interaction between the E2 and the SCF complex is strengthened (By similarity). When phosphorylated, interacts with beta-TrCP (BTRC) (By similarity). Interacts with casein kinase subunit CSNK2B. {ECO:0000250|UniProtKB:P49427}. DOMAIN: The C-terminal acidic tail is required for nuclear localization and is involved in the binding to SCF E3 ligase complexes, and more specifically with the CUL1 subunit. {ECO:0000250|UniProtKB:P49427}. +Q9Z255 UBE2A_MOUSE Ubiquitin-conjugating enzyme E2 A (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme A) (RAD6 homolog A) (HR6A) (mHR6A) (Ubiquitin carrier protein A) (Ubiquitin-protein ligase A) 152 17,315 Active site (1); Chain (1); Modified residue (1) Protein modification; protein ubiquitination. FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In association with the E3 enzyme BRE1 (RNF20 and/or RNF40), it plays a role in transcription regulation by catalyzing the monoubiquitination of histone H2B at 'Lys-120' to form H2BK120ub1. H2BK120ub1 gives a specific tag for epigenetic transcriptional activation, elongation by RNA polymerase II, telomeric silencing, and is also a prerequisite for H3K4me and H3K79me formation. In vitro catalyzes 'Lys-11', as well as 'Lys-48'-linked polyubiquitination. Required for postreplication repair of UV-damaged DNA. {ECO:0000250|UniProtKB:P49459}. PTM: Phosphorylation at Ser-120 by CDK9 increases activity towards histone H2B. {ECO:0000250|UniProtKB:P49459}. SUBUNIT: Interacts with RAD18 and WAC (By similarity). Interacts with RFPL4A and CCNB1 (PubMed:12525704). {ECO:0000250|UniProtKB:P49459, ECO:0000269|PubMed:12525704}. +Q9D1C1 UBE2C_MOUSE Ubiquitin-conjugating enzyme E2 C (EC 2.3.2.23) ((E3-independent) E2 ubiquitin-conjugating enzyme C) (EC 2.3.2.24) (E2 ubiquitin-conjugating enzyme C) (UbcH10) (Ubiquitin carrier protein C) (Ubiquitin-protein ligase C) 179 19,606 Active site (1); Chain (1); Initiator methionine (1); Modified residue (2) Protein modification; protein ubiquitination. FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'- and 'Lys-48'-linked polyubiquitination. Acts as an essential factor of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated ubiquitin ligase that controls progression through mitosis. Acts by initiating 'Lys-11'-linked polyubiquitin chains on APC/C substrates, leading to the degradation of APC/C substrates by the proteasome and promoting mitotic exit. {ECO:0000250|UniProtKB:O00762}. PTM: Autoubiquitinated by the APC/C complex, leading to its degradation by the proteasome. Its degradation plays a central role in APC/C regulation, allowing cyclin-A accumulation before S phase entry. APC/C substrates inhibit the autoubiquitination of UBE2C/UBCH10 but not its E2 function, hence APC/C remaining active until its substrates have been destroyed. {ECO:0000250|UniProtKB:O00762}. SUBUNIT: Component of the APC/C complex, composed of at least 14 distinct subunits that assemble into a complex of at least 19 chains with a combined molecular mass of around 1.2 MDa. Within this complex, directly interacts with ANAPC2. {ECO:0000250|UniProtKB:O00762}. +P60605 UB2G2_MOUSE Ubiquitin-conjugating enzyme E2 G2 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme G2) (Ubiquitin carrier protein G2) (Ubiquitin-protein ligase G2) 165 18,566 Active site (1); Beta strand (5); Chain (1); Helix (6); Initiator methionine (1); Modified residue (1); Turn (2) Protein modification; protein ubiquitination. FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination. Involved in endoplasmic reticulum-associated degradation (ERAD). {ECO:0000250|UniProtKB:P60604}. +Q8BX13 UBE3D_MOUSE E3 ubiquitin-protein ligase E3D (EC 2.3.2.26) (HECT-type E3 ubiquitin transferase E3D) (UbcH10-binding protein with a HECT-like domain) (Ubiquitin-conjugating enzyme E2C-binding protein) 368 40,753 Chain (1); Initiator methionine (1); Modified residue (1); Region (2) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and transfers it to substrates, generally promoting their degradation by the proteasome. {ECO:0000250|UniProtKB:Q7Z6J8}. PTM: Ubiquitinated by UBCH10 (E2 ubiquitin-conjugating enzyme). {ECO:0000250|UniProtKB:Q7Z6J8}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. SUBUNIT: Interacts with UBE2C/UbcH10 (E2 ubiquitin-conjugating enzyme). {ECO:0000250|UniProtKB:Q7Z6J8}. DOMAIN: The C-terminal half (AA 167-368) is able to bind cyclin-B and shows a self-ubiquitination activity (mono-, poly, or multi-ubiquitination) in a HECT-like sequence dependent manner. {ECO:0000250|UniProtKB:Q7Z6J8}. +P35545 UBIM_MOUSE Ubiquitin-like protein FUBI (Monoclonal non-specific suppressor factor beta) (MNSF-beta) 74 7,786 Chain (1) +Q811S7 UBIP1_MOUSE Upstream-binding protein 1 (Nuclear factor 2d9) (NF2d9) 540 60,212 Alternative sequence (1); Chain (1); Modified residue (3); Region (2); Sequence conflict (1) FUNCTION: Functions as a transcriptional activator in a promoter context-dependent manner. Involved in regulation of the alpha-globin gene in erythroid cells. Activation of the alpha-globin promoter in erythroid cells is via synergistic interaction with TFCP2. Functions as a trans-acting factor that regulates the domestic strain CYP2D9 gene through specific association with the regulatory element SDI-A1. Binding to SDI-A1 depends on the type of nucleotide at position 299; binding is abolished by a nucleotide substitution at this position. Modulates the placental expression of CYP11A1 (By similarity). {ECO:0000250, ECO:0000269|PubMed:15988015, ECO:0000269|PubMed:7623810}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with TFCP2 and PIAS1, and is probably part of a complex containing TFCP2, UBP1 and PIAS1. {ECO:0000269|PubMed:15988015, ECO:0000269|PubMed:7623810}. TISSUE SPECIFICITY: Ubiquitous. Highly expressed in erythroid cells. {ECO:0000269|PubMed:15988015, ECO:0000269|PubMed:7623810}. +Q99K46 UBP11_MOUSE Ubiquitin carboxyl-terminal hydrolase 11 (EC 3.4.19.12) (Deubiquitinating enzyme 11) (Ubiquitin thioesterase 11) (Ubiquitin-specific-processing protease 11) 921 105,384 Active site (2); Chain (1); Domain (2); Erroneous initiation (1); Modified residue (4); Sequence conflict (1) FUNCTION: Protease that can remove conjugated ubiquitin from target proteins and polyubiquitin chains. Inhibits the degradation of target proteins by the proteasome. Cleaves preferentially 'Lys-6' and 'Lys-63'-linked ubiquitin chains. Has lower activity with 'Lys-11' and 'Lys-33'-linked ubiquitin chains, and extremely low activity with 'Lys-27', 'Lys-29' and 'Lys-48'-linked ubiquitin chains (in vitro). Plays a role in the regulation of pathways leading to NF-kappa-B activation. Plays a role in the regulation of DNA repair after double-stranded DNA breaks. Acts as a chromatin regulator via its association with the Polycomb group (PcG) multiprotein PRC1-like complex; may act by deubiquitinating components of the PRC1-like complex. {ECO:0000250|UniProtKB:P51784}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P51784}. Cytoplasm {ECO:0000250|UniProtKB:P51784}. Chromosome {ECO:0000250|UniProtKB:P51784}. Note=Predominantly nuclear. Associates with chromatin. {ECO:0000250|UniProtKB:P51784}. SUBUNIT: Monomer. Interacts with RANBP9/RANBPM. Interacts with BRCA2. Interacts with CHUK/IKKA. Interacts with NFKBIA. Associated component of the Polycomb group (PcG) multiprotein PRC1-like complex. {ECO:0000250|UniProtKB:P51784}. +Q9EPV8 UBL5_MOUSE Ubiquitin-like protein 5 73 8,547 Beta strand (5); Chain (1); Domain (1); Helix (3) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with CLK1, CLK3 and CLK4. {ECO:0000250}. +Q91W67 UBL7_MOUSE Ubiquitin-like protein 7 380 40,433 Beta strand (4); Chain (1); Domain (2); Helix (2); Modified residue (1); Sequence conflict (4); Turn (1) SUBUNIT: Binds ubiquitin. {ECO:0000250}. +Q5DU02 UBP22_MOUSE Ubiquitin carboxyl-terminal hydrolase 22 (EC 3.4.19.12) (Deubiquitinating enzyme 22) (Ubiquitin thioesterase 22) (Ubiquitin-specific-processing protease 22) 525 59,954 Active site (2); Chain (1); Domain (1); Erroneous initiation (1); Modified residue (1); Sequence conflict (2); Zinc finger (1) FUNCTION: Histone deubiquitinating component of the transcription regulatory histone acetylation (HAT) complex SAGA. Catalyzes the deubiquitination of both histones H2A and H2B, thereby acting as a coactivator. Recruited to specific gene promoters by activators such as MYC, where it is required for transcription. Required for nuclear receptor-mediated transactivation and cell cycle progression (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27013495}. SUBUNIT: Component of some SAGA transcription coactivator-HAT complexes, at least composed of ATXN7, ATXN7L3, ENY2, GCN5L2, SUPT3H, TAF10, TRRAP and USP22. Within the SAGA complex, ATXN7L3, ENY2 and USP22 form a subcomplex required for histone deubiquitination. Interacts directly with ATXN7L3; leading to its recruitment to the SAGA complex. Interacts with ATXN7L3 and weakly with ATXN7L3B. {ECO:0000250|UniProtKB:Q9UPT9}. TISSUE SPECIFICITY: Highly expressed in brain and weakly in other organs. {ECO:0000269|PubMed:16378762}. +Q3UN04 UBP30_MOUSE Ubiquitin carboxyl-terminal hydrolase 30 (EC 3.4.19.12) (Deubiquitinating enzyme 30) (Ubiquitin thioesterase 30) (Ubiquitin-specific-processing protease 30) (Ub-specific protease 30) 517 58,221 Active site (2); Chain (1); Cross-link (2); Domain (1); Erroneous initiation (1); Mutagenesis (4); Topological domain (2); Transmembrane (1) TRANSMEM 36 56 Helical. {ECO:0000255}. TOPO_DOM 1 35 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 57 517 Cytoplasmic. {ECO:0000255}. FUNCTION: Deubiquitinating enzyme tethered to the mitochondrial outer membrane that acts as a key inhibitor of mitophagy by counteracting the action of parkin (PRKN): hydrolyzes ubiquitin attached by parkin on target proteins, such as RHOT1/MIRO1 and TOMM20, thereby blocking parkin's ability to drive mitophagy. Preferentially cleaves 'Lys-6'- and 'Lys-11'-linked polyubiquitin chains, 2 types of linkage that participate in mitophagic signaling. Does not cleave efficiently polyubiquitin phosphorylated at 'Ser-65' (By similarity). Acts as negative regulator of mitochondrial fusion by mediating deubiquitination of MFN1 and MFN2 (PubMed:24513856). {ECO:0000250|UniProtKB:Q70CQ3, ECO:0000269|PubMed:24513856}. PTM: Ubiquitinated by parkin (PRKN) at Lys-235 and Lys-289, leading to its degradation. {ECO:0000250|UniProtKB:Q70CQ3}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:24513856}. +Q99MX1 UBP26_MOUSE Ubiquitin carboxyl-terminal hydrolase 26 (EC 3.4.19.12) (Deubiquitinating enzyme 26) (Ubiquitin thioesterase 26) (Ubiquitin-specific-processing protease 26) 835 95,452 Active site (2); Chain (1); Domain (1); Sequence conflict (1) FUNCTION: Involved in the ubiquitin-dependent proteolytic pathway in conjunction with the 26S proteasome. Deubiquitinates the androgen receptor and regulates the androgen receptor signaling pathway. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with AR. {ECO:0000250}. +Q8R5K2 UBP33_MOUSE Ubiquitin carboxyl-terminal hydrolase 33 (EC 3.4.19.12) (Deubiquitinating enzyme 33) (Ubiquitin thioesterase 33) (Ubiquitin-specific-processing protease 33) (VHL-interacting deubiquitinating enzyme 1) 909 102,728 Active site (2); Alternative sequence (1); Chain (1); Domain (3); Erroneous initiation (2); Modified residue (1); Sequence conflict (6); Zinc finger (1) FUNCTION: Deubiquitinating enzyme involved in various processes such as centrosome duplication, cellular migration and beta-2 adrenergic receptor/ADRB2 recycling. Involved in regulation of centrosome duplication by mediating deubiquitination of CCP110 in S and G2/M phase, leading to stabilize CCP110 during the period which centrioles duplicate and elongate. Involved in cell migration via its interaction with intracellular domain of ROBO1, leading to regulate the Slit signaling. Plays a role in commissural axon guidance cross the ventral midline of the neural tube in a Slit-dependent manner, possibly by mediating the deubiquitination of ROBO1. Acts as a regulator of G-protein coupled receptor (GPCR) signaling by mediating the deubiquitination of beta-arrestins (ARRB1 and ARRB2) and beta-2 adrenergic receptor (ADRB2). Plays a central role in ADRB2 recycling and resensitization after prolonged agonist stimulation by constitutively binding ADRB2, mediating deubiquitination of ADRB2 and inhibiting lysosomal trafficking of ADRB2. Upon dissociation, it is probably transferred to the translocated beta-arrestins, leading to beta-arrestins deubiquitination and disengagement from ADRB2. This suggests the existence of a dynamic exchange between the ADRB2 and beta-arrestins. Deubiquitinates DIO2, thereby regulating thyroid hormone regulation. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. {ECO:0000269|PubMed:19684588, ECO:0000269|PubMed:19706539}. PTM: Ubiquitinated via a VHL-dependent pathway for proteasomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8TEY7}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q8TEY7}. Note=Associates with centrosomes predominantly in S and G2 phases but less in G1 phase (By similarity). {ECO:0000250|UniProtKB:Q8TEY7}. SUBUNIT: Interacts with VHL, leading to its ubiquitination and subsequent degradation. Interacts with ARRB1, ARRB2, ADRB2 and DIO2. Interacts with SELENBP1; in a selenium-dependent manner. Interacts with CCP110 (By similarity). Interacts with ROBO1. {ECO:0000250, ECO:0000269|PubMed:19684588, ECO:0000269|PubMed:19706539}. DOMAIN: The UBP-type zinc finger binds 3 zinc ions. However, it does not bind ubiquitin, probably because the conserved Arg in position 55 is replaced by a Glu residue (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Present in E9.5 and E11.5 commissural neurons (at protein level). {ECO:0000269|PubMed:19684588}. +Q8BY87 UBP47_MOUSE Ubiquitin carboxyl-terminal hydrolase 47 (EC 3.4.19.12) (Deubiquitinating enzyme 47) (Ubiquitin thioesterase 47) (Ubiquitin-specific-processing protease 47) 1376 157,455 Active site (2); Alternative sequence (1); Chain (1); Domain (1); Erroneous initiation (2); Frameshift (1); Modified residue (7); Sequence conflict (8) FUNCTION: Ubiquitin-specific protease that specifically deubiquitinates monoubiquitinated DNA polymerase beta (POLB), stabilizing POLB thereby playing a role in base-excision repair (BER) (By similarity). Acts as a regulator of cell growth and genome integrity. May also indirectly regulate CDC25A expression at a transcriptional level. {ECO:0000250, ECO:0000269|PubMed:19966869}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with BTRC and FBXW11. Interacts with POLB (By similarity). {ECO:0000250}. +Q8BWR4 UBP40_MOUSE Ubiquitin carboxyl-terminal hydrolase 40 (EC 3.4.19.12) (Deubiquitinating enzyme 40) (Ubiquitin thioesterase 40) (Ubiquitin-specific-processing protease 40) 1235 139,952 Active site (2); Alternative sequence (4); Chain (1); Domain (1); Sequence conflict (4) +P35123 UBP4_MOUSE Ubiquitin carboxyl-terminal hydrolase 4 (EC 3.4.19.12) (Deubiquitinating enzyme 4) (Ubiquitin thioesterase 4) (Ubiquitin-specific-processing protease 4) (Ubiquitous nuclear protein) 962 108,343 Active site (2); Beta strand (12); Chain (1); Domain (4); Helix (6); Metal binding (4); Modified residue (3); Motif (2); Mutagenesis (2); Region (6); Sequence conflict (3); Turn (5) FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin from target proteins. Deubiquitinates PDPK1. Deubiquitinates TRIM21. Deubiquitinates receptor ADORA2A which increases the amount of functional receptor at the cell surface. May regulate mRNA splicing through deubiquitination of the U4 spliceosomal protein PRPF3. This may prevent its recognition by the U5 component PRPF8 thereby destabilizing interactions within the U4/U6.U5 snRNP. May also play a role in the regulation of quality control in the ER. {ECO:0000250|UniProtKB:Q13107}. PTM: Monoubiquitinated by TRIM21. Ubiquitination does not lead to its proteasomal degradation. Autodeubiquitinated. {ECO:0000250|UniProtKB:Q13107}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15494318}. Nucleus {ECO:0000269|PubMed:15494318}. Note=Shuttles between the nucleus and cytoplasm. Exported to the cytoplasm in a CRM1-dependent manner and recycled back to the nucleus via the importin alpha/beta heterodimeric import receptor. {ECO:0000269|PubMed:15494318}. SUBUNIT: Interacts with RB1 (both dephosphorylated and hypophosphorylated forms) (PubMed:11571651). Interacts with RBL1 and RBL2 (PubMed:11571651). Interacts with ADORA2A (via cytoplasmic C-terminus); the interaction is direct. Interacts with SART3; recruits USP4 to its substrate PRPF3 (By similarity). {ECO:0000250|UniProtKB:Q13107, ECO:0000269|PubMed:11571651}. DOMAIN: The DUSP and ubiquitin-like 1 domains promote ubiquitin release and thus enhance USB4 catalytic activity. However, these domains do not bind ubiquitin. {ECO:0000250|UniProtKB:Q13107}. TISSUE SPECIFICITY: Expressed in brain, kidney, liver and spleen (at protein level). {ECO:0000269|PubMed:15494318}. +Q9ES63 UBP29_MOUSE Ubiquitin carboxyl-terminal hydrolase 29 (EC 3.4.19.12) (Deubiquitinating enzyme 29) (Ubiquitin thioesterase 29) (Ubiquitin-specific-processing protease 29) 869 97,823 Active site (2); Chain (1); Domain (1); Sequence conflict (1) TISSUE SPECIFICITY: Highest expression levels in adult brain, especially in the cerebral cortex and hippocampus, and in the forebrain, face, and limb buds of midgestation mouse embryos. +Q80X50 UBP2L_MOUSE Ubiquitin-associated protein 2-like 1107 116,799 Alternative sequence (6); Beta strand (3); Chain (1); Compositional bias (3); Domain (1); Frameshift (1); Helix (4); Modified residue (18); Natural variant (1); Sequence conflict (2) FUNCTION: Plays an important role in the activity of long-term repopulating hematopoietic stem cells (LT-HSCs) (PubMed:25185265). {ECO:0000269|PubMed:25185265}. SUBUNIT: Interacts with BMI1. Part of a complex consisting of UBAP2L, BMI1 and RNF2. {ECO:0000250|UniProtKB:Q14157}. +Q80U87 UBP8_MOUSE Ubiquitin carboxyl-terminal hydrolase 8 (EC 3.4.19.12) (Deubiquitinating enzyme 8) (Ubiquitin isopeptidase Y) (mUBPy) (Ubiquitin thioesterase 8) (Ubiquitin-specific-processing protease 8) 1080 122,611 Active site (2); Chain (1); Domain (3); Erroneous initiation (1); Helix (1); Modified residue (7); Motif (1); Mutagenesis (12); Sequence conflict (10) FUNCTION: Hydrolase that can remove conjugated ubiquitin from proteins and therefore plays an important regulatory role at the level of protein turnover by preventing degradation. Converts both 'Lys-48' an 'Lys-63'-linked ubiquitin chains. Catalytic activity is enhanced in the M phase. Involved in cell proliferation. Required to enter into S phase in response to serum stimulation. May regulate T-cell anergy mediated by RNF128 via the formation of a complex containing RNF128 and OTUB1. Probably regulates the stability of STAM2 and RASGRF1. Regulates endosomal ubiquitin dynamics, cargo sorting, membrane traffic at early endosomes, and maintenance of ESCRT-0 stability. The level of protein ubiquitination on endosomes is essential for maintaining the morphology of the organelle. Deubiquitinates EPS15 and controles tyrosine kinase stability. Removes conjugated ubiquitin from EGFR thus regulating EGFR degradation and downstream MAPK signaling. Involved in acrosome biogenesis through interaction with the spermatid ESCRT-0 complex and microtubules. Deubiquitinates BIRC6/bruce and KIF23/MKLP1 (By similarity). Deubiquitinates BACE1 which inhibits BACE1 lysosomal degradation and modulates BACE-mediated APP cleavage and amyloid-beta formation (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P40818, ECO:0000269|PubMed:11500497, ECO:0000269|PubMed:15314180, ECO:0000269|PubMed:16120644, ECO:0000269|PubMed:16771824, ECO:0000269|PubMed:17121848, ECO:0000269|PubMed:17210635, ECO:0000269|PubMed:17452457, ECO:0000269|PubMed:17720156, ECO:0000269|PubMed:20130268}. PTM: Phosphorylation of Ser-680 is essential for interaction with YWHAE and for cytosol localization. Undergoes dephosphorylation at Ser-680 in the M phase. Tyrosine-phosphorylated in its N-terminal half in an EGFR-dependent manner. {ECO:0000269|PubMed:16944949, ECO:0000269|PubMed:17121848, ECO:0000269|PubMed:17210635, ECO:0000269|PubMed:17720156}.; PTM: Ubiquitinated. Inactive form is mostly monoubiquitinated, but polyubiquitination happens too. Ubiquitination is increased in EGF-stimulated cells. Ubiquitination of active form is undetectable, suggesting a possibility that USP8 deubiquitinates itself, thereby regulating its own function. {ECO:0000269|PubMed:16120644}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17720156}. Nucleus {ECO:0000269|PubMed:16944949}. Endosome membrane {ECO:0000269|PubMed:16120644}; Peripheral membrane protein {ECO:0000305}. Cell membrane {ECO:0000250|UniProtKB:P40818}; Peripheral membrane protein {ECO:0000305}. SUBUNIT: Forms a ternary complex with RNF128 and OTUB1. Interacts (via C-terminal UCH catalytic domain) with OTUB1 isoform 1. Interacts with STAM2 (via SH3 domain). Interacts with DNAJB3, EGFR, EPS15, RASGRF1, RNF41, YWHAE, YWHAG and YWHAZ. Interacts with NBR1, RASGRF1, RNF41 and IST1 (By similarity). Associates with the ESCRT-0 complex and with microtubules. Interacts with BIRC6/bruce and KIF23/MKLP1. {ECO:0000250, ECO:0000269|PubMed:10982817, ECO:0000269|PubMed:11500497, ECO:0000269|PubMed:14661020, ECO:0000269|PubMed:15314180, ECO:0000269|PubMed:15342353, ECO:0000269|PubMed:16771824, ECO:0000269|PubMed:16944949, ECO:0000269|PubMed:17121848, ECO:0000269|PubMed:17720156}. DOMAIN: The MIT domain is required for endosomal localization, CHMP1B-binding, maintenance of ESCRT-0 stability and EGFR degradation. {ECO:0000250}.; DOMAIN: The rhodanese domain is sufficient for RNF41-binding. TISSUE SPECIFICITY: Highly expressed in testis. Expressed at intermediate level in brain. {ECO:0000269|PubMed:11500497, ECO:0000269|PubMed:15342353}. +Q6P8X6 UBP50_MOUSE Putative ubiquitin carboxyl-terminal hydrolase 50 (EC 3.4.19.12) (Deubiquitinating enzyme 50) (Ubiquitin thioesterase 50) (Ubiquitin-specific-processing protease 50) 390 44,543 Active site (2); Alternative sequence (2); Chain (1); Domain (1); Sequence conflict (1) FUNCTION: May recognize and hydrolyze the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins (By similarity). {ECO:0000250}. +B1AY15 UBP51_MOUSE Ubiquitin carboxyl-terminal hydrolase 51 (EC 3.4.19.12) (Deubiquitinating enzyme 51) 661 74,783 Active site (2); Chain (1); Compositional bias (1); Domain (1); Mutagenesis (2); Zinc finger (1) FUNCTION: Deubiquitinates histone H2A at 'Lys-13' and 'Lys-15' and regulates DNA damage response. USP51 is recruited to chromatin after DNA damage and regulates the dynamic assembly/disassembly of TP53BP1 and BRCA1 foci. {ECO:0000269|PubMed:27083998}. SUBCELLULAR LOCATION: Chromosome {ECO:0000250|UniProtKB:Q70EK9}. Note=Dissociates from chromatin immediately after DNA damage and reassociates with chromatin following DNA repair. {ECO:0000250|UniProtKB:Q70EK9}. SUBUNIT: Interacts with H2A. {ECO:0000250|UniProtKB:Q70EK9}. +Q8BU04 UBR7_MOUSE Putative E3 ubiquitin-protein ligase UBR7 (EC 2.3.2.27) (N-recognin-7) (RING-type E3 ubiquitin transferase UBR7) 425 48,065 Chain (1); Cross-link (4); Modified residue (1); Zinc finger (2) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in testis and sperm (at protein level). {ECO:0000269|PubMed:24664117}. +Q91WB7 UBTD1_MOUSE Ubiquitin domain-containing protein 1 227 25,985 Chain (1); Domain (1) FUNCTION: May be involved in the regulation of cellular senescence through a positive feedback loop with TP53. Is a TP53 downstream target gene that increases the stability of TP53 protein by promoting the ubiquitination and degradation of MDM2. {ECO:0000250|UniProtKB:Q9HAC8}. SUBUNIT: Interacts with UBTD1. {ECO:0000250|UniProtKB:Q9HAC8}. +Q9JKB1 UCHL3_MOUSE Ubiquitin carboxyl-terminal hydrolase isozyme L3 (UCH-L3) (EC 3.4.19.12) (Ubiquitin thioesterase L3) 230 26,152 Active site (2); Chain (1); Modified residue (1); Mutagenesis (1); Region (3); Sequence conflict (1); Site (1) "FUNCTION: Deubiquitinating enzyme (DUB) that controls levels of cellular ubiquitin through processing of ubiquitin precursors and ubiquitinated proteins. Thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of either ubiquitin or NEDD8. Has a 10-fold preference for Arg and Lys at position P3"", and exhibits a preference towards 'Lys-48'-linked ubiquitin chains. Deubiquitinates ENAC in apical compartments, thereby regulating apical membrane recycling. Indirectly increases the phosphorylation of IGFIR, AKT and FOXO1 and promotes insulin-signaling and insulin-induced adipogenesis. Required for stress-response retinal, skeletal muscle and germ cell maintenance. May be involved in working memory. Can hydrolyze UBB(+1), a mutated form of ubiquitin which is not effectively degraded by the proteasome. {ECO:0000269|PubMed:15884048, ECO:0000269|PubMed:16816367, ECO:0000269|PubMed:17460351, ECO:0000269|PubMed:17967898, ECO:0000269|PubMed:19837878, ECO:0000269|PubMed:21762696}." SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11341770, ECO:0000269|PubMed:17967898}. SUBUNIT: Preferentially binds diubiquitin; the interaction does not hydrolyze diubiquitin but, in vitro, inhibits the hydrolyzing activity on other substrates. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in brain, liver, heart, thymus, kidney and testis. Highly expressed in the cauda epididymidis, in meiotic pachytene spermatocytes and post-meiotic spematids. In the retina, enriched in the photoreceptor inner segment. {ECO:0000269|PubMed:10713173, ECO:0000269|PubMed:11341770, ECO:0000269|PubMed:16816367, ECO:0000269|PubMed:17460351}. +Q8BG34 UBX10_MOUSE UBX domain-containing protein 10 (UBX domain-containing protein 3) 277 30,341 Chain (1); Domain (1); Modified residue (1); Sequence conflict (3) FUNCTION: VCP/p97-binding protein required for ciliogenesis. Acts as a tethering factor that facilitates recruitment of VCP/p97 to the intraflagellar transport complex B (IFT-B) in cilia. UBX domain-containing proteins act as tethering factors for VCP/p97 and may specify substrate specificity of VCP/p97. {ECO:0000250|UniProtKB:Q96LJ8}. SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000250|UniProtKB:Q96LJ8}. Note=Recruited to cilia in a VCP-dependent manner. {ECO:0000250|UniProtKB:Q96LJ8}. SUBUNIT: Interacts with CLUAP1; the interaction is direct and mediates interaction with the intraflagellar transport complex B (IFT-B). Interacts with VCP; the interaction is direct. {ECO:0000250|UniProtKB:Q96LJ8}. +Q9WUP7 UCHL5_MOUSE Ubiquitin carboxyl-terminal hydrolase isozyme L5 (UCH-L5) (EC 3.4.19.12) (Ubiquitin C-terminal hydrolase UCH37) (Ubiquitin thioesterase L5) 329 37,617 Active site (2); Alternative sequence (1); Beta strand (9); Chain (1); Helix (13); Modified residue (3); Region (1); Sequence conflict (3); Site (1) FUNCTION: Protease that specifically cleaves 'Lys-48'-linked polyubiquitin chains. Deubiquitinating enzyme associated with the 19S regulatory subunit of the 26S proteasome. Putative regulatory component of the INO80 complex; however is inactive in the INO80 complex and is activated by a transient interaction of the INO80 complex with the proteasome via ADRM1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Associates with the proteasome 19S subunit in the cytoplasm. Associates with the INO80 complex in the nucleus (By similarity). {ECO:0000250}. SUBUNIT: Component of the 19S (PA700) regulatory complex of the 26S proteasome. Interacts with ADRM1 and NFRKB. Component of the INO80 complex; specifically part of a complex module associated with N-terminus of INO80 (By similarity). {ECO:0000250}. +Q9Z2B2 UCP5_MOUSE Brain mitochondrial carrier protein 1 (BMCP-1) (Mitochondrial uncoupling protein 5) (UCP 5) (Solute carrier family 25 member 14) 325 36,286 Alternative sequence (1); Chain (1); Repeat (3); Transmembrane (6) TRANSMEM 38 54 Helical; Name=1. {ECO:0000255}.; TRANSMEM 112 128 Helical; Name=2. {ECO:0000255}.; TRANSMEM 145 165 Helical; Name=3. {ECO:0000255}.; TRANSMEM 199 215 Helical; Name=4. {ECO:0000255}.; TRANSMEM 240 256 Helical; Name=5. {ECO:0000255}.; TRANSMEM 298 315 Helical; Name=6. {ECO:0000255}. FUNCTION: Participates in the mitochondrial proton leak measured in brain mitochondria. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Mainly expressed in brain, particularly abundant in cortex, hippocampus thalamus, amygdala and hypothalamus. Expressed in other tissues to a lesser extent. {ECO:0000269|PubMed:10928996}. +Q99PM9 UCK2_MOUSE Uridine-cytidine kinase 2 (UCK 2) (EC 2.7.1.48) (Cytidine monophosphokinase 2) (Uridine monophosphokinase 2) 261 29,404 Binding site (7); Chain (1); Initiator methionine (1); Modified residue (2); Nucleotide binding (1) Pyrimidine metabolism; CTP biosynthesis via salvage pathway; CTP from cytidine: step 1/3. Pyrimidine metabolism; UMP biosynthesis via salvage pathway; UMP from uridine: step 1/1. FUNCTION: Phosphorylates uridine and cytidine to uridine monophosphate and cytidine monophosphate. Does not phosphorylate deoxyribonucleosides or purine ribonucleosides. Can use ATP or GTP as a phosphate donor. Can also phosphorylate cytidine and uridine nucleoside analogs such as 6-azauridine, 5-fluorouridine, 4-thiouridine, 5-bromouridine, N(4)-acetylcytidine, N(4)-benzoylcytidine, 5-fluorocytidine, 2-thiocytidine, 5-methylcytidine, and N(4)-anisoylcytidine (By similarity). {ECO:0000250}. SUBUNIT: Homotetramer. {ECO:0000250}. +Q91YL3 UCKL1_MOUSE Uridine-cytidine kinase-like 1 (EC 2.7.1.48) 548 60,842 Chain (1); Modified residue (3); Nucleotide binding (1) Pyrimidine metabolism; UMP biosynthesis via salvage pathway; UMP from uridine: step 1/1. FUNCTION: May contribute to UTP accumulation needed for blast transformation and proliferation. {ECO:0000250}. PTM: Ubiquitinated by RNF19B; which induces proteasomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Interacts with RNF19B. {ECO:0000250}. +Q99ML8 UCN2_MOUSE Urocortin-2 (Urocortin II) (Ucn II) 113 12,310 Chain (1); Modified residue (1); Propeptide (1); Signal peptide (1) FUNCTION: Suppresses food intake, delays gastric emptying and decreases heat-induced edema. Might represent an endogenous ligand for maintaining homeostasis after stress (By similarity). {ECO:0000250}. PTM: Glycosylated. {ECO:0000269|PubMed:23493376}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23493376}. SUBUNIT: Binds with high affinity to CRF receptors 2-alpha and 2-beta. {ECO:0000250}. +Q924A4 UCN3_MOUSE Urocortin-3 (Urocortin III) (Ucn III) 164 18,063 Chain (1); Modified residue (1); Propeptide (1); Signal peptide (1) FUNCTION: Suppresses food intake, delays gastric emptying and decreases heat-induced edema. Might represent an endogenous ligand for maintaining homeostasis after stress (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Binds with high affinity to CRF receptors 2-alpha and 2-beta. TISSUE SPECIFICITY: Expressed in some areas of the brain including the hypothalamus, amygdala, and brainstem, but is not evident in the cerebellum, pituitary, or cerebral cortex; it is also expressed peripherally in small intestine and skin. {ECO:0000269|PubMed:11416224}. +Q80X89 UD2A1_MOUSE UDP-glucuronosyltransferase 2A1 (UDPGT 2A1) (EC 2.4.1.17) 528 59,965 Chain (1); Glycosylation (2); Modified residue (1); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 495 515 Helical. {ECO:0000255}. TOPO_DOM 22 494 Extracellular. {ECO:0000255}.; TOPO_DOM 516 528 Cytoplasmic. {ECO:0000255}. FUNCTION: UDP-glucuronosyltransferases catalyze phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase water solubility and enhance excretion. They are of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. Active on odorants and seems to be involved in olfaction; it could help clear lipophilic odorant molecules from the sensory epithelium. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q3UP75 UD3A1_MOUSE UDP-glucuronosyltransferase 3A1 (UDPGT 3A1) (EC 2.4.1.17) 523 59,698 Chain (1); Glycosylation (1); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 488 508 Helical. {ECO:0000255}. TOPO_DOM 23 487 Extracellular. {ECO:0000255}.; TOPO_DOM 509 523 Cytoplasmic. {ECO:0000255}. FUNCTION: UDP-glucuronosyltransferases catalyze phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase water solubility and enhance excretion. They are of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Highly expressed in kidney, while it is expressed at low levels in liver. Not detected in other tissues examined. {ECO:0000269|PubMed:17050650}. +Q8CCJ3 UFL1_MOUSE E3 UFM1-protein ligase 1 (EC 2.3.2.-) (E3 UFM1-protein transferase 1) 793 89,520 Alternative sequence (3); Chain (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (5); Region (4); Sequence conflict (6) FUNCTION: E3 protein ligase that mediates ufmylation, the covalent attachment of the ubiquitin-like modifier UFM1 to substrate proteins, a post-translational modification on lysine residues of proteins that may play a crucial role in a number of cellular processes. Mediates DDRGK1 ufmylation and may regulate the proteasomal degradation of DDRGK1 and CDK5RAP3 thereby modulating NF-kappa-B signaling. May also through TRIP4 ufmylation play a role in nuclear receptors-mediated transcription. May play a role in the unfolded protein response, mediating the ufmylation of multiple proteins in response to endoplasmic reticulum stress. {ECO:0000250|UniProtKB:O94874}. PTM: Ubiquitinated, leading to its degradation by the proteasome. Interaction with CDK5RAP3 protects each other against ubiquitination and degradation via the proteasome. {ECO:0000250|UniProtKB:O94874}. SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:O94874}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:O94874}. SUBUNIT: Interacts with DDRGK1 (By similarity). Interacts with UFC1 (By similarity). Interacts with RELA (By similarity). Interacts with TRIP4 (By similarity). Interacts with CDK5RAP3; the interaction is direct (PubMed:21494687). {ECO:0000250|UniProtKB:O94874}. TISSUE SPECIFICITY: Ubiquitously expressed with higher expression in pancreatic islets and other secretory tissues. {ECO:0000269|PubMed:20228063, ECO:0000269|PubMed:21494687}. +O70475 UGDH_MOUSE UDP-glucose 6-dehydrogenase (UDP-Glc dehydrogenase) (UDP-GlcDH) (UDPGDH) (EC 1.1.1.22) 493 54,832 Active site (1); Binding site (6); Chain (1); Modified residue (2); Nucleotide binding (4); Region (4) Nucleotide-sugar biosynthesis; UDP-alpha-D-glucuronate biosynthesis; UDP-alpha-D-glucuronate from UDP-alpha-D-glucose: step 1/1. FUNCTION: Involved in the biosynthesis of glycosaminoglycans; hyaluronan, chondroitin sulfate, and heparan sulfate. {ECO:0000269|PubMed:9737970}. SUBUNIT: Homohexamer. {ECO:0000250}. +P62960 YBOX1_MOUSE Nuclease-sensitive element-binding protein 1 (CCAAT-binding transcription factor I subunit A) (CBF-A) (DNA-binding protein B) (DBPB) (Enhancer factor I subunit A) (EFI-A) (Y-box transcription factor) (Y-box-binding protein 1) (YB-1) 322 35,730 Chain (1); Cross-link (2); Domain (1); Initiator methionine (1); Modified residue (10); Region (1); Sequence conflict (3); Site (1) FUNCTION: Mediates pre-mRNA alternative splicing regulation. Component of the CRD-mediated complex that promotes MYC mRNA stability. Binds to splice sites in pre-mRNA and regulates splice site selection. Binds and stabilizes cytoplasmic mRNA. Contributes to the regulation of translation by modulating the interaction between the mRNA and eukaryotic initiation factors. Binds to promoters that contain a Y-box (5'-CTGATTGGCCAA-3'), such as HLA class II genes. Regulates the transcription of numerous genes. Promotes separation of DNA strands that contain mismatches or are modified by cisplatin. Has endonucleolytic activity and can introduce nicks or breaks into double-stranded DNA (in vitro). May play a role in DNA repair. Its transcriptional activity on the multidrug resistance gene MDR1 is enhanced in presence of the APEX1 acetylated form at 'Lys-6' and 'Lys-7'. Binds preferentially to 5'-[CU]CUGCG-3' motif in vitro (By similarity). {ECO:0000250|UniProtKB:P67809, ECO:0000250|UniProtKB:Q28618}.; FUNCTION: The secreted form acts as an extracellular mitogen and stimulates cell migration and proliferation. {ECO:0000250|UniProtKB:P67809, ECO:0000250|UniProtKB:Q28618}. PTM: Ubiquitinated by RBBP6; leading to a decrease of YBX1 transcactivational ability. {ECO:0000250|UniProtKB:P67809}.; PTM: In the absence of phosphorylation the protein is retained in the cytoplasm. {ECO:0000250|UniProtKB:P67809}.; PTM: Cleaved by a 20S proteasomal protease in response to agents that damage DNA. Cleavage takes place in the absence of ubiquitination and ATP. The resulting N-terminal fragment accumulates in the nucleus (By similarity). {ECO:0000250|UniProtKB:Q28618}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasmic granule {ECO:0000250|UniProtKB:P67809}. Secreted {ECO:0000250}. Note=Shuttles between nucleus and cytoplasm. Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Shuttles between nucleus and cytoplasm. Predominantly cytoplasmic in proliferating cells. Cytotoxic stress and DNA damage enhance translocation to the nucleus. Localized with DDX1, MBNL1 and TIAL1 in stress granules upon stress. Secreted by mesangial and monocytic cells after inflammatory challenges (By similarity). {ECO:0000250}. SUBUNIT: Component of the coding region determinant (CRD)-mediated complex, composed of DHX9, HNRNPU, IGF2BP1, SYNCRIP and YBX1. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Component of cytoplasmic messenger ribonucleoprotein particles (mRNPs). Component of the U11/U12 snRNPs that are part of the U12-type spliceosome. Interacts with AKT1, MBNL1, IGF2BP1, SFRS9, ALYREF/THOC4, MSH2, XRCC5, RBBP6, WRN and NCL. Can bind to DNA as a homomeric form, (EFI-A)n or as a heteromeric form in association with EFI-B. Homodimer in the presence of ATP. Can form heterotrimer with PURA and PURB. Interacts (via C-terminus) with APEX1 (via N-terminus); the interaction is increased with APEX1 acetylated at 'Lys-6' and 'Lys-7'. Interacts with AGO1 and AGO2 (By similarity). Interacts with ANKRD2 (By similarity). Interacts with DERA (By similarity). Can form heterotrimer with PURA and PURB. Identified in a histone pre-mRNA complex, at least composed of ERI1, LSM11, SLBP, SNRPB, SYNCRIP and YBX1. Interacts with FMR1; this interaction occurs in association with polyribosome (PubMed:11162447). Interacts with ZBTB7B (PubMed:28784777). {ECO:0000250|UniProtKB:P67809, ECO:0000250|UniProtKB:Q28618, ECO:0000269|PubMed:10318844, ECO:0000269|PubMed:11162447, ECO:0000269|PubMed:19470752, ECO:0000269|PubMed:28784777, ECO:0000269|PubMed:8505341}. TISSUE SPECIFICITY: Expressed at high levels in the testis. Present in the mRNP particles that mediate the storage and masking of mRNAs during spermiogenesis. {ECO:0000269|PubMed:8505341}. +O35304 VACHT_MOUSE Vesicular acetylcholine transporter (VAChT) (Solute carrier family 18 member 3) 530 56,615 Chain (1); Glycosylation (2); Region (1); Topological domain (13); Transmembrane (12) TRANSMEM 34 54 Helical. {ECO:0000255}.; TRANSMEM 126 146 Helical. {ECO:0000255}.; TRANSMEM 153 173 Helical. {ECO:0000255}.; TRANSMEM 183 203 Helical. {ECO:0000255}.; TRANSMEM 214 234 Helical. {ECO:0000255}.; TRANSMEM 243 263 Helical. {ECO:0000255}.; TRANSMEM 289 309 Helical. {ECO:0000255}.; TRANSMEM 326 346 Helical. {ECO:0000255}.; TRANSMEM 357 377 Helical. {ECO:0000255}.; TRANSMEM 389 409 Helical. {ECO:0000255}.; TRANSMEM 423 443 Helical. {ECO:0000255}.; TRANSMEM 448 468 Helical. {ECO:0000255}. TOPO_DOM 1 33 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 55 125 Lumenal, vesicle. {ECO:0000255}.; TOPO_DOM 147 152 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 174 182 Lumenal, vesicle. {ECO:0000255}.; TOPO_DOM 204 213 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 235 242 Lumenal, vesicle. {ECO:0000255}.; TOPO_DOM 264 288 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 310 325 Lumenal, vesicle. {ECO:0000255}.; TOPO_DOM 347 356 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 378 388 Lumenal, vesicle. {ECO:0000255}.; TOPO_DOM 410 422 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 444 447 Lumenal, vesicle. {ECO:0000255}.; TOPO_DOM 469 530 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in acetylcholine transport into synaptic vesicles. {ECO:0000250|UniProtKB:Q16572}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Interacts with SEC14L1. {ECO:0000269|PubMed:17092608}. TISSUE SPECIFICITY: Expressed in the spinal cord, brain (excluding the cerebellum), brain stem and cholinergic tissues. Not expressed in peripheral tissues such as liver and kidney. {ECO:0000269|PubMed:9427309}. +Q60930 VDAC2_MOUSE Voltage-dependent anion-selective channel protein 2 (VDAC-2) (mVDAC2) (Outer mitochondrial membrane protein porin 2) (Voltage-dependent anion-selective channel protein 6) (VDAC-6) (mVDAC6) 295 31,733 Chain (1); Cross-link (6); Modified residue (7); Nucleotide binding (2); Sequence conflict (1); Site (1); Transmembrane (19) TRANSMEM 38 47 Beta stranded. {ECO:0000250}.; TRANSMEM 51 59 Beta stranded. {ECO:0000250}.; TRANSMEM 66 76 Beta stranded. {ECO:0000250}.; TRANSMEM 81 88 Beta stranded. {ECO:0000250}.; TRANSMEM 92 101 Beta stranded. {ECO:0000250}.; TRANSMEM 107 116 Beta stranded. {ECO:0000250}.; TRANSMEM 123 132 Beta stranded. {ECO:0000250}.; TRANSMEM 135 142 Beta stranded. {ECO:0000250}.; TRANSMEM 149 157 Beta stranded. {ECO:0000250}.; TRANSMEM 162 170 Beta stranded. {ECO:0000250}.; TRANSMEM 175 187 Beta stranded. {ECO:0000250}.; TRANSMEM 190 197 Beta stranded. {ECO:0000250}.; TRANSMEM 201 210 Beta stranded. {ECO:0000250}.; TRANSMEM 214 223 Beta stranded. {ECO:0000250}.; TRANSMEM 230 239 Beta stranded. {ECO:0000250}.; TRANSMEM 243 250 Beta stranded. {ECO:0000250}.; TRANSMEM 254 263 Beta stranded. {ECO:0000250}.; TRANSMEM 266 275 Beta stranded. {ECO:0000250}.; TRANSMEM 285 294 Beta stranded. {ECO:0000250}. FUNCTION: Forms a channel through the mitochondrial outer membrane that allows diffusion of small hydrophilic molecules. The channel adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The open state has a weak anion selectivity whereas the closed state is cation-selective (By similarity). {ECO:0000250}. PTM: Ubiquitinated by PRKN during mitophagy, leading to its degradation and enhancement of mitophagy. Deubiquitinated by USP30. {ECO:0000250|UniProtKB:P45880}. SUBCELLULAR LOCATION: Mitochondrion outer membrane. SUBUNIT: Interacts with hexokinases. {ECO:0000250}. DOMAIN: Consists mainly of a membrane-spanning beta-barrel formed by 19 beta-strands. {ECO:0000250}. TISSUE SPECIFICITY: Highest levels of expression detected in testis, less but still abundant expression in heart, kidney, brain, and skeletal muscle. +Q9QZ25 VNN3_MOUSE Vascular non-inflammatory molecule 3 (Vanin-3) (EC 3.5.1.92) 500 56,305 Active site (3); Chain (1); Domain (1); Erroneous initiation (1); Glycosylation (5); Lipidation (1); Propeptide (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Amidohydrolase that hydrolyzes specifically one of the carboamide linkages in D-pantetheine thus recycling pantothenic acid (vitamin B5) and releasing cysteamine. {ECO:0000269|PubMed:11491533}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}. Note=According to PubMed:11491533, secreted. {ECO:0000269|PubMed:11491533}. TISSUE SPECIFICITY: Ubiquitous with higher expression in liver. {ECO:0000269|PubMed:11491533}. +Q8BUZ3 TIGD4_MOUSE Tigger transposable element-derived protein 4 513 57,472 Chain (1); DNA binding (2); Domain (3) SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q499M4 TIGD5_MOUSE Tigger transposable element derived 5 642 70,249 Alternative sequence (1); Chain (1); Compositional bias (2); DNA binding (2); Domain (3); Frameshift (2); Sequence conflict (2) SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q9QXG9 TINF2_MOUSE TERF1-interacting nuclear factor 2 (TRF1-interacting nuclear protein 2) 341 37,887 Chain (1); Initiator methionine (1); Modified residue (1); Motif (2); Sequence conflict (1) FUNCTION: Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded TTAGGG repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways. Plays a role in shelterin complex assembly (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, telomere {ECO:0000250}. SUBUNIT: Monomer. Found in a complex with POT1; TERF1 and TNKS1. Component of the shelterin complex (telosome) composed of TERF1, TERF2, TINF2, TERF2IP, ACD and POT1 (By similarity). Interacts with TERF1. {ECO:0000250, ECO:0000269|PubMed:19487455}. DOMAIN: The TBM domain mediates interaction with TERF1. {ECO:0000250}. +P39876 TIMP3_MOUSE Metalloproteinase inhibitor 3 (Tissue inhibitor of metalloproteinases 3) (TIMP-3) 211 24,182 Chain (1); Disulfide bond (6); Domain (1); Metal binding (1); Region (3); Sequence conflict (3); Signal peptide (1); Site (1) FUNCTION: Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. May form part of a tissue-specific acute response to remodeling stimuli. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SUBUNIT: Interacts with EFEMP1. {ECO:0000250}. TISSUE SPECIFICITY: Highest levels are found in kidney, lung and brain followed by ovary and uterus. Low levels are found in bone. +Q8BZ10 TM11G_MOUSE Transmembrane protease serine 11G (EC 3.4.21.-) (Serine protease DESC4) [Cleaved into: Transmembrane protease serine 11G non-catalytic chain; Transmembrane protease serine 11G catalytic chain] 417 46,614 Active site (3); Chain (2); Disulfide bond (3); Domain (2); Erroneous initiation (1); Glycosylation (1); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 22 42 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 21 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 43 417 Extracellular. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. +Q9D2E9 TM190_MOUSE Transmembrane protein 190 166 18,491 Chain (1); Disulfide bond (3); Domain (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 82 102 Helical. {ECO:0000255}. TOPO_DOM 22 81 Extracellular. {ECO:0000255}.; TOPO_DOM 103 166 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:21273369}; Single-pass type I membrane protein {ECO:0000269|PubMed:21273369}. Note=Localizes in the intracellular space in testicular germ cells and sperm. Detected also on the cell surface in post-meiotic round spermatids. In cauda epididymal sperm relocates during the acrosome reaction from the inner-acrosomal membrane onto the equatorial segment surface, on which sperm-oocyte fusion occurs. Colocalizes with IZUMO1 at the inner-acrosomal membrane. TISSUE SPECIFICITY: Detected in testis and in a mixture of spermatogenic cells at various stages (testicular germ cells). Not detected in heart, brain, spleen, lung, liver, skeletal muscle and kidney. {ECO:0000269|PubMed:21273369}. +Q80XA0 TM121_MOUSE Transmembrane protein 121 (Protein hole) 318 35,684 Chain (1); Compositional bias (1); Transmembrane (6) TRANSMEM 10 30 Helical. {ECO:0000255}.; TRANSMEM 43 63 Helical. {ECO:0000255}.; TRANSMEM 74 94 Helical. {ECO:0000255}.; TRANSMEM 112 132 Helical. {ECO:0000255}.; TRANSMEM 174 194 Helical. {ECO:0000255}.; TRANSMEM 214 234 Helical. {ECO:0000255}. FUNCTION: May play a role in MAPK signaling. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=May localize to the plasma membrane. {ECO:0000250}. +Q8BG75 TM198_MOUSE Transmembrane protein 198 360 39,752 Chain (1); Compositional bias (2); Transmembrane (7) TRANSMEM 36 56 Helical. {ECO:0000255}.; TRANSMEM 59 79 Helical. {ECO:0000255}.; TRANSMEM 93 113 Helical. {ECO:0000255}.; TRANSMEM 116 136 Helical. {ECO:0000255}.; TRANSMEM 145 165 Helical. {ECO:0000255}.; TRANSMEM 177 197 Helical. {ECO:0000255}.; TRANSMEM 218 238 Helical. {ECO:0000255}. FUNCTION: Promotes LRP6 phosphorylation by casein kinases and thereby plays a role in Wnt signaling. May be a membrane scaffold protein involved in the self-aggregation of LRP6 to further enhance its activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cell membrane {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Note=Largely located to vesicle-like structures. {ECO:0000250}. SUBUNIT: Interacts with LRP6. {ECO:0000250}. +Q5SYH2 TM199_MOUSE Transmembrane protein 199 208 23,099 Chain (1); Initiator methionine (1); Modified residue (1); Transmembrane (2) TRANSMEM 146 166 Helical. {ECO:0000255}.; TRANSMEM 179 199 Helical. {ECO:0000255}. FUNCTION: Accessory component of the proton-transporting vacuolar (V)-ATPase protein pump involved in intracellular iron homeostasis. In aerobic conditions, required for intracellular iron homeostasis, thus triggering the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent proteasomal degradation. Necessary for endolysosomal acidification and lysosomal degradation (By similarity). May be involved in Golgi homeostasis (By similarity). {ECO:0000250|UniProtKB:Q8N511}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250|UniProtKB:Q8N511}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q8N511}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8N511}; Multi-pass membrane protein {ECO:0000255}. Note=Partial colocalization with GOLGB1. {ECO:0000250|UniProtKB:Q8N511}. SUBUNIT: Accessory component of the multisubunit proton-transporting vacuolar (V)-ATPase protein pump. {ECO:0000250|UniProtKB:Q8N511}. +Q9D4Y8 TM269_MOUSE Transmembrane protein 269 254 28,198 Chain (1); Transmembrane (5) TRANSMEM 44 64 Helical. {ECO:0000255}.; TRANSMEM 69 89 Helical. {ECO:0000255}.; TRANSMEM 113 135 Helical. {ECO:0000255}.; TRANSMEM 171 191 Helical. {ECO:0000255}.; TRANSMEM 210 230 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. +Q922Z1 TM159_MOUSE Promethin (Transmembrane protein 159) 161 17,643 Chain (1); Glycosylation (1); Sequence conflict (1); Transmembrane (3) TRANSMEM 55 75 Helical. {ECO:0000255}.; TRANSMEM 89 109 Helical. {ECO:0000255}.; TRANSMEM 112 132 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Prominently expressed in the heart and kidney. Expressed at higher levels in white fat as compared to brown fat and skeletal muscle. Expressed at lower levels in lung, liver and testis. {ECO:0000269|PubMed:15589683}. +Q99MB3 TM2D1_MOUSE TM2 domain-containing protein 1 (Amyloid-beta-binding protein) (mBBP) 208 22,272 Alternative sequence (1); Chain (1); Erroneous gene model prediction (1); Frameshift (1); Glycosylation (2); Sequence conflict (2); Signal peptide (1); Transmembrane (2) TRANSMEM 120 137 Helical. {ECO:0000255}.; TRANSMEM 155 175 Helical. {ECO:0000255}. FUNCTION: May participate in amyloid-beta-induced apoptosis via its interaction with beta-APP42. {ECO:0000250}. PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with APP beta-APP42 (amyloid-beta protein 42). {ECO:0000250}. +A2ARJ3 TM236_MOUSE Transmembrane protein 236 344 38,680 Chain (1); Glycosylation (1); Transmembrane (6) TRANSMEM 9 29 Helical. {ECO:0000255}.; TRANSMEM 47 67 Helical. {ECO:0000255}.; TRANSMEM 86 106 Helical. {ECO:0000255}.; TRANSMEM 122 142 Helical. {ECO:0000255}.; TRANSMEM 257 277 Helical. {ECO:0000255}.; TRANSMEM 294 314 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q14C59 TM11B_MOUSE Transmembrane protease serine 11B-like protein (EC 3.4.21.-) (Airway trypsin-like protease 5) (Transmembrane protease serine 11B) 416 46,713 Active site (3); Chain (1); Disulfide bond (3); Domain (2); Glycosylation (2); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 16 36 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 15 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 37 416 Extracellular. {ECO:0000255}. FUNCTION: Serine protease. {ECO:0000250|UniProtKB:Q86T26}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q86T26}; Single-pass type II membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in esophagus, cervix, tongue, and testes. {ECO:0000269|PubMed:24498351}. +Q9D8N3 TM86A_MOUSE Lysoplasmalogenase-like protein TMEM86A (Transmembrane protein 86A) 241 26,273 Chain (1); Sequence conflict (1); Transmembrane (7) TRANSMEM 15 35 Helical. {ECO:0000255}.; TRANSMEM 36 56 Helical. {ECO:0000255}.; TRANSMEM 67 87 Helical. {ECO:0000255}.; TRANSMEM 93 113 Helical. {ECO:0000255}.; TRANSMEM 134 154 Helical. {ECO:0000255}.; TRANSMEM 175 195 Helical. {ECO:0000255}.; TRANSMEM 207 227 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q497J1 TM86B_MOUSE Lysoplasmalogenase (EC 3.3.2.2) (Transmembrane protein 86B) 226 24,989 Chain (1); Transmembrane (7) TRANSMEM 24 44 Helical. {ECO:0000255}.; TRANSMEM 57 77 Helical. {ECO:0000255}.; TRANSMEM 97 117 Helical. {ECO:0000255}.; TRANSMEM 122 141 Helical. {ECO:0000255}.; TRANSMEM 147 163 Helical. {ECO:0000255}.; TRANSMEM 166 186 Helical. {ECO:0000255}.; TRANSMEM 195 215 Helical. {ECO:0000255}. FUNCTION: Enzyme catalyzing the degradation of lysoplasmalogen. Lysoplasmalogens are formed by the hydrolysis of the abundant membrane glycerophospholipids plasmalogens. May control the respective levels of plasmalogens and lysoplasmalogens in cells and modulate cell membrane properties. {ECO:0000250|UniProtKB:B0BNF0}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm {ECO:0000250|UniProtKB:Q8N661}. SUBUNIT: Homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Enriched in liver. Also detected in brain and testis. {ECO:0000269|PubMed:21515882}. +Q8BM55 TM214_MOUSE Transmembrane protein 214 687 76,430 Alternative sequence (2); Chain (1); Erroneous initiation (2); Glycosylation (2); Initiator methionine (1); Modified residue (1); Sequence conflict (7); Transmembrane (2) TRANSMEM 481 501 Helical. {ECO:0000255}.; TRANSMEM 614 634 Helical. {ECO:0000255}. FUNCTION: Critical mediator, in cooperation with CASP4, of endoplasmic reticulum-stress induced apoptosis. Required or the activation of CASP4 following endoplasmic reticulum stress (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Constitutively interacts with CASP4; required for the localization of procaspase 4 to the ER. {ECO:0000250}. +Q60774 TM45A_MOUSE Transmembrane protein 45A (19.5) (Dermal papilla-derived protein 7 homolog) 273 31,343 Chain (1); Transmembrane (5) TRANSMEM 8 27 Helical. {ECO:0000255}.; TRANSMEM 55 79 Helical. {ECO:0000255}.; TRANSMEM 108 131 Helical. {ECO:0000255}.; TRANSMEM 153 171 Helical. {ECO:0000255}.; TRANSMEM 217 236 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q7TQ65 TMC4_MOUSE Transmembrane channel-like protein 4 694 77,367 Alternative sequence (3); Chain (1); Glycosylation (1); Sequence conflict (9); Topological domain (11); Transmembrane (10) TRANSMEM 151 171 Helical. {ECO:0000255}.; TRANSMEM 232 252 Helical. {ECO:0000255}.; TRANSMEM 331 351 Helical. {ECO:0000255}.; TRANSMEM 377 397 Helical. {ECO:0000255}.; TRANSMEM 408 428 Helical. {ECO:0000255}.; TRANSMEM 466 486 Helical. {ECO:0000255}.; TRANSMEM 514 534 Helical. {ECO:0000255}.; TRANSMEM 536 556 Helical. {ECO:0000255}.; TRANSMEM 575 595 Helical. {ECO:0000255}.; TRANSMEM 636 656 Helical. {ECO:0000255}. TOPO_DOM 1 150 Extracellular. {ECO:0000255}.; TOPO_DOM 172 231 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 253 330 Extracellular. {ECO:0000255}.; TOPO_DOM 352 376 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 398 407 Extracellular. {ECO:0000255}.; TOPO_DOM 429 465 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 487 513 Extracellular. {ECO:0000255}.; TOPO_DOM 535 535 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 557 574 Extracellular. {ECO:0000255}.; TOPO_DOM 596 635 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 657 694 Extracellular. {ECO:0000255}. FUNCTION: Probable ion channel. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:12812529}. +Q9ET30 TM9S3_MOUSE Transmembrane 9 superfamily member 3 587 67,545 Chain (1); Erroneous initiation (1); Glycosylation (2); Signal peptide (1); Transmembrane (9) TRANSMEM 222 242 Helical. {ECO:0000255}.; TRANSMEM 292 312 Helical. {ECO:0000255}.; TRANSMEM 326 346 Helical. {ECO:0000255}.; TRANSMEM 358 378 Helical. {ECO:0000255}.; TRANSMEM 387 407 Helical. {ECO:0000255}.; TRANSMEM 447 467 Helical. {ECO:0000255}.; TRANSMEM 480 500 Helical. {ECO:0000255}.; TRANSMEM 517 537 Helical. {ECO:0000255}.; TRANSMEM 549 569 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q7TNI2 TM59L_MOUSE Transmembrane protein 59-like (Brain-specific membrane-anchored protein) 337 37,661 Chain (1); Glycosylation (1); Motif (1); Signal peptide (1); Transmembrane (1) TRANSMEM 263 283 Helical. {ECO:0000255}. FUNCTION: Modulates the O-glycosylation and complex N-glycosylation steps occurring during the Golgi maturation of APP. Inhibits APP transport to the cell surface and further shedding (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. +Q8K174 TMM60_MOUSE Transmembrane protein 60 133 15,518 Chain (1); Transmembrane (4) TRANSMEM 5 25 Helical. {ECO:0000255}.; TRANSMEM 35 55 Helical. {ECO:0000255}.; TRANSMEM 78 98 Helical. {ECO:0000255}.; TRANSMEM 110 130 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8BXJ9 TMM62_MOUSE Transmembrane protein 62 643 72,862 Chain (1); Glycosylation (1); Transmembrane (5) TRANSMEM 9 29 Helical. {ECO:0000255}.; TRANSMEM 431 451 Helical. {ECO:0000255}.; TRANSMEM 484 504 Helical. {ECO:0000255}.; TRANSMEM 532 552 Helical. {ECO:0000255}.; TRANSMEM 572 592 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9DCF1 TMM25_MOUSE Transmembrane protein 25 365 39,170 Alternative sequence (1); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (4); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 233 253 Helical. {ECO:0000255}. TOPO_DOM 27 232 Extracellular. {ECO:0000255}.; TOPO_DOM 254 365 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Isoform 1: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: Isoform 2: Secreted {ECO:0000305}. +Q60769 TNAP3_MOUSE Tumor necrosis factor alpha-induced protein 3 (TNF alpha-induced protein 3) (EC 2.3.2.-) (EC 3.4.19.12) (Putative DNA-binding protein A20) (Zinc finger protein A20) 775 87,654 Active site (3); Beta strand (13); Chain (1); Domain (1); Helix (14); Initiator methionine (1); Modified residue (2); Mutagenesis (2); Region (9); Sequence conflict (1); Turn (5); Zinc finger (7) FUNCTION: Ubiquitin-editing enzyme that contains both ubiquitin ligase and deubiquitinase activities. Involved in immune and inflammatory responses signaled by cytokines, such as TNF-alpha and IL-1 beta, or pathogens via Toll-like receptors (TLRs) through terminating NF-kappa-B activity. Essential component of a ubiquitin-editing protein complex, comprising also RNF11, ITCH and TAX1BP1, that ensures the transient nature of inflammatory signaling pathways. In cooperation with TAX1BP1 promotes disassembly of E2-E3 ubiquitin protein ligase complexes in IL-1R and TNFR-1 pathways; affected are at least E3 ligases TRAF6, TRAF2 and BIRC2, and E2 ubiquitin-conjugating enzymes UBE2N and UBE2D3. In cooperation with TAX1BP1 promotes ubiquitination of UBE2N and proteasomal degradation of UBE2N and UBE2D3. Upon TNF stimulation, deubiquitinates 'Lys-63'-polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-48'-polyubiquitin chains. This leads to RIPK1 proteasomal degradation and consequently termination of the TNF- or LPS-mediated activation of NF-kappa-B. Deubiquitinates TRAF6 probably acting on 'Lys-63'-linked polyubiquitin. Upon T-cell receptor (TCR)-mediated T-cell activation, deubiquitinates 'Lys-63'-polyubiquitin chains on MALT1 thereby mediating disassociation of the CBM (CARD11:BCL10:MALT1) and IKK complexes and preventing sustained IKK activation. Deubiquitinates NEMO/IKBKG; the function is facilitated by TNIP1 and leads to inhibition of NF-kappa-B activation. Upon stimulation by bacterial peptidoglycans, probably deubiquitinates RIPK2. Can also inhibit I-kappa-B-kinase (IKK) through a non-catalytic mechanism which involves polyubiquitin; polyubiquitin promotes association with IKBKG and prevents IKK MAP3K7-mediated phosphorylation. Targets TRAF2 for lysosomal degradation. In vitro able to deubiquitinate 'Lys-11'-, 'Lys-48'- and 'Lys-63' polyubiquitin chains. Inhibitor of programmed cell death. Has a role in the function of the lymphoid system. Required for LPS-induced production of proinflammatory cytokines and IFN beta in LPS-tolerized macrophages. {ECO:0000269|PubMed:10385526, ECO:0000269|PubMed:11389905, ECO:0000269|PubMed:15334086, ECO:0000269|PubMed:18342009, ECO:0000269|PubMed:20185725, ECO:0000269|PubMed:23609450}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Lysosome {ECO:0000250}. SUBUNIT: Homodimer. Interacts with TNIP1, TAX1BP1 and TRAF2. Interacts with RNF11, ITCH and TAX1BP1 only after TNF stimulation; these interaction are transient and they are lost after 1 hour of stimulation with TNF (By similarity). Interacts with YWHAZ and YWHAH. Interacts with IKBKG; the interaction is induced by TNF stimulation and by polyubiquitin. Interacts with RIPK1. Interacts with UBE2N; the interaction requires TAX1BP1. Interacts with TRAF6 (By similarity). {ECO:0000250}. DOMAIN: The A20-type zinc fingers mediate the ubiquitin ligase activity. The A20-type zinc finger 4 selectively recognizes 'Lys-63'-linked polyubiquitin. The A20-type zinc finger 4-7 are sufficient to bind polyubiquitin (By similarity). {ECO:0000250}.; DOMAIN: The OTU domain mediates the deubiquitinase activity. {ECO:0000250}. TISSUE SPECIFICITY: Found in most tissues during development. Strikingly high levels are found in lymphoid organs, including the thymus, spleen, and gut-associated lymphoid tissue. Constitutively expressed in immature and mature thymocyte subpopulations as well as in resting peripheral T-cells; activation of these leads to down-regulation. +Q8K467 TMIE_MOUSE Transmembrane inner ear expressed protein 153 17,027 Chain (1); Compositional bias (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 59 79 Helical. {ECO:0000255}. TOPO_DOM 29 58 Extracellular. {ECO:0000255}.; TOPO_DOM 80 153 Cytoplasmic. {ECO:0000255}. FUNCTION: Unknown. The protein may play some role in a cellular membrane location. May reside within an internal membrane compartment and function in pathways such as those involved in protein and/or vesicle trafficking. Alternatively, the mature protein may be localized in the plasma membrane and serve as a site of interaction for other molecules through its highly charged C-terminal domain. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Interacts with TOMT. {ECO:0000269|PubMed:28504928}. TISSUE SPECIFICITY: Expressed in brain, kidney, liver, lung and cochlea. {ECO:0000269|PubMed:12140191}. DISEASE: Note=Defects in Tmie are the cause of the spinner mutant strain phenotype (sr). This disorder results in hearing loss and vestibular dysfunction due to neuroepithelial defects in the inner ear. It is recognized by behavioral dysfunction, including bidirectional circling and head shaking. Auditory function in spinner mice is found to be reduced, based upon the lack of a startle reflex to sound at any age. Breeding experiments indicated that these defects are inherited in an autosomal recessive fashion. The postnatal defects present in the cochleae of sr/sr mice suggest a requirement for Tmie during maturation of sensory cells, including the normal development or maintenance of stereocilia bundles. {ECO:0000269|PubMed:12140191}. +Q8BG19 TMTC4_MOUSE Protein O-mannosyl-transferase TMTC4 (EC 2.4.1.109) (Transmembrane and TPR repeat-containing protein 4) 741 82,963 Alternative sequence (3); Chain (1); Erroneous initiation (2); Frameshift (1); Repeat (8); Sequence conflict (1); Transmembrane (12) TRANSMEM 11 31 Helical. {ECO:0000255}.; TRANSMEM 111 131 Helical. {ECO:0000255}.; TRANSMEM 147 164 Helical. {ECO:0000255}.; TRANSMEM 165 185 Helical. {ECO:0000255}.; TRANSMEM 199 219 Helical. {ECO:0000255}.; TRANSMEM 225 245 Helical. {ECO:0000255}.; TRANSMEM 266 286 Helical. {ECO:0000255}.; TRANSMEM 327 347 Helical. {ECO:0000255}.; TRANSMEM 355 375 Helical. {ECO:0000255}.; TRANSMEM 383 403 Helical. {ECO:0000255}.; TRANSMEM 413 433 Helical. {ECO:0000255}.; TRANSMEM 442 462 Helical. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Transfers mannosyl residues to the hydroxyl group of serine or threonine residues. The 4 members of the TMTC family are O-mannosyl-transferases dedicated primarily to the cadherin superfamily, each member seems to have a distinct role in decorating the cadherin domains with O-linked mannose glycans at specific regions. Also acts as O-mannosyl-transferase on other proteins such as PDIA3. {ECO:0000250|UniProtKB:Q5T4D3}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q5T4D3}. +O88346 TNNT1_MOUSE Troponin T, slow skeletal muscle (TnTs) (Slow skeletal muscle troponin T) (sTnT) 262 31,344 Alternative sequence (2); Chain (1); Modified residue (1) FUNCTION: Troponin T is the tropomyosin-binding subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity. TISSUE SPECIFICITY: Expressed in adult soleus muscle. {ECO:0000269|PubMed:9651500}. +Q9D850 TMM68_MOUSE Transmembrane protein 68 329 37,810 Alternative sequence (2); Chain (1); Sequence conflict (1); Transmembrane (2) TRANSMEM 51 71 Helical. {ECO:0000255}.; TRANSMEM 121 141 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +G3X8R9 TMIG3_MOUSE Transmembrane domain-containing protein TMIGD3 209 23,452 Chain (1); Sequence conflict (1); Signal peptide (1); Transmembrane (1) TRANSMEM 152 172 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P0DMS9}; Single-pass type I membrane protein {ECO:0000255}. +Q9D1D4 TMEDA_MOUSE Transmembrane emp24 domain-containing protein 10 (21 kDa transmembrane-trafficking protein) (Transmembrane protein Tmp21) (p24 family protein delta-1) (p24delta1) 219 24,911 Alternative sequence (1); Chain (1); Domain (1); Glycosylation (1); Modified residue (4); Motif (2); Region (4); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 186 206 Helical. {ECO:0000255}. TOPO_DOM 32 185 Lumenal. {ECO:0000255}.; TOPO_DOM 207 219 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in vesicular protein trafficking. Mainly functions in the early secretory pathway. Thought to act as cargo receptor at the lumenal side for incorporation of secretory cargo molecules into transport vesicles and to be involved in vesicle coat formation at the cytoplasmic side. In COPII vesicle-mediated anterograde transport involved in the transport of GPI-anchored proteins and proposed to act together with TMED2 as their cargo receptor; the function specifically implies SEC24C and SEC24D of the COPII vesicle coat and lipid raft-like microdomains of the ER. Recognizes GPI anchors structural remodeled in the ER by PGAP1 and MPPE1. In COPI vesicle-mediated retrograde transport involved in the biogenesis of COPI vesicles and vesicle coat recruitment. On Golgi membranes, acts as primary receptor for ARF1-GDP which is involved in COPI-vesicle formation. Increases coatomer-dependent GTPase-activating activity of ARFGAP2. Involved in trafficking of G protein-coupled receptors (GPCRs). Regulates F2LR1, OPRM1 and P2RY4 exocytic trafficking from the Golgi to the plasma membrane thus contributing to receptor resensitization. Involved in trafficking of amyloid beta A4 protein and soluble APP-beta release (independent of modulation of gamma-secretase activity). As part of the presenilin-dependent gamma-secretase complex regulates gamma-cleavages of the amyloid beta A4 protein to yield amyloid-beta 40 (Abeta40). Involved in organization of the Golgi apparatus (By similarity). {ECO:0000250, ECO:0000269|PubMed:10660306}. SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Melanosome {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000269|PubMed:17101722}; Single-pass type I membrane protein {ECO:0000269|PubMed:17101722}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Cycles between compartments of the early secretatory pathway. {ECO:0000250}. SUBUNIT: Predominantly homodimeric and to lesser extent monomeric in endoplasmic reticulum. Homodimer and monomer in endoplasmic reticulum-Golgi intermediate compartment and cis-Golgi network. Probably oligomerizes with other members of the EMP24/GP25L family such as TMED2, TMED7 and TMED9. Interacts (via GOLD domain) with TMED2 (via GOLD domain). Associates with the COPI vesicle coat (coatomer); TMED10:TMED2 heterotetramers are proposed to be involved in coatomer association. Interacts (via C-terminus) with COPG1; the interaction involves dimeric TMED10. Interacts with ARF1 (GDP-bound); the interaction probably involves a TMED10 oligomer. Interacts with SEC23A; indicative for an association of TMED10 with the COPII vesicle coat. Interacts with CD59, SEC24B, SEC24C and SEC24D. Interacts with MPPE1/PGAP5. Interacts with F2LR1. Interacts with KDELR2; the interaction is disrupted by KDELR2 ligand. Found in a complex composed at least of SURF4, TMED2 and TMED10. Associates with the presenilin-dependent gamma-secretase complex. Interacts with STX17; the interaction is direct (By similarity). {ECO:0000250|UniProtKB:O35587, ECO:0000250|UniProtKB:P49755, ECO:0000250|UniProtKB:Q63584}. DOMAIN: The lumenal domain mediates localization to the plasma membrane by partially overriding the ER retention by the cytoplasmic domain. +Q5U405 TMPSD_MOUSE Transmembrane protease serine 13 (EC 3.4.21.-) (Membrane-type mosaic serine protease) (Mosaic serine protease) 543 59,806 Active site (3); Chain (1); Compositional bias (1); Disulfide bond (6); Domain (3); Glycosylation (4); Region (2); Repeat (12); Sequence conflict (3); Topological domain (2); Transmembrane (1) TRANSMEM 144 164 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 143 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 165 543 Extracellular. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. +Q8VBT0 TMX1_MOUSE Thioredoxin-related transmembrane protein 1 (Thioredoxin domain-containing protein 1) 278 31,396 Chain (1); Disulfide bond (1); Domain (1); Modified residue (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 182 202 Helical. {ECO:0000255}. TOPO_DOM 27 181 Extracellular. {ECO:0000255}.; TOPO_DOM 203 278 Cytoplasmic. {ECO:0000255}. FUNCTION: May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Predominantly found in the endoplasmic reticulum. {ECO:0000250}. +Q91ZE0 TMLH_MOUSE Trimethyllysine dioxygenase, mitochondrial (EC 1.14.11.8) (Epsilon-trimethyllysine 2-oxoglutarate dioxygenase) (TML hydroxylase) (TML-alpha-ketoglutarate dioxygenase) (TML dioxygenase) (TMLD) 421 49,610 Chain (1); Erroneous initiation (1); Metal binding (3); Modified residue (2); Sequence conflict (2); Transit peptide (1) Amine and polyamine biosynthesis; carnitine biosynthesis. FUNCTION: Converts trimethyllysine (TML) into hydroxytrimethyllysine (HTML). {ECO:0000250|UniProtKB:Q9NVH6}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:Q9NVH6}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q91ZW6}. +Q04750 TOP1_MOUSE DNA topoisomerase 1 (EC 5.99.1.2) (DNA topoisomerase I) 767 90,876 Active site (1); Chain (1); Compositional bias (1); Cross-link (19); Initiator methionine (1); Modified residue (8); Region (3); Sequence conflict (10); Site (9) FUNCTION: Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free DNA strand then rotates around the intact phosphodiester bond on the opposing strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells. Involved in the circadian transcription of the core circadian clock component ARNTL/BMAL1 by altering the chromatin structure around the ROR response elements (ROREs) on the ARNTL/BMAL1 promoter. {ECO:0000250|UniProtKB:P11387}. PTM: Sumoylated. Lys-119 is the main site of sumoylation. Sumoylation plays a role in partitioning TOP1 between nucleoli and nucleoplasm. Levels are dramatically increased on camptothecin (CPT) treatment. {ECO:0000250|UniProtKB:P11387}.; PTM: Phosphorylation at Ser-508 by CK2 increases binding to supercoiled DNA and sensitivity to camptothecin. {ECO:0000250|UniProtKB:P11387}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:P11387}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P11387}. Note=Diffuse nuclear localization with some enrichment in nucleoli. On CPT treatment, cleared from nucleoli into nucleoplasm. Sumoylated forms found in both nucleoplasm and nucleoli. {ECO:0000250|UniProtKB:P11387}. SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P11387}. +Q9ER39 TOR1A_MOUSE Torsin-1A (Dystonia 1 protein) (Torsin ATPase 1) (EC 3.6.4.-) (Torsin family 1 member A) 333 37,830 Chain (1); Glycosylation (2); Mutagenesis (1); Nucleotide binding (1); Region (3); Signal peptide (1) FUNCTION: Protein with chaperone functions important for the control of protein folding, processing, stability and localization as well as for the reduction of misfolded protein aggregates. Involved in the regulation of synaptic vesicle recycling, controls STON2 protein stability in collaboration with the COP9 signalosome complex (CSN). In the nucleus, may link the cytoskeleton with the nuclear envelope, this mechanism seems to be crucial for the control of nuclear polarity, cell movement and, specifically in neurons, nuclear envelope integrity. Participates in the cellular trafficking and may regulate the subcellular location of multipass membrane proteins such as the dopamine transporter SLC6A3, leading to the modulation of dopamine neurotransmission. In the endoplasmic reticulum, plays a role in the quality control of protein folding by increasing clearance of misfolded proteins such as SGCE variants or holding them in an intermediate state for proper refolding. May have a redundant function with TOR1B in non-neural tissues. {ECO:0000269|PubMed:16364897, ECO:0000269|PubMed:17200151, ECO:0000269|PubMed:17428918, ECO:0000269|PubMed:18827015, ECO:0000269|PubMed:20457914}. PTM: N-glycosylated. {ECO:0000269|PubMed:20015956}. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Nucleus membrane; Peripheral membrane protein. Cell projection, growth cone. Cytoplasmic vesicle membrane {ECO:0000250}. Cell junction, synapse, synaptosome {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250}. Note=Upon oxidative stress, redistributes to protusions from the cell surface (By similarity). Peripherally associated with the inner face of the ER membrane, probably mediated by the interaction with TOR1AIP1. The association with nucleus membrane is mediated by the interaction with TOR1AIP2. {ECO:0000250}. SUBUNIT: Homohexamer. Interacts with TOR1B; the interaction may be specific of neural tissues. Interacts (ATP-bound) with TOR1AIP1 and TOR1AIP2; the interactions induce ATPase activity. Interacts with KLHL14; preferentially when ATP-free. Interacts with KLC1 (via TPR repeats); the interaction associates TOR1A with the kinesin oligomeric complex. Interacts with COPS4; the interaction associates TOR1A with the CSN complex. Interacts with SNAPIN; the interaction is direct and associates SNAPIN with the CSN complex. Interacts with STON2. Interacts (ATP-bound) with SYNE3 (via KASH domain); the interaction is required for SYNE3 nuclear envelope localization. Interacts with VIM; the interaction associates TOR1A with the cytoskeleton. Interacts with PLEC. Interacts (ATP-bound) with SLC6A3; regulates SLC6A3 transport to the plasma membrane. {ECO:0000269|PubMed:18827015, ECO:0000269|PubMed:19535332, ECO:0000269|PubMed:20457914}. TISSUE SPECIFICITY: Widely expressed (at protein level). {ECO:0000269|PubMed:16364897, ECO:0000269|PubMed:20015956}. +Q9D173 TOM7_MOUSE Mitochondrial import receptor subunit TOM7 homolog (Translocase of outer membrane 7 kDa subunit homolog) 55 6,177 Chain (1); Topological domain (2); Transmembrane (1) TRANSMEM 21 40 Helical. {ECO:0000255}. TOPO_DOM 1 20 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 41 55 Mitochondrial intermembrane. {ECO:0000250}. FUNCTION: Required for assembly and stability of the TOM complex (By similarity). Positive regulator of PRKN translocation to damaged mitochondria. Acts probably by stabilizing PINK1 on the outer membrane of depolarized mitochondria (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. SUBUNIT: Forms part of the preprotein translocase complex of the outer mitochondrial membrane (TOM complex) which consists of at least 7 different proteins (TOMM5, TOMM6, TOMM7, TOMM20, TOMM22, TOMM40 and TOMM70). {ECO:0000250}. +Q8BU11 TOX4_MOUSE TOX high mobility group box family member 4 (Epidermal Langerhans cell protein LCP1) 619 65,961 Chain (1); Compositional bias (2); DNA binding (1); Modified residue (12); Motif (1); Sequence conflict (9) FUNCTION: Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}. Note=Associated with chromatin. SUBUNIT: Component of the PTW/PP1 phosphatase complex, composed of PPP1R10/PNUTS, TOX4, WDR82 and PPP1CA or PPP1CB or PPP1CC. Interacts with PPP1R10/PNUTS (By similarity). {ECO:0000250}. +Q9Z0L0 TPBG_MOUSE Trophoblast glycoprotein (5T4 oncofetal trophoblast glycoprotein) (5T4 oncotrophoblast glycoprotein) (Wnt-activated inhibitory factor 1) (WAIF1) 426 46,451 Chain (1); Compositional bias (1); Disulfide bond (4); Domain (2); Glycosylation (2); Modified residue (1); Repeat (7); Sequence conflict (5); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 362 382 Helical. {ECO:0000255}. TOPO_DOM 32 361 Extracellular. {ECO:0000255}.; TOPO_DOM 383 426 Cytoplasmic. {ECO:0000255}. FUNCTION: May function as an inhibitor of Wnt/beta-catenin signaling by indirectly interacting with LRP6 and blocking Wnt3a-dependent LRP6 internalization. {ECO:0000250}. PTM: Highly glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. DOMAIN: The C-terminus of LRR N-terminal cap (LRRNT) and LRR 1 are essential for the inhibition of the Wnt signaling pathway. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in embryo and placenta. In adult, expressed only in brain and ovary. Not detected in kidney small intestine, heart, spleen, testis, liver, lung, thymus and stomach. {ECO:0000269|PubMed:10366710}. +Q4KL14 TPC3L_MOUSE Trafficking protein particle complex subunit 3-like protein (TRAPPC3-like protein) (BET3-like protein) 181 20,763 Chain (1); Lipidation (1) FUNCTION: May play a role in vesicular transport from endoplasmic reticulum to Golgi. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. SUBUNIT: Homodimer. Component of the multisubunit TRAPP (transport protein particle) complex, which includes at least TRAPPC2, TRAPPC2L, TRAPPC3, TRAPPC3L, TRAPPC4, TRAPPC5, TRAPPC8, TRAPPC9, TRAPPC10, TRAPPC11 and TRAPPC12 (By similarity). {ECO:0000250}. +Q9CQA1 TPPC5_MOUSE Trafficking protein particle complex subunit 5 188 20,795 Chain (1); Modified residue (1); Sequence conflict (1) FUNCTION: May play a role in vesicular transport from endoplasmic reticulum to Golgi. SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. SUBUNIT: Component of the multisubunit TRAPP (transport protein particle) complex, which includes at least TRAPPC2, TRAPPC2L, TRAPPC3, TRAPPC3L, TRAPPC4, TRAPPC5, TRAPPC8, TRAPPC9, TRAPPC10, TRAPPC11 and TRAPPC12. {ECO:0000250}. +Q7M712 TR110_MOUSE Taste receptor type 2 member 110 (T2R110) (mT2r57) (STC 9-1) 333 37,837 Chain (1); Glycosylation (2); Sequence conflict (4); Topological domain (8); Transmembrane (7) TRANSMEM 14 34 Helical; Name=1. {ECO:0000255}.; TRANSMEM 61 81 Helical; Name=2. {ECO:0000255}.; TRANSMEM 90 110 Helical; Name=3. {ECO:0000255}.; TRANSMEM 134 154 Helical; Name=4. {ECO:0000255}.; TRANSMEM 206 226 Helical; Name=5. {ECO:0000255}.; TRANSMEM 256 276 Helical; Name=6. {ECO:0000255}.; TRANSMEM 284 304 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 13 Extracellular. {ECO:0000255}.; TOPO_DOM 35 60 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 82 89 Extracellular. {ECO:0000255}.; TOPO_DOM 111 133 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 155 205 Extracellular. {ECO:0000255}.; TOPO_DOM 227 255 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 277 283 Extracellular. {ECO:0000255}.; TOPO_DOM 305 333 Cytoplasmic. {ECO:0000255}. FUNCTION: Gustducin-coupled receptor implicated in the perception of bitter compounds in the oral cavity and the gastrointestinal tract. Signals through PLCB2 and the calcium-regulated cation channel TRPM5 (By similarity). {ECO:0000250|UniProtKB:Q9JKE8}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +O55055 TRDMT_MOUSE tRNA (cytosine(38)-C(5))-methyltransferase (EC 2.1.1.204) (DNA (cytosine-5)-methyltransferase-like protein 2) (Dnmt2) (DNA methyltransferase homolog MmuIIP) (DNA MTase homolog MmuIIP) (M.MmuIIP) (Met-2) 415 46,794 Active site (1); Binding site (3); Chain (1); Domain (1); Region (2); Sequence conflict (1) FUNCTION: Specifically methylates cytosine 38 in the anticodon loop of tRNA(Asp). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: Highly expressed in thymus, testis, and at much lower levels in spleen, lung, brain, heart, kidney, liver, skeletal muscle and embryonic stem cells. {ECO:0000269|PubMed:9592134}. +Q9WU56 TRUA_MOUSE tRNA pseudouridine synthase A (EC 5.4.99.12) (tRNA pseudouridine(38-40) synthase) (tRNA pseudouridylate synthase I) (tRNA-uridine isomerase I) 423 47,502 Active site (1); Alternative sequence (3); Binding site (1); Chain (1); Erroneous initiation (1); Frameshift (1); Modified residue (3); Sequence conflict (3); Transit peptide (1) FUNCTION: Converts specific uridines to PSI in a number of tRNA substrates. Acts on positions 27/28 in the anticodon stem and also positions 34 and 36 in the anticodon of an intron containing tRNA (PubMed:10094309). Involved in regulation of nuclear receptor activity possibly through pseudouridylation of SRA1 RNA (PubMed:15327771). Isoforms 3 and 4 do not form pseudouridine when expressed in vitro (PubMed:11085940). {ECO:0000269|PubMed:10094309, ECO:0000269|PubMed:11085940, ECO:0000269|PubMed:15327771}. SUBCELLULAR LOCATION: Isoform 1: Mitochondrion {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 2: Nucleus {ECO:0000250}. SUBUNIT: Monomer (By similarity). Forms a complex with RARG and the SRA1 RNA in the nucleus (PubMed:15327771). {ECO:0000250|UniProtKB:Q9Y606, ECO:0000269|PubMed:15327771}. +Q9Z273 TULP1_MOUSE Tubby-related protein 1 (Tubby-like protein 1) 543 60,336 Chain (1); Compositional bias (3) FUNCTION: Required for normal development of photoreceptor synapses. Required for normal photoreceptor function and for long-term survival of photoreceptor cells. Interacts with cytoskeleton proteins and may play a role in protein transport in photoreceptor cells. Binds lipids, especially phosphatidylinositol 3-phosphate, phosphatidylinositol 4-phosphate, phosphatidylinositol 5-phosphate, phosphatidylinositol 3,4-bisphosphate, phosphatidylinositol 4,5-bisphosphate, phosphatidylinositol 3,4,5-bisphosphate, phosphatidylserine and phosphatidic acid (in vitro) (By similarity). Contribute to stimulation of phagocytosis of apoptotic retinal pigment epithelium (RPE) cells and macrophages. {ECO:0000250, ECO:0000269|PubMed:11481257, ECO:0000269|PubMed:17525220, ECO:0000269|PubMed:19218615, ECO:0000269|PubMed:19837063}. SUBCELLULAR LOCATION: Cytoplasm. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Secreted. Cell junction, synapse. Note=Detected at synapses between photoreceptor cells and second-order neurons. Does not have a cleavable signal peptide and is secreted by an alternative pathway. SUBUNIT: Homodimer (Probable). May interact with ABCF1, PSIP1, ZEB1 and HMGB2 (Potential). Interacts with F-actin (By similarity). Interacts with DNM1. Interacts with TUB. Interacts with TYRO3. {ECO:0000250, ECO:0000269|PubMed:17525220, ECO:0000269|PubMed:19718693, ECO:0000269|PubMed:19837063, ECO:0000269|PubMed:20978472, ECO:0000305}. TISSUE SPECIFICITY: Retina specific. Detected in the outer plexiform layer in photoreceptor cells (at protein level). {ECO:0000269|PubMed:19218615}. +P06323 TVA3_MOUSE T-cell receptor alpha chain V region CTL-F3 132 14,747 Chain (1); Disulfide bond (1); Glycosylation (1); Non-terminal residue (1); Region (2); Signal peptide (1) +P04214 TVB6_MOUSE T-cell receptor beta chain V region E1 136 15,538 Beta strand (12); Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (3); Signal peptide (1) +P06320 TVB7_MOUSE T-cell receptor beta chain V region CTL-F3 134 14,946 Chain (1); Disulfide bond (1); Glycosylation (1); Non-terminal residue (1); Region (3); Signal peptide (1) +P01735 TVB86_MOUSE T-cell receptor beta chain V region 86T1 133 14,986 Chain (1); Disulfide bond (1); Glycosylation (2); Non-terminal residue (1); Region (2); Signal peptide (1) +P01740 TVC1_MOUSE T-cell receptor gamma chain V region V108A 135 15,930 Chain (1); Non-terminal residue (1); Region (2); Signal peptide (1) +P03978 TVC2_MOUSE T-cell receptor gamma chain V region V108B (Fragment) 115 13,496 Chain (1); Non-terminal residue (1); Region (1); Signal peptide (1) +P04212 TVB4_MOUSE T-cell receptor beta chain V region LB2 136 15,369 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (3); Signal peptide (1) +Q99MV2 TX19A_MOUSE Testis-expressed protein 19.1 (mTex19.1) (Testis-expressed protein 19A) 351 40,401 Chain (1); Mutagenesis (1); Region (2); Sequence conflict (5) FUNCTION: Required during spermatogenesis and placenta development, participating in the repression of retrotransposable elements and preventing their mobilization (PubMed:18802469, PubMed:21103378, PubMed:23364048, PubMed:23674551, PubMed:28254886). With its paralog, Tex19.2, collaborates with the Piwi-interacting RNA (piRNA) pathway, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins. Interacts with Piwi proteins and directly binds piRNAs, a class of 24 to 30 nucleotide RNAs that are generated by a Dicer-independent mechanism and are primarily derived from transposons and other repeated sequence elements (PubMed:28254886). Also during spermatogenesis, promotes, with UBR2, SPO11-dependent meiotic recombination (PubMed:28708824). Interacts with LINE-1 retrotransposon encoded LIRE1, stimulates LIRE1 polyubiquitination, mediated by UBR2, and degradation, inhibiting LINE-1 retranstoposon mobilization (PubMed:28806172). {ECO:0000269|PubMed:18802469, ECO:0000269|PubMed:21103378, ECO:0000269|PubMed:23364048, ECO:0000269|PubMed:23674551, ECO:0000269|PubMed:28254886, ECO:0000269|PubMed:28708824, ECO:0000269|PubMed:28806172}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18802469}. Note=Was initially reported to localize in the nucleus (PubMed:18096721). However, it was later shown to localize in cytoplasm only (PubMed:18802469). Cytoplasmic localization is distinct from the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis (PubMed:18802469). {ECO:0000269|PubMed:18096721, ECO:0000269|PubMed:18802469}. SUBUNIT: Interacts with UBR2; does not lead to Tex19.1 degradation and stabilizes it (PubMed:21103378). Interacts with piRNA-associated proteins DDX4, EDC4, MAEL, PIWIL1, PIWIL2, RANBP9 and TDRD6 (PubMed:28254886). Interacts with L1RE1 (PubMed:28806172). {ECO:0000269|PubMed:21103378, ECO:0000269|PubMed:28254886, ECO:0000269|PubMed:28806172}. TISSUE SPECIFICITY: Expressed in testis, placenta and ovary. Expressed in pluripotent stem cells. In testis, expression is highest in mitotic spermatogonia, decreases as spermatocytes progress through meiosis, and is present at low levels in round spermatids (at protein level). {ECO:0000269|PubMed:18096721, ECO:0000269|PubMed:18802469, ECO:0000269|PubMed:22447323, ECO:0000269|PubMed:28254886}. +Q8K2W3 TXD11_MOUSE Thioredoxin domain-containing protein 11 948 105,959 Alternative sequence (2); Chain (1); Coiled coil (1); Disulfide bond (2); Domain (2); Erroneous initiation (1); Modified residue (1); Transmembrane (1) TRANSMEM 61 81 Helical. {ECO:0000255}. FUNCTION: May act as a redox regulator involved in DUOX proteins folding. The interaction with DUOX1 and DUOX2 suggest that it belongs to a multiprotein complex constituting the thyroid H(2)O(2) generating system. It is however not sufficient to assist DUOX1 and DUOX2 in H(2)O(2) generation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with the cytoplasmic part of DUOX1 and DUOX2. Interacts with TPO and CYBA (By similarity). {ECO:0000250}. +P63044 VAMP2_MOUSE Vesicle-associated membrane protein 2 (VAMP-2) (Synaptobrevin-2) 116 12,691 Chain (1); Domain (1); Initiator methionine (1); Modified residue (1); Region (1); Site (2); Topological domain (2); Transmembrane (1) TRANSMEM 95 114 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 2 94 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 115 116 Vesicular. {ECO:0000255}. FUNCTION: Involved in the targeting and/or fusion of transport vesicles to their target membrane (PubMed:9430681). Modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1 (By similarity). {ECO:0000250|UniProtKB:P63045, ECO:0000269|PubMed:9430681}. PTM: Phosphorylated by PRKCZ in vitro and this phosphorylation is increased in the presence of WDFY2. {ECO:0000250|UniProtKB:P63027}.; PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type B (BoNT/B, botB); 20 hours after treatment of spinal cord cells almost all the protein has been digested (PubMed:10413679). BoNT/B hydrolyzes the 76-Gln-|-Phe-77 bond and inhibits neurotransmitter release (Probable). {ECO:0000269|PubMed:10413679, ECO:0000305|PubMed:10413679}.; PTM: (Microbial infection) Targeted and hydrolyzed by C.tetani toxin (tetX); 20 hours after treatment of spinal cord cells almost all the protein has been digested (PubMed:10413679). Tetanus toxin hydrolyzes the 76-Gln-|-Phe-77 bond and inhibits neurotransmitter release (Probable). {ECO:0000269|PubMed:10413679, ECO:0000305|PubMed:10413679}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Single-pass type IV membrane protein. Cell junction, synapse, synaptosome. Cell membrane {ECO:0000250|UniProtKB:P63045}. Note=Neuronal synaptic vesicles. Colocalizes with PRKCZ and WDFY2 in intracellular vesicles. {ECO:0000250|UniProtKB:P63027}. SUBUNIT: Interacts (via N-terminus) with KCNB1 (via N-terminus and C-terminus); stimulates the channel inactivation rate of KCNB1 (By similarity). Part of the SNARE core complex containing SNAP25, VAMP2 and STX1A (PubMed:19196426). This complex binds to CPLX1. Interacts with VAPA and VAPB (By similarity). Interacts with BVES and STX4. Interacts with WDFY2, PRKCZ and PRKCI (PubMed:17313651). Forms a complex with WDFY2 and PRKCZ (PubMed:17313651). Interacts with SEPT8; the interaction inhibits interaction of VAMP2 with SYP (PubMed:19196426). Interacts with SYP; the interaction is inhibit by interaction with SEPT8 (PubMed:19196426). {ECO:0000250|UniProtKB:P63045, ECO:0000269|PubMed:17313651, ECO:0000269|PubMed:17548353, ECO:0000269|PubMed:19196426, ECO:0000269|PubMed:20057356}. +P62814 VATB2_MOUSE V-type proton ATPase subunit B, brain isoform (V-ATPase subunit B 2) (Endomembrane proton pump 58 kDa subunit) (Vacuolar proton pump subunit B 2) 511 56,551 Chain (1); Erroneous initiation (3); Sequence conflict (18) FUNCTION: Non-catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. SUBCELLULAR LOCATION: Endomembrane system; Peripheral membrane protein. Melanosome {ECO:0000250}. Note=Endomembrane. SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (main components: subunits A, B, C, D, E, and F) attached to an integral membrane V0 proton pore complex (main component: the proteolipid protein). TISSUE SPECIFICITY: Mainly expressed in the organ of Corti and spiral ganglion neurons, in both the early postnatal cochlea (P2) and the adult cochlea (P30). {ECO:0000269|PubMed:24913193}. +Q9Z1G3 VATC1_MOUSE V-type proton ATPase subunit C 1 (V-ATPase subunit C 1) (Vacuolar proton pump subunit C 1) 382 43,888 Chain (1); Initiator methionine (1); Modified residue (1); Sequence conflict (1) FUNCTION: Subunit of the peripheral V1 complex of vacuolar ATPase. Subunit C is necessary for the assembly of the catalytic sector of the enzyme and is likely to have a specific function in its catalytic activity. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'' and d). TISSUE SPECIFICITY: Ubiquitous. Abundant in brain, liver, kidney and testis. {ECO:0000269|PubMed:12527205}. +Q60932 VDAC1_MOUSE Voltage-dependent anion-selective channel protein 1 (VDAC-1) (mVDAC1) (Outer mitochondrial membrane protein porin 1) (Plasmalemmal porin) (Voltage-dependent anion-selective channel protein 5) (VDAC-5) (mVDAC5) 296 32,351 Alternative sequence (1); Beta strand (20); Chain (1); Cross-link (5); Helix (2); Initiator methionine (1); Modified residue (12); Nucleotide binding (2); Site (1); Transmembrane (19); Turn (6) TRANSMEM 39 46 Beta stranded. {ECO:0000269|PubMed:18988731}.; TRANSMEM 52 61 Beta stranded. {ECO:0000269|PubMed:18988731}.; TRANSMEM 67 77 Beta stranded. {ECO:0000269|PubMed:18988731}.; TRANSMEM 82 89 Beta stranded. {ECO:0000269|PubMed:18988731}.; TRANSMEM 93 101 Beta stranded. {ECO:0000269|PubMed:18988731}.; TRANSMEM 108 117 Beta stranded. {ECO:0000269|PubMed:18988731}.; TRANSMEM 123 132 Beta stranded. {ECO:0000269|PubMed:18988731}.; TRANSMEM 136 145 Beta stranded. {ECO:0000269|PubMed:18988731}.; TRANSMEM 149 158 Beta stranded. {ECO:0000269|PubMed:18988731}.; TRANSMEM 162 171 Beta stranded. {ECO:0000269|PubMed:18988731}.; TRANSMEM 178 188 Beta stranded. {ECO:0000269|PubMed:18988731}.; TRANSMEM 191 198 Beta stranded. {ECO:0000269|PubMed:18988731}.; TRANSMEM 202 211 Beta stranded. {ECO:0000269|PubMed:18988731}.; TRANSMEM 215 223 Beta stranded. {ECO:0000269|PubMed:18988731}.; TRANSMEM 230 239 Beta stranded. {ECO:0000269|PubMed:18988731}.; TRANSMEM 244 251 Beta stranded. {ECO:0000269|PubMed:18988731}.; TRANSMEM 255 264 Beta stranded. {ECO:0000269|PubMed:18988731}.; TRANSMEM 268 276 Beta stranded. {ECO:0000269|PubMed:18988731}.; TRANSMEM 286 296 Beta stranded. {ECO:0000269|PubMed:18988731}. FUNCTION: Forms a channel through the mitochondrial outer membrane and also the plasma membrane. The channel at the outer mitochondrial membrane allows diffusion of small hydrophilic molecules; in the plasma membrane it is involved in cell volume regulation and apoptosis. It adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The open state has a weak anion selectivity whereas the closed state is cation-selective. May participate in the formation of the permeability transition pore complex (PTPC) responsible for the release of mitochondrial products that triggers apoptosis. {ECO:0000269|PubMed:10716730, ECO:0000269|PubMed:15477379, ECO:0000269|PubMed:18988731}. PTM: Phosphorylation at Ser-206 by NEK1 promotes the open conformational state preventing excessive mitochondrial membrane permeability and subsequent apoptotic cell death after injury. Phosphorylation by the AKT-GSK3B axis stabilizes the protein probably by preventing ubiquitin-mediated proteasomal degradation. {ECO:0000250|UniProtKB:P21796}.; PTM: Ubiquitinated by PRKN during mitophagy, leading to its degradation and enhancement of mitophagy. Deubiquitinated by USP30. {ECO:0000250|UniProtKB:P21796}. SUBCELLULAR LOCATION: Isoform Mt-VDAC1: Mitochondrion outer membrane {ECO:0000269|PubMed:10716730}; Multi-pass membrane protein {ECO:0000269|PubMed:18988731}.; SUBCELLULAR LOCATION: Isoform Pl-VDAC1: Cell membrane {ECO:0000269|PubMed:10716730}; Multi-pass membrane protein {ECO:0000269|PubMed:18988731}. Membrane raft {ECO:0000269|PubMed:25168729}; Multi-pass membrane protein {ECO:0000269|PubMed:18988731}. SUBUNIT: Interacts with hexokinases including HK1. The HK1-VDAC1 complex interacts with ATF2. Interacts with BCL2L1. Interacts with BAK1. Interacts with RTL10/BOP (via BH3 domain) (By similarity). Interacts with amyloid-beta and APP; induces VDAC1 dephosphorylation (PubMed:25168729). Component of the mitochondrial permeability transition pore complex (mPTPC), at least composed of SPG7, VDAC1 and PPIF. Interacts with SPG7, NIPSNAP2 and SLC25A30 (By similarity). {ECO:0000250|UniProtKB:P21796, ECO:0000269|PubMed:25168729}. DOMAIN: Consists mainly of a membrane-spanning beta-barrel formed by 19 beta-strands. The helical N-terminus folds back into the pore opening and plays a role in voltage-gated channel activity (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: High levels of expression detected in heart, kidney, brain, and skeletal muscle. Not expressed in testis. {ECO:0000269|PubMed:8660977}. +P49766 VEGFB_MOUSE Vascular endothelial growth factor B (VEGF-B) (VEGF-related factor) (VRF) 207 21,914 Alternative sequence (1); Chain (1); Disulfide bond (5); Sequence conflict (1); Signal peptide (1) FUNCTION: Growth factor for endothelial cells. VEGF-B167 binds heparin and neuropilin-1 whereas the binding to neuropilin-1 of VEGF-B186 is regulated by proteolysis. VEGF-B seems to be required for normal heart function in adult but is not required for proper development of the cardiovascular system either during development or for angiogenesis in adults. {ECO:0000269|PubMed:11457758}. PTM: VEGF-B186 is O-glycosylated. SUBCELLULAR LOCATION: Secreted. Note=Secreted but remains associated to cells or to the extracellular matrix unless released by heparin. SUBUNIT: Homodimer; disulfide-linked. Can also form heterodimer with VEGF. TISSUE SPECIFICITY: Abundantly expressed in heart, brain, kidney and skeletal muscle. +Q8BLE7 VGLU2_MOUSE Vesicular glutamate transporter 2 (VGluT2) (Differentiation-associated BNPI) (Differentiation-associated Na(+)-dependent inorganic phosphate cotransporter) (Solute carrier family 17 member 6) 582 64,561 Chain (1); Glycosylation (3); Topological domain (13); Transmembrane (12) TRANSMEM 72 92 Helical. {ECO:0000255}.; TRANSMEM 126 146 Helical. {ECO:0000255}.; TRANSMEM 149 169 Helical. {ECO:0000255}.; TRANSMEM 178 198 Helical. {ECO:0000255}.; TRANSMEM 217 237 Helical. {ECO:0000255}.; TRANSMEM 245 265 Helical. {ECO:0000255}.; TRANSMEM 311 331 Helical. {ECO:0000255}.; TRANSMEM 350 370 Helical. {ECO:0000255}.; TRANSMEM 387 407 Helical. {ECO:0000255}.; TRANSMEM 410 430 Helical. {ECO:0000255}.; TRANSMEM 444 464 Helical. {ECO:0000255}.; TRANSMEM 478 498 Helical. {ECO:0000255}. TOPO_DOM 1 71 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 93 125 Vesicular. {ECO:0000255}.; TOPO_DOM 147 148 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 170 177 Vesicular. {ECO:0000255}.; TOPO_DOM 199 216 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 238 244 Vesicular. {ECO:0000255}.; TOPO_DOM 266 310 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 332 349 Vesicular. {ECO:0000255}.; TOPO_DOM 371 386 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 408 409 Vesicular. {ECO:0000255}.; TOPO_DOM 431 443 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 465 477 Vesicular. {ECO:0000255}.; TOPO_DOM 499 582 Cytoplasmic. {ECO:0000255}. FUNCTION: Mediates the uptake of glutamate into synaptic vesicles at presynaptic nerve terminals of excitatory neural cells. May also mediate the transport of inorganic phosphate. {ECO:0000269|PubMed:11432869, ECO:0000269|PubMed:15103023, ECO:0000269|PubMed:15118123, ECO:0000269|PubMed:17108179}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:16942593}. Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cell junction, synapse, synaptosome {ECO:0000269|PubMed:16942593}. TISSUE SPECIFICITY: Expressed in brain. Expressed in hippocampal neurons (at protein level). {ECO:0000269|PubMed:11432869, ECO:0000269|PubMed:15103023, ECO:0000269|PubMed:15118123, ECO:0000269|PubMed:16942593}. +P35917 VGFR3_MOUSE Vascular endothelial growth factor receptor 3 (VEGFR-3) (EC 2.7.10.1) (Fms-like tyrosine kinase 4) (FLT-4) (Tyrosine-protein kinase receptor FLT4) 1363 153,016 Active site (1); Binding site (1); Chain (1); Disulfide bond (7); Domain (8); Glycosylation (13); Modified residue (10); Nucleotide binding (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 776 796 Helical. {ECO:0000255}. TOPO_DOM 25 775 Extracellular. {ECO:0000255}.; TOPO_DOM 797 1363 Cytoplasmic. {ECO:0000255}. FUNCTION: Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFC and VEGFD, and plays an essential role in adult lymphangiogenesis and in the development of the vascular network and the cardiovascular system during embryonic development. Promotes proliferation, survival and migration of endothelial cells, and regulates angiogenic sprouting. Signaling by activated FLT4 leads to enhanced production of VEGFC, and to a lesser degree VEGFA, thereby creating a positive feedback loop that enhances FLT4 signaling. Modulates KDR signaling by forming heterodimers. Mediates activation of the MAPK1/ERK2, MAPK3/ERK1 signaling pathway, of MAPK8 and the JUN signaling pathway, and of the AKT1 signaling pathway. Phosphorylates SHC1. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase. Promotes phosphorylation of MAPK8 at 'Thr-183' and 'Tyr-185', and of AKT1 at 'Ser-473'. {ECO:0000269|PubMed:18594512, ECO:0000269|PubMed:20445537, ECO:0000269|PubMed:20697430, ECO:0000269|PubMed:21481239, ECO:0000269|PubMed:21909098, ECO:0000269|PubMed:9794766}. PTM: Autophosphorylated on tyrosine residues upon ligand binding. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Phosphorylation in response to H(2)O(2) is mediated by a process that requires SRC and PRKCD activity. Phosphorylation at Tyr-1068 is required for autophosphorylation at additional tyrosine residues. Phosphorylation at Tyr-1063 and Tyr-1337 is important for interaction with CRK and subsequent activation of MAPK8. Phosphorylation at Tyr-1230, Tyr-1231 and Tyr-1337 is important for interaction with GRB2 and subsequent activation of the AKT1 and MAPK1/ERK2 and/or MAPK3/ERK1 signaling pathways. In response to endothelial cell adhesion onto collagen, can also be phosphorylated in the absence of FLT4 kinase activity by SRC (By similarity). {ECO:0000250|UniProtKB:P35916}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20445537}; Single-pass type I membrane protein {ECO:0000269|PubMed:20445537}. Cytoplasm {ECO:0000269|PubMed:20445537}. Nucleus {ECO:0000269|PubMed:20445537}. Note=Ligand-mediated autophosphorylation leads to rapid internalization. SUBUNIT: Interacts with VEGFC and VEGFD. Monomer in the absence of bound VEGFC or VEGFD. Homodimer in the presence of bound VEGFC or VEGFD. Can also form a heterodimer with KDR. Interacts with PTPN14; the interaction is enhanced by stimulation with VEGFC. Interacts with CRK, GRB2, PTK2/FAK1, SHC1, PIK3R1 and PTPN11/SHP-2. Identified in a complex with SRC and ITGB1 (By similarity). {ECO:0000250|UniProtKB:P35916}. DOMAIN: The first and second Ig-like C2-type (immunoglobulin-like) domains are sufficient for VEGFC binding. The fourth and fifth Ig-like C2-type (immunoglobulin-like) domains are sufficient for homodimerization. The fifth and seventh Ig-like C2-type (immunoglobulin-like) domains are required for autophosphorylation and further activation. {ECO:0000250|UniProtKB:P35916}. TISSUE SPECIFICITY: Expressed in adult lung and liver, and in fetal liver, brain, intestine and placenta. {ECO:0000269|PubMed:18594512}. +P97751 VIPR1_MOUSE Vasoactive intestinal polypeptide receptor 1 (VIP-R-1) (Pituitary adenylate cyclase-activating polypeptide type II receptor) (PACAP type II receptor) (PACAP-R-2) (PACAP-R2) (VPAC1) 459 52,096 Chain (1); Disulfide bond (4); Glycosylation (5); Sequence conflict (1); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 144 168 Helical; Name=1. {ECO:0000255}.; TRANSMEM 176 195 Helical; Name=2. {ECO:0000255}.; TRANSMEM 218 241 Helical; Name=3. {ECO:0000255}.; TRANSMEM 256 277 Helical; Name=4. {ECO:0000255}.; TRANSMEM 295 318 Helical; Name=5. {ECO:0000255}.; TRANSMEM 344 363 Helical; Name=6. {ECO:0000255}.; TRANSMEM 376 395 Helical; Name=7. {ECO:0000255}. TOPO_DOM 31 143 Extracellular. {ECO:0000255}.; TOPO_DOM 169 175 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 196 217 Extracellular. {ECO:0000255}.; TOPO_DOM 242 255 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 278 294 Extracellular. {ECO:0000255}.; TOPO_DOM 319 343 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 364 375 Extracellular. {ECO:0000255}.; TOPO_DOM 396 459 Cytoplasmic. {ECO:0000255}. FUNCTION: This is a receptor for VIP. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q91YD6 VILL_MOUSE Villin-like protein (EF-6) 859 96,509 Alternative sequence (3); Chain (1); Domain (1); Repeat (6); Sequence conflict (12) FUNCTION: Possible tumor suppressor. {ECO:0000250|UniProtKB:O15195}. +P20152 VIME_MOUSE Vimentin 466 53,688 Chain (1); Coiled coil (3); Cross-link (12); Domain (1); Glycosylation (3); Initiator methionine (1); Modified residue (57); Motif (1); Region (7); Sequence conflict (6); Site (1) FUNCTION: Vimentins are class-III intermediate filaments found in various non-epithelial cells, especially mesenchymal cells. Vimentin is attached to the nucleus, endoplasmic reticulum, and mitochondria, either laterally or terminally.; FUNCTION: Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2. {ECO:0000250}. PTM: Phosphorylation by PKN1 inhibits the formation of filaments. Filament disassembly during mitosis is promoted by phosphorylation at Ser-55 as well as by nestin. One of the most prominent phosphoproteins in various cells of mesenchymal origin. Phosphorylation is enhanced during cell division, at which time vimentin filaments are significantly reorganized. Phosphorylated at Ser-56 by CDK5 during neutrophil secretion in the cytoplasm. Phosphorylated by STK33. Phosphorylated on tyrosine residues by SRMS. {ECO:0000250|UniProtKB:P08670, ECO:0000250|UniProtKB:P31000}.; PTM: S-nitrosylation is induced by interferon-gamma and oxidatively-modified low-densitity lipoprotein (LDL(ox)) possibly implicating the iNOS-S100A8/9 transnitrosylase complex. {ECO:0000250|UniProtKB:P08670}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P08670}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P08670}. Nucleus matrix {ECO:0000250|UniProtKB:P31000}. SUBUNIT: Interacts with BCAS3 (By similarity). Homopolymer assembled from elementary dimers. Interacts with LGSN (PubMed:18178558). Interacts with SYNM (PubMed:17356066). Interacts (via rod region) with PLEC (via CH 1 domain) (PubMed:15128297). Interacts with SLC6A4. Interacts with STK33. Interacts with LARP6. Interacts with RAB8B. Interacts with TOR1A; the interaction associates TOR1A with the cytoskeleton. Interacts with TOR1AIP1. Interacts with DIAPH1 (By similarity). Identified in complexes that contain VIM, EZR, AHNAK, BFSP1, BFSP2, ANK2, PLEC, PRX and spectrin (PubMed:21745462). Interacts with EPPK1; interaction is dependent of higher-order structure of intermediate filament (By similarity). Interacts with the non-receptor tyrosine kinase SRMS; the interaction leads to phosphorylation of VIM (By similarity). Interacts with NOD2 (By similarity). Interacts (via head region) with CORO1C (PubMed:27178841). {ECO:0000250|UniProtKB:P08670, ECO:0000250|UniProtKB:P31000, ECO:0000269|PubMed:15128297, ECO:0000269|PubMed:17356066, ECO:0000269|PubMed:18178558, ECO:0000269|PubMed:18827015, ECO:0000269|PubMed:21745462, ECO:0000269|PubMed:27178841}. DOMAIN: The central alpha-helical coiled-coil IF rod domain mediates elementary homodimerization. {ECO:0000250}.; DOMAIN: The [IL]-x-C-x-x-[DE] motif is a proposed target motif for cysteine S-nitrosylation mediated by the iNOS-S100A8/A9 transnitrosylase complex. {ECO:0000250|UniProtKB:P08670}. TISSUE SPECIFICITY: Detected in eye lens fiber cells (at protein level). {ECO:0000269|PubMed:21745462}. +Q8BP01 VMAC_MOUSE Vimentin-type intermediate filament-associated coiled-coil protein 174 19,017 Chain (1); Coiled coil (1) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Colocalizes with vimentin-type intermediate filaments. {ECO:0000250}. +Q99KU0 VMP1_MOUSE Vacuole membrane protein 1 (NF-E2-inducible protein 2) (Protein ni-2) (Transmembrane protein 49) 406 45,960 Chain (1); Initiator methionine (1); Modified residue (1); Region (1); Sequence conflict (4); Topological domain (7); Transmembrane (6) TRANSMEM 78 98 Helical. {ECO:0000255}.; TRANSMEM 110 130 Helical. {ECO:0000255}.; TRANSMEM 251 271 Helical. {ECO:0000255}.; TRANSMEM 274 294 Helical. {ECO:0000255}.; TRANSMEM 306 326 Helical. {ECO:0000255}.; TRANSMEM 364 384 Helical. {ECO:0000255}. TOPO_DOM 2 77 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 99 109 Extracellular. {ECO:0000255}.; TOPO_DOM 131 250 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 272 273 Extracellular. {ECO:0000255}.; TOPO_DOM 295 305 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 327 363 Extracellular. {ECO:0000255}.; TOPO_DOM 385 406 Cytoplasmic. {ECO:0000255}. FUNCTION: Stress-induced protein that, when overexpressed, promotes formation of intracellular vacuoles followed by cell death (By similarity). May be involved in the cytoplasmic vacuolization of acinar cells during the early stage of acute pancreatitis (PubMed:17940279). Involved in cell-cell adhesion. Plays an essential role in formation of cell junctions. Plays a role in the initial stages of the autophagic process through its interaction with BECN1. Required for autophagosome formation (By similarity). {ECO:0000250|UniProtKB:Q91ZQ0, ECO:0000250|UniProtKB:Q96GC9, ECO:0000269|PubMed:17940279}. SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q91ZQ0}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q96GC9}; Multi-pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000250|UniProtKB:Q91ZQ0}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q96GC9}. SUBUNIT: Interacts with BECN1 (By similarity). Interacts with TJP1 (By similarity). Interacts with TP53INP2 (By similarity). Interacts with TMEM41B (By similarity). {ECO:0000250|UniProtKB:Q91ZQ0, ECO:0000250|UniProtKB:Q96GC9}. DOMAIN: The VTT domain was previously called the SNARE-assoc domain. As there is no evidence that this domain associates with SNARE proteins, it was renamed as VMP1, TMEM41, and TVP38 (VTT) domain. {ECO:0000250|UniProtKB:Q96GC9}. +Q8R0J7 VP37B_MOUSE Vacuolar protein sorting-associated protein 37B (Vps37B) (ESCRT-I complex subunit VPS37B) 285 31,056 Chain (1); Compositional bias (1); Domain (1); Region (1); Sequence conflict (2) FUNCTION: Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies. May be involved in cell growth and differentiation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Recruited to the endosomal membrane in a VPS4A-dependent fashion. {ECO:0000250}. SUBUNIT: Component of the ESCRT-I complex (endosomal sorting complex required for transport I) which consists of TSG101, VPS28, a VPS37 protein (VPS37A to -D) and MVB12A or MVB12B in a 1:1:1:1 stoichiometry. Interacts with TSG101, VPS28, MVB12A and MVB12B. Component of the ESCRT-I complex (endosomal sorting complex required for transport I) which consists of TSG101, VPS28, a VPS37 protein (VPS37A to -D) and UBAP1 in a 1:1:1:1 stoichiometry. Interacts with CEP55. Interacts with IST1 (By similarity). {ECO:0000250}. +P15920 VPP2_MOUSE V-type proton ATPase 116 kDa subunit a isoform 2 (V-ATPase 116 kDa isoform a2) (Immune suppressor factor J6B7) (ISF) (Lysosomal H(+)-transporting ATPase V0 subunit a2) (ShIF) (Vacuolar proton translocating ATPase 116 kDa subunit a isoform 2) 856 98,145 Alternative sequence (1); Chain (1); Erroneous initiation (1); Helix (1); Modified residue (2); Sequence conflict (4); Topological domain (9); Transmembrane (8) TRANSMEM 394 412 Helical. {ECO:0000255}.; TRANSMEM 415 431 Helical. {ECO:0000255}.; TRANSMEM 446 475 Helical. {ECO:0000255}.; TRANSMEM 550 569 Helical. {ECO:0000255}.; TRANSMEM 588 608 Helical. {ECO:0000255}.; TRANSMEM 652 671 Helical. {ECO:0000255}.; TRANSMEM 740 764 Helical. {ECO:0000255}.; TRANSMEM 786 824 Helical. {ECO:0000255}. TOPO_DOM 1 393 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 413 414 Vacuolar. {ECO:0000255}.; TOPO_DOM 432 445 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 476 549 Vacuolar. {ECO:0000255}.; TOPO_DOM 570 587 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 609 651 Vacuolar. {ECO:0000255}.; TOPO_DOM 672 739 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 765 785 Vacuolar. {ECO:0000255}.; TOPO_DOM 825 856 Cytoplasmic. {ECO:0000255}. FUNCTION: Part of the proton channel of V-ATPases (By similarity). Essential component of the endosomal pH-sensing machinery. May play a role in maintaining the Golgi functions, such as glycosylation maturation, by controlling the Golgi pH. In aerobic conditions, involved in intracellular iron homeostasis, thus triggering the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent proteasomal degradation (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9Y487, ECO:0000269|PubMed:16415858}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16415858}; Multi-pass membrane protein {ECO:0000269|PubMed:16415858}. Endosome membrane {ECO:0000269|PubMed:16415858}. Note=In kidney proximal tubules, detected in subapical early endosomes. SUBUNIT: The V-ATPase is a heteromultimeric enzyme composed of at least thirteen different subunits. It has a membrane peripheral V1 sector for ATP hydrolysis and an integral V0 for proton translocation. The V1 sector comprises subunits A-H, whereas V0 includes subunits a, d, c, c', and c''. Directly interacts with PSCD2 through its N-terminal cytosolic tail in an intra-endosomal acidification-dependent manner (PubMed:16415858). Disruption of this interaction results in the inhibition of endocytosis (PubMed:16415858). Interacts with SPAAR (By similarity). {ECO:0000250|UniProtKB:Q9Y487, ECO:0000269|PubMed:16415858}. TISSUE SPECIFICITY: Relatively high expression in kidney and liver. Lower levels in the spleen, testis, and skeletal muscle. Also expressed in the thymus. {ECO:0000269|PubMed:11375395}. +Q6PDS0 VTM2L_MOUSE V-set and transmembrane domain-containing protein 2-like protein 220 23,723 Chain (1); Disulfide bond (1); Domain (1); Signal peptide (1) +P35918 VGFR2_MOUSE Vascular endothelial growth factor receptor 2 (VEGFR-2) (EC 2.7.10.1) (Fetal liver kinase 1) (FLK-1) (Kinase NYK) (Protein-tyrosine kinase receptor flk-1) (CD antigen CD309) 1367 152,517 Active site (1); Alternative sequence (2); Binding site (1); Chain (1); Disulfide bond (7); Domain (8); Glycosylation (17); Modified residue (15); Mutagenesis (5); Nucleotide binding (1); Sequence conflict (5); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 763 783 Helical. {ECO:0000255}. TOPO_DOM 20 762 Extracellular. {ECO:0000255}.; TOPO_DOM 784 1367 Cytoplasmic. {ECO:0000255}. FUNCTION: Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFA, VEGFC and VEGFD. Plays an essential role in the regulation of angiogenesis, vascular development, vascular permeability, and embryonic hematopoiesis. Promotes proliferation, survival, migration and differentiation of endothelial cells. Promotes reorganization of the actin cytoskeleton. Isoforms lacking a transmembrane domain, such as isoform 2, may function as decoy receptors for VEGFA, VEGFC and/or VEGFD. Isoform 2 plays an important role as a negative regulator of VEGFA- and VEGFC-mediated lymphangiogenesis by limiting the amount of free VEGFA and/or VEGFC and by preventing their binding to FLT4. Modulates FLT1 and FLT4 signaling by forming heterodimers. Binding of vascular growth factors to isoform 1 leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate and the activation of protein kinase C. Mediates activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, reorganization of the actin cytoskeleton and activation of PTK2/FAK1. Required for VEGFA-mediated induction of NOS2 and NOS3, leading to the production of the signaling molecule nitric oxide (NO) by endothelial cells. Phosphorylates PLCG1. Promotes phosphorylation of FYN, NCK1, NOS3, PIK3R1, PTK2/FAK1 and SRC. {ECO:0000269|PubMed:12023952, ECO:0000269|PubMed:15673613, ECO:0000269|PubMed:19635461, ECO:0000269|PubMed:19652084, ECO:0000269|PubMed:19668192, ECO:0000269|PubMed:20705758, ECO:0000269|PubMed:7596435, ECO:0000269|PubMed:8356051}. PTM: N-glycosylated. {ECO:0000250}.; PTM: Ubiquitinated. Tyrosine phosphorylation of the receptor promotes its poly-ubiquitination, leading to its degradation via the proteasome or lysosomal proteases (By similarity). {ECO:0000250}.; PTM: Autophosphorylated on tyrosine residues upon ligand binding. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Phosphorylation at Tyr-949 is important for interaction with SH2D2A/TSAD and VEGFA-mediated reorganization of the actin cytoskeleton. Phosphorylation at Tyr-1173 is important for interaction with PLCG1 and SHB. Phosphorylation at Tyr-1212 is important for interaction with NCK1 and FYN. Dephosphorylated by PTPRJ at Tyr-799, Tyr-949, Tyr-994, Tyr-1052, Tyr-1057, Tyr-1173 and Tyr-1212 (By similarity). {ECO:0000250}.; PTM: The inhibitory disulfide bond between Cys-1022 and Cys-1043 may serve as a specific molecular switch for H(2)S-induced modification that regulates VEGFR2 function. {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction {ECO:0000269|PubMed:15673613, ECO:0000269|PubMed:19635461, ECO:0000269|PubMed:19668192}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P35968}. Note=Colocalizes with ERN1 and XBP1 in the endoplasmic reticulum in endothelial cells in a vascular endothelial growth factor (VEGF)-dependent manner (By similarity). Localized with RAP1A at cell-cell junctions. {ECO:0000250|UniProtKB:P35968}.; SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I membrane protein. Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Early endosome {ECO:0000250}. Note=Detected on caveolae-enriched lipid rafts at the cell surface. Is recycled from the plasma membrane to endosomes and back again. Phosphorylation triggered by VEGFA binding promotes internalization and subsequent degradation. VEGFA binding triggers internalization and translocation to the nucleus (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 2: Secreted. SUBUNIT: Homodimer in the presence of bound dimeric VEGFA, VEGFC or VEGFD ligands; monomeric in the absence of bound ligands. Can also form heterodimers with FLT1/VEGFR1 and FLT4/VEGFR2. Interacts (tyrosine phosphorylated) with LFYN, NCK1, PLCG1. Interacts (tyrosine-phosphorylated active form preferentially) with DAB2IP (via C2 domain and active form preferentially); the interaction occurs at the late phase of VEGFA response and inhibits KDR/VEGFR2 activity. Interacts with SHBSH2D2A/TSAD, GRB2, MYOF, CBL and PDCD6 (PubMed:12796773, PubMed:12881528, PubMed:15026417, PubMed:15673613, PubMed:17702744, PubMed:19668192, PubMed:7681362, PubMed:8356051). Interacts (via C-terminus domain) with ERN1 (via kinase domain); the interaction is facilitated in a XBP1 isoform 1- and vascular endothelial growth factor (VEGF)-dependent manner in endothelial cells (By similarity). {ECO:0000250|UniProtKB:P35968, ECO:0000269|PubMed:12796773, ECO:0000269|PubMed:12881528, ECO:0000269|PubMed:15026417, ECO:0000269|PubMed:15673613, ECO:0000269|PubMed:17702744, ECO:0000269|PubMed:19668192, ECO:0000269|PubMed:7681362, ECO:0000269|PubMed:8356051}. DOMAIN: The second and third Ig-like C2-type (immunoglobulin-like) domains are sufficient for VEGFC binding. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in endothelial cells (at protein level). Detected in embryonic endothelial cells, as well as hematopoietic stem and progenitor cells. Detected in vascular endothelium. Expressed at high levels in adult heart, lung, kidney, brain and skeletal muscle, but is also expressed at lower levels in most other adult tissues. {ECO:0000269|PubMed:1717995, ECO:0000269|PubMed:19635461, ECO:0000269|PubMed:8356051, ECO:0000269|PubMed:8423988}. +Q8BFU8 VGLU3_MOUSE Vesicular glutamate transporter 3 (VGluT3) (Solute carrier family 17 member 8) 601 66,148 Chain (1); Compositional bias (1); Glycosylation (1); Topological domain (13); Transmembrane (12) TRANSMEM 90 110 Helical. {ECO:0000255}.; TRANSMEM 144 164 Helical. {ECO:0000255}.; TRANSMEM 167 187 Helical. {ECO:0000255}.; TRANSMEM 196 216 Helical. {ECO:0000255}.; TRANSMEM 235 255 Helical. {ECO:0000255}.; TRANSMEM 263 283 Helical. {ECO:0000255}.; TRANSMEM 328 348 Helical. {ECO:0000255}.; TRANSMEM 367 387 Helical. {ECO:0000255}.; TRANSMEM 404 424 Helical. {ECO:0000255}.; TRANSMEM 427 447 Helical. {ECO:0000255}.; TRANSMEM 461 481 Helical. {ECO:0000255}.; TRANSMEM 495 515 Helical. {ECO:0000255}. TOPO_DOM 1 89 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 111 143 Vesicular. {ECO:0000255}.; TOPO_DOM 165 166 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 188 195 Vesicular. {ECO:0000255}.; TOPO_DOM 217 234 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 256 262 Vesicular. {ECO:0000255}.; TOPO_DOM 284 327 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 349 366 Vesicular. {ECO:0000255}.; TOPO_DOM 388 403 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 425 426 Vesicular. {ECO:0000255}.; TOPO_DOM 448 460 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 482 494 Vesicular. {ECO:0000255}.; TOPO_DOM 516 598 Cytoplasmic. {ECO:0000255}. FUNCTION: Mediates the uptake of glutamate into synaptic vesicles at presynaptic nerve terminals of excitatory neural cells. May also mediate the transport of inorganic phosphate. {ECO:0000269|PubMed:12384506, ECO:0000269|PubMed:18080752, ECO:0000269|PubMed:18215623, ECO:0000269|PubMed:18278042}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q7TSF2}. Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cell junction, synapse, synaptosome {ECO:0000250|UniProtKB:Q7TSF2}. TISSUE SPECIFICITY: Expressed in restricted areas of the brain. Highest expression is found in the neurons of the basal forebrain, the hippocampal formation, and the majority of the neurons of the mesencephalic raphe nuclei. Expressed in inner hair cells of the ear. {ECO:0000269|PubMed:12384506, ECO:0000269|PubMed:18215623}. +Q99NC0 VGLL1_MOUSE Transcription cofactor vestigial-like protein 1 (Vgl-1) (Vestigial-related factor) 307 34,691 Beta strand (2); Chain (1); Helix (1) FUNCTION: May act as a specific coactivator for the mammalian TEFs. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with TEFs. {ECO:0000250}. +Q80V24 VGLL4_MOUSE Transcription cofactor vestigial-like protein 4 (Vgl-4) 287 30,999 Beta strand (1); Chain (1); Helix (4); Modified residue (2) FUNCTION: May act as a specific coactivator for the mammalian TEFs. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with TEFs. Interacts with IRF2BP2 (By similarity). {ECO:0000250}. +Q64727 VINC_MOUSE Vinculin (Metavinculin) 1066 116,717 Beta strand (1); Chain (1); Compositional bias (1); Helix (7); Modified residue (20); Region (8); Repeat (3); Sequence conflict (8); Turn (1) FUNCTION: Actin filament (F-actin)-binding protein involved in cell-matrix adhesion and cell-cell adhesion. Regulates cell-surface E-cadherin expression and potentiates mechanosensing by the E-cadherin complex. May also play important roles in cell morphology and locomotion (By similarity). {ECO:0000250|UniProtKB:P18206, ECO:0000269|PubMed:7568093}. PTM: Phosphorylated; on serines, threonines and tyrosines. Phosphorylation on Tyr-1065 in activated platelets affects head-tail interactions and cell spreading but has no effect on actin binding nor on localization to focal adhesion plaques (By similarity). {ECO:0000250|UniProtKB:P12003}.; PTM: Acetylated; mainly by myristic acid but also by a small amount of palmitic acid. {ECO:0000250|UniProtKB:P12003}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P12003}; Peripheral membrane protein {ECO:0000250|UniProtKB:P12003}; Cytoplasmic side {ECO:0000250|UniProtKB:P12003}. Cell junction, adherens junction {ECO:0000250|UniProtKB:P12003}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:P12003}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P85972}. Cell membrane, sarcolemma {ECO:0000269|PubMed:26359501}; Peripheral membrane protein {ECO:0000269|PubMed:26359501}; Cytoplasmic side {ECO:0000269|PubMed:26359501}. Note=Recruitment to cell-cell junctions occurs in a myosin II-dependent manner. Interaction with CTNNB1 is necessary for its localization to the cell-cell junctions. {ECO:0000250|UniProtKB:P12003}. SUBUNIT: Exhibits self-association properties. Interacts with APBB1IP, NRAP and TLN1. Interacts with SYNM. Interacts with CTNNB1 and this interaction is necessary for its localization to the cell-cell junctions and for its function in regulating cell surface expression of E-cadherin (By similarity). Interacts with SORBS1 (PubMed:10085297). Interacts with SYNM (By similarity). Interacts with CTNNA1 (By similarity). Binds to ACTN4; this interaction triggers conformational changes (By similarity). {ECO:0000250|UniProtKB:P12003, ECO:0000250|UniProtKB:P18206, ECO:0000269|PubMed:10085297, ECO:0000269|PubMed:20610383}. DOMAIN: Exists in at least two conformations. When in the closed, 'inactive' conformation, extensive interactions between the head and tail domains prevent detectable binding to most of its ligands. It takes on an 'active' conformation after cooperative and simultaneous binding of two different ligands. This activation involves displacement of the head-tail interactions and leads to a significant accumulation of ternary complexes. The active form then binds a number of proteins that have both signaling and structural roles that are essential for cell adhesion. {ECO:0000250|UniProtKB:P18206}.; DOMAIN: The N-terminal globular head (Vh) comprises of subdomains D1-D4. The C-terminal tail (Vt) binds F-actin and cross-links actin filaments into bundles. An intramolecular interaction between Vh and Vt masks the F-actin-binding domain located in Vt. The binding of talin and alpha-actinin to the D1 subdomain of vinculin induces a helical bundle conversion of this subdomain, leading to the disruption of the intramolecular interaction and the exposure of the cryptic F-actin-binding domain of Vt. Vt inhibits actin filament barbed end elongation without affecting the critical concentration of actin assembly. {ECO:0000250|UniProtKB:P18206}. +P32648 VIP_MOUSE VIP peptides [Cleaved into: Intestinal peptide PHI-42; Intestinal peptide PHI-27 (Peptide histidine isoleucinamide 27); Vasoactive intestinal peptide (VIP) (Vasoactive intestinal polypeptide)] 170 19,049 Glycosylation (1); Modified residue (3); Peptide (3); Propeptide (2); Sequence conflict (3); Signal peptide (1) FUNCTION: VIP causes vasodilation, lowers arterial blood pressure, stimulates myocardial contractility, increases glycogenolysis and relaxes the smooth muscle of trachea, stomach and gall bladder.; FUNCTION: PHM-27 is a potent agonist of the calcitonin receptor CALCR, with similar efficacy as calcitonin (By similarity). PHM also causes vasodilation. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. +Q8BRU6 VMAT2_MOUSE Synaptic vesicular amine transporter (Monoamine transporter) (Solute carrier family 18 member 2) (Vesicular amine transporter 2) (VAT2) 517 55,754 Chain (1); Disulfide bond (1); Glycosylation (5); Modified residue (2); Sequence conflict (1); Topological domain (13); Transmembrane (12) TRANSMEM 21 41 Helical. {ECO:0000255}.; TRANSMEM 133 153 Helical. {ECO:0000255}.; TRANSMEM 163 183 Helical. {ECO:0000255}.; TRANSMEM 193 213 Helical. {ECO:0000255}.; TRANSMEM 223 245 Helical. {ECO:0000255}.; TRANSMEM 252 274 Helical. {ECO:0000255}.; TRANSMEM 295 314 Helical. {ECO:0000255}.; TRANSMEM 332 355 Helical. {ECO:0000255}.; TRANSMEM 361 381 Helical. {ECO:0000255}.; TRANSMEM 393 413 Helical. {ECO:0000255}.; TRANSMEM 418 438 Helical. {ECO:0000255}.; TRANSMEM 444 465 Helical. {ECO:0000255}. TOPO_DOM 1 20 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 42 132 Lumenal, vesicle. {ECO:0000255}.; TOPO_DOM 154 162 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 184 192 Lumenal, vesicle. {ECO:0000255}.; TOPO_DOM 214 222 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 246 251 Lumenal, vesicle. {ECO:0000255}.; TOPO_DOM 275 294 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 315 331 Lumenal, vesicle. {ECO:0000255}.; TOPO_DOM 356 360 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 382 392 Lumenal, vesicle. {ECO:0000255}.; TOPO_DOM 414 417 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 439 443 Lumenal, vesicle. {ECO:0000255}.; TOPO_DOM 466 517 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in the ATP-dependent vesicular transport of biogenic amine neurotransmitters. Pumps cytosolic monoamines including dopamine, norepinephrine, serotonin, and histamine into synaptic vesicles. Requisite for vesicular amine storage prior to secretion via exocytosis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with SLC6A3. {ECO:0000269|PubMed:19357284}. +P40336 VP26A_MOUSE Vacuolar protein sorting-associated protein 26A (H58 protein) (H beta 58) (Vesicle protein sorting 26A) (mVPS26) 327 38,114 Alternative sequence (1); Beta strand (22); Chain (1); Helix (1); Modified residue (1); Mutagenesis (3); Sequence conflict (4); Turn (2) FUNCTION: Acts as component of the retromer cargo-selective complex (CSC). The CSC is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway. The recruitment of the CSC to the endosomal membrane involves RAB7A and SNX3.The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX3-retromer mediates the retrograde endosome-to-TGN transport of WLS distinct from the SNX-BAR retromer pathway. The SNX27-retromer is believed to be involved in endosome-to-plasma membrane trafficking and recycling of a broad spectrum of cargo proteins. The CSC complex seems to act as recruitment hub for other proteins, such as the WASH complex and TBC1D5 (By similarity). Required for retrograde transport of lysosomal enzyme receptor IGF2R (PubMed:15078902). Required to regulate transcytosis of the polymeric immunoglobulin receptor (pIgR-pIgA). Required for the endosomal localization of WASHC2 (indicative for the WASH complex). Required for the endosomal localization of TBC1D5. Mediates retromer cargo recognition of SORL1 and is involved in trafficking of SORL1 implicated in sorting and processing of APP (By similarity). Involved in retromer-independent lysosomal sorting of F2R. Involved in recycling of ADRB2 (By similarity). Acts redundantly with VSP26B in SNX-27 mediated endocytic recycling of SLC2A1/GLUT1. Enhances the affinity of SNX27 for PDZ-binding motifs in cargo proteins (PubMed:25136126). {ECO:0000250|UniProtKB:O75436, ECO:0000269|PubMed:15078902, ECO:0000269|PubMed:25136126}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15078902}. Endosome membrane {ECO:0000269|PubMed:15078902}; Peripheral membrane protein {ECO:0000269|PubMed:15078902}. Early endosome {ECO:0000269|PubMed:18088321, ECO:0000269|PubMed:21920005}. Note=Predominantly found in early not late endosomes. {ECO:0000269|PubMed:21920005}. SUBUNIT: Component of the heterotrimeric retromer cargo-selective complex (CSC), also described as vacuolar protein sorting subcomplex (VPS), formed by VPS26 (VPS26A or VPS26B), VPS29 and VPS35 (PubMed:18088321, PubMed:20875039). The CSC has a highly elongated structure with VPS26 and VPS29 binding independently at opposite distal ends of VPS35 as central platform (Probable). The CSC is believed to associate with variable sorting nexins to form functionally distinct retromer complex variants. The originally described retromer complex (also called SNX-BAR retromer) is a pentamer containing the CSC and a heterodimeric membrane-deforming subcomplex formed between SNX1 or SNX2 and SNX5 or SNX6 (also called SNX-BAR subcomplex); the respective CSC and SNX-BAR subcomplexes associate with low affinity. The CSC associates with SNX3 to form a SNX3-retromer complex. The CSC associates with SNX27, the WASH complex and the SNX-BAR subcomplex to form the SNX27-retromer complex (By similarity). Interacts with VPS29, VPS35, SNX27 (PubMed:18088321, PubMed:20875039, PubMed:25136126). Interacts with SNX1, SNX2, SNX5, SNX6, SNX3, RAB7A, ECPAS, EHD1, WASHC5, SORL1 (By similarity). {ECO:0000250|UniProtKB:O75436, ECO:0000269|PubMed:18088321, ECO:0000269|PubMed:20875039, ECO:0000269|PubMed:25136126, ECO:0000303|PubMed:20875039}. +P10639 THIO_MOUSE Thioredoxin (Trx) (ATL-derived factor) (ADF) 105 11,675 Active site (2); Chain (1); Disulfide bond (2); Domain (1); Modified residue (8); Sequence conflict (1); Site (3) FUNCTION: Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions (By similarity). Plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide. Nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO), and thereby inhibits caspase-3 activity. Induces the FOS/JUN AP-1 DNA binding activity in ionizing radiation (IR) cells through its oxidation/reduction status and stimulates AP-1 transcriptional activity (By similarity). {ECO:0000250}.; FUNCTION: ADF augments the expression of the interleukin-2 receptor TAC (IL2R/P55). PTM: In the fully reduced protein, both Cys-69 and Cys-73 are nitrosylated in response to nitric oxide (NO). When two disulfide bonds are present in the protein, only Cys-73 is nitrosylated. Cys-73 can serve as donor for nitrosylation of target proteins (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P10599}. Cytoplasm {ECO:0000250|UniProtKB:P10599}. Secreted {ECO:0000250|UniProtKB:P10599}. Note=Translocates from the cytoplasm into the nucleus after phorbol 12-myristate 13-acetate induction (PMA). Predominantly in the cytoplasm in non irradiated cells. Radiation induces translocation of TRX from the cytoplasm to the nucleus. Secreted by a leaderless secretory pathway. {ECO:0000250|UniProtKB:P10599}. SUBUNIT: Homodimer; disulfide-linked. Interacts with TXNIP through the redox-active site. Interacts with MAP3K5 and CASP3. Interacts with APEX1; the interaction stimulates the FOS/JUN AP-1 DNA-binding activity in a redox-dependent manner (By similarity). {ECO:0000250}. +Q8BWT1 THIM_MOUSE 3-ketoacyl-CoA thiolase, mitochondrial (EC 2.3.1.16) (Acetyl-CoA acyltransferase) (Beta-ketothiolase) (Mitochondrial 3-oxoacyl-CoA thiolase) 397 41,830 Active site (3); Chain (1); Modified residue (37); Sequence conflict (1); Transit peptide (1) Lipid metabolism; fatty acid metabolism. FUNCTION: Abolishes BNIP3-mediated apoptosis and mitochondrial damage. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Note=Colocalizes with BNIP3 in the mitochondria. {ECO:0000250}. SUBUNIT: Homotetramer. Interacts with BNIP3 (By similarity). {ECO:0000250}. +Q8BGW0 THMS1_MOUSE Protein THEMIS (Grb2-associating protein) (Gasp) (Protein thylex) (Thymocyte-expressed molecule involved in selection) 636 72,780 Alternative sequence (6); Chain (1); Modified residue (1); Mutagenesis (1); Region (2); Sequence conflict (1) FUNCTION: Plays a central role in late thymocyte development by controlling both positive and negative T-cell selection. Required to sustain and/or integrate signals required for proper lineage commitment and maturation of T-cells. Regulates T-cell development through T-cell antigen receptor (TCR) signaling and in particular through the regulation of calcium influx and phosphorylation of Erk. {ECO:0000269|PubMed:19597497, ECO:0000269|PubMed:19597498, ECO:0000269|PubMed:19597499, ECO:0000269|PubMed:19620281, ECO:0000269|PubMed:19805304}. PTM: Phosphorylated on Tyr residues quickly after TCR stimulation. {ECO:0000269|PubMed:19597498, ECO:0000269|PubMed:19597499}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19597497, ECO:0000269|PubMed:19597498, ECO:0000269|PubMed:19620281}. Nucleus {ECO:0000269|PubMed:19597498, ECO:0000269|PubMed:19620281}. SUBUNIT: Interacts with PLCG1, ITK, GRB2, and LAT. {ECO:0000269|PubMed:19597497, ECO:0000269|PubMed:19597498, ECO:0000269|PubMed:19597499, ECO:0000269|PubMed:19805304, ECO:0000269|PubMed:22561606}. TISSUE SPECIFICITY: Expressed in the thymus and to a lesser extent in the spleen but not detectable in non-lymphoid tissues. Highly expressed in thymocytes between the pre-T-cell antigen receptor (pre-TCR) and positive-selection checkpoints and expressed at low level in mature T-cells (at protein level). {ECO:0000269|PubMed:19597497, ECO:0000269|PubMed:19597498, ECO:0000269|PubMed:19597499, ECO:0000269|PubMed:19805304}. +Q8BH55 THNS1_MOUSE Threonine synthase-like 1 (TSH1) 747 83,100 Chain (1); Modified residue (1) +P62073 TIM10_MOUSE Mitochondrial import inner membrane translocase subunit Tim10 90 10,333 Chain (1); Disulfide bond (2); Motif (1); Sequence conflict (1) FUNCTION: Mitochondrial intermembrane chaperone that participates in the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. May also be required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Intermembrane side {ECO:0000250}. SUBUNIT: Heterohexamer; composed of 3 copies of TIMM9 and 3 copies of TIMM10/TIM10A, named soluble 70 kDa complex. The complex forms a 6-bladed alpha-propeller structure and associates with the TIMM22 component of the TIM22 complex. Interacts with multi-pass transmembrane proteins in transit. Also forms a complex composed of TIMM9, TIMM10/TIM10A and FXC1/TIM10B (By similarity). {ECO:0000250}. DOMAIN: The twin CX3C motif contains 4 conserved Cys residues that form 2 disulfide bonds in the mitochondrial intermembrane space. However, during the transit of TIMM10 from cytoplasm into mitochondrion, the Cys residues probably coordinate zinc, thereby preventing folding and allowing its transfer across mitochondrial outer membrane (By similarity). {ECO:0000250}. +B1ATG9 TIKI2_MOUSE Metalloprotease TIKI2 (EC 3.4.-.-) (Heart, kidney and adipose-enriched transmembrane protein) (TRAB domain-containing protein 2B) 517 57,368 Chain (1); Glycosylation (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 495 515 Helical. {ECO:0000255}. TOPO_DOM 20 494 Extracellular. {ECO:0000255}.; TOPO_DOM 516 517 Cytoplasmic. {ECO:0000255}. FUNCTION: Metalloprotease that acts as a negative regulator of the Wnt signaling pathway by mediating the cleavage of the 8 N-terminal residues of a subset of Wnt proteins. Following cleavage, Wnt proteins become oxidized and form large disulfide-bond oligomers, leading to their inactivation. Able to cleave WNT3A, WNT5, but not WNT11. Required for head formation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23152936}; Single-pass type I membrane protein {ECO:0000269|PubMed:23152936}. TISSUE SPECIFICITY: Highly expressed in heart and kidney. Also found in white and brown adipose tissue. {ECO:0000269|PubMed:23152936}. +Q6U7R4 TIMD4_MOUSE T-cell immunoglobulin and mucin domain-containing protein 4 (TIMD-4) (Spleen, mucin-containing, knockout of lymphotoxin protein) (SMUCKLER) (T-cell immunoglobulin mucin receptor 4) (TIM-4) (T-cell membrane protein 4) 343 37,548 Beta strand (11); Chain (1); Compositional bias (1); Disulfide bond (3); Domain (1); Glycosylation (1); Helix (2); Modified residue (3); Natural variant (2); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 280 300 Helical. {ECO:0000255}. TOPO_DOM 23 279 Extracellular. {ECO:0000255}.; TOPO_DOM 301 343 Cytoplasmic. {ECO:0000255}. FUNCTION: Phosphatidylserine receptor that enhances the engulfment of apoptotic cells. Involved in regulating T-cell proliferation and lymphotoxin signaling. Ligand for HAVCR1/TIMD1. {ECO:0000269|PubMed:14768054, ECO:0000269|PubMed:15793576, ECO:0000269|PubMed:17960135}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Homodimer. {ECO:0000305|PubMed:17960135, ECO:0000305|PubMed:18083575}. TISSUE SPECIFICITY: Predominantly expressed in lymphoid tissues, such as spleen, lymph nodes, and Peyer patches. Also expressed in fetal liver, salivary gland, and spleen stromal cells, predominantly in the marginal zone and to a lesser extent throughout the white pulp. Not expressed by bone marrow-derived cells. In spleen, expressed mostly by stromal cells in T- and B-cell areas, but not by T or B-lymphocytes. {ECO:0000269|PubMed:14768054, ECO:0000269|PubMed:17960135}. +Q9CQV7 TIM14_MOUSE Mitochondrial import inner membrane translocase subunit TIM14 (DnaJ homolog subfamily C member 19) 116 12,437 Alternative sequence (2); Chain (1); Domain (1); Initiator methionine (1); Modified residue (3); Topological domain (2); Transmembrane (1) TRANSMEM 4 24 Helical. {ECO:0000255}. TOPO_DOM 2 3 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 25 116 Mitochondrial matrix. {ECO:0000255}. FUNCTION: Probable component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. May act as a co-chaperone that stimulate the ATP-dependent activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. SUBUNIT: Probable component of the PAM complex at least composed of a mitochondrial HSP70 protein, GRPEL1 or GRPEL2, TIMM44, TIMM16/PAM16 and TIMM14/DNAJC19. {ECO:0000250}. +P55099 TKNK_MOUSE Tachykinin-3 (Neurokinin B-like protein Zneurok1) (Preprotachykinin-B) (PPT-B) [Cleaved into: Neurokinin-B (NKB) (Neuromedin-K)] 116 12,737 Modified residue (1); Peptide (1); Propeptide (2); Sequence conflict (1); Signal peptide (1) FUNCTION: Tachykinins are active peptides which excite neurons, evoke behavioral responses, are potent vasodilators and secretagogues, and contract (directly or indirectly) many smooth muscles. Is a critical central regulator of gonadal function (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. +Q8C0V0 TLK1_MOUSE Serine/threonine-protein kinase tousled-like 1 (EC 2.7.11.1) (Tousled-like kinase 1) 766 86,624 Active site (1); Binding site (1); Chain (1); Coiled coil (2); Domain (1); Erroneous initiation (1); Modified residue (9); Nucleotide binding (1) FUNCTION: Rapidly and transiently inhibited by phosphorylation following the generation of DNA double-stranded breaks during S-phase. This is cell cycle checkpoint and ATM-pathway dependent and appears to regulate processes involved in chromatin assembly (By similarity). Isoform 3 protects the cells from the ionizing radiation by facilitating the repair of DSBs. In vitro, phosphorylates histone H3 at 'Ser-10' (By similarity). {ECO:0000250, ECO:0000269|PubMed:16156902}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Heterodimerizes with TLK2. Interacts with ASF1A and ASF1B (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed in all tissues examined. {ECO:0000269|PubMed:10523312}. +P23949 TISD_MOUSE mRNA decay activator protein ZFP36L2 (Butyrate response factor 2) (TPA-induced sequence 11d) (Zinc finger protein 36, C3H1 type-like 2) (ZFP36-like 2) 484 50,070 Chain (1); Compositional bias (8); Erroneous gene model prediction (1); Erroneous initiation (1); Frameshift (1); Modified residue (4); Motif (1); Mutagenesis (1); Region (1); Sequence conflict (1); Zinc finger (2) FUNCTION: Zinc-finger RNA-binding protein that destabilizes several cytoplasmic AU-rich element (ARE)-containing mRNA transcripts by promoting their poly(A) tail removal or deadenylation, and hence provide a mechanism for attenuating protein synthesis (PubMed:22701344, PubMed:22367205, PubMed:25505318, PubMed:24830504, PubMed:27102483). Acts as a 3'-untranslated region (UTR) ARE mRNA-binding adapter protein to communicate signaling events to the mRNA decay machinery (By similarity). Functions by recruiting the CCR4-NOT deadenylase complex and probably other components of the cytoplasmic RNA decay machinery to the bound ARE-containing mRNAs, and hence promotes ARE-mediated mRNA deadenylation and decay processes (By similarity). Binds to 3'-UTR ARE of numerous mRNAs (PubMed:22701344, PubMed:22367205, PubMed:25505318, PubMed:24830504). Promotes ARE-containing mRNA decay of the low-density lipoprotein (LDL) receptor (LDLR) mRNA in response to phorbol 12-myristate 13-acetate (PMA) treatment in a p38 MAPK-dependent manner (By similarity). Positively regulates early adipogenesis by promoting ARE-mediated mRNA decay of immediate early genes (IEGs) (PubMed:22701344). Plays a role in mature peripheral neuron integrity by promoting ARE-containing mRNA decay of the transcriptional repressor REST mRNA (PubMed:25505318). Plays a role in ovulation and oocyte meiotic maturation by promoting ARE-mediated mRNA decay of the luteinizing hormone receptor LHCGR mRNA (PubMed:24830504). Acts as a negative regulator of erythroid cell differentiation: promotes glucocorticoid-induced self-renewal of erythroid cells by binding mRNAs that are induced or highly expressed during terminal erythroid differentiation and promotes their degradation, preventing erythroid cell differentiation (PubMed:19633199, PubMed:23748442). In association with ZFP36L1 maintains quiescence on developing B lymphocytes by promoting ARE-mediated decay of several mRNAs encoding cell cycle regulators that help B cells progress through the cell cycle, and hence ensuring accurate variable-diversity-joining (VDJ) recombination process and functional immune cell formation (PubMed:27102483). Together with ZFP36L1 is also necessary for thymocyte development and prevention of T-cell acute lymphoblastic leukemia (T-ALL) transformation by promoting ARE-mediated mRNA decay of the oncogenic transcription factor NOTCH1 mRNA (PubMed:20622884). {ECO:0000250|UniProtKB:P47974, ECO:0000269|PubMed:19633199, ECO:0000269|PubMed:20622884, ECO:0000269|PubMed:22367205, ECO:0000269|PubMed:22701344, ECO:0000269|PubMed:23748442, ECO:0000269|PubMed:24830504, ECO:0000269|PubMed:25505318, ECO:0000269|PubMed:27102483}. PTM: Phosphorylated by RPS6KA1 at Ser-480 and Ser-482 upon phorbol 12-myristate 13-acetate (PMA) treatment; this phosphorylation results in dissociation of the CCR4-NOT-deadenylase complex and induces p38 MAPK-mediated stabilization of the low-density lipoprotein (LDL) receptor (LDLR) mRNA (By similarity). Phosphorylation occurs during early preadipocyte differentiation (PubMed:22701344). {ECO:0000250|UniProtKB:P47974, ECO:0000269|PubMed:22701344}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11796723, ECO:0000269|PubMed:22367205, ECO:0000269|PubMed:24733888}. Cytoplasm {ECO:0000269|PubMed:11796723, ECO:0000269|PubMed:22367205, ECO:0000269|PubMed:24733888}. Note=Shuttles between the nucleus and the cytoplasm in a XPO1/CRM1-dependent manner (PubMed:11796723, PubMed:22367205). {ECO:0000269|PubMed:11796723, ECO:0000269|PubMed:22367205}. SUBUNIT: Associates with the cytoplasmic CCR4-NOT deadenylase to trigger ARE-containing mRNA deadenylation and decay processes. Interacts with CNOT7; this interaction is inhibited in response to phorbol 12-myristate 13-acetate (PMA) treatment in a p38 MAPK-dependent manner. {ECO:0000250|UniProtKB:P47974}. TISSUE SPECIFICITY: Expressed in preadipocytes and adipocytes (at protein level) (PubMed:22701344). Expressed at highest level in lymphoid tissues such as thymus, spleen, lung, uterus, ovary, small and large intestine, mammary gland, fat and bone marrow (PubMed:19633199, PubMed:22367205). Expressed at intermediate level in kidney, heart, adrenal, eye and fetal liver (PubMed:19633199). Weakly expressed in brain, skeletal muscle and liver (PubMed:19633199, PubMed:22367205). Expressed through B lymphocyte development (PubMed:27102483). Expressed in superior cervical ganglion (SCG) and dorsal root ganglion (DRG) (PubMed:25505318). Expressed in embryonic stem cells (ESCs) (PubMed:24733888). {ECO:0000269|PubMed:19633199, ECO:0000269|PubMed:22367205, ECO:0000269|PubMed:22701344, ECO:0000269|PubMed:24733888, ECO:0000269|PubMed:25505318, ECO:0000269|PubMed:27102483}. +Q9EPQ1 TLR1_MOUSE Toll-like receptor 1 (Toll/interleukin-1 receptor-like protein) (TIL) (CD antigen CD281) 795 90,673 Chain (1); Disulfide bond (4); Domain (2); Glycosylation (9); Region (1); Repeat (19); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 583 603 Helical. {ECO:0000255}. TOPO_DOM 26 582 Extracellular. {ECO:0000255}.; TOPO_DOM 604 795 Cytoplasmic. {ECO:0000255}. FUNCTION: Participates in the innate immune response to microbial agents. Specifically recognizes diacylated and triacylated lipopeptides. Cooperates with TLR2 to mediate the innate immune response to bacterial lipoproteins or lipopeptides. Forms the activation cluster TLR2:TLR1:CD14 in response to triacylated lipopeptides, this cluster triggers signaling from the cell surface and subsequently is targeted to the Golgi in a lipid-raft dependent pathway. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (By similarity). Acts as a coreceptor for M.tuberculosis lipoproteins LprG, LpqH and PhoS1 (pstS1), in conjunction with TLR2 and for some but not all lipoproteins CD14 and/or CD36. The lipoproteins act as agonists to modulate antigen presenting cell functions in response to the pathogen (PubMed:19362712). {ECO:0000250|UniProtKB:Q15399, ECO:0000269|PubMed:19362712}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11095740, ECO:0000269|PubMed:17998391}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasmic vesicle, phagosome membrane {ECO:0000269|PubMed:11095740}; Single-pass type I membrane protein {ECO:0000255}. Membrane raft {ECO:0000250|UniProtKB:Q15399}. Golgi apparatus {ECO:0000250|UniProtKB:Q15399}. Note=Does not reside in lipid rafts before stimulation but accumulates increasingly in the raft upon the presence of the microbial ligand. In response to triacylated lipoproteins, TLR2:TLR1 heterodimers are recruited in lipid rafts, this recruitment determine the intracellular targeting to the Golgi apparatus. {ECO:0000250|UniProtKB:Q15399}. SUBUNIT: Interacts (via extracellular domain) with TLR2. TLR2 seems to exist in heterodimers with either TLR1 or TLR6 before stimulation by the ligand. The heterodimers form bigger oligomers in response to their corresponding ligands as well as further heterotypic associations with other receptors such as CD14 and/or CD36 (By similarity). Binds MYD88 (via TIR domain). Interacts with CNPY3 (PubMed:17998391). {ECO:0000250|UniProtKB:Q15399, ECO:0000269|PubMed:17998391}. +Q8BGY5 TM140_MOUSE Transmembrane protein 140 185 20,767 Chain (1); Sequence conflict (2); Topological domain (5); Transmembrane (4) TRANSMEM 14 34 Helical. {ECO:0000255}.; TRANSMEM 85 105 Helical. {ECO:0000255}.; TRANSMEM 115 135 Helical. {ECO:0000255}.; TRANSMEM 146 166 Helical. {ECO:0000255}. TOPO_DOM 1 13 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 35 84 Extracellular. {ECO:0000255}.; TOPO_DOM 106 114 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 136 145 Extracellular. {ECO:0000255}.; TOPO_DOM 167 185 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9CR76 TM186_MOUSE Transmembrane protein 186 216 24,632 Chain (1); Frameshift (1); Sequence conflict (1); Transmembrane (2) TRANSMEM 69 91 Helical. {ECO:0000255}.; TRANSMEM 104 124 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q3UBX0 TM109_MOUSE Transmembrane protein 109 (Mitsugumin-23) (Mg23) 243 26,306 Chain (1); Sequence conflict (1); Signal peptide (1); Topological domain (4); Transmembrane (3) TRANSMEM 84 104 Helical. {ECO:0000255}.; TRANSMEM 136 156 Helical. {ECO:0000255}.; TRANSMEM 186 205 Helical. {ECO:0000255}. TOPO_DOM 34 83 Lumenal. {ECO:0000250|UniProtKB:O77751}.; TOPO_DOM 105 135 Cytoplasmic. {ECO:0000250|UniProtKB:O77751}.; TOPO_DOM 157 185 Lumenal. {ECO:0000250|UniProtKB:O77751}.; TOPO_DOM 206 243 Cytoplasmic. {ECO:0000250|UniProtKB:O77751}. FUNCTION: May mediate cellular response to DNA damage by protecting against ultraviolet C-induced cell death (PubMed:20060811). Can form voltage-gated calcium and potassium channels in vitro (By similarity). {ECO:0000250|UniProtKB:O77751, ECO:0000250|UniProtKB:Q9BVC6, ECO:0000269|PubMed:20060811}. SUBCELLULAR LOCATION: Nucleus outer membrane {ECO:0000250|UniProtKB:O77751}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O77751}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O77751}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O77751}. Sarcoplasmic reticulum membrane {ECO:0000250|UniProtKB:O77751}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O77751}. SUBUNIT: Homooligomer. Interacts with CRYAB. {ECO:0000250|UniProtKB:O77751, ECO:0000250|UniProtKB:Q9BVC6}. +Q8BVA2 TM222_MOUSE Transmembrane protein 222 208 23,180 Chain (1); Frameshift (1); Topological domain (4); Transmembrane (3) TRANSMEM 56 76 Helical. {ECO:0000255}.; TRANSMEM 165 185 Helical. {ECO:0000255}.; TRANSMEM 187 207 Helical. {ECO:0000255}. TOPO_DOM 1 55 Extracellular. {ECO:0000255}.; TOPO_DOM 77 164 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 186 186 Extracellular. {ECO:0000255}.; TOPO_DOM 208 208 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8BG50 TM169_MOUSE Transmembrane protein 169 297 33,424 Chain (1); Topological domain (3); Transmembrane (2) TRANSMEM 160 180 Helical. {ECO:0000255}.; TRANSMEM 211 231 Helical. {ECO:0000255}. TOPO_DOM 1 159 Extracellular. {ECO:0000255}.; TOPO_DOM 181 210 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 232 297 Extracellular. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8VDR5 TM267_MOUSE Transmembrane protein 267 215 24,152 Chain (1); Sequence conflict (1); Transmembrane (3) TRANSMEM 77 97 Helical. {ECO:0000255}.; TRANSMEM 114 134 Helical. {ECO:0000255}.; TRANSMEM 178 198 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q3TBN1 TM248_MOUSE Transmembrane protein 248 314 35,041 Chain (1); Frameshift (1); Sequence conflict (1); Transmembrane (4) TRANSMEM 21 41 Helical. {ECO:0000255}.; TRANSMEM 179 199 Helical. {ECO:0000255}.; TRANSMEM 236 258 Helical. {ECO:0000255}.; TRANSMEM 270 290 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8R239 TM268_MOUSE Transmembrane protein 268 342 37,763 Alternative sequence (3); Chain (1); Erroneous gene model prediction (2); Frameshift (1); Sequence conflict (2); Transmembrane (2) TRANSMEM 106 126 Helical. {ECO:0000255}.; TRANSMEM 133 153 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q3UUA0 TM211_MOUSE Transmembrane protein 211 195 20,752 Chain (1); Transmembrane (4) TRANSMEM 7 27 Helical. {ECO:0000255}.; TRANSMEM 73 93 Helical. {ECO:0000255}.; TRANSMEM 108 128 Helical. {ECO:0000255}.; TRANSMEM 149 169 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8BPE4 TM177_MOUSE Transmembrane protein 177 311 34,067 Chain (1); Topological domain (4); Transmembrane (3) TRANSMEM 18 38 Helical. {ECO:0000255}.; TRANSMEM 165 185 Helical. {ECO:0000255}.; TRANSMEM 191 211 Helical. {ECO:0000255}. TOPO_DOM 1 17 Mitochondrial matrix. {ECO:0000305}.; TOPO_DOM 39 164 Mitochondrial intermembrane. {ECO:0000305}.; TOPO_DOM 186 190 Mitochondrial matrix. {ECO:0000305}.; TOPO_DOM 212 311 Mitochondrial intermembrane. {ECO:0000305}. FUNCTION: Plays a role in the early steps of cytochrome c oxidase subunit II (MT-CO2/COX2) maturation and is required for the stabilization of COX20 and the newly synthesized MT-CO2/COX2 protein. {ECO:0000250|UniProtKB:Q53S58}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q53S58}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Found in a complex with COX20, COA6, MT-CO2/COX2, COX18, SCO1 and SCO2. Interacts with COX20. Interacts with COX1, MT-CO2/COX2, SCO1 and SCO2 in a COX20-dependent manner. {ECO:0000250|UniProtKB:Q53S58}. +Q6UJB9 TM270_MOUSE Transmembrane protein 270 264 29,547 Alternative sequence (1); Chain (1); Transmembrane (3) TRANSMEM 31 51 Helical. {ECO:0000255}.; TRANSMEM 74 94 Helical. {ECO:0000255}.; TRANSMEM 133 153 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Testis. {ECO:0000269|PubMed:18398435}. +P50592 TNF10_MOUSE Tumor necrosis factor ligand superfamily member 10 (TNF-related apoptosis-inducing ligand) (Protein TRAIL) (CD antigen CD253) 291 33,477 Chain (1); Glycosylation (1); Metal binding (1); Topological domain (2); Transmembrane (1) TRANSMEM 18 38 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 17 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 39 291 Extracellular. {ECO:0000255}. FUNCTION: Cytokine that binds to TNFRSF10A/TRAILR1, TNFRSF10B/TRAILR2, TNFRSF10C/TRAILR3, TNFRSF10D/TRAILR4 and possibly also to TNFRSF11B/OPG. Induces apoptosis. Its activity may be modulated by binding to the decoy receptors TNFRSF10C/TRAILR3, TNFRSF10D/TRAILR4 and TNFRSF11B/OPG that cannot induce apoptosis. {ECO:0000250|UniProtKB:P50591}. PTM: Tyrosine phosphorylated by PKDCC/VLK. {ECO:0000250|UniProtKB:P50591}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P50591}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P50591}. Secreted {ECO:0000250|UniProtKB:P50591}. Note=Exists both as membrane-bound and soluble form. {ECO:0000250|UniProtKB:P50591}. SUBUNIT: Homotrimer. One TNFSF10 homotrimer interacts with three TNFSF10A mononers. One TNFSF10 homotrimer interacts with three TNFSF10B mononers. {ECO:0000250|UniProtKB:P50591}. TISSUE SPECIFICITY: Widespread. +Q4FJU9 TMM40_MOUSE Transmembrane protein 40 225 24,926 Chain (1); Compositional bias (1); Erroneous initiation (1); Modified residue (2); Sequence conflict (2); Transmembrane (2) TRANSMEM 152 172 Helical. {ECO:0000255}.; TRANSMEM 179 199 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9EP64 TNMD_MOUSE Tenomodulin (TeM) (mTeM) (Chondromodulin-1-like protein) (ChM1L) (mChM1L) (Chondromodulin-I-like protein) (Myodulin) (Tendin) 317 37,047 Chain (1); Disulfide bond (1); Domain (1); Erroneous termination (1); Glycosylation (2); Modified residue (1); Sequence conflict (6); Topological domain (2); Transmembrane (1) TRANSMEM 31 50 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 30 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 51 317 Extracellular. {ECO:0000255}. FUNCTION: May be an angiogenesis inhibitor. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Nucleus envelope {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed with highest expression in tendons and ligaments, in the diaphragm, eye and skeletal muscle. Expressed in neuronal cells of all brain regions. Very low expression, if any, in glial cells. {ECO:0000269|PubMed:11357195}. +O54907 TNF12_MOUSE Tumor necrosis factor ligand superfamily member 12 (TNF-related weak inducer of apoptosis) (TWEAK) [Cleaved into: Tumor necrosis factor ligand superfamily member 12, membrane form; Tumor necrosis factor ligand superfamily member 12, secreted form] 249 27,441 Chain (2); Disulfide bond (1); Glycosylation (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 22 45 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 21 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 46 249 Extracellular. {ECO:0000255}. FUNCTION: Binds to FN14 and possibly also to TNRFSF12/APO3. Weak inducer of apoptosis in some cell types. Mediates NF-kappa-B activation. Promotes angiogenesis and the proliferation of endothelial cells. Also involved in induction of inflammatory cytokines. Promotes IL8 secretion (By similarity). {ECO:0000250}. PTM: The soluble form is produced from the membrane form by proteolytic processing. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: Tumor necrosis factor ligand superfamily member 12, secreted form: Secreted {ECO:0000250}. SUBUNIT: Homotrimer. Interacts with the angiogenic factor AGGF1/VG5Q (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. +Q9DBS1 TMM43_MOUSE Transmembrane protein 43 (Protein LUMA) 400 44,783 Chain (1); Initiator methionine (1); Modified residue (1); Topological domain (5); Transmembrane (4) TRANSMEM 32 52 Helical. {ECO:0000255}.; TRANSMEM 314 334 Helical. {ECO:0000255}.; TRANSMEM 346 366 Helical. {ECO:0000255}.; TRANSMEM 369 389 Helical. {ECO:0000255}. TOPO_DOM 2 31 Nuclear. {ECO:0000255}.; TOPO_DOM 53 313 Perinuclear space. {ECO:0000255}.; TOPO_DOM 335 345 Nuclear. {ECO:0000255}.; TOPO_DOM 367 368 Perinuclear space. {ECO:0000255}.; TOPO_DOM 390 400 Nuclear. {ECO:0000255}. FUNCTION: May have an important role in maintaining nuclear envelope structure by organizing protein complexes at the inner nuclear membrane. Required for retaining emerin at the inner nuclear membrane. {ECO:0000269|PubMed:18230648}. SUBCELLULAR LOCATION: Endoplasmic reticulum. Nucleus inner membrane; Multi-pass membrane protein. Note=Retained in the inner nuclear membrane through interaction with EMD and A- and B-lamins. The N- and C-termini are oriented towards the nucleoplasm. The majority of the hydrophilic domain resides in the endoplasmic reticulum lumen. SUBUNIT: Can form oligomers through the transmembrane domains. Interacts with EMD; the interaction retains EMD at the inner nuclear membrane. Interacts with LMNA and LMNB2. Interacts with SUN2 (By similarity). {ECO:0000250}. +Q5UBV8 TNF15_MOUSE Tumor necrosis factor ligand superfamily member 15 (TNF ligand-related molecule 1) (Vascular endothelial cell growth inhibitor) 252 27,723 Chain (1); Disulfide bond (1); Glycosylation (2); Sequence conflict (4); Site (2); Topological domain (2); Transmembrane (1) TRANSMEM 40 60 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 39 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 61 252 Extracellular. {ECO:0000255}. FUNCTION: Receptor for TNFRSF25 and TNFRSF6B. Mediates activation of NF-kappa-B. Inhibits vascular endothelial growth and angiogenesis (in vitro). Promotes activation of caspases and apoptosis (By similarity). Promotes splenocyte alloactivation. {ECO:0000250, ECO:0000269|PubMed:11911831}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. SUBUNIT: Homotrimer. {ECO:0000250}. +Q8BFY9 TNPO1_MOUSE Transportin-1 (Importin beta-2) (Karyopherin beta-2) 898 102,357 Alternative sequence (1); Chain (1); Domain (1); Erroneous initiation (2); Repeat (20); Sequence conflict (1); Site (2) FUNCTION: Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates (PubMed:11493596). Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (By similarity). Involved in nuclear import of M9-containing proteins. In vitro, binds directly to the M9 region of the heterogeneous nuclear ribonucleoproteins (hnRNP), A1 and A2 and mediates their nuclear import. Appears also to be involved in hnRNP A1/A2 nuclear export. Mediates the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5. Binds to a beta-like import receptor binding (BIB) domain of RPL23A (By similarity). In vitro, mediates nuclear import of SRP19 (By similarity). Mediates the import of histones H2A, H2B, H3 and H4 (PubMed:11493596). Mediates nuclear import of ADAR/ADAR1 in a RanGTP-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q92973, ECO:0000269|PubMed:11493596}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Identified in a complex that contains TNPO1, RAN and RANBP1 (By similarity). Binds HNRPA1, HNRPA2, HNRNPDL, RPL23A, RPS7, RPL5, RAN and SRP19. Interacts with H2A, H2B, H3 and H4 histones (PubMed:11493596). Interacts with isoform 1 and isoform 5 of ADAR/ADAR1 (via DRBM 3 domain). Interacts with SNAI1 (via zinc fingers); the interaction mediates SNAI1 nuclear import. Interacts with SNAI2 (via zinc fingers) (By similarity). {ECO:0000250|UniProtKB:Q92973, ECO:0000269|PubMed:11493596}. +Q9D0Z3 TMM53_MOUSE Transmembrane protein 53 276 31,589 Alternative sequence (3); Chain (1); Transmembrane (1) TRANSMEM 170 190 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q9D5K1 TMM81_MOUSE Transmembrane protein 81 259 28,748 Chain (1); Disulfide bond (1); Domain (1); Glycosylation (3); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 224 244 Helical. {ECO:0000255}. TOPO_DOM 26 223 Extracellular. {ECO:0000255}.; TOPO_DOM 245 259 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q8R115 TMM82_MOUSE Transmembrane protein 82 356 38,882 Chain (1); Compositional bias (1); Sequence conflict (1); Transmembrane (8) TRANSMEM 31 51 Helical. {ECO:0000255}.; TRANSMEM 77 97 Helical. {ECO:0000255}.; TRANSMEM 120 140 Helical. {ECO:0000255}.; TRANSMEM 144 164 Helical. {ECO:0000255}.; TRANSMEM 202 222 Helical. {ECO:0000255}.; TRANSMEM 232 250 Helical. {ECO:0000255}.; TRANSMEM 263 283 Helical. {ECO:0000255}.; TRANSMEM 285 305 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +P86176 TIGIT_MOUSE T-cell immunoreceptor with Ig and ITIM domains (V-set and transmembrane domain-containing protein 3) 249 26,959 Chain (1); Disulfide bond (1); Domain (1); Glycosylation (1); Motif (1); Region (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 149 169 Helical. {ECO:0000255}. TOPO_DOM 29 148 Extracellular. {ECO:0000255}.; TOPO_DOM 170 249 Cytoplasmic. {ECO:0000255}. FUNCTION: Binds with high affinity to the poliovirus receptor (PVR) which causes increased secretion of IL10 and decreased secretion of IL12B and suppresses T-cell activation by promoting the generation of mature immunoregulatory dendritic cells. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q495A1}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q495A1}. SUBUNIT: Homodimer in cis; binds with high affinity to PVR, forming a heterotetrameric assembly of two TIGIT and two PVR molecules. Binds with lower affinity to NECTIN2 and NECTIN3 (By similarity). {ECO:0000250}. DOMAIN: Contains 1 copy of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is involved in modulation of cellular responses. The phosphorylated ITIM motif can bind the SH2 domain of several SH2-containing phosphatases. {ECO:0000250|UniProtKB:Q495A1, ECO:0000305}. +Q9WVA2 TIM8A_MOUSE Mitochondrial import inner membrane translocase subunit Tim8 A (Deafness dystonia protein 1 homolog) 97 11,042 Chain (1); Disulfide bond (2); Modified residue (4); Motif (1) FUNCTION: Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space. The TIMM8-TIMM13 complex mediates the import of proteins such as TIMM23, SLC25A12/ARALAR1 and SLC25A13/ARALAR2, while the predominant TIMM9-TIMM10 70 kDa complex mediates the import of much more proteins (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Intermembrane side {ECO:0000250}. SUBUNIT: Heterohexamer; composed of 3 copies of TIMM8A and 3 copies of TIMM13, named soluble 70 kDa complex. Associates with the TIM22 complex, whose core is composed of TIMM22 (By similarity). {ECO:0000250}. DOMAIN: The twin CX3C motif contains 4 conserved Cys residues that form 2 disulfide bonds in the mitochondrial intermembrane space. However, during the transit of TIMM8A from cytoplasm into mitochondrion, the Cys residues probably coordinate zinc, thereby preventing folding and allowing its transfer across mitochondrial outer membrane (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Present at high level in liver and brain, and at lower level in muscle and heart. In CNS sections, it is predominantly present in the soma and the dendritic portion of the Purkinje cells of the cerebellum, but not in the glial cells. Scattered expression also is also detected in the brain stem, olfactory bulb, substantia nigra, hippocampus and striatum (at protein level). Ubiquitously expressed. {ECO:0000269|PubMed:10873677, ECO:0000269|PubMed:15254020}. +Q9CQV1 TIM16_MOUSE Mitochondrial import inner membrane translocase subunit TIM16 (Mitochondria-associated granulocyte macrophage CSF-signaling molecule) (Presequence translocated-associated motor subunit PAM16) 125 13,785 Chain (1); Modified residue (1); Region (1) FUNCTION: Regulates ATP-dependent protein translocation into the mitochondrial matrix. Inhibits DNAJC19 stimulation of HSPA9/Mortalin ATPase activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Matrix side {ECO:0000250}. SUBUNIT: Probable component of the PAM complex at least composed of a mitochondrial HSP70 protein, GRPEL1 or GRPEL2, TIMM44, TIMM16/PAM16 and TIMM14/DNAJC19 (By similarity). Interacts with DNAJC19. Directly interacts with DNAJC15; this interaction counteracts DNAJC15-dependent stimulation of HSPA9 ATPase activity (By similarity). Associates with the TIM23 complex (By similarity). {ECO:0000250}. DOMAIN: The J-like region, although related to the J domain does not have co-chaperone activity. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in trabecular bone and cartilage and by differentiated chondrocytes localized in the hypertrophic zone and by osteoblasts at early developmental stages. {ECO:0000269|PubMed:24786642}. +Q8BGX2 TIM29_MOUSE Mitochondrial import inner membrane translocase subunit Tim29 (TIM29) 266 29,415 Chain (1); Topological domain (2); Transit peptide (1); Transmembrane (1) TRANSMEM 66 83 Helical. {ECO:0000255}. TOPO_DOM 38 65 Mitochondrial matrix. {ECO:0000250|UniProtKB:Q9BSF4}.; TOPO_DOM 84 266 Mitochondrial intermembrane. {ECO:0000250|UniProtKB:Q9BSF4}. FUNCTION: Component of the TIM22 complex, a complex that mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. The TIM22 complex forms a twin-pore translocase that uses the membrane potential as the external driving force. Required for the stability of the TIM22 complex and functions in the assembly of the TIMM22 protein into the TIM22 complex. May facilitate cooperation between TIM22 and TOM complexes by interacting with TOMM40. {ECO:0000250|UniProtKB:Q9BSF4}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9BSF4}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9BSF4}; Intermembrane side {ECO:0000250|UniProtKB:Q9BSF4}. SUBUNIT: Component of the TIM22 complex, which core is composed of TIMM22, associated with TIMM10 (TIMM10A and/or TIMM10B), TIMM9, AGK and TIMM29. Interacts with TIMM10B; the interaction is direct. Interacts with TOMM40; linking the TIM22 complex to the TOM complex. Interacts with TIMM22 (when oxidized); the interaction is direct. {ECO:0000250|UniProtKB:Q9BSF4}. +Q06806 TIE1_MOUSE Tyrosine-protein kinase receptor Tie-1 (EC 2.7.10.1) 1134 124,583 Active site (1); Binding site (1); Chain (1); Disulfide bond (9); Domain (9); Glycosylation (5); Modified residue (1); Nucleotide binding (1); Sequence conflict (9); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 756 780 Helical. {ECO:0000255}. TOPO_DOM 23 755 Extracellular. {ECO:0000255}.; TOPO_DOM 781 1134 Cytoplasmic. {ECO:0000255}. FUNCTION: Transmembrane tyrosine-protein kinase that may modulate TEK/TIE2 activity and contribute to the regulation of angiogenesis. {ECO:0000250}. PTM: Phosphorylated on tyrosine residues in response to ANGPT1, most likely by TEK/TIE2. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Heterodimer with TEK/TIE2. {ECO:0000250}. TISSUE SPECIFICITY: Specifically expressed in developing vascular endothelial cells. Abundantly expressed in lung and heart, moderately in brain, liver and kidney, and weakly in thymus, spleen and testis. {ECO:0000269|PubMed:8395828}. +Q62318 TIF1B_MOUSE Transcription intermediary factor 1-beta (TIF1-beta) (E3 SUMO-protein ligase TRIM28) (EC 2.3.2.27) (KRAB-A-interacting protein) (KRIP-1) (RING-type E3 ubiquitin transferase TIF1-beta) (Tripartite motif-containing protein 28) 834 88,847 Alternative sequence (2); Chain (1); Compositional bias (3); Cross-link (28); Domain (1); Initiator methionine (1); Modified residue (34); Motif (1); Mutagenesis (1); Region (4); Sequence conflict (2); Zinc finger (4) Protein modification; protein sumoylation. FUNCTION: Nuclear corepressor for KRAB domain-containing zinc finger proteins (KRAB-ZFPs). Mediates gene silencing by recruiting CHD3, a subunit of the nucleosome remodeling and deacetylation (NuRD) complex, and SETDB1 (which specifically methylates histone H3 at 'Lys-9' (H3K9me)) to the promoter regions of KRAB target genes. Enhances transcriptional repression by coordinating the increase in H3K9me, the decrease in histone H3 'Lys-9 and 'Lys-14' acetylation (H3K9ac and H3K14ac, respectively) and the disposition of HP1 proteins to silence gene expression. Recruitment of SETDB1 induces heterochromatinization. May play a role as a coactivator for CEBPB and NR3C1 in the transcriptional activation of ORM1. Also corepressor for ERBB4. Inhibits E2F1 activity by stimulating E2F1-HDAC1 complex formation and inhibiting E2F1 acetylation. May serve as a partial backup to prevent E2F1-mediated apoptosis in the absence of RB1. Important regulator of CDKN1A/p21(CIP1). Has E3 SUMO-protein ligase activity toward itself via its PHD-type zinc finger. Specifically sumoylates IRF7, thereby inhibiting its transactivation activity. Ubiquitinates p53/TP53 leading to its proteosomal degradation; the function is enhanced by MAGEC2 and MAGEA2, and possibly MAGEA3 and MAGEA6. Mediates the nuclear localization of KOX1, ZNF268 and ZNF300 transcription factors. Probably forms a corepressor complex required for activated KRAS-mediated promoter hypermethylation and transcriptional silencing of tumor suppressor genes (TSGs) or other tumor-related genes in colorectal cancer (CRC) cells. Also required to maintain a transcriptionally repressive state of genes in undifferentiated embryonic stem cells (ESCs). Associates at promoter regions of tumor suppressor genes (TSGs) leading to their gene silencing. The SETDB1-TRIM28-ZNF274 complex may play a role in recruiting ATRX to the 3'-exons of zinc-finger coding genes with atypical chromatin signatures to establish or maintain/protect H3K9me3 at these transcriptionally active regions (By similarity). Acts as a corepressor for ZFP568 (PubMed:22110054, PubMed:27658112). {ECO:0000250|UniProtKB:Q13263, ECO:0000269|PubMed:21518874, ECO:0000269|PubMed:22110054, ECO:0000269|PubMed:27658112, ECO:0000269|PubMed:9742105}. PTM: ATM-induced phosphorylation on Ser-824 represses sumoylation leading to the de-repression of expression of a subset of genes involved in cell cycle control and apoptosis in response to genotoxic stress. Dephosphorylation by the phosphatases, PPP1CA and PP1CB forms, allows sumoylation and expression of TRIM28 target genes (By similarity). {ECO:0000250}.; PTM: Sumoylation/desumoylation events regulate TRIM28-mediated transcriptional repression. Sumoylation is required for interaction with CHD3 and SETDB1 and the corepressor activity. Represses and is repressed by Ser-824 phosphorylation. Enhances the TRIM28 corepressor activity, inhibiting transcriptional activity of a number of genes including GADD45A and CDKN1A/p21. Lys-554, Lys-779 and Lys-804 are the major sites of sumoylation. In response to Dox-induced DNA damage, enhanced phosphorylation on Ser-824 prevents sumoylation and allows de-repression of CDKN1A/p21 (By similarity). {ECO:0000250}.; PTM: Auto-ubiquitinated; enhanced by MAGEA2 and MAGEC2. {ECO:0000250}.; PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10330177, ECO:0000269|PubMed:11154279, ECO:0000269|PubMed:12154074, ECO:0000269|PubMed:22110054}. Note=Associated with centromeric heterochromatin during cell differentiation through CBX1. SUBUNIT: Oligomer; the RBCC domain homotrimerizes and interacts with one molecule of KRAB to form the KRAB-KAP1 corepressor complex. Interacts with SETX (By similarity). Binding to a KRAB domain is an absolute requirement for silencing gene expression. Interacts with a number of KRAB-ZFP proteins including ZNF10, ZFP53, ZFP68, ZNF382 and ZNF256. Interacts with NCOR1, NR3C1 and CHD3. Interacts with CEBPB (via the RING-type and PHD-type zinc fingers). Interacts with CBX5 (via the PxVxL motif); the interaction occurs in interphase nuclei and competes for binding POGZ. Interacts with POGZ; the interaction competes for interaction with CBX5. Interacts with SETDB1; the interaction is enhanced by KAP1 sumoylation, stimulates SETB1 histone methyltransferase activity and gene silencing. Interacts (via the PHD-type zinc finger) with UBE2I; the interaction is required for sumoylation and repressor activity. Component of the TRIM28/KAP1-ERBB4-MDM2 complex involved in connecting growth factor and DNA damage responses. Interacts directly with ERBB4; the interaction represses ERBB4-mediated transcription activity. Interacts with MDM2; the interaction contributes to p53/TP53 inactivation. Component of the TRIM28/KAP1-MDM2-p53/TP53; involved in regulating p53/TP53 stabilization and activity. Interacts (via the leucine zipper alpha helical coiled-coil) with E2F1 (central region); the interaction inhibits E2F1 acetylation and transcriptional activity. Interacts with PPP1CA; the interaction dephosphorylates TRIM28 at Ser-824 and forms a complex at the p21 promoter site. Interacts with PPP1CB; the interaction is weak but is increased on dephosphorylation at Ser-824. Interacts with CEBPB and NR3C1. Interacts with CBX5 (via the PxVxL motif); the interaction occurs in interphase nuclei and competes for binding POGZ. Component of a ternary complex that includes TRIM28, a HP1 protein (CBX1, CBX3 OR CBX5), a KRAB domain-containing protein, and DNA. Interacts with SMARCAD1. Interacts with, and sumoylates IRF7. Interacts with MAGEC2. Part of a complex composed of TRIM28, HDAC1, HDAC2 and EHMT2. Interacts (via the RBCC domain) with KOX1 (via the KRAB domain), ZNF268 (via the KRAB domain) and ZNF300 (via the KRAB domain); the interactions increase KOX1, ZNF268 and ZNF300 nuclear localization activities. Interacts with AICDA. The large PER complex involved in the histone methylation is composed of at least PER2, CBX3, TRIM28, SUV39H1 and/or SUV39H2; CBX3 mediates the formation of the complex. Interacts with NR4A3; the interactions potentiates NR4A3 activity on NurRE promoter (PubMed:19321449). Interacts (unphosphorylated or phosphorylated form) with ZBTB1 (via BTB domain) (By similarity). Probably part of a corepressor complex containing ZNF304, TRIM28, SETDB1 and DNMT1. Interacts with ATRX. Forms a complex with ATRX, SETDB1 and ZNF274 (By similarity). Interacts with ZFP568; the interaction mediates ZFP568 transcriptional repression activity (PubMed:22110054, PubMed:27658112). Interacts with RRP1B (By similarity). {ECO:0000250|UniProtKB:O08629, ECO:0000250|UniProtKB:Q13263, ECO:0000269|PubMed:10330177, ECO:0000269|PubMed:10562550, ECO:0000269|PubMed:11154279, ECO:0000269|PubMed:19321449, ECO:0000269|PubMed:21518874, ECO:0000269|PubMed:22110054, ECO:0000269|PubMed:27658112, ECO:0000269|PubMed:9742105}. DOMAIN: The HP1 box is both necessary and sufficient for HP1 binding. {ECO:0000250}.; DOMAIN: The PHD-type zinc finger enhances CEBPB transcriptional activity. The PHD-type zinc finger, the HP1 box and the bromo domain, function together to assemble the machinery required for repression of KRAB domain-containing proteins. Acts as an intramolecular SUMO E3 ligase for autosumoylation of bromodomain (By similarity). {ECO:0000250}.; DOMAIN: The RING-finger-B Box-coiled-coil/tripartite motif (RBCC/TRIM motif) is required for interaction with the KRAB domain of KRAB-zinc finger proteins. Binds four zinc ions per molecule. The RING finger and the N-terminal of the leucine zipper alpha helical coiled-coil region of RBCC are required for oligomerization (By similarity). {ECO:0000250}.; DOMAIN: Contains one Pro-Xaa-Val-Xaa-Leu (PxVxL) motif, which is required for interaction with chromoshadow domains. This motif requires additional residues -7, -6, +4 and +5 of the central Val which contact the chromoshadow domain (By similarity). {ECO:0000250}. +Q71LX4 TLN2_MOUSE Talin-2 2375 253,621 Beta strand (7); Chain (1); Compositional bias (1); Domain (2); Erroneous initiation (2); Helix (9); Modified residue (5); Region (1); Sequence conflict (11); Turn (4) FUNCTION: As a major component of focal adhesion plaques that links integrin to the actin cytoskeleton, may play an important role in cell adhesion. Recruits PIP5K1C to focal adhesion plaques and strongly activates its kinase activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y4G6}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q9Y4G6}. Cell junction, synapse {ECO:0000250|UniProtKB:Q9Y4G6}. Cell membrane {ECO:0000250|UniProtKB:Q9Y4G6}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9Y4G6}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9Y4G6}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9Y4G6}. Note=Focal adhesion plaques and synapses. {ECO:0000250|UniProtKB:Q9Y4G6}. SUBUNIT: Interacts directly with PIP5K1C. {ECO:0000250|UniProtKB:Q9Y4G6}. +Q8VHN8 TIRR_MOUSE Tudor-interacting repair regulator protein (NUDT16-like protein 1) (Protein syndesmos) 211 23,414 Alternative sequence (3); Beta strand (9); Chain (1); Cross-link (2); Helix (7); Region (1); Sequence conflict (2); Site (1); Turn (3) FUNCTION: Key regulator of TP53BP1 required to stabilize TP53BP1 and regulate its recruitment to chromatin. In absence of DNA damage, interacts with the tandem Tudor-like domain of TP53BP1, masking the region that binds histone H4 dimethylated at 'Lys-20' (H4K20me2), thereby preventing TP53BP1 recruitment to chromatin and maintaining TP53BP1 localization to the nucleus. Following DNA damage, ATM-induced phosphorylation of TP53BP1 and subsequent recruitment of RIF1 leads to dissociate NUDT16L1/TIRR from TP53BP1, unmasking the tandem Tudor-like domain and allowing recruitment of TP53BP1 to DNA double strand breaks (DSBs). Binds U8 snoRNA. {ECO:0000250|UniProtKB:Q9BRJ7}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BRJ7}. SUBUNIT: Homodimer (PubMed:26100207). Interacts with TP53BP1 (via the Tudor-like domain); interaction is abolished following DNA damage and TP53BP1 phosphorylation by ATM (By similarity). Interacts (via the cytoplasmic part) with SDC4 (PubMed:11805099). Interacts with TGFB1I1 and PXN (PubMed:11805099). {ECO:0000250|UniProtKB:Q9BRJ7, ECO:0000269|PubMed:11805099, ECO:0000269|PubMed:26100207}. +P23950 TISB_MOUSE mRNA decay activator protein ZFP36L1 (Butyrate response factor 1) (TPA-induced sequence 11b) (Zinc finger protein 36, C3H1 type-like 1) (ZFP36-like 1) 338 36,385 Chain (1); Compositional bias (1); Modified residue (6); Region (2); Zinc finger (2) FUNCTION: Zinc-finger RNA-binding protein that destabilizes several cytoplasmic AU-rich element (ARE)-containing mRNA transcripts by promoting their poly(A) tail removal or deadenylation, and hence provide a mechanism for attenuating protein synthesis (PubMed:22701344, PubMed:24700863, PubMed:24733888, PubMed:27102483). Acts as a 3'-untranslated region (UTR) ARE mRNA-binding adapter protein to communicate signaling events to the mRNA decay machinery (By similarity). Functions by recruiting the CCR4-NOT deadenylating complex and components of the cytoplasmic RNA decay machinery to the bound ARE-containing mRNAs, and hence promotes ARE-mediated mRNA deadenylation and decay processes (By similarity). Induces also the degradation of ARE-containing mRNAs even in absence of poly(A) tail (By similarity). Binds to 3'-UTR ARE of numerous mRNAs (PubMed:22701344, PubMed:24700863, PubMed:24733888). Positively regulates early adipogenesis by promoting ARE-mediated mRNA decay of immediate early genes (IEGs) (PubMed:22701344). Promotes ARE-mediated mRNA decay of mineralocorticoid receptor NR3C2 mRNA in response to hypertonic stress (PubMed:24700863). Negatively regulates hematopoietic/erythroid cell differentiation by promoting ARE-mediated mRNA decay of the transcription factor STAT5B mRNA (By similarity). Positively regulates monocyte/macrophage cell differentiation by promoting ARE-mediated mRNA decay of the cyclin-dependent kinase CDK6 mRNA (By similarity). Promotes degradation of ARE-containing pluripotency-associated mRNAs in embryonic stem cells (ESCs), such as NANOG, through a fibroblast growth factor (FGF)-induced MAPK-dependent signaling pathway, and hence attenuates ESC self-renewal and positively regulates mesendoderm differentiation (PubMed:24733888). May play a role in mediating pro-apoptotic effects in malignant B-cells by promoting ARE-mediated mRNA decay of BCL2 mRNA (By similarity). In association with ZFP36L2 maintains quiescence on developing B lymphocytes by promoting ARE-mediated decay of several mRNAs encoding cell cycle regulators that help B cells progress through the cell cycle, and hence ensuring accurate variable-diversity-joining (VDJ) recombination and functional immune cell formation (PubMed:27102483). Together with ZFP36L2 is also necessary for thymocyte development and prevention of T-cell acute lymphoblastic leukemia (T-ALL) transformation by promoting ARE-mediated mRNA decay of the oncogenic transcription factor NOTCH1 mRNA (PubMed:20622884). Involved in the delivery of target ARE-mRNAs to processing bodies (PBs) (By similarity). In addition to its cytosolic mRNA-decay function, plays a role in the regulation of nuclear mRNA 3'-end processing; modulates mRNA 3'-end maturation efficiency of the DLL4 mRNA through binding with an ARE embedded in a weak noncanonical polyadenylation (poly(A)) signal in endothelial cells (By similarity). Also involved in the regulation of stress granule (SG) and P-body (PB) formation and fusion (By similarity). Plays a role in vasculogenesis and endocardial development (PubMed:15226444, PubMed:17013884). Involved in the regulation of keratinocyte proliferation, differentiation and apoptosis (By similarity). Plays a role in myoblast cell differentiation (PubMed:17889962). {ECO:0000250|UniProtKB:P17431, ECO:0000250|UniProtKB:Q07352, ECO:0000269|PubMed:15226444, ECO:0000269|PubMed:17013884, ECO:0000269|PubMed:17889962, ECO:0000269|PubMed:20622884, ECO:0000269|PubMed:22701344, ECO:0000269|PubMed:24700863, ECO:0000269|PubMed:24733888, ECO:0000269|PubMed:27102483}. PTM: Phosphorylated (PubMed:19179481). Phosphorylated by RPS6KA1 at Ser-334 upon phorbol 12-myristate 13-acetate (PMA) treatment; this phosphorylation results in dissociation of the CCR4-NOT deadenylase complex and induces p38 MAPK-mediated stabilization of the low-density lipoprotein receptor LDLR mRNA. Phosphorylated by protein kinase AKT1 at Ser-92 and Ser-203 in response to insulin; these phosphorylations stabilize ZFP36L1, increase the association with 14-3-3 proteins and mediate ARE-containing mRNA stabilization. AKT1-mediated phosphorylation at Ser-92 does not impair ARE-containing RNA-binding. Phosphorylated at Ser-54, Ser-92 and Ser-203 by MAPKAPK2; these phosphorylations increase the association with 14-3-3 proteins and mediate ARE-containing mRNA stabilization in a protein kinase AKT1-independent manner. MAPKAPK2-mediated phosphorylations at Ser-54, Ser-92 and Ser-203 do not impair ARE-containing RNA-binding (By similarity). Phosphorylations increase the association with 14-3-3 proteins and mediate ARE-containing mRNA stabilization during early adipogenesis in a p38 MAPK- and AKT-dependent manner (PubMed:22701344). {ECO:0000250|UniProtKB:Q07352, ECO:0000269|PubMed:19179481, ECO:0000269|PubMed:22701344}.; PTM: Ubiquitinated. Ubiquitination leads to proteasomal degradation, a process inhibited by phosphorylations at Ser-90, Ser-92 and Ser-203. {ECO:0000250|UniProtKB:Q07352}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11796723}. Cytoplasm {ECO:0000269|PubMed:11796723, ECO:0000269|PubMed:24700863, ECO:0000269|PubMed:24733888}. Cytoplasmic granule {ECO:0000250|UniProtKB:Q07352}. Cytoplasm, P-body {ECO:0000250|UniProtKB:Q07352}. Note=Shuttles between the nucleus and the cytoplasm in a XPO1/CRM1-dependent manner (PubMed:11796723). Component of cytoplasmic stress granules (By similarity). Localizes in processing bodies (PBs) (By similarity). {ECO:0000250|UniProtKB:Q07352, ECO:0000269|PubMed:11796723}. SUBUNIT: Associates with the cytoplasmic CCR4-NOT deadenylase and RNA exosome complexes to trigger ARE-containing mRNA deadenylation and decay processes. Interacts with CNOT1. Interacts (via N-terminus) with CNOT6. Interacts with CNOT7; this interaction is inhibited in response to phorbol 12-myristate 13-acetate (PMA) treatment in a p38 MAPK-dependent manner. Interacts with DCP1A. Interacts (via N-terminus) with DCP2. Interacts (via N-terminus) with EXOSC2. Interacts with XRN1. Interacts (via phosphorylated form) with YWHAB; this interaction occurs in a protein kinase AKT1-dependent manner (By similarity). Interacts (via phosphorylated form) with YWHAZ; this interaction occurs in a p38 MAPK- and AKT-signaling pathways (PubMed:22701344). {ECO:0000250|UniProtKB:Q07352, ECO:0000269|PubMed:22701344}. TISSUE SPECIFICITY: Expressed in preadipocytes and adipocytes (PubMed:22701344). Expressed in the proximal and distal tubules in the renal cortex (at protein level) (PubMed:24700863). Expressed in ovary, heart, kidney, lung, spleen and thymus (PubMed:15226444). Weakly expressed in brain, liver and testis (PubMed:15226444). Expressed in osteoblasts (PubMed:15465005). Expressed in embryonic stem cells (ESCs) (PubMed:24733888). Expressed through B lymphocyte development (PubMed:27102483). {ECO:0000269|PubMed:15226444, ECO:0000269|PubMed:15465005, ECO:0000269|PubMed:22701344, ECO:0000269|PubMed:24700863, ECO:0000269|PubMed:24733888, ECO:0000269|PubMed:27102483}. +Q6R5P0 TLR11_MOUSE Toll-like receptor 11 (Toll-like receptor 12) 926 105,873 Chain (1); Domain (1); Glycosylation (9); Repeat (10); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 722 742 Helical. {ECO:0000255}. TOPO_DOM 31 721 Extracellular. {ECO:0000255}.; TOPO_DOM 743 926 Cytoplasmic. {ECO:0000255}. FUNCTION: Participates in the innate immune response to microbial agents. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. {ECO:0000250|UniProtKB:Q6QNU9}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Binds MYD88 via their respective TIR domains (By similarity). Interacts with HSP90B1; this interaction is required for proper folding in the endoplasmic reticulum (PubMed:20865800). {ECO:0000250|UniProtKB:Q9EQU3, ECO:0000269|PubMed:20865800}. +Q6QNU9 TLR12_MOUSE Toll-like receptor 12 (Toll-like receptor 11) 906 99,945 Chain (1); Domain (1); Glycosylation (4); Mutagenesis (1); Repeat (17); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 710 730 Helical. {ECO:0000255}. TOPO_DOM 22 709 Extracellular. {ECO:0000255}.; TOPO_DOM 731 906 Cytoplasmic. {ECO:0000255}. FUNCTION: Participates in the innate immune response to microbial agents. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. Plays a role in preventing infection of internal organs of the urogenital system. {ECO:0000269|PubMed:15001781}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Binds MYD88 via their respective TIR domains. {ECO:0000250}. TISSUE SPECIFICITY: Macrophages, liver, kidney and bladder epithelial cells. {ECO:0000269|PubMed:15001781}. +Q6R5N8 TLR13_MOUSE Toll-like receptor 13 991 114,443 Beta strand (31); Chain (1); Domain (2); Erroneous initiation (1); Glycosylation (20); Helix (14); Repeat (25); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (13) TRANSMEM 784 804 Helical. {ECO:0000255}. TOPO_DOM 69 783 Extracellular. {ECO:0000255}.; TOPO_DOM 805 991 Cytoplasmic. {ECO:0000255}. FUNCTION: Component of innate and adaptive immunity that recognizes and binds 23S rRNA from bacteria. TLRs (Toll-like receptors) control host immune response against pathogens through recognition of molecular patterns specific to microorganisms. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. Specifically binds the 5'-CGGAAAGACC-3' sequence on bacterial 23S rRNA, a sequence also bound by MLS group antibiotics (including erythromycin). May also recognize vesicular stomatitis virus; however, these data require additional evidences. {ECO:0000269|PubMed:21131352, ECO:0000269|PubMed:22821982, ECO:0000269|PubMed:22896636}. SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:22896636}; Single-pass type I membrane protein {ECO:0000269|PubMed:22896636}. SUBUNIT: Binds MYD88 via their respective TIR domains (By similarity). Interacts with UNC93B1. {ECO:0000250, ECO:0000269|PubMed:17452530}. +Q9QUN7 TLR2_MOUSE Toll-like receptor 2 (CD antigen CD282) 784 89,449 Beta strand (29); Chain (1); Cross-link (1); Disulfide bond (3); Domain (2); Glycosylation (3); Helix (15); Motif (1); Mutagenesis (1); Repeat (19); Sequence conflict (2); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1); Turn (7) TRANSMEM 588 608 Helical. {ECO:0000255}. TOPO_DOM 25 587 Extracellular. {ECO:0000255}.; TOPO_DOM 609 784 Cytoplasmic. {ECO:0000255}. FUNCTION: Cooperates with LY96 to mediate the innate immune response to bacterial lipoproteins and other microbial cell wall components. Cooperates with TLR1 or TLR6 to mediate the innate immune response to bacterial lipoproteins or lipopeptides. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (By similarity) (PubMed:15690042). May also promote apoptosis in response to lipoproteins (By similarity). Forms activation clusters composed of several receptors depending on the ligand, these clusters trigger signaling from the cell surface and subsequently are targeted to the Golgi in a lipid-raft dependent pathway. Forms the cluster TLR2:TLR6:CD14:CD36 in response to diacylated lipopeptides and TLR2:TLR1:CD14 in response to triacylated lipopeptides (By similarity). Recognizes M.tuberculosis major T-antigen EsxA (ESAT-6) which inhibits downstream MYD88-dependent signaling (PubMed:17486091). Acts as the major receptor for M.tuberculosis lipoproteins LprA, LprG, LpqH and PhoS1 (pstS1), in conjunction with TLR1 and for some but not all lipoproteins CD14 and/or CD36. The lipoproteins act as agonists to modulate antigen presenting cell functions in response to the pathogen (PubMed:19362712). Recombinant MPT83 from M.tuberculosis stimulates secretion of cytokines (TNF-alpha, IL-6 and IL-12p40) by mouse macrophage cell lines in a TLR2-dependent fashion, which leads to increased host innate immunity responses against the bacterium (PubMed:22174456). Lung macrophages which express low levels of TLR2 respond poorly to stimulation by M.tuberculosis LpqH (PubMed:19362712). Required for normal uptake of M.tuberculosis, a process that is inhibited by M.tuberculosis LppM (PubMed:27220037). {ECO:0000250|UniProtKB:O60603, ECO:0000269|PubMed:15690042, ECO:0000269|PubMed:17486091, ECO:0000269|PubMed:19362712, ECO:0000269|PubMed:22174456, ECO:0000269|PubMed:27220037}. PTM: Ubiquitinated at Lys-754 by PPP1R11, leading to its degradation. Deubiquitinated by USP2. {ECO:0000269|PubMed:27805901}.; PTM: Glycosylation of Asn-442 is critical for secretion of the N-terminal ectodomain of TLR2. {ECO:0000250|UniProtKB:O60603}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11095740}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasmic vesicle, phagosome membrane {ECO:0000269|PubMed:11095740}; Single-pass type I membrane protein {ECO:0000255}. Membrane raft {ECO:0000250|UniProtKB:O60603}. Note=Does not reside in lipid rafts before stimulation but accumulates increasingly in the raft upon the presence of the microbial ligand. In response to diacylated lipoproteins, TLR2:TLR6 heterodimers are recruited in lipid rafts, this recruitment determine the intracellular targeting to the Golgi apparatus. Triacylated lipoproteins induce the same mechanism for TLR2:TLR1 heterodimers. {ECO:0000250|UniProtKB:O60603}. SUBUNIT: Interacts with LY96, TLR1 and TLR6 (via extracellular domain). TLR2 seems to exist in heterodimers with either TLR1 or TLR6 before stimulation by the ligand (PubMed:19931471). The heterodimers form bigger oligomers in response to their corresponding ligands as well as further heterotypic associations with other receptors such as CD14 and/or CD36 (By similarity). Binds MYD88 (via TIR domain). Interacts with TICAM1 (By similarity). Interacts with CNPY3 (PubMed:18780723). Interacts with ATG16L1 (By similarity). Interacts with non-modified M.tuberculosis protein MPT83 (PubMed:22174456). Interacts with PPP1R11 (PubMed:27805901). {ECO:0000250|UniProtKB:O60603, ECO:0000269|PubMed:18780723, ECO:0000269|PubMed:19931471, ECO:0000269|PubMed:22174456, ECO:0000269|PubMed:27805901}. DOMAIN: Ester-bound lipid substrates are bound through a crevice formed between the LRR 11 and LRR 12.; DOMAIN: The ATG16L1-binding motif mediates interaction with ATG16L1. {ECO:0000250}. TISSUE SPECIFICITY: Detected in a macrophage cell line, smooth muscle, lung, spleen, thymus, brain and adipose tissue. Cell surface expression detected in lung alveolar macrophages, dendritic macrophages and at lower levels in lung macrophages (at protein level) (PubMed:19362712). {ECO:0000269|PubMed:19362712}. +Q3TB48 TM104_MOUSE Transmembrane protein 104 496 55,838 Chain (1); Glycosylation (1); Sequence conflict (1); Topological domain (12); Transmembrane (11) TRANSMEM 11 31 Helical. {ECO:0000255}.; TRANSMEM 37 57 Helical. {ECO:0000255}.; TRANSMEM 147 167 Helical. {ECO:0000255}.; TRANSMEM 205 225 Helical. {ECO:0000255}.; TRANSMEM 234 254 Helical. {ECO:0000255}.; TRANSMEM 266 286 Helical. {ECO:0000255}.; TRANSMEM 307 327 Helical. {ECO:0000255}.; TRANSMEM 355 375 Helical. {ECO:0000255}.; TRANSMEM 398 418 Helical. {ECO:0000255}.; TRANSMEM 422 442 Helical. {ECO:0000255}.; TRANSMEM 471 491 Helical. {ECO:0000255}. TOPO_DOM 1 10 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 32 36 Extracellular. {ECO:0000255}.; TOPO_DOM 58 146 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 168 204 Extracellular. {ECO:0000255}.; TOPO_DOM 226 233 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 255 265 Extracellular. {ECO:0000255}.; TOPO_DOM 287 306 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 328 354 Extracellular. {ECO:0000255}.; TOPO_DOM 376 397 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 419 421 Extracellular. {ECO:0000255}.; TOPO_DOM 443 470 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 492 496 Extracellular. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8VD26 TM143_MOUSE Transmembrane protein 143 458 51,596 Alternative sequence (5); Chain (1); Modified residue (1); Sequence conflict (3); Transmembrane (2) TRANSMEM 277 297 Helical. {ECO:0000255}.; TRANSMEM 298 318 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +P52875 TM165_MOUSE Transmembrane protein 165 (TPA-regulated locus protein) (Transmembrane protein PFT27) (Transmembrane protein TPARL) 323 34,791 Chain (1); Coiled coil (1); Frameshift (1); Signal peptide (1); Topological domain (7); Transmembrane (6) TRANSMEM 90 110 Helical. {ECO:0000255}.; TRANSMEM 127 147 Helical. {ECO:0000255}.; TRANSMEM 152 172 Helical. {ECO:0000255}.; TRANSMEM 228 248 Helical. {ECO:0000255}.; TRANSMEM 267 287 Helical. {ECO:0000255}.; TRANSMEM 299 319 Helical. {ECO:0000255}. TOPO_DOM 34 89 Lumenal. {ECO:0000255}.; TOPO_DOM 111 126 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 148 151 Lumenal. {ECO:0000255}.; TOPO_DOM 173 227 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 249 266 Lumenal. {ECO:0000255}.; TOPO_DOM 288 298 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 320 323 Lumenal. {ECO:0000255}. FUNCTION: May function as a calcium/proton transporter involved in calcium and in lysosomal pH homeostasis. Therefore, it may play an indirect role in protein glycosylation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250}. Lysosome membrane {ECO:0000250}. Early endosome membrane {ECO:0000250}. Late endosome membrane {ECO:0000250}. +Q3U284 TM231_MOUSE Transmembrane protein 231 315 36,261 Chain (1); Glycosylation (3); Transmembrane (2) TRANSMEM 23 43 Helical. {ECO:0000255}.; TRANSMEM 262 282 Helical. {ECO:0000255}. FUNCTION: Transmembrane component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. Required for ciliogenesis and sonic hedgehog/SHH signaling. {ECO:0000269|PubMed:22179047}. SUBCELLULAR LOCATION: Cell projection, cilium membrane {ECO:0000269|PubMed:22179047}; Multi-pass membrane protein {ECO:0000269|PubMed:22179047}. Note=Localizes to the transition zone of primary cilia; SEPT2 is required for localization to the transition zone. SUBUNIT: Part of the tectonic-like complex (also named B9 complex) (PubMed:22179047). Interacts with TMEM107 (By similarity). {ECO:0000250|UniProtKB:Q9H6L2, ECO:0000269|PubMed:22179047}. +Q8BH26 TM251_MOUSE Transmembrane protein 251 163 18,720 Chain (1); Transmembrane (2) TRANSMEM 40 60 Helical. {ECO:0000255}.; TRANSMEM 98 118 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8C353 TM252_MOUSE Transmembrane protein 252 183 20,376 Chain (1); Transmembrane (2) TRANSMEM 8 28 Helical. {ECO:0000255}.; TRANSMEM 39 59 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9CYV5 TM135_MOUSE Transmembrane protein 135 (Peroxisomal membrane protein 52) (PMP52) 458 52,364 Chain (1); Sequence conflict (2); Transmembrane (6) TRANSMEM 68 88 Helical. {ECO:0000255}.; TRANSMEM 96 116 Helical. {ECO:0000255}.; TRANSMEM 149 169 Helical. {ECO:0000255}.; TRANSMEM 298 318 Helical. {ECO:0000255}.; TRANSMEM 331 351 Helical. {ECO:0000255}.; TRANSMEM 377 397 Helical. {ECO:0000255}. FUNCTION: Involved in mitochondrial metabolism by regulating the balance between mitochondrial fusion and fission (PubMed:27863209). May act as a regulator of mitochondrial fission that promotes DNM1L-dependent fission through activation of DNM1L (PubMed:27863209). May be involved in peroxisome organization (By similarity). {ECO:0000250|UniProtKB:Q5U4F4, ECO:0000269|PubMed:27863209}. SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000305|PubMed:27863209}; Multi-pass membrane protein {ECO:0000305}. Peroxisome membrane {ECO:0000305|PubMed:17768142}; Multi-pass membrane protein {ECO:0000255}. +Q8R138 TM119_MOUSE Transmembrane protein 119 (Osteoblast induction factor) (OBIF) 280 29,401 Chain (1); Glycosylation (1); Modified residue (1); Mutagenesis (5); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 92 112 Helical. {ECO:0000255}. TOPO_DOM 21 91 Extracellular. {ECO:0000255}.; TOPO_DOM 113 280 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays an important role in bone formation and normal bone mineralization (PubMed:26207632, PubMed:22416756, PubMed:20025746). Promotes the differentiation of myoblasts into osteoblasts (PubMed:22416756, PubMed:20025746, PubMed:22579779). May induce the commitment and differentiation of myoblasts into osteoblasts through an enhancement of BMP2 production and interaction with the BMP-RUNX2 pathway (PubMed:21239498, PubMed:22579779). Upregulates the expression of ATF4 which plays a central role in osteoblast differentiation (PubMed:24362451). Essential for normal spermatogenesis and late testicular differentiation (PubMed:26207632). {ECO:0000269|PubMed:20025746, ECO:0000269|PubMed:21239498, ECO:0000269|PubMed:22416756, ECO:0000269|PubMed:22579779, ECO:0000269|PubMed:24362451, ECO:0000269|PubMed:26207632}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20025746}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:21239498}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:21239498}. SUBUNIT: Interacts with SMAD1, SMAD5 and RUNX2. {ECO:0000269|PubMed:21239498}. TISSUE SPECIFICITY: Expressed in spermatocytes and spermatids in the developing testis (at protein level). Expressed in the brain, heart, lung, spleen, skeletal muscle, ovary, testis and epididymis (PubMed:26207632). Predominantly expressed in osteoblasts (PubMed:20025746). {ECO:0000269|PubMed:20025746, ECO:0000269|PubMed:26207632}. +Q3UQ41 TM11A_MOUSE Transmembrane protease serine 11A (EC 3.4.21.-) (Airway trypsin-like protease 1) (Serine protease DESC3) (DESC-3) 389 43,605 Active site (3); Chain (1); Disulfide bond (3); Domain (2); Glycosylation (1); Topological domain (2); Transmembrane (1) TRANSMEM 24 44 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 23 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 45 389 Extracellular. {ECO:0000255}. FUNCTION: Probable serine protease which may play a role in cellular senescence. Overexpression inhibits cell growth and induce G1 cell cycle arrest. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. +Q9D6G5 TM138_MOUSE Transmembrane protein 138 162 19,150 Alternative sequence (2); Chain (1); Glycosylation (1); Transmembrane (4) TRANSMEM 7 27 Helical. {ECO:0000255}.; TRANSMEM 41 61 Helical. {ECO:0000255}.; TRANSMEM 80 100 Helical. {ECO:0000255}.; TRANSMEM 115 134 Helical. {ECO:0000255}. FUNCTION: Required for ciliogenesis. {ECO:0000250}. SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell projection, cilium {ECO:0000250}. Note=Localizes to vesicles en route to the base of cilium. {ECO:0000250}. +Q8R4P5 TMC1_MOUSE Transmembrane channel-like protein 1 (Beethoven protein) (Deafness protein) (Transmembrane cochlear-expressed protein 1) 757 87,264 Alternative sequence (3); Chain (1); Compositional bias (2); Natural variant (1); Topological domain (7); Transmembrane (6) TRANSMEM 194 214 Helical. {ECO:0000255}.; TRANSMEM 267 287 Helical. {ECO:0000255}.; TRANSMEM 360 380 Helical. {ECO:0000255}.; TRANSMEM 435 455 Helical. {ECO:0000255}.; TRANSMEM 632 652 Helical. {ECO:0000255}.; TRANSMEM 697 717 Helical. {ECO:0000255}. TOPO_DOM 1 193 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 215 266 Extracellular. {ECO:0000255}.; TOPO_DOM 288 359 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 381 434 Extracellular. {ECO:0000255}.; TOPO_DOM 456 631 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 653 696 Extracellular. {ECO:0000255}.; TOPO_DOM 718 757 Cytoplasmic. {ECO:0000255}. FUNCTION: Probable ion channel required for the normal function of cochlear hair cells. {ECO:0000269|PubMed:11850618}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25114259, ECO:0000269|PubMed:28534737}; Multi-pass membrane protein {ECO:0000305}. Note=Localized to the stereocilia of the cochlear hair cells. {ECO:0000269|PubMed:28504928}. SUBUNIT: Interacts with TOMT. The interaction of TMC1 and TMC2 with TOMT is required for the transportation of TMC1/2 into the stereocilia of hair cells. Interacts (via N-terminus) with both isoforms CD1 and CD3 of PCDH15. {ECO:0000269|PubMed:28504928, ECO:0000269|PubMed:28534737}. TISSUE SPECIFICITY: Detected in cochlear inner and outer hair cells and in neurosensory epithelia of the vestibular end organs. Also expressed in cortex, cerebellum, eye, colon, ovary and testis. {ECO:0000269|PubMed:12812529}. DISEASE: Note=Defects in Tmc1 are the cause of the dominant deaf mutant Beethoven (BTH). Heterozygotes show progressive hair-cell degeneration from day 20 onwards, leading to severe depletion of inner hair cells and scattered loss of outer hair cells, and progressive loss of the Preyer reflex from around day 30. Homozygotes show almost complete degeneration of inner hair cells, and little or no Preyer reflex at any age.; DISEASE: Note=Defects in Tmc1 are the cause of recessive deaf mutant dn. The dn mutant shows profound deafness with degeneration of the organ of Corti, stria vascularis, and occasionally the saccular macula, starting at about 10 days after birth (PubMed:11850618). {ECO:0000269|PubMed:11850618}. +A7E1Z1 TM215_MOUSE Transmembrane protein 215 235 25,812 Chain (1); Sequence conflict (1); Transmembrane (2) TRANSMEM 12 32 Helical. {ECO:0000255}.; TRANSMEM 40 60 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q3TYP4 TM88B_MOUSE Transmembrane protein 88B 173 18,549 Chain (1); Sequence conflict (4); Transmembrane (3) TRANSMEM 31 51 Helical. {ECO:0000255}.; TRANSMEM 53 73 Helical. {ECO:0000255}.; TRANSMEM 107 127 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q32NZ6 TMC5_MOUSE Transmembrane channel-like protein 5 967 111,070 Alternative sequence (2); Chain (1); Sequence conflict (6); Topological domain (11); Transmembrane (10) TRANSMEM 421 441 Helical. {ECO:0000255}.; TRANSMEM 450 470 Helical. {ECO:0000255}.; TRANSMEM 488 508 Helical. {ECO:0000255}.; TRANSMEM 582 602 Helical. {ECO:0000255}.; TRANSMEM 617 637 Helical. {ECO:0000255}.; TRANSMEM 661 681 Helical. {ECO:0000255}.; TRANSMEM 695 715 Helical. {ECO:0000255}.; TRANSMEM 750 770 Helical. {ECO:0000255}.; TRANSMEM 797 817 Helical. {ECO:0000255}.; TRANSMEM 862 882 Helical. {ECO:0000255}. TOPO_DOM 1 420 Extracellular. {ECO:0000255}.; TOPO_DOM 442 449 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 471 487 Extracellular. {ECO:0000255}.; TOPO_DOM 509 581 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 603 616 Extracellular. {ECO:0000255}.; TOPO_DOM 638 660 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 682 694 Extracellular. {ECO:0000255}.; TOPO_DOM 716 749 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 771 796 Extracellular. {ECO:0000255}.; TOPO_DOM 818 861 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 883 967 Extracellular. {ECO:0000255}. FUNCTION: Probable ion channel. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:12812529}. +Q8R1J1 TM6S2_MOUSE Transmembrane 6 superfamily member 2 378 43,027 Alternative sequence (1); Chain (1); Domain (2); Sequence conflict (2); Transmembrane (10) TRANSMEM 10 30 Helical; Name=1. {ECO:0000255}.; TRANSMEM 34 54 Helical; Name=2. {ECO:0000255}.; TRANSMEM 63 83 Helical; Name=3. {ECO:0000255}.; TRANSMEM 110 130 Helical; Name=4. {ECO:0000255}.; TRANSMEM 140 160 Helical; Name=5. {ECO:0000255}.; TRANSMEM 170 190 Helical; Name=6. {ECO:0000255}.; TRANSMEM 219 239 Helical; Name=7. {ECO:0000255}.; TRANSMEM 269 289 Helical; Name=8. {ECO:0000255}.; TRANSMEM 291 311 Helical; Name=9. {ECO:0000255}.; TRANSMEM 332 352 Helical; Name=10. {ECO:0000255}. FUNCTION: Regulator of liver fat metabolism influencing triglyceride secretion and hepatic lipid droplet content. May function as sterol isomerase. {ECO:0000250|UniProtKB:Q9BZW4, ECO:0000269|PubMed:24531328, ECO:0000269|PubMed:24633158}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9BZW4}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q9BZW4}; Multi-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Highly expressed in the liver at both the mRNA and protein levels. {ECO:0000269|PubMed:24633158}. +Q8R182 TMG2_MOUSE Transmembrane gamma-carboxyglutamic acid protein 2 (NEDD4 WW domain-binding protein 1) (Proline-rich gamma-carboxyglutamic acid protein 2) (Proline-rich Gla protein 2) 198 22,369 Chain (1); Disulfide bond (1); Domain (1); Mutagenesis (1); Propeptide (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 112 134 Helical. {ECO:0000255}. TOPO_DOM 52 111 Extracellular. {ECO:0000255}.; TOPO_DOM 135 198 Cytoplasmic. {ECO:0000255}. PTM: Gla residues are produced after subsequent post-translational modifications of glutamate by a vitamin K-dependent gamma-carboxylase. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Interacts with NEDD4. {ECO:0000269|PubMed:11042109}. +Q9CR22 TMM42_MOUSE Transmembrane protein 42 157 16,636 Chain (1); Transmembrane (4) TRANSMEM 37 57 Helical. {ECO:0000255}.; TRANSMEM 67 87 Helical. {ECO:0000255}.; TRANSMEM 100 120 Helical. {ECO:0000255}.; TRANSMEM 124 144 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9D702 TMM52_MOUSE Transmembrane protein 52 196 21,052 Chain (1); Signal peptide (1); Transmembrane (1) TRANSMEM 47 67 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q7TS55 TNF18_MOUSE Tumor necrosis factor ligand superfamily member 18 (GITR ligand) (GITRL) (Glucocorticoid-induced TNF-related ligand) 173 19,732 Beta strand (11); Chain (1); Disulfide bond (1); Glycosylation (1); Helix (2); Sequence conflict (6); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 21 41 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 20 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 42 173 Extracellular. {ECO:0000255}. FUNCTION: Cytokine that binds to TNFRSF18/AITR/GITR (PubMed:14521928, PubMed:14647196). Regulates T-cell responses (PubMed:14647196). Can function as costimulator and lower the threshold for T-cell activation and T-cell proliferation (PubMed:14608036, PubMed:15128759). Important for interactions between activated T-lymphocytes and endothelial cells. Mediates activation of NF-kappa-B (PubMed:14521928, PubMed:14647196, PubMed:18178614). Triggers increased phosphorylation of STAT1 and up-regulates expression of VCAM1 and ICAM1 (By similarity). Promotes leukocyte adhesion to endothelial cells (PubMed:23892569). Regulates migration of monocytes from the splenic reservoir to sites of inflammation (PubMed:24107315). {ECO:0000250|UniProtKB:Q9UNG2, ECO:0000269|PubMed:14521928, ECO:0000269|PubMed:14608036, ECO:0000269|PubMed:14647196, ECO:0000269|PubMed:15128759, ECO:0000269|PubMed:18178614, ECO:0000269|PubMed:23892569, ECO:0000269|PubMed:24107315}. PTM: N-glycosylated. {ECO:0000269|PubMed:19390148}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14521928, ECO:0000269|PubMed:14608036}; Single-pass type II membrane protein {ECO:0000269|PubMed:14521928, ECO:0000269|PubMed:14608036}. SUBUNIT: Homotrimer. Homodimer. {ECO:0000269|PubMed:15128759, ECO:0000269|PubMed:18178614, ECO:0000269|PubMed:18182486, ECO:0000269|PubMed:19390148}. TISSUE SPECIFICITY: Detected in immature and mature dendritic cells and in macrophages (at protein level). Detected in spleen, lung, heart, thymus, monocytes, macrophages, B-cells and dendritic cells. {ECO:0000269|PubMed:14521928, ECO:0000269|PubMed:14608036, ECO:0000269|PubMed:14647196}. +Q8BK08 TMM11_MOUSE Transmembrane protein 11, mitochondrial (Protein PM1) 190 21,312 Chain (1); Erroneous gene model prediction (1); Transmembrane (2) TRANSMEM 84 100 Helical. {ECO:0000255}.; TRANSMEM 107 124 Helical. {ECO:0000255}. FUNCTION: Plays a role in mitochondrial morphogenesis. {ECO:0000250|UniProtKB:P17152}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P17152}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17152}. SUBUNIT: Associates with the mitochondrial contact site and cristae organizing system (MICOS) complex, composed of at least MINOS1/MIC10, CHCHD3/MIC19, CHCHD6/MIC25, APOOL/MIC27, IMMT/MIC60, APOO/MIC23/MIC26 and QIL1/MIC13. This complex was also known under the names MINOS or MitOS complex. The MICOS complex associates with mitochondrial outer membrane proteins SAMM50, MTX1, MTX2 and DNAJC11, mitochondrial inner membrane protein TMEM11 and with HSPA9. Interacts with IMMT/MIC60. {ECO:0000250|UniProtKB:P17152}. +Q99LG2 TNPO2_MOUSE Transportin-2 (Karyopherin beta-2b) 887 100,456 Chain (1); Domain (1); Modified residue (1); Repeat (20); Sequence conflict (1) FUNCTION: Probably functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. +Q9CR75 TNR12_MOUSE Tumor necrosis factor receptor superfamily member 12A (Fibroblast growth factor-inducible immediate-early response protein 14) (FGF-inducible 14) (Fibroblast growth factor-regulated protein 2) (Tweak-receptor) (TweakR) (CD antigen CD266) 129 13,641 Chain (1); Disulfide bond (3); Repeat (1); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 81 101 Helical. {ECO:0000255}. TOPO_DOM 28 80 Extracellular. {ECO:0000255}.; TOPO_DOM 102 129 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for TNFSF12/TWEAK (By similarity). Weak inducer of apoptosis in some cell types. Promotes angiogenesis and the proliferation of endothelial cells. May modulate cellular adhesion to matrix proteins. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Associates with TRAF1 and TRAF2, and probably also with TRAF3. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in fetal heart, intestine, kidney, liver, lung and skin, and in adult heart and ovary. Intermediate expression in adult kidney, lung and skin. +P54797 TNG2_MOUSE Transport and Golgi organization 2 homolog (Ser/Thr-rich protein T10 in DGCR region) 276 30,947 Chain (1) SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:Q6ICL3}. TISSUE SPECIFICITY: Expressed in fetal liver, lung, heart and kidney. {ECO:0000269|PubMed:8268909}. +Q9D4V6 TO20L_MOUSE TOMM20-like protein 1 152 17,580 Chain (1); Topological domain (2); Transmembrane (1) TRANSMEM 7 27 Helical. {ECO:0000255}. TOPO_DOM 1 6 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 28 152 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +J3QMY9 TO6BL_MOUSE Type 2 DNA topoisomerase 6 subunit B-like (Type 2 DNA topoisomerase VI subunit B-like) (TOPOVIBL) 579 63,797 Alternative sequence (2); Chain (1) FUNCTION: Component of a topoisomerase 6 complex specifically required for meiotic recombination. Together with SPO11, mediates DNA cleavage that forms the double-strand breaks (DSB) that initiate meiotic recombination. The complex promotes relaxation of negative and positive supercoiled DNA and DNA decatenation through cleavage and ligation cycles. {ECO:0000269|PubMed:26917764}. SUBCELLULAR LOCATION: Chromosome {ECO:0000305}. Note=Localizes to meiotic chromosomes. {ECO:0000305}. SUBUNIT: Heterotetramer of SPO11 and 2 TOP6BL chains (Probable). Interacts with SPO11 (PubMed:26917764). {ECO:0000269|PubMed:26917764, ECO:0000305}. DOMAIN: Despite a weak sequence similarity, retains most of the structural features of the ancestral archaeal Top6B subunit (AC O05207), including the transducer domain that interacts with the SPO11 subunit and the ATP-binding fold, also named GHKL fold. {ECO:0000269|PubMed:26917764}. TISSUE SPECIFICITY: In males, expressed in testis but not in other tissues. Expressed in testis from 8 days postpartum (dpp) onward, with a peak of expression around 12 to 14 dpp, at the beginning of meiotic prophase. In females, expressed in embryonic ovaries when oocytes proceed through meiotic prophase (PubMed:26917764). {ECO:0000269|PubMed:26917764}. +P83510 TNIK_MOUSE Traf2 and NCK-interacting protein kinase (EC 2.7.11.1) 1323 150,367 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Domain (2); Modified residue (20); Nucleotide binding (1); Region (1); Sequence caution (1); Sequence conflict (1) FUNCTION: Serine/threonine kinase that acts as an essential activator of the Wnt signaling pathway. Recruited to promoters of Wnt target genes and required to activate their expression. May act by phosphorylating TCF4/TCF7L2. Appears to act upstream of the JUN N-terminal pathway. May play a role in the response to environmental stress. Part of a signaling complex composed of NEDD4, RAP2A and TNIK which regulates neuronal dendrite extension and arborization during development. More generally, it may play a role in cytoskeletal rearrangements and regulate cell spreading (By similarity). {ECO:0000250}. PTM: Autophosphorylated. Autophosphorylation is activated by RAP2A and induces association to the cytoskeletal fraction. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19816403}. Cytoplasm {ECO:0000269|PubMed:19816403}. Recycling endosome {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Associated with recycling endosomes and the cytoskeletal fraction upon RAP2A overexpression. {ECO:0000250}. SUBUNIT: Interacts (via the CNH domain) with RAP2A (GTP-bound form preferentially); the interaction is direct and required for the activation of TNIK by RAP2A. Interacts with NEDD4; recruits RAP2A to NEDD4. Interacts with TRAF2 and NCK. Interacts with TCF7L2/TCF4 and CTNNB1; the interaction is direct. Interacts with TANC1. {ECO:0000269|PubMed:19816403, ECO:0000269|PubMed:20159449}. +P25446 TNR6_MOUSE Tumor necrosis factor receptor superfamily member 6 (Apo-1 antigen) (Apoptosis-mediating surface antigen FAS) (FASLG receptor) (CD antigen CD95) 327 37,437 Chain (1); Disulfide bond (9); Domain (1); Glycosylation (2); Helix (2); Modified residue (4); Natural variant (1); Region (2); Repeat (3); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 170 186 Helical. {ECO:0000255}. TOPO_DOM 22 169 Extracellular. {ECO:0000255}.; TOPO_DOM 187 327 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for TNFSF6/FASLG. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. FAS-mediated apoptosis may have a role in the induction of peripheral tolerance, in the antigen-stimulated suicide of mature T-cells, or both (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P51867}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P51867}. SUBUNIT: Binds DAXX (PubMed:9215629). Interacts with HIPK3 (PubMed:11034606). Part of a complex containing HIPK3 and FADD (By similarity). Binds RIPK1 and FAIM2. Interacts with BABAM2 and FEM1B. Interacts with FADD (By similarity). Interacts directly (via DED domain) with NOL3 (via CARD domain); inhibits death-inducing signaling complex (DISC) assembly by inhibiting the increase in FAS-FADD binding induced by FAS activation (PubMed:15383280). Interacts with CALM (By similarity). {ECO:0000250|UniProtKB:P25445, ECO:0000269|PubMed:11034606, ECO:0000269|PubMed:15383280, ECO:0000269|PubMed:9215629}. DOMAIN: Contains a death domain involved in the binding of FADD, and maybe to other cytosolic adapter proteins. TISSUE SPECIFICITY: Detected in various tissues including thymus, liver, lung, heart, and adult ovary. {ECO:0000269|PubMed:1371136}. DISEASE: Note=Defects in Fas are the cause of the lymphoproliferation phenotype (lpr). Lpr mice show lymphadenopathy and autoantibody production. +Q9DCC8 TOM20_MOUSE Mitochondrial import receptor subunit TOM20 homolog (Mitochondrial 20 kDa outer membrane protein) (Outer mitochondrial membrane receptor Tom20) 145 16,284 Chain (1); Cross-link (4); Modified residue (2); Topological domain (2); Transmembrane (1) TRANSMEM 7 24 Helical. {ECO:0000255}. TOPO_DOM 1 6 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 25 145 Cytoplasmic. {ECO:0000255}. FUNCTION: Central component of the receptor complex responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. Together with TOM22 functions as the transit peptide receptor at the surface of the mitochondrion outer membrane and facilitates the movement of preproteins into the TOM40 translocation pore (By similarity). {ECO:0000250}. PTM: Ubiquitinated by PRKN during mitophagy, leading to its degradation and enhancement of mitophagy. Deubiquitinated by USP30. {ECO:0000250|UniProtKB:Q15388}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q15388}; Single-pass membrane protein {ECO:0000255}. SUBUNIT: Forms part of the preprotein translocase complex of the outer mitochondrial membrane (TOM complex) which consists of at least 7 different proteins (TOMM5, TOMM6, TOMM7, TOMM20, TOMM22, TOMM40 and TOMM70). Interacts with TOM22. Interacts with APEX1 (By similarity). {ECO:0000250}. +B1AXP6 TOM5_MOUSE Mitochondrial import receptor subunit TOM5 homolog 51 6,037 Alternative sequence (3); Chain (1); Cross-link (1); Modified residue (1); Transmembrane (1) TRANSMEM 27 45 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q8N4H5}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8N4H5}. SUBUNIT: Forms part of the preprotein translocase complex of the outer mitochondrial membrane (TOM complex) which consists of at least 7 different proteins (TOMM5, TOMM6, TOMM7, TOMM20, TOMM22, TOMM40 and TOMM70). {ECO:0000250|UniProtKB:Q8N4H5}. +Q9CPQ3 TOM22_MOUSE Mitochondrial import receptor subunit TOM22 homolog (Translocase of outer membrane 22 kDa subunit homolog) 142 15,537 Chain (1); Compositional bias (2); Initiator methionine (1); Modified residue (4); Region (3); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 84 103 Helical. {ECO:0000255}. TOPO_DOM 2 83 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 104 142 Mitochondrial intermembrane. {ECO:0000255}. FUNCTION: Central receptor component of the translocase of the outer membrane of mitochondria (TOM complex) responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. Together with the peripheral receptor TOM20 functions as the transit peptide receptor and facilitates the movement of preproteins into the translocation pore (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. SUBUNIT: Forms part of the preprotein translocase complex of the outer mitochondrial membrane (TOM complex) which consists of at least 7 different proteins (TOMM5, TOMM6, TOMM7, TOMM20, TOMM22, TOMM40 and TOMM70). Interacts with PPP2R2B and TOMM40 (By similarity). {ECO:0000250}. DOMAIN: The N-terminal domain (residues 1-62) is important for binding to the unfolded mature imported proteins. Residues (49-71) of the cytoplasmic domain interacts with TOMM20 while the C-terminal segment (residues 63-82) binds presequence of preproteins. Requires the transmembrane domain (TMD), a short segment (the import sequence) in the cytoplasmic domain localizing separately from the TMD and the C-tail signal in the C-terminal domain for efficient targeting and integration into the TOM complex (By similarity). {ECO:0000250}. +Q9QYA2 TOM40_MOUSE Mitochondrial import receptor subunit TOM40 homolog (Mitochondrial outer membrane protein of 35 kDa) (MOM35) (Protein Haymaker) (Translocase of outer membrane 40 kDa subunit homolog) 361 37,895 Chain (1); Compositional bias (1); Frameshift (1); Sequence conflict (5) FUNCTION: Channel-forming protein essential for import of protein precursors into mitochondria. {ECO:0000250|UniProtKB:O96008}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:O96008}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Forms part of the preprotein translocase complex of the outer mitochondrial membrane (TOM complex) which consists of at least 7 different proteins (TOMM5, TOMM6, TOMM7, TOMM20, TOMM22, TOMM40 and TOMM70). Interacts with mitochondrial targeting sequences. Interacts with TIMM29; linking the TIM22 complex to the TOM complex. {ECO:0000250|UniProtKB:O96008}. +Q8R1J9 TOR2A_MOUSE Torsin-2A (Torsin family 2 member A) 321 35,897 Alternative sequence (1); Chain (1); Glycosylation (1); Mutagenesis (1); Nucleotide binding (1); Signal peptide (1) PTM: N-glycosylated. {ECO:0000269|PubMed:20015956}. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000269|PubMed:20015956}. SUBUNIT: Homohexamer. Interacts with TOR1AIP1. {ECO:0000269|PubMed:16364897, ECO:0000269|PubMed:20015956}. TISSUE SPECIFICITY: Expressed at similar levels in liver, muscle and brain (at protein level). {ECO:0000269|PubMed:20015956}. +E5FYH1 TOPZ1_MOUSE Protein TOPAZ1 (Testis- and ovary-specific PAZ domain-containing protein 1) 1653 185,487 Chain (1) FUNCTION: Important for normal spermatogenesis and male fertility. Specifically required for progression to the post-meiotic stages of spermatocyte development. Seems to be necessary for normal expression levels of a number of testis-expressed gene transcripts, although its role in this process is unclear. {ECO:0000269|PubMed:26358182}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:22069478}. TISSUE SPECIFICITY: Restricted to testis, where it localizes to germ cells. {ECO:0000269|PubMed:22069478, ECO:0000269|PubMed:26358182}. +P70399 TP53B_MOUSE TP53-binding protein 1 (53BP1) (p53-binding protein 1) (p53BP1) 1969 212,735 Alternative sequence (2); Beta strand (11); Chain (1); Compositional bias (6); Cross-link (9); Domain (2); Erroneous initiation (1); Helix (2); Modified residue (66); Motif (2); Region (2); Sequence conflict (12); Turn (4) FUNCTION: Double-strand break (DSB) repair protein involved in response to DNA damage, telomere dynamics and class-switch recombination (CSR) during antibody genesis (PubMed:15159415, PubMed:15077110, PubMed:20453858, PubMed:23333305, PubMed:26308889, PubMed:20362325). Plays a key role in the repair of double-strand DNA breaks (DSBs) in response to DNA damage by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs and specifically counteracting the function of the homologous recombination (HR) repair protein BRCA1 (PubMed:23333305, PubMed:20362325). In response to DSBs, phosphorylation by ATM promotes interaction with RIF1 and dissociation from NUDT16L1/TIRR, leading to recruitment to DSBs sites. Recruited to DSBs sites by recognizing and binding histone H2A monoubiquitinated at 'Lys-15' (H2AK15Ub) and histone H4 dimethylated at 'Lys-20' (H4K20me2), two histone marks that are present at DSBs sites. Required for immunoglobulin class-switch recombination (CSR) during antibody genesis, a process that involves the generation of DNA DSBs (PubMed:15159415, PubMed:15077110). Participates to the repair and the orientation of the broken DNA ends during CSR (PubMed:26308889). In contrast, it is not required for classic NHEJ and V(D)J recombination (PubMed:15159415). Promotes NHEJ of dysfunctional telomeres (By similarity). {ECO:0000250|UniProtKB:Q12888, ECO:0000269|PubMed:15077110, ECO:0000269|PubMed:15159415, ECO:0000269|PubMed:20362325, ECO:0000269|PubMed:20453858, ECO:0000269|PubMed:23333305, ECO:0000269|PubMed:26308889}. PTM: Phosphorylated at basal level in the absence of DNA damage (By similarity). Phosphorylated by ATM in response to DNA damage: phosphorylation at different sites promotes interaction with different set of proteins: phosphorylation at the N-terminus by ATM (residues from 11-181) promotes interaction with PAXIP1 and non-homologous end joining (NHEJ) of dysfunctional telomeres (By similarity). Phosphorylation by ATM at residues that are located more C-terminus (residues 300-650) leads to promote interaction with RIF1 (PubMed:23333305, PubMed:23306439). Interaction with RIF1 leads to disrupt interaction with NUDT16L1/TIRR (By similarity). Phosphorylation at Thr-1606 and Ser-1615 in the UDR motif blocks interaction with H2AK15ub (By similarity). Dephosphorylated by PPP4C (By similarity). Hyperphosphorylation during mitosis correlates with its exclusion from chromatin and DNA lesions (By similarity). Hyperphosphorylated in an ATR-dependent manner in response to DNA damage induced by UV irradiation (By similarity). Dephosphorylated by PPP5C (By similarity). {ECO:0000250|UniProtKB:Q12888, ECO:0000269|PubMed:23306439, ECO:0000269|PubMed:23333305}.; PTM: Asymmetrically dimethylated on Arg residues by PRMT1. Methylation is required for DNA binding. {ECO:0000250|UniProtKB:Q12888}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11801725}. Chromosome {ECO:0000269|PubMed:11673449, ECO:0000269|PubMed:23209566, ECO:0000269|PubMed:23306439, ECO:0000269|PubMed:23333305}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:11801725}. Note=Localizes to the nucleus in absence of DNA damage (PubMed:11801725). Following DNA damage, recruited to sites of DNA damage, such as double stand breaks (DSBs) (PubMed:11673449, PubMed:23209566, PubMed:23333305, PubMed:23306439). Recognizes and binds histone H2A monoubiquitinated at 'Lys-15' (H2AK15Ub) and histone H4 dimethylated at 'Lys-20' (H4K20me2), two histone marks that are present at DSBs sites (PubMed:23209566). Associated with kinetochores during mitosis (PubMed:11801725). {ECO:0000269|PubMed:11673449, ECO:0000269|PubMed:11801725, ECO:0000269|PubMed:23209566, ECO:0000269|PubMed:23306439, ECO:0000269|PubMed:23333305}. SUBUNIT: Homoligomer (By similarity). Interacts with p53/TP53 (via the central domain) (By similarity). Interacts with DCLRE1C (By similarity). Interacts with histone H2AFX and this requires phosphorylation of H2AFX on 'Ser-139' (By similarity). Interacts with histone H4 that has been dimethylated at 'Lys-20' (H4K20me2) (PubMed:23209566). Has low affinity for histone H4 containing monomethylated 'Lys-20' (H4K20me1) (By similarity). Does not bind histone H4 containing unmethylated or trimethylated 'Lys-20' (H4K20me3) (By similarity). Has low affinity for histone H3 that has been dimethylated on 'Lys-79' (By similarity). Has very low affinity for histone H3 that has been monomethylated on 'Lys-79' (in vitro) (By similarity). Does not bind unmethylated histone H3 (By similarity). Interacts with histone H2A monoubiquitinated at 'Lys-15' (H2AK15Ub) (By similarity). Interacts with PWWP3A/EXPAND1 (By similarity). Interacts with CHEK2; modulates CHEK2 phosphorylation at 'Thr-68' in response to infrared (By similarity). Interacts with MSL1; this interaction may be required for MSL1 DNA repair activity, but not for histone acetyltransferase activity (By similarity). Interacts (when phosphorylated by ATM) with RIF1 (PubMed:23333305, PubMed:23306439). Interacts (via the Tudor-like domain) with NUDT16L1/TIRR; interaction masks the Tudor-like domain and prevents recruitment to chromatin (By similarity). Interacts with PAXIP1 (By similarity). Interacts with IFI202A (PubMed:8910340). Interacts with SHLD2 (By similarity). {ECO:0000250|UniProtKB:Q12888, ECO:0000269|PubMed:23209566, ECO:0000269|PubMed:23306439, ECO:0000269|PubMed:23333305, ECO:0000269|PubMed:8910340}. DOMAIN: The Tudor-like region mediates binding to histone H4 dimethylated at 'Lys-20' (H4K20me2) (PubMed:23209566). Interaction with NUDT16L1/TIRR masks the Tudor-like domain and prevents recruitment to chromatin (By similarity). {ECO:0000250|UniProtKB:Q12888, ECO:0000269|PubMed:23209566}.; DOMAIN: The UDR (ubiquitin-dependent recruitment) motif specifically recognizes and binds histone H2A monoubiquitinated at 'Lys-15' (H2AK15ub). Phosphorylation of the UDR blocks interaction with H2AK15ub. {ECO:0000250|UniProtKB:Q12888}. +Q0P5Y3 TPPP2_MOUSE Tubulin polymerization-promoting protein family member 2 170 18,681 Chain (1) FUNCTION: May bind tubulin but has no microtubule bundling activity. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. +A2APB8 TPX2_MOUSE Targeting protein for Xklp2 745 85,894 Chain (1); Cross-link (4); Modified residue (13); Mutagenesis (1); Sequence conflict (3) FUNCTION: Spindle assembly factor required for normal assembly of mitotic spindles. Required for normal assembly of microtubules during apoptosis. Required for chromatin and/or kinetochore dependent microtubule nucleation. Mediates AURKA localization to spindle microtubules. Activates AURKA by promoting its autophosphorylation at 'Thr-288' and protects this residue against dephosphorylation. TPX2 is inactivated upon binding to importin-alpha. At the onset of mitosis, GOLGA2 interacts with importin-alpha, liberating TPX2 from importin-alpha, allowing TPX2 to activates AURKA kinase and stimulates local microtubule nucleation. {ECO:0000250|UniProtKB:Q9ULW0, ECO:0000269|PubMed:18663142}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9ULW0}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9ULW0}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q9ULW0}. Note=During mitosis it is strictly associated with the spindle pole and with the mitotic spindle, whereas during S and G2, it is diffusely distributed throughout the nucleus. Is released from the nucleus in apoptotic cells and is detected on apoptotic microtubules. {ECO:0000250|UniProtKB:Q9ULW0}. SUBUNIT: Interacts with AURKA (PubMed:18663142). Interacts with importin-alpha; leading to inactivate TPX2 (By similarity). Interacts with HNRNPU; this interaction recruits HNRNPU to spindle microtubules (MTs) (By similarity). {ECO:0000250|UniProtKB:Q9ULW0, ECO:0000269|PubMed:18663142}. +Q9JKA3 TR103_MOUSE Taste receptor type 2 member 103 (T2R103) (Taste receptor family B member 2) (TRB2) (Taste receptor type 2 member 10) (T2R10) 312 35,156 Chain (1); Glycosylation (1); Sequence conflict (11); Topological domain (8); Transmembrane (7) TRANSMEM 7 27 Helical; Name=1. {ECO:0000255}.; TRANSMEM 62 82 Helical; Name=2. {ECO:0000255}.; TRANSMEM 93 113 Helical; Name=3. {ECO:0000255}.; TRANSMEM 133 153 Helical; Name=4. {ECO:0000255}.; TRANSMEM 186 206 Helical; Name=5. {ECO:0000255}.; TRANSMEM 230 250 Helical; Name=6. {ECO:0000255}.; TRANSMEM 265 285 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 6 Extracellular. {ECO:0000255}.; TOPO_DOM 28 61 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 83 92 Extracellular. {ECO:0000255}.; TOPO_DOM 114 132 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 154 185 Extracellular. {ECO:0000255}.; TOPO_DOM 207 229 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 251 264 Extracellular. {ECO:0000255}.; TOPO_DOM 286 312 Cytoplasmic. {ECO:0000255}. FUNCTION: Gustducin-coupled receptor implicated in the perception of bitter compounds in the oral cavity and the gastrointestinal tract. Signals through PLCB2 and the calcium-regulated cation channel TRPM5. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed in subsets of taste receptor cells of the tongue and palate epithelium and exclusively in gustducin-positive cells. Expressed in 15% taste bud cells in circumvallate and foliate papillae but only in 2% in fungiform papillae. +Q7M725 TR107_MOUSE Taste receptor type 2 member 107 (T2R107) (mT2R43) (STC5-1) (T2R4) 308 35,427 Chain (1); Glycosylation (3); Sequence conflict (5); Topological domain (8); Transmembrane (7) TRANSMEM 8 28 Helical; Name=1. {ECO:0000255}.; TRANSMEM 44 64 Helical; Name=2. {ECO:0000255}.; TRANSMEM 88 108 Helical; Name=3. {ECO:0000255}.; TRANSMEM 126 146 Helical; Name=4. {ECO:0000255}.; TRANSMEM 181 201 Helical; Name=5. {ECO:0000255}.; TRANSMEM 233 253 Helical; Name=6. {ECO:0000255}.; TRANSMEM 259 279 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 7 Extracellular. {ECO:0000255}.; TOPO_DOM 29 43 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 65 87 Extracellular. {ECO:0000255}.; TOPO_DOM 109 125 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 147 180 Extracellular. {ECO:0000255}.; TOPO_DOM 202 232 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 254 258 Extracellular. {ECO:0000255}.; TOPO_DOM 280 308 Cytoplasmic. {ECO:0000255}. FUNCTION: Putative taste receptor which may play a role in the perception of bitterness. {ECO:0000305}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +O88413 TULP3_MOUSE Tubby-related protein 3 (Tubby-like protein 3) 460 51,231 Chain (1) FUNCTION: Negative regulator of the Shh signaling transduction pathway: recruited to primary cilia via association with the IFT complex A (IFT-A) and is required for recruitment of G protein-coupled receptor GPR161 to cilia, a promoter of PKA-dependent basal repression machinery in Shh signaling. Binds to phosphorylated inositide (phosphoinositide) lipids. Both IFT-A- and phosphoinositide-binding properties are required to regulate ciliary G protein-coupled receptor trafficking. Not involved in ciliogenesis. {ECO:0000269|PubMed:19286674, ECO:0000269|PubMed:19334287}. SUBCELLULAR LOCATION: Nucleus. Cell membrane. Cell projection, cilium. Cytoplasm. Secreted. Note=Translocates from the plasma membrane to the nucleus upon activation of guanine nucleotide-binding protein G(q) subunit alpha (By similarity). Does not have a cleavable signal peptide and is secreted by a non-conventional pathway. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed including eyes and adipose depots. {ECO:0000269|PubMed:9828123}. +Q9DBG9 TX1B3_MOUSE Tax1-binding protein 3 (Tax interaction protein 1) (TIP-1) 124 13,723 Beta strand (8); Chain (1); Domain (1); Helix (5); Initiator methionine (1); Modified residue (2) FUNCTION: May regulate a number of protein-protein interactions by competing for PDZ domain binding sites. Binds CTNNB1 and may thereby act as an inhibitor of the Wnt signaling pathway. Competes with LIN7A for KCNJ4 binding, and thereby promotes KCNJ4 internalization. May play a role in the Rho signaling pathway (By similarity). {ECO:0000250, ECO:0000269|PubMed:12874278}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12874278}. Nucleus {ECO:0000269|PubMed:12874278}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Recruited to the cell membrane by interaction with membrane proteins. {ECO:0000250}. SUBUNIT: Interacts (via its PDZ domain) with GLS2. Interacts (via its PDZ domain) with RTKN (via the C-terminal region); this interaction facilitates Rho-mediated activation of the FOS serum response element (SRE). Interacts (via PDZ domain) with ARHGEF16. Interacts (via PDZ domain) with KCNJ4 (via C-terminus). Competes with LIN7A for KCNJ4 binding (By similarity). Interacts (via its PDZ domain) with CTNNB1; this interaction inhibits the transcriptional activity of CTNNB1. Interacts with ADGRB2 (By similarity). {ECO:0000250|UniProtKB:O14907, ECO:0000269|PubMed:12874278, ECO:0000269|PubMed:18835279}. +Q62302 TX261_MOUSE Protein TEX261 (Testis-expressed protein 261) 196 22,524 Chain (1); Transmembrane (5) TRANSMEM 3 23 Helical. {ECO:0000255}.; TRANSMEM 42 62 Helical. {ECO:0000255}.; TRANSMEM 70 90 Helical. {ECO:0000255}.; TRANSMEM 97 117 Helical. {ECO:0000255}.; TRANSMEM 125 145 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Detected in testis. {ECO:0000269|PubMed:8703127}. +P24529 TY3H_MOUSE Tyrosine 3-monooxygenase (EC 1.14.16.2) (Tyrosine 3-hydroxylase) (TH) 498 55,993 Chain (1); Compositional bias (1); Metal binding (3); Modified residue (4) Catecholamine biosynthesis; dopamine biosynthesis; dopamine from L-tyrosine: step 1/2. FUNCTION: Plays an important role in the physiology of adrenergic neurons. +Q99P25 TXIP1_MOUSE Translin-associated factor X-interacting protein 1 (Trax-interacting protein 1) 704 81,762 Chain (1); Coiled coil (2); Erroneous initiation (1) FUNCTION: Possible role in spermatogenesis. {ECO:0000269|PubMed:12036294}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:12036294}. SUBUNIT: Interacts with TSNAX. {ECO:0000269|PubMed:12036294}. TISSUE SPECIFICITY: Specifically expressed in testes. Predominantly detected in the post-meiotic stages of germ cells. {ECO:0000269|PubMed:12036294}. +Q6PAM1 TXLNA_MOUSE Alpha-taxilin 554 62,369 Alternative sequence (2); Chain (1); Coiled coil (1); Modified residue (3) FUNCTION: May be involved in intracellular vesicle traffic and potentially in calcium-dependent exocytosis in neuroendocrine cells. {ECO:0000250}. SUBUNIT: Binds to the C-terminal coiled coil region of syntaxin family members STX1A, STX3A and STX4A, but not when these proteins are complexed with SNAP25, VAMP2 or STXBP1, suggesting that it interacts with syntaxins that do not form the SNARE complex. {ECO:0000250}. +Q7M764 U17PE_MOUSE Ubiquitin carboxyl-terminal hydrolase 17-like protein E (USP17-E) (EC 3.4.19.12) (Deubiquitinating enzyme 17-like protein 2) (Deubiquitinating protein 3) (DUB-3) (Deubiquitinating protein 6) (Ubiquitin carboxyl-terminal hydrolase 17-like protein 2) (Ubiquitin thioesterase 17-like protein 2) (Ubiquitin-specific-processing protease 17-like protein 2) 540 60,219 Active site (2); Chain (1); Domain (1); Erroneous gene model prediction (1) FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes that may include cell proliferation, progression through the cell cycle, apoptosis, cell migration, and the cellular response to viral infection. {ECO:0000269|PubMed:20228808}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. SUBUNIT: Interacts with SUDS3; the interaction is direct. {ECO:0000250}. +A0PJN4 U2QL1_MOUSE Ubiquitin-conjugating enzyme E2Q-like protein 1 (EC 2.3.2.23) (E2Q-like ubiquitin-conjugating enzyme 1) 161 18,364 Active site (1); Chain (1); Erroneous initiation (2); Sequence conflict (1) Protein modification; protein ubiquitination. FUNCTION: Probable E2 ubiquitin-protein ligase that catalyzes the covalent attachment of ubiquitin to target proteins. May facilitate the monoubiquitination and degradation of MTOR and CCNE1 through interaction with FBXW7. {ECO:0000250|UniProtKB:A1L167}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:A1L167}. SUBUNIT: Interacts with FBXW7. {ECO:0000250|UniProtKB:A1L167}. +Q6ZPF3 TIAM2_MOUSE T-lymphoma invasion and metastasis-inducing protein 2 (TIAM-2) (SIF and TIAM1-like exchange factor) 1715 192,567 Alternative sequence (4); Beta strand (8); Chain (1); Coiled coil (1); Compositional bias (2); Domain (5); Erroneous initiation (1); Helix (7); Initiator methionine (1); Lipidation (1); Modified residue (2); Mutagenesis (5); Sequence conflict (13) FUNCTION: Modulates the activity of RHO-like proteins and connects extracellular signals to cytoskeletal activities. Acts as a GDP-dissociation stimulator protein that stimulates the GDP-GTP exchange activity of RHO-like GTPases and activates them. Activates specifically RAC1, but not CDC42 and RHOA. Mediates extracellular laminin signals to activate Rac1, contributing to neurite growth. Involved in lamellipodial formation and advancement of the growth cone of embryonic hippocampal neurons. Promotes migration of neurons in the cerebral cortex. When overexpressed, induces membrane ruffling accompanied by the accumulation of actin filaments along the altered plasma membrane. {ECO:0000269|PubMed:10364228, ECO:0000269|PubMed:11707441, ECO:0000269|PubMed:12912917, ECO:0000269|PubMed:14550769, ECO:0000269|PubMed:17320046}. PTM: Phosphorylated on serine and threonine residues. Phosphorylated on Thr-1662 by Rho-kinase. Its phosphorylation by Rho-kinase inhibits its guanine nucleotide exchange activity, its interaction with MAP1A, MAP1B, PARP1 and YWHAE and reduces its ability to promote neurite growth. {ECO:0000269|PubMed:17320046}. SUBCELLULAR LOCATION: Cytoplasm. Cell projection, lamellipodium. Cell projection, filopodium. Cell projection, growth cone. Note=Localizes to the plasma membrane in neurites. SUBUNIT: Interacts with MAP1A, MAP1B, PARP1 and YWHAE. Interacts with CD44, PARD3 and MAPK8IP2. {ECO:0000269|PubMed:17320046, ECO:0000269|PubMed:19893486}. DOMAIN: The PH 1 domain and amino acids 619-780 (a region called TSS; otherwise known as CC-Ex) are necessary for membrane localization. PH 1 and TSS domains are necessary for Rac1 activity. The PH 2 domain is engaged in the enhancement of the catalytic activity of the adjacent DH domain. The PH 1, TSS and DH domains are necessary to induce neurite-like structure. TISSUE SPECIFICITY: Expressed in fetal brain (at protein level). Expressed in the olfactory bulb, cortical plate of the cerebral cortex, caudate putamen, hippocampus, ependymal cells of the lateral surface of the lateral ventricles of the brain. Weakly expressed in heart, lung, liver, skeletal muscle, kidney and testis. {ECO:0000269|PubMed:10364228, ECO:0000269|PubMed:10512681, ECO:0000269|PubMed:11707441, ECO:0000269|PubMed:11900975, ECO:0000269|PubMed:12912917, ECO:0000269|PubMed:14550769}. +Q8BZA9 TIGAR_MOUSE Fructose-2,6-bisphosphatase TIGAR (EC 3.1.3.46) (TP53-induced glycolysis and apoptosis regulator) (TP53-induced glycolysis regulatory phosphatase) 269 29,191 Active site (2); Chain (1); Site (1) FUNCTION: Fructose-bisphosphatase hydrolyzing fructose-2,6-bisphosphate as well as fructose-1,6-bisphosphate (By similarity). Acts as a negative regulator of glycolysis by lowering intracellular levels of fructose-2,6-bisphosphate in a p53/TP53-dependent manner, resulting in the pentose phosphate pathway (PPP) activation and NADPH production (PubMed:23726973). Contributes to the generation of reduced glutathione to cause a decrease in intracellular reactive oxygen species (ROS) content, correlating with its ability to protect cells from oxidative or metabolic stress-induced cell death (PubMed:23726973). Plays a role in promoting protection against cell death during hypoxia by decreasing mitochondria ROS levels in a HK2-dependent manner through a mechanism that is independent of its fructose-bisphosphatase activity (By similarity). In response to cardiac damage stress, mediates p53-induced inhibition of myocyte mitophagy through ROS levels reduction and the subsequent inactivation of BNIP3 (PubMed:22044588). Reduced mitophagy results in an enhanced apoptotic myocyte cell death, and exacerbates cardiac damage (PubMed:22044588). Plays a role in adult intestinal regeneration; contributes to the growth, proliferation and survival of intestinal crypts following tissue ablation (PubMed:23726973). Plays a neuroprotective role against ischemic brain damage by enhancing PPP flux and preserving mitochondria functions (PubMed:24872551). Protects glioma cells from hypoxia- and ROS-induced cell death by inhibiting glycolysis and activating mitochondrial energy metabolism and oxygen consumption in a TKTL1-dependent and p53/TP53-independent manner. Plays a role in cancer cell survival by promoting DNA repair through activating PPP flux in a CDK5-ATM-dependent signaling pathway during hypoxia and/or genome stress-induced DNA damage responses (By similarity). Involved in intestinal tumor progression (PubMed:23726973). {ECO:0000250|UniProtKB:Q9NQ88, ECO:0000269|PubMed:22044588, ECO:0000269|PubMed:23726973, ECO:0000269|PubMed:24872551}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24872551}. Nucleus {ECO:0000250|UniProtKB:Q9NQ88}. Mitochondrion {ECO:0000269|PubMed:24872551}. Note=Translocated to the mitochondria during hypoxia in a HIF1A-dependent manner. Colocalizes with HK2 in the mitochondria during hypoxia. Translocated to the nucleus during hypoxia and/or genome stress-induced DNA damage responses in cancer cells (By similarity). Translocation to the mitochondria is enhanced in ischemic cortex after reperfusion and/or during oxygen and glucose deprivation (OGD)/reoxygenation insult in primary neurons (PubMed:24872551). {ECO:0000250|UniProtKB:Q9NQ88, ECO:0000269|PubMed:24872551}. SUBUNIT: Interacts with HK2; the interaction increases hexokinase HK2 activity in a hypoxia- and HIF1A-dependent manner, resulting in the regulation of mitochondrial membrane potential, thus increasing NADPH production and decreasing intracellular ROS levels. {ECO:0000250|UniProtKB:Q9NQ88}. TISSUE SPECIFICITY: Expressed in olfactory bulb, cerebellum, and cortex (PubMed:24872551). Expressed in neurons and astrocytes (PubMed:24872551) (at protein level). Expressed in intestinal crypt (PubMed:23726973). {ECO:0000269|PubMed:23726973, ECO:0000269|PubMed:24872551}. +Q7TM95 TIGD3_MOUSE Tigger transposable element-derived protein 3 470 52,223 Chain (1); DNA binding (2); Domain (3) SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00320, ECO:0000255|PROSITE-ProRule:PRU00583}. +P62075 TIM13_MOUSE Mitochondrial import inner membrane translocase subunit Tim13 95 10,458 Chain (1); Disulfide bond (2); Modified residue (3); Motif (1); Sequence conflict (2) FUNCTION: Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space. The TIMM8-TIMM13 complex mediates the import of proteins such as TIMM23, SLC25A12/ARALAR1 and SLC25A13/ARALAR2, while the predominant TIMM9-TIMM10 70 kDa complex mediates the import of much more proteins (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Intermembrane side {ECO:0000250}. SUBUNIT: Heterohexamer; composed of 3 copies of TIMM8 (TIMM8A or TIMM8B) and 3 copies of TIMM13, named soluble 70 kDa complex. Associates with the TIM22 complex, whose core is composed of TIMM22 (By similarity). {ECO:0000250}. DOMAIN: The twin CX3C motif contains 4 conserved Cys residues that form 2 disulfide bonds in the mitochondrial intermembrane space. However, during the transit of TIMM13 from cytoplasm into mitochondrion, the Cys residues probably coordinate zinc, thereby preventing folding and allowing its transfer across mitochondrial outer membrane (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Present at high level in liver and brain, and at lower level in muscle and heart. In CNS sections, it is predominantly present in the soma and the dendritic portion of the Purkinje cells of the cerebellum, but not in the glial cells. Scattered expression also is also detected in the brain stem, olfactory bulb, substantia nigra, hippocampus and striatum (at protein level). {ECO:0000269|PubMed:15254020}. +Q9D4D4 TKTL2_MOUSE Transketolase-like protein 2 (EC 2.2.1.1) 627 68,447 Active site (1); Binding site (16); Chain (1); Metal binding (3); Nucleotide binding (1); Sequence conflict (2); Site (2) FUNCTION: Plays an essential role in total transketolase activity and cell proliferation in cancer cells; after transfection with anti-TKTL1 siRNA, total transketolase activity dramatically decreases and proliferation was significantly inhibited in cancer cells. Plays a pivotal role in carcinogenesis (By similarity). {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +Q91W27 TIP39_MOUSE Tuberoinfundibular peptide of 39 residues (TIP39) (Parathyroid hormone 2) 100 11,022 Peptide (1); Propeptide (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Plays a role as a potent and selective agonist of PTH2R resulting in adenyl cyclase activation and intracellular calcium levels elevation. Induces protein kinase C beta activation, recruitment of beta-arrestin and PTH2R internalization. May inhibit cell proliferation via its action of PTH2R activation. Neuropeptide which may also have a role in spermatogenesis. May activate nociceptors and nociceptive circuits. {ECO:0000269|PubMed:11818570, ECO:0000269|PubMed:11861531, ECO:0000269|PubMed:12084532}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Ligand of high affinity for the PTH2 receptor (PTH2R). TISSUE SPECIFICITY: Expressed in testis and, less abundantly, in liver and kidney. Expressed in seminiferous tubuli and several brain regions, including nucleus ruber, caudal paralemniscal nucleus, nucleus centralis pontis, and nucleus subparafascicularis thalami. Expressed in neurons of cerebral cortex and subcortical areas. Expressed in Purkinje cells of cerebellum. {ECO:0000269|PubMed:11818570, ECO:0000269|PubMed:11861531, ECO:0000269|PubMed:12098667}. +Q6PHN7 TM164_MOUSE Transmembrane protein 164 296 33,441 Chain (1); Transmembrane (7) TRANSMEM 40 60 Helical. {ECO:0000255}.; TRANSMEM 92 112 Helical. {ECO:0000255}.; TRANSMEM 125 145 Helical. {ECO:0000255}.; TRANSMEM 149 169 Helical. {ECO:0000255}.; TRANSMEM 171 191 Helical. {ECO:0000255}.; TRANSMEM 209 229 Helical. {ECO:0000255}.; TRANSMEM 261 281 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8BHE4 TM108_MOUSE Transmembrane protein 108 (Retrolinkin) 574 59,642 Chain (1); Compositional bias (1); Region (3); Transmembrane (2) TRANSMEM 9 29 Helical. {ECO:0000255}.; TRANSMEM 468 488 Helical. {ECO:0000255}. FUNCTION: Transmembrane protein required for proper cognitive functions. Involved in the development of dentate gyrus (DG) neuron circuitry, is neccessary for AMPA receptors surface expression and proper excitatory postsynaptic currents of DG granule neurons (PubMed:28096412). Regulates the organization and stability of the microtubule network of sensory neurons to allow axonal transport. Through the interaction with DST, mediates the docking of the dynein/dynactin motor complex to vesicle cargos for retrograde axonal transport (PubMed:17287360). In hippocampal neurons, required for BDNF-dependent dendrite outgrowth (PubMed:21849472). Cooperates with SH3GL2 and recruits the WAVE1 complex to facilitate actin-dependent BDNF:NTRK2 early endocytic trafficking and mediate signaling from early endosomes (PubMed:21849472, PubMed:27605705). {ECO:0000269|PubMed:17287360, ECO:0000269|PubMed:21849472, ECO:0000269|PubMed:27605705, ECO:0000269|PubMed:28096412}. PTM: Glycosylated. {ECO:0000269|PubMed:17287360}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:17287360}; Multi-pass membrane protein {ECO:0000255}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000269|PubMed:28096412}. Endosome membrane {ECO:0000269|PubMed:17287360}. Cell projection, axon {ECO:0000269|PubMed:17287360, ECO:0000269|PubMed:21849472}. Cell projection, dendrite {ECO:0000269|PubMed:21849472}. Early endosome {ECO:0000269|PubMed:21849472}. SUBUNIT: Interacts with DST (isoform 1) (PubMed:17287360). Interacts with SH3GL2 (PubMed:21849472). Interacts (via N-terminus) with CYFIP1 and CYFIP2; the interactions associate TMEM108 with the WAVE1 complex (PubMed:27605705). {ECO:0000269|PubMed:17287360, ECO:0000269|PubMed:21849472, ECO:0000269|PubMed:27605705}. TISSUE SPECIFICITY: Expressed in the nervous system tissues, such as hippocampus and spinal cord, is barely detectable in peripheral tissues such as heart, lung, liver, kidney and muscle (PubMed:17287360, PubMed:28096412). In brain, highly expressed in dentate gyrus neurons and expressed in cortex, olfactory bulb, ammon's horn, cerebellum, hypothalamus and striatum (PubMed:28096412, PubMed:21849472). {ECO:0000269|PubMed:17287360, ECO:0000269|PubMed:21849472, ECO:0000269|PubMed:28096412}. +Q9CQG6 TM147_MOUSE Transmembrane protein 147 224 25,335 Alternative sequence (2); Chain (1); Frameshift (1); Sequence conflict (1); Transmembrane (6) TRANSMEM 1 21 Helical. {ECO:0000255}.; TRANSMEM 38 58 Helical. {ECO:0000255}.; TRANSMEM 99 119 Helical. {ECO:0000255}.; TRANSMEM 137 157 Helical. {ECO:0000255}.; TRANSMEM 170 190 Helical. {ECO:0000255}.; TRANSMEM 202 222 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein. SUBUNIT: Forms a complex with NCLN and NOMO, resulting in a stabilization of the 3 proteins, which are otherwise quickly degraded by the proteasome. {ECO:0000250}. +Q8C6V3 TM212_MOUSE Transmembrane protein 212 187 20,747 Chain (1); Erroneous initiation (1); Transmembrane (5) TRANSMEM 11 31 Helical. {ECO:0000255}.; TRANSMEM 42 62 Helical. {ECO:0000255}.; TRANSMEM 76 96 Helical. {ECO:0000255}.; TRANSMEM 106 126 Helical. {ECO:0000255}.; TRANSMEM 148 168 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q5K6N0 TM232_MOUSE Transmembrane protein 232 (Testis-specific protein 13) 675 78,275 Alternative sequence (2); Chain (1); Coiled coil (1); Compositional bias (1); Sequence conflict (13); Transmembrane (1) TRANSMEM 163 183 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +D3Z1U7 TM233_MOUSE Transmembrane protein 233 (Dispanin subfamily B member 2) (DSPB2) 110 11,997 Chain (1); Erroneous initiation (1); Topological domain (3); Transmembrane (2) TRANSMEM 43 63 Helical. {ECO:0000255}.; TRANSMEM 86 106 Helical. {ECO:0000255}. TOPO_DOM 1 42 Extracellular. {ECO:0000255}.; TOPO_DOM 64 85 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 107 110 Extracellular. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8R1E7 TM234_MOUSE Transmembrane protein 234 140 14,922 Chain (1); Transmembrane (3) TRANSMEM 1 21 Helical. {ECO:0000255}.; TRANSMEM 82 102 Helical. {ECO:0000255}.; TRANSMEM 111 131 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +B1AQL3 TM235_MOUSE Transmembrane protein 235 (Claudin-27) 211 21,957 Chain (1); Signal peptide (1); Transmembrane (3) TRANSMEM 91 111 Helical. {ECO:0000255}.; TRANSMEM 118 138 Helical. {ECO:0000255}.; TRANSMEM 173 193 Helical. {ECO:0000255}. PTM: N-glycosylated. {ECO:0000269|PubMed:21689651}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Endoplasmic reticulum {ECO:0000305|PubMed:21689651}. +Q9D8U2 TM41A_MOUSE Transmembrane protein 41A 264 29,370 Chain (1); Region (1); Signal peptide (1); Transmembrane (5) TRANSMEM 67 87 Helical. {ECO:0000255}.; TRANSMEM 100 122 Helical. {ECO:0000255}.; TRANSMEM 153 173 Helical. {ECO:0000255}.; TRANSMEM 175 195 Helical. {ECO:0000255}.; TRANSMEM 219 239 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. DOMAIN: The VTT domain was previously called the SNARE-assoc domain. As there is no evidence that this domain associates with SNARE proteins, it was renamed as VMP1, TMEM41, and TVP38 (VTT) domain. {ECO:0000250|UniProtKB:Q96HV5}. +Q08EA8 TM213_MOUSE Transmembrane protein 213 116 12,442 Chain (1); Erroneous initiation (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 80 100 Helical. {ECO:0000255}. TOPO_DOM 36 79 Extracellular. {ECO:0000255}.; TOPO_DOM 101 116 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q8R4P4 TMC2_MOUSE Transmembrane channel-like protein 2 (Transmembrane cochlear-expressed protein 2) 888 101,134 Chain (1); Compositional bias (1); Topological domain (7); Transmembrane (6) TRANSMEM 246 266 Helical. {ECO:0000255}.; TRANSMEM 319 339 Helical. {ECO:0000255}.; TRANSMEM 413 433 Helical. {ECO:0000255}.; TRANSMEM 491 511 Helical. {ECO:0000255}.; TRANSMEM 676 696 Helical. {ECO:0000255}.; TRANSMEM 733 753 Helical. {ECO:0000255}. TOPO_DOM 1 245 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 267 318 Extracellular. {ECO:0000255}.; TOPO_DOM 340 412 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 434 490 Extracellular. {ECO:0000255}.; TOPO_DOM 512 675 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 697 732 Extracellular. {ECO:0000255}.; TOPO_DOM 754 888 Cytoplasmic. {ECO:0000255}. FUNCTION: Probable ion channel required for the normal function of cochlear hair cells (By similarity). Component of the hair cell's mechanotransduction (MET) machinery. Involved in mechanosensitive responses of the hair cells (By similarity). {ECO:0000250|UniProtKB:E7FFT2, ECO:0000250|UniProtKB:Q8TDI7}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:E7FFT2}; Multi-pass membrane protein {ECO:0000305}. Note=Localized to the stereocilia of the cochlear hair cells. {ECO:0000269|PubMed:28504928}. SUBUNIT: Interacts with TOMT. The interaction of TMC1 and TMC2 with TOMT is required for the transportation of TMC1/2 into the stereocilia of hair cells (PubMed:28504928). Interacts (via N-terminus) with both isoforms CD1 and CD3 of PCDH15 (PubMed:25114259). {ECO:0000269|PubMed:25114259, ECO:0000269|PubMed:28504928}. TISSUE SPECIFICITY: Inner ear and testis. {ECO:0000269|PubMed:11850618, ECO:0000269|PubMed:12812529}. +Q7TQ69 TMC3_MOUSE Transmembrane channel-like protein 3 1130 128,691 Alternative sequence (2); Chain (1); Glycosylation (1); Sequence conflict (3); Topological domain (11); Transmembrane (10) TRANSMEM 149 169 Helical. {ECO:0000255}.; TRANSMEM 193 213 Helical. {ECO:0000255}.; TRANSMEM 226 246 Helical. {ECO:0000255}.; TRANSMEM 320 340 Helical. {ECO:0000255}.; TRANSMEM 362 382 Helical. {ECO:0000255}.; TRANSMEM 394 414 Helical. {ECO:0000255}.; TRANSMEM 510 530 Helical. {ECO:0000255}.; TRANSMEM 571 591 Helical. {ECO:0000255}.; TRANSMEM 620 640 Helical. {ECO:0000255}.; TRANSMEM 681 701 Helical. {ECO:0000255}. TOPO_DOM 1 148 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 170 192 Extracellular. {ECO:0000255}.; TOPO_DOM 214 225 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 247 319 Extracellular. {ECO:0000255}.; TOPO_DOM 341 361 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 383 393 Extracellular. {ECO:0000255}.; TOPO_DOM 415 509 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 531 570 Extracellular. {ECO:0000255}.; TOPO_DOM 592 619 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 641 680 Extracellular. {ECO:0000255}.; TOPO_DOM 702 1130 Cytoplasmic. {ECO:0000255}. FUNCTION: Probable ion channel. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Detected in most neuronal organs and also in some non-neuronal tissues. {ECO:0000269|PubMed:12812529}. +Q3UV71 TMTC1_MOUSE Protein O-mannosyl-transferase TMTC1 (EC 2.4.1.109) (Transmembrane and TPR repeat-containing protein 1) 942 105,811 Alternative sequence (1); Chain (1); Frameshift (1); Repeat (10); Sequence conflict (2); Transmembrane (11) TRANSMEM 21 41 Helical. {ECO:0000255}.; TRANSMEM 110 130 Helical. {ECO:0000255}.; TRANSMEM 142 159 Helical. {ECO:0000255}.; TRANSMEM 160 180 Helical. {ECO:0000255}.; TRANSMEM 197 217 Helical. {ECO:0000255}.; TRANSMEM 332 352 Helical. {ECO:0000255}.; TRANSMEM 374 394 Helical. {ECO:0000255}.; TRANSMEM 415 435 Helical. {ECO:0000255}.; TRANSMEM 442 462 Helical. {ECO:0000255}.; TRANSMEM 464 484 Helical. {ECO:0000255}.; TRANSMEM 499 519 Helical. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Transfers mannosyl residues to the hydroxyl group of serine or threonine residues. The 4 members of the TMTC family are O-mannosyl-transferases dedicated primarily to the cadherin superfamily, each member seems to have a distinct role in decorating the cadherin domains with O-linked mannose glycans at specific regions. Also acts as O-mannosyl-transferase on other proteins such as PDIA3. {ECO:0000250|UniProtKB:Q8IUR5}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q8IUR5}. SUBUNIT: May interact with FAM168B. {ECO:0000250|UniProtKB:Q8IUR5}. +P48787 TNNI3_MOUSE Troponin I, cardiac muscle (Cardiac troponin I) 211 24,259 Calcium binding (1); Chain (1); Helix (2); Initiator methionine (1); Modified residue (16); Region (2); Site (2) FUNCTION: Troponin I is the inhibitory subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity. PTM: Phosphorylated at Ser-23 and Ser-24 by PRKD1; phosphorylation reduces myofilament calcium sensitivity. Phosphorylated preferentially at Thr-32. Phosphorylation by STK4/MST1 alters its binding affinity to TNNC1 (cardiac Tn-C) and TNNT2 (cardiac Tn-T) (By similarity). Phosphorylated at Ser-43 and Ser-45 by PRKCE; phosphorylation increases myocardium contractile dysfunction. {ECO:0000250, ECO:0000269|PubMed:16445938, ECO:0000269|PubMed:17854829}. SUBUNIT: Interacts with TRIM63 (By similarity). Binds to actin and tropomyosin. Interacts with STK4/MST1 (By similarity). {ECO:0000250}. +Q6PAQ9 TMG3_MOUSE Transmembrane gamma-carboxyglutamic acid protein 3 (Proline-rich gamma-carboxyglutamic acid protein 3) (Proline-rich Gla protein 3) 231 25,877 Chain (1); Disulfide bond (1); Domain (1); Frameshift (1); Modified residue (13); Propeptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 79 101 Helical. {ECO:0000255}. TOPO_DOM 20 78 Extracellular. {ECO:0000255}.; TOPO_DOM 102 231 Cytoplasmic. {ECO:0000255}. PTM: Gla residues are produced after subsequent post-translational modifications of glutamate by a vitamin K-dependent gamma-carboxylase. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. +Q9ER04 TMPS5_MOUSE Transmembrane protease serine 5 (EC 3.4.21.-) (Spinesin) 455 49,644 Active site (3); Alternative sequence (4); Chain (1); Disulfide bond (7); Domain (2); Glycosylation (4); Sequence conflict (16); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 50 70 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 49 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 71 455 Extracellular. {ECO:0000255}. FUNCTION: May play a role in hearing. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. +Q9DBI0 TMPS6_MOUSE Transmembrane protease serine 6 (EC 3.4.21.-) (Matriptase-2) 811 90,978 Active site (3); Alternative sequence (4); Chain (1); Disulfide bond (14); Domain (7); Erroneous initiation (1); Glycosylation (7); Mutagenesis (1); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 60 80 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 59 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 81 811 Extracellular. {ECO:0000255}. FUNCTION: Serine protease which hydrolyzes a range of proteins including type I collagen, fibronectin and fibrinogen. Can also activate urokinase-type plasminogen activator with low efficiency. May play a specialized role in matrix remodeling processes in liver. Through the cleavage of HJV, a regulator of the expression of the iron absorption-regulating hormone hepicidin/HAMP, plays a role in iron homeostasis. {ECO:0000269|PubMed:18451267}. PTM: The single-chain zymogen undergoes autoproteolytic processing. This results in TMPRSS6 shedding from the cell surface and conversion into an activated two-chains form which is released extracellularly. The process involves a trans-activation mechanism that requires TMPRSS6 oligomerization. {ECO:0000250|UniProtKB:Q8IU80}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12744720}; Single-pass type II membrane protein {ECO:0000269|PubMed:12744720}. Note=The processed, activated two-chains form is released in the extracellular space. {ECO:0000250|UniProtKB:Q8IU80}. SUBUNIT: Interacts with HJV. {ECO:0000250|UniProtKB:Q8IU80}. DOMAIN: Cytoplasmic domain mediates HAMP suppression via proximal promoter element(s). {ECO:0000269|PubMed:18451267}. TISSUE SPECIFICITY: Expressed at highest levels in adult mice liver, kidney and uterus. Also strongly expressed within the nasal cavity by olfactory epithelial cells. A weak, but detectable, signal in adult mice tissues analyzed including brain, lung, heart, kidney, spleen, muscle, intestine, thymus and pancreas. No signal in residual embryonic yolk sac, developing kidney tubules or in embryonic tissues analyzed including lung, heart, gastrointestinal tract and epithelium of the oral cavity. {ECO:0000269|PubMed:12744720}. +Q9QYH9 TNF14_MOUSE Tumor necrosis factor ligand superfamily member 14 (CD antigen CD258) [Cleaved into: Tumor necrosis factor ligand superfamily member 14, membrane form; Tumor necrosis factor ligand superfamily member 14, soluble form] 239 26,338 Chain (2); Disulfide bond (1); Glycosylation (2); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 38 58 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 37 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 59 239 Extracellular. {ECO:0000255}. FUNCTION: Cytokine that binds to TNFRSF3/LTBR. Binding to the decoy receptor TNFRSF6B modulates its effects. Activates NFKB and stimulates the proliferation of T-cells. Acts as a ligand for TNFRSF14/HVEM. Upon binding to TNFRSF14/HVEM, delivers costimulatory signals to T cells, leading to T cell proliferation and IFNG production (By similarity). {ECO:0000250|UniProtKB:O43557}. PTM: The soluble form derives from the membrane form by proteolytic processing. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: Tumor necrosis factor ligand superfamily member 14, soluble form: Secreted {ECO:0000250}. SUBUNIT: Homotrimer. Interacts with TNFRSF14. {ECO:0000250|UniProtKB:O43557}. +Q9CR23 TMEM9_MOUSE Transmembrane protein 9 183 20,633 Chain (1); Glycosylation (3); Modified residue (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 90 110 Helical. {ECO:0000255}. TOPO_DOM 21 89 Extracellular. {ECO:0000255}.; TOPO_DOM 111 183 Cytoplasmic. {ECO:0000255}. FUNCTION: May be involved in intracellular transport. PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Lysosome membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Dimer. {ECO:0000305}. +Q9JLH8 TMOD4_MOUSE Tropomodulin-4 (Skeletal muscle tropomodulin) (Sk-Tmod) 345 39,261 Chain (1) FUNCTION: Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9NZQ9}. Note=In myofibrils with sarcomeric structure, localizes to the pointed end of actin thin filaments. {ECO:0000250|UniProtKB:Q9NZQ9}. SUBUNIT: Binds to the N-terminus of tropomyosin and to actin. {ECO:0000250}. +Q63739 TP4A1_MOUSE Protein tyrosine phosphatase type IVA 1 (EC 3.1.3.48) (Protein-tyrosine phosphatase 4a1) (Protein-tyrosine phosphatase of regenerating liver 1) (PRL-1) 173 19,815 Active site (2); Beta strand (7); Binding site (1); Chain (1); Disulfide bond (1); Domain (1); Helix (6); Lipidation (1); Modified residue (1); Mutagenesis (1); Propeptide (1); Region (2) FUNCTION: Protein tyrosine phosphatase which stimulates progression from G1 into S phase during mitosis. May play a role in the development and maintenance of differentiating epithelial tissues (By similarity). {ECO:0000250}. PTM: Farnesylated. Farnesylation is required for membrane targeting. Unfarnesylated forms are shifted into the nucleus. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10747914}. Early endosome {ECO:0000269|PubMed:10747914}. Endoplasmic reticulum {ECO:0000269|PubMed:10747914}. Cytoplasm {ECO:0000269|PubMed:10747914}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:10747914}. Note=And mitotic spindle. SUBUNIT: Homotrimer. Interacts with tubulin (By similarity). Interacts with ATF5. {ECO:0000250, ECO:0000269|PubMed:11278933}. +Q64514 TPP2_MOUSE Tripeptidyl-peptidase 2 (TPP-2) (EC 3.4.14.10) (Tripeptidyl aminopeptidase) (Tripeptidyl-peptidase II) (TPP-II) 1262 139,879 Active site (3); Alternative sequence (1); Chain (1); Domain (1); Initiator methionine (1); Modified residue (3); Mutagenesis (1) FUNCTION: Component of the proteolytic cascade acting downstream of the 26S proteasome in the ubiquitin-proteasome pathway. May be able to complement the 26S proteasome function to some extent under conditions in which the latter is inhibited (By similarity). Stimulates adipogenesis. {ECO:0000250, ECO:0000269|PubMed:17932511}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19747897}. Nucleus {ECO:0000269|PubMed:19747897}. Note=Translocates to the nucleus in responce to gamma-irradiation. TISSUE SPECIFICITY: Expressed in the brain, skeletal muscle, gonadal and mesenteric white adipose tissue and brown adipose tissues. {ECO:0000269|PubMed:17932511}. +P58774 TPM2_MOUSE Tropomyosin beta chain (Beta-tropomyosin) (Tropomyosin-2) 284 32,837 Alternative sequence (2); Chain (1); Coiled coil (1); Modified residue (14); Mutagenesis (1); Sequence conflict (1) FUNCTION: Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments. The non-muscle isoform may have a role in agonist-mediated receptor internalization (PubMed:16094730). {ECO:0000250|UniProtKB:P58775, ECO:0000269|PubMed:16094730}. PTM: Phosphorylated on Ser-61 by PIK3CG. Phosphorylation on Ser-61 is required for ADRB2 internalization. {ECO:0000269|PubMed:16094730}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P58775}. Note=Associates with F-actin stress fibers. {ECO:0000250|UniProtKB:P58775}. SUBUNIT: Homodimer. Heterodimer of an alpha (TPM1, TPM3 or TPM4) and a beta (TPM2) chain. {ECO:0000250|UniProtKB:P58775}. DOMAIN: The molecule is in a coiled coil structure that is formed by 2 polypeptide chains. The sequence exhibits a prominent seven-residues periodicity. +P42682 TXK_MOUSE Tyrosine-protein kinase TXK (EC 2.7.10.2) (PTK-RL-18) (Resting lymphocyte kinase) 527 61,108 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Compositional bias (1); Domain (3); Modified residue (2); Mutagenesis (1); Nucleotide binding (1); Sequence conflict (4) FUNCTION: Non-receptor tyrosine kinase that plays a redundant role with ITK in regulation of the adaptive immune response. Regulates the development, function and differentiation of conventional T-cells and nonconventional NKT-cells. When antigen presenting cells (APC) activate T-cell receptor (TCR), a series of phosphorylation lead to the recruitment of TXK to the cell membrane, where it is phosphorylated at Tyr-420. Phosphorylation leads to TXK full activation. Contributes also to signaling from many receptors and participates in multiple downstream pathways, including regulation of the actin cytoskeleton. Like ITK, can phosphorylate PLCG1, leading to its localization in lipid rafts and activation, followed by subsequent cleavage of its substrates. In turn, the endoplasmic reticulum releases calcium in the cytoplasm and the nuclear activator of activated T-cells (NFAT) translocates into the nucleus to perform its transcriptional duty. With PARP1 and EEF1A1, TXK forms a complex that acts as a T-helper 1 (Th1) cell-specific transcription factor and binds the promoter of IFNG to directly regulate its transcription, and is thus involved importantly in Th1 cytokine production. Phosphorylates both PARP1 and EEF1A1. Phosphorylates also key sites in LCP2 leading to the up-regulation of Th1 preferred cytokine IL-2. Phosphorylates 'Tyr-201' of CTLA4 which leads to the association of PI-3 kinase with the CTLA4 receptor. {ECO:0000269|PubMed:10562318, ECO:0000269|PubMed:10587356, ECO:0000269|PubMed:10660534, ECO:0000269|PubMed:18941202}. PTM: Phosphorylated at Tyr-420 by FYN. Autophosphorylation at Tyr-91 is critical for the activation of TXK, leading to the up-regulation of IFN-gamma gene transcription. {ECO:0000250}.; PTM: The cysteine string at the N-terminus is palmitoylated and required for the proper subcellular location. {ECO:0000269|PubMed:9891083}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cell membrane; Peripheral membrane protein. Note=Localizes in the vicinity of cell surface receptors in the plasma membrane after receptor stimulation. Translocates into the nucleus and enhances IFN-gamma gene transcription in T-cells. {ECO:0000250}. SUBUNIT: Interacts with PARP1 and EEF1A1 (By similarity). Interacts with SH2D2A. {ECO:0000250, ECO:0000269|PubMed:10587356, ECO:0000269|PubMed:11353545}. TISSUE SPECIFICITY: Expressed in early thymocytes, T-cells and mast cells. +Q7TN22 TXD16_MOUSE Thioredoxin domain-containing protein 16 820 92,105 Alternative sequence (1); Chain (1); Disulfide bond (1); Domain (1); Erroneous initiation (1); Glycosylation (1); Motif (1); Signal peptide (1) PTM: Glycosylated. {ECO:0000250|UniProtKB:Q9P2K2}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9P2K2}. Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:Q9P2K2}. DOMAIN: Contains a masked and non-functional KDEL endoplasmic reticulum retrieval motif. {ECO:0000250|UniProtKB:Q9P2K2}. +Q8CDN6 TXNL1_MOUSE Thioredoxin-like protein 1 (32 kDa thioredoxin-related protein) 289 32,237 Chain (1); Disulfide bond (1); Domain (2); Modified residue (1); Sequence conflict (1) FUNCTION: Active thioredoxin with a redox potential of about -250 mV. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=At least 85% of the cellular TXNL1 is proteasome-associated. {ECO:0000250}. SUBUNIT: Component of the 19S regulatory cap of the 26S proteasome. Interacts with PSMD14/RPN11. Interacts with, and reduces EEF1A1 (By similarity). {ECO:0000250}. +Q9D384 U1SBP_MOUSE U11/U12 small nuclear ribonucleoprotein 35 kDa protein (U11/U12 snRNP 35 kDa protein) (U1 snRNP-binding protein homolog) 244 29,290 Chain (1); Compositional bias (1); Cross-link (1); Domain (1) SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the U11/U12 snRNPs that are part of the U12-type spliceosome. {ECO:0000250}. +Q8VDI7 UBAC1_MOUSE Ubiquitin-associated domain-containing protein 1 (UBA domain-containing protein 1) (E3 ubiquitin-protein ligase subunit KPC2) (Kip1 ubiquitination-promoting complex protein 2) 409 45,531 Chain (1); Domain (4); Modified residue (1); Natural variant (3) Protein modification; protein ubiquitination. FUNCTION: Non-catalytic subunit of the KPC complex that acts as E3 ubiquitin-protein ligase. Required for poly-ubiquitination and proteasome-mediated degradation of CDKN1B during G1 phase of the cell cycle (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Component of the KPC complex composed of RNF123/KPC1 and UBAC1/KPC2. Interacts with RNF123 via its N-terminal domain. Interacts with the proteasome via its N-terminal domain (By similarity). {ECO:0000250}. +P63280 UBC9_MOUSE SUMO-conjugating enzyme UBC9 (EC 2.3.2.-) (RING-type E3 SUMO transferase UBC9) (SUMO-protein ligase) (Ubiquitin carrier protein 9) (mUBC9) (Ubiquitin carrier protein I) (Ubiquitin-conjugating enzyme E2 I) (Ubiquitin-protein ligase I) 158 18,007 Active site (1); Beta strand (5); Chain (1); Cross-link (6); Helix (5); Initiator methionine (1); Modified residue (3); Region (1); Site (4); Turn (3) Protein modification; protein sumoylation. FUNCTION: Accepts the ubiquitin-like proteins SUMO1, SUMO2 and SUMO3 from the UBLE1A-UBLE1B E1 complex and catalyzes their covalent attachment to other proteins with the help of an E3 ligase such as RANBP2, CBX4 and ZNF451. Can catalyze the formation of poly-SUMO chains. Essential for nuclear architecture, chromosome segregation and embryonic viability. Necessary for sumoylation of FOXL2 and KAT5 (By similarity). Sumoylates p53/TP53 at 'Lys-386'. {ECO:0000250|UniProtKB:P63279, ECO:0000269|PubMed:16326389, ECO:0000269|PubMed:17187077, ECO:0000269|PubMed:22214662}. PTM: Phosphorylation at Ser-71 significantly enhances SUMOylation activity. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Mainly nuclear. In spermatocytes, localizes in synaptonemal complexes. Recruited by BCL11A into the nuclear body. SUBUNIT: Forms a tight complex with RANGAP1 and RANBP2. Interacts with SIAH1 and PARP. Interacts with various transcription factors such as TFAP2A, TFAP2B, TFAP2C, AR, ETS1 and SOX4. Interacts with RASD2. Interacts with RWDD3; the interaction enhances the sumoylation of a number of proteins such as HIF1A and I-kappa-B. Interacts with FOXL2. Forms a complex with SENP6 and UBE2I in response to UV irradiation. Interacts with DNM1L (via its GTPase and B domains); the interaction promotes sumoylation of DNM1L, mainly in the B domain (By similarity). Interacts with HIPK1, HIPK2, PPM1J and TCF3. Interacts with Moloney murine leukemia virus CA and adenovirus type 5 and type 12 E1A. Interacts with NR2C1; the interaction promotes its sumoylation. Interacts with NFATC2IP; this inhibits formation of poly-SUMO chains. Interacts with FHIT (By similarity). Interacts with PRKRA and p53/TP53. Interacts with UHRF2. Interacts with NR3C1 and this interaction is enhanced in the presence of RWDD3. Interacts with MTA1 (By similarity). Interacts with ZNF451. Identified in a complex with SUMO2 and UBE2I, where one ZNF451 interacts with one UBE2I and two SUMO2 chains, one bound to the UBE2I active site and the other to another region of the same UBE2I molecule. Interacts with SETX (By similarity). Interacts with CPEB3 (PubMed:26074071). {ECO:0000250|UniProtKB:P63279, ECO:0000269|PubMed:26074071}. TISSUE SPECIFICITY: Present in spleen, kidney, lung, brain, heart and testis (at protein level). {ECO:0000269|PubMed:9409784}. +Q8JZM6 TIFAB_MOUSE TRAF-interacting protein with FHA domain-containing protein B (TIFA-like protein) 147 16,636 Chain (1); Domain (1); Erroneous initiation (1); Sequence conflict (3) FUNCTION: Inhibits TIFA-mediated TRAF6 activation possibly by inducing a conformational change in TIFA. {ECO:0000269|PubMed:15047173}. SUBUNIT: Interacts with TIFA. {ECO:0000250}. TISSUE SPECIFICITY: Expressed at high levels in spleen and at moderate levels in lung, thymus, and small intestine. {ECO:0000269|PubMed:15047173}. +P52912 TIA1_MOUSE Nucleolysin TIA-1 (RNA-binding protein TIA-1) (T-cell-restricted intracellular antigen-1) (TIA-1) 386 42,800 Beta strand (4); Chain (1); Domain (3); Helix (3); Modified residue (1); Turn (2) FUNCTION: Involved in alternative pre-RNA splicing and regulation of mRNA translation by binding to AU-rich elements (AREs) located in mRNA 3' untranslated regions (3' UTRs). Possesses nucleolytic activity against cytotoxic lymphocyte target cells. May be involved in apoptosis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, Stress granule {ECO:0000250|UniProtKB:P31483}. Nucleus {ECO:0000250|UniProtKB:P31483}. Note=Accumulates in cytoplasmic stress granules (SG) following cellular damage. {ECO:0000250|UniProtKB:P31483}. +Q8BQ33 TICRR_MOUSE Treslin (TopBP1-interacting checkpoint and replication regulator) (TopBP1-interacting, replication-stimulating protein) 1889 208,335 Chain (1); Compositional bias (1); Erroneous initiation (2); Frameshift (1); Modified residue (12); Sequence conflict (2) FUNCTION: Regulator of DNA replication and S/M and G2/M checkpoints. Regulates the triggering of DNA replication initiation via its interaction with TOPBP1 by participating in CDK2-mediated loading of CDC45L onto replication origins. Required for the transition from pre-replication complex (pre-RC) to pre-initiation complex (pre-IC). Required to prevent mitotic entry after treatment with ionizing radiation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Associates with chromatin. SUBUNIT: Interacts with TOPBP1 (via BRCT domains); interaction takes place in a CDK2-dependent manner (By similarity). Component of the replisome complex composed of at least DONSON, MCM2, MCM7, PCNA and TICRR (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q7Z2Z1}. +Q9D880 TIM50_MOUSE Mitochondrial import inner membrane translocase subunit TIM50 353 39,776 Chain (1); Domain (1); Erroneous initiation (1); Modified residue (1); Topological domain (2); Transit peptide (1); Transmembrane (1) TRANSMEM 66 86 Helical. {ECO:0000255}. TOPO_DOM 22 65 Mitochondrial matrix. {ECO:0000255}.; TOPO_DOM 87 353 Mitochondrial intermembrane. {ECO:0000255}. FUNCTION: Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane. Has some phosphatase activity in vitro; however such activity may not be relevant in vivo. {ECO:0000250|UniProtKB:Q3ZCQ8}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q3ZCQ8}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q3ZCQ8}. SUBUNIT: Component of the TIM23 complex at least composed of TIMM23, TIMM17 (TIMM17A or TIMM17B) and TIMM50; within this complex, directly interacts with TIMM23. The complex interacts with the TIMM44 component of the PAM complex and with DNAJC15. {ECO:0000250|UniProtKB:Q3ZCQ8}. +O55047 TLK2_MOUSE Serine/threonine-protein kinase tousled-like 2 (EC 2.7.11.1) (PKU-alpha) (Tousled-like kinase 2) 718 82,261 Active site (1); Alternative sequence (3); Binding site (1); Chain (1); Coiled coil (3); Domain (1); Erroneous initiation (1); Modified residue (5); Nucleotide binding (1); Sequence conflict (7) FUNCTION: Serine/threonine-protein kinase involved in the process of chromatin assembly and probably also DNA replication, transcription, repair, and chromosome segregation. Phosphorylates the chromatin assembly factors ASF1A AND ASF1B. Phosphorylation of ASF1A prevents its proteasome-mediated degradation, thereby enhancing chromatin assembly (By similarity). Negative regulator of amino acid starvation-induced autophagy (By similarity). {ECO:0000250}.; FUNCTION: Testis-specific isoforms may play a role in spermatogenesis. Highly expressed in embryos throughout development. {ECO:0000269|PubMed:10092119}. PTM: Phosphorylated at Ser-696, probably by CHEK1. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10455159}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10455159}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10455159}. Note=Colocalizes with the cytoplasmic intermediate filament system during the G1 phase of the cell cycle. Present in the perinuclear region at S phase and in the nucleus at late G2. SUBUNIT: Monomer and heterodimer with TLK1. Interacts with ASF1A and ASF1B. May also interact with FEZ1/LZTS1 and FEZ2 (By similarity). Association with 14-3-3 proteins such as YWHAZ regulates subcellular location. {ECO:0000250, ECO:0000269|PubMed:10455159}. TISSUE SPECIFICITY: Ubiquitously expressed in all tissues examined, with high levels in heart and testis, in particular the pachytene spermatocytes and in round spermatids. Some evidence for the existence of a testis-specific isoform suggesting a role in spermatogenesis. {ECO:0000269|PubMed:10092119, ECO:0000269|PubMed:10455159, ECO:0000269|PubMed:10523312, ECO:0000303|PubMed:10092119}. +Q62381 TLL1_MOUSE Tolloid-like protein 1 (mTll) (EC 3.4.24.-) 1013 114,533 Active site (1); Alternative sequence (2); Chain (1); Disulfide bond (19); Domain (8); Glycosylation (4); Metal binding (3); Propeptide (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Protease which processes procollagen C-propeptides, such as chordin, pro-biglycan and pro-lysyl oxidase. Required for the embryonic development, especially heart development. Predominant protease, which in the development, influences dorsal-ventral patterning and skeletogenesis. {ECO:0000269|PubMed:10331975}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Highly expressed in brain and kidney and weakly in lung, skeletal muscle. A perceptible level of expression is observed in heart and testis. {ECO:0000269|PubMed:8661043}. +Q62440 TLE1_MOUSE Transducin-like enhancer protein 1 (Groucho-related protein 1) (Grg-1) 770 83,097 Alternative sequence (9); Chain (1); Modified residue (5); Motif (1); Region (4); Repeat (6); Sequence conflict (22) FUNCTION: Transcriptional corepressor that binds to a number of transcription factors. Inhibits NF-kappa-B-regulated gene expression. Inhibits the transcriptional activation mediated by FOXA2, and by CTNNB1 and TCF family members in Wnt signaling. The effects of full-length TLE family members may be modulated by association with dominant-negative AES. Unusual function as coactivator for ESRRG (By similarity). {ECO:0000250}. PTM: Phosphorylated, probably by CDK1. The degree of phosphorylation varies throughout the cell cycle, and is highest at the G2/M transition. Becomes hyperphosphorylated in response to cell differentiation and interaction with HES1 or RUNX1. {ECO:0000269|PubMed:11756536, ECO:0000269|PubMed:8713081}.; PTM: Ubiquitinated by XIAP/BIRC4. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8713081}. Note=Nuclear and chromatin-associated, depending on isoforms and phosphorylation status. Hyperphosphorylation decreases the affinity for nuclear components.; SUBCELLULAR LOCATION: Isoform 7: Nucleus. Cytoplasm.; SUBCELLULAR LOCATION: Isoform 8: Nucleus. Cytoplasm. SUBUNIT: Homooligomer and heterooligomer with other family members. Binds RUNX1, RUNX2, FOXA2, KDM6A, UTY, histone H3, HESX1, ESRRG and the NF-kappa-B subunit RELA. Interacts with HES1 (via WRPW motif) (By similarity). Binds TCF7, LEF1, TCF7L1 and TCF7L2. Interacts with SIX3 (By similarity). Interacts with EFNB1. {ECO:0000250, ECO:0000250|UniProtKB:Q04724, ECO:0000269|PubMed:11266540, ECO:0000269|PubMed:21429299}. DOMAIN: WD repeat Groucho/TLE family members are characterized by 5 regions, a glutamine-rich Q domain, a glycine/proline-rich GP domain, a central CcN domain, containing a nuclear localization signal, and a serine/proline-rich SP domain. The most highly conserved are the N-terminal Q domain and the C-terminal WD-repeat domain. {ECO:0000305|PubMed:18254933}. TISSUE SPECIFICITY: Highly expressed in liver and lung. Detected at slightly lower levels in heart, brain, kidney and testis. Detected in fetal and adult stomach and small intestine, in adult ileum, duodenum and colon. In adult small intestine isoform 7 and isoform 8 are most strongly expressed at the base of the crypts of Lieberkuhn. +Q9WVB2 TLE2_MOUSE Transducin-like enhancer protein 2 767 82,623 Chain (1); Modified residue (4); Motif (1); Region (4); Repeat (6) FUNCTION: Transcriptional corepressor that binds to a number of transcription factors. Inhibits the transcriptional activation mediated by CTNNB1 and TCF family members in Wnt signaling. The effects of full-length TLE family members may be modulated by association with dominant-negative AES (By similarity). {ECO:0000250}. PTM: Ubiquitinated by XIAP/BIRC4. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Homooligomer and heterooligomer with other family members. Binds LEF1, TCF7, TCF7L1, TCF7L2, UTY, HES1 and HES5 (By similarity). {ECO:0000250}. DOMAIN: WD repeat Groucho/TLE family members are characterized by 5 regions, a glutamine-rich Q domain, a glycine/proline-rich GP domain, a central CcN domain, containing a nuclear localization signal, and a serine/proline-rich SP domain. The most highly conserved are the N-terminal Q domain and the C-terminal WD-repeat domain. {ECO:0000305|PubMed:18254933}. +Q8VC26 TLCD2_MOUSE TLC domain-containing protein 2 310 34,139 Alternative sequence (2); Chain (1); Domain (1); Transmembrane (6) TRANSMEM 6 26 Helical. {ECO:0000255}.; TRANSMEM 40 60 Helical. {ECO:0000255}.; TRANSMEM 79 99 Helical. {ECO:0000255}.; TRANSMEM 117 137 Helical. {ECO:0000255}.; TRANSMEM 167 187 Helical. {ECO:0000255}.; TRANSMEM 194 214 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q62441 TLE4_MOUSE Transducin-like enhancer protein 4 (Grg-4) (Groucho-related protein 4) 773 83,787 Chain (1); Erroneous initiation (1); Modified residue (20); Region (4); Repeat (7); Sequence conflict (4) FUNCTION: Transcriptional corepressor that binds to a number of transcription factors. Inhibits the transcriptional activation mediated by PAX5, and by CTNNB1 and TCF family members in Wnt signaling. The effects of full-length TLE family members may be modulated by association with dominant-negative AES. Essential for the transcriptional repressor activity of SIX3 during retina and lens development and for SIX3 transcriptional auto-repression. {ECO:0000269|PubMed:12050133, ECO:0000269|PubMed:21317240}. PTM: Phosphorylated. PAX5 binding increases phosphorylation. {ECO:0000269|PubMed:10811620}.; PTM: Ubiquitinated by XIAP/BIRC4. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Homooligomer and heterooligomer with other family members (By similarity). Binds PAX5, LEF1, TCF7, TCF7L1 and TCF7L2. Interacts with ZNF703; TLE4 may mediate ZNF703 transcriptional repression. Interacts with SIX3 and SIX6. Interacts with PAX2 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q04727, ECO:0000269|PubMed:10811620, ECO:0000269|PubMed:11266540, ECO:0000269|PubMed:12050133, ECO:0000269|PubMed:21317240}. DOMAIN: WD repeat Groucho/TLE family members are characterized by 5 regions, a glutamine-rich Q domain, a glycine/proline-rich GP domain, a central CcN domain, containing a nuclear localization signal, and a serine/proline-rich SP domain. The most highly conserved are the N-terminal Q domain and the C-terminal WD-repeat domain. {ECO:0000305|PubMed:18254933}. +Q9WVB3 TLE6_MOUSE Transducin-like enhancer protein 6 (Groucho-related protein 6) 581 65,116 Chain (1); Modified residue (4); Motif (1); Repeat (8) FUNCTION: As a member of the subcortical maternal complex (SCMC), plays an essential role for zygotes to progress beyond the first embryonic cell divisions. {ECO:0000269|PubMed:18804437}. SUBCELLULAR LOCATION: Cytoplasm. Note=In the subcortical cytoplasm of early embryos from the 1-cell to the blastocyst stages. From the 2-cell stage, still detected in the subcortex, but excluded from cell-cell contact regions. SUBUNIT: Component of the SCMC which also includes KHDC3, OOEP and NLRP5. {ECO:0000269|PubMed:18804437}. DOMAIN: Contrary to other WD repeat Groucho/TLE family members, does not contain any identifiable Q, GP, CcN or SP domains. Only the C-terminal WD-repeat domain is conserved. {ECO:0000305|PubMed:18254933}. TISSUE SPECIFICITY: Expressed predominantly in ovaries, where it is restricted to growing oocytes, with greatest levels in fully grown oocytes (PubMed:18804437). Expressed predominantly in testis, heart, lung, liver and muscle, and at very low levels in the brain, spleen and kidney (PubMed:11486032). {ECO:0000269|PubMed:11486032, ECO:0000269|PubMed:18804437}. +Q9D938 TM160_MOUSE Transmembrane protein 160 188 19,587 Chain (1); Modified residue (1); Transmembrane (3) TRANSMEM 70 90 Helical. {ECO:0000255}.; TRANSMEM 102 122 Helical. {ECO:0000255}.; TRANSMEM 135 155 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q5S248 TM11E_MOUSE Transmembrane protease serine 11E (EC 3.4.21.-) (Serine protease DESC1) [Cleaved into: Transmembrane protease serine 11E non-catalytic chain; Transmembrane protease serine 11E catalytic chain] 423 48,065 Active site (3); Chain (2); Disulfide bond (4); Domain (2); Erroneous initiation (1); Glycosylation (4); Topological domain (2); Transmembrane (1) TRANSMEM 19 39 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 18 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 40 423 Extracellular. {ECO:0000255}. FUNCTION: Serine protease which possesses both gelatinolytic and caseinolytic activities. Shows a preference for Arg in the P1 position. {ECO:0000269|PubMed:15328353}. PTM: N-glycosylated. {ECO:0000269|PubMed:15328353}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15328353}; Single-pass type II membrane protein {ECO:0000269|PubMed:15328353}.; SUBCELLULAR LOCATION: Transmembrane protease serine 11E catalytic chain: Secreted {ECO:0000269|PubMed:15328353}. Note=Activated by cleavage and secreted. {ECO:0000269|PubMed:15328353}. SUBUNIT: Forms a heterodimer with SERPINA5 and SERPINE1. TISSUE SPECIFICITY: Expressed in epidermal, oral and male reproductive tissues. {ECO:0000269|PubMed:15328353}. +Q99MB1 TLR3_MOUSE Toll-like receptor 3 (CD antigen CD283) 905 103,671 Beta strand (36); Chain (1); Disulfide bond (4); Domain (3); Glycosylation (15); Helix (13); Modified residue (2); Repeat (22); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (16) TRANSMEM 706 726 Helical. {ECO:0000255}. TOPO_DOM 26 705 Lumenal. {ECO:0000255}.; TOPO_DOM 727 905 Cytoplasmic. {ECO:0000255}. FUNCTION: Key component of innate and adaptive immunity. TLRs (Toll-like receptors) control host immune response against pathogens through recognition of molecular patterns specific to microorganisms. TLR3 is a nucleotide-sensing TLR which is activated by double-stranded RNA, a sign of viral infection. Acts via the adapter TRIF/TICAM1, leading to NF-kappa-B activation, IRF3 nuclear translocation, cytokine secretion and the inflammatory response (By similarity). {ECO:0000250, ECO:0000269|PubMed:14993594}. PTM: TLR3 signaling requires a proteolytic cleavage mediated by cathepsins CTSB and CTSH, the cleavage occurs between amino acids 252 and 346. The cleaved form of TLR3 is the predominant form found in endosomes (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein. Endosome membrane {ECO:0000250|UniProtKB:O15455}. Early endosome {ECO:0000250|UniProtKB:O15455}. SUBUNIT: Monomer and homodimer; dimerization is triggered by ligand-binding, the signaling unit is composed of one ds-RNA of around 40 bp and two TLR3 molecules, and lateral clustering of signaling units along the length of the ds-RNA ligand is required for TLR3 signal transduction. Interacts (via transmembrane domain) with UNC93B1; the interaction is required for transport from the ER to the endosomes. Interacts with SRC; upon binding of double-stranded RNA (By similarity). Interacts with TICAM1 (via the TIR domain) in response to poly(I:C) and this interaction is enhanced in the presence of WDFY1 (PubMed:25736436). The tyrosine-phosphorylated form (via TIR domain) interacts with WDFY1 (via WD repeat 2) in response to poly(I:C) (PubMed:25736436). {ECO:0000250|UniProtKB:O15455, ECO:0000269|PubMed:25736436}. DOMAIN: ds-RNA binding is mediated by LRR 1 to 3, and LRR 17 to 18. TISSUE SPECIFICITY: Highly expressed in lung. After intraperitoneal injection of lipopolysaccharide, highly expressed in brain, heart, kidney, liver, lung and spleen. +Q8BP07 TM220_MOUSE Transmembrane protein 220 167 18,324 Alternative sequence (3); Chain (1); Transmembrane (5) TRANSMEM 10 30 Helical. {ECO:0000255}.; TRANSMEM 40 60 Helical. {ECO:0000255}.; TRANSMEM 69 89 Helical. {ECO:0000255}.; TRANSMEM 104 122 Helical. {ECO:0000255}.; TRANSMEM 130 150 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8BMD6 TM260_MOUSE Transmembrane protein 260 703 78,947 Alternative sequence (1); Chain (1); Erroneous initiation (3); Sequence conflict (1); Transmembrane (8) TRANSMEM 20 40 Helical. {ECO:0000255}.; TRANSMEM 68 88 Helical. {ECO:0000255}.; TRANSMEM 90 110 Helical. {ECO:0000255}.; TRANSMEM 137 157 Helical. {ECO:0000255}.; TRANSMEM 182 202 Helical. {ECO:0000255}.; TRANSMEM 218 238 Helical. {ECO:0000255}.; TRANSMEM 314 334 Helical. {ECO:0000255}.; TRANSMEM 352 372 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9NX78}; Multi-pass membrane protein {ECO:0000305}. Note=Shows strong localization in the vicinity of the cell membrane. {ECO:0000250|UniProtKB:Q9NX78}. +Q9D771 TM206_MOUSE Transmembrane protein 206 350 40,178 Chain (1); Glycosylation (2); Modified residue (4); Topological domain (3); Transmembrane (2) TRANSMEM 65 85 Helical. {ECO:0000255}.; TRANSMEM 302 318 Helical. {ECO:0000255}. TOPO_DOM 1 64 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 86 301 Extracellular. {ECO:0000255}.; TOPO_DOM 319 350 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q4KL18 TM171_MOUSE Transmembrane protein 171 322 34,585 Chain (1); Transmembrane (4) TRANSMEM 22 42 Helical. {ECO:0000255}.; TRANSMEM 57 77 Helical. {ECO:0000255}.; TRANSMEM 112 132 Helical. {ECO:0000255}.; TRANSMEM 159 179 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9WUH1 TM115_MOUSE Transmembrane protein 115 (Protein PL6 homolog) 350 38,099 Chain (1); Erroneous initiation (1); Modified residue (1); Region (2); Topological domain (5); Transmembrane (4) TRANSMEM 20 40 Helical; Name=1. {ECO:0000255}.; TRANSMEM 98 118 Helical; Name=2. {ECO:0000255}.; TRANSMEM 127 147 Helical; Name=3. {ECO:0000255}.; TRANSMEM 166 186 Helical; Name=4. {ECO:0000255}. TOPO_DOM 1 19 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 41 97 Lumenal. {ECO:0000305}.; TOPO_DOM 119 126 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 148 165 Lumenal. {ECO:0000305}.; TOPO_DOM 187 350 Cytoplasmic. {ECO:0000305}. FUNCTION: May play a role in retrograde transport of proteins from the Golgi to the endoplasmic reticulum. May indirectly play a role in protein glycosylation in the Golgi. {ECO:0000250|UniProtKB:Q12893}. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:Q12893}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q12893}. SUBUNIT: Homooligomer. Interacts with COPB1. May interact with LMAN1. Interacts with the COG complex; probably through COG3. {ECO:0000250|UniProtKB:Q12893}. +O70472 TM131_MOUSE Transmembrane protein 131 (Protein RW1) 1877 204,651 Chain (1); Compositional bias (3); Modified residue (5); Sequence caution (1); Sequence conflict (5); Transmembrane (2) TRANSMEM 1089 1109 Helical. {ECO:0000255}.; TRANSMEM 1116 1136 Helical. {ECO:0000255}. FUNCTION: May play a role in the immune response to viral infection. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8BXN9 TM87A_MOUSE Transmembrane protein 87A 555 63,380 Alternative sequence (3); Chain (1); Erroneous initiation (3); Glycosylation (3); Modified residue (1); Sequence conflict (4); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 226 246 Helical; Name=1. {ECO:0000255}.; TRANSMEM 258 278 Helical; Name=2. {ECO:0000255}.; TRANSMEM 306 322 Helical; Name=3. {ECO:0000255}.; TRANSMEM 326 346 Helical; Name=4. {ECO:0000255}.; TRANSMEM 362 382 Helical; Name=5. {ECO:0000255}.; TRANSMEM 404 424 Helical; Name=6. {ECO:0000255}.; TRANSMEM 438 458 Helical; Name=7. {ECO:0000255}. TOPO_DOM 22 225 Lumenal. {ECO:0000305}.; TOPO_DOM 247 257 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 279 305 Lumenal. {ECO:0000305}.; TOPO_DOM 323 325 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 347 361 Lumenal. {ECO:0000305}.; TOPO_DOM 383 403 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 425 437 Lumenal. {ECO:0000305}.; TOPO_DOM 459 555 Cytoplasmic. {ECO:0000305}. FUNCTION: May be involved in retrograde transport from endosomes to the trans-Golgi network (TGN). {ECO:0000250|UniProtKB:Q8NBN3}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q8NBN3}; Multi-pass membrane protein {ECO:0000255}. +Q9DBU0 TM9S1_MOUSE Transmembrane 9 superfamily member 1 606 68,928 Chain (1); Glycosylation (3); Sequence conflict (1); Signal peptide (1); Transmembrane (9) TRANSMEM 237 257 Helical. {ECO:0000255}.; TRANSMEM 310 330 Helical. {ECO:0000255}.; TRANSMEM 339 359 Helical. {ECO:0000255}.; TRANSMEM 373 393 Helical. {ECO:0000255}.; TRANSMEM 412 432 Helical. {ECO:0000255}.; TRANSMEM 469 489 Helical. {ECO:0000255}.; TRANSMEM 499 519 Helical. {ECO:0000255}.; TRANSMEM 535 555 Helical. {ECO:0000255}.; TRANSMEM 570 590 Helical. {ECO:0000255}. FUNCTION: Plays an essential role in autophagy. {ECO:0000250}. SUBCELLULAR LOCATION: Lysosome membrane; Multi-pass membrane protein. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q9D1X9 TM50B_MOUSE Transmembrane protein 50B 158 17,948 Chain (1); Initiator methionine (1); Modified residue (1); Transmembrane (4) TRANSMEM 28 48 Helical. {ECO:0000255}.; TRANSMEM 56 76 Helical. {ECO:0000255}.; TRANSMEM 98 118 Helical. {ECO:0000255}.; TRANSMEM 128 148 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18541381}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:18541381}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: May form homotrimers or homodimers. {ECO:0000269|PubMed:18541381}. TISSUE SPECIFICITY: Expressed in brain, heart and testis (at protein level). In the cerebellum, has particularly strong expression in Bergmann astroglial cells (at protein level). {ECO:0000269|PubMed:18541381}. +P58749 TM6S1_MOUSE Transmembrane 6 superfamily member 1 370 41,662 Chain (1); Domain (2); Sequence conflict (1); Transmembrane (9) TRANSMEM 3 23 Helical; Name=1. {ECO:0000255}.; TRANSMEM 34 54 Helical; Name=2. {ECO:0000255}.; TRANSMEM 62 82 Helical; Name=3. {ECO:0000255}.; TRANSMEM 110 130 Helical; Name=4. {ECO:0000255}.; TRANSMEM 139 159 Helical; Name=5. {ECO:0000255}.; TRANSMEM 166 186 Helical; Name=6. {ECO:0000255}.; TRANSMEM 218 238 Helical; Name=7. {ECO:0000255}.; TRANSMEM 268 288 Helical; Name=8. {ECO:0000255}.; TRANSMEM 331 351 Helical; Name=9. {ECO:0000255}. FUNCTION: May function as sterol isomerase. {ECO:0000250|UniProtKB:Q9BZW5}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:25422095}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Broad expression. {ECO:0000269|PubMed:25422095}. +Q9JIQ8 TMPS2_MOUSE Transmembrane protease serine 2 (EC 3.4.21.-) (Epitheliasin) (Plasmic transmembrane protein X) [Cleaved into: Transmembrane protease serine 2 non-catalytic chain; Transmembrane protease serine 2 catalytic chain] 490 53,526 Active site (3); Chain (2); Disulfide bond (9); Domain (3); Glycosylation (3); Sequence conflict (12); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 84 104 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 83 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 105 490 Extracellular. {ECO:0000255}. FUNCTION: Serine protease that proteolytically cleaves and activates the viral spike glycoproteins which facilitate virus-cell membrane fusions. The spike proteins are synthesized and maintained in precursor intermediate folding states and proteolysis permits the refolding and energy release required to create stable virus-cell linkages and membrane coalescence. Facilitates human SARS coronavirus (SARS-CoV) infection via two independent mechanisms, proteolytic cleavage of ACE2, which might promote viral uptake, and cleavage of coronavirus spike glycoprotein which activates the glycoprotein for cathepsin L-independent host cell entry. Proteolytically cleaves and activates the spike glycoproteins of human coronavirus 229E (HCoV-229E) and human coronavirus EMC (HCoV-EMC) and the fusion glycoproteins F0 of Sendai virus (SeV), human metapneumovirus (HMPV), human parainfluenza 1, 2, 3, 4a and 4b viruses (HPIV). Essential for spread and pathogenesis of influenza A virus (strains H1N1, H3N2 and H7N9) and is involved in proteolytic cleavage and activation of hemagglutinin (HA) protein which is essential for viral infectivity. {ECO:0000269|PubMed:24227843, ECO:0000269|PubMed:24348248, ECO:0000269|PubMed:24522916, ECO:0000269|PubMed:24600012}. PTM: Proteolytically processed; by an autocatalytic mechanism. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O15393}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:O15393}.; SUBCELLULAR LOCATION: Transmembrane protease serine 2 catalytic chain: Secreted {ECO:0000250|UniProtKB:O15393}. Note=Activated by cleavage and secreted. {ECO:0000250|UniProtKB:O15393}. SUBUNIT: The catalytically active form interacts with ACE2. {ECO:0000250|UniProtKB:O15393}. TISSUE SPECIFICITY: Larynx, trachea and bronchi, lung, prostate and kidney. {ECO:0000269|PubMed:11169526, ECO:0000269|PubMed:24522916}. +P09225 TNFB_MOUSE Lymphotoxin-alpha (LT-alpha) (TNF-beta) (Tumor necrosis factor ligand superfamily member 1) 202 21,999 Chain (1); Glycosylation (1); Sequence conflict (2); Signal peptide (1) FUNCTION: Cytokine that in its homotrimeric form binds to TNFRSF1A/TNFR1, TNFRSF1B/TNFBR and TNFRSF14/HVEM (By similarity). In its heterotrimeric form with LTB binds to TNFRSF3/LTBR. Lymphotoxin is produced by lymphocytes and is cytotoxic for a wide range of tumor cells in vitro and in vivo. {ECO:0000250|UniProtKB:P01374}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Membrane {ECO:0000250}. Note=The homotrimer is secreted. The heterotrimer is membrane-associated. {ECO:0000250}. SUBUNIT: Homotrimer, and heterotrimer of either two LTB and one LTA subunits or (less prevalent) two LTA and one LTB subunits. Interacts with TNFRSF14. {ECO:0000250|UniProtKB:P01374}. +P69525 TMPS9_MOUSE Transmembrane protease serine 9 (EC 3.4.21.-) (Polyserase-I) (Polyserine protease 1) (Polyserase-1) [Cleaved into: Serase-1; Serase-2; Serase-3] 1065 114,486 Active site (6); Chain (4); Disulfide bond (15); Domain (4); Glycosylation (4); Site (3); Topological domain (2); Transmembrane (1) TRANSMEM 32 52 Helical. {ECO:0000255}. TOPO_DOM 3 31 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 53 1065 Extracellular. {ECO:0000255}. FUNCTION: Serase-1 and serase-2 are serine proteases that hydrolyze the peptides N-t-Boc-Gln-Ala-Arg-AMC and N-t-Boc-Gln-Gly-Arg-AMC. In contrast, N-t-Boc-Ala-Phe-Lys-AMC and N-t-Boc-Ala-Pro-Ala-AMC are not significantly hydrolyzed (By similarity). {ECO:0000250}. PTM: Proteolytically cleaved to generate 3 independent serine protease chains. The cleaved chains may remain attached to the membrane thanks to disulfide bonds. It is unclear whether cleavage always takes place (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. DOMAIN: The serine protease 1 and 2 domains are catalytically active, whereas the serine protease 3 domain lacks the essential Ser residue of the catalytic triad at position 1015 and is predicted to be inactive. {ECO:0000250}. +Q9JJG6 TMM47_MOUSE Transmembrane protein 47 (Transmembrane 4 superfamily member 10) 181 19,995 Alternative sequence (1); Chain (1); Frameshift (1); Initiator methionine (1); Modified residue (1); Transmembrane (4) TRANSMEM 21 41 Helical. {ECO:0000255}.; TRANSMEM 83 103 Helical. {ECO:0000255}.; TRANSMEM 115 135 Helical. {ECO:0000255}.; TRANSMEM 152 172 Helical. {ECO:0000255}. FUNCTION: Regulates cell junction organization in epithelial cells. May play a role in the transition from adherens junction to tight junction assembly. May regulate F-actin polymerization required for tight junctional localization dynamics and affect the junctional localization of PARD6B (PubMed:26990309). During podocyte differentiation may negatively regulate activity of FYN and subsequently the abundance of nephrin (PubMed:21881001). {ECO:0000269|PubMed:21881001, ECO:0000269|PubMed:26990309}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cell junction {ECO:0000269|PubMed:17195181, ECO:0000269|PubMed:26990309}. Cell junction, adherens junction {ECO:0000250|UniProtKB:Q9XSV3}. Note=In undifferentiated cultured podocytes localizes to the perinuclear region and translocates to the cell membrane after Cadherin appearance at cell-cell contacts. Upon differentiation of cultured podocytes, protein disappears from cell contacts and expression ceases. Re-expressed upon induced podocyte injury. Colocalizes with FYB1 at cell-cell contacts in podocytes. {ECO:0000269|PubMed:17195181, ECO:0000269|PubMed:21881001}. SUBUNIT: Interacts with CTNNB1, CTNNA1, PRKCI, PARD6B (By similarity). Interacts with FYB1. {ECO:0000250|UniProtKB:Q9XSV3, ECO:0000269|PubMed:21881001}. TISSUE SPECIFICITY: Expressed in podocytes (at protein level). {ECO:0000269|PubMed:21881001}. +Q6P2B1 TNPO3_MOUSE Transportin-3 923 104,170 Alternative sequence (3); Chain (1); Modified residue (4) FUNCTION: Seems to function in nuclear protein import as nuclear transport receptor. In vitro, mediates the nuclear import of splicing factor SR proteins RBM4, SFRS1 and SFRS2, by recognizing phosphorylated RS domains (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Interacts with phosphorylated SFRS1 and SFRS2. Interacts with NUP62 and RBM4 (By similarity). {ECO:0000250}. +P32972 TNFL8_MOUSE Tumor necrosis factor ligand superfamily member 8 (CD30 ligand) (CD30-L) (CD antigen CD153) 239 26,519 Chain (1); Disulfide bond (1); Glycosylation (6); Topological domain (2); Transmembrane (1) TRANSMEM 44 67 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 43 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 68 239 Extracellular. {ECO:0000255}. FUNCTION: Cytokine that binds to TNFRSF8/CD30. Induces proliferation of T-cells. SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. SUBUNIT: Homotrimer. {ECO:0000305}. +P41274 TNFL9_MOUSE Tumor necrosis factor ligand superfamily member 9 (4-1BB ligand) (4-1BBL) 309 33,853 Chain (1); Glycosylation (3); Topological domain (2); Transmembrane (1) TRANSMEM 83 103 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 82 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 104 309 Extracellular. {ECO:0000255}. FUNCTION: Cytokine that binds to TNFRSF9. Induces the proliferation of activated peripheral blood T-cells. May have a role in activation-induced cell death (AICD). May play a role in cognate interactions between T-cells and B-cells/macrophages. SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. SUBUNIT: Homotrimer. {ECO:0000305}. +P27512 TNR5_MOUSE Tumor necrosis factor receptor superfamily member 5 (B-cell surface antigen CD40) (Bp50) (CD40L receptor) (CD antigen CD40) 289 32,093 Alternative sequence (7); Chain (1); Disulfide bond (8); Glycosylation (1); Repeat (4); Sequence conflict (13); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 194 215 Helical. {ECO:0000255}. TOPO_DOM 20 193 Extracellular. {ECO:0000255}.; TOPO_DOM 216 289 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for TNFSF5/CD40LG. Transduces TRAF6- and MAP3K8-mediated signals that activate ERK in macrophages and B cells, leading to induction of immunoglobulin secretion. {ECO:0000269|PubMed:12881420}. SUBCELLULAR LOCATION: Isoform I: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Isoform III: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Isoform IV: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Isoform V: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Isoform II: Secreted. SUBUNIT: Monomer and homodimer. Interacts with TRAF1, TRAF2 and TRAF6 (By similarity). Interacts with TRAF3 and TRAF5. Interacts with TRAF6 and MAP3K8; the interaction is required for ERK activation. {ECO:0000250, ECO:0000269|PubMed:12881420, ECO:0000269|PubMed:7533327, ECO:0000269|PubMed:8790348}. +Q9JHJ0 TMOD3_MOUSE Tropomodulin-3 (Ubiquitous tropomodulin) (U-Tmod) 352 39,503 Chain (1); Modified residue (1) FUNCTION: Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. SUBUNIT: Binds to the N-terminus of tropomyosin and to actin. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. +P25118 TNR1A_MOUSE Tumor necrosis factor receptor superfamily member 1A (Tumor necrosis factor receptor 1) (TNF-R1) (Tumor necrosis factor receptor type I) (TNF-RI) (TNFR-I) (p55) (p60) (CD antigen CD120a) 454 50,130 Chain (1); Disulfide bond (12); Domain (1); Glycosylation (3); Region (1); Repeat (4); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 213 235 Helical. {ECO:0000255}. TOPO_DOM 30 212 Extracellular. {ECO:0000255}.; TOPO_DOM 236 454 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for TNFSF2/TNF-alpha and homotrimeric TNFSF1/lymphotoxin-alpha. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Golgi apparatus membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Binding of TNF to the extracellular domain leads to homotrimerization. The aggregated death domains provide a novel molecular interface that interacts specifically with the death domain of TRADD. Various TRADD-interacting proteins such as TRAFS, RIPK1 and possibly FADD, are recruited to the complex by their association with TRADD. This complex activates at least two distinct signaling cascades, apoptosis and NF-kappa-B signaling. Interacts with BAG4, BABAM2, FEM1B, GRB2, SQSTM1 and TRPC4AP. Interacts with DAB2IP (By similarity). Interacts directly with NOL3 (via CARD domain); inhibits TNF-signaling pathway (PubMed:24440909). Interacts with SH3RF2, TRADD and RIPK1. SH3RF2 facilitates the recruitment of RIPK1 and TRADD to TNFRSF1A in a TNF-alpha-dependent process (By similarity). {ECO:0000250|UniProtKB:P19438, ECO:0000269|PubMed:24440909}. DOMAIN: Both the cytoplasmic membrane-proximal region and the C-terminal region containing the death domain are involved in the interaction with TRPC4AP. +Q9EPU5 TNR21_MOUSE Tumor necrosis factor receptor superfamily member 21 (Death receptor 6) (CD antigen CD358) 655 71,983 Beta strand (16); Chain (1); Disulfide bond (9); Domain (1); Glycosylation (6); Helix (1); Lipidation (1); Repeat (4); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 350 370 Helical. {ECO:0000255}. TOPO_DOM 42 349 Extracellular. {ECO:0000255}.; TOPO_DOM 371 655 Cytoplasmic. {ECO:0000255}. FUNCTION: Promotes apoptosis, possibly via a pathway that involves the activation of NF-kappa-B. Can also promote apoptosis mediated by BAX and by the release of cytochrome c from the mitochondria into the cytoplasm. Plays a role in neuronal apoptosis, including apoptosis in response to amyloid peptides derived from APP, and is required for both normal cell body death and axonal pruning. Trophic-factor deprivation triggers the cleavage of surface APP by beta-secretase to release sAPP-beta which is further cleaved to release an N-terminal fragment of APP (N-APP). N-APP binds TNFRSF21; this triggers caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6). Negatively regulates oligodendrocyte survival, maturation and myelination. Plays a role in signaling cascades triggered by stimulation of T-cell receptors, in the adaptive immune response and in the regulation of T-cell differentiation and proliferation. Negatively regulates T-cell responses and the release of cytokines such as IL4, IL5, IL10, IL13 and IFNG by Th2 cells. Negatively regulates the production of IgG, IgM and IgM in response to antigens. May inhibit the activation of JNK in response to T-cell stimulation. {ECO:0000269|PubMed:11485735, ECO:0000269|PubMed:11714751, ECO:0000269|PubMed:12515813, ECO:0000269|PubMed:19225519, ECO:0000269|PubMed:21725297, ECO:0000269|PubMed:23559013}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12515813}; Single-pass type I membrane protein {ECO:0000269|PubMed:12515813}. SUBUNIT: Associates with TRADD. Interacts with NGFR (By similarity). Interacts with N-APP. {ECO:0000250, ECO:0000269|PubMed:19225519}. TISSUE SPECIFICITY: Detected in spleen B-cells (at protein level). Ubiquitous. Highly expressed in adult spleen, thymus, testis, prostate, ovary, small intestine, colon, brain, lung and kidney, and in fetal brain, liver and lung. Detected at lower levels in adult peripheral blood leukocytes, lung, and in fetal muscle, heart, kidney, small intestine and skin. Detected in T-cells, B-cells and monocytes. In T-cells expression is highest in Th0 cells, intermediate in Th2 cells and lower in Th1 cells. Expressed at low levels in proliferating progenitors in the spinal cord, but is highly expressed by differentiating neurons within the spinal cord and adjacent dorsal root ganglia. Expressed by developing neurons as they differentiate and enter a pro-apoptotic state. Expressed by both cell bodies and axons. {ECO:0000269|PubMed:11485735, ECO:0000269|PubMed:11714751, ECO:0000269|PubMed:12515813, ECO:0000269|PubMed:19225519}. +Q9ER62 TNR22_MOUSE Tumor necrosis factor receptor superfamily member 22 (Decoy TRAIL receptor 2) (TNF receptor family member SOBa) (TNF receptor homolog 2) (Tumor necrosis factor receptor p60 homolog 2) 198 22,375 Alternative sequence (1); Chain (1); Disulfide bond (9); Erroneous gene model prediction (1); Erroneous initiation (1); Frameshift (1); Glycosylation (2); Repeat (3); Sequence conflict (3); Topological domain (2); Transmembrane (1) TRANSMEM 21 41 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 20 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 42 198 Extracellular. {ECO:0000255}. FUNCTION: Receptor for the cytotoxic ligand TNFSF10/TRAIL. Lacks a cytoplasmic death domain and hence is not capable of inducing apoptosis. Protects cells against TRAIL mediated apoptosis possibly through ligand competition. Cannot induce the NF-kappa-B pathway. {ECO:0000269|PubMed:12466268}. SUBCELLULAR LOCATION: Isoform 1: Cell membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: Isoform 2: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Ubiquitous. +Q9ER63 TNR23_MOUSE Tumor necrosis factor receptor superfamily member 23 (Decoy TRAIL receptor 1) (TNF receptor family member SOB) (TNF receptor homolog 1) (Tumor necrosis factor receptor p60 homolog 1) 176 19,595 Chain (1); Disulfide bond (9); Glycosylation (1); Lipidation (1); Propeptide (1); Repeat (3); Signal peptide (1) FUNCTION: Receptor for the cytotoxic ligand TRAIL. Lacks a cytoplasmic death domain and hence is not capable of inducing apoptosis. May protect cells against TRAIL mediated apoptosis through ligand competition. Cannot induce the NF-kappa-B pathway. {ECO:0000269|PubMed:12466268}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12466268}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:12466268}. TISSUE SPECIFICITY: Ubiquitous. +P83626 TNR26_MOUSE Tumor necrosis factor receptor superfamily member 26 (TNF receptor homolog 3) 204 22,708 Chain (1); Compositional bias (1); Disulfide bond (9); Glycosylation (2); Repeat (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 165 185 Helical. {ECO:0000255}. TOPO_DOM 20 164 Extracellular. {ECO:0000255}.; TOPO_DOM 186 204 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in thymus and spleen. Detectable levels in lung. {ECO:0000269|PubMed:12466268}. +P06804 TNFA_MOUSE Tumor necrosis factor (Cachectin) (TNF-alpha) (Tumor necrosis factor ligand superfamily member 2) (TNF-a) [Cleaved into: Tumor necrosis factor, membrane form (N-terminal fragment) (NTF); Intracellular domain 1 (ICD1); Intracellular domain 2 (ICD2); C-domain 1; C-domain 2; Tumor necrosis factor, soluble form] 235 25,896 Beta strand (12); Chain (6); Disulfide bond (1); Glycosylation (2); Helix (1); Lipidation (1); Modified residue (1); Natural variant (2); Sequence conflict (3); Site (5); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 36 56 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 35 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 57 235 Extracellular. {ECO:0000255}. FUNCTION: Cytokine that binds to TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR. It is mainly secreted by macrophages and can induce cell death of certain tumor cell lines. It is potent pyrogen causing fever by direct action or by stimulation of interleukin-1 secretion and is implicated in the induction of cachexia, Under certain conditions it can stimulate cell proliferation and induce cell differentiation (By similarity). Induces insulin resistance in adipocytes via inhibition of insulin-induced IRS1 tyrosine phosphorylation and insulin-induced glucose uptake. Induces GKAP42 protein degradation in adipocytes which is partially responsible for TNF-induced insulin resistance (PubMed:25586176). {ECO:0000250|UniProtKB:P01375, ECO:0000269|PubMed:25586176}.; FUNCTION: The TNF intracellular domain (ICD) form induces IL12 production in dendritic cells. {ECO:0000250|UniProtKB:P01375}. PTM: The membrane-bound form is further proteolytically processed by SPPL2A or SPPL2B through regulated intramembrane proteolysis producing TNF intracellular domains (ICD1 and ICD2) released in the cytosol and TNF C-domain 1 and C-domain 2 secreted into the extracellular space (By similarity). The soluble form derives from the membrane form by proteolytic processing. {ECO:0000250}.; PTM: The membrane form, but not the soluble form, is phosphorylated on serine residues. Dephosphorylation of the membrane form occurs by binding to soluble TNFRSF1A/TNFR1 (By similarity). {ECO:0000250}.; PTM: O-glycosylated; glycans contain galactose, N-acetylgalactosamine and N-acetylneuraminic acid. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein.; SUBCELLULAR LOCATION: Tumor necrosis factor, membrane form: Membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: Tumor necrosis factor, soluble form: Secreted.; SUBCELLULAR LOCATION: C-domain 1: Secreted {ECO:0000250}.; SUBCELLULAR LOCATION: C-domain 2: Secreted {ECO:0000250}. SUBUNIT: Interacts with SPPL2B (By similarity). Homotrimer. {ECO:0000250}. +Q9CYG7 TOM34_MOUSE Mitochondrial import receptor subunit TOM34 (Translocase of outer membrane 34 kDa subunit) 309 34,278 Alternative sequence (1); Chain (1); Cross-link (1); Modified residue (4); Repeat (6); Sequence conflict (2) FUNCTION: Plays a role in the import of cytosolically synthesized preproteins into mitochondria. Binds the mature portion of precursor proteins. Interacts with cellular components, and possesses weak ATPase activity. May be a chaperone-like protein that helps to keep newly synthesized precursors in an unfolded import compatible state (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Mitochondrion outer membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. SUBUNIT: Interacts with HSP90A, VCP, ATP6M, KIAA0665, AMPK, and DMAP1 through its TPR repeat. {ECO:0000250}. TISSUE SPECIFICITY: Isoform 1 is ubiquitously expressed while isoform 2 is expressed only in mature testicular germ cells. Isoform 1 is expressed in all testicular cells. Isoform 2 is highly expressed in early to late pachytene cells but expression is significantly decreased in round spermatid cells. {ECO:0000269|PubMed:12801914}. +A1Y9I9 TOMT_MOUSE Transmembrane O-methyltransferase homolog (mTOMT) (EC 2.1.1.6) (Catechol O-methyltransferase 2) (Protein LRTOMT2) 258 28,846 Binding site (4); Chain (1); Mutagenesis (4); Region (1) FUNCTION: Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones (PubMed:18794526). Required for auditory function (PubMed:18794526, PubMed:28504928). Component of the cochlear hair cell's mechanotransduction (MET) machinery. Involved in the assembly of the asymmetric tip-link MET complex. Required for transportation of TMC1 and TMC2 proteins into the mechanically sensitive stereocilia of the hair cells. The function in MET is independent of the enzymatic activity (PubMed:28504928). {ECO:0000269|PubMed:18794526, ECO:0000269|PubMed:28504928}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18953341, ECO:0000269|PubMed:28504928}. Endoplasmic reticulum {ECO:0000269|PubMed:28504928}. Note=Localized to the cell body of the cochlear hair cells, but is not present in the stereocilia. Present but not restricted to the apical cistern, Hensen's body and the subsurface cistern. {ECO:0000269|PubMed:28504928}. SUBUNIT: Interacts with LHFPL5, PCDH15, TMC1, TMC2 and TMIE (PubMed:28504928). The interaction of TOMT with TMC1 and TMC2 is required for the transportation of TMC1/2 into the stereocilia of hair cells (PubMed:28504928, PubMed:28534737). Interacts directly with TMC1 (PubMed:28534737). {ECO:0000269|PubMed:28504928, ECO:0000269|PubMed:28534737}. TISSUE SPECIFICITY: Widely expressed with high levels in outer and inner hair cells of the cochlea and vestibule. {ECO:0000269|PubMed:18794526, ECO:0000269|PubMed:18953341}. +Q62393 TPD52_MOUSE Tumor protein D52 (mD52) 224 24,313 Alternative sequence (2); Chain (1); Coiled coil (1); Modified residue (6); Sequence conflict (1) SUBUNIT: Forms a homodimer or heterodimer with other members of the family. {ECO:0000250}. TISSUE SPECIFICITY: Isoform 2 is expressed at higher levels in kidney and brain than in liver, lung, testis and heart. Within the brain, isoform 2 is highly expressed in the granular layer of the cerebellum, the cortex and the hippocampus. In embryos, isoform 2 is expressed in the epithelium of the developing intestine, stomach, olfactory epithelium, neuronal layers of the retina, salivary gland, kidney and dorsal root ganglion. {ECO:0000269|PubMed:8632896}. +Q99MU1 TPRA1_MOUSE Transmembrane protein adipocyte-associated 1 (Integral membrane protein GPR175) (TPRA40) (Transmembrane domain protein of 40 kDa regulated in adipocytes) 369 40,578 Chain (1); Frameshift (1); Glycosylation (2); Transmembrane (7) TRANSMEM 45 65 Helical; Name=1. {ECO:0000255}.; TRANSMEM 73 93 Helical; Name=2. {ECO:0000255}.; TRANSMEM 120 140 Helical; Name=3. {ECO:0000255}.; TRANSMEM 148 168 Helical; Name=4. {ECO:0000255}.; TRANSMEM 189 209 Helical; Name=5. {ECO:0000255}.; TRANSMEM 237 257 Helical; Name=6. {ECO:0000255}.; TRANSMEM 262 282 Helical; Name=7. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Ubiquitous, with higher levels in heart, brain, lung, liver and kidney. {ECO:0000269|PubMed:10342878}. +Q7M717 TR102_MOUSE Taste receptor type 2 member 102 (T2R102) (mT2R51) (STC9-7) 329 38,450 Chain (1); Erroneous initiation (1); Glycosylation (1); Sequence conflict (2); Topological domain (8); Transmembrane (7) TRANSMEM 10 30 Helical; Name=1. {ECO:0000255}.; TRANSMEM 48 68 Helical; Name=2. {ECO:0000255}.; TRANSMEM 86 108 Helical; Name=3. {ECO:0000255}.; TRANSMEM 130 150 Helical; Name=4. {ECO:0000255}.; TRANSMEM 182 202 Helical; Name=5. {ECO:0000255}.; TRANSMEM 232 252 Helical; Name=6. {ECO:0000255}.; TRANSMEM 263 283 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 9 Extracellular. {ECO:0000255}.; TOPO_DOM 31 47 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 69 85 Extracellular. {ECO:0000255}.; TOPO_DOM 109 129 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 151 181 Extracellular. {ECO:0000255}.; TOPO_DOM 203 231 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 253 262 Extracellular. {ECO:0000255}.; TOPO_DOM 284 329 Cytoplasmic. {ECO:0000255}. FUNCTION: Putative taste receptor which may play a role in the perception of bitterness. {ECO:0000305}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9JKT4 TR105_MOUSE Taste receptor type 2 member 105 (T2R105) (Taste receptor type 2 member 5) (T2R5) (Taste receptor type 2 member 9) (T2R9) 300 34,416 Chain (1); Glycosylation (1); Natural variant (3); Topological domain (8); Transmembrane (7) TRANSMEM 8 28 Helical; Name=1. {ECO:0000255}.; TRANSMEM 44 64 Helical; Name=2. {ECO:0000255}.; TRANSMEM 88 108 Helical; Name=3. {ECO:0000255}.; TRANSMEM 129 149 Helical; Name=4. {ECO:0000255}.; TRANSMEM 182 202 Helical; Name=5. {ECO:0000255}.; TRANSMEM 234 254 Helical; Name=6. {ECO:0000255}.; TRANSMEM 260 280 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 7 Extracellular. {ECO:0000255}.; TOPO_DOM 29 43 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 65 87 Extracellular. {ECO:0000255}.; TOPO_DOM 109 128 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 150 181 Extracellular. {ECO:0000255}.; TOPO_DOM 203 233 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 255 259 Extracellular. {ECO:0000255}.; TOPO_DOM 281 300 Cytoplasmic. {ECO:0000255}. FUNCTION: Gustducin-coupled cycloheximide receptor implicated in the perception of bitter compounds in the oral cavity and the gastrointestinal tract. Signals through PLCB2 and the calcium-regulated cation channel TRPM5. {ECO:0000269|PubMed:10761935, ECO:0000269|PubMed:15759003}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed in subsets of taste receptor cells of the tongue and palate epithelium and exclusively in gustducin-positive cells. Expressed in gastric and duodenal tissues. +P20065 TYB4_MOUSE Thymosin beta-4 (T beta 4) [Cleaved into: Hematopoietic system regulatory peptide (Seraspenide)] 50 5,679 Alternative sequence (1); Chain (1); Cross-link (1); Modified residue (9); Peptide (1) FUNCTION: Plays an important role in the organization of the cytoskeleton. Binds to and sequesters actin monomers (G actin) and therefore inhibits actin polymerization.; FUNCTION: Seraspenide inhibits the entry of hematopoietic pluripotent stem cells into the S-phase. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SUBUNIT: Interacts with SERPINB1. Identified in a complex composed of ACTA1, COBL, GSN AND TMSB4X (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Originally found in thymus but it is widely distributed in many tissues. +Q8BG60 TXNIP_MOUSE Thioredoxin-interacting protein (Vitamin D3 up-regulated protein 1) 397 44,363 Alternative sequence (1); Chain (1); Cross-link (1); Disulfide bond (1); Modified residue (1); Sequence conflict (7) FUNCTION: May act as an oxidative stress mediator by inhibiting thioredoxin activity or by limiting its bioavailability. Interacts with COPS5 and restores COPS5-induced suppression of CDKN1B stability, blocking the COPS5-mediated translocation of CDKN1B from the nucleus to the cytoplasm. Inhibits the proteasomal degradation of DDIT4, and thereby contributes to the inhibition of the mammalian target of rapamycin complex 1 (mTORC1) (By similarity). Functions as a transcriptional repressor, possibly by acting as a bridge molecule between transcription factors and corepressor complexes, and over-expression will induce G0/G1 cell cycle arrest. Required for the maturation of natural killer cells. Acts as a suppressor of tumor cell growth. {ECO:0000250, ECO:0000269|PubMed:15723808, ECO:0000269|PubMed:15930262}. PTM: Ubiquitinated; undergoes polyubiquitination catalyzed by ITCH resulting in proteasomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10843682}. SUBUNIT: Homodimer; disulfide-linked. Interacts with TXN/thioredoxin through its redox-active site. Interacts with transcriptional repressors ZBTB16, ZBTB32 and HDAC1. Interacts (via C-terminus) with ITCH (via WW domains). Interacts with DDIT4 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:10843682}. +Q9R117 TYK2_MOUSE Non-receptor tyrosine-protein kinase TYK2 (EC 2.7.10.2) 1184 133,315 Active site (1); Beta strand (11); Binding site (1); Chain (1); Domain (4); Erroneous gene model prediction (1); Erroneous initiation (2); Helix (16); Modified residue (5); Nucleotide binding (1); Sequence conflict (5); Turn (1) FUNCTION: Involved in intracellular signal transduction by amplifying type I and type II IFN signaling. Phosphorylates the interferon-alpha/beta receptor alpha chain. Plays an essential role in promoting selective immune responses, including innate host defense mechanisms and specific antiviral activities. SUBUNIT: Interacts with JAKMIP1. {ECO:0000250}. DOMAIN: The FERM domain mediates interaction with JAKMIP1. {ECO:0000250}. +O54885 TYOBP_MOUSE TYRO protein tyrosine kinase-binding protein (DNAX-activation protein 12) (Killer-activating receptor-associated protein) (KAR-associated protein) 114 12,367 Chain (1); Disulfide bond (1); Domain (1); Modified residue (2); Sequence conflict (1); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 43 63 Helical. {ECO:0000255}. TOPO_DOM 22 42 Extracellular. {ECO:0000255}.; TOPO_DOM 64 114 Cytoplasmic. {ECO:0000255}. FUNCTION: Non-covalently associates with activating receptors of the CD300 family. Cross-linking of CD300-TYROBP complexes results in cellular activation. Involved for instance in neutrophil activation mediated by integrin. {ECO:0000269|PubMed:17086186}. PTM: Tyrosine phosphorylated. {ECO:0000269|PubMed:11754004, ECO:0000269|PubMed:12426565, ECO:0000269|PubMed:17086186, ECO:0000269|PubMed:9490415, ECO:0000269|PubMed:9852069}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Homodimer; disulfide-linked. Interacts with SIRPB1 and TREM1. Interacts with SIGLEC14 (By similarity). Interacts with CLECSF5 (PubMed:10449773). Interacts with CD300LB and CD300D (PubMed:12874256, PubMed:12893283, PubMed:17202337, PubMed:17928527). Interacts with CD300E. Interacts (via ITAM domain) with SYK (via SH2 domains); activates SYK mediating neutrophils and macrophages integrin-mediated activation (PubMed:17086186). Interacts (via transmembrane domain) with KLRK1 isoform 2 (via transmembrane domain); the interaction is required for KLRK1 NK cell surface expression and induce NK cell-mediated cytotoxicity (PubMed:12426564, PubMed:12426565, PubMed:15294961). Interacts with KLRC2 (By similarity). Interacts with TREM3 (PubMed:11754004). Interacts with CD300H (By similarity). {ECO:0000250|UniProtKB:O43914, ECO:0000269|PubMed:10449773, ECO:0000269|PubMed:11754004, ECO:0000269|PubMed:12426564, ECO:0000269|PubMed:12426565, ECO:0000269|PubMed:12874256, ECO:0000269|PubMed:12893283, ECO:0000269|PubMed:15294961, ECO:0000269|PubMed:17086186, ECO:0000269|PubMed:17202337, ECO:0000269|PubMed:17928527}. +Q8JZU2 TXTP_MOUSE Tricarboxylate transport protein, mitochondrial (Citrate transport protein) (CTP) (Solute carrier family 25 member 1) (Tricarboxylate carrier protein) 311 33,931 Chain (1); Modified residue (1); Repeat (3); Sequence conflict (2); Transit peptide (1); Transmembrane (6) TRANSMEM 29 46 Helical; Name=1. {ECO:0000255}.; TRANSMEM 86 105 Helical; Name=2. {ECO:0000255}.; TRANSMEM 129 143 Helical; Name=3. {ECO:0000255}.; TRANSMEM 183 202 Helical; Name=4. {ECO:0000255}.; TRANSMEM 224 241 Helical; Name=5. {ECO:0000255}.; TRANSMEM 278 297 Helical; Name=6. {ECO:0000255}. FUNCTION: Involved in citrate-H(+)/malate exchange. Important for the bioenergetics of hepatic cells as it provides a carbon source for fatty acid and sterol biosyntheses, and NAD(+) for the glycolytic pathway. {ECO:0000250|UniProtKB:P53007}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P53007, ECO:0000269|PubMed:18775783}; Multi-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Expressed minimally but ubiquitously throughout the adult brain. Detected at higher levels in the olfactory bulb, neocortex and cerebellum. Also expressed in a subset of large cells in the globus pallidus. {ECO:0000269|PubMed:18775783}. +P55144 TYRO3_MOUSE Tyrosine-protein kinase receptor TYRO3 (EC 2.7.10.1) (Etk2/tyro3) (TK19-2) (Tyrosine-protein kinase DTK) (Tyrosine-protein kinase RSE) (Tyrosine-protein kinase TIF) 880 96,208 Active site (1); Alternative sequence (2); Beta strand (7); Binding site (1); Chain (1); Disulfide bond (2); Domain (5); Erroneous initiation (2); Glycosylation (8); Helix (12); Modified residue (7); Nucleotide binding (1); Sequence conflict (8); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 420 440 Helical. {ECO:0000255}. TOPO_DOM 31 419 Extracellular. {ECO:0000255}.; TOPO_DOM 441 880 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to several ligands including TULP1 or GAS6. Regulates many physiological processes including cell survival, migration and differentiation. Ligand binding at the cell surface induces dimerization and autophosphorylation of TYRO3 on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with PIK3R1 and thereby enhances PI3-kinase activity. Activates the AKT survival pathway, including nuclear translocation of NF-kappa-B and up-regulation of transcription of NF-kappa-B-regulated genes. TYRO3 signaling plays a role in various processes such as neuron protection from excitotoxic injury, platelet aggregation and cytoskeleton reorganization. Plays also an important role in inhibition of Toll-like receptors (TLRs)-mediated innate immune response by activating STAT1, which selectively induces production of suppressors of cytokine signaling SOCS1 and SOCS3. {ECO:0000269|PubMed:15650770, ECO:0000269|PubMed:20363878, ECO:0000269|PubMed:21084607, ECO:0000269|PubMed:21291561}. PTM: Autophosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SUBUNIT: Monomer and homodimer. Interacts (via N-terminus) with extracellular ligands TULP1 and GAS6. Interacts with PIK3R1; this interaction increases PI3-kinase activity (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Abundant in the brain and lower levels in other tissues. +Q62377 U2AFM_MOUSE U2 small nuclear ribonucleoprotein auxiliary factor 35 kDa subunit-related protein 2 (CCCH type zinc finger, RNA-binding motif and serine/arginine rich protein 2) (U2(RNU2) small nuclear RNA auxiliary factor 1-like 2) (U2AF35-related protein) (URP) 462 55,358 Chain (1); Compositional bias (4); Cross-link (1); Domain (1); Modified residue (2); Zinc finger (2) FUNCTION: Pre-mRNA-binding protein required for splicing of both U2- and U12-type introns. Selectively interacts with the 3'-splice site of U2- and U12-type pre-mRNAs and promotes different steps in U2 and U12 intron splicing. Recruited to U12 pre-mRNAs in an ATP-dependent manner and is required for assembly of the prespliceosome, a precursor to other spliceosomal complexes. For U2-type introns, it is selectively and specifically required for the second step of splicing (By similarity). {ECO:0000250}. PTM: Phosphorylated in the RS domain by SRPK1. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the U11/U12 snRNPs that are part of the U12-type spliceosome. Interacts (via RS domain) with SRSF1 and SRSF2. Interacts with U2AF2/U2AF65 (By similarity). {ECO:0000250}. +Q6ZWY6 U2D2B_MOUSE Ubiquitin-conjugating enzyme E2 D2B (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme D2B) (Ubiquitin carrier protein D2B) (Ubiquitin-protein ligase D2B) 147 16,659 Active site (1); Chain (1) Protein modification; protein ubiquitination. FUNCTION: Catalyzes the covalent attachment of ubiquitin to other proteins. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Mediates ubiquitination of PEX5 and autoubiquitination of STUB1 and TRAF6. Involved in the signal-induced conjugation and subsequent degradation of NFKBIA, FBXW2-mediated GCM1 ubiquitination and degradation, MDM2-dependent degradation of p53/TP53 and the activation of MAVS in the mitochondria by DDX58/RIG-I in response to viral infection (By similarity). Plays a role in early maturation of the testis. {ECO:0000250|UniProtKB:P62837, ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000269|PubMed:16024774}. SUBUNIT: Interacts with CNOT4 (via RING domain). {ECO:0000250|UniProtKB:P62837}. TISSUE SPECIFICITY: Testis-specific. +Q6ZPJ3 UBE2O_MOUSE (E3-independent) E2 ubiquitin-conjugating enzyme UBE2O (EC 2.3.2.24) (E2/E3 hybrid ubiquitin-protein ligase UBE2O) (Ubiquitin carrier protein O) (Ubiquitin-conjugating enzyme E2 O) (Ubiquitin-conjugating enzyme E2 of 230 kDa) (Ubiquitin-conjugating enzyme E2-230K) (Ubiquitin-protein ligase O) 1288 140,834 Active site (1); Chain (1); Coiled coil (1); Compositional bias (1); Erroneous initiation (3); Frameshift (1); Modified residue (12); Sequence conflict (6) Protein modification; protein ubiquitination. FUNCTION: E2/E3 hybrid ubiquitin-protein ligase that displays both E2 and E3 ligase activities and mediates monoubiquitination of target proteins. Negatively regulates TRAF6-mediated NF-kappa-B activation independently of its E2 activity. Acts as a positive regulator of BMP7 signaling by mediating monoubiquitination of SMAD6, thereby regulating adipogenesis. Mediates monoubiquitination at different sites of the nuclear localization signal (NLS) of BAP1, leading to cytoplasmic retention of BAP1. Also able to monoubiquitinate the NLS of other chromatin-associated proteins, such as INO80 and CXXC1, affecting their subcellular location. Acts as a regulator of retrograde transport by assisting the TRIM27:MAGEL2 E3 ubiquitin ligase complex to mediate 'Lys-63'-linked ubiquitination of WASHC1, leading to promote endosomal F-actin assembly. {ECO:0000250|UniProtKB:Q9C0C9}. PTM: Phosphorylated. Phosphorylation affects subcellular location. {ECO:0000250|UniProtKB:Q9C0C9}.; PTM: Ubiquitinated: autoubiquitinates, possibly affecting its subcellular location. {ECO:0000250|UniProtKB:Q9C0C9}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9C0C9}. Nucleus {ECO:0000250|UniProtKB:Q9C0C9}. Note=Mainly localizes to the cytoplasm. {ECO:0000250|UniProtKB:Q9C0C9}. SUBUNIT: Interacts with CPNE1 (via VWFA domain) and CPNE4 (via VWFA domain) (PubMed:12522145). {ECO:0000269|PubMed:12522145}. TISSUE SPECIFICITY: Highly expressed in reticulocytes. {ECO:0000269|PubMed:7761435}. +Q02053 UBA1_MOUSE Ubiquitin-like modifier-activating enzyme 1 (EC 6.2.1.45) (Ubiquitin-activating enzyme E1) (Ubiquitin-activating enzyme E1 X) (Ubiquitin-like modifier-activating enzyme 1 X) 1058 117,809 Active site (1); Beta strand (7); Binding site (4); Chain (1); Frameshift (1); Helix (15); Initiator methionine (1); Modified residue (15); Nucleotide binding (1); Region (1); Repeat (2); Sequence conflict (1); Turn (2) Protein modification; protein ubiquitination. FUNCTION: Catalyzes the first step in ubiquitin conjugation to mark cellular proteins for degradation through the ubiquitin-proteasome system (PubMed:1511901). Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP. Essential for the formation of radiation-induced foci, timely DNA repair and for response to replication stress. Promotes the recruitment of TP53BP1 and BRCA1 at DNA damage sites. {ECO:0000250|UniProtKB:P22314, ECO:0000305|PubMed:1511901}. PTM: ISGylated. {ECO:0000269|PubMed:16139798}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P22314}. Mitochondrion {ECO:0000250|UniProtKB:P22314}. Nucleus {ECO:0000250|UniProtKB:P22314}. SUBUNIT: Monomer. Interacts with GAN (via BTB domain). TISSUE SPECIFICITY: Ubiquitously expressed. In testis, expressed in A spermatogonia and spermatids but at very low levels in pachytene spermatocytes. {ECO:0000269|PubMed:8948595}. +Q7TSS2 UB2Q1_MOUSE Ubiquitin-conjugating enzyme E2 Q1 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme Q1) (Galactosyl transferase-associated protein) (GTAP) (Ubiquitin carrier protein Q1) (Ubiquitin-protein ligase Q1) 422 46,173 Active site (1); Alternative sequence (1); Chain (1); Erroneous initiation (2); Modified residue (1); Mutagenesis (1); Sequence conflict (3) Protein modification; protein ubiquitination. FUNCTION: Catalyzes the covalent attachment of ubiquitin to other proteins (By similarity). Involved in female fertility and embryo implantation (PubMed:23108111). May be involved in hormonal homeostasis in females (PubMed:23108111). Involved in regulation of B4GALT1 cell surface expression, B4GALT1-mediated cell adhesion to laminin and embryoid body formation (PubMed:18511602). {ECO:0000250|UniProtKB:Q7Z7E8, ECO:0000269|PubMed:18511602, ECO:0000269|PubMed:23108111, ECO:0000303|PubMed:23108111}. PTM: Autoubiquitinated in vitro in the presence of NEDD4L. {ECO:0000250|UniProtKB:Q7Z7E8}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18511602}. Cell projection, filopodium {ECO:0000269|PubMed:18511602}. Cytoplasm, cytosol {ECO:0000269|PubMed:18511602}. SUBUNIT: Monomer and homodimer. Only the homodimer is linked to ubiquitin through thiolester activation. Interacts (via N-terminus) with B4GALT1 (via N-terminal cytoplasmic domain); the interaction is direct. {ECO:0000269|PubMed:18511602}. TISSUE SPECIFICITY: Expressed in liver, brain, heart, spleen, lung, kidney, muscle, ovary, epididymis, testis and placenta (PubMed:23108111). Also expressed in thymus and ES cells (PubMed:18511602). Only expressed in the uterus during pregnancy (PubMed:23108111). Expressed in oocytes and during subsequent embryonic development stages (4-cell stage, blastocyst, E8.5, E.13.5, E16.5 and E18.5) (PubMed:23108111). {ECO:0000269|PubMed:18511602, ECO:0000269|PubMed:23108111}. +Q921J4 UBE2S_MOUSE Ubiquitin-conjugating enzyme E2 S (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme S) (Ubiquitin carrier protein S) (Ubiquitin-conjugating enzyme E2-24 kDa) (Ubiquitin-conjugating enzyme E2-EPF5) (Ubiquitin-protein ligase S) 223 24,183 Active site (1); Chain (1); Modified residue (2); Sequence conflict (1) Protein modification; protein ubiquitination. FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes 'Lys-11'-linked polyubiquitination. Acts as an essential factor of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated ubiquitin ligase that controls progression through mitosis. Acts by specifically elongating 'Lys-11'-linked polyubiquitin chains initiated by the E2 enzyme UBE2C/UBCH10 on APC/C substrates, enhancing the degradation of APC/C substrates by the proteasome and promoting mitotic exit. Also acts by elongating ubiquitin chains initiated by the E2 enzyme UBE2D1/UBCH5 in vitro; it is however unclear whether UBE2D1/UBCH5 acts as an E2 enzyme for the APC/C in vivo. Also involved in ubiquitination and subsequent degradation of VHL, resulting in an accumulation of HIF1A. In vitro able to promote polyubiquitination using all 7 ubiquitin Lys residues, except 'Lys-48'-linked polyubiquitination. {ECO:0000250|UniProtKB:Q16763}. PTM: Autoubiquitinated by the APC/C complex during G1, leading to its degradation by the proteasome. {ECO:0000250|UniProtKB:Q16763}. SUBUNIT: Component of the APC/C complex, composed of at least 14 distinct subunits that assemble into a complex of at least 19 chains with a combined molecular mass of around 1.2 MDa. Within this complex, directly interacts with ANAPC2 and ANAPC4. Interacts with CDC20, FZR1/CDH1 and VHL. {ECO:0000250|UniProtKB:Q16763}. +P52482 UB2E1_MOUSE Ubiquitin-conjugating enzyme E2 E1 (EC 2.3.2.23) ((E3-independent) E2 ubiquitin-conjugating enzyme E1) (EC 2.3.2.24) (E2 ubiquitin-conjugating enzyme E1) (UbcM3) (Ubiquitin carrier protein E1) (Ubiquitin-protein ligase E1) 193 21,333 Active site (1); Chain (1); Compositional bias (1); Cross-link (1); Initiator methionine (1); Modified residue (1) Protein modification; protein ubiquitination. FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes the covalent attachment of ISG15 to other proteins. Mediates the selective degradation of short-lived and abnormal proteins. In vitro also catalyzes 'Lys-48'-linked polyubiquitination. {ECO:0000250|UniProtKB:P51965}. PTM: ISGylation suppresses ubiquitin E2 enzyme activity. {ECO:0000250|UniProtKB:P51965}.; PTM: Autoubiquitinated. {ECO:0000250|UniProtKB:P51965}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P51965}. SUBUNIT: Interacts with RNF14. +P63147 UBE2B_MOUSE Ubiquitin-conjugating enzyme E2 B (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme B) (E214K) (RAD6 homolog B) (HR6B) (mHR6B) (Ubiquitin carrier protein B) (Ubiquitin-protein ligase B) 152 17,312 Active site (1); Chain (1); Sequence conflict (1) Protein modification; protein ubiquitination. FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In association with the E3 enzyme BRE1 (RNF20 and/or RNF40), it plays a role in transcription regulation by catalyzing the monoubiquitination of histone H2B at 'Lys-120' to form H2BK120ub1. H2BK120ub1 gives a specific tag for epigenetic transcriptional activation, elongation by RNA polymerase II, telomeric silencing, and is also a prerequisite for H3K4me and H3K79me formation. In vitro catalyzes 'Lys-11'-, as well as 'Lys-48'- and 'Lys-63'-linked polyubiquitination. Required for postreplication repair of UV-damaged DNA. Associates to the E3 ligase RAD18 to form the UBE2B-RAD18 ubiquitin ligase complex involved in mono-ubiquitination of DNA-associated PCNA on 'Lys-164'. May be involved in neurite outgrowth. {ECO:0000250|UniProtKB:P63146}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P63149}. Nucleus {ECO:0000250|UniProtKB:P63149}. Note=In peripheral neurons, expressed both at the plasma membrane and in nuclei. {ECO:0000250|UniProtKB:P63149}. SUBUNIT: Interacts with RAD18, UBR2 and WAC. {ECO:0000269|PubMed:14585983}. +P62257 UBE2H_MOUSE Ubiquitin-conjugating enzyme E2 H (EC 2.3.2.23) ((E3-independent) E2 ubiquitin-conjugating enzyme H) (EC 2.3.2.24) (E2 ubiquitin-conjugating enzyme H) (UBCH2) (Ubiquitin carrier protein H) (Ubiquitin-conjugating enzyme E2-20K) (Ubiquitin-protein ligase H) 183 20,655 Active site (1); Chain (1); Modified residue (1) Protein modification; protein ubiquitination. FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. E2 ubiquitin conjugating enzyme that transfers ubiquitin to MAEA, a core component of the CTLH E3 ubiquitin-protein ligase complex. In vitro catalyzes 'Lys-11'- and 'Lys-48'-linked polyubiquitination. Capable, in vitro, to ubiquitinate histone H2A. {ECO:0000250|UniProtKB:P62256}. PTM: Autoubiquitinated in vitro in the presence of NEDD4L. {ECO:0000250|UniProtKB:P62256}. SUBUNIT: Interacts with MAEA and WDR26, components of the CTLH complex that contains GID4, RANBP9 and/or RANBP10, MKLN1, MAEA, RMND5A (or alternatively its paralog RMND5B), GID8, ARMC8, WDR26 and YPEL5. {ECO:0000250|UniProtKB:P62256}. TISSUE SPECIFICITY: Detected in reticulocytes, lung, brain and skeletal muscle (at protein level) (PubMed:7761435). Ubiquitous. Detected in cardiac muscle, brain, spleen, lung, liver, skeletal muscle, kidney andmso testis (PubMed:7590289). {ECO:0000269|PubMed:7590289, ECO:0000269|PubMed:7761435}. +P21126 UBL4A_MOUSE Ubiquitin-like protein 4A (Ubiquitin-like protein GDX) 157 17,801 Chain (1); Cross-link (1); Domain (1); Modified residue (1); Region (1) FUNCTION: As part of a cytosolic protein quality control complex, the BAG6/BAT3 complex, maintains misfolded and hydrophobic patches-containing proteins in a soluble state and participates to their proper delivery to the endoplasmic reticulum or alternatively can promote their sorting to the proteasome where they undergo degradation. The BAG6/BAT3 complex is involved in the post-translational delivery of tail-anchored/type II transmembrane proteins to the endoplasmic reticulum membrane. Recruited to ribosomes, it interacts with the transmembrane region of newly synthesized tail-anchored proteins and together with SGTA and ASNA1 mediates their delivery to the endoplasmic reticulum. Client proteins that cannot be properly delivered to the endoplasmic reticulum are ubiquitinated and sorted to the proteasome. Similarly, the BAG6/BAT3 complex also functions as a sorting platform for proteins of the secretory pathway that are mislocalized to the cytosol either delivering them to the proteasome for degradation or to the endoplasmic reticulum. The BAG6/BAT3 complex also plays a role in the endoplasmic reticulum-associated degradation (ERAD), a quality control mechanism that eliminates unwanted proteins of the endoplasmic reticulum through their retrotranslocation to the cytosol and their targeting to the proteasome. It maintains these retrotranslocated proteins in an unfolded yet soluble state condition in the cytosol to ensure their proper delivery to the proteasome. {ECO:0000250|UniProtKB:P11441}. PTM: Polyubiquitinated. Ubiquitination by AMFR and deubiquitination by USP13 may regulate the interaction between the BAG6/BAT3 complex and SGTA and therefore may regulate client proteins fate. {ECO:0000250|UniProtKB:P11441}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P11441}. Nucleus {ECO:0000250|UniProtKB:P11441}. SUBUNIT: Component of the BAG6/BAT3 complex, at least composed of BAG6, UBL4A and GET4/TRC35. Interacts with BAG6; the interaction is direct and required for UBL4A protein stability. Interacts with USP13; may be indirect via BAG6. {ECO:0000250|UniProtKB:P11441}. +Q8BJQ2 UBP1_MOUSE Ubiquitin carboxyl-terminal hydrolase 1 (EC 3.4.19.12) (Deubiquitinating enzyme 1) (Ubiquitin thioesterase 1) (Ubiquitin-specific-processing protease 1) 784 87,456 Active site (2); Chain (1); Domain (1); Modified residue (5); Sequence conflict (3); Site (1) FUNCTION: Negative regulator of DNA damage repair which specifically deubiquitinates monoubiquitinated FANCD2. Also involved in PCNA-mediated translesion synthesis (TLS) by deubiquitinating monoubiquitinated PCNA. Has almost no deubiquitinating activity by itself and requires the interaction with WDR48 to have a high activity. {ECO:0000250|UniProtKB:O94782}. PTM: Autocatalytic cleavage of USP1 following UV irradiation inactivates it leading to an increase in ubiquitinated PCNA, recruitment of POLH and translesion synthesis. {ECO:0000250|UniProtKB:O94782}.; PTM: Ubiquitinated; leading to its subsequent proteasomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O94782}. SUBUNIT: Interacts with FANCD2 and PCNA. Interacts with WDR48. {ECO:0000250|UniProtKB:O94782}. +Q9JMA1 UBP14_MOUSE Ubiquitin carboxyl-terminal hydrolase 14 (EC 3.4.19.12) (Deubiquitinating enzyme 14) (Ubiquitin thioesterase 14) (Ubiquitin-specific-processing protease 14) 493 56,002 Active site (2); Beta strand (3); Chain (1); Domain (2); Helix (1); Modified residue (8); Sequence conflict (3); Turn (1) FUNCTION: Proteasome-associated deubiquitinase which releases ubiquitin from the proteasome targeted ubiquitinated proteins. Ensures the regeneration of ubiquitin at the proteasome. Is a reversibly associated subunit of the proteasome and a large fraction of proteasome-free protein exists within the cell. Required for the degradation of the chemokine receptor CXCR4 which is critical for CXCL12-induced cell chemotaxis. Serves also as a physiological inhibitor of endoplasmic reticulum-associated degradation (ERAD) under the non-stressed condition by inhibiting the degradation of unfolded endoplasmic reticulum proteins via interaction with ERN1. Plays a role in the innate immune defense against viruses by stabilizing the viral DNA sensor CGAS and thus inhibiting its autophagic degradation. {ECO:0000250|UniProtKB:P54578, ECO:0000269|PubMed:16190881, ECO:0000269|PubMed:19726649}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. SUBUNIT: Homodimer (Potential). Associates with the 26S proteasome. Interacts with FANCC, CXCR4 and ERN1. Interacts with TRIM14; this interaction recruits USP14 to cleave ubiquitin chains of CGAS (By similarity). {ECO:0000250|UniProtKB:P54578}. +Q8C6M1 UBP20_MOUSE Ubiquitin carboxyl-terminal hydrolase 20 (EC 3.4.19.12) (Deubiquitinating enzyme 20) (Ubiquitin thioesterase 20) (Ubiquitin-specific-processing protease 20) (VHL-interacting deubiquitinating enzyme 2) 916 102,140 Active site (2); Chain (1); Domain (3); Erroneous initiation (1); Modified residue (9); Sequence conflict (2); Zinc finger (1) FUNCTION: Deubiquitinating enzyme involved in beta-2 adrenergic receptor (ADRB2) recycling. Acts as a regulator of G-protein coupled receptor (GPCR) signaling by mediating the deubiquitination beta-2 adrenergic receptor (ADRB2). Plays a central role in ADRB2 recycling and resensitization after prolonged agonist stimulation by constitutively binding ADRB2, mediating deubiquitination of ADRB2 and inhibiting lysosomal trafficking of ADRB2. Upon dissociation, it is probably transferred to the translocated beta-arrestins, possibly leading to beta-arrestins deubiquitination and disengagement from ADRB2. This suggests the existence of a dynamic exchange between the ADRB2 and beta-arrestins. Deubiquitinates DIO2, thereby regulating thyroid hormone regulation. Deubiquitinates HIF1A, leading to stabilize HIF1A and enhance HIF1A-mediated activity. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By similarity). {ECO:0000250}. PTM: Ubiquitinated via a VHL-dependent pathway for proteasomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. SUBUNIT: Interacts with VHL, leading to its ubiquitination and subsequent degradation. Interacts with CCP110, DIO2 and HIF1A (By similarity). {ECO:0000250}. DOMAIN: The UBP-type zinc finger binds 3 zinc ions. However, it does not bind ubiquitin, probably because the conserved Arg in position 55 is replaced by a Glu residue (By similarity). {ECO:0000250}. +Q8R5H1 UBP15_MOUSE Ubiquitin carboxyl-terminal hydrolase 15 (EC 3.4.19.12) (Deubiquitinating enzyme 15) (Ubiquitin thioesterase 15) (Ubiquitin-specific-processing protease 15) 981 112,325 Active site (2); Alternative sequence (5); Chain (1); Domain (2); Erroneous initiation (2); Initiator methionine (1); Modified residue (7); Region (1); Sequence conflict (5) FUNCTION: Hydrolase that removes conjugated ubiquitin from target proteins and regulates various pathways such as the TGF-beta receptor signaling, NF-kappa-B and RNF41/NRDP1-PRKN pathways. Acts as a key regulator of TGF-beta receptor signaling pathway, but the precise mechanism is still unclear: according to a report, acts by promoting deubiquitination of monoubiquitinated R-SMADs (SMAD1, SMAD2 and/or SMAD3), thereby alleviating inhibition of R-SMADs and promoting activation of TGF-beta target genes. According to another reports, regulates the TGF-beta receptor signaling pathway by mediating deubiquitination and stabilization of TGFBR1, leading to an enhanced TGF-beta signal. Able to mediate deubiquitination of monoubiquitinated substrates as well as 'Lys-48'-linked polyubiquitin chains, protecting them against proteasomal degradation. May also regulate gene expression and/or DNA repair through the deubiquitination of histone H2B. Acts as an inhibitor of mitophagy by counteracting the action of parkin (PRKN): hydrolyzes cleavage of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains attached by parkin on target proteins such as MFN2, thereby reducing parkin's ability to drive mitophagy. Acts as an associated component of COP9 signalosome complex (CSN) and regulates different pathways via this association: regulates NF-kappa-B by mediating deubiquitination of NFKBIA and deubiquitinates substrates bound to VCP. Involved in endosome organization by mediating deubiquitination of SQSTM1: ubiquitinated SQSTM1 forms a molecular bridge that restrains cognate vesicles in the perinuclear region and its deubiquitination releases target vesicles for fast transport into the cell periphery. {ECO:0000250|UniProtKB:Q9Y4E8}. PTM: Phosphorylated. Phosphorylation protects against ubiquitination and subsequent degradation by the proteasome. {ECO:0000250|UniProtKB:Q9Y4E8}.; PTM: Ubiquitinated, leading to degradation by the proteasome. {ECO:0000250|UniProtKB:Q9Y4E8}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24852371}. Nucleus {ECO:0000250|UniProtKB:Q9Y4E8}. Mitochondrion {ECO:0000250|UniProtKB:Q9Y4E8}. SUBUNIT: A homodimer structure has been reported; however it is unclear whether the protein form a homodimer in vivo. Identified in a complex with the COP9 signalosome complex (CSN). Interacts with SMAD1, SMAD2 and SMAD3; the interaction is direct. Forms a complex with SMURF2 and SMAD7. Interacts with TGFBR1. Interacts with SART3; the interaction is direct. May interact with RNF20 and RNF40. May interact with PRKN. Interacts with INCA1. {ECO:0000250|UniProtKB:Q9Y4E8}. TISSUE SPECIFICITY: Widely expressed with highest levels in the brain and spleen, and lowest levels in the muscles (at protein level) (PubMed:24852371). In the midbrain, strong expression in neurons including the dopaminergic neurons (at protein level) (PubMed:24852371). Widely expressed with highest levels in testis, heart and liver (PubMed:12532266). {ECO:0000269|PubMed:12532266, ECO:0000269|PubMed:24852371}. +Q8CEG8 UBP27_MOUSE Ubiquitin carboxyl-terminal hydrolase 27 (EC 3.4.19.12) (Deubiquitinating enzyme 27) (Ubiquitin thioesterase 27) (Ubiquitin-specific-processing protease 27) (X-linked ubiquitin carboxyl-terminal hydrolase 27) 438 49,599 Active site (2); Chain (1); Domain (1); Erroneous initiation (3); Frameshift (1); Mutagenesis (1); Sequence conflict (4) FUNCTION: Deubiquitinase that can reduce the levels of BCL2L11/BIM ubiquitination and stabilize BCL2L11 in response to the RAF-MAPK-degradation signal. By acting on BCL2L11 levels, may counteract the anti-apoptotic effects of MAPK activity. {ECO:0000269|PubMed:27013495}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:27013495}. Nucleus {ECO:0000269|PubMed:27013495}. SUBUNIT: Interacts with phosphorylated BCL2L11 isoform BIMEL; this interaction leads to BCL2L11 deubiquitination and stabilization. {ECO:0000269|PubMed:27013495}. +B2RQC2 UBP42_MOUSE Ubiquitin carboxyl-terminal hydrolase 42 (EC 3.4.19.12) (Deubiquitinating enzyme 42) (Ubiquitin thioesterase 42) (Ubiquitin-specific-processing protease 42) 1324 146,223 Active site (2); Chain (1); Compositional bias (1); Domain (1); Modified residue (10) FUNCTION: Deubiquitinating enzyme which may play an important role during spermatogenesis. {ECO:0000269|PubMed:16904385}. TISSUE SPECIFICITY: Highest expression seen in the testis. Also expressed in brain, lung and thymus. The expression level gradually increases from 2 weeks after birth and then decreases from the pachytene spermatocyte (PS) stage during spermatogenesis. {ECO:0000269|PubMed:16904385}. +Q9DAM5 TPC_MOUSE Mitochondrial thiamine pyrophosphate carrier (Solute carrier family 25 member 19) 318 35,618 Chain (1); Motif (1); Repeat (3); Transmembrane (6) TRANSMEM 19 39 Helical; Name=1. {ECO:0000255}.; TRANSMEM 87 107 Helical; Name=2. {ECO:0000255}.; TRANSMEM 122 142 Helical; Name=3. {ECO:0000255}.; TRANSMEM 173 193 Helical; Name=4. {ECO:0000255}.; TRANSMEM 220 240 Helical; Name=5. {ECO:0000255}.; TRANSMEM 293 313 Helical; Name=6. {ECO:0000255}. FUNCTION: Mitochondrial transporter mediating uptake of thiamine pyrophosphate (ThPP) into mitochondria. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q9EQJ0 TPC1_MOUSE Two pore calcium channel protein 1 (Voltage-dependent calcium channel protein TPC1) 817 94,496 Alternative sequence (2); Beta strand (16); Chain (1); Coiled coil (1); Glycosylation (1); Helix (39); Intramembrane (2); Topological domain (15); Transmembrane (12); Turn (5) INTRAMEM 264 287 Helical; Pore-forming. {ECO:0000255}.; INTRAMEM 631 654 Helical; Pore-forming. {ECO:0000255}. TRANSMEM 114 134 Helical; Name=S1 of repeat I. {ECO:0000255}.; TRANSMEM 138 158 Helical; Name=S2 of repeat I. {ECO:0000255}.; TRANSMEM 173 193 Helical; Name=S3 of repeat I. {ECO:0000255}.; TRANSMEM 203 221 Helical; Name=S4 of repeat I. {ECO:0000255}.; TRANSMEM 236 256 Helical; Name=S5 of repeat I. {ECO:0000255}.; TRANSMEM 299 319 Helical; Name=S6 of repeat I. {ECO:0000255}.; TRANSMEM 446 466 Helical; Name=S1 of repeat II. {ECO:0000255}.; TRANSMEM 481 501 Helical; Name=S2 of repeat II. {ECO:0000255}.; TRANSMEM 505 527 Helical; Name=S3 of repeat II. {ECO:0000255}.; TRANSMEM 536 550 Helical; Name=S4 of repeat II. {ECO:0000255}.; TRANSMEM 570 590 Helical; Name=S5 of repeat II. {ECO:0000255}.; TRANSMEM 672 692 Helical; Name=S6 of repeat II. {ECO:0000255}. TOPO_DOM 1 113 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 135 137 Extracellular. {ECO:0000255}.; TOPO_DOM 159 172 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 194 202 Extracellular. {ECO:0000255}.; TOPO_DOM 222 235 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 257 263 Extracellular. {ECO:0000255}.; TOPO_DOM 288 298 Extracellular. {ECO:0000255}.; TOPO_DOM 320 445 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 467 480 Extracellular. {ECO:0000255}.; TOPO_DOM 502 504 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 528 535 Extracellular. {ECO:0000255}.; TOPO_DOM 551 569 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 591 630 Extracellular. {ECO:0000255}.; TOPO_DOM 655 671 Extracellular. {ECO:0000255}.; TOPO_DOM 693 817 Cytoplasmic. {ECO:0000255}. FUNCTION: Nicotinic acid adenine dinucleotide phosphate (NAADP) receptor that may function as one of the major voltage-gated Ca(2+) channels (VDCC) across the lysosomal and endosomal membrane. {ECO:0000250}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Dimer. {ECO:0000305}. DOMAIN: Each of the two internal repeats contains five hydrophobic transmembrane segments (S1, S2, S3, S5, S6) and one positively charged transmembrane segment (S4). S4 segments probably represent the voltage-sensor and are characterized by a series of positively charged amino acids at every third position (By similarity). {ECO:0000250}. +Q9JME7 TPC2L_MOUSE Trafficking protein particle complex subunit 2-like protein 139 16,019 Chain (1); Erroneous initiation (1) FUNCTION: May play a role in vesicular transport from endoplasmic reticulum to Golgi. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Golgi apparatus {ECO:0000250}. SUBUNIT: Component of the multisubunit TRAPP (transport protein particle) complex, which includes at least TRAPPC2, TRAPPC2L, TRAPPC3, TRAPPC3L, TRAPPC4, TRAPPC5, TRAPPC8, TRAPPC9, TRAPPC10, TRAPPC11 and TRAPPC12. Interacts with the heterodimer TRAPPC3-TRAPPC6A (By similarity). {ECO:0000250}. +F6ZDS4 TPR_MOUSE Nucleoprotein TPR (NPC-associated intranuclear protein) (Translocated promoter region and nuclear basket protein) 2431 273,990 Chain (1); Coiled coil (5); Compositional bias (2); Modified residue (32); Region (5) FUNCTION: Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs, plays a role in the establishment of nuclear-peripheral chromatin compartmentalization in interphase, and in the mitotic spindle checkpoint signaling during mitosis. Involved in the quality control and retention of unspliced mRNAs in the nucleus; in association with NUP153, regulates the nuclear export of unspliced mRNA species bearing constitutive transport element (CTE) in a NXF1- and KHDRBS1-independent manner. Negatively regulates both the association of CTE-containing mRNA with large polyribosomes and translation initiation. Does not play any role in Rev response element (RRE)-mediated export of unspliced mRNAs. Implicated in nuclear export of mRNAs transcribed from heat shock gene promoters; associates both with chromatin in the HSP70 promoter and with mRNAs transcribed from this promoter under stress-induced conditions. Plays a limited role in the regulation of nuclear protein export. Modulates the nucleocytoplasmic transport of activated MAPK1/ERK2 and huntingtin/HTT and may serve as a docking site for the XPO1/CRM1-mediated nuclear export complex. Plays also a role as a structural and functional element of the perinuclear chromatin distribution; involved in the formation and/or maintenance of NPC-associated perinuclear heterochromatin exclusion zones (HEZs). Finally, acts as a spatial regulator of the spindle-assembly checkpoint (SAC) response ensuring a timely and effective recruitment of spindle checkpoint proteins like MAD1L1 and MAD2L1 to unattached kinetochore during the metaphase-anaphase transition before chromosome congression. Its N-terminus is involved in activation of oncogenic kinases (By similarity). {ECO:0000250}. PTM: Phosphorylated. Phosphorylation occurs on serine and threonine residues (comprised in the C-terminal region) by MAPK1/ERK2 and stabilizes the interaction between these two proteins (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P12270}. Nucleus membrane {ECO:0000250|UniProtKB:P12270}; Peripheral membrane protein {ECO:0000250|UniProtKB:P12270}; Nucleoplasmic side {ECO:0000250|UniProtKB:P12270}. Nucleus envelope {ECO:0000269|PubMed:12424524, ECO:0000269|PubMed:12513910}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P12270, ECO:0000269|PubMed:12513910}. Cytoplasm {ECO:0000250|UniProtKB:P12270}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P12270}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:P12270}. Nucleus membrane {ECO:0000250|UniProtKB:P12270}; Peripheral membrane protein {ECO:0000250|UniProtKB:P12270}; Cytoplasmic side {ECO:0000250|UniProtKB:P12270}. Note=Detected as discrete intranuclear foci with IFI204 (By similarity). In interphase, localizes to the nucleoplasmic side of the nuclear pore complex (NPC) core structure, forming a fibrous structure called the nuclear basket. Detected exclusively to the cytoplasmic margin of NPC (By similarity). Docking to the inner nucleoplasmic side of the NPC is mediated through binding to nucleoporins. Anchored by NUP153 to the NPC. The assembly of the NPC is a stepwise process in which Trp-containing peripheral structures assemble after other components, including p62. Detected as filaments that emanate from the nuclear basket of the NPC and extend to the nucleolus to delineate a chromatin-free network extending from the nuclear envelope to the perinucleolar region. Detected in diffuse and discrete spheroidal intranuclear foci. Nucleocytoplasmic shuttling protein imported into the nucleus in a XPO1/CRM1- and Importin alpha/Importin beta receptor-dependent manner. Remains localized to the nuclear membrane after poliovirus (PV) infection. During mitosis, remains associated with the nuclear envelope until prometaphase. Associated with the mitotic spindle from late prometaphase until anaphase. Reorganized during mitosis in a viscous and dynamic nuclear-derived spindle matrix that embeds the microtubule spindle apparatus from pole to pole in a microtubule-independent manner. Recruited to the reforming nuclear envelope during telophase and cytokinesis. Detected at kinetochores during prometaphase. Colocalizes with MAD2L1 in the spindle matrix but not at kinetochore. Colocalizes with dynein, dynactin, tubulin at kinetochore during the metaphase-anaphase transition. Colocalizes with DYNLL1 at the mitotic spindle (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P12270}. SUBUNIT: Homodimer. Part of the nuclear pore complex (NPC). Associates with the XPO1/CRM1-mediated nuclear export complex, the Importin alpha/Importin beta receptor and the dynein 1 complex. Interacts (via C-terminal domain) with the KPNB1; the interaction occurs in a RanGTP-dependent manner. Interacts (via C-terminal region and phosphorylated form) with MAPK1/ERK2 (via phosphorylated form); the interaction requires dimerization of MAPK1/ERK2 and increases following EGF stimulation. Interacts with MAPK3/ERK1; the interaction increases following EGF stimulation. Interacts (via coiled coil region) with NUP153; the interaction is direct. Interacts with HSF1; the interaction increases in a stress-responsive manner and stimulates export of stress-induced HSP70 mRNA. Interacts with huntingtin/HTT; the interaction is inhibited by aggregated huntingtin/HTT forms with expanded polyglutamine stretch. Interacts with MAD1L1 (via N-terminal region), MAD2L1, and TTK; the interactions occurs in a microtubule-independent manner. Interacts (via middle region) with DYNLL1. Interacts with DCTN1, dynein, NUP153 and tubulin. Interacts with MTA1 (By similarity). Interacts with IFI204 (via C-terminal region). Interacts with IFI203. {ECO:0000250, ECO:0000269|PubMed:12513910}. DOMAIN: The N-terminal domain mediates intranuclear attachment to the nuclear pore complex. The C-terminal domain mediates its nuclear import (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the heart, liver, kidney, spleen, lung and skeletal muscles. {ECO:0000269|PubMed:12424524}. +Q9R233 TPSN_MOUSE Tapasin (TPN) (TPSN) (TAP-associated protein) (TAP-binding protein) 465 49,736 Alternative sequence (1); Chain (1); Compositional bias (1); Disulfide bond (3); Domain (1); Glycosylation (1); Sequence conflict (4); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 417 437 Helical. {ECO:0000255}. TOPO_DOM 24 416 Lumenal. {ECO:0000255}.; TOPO_DOM 438 465 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in the association of MHC class I with transporter associated with antigen processing (TAP) and in the assembly of MHC class I with peptide (peptide loading). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Interacts with TAP1 and is thus a subunit of the TAP complex. Interaction with TAP1 is TAP2 independent and is required for efficient peptide-TAP interaction. Obligatory mediator for the interaction between newly assembled MHC class I molecules, calreticulin, ERp57 and TAP. Up to 4 MHC class I/tapasin complexes bind to 1 TAP. DOMAIN: The N-terminus is required for efficient association with MHC class I molecule and for a stable interaction between MHC I and calreticulin. Binding to TAP is mediated by the C-terminal region (By similarity). {ECO:0000250}. +Q8CB49 TPRG1_MOUSE Tumor protein p63-regulated gene 1 protein (Protein FAM79B) 279 31,269 Chain (1); Domain (1) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18256694}. TISSUE SPECIFICITY: Highly expressed in skin. Also detected at low levels in tongue and esophagus. {ECO:0000269|PubMed:18256694}. +Q3U0M1 TPPC9_MOUSE Trafficking protein particle complex subunit 9 (NIK- and IKBKB-binding protein) 1148 128,232 Alternative sequence (6); Chain (1); Erroneous initiation (1); Modified residue (2); Sequence conflict (1) FUNCTION: Functions as an activator of NF-kappa-B through increased phosphorylation of the IKK complex. May function in neuronal cells differentiation. May play a role in vesicular transport from endoplasmic reticulum to Golgi. {ECO:0000269|PubMed:15951441}. SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Cytoplasm {ECO:0000305|PubMed:15951441}. Note=Processes and cell bodies of neurons. SUBUNIT: Component of the multisubunit TRAPP (transport protein particle) complex, which includes at least TRAPPC2, TRAPPC2L, TRAPPC3, TRAPPC3L, TRAPPC4, TRAPPC5, TRAPPC8, TRAPPC9, TRAPPC10, TRAPPC11 and TRAPPC12 (By similarity). Directly interacts with IKBKB and MAP3K14. {ECO:0000250, ECO:0000269|PubMed:15951441}. TISSUE SPECIFICITY: Expressed in neurons of the pyramidal layer of the cortex, in spinal cord motor neurons and white matter neurons (at protein level). {ECO:0000269|PubMed:15951441}. +Q5BLK4 TUT7_MOUSE Terminal uridylyltransferase 7 (TUTase 7) (EC 2.7.7.52) (Zinc finger CCHC domain-containing protein 6) 1491 169,103 Binding site (3); Chain (1); Compositional bias (3); Domain (2); Erroneous initiation (2); Metal binding (2); Modified residue (7); Region (4); Sequence caution (1); Sequence conflict (5); Zinc finger (4) FUNCTION: Uridylyltransferase that mediates the terminal uridylation of mRNAs with short (less than 25 nucleotides) poly(A) tails, hence facilitating global mRNA decay (PubMed:28792939). Essential for both oocyte maturation and fertility. Through 3' terminal uridylation of mRNA, sculpts, with TUT7, the maternal transcriptome by eliminating transcripts during oocyte growth (PubMed:28792939). Involved in microRNA (miRNA)-induced gene silencing through uridylation of deadenylated miRNA targets. Also acts as a suppressor of miRNA biogenesis by mediating the terminal uridylation of miRNA precursors, including that of let-7 (pre-let-7) (PubMed:22898984). Uridylated pre-let-7 RNA is not processed by Dicer and undergo degradation. Pre-let-7 uridylation is strongly enhanced in the presence of LIN28A. Due to functional redundancy between ZCCHC6 and ZCCHC11, the identification of the specific role of each of these proteins is difficult (By similarity) (PubMed:22898984). Involved in microRNA (miRNA)-induced gene silencing through uridylation of deadenylated miRNA targets (By similarity). Also functions as an integral regulator of microRNA biogenesiS using 3 different uridylation mechanisms (By similarity). Acts as a suppressor of miRNA biogenesis by mediating the terminal uridylation of some miRNA precursors, including that of let-7 (pre-let-7). Uridylated pre-let-7 RNA is not processed by Dicer and undergo degradation. Pre-let-7 oligouridylation is strongly enhanced in the presence of LIN28A (PubMed:22898984). In the absence of LIN28A, TUT7 and TUT4 monouridylate group II pre-miRNAs, which includes most of pre-let7 members, that shapes an optimal 3' end overhang for efficient processing (By similarity). Add oligo-U tails to truncated pre-miRNAS with a 5' overhang which may promote rapid degradation of non-functional pre-miRNA species (By similarity). Does not play a role in replication-dependent histone mRNA degradation (By similarity). Due to functional redundancy between TUT4 and TUT7, the identification of the specific role of each of these proteins is difficult (PubMed:28792939, PubMed:22898984). TUT4 and TUT7 restrict retrotransposition of long interspersed element-1 (LINE-1) in cooperation with MOV10 counteracting the RNA chaperonne activity of L1RE1. TUT7 uridylates LINE-1 mRNAs in the cytoplasm which inhibits initiation of reverse transcription once in the nucleus, whereas uridylation by TUT4 destabilizes mRNAs in cytoplasmic ribonucleoprotein granules (By similarity). {ECO:0000250|UniProtKB:Q5VYS8, ECO:0000269|PubMed:22898984, ECO:0000269|PubMed:28792939}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q5VYS8}. DOMAIN: Utilizes two multidomain functional modules during the switch from monouridylation to oligouridylation. The catalytic module (containing the 3 CCHC-type Zinc finger domains) is essential for both activites while the Lin28-interacting module (LIM) at the N-termail part is indispensable for oligouridylation. {ECO:0000250|UniProtKB:Q5VYS8}. +Q05BQ1 TUTLA_MOUSE Protein turtle homolog A (Dendrite arborization and synapse maturation protein 1) (Immunoglobulin superfamily member 9A) (IgSF9A) 1179 127,330 Alternative sequence (2); Chain (1); Compositional bias (1); Disulfide bond (5); Domain (7); Glycosylation (5); Modified residue (1); Motif (1); Mutagenesis (1); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 735 755 Helical. {ECO:0000255}. TOPO_DOM 21 734 Extracellular. {ECO:0000255}.; TOPO_DOM 756 1179 Cytoplasmic. {ECO:0000255}. FUNCTION: Functions in dendrite outgrowth and synapse maturation. {ECO:0000269|PubMed:15340156, ECO:0000269|PubMed:15340157}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cell junction, synapse {ECO:0000250}. Note=Enriched at the excitatory synapses in mature neurons. {ECO:0000250}. SUBUNIT: Interacts with MAGI2 and SHANK1. {ECO:0000269|PubMed:15340156}. DOMAIN: The PDZ-binding motif mediates interactions with MAGI2 and SHANK1. TISSUE SPECIFICITY: Expressed in both cell bodies and dendrites of cortical and hippocampal neurons and also cerebellar Purkinje cells (at protein level). {ECO:0000269|PubMed:15340157}. +E9PZ19 TUTLB_MOUSE Protein turtle homolog B (Immunoglobulin superfamily member 9B) 1328 144,951 Chain (1); Compositional bias (1); Disulfide bond (5); Domain (7); Glycosylation (3); Modified residue (6); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 723 743 Helical. {ECO:0000255}. TOPO_DOM 18 722 Extracellular. {ECO:0000305}.; TOPO_DOM 744 1328 Cytoplasmic. {ECO:0000305}. FUNCTION: Transmembrane protein which is abundantly expressed in interneurons, where it may regulate inhibitory synapse development (By similarity). May mediate homophilic cell adhesion (PubMed:23751499). {ECO:0000250|UniProtKB:D3ZB51, ECO:0000269|PubMed:23751499}. PTM: N-glycosylated and sialylated. Not significantly O-glycosylated. {ECO:0000250|UniProtKB:D3ZB51}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23751499}; Single-pass type I membrane protein {ECO:0000255}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000250|UniProtKB:D3ZB51}; Single-pass type I membrane protein {ECO:0000255}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250|UniProtKB:D3ZB51}. SUBUNIT: Found in a complex with MAGI2 and NLGN2, where it interacts with MAGI2 (via PDZ 5 and PDZ 6 domains). {ECO:0000269|PubMed:23751499}. TISSUE SPECIFICITY: Detected in brain. {ECO:0000269|PubMed:23751499}. +Q9D8T4 TV23B_MOUSE Golgi apparatus membrane protein TVP23 homolog B 205 23,305 Chain (1); Modified residue (1); Transmembrane (4) TRANSMEM 34 53 Helical. {ECO:0000255}.; TRANSMEM 54 72 Helical. {ECO:0000255}.; TRANSMEM 126 146 Helical. {ECO:0000255}.; TRANSMEM 152 172 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +P01739 TVA2_MOUSE T-cell receptor alpha chain V region 2B4 132 14,668 Beta strand (6); Chain (1); Glycosylation (1); Non-terminal residue (1); Region (3); Signal peptide (1); Turn (1) +P01738 TVA1_MOUSE T-cell receptor alpha chain V region PHDS58 130 14,320 Beta strand (13); Chain (1); Glycosylation (1); Helix (3); Non-terminal residue (1); Region (2); Signal peptide (1); Turn (1) +P06321 TVB8_MOUSE T-cell receptor beta chain V region A20.2.25 130 14,732 Chain (1); Glycosylation (2); Non-terminal residue (1); Region (3); Signal peptide (1) +P06324 TVC3_MOUSE T-cell receptor gamma chain V region DFL12 132 15,434 Chain (1); Non-terminal residue (1); Region (2); Signal peptide (1) +P06325 TVC4_MOUSE T-cell receptor gamma chain V region 5/10-13 135 15,508 Chain (1); Non-terminal residue (1); Region (2); Signal peptide (1) +P01736 TVB3_MOUSE T-cell receptor beta chain V region PHDS203 (Fragment) 120 13,670 Chain (1); Disulfide bond (1); Non-terminal residue (2); Region (2); Signal peptide (1) +P04213 TVB5_MOUSE T-cell receptor beta chain V region C5 (Fragment) 122 13,349 Beta strand (12); Chain (1); Disulfide bond (1); Helix (1); Non-terminal residue (2); Region (3); Signal peptide (1) +Q9D5S1 TX19B_MOUSE Testis-expressed protein 19.2 (Testis-expressed protein 19B) 317 35,235 Chain (1); Region (1) FUNCTION: May be required during spermatogenesis, probably by participating in the repression of retrotransposable elements and prevent their mobilization (Probable). With its paralog, Tex19.1, collaborates with the Piwi-interacting RNA (piRNA) pathway, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins. Interacts with Piwi proteins and directly binds piRNAs, a class of 24 to 30 nucleotide RNAs that are generated by a Dicer-independent mechanism and are primarily derived from transposons and other repeated sequence elements (PubMed:28254886). {ECO:0000269|PubMed:28254886, ECO:0000305|PubMed:28254886}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q99MV2}. Note=Was initially reported to localize in the nucleus. {ECO:0000269|PubMed:18096721}. SUBUNIT: Interacts with UBR2 (PubMed:21103378). Interacts with piRNA-associated proteins DDX4, EDC4, MAEL, PIWIL1, PIWIL2, RANBP9 and TDRD6 (Probable). {ECO:0000269|PubMed:21103378, ECO:0000305|PubMed:28254886}. TISSUE SPECIFICITY: Specifically expressed in somatic cells of male gonad lineage. {ECO:0000269|PubMed:18096721, ECO:0000269|PubMed:28254886}. +Q8BUH1 TXN4B_MOUSE Thioredoxin-like protein 4B 149 17,020 Chain (1); Sequence conflict (3) FUNCTION: Essential role in pre-mRNA splicing. Required in cell cycle progression for S/G(2) transition (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Homodimer. Interacts with the U5-102 kDa protein subunit of the spliceosome (By similarity). {ECO:0000250}. +Q8VBT1 TXLNB_MOUSE Beta-taxilin (Muscle-derived protein 77) 685 77,207 Chain (1); Coiled coil (2); Modified residue (3); Sequence conflict (2) FUNCTION: Promotes motor nerve regeneration. May be involved in intracellular vesicle traffic (By similarity). {ECO:0000250}. SUBUNIT: Binds to the C-terminal coiled coil region of syntaxin family members STX1A, STX3A and STX4A. Has a preference for STX1A (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Specifically expressed in skeletal muscle. {ECO:0000269|PubMed:11805063}. +Q91W90 TXND5_MOUSE Thioredoxin domain-containing protein 5 (Endoplasmic reticulum resident protein 46) (ER protein 46) (ERp46) (Plasma cell-specific thioredoxin-related protein) (PC-TRP) (Thioredoxin-like protein p46) 417 46,415 Chain (1); Disulfide bond (3); Domain (3); Mass spectrometry (1); Motif (1); Sequence conflict (4); Signal peptide (1) FUNCTION: Possesses thioredoxin activity. Has been shown to reduce insulin disulfide bonds. Also complements protein disulfide-isomerase deficiency in yeast. {ECO:0000269|PubMed:12930873, ECO:0000269|PubMed:14971039}. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138, ECO:0000269|PubMed:12930873}. TISSUE SPECIFICITY: Expressed at high levels in plasma cells and at very low levels in all other cells and tissues examined (at protein level). {ECO:0000269|PubMed:14971039}. +Q69AB2 TXND8_MOUSE Thioredoxin domain-containing protein 8 (Spermatid-specific thioredoxin-3) (Sptrx-3) (Thioredoxin-6) 127 14,517 Alternative sequence (1); Chain (1); Disulfide bond (1); Domain (1); Erroneous initiation (1); Sequence conflict (1) FUNCTION: May be required for post-translational modifications of proteins required for acrosomal biogenesis. May act by reducing disulfide bonds within the sperm (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15181017}. Golgi apparatus {ECO:0000269|PubMed:15181017}. TISSUE SPECIFICITY: Testis-specific. Only expressed during spermiogenesis, prominently in the Golgi apparatus of pachytene spermatocytes and round and elongated spermatids, with a transient localization in the developing acrosome of round spermatids (at protein level). {ECO:0000269|PubMed:15181017}. +Q9JJX7 TYDP2_MOUSE Tyrosyl-DNA phosphodiesterase 2 (Tyr-DNA phosphodiesterase 2) (EC 3.1.4.-) (5'-tyrosyl-DNA phosphodiesterase) (5'-Tyr-DNA phosphodiesterase) (TRAF and TNF receptor-associated protein) 370 41,034 Active site (1); Beta strand (14); Chain (1); Cross-link (1); Helix (7); Metal binding (6); Modified residue (2); Turn (4) FUNCTION: DNA repair enzyme that can remove a variety of covalent adducts from DNA through hydrolysis of a 5'-phosphodiester bond, giving rise to DNA with a free 5' phosphate (By similarity). Catalyzes the hydrolysis of dead-end complexes between DNA and the topoisomerase 2 (TOP2) active site tyrosine residue. The 5'-tyrosyl DNA phosphodiesterase activity can enable the repair of TOP2-induced DNA double-strand breaks/DSBs without the need for nuclease activity, creating a 'clean' DSB with 5'-phosphate termini that are ready for ligation. Thereby, protects the transcription of many genes involved in neurological development and maintenance from the abortive activity of TOP2 (PubMed:22740648). Hydrolyzes 5'-phosphoglycolates on protruding 5' ends on DSBs due to DNA damage by radiation and free radicals. Has preference for single-stranded DNA or duplex DNA with a 4 base pair overhang as substrate. Has also 3'-tyrosyl DNA phosphodiesterase activity, but less efficiently and much slower than TDP1. Constitutes the major if not only 5'-tyrosyl-DNA phosphodiesterase in cells. Also acts as an adapter by participating in the specific activation of MAP3K7/TAK1 in response to TGF-beta: associates with components of the TGF-beta receptor-TRAF6-TAK1 signaling module and promotes their ubiquitination dependent complex formation. Involved in non-canonical TGF-beta induced signaling routes. May also act as a negative regulator of ETS1 and may inhibit NF-kappa-B activation. Acts as a regulator of ribosome biogenesis following stress (By similarity). {ECO:0000250|UniProtKB:O95551, ECO:0000269|PubMed:22740648}. PTM: Ubiquitinated by TRAF6. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus, PML body {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Note=Localizes to nucleolar cavities following stress; localization to nucleolus is dependent on PML protein. {ECO:0000250}. SUBUNIT: Interacts with TRAF2, TRAF3, TRAF5, TRAF6, TNFRSF8/CD30, TNFRSF5/CD40, TNFRSF1B/TNF-R75, ETS1, ETS2, FLI1, SMAD3 and ACVR1B/ALK4. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed (PubMed:10764746). Expressed in whole brain, cerebellum, quiescent cortical astrocytes and cerebellar granule neurons (PubMed:24658003). {ECO:0000269|PubMed:10764746, ECO:0000269|PubMed:24658003}. +P07147 TYRP1_MOUSE 5,6-dihydroxyindole-2-carboxylic acid oxidase (DHICA oxidase) (EC 1.14.18.-) (Brown locus protein) (Catalase B) (Tyrosinase-related protein 1) (TRP) (TRP-1) (TRP1) 537 60,761 Chain (1); Disulfide bond (7); Glycosylation (6); Metal binding (6); Natural variant (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 478 501 Helical. {ECO:0000255}. TOPO_DOM 25 477 Lumenal, melanosome. {ECO:0000255}.; TOPO_DOM 502 537 Cytoplasmic. {ECO:0000255}. Pigment biosynthesis; melanin biosynthesis. FUNCTION: Catalyzes the oxidation of 5,6-dihydroxyindole-2-carboxylic acid (DHICA) into indole-5,6-quinone-2-carboxylic acid (PubMed:7813420). May regulate or influence the type of melanin synthesized (PubMed:7813420, PubMed:2245916). Also to a lower extent, capable of hydroxylating tyrosine and producing melanin (PubMed:1537333). {ECO:0000269|PubMed:1537333, ECO:0000269|PubMed:2245916, ECO:0000269|PubMed:7813420}. PTM: Glycosylated. {ECO:0000269|PubMed:1537333}. SUBCELLULAR LOCATION: Melanosome membrane {ECO:0000269|PubMed:17182842}; Single-pass type I membrane protein {ECO:0000269|PubMed:17182842}. Melanosome {ECO:0000269|PubMed:26620560}. Note=Located to mature stage III and IV melanosomes and apposed endosomal tubular membranes. Transported to pigmented melanosomes by the BLOC-1 complex. Proper trafficking to melanosome is regulated by SGSM2, ANKRD27, RAB9A, RAB32 and RAB38. {ECO:0000269|PubMed:17182842, ECO:0000269|PubMed:26620560}. TISSUE SPECIFICITY: Pigment cells. DISEASE: Note=Defects in Tyrp1 are the cause of the brown (b) phenotype. Brown mice have a brown or hypopigmented coat. {ECO:0000269|PubMed:2245916}. +Q8BGJ9 U2AF4_MOUSE Splicing factor U2AF 26 kDa subunit (U2 auxiliary factor 26) (U2 small nuclear RNA auxiliary factor 1-like protein 4) (U2AF1-like 4) 220 25,836 Alternative sequence (4); Chain (1); Domain (1); Initiator methionine (1); Modified residue (1); Mutagenesis (3); Zinc finger (2) FUNCTION: RNA-binding protein that function as a pre-mRNA splicing factor. Plays a critical role in both constitutive and enhancer-dependent splicing by mediating protein-protein interactions and protein-RNA interactions required for accurate 3'-splice site selection. It can functionally substitute for U2AF1 in constitutive splicing and enhancer-dependent splicing. Acts by enhancing the binding of U2AF2 to weak pyrimidine tracts. Also participates in the regulation of alternative pre-mRNA splicing. Activates exon 5 skipping of PTPRC during T-cell activation; an event reversed by GFI1. Binds to RNA at the AG dinucleotide at the 3'-splice site. Shows a preference for AGC or AGA (PubMed:11739736, PubMed:16819553, PubMed:18460468). Alternative splicing of U2AF1L4 may play a role in connecting the circadian rhythm to changing external cues: may provide a circadian buffering system in central and periphery clocks that allows synchronized adaption to clock-resetting stimuli in order to prevent potentially pathogenic desynchronization (PubMed:24837677). {ECO:0000269|PubMed:11739736, ECO:0000269|PubMed:16819553, ECO:0000269|PubMed:24837677, ECO:0000303|PubMed:18460468}. PTM: Isoform 3 is rapidly degraded by a proteasome-mediated degradation pathway. {ECO:0000269|PubMed:24837677}. SUBCELLULAR LOCATION: Isoform 1: Nucleus {ECO:0000269|PubMed:11739736, ECO:0000269|PubMed:18460468}. Nucleus speckle {ECO:0000269|PubMed:11739736}. Cytoplasm {ECO:0000269|PubMed:16819553, ECO:0000269|PubMed:18460468, ECO:0000269|PubMed:24837677}. Note=Interaction with C1QBP is required for the nuclear translocation. Displays active nucleo-cytoplasmic shuttling. {ECO:0000269|PubMed:18460468}.; SUBCELLULAR LOCATION: Isoform 3: Cytoplasm {ECO:0000269|PubMed:18460468, ECO:0000269|PubMed:24837677}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm {ECO:0000269|PubMed:18460468}. SUBUNIT: Interacts with GFI1, U2AF2 and C1QBP. Isoform 3 interacts with PER1. {ECO:0000269|PubMed:11739736, ECO:0000269|PubMed:16819553, ECO:0000269|PubMed:18460468, ECO:0000269|PubMed:24837677}. DOMAIN: The second zinc finger in necessary for interaction with GFI1 and for alternative pre-mRNA splicing events.; DOMAIN: The region 162-220 is essential for the nuclear import of the protein in spite of the absence of a nuclear localization signal (NLS). This region is essential for the interaction with C1QBP, interaction which is required for the nuclear translocation. This region may be involved in the localization in nuclear dot-like structures and it also confers the ability of nucleo-cytoplasmic shuttling. {ECO:0000269|PubMed:18460468}.; DOMAIN: Isoform 3 contains a C-terminus domain with homology to Drosophila TIM (THD domain). Isoform 3 interacts with Per1 and specifically down-regulates its expression, probably by facilitating its recruitment to the proteasome. The interaction with PER1 depends on the presence of the THD domain, but the THD domain is not directly involved in the interaction. {ECO:0000269|PubMed:24837677}. TISSUE SPECIFICITY: Ubiquitous. Highly expressed in the brain. {ECO:0000269|PubMed:11739736}. +Q6P4T2 U520_MOUSE U5 small nuclear ribonucleoprotein 200 kDa helicase (EC 3.6.4.13) (BRR2 homolog) (U5 snRNP-specific 200 kDa protein) (U5-200KD) 2136 244,547 Chain (1); Coiled coil (1); Cross-link (6); Domain (6); Modified residue (12); Motif (2); Nucleotide binding (2) FUNCTION: RNA helicase that plays an essential role in pre-mRNA splicing as component of the U5 snRNP and U4/U6-U5 tri-snRNP complexes. Involved in spliceosome assembly, activation and disassembly. Mediates changes in the dynamic network of RNA-RNA interactions in the spliceosome. Catalyzes the ATP-dependent unwinding of U4/U6 RNA duplices, an essential step in the assembly of a catalytically active spliceosome (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of a core complex containing at least PRPF8, SNRNP200, EFTUD2 and SNRNP40. Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39. Identified in the spliceosome C complex (By similarity). {ECO:0000250}. DOMAIN: Contains two helicase domains. The N-terminal helicase domain has catalytic activity by itself, contrary to C-terminal helicase domain that may have a regulatory role and enhance the activity of the first helicase domain. {ECO:0000250}. +P0C1Z5 U730_MOUSE Putative UPF0730 protein encoded by LINC00643 homolog 52 6,127 Chain (1) +Q91WM3 U3IP2_MOUSE U3 small nucleolar RNA-interacting protein 2 (RRP9 homolog) (U3 small nucleolar ribonucleoprotein-associated 55 kDa protein) (U3 snoRNP-associated 55 kDa protein) (U3-55K) 475 52,107 Chain (1); Compositional bias (1); Cross-link (1); Modified residue (6); Motif (1); Repeat (7) FUNCTION: Component of a nucleolar small nuclear ribonucleoprotein particle (snoRNP) thought to participate in the processing and modification of pre-ribosomal RNA. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. SUBUNIT: Interacts specifically with the U3 small nucleolar RNA (U3 snoRNA). Binds a sub-fragment of the U3 snoRNA surrounding the B/C motif (3UBC). This association with the U3BC RNA is dependent on the binding of a protein called 15.5K to the box B/C motif. The association of the protein with the U3BC RNA was found to be also dependent on a conserved RNA structure that flanks the box B/C motif (By similarity). {ECO:0000250}. DOMAIN: The WD domains are required for nucleolar localization and U3 small nucleolar RNAs binding. {ECO:0000250}. +P61080 UB2D1_MOUSE Ubiquitin-conjugating enzyme E2 D1 (EC 2.3.2.23) ((E3-independent) E2 ubiquitin-conjugating enzyme D1) (EC 2.3.2.24) (E2 ubiquitin-conjugating enzyme D1) (Ubiquitin carrier protein D1) (Ubiquitin-conjugating enzyme E2(17)KB 1) (Ubiquitin-conjugating enzyme E2-17 kDa 1) (Ubiquitin-protein ligase D1) 147 16,602 Active site (1); Chain (1) Protein modification; protein ubiquitination. FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Mediates ubiquitination of PEX5 and auto-ubiquitination of STUB1, TRAF6 and TRIM63/MURF1. Ubiquitinates STUB1-associated HSP90AB1 in vitro. Lacks inherent specificity for any particular lysine residue of ubiquitin. Essential for viral activation of IRF3. Mediates polyubiquitination of CYP3A4. {ECO:0000250|UniProtKB:P51668}. PTM: Autoubiquitinated. {ECO:0000250|UniProtKB:P51668}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P51668}. SUBUNIT: Component of a E3 ubiquitin ligase complex containing UBE2D1, SIAH1, CACYBP/SIP, SKP1, APC and TBL1X. Interacts with RNF11. {ECO:0000250|UniProtKB:P51668}. +Q3US16 TEANC_MOUSE Transcription elongation factor A N-terminal and central domain-containing protein (TFIIS central domain-containing protein 1) 359 40,635 Chain (1); Domain (2); Frameshift (1) +G3UW99 TEX54_MOUSE Testis-expressed protein 54 86 10,080 Chain (1) TISSUE SPECIFICITY: Expressed in Testis. {ECO:0000305}. +Q9ERA0 TFCP2_MOUSE Alpha-globin transcription factor CP2 502 57,031 Alternative sequence (2); Chain (1); Modified residue (1); Region (1) FUNCTION: Binds a variety of cellular promoters including fibrinogen, alpha-globin promoters. Activation of the alpha-globin promoter in erythroid cells is via synergistic interaction with UBP1 (By similarity). Functions as part of the SSP (stage selector protein) complex. Facilitates the interaction of the gamma-globin genes with enhancer elements contained in the locus control region in fetal erythroid cells. Interacts by binding to the stage selector element (SSE) in the proximal gamma-globin promoter (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Binds to DNA as a dimer. Interacts with UBP1 and PIAS1, and is probably part of a complex containing TFCP2, UBP1 and PIAS1. Component of the SSP (stage selector protein) complex, which appears to be a heteromer of TFCP2 and 2 copies of NFE4 (By similarity). {ECO:0000250}. +F8VPN2 TEX15_MOUSE Testis-expressed protein 15 2785 311,280 Alternative sequence (1); Chain (1); Compositional bias (1); Sequence conflict (9) FUNCTION: Required during spermatogenesis for normal chromosome synapsis and meiotic recombination in germ cells. Necessary for formation of DMC1 and RAD51 foci on meiotic chromosomes, suggesting a specific role in DNA double-stranded break repair. {ECO:0000269|PubMed:18283110}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18283110}. Nucleus {ECO:0000269|PubMed:18283110}. TISSUE SPECIFICITY: Detected in testis and ovary, and at lower levels in lung and brain. {ECO:0000269|PubMed:11279525}. +Q6ZPJ0 TEX2_MOUSE Testis-expressed protein 2 1128 125,226 Chain (1); Compositional bias (4); Domain (1); Erroneous initiation (1); Glycosylation (1); Modified residue (13); Transmembrane (2) TRANSMEM 473 493 Helical. {ECO:0000255}.; TRANSMEM 495 515 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q99PM3 TF2AA_MOUSE Transcription initiation factor IIA subunit 1 (General transcription factor IIA subunit 1) [Cleaved into: Transcription initiation factor IIA alpha chain (TFIIA p35 subunit); Transcription initiation factor IIA beta chain (TFIIA p19 subunit)] 378 41,614 Chain (3); Compositional bias (2); Erroneous initiation (1); Initiator methionine (1); Modified residue (5); Sequence conflict (3); Site (1) FUNCTION: TFIIA is a component of the transcription machinery of RNA polymerase II and plays an important role in transcriptional activation. TFIIA in a complex with TBP mediates transcriptional activity (By similarity). {ECO:0000250}. PTM: The alpha and beta subunits are postranslationally produced from the precursor form by TASP1. The cleavage promotes proteasomal degradation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: TFIIA is a heterodimer of a unprocessed large subunit 1 and a small subunit gamma. It was originally believed to be a heterotrimer of an alpha, a beta and a gamma subunit. TFIIA forms a complex with TBP (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in pachytene spermatocytes and spermatids. {ECO:0000269|PubMed:11159353}. +Q8VHT7 TF3A_MOUSE Transcription factor IIIA (TFIIIA) 364 41,571 Chain (1); Erroneous initiation (3); Sequence conflict (6); Zinc finger (9) FUNCTION: Involved in ribosomal large subunit biogenesis. Binds the approximately 50 base pairs internal control region (ICR) of 5S ribosomal RNA genes. It is required for their RNA polymerase III-dependent transcription and may also maintain the transcription of other genes (By similarity). Also binds the transcribed 5S RNA's (By similarity). {ECO:0000250|UniProtKB:P17842, ECO:0000250|UniProtKB:Q92664}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +Q3T9E4 TGTP2_MOUSE T-cell-specific guanine nucleotide triphosphate-binding protein 2 (EC 3.6.5.-) (Interferon-gamma-inducible GTPase Ifggb6 protein) (T-cell-specific guanine nucleotide triphosphate-binding protein) 415 47,121 Chain (1); Domain (1); Nucleotide binding (3); Sequence conflict (1) FUNCTION: Involved in innate cell-autonomous resistance to intracellular pathogens, such as Toxoplasma gondii. During avirulent type II T. gondii infection, recruited to the parasitophorous vacuole (PV) membrane, leading to PV vesiculation and rupture, and subsequent digestion of the parasite within the cytosol (PubMed:19265156, PubMed:24563254). Not recruited to virulent type I T. gondii PV membrane (PubMed:19265156). May confer an antiviral state for vesicular stomatitis virus (PubMed:9725230). {ECO:0000269|PubMed:19265156, ECO:0000269|PubMed:24563254, ECO:0000269|PubMed:9725230}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19285957}. Endoplasmic reticulum {ECO:0000269|PubMed:19285957}. Golgi apparatus {ECO:0000269|PubMed:19285957}. Note=In astrocytes stimulated with IFNG or TNF, diffuse cytoplasmic localization decreases and the protein partially relocalizes to the endoplasmic reticulum and Golgi apparatus (PubMed:19285957). Due to sequence similarity with Tgtp1, it is impossible to assign unambiguously experimental data published in the literature to Tgtp1 or Tgtp2 gene (Probable). {ECO:0000269|PubMed:19285957, ECO:0000305|PubMed:22892676}. TISSUE SPECIFICITY: Expressed in thymus and lymph nodes, predominantly T-cells. Not expressed by immature CD4(+) CD8(+) thymocytes (at protein level) (PubMed:7836757). Expressed in IFNG-stimulated macrophages (PubMed:7884320). Expressed at low levels in unstimulated astrocytes (PubMed:19285957). Due to sequence similarity with Tgtp1, it is impossible to assign unambiguously experimental data published in the literature to Tgtp1 or Tgtp2 gene. {ECO:0000269|PubMed:19285957, ECO:0000269|PubMed:7836757, ECO:0000269|PubMed:7884320}. +Q8BG87 TET3_MOUSE Methylcytosine dioxygenase TET3 (EC 1.14.11.n2) 1668 180,378 Alternative sequence (3); Beta strand (1); Binding site (4); Chain (1); Cross-link (5); Erroneous initiation (1); Helix (1); Metal binding (15); Modified residue (1); Mutagenesis (2); Region (3); Sequence caution (1); Sequence conflict (1); Turn (1) FUNCTION: Dioxygenase that catalyzes the conversion of the modified genomic base 5-methylcytosine (5mC) into 5-hydroxymethylcytosine (5hmC) and plays a key role in epigenetic chromatin reprogramming in the zygote following fertilization. Also mediates subsequent conversion of 5hmC into 5-formylcytosine (5fC), and conversion of 5fC to 5-carboxylcytosine (5caC). Conversion of 5mC into 5hmC, 5fC and 5caC probably constitutes the first step in cytosine demethylation. Selectively binds to the promoter region of target genes and contributes to regulate the expression of numerous developmental genes. In zygotes, DNA demethylation occurs selectively in the paternal pronucleus before the first cell division, while the adjacent maternal pronucleus and certain paternally-imprinted loci are protected from this process. Participates in DNA demethylation in the paternal pronucleus by mediating conversion of 5mC into 5hmC, 5fC and 5caC. Does not mediate DNA demethylation of maternal pronucleus because of the presence of DPPA3/PGC7 on maternal chromatin that prevents TET3-binding to chromatin. In addition to its role in DNA demethylation, also involved in the recruitment of the O-GlcNAc transferase OGT to CpG-rich transcription start sites of active genes, thereby promoting histone H2B GlcNAcylation by OGT. {ECO:0000269|PubMed:20639862, ECO:0000269|PubMed:21407207, ECO:0000269|PubMed:21778364, ECO:0000269|PubMed:21892189, ECO:0000269|PubMed:22722204, ECO:0000269|PubMed:23690950, ECO:0000269|PubMed:26774490}.; FUNCTION: Isoform 3: Has higher affinity for DNA and lower catalytic activity than isoform 1, probably due to the N-terminal CXXC-type zinc-finger domain that mediates high-affinity binding to DNA and that is not present in isoform 1. {ECO:0000269|PubMed:26774490}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21892189, ECO:0000269|PubMed:26774490}. Chromosome {ECO:0000269|PubMed:26774490}. Cytoplasm {ECO:0000269|PubMed:21892189}. Note=At the zygotic stage, localizes in the male pronucleus, while it localizes to the cytoplasm at other preimplantation stages (PubMed:21892189). Binds to the promoter of target genes, close to the transcription start site (PubMed:26774490). {ECO:0000269|PubMed:21892189, ECO:0000269|PubMed:26774490}. SUBUNIT: Interacts with HCFC1 and OGT. {ECO:0000250|UniProtKB:O43151}. DOMAIN: Isoform 3 contains an N-terminal CXXC-type zinc-finger domain that binds to DNA sequences containing unmethylated cytosine or 5-carboxylcytosine in 5'-CCG-3' DNA sequence motifs. {ECO:0000269|PubMed:26774490}. TISSUE SPECIFICITY: Highly expressed in oocytes and zygotes. Not expressed in embryonic stem cells (ES cells). {ECO:0000269|PubMed:20639862, ECO:0000269|PubMed:21321204, ECO:0000269|PubMed:21407207, ECO:0000269|PubMed:21892189, ECO:0000269|PubMed:26774490}. +Q9JLF6 TGM1_MOUSE Protein-glutamine gamma-glutamyltransferase K (EC 2.3.2.13) (Epidermal TGase) (Transglutaminase K) (TG(K)) (TGK) (TGase K) (Transglutaminase-1) (TGase-1) 815 89,826 Active site (3); Chain (1); Metal binding (4); Modified residue (7); Sequence conflict (1) FUNCTION: Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. Responsible for cross-linking epidermal proteins during formation of the stratum corneum. Involved in cell proliferation (By similarity). {ECO:0000250|UniProtKB:P22735}. PTM: Tyrosine-phosphorylated. {ECO:0000269|PubMed:10567386}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Expressed in large amounts in epithelial tissues (lung, liver and kidney). {ECO:0000269|PubMed:10567386}. +Q5SSF7 TET5C_MOUSE Terminal nucleotidyltransferase 5C (EC 2.7.7.19) 391 44,797 Chain (1); Erroneous initiation (2); Sequence conflict (2) FUNCTION: Nucleotidyltransferase that act as a non-canonical poly(A) RNA polymerase which enhances mRNA stability and gene expression. Mainly targets mRNAs encoding endoplasmic reticulum-targeted protein and may be involved in induction of cell death. {ECO:0000269|PubMed:28931820}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28931820}. Nucleus {ECO:0000250|UniProtKB:Q5VWP2}. SUBUNIT: Interacts with BCCIP and PABPC1; the interaction has no effect on TENT5C poly(A) polymerase function. {ECO:0000250|UniProtKB:Q5VWP2}. TISSUE SPECIFICITY: Expressed by splenocytes, expression is increased in activated splenocytes. {ECO:0000269|PubMed:28931820}. +Q3TYG6 TGRM2_MOUSE TOG array regulator of axonemal microtubules protein 2 (Crescerin-2) (Protein FAM179A) 1002 108,975 Alternative sequence (2); Chain (1) +Q9EQH3 VPS35_MOUSE Vacuolar protein sorting-associated protein 35 (Maternal-embryonic 3) (Vesicle protein sorting 35) 796 91,713 Chain (1); Frameshift (1); Modified residue (3); Region (4) FUNCTION: Acts as component of the retromer cargo-selective complex (CSC). The CSC is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway. The recruitment of the CSC to the endosomal membrane involves RAB7A and SNX3. The CSC seems to associate with the cytoplasmic domain of cargo proteins predominantly via VPS35; however, these interactions seem to be of low affinity and retromer SNX proteins may also contribute to cargo selectivity thus questioning the classical function of the CSC. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX3-retromer mediates the retrograde transport of WLS distinct from the SNX-BAR retromer pathway. The SNX27-retromer is believed to be involved in endosome-to-plasma membrane trafficking and recycling of a broad spectrum of cargo proteins. The CSC seems to act as recruitment hub for other proteins, such as the WASH complex and TBC1D5 (Probable). Required for retrograde transport of lysosomal enzyme receptor IGF2R and SLC11A2. Required to regulate transcytosis of the polymeric immunoglobulin receptor (pIgR-pIgA). Required for endosomal localization of WASHC2 and mediates the association of the CSC with the WASH complex (By similarity). {ECO:0000250|UniProtKB:Q96QK1}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Endosome {ECO:0000250|UniProtKB:Q96QK1}. Early endosome {ECO:0000305}. Late endosome {ECO:0000305}. SUBUNIT: Component of the heterotrimeric retromer cargo-selective complex (CSC), also described as vacuolar protein sorting subcomplex (VPS) formed by VPS26 (VPS26A or VPS26B), VPS29 and VPS35. The CSC has a highly elongated structure with VPS26 and VPS29 binding independently at opposite distal ends of VPS35 as central platform (PubMed:21040701, PubMed:20875039, PubMed:21920005). The CSC is believed to associate with variable sorting nexins to form functionally distinct retromer complex variants. The originally described retromer complex (also called SNX-BAR retromer) is a pentamer containing the CSC and a heterodimeric membrane-deforming subcomplex formed between SNX1 or SNX2 and SNX5 or SNX6 (also called SNX-BAR subcomplex); the affinity between the respective CSC and SNX-BAR subcomplexes is low. The CSC associates with SNX3 to form a SNX3-retromer complex. The CSC associates with SNX27, the WASH complex and the SNX-BAR subcomplex to form the SNX27-retromer complex (Probable). Interacts with VPS26A, VPS29, VPS26B and LRRK2 (PubMed:16190980, PubMed:21040701, PubMed:20875039, PubMed:21920005, PubMed:23395371). Interacts with SNX1, SNX2, IGF2R, SNX3, GOLPH3, SLC11A2, WASHC2, FKBP15, WASHC1, EHD1. Interacts with MAGEL2; leading to recruitment of the TRIM27:MAGEL2 E3 ubiquitin ligase complex retromer-containing endosomes (By similarity). {ECO:0000250|UniProtKB:Q96QK1, ECO:0000269|PubMed:16190980, ECO:0000269|PubMed:20875039, ECO:0000269|PubMed:21040701, ECO:0000269|PubMed:21920005, ECO:0000269|PubMed:23395371}. TISSUE SPECIFICITY: Ubiquitous. Highly expressed in fat tissue, testis, brain, kidney, thymus, liver and pancreas, and at lower levels in heart, intestine and skeletal muscle. Detected in oocytes, pre-implantation embryos and at E6.5-E12.5. +Q5KU39 VPS41_MOUSE Vacuolar protein sorting-associated protein 41 homolog (VAM2 homolog) (mVAM2) 853 98,602 Chain (1); Region (1); Repeat (1); Sequence conflict (4); Zinc finger (1) FUNCTION: Plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport and autophagic pathways. Believed to act in part as a core component of the putative HOPS endosomal tethering complex is proposed to be involved in the Rab5-to-Rab7 endosome conversion probably implicating MON1A/B, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion. The HOPS complex is proposed to be recruited to Rab7 on the late endosomal membrane and to regulate late endocytic, phagocytic and autophagic traffic towards lysosomes. Involved in homotypic vesicle fusions between late endosomes and in heterotypic fusions between late endosomes and lysosomes implicated in degradation of endocytosed cargo. Required for fusion of autophagosomes with lysosomes. May link the HOPS complex to endosomal Rab7 via its association with RILP and to lysosomal membranes via its association with ARL8B, suggesting that these interactions may bring the compartments to close proximity for fusion. Involved in the direct trans-Golgi network to late endosomes transport of lysosomal membrane proteins independently of HOPS. Involved in sorting to the regulated secretory pathway presumably implicating the AP-3 adaptor complex. May play a role in HOPS-independent function in the regulated secretory pathway (By similarity). {ECO:0000250|UniProtKB:P49754}. SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250|UniProtKB:P49754}. Late endosome {ECO:0000250|UniProtKB:P49754}. Lysosome {ECO:0000250|UniProtKB:P49754}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:P49754}. Early endosome {ECO:0000250|UniProtKB:P49754}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:P49754}. SUBUNIT: Component of the putative homotypic fusion and vacuole protein sorting (HOPS) complex; the core of which composed of the class C Vps proteins VPS11, VPS16, VPS18 and VPS33A, is associated with VPS39 and VPS41. Interacts with RILP, MON1B. Interacts with ARL8B (GTP-bound form); involved in recruitment to lysosomes and probably hierarchial assembly of the HOPS complex at lysosomal membranes. In vitro can self-assemble into a lattice. Associates with adaptor protein complex 3 (AP-3) and clathrin:AP-3 complexes (By similarity). {ECO:0000250|UniProtKB:P49754}. +Q91VM3 WIPI4_MOUSE WD repeat domain phosphoinositide-interacting protein 4 (WIPI-4) (WD repeat domain X-linked 1) (WD repeat-containing protein 45) 360 39,787 Alternative sequence (1); Chain (1); Repeat (3) FUNCTION: Component of the autophagy machinery that controls the major intracellular degradation process by which cytoplasmic materials are packaged into autophagosomes and delivered to lysosomes for degradation. Activated by the STK11/AMPK signaling pathway upon starvation, WDR45 is involved in autophagosome assembly downstream of WIPI2, regulating the size of forming autophagosomes. Probably recruited to membranes through its PtdIns3P activity. {ECO:0000250|UniProtKB:Q9Y484}. SUBCELLULAR LOCATION: Preautophagosomal structure {ECO:0000250|UniProtKB:Q9Y484}. Cytoplasm {ECO:0000250|UniProtKB:Q9Y484}. Note=Diffusely localized in the cytoplasm under nutrient-rich conditions. Localizes to autophagic structures during starvation-induced autophagy. {ECO:0000250|UniProtKB:Q9Y484}. SUBUNIT: Interacts with WIPI1. Interacts with WIPI2. Interacts with ATG2A and probably ATG2B. Interacts with ULK1. May interact with the PRKAA1, PRKAA2, PRKAB1 and PRKAG1 subunits of the AMPK kinase. May interact with NUDC. {ECO:0000250|UniProtKB:Q9Y484}. +Q3UES3 TNKS2_MOUSE Poly [ADP-ribose] polymerase tankyrase-2 (EC 2.4.2.30) (ADP-ribosyltransferase diphtheria toxin-like 6) (ARTD6) (Protein poly-ADP-ribosyltransferase tankyrase-2) (EC 2.4.2.-) (TNKS-2) (TRF1-interacting ankyrin-related ADP-ribose polymerase 2) (Tankyrase II) (Tankyrase-2) (TANK2) 1166 126,744 Chain (1); Compositional bias (1); Domain (2); Metal binding (4); Modified residue (10); Region (1); Repeat (18); Sequence conflict (4) FUNCTION: Poly-ADP-ribosyltransferase involved in various processes such as Wnt signaling pathway, telomere length and vesicle trafficking. Acts as an activator of the Wnt signaling pathway by mediating poly-ADP-ribosylation of AXIN1 and AXIN2, 2 key components of the beta-catenin destruction complex: poly-ADP-ribosylated target proteins are recognized by RNF146, which mediates their ubiquitination and subsequent degradation. Also mediates poly-ADP-ribosylation of BLZF1 and CASC3, followed by recruitment of RNF146 and subsequent ubiquitination. Mediates poly-ADP-ribosylation of TERF1, thereby contributing to the regulation of telomere length. Stimulates 26S proteasome activity. {ECO:0000250|UniProtKB:Q9H2K2}. PTM: Ubiquitinated by RNF146 when auto-poly-ADP-ribosylated, leading to its degradation. {ECO:0000250|UniProtKB:Q9H2K2}.; PTM: ADP-ribosylated (-auto). Poly-ADP-ribosylated protein is recognized by RNF146, followed by ubiquitination. {ECO:0000250|UniProtKB:Q9H2K2}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H2K2}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9H2K2}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9H2K2}. Nucleus {ECO:0000250|UniProtKB:Q9H2K2}. Chromosome, telomere {ECO:0000250|UniProtKB:Q9H2K2}. Note=Associated with the Golgi and with juxtanuclear SLC2A4/GLUT4-vesicles (By similarity). Also found around the pericentriolar matrix of mitotic centromeres (By similarity). During interphase, a small fraction of TNKS2 is found in the nucleus, associated with TRF1 (By similarity). {ECO:0000250|UniProtKB:Q9H2K2}. SUBUNIT: Oligomerizes and associates with TNKS. Interacts with the cytoplasmic domain of LNPEP/Otase in SLC2A4/GLUT4-vesicles. Binds to the N-terminus of Grb14 and TRF1 with its ankyrin repeat region. Interacts with HIF1AN. Interacts with RNF146; this interaction leads to ubiquitination and proteasomal degradation. Interacts with NUMA1 (By similarity). {ECO:0000250|UniProtKB:Q9H2K2}. +P41155 TNFC_MOUSE Lymphotoxin-beta (LT-beta) (Tumor necrosis factor C) (TNF-C) (Tumor necrosis factor ligand superfamily member 3) 306 32,329 Chain (1); Glycosylation (2); Topological domain (2); Transmembrane (1) TRANSMEM 28 48 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 27 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 49 306 Extracellular. {ECO:0000255}. FUNCTION: Cytokine that binds to LTBR/TNFRSF3. May play a specific role in immune response regulation. Provides the membrane anchor for the attachment of the heterotrimeric complex to the cell surface. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. SUBUNIT: Heterotrimer of either two LTB and one LTA subunits or (less prevalent) two LTA and one LTB subunits. {ECO:0000250}. +Q9JMG3 TMUB1_MOUSE Transmembrane and ubiquitin-like domain-containing protein 1 (Hepatocyte odd protein shuttling protein) [Cleaved into: iHOPS] 245 26,316 Alternative sequence (1); Chain (2); Domain (1); Modified residue (3); Region (1); Sequence conflict (1); Transmembrane (3) TRANSMEM 11 31 Helical. {ECO:0000255}.; TRANSMEM 194 214 Helical. {ECO:0000255}.; TRANSMEM 219 239 Helical. {ECO:0000255}. FUNCTION: Involved in sterol-regulated ubiquitination and degradation of HMG-CoA reductase HMGCR (By similarity). Involved in positive regulation of AMPA-selective glutamate receptor GRIA2 recycling to the cell surface (By similarity). Acts as negative regulator of hepatocyte growth during regeneration (By similarity). {ECO:0000250|UniProtKB:Q53AQ4, ECO:0000250|UniProtKB:Q9BVT8, ECO:0000269|PubMed:16014383, ECO:0000269|PubMed:18418082, ECO:0000269|PubMed:22890319}.; FUNCTION: iHOPS: May contribute to the regulation of translation during cell-cycle progression. May contribute to the regulation of cell proliferation (PubMed:16014383). May be involved in centrosome assembly (PubMed:18418082). Modulates stabilization and nucleolar localization of tumor suppressor CDKN2A and enhances association between CDKN2A and NPM1 (PubMed:22890319). {ECO:0000269|PubMed:18418082, ECO:0000269|PubMed:22890319}. PTM: iHOPS: Isoform 1 (lHOPS) is processed by regulated intramembrane proteolysis (RIP) in the N-terminus to release iHOPS from membranes. {ECO:0000269|PubMed:24240191}.; PTM: Isoform 2 seems to undergo a selective cleavage in the C-terminal region to release an additional cytoplasmic form. {ECO:0000269|PubMed:24240191}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:18665261}; Multi-pass membrane protein {ECO:0000305}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000269|PubMed:18665261}. Recycling endosome {ECO:0000250|UniProtKB:Q53AQ4}. Cytoplasm {ECO:0000269|PubMed:16014383, ECO:0000269|PubMed:20582322}. Nucleus {ECO:0000269|PubMed:16014383}. Nucleus, nucleolus {ECO:0000269|PubMed:22890319}.; SUBCELLULAR LOCATION: Isoform 1: Membrane {ECO:0000250|UniProtKB:Q53AQ4, ECO:0000305|PubMed:24240191}.; SUBCELLULAR LOCATION: Isoform 2: Membrane {ECO:0000250|UniProtKB:Q53AQ4, ECO:0000305|PubMed:24240191}.; SUBCELLULAR LOCATION: iHOPS: Cytoplasm {ECO:0000250|UniProtKB:Q53AQ4, ECO:0000305|PubMed:24240191}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000305|PubMed:24240191}. Nucleus, nucleolus {ECO:0000305|PubMed:24240191}. Nucleus {ECO:0000305|PubMed:24240191}. Note=iHOPS is proposed to be the shuttling form across different cellular compartments (PubMed:24240191). XPO1-dependent exported from the nucleus in dividing cells. Predominantly nuclear during growth arrest (PubMed:16014383). {ECO:0000269|PubMed:16014383, ECO:0000305|PubMed:24240191}. SUBUNIT: Interacts with EEF1A1, CAMLG, GRIA2 and GRIP1. Interacts with NPM1 and CDKN2A; TMUB1 can enhance interaction between NPM1 and CDKN2A and is proposed to bridge the proteins; proposed to be mediated by iHOPS (PubMed:16014383, PubMed:18665261, PubMed:20582322, PubMed:22890319, PubMed:24240191). Interacts with TUBG1 (By similarity). Interacts with ERLIN2 and AMFR; TMUB1 promotes the interaction of ERLIN2 with AMFR (By similarity). {ECO:0000250|UniProtKB:Q53AQ4, ECO:0000250|UniProtKB:Q9BVT8, ECO:0000269|PubMed:16014383, ECO:0000269|PubMed:18665261, ECO:0000269|PubMed:20582322, ECO:0000269|PubMed:22890319, ECO:0000269|PubMed:24240191}. TISSUE SPECIFICITY: Expressed in adult brain; at protein level (PubMed:18665261, PubMed:20582322). Isoform 1 (lHOPS) is highly expressed in small intestine, stomach and epididymis. Isoform 2 (sHOPS) and iHOPS are abundantly expressed in brain, liver and adrenal gland (PubMed:24240191). {ECO:0000269|PubMed:20582322, ECO:0000269|PubMed:24240191}. +Q3KQJ0 TMM69_MOUSE Transmembrane protein 69 245 27,313 Chain (1); Sequence caution (1); Sequence conflict (1); Transmembrane (5) TRANSMEM 97 117 Helical. {ECO:0000255}.; TRANSMEM 122 142 Helical. {ECO:0000255}.; TRANSMEM 159 179 Helical. {ECO:0000255}.; TRANSMEM 185 205 Helical. {ECO:0000255}.; TRANSMEM 216 236 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +P50752 TNNT2_MOUSE Troponin T, cardiac muscle (TnTc) (Cardiac muscle troponin T) (cTnT) 301 35,825 Alternative sequence (3); Chain (1); Initiator methionine (1); Modified residue (6) FUNCTION: Troponin T is the tropomyosin-binding subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity. PTM: Phosphorylation at Thr-216 by PRKCA induces significant reduction in myofilament calcium sensitivity and actomyosin ATPase activity. {ECO:0000269|PubMed:12832403}. +Q9D777 TNF13_MOUSE Tumor necrosis factor ligand superfamily member 13 (A proliferation-inducing ligand) (APRIL) (CD antigen CD256) 241 26,889 Beta strand (10); Chain (1); Disulfide bond (1); Glycosylation (1); Propeptide (1); Sequence conflict (1); Site (1); Turn (3) FUNCTION: Cytokine that binds to TNFRSF13B/TACI and to TNFRSF17/BCMA. Plays a role in the regulation of tumor cell growth. May be involved in monocyte/macrophage-mediated immunological processes. {ECO:0000269|PubMed:15488762}. PTM: The soluble form derives from the membrane form by proteolytic processing. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Homotrimer. {ECO:0000305}. +Q8BQU7 TMM74_MOUSE Transmembrane protein 74 305 33,416 Chain (1); Compositional bias (1); Modified residue (1); Transmembrane (2) TRANSMEM 178 198 Helical. {ECO:0000255}.; TRANSMEM 232 252 Helical. {ECO:0000255}. FUNCTION: Plays an essential role in autophagy. TMEM74-induced autophagy may involve PI3K signal transduction (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Lysosome membrane; Multi-pass membrane protein. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q91X86 TMM98_MOUSE Transmembrane protein 98 226 24,684 Chain (1); Transmembrane (1) TRANSMEM 4 24 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q8BXZ1 TMX3_MOUSE Protein disulfide-isomerase TMX3 (EC 5.3.4.1) (Thioredoxin domain-containing protein 10) (Thioredoxin-related transmembrane protein 3) 456 51,848 Chain (1); Disulfide bond (1); Domain (1); Erroneous initiation (1); Frameshift (1); Glycosylation (3); Motif (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 379 399 Helical. {ECO:0000255}. TOPO_DOM 30 378 Lumenal. {ECO:0000255}.; TOPO_DOM 400 456 Cytoplasmic. {ECO:0000255}. FUNCTION: Probable disulfide isomerase, which participates in the folding of proteins containing disulfide bonds. May act as a dithiol oxidase (By similarity). {ECO:0000250}. PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. DOMAIN: The di-lysine motif confers endoplasmic reticulum localization for type I membrane proteins. {ECO:0000250}. +P41047 TNFL6_MOUSE Tumor necrosis factor ligand superfamily member 6 (CD95 ligand) (CD95-L) (Fas antigen ligand) (Fas ligand) (FasL) (CD antigen CD178) [Cleaved into: Tumor necrosis factor ligand superfamily member 6, membrane form; Tumor necrosis factor ligand superfamily member 6, soluble form (Receptor-binding FasL ectodomain) (Soluble Fas ligand) (sFasL); ADAM10-processed FasL form (APL); FasL intracellular domain (FasL ICD) (SPPL2A-processed FasL form) (SPA)] 279 31,442 Alternative sequence (1); Chain (4); Compositional bias (2); Disulfide bond (1); Glycosylation (4); Natural variant (3); Site (2); Topological domain (2); Transmembrane (1) TRANSMEM 79 100 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 78 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 101 279 Extracellular. {ECO:0000255}. FUNCTION: Cytokine that binds to TNFRSF6/FAS, a receptor that transduces the apoptotic signal into cells (PubMed:7511063). Involved in cytotoxic T-cell-mediated apoptosis, natural killer cell-mediated apoptosis and in T-cell development (PubMed:19794494, PubMed:7532682). Initiates fratricidal/suicidal activation-induced cell death (AICD) in antigen-activated T-cells contributing to the termination of immune responses (PubMed:19794494). TNFRSF6/FAS-mediated apoptosis has also a role in the induction of peripheral tolerance (PubMed:10779162). Binds to TNFRSF6B/DcR3, a decoy receptor that blocks apoptosis (By similarity). {ECO:0000250|UniProtKB:P48023, ECO:0000269|PubMed:19794494, ECO:0000269|PubMed:7511063, ECO:0000269|PubMed:7532682}.; FUNCTION: Tumor necrosis factor ligand superfamily member 6, soluble form: Induces FAS-mediated activation of NF-kappa-B, initiating non-apoptotic signaling pathways (PubMed:19794494). Can induce apoptosis but does not appear to be essential for this process (By similarity). {ECO:0000250|UniProtKB:P48023, ECO:0000269|PubMed:19794494}.; FUNCTION: FasL intracellular domain: Cytoplasmic form induces gene transcription inhibition. {ECO:0000250|UniProtKB:P48023}. PTM: The soluble form derives from the membrane form by proteolytic processing. The membrane-bound form undergoes two successive intramembrane proteolytic cleavages. The first one is processed by ADAM10 producing an N-terminal fragment, which lacks the receptor-binding extracellular domain. This ADAM10-processed FasL (FAsL APL) remnant form is still membrane anchored and further processed by SPPL2A that liberates the FasL intracellular domain (FasL ICD). FasL shedding by ADAM10 is a prerequisite for subsequent intramembrane cleavage by SPPL2A in T-cells. {ECO:0000250|UniProtKB:P48023}.; PTM: Phosphorylated by FGR on tyrosine residues; this is required for ubiquitination and subsequent internalization. {ECO:0000250|UniProtKB:P48023}.; PTM: N-glycosylated. Glycosylation enhances apoptotic activity. {ECO:0000250|UniProtKB:P48023}.; PTM: Monoubiquitinated. {ECO:0000250|UniProtKB:P48023}. SUBCELLULAR LOCATION: Isoform FasL: Cell membrane {ECO:0000269|PubMed:19794494, ECO:0000269|PubMed:7532682}; Single-pass type II membrane protein {ECO:0000255}. Cytoplasmic vesicle lumen {ECO:0000250|UniProtKB:P48023}. Lysosome lumen {ECO:0000250|UniProtKB:P48023}. Note=Is internalized into multivesicular bodies of secretory lysosomes after phosphorylation by FGR and monoubiquitination. Colocalizes with the SPPL2A protease at the cell membrane. {ECO:0000250|UniProtKB:P48023}.; SUBCELLULAR LOCATION: Tumor necrosis factor ligand superfamily member 6, soluble form: Secreted {ECO:0000269|PubMed:10552956, ECO:0000269|PubMed:19794494}. Note=May be released into the extracellular fluid by cleavage from the cell surface. {ECO:0000250|UniProtKB:P48023}.; SUBCELLULAR LOCATION: FasL intracellular domain: Nucleus {ECO:0000250|UniProtKB:P48023}. Note=The FasL ICD cytoplasmic form is translocated into the nucleus. {ECO:0000250|UniProtKB:P48023}. SUBUNIT: Homotrimer. Interacts with ARHGAP9, BAIAP2L1, BTK, CACNB3, CACNB4, CRK, DLG2, DNMBP, DOCK4, EPS8L3, FGR, FYB1, FYN, HCK, ITK, ITSN2, KALRN, LYN, MACC1, MIA, MPP4, MYO15A, NCF1, NCK1, NCK2, NCKIPSD, OSTF1, PIK3R1, PSTPIP1, RIMBP3C, SAMSN1, SH3GL3, SH3PXD2B, SH3PXD2A, SH3RF2, SKAP2, SNX33, SNX9, SORBS3, SPTA1, SRC, SRGAP1, SRGAP2, SRGAP3, TEC, TJP3 and YES1. {ECO:0000250|UniProtKB:P48023}. TISSUE SPECIFICITY: Expressed in T-cells (PubMed:19794494). Expressed in natural killer cells (PubMed:7532682). {ECO:0000269|PubMed:19794494, ECO:0000269|PubMed:7532682}. DISEASE: Note=A deficiency in this protein is the cause of generalized lymphoproliferation disease phenotype (gld). Gld mice present lymphadenopathy and autoantibody production. The phenotype is recessively inherited. {ECO:0000269|PubMed:7511063}. +P47741 TNR4_MOUSE Tumor necrosis factor receptor superfamily member 4 (OX40 antigen) (OX40L receptor) (CD antigen CD134) 272 30,154 Chain (1); Disulfide bond (9); Glycosylation (1); Repeat (4); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 212 236 Helical. {ECO:0000255}. TOPO_DOM 20 211 Extracellular. {ECO:0000255}.; TOPO_DOM 237 272 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for TNFSF4/OX40L/GP34. Is a costimulatory molecule implicated in long-term T-cell immunity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Interacts with TRAF2, TRAF3 and TRAF5. {ECO:0000250}. +Q9WU72 TN13B_MOUSE Tumor necrosis factor ligand superfamily member 13B (B-cell-activating factor) (BAFF) (CD antigen CD257) [Cleaved into: Tumor necrosis factor ligand superfamily member 13b, membrane form; Tumor necrosis factor ligand superfamily member 13b, soluble form] 309 34,192 Alternative sequence (1); Chain (2); Disulfide bond (1); Glycosylation (2); Natural variant (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 48 68 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 47 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 69 309 Extracellular. {ECO:0000255}. FUNCTION: Cytokine that binds to TNFRSF13B/TACI and TNFRSF17/BCMA. TNFSF13/APRIL binds to the same 2 receptors. Together, they form a 2 ligands -2 receptors pathway involved in the stimulation of B- and T-cell function and the regulation of humoral immunity. A third B-cell specific BAFF-receptor (BAFFR/BR3) promotes the survival of mature B-cells and the B-cell response. {ECO:0000269|PubMed:12867412}.; FUNCTION: Isoform 2 seems to inhibit isoform 1 secretion and bioactivity. {ECO:0000269|PubMed:12867412}. PTM: The soluble form derives from the membrane form by proteolytic processing.; PTM: Isoform 2 is not efficiently shed from the membrane unlike isoform 1. SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein.; SUBCELLULAR LOCATION: Tumor necrosis factor ligand superfamily member 13b, soluble form: Secreted. SUBUNIT: Homotrimer. Isoform 2 heteromultimerizes with isoform 1, probably limiting the amount of functional isoform 1 on the cell surface. {ECO:0000269|PubMed:12867412}. TISSUE SPECIFICITY: Isoform 2 is expressed in many myeloid cell lines. {ECO:0000269|PubMed:12867412}. +Q8BKI2 TNR6B_MOUSE Trinucleotide repeat-containing gene 6B protein 1810 191,963 Alternative sequence (4); Chain (1); Coiled coil (1); Domain (1); Modified residue (7); Region (3); Sequence conflict (2) FUNCTION: Plays a role in RNA-mediated gene silencing by both micro-RNAs (miRNAs) and short interfering RNAs (siRNAs). Required for miRNA-dependent translational repression and siRNA-dependent endonucleolytic cleavage of complementary mRNAs by argonaute family proteins As scaffoldng protein associates with argonaute proteins bound to partially complementary mRNAs and simultaneously can recruit CCR4-NOT and PAN deadenylase complexes (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000250}. Note=Mammalian P-bodies are also known as GW bodies (GWBs). {ECO:0000250}. SUBUNIT: Interacts with AGO1, AGO2, AGO3 and AGO4. Interacts with CNOT1; the interaction mediates the association with the CCR4-NOT complex. Interacts with PAN3; the interaction mediates the association with the PAN complex (By similarity). Interacts with MOV10; the interaction is direct and RNA-dependent (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9UPQ9}. +P20801 TNNC2_MOUSE Troponin C, skeletal muscle (STNC) 160 18,110 Calcium binding (4); Chain (1); Domain (4); Initiator methionine (1); Modified residue (1) FUNCTION: Troponin is the central regulatory protein of striated muscle contraction. Tn consists of three components: Tn-I which is the inhibitor of actomyosin ATPase, Tn-T which contains the binding site for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the inhibitory action of Tn on actin filaments. TISSUE SPECIFICITY: Fast skeletal muscle. +Q6ZQF0 TOPB1_MOUSE DNA topoisomerase 2-binding protein 1 (DNA topoisomerase II-beta-binding protein 1) (TopBP1) (DNA topoisomerase II-binding protein 1) 1515 168,860 Beta strand (6); Chain (1); Compositional bias (1); Domain (7); Erroneous initiation (2); Frameshift (1); Helix (9); Modified residue (8); Motif (1); Natural variant (1); Sequence conflict (6); Turn (3) FUNCTION: Required for DNA replication (By similarity). Plays a role in the rescue of stalled replication forks and checkpoint control (PubMed:14718568). Binds double-stranded DNA breaks and nicks as well as single-stranded DNA (By similarity). Recruits the SWI/SNF chromatin remodeling complex to E2F1-responsive promoters. Down-regulates E2F1 activity and inhibits E2F1-dependent apoptosis during G1/S transition and after DNA damage (By similarity). Induces a large increase in the kinase activity of ATR (By similarity). {ECO:0000250|UniProtKB:Q92547, ECO:0000269|PubMed:14718568}. PTM: Phosphorylated on serine and threonine residues in response to X-ray irradiation. {ECO:0000250|UniProtKB:Q92547}.; PTM: Ubiquitinated and degraded by the proteasome. X-ray irradiation reduces ubiquitination. {ECO:0000250|UniProtKB:Q92547}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle pole. Chromosome. Note=Has a uniform nuclear distribution during G phase. Colocalizes with BRCA1 at stalled replication forks during S phase. In mitotic cells it colocalizes with BRCA1 at spindle poles and centrosomes during metaphase and anaphase. Detected in discrete foci together with PML and numerous DNA repair enzymes after DNA damage by alkylating agents, UV or gamma irradiation. Localizes to sites of DNA damage in a H2AX-independent manner (By similarity). Detected on unpaired autosomes in meiotic prophase cells. Detected on X and Y chromosomes during later stages of prophase. Colocalizes with ATR and H2AFX at unsynapsed chromosome cores during prophase. {ECO:0000250}. SUBUNIT: Interacts with POLE. Interacts with RAD9A. Interacts with UBR5. Interacts with E2F1. Interacts with PML. Interacts with SMARCA2. Interacts with SMARCA4. Interacts with RHNO1. May interact with TOP2B. Interacts with TICRR. Interacts with HELB. {ECO:0000250|UniProtKB:Q92547}. TISSUE SPECIFICITY: Highly expressed in testis. {ECO:0000269|PubMed:15138768}. +Q9JJ78 TOPK_MOUSE Lymphokine-activated killer T-cell-originated protein kinase (EC 2.7.12.2) (PDZ-binding kinase) (T-LAK cell-originated protein kinase) 330 36,745 Active site (1); Binding site (1); Chain (1); Cross-link (1); Domain (1); Modified residue (5); Nucleotide binding (1); Sequence conflict (1) FUNCTION: Phosphorylates MAP kinase p38. Seems to be active only in mitosis. May also play a role in the activation of lymphoid cells. When phosphorylated, forms a complex with TP53, leading to TP53 destabilization (By similarity). {ECO:0000250}. PTM: Phosphorylated; in a cell-cycle dependent manner at mitosis. {ECO:0000250}. SUBUNIT: Interacts with DLG1 and TP53. {ECO:0000250}. +Q80Z37 TOPRS_MOUSE E3 ubiquitin-protein ligase Topors (EC 2.3.2.27) (RING-type E3 ubiquitin transferase Topors) (SUMO1-protein E3 ligase Topors) (Topoisomerase I-binding RING finger protein) (Topoisomerase I-binding arginine/serine-rich protein) (Tumor suppressor p53-binding protein 3) (p53-binding protein 3) (p53BP3) 1033 117,082 Chain (1); Compositional bias (2); Cross-link (10); Modified residue (13); Region (6); Sequence caution (1); Sequence conflict (4); Zinc finger (1) FUNCTION: Functions as an E3 ubiquitin-protein ligase and as a E3 SUMO1-protein ligase. Probable tumor suppressor involved in cell growth, cell proliferation and apoptosis that regulates p53/TP53 stability through ubiquitin-dependent degradation. May regulate chromatin modification through sumoylation of several chromatin modification-associated proteins. May be involved in DNA-damage-induced cell death through IKBKE sumoylation. {ECO:0000269|PubMed:15703819, ECO:0000269|PubMed:15735665}. PTM: Phosphorylation at Ser-99 regulates the E3 ubiquitin-protein ligase activity but not the SUMO1-protein ligase activity. Phosphorylation at Ser-718 increases the E3 ubiquitin-protein ligase activity versus the E3 SUMO1-protein ligase activity resulting in increased p53/TP53 ubiquitination and degradation. {ECO:0000250|UniProtKB:Q9NS56}.; PTM: Sumoylated. {ECO:0000250|UniProtKB:Q9NS56}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15703819, ECO:0000269|PubMed:15735665}. Nucleus, PML body {ECO:0000250|UniProtKB:Q9NS56}. Note=Localizes to discrete nuclear foci which partly overlap with PML nuclear bodies. Targeted to PML nuclear bodies upon DNA damage. {ECO:0000250|UniProtKB:Q9NS56}. SUBUNIT: Interacts with TOP1. Interacts with the SUMO1 conjugating enzyme UBE2I. Interacts with SUMO1. Interacts with NKX3-1; polyubiquitinates NKX3-1 and induces its proteasomal degradation. Interacts with SIN3A; sumoylates SIN3A. Interacts with IKBKE; induced by DNA damage (By similarity). Interacts with p53/TP53. Interacts with PARK7/DJ-1. {ECO:0000250|UniProtKB:Q9NS56, ECO:0000269|PubMed:15703819, ECO:0000269|PubMed:15735665}. +Q78XR0 TPC6A_MOUSE Trafficking protein particle complex subunit 6A (TRAPP complex subunit 6A) 159 17,430 Alternative sequence (1); Chain (1); Modified residue (1); Sequence conflict (4) FUNCTION: May play a role in vesicular transport during the biogenesis of melanosomes. {ECO:0000269|PubMed:16697553}. SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. SUBUNIT: Part of the multisubunit transport protein particle (TRAPP) complex. Heterodimer with TRAPPC3 (By similarity). The heterodimer TRAPPC3-TRAPPC6A interacts with TRAPPC2L. Interacts with TRAPPC2L (By similarity). {ECO:0000250|UniProtKB:O75865}. TISSUE SPECIFICITY: Ubiquitous, with lowest expression in skeletal muscle and brain and highest in kidney, liver and testis, as well as in cultured melanocytes. {ECO:0000269|PubMed:16697553}. +Q3TBL6 TP8L3_MOUSE Tumor necrosis factor alpha-induced protein 8-like protein 3 (TNF alpha-induced protein 8-like protein 3) (TNFAIP8-like protein 3) 204 23,243 Chain (1); Mutagenesis (7); Region (1) FUNCTION: Acts as a lipid transfer protein. Preferentially captures and shuttles two lipid second messengers, i.e., phosphatidylinositol 4,5- bisphosphate and phosphatidylinositol 3,4,5-trisphosphate and increases their levels in the plasma membrane. Additionally, may also function as a lipid-presenting protein to enhance the activity of the PI3K-AKT and MEK-ERK pathways. May act as a regulator of tumorigenesis through its activation of phospholipid signaling. {ECO:0000269|PubMed:25242044}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25479791}. Cell membrane {ECO:0000269|PubMed:25242044}. Note=On PDGF activation, translocates from cytoplasm to plasma membrane. {ECO:0000269|PubMed:25242044}. DOMAIN: The N-terminal domain (AA 2-20) is essential for its effect on cell growth and survival. {ECO:0000269|PubMed:25242044}. TISSUE SPECIFICITY: Widely expressed (at protein level). {ECO:0000269|PubMed:25242044, ECO:0000269|PubMed:25479791}. +Q99JR5 TINAL_MOUSE Tubulointerstitial nephritis antigen-like (Adrenocortical zonation factor 1) (AZ-1) (Androgen-regulated gene 1 protein) (Tubulointerstitial nephritis antigen-related protein) (TARP) 466 52,665 Chain (1); Disulfide bond (5); Domain (1); Frameshift (1); Glycosylation (2); Signal peptide (1) FUNCTION: May be implicated in the adrenocortical zonation and in mechanisms for repressing the CYP11B1 gene expression in adrenocortical cells. This is a non catalytic peptidase C1 family protein. {ECO:0000269|PubMed:12600995}. PTM: Glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Highly expressed in kidney, heart and adrenocortical cells of adrenal glands. Moderately expressed in spleen and liver. Also found in prostate, seminal vesicle, epididymis and testis in male reproductive organs. In adrenal glands is found in the outer cortical regions corresponding to the zona glomerulosa (zG) and the undifferentiated cell zone (zU) (at protein level). {ECO:0000269|PubMed:11377975, ECO:0000269|PubMed:12600995}. +Q9ER58 TICN2_MOUSE Testican-2 (SPARC/osteonectin, CWCV, and Kazal-like domains proteoglycan 2) 423 46,863 Chain (1); Compositional bias (1); Disulfide bond (8); Domain (2); Glycosylation (3); Modified residue (1); Signal peptide (1) FUNCTION: May participate in diverse steps of neurogenesis. Binds calcium (By similarity). {ECO:0000250}. PTM: O-glycosylated; contains chondroitin sulfate and heparan sulfate. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000305}. TISSUE SPECIFICITY: Brain specific. +Q8BHM9 TM11F_MOUSE Transmembrane protease serine 11F (EC 3.4.21.-) (Airway trypsin-like protease 4) 439 49,776 Active site (3); Chain (1); Disulfide bond (3); Domain (2); Topological domain (2); Transmembrane (1) TRANSMEM 34 54 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 33 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 55 439 Extracellular. {ECO:0000255}. FUNCTION: Probable serine protease. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. +Q3UME2 TM241_MOUSE Transmembrane protein 241 297 32,965 Alternative sequence (6); Chain (1); Frameshift (1); Sequence conflict (2); Transmembrane (10) TRANSMEM 7 29 Helical. {ECO:0000255}.; TRANSMEM 32 52 Helical. {ECO:0000255}.; TRANSMEM 69 89 Helical. {ECO:0000255}.; TRANSMEM 93 113 Helical. {ECO:0000255}.; TRANSMEM 121 141 Helical. {ECO:0000255}.; TRANSMEM 146 166 Helical. {ECO:0000255}.; TRANSMEM 187 207 Helical. {ECO:0000255}.; TRANSMEM 211 231 Helical. {ECO:0000255}.; TRANSMEM 250 270 Helical. {ECO:0000255}.; TRANSMEM 271 291 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q6PFX9 TNKS1_MOUSE Poly [ADP-ribose] polymerase tankyrase-1 (EC 2.4.2.30) (ADP-ribosyltransferase diphtheria toxin-like 5) (ARTD5) (Protein poly-ADP-ribosyltransferase tankyrase-1) (EC 2.4.2.-) (TRF1-interacting ankyrin-related ADP-ribose polymerase 1) (Tankyrase I) (Tankyrase-1) (TANK1) 1320 140,944 Alternative sequence (1); Beta strand (10); Chain (1); Compositional bias (4); Domain (2); Helix (26); Metal binding (4); Repeat (18); Sequence conflict (2); Turn (6) FUNCTION: Poly-ADP-ribosyltransferase involved in various processes such as Wnt signaling pathway, telomere length and vesicle trafficking. Acts as an activator of the Wnt signaling pathway by mediating poly-ADP-ribosylation (PARsylation) of AXIN1 and AXIN2, 2 key components of the beta-catenin destruction complex: poly-ADP-ribosylated target proteins are recognized by RNF146, which mediates their ubiquitination and subsequent degradation. Also mediates PARsylation of BLZF1 and CASC3, followed by recruitment of RNF146 and subsequent ubiquitination. Mediates PARsylation of TERF1, thereby contributing to the regulation of telomere length. Involved in centrosome maturation during prometaphase by mediating PARsylation of HEPACAM2/MIKI. May also regulate vesicle trafficking and modulate the subcellular distribution of SLC2A4/GLUT4-vesicles. May be involved in spindle pole assembly through PARsylation of NUMA1. Stimulates 26S proteasome activity. {ECO:0000250|UniProtKB:O95271}. PTM: Phosphorylated on serine residues by MAPK kinases upon insulin stimulation. Phosphorylated during mitosis. {ECO:0000250|UniProtKB:O95271}.; PTM: Ubiquitinated by RNF146 when auto-poly-ADP-ribosylated, leading to its degradation. {ECO:0000250|UniProtKB:O95271}.; PTM: ADP-ribosylated (-auto). Poly-ADP-ribosylated protein is recognized by RNF146, followed by ubiquitination. {ECO:0000250|UniProtKB:O95271}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O95271}. Golgi apparatus membrane {ECO:0000250|UniProtKB:O95271}; Peripheral membrane protein {ECO:0000250|UniProtKB:O95271}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:O95271}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:O95271}. Chromosome, telomere {ECO:0000250|UniProtKB:O95271}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:O95271}. Note=Associated with the Golgi and with juxtanuclear SLC2A4/GLUT4-vesicles. A minor proportion is also found at nuclear pore complexes and around the pericentriolar matrix of mitotic centromeres. During interphase, a small fraction of TNKS is found in the nucleus, associated with TERF1. Localizes to spindle poles at mitosis onset via interaction with NUMA1. {ECO:0000250|UniProtKB:O95271}. SUBUNIT: Oligomerizes and associates with TNKS2. Interacts with the cytoplasmic domain of LNPEP/Otase in SLC2A4/GLUT4-vesicles. Binds to the N-terminus of telomeric TERF1 via the ANK repeats. Found in a complex with POT1; TERF1 and TINF2. Interacts with AXIN1. Interacts with AXIN2. Interacts with BLZF1 and CASC3. Interacts with NUMA1. {ECO:0000250|UniProtKB:O95271}. +Q8VCA5 TMPS4_MOUSE Transmembrane protease serine 4 (EC 3.4.21.-) (Channel-activating protease 2) (mCAP2) 435 47,496 Active site (3); Chain (1); Disulfide bond (8); Domain (3); Glycosylation (2); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 31 51 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 30 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 52 435 Extracellular. {ECO:0000255}. FUNCTION: Probable protease. Seems to be capable of activating ENaC. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. +Q8BIK6 TMPS7_MOUSE Transmembrane protease serine 7 (EC 3.4.21.-) (Matriptase-3) 829 92,590 Active site (3); Chain (1); Disulfide bond (15); Domain (7); Frameshift (1); Glycosylation (2); Sequence caution (1); Sequence conflict (5); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 63 83 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 62 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 84 829 Extracellular. {ECO:0000255}. FUNCTION: Serine protease which preferentially hydrolyzes peptides with Arg at the P1 position. {ECO:0000269|PubMed:15853774}. PTM: N-glycosylated. {ECO:0000269|PubMed:15853774}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15853774}; Single-pass type II membrane protein {ECO:0000269|PubMed:15853774}. SUBUNIT: Forms a heterodimer with SERPINA5. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain, eye, testis, skin, epididymis and salivary gland with lower levels in heart, skeletal muscle, thymus, ovary, prostate and uterus. {ECO:0000269|PubMed:15853774}. +P19123 TNNC1_MOUSE Troponin C, slow skeletal and cardiac muscles (TN-C) 161 18,421 Calcium binding (3); Chain (1); Domain (4); Modified residue (2) FUNCTION: Troponin is the central regulatory protein of striated muscle contraction. Tn consists of three components: Tn-I which is the inhibitor of actomyosin ATPase, Tn-T which contains the binding site for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the inhibitory action of Tn on actin filaments. +Q9D7S1 TMM54_MOUSE Transmembrane protein 54 219 23,427 Chain (1); Sequence conflict (1); Transmembrane (4) TRANSMEM 22 42 Helical. {ECO:0000255}.; TRANSMEM 62 82 Helical. {ECO:0000255}.; TRANSMEM 94 114 Helical. {ECO:0000255}.; TRANSMEM 155 175 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8C0L0 TMX4_MOUSE Thioredoxin-related transmembrane protein 4 (Thioredoxin domain-containing protein 13) 335 37,131 Chain (1); Compositional bias (1); Disulfide bond (1); Domain (1); Erroneous initiation (2); Modified residue (2); Sequence conflict (1); Signal peptide (1); Transmembrane (1) TRANSMEM 186 206 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q9QY73 TMM59_MOUSE Transmembrane protein 59 (Thymic dendritic cell-derived factor 1) 323 36,314 Chain (1); Glycosylation (1); Modified residue (1); Motif (1); Sequence conflict (8); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 239 259 Helical. {ECO:0000255}. TOPO_DOM 36 238 Extracellular. {ECO:0000255}.; TOPO_DOM 260 323 Cytoplasmic. {ECO:0000255}. FUNCTION: Acts as a regulator of autophagy in response to S.aureus infection by promoting activation of LC3 (MAP1LC3A, MAP1LC3B or MAP1LC3C). Acts by interacting with ATG16L1, leading to promote a functional complex between LC3 and ATG16L1 and promoting LC3 lipidation and subsequent activation of autophagy. Modulates the O-glycosylation and complex N-glycosylation steps occurring during the Golgi maturation of several proteins such as APP, BACE1, SEAP or PRNP. Inhibits APP transport to the cell surface and further shedding. {ECO:0000250|UniProtKB:Q9BXS4}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9BXS4}. SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250|UniProtKB:Q9BXS4}; Single-pass type I membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:Q9BXS4}; Single-pass type I membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q9BXS4}; Single-pass type I membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9BXS4}; Single-pass type I membrane protein {ECO:0000255}. Note=Mainly localizes to late endosomes/lysosomes. Probably first exported to the cell surface and then actively endocytosed to transiently localize in early endosomes on its way to the late endosomal/lysosomal compartment where it becomes quickly degraded. {ECO:0000250|UniProtKB:Q9BXS4}. SUBUNIT: Interacts with ATG16L1 (via WD repeats). {ECO:0000250|UniProtKB:Q9BXS4}. DOMAIN: The ATG16L1-binding motif mediates interaction with ATG16L1 and promotes autophagy. {ECO:0000250|UniProtKB:Q9BXS4}. +Q3TUD9 TMM18_MOUSE Transmembrane protein 18 140 16,526 Chain (1); Coiled coil (1); Erroneous initiation (1); Motif (1); Region (1); Topological domain (4); Transmembrane (3) TRANSMEM 26 46 Helical. {ECO:0000255}.; TRANSMEM 53 73 Helical. {ECO:0000255}.; TRANSMEM 92 112 Helical. {ECO:0000255}. TOPO_DOM 1 25 Perinuclear space. {ECO:0000255}.; TOPO_DOM 47 52 Nuclear. {ECO:0000255}.; TOPO_DOM 74 91 Perinuclear space. {ECO:0000255}.; TOPO_DOM 113 140 Nuclear. {ECO:0000255}. FUNCTION: Transcription repressor. Sequence-specific ssDNA and dsDNA binding protein, with preference for GCT end CTG repeats. Cell migration modulator which enhances the glioma-specific migration ability of neural stem cells (NSC) and neural precursor cells (NPC) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96B42}. Nucleus membrane {ECO:0000250|UniProtKB:Q96B42}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Forms homooligomers, independently of the DNA-binding domain. {ECO:0000250}. +P49813 TMOD1_MOUSE Tropomodulin-1 (Erythrocyte tropomodulin) (E-Tmod) 359 40,466 Chain (1); Region (1); Sequence conflict (1) FUNCTION: Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P28289}. Note=In myofibrils with sarcomeric structure, localizes to the pointed end of actin thin filaments. {ECO:0000250|UniProtKB:P28289}. SUBUNIT: Binds to the N-terminus of tropomyosin and to actin. TISSUE SPECIFICITY: Highly expressed in the erythrocyte, heart and skeletal muscle. +Q9WUZ5 TNNI1_MOUSE Troponin I, slow skeletal muscle (Troponin I, slow-twitch isoform) 187 21,698 Calcium binding (1); Chain (1); Initiator methionine (1); Modified residue (2); Region (2) FUNCTION: Troponin I is the inhibitory subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity. SUBUNIT: Binds to actin and tropomyosin. +Q9WUU8 TNIP1_MOUSE TNFAIP3-interacting protein 1 (A20-binding inhibitor of NF-kappa-B activation 1) (ABIN) (ABIN-1) (Nef-associated factor 1) (Naf1) (Virion-associated nuclear shuttling protein) (VAN) (mVAN) 647 73,050 Alternative sequence (2); Chain (1); Coiled coil (3); Compositional bias (2); Modified residue (9); Motif (1); Mutagenesis (5); Region (3); Sequence conflict (3) FUNCTION: Inhibits NF-kappa-B activation and TNF-induced NF-kappa-B-dependent gene expression by regulating A20/TNFAIP3-mediated deubiquitination of IKBKG; proposed to link A20/TNFAIP3 to ubiquitinated IKBKG. Involved in regulation of EGF-induced ERK1/ERK2 signaling pathway; blocks MAPK3/MAPK1 nuclear translocation and MAPK1-dependent transcription. Increases cell surface CD4(T4) antigen expression. Involved in the anti-inflammatory response of macrophages and positively regulates TLR-induced activation of CEBPB. Involved in the prevention of autoimmunity; this function implicates binding to polyubiquitin. Involved in leukocyte integrin activation during inflammation; this function is mediated by association with SELPLG and dependent on phosphorylation by SRC-family kinases. {ECO:0000269|PubMed:12586352, ECO:0000269|PubMed:21606507, ECO:0000269|PubMed:22011580}. PTM: Phosphorylation at Tyr-565 by SRC-family kinases recruits phosphoinositide-3-kinase (PI3K) PIK3CD:p85 heterodimer which results in integrin activation and leukocyte adhesion to activated endothelium during inflammation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Shuttles between the nucleus and cytoplasm in a CRM1-dependent manner. {ECO:0000250}. SUBUNIT: Interacts with TNFAIP3 and IKBKG (polyubiquitinated); facilitates TNFAIP3-mediated de-ubiquitination of NEMO/IKBKG. Interacts with polyubiquitin. Interacts with MAPK1, SELPLG and PIK3CD. Interacts with IRAK1 (polyubiquitinated). Interacts with MYD88; the interaction is indicative for participation in an activated TLR-signaling complex. {ECO:0000269|PubMed:11389905, ECO:0000269|PubMed:12586352, ECO:0000269|PubMed:18212736, ECO:0000269|PubMed:22011580}. TISSUE SPECIFICITY: Ubiquitous. Abundant in heart and skeletal muscle and expressed at lower levels in thymus, liver, kidney, brain and intestinal tract. +Q9JM55 TOB2_MOUSE Protein Tob2 (Transducer of erbB-2 2) 345 36,798 Chain (1); Modified residue (1) FUNCTION: Anti-proliferative protein inhibits cell cycle progression from the G0/G1 to S phases. {ECO:0000250}. SUBUNIT: Associates with CAF1. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. +Q64511 TOP2B_MOUSE DNA topoisomerase 2-beta (EC 5.99.1.3) (DNA topoisomerase II, beta isozyme) 1612 181,909 Active site (1); Binding site (2); Chain (1); Cross-link (32); Domain (1); Initiator methionine (1); Metal binding (4); Modified residue (33); Nucleotide binding (3); Region (2); Sequence conflict (2); Site (9) FUNCTION: Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks. {ECO:0000250|UniProtKB:Q02880}. SUBCELLULAR LOCATION: Nucleus, nucleolus. SUBUNIT: Homodimer (By similarity). Interacts with KIAA1210 (PubMed:28203736). {ECO:0000250|UniProtKB:Q02880, ECO:0000269|PubMed:28203736}. +Q8BH02 TOR4A_MOUSE Torsin-4A (Torsin family 4 member A) 426 47,586 Chain (1); Frameshift (1); Modified residue (4); Nucleotide binding (1); Transmembrane (1) TRANSMEM 117 133 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +O70157 TOP3A_MOUSE DNA topoisomerase 3-alpha (EC 5.99.1.2) (DNA topoisomerase III alpha) 1003 112,358 Active site (1); Chain (1); Domain (1); Region (1); Repeat (2); Zinc finger (1) FUNCTION: Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone. As an essential component of the RMI complex it is involved in chromosome separation and the processing of homologous recombination intermediates to limit DNA crossover formation in cells. Has DNA decatenation activity. It is required for mtDNA decatenation and segregation after completion of replication, in a process that does not require BLM, RMI1 and RMI2. {ECO:0000250|UniProtKB:Q13472}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:Q13472}. SUBUNIT: Binds ssDNA. Interacts (via N-terminal region) with BLM; the interaction is direct. Directly interacts with RMI1. Component of the RMI complex, containing at least TOP3A, RMI1 and RMI2. The RMI complex interacts with BLM. {ECO:0000250|UniProtKB:Q13472}. TISSUE SPECIFICITY: Highly expressed in testis. +Q9D289 TPC6B_MOUSE Trafficking protein particle complex subunit 6B (TRAPP complex subunit 6B) 158 17,936 Chain (1) FUNCTION: Component of a transport protein particle (TRAPP) complex that may function in specific stages of inter-organelle traffic (By similarity). Specifically involved in the early development of neural circuitry, likely by controlling the frequency and amplitude of intracellular calcium transients implicated in the regulation of neuron differentiation and survival (By similarity). {ECO:0000250|UniProtKB:Q86SZ2}. SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. SUBUNIT: Homodimer (By similarity). Part of a TRAPP complex. Heterodimer with TRAPPC3 (By similarity). The heterodimer TRAPPC6B-TRAPPC3 interacts with TRAPPC1 likely providing a core for TRAPP complex formation (By similarity). {ECO:0000250|UniProtKB:Q86SZ2}. TISSUE SPECIFICITY: Widely expressed. Expressed in lung, heart, liver, spleen, brain and kidney. {ECO:0000269|PubMed:16828797}. +Q80W03 TOX3_MOUSE TOX high mobility group box family member 3 (Trinucleotide repeat-containing gene 9 protein) 575 63,174 Chain (1); Compositional bias (2); DNA binding (1); Sequence conflict (2) FUNCTION: Transcriptional coactivator of the p300/CBP-mediated transcription complex. Activates transactivation through cAMP response element (CRE) sites. Protects against cell death by inducing antiapoptotic and repressing pro-apoptotic transcripts. Stimulates transcription from the estrogen-responsive or BCL-2 promoters. Required for depolarization-induced transcription activation of the C-FOS promoter in neurons. Associates with chromatin to the estrogen-responsive C3 promoter region (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Homodimer. Interacts (via HGM box) with CITED1 (via C-terminus); the interaction increases estrogen-response element (ERE)-dependent transcription and protection against cell death. Interacts with CREB1 (phosphorylated form). Interacts with CREB1; the interaction is not depolarization dependent. Interacts with CREBBP (via C-terminus) (By similarity). {ECO:0000250}. DOMAIN: the C-terminus is required for calcium responsiveness but not for transactivation activity. {ECO:0000250}.; DOMAIN: The N-terminus is absolutely necessary for transactivation activity. {ECO:0000250}. +Q8CGV2 TPH2_MOUSE Tryptophan 5-hydroxylase 2 (EC 1.14.16.4) (Neuronal tryptophan hydroxylase) (Tryptophan 5-monooxygenase 2) 488 55,859 Chain (1); Domain (1); Metal binding (3); Modified residue (1); Sequence conflict (1) Aromatic compound metabolism; serotonin biosynthesis; serotonin from L-tryptophan: step 1/2. TISSUE SPECIFICITY: Brain specific. +Q66JW3 TOX_MOUSE Thymocyte selection-associated high mobility group box protein TOX (Thymus high mobility group box protein TOX) 526 57,203 Alternative sequence (2); Chain (1); Compositional bias (1); DNA binding (1); Helix (4); Motif (1); Sequence conflict (2) FUNCTION: May play a role in regulating T-cell development. {ECO:0000269|PubMed:11850626}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267, ECO:0000269|PubMed:11850626}. TISSUE SPECIFICITY: Detected in brain, liver, small intestine, spleen, stomach, testis and thymus. {ECO:0000269|PubMed:11850626}. +Q8C013 TPBGL_MOUSE Trophoblast glycoprotein-like 384 41,085 Chain (1); Disulfide bond (4); Glycosylation (1); Repeat (5); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 310 330 Helical. {ECO:0000255}. TOPO_DOM 31 309 Extracellular. {ECO:0000255}.; TOPO_DOM 331 384 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q3TLI0 TPC10_MOUSE Trafficking protein particle complex subunit 10 (Trafficking protein particle complex subunit TMEM1) (Transport protein particle subunit TMEM1) (TRAPP subunit TMEM1) 1259 141,589 Chain (1); Compositional bias (1); Modified residue (1); Sequence conflict (2) FUNCTION: May play a role in vesicular transport from endoplasmic reticulum to Golgi. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network {ECO:0000250}. SUBUNIT: Component of the multisubunit TRAPP (transport protein particle) complex, which includes at least TRAPPC2, TRAPPC2L, TRAPPC3, TRAPPC3L, TRAPPC4, TRAPPC5, TRAPPC8, TRAPPC9, TRAPPC10, TRAPPC11 and TRAPPC12. {ECO:0000250}. +Q9CQP2 TPPC2_MOUSE Trafficking protein particle complex subunit 2 (Sedlin) 140 16,441 Beta strand (5); Chain (1); Helix (5); Mutagenesis (4); Sequence conflict (21) FUNCTION: Prevents ENO1-mediated transcriptional repression and antagonizes ENO1-mediated cell death. May play a role in vesicular transport from endoplasmic reticulum to Golgi (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:19650763}. Nucleus {ECO:0000250|UniProtKB:P0DI81}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250|UniProtKB:P0DI81}. Cytoplasm {ECO:0000269|PubMed:19650763}. Note=Localized in perinuclear granular structures. {ECO:0000269|PubMed:19650763}. SUBUNIT: Part of the multisubunit TRAPP (transport protein particle) complex. Interacts with ENO1, PITX1, SF1 and TRAPPC2L (By similarity). Interacts with TRAPPC3. {ECO:0000250, ECO:0000269|PubMed:19650763}. TISSUE SPECIFICITY: Expressed in chondrocytes at various stages of differentiation, including proliferating, prehypertrophic and hypertrophic chondrocytes in the distal femoral joint. {ECO:0000269|PubMed:19650763}. +O70281 TPST1_MOUSE Protein-tyrosine sulfotransferase 1 (EC 2.8.2.20) (Tyrosylprotein sulfotransferase 1) (TPST-1) 370 42,132 Active site (1); Binding site (5); Chain (1); Disulfide bond (2); Glycosylation (2); Region (3); Site (2); Topological domain (2); Transmembrane (1) TRANSMEM 9 25 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 8 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 26 370 Lumenal. {ECO:0000255}. FUNCTION: Catalyzes the O-sulfation of tyrosine residues within acidic motifs of polypeptides, using 3'-phosphoadenylyl sulfate (PAPS) as cosubstrate. {ECO:0000269|PubMed:9501187}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:O60507}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:O60507}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:O60507}. SUBUNIT: Homodimer. Can also form heterodimers with TPST2. {ECO:0000250|UniProtKB:O60507}. TISSUE SPECIFICITY: Ubiquitous. Detected in heart, brain, lung, liver, spleen, kidney, skeletal muscle and testis. {ECO:0000269|PubMed:9501187}. +O88856 TPST2_MOUSE Protein-tyrosine sulfotransferase 2 (EC 2.8.2.20) (Tyrosylprotein sulfotransferase 2) (TPST-2) 376 42,067 Active site (1); Binding site (5); Chain (1); Disulfide bond (2); Glycosylation (2); Region (3); Sequence conflict (1); Site (2); Topological domain (2); Transmembrane (1) TRANSMEM 9 25 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 8 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 26 376 Lumenal. {ECO:0000255}. FUNCTION: Catalyzes the O-sulfation of tyrosine residues within acidic motifs of polypeptides, using 3'-phosphoadenylyl sulfate (PAPS) as cosubstrate. {ECO:0000269|PubMed:9733778}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:O60704}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:O60704}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:O60704}. SUBUNIT: Homodimer. Can also form heterodimers with TPST1. {ECO:0000250|UniProtKB:O60704}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9733778}. +Q9CQM5 TXD17_MOUSE Thioredoxin domain-containing protein 17 (14 kDa thioredoxin-related protein) (TRP14) (Protein 42-9-9) (Thioredoxin-like protein 5) 123 14,015 Active site (2); Beta strand (5); Chain (1); Disulfide bond (1); Domain (1); Helix (6); Initiator methionine (1); Modified residue (1); Sequence conflict (4); Site (2) FUNCTION: Disulfide reductase. May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions. Modulates TNF-alpha signaling and NF-kappa-B activation. Has peroxidase activity and may contribute to the elimination of cellular hydrogen peroxide (By similarity). {ECO:0000250}. PTM: The oxidized protein is reduced by TRXR1. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with TRXR1 and DYNLL1/DNCL1. {ECO:0000250}. +P11344 TYRO_MOUSE Tyrosinase (EC 1.14.18.1) (Albino locus protein) (Monophenol monooxygenase) 533 60,606 Chain (1); Compositional bias (1); Glycosylation (6); Metal binding (6); Natural variant (3); Sequence caution (1); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 477 497 Helical. {ECO:0000255}. TOPO_DOM 19 476 Lumenal, melanosome. {ECO:0000255}.; TOPO_DOM 498 533 Cytoplasmic. {ECO:0000255}. FUNCTION: This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. Catalyzes the initial and rate limiting step in the cascade of reactions leading to melanin production from tyrosine. In addition to hydroxylating tyrosine to DOPA (3,4-dihydroxyphenylalanine), also catalyzes the oxidation of DOPA to DOPA-quinone, and possibly the oxidation of DHI (5,6-dihydroxyindole) to indole-5,6 quinone (PubMed:2494997, PubMed:2517217, PubMed:1537333). {ECO:0000269|PubMed:1537333, ECO:0000269|PubMed:2494997, ECO:0000269|PubMed:2517217}. PTM: Glycosylated. {ECO:0000269|PubMed:1537333}. SUBCELLULAR LOCATION: Melanosome membrane {ECO:0000250|UniProtKB:P14679}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P14679}. Melanosome {ECO:0000269|PubMed:26620560}. Note=Proper trafficking to melanosome is regulated by SGSM2, ANKRD27, RAB9A, RAB32 and RAB38. {ECO:0000269|PubMed:26620560}. DISEASE: Note=Defects in Tyr result in various forms of albinism. Himalayan strain tyrosinase is temperature-sensitive. {ECO:0000269|PubMed:2110899, ECO:0000269|PubMed:2118105, ECO:0000269|PubMed:2507645, ECO:0000269|PubMed:2567165}. +P62077 TIM8B_MOUSE Mitochondrial import inner membrane translocase subunit Tim8 B (Deafness dystonia protein 2 homolog) 83 9,286 Chain (1); Disulfide bond (2); Initiator methionine (1); Modified residue (1); Motif (1) FUNCTION: Probable mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Intermembrane side {ECO:0000250}. SUBUNIT: Heterohexamer; possibly composed of 3 copies of TIMM8B and 3 copies of TIMM13, named soluble 70 kDa complex. Associates with the TIM22 complex, whose core is composed of TIMM22 (By similarity). {ECO:0000250}. DOMAIN: The twin CX3C motif contains 4 conserved Cys residues that form 2 disulfide bonds in the mitochondrial intermembrane space. However, during the transit of TIMM8B from cytoplasm into mitochondrion, the Cys residues probably coordinate zinc, thereby preventing folding and allowing its transfer across mitochondrial outer membrane (By similarity). {ECO:0000250}. +P12032 TIMP1_MOUSE Metalloproteinase inhibitor 1 (Collagenase inhibitor 16C8 fibroblast) (Erythroid-potentiating activity) (EPA) (TPA-S1) (TPA-induced protein) (Tissue inhibitor of metalloproteinases 1) (TIMP-1) 205 22,628 Chain (1); Disulfide bond (6); Domain (1); Glycosylation (2); Metal binding (1); Modified residue (1); Region (2); Sequence conflict (8); Signal peptide (1); Site (1) FUNCTION: Metalloproteinase inhibitor that functions by forming one to one complexes with target metalloproteinases, such as collagenases, and irreversibly inactivates them by binding to their catalytic zinc cofactor. Acts on MMP1, MMP2, MMP3, MMP7, MMP8, MMP9, MMP10, MMP11, MMP12, MMP13 and MMP16. Does not act on MMP14 (By similarity). Also functions as a growth factor that regulates cell differentiation, migration and cell death and activates cellular signaling cascades via CD63 and ITGB1. Plays a role in integrin signaling. {ECO:0000250, ECO:0000269|PubMed:23522389}. PTM: The activity of TIMP1 is dependent on the presence of disulfide bonds. {ECO:0000250}.; PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23522389}. SUBUNIT: Interacts with MMP1, MMP3, MMP10 and MMP13, but has only very low affinity for MMP14 (By similarity). Interacts with CD63; identified in a complex with CD63 and ITGB1. {ECO:0000250, ECO:0000269|PubMed:23522389}. TISSUE SPECIFICITY: Found in fetal and adult tissues. Highest levels are found in bone. Also found in lung, ovary and uterus. +Q8BKV0 TICN3_MOUSE Testican-3 (SPARC/osteonectin, CWCV, and Kazal-like domains proteoglycan 3) 436 49,098 Alternative sequence (1); Chain (1); Compositional bias (1); Disulfide bond (8); Domain (2); Glycosylation (2); Signal peptide (1) FUNCTION: May participate in diverse steps of neurogenesis. Inhibits the processing of pro-matrix metalloproteinase 2 (MMP-2) by MT1-MMP and MT3-MMP. May interfere with tumor invasion (By similarity). {ECO:0000250}. PTM: Contains chondroitin sulfate and heparan sulfate O-linked oligosaccharides. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain. +Q8BH58 TIPRL_MOUSE TIP41-like protein 271 31,254 Beta strand (13); Chain (1); Helix (7); Modified residue (3); Region (1); Turn (1) FUNCTION: May be a allosteric regulator of serine/threonine-protein phosphatase 2A (PP2A). Inhibits catalytic activity of the PP2A(D) core complex in vitro. The PP2A(C):TIPRL complex does not show phosphatase activity. Acts as negative regulator of serine/threonine-protein phosphatase 4 probably by inhibiting the formation of the active PPP4C:PPP4R2 complex; the function is proposed to implicate it in DNA damage response by promoting H2AFX phosphorylated on Ser-140 (gamma-H2AFX). May play a role in the regulation of ATM/ATR signaling pathway controlling DNA replication and repair (By similarity). {ECO:0000250|UniProtKB:O75663}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O75663}. SUBUNIT: Interacts with PPP2CA. Interacts with PPP2CB, PPP4C and PPP6C. Interacts with IGBP1; the interaction is dependent on PPP2CA. Associates with a protein phosphatase 2A PP2A(C):IGBP1 complex (By similarity). Interacts with PPP4C and PPP4R2 (PubMed:26717153). {ECO:0000250|UniProtKB:O75663, ECO:0000269|PubMed:26717153}. +Q9WV98 TIM9_MOUSE Mitochondrial import inner membrane translocase subunit Tim9 89 10,344 Chain (1); Disulfide bond (2); Initiator methionine (1); Modified residue (1); Motif (1) FUNCTION: Mitochondrial intermembrane chaperone that participates in the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. May also be required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Intermembrane side {ECO:0000250}. SUBUNIT: Heterohexamer; composed of 3 copies of TIMM9 and 3 copies of TIMM10/TIM10A, named soluble 70 kDa complex. The complex forms a 6-bladed alpha-propeller structure and associates with the TIMM22 component of the TIM22 complex. Interacts with multi-pass transmembrane proteins in transit. Also forms a complex composed of TIMM9, TIMM10/TIM10A and FXC1/TIM10B (By similarity). {ECO:0000250}. DOMAIN: The twin CX3C motif contains 4 conserved Cys residues that form 2 disulfide bonds in the mitochondrial intermembrane space. However, during the transit of TIMM9 from cytoplasm into mitochondrion, the Cys residues probably coordinate zinc, thereby preventing folding and allowing its transfer across mitochondrial outer membrane (By similarity). {ECO:0000250}. +Q99KW9 TIP_MOUSE T-cell immunomodulatory protein (Protein TIP) (Integrin-alpha FG-GAP repeat-containing protein 1) (Linkin) 610 67,465 Chain (1); Glycosylation (10); Repeat (3); Sequence conflict (2); Signal peptide (1); Transmembrane (1) TRANSMEM 565 585 Helical. {ECO:0000255}. FUNCTION: Modulator of T-cell function. Has a protective effect in graft versus host disease model. {ECO:0000269|PubMed:12598909}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Interacts with RUVBL1, RUVBL2 and alpha-tubulin. {ECO:0000250|UniProtKB:Q8TB96}. +Q56A06 TMTC2_MOUSE Protein O-mannosyl-transferase TMTC2 (EC 2.4.1.109) (Transmembrane and TPR repeat-containing protein 2) 836 94,176 Alternative sequence (2); Chain (1); Glycosylation (1); Repeat (10); Transmembrane (11) TRANSMEM 1 21 Helical. {ECO:0000255}.; TRANSMEM 78 98 Helical. {ECO:0000255}.; TRANSMEM 108 128 Helical. {ECO:0000255}.; TRANSMEM 133 153 Helical. {ECO:0000255}.; TRANSMEM 169 183 Helical. {ECO:0000255}.; TRANSMEM 184 204 Helical. {ECO:0000255}.; TRANSMEM 222 241 Helical. {ECO:0000255}.; TRANSMEM 313 333 Helical. {ECO:0000255}.; TRANSMEM 400 420 Helical. {ECO:0000255}.; TRANSMEM 423 443 Helical. {ECO:0000255}.; TRANSMEM 450 470 Helical. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Transfers mannosyl residues to the hydroxyl group of serine or threonine residues. The 4 members of the TMTC family are O-mannosyl-transferases dedicated primarily to the cadherin superfamily, each member seems to have a distinct role in decorating the cadherin domains with O-linked mannose glycans at specific regions. Also acts as O-mannosyl-transferase on other proteins such as PDIA3. {ECO:0000250|UniProtKB:Q8N394}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q8N394}. +Q8K1T0 TMPS3_MOUSE Transmembrane protease serine 3 (EC 3.4.21.-) 453 49,506 Active site (3); Alternative sequence (1); Chain (1); Disulfide bond (10); Domain (3); Glycosylation (1); Sequence conflict (2); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 49 69 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 48 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 70 453 Extracellular. {ECO:0000255}. FUNCTION: Probable serine protease that plays a role in hearing. Acts as a permissive factor for cochlear hair cell survival and activation at the onset of hearing and is required for saccular hair cell survival. Activates ENaC (in vitro). {ECO:0000269|PubMed:12393794, ECO:0000269|PubMed:21454591}. PTM: Undergoes autoproteolytic activation. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12393794, ECO:0000269|PubMed:21454591}; Single-pass type II membrane protein {ECO:0000269|PubMed:12393794, ECO:0000269|PubMed:21454591}. TISSUE SPECIFICITY: Strongly expressed in liver, cochlea, brain, cerebellum, spleen, lung, and muscle and at a lower degree in retina, kidney, and heart. Expressed in the spiral ganglion, the cells supporting the organ of Corti and the stria vascularis. Isoform 2 is strongly expressed only in the cochlea with very faint expression in the cerebellum, spleen and muscle. {ECO:0000269|PubMed:21454591}. +Q9CR67 TMM33_MOUSE Transmembrane protein 33 (Protein DB83) 247 28,031 Chain (1); Initiator methionine (1); Modified residue (1); Sequence conflict (2); Topological domain (4); Transmembrane (3) TRANSMEM 32 52 Helical. {ECO:0000255}.; TRANSMEM 101 121 Helical. {ECO:0000255}.; TRANSMEM 156 176 Helical. {ECO:0000255}. TOPO_DOM 2 31 Lumenal. {ECO:0000305}.; TOPO_DOM 53 100 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 122 155 Lumenal. {ECO:0000305}.; TOPO_DOM 177 247 Cytoplasmic. {ECO:0000305}. FUNCTION: Acts as a regulator of the tubular endoplasmic reticulum (ER) network. Suppresses the RTN3/4-induced formation of the ER tubules. Positively regulates PERK-mediated and IRE1-mediated unfolded protein response signaling. {ECO:0000250|UniProtKB:P57088}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P57088}; Multi-pass membrane protein {ECO:0000255}. Melanosome {ECO:0000250|UniProtKB:P57088}. Nucleus envelope {ECO:0000250|UniProtKB:P57088}. Note=Co-localizes with RTN4 at the ER sheets. {ECO:0000250|UniProtKB:P57088}. SUBUNIT: Interacts with EIF2AK3. Interacts with RTN1, RTN2, RTN3, RTN4 and ARL6IP1. {ECO:0000250|UniProtKB:P57088}. +Q9D7L8 TMIG1_MOUSE Transmembrane and immunoglobulin domain-containing protein 1 261 29,051 Chain (1); Disulfide bond (2); Domain (2); Glycosylation (6); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 216 236 Helical. {ECO:0000255}. TOPO_DOM 27 215 Extracellular. {ECO:0000255}.; TOPO_DOM 237 261 Cytoplasmic. {ECO:0000255}. FUNCTION: May control cell-cell adhesion, cell migration and proliferation, cell morphology, and protects renal epithelial cells from oxidative cell injury to promote cell survival. {ECO:0000250|UniProtKB:Q6UXZ0}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q6UXZ0}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6UXZ0}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q6UXZ0}. Cytoplasm {ECO:0000250|UniProtKB:Q6UXZ0}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q6UXZ0}. +O35235 TNF11_MOUSE Tumor necrosis factor ligand superfamily member 11 (Osteoclast differentiation factor) (ODF) (Osteoprotegerin ligand) (OPGL) (Receptor activator of nuclear factor kappa-B ligand) (RANKL) (TNF-related activation-induced cytokine) (TRANCE) (CD antigen CD254) [Cleaved into: Tumor necrosis factor ligand superfamily member 11, membrane form; Tumor necrosis factor ligand superfamily member 11, soluble form] 316 35,003 Alternative sequence (2); Beta strand (12); Chain (2); Glycosylation (2); Helix (3); Sequence conflict (7); Site (1); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 49 69 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 48 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 70 316 Extracellular. {ECO:0000255}. FUNCTION: Cytokine that binds to TNFRSF11B/OPG and to TNFRSF11A/RANK. Osteoclast differentiation and activation factor. Augments the ability of dendritic cells to stimulate naive T-cell proliferation. May be an important regulator of interactions between T-cells and dendritic cells and may play a role in the regulation of the T-cell-dependent immune response. May also play an important role in enhanced bone-resorption in humoral hypercalcemia of malignancy (By similarity). Induces osteoclastogenesis by activating multiple signaling pathways in osteoclast precursor cells, chief among which is induction of long lasting oscillations in the intracellular concentration of Ca (2+) resulting in the activation of NFATC1, which translocates to the nucleus and induces osteoclast-specific gene transcription to allow differentiation of osteoclasts (PubMed:24039232). During osteoclast differentiation, in a TMEM64 and ATP2A2-dependent manner induces activation of CREB1 and mitochondrial ROS generation necessary for proper osteoclast generation (PubMed:23395171, PubMed:26644563). {ECO:0000250|UniProtKB:O14788, ECO:0000269|PubMed:23395171, ECO:0000269|PubMed:24039232, ECO:0000269|PubMed:26644563}. PTM: N-glycosylated. {ECO:0000269|PubMed:10224132}.; PTM: The soluble form of isoform 1 derives from the membrane form by proteolytic processing. The cleavage may be catalyzed by ADAM17. A further shorter soluble form was observed. {ECO:0000269|PubMed:10224132}. SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type II membrane protein.; SUBCELLULAR LOCATION: Isoform 2: Cell membrane; Single-pass type II membrane protein.; SUBCELLULAR LOCATION: Isoform 3: Cytoplasm.; SUBCELLULAR LOCATION: Tumor necrosis factor ligand superfamily member 11, soluble form: Secreted. SUBUNIT: Homotrimer (PubMed:11581298, PubMed:11733492, PubMed:20483727). Interacts with TNFRSF11A and TNFRSF11B (PubMed:20483727, PubMed:23039992). Interacts with FBN1 (via N-terminal domain) in a Ca(+2)-dependent manner (PubMed:24039232). {ECO:0000269|PubMed:11581298, ECO:0000269|PubMed:11733492, ECO:0000269|PubMed:20483727, ECO:0000269|PubMed:23039992, ECO:0000269|PubMed:24039232}. TISSUE SPECIFICITY: Highly expressed in thymus and lymph nodes, but not in non-lymphoid tissues and is abundantly expressed in T-cells but not in B-cells. A high level expression is also seen in the trabecular bone and lung. DISEASE: Note=Deficiency in Tnfsf11 results in failure to form lobulo-alveolar mammary structures during pregnancy, resulting in death of newborns. Trance-deficient mice show severe osteopetrosis, with no osteoclasts, marrow spaces, or tooth eruption, and exhibit profound growth retardation at several skeletal sites, including the limbs, skull, and vertebrae and have marked chondrodysplasia, with thick, irregular growth plates and a relative increase in hypertrophic chondrocytes. +P43488 TNFL4_MOUSE Tumor necrosis factor ligand superfamily member 4 (OX40 ligand) (OX40L) (CD antigen CD252) 198 22,255 Beta strand (11); Chain (1); Disulfide bond (2); Glycosylation (1); Helix (1); Topological domain (2); Transmembrane (1) TRANSMEM 29 50 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 28 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 51 198 Extracellular. {ECO:0000255}. FUNCTION: Cytokine that binds to TNFRSF4. Co-stimulates T-cell proliferation and cytokine production. SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. SUBUNIT: Homotrimer. {ECO:0000269|PubMed:16905106}. +Q99LG1 TMM51_MOUSE Transmembrane protein 51 249 27,398 Chain (1); Modified residue (4); Transmembrane (2) TRANSMEM 17 37 Helical. {ECO:0000255}.; TRANSMEM 64 84 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9JJR8 TMM9B_MOUSE Transmembrane protein 9B 199 22,607 Chain (1); Glycosylation (1); Modified residue (2); Signal peptide (1); Transmembrane (1) TRANSMEM 106 126 Helical. {ECO:0000255}. FUNCTION: Enhances production of proinflammatory cytokines induced by TNF, IL1B, and TLR ligands. Has a role in TNF activation of both the NF-kappaB and MAPK pathways. {ECO:0000250|UniProtKB:Q9NQ34}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9NQ34}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q9NQ34}; Single-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:Q9NQ34}; Single-pass membrane protein {ECO:0000255}. +Q9ER41 TOR1B_MOUSE Torsin-1B (Torsin ATPase-1B) (EC 3.6.4.-) (Torsin family 1 member B) 336 37,818 Chain (1); Glycosylation (2); Nucleotide binding (1); Sequence conflict (2); Signal peptide (1) FUNCTION: May serve as a molecular chaperone assisting in the proper folding of secreted and/or membrane proteins. Plays a role in non-neural cells nuclear envelope and endoplasmic reticulum integrity. May have a redundant function with TOR1A in non-neural tissues. {ECO:0000269|PubMed:20457914}. PTM: N-glycosylated. {ECO:0000269|PubMed:20015956}. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Nucleus membrane. SUBUNIT: Homohexamer. Interacts with TOR1A; the interaction may be specific of neural tissues. Interacts with TOR1AIP1; TOR1AIP1 is required for TOR1B location on the nuclear membrane. Interacts (ATP-bound) with TOR1AIP2; important for endoplasmic reticulum integrity. {ECO:0000269|PubMed:20457914}. TISSUE SPECIFICITY: Highly expressed in liver and muscle; lower expression levels are observed in brain (at protein level). {ECO:0000269|PubMed:20015956}. +P17532 TPH1_MOUSE Tryptophan 5-hydroxylase 1 (EC 1.14.16.4) (Tryptophan 5-monooxygenase 1) 447 51,343 Binding site (5); Chain (1); Domain (1); Metal binding (3); Modified residue (1) Aromatic compound metabolism; serotonin biosynthesis; serotonin from L-tryptophan: step 1/2. SUBUNIT: Homotetramer. +B2RXC1 TPC11_MOUSE Trafficking protein particle complex subunit 11 1133 128,396 Alternative sequence (3); Chain (1); Modified residue (1) FUNCTION: Involved in endoplasmic reticulum to Golgi apparatus trafficking at a very early stage. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:Q7Z392}. Golgi apparatus, cis-Golgi network {ECO:0000250}. SUBUNIT: Component of the multisubunit TRAPP (transport protein particle) complex, which includes at least TRAPPC2, TRAPPC2L, TRAPPC3, TRAPPC3L, TRAPPC4, TRAPPC5, TRAPPC8, TRAPPC9, TRAPPC10, TRAPPC11 and TRAPPC12. {ECO:0000250}. +Q8K2L8 TPC12_MOUSE Trafficking protein particle complex subunit 12 (Tetratricopeptide repeat protein 15) (TPR repeat protein 15) 797 87,694 Chain (1); Erroneous initiation (1); Modified residue (6); Repeat (4); Sequence conflict (3) FUNCTION: Component of the TRAPP complex, which is involved in endoplasmic reticulum to Golgi apparatus trafficking at a very early stage. Also plays a role in chromosome congression, kinetochore assembly and stability and controls the recruitment of CENPE to the kinetochores. {ECO:0000250|UniProtKB:Q8WVT3}. PTM: Phosphorylated as the cells enter mitosis but is dephosphorylated at or before the onset of anaphase. The phosphorylated form recruits CENPE to kinetochores more efficiently than the non-phosphorylated form. {ECO:0000250|UniProtKB:Q8WVT3}. SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250|UniProtKB:Q8WVT3}. Nucleus {ECO:0000250|UniProtKB:Q8WVT3}. Note=Mainly localizes to structures resembling the Golgi and a small amount is found in the nucleus. {ECO:0000250|UniProtKB:Q8WVT3}. SUBUNIT: Component of the multisubunit TRAPP (transport protein particle) complex, which includes at least TRAPPC2, TRAPPC2L, TRAPPC3, TRAPPC3L, TRAPPC4, TRAPPC5, TRAPPC8, TRAPPC9, TRAPPC10, TRAPPC11 and TRAPPC12. Interacts with CENPE. {ECO:0000250|UniProtKB:Q8WVT3}. +Q3TIR1 TPC13_MOUSE Trafficking protein particle complex subunit 13 417 46,477 Alternative sequence (2); Chain (1); Erroneous initiation (3); Sequence conflict (3) SUBUNIT: Part of the multisubunit TRAPP (transport protein particle) complex. {ECO:0000250}. +Q5NCF2 TPPC1_MOUSE Trafficking protein particle complex subunit 1 145 16,882 Beta strand (5); Chain (1); Helix (4); Turn (1) FUNCTION: May play a role in vesicular transport from endoplasmic reticulum to Golgi. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. SUBUNIT: Part of the multisubunit transport protein particle (TRAPP) complex. The heterodimer TRAPPC6B-TRAPPC3 interacts with TRAPPC1 likely providing a core for TRAPP complex formation. {ECO:0000250|UniProtKB:Q9Y5R8}. +O55013 TPPC3_MOUSE Trafficking protein particle complex subunit 3 (BET3 homolog) 180 20,302 Beta strand (5); Chain (1); Helix (8); Lipidation (1); Turn (3) FUNCTION: May play a role in vesicular transport from endoplasmic reticulum to Golgi. SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. SUBUNIT: Homodimer. Component of the multisubunit transport protein particle (TRAPP) complex, which includes at least TRAPPC2, TRAPPC2L, TRAPPC3, TRAPPC3L, TRAPPC4, TRAPPC5, TRAPPC8, TRAPPC9, TRAPPC10, TRAPPC11 and TRAPPC12. Heterodimer with TRAPPC6A. The heterodimer TRAPPC3-TRAPPC6A interacts with TRAPPC2L. Heterodimer with TRAPPC6b. The heterodimer TRAPPC6B-TRAPPC3 interacts with TRAPPC1 likely providing a core for TRAPP complex formation. {ECO:0000250|UniProtKB:O43617}. TISSUE SPECIFICITY: Widely expressed. Expressed in lung, heart, liver, spleen, brain and kidney. {ECO:0000269|PubMed:16828797}. +P17751 TPIS_MOUSE Triosephosphate isomerase (TIM) (EC 5.3.1.1) (Methylglyoxal synthase) (EC 4.2.3.3) (Triose-phosphate isomerase) 299 32,192 Active site (2); Binding site (2); Chain (1); Cross-link (1); Erroneous initiation (11); Modified residue (17); Mutagenesis (2); Sequence conflict (8) Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate from glycerone phosphate: step 1/1. Carbohydrate biosynthesis; gluconeogenesis. FUNCTION: Triosephosphate isomerase is an extremely efficient metabolic enzyme that catalyzes the interconversion between dihydroxyacetone phosphate (DHAP) and D-glyceraldehyde-3-phosphate (G3P) in glycolysis and gluconeogenesis. {ECO:0000250|UniProtKB:P00939}.; FUNCTION: It is also responsible for the non-negligible production of methylglyoxal a reactive cytotoxic side-product that modifies and can alter proteins, DNA and lipids. {ECO:0000250|UniProtKB:P00939}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU10127}. SUBUNIT: Homodimer. {ECO:0000255|PROSITE-ProRule:PRU10127}. +Q8BHN1 TXLNG_MOUSE Gamma-taxilin (Factor inhibiting ATF4-mediated transcription) (FIAT) (Lipopolysaccharide-responsive gene protein) 524 60,309 Alternative sequence (3); Chain (1); Coiled coil (1); Erroneous termination (2); Frameshift (2); Modified residue (7); Sequence conflict (7) FUNCTION: May be involved in intracellular vesicle traffic (By similarity). Inhibits ATF4-mediated transcription, possibly by dimerizing with ATF4 to form inactive dimers that cannot bind DNA. May be involved in regulating bone mass density through an ATF4-dependent pathway. May be involved in cell cycle progression. {ECO:0000250, ECO:0000269|PubMed:15911876, ECO:0000269|PubMed:19016261, ECO:0000269|PubMed:19913514}. SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:19913514}. Cytoplasm, cytosol {ECO:0000269|PubMed:19913514}. SUBUNIT: Binds to the C-terminal coiled coil region of syntaxin family members STX1A, STX3A and STX4A (By similarity). Forms a heterodimer with ATF4 in osteoblasts. {ECO:0000250, ECO:0000269|PubMed:15911876}. +Q9CQ79 TXND9_MOUSE Thioredoxin domain-containing protein 9 (ATP-binding protein associated with cell differentiation) 226 26,260 Chain (1); Domain (1); Modified residue (3) FUNCTION: Significantly diminishes the chaperonin TCP1 complex ATPase activity, thus negatively impacts protein folding, including that of actin or tubulin. {ECO:0000250|UniProtKB:O14530}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15009089}. Nucleus {ECO:0000269|PubMed:15009089}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:15009089}. Midbody {ECO:0000269|PubMed:15009089}. Note=Co-localizes with beta-tubulin in the centrosome. {ECO:0000269|PubMed:15009089}. SUBUNIT: Forms ternary complexes with the chaperonin TCP1 complex, spanning the cylindrical chaperonin cavity and contacting at least 2 subunits. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in testis, liver, heart, kidney, brain, spleen and lung. {ECO:0000269|PubMed:15009089}. +P0CG50 UBC_MOUSE Polyubiquitin-C [Cleaved into: Ubiquitin; Ubiquitin-related 1; Ubiquitin-related 2] 734 82,550 Beta strand (6); Binding site (2); Chain (10); Cross-link (8); Domain (9); Helix (3); Modified residue (3); Sequence conflict (3); Site (1) FUNCTION: Ubiquitin: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling. {ECO:0000269|PubMed:19754430}. PTM: Ubiquitin: Phosphorylated at Ser-65 by PINK1 during mitophagy. Phosphorylated ubiquitin specifically binds and activates parkin (PRKN), triggering mitophagy. Phosphorylation does not affect E1-mediated E2 charging of ubiquitin but affects discharging of E2 enzymes to form polyubiquitin chains. It also affects deubiquitination by deubiquitinase enzymes such as USP30. {ECO:0000250|UniProtKB:P0CG48}.; PTM: Ubiquitin: Mono-ADP-ribosylated at the C-terminus by PARP9, a component of the PPAR9-DTX3L complex. ADP-ribosylation requires processing by E1 and E2 enzymes and prevents ubiquitin conjugation to substrates such as histones. {ECO:0000250|UniProtKB:P0CG48}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. +Q8C878 UBA3_MOUSE NEDD8-activating enzyme E1 catalytic subunit (EC 6.2.1.-) (NEDD8-activating enzyme E1C) (Ubiquitin-activating enzyme E1C) (Ubiquitin-like modifier-activating enzyme 3) (Ubiquitin-activating enzyme 3) 462 51,737 Active site (1); Alternative sequence (1); Chain (1); Initiator methionine (1); Modified residue (1); Nucleotide binding (2); Region (9); Sequence conflict (3); Site (1) Protein modification; protein neddylation. FUNCTION: Catalytic subunit of the dimeric UBA3-NAE1 E1 enzyme. E1 activates NEDD8 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-UBA3 thioester and free AMP. E1 finally transfers NEDD8 to the catalytic cysteine of UBE2M. Down-regulates steroid receptor activity. Necessary for cell cycle progression. {ECO:0000269|PubMed:11696557}. SUBUNIT: Heterodimer of UBA3 and NAE1. Interacts with NEDD8, UBE2F and UBE2M. Binds ESR1 and ESR2 with bound steroid ligand (By similarity). Interacts with TBATA. {ECO:0000250, ECO:0000269|PubMed:20937703}. DISEASE: Note=Defects in Uba3 are a cause of embryonic lethality. Mouse embryos deficient in Uba3 die at the preimplantation stage (PubMed:11696557). {ECO:0000269|PubMed:11696557}. +Q9DC60 UBIA1_MOUSE UbiA prenyltransferase domain-containing protein 1 (EC 2.5.1.-) 336 36,684 Chain (1); Initiator methionine (1); Modified residue (1); Sequence conflict (3); Transmembrane (8) TRANSMEM 81 101 Helical. {ECO:0000255}.; TRANSMEM 132 152 Helical. {ECO:0000255}.; TRANSMEM 158 178 Helical. {ECO:0000255}.; TRANSMEM 186 206 Helical. {ECO:0000255}.; TRANSMEM 207 227 Helical. {ECO:0000255}.; TRANSMEM 243 265 Helical. {ECO:0000255}.; TRANSMEM 275 295 Helical. {ECO:0000255}.; TRANSMEM 313 333 Helical. {ECO:0000255}. Quinol/quinone metabolism; menaquinone biosynthesis. Cofactor biosynthesis; ubiquinone biosynthesis. FUNCTION: Prenyltransferase that mediates the formation of menaquinone-4 (MK-4) and coenzyme Q10. MK-4 is a vitamin K2 isoform required for endothelial cell development. Mediates the conversion of phylloquinone (PK) into MK-4, probably by cleaving the side chain of phylloquinone (PK) to release 2-methyl-1,4-naphthoquinone (menadione; K3) and then prenylating it with geranylgeranyl pyrophosphate (GGPP) to form MK-4. Also plays a role in cardiovascular development independently of MK-4 biosynthesis, by acting as a coenzyme Q10 biosynthetic enzyme: coenzyme Q10, also named ubiquinone, plays a important antioxidant role in the cardiovascular system. Mediates biosynthesis of coenzyme Q10 in the Golgi membrane, leading to protect cardiovascular tissues from NOS3/eNOS-dependent oxidative stress (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Mitochondrion {ECO:0000250}. SUBUNIT: Interacts with HMGCR and SOAT1. {ECO:0000250}. +Q9CY34 UB2FA_MOUSE NEDD8-conjugating enzyme UBE2F (EC 2.3.2.-) (NEDD8 carrier protein UBE2F) (NEDD8 protein ligase UBE2F) (NEDD8-conjugating enzyme 2) (RING-type E3 NEDD8 transferase UBE2F) (Ubiquitin-conjugating enzyme E2 F) 185 21,110 Active site (1); Chain (1); Modified residue (1); Region (1); Sequence conflict (2) Protein modification; protein neddylation. FUNCTION: Accepts the ubiquitin-like protein NEDD8 from the UBA3-NAE1 E1 complex and catalyzes its covalent attachment to other proteins. The specific interaction with the E3 ubiquitin ligase RBX2, but not RBX1, suggests that the RBX2-UBE2F complex neddylates specific target proteins, such as CUL5. {ECO:0000269|PubMed:19250909}. PTM: The acetylation of Met-1 increases affinity for DCUN1D3 by about 2 orders of magnitude and is crucial for NEDD8 transfer to cullins. {ECO:0000250}. SUBUNIT: Interacts with UBA3 and RBX2. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed (at protein level). {ECO:0000269|PubMed:19250909}. +O08759 UBE3A_MOUSE Ubiquitin-protein ligase E3A (EC 2.3.2.26) (HECT-type ubiquitin transferase E3A) (Oncogenic protein-associated protein E6-AP) 870 99,819 Active site (1); Alternative sequence (2); Chain (1); Compositional bias (1); Domain (1); Frameshift (1); Modified residue (3); Mutagenesis (1); Sequence conflict (13); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and transfers it to its substrates. Several substrates have been identified including the ARNTL/BMAL1, ARC, RAD23A and RAD23B, MCM7 (which is involved in DNA replication), annexin A1, the PML tumor suppressor, and the cell cycle regulator CDKN1B (PubMed:20211139, PubMed:24728990). Additionally, may function as a cellular quality control ubiquitin ligase by helping the degradation of the cytoplasmic misfolded proteins. Finally, UBE3A also promotes its own degradation in vivo (By similarity). Plays an important role in the regulation of the circadian clock: involved in the ubiquitination of the core clock component ARNTL/BMAL1, leading to its proteasomal degradation (PubMed:24728990). Acts as a regulator of synaptic development by mediating ubiquitination and degradation of ARC (PubMed:20211139). Synergizes with WBP2 in enhancing PGR activity (By similarity). {ECO:0000250|UniProtKB:Q05086, ECO:0000269|PubMed:20211139, ECO:0000269|PubMed:24728990}. PTM: Phosphorylation at Tyr-654 by ABL1 impairs E3 ligase activity. {ECO:0000250|UniProtKB:Q05086}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9182527}. Nucleus {ECO:0000269|PubMed:9182527}. SUBUNIT: The active form is probably a homotrimer. Binds UBQLN1 and UBQLN2. Interacts with the 26S proteasome. Interacts with BPY2. Interacts with HIF1AN, MAPK6 AND NEURL4; interaction with MAPK6 may be mediated by NEURL4. Interacts with the proteasomal subunit PSMD4. Interacts with ARNTL/BMAL1 (PubMed:24728990). Interacts with ARC (PubMed:20211139). Interacts with ESR1 and WBP2 (By similarity). {ECO:0000250|UniProtKB:Q05086, ECO:0000269|PubMed:20211139, ECO:0000269|PubMed:24728990}. TISSUE SPECIFICITY: Widely expressed. Most abundant in brain, heart and thymus. {ECO:0000269|PubMed:24728990, ECO:0000269|PubMed:9110176}. +Q9CR39 WIPI3_MOUSE WD repeat domain phosphoinositide-interacting protein 3 (WIPI-3) (WD repeat-containing protein 45-like) (WDR45-like protein) (WD repeat-containing protein 45B) 344 38,021 Chain (1); Repeat (2); Sequence conflict (1) FUNCTION: Component of the autophagy machinery that controls the major intracellular degradation process by which cytoplasmic materials are packaged into autophagosomes and delivered to lysosomes for degradation. Binds phosphatidylinositol 3-phosphate (PtdIns3P) forming on membranes of the endoplasmic reticulum upon activation of the upstream ULK1 and PI3 kinases and is recruited at phagophore assembly sites where it regulates the elongation of nascent phagophores downstream of WIPI2. In the cellular response to starvation, may also function together with the TSC1-TSC2 complex and RB1CC1 in the inhibition of the mTORC1 signaling pathway. {ECO:0000250|UniProtKB:Q5MNZ6}. SUBCELLULAR LOCATION: Preautophagosomal structure {ECO:0000250|UniProtKB:Q5MNZ6}. Lysosome {ECO:0000250|UniProtKB:Q5MNZ6}. SUBUNIT: Interacts with the TSC1-TSC2 complex; stimulated upon starvation. Interacts with RB1CC1. {ECO:0000269|PubMed:28561066}. +O54775 WISP1_MOUSE WNT1-inducible-signaling pathway protein 1 (WISP-1) (CCN family member 4) (ELM-1) 367 40,703 Chain (1); Disulfide bond (5); Domain (4); Glycosylation (4); Sequence conflict (4); Signal peptide (1) FUNCTION: Downstream regulator in the Wnt/Frizzled-signaling pathway (By similarity). Associated with cell survival. Adheres to skin and melanoma fibroblasts (By similarity). In vitro binding to skin fibroblasts occurs through the proteoglycans, decorin and biglycan (By similarity). Suppresses tumor growth in vivo. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in kidney and lung. Lower levels in heart, brain, spleen, liver, skeletal muscle and testis. Expressed in low metastatic melanoma cells. +Q793I8 TIFA_MOUSE TRAF-interacting protein with FHA domain-containing protein A (TRAF2-binding protein) 184 21,560 Chain (1); Domain (1); Modified residue (1); Sequence conflict (1) FUNCTION: Adapter molecule that plays a key role in the activation of proinflammatory NF-kappa-B signaling following detection of bacterial pathogen-associated molecular pattern metabolites (PAMPs) (PubMed:11798190). Promotes activation of an innate immune response by inducing the oligomerization and polyubiquitination of TRAF6, which leads to the activation of TAK1 and IKK through a proteasome-independent mechanism (By similarity). TIFA-dependent innate immune response is triggered by ADP-D-glycero-beta-D-manno-heptose (ADP-Heptose), a potent PAMP present in all Gram-negative and some Gram-positive bacteria: ADP-Heptose is recognized by ALPK1, which phosphorylates TIFA at Thr-9, leading to TIFA homooligomerization and subsequent activation of proinflammatory NF-kappa-B signaling (By similarity). {ECO:0000250|UniProtKB:Q96CG3, ECO:0000269|PubMed:11798190}. PTM: Phosphorylated at Thr-9 following detection of ADP-D-glycero-beta-D-manno-heptose (ADP-Heptose) by ALPK1. Phosphorylation at Thr-9 by ALPK1 leads to the formation of an intermolecular binding between the FHA domain and phosphorylated Thr-9, promoting TIFA oligomerization and TIFA-mediated NF-kappa-B activation. {ECO:0000250|UniProtKB:Q96CG3}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96CG3}. Note=Colocalizes with lysosomal marker LAMP2 following homooligomerization and subsequent activation. {ECO:0000250|UniProtKB:Q96CG3}. SUBUNIT: Homooligomer; homooligomerizes following phosphorylation at Thr-9 (By similarity). Interacts with IRAK1, TRAF2 and TRAF6 (PubMed:11798190). Interacts with TIFAB; binding to TIFAB inhibits TRAF6 activation, possibly by inducing a conformational change in TIFA (By similarity). Interacts with ZCCHC11; binding to ZCCHC11 suppresses the TRAF6-dependent activation of NF-kappa-B (By similarity). {ECO:0000250|UniProtKB:Q96CG3, ECO:0000269|PubMed:11798190}. DOMAIN: The FHA domain recognizes and binds phosphorylated Thr-9, promoting homooligomerization and subsequent activation of NF-kappa-B. {ECO:0000250|UniProtKB:Q96CG3}. TISSUE SPECIFICITY: Highly expressed in the spleen and at lower levels in heart, brain, lung, liver, kidney and testes. {ECO:0000269|PubMed:11798190, ECO:0000269|PubMed:12566447}. +P40142 TKT_MOUSE Transketolase (TK) (EC 2.2.1.1) (P68) 623 67,630 Active site (1); Binding site (15); Chain (1); Cross-link (1); Metal binding (3); Modified residue (15); Nucleotide binding (1); Sequence conflict (1); Site (2) FUNCTION: Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate. {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +P26039 TLN1_MOUSE Talin-1 2541 269,821 Beta strand (36); Chain (1); Domain (2); Helix (87); Modified residue (21); Natural variant (2); Region (3); Sequence conflict (2); Turn (10) FUNCTION: Probably involved in connections of major cytoskeletal structures to the plasma membrane. High molecular weight cytoskeletal protein concentrated at regions of cell-substratum contact and, in lymphocytes, at cell-cell contacts. SUBCELLULAR LOCATION: Cell projection, ruffle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell surface {ECO:0000269|PubMed:21768292}. Cell junction, focal adhesion {ECO:0000269|PubMed:21768292}. Note=Colocalizes with LAYN at the membrane ruffles (By similarity). Localized preferentially in focal adhesions than fibrillar adhesions. {ECO:0000250}. SUBUNIT: Interacts with NRAP and LAYN (By similarity). Interacts with SYNM (By similarity). Interacts with ITGB1; the interaction is prevented by competitive binding of ITGB1BP1 (By similarity). Binds with high affinity to VCL and with low affinity to integrins (PubMed:23389036, PubMed:20610383, PubMed:15642262, PubMed:15272303). Interacts with APBB1IP; this inhibits VCL binding (PubMed:23389036). Interacts with PTK2/FAK1 (PubMed:7622520). Interacts with PIP5K1C (PubMed:15623515). Interacts with F-actin (PubMed:20610383). {ECO:0000250|UniProtKB:P54939, ECO:0000250|UniProtKB:Q9Y490, ECO:0000269|PubMed:15272303, ECO:0000269|PubMed:15623515, ECO:0000269|PubMed:15642262, ECO:0000269|PubMed:20610383, ECO:0000269|PubMed:23389036, ECO:0000269|PubMed:7622520}. +Q99JY1 TIRAP_MOUSE Toll/interleukin-1 receptor domain-containing adapter protein (TIR domain-containing adapter protein) (Adaptor protein Wyatt) (MyD88 adapter-like protein) 241 26,035 Chain (1); Compositional bias (1); Disulfide bond (2); Domain (1); Sequence conflict (1) FUNCTION: Adapter involved in the TLR2 and TLR4 signaling pathways in the innate immune response. Acts via IRAK2 and TRAF-6, leading to the activation of NF-kappa-B, MAPK1, MAPK3 and JNK, and resulting in cytokine secretion and the inflammatory response (By similarity). Positively regulates the production of TNF-alpha and interleukin-6 (By similarity). {ECO:0000250}. PTM: Phosphorylated by IRAK1 and IRAK4. Also phosphorylated by BTK. {ECO:0000250}.; PTM: Polyubiquitinated. Polyubiquitination follows phosphorylation by BTK and leads to TIRAP degradation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Membrane {ECO:0000250}. Note=Colocalizes with DAB2IP at the plasma membrane. {ECO:0000250}. SUBUNIT: Homodimer. Also forms heterodimers with MYD88. Interacts with BMX and TBK1 (By similarity). Interacts with TLR4 and IRAK2 via their respective TIR domains. Interacts with EIF2AK2. Does not interact with IRAK1-1, nor TLR9. May interact with PIK3AP1. {ECO:0000250, ECO:0000269|PubMed:22187460}. +Q9CQ44 TM218_MOUSE Transmembrane protein 218 115 12,464 Chain (1); Sequence conflict (2); Transmembrane (3) TRANSMEM 5 25 Helical. {ECO:0000255}.; TRANSMEM 38 58 Helical. {ECO:0000255}.; TRANSMEM 81 101 Helical. {ECO:0000255}. FUNCTION: May be involved in ciliary biogenesis or function. {ECO:0000305|PubMed:25161209}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cell projection, cilium {ECO:0000269|PubMed:26982032}. Note=Localizes at the transition zone, a region between the basal body and the ciliary axoneme. {ECO:0000269|PubMed:26982032}. +Q7TQI0 TM204_MOUSE Transmembrane protein 204 (Claudin-like protein 24) 226 24,785 Chain (1); Glycosylation (1); Topological domain (5); Transmembrane (4) TRANSMEM 6 26 Helical. {ECO:0000255}.; TRANSMEM 104 124 Helical. {ECO:0000255}.; TRANSMEM 137 157 Helical. {ECO:0000255}.; TRANSMEM 171 191 Helical. {ECO:0000255}. TOPO_DOM 1 5 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 27 103 Extracellular. {ECO:0000255}.; TOPO_DOM 125 136 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 158 170 Extracellular. {ECO:0000255}.; TOPO_DOM 192 226 Cytoplasmic. {ECO:0000255}. FUNCTION: Can influence paracellular permeability. Appears to be involved in cell-cell interactions through adherens (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, adherens junction. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Co-localizes with the beta-catenin adherins. {ECO:0000250}. +Q91XE8 TM205_MOUSE Transmembrane protein 205 189 21,180 Chain (1); Sequence conflict (1); Transmembrane (4) TRANSMEM 18 38 Helical. {ECO:0000255}.; TRANSMEM 53 73 Helical. {ECO:0000255}.; TRANSMEM 81 101 Helical. {ECO:0000255}.; TRANSMEM 166 186 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8C4U2 TM145_MOUSE Transmembrane protein 145 746 82,473 Chain (1); Glycosylation (3); Transmembrane (8) TRANSMEM 9 29 Helical. {ECO:0000255}.; TRANSMEM 189 209 Helical. {ECO:0000255}.; TRANSMEM 221 241 Helical. {ECO:0000255}.; TRANSMEM 255 275 Helical. {ECO:0000255}.; TRANSMEM 296 316 Helical. {ECO:0000255}.; TRANSMEM 332 352 Helical. {ECO:0000255}.; TRANSMEM 363 383 Helical. {ECO:0000255}.; TRANSMEM 395 415 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q91YV9 TM246_MOUSE Transmembrane protein 246 403 46,592 Chain (1); Sequence conflict (1); Transmembrane (3) TRANSMEM 23 43 Helical. {ECO:0000255}.; TRANSMEM 265 285 Helical. {ECO:0000255}.; TRANSMEM 288 308 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9CR96 TM208_MOUSE Transmembrane protein 208 173 19,624 Alternative sequence (1); Chain (1); Modified residue (1); Sequence conflict (1); Transmembrane (3) TRANSMEM 25 45 Helical. {ECO:0000255}.; TRANSMEM 51 68 Helical. {ECO:0000255}.; TRANSMEM 105 129 Helical. {ECO:0000255}. FUNCTION: May function as a negative regulator of endoplasmic reticulum-stress induced autophagy. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q497K7 TM247_MOUSE Transmembrane protein 247 211 23,971 Chain (1); Coiled coil (1); Compositional bias (1); Erroneous initiation (1); Sequence conflict (1); Transmembrane (2) TRANSMEM 159 179 Helical. {ECO:0000255}.; TRANSMEM 186 206 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9D2F0 TM210_MOUSE Transmembrane protein 210 147 15,214 Chain (1); Compositional bias (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 48 68 Helical. {ECO:0000255}. TOPO_DOM 32 47 Extracellular. {ECO:0000255}.; TOPO_DOM 69 147 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q6F5E0 TM158_MOUSE Transmembrane protein 158 (40 kDa BINP-binding protein) (p40BBP) (Ras-induced senescence protein 1) 286 29,145 Chain (1); Compositional bias (1); Glycosylation (1); Signal peptide (1); Transmembrane (2) TRANSMEM 215 235 Helical. {ECO:0000255}.; TRANSMEM 263 283 Helical. {ECO:0000255}. FUNCTION: Receptor for brain injury-derived neurotrophic peptide (BINP), a synthetic 13-mer peptide. {ECO:0000250}. PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Ubiquitously expressed. Brain is the major site of expression. {ECO:0000269|PubMed:16964279}. +Q9D563 TM114_MOUSE Transmembrane protein 114 (Claudin-26) 222 24,388 Chain (1); Glycosylation (2); Mutagenesis (2); Transmembrane (4) TRANSMEM 7 27 Helical. {ECO:0000255}.; TRANSMEM 105 125 Helical. {ECO:0000255}.; TRANSMEM 133 153 Helical. {ECO:0000255}.; TRANSMEM 188 208 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21689651}; Multi-pass membrane protein {ECO:0000269|PubMed:21689651}. Note=N-glycosylation at Asn-54 and Asn-88 is required for plasma membrane localization. +Q3UNB8 TM253_MOUSE Transmembrane protein 253 204 22,415 Chain (1); Transmembrane (4) TRANSMEM 33 53 Helical. {ECO:0000255}.; TRANSMEM 62 82 Helical. {ECO:0000255}.; TRANSMEM 96 116 Helical. {ECO:0000255}.; TRANSMEM 138 158 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9CR02 TMA16_MOUSE Translation machinery-associated protein 16 221 25,782 Alternative sequence (1); Chain (1) +Q99KF1 TMED9_MOUSE Transmembrane emp24 domain-containing protein 9 (Glycoprotein 25L2) (p24 family protein alpha-2) (p24alpha2) 235 27,127 Chain (1); Coiled coil (1); Domain (1); Erroneous initiation (1); Glycosylation (1); Modified residue (1); Motif (2); Region (1); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 203 222 Helical. {ECO:0000255}. TOPO_DOM 38 202 Lumenal. {ECO:0000255}.; TOPO_DOM 223 235 Cytoplasmic. {ECO:0000255}. FUNCTION: Appears to be involved in vesicular protein trafficking, mainly in the early secretory pathway. In COPI vesicle-mediated retrograde transport involved in the coatomer recruitment to membranes of the early secretory pathway. Increases coatomer-dependent activity of ARFGAP2. Thought to play a crucial role in the specific retention of p24 complexes in cis-Golgi membranes; specifically contributes to the coupled localization of TMED2 and TMED10 in the cis-Golgi network. May be involved in organization of intracellular membranes, such as of the ER-Golgi intermediate compartment and the Golgi apparatus. Involved in ER localization of PTPN2 (By similarity). {ECO:0000250}. PTM: N-linked glycosylated containing high mannose. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Golgi apparatus, cis-Golgi network membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Cycles between compartments of the early secretatory pathway. {ECO:0000250}. SUBUNIT: Monomer and homodimer in endoplasmic reticulum. Predominantly monomeric and to lesser extent homodimeric in endoplasmic reticulum-Golgi intermediate compartment and cis-Golgi network. Probably oligomerizes with other members of the EMP24/GP25L family such as TMED2, TMED7 and TMED10. Interacts with TMED5. Interacts (via C-terminus) with COPG1; the interaction involves dimeric TMED9. Interacts with PTPN2 and SPAST. Interacts with STX17; the interaction is direct (By similarity). {ECO:0000250}. +B1AWJ5 TMM8B_MOUSE Transmembrane protein 8B (Protein NGX6) 472 52,114 Chain (1); Disulfide bond (3); Domain (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 234 254 Helical. {ECO:0000255}.; TRANSMEM 258 277 Helical. {ECO:0000255}.; TRANSMEM 293 313 Helical. {ECO:0000255}.; TRANSMEM 316 336 Helical. {ECO:0000255}.; TRANSMEM 343 363 Helical. {ECO:0000255}.; TRANSMEM 380 400 Helical. {ECO:0000255}.; TRANSMEM 406 426 Helical. {ECO:0000255}. TOPO_DOM 1 233 Extracellular. {ECO:0000255}.; TOPO_DOM 255 257 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 278 292 Extracellular. {ECO:0000255}.; TOPO_DOM 314 315 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 337 342 Extracellular. {ECO:0000255}.; TOPO_DOM 364 379 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 401 405 Extracellular. {ECO:0000255}.; TOPO_DOM 427 472 Cytoplasmic. {ECO:0000255}. FUNCTION: May function as a regulator of the EGFR pathway. Probable tumor suppressor which may function in cell growth, proliferation and adhesion (By similarity). {ECO:0000250}. PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:A6NDV4}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A6NDV4}. Cytoplasm {ECO:0000250|UniProtKB:A6NDV4}. Nucleus {ECO:0000250|UniProtKB:A6NDV4}. Mitochondrion {ECO:0000250|UniProtKB:A6NDV4}. Endoplasmic reticulum {ECO:0000250|UniProtKB:A6NDV4}. Note=Also detected in mitochondrion and endoplasmic reticulum. {ECO:0000250|UniProtKB:A6NDV4}. SUBUNIT: May interact with EZR. {ECO:0000250}. +Q3UP23 TMM26_MOUSE Transmembrane protein 26 366 41,637 Chain (1); Glycosylation (1); Sequence conflict (2); Transmembrane (8) TRANSMEM 4 24 Helical. {ECO:0000255}.; TRANSMEM 36 56 Helical. {ECO:0000255}.; TRANSMEM 64 84 Helical. {ECO:0000255}.; TRANSMEM 138 158 Helical. {ECO:0000255}.; TRANSMEM 176 196 Helical. {ECO:0000255}.; TRANSMEM 208 228 Helical. {ECO:0000255}.; TRANSMEM 258 278 Helical. {ECO:0000255}.; TRANSMEM 282 302 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q80WC3 TNC18_MOUSE Trinucleotide repeat-containing gene 18 protein (Zinc finger protein 469) 2878 307,635 Alternative sequence (5); Chain (1); Coiled coil (1); Compositional bias (7); Cross-link (1); Domain (1); Erroneous initiation (1); Modified residue (9); Sequence conflict (5) +Q4VAE3 TMM65_MOUSE Transmembrane protein 65 234 24,918 Chain (1); Erroneous initiation (1); Topological domain (4); Transit peptide (1); Transmembrane (3) TRANSMEM 111 131 Helical. {ECO:0000255}.; TRANSMEM 139 159 Helical. {ECO:0000255}.; TRANSMEM 204 224 Helical. {ECO:0000255}. TOPO_DOM 56 110 Cytoplasmic. {ECO:0000250|UniProtKB:Q6PI78}.; TOPO_DOM 132 138 Extracellular. {ECO:0000250|UniProtKB:Q6PI78}.; TOPO_DOM 160 203 Cytoplasmic. {ECO:0000250|UniProtKB:Q6PI78}.; TOPO_DOM 225 234 Extracellular. {ECO:0000250|UniProtKB:Q6PI78}. FUNCTION: May play an important role in cardiac development and function. May regulate cardiac conduction and the function of the gap junction protein GJA1. May contributes to the stability and proper localization of GJA1 to cardiac intercalated disk thereby regulating gap junction communication (PubMed:26403541). Regulates mitochondrial respiration and mitochondrial DNA copy number maintenance (By similarity). {ECO:0000250|UniProtKB:Q6PI78, ECO:0000269|PubMed:26403541}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26403541}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q6PI78}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes at the intercalated disk in ventricular tissue and cardiomyocytes. {ECO:0000269|PubMed:26403541}. SUBUNIT: Monomer. Homodimer. Interacts with GJA1. Interacts weakly with DSP. {ECO:0000269|PubMed:26403541}. TISSUE SPECIFICITY: Predominantly expressed in the ventricular tissue (at protein level). {ECO:0000269|PubMed:26403541}. +Q9D709 TMM79_MOUSE Transmembrane protein 79 (Mattrin) 391 43,464 Chain (1); Topological domain (6); Transmembrane (5) TRANSMEM 201 221 Helical. {ECO:0000255}.; TRANSMEM 241 261 Helical. {ECO:0000255}.; TRANSMEM 280 300 Helical. {ECO:0000255}.; TRANSMEM 310 330 Helical. {ECO:0000255}.; TRANSMEM 340 360 Helical. {ECO:0000255}. TOPO_DOM 1 200 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 222 240 Extracellular. {ECO:0000255}.; TOPO_DOM 262 279 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 301 309 Extracellular. {ECO:0000255}.; TOPO_DOM 331 339 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 361 391 Extracellular. {ECO:0000255}. FUNCTION: Contributes to the epidermal integrity and skin barrier function. Plays a role in the lamellar granule (LG) secretory system and in the stratum corneum (SC) epithelial cell formation. {ECO:0000269|PubMed:24060273}. SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:24060273}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:24060273}. Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=Colocalized with TGOLN2 in the trans-Golgi network. Colocalized with LAMP1 in the lysosome. TISSUE SPECIFICITY: Expressed in the epidermis of the skin. Expressed in epithelial cells of the outermost layer of the stratum granulosum (SG) and in hair follicles (at protein level). {ECO:0000269|PubMed:24060273, ECO:0000269|PubMed:24084074}. DISEASE: Note=Defects in Tmem79 are the cause of the spontaneous matted (matt) mutant phenotype, a model for human atopic dermatitis. Atopic dermatitis (ma/ma) mice have a matted hair phenotype with progressive dermatitis-like skin inflammation and a scratching behavior. Mice display an altered skin barrier that facilitates allergic sensitization. {ECO:0000269|PubMed:24084074}. +Q61333 TNAP2_MOUSE Tumor necrosis factor alpha-induced protein 2 (TNF alpha-induced protein 2) (Primary response gene B94 protein) 691 78,102 Beta strand (4); Chain (1); Erroneous initiation (1); Helix (27); Sequence conflict (2); Turn (5) FUNCTION: May play a role as a mediator of inflammation and angiogenesis. +Q8CGF5 TMM56_MOUSE Transmembrane protein 56 276 31,236 Alternative sequence (2); Chain (1); Domain (1); Modified residue (1); Transmembrane (6) TRANSMEM 20 40 Helical. {ECO:0000255}.; TRANSMEM 66 86 Helical. {ECO:0000255}.; TRANSMEM 101 121 Helical. {ECO:0000255}.; TRANSMEM 130 150 Helical. {ECO:0000255}.; TRANSMEM 191 211 Helical. {ECO:0000255}.; TRANSMEM 224 244 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8K0U3 TMM17_MOUSE Transmembrane protein 17 198 22,623 Chain (1); Glycosylation (1); Transmembrane (4) TRANSMEM 47 67 Helical. {ECO:0000255}.; TRANSMEM 78 98 Helical. {ECO:0000255}.; TRANSMEM 110 130 Helical. {ECO:0000255}.; TRANSMEM 142 162 Helical. {ECO:0000255}. FUNCTION: Transmembrane component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. Required for ciliogenesis and sonic hedgehog/SHH signaling. {ECO:0000269|PubMed:22179047}. SUBCELLULAR LOCATION: Cell projection, cilium membrane {ECO:0000269|PubMed:22179047}; Multi-pass membrane protein {ECO:0000269|PubMed:22179047}. Note=Localizes to the transition zone of primary cilia. SUBUNIT: Part of the tectonic-like complex (also named B9 complex). {ECO:0000269|PubMed:22179047}. +Q9DA04 TMM89_MOUSE Transmembrane protein 89 169 18,598 Alternative sequence (2); Chain (1); Frameshift (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 76 96 Helical. {ECO:0000255}. TOPO_DOM 23 75 Extracellular. {ECO:0000255}.; TOPO_DOM 97 169 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q80WM9 TNR14_MOUSE Tumor necrosis factor receptor superfamily member 14 (Herpes virus entry mediator A) (Herpesvirus entry mediator A) (HveA) (Tumor necrosis factor receptor-like 2) (TR2) (CD antigen CD270) 275 30,171 Chain (1); Disulfide bond (8); Glycosylation (2); Repeat (3); Signal peptide (1); Transmembrane (1) TRANSMEM 211 231 Helical. {ECO:0000255}. FUNCTION: Receptor for four distinct ligands: The TNF superfamily members TNFSF14/LIGHT and homotrimeric LTA/lymphotoxin-alpha and the immunoglobulin superfamily members BTLA and CD160, altogether defining a complex stimulatory and inhibitory signaling network (By similarity). Signals via the TRAF2-TRAF3 E3 ligase pathway to promote immune cell survival and differentiation (PubMed:19915044). Participates in bidirectional cell-cell contact signaling between antigen presenting cells and lymphocytes. In response to ligation of TNFSF14/LIGHT, delivers costimulatory signals to T cells, promoting cell proliferation and effector functions (By similarity). Interacts with CD160 on NK cells, enhancing IFNG production and anti-tumor immune response (PubMed:25711213). In the context of bacterial infection, acts as a signaling receptor on epithelial cells for CD160 from intraepithelial lymphocytes, triggering the production of antimicrobial proteins and proinflammatory cytokines (PubMed:22801499). Upon binding to CD160 on activated CD4+ T cells, downregulates CD28 costimulatory signaling, restricting memory and alloantigen-specific immune response (By similarity). May interact in cis (on the same cell) or in trans (on other cells) with BTLA (PubMed:19915044, PubMed:15568026). In cis interactions, appears to play an immune regulatory role inhibiting in trans interactions in naive T cells to maintain a resting state. In trans interactions, can predominate during adaptive immune response to provide survival signals to effector T cells (PubMed:19915044, PubMed:15568026). {ECO:0000250|UniProtKB:Q92956, ECO:0000269|PubMed:15568026, ECO:0000269|PubMed:19915044, ECO:0000269|PubMed:22801499, ECO:0000269|PubMed:25711213}. PTM: N-glycosylated. {ECO:0000255|PROSITE-ProRule:PRU00498}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15568026}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q92956}. SUBUNIT: Interacts with TRAF2, TRAF3 and TRAF5 (By similarity). Interacts (via CRD1/TNFR-Cys 1) with CD160; this interaction is direct (PubMed:18193050). Interacts (via CRD1/TNFR-Cys 1) with BTLA; this interaction is direct (PubMed:15568026). {ECO:0000250|UniProtKB:Q92956, ECO:0000269|PubMed:15568026, ECO:0000269|PubMed:18193050}. DOMAIN: The cysteine rich domain I (CRD1/TNFR-Cys 1) is required for interaction with CD160 and BTLA. {ECO:0000269|PubMed:15568026}. TISSUE SPECIFICITY: Expressed at mucosal sites including colon and pulmonary epithelial cells (PubMed:22801499). Expressed in naive T cells (PubMed:19915044). {ECO:0000269|PubMed:19915044, ECO:0000269|PubMed:22801499}. +Q9Z0W1 TNR16_MOUSE Tumor necrosis factor receptor superfamily member 16 (Low affinity neurotrophin receptor p75NTR) (Low-affinity nerve growth factor receptor) (NGF receptor) (CD antigen CD271) 417 44,686 Chain (1); Compositional bias (1); Disulfide bond (12); Domain (1); Glycosylation (1); Modified residue (1); Region (1); Repeat (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 247 265 Helical. {ECO:0000255}. TOPO_DOM 22 246 Extracellular. {ECO:0000255}.; TOPO_DOM 266 417 Cytoplasmic. {ECO:0000255}. FUNCTION: Low affinity receptor which can bind to NGF, BDNF, NT-3, and NT-4. Can mediate cell survival as well as cell death of neural cells (By similarity). Plays a role in the regulation of the translocation of GLUT4 to the cell surface in adipocytes and skeletal muscle cells in response to insulin, probably by regulating RAB31 activity, and thereby contributes to the regulation of insulin-dependent glucose uptake. Binds to rabies virus glycoprotein Gs. Necessary for the circadian oscillation of the clock genes ARNTL/BMAL1, PER1, PER2 and NR1D1 in the suprachiasmatic nucleus (SCN) of the brain and in liver and of the genes involved in glucose and lipid metabolism in the liver. {ECO:0000250, ECO:0000269|PubMed:22460790, ECO:0000269|PubMed:23785138}. PTM: N- and O-glycosylated. {ECO:0000250}.; PTM: Phosphorylated on serine residues. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Homodimer; disulfide-linked. Interacts with p75NTR-associated cell death executor. Interacts with TRAF2, TRAF4, TRAF6, PTPN13 and RANBP9. Interacts through TRAF6 with SQSTM1 which bridges NGFR to NTRK1. Interacts with BEX1 and BEX3. Interacts with KIDINS220 and NTRK1. Can form a ternary complex with NTRK1 and KIDINS220 and this complex is affected by the expression levels of KIDINS220. An increase in KIDINS220 expression leads to a decreased association of NGFR and NTRK1. Interacts (via death domain) with RAB31. Interacts with NTRK2; may regulate the ligand specificity of the NTRK2 receptor. Interacts with LINGO1 and NRADD. Interacts with MAGED1; the interaction antagonizes the association NGFR:NTRK1. Interacts with RTN4R (PubMed:22923615). {ECO:0000269|PubMed:11830582, ECO:0000269|PubMed:22460790, ECO:0000269|PubMed:22923615}. DOMAIN: Death domain is responsible for interaction with RANBP9. {ECO:0000250}.; DOMAIN: The extracellular domain is responsible for interaction with NTRK1. {ECO:0000250}. +O35714 TNR18_MOUSE Tumor necrosis factor receptor superfamily member 18 (Glucocorticoid-induced TNFR-related protein) (CD antigen CD357) 228 25,334 Alternative sequence (3); Chain (1); Disulfide bond (5); Glycosylation (4); Mutagenesis (5); Repeat (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 154 174 Helical. {ECO:0000255}. TOPO_DOM 20 153 Extracellular. {ECO:0000255}.; TOPO_DOM 175 228 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for TNFSF18. Seems to be involved in interactions between activated T-lymphocytes and endothelial cells and in the regulation of T-cell receptor-mediated cell death. Mediated NF-kappa-B activation via the TRAF2/NIK pathway (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Isoform A: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Isoform B: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Isoform C: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Isoform D: Secreted. SUBUNIT: Binds to TRAF1, TRAF2, and TRAF3, but not TRAF5 and TRAF6 (By similarity). Binds through its C-terminus to SIVA1/SIVA. {ECO:0000250}. TISSUE SPECIFICITY: Preferentially expressed in activated T lymphocytes. +Q61471 TOB1_MOUSE Protein Tob1 (Transducer of erbB-2 1) 362 40,056 Chain (1); Compositional bias (3); Modified residue (1); Motif (2); Mutagenesis (4); Region (2); Sequence conflict (3) FUNCTION: Anti-proliferative protein; the function is mediated by association with deadenylase subunits of the CCR4-NOT complex. Mediates CPEB3-accelerated mRNA deadenylation by binding to CPEB3 and recruiting CNOT7 which leads to target mRNA deadenylation and decay. {ECO:0000250|UniProtKB:P50616}. PTM: Phosphorylated on Ser and Thr residues. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15235587}. Nucleus {ECO:0000269|PubMed:15235587}. Note=Only a small fraction localizes to the cytoplasm except in late S-phase where more than half of proteins become cytoplasmic. SUBUNIT: Interacts with ERBB2. Interacts with CNOT7. Interacts with CPEB3 (via C-terminal RNA-binding region); recruits CNOT7 to CPEB3 to form a ternary complex required for mRNA deadenylation and decay. Interacts with CNOT8. Interacts with CPEB4. {ECO:0000250|UniProtKB:P50616, ECO:0000250|UniProtKB:Q8R5K6}. TISSUE SPECIFICITY: Ubiquitous. +P25119 TNR1B_MOUSE Tumor necrosis factor receptor superfamily member 1B (Tumor necrosis factor receptor 2) (TNF-R2) (Tumor necrosis factor receptor type II) (TNF-RII) (TNFR-II) (p75) (p80 TNF-alpha receptor) (CD antigen CD120b) 474 50,320 Chain (1); Disulfide bond (10); Glycosylation (5); Modified residue (1); Repeat (4); Sequence conflict (7); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 259 288 Helical. {ECO:0000255}. TOPO_DOM 23 258 Extracellular. {ECO:0000255}.; TOPO_DOM 289 474 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor with high affinity for TNFSF2/TNF-alpha and approximately 5-fold lower affinity for homotrimeric TNFSF1/lymphotoxin-alpha. The TRAF1/TRAF2 complex recruits the apoptotic suppressors BIRC2 and BIRC3 to TNFRSF1B/TNFR2 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Binds to TRAF2. Interacts with BMX. Interacts (activated form) with XPNPEP3. {ECO:0000250|UniProtKB:P20333}. +Q8CGB6 TNS2_MOUSE Tensin-2 (EC 3.1.3.-) (C1 domain-containing phosphatase and tensin homolog) (C1-TEN) (Tensin-like C1 domain-containing phosphatase) 1400 152,013 Active site (1); Alternative sequence (3); Chain (1); Compositional bias (2); Domain (3); Frameshift (1); Modified residue (25); Sequence conflict (4); Zinc finger (1) FUNCTION: Regulates cell motility and proliferation. May have phosphatase activity. Reduces AKT1 phosphorylation. Lowers AKT1 kinase activity and interferes with AKT1 signaling (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q63HR2}. Cell membrane {ECO:0000250|UniProtKB:Q63HR2}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q63HR2}; Cytoplasmic side {ECO:0000250|UniProtKB:Q63HR2}. Note=Detected at the end of actin stress fibers. Detected in cytoplasmic punctate bodies. {ECO:0000250|UniProtKB:Q63HR2}. SUBUNIT: Interacts with AXL. Interacts with SYK; leading to its phosphorylation (By similarity). {ECO:0000250|UniProtKB:Q63HR2}. +Q6NZL6 TONSL_MOUSE Tonsoku-like protein (Inhibitor of kappa B-related protein) (I-kappa-B-related protein) (IkappaBR) (NF-kappa-B inhibitor-like protein 2) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells inhibitor-like 2) 1363 151,108 Chain (1); Compositional bias (1); Erroneous gene model prediction (1); Erroneous initiation (2); Modified residue (1); Repeat (21); Sequence conflict (2) FUNCTION: Component of the MMS22L-TONSL complex, a complex that stimulates the recombination-dependent repair of stalled or collapsed replication forks. The MMS22L-TONSL complex is required to maintain genome integrity during DNA replication by promoting homologous recombination-mediated repair of replication fork-associated double-strand breaks. It may act by mediating the assembly of RAD51 filaments on ssDNA. Within the complex, may act as a scaffold (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Mainly nuclear. Localizes to DNA damage sites, accumulates at stressed replication forks (By similarity). {ECO:0000250}. SUBUNIT: Component of the MMS22L-TONSL complex, a complex at least composed of MMS22L and TONSL/NFKBIL2. Interacts with the MCM complex, the FACT complex and the RPA complex. Binds histones (By similarity). {ECO:0000250}. DOMAIN: The ANK repeats mediate the interaction with the MCM complex and histones, while the LRR repeats mediate the interaction with MMS22L. {ECO:0000250}. +Q8R4U6 TOP1M_MOUSE DNA topoisomerase I, mitochondrial (TOP1mt) (EC 5.99.1.2) 593 69,003 Active site (1); Chain (1); Region (3); Site (9); Transit peptide (1) FUNCTION: Releases the supercoiling and torsional tension of DNA introduced during duplication of mitochondrial DNA by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free DNA strand then rotates around the intact phosphodiester bond on the opposing strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. +Q9Z109 VSIG2_MOUSE V-set and immunoglobulin domain-containing protein 2 (Cortical thymocyte-like protein) (CT-like protein) 328 34,514 Alternative sequence (1); Chain (1); Disulfide bond (2); Domain (2); Glycosylation (3); Sequence conflict (9); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 245 265 Helical. {ECO:0000255}. TOPO_DOM 25 244 Extracellular. {ECO:0000255}.; TOPO_DOM 266 328 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in the stomach, colon and prostate. {ECO:0000269|PubMed:9862345}. +Q91V10 VSX1_MOUSE Visual system homeobox 1 (Homeodomain protein RINX) (Retinal inner nuclear layer homeobox protein) (Transcription factor VSX1) 363 38,755 Chain (1); Compositional bias (3); DNA binding (1); Domain (1); Motif (2) FUNCTION: Binds to the 37-bp core of the locus control region (LCR) of the red/green visual pigment gene cluster. May regulate the activity of the LCR and the cone opsin genes at earlier stages of development (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. TISSUE SPECIFICITY: In the adult, expressed exclusively in the cells of the neural retina with expression restricted to postnatal cone bipolar interneurons. +Q70UZ7 VWA2_MOUSE von Willebrand factor A domain-containing protein 2 (A domain-containing protein similar to matrilin and collagen) (AMACO) 791 85,639 Alternative sequence (2); Chain (1); Disulfide bond (6); Domain (5); Glycosylation (1); Sequence conflict (10); Signal peptide (1) SUBCELLULAR LOCATION: Secreted. SUBUNIT: Forms monomers and multimers. {ECO:0000269|PubMed:14506275}. TISSUE SPECIFICITY: Detected in uterus, kidney, and skin. Also detected in intestine and lung of adult mice, and in calvaria, femur, brain, heart, intestine, skeletal muscle, and lung of newborn mice. {ECO:0000269|PubMed:14506275}. +Q6NXJ0 WWC2_MOUSE Protein WWC2 (WW domain-containing protein 2) 1187 132,620 Chain (1); Coiled coil (5); Domain (3); Erroneous initiation (1); Frameshift (1); Modified residue (3); Sequence conflict (9) +Q5GH67 XKR4_MOUSE XK-related protein 4 647 71,503 Chain (1); Modified residue (1); Transmembrane (10) TRANSMEM 112 132 Helical. {ECO:0000255}.; TRANSMEM 142 162 Helical. {ECO:0000255}.; TRANSMEM 245 265 Helical. {ECO:0000255}.; TRANSMEM 303 323 Helical. {ECO:0000255}.; TRANSMEM 328 348 Helical. {ECO:0000255}.; TRANSMEM 362 382 Helical. {ECO:0000255}.; TRANSMEM 393 415 Helical. {ECO:0000255}.; TRANSMEM 425 445 Helical. {ECO:0000255}.; TRANSMEM 454 474 Helical. {ECO:0000255}.; TRANSMEM 484 504 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q5GH62 XKR9_MOUSE XK-related protein 9 373 43,271 Chain (1); Transmembrane (8) TRANSMEM 8 28 Helical. {ECO:0000255}.; TRANSMEM 38 58 Helical. {ECO:0000255}.; TRANSMEM 166 186 Helical. {ECO:0000255}.; TRANSMEM 206 226 Helical. {ECO:0000255}.; TRANSMEM 230 250 Helical. {ECO:0000255}.; TRANSMEM 256 276 Helical. {ECO:0000255}.; TRANSMEM 295 315 Helical. {ECO:0000255}.; TRANSMEM 318 338 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q6P205 XL3B_MOUSE X-linked lymphocyte-regulated protein 3B 226 26,147 Chain (1); Coiled coil (1) +Q3U3V8 XRRA1_MOUSE X-ray radiation resistance-associated protein 1 786 88,884 Chain (1); Coiled coil (1); Erroneous initiation (1); Repeat (5) FUNCTION: May be involved in the response of cells to X-ray radiation. {ECO:0000250|UniProtKB:Q6P2D8}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6P2D8}. Nucleus {ECO:0000250|UniProtKB:Q6P2D8}. +Q9EPL0 XYLT2_MOUSE Xylosyltransferase 2 (EC 2.4.2.26) (Peptide O-xylosyltransferase 2) (Xylosyltransferase II) 865 96,811 Binding site (3); Chain (1); Disulfide bond (6); Erroneous initiation (1); Glycosylation (3); Region (3); Sequence conflict (16); Topological domain (2); Transmembrane (1) TRANSMEM 16 36 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 15 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 37 865 Lumenal. {ECO:0000255}. Glycan metabolism; chondroitin sulfate biosynthesis. Glycan metabolism; heparan sulfate biosynthesis. FUNCTION: Catalyzes the first step in the biosynthesis of chondroitin sulfate, heparan sulfate and dermatan sulfate proteoglycans, such as DCN (PubMed:17517600). Transfers D-xylose from UDP-D-xylose to specific serine residues of the core protein (By similarity). {ECO:0000250|UniProtKB:Q9H1B5, ECO:0000269|PubMed:17517600}. PTM: Contains disulfide bonds. {ECO:0000250|UniProtKB:Q86Y38}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9H1B5}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9H1B5}. Secreted {ECO:0000250|UniProtKB:Q9H1B5}. SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q86Y38}. TISSUE SPECIFICITY: Detected in brain, liver, lung, kidney, heart, spleen and testis, and at lower levels in skeletal muscle. {ECO:0000269|PubMed:17189265}. +Q924T3 XRCC4_MOUSE DNA repair protein XRCC4 (X-ray repair cross-complementing protein 4) 326 37,061 Alternative sequence (1); Chain (1); Coiled coil (2); Modified residue (11); Region (1); Sequence conflict (7) FUNCTION: Involved in DNA nonhomologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. Binds to DNA and to DNA ligase IV (LIG4). The LIG4-XRCC4 complex is responsible for the NHEJ ligation step, and XRCC4 enhances the joining activity of LIG4. Binding of the LIG4-XRCC4 complex to DNA ends is dependent on the assembly of the DNA-dependent protein kinase complex DNA-PK to these DNA ends (By similarity). {ECO:0000250, ECO:0000269|PubMed:9875844}. PTM: Phosphorylation by CK2 promotes interaction with APTX. {ECO:0000250}.; PTM: Monoubiquitinated. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Homodimer and homotetramer in solution. The homodimer associates with LIG4. The LIG4-XRCC4 complex associates in a DNA-dependent manner with the DNA-PK complex composed of PRKDC, XRCC6/Ku70 and XRCC5/Ku86 to form the core non-homologous end joining (NHEJ) complex. Additional components of the NHEJ complex include NHEJ1/XLF and PAXX. Interacts directly with PRKDC but not with the XRCC6/Ku70 and XRCC5/Ku86 dimer. Interacts with APTX and APLF. {ECO:0000250|UniProtKB:Q13426}. +P27641 XRCC5_MOUSE X-ray repair cross-complementing protein 5 (EC 3.6.4.-) (ATP-dependent DNA helicase 2 subunit 2) (ATP-dependent DNA helicase II 80 kDa subunit) (CTC box-binding factor 85 kDa subunit) (CTC85) (CTCBF) (DNA repair protein XRCC5) (Ku autoantigen protein p86 homolog) (Ku80) (Nuclear factor IV) 732 83,057 Chain (1); Compositional bias (1); Cross-link (7); Domain (1); Modified residue (10); Motif (1); Region (1); Sequence conflict (23) FUNCTION: Single-stranded DNA-dependent ATP-dependent helicase. Has a role in chromosome translocation. The DNA helicase II complex binds preferentially to fork-like ends of double-stranded DNA in a cell cycle-dependent manner. It works in the 3'-5' direction. Binding to DNA may be mediated by XRCC6. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. The XRCC5/6 dimer acts as regulatory subunit of the DNA-dependent protein kinase complex DNA-PK by increasing the affinity of the catalytic subunit PRKDC to DNA by 100-fold. The XRCC5/6 dimer is probably involved in stabilizing broken DNA ends and bringing them together. The assembly of the DNA-PK complex to DNA ends is required for the NHEJ ligation step. In association with NAA15, the XRCC5/6 dimer binds to the osteocalcin promoter and activates osteocalcin expression. The XRCC5/6 dimer probably also acts as a 5'-deoxyribose-5-phosphate lyase (5'-dRP lyase), by catalyzing the beta-elimination of the 5' deoxyribose-5-phosphate at an abasic site near double-strand breaks. XRCC5 probably acts as the catalytic subunit of 5'-dRP activity, and allows to 'clean' the termini of abasic sites, a class of nucleotide damage commonly associated with strand breaks, before such broken ends can be joined. The XRCC5/6 dimer together with APEX1 acts as a negative regulator of transcription. Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway. {ECO:0000250|UniProtKB:P13010}. PTM: ADP-ribosylated by PARP3. {ECO:0000250|UniProtKB:P13010}.; PTM: Phosphorylated on serine residues. Phosphorylation by PRKDC may enhance helicase activity. {ECO:0000250|UniProtKB:P13010}.; PTM: Sumoylated. {ECO:0000250|UniProtKB:P13010}.; PTM: Ubiquitinated by RNF8 via 'Lys-48'-linked ubiquitination following DNA damage, leading to its degradation and removal from DNA damage sites. Ubiquitinated by RNF138, leading to remove the Ku complex from DNA breaks. {ECO:0000250|UniProtKB:P13010}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P13010}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P13010}. Chromosome {ECO:0000250|UniProtKB:P13010}. SUBUNIT: Heterodimer composed of XRCC5/Ku80 and XRCC6/Ku70. The dimer associates in a DNA-dependent manner with PRKDC to form the DNA-dependent protein kinase complex DNA-PK, and with the LIG4-XRCC4 complex to form the core of the non-homologous end joining (NHEJ) complex. Additional components of the NHEJ complex include NHEJ1/XLF and PAXX. The dimer also associates with NAA15, and this complex displays DNA binding activity towards the osteocalcin FGF response element (OCFRE). In addition, XRCC5 binds to the osteoblast-specific transcription factors MSX2 and RUNX2. Interacts with ELF3. May interact with APLF. The XRCC5/XRCC6 dimer associates in a DNA-dependent manner with APEX1. Identified in a complex with DEAF1 and XRCC6. Interacts with NR4A3; the DNA-dependent protein kinase complex DNA-PK phosphorylates and activates NR4A3 and prevents NR4A3 ubiquitinylation and degradation. Interacts with RNF138. Interacts with CYREN. Interacts (via N-terminus) with HSF1 (via N-terminus); this interaction is direct and prevents XRCC5/XRCC6 heterodimeric binding and non-homologous end joining (NHEJ) repair activities induced by ionizing radiation (IR). Interacts with DHX9; this interaction occurs in a RNA-dependent manner. Part of the HDP-RNP complex composed of at least HEXIM1, PRKDC, XRCC5, XRCC6, paraspeckle proteins (SFPQ, NONO, PSPC1, RBM14, and MATR3) and NEAT1 RNA. {ECO:0000250|UniProtKB:P13010}. DOMAIN: The EEXXXDDL motif is required for the interaction with catalytic subunit PRKDC and its recruitment to sites of DNA damage. {ECO:0000250|UniProtKB:P13010}. +D3YX43 VSI10_MOUSE V-set and immunoglobulin domain-containing protein 10 558 60,522 Chain (1); Compositional bias (1); Disulfide bond (4); Domain (4); Glycosylation (7); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 427 447 Helical. {ECO:0000255}. TOPO_DOM 21 426 Extracellular. {ECO:0000255}.; TOPO_DOM 448 558 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q61048 WBP4_MOUSE WW domain-binding protein 4 (WBP-4) (Formin-binding protein 21) (WW domain-containing-binding protein 4) 376 42,137 Chain (1); Compositional bias (2); Domain (2); Modified residue (2); Sequence conflict (2); Zinc finger (1) FUNCTION: Involved in pre-mRNA splicing as a component of the spliceosome. May play a role in cross-intron bridging of U1 and U2 snRNPs in the mammalian A complex. {ECO:0000269|PubMed:9724750}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O75554}. Nucleus speckle {ECO:0000255|PROSITE-ProRule:PRU00130, ECO:0000269|PubMed:9724750}. SUBUNIT: Component of the spliceosome B complex (PubMed:9724750). Associated with U2 snRNPs. Binds splicing factors SNRPB, SNRPC and SF1 (PubMed:9724750). Interacts via the WW domains with the Pro-rich domains of KHDRBS1/SAM68 (PubMed:10748127). Interacts via the WW domains with the Pro-rich domains of WBP11 (By similarity). {ECO:0000250|UniProtKB:O75554, ECO:0000269|PubMed:10748127, ECO:0000269|PubMed:9724750}. DOMAIN: The WW domain recognizes the proline, glycine and methionine-rich (PGM) motif present in the splicing factors, as well as the Arg/Gly-rich-flanked Pro-rich domains found in several WW domain-binding proteins. +Q9EPK2 XRP2_MOUSE Protein XRP2 347 39,377 Alternative sequence (4); Chain (1); Domain (1); Initiator methionine (1); Lipidation (2); Nucleotide binding (2) FUNCTION: Acts as a GTPase-activating protein (GAP) involved in trafficking between the Golgi and the ciliary membrane. Involved in localization of proteins, such as NPHP3, to the cilium membrane by inducing hydrolysis of GTP ARL3, leading to the release of UNC119 (or UNC119B). Acts as a GTPase-activating protein (GAP) for tubulin in concert with tubulin-specific chaperone C, but does not enhance tubulin heterodimerization. Acts as guanine nucleotide dissociation inhibitor towards ADP-ribosylation factor-like proteins. PTM: Myristoylated on Gly-2; which may be required for membrane targeting. {ECO:0000305}.; PTM: Palmitoylated on Cys-3; which may be required for plasma membrane targeting. {ECO:0000305}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O75695}; Lipid-anchor {ECO:0000250|UniProtKB:O75695}; Cytoplasmic side {ECO:0000250|UniProtKB:O75695}. Cell projection, cilium {ECO:0000250|UniProtKB:O75695}. Note=Detected predominantly at the plasma membrane of rod and cone photoreceptors. Not detected in the nucleus. {ECO:0000250|UniProtKB:O75695}. SUBUNIT: Found in a complex with ARL3, RP2 and UNC119 (or UNC119B); RP2 induces hydrolysis of GTP ARL3 in the complex, leading to the release of UNC119 (or UNC119B). Interacts with ARL3; interaction is direct and stimulated with the activated GTP-bound form of ARL3 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Retina (at protein level). {ECO:0000269|PubMed:12417528}. +Q9CXE6 XRCC3_MOUSE DNA repair protein XRCC3 (X-ray repair cross-complementing protein 3) 349 38,446 Chain (1); Modified residue (1); Nucleotide binding (1) FUNCTION: Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA, thought to repair chromosomal fragmentation, translocations and deletions. Part of the RAD21 paralog protein complex CX3 which acts in the BRCA1-BRCA2-dependent HR pathway. Upon DNA damage, CX3 acts downstream of RAD51 recruitment; the complex binds predominantly to the intersection of the four duplex arms of the Holliday junction (HJ) and to junctions of replication forks. Involved in HJ resolution and thus in processing HR intermediates late in the DNA repair process; the function may be linked to the CX3 complex and seems to involve GEN1 during mitotic cell cycle progression. Part of a PALB2-scaffolded HR complex containing BRCA2 and RAD51C and which is thought to play a role in DNA repair by HR. Plays a role in regulating mitochondrial DNA copy number under conditions of oxidative stress in the presence of RAD51 and RAD51C (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Mitochondrion matrix {ECO:0000250}. Note=Accumulates in discrete nuclear foci prior to DNA damage, and these foci persist throughout the time course of DNA repair. {ECO:0000250}. SUBUNIT: Interacts with RAD51C and RAD51. Part of the CX3 complex consisting of RAD51C and XRCC3; the complex has a ring-like structure arranged into a flat disc around a central channel; CX3 can interact with RAD51 in vitro. Forms a complex with FANCD2, BRCA2 and phosphorylated FANCG. Interacts with SWSAP1 and ZSWIM7; involved in homologous recombination repair. Interacts directly with PALB2 which may serve as a scaffold for a HR complex containing PALB2, BRCA2, RAD51C, RAD51 and XRCC3 (By similarity). {ECO:0000250}. +Q8VCS3 XYLK_MOUSE Glycosaminoglycan xylosylkinase (EC 2.7.1.-) (Xylose kinase) 409 46,581 Active site (1); Binding site (4); Chain (1); Disulfide bond (4); Glycosylation (1); Metal binding (2); Nucleotide binding (1); Topological domain (2); Transmembrane (1) TRANSMEM 7 25 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 26 409 Lumenal. {ECO:0000255}. FUNCTION: Responsible for the 2-O-phosphorylation of xylose in the glycosaminoglycan-protein linkage region of proteoglycans thereby regulating the amount of mature GAG chains. Sulfated glycosaminoglycans (GAGs), including heparan sulfate and chondroitin sulfate, are synthesized on the so-called common GAG-protein linkage region (GlcUAbeta1-3Galbeta1-3Galbeta1-4Xylbeta1-O-Ser) of core proteins, which is formed by the stepwise addition of monosaccharide residues by the respective specific glycosyltransferases. Xylose 2-O-phosphorylation may influence the catalytic activity of B3GAT3 (GlcAT-I) which completes the precursor tetrasaccharide of GAG-protein linkage regions on which the repeating disaccharide region is synthesized. {ECO:0000250|UniProtKB:O75063}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:22900076}; Single-pass type II membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Little expression detected in the secretory stage enamel. Weak to moderate expression is observed in the gingivae and odontoblasts. Strong expression in maturation stage ameloblasts. {ECO:0000269|PubMed:21549343}. +Q61412 VSX2_MOUSE Visual system homeobox 2 (Ceh-10 homeodomain-containing homolog) (Homeobox protein CHX10) 361 39,436 Chain (1); Compositional bias (3); DNA binding (1); Domain (1); Motif (1) FUNCTION: Plays a significant role in the specification and morphogenesis of the sensory retina. May also participate in the development of the cells of the inner nuclear layer, particularly bipolar cells. {ECO:0000269|PubMed:8630490}. SUBCELLULAR LOCATION: Nucleus. TISSUE SPECIFICITY: Expressed throughout the anterior optic vesicle and all neuroblasts of the optic cup. In the mature retina Is restricted to the inner nuclear layer, in which its expression decreases from the outer to the inner margin. Also detected in regions of the developing thalamus, hindbrain, and ventral spinal cord. DISEASE: Note=Defects in Vsx2 are the cause of ocular retardation (OR(J)), a mouse disease characterized by microphthalmia, progressive destruction of the retina, and absence of the optic nerve. The OR(J) mutation is due to an OCHR (STOP) mutation. {ECO:0000269|PubMed:8630490}. +Q8R5M2 WNT9A_MOUSE Protein Wnt-9a (Protein Wnt-14) 365 40,388 Chain (1); Disulfide bond (11); Glycosylation (1); Lipidation (1); Signal peptide (1) FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors (Probable). Functions in the canonical Wnt/beta-catenin signaling pathway (By similarity). Required for normal timing of IHH expression during embryonic bone development, normal chondrocyte maturation and for normal bone mineralization during embryonic bone development (PubMed:16818445). Plays a redundant role in maintaining joint integrity (PubMed:16818445). {ECO:0000250|UniProtKB:O42280, ECO:0000269|PubMed:16818445, ECO:0000305}. PTM: Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition. {ECO:0000250|UniProtKB:P27467, ECO:0000250|UniProtKB:P56704}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:O14904}. Secreted {ECO:0000250|UniProtKB:O14904}. SUBUNIT: Forms a soluble 1:1 complex with AFM; this prevents oligomerization and is required for prolonged biological activity. The complex with AFM may represent the physiological form in body fluids. {ECO:0000250|UniProtKB:O14904}. TISSUE SPECIFICITY: Expressed in adult brain, lung, skeletal muscle, heart, and 17-day embryo. {ECO:0000269|PubMed:11836627}. +Q6P5F9 XPO1_MOUSE Exportin-1 (Exp1) (Chromosome region maintenance 1 protein homolog) 1071 123,093 Beta strand (11); Chain (1); Domain (1); Helix (65); Modified residue (7); Region (2); Repeat (10); Turn (10) FUNCTION: Mediates the nuclear export of cellular proteins (cargos) bearing a leucine-rich nuclear export signal (NES) and of RNAs. In the nucleus, in association with RANBP3, binds cooperatively to the NES on its target protein and to the GTPase Ran in its active GTP-bound form. Docking of this complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of the cargo from the export receptor. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Involved in U3 snoRNA transport from Cajal bodies to nucleoli. Binds to late precursor U3 snoRNA bearing a TMG cap (By similarity). {ECO:0000250, ECO:0000269|PubMed:20921223}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Nucleus, Cajal body {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Note=Located in the nucleoplasm, Cajal bodies and nucleoli. Shuttles between the nucleus/nucleolus and the cytoplasm (By similarity). {ECO:0000250}. SUBUNIT: Found in a U snRNA export complex with PHAX/RNUXA, NCBP1/CBP80, NCBP2/CBP20, RAN, XPO1 and m7G-capped RNA (PubMed:10786834). Component of a nuclear export receptor complex composed of KPNB1, RAN, SNUPN and XPO1. Found in a trimeric export complex with SNUPN, RAN and XPO1. Found in a nuclear export complex with RANBP3 and RAN. Found in a 60S ribosomal subunit export complex with NMD3, RAN, XPO1. Interacts with DDX3X, NMD3, NUPL2, NUP88, NUP214, RANBP3 and TERT. Interacts with NEMF (via its N-terminus). Interacts with the monomeric form of BIRC5/survivin deacetylated at 'Lys-129'. Interacts with SERTAD2; the interaction translocates SERTAD2 out of the nucleus. Interacts with ATF2. Interacts with SLC35G1 and STIM1. Interacts with DCAF8 (By similarity). Interacts with DTNBP1 and the interaction translocates DTNBP1 out of the nucleus (PubMed:20921223). Interacts with CPEB3 (By similarity). Interacts with HAX1 (By similarity). Interacts with BOK; translocates to the cytoplasm (By similarity). Interacts with HSP90AB1 (By similarity). {ECO:0000250|UniProtKB:O14980, ECO:0000269|PubMed:10786834, ECO:0000269|PubMed:20921223}. +Q61806 XL3C_MOUSE X-linked lymphocyte-regulated protein 3C (XLR-related protein A12) 226 26,179 Chain (1); Coiled coil (1); Sequence conflict (2) TISSUE SPECIFICITY: Expressed in lymphoid cells. +Q6P1B1 XPP1_MOUSE Xaa-Pro aminopeptidase 1 (EC 3.4.11.9) (Aminoacylproline aminopeptidase) (Cytosolic aminopeptidase P) (Soluble aminopeptidase P) (sAmp) (X-Pro aminopeptidase 1) (X-prolyl aminopeptidase 1, soluble) 623 69,591 Binding site (5); Chain (1); Metal binding (7); Modified residue (1); Sequence conflict (5) FUNCTION: Contributes to the degradation of bradykinin. Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9NQW7}. +Q9ESJ0 XPO4_MOUSE Exportin-4 (Exp4) 1151 129,979 Beta strand (5); Chain (1); Helix (61); Modified residue (2); Sequence conflict (2); Turn (5) FUNCTION: Mediates the nuclear export of proteins (cargos) with broad substrate specificity. In the nucleus binds cooperatively to its cargo and to the GTPase Ran in its active GTP-bound form. Docking of this trimeric complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of the cargo from the export receptor. XPO4 then return to the nuclear compartment and mediate another round of transport. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Shuttles between the nucleus and the cytoplasm. {ECO:0000250}. SUBUNIT: Found in a complex with XPO4, Ran and EIF5A. Found in a complex with XPO4, Ran and SMAD3. Interacts with SMAD3. Interacts with Ran and cargo proteins in a GTP-dependent manner (By similarity). {ECO:0000250}. +B1AVD1 XPP2_MOUSE Xaa-Pro aminopeptidase 2 (EC 3.4.11.9) (Membrane-bound aminopeptidase P) (Membrane-bound APP) (mAPP) (X-prolyl aminopeptidase 2) 674 76,434 Binding site (5); Chain (1); Frameshift (3); Glycosylation (4); Lipidation (1); Metal binding (7); Propeptide (1); Sequence conflict (5); Signal peptide (1) FUNCTION: Membrane-bound metalloprotease which catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro. May play a role in the metabolism of the vasodilator bradykinin. {ECO:0000250|UniProtKB:Q95333}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q99MA2}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q95333}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q95333}. SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:Q95333}. TISSUE SPECIFICITY: Strongly expressed in small intestine, heart and lung. Also detected in testis, skeletal muscle, spleen, liver, kidney, brain, uterus, eye, lymph node, thymus, stomach, prostate and bone marrow. {ECO:0000269|PubMed:12941294}. +B7ZMP1 XPP3_MOUSE Xaa-Pro aminopeptidase 3 (X-Pro aminopeptidase 3) (EC 3.4.11.9) (Aminopeptidase P3) (APP3) 506 56,677 Alternative sequence (2); Binding site (7); Chain (1); Metal binding (7); Region (1); Transit peptide (1) FUNCTION: Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Leu-Pro-Ala. Also shows low activity towards peptides with Ala or Ser at the P1 position. Promotes TNFRSF1B-mediated phosphorylation of MAPK8/JNK1 and MAPK9/JNK2, suggesting a function as an adapter protein for TNFRSF1B; the effect is independent of XPNPEP3 peptidase activity. May inhibit apoptotic cell death induced via TNF-TNFRSF1B signaling. {ECO:0000250|UniProtKB:Q9NQH7}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9NQH7}. Cytoplasm {ECO:0000250|UniProtKB:Q9NQH7}. Note=Mainly mitochondrial. Translocates to the cytoplasm following TNFRSF1B activation. {ECO:0000250|UniProtKB:Q9NQH7}. SUBUNIT: Homodimer. Interacts with TNFRSF1B/TNFR2 (activated) and TRAF2. {ECO:0000250|UniProtKB:Q9NQH7}. TISSUE SPECIFICITY: Expressed in brain, kidney, heart, liver, skeletal muscle and testis. {ECO:0000269|PubMed:20179356}. +Q9JJR2 XLR5C_MOUSE X-linked lymphocyte-regulated protein 5C 179 20,702 Chain (1); Coiled coil (1) SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26075718}. Chromosome {ECO:0000269|PubMed:26075718}. Note=May localize to synaptonemal complexes in meiotic spermatocytes. {ECO:0000269|PubMed:26075718}. TISSUE SPECIFICITY: Expressed in testis (at protein level). Also expressed in ovary. Not detected in other tissues tested. {ECO:0000269|PubMed:26075718}. +Q924Z6 XPO6_MOUSE Exportin-6 (Exp6) (Ran-binding protein 20) 1125 128,664 Alternative sequence (3); Chain (1); Domain (1); Initiator methionine (1); Modified residue (6); Sequence conflict (3) FUNCTION: Mediates the nuclear export of actin and profilin-actin complexes in somatic cells. {ECO:0000269|PubMed:22323606}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96QU8}. Cytoplasm {ECO:0000250|UniProtKB:Q96QU8}. Note=Shuttles between the nucleus and the cytoplasm. {ECO:0000250|UniProtKB:Q96QU8}. SUBUNIT: Found in a complex with XPO6, Ran, ACTB and PFN1. Interacts with ACTB. Interacts with ACTB in a RanGTP-dependent manner. {ECO:0000250|UniProtKB:Q96QU8}. +Q9DBR1 XRN2_MOUSE 5'-3' exoribonuclease 2 (EC 3.1.13.-) (Protein Dhm1) 951 108,687 Alternative sequence (1); Chain (1); Erroneous initiation (1); Modified residue (23); Sequence conflict (16); Zinc finger (1) FUNCTION: Possesses 5'->3' exoribonuclease activity. May promote the termination of transcription by RNA polymerase II. During transcription termination, cleavage at the polyadenylation site liberates a 5' fragment which is subsequently processed to form the mature mRNA and a 3' fragment which remains attached to the elongating polymerase. The processive degradation of this 3' fragment by this protein may promote termination of transcription. Binds to RNA polymerase II (RNAp II) transcription termination R-loops formed by G-rich pause sites (By similarity). {ECO:0000250|UniProtKB:Q9H0D6}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9H0D6}. SUBUNIT: Interacts with POLR2A and SMN1/SMN2. Interacts with CDKN2AIP and NKRF. Interacts with CDKN2AIPNL; the interaction is direct. Interacts with TRIM71 (via NHL repeats) in an RNA-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q9H0D6}. TISSUE SPECIFICITY: Expressed in the spleen, testis, heart, brain, lung, liver, skeletal muscle, and kidney. {ECO:0000269|PubMed:7885830}. +Q9CX47 XRCC2_MOUSE DNA repair protein XRCC2 (X-ray repair cross-complementing protein 2) 278 31,391 Chain (1); Modified residue (1) FUNCTION: Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA, thought to repair chromosomal fragmentation, translocations and deletions. Part of the Rad21 paralog protein complex BCDX2 which acts in the BRCA1-BRCA2-dependent HR pathway. Upon DNA damage, BCDX2 acts downstream of BRCA2 recruitment and upstream of RAD51 recruitment. BCDX2 binds predominantly to the intersection of the four duplex arms of the Holliday junction and to junction of replication forks. The BCDX2 complex was originally reported to bind single-stranded DNA, single-stranded gaps in duplex DNA and specifically to nicks in duplex DNA (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with RAD51D. Part of the BCDX2 complex consisting of RAD51B, RAD51C, RAD51D and XRCC2; the complex has a ring-like structure arranged into a flat disc around a central channel. In the absence of DNA, the BCDX2 subcomplex XRCC2:RAD51D formed a multimeric ring structure; in the presence of single-stranded DNA it formed a filamentous structure with the ssDNA (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed at low level in somatic tissues and at high level in testis. +Q3UVV9 VWA3A_MOUSE von Willebrand factor A domain-containing protein 3A 1148 130,106 Chain (1); Domain (2); Erroneous termination (1); Frameshift (1); Sequence conflict (2) +P01173 WAP_MOUSE Whey acidic protein (WAP) 134 14,423 Chain (1); Disulfide bond (6); Domain (2); Sequence conflict (7); Signal peptide (1) FUNCTION: Could be a protease inhibitor. May play an important role in mammary gland development and tissue remodeling. PTM: No phosphate or carbohydrate binding could be detected; however, both cholesterol and triglyceride are associated with the mouse protein. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Milk-specific; major protein component of milk whey. +Q8CBE3 WDR37_MOUSE WD repeat-containing protein 37 496 55,046 Chain (1); Erroneous initiation (1); Repeat (7); Sequence conflict (3) +Q7TMQ7 WDR91_MOUSE WD repeat-containing protein 91 748 83,421 Chain (1); Coiled coil (1); Modified residue (3); Repeat (7); Sequence conflict (1) FUNCTION: Functions as a negative regulator of the PI3 kinase/PI3K activity associated with endosomal membranes via BECN1, a core subunit of the PI3K complex. By modifying the phosphatidylinositol 3-phosphate/PtdInsP3 content of endosomal membranes may regulate endosome fusion, recycling, sorting and early to late endosome transport. It is for instance, required for the delivery of cargos like BST2/tetherin from early to late endosome and thereby participates indirectly to their degradation by the lysosome (By similarity). May play a role in meiosis (PubMed:27346680). {ECO:0000250|UniProtKB:A4D1P6, ECO:0000269|PubMed:27346680}. SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000250|UniProtKB:A4D1P6}; Peripheral membrane protein {ECO:0000250|UniProtKB:A4D1P6}. Late endosome membrane {ECO:0000250|UniProtKB:A4D1P6}. SUBUNIT: Interacts with WDR81; involved in early to late endosome cargo transport. Interacts with BECN1; negatively regulates the PI3 kinase/PI3K activity associated with endosomal membranes. {ECO:0000250|UniProtKB:A4D1P6}. +D3YZF7 VS10L_MOUSE V-set and immunoglobulin domain-containing protein 10-like 868 91,519 Chain (1); Compositional bias (1); Disulfide bond (2); Domain (2); Glycosylation (7); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 764 784 Helical. {ECO:0000255}. TOPO_DOM 28 763 Extracellular. {ECO:0000255}.; TOPO_DOM 785 868 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q8VCG3 WDR74_MOUSE WD repeat-containing protein 74 384 42,636 Chain (1); Modified residue (2); Region (1); Repeat (6) FUNCTION: Regulatory protein of the MTREX-exosome complex involved in the synthesis of the 60S ribosomal subunit. Participates in an early cleavage of the pre-rRNA processing pathway in cooperation with NVL (By similarity). Required for blastocyst formation, is necessary for RNA transcription, processing and/or stability during preimplantation development (PubMed:21799883). {ECO:0000250|UniProtKB:Q6RFH5, ECO:0000269|PubMed:21799883}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q6RFH5}. Nucleus {ECO:0000269|PubMed:21799883}. Note=Nucleolar location depends on active PolI transcription of pre-rRNA. {ECO:0000250|UniProtKB:Q6RFH5}. SUBUNIT: Isoform 1 interacts (through WDR repeats) with NVL; the interaction is independent of RNA or pre-60S ribosome particles. Isoform 2 does not interact with NVL. Interacts with MTREX; the interaction dissociation in a late stage of rRNA synthesis is required for appropriate maturation of pre-60S particles and depends on the ATPase activity of NVL. {ECO:0000250|UniProtKB:Q6RFH5}. +E9Q4P1 WDFY1_MOUSE WD repeat and FYVE domain-containing protein 1 (WD40- and FYVE domain-containing protein 1) 410 46,218 Chain (1); Erroneous initiation (1); Modified residue (1); Repeat (7); Sequence conflict (1); Zinc finger (1) FUNCTION: Positively regulates TLR3- and TLR4-mediated signaling pathways by bridging the interaction between TLR3 or TLR4 and TICAM1. Promotes TLR3/4 ligand-induced activation of transcription factors IRF3 and NF-kappa-B, as well as the production of IFN-beta and inflammatory cytokines (PubMed:25736436). {ECO:0000269|PubMed:25736436}. SUBCELLULAR LOCATION: Early endosome {ECO:0000250|UniProtKB:Q8IWB7}. SUBUNIT: Binds PtdIns3P in vitro with high specificity over other phosphoinositides (By similarity). Interacts (via WD repeat 2) with tyrosine-phosphorylated TLR3 (via TIR domain) in response to poly(I:C) (PubMed:25736436). Interacts with TLR4 in response to LPS (PubMed:25736436). Interacts with TICAM1 in response to poly(I:C) (PubMed:25736436). {ECO:0000250|UniProtKB:Q8IWB7, ECO:0000269|PubMed:25736436}. DOMAIN: The FYVE-type zinc finger domain mediates interactions with phosphatidylinositol 3-phosphate in membranes of early endosomes and penetrates bilayers. The FYVE domain insertion into PtdIns(3)P-enriched membranes is substantially increased in acidic conditions. The FYVE domain is required for its function in regulating TLR3 signaling. {ECO:0000250|UniProtKB:Q8IWB7}. +Q5NBU8 XAF1_MOUSE XIAP-associated factor 1 (BIRC4-binding protein) 273 31,117 Alternative sequence (1); Chain (1); Erroneous gene model prediction (1); Sequence caution (1); Zinc finger (1) FUNCTION: Seems to function as a negative regulator of members of the IAP (inhibitor of apoptosis protein) family. Inhibits anti-caspase activity of BIRC4. Induces cleavage and inactivation of BIRC4 independent of caspase activation. Mediates TNF-alpha-induced apoptosis and is involved in apoptosis in trophoblast cells. May inhibit BIRC4 indirectly by activating the mitochondrial apoptosis pathway. After translocation to mitochondria, promotes translocation of BAX to mitochondria and cytochrome c release from mitochondria. Seems to promote the redistribution of BIRC4 from the cytoplasm to the nucleus, probably independent of BIRC4 inactivation which seems to occur in the cytoplasm. The BIRC4-XAF1 complex mediates down-regulation of BIRC5/survivin; the process requires the E3 ligase activity of BIRC4. Seems to be involved in cellular sensitivity to the proapoptotic actions of TRAIL. May be a tumor suppressor by mediating apoptosis resistance of cancer cells (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Mitochondrion {ECO:0000250}. SUBUNIT: Interacts with BIRC1, BIRC2, BIRC3, BIRC4, BIRC7 and BIRC8. Part of an complex consisting of BIRC4, XAF1 and BIRC5; the complex formation requires IFN-beta stimulation. Interacts with RNF114, the interaction increases XAF1 stability and proapoptotic effects, and may regulate IFN signaling (By similarity). {ECO:0000250}. +Q9R0M1 XCR1_MOUSE Chemokine XC receptor 1 (Lymphotactin receptor) (SCM1 receptor) (XC chemokine receptor 1) (mXCR1) 322 37,308 Chain (1); Disulfide bond (1); Topological domain (8); Transmembrane (7) TRANSMEM 28 55 Helical; Name=1. {ECO:0000255}.; TRANSMEM 66 85 Helical; Name=2. {ECO:0000255}.; TRANSMEM 99 120 Helical; Name=3. {ECO:0000255}.; TRANSMEM 138 162 Helical; Name=4. {ECO:0000255}.; TRANSMEM 186 204 Helical; Name=5. {ECO:0000255}.; TRANSMEM 221 243 Helical; Name=6. {ECO:0000255}.; TRANSMEM 260 283 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 27 Extracellular. {ECO:0000255}.; TOPO_DOM 56 65 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 86 98 Extracellular. {ECO:0000255}.; TOPO_DOM 121 137 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 163 185 Extracellular. {ECO:0000255}.; TOPO_DOM 205 220 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 244 259 Extracellular. {ECO:0000255}.; TOPO_DOM 284 322 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for chemokines SCYC1 and SCYC2. Subsequently transduces a signal by increasing the intracellular calcium ions level. Receptor for XCL1/Lymphotactin (Probable). {ECO:0000305|PubMed:21300913}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed by dendritic cells from the thymus, slpeen, subcutaneous lymph nodes and mesenteric lymph nodes. {ECO:0000269|PubMed:21300913}. +Q9WTR6 XCT_MOUSE Cystine/glutamate transporter (Amino acid transport system xc-) (Solute carrier family 7 member 11) (xCT) 502 55,456 Chain (1); Modified residue (1); Topological domain (13); Transmembrane (12) TRANSMEM 44 64 Helical. {ECO:0000255}.; TRANSMEM 75 95 Helical. {ECO:0000255}.; TRANSMEM 114 134 Helical. {ECO:0000255}.; TRANSMEM 159 179 Helical. {ECO:0000255}.; TRANSMEM 190 210 Helical. {ECO:0000255}.; TRANSMEM 232 252 Helical. {ECO:0000255}.; TRANSMEM 266 286 Helical. {ECO:0000255}.; TRANSMEM 318 338 Helical. {ECO:0000255}.; TRANSMEM 366 386 Helical. {ECO:0000255}.; TRANSMEM 388 408 Helical. {ECO:0000255}.; TRANSMEM 423 443 Helical. {ECO:0000255}.; TRANSMEM 450 470 Helical. {ECO:0000255}. TOPO_DOM 1 43 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 65 74 Extracellular. {ECO:0000255}.; TOPO_DOM 96 113 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 135 158 Extracellular. {ECO:0000255}.; TOPO_DOM 180 189 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 211 231 Extracellular. {ECO:0000255}.; TOPO_DOM 253 265 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 287 317 Extracellular. {ECO:0000255}.; TOPO_DOM 339 365 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 387 387 Extracellular. {ECO:0000255}.; TOPO_DOM 409 422 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 444 449 Extracellular. {ECO:0000255}.; TOPO_DOM 471 502 Cytoplasmic. {ECO:0000255}. FUNCTION: Sodium-independent, high-affinity exchange of anionic amino acids with high specificity for anionic form of cystine and glutamate. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Disulfide-linked heterodimer with the amino acid transport protein SLC3A2/4F2hc. +P97789 XRN1_MOUSE 5'-3' exoribonuclease 1 (mXRN1) (EC 3.1.13.-) (Protein Dhm2) (Strand-exchange protein 1 homolog) 1719 194,307 Alternative sequence (3); Chain (1); Modified residue (1); Sequence conflict (6) FUNCTION: Major 5'-3' exoribonuclease involved in mRNA decay. Required for the 5'-3'-processing of the G4 tetraplex-containing DNA and RNA substrates. The kinetic of hydrolysis is faster for G4 RNA tetraplex than for G4 DNA tetraplex and monomeric RNA tetraplex. Binds to RNA and DNA. Plays a role in replication-dependent histone mRNA degradation (By similarity). {ECO:0000250|UniProtKB:Q8IZH2, ECO:0000269|PubMed:9049243}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9049243}. Note=Discrete foci at the inner surface of the cell membrane. SUBUNIT: Found in a mRNP complex with UPF1, UPF2, UPF3B and XRN1 (By similarity). Associates with alpha and beta tubulins (PubMed:14580940). Interacts with DIS3L2 (By similarity). Interacts with ZC3HAV1 in an RNA-dependent manner (By similarity). Interacts with ZFP36L1 (By similarity). Interacts with TRIM71 (via NHL repeats) in an RNA-dependent manner (By similarity). Interacts with YTHDC2 (via ANK repeats) (PubMed:29033321). {ECO:0000250|UniProtKB:Q8IZH2, ECO:0000269|PubMed:14580940, ECO:0000269|PubMed:29033321}. TISSUE SPECIFICITY: Expressed in heart, brain (spinal cord, dorsal root and superior cervical ganglia, neurons of the cerebrum and brain stem), peripheral nerve fibers in the skin and intestine, spleen, lung, liver, skeletal muscle, kidney and testis. {ECO:0000269|PubMed:14580940, ECO:0000269|PubMed:9049243, ECO:0000269|PubMed:9218715}. +Q3UR50 VW5B2_MOUSE von Willebrand factor A domain-containing protein 5B2 1248 133,414 Alternative sequence (4); Chain (1); Domain (2); Sequence caution (2) +Q8R2Z5 VWA1_MOUSE von Willebrand factor A domain-containing protein 1 (von Willebrand factor A domain-related protein) 415 44,709 Alternative sequence (1); Chain (1); Disulfide bond (1); Domain (3); Glycosylation (1); Modified residue (3); Mutagenesis (2); Sequence conflict (2); Signal peptide (1) FUNCTION: Promotes matrix assembly. {ECO:0000269|PubMed:18757743}. PTM: N-glycosylated. {ECO:0000269|PubMed:12062410}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000269|PubMed:12062410, ECO:0000269|PubMed:16407285, ECO:0000269|PubMed:18757743}. SUBUNIT: Homodimer or homomultimer; disulfide-linked. Interacts with HSPG2. {ECO:0000269|PubMed:12062410, ECO:0000269|PubMed:16407285}. TISSUE SPECIFICITY: Expressed at high levels in the chondrocytes. Detected in the vasculature of neural tissues, in basement membrane structures of the peripheral nervous system, in the apical ectodermal ridge of developing limb buds, and in skeletal and cardiac muscle (at protein level). {ECO:0000269|PubMed:12062410, ECO:0000269|PubMed:18314316}. +Q8C0M0 WDR59_MOUSE GATOR complex protein WDR59 (CUL4- and DDB1-associated WDR protein 12) (WD repeat-containing protein 59) 992 111,726 Alternative sequence (2); Chain (1); Domain (1); Erroneous initiation (2); Erroneous termination (1); Modified residue (4); Repeat (8); Sequence conflict (5) FUNCTION: As a component of the GATOR subcomplex GATOR2, functions within the amino acid-sensing branch of the TORC1 signaling pathway. Indirectly activates mTORC1 and the TORC1 signaling pathway through the inhibition of the GATOR1 subcomplex. It is negatively regulated by the upstream amino acid sensors SESN2 and CASTOR1. {ECO:0000250|UniProtKB:Q6PJI9}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q6PJI9}. SUBUNIT: Interacts with DDB1-CUL4A/B E3 ligase complexes (By similarity). Within the GATOR complex, component of the GATOR2 subcomplex, made of MIOS, SEC13, SEH1L, WDR24 and WDR59. The GATOR complex strongly interacts with RRAGA/RRAGC and RRAGB/RRAGC heterodimers (By similarity). The GATOR2 complex interacts with CASTOR2 and CASTOR1; the interaction is negatively regulated by arginine. The GATOR2 complex interacts with SESN1, SESN2 and SESN3; the interaction is negatively regulated by amino acids (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q6PJI9}. +Q8C761 WDR60_MOUSE WD repeat-containing protein 60 999 115,382 Chain (1); Coiled coil (3); Modified residue (1); Repeat (4); Sequence conflict (2) FUNCTION: May play a role in ciliogenesis. {ECO:0000250|UniProtKB:Q8WVS4}. SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000250|UniProtKB:Q8WVS4}. Note=Located at the base of the primary cilium in serum-starved fibroblasts. {ECO:0000250|UniProtKB:Q8WVS4}. SUBUNIT: Interacts with TCTEX1D2. {ECO:0000250|UniProtKB:Q8WVS4}. +O88384 VTI1B_MOUSE Vesicle transport through interaction with t-SNAREs homolog 1B (Vesicle transport v-SNARE protein Vti1-like 1) (Vti1-rp1) 232 26,713 Chain (1); Coiled coil (2); Helix (4); Initiator methionine (1); Modified residue (3); Region (2); Topological domain (2); Transmembrane (1) TRANSMEM 209 229 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 2 208 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 230 232 Vesicular. {ECO:0000255}. FUNCTION: V-SNARE that mediates vesicle transport pathways through interactions with t-SNAREs on the target membrane. These interactions are proposed to mediate aspects of the specificity of vesicle trafficking and to promote fusion of the lipid bilayers. {ECO:0000305|PubMed:15363411}. SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000250|UniProtKB:Q9UEU0}; Single-pass type IV membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000250|UniProtKB:Q9UEU0}; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:Q9UEU0}. Lysosome membrane {ECO:0000250|UniProtKB:Q9UEU0}. Cytoplasmic granule {ECO:0000250|UniProtKB:Q9UEU0}. Recycling endosome membrane {ECO:0000250|UniProtKB:Q9UEU0}; Single-pass type IV membrane protein {ECO:0000255}. SUBUNIT: Forms a SNARE complex with STX7, STX8 and VAMP8 which functions in the homotypic fusion of late endosomes. Component of the SNARE complex composed of STX7, STX8, VAMP7 and VIT1B that is required for heterotypic fusion of late endosomes with lysosomes (PubMed:11786915, PubMed:15363411). May interact with STX17. Interacts with CLINT1 (By similarity). {ECO:0000250|UniProtKB:Q9UEU0, ECO:0000269|PubMed:11786915, ECO:0000269|PubMed:15363411}. TISSUE SPECIFICITY: Broadly expressed. +Q8BH89 WF15A_MOUSE WAP four-disulfide core domain protein 15A 80 9,062 Chain (1); Disulfide bond (4); Domain (1); Signal peptide (1) FUNCTION: Antibacterial protein. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +F6ULY1 WFC6B_MOUSE WAP four-disulfide core domain protein 6B (Putative protease inhibitor WAP6B) 148 17,169 Chain (1); Disulfide bond (7); Domain (2); Erroneous initiation (3); Sequence conflict (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +P56695 WFS1_MOUSE Wolframin 890 100,579 Chain (1); Compositional bias (3); Glycosylation (2); Modified residue (4); Sequence conflict (1); Topological domain (1); Transmembrane (11) TRANSMEM 314 334 Helical. {ECO:0000255}.; TRANSMEM 340 360 Helical. {ECO:0000255}.; TRANSMEM 402 422 Helical. {ECO:0000255}.; TRANSMEM 427 447 Helical. {ECO:0000255}.; TRANSMEM 465 485 Helical. {ECO:0000255}.; TRANSMEM 496 516 Helical. {ECO:0000255}.; TRANSMEM 529 549 Helical. {ECO:0000255}.; TRANSMEM 563 583 Helical. {ECO:0000255}.; TRANSMEM 589 609 Helical. {ECO:0000255}.; TRANSMEM 632 652 Helical. {ECO:0000255}.; TRANSMEM 870 890 Helical. {ECO:0000255}. TOPO_DOM 653 869 Lumenal. {ECO:0000255}. FUNCTION: Participates in the regulation of cellular Ca(2+) homeostasis, at least partly, by modulating the filling state of the endoplasmic reticulum Ca(2+) store. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Highly expressed in the developing lens. {ECO:0000269|PubMed:23531866}. +P97765 WBP2_MOUSE WW domain-binding protein 2 (WBP-2) 261 28,032 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (1); Modified residue (2); Motif (2); Mutagenesis (3) FUNCTION: Acts as transcriptional coactivator of estrogen and progesterone receptors (ESR1 and PGR) upon hormone activation. In presence of estrogen, binds to ESR1-responsive promoters. Required for YAP1 coactivation function on PGR activity. Synergizes with WBP2 in enhancing PGR activity (By similarity). Modulates expression of post-synaptic scaffolding proteins via regulation of ESR1, ESR2 and PGR (PubMed:26881968). {ECO:0000250|UniProtKB:Q969T9, ECO:0000269|PubMed:26881968}. PTM: Phosphorylated in repsonse to EGF as well as estrogen and progesterone hormones. Tyr-192 and Tyr-231 are phosphorylated by YES and SRC inducing nuclear translocation. {ECO:0000250|UniProtKB:Q969T9}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q969T9}. Nucleus {ECO:0000250|UniProtKB:Q969T9}. Note=Translocates from cytoplasm to nucleus when phosphorylated. {ECO:0000250|UniProtKB:Q969T9}. SUBUNIT: Binds to the WW domain of YAP1, WWP1 and WWP2 (By similarity) (PubMed:7644498). Interacts with NEDD4 (PubMed:11042109). Interacts with ESR1 and UBE3A (By similarity). {ECO:0000250|UniProtKB:Q969T9, ECO:0000269|PubMed:11042109, ECO:0000269|PubMed:7644498}. DOMAIN: The PPxY motif 1 mediates interaction with NEDD4 (PubMed:11042109). The PPxY motif 2 is required for the coactivation function (By similarity). {ECO:0000250|UniProtKB:Q969T9, ECO:0000269|PubMed:11042109}. TISSUE SPECIFICITY: Expressed in the ear and the eye (PubMed:26881968). Isoform 1 is expressed in brain, inner ear and organ of Corti. Isoform 2 is only detected in brain (PubMed:26881968). {ECO:0000269|PubMed:26881968}. +Q8BFQ4 WDR82_MOUSE WD repeat-containing protein 82 313 35,079 Chain (1); Repeat (6); Sequence conflict (1) FUNCTION: Regulatory component of the SET1 complex implicated in the tethering of this complex to transcriptional start sites of active genes. Facilitates histone H3 'Lys-4' methylation via recruitment of the SETD1A or SETD1B to the 'Ser-5' phosphorylated C-terminal domain (CTD) of RNA polymerase II large subunit (POLR2A). Component of PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. Possible role in telomere length maintenance and in mRNA processing (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Associates with chromatin. {ECO:0000250}. SUBUNIT: Component of the SET1 complex, at least composed of the catalytic subunit (SETD1A or SETD1B), WDR5, WDR82, RBBP5, ASH2L/ASH2, CXXC1/CFP1, HCFC1 and DPY30. Component of the PTW/PP1 phosphatase complex, composed of PPP1R10/PNUTS, TOX4, WDR82 and PPP1CA or PPP1CB or PPP1CC. Associated with multiple protein complexes including an RNA polymerase II complex, MLL3/MLL4 complex and a chaperonin-containing TCP1 complex. Interacts with CUL4B. Interacts with RBBP5 and SETD1B. Interacts with SETD1A (via RRM domain). Interacts with POLR2B. Interacts with hyperphosphorylated C-terminal domain (CTD) of RNA polymerase II large subunit (POLR2A). Binds specifically to CTD heptad repeats phosphorylated on 'Ser-5' of each heptad. SETD1A enhances its interaction with POLR2A. Interacts with PPP1R10/PNUTS. Interacts with PPP1CA in the presence of PPP1R10/PNUTS (By similarity). {ECO:0000250}. +P62810 WFD18_MOUSE WAP four-disulfide core domain protein 18 (Extracellular peptidase inhibitor) (Protein WDNM1) 74 7,787 Chain (1); Domain (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Could have proteinase inhibiting capacity. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q9DAJ4 WDR83_MOUSE WD repeat domain-containing protein 83 (Mitogen-activated protein kinase organizer 1) (MAPK organizer 1) 315 34,444 Alternative sequence (4); Chain (1); Repeat (7); Sequence conflict (6) FUNCTION: Molecular scaffold protein for various multimeric protein complexes. Involved in response to hypoxia by acting as a negative regulator of HIF1A/HIF-1-alpha via its interaction with EGLN3/PHD3. May promote degradation of HIF1A. May act by recruiting signaling complexes to a specific upstream activator (By similarity). Also acts as a module in the assembly of a multicomponent scaffold for the ERK pathway, linking ERK responses to specific agonists. At low concentrations it enhances ERK activation, whereas high concentrations lead to the inhibition of ERK activation. May also be involved in pre-mRNA splicing. {ECO:0000250, ECO:0000269|PubMed:15118098}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Predominantly cytoplasmic. Partially nuclear. {ECO:0000250}. SUBUNIT: Interacts with EGLN3/PHD3. Identified in the spliceosome C complex (By similarity). Interacts with ERK signaling proteins MAP2K1/MEK1, MAP2K2/MEK2, LAMTOR3, ARAF/Raf-1, MAPK1/ERK2 and MAPK3/ERK1. {ECO:0000250, ECO:0000269|PubMed:15118098}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15118098}. +Q14AE4 WFDC3_MOUSE WAP four-disulfide core domain protein 3 (Putative protease inhibitor WAP14) 130 13,718 Chain (1); Disulfide bond (8); Domain (2); Glycosylation (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +O35468 WNT9B_MOUSE Protein Wnt-9b (Protein Wnt-14b) (Protein Wnt-15) 359 38,982 Chain (1); Disulfide bond (11); Glycosylation (1); Lipidation (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors (Probable). Functions in the canonical Wnt/beta-catenin signaling pathway (PubMed:22461561, PubMed:16054034, PubMed:17537789). Required for normal embryonic kidney development, and for normal development of the urogenital tract, including uterus and part of the oviduct and the upper vagina in females, and epididymis and vas deferens in males (PubMed:16054034). Activates a signaling cascade in the metanephric mesenchyme that induces tubulogenesis (PubMed:16054034, PubMed:17537789). Acts upstream of WNT4 in the signaling pathways that mediate development of kidney tubules and the Muellerian ducts (PubMed:16054034). Plays a role in cranofacial development and is required for normal fusion of the palate during embryonic development (PubMed:16054034, PubMed:22461561, PubMed:25257647). {ECO:0000269|PubMed:16054034, ECO:0000269|PubMed:17537789, ECO:0000269|PubMed:22461561, ECO:0000269|PubMed:25257647, ECO:0000305}. PTM: Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition. {ECO:0000250|UniProtKB:P27467, ECO:0000250|UniProtKB:P56704}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:O14905}. Secreted {ECO:0000250|UniProtKB:O14905}. SUBUNIT: Forms a soluble 1:1 complex with AFM; this prevents oligomerization and is required for prolonged biological activity. The complex with AFM may represent the physiological form in body fluids. Component of the Wnt-Fzd-LRP5-LRP6 signaling complex that contains a WNT protein, a FZD protein and LRP5 or LRP6. Interacts directly in the complex with LRP6. Interacts with PKD1 (via extracellular domain). {ECO:0000250|UniProtKB:O14905}. DISEASE: Note=Spontaneous insertion of a retrotransposon in the Wnt9b promoter region causes reduced Wnt9b expression. Decreased Wnt9b expression is correlated with increased incidence of cleft lip and palate. {ECO:0000269|PubMed:25257647}. +Q811B1 XYLT1_MOUSE Xylosyltransferase 1 (EC 2.4.2.26) (Peptide O-xylosyltransferase 1) (Xylosyltransferase I) 953 107,298 Binding site (3); Chain (1); Disulfide bond (6); Glycosylation (3); Mutagenesis (1); Region (3); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 18 38 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 17 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 39 953 Lumenal. {ECO:0000255}. Glycan metabolism; chondroitin sulfate biosynthesis. Glycan metabolism; heparan sulfate biosynthesis. FUNCTION: Catalyzes the first step in the biosynthesis of chondroitin sulfate and dermatan sulfate proteoglycans, such as DCN. Transfers D-xylose from UDP-D-xylose to specific serine residues of the core protein. Required for normal maturation of chondrocytes during bone development, normal onset of ossification and normal embryonic and postnatal skeleton development, especially of the long bones. {ECO:0000269|PubMed:24161523}. PTM: Contains 7 disulfide bonds. {ECO:0000250|UniProtKB:Q86Y38}.; PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q86Y38}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:24161523}; Single-pass type II membrane protein {ECO:0000305}. SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q86Y38}. TISSUE SPECIFICITY: Detected in brain, spleen, kidney and testis, and at low levels in skeletal muscle. {ECO:0000269|PubMed:17189265, ECO:0000269|PubMed:17517600}. +Q9CX97 WDR55_MOUSE WD repeat-containing protein 55 388 42,611 Chain (1); Compositional bias (1); Modified residue (1); Repeat (7) FUNCTION: Nucleolar protein that acts as a modulator of rRNA synthesis. Plays a central role during organogenesis. {ECO:0000269|PubMed:18769712}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:18769712}. Cytoplasm {ECO:0000269|PubMed:18769712}. +P61965 WDR5_MOUSE WD repeat-containing protein 5 (BMP2-induced 3-kb gene protein) (WD repeat-containing protein BIG-3) 334 36,588 Beta strand (30); Chain (1); Cross-link (3); Initiator methionine (1); Modified residue (2); Repeat (7); Site (4); Turn (8) FUNCTION: Contributes to histone modification. May position the N-terminus of histone H3 for efficient trimethylation at 'Lys-4'. As part of the MLL1/MLL complex it is involved in methylation and dimethylation at 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. May regulate osteoblasts differentiation (By similarity). {ECO:0000250, ECO:0000269|PubMed:11551928}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15860628}. SUBUNIT: Interacts with PAXBP1; the interaction is direct and links a WDR5-containing histone methyltransferase complex to PAX7 and PAX3. Interacts with HCFC1. Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4. Component of the SET1 complex, at least composed of the catalytic subunit (SETD1A or SETD1B), WDR5, WDR82, RBBP5, ASH2L/ASH2, CXXC1/CFP1, HCFC1 and DPY30. Core component of several methyltransferase-containing complexes including MLL1/MLL, MLL2/3 (also named ASCOM complex) and MLL4/WBP7. Each complex is at least composed of ASH2L, RBBP5, WDR5, DPY30, one or more specific histone methyltransferases (KMT2A/MLL1, KMT2D/MLL2, KMT2C/MLL3 and KMT2B/MLL4), and the facultative components PAGR1, BAP18, CHD8, E2F6, HCFC1, HCFC2, HSP70, INO80C, KDM6A, KANSL1, LAS1L, MAX, MCRS1, MEN1, MGA, MYST1/MOF, NCOA6, PAXIP1/PTIP, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9, TEX10 and alpha- and beta-tubulin. Component of the NSL complex at least composed of MOF/KAT8, KANSL1, KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT, WDR5 and HCFC1. Interacts with KMT2A/MLL1 and RBBP5; the interaction is direct. Component ofthe ADA2A-containing complex (ATAC), composed of KAT14, KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1. In the complex, it probably interacts directly with KAT2A, MBIP and KAT14. Interacts with histone H3. Interacts with SETD1A. Part of a complex composed at least of ASCL2, EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; this complex may have a histone H3-specific methyltransferase activity. Interacts with PER1. {ECO:0000269|PubMed:21335234, ECO:0000269|PubMed:22862948, ECO:0000269|PubMed:23178126}. TISSUE SPECIFICITY: Expressed in liver (at protein level). Detected in brain, testis and kidney. {ECO:0000269|PubMed:15860628}. +Q8BND3 WDR35_MOUSE WD repeat-containing protein 35 1181 133,991 Alternative sequence (1); Chain (1); Repeat (5); Sequence conflict (3) FUNCTION: May promote CASP3 activation and TNF-stimulated apoptosis (By similarity). Component of the IFT complex A (IFT-A), a complex required for retrograde ciliary transport. Required for ciliogenesis. {ECO:0000250, ECO:0000269|PubMed:21473986}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:21473986}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:21473986}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:21473986}. Note=Immunofluorescence studies in IMCD3 cells show that Wdr35 accumulates at and around centrosomes and basal bodies of serum-starved cells, with fainter punctate staining along the cilia axoneme. SUBUNIT: Component of the IFT complex A (IFT-A). Interacts with IFT43 (By similarity). {ECO:0000250}. +Q91V09 WDR13_MOUSE WD repeat-containing protein 13 485 53,664 Chain (1); Modified residue (5); Repeat (5) SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +P70315 WASP_MOUSE Wiskott-Aldrich syndrome protein homolog (WASp) 520 54,192 Chain (1); Compositional bias (9); Domain (3); Modified residue (3); Repeat (2) FUNCTION: Effector protein for Rho-type GTPases that regulates actin filament reorganization via its interaction with the Arp2/3 complex. Important for efficient actin polymerization. Possible regulator of lymphocyte and platelet function. Mediates actin filament reorganization and the formation of actin pedestals upon infection by pathogenic bacteria. In addition to its role in the cytoplasmic cytoskeleton, also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA. Promotes homologous recombination (HR) repair in response to DNA damage by promoting nuclear actin polymerization, leading to drive motility of double-strand breaks (DSBs). {ECO:0000250|UniProtKB:P42768}. PTM: Phosphorylated at Tyr-293 by FYN and HCK, inducing WAS effector activity after TCR engagement. Phosphorylation at Tyr-293 enhances WAS activity in promoting actin polymerization and filopodia formation. {ECO:0000250|UniProtKB:P42768}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P42768}. Nucleus {ECO:0000250|UniProtKB:P42768}. SUBUNIT: Binds the Arp2/3 complex (By similarity). Interacts with CDC42, RAC, NCK, HCK, FYN, SRC kinase FGR, BTK, ABL1, PSTPIP1, WIP, and to the p85 subunit of PLC-gamma (PubMed:9488710). Interacts (via C-terminus) with ALDOA (By similarity). Interacts with NCK1 (via SH3 domains) (PubMed:8910519). {ECO:0000250|UniProtKB:P42768, ECO:0000269|PubMed:8910519, ECO:0000269|PubMed:9488710}. DOMAIN: The WH1 (Wasp homology 1) domain may bind a Pro-rich ligand.; DOMAIN: The CRIB (Cdc42/Rac-interactive-binding) region binds to the C-terminal WH2 domain in the autoinhibited state of the protein. Binding of Rho-type GTPases to the CRIB induces a conformation change and leads to activation. +D3YYM4 WDR72_MOUSE WD repeat-containing protein 72 1114 124,410 Chain (1); Modified residue (2); Repeat (7) FUNCTION: Plays a major role in formation of tooth enamel (PubMed:25008349, PubMed:26247047). Specifically required during the maturation phase of amelogenesis for normal formation of the enamel matrix and clearance of enamel proteins (PubMed:25008349, PubMed:26247047). May be involved in localization of the calcium transporter SLC24A4 to the ameloblast cell membrane (PubMed:26247047). {ECO:0000269|PubMed:25008349, ECO:0000269|PubMed:26247047}. SUBCELLULAR LOCATION: Cytoplasmic vesicle {ECO:0000269|PubMed:25008349}. TISSUE SPECIFICITY: Expressed in maturation stage ameloblasts (at protein level) (PubMed:19853237, PubMed:25008349). +A2A5H7 WFD11_MOUSE Protein WFDC11 82 9,601 Chain (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q6VNB8 WDFY3_MOUSE WD repeat and FYVE domain-containing protein 3 (Beach domain, WD repeat and FYVE domain-containing protein 1) (BWF1) 3508 392,338 Alternative sequence (2); Chain (1); Compositional bias (2); Domain (2); Frameshift (1); Modified residue (5); Motif (1); Region (3); Repeat (5); Zinc finger (1) FUNCTION: Required for selective macroautophagy (aggrephagy). Acts as an adapter protein by linking specific proteins destined for degradation to the core autophagic machinery members, such as the ATG5-ATG12-ATG16L E3-like ligase, SQSTM1 and LC3. Involved in the formation and autophagic degradation of cytoplasmic ubiquitin-containing inclusions (p62 bodies, ALIS/aggresome-like induced structures) (By similarity). Important for normal brain development (PubMed:25198012, PubMed:27648578). Essential for the formation of axonal tracts throughout the brain and spinal cord, including the formation of the major forebrain commissures. Involved in the ability of neural cells to respond to guidance cues. Required for cortical neurons to respond to the trophic effects of netrin-1/NTN1 (PubMed:27648578). Regulates Wnt signaling through the removal of DVL3 aggregates, likely in an autophagy-dependent manner. This process may be important for the determination of brain size during embryonic development (By similarity). May regulate osteoclastogenesis by acting on the TNFSF11/RANKL - TRAF6 pathway (PubMed:27330028). After cytokinetic abscission, involved in midbody remnant degradation. In vitro strongly binds to phosphatidylinositol 3-phosphate (PtdIns3P) (By similarity). {ECO:0000250|UniProtKB:Q8IZQ1, ECO:0000269|PubMed:25198012, ECO:0000269|PubMed:27330028, ECO:0000269|PubMed:27648578}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8IZQ1}. Cytoplasm, cytosol {ECO:0000269|PubMed:15342963, ECO:0000269|PubMed:25198012, ECO:0000269|PubMed:27330028}. Nucleus, PML body {ECO:0000250|UniProtKB:Q8IZQ1}. Membrane {ECO:0000269|PubMed:27648578}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8IZQ1}; Cytoplasmic side {ECO:0000305}. Perikaryon {ECO:0000269|PubMed:27648578}. Cell projection, axon {ECO:0000269|PubMed:27648578}. Note=Relocalization from the nucleus to the cytosol is stimulated by cellular stress, such as starvation or proteasomal inhibition. In the cytosol of starved cells, colocalizes with autophagic structures. This redistribution is dependent on p62/SQSTM1. When nuclear export is blocked by treatment with leptomycin B, accumulates in nuclear bodies, that completely or partially colocalize with promyelocytic leukemia (PML) bodies (By similarity). Localizes throughout neurons, including within axons. In neurons, enriched in the light membrane fraction along with the synaptosomal membrane protein synaptophysin and the membrane-bound form of LC3/MAP1LC3A/MAP1LC3B, called LC3-II, a classic marker for autophagic vesicles (PubMed:27648578). {ECO:0000250|UniProtKB:Q8IZQ1, ECO:0000269|PubMed:27648578}. SUBUNIT: Directly interacts with ATG5 and associates with the ATG12-ATG5-ATG16L complex. Interacts with p62/SQSTM1. Directly interacts with GABARAP, GABARAPL1 and GABARAPL2; the interaction with GABARAP is required for WDFY3 recruitment to MAP1LC3B-positive p62/SQSTM1 bodies. Weakly interacts with MAP1LC3C; this interaction is direct. Does not interact with MAP1LC3A, nor MAP1LC3B (By similarity). Interacts with TRAF6 (PubMed:27330028). {ECO:0000250|UniProtKB:Q8IZQ1, ECO:0000269|PubMed:27330028}. DOMAIN: The LIR (LC3-interacting region) motif mediates the interaction with MAP1LC3C and other ATG8 family members. {ECO:0000250|UniProtKB:Q8IZQ1}.; DOMAIN: The FYVE domain mediates binding to phosphatidylinositol 3-phosphate (PtdIns3P). {ECO:0000250|UniProtKB:Q8IZQ1}. TISSUE SPECIFICITY: Widely expressed, with high levels in the brain (at protein level) (PubMed:15342963, PubMed:15292400, PubMed:27648578). In the brain, expressed by both neuronal and non-neuronal cells (PubMed:27648578). Expressed in bones, in the periosteum, cartilage, growth plate, trabeculae of the primary spongiosa, and scattered hematopoietic cells within the medullary cavity. Tends to be expressed at lower levels in the hypertrophic zone compared to trabeculae. Expressed in osteoblasts, osteoclasts and bone-marrow derived macrophages (PubMed:27330028). {ECO:0000269|PubMed:15292400, ECO:0000269|PubMed:15342963, ECO:0000269|PubMed:27330028, ECO:0000269|PubMed:27648578}. +P22724 WNT4_MOUSE Protein Wnt-4 351 39,050 Chain (1); Disulfide bond (11); Glycosylation (2); Lipidation (1); Signal peptide (1) FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors (Probable). Plays an important role in the embryonic development of the urogenital tract and the lung (PubMed:7990960, PubMed:9989404, PubMed:16054034, PubMed:17537789, PubMed:19830824, PubMed:26321050). Required for normal mesenchyme to epithelium transition during embryonic kidney development (PubMed:7990960, PubMed:16054034, PubMed:17537789, PubMed:19830824). Required for the formation of early epithelial renal vesicles during kidney development (PubMed:16054034). Required for normal formation of the Mullerian duct in females, and normal levels of oocytes in the ovaries (PubMed:9989404, PubMed:19830824). Required for normal down-regulation of 3 beta-hydroxysteroid dehydrogenase in the ovary (PubMed:9989404). Required for normal lung development and for normal patterning of trachael cartilage rings (PubMed:26321050). {ECO:0000269|PubMed:16054034, ECO:0000269|PubMed:17537789, ECO:0000269|PubMed:19830824, ECO:0000269|PubMed:26321050, ECO:0000269|PubMed:7990960, ECO:0000269|PubMed:9989404, ECO:0000305}. PTM: Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition. {ECO:0000250|UniProtKB:P27467, ECO:0000250|UniProtKB:P56704}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SUBUNIT: Interacts with PORCN (PubMed:10866835). Interacts with PKD1 (By similarity). {ECO:0000250|UniProtKB:P56705, ECO:0000269|PubMed:10866835}. TISSUE SPECIFICITY: In adults in lung and brain. {ECO:0000269|PubMed:2279700}. +P22727 WNT6_MOUSE Protein Wnt-6 364 39,656 Chain (1); Disulfide bond (11); Glycosylation (2); Lipidation (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors. Probable developmental protein. May be a signaling molecule which affects the development of discrete regions of tissues. Is likely to signal over only few cell diameters. PTM: Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition. {ECO:0000250|UniProtKB:P27467, ECO:0000250|UniProtKB:P56704}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SUBUNIT: Interacts with PORCN. {ECO:0000269|PubMed:10866835}. TISSUE SPECIFICITY: Detected in ileum, colon and stomach (at protein level). {ECO:0000269|PubMed:22370641}. +Q3TNA1 XYLB_MOUSE Xylulose kinase (Xylulokinase) (EC 2.7.1.17) 551 59,544 Binding site (6); Chain (1); Erroneous initiation (1); Nucleotide binding (1) FUNCTION: Phosphorylates D-xylulose to produce D-xylulose 5-phosphate, a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. +Q9D806 VSTM5_MOUSE V-set and transmembrane domain-containing protein 5 199 22,564 Chain (1); Domain (1); Glycosylation (3); Region (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 147 167 Helical. {ECO:0000255}. TOPO_DOM 28 146 Extracellular. {ECO:0000255}.; TOPO_DOM 168 199 Cytoplasmic. {ECO:0000255}. FUNCTION: Cell adhesion-like membrane protein of the central nervous system (CNS) which modulates both the position and complexity of central neurons by altering their membrane morphology and dynamics. Involved in the formation of neuronal dendrites and protrusions including dendritic filopodia. In synaptogenesis, regulates synapse formation by altering dendritic spine morphology and actin distribution. Promotes formation of unstable neuronal spines such as thin and branched types. Regulates neuronal morphogenesis and migration during cortical development in the brain. {ECO:0000269|PubMed:27683913}. PTM: N-glycosylated. {ECO:0000269|PubMed:27683913}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27683913}; Single-pass type I membrane protein {ECO:0000305}. Cell projection, dendrite {ECO:0000269|PubMed:27683913}. Cell projection, axon {ECO:0000269|PubMed:27683913}. SUBUNIT: Can homooligomerize through cis interactions within the same cell membrane. {ECO:0000269|PubMed:27683913}. TISSUE SPECIFICITY: Highly expressed in the central nervous system (CNS), with the highest expression in thalamus, hippocampus, cerebrum, midbrain and spinal cord. Also highly expressed in stomach, kidney and small intestine. {ECO:0000269|PubMed:27683913}. +Q8C8N3 VWC2_MOUSE Brorin (Brain-specific chordin-like protein) (CR (chordin-like cysteine-rich) domain-containing adhesive protein) (Cradin) (von Willebrand factor C domain-containing protein 2) 324 35,383 Chain (1); Domain (2); Erroneous initiation (1); Motif (1); Signal peptide (1) FUNCTION: BMP antagonist which may play a role in neural development. Promotes cell adhesion. {ECO:0000269|PubMed:17400546, ECO:0000269|PubMed:18757743}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane. Cell junction, synapse {ECO:0000305}. SUBUNIT: Peripherally associated with AMPAR complex. AMPAR complex consists of an inner core made of 4 pore-forming GluA/GRIA proteins (GRIA1, GRIA2, GRIA3 and GRIA4) and 4 major auxiliary subunits arranged in a twofold symmetry. One of the two pairs of distinct binding sites is occupied either by CNIH2, CNIH3 or CACNG2, CACNG3. The other harbors CACNG2, CACNG3, CACNG4, CACNG8 or GSG1L. This inner core of AMPAR complex is complemented by outer core constituents binding directly to the GluA/GRIA proteins at sites distinct from the interaction sites of the inner core constituents. Outer core constituents include at least PRRT1, PRRT2, CKAMP44/SHISA9, FRRS1L and NRN1. The proteins of the inner and outer core serve as a platform for other, more peripherally associated AMPAR constituents, including VWC2. Alone or in combination, these auxiliary subunits control the gating and pharmacology of the AMPAR complex and profoundly impact their biogenesis and protein processing. {ECO:0000269|PubMed:22632720}. TISSUE SPECIFICITY: Predominantly expressed in the brain (at protein level). It is expressed in the neurons but not the glial cells. {ECO:0000269|PubMed:17400546, ECO:0000269|PubMed:18757743, ECO:0000269|PubMed:22632720}. +Q9D2J4 VSIG1_MOUSE V-set and immunoglobulin domain-containing protein 1 (Cell surface A33 antigen) (Glycoprotein A34) 407 44,015 Alternative sequence (1); Chain (1); Compositional bias (1); Disulfide bond (2); Domain (2); Glycosylation (3); Modified residue (2); Sequence conflict (6); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 235 255 Helical. {ECO:0000255}. TOPO_DOM 23 234 Extracellular. {ECO:0000255}.; TOPO_DOM 256 407 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q65Z40 WAPL_MOUSE Wings apart-like protein homolog (Dioxin-inducible factor 2) (DIF-2) (WAPL cohesin release factor) 1200 134,070 Chain (1); Coiled coil (2); Domain (1); Erroneous initiation (1); Modified residue (11); Motif (3); Region (1); Sequence conflict (1) FUNCTION: Regulator of sister chromatid cohesion in mitosis which negatively regulates cohesin association with chromatin. Involved in both sister chromatid cohesion during interphase and sister-chromatid resolution during early stages of mitosis. Couples DNA replication to sister chromatid cohesion. Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Associates with chromatin through the cohesin complex during interphase. Released in the cytoplasm from nuclear envelope breakdown until anaphase, it reaccumulates in nucleus at telophase (By similarity). {ECO:0000250}. SUBUNIT: Interacts with the cohesin complex throughout the cell cycle; interacts with both chromatin-bound and soluble pools of the complex. Interacts with RAD21; the interaction is direct (By similarity). Interacts with PDS5A; the interaction is direct, cohesin-dependent and competitive with CDCA5/SORORIN (By similarity). Interacts (via FGF motifs) with PDS5B; the interaction is direct (By similarity). Interacts with a SMC1 protein (SMC1A or SMC1B) and SMC3 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in large pachytene spermatocytes of testis. Down-regulated by dioxin in testis. {ECO:0000269|PubMed:15620708}. +Q8BUB4 WDFY2_MOUSE WD repeat and FYVE domain-containing protein 2 (Propeller-FYVE protein) (Prof) (WD40- and FYVE domain-containing protein 2) 400 45,094 Chain (1); Repeat (7); Sequence conflict (1); Zinc finger (1) FUNCTION: Acts in an adapter protein-like fashion to mediate the interaction between the kinase PRKCZ and its substrate VAMP2 and increases the PRKCZ-dependent phosphorylation of VAMP2 (By similarity). Positively regulates adipocyte differentiation, by facilitating the phosphorylation and thus inactivation of the anti-adipogenetic transcription factor FOXO1 by the kinase AKT1 (PubMed:18388859). Plays a role in endosomal control of AKT2 signaling; required for insulin-stimulated AKT2 phosphorylation and glucose uptake and insulin-stimulated phosphorylation of AKT2 substrates (PubMed:20189988). Participates in transferrin receptor endocytosis (By similarity). {ECO:0000250|UniProtKB:Q96P53, ECO:0000269|PubMed:18388859, ECO:0000269|PubMed:20189988}. SUBCELLULAR LOCATION: Endosome {ECO:0000250|UniProtKB:Q96P53}. Early endosome {ECO:0000269|PubMed:20189988}. Cytoplasm {ECO:0000269|PubMed:18388859}. Note=Localizes to intracellular vesicles. Colocalizes with VAMP2 and PRKCZ in intracellular vesicles (By similarity). Colocalizes with AKT2 in early endosomes (PubMed:20189988). {ECO:0000250|UniProtKB:Q96P53, ECO:0000269|PubMed:20189988}. SUBUNIT: Homodimer (By similarity). Interacts (via WD repeats 1-3) with AKT1, AKT2, PRKCZ and PRKCI (PubMed:16792529, PubMed:20189988). Interacts with VAMP2 (PubMed:17313651). Forms a complex with VAMP2 and PRKCZ (PubMed:17313651). Interacts with FOXO1 (PubMed:18388859). Forms a complex with AKT1 and FOXO1 (PubMed:18388859). {ECO:0000250|UniProtKB:Q96P53, ECO:0000269|PubMed:16792529, ECO:0000269|PubMed:17313651, ECO:0000269|PubMed:18388859, ECO:0000269|PubMed:20189988}. DOMAIN: The FYVE-type zinc finger is essential for its vesicular localization. {ECO:0000250|UniProtKB:Q96P53}. TISSUE SPECIFICITY: Highly expressed in the brain (at protein level). {ECO:0000269|PubMed:16792529}. +P22725 WNT5A_MOUSE Protein Wnt-5a 380 42,309 Alternative sequence (1); Chain (1); Disulfide bond (11); Glycosylation (4); Lipidation (1); Mutagenesis (5); Propeptide (1); Sequence conflict (3); Signal peptide (1) FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors (PubMed:17117926). Can activate or inhibit canonical Wnt signaling, depending on receptor context (PubMed:16602827). In the presence of FZD4, activates beta-catenin signaling. In the presence of ROR2, inhibits the canonical Wnt pathway by promoting beta-catenin degradation through a GSK3-independent pathway which involves down-regulation of beta-catenin-induced reporter gene expression (PubMed:16602827). Suppression of the canonical pathway allows chondrogenesis to occur and inhibits tumor formation. Stimulates cell migration (PubMed:17117926). Decreases proliferation, migration, invasiveness and clonogenicity of carcinoma cells and may act as a tumor suppressor. Mediates motility of melanoma cells (By similarity). Required during embryogenesis for extension of the primary anterior-posterior axis and for outgrowth of limbs and the genital tubercle (PubMed:10021340). Inhibits type II collagen expression in chondrocytes (By similarity). {ECO:0000250|UniProtKB:P41221, ECO:0000250|UniProtKB:Q27Q52, ECO:0000269|PubMed:10021340, ECO:0000269|PubMed:12952940, ECO:0000269|PubMed:16602827, ECO:0000269|PubMed:17117926}. PTM: Glycosylation is necessary for secretion but not for activity. {ECO:0000269|PubMed:17117926}.; PTM: Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition. {ECO:0000250|UniProtKB:P27467, ECO:0000250|UniProtKB:P56704}.; PTM: Proteolytic processing by TIKI1 and TIKI2 promotes oxidation and formation of large disulfide-bond oligomers, leading to inactivation of WNT5A. {ECO:0000269|PubMed:22726442}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000305}. Secreted {ECO:0000269|PubMed:17117926}. SUBUNIT: Forms a soluble 1:1 complex with AFM; this prevents oligomerization and is required for prolonged biological activity. The complex with AFM may represent the physiological form in body fluids (By similarity). Homooligomer; disulfide-linked, leading to inactivation (PubMed:22726442). Interacts with PORCN (PubMed:10866835). Interacts with WLS (PubMed:19841259). Interacts with glypican GCP3 (By similarity). Interacts with PKD1 (via extracellular domain) (PubMed:27214281). {ECO:0000250|UniProtKB:P41221, ECO:0000269|PubMed:10866835, ECO:0000269|PubMed:19841259, ECO:0000269|PubMed:22726442, ECO:0000269|PubMed:27214281}. TISSUE SPECIFICITY: Expressed in a gradient at the caudal end of the embryo during gastrulation and later in the distal-most aspect of several structures that extend from the body such as the limbs and genital tubercle. {ECO:0000269|PubMed:10021340}. +Q91XU0 WRIP1_MOUSE ATPase WRNIP1 (EC 3.6.1.3) (Werner helicase-interacting protein 1) 660 71,794 Alternative sequence (2); Chain (1); Compositional bias (1); Cross-link (13); Frameshift (1); Metal binding (5); Modified residue (10); Nucleotide binding (1); Sequence conflict (8); Zinc finger (1) FUNCTION: Functions as a modulator of initiation or reinitiation events during DNA polymerase delta-mediated DNA synthesis. In the presence of ATP, stimulation of DNA polymerase delta-mediated DNA synthesis is decreased. Plays also a role in the innate immune defense against viruses. Stabilizes the RIG-I/DDX58 dsRNA interaction and promotes RIG-I/DDX58 'Lys-63'-linked polyubiquitination. In turn, RIG-I/DDX58 transmits the signal through mitochondrial MAVS. {ECO:0000250|UniProtKB:Q96S55}. PTM: Sumoylated with SUMO1 and SUMO2/3. {ECO:0000250|UniProtKB:Q96S55}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11301316}. Cytoplasm {ECO:0000250|UniProtKB:Q96S55}. Note=Colocalizes with WRN in granular structures in the nucleus. {ECO:0000269|PubMed:11301316}. SUBUNIT: Forms homooligomers, possibly octamers. Directly interacts with POLD1, POLD2 and POLD4 (By similarity). Interacts with the N-terminal domain of WRN (By similarity). Interacts (via UBZ-type zinc finger) with monoubiquitin and polyubiquitin. Interacts with TRIM14 and PPP6C; these interactions positively regulate the RIG-I/DDX58 signaling pathway (By similarity). {ECO:0000250|UniProtKB:Q96S55, ECO:0000269|PubMed:11301316}. DOMAIN: The UBZ-type zinc finger binds ubiquitin. {ECO:0000250|UniProtKB:Q96S55}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000250|UniProtKB:Q96S55}. +P22561 WT1_MOUSE Wilms tumor protein homolog 449 49,246 Alternative sequence (3); Chain (1); Compositional bias (1); Cross-link (3); Motif (1); Natural variant (1); Region (2); Sequence caution (1); Sequence conflict (3); Site (2); Zinc finger (4) FUNCTION: Transcription factor that plays an important role in cellular development and cell survival (PubMed:16467207, PubMed:16920711, PubMed:17537799). Recognizes and binds to the DNA sequence 5'-GCG(T/G)GGGCG-3' (By similarity). Regulates the expression of numerous target genes, including EPO (PubMed:16467207). Plays an essential role for development of the urogenital system. It has a tumor suppressor as well as an oncogenic role in tumor formation. Function may be isoform-specific: isoforms lacking the KTS motif may act as transcription factors. Isoforms containing the KTS motif may bind mRNA and play a role in mRNA metabolism or splicing (PubMed:17167543). Isoform 1 has lower affinity for DNA, and can bind RNA. {ECO:0000250|UniProtKB:P19544, ECO:0000269|PubMed:16467207, ECO:0000269|PubMed:16920711, ECO:0000269|PubMed:17167543, ECO:0000269|PubMed:17537799}. SUBCELLULAR LOCATION: Isoform 1: Nucleus speckle.; SUBCELLULAR LOCATION: Isoform 4: Nucleus, nucleoplasm.; SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14681305}. Nucleus, nucleolus {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:14681305}. Nucleus speckle. Note=Shuttles between nucleus and cytoplasm. {ECO:0000269|PubMed:14681305}. SUBUNIT: Interacts with ZNF224 via the zinc-finger region. Interacts with WTAP, AMER1 and SRY. Interacts with RBM4 (By similarity). Homodimer. Interacts with WTIP. Interacts with actively translating polysomes. Detected in nuclear ribonucleoprotein (mRNP) particles. Interacts with U2AF2. Interacts with HNRNPU via the zinc-finger region. Isoform 1 and isoform 3 interacts with CITED2. {ECO:0000250, ECO:0000269|PubMed:14681305, ECO:0000269|PubMed:14736876, ECO:0000269|PubMed:16924231, ECO:0000269|PubMed:17537799, ECO:0000269|PubMed:9784496}. DOMAIN: Binds to DNA motifs with the sequence 5'-GCG(T/G)GGGCG-3' via its C2H2-type zinc fingers. Starting from the N-terminus, the second zinc finger binds to the 3'-GCG motif, the middle zinc finger interacts with the central TGG motif, and the C-terminal zinc finger binds to the 5'-GCG motif. Binds double-stranded target DNA, irrespective of the cytosine methylation status. Has reduced affinity for target DNA where the cytosines have been oxidized to 5-hydroxymethylcytosine, 5-formylcytosine or 5-carboxylcytosine. {ECO:0000250|UniProtKB:P19544}. TISSUE SPECIFICITY: Detected in neurons of the embryonic dorsal root ganglion and in Sertoli cells of the adult testis (at protein level). Detected in kidney. {ECO:0000269|PubMed:16467207}. +O35426 XBP1_MOUSE X-box-binding protein 1 (XBP-1) (Tax-responsive element-binding protein 5) (TREB-5) [Cleaved into: X-box-binding protein 1, cytoplasmic form; X-box-binding protein 1, luminal form] 267 29,619 Alternative sequence (1); Chain (3); Domain (1); Modified residue (1); Mutagenesis (4); Region (4); Sequence conflict (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 181 198 Helical; Signal-anchor for type II membrane protein. {ECO:0000250|UniProtKB:P17861, ECO:0000255}. TOPO_DOM 1 180 Cytoplasmic. {ECO:0000250|UniProtKB:P17861}.; TOPO_DOM 199 267 Lumenal. {ECO:0000250|UniProtKB:P17861}. FUNCTION: Functions as a transcription factor during endoplasmic reticulum stress by regulating the unfolded protein response (UPR). Required for cardiac myogenesis and hepatogenesis during embryonic development and the development of secretory tissues such as exocrine pancreas and salivary gland (PubMed:10425189, PubMed:10652269, PubMed:16362047, PubMed:17612490). Involved in differentiation of B lymphocytes to plasma cells and production of immunoglobulins. Modulates the cellular response to ER stress in a PIK3R-dependent manner. Binds to the cis-acting X box present in the promoter regions of major histocompatibility complex class II genes (By similarity). Involved in VEGF-induced endothelial cell (EC) proliferation and retinal blood vessel formation during embryonic development but also for angiogenesis in adult tissues under ischemic conditions (PubMed:23529610). Functions also as a major regulator of the UPR in obesity-induced insulin resistance and type 2 diabetes for the management of obesity and diabetes prevention (PubMed:15486293). {ECO:0000250|UniProtKB:P17861, ECO:0000269|PubMed:10425189, ECO:0000269|PubMed:10652269, ECO:0000269|PubMed:15486293, ECO:0000269|PubMed:16362047, ECO:0000269|PubMed:17612490, ECO:0000269|PubMed:23529610}.; FUNCTION: Isoform 1: Plays a role in the unconventional cytoplasmic splicing processing of its own mRNA triggered by the endoplasmic reticulum (ER) transmembrane endoribonuclease ENR1: upon ER stress, the emerging XBP1 polypeptide chain, as part of a mRNA-ribosome-nascent chain (R-RNC) complex, cotranslationally recruits its own unprocessed mRNA through transient docking to the ER membrane and translational pausing, therefore facilitating efficient IRE1-mediated XBP1 mRNA isoform 2 production. In endothelial cells (EC), associated with KDR, promotes IRE1-mediated XBP1 mRNA isoform 2 production in a vascular endothelial growth factor (VEGF)-dependent manner, leading to EC proliferation and angiogenesis (By similarity). Functions as a negative feed-back regulator of the potent transcription factor XBP1 isoform 2 protein levels through proteasome-mediated degradation, thus preventing the constitutive activation of the ER stress response signaling pathway (PubMed:16332684). Inhibits the transactivation activity of XBP1 isoform 2 in myeloma cells (PubMed:12902539). Acts as a weak transcriptional factor. Together with HDAC3, contributes to the activation of NFE2L2-mediated HMOX1 transcription factor gene expression in a PI(3)K/mTORC2/Akt-dependent signaling pathway leading to EC survival under disturbed flow/oxidative stress. Binds to the ER stress response element (ERSE) upon ER stress. Binds to the consensus 5'-GATGACGTG[TG]N(3)[AT]T-3' sequence related to cAMP responsive element (CRE)-like sequences. Binds the Tax-responsive element (TRE) present in the long terminal repeat (LTR) of T-cell leukemia virus type 1 (HTLV-I) and to the TPA response elements (TRE). Associates preferentially to the HDAC3 gene promoter region in a static flow-dependent manner. Binds to the CDH5/VE-cadherin gene promoter region (By similarity). {ECO:0000250|UniProtKB:P17861, ECO:0000269|PubMed:12902539, ECO:0000269|PubMed:16332684}.; FUNCTION: Isoform 2: Functions as a stress-inducible potent transcriptional activator during endoplasmic reticulum (ER) stress by inducing unfolded protein response (UPR) target genes via binding to the UPR element (UPRE). Up-regulates target genes encoding ER chaperones and ER-associated degradation (ERAD) components to enhance the capacity of productive folding and degradation mechanism, respectively, in order to maintain the homeostasis of the ER under ER stress (PubMed:11850408, PubMed:14559994). Plays a role in the production of immunoglobulins and interleukin-6 in the presence of stimuli required for plasma cell differentiation, and promotes as well membrane phospholipid biosynthesis necessary for ER expansion (PubMed:12612580, PubMed:17213183). Contributes to the VEGF-induced endothelial cell (EC) growth and proliferation in a Akt/GSK-dependent and/or -independent signaling pathway, respectively, leading to beta-catenin nuclear translocation and E2F2 gene expression. Promotes umbilical vein EC apoptosis and atherosclerotisis development in a caspase-dependent signaling pathway, and contributes to VEGF-induced EC proliferation and angiogenesis in adult tissues under ischemic conditions. Involved in the regulation of endostatin-induced autophagy in EC through BECN1 transcriptional activation. Plays a role as an oncogene by promoting tumor progression: stimulates zinc finger protein SNAI1 transcription to induce epithelial-to-mesenchymal (EMT) transition, cell migration and invasion of breast cancer cells (By similarity). Involved in adipocyte differentiation by regulating lipogenic gene expression during lactation (PubMed:23623498, PubMed:25223794). Plays a role in the survival of both dopaminergic neurons of the substantia nigra pars compacta (SNpc), by maintaining protein homeostasis and of myeloma cells (PubMed:12902539, PubMed:24753614). Increases insulin sensitivity in the liver as a response to a high carbohydrate diet, resulting in improved glucose tolerance (PubMed:20348926). Improves also glucose homeostasis in an ER stress- and/or insulin-independent manner through both binding and proteasome-induced degradation of the transcription factor FOXO1, hence resulting in suppression of gluconeogenic genes expression and in a reduction of blood glucose levels (PubMed:21317886). Controls the induction of de novo fatty acid synthesis in hepatocytes by regulating the expression of a subset of lipogenic genes in an ER stress- and UPR-independent manner (PubMed:18556558). Binds to the 5'-CCACG-3' motif in the PPARG promoter (PubMed:25223794). Associates preferentially to the HDAC3 gene promoter region in a disturbed flow-dependent manner. Binds to the BECN1 gene promoter region. Binds to the CDH5/VE-cadherin gene promoter region. Binds to the ER stress response element (ERSE) upon ER stress (By similarity). {ECO:0000250|UniProtKB:P17861, ECO:0000269|PubMed:11850408, ECO:0000269|PubMed:12612580, ECO:0000269|PubMed:12902539, ECO:0000269|PubMed:14559994, ECO:0000269|PubMed:17213183, ECO:0000269|PubMed:18556558, ECO:0000269|PubMed:20348926, ECO:0000269|PubMed:21317886, ECO:0000269|PubMed:23623498, ECO:0000269|PubMed:24753614, ECO:0000269|PubMed:25223794}. PTM: Isoform 2 is acetylated by EP300; acetylation positively regulates the transcriptional activity of XBP1 isoform 2 (PubMed:20955178). Isoform 2 is deacetylated by SIRT1; deacetylation negatively regulates the transcriptional activity of XBP1 isoform 2 (PubMed:20955178). {ECO:0000269|PubMed:20955178, ECO:0000305|PubMed:20955178}.; PTM: Isoform 1 is ubiquitinated, leading to proteasomal degradation in response to ER stress (PubMed:11780124, PubMed:12902539, PubMed:16332684). {ECO:0000250|UniProtKB:P17861, ECO:0000269|PubMed:11780124, ECO:0000269|PubMed:12902539, ECO:0000269|PubMed:16332684}.; PTM: X-box-binding protein 1, cytoplasmic form and luminal form are produced by intramembrane proteolytic cleavage of ER membrane-anchored isoform 1 triggered by HM13/SPP in a DERL1-RNF139-dependent and VCP/p97-independent manner. X-box-binding protein 1, luminal form is ubiquitinated leading to proteasomal degradation (By similarity). {ECO:0000250|UniProtKB:P17861}. SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:P17861}. Note=Colocalizes with ERN1 and KDR in the endoplasmic reticulum in endothelial cells in a vascular endothelial growth factor (VEGF)-dependent manner (By similarity). {ECO:0000250|UniProtKB:P17861}.; SUBCELLULAR LOCATION: Isoform 1: Nucleus {ECO:0000269|PubMed:16332684}. Cytoplasm {ECO:0000269|PubMed:16332684}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17861}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P17861}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17861}; Peripheral membrane protein {ECO:0000250|UniProtKB:P17861}. Membrane {ECO:0000250|UniProtKB:P17861}; Peripheral membrane protein {ECO:0000250|UniProtKB:P17861}. Note=Shuttles between the nucleus and the cytoplasm in a CRM1-dependent manner. Localizes predominantly at the endoplasmic reticulum membrane as a membrane-spanning protein; whereas may be only marginally localized on the cytosolic side of the ER membrane as a peripheral membrane (By similarity). Shows no preferential localization to either the nucleus or the cytoplasm (PubMed:16332684). {ECO:0000250|UniProtKB:P17861, ECO:0000269|PubMed:16332684}.; SUBCELLULAR LOCATION: Isoform 2: Nucleus {ECO:0000269|PubMed:16332684, ECO:0000269|PubMed:18556558, ECO:0000269|PubMed:20348926, ECO:0000269|PubMed:20955178}. Cytoplasm {ECO:0000269|PubMed:16332684}. Note=Localizes predominantly in the nucleus (PubMed:16332684). Colocalizes in the nucleus with SIRT1 (PubMed:20955178). Translocates into the nucleus in a PIK3R-, ER stress-induced- and/or insulin-dependent manner (PubMed:20348926). {ECO:0000269|PubMed:16332684, ECO:0000269|PubMed:18556558, ECO:0000269|PubMed:20348926, ECO:0000269|PubMed:20955178}.; SUBCELLULAR LOCATION: X-box-binding protein 1, cytoplasmic form: Cytoplasm {ECO:0000250|UniProtKB:P17861}. Nucleus {ECO:0000250|UniProtKB:P17861}. Note=Localizes in the cytoplasm and nucleus after HM13/SPP-mediated intramembranaire proteolytic cleavage of isoform 1 (By similarity). {ECO:0000250|UniProtKB:P17861}. SUBUNIT: Isoform 1 interacts with HM13. Isoform 1 interacts with RNF139; the interaction induces ubiquitination and degradation of isoform 1. Isoform 1 interacts (via luminal domain) with DERL1; the interaction obviates the need for ectodomain shedding prior HM13/SPP-mediated XBP1 isoform 1 cleavage. Isoform 1 interacts with isoform 2; the interaction sequesters isoform 2 from the nucleus and enhances isoform 2 degradation in the cytoplasm. Isoform 1 interacts with HDAC3 and AKT1; the interactions occur in endothelial cell (EC) under disturbed flow. Isoform 1 interacts with the oncoprotein FOS. Isoform 2 interacts with ATF6; the interaction occurs in a ER stress-dependent manner and is required for DNA binding to the unfolded protein response element (UPRE). Isoform 2 interacts with PIK3R1; the interaction is direct and induces translocation of XBP1 isoform 2 into the nucleus and the unfolded protein response (UPR) XBP1-dependent target genes activation in a ER stress- and/or insulin-dependent but PI3K-independent manner (By similarity). Isoform 2 interacts with SIRT1 (PubMed:20955178). Isoform 2 interacts with PIK3R1 and PIK3R2; the interactions are direct and induce translocation of XBP1 isoform 2 into the nucleus and the unfolded protein response (UPR) XBP1-dependent target genes activation in a ER stress- and/or insulin-dependent but PI3K-independent manner (PubMed:20348926). Isoform 2 interacts with FOXO1; the interaction is direct and leads to FOXO1 ubiquitination and degradation via the proteasome pathway in hepatocytes (PubMed:21317886). {ECO:0000250|UniProtKB:P17861, ECO:0000269|PubMed:20348926, ECO:0000269|PubMed:20955178, ECO:0000269|PubMed:21317886}. DOMAIN: Isoform 1 transmembrane signal-anchor domain is necessary for its own mRNA to be recruited to the endoplasmic reticulum (ER) which will undergo unconventional ERN1-dependent splicing in response to ER stress. Isoform 1 N-terminus and C-terminus regions are necessary for DNA-binding and weak transcriptional activity, respectively. Isoform 2 N-terminus and C-terminus regions are necessary for DNA-binding and strong transcriptional activity upon ER stress, respectively. Isoform 2 C-terminus region contains a nuclear exclusion signal (NES) at positions 182 through 204. Isoform 2 C-terminus region contains a degradation domain at positions 204 through 256 (By similarity). Isoform 1 and isoform 2 N-terminus domains are necessary for nuclear localization targeting. Isoform 1 C-terminus domain confers localization to the cytoplasm and is sufficient to impose rapid degradation (PubMed:16332684). {ECO:0000250|UniProtKB:P17861, ECO:0000269|PubMed:16332684}. TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed at higher level in branch curves of vessel walls and in atherosclerotic plaques relative to healthy segments of the same aortas (at protein level) (PubMed:19416856). Expressed in skeletal muscles, plasma cells and pancreatic beta cells (PubMed:17612490). Isoform 1 and isoform 2 are expressed in gonadal adipose tissue. Isoform 1 is expressed in inguinal adipose tissue (PubMed:23623498). {ECO:0000269|PubMed:17612490, ECO:0000269|PubMed:19416856, ECO:0000269|PubMed:23623498}. +Q5GH68 XKR2_MOUSE XK-related protein 2 (X Kell blood group-related, X-linked) 449 51,778 Chain (1); Transmembrane (10) TRANSMEM 35 55 Helical. {ECO:0000255}.; TRANSMEM 68 88 Helical. {ECO:0000255}.; TRANSMEM 98 118 Helical. {ECO:0000255}.; TRANSMEM 174 194 Helical. {ECO:0000255}.; TRANSMEM 204 224 Helical. {ECO:0000255}.; TRANSMEM 241 261 Helical. {ECO:0000255}.; TRANSMEM 269 289 Helical. {ECO:0000255}.; TRANSMEM 306 326 Helical. {ECO:0000255}.; TRANSMEM 357 377 Helical. {ECO:0000255}.; TRANSMEM 382 402 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9Z0U0 XPR1_MOUSE Xenotropic and polytropic retrovirus receptor 1 (Protein SYG1 homolog) (Rmc-1) 695 81,751 Alternative sequence (1); Chain (1); Domain (2); Modified residue (2); Mutagenesis (2); Region (1); Sequence conflict (17); Site (2); Topological domain (9); Transmembrane (8) TRANSMEM 237 257 Helical. {ECO:0000255}.; TRANSMEM 265 285 Helical. {ECO:0000255}.; TRANSMEM 315 337 Helical. {ECO:0000255}.; TRANSMEM 341 360 Helical. {ECO:0000255}.; TRANSMEM 377 397 Helical. {ECO:0000255}.; TRANSMEM 403 423 Helical. {ECO:0000255}.; TRANSMEM 476 498 Helical. {ECO:0000255}.; TRANSMEM 508 528 Helical. {ECO:0000255}. TOPO_DOM 1 236 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 258 264 Extracellular. {ECO:0000255}.; TOPO_DOM 286 314 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 338 340 Extracellular. {ECO:0000255}.; TOPO_DOM 361 376 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 398 402 Extracellular. {ECO:0000255}.; TOPO_DOM 424 475 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 499 507 Extracellular. {ECO:0000255}.; TOPO_DOM 529 695 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a role in phosphate homeostasis. Mediates phosphate export from the cell. Binds inositol hexakisphosphate (Ins6P) and similar inositol polyphosphates, such as 5-diphospho-inositol pentakisphosphate (5-InsP7); these are important intracellular signaling molecules (By similarity). Potential receptor for xenotropic and polytropic murine leukemia retroviruses (PubMed:10516044, PubMed:9988277). {ECO:0000250|UniProtKB:Q9UBH6, ECO:0000269|PubMed:10516044, ECO:0000269|PubMed:9988277}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9UBH6}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9UBH6}. DOMAIN: The SPX domain has high affinity for inositol polyphosphates, such as myo-inositol hexakisphosphate and 5-diphospho-myo-inositol pentakisphosphate (5-InsP7). Its affinity for inorganic phosphate is tow to three orders of magnitude lower. {ECO:0000250|UniProtKB:Q9UBH6}. +Q3U4G3 XXLT1_MOUSE Xyloside xylosyltransferase 1 (EC 2.4.2.n3) (UDP-xylose:alpha-xyloside alpha-1,3-xylosyltransferase) 392 43,839 Beta strand (11); Binding site (7); Chain (1); Disulfide bond (2); Erroneous initiation (1); Helix (18); Metal binding (3); Mutagenesis (16); Region (2); Sequence conflict (6); Topological domain (2); Transmembrane (1); Turn (3) TRANSMEM 20 42 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 19 Cytoplasmic. {ECO:0000305|PubMed:26414444}.; TOPO_DOM 43 392 Lumenal. {ECO:0000305|PubMed:26414444}. FUNCTION: Alpha-1,3-xylosyltransferase, which elongates the O-linked xylose-glucose disaccharide attached to EGF-like repeats in the extracellular domain of target proteins by catalyzing the addition of the second xylose. Known targets include Notch proteins and coagulation factors, such as F9. {ECO:0000269|PubMed:26414444}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8NBI6}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q8NBI6}. SUBUNIT: Homodimer (PubMed:26414444). Dimer formation may be essential for the retention in endoplasmic reticulum (Probable). {ECO:0000269|PubMed:26414444, ECO:0000305}. +P23475 XRCC6_MOUSE X-ray repair cross-complementing protein 6 (EC 3.6.4.-) (EC 4.2.99.-) (5'-deoxyribose-5-phosphate lyase Ku70) (5'-dRP/AP lyase Ku70) (ATP-dependent DNA helicase 2 subunit 1) (ATP-dependent DNA helicase II 70 kDa subunit) (CTC box-binding factor 75 kDa subunit) (CTC75) (CTCBF) (DNA repair protein XRCC6) (Ku autoantigen protein p70 homolog) (Ku70) 608 69,484 Active site (1); Chain (1); Compositional bias (2); Cross-link (2); Domain (2); Initiator methionine (1); Modified residue (12); Region (1); Sequence conflict (9) FUNCTION: Single-stranded DNA-dependent ATP-dependent helicase. Has a role in chromosome translocation. The DNA helicase II complex binds preferentially to fork-like ends of double-stranded DNA in a cell cycle-dependent manner. It works in the 3'-5' direction. Binding to DNA may be mediated by XRCC6. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. The XRCC5/6 dimer acts as regulatory subunit of the DNA-dependent protein kinase complex DNA-PK by increasing the affinity of the catalytic subunit PRKDC to DNA by 100-fold. The XRCC5/6 dimer is probably involved in stabilizing broken DNA ends and bringing them together. The assembly of the DNA-PK complex to DNA ends is required for the NHEJ ligation step. Required for osteocalcin gene expression. Probably also acts as a 5'-deoxyribose-5-phosphate lyase (5'-dRP lyase), by catalyzing the beta-elimination of the 5' deoxyribose-5-phosphate at an abasic site near double-strand breaks. 5'-dRP lyase activity allows to 'clean' the termini of abasic sites, a class of nucleotide damage commonly associated with strand breaks, before such broken ends can be joined. The XRCC5/6 dimer together with APEX1 acts as a negative regulator of transcription. Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway (By similarity). {ECO:0000250|UniProtKB:P12956, ECO:0000269|PubMed:12145306}. PTM: Phosphorylation by PRKDC may enhance helicase activity. Phosphorylation of Ser-49 does not affect DNA repair. {ECO:0000250|UniProtKB:P12956}.; PTM: ADP-ribosylated by PARP3. {ECO:0000250|UniProtKB:P12956}. SUBCELLULAR LOCATION: Nucleus. Chromosome. SUBUNIT: Heterodimer composed of XRCC5/Ku80 and XRCC6/Ku70. The dimer associates in a DNA-dependent manner with PRKDC to form the DNA-dependent protein kinase complex DNA-PK, and with the LIG4-XRCC4 complex to form the core of the non-homologous end joining (NHEJ) complex. Additional components of the NHEJ complex include NHEJ1/XLF and PAXX. The dimer also associates with NAA15, and this complex binds to the osteocalcin promoter and activates osteocalcin expression. In addition, XRCC6 interacts with the osteoblast-specific transcription factors MSX2, RUNX2 and DLX5. Interacts with ELF3. Interacts with ATP23. The XRCC5/6 dimer associates in a DNA-dependent manner with APEX1. Binds to CDK9 (By similarity). Identified in a complex with DEAF1 and XRCC5. Interacts with DEAF1 (via the SAND domain); the interaction is direct and may be inhibited by DNA-binding (By similarity). Interacts with CLU (PubMed:12551933). Interacts with NR4A3; the DNA-dependent protein kinase complex DNA-PK phosphorylates and activates NR4A3 and prevents NR4A3 ubiquitinylation and degradation (By similarity). Interacts with CYREN (By similarity). Interacts (via N-terminus) with HSF1 (via N-terminus); this interaction is direct and prevents XRCC5/XRCC6 heterodimeric binding and non-homologous end joining (NHEJ) repair activities induced by ionizing radiation (IR) (By similarity). Part of the HDP-RNP complex composed of at least HEXIM1, PRKDC, XRCC5, XRCC6, paraspeckle proteins (SFPQ, NONO, PSPC1, RBM14, and MATR3) and NEAT1 RNA (By similarity). Interacts with HMBOX1 (By similarity). {ECO:0000250|UniProtKB:P12956, ECO:0000269|PubMed:12551933}. +Q505H4 VWC2L_MOUSE von Willebrand factor C domain-containing protein 2-like (Brorin-like) 222 24,528 Alternative sequence (6); Chain (1); Domain (2); Signal peptide (1) FUNCTION: May play a role in neurogenesis. May promote matrix mineralization (PubMed:22209847), but has been shown to weakly, but significantly inhibit BMP2 and BMP6 activity in a preosteoblastic cell line (PubMed:19852960). {ECO:0000269|PubMed:19852960, ECO:0000269|PubMed:22209847}. SUBCELLULAR LOCATION: Secreted. Cell junction, synapse {ECO:0000305}. SUBUNIT: Peripherally associated with AMPAR complex. AMPAR complex consists of an inner core made of 4 pore-forming GluA/GRIA proteins (GRIA1, GRIA2, GRIA3 and GRIA4) and 4 major auxiliary subunits arranged in a twofold symmetry. One of the two pairs of distinct binding sites is occupied either by CNIH2, CNIH3 or CACNG2, CACNG3. The other harbors CACNG2, CACNG3, CACNG4, CACNG8 or GSG1L. This inner core of AMPAR complex is complemented by outer core constituents binding directly to the GluA/GRIA proteins at sites distinct from the interaction sites of the inner core constituents. Outer core constituents include at least PRRT1, PRRT2, CKAMP44/SHISA9, FRRS1L and NRN1. The proteins of the inner and outer core serve as a platform for other, more peripherally associated AMPAR constituents, including VWC2L. Alone or in combination, these auxiliary subunits control the gating and pharmacology of the AMPAR complex and profoundly impact their biogenesis and protein processing. {ECO:0000269|PubMed:22632720}. TISSUE SPECIFICITY: Predominantly expressed in the brain (at protein level). Also detected in bones, including femur and calvaria, heart, lung and kidney. Isoform 5 is predominant in lung and heart, compared to isoforms 1 and 3. Isoform 4 is expressed in femur and calvaria at higher levels than isoforms 1 and 5. Isoforms 1 and 4 are expressed at higher levels than isoform 5 in kidney and brain. {ECO:0000269|PubMed:19852960, ECO:0000269|PubMed:22209847, ECO:0000269|PubMed:22632720}. +Q0P5W1 VPS8_MOUSE Vacuolar protein sorting-associated protein 8 homolog 1427 161,146 Alternative sequence (4); Chain (1); Erroneous initiation (2); Frameshift (1); Modified residue (3); Repeat (1); Sequence conflict (1); Zinc finger (1) FUNCTION: Plays a role in vesicle-mediated protein trafficking of the endocytic membrane transport pathway. Believed to act as a component of the putative CORVET endosomal tethering complexes which is proposed to be involved in the Rab5-to-Rab7 endosome conversion probably implicating MON1A/B, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion. The CORVET complex is proposed to function as a Rab5 effector to mediate early endosome fusion probably in specific endosome subpopulations. Functions predominantly in APPL1-containing endosomes (By similarity). {ECO:0000250|UniProtKB:Q8N3P4}. SUBUNIT: Interacts with RAB5C (PubMed:25266290). Interacts with TGFBRAP1 (By similarity). Component of the putative class C core vacuole/endosome tethering (CORVET) complex; the core of which is composed of the class C Vps proteins VPS11, VPS16, VPS18 and VPS33A, associated with VPS8 and TGFBRAP1 (PubMed:25266290). {ECO:0000250|UniProtKB:Q8N3P4, ECO:0000269|PubMed:25266290, ECO:0000305|PubMed:25266290}. +Q9D994 WDR38_MOUSE WD repeat-containing protein 38 303 33,052 Chain (1); Repeat (7) +Q8BHB4 WDR3_MOUSE WD repeat-containing protein 3 942 105,775 Chain (1); Compositional bias (1); Cross-link (1); Modified residue (2); Repeat (13) SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. +Q9R0D8 WDR54_MOUSE WD repeat-containing protein 54 334 35,613 Chain (1); Repeat (4) +Q3UW41 WFDC9_MOUSE Protein WFDC9 83 9,564 Chain (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q3SYK4 VRTN_MOUSE Vertnin 740 83,135 Chain (1) +P59328 WDHD1_MOUSE WD repeat and HMG-box DNA-binding protein 1 (Acidic nucleoplasmic DNA-binding protein 1) (And-1) 1117 124,254 Alternative sequence (3); Chain (1); Cross-link (3); DNA binding (1); Modified residue (9); Repeat (7); Sequence conflict (2) FUNCTION: Acts as a replication initiation factor that brings together the MCM2-7 helicase and the DNA polymerase alpha/primase complex in order to initiate DNA replication. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}. SUBUNIT: Interacts with the polymerase alpha catalytic subunit POLA1. Interacts with MCM10. Interacts with DNA2 (By similarity). {ECO:0000250}. +Q9JHY3 WFD12_MOUSE WAP four-disulfide core domain protein 12 (Elafin-like protein II) (Single WAP motif protein 2) (Whey acidic protein 2) 85 9,559 Chain (1); Disulfide bond (4); Domain (1); Signal peptide (1) FUNCTION: Antibacterial protein which inhibits the growth of E.coli and S.aureus. Putative acid-stable proteinase inhibitor. {ECO:0000250|UniProtKB:Q8WWY7, ECO:0000269|PubMed:12574366}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Constitutively expressed in tongue. {ECO:0000269|PubMed:12574366}. +Q9WUD6 WNT8B_MOUSE Protein Wnt-8b 350 38,576 Chain (1); Disulfide bond (11); Glycosylation (2); Lipidation (1); Signal peptide (1) FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors. May play an important role in the development and differentiation of certain forebrain structures, notably the hippocampus. PTM: Palmitoleoylation is required for efficient binding to frizzled receptors (By similarity). Depalmitoleoylation leads to Wnt signaling pathway inhibition (By similarity). {ECO:0000250|UniProtKB:P28026, ECO:0000250|UniProtKB:P56704}.; PTM: Proteolytic processing by TIKI1 and TIKI2 promotes oxidation and formation of large disulfide-bond oligomers, leading to inactivation of WNT8B. {ECO:0000250|UniProtKB:P28026}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. +Q8K0D7 WRB_MOUSE Tail-anchored protein insertion receptor WRB (Tryptophan-rich basic protein) (WRB) 174 19,867 Chain (1); Coiled coil (1); Region (1); Topological domain (4); Transmembrane (3) TRANSMEM 9 29 Helical. {ECO:0000255}.; TRANSMEM 100 120 Helical. {ECO:0000255}.; TRANSMEM 149 169 Helical. {ECO:0000255}. TOPO_DOM 1 8 Lumenal. {ECO:0000255}.; TOPO_DOM 30 99 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 121 148 Lumenal. {ECO:0000255}.; TOPO_DOM 170 174 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for ASNA1/TRC40-mediated insertion of tail-anchored (TA) proteins into the ER membrane. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with ASNA1/TRC40. {ECO:0000250}. +O09053 WRN_MOUSE Werner syndrome ATP-dependent helicase homolog (EC 3.6.4.12) (Exonuclease WRN) (EC 3.1.-.-) 1401 157,204 Beta strand (7); Chain (1); Compositional bias (1); Cross-link (3); Domain (4); Helix (8); Metal binding (4); Modified residue (5); Motif (1); Mutagenesis (3); Nucleotide binding (1); Region (2); Sequence conflict (51); Site (2) FUNCTION: Multifunctional enzyme that has both magnesium and ATP-dependent DNA-helicase activity and 3'->5' exonuclease activity towards double-stranded DNA with a 5'-overhang. Has no nuclease activity towards single-stranded DNA or blunt-ended double-stranded DNA. Binds preferentially to DNA substrates containing alternate secondary structures, such as replication forks and Holliday junctions. May play an important role in the dissociation of joint DNA molecules that can arise as products of homologous recombination, at stalled replication forks or during DNA repair. Alleviates stalling of DNA polymerases at the site of DNA lesions. Important for genomic integrity. Plays a role in the formation of DNA replication focal centers; stably associates with foci elements generating binding sites for RP-A (By similarity). Plays a role in double-strand break repair after gamma-irradiation (By similarity). {ECO:0000250, ECO:0000269|PubMed:10757812, ECO:0000269|PubMed:17229737}. PTM: Phosphorylated by PRKDC. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9618508}. Nucleus, nucleolus {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Note=Gamma-irradiation leads to its translocation from nucleoli to nucleoplasm and PML regulates the irradiation-induced WRN relocation. {ECO:0000250}. SUBUNIT: Monomer, and homooligomer. May exist as homodimer, homotrimer, homotetramer and/or homohexamer. Homotetramer, or homohexamer, when bound to DNA. Interacts via its N-terminal domain with WRNIP1. Interacts with PCNA; EXO1 and SUPV3L1 (By similarity). Interacts with PML (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed ubiquitously in most organs at a low level, highly expressed in testis, ovary and spleen. {ECO:0000269|PubMed:10757812, ECO:0000269|PubMed:9143515}. +P17553 WNT3_MOUSE Proto-oncogene Wnt-3 (Proto-oncogene Int-4) 355 39,659 Chain (1); Disulfide bond (11); Glycosylation (2); Lipidation (1); Signal peptide (1) FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors (Probable). Functions in the canonical Wnt signaling pathway that results in activation of transcription factors of the TCF/LEF family (By similarity). Required for normal gastrulation, formation of the primitive streak, and for the formation of the mesoderm during early embryogenesis (PubMed:10431240). Required for normal formation of the apical ectodermal ridge and for normal embryonic limb development (PubMed:12569130). {ECO:0000250|UniProtKB:P56703, ECO:0000269|PubMed:10431240, ECO:0000269|PubMed:12569130, ECO:0000305}. PTM: Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition. {ECO:0000250|UniProtKB:P27467, ECO:0000250|UniProtKB:P56704}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P56703}. Secreted {ECO:0000250|UniProtKB:P56703}. SUBUNIT: Forms a soluble 1:1 complex with AFM; this prevents oligomerization and is required for prolonged biological activity. The complex with AFM may represent the physiological form in body fluids (By similarity). Interacts with PORCN (PubMed:10866835). Interacts with WLS (PubMed:19841259). {ECO:0000250|UniProtKB:P56703, ECO:0000269|PubMed:10866835, ECO:0000269|PubMed:19841259}. TISSUE SPECIFICITY: Detected at low levels in adult brain (PubMed:2162045). Dorsal portion of the neural tube, dorsal ectoderm, the branchial arches, and the limb buds. {ECO:0000269|PubMed:2162045}. +O54929 WSB2_MOUSE WD repeat and SOCS box-containing protein 2 (WSB-2) (SOCS box-containing WD protein SWiP-2) 404 45,261 Chain (1); Domain (1); Repeat (5); Sequence conflict (1) Protein modification; protein ubiquitination. FUNCTION: May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000250}. DOMAIN: The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin ligase complexes. {ECO:0000250}. +Q8C0T0 XKR8_MOUSE XK-related protein 8 (mXkr8) [Cleaved into: XK-related protein 8, processed form] 401 45,563 Chain (2); Site (1); Topological domain (9); Transmembrane (8) TRANSMEM 9 29 Helical. {ECO:0000255}.; TRANSMEM 48 68 Helical. {ECO:0000255}.; TRANSMEM 159 179 Helical. {ECO:0000255}.; TRANSMEM 201 221 Helical. {ECO:0000255}.; TRANSMEM 224 244 Helical. {ECO:0000255}.; TRANSMEM 259 279 Helical. {ECO:0000255}.; TRANSMEM 285 305 Helical. {ECO:0000255}.; TRANSMEM 314 334 Helical. {ECO:0000255}. TOPO_DOM 1 8 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 30 47 Extracellular. {ECO:0000255}.; TOPO_DOM 69 158 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 180 200 Extracellular. {ECO:0000255}.; TOPO_DOM 222 223 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 245 258 Extracellular. {ECO:0000255}.; TOPO_DOM 280 284 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 306 313 Extracellular. {ECO:0000255}.; TOPO_DOM 335 401 Cytoplasmic. {ECO:0000255}. FUNCTION: Promotes phosphatidylserine exposure on apoptotic cell surface, possibly by mediating phospholipid scrambling. Phosphatidylserine is a specific marker only present at the surface of apoptotic cells and acts as a specific signal for engulfment. Has no effect on calcium-induced exposure of phosphatidylserine. Activated upon caspase cleavage, suggesting that it does not act prior the onset of apoptosis. {ECO:0000269|PubMed:23845944}. PTM: Undergoes proteolytic processing by caspase-3 (CASP3), leading to its activation. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed with higher expression in testis. {ECO:0000269|PubMed:23845944}. +Q9QZD4 XPF_MOUSE DNA repair endonuclease XPF (EC 3.1.-.-) (DNA excision repair protein ERCC-4) 917 103,690 Chain (1); Domain (1); Erroneous initiation (1); Modified residue (3); Motif (1); Region (5); Sequence conflict (1) FUNCTION: Catalytic component of a structure-specific DNA repair endonuclease responsible for the 5-prime incision during DNA repair. Involved in homologous recombination that assists in removing interstrand cross-link (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Heterodimer composed of ERCC1 and XPF/ERCC4. Interacts with SLX4/BTBD12; this interaction is direct and links the ERCC1-XPF/ERCC1 complex to SLX4, which may coordinate the action of the structure-specific endonuclease during DNA repair (By similarity). {ECO:0000250}. +Q64267 XPA_MOUSE DNA repair protein complementing XP-A cells homolog (Xeroderma pigmentosum group A-complementing protein homolog) 272 31,398 Alternative sequence (1); Chain (1); Compositional bias (1); Cross-link (2); Initiator methionine (1); Modified residue (2); Motif (1); Region (1); Sequence conflict (2); Zinc finger (1) FUNCTION: Involved in DNA excision repair. Initiates repair by binding to damaged sites with various affinities, depending on the photoproduct and the transcriptional state of the region. Required for UV-induced CHEK1 phosphorylation and the recruitment of CEP164 to cyclobutane pyrimidine dimmers (CPD), sites of DNA damage after UV irradiation (By similarity). {ECO:0000250}. PTM: Ubiquitinated by HERC2 leading to degradation by the proteasome. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with GPN1. Interacts with RPA1 and RPA2; the interaction is direct and associates XPA with the RPA complex. Interacts (via N-terminus) with CEP164 upon UV irradiation. Interacts with HERC2 (By similarity). {ECO:0000250}. +Q9CRT8 XPOT_MOUSE Exportin-T (Exportin(tRNA)) (tRNA exportin) 963 109,734 Chain (1); Modified residue (2); Sequence conflict (1) FUNCTION: Mediates the nuclear export of aminoacylated tRNAs. In the nucleus binds to tRNA and to the GTPase Ran in its active GTP-bound form. Docking of this trimeric complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of the tRNA from the export receptor. XPOT then return to the nuclear compartment and mediate another round of transport. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Nuclear, once bound to tRNA and Ran the complex translocates to the cytoplasm. Shuttles between the nucleus and the cytoplasm (By similarity). {ECO:0000250}. SUBUNIT: Found in a complex with XPOT, Ran and tRNA. Probably found in a complex with nucleoporins. Interacts with Ran and tRNA in a GTP-dependent manner (By similarity). {ECO:0000250}. +Q8BR70 YIPF6_MOUSE Protein YIPF6 (YIP1 family member 6) 236 26,088 Chain (1); Initiator methionine (1); Modified residue (2); Topological domain (6); Transmembrane (5) TRANSMEM 85 105 Helical. {ECO:0000255}.; TRANSMEM 117 137 Helical. {ECO:0000255}.; TRANSMEM 148 168 Helical. {ECO:0000255}.; TRANSMEM 186 206 Helical. {ECO:0000255}.; TRANSMEM 214 234 Helical. {ECO:0000255}. TOPO_DOM 2 84 Cytoplasmic. {ECO:0000250|UniProtKB:Q96EC8}.; TOPO_DOM 106 116 Lumenal. {ECO:0000305}.; TOPO_DOM 138 147 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 169 185 Lumenal. {ECO:0000305}.; TOPO_DOM 207 213 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 235 236 Lumenal. {ECO:0000250|UniProtKB:Q96EC8}. FUNCTION: May be required for stable YIPF1 and YIPF2 protein expression. {ECO:0000250|UniProtKB:Q96EC8}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q96EC8}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q96EC8}. Note=Evenly distributed between cis- and trans-Golgi apparatus. Mainly localizes within medial-/trans-Golgi and trans-Golgi network (TGN), while less so within cis-Golgi. {ECO:0000250|UniProtKB:Q96EC8}. SUBUNIT: Predominantly interacts with YIPF1 or YIPF2, but may also form a ternary complex with YIPF1 and YIPF2. This interaction may stabilize YIPF1 and YIPF2. {ECO:0000250|UniProtKB:Q96EC8}. +F6W8I0 YJEN3_MOUSE YjeF N-terminal domain-containing protein 3 (YjeF_N3) (hYjeF_N3) 251 27,016 Chain (1); Domain (1) FUNCTION: May play a role in spermiogenesis and oogenesis. {ECO:0000250}. +O88967 YMEL1_MOUSE ATP-dependent zinc metalloprotease YME1L1 (EC 3.4.24.-) (ATP-dependent metalloprotease FtsH1) (YME1-like protein 1) 715 80,028 Active site (1); Chain (1); Metal binding (3); Nucleotide binding (1); Topological domain (2); Transmembrane (1) TRANSMEM 238 258 Helical. {ECO:0000255}. TOPO_DOM 1 237 Mitochondrial matrix. {ECO:0000255}.; TOPO_DOM 259 715 Mitochondrial intermembrane. {ECO:0000255}. FUNCTION: ATP-dependent metalloprotease that catalyzes the degradation of folded and unfolded proteins with a suitable degron sequence in the mitochondrial intermembrane region (By similarity). Plays an important role in regulating mitochondrial morphology and function by cleaving OPA1 at position S2, giving rise to a form of OPA1 that promotes maintenance of normal mitochondrial structure (PubMed:17709429, PubMed:24616225, PubMed:26785494, PubMed:27495975). Ensures cell proliferation, maintains normal cristae morphology and complex I respiration activity, promotes antiapoptotic activity and protects mitochondria from the accumulation of oxidatively damaged membrane proteins (By similarity). Required for normal, constitutive degradation of PRELID1 (PubMed:26785494). Catalyzes the degradation of OMA1 in response to membrane depolarization. Required to control the accumulation of nonassembled respiratory chain subunits (NDUFB6, OX4 and ND1) (By similarity). {ECO:0000250|UniProtKB:Q96TA2, ECO:0000269|PubMed:17709429, ECO:0000269|PubMed:24616225, ECO:0000269|PubMed:26785494, ECO:0000269|PubMed:27495975}. PTM: Proteolytically processed by mitochondrial processing peptidase (MPP) to generate the mature form. {ECO:0000250|UniProtKB:Q96TA2}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q96TA2}. Mitochondrion {ECO:0000250|UniProtKB:Q96TA2}. SUBUNIT: Homohexamer; may also form heterohexamers. Exists in several complexes of 600-1100 kDa. Interacts with AFG1L. {ECO:0000250|UniProtKB:Q96TA2}. TISSUE SPECIFICITY: Detected in heart and skeletal muscle (at protein level). {ECO:0000269|PubMed:26785494}. +Q9CWB7 YD286_MOUSE Glutaredoxin-like protein C5orf63 homolog 115 13,430 Beta strand (4); Chain (1); Disulfide bond (1); Helix (3) +Q14BV6 YDJC_MOUSE Carbohydrate deacetylase (EC 3.5.1.-) 310 33,094 Active site (1); Alternative sequence (1); Chain (1); Frameshift (1); Metal binding (2); Sequence conflict (3) FUNCTION: Probably catalyzes the deacetylation of acetylated carbohydrates an important step in the degradation of oligosaccharides. {ECO:0000250|UniProtKB:Q53WD3}. +Q9Z1K8 YLAT1_MOUSE Y+L amino acid transporter 1 (Solute carrier family 7 member 7) (y(+)L-type amino acid transporter 1) (Y+LAT1) (y+LAT-1) 510 55,677 Chain (1); Glycosylation (2); Modified residue (2); Natural variant (1); Transmembrane (12) TRANSMEM 38 58 Helical. {ECO:0000255}.; TRANSMEM 70 90 Helical. {ECO:0000255}.; TRANSMEM 108 128 Helical. {ECO:0000255}.; TRANSMEM 134 154 Helical. {ECO:0000255}.; TRANSMEM 161 181 Helical. {ECO:0000255}.; TRANSMEM 187 207 Helical. {ECO:0000255}.; TRANSMEM 223 243 Helical. {ECO:0000255}.; TRANSMEM 260 280 Helical. {ECO:0000255}.; TRANSMEM 305 325 Helical. {ECO:0000255}.; TRANSMEM 384 404 Helical. {ECO:0000255}.; TRANSMEM 417 437 Helical. {ECO:0000255}.; TRANSMEM 442 462 Helical. {ECO:0000255}. FUNCTION: Involved in the sodium-independent uptake of dibasic amino acids and sodium-dependent uptake of some neutral amino acids. Requires coexpression with SLC3A2/4F2hc to mediate the uptake of arginine, leucine and glutamine. Plays a role in nitric oxide synthesis via transport of L-arginine, and is involved in the transport of L-arginine in monocytes. {ECO:0000269|PubMed:9878049}. SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Disulfide-linked heterodimer with the amino acid transport protein SLC3A2/4F2hc. {ECO:0000250}. TISSUE SPECIFICITY: Strongly expressed in kidney and intestine. Weaker expression observed in epididymis, testis, ovary, thyroid pancreas, sub-gland and liver. {ECO:0000269|PubMed:9878049}. +Q8BGK6 YLAT2_MOUSE Y+L amino acid transporter 2 (Solute carrier family 7 member 6) (y(+)L-type amino acid transporter 2) (Y+LAT2) (y+LAT-2) 515 56,771 Alternative sequence (2); Chain (1); Erroneous initiation (1); Frameshift (1); Modified residue (1); Sequence conflict (2); Topological domain (13); Transmembrane (12) TRANSMEM 45 65 Helical. {ECO:0000255}.; TRANSMEM 79 99 Helical. {ECO:0000255}.; TRANSMEM 115 135 Helical. {ECO:0000255}.; TRANSMEM 168 188 Helical. {ECO:0000255}.; TRANSMEM 195 215 Helical. {ECO:0000255}.; TRANSMEM 236 256 Helical. {ECO:0000255}.; TRANSMEM 267 287 Helical. {ECO:0000255}.; TRANSMEM 312 332 Helical. {ECO:0000255}.; TRANSMEM 364 384 Helical. {ECO:0000255}.; TRANSMEM 386 406 Helical. {ECO:0000255}.; TRANSMEM 425 445 Helical. {ECO:0000255}.; TRANSMEM 452 472 Helical. {ECO:0000255}. TOPO_DOM 1 44 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 66 78 Extracellular. {ECO:0000255}.; TOPO_DOM 100 114 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 136 167 Extracellular. {ECO:0000255}.; TOPO_DOM 189 194 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 216 235 Extracellular. {ECO:0000255}.; TOPO_DOM 257 266 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 288 311 Extracellular. {ECO:0000255}.; TOPO_DOM 333 363 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 385 385 Extracellular. {ECO:0000255}.; TOPO_DOM 407 424 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 446 451 Extracellular. {ECO:0000255}.; TOPO_DOM 473 515 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in the sodium-independent uptake of dibasic amino acids and sodium-dependent uptake of some neutral amino acids. Requires coexpression with SLC3A2/4F2hc to mediate the uptake of arginine, leucine and glutamine. Also acts as an arginine/glutamine exchanger, following an antiport mechanism for amino acid transport, influencing arginine release in exchange for extracellular amino acids. Plays a role in nitric oxide synthesis via transport of L-arginine. Involved in the transport of L-arginine in monocytes. Reduces uptake of ornithine in retinal pigment epithelial cells (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000250|UniProtKB:Q92536}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q92536}. SUBUNIT: Disulfide-linked heterodimer with the amino acid transport protein SLC3A2/4F2hc. {ECO:0000250|UniProtKB:Q92536}. TISSUE SPECIFICITY: Strongest expression in brain but also detected in testis, parotis, small intestine, heart and kidney. Weakly expressed in spleen, lung and liver. {ECO:0000269|PubMed:10903140}. +Q65Z95 YPEL2_MOUSE Protein yippee-like 2 119 13,577 Chain (1); Domain (1); Metal binding (4) SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. SUBUNIT: May interact with FAM168B. {ECO:0000250}. TISSUE SPECIFICITY: Detected in testis, heart, brain, spleen, lung and liver. {ECO:0000269|PubMed:15556292}. +Q65Z93 YPEL4_MOUSE Protein yippee-like 4 127 14,315 Chain (1); Domain (1); Metal binding (4); Modified residue (3) SUBCELLULAR LOCATION: Nucleus, nucleolus. TISSUE SPECIFICITY: Detected in brain, spleen and testis. {ECO:0000269|PubMed:15556292}. +P62700 YPEL5_MOUSE Protein yippee-like 5 121 13,842 Chain (1); Domain (1); Metal binding (4); Modified residue (1) FUNCTION: Component of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1 (By similarity). Required for normal cell proliferation (By similarity). {ECO:0000250|UniProtKB:P62699, ECO:0000250|UniProtKB:Q65Z55}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q65Z55}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q65Z55}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q65Z55}. Midbody {ECO:0000250|UniProtKB:Q65Z55}. Note=Deteted in nucleus and at the centrosome during interphase. During mitosis, detected on the mitotic spindle, at spindle poles and at the midbody. {ECO:0000250|UniProtKB:Q65Z55}. SUBUNIT: Identified in the CTLH complex that contains GID4, RANBP9 and/or RANBP10, MKLN1, MAEA, RMND5A (or alternatively its paralog RMND5B), GID8, ARMC8, WDR26 and YPEL5. Within this complex, MAEA, RMND5A (or alternatively its paralog RMND5B), GID8, WDR26, and RANBP9 and/or RANBP10 form the catalytic core, while GID4, MKLN1, ARMC8 and YPEL5 have ancillary roles. Interacts with RANBP9 and RANBP10. {ECO:0000250|UniProtKB:P62699}. +Q3TNU4 YD021_MOUSE Putative uncharacterized protein ENSP00000382790 homolog 584 66,631 Chain (1) +Q6PIU9 YJ005_MOUSE Uncharacterized protein FLJ45252 homolog 354 37,705 Chain (1); Erroneous initiation (2); Modified residue (5) +Q99LW6 YAF2_MOUSE YY1-associated factor 2 179 19,655 Alternative sequence (2); Chain (1); Modified residue (1); Sequence conflict (3); Zinc finger (1) FUNCTION: Binds to MYC and inhibits MYC-mediated transactivation. Also binds to MYCN and enhances MYCN-dependent transcriptional activation. Increases calpain 2-mediated proteolysis of YY1 in vitro. Component of the E2F6.com-1 complex, a repressive complex that methylates 'Lys-9' of histone H3, suggesting that it is involved in chromatin-remodeling. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14557078}. SUBUNIT: Interacts with MYC, MYCN, RNF2/RING1B and YY1. Part of the E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1, RING1, RNF2, MBLR, L3MBTL2 and YAF2. {ECO:0000269|PubMed:14557078}. TISSUE SPECIFICITY: In the mesoderm, expressed in the region close to the surface ectoderm. {ECO:0000269|PubMed:14557078}. +Q9CX30 YIF1B_MOUSE Protein YIF1B (YIP1-interacting factor homolog B) 311 33,983 Alternative sequence (1); Chain (1); Modified residue (3); Sequence conflict (3); Topological domain (6); Transmembrane (5) TRANSMEM 154 174 Helical. {ECO:0000255}.; TRANSMEM 190 210 Helical. {ECO:0000255}.; TRANSMEM 217 237 Helical. {ECO:0000255}.; TRANSMEM 239 259 Helical. {ECO:0000255}.; TRANSMEM 290 310 Helical. {ECO:0000255}. TOPO_DOM 1 153 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 175 189 Extracellular. {ECO:0000255}.; TOPO_DOM 211 216 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 238 238 Extracellular. {ECO:0000255}.; TOPO_DOM 260 289 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 311 311 Extracellular. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9EQQ2 YIPF5_MOUSE Protein YIPF5 (YIP1 family member 5) (YPT-interacting protein 1 A) 257 27,873 Chain (1); Region (1); Topological domain (5); Transmembrane (5) TRANSMEM 125 145 Helical. {ECO:0000255}.; TRANSMEM 147 167 Helical. {ECO:0000255}.; TRANSMEM 174 194 Helical. {ECO:0000255}.; TRANSMEM 197 217 Helical. {ECO:0000255}.; TRANSMEM 237 257 Helical. {ECO:0000255}. TOPO_DOM 1 124 Cytoplasmic. {ECO:0000250|UniProtKB:Q969M3}.; TOPO_DOM 146 146 Lumenal. {ECO:0000305}.; TOPO_DOM 168 173 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 195 196 Lumenal. {ECO:0000305}.; TOPO_DOM 218 236 Cytoplasmic. {ECO:0000305}. FUNCTION: Plays a role in transport between endoplasmic reticulum and Golgi. {ECO:0000250|UniProtKB:Q969M3}. SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:15254263}; Multi-pass membrane protein {ECO:0000269|PubMed:15254263}. Cytoplasmic vesicle, COPII-coated vesicle {ECO:0000250|UniProtKB:Q5XID0}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:15254263}; Multi-pass membrane protein {ECO:0000269|PubMed:15254263}. Note=Incorporated into COPII coated vesicles (By similarity). Enriched at the endoplasmic reticulum exit sites. {ECO:0000250}. SUBUNIT: Interacts with the COPII coat components Sec23 (SEC23A and/or SEC23B) and Sec24 (SEC24A and/or SEC24B) (By similarity). Interacts with YIF1A (By similarity). May interact with RAB1A (By similarity). Interacts with YIPF3 and YIPF4 (By similarity). {ECO:0000250|UniProtKB:Q969M3}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:11489904}. +Q91XB7 YIF1A_MOUSE Protein YIF1A (YIP1-interacting factor homolog A) 293 32,134 Chain (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (2); Topological domain (5); Transmembrane (5) TRANSMEM 139 159 Helical. {ECO:0000255}.; TRANSMEM 175 195 Helical. {ECO:0000255}.; TRANSMEM 204 226 Helical. {ECO:0000255}.; TRANSMEM 230 249 Helical. {ECO:0000255}.; TRANSMEM 272 292 Helical. {ECO:0000255}. TOPO_DOM 2 138 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 160 174 Lumenal. {ECO:0000305}.; TOPO_DOM 196 203 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 227 229 Lumenal. {ECO:0000305}.; TOPO_DOM 250 271 Cytoplasmic. {ECO:0000305}. FUNCTION: Possible role in transport between endoplasmic reticulum and Golgi. {ECO:0000250|UniProtKB:O95070}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O95070}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:O95070}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:O95070}; Multi-pass membrane protein {ECO:0000255}. Note=Cycles between the endoplasmic reticulum and the endoplasmic reticulum-Golgi intermediate compartment. {ECO:0000250|UniProtKB:O95070}. SUBUNIT: Interacts with YIPF5. {ECO:0000250|UniProtKB:O95070}. +Q91VU1 YIPF1_MOUSE Protein YIPF1 (YIP1 family member 1) 306 34,258 Chain (1); Glycosylation (1); Sequence conflict (1); Topological domain (6); Transmembrane (5) TRANSMEM 120 140 Helical. {ECO:0000255}.; TRANSMEM 163 183 Helical. {ECO:0000255}.; TRANSMEM 201 221 Helical. {ECO:0000255}.; TRANSMEM 228 248 Helical. {ECO:0000255}.; TRANSMEM 257 277 Helical. {ECO:0000255}. TOPO_DOM 1 119 Cytoplasmic. {ECO:0000250|UniProtKB:Q9Y548}.; TOPO_DOM 141 162 Lumenal. {ECO:0000305}.; TOPO_DOM 184 200 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 222 227 Lumenal. {ECO:0000305}.; TOPO_DOM 249 256 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 278 306 Lumenal. {ECO:0000250|UniProtKB:Q9Y548}. SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane {ECO:0000250|UniProtKB:Q9Y548}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9Y548}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q9Y548}. Late endosome membrane {ECO:0000250|UniProtKB:Q9Y548}. Note=Mainly localizes within medial-/trans-Golgi and trans-Golgi network (TGN), while less so within cis-Golgi. {ECO:0000250|UniProtKB:Q9Y548}. SUBUNIT: Interacts with YIPF6; this interaction may stabilize YIPF1. May also form a ternary complex with YIPF2 and YIPF6. {ECO:0000250|UniProtKB:Q9Y548}. +Q9R0I7 YLPM1_MOUSE YLP motif-containing protein 1 (Nuclear protein ZAP3) 1386 155,129 Chain (1); Compositional bias (3); Cross-link (2); Erroneous initiation (1); Modified residue (1); Region (1); Sequence conflict (3) FUNCTION: Plays a role in the reduction of telomerase activity during differentiation of embryonic stem cells by binding to the core promoter of TERT and controlling its down-regulation. {ECO:0000269|PubMed:15511642}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus speckle {ECO:0000269|PubMed:10716735}. Note=Migrates to nucleolar caps upon blockage of transcription. {ECO:0000250}. SUBUNIT: Interacts with PPP1CA and NCOA5. Forms a complex with ILF2, ILF3, KHDRBS1, RBMX, NCOA5 and PPP1CA (By similarity). {ECO:0000250}. +Q9ESC7 YPEL1_MOUSE Protein yippee-like 1 (DGL-1) (Mdgl-1) 118 13,468 Chain (1); Domain (1); Metal binding (4); Motif (1) FUNCTION: May play a role in epithelioid conversion of fibroblasts. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11473580}. +Q8CII0 ZBT8B_MOUSE Zinc finger and BTB domain-containing protein 8B 484 53,387 Chain (1); Compositional bias (1); Domain (1); Sequence conflict (3); Zinc finger (2) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +A2A5E6 Z385C_MOUSE Zinc finger protein 385C 429 44,644 Alternative sequence (1); Chain (1); Compositional bias (1); Sequence conflict (4); Zinc finger (3) SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +Q04736 YES_MOUSE Tyrosine-protein kinase Yes (EC 2.7.10.2) (Proto-oncogene c-Yes) (p61-Yes) 541 60,630 Active site (1); Beta strand (14); Binding site (1); Chain (1); Domain (3); Helix (2); Initiator methionine (1); Lipidation (2); Modified residue (5); Nucleotide binding (1); Turn (3) FUNCTION: Non-receptor protein tyrosine kinase that is involved in the regulation of cell growth and survival, apoptosis, cell-cell adhesion, cytoskeleton remodeling, and differentiation. Stimulation by receptor tyrosine kinases (RTKs) including EGRF, PDGFR, CSF1R and FGFR leads to recruitment of YES1 to the phosphorylated receptor, and activation and phosphorylation of downstream substrates. Upon EGFR activation, promotes the phosphorylation of PARD3 to favor epithelial tight junction assembly. Participates in the phosphorylation of specific junctional components such as CTNND1 by stimulating the FYN and FER tyrosine kinases at cell-cell contacts. Upon T-cell stimulation by CXCL12, phosphorylates collapsin response mediator protein 2/DPYSL2 and induces T-cell migration. Participates in CD95L/FASLG signaling pathway and mediates AKT-mediated cell migration. Plays a role in cell cycle progression by phosphorylating the cyclin dependent kinase 4/CDK4 thus regulating the G1 phase. Also involved in G2/M progression and cytokinesis (By similarity). {ECO:0000250}. PTM: Phosphorylation by CSK on the C-terminal tail maintains the enzyme in an inactive state. Autophosphorylation at Tyr-424 maintains enzyme activity by blocking CSK-mediated inhibition (By similarity). {ECO:0000250}.; PTM: Palmitoylation at Cys-3 promotes membrane localization. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Note=Newly synthesized protein initially accumulates in the Golgi region and traffics to the plasma membrane through the exocytic pathway. {ECO:0000250}. SUBUNIT: Interacts with YAP1. Interacts with FASLG. Interacts with CTNND1; this interaction allows YES1-mediated activation of FYN and FER and subsequent phosphorylation of CTNND1 (By similarity). Interacts with CSF1R. {ECO:0000250, ECO:0000269|PubMed:7681396}. +Q3TUF7 YETS2_MOUSE YEATS domain-containing protein 2 1407 148,950 Alternative sequence (3); Chain (1); Coiled coil (1); Compositional bias (1); Cross-link (14); Domain (1); Erroneous initiation (1); Modified residue (14); Region (2); Sequence caution (1); Sequence conflict (3) FUNCTION: Chromatin reader component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4. YEATS2 specifically recognizes and binds histone H3 crotonylated at 'Lys-27' (H3K27cr). Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. {ECO:0000250|UniProtKB:Q9ULM3}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9ULM3}. SUBUNIT: Component of the ADA2A-containing complex (ATAC), composed of KAT14, KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, SGF29 and DR1. {ECO:0000250|UniProtKB:Q9ULM3}. DOMAIN: The YEATS domain specifically recognizes and binds crotonylated histones. {ECO:0000250|UniProtKB:Q9ULM3}. +Q91YT7 YTHD2_MOUSE YTH domain-containing family protein 2 579 62,280 Binding site (4); Chain (1); Compositional bias (1); Domain (1); Initiator methionine (1); Modified residue (9); Region (4); Sequence conflict (4) FUNCTION: Specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs, and regulates mRNA stability (PubMed:28867294). M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in mRNA stability and processing (PubMed:28867294). Acts as a regulator of mRNA stability: binding to m6A-containing mRNAs results in the localization to mRNA decay sites, such as processing bodies (P-bodies), leading to mRNA degradation (By similarity). Required maternally to regulate oocyte maturation: probably acts by binding to m6A-containing mRNAs, thereby regulating maternal transcript dosage during oocyte maturation, which is essential for the competence of oocytes to sustain early zygotic development (PubMed:28867294). Also involved in haematopoietic stem cells specification: acts by binding to m6A-containing mRNAs, leading to decrease Notch dignaling and promote endothelial to haematopoietic transition (By similarity). Also acts as a promoter of cap-independent mRNA translation following heat shock stress: upon stress, relocalizes to the nucleus and specifically binds mRNAs with some m6A methylation mark at their 5'-UTR, protecting demethylation of mRNAs by FTO, thereby promoting cap-independent mRNA translation (By similarity). {ECO:0000250|UniProtKB:E7F1H9, ECO:0000250|UniProtKB:Q9Y5A9, ECO:0000269|PubMed:28867294}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305|PubMed:28867294}. Nucleus {ECO:0000250|UniProtKB:Q9Y5A9}. Cytoplasm, P-body {ECO:0000250|UniProtKB:Q9Y5A9}. Note=Localizes to the cytosol and relocates to the nucleus following heat shock stress. {ECO:0000250|UniProtKB:Q9Y5A9}. SUBUNIT: Interacts with YTHDF3. {ECO:0000250|UniProtKB:Q9Y5A9}. TISSUE SPECIFICITY: Widely expressed, with highest expression in testis. {ECO:0000269|PubMed:28867294}. +Q61751 Z354A_MOUSE Zinc finger protein 354A (Kidney, ischemia, and developmentally-regulated protein 1) (Renal transcription factor Kid-1) (Transcription factor 17) (TCF-17) 572 65,662 Chain (1); Cross-link (3); Domain (1); Sequence conflict (1); Zinc finger (13) FUNCTION: It may play a role in renal development and may also be involved in the repair of the kidney after ischemia-reperfusion or folic acid administration. SUBCELLULAR LOCATION: Nucleus. TISSUE SPECIFICITY: Highly expressed in eye and kidney. Detected at high levels in adult brain and kidney, and at lower levels in adult liver, lung, skeletal muscle, heart, salivary gland, testis and tongue. Detected in embryonic brain, heart, lung,kidney and gut. {ECO:0000269|PubMed:10564808}. +Q571J5 Z354C_MOUSE Zinc finger protein 354C (Kidney, ischemia, and developmentally-regulated protein 3) 560 64,065 Chain (1); Cross-link (2); Domain (1); Erroneous initiation (1); Sequence conflict (4); Zinc finger (11) FUNCTION: May function as a transcription repressor. Binds to 5'-CCACA-3' core sequence. Suppresses osteogenic effects of RUNX2. May be involved in osteoblastic differentiation (By similarity). Plays a role in postnatal myogenesis, may be involved in the regulation of satellite cells self-renewal (PubMed:27446912). {ECO:0000250|UniProtKB:Q86Y25, ECO:0000250|UniProtKB:Q9EPU7, ECO:0000269|PubMed:27446912}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9EPU7}. DOMAIN: KRAB domain is not required for nuclear targeting or for DNA binding. {ECO:0000250|UniProtKB:Q9EPU7}.; DOMAIN: Zinc finger region is involved in nuclear targeting and DNA-binding. {ECO:0000250|UniProtKB:Q9EPU7}. TISSUE SPECIFICITY: Expressed in brain. Lower levels in kidney, heart, lung, spleen and eye. Down-regulated during kidney maturation. Expressed in embryonic myogenic progenitor cells, not expressed in adult and aged satellite cells (PubMed:27446912). {ECO:0000269|PubMed:10786630, ECO:0000269|PubMed:27446912}. +Q8BLB0 ZFP3_MOUSE Zinc finger protein 3 (Zfp-3) 497 56,574 Chain (1); Cross-link (2); Zinc finger (13) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q9DCH6 ZFAN6_MOUSE AN1-type zinc finger protein 6 (Associated with PRK1 protein) (Zinc finger A20 domain-containing protein 3) 223 24,001 Chain (1); Modified residue (2); Mutagenesis (2); Sequence conflict (2); Zinc finger (2) FUNCTION: Involved in regulation of TNF-alpha induced NF-kappa-B activation and apoptosis. Involved in modulation of 'Lys-48'-linked polyubiquitination status of TRAF2 and decreases association of TRAF2 with RIPK1 (By similarity). Required for PTS1 target sequence-dependent protein import into peroxisomes and PEX5 stability; may cooperate with PEX6. In vitro involved in PEX5 export from the cytosol to peroxisomes. {ECO:0000250, ECO:0000269|PubMed:21980954}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with PKN1. Interacts with TRAF2 (By similarity). Interacts with mono- and polyubiquitin. Interacts with PEX6. Interacts with PEX5 (Cys-linked ubiquitinated). {ECO:0000250, ECO:0000269|PubMed:11054541, ECO:0000269|PubMed:21980954}. DOMAIN: The A20-type zinc finger domain mediates regulation of NF-kappa-B activity. {ECO:0000250}.; DOMAIN: The AN1-type zinc finger domain mediates association with TRAF2. {ECO:0000250}. +B2RUI1 ZN551_MOUSE Zinc finger protein 551 696 79,722 Chain (1); Cross-link (1); Domain (1); Sequence conflict (2); Zinc finger (13) FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +Q8R0A2 ZBT44_MOUSE Zinc finger and BTB domain-containing protein 44 (BTB/POZ domain-containing protein 15) 453 50,175 Alternative sequence (1); Chain (1); Compositional bias (2); Cross-link (2); Domain (1); Erroneous termination (1); Modified residue (8); Zinc finger (2) SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +Q8K3J5 ZN131_MOUSE Zinc finger protein 131 619 71,022 Alternative sequence (3); Chain (1); Cross-link (3); Domain (1); Modified residue (1); Motif (2); Sequence conflict (4); Zinc finger (6) FUNCTION: May be involved in transcriptional regulation as a repressor of ESR1/ER-alpha signaling (By similarity). Plays a role during development and organogenesis as well as in the function of the adult central nervous system. {ECO:0000250, ECO:0000269|PubMed:12163020}. PTM: Monosumoylated at Lys-598 by CBX4 and UHRF2. Sumoylation may potentiate ZNF131 inhibition of estrogen signaling. Sumoylation does not interfere with ubiquitination (By similarity). {ECO:0000250}.; PTM: Ubiquitinated. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed. Predominant expression is found in the developing central nervous system with strongest signals in the forebrain, midbrain, and hindbrain areas and in the neural tube. {ECO:0000269|PubMed:12163020}. +Q6P1E1 ZMIZ1_MOUSE Zinc finger MIZ domain-containing protein 1 (PIAS-like protein Zimp10) (Retinoic acid-induced protein 17) 1072 115,851 Alternative sequence (1); Chain (1); Compositional bias (3); Cross-link (3); Erroneous initiation (1); Frameshift (1); Region (2); Sequence caution (1); Zinc finger (1) FUNCTION: Acts as transcriptional coactivator. Increases ligand-dependent transcriptional activity of AR and promotes AR sumoylation. The stimulation of AR activity is dependent upon sumoylation (By similarity). Involved in transcriptional activation of a subset of NOTCH1 target genes including MYC. Involved in thymocyte and T cell development (PubMed:26522984). {ECO:0000250|UniProtKB:Q9ULJ6, ECO:0000269|PubMed:26522984}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}. Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with AR, but not with ESR1, NR3C1, PGR, THRB nor VDR. Interacts with NOTCH1 and RBPJ (By similarity). Interacts with SMARCA4. {ECO:0000250|UniProtKB:Q9ULJ6, ECO:0000269|PubMed:26163108}. DOMAIN: The C-terminal proline-rich domain possesses a significant intrinsic transcriptional activity. This activity is inhibited by the N-terminus in the full-length protein (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain. {ECO:0000269|PubMed:26163108}. +Q6IR37 ZDH24_MOUSE Probable palmitoyltransferase ZDHHC24 (EC 2.3.1.225) (Zinc finger DHHC domain-containing protein 24) (DHHC-24) 284 30,430 Chain (1); Compositional bias (1); Domain (1); Frameshift (1); Sequence conflict (3); Transmembrane (5) TRANSMEM 19 39 Helical. {ECO:0000255}.; TRANSMEM 53 73 Helical. {ECO:0000255}.; TRANSMEM 138 158 Helical. {ECO:0000255}.; TRANSMEM 167 187 Helical. {ECO:0000255}.; TRANSMEM 196 216 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. DOMAIN: The DHHC domain is required for palmitoyltransferase activity. {ECO:0000250}. +Q9JJN2 ZFHX4_MOUSE Zinc finger homeobox protein 4 (Zinc finger homeodomain protein 4) (ZFH-4) 3550 392,323 Beta strand (1); Chain (1); Coiled coil (1); Compositional bias (6); Cross-link (5); DNA binding (4); Helix (2); Modified residue (2); Turn (1); Zinc finger (20) FUNCTION: May play a role in neural and muscle differentiation. May be involved in transcriptional regulation. {ECO:0000269|PubMed:16946494}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: Expressed in brain, heart, lung, muscle and small intestine. No expression detected in undifferentiated P19 cells, however, expression was seen following retinoic acid treatment to induce neuronal differentiation. Expressed in undifferentiated C2C12 cells, following induction of muscle differentiation in a low-serum medium, expression levels were decreased. {ECO:0000269|PubMed:10873665, ECO:0000269|PubMed:16946494}. +Q3UHF7 ZEP2_MOUSE Transcription factor HIVEP2 (Human immunodeficiency virus type I enhancer-binding protein 2 homolog) (Myc intron-binding protein 1) (MIBP-1) 2430 266,705 Chain (1); Compositional bias (4); Modified residue (11); Motif (1); Region (1); Repeat (10); Sequence conflict (14); Zinc finger (4) FUNCTION: Specifically binds to the DNA sequence 5'-GGGACTTTCC-3' which is found in the enhancer elements of numerous viral promoters such as those of SV40, CMV, or HIV1. In addition, related sequences are found in the enhancer elements of a number of cellular promoters, including those of the class I MHC, interleukin-2 receptor, somatostatin receptor II, and interferon-beta genes. It may act in T-cell activation (By similarity). {ECO:0000250, ECO:0000269|PubMed:10207097}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with TCF4. {ECO:0000269|PubMed:10207097}. TISSUE SPECIFICITY: Expressed in heart, lung, skeletal muscle and liver. In the brain expressed in cerebral cortex, hippocampus, corpora amygdala and cerebellar cortex. {ECO:0000269|PubMed:10207097}. +Q8CE64 ZN276_MOUSE Zinc finger protein 276 (Zfp-276) 614 67,339 Alternative sequence (2); Chain (1); Domain (1); Erroneous initiation (2); Sequence conflict (4); Zinc finger (5) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q8N554}. TISSUE SPECIFICITY: Found in all the examined tissues, with highest levels in kidney, liver, lung, and spleen. {ECO:0000269|PubMed:10936049}. +A2A791 ZMYM4_MOUSE Zinc finger MYM-type protein 4 (Zinc finger protein 262) 1549 172,438 Alternative sequence (1); Chain (1); Cross-link (18); Erroneous gene model prediction (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (14); Sequence conflict (1); Zinc finger (9) FUNCTION: Plays a role in the regulation of cell morphology and cytoskeletal organization. {ECO:0000250}. +Q8BY46 ZN574_MOUSE Zinc finger protein 574 900 99,461 Chain (1); Compositional bias (1); Frameshift (1); Modified residue (5); Sequence conflict (5); Zinc finger (20) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q9D115 ZN706_MOUSE Zinc finger protein 706 76 8,498 Chain (1); Mutagenesis (1); Zinc finger (1) FUNCTION: Transcription repressor involved in the exit of embryonic stem cells (ESCs) from self-renewal. Acts by repressing expression of KLF4. {ECO:0000269|PubMed:24412312}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24412312}. Nucleus {ECO:0000269|PubMed:24412312}. +Q3U288 ZN710_MOUSE Zinc finger protein 710 666 75,052 Alternative sequence (2); Chain (1); Compositional bias (2); Cross-link (3); Erroneous initiation (3); Sequence conflict (4); Zinc finger (11) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +A2ANX9 ZN711_MOUSE Zinc finger protein 711 761 86,415 Chain (1); Cross-link (3); Zinc finger (12) FUNCTION: Transcription regulator required for brain development. Probably acts as a transcription factor that binds to the promoter of target genes and recruits PHF8 histone demethylase, leading to activate expression of genes involved in neuron development, such as KDM5C (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with PHF8. {ECO:0000250}. +Q5SXI5 ZN496_MOUSE Zinc finger protein 496 (NSD1-interacting zinc finger protein 1) (Zinc finger protein with KRAB and SCAN domains 17) 585 66,577 Alternative sequence (2); Beta strand (1); Chain (1); Cross-link (2); Domain (2); Helix (2); Modified residue (1); Motif (1); Sequence conflict (1); Turn (1); Zinc finger (5) FUNCTION: DNA-binding transcription factor that can both act as an activator and a repressor. {ECO:0000269|PubMed:15169884, ECO:0000269|PubMed:17521633}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187, ECO:0000269|PubMed:15169884, ECO:0000269|PubMed:17521633}. SUBUNIT: Interacts (via zinc-fingers) with JARID2. Interacts with NSD1. {ECO:0000269|PubMed:15169884, ECO:0000269|PubMed:17521633}. DOMAIN: The C2H2-type zinc finger 1, also named C2HR, mediates the interaction with NSD1. +Q9JKN1 ZNT7_MOUSE Zinc transporter 7 (ZnT-7) (Solute carrier family 30 member 7) (Znt-like transporter 2) 378 41,790 Chain (1); Region (1); Sequence conflict (1); Topological domain (7); Transmembrane (6) TRANSMEM 38 58 Helical. {ECO:0000255}.; TRANSMEM 68 88 Helical. {ECO:0000255}.; TRANSMEM 103 123 Helical. {ECO:0000255}.; TRANSMEM 141 161 Helical. {ECO:0000255}.; TRANSMEM 239 259 Helical. {ECO:0000255}.; TRANSMEM 265 285 Helical. {ECO:0000255}. TOPO_DOM 1 37 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 59 67 Extracellular. {ECO:0000255}.; TOPO_DOM 89 102 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 124 140 Extracellular. {ECO:0000255}.; TOPO_DOM 162 238 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 260 264 Extracellular. {ECO:0000255}.; TOPO_DOM 286 378 Cytoplasmic. {ECO:0000255}. FUNCTION: Seems to facilitate zinc transport from the cytoplasm into the Golgi apparatus. Partly regulates cellular zinc homeostasis. Required with ZNT5 for the activation of zinc-requiring enzymes, alkaline phosphatases (ALPs). Transports zinc into the lumens of the Golgi apparatus and the vesicular compartments where ALPs locate, thus, converting apoALPs to holoALPs. Required with ZNT5 and ZNT6 for the activation of TNAP (By similarity). {ECO:0000250, ECO:0000269|PubMed:12446736, ECO:0000269|PubMed:17954933}. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:12446736}; Multi-pass membrane protein {ECO:0000269|PubMed:12446736}. SUBUNIT: Homooligomer. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in liver, spleen, duodenum and part of the jejunum of small intestine (at protein level). Moderately expressed in kidney, lung, and brain. Barely detectable in heart. {ECO:0000269|PubMed:12446736, ECO:0000269|PubMed:17954933}. +P20662 ZFY2_MOUSE Zinc finger Y-chromosomal protein 2 777 88,127 Chain (1); Motif (1); Sequence conflict (6); Zinc finger (12) FUNCTION: Probable transcriptional activator. Binds to the consensus sequence 5'-AGGCCY-3' (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. DOMAIN: The binding of ZFY to DNA is mediated by the interaction of the GGCC core base pairs with zinc fingers 12 and 13. {ECO:0000250}. +Q62522 ZPBP1_MOUSE Zona pellucida-binding protein 1 (Inner acrosomal membrane IAM38) (Sp38) 350 39,232 Chain (1); Erroneous initiation (1); Glycosylation (3); Signal peptide (1) FUNCTION: Plays a role in acrosome compaction and sperm morphogenesis. Is implicated in sperm-oocyte interaction during fertilization. {ECO:0000269|PubMed:17664285}. PTM: N-glycosylated. {ECO:0000269|PubMed:17664285, ECO:0000269|PubMed:19204925}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome membrane {ECO:0000269|PubMed:17664285, ECO:0000269|PubMed:19204925}; Peripheral membrane protein {ECO:0000305|PubMed:19204925}. Secreted {ECO:0000305}. Note=First localized in acrosome granule, later migrates to the inner and outer acrosomal membrane (PubMed:19204925). Released after the acrosomal reaction (PubMed:17664285). {ECO:0000269|PubMed:17664285, ECO:0000269|PubMed:19204925}. TISSUE SPECIFICITY: Expressed in testis (at protein level) (PubMed:19204925). Expressed in male germ cells (PubMed:17664285). {ECO:0000269|PubMed:17664285, ECO:0000269|PubMed:19204925}. +Q8BGZ8 ZPLD1_MOUSE Zona pellucida-like domain-containing protein 1 (ZP domain-containing protein 1) (Cupulin) [Cleaved into: Zona pellucida-like domain-containing protein 1, secreted form] 415 45,448 Chain (2); Disulfide bond (4); Domain (1); Glycosylation (1); Sequence conflict (2); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 374 394 Helical. {ECO:0000255}. TOPO_DOM 20 373 Extracellular. {ECO:0000255}.; TOPO_DOM 395 415 Cytoplasmic. {ECO:0000255}. FUNCTION: Glycoprotein which is a component of the gelatinous extracellular matrix in the cupulae of the vestibular organ. {ECO:0000250|UniProtKB:C0H9B6}. PTM: Proteolytically cleaved before the transmembrane segment to yield the secreted form found in the extracellular matrix of the cupula. {ECO:0000250|UniProtKB:C0H9B6}. SUBCELLULAR LOCATION: Zona pellucida-like domain-containing protein 1: Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:C0H9B6}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: Zona pellucida-like domain-containing protein 1, secreted form: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:C0H9B6}. +Q5RJ54 ZSC26_MOUSE Zinc finger and SCAN domain-containing protein 26 (Zinc finger protein 187) 466 53,526 Alternative sequence (1); Chain (1); Cross-link (1); Domain (1); Zinc finger (8) FUNCTION: May be involved in transcriptional regulation. {ECO:0000305}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}. +Q7M760 ZRAN1_MOUSE Ubiquitin thioesterase Zranb1 (EC 3.4.19.12) (Zinc finger Ran-binding domain-containing protein 1) 708 80,934 Active site (2); Chain (1); Domain (1); Repeat (2); Zinc finger (3) FUNCTION: Specifically hydrolyzes 'Lys-29'-linked and 'Lys-33'-linked diubiquitin. Also cleaves 'Lys-63'-linked chains, but with 40-fold less efficiency compared to 'Lys-29'-linked ones. Positive regulator of the Wnt signaling pathway that deubiquitinates APC protein, a negative regulator of Wnt-mediated transcription. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the stress fiber dynamics and cell migration. May also modulate TNF-alpha signaling (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Enriched in punctate localization in the cytoplasm. {ECO:0000250}. SUBUNIT: Interacts with APC and TRAF6. {ECO:0000250}. DOMAIN: The OTU domain mediates the deubiquitinating activity. {ECO:0000250}.; DOMAIN: The RanBP2-type zinc fingers mediate the specific interaction with 'Lys-63'-linked ubiquitin. {ECO:0000250}.; DOMAIN: The second ankyrin repeat ANK 2 is termed AnkUBD, it interacts with ubiquitin hydrophobic patch and contributes to linkage specificity. {ECO:0000250}.; DOMAIN: The RanBP2-type zinc fingers, also called NZFs, may provide additional ubiquitin-binding sites when hydrolyzing long 'Lys-63'-linked chains. {ECO:0000250}. +Q80VJ6 ZSC4C_MOUSE Zinc finger and SCAN domain containing protein 4C 506 57,600 Chain (1); Domain (1); Zinc finger (4) FUNCTION: Embryonic stem (ES) cell-specific transcription factor required to regulate ES cell pluripotency. Binds telomeres and plays a key role in genomic stability in ES cells by regulating telomere elongation. Acts as an activator of spontaneous telomere sister chromatid exchange (T-SCE) and telomere elongation in undifferentiated ES cells. {ECO:0000269|PubMed:17553482, ECO:0000269|PubMed:19350676, ECO:0000269|PubMed:20336070}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187, ECO:0000269|PubMed:20336070}. Chromosome, telomere {ECO:0000269|PubMed:20336070}. TISSUE SPECIFICITY: Embryonic stem (ES) cell-specific. Expressed in only 5% of ES cells at a given time, but nearly all ES cells express it at least once during 9 passages. {ECO:0000269|PubMed:17553482, ECO:0000269|PubMed:20336070}. +Q80SU3 ZAR1_MOUSE Zygote arrest protein 1 (Oocyte-specific maternal effect factor) 361 39,986 Chain (1) FUNCTION: Essential for female fertility. May play a role in the oocyte-to-embryo transition. {ECO:0000269|PubMed:12539046}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12539046}. TISSUE SPECIFICITY: Ovary. Expressed in primary oocytes (from primary through antral follicle stages) and during the progression from Meiosis I to Meiosis II. The mRNA is detected in growing oocytes (early primary follicle, type 3a) through fully grown oocytes (antral follicle, type 8). {ECO:0000269|PubMed:12539046, ECO:0000269|PubMed:12773403}. +Q8R173 ZDHC3_MOUSE Palmitoyltransferase ZDHHC3 (EC 2.3.1.225) (GABA-A receptor-associated membrane protein 1) (Golgi-specific DHHC zinc finger protein) (Zinc finger DHHC domain-containing protein 3) (DHHC-3) 299 34,041 Active site (1); Chain (1); Domain (1); Mutagenesis (1); Sequence conflict (1); Topological domain (5); Transmembrane (4) TRANSMEM 48 68 Helical. {ECO:0000255}.; TRANSMEM 73 93 Helical. {ECO:0000255}.; TRANSMEM 172 192 Helical. {ECO:0000255}.; TRANSMEM 215 235 Helical. {ECO:0000255}. TOPO_DOM 1 47 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 69 72 Lumenal. {ECO:0000255}.; TOPO_DOM 94 171 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 193 214 Lumenal. {ECO:0000255}.; TOPO_DOM 236 299 Cytoplasmic. {ECO:0000255}. FUNCTION: Palmitoyltransferase with broad specificity. Palmitoylates GABA receptors on their gamma subunit (GABRG1, GABRG2 and GABRG3), which regulates synaptic clustering and/or cell surface stability (PubMed:15229235). Palmitoylates glutamate receptors GRIA1 and GRIA2, which leads to their retention in Golgi (PubMed:16129400). May also palmitoylate DLG4, DNAJC5 and SNAP25 (PubMed:15603741, PubMed:25253725). {ECO:0000269|PubMed:15229235, ECO:0000269|PubMed:15603741, ECO:0000269|PubMed:16129400, ECO:0000269|PubMed:25253725}. PTM: Autopalmitoylated. {ECO:0000269|PubMed:15229235, ECO:0000269|PubMed:16129400, ECO:0000269|PubMed:25253725}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:12163046, ECO:0000269|PubMed:15229235, ECO:0000269|PubMed:16129400}; Multi-pass membrane protein {ECO:0000255}. DOMAIN: The DHHC domain is required for palmitoyltransferase activity. {ECO:0000250|UniProtKB:Q8IUH5}. TISSUE SPECIFICITY: Widely expressed, with highest levels in brain. In the brain, expressed only in neurons (at protein level). {ECO:0000269|PubMed:12163046, ECO:0000269|PubMed:15229235, ECO:0000269|PubMed:15603741}. +Q8CDC7 ZBTB9_MOUSE Zinc finger and BTB domain-containing protein 9 459 49,536 Chain (1); Cross-link (3); Domain (1); Sequence conflict (2); Zinc finger (2) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +P10078 ZFP28_MOUSE Zinc finger protein 28 (Zfp-28) (Protein mKR5) 825 93,309 Alternative sequence (1); Chain (1); Domain (1); Natural variant (1); Sequence conflict (11); Zinc finger (15) FUNCTION: May be involved in transcriptional regulation. May have a role in embryonic development. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: Expressed predominantly in ovary. +P08043 ZFP2_MOUSE Zinc finger protein 2 (Zfp-2) (Protein mKR2) 459 52,534 Alternative sequence (1); Chain (1); Frameshift (1); Sequence conflict (6); Zinc finger (13) FUNCTION: Probable transcription factor involved in neuronal differentiation and/or phenotypic maintenance. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +P22227 ZFP42_MOUSE Zinc finger protein 42 (Zfp-42) (Reduced expression protein 1) (REX-1) (mREX-1) 288 32,398 Chain (1); Compositional bias (1); Cross-link (2); Sequence conflict (4); Zinc finger (4) FUNCTION: Involved in the reprogramming of X-chromosome inactivation during the acquisition of pluripotency. Required for efficient elongation of TSIX, a non-coding RNA antisense to XIST. Binds DXPas34 enhancer within the TSIX promoter. Involved in ES cell self-renewal. {ECO:0000269|PubMed:16960129, ECO:0000269|PubMed:21085182}. PTM: Polyubiquitinated by RNF12, leading to proteasomal degradation. {ECO:0000269|PubMed:22596162}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16960129}. TISSUE SPECIFICITY: Restricted to testis, to germ cells in the early stages of spermatogenesis. Not expressed in spermatids, nor spermatozoa. Expressed in embryonic stem (ES) cells. {ECO:0000269|PubMed:15749260, ECO:0000269|PubMed:16908534, ECO:0000269|PubMed:16960129, ECO:0000269|PubMed:1821852}. +P16373 ZFP59_MOUSE Zinc finger protein 59 (Zfp-59) (Zinc finger protein Mfg-2) 634 72,538 Chain (1); Domain (1); Sequence conflict (1); Zinc finger (16) FUNCTION: May have a role during differentiation processes. {ECO:0000269|PubMed:8547218}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8547218}. TISSUE SPECIFICITY: Expressed predominantly in the testis. +Q99KE8 ZFP64_MOUSE Zinc finger protein 64 (Zfp-64) 643 71,765 Alternative sequence (5); Chain (1); Compositional bias (1); Metal binding (8); Sequence conflict (5); Zinc finger (12) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9034307}. +Q62521 ZIC3_MOUSE Zinc finger protein ZIC 3 (Zinc finger protein of the cerebellum 3) 466 50,446 Alternative sequence (1); Chain (1); Compositional bias (2); Cross-link (1); Motif (2); Sequence conflict (2); Zinc finger (5) FUNCTION: Acts as transcriptional activator. Required in the earliest stages in both axial midline development and left-right (LR) asymmetry specification. Binds to the minimal GLI-consensus sequence 5'-GGGTGGTC-3'. {ECO:0000269|PubMed:11053430, ECO:0000269|PubMed:11959836, ECO:0000269|PubMed:15207726}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11238441}. Cytoplasm {ECO:0000269|PubMed:11238441}. Note=Translocation to the nucleus requires KPNA1 or KPNA6 (By similarity). Localizes in the cytoplasm in presence of MDFIC overexpression. {ECO:0000250}. SUBUNIT: Interacts with KPNA1 and KPNA6. Interacts (via C2H2-type domains 3, 4 and 5) with GLI3; the interaction enhances its transcriptional activity (By similarity). Interacts (via the C2H2-type domains 3, 4 and 5) with MDFIC (via the C2H2-type domains 3, 4 and 5); the interaction reduces its transcriptional activity. {ECO:0000250, ECO:0000269|PubMed:15207726}. DOMAIN: The C2H2-type 3, 4 and 5 zinc finger domains are necessary for transcription activation. TISSUE SPECIFICITY: CNS. A high level expression is seen in the cerebellum. +Q8R4H9 ZNT5_MOUSE Zinc transporter 5 (ZnT-5) (Solute carrier family 30 member 5) 761 83,773 Chain (1); Erroneous initiation (1); Modified residue (1); Region (1); Topological domain (17); Transmembrane (16) TRANSMEM 30 46 Helical. {ECO:0000255}.; TRANSMEM 55 75 Helical. {ECO:0000255}.; TRANSMEM 97 117 Helical. {ECO:0000255}.; TRANSMEM 119 139 Helical. {ECO:0000255}.; TRANSMEM 151 171 Helical. {ECO:0000255}.; TRANSMEM 192 212 Helical. {ECO:0000255}.; TRANSMEM 237 257 Helical. {ECO:0000255}.; TRANSMEM 265 285 Helical. {ECO:0000255}.; TRANSMEM 302 322 Helical. {ECO:0000255}.; TRANSMEM 341 361 Helical. {ECO:0000255}.; TRANSMEM 417 437 Helical. {ECO:0000255}.; TRANSMEM 447 467 Helical. {ECO:0000255}.; TRANSMEM 482 502 Helical. {ECO:0000255}.; TRANSMEM 519 539 Helical. {ECO:0000255}.; TRANSMEM 589 609 Helical. {ECO:0000255}.; TRANSMEM 614 634 Helical. {ECO:0000255}. TOPO_DOM 1 29 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 47 54 Exoplasmic loop. {ECO:0000255}.; TOPO_DOM 76 96 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 118 118 Exoplasmic loop. {ECO:0000255}.; TOPO_DOM 140 150 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 172 191 Exoplasmic loop. {ECO:0000255}.; TOPO_DOM 213 236 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 258 264 Exoplasmic loop. {ECO:0000255}.; TOPO_DOM 286 301 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 323 340 Exoplasmic loop. {ECO:0000255}.; TOPO_DOM 362 416 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 438 446 Exoplasmic loop. {ECO:0000255}.; TOPO_DOM 468 481 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 503 518 Exoplasmic loop. {ECO:0000255}.; TOPO_DOM 540 588 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 610 613 Exoplasmic loop. {ECO:0000255}.; TOPO_DOM 635 761 Cytoplasmic. {ECO:0000255}. FUNCTION: Functions as a zinc transporter. May be a transporter of zinc into beta cells in order to form insulin crystals. Partly regulates cellular zinc homeostasis. Required with ZNT7 for the activation of zinc-requiring enzymes, alkaline phosphatases (ALPs). Transports zinc into the lumens of the Golgi apparatus and vesicular compartments where ALPs locate, thus, converting apoALPs to holoALPs. Required with ZNT6 and ZNT7 for the activation of TNAP (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Perimeter of granules, localizes to the brush border membrane of the enterocyte. Concentrated in early compartments of the secretory pathway such as COPII-coated vesicles (By similarity). {ECO:0000250}. SUBUNIT: Heterooligomer. Interacts with ZNT6 (By similarity). {ECO:0000250}. +Q8BPP0 ZN436_MOUSE Zinc finger protein 436 (Zinc finger protein 46) (Zfp-46) (Zinc finger protein MLZ-4) 452 52,363 Chain (1); Cross-link (1); Domain (1); Erroneous initiation (2); Sequence conflict (2); Zinc finger (12) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: Lens, liver, heart, kidney, spleen and brain. {ECO:0000269|PubMed:8444344}. +Q8BI99 ZN879_MOUSE Zinc finger protein 879 563 64,066 Chain (1); Domain (1); Zinc finger (13) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q8BHZ4 ZN592_MOUSE Zinc finger protein 592 (Zfp-592) 1262 137,514 Chain (1); Compositional bias (1); Cross-link (3); Erroneous initiation (1); Frameshift (1); Modified residue (10); Sequence conflict (4); Zinc finger (13) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: Expressed in the brain. {ECO:0000269|PubMed:20531441}. +Q5IRJ6 ZNT9_MOUSE Zinc transporter 9 (ZnT-9) (GRIP1-associated coactivator 63) (GAC63) (Solute carrier family 30 member 9) 567 62,875 Alternative sequence (1); Chain (1); Motif (1); Sequence conflict (4); Transmembrane (5) TRANSMEM 238 258 Helical. {ECO:0000255}.; TRANSMEM 313 333 Helical. {ECO:0000255}.; TRANSMEM 341 361 Helical. {ECO:0000255}.; TRANSMEM 391 411 Helical. {ECO:0000255}.; TRANSMEM 423 443 Helical. {ECO:0000255}. FUNCTION: Acts as a zinc transporter involved in intracellular zinc homeostasis (By similarity). Functions as a secondary coactivator for nuclear receptors by cooperating with p160 coactivators subtypes (PubMed:15988012). Plays a role in transcriptional activation of Wnt-responsive genes (PubMed:17344318). {ECO:0000250|UniProtKB:Q6PML9, ECO:0000269|PubMed:15988012, ECO:0000269|PubMed:17344318}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. Nucleus {ECO:0000269|PubMed:11906820}. Cytoplasm {ECO:0000250|UniProtKB:Q6PML9}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q6PML9}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q6PML9}. Note=Mainly in the cytoplasm. Partial co-localization with endoplasmic reticulum. {ECO:0000250|UniProtKB:Q6PML9}. SUBUNIT: Interacts with GRIP1, ESR1, AR and CTNNB1. {ECO:0000269|PubMed:15988012, ECO:0000269|PubMed:17344318}. +Q69Z99 ZN512_MOUSE Zinc finger protein 512 562 63,908 Chain (1); Cross-link (4); Erroneous initiation (1); Sequence conflict (6); Zinc finger (3) FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q8BH05 ZN750_MOUSE Zinc finger protein 750 703 76,645 Chain (1); Sequence conflict (3); Zinc finger (1) FUNCTION: Transcription factor involved in epidermis differentiation. Required for terminal epidermal differentiation: acts downstream of p63/TP63 and activates expression of late epidermal differentiation genes. Specifically binds to the promoter of KLF4 and promotes its expression (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +Q8R1N0 ZN830_MOUSE Zinc finger protein 830 (Coiled-coil domain-containing protein 16) (Ovus mutant candidate gene 1 protein) 363 40,658 Chain (1); Coiled coil (2); Initiator methionine (1); Modified residue (4); Sequence conflict (4); Zinc finger (1) FUNCTION: May play a role in pre-mRNA splicing as component of the spliceosome (By similarity). Acts as an important regulator of the cell cycle that participates in the maintenance of genome integrity (PubMed:21191184, PubMed:23213458, PubMed:25168238, PubMed:15988037). During cell cycle progression in embryonic fibroblast, prevents replication fork collapse, double-strand break formation and cell cycle checkpoint activation (PubMed:21191184). Controls mitotic cell cycle progression and cell survival in rapidly proliferating intestinal epithelium and embryonic stem cells (PubMed:23213458). During the embryo preimplantation, controls different aspects of M phase (PubMed:15988037). During early oocyte growth, plays a role in oocyte survival by preventing chromosomal breaks formation, activation of TP63 and reduction of transcription (PubMed:25168238). {ECO:0000250|UniProtKB:Q96NB3, ECO:0000269|PubMed:15988037, ECO:0000269|PubMed:21191184, ECO:0000269|PubMed:23213458, ECO:0000269|PubMed:25168238}. PTM: Phosphorylated in response to DNA damage by the cell cycle checkpoint kinases ATR/ATM. {ECO:0000269|PubMed:21191184}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15988037}. Chromosome {ECO:0000269|PubMed:15988037}. Nucleus speckle {ECO:0000269|PubMed:21191184}. Note=Excluded from nucleolus. In metaphase II oocytes and in mitotic blastomeres, it is detected in cytoplasm, suggesting that it is not associated with chromosomes during mitosis. {ECO:0000269|PubMed:15988037}. SUBUNIT: Component of the XAB2 complex, a multimeric protein complex composed of XAB2, PRPF19, AQR, ZNF830, ISY1, and PPIE; this complex binds preferentially to RNA. Interacts with XAB2. Identified in a pentameric intron-binding (IB) complex composed of AQR, XAB2, ISY1, ZNF830 and PPIE that is incorporated into the spliceosome as a preassembled complex. The IB complex does not contain PRPF19. {ECO:0000250|UniProtKB:Q96NB3}. TISSUE SPECIFICITY: Widely expressed at low level. Expressed in oocytes from primordial to antral follicles. Also detected in somatic cells of the ovary, namely, in granulosa cells from the pre-antral follicle stage onward (PubMed:25168238). {ECO:0000269|PubMed:15988037, ECO:0000269|PubMed:25168238}. +Q8R060 ZWILC_MOUSE Protein zwilch homolog 589 66,839 Chain (1); Modified residue (1); Sequence conflict (3) FUNCTION: Essential component of the mitotic checkpoint, which prevents cells from prematurely exiting mitosis. Required for the assembly of the dynein-dynactin and MAD1-MAD2 complexes onto kinetochores. Its function related to the spindle assembly machinery is proposed to depend on its association in the mitotic RZZ complex (By similarity). {ECO:0000250|UniProtKB:Q9H900}. SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q9H900}. SUBUNIT: Component of the RZZ complex composed of KNTC1/ROD, ZW10 and ZWILCH; in the complex interacts directly with KNTC1/ROD (By similarity). {ECO:0000250|UniProtKB:Q9H900}. +Q3T9Z9 ZUP1_MOUSE Zinc finger-containing ubiquitin peptidase 1 (EC 3.4.19.12) (Lys-63-specific deubiquitinase ZUFSP) (DUB) (Zinc finger with UFM1-specific peptidase domain protein) 577 65,593 Active site (3); Alternative sequence (4); Chain (1); Frameshift (1); Modified residue (1); Region (2); Sequence conflict (3); Site (1); Zinc finger (4) FUNCTION: Deubiquitinase with endodeubiquitinase activity that specifically interacts with and cleaves 'Lys-63'-linked long polyubiquitin chains. Shows only weak activity against 'Lys-11' and 'Lys-48'-linked chains. Plays an important role in genome stability pathways, functioning to prevent spontaneous DNA damage and also promote cellular survival in response to exogenous DNA damage. Modulates the ubiquitination status of replication protein A (RPA) complex proteins in response to replication stress. {ECO:0000250|UniProtKB:Q96AP4}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96AP4}. Nucleus {ECO:0000250|UniProtKB:Q96AP4}. Note=Mostly present in the nuclear fraction. Localizes to DNA lesions. {ECO:0000250|UniProtKB:Q96AP4}. SUBUNIT: Interacts with RPA1 and RPA2. {ECO:0000250|UniProtKB:Q96AP4}. DOMAIN: The motif interacting with ubiquitin (MIU) and ZUFSP ubiquitin-binding domain (zUBD, also called ZUFSP helical arm ZHA) are responsible for binding the distal (outgoing) ubiquitin units S1 and S2 respectively. {ECO:0000250|UniProtKB:Q96AP4}.; DOMAIN: C2H2-type zinc finger 4 is a ubiquitin-binding zinc finger (UBZ) and required for polyubiquitin binding, possibly binding the proximal ubiqutin, and for catalytic activity. C2H2-type zinc fingers 1-3 are required for localization to sites of DNA damage. {ECO:0000250|UniProtKB:Q96AP4}. +A7KBS4 ZSC4D_MOUSE Zinc finger and SCAN domain containing protein 4D 506 58,000 Chain (1); Domain (1); Zinc finger (4) FUNCTION: Transcription factor required to regulate early development. Binds telomeres and plays a key role in genomic stability by regulating telomere elongation. Acts as an activator of spontaneous telomere sister chromatid exchange (T-SCE) and telomere elongation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}. Chromosome, telomere {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed at the 2-cell stage but its expression is rapidly turned off. {ECO:0000269|PubMed:17553482}. +Q3UDR8 YIPF3_MOUSE Protein YIPF3 (Killer lineage protein 1) (YIP1 family member 3) [Cleaved into: Protein YIPF3, N-terminally processed] 347 37,998 Chain (2); Erroneous initiation (1); Glycosylation (1); Initiator methionine (1); Modified residue (1); Sequence conflict (1); Topological domain (6); Transmembrane (5) TRANSMEM 146 166 Helical. {ECO:0000255}.; TRANSMEM 185 205 Helical. {ECO:0000255}.; TRANSMEM 212 234 Helical. {ECO:0000255}.; TRANSMEM 238 260 Helical. {ECO:0000255}.; TRANSMEM 272 292 Helical. {ECO:0000255}. TOPO_DOM 2 145 Cytoplasmic. {ECO:0000250|UniProtKB:Q9GZM5}.; TOPO_DOM 167 184 Lumenal. {ECO:0000305}.; TOPO_DOM 206 211 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 235 237 Lumenal. {ECO:0000305}.; TOPO_DOM 261 271 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 293 347 Lumenal. {ECO:0000250|UniProtKB:Q9GZM5}. FUNCTION: Involved in the maintenance of the Golgi structure. May play a role in hematopoiesis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein. Golgi apparatus, cis-Golgi network membrane {ECO:0000250}; Multi-pass membrane protein. Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with YIPF4 and YIPF5. {ECO:0000250|UniProtKB:Q9GZM5}. TISSUE SPECIFICITY: Expressed by splenocytes (at protein level). {ECO:0000269|PubMed:12490290}. +O54836 ZMAT3_MOUSE Zinc finger matrin-type protein 3 (Wild-type p53-induced gene 1 protein) (Zinc finger protein WIG-1) (p53-activated gene 608 protein) 290 32,001 Chain (1); Zinc finger (3) FUNCTION: Acts as a bona fide target gene of p53/TP53. May play a role in the TP53-dependent growth regulatory pathway. May contribute to TP53-mediated apoptosis by regulation of TP53 expression and translocation to the nucleus and nucleolus. {ECO:0000269|PubMed:12135743}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O08781}. Nucleus, nucleolus {ECO:0000250|UniProtKB:O08781}. SUBUNIT: Interacts with dsRNA. {ECO:0000250|UniProtKB:Q9HA38}. TISSUE SPECIFICITY: Constitutively expressed in brain and testis. Also expressed in lung, kidney and spleen after whole body gamma irradiation. {ECO:0000269|PubMed:9400996}. +Q8BGS3 ZKSC1_MOUSE Zinc finger protein with KRAB and SCAN domains 1 561 63,439 Alternative sequence (1); Chain (1); Cross-link (12); Domain (2); Frameshift (1); Modified residue (1); Sequence conflict (1); Zinc finger (6) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}. +Q62511 ZFP91_MOUSE E3 ubiquitin-protein ligase ZFP91 (EC 2.3.2.27) (Penta Zf protein) (RING-type E3 ubiquitin transferase ZFP91) (Zinc finger protein 91 homolog) (Zfp-91) (Zinc finger protein PZF) 572 63,389 Alternative sequence (2); Chain (1); Compositional bias (1); Erroneous initiation (1); Frameshift (2); Modified residue (2); Region (1); Sequence conflict (10); Zinc finger (5) Protein modification; protein ubiquitination. FUNCTION: Atypical E3 ubiquitin-protein ligase that mediates 'Lys-63'-linked ubiquitination of MAP3K14/NIK, leading to stabilize and activate MAP3K14/NIK. It thereby acts as an activator of the non-canonical NF-kappa-B2/NFKB2 pathway. May also play an important role in cell proliferation and/or anti-apoptosis. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Interacts with MAP3K14/NIK. {ECO:0000250}. TISSUE SPECIFICITY: Found in all the examined tissues including brain, heart, kidney, lung, liver, spleen, thymus, skeletal muscle, ovary and testis. {ECO:0000269|PubMed:7835706}. +Q9CZA5 ZCH12_MOUSE Zinc finger CCHC domain-containing protein 12 (Smad-interacting zinc finger protein 1) 402 45,107 Chain (1); Compositional bias (1); Zinc finger (1) FUNCTION: Transcriptional coactivator in the bone morphogenetic protein (BMP)-signaling pathway. It positively modulates BMP signaling by interacting with SMAD1 and associating with CBP in the transcription complex. It contributes to the BMP-induced enhancement of cholinergic-neuron-specific gene expression. {ECO:0000269|PubMed:18160706}. SUBUNIT: Interacts with SMAD1 and CREB-binding protein (CBP). Forms a protein-DNA complex through its association with SMAD1. {ECO:0000269|PubMed:18160706}. TISSUE SPECIFICITY: In embryonic brains expression is restricted to the ventral region of the forebrain, including the septum, amygdala, caudal putamen, and in the basal-forebrain cholinergic neurons. In adults, expressed in the brain, and at low levels in the testis. {ECO:0000269|PubMed:18160706}. +Q8BKX7 ZN410_MOUSE Zinc finger protein 410 (Another partner for ARF 1) (Zinc finger protein APA-1) 478 52,208 Alternative sequence (4); Chain (1); Sequence conflict (5); Zinc finger (5) FUNCTION: Transcription factor that activates transcription of matrix-remodeling genes such as MMP1 during fibroblast senescence. {ECO:0000250}. PTM: Sumoylated. Sumoylation increases its half-life, possibly by blocking ubiquitin-mediated degradation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Interacts with CDKN2A/p14ARF. {ECO:0000250}. +Q8BJH1 ZC21A_MOUSE Zinc finger C2HC domain-containing protein 1A 324 35,152 Alternative sequence (1); Chain (1); Modified residue (3); Zinc finger (1) +Q9JLM4 ZMYM3_MOUSE Zinc finger MYM-type protein 3 (DXHXS6673E protein) (Zinc finger protein 261) 1370 152,879 Chain (1); Cross-link (10); Erroneous initiation (1); Modified residue (5); Sequence conflict (3); Zinc finger (9) FUNCTION: Plays a role in the regulation of cell morphology and cytoskeletal organization. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10662551}. SUBUNIT: May be a component of a BHC histone deacetylase complex that contains HDAC1, HDAC2, HMG20B/BRAF35, KDM1A, RCOR1/CoREST, PHF21A/BHC80, ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed in all embryonic stages and adult tissues. {ECO:0000269|PubMed:10662551}. +Q7TSH9 ZN184_MOUSE Zinc finger protein 184 737 84,027 Chain (1); Cross-link (1); Domain (1); Modified residue (1); Zinc finger (19) FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +Q0VAW7 ZN112_MOUSE Zinc finger protein 112 (Zfp-112) 879 98,510 Alternative sequence (1); Chain (1); Domain (1); Sequence conflict (7); Zinc finger (12) FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q3TXZ1 ZN575_MOUSE Zinc finger protein 575 239 26,282 Chain (1); Zinc finger (6) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q9DAB9 YJ017_MOUSE Putative uncharacterized protein LOC439951 homolog 146 15,492 Chain (1) +Q8C407 YIPF4_MOUSE Protein YIPF4 (YIP1 family member 4) 246 27,283 Alternative sequence (1); Chain (1); Topological domain (5); Transmembrane (5) TRANSMEM 116 136 Helical. {ECO:0000255}.; TRANSMEM 141 161 Helical. {ECO:0000255}.; TRANSMEM 169 189 Helical. {ECO:0000255}.; TRANSMEM 198 218 Helical. {ECO:0000255}.; TRANSMEM 226 246 Helical. {ECO:0000255}. TOPO_DOM 1 115 Cytoplasmic. {ECO:0000250|UniProtKB:Q9BSR8}.; TOPO_DOM 137 140 Lumenal. {ECO:0000305}.; TOPO_DOM 162 168 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 190 197 Lumenal. {ECO:0000305}.; TOPO_DOM 219 225 Cytoplasmic. {ECO:0000305}. FUNCTION: Involved in the maintenance of the Golgi structure. {ECO:0000250|UniProtKB:Q9BSR8}. SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane {ECO:0000250|UniProtKB:Q9BSR8}; Multi-pass membrane protein. SUBUNIT: Interacts with YIPF3 and YIPF5. {ECO:0000250|UniProtKB:Q9BSR8}. +Q9CQW1 YKT6_MOUSE Synaptobrevin homolog YKT6 (EC 2.3.1.-) 198 22,314 Chain (1); Domain (2); Lipidation (2); Modified residue (2); Propeptide (1); Sequence conflict (2) FUNCTION: Vesicular soluble NSF attachment protein receptor (v-SNARE) mediating vesicle docking and fusion to a specific acceptor cellular compartment. Functions in endoplasmic reticulum to Golgi transport; as part of a SNARE complex composed of GOSR1, GOSR2 and STX5. Functions in early/recycling endosome to TGN transport; as part of a SNARE complex composed of BET1L, GOSR1 and STX5. Has a S-palmitoyl transferase activity. {ECO:0000250|UniProtKB:O15498}. PTM: Palmitoylated; catalyzes its own palmitoylation. Palmitoylation is required for Golgi targeting. {ECO:0000250|UniProtKB:O15498}.; PTM: Farnesylation is required for Golgi targeting. {ECO:0000250|UniProtKB:O15498}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Probably cycles through vesicles between Golgi and endosomes. {ECO:0000250}. SUBUNIT: Identified in 2 different SNARE complexes; the first one composed of GOSR1, GOSR2 and STX5 and the second one composed of BET1L, GOSR1 and STX5. {ECO:0000250}. DOMAIN: The longin domain regulates palmitoylation and membrane targeting. {ECO:0000250}. +Q9D6J3 YJU2_MOUSE YJU2 splicing factor homolog (Coiled-coil domain-containing protein 94) 314 35,988 Chain (1); Coiled coil (1); Modified residue (6) FUNCTION: Part of the catalytic step I spliceosome, C complex. May protect cells from TP53-dependent apoptosis upon dsDNA break damage through association with PRP19-CD5L complex. {ECO:0000250|UniProtKB:Q9BW85}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BW85}. SUBUNIT: Part of the spliceosome C complex; in the complex interacts directly with PRP16. {ECO:0000250|UniProtKB:Q9BW85}. +Q8BYK6 YTHD3_MOUSE YTH domain-containing family protein 3 585 63,961 Alternative sequence (2); Binding site (4); Chain (1); Compositional bias (3); Domain (1); Initiator methionine (1); Modified residue (2); Region (2); Sequence conflict (3) FUNCTION: Specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs and promotes RNA translation efficiency. M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in the efficiency of mRNA splicing, processing and stability. Shares m6A-containing mRNAs targets with YTHDF1 and YTHDF2, and regulates different processes depending on the context. Facilitates the translation of targeted mRNAs in cooperation with YTHDF1 by binding to m6A-containing mRNAs and interacting with 40S and 60S ribosome subunits. Can also act as a regulator of mRNA stability in cooperation with YTHDF2 by binding to m6A-containing mRNA and promoting their degradation. Recognizes and binds m6A-containing circular RNAs (circRNAs) and promotes their translation. circRNAs are generated through back-splicing of pre-mRNAs, a non-canonical splicing process promoted by dsRNA structures across circularizing exons. {ECO:0000250|UniProtKB:Q7Z739}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q7Z739}. SUBUNIT: Interacts with YTHDF1. Interacts with YTHDF2. {ECO:0000250|UniProtKB:Q7Z739}. +Q69ZB8 ZCHC2_MOUSE Zinc finger CCHC domain-containing protein 2 1166 124,517 Alternative sequence (1); Chain (1); Compositional bias (2); Zinc finger (1) +Q9JJ48 ZC3H8_MOUSE Zinc finger CCCH domain-containing protein 8 (Fetal liver zinc finger protein 1) 305 34,913 Chain (1); Cross-link (1); Modified residue (4); Sequence conflict (1); Zinc finger (3) FUNCTION: Component of the little elongation complex (LEC), a complex required to regulate small nuclear RNA (snRNA) gene transcription by RNA polymerase II and III. Acts as a transcriptional repressor of the GATA3 promoter. Induces thymocyte apoptosis when overexpressed, which may indicate a role in regulation of thymocyte homeostasis (By similarity). Sequence-specific DNA-binding factor that binds to the 5'-AGGTCTC-3' sequence within the negative cis-acting element intronic regulatory region (IRR) of the GATA3 gene. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11318609}. Note=Colocalizes with coilin in subnuclear cajal and histone locus bodies. Translocates in the LEC complex to cajal and histone locus bodies at snRNA genes in a ICE1-dependent manner. Associates to transcriptionally active chromatin at snRNA genes (By similarity). {ECO:0000250}. SUBUNIT: Component of the little elongation complex (LEC), at least composed of ELL (ELL, ELL2 or ELL3), ZC3H8, ICE1 and ICE2. Interacts with ICE1 (via C-terminus domain) (By similarity). {ECO:0000250}. DOMAIN: The N-terminal region and all three C3H1-type zinc fingers are necessary to induce transcriptional repression. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in heart, muscle, testis, kidney, brain, liver, lung and spleen. {ECO:0000269|PubMed:11318609}. +Q91X45 ZBTB3_MOUSE Zinc finger and BTB domain-containing protein 3 518 55,901 Chain (1); Compositional bias (1); Cross-link (3); Domain (1); Erroneous initiation (1); Modified residue (2); Sequence conflict (1); Zinc finger (2) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q8BKW4 ZCHC4_MOUSE Zinc finger CCHC domain-containing protein 4 512 58,567 Alternative sequence (1); Chain (1); Domain (1); Zinc finger (1) FUNCTION: May be a methyltransferase. {ECO:0000250}. +A2AKY4 Z804A_MOUSE Zinc finger protein 804A 1200 134,850 Chain (1); Zinc finger (1) +P10755 ZFP14_MOUSE Zinc finger protein 14 (Zfp-14) (Zinc finger protein Krox-9) 501 59,060 Chain (1); Domain (1); Erroneous initiation (1); Sequence conflict (1); Zinc finger (13) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q9QY24 ZBP1_MOUSE Z-DNA-binding protein 1 (DNA-dependent activator of IFN-regulatory factors) (DAI) (Tumor stroma and activated macrophage protein DLM-1) 411 44,331 Alternative sequence (2); Beta strand (2); Chain (1); Helix (3); Motif (2); Repeat (2); Sequence conflict (5) FUNCTION: Participates in the detection by the host's innate immune system of DNA from viral, bacterial or even host origin. Plays a role in host defense against tumors and pathogens. Acts as a cytoplasmic DNA sensor which, when activated, induces the recruitment of TBK1 and IRF3 to its C-terminal region and activates the downstream interferon regulatory factor (IRF) and NF-kappa B transcription factors, leading to type-I interferon production. ZBP1-induced NF-kappaB activation probably involves the recruitment of the RHIM containing kinases RIPK1 and RIPK3. {ECO:0000269|PubMed:17618271, ECO:0000269|PubMed:19590578}. SUBUNIT: Interacts (via RIP homotypic interaction motif) with murid herpesvirus 1 viral inhibitor of RIP activation (via RIP homotypic interaction motif); this interaction inhibits recruitment of RIPK1 and RIPK3 to ZBP1 and prevents ZBP1-induced NFkappa-B activation. {ECO:0000269|PubMed:19590578}. TISSUE SPECIFICITY: Expressed in lung, spleen and liver. Lower levels were seen in heart, kidney and testis. Expression is greatly up-regulated in tumor stromal cells and activated macrophages. +O88878 ZFAN5_MOUSE AN1-type zinc finger protein 5 (Zinc finger A20 domain-containing protein 2) (Zinc finger protein 216) 213 23,058 Beta strand (2); Chain (1); Helix (2); Modified residue (3); Turn (1); Zinc finger (2) FUNCTION: Involved in protein degradation via the ubiquitin-proteasome system. May act by anchoring ubiquitinated proteins to the proteasome. Plays a role in ubiquitin-mediated protein degradation during muscle atrophy. Plays a role in the regulation of NF-kappa-B activation and apoptosis. Inhibits NF-kappa-B activation triggered by overexpression of RIPK1 and TRAF6 but not of RELA. Inhibits also tumor necrosis factor (TNF), IL-1 and TLR4-induced NF-kappa-B activation in a dose-dependent manner. Overexpression sensitizes cells to TNF-induced apoptosis. Is a potent inhibitory factor for osteoclast differentiation. {ECO:0000269|PubMed:16194934, ECO:0000269|PubMed:16424905}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homooligomer and/or heterooligomer. Interacts (via A20-type domain) with IKBKG and RIPK1 and with TRAF6 (via AN1-type domain) (By similarity). Interacts with ubiquitin and polyubiquitinated proteins. Identified in a heterotrimeric complex with ubiquitin and SQSTM1, where ZFAND5 and SQSTM1 both interact with the same ubiquitin molecule (By similarity). {ECO:0000250}. DOMAIN: The A20-type zinc finger directly binds polyubiquitin chains and associates with the 26S proteasome. The zinc-finger A20-type domain is essential for inhibition of NF-kappa-B activation. {ECO:0000269|PubMed:16424905}. TISSUE SPECIFICITY: Expressed in brain, muscle, eye, and heart, lower expression in lung, kidney, and spleen, and very low expression in liver. Expressed in myoblast C2C12 cells (at protein level). {ECO:0000269|PubMed:14754897, ECO:0000269|PubMed:9758550}. +O88532 ZFR_MOUSE Zinc finger RNA-binding protein 1074 116,859 Chain (1); Compositional bias (1); Cross-link (3); Domain (1); Erroneous initiation (5); Modified residue (3); Sequence caution (2); Sequence conflict (5) FUNCTION: Involved in postimplantation and gastrulation stages of development. Binds to DNA and RNA. Involved in the nucleocytoplasmic shuttling of STAU2 (By similarity). {ECO:0000250, ECO:0000269|PubMed:16277607}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasmic granule {ECO:0000250}. Chromosome {ECO:0000250}. Note=Associated with chromosome foci in meiotic cells. Localizes in somatodendritic compartment of primary hippocampal neurons (By similarity). Colocalizes with STAU2 in several cytosolic RNA granules (By similarity). Associated with chromosomes. {ECO:0000250}. SUBUNIT: Found in a cytoplasmic mRNP complex with STAU2. Does not interact with STAU1 (By similarity). Interacts with STAU2. {ECO:0000250, ECO:0000269|PubMed:16277607}. TISSUE SPECIFICITY: Expressed in Sertoli cells, spermatocytes, primary and growing oocytes and granulosa cells (at protein level). Expressed in testis, ovary and brain. {ECO:0000269|PubMed:10072773, ECO:0000269|PubMed:11283266}. +Q91WU6 ZDHC7_MOUSE Palmitoyltransferase ZDHHC7 (EC 2.3.1.225) (GABA-A receptor-associated membrane protein 2) (Zinc finger DHHC domain-containing protein 7) (DHHC-7) 308 35,213 Chain (1); Domain (1); Mutagenesis (1); Sequence conflict (1); Transmembrane (4) TRANSMEM 51 71 Helical. {ECO:0000255}.; TRANSMEM 76 96 Helical. {ECO:0000255}.; TRANSMEM 174 194 Helical. {ECO:0000255}.; TRANSMEM 218 238 Helical. {ECO:0000255}. FUNCTION: Palmitoyltransferase with broad specificity (PubMed:15603741, PubMed:25253725). Palmitoylates JAM3 (By similarity). Palmitoylates SNAP25 and DLG4/PSD95 (PubMed:15603741, PubMed:25253725). Palmitoylates sex steroid hormone receptors, including ESR1, PGR and AR, thereby regulating their targeting to the plasma membrane and their function in rapid intracellular signaling upon binding of sex hormones (By similarity). May play a role in follicle stimulation hormone (FSH) activation of testicular Sertoli cells (By similarity). {ECO:0000250|UniProtKB:Q923G5, ECO:0000250|UniProtKB:Q9NXF8, ECO:0000269|PubMed:15603741, ECO:0000269|PubMed:25253725}. PTM: Autopalmitoylated. {ECO:0000269|PubMed:25253725}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9NXF8}; Multi-pass membrane protein {ECO:0000255}. DOMAIN: The DHHC domain is required for palmitoyltransferase activity. {ECO:0000250|UniProtKB:Q8IUH5}. TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in liver, kidney and brain. Expressed in all brain regions. {ECO:0000269|PubMed:15603741}. +Q8BQQ1 ZDH14_MOUSE Probable palmitoyltransferase ZDHHC14 (EC 2.3.1.225) (NEW1 domain-containing protein) (NEW1CP) (Zinc finger DHHC domain-containing protein 14) (DHHC-14) 489 53,659 Active site (1); Alternative sequence (1); Chain (1); Domain (1); Frameshift (1); Modified residue (1); Sequence conflict (1); Transmembrane (4) TRANSMEM 61 81 Helical. {ECO:0000255}.; TRANSMEM 90 110 Helical. {ECO:0000255}.; TRANSMEM 209 229 Helical. {ECO:0000255}.; TRANSMEM 256 276 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. DOMAIN: The DHHC domain is required for palmitoyltransferase activity. {ECO:0000250}. +Q8VCM3 ZFY21_MOUSE Zinc finger FYVE domain-containing protein 21 234 26,047 Chain (1); Erroneous initiation (4); Region (1); Sequence conflict (1); Zinc finger (1) FUNCTION: Plays a role in cell adhesion, and thereby in cell motility which requires repeated formation and disassembly of focal adhesions. Regulates microtubule-induced PTK2/FAK1 dephosphorylation, an event important for focal adhesion disassembly, as well as integrin beta-1/ITGB1 cell surface expression (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, focal adhesion. Cytoplasmic vesicle {ECO:0000250}. Endosome {ECO:0000250}. SUBUNIT: Interacts with PTK2/FAK1. {ECO:0000250}. DOMAIN: The FYVE-type zinc finger mediates interaction with PTK2/FAK1, and also interaction with PI(3)P and association with endosomes. {ECO:0000250}.; DOMAIN: The C-terminal region exhibits a structure similar to canonical PH domains, but lacks a positively charged interface to bind phosphatidylinositol phosphate. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:20439989}. +Q3TIV5 ZC3HF_MOUSE Zinc finger CCCH domain-containing protein 15 (DRG family-regulatory protein 1) (Epo-immediate response gene protein FM22) 426 48,327 Alternative sequence (3); Chain (1); Coiled coil (2); Compositional bias (1); Frameshift (1); Modified residue (3); Region (1); Sequence conflict (3); Zinc finger (2) FUNCTION: Protects DRG1 from proteolytic degradation (PubMed:15676025). Stimulates DRG1 GTPase activity likely by increasing the affinity for the potassium ions (By similarity). {ECO:0000250|UniProtKB:Q8WU90, ECO:0000269|PubMed:15676025}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250|UniProtKB:Q8WU90}. Note=The DRG1-DFRP2/ZC3H15 complex associates with polysomes. {ECO:0000250|UniProtKB:Q8WU90}. SUBUNIT: Interacts with DRG1; the interaction forms a polysomal DRG1-DFRP1/ZC3H15 complex which provides protein stability to DRG1 possibly by blocking poly-ubiquitination (PubMed:15676025). Associates with microtubules (By similarity). {ECO:0000250|UniProtKB:Q8WU90, ECO:0000269|PubMed:15676025}. +Q80YP6 ZIK1_MOUSE Zinc finger protein interacting with ribonucleoprotein K 463 52,727 Chain (1); Domain (1); Sequence conflict (1); Zinc finger (9) FUNCTION: May be a transcriptional repressor. {ECO:0000269|PubMed:8910362}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Interacts with HNRPK. {ECO:0000269|PubMed:8910362}. TISSUE SPECIFICITY: Expressed in ovary and liver, and at lower levels in brain and muscle. {ECO:0000269|PubMed:8910362}. +Q68FG0 ZC4H2_MOUSE Zinc finger C4H2 domain-containing protein (Hepatocellular carcinoma-associated antigen 127 homolog) 224 26,244 Alternative sequence (1); Chain (1); Coiled coil (1); Compositional bias (2); Erroneous initiation (1); Sequence conflict (2); Zinc finger (1) FUNCTION: Plays a role in interneurons differentiation. Involved in neuronal development and in neuromuscular junction formation. {ECO:0000250|UniProtKB:Q9NQZ6}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NQZ6}. Nucleus {ECO:0000250|UniProtKB:Q9NQZ6}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000250|UniProtKB:Q9NQZ6}. TISSUE SPECIFICITY: Expressed in embryonic and adult brain and spinal cord. {ECO:0000269|PubMed:23623388}. +Q9CR11 YETS4_MOUSE YEATS domain-containing protein 4 227 26,530 Chain (1); Coiled coil (1); Cross-link (1); Domain (1); Region (2) FUNCTION: Component of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00376}. SUBUNIT: Component of numerous complexes with chromatin remodeling and histone acetyltransferase activity. Component of the NuA4 histone acetyltransferase complex which contains the catalytic subunit KAT5/TIP60 and the subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6. The NuA4 complex interacts with MYC. Component of a NuA4-related complex which contains EP400, TRRAP/PAF400, SRCAP, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, actin, ACTL6A/BAF53A, VPS72 and YEATS4/GAS41. YEATS4 interacts with MLLT10/AF10. YEATS4 may also interact with the SWI/SNF component SMARCB1/BAF47, TACC1 and TACC2, and the nuclear matrix protein NUMA1 (By similarity). {ECO:0000250}. +Q9JIM5 YIPF7_MOUSE Protein YIPF7 (YIP1 family member 7) 254 27,490 Chain (1); Topological domain (5); Transmembrane (5) TRANSMEM 124 144 Helical. {ECO:0000255}.; TRANSMEM 146 166 Helical. {ECO:0000255}.; TRANSMEM 180 200 Helical. {ECO:0000255}.; TRANSMEM 210 230 Helical. {ECO:0000255}.; TRANSMEM 234 254 Helical. {ECO:0000255}. TOPO_DOM 1 123 Cytoplasmic. {ECO:0000250|UniProtKB:Q8N8F6}.; TOPO_DOM 145 145 Lumenal. {ECO:0000305}.; TOPO_DOM 167 179 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 201 209 Lumenal. {ECO:0000305}.; TOPO_DOM 231 233 Cytoplasmic. {ECO:0000305}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11489904}; Multi-pass membrane protein {ECO:0000269|PubMed:11489904}. Golgi apparatus, cis-Golgi network membrane {ECO:0000250|UniProtKB:Q8N8F6}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q8N8F6}. TISSUE SPECIFICITY: Specifically expressed in the heart. {ECO:0000269|PubMed:11489904}. +Q99LP8 YIPF2_MOUSE Protein YIPF2 (YIP1 family member 2) 312 34,900 Chain (1); Initiator methionine (1); Modified residue (1); Sequence conflict (1); Topological domain (6); Transmembrane (5) TRANSMEM 122 142 Helical. {ECO:0000255}.; TRANSMEM 161 181 Helical. {ECO:0000255}.; TRANSMEM 194 216 Helical. {ECO:0000255}.; TRANSMEM 229 249 Helical. {ECO:0000255}.; TRANSMEM 254 274 Helical. {ECO:0000255}. TOPO_DOM 2 121 Cytoplasmic. {ECO:0000250|UniProtKB:Q9BWQ6}.; TOPO_DOM 143 160 Lumenal. {ECO:0000305}.; TOPO_DOM 182 193 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 217 228 Lumenal. {ECO:0000305}.; TOPO_DOM 250 253 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 275 312 Lumenal. {ECO:0000250|UniProtKB:Q9BWQ6}. SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane {ECO:0000250|UniProtKB:Q9BWQ6}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9BWQ6}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q9BWQ6}. Late endosome membrane {ECO:0000250|UniProtKB:Q9BWQ6}. Note=Mainly localizes within medial-/trans-Golgi and trans-Golgi network (TGN), while less so within cis-Golgi. {ECO:0000250|UniProtKB:Q9BWQ6}. SUBUNIT: Interacts with YIPF6; this interaction may stabilize YIPF2. May also form a ternary complex with YIPF1 and YIPF6. {ECO:0000250|UniProtKB:Q9BWQ6}. +P61237 YPEL3_MOUSE Protein yippee-like 3 (Small ubiquitinated apoptotic protein) 119 13,608 Chain (1); Domain (1); Erroneous initiation (1); Metal binding (4); Sequence conflict (2) FUNCTION: Involved in proliferation and apoptosis in myeloid precursor cells. {ECO:0000269|PubMed:12566317}. PTM: Probably ubiquitinated leading to its degradation by the proteasome. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. Strongly expressed in heart, brain, testis, lung, spleen, liver, kidney and myeloid cells. {ECO:0000269|PubMed:12566317, ECO:0000269|PubMed:15556292}. +P59326 YTHD1_MOUSE YTH domain-containing family protein 1 (Dermatomyositis associated with cancer putative autoantigen 1 homolog) (DACA-1 homolog) 559 60,879 Binding site (4); Chain (1); Compositional bias (1); Domain (1); Initiator methionine (1); Modified residue (2); Region (2) FUNCTION: Specifically recognizes and binds N6-methyladenosine (m6A)-containing mRNAs, and promotes mRNA translation efficiency. M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in the efficiency of mRNA splicing, processing and stability. Acts as a regulator of mRNA translation efficiency: promotes ribosome loading to m6A-containing mRNAs and interacts with translation initiation factors eIF3 (EIF3A or EIF3B) to facilitate translation initiation. {ECO:0000250|UniProtKB:Q9BYJ9}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BYJ9}. SUBUNIT: Interacts with ribosomes. Interacts with eIF3 (EIF3A or EIF3B). Interacts with YTHDF3. {ECO:0000250|UniProtKB:Q9BYJ9}. +Q5ISE2 Z36L3_MOUSE mRNA decay activator protein ZFP36L3 (Zinc finger protein 36, C3H1 type-like 3) (zinc finger protein 36-like 3) 725 72,346 Chain (1); Compositional bias (2); Mutagenesis (2); Region (1); Transmembrane (4); Zinc finger (2) TRANSMEM 380 400 Helical. {ECO:0000255}.; TRANSMEM 420 440 Helical. {ECO:0000255}.; TRANSMEM 441 461 Helical. {ECO:0000255}.; TRANSMEM 468 488 Helical. {ECO:0000255}. FUNCTION: Placenta-specific zinc-finger RNA-binding protein that destabilizes cytoplasmic AU-rich element (ARE)-containing mRNA transcripts by promoting their poly(A) tail removal or deadenylation, and hence provide a mechanism for attenuating protein synthesis (PubMed:15814898, PubMed:26952984). Binds to the 3'-UTR ARE of placental target mRNAs, such as TNF, HBEGF and LIPG (PubMed:15814898, PubMed:18367448, PubMed:26952984). Involved in placental expression of many genes important for normal placental physiology (PubMed:26952984). {ECO:0000269|PubMed:15814898, ECO:0000269|PubMed:18367448, ECO:0000269|PubMed:26952984}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15814898, ECO:0000269|PubMed:18367448, ECO:0000269|PubMed:26493225}. Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=Localizes exlusively in the cytoplasm (PubMed:18367448, PubMed:15814898). Not detected in the nucleus despite the presence of a nuclear localization signal (NLS) in the zinc finger regions; a C-terminal alanine-rich repeat domain is able to override the activity of the nuclear localization signal and prevent import into the nucleus (PubMed:18367448, PubMed:26493225). {ECO:0000269|PubMed:15814898, ECO:0000269|PubMed:18367448, ECO:0000269|PubMed:26493225}. DOMAIN: Contains long series of C-terminal alanine-rich repeats that serve to maintain the protein in the cytoplasm. {ECO:0000269|PubMed:18367448}. TISSUE SPECIFICITY: Expressed in placenta and extraembryonic tissues (at protein level). Not detected in embryos and fetus (PubMed:15814898, PubMed:26952984). {ECO:0000269|PubMed:15814898, ECO:0000269|PubMed:26952984}. +Q8VD12 Z385A_MOUSE Zinc finger protein 385A (Hematopoietic zinc finger protein) 386 40,447 Alternative sequence (1); Chain (1); Frameshift (1); Modified residue (2); Region (1); Sequence conflict (6); Zinc finger (3) FUNCTION: RNA-binding protein that affects the localization and the translation of a subset of mRNA. May play a role in adipogenesis through binding to the 3'-UTR of CEBPA mRNA and regulation of its translation. Targets ITPR1 mRNA to dendrites in Purkinje cells, and may regulate its activity-dependent translation. With ELAVL1, binds the 3'-UTR of p53/TP53 mRNAs to control their nuclear export induced by CDKN2A. Hence, may regulate p53/TP53 expression and mediate in part the CDKN2A anti-proliferative activity. May also bind CCNB1 mRNA. Alternatively, may also regulate p53/TP53 activity through direct protein-protein interaction. Interacts with p53/TP53 and promotes cell-cycle arrest over apoptosis enhancing preferentially the DNA binding and transactivation of p53/TP53 on cell-cycle arrest target genes over proapoptotic target genes. May also regulate the ubiquitination and stability of CDKN1A promoting DNA damage-induced cell cycle arrest. Also plays a role in megakaryocytes differentiation. {ECO:0000269|PubMed:11927637, ECO:0000269|PubMed:16286649, ECO:0000269|PubMed:16382142, ECO:0000269|PubMed:17719541, ECO:0000269|PubMed:18418387, ECO:0000269|PubMed:21402775}. PTM: Ubiquitinated upon prolonged exposure to genotoxic stress, which leads to proteasomal degradation of ZNF385A and releases p53/TP53 from cell-cycle arrest target gene promoters. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16286649}. Nucleus, nucleolus {ECO:0000250}. Cell projection, dendrite {ECO:0000269|PubMed:16286649}. Note=Detected in dendrites of Purkinje cells and hippocampal neurons. SUBUNIT: Interacts with p53/TP53; the interaction is direct and enhances p53/TP53 transactivation functions on cell-cycle arrest target genes, resulting in growth arrest. Interacts with ELAVL1; the interaction is indirect, mRNA-dependent and may regulate p53/TP53 expression. {ECO:0000269|PubMed:17719541, ECO:0000269|PubMed:21402775}. TISSUE SPECIFICITY: Expressed in brain and testis (at protein level). In brain, the expression is located to olfactory bulb, cerebral cortex, hippocampus, satellite cells and Purkinje cells of the cerebellum molecular layer. Detected in bone marrow, white and brown adipose tissue, lung and at lower levels in the thymus. {ECO:0000269|PubMed:10585558, ECO:0000269|PubMed:11927637, ECO:0000269|PubMed:16286649, ECO:0000269|PubMed:18418387}. +Q5F293 ZBTB4_MOUSE Zinc finger and BTB domain-containing protein 4 982 102,663 Chain (1); Compositional bias (4); Cross-link (3); Domain (1); Erroneous initiation (1); Modified residue (4); Region (1); Sequence conflict (1); Zinc finger (6) FUNCTION: Transcriptional repressor with bimodal DNA-binding specificity. Represses transcription in a methyl-CpG-dependent manner. Binds with a higher affinity to methylated CpG dinucleotides in the consensus sequence 5'-CGCG-3' but can also bind to the non-methylated consensus sequence 5'-CTGCNA-3' also known as the consensus kaiso binding site (KBS). Can also bind specifically to a single methyl-CpG pair and can bind hemimethylated DNA but with a lower affinity compared to methylated DNA. Plays a role in postnatal myogenesis, may be involved in the regulation of satellite cells self-renewal (PubMed:27446912). {ECO:0000250|UniProtKB:Q9P1Z0, ECO:0000269|PubMed:27446912}. PTM: Phosphorylated by HIPK2. This phosphorylation reduces stability and triggers ZBTB4 protein degradation in response to DNA damage. {ECO:0000250|UniProtKB:Q9P1Z0}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9P1Z0}. Chromosome {ECO:0000250|UniProtKB:Q9P1Z0}. Note=Localizes to chromocenters. {ECO:0000250|UniProtKB:Q9P1Z0}. SUBUNIT: Interacts with HIPK2. Interacts with CBFA2T3. Interacts with ZBTB38. {ECO:0000250|UniProtKB:Q9P1Z0}. TISSUE SPECIFICITY: Expressed in adult and aged myogenic satellite cells. {ECO:0000269|PubMed:27446912}. +P08042 ZFP1_MOUSE Zinc finger protein 1 (Zfp-1) (Protein mKR1) 402 46,511 Alternative sequence (1); Chain (1); Cross-link (3); Domain (1); Frameshift (2); Region (2); Sequence conflict (2); Zinc finger (8) FUNCTION: May be involved in transcriptional regulation. {ECO:0000305}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20624068}. Note=Shows widespread expression throughout the nucleus, but appears to be excluded from nucleoli. {ECO:0000269|PubMed:20624068}. +Q8C0Q2 ZHX3_MOUSE Zinc fingers and homeoboxes protein 3 (Triple homeobox protein 1) (Zinc finger and homeodomain protein 3) 951 104,343 Chain (1); DNA binding (5); Modified residue (5); Region (4); Sequence conflict (1); Zinc finger (2) FUNCTION: Acts as a transcriptional repressor. Involved in the early stages of mesenchymal stem cell (MSC) osteogenic differentiation. Is a regulator of podocyte gene expression during primary glomerula disease. Binds to promoter DNA. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H4I2, ECO:0000255|PROSITE-ProRule:PRU00108}. SUBUNIT: Homodimer (via homeobox domain 1). Heterodimer with ZHX1 (via homeobox domain 1). Heterodimer with ZHX2 (via homeobox domain 1). Heterodimerization with ZHX1 is a prerequisite for repressor activity. Interacts with NFYA. {ECO:0000250|UniProtKB:Q9H4I2}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:14659886}. +P43404 ZAP70_MOUSE Tyrosine-protein kinase ZAP-70 (EC 2.7.10.2) (70 kDa zeta-chain associated protein) (Syk-related tyrosine kinase) 618 70,112 Active site (1); Alternative sequence (3); Binding site (1); Chain (1); Cross-link (1); Domain (3); Modified residue (7); Natural variant (1); Nucleotide binding (1); Region (2); Sequence conflict (5) FUNCTION: Tyrosine kinase that plays an essential role in regulation of the adaptive immune response. Regulates motility, adhesion and cytokine expression of mature T-cells, as well as thymocyte development. Contributes also to the development and activation of primary B-lymphocytes. When antigen presenting cells (APC) activate T-cell receptor (TCR), a serie of phosphorylations lead to the recruitment of ZAP70 to the doubly phosphorylated TCR component CD3Z through ITAM motif at the plasma membrane. This recruitment serves to localization to the stimulated TCR and to relieve its autoinhibited conformation. Release of ZAP70 active conformation is further stabilized by phosphorylation mediated by LCK. Subsequently, ZAP70 phosphorylates at least 2 essential adapter proteins: LAT and LCP2. In turn, a large number of signaling molecules are recruited and ultimately lead to lymphokine production, T-cell proliferation and differentiation. Furthermore, ZAP70 controls cytoskeleton modifications, adhesion and mobility of T-lymphocytes, thus ensuring correct delivery of effectors to the APC. ZAP70 is also required for TCR-CD3Z internalization and degradation through interaction with the E3 ubiquitin-protein ligase CBL and adapter proteins SLA and SLA2. Thus, ZAP70 regulates both T-cell activation switch on and switch off by modulating TCR expression at the T-cell surface. During thymocyte development, ZAP70 promotes survival and cell-cycle progression of developing thymocytes before positive selection (when cells are still CD4/CD8 double negative). Additionally, ZAP70-dependent signaling pathway may also contribute to primary B-cells formation and activation through B-cell receptor (BCR). {ECO:0000269|PubMed:12705855, ECO:0000269|PubMed:14985102, ECO:0000269|PubMed:17606633, ECO:0000269|PubMed:26903241, ECO:0000269|PubMed:7630421}. PTM: Phosphorylated on tyrosine residues upon T-cell antigen receptor (TCR) stimulation. Phosphorylation of Tyr-314 and Tyr-314 are essential for ZAP70 positive function on T-lymphocyte activation whereas Tyr-290 has a negative regulatory role. Within the C-terminal kinase domain, Tyr-491 and Tyr-492 are phosphorylated after TCR induction, Tyr-491 playing a negative regulatory role and Tyr-492 a positive. Tyr-492 is dephosphorylated by PTN22.; PTM: Ubiquitinated in response to T cell activation. Deubiquitinated by OTUD7B. {ECO:0000269|PubMed:26903241}. SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral membrane protein. Note=In quiescent T-lymphocytes, ZAP70 is cytoplasmic. Upon TCR activation, it is recruited at the plasma membrane by interacting with CD3Z. Colocalizes together with RHOH in the immunological synapse. RHOH is required for its proper localization to the cell membrane and cytoskeleton fractions in the thymocytes. SUBUNIT: Interacts with CD247/CD3Z; this interaction docks ZAP70 at the stimulated TCR (By similarity). Interacts with NFAM1 (PubMed:15143214). Interacts with adapter protein SLA; this interaction negatively regulates T-cell receptor signaling (PubMed:10662792). Interacts with VAV1 (By similarity). Interacts with CBL; this interaction promotes ubiquitination, internalization and subsequent degradation of CD247/CD3Z (By similarity). Identified in a complex with CBL and UBE2L3 (By similarity). Interacts with SHB (By similarity). Interacts with adapter protein SLA2; this interaction negatively regulates T-cell receptor signaling (PubMed:11891219). Interacts with CBLB (PubMed:10646608). Interacts (via SH2 domains) with RHOH; this interaction regulates ZAP70 subcellular localization (PubMed:17028588). Interacts with DEF6 (PubMed:12648457). Interacts (ubiquitinated form) with OTUD7B and UBASH3B (PubMed:26903241). {ECO:0000250|UniProtKB:P43403, ECO:0000269|PubMed:10646608, ECO:0000269|PubMed:10662792, ECO:0000269|PubMed:11891219, ECO:0000269|PubMed:12648457, ECO:0000269|PubMed:15143214, ECO:0000269|PubMed:17028588, ECO:0000269|PubMed:26903241}. DOMAIN: Composed of 2 N-terminal SH2 domains and a C-terminal kinase domain. The tandem SH2 domains bind to the doubly phosphorylated tyrosine-based activation motif (ITAM) of CD247/CD3Z and the non-canonical phosphorylated tyrosine-based activation motif (TAM) of RHOH (By similarity). The interdomain B located between the second SH2 and the kinase domain has been implicated in binding to other signaling molecules including CBL or VAV1. Thus, ZAP70 can also function as a scaffold by recruiting additional factors to the stimulated TCR complex (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in thymus, spleen and lymph nodes. {ECO:0000269|PubMed:14985102}. +Q0VGT4 ZGRF1_MOUSE Protein ZGRF1 (GRF-type zinc finger domain-containing protein 1) 1863 205,737 Alternative sequence (2); Chain (1); Modified residue (2); Transmembrane (1) TRANSMEM 1705 1725 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q9D6H5 ZDHC4_MOUSE Probable palmitoyltransferase ZDHHC4 (EC 2.3.1.225) (Zinc finger DHHC domain-containing protein 4) (DHHC-4) 343 39,528 Active site (1); Chain (1); Domain (1); Motif (1); Transmembrane (5) TRANSMEM 3 23 Helical. {ECO:0000255}.; TRANSMEM 68 88 Helical. {ECO:0000255}.; TRANSMEM 101 121 Helical. {ECO:0000255}.; TRANSMEM 194 214 Helical. {ECO:0000255}.; TRANSMEM 256 276 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9NPG8}; Multi-pass membrane protein {ECO:0000255}. DOMAIN: The C-terminal di-lysine motif confers endoplasmic reticulum localization. {ECO:0000250|UniProtKB:Q9NPG8}.; DOMAIN: The DHHC domain is required for palmitoyltransferase activity. {ECO:0000250|UniProtKB:Q8IUH5}. +Q14AK4 ZDH11_MOUSE Probable palmitoyltransferase ZDHHC11 (EC 2.3.1.225) (DHHC-containing protein 10) (Zinc finger DHHC domain-containing protein 11) (DHHC-11) 347 39,660 Chain (1); Domain (1); Transmembrane (5) TRANSMEM 47 67 Helical. {ECO:0000255}.; TRANSMEM 76 96 Helical. {ECO:0000255}.; TRANSMEM 171 191 Helical. {ECO:0000255}.; TRANSMEM 214 234 Helical. {ECO:0000255}.; TRANSMEM 235 255 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. DOMAIN: The DHHC domain is required for palmitoyltransferase activity. {ECO:0000250}. +P23607 ZFA_MOUSE Zinc finger autosomal protein 742 84,658 Chain (1); Zinc finger (13) FUNCTION: Probable transcriptional activator. ZFA is an expressed retroposon derived from an alternative transcript of the ZFX gene. SUBCELLULAR LOCATION: Nucleus. +Q9D270 ZDH21_MOUSE Probable palmitoyltransferase ZDHHC21 (EC 2.3.1.225) (GABA-A receptor-associated membrane protein 3) (Zinc finger DHHC domain-containing protein 21) (DHHC-21) 265 31,331 Chain (1); Domain (1); Sequence conflict (2); Transmembrane (4) TRANSMEM 17 37 Helical. {ECO:0000255}.; TRANSMEM 45 65 Helical. {ECO:0000255}.; TRANSMEM 134 154 Helical. {ECO:0000255}.; TRANSMEM 186 206 Helical. {ECO:0000255}. FUNCTION: Palmitoylates sex steroid hormone receptors, including ESR1, PGR and AR, thereby regulating their targeting to the plasma membrane. This affects rapid intracellular signaling by sex hormones via ERK and AKT kinases and the generation of cAMP, but does not affect that mediated by their nuclear receptor (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Golgi apparatus {ECO:0000250}. DOMAIN: The DHHC domain is required for palmitoyltransferase activity. {ECO:0000250}. +P10925 ZFY1_MOUSE Zinc finger Y-chromosomal protein 1 782 88,230 Chain (1); Motif (1); Sequence conflict (7); Zinc finger (13) FUNCTION: Probable transcriptional activator. Binds to the consensus sequence 5'-AGGCCY-3' (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. DOMAIN: The binding of ZFY to DNA is mediated by the interaction of the GGCC core base pairs with zinc fingers 12 and 13. {ECO:0000250}. +Q91X58 ZFN2B_MOUSE AN1-type zinc finger protein 2B (Arsenite-inducible RNA-associated protein-like protein) (AIRAP-like protein) 257 27,895 Chain (1); Compositional bias (1); Domain (2); Helix (2); Lipidation (1); Modified residue (4); Motif (1); Mutagenesis (23); Propeptide (1); Region (1); Sequence conflict (1); Turn (1); Zinc finger (2) FUNCTION: Plays a role in protein homeostasis by regulating both the translocation and the ubiquitin-mediated proteasomal degradation of nascent proteins at the endoplasmic reticulum (PubMed:24160817, PubMed:26337389, PubMed:26692333). It is involved in the regulation of signal-mediated translocation of proteins into the endoplasmic reticulum (PubMed:24160817). It also plays a role in the ubiquitin-mediated proteasomal degradation of proteins for which signal-mediated translocation to the endoplasmic reticulum has failed (PubMed:18467495, PubMed:26337389). May therefore function in the endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for proteasomal degradation (PubMed:24160817, PubMed:26337389). By controlling the steady-state expression of the IGF1R receptor, indirectly regulates the insulin-like growth factor receptor signaling pathway (PubMed:26692333). {ECO:0000269|PubMed:18467495, ECO:0000269|PubMed:24160817, ECO:0000269|PubMed:26337389, ECO:0000269|PubMed:26692333}. PTM: Phosphorylated by MAPK14 (Probable). Phosphorylation has no effect on association with the proteasome complex (Probable). {ECO:0000305|PubMed:18467495}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18467495}; Lipid-anchor {ECO:0000305|PubMed:18467495}. SUBUNIT: Binds 'Lys-48'-linked polyubiquitin chains of ubiquitinated proteins (PubMed:18467495, PubMed:24160817, PubMed:26876100). Associates with the proteasome complex; upon exposure to arsenite (PubMed:18467495, PubMed:26876100). Interacts (via VIM motif) with VCP; the interaction is direct (PubMed:24160817, PubMed:26337389). Interacts with BAG6 (PubMed:24160817, PubMed:26337389, PubMed:26876100). Interacts with IGF1R (nascent precursor form) (PubMed:26692333). Interacts with DERL1, FAF2, NPLOC4 and UFD1; probably through VCP (PubMed:24160817). {ECO:0000269|PubMed:18467495, ECO:0000269|PubMed:24160817, ECO:0000269|PubMed:26337389, ECO:0000269|PubMed:26692333, ECO:0000269|PubMed:26876100}. DOMAIN: The UIM domains specifically bind 'Lys-48'-linked ubiquitin polymers (PubMed:18467495, PubMed:26876100). The UIM domains mediate interaction with polyubiquitinated proteins (PubMed:18467495, PubMed:26337389). {ECO:0000269|PubMed:18467495, ECO:0000269|PubMed:26337389, ECO:0000269|PubMed:26876100}. +P10751 ZFP11_MOUSE Zinc finger protein 11 (Zfp-11) (Zinc finger protein Krox-6.1A/6.1B+/6.1B-) 647 75,605 Chain (1); Erroneous initiation (1); Frameshift (1); Sequence conflict (3); Zinc finger (21) SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +P10754 ZFP13_MOUSE Zinc finger protein 13 (Zfp-13) (Zinc finger protein Krox-8) 512 56,054 Alternative sequence (1); Chain (1); Domain (1); Sequence conflict (1); Zinc finger (8) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q9CQG3 ZMY19_MOUSE Zinc finger MYND domain-containing protein 19 (Melanin-concentrating hormone receptor 1-interacting zinc finger protein) (MCH-R1-interacting zinc finger protein) 227 26,433 Alternative sequence (1); Chain (1); Compositional bias (1); Zinc finger (1) FUNCTION: May be involved as a regulatory molecule in GPR24/MCH-R1 signaling. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. SUBUNIT: Interacts with GPR24/MCH-R1. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain. {ECO:0000269|PubMed:12208518}. +Q0P678 ZCH18_MOUSE Zinc finger CCCH domain-containing protein 18 (Nuclear protein NHN1) 948 105,694 Alternative sequence (2); Chain (1); Coiled coil (2); Compositional bias (3); Cross-link (5); Erroneous initiation (1); Modified residue (25); Zinc finger (1) SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with ZFC3H1 in a RNase-insensitive manner. {ECO:0000250|UniProtKB:Q86VM9}. +Q8JZL0 ZN467_MOUSE Zinc finger protein 467 (Endothelial cell-derived zinc finger protein) (EZI) 594 65,633 Chain (1); Cross-link (2); Frameshift (1); Region (1); Sequence conflict (1); Zinc finger (12) FUNCTION: Transcription factor that promotes adipocyte differentiation and suppresses osteoblast differentiation in the bone marrow. Enhances the osteoclast-supporting ability of stromal cells. Binds with STAT3 the consensus sequence 5'-CTTCTGGGAAGA-3' of the acute phase response element (APRE). Transactivates several promoters including FOS, OSM and PPARG. Recruits a histone deacetylase complex. {ECO:0000269|PubMed:12426389, ECO:0000269|PubMed:21123171}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12426389}. SUBUNIT: Interacts with STAT3. Enhances STAT3 activity by keeping it in the nucleus. {ECO:0000269|PubMed:12426389}. +Q99LI5 ZN281_MOUSE Zinc finger protein 281 893 96,685 Chain (1); Compositional bias (3); Cross-link (29); Modified residue (6); Sequence conflict (5); Zinc finger (4) FUNCTION: Transcription repressor that plays a role in regulation of embryonic stem cells (ESCs) differentiation. Required for ESCs differentiation and acts by mediating autorepression of NANOG in ESCs: binds to the NANOG promoter and promotes association of NANOG protein to its own promoter and recruits the NuRD complex, which deacetylates histones. Not required for establishement and maintenance of ESCs. Represses the transcription of a number of genes including GAST, ODC1 and VIM. Binds to the G-rich box in the enhancer region of these genes. {ECO:0000269|PubMed:18757296, ECO:0000269|PubMed:21915945, ECO:0000269|PubMed:22988117}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Interacts with NANOG. Associates with the NuRD complex. {ECO:0000269|PubMed:21915945, ECO:0000269|PubMed:22988117}. +Q6ZPZ3 ZC3H4_MOUSE Zinc finger CCCH domain-containing protein 4 1304 140,967 Alternative sequence (1); Chain (1); Coiled coil (2); Compositional bias (4); Modified residue (16); Zinc finger (3) +Q9ERQ3 ZN704_MOUSE Zinc finger protein 704 (Glucocorticoid-induced gene 1 protein) 566 61,150 Chain (1); Compositional bias (3); Modified residue (2); Motif (2); Mutagenesis (2); Region (1); Zinc finger (1) FUNCTION: Transcription factor which binds to RE2 sequence elements in the MYOD1 enhancer. {ECO:0000269|PubMed:17693064}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17693064}. DOMAIN: The CR1 and CR2 motifs mediate sequence-specific DNA binding, and are important for binding to the MYOD1 enhancer. {ECO:0000269|PubMed:17693064}. +Q8BJ90 ZN771_MOUSE Zinc finger protein 771 317 35,767 Chain (1); Compositional bias (1); Cross-link (1); Zinc finger (8) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q8K2R5 ZN668_MOUSE Zinc finger protein 668 619 68,347 Chain (1); Cross-link (5); Modified residue (3); Sequence conflict (6); Zinc finger (16) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q3V080 ZN583_MOUSE Zinc finger protein 583 568 65,709 Chain (1); Domain (1); Zinc finger (12) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q8BIQ3 ZNF2_MOUSE Zinc finger protein 2 (Zinc finger protein 661) (Zfp-661) 427 48,640 Chain (1); Domain (1); Sequence conflict (3); Zinc finger (9) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q9DB42 ZN593_MOUSE Zinc finger protein 593 (Zinc finger protein T86) 134 15,147 Chain (1); Erroneous initiation (2); Sequence conflict (1); Zinc finger (1) FUNCTION: Negatively modulates the DNA binding activity of Oct-2 and therefore its transcriptional regulatory activity. Could act either by binding to DNA octamer or by interacting with Oct-2. May also be a modulator of other octamer-binding proteins (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. DOMAIN: The protein is largely disordered, with the exception of the zinc finger domain. {ECO:0000250}. +Q71FD5 ZNRF2_MOUSE E3 ubiquitin-protein ligase ZNRF2 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase ZNRF2) (Zinc/RING finger protein 2) 238 23,705 Chain (1); Compositional bias (3); Initiator methionine (1); Lipidation (1); Modified residue (9); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: May play a role in the establishment and maintenance of neuronal transmission and plasticity via its ubiquitin ligase activity. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates. {ECO:0000250}. SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Lysosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell junction, synapse, presynaptic cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Present in presynaptic plasma membranes in neurons. {ECO:0000250}. SUBUNIT: Interacts with UBE2N. {ECO:0000250}. DOMAIN: The RING-type zinc finger domain is required for E3 ligase activity. {ECO:0000250}. TISSUE SPECIFICITY: Expressed primarily in the nervous system. Expression is more intense in the granular cell layer of hippocampus, Purkinje cell layer of the cerebellum and the granular cell layer of the olfactory bulb. Detected in sensory neurons but not expressed in sympatic or enteric neurons. Expressed in testis, adipose tissue, columnar epithelial cells of the gut. {ECO:0000269|PubMed:14561866}. +Q569E7 ZN697_MOUSE Zinc finger protein 697 569 63,065 Chain (1); Compositional bias (1); Sequence conflict (4); Zinc finger (11) FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q91VL9 ZBTB1_MOUSE Zinc finger and BTB domain-containing protein 1 713 81,952 Chain (1); Cross-link (15); Domain (1); Modified residue (2); Sequence conflict (2); Zinc finger (8) FUNCTION: Acts as a transcriptional repressor (By similarity). Represses cAMP-responsive element (CRE)-mediated transcriptional activation (By similarity). In addition, has a role in translesion DNA synthesis. Requires for UV-inducible RAD18 loading, PCNA monoubiquitination, POLH recruitment to replication factories and efficient translesion DNA synthesis (By similarity). Plays a key role in the transcriptional regulation of T lymphocyte development (PubMed:22201126, PubMed:22753936). {ECO:0000250|UniProtKB:Q9Y2K1, ECO:0000269|PubMed:22201126, ECO:0000269|PubMed:22753936}. PTM: Sumoylated with SUMO2 at Lys-328 and to a lesser extent at Lys-266. Sumoylation inhibits its transcriptional repression activity and regulates its subcellular localization (By similarity). {ECO:0000250|UniProtKB:Q9Y2K1}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y2K1}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9Y2K1}. Note=Localized in dot-like structures in the nucleus. Colocalized with SMRT in nuclear bodies. The sumoylated form is preferentially located in the nucleoplasm outside the nuclear bodies (By similarity). {ECO:0000250|UniProtKB:Q9Y2K1}. SUBUNIT: Homodimer (By similarity). Homodimer (PubMed:22753936). Interacts (via BTB domain) with TRIM28 (unphosphorylated or phosphorylated form) (By similarity). {ECO:0000250|UniProtKB:Q9Y2K1}. DOMAIN: Both the BTB domain and C2H2-type motifs are necessary for transcriptional repression activity. The BTB domain is also necessary for oligomerization and efficient sumoylation. The hydrophobic cluster preceding Lys-328 enhanced sumoylation efficiency (By similarity). {ECO:0000250|UniProtKB:Q9Y2K1}.; DOMAIN: The UBZ-type zinc finger domain is required for targeting ZBTB1 to UV damage sites and for PCNA monoubiquitination. UBZ-type zinc finger domain mediates binding to 'Lys-63'-linked polyubiquitin chains (in vitro). {ECO:0000250|UniProtKB:Q9Y2K1}. TISSUE SPECIFICITY: Expressed strongly in thymus and spleen, less in lymph nodes and peripheral blood mononuclear cells (PBMCs) and weakly in bone marrow. Strongly expressed in immature, but weakly in mature bone marrow-lymphocyte B. {ECO:0000269|PubMed:22753936}. +Q8K0L9 ZBT20_MOUSE Zinc finger and BTB domain-containing protein 20 (BTB/POZ domain zinc finger factor HOF) (Zinc finger protein 288) 741 81,034 Alternative sequence (1); Chain (1); Cross-link (4); Domain (1); Modified residue (5); Sequence conflict (2); Zinc finger (5) FUNCTION: May be a transcription factor that may be involved in hematopoiesis, oncogenesis, and immune responses (By similarity). Plays a role in postnatal myogenesis, may be involved in the regulation of satellite cells self-renewal (PubMed:27446912). {ECO:0000250|UniProtKB:Q9HC78, ECO:0000269|PubMed:27446912}. PTM: Sumoylated with SUMO1. {ECO:0000269|PubMed:23213215}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:11744704}. SUBUNIT: Can homodimerize. Binds to DNA. TISSUE SPECIFICITY: Specifically expressed in early hippocampal neurons, cerebellar granule cells and gliogenic progenitors as well as in differentiated glia (PubMed:11744704). Expressed in adult and aged myogenic satellite cells (PubMed:27446912). {ECO:0000269|PubMed:11744704, ECO:0000269|PubMed:27446912}. +Q8BPK2 ZCHC3_MOUSE Zinc finger CCHC domain-containing protein 3 400 43,771 Chain (1); Modified residue (1); Zinc finger (2) FUNCTION: Nucleic acid-binding protein involved in innate immune response to DNA and RNA viruses (PubMed:30193849, PubMed:30135424). Binds DNA and RNA in the cytoplasm and acts by promoting recognition of viral nucleic acids by virus sensors, such as DDX58/RIG-I, IFIH1/MDA5 and CGAS (PubMed:30193849, PubMed:30135424). Acts as a co-sensor for recognition of double-stranded DNA (dsDNA) by cGAS in the cytoplasm, thereby playing a role in innate immune response to cytosolic dsDNA and DNA virus (By similarity). Binds dsDNA and probably acts by promoting sensing of dsDNA by CGAS, leading to enhance CGAS oligomerization and activation (By similarity). Promotes sensing of viral RNA by RIG-I-like receptors proteins DDX58/RIG-I and IFIH1/MDA5 via two mechanisms: binds double-stranded RNA (dsRNA), enhancing the binding of DDX58/RIG-I and IFIH1/MDA5 to dsRNA and promotes 'Lys-63'-linked ubiquitination and subsequent activation of DDX58/RIG-I and IFIH1/MDA5 (By similarity). {ECO:0000250|UniProtKB:Q9NUD5, ECO:0000269|PubMed:30135424, ECO:0000269|PubMed:30193849}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NUD5}. SUBUNIT: Interacts with CGAS (By similarity). Interacts with DDX58/RIG-I (By similarity). Interacts with IFIH1/MDA5 (By similarity). {ECO:0000250|UniProtKB:Q9NUD5}. +Q80X44 ZBT24_MOUSE Zinc finger and BTB domain-containing protein 24 (Bone morphogenetic protein-induced factor 1) (Brain-specific protein 1) (Zinc finger protein 450) 710 78,751 Alternative sequence (3); Chain (1); DNA binding (1); Domain (1); Zinc finger (8) FUNCTION: May be involved in BMP2-induced transcription. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: Widely expressed. Highest level in liver, testis and kidney. {ECO:0000269|PubMed:15526281}. +Q8BGJ0 ZDH15_MOUSE Palmitoyltransferase ZDHHC15 (EC 2.3.1.225) (Zinc finger DHHC domain-containing protein 15) (DHHC-15) 337 39,269 Active site (1); Chain (1); Domain (1); Metal binding (8); Mutagenesis (2); Topological domain (5); Transmembrane (4) TRANSMEM 21 41 Helical. {ECO:0000250|UniProtKB:F1QXD3}.; TRANSMEM 57 77 Helical. {ECO:0000250|UniProtKB:F1QXD3}.; TRANSMEM 173 193 Helical. {ECO:0000250|UniProtKB:F1QXD3}.; TRANSMEM 211 234 Helical. {ECO:0000250|UniProtKB:F1QXD3}. TOPO_DOM 1 20 Cytoplasmic. {ECO:0000250|UniProtKB:F1QXD3}.; TOPO_DOM 42 56 Lumenal. {ECO:0000250|UniProtKB:F1QXD3}.; TOPO_DOM 78 172 Cytoplasmic. {ECO:0000250|UniProtKB:F1QXD3}.; TOPO_DOM 194 210 Lumenal. {ECO:0000250|UniProtKB:F1QXD3}.; TOPO_DOM 235 337 Cytoplasmic. {ECO:0000250|UniProtKB:F1QXD3}. FUNCTION: Catalyzes palmitoylation of Cys residues on target proteins. Catalyzes palmitoylation of GAP43 and DLG4/PSD95. {ECO:0000269|PubMed:15603741}. PTM: Autopalmitoylated (in vitro). {ECO:0000269|PubMed:15603741}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:F1QXD3}; Multi-pass membrane protein {ECO:0000250|UniProtKB:F1QXD3}. DOMAIN: The DHHC domain is required for palmitoyltransferase activity. {ECO:0000269|PubMed:15603741}. TISSUE SPECIFICITY: Expressed mainly in brain. {ECO:0000269|PubMed:15603741}. +P10077 ZFP27_MOUSE Zinc finger protein 27 (Zfp-27) (Protein mKR4) 819 92,894 Alternative sequence (1); Chain (1); Domain (1); Frameshift (1); Sequence conflict (7); Zinc finger (21) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q80TN5 ZDH17_MOUSE Palmitoyltransferase ZDHHC17 (EC 2.3.1.225) (Huntingtin-interacting protein 14) (Zinc finger DHHC domain-containing protein 17) (DHHC-17) 632 72,621 Active site (1); Alternative sequence (2); Chain (1); Domain (1); Erroneous initiation (4); Mutagenesis (2); Region (1); Repeat (7); Sequence caution (1); Sequence conflict (1); Topological domain (6); Transmembrane (6) TRANSMEM 305 325 Helical. {ECO:0000255}.; TRANSMEM 326 346 Helical. {ECO:0000255}.; TRANSMEM 358 378 Helical. {ECO:0000255}.; TRANSMEM 382 402 Helical. {ECO:0000255}.; TRANSMEM 481 501 Helical. {ECO:0000255}.; TRANSMEM 530 550 Helical. {ECO:0000255}. TOPO_DOM 1 304 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 347 357 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 379 381 Lumenal. {ECO:0000255}.; TOPO_DOM 403 480 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 502 529 Lumenal. {ECO:0000255}.; TOPO_DOM 551 632 Cytoplasmic. {ECO:0000255}. FUNCTION: Palmitoyltransferase specific for a subset of neuronal proteins, including SNAP25, DLG4/PSD95, GAD2, SYT1 and HTT (PubMed:15489887, PubMed:15603741, PubMed:25253725). May be involved in the sorting or targeting of critical proteins involved in the initiating events of endocytosis at the plasma membrane (By similarity). May play a role in Mg(2+) transport (By similarity). {ECO:0000250|UniProtKB:Q8IUH5, ECO:0000269|PubMed:15489887, ECO:0000269|PubMed:15603741, ECO:0000269|PubMed:25253725}. PTM: Autopalmitoylated. Autopalmitoylation has a regulatory role in ZDHHC17-mediated Mg(2+) transport. {ECO:0000250|UniProtKB:Q8IUH5}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:25253725}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q8IUH5}; Multi-pass membrane protein {ECO:0000255}. Cell junction, synapse, presynaptic cell membrane {ECO:0000250|UniProtKB:Q8IUH5}; Multi-pass membrane protein {ECO:0000255}. Note=Low extracellular Mg(2+) induces increase in Golgi and in post-Golgi membrane vesicles. {ECO:0000250|UniProtKB:Q8IUH5}. SUBUNIT: Interacts (via ANK repeats) with numerous proteins (via the consensus sequence motif [VIAP]-[VIT]-x-x-Q-P) (By similarity). Interacts (via ANK repeats) with CLIP3 (PubMed:26198635). Interacts (via ANK repeats) with DNAJC5 (via C-terminus) (PubMed:25253725, PubMed:26198635). Interacts (via ANK repeats) with HTT (PubMed:26198635). Interacts (via ANK repeats) with MAP6 (PubMed:26198635). Interacts (via ANK repeats) with SNAP23 (PubMed:26198635). Interacts (via ANK repeats) with SNAP25 (PubMed:25253725, PubMed:26198635). Interacts (via ANK repeats) with EVL (By similarity). May interact (via ANK repeats) with SPRED2 (PubMed:28882895). {ECO:0000250|UniProtKB:Q8IUH5, ECO:0000269|PubMed:25253725, ECO:0000269|PubMed:26198635, ECO:0000269|PubMed:28882895}. DOMAIN: The DHHC domain is required for palmitoyltransferase activity. {ECO:0000250|UniProtKB:Q8IUH5}. TISSUE SPECIFICITY: Expressed in liver, testis, kidney, heart, pancreas and brain. Highest expression was seen in the brain. Localized predominantly in the perinuclear regions of neurons from the cortex, striatum and hippocampus. Colocalized with HTT in the medium spiny neurons of the striatum and the spiny neurons that project into the globus pallidus. {ECO:0000269|PubMed:12393793}. +Q60585 ZFP30_MOUSE Zinc finger protein 30 (Zfp-30) 533 62,769 Chain (1); Cross-link (1); Domain (1); Erroneous initiation (1); Modified residue (1); Zinc finger (13) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q5SS00 ZDBF2_MOUSE DBF4-type zinc finger-containing protein 2 homolog 2493 273,748 Chain (1); Coiled coil (2); Compositional bias (4) +Q810M5 ZDH19_MOUSE Probable palmitoyltransferase ZDHHC19 (EC 2.3.1.225) (Zinc finger DHHC domain-containing protein 19) (DHHC-19) 347 39,009 Chain (1); Domain (1); Transmembrane (4) TRANSMEM 29 49 Helical. {ECO:0000255}.; TRANSMEM 59 79 Helical. {ECO:0000255}.; TRANSMEM 156 176 Helical. {ECO:0000255}.; TRANSMEM 194 214 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. DOMAIN: The DHHC domain is required for palmitoyltransferase activity. {ECO:0000250}. +E9PW05 ZFP54_MOUSE Zinc finger protein 54 (Krueppel-associated box protein 10) (KRAB10) 585 68,369 Chain (1); Domain (1); Erroneous gene model prediction (1); Erroneous initiation (1); Region (1); Sequence conflict (3); Zinc finger (14) FUNCTION: May be involved in transcriptional regulation. {ECO:0000305}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20624068}. Note=Shows widespread expression throughout the nucleus, but appears to be excluded from nucleoli. {ECO:0000269|PubMed:20624068}. TISSUE SPECIFICITY: Expressed at high levels in testis, may also be expressed at low levels in heart, brain, and skeletal muscle. {ECO:0000269|PubMed:10384051}. +P16374 ZFP60_MOUSE Zinc finger protein 60 (Zfp-60) (Zinc finger protein Mfg-3) 707 82,274 Chain (1); Domain (1); Zinc finger (19) FUNCTION: May have a role during differentiation processes. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: Expressed widely and evenly in most adult mouse tissues. +Q6P9Y7 ZFP82_MOUSE Zinc finger protein 82 (Zfp-82) (Zinc finger protein 545) 530 62,122 Alternative sequence (3); Chain (1); Cross-link (1); Domain (1); Erroneous translation (1); Zinc finger (13) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q9CR50 ZN363_MOUSE RING finger and CHY zinc finger domain-containing protein 1 (EC 2.3.2.27) (Androgen receptor N-terminal-interacting protein) (CH-rich-interacting match with PLAG1) (E3 ubiquitin-protein ligase Pirh2) (RING-type E3 ubiquitin transferase RCHY1) (Zinc finger protein 363) 261 30,014 Beta strand (16); Chain (1); Helix (4); Turn (5); Zinc finger (3) Protein modification; protein ubiquitination. FUNCTION: Mediates E3-dependent ubiquitination and proteasomal degradation of target proteins, including p53/TP53, P73, HDAC1 and CDKN1B. Preferentially acts on tetrameric p53/TP53. Increases AR transcription factor activity. Monoubiquitinates the translesion DNA polymerase POLH (By similarity). Contributes to the regulation of the cell cycle progression. {ECO:0000250, ECO:0000269|PubMed:12654245}. PTM: Subject to ubiquitination and proteasomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus speckle {ECO:0000250}. Cytoplasm {ECO:0000250}. SUBUNIT: Monomer and homodimer. Interacts with AR, p53/TP53, MDM2, HDAC1, KAT5, PLAG1, PLAGL2, CDKN1B, COPE, UBE2D2 and GORAB/NTKLBP1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Detected in testis, liver, kidney and heart. {ECO:0000269|PubMed:12654245}. +Q8BG89 ZN365_MOUSE Protein ZNF365 (DISC1-binding zinc-finger protein) (Su48) 408 46,860 Alternative sequence (2); Chain (1); Coiled coil (1); Erroneous initiation (1); Modified residue (5); Sequence conflict (7); Zinc finger (1) FUNCTION: Contributes to genomic stability by preventing telomere dysfunction (PubMed:23776040). Involved in the morphogenesis of basket cells in the somatosensory cortex during embryogenesis (PubMed:23912123). Involved in the positive regulation of oligodendrocyte differentiation during postnatal growth (PubMed:24481677). Involved in dendritic arborization, morphogenesis of spine density dendrite, and establishment of postsynaptic dendrite density in cortical pyramidal neurons (PubMed:25983680). Involved in the regulation of neurogenesis. Negatively regulates neurite outgrowth. Involved in homologous recombination (HR) repair pathway. Required for proper resolution of DNA double-strand breaks (DSBs) by HR. Is required for recovery of stalled replication forks, and directly contributes to genomic stability. Interacts with PARP1 and mediates MRE11-dependent DNA end resection during replication fork recovery (By similarity). {ECO:0000250|UniProtKB:Q70YC5, ECO:0000269|PubMed:23776040, ECO:0000269|PubMed:23912123, ECO:0000269|PubMed:24481677, ECO:0000269|PubMed:25983680}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q70YC5}. SUBUNIT: Homodimer. Interacts with NDE1 and NDEL1 (By similarity). Interacts with DISC1. Interacts with PARP1 (By similarity). {ECO:0000250|UniProtKB:Q70YC5}. TISSUE SPECIFICITY: Detected in several tissues, with highest levels in brain. Also expressed during embryonic development. Expressed in cerebral cortex, hippocampus, striatum, inferior colliculus and thalamus (PubMed:23912123). {ECO:0000269|PubMed:15363853, ECO:0000269|PubMed:16617106, ECO:0000269|PubMed:23912123}. +Q9D2D7 ZN687_MOUSE Zinc finger protein 687 1237 130,350 Alternative sequence (4); Chain (1); Compositional bias (4); Cross-link (12); Modified residue (23); Zinc finger (10) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8N1G0}. Nucleus {ECO:0000250|UniProtKB:Q8N1G0}. Note=Predominantly nuclear. {ECO:0000250|UniProtKB:Q8N1G0}. +B2RXC5 ZN382_MOUSE Zinc finger protein 382 (KRAB/zinc finger suppressor protein 1) (KS1) (Multiple zinc finger and krueppel-associated box protein KS1) 579 66,547 Chain (1); Domain (1); Region (4); Sequence conflict (1); Zinc finger (10) FUNCTION: Functions as a sequence-specific transcriptional repressor. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with TRIM28; enhances the transcriptional repressor activity. {ECO:0000269|PubMed:11154279}. +Q8BKK5 ZN689_MOUSE Zinc finger protein 689 500 57,082 Chain (1); Cross-link (1); Domain (1); Sequence conflict (1); Zinc finger (12) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q80YR4 ZN598_MOUSE E3 ubiquitin-protein ligase ZNF598 (EC 2.3.2.27) (Zinc finger protein 598) 908 99,192 Alternative sequence (2); Chain (1); Compositional bias (2); Erroneous initiation (1); Modified residue (3); Sequence conflict (1); Zinc finger (2) FUNCTION: E3 ubiquitin-protein ligase that plays a key role in the ribosome quality control (RQC), a pathway that takes place when a ribosome has stalled during translation. Required for ribosomes to terminally stall during translation of poly(A) sequences by mediating monoubiquitination of 40S ribosomal protein RPS10/eS10, RPS20/uS10 and RPS3/uS3. Stalling precludes synthesis of a long poly-lysine tail and initiates the RQC pathway to degrade the potentially detrimental aberrant nascent polypeptide. Also acts as a component of the 4EHP-GYF2 complex, a multiprotein complex that acts as a repressor of translation initiation. {ECO:0000250|UniProtKB:Q86UK7}. SUBUNIT: Component of the 4EHP-GYF2 complex, at least composed of EIF4E2, GIGYF2 and ZNF598. {ECO:0000250|UniProtKB:Q86UK7}. +Q3TDE8 ZN691_MOUSE Zinc finger protein 691 283 32,199 Chain (1); Cross-link (1); Modified residue (1); Sequence conflict (4); Zinc finger (7) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q80ZJ6 ZER1_MOUSE Protein zer-1 homolog (Zyg-11 homolog B-like protein) 779 89,076 Alternative sequence (3); Chain (1); Initiator methionine (1); Modified residue (1); Repeat (8) FUNCTION: Probably acts as target recruitment subunit in the E3 ubiquitin ligase complex ZER1-CUL2-Elongin BC. {ECO:0000250}. SUBUNIT: Interacts with the ELOC-ELOB/Elongin BC complex. Part of an E3 ubiquitin ligase complex including ZER1, CUL2 and Elongin BC (By similarity). {ECO:0000250}. +Q64726 ZA2G_MOUSE Zinc-alpha-2-glycoprotein (Zn-alpha-2-GP) (Zn-alpha-2-glycoprotein) 307 35,332 Chain (1); Disulfide bond (2); Domain (1); Glycosylation (3); Modified residue (1); Sequence conflict (2); Signal peptide (1) FUNCTION: Stimulates lipid degradation in adipocytes and causes the extensive fat losses associated with some advanced cancers. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Interacts with PIP. {ECO:0000250}. +Q8BZW4 ZN120_MOUSE Zinc finger protein 120 (Zinc finger protein 31) (mZF31) 436 51,252 Alternative sequence (1); Chain (1); Domain (1); Erroneous gene model prediction (1); Erroneous initiation (2); Frameshift (1); Zinc finger (10) FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed with highest levels in kidney, brain, and liver, and the lowest levels in spleen. {ECO:0000269|PubMed:10360839}. +Q9DAI4 ZBT43_MOUSE Zinc finger and BTB domain-containing protein 43 (Zinc finger protein 297B) 467 52,652 Chain (1); Cross-link (5); Domain (1); Erroneous initiation (2); Modified residue (2); Sequence conflict (1); Zinc finger (3) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Interacts with BDP1. {ECO:0000250}. +Q52KG4 ZBT45_MOUSE Zinc finger and BTB domain-containing protein 45 (Zinc finger protein 499) 520 55,012 Chain (1); Compositional bias (2); Domain (1); Sequence conflict (1); Zinc finger (4) FUNCTION: May be involved in transcriptional regulation (Probable). In the central nervous system, may play a role in glial cell differentiation (PubMed:21131782). {ECO:0000269|PubMed:21131782, ECO:0000305}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q8C827 ZFP62_MOUSE Zinc finger protein 62 (Zfp-62) (ZT3) 914 104,812 Alternative sequence (2); Chain (1); Cross-link (8); Erroneous termination (2); Modified residue (1); Sequence conflict (1); Zinc finger (26) FUNCTION: May play a role in differentiating skeletal muscle. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: Expressed in skeletal and cardiac muscle. {ECO:0000269|PubMed:8808410}. +Q8BJ05 ZC3HE_MOUSE Zinc finger CCCH domain-containing protein 14 735 82,409 Alternative sequence (4); Chain (1); Cross-link (11); Modified residue (13); Sequence conflict (2); Zinc finger (5) FUNCTION: Involved in poly(A) tail length control in neuronal cells. Binds the polyadenosine RNA oligonucleotides. {ECO:0000250|UniProtKB:Q6PJT7}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:19303045, ECO:0000269|PubMed:21734151}. Note=Colocalizes with poly(A) RNA in nuclear speckles. {ECO:0000269|PubMed:21734151}. SUBUNIT: Interacts with HOOK2. Interacts with ZFC3H1 in a RNase-sensitive manner. {ECO:0000250|UniProtKB:Q6PJT7}. TISSUE SPECIFICITY: Expressed in hippocampal pyramidal neurons (at protein level) (PubMed:21734151).Expressed in kidney, liver, muscle, heart brain and testes (PubMed:19303045). Expressed in hippocampal pyramidal neurons (PubMed:21734151). {ECO:0000269|PubMed:21734151}. +Q61467 ZIC4_MOUSE Zinc finger protein ZIC 4 (Zinc finger protein of the cerebellum 4) 341 37,437 Chain (1); Zinc finger (5) FUNCTION: Binds to DNA. {ECO:0000269|PubMed:15465018}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15465018}. TISSUE SPECIFICITY: Exclusively expressed in the cerebellum. {ECO:0000269|PubMed:8682319}. +Q9Z1D8 ZKSC5_MOUSE Zinc finger protein with KRAB and SCAN domains 5 (Zinc finger protein 95) (Zfp-95) 819 93,788 Chain (1); Cross-link (5); Domain (2); Sequence conflict (5); Zinc finger (12) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}. TISSUE SPECIFICITY: Testis specific. {ECO:0000269|PubMed:12860387}. +Q03172 ZEP1_MOUSE Zinc finger protein 40 (Alpha A-crystallin-binding protein 1) (Alpha A-CRYBP1) (Alpha A-crystallin-binding protein I) (Transcription factor alphaA-CRYBP1) 2688 288,344 Chain (1); Compositional bias (5); Modified residue (15); Zinc finger (5) FUNCTION: Transcription factor which binds specifically to the palindromic sequence 5'-GGGAAATCCC-3' in the alpha-A crystallin promoter. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with UTP4. {ECO:0000250}. DOMAIN: Contains two sets of 2 zinc-fingers, which are widely separated and recognize the same DNA sequence. There is a fifth zinc-finger in-between. +A2A884 ZEP3_MOUSE Transcription factor HIVEP3 (Human immunodeficiency virus type I enhancer-binding protein 3 homolog) (KB-binding and recognition component) (Kappa-B and V(D)J recombination signal sequences-binding protein) (Kappa-binding protein 1) (KBP-1) (Recombinant component) (Schnurri-3) (Zinc finger protein ZAS3) 2348 253,413 Chain (1); Coiled coil (1); Compositional bias (6); Erroneous initiation (1); Frameshift (2); Motif (1); Region (7); Repeat (5); Sequence conflict (19); Zinc finger (5) FUNCTION: Plays a role of transcription factor; binds to recognition signal sequences (Rss heptamer) for somatic recombination of immunoglobulin and T-cell receptor gene segments; Binds also to the kappa-B motif of gene such as S100A4, involved in cell progression and differentiation. Kappa-B motif is a gene regulatory element found in promoters and enhancers of genes involved in immunity, inflammation, and growth and that responds to viral antigens, mitogens, and cytokines. Involvement of HIVEP3 in cell growth is strengthened by the fact that its down-regulation promotes cell cycle progression with ultimate formation of multinucleated giant cells. Strongly inhibits TNF-alpha-induced NF-kappa-B activation; Interferes with nuclear factor NF-kappa-B by several mechanisms: as transcription factor, by competing for Kappa-B motif and by repressing transcription in the nucleus; through a non transcriptional process, by inhibiting nuclear translocation of RELA by association with TRAF2, an adapter molecule in the tumor necrosis factor signaling, which blocks the formation of IKK complex. Interaction with TRAF proteins inhibits both NF-Kappa-B-mediated and c-Jun N-terminal kinase/JNK-mediated responses that include apoptosis and proinflammatory cytokine gene expression. Positively regulates the expression of IL2 in T-cell. Essential regulator of adult bone formation. {ECO:0000269|PubMed:10625627, ECO:0000269|PubMed:11035930, ECO:0000269|PubMed:11804591, ECO:0000269|PubMed:12001065, ECO:0000269|PubMed:12193271, ECO:0000269|PubMed:14530385, ECO:0000269|PubMed:14707112, ECO:0000269|PubMed:8255760, ECO:0000269|PubMed:8812474}. PTM: Phosphorylated on threonine and serine residues. Phosphorylation by cyclin-dependent kinase CDK1 decreases HIVEP3 DNA binding affinity, and by epidermal growth factor receptor kinase increases its DNA binding affinity. {ECO:0000269|PubMed:9862992}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11804591}. Nucleus {ECO:0000269|PubMed:11804591}. SUBUNIT: Interacts with TRAF1 AND TRAF2 as well as with JUN. Forms a multimeric complex with RUNX2 and E3 ubiquitin ligase WWP1. {ECO:0000269|PubMed:11804591, ECO:0000269|PubMed:14707112, ECO:0000269|PubMed:16728642}. DOMAIN: ZAS2 domain binds DNA as dimers, tetramers, and multiple of tetramers and readily forms highly ordred DNA-protein structures. {ECO:0000269|PubMed:12193271, ECO:0000269|PubMed:8255760, ECO:0000269|PubMed:8812474}. TISSUE SPECIFICITY: Expressed in macrophages, lymphocytes, brain, thymus, spleen and bone marrow. Expressed in osteoblasts, whole bone and, to a lesser extent, in osteoclasts. {ECO:0000269|PubMed:14530385, ECO:0000269|PubMed:16728642, ECO:0000269|PubMed:8255760, ECO:0000269|PubMed:8812474}. +Q8C0R7 ZMY15_MOUSE Zinc finger MYND domain-containing protein 15 736 81,604 Alternative sequence (2); Chain (1); Compositional bias (2); Sequence conflict (1); Zinc finger (1) FUNCTION: Acts as a transcriptional repressor through interaction with histone deacetylases (HDACs). May regulate haploid genes important for spermiogenesis. {ECO:0000269|PubMed:20675388}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20675388}. Cytoplasm {ECO:0000269|PubMed:20675388}. Note=In step 9-11 spermatids, shifts from nucleus to cytoplasm. SUBUNIT: Interacts with HDAC1, HDAC3, HDAC6 and, to a lesser extent, with HDAC7. {ECO:0000269|PubMed:20675388}. TISSUE SPECIFICITY: Testis-specific. Expressed in pachytene spermatocytes and all developing spermatids, but not in Sertoli, nor Leydig cells (at protein level). {ECO:0000269|PubMed:20675388}. +Q9CU65 ZMYM2_MOUSE Zinc finger MYM-type protein 2 (Zinc finger protein 198) 1376 154,642 Chain (1); Cross-link (29); Modified residue (4); Zinc finger (9) FUNCTION: May function as a transcription factor. {ECO:0000305}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: May be a component of a BHC histone deacetylase complex that contains HDAC1, HDAC2, HMG20B/BRAF35, KDM1A, RCOR1/CoREST, PHF21A/BHC80, ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I. {ECO:0000250}. +Q9D534 ZC21B_MOUSE Zinc finger C2HC domain-containing protein 1B 172 19,689 Chain (1); Zinc finger (1) +Q7TSH3 ZN516_MOUSE Zinc finger protein 516 1157 124,788 Chain (1); Cross-link (4); Region (1); Zinc finger (10) FUNCTION: Transcriptional regulator that binds to the promoter and activates the transcription of genes promoting brown adipose tissue (BAT) differentiation. Among brown adipose tissue-specific genes, binds the proximal region of the promoter of the UCP1 gene to activate its transcription and thereby regulate thermogenesis. May also play a role in the cellular response to replication stress (By similarity). {ECO:0000250|UniProtKB:Q92618, ECO:0000269|PubMed:25578880}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25578880}. SUBUNIT: Interacts with PRDM16; the interaction is direct and may play a role in the transcription of brown adipose tissue-specific genes. {ECO:0000269|PubMed:25578880}. TISSUE SPECIFICITY: Expressed by adipocytes more specifically in brown adipose tissue compared to white adipose tissue (WAT). {ECO:0000269|PubMed:25578880}. +Q62394 ZN185_MOUSE Zinc finger protein 185 (LIM domain protein Zfp185) (P1-A) 352 38,322 Chain (1); Compositional bias (1); Domain (1); Modified residue (2) FUNCTION: May be involved in the regulation of cellular proliferation and/or differentiation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell junction, focal adhesion {ECO:0000250}. TISSUE SPECIFICITY: Expressed in skin, kidney, ovary, testis. Also expressed in brain, cartilage, heart, lung, spleen and thymus. +Q80TS5 ZN423_MOUSE Zinc finger protein 423 (Early B-cell factor-associated zinc finger protein) (Olf1/EBF-associated zinc finger protein) (Smad- and Olf-interacting zinc finger protein) 1292 145,351 Alternative sequence (1); Chain (1); Erroneous initiation (2); Modified residue (4); Sequence caution (1); Sequence conflict (3); Zinc finger (30) FUNCTION: Transcription factor that can both act as an activator or a repressor depending on the context. Plays a central role in BMP signaling and olfactory neurogenesis. Associates with SMADs in response to BMP2 leading to activate transcription of BMP target genes. Acts as a transcriptional repressor via its interaction with EBF1, a transcription factor involved in terminal olfactory receptor neurons differentiation; this interaction preventing EBF1 to bind DNA and activate olfactory-specific genes. Involved in olfactory neurogenesis by participating in a developmental switch that regulates the transition from differentiation to maturation in olfactory receptor neurons. Controls proliferation and differentiation of neural precursors in cerebellar vermis formation. {ECO:0000269|PubMed:16943432, ECO:0000269|PubMed:17151198, ECO:0000269|PubMed:17521568, ECO:0000269|PubMed:17524391}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Homodimer (By similarity). Interacts with SMAD1 and SMAD4. Interacts with EBF1 (By similarity). Interacts with PARP1. Interacts with CEP290 (By similarity). {ECO:0000250}. DOMAIN: Uses different DNA- and protein-binding zinc fingers to regulate the distinct BMP-Smad and Olf signaling pathways. C2H2-type zinc fingers 14-19 mediate the interaction with SMAD1 and SMAD4, while zinc fingers 28-30 mediate the interaction with EBF1. zinc fingers 2-8 bind the 5'-CCGCCC-3' DNA sequence in concert with EBF1, while zinc fingers 9-13 bind BMP target gene promoters in concert with SMADs (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Within the cerebellum, Zfp423 is expressed in both ventricular and external germinal zones. Transiently expressed in newly differentiating olfactory-receptor neurons. {ECO:0000269|PubMed:16943432, ECO:0000269|PubMed:17151198, ECO:0000269|PubMed:17521568}. +E9QAG8 ZN431_MOUSE Zinc finger protein 431 (Zinc finger protein 932) 526 61,280 Chain (1); Domain (1); Sequence conflict (1); Zinc finger (15) FUNCTION: Sequence-specific DNA binding transcriptional repressor. Represses target gene transcription by recruiting HDAC1 and HDAC2 histone deacetylases. Acts as a specific transcriptional repressor for PTCH1 during embryonic development. Required for osteoblast differentiation and sonic hedgehog/SHH signaling response. Binds to the consensus site 5'-GCGCCC-3' in the promoter of PTCH1. {ECO:0000269|PubMed:21177534, ECO:0000269|PubMed:22391310}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21177534}. SUBUNIT: Interacts (via KRAB domain) with HDAC2; the interaction is direct. Interacts (via KRAB domain) with HDAC1. {ECO:0000269|PubMed:21177534, ECO:0000269|PubMed:22391310}. DOMAIN: The KRAB domain is necessary for its repressive activity. TISSUE SPECIFICITY: Expressed in brain, heart, lung, thymus, spleen, lymph node, liver, kidney, muscle, testis, ovary, skin and uterus. {ECO:0000269|PubMed:21177534}. +Q8R151 ZNFX1_MOUSE NFX1-type zinc finger-containing protein 1 1909 218,828 Chain (1); Coiled coil (2); Compositional bias (3); Erroneous initiation (2); Sequence conflict (4); Zinc finger (4) +Q3TXX3 ZFY27_MOUSE Protrudin (Zinc finger FYVE domain-containing protein 27) 415 46,202 Alternative sequence (1); Chain (1); Erroneous initiation (1); Intramembrane (1); Region (5); Sequence conflict (1); Topological domain (4); Transmembrane (2); Zinc finger (1) INTRAMEM 193 213 Helical. {ECO:0000255}. TRANSMEM 67 87 Helical. {ECO:0000255}.; TRANSMEM 89 109 Helical. {ECO:0000255}. TOPO_DOM 1 66 Cytoplasmic. {ECO:0000269|PubMed:24668814}.; TOPO_DOM 88 88 Lumenal. {ECO:0000269|PubMed:24668814}.; TOPO_DOM 110 192 Cytoplasmic. {ECO:0000269|PubMed:24668814}.; TOPO_DOM 214 415 Cytoplasmic. {ECO:0000269|PubMed:24668814}. FUNCTION: Key regulator of RAB11-dependent vesicular trafficking during neurite extension through polarized membrane transport (By similarity). Promotes axonal elongation and contributes to the establishment of neuronal cell polarity (PubMed:24251978). Involved in nerve growth factor-induced neurite formation in VAPA-dependent manner. Contributes to both the formation and stabilization of the tubular ER network. Involved in ER morphogenesis by regulating the sheet-to-tubule balance and possibly the density of tubule interconnections (By similarity). Acts as an adapter protein that facilitates the interaction of KIF5A with VAPA, VAPB, SURF4, RAB11A, RAB11B and RTN3 and the ZFYVE27-KIF5A complex contributes to the transport of these proteins in neurons. Can induce formation of neurite-like membrane protrusions in non-neuronal cells in a KIF5A/B-dependent manner (PubMed:21976701). {ECO:0000250|UniProtKB:Q5T4F4, ECO:0000269|PubMed:21976701, ECO:0000269|PubMed:24251978}. PTM: Phosphorylated. Phosphorylation is induced by NGF through the MAPK/ERK pathway and modulates interaction with RAB11A (Probable). {ECO:0000305|PubMed:18459960}. SUBCELLULAR LOCATION: Recycling endosome membrane {ECO:0000305|PubMed:17082457}; Multi-pass membrane protein {ECO:0000305|PubMed:17082457}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:24668814}; Multi-pass membrane protein {ECO:0000269|PubMed:24668814}. Cell projection, growth cone membrane {ECO:0000269|PubMed:17082457}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes at both dendrites and axons (PubMed:17082457). Localizes to endoplasmic reticulum tubular network. {ECO:0000269|PubMed:17082457, ECO:0000269|PubMed:24668814}. SUBUNIT: Can form homooligomers (monomers, dimers and tetramers) (By similarity). Interacts with RAB11A (GDP-bound form); regulates RAB11A (PubMed:21976701). Interacts with FKBP8; may negatively regulate ZFYVE27 phosphorylation (By similarity). Isoform 1 interacts to a greater extent than isoform 2 with VAPB (via MSP domain). Isoform 1 interacts to a greater extent than isoform 2 with VAPA (via MSP domain) (PubMed:24251978). Interaction with VAPA may regulate ZFYVE27 retention in the endoplasmic reticulum and its function in cell projections formation. Interacts with ATL2, ATL3, SPAST and RTN3 (By similarity). Interacts with REEP1, REEP5 and ATL1 (PubMed:24668814). Interacts with RAB11B (GDP-bound form), SURF4, KIF5B and KIF5C (PubMed:21976701). Isoform 1 and 2 interact with KIFA (PubMed:21976701, PubMed:24251978). {ECO:0000250|UniProtKB:Q5T4F4, ECO:0000269|PubMed:21976701, ECO:0000269|PubMed:24251978, ECO:0000269|PubMed:24668814}. TISSUE SPECIFICITY: Astrocytes express both isoform 1 and isoform 2 and oligodendrocytes express only isoform 2 (at protein level). Isoform 1 is expressed specifically in the central nervous system and selectively in neuronal cells. Isoform 2 is expressed in cerebrum, cerebellum, spinal cord, heart, thymus, spleen, intestine and lung. {ECO:0000269|PubMed:17082457, ECO:0000269|PubMed:24251978}. +P0CL69 ZN703_MOUSE Zinc finger protein 703 (Zinc finger elbow-related proline domain protein 1) 594 58,730 Chain (1); Compositional bias (1); Initiator methionine (1); Modified residue (3); Zinc finger (1) FUNCTION: Transcriptional corepressor which does not bind directly to DNA and may regulate transcription through recruitment of histone deacetylases to gene promoters. Regulates cell adhesion, migration and proliferation. May be required for segmental gene expression during hindbrain development. {ECO:0000269|PubMed:21317240}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21317240}. Cytoplasm {ECO:0000269|PubMed:21317240}. SUBUNIT: Interacts with DCAF7 and PHB2 (By similarity). Interacts with TLE4; increases transcriptional repression. {ECO:0000250, ECO:0000269|PubMed:21317240}. TISSUE SPECIFICITY: Expressed in mammary epithelium. {ECO:0000269|PubMed:21317240}. +Q9Z0U1 ZO2_MOUSE Tight junction protein ZO-2 (Tight junction protein 2) (Zona occludens protein 2) (Zonula occludens protein 2) 1167 131,280 Beta strand (6); Chain (1); Compositional bias (1); Domain (5); Helix (2); Modified residue (36); Region (1); Sequence conflict (23) FUNCTION: Plays a role in tight junctions and adherens junctions. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus {ECO:0000250}. Cell junction, tight junction {ECO:0000269|PubMed:26609154}. Note=Also nuclear under environmental stress conditions and in migratory endothelial cells and subconfluent epithelial cell cultures. {ECO:0000250}. SUBUNIT: Homodimer, and heterodimer with ZO1. Interacts with UBN1. Interacts with SCRIB (By similarity). Interacts with occludin and SAFB. Interaction with SAFB occurs in the nucleus. Interacts with USP53 (via the C-terminal region) (PubMed:26609154). {ECO:0000250|UniProtKB:Q9UDY2, ECO:0000269|PubMed:12403786, ECO:0000269|PubMed:26609154}. +Q9QXY1 ZO3_MOUSE Tight junction protein ZO-3 (Tight junction protein 3) (Zona occludens protein 3) (Zonula occludens protein 3) 905 99,324 Chain (1); Domain (5); Modified residue (14) FUNCTION: Tjp1, Tjp2, and Tjp3 are closely related scaffolding proteins that link tight junction (TJ) transmembrane proteins such as claudins, junctional adhesion molecules, and occludin to the actin cytoskeleton (PubMed:17000770). The tight junction acts to limit movement of substances through the paracellular space and as a boundary between the compositionally distinct apical and basolateral plasma membrane domains of epithelial and endothelial cells. Binds and recruits PatJ to tight junctions where it connects and stabilizes apical and lateral components of tight junctions (By similarity). Promotes cell-cycle progression through the sequestration of cyclin D1 (Ccnd1) at tight junctions during mitosis which prevents Ccnd1 degradation during M-phase and enables S-phase transition (PubMed:21411630). With Tjp1 and Tjp2, participates to the junctional retention and stability of the transcription factor DbpA, but is not involved in its shuttling to the nucleus (By similarity). Contrary to Tjp2, Tjp3 is dispensable for individual viability, embryonic development, epithelial differentiation, and the establishment of TJs, at least in the laboratory environment (PubMed:17000770, PubMed:18172007). {ECO:0000250|UniProtKB:O62683, ECO:0000250|UniProtKB:O95049, ECO:0000269|PubMed:17000770, ECO:0000269|PubMed:18172007, ECO:0000269|PubMed:21411630}. PTM: Phosphorylated (By similarity). {ECO:0000250|UniProtKB:O62683}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21411630}; Peripheral membrane protein {ECO:0000269|PubMed:21411630}; Cytoplasmic side {ECO:0000269|PubMed:21411630}. Cell junction, tight junction {ECO:0000269|PubMed:10601346, ECO:0000269|PubMed:14622136, ECO:0000269|PubMed:19538286, ECO:0000269|PubMed:21411630}. Nucleus {ECO:0000250|UniProtKB:O95049}. Note=Exhibits predominant nuclear expression in proliferating cells but is exclusively junctionally expressed after confluence is reached (By similarity). Shows an epithelial-specific tight junction localization in a Tjp1/Tjp2-dependent fashion (PubMed:21411630). {ECO:0000250|UniProtKB:O95049, ECO:0000269|PubMed:21411630}. SUBUNIT: Interacts with occludin OCLN, claudins and TPJ1 (By similarity). Interacts with PATJ (By similarity). Interacts with UBN1 (By similarity). Interacts with FASLG (By similarity). Interacts with CCND1 (PubMed:21411630). {ECO:0000250|UniProtKB:O62683, ECO:0000269|PubMed:21411630}. TISSUE SPECIFICITY: Is concentrated in various types of epithelium, in tissues such as the lung, liver and kidney, but not in endothelium or at cadherin-based cell-cell adhesion sites (PubMed:14622136). {ECO:0000269|PubMed:14622136}. +Q9DAU9 ZN654_MOUSE Zinc finger protein 654 571 65,164 Chain (1); Compositional bias (1); Erroneous initiation (1); Modified residue (2); Zinc finger (5) FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q3UHH1 ZSWM8_MOUSE Zinc finger SWIM domain-containing protein 8 1832 197,061 Alternative sequence (9); Chain (1); Compositional bias (4); Erroneous initiation (1); Modified residue (11); Sequence conflict (3); Zinc finger (1) +Q9CQU5 ZWINT_MOUSE ZW10 interactor (ZW10-interacting protein 1) (Zwint-1) 252 28,713 Chain (1); Coiled coil (1); Modified residue (2); Region (1); Sequence conflict (1) FUNCTION: Part of the MIS12 complex, which is required for kinetochore formation and spindle checkpoint activity. Required to target ZW10 to the kinetochore at prometaphase (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Note=Localizes to kinetochores from late prophase to anaphase. {ECO:0000250}. SUBUNIT: Interacts with ZW10 and MIS12. Interacts with the NDC80 subunit of the NDC80 complex specifically during mitosis. Also interacts with KNL1, CETN3, DSN1 and PMF1 (By similarity). {ECO:0000250}. +B2KFW1 ZSC20_MOUSE Zinc finger and SCAN domain-containing protein 20 (Zinc finger protein 31) 1030 115,379 Alternative sequence (1); Chain (1); Domain (1); Erroneous initiation (2); Sequence conflict (4); Zinc finger (10) FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}. +A2CE44 ZXDB_MOUSE Zinc finger X-linked protein ZXDB 873 90,376 Chain (1); Compositional bias (2); Frameshift (1); Modified residue (1); Region (2); Sequence conflict (6); Zinc finger (10) FUNCTION: Cooperates with CIITA to promote transcription of MHC class I and MHC class II genes. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Self-associates. Interacts with ZXDC and CIITA (By similarity). {ECO:0000250}. +Q8C8V1 ZXDC_MOUSE Zinc finger protein ZXDC 858 90,755 Alternative sequence (6); Chain (1); Cross-link (1); Erroneous initiation (2); Frameshift (2); Sequence conflict (3); Zinc finger (10) FUNCTION: Cooperates with CIITA to promote transcription of MHC class I and MHC class II genes. {ECO:0000250}. PTM: Sumoylated at Lys-661 with SUMO1, SUMO2 and SUMO3; sumoylation enhances the activity of the transcriptional activation domain. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Self-associates. Interacts with ZXDB and CIITA (By similarity). {ECO:0000250}. +Q8R205 ZC3HA_MOUSE Zinc finger CCCH domain-containing protein 10 435 46,121 Chain (1); Coiled coil (1); Compositional bias (3); Modified residue (2); Zinc finger (3) FUNCTION: Specific regulator of miRNA biogenesis. Binds, via the C3H1-type zinc finger domains, to the binding motif 5'-GCAGCGC-3' on microRNA pri-MIR143 and negatively regulates the processing to mature microRNA. {ECO:0000250|UniProtKB:Q96K80}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96K80}. +E9Q784 ZC3HD_MOUSE Zinc finger CCCH domain-containing protein 13 1729 203,755 Chain (1); Coiled coil (2); Compositional bias (6); Cross-link (1); Modified residue (46); Sequence conflict (1); Zinc finger (1) FUNCTION: Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing (PubMed:29535189, PubMed:29547716). Acts as a key regulator of m6A methylation by promoting m6A methylation of mRNAs at the 3'-UTR (PubMed:29547716). Controls embryonic stem cells (ESCs) pluripotency via its role in m6A methylation (PubMed:29547716). In the WMM complex, anchors component of the MACOM subcomplex in the nucleus (PubMed:29547716). Also required for bridging WTAP to the RNA-binding component RBM15 (RBM15 or RBM15B) (PubMed:29535189). {ECO:0000269|PubMed:29535189, ECO:0000269|PubMed:29547716}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q5T200}. Nucleus, nucleoplasm {ECO:0000269|PubMed:29547716}. SUBUNIT: Component of the WMM complex, a N6-methyltransferase complex composed of a catalytic subcomplex, named MAC, and of an associated subcomplex, named MACOM (PubMed:29535189, PubMed:29547716). The MAC subcomplex is composed of METTL3 and METTL14 (PubMed:29535189, PubMed:29547716). The MACOM subcomplex is composed of WTAP, ZC3H13, CBLL1/HAKAI, VIRMA, and, in some cases of RBM15 (RBM15 or RBM15B) (PubMed:29535189, PubMed:29547716). Also component of a MACOM-like complex, named WTAP complex, composed of WTAP, ZC3H13, CBLL1/HAKAI, VIRMA, RBM15, BCLAF1 and THRAP3 (By similarity). {ECO:0000250|UniProtKB:Q5T200, ECO:0000269|PubMed:29535189, ECO:0000269|PubMed:29547716}. +B2RRE4 Z518B_MOUSE Zinc finger protein 518B 1077 118,997 Chain (1); Cross-link (3); Zinc finger (3) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +D2EAC2 ZBED6_MOUSE Zinc finger BED domain-containing protein 6 (Muscle growth regulator) (MGR) 980 109,152 Alternative sequence (1); Chain (1); Erroneous initiation (1); Modified residue (1); Region (1); Sequence conflict (2); Zinc finger (2) FUNCTION: Transcriptional repressor which binds to the consensus sequence 5'-GCTCGC-3' and represses transcription of IGF2. May also regulate expression of other target genes containing the binding site. {ECO:0000269|PubMed:20016685, ECO:0000269|PubMed:20134481}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20016685}. Nucleus, nucleolus {ECO:0000269|PubMed:20016685}. Note=Located predominantly in the nucleolus but is also dispersed throughout the nucleus. {ECO:0000269|PubMed:20016685}. TISSUE SPECIFICITY: Shows broad tissue distribution with expression detected in brain, stomach, intestine, heart, kidney, liver, lung, skeletal muscle, ovary, spleen, tail and testis. {ECO:0000269|PubMed:20016685}. +Q7TQG0 ZBTB5_MOUSE Zinc finger and BTB domain-containing protein 5 (Transcription factor ZNF-POZ) 670 73,215 Chain (1); Cross-link (10); Domain (1); Erroneous initiation (1); Modified residue (2); Sequence conflict (1); Zinc finger (2) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q6IR42 ZCPW1_MOUSE Zinc finger CW-type PWWP domain protein 1 630 70,569 Chain (1); Coiled coil (1); Domain (1); Modified residue (1); Sequence conflict (1); Zinc finger (1) +Q6NZF1 ZC11A_MOUSE Zinc finger CCCH domain-containing protein 11A 792 86,492 Chain (1); Coiled coil (1); Compositional bias (1); Cross-link (5); Erroneous initiation (1); Frameshift (1); Modified residue (6); Sequence caution (1); Sequence conflict (8); Zinc finger (3) FUNCTION: Involved in nuclear mRNA export; probably mediated by association with the TREX complex. {ECO:0000250}. SUBUNIT: Interacts with THOC2, DDX39 and POLDIP3; the interactions are ATP-dependent and indicative for an association with the TREX complex. {ECO:0000250}. +Q8K0C5 ZG16_MOUSE Zymogen granule membrane protein 16 (Zymogen granule protein 16) (Secretory lectin ZG16) 167 18,210 Chain (1); Domain (1); Signal peptide (1) FUNCTION: May play a role in protein trafficking. May act as a linker molecule between the submembranous matrix on the luminal side of zymogen granule membrane (ZGM) and aggregated secretory proteins during granule formation in the TGN (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. Cytoplasmic vesicle lumen {ECO:0000250}. Golgi apparatus lumen {ECO:0000250}. Note=Stored in zymogen granules. {ECO:0000250}. +Q5D1E7 ZC12A_MOUSE Endoribonuclease ZC3H12A (EC 3.1.-.-) (Monocyte chemotactic protein-induced protein 1) (MCP-induced protein 1) (MCPIP-1) (Regnase-1) (Reg1) (Zinc finger CCCH domain-containing protein 12A) 596 65,598 Beta strand (14); Chain (1); Compositional bias (1); Helix (14); Metal binding (1); Modified residue (3); Mutagenesis (15); Region (5); Sequence conflict (2); Turn (1); Zinc finger (1) FUNCTION: Endoribonuclease involved in various biological functions such as cellular inflammatory response and immune homeostasis, glial differentiation of neuroprogenitor cells, cell death of cardiomyocytes, adipogenesis and angiogenesis. Functions as an endoribonuclease involved in mRNA decay (PubMed:26000482). Modulates the inflammatory response by promoting the degradation of a set of translationally active cytokine-induced inflammation-related mRNAs, such as IL6 and IL12B, during the early phase of inflammation (PubMed:19322177, PubMed:21115689, PubMed:23185455, PubMed:26000482). Prevents aberrant T-cell-mediated immune reaction by degradation of multiple mRNAs controlling T-cell activation, such as those encoding cytokines (IL6 and IL2), cell surface receptors (ICOS, TNFRSF4 and TNFR2) and transcription factor (REL) (PubMed:23706741, PubMed:26000482, PubMed:19322177, PubMed:21115689, PubMed:23185455). Inhibits cooperatively with ZC3H12A the differentiation of helper T cells Th17 in lungs. They repress target mRNA encoding the Th17 cell-promoting factors IL6, ICOS, REL, IRF4, NFKBID and NFKBIZ. The cooperation requires RNA-binding by RC3H1 and the nuclease activity of ZC3H12A (PubMed:25282160). Self regulates by destabilizing its own mRNA (PubMed:22037600). Cleaves mRNA harboring a stem-loop (SL), often located in their 3'-UTRs, during the early phase of inflammation in a helicase UPF1-dependent manner (PubMed:19322177, PubMed:23185455, PubMed:23706741, PubMed:26000482, PubMed:26134560). Plays a role in the inhibition of microRNAs (miRNAs) biogenesis (By similarity). Cleaves the terminal loop of a set of precursor miRNAs (pre-miRNAs) important for the regulation of the inflammatory response leading to their degradation, and thus preventing the biosynthesis of mature miRNAs (By similarity). Plays also a role in promoting angiogenesis in response to inflammatory cytokines by inhibiting the production of antiangiogenic microRNAs via its anti-dicer RNase activity (By similarity). Affects the overall ubiquitination of cellular proteins (PubMed:21115689). Positively regulates deubiquitinase activity promoting the cleavage at 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains on TNF receptor-associated factors (TRAFs), preventing JNK and NF-kappa-B signaling pathway activation, and hence negatively regulating macrophage-mediated inflammatory response and immune homeostasis (PubMed:21115689). Induces also deubiquitination of the transcription factor HIF1A, probably leading to its stabilization and nuclear import, thereby positively regulating the expression of proangiogenic HIF1A-targeted genes. Involved in a TANK-dependent negative feedback response to attenuate NF-kappaB activation through the deubiquitination of IKBKG or TRAF6 in response to interleukin-1-beta (IL1B) stimulation or upon DNA damage (By similarity). Prevents stress granules (SGs) formation and promotes macrophage apoptosis under stress conditions, including arsenite-induced oxidative stress, heat shock, and energy deprivation (PubMed:21971051). Plays a role in the regulation of macrophage polarization; promotes IL4-induced polarization of macrophages M1 into anti-inflammatory M2 state (PubMed:25934862). May also act as a transcription factor that regulates the expression of multiple genes involved in inflammatory response, angiogenesis, adipogenesis and apoptosis (PubMed:18178554, PubMed:19666473, PubMed:22739135). Functions as a positive regulator of glial differentiation of neuroprogenitor cells through an amyloid precursor protein (APP)-dependent signaling pathway (By similarity). Attenuates septic myocardial contractile dysfunction in response to lipopolysaccharide (LPS) by reducing I-kappa-B-kinase (IKK)-mediated NF-kappa-B activation, and hence myocardial proinflammatory cytokine production (PubMed:21616078). {ECO:0000250|UniProtKB:Q5D1E8, ECO:0000269|PubMed:18178554, ECO:0000269|PubMed:19322177, ECO:0000269|PubMed:19666473, ECO:0000269|PubMed:21115689, ECO:0000269|PubMed:21616078, ECO:0000269|PubMed:21971051, ECO:0000269|PubMed:22037600, ECO:0000269|PubMed:22739135, ECO:0000269|PubMed:23185455, ECO:0000269|PubMed:23706741, ECO:0000269|PubMed:25282160, ECO:0000269|PubMed:25934862, ECO:0000269|PubMed:26000482, ECO:0000269|PubMed:26134560}. PTM: Proteolytically cleaved between Arg-111 and Arg-214 by MALT1 in activated T-cells; cleavage at Arg-111 is critical for promoting ZC3H12A degradation in response to T-cell receptor (TCR) stimulation, and hence is necessary for prolonging the stability of a set of mRNAs controlling T-cell activation and Th17 cell differentiation. {ECO:0000269|PubMed:23706741, ECO:0000269|PubMed:25282160}.; PTM: Phosphorylated by IRAK1; phosphorylation is necessary for subsequent phosphorylation by the I-kappa-B-kinase (IKK) complex. Phosphorylated by I-kappa-B-kinases (IKKs) at Ser-435 and Ser-439 upon lipopolysaccharide (LPS) or IL1B stimulation in macrophages through the MyD88-dependent signaling pathway; these phosphorylations promote rapid ubiquitin proteasome-mediated degradation of ZC3H12A in macrophages and hence allows its target mRNAs, such as IL6, to escape from degradation and accumulate during the inflammatory response (PubMed:22037600). {ECO:0000269|PubMed:22037600}.; PTM: Ubiquitinated; ubiquitination is induced in response to interleukin IL1 receptor stimuli in a IKBKB/IKKB and IRAK1-dependent manner, leading to proteasome-mediated degradation (PubMed:22037600). {ECO:0000269|PubMed:22037600}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16574901, ECO:0000269|PubMed:19322177}. Cytoplasm {ECO:0000269|PubMed:19322177, ECO:0000269|PubMed:21971051, ECO:0000269|PubMed:26000482}. Rough endoplasmic reticulum membrane {ECO:0000269|PubMed:26000482}; Peripheral membrane protein {ECO:0000269|PubMed:26000482}; Cytoplasmic side {ECO:0000269|PubMed:26000482}. Cytoplasmic granule {ECO:0000269|PubMed:21971051}. Cytoplasm, P-body {ECO:0000250|UniProtKB:Q5D1E8}. Note=Predominantly localized in the cytoplasm (PubMed:19322177). Colocalizes with GW182 on many granule-like structures, probably corresponding to cytoplasmic GW bodies (GWBs), also called processing bodies (P bodies) (PubMed:21971051). Colocalizes with calnexin on the surface of the rough endoplasmic reticulum (RER) membrane and with translationally active polysomes (PubMed:26000482). Colocalizes with ZC3H12D in cytoplasmic mRNA processing P-body, also known as GW bodies (GWBs) (By similarity). {ECO:0000250|UniProtKB:Q5D1E8, ECO:0000269|PubMed:19322177, ECO:0000269|PubMed:21971051, ECO:0000269|PubMed:26000482}. SUBUNIT: Oligomer (By similarity). Found in a deubiquitination complex with TANK, USP10 and ZC3H12A; this complex inhibits genotoxic stress- or interleukin-1-beta-mediated NF-kappaB activation by promoting IKBKG or TRAF6 deubiquitination. Interacts with IKBKG; this interaction increases in response to DNA damage. Interacts with TANK; this interaction increases in response to DNA damage and serves as a bridge to anchor both TANK and USP10 into a deubiquitinating complex. Interacts with TRAF6; this interaction increases in response to DNA damage and is stimulated by TANK. Interacts with USP10; this interaction increases in response to DNA damage and serves as a bridge to anchor both TANK and USP10 into a deubiquitinating complex. Interacts with ZC3H12D. Interacts with TNRC6A. Interacts with IKBKB/IKKB. Interacts with IKBKB/IKKB (By similarity). Interacts with IKBKB/IKKB (PubMed:22037600). Interacts with BTRC; the interaction occurs when ZC3H12A is phosphorylated in a IKBKB/IKKB-dependent manner (PubMed:22037600). Interacts with IRAK1; this interaction increases the interaction between ZC3H12A and IKBKB/IKKB (PubMed:22037600). Interacts with UPF1; this interaction occurs in a mRNA translationally active- and termination-dependent manner and is essential for ZC3H12A-mediated degradation of target mRNAs (PubMed:26000482). Associates with ribosomes (PubMed:26000482). Interacts with ubiquitin (PubMed:21115689). {ECO:0000250|UniProtKB:Q5D1E8, ECO:0000269|PubMed:21115689, ECO:0000269|PubMed:22037600, ECO:0000269|PubMed:26000482}. DOMAIN: The C3H1-type zinc finger domain and C-terminal region are necessary for pre-miRNA binding (By similarity). The C-terminal region and proline-rich domain are necessary for oligomerization (By similarity). {ECO:0000250|UniProtKB:Q5D1E8}. TISSUE SPECIFICITY: Highly expressed in macrophages (PubMed:18178554). Expressed in lung, lymph nodes, spleen and thymus (PubMed:22037600). Expressed weakly in heart (PubMed:21616078). Expressed weakly in cardiomyocytes (at protein level) (PubMed:16574901). Expressed in spleen, lung, intestine, brown adipose tissue and thymus (PubMed:18682727). Weakly expressed in the heart (PubMed:16574901). Weakly expressed in cardiomyocytes (PubMed:16574901). {ECO:0000269|PubMed:16574901, ECO:0000269|PubMed:18178554, ECO:0000269|PubMed:18682727, ECO:0000269|PubMed:21616078, ECO:0000269|PubMed:22037600}. DISEASE: Note=Increased expression of ZC3H12A is associated with ischemic heart disease (PubMed:16574901). {ECO:0000269|PubMed:16574901}. +Q8BID6 ZBT46_MOUSE Zinc finger and BTB domain-containing protein 46 (BTB-ZF protein expressed in effector lymphocytes) (BZEL) (BTB/POZ domain-containing protein 4) 600 65,499 Alternative sequence (2); Chain (1); Cross-link (1); Domain (1); Erroneous initiation (2); Modified residue (1); Sequence conflict (1); Zinc finger (2) FUNCTION: Function as a transcriptional repressor for PRDM1. {ECO:0000269|PubMed:22370726}. PTM: Sumoylated. Desumoylation by PPPDE2 reverses transcriptional repression activity. {ECO:0000269|PubMed:22370726}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q61329 ZFHX3_MOUSE Zinc finger homeobox protein 3 (AT motif-binding factor 1) (AT-binding transcription factor 1) (Alpha-fetoprotein enhancer-binding protein) (Zinc finger homeodomain protein 3) (ZFH-3) 3726 406,570 Chain (1); Compositional bias (14); Cross-link (4); DNA binding (4); Modified residue (16); Motif (1); Mutagenesis (1); Zinc finger (23) FUNCTION: Transcriptional regulator which can act as an activator or a repressor. Inhibits the enhancer element of the AFP gene by binding to its AT-rich core sequence. In concert with SMAD-dependent TGF-beta signaling can repress the transcription of AFP via its interaction with SMAD2/3 (By similarity). Regulates the circadian locomotor rhythms via transcriptional activation of neuropeptidergic genes which are essential for intercellular synchrony and rhythm amplitude in the suprachiasmatic nucleus (SCN) of the brain (PubMed:26232227). Regulator of myoblasts differentiation through the binding to the AT-rich sequence of MYF6 promoter and promoter repression. Down-regulates the MUC5AC promoter in gastric cancer. In association with RUNX3, upregulates CDKN1A promoter activity following TGF-beta stimulation (By similarity). {ECO:0000250|UniProtKB:Q15911, ECO:0000269|PubMed:26232227}. PTM: Phosphorylated at Ser-2634 in embryonic and adult brain. Phosphorylated at Ser-1600, Ser-2795, Ser-2804, Ser-2900, Ser-3434, Ser-3443, Ser-3616 and Ser-3700 in the embryonic brain only. Hpyerphosphorylated in embryonic brain and phosphorylation decreases its sensitivity to calpain-mediated proteolysis. {ECO:0000269|PubMed:23022192}.; PTM: Adult brain-derived ZFHX3 is sensitive, but embryonic brain-derived ZFHX3 is resistant to calpain 1-mediated proteolysis. {ECO:0000269|PubMed:23022192}.; PTM: Ubiquitinated, leading to its proteasomal degradation. {ECO:0000250|UniProtKB:Q15911}.; PTM: Nuclear localization is essential for its sumoylation. {ECO:0000250|UniProtKB:Q15911}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15911}. Cytoplasm {ECO:0000250|UniProtKB:Q15911}. Note=Translocates from the cytoplasm to the nucleus following TGF-beta stimulation. Expressed in nuclear body (NB)-like dots in the nucleus some of which overlap or closely associate with PML body. {ECO:0000250|UniProtKB:Q15911}. SUBUNIT: Interacts with ALKBH4 and PIAS3 (By similarity). Interacts with FNBP3. Interacts with ESR1, RUNX3, TRIM25, SMAD2 and SMAD3 (By similarity). {ECO:0000250|UniProtKB:Q15911, ECO:0000269|PubMed:9171351}. TISSUE SPECIFICITY: Expressed in suprachiasmatic nucleus (SCN) of the brain (at protein level). Expressed in skeletal muscle. Levels of expression are high in myoblasts but low in differentiated muscle. {ECO:0000269|PubMed:11312261, ECO:0000269|PubMed:26232227}. +Q9CWU2 ZDH13_MOUSE Palmitoyltransferase ZDHHC13 (EC 2.3.1.225) (Huntingtin-interacting protein 14-related protein) (HIP14-related protein) (Zinc finger DHHC domain-containing protein 13) (DHHC-13) 622 70,890 Active site (1); Chain (1); Compositional bias (1); Domain (1); Modified residue (1); Repeat (7); Sequence conflict (1); Transmembrane (6) TRANSMEM 292 312 Helical. {ECO:0000255}.; TRANSMEM 321 341 Helical. {ECO:0000255}.; TRANSMEM 348 368 Helical. {ECO:0000255}.; TRANSMEM 372 392 Helical. {ECO:0000255}.; TRANSMEM 471 491 Helical. {ECO:0000255}.; TRANSMEM 519 539 Helical. {ECO:0000255}. FUNCTION: Palmitoyltransferase for HTT and GAD2 (PubMed:19299482). May play a role in Mg(2+) transport (PubMed:18794299). {ECO:0000269|PubMed:18794299, ECO:0000269|PubMed:19299482}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:18794299, ECO:0000269|PubMed:19299482, ECO:0000269|PubMed:25253725}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:18794299}; Multi-pass membrane protein {ECO:0000255}. Note=Low extracellular Mg(2+) induces increase in Golgi and in post-Golgi vesicles. {ECO:0000269|PubMed:18794299}. SUBUNIT: Interacts (via ANK repeats) with CLIP3 (PubMed:26198635). Interacts (via ANK repeats) with DNAJC5 (via C-terminus) (PubMed:25253725, PubMed:26198635). Interacts (via ANK repeats) with HTT (PubMed:26198635). Interacts (via ANK repeats) with MAP6 (PubMed:26198635). Interacts (via ANK repeats) with SNAP23 (PubMed:26198635). Interacts (via ANK repeats) with SNAP25 (PubMed:25253725, PubMed:26198635). May interact (via ANK repeats) with SPRED2 (PubMed:28882895). {ECO:0000269|PubMed:25253725, ECO:0000269|PubMed:26198635, ECO:0000269|PubMed:28882895}. DOMAIN: The DHHC domain is required for palmitoyltransferase activity. {ECO:0000250|UniProtKB:Q8IUH5}. +Q80U44 ZFY16_MOUSE Zinc finger FYVE domain-containing protein 16 (Endofin) (Endosomal-associated FYVE domain protein) 1528 166,670 Chain (1); Erroneous initiation (1); Modified residue (5); Sequence conflict (1); Zinc finger (1) FUNCTION: May be involved in regulating membrane trafficking in the endosomal pathway. Overexpression induces endosome aggregation. Required to target TOM1 to endosomes (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Early endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Localized to early endosomes. Membrane-associated, probably via its association with phosphatidylinositol 3-phosphate (PI3P) (By similarity). {ECO:0000250}. SUBUNIT: Interacts with the C-terminus of TOM1. Does not interact with TOM1L1 or TOM1L2 (By similarity). {ECO:0000250}. DOMAIN: The FYVE-type zinc finger is necessary and sufficient for its localization into early endosomes and mediates the association with PI3P. {ECO:0000250}. +Q8VD24 ZCC18_MOUSE Zinc finger CCHC domain-containing protein 18 393 43,975 Chain (1); Sequence conflict (1); Zinc finger (1) +Q8BFR1 ZCCHL_MOUSE Zinc finger CCCH-type antiviral protein 1-like 296 32,831 Alternative sequence (1); Chain (1); Initiator methionine (1); Modified residue (1); Zinc finger (2) +Q9CX48 ZCH10_MOUSE Zinc finger CCHC domain-containing protein 10 178 19,148 Chain (1); Compositional bias (3); Zinc finger (1) +O88466 ZN106_MOUSE Zinc finger protein 106 (Zfp-106) (H3a minor histocompatibility antigen) (Son of insulin receptor mutant) (Zinc finger protein 474) 1888 208,964 Alternative sequence (4); Chain (1); Cross-link (34); Erroneous initiation (1); Frameshift (1); Modified residue (19); Natural variant (19); Repeat (6); Sequence conflict (3); Zinc finger (3) FUNCTION: RNA-binding protein (PubMed:27418600, PubMed:28072389). Specifically binds to 5'-GGGGCC-3' sequence repeats in RNA (PubMed:28072389). Essential for maintenance of peripheral motor neuron and skeletal muscle function (PubMed:26604141, PubMed:27418600, PubMed:28072389). Required for normal expression and/or alternative splicing of a number of genes in spinal cord and skeletal muscle, including the neurite outgrowth inhibitor RTN4 (PubMed:26604141, PubMed:27418600). Also contributes to normal mitochondrial respiratory function in motor neurons, via an unknown mechanism (PubMed:26604141). {ECO:0000269|PubMed:26604141, ECO:0000269|PubMed:27418600, ECO:0000269|PubMed:28072389}. PTM: Phosphorylated by FYN in vitro. {ECO:0000269|PubMed:9507006}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:15833274, ECO:0000269|PubMed:27418600, ECO:0000269|PubMed:28072389, ECO:0000269|PubMed:9507006}. Nucleus speckle {ECO:0000269|PubMed:27418600, ECO:0000269|PubMed:28072389}. Note=Colocalizes with RBM39 in nuclear speckles. Inhibition of RNA synthesis, or overexpression of KNOP1, induces translocation from nuclear speckles to the nucleolus. {ECO:0000269|PubMed:27418600}. SUBUNIT: Interacts with KNOP1 (PubMed:15833274). Interacts with TARDBP and NUP107 (PubMed:28072389). Interacts (via N-terminus) with RBM39 (PubMed:27418600). Interacts with the SH3 domains of FYN and GRB2 (PubMed:9507006). {ECO:0000269|PubMed:15833274, ECO:0000269|PubMed:27418600, ECO:0000269|PubMed:28072389, ECO:0000269|PubMed:9507006}. TISSUE SPECIFICITY: Widely expressed, with strongest expression in skeletal muscle, heart and brain (at protein level) (PubMed:9507006, PubMed:26604141, PubMed:27418600, PubMed:28072389). Detected in spinal cord motor neurons (PubMed:28072389). {ECO:0000269|PubMed:26604141, ECO:0000269|PubMed:27418600, ECO:0000269|PubMed:28072389, ECO:0000269|PubMed:9507006}. +Q9Z2U2 ZN292_MOUSE Zinc finger protein 292 (Zinc finger protein 15) (Zfp-15) 2698 301,048 Alternative sequence (1); Chain (1); Erroneous initiation (3); Modified residue (4); Sequence caution (1); Sequence conflict (20); Zinc finger (15) FUNCTION: May be involved in transcriptional regulation. {ECO:0000305}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: Expressed in postnatal day 1 (P1) pituitary. Also detected in presomatotrophic cell line GHFT1-5. {ECO:0000269|PubMed:10687855}. +Q6V5K9 ZN474_MOUSE Zinc finger protein 474 (Testis-specific zinc finger protein) (TSZFP) 347 38,134 Chain (1); Sequence conflict (1); Zinc finger (1) +Q8BI73 ZN775_MOUSE Zinc finger protein 775 538 60,720 Chain (1); Zinc finger (11) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q8R331 ZNHI1_MOUSE Zinc finger HIT domain-containing protein 1 154 17,504 Chain (1); Coiled coil (1); Compositional bias (1); Modified residue (1); Motif (1); Region (1); Sequence conflict (2); Zinc finger (1) FUNCTION: Seems to play a role in p53-mediated apoptosis induction. Binds to NR1D2 and relieves it of its inhibitory effect on the transcription of APOC3 without affecting its DNA-binding activity (By similarity). {ECO:0000250}. PTM: Phosphorylated on Thr by MAPK11 or MAPK14. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with MAPK11 and MAPK14. Component of the chromatin-remodeling SRCAP complex composed of at least SRCAP, DMAP1, RUVBL1, RUVBL2, ACTL6A, YEATS4, ACTR6 and ZNHIT1. Interacts with NR1D1 and NR2D2 (By similarity). {ECO:0000250}. +Q6P5C7 ZN728_MOUSE Zinc finger protein 728 752 86,422 Chain (1); Domain (1); Zinc finger (23) +Q91V17 ZNRF1_MOUSE E3 ubiquitin-protein ligase ZNRF1 (EC 2.3.2.27) (Nerve injury-induced gene 283 protein) (RING-type E3 ubiquitin transferase ZNRF1) (Zinc/RING finger protein 1) 227 23,843 Chain (1); Initiator methionine (1); Lipidation (1); Modified residue (3); Mutagenesis (2); Region (1); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that mediates the ubiquitination of AKT1 and GLUL, thereby playing a role in neuron cells differentiation. Plays a role in the establishment and maintenance of neuronal transmission and plasticity. Regulates Schwann cells differentiation by mediating ubiquitination of GLUL. Promotes Wallerian degeneration, a neurodegeneration disorder, by mediating 'Lys-48'-linked polyubiquitination and subsequent degradation of AKT1 in axons: degradation of AKT1 prevents AKT1-mediated phosphorylation of GSK3B, leading to GSK3B activation and phosphorylation of DPYSL2/CRMP2 followed by destabilization of microtubule assembly in axons. {ECO:0000269|PubMed:20107048, ECO:0000269|PubMed:22057101}. SUBCELLULAR LOCATION: Endosome. Lysosome. Membrane; Peripheral membrane protein. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=Associated with synaptic vesicle membranes in neurons. SUBUNIT: Interacts with AKT1, GLUL and TUBB2A. {ECO:0000269|PubMed:19737534, ECO:0000269|PubMed:20107048, ECO:0000269|PubMed:22057101}. DOMAIN: The RING-type zinc finger domain is required for E3 ligase activity. {ECO:0000250}. +Q7TMA2 ZN503_MOUSE Zinc finger protein 503 (Zinc finger protein Nolz-1) 652 63,036 Alternative sequence (3); Chain (1); Compositional bias (3); Modified residue (5); Zinc finger (1) FUNCTION: May function as a transcriptional repressor. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +Q8BI69 ZN784_MOUSE Zinc finger protein 784 297 32,230 Chain (1); Compositional bias (1); Modified residue (1); Zinc finger (6) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q9ERR8 ZN319_MOUSE Zinc finger protein 319 581 65,644 Chain (1); Cross-link (1); Modified residue (1); Zinc finger (16) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +I7HJS4 ZN683_MOUSE Tissue-resident T-cell transcription regulator protein ZNF683 (Homolog of Blimp-1 in T-cell) (Hobit) (Zinc finger protein 683) 458 50,419 Chain (1); Zinc finger (3) FUNCTION: Transcription factor that mediates a transcriptional program in various innate and adaptive immune tissue-resident lymphocyte T-cell types such as tissue-resident memory T (Trm), natural killer (trNK) and natural killer T (NKT) cells and negatively regulates gene expression of proteins that promote the egress of tissue-resident T-cell populations from non-lymphoid organs (PubMed:22885984, PubMed:27102484). Plays a role in the development, retention and long-term establishment of adaptive and innate tissue-resident lymphocyte T-cell types in non-lymphoid organs, such as the skin and gut, but also in other nonbarrier tissues like liver and kidney, and therefore may provide immediate immunological protection against reactivating infections or viral reinfection (PubMed:22885984, PubMed:27102484). Plays also a role in the differentiation of both thymic and peripheral NKT cells (PubMed:22885984). Negatively regulates the accumulation of interferon-gamma (IFN-gamma) in NKT cells at steady state or after antigenic stimulation (PubMed:22885984). Positively regulates granzyme B production in NKT cells after innate stimulation (PubMed:22885984). Associates with the transcriptional repressor PRDM1/BLIMP1 to chromatin at gene promoter regions (PubMed:27102484). {ECO:0000269|PubMed:22885984, ECO:0000269|PubMed:27102484}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: Expressed in tissue-resident memory T (Trm) cell population in non-lymphoid organs, such as skin and gut (PubMed:27102484). Expressed in innate lymphocytes, including tissue-resident natural killer (trNK) and natural killer T (NKT) cells in thymus, spleen and liver (PubMed:22885984, PubMed:27102484). {ECO:0000269|PubMed:22885984, ECO:0000269|PubMed:27102484}. +Q7TSI0 ZNF12_MOUSE Zinc finger protein 12 686 78,617 Alternative sequence (1); Chain (1); Cross-link (9); Domain (1); Zinc finger (15) FUNCTION: Transcriptional repressor which suppresses activation protein 1 (AP-1)- and serum response element (SRE)-mediated transcriptional activity. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +Q62005 ZP1_MOUSE Zona pellucida sperm-binding protein 1 (Zona pellucida glycoprotein 1) (Zp-1) [Cleaved into: Processed zona pellucida sperm-binding protein 1] 623 68,723 Chain (2); Disulfide bond (4); Domain (2); Glycosylation (6); Modified residue (1); Propeptide (1); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 591 611 Helical. {ECO:0000255}. TOPO_DOM 21 590 Extracellular. {ECO:0000255}.; TOPO_DOM 612 623 Cytoplasmic. {ECO:0000255}. FUNCTION: The mammalian zona pellucida, which mediates species-specific sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy, is composed of three to four glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP1 ensures the structural integrity of the zona pellucida. PTM: Proteolytically cleaved before the transmembrane segment to yield the secreted ectodomain incorporated in the zona pellucida.; PTM: O-glycosylated. {ECO:0000269|PubMed:12799386}. SUBCELLULAR LOCATION: Processed zona pellucida sperm-binding protein 1: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:I6M4H4}. Note=The glycoproteinaceous translucent extracellular matrix that surrounds the mammalian oocyte is called zona pellucida. {ECO:0000305}.; SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P48829}; Single-pass type I membrane protein {ECO:0000255}. SUBUNIT: Polymers of ZP2 and ZP3 organized into long filaments cross-linked by ZP1 homodimers. Interacts with ZP3. {ECO:0000250|UniProtKB:P20239, ECO:0000250|UniProtKB:P60852}. DOMAIN: The ZP domain is involved in the polymerization of the ZP proteins to form the zona pellucida. TISSUE SPECIFICITY: Oocytes. {ECO:0000269|PubMed:7635043}. +Q8CJ78 ZN628_MOUSE Zinc finger protein 628 (Zinc finger protein expressed in embryonal cells and certain adult organs) 1038 109,047 Alternative sequence (2); Chain (1); Compositional bias (2); Erroneous initiation (3); Modified residue (2); Region (1); Repeat (4); Zinc finger (16) FUNCTION: Transcription activator. Binds DNA on GT-box consensus sequence 5'-TTGGTT-3'. {ECO:0000269|PubMed:15556296}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15556296}. TISSUE SPECIFICITY: Expressed in the testis, liver and kidney, Expressed in D3 embryonic stem cells and F9 embryonal carcinoma cells. {ECO:0000269|PubMed:15556296}. +Q60736 ZP3R_MOUSE Zona pellucida sperm-binding protein 3 receptor (Sperm fertilization protein 56) (sp56) 579 64,950 Chain (1); Disulfide bond (14); Domain (7); Glycosylation (13); Signal peptide (1) FUNCTION: Binds to ZP3 glycoprotein in egg zona pellucida. Probably involved in interactions between sperm acrosome and egg zona pellucida during and immediately following the acrosome reaction. {ECO:0000269|PubMed:7604284, ECO:0000303|PubMed:11133656}. PTM: Glycosylated. {ECO:0000269|PubMed:11133656}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome lumen {ECO:0000269|PubMed:11133656}. Note=Sperm acrosomal matrix. SUBUNIT: Homomultimer; disulfide-linked. {ECO:0000269|PubMed:8188752}. TISSUE SPECIFICITY: Testis-specific. Not expressed in heart, liver, abdominal muscle, lung, brain or kidney. {ECO:0000269|PubMed:7604284}. +Q6GQR8 ZN329_MOUSE Zinc finger protein 329 522 59,832 Chain (1); Frameshift (1); Modified residue (1); Sequence conflict (1); Zinc finger (12) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q61464 ZN638_MOUSE Zinc finger protein 638 (Nuclear protein 220) (Zinc finger matrin-like protein) 1960 218,134 Alternative sequence (8); Chain (1); Compositional bias (2); Cross-link (3); Domain (2); Modified residue (18); Region (1); Sequence conflict (1); Zinc finger (1) FUNCTION: Early regulator of adipogenesis that works as a transcription cofactor of CEBPs, controlling the expression of PPARG and probably of other proadipogenic genes, such as SREBF1 (PubMed:21602272). Binds to cytidine clusters in double-stranded DNA (By similarity). May also regulate alternative splicing of target genes during adipogenesis (PubMed:25024404). {ECO:0000250|UniProtKB:Q14966, ECO:0000269|PubMed:21602272, ECO:0000269|PubMed:25024404}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000255|PROSITE-ProRule:PRU00130, ECO:0000269|PubMed:21602272, ECO:0000269|PubMed:25024404}. SUBUNIT: Interacts with FHL2 (By similarity). Interacts with CEBPA, CEBPD and CEBPG. {ECO:0000250|UniProtKB:Q14966, ECO:0000269|PubMed:21602272}. DOMAIN: The matrin-type zinc finger domain is required for localization to nuclear speckles. {ECO:0000269|PubMed:25024404}. +Q922H9 ZN330_MOUSE Zinc finger protein 330 (Nucleolar autoantigen 36) (Nucleolar cysteine-rich protein) 316 35,608 Alternative sequence (1); Chain (1); Compositional bias (1); Modified residue (1); Motif (1); Zinc finger (4) SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Chromosome, centromere {ECO:0000250}. Note=Predominantly expressed in nucleolus. In mitosis associated with centromeres and concentrated at the midbody in cytokinesis (By similarity). {ECO:0000250}. +O35149 ZNT4_MOUSE Zinc transporter 4 (ZnT-4) (Lethal milk protein) (Solute carrier family 30 member 4) 430 47,800 Chain (1); Compositional bias (2); Modified residue (1); Sequence conflict (1); Topological domain (7); Transmembrane (6) TRANSMEM 114 134 Helical. {ECO:0000255}.; TRANSMEM 144 164 Helical. {ECO:0000255}.; TRANSMEM 179 199 Helical. {ECO:0000255}.; TRANSMEM 217 237 Helical. {ECO:0000255}.; TRANSMEM 276 296 Helical. {ECO:0000255}.; TRANSMEM 312 332 Helical. {ECO:0000255}. TOPO_DOM 1 113 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 135 143 Vacuolar. {ECO:0000255}.; TOPO_DOM 165 178 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 200 216 Vacuolar. {ECO:0000255}.; TOPO_DOM 238 275 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 297 311 Vacuolar. {ECO:0000255}.; TOPO_DOM 333 430 Cytoplasmic. {ECO:0000255}. FUNCTION: Probably involved in zinc transport out of the cytoplasm, may be by sequestration into an intracellular compartment. SUBCELLULAR LOCATION: Endosome membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Late endosome membrane {ECO:0000250|UniProtKB:O14863}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:O14863}; Multi-pass membrane protein {ECO:0000255}. DOMAIN: Contains a histidine-rich region which is a ligand for zinc and an aspartate-rich region which is a potential ligand for zinc. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. Highly expressed in the brain and in mammary epithelial cell lines. DISEASE: Note=Defects in Slc30a4 are the cause of the lethal milk (lm) phenotype. Mice with lm are defective in zinc transport into breast milk, due to a premature translation termination codon at position 297. Only homozygous mutant adults develop dermatitis, skin lesions, and hair loss due to a systemic zinc deficiency. However, neonatal mice (of any genotype) suckled on homozygous mutant female also develop symptoms characteristic of nutritional zinc deficiency, including dermatitis, alopecia and stunted growth. +Q505G8 ZN827_MOUSE Zinc finger protein 827 1078 118,536 Alternative sequence (2); Chain (1); Compositional bias (2); Cross-link (25); Erroneous initiation (1); Zinc finger (9) FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +O54692 ZW10_MOUSE Centromere/kinetochore protein zw10 homolog 779 88,063 Chain (1); Coiled coil (1); Initiator methionine (1); Modified residue (4); Region (2); Sequence conflict (5) FUNCTION: Essential component of the mitotic checkpoint, which prevents cells from prematurely exiting mitosis. Required for the assembly of the dynein-dynactin and MAD1-MAD2 complexes onto kinetochores. Its function related to the spindle assembly machinery is proposed to depend on its association in the mitotic RZZ complex. Involved in regulation of membrane traffic between the Golgi and the endoplasmic reticulum (ER); the function is proposed to depend on its association in the interphase NRZ complex which is believed to play a role in SNARE assembly at the ER (By similarity). {ECO:0000250|UniProtKB:O43264}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O43264}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O43264}; Peripheral membrane protein {ECO:0000250|UniProtKB:O43264}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:O43264}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:O43264}. Note=Dynamic pattern of localization during the cell cycle. In most cells at interphase, present diffusely in the cytoplasm. In prometaphase, associated with the kinetochore. At metaphase, detected both at the kinetochores and, most prominently, at the spindle, particularly at the spindle poles. In very early anaphase, detected on segregating kinetochores. In late anaphase and telophase, accumulates at the spindle midzone. {ECO:0000250|UniProtKB:O43264}. SUBUNIT: Interacts with NBAS and KNTC1/ROD; the interactions are mutually exclusive and indicative for its association in two different vesicle tethering complexes. Component of the RZZ complex composed of KNTC1/ROD, ZW10 and ZWILCH. Component of the NRZ complex composed of NBAS, ZW10 and RINT1/TIP20L; NRZ associates with SNAREs STX18, USE1L, BNIP1/SEC20L and SEC22B (the assembly has been described as syntaxin 18 complex). Interacts directly with RINT1/TIP20L bound to BNIP1/SEC20L. Interacts with C19orf25 and ZWINT STOPPED Associated with a SNARE complex consisting of STX18, USE1L, BNIP1/SEC20L, and SEC22B through direct interaction with RINT1/TIP20L bound to BNIP1/SEC20L. Component of the RZZ complex composed of KNTC1/ROD, ZW10 and ZWILCH. Interacts with C19orf25, KNTC1 and ZWINT. {ECO:0000250|UniProtKB:O43264}. +Q80TC6 ZSWM5_MOUSE Zinc finger SWIM domain-containing protein 5 1188 130,927 Chain (1); Zinc finger (1) +Q9CWQ2 ZSWM7_MOUSE Zinc finger SWIM domain-containing protein 7 (SWIM domain-containing and Srs2-interacting protein 1 homolog) 152 16,658 Chain (1); Zinc finger (1) FUNCTION: Involved in early stages of the homologous recombination repair (HRR) pathway of double-stranded DNA breaks arising during DNA replication or induced by DNA-damaging agents. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with RAD51D and XRCC3; involved in homologous recombination repair. Interacts with SWSAP1; they form a functional complex involved in homologous recombination repair and stabilize each other (By similarity). {ECO:0000250}. +Q6DI92 ZSWM9_MOUSE Uncharacterized protein ZSWIM9 447 50,467 Alternative sequence (6); Chain (1); Frameshift (3) +Q6X786 ZPBP2_MOUSE Zona pellucida-binding protein 2 326 37,116 Alternative sequence (2); Chain (1); Glycosylation (3); Sequence conflict (3); Signal peptide (1) FUNCTION: Is implicated in sperm-oocyte interaction during fertilization. {ECO:0000269|PubMed:17664285}. PTM: N-glycosylated. {ECO:0000269|PubMed:17664285}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:17664285}. Secreted {ECO:0000250}. Note=Released after the acrosomal reaction. {ECO:0000269|PubMed:17664285}. TISSUE SPECIFICITY: Expressed specifically in male germ cells. {ECO:0000269|PubMed:17664285}. +Q8R121 ZPI_MOUSE Protein Z-dependent protease inhibitor (PZ-dependent protease inhibitor) (PZI) (Serpin A10) 448 51,797 Alternative sequence (1); Beta strand (15); Chain (1); Glycosylation (4); Helix (14); Mutagenesis (6); Region (1); Signal peptide (1); Site (3); Turn (5) FUNCTION: Inhibits activity of the coagulation protease factor Xa in the presence of PROZ, calcium and phospholipids. Also inhibits factor XIa in the absence of cofactors (By similarity). {ECO:0000250}. PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000250|UniProtKB:Q9UK55}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. TISSUE SPECIFICITY: Detectable in liver, but not in heart, brain, spleen, lung, kidney, skeletal muscle or testes. {ECO:0000269|PubMed:11372680}. +Q3V0C1 ZMAT1_MOUSE Zinc finger matrin-type protein 1 714 84,176 Alternative sequence (2); Chain (1); Compositional bias (2); Erroneous gene model prediction (1); Frameshift (1); Sequence conflict (3); Zinc finger (2) SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q8C6P8 ZFP57_MOUSE Zinc finger protein 57 (Zfp-57) 421 47,959 Alternative sequence (1); Beta strand (2); Chain (1); Compositional bias (1); Domain (1); Helix (3); Sequence caution (1); Sequence conflict (1); Site (1); Turn (2); Zinc finger (5) FUNCTION: Transcription regulator required to maintain maternal and paternal gene imprinting, a process by which gene expression is restricted in a parent of origin-specific manner by epigenetic modification of genomic DNA and chromatin, including DNA methylation. Acts by controlling DNA methylation during the earliest multicellular stages of development at multiple imprinting control regions. Required for the establishment of maternal methylation imprints at SNRPN locus. Acts as a transcriptional repressor in Schwann cells. Binds to a 5'-TGCCGC-3' consensus sequence and recognizes the methylated CpG within this element. {ECO:0000269|PubMed:15070898, ECO:0000269|PubMed:18854139, ECO:0000269|PubMed:23059534}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15070898, ECO:0000269|PubMed:18854139, ECO:0000269|PubMed:8120052}. Note=Binds various differentially methylated regions (DMR), including the Snrpn DMR. DOMAIN: The KRAB domain is required for function as transcriptional repressor.; DOMAIN: Zinc fingers 2 and 3 mediate recognition of the target element, ZF2 interacting with the 5' half (TGC) and ZF3 interacting with the 3' half (CGC). TISSUE SPECIFICITY: Expressed in oocytes and in a subset of adult tissues. Expressed at high levels in testis, and at low levels in cerebellum. Present in sciatic nerve and spinal cord (at protein level). {ECO:0000269|PubMed:15070898, ECO:0000269|PubMed:8120052}. +Q91ZR3 ZHANG_MOUSE CREB/ATF bZIP transcription factor (Host cell factor-binding transcription factor Zhangfei) (HCF-binding transcription factor Zhangfei) (Tyrosine kinase-associated leucine zipper protein LAZip) 358 37,825 Chain (1); Domain (1); Erroneous initiation (1); Modified residue (1); Motif (1); Region (2); Sequence caution (1) FUNCTION: Strongly activates transcription when bound to HCFC1. Suppresses the expression of HSV proteins in cells infected with the virus in a HCFC1-dependent manner. Also suppresses the HCFC1-dependent transcriptional activation by CREB3 and reduces the amount of CREB3 in the cell. Able to down-regulate expression of some cellular genes in CREBZF-expressing cells (By similarity). {ECO:0000250|UniProtKB:Q9NS37}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NS37}. Note=Colocalizes in promyelocytic leukemia protein nuclear bodies (PML-NB) with CREB3 and HCFC1. {ECO:0000250|UniProtKB:Q9NS37}. SUBUNIT: Interacts with HCFC1; the interaction inhibits CREB3 transcriptional activity. Interacts with CREB3; the interaction occurs only in combination with HCFC1. {ECO:0000250|UniProtKB:Q9NS37}. +Q5Y5T3 ZDH23_MOUSE Palmitoyltransferase ZDHHC23 (EC 2.3.1.225) (DHHC-containing protein 11) (Zinc finger DHHC domain-containing protein 23) (DHHC-23) (zDHHC23) 425 48,150 Chain (1); Domain (1); Erroneous initiation (1); Region (1); Sequence conflict (1); Transmembrane (6) TRANSMEM 82 99 Helical. {ECO:0000255}.; TRANSMEM 103 125 Helical. {ECO:0000255}.; TRANSMEM 131 151 Helical. {ECO:0000255}.; TRANSMEM 160 180 Helical. {ECO:0000255}.; TRANSMEM 293 313 Helical. {ECO:0000255}.; TRANSMEM 344 364 Helical. {ECO:0000255}. FUNCTION: Palmitoyltransferase that mediates palmitoylation of KCNMA1, regulating localization of KCNMA1 to the plasma membrane. May be involved in NOS1 regulation and targeting to the synaptic membrane (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Interacts with NOS1. {ECO:0000250}. DOMAIN: The DHHC domain is required for palmitoyltransferase activity. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the brain. {ECO:0000269|PubMed:15603741}. +A2A761 ZFP69_MOUSE Zinc finger protein 69 (Zinc finger protein 642) 587 65,725 Chain (1); Domain (1); Zinc finger (9) FUNCTION: Putative transcription factor that appears to regulate lipid metabolism. {ECO:0000269|PubMed:19578398, ECO:0000269|PubMed:26232096}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26232096}. +Q6ZPY5 ZN507_MOUSE Zinc finger protein 507 941 102,884 Chain (1); Erroneous initiation (1); Modified residue (2); Sequence conflict (2); Zinc finger (9) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q6A085 ZN629_MOUSE Zinc finger protein 629 867 96,033 Chain (1); Cross-link (4); Erroneous initiation (1); Modified residue (1); Sequence conflict (3); Zinc finger (19) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q6P0X2 ZN511_MOUSE Zinc finger protein 511 227 25,761 Alternative sequence (1); Chain (1); Modified residue (1); Zinc finger (3) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +O88291 ZN326_MOUSE DBIRD complex subunit ZNF326 (Zinc finger protein 326) (Zinc finger protein interacting with mRNPs) (Zinc finger protein-associated with nuclear matrix of 75 kDa) 580 65,225 Alternative sequence (3); Chain (1); Compositional bias (2); Cross-link (8); Modified residue (17); Motif (1); Region (1); Sequence caution (1); Sequence conflict (3); Zinc finger (2) FUNCTION: Core component of the DBIRD complex, a multiprotein complex that acts at the interface between core mRNP particles and RNA polymerase II (RNAPII) and integrates transcript elongation with the regulation of alternative splicing: the DBIRD complex affects local transcript elongation rates and alternative splicing of a large set of exons embedded in (A + T)-rich DNA regions (By similarity). May also play a role in neuronal differentiation. Able to bind DNA and activate expression in vitro. {ECO:0000250, ECO:0000269|PubMed:10798446}. SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000269|PubMed:10798446, ECO:0000269|PubMed:9809746}. SUBUNIT: Component of the DBIRD complex. Interacts with CCAR2; the interaction is direct (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed in adult tissues. Highly expressed in neuronal tissues such as brain and neural tube. {ECO:0000269|PubMed:10798446, ECO:0000269|PubMed:9809746}. +Q3ZK22 VEZA_MOUSE Vezatin 780 87,987 Alternative sequence (7); Chain (1); Coiled coil (1); Compositional bias (3); Sequence conflict (12); Transmembrane (2) TRANSMEM 140 160 Helical. {ECO:0000255}.; TRANSMEM 162 182 Helical. {ECO:0000255}. FUNCTION: Plays a pivotal role in the establishment of adherens junctions and their maintenance in adult life. Required for morphogenesis of the preimplantation embryo, and for the implantation process. {ECO:0000269|PubMed:16199027, ECO:0000269|PubMed:17452094}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16199027}; Multi-pass membrane protein {ECO:0000305}. Cell projection, stereocilium membrane {ECO:0000269|PubMed:17567809}. Cell junction, adherens junction {ECO:0000269|PubMed:16199027}. Nucleus {ECO:0000269|PubMed:16199027}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:17379651}. SUBUNIT: Interacts with USH2A (via the cytoplasmic region); the interaction associates VEZT with the USH2 complex at the stereocilia base (PubMed:17567809). Interacts with myosin MYO7A and the cadherin-catenins complex (By similarity). {ECO:0000250|UniProtKB:Q9HBM0, ECO:0000269|PubMed:17567809}. TISSUE SPECIFICITY: Expressed in developing cochlear hair cells (PubMed:17567809). Isoform 1, isoform 2 and isoform 3 are expressed in testis. In the seminiferous epithelium, present exclusively in the acrosome of spermatids (at protein level). {ECO:0000269|PubMed:17379651, ECO:0000269|PubMed:17567809}. +O35633 VIAAT_MOUSE Vesicular inhibitory amino acid transporter (GABA and glycine transporter) (Solute carrier family 32 member 1) (Vesicular GABA transporter) (mVGAT) (mVIAAT) 525 57,381 Alternative sequence (1); Chain (1); Glycosylation (1); Modified residue (1); Sequence conflict (1); Topological domain (11); Transmembrane (10) TRANSMEM 134 154 Helical. {ECO:0000255}.; TRANSMEM 205 225 Helical. {ECO:0000255}.; TRANSMEM 243 263 Helical. {ECO:0000255}.; TRANSMEM 266 286 Helical. {ECO:0000255}.; TRANSMEM 306 326 Helical. {ECO:0000255}.; TRANSMEM 342 362 Helical. {ECO:0000255}.; TRANSMEM 385 405 Helical. {ECO:0000255}.; TRANSMEM 439 459 Helical. {ECO:0000255}.; TRANSMEM 462 482 Helical. {ECO:0000255}.; TRANSMEM 490 510 Helical. {ECO:0000255}. TOPO_DOM 1 133 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 155 204 Lumenal, vesicle. {ECO:0000255}.; TOPO_DOM 226 242 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 264 265 Lumenal, vesicle. {ECO:0000255}.; TOPO_DOM 287 305 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 327 341 Lumenal, vesicle. {ECO:0000255}.; TOPO_DOM 363 384 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 406 438 Lumenal, vesicle. {ECO:0000255}.; TOPO_DOM 460 461 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 483 489 Lumenal, vesicle. {ECO:0000255}.; TOPO_DOM 511 525 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in the uptake of GABA and glycine into the synaptic vesicles. {ECO:0000250|UniProtKB:O35458, ECO:0000269|PubMed:9395291}. SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:O35458}; Multi-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Brain and retina. Localized in horizontal cell tips at both rod and cone terminals. {ECO:0000269|PubMed:12115694}. +Q8VDJ3 VIGLN_MOUSE Vigilin (High density lipoprotein-binding protein) (HDL-binding protein) 1268 141,743 Chain (1); Domain (14); Initiator methionine (1); Modified residue (12) FUNCTION: Appears to play a role in cell sterol metabolism. It may function to protect cells from over-accumulation of cholesterol (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. +Q3TXX4 VGLU1_MOUSE Vesicular glutamate transporter 1 (VGluT1) (Brain-specific Na(+)-dependent inorganic phosphate cotransporter) (Solute carrier family 17 member 7) 560 61,637 Chain (1); Compositional bias (1); Modified residue (1); Sequence conflict (1); Topological domain (13); Transmembrane (12) TRANSMEM 64 84 Helical. {ECO:0000255}.; TRANSMEM 117 137 Helical. {ECO:0000255}.; TRANSMEM 141 161 Helical. {ECO:0000255}.; TRANSMEM 170 190 Helical. {ECO:0000255}.; TRANSMEM 209 229 Helical. {ECO:0000255}.; TRANSMEM 237 257 Helical. {ECO:0000255}.; TRANSMEM 303 323 Helical. {ECO:0000255}.; TRANSMEM 342 362 Helical. {ECO:0000255}.; TRANSMEM 379 399 Helical. {ECO:0000255}.; TRANSMEM 402 422 Helical. {ECO:0000255}.; TRANSMEM 436 456 Helical. {ECO:0000255}.; TRANSMEM 470 490 Helical. {ECO:0000255}. TOPO_DOM 1 63 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 85 116 Extracellular. {ECO:0000255}.; TOPO_DOM 138 140 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 162 169 Extracellular. {ECO:0000255}.; TOPO_DOM 191 208 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 230 236 Extracellular. {ECO:0000255}.; TOPO_DOM 258 302 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 324 341 Extracellular. {ECO:0000255}.; TOPO_DOM 363 378 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 400 401 Extracellular. {ECO:0000255}.; TOPO_DOM 423 435 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 457 469 Extracellular. {ECO:0000255}.; TOPO_DOM 491 560 Cytoplasmic. {ECO:0000255}. FUNCTION: Mediates the uptake of glutamate into synaptic vesicles at presynaptic nerve terminals of excitatory neural cells. May also mediate the transport of inorganic phosphate. {ECO:0000269|PubMed:15103023, ECO:0000269|PubMed:15118123, ECO:0000269|PubMed:17611277}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:16942593}. Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cell junction, synapse, synaptosome {ECO:0000269|PubMed:16595674}. SUBUNIT: Interacts with SHANK3. {ECO:0000269|PubMed:24153177}. TISSUE SPECIFICITY: Expressed in hippocampus (at protein level). Expressed in the molecular layer of the cerebellum and in retina. {ECO:0000269|PubMed:15103023, ECO:0000269|PubMed:16595674, ECO:0000269|PubMed:17611277, ECO:0000269|PubMed:24153177}. +Q9EQ48 VN1A8_MOUSE Vomeronasal type-1 receptor A8 279 31,564 Chain (1); Disulfide bond (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 20 40 Helical; Name=1. {ECO:0000255}.; TRANSMEM 50 70 Helical; Name=2. {ECO:0000255}.; TRANSMEM 94 114 Helical; Name=3. {ECO:0000255}.; TRANSMEM 135 155 Helical; Name=4. {ECO:0000255}.; TRANSMEM 160 180 Helical; Name=5. {ECO:0000255}.; TRANSMEM 188 208 Helical; Name=6. {ECO:0000255}.; TRANSMEM 239 259 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 19 Extracellular. {ECO:0000255}.; TOPO_DOM 41 49 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 71 93 Extracellular. {ECO:0000255}.; TOPO_DOM 115 134 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 156 159 Extracellular. {ECO:0000255}.; TOPO_DOM 181 187 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 209 238 Extracellular. {ECO:0000255}.; TOPO_DOM 260 279 Cytoplasmic. {ECO:0000255}. FUNCTION: Putative pheromone receptor implicated in the regulation of social and reproductive behavior. {ECO:0000269|PubMed:12214233}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Expressed in a subset of sensory neurons located in the apical layer of the vomeronasal organ. {ECO:0000269|PubMed:11802169}. +Q80TY5 VP13B_MOUSE Vacuolar protein sorting-associated protein 13B (Cohen syndrome protein 1 homolog) 3993 444,015 Chain (1); Modified residue (5); Sequence conflict (1) FUNCTION: May be involved in protein sorting in post Golgi membrane traffic. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed in all examined tissues. {ECO:0000269|PubMed:19006247}. +Q8BX70 VP13C_MOUSE Vacuolar protein sorting-associated protein 13C 3748 420,089 Alternative sequence (3); Chain (1); Compositional bias (1); Erroneous initiation (2); Frameshift (1); Modified residue (14); Sequence conflict (3) FUNCTION: Necessary for proper mitochondrial function and maintenance of mitochondrial transmembrane potential. Involved in the regulation of PINK1/PRKN-mediated mitophagy in response to mitochondrial depolarization. {ECO:0000250|UniProtKB:Q709C8}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q709C8}. +Q9D2N9 VP33A_MOUSE Vacuolar protein sorting-associated protein 33A 598 67,555 Chain (1); Natural variant (1); Sequence conflict (1) FUNCTION: Plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport and autophagic pathways. Believed to act as a core component of the putative HOPS and CORVET endosomal tethering complexes which are proposed to be involved in the Rab5-to-Rab7 endosome conversion probably implicating MON1A/B, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion. The HOPS complex is proposed to be recruited to Rab7 on the late endosomal membrane and to regulate late endocytic, phagocytic and autophagic traffic towards lysosomes. The CORVET complex is proposed to function as a Rab5 effector to mediate early endosome fusion probably in specific endosome subpopulations. Required for fusion of endosomes and autophagosomes with lysosomes; the function is dependent on its association with VPS16 but not VIPAS39. The function in autophagosome-lysosome fusion implicates STX17 but not UVRAG. {ECO:0000250|UniProtKB:Q96AX1}. SUBCELLULAR LOCATION: Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q63615}. Late endosome membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Lysosome membrane {ECO:0000269|PubMed:27628032}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Early endosome {ECO:0000305}. Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:27628032}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000305}. SUBUNIT: Core component of at least two putative endosomal tethering complexes, the homotypic fusion and vacuole protein sorting (HOPS) complex and the class C core vacuole/endosome tethering (CORVET) complex. Their common core is composed of the class C Vps proteins VPS11, VPS16, VPS18 and VPS33A, which in HOPS further associates with VPS39 and VPS41 and in CORVET with VPS8 and TGFBRAP1 (PubMed:25266290). Interacts with RAB5C (PubMed:25266290). Interacts with UVRAG, STX17, MON1A and MON1B (By similarity). Associates with adaptor protein complex 3 (AP-3) and clathrin (By similarity). {ECO:0000250|UniProtKB:Q63615, ECO:0000250|UniProtKB:Q96AX1, ECO:0000269|PubMed:25266290, ECO:0000305|PubMed:25266290}. DISEASE: Note=Defects in Vps33a are the cause of the buff mutant which exhibits hypopigmentation in the coat and eyes, due to reduced size and number of melanosomes in their cells. In addition, mice are prone to prolonged bleeding, due to a platelet-storage pool defect. +P59016 VP33B_MOUSE Vacuolar protein sorting-associated protein 33B 617 70,526 Chain (1); Initiator methionine (1); Modified residue (1); Sequence conflict (2) FUNCTION: May play a role in vesicle-mediated protein trafficking to lysosomal compartments and in membrane docking/fusion reactions of late endosomes/lysosomes. Mediates phagolysosomal fusion in macrophages. Proposed to be involved in endosomal maturation implicating in part VIPAS39 (By similarity). In epithelial cells, the VPS33B:VIPAS39 complex may play a role in the apical RAB11A-dependentrecycling pathway and in the maintenance of the apical-basolateral polarity (PubMed:20190753). Seems to be involved in the sorting of specific cargos from the trans-Golgi network to alpha-granule-destined multivesicular bodies (MVBs) promoting MVBs maturation in megakaryocytes (PubMed:25947942). {ECO:0000250|UniProtKB:Q9H267, ECO:0000269|PubMed:20190753, ECO:0000269|PubMed:25947942}. PTM: Phosphorylated on tyrosine residues. {ECO:0000250}. SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250|UniProtKB:Q9H267}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9H267}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9H267}. Lysosome membrane {ECO:0000250|UniProtKB:Q9H267}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9H267}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9H267}. Early endosome {ECO:0000250|UniProtKB:Q9H267}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:Q9H267}. Recycling endosome {ECO:0000250|UniProtKB:Q9H267}. Note=Colocalizes in clusters with VIPAS39 at cytoplasmic organelles. Colocalizes with RAB11A and VIPAS39 on recycling endosomes. Colocalizes with AP-3, clathrin, Rab5 and Rab7b. {ECO:0000250|UniProtKB:Q9H267}. SUBUNIT: Interacts with RAB11A and VIPAS39 (PubMed:20190753). Associates with adaptor protein complex 3 (AP-3), clathrin:AP-3 and clathrin:HGS complexes (PubMed:21411634). {ECO:0000269|PubMed:20190753, ECO:0000269|PubMed:21411634}. +Q6P3A4 VSIG8_MOUSE V-set and immunoglobulin domain-containing protein 8 417 44,187 Alternative sequence (1); Chain (1); Compositional bias (1); Disulfide bond (2); Domain (2); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 263 283 Helical. {ECO:0000255}. TOPO_DOM 22 262 Extracellular. {ECO:0000255}.; TOPO_DOM 284 417 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q9CR26 VTA1_MOUSE Vacuolar protein sorting-associated protein VTA1 homolog (SKD1-binding protein 1) (SBP1) 309 33,913 Chain (1); Initiator methionine (1); Modified residue (1); Region (3) FUNCTION: Involved in the endosomal multivesicular bodies (MVB) pathway. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. Thought to be a cofactor of VPS4A/B, which catalyzes disassembles membrane-associated ESCRT-III assemblies (By similarity). Involved in the sorting and down-regulation of EGFR. {ECO:0000250, ECO:0000269|PubMed:15173323}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15173323}. Endosome membrane {ECO:0000269|PubMed:15173323}; Peripheral membrane protein {ECO:0000269|PubMed:15173323}. SUBUNIT: Interacts with VPS4B. Interacts with CHMP1B. Interacts with CHMP2A; the interaction probably involves the open conformation of (polymerized) CHMP2A. Interacts with CHMP3. Interacts with CHMP5; the interaction involves soluble CHMP5. Interacts with IST1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. Expressed in brain, liver, kidney, spleen, lung and heart (at protein level). {ECO:0000269|PubMed:15173323}. +Q80X41 VRK1_MOUSE Serine/threonine-protein kinase VRK1 (EC 2.7.11.1) (Serine/threonine-protein kinase 51PK) (Vaccinia-related kinase 1) 440 49,741 Active site (1); Alternative sequence (3); Binding site (1); Chain (1); Cross-link (1); Domain (1); Modified residue (3); Nucleotide binding (1) FUNCTION: Serine/threonine kinase involved in Golgi disassembly during the cell cycle: following phosphorylation by PLK3 during mitosis, required to induce Golgi fragmentation. Acts by mediating phosphorylation of downstream target protein. Phosphorylates 'Thr-18' of p53/TP53 and may thereby prevent the interaction between p53/TP53 and MDM2. Phosphorylates casein and histone H3. Phosphorylates BANF1: disrupts its ability to bind DNA, reduces its binding to LEM domain-containing proteins and causes its relocalization from the nucleus to the cytoplasm. Phosphorylates ATF2 which activates its transcriptional activity (By similarity). {ECO:0000250, ECO:0000269|PubMed:14645249, ECO:0000269|PubMed:9521809}. PTM: Phosphorylation by PLK3 leads to induction of Golgi fragmentation during mitosis (By similarity). Autophosphorylated at various serine and threonine residues. Autophosphorylation does not impair its ability to phosphorylate p53/TP53. {ECO:0000250, ECO:0000269|PubMed:14645249}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Dispersed throughout the cell but not located on mitotic spindle or chromatids during mitosis. TISSUE SPECIFICITY: Highly expressed in testis. Expressed in liver, kidney and muscle. Weakly expressed in thymus, bone marrow and spleen. {ECO:0000269|PubMed:12782311, ECO:0000269|PubMed:9521809}. +Q62481 VPS72_MOUSE Vacuolar protein sorting-associated protein 72 homolog (Protein YL-1) (Transcription factor-like 1) 368 40,784 Chain (1); Compositional bias (4); Cross-link (1); DNA binding (1); Modified residue (2); Sequence conflict (4) FUNCTION: Deposition-and-exchange histone chaperone specific for H2AFZ, specifically chaperones H2AFZ and deposits it into nucleosomes. As component of the SRCAP complex, mediates the ATP-dependent exchange of histone H2AFZ/H2B dimers for nucleosomal H2A/H2B, leading to transcriptional regulation of selected genes by chromatin remodeling. {ECO:0000250|UniProtKB:Q15906}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15906}. SUBUNIT: Component of the NuA4 histone acetyltransferase complex which contains the catalytic subunit KAT5/TIP60 and the subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, YEATS4/GAS41 and VPS72/YL1. Component of a NuA4-related complex which contains EP400, TRRAP/PAF400, SRCAP, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, actin, ACTL6A/BAF53A, VPS72 and YEATS4/GAS41. Also part of a multiprotein complex which contains SRCAP and which binds to H2AFZ/H2AZ. Interacts (via N-terminal domain) with H2AFZ. {ECO:0000250|UniProtKB:Q15906}. TISSUE SPECIFICITY: In all tissues examined, most abundantly in brain and thymus. +A9Z1V5 VW5B1_MOUSE von Willebrand factor A domain-containing protein 5B1 1215 133,972 Chain (1); Compositional bias (2); Domain (2); Glycosylation (1); Modified residue (1); Sequence conflict (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q9JHA8 VWA7_MOUSE von Willebrand factor A domain-containing protein 7 (Protein G7c) 891 95,984 Chain (1); Compositional bias (2); Domain (1); Erroneous gene model prediction (1); Glycosylation (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Expressed at low level in many tissues. {ECO:0000269|PubMed:10803853}. +P21614 VTDB_MOUSE Vitamin D-binding protein (DBP) (VDB) (Gc-globulin) (Group-specific component) 476 53,600 Chain (1); Disulfide bond (14); Domain (3); Glycosylation (1); Modified residue (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Involved in vitamin D transport and storage, scavenging of extracellular G-actin, enhancement of the chemotactic activity of C5 alpha for neutrophils in inflammation and macrophage activation. {ECO:0000250|UniProtKB:P02774}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10052453}. SUBUNIT: Associates with membrane-bound immunoglobulin on the surface of B-lymphocytes and with IgG Fc receptor on the membranes of T-lymphocytes (By similarity). Interacts with LRP2; the interaction is required for renal uptake of GC in complex with 25-hydroxyvitamin D3 (PubMed:10052453). {ECO:0000250|UniProtKB:P02774, ECO:0000269|PubMed:10052453}. +Q8BH57 WDR48_MOUSE WD repeat-containing protein 48 (USP1-associated factor 1) 676 76,007 Alternative sequence (3); Chain (1); Erroneous initiation (1); Modified residue (4); Repeat (8); Sequence conflict (3) FUNCTION: Regulator of deubiquitinating complexes. Acts as a strong activator of USP1 and USP46. Enhances the USP1-mediated deubiquitination of FANCD2; USP1 being almost inactive by itself. Also activates deubiquitinating activity of complexes containing USP12. Activates deubiquitination by increasing the catalytic turnover without increasing the affinity of deubiquitinating enzymes for the substrate. {ECO:0000250|UniProtKB:Q8TAF3}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8TAF3}. Cytoplasm {ECO:0000250|UniProtKB:Q8TAF3}. Lysosome {ECO:0000250|UniProtKB:Q8TAF3}. Late endosome {ECO:0000250|UniProtKB:Q8TAF3}. Note=Mainly in cytoplasmic compartments. {ECO:0000250|UniProtKB:Q8TAF3}. SUBUNIT: Interacts with USP46. Interacts with USP1. Interacts with USP12. Component of the USP12/WDR20/WDR48 deubiquitinating complex. Interacts with PHLPP1. {ECO:0000250|UniProtKB:Q8TAF3}. DOMAIN: The WD repeats are required for the interaction with deubiquitinating enzymes USP1, USP12 and USP46. {ECO:0000250|UniProtKB:Q8TAF3}. +Q9JJA4 WDR12_MOUSE Ribosome biogenesis protein WDR12 (WD repeat-containing protein 12) 423 47,347 Chain (1); Cross-link (1); Initiator methionine (1); Modified residue (2); Region (2); Repeat (7); Sequence conflict (3) FUNCTION: Component of the PeBoW complex, which is required for maturation of 28S and 5.8S ribosomal RNAs and formation of the 60S ribosome. {ECO:0000255|HAMAP-Rule:MF_03029}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000255|HAMAP-Rule:MF_03029}. Nucleus, nucleoplasm {ECO:0000255|HAMAP-Rule:MF_03029}. SUBUNIT: Component of the PeBoW complex, composed of BOP1, PES1 and WDR12. The complex is held together by BOP1, which interacts with PES1 via its N-terminal domain and with WDR12 via a high-affinity interaction between the seven-bladed beta-propeller domains of the 2 proteins. The PeBoW complex associates with the 66S pre-ribosome. Interacts (via UBL domain) with MDN1 (via VWFA/MIDAS domain). {ECO:0000255|HAMAP-Rule:MF_03029}. +Q5U4F6 WDR34_MOUSE WD repeat-containing protein 34 535 57,971 Chain (1); Erroneous initiation (1); Modified residue (1); Repeat (5) FUNCTION: Critical for ciliary functions, essential to normal development and survival, most probably as a previously unrecognized component of the mammalian dynein-motor-based intraflagellar transport (IFT) machinery. Acts as a negative regulator of the Toll-like and IL-1R receptor signaling pathways. Inhibits the MAP3K7-induced NF-kappa-B activation pathway. Inhibits MAP3K7 phosphorylation at 'Thr-184' and 'Thr-187' upon Il-1 beta stimulation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:24183451}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:24183451}. Note=Concentrates around the centrioles and basal bodies also showing axonemal staining. SUBUNIT: Interacts (via WD domains) with MAP3K7 and TAB3. Interacts (via WD domains) with TAB2 (via C-terminus). Interacts (via WD domains) with TRAF6 (via TRAF-type domains) (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain, thymus, heart, lung, liver, spleen, kidney, testis and intestine. {ECO:0000269|PubMed:19521662}. +Q9EP82 WDR4_MOUSE tRNA (guanine-N(7)-)-methyltransferase non-catalytic subunit WDR4 (WD repeat-containing protein 4) 413 45,756 Chain (1); Initiator methionine (1); Modified residue (3); Repeat (5); Sequence conflict (2) tRNA modification; N(7)-methylguanine-tRNA biosynthesis. FUNCTION: Required for the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. In the complex, it is required to stabilize and induce conformational changes of the catalytic subunit. {ECO:0000255|HAMAP-Rule:MF_03056}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03056}. SUBUNIT: Forms a heterodimer with the catalytic subunit METTL1. {ECO:0000255|HAMAP-Rule:MF_03056}. +Q9CWR1 WDR73_MOUSE WD repeat-containing protein 73 371 40,856 Alternative sequence (4); Chain (1); Erroneous initiation (1); Frameshift (1); Repeat (3); Sequence conflict (2) FUNCTION: May play a role in the regulation of microtubule organization and dynamics. {ECO:0000250|UniProtKB:Q6P4I2}. SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q6P4I2}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q6P4I2}. Cleavage furrow {ECO:0000250|UniProtKB:Q6P4I2}. Note=During interphase, located in the cytosol. During mitosis, accumulates at the spindle poles and microtubule asters and later in the cleavage furrow. {ECO:0000250|UniProtKB:Q6P4I2}. +Q3UW55 WFC6A_MOUSE WAP four-disulfide core domain protein 6A (Putative protease inhibitor WAP6A) 136 15,903 Chain (1); Disulfide bond (7); Domain (2); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q7TQN3 WFKN2_MOUSE WAP, Kazal, immunoglobulin, Kunitz and NTR domain-containing protein 2 (Growth and differentiation factor-associated serum protein 1) (GASP-1) (mGASP-1) 571 63,333 Chain (1); Disulfide bond (17); Domain (6); Glycosylation (2); Sequence conflict (1); Signal peptide (1); Site (1) FUNCTION: Protease-inhibitor that contains multiple distinct protease inhibitor domains. Probably has serine protease- and metalloprotease-inhibitor activity (By similarity). Inhibits the biological activity of mature myostatin, but not activin. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12595574}. SUBUNIT: Interacts with both mature and propeptide myostatin/MSTN. {ECO:0000269|PubMed:12595574}. TISSUE SPECIFICITY: Widely expressed, with high expression in skeletal muscle and heart. Also expressed in brain, lung and testis. Weakly expressed in liver and kidney. {ECO:0000269|PubMed:12595574}. +Q5ND34 WDR81_MOUSE WD repeat-containing protein 81 1934 211,945 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (1); Erroneous translation (1); Mutagenesis (1); Region (1); Repeat (5) FUNCTION: Functions as a negative regulator of the PI3 kinase/PI3K activity associated with endosomal membranes via BECN1, a core subunit of the PI3K complex. By modifying the phosphatidylinositol 3-phosphate/PtdInsP3 content of endosomal membranes may regulate endosome fusion, recycling, sorting and early to late endosome transport. It is for instance, required for the delivery of cargos like BST2/tetherin from early to late endosome and thereby participates indirectly to their degradation by the lysosome. May also play a role in aggrephagy, the macroautophagic degradation of ubiquitinated protein aggregates. In this process, may regulate the interaction of SQSTM1 with ubiquitinated proteins and also recruit MAP1LC3C (By similarity). May also be involved in maintenance of normal mitochondrial structure and organization (PubMed:23595742). {ECO:0000250|UniProtKB:Q562E7, ECO:0000269|PubMed:23595742}. SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000250|UniProtKB:Q562E7}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q562E7}. Late endosome membrane {ECO:0000250|UniProtKB:Q562E7}. Lysosome membrane {ECO:0000250|UniProtKB:Q562E7}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:Q562E7}. Mitochondrion {ECO:0000269|PubMed:23595742}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q562E7}. SUBUNIT: Interacts with WDR91; involved in early to late endosome cargo transport. Interacts with BECN1; negatively regulates the PI3 kinase/PI3K activity associated with endosomal membranes. Interacts with SQSTM1; the interaction is direct and regulates the interaction of SQSTM1 with ubiquitinated proteins. Interacts with MAP1LC3C; recruits MAP1LC3C to ubiquitinated protein aggregates in the aggrephagy process. {ECO:0000250|UniProtKB:Q562E7}. TISSUE SPECIFICITY: Expressed in brain, Purkinje cells of cerebellum, retinal photoreceptor cells and spinal cord (at protein level) (PubMed:23595742). In brain, specifically expressed by neuronal cells (at protein level). Detected in a wide range of tissues including intestine, adipose tissue, liver, pancreas, thymus, spleen, kidney, heart, eye, sciatic nerve, and testis (PubMed:21885617, PubMed:23595742, PubMed:28404643). {ECO:0000269|PubMed:21885617, ECO:0000269|PubMed:23595742, ECO:0000269|PubMed:28404643}. +Q9DAU7 WFDC2_MOUSE WAP four-disulfide core domain protein 2 (WAP domain-containing protein HE4) 174 18,032 Chain (1); Disulfide bond (8); Domain (2); Signal peptide (1) FUNCTION: Broad range protease inhibitor. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Homotrimer; disulfide-linked. {ECO:0000250}. +Q66JT0 WEE2_MOUSE Wee1-like protein kinase 2 (EC 2.7.10.2) (Wee1-like protein kinase 1B) (Wee1B kinase) (mWee1B) 555 62,343 Active site (1); Binding site (1); Chain (1); Coiled coil (1); Domain (1); Metal binding (2); Modified residue (2); Motif (2); Mutagenesis (8); Nucleotide binding (1); Sequence conflict (5) FUNCTION: Oocyte-specific protein tyrosine kinase that phosphorylates and inhibits CDK1 and acts as a key regulator of meiosis during both prophase I and metaphase II. Required to maintain meiotic arrest in oocytes during the germinal vesicle (GV) stage, a long period of quiescence at dictyate prophase I, by phosphorylating CDK1 at 'Tyr-15', leading to inhibit CDK1 activity and prevent meiotic reentry. Also required for metaphase II exit during egg activation by phosphorylating CDK1 at 'Tyr-15', to ensure exit from meiosis in oocytes and promote pronuclear formation. {ECO:0000269|PubMed:16169490, ECO:0000269|PubMed:20083600, ECO:0000269|PubMed:21454751}. PTM: Phosphorylated by PKA at Ser-15 in vitro, leading to activate kinase activity. Phosphorylation at Ser-15 by CaMK2, leading to increase its activity and promote metaphase II exit during egg activation. {ECO:0000269|PubMed:16169490, ECO:0000269|PubMed:21454751}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Localizes mainly in the nucleus. Exported from the nucleus to the cytoplasm before germinal vesicle breakdown (GVBD), allowing meiosis resumption. TISSUE SPECIFICITY: Ovary-specific. {ECO:0000269|PubMed:16169490}. +Q80XH4 WSCD1_MOUSE WSC domain-containing protein 1 572 64,981 Alternative sequence (2); Chain (1); Domain (2); Erroneous initiation (1); Glycosylation (2); Sequence conflict (2); Transmembrane (1) TRANSMEM 15 35 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q7TQJ8 WTIP_MOUSE Wilms tumor protein 1-interacting protein (WT1-interacting protein) 398 42,254 Chain (1); Compositional bias (2); Domain (3) FUNCTION: Adapter or scaffold protein which participates in the assembly of numerous protein complexes and is involved in several cellular processes such as cell fate determination, cytoskeletal organization, repression of gene transcription, cell-cell adhesion, cell differentiation, proliferation and migration. Positively regulates microRNA (miRNA)-mediated gene silencing. Negatively regulates Hippo signaling pathway and antagonizes phosphorylation of YAP1. Acts as a transcriptional corepressor for SNAI1 and SNAI2/SLUG-dependent repression of E-cadherin transcription. Acts as a hypoxic regulator by bridging an association between the prolyl hydroxylases and VHL enabling efficient degradation of HIF1A. In podocytes, may play a role in the regulation of actin dynamics and/or foot process cytoarchitecture. In the course of podocyte injury, shuttles into the nucleus and acts as a transcription regulator that represses WT1-dependent transcription regulation, thereby translating changes in slit diaphragm structure into altered gene expression and a less differentiated phenotype. Involved in the organization of the basal body (By similarity). Involved in cilia growth and positioning (By similarity). {ECO:0000250|UniProtKB:A9LS46, ECO:0000269|PubMed:14736876, ECO:0000269|PubMed:15798086, ECO:0000269|PubMed:17909014, ECO:0000269|PubMed:20086015}. SUBCELLULAR LOCATION: Cell junction, focal adhesion. Cell junction, adherens junction. Nucleus. Cytoplasm, cytosol. Cell membrane. Note=In adherent but isolated podocytes, targets to focal adhesions and then shifts to adherens junctions after cells make homotypic contacts. Following podocyte injury, caused by treatment with LPS, puromycin aminonucleoside, ultraviolet or hydrogen peroxide, translocates from sites of cell-cell contacts into the cytosol and nucleus. Maximal nuclear localization is achieved 6 hours after LPS treatment. Nuclear translocation requires dynein motor activity and intact microtubule network (By similarity). Returns to cell-cell contacts several hours after LPS stimulation. In the presence of ROR2, localizes to the plasma membrane. {ECO:0000250}. SUBUNIT: Forms homodimers. Interacts with EIF4E, AGO1, AGO2, DCP2, DDX6, LATS1, LATS2, SAV1, EGLN2/PHD1 and EGLN3/PHD3. Interacts (via LIM domains) with VHL (By similarity). Interacts with CD2AP and WT1. Interacts (via LIM domains) with SNAI1 (via SNAG domain), SNAI2/SLUG (via SNAG domain) and SCRT1 (via SNAG domain). Interacts with ROR2. Following treatment with bacterial lipopolysaccharide (LPS), forms a complex with MAPK8IP3 and dynein intermediate chain. Interacts with PRICKLE3 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:A9LS46, ECO:0000269|PubMed:14736876, ECO:0000269|PubMed:18331720, ECO:0000269|PubMed:19785987, ECO:0000269|PubMed:20086015}. TISSUE SPECIFICITY: Expressed in kidney, lung, eye and ovary. In kidney, restricted to podocytes. {ECO:0000269|PubMed:14736876, ECO:0000269|PubMed:20086015}. +E9Q6C8 XKR6_MOUSE XK-related protein 6 638 70,928 Alternative sequence (2); Chain (1); Compositional bias (1); Transmembrane (7) TRANSMEM 127 147 Helical. {ECO:0000255}.; TRANSMEM 158 178 Helical. {ECO:0000255}.; TRANSMEM 315 335 Helical. {ECO:0000255}.; TRANSMEM 369 389 Helical. {ECO:0000255}.; TRANSMEM 410 430 Helical. {ECO:0000255}.; TRANSMEM 439 459 Helical. {ECO:0000255}.; TRANSMEM 470 490 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q60989 XIAP_MOUSE E3 ubiquitin-protein ligase XIAP (EC 2.3.2.27) (Baculoviral IAP repeat-containing protein 4) (IAP homolog A) (Inhibitor of apoptosis protein 3) (IAP-3) (mIAP-3) (mIAP3) (RING-type E3 ubiquitin transferase XIAP) (X-linked inhibitor of apoptosis protein) (X-linked IAP) 496 56,079 Chain (1); Cross-link (2); Metal binding (4); Modified residue (2); Region (1); Repeat (3); Sequence conflict (10); Zinc finger (1) FUNCTION: Multi-functional protein which regulates not only caspases and apoptosis, but also modulates inflammatory signaling and immunity, copper homeostasis, mitogenic kinase signaling, cell proliferation, as well as cell invasion and metastasis. Acts as a direct caspase inhibitor. Directly bind to the active site pocket of CASP3 and CASP7 and obstructs substrate entry. Inactivates CASP9 by keeping it in a monomeric, inactive state. Acts as an E3 ubiquitin-protein ligase regulating NF-kappa-B signaling and the target proteins for its E3 ubiquitin-protein ligase activity include: RIPK1, CASP3, CASP7, CASP8, CASP9, MAP3K2/MEKK2, DIABLO/SMAC, AIFM1, CCS and BIRC5/survivin. Ubiquitinion of CCS leads to enhancement of its chaperone activity toward its physiologic target, SOD1, rather than proteasomal degradation. Ubiquitinion of MAP3K2/MEKK2 and AIFM1 does not lead to proteasomal degradation. Plays a role in copper homeostasis by ubiquitinationg COMMD1 and promoting its proteasomal degradation. Can also function as E3 ubiquitin-protein ligase of the NEDD8 conjugation pathway, targeting effector caspases for neddylation and inactivation. Regulates the BMP signaling pathway and the SMAD and MAP3K7/TAK1 dependent pathways leading to NF-kappa-B and JNK activation. Acts as an important regulator of innate immune signaling via regulation of Nodlike receptors (NLRs). Protects cells from spontaneous formation of the ripoptosome, a large multi-protein complex that has the capability to kill cancer cells in a caspase-dependent and caspase-independent manner. Suppresses ripoptosome formation by ubiquitinating RIPK1 and CASP8. Acts as a positive regulator of Wnt signaling and ubiquitinates TLE1, TLE2, TLE3, TLE4 and AES. Ubiquitination of TLE3 results in inhibition of its interaction with TCF7L2/TCF4 thereby allowing efficient recruitment and binding of the transcriptional coactivator beta-catenin to TCF7L2/TCF4 that is required to initiate a Wnt-specific transcriptional program. {ECO:0000269|PubMed:18761086, ECO:0000269|PubMed:19473982}. PTM: S-Nitrosylation down-regulates its E3 ubiquitin-protein ligase activity. {ECO:0000250}.; PTM: Autoubiquitinated and degraded by the proteasome in apoptotic cells. {ECO:0000250}.; PTM: Phosphorylation by PKB/AKT protects XIAP against ubiquitination and protects the protein against proteasomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=TLE3 promotes its nuclear localization. {ECO:0000250}. SUBUNIT: Monomer, and homodimer. Interacts with DIABLO/SMAC and with PRSS25; these interactions inhibit apoptotic suppressor activity. Interacts with TAB1/MAP3K7IP1 and AIFM1. Interaction with SMAC hinders binding of TAB1/MAP3K7IP1 and AIFM1. Interacts with TCF25 and COMMD1. Interacts with SEPT4 isoform 6, but not with other SEPT4 isoforms. Interacts with RIP1, RIP2, RIP3, RIP4, CCS and USP19. Interacts (via BIR 2 domain and BIR 3 domain) with HAX1 (via C-terminus) and this interaction blocks ubiquitination of XIAP/BIRC4. Interacts with the monomeric form of BIRC5/survivin (By similarity). Interacts with TLE3 and TCF7L2/TCF4 (By similarity). {ECO:0000250}. DOMAIN: The first BIR domain is involved in interaction with TAB1/MAP3K7IP1 and is important for dimerization. The second BIR domain is sufficient to inhibit caspase-3 and caspase-7, while the third BIR is involved in caspase-9 inhibition. The interactions with DIABLO/SMAC and PRSS25 are mediated by the second and third BIR domains (By similarity). {ECO:0000250}. +Q9WTP9 VAX2_MOUSE Ventral anterior homeobox 2 (Ventral retina homeodomain protein) 292 31,701 Chain (1); DNA binding (1) FUNCTION: Transcription factor that may function in dorsoventral specification of the forebrain. Regulates the expression of Wnt signaling antagonists including the expression of a truncated TCF7L2 isoform that cannot bind CTNNB1 and acts therefore as a potent dominant-negative Wnt antagonist. Plays a crucial role in eye development and, in particular, in the specification of the ventral optic vesicle. May be a regulator of axial polarization in the retina. {ECO:0000269|PubMed:10421837, ECO:0000269|PubMed:10595508, ECO:0000269|PubMed:11830578, ECO:0000269|PubMed:21856776}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: Expressed in the developing and mature retina. {ECO:0000269|PubMed:10421837, ECO:0000269|PubMed:10595508}. +Q62468 VILI_MOUSE Villin-1 827 92,775 Calcium binding (1); Chain (1); Domain (1); Modified residue (3); Region (6); Repeat (6); Sequence conflict (1) FUNCTION: Epithelial cell-specific Ca(2+)-regulated actin-modifying protein that modulates the reorganization of microvillar actin filaments. Plays a role in the actin nucleation, actin filament bundle assembly, actin filament capping and severing. Binds phosphatidylinositol 4,5-bisphosphate (PIP2) and lysophosphatidic acid (LPA); binds LPA with higher affinity than PIP2. Binding to LPA increases its phosphorylation by SRC and inhibits all actin-modifying activities. Binding to PIP2 inhibits actin-capping and -severing activities but enhances actin-bundling activity. Regulates the intestinal epithelial cell morphology, cell invasion, cell migration and apoptosis. Protects against apoptosis induced by dextran sodium sulfate (DSS) in the gastrointestinal epithelium. Appears to regulate cell death by maintaining mitochondrial integrity. Enhances hepatocyte growth factor (HGF)-induced epithelial cell motility, chemotaxis and wound repair. Upon S.flexneri cell infection, its actin-severing activity enhances actin-based motility of the bacteria and plays a role during the dissemination. {ECO:0000269|PubMed:12937273, ECO:0000269|PubMed:16008578, ECO:0000269|PubMed:18198174}. PTM: Phosphorylated on tyrosine residues by SRC. The unphosphorylated form increases the initial rate of actin-nucleating activity, whereas the tyrosine phosphorylated form inhibits actin-nucleating activity, enhances actin-bundling activity and enhances actin-severing activity by reducing high Ca(2+) requirements. The tyrosine phosphorylated form does not regulate actin-capping activity. Tyrosine phosphorylation is essential for cell migration: tyrosine phosphorylation sites in the N-terminus half regulate actin reorganization and cell morphology, whereas tyrosine phosphorylation sites in the C-terminus half regulate cell migration via interaction with PLCG1 (By similarity). Tyrosine phosphorylation is induced by epidermal growth factor (EGF) and stimulates cell migration. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell projection, microvillus {ECO:0000250}. Cell projection, lamellipodium. Cell projection, ruffle {ECO:0000250}. Cell projection, filopodium tip. Cell projection, filopodium. Note=Rapidly redistributed to ruffles and lamellipodia structures in response to autotaxin, lysophosphatidic acid (LPA) and epidermal growth factor (EGF) treatment (By similarity). Relocalized in the tip of cellular protrusions and filipodial extensions upon infection with S.flexneri in primary intestinal epithelial cells (IEC) and in the tail-like structures forming the actin comets of S.flexneri. Redistributed to the leading edge of hepatocyte growth factor (HGF)-induced lamellipodia. {ECO:0000250}. SUBUNIT: Monomer. Homodimer; homodimerization is necessary for actin-bundling. Associates with F-actin; phosphorylation at tyrosine residues decreases the association with F-actin. Interacts (phosphorylated at C-terminus tyrosine phosphorylation sites) with PLCG1 (via the SH2 domains) (By similarity). Interacts (phosphorylated form) with PLCG1; the interaction is enhanced by hepatocyte growth factor (HGF). {ECO:0000250}. DOMAIN: Consists of a large core fragment in the N-terminal portion and a small headpiece (HP) in the C-terminal portion. The core fragment is necessary for both actin-nucleating and -severing activities, whereas the HP binds F-actin strongly in both the presence and absence of calcium and is necessary in actin-bundling activity. The Gelsolin-like 1 repeat is necessary for the actin-capping activity. The entire core fragment is necessary for the actin-severing activity. Two major calcium-sensitive sites are involved in conformational changes and determine separate functional properties: the first site (Glu-25, Asp-44 and Glu-74) regulates the actin-capping and actin-severing activities; while the second site (Asp-61, Asp-86 and Ala-93) regulates only the actin-severing activity (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in small intestin, colon, kidney and enterocytes (at protein level). {ECO:0000269|PubMed:10459016, ECO:0000269|PubMed:16008578}. +P41588 VIPR2_MOUSE Vasoactive intestinal polypeptide receptor 2 (VIP-R-2) (Pituitary adenylate cyclase-activating polypeptide type III receptor) (PACAP type III receptor) (PACAP-R-3) (PACAP-R3) 437 49,474 Chain (1); Disulfide bond (4); Glycosylation (3); Sequence conflict (1); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 126 150 Helical; Name=1. {ECO:0000255}.; TRANSMEM 158 177 Helical; Name=2. {ECO:0000255}.; TRANSMEM 203 226 Helical; Name=3. {ECO:0000255}.; TRANSMEM 240 261 Helical; Name=4. {ECO:0000255}.; TRANSMEM 279 302 Helical; Name=5. {ECO:0000255}.; TRANSMEM 328 347 Helical; Name=6. {ECO:0000255}.; TRANSMEM 360 379 Helical; Name=7. {ECO:0000255}. TOPO_DOM 23 125 Extracellular. {ECO:0000255}.; TOPO_DOM 151 157 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 178 202 Extracellular. {ECO:0000255}.; TOPO_DOM 227 239 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 262 278 Extracellular. {ECO:0000255}.; TOPO_DOM 303 327 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 348 359 Extracellular. {ECO:0000255}.; TOPO_DOM 380 437 Cytoplasmic. {ECO:0000255}. FUNCTION: This is a receptor for VIP as well as PACAP-38 and -27, the activity of this receptor is mediated by G proteins which activate adenylyl cyclase. Can be coupled to phospholipase C. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed at high levels in the MIN6 cells, at moderate levels in pancreatic islets, insulin-secreting cells, lung, brain, stomach, and colon, and at low levels in the heart. +A2AIV2 VIR_MOUSE Protein virilizer homolog 1811 201,439 Alternative sequence (2); Chain (1); Compositional bias (3); Erroneous initiation (1); Initiator methionine (1); Modified residue (15); Sequence conflict (4) FUNCTION: Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing. Acts as a key regulator of m6A methylation by promoting m6A methylation of mRNAs in the 3'-UTR near the stop codon: recruits the catalytic core components METTL3 and METTL14, thereby guiding m6A methylation at specific sites. Required for mRNA polyadenylation via its role in selective m6A methylation: m6A methylation of mRNAs in the 3'-UTR near the stop codon correlating with alternative polyadenylation (APA). {ECO:0000250|UniProtKB:Q69YN4}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q69YN4}. Nucleus, nucleoplasm {ECO:0000269|PubMed:29547716}. Cytoplasm {ECO:0000269|PubMed:29547716}. Note=Mainly nuclear with some fraction located in the cytoplasm (PubMed:29547716). ZC3H13 is required to anchor component of the MACOM subcomplex, such as VIRMA, in the nucleus (PubMed:29547716). {ECO:0000269|PubMed:29547716}. SUBUNIT: Component of the WMM complex, a N6-methyltransferase complex composed of a catalytic subcomplex, named MAC, and of an associated subcomplex, named MACOM (PubMed:29535189, PubMed:29547716). The MAC subcomplex is composed of METTL3 and METTL14 (PubMed:29535189, PubMed:29547716). The MACOM subcomplex is composed of WTAP, ZC3H13, CBLL1/HAKAI, VIRMA, and, in some cases of RBM15 (RBM15 or RBM15B) (PubMed:29535189, PubMed:29547716). Interacts with WTAP (By similarity). Also component of a MACOM-like complex, named WTAP complex, composed of WTAP, ZC3H13, CBLL1, VIRMA, RBM15, BCLAF1 and THRAP3 (By similarity). Interacts with NUDT21 and CPSF6 (By similarity). {ECO:0000250|UniProtKB:Q69YN4, ECO:0000269|PubMed:29535189, ECO:0000269|PubMed:29547716}. +P62761 VISL1_MOUSE Visinin-like protein 1 (VILIP) (Neural visinin-like protein 1) (NVL-1) (NVP-1) 191 22,142 Calcium binding (3); Chain (1); Domain (4); Initiator methionine (1); Lipidation (1) FUNCTION: Regulates (in vitro) the inhibition of rhodopsin phosphorylation in a calcium-dependent manner. {ECO:0000250}. +Q80XI7 VOME_MOUSE Vomeromodulin (BPI fold-containing family B member 9A) 591 62,448 Alternative sequence (1); Chain (1); Compositional bias (2); Glycosylation (2); Signal peptide (1) PTM: N-glycosylated. The N-glycans consist mainly of complex sialylated and fucosylated biantennary structures. {ECO:0000250|UniProtKB:Q63751}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20368189}. TISSUE SPECIFICITY: Expressed in lung. Not detected in other tissues tested (at protein level). {ECO:0000269|PubMed:20368189}. +P13373 VPRE2_MOUSE Immunoglobulin omega chain (Protein VPreB2) 142 16,052 Chain (1); Disulfide bond (1); Region (5); Signal peptide (1) FUNCTION: Associates with the Ig-mu chain to form a molecular complex that is expressed on the surface of pre-B-cells. This complex presumably regulates Ig gene rearrangements in the early steps of B-cell differentiation. TISSUE SPECIFICITY: Only expressed by pre-B-cells. +Q6NVE8 WDR44_MOUSE WD repeat-containing protein 44 (Rabphilin-11) 915 101,555 Alternative sequence (1); Chain (1); Coiled coil (1); Compositional bias (1); Initiator methionine (1); Modified residue (24); Region (1); Repeat (8); Sequence conflict (1) FUNCTION: Downstream effector for RAB11. May be involved in vesicle recycling (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cytoplasm, perinuclear region. Endosome membrane. Golgi apparatus, trans-Golgi network. Note=Colocalized with RAB11 along microtubules oriented toward lamellipodia. {ECO:0000250}. SUBUNIT: Interacts with the GTP-bound form of RAB11 when membrane-associated. Does not bind to other Rab and Rho small G proteins (By similarity). {ECO:0000250}. +Q9CR27 WASC3_MOUSE WASH complex subunit 3 (Coiled-coil domain-containing protein 53) 194 21,093 Chain (1); Coiled coil (1); Modified residue (1); Sequence conflict (3) FUNCTION: Acts at least in part as component of the WASH core complex whose assembly at the surface of endosomes seems to inhibit WASH nucleation-promoting factor (NPF) activity in recruiting and activating the Arp2/3 complex to induce actin polymerization, and which is involved in regulation of the fission of tubules that serve as transport intermediates during endosome sorting. {ECO:0000250|UniProtKB:Q9Y3C0}. SUBCELLULAR LOCATION: Early endosome {ECO:0000305}. SUBUNIT: Component of the WASH core complex also described as WASH regulatory complex (SHRC) composed of WASHC1, WASHC2, WASHC3, WASHC4 and WASHC5. The WASH core complex associates via WASHC2 with the F-actin-capping protein dimer (formed by CAPZA1, CAPZA2 or CAPZA3 and CAPZB) in a transient or substoichiometric manner which was initially described as WASH complex. {ECO:0000250|UniProtKB:Q9Y3C0}. +E9Q349 WDR25_MOUSE WD repeat-containing protein 25 535 58,480 Alternative sequence (2); Chain (1); Repeat (7) +P48281 VDR_MOUSE Vitamin D3 receptor (VDR) (1,25-dihydroxyvitamin D3 receptor) (Nuclear receptor subfamily 1 group I member 1) 422 47,834 Binding site (3); Chain (1); DNA binding (1); Domain (1); Region (4); Sequence conflict (1); Zinc finger (2) FUNCTION: Nuclear receptor for calcitriol, the active form of vitamin D3 which mediates the action of this vitamin on cells (By similarity). Enters the nucleus upon vitamin D3 binding where it forms heterodimers with the retinoid X receptor/RXR (By similarity). The VDR-RXR heterodimers bind to specific response elements on DNA and activate the transcription of vitamin D3-responsive target genes (By similarity). Plays a central role in calcium homeostasis (By similarity). {ECO:0000250|UniProtKB:P11473, ECO:0000250|UniProtKB:P13053}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}. Cytoplasm {ECO:0000250|UniProtKB:P11473}. Note=Localizes mainly to the nucleus. Localization to the nucleus is enhanced by vitamin D3. {ECO:0000250|UniProtKB:P11473}. SUBUNIT: Homodimer in the absence of bound vitamin D3. Heterodimer with RXRA after vitamin D3 binding. Interacts with MED1, NCOA1, NCOA2, NCOA3 and NCOA6 coactivators, leading to a strong increase of transcription of target genes. Interacts with the corepressor NCOR1. Interacts with SNW1. Interacts with IRX4, the interaction does not affect its transactivation activity. {ECO:0000250|UniProtKB:P11473}. DOMAIN: Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain. {ECO:0000250}. +Q9R1Z8 VINEX_MOUSE Vinexin (SH3 domain-containing protein SH3P3) (SH3-containing adapter molecule 1) (SCAM-1) (Sorbin and SH3 domain-containing protein 3) 733 82,349 Chain (1); Domain (4); Modified residue (6); Region (2) FUNCTION: Promotes up-regulation of actin stress fiber formation. PTM: Phosphorylated at Ser-594 by MAPK1/ERK2 during cell spreading. {ECO:0000269|PubMed:15184391}. SUBCELLULAR LOCATION: Cell junction, focal adhesion. Cell junction. Cytoplasm, cytoskeleton. Note=Localized at focal adhesion sites, cell-cell junctions and cell-extracellular matrix junctions. SUBUNIT: Interacts with vinculin by the first two SH3 domains and the proline rich region of vinculin. Binds to SOS (guanine nucleotide exchange factor of RAS and RAC), through its third SH3 domain. The formation of this complex is down-regulated by phosphorylation of SOS. Interacts with SAFB2, INPPL1/SHIP2 and SRCIN1 (By similarity). Interacts with DLG5 through its third SH3 domain. Interacts with SOCS7 and MAPK1/ERK2. Interacts with FASLG (By similarity). {ECO:0000250}. +Q6ZQB6 VIP2_MOUSE Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2 (EC 2.7.4.21) (EC 2.7.4.24) (Diphosphoinositol pentakisphosphate kinase 2) (Histidine acid phosphatase domain-containing protein 1) (InsP6 and PP-IP5 kinase 2) (VIP1 homolog 2) (mmVIP2) 1129 128,427 Alternative sequence (3); Binding site (8); Chain (1); Erroneous initiation (1); Modified residue (7); Nucleotide binding (3); Region (4); Sequence conflict (5) FUNCTION: Bifunctional inositol kinase that acts in concert with the IP6K kinases IP6K1, IP6K2 and IP6K3 to synthesize the diphosphate group-containing inositol pyrophosphates diphosphoinositol pentakisphosphate, PP-InsP5, and bis-diphosphoinositol tetrakisphosphate, (PP)2-InsP4. PP-InsP5 and (PP)2-InsP4, also respectively called InsP7 and InsP8, regulate a variety of cellular processes, including apoptosis, vesicle trafficking, cytoskeletal dynamics, exocytosis, insulin signaling and neutrophil activation. Phosphorylates inositol hexakisphosphate (InsP6) at positions 1 or 3 to produce PP-InsP5 which is in turn phosphorylated by IP6Ks to produce (PP)2-InsP4. Alternatively, phosphorylates at position 1 or 3 PP-InsP5, produced by IP6Ks from InsP6, to produce (PP)2-InsP4. {ECO:0000269|PubMed:17690096}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:O43314}. DOMAIN: The C-terminal acid phosphatase-like domain binds PtdIns(3,4,5)P3 and InsP6. Despite its similarity with the phosphatase domain of histidine acid phosphatases, it has no phosphatase activity. {ECO:0000250|UniProtKB:O43314}. +Q6TEK5 VKORL_MOUSE Vitamin K epoxide reductase complex subunit 1-like protein 1 (VKORC1-like protein 1) (EC 1.17.4.4) 176 19,779 Chain (1); Disulfide bond (1); Site (2); Topological domain (5); Transmembrane (4) TRANSMEM 17 37 Helical. {ECO:0000255}.; TRANSMEM 89 111 Helical. {ECO:0000255}.; TRANSMEM 118 135 Helical. {ECO:0000255}.; TRANSMEM 140 162 Helical. {ECO:0000255}. TOPO_DOM 1 16 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 38 88 Lumenal. {ECO:0000255}.; TOPO_DOM 112 117 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 136 139 Lumenal. {ECO:0000255}.; TOPO_DOM 163 176 Cytoplasmic. {ECO:0000305}. FUNCTION: Involved in vitamin K metabolism. Can reduce inactive vitamin K 2,3-epoxide to active vitamin K (in vitro), and may contribute to vitamin K-mediated protection against oxidative stress. Plays a role in vitamin K-dependent gamma-carboxylation of Glu residues in target proteins. {ECO:0000269|PubMed:23928358}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23928358}; Multi-pass membrane protein {ECO:0000269|PubMed:23928358}. TISSUE SPECIFICITY: Detected in testis and lung. {ECO:0000269|PubMed:23928358}. +Q9D659 VISTA_MOUSE V-type immunoglobulin domain-containing suppressor of T-cell activation (Platelet receptor Gi24) (V-set domain-containing immunoregulatory receptor) (V-set immunoregulatory receptor) 308 33,559 Chain (1); Disulfide bond (1); Domain (1); Erroneous initiation (1); Frameshift (2); Glycosylation (3); Modified residue (1); Sequence conflict (8); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 192 212 Helical. {ECO:0000255}. TOPO_DOM 33 191 Extracellular. {ECO:0000269|PubMed:20042595}.; TOPO_DOM 213 308 Cytoplasmic. {ECO:0000305}. FUNCTION: Immunoregulatory receptor which inhibits the T-cell response (PubMed:21383057, PubMed:24743150, PubMed:25267631). May promote differentiation of embryonic stem cells, by inhibiting BMP4 signaling (PubMed:20042595). May stimulate MMP14-mediated MMP2 activation (By similarity). {ECO:0000250|UniProtKB:Q9H7M9, ECO:0000269|PubMed:20042595, ECO:0000269|PubMed:21383057, ECO:0000269|PubMed:24743150, ECO:0000269|PubMed:25267631}. PTM: At the cell surface, may be cleaved by MMP14. {ECO:0000250}.; PTM: N-glycosylated. {ECO:0000269|PubMed:20042595}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20042595, ECO:0000269|PubMed:21768399}; Single-pass type I membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Expressed in spleen, thymus, bone marrow, lymph node, and in T-cells within the lamina propria of the small intestine (PubMed:21768399). Detected on CD4+ and CD8+ T-cells, bone marrow-derived dendritic cells (BMDCs), peritoneal macrophages, neutrophils, and natural killer (NK) cells (PubMed:21768399). In spleen and lymph nodes, highly expressed on CD4+ T-cell populations, and at lower levels on CD8+ T-cells (PubMed:21383057). In thymus, has low expression on CD4+ cells and CD8+ cells, and not detected on CD4+CD8+ cells (PubMed:21383057). Expressed in splenic and peritoneal CD11b cells (PubMed:21383057). Not detected in most B cells and NK cells (at protein level) (PubMed:21383057). Also detected at lower levels in non-hematopoeitic tissues such as heart, brain, lung, kidney, muscle, ovary, and testis (PubMed:21768399, PubMed:21383057). {ECO:0000269|PubMed:21383057, ECO:0000269|PubMed:21768399}. +Q99KC8 VMA5A_MOUSE von Willebrand factor A domain-containing protein 5A (Loss of heterozygosity 11 chromosomal region 2 gene A protein homolog) 793 87,143 Chain (1); Domain (2); Modified residue (1); Sequence conflict (5) FUNCTION: May play a role in tumorigenesis as a tumor suppressor. Altered expression of this protein and disruption of the molecular pathway it is involved in may contribute directly to or modify tumorigenesis (By similarity). {ECO:0000250}. +Q62472 VNS2_MOUSE Vomeronasal secretory protein 2 (Lipocalin-4) (Vomeronasal secretory protein II) (VNSP II) 185 21,399 Chain (1); Disulfide bond (1); Signal peptide (1) FUNCTION: Transport of lipophilic molecules, possible pheromone-carrier. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Specifically expressed in vomeronasal and posterior glands of the nasal septum, the ducts of which open into the lumen of the vomeronasal organ. +Q5H8C4 VP13A_MOUSE Vacuolar protein sorting-associated protein 13A (Chorea-acanthocytosis protein homolog) (Chorein) 3166 359,401 Alternative sequence (2); Chain (1); Modified residue (3); Repeat (6); Sequence caution (1) FUNCTION: May play a role in the control of protein cycling through the trans-Golgi network to early and late endosomes, lysosomes and plasma membrane. {ECO:0000250|UniProtKB:Q96RL7}. +Q8R1C3 VOPP1_MOUSE Vesicular, overexpressed in cancer, prosurvival protein 1 (EGFR-coamplified and overexpressed protein) (ECop) 172 19,424 Alternative sequence (2); Chain (1); Compositional bias (1); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 61 81 Helical. {ECO:0000255}. TOPO_DOM 23 60 Extracellular. {ECO:0000255}.; TOPO_DOM 82 172 Cytoplasmic. {ECO:0000255}. FUNCTION: Increases the transcriptional activity of NFKB1 by facilitating its nuclear translocation, DNA-binding and associated apoptotic response, when overexpressed. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=When overexpressed, localizes in the nucleus and perinuclear regions. {ECO:0000250}. +Q8CHS8 VP37A_MOUSE Vacuolar protein sorting-associated protein 37A (Vps37A) (ESCRT-I complex subunit VPS37A) 397 44,419 Alternative sequence (3); Chain (1); Compositional bias (1); Domain (1); Modified residue (1); Sequence conflict (4) FUNCTION: Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies. May be involved in cell growth and differentiation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Component of the ESCRT-I complex (endosomal sorting complex required for transport I) which consists of TSG101, VPS28, a VPS37 protein (VPS37A to -D) and MVB12A or MVB12B in a 1:1:1:1 stoichiometry. Interacts with TSG101, VPS28 and HGS. Component of an ESCRT-I complex (endosomal sorting complex required for transport I) which consists of TSG101, VPS28, VPS37A and UBAP1 in a 1:1:1:1 stoichiometry (By similarity). {ECO:0000250}. +Q8R105 VP37C_MOUSE Vacuolar protein sorting-associated protein 37C (ESCRT-I complex subunit VPS37C) 352 38,453 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (1); Modified residue (1) FUNCTION: Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies. May be involved in cell growth and differentiation (By similarity). {ECO:0000250}. PTM: Phosphorylated by TBK1. {ECO:0000250}. SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Probably associates with membranes. {ECO:0000250}. SUBUNIT: Component of the ESCRT-I complex (endosomal sorting complex required for transport I) which consists of TSG101, VPS28, a VPS37 protein (VPS37A to -D) and MVB12A or MVB12B in a 1:1:1:1 stoichiometry. Interacts with TSG101, VPS28, MVB12A and MVB12B. Component of the ESCRT-I complex (endosomal sorting complex required for transport I) which consists of TSG101, VPS28, a VPS37 protein (VPS37A to -D) and UBAP1 in a 1:1:1:1 stoichiometry. Interacts with HGS and STAM2. Interacts with CEP55 (By similarity). {ECO:0000250}. +Q810I0 VP37D_MOUSE Vacuolar protein sorting-associated protein 37D (ESCRT-I complex subunit VPS37D) (Williams-Beuren syndrome region protein 24 homolog) 261 28,563 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (1) FUNCTION: Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies. May be involved in cell growth and differentiation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. SUBUNIT: Component of the ESCRT-I complex (endosomal sorting complex required for transport I) which consists of TSG101, VPS28, a VPS37 protein (VPS37A to -D) and MVB12A or MVB12B in a 1:1:1:1 stoichiometry. Interacts with TSG101 and MVB12A. Component of the ESCRT-I complex (endosomal sorting complex required for transport I) which consists of TSG101, VPS28, a VPS37 protein (VPS37A to -D) and UBAP1 in a 1:1:1:1 stoichiometry (By similarity). {ECO:0000250}. +Q8BN21 VRK2_MOUSE Serine/threonine-protein kinase VRK2 (EC 2.7.11.1) (Vaccinia-related kinase 2) 503 58,119 Active site (1); Alternative sequence (3); Binding site (1); Chain (1); Domain (1); Modified residue (1); Nucleotide binding (1); Region (1); Sequence conflict (6); Transmembrane (1) TRANSMEM 482 502 Helical; Anchor for type IV membrane protein. {ECO:0000255}. FUNCTION: Serine/threonine kinase that regulates several signal transduction pathways. Isoform 1 modulates the stress response to hypoxia and cytokines, such as interleukin-1 beta (IL1B) and this is dependent on its interaction with MAPK8IP1, which assembles mitogen-activated protein kinase (MAPK) complexes. Inhibition of signal transmission mediated by the assembly of MAPK8IP1-MAPK complexes reduces JNK phosphorylation and JUN-dependent transcription. Phosphorylates histone H3. Phosphorylates 'Thr-18' of p53/TP53, and thereby increases its stability and activity. Phosphorylates BANF1 and disrupts its ability to bind DNA and reduces its binding to LEM domain-containing proteins. Downregulates the transactivation of transcription induced by ERBB2, HRAS, BRAF, and MEK1. Blocks the phosphorylation of ERK in response to ERBB2 and HRAS. May also phosphorylate MAPK8IP1. Can also phosphorylate the following substrates that are commonly used to establish in vitro kinase activity: casein, MBP and histone H2B, but it is not sure that this is physiologically relevant (By similarity). {ECO:0000250, ECO:0000269|PubMed:14645249}. PTM: Autophosphorylated. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14645249}. Endoplasmic reticulum membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}. Mitochondrion membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}. SUBUNIT: Interacts with MAP3K7, MAP2K7, MAP2K1, KSR1, RAN and MAPK8IP1. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in liver, kidney and muscle. Weakly expressed in thymus, bone marrow and spleen. {ECO:0000269|PubMed:12782311}. +Q8CIZ8 VWF_MOUSE von Willebrand factor (vWF) [Cleaved into: von Willebrand antigen 2 (von Willebrand antigen II)] 2813 309,269 Alternative sequence (2); Beta strand (6); Chain (2); Disulfide bond (29); Domain (15); Erroneous initiation (1); Glycosylation (24); Helix (7); Motif (1); Mutagenesis (1); Region (4); Sequence conflict (10); Signal peptide (1); Turn (1) FUNCTION: Important in the maintenance of hemostasis, it promotes adhesion of platelets to the sites of vascular injury by forming a molecular bridge between sub-endothelial collagen matrix and platelet-surface receptor complex GPIb-IX-V. Also acts as a chaperone for coagulation factor VIII, delivering it to the site of injury, stabilizing its heterodimeric structure and protecting it from premature clearance from plasma. {ECO:0000250|UniProtKB:P04275, ECO:0000269|PubMed:10930441}. PTM: All cysteine residues are involved in intrachain or interchain disulfide bonds. {ECO:0000250|UniProtKB:P04275}.; PTM: N- and O-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Secreted, extracellular space, extracellular matrix {ECO:0000250}. Note=Localized to storage granules. {ECO:0000250}. SUBUNIT: Multimeric. Interacts with F8 (By similarity). {ECO:0000250}. DOMAIN: The von Willebrand antigen 2 is required for multimerization of vWF and for its targeting to storage granules. {ECO:0000250}. TISSUE SPECIFICITY: Plasma. Expressed in liver. {ECO:0000269|PubMed:14613933}. +Q8BH43 WASF2_MOUSE Wiskott-Aldrich syndrome protein family member 2 (WASP family protein member 2) (Protein WAVE-2) 497 54,074 Chain (1); Compositional bias (8); Domain (1); Modified residue (1) FUNCTION: Downstream effector molecule involved in the transmission of signals from tyrosine kinase receptors and small GTPases to the actin cytoskeleton. Promotes formation of actin filaments. Part of the WAVE complex that regulates lamellipodia formation. The WAVE complex regulates actin filament reorganization via its interaction with the Arp2/3 complex (By similarity). {ECO:0000250|UniProtKB:Q9Y6W5}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Note=At the interface between the lamellipodial actin meshwork and the membrane. {ECO:0000250}. SUBUNIT: Binds actin and the Arp2/3 complex. Interacts with BAIAP2. Component of the WAVE2 complex composed of ABI1, CYFIP1/SRA1, NCKAP1/NAP1 (NCKAP1l/HEM1 in hematopoietic cells) and WASF2/WAVE2. Directly interacts with BRK1. Interacts with human cytomegalovirus protein UL135. Interacts with FNBP1L (via the SH3 domain). {ECO:0000250|UniProtKB:Q9Y6W5}. DOMAIN: Binds and activates the Arp2/3 complex via the C-terminal domain. Interacts with actin via the WH2 domain (By similarity). {ECO:0000250|UniProtKB:Q9Y6W5}. +Q3U3T8 WDR62_MOUSE WD repeat-containing protein 62 1523 167,283 Alternative sequence (4); Chain (1); Erroneous initiation (2); Initiator methionine (1); Modified residue (11); Repeat (13); Sequence conflict (2) FUNCTION: Required for cerebral cortical development. Plays a role in neuronal proliferation and migration (By similarity). Plays a role in mother-centriole-dependent centriole duplication; the function seems also to involve CEP152, CDK5RAP2 and CEP63 through a stepwise assembled complex at the centrosome that recruits CDK2 required for centriole duplication (By similarity). {ECO:0000250|UniProtKB:O43379}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O43379}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:O43379}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:O43379}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:O43379}. Note=Shows cell cycle-dependent localization. Accumulates to the spindle pole during mitosis (By similarity). Colocalizes with CDK5RAP2, CEP152 and WDR62 in a discrete ring around the proximal end of the parental centriole. At this site, a cohesive structure is predicted to engage parental centrioles and procentrioles (By similarity). {ECO:0000250|UniProtKB:O43379}. SUBUNIT: Can form homodimers (via C-terminus). Interacts (via C-terminus) with MAPKBP1 (via C-terminus). Interacts with CDK5RAP2, CEP152, CEP63 and KIAA0753. CEP63, CDK5RAP2, CEP152, WDR62 are proposed to form a stepwise assembled complex at the centrosome forming a ring near parental centrioles. {ECO:0000250|UniProtKB:O43379}. TISSUE SPECIFICITY: Prominent in neural crest lineages from embryonic day (E) 9.5 to E11.5. Also expressed in the ventricular and subventricular zones during the period of cerebral cortical neurogenesis (E11.5-E16.5), with expression decreasing in intensity by E17.5 In the cerebellum, it is strongly expressed in precursors of granule neurons at late embryonic and early postnatal stages; by postnatal day 9 (P9). Present in fetal brain, enriched within the ventricular and subventricular zone (at protein level). {ECO:0000269|PubMed:20729831}. +Q99ME2 WDR6_MOUSE WD repeat-containing protein 6 (mWDR6) 1125 121,898 Chain (1); Modified residue (1); Repeat (19) FUNCTION: Enhances the STK11/LKB1-induced cell growth suppression activity. Negative regulator of amino acid starvation-induced autophagy. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Colocalizes in the cytoplasm with STK11/LKB1. {ECO:0000250}. SUBUNIT: Interacts with STK11/LKB1. Interacts with IRS4 (By similarity). {ECO:0000250}. +Q9JHY4 WF15B_MOUSE WAP four-disulfide core domain protein 15B (Elafin-like protein I) (Single WAP motif protein 1) 80 9,237 Chain (1); Disulfide bond (4); Domain (1); Signal peptide (1) FUNCTION: Antibacterial protein which inhibits the growth of E.coli and S.aureus. {ECO:0000269|PubMed:12574366}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Constitutively expressed in kidney and epididymis. {ECO:0000269|PubMed:12574366}. +A6PWY4 WDR76_MOUSE WD repeat-containing protein 76 622 69,007 Alternative sequence (4); Chain (1); Repeat (7); Sequence conflict (2) FUNCTION: Specifically binds 5-hydroxymethylcytosine (5hmC), suggesting that it acts as a specific reader of 5hmC. {ECO:0000269|PubMed:23434322}. SUBUNIT: Interacts with CUL4A and/or CUL4B. {ECO:0000250}. +E9PYY5 WDR78_MOUSE WD repeat-containing protein 78 807 90,173 Alternative sequence (5); Chain (1); Compositional bias (1); Repeat (6) +Q9R0C8 VAV3_MOUSE Guanine nucleotide exchange factor VAV3 (VAV-3) 847 97,968 Alternative sequence (4); Chain (1); Domain (6); Modified residue (1); Region (1); Sequence conflict (2); Zinc finger (1) FUNCTION: Exchange factor for GTP-binding proteins RhoA, RhoG and, to a lesser extent, Rac1. Binds physically to the nucleotide-free states of those GTPases (By similarity). Plays an important role in angiogenesis. Its recruitment by phosphorylated EPHA2 is critical for EFNA1-induced RAC1 GTPase activation and vascular endothelial cell migration and assembly. May be important for integrin-mediated signaling, at least in some cell types. In osteoclasts, along with SYK tyrosine kinase, required for signaling through integrin alpha-v/beta-1 (ITAGV-ITGB1), a crucial event for osteoclast proper cytoskeleton organization and function. This signaling pathway involves RAC1, but not RHO, activation. Necessary for proper wound healing. In the course of wound healing, required for the phagocytotic cup formation preceding macrophage phagocytosis of apoptotic neutrophils. Responsible for integrin beta-2-mediated macrophage adhesion and, to a lesser extent, contributes to beta-3-mediated adhesion. Does not affect integrin beta-1-mediated adhesion. {ECO:0000250, ECO:0000269|PubMed:15711558, ECO:0000269|PubMed:16782872, ECO:0000269|PubMed:19147786}. PTM: Phosphorylated. Phosphorylation can be mediated by ROS1 (By similarity). In osteoclasts, undergoes tyrosine phosphorylation in response to CSF1. {ECO:0000250}. SUBUNIT: Interacts with the PH domain of APS. Interacts with ROS1; constitutive interaction that mediates VAV3 phosphorylation (By similarity). Interacts (via SH2 domains) with the phosphorylated form of EPHA2. {ECO:0000250, ECO:0000269|PubMed:16782872}. TISSUE SPECIFICITY: Abundantly expressed in osteoclasts and mature osteoblasts. Also expressed in bone marrow macrophages (at protein level):. +Q9CR51 VATG1_MOUSE V-type proton ATPase subunit G 1 (V-ATPase subunit G 1) (V-ATPase 13 kDa subunit 1) (Vacuolar proton pump subunit G 1) 118 13,724 Chain (1); Initiator methionine (1); Modified residue (1) FUNCTION: Catalytic subunit of the peripheral V1 complex of vacuolar ATPase (V-ATPase). V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. In aerobic conditions, involved in intracellular iron homeostasis, thus triggering the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent proteasomal degradation (By similarity). {ECO:0000250|UniProtKB:O75348}. SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'' and d). TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12527205}. +Q9WTT4 VATG2_MOUSE V-type proton ATPase subunit G 2 (V-ATPase subunit G 2) (V-ATPase 13 kDa subunit 2) (Vacuolar proton pump subunit G 2) 118 13,651 Chain (1) FUNCTION: Catalytic subunit of the peripheral V1 complex of vacuolar ATPase (V-ATPase). V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. SUBCELLULAR LOCATION: Melanosome {ECO:0000250}. SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'' and d). {ECO:0000250}. +P98156 VLDLR_MOUSE Very low-density lipoprotein receptor (VLDL receptor) (VLDL-R) 873 96,373 Chain (1); Cross-link (1); Disulfide bond (33); Domain (11); Glycosylation (3); Motif (1); Region (1); Repeat (6); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 798 819 Helical. {ECO:0000255}. TOPO_DOM 28 797 Extracellular. {ECO:0000255}.; TOPO_DOM 820 873 Cytoplasmic. {ECO:0000255}. FUNCTION: Binds VLDL and transports it into cells by endocytosis. In order to be internalized, the receptor-ligand complexes must first cluster into clathrin-coated pits. Binding to Reelin induces tyrosine phosphorylation of Dab1 and modulation of Tau phosphorylation. PTM: Ubiquitinated at Lys-839 by MYLIP leading to degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. Membrane, clathrin-coated pit; Single-pass type I membrane protein. SUBUNIT: Binds to the extracellular matrix protein Reelin. Interacts with DAB1. Interacts with VLDLR. Interacts with SNX17. Interacts with PCSK9 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Abundant in heart and muscle; less in kidney, brain, ovary, testis, lung and adipose tissue. +Q8R090 VMAT1_MOUSE Chromaffin granule amine transporter (Solute carrier family 18 member 1) (Vesicular amine transporter 1) (VAT1) 521 56,033 Chain (1); Glycosylation (3); Topological domain (13); Transmembrane (12) TRANSMEM 22 42 Helical. {ECO:0000255}.; TRANSMEM 136 155 Helical. {ECO:0000255}.; TRANSMEM 165 185 Helical. {ECO:0000255}.; TRANSMEM 195 215 Helical. {ECO:0000255}.; TRANSMEM 225 247 Helical. {ECO:0000255}.; TRANSMEM 254 276 Helical. {ECO:0000255}.; TRANSMEM 297 316 Helical. {ECO:0000255}.; TRANSMEM 333 357 Helical. {ECO:0000255}.; TRANSMEM 363 383 Helical. {ECO:0000255}.; TRANSMEM 395 415 Helical. {ECO:0000255}.; TRANSMEM 420 440 Helical. {ECO:0000255}.; TRANSMEM 446 467 Helical. {ECO:0000255}. TOPO_DOM 1 21 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 43 135 Lumenal, vesicle. {ECO:0000255}.; TOPO_DOM 156 164 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 186 194 Lumenal, vesicle. {ECO:0000255}.; TOPO_DOM 216 224 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 248 253 Lumenal, vesicle. {ECO:0000255}.; TOPO_DOM 277 296 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 317 332 Lumenal, vesicle. {ECO:0000255}.; TOPO_DOM 358 362 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 384 394 Lumenal, vesicle. {ECO:0000255}.; TOPO_DOM 416 419 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 441 445 Lumenal, vesicle. {ECO:0000255}.; TOPO_DOM 468 521 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in the transport of biogenic monoamines, such as serotonin, from the cytoplasm into the secretory vesicles of neuroendocrine and endocrine cells. {ECO:0000269|PubMed:21712771}. SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000305|PubMed:21712771}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000305|PubMed:23201251}; Multi-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Detected in adrenal medulla, and brain (at protein level). In brain, specifically found in the medulla oblongata, pons, prefrontal cortex, striatum, dentate gyrus and hippocampus (at protein level). {ECO:0000269|PubMed:21712771, ECO:0000269|PubMed:23201251}. +Q9Z1G4 VPP1_MOUSE V-type proton ATPase 116 kDa subunit a isoform 1 (V-ATPase 116 kDa isoform a1) (Clathrin-coated vesicle/synaptic vesicle proton pump 116 kDa subunit) (Vacuolar adenosine triphosphatase subunit Ac116) (Vacuolar proton pump subunit 1) (Vacuolar proton translocating ATPase 116 kDa subunit a isoform 1) 839 96,467 Alternative sequence (2); Chain (1); Modified residue (3); Natural variant (1); Sequence conflict (11); Topological domain (9); Transmembrane (8) TRANSMEM 396 414 Helical. {ECO:0000255}.; TRANSMEM 417 433 Helical. {ECO:0000255}.; TRANSMEM 449 478 Helical. {ECO:0000255}.; TRANSMEM 543 562 Helical. {ECO:0000255}.; TRANSMEM 581 601 Helical. {ECO:0000255}.; TRANSMEM 647 666 Helical. {ECO:0000255}.; TRANSMEM 727 751 Helical. {ECO:0000255}.; TRANSMEM 773 811 Helical. {ECO:0000255}. TOPO_DOM 1 395 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 415 416 Vacuolar. {ECO:0000255}.; TOPO_DOM 434 448 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 479 542 Vacuolar. {ECO:0000255}.; TOPO_DOM 563 580 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 602 646 Vacuolar. {ECO:0000255}.; TOPO_DOM 667 726 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 752 772 Vacuolar. {ECO:0000255}.; TOPO_DOM 812 839 Cytoplasmic. {ECO:0000255}. FUNCTION: Required for assembly and activity of the vacuolar ATPase. Potential role in differential targeting and regulation of the enzyme for a specific organelle (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Multi-pass membrane protein. Melanosome {ECO:0000250}. Note=Coated vesicle. SUBUNIT: The V-ATPase is a heteromultimeric enzyme composed of at least thirteen different subunits. It has a membrane peripheral V1 sector for ATP hydrolysis and an integral V0 for proton translocation. The V1 sector comprises subunits A-H, whereas V0 includes subunits a, d, c, c', and c''. Interacts with SPAAR (PubMed:28024296). {ECO:0000269|PubMed:28024296}. +Q91W86 VPS11_MOUSE Vacuolar protein sorting-associated protein 11 homolog 941 107,719 Chain (1); Coiled coil (1); Initiator methionine (1); Modified residue (4); Repeat (2); Sequence conflict (12); Zinc finger (1) FUNCTION: Plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport and autophagic pathways. Believed to act as a core component of the putative HOPS and CORVET endosomal tethering complexes which are proposed to be involved in the Rab5-to-Rab7 endosome conversion probably implicating MON1A/B, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion. The HOPS complex is proposed to be recruited to Rab7 on the late endosomal membrane and to regulate late endocytic, phagocytic and autophagic traffic towards lysosomes. The CORVET complex is proposed to function as a Rab5 effector to mediate early endosome fusion probably in specific endosome subpopulations. Required for fusion of endosomes and autophagosomes with lysosomes. Involved in cargo transport from early to late endosomes and required for the transition from early to late endosomes (By similarity). {ECO:0000250|UniProtKB:Q9H270}. SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250|UniProtKB:Q9H270}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9H270}; Cytoplasmic side {ECO:0000305}. Lysosome membrane {ECO:0000250|UniProtKB:Q9H270}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9H270}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle {ECO:0000305}. Early endosome {ECO:0000305}. Cytoplasmic vesicle, autophagosome {ECO:0000305}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000305}. SUBUNIT: Core component of at least two putative endosomal tethering complexes, the homotypic fusion and vacuole protein sorting (HOPS) complex and the class C core vacuole/endosome tethering (CORVET) complex. Their common core is composed of the class C Vps proteins VPS11, VPS16, VPS18 and VPS33A, which in HOPS further associates with VPS39 and VPS41 and in CORVET with VPS8 and TGFBRAP1 (PubMed:25266290). Interacts with RAB5C (PubMed:25266290). Interacts with TGFBRAP1, MON1B, STX7, STX17, ECPAS, EZR, RDX, MSN (By similarity). Associates with adaptor protein complex 3 (AP-3) and clathrin:AP-3 complexes (PubMed:21411634). {ECO:0000250|UniProtKB:Q9H270, ECO:0000269|PubMed:21411634, ECO:0000269|PubMed:25266290, ECO:0000305|PubMed:25266290}. +Q8C754 VPS52_MOUSE Vacuolar protein sorting-associated protein 52 homolog 723 82,044 Alternative sequence (2); Chain (1); Coiled coil (2); Erroneous gene model prediction (2); Initiator methionine (1); Modified residue (2); Sequence conflict (2) FUNCTION: Acts as component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN). The GARP complex is required for the maintenance of the cycling of mannose 6-phosphate receptors between the TGN and endosomes, this cycling is necessary for proper lysosomal sorting of acid hydrolases such as CTSD. Acts as component of the EARP complex that is involved in endocytic recycling. The EARP complex associates with Rab4-positive endosomes and promotes recycling of internalized transferrin receptor (TFRC) to the plasma membrane. {ECO:0000250|UniProtKB:Q8N1B4}. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q8N1B4}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8N1B4}. Endosome membrane {ECO:0000250|UniProtKB:Q8N1B4}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8N1B4}. Recycling endosome {ECO:0000250|UniProtKB:Q8N1B4}. Note=Localizes to the trans-Golgi network as part of the GARP complex, while it localizes to recycling endosomes as part of the EARP complex. {ECO:0000250|UniProtKB:Q8N1B4}. SUBUNIT: Component of the Golgi-associated retrograde protein (GARP) complex, also called VFT (VPS fifty-three) complex, composed of VPS51, VPS52, VPS53 and VPS54. Component of the endosome-associated retrograde protein (EARP) complex, composed of VPS51, VPS52, VPS53 and VPS50/Syndetin. EIPR1 interacts with both EARP and GARP complexes and mediates the recruitment of the GARP complex to the trans-Golgi network. Interacts with RAB6A and STX10. Interacts with UHRF1BP1L. {ECO:0000250|UniProtKB:Q8N1B4}. +Q8CCB4 VPS53_MOUSE Vacuolar protein sorting-associated protein 53 homolog 832 94,423 Alternative sequence (1); Chain (1); Coiled coil (1); Erroneous initiation (1); Modified residue (5); Sequence conflict (3) FUNCTION: Acts as component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN). The GARP complex is required for the maintenance of the cycling of mannose 6-phosphate receptors between the TGN and endosomes, this cycling is necessary for proper lysosomal sorting of acid hydrolases such as CTSD. Acts as component of the EARP complex that is involved in endocytic recycling. The EARP complex associates with Rab4-positive endosomes and promotes recycling of internalized transferrin receptor (TFRC) to the plasma membrane. {ECO:0000250|UniProtKB:Q5VIR6}. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q5VIR6}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q5VIR6}. Endosome membrane {ECO:0000250|UniProtKB:Q5VIR6}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q5VIR6}. Recycling endosome {ECO:0000250|UniProtKB:Q5VIR6}. Note=Localizes to the trans-Golgi network as part of the GARP complex, while it localizes to recycling endosomes as part of the EARP complex. {ECO:0000250|UniProtKB:Q5VIR6}. SUBUNIT: Component of the Golgi-associated retrograde protein (GARP) complex, also called VFT (VPS fifty-three) complex, composed of VPS51, VPS52, VPS53 and VPS54. Component of the endosome-associated retrograde protein (EARP) complex, composed of VPS51, VPS52, VPS53 and VPS50/Syndetin. EIPR1 interacts with both EARP and GARP complexes and mediates the recruitment of the GARP complex to the trans-Golgi network. {ECO:0000250|UniProtKB:Q5VIR6}. +Q5SPW0 VPS54_MOUSE Vacuolar protein sorting-associated protein 54 (Tumor antigen SLP-8p homolog) 977 110,397 Alternative sequence (1); Beta strand (2); Chain (1); Coiled coil (1); Erroneous initiation (1); Helix (6); Modified residue (1); Natural variant (1); Sequence conflict (1); Turn (1) FUNCTION: Acts as component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN). The GARP complex is required for the maintenance of the cycling of mannose 6-phosphate receptors between the TGN and endosomes, this cycling is necessary for proper lysosomal sorting of acid hydrolases such as CTSD. Within the GARP complex, required to tether the complex to the TGN. Not involved in endocytic recycling. {ECO:0000250|UniProtKB:Q9P1Q0}. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q9P1Q0}. SUBUNIT: Component of the Golgi-associated retrograde protein (GARP) complex, also called VFT (VPS fifty-three) complex, composed of VPS51, VPS52, VPS53 and VPS54. EIPR1 interacts with GARP complex and mediates its recruitment to the trans-Golgi network. {ECO:0000250|UniProtKB:Q9P1Q0}. DISEASE: Note=Defects in Vps54 are the cause of wobbler phenotype (wr). Wr is autosomal recessive and is a spontaneous mutation discovered almost 50 years ago. It causes spinal muscular atrophy and defective spermiogenesis. {ECO:0000269|PubMed:16244655, ECO:0000269|PubMed:20615984}. +Q8R0A6 VTM2A_MOUSE V-set and transmembrane domain-containing protein 2A 236 25,876 Chain (1); Disulfide bond (1); Domain (1); Erroneous initiation (1); Glycosylation (2); Mutagenesis (2); Signal peptide (1) FUNCTION: Plays a role in the regulation of the early stage of white and brown preadipocyte cell differentiation. Promotes adipogenic commitment of preadipocytes by increasing gene expression of the transcription factor PPARG in a BMP4-dependent signaling pathway. {ECO:0000269|PubMed:28052263}. PTM: N-glycosylated. N-linked glycosylation on Asn-35 and Asn-175 is critical for secretion but not for preadipocyte cell differentiation activity. {ECO:0000269|PubMed:28052263}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28052263}. Note=Secreted by adipose precursor cells (PubMed:28052263). Not detected in the nucleus (By similarity). {ECO:0000250|UniProtKB:Q8TAG5, ECO:0000269|PubMed:28052263}. SUBUNIT: Homodimer. {ECO:0000269|PubMed:28052263}. TISSUE SPECIFICITY: Expressed in brain. Expressed in neurons. Expressed in adipose precursor cells in epididymal white adipose tissue (at protein level). Strongly expressed in adipose precursor cells. Weakly expressed in adipocytes. {ECO:0000269|PubMed:28052263}. +P29788 VTNC_MOUSE Vitronectin (VN) (S-protein) (Serum-spreading factor) 478 54,849 Chain (1); Disulfide bond (8); Domain (1); Glycosylation (3); Modified residue (12); Motif (1); Region (1); Repeat (4); Sequence conflict (7); Signal peptide (1) FUNCTION: Vitronectin is a cell adhesion and spreading factor found in serum and tissues. Vitronectin interact with glycosaminoglycans and proteoglycans. Is recognized by certain members of the integrin family and serves as a cell-to-substrate adhesion molecule. Inhibitor of the membrane-damaging effect of the terminal cytolytic complement pathway. PTM: Sulfated on 2 tyrosine residues. {ECO:0000250}.; PTM: N- and O-glycosylated. {ECO:0000250}.; PTM: It has been suggested that the active SMB domain may be permitted considerable disulfide bond heterogeneity or variability, thus two alternate disulfide patterns based on 3D structures are described with 1 disulfide bond conserved in both. SUBCELLULAR LOCATION: Secreted, extracellular space. SUBUNIT: Interacts with SERPINE1/PAI1, insulin and C1QBP. {ECO:0000250}. DOMAIN: The SMB domain mediates interaction with SERPINE1/PAI1. The heparin-binding domain mediates interaction with insulin (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Plasma. +Q7TSP5 VTCN1_MOUSE V-set domain containing T-cell activation inhibitor 1 (B7 homolog 4) (B7-H4) (Immune costimulatory protein B7-H4) (Protein B7S1) (T cell costimulatory molecule B7x) 283 30,875 Chain (1); Disulfide bond (2); Domain (2); Glycosylation (1); Lipidation (1); Propeptide (1); Sequence conflict (3); Signal peptide (1) FUNCTION: Negatively regulates T-cell-mediated immune response by inhibiting T-cell activation, proliferation, cytokine production and development of cytotoxicity. When expressed on the cell surface of tumor macrophages, plays an important role, together with regulatory T-cells (Treg), in the suppression of tumor-associated antigen-specific T-cell immunity. Involved in promoting epithelial cell transformation. {ECO:0000250|UniProtKB:Q7Z7D3, ECO:0000269|PubMed:12818165, ECO:0000269|PubMed:12818166, ECO:0000269|PubMed:12920180}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q7Z7D3}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12818165, ECO:0000269|PubMed:12818166, ECO:0000269|PubMed:12920180}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:12818165, ECO:0000269|PubMed:12818166, ECO:0000269|PubMed:12920180}. Note=Expressed at the cell surface. A soluble form has also been detected. {ECO:0000269|PubMed:12818165, ECO:0000269|PubMed:12818166, ECO:0000269|PubMed:12920180}. TISSUE SPECIFICITY: Expressed on the surface of professional antigen-presenting cells (at protein level). Widely expressed, including in kidney, liver, lung, pancreas, placenta, prostate, spleen, testis and thymus. {ECO:0000269|PubMed:12818165, ECO:0000269|PubMed:12818166, ECO:0000269|PubMed:12920180}. +O88342 WDR1_MOUSE WD repeat-containing protein 1 (Actin-interacting protein 1) (AIP1) 606 66,407 Chain (1); Modified residue (6); Repeat (13) FUNCTION: Induces disassembly of actin filaments in conjunction with ADF/cofilin family proteins (By similarity). Enhances cofilin-mediated actin severing (PubMed:25915128). Involved in cytokinesis. Involved in chemotactic cell migration by restricting lamellipodial membrane protrusions (By similarity). Involved in myocardium sarcomere organization. Required for cardiomyocyte growth at the postnatal and maintenance at the adult stage (PubMed:24840128). Involved in neutrophil actin dynamics and migration. Involved in megakaryocyte maturation and platelet shedding (PubMed:17515402). Required for the establishment of planar cell polarity (PCP) during follicular epithelium development and for cell shape changes during PCP; the function seems to implicate cooperation with CFL1 and/or DSTN/ADF. Involved in the generation/maintenance of cortical tension (PubMed:25915128). Involved in assembly and maintenance of epithelial apical cell junctions and plays a role in the organization of the perijunctional actomyosin belt (By similarity). {ECO:0000250|UniProtKB:O75083, ECO:0000250|UniProtKB:Q9W7F2, ECO:0000269|PubMed:24840128, ECO:0000269|PubMed:25915128}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q5RKI0}. Cell projection, podosome {ECO:0000250|UniProtKB:O75083}. +Q8C6G8 WDR26_MOUSE WD repeat-containing protein 26 641 70,543 Chain (1); Domain (2); Erroneous initiation (1); Modified residue (2); Repeat (6) FUNCTION: G-beta-like protein involved in cell signal transduction. Acts as a negative regulator in MAPK signaling pathway. Functions as a scaffolding protein to promote G beta:gamma-mediated PLCB2 plasma membrane translocation and subsequent activation in leukocytes. Core component of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1 (By similarity). Acts as a negative regulator of the canonical Wnt signaling pathway through preventing ubiquitination of beta-catenin CTNNB1 by the beta-catenin destruction complex, thus negatively regulating CTNNB1 degradation. Serves as a scaffold to coordinate PI3K/AKT pathway-driven cell growth and migration. Protects cells from oxidative stress-induced apoptosis via the down-regulation of AP-1 transcriptional activity as well as by inhibiting cytochrome c release from mitochondria (By similarity). Protects also cells by promoting hypoxia-mediated autophagy and mitophagy (By similarity). {ECO:0000250|UniProtKB:F1LTR1, ECO:0000250|UniProtKB:Q9H7D7}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H7D7}. Nucleus {ECO:0000250|UniProtKB:Q9H7D7}. Mitochondrion {ECO:0000250|UniProtKB:F1LTR1}. SUBUNIT: Forms homooligomers. Identified in the CTLH complex that contains GID4, RANBP9 and/or RANBP10, MKLN1, MAEA, RMND5A (or alternatively its paralog RMND5B), GID8, ARMC8, WDR26 and YPEL5. Within this complex, MAEA, RMND5A (or alternatively its paralog RMND5B), GID8, WDR26, and RANBP9 and/or RANBP10 form the catalytic core, while GID4, MKLN1, ARMC8 and YPEL5 have ancillary roles. Interacts with DDB1-CUL4A/B E3 ligase complexes. Forms a complex composed of at least WDR26, a G-beta:gamma unit, and PLCB2. Interacts with AXIN1. {ECO:0000250|UniProtKB:Q9H7D7}. +Q9JHB4 WDR31_MOUSE WD repeat-containing protein 31 (Spermatid WD repeat-containing protein) (spWD) 367 40,530 Alternative sequence (1); Chain (1); Repeat (5) +Q8K4P0 WDR33_MOUSE pre-mRNA 3' end processing protein WDR33 (WD repeat-containing protein 33) (WD repeat-containing protein of 146 kDa) 1330 145,267 Chain (1); Cross-link (3); Domain (1); Initiator methionine (1); Modified residue (11); Repeat (7) FUNCTION: Essential for both cleavage and polyadenylation of pre-mRNA 3' ends. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11162572}. SUBUNIT: Component of the cleavage and polyadenylation specificity factor (CPSF) module of the pre-mRNA 3'-end processing complex. Interacts with CPSF3/CPSF73 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Most highly expressed in testis. {ECO:0000269|PubMed:11162572}. +Q8VDD8 WASH1_MOUSE WASH complex subunit 1 (WAS protein family homolog 1) 475 51,659 Chain (1); Compositional bias (2); Cross-link (1); Domain (1); Erroneous initiation (1); Region (3); Sequence conflict (1) FUNCTION: Acts as a nucleation-promoting factor at the surface of endosomes, where it recruits and activates the Arp2/3 complex to induce actin polymerization, playing a key role in the fission of tubules that serve as transport intermediates during endosome sorting (PubMed:19922875). Its assembly in the WASH core complex seems to inhibit its NPF activity and via WASHC2 is required for its membrane targeting (By similarity). Regulates the trafficking of endosomal alpha5beta1 integrin to the plasma membrane and involved in invasive cell migration (PubMed:22114305). In T-cells involved in endosome-to-membrane recycling of receptors including T-cell receptor (TCR), CD28 and ITGAL; proposed to be implicated in T-cell proliferation and effector function (PubMed:23275443). In dendritic cells involved in endosome-to-membrane recycling of major histocompatibility complex (MHC) class II probably involving retromer and subsequently allowing antigen sampling, loading and presentation during T-cell activation (PubMed:24886983). Involved in cytokinesis and following polar body extrusion during oocyte meiotic maturation (PubMed:24998208). Involved in Arp2/3 complex-dependent actin assembly driving Salmonella typhimurium invasion independent of ruffling (PubMed:19732055). Involved in the exocytosis of MMP14 leading to matrix remodeling during invasive migration and implicating late endosome-to-plasma membrane tubular connections and cooperation with the exocyst complex (By similarity). Involved in negative regulation of autophagy independently from its role in endosomal sorting by inhibiting BECN1 ubiquitination to inactivate PIK3C3/Vps34 activity (PubMed:23974797). {ECO:0000250|UniProtKB:A8K0Z3, ECO:0000250|UniProtKB:C4AMC7, ECO:0000269|PubMed:19732055, ECO:0000269|PubMed:19922875, ECO:0000269|PubMed:20308062, ECO:0000269|PubMed:22114305, ECO:0000269|PubMed:23275443, ECO:0000269|PubMed:23974797, ECO:0000269|PubMed:24886983, ECO:0000269|PubMed:24998208, ECO:0000305|PubMed:20308062}. PTM: Ubiquitinated at Lys-219 via 'Lys-63'-linked ubiquitin chains by the TRIM27:MAGEL2 E3 ubiquitin ligase complex, leading to promote endosomal F-actin assembly. {ECO:0000250|UniProtKB:A8K0Z3}. SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000269|PubMed:19922875}. Recycling endosome membrane {ECO:0000269|PubMed:19922875}. Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:23974797}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:20308062}. Note=Localization to the endosome membrane is mediated via its interaction with WASHC2 (By similarity). Localized to Salmonella typhimurium entry sites (PubMed:19732055). {ECO:0000250|UniProtKB:A8K0Z3, ECO:0000269|PubMed:19732055}. SUBUNIT: Component of the WASH core complex also described as WASH regulatory complex SHRC composed of WASHC1, WASHC2, WASHC3, WASHC4 and WASHC5. The WASH core complex associates with the F-actin-capping protein dimer (formed by CAPZA1, CAPZA2 or CAPZA3 and CAPZB) in a transient or substoichiometric manner which was initially described as WASH complex. Interacts (via WHD1 region) with WASHC2; the interaction is direct (By similarity). Interacts with BECN1; WASHC1 and AMBRA1 can competetively interact with BECN1 (PubMed:23974797). Interacts with BLOC1S2; may associate with the BLOC-1 complex. Interacts with tubulin gamma chain (TUBG1 or TUBG2) (PubMed:20308062). Interacts with TBC1D23 (PubMed:29084197). {ECO:0000250|UniProtKB:A8K0Z3, ECO:0000250|UniProtKB:C4AMC7, ECO:0000269|PubMed:20308062, ECO:0000269|PubMed:23974797, ECO:0000269|PubMed:29084197}. DOMAIN: The VCA (verprolin, cofilin, acidic) domain promotes actin polymerization by the Arp2/3 complex in vitro. {ECO:0000250|UniProtKB:C4AMC7}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:19922875}. +Q4VBE8 WDR18_MOUSE WD repeat-containing protein 18 431 47,211 Chain (1); Repeat (6) FUNCTION: May play a role during development (By similarity). Functions as a component of the Five Friends of Methylated CHTOP (5FMC) complex; the 5FMC complex is recruited to ZNF148 by methylated CHTOP, leading to desumoylation of ZNF148 and subsequent transactivation of ZNF148 target genes. {ECO:0000250, ECO:0000269|PubMed:22872859}.; FUNCTION: Functions as a component of the Five Friends of Methylated CHTOP (5FMC) complex; the 5FMC complex is recruited to ZNF148 by methylated CHTOP, leading to desumoylation of ZNF148 and subsequent transactivation of ZNF148 target genes (PubMed:22872859). Component of the PELP1 complex involved in the nucleolar steps of 28S rRNA maturation and the subsequent nucleoplasmic transit of the pre-60S ribosomal subunit (By similarity). {ECO:0000250|UniProtKB:Q9BV38, ECO:0000269|PubMed:22872859}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9BV38}. Nucleus, nucleoplasm {ECO:0000269|PubMed:22872859}. Cytoplasm {ECO:0000269|PubMed:22872859}. Note=Mainly found in the nucleoplasm, with low levels detected in the cytoplasmic and chromatin fractions. {ECO:0000269|PubMed:22872859}. SUBUNIT: Component of the 5FMC complex, at least composed of PELP1, LAS1L, TEX10, WDR18 and SENP3; the complex interacts with methylated CHTOP and ZNF148. Interacts with NOL9 (PubMed:22872859). Component of the PELP1 complex, composed of at least PELP1, TEX10 and WDR18. The complex interacts with pre-60S ribosome particles (By similarity). {ECO:0000250|UniProtKB:Q9BV38, ECO:0000269|PubMed:22872859}. +Q402B2 WDR93_MOUSE WD repeat-containing protein 93 (Protein MA0035) 695 78,911 Chain (1); Repeat (1) TISSUE SPECIFICITY: Testis-specific. Expressed in spermatogonia, spermatocytes and spermatids. {ECO:0000269|Ref.1}. +Q8R0S6 WFKN1_MOUSE WAP, Kazal, immunoglobulin, Kunitz and NTR domain-containing protein 1 (Growth and differentiation factor-associated serum protein 2) (GASP-2) (mGASP-2) 552 59,794 Chain (1); Disulfide bond (17); Domain (6); Glycosylation (1); Signal peptide (1); Site (1) FUNCTION: Protease-inhibitor that contains multiple distinct protease inhibitor domains. Probably has serine protease- and metalloprotease-inhibitor activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. DOMAIN: The second BPTI/Kunitz inhibitor domain is able to inhibit trypsin. It has however no activity toward chymotrypsin, elastase, plasmin, pancreatic kallikrein, lung tryptase, plasma kallikrein, thrombin, urokinase or tissue plasminogen activator (By similarity). {ECO:0000250}. +P47810 WEE1_MOUSE Wee1-like protein kinase (EC 2.7.10.2) (Wee1A kinase) 646 71,578 Active site (1); Binding site (1); Chain (1); Compositional bias (3); Domain (1); Metal binding (2); Modified residue (15); Nucleotide binding (1); Sequence conflict (5) FUNCTION: Acts as a negative regulator of entry into mitosis (G2 to M transition) by protecting the nucleus from cytoplasmically activated cyclin B1-complexed CDK1 before the onset of mitosis by mediating phosphorylation of CDK1 on 'Tyr-15'. Specifically phosphorylates and inactivates cyclin B1-complexed CDK1 reaching a maximum during G2 phase and a minimum as cells enter M phase. Phosphorylation of cyclin B1-CDK1 occurs exclusively on 'Tyr-15' and phosphorylation of monomeric CDK1 does not occur. Its activity increases during S and G2 phases and decreases at M phase when it is hyperphosphorylated. A correlated decrease in protein level occurs at M/G1 phase, probably due to its degradation (By similarity). {ECO:0000250}. PTM: Phosphorylated during M and G1 phases. Also autophosphorylated. Phosphorylation at Ser-642 by BRSK1 and BRSK2 in post-mitotic neurons, leads to down-regulate WEE1 activity in polarized neurons. Phosphorylated at Ser-52 and Ser-123 by PLK1 and CDK1, respectively, generating an signal for degradation that can be recognized by the SCF(BTRC) complex, leading to its ubiquitination and degradation at the onset of G2/M phase (By similarity). {ECO:0000250}.; PTM: Dephosphorylated at Thr-239 by CTDP1. {ECO:0000250}.; PTM: Ubiquitinated and degraded at the onset of G2/M phase. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Binds to 14-3-3 protein zeta. +P47993 XCL1_MOUSE Lymphotactin (C motif chemokine 1) (Cytokine SCM-1) (Lymphotaxin) (Small-inducible cytokine C1) 114 12,467 Chain (1); Disulfide bond (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Chemotactic activity for lymphocytes but not for monocytes or neutrophils. In thymus, mediates medullary accumulation of thymic dendritic cells and contributes to regulatoy T cell development, playing a role in self-tolerance establishment. {ECO:0000269|PubMed:21300913}. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Expressed in activated CD8(+) T cells. In the thymus, expressed by medullary thymic epithelial cells. {ECO:0000269|PubMed:21300913}. +O35188 X3CL1_MOUSE Fractalkine (C-X3-C motif chemokine 1) (CX3C membrane-anchored chemokine) (Neurotactin) (Small-inducible cytokine D1) [Cleaved into: Processed fractalkine] 395 42,099 Chain (2); Disulfide bond (2); Region (2); Sequence conflict (1); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 337 357 Helical. {ECO:0000255}. TOPO_DOM 25 336 Extracellular. {ECO:0000255}.; TOPO_DOM 358 395 Cytoplasmic. {ECO:0000255}. FUNCTION: Acts as a ligand for both CX3CR1 and integrins. Binds to CX3CR1 and to integrins ITGAV:ITGB3 and ITGA4:ITGB1. Can activate integrins in both a CX3CR1-dependent and CX3CR1-independent manner. In the presence of CX3CR1, activates integrins by binding to the classical ligand-binding site (site 1) in integrins. In the absence of CX3CR1, binds to a second site (site 2) in integrins which is distinct from site 1 and enhances the binding of other integrin ligands to site 1 (By similarity). The soluble form is chemotactic for T-cells and monocytes, but not for neutrophils. The membrane-bound form promotes adhesion of those leukocytes to endothelial cells. May play a role in regulating leukocyte adhesion and migration processes at the endothelium (PubMed:9177350, PubMed:10382755). {ECO:0000250|UniProtKB:P78423, ECO:0000269|PubMed:10382755, ECO:0000269|PubMed:9177350}. PTM: A soluble short 80 kDa form may be released by proteolytic cleavage from the long membrane-anchored form. {ECO:0000269|PubMed:10382755}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9177350}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: Processed fractalkine: Secreted {ECO:0000269|PubMed:10382755}. SUBUNIT: Monomer. Forms a ternary complex with CX3CR1 and ITGAV:ITGB3 or ITGA4:ITGB1. {ECO:0000250|UniProtKB:P78423}. TISSUE SPECIFICITY: Highest levels in brain. Lower levels in kidney, heart and lung. Also found in skeletal muscle and testis. {ECO:0000269|PubMed:9177350, ECO:0000269|PubMed:9479488, ECO:0000269|PubMed:9845323}. +P27467 WNT3A_MOUSE Protein Wnt-3a 352 39,258 Chain (1); Disulfide bond (11); Glycosylation (2); Lipidation (1); Mutagenesis (8); Signal peptide (1); Site (1) FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors (Probable). Functions in the canonical Wnt signaling pathway that results in activation of transcription factors of the TCF/LEF family (PubMed:26902720). Required for normal embryonic mesoderm development and formation of caudal somites (PubMed:8299937). Required for normal morphogenesis of the developing neural tube (PubMed:8299937). Mediates self-renewal of the stem cells at the bottom on intestinal crypts (in vitro) (PubMed:26902720). {ECO:0000269|PubMed:26902720, ECO:0000269|PubMed:8299937, ECO:0000305}. PTM: Proteolytic processing by TIKI1 and TIKI2 promotes oxidation and formation of large disulfide-bond oligomers, leading to inactivation of WNT3A. {ECO:0000269|PubMed:22726442}.; PTM: Disulfide bonds have critical and distinct roles in secretion and activity. Loss of each conserved cysteine in WNT3A results in high molecular weight oxidized Wnt oligomers, which are formed through inter-Wnt disulfide bonding. {ECO:0000269|PubMed:22726442}.; PTM: Palmitoleoylation by PORCN is required for efficient binding to frizzled receptors. Palmitoleoylation is required for proper trafficking to cell surface, vacuolar acidification is critical to release palmitoleoylated WNT3A from WLS in secretory vesicles (PubMed:17141155, PubMed:24798332). Depalmitoleoylated by NOTUM, leading to inhibit Wnt signaling pathway, possibly by promoting disulfide bond formation and oligomerization (PubMed:25771893). {ECO:0000250|UniProtKB:P56704, ECO:0000269|PubMed:17141155, ECO:0000269|PubMed:24798332, ECO:0000269|PubMed:25771893}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000305}. Secreted {ECO:0000269|PubMed:17141155, ECO:0000269|PubMed:26902720}. SUBUNIT: Forms a soluble 1:1 complex with AFM; this prevents oligomerization and is required for prolonged biological activity (PubMed:26902720). The complex with AFM may represent the physiological form in body fluids (PubMed:26902720). Homooligomer; disulfide-linked, leading to inactivation (PubMed:25771893). Interacts with APCDD1 and WLS. Component of the Wnt-Fzd-LRP5-LRP6 signaling complex that contains a WNT protein, a FZD protein and LRP5 or LRP6. Interacts directly in the complex with LRP6 (By similarity). Interacts with PORCN (PubMed:10866835). Interacts with glypican GPC3 (By similarity). Interacts with PKD1 (via extracellular domain) (By similarity). {ECO:0000250|UniProtKB:P56704, ECO:0000269|PubMed:10866835, ECO:0000269|PubMed:22726442, ECO:0000269|PubMed:25771893, ECO:0000269|PubMed:26902720}. TISSUE SPECIFICITY: Dorsal portion of the neural tube (developing roof plate), and mesenchyme tissue surrounding the umbilical veins. {ECO:0000269|PubMed:2001840}. +Q00519 XDH_MOUSE Xanthine dehydrogenase/oxidase [Includes: Xanthine dehydrogenase (XD) (EC 1.17.1.4); Xanthine oxidase (XO) (EC 1.17.3.2) (Xanthine oxidoreductase) (XOR)] 1335 146,562 Active site (1); Binding site (8); Chain (1); Disulfide bond (1); Domain (2); Initiator methionine (1); Metal binding (12); Nucleotide binding (2); Sequence conflict (4) FUNCTION: Key enzyme in purine degradation. Catalyzes the oxidation of hypoxanthine to xanthine. Catalyzes the oxidation of xanthine to uric acid. Contributes to the generation of reactive oxygen species. {ECO:0000250|UniProtKB:P22985}. PTM: Subject to partial proteolysis; this alters the enzyme from the dehydrogenase form (D) to the oxidase form (O). {ECO:0000250}.; PTM: Contains sulfhydryl groups that are easily oxidized (in vitro); this alters the enzyme from the dehydrogenase form (D) to the oxidase form (O). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Peroxisome {ECO:0000250}. Secreted {ECO:0000250}. SUBUNIT: Homodimer. Interacts with BTN1A1. {ECO:0000269|PubMed:8541302}. +Q60595 XL3A_MOUSE X-linked lymphocyte-regulated protein 3A 226 26,075 Chain (1); Coiled coil (1) TISSUE SPECIFICITY: Expressed in lymphoid cells. +P51612 XPC_MOUSE DNA repair protein complementing XP-C cells homolog (Xeroderma pigmentosum group C-complementing protein homolog) (p125) 930 104,522 Chain (1); Compositional bias (5); Cross-link (4); Frameshift (1); Modified residue (9); Motif (1); Region (6); Sequence conflict (24) FUNCTION: Involved in global genome nucleotide excision repair (GG-NER) by acting as damage sensing and DNA-binding factor component of the XPC complex. Has only a low DNA repair activity by itself which is stimulated by Rad23b and Rad23a. Has a preference to bind DNA containing a short single-stranded segment but not to damaged oligonucleotides. This feature is proposed to be related to a dynamic sensor function: XPC can rapidly screen duplex DNA for non-hydrogen-bonded bases by forming a transient nucleoprotein intermediate complex which matures into a stable recognition complex through an intrinsic single-stranded DNA-binding activity.; FUNCTION: The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, Xpa, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. In vitro, the Xpc:Rad23b dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts. XPC:RAD23B contacts DNA both 5' and 3' of a cisplatin lesion with a preference for the 5' side. Xpc:Rad23b induces a bend in DNA upon binding. Xpc:Rad23b stimulates the activity of DNA glycosylases Tdg and Smug1 (By similarity). {ECO:0000250}. PTM: Ubiquitinated upon UV irradiation; the ubiquitination requires the UV-DDB complex, appears to be reversible and does not serve as a signal for degradation. Ubiquitinated by RNF11 via 'Lys-63'-linked ubiquitination. Ubiquitination by RNF111 is polysumoylation-dependent and promotes nucleotide excision repair. {ECO:0000250|UniProtKB:Q01831}.; PTM: Sumoylated; sumoylation promotes ubiquitination by RNF111. {ECO:0000250|UniProtKB:Q01831}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Omnipresent in the nucleus and consistently associates with and dissociates from DNA in the absence of DNA damage. Continuously shuttles between the cytoplasm and the nucleus, which is impeded by the presence of NER lesions (By similarity). {ECO:0000250}. SUBUNIT: Component of the XPC complex composed of XPC, RAD23B and CETN2. Interacts with RAD23A; the interaction is suggesting the existence of a functional equivalent variant XPC complex. Interacts with TDG; the interaction is demonstrated using the XPC:RAD23B dimer. Interacts with SMUG1; the interaction is demonstrated using the XPC:RAD23B dimer. Interacts with DDB2. Interacts with CCNH, GTF2H1 and ERCC3 (By similarity). {ECO:0000250}. +Q9ERK4 XPO2_MOUSE Exportin-2 (Exp2) (Chromosome segregation 1-like protein) (Importin-alpha re-exporter) 971 110,455 Chain (1); Domain (1); Modified residue (5) FUNCTION: Export receptor for importin-alpha. Mediates importin-alpha re-export from the nucleus to the cytoplasm after import substrates (cargos) have been released into the nucleoplasm. In the nucleus binds cooperatively to importin-alpha and to the GTPase Ran in its active GTP-bound form. Docking of this trimeric complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of the importin-alpha from the export receptor. CSE1L/XPO2 then return to the nuclear compartment and mediate another round of transport. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. {ECO:0000250|UniProtKB:P55060}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P55060}. Nucleus {ECO:0000250|UniProtKB:P55060}. Note=Shuttles between the nucleus and the cytoplasm. {ECO:0000250|UniProtKB:P55060}. SUBUNIT: Found in a complex with CSE1L/XPO2, Ran and KPNA2. Binds with high affinity to importin-alpha only in the presence of RanGTP. The complex is dissociated by the combined action of RanBP1 and RanGAP1. Interacts with CFTR. {ECO:0000250|UniProtKB:P55060}. TISSUE SPECIFICITY: Ubiquitous. Detected in embryos from 5 to 17 dpc. Highly expressed in adult testis, heart, brain, lung, liver, skeletal muscle, spleen and kidney. {ECO:0000269|PubMed:11564884}. +Q9EPK7 XPO7_MOUSE Exportin-7 (Exp7) (Ran-binding protein 16) 1087 123,810 Alternative sequence (1); Chain (1); Domain (1); Initiator methionine (1); Modified residue (2); Sequence conflict (4) FUNCTION: Mediates the nuclear export of proteins (cargos) with broad substrate specificity. In the nucleus binds cooperatively to its cargo and to the GTPase Ran in its active GTP-bound form. Docking of this trimeric complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of the cargo from the export receptor. XPO7 then return to the nuclear compartment and mediate another round of transport. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250}. Note=Shuttles between the nucleus and the cytoplasm. {ECO:0000250}. SUBUNIT: Binds to nucleoporins. Found in a complex with XPO7, EIF4A1, ARHGAP1, VPS26A, VPS29, VPS35 and SFN. Interacts with ARHGAP1 and SFN. Interacts with Ran and cargo proteins in a GTP-dependent manner (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in testis and spleen, moderate in kidney and liver and low in heart, brain, lung and skeletal muscle. {ECO:0000269|PubMed:11071879}. +Q6PGL7 WASC2_MOUSE WASH complex subunit 2 1334 145,311 Alternative sequence (1); Chain (1); Compositional bias (4); Modified residue (27); Motif (17); Region (5); Sequence caution (1); Sequence conflict (4) FUNCTION: Acts at least in part as component of the WASH core complex whose assembly at the surface of endosomes inhibits WASH nucleation-promoting factor (NPF) activity in recruiting and activating the Arp2/3 complex to induce actin polymerization and is involved in the fission of tubules that serve as transport intermediates during endosome sorting. Mediates the recruitment of the WASH core complex to endosome membranes via binding to phospholipids and VPS35 of the retromer CSC. Mediates the recruitment of the F-actin-capping protein dimer to the WASH core complex probably promoting localized F-actin polymerization needed for vesicle scission. Via its C-terminus binds various phospholipids, most strongly phosphatidylinositol 4-phosphate (PtdIns-(4)P), phosphatidylinositol 5-phosphate (PtdIns-(5)P) and phosphatidylinositol 3,5-bisphosphate (PtdIns-(3,5)P2). Involved in the endosome-to-plasma membrane trafficking and recycling of SNX27-retromer-dependent cargo proteins, such as GLUT1. Required for the association of DNAJC13, ENTR1, ANKRD50 with retromer CSC subunit VPS35. Required for the endosomal recruitment of CCC complex subunits COMMD1, CCDC93 and C16orf62 homolog (By similarity). {ECO:0000250|UniProtKB:Q9Y4E1}. SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000250|UniProtKB:Q9Y4E1}. Cell membrane {ECO:0000250|UniProtKB:Q9Y4E1}. SUBUNIT: Component of the WASH core complex also described as WASH regulatory complex SHRC composed of WASHC1, WASHC2, WASHC3, WASHC4 and WASHC5; in the complex interacts (via N-terminus) directly with WASHC1. The WASH core complex associates with the F-actin-capping protein dimer (formed by CAPZA1, CAPZA2 or CAPZA3 and CAPZB) in a transient or substoichiometric manner which was initially described as WASH complex. Interacts with VPS35; mediates the association with the retromer CSC complex. Interacts with FKBP15. Interacts with CCDC93, CCDC22, C16orf62 homolog; indicative for an association of the WASH core complex with the CCC complex (By similarity). Directly interacts with TBC1D23 (PubMed:29084197). {ECO:0000250|UniProtKB:Q9Y4E1, ECO:0000269|PubMed:29084197}. DOMAIN: The LFa (leucine-phenylalanine-acidic) motif bind directly to VPS35 of retromer CSC; adjacent motifs can act cooperatively to bind multiple CSCs, although there is significant variability in the affinities of different motifs for retromer. {ECO:0000250|UniProtKB:Q9Y4E1}. +Q8K1X1 WDR11_MOUSE WD repeat-containing protein 11 (Bromodomain and WD repeat-containing protein 2) 1223 135,937 Chain (1); Compositional bias (1); Modified residue (4); Repeat (9); Sequence conflict (2) FUNCTION: Involved in the Hedgehog (Hh) signaling pathway, is essential for normal ciliogenesis (PubMed:29263200). Regulates the proteolytic processing of GLI3 and cooperates with the transcription factor EMX1 in the induction of downstream Hh pathway gene expression and gonadotropin-releasing hormone production (PubMed:29263200). WDR11 complex facilitates the tethering of Adaptor protein-1 complex (AP-1)-derived vesicles. WDR11 complex acts together with TBC1D23 to facilitate the golgin-mediated capture of vesicles generated using AP-1 (By similarity). {ECO:0000250|UniProtKB:Q9BZH6, ECO:0000269|PubMed:29263200}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:29263200}. Cytoplasm {ECO:0000269|PubMed:29263200}. Nucleus {ECO:0000250|UniProtKB:Q9BZH6}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:29263200}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q9BZH6}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q9BZH6}. Note=Shuttles from the cilium to the nucleus in response to Hh signaling. Might be shuttling between the nucleus and the cytoplasm. {ECO:0000250|UniProtKB:Q9BZH6}. SUBUNIT: Component of the complex WDR11 composed of C17orf75, FAM91A1 and WDR11; FAM91A1 and WDR11 are required for proper location of the complex (By similarity). Interacts with GLI3; the interaction associateS EMX1 with GLI3 (PubMed:29263200). Interacts with TBC1D23; this interaction may be indirect and recruits TBC1D23 to AP-1-derived vesicles (PubMed:29084197). Interacts (via the N-terminal and the central portion of the protein) with EMX1 (PubMed:29263200). {ECO:0000250|UniProtKB:Q9BZH6, ECO:0000269|PubMed:29084197, ECO:0000269|PubMed:29263200}. TISSUE SPECIFICITY: Broadly expressed in various organs including brain, eye,ear, lung, heart, kideny and gonads (PubMed:29263200). Cerebral cortex. The entire developing central nervous system, except for the spinal cord, reveals expression. Expressed in the neuroepithelium, including the diencephalic region that gives rise to hypothalamic neurons. In the adult brain, intense expression is restricted to the olfactory bulb, the olfaction-related piriform cortex, the granule cell layer of the cerebellum, and neurons of the hippocampal formation. The brain demonstrated expression scattered throughout the hypothalamus, sometimes in clusters of neurons (PubMed:20887964). {ECO:0000269|PubMed:20887964, ECO:0000269|PubMed:29263200}. +Q8C2E7 WASC5_MOUSE WASH complex subunit 5 (WASH complex subunit strumpellin) 1159 134,110 Alternative sequence (2); Chain (1); Sequence conflict (1) FUNCTION: Acts at least in part as component of the WASH core complex whose assembly at the surface of endosomes seems to inhibit WASH nucleation-promoting factor (NPF) activity in recruiting and activating the Arp2/3 complex to induce actin polymerization, and which is involved in regulation of the fission of tubules that serve as transport intermediates during endosome sorting. May be involved in axonal outgrowth. Involved in cellular localization of ADRB2. Involved in cellular trafficking of BLOC-1 complex cargos such as ATP7A and VAMP7 (By similarity). Involved in cytokinesis and following polar body extrusion during oocyte meiotic maturation (PubMed:24998208). {ECO:0000250|UniProtKB:Q12768, ECO:0000269|PubMed:24998208}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q12768}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q12768}. Early endosome {ECO:0000250|UniProtKB:Q12768}. Note=Colocalizes with SYP/synaptophysin in the external molecular layer of the dentate gyrus and in motoneurons of the ventral horn of spinal cord. {ECO:0000250|UniProtKB:Q12768}. SUBUNIT: Component of the WASH core complex also described as WASH regulatory complex (SHRC) composed of WASH (WASHC1, WASH2P or WASH3P), WASHC2 (WASHC2A or WASHC2C), WASHC3, WASHC4 and WASHC5. The WASH core complex associates via WASHC2 with the F-actin-capping protein dimer (formed by CAPZA1, CAPZA2 or CAPZA3 and CAPZB) in a transient or substoichiometric manner which was initially described as WASH complex. Interacts with VCP, PI4K2A (By similarity). {ECO:0000250|UniProtKB:Q12768}. +Q8CFJ9 WDR24_MOUSE GATOR complex protein WDR24 (WD repeat-containing protein 24) 790 88,184 Chain (1); Modified residue (5); Repeat (6) FUNCTION: As a component of the GATOR subcomplex GATOR2, functions within the amino acid-sensing branch of the TORC1 signaling pathway. Indirectly activates mTORC1 and the TORC1 signaling pathway through the inhibition of the GATOR1 subcomplex. It is negatively regulated by the upstream amino acid sensors SESN2 and CASTOR1. In addition to its role in regulation of the TORC1 complex, promotes the acidification of lysosomes and facilitates autophagic flux. {ECO:0000250|UniProtKB:Q96S15}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q96S15}. SUBUNIT: Within the GATOR complex, component of the GATOR2 subcomplex, made of MIOS, SEC13, SEH1L, WDR24 and WDR59. The GATOR complex strongly interacts with RRAGA/RRAGC and RRAGB/RRAGC heterodimers. The GATOR2 complex interacts with CASTOR2 and CASTOR1; the interaction is negatively regulated by arginine. The GATOR2 complex interacts with SESN1, SESN2 and SESN3; the interaction is negatively regulated by amino acids. {ECO:0000250|UniProtKB:Q96S15}. +Q8R5H6 WASF1_MOUSE Wiskott-Aldrich syndrome protein family member 1 (WASP family protein member 1) (Protein WAVE-1) 559 61,509 Chain (1); Compositional bias (5); Domain (1); Modified residue (3); Sequence conflict (2) FUNCTION: Downstream effector molecule involved in the transmission of signals from tyrosine kinase receptors and small GTPases to the actin cytoskeleton. Promotes formation of actin filaments. Part of the WAVE complex that regulates lamellipodia formation. The WAVE complex regulates actin filament reorganization via its interaction with the Arp2/3 complex (By similarity). As component of the WAVE1 complex, required for BDNF-NTRK2 endocytic trafficking and signaling from early endosomes (PubMed:27605705). {ECO:0000250|UniProtKB:Q92558, ECO:0000269|PubMed:27605705}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q92558}. Cell junction, synapse {ECO:0000269|PubMed:24153177}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q92558}. Note=Dot-like pattern in the cytoplasm. Concentrated in Rac-regulated membrane-ruffling areas. Partial translocation to focal adhesion sites might be mediated by interaction with SORBS2. In neurons, colocalizes with activated NTRK2 after BDNF addition in endocytic sites through the association with TMEM108 (PubMed:27605705). {ECO:0000250|UniProtKB:Q92558, ECO:0000269|PubMed:27605705}. SUBUNIT: Component of the WAVE1 complex composed of ABI2, CYFIP1 or CYFIP2, BRK1, NCKAP1 and WASF1/WAVE1. Within the complex, a heterodimer containing NCKAP1 and CYFIP1 interacts with a heterotrimer formed by WAVE1, ABI2 and BRK1. CYFIP2 binds to activated RAC1 which causes the complex to dissociate, releasing activated WASF1. The complex can also be activated by NCK1. Binds actin and the Arp2/3 complex. Interacts with BAIAP2. Interacts with SHANK3; the interaction mediates the association of SHANK3 with the WAVE1 complex. Interacts with ABI1 (via N-terminus). Interacts with SORBS2; this interaction greatly enhances phosphorylation by ABL1 and dephosphorylation by PTPN12 and might mediate partial to focal adhesion sites (By similarity). {ECO:0000250|UniProtKB:Q92558, ECO:0000269|PubMed:24153177}. DOMAIN: Binds the Arp2/3 complex through the C-terminal region and actin through verprolin homology (VPH) domain. {ECO:0000250|UniProtKB:Q92558}. TISSUE SPECIFICITY: Highly expressed in brain. {ECO:0000269|PubMed:12062808, ECO:0000269|PubMed:24153177}. +D4PHA7 WSCD2_MOUSE WSC domain-containing protein 2 571 64,598 Alternative sequence (2); Chain (1); Domain (2); Erroneous initiation (1); Glycosylation (2); Transmembrane (1) TRANSMEM 21 43 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q8BZZ3 WWP1_MOUSE NEDD4-like E3 ubiquitin-protein ligase WWP1 (EC 2.3.2.26) (HECT-type E3 ubiquitin transferase WWP1) (WW domain-containing protein 1) 918 104,694 Active site (1); Chain (1); Domain (6); Erroneous initiation (1); Mutagenesis (1); Region (1); Sequence caution (1); Sequence conflict (1); Site (1) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Ubiquitinates and promotes degradation of SMAD2 in response to TGF-beta signaling, which requires interaction with TGIF (By similarity). Ubiquitinates ERBB4 isoforms JM-A CYT-1 and JM-B CYT-1, KLF2, KLF5 and TP63 and promotes their proteasomal degradation. Ubiquitinates RNF11 without targeting it for degradation. Ubiquitinates and promotes degradation of TGFBR1; the ubiquitination is enhanced by SMAD7. Ubiquitinates SMAD6 and SMAD7. {ECO:0000250, ECO:0000269|PubMed:15003522, ECO:0000269|PubMed:15735697, ECO:0000269|PubMed:18724389, ECO:0000269|PubMed:18806757, ECO:0000269|PubMed:19561640}. PTM: Auto-ubiquitinated and ubiquitinated by RNF11. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15735697}. Cell membrane {ECO:0000269|PubMed:15735697}; Peripheral membrane protein {ECO:0000269|PubMed:15735697}. Nucleus {ECO:0000269|PubMed:15735697}. SUBUNIT: Binds SCNN1A, SCNN1B, SCNN1G, WBP1, WBP2, DRPLA and adenovirus type 2 PIII. Interacts with TGIF (By similarity). Binds KLF2 AND HIVEP3. Interacts with RNF11. Interacts with SPART. Interacts with NDFIP1 and NDFIP2; this interaction activates the E3 ubiquitin-protein ligase (By similarity). Interacts with ERBB4 isoforms JM-B CYT-1 and JM-A CYT-1. Does not interact with ERB4 isoform JMA-A CYT-2. Interacts with SMAD1, SMAD2, SMAD3, SMAD5, SMAD6, SMAD7, TGFBR1 AND TGFBR2. Associates with the TGFBR1:TGFBR2 receptor complex in presence of SMAD7. Interacts with SKIL isoform 1. Interacts with TP63 isoform 1 and isoform 2. Interacts (via WW domains) with ARRDC1, ARRDC2 and ARRDC3 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9H0M0, ECO:0000269|PubMed:11375995, ECO:0000269|PubMed:15735697, ECO:0000269|PubMed:16728642, ECO:0000269|PubMed:18724389, ECO:0000269|PubMed:18806757, ECO:0000269|PubMed:19561640}. DOMAIN: The WW domains mediate interaction with PPxY motif-containing proteins. {ECO:0000250|UniProtKB:Q9H0M0}. +Q9DBH0 WWP2_MOUSE NEDD4-like E3 ubiquitin-protein ligase WWP2 (EC 2.3.2.26) (HECT-type E3 ubiquitin transferase WWP2) (WW domain-containing protein 2) 870 98,761 Active site (1); Chain (1); Domain (6); Modified residue (1) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Polyubiquitinates POU5F1 by 'Lys-63'-linked conjugation and promotes it to proteasomal degradation; regulates POU5F1 protein level during differentiation of embryonal carcinoma cells (ECCs) but not in undifferentiated ECCs and embryonic stem cells (ESCs). Ubiquitinates EGR2 and promotes it to proteasomal degradation; in T-cells the ubiquitination inhibits activation-induced cell death. Ubiquitinates SLC11A2; the ubiquitination is enhanced by presence of NDFIP1 and NDFIP2. Ubiquitinates RPB1 and promotes it to proteasomal degradation. {ECO:0000269|PubMed:17526739, ECO:0000269|PubMed:18776082, ECO:0000269|PubMed:19651900, ECO:0000269|PubMed:19997087}. PTM: Autoubiquitinated. Ubiquitinated by the SCF(FBXL15) complex, leading to its degradation by the proteasome (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O00308}. SUBUNIT: Interacts with SCNN1A, SCNN1B, SCNN1G, WBP1, WBP2 and ATN1. Interacts with ERBB4, NDFIP1 and NDFIP2. Interacts with ARRDC4 (By similarity). Interacts with POU5F1, RBP1, EGR2 and SLC11A2. Interacts (via WW domains) with ARRDC1 (via PPxY motifs); ubiquitinates ARRDC1 (By similarity). Interacts (via WW domains) with ARRDC2 and ARRDC3 (By similarity). {ECO:0000250|UniProtKB:O00308, ECO:0000269|PubMed:17526739, ECO:0000269|PubMed:18776082, ECO:0000269|PubMed:19651900}. DOMAIN: The C2 domain is involved in autoinhibition of the catalytic activity by interacting with the HECT domain. {ECO:0000250}.; DOMAIN: The WW domains mediate interaction with PPxY motif-containing proteins. {ECO:0000250|UniProtKB:O00308}. +Q5GH64 XKR7_MOUSE XK-related protein 7 580 64,302 Chain (1); Transmembrane (8) TRANSMEM 59 79 Helical. {ECO:0000255}.; TRANSMEM 89 109 Helical. {ECO:0000255}.; TRANSMEM 260 280 Helical. {ECO:0000255}.; TRANSMEM 303 323 Helical. {ECO:0000255}.; TRANSMEM 326 346 Helical. {ECO:0000255}.; TRANSMEM 355 375 Helical. {ECO:0000255}.; TRANSMEM 384 404 Helical. {ECO:0000255}.; TRANSMEM 415 435 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q924C1 XPO5_MOUSE Exportin-5 (Exp5) (Ran-binding protein 21) 1204 136,973 Alternative sequence (4); Chain (1); Modified residue (1); Region (3); Sequence conflict (2); Site (4) FUNCTION: Mediates the nuclear export of proteins bearing a double-stranded RNA binding domain (dsRBD) and double-stranded RNAs (cargos). XPO5 in the nucleus binds cooperatively to the RNA and to the GTPase Ran in its active GTP-bound form. Proteins containing dsRBDs can associate with this trimeric complex through the RNA. Docking of this complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause disassembly of the complex and release of the cargo from the export receptor. XPO5 then returns to the nuclear compartment by diffusion through the nuclear pore complex, to mediate another round of transport. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Overexpression may in some circumstances enhance RNA-mediated gene silencing (RNAi) (By similarity). Mediates nuclear export of ADAR/ADAR1 in a RanGTP-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q9HAV4}.; FUNCTION: Mediates the nuclear export of micro-RNA precursors, which form short hairpins. Also mediates the nuclear export of synthetic short hairpin RNAs used for RNA interference. In some circumstances can also mediate the nuclear export of deacylated and aminoacylated tRNAs. Specifically recognizes dsRNAs that lack a 5'-overhang in a sequence-independent manner, have only a short 3'-overhang, and that have a double-stranded length of at least 15 base-pairs. Binding is dependent on Ran-GTP (By similarity). {ECO:0000250|UniProtKB:Q9HAV4}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9HAV4}. Cytoplasm {ECO:0000250|UniProtKB:Q9HAV4}. Note=Shuttles between the nucleus and the cytoplasm. {ECO:0000250|UniProtKB:Q9HAV4}. SUBUNIT: Component of a nuclear export receptor complex composed of XPO5, RAN, dsRNA-binding proteins and dsRNA. Found in a nuclear export complex with XPO5, RAN, EEF1A1, and aminoacylated tRNA. Found in a nuclear export complex with XPO5, RAN, ILF3 and dsRNA. Found in a nuclear export complex with XPO5, RAN and pre-miRNA. Found in a nuclear export complex with XPO5, RAN, ILF3 and minihelix VA1 dsRNA. Found in a nuclear export complex with XPO5, RAN, ILF3, ZNF346 and dsRNA. Interacts with EEF1A1, ILF3, NUP153, NUP214 and ZNF346. Interacts with RAN and cargo proteins in a GTP-dependent manner. Interacts with ADAR/ADAR1 (via DRBM domains). Interacts with SMAD4; mediates nuclear export of SMAD4. Interacts with RAN (GTP-bound form). {ECO:0000250|UniProtKB:Q9HAV4}. +P05531 XLR_MOUSE X-linked lymphocyte-regulated protein PM1 208 24,613 Chain (1); Coiled coil (1) TISSUE SPECIFICITY: Expressed in lymphoid cells. +Q64705 USF2_MOUSE Upstream stimulatory factor 2 (Major late transcription factor 2) (Upstream transcription factor 2) 346 36,954 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (2); Region (1); Sequence conflict (2) FUNCTION: Transcription factor that binds to a symmetrical DNA sequence (E-boxes) (5'-CACGTG-3') that is found in a variety of viral and cellular promoters. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Efficient DNA binding requires dimerization with another bHLH protein. Binds DNA as a homodimer or a heterodimer (USF1/USF2). Interacts with MAF. {ECO:0000269|PubMed:9070273}. +Q91W78 USB1_MOUSE U6 snRNA phosphodiesterase (EC 3.1.4.-) 267 30,250 Active site (2); Chain (1); Sequence conflict (3) FUNCTION: Phosphodiesterase responsible for the U6 snRNA 3' end processing. Acts as an exoribonuclease (RNase) responsible for trimming the poly(U) tract of the last nucleotides in the pre-U6 snRNA molecule, leading to the formation of mature U6 snRNA 3' end-terminated with a 2',3'-cyclic phosphate. {ECO:0000255|HAMAP-Rule:MF_03040}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03040}. +Q8R370 USBP1_MOUSE Usher syndrome type-1C protein-binding protein 1 (USH1C-binding protein 1) 680 74,906 Chain (1); Coiled coil (4); Sequence conflict (8) SUBUNIT: Interacts via its C-terminus with the first PDZ domain of USH1C. {ECO:0000250|UniProtKB:Q8N6Y0}. +Q06318 UTER_MOUSE Uteroglobin (Clara cell 17 kDa protein) (Clara cell phospholipid-binding protein) (CCPBP) (Clara cells 10 kDa secretory protein) (CC10) (PCB-binding protein) (Secretoglobin family 1A member 1) 96 10,519 Chain (1); Disulfide bond (2); Signal peptide (1) FUNCTION: Binds phosphatidylcholine, phosphatidylinositol, polychlorinated biphenyls (PCB) and weakly progesterone, potent inhibitor of phospholipase A2. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Homodimer; antiparallel disulfide-linked. TISSUE SPECIFICITY: Clara cells (nonciliated cells of the surface epithelium of the pulmonary airways). +Q8R2N2 UTP4_MOUSE U3 small nucleolar RNA-associated protein 4 homolog (Cirhin) (Testis-expressed gene 292 protein) 686 76,909 Chain (1); Cross-link (1); Erroneous initiation (3); Frameshift (2); Repeat (11) FUNCTION: Ribosome biogenesis factor. Involved in nucleolar processing of pre-18S ribosomal RNA. Involved in small subunit (SSU) pre-rRNA processing at sites A', A0, 1 and 2b. Required for optimal pre-ribosomal RNA transcription by RNA polymerase. May be a transcriptional regulator. Acts as a positive regulator of HIVEP1. {ECO:0000250|UniProtKB:Q969X6}. PTM: May be phosphorylated during mitosis; may control the association of this protein with WRD43 and UTP15. {ECO:0000250|UniProtKB:Q969X6}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q969X6}. Chromosome {ECO:0000250|UniProtKB:Q969X6}. Note=Found predominantly at the fibrillar center. {ECO:0000250|UniProtKB:Q969X6}. SUBUNIT: Interacts with HIVEP1. Interacts with NOL11. Interacts directly with UTP15 and WDR43. May be a component of the proposed t-UTP subcomplex of the ribosomal small subunit (SSU) processome containing at least UTP4, WDR43, HEATR1, UTP15, WDR75. {ECO:0000250|UniProtKB:Q969X6}. TISSUE SPECIFICITY: Expressed in liver. {ECO:0000269|PubMed:12417987, ECO:0000269|PubMed:8703127}. +Q9QZQ3 UTS2_MOUSE Urotensin-2 (Urotensin II) (U-II) (UII) 123 13,625 Disulfide bond (1); Peptide (1); Propeptide (2); Signal peptide (1) FUNCTION: Highly potent vasoconstrictor. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Brain specific. Predominantly expressed in motoneurons of the brainstem and spinal cord. +P79457 UTY_MOUSE Histone demethylase UTY (EC 1.14.11.-) (Male-specific histocompatibility antigen H-YDB) (Ubiquitously transcribed TPR protein on the Y chromosome) (Ubiquitously transcribed Y chromosome tetratricopeptide repeat protein) 1212 136,737 Chain (1); Domain (1); Metal binding (7); Modified residue (1); Repeat (8); Sequence conflict (2) FUNCTION: Male-specific histone demethylase that catalyzes trimethylated 'Lys-27' (H3K27me3) demethylation in histone H3. Has relatively low KDM activity. {ECO:0000250|UniProtKB:O14607}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Binds TLE1 and TLE2. +Q9WV55 VAPA_MOUSE Vesicle-associated membrane protein-associated protein A (VAMP-A) (VAMP-associated protein A) (VAP-A) (33 kDa VAMP-associated protein) (VAP-33) 249 27,855 Beta strand (9); Chain (1); Coiled coil (1); Domain (1); Erroneous initiation (2); Helix (1); Initiator methionine (1); Modified residue (7); Sequence conflict (2); Topological domain (1); Transmembrane (1); Turn (1) TRANSMEM 229 249 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 2 228 Cytoplasmic. {ECO:0000255}. FUNCTION: Binds to OSBPL3, which mediates recruitment of VAPA to plasma membrane sites. The ORP3-VAPA complex stimulates RRAS signaling which in turn attenuates integrin beta-1 (ITGB1) activation at the cell surface. With OSBPL3, may regulate ER morphology. May play a role in vesicle trafficking. {ECO:0000250|UniProtKB:Q9P0L0}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10655491}; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:Q9P0L0}. Cell membrane {ECO:0000250|UniProtKB:Q9P0L0}; Single-pass type IV membrane protein {ECO:0000305}. Cell junction, tight junction {ECO:0000250|UniProtKB:Q9P0L0}. Nucleus membrane {ECO:0000250|UniProtKB:Q9Z270}. Note=Present in the plasma membrane and in intracellular vesicles, together with SNARE proteins. May also associate with the cytoskeleton. Colocalizes with OCLN at the tight junction in polarized epithelial cells. {ECO:0000250|UniProtKB:Q9P0L0}. SUBUNIT: Homodimer, and heterodimer with VAPB. Interacts with VAMP1, VAMP2, STX1A, BET1, SEC22C and with the C-terminal domain of OCLN. Interacts with OSBPL1A (By similarity). Interacts (via MSP domain) with ZFYVE27 (PubMed:24251978). May retain ZFYVE27 in the endoplasmic reticulum and regulate its function in cell projections formation. Interacts with OSBP. Interacts (via C-terminus) with RSAD2/viperin (via C-terminus). Interacts with OSBPL3 (phosphorylated form). Interacts with KIF5A in a ZFYVE27-dependent manner (By similarity). Interacts with STARD3 (via FFAT motif) (By similarity). Interacts with STARD3NL (via FFAT motif) (By similarity). {ECO:0000250|UniProtKB:Q9P0L0, ECO:0000250|UniProtKB:Q9Z270, ECO:0000269|PubMed:24251978}. TISSUE SPECIFICITY: Ubiquitous. +P83853 VAM6L_MOUSE Vam6-like protein (Fragment) 8 1,075 Chain (1); Non-terminal residue (1) FUNCTION: May play a role in clustering and fusion of late endosomes and lysosomes. {ECO:0000250|UniProtKB:Q96JC1}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Lysosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Late endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. SUBUNIT: Homooligomer. {ECO:0000250|UniProtKB:Q96JC1}. +Q91ZD4 VANG2_MOUSE Vang-like protein 2 (Loop-tail protein 1) (Loop-tail-associated protein) (Van Gogh-like protein 2) 521 59,771 Chain (1); Natural variant (2); Topological domain (5); Transmembrane (4) TRANSMEM 109 129 Helical; Name=1. {ECO:0000255}.; TRANSMEM 148 168 Helical; Name=2. {ECO:0000255}.; TRANSMEM 179 199 Helical; Name=3. {ECO:0000255}.; TRANSMEM 218 238 Helical; Name=4. {ECO:0000255}. TOPO_DOM 1 108 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 130 147 Extracellular. {ECO:0000255}.; TOPO_DOM 169 178 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 200 217 Extracellular. {ECO:0000255}.; TOPO_DOM 239 521 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in the control of early morphogenesis and patterning of both axial midline structures and the development of neural plate. Plays a role in the regulation of planar cell polarity, particularly in the orientation of stereociliary bundles in the cochlea. Required for polarization and movement of myocardializing cells in the outflow tract and seems to act via RHOA signaling to regulate this process. Required for cell surface localization of FZD3 and FZD6 in the inner ear (PubMed:16495441). {ECO:0000269|PubMed:12724779, ECO:0000269|PubMed:15637299, ECO:0000269|PubMed:16495441}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23029439}; Multi-pass membrane protein {ECO:0000269|PubMed:23029439}. SUBUNIT: Homodimer and heterodimer with Vangl1. Interacts through its C-terminal region with the N-terminal half of DVL1, DVL2 and DVL3. The PDZ domain of DVL1, DVL2 and DVL3 is required for the interaction. Variants Glu-255 and Asn-464 impair interaction with the DVL proteins. Also interacts with the PDZ domains of MAGI3, SCRIB/SCRB1 and FZD3 (PubMed:15195140). Interacts with PRICKLE3 (By similarity). {ECO:0000250|UniProtKB:Q90X64, ECO:0000269|PubMed:15195140, ECO:0000269|PubMed:15456783, ECO:0000269|PubMed:16687519, ECO:0000269|PubMed:23029439}. TISSUE SPECIFICITY: Primarily expressed in the brain and epididymis. Not detected in the cochlea of Lp mice. {ECO:0000269|PubMed:11431695, ECO:0000269|PubMed:11709546, ECO:0000269|PubMed:12724779, ECO:0000269|PubMed:16687519}. DISEASE: Note=Defects in Vangl2 are a cause of the loop-tail (Lp) mutant phenotype. Heterozygous Lp mice exhibit a characteristic looped tail, while homozygous embryos show a completely open neural tube in the hindbrain and spinal region, a condition similar to the severe craniorachischisis defect in humans. Homozygotes also have complex cardiovascular defects including double-outlet right ventricle, perimembranous ventricular defects, double-sided aortic arch and associated abnormalities in the aortic arch arteries. Homozygotes show cytoplasmic accumulation of Vangl2 instead of the normal membrane localization, and Rhoa expression, which is detected in the mesenchymal cushion cells adjacent to the outflow tract, is lost in homozygotes. Homozygous embryos typically die shortly before or at birth. {ECO:0000269|PubMed:11440971}. +P57746 VATD_MOUSE V-type proton ATPase subunit D (V-ATPase subunit D) (V-ATPase 28 kDa accessory protein) (Vacuolar proton pump subunit D) 247 28,369 Chain (1) FUNCTION: Subunit of the peripheral V1 complex of vacuolar ATPase. Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells, thus providing most of the energy required for transport processes in the vacuolar system. May play a role in cilium biogenesis through regulation of the transport and the localization of proteins to the cilium (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Localizes to centrosome and the base of the cilium. {ECO:0000250}. SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'' and d). Interacts with SNX10; may play a role in ciliogenesis (By similarity). {ECO:0000250}. +Q60992 VAV2_MOUSE Guanine nucleotide exchange factor VAV2 (VAV-2) 868 99,915 Chain (1); Domain (6); Modified residue (5); Zinc finger (1) FUNCTION: Guanine nucleotide exchange factor for the Rho family of Ras-related GTPases. Plays an important role in angiogenesis. Its recruitment by phosphorylated EPHA2 is critical for EFNA1-induced RAC1 GTPase activation and vascular endothelial cell migration and assembly. {ECO:0000269|PubMed:16782872}. PTM: Phosphorylated on tyrosine residues in response to FGR activation. {ECO:0000250}. SUBUNIT: Interacts (via SH2 domains) with the phosphorylated form of EPHA2. Interacts with NEK3 and PRLR and this interaction is prolactin-dependent (By similarity). Interacts with SSX2IP. {ECO:0000250, ECO:0000269|PubMed:16782872, ECO:0000269|PubMed:22027834}. +Q8BG31 VEXIN_MOUSE Vexin 207 22,491 Chain (1) FUNCTION: Required for neurogenesis in the neural plate and retina. Strongly cooperates with neural bHLH factors to promote neurogenesis (PubMed:29518376). {ECO:0000269|PubMed:29518376}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:29518376}. Nucleus {ECO:0000269|PubMed:29518376}. Note=Nuclear localization is essential for its function in neurogenesis. {ECO:0000269|PubMed:29518376}. +Q6DFV8 VWDE_MOUSE von Willebrand factor D and EGF domain-containing protein 926 103,786 Chain (1); Domain (1); Erroneous initiation (1); Erroneous termination (1); Frameshift (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +P28047 WNT7B_MOUSE Protein Wnt-7b 349 39,302 Chain (1); Disulfide bond (11); Glycosylation (3); Lipidation (1); Region (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors that functions in the canonical Wnt/beta-catenin signaling pathway (PubMed:15923619, PubMed:28803732). Required for normal fusion of the chorion and the allantois during placenta development (PubMed:11543617). Required for central nervous system (CNS) angiogenesis and blood-brain barrier regulation (PubMed:28803732). {ECO:0000269|PubMed:11543617, ECO:0000269|PubMed:15923619, ECO:0000269|PubMed:28803732}. PTM: Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition. {ECO:0000250|UniProtKB:P27467, ECO:0000250|UniProtKB:P56704}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P56706}. Secreted {ECO:0000269|PubMed:15923619}. SUBUNIT: Forms a soluble 1:1 complex with AFM; this prevents oligomerization and is required for prolonged biological activity. The complex with AFM may represent the physiological form in body fluids (By similarity). Interacts with FZD1 and FZD10 (PubMed:15923619). Interacts with FZD4 (in vitro) (PubMed:15923619). Interacts with PORCN (PubMed:10866835). Interacts with glypican GPC3 (By similarity). Interacts (via intrinsically disordered linker region) with RECK; interaction with RECK confers ligand selectivity for Wnt7 in brain endothelial cells and allows these cells to selectively respond to Wnt7 (By similarity). {ECO:0000250|UniProtKB:P56706, ECO:0000269|PubMed:10866835, ECO:0000269|PubMed:15923619}. DOMAIN: The intrinsically disordered linker region is required for recognition by RECK in brain endothelial cells. {ECO:0000250|UniProtKB:P56706}. +Q91WL8 WWOX_MOUSE WW domain-containing oxidoreductase (EC 1.1.1.-) 414 46,512 Active site (1); Alternative sequence (6); Binding site (1); Chain (1); Domain (2); Modified residue (4); Motif (1); Mutagenesis (1); Nucleotide binding (1); Region (2); Sequence conflict (3) FUNCTION: Putative oxidoreductase. Acts as a tumor suppressor and plays a role in apoptosis. May function synergistically with p53/TP53 to control genotoxic stress-induced cell death. Plays a role in TGFB1 signaling and TGFB1-mediated cell death. Inhibits Wnt signaling, probably by sequestering DVL2 in the cytoplasm (By similarity). May also play a role in tumor necrosis factor (TNF)-mediated cell death. Required for normal bone development. {ECO:0000250, ECO:0000269|PubMed:11058590, ECO:0000269|PubMed:19366691}. PTM: Phosphorylated upon genotoxic stress. Phosphorylation of Tyr-33 regulates interaction with TP53, TP73 and MAPK8. May also regulate proapoptotic activity. Phosphorylation by TNK2 is associated with polyubiquitination and degradation (By similarity). {ECO:0000250}.; PTM: Ubiquitinated when phosphorylated by TNK2, leading to its degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19366691}. Nucleus {ECO:0000269|PubMed:11058590, ECO:0000269|PubMed:19366691}. Mitochondrion {ECO:0000269|PubMed:11058590}. Note=Partially localizes to the mitochondria (By similarity). Translocates to the nucleus in response to TGFB1 (PubMed:19366691). Translocates to the nucleus upon genotoxic stress or TNF stimulation (PubMed:11058590). {ECO:0000250|UniProtKB:Q9NZC7, ECO:0000269|PubMed:11058590, ECO:0000269|PubMed:19366691}. SUBUNIT: Interacts with TP53, TP73/p73 and MAPK8. Interacts with MAPT/TAU. Forms a ternary complex with TP53 and MDM2 and interacts with ERBB4, LITAF and WBP1. May interact with FAM189B and SCOTIN (By similarity). Interacts with HYAL2 and RUNX2. Interacts with TNK2 (By similarity). Interacts with TMEM207 (By similarity). {ECO:0000250}. DOMAIN: The WW 1 domain mediates interaction with TP73, TFAP2C, LITAF, WBP1 and probably TP53. {ECO:0000269|PubMed:11058590, ECO:0000269|PubMed:16219768}. TISSUE SPECIFICITY: Ubiquitous. In the brain, expressed in cortex, striatum, hippocampus and cerebellum (at protein level). Detected in embryonic skeleton, in cranofacial bones, vertebrae and limb bones. Detected in chondrocytes and osteoblasts. {ECO:0000269|PubMed:15026124, ECO:0000269|PubMed:17360458, ECO:0000269|PubMed:18487609}. +Q8CGF6 WDR47_MOUSE WD repeat-containing protein 47 (Neuronal enriched MAP interacting protein) (Nemitin) 920 102,312 Chain (1); Compositional bias (1); Domain (2); Erroneous initiation (1); Modified residue (7); Repeat (7); Sequence conflict (1) SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:22523538}. Note=Localization along microtubules is mediated by MAP1S. SUBUNIT: Interacts with MAP1S (via WD repeats). {ECO:0000269|PubMed:22523538}. TISSUE SPECIFICITY: Enriched in the nervous system (at protein level). {ECO:0000269|PubMed:22523538}. +Q9D7H2 WDR5B_MOUSE WD repeat-containing protein 5B 328 36,033 Chain (1); Motif (1); Repeat (7) FUNCTION: May function as a substrate receptor for CUL4-DDB1 ubiquitin E3 ligase complex. {ECO:0000269|PubMed:17041588}. SUBUNIT: Probable part of a cullin-RING E3 protein ligase complex containing CUL4B-DDB1 and a substrate-recruiting component (DCAF). Interacts with CUL4B and DDB1. {ECO:0000269|PubMed:17041588}. +Q924H7 WAC_MOUSE WW domain-containing adapter protein with coiled-coil 646 70,680 Alternative sequence (2); Chain (1); Coiled coil (1); Domain (1); Erroneous initiation (1); Modified residue (11); Sequence conflict (3) FUNCTION: Acts as a linker between gene transcription and histone H2B monoubiquitination at 'Lys-120' (H2BK120ub1). Interacts with the RNA polymerase II transcriptional machinery via its WW domain and with RNF20-RNF40 via its coiled coil region, thereby linking and regulating H2BK120ub1 and gene transcription. Regulates the cell-cycle checkpoint activation in response to DNA damage. Positive regulator of amino acid starvation-induced autophagy. Also acts as a negative regulator of basal autophagy. Positively regulates MTOR activity by promoting, in an energy-dependent manner, the assembly of the TTT complex composed of TELO2, TTI1 and TTI2 and the RUVBL complex composed of RUVBL1 and RUVBL2 into the TTT-RUVBL complex. This leads to the dimerization of the mTORC1 complex and its subsequent activation. May negatively regulate the ubiquitin proteasome pathway. {ECO:0000250|UniProtKB:Q9BTA9}. PTM: Phosphorylated on tyrosine residues. {ECO:0000269|PubMed:11827461}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:11827461}. Nucleus {ECO:0000250|UniProtKB:Q9BTA9}. Note=In distinct nuclear speckles. Colocalizes with pre-mRNA processing complexes. SUBUNIT: Interacts (via coiled coil domain) with RNF20, RNF40 and UBE2A. Interacts (via WW domain) with RNA polymerase II. Interacts with MTOR and other components of the MTOR pathway including RPTOR, RUVBL1, RUVBL2, TTI1 and TTI2. {ECO:0000250|UniProtKB:Q9BTA9}. +Q8C5V5 WDR27_MOUSE WD repeat-containing protein 27 780 86,582 Chain (1); Erroneous initiation (1); Frameshift (1); Repeat (13) +Q8VHI6 WASF3_MOUSE Wiskott-Aldrich syndrome protein family member 3 (WASP family protein member 3) (Protein WAVE-3) 501 55,204 Chain (1); Coiled coil (2); Compositional bias (3); Domain (1); Modified residue (4) FUNCTION: Downstream effector molecules involved in the transmission of signals from tyrosine kinase receptors and small GTPases to the actin cytoskeleton. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape (By similarity). {ECO:0000250}. PTM: Phosphorylation by ABL1 promotes lamellipodia formation and cell migration. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. SUBUNIT: Binds actin and the Arp2/3 complex. {ECO:0000250}. DOMAIN: Binds the Arp2/3 complex through the C-terminal region and actin through verprolin homology (VPH) domain. +Q9D565 WDR64_MOUSE WD repeat-containing protein 64 1086 123,893 Alternative sequence (3); Chain (1); Frameshift (2); Repeat (12); Sequence conflict (1) +Q3UGF1 WDR19_MOUSE WD repeat-containing protein 19 (Intraflagellar transport 144 homolog) 1341 151,457 Alternative sequence (3); Chain (1); Frameshift (1); Mutagenesis (1); Repeat (12); Sequence conflict (3) FUNCTION: Component of the IFT complex A (IFT-A), a complex required for retrograde ciliary transport (By similarity). Involved in cilia function and/or assembly (PubMed:16957054). Associates with the BBSome complex to mediate ciliary transport (PubMed:22922713). {ECO:0000250|UniProtKB:Q8NEZ3, ECO:0000269|PubMed:16957054, ECO:0000269|PubMed:22922713}. SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000269|PubMed:16957054}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:16957054}. Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:19208653}. Note=Localizes to photoreceptor connecting cilia, to the base of motile cilia in brain ependymal cells and to the base of and along primary cilia in cultured kidney inner mnedullary collecting duct (IMCD) cells. {ECO:0000269|PubMed:16957054, ECO:0000269|PubMed:19208653}. SUBUNIT: Component of the IFT complex A (IFT-A) (By similarity). Interacts with BBS1 (PubMed:22922713). Interacts with TTC25 (PubMed:25860617). {ECO:0000250|UniProtKB:Q8NEZ3, ECO:0000269|PubMed:22922713, ECO:0000269|PubMed:25860617}. TISSUE SPECIFICITY: Tissue-specific expression of isoforms (PubMed:12906858). Expressed in the prostate, testis, epididymis, submaxillary and salivary glands (PubMed:12906858). Expressed in ependymal cells lining brain ventricles (at protein level) (PubMed:16957054). {ECO:0000269|PubMed:12906858, ECO:0000269|PubMed:16957054}. +Q3UDP0 WDR41_MOUSE WD repeat-containing protein 41 460 51,511 Alternative sequence (2); Chain (1); Repeat (6); Sequence conflict (1) FUNCTION: Non-catalytic component of the C9orf72-SMCR8 complex, a complex that has guanine nucleotide exchange factor (GEF) activity and regulates autophagy. The C9orf72-SMCR8 complex promotes the exchange of GDP to GTP, converting inactive GDP-bound RAB8A and RAB39B into their active GTP-bound form, thereby promoting autophagosome maturation. The C9orf72-SMCR8 complex also acts as a negative regulator of autophagy initiation by interacting with the ATG1/ULK1 kinase complex and inhibiting its protein kinase activity. {ECO:0000250|UniProtKB:Q9HAD4}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27617292}. SUBUNIT: Component of the C9orf72-SMCR8 complex, at least composed of C9orf72, SMCR8 and WDR41. The C9orf72-SMCR8 complex associates with the ATG1/ULK1 kinase complex. {ECO:0000250|UniProtKB:Q9HAD4}. +Q3TWF6 WDR70_MOUSE WD repeat-containing protein 70 657 73,119 Chain (1); Compositional bias (1); Cross-link (3); Modified residue (4); Repeat (7) +Q4KUS1 WFDC8_MOUSE WAP four-disulfide core domain protein 8 (Putative protease inhibitor WAP8C) 273 31,279 Chain (1); Disulfide bond (15); Domain (4); Transmembrane (1) TRANSMEM 45 65 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q923D5 WBP11_MOUSE WW domain-binding protein 11 (WBP-11) (Splicing factor that interacts with PQBP-1 and PP1) 641 69,875 Chain (1); Coiled coil (1); Compositional bias (4); Cross-link (2); Frameshift (1); Modified residue (12); Motif (1); Mutagenesis (4); Region (4); Sequence conflict (2) FUNCTION: Activates pre-mRNA splicing. May inhibit PP1 phosphatase activity. {ECO:0000269|PubMed:14640981, ECO:0000269|PubMed:16162498}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Predominantly located in the nucleus with granular heterogeneous distribution. Excluded from nucleoli in interphase cells, distributed throughout cytoplasm in dividing cells. Colocalized with SC35 and U2B in the nucleus. In the cytoplasm, associates with the intermediate filament protein vimentin. SUBUNIT: Interacts via the PGR motif with PQBP1 in the nucleus. Interacts with the WW domains of WBP4 (By similarity). Interacts with PPP1CA, PPP1CB and PPP1CC. {ECO:0000250, ECO:0000269|PubMed:14640981}. TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in testis. {ECO:0000269|PubMed:14640981}. +Q920I9 WDR7_MOUSE WD repeat-containing protein 7 (TGF-beta resistance-associated protein TRAG) 1489 163,450 Alternative sequence (1); Chain (1); Modified residue (2); Repeat (9); Sequence conflict (9) +Q9D529 WBP2L_MOUSE Postacrosomal sheath WW domain-binding protein (WW domain-binding protein 2-like) 359 37,485 Chain (1); Compositional bias (1); Domain (1); Motif (6); Region (1); Repeat (6) FUNCTION: May play a role in meotic resumption and pronuclear formation, mediated by a WW domain-signaling pathway during fertilization. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:17289678}. +Q8BTE6 WFD21_MOUSE Protein Wfdc21 (Wdnm1-like protein) 63 6,792 Chain (1); Disulfide bond (3); Domain (1); Signal peptide (1) FUNCTION: May promote activation of the metalloproteinase MMP2. {ECO:0000269|PubMed:18492766}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18492766}. TISSUE SPECIFICITY: Predominantly expressed in white adipose tissue and liver. {ECO:0000269|PubMed:18492766}. +Q9ESH5 WFDC1_MOUSE WAP four-disulfide core domain protein 1 (Prostate stromal protein ps20) (ps20 growth inhibitor) 211 23,079 Chain (1); Disulfide bond (4); Domain (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Has growth inhibitory activity. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +P21552 WNT2_MOUSE Protein Wnt-2 (INT-1-related protein) (IRP) 360 40,482 Chain (1); Disulfide bond (11); Glycosylation (1); Lipidation (1); Sequence conflict (2); Signal peptide (1) FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors. Functions in the canonical Wnt/beta-catenin signaling pathway (PubMed:19686689). Functions as upstream regulator of FGF10 expression (PubMed:19686689). Plays an important role in embryonic lung development (PubMed:19686689). May contribute to embryonic brain development by regulating the proliferation of dopaminergic precursors and neurons (PubMed:20018874). {ECO:0000269|PubMed:19686689, ECO:0000305, ECO:0000305|PubMed:20018874}. PTM: Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition. {ECO:0000250|UniProtKB:P09544}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P09544}. Secreted {ECO:0000250|UniProtKB:P09544}. TISSUE SPECIFICITY: In embryos in the developing allantois, pericardium heart, and ventral-lateral mesoderm; in adults in lung, brain, heart and placenta. +P22726 WNT5B_MOUSE Protein Wnt-5b 359 40,343 Chain (1); Disulfide bond (11); Erroneous initiation (2); Glycosylation (4); Lipidation (1); Signal peptide (1) FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors. Probable developmental protein. May be a signaling molecule which affects the development of discrete regions of tissues. Is likely to signal over only few cell diameters. PTM: Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition. {ECO:0000250|UniProtKB:P27467, ECO:0000250|UniProtKB:P56704}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SUBUNIT: Interacts with PORCN. {ECO:0000269|PubMed:10866835}. +Q9JM98 WRP73_MOUSE WD repeat-containing protein WRAP73 (WD repeat-containing protein 8) (WD repeat-containing protein antisense to TP73 gene) 462 52,053 Chain (1); Modified residue (1); Repeat (6); Sequence conflict (1) FUNCTION: The SSX2IP:WRAP73 complex is proposed to act as regulator of spindle anchoring at the mitotic centrosome. Required for the centrosomal localization of SSX2IP and normal mitotic bipolar spindle morphology. Required for the targeting of centriole satellite proteins to centrosomes such as of PCM1, SSX2IP, CEP290 and PIBF1/CEP90. Required for ciliogenesis and involved in the removal of the CEP97:CCP110 complex from the mother centriole. Involved in ciliary vesicle formation at the mother centriole and required for the docking of vesicles to the basal body during ciliogenesis; may promote docking of RAB8A- and ARL13B-containing vesicles (By similarity). {ECO:0000250|UniProtKB:Q9P2S5}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9P2S5}. Note=Enriched in the proximal end of the mother centriole. During ciliogenesis also associated with the basal body of the adjacent centriole (By similarity). {ECO:0000250|UniProtKB:Q9P2S5}. SUBUNIT: Interacts with SSX2IP (PubMed:26675238). {ECO:0000269|PubMed:26675238}. TISSUE SPECIFICITY: Ubiquitous. +Q9QXY7 XK_MOUSE Membrane transport protein XK (XK homolog) (XK-related protein 1) 446 51,115 Chain (1); Disulfide bond (1); Modified residue (1); Topological domain (11); Transmembrane (10) TRANSMEM 3 23 Helical. {ECO:0000255}.; TRANSMEM 38 58 Helical. {ECO:0000255}.; TRANSMEM 69 89 Helical. {ECO:0000255}.; TRANSMEM 141 161 Helical. {ECO:0000255}.; TRANSMEM 172 192 Helical. {ECO:0000255}.; TRANSMEM 209 229 Helical. {ECO:0000255}.; TRANSMEM 236 256 Helical. {ECO:0000255}.; TRANSMEM 278 298 Helical. {ECO:0000255}.; TRANSMEM 318 338 Helical. {ECO:0000255}.; TRANSMEM 350 370 Helical. {ECO:0000255}. TOPO_DOM 1 2 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 24 37 Extracellular. {ECO:0000255}.; TOPO_DOM 59 68 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 90 140 Extracellular. {ECO:0000255}.; TOPO_DOM 162 171 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 193 208 Extracellular. {ECO:0000255}.; TOPO_DOM 230 235 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 257 277 Extracellular. {ECO:0000255}.; TOPO_DOM 299 317 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 339 349 Extracellular. {ECO:0000255}.; TOPO_DOM 371 446 Cytoplasmic. {ECO:0000255}. FUNCTION: May be involved in sodium-dependent transport of neutral amino acids or oligopeptides. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Heterodimer with Kell; disulfide-linked. {ECO:0000269|PubMed:11132157}. +O70373 XIRP1_MOUSE Xin actin-binding repeat-containing protein 1 (Cardiomyopathy-associated protein 1) 1129 123,431 Chain (1); Modified residue (6); Region (2); Repeat (17) FUNCTION: Protects actin filaments from depolymerization. {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction {ECO:0000250}. Note=Colocalizes with actin stress fibers. {ECO:0000250}. SUBUNIT: Interacts with FLNC and VASP (By similarity). Interacts with F-actin and CTNNB1. {ECO:0000250, ECO:0000269|PubMed:17925400}. DOMAIN: Xin repeats bind F-actin. TISSUE SPECIFICITY: Expressed in heart and skeletal muscle. In heart, present in intercalated disks (at protein level). {ECO:0000269|PubMed:10021346, ECO:0000269|PubMed:17766470}. +Q9Z1L4 XLRS1_MOUSE Retinoschisin (X-linked juvenile retinoschisis protein homolog) 224 25,575 Chain (1); Disulfide bond (5); Domain (1); Mutagenesis (2); Signal peptide (1) FUNCTION: Binds negatively charged membrane lipids, such as phosphatidylserine and phosphoinositides (PubMed:17325137, PubMed:20677810). May play a role in cell-cell adhesion processes in the retina, via homomeric interaction between octamers present on the surface of two neighboring cells (By similarity). Required for normal structure and function of the retina (PubMed:11983912, PubMed:17325137). {ECO:0000250|UniProtKB:O15537, ECO:0000269|PubMed:11983912, ECO:0000269|PubMed:17325137, ECO:0000269|PubMed:20677810}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O15537}. Cell membrane {ECO:0000269|PubMed:17325137, ECO:0000305|PubMed:20677810}; Peripheral membrane protein {ECO:0000269|PubMed:17325137, ECO:0000269|PubMed:20677810}; Extracellular side {ECO:0000269|PubMed:17325137, ECO:0000305|PubMed:20677810}. Note=Binds to phosphatidylserine-containing lipid membranes and embeds itself partially into the lipid bilayer. Lipid-binding requires the presence of Ca(2+) ions. {ECO:0000269|PubMed:20677810}. SUBUNIT: Homooctamer of 4 homodimers; disulfide-linked. The homooctamer has a flat, cogwheel structure with a diameter of about 14 nm. Two stacked octamers can assemble to form a hexadecamer. {ECO:0000250|UniProtKB:O15537}. TISSUE SPECIFICITY: Detected in the eye cup (PubMed:11983912). Detected in retina, in the inner segment of the photoreceptors, the inner nuclear layer, the inner plexiform layer and the ganglion cell layer (at protein level) (PubMed:10915776, PubMed:11983912, PubMed:17325137). Restricted to the retina (PubMed:10023077, PubMed:10915776). At the mRNA level, detected only within the photoreceptor cell layer, most prominently within the inner segments of the photoreceptors (PubMed:10023077, PubMed:10915776). Undetectable in the inner plexiform layers and the inner nuclear layer (PubMed:10915776). {ECO:0000269|PubMed:10023077, ECO:0000269|PubMed:10915776, ECO:0000269|PubMed:11983912, ECO:0000269|PubMed:17325137}. +Q4U4S6 XIRP2_MOUSE Xin actin-binding repeat-containing protein 2 (Beta-xin) (Cardiomyopathy-associated protein 3) (Myogenic MEF2-activated Xin-related protein) (Myomaxin) (mXinbeta) 3784 428,259 Alternative sequence (2); Chain (1); Coiled coil (4); Compositional bias (4); Domain (1); Modified residue (10); Repeat (28); Sequence conflict (9) FUNCTION: Protects actin filaments from depolymerization. {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction {ECO:0000269|PubMed:17766470}. Note=Colocalizes with actin stress fibers. SUBUNIT: Interacts with ACTN2. Interacts with F-actin (By similarity). {ECO:0000250}. DOMAIN: Xin repeats bind F-actin. TISSUE SPECIFICITY: Expression is restricted to heart and skeletal muscle. Present in intercalated disks of the heart and in the Z-disk region of skeletal muscle (at protein level). {ECO:0000269|PubMed:17046827, ECO:0000269|PubMed:17766470}. +Q60596 XRCC1_MOUSE DNA repair protein XRCC1 (X-ray repair cross-complementing protein 1) 631 68,971 Beta strand (4); Chain (1); Cross-link (2); Domain (2); Helix (4); Modified residue (21); Sequence conflict (10); Turn (1) FUNCTION: Involved in DNA single-strand break repair by mediating the assembly of DNA break repair protein complexes (By similarity). Probably during DNA repair, negatively regulates ADP-ribose levels by modulating ADP-ribosyltransferase PARP1 activity (PubMed:28002403). {ECO:0000250|UniProtKB:P18887, ECO:0000269|PubMed:28002403}. PTM: Phosphorylation of Ser-371 causes dimer dissociation. Phosphorylation by CK2 promotes interaction with APTX and APLF (By similarity). {ECO:0000250}.; PTM: Sumoylated. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P18887}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P18887}. Note=Moves from the nucleoli to the global nuclear chromatin upon DNA damage. {ECO:0000250|UniProtKB:P18887}. SUBUNIT: Homodimer. Interacts with polynucleotide kinase (PNK), DNA polymerase-beta (POLB) and DNA ligase III (LIG3). Interacts with APTX and APLF. Interacts with APEX1; the interaction is induced by SIRT1 and increases with the acetylated form of APEX1 (By similarity). {ECO:0000250}. +Q2NKI2 VAX1_MOUSE Ventral anterior homeobox 1 338 35,167 Alternative sequence (1); Chain (1); Compositional bias (1); DNA binding (1); Erroneous initiation (1) FUNCTION: Transcription factor that may function in dorsoventral specification of the forebrain. Required for axon guidance and major tract formation in the developing forebrain. May contribute to the differentiation of the neuroretina, pigmented epithelium and optic stalk. {ECO:0000269|PubMed:10421837, ECO:0000269|PubMed:10601035, ECO:0000269|PubMed:21856776, ECO:0000269|PubMed:9636075}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. +Q920R6 VPP4_MOUSE V-type proton ATPase 116 kDa subunit a isoform 4 (V-ATPase 116 kDa isoform a4) (Vacuolar proton translocating ATPase 116 kDa subunit a isoform 4) (Vacuolar proton translocating ATPase 116 kDa subunit a kidney isoform) 833 95,605 Chain (1); Sequence conflict (3); Topological domain (9); Transmembrane (8) TRANSMEM 391 409 Helical. {ECO:0000255}.; TRANSMEM 412 428 Helical. {ECO:0000255}.; TRANSMEM 444 473 Helical. {ECO:0000255}.; TRANSMEM 539 558 Helical. {ECO:0000255}.; TRANSMEM 577 597 Helical. {ECO:0000255}.; TRANSMEM 643 662 Helical. {ECO:0000255}.; TRANSMEM 721 745 Helical. {ECO:0000255}.; TRANSMEM 767 805 Helical. {ECO:0000255}. TOPO_DOM 1 390 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 410 411 Vacuolar. {ECO:0000255}.; TOPO_DOM 429 443 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 474 538 Vacuolar. {ECO:0000255}.; TOPO_DOM 559 576 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 598 642 Vacuolar. {ECO:0000255}.; TOPO_DOM 663 720 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 746 766 Vacuolar. {ECO:0000255}.; TOPO_DOM 806 833 Cytoplasmic. {ECO:0000255}. FUNCTION: Part of the proton channel of the V-ATPase that is involved in normal vectorial acid transport into the urine by the kidney. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Note=Apical immunostaining present in male genital tissue. According to PubMed:11498539, clearly detectable not only on the apical surface of alpha-intercalated cells but also on the basolateral surface of beta cells. SUBUNIT: The V-ATPase is a heteromultimeric enzyme composed of at least thirteen different subunits. It has a membrane peripheral V1 sector for ATP hydrolysis and an integral V0 for proton translocation. The V1 sector comprises subunits A-H, whereas V0 includes subunits a, d, c, c', and c''. TISSUE SPECIFICITY: Specifically expressed in kidney, but not in the heart, brain, spleen, lung, liver, muscle, or testis. Distribution within the kidney appears more widespread than that seen in man. High intensity staining at the surface of intercalated cells, with additional expression in the proximal tubule. +Q9JME9 VTM2B_MOUSE V-set and transmembrane domain-containing protein 2B 285 30,160 Chain (1); Disulfide bond (1); Domain (1); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 264 284 Helical. {ECO:0000255}. TOPO_DOM 29 263 Extracellular. {ECO:0000255}.; TOPO_DOM 285 285 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q8K3G5 VRK3_MOUSE Inactive serine/threonine-protein kinase VRK3 (Serine/threonine-protein pseudokinase VRK3) (Vaccinia-related kinase 3) 453 50,830 Chain (1); Domain (1); Modified residue (5); Motif (1); Sequence conflict (2) FUNCTION: Inactive kinase that suppresses ERK activity by promoting phosphatase activity of DUSP3 which specifically dephosphorylates and inactivates ERK in the nucleus. {ECO:0000269|PubMed:14645249, ECO:0000269|PubMed:16845380}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14645249}. SUBUNIT: Interacts with DUSP3. Interacts with RAN (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in liver, kidney, muscle, thymus, and bone marrow. Weakly expressed in spleen. {ECO:0000269|PubMed:12782311}. +Q9ERF3 WDR61_MOUSE WD repeat-containing protein 61 (Meiotic recombination REC14 protein homolog) [Cleaved into: WD repeat-containing protein 61, N-terminally processed] 305 33,773 Chain (2); Initiator methionine (1); Modified residue (2); Repeat (7); Sequence conflict (2) FUNCTION: Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and is involved in transcriptional elongation, acting both indepentently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1. PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B ubiquitination is proposed to be coupled to transcription. PAF1C is involved in mRNA 3' end formation probably through association with cleavage and poly(A) factors. Required for mono- and trimethylation on histone H3 'Lys-4' (H3K4me3), dimethylation on histone H3 'Lys-79' (H3K4me3). Required for Hox gene transcription. Component of the SKI complex which is thought to be involved in exosome-mediated RNA decay and associates with transcriptionally active genes in a manner dependent on PAF1C (By similarity). {ECO:0000250, ECO:0000269|PubMed:19345177}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Component of the PAF1 complex, which consists of CDC73, PAF1, LEO1, CTR9, RTF1 and WDR61. The PAF1 complex interacts with PHF5A (PubMed:27749823). Within the PAF1 complex interacts directly with PHF5A (PubMed:27749823). Component of the SKI complex which consists of WDR61, SKIV2L and TTC37 (By similarity). {ECO:0000250|UniProtKB:Q9GZS3, ECO:0000269|PubMed:27749823}. +O89116 VTI1A_MOUSE Vesicle transport through interaction with t-SNAREs homolog 1A (Vesicle transport v-SNARE protein Vti1-like 2) (Vti1-rp2) 217 24,986 Chain (1); Coiled coil (2); Helix (5); Topological domain (2); Transmembrane (1); Turn (2) TRANSMEM 193 213 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 1 192 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 214 217 Vesicular. {ECO:0000255}. FUNCTION: V-SNARE that mediates vesicle transport pathways through interactions with t-SNAREs on the target membrane. These interactions are proposed to mediate aspects of the specificity of vesicle trafficking and to promote fusion of the lipid bilayers. Involved in vesicular transport from the late endosomes to the trans-Golgi network. Along with VAMP7, involved in an non-conventional RAB1-dependent traffic route to the cell surface used by KCNIP1 and KCND2. May be concerned with increased secretion of cytokines associated with cellular senescence. {ECO:0000269|PubMed:19138172}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. SUBUNIT: Interacts with distinct SNARE complexes that contain either STX5 or STX6. Interacts with NAPA and, to a lesser extent, with NAPG. Identified in a complex containing STX6, STX12, VAMP4 and VTI1A (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9705316}. +Q6NV72 WDCP_MOUSE WD repeat and coiled-coil-containing protein 663 72,268 Alternative sequence (1); Chain (1); Coiled coil (1); Modified residue (5); Region (1); Repeat (2); Sequence conflict (4) PTM: Phosphorylated on Tyr when associated with HCK. {ECO:0000250|UniProtKB:Q9H6R7}. SUBUNIT: Oligomer. Interacts with HCK (via SH3 domain). {ECO:0000250|UniProtKB:Q9H6R7}. +Q9DB94 WDR53_MOUSE WD repeat-containing protein 53 358 38,642 Chain (1); Repeat (5) +Q91YD9 WASL_MOUSE Neural Wiskott-Aldrich syndrome protein (N-WASP) 501 54,274 Chain (1); Compositional bias (2); Domain (4); Initiator methionine (1); Modified residue (6); Mutagenesis (2) FUNCTION: Regulates actin polymerization by stimulating the actin-nucleating activity of the Arp2/3 complex. Involved in various processes, such as mitosis and cytokinesis, via its role in the regulation of actin polymerization. Together with CDC42, involved in the extension and maintenance of the formation of thin, actin-rich surface projections called filopodia. In addition to its role in the cytoplasm, also plays a role in the nucleus by regulating gene transcription, probably by promoting nuclear actin polymerization (By similarity). Binds to HSF1/HSTF1 and forms a complex on heat shock promoter elements (HSE) that negatively regulates HSP90 expression (PubMed:12871950). Plays a role in dendrite spine morphogenesis (PubMed:25851601). {ECO:0000250|UniProtKB:O00401, ECO:0000269|PubMed:12871950, ECO:0000269|PubMed:25851601}. PTM: Phosphorylation at Ser-239, Tyr-253, Ser-480 and Ser-481 enhances actin polymerization activity. {ECO:0000250|UniProtKB:O00401}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O08816}. Nucleus {ECO:0000269|PubMed:12871950, ECO:0000269|PubMed:14676198}. Cytoplasm {ECO:0000269|PubMed:12871950, ECO:0000269|PubMed:14676198}. Note=Preferentially localized in the cytoplasm when phosphorylated and in the nucleus when unphosphorylated (PubMed:12871950, PubMed:14676198). Exported from the nucleus by an nuclear export signal (NES)-dependent mechanism to the cytoplasm (PubMed:12871950). {ECO:0000269|PubMed:12871950, ECO:0000269|PubMed:14676198}. SUBUNIT: Binds actin and the Arp2/3 complex. Interacts with CDC42 (By similarity). Binds to SH3 domains of GRB2. Interacts with the C-terminal SH3 domain of DNMBP (PubMed:14506234). Interacts with SNX9 (By similarity). Interacts with the WW domains of PRPF40A/FBP11 (PubMed:14697212). Interacts with PTK2/FAK1 (PubMed:14676198). Interacts with PACSIN1, PACSIN2 and PACSIN3 (PubMed:11082044). Interacts with NOSTRIN. Binds to TNK2. Interacts with SNX33. Interacts with NONO (via second RRM domain); the interaction is direct. Component of a multiprotein complex with NONO and SFPQ; associates with the complex via direct interaction with NONO (By similarity). {ECO:0000250|UniProtKB:O00401, ECO:0000250|UniProtKB:Q95107, ECO:0000269|PubMed:11082044, ECO:0000269|PubMed:14506234, ECO:0000269|PubMed:14676198, ECO:0000269|PubMed:14697212}. +Q8BGF3 WDR92_MOUSE WD repeat-containing protein 92 (WD repeat-containing protein Monad) 357 39,790 Chain (1); Repeat (6) FUNCTION: Seems to act as a modulator of apoptosis. {ECO:0000250}. SUBUNIT: Interacts with PIH1D1. {ECO:0000250|UniProtKB:Q96MX6}. +Q3U821 WDR75_MOUSE WD repeat-containing protein 75 (U3 small nucleolar RNA-associated protein 17 homolog) 830 94,037 Chain (1); Cross-link (2); Modified residue (6); Repeat (13); Sequence conflict (2) FUNCTION: Ribosome biogenesis factor. Involved in nucleolar processing of pre-18S ribosomal RNA. Required for optimal pre-ribosomal RNA transcription by RNA polymerase I. {ECO:0000250|UniProtKB:Q8IWA0}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q8IWA0}. SUBUNIT: May be a component of the proposed t-UTP subcomplex of the ribosomal small subunit (SSU) processome containing at least UTP4, WDR43, HEATR1, UTP15, WDR75. {ECO:0000250|UniProtKB:Q8IWA0}. +Q8BGW2 WBP1L_MOUSE WW domain binding protein 1-like (Outcome predictor in acute leukemia 1 homolog) 348 38,347 Alternative sequence (4); Chain (1); Compositional bias (1); Erroneous initiation (2); Erroneous translation (1); Modified residue (1); Sequence conflict (1); Transmembrane (1) TRANSMEM 42 62 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +P97764 WBP1_MOUSE WW domain-binding protein 1 (WBP-1) 304 33,165 Alternative sequence (1); Chain (1); Compositional bias (2); Motif (2); Mutagenesis (2); Sequence conflict (1) SUBUNIT: Binds to the WW domain of YAP1, WWP1 and WWP2. Interacts with WWOX (By similarity). Interacts with NEDD4. {ECO:0000250, ECO:0000269|PubMed:11042109, ECO:0000269|PubMed:7644498}. DOMAIN: The PPxY motif 2 mediates interaction with WWOX (By similarity). Both PPxY motifs mediate interaction with NEDD4. {ECO:0000250, ECO:0000269|PubMed:11042109}. +Q5DQQ6 WFD13_MOUSE WAP four-disulfide core domain protein 13 (WAP four-disulfide core domain 13-like 1) 81 8,798 Chain (1); Disulfide bond (4); Domain (1); Signal peptide (1) FUNCTION: Putative acid-stable proteinase inhibitor. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +P24383 WNT7A_MOUSE Protein Wnt-7a 349 38,974 Chain (1); Disulfide bond (11); Glycosylation (3); Lipidation (1); Region (1); Sequence conflict (2); Signal peptide (1) FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors that functions in the canonical Wnt/beta-catenin signaling pathway (PubMed:18230341, PubMed:20530549, PubMed:23629626). Plays an important role in embryonic development, including dorsal versus ventral patterning during limb development, skeleton development and urogenital tract development (PubMed:7885472, PubMed:9769174, PubMed:9790192). Required for central nervous system (CNS) angiogenesis and blood-brain barrier regulation (PubMed:28803732). Required for normal, sexually dimorphic development of the Mullerian ducts, and for normal fertility in both sexes (PubMed:9790192). Required for normal neural stem cell proliferation in the hippocampus dentate gyrus (PubMed:23629626). Required for normal progress through the cell cycle in neural progenitor cells, for self-renewal of neural stem cells, and for normal neuronal differentiation and maturation (PubMed:23629626). Promotes formation of synapses via its interaction with FZD5 (PubMed:20530549). {ECO:0000269|PubMed:18230341, ECO:0000269|PubMed:20530549, ECO:0000269|PubMed:23629626, ECO:0000269|PubMed:28803732, ECO:0000269|PubMed:7885472, ECO:0000269|PubMed:9769174, ECO:0000269|PubMed:9790192}. PTM: Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition. {ECO:0000250|UniProtKB:P27467, ECO:0000250|UniProtKB:P56704}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000305}. Secreted {ECO:0000305|PubMed:20530549}. SUBUNIT: Forms a soluble 1:1 complex with AFM; this prevents oligomerization and is required for prolonged biological activity (By similarity). The complex with AFM may represent the physiological form in body fluids (By similarity). Interacts with FZD5 (PubMed:18230341, PubMed:20530549). Interacts with PORCN (PubMed:10866835). Interacts (via intrinsically disordered linker region) with RECK; interaction with RECK confers ligand selectivity for Wnt7 in brain endothelial cells and allows these cells to selectively respond to Wnt7 (By similarity). {ECO:0000250|UniProtKB:O00755, ECO:0000269|PubMed:10866835, ECO:0000269|PubMed:18230341, ECO:0000269|PubMed:20530549}. DOMAIN: The intrinsically disordered linker region is required for recognition by RECK in brain endothelial cells. {ECO:0000250|UniProtKB:O00755}. DISEASE: Note=Defects in Wnt7a cause the postaxial hemimelia (px) phenotype that is characterized by limb patterning defects accompanied by Mullerian duct-associated sterility in both sexes. {ECO:0000269|PubMed:9769174}. +Q8CDG3 VCIP1_MOUSE Deubiquitinating protein VCIP135 (EC 3.4.19.12) (Valosin-containing protein p97/p47 complex-interacting protein 1) (Valosin-containing protein p97/p47 complex-interacting protein p135) 1220 134,503 Active site (3); Alternative sequence (2); Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (1); Modified residue (9); Sequence conflict (1) FUNCTION: Acts as a deubiquitinating enzyme. Necessary for VCP-mediated reassembly of Golgi stacks after mitosis. May play a role in VCP-mediated formation of transitional endoplasmic reticulum (tER). Mediates dissociation of the ternary complex containing STX5A, NSFL1C and VCP. Hydrolyzes 'Lys-11'- and 'Lys-48'-linked polyubiquitin chains (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250}. Golgi apparatus, Golgi stack {ECO:0000250}. Note=Associated with Golgi stacks and endoplasmic reticulum. {ECO:0000250}. SUBUNIT: Binds VCP and the ternary complex containing STX5A, NSFL1C and VCP. {ECO:0000250}. +Q91V37 VATO_MOUSE V-type proton ATPase 21 kDa proteolipid subunit (V-ATPase 21 kDa proteolipid subunit) (23 kDa subunit of V-ATPase) (Vacuolar proton pump 21 kDa proteolipid subunit) 205 21,607 Chain (1); Site (1); Topological domain (6); Transmembrane (5) TRANSMEM 4 24 Helical. {ECO:0000255}.; TRANSMEM 52 72 Helical. {ECO:0000255}.; TRANSMEM 91 111 Helical. {ECO:0000255}.; TRANSMEM 138 158 Helical. {ECO:0000255}.; TRANSMEM 176 196 Helical. {ECO:0000255}. TOPO_DOM 1 3 Lumenal. {ECO:0000255}.; TOPO_DOM 25 51 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 73 90 Lumenal. {ECO:0000255}.; TOPO_DOM 112 137 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 159 175 Lumenal. {ECO:0000255}.; TOPO_DOM 197 205 Cytoplasmic. {ECO:0000255}. FUNCTION: Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein. SUBUNIT: Interacts with IFITM3. {ECO:0000269|PubMed:22467717}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11441017}. +Q8BMC1 VATG3_MOUSE V-type proton ATPase subunit G 3 (V-ATPase subunit G 3) (V-ATPase 13 kDa subunit 3) (Vacuolar proton pump subunit G 3) 118 13,749 Chain (1); Coiled coil (1) FUNCTION: Catalytic subunit of the peripheral V1 complex of vacuolar ATPase (V-ATPase). V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'' and d). {ECO:0000250}. TISSUE SPECIFICITY: Kidney. {ECO:0000269|PubMed:12527205}. +P97953 VEGFC_MOUSE Vascular endothelial growth factor C (VEGF-C) (Flt4 ligand) (Flt4-L) (Vascular endothelial growth factor-related protein) (VRP) 415 46,471 Alternative sequence (6); Chain (1); Disulfide bond (5); Glycosylation (3); Propeptide (2); Region (1); Repeat (4); Signal peptide (1) FUNCTION: Growth factor active in angiogenesis, and endothelial cell growth, stimulating their proliferation and migration and also has effects on the permeability of blood vessels. May function in angiogenesis of the venous and lymphatic vascular systems during embryogenesis, and also in the maintenance of differentiated lymphatic endothelium in adults. Binds and activates KDR/VEGFR2 and FLT4/VEGFR3 receptors. {ECO:0000269|PubMed:9012504, ECO:0000269|PubMed:9247316}. PTM: Undergoes a complex proteolytic maturation which generates a variety of processed secreted forms with increased activity toward VEGFR-3, but only the fully processed form could activate VEGFR-2. VEGF-C first form an antiparallel homodimer linked by disulfide bonds. Before secretion, a cleavage occurs between Arg-223 and Ser-224 producing a heterotetramer. The next extracellular step of the processing removes the N-terminal propeptide. Finally the mature VEGF-C is composed mostly of two VEGF homology domains (VHDs) bound by non-covalent interactions (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Homodimer; non-covalent and antiparallel (PubMed:9247316). Interacts with FLT4/VEGFR3; the interaction is required for FLT4/VEGFR3 homodimarization and activation (By similarity). {ECO:0000250|UniProtKB:P49767, ECO:0000269|PubMed:9247316}. TISSUE SPECIFICITY: Expressed in adult heart, brain, spleen, lung, liver, skeletal muscle, kidney, testis and intestine with higher levels in heart, brain and kidney. Isoform 4 levels are very low. Isoform 3 is mostly expressed in liver and has reduced expression level in other tissues. Isoform 2 is mostly expressed in brain and kidney, although a lower level expression in other tissues is also detectable. {ECO:0000269|PubMed:20415667, ECO:0000269|PubMed:9012504, ECO:0000269|PubMed:9247316}. +P35969 VGFR1_MOUSE Vascular endothelial growth factor receptor 1 (VEGFR-1) (EC 2.7.10.1) (Embryonic receptor kinase 2) (Fms-like tyrosine kinase 1) (FLT-1) (Tyrosine-protein kinase receptor FLT) 1333 149,876 Active site (1); Binding site (1); Chain (1); Disulfide bond (6); Domain (8); Glycosylation (12); Modified residue (7); Nucleotide binding (1); Sequence conflict (14); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 760 781 Helical. {ECO:0000255}. TOPO_DOM 23 759 Extracellular. {ECO:0000255}.; TOPO_DOM 782 1333 Cytoplasmic. {ECO:0000255}. FUNCTION: Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFA, VEGFB and PGF, and plays an essential role in the development of embryonic vasculature, the regulation of angiogenesis, cell survival, cell migration, macrophage function, chemotaxis, and cancer cell invasion. May play an essential role as a negative regulator of embryonic angiogenesis by inhibiting excessive proliferation of endothelial cells. Can promote endothelial cell proliferation, survival and angiogenesis in adulthood. Its function in promoting cell proliferation seems to be cell-type specific. Promotes PGF-mediated proliferation of endothelial cells, and proliferation of some types of cancer cells, but does not promote proliferation of normal fibroblasts. Has very high affinity for VEGFA and relatively low protein kinase activity; may function as a negative regulator of VEGFA signaling by limiting the amount of free VEGFA and preventing its binding to KDR. Modulates KDR signaling by forming heterodimers with KDR. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate and the activation of protein kinase C. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, leading to the activation of phosphatidylinositol kinase and the downstream signaling pathway. Mediates activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Phosphorylates SRC, YES1 and PLCG, and may also phosphorylate CBL. Promotes phosphorylation of AKT1 and PTK2/FAK1 (By similarity). {ECO:0000250, ECO:0000269|PubMed:11221852, ECO:0000269|PubMed:14982871, ECO:0000269|PubMed:18583712, ECO:0000269|PubMed:20924106, ECO:0000269|PubMed:7596436, ECO:0000269|PubMed:9689083}. PTM: N-glycosylated. {ECO:0000250}.; PTM: Ubiquitinated after VEGFA-mediated autophosphorylation, leading to proteolytic degradation. {ECO:0000250}.; PTM: Autophosphorylated on tyrosine residues upon ligand binding. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Phosphorylation at Tyr-1169 is important for interaction with PLCG. Phosphorylation at Tyr-1213 is important for interaction with PIK3R1, PTPN11, GRB2, and PLCG. Phosphorylation at Tyr-1328 is important for endocytosis and for interaction with CBL, NCK1 and CRK. Is probably dephosphorylated by PTPRB (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Endosome {ECO:0000250}. Note=Autophosphorylation promotes ubiquitination and endocytosis. {ECO:0000250}. SUBUNIT: Interacts with VEGFA, VEGFB and PGF. Monomer in the absence of bound VEGFA, VEGFB or PGF. Homodimer in the presence of bound VEGFA, VEGFB and PGF. Can also form a heterodimer with KDR. Interacts (tyrosine phosphorylated) with CBL, CRK, GRB2, NCK1, PIK3R1, PLCG, PSEN1 and PTPN11. Probably interacts with PTPRB. Interacts with RACK1. Identified in a complex with CBL and CD2AP (By similarity). {ECO:0000250}. DOMAIN: The second and third Ig-like C2-type (immunoglobulin-like) domains are sufficient for VEGFA binding. {ECO:0000250}. +P40338 VHL_MOUSE von Hippel-Lindau disease tumor suppressor (pVHL) 181 20,770 Chain (1); Helix (1); Region (1) Protein modification; protein ubiquitination. FUNCTION: Involved in the ubiquitination and subsequent proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Seems to act as a target recruitment subunit in the E3 ubiquitin ligase complex and recruits hydroxylated hypoxia-inducible factor (HIF) under normoxic conditions. Involved in transcriptional repression through interaction with HIF1A, HIF1AN and histone deacetylases. Ubiquitinates, in an oxygen-responsive manner, ADRB2 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Nucleus {ECO:0000250}. Note=Colocalizes with ADRB2 at the cell membrane. {ECO:0000250}. SUBUNIT: Component of the VCB (VHL-Elongin BC-CUL2) complex; this complex acts as a ubiquitin-ligase E3 and directs proteasome-dependent degradation of targeted proteins. Interacts with CUL2; this interaction is dependent on the integrity of the trimeric VBC complex. Interacts (via the beta domain) with HIF1A (via the NTAD domain); this interaction mediates degradation of HIF1A in normoxia and, in hypoxia, prevents ubiquitination and degradation of HIF1A by mediating hypoxia-induced translocation to the nucleus, a process which requires a hypoxia-dependent regulatory signal. Interacts with ADRB2; the interaction, in normoxia, is dependent on hydroxylation of ADRB2 and the subsequent VCB-mediated ubiquitination and degradation of ADRB2. Under hypoxia, hydroxylation, interaction with VHL, ubiquitination and subsequent degradation of ADRB2 are dramatically decreased. Interacts with RNF139, USP33 and JADE1 (By similarity). Found in a complex composed of LIMD1, VHL, EGLN1/PHD2, ELOB and CUL2. Interacts with LIMD1 (via LIM zinc-binding 2). Interacts with AJUBA (via LIM domains) and WTIP (via LIM domains) (By similarity). Interacts with EPAS1. Interacts with CARD9 (By similarity). {ECO:0000250}. DOMAIN: The Elongin BC complex binding domain is also known as BC-box with the consensus [APST]-L-x(3)-C-x(3)-[AILV]. +Q8CC88 VWA8_MOUSE von Willebrand factor A domain-containing protein 8 1905 213,421 Alternative sequence (2); Chain (1); Domain (1); Mutagenesis (2); Nucleotide binding (1); Region (1); Sequence conflict (5); Transit peptide (1) FUNCTION: Exhibits ATPase activity in vitro. {ECO:0000269|PubMed:28414126}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:28414126}. SUBUNIT: Monomer (By similarity). Interacts with PEX7. Interacts with PEX5 in a PEX7-dependent manner (By similarity). {ECO:0000250|UniProtKB:A3KMH1}. TISSUE SPECIFICITY: Isoform 1 is predominantly expressed in liver, kidney, pancreas, heart, and skeletal muscle (at protein level). {ECO:0000269|PubMed:28414126}. +Q3U515 VWCE_MOUSE von Willebrand factor C and EGF domain-containing protein 929 97,668 Chain (1); Compositional bias (4); Disulfide bond (9); Domain (10); Glycosylation (3); Sequence conflict (3); Signal peptide (1) FUNCTION: May be a regulatory element in the beta-catenin signaling pathway and a target for chemoprevention of hapatocellular carcinoma. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q9Z0H1 WDR46_MOUSE WD repeat-containing protein 46 (WD repeat-containing protein BING4) 622 69,048 Chain (1); Modified residue (1); Repeat (5) FUNCTION: Scaffold component of the nucleolar structure. Required for localization of DDX21 and NCL to the granular compartment of the nucleolus. {ECO:0000250|UniProtKB:O15213}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:O15213}. SUBUNIT: Interacts with DDX21, NCL, NOP2 and EBNA1BP2. {ECO:0000250|UniProtKB:O15213}. +Q6ZQL4 WDR43_MOUSE WD repeat-containing protein 43 677 75,381 Chain (1); Cross-link (2); Modified residue (6); Repeat (6) FUNCTION: Ribosome biogenesis factor. Involved in nucleolar processing of pre-18S ribosomal RNA. Required for optimal pre-ribosomal RNA transcription by RNA polymerase I. {ECO:0000250|UniProtKB:Q15061}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q15061}. Note=Found predominantly at the fibrillar center. {ECO:0000250|UniProtKB:Q15061}. SUBUNIT: Interacts with UTP4 and UTP15. May be a component of the proposed t-UTP subcomplex of the ribosomal small subunit (SSU) processome containing at least UTP4, WDR43, HEATR1, UTP15, WDR75. {ECO:0000250|UniProtKB:Q15061}. +Q6ZPG2 WDR90_MOUSE WD repeat-containing protein 90 1874 202,972 Alternative sequence (6); Chain (1); Erroneous initiation (1); Modified residue (3); Repeat (21) FUNCTION: Required for efficient primary cilium formation. {ECO:0000250|UniProtKB:Q96KV7}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q96KV7}. +Q80ZK9 WDTC1_MOUSE WD and tetratricopeptide repeats protein 1 677 75,733 Chain (1); Modified residue (2); Repeat (9) Protein modification; protein ubiquitination. FUNCTION: May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex. {ECO:0000250}. +Q571B6 WHAMM_MOUSE WASP homolog-associated protein with actin, membranes and microtubules (WAS protein homology region 2 domain-containing protein 1) (WH2 domain-containing protein 1) 793 88,997 Alternative sequence (2); Chain (1); Coiled coil (3); Compositional bias (1); Domain (2); Erroneous initiation (1); Modified residue (1); Region (3); Sequence caution (2); Sequence conflict (5) FUNCTION: Acts as a nucleation-promoting factor (NPF) that stimulates Arp2/3-mediated actin polymerization both at the Golgi apparatus and along tubular membranes. Involved as a regulator of Golgi positioning and morphology. Its activity in membrane tubulation requires F-actin and interaction with microtubules. Proposed to use coordinated actin-nucleating and microtubule-binding activities of distinct WHAMM molecules to drive membrane tubule elongation; when MT-bound can recruit and remodel membrane vesicles but is prevented to activate the Arp2/3 complex. Required for RhoD-dependent actin reorganization such as in cell adhesion and cell migration (By similarity). Participates in vesicle transport between the reticulum endoplasmic and the Golgi complex. {ECO:0000250|UniProtKB:Q8TF30, ECO:0000269|PubMed:18614018}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8TF30}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250|UniProtKB:Q8TF30}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q8TF30}. Golgi apparatus, cis-Golgi network {ECO:0000250|UniProtKB:Q8TF30}. Note=Localized to a perinuclear compartment near the microtubule-organizing center (MTOC). Also detected on tubulo-vesicular structures in the cell periphery that frequently localized along microtubules. {ECO:0000250|UniProtKB:Q8TF30}. SUBUNIT: Interacts with ACTR3; indicative for an association with the ARP2/3 complex. Associates with microtubules; in vitro binds to tubulin heterodimer in a 1:1 stoichiometry; decorates microtubules with a repeat of 80 A along protofilaments. Interacts with RHOD (in GTP-bound form). {ECO:0000250|UniProtKB:Q8TF30}. DOMAIN: The N-terminal region associates with membranes, the coiled-coil region binds to microtubules and the WH2 domains promotes actin nucleation. {ECO:0000250}. +Q9D0R9 WDR89_MOUSE WD repeat-containing protein 89 386 42,470 Chain (1); Repeat (6) +Q9EPK5 WWTR1_MOUSE WW domain-containing transcription regulator protein 1 (Transcriptional coactivator with PDZ-binding motif) 395 43,620 Alternative sequence (1); Chain (1); Coiled coil (1); Domain (1); Helix (3); Modified residue (5); Motif (1); Mutagenesis (2); Sequence conflict (1) FUNCTION: Transcriptional coactivator which acts as a downstream regulatory target in the Hippo signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. WWTR1 enhances PAX8 and NKX2-1/TTF1-dependent gene activation. Regulates the nuclear accumulation of SMADS and has a key role in coupling them to the transcriptional machinery such as the mediator complex. Regulates embryonic stem-cell self-renewal, promotes cell proliferation and epithelial-mesenchymal transition (By similarity). {ECO:0000250, ECO:0000269|PubMed:11118213}. PTM: Phosphorylated by LATS2 and STK3/MST2. Phosphorylation by LATS2 results in creation of 14-3-3 binding sites, retention in the cytoplasm, and functional inactivation (By similarity). Phosphorylation results in the inhibition of transcriptional coactivation through YWHAZ-mediated nuclear export. {ECO:0000250, ECO:0000269|PubMed:11118213}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11118213}. Cytoplasm {ECO:0000269|PubMed:11118213}. Note=Concentrates along specific portions of the plasma membrane, and accumulates in punctate nuclear bodies. When phosphorylated is retained in cytoplasm by YWHAZ. Can be retained in the nucleus by MED15 (By similarity). {ECO:0000250}. SUBUNIT: Binds to SLC9A3R2 via the PDZ motif at the plasma membrane. Binds to YWHAZ in vivo and in vitro through the phosphoserine-binding motif RSHSSP. Interacts (via coiled-coil domain) with SMAD2 (via MH1 domain), SMAD3 and SMAD4. Interacts with MED15, PAX8 and NKX2-1. Interacts with TEAD1, TEAD2, TEAD3 and TEAD4 (By similarity). {ECO:0000250}. DOMAIN: The PDZ-binding motif is essential for stimulated gene transcription. It localizes the protein into both punctate nuclear foci and plasma membrane-associated complexes.; DOMAIN: Binds to transcription factors via its WW domain. TISSUE SPECIFICITY: Highly expressed in kidney, heart, placenta and lung. {ECO:0000269|PubMed:11118213}. +Q8BXJ8 Z385B_MOUSE Zinc finger protein 385B (Zinc finger protein 533) 482 51,356 Alternative sequence (1); Chain (1); Region (2); Zinc finger (4) FUNCTION: May play a role in p53/TP53-mediated apoptosis. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with p53/TP53; the interaction is direct. {ECO:0000250}. +B2RRF6 Z518A_MOUSE Zinc finger protein 518A 1478 165,604 Chain (1); Compositional bias (1); Cross-link (16); Modified residue (1); Sequence conflict (1); Zinc finger (5) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +B1AX39 ZCHC7_MOUSE Zinc finger CCHC domain-containing protein 7 (TRAMP-like complex RNA-binding factor ZCCHC7) 541 63,000 Alternative sequence (2); Chain (1); Cross-link (12); Modified residue (1); Sequence caution (5); Zinc finger (4) SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. SUBUNIT: Component of a nucleolar TRAMP-like complex, an ATP-dependent exosome regulatory complex consisting of a helicase (MTREX), an oligadenylate polymerase (TENT4B or TENT4A), and a substrate specific RNA-binding factor (ZCCHC7 or ZCCHC8). Several TRAMP-like complexes exist with specific compositions and are associated with nuclear, or nucleolar RNA exosomes (By similarity). {ECO:0000250}. +Q6PGE4 ZF316_MOUSE Zinc finger protein 316 1016 110,812 Chain (1); Domain (1); Zinc finger (15) FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +Q5Y5T2 ZDH18_MOUSE Palmitoyltransferase ZDHHC18 (EC 2.3.1.225) (Zinc finger DHHC domain-containing protein 18) (DHHC-18) 380 41,148 Active site (1); Chain (1); Compositional bias (1); Domain (1); Modified residue (1); Transmembrane (4) TRANSMEM 83 103 Helical. {ECO:0000255}.; TRANSMEM 112 132 Helical. {ECO:0000255}.; TRANSMEM 228 248 Helical. {ECO:0000255}.; TRANSMEM 270 290 Helical. {ECO:0000255}. FUNCTION: Has palmitoyltransferase activity towards HRAS and LCK. {ECO:0000269|PubMed:15603741}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. DOMAIN: The DHHC domain is required for palmitoyltransferase activity. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:15603741}. +Q8BFR6 ZFAN1_MOUSE AN1-type zinc finger protein 1 (Zinc finger AN1-type-containing protein 1) 268 30,203 Beta strand (2); Chain (1); Helix (3); Metal binding (8); Region (1); Sequence conflict (1); Turn (3); Zinc finger (2) FUNCTION: Plays a role in the regulation of cytoplasmic stress granules (SGs) turnover. SGs are dynamic and transient cytoplasmic ribonucleoprotein assemblies important for cellular protein homeostasis when protein production is suspended after acute exogenous stress. Associates with SGs and is involved in the efficient and specific arsenite-induced clearance process of SGs through the recruitment of the ubiquitin-selective ATPase VCP and the 26S proteasome. This process requires both complexes for efficient degradation of damaged ubiquitinated SG proteins during recovery from arsenite stress, and hence avoiding aberrant cytoplasmic SGs degradation via autophagy. {ECO:0000250|UniProtKB:Q8TCF1}. SUBCELLULAR LOCATION: Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q8TCF1}. Note=Colocalizes with TIA1, G3BP1, VCP and 26S proteasome in cytoplasmic stress granules (SGs) in response to arsenite-induced stress treatment in a VCP-independent manner. Not localized in SGs in response to other heat- oxidative- or osmotic-induced stress treatments. Colocalizes with VCP in cytoplasmic speckles. {ECO:0000250|UniProtKB:Q8TCF1}. SUBUNIT: Associates with the 26S proteasome; this association occurs upon exposure to arsenite and is reduced in the presence of ATP. Interacts (via AN1-type 1 and 2 zinc fingers) with PSMD1; this interaction is increased upon arsenite treatment and occurs in an ATP-independent manner. Interacts with PSMC4. Interacts with PSMA1. Interacts (via its ubiquitin-like region) with VCP; this interaction occurs in an arsenite-dependent manner and is necessary for the recruitment of the ubiquitin-selective ATPase VCP to stress granules (SGs). {ECO:0000250|UniProtKB:Q8TCF1}. DOMAIN: The ubiquitin-like region is necessary for its localization to stress granules (SGs) in a VCP-independent manner. The AN1-type 1 and 2 zinc finger domains are necessary for the recruitment of the 26S proteasome to SGs. Both the AN1-type 1 and 2 zinc finger domains and the ubiquitin-like region are necessary for efficient SGs clearance upon specific arsenite-induced responses. {ECO:0000250|UniProtKB:Q8TCF1}. +Q8VDM1 ZGPAT_MOUSE Zinc finger CCCH-type with G patch domain-containing protein 511 56,411 Chain (1); Compositional bias (1); Domain (1); Erroneous gene model prediction (1); Modified residue (5); Sequence caution (1); Sequence conflict (2); Zinc finger (1) FUNCTION: Transcription repressor that specifically binds the 5'-GGAG[GA]A[GA]A-3' consensus sequence. Represses transcription by recruiting the chromatin multiprotein complex NuRD to target promoters. Negatively regulates expression of EGFR, a gene involved in cell proliferation, survival and migration. Its ability to repress genes of the EGFR pathway suggest it may act as a tumor suppressor (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with CHD4/Mi-2; the interaction is direct. {ECO:0000250}. +Q8VC90 ZDH12_MOUSE Probable palmitoyltransferase ZDHHC12 (EC 2.3.1.225) (Zinc finger DHHC domain-containing protein 12) (DHHC-12) 267 30,708 Active site (1); Alternative sequence (1); Chain (1); Domain (1); Frameshift (1); Sequence conflict (2); Transmembrane (4) TRANSMEM 10 30 Helical. {ECO:0000255}.; TRANSMEM 44 64 Helical. {ECO:0000255}.; TRANSMEM 141 161 Helical. {ECO:0000255}.; TRANSMEM 179 199 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. DOMAIN: The DHHC domain is required for palmitoyltransferase activity. {ECO:0000250}. +A0PK84 ZDH22_MOUSE Palmitoyltransferase ZDHHC22 (EC 2.3.1.225) (Zinc finger DHHC domain-containing protein 22) (DHHC-22) (zDHHC22) 263 29,318 Chain (1); Domain (1); Transmembrane (2) TRANSMEM 10 30 Helical. {ECO:0000255}.; TRANSMEM 49 69 Helical. {ECO:0000255}. FUNCTION: Palmitoyltransferase that mediates palmitoylation of KCNMA1, regulating localization of KCNMA1 to the plasma membrane (By similarity). Might also mediate palmitoylation of CNN3 (PubMed:29287726). {ECO:0000250|UniProtKB:Q8N966, ECO:0000305|PubMed:29287726}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Interacts with CNN3. {ECO:0000269|PubMed:29287726}. DOMAIN: The DHHC domain is required for palmitoyltransferase activity. {ECO:0000250}. +Q2MHN3 ZFHX2_MOUSE Zinc finger homeobox protein 2 (Zinc finger homeodomain protein 5) 2562 273,485 Chain (1); Compositional bias (7); DNA binding (3); Erroneous initiation (1); Mutagenesis (1); Sequence conflict (1); Zinc finger (13) FUNCTION: Transcriptional regulator that is critical for the regulation of pain perception and processing of noxious stimuli. {ECO:0000269|PubMed:29253101}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29253101}. TISSUE SPECIFICITY: Expressed in brain (at protein level) (PubMed:23300874). Expressed at the highest levels in the pyramidal cell layer of the hippocampus, the suprachiasmatic nucleus, laterodorsal thalamic nucleus, lateral geniculate nucleus, substantia nigra pars compacta, and magnocellular part of the red nucleus (at protein level) (PubMed:23300874). Higly expressed in dorsal root ganglia (PubMed:29253101). Expressed at lower levels in kidney, stomach, liver, heart and testis (PubMed:16257534, PubMed:23300874). {ECO:0000269|PubMed:16257534, ECO:0000269|PubMed:23300874, ECO:0000269|PubMed:29253101}. +Q64321 ZBT7B_MOUSE Zinc finger and BTB domain-containing protein 7B (Krueppel-related zinc finger protein cKrox) (c-Krox) (T-helper-inducing POZ/Krueppel-like factor) (Zinc finger protein 67) (Zfp-67) (Zinc finger protein Th-POK) 544 58,918 Chain (1); Compositional bias (1); Cross-link (3); Domain (1); Frameshift (2); Modified residue (5); Mutagenesis (7); Natural variant (2); Region (1); Sequence caution (2); Sequence conflict (2); Zinc finger (4) FUNCTION: Transcription regulator that acts as a key regulator of lineage commitment of immature T-cell precursors. Exerts distinct biological functions in the mammary epithelial cells and T cells in a tissue-specific manner (PubMed:15729333, PubMed:29420538). Necessary and sufficient for commitment of CD4 lineage, while its absence causes CD8 commitment. Development of immature T-cell precursors (thymocytes) to either the CD4 helper or CD8 killer T-cell lineages correlates precisely with their T-cell receptor specificity for major histocompatibility complex class II or class I molecules, respectively. Cross-antagonism between ZBTB7B and CBF complexes are determinative to CD4 versus CD8 cell fate decision (PubMed:15729333, PubMed:24880459, PubMed:18258917, PubMed:23481257). Suppresses RUNX3 expression and imposes CD4+ lineage fate by inducing the SOCS suppressors of cytokine signaling. induces, as a transcriptional activator, SOCS genes expression which represses RUNX3 expression and promotes the CD4+ lineage fate (PubMed:24880459). During CD4 lineage commitment, associates with multiple sites at the CD8 locus, acting as a negative regulator of the CD8 promoter and enhancers by epigenetic silencing through the recruitment of class II histone deacetylases, such as HDAC4 and HDAC5, to these loci (PubMed:22730529). Regulates the development of IL17-producing CD1d-restricted naural killer (NK) T cells (PubMed:23105140). Also functions as an important metabolic regulator in the lactating mammary glands. Critical feed-forward regulator of insulin signaling in mammary gland lactation, directly regulates expression of insulin receptor substrate-1 (IRS-1) and insulin-induced Akt-mTOR-SREBP signaling (PubMed:29420538). Transcriptional repressor of the collagen COL1A1 and COL1A2 genes. May also function as a repressor of fibronectin and possibly other extracellular matrix genes (PubMed:7937772). Potent driver of brown fat development, thermogenesis and cold-induced beige fat formation (PubMed:28784777). Recruits the brown fat lncRNA 1 (Blnc1):HNRNPU ribonucleoprotein complex to activate thermogenic gene expression in brown and beige adipocytes (PubMed:28784777). {ECO:0000269|PubMed:15729333, ECO:0000269|PubMed:18258917, ECO:0000269|PubMed:22730529, ECO:0000269|PubMed:23105140, ECO:0000269|PubMed:23481257, ECO:0000269|PubMed:24880459, ECO:0000269|PubMed:28784777, ECO:0000269|PubMed:29420538, ECO:0000269|PubMed:7937772}. PTM: Acetylated directly and specifically by EP300. EP300-mediated acetylation of Lys-210, Lys-216 and Lys-339 stabilizes the protein by antagonizing ubiquitin conjugation. {ECO:0000269|PubMed:20810990}.; PTM: Ubiquitinated, leading to proteasomal degradation. Competes with acetylation on Lys-210, Lys-216 and Lys-339. {ECO:0000269|PubMed:20810990}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22730529, ECO:0000269|PubMed:29420538}. SUBUNIT: Homodimerizes (PubMed:22730529). Interacts with NCL, NEDD4 and YBX1 (PubMed:28784777). Interacts with HNRNPU (via RNA-binding RGG-box region); the interaction facilitates the recruitment of long non-coding RNA Blnc1 by ZBTB7B (PubMed:28784777). Interacts with HDAC4 and HDAC5; the interaction allows the recruitment of HDAC4 and HDAC5 on CD8 loci for deacetylation and possible inhibition of CD8 genes expression (PubMed:22730529). {ECO:0000269|PubMed:22730529, ECO:0000269|PubMed:28784777}. TISSUE SPECIFICITY: Widely expressed, with a higher level in skin. Expressed in thymus. Restricted to CD4 cells (mature single positive CD4(+) and intermediate CD4(+)CD8(+) cells). Expressed in the luminal epithelial cells in the mammary glands where is up-regulated at late pregnancy and lactation (PubMed:29420538). Expression is enriched in brown fat (PubMed:28784777). {ECO:0000269|PubMed:15729333, ECO:0000269|PubMed:28784777, ECO:0000269|PubMed:29420538, ECO:0000269|PubMed:7937772}. DISEASE: Note=Defects in Zbtb7b are the cause of helper deficient disease (HD) or helpless disease. HD and helpless mice are distinguished by the virtual absence of peripheral T-cells of the CD4(+)CD8(-) major histocompatibility complex (MHC) class II-restricted T-helper subset due to a specific block in thymic development. The developmental defect is selective for CD4(+)CD8(-) cells; the maturation of CD4(-)CD8(+) and gamma delta T-cells is normal indicating that lineage commitment is specifically perturbed without affecting positive selection. In helpless disease, NKT cells are hyperproliferative, most lack CD4 and instead express CD8. The majority of NKT cells in the thymus produce IL17 with high frequency while very few produce IFNG or other cytokines (PubMed:23105140). {ECO:0000269|PubMed:15729333, ECO:0000269|PubMed:22730529, ECO:0000269|PubMed:23105140, ECO:0000269|PubMed:24880459}. +Q8VCZ7 ZBT7C_MOUSE Zinc finger and BTB domain-containing protein 7C (Zinc finger and BTB domain-containing protein 36) 619 69,086 Chain (1); Compositional bias (3); Domain (1); Zinc finger (4) FUNCTION: May be a tumor suppressor gene. {ECO:0000250}. +Q9CWH1 ZBT8A_MOUSE Zinc finger and BTB domain-containing protein 8A 434 49,151 Chain (1); Compositional bias (1); Cross-link (4); Domain (1); Modified residue (2); Sequence conflict (1); Zinc finger (2) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q8C0C0 ZHX2_MOUSE Zinc fingers and homeoboxes protein 2 (Alpha-fetoprotein regulator 1) (AFP regulator 1) (Regulator of AFP) (Zinc finger and homeodomain protein 2) 836 92,259 Chain (1); Cross-link (2); DNA binding (4); Modified residue (2); Region (5); Sequence conflict (4); Zinc finger (2) FUNCTION: Acts as a transcriptional repressor (PubMed:19515908). Represses the promoter activity of the CDC25C gene stimulated by NFYA (By similarity). May play a role in retinal development where it regulates the composition of bipolar cell populations, by promoting differentiation of bipolar OFF-type cells (PubMed:30146259). In the brain, may promote maintenance and suppress differentiation of neural progenitor cells in the developing cortex (PubMed:19515908). {ECO:0000250|UniProtKB:Q9Y6X8, ECO:0000269|PubMed:19515908, ECO:0000269|PubMed:30146259}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:17056598, ECO:0000269|PubMed:19515908, ECO:0000269|PubMed:30146259}. Note=Colocalizes with EFNB1 intracellular domain in the nucleus. {ECO:0000269|PubMed:19515908}. SUBUNIT: Homodimer (via homeobox domain 1) (By similarity). Heterodimer with ZHX1 (via homeobox domain 1) (By similarity). Heterodimer with ZHX3 (via homeobox domain 1) (By similarity). Heterodimerization with ZHX1 is not necessary for repressor activity (By similarity). Interacts (via homeobox domain) with NFYA (via N-terminus) (By similarity). Interacts with EFNB1 intracellular domain peptide; the interaction enhances ZHX2 transcriptional repression activity (PubMed:19515908). {ECO:0000250|UniProtKB:Q9Y6X8, ECO:0000269|PubMed:19515908}. TISSUE SPECIFICITY: Expressed in retina where it localizes to Muller glial cells of the inner nuclear layer (at protein level) (PubMed:30146259). Detected in heart, brain, spleen, lung, liver, skeletal muscle, kidney and testis (PubMed:14659886). {ECO:0000269|PubMed:14659886, ECO:0000269|PubMed:30146259}. +Q9DCK4 ZN414_MOUSE Zinc finger protein 414 299 31,988 Alternative sequence (1); Chain (1); Zinc finger (3) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q6P560 ZN182_MOUSE Zinc finger protein 182 (Zinc finger protein 21) 627 72,439 Chain (1); Domain (1); Sequence conflict (2); Zinc finger (14) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q80W31 ZN569_MOUSE Zinc finger protein 569 (Mszf21) (Zinc finger protein 74) (Zfp-74) 679 77,248 Chain (1); Domain (1); Sequence conflict (2); Zinc finger (18) FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +Q8BI66 ZN526_MOUSE Zinc finger protein 526 675 73,971 Alternative sequence (2); Chain (1); Compositional bias (3); Erroneous initiation (1); Frameshift (1); Sequence caution (1); Sequence conflict (1); Zinc finger (13) FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q4VA44 ZN664_MOUSE Zinc finger protein 664 261 30,326 Chain (1); Cross-link (1); Zinc finger (9) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q6NXK2 ZN532_MOUSE Zinc finger protein 532 1036 110,949 Alternative sequence (1); Chain (1); Compositional bias (1); Cross-link (4); Erroneous initiation (1); Modified residue (8); Zinc finger (6) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q80VM4 ZN579_MOUSE Zinc finger protein 579 562 60,792 Chain (1); Compositional bias (2); Modified residue (3); Zinc finger (8) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q80YY7 ZN618_MOUSE Zinc finger protein 618 953 104,866 Alternative sequence (3); Chain (1); Compositional bias (1); Cross-link (4); Frameshift (1); Modified residue (1); Sequence conflict (1); Zinc finger (4) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q6NS86 ZN366_MOUSE Zinc finger protein 366 (Dendritic cell-specific transcript protein) (DC-SCRIPT) 746 84,826 Chain (1); Compositional bias (1); Motif (1); Region (1); Zinc finger (11) FUNCTION: Has transcriptional repression activity. Acts as corepressor of ESR1; the function seems to involve CTBP1 and histone deacetylases. {ECO:0000250|UniProtKB:Q8N895}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16522745}. SUBUNIT: Interacts with ESR1 and NRIP1. Interacts (via PXDLS motif) with CTBP1. {ECO:0000250|UniProtKB:Q8N895}. TISSUE SPECIFICITY: Expressed in immature and mature dendritic cells (DCs). {ECO:0000269|PubMed:16522745}. +Q8BGG0 ZNT8_MOUSE Zinc transporter 8 (ZnT-8) (Solute carrier family 30 member 8) 367 40,223 Chain (1); Motif (1); Topological domain (7); Transmembrane (6) TRANSMEM 79 99 Helical. {ECO:0000255}.; TRANSMEM 103 123 Helical. {ECO:0000255}.; TRANSMEM 140 160 Helical. {ECO:0000255}.; TRANSMEM 175 195 Helical. {ECO:0000255}.; TRANSMEM 217 237 Helical. {ECO:0000255}.; TRANSMEM 245 265 Helical. {ECO:0000255}. TOPO_DOM 1 78 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 100 102 Extracellular. {ECO:0000255}.; TOPO_DOM 124 139 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 161 174 Extracellular. {ECO:0000255}.; TOPO_DOM 196 216 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 238 244 Extracellular. {ECO:0000255}.; TOPO_DOM 266 367 Cytoplasmic. {ECO:0000255}. FUNCTION: Facilitates the accumulation of zinc from the cytoplasm into intracellular vesicles, being a zinc-efflux transporter. May be a major component for providing zinc to insulin maturation and/or storage processes in insulin-secreting pancreatic beta-cells (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Associated with the insulin and glucagon secretory granules. {ECO:0000269|PubMed:19095428}. SUBUNIT: Homodimer. DOMAIN: Contains a histidine-rich region, HXXXXXHNH-motif, which is a ligand for zinc. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in endocrine pancreatic islet alpha and beta cells. Not detected in the brain. {ECO:0000269|PubMed:16984975, ECO:0000269|PubMed:18250168, ECO:0000269|PubMed:19095428}. +Q9Z1D9 ZN394_MOUSE Zinc finger protein 394 (Zinc finger protein 94) (Zfp-94) (Zinc finger protein with KRAB and SCAN domains 14) 521 59,038 Chain (1); Cross-link (3); Domain (2); Frameshift (1); Sequence conflict (6); Zinc finger (7) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}. TISSUE SPECIFICITY: Expressed at high level in testis. {ECO:0000269|PubMed:12860387}. +G3X9G7 ZN809_MOUSE Zinc finger protein 809 402 46,942 Alternative sequence (2); Chain (1); Domain (1); Sequence conflict (1); Zinc finger (7) FUNCTION: Transcription factor specifically required to repress retrotransposons in embryonic stem cells. Recognizes and binds retroviral DNA sequences from a large subset of mammalian retroviruses and retroelements and repress their expression by recruiting a repressive complex containing TRIM28/KAP1 (PubMed:19270682). {ECO:0000269|PubMed:19270682}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q9ERU3 ZNF22_MOUSE Zinc finger protein 22 (Zinc finger protein 422) (Zinc finger protein Krox-25) (Zinc finger protein Krox-26) 237 27,294 Chain (1); Frameshift (1); Modified residue (2); Sequence conflict (6); Zinc finger (5) FUNCTION: Binds DNA through the consensus sequence 5'-CAATG-3'. May be involved in transcriptional regulation and may play a role in tooth formation. {ECO:0000269|PubMed:12952191, ECO:0000303|PubMed:12489153}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. TISSUE SPECIFICITY: Expressed predominantly in developing craniofacial bones and dental organs, and in molar tooth germs of postnatal animals. Also detected in embryonic heart, liver, thymus, kidney, brain, lung, muscle and calvaria. In the adult, highly expressed in lung, kidney, bone and incisors. {ECO:0000269|PubMed:12489153, ECO:0000269|PubMed:12952191, ECO:0000269|PubMed:14706453}. +P24399 ZN239_MOUSE Zinc finger protein 239 (Zfp-239) (Zinc finger protein MOK-2) 201 22,818 Chain (1); Sequence conflict (1); Zinc finger (7) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: Preferentially expressed in transformed mouse cells. +P97441 ZNT3_MOUSE Zinc transporter 3 (ZnT-3) (Solute carrier family 30 member 3) 388 41,824 Chain (1); Modified residue (2); Topological domain (7); Transmembrane (6) TRANSMEM 76 96 Helical. {ECO:0000255}.; TRANSMEM 106 126 Helical. {ECO:0000255}.; TRANSMEM 146 166 Helical. {ECO:0000255}.; TRANSMEM 178 198 Helical. {ECO:0000255}.; TRANSMEM 236 256 Helical. {ECO:0000255}.; TRANSMEM 264 284 Helical. {ECO:0000255}. TOPO_DOM 1 75 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 97 105 Vacuolar. {ECO:0000255}.; TOPO_DOM 127 145 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 167 177 Vacuolar. {ECO:0000255}.; TOPO_DOM 199 235 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 257 263 Vacuolar. {ECO:0000255}.; TOPO_DOM 285 388 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in accumulation of zinc in synaptic vesicles. {ECO:0000269|PubMed:8962159}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000305|PubMed:21998198}; Multi-pass membrane protein {ECO:0000305|PubMed:21998198}. Cell junction, synapse, synaptosome {ECO:0000269|PubMed:21998198}. Late endosome membrane {ECO:0000250|UniProtKB:Q99726}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:Q99726}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250|UniProtKB:Q99726}. TISSUE SPECIFICITY: Brain and testis. In the brain, most abundant in hippocampus and cerebral cortex. In the testis, expression is restricted to germ cells and is highest in pachytene spermatocytes and round spermatids. {ECO:0000269|PubMed:8962159}. +Q8R0T2 ZN768_MOUSE Zinc finger protein 768 568 62,711 Chain (1); Compositional bias (1); Modified residue (13); Zinc finger (10) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +P10761 ZP3_MOUSE Zona pellucida sperm-binding protein 3 (Sperm receptor) (Zona pellucida glycoprotein 3) (Zp-3) (Zona pellucida protein C) [Cleaved into: Processed zona pellucida sperm-binding protein 3] 424 46,304 Beta strand (9); Chain (2); Disulfide bond (4); Domain (1); Glycosylation (10); Helix (2); Modified residue (1); Mutagenesis (4); Propeptide (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 388 408 Helical. {ECO:0000255}. TOPO_DOM 23 387 Extracellular.; TOPO_DOM 409 424 Cytoplasmic. FUNCTION: The mammalian zona pellucida, which mediates species-specific sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy, is composed of three to four glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP3 is essential for sperm binding and zona matrix formation. PTM: Proteolytically cleaved before the transmembrane segment to yield the secreted ectodomain incorporated in the zona pellucida.; PTM: O-glycosylated; removal of O-linked glycans may play an important role in the post-fertilization block to polyspermy. {ECO:0000269|PubMed:12799386}.; PTM: Cys-320, Cys-322, Cys-323 and Cys-328 are involved in two additional disulfide bonds. SUBCELLULAR LOCATION: Processed zona pellucida sperm-binding protein 3: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:19052627}. Note=The glycoproteinaceous translucent extracellular matrix that surrounds the mammalian oocyte is called zona pellucida. {ECO:0000305}.; SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19052627}; Single-pass type I membrane protein {ECO:0000255}. SUBUNIT: Polymers of ZP2 and ZP3 organized into long filaments cross-linked by ZP1 homodimers. Interacts with ZP1 and ZP2. {ECO:0000250|UniProtKB:P20239, ECO:0000250|UniProtKB:P21754}. DOMAIN: The ZP domain is involved in the polymerization of the ZP proteins to form the zona pellucida. TISSUE SPECIFICITY: Oocytes. +Q62513 ZN260_MOUSE Zinc finger protein 260 (Zfp-260) 407 46,443 Chain (1); Sequence conflict (4); Zinc finger (13) FUNCTION: Transcription factor that acts as a cardiac regulator and an effector of alpha1-adrenergic signaling. Binds to PE response elements (PERE) present in the promoter of genes such as ANF/NPPA and acts as a direct transcriptional activator of NPPA. Also acts as a cofactor with GATA4, a key cardiac regulator. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Binds DNA. Interacts with GATA4 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Predominantly present in heart. Outside the heart, it is detected in embryonic and postnatal vascular smooth muscle cells and in epithelial cells of the lung, gut and kidney at sites of epithelial morphogenesis and in the spinal cord (at protein level). {ECO:0000269|PubMed:10449921, ECO:0000269|PubMed:16166646}. +Q3URS2 ZSC4F_MOUSE Zinc finger and SCAN domain containing protein 4F 506 57,648 Chain (1); Domain (1); Sequence conflict (1); Zinc finger (4) FUNCTION: Transcription factor required to regulate early development. Binds telomeres and plays a key role in genomic stability by regulating telomere elongation. Acts as an activator of spontaneous telomere sister chromatid exchange (T-SCE) and telomere elongation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}. Chromosome, telomere {ECO:0000250}. TISSUE SPECIFICITY: Up-regulated in blastocyst outgrowths and is detectable in a mosaic fashion in ES cultures. {ECO:0000269|PubMed:17553482}. +Q8R0E5 ZRAS1_MOUSE Putative uncharacterized protein ZNRD1-AS1 (T-complex testis-expressed protein 4) (ZNRD1 antisense RNA 1) (ZNRD1 antisense gene protein 1) 213 25,489 Chain (1); Erroneous initiation (2); Frameshift (1); Sequence conflict (1) FUNCTION: May be involved in male sterility. {ECO:0000269|PubMed:1718647}. TISSUE SPECIFICITY: Specifically expressed in testis. {ECO:0000269|PubMed:1718647}. +Q60931 VDAC3_MOUSE Voltage-dependent anion-selective channel protein 3 (VDAC-3) (mVDAC3) (Outer mitochondrial membrane protein porin 3) 283 30,753 Chain (1); Cross-link (4); Initiator methionine (1); Modified residue (8); Nucleotide binding (2); Sequence conflict (2); Transmembrane (19) TRANSMEM 26 35 Beta stranded. {ECO:0000250}.; TRANSMEM 39 47 Beta stranded. {ECO:0000250}.; TRANSMEM 54 64 Beta stranded. {ECO:0000250}.; TRANSMEM 69 76 Beta stranded. {ECO:0000250}.; TRANSMEM 80 89 Beta stranded. {ECO:0000250}.; TRANSMEM 95 104 Beta stranded. {ECO:0000250}.; TRANSMEM 111 120 Beta stranded. {ECO:0000250}.; TRANSMEM 123 130 Beta stranded. {ECO:0000250}.; TRANSMEM 137 145 Beta stranded. {ECO:0000250}.; TRANSMEM 150 158 Beta stranded. {ECO:0000250}.; TRANSMEM 163 175 Beta stranded. {ECO:0000250}.; TRANSMEM 178 185 Beta stranded. {ECO:0000250}.; TRANSMEM 189 198 Beta stranded. {ECO:0000250}.; TRANSMEM 202 211 Beta stranded. {ECO:0000250}.; TRANSMEM 218 227 Beta stranded. {ECO:0000250}.; TRANSMEM 231 238 Beta stranded. {ECO:0000250}.; TRANSMEM 242 251 Beta stranded. {ECO:0000250}.; TRANSMEM 254 263 Beta stranded. {ECO:0000250}.; TRANSMEM 273 282 Beta stranded. {ECO:0000250}. FUNCTION: Forms a channel through the mitochondrial outer membrane that allows diffusion of small hydrophilic molecules. {ECO:0000250}. PTM: Ubiquitinated by PRKN during mitophagy, leading to its degradation and enhancement of mitophagy. Deubiquitinated by USP30. {ECO:0000250|UniProtKB:Q9Y277}. SUBCELLULAR LOCATION: Mitochondrion outer membrane. DOMAIN: Consists mainly of a membrane-spanning beta-barrel formed by 19 beta-strands. {ECO:0000250}. TISSUE SPECIFICITY: Highest levels of expression detected in testis, less but still abundant expression in heart, kidney, brain, and skeletal muscle. +P27870 VAV_MOUSE Proto-oncogene vav (p95vav) 845 98,137 Beta strand (22); Chain (1); Compositional bias (1); Domain (6); Helix (20); Modified residue (2); Mutagenesis (3); Sequence conflict (2); Turn (8); Zinc finger (1) FUNCTION: Couples tyrosine kinase signals with the activation of the Rho/Rac GTPases, thus leading to cell differentiation and/or proliferation. PTM: Phosphorylated by FYN (By similarity). Phosphorylated on tyrosine residues by HCK in response to IFNG and bacterial lipopolysaccharide (LPS). {ECO:0000250, ECO:0000269|PubMed:10646608, ECO:0000269|PubMed:10646609, ECO:0000269|PubMed:9400828}. SUBUNIT: Interacts with SHB (By similarity). Interacts with APS, DOCK2, GRB2, GRB3, DOCK2, SLA, TEC and ZNF655/VIK. Interacts with SIAH2; without leading to its degradation. Associates with BLNK, PLCG1, GRB2 and NCK1 in a B-cell antigen receptor-dependent fashion. Interacts with CBLB; which inhibits tyrosine phosphorylation and down-regulates activity (PubMed:10646609, PubMed:10646608). May interact with CCPG1 (PubMed:17000758). Interacts with CLNK (PubMed:11463797). Interacts with THEMIS2 (PubMed:20644716). Interacts with NEK3 and this interaction is prolactin-dependent. Interacts with ITK. Interacts with PTK2B/PYK2 (By similarity). Interacts with HCK. Interacts with PTK2B/PYK2. Interacts (via SH2 domain) with SYK (By similarity). Interacts with ANKRD54 (PubMed:19064729). Interacts with CD6 (PubMed:24584089). {ECO:0000250|UniProtKB:P15498, ECO:0000269|PubMed:10646608, ECO:0000269|PubMed:10646609, ECO:0000269|PubMed:10662792, ECO:0000269|PubMed:11463797, ECO:0000269|PubMed:19064729, ECO:0000269|PubMed:20644716, ECO:0000269|PubMed:24584089, ECO:0000269|PubMed:8877094, ECO:0000269|PubMed:9400828}. DOMAIN: The DH domain is involved in interaction with CCPG1. TISSUE SPECIFICITY: Widely expressed in hematopoietic cells but not in other cell types. Found in the spleen and lung. {ECO:0000269|PubMed:2069873}. +Q5SXG7 VMO1_MOUSE Vitelline membrane outer layer protein 1 homolog 201 21,957 Chain (1); Disulfide bond (4); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +Q78T54 VMA21_MOUSE Vacuolar ATPase assembly integral membrane protein Vma21 101 11,365 Alternative sequence (1); Chain (1); Topological domain (3); Transmembrane (2) TRANSMEM 26 46 Helical. {ECO:0000255|HAMAP-Rule:MF_03058}.; TRANSMEM 66 86 Helical. {ECO:0000255|HAMAP-Rule:MF_03058}. TOPO_DOM 1 25 Cytoplasmic. {ECO:0000255|HAMAP-Rule:MF_03058}.; TOPO_DOM 47 65 Lumenal. {ECO:0000255|HAMAP-Rule:MF_03058}.; TOPO_DOM 87 101 Cytoplasmic. {ECO:0000255|HAMAP-Rule:MF_03058}. FUNCTION: Required for the assembly of the V0 complex of the vacuolar ATPase (V-ATPase) in the endoplasmic reticulum. {ECO:0000255|HAMAP-Rule:MF_03058}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03058}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03058}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000255|HAMAP-Rule:MF_03058}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03058}. Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000255|HAMAP-Rule:MF_03058}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03058}. SUBUNIT: Associates with the V0 complex of the vacuolar ATPase (V-ATPase). {ECO:0000255|HAMAP-Rule:MF_03058}. +Q9Z0K8 VNN1_MOUSE Pantetheinase (EC 3.5.1.92) (Pantetheine hydrolase) (Vascular non-inflammatory molecule 1) (Vanin-1) 512 57,091 Active site (3); Chain (1); Domain (1); Glycosylation (4); Lipidation (1); Propeptide (1); Sequence conflict (4); Signal peptide (1) FUNCTION: Amidohydrolase that hydrolyzes specifically one of the carboamide linkages in D-pantetheine thus recycling pantothenic acid (vitamin B5) and releasing cysteamine. {ECO:0000269|PubMed:11042271}. PTM: N-glycosylated. {ECO:0000269|PubMed:8934567}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:11042271, ECO:0000305|PubMed:8934567}; Lipid-anchor, GPI-anchor {ECO:0000305|PubMed:11042271, ECO:0000305|PubMed:8934567}. SUBUNIT: Monomer. {ECO:0000250|UniProtKB:O95497}. TISSUE SPECIFICITY: Detected in kidney (at protein level). Ubiquitous. {ECO:0000269|PubMed:11042271}. +Q8C0E2 VP26B_MOUSE Vacuolar protein sorting-associated protein 26B (Vesicle protein sorting 26B) 336 39,125 Alternative sequence (1); Beta strand (22); Chain (1); Helix (2); Modified residue (3); Mutagenesis (8); Turn (3) FUNCTION: Acts as component of the retromer cargo-selective complex (CSC) (PubMed:21040701, PubMed:21920005). The CSC is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway. The recruitment of the CSC to the endosomal membrane involves RAB7A and SNX3. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX3-retromer mediates the retrograde transport of WLS distinct from the SNX-BAR retromer pathway. The SNX27-retromer is believed to be involved in endosome-to-plasma membrane trafficking and recycling of a broad spectrum of cargo proteins. The CSC seems to act as recruitment hub for other proteins, such as the WASH complex and TBC1D5 (By similarity). May be involved in retrograde transport of SORT1 but not of IGF2R (PubMed:21040701). Acts redundantly with VSP26A in SNX-27 mediated endocytic recycling of SLC2A1/GLUT1 (PubMed:25136126). {ECO:0000250|UniProtKB:O75436, ECO:0000269|PubMed:21040701, ECO:0000269|PubMed:21920005, ECO:0000269|PubMed:25136126}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16190980}. Membrane {ECO:0000269|PubMed:16190980}; Peripheral membrane protein {ECO:0000269|PubMed:16190980}. Early endosome {ECO:0000269|PubMed:21920005}. Late endosome {ECO:0000269|PubMed:21920005}. Note=Endosomal localization is reported controversially. Does not localize to endosomes (PubMed:16190980). Localizes to early and late endosomal structures (PubMed:21920005, PubMed:18088321). {ECO:0000269|PubMed:16190980, ECO:0000269|PubMed:18088321, ECO:0000269|PubMed:21920005}. SUBUNIT: Component of the heterotrimeric retromer cargo-selective complex (CSC), also described as vacuolar protein sorting subcomplex (VPS), formed by VPS26 (VPS26A or VPS26B), VPS29 and VPS35 (PubMed:21040701, PubMed:21920005, PubMed:18088321, PubMed:20875039). The CSC has a highly elongated structure with VPS26 and VPS29 binding independently at opposite distal ends of VPS35 as central platform (Probable). The CSC is believed to associate with variable sorting nexins to form functionally distinct retromer complex variants. The originally described SNX-BAR retromer is a pentamer containing the CSC and a heterodimeric membrane-deforming subcomplex formed between SNX1 or SNX2 and SNX5 or SNX6 (also called SNX-BAR subcomplex); the respective CSC and SNX-BAR subcomplexes associate with low affinity. The CSC associates with SNX3 to form a SNX3-retromer complex. The CSC associates with SNX27, the WASH complex and the SNX-BAR subcomplex to form the SNX27-retromer complex (By similarity). Interacts with VPS29, VPS35, TBC1D5, GOLPH3, SNX27 (PubMed:16190980, PubMed:21040701, PubMed:21920005, PubMed:25136126). {ECO:0000250|UniProtKB:O75436, ECO:0000269|PubMed:16190980, ECO:0000269|PubMed:18088321, ECO:0000269|PubMed:20875039, ECO:0000269|PubMed:21040701, ECO:0000269|PubMed:21920005, ECO:0000269|PubMed:25136126, ECO:0000303|PubMed:20875039}. TISSUE SPECIFICITY: Ubiquitously expressed in developing embryo and adult. Highly expressed in brain. {ECO:0000269|PubMed:16190980, ECO:0000269|PubMed:21920005}. +P13372 VPRE1_MOUSE Immunoglobulin iota chain (Protein VPreB1) (CD antigen CD179a) 142 16,125 Chain (1); Disulfide bond (1); Region (5); Signal peptide (1) FUNCTION: Associates with the Ig-mu chain to form a molecular complex that is expressed on the surface of pre-B-cells. This complex presumably regulates Ig gene rearrangements in the early steps of B-cell differentiation. TISSUE SPECIFICITY: Only expressed by pre-B-cells. +Q8C190 VP9D1_MOUSE VPS9 domain-containing protein 1 (5-day ovary-specific transcript 1 protein) 649 71,284 Alternative sequence (2); Chain (1); Domain (1); Modified residue (1) +T1NXB5 VSTM4_MOUSE V-set and transmembrane domain-containing protein 4 [Cleaved into: Peptide Lv] 319 35,899 Chain (1); Disulfide bond (1); Domain (1); Glycosylation (3); Mass spectrometry (1); Peptide (1); Signal peptide (1); Transmembrane (1) TRANSMEM 180 200 Helical. {ECO:0000255}. FUNCTION: Peptide Lv enhances L-type voltage-gated calcium channel (L-VGCC) currents in retinal photoreceptors. {ECO:0000269|PubMed:22912796}. PTM: Proteolytically cleaved to generate a bioactive peptide. {ECO:0000269|PubMed:22912796}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: Peptide Lv: Secreted {ECO:0000269|PubMed:22912796}. TISSUE SPECIFICITY: Peptide Lv is widely expressed in various tissues and the central nervous system, including the retinal photoreceptor layer, hippocampus, olfactory bulb, and cerebellum. {ECO:0000269|PubMed:22912796}. +A0A140LHF2 VSXL2_MOUSE V-set and immunoglobulin domain-containing protein 10-like 2 776 83,270 Chain (1); Disulfide bond (5); Domain (6); Glycosylation (2); Signal peptide (1); Transmembrane (1) TRANSMEM 713 733 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. +Q9D5R2 WDR20_MOUSE WD repeat-containing protein 20 567 62,782 Chain (1); Initiator methionine (1); Modified residue (6); Repeat (5); Sequence conflict (1) FUNCTION: Regulator of deubiquitinating complexes. Activates deubiquitinating activity of complexes containing USP12. {ECO:0000250|UniProtKB:P62068}. SUBUNIT: Interacts with USP12. Component of the USP12/WDR20/WDR48 deubiquitinating complex. Interacts with USP46. {ECO:0000250|UniProtKB:P62068}. +Q3UMB9 WASC4_MOUSE WASH complex subunit 4 (WASH complex subunit SWIP) 1173 136,370 Chain (1); Coiled coil (1); Erroneous initiation (2); Initiator methionine (1); Modified residue (3); Region (1); Sequence caution (1) FUNCTION: Acts at least in part as component of the WASH core complex whose assembly at the surface of endosomes seems to inhibit WASH nucleation-promoting factor (NPF) activity in recruiting and activating the Arp2/3 complex to induce actin polymerization, and which is involved in regulation of the fission of tubules that serve as transport intermediates during endosome sorting (PubMed:19922875). {ECO:0000250|UniProtKB:Q2M389, ECO:0000305|PubMed:19922875}. SUBCELLULAR LOCATION: Early endosome {ECO:0000250|UniProtKB:Q2M389}. SUBUNIT: Component of the WASH core complex also described as WASH regulatory complex (SHRC) composed of WASH (WASHC1, WASH2P or WASH3P), WASHC2 (WASHC2A or WASHC2C), WASHC3, WASHC4 and WASHC5. The WASH core complex associates via WASHC2 with the F-actin-capping protein dimer (formed by CAPZA1, CAPZA2 or CAPZA3 and CAPZB) in a transient or substoichiometric manner which was initially described as WASH complex (By similarity). {ECO:0000250|UniProtKB:Q2M389}. +Q64527 WNT8A_MOUSE Protein Wnt-8a (Protein Wnt-8d) (Stimulated by retinoic acid gene 11 protein) 354 39,573 Chain (1); Disulfide bond (11); Glycosylation (2); Lipidation (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors. Plays a role in embryonic patterning. {ECO:0000250|UniProtKB:P51028}. PTM: Palmitoleoylation is required for efficient binding to frizzled receptors (By similarity). Depalmitoleoylation leads to Wnt signaling pathway inhibition (By similarity). {ECO:0000250|UniProtKB:P28026, ECO:0000250|UniProtKB:P56704}.; PTM: Proteolytic processing by TIKI1 and TIKI2 promotes oxidation and formation of large disulfide-bond oligomers, leading to inactivation of WNT8A. {ECO:0000250|UniProtKB:P28026}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q9H1J5}. Secreted {ECO:0000250|UniProtKB:Q9H1J5}. SUBUNIT: Forms a soluble 1:1 complex with AFM; this prevents oligomerization and is required for prolonged biological activity. The complex with AFM may represent the physiological form in body fluids. {ECO:0000250|UniProtKB:Q9H1J5}. +Q9D0I6 WSDU1_MOUSE WD repeat, SAM and U-box domain-containing protein 1 474 51,691 Chain (1); Domain (2); Erroneous initiation (1); Modified residue (1); Repeat (7); Sequence conflict (1) +O54927 WSB1_MOUSE WD repeat and SOCS box-containing protein 1 (WSB-1) 421 47,065 Chain (1); Domain (1); Repeat (5) Protein modification; protein ubiquitination. FUNCTION: Probable substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Recognizes type II iodothyronine deiodinase/DIO2. Confers constitutive instability to HIPK2 through proteasomal degradation (By similarity). {ECO:0000250}. SUBUNIT: Interacts with DIO2. Component of the probable ECS(WSB1) E3 ubiquitin-protein ligase complex which contains CUL5, RNF7/RBX2, Elongin BC complex and WSB1. Component of a probable ECS-like E3 ubiquitin-protein ligase complex which contains CUL5, RBX1, Elongin BC complex and WSB1. Interacts with CUL5, RNF7, ELOB and ELOC. Binds to HIPK2 through WD40 repeats (By similarity). {ECO:0000250}. DOMAIN: The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin ligase complexes. {ECO:0000250}. +Q5GH66 XKR5_MOUSE XK-related protein 5 676 74,634 Chain (1); Transmembrane (7) TRANSMEM 37 57 Helical. {ECO:0000255}.; TRANSMEM 114 134 Helical. {ECO:0000255}.; TRANSMEM 140 160 Helical. {ECO:0000255}.; TRANSMEM 206 226 Helical. {ECO:0000255}.; TRANSMEM 239 259 Helical. {ECO:0000255}.; TRANSMEM 266 286 Helical. {ECO:0000255}.; TRANSMEM 294 314 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8BXX2 ZBT49_MOUSE Zinc finger and BTB domain-containing protein 49 (Zinc finger protein 509) 756 83,091 Alternative sequence (3); Chain (1); Domain (1); Zinc finger (7) FUNCTION: Transcription factor. Inhibits cell proliferation by activating either CDKN1A/p21 transcription or RB1 transcription. {ECO:0000250|UniProtKB:Q6ZSB9}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6ZSB9}. Nucleus {ECO:0000250|UniProtKB:Q6ZSB9}. SUBUNIT: Interacts with EP300, KAT5/Tip60 and ZBTB17. The interaction with EP300 is direct and leads to synergistic induction of CDKN1A. On the CDKN1A promoter, forms a complex with ZBTB17; this interaction leads to additive CDKN1A transactivation. The interaction with ZBTB17 may block ZBTB17 repressor activity. {ECO:0000250|UniProtKB:Q6ZSB9}. TISSUE SPECIFICITY: Widely expressed, with highest levels in white adipose tissue and kidney, intermediate levels in brain, liver and heart, and lowest levels in spleen, brown adipose tissue and muscle. {ECO:0000269|PubMed:25245946}. +Q7TQ40 ZIC5_MOUSE Zinc finger protein ZIC 5 (Odd paired-related protein) (Opa-related protein) (Zinc finger protein of the cerebellum 5) 622 64,542 Chain (1); Compositional bias (2); Modified residue (3); Sequence conflict (1); Zinc finger (4) FUNCTION: Essential for neural crest development, converting cells from an epidermal fate to a neural crest cell fate. Binds to DNA. {ECO:0000269|PubMed:15465018}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15465018}. +Q8CIE2 ZMIZ2_MOUSE Zinc finger MIZ domain-containing protein 2 (PIAS-like protein Zimp7) 920 96,719 Alternative sequence (2); Chain (1); Cross-link (3); Erroneous initiation (1); Modified residue (3); Region (1); Zinc finger (1) FUNCTION: Increases ligand-dependent transcriptional activity of AR and other nuclear hormone receptors. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Detected at replication foci throughout S phase. {ECO:0000250}. SUBUNIT: Interacts with AR, SMARCA4/BRG1 and SMARCE1/BAF57. Interaction with either SMARCA4 and SMARCE1 enhances AR-mediated transcription (By similarity). {ECO:0000250}. +Q8R0N9 ZDHC1_MOUSE Probable palmitoyltransferase ZDHHC1 (EC 2.3.1.225) (Zinc finger DHHC domain-containing protein 1) (DHHC-1) 484 52,979 Chain (1); Domain (1); Transmembrane (4) TRANSMEM 50 70 Helical. {ECO:0000255}.; TRANSMEM 75 95 Helical. {ECO:0000255}.; TRANSMEM 183 203 Helical. {ECO:0000255}.; TRANSMEM 239 259 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. DOMAIN: The DHHC domain is required for palmitoyltransferase activity. {ECO:0000250}. TISSUE SPECIFICITY: Expressed at high levels in fetal lung and heart. Expressed at lower levels in fetal liver and brain. Also detected in adult islet cells of pancreas, Leydig cells of testis, retina and molecular layer of cerebellum. {ECO:0000269|PubMed:10395086}. +Q61967 ZFP90_MOUSE Zinc finger protein 90 (Zfp-90) (Zinc finger protein NK10) 636 72,423 Chain (1); Cross-link (1); Domain (1); Frameshift (1); Sequence caution (1); Sequence conflict (2); Zinc finger (13) FUNCTION: Inhibits the transcriptional repressor activity of REST by inhibiting its binding to DNA, thereby derepressing transcription of REST target genes. {ECO:0000269|PubMed:21284946, ECO:0000269|PubMed:7576184}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21284946, ECO:0000269|PubMed:7576184}. Note=Colocalizes with REST in the nucleus. {ECO:0000269|PubMed:21284946}. SUBUNIT: Interacts (via N- and C-termini) with REST (via zinc-finger DNA-binding domain); the interaction inhibits REST repressor activity. {ECO:0000269|PubMed:21284946}. TISSUE SPECIFICITY: Brain, spleen, thymus, and testis (PubMed:7576184). Expressed in heart (PubMed:7576184, PubMed:21284946). {ECO:0000269|PubMed:21284946, ECO:0000269|PubMed:7576184}. +B1AWL2 ZN462_MOUSE Zinc finger protein 462 (Zinc finger PBX1-interacting protein) (ZFPIP) 2495 282,713 Chain (1); Cross-link (28); Modified residue (8); Region (1); Sequence conflict (4); Zinc finger (27) FUNCTION: Zinc finger nuclear factor involved in transcription by regulating chromatin structure and organization (PubMed:20219459, PubMed:21570965). Involved in the pluripotency and differentiation of embryonic stem cells by regulating SOX2, POU5F1/OCT4, and NANOG (PubMed:21570965). By binding PBX1, prevents the heterodimerization of PBX1 and HOXA9 and their binding to DNA (PubMed:17353115). Regulates neuronal development and neural cell differentiation (PubMed:21570965, PubMed:27621227). {ECO:0000269|PubMed:17353115, ECO:0000269|PubMed:20219459, ECO:0000269|PubMed:21570965, ECO:0000269|PubMed:27621227}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17353115, ECO:0000269|PubMed:20219459, ECO:0000269|PubMed:21570965}. SUBUNIT: Interacts with PBX1 isoform PBX1b; this interaction prevents PBX1-HOXA9 heterodimer from forming and binding to DNA. {ECO:0000269|PubMed:17353115}. TISSUE SPECIFICITY: Expressed in the cerebral cortex (at protein level) (PubMed:17207666, PubMed:27621227). Expressed in embryonic stem cells (at protein level) (PubMed:20219459). Expressed in heart, liver, kidney, muscle, and female and male genital tracts (at protein level) (PubMed:27621227, PubMed:17353115). {ECO:0000269|PubMed:17207666, ECO:0000269|PubMed:17353115, ECO:0000269|PubMed:20219459, ECO:0000269|PubMed:27621227}. +Q8CCG1 ZC21C_MOUSE Zinc finger C2HC domain-containing protein 1C 527 59,642 Chain (1); Coiled coil (1); Compositional bias (3); Sequence conflict (1); Zinc finger (1) +E9PYI1 ZN568_MOUSE Zinc finger protein 568 671 77,116 Alternative sequence (1); Beta strand (13); Chain (1); Domain (2); Helix (13); Mutagenesis (10); Sequence conflict (1); Turn (10); Zinc finger (11) FUNCTION: Has transcriptional repression activity, partially through the recruitment of the corepressor TRIM28 but has also repression activity independently of this interaction (PubMed:22110054, PubMed:27658112). Essential during embryonic development, where it acts as direct repressor of IGF2-P0, placental-specific transcript of IGF2, in early development and regulates convergent extension movements required for axis elongation and tissue morphogenesis in all germ layers (PubMed:18701545, PubMed:22110054, PubMed:28522536). Also important for normal morphogenesis of extraembryonic tissues including the yolk sac, extraembryonic mesoderm and placenta (PubMed:18701545, PubMed:21094155). May enhance proliferation or maintenance of neural stem cells (PubMed:23071813). {ECO:0000269|PubMed:18701545, ECO:0000269|PubMed:21094155, ECO:0000269|PubMed:22110054, ECO:0000269|PubMed:23071813, ECO:0000269|PubMed:27658112}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22110054, ECO:0000269|PubMed:23071813}. SUBUNIT: Interacts with TRIM28. {ECO:0000269|PubMed:22110054, ECO:0000269|PubMed:27658112, ECO:0000269|PubMed:28522536}. DOMAIN: KRAB domain 1, but not KRAB domain 2, is required for transcriptional repression. Both contribute to interaction with TRIM28. Differences in repressive activity between KRAB domain 1 and 2 are likely due to amino acid differences at multiple residues. {ECO:0000269|PubMed:27658112}. TISSUE SPECIFICITY: Little or no expression detected in most adult tissues (brain, liver, kidney, spleen, testis, ovary). In the hippocampus, detected in neural stem cells within the subventricular zone and subgranular zone. {ECO:0000269|PubMed:23071813}. +Q3U2E2 ZMYM5_MOUSE Zinc finger MYM-type protein 5 627 70,071 Chain (1); Compositional bias (1); Cross-link (6); Sequence caution (1); Zinc finger (4) FUNCTION: Functions as a transcriptional regulator. {ECO:0000250|UniProtKB:Q9UJ78}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Interacts (via N-terminal 120 amino acid region) with ETV5 (via C-terminal). {ECO:0000250|UniProtKB:Q9UJ78}. +Q56A10 ZN608_MOUSE Zinc finger protein 608 1511 162,345 Alternative sequence (4); Chain (1); Coiled coil (1); Compositional bias (3); Cross-link (12); Erroneous initiation (1); Modified residue (9); Sequence conflict (6); Zinc finger (1) FUNCTION: Transcription factor, which represses ZNF609 transcription. {ECO:0000269|PubMed:23076336}. TISSUE SPECIFICITY: Expressed at low levels in thymocytes. {ECO:0000269|PubMed:23076336}. +Q8BZ47 ZN609_MOUSE Zinc finger protein 609 1413 151,117 Alternative sequence (2); Chain (1); Compositional bias (5); Cross-link (5); Erroneous initiation (1); Modified residue (22); Sequence conflict (3); Zinc finger (1) FUNCTION: Transcription factor, which activates RAG1, and possibly RAG2, transcription. Through the regulation of RAG1/2 expression, may regulate thymocyte maturation (PubMed:28344082). Along with NIPBL and the multiprotein complex Integrator, promotes cortical neuron migration during brain development by regulating the transcription of crucial genes in this process. Preferentially binds promoters containing paused RNA polymerase II. Up-regulates the expression of SEMA3A, NRP1, PLXND1 and GABBR2 genes, among others (PubMed:28041881). {ECO:0000269|PubMed:28041881, ECO:0000269|PubMed:28344082}.; FUNCTION: Isoform 2: Involved in regulation of myoblast proliferation during myogenesis. {ECO:0000269|PubMed:28344082}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28041881}. SUBUNIT: Interacts (via N-terminus) with NIPBL (PubMed:28041881). Interacts with the multiprotein complex Integrator (PubMed:28041881). {ECO:0000269|PubMed:28041881}. TISSUE SPECIFICITY: Expressed in myoblasts (PubMed:28344082). Expressed in neurons in various brain regions, including striatum, prefrontal cortex, olfactory bulb, midbrain, cerebellum and hippocampus (PubMed:25921068). Expressed in neural stem cells (at protein level) (PubMed:28041881). Expressed in thymocytes (PubMed:23076336). {ECO:0000269|PubMed:23076336, ECO:0000269|PubMed:25921068, ECO:0000269|PubMed:28041881, ECO:0000269|PubMed:28344082}. +Q8C1M2 ZN428_MOUSE Zinc finger protein 428 176 19,003 Chain (1); Compositional bias (2); Modified residue (1); Sequence conflict (2); Zinc finger (1) +Q61116 ZN235_MOUSE Zinc finger protein 235 (Zinc finger protein 93) (Zfp-93) 645 73,012 Chain (1); Domain (1); Sequence conflict (1); Zinc finger (13) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q80V23 ZNF32_MOUSE Zinc finger protein 32 (Zinc finger protein 637) 272 30,773 Alternative sequence (1); Chain (1); Zinc finger (7) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q8BZ89 ZN322_MOUSE Zinc finger protein 322 (Zinc finger protein 322A) 410 48,492 Chain (1); Erroneous initiation (1); Modified residue (1); Sequence conflict (1); Zinc finger (10) FUNCTION: Transcriptional activator. Important for maintenance of pluripotency in embryonic stem cells. Binds directly to the POU5F1 distal enhancer and the NANOG proximal promoter, and enhances expression of both genes. Can also bind to numerous other gene promoters and regulates expression of many other pluripotency factors, either directly or indirectly. Promotes inhibition of MAPK signaling during embryonic stem cell differentiation. {ECO:0000269|PubMed:24550733}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24550733}. Cytoplasm {ECO:0000269|PubMed:24550733}. Note=Mainly found in the nucleus. {ECO:0000269|PubMed:24550733}. SUBUNIT: Interacts with POU5F1. {ECO:0000269|PubMed:24550733}. +Q3U133 ZN746_MOUSE Zinc finger protein 746 652 69,821 Chain (1); Coiled coil (1); Compositional bias (2); Cross-link (2); Domain (1); Erroneous initiation (1); Sequence conflict (1); Zinc finger (4) FUNCTION: Transcription repressor that specifically binds to the 5'-TATTTT[T/G]-3' consensus sequence on promoters and repress transcription of PGC-1-alpha (PPARGC1A), thereby playing a role in regulation of neuron death. {ECO:0000250}. PTM: Ubiquitinated by PRKN. 'Lys-48'-linked polyubiquitination by PRKN leads to degradation by the proteasome and may play a key role in regulation of neuron death (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Mainly localizes to the cytoplasm; probably translocates to the nucleus to repress selected genes. {ECO:0000250}. SUBUNIT: Interacts (via C2H2-type zinc fingers) with PRKN. {ECO:0000269|PubMed:21376232}. TISSUE SPECIFICITY: Widely expressed. In brain, it is heterogeneously distributed throughout the brain and localizes to neurons, including substantia nigra pars compacta dopamine-containing neurons. Weakly expressed in cerebellum and midbrain (at protein level). {ECO:0000269|PubMed:21376232}. +Q3U381 ZN692_MOUSE Zinc finger protein 692 531 59,010 Chain (1); Compositional bias (3); Modified residue (1); Zinc finger (5) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q2HJ10 ZNT2_MOUSE Zinc transporter 2 (ZnT-2) (Solute carrier family 30 member 2) 371 40,639 Chain (1); Topological domain (8); Transmembrane (7) TRANSMEM 70 90 Helical. {ECO:0000255}.; TRANSMEM 100 120 Helical. {ECO:0000255}.; TRANSMEM 137 157 Helical. {ECO:0000255}.; TRANSMEM 173 193 Helical. {ECO:0000255}.; TRANSMEM 220 240 Helical. {ECO:0000255}.; TRANSMEM 249 269 Helical. {ECO:0000255}.; TRANSMEM 304 324 Helical. {ECO:0000255}. TOPO_DOM 1 69 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 91 99 Vacuolar. {ECO:0000255}.; TOPO_DOM 121 136 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 158 172 Vacuolar. {ECO:0000255}.; TOPO_DOM 194 219 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 241 248 Vacuolar. {ECO:0000255}.; TOPO_DOM 270 303 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 325 371 Vacuolar. {ECO:0000255}. SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein. +Q7TNU6 ZN250_MOUSE Zinc finger protein 250 (Zinc finger protein 647) 535 59,873 Chain (1); Cross-link (3); Domain (1); Sequence conflict (2); Zinc finger (13) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q9CWV7 ZSWM1_MOUSE Zinc finger SWIM domain-containing protein 1 455 51,481 Chain (1); Erroneous initiation (1); Zinc finger (1) +Q9D9X6 ZSWM2_MOUSE E3 ubiquitin-protein ligase Zswim2 (EC 2.3.2.27) (MEKK1-related protein X) (MEX) (RING-type E3 ubiquitin transferase Zswim2) (ZZ-type zinc finger-containing protein 2) (Zinc finger SWIM domain-containing protein 2) 631 71,793 Chain (1); Mutagenesis (2); Region (1); Zinc finger (4) FUNCTION: E3 ubiquitin-protein ligase involved in the regulation of Fas-, DR3- and DR4-mediated apoptosis. Functions in conjunction with the UBE2D1, UBE2D3 and UBE2E1 E2 ubiquitin-conjugating enzymes. {ECO:0000269|PubMed:16522193}. PTM: Polyubiquitinated. Polyubiquitination is followed by degradation via the proteasome. {ECO:0000269|PubMed:16522193}. SUBUNIT: Dimer. Interacts with UBE2D1. {ECO:0000269|PubMed:16522193}. DOMAIN: The SWIM-type zinc finger is required for ubiquitination activity. {ECO:0000269|PubMed:16522193}. TISSUE SPECIFICITY: Expressed only in testis. {ECO:0000269|PubMed:16522193}. +E9Q5K9 YTDC1_MOUSE YTH domain-containing protein 1 736 85,649 Alternative sequence (2); Binding site (2); Chain (1); Compositional bias (3); Cross-link (1); Domain (1); Erroneous initiation (1); Modified residue (13); Region (1); Sequence conflict (2) FUNCTION: Regulator of alternative splicing that specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs (By similarity). M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in the efficiency of mRNA splicing, processing and stability (By similarity). Acts as a key regulator of exon-inclusion or exon-skipping during alternative splicing via interaction with mRNA splicing factors SRSF3 and SRSF10 (By similarity). Specifically binds m6A-containing mRNAs and promotes recruitment of SRSF3 to its mRNA-binding elements adjacent to m6A sites, leading to exon-inclusion during alternative splicing (By similarity). In contrast, interaction with SRSF3 prevents interaction with SRSF10, a splicing factor that promotes exon skipping: this prevents SRSF10 from binding to its mRNA-binding sites close to m6A-containing regions, leading to inhibit exon skipping during alternative splicing (By similarity). May also regulate alternative splice site selection (By similarity). Also involved in nuclear export of m6A-containing mRNAs via interaction with SRSF3: interaction with SRSF3 facilitates m6A-containing mRNA-binding to both SRSF3 and NXF1, promoting mRNA nuclear export (By similarity). Also recognizes and binds m6A on other RNA molecules (By similarity). Involved in random X inactivation mediated by Xist RNA: recognizes and binds m6A-containing Xist and promotes transcription repression activity of Xist (By similarity). Involved in S-adenosyl-L-methionine homeostasis by regulating expression of MAT2A transcripts, probably by binding m6A-containing MAT2A mRNAs (PubMed:29262316). {ECO:0000250|UniProtKB:Q96MU7, ECO:0000269|PubMed:29262316}. PTM: Tyrosine phosphorylated. {ECO:0000250|UniProtKB:Q9QY02}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96MU7}. Nucleus speckle {ECO:0000250|UniProtKB:Q96MU7}. Note=Localizes to a novel subnuclear structure, the YT bodies. {ECO:0000250|UniProtKB:Q9QY02}. SUBUNIT: Interacts with KHDRBS1/SAM68 (By similarity). Interacts with SRSF1 (By similarity). Interacts with SRSF2 (By similarity). Interacts with TRA2B (By similarity). Interacts with SRSF3 (By similarity). Interacts with SRSF10 (By similarity). Interacts with KHDRBS3 (By similarity). Interacts with EMD (By similarity). Interacts with RBMX (By similarity). Interacts with ZCCHC8 (By similarity). {ECO:0000250|UniProtKB:Q96MU7, ECO:0000250|UniProtKB:Q9QY02}. DOMAIN: The YTH domain mediates RNA-binding. {ECO:0000250|UniProtKB:Q96MU7}. +Q3U5F4 YRDC_MOUSE YrdC domain-containing protein, mitochondrial (Ischemia/reperfusion-inducible protein) (mIRIP) 280 29,454 Chain (1); Domain (1); Erroneous gene model prediction (1); Erroneous initiation (3); Modified residue (1); Sequence conflict (3); Transit peptide (1) FUNCTION: May regulate the activity of some transporters. {ECO:0000269|PubMed:16024787}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}. Membrane {ECO:0000269|PubMed:16024787}; Peripheral membrane protein {ECO:0000269|PubMed:16024787}. Note=Predominantly localized in the plasma membrane. SUBUNIT: Interacts with RSC1A1. {ECO:0000269|PubMed:16024787}. TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in testis, secretory, and endocrine organs. {ECO:0000269|PubMed:16024787}. +Q5Y5T1 ZDH20_MOUSE Palmitoyltransferase ZDHHC20 (EC 2.3.1.225) (Zinc finger DHHC domain-containing protein 20) (DHHC-20) 380 43,976 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Domain (1); Metal binding (8); Modified residue (3); Region (1); Sequence conflict (3); Site (2); Topological domain (5); Transmembrane (4) TRANSMEM 15 35 Helical. {ECO:0000250|UniProtKB:Q5W0Z9}.; TRANSMEM 54 74 Helical. {ECO:0000250|UniProtKB:Q5W0Z9}.; TRANSMEM 170 190 Helical. {ECO:0000250|UniProtKB:Q5W0Z9}.; TRANSMEM 223 246 Helical. {ECO:0000250|UniProtKB:Q5W0Z9}. TOPO_DOM 1 14 Cytoplasmic. {ECO:0000250|UniProtKB:Q5W0Z9}.; TOPO_DOM 36 53 Lumenal. {ECO:0000250|UniProtKB:Q5W0Z9}.; TOPO_DOM 75 169 Cytoplasmic. {ECO:0000250|UniProtKB:Q5W0Z9}.; TOPO_DOM 191 222 Lumenal. {ECO:0000250|UniProtKB:Q5W0Z9}.; TOPO_DOM 247 380 Cytoplasmic. {ECO:0000250|UniProtKB:Q5W0Z9}. FUNCTION: Catalyzes palmitoylation of Cys residues on target proteins (PubMed:15603741). Catalyzes palmitoylation of Cys residues in the cytoplasmic C-terminus of EGFR, and modulates the duration of EGFR signaling by modulating palmitoylation-dependent EGFR internalization and degradation. Has a preference for acyl-CoA with C16 fatty acid chains. Can also utilize acyl-CoA with C14 and C18 fatty acid chains (By similarity). {ECO:0000250|UniProtKB:Q5W0Z9, ECO:0000305|PubMed:15603741}. PTM: Autopalmitoylated (in vitro). {ECO:0000250|UniProtKB:Q5W0Z9}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q5W0Z9}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5W0Z9}. Cell membrane {ECO:0000250|UniProtKB:Q5W0Z9}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5W0Z9}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q5W0Z9}. DOMAIN: The DHHC domain is required for palmitoyltransferase activity. {ECO:0000250|UniProtKB:Q5W0Z9}. TISSUE SPECIFICITY: Highest levels in lung. {ECO:0000269|PubMed:15603741}. +P20239 ZP2_MOUSE Zona pellucida sperm-binding protein 2 (Zona pellucida glycoprotein 2) (Zp-2) (Zona pellucida protein A) [Cleaved into: Processed zona pellucida sperm-binding protein 2] 713 80,210 Beta strand (18); Chain (2); Disulfide bond (7); Domain (1); Glycosylation (7); Helix (5); Mutagenesis (1); Propeptide (1); Region (1); Signal peptide (1); Site (2); Topological domain (2); Transmembrane (1); Turn (2) TRANSMEM 684 703 Helical. {ECO:0000255}. TOPO_DOM 35 683 Extracellular.; TOPO_DOM 704 713 Cytoplasmic. FUNCTION: The mammalian zona pellucida, which mediates species-specific sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy, is composed of three to four glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP2 may act as a secondary sperm receptor. {ECO:0000269|PubMed:22472438}. PTM: Proteolytically cleaved before the transmembrane segment to yield the secreted ectodomain incorporated in the zona pellucida. {ECO:0000269|PubMed:22472438, ECO:0000269|PubMed:26811476}.; PTM: Proteolytically cleaved in the N-terminal part by the metalloendopeptidase ASTL exocytosed from cortical granules after fertilization, yielding a N-terminal peptide of about 30 kDa which remains covalently attached to the C-terminal peptide via disulfide bond(s). This cleavage may play an important role in the post-fertilization block to polyspermy. Additional proteolytically cleavage of the N-terminal peptide of 30 kDa occurs in one-cell and two-cell embryos. {ECO:0000269|PubMed:22472438}.; PTM: N-glycosylated. {ECO:0000269|PubMed:12799386}.; PTM: O-glycosylated; contains sulfate-substituted glycans. {ECO:0000269|PubMed:12799386}. SUBCELLULAR LOCATION: Processed zona pellucida sperm-binding protein 2: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:12799386, ECO:0000269|PubMed:17559063, ECO:0000269|PubMed:22472438, ECO:0000269|PubMed:3845123}. Note=The glycoproteinaceous translucent extracellular matrix that surrounds the mammalian oocyte is called zona pellucida. {ECO:0000305}.; SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22472438}; Single-pass type I membrane protein {ECO:0000255}. SUBUNIT: Can form homopolymers that assemble into long fibers (in vitro) (PubMed:17559063). Polymers of ZP2 and ZP3 organized into long filaments cross-linked by ZP1 homodimers (PubMed:3845123). Interacts with ZP3 (By similarity). {ECO:0000250|UniProtKB:Q05996, ECO:0000269|PubMed:17559063, ECO:0000269|PubMed:3845123}. DOMAIN: The ZP domain is involved in the polymerization of the ZP proteins to form the zona pellucida. {ECO:0000269|PubMed:26811476}. TISSUE SPECIFICITY: Detected in the zona pellucida that surrounds the oocyte (at protein level) (PubMed:12799386, PubMed:3845123, PubMed:17559063). Oocyte. {ECO:0000269|PubMed:1690843}. +Q62384 ZPR1_MOUSE Zinc finger protein ZPR1 (Zinc finger protein 259) 459 50,715 Beta strand (25); Chain (1); Helix (12); Turn (8); Zinc finger (2) FUNCTION: Acts as a signaling molecule that communicates proliferative growth signals from the cytoplasm to the nucleus. Plays a role for the localization and accumulation of the survival motor neuron protein SMN1 in sub-nuclear bodies, including gems and Cajal bodies. Induces neuron differentiation and stimulates axonal growth and formation of growth cone in spinal cord motor neurons. Plays a role in the splicing of cellular pre-mRNAs. May be involved in H(2)O(2)-induced neuronal cell death. {ECO:0000269|PubMed:15767679, ECO:0000269|PubMed:16648254, ECO:0000269|PubMed:22422766, ECO:0000269|PubMed:8650580}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Nucleus, nucleolus. Cytoplasm, perinuclear region {ECO:0000250}. Nucleus, gem. Nucleus, Cajal body. Cell projection, axon. Cell projection, growth cone. Note=Localized predominantly in the cytoplasm in serum-starved cells growth arrested in G0 of the mitotic cell cycle. Localized both in the nucleus and cytoplasm at the G1 phase of the mitotic cell cycle. Accumulates in the subnuclear bodies during progression into the S phase of the mitotic cell cycle. Diffusely localized throughout the cell during mitosis. Colocalized with NPAT and SMN1 in nuclear bodies including gems (Gemini of coiled bodies) and Cajal bodies in a cell cycle-dependent manner. Colocalized with EGFR in the cytoplasm of quiescent cells. Translocates from the cytoplasm to the nucleus in a epidermal growth factor (EGF)-dependent manner (By similarity). Translocates together with EEF1A1 from the cytoplasm to the nucleolus after treatment with mitogens. Colocalized with SMN1 in Gemini of coiled bodies (gems), Cajal bodies, axon and growth cones of neurons. {ECO:0000250}. SUBUNIT: Component of an import snRNP complex composed of KPNB1, SNUPN, SMN1 and ZNF259. Interacts (via C-terminal region) with SMN1 (via C-terminal region); the interaction occurs after treatment with serum (By similarity). Interacts with elongation factor 1-alpha EEF1A1; the interaction occurs in a epidermal growth factor (EGF)-dependent manner. Interacts (via zinc fingers) with EGFR (via C-terminal cytoplasmic kinase domain); the interaction is negatively regulated in response to epidermal growth factor (EGF) stimulation and EGFR kinase activity. May also bind to the PDGFR receptor. {ECO:0000250, ECO:0000269|PubMed:17704259, ECO:0000269|PubMed:19966453, ECO:0000269|PubMed:22422766, ECO:0000269|PubMed:8650580, ECO:0000269|PubMed:9852145}. TISSUE SPECIFICITY: Expressed in brain. Expressed in the spinal cord motor neurons (at protein level). Expressed in spleen, liver, muscle, kidney and testis. Expressed in the frontal cortex, cornus ammonis, dentate gyrus of the hippocampus and in Purkinje cells of the cerebellum. {ECO:0000269|PubMed:16465397, ECO:0000269|PubMed:16648254, ECO:0000269|PubMed:8650580}. DISEASE: Note=May contribute to the severity of spinal muscular atrophy by increasing spinal motor neurons degeneration. {ECO:0000269|PubMed:16648254}. +Q8CFL8 ZSWM3_MOUSE Zinc finger SWIM domain-containing protein 3 695 79,132 Chain (1); Zinc finger (1) +Q07231 ZSC21_MOUSE Zinc finger and SCAN domain-containing protein 21 (CtFIN51) (Transcription factor RU49) (Zinc finger protein 38) (Zfp-38) 555 63,012 Chain (1); Cross-link (4); Domain (1); Region (1); Repeat (3); Sequence conflict (9); Zinc finger (7) FUNCTION: Strong transcriptional activator. Associated with meiosis in both male and female gametogenesis. May have different functions in somatic cells. SUBCELLULAR LOCATION: Nucleus. TISSUE SPECIFICITY: Expressed predominantly in the spermatocytes and spermatids of adult testes. It is also present at lower levels in the ovary, brain, spleen, embryo and fetus. +Q62523 ZYX_MOUSE Zyxin 564 60,546 Chain (1); Compositional bias (4); Domain (3); Initiator methionine (1); Modified residue (14); Sequence conflict (3) FUNCTION: Adhesion plaque protein. Binds alpha-actinin and the CRP protein. Important for targeting TES and ENA/VASP family members to focal adhesions and for the formation of actin-rich structures. May be a component of a signal transduction pathway that mediates adhesion-stimulated changes in gene expression (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell junction, focal adhesion {ECO:0000250}. Nucleus {ECO:0000250}. Note=Associates with the actin cytoskeleton near the adhesion plaques. Enters the nucleus in the presence of HESX1 (By similarity). {ECO:0000250}. SUBUNIT: Interacts, via the Pro-rich regions, with the EVH1 domains of ENAH, EVL and VASP. Interacts with the first LIM domain of TES. Interacts with SYNPO2 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q15942}. +Q68FE8 Z280D_MOUSE Zinc finger protein 280D (Suppressor of hairy wing homolog 4) 974 107,836 Alternative sequence (5); Chain (1); Compositional bias (1); Cross-link (11); Modified residue (3); Zinc finger (5) FUNCTION: May function as a transcription factor. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q9QXT9 Z354B_MOUSE Zinc finger protein 354B (Kidney, ischemia, and developmentally-regulated protein 2) 601 68,664 Chain (1); Cross-link (1); Domain (1); Zinc finger (13) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: Expressed in brain and kidney. Lower levels in lung, muscle, heart, testis, tongue and eye. {ECO:0000269|PubMed:10564808}. +Q60821 ZBT17_MOUSE Zinc finger and BTB domain-containing protein 17 (LP-1) (Polyomavirus late initiator promoter-binding protein) (Zinc finger protein 100) (Zfp-100) (Zinc finger protein 151) (Zinc finger protein Z13) 794 86,758 Chain (1); Cross-link (2); Domain (1); Region (3); Sequence conflict (6); Zinc finger (13) FUNCTION: Transcription factor that can function as an activator or repressor depending on its binding partners, and by targeting negative regulators of cell cycle progression. Has been shown to bind to the promoters of adenovirus major late protein and cyclin D1 and activate transcription. Required for early embryonic development during gastrulation. Plays a critical role in early lymphocyte development, where it is essential to prevent apoptosis in lymphoid precursors, allowing them to survive in response to IL7 and undergo proper lineage commitment. Represses RB1 transcription; this repression can be blocked by interaction with ZBTB49 (By similarity). {ECO:0000250|UniProtKB:Q13105, ECO:0000269|PubMed:14560010, ECO:0000269|PubMed:20190815, ECO:0000269|PubMed:21258009}. PTM: Undergoes 'Lys-48'-linked polyubiquitination at Lys-388 and Lys-472 and subsequent proteasomal degradation in a TRAF2-dependent manner and upon TNFA stimulation. {ECO:0000269|PubMed:22184250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Homooligomerizes (via the BTB/POZ domain), multimerization is required for DNA binding. Binds to the C-terminal helix-loop-helix motif of MYC which inhibits ZBTB17 transactivation and growth arrest activities and renders it insoluble in the nucleus. Also interacts with HCFC1, MAGEA4 and TMPRSS11A. Interacts (via the C-terminal zinc fingers) with GFI1; the interaction results in the recruitment of MYC to the CDKN1A/p21 and CDKN1B promoters and repression of transcription. Interacts with TRAF2, interfering with the binding of UBC13 to TRAF2, and inhibiting TRAF2 E3 ligase activity. Interacts with BCL6; the interaction inhibits ZBTB17 transactivation activity on target genes involved in cell cycle arrest. Interacts with ZBTB49; this interaction blocks ZBTB17-mediated repression of RB1 (By similarity). {ECO:0000250|UniProtKB:Q13105, ECO:0000269|PubMed:20190815, ECO:0000269|PubMed:22184250}. TISSUE SPECIFICITY: Found in all the embryonic and adult tissues examined. +Q811H0 ZBT42_MOUSE Zinc finger and BTB domain-containing protein 42 (Protein simiRP58) 420 46,717 Alternative sequence (1); Chain (1); Domain (1); Erroneous initiation (1); Sequence conflict (3); Zinc finger (4) FUNCTION: Transcriptional repressor. Specifically binds DNA and probably acts by recruiting chromatin remodeling multiprotein complexes. {ECO:0000269|PubMed:18262495}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18262495}. Nucleus, nucleoplasm {ECO:0000269|PubMed:21193930}. Note=In skeletal myofibers, highly enriched in subsynaptic nuclei at the neuromuscular junctions. {ECO:0000269|PubMed:21193930}. TISSUE SPECIFICITY: Highly expressed in skeletal muscle and ovary (at protein level). Low expression in brain, lung, spleen, liver and heart (at protein level). Not detected in kidney and intestines (at protein level). Also observed in testis and, at lower levels, in stomach and nervous system. {ECO:0000269|PubMed:18262495, ECO:0000269|PubMed:21193930}. +Q2TL60 ZN667_MOUSE Zinc finger protein 667 (Myocardial ischemic preconditioning up-regulated protein 1) 609 70,263 Chain (1); Domain (1); Zinc finger (14) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +E9Q6W4 ZN296_MOUSE Zinc finger protein 296 (Hepatocellular carcinoma-associated antigen MHCA108) 445 47,821 Chain (1); Cross-link (1); Erroneous gene model prediction (1); Erroneous initiation (1); Frameshift (2); Sequence conflict (3); Zinc finger (6) FUNCTION: May be a transcriptional corepressor with KLF4. {ECO:0000269|PubMed:24161396}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24161396}. SUBUNIT: Interacts with KLF4. {ECO:0000269|PubMed:24161396}. TISSUE SPECIFICITY: Strongly expressed in testis and embryonic stem cells. {ECO:0000269|PubMed:11063263}. +Q8R1D1 ZN426_MOUSE Zinc finger protein 426 550 63,020 Chain (1); Domain (1); Erroneous initiation (1); Sequence caution (1); Sequence conflict (4); Zinc finger (11) FUNCTION: May be involved in transcriptional regulation. {ECO:0000305}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q8K083 ZN536_MOUSE Zinc finger protein 536 1302 141,576 Chain (1); Erroneous initiation (1); Modified residue (2); Sequence conflict (4); Zinc finger (9) FUNCTION: May be involved in transcriptional regulation. Recognizes and binds 2 copies of the core DNA sequence 5'-CCCCCA-3' (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q8BJM5 ZNT6_MOUSE Zinc transporter 6 (ZnT-6) (Solute carrier family 30 member 6) 460 51,027 Chain (1); Erroneous initiation (1); Sequence conflict (12); Topological domain (7); Transmembrane (6) TRANSMEM 34 54 Helical. {ECO:0000255}.; TRANSMEM 65 85 Helical. {ECO:0000255}.; TRANSMEM 99 119 Helical. {ECO:0000255}.; TRANSMEM 135 155 Helical. {ECO:0000255}.; TRANSMEM 201 221 Helical. {ECO:0000255}.; TRANSMEM 224 244 Helical. {ECO:0000255}. TOPO_DOM 1 33 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 55 64 Extracellular. {ECO:0000255}.; TOPO_DOM 86 98 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 120 134 Extracellular. {ECO:0000255}.; TOPO_DOM 156 200 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 222 223 Extracellular. {ECO:0000255}.; TOPO_DOM 245 460 Cytoplasmic. {ECO:0000255}. FUNCTION: Zinc-efflux transporter which allocates the cytoplasmic zinc to the trans-Golgi network (TGN) as well as the vesicular compartment. {ECO:0000269|PubMed:11997387}. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:11997387}; Multi-pass membrane protein {ECO:0000269|PubMed:11997387}. Note=Found in vesicles. SUBUNIT: Heterooligomer. Interacts with ZNT5 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain and liver, and to a lower extent also in lung. Highly expressed in brain (at protein level). {ECO:0000269|PubMed:11997387}. +Q9QY66 ZNHI2_MOUSE Zinc finger HIT domain-containing protein 2 (Protein FON) 399 42,897 Chain (1); Modified residue (2); Sequence conflict (2); Zinc finger (1) TISSUE SPECIFICITY: Low expression in most tissues; highly expressed in testis; particularly in seminiferous tubules. {ECO:0000269|PubMed:10602999}. +Q9CQK1 ZNHI3_MOUSE Zinc finger HIT domain-containing protein 3 (Thyroid hormone receptor interactor 3) (Thyroid receptor-interacting protein 3) (TR-interacting protein 3) (TRIP-3) 151 17,068 Chain (1); Modified residue (1); Zinc finger (1) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q15649}. Nucleus {ECO:0000250|UniProtKB:Q15649}. SUBUNIT: Thyroid receptor interacting proteins (TRIPs) specifically interact with the ligand binding domain of the thyroid receptor (TR). Requires the presence of thyroid hormone for its interaction (By similarity). Interacts with NUFIP1 (By similarity). {ECO:0000250|UniProtKB:Q15649}. TISSUE SPECIFICITY: Expressed in the cerebellum. {ECO:0000269|PubMed:28335020}. +Q0VDT2 ZN367_MOUSE Zinc finger protein 367 (C2H2 zinc finger protein ZFF29) 340 37,453 Alternative sequence (1); Chain (1); Coiled coil (1); Compositional bias (1); Erroneous initiation (1); Modified residue (1); Sequence conflict (4); Zinc finger (2) FUNCTION: Transcriptional activator. Isoform 1 may be involved in transcriptional activation of erythroid genes (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. TISSUE SPECIFICITY: Expressed in bone marrow and ovary. {ECO:0000269|PubMed:15344908}. +Q3US17 ZNF48_MOUSE Zinc finger protein 48 (Zinc finger protein 553) 591 64,599 Chain (1); Compositional bias (1); Cross-link (6); Erroneous initiation (1); Modified residue (2); Sequence conflict (3); Zinc finger (12) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q810A1 ZNF18_MOUSE Zinc finger protein 18 (Zinc finger protein 535) (Zinc finger protein with KRAB and SCAN domains 6) 556 62,929 Chain (1); Domain (2); Sequence conflict (2); Zinc finger (5) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}. +Q9DAH2 ZNRF4_MOUSE E3 ubiquitin-protein ligase ZNRF4 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase ZNRF4) (Sperizin) (Zinc/RING finger protein 4) 327 35,628 Chain (1); Glycosylation (1); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1); Zinc finger (1) TRANSMEM 151 171 Helical. {ECO:0000255}. TOPO_DOM 29 150 Lumenal. {ECO:0000305}.; TOPO_DOM 172 327 Cytoplasmic. {ECO:0000305}. Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase which specifically induces ubiquitination and proteasomal degradation of CANX within the endoplasmic reticulum (By similarity). Could have a role in spermatogenesis (Probable). {ECO:0000250|UniProtKB:Q8WWF5, ECO:0000305|PubMed:10191088}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8WWF5}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Interacts with CANX. {ECO:0000250|UniProtKB:Q8WWF5}. DOMAIN: The RING-type zinc finger is involved in CANX ubiquitination and degradation, but is not required for interaction with CANX. {ECO:0000250|UniProtKB:Q8WWF5}. TISSUE SPECIFICITY: Expressed exclusively in spermatids (at protein level). {ECO:0000269|PubMed:10191088}. +Q6PD29 ZN513_MOUSE Zinc finger protein 513 541 58,067 Alternative sequence (1); Chain (1); Compositional bias (1); Erroneous initiation (1); Modified residue (2); Sequence caution (1); Sequence conflict (1); Zinc finger (8) FUNCTION: Transcriptional regulator that plays a role in retinal development and maintenance. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Binds DNA. Can associate with the proximal promoter regions of PAX6 and SP4, and their known targets including ARR3, RHO, OPN1MW2 and OPN1SW. {ECO:0000269|PubMed:20797688}. TISSUE SPECIFICITY: Widely expressed. In the eye, expression is greatest in the retina and least in the lens and cornea. {ECO:0000269|PubMed:20797688}. +Q60738 ZNT1_MOUSE Zinc transporter 1 (ZnT-1) (Solute carrier family 30 member 1) 503 54,716 Chain (1); Glycosylation (1); Modified residue (1); Region (1); Topological domain (7); Transmembrane (6) TRANSMEM 11 31 Helical. {ECO:0000255}.; TRANSMEM 36 56 Helical. {ECO:0000255}.; TRANSMEM 79 99 Helical. {ECO:0000255}.; TRANSMEM 114 134 Helical. {ECO:0000255}.; TRANSMEM 244 264 Helical. {ECO:0000255}.; TRANSMEM 304 324 Helical. {ECO:0000255}. TOPO_DOM 1 10 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 32 35 Extracellular. {ECO:0000255}.; TOPO_DOM 57 78 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 100 113 Extracellular. {ECO:0000255}.; TOPO_DOM 135 243 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 265 303 Extracellular. {ECO:0000255}.; TOPO_DOM 325 503 Cytoplasmic. {ECO:0000255}. FUNCTION: May be involved in zinc transport out of the cell. Lethality of knockout early in gestation suggests a role of the protein in fetal zinc acquisition and retention. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Multimer. {ECO:0000305}. TISSUE SPECIFICITY: Widely expressed. +Q3URR7 ZSC10_MOUSE Zinc finger and SCAN domain-containing protein 10 (Zinc finger protein 206) 782 88,355 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (1); Helix (6); Modified residue (3); Sequence conflict (6); Turn (2); Zinc finger (14) FUNCTION: Embryonic stem (ES) cell-specific transcription factor required to maintain ES cell pluripotency. Can both activate and /or repress expression of target genes, depending on the context. Specifically binds the 5'-[GA]CGCNNGCG[CT]-3' DNA consensus sequence. Regulates expression of POU5F1/OCT4, ZSCAN4 and ALYREF/THOC4. {ECO:0000269|PubMed:16971461, ECO:0000269|PubMed:17628018, ECO:0000269|PubMed:19740739}. PTM: Methylated at Gln-485 by N6AMT1. {ECO:0000250|UniProtKB:Q96SZ4}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187, ECO:0000269|PubMed:16971461, ECO:0000269|PubMed:17628018}. SUBUNIT: Interacts with POU5F1/OCT4 and SOX2. {ECO:0000269|PubMed:19740739}. TISSUE SPECIFICITY: Embryonic stem (ES) cell-specific. Not expressed in adult, except in testis. {ECO:0000269|PubMed:16971461, ECO:0000269|PubMed:17628018}. +Q9Z1D7 ZSC12_MOUSE Zinc finger and SCAN domain-containing protein 12 (Zinc finger protein 96) (Zfp-96) 501 57,492 Chain (1); Cross-link (3); Domain (1); Sequence conflict (2); Zinc finger (8) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}. TISSUE SPECIFICITY: Testis specific. {ECO:0000269|PubMed:12860387}. +Q9R020 ZRAB2_MOUSE Zinc finger Ran-binding domain-containing protein 2 (Zinc finger protein 265) (Zinc finger, splicing) 330 37,350 Alternative sequence (1); Chain (1); Compositional bias (1); Erroneous initiation (1); Frameshift (4); Modified residue (9); Region (1); Sequence conflict (2); Zinc finger (2) FUNCTION: Splice factor required for alternative splicing of TRA2B/SFRS10 transcripts. May interfere with constitutive 5'-splice site selection (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with the C-terminal half of SNRNP70, the Arg/Ser-rich domain of AKAP17A as well as with U2AF1 and CLK1. {ECO:0000250}. DOMAIN: The RanBP2-type zinc fingers mediate binding to RNA. {ECO:0000250}. +Q6NZP1 ZRAB3_MOUSE DNA annealing helicase and endonuclease ZRANB3 (Annealing helicase 2) (AH2) (Zinc finger Ran-binding domain-containing protein 3) [Includes: DNA annealing helicase ZRANB3 (EC 3.6.4.-); Endonuclease ZRANB3 (EC 3.1.-.-)] 1069 120,896 Chain (1); Domain (3); Motif (3); Nucleotide binding (1); Region (2); Sequence conflict (10); Zinc finger (1) FUNCTION: DNA annealing helicase and endonuclease required to maintain genome stability at stalled or collapsed replication forks by facilitating fork restart and limiting inappropriate recombination that could occur during template switching events. Recruited to the sites of stalled DNA replication by polyubiquitinated PCNA and acts as a structure-specific endonuclease that cleaves the replication fork D-loop intermediate, generating an accessible 3'-OH group in the template of the leading strand, which is amenable to extension by DNA polymerase. In addition to endonuclease activity, also catalyzes the fork regression via annealing helicase activity in order to prevent disintegration of the replication fork and the formation of double-strand breaks (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}. Note=Following DNA damage, recruited to sites of DNA damage and stalled replication forks by polyubiquitinated PCNA. {ECO:0000250}. SUBUNIT: Interacts (via PIP-box and RanBP2-type zinc finger) with PCNA (when PCNA is polyubiquitinated via 'Lys-63'-linked polyubiquitin). {ECO:0000250}. DOMAIN: The PIP-box mediates the interaction with PCNA, while the RanBP2-type zinc finger mediates binding to 'Lys-63'-linked polyubiquitin. {ECO:0000250}. +Q5SSH7 ZZEF1_MOUSE Zinc finger ZZ-type and EF-hand domain-containing protein 1 2924 328,312 Alternative sequence (2); Chain (1); Domain (2); Erroneous initiation (3); Initiator methionine (1); Lipidation (1); Modified residue (12); Sequence conflict (2); Zinc finger (2) +Q0P5X5 ZBBX_MOUSE Zinc finger B-box domain-containing protein 1 716 80,339 Chain (1); Compositional bias (1); Sequence conflict (1); Zinc finger (1) +Q810J8 ZFYV1_MOUSE Zinc finger FYVE domain-containing protein 1 777 86,940 Chain (1); Sequence conflict (2); Zinc finger (2) SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack {ECO:0000250}. Endoplasmic reticulum. Note=Resides predominantly in the cisternal stacks of the Golgi. Colocalizes with TRIM13 on the perinuclear endoplasmic reticulum (By similarity). {ECO:0000250}. SUBUNIT: Binds to phosphatidylinositol 3-phosphate (PtdIns3P) through its FYVE-type zinc finger. {ECO:0000250}. +Q9CZ96 ZCRB1_MOUSE Zinc finger CCHC-type and RNA-binding motif-containing protein 1 (MADP-1) (U11/U12 small nuclear ribonucleoprotein 31 kDa protein) (U11/U12 snRNP 31 kDa protein) 217 24,583 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (1); Modified residue (3); Zinc finger (1) SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}. SUBUNIT: Component of the U11/U12 snRNPs that are part of the U12-type spliceosome. Interacts with ZRSR1 (PubMed:29617656). {ECO:0000250, ECO:0000269|PubMed:29617656}. TISSUE SPECIFICITY: Expressed at higher level in heart and testis, and at lower level in cerebellum. Weakly expressed at low level in liver. {ECO:0000269|PubMed:16959469}. +P46684 ZIC1_MOUSE Zinc finger protein ZIC 1 (Zinc finger protein of the cerebellum 1) 447 48,331 Chain (1); Compositional bias (4); Sequence conflict (1); Zinc finger (5) FUNCTION: Acts as a transcriptional activator. Involved in neurogenesis. Plays important roles in the early stage of organogenesis of the CNS, as well as during dorsal spinal cord development and maturation of the cerebellum. Involved in the spatial distribution of mossy fiber (MF) neurons within the pontine gray nucleus (PGN). Plays a role in the regulation of MF axon pathway choice. Promotes MF migration towards ipsilaterally-located cerebellar territories. May have a role in shear flow mechanotransduction in osteocytes. Retains nuclear GLI1 and GLI3 in the cytoplasm. Binds to the minimal GLI-consensus sequence 5'-TGGGTGGTC-3'. {ECO:0000269|PubMed:11053430, ECO:0000269|PubMed:11238441, ECO:0000269|PubMed:11944941, ECO:0000269|PubMed:15207726, ECO:0000269|PubMed:19303920, ECO:0000269|PubMed:20354137, ECO:0000269|PubMed:7931345}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Localizes in the cytoplasm in presence of MDFIC overexpression. SUBUNIT: Interacts (via the C2H2-type domains 3, 4 and 5) with MDFIC (via the C2H2-type domains 3, 4 and 5). Interacts with GLI1; the interaction enhances transcription activation. Interacts with GLI2. Interacts with GLI3; the interaction enhances transcription activation. {ECO:0000269|PubMed:11238441, ECO:0000269|PubMed:15207726}. DOMAIN: The C2H2-type 3, 4 and 5 zinc finger domains are necessary for transcription activation. TISSUE SPECIFICITY: Expressed in osteoblasts (at protein level). Expressed in the CNS. A high level expression is seen in the cerebellum, while a low level expression is seen in the olfactory bulb, diencephalon, and brainstem. Expressed in lumbar spine and iliac crest. {ECO:0000269|PubMed:19303920, ECO:0000269|PubMed:20354137, ECO:0000269|PubMed:7931345}. +Q7TS63 ZFAT_MOUSE Zinc finger protein ZFAT (Zinc finger protein 406) 1237 137,883 Alternative sequence (2); Beta strand (4); Chain (1); Helix (2); Zinc finger (19) FUNCTION: May be involved in transcriptional regulation. Overexpression causes down-regulation of a number of genes involved in the immune response. Some genes are also up-regulated. {ECO:0000269|PubMed:18329245}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18329245}. Cytoplasm, cytosol {ECO:0000269|PubMed:18329245}. TISSUE SPECIFICITY: Detected in spleen and thymus but not in liver, muscle, heart, kidney, brain, bone marrow or pancreas. Expressed in CD19+, CD4+ and CD8+ lymphocytes but not in CD11b+ lymphocytes or peritoneal macrophages (at protein level). {ECO:0000269|PubMed:18329245}. +Q8VIG0 ZCH14_MOUSE Zinc finger CCHC domain-containing protein 14 (BDG-29) 956 99,835 Alternative sequence (2); Chain (1); Compositional bias (6); Erroneous initiation (1); Zinc finger (1) +Q9EQB9 ZN287_MOUSE Zinc finger protein 287 (Zfp-287) (Zinc finger protein SKAT-2) 759 86,635 Chain (1); Domain (2); Sequence conflict (5); Zinc finger (14) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: Expressed in brain and at low levels in kidney and spleen and few hematopoietic cell lines. +Q6IQX8 ZN219_MOUSE Zinc finger protein 219 726 77,796 Chain (1); Compositional bias (1); Modified residue (5); Sequence conflict (2); Zinc finger (9) FUNCTION: Transcriptional regulator (PubMed:20940257). Recognizes and binds 2 copies of the core DNA sequence motif 5'-GGGGG-3' (PubMed:20940257). Binds to the HMGN1 promoter and may repress HMGN1 expression (By similarity). Regulates SNCA expression in primary cortical neurons (By similarity). Binds to the COL2A1 promoter and activates COL2A1 expression, as part of a complex with SOX9 (PubMed:20940257). Plays a role in chondrocyte differentiation (PubMed:20940257). {ECO:0000250|UniProtKB:Q9P2Y4, ECO:0000269|PubMed:20940257}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20940257}. SUBUNIT: Interacts with SOX9 (via C-terminus). {ECO:0000269|PubMed:20940257}. DOMAIN: C2H2-type zinc-finger domains 5 and 6 are important for the interaction with SOX9. {ECO:0000269|PubMed:20940257}. TISSUE SPECIFICITY: Highly expressed in primary chondrocytes, heart, pancreas and testis. {ECO:0000269|PubMed:20940257}. +Q9R0B7 ZN346_MOUSE Zinc finger protein 346 (Just another zinc finger protein) 294 32,698 Chain (1); Cross-link (2); Metal binding (8); Modified residue (1); Mutagenesis (4); Zinc finger (4) FUNCTION: Binds with low affinity to dsDNA and ssRNA, and with high affinity to dsRNA, with no detectable sequence specificity (By similarity) (PubMed:10488071). May bind to specific miRNA hairpins (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9UL40, ECO:0000269|PubMed:10488071}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Nuclear at steady state, primarily in the nucleolus. Shuttles between the nucleus and cytoplasm when associated with XPO5 (By similarity). {ECO:0000250}. SUBUNIT: Forms a heteromeric complex with XPO5 and ILF3. Found in a nuclear export complex with XPO5, RAN, ILF3, ZNF346 and double-stranded RNA. Interacts with XPO5. Interacts with ILF3 in an RNA-independent manner (By similarity). {ECO:0000250}. DOMAIN: The zinc-finger domains are required for binding to dsRNA, and also for nuclear localization. TISSUE SPECIFICITY: Expressed in all tissues tested, including heart, brain, spleen, lung, liver, muscle, kidney and testis. Exogenous expression induced apoptosis. {ECO:0000269|PubMed:10488071}. +Q8C0P7 ZN451_MOUSE E3 SUMO-protein ligase ZNF451 (EC 2.3.2.-) (E3 SUMO-protein transferase ZNF451) (Zinc finger protein 451) 1056 120,070 Chain (1); Cross-link (28); Modified residue (3); Motif (1); Region (6); Zinc finger (12) Protein modification; protein sumoylation. FUNCTION: E3 SUMO-protein ligase; has a preference for SUMO2 and SUMO3 and facilitates UBE2I/UBC9-mediated sumoylation of target proteins. Plays a role in protein SUMO2 modification in response to stress caused by DNA damage and by proteasome inhibitors (in vitro). Required for MCM4 sumoylation. Has no activity with SUMO1 (PubMed:26524493). Preferentially transfers an additional SUMO2 chain onto the SUMO2 consensus site 'Lys-11'. Negatively regulates transcriptional activation mediated by the SMAD4 complex in response to TGF-beta signaling. Inhibits EP300-mediated acetylation of histone H3 at 'Lys-9'. Plays a role in regulating the transcription of AR targets (By similarity). {ECO:0000250|UniProtKB:Q9Y4E5, ECO:0000269|PubMed:26524493}. PTM: Sumoylated. Predominantly sumoylated on the N-terminal region that is important for interaction with SUMO1 and SUMO2. Sumoylation is important for localization in nuclear granules; desumoylation leads to diffuse nucleoplasmic location. Autosumoylated (in vitro). Sumoylation enhances E3 SUMO-protein ligase activity. {ECO:0000250|UniProtKB:Q9Y4E5}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y4E5}. Nucleus, PML body {ECO:0000250|UniProtKB:Q9Y4E5}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9Y4E5}. Note=Colocalizes with UBE2I/UBC9, SUMO1 and SUMO2 in nuclear granules; this probably requires sumoylation. Desumoylation leads to diffuse nucleoplasmic location. {ECO:0000250|UniProtKB:Q9Y4E5}. SUBUNIT: Homooligomer. Interacts (via N-terminal region) with SUMO1. Interacts (via N-terminal region) with SUMO2. Interacts simultaneously with two SUMO2 chains. Identified in a complex with SUMO2 and UBE2I/UBC9, where one ZNF451 interacts with one UBE2I/UBC9 and two SUMO2 chains, one bound to the UBE2I/UBC9 active site and the other to another region of the same UBE2I/UBC9 molecule. Interacts (via C-terminus) with ubiquitin. Interacts (via N-terminal zinc-finger domains) with SMAD4 (via MH2 domain). Interacts with SMAD2 and SMAD3. Identified in a complex that contains at least ZNF451, SMAD2, SMAD3 and SMAD4. Interacts with EP300. Inhibits interaction between EP300 and the SMAD4 complex. {ECO:0000250|UniProtKB:Q9Y4E5}. DOMAIN: Binds UBE2I/UBC9 and two SUMO2 molecules via its N-terminus. The most N-terminal region interacts with the SUMO2 chain that is covalently bound to the UBE2I/UBC9 active site, while the second region interacts with another SUMO2 that is non-covalently associated with the same UBE2I/UBC9 chain. {ECO:0000250|UniProtKB:Q9Y4E5}. +Q5SSZ7 ZNRF3_MOUSE E3 ubiquitin-protein ligase ZNRF3 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase ZNRF3) (Zinc/RING finger protein 3) 913 98,967 Alternative sequence (3); Beta strand (12); Chain (1); Compositional bias (1); Erroneous initiation (2); Helix (6); Sequence conflict (7); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (1); Zinc finger (1) TRANSMEM 217 237 Helical. {ECO:0000255}. TOPO_DOM 53 216 Extracellular. {ECO:0000255}.; TOPO_DOM 238 913 Cytoplasmic. {ECO:0000255}. Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that acts as a negative regulator of the Wnt signaling pathway by mediating the ubiquitination and subsequent degradation of Wnt receptor complex components Frizzled and LRP6. Acts on both canonical and non-canonical Wnt signaling pathway. Acts as a tumor suppressor in the intestinal stem cell zone by inhibiting the Wnt signaling pathway, thereby resticting the size of the intestinal stem cell zone (PubMed:22575959, PubMed:22895187). Along with RSPO2 and RNF43, constitutes a master switch that governs limb specification (By similarity). {ECO:0000250|UniProtKB:Q08D68, ECO:0000269|PubMed:22575959, ECO:0000269|PubMed:22895187}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Interacts with LRP6, FZD4, FZD5, FZD6 and FZD8. Interacts with RSPO1; interaction promotes indirect interaction with LGR4 and membrane clearance of ZNRF3 (By similarity). {ECO:0000250}. +Q3UVU3 ZNT10_MOUSE Zinc transporter 10 (ZnT-10) (Solute carrier family 30 member 10) 470 50,911 Alternative sequence (1); Chain (1); Compositional bias (1); Region (1); Sequence conflict (1); Topological domain (7); Transmembrane (6) TRANSMEM 11 31 Helical. {ECO:0000255}.; TRANSMEM 35 55 Helical. {ECO:0000255}.; TRANSMEM 82 102 Helical. {ECO:0000255}.; TRANSMEM 114 134 Helical. {ECO:0000255}.; TRANSMEM 234 254 Helical. {ECO:0000255}.; TRANSMEM 271 291 Helical. {ECO:0000255}. TOPO_DOM 1 10 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 32 34 Extracellular. {ECO:0000255}.; TOPO_DOM 56 81 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 103 113 Extracellular. {ECO:0000255}.; TOPO_DOM 135 233 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 255 270 Extracellular. {ECO:0000255}.; TOPO_DOM 292 470 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a pivotal role in manganese transport. Manganese is an essential cation for the function of several enzymes, including some crucially important for the metabolism of neurotransmitters and other neuronal metabolic pathways. However, elevated levels of manganese are cytotoxic and induce oxidative stress, mitochondrial dysfunction and apoptosis. Acts as manganese efflux transporter and confers protection against manganese-induced cell death. Also acts as zinc transporter involved in zinc homeostasis. Seems to mediate zinc transport into early endosomes and recycling endosomes to prevent zinc toxicity; the function may be regulated by heterodimerization with other zinc transporters of the SLC30A subfamily. The SLC30A3:SLC30A10 heterodimer is involved in zinc transport-dependent regulation of the EGFR/ERK transduction pathway in endosomes. May be involved in regulation of zinc-dependent senescence of vascular smooth muscle cells. {ECO:0000250|UniProtKB:Q6XR72}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6XR72}; Multi-pass membrane protein {ECO:0000305}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q6XR72}. Recycling endosome {ECO:0000250|UniProtKB:Q6XR72}. Early endosome {ECO:0000250|UniProtKB:Q6XR72}. Note=Relocalized from the trans-Golgi network to the plasma membrane upon elevated extracellular Zn concentrations. {ECO:0000250|UniProtKB:Q6XR72}. SUBUNIT: Forms homodimers. Forms heterodimers and high-molecular weight oligomers with SLC30A3, SLC30A2 and SLC30A4; heterodimerization is mediated by covalent-bound tyrosine residues and occurs probably in a tissue-specific manner. {ECO:0000250|UniProtKB:Q6XR72}. TISSUE SPECIFICITY: Specifically expressed in fetal liver and fetal brain. +A2BFL2 ZY11A_MOUSE Protein zyg-11 homolog A 627 70,404 Chain (1); Repeat (3); Sequence conflict (1) FUNCTION: Probably acts as target recruitment subunit in an E3 ubiquitin ligase complex ZYGA-CUL2-elongin BC. {ECO:0000250}. +Q3UFS0 ZY11B_MOUSE Protein zyg-11 homolog B 744 83,991 Alternative sequence (4); Chain (1); Repeat (3); Sequence conflict (5) FUNCTION: Probably acts as target recruitment subunit in the E3 ubiquitin ligase complex ZYG11B-CUL2-Elongin BC. {ECO:0000250}. SUBUNIT: Interacts with TCEB1/Elongin C. Part of an E3 ubiquitin ligase complex including ZYG11B, CUL2 and Elongin BC (By similarity). {ECO:0000250}. +Q07230 ZSCA2_MOUSE Zinc finger and SCAN domain-containing protein 2 (Zinc finger protein 29) (Zfp-29) 614 68,714 Beta strand (5); Chain (1); Domain (1); Helix (7); Turn (6); Zinc finger (14) FUNCTION: May be involved in transcriptional regulation during the post-meiotic stages of spermatogenesis. {ECO:0000269|PubMed:1937051}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187, ECO:0000269|PubMed:1937051}. TISSUE SPECIFICITY: In the adult, predominantly found in spermatids. Also present in the embryo. {ECO:0000269|PubMed:1937051}. +Q6KAQ7 ZZZ3_MOUSE ZZ-type zinc finger-containing protein 3 910 102,307 Alternative sequence (5); Chain (1); Cross-link (3); DNA binding (1); Domain (1); Modified residue (8); Zinc finger (1) FUNCTION: Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625}. SUBUNIT: Component of the ADA2A-containing complex (ATAC), composed of KAT14, KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1. {ECO:0000250}. +Q9WUK6 ZBT18_MOUSE Zinc finger and BTB domain-containing protein 18 (58 kDa repressor protein) (Transcriptional repressor RP58) (Zinc finger protein 238) (Zfp-238) 522 58,385 Chain (1); Cross-link (1); Domain (1); Erroneous initiation (1); Modified residue (3); Region (1); Sequence conflict (2); Zinc finger (4) FUNCTION: Transcriptional repressor that plays a role in various developmental processes such as myogenesis and brain development. Specifically binds the consensus DNA sequence 5'-[AC]ACATCTG[GT][AC]-3' which contains the E box core, and acts by recruiting chromatin remodeling multiprotein complexes. Plays a key role in myogenesis by directly repressing the expression of ID2 and ID3, 2 inhibitors of skeletal myogenesis. Also involved in controlling cell division of progenitor cells and regulating the survival of postmitotic cortical neurons. May also play a role in the organization of chromosomes in the nucleus. {ECO:0000269|PubMed:19409883, ECO:0000269|PubMed:20059953}. SUBCELLULAR LOCATION: Nucleus. Note=Associates with condensed chromatin. SUBUNIT: Interacts with DNMT3A. {ECO:0000250}. +Q9D0L1 ZBED3_MOUSE Zinc finger BED domain-containing protein 3 (Axin-interacting protein) 228 25,609 Chain (1); Coiled coil (1); Motif (1); Mutagenesis (2); Zinc finger (1) FUNCTION: Acts as a positive regulator in the activation of the canonical Wnt/beta-catenin signaling pathway by stabilizing cytoplasmic beta-catenin. Involved in transcription activation of Wnt target gene expression. {ECO:0000269|PubMed:19141611}. PTM: Dual phosphorylation on serine and tyrosine residues of the cytoplasmic PPPSP motif by GSK3 and CK1 may be required for AXIN1-binding. {ECO:0000305}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19141611}. Membrane {ECO:0000269|PubMed:19141611}. Note=Colocalizes with AXIN1 in the cytoplasm. SUBUNIT: Interacts (via PPPSP motif) with AXIN1; the interaction is direct, enhanced by protein kinase GSK3B and casein kinase CSNK1E activities and decreases GSK3B-induced beta-catenin serine and threonine phosphorylations. {ECO:0000269|PubMed:19141611}. +Q80WQ9 ZBED4_MOUSE Zinc finger BED domain-containing protein 4 1168 130,402 Chain (1); Compositional bias (2); Cross-link (2); Modified residue (1); Sequence caution (1); Sequence conflict (1); Zinc finger (4) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000269|PubMed:19369242}. SUBUNIT: Homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Thymus and retina. In the retina, expressed in the cone photoreceptors. {ECO:0000269|PubMed:19369242}. +Q9CYA6 ZCHC8_MOUSE Zinc finger CCHC domain-containing protein 8 (TRAMP-like complex RNA-binding factor ZCCHC8) 709 78,026 Chain (1); Coiled coil (1); Compositional bias (3); Initiator methionine (1); Modified residue (8); Sequence conflict (5); Zinc finger (1) FUNCTION: Scaffolding subunit of the trimeric nuclear exosome targeting (NEXT) complex, a complex that directs a subset of non-coding short-lived RNAs for exosomal degradation. The RNA exosome is fundamental for the degradation of RNA in eukaryotic nuclei. Substrate targeting is facilitated by its cofactor MTREX, which links to RNA-binding protein adapters. May be involved in pre-mRNA splicing. {ECO:0000250|UniProtKB:Q6NZY4}. PTM: Phosphorylation at Thr-495 by GSK3 is triggered in cells entering mitosis. {ECO:0000250|UniProtKB:Q6NZY4}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q6NZY4}. Note=Excluded from nucleolus. {ECO:0000250|UniProtKB:Q6NZY4}. SUBUNIT: Component of a nuclear TRAMP-like complex, an ATP-dependent exosome regulatory complex consisting of a helicase (MTREX), an oligadenylate polymerase (TENT4B or TENT4A), and a substrate specific RNA-binding factor (ZCCHC7 or ZCCHC8). Several TRAMP-like complexes exist with specific compositions and are associated with nuclear, or nucleolar RNA exosomes. Identified in the spliceosome C complex. Component of the nuclear exosome targeting (NEXT) complex composed of MTREX, ZCCHC8, and RBM7 that directs a subset of non-coding short-lived RNAs for exosomal degradation. Interacts with proteins involved in RNA processing and degradation such as MTREX and RBM7. {ECO:0000250|UniProtKB:Q6NZY4}. +Q8K088 ZBTB6_MOUSE Zinc finger and BTB domain-containing protein 6 (Zinc finger protein 482) 423 48,188 Chain (1); Domain (1); Modified residue (1); Sequence conflict (1); Zinc finger (4) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +P10076 ZFP26_MOUSE Zinc finger protein 26 (Zfp-26) (Protein mKR3) 861 97,989 Chain (1); Domain (1); Sequence conflict (22); Zinc finger (23) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q8VDZ4 ZDHC5_MOUSE Palmitoyltransferase ZDHHC5 (EC 2.3.1.225) (Zinc finger DHHC domain-containing protein 5) (DHHC-5) 715 77,501 Active site (1); Alternative sequence (2); Chain (1); Domain (1); Erroneous initiation (1); Modified residue (27); Mutagenesis (1); Topological domain (5); Transmembrane (4) TRANSMEM 14 34 Helical. {ECO:0000255}.; TRANSMEM 53 73 Helical. {ECO:0000255}.; TRANSMEM 149 169 Helical. {ECO:0000255}.; TRANSMEM 192 212 Helical. {ECO:0000255}. TOPO_DOM 1 13 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 35 52 Extracellular. {ECO:0000255}.; TOPO_DOM 74 148 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 170 191 Extracellular. {ECO:0000255}.; TOPO_DOM 213 715 Cytoplasmic. {ECO:0000255}. FUNCTION: Palmitoyl acyltransferase for the G-protein coupled receptor SSTR5 and for FLOT2. {ECO:0000269|PubMed:21820437, ECO:0000269|PubMed:22081607}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21820437}. Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. DOMAIN: The DHHC domain is required for palmitoyltransferase activity. {ECO:0000250}. +Q64318 ZEB1_MOUSE Zinc finger E-box-binding homeobox 1 (Delta EF1) (Transcription factor 8) (TCF-8) (Zinc finger homeobox protein 1a) (MEB1) 1117 122,465 Chain (1); Compositional bias (1); Cross-link (14); DNA binding (1); Modified residue (10); Sequence conflict (13); Zinc finger (7) FUNCTION: Acts as a transcriptional repressor. Binds to E-box sequences in the immunoglobulin heavy chain enhancer as well as in the regulatory regions of many other tissue-specific genes. Represses E-cadherin promoter and induces an epithelial-mesenchymal transition (EMT) by recruiting SMARCA4/BRG1. Represses BCL6 transcription in the presence of the corepressor CTBP1 (By similarity). Positively regulates neuronal differentiation. Represses RCOR1 transcription activation during neurogenesis. Represses transcription by binding to the E box (5'-CANNTG-3'). Promotes tumorigenicity by repressing stemness-inhibiting microRNAs. {ECO:0000250, ECO:0000269|PubMed:19935649, ECO:0000269|PubMed:20346398}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20346398}. SUBUNIT: Interacts (via N-terminus) with SMARCA4/BRG1. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the external germinal layer (EGL) and internal granular layer (IGL) of the cerebellum (at protein level). {ECO:0000269|PubMed:20346398}. +Q8BZ94 ZMAT4_MOUSE Zinc finger matrin-type protein 4 229 25,671 Alternative sequence (2); Chain (1); Zinc finger (4) SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00130}. +Q91VW9 ZKSC3_MOUSE Zinc finger protein with KRAB and SCAN domains 3 (SCAN-KRAB-zinc finger protein) (Zinc finger protein 306) (Zinc finger protein 307) (Zinc finger protein 47 homolog) (Zf47) (Zfp-47) 553 62,642 Chain (1); Cross-link (1); Domain (2); Frameshift (1); Modified residue (6); Sequence conflict (5); Zinc finger (7) FUNCTION: Transcriptional factor that binds to the consensus sequence 5'-[GT][AG][AGT]GGGG-3' and acts as a repressor of autophagy. Specifically represses expression of genes involved in autophagy and lysosome biogenesis/function such as MAP1LC3B, ULK1 or WIPI2. Associates with chromatin at the ITGB4 and VEGF promoters (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}. Cytoplasm {ECO:0000250}. Note=Mainly localizes in the nucleus. Under starvation conditions translocates to the cytoplasm, allowing expression of target genes involved in autophagy and lysosome biogenesis/function (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in heart, brain, spleen, lung, liver, skeletal muscle, kidney and testis. {ECO:0000269|PubMed:11342224}. +O88939 ZBT7A_MOUSE Zinc finger and BTB domain-containing protein 7A (Leukemia/lymphoma-related factor) (POZ and Krueppel erythroid myeloid ontogenic factor) (POK erythroid myeloid ontogenic factor) (Pokemon) 569 60,281 Alternative sequence (1); Chain (1); Cross-link (2); Domain (1); Modified residue (3); Region (3); Sequence conflict (2); Zinc finger (4) FUNCTION: Transcription factor that represses the transcription of a wide range of genes involved in cell proliferation and differentiation (PubMed:15337766, PubMed:15662416, PubMed:17495164, PubMed:26816381, PubMed:29813070). Directly and specifically binds to the consensus sequence 5'-[GA][CA]GACCCCCCCCC-3' and represses transcription both by regulating the organization of chromatin and through the direct recruitment of transcription factors to gene regulatory regions (PubMed:15337766, PubMed:15662416, PubMed:26816381, PubMed:29813070). Negatively regulates SMAD4 transcriptional activity in the TGF-beta signaling pathway through these two mechanisms (By similarity). That is, recruits the chromatin regulator HDAC1 to the SMAD4-DNA complex and in parallel prevents the recruitment of the transcriptional activators CREBBP and EP300 (By similarity). Collaborates with transcription factors like RELA to modify the accessibility of gene transcription regulatory regions to secondary transcription factors (PubMed:29813070). Also directly interacts with transcription factors like SP1 to prevent their binding to DNA (By similarity). Functions as an androgen receptor/AR transcriptional corepressor by recruiting NCOR1 and NCOR2 to the androgen response elements/ARE on target genes (By similarity). Thereby, negatively regulates androgen receptor signaling and androgen-induced cell proliferation (By similarity). Involved in the switch between fetal and adult globin expression during erythroid cells maturation (PubMed:26816381). Through its interaction with the NuRD complex regulates chromatin at the fetal globin genes to repress their transcription (PubMed:26816381). Specifically represses the transcription of the tumor suppressor ARF isoform from the CDKN2A gene (PubMed:15662416). Efficiently abrogates E2F1-dependent CDKN2A transactivation (PubMed:15662416). Regulates chondrogenesis through the transcriptional repression of specific genes via a mechanism that also requires histone deacetylation (PubMed:15337766). Regulates cell proliferation through the transcriptional regulation of genes involved in glycolysis (By similarity). Involved in adipogenesis through the regulation of genes involved in adipocyte differentiation (By similarity). Plays a key role in the differentiation of lymphoid progenitors into B and T lineages (PubMed:17495164). Promotes differentiation towards the B lineage by inhibiting the T-cell instructive Notch signaling pathway through the specific transcriptional repression of Notch downstream target genes (PubMed:17495164). Also regulates osteoclast differentiation (By similarity). May also play a role, independently of its transcriptional activity, in double-strand break repair via classical non-homologous end joining/cNHEJ (PubMed:26446488). Recruited to double-strand break sites on damage DNA, interacts with the DNA-dependent protein kinase complex and directly regulates its stability and activity in DNA repair (PubMed:26446488). May also modulate the splicing activity of KHDRBS1 toward BCL2L1 in a mechanism which is histone deacetylase-dependent and thereby negatively regulates the pro-apoptotic effect of KHDRBS1 (By similarity). {ECO:0000250|UniProtKB:O95365, ECO:0000250|UniProtKB:Q9QZ48, ECO:0000269|PubMed:15337766, ECO:0000269|PubMed:15662416, ECO:0000269|PubMed:17495164, ECO:0000269|PubMed:26446488, ECO:0000269|PubMed:26816381, ECO:0000269|PubMed:29813070}. PTM: Sumoylated. Undergoes sumoylation with SUMO1 that may regulate its transcriptional activity. {ECO:0000250|UniProtKB:O95365}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15662416, ECO:0000269|PubMed:9927193}. Note=Recruited to double-strand break sites of damaged DNA. {ECO:0000269|PubMed:26446488}. SUBUNIT: Homodimer (By similarity). Interacts with BCL6 (PubMed:9927193). Interacts with RELA; involved in the control by RELA of the accessibility of target gene promoters (PubMed:29813070). Interacts with AR (via NR LBD domain); the interaction is direct and androgen-dependent (By similarity). Interacts with NCOR1 (By similarity). Interacts with NCOR2 (By similarity). Interacts with SMAD4; the interaction is direct and stimulated by TGFB1 (By similarity). Interacts with HDAC1 (By similarity). Interacts with SP1; ZBTB7A prevents the binding to GC-rich motifs in promoters and represses the transcriptional activity of SP1 (By similarity). Interacts with the DNA-dependent protein kinase complex/DNA-PKc (PubMed:26446488). Interacts with KHDRBS1; negatively regulates KHDRBS1 splicing activity (By similarity). {ECO:0000250|UniProtKB:O95365, ECO:0000269|PubMed:26446488, ECO:0000269|PubMed:29813070, ECO:0000269|PubMed:9927193}. DOMAIN: The BTB domain mediates the interaction with the androgen receptor/AR and HDAC1. Also mediates the interaction with SP1. {ECO:0000250|UniProtKB:O95365}. TISSUE SPECIFICITY: Widely expressed (PubMed:9927193). In normal thymus, expressed in medullary epithelial cells and Hassle's corpuscles (at protein level) (PubMed:15662416). In the spleen, mainly expressed in the white pulp germinal centers (at protein level) (PubMed:15662416). Up-regulated in thymic lymphomas (PubMed:15662416). {ECO:0000269|PubMed:15662416, ECO:0000269|PubMed:9927193}. +Q5Y5T5 ZDHC8_MOUSE Probable palmitoyltransferase ZDHHC8 (EC 2.3.1.225) (Zinc finger DHHC domain-containing protein 8) (DHHC-8) 762 82,031 Active site (1); Chain (1); Domain (1); Modified residue (8); Topological domain (5); Transmembrane (4) TRANSMEM 14 34 Helical. {ECO:0000255}.; TRANSMEM 53 73 Helical. {ECO:0000255}.; TRANSMEM 149 169 Helical. {ECO:0000255}.; TRANSMEM 191 211 Helical. {ECO:0000255}. TOPO_DOM 1 13 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 35 52 Lumenal. {ECO:0000255}.; TOPO_DOM 74 148 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 170 190 Lumenal. {ECO:0000255}.; TOPO_DOM 212 762 Cytoplasmic. {ECO:0000255}. FUNCTION: Palmitoyltransferase involved in glutamatergic transmission. Mediates palmitoylation of ABCA1. {ECO:0000269|PubMed:15184899}. SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. DOMAIN: The DHHC domain is required for palmitoyltransferase activity. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain cortex and hippocampus. {ECO:0000269|PubMed:15184899}. +O70230 ZN143_MOUSE Zinc finger protein 143 (Zfp-143) (Selenocysteine tRNA gene transcription-activating factor) (mStaf) 638 69,040 Alternative sequence (2); Chain (1); Cross-link (2); Erroneous initiation (4); Frameshift (1); Modified residue (2); Sequence conflict (8); Zinc finger (7) FUNCTION: Transcriptional activator. Activates the gene for selenocysteine tRNA (tRNAsec). Binds to the SPH motif of small nuclear RNA (snRNA) gene promoters. Participates in efficient U6 RNA polymerase III transcription via its interaction with CHD8 (By similarity). {ECO:0000250, ECO:0000269|PubMed:9535833}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Interacts with CHD8. {ECO:0000250}. +Q99ML0 ZMY10_MOUSE Zinc finger MYND domain-containing protein 10 (Protein BLu) 440 50,646 Chain (1); Sequence conflict (1); Zinc finger (1) FUNCTION: Plays a role in axonemal structure organization and motility (PubMed:29601588). Involved in axonemal pre-assembly of inner and outer dynein arms (IDA and ODA, respectively) for proper axoneme building for cilia motility (PubMed:29601588). May act by indirectly regulating transcription of dynein proteins (By similarity). {ECO:0000250, ECO:0000269|PubMed:29601588}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6AXZ5}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000250|UniProtKB:Q6AXZ5}. Apical cell membrane {ECO:0000269|PubMed:29601588}. Note=Localizes to sites proximal to the axoneme. {ECO:0000250}. SUBUNIT: Interacts (via C-terminus) with LRRC6 (via CS domain); this interaction stabilizes LRRC6 at the protein level. Interacts (via C-terminus) with DNAL1; this interaction stabilizes DNAL1 at the protein level. Interacts with DNAAF4, HSPA8, IQUB, RUVBL2 and TCTEX1D1. {ECO:0000250|UniProtKB:O75800}. TISSUE SPECIFICITY: Expressed in the testis. Expressed in the tracheal epithelium (PubMed:29601588). Restricted to regions containing motile cilia (PubMed:23891471). {ECO:0000269|PubMed:23891471, ECO:0000269|PubMed:29601588}. +P59268 ZDHC9_MOUSE Palmitoyltransferase ZDHHC9 (EC 2.3.1.225) (Zinc finger DHHC domain-containing protein 9) (DHHC-9) (DHHC9) 364 40,940 Active site (1); Chain (1); Domain (1); Topological domain (5); Transmembrane (4) TRANSMEM 36 56 Helical. {ECO:0000255}.; TRANSMEM 64 84 Helical. {ECO:0000255}.; TRANSMEM 184 204 Helical. {ECO:0000255}.; TRANSMEM 229 249 Helical. {ECO:0000255}. TOPO_DOM 1 35 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 57 63 Lumenal. {ECO:0000255}.; TOPO_DOM 85 183 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 205 228 Lumenal. {ECO:0000255}.; TOPO_DOM 250 364 Cytoplasmic. {ECO:0000255}. FUNCTION: The ZDHHC9-GOLGA7 complex is a palmitoyltransferase specific for HRAS and NRAS. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with GOLGA7. {ECO:0000250}. DOMAIN: The DHHC domain is required for palmitoyltransferase activity. {ECO:0000250}. +Q61624 ZN148_MOUSE Zinc finger protein 148 (Beta enolase repressor factor 1) (G-rich box-binding protein) (Transcription factor BFCOL1) (Transcription factor ZBP-89) (Zinc finger DNA-binding protein 89) 794 88,751 Chain (1); Cross-link (11); Modified residue (9); Sequence conflict (3); Zinc finger (4) FUNCTION: Involved in transcriptional regulation. Represses the transcription of a number of genes including gastrin, stromelysin and enolase. Binds to the G-rich box in the enhancer region of these genes. {ECO:0000269|PubMed:9417107}. PTM: Sumoylated with SUMO2. Desumoylated by SENP3, resulting in the stimulation of transcription of its target genes. {ECO:0000269|PubMed:22872859}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with HNRNPDL (By similarity). Interacts with the 5FMC complex; the interaction requires association with CHTOP (PubMed:22872859). Interacts with CAVIN1 (PubMed:10727401). {ECO:0000250|UniProtKB:Q9UQR1, ECO:0000269|PubMed:10727401, ECO:0000269|PubMed:22872859}. TISSUE SPECIFICITY: Strong expression detected in brain, lung, liver and kidney, with lower levels detected in spleen, skeletal muscle, testis and heart. {ECO:0000269|PubMed:9417107}. +P15620 ZN271_MOUSE Zinc finger protein 271 (Zinc finger protein 35) (Zfp-35) 580 67,036 Chain (1); Compositional bias (1); Sequence conflict (1); Zinc finger (18) FUNCTION: May act to control gene activity during the pachytene stage of meiotic prophase. May function as a transcription activator. SUBCELLULAR LOCATION: Nucleus. TISSUE SPECIFICITY: Selectively expressed in adult testis. {ECO:0000269|PubMed:2104800}. +Q9JMD0 ZN207_MOUSE BUB3-interacting and GLEBS motif-containing protein ZNF207 (BuGZ) (49 kDa zinc finger protein) (Zinc finger protein 207) 495 52,793 Alternative sequence (3); Chain (1); Compositional bias (3); Mutagenesis (1); Region (2); Zinc finger (2) FUNCTION: Kinetochore- and microtubule-binding protein that plays a key role in spindle assembly. ZNF207/BuGZ is mainly composed of disordered low-complexity regions and undergoes phase transition or coacervation to form temperature-dependent liquid droplets. Coacervation promotes microtubule bundling and concentrates tubulin, promoting microtubule polymerization and assembly of spindle and spindle matrix by concentrating its building blocks (PubMed:26388440). Also acts as a regulator of mitotic chromosome alignment by mediating the stability and kinetochore loading of BUB3. Mechanisms by which BUB3 is protected are unclear: according to a first report, ZNF207/BuGZ may act by blocking ubiquitination and proteasomal degradation of BUB3. According to another report, the stabilization is independent of the proteasome (By similarity). {ECO:0000250|UniProtKB:O43670, ECO:0000269|PubMed:26388440}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9832628}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:O43670}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:O43670}. Note=Localizes primarily to the nucleus in interphase, concentrates at kinetochores prior to nuclear envelope breakdown and during early prometaphase, and disappears from kinetochores upon microtubule-binding. {ECO:0000250|UniProtKB:O43670}. SUBUNIT: Interacts (via GLEBS region) with BUB3. {ECO:0000269|PubMed:26388440}. DOMAIN: Mainly composed of disordered low-complexity regions outside of the C2H2-type zinc fingers. Coacervation depends on hydrophobic and aromatic Phe and Tyr in the disordered low-complexity region, that may promote coacervation by forming intermolecular hydrophobic interactions. {ECO:0000269|PubMed:26388440}.; DOMAIN: The GLEBS region mediates interaction with BUB3. {ECO:0000250|UniProtKB:O43670}.; DOMAIN: The microtubule-binding region is required for efficient loading of BUB3 onto kinetochores and proper mitosis. {ECO:0000250|UniProtKB:O43670}. TISSUE SPECIFICITY: In day-13 embryo, strongly expressed in the nervous system (brain, spinal cord and dorsal root ganglia), with strong to weak expression in other regions. Continues to be strongly expressed in the neonatal brain while expression is weak in the brain and spinal cord of adult. {ECO:0000269|PubMed:9832628}. +B2RVL6 ZCH24_MOUSE Zinc finger CCHC domain-containing protein 24 241 26,961 Chain (1); Modified residue (2); Zinc finger (1) +Q9D0B1 ZN524_MOUSE Zinc finger protein 524 321 34,809 Chain (1); DNA binding (1); Frameshift (1); Sequence conflict (1); Zinc finger (4) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q8BIQ8 ZN770_MOUSE Zinc finger protein 770 705 81,252 Chain (1); Compositional bias (1); Cross-link (6); Sequence conflict (3); Zinc finger (11) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q0GGX2 ZN541_MOUSE Zinc finger protein 541 (Spermatogenic cell HDAC-interacting protein 1) 1363 148,297 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (2); Sequence conflict (2); Zinc finger (5) FUNCTION: Component of some chromatin remodeling multiprotein complex that plays a role during spermatogenesis. {ECO:0000269|PubMed:18849567}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00512, ECO:0000255|PROSITE-ProRule:PRU00624, ECO:0000269|PubMed:17662146, ECO:0000269|PubMed:18849567}. SUBUNIT: Interacts with DNTTIP1 (PubMed:18849567). Identified in a complex with KCDT19, HDAC1 and HSPA2 (PubMed:18849567). Component of a histone deacetylase complex containing DNTTIP1, ZNF541, HDAC1 and HDAC2 (By similarity). {ECO:0000250|UniProtKB:Q9H0D2, ECO:0000269|PubMed:18849567}. TISSUE SPECIFICITY: Germ-cell-specific. Specifically present in testicular spermatogenic cells, but not in testicular and mature sperm. During spermatogenesis, it is present in spermatocytes and round spermatids only (at protein level). {ECO:0000269|PubMed:17662146, ECO:0000269|PubMed:18849567}. +Q5HZG9 ZN488_MOUSE Zinc finger protein 488 337 37,195 Chain (1); Erroneous initiation (1); Motif (1); Region (1); Zinc finger (2) FUNCTION: Transcriptional repressor (PubMed:16908628). Plays a role in oligodendrocyte differentiation, together with OLIG2 (PubMed:16908628, PubMed:22355521). Mediates Notch signaling-activated formation of oligodendrocyte precursors (PubMed:16908628). Promotes differentiation of adult neural stem progenitor cells (NSPCs) into mature oligodendrocytes and contributes to remyelination following nerve injury (PubMed:22355521). {ECO:0000269|PubMed:16908628, ECO:0000269|PubMed:22355521}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16908628}. SUBUNIT: Interacts with OLIG2. {ECO:0000269|PubMed:16908628}. +Q99PP2 ZN318_MOUSE Zinc finger protein 318 (Testicular zinc finger protein) 2237 246,324 Alternative sequence (2); Chain (1); Coiled coil (3); Compositional bias (1); Cross-link (4); Erroneous initiation (3); Frameshift (3); Modified residue (26); Region (1); Sequence conflict (7); Zinc finger (2) FUNCTION: Isoform 2: Acts as a transcriptional corepressor for AR-mediated transactivation function. May act as a transcriptional regulator during spermatogenesis and in particular, during meiotic division. {ECO:0000269|PubMed:10873617, ECO:0000269|PubMed:12589823, ECO:0000269|PubMed:15882980}.; FUNCTION: Isoform 1: Acts as a transcriptional coactivator for AR-mediated transactivation function. May act as a transcriptional regulator during spermatogenesis and in particular, during meiotic division. {ECO:0000269|PubMed:12589823, ECO:0000269|PubMed:16446156}. SUBCELLULAR LOCATION: Isoform 1: Nucleus {ECO:0000269|PubMed:12589823, ECO:0000269|PubMed:16446156}.; SUBCELLULAR LOCATION: Isoform 2: Nucleus {ECO:0000269|PubMed:12589823, ECO:0000269|PubMed:16446156}. SUBUNIT: Homodimer. Heterodimer of isoform 1 and isoform 2. Isoform 1 and isoform 2 interact with AR. {ECO:0000269|PubMed:15882980, ECO:0000269|PubMed:16446156}. TISSUE SPECIFICITY: Isoform 1 and isoform 2 are highly expressed in testis, moderately expressed in adrenal gland and uterus and faintly expressed in brain, kidney and liver. Isoform 1 is expressed more in adrenal gland, uterus and liver than isoform 2 is. Expression during testicular development of isoform 1 and isoform 2 is restricted to spermatocytes at the pachytene stage of meiotic prophase and to round and elongated spermatids. {ECO:0000269|PubMed:10873617, ECO:0000269|PubMed:12589823}. +Q8BIF9 ZN787_MOUSE Zinc finger protein 787 381 40,477 Chain (1); Compositional bias (1); Cross-link (2); Frameshift (1); Modified residue (3); Sequence conflict (1); Zinc finger (7) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q6NZQ6 ZN740_MOUSE Zinc finger protein 740 180 20,892 Alternative sequence (3); Chain (1); Cross-link (1); Modified residue (1); Sequence conflict (2); Zinc finger (3) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +P39447 ZO1_MOUSE Tight junction protein ZO-1 (Tight junction protein 1) (Zona occludens protein 1) (Zonula occludens protein 1) 1745 194,742 Beta strand (8); Chain (1); Compositional bias (2); Domain (6); Helix (1); Modified residue (47); Region (2); Sequence conflict (7); Turn (2) FUNCTION: Tjp1, TjpP2, and Tjp3 are closely related scaffolding proteins that link tight junction (TJ) transmembrane proteins such as claudins, junctional adhesion molecules, and occludin to the actin cytoskeleton (By similarity). The tight junction acts to limit movement of substances through the paracellular space and as a boundary between the compositionally distinct apical and basolateral plasma membrane domains of epithelial and endothelial cells. Necessary for lumenogenesis, and particularly efficient epithelial polarization and barrier formation (By similarity). Plays a role in the regulation of cell migration by targeting Cdc42bpb to the leading edge of migrating cells (By similarity). Plays an important role in podosome formation and associated function, thus regulating cell adhesion and matrix remodeling (By similarity). With Tjp2 and TJjp3, participates to the junctional retention and stability of the transcription factor Dbpa, but is not involved in its shuttling to the nucleus (By similarity). {ECO:0000250|UniProtKB:O97758, ECO:0000250|UniProtKB:Q07157}. PTM: Phosphorylated at tyrosine redidues in response to epidermal growth factor (EGF) (By similarity). This response is dependent on an intact actin microfilament system (By similarity). Dephosphorylated by PTPRJ (By similarity). {ECO:0000250|UniProtKB:Q07157}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q07157}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q07157}; Cytoplasmic side {ECO:0000250|UniProtKB:Q07157}. Cell junction, tight junction {ECO:0000269|PubMed:10601346, ECO:0000269|PubMed:3528172}. Cell junction, gap junction {ECO:0000269|PubMed:20093627}. Cytoplasm, myofibril, sarcomere, I band {ECO:0000269|PubMed:20093627}. Note=Moves from the cytoplasm to the cell membrane concurrently with cell-cell contact (By similarity). Detected at the leading edge of migrating and wounded cells (By similarity). {ECO:0000250|UniProtKB:Q07157}. SUBUNIT: Homodimer, and heterodimer with TJP2 and TJP3. Interacts with OCLN, CALM, claudins, CGN/cingulin, CXADR, GJD3 and UBN1 (PubMed:10601346). Interacts (via ZU5 domain) with CDC42BPB (By similarity). Interacts (via PDZ domain) with GJA1 (By similarity). Interacts (via PDZ domains) with ANKRD2 (By similarity). Interacts with BVES (via the C-terminus cytoplasmic tail) (PubMed:16188940). Interacts with GJA12 and KIRREL1 (PubMed:12424224, PubMed:15183511). Interacts with HSPA4 (By similarity). Interacts (via ZU5 domain) with MYZAP (PubMed:20093627). Interacts with DLL1 (PubMed:24715457). Interacts with USP53 (via the C-terminal region) (PubMed:26609154). {ECO:0000250|UniProtKB:O97758, ECO:0000250|UniProtKB:Q07157, ECO:0000269|PubMed:10601346, ECO:0000269|PubMed:12424224, ECO:0000269|PubMed:15183511, ECO:0000269|PubMed:16188940, ECO:0000269|PubMed:20093627, ECO:0000269|PubMed:24715457, ECO:0000269|PubMed:26609154}. DOMAIN: The 244-aa domain between residues 633 and 876 is the primary occludin (Ocln)-binding site and is required for stable association with the tight junction (By similarity). {ECO:0000250|UniProtKB:Q07157}.; DOMAIN: The C-terminal region (residues 1151-1372) is an actin-binding region (ABR) that interacts directly with F-actin and plays an important role in the localization of Tjp1 at junctions (By similarity). The ABR is also required for the localization to puncta at the free edge of cells before initiation of cell-cell contact (By similarity). The ABR is also necessary for Tjp1 recruitment to podosomes (By similarity). {ECO:0000250|UniProtKB:Q07157}.; DOMAIN: The second PDZ domain (PDZ2) mediates homodimerization and heterodimerization with Tjp2 and Tjp3 (By similarity). PDZ2 domain also mediates interaction with Gja12 (PubMed:15183511). {ECO:0000250|UniProtKB:Q07157, ECO:0000269|PubMed:15183511}. +Q91VN1 ZNF24_MOUSE Zinc finger protein 24 (Hypomyelinated CNS protein) (Zinc finger protein 191) (Zinc finger protein ZF-12) 368 41,919 Chain (1); Cross-link (10); Domain (1); Modified residue (5); Region (1); Sequence conflict (2); Zinc finger (4) FUNCTION: Transcription factor required for myelination of differentiated oligodendrocytes. Required for the conversion of oligodendrocytes from the premyelinating to the myelinating state. In the developing central nervous system (CNS), involved in the maintenance in the progenitor stage by promoting the cell cycle. Specifically binds to the 5'-TCAT-3' DNA sequence. Has transcription repressor activity in vitro. {ECO:0000269|PubMed:19544452, ECO:0000269|PubMed:20080941}. PTM: Sumoylated. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187, ECO:0000269|PubMed:20080941}. TISSUE SPECIFICITY: Widely expressed with highest levels in heart, brain, liver, skeletal muscle, kidney and testis and very low levels in spleen and lung. {ECO:0000269|PubMed:10542327, ECO:0000269|PubMed:20080941}. +Q99KZ6 ZN639_MOUSE Zinc finger protein 639 (Zinc finger protein ZASC1) 485 55,678 Chain (1); Cross-link (4); Modified residue (2); Region (1); Sequence conflict (1); Zinc finger (8) FUNCTION: Binds DNA and may function as a transcriptional repressor. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with CTNNA2. {ECO:0000250}. +Q8BZ34 ZN641_MOUSE Zinc finger protein 641 422 47,398 Alternative sequence (1); Chain (1); Domain (1); Modified residue (1); Region (1); Zinc finger (5) FUNCTION: Transcriptional activator. Activates transcriptional activities of SRE and AP-1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +Q6PD05 ZN821_MOUSE Zinc finger protein 821 413 46,828 Chain (1); Coiled coil (1); Compositional bias (1); Sequence conflict (2); Zinc finger (2) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q6YND2 ZN653_MOUSE Zinc finger protein 653 (67 kDa zinc finger protein) (Zinc finger protein Zip67) 615 67,517 Alternative sequence (1); Chain (1); Compositional bias (3); Sequence conflict (3); Zinc finger (5) FUNCTION: Transcriptional repressor. May repress NR5A1, PPARG, NR1H3, NR4A2, ESR1 and NR3C1 transcriptional activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Interacts with NR5A1. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in testis and spleen. Moderately expressed in lung, adrenal gland, uterus, and ovary. Very low expression in pancreas, heart, skeletal muscle, adipose tissue, kidney, and liver. {ECO:0000269|PubMed:12920234}. +Q8C7B8 ZSWM4_MOUSE Zinc finger SWIM domain-containing protein 4 1101 122,445 Chain (1); Erroneous initiation (1); Sequence conflict (2); Zinc finger (1) +Q80TB7 ZSWM6_MOUSE Zinc finger SWIM domain-containing protein 6 1207 133,109 Alternative sequence (3); Chain (1); Zinc finger (1) TISSUE SPECIFICITY: Mouse embryos and newborn mice shown expression in the central nervous system (at protein level). {ECO:0000269|PubMed:25105228}. +B2RR83 YTDC2_MOUSE 3'-5' RNA helicase YTHDC2 (EC 3.6.4.13) (Keen to exit meiosis leaving testes under-populated protein) (Ketu) (YTH domain-containing protein C2) (mYTHDC2) 1445 161,092 Binding site (2); Chain (1); Compositional bias (2); Domain (4); Modified residue (6); Motif (1); Mutagenesis (1); Nucleotide binding (1); Region (1); Repeat (2) FUNCTION: 3'-5' RNA helicase that plays a key role in the male and female germline by promoting transition from mitotic to meiotic divisions in stem cells (PubMed:28380054, PubMed:28809393, PubMed:29087293, PubMed:29033321, PubMed:29360036). Specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs, a modification present at internal sites of mRNAs and some non-coding RNAs that plays a role in the efficiency of RNA processing and stability (PubMed:29360036). Essential for ensuring a successful progression of the meiotic program in the germline by regulating the level of m6A-containing RNAs (PubMed:29033321). Acts by binding and promoting degradation of m6A-containing mRNAs: the 3'-5' RNA helicase activity is required for this process and RNA degradation may be mediated by XRN1 exoribonuclease (PubMed:29033321). Required for both spermatogenesis and oogenesis (PubMed:28809393, PubMed:29033321). {ECO:0000269|PubMed:28380054, ECO:0000269|PubMed:28809393, ECO:0000269|PubMed:29033321, ECO:0000269|PubMed:29087293, ECO:0000269|PubMed:29360036}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29033321, ECO:0000269|PubMed:29087293, ECO:0000269|PubMed:29360036}. SUBUNIT: Interacts with MEIOC; binds transcripts that regulate the mitotic cell cycle inhibiting progression into metaphase, thereby allowing meiotic prophase to proceed normally (PubMed:28380054, PubMed:29087293). Interacts (via ANK repeats) with XRN1 (By similarity). {ECO:0000250|UniProtKB:Q9H6S0, ECO:0000269|PubMed:28380054, ECO:0000269|PubMed:29087293}. DOMAIN: The YTH domain mediates RNA-binding. It recognizes and binds N6-methyladenosine (m6A)-containing RNAs. {ECO:0000250|UniProtKB:Q9H6S0}. TISSUE SPECIFICITY: Highly expressed in testis (PubMed:28809393, PubMed:29087293, PubMed:29033321, PubMed:29360036). Present in germ cells (at protein level) (PubMed:29033321). Not detected in spermatogonia next to the tubule wall but is strongly expressed in spermatocytes, suggesting that it is up-regulated in germ cells upon entry into meiosis (at protein level) (PubMed:29087293). {ECO:0000269|PubMed:28809393, ECO:0000269|PubMed:29033321, ECO:0000269|PubMed:29087293, ECO:0000269|PubMed:29360036}. +Q9JKD9 ZBT32_MOUSE Zinc finger and BTB domain-containing protein 32 (Repressor of GATA) (Testis zinc finger protein) 465 50,828 Alternative sequence (1); Beta strand (7); Chain (1); Domain (1); Helix (3); Turn (1); Zinc finger (3) FUNCTION: DNA-binding protein that binds to the to a 5'-TGTACAGTGT-3' core sequence. May function as a transcriptional transactivator and transcriptional repressor (By similarity). Probably exerts its repressor effect by preventing GATA3 from binding to DNA. May play a role in regulating the differentiation and activation of helper T-cells. {ECO:0000250, ECO:0000269|PubMed:11279021}. SUBCELLULAR LOCATION: Nucleus. Note=Located in nuclear speckles. {ECO:0000250}. SUBUNIT: Homodimer (via PTB domain). Interacts with the N-terminal of FANCC. Interacts with ZBTB16 (By similarity). Interacts with GATA3. {ECO:0000250, ECO:0000269|PubMed:10755619}. DOMAIN: The C-terminal zinc finger domain functions as a transcriptional transactivator.; DOMAIN: The BTB (POZ) domain possesses repressor activity. TISSUE SPECIFICITY: Isoform 1 is testis-specific and is not expressed in lymphoid organs such as thymus or spleen. Isoform 2 is expressed in both B-and T-lymphoid cells. {ECO:0000269|PubMed:10755619}. +Q9ESG8 ZDH16_MOUSE Palmitoyltransferase ZDHHC16 (EC 2.3.1.225) (Abl-philin 2) (Zinc finger DHHC domain-containing protein 16) (DHHC-16) 361 41,794 Active site (1); Chain (1); Domain (1); Sequence conflict (4); Topological domain (5); Transmembrane (4) TRANSMEM 78 98 Helical. {ECO:0000255}.; TRANSMEM 117 137 Helical. {ECO:0000255}.; TRANSMEM 199 219 Helical. {ECO:0000255}.; TRANSMEM 251 271 Helical. {ECO:0000255}. TOPO_DOM 1 77 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 99 116 Lumenal. {ECO:0000255}.; TOPO_DOM 138 198 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 220 250 Lumenal. {ECO:0000255}.; TOPO_DOM 272 361 Cytoplasmic. {ECO:0000255}. FUNCTION: Palmitoyl acyltransferase that mediates palmitoylation of proteins such as PLN and ZDHHC6 (PubMed:26644582). Required during embryonic heart development and cardiac function, possibly by mediating palmitoylation of PLN, thereby affecting PLN phosphorylation and homooligomerization (PubMed:26644582). Also required for eye development (PubMed:26644582). Palmitoylates ZDHHC6, affecting the quaternary assembly of ZDHHC6, its localization, stability and function (By similarity). May play a role in DNA damage response (PubMed:27159997). May be involved in apoptosis regulation (PubMed:12021275). Involved in the proliferation of neural stem cells by regulating the FGF/ERK pathway (By similarity). {ECO:0000250|UniProtKB:B8A4F0, ECO:0000250|UniProtKB:Q969W1, ECO:0000269|PubMed:12021275, ECO:0000269|PubMed:26644582, ECO:0000269|PubMed:27159997}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12021275}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Interacts with ABL1 (PubMed:12021275). Interacts with COPS5 (By similarity). {ECO:0000250|UniProtKB:Q969W1, ECO:0000269|PubMed:12021275}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:12021275}. +Q62396 ZFP92_MOUSE Zinc finger protein 92 (Zfp-92) 488 55,976 Chain (1); Domain (1); Sequence conflict (1); Zinc finger (9) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +O88799 ZAN_MOUSE Zonadhesin 5376 579,913 Chain (1); Disulfide bond (3); Domain (58); Glycosylation (32); Region (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 5311 5337 Helical. {ECO:0000255}. TOPO_DOM 18 5310 Extracellular. {ECO:0000255}.; TOPO_DOM 5338 5376 Cytoplasmic. {ECO:0000255}. FUNCTION: Binds in a species-specific manner to the zona pellucida of the egg. May be involved in gamete recognition and/or signaling. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Note=Exclusively on the apical region of the sperm head. SUBUNIT: Probably forms covalent oligomers. DOMAIN: The MAM domains probably mediates sperm adhesion to the zona pellucida.; DOMAIN: During sperm migration through the reproductive tracts, the mucin-like domain might inhibit inappropriate trapping of spermatozoa or promoting adhesion to the oviductal isthmus.; DOMAIN: The VWFD domain 2 may mediate covalent oligomerization. {ECO:0000250}. TISSUE SPECIFICITY: In testis, primarily in haploid spermatids. +P17141 ZFP37_MOUSE Zinc finger protein 37 (Zfp-37) (Male germ cell-specific zinc finger protein) 594 67,226 Chain (1); Domain (1); Erroneous initiation (1); Modified residue (2); Sequence conflict (8); Zinc finger (12) FUNCTION: May have a role in regulating spermiogenesis. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: Expressed in testis and brain. +Q02525 ZFP39_MOUSE Zinc finger protein 39 (Zfp-39) (CtFIN33) 718 84,223 Chain (1); Domain (1); Frameshift (1); Sequence conflict (23); Zinc finger (13) FUNCTION: A putative DNA-binding regulatory protein associated with meiosis in spermatogenesis. SUBCELLULAR LOCATION: Nucleus. TISSUE SPECIFICITY: Predominantly in the spermatocytes and spermatids of testes. +Q9DB43 ZFPL1_MOUSE Zinc finger protein-like 1 310 34,155 Chain (1); Topological domain (2); Transmembrane (1); Zinc finger (2) TRANSMEM 267 287 Helical. {ECO:0000255}. TOPO_DOM 1 266 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 288 310 Lumenal. {ECO:0000255}. FUNCTION: Required for cis-Golgi integrity and efficient ER to Golgi transport. Involved in the maintenance of the integrity of the cis-Golgi, possibly via its interaction with GOLGA2/GM130 (By similarity). {ECO:0000250}. PTM: Phosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with GOLGA2/GM130. {ECO:0000250}. DOMAIN: The B box-type and RING-type zinc fingers although degenerate play a central role in function of the protein. {ECO:0000250}. +Q62520 ZIC2_MOUSE Zinc finger protein ZIC 2 (Zinc finger protein of the cerebellum 2) 530 54,954 Chain (1); Compositional bias (7); Cross-link (1); Modified residue (2); Mutagenesis (2); Region (1); Zinc finger (5) FUNCTION: Acts as a transcriptional activator or repressor. Plays important roles in the early stage of organogenesis of the CNS. Activates the transcription of the serotonin transporter SERT in uncrossed ipsilateral retinal ganglion cells (iRGCs) to refine eye-specific projections in primary visual targets. Its transcriptional activity is repressed by MDFIC. Involved in the formation of the ipsilateral retinal projection at the optic chiasm midline. Drives the expression of EPHB1 on ipsilaterally projecting growth cones. Binds to the minimal GLI-consensus sequence 5'-TGGGTGGTC-3'. Associates to the basal SERT promoter region from ventrotemporal retinal segments of retinal embryos. {ECO:0000269|PubMed:10677508, ECO:0000269|PubMed:11053430, ECO:0000269|PubMed:11756505, ECO:0000269|PubMed:13678579, ECO:0000269|PubMed:15207726, ECO:0000269|PubMed:15465018, ECO:0000269|PubMed:18417618, ECO:0000269|PubMed:18524895, ECO:0000269|PubMed:20676059}. PTM: Phosphorylated. {ECO:0000269|PubMed:18068128}.; PTM: Ubiquitinated by RNF180, leading to its degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Localizes in the cytoplasm in presence of MDFIC overexpression. Both phosphorylated and unphosphorylated forms are localized in the nucleus. SUBUNIT: Interacts with RNF180 (PubMed:18363970). Interacts (via the C2H2-type domains 3, 4 and 5) with MDFIC (via the C2H2-type domains 3, 4 and 5); the interaction reduces its transcriptional activity (PubMed:15207726, PubMed:15465018). Interacts (via C2H2-type domain 3) with DHX9 (PubMed:18068128). Interacts with GLI1 and GLI2 (PubMed:11238441). {ECO:0000250|UniProtKB:O95409, ECO:0000269|PubMed:11238441, ECO:0000269|PubMed:15207726, ECO:0000269|PubMed:15465018, ECO:0000269|PubMed:18068128, ECO:0000269|PubMed:18363970}. DOMAIN: The C2H2-type 3, 4 and 5 zinc finger domains are necessary for transcription activation. TISSUE SPECIFICITY: CNS. A high level expression is seen in the cerebellum. +Q9CPV7 ZDHC6_MOUSE Palmitoyltransferase ZDHHC6 (EC 2.3.1.225) (Zinc finger DHHC domain-containing protein 6) (DHHC-6) 413 47,527 Active site (1); Alternative sequence (4); Chain (1); Domain (2); Lipidation (3); Motif (1); Sequence conflict (1); Transmembrane (4) TRANSMEM 25 45 Helical. {ECO:0000255}.; TRANSMEM 58 78 Helical. {ECO:0000255}.; TRANSMEM 144 164 Helical. {ECO:0000255}.; TRANSMEM 195 215 Helical. {ECO:0000255}. FUNCTION: Endoplasmic reticulum palmitoyl acyltransferase that mediates palmitoylation of proteins such as AMFR, CALX, ITPR1 and TFRC (PubMed:25368151). Palmitoylates calnexin (CALX), which is required for its association with the ribosome-translocon complex and efficient folding of glycosylated proteins (By similarity). Mediates palmitoylation of AMFR, promoting AMFR distribution to the peripheral endoplasmic reticulum (By similarity). Together with SELENOK, palmitoylates ITPR1 in immune cells, leading to regulate ITPR1 stability and function (PubMed:25368151). {ECO:0000250|UniProtKB:Q9H6R6, ECO:0000269|PubMed:25368151}. PTM: Palmitoylated at 3 different sites by ZDHHC16. The combination of the different palmitoylation events strongly affects the quaternary assembly of ZDHHC6, its localization, stability and function. Palmitoylation at Cys-328 accelerates the turnover of ZDHHC6. Depalmitoylated by LYPLA2. {ECO:0000250|UniProtKB:Q9H6R6, ECO:0000269|PubMed:28826475}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9H6R6}; Multi-pass membrane protein {ECO:0000255}. Note=When not palmitoylated, accumulates to dot-like structures in the endoplasmic reticulum. {ECO:0000250|UniProtKB:Q9H6R6}. SUBUNIT: Homooligomerizes (By similarity). Interacts with SELENOK (PubMed:25368151). {ECO:0000250|UniProtKB:Q9H6R6, ECO:0000269|PubMed:25368151}. DOMAIN: The DHHC domain is required for palmitoyltransferase activity. {ECO:0000250|UniProtKB:Q8IUH5}.; DOMAIN: The C-terminal di-lysine motif confers endoplasmic reticulum localization. {ECO:0000250|UniProtKB:Q9H6R6}. +Q9R0G7 ZEB2_MOUSE Zinc finger E-box-binding homeobox 2 (Smad-interacting protein 1) (Zinc finger homeobox protein 1b) 1215 136,615 Chain (1); Compositional bias (1); Cross-link (9); DNA binding (1); Modified residue (13); Region (1); Sequence conflict (2); Zinc finger (8) FUNCTION: Transcriptional inhibitor that binds to DNA sequence 5'-CACCT-3' in different promoters. Represses transcription of E-cadherin. PTM: Sumoylation on Lys-391 and Lys-866 is promoted by the E3 SUMO-protein ligase CBX4, and impairs interaction with CTBP1 and transcription repression activity. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with CBX4 and CTBP1 (By similarity). Binds activated SMAD1, activated SMAD2 and activated SMAD3; binding with SMAD4 is not detected. {ECO:0000250}. +Q9JII7 ZFN2A_MOUSE AN1-type zinc finger protein 2A (Arsenite-inducible RNA-associated protein) 171 19,281 Chain (1); Zinc finger (2) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11525245}. Nucleus {ECO:0000269|PubMed:11525245}. +Q8R5C8 ZMY11_MOUSE Zinc finger MYND domain-containing protein 11 602 70,838 Beta strand (5); Chain (1); Cross-link (3); Domain (2); Erroneous initiation (1); Helix (11); Metal binding (4); Modified residue (1); Motif (1); Mutagenesis (8); Region (1); Sequence conflict (5); Turn (2); Zinc finger (2) FUNCTION: Chromatin reader that specifically recognizes and binds histone H3.3 trimethylated at 'Lys-36' (H3.3K36me3) and regulates RNA polymerase II elongation. Does not bind other histone H3 subtypes (H3.1 or H3.2). Colocalizes with highly expressed genes and functions as a transcription corepressor by modulating RNA polymerase II at the elongation stage (PubMed:24590075). Binds non-specifically to dsDNA (By similarity). Acts as a tumor-suppressor by repressing a transcriptional program essential for tumor cell growth (PubMed:24590075). {ECO:0000250|UniProtKB:Q15326, ECO:0000269|PubMed:24590075}. PTM: Ubiquitinated, leading to proteasomal degradation. {ECO:0000250|UniProtKB:Q15326}.; PTM: Sumoylated following its interaction with PIAS1 and UBE2I. {ECO:0000250|UniProtKB:Q15326}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15326}. Chromosome {ECO:0000250|UniProtKB:Q15326}. Note=Associates with chromatin and mitotic chromosomes. {ECO:0000250|UniProtKB:Q15326}. SUBUNIT: Homooligomer; forms homooligomers via its C-terminus. Interacts with histone H3.3 trimethylated at 'Lys-36' (H3.3K36me3). Interacts (via MYND-type zinc finger) with NCOR1. Interacts (via MYND-type zinc finger) with MGA protein (via PXLXP motif). Interacts (via MYND-type zinc finger) with EZH2. Interacts with EMSY and E2F6. Interacts with PIAS1 and UBE2I (By similarity). {ECO:0000250|UniProtKB:Q15326}. DOMAIN: The PWWP domain specifically recognizes and binds histone H3.3 trimethylated at 'Lys-36' (H3.3K36me3) and adopts a five-bladed beta-barrel fold with an extended C-terminal alpha-helix, with a conserved H3.3K36me3-binding aromatic cage formed by Phe-291 and Trp-294 of the beta1-beta2 loop and Phe-310 of the beta3-beta4 loop. Specific recognition of H3.3 histone is mediated by the encapsulation of the H3.3-specific 'Ser 31' residue in a composite pocket formed by the tandem bromo-PWWP domains (PubMed:24590075). {ECO:0000269|PubMed:24590075}. +Q8BI67 ZN473_MOUSE Zinc finger protein 473 homolog (Zinc finger protein 100) (Zfp-100) 892 101,741 Chain (1); Cross-link (2); Domain (1); Sequence conflict (2); Zinc finger (17) FUNCTION: Involved in histone 3'-end pre-mRNA processing by associating with U7 snRNP and interacting with SLBP/pre-mRNA complex. Increases histone 3'-end pre-mRNA processing but has no effect on U7 snRNP levels, when overexpressed. Required for cell cycle progression from G1 to S phases (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Stable component of Cajal bodies (CBs). Colocalizes with SMN, coilin and U7 snRNA (By similarity). {ECO:0000250}. SUBUNIT: Interacts with the SLBP/pre-mRNA complex but not with SLBP alone. Interacts with LSM11 in a U7 snRNP-dependent manner (By similarity). {ECO:0000250}. DOMAIN: The C2H2-type zinc fingers are involved in discrete Cajal bodies localization, interaction with LSM11 and the SLBP/RNA complex and histone pre-mRNA processing. {ECO:0000250}. +Q9DB38 ZN580_MOUSE Zinc finger protein 580 172 18,837 Chain (1); Compositional bias (1); Cross-link (2); Zinc finger (3) FUNCTION: Involved in the regulation of endothelial cell proliferation and migration. Mediates H(2)O(2)-induced leukocyte chemotaxis by elevating interleukin-8 production and may play a role in inflammation. May be involved in transcriptional regulation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Colocalized with SMAD2 in the nucleus. {ECO:0000250}. SUBUNIT: Interacts with SMAD2. {ECO:0000250}. +Q3U3I9 ZN865_MOUSE Zinc finger protein 865 1058 111,676 Chain (1); Compositional bias (4); Cross-link (2); Zinc finger (20) FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +Q91VY9 ZN622_MOUSE Zinc finger protein 622 476 53,451 Chain (1); Compositional bias (1); Initiator methionine (1); Modified residue (2); Zinc finger (2) FUNCTION: May behave as an activator of the bound transcription factor, MYBL2, and be involved in embryonic development. PTM: Phosphorylated by MELK. The phosphorylation may redirect the protein to the nucleus (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Homo- and heterodimer. Interacts with MELK and MYBL2. Interacts with DNAJC21. {ECO:0000250|UniProtKB:Q969S3}. +Q8BV42 ZN786_MOUSE Zinc finger protein 786 777 89,484 Chain (1); Domain (1); Zinc finger (15) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q8R2V3 ZN445_MOUSE Zinc finger protein 445 986 114,774 Chain (1); Cross-link (7); Domain (2); Erroneous initiation (1); Sequence conflict (2); Zinc finger (12) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}. +Q0VEE6 ZN800_MOUSE Zinc finger protein 800 662 74,813 Chain (1); Compositional bias (1); Cross-link (5); Modified residue (9); Zinc finger (7) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q8BMU0 ZNF76_MOUSE Zinc finger protein 76 (Zinc finger protein 523) 568 61,454 Alternative sequence (2); Chain (1); Cross-link (1); Region (1); Repeat (3); Zinc finger (7) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q8BGV5 ZNF8_MOUSE Zinc finger protein 8 (Zinc finger protein 128) 572 64,737 Chain (1); Cross-link (3); Domain (1); Frameshift (1); Sequence conflict (1); Zinc finger (7) FUNCTION: Transcriptional repressor. May modulate BMP and TGF-beta signal transduction, through its interaction with SMAD proteins. {ECO:0000269|PubMed:12370310}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12370310}. SUBUNIT: Interacts with SMAD1 (via MH1 and MH2 domains). Interacts with SMAD5. Interacts weakly with SMAD2, SMAD3 and SMAD4. {ECO:0000269|PubMed:12370310}. TISSUE SPECIFICITY: Strongly expressed in testis, where it localizes to seminiferous tubules. Weakly expressed in heart, brain, lung, liver and kidney. {ECO:0000269|PubMed:12370310}. +Q5DU09 ZN652_MOUSE Zinc finger protein 652 608 69,441 Alternative sequence (2); Chain (1); Compositional bias (3); Modified residue (5); Region (1); Zinc finger (9) FUNCTION: Functions as a transcriptional repressor. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Interacts with CBFA2T3. {ECO:0000250}. +Q6P3Y5 Z280C_MOUSE Zinc finger protein 280C (Suppressor of hairy wing homolog 3) 742 83,146 Alternative sequence (3); Chain (1); Compositional bias (2); Cross-link (11); Erroneous initiation (1); Zinc finger (5) FUNCTION: May function as a transcription factor. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q9Z0G7 ZBT22_MOUSE Zinc finger and BTB domain-containing protein 22 (Protein BING1) (Zinc finger protein 297) 638 66,029 Chain (1); Domain (1); Modified residue (1); Zinc finger (3) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +P59267 ZDHC2_MOUSE Palmitoyltransferase ZDHHC2 (EC 2.3.1.225) (Zinc finger DHHC domain-containing protein 2) (DHHC-2) 366 41,982 Chain (1); Domain (1); Transmembrane (4) TRANSMEM 16 36 Helical. {ECO:0000255}.; TRANSMEM 48 68 Helical. {ECO:0000255}.; TRANSMEM 170 190 Helical. {ECO:0000255}.; TRANSMEM 208 228 Helical. {ECO:0000255}. FUNCTION: Palmitoyltransferase specific for GAP43 and DLG4/PSD95. {ECO:0000269|PubMed:15603741}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. DOMAIN: The DHHC domain is required for palmitoyltransferase activity. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in all brain regions. {ECO:0000269|PubMed:15603741}. +Q8R1J3 ZCHC9_MOUSE Zinc finger CCHC domain-containing protein 9 271 30,488 Chain (1); Compositional bias (1); Erroneous termination (1); Sequence conflict (1); Zinc finger (4) FUNCTION: May down-regulate transcription mediated by NF-kappa-B and the serum response element. {ECO:0000250|UniProtKB:Q8N567}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q8N567}. Nucleus {ECO:0000250|UniProtKB:Q8N567}. Note=Expressed throughout the nucleus and concentrated mainly in the nucleolus. {ECO:0000250|UniProtKB:Q8N567}. TISSUE SPECIFICITY: Detected in brain cortex and in testis. {ECO:0000269|PubMed:18721783}. +Q08EN7 ZCPW2_MOUSE Zinc finger CW-type PWWP domain protein 2 homolog 125 14,225 Chain (1); Zinc finger (1) +Q08376 ZBT14_MOUSE Zinc finger and BTB domain-containing protein 14 (Zinc finger protein 161) (Zfp-161) (Zinc finger protein 5) (ZF5) 449 50,899 Chain (1); Compositional bias (1); Cross-link (3); Domain (1); Motif (1); Zinc finger (5) FUNCTION: Transcriptional activator of the dopamine transporter (DAT), binding it's promoter at the consensus sequence 5'-CCTGCACAGTTCACGGA-3'. Binds to 5'-d(GCC)(n)-3' trinucleotide repeats in promoter regions and acts as a repressor of the FMR1 gene (By similarity). Transcriptional repressor of MYC and thymidine kinase promoters. {ECO:0000250, ECO:0000269|PubMed:8367294}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with ZBTB21. {ECO:0000250}. DOMAIN: The BTB/POZ domain seems to direct the protein to discrete regions in the nucleus. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:8367294}. +Q497H0 ZFAN3_MOUSE AN1-type zinc finger protein 3 (Testis-expressed protein 27) 227 25,081 Alternative sequence (1); Chain (1); Erroneous initiation (1); Zinc finger (2) TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:8703127}. +D3Z3C6 ZFAN4_MOUSE AN1-type zinc finger protein 4 (AN1-type zinc finger and ubiquitin domain-containing protein-like 1) 739 81,554 Chain (1); Domain (1); Zinc finger (1) +Q811F1 ZBT41_MOUSE Zinc finger and BTB domain-containing protein 41 908 104,683 Chain (1); Domain (1); Erroneous initiation (1); Frameshift (2); Sequence conflict (5); Zinc finger (14) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q02526 ZFP41_MOUSE Zinc finger protein 41 (Zfp-41) (CtFIN92) 198 22,724 Chain (1); Zinc finger (4) FUNCTION: A putative DNA-binding regulatory protein associated with meiosis in spermatogenesis. {ECO:0000269|PubMed:1397691}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:1397691}. TISSUE SPECIFICITY: Predominantly in the spermatocytes and spermatids of testes. It is also expressed in the fetus and embryonic stem cells at lower levels. {ECO:0000269|PubMed:1397691}. +Q9CPW7 ZMAT2_MOUSE Zinc finger matrin-type protein 2 199 23,612 Chain (1); Cross-link (10); Initiator methionine (1); Modified residue (1); Zinc finger (1) FUNCTION: Involved in pre-mRNA splicing as a component of the spliceosome. {ECO:0000250|UniProtKB:Q96NC0}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96NC0}. SUBUNIT: Component of the spliceosome B complex. {ECO:0000250|UniProtKB:Q96NC0}. +Q1WG82 ZGLP1_MOUSE GATA-type zinc finger protein 1 (GATA-like protein 1) (GLP-1) 266 29,107 Chain (1); Zinc finger (1) FUNCTION: Transcriptional repressor that plays a central role in somatic cells of the gonad and is required for germ cell development. Able to repress GATA transcription factor function. {ECO:0000269|PubMed:16982049}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16982049}. TISSUE SPECIFICITY: Specifically expressed in adult testis and ovary. Expressed at high levels in the somatic cells of the developing gonads, including Leydig cells in the testes and granulosa cells in the ovaries. {ECO:0000269|PubMed:16982049}. +P16372 ZFP58_MOUSE Zinc finger protein 58 (Zfp-58) (Regulator of sex-limitation candidate 5) (Zinc finger protein Mfg-1) 489 57,232 Chain (1); Domain (1); Sequence caution (1); Sequence conflict (1); Zinc finger (15) FUNCTION: May have a role during differentiation processes. {ECO:0000269|PubMed:2512579}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: Expressed in liver, testis and, at considerably lower levels, in brain, spleen and heart. {ECO:0000269|PubMed:2512579}. +Q9CQR5 ZMAT5_MOUSE Zinc finger matrin-type protein 5 (U11/U12 small nuclear ribonucleoprotein 20 kDa protein) (U11/U12 snRNP 20 kDa protein) 170 19,886 Chain (1); Zinc finger (1) SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the U11/U12 snRNPs that are part of the U12-type spliceosome. Not found in the major spliceosome (By similarity). {ECO:0000250}. +P17012 ZFX_MOUSE Zinc finger X-chromosomal protein 799 90,026 Chain (1); Modified residue (1); Sequence caution (1); Zinc finger (13) FUNCTION: Probable transcriptional activator. SUBCELLULAR LOCATION: Nucleus. +Q5DU37 ZFY26_MOUSE Zinc finger FYVE domain-containing protein 26 2529 282,961 Alternative sequence (5); Chain (1); Coiled coil (2); Compositional bias (2); Erroneous initiation (1); Modified residue (7); Sequence conflict (4); Zinc finger (1) FUNCTION: Phosphatidylinositol 3-phosphate-binding protein required for the abcission step in cytokinesis: recruited to the midbody during cytokinesis and acts as a regulator of abcission. May also be required for efficient homologous recombination DNA double-strand break repair (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Midbody {ECO:0000250}. Note=Localizes to the centrosome during all stages of the cell cycle. Recruited to the midbody during cytokinesis by KIF13A (By similarity). {ECO:0000250}. SUBUNIT: Interacts with AP5Z1, AP5B1, AP5S1 and SPG11. Interacts with TTC19 and KIF13A (By similarity). {ECO:0000250}. DOMAIN: The FYVE-type zinc finger mediates binding to phosphatidylinositol 3-phosphate and recruitment to the midbody during cytokinesis. {ECO:0000250}. +Q5DTV4 ZC12C_MOUSE Probable ribonuclease ZC3H12C (EC 3.1.-.-) (Zinc finger CCCH domain-containing protein 12C) 884 99,430 Chain (1); Modified residue (1); Zinc finger (1) FUNCTION: May function as RNase and regulate the levels of target RNA species. {ECO:0000305}. +P70121 ZHX1_MOUSE Zinc fingers and homeoboxes protein 1 873 97,551 Chain (1); Cross-link (4); DNA binding (5); Modified residue (7); Region (4); Sequence conflict (5); Zinc finger (2) FUNCTION: Acts as a transcriptional repressor. Increases DNMT3B-mediated repressive transcriptional activity when DNMT3B is tethered to DNA. May link molecule between DNMT3B and other co-repressor proteins (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:17056598}. Note=Colocalized in the nucleus with DNMT3B. {ECO:0000250}. SUBUNIT: Forms homodimers. Heterodimer (via HD1 domain) with ZHX2 (via HD1 domain). Also forms a heterodimer with ZHX3 which is a prerequisite for repressor activity. Interacts with ATF7IP and NFYA. Interacts (via homeobox domains) with DNMT3B (via PWWP domain) (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed with highest levels in brain. {ECO:0000269|PubMed:8713137}. +Q3UPF5 ZCCHV_MOUSE Zinc finger CCCH-type antiviral protein 1 (ADP-ribosyltransferase diphtheria toxin-like 13) (ARTD13) (Inactive Poly [ADP-ribose] polymerase 13) (PARP13) 946 106,688 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (2); Modified residue (13); Motif (3); Region (2); Zinc finger (4) FUNCTION: Antiviral protein which inhibits the replication of viruses by recruiting the cellular RNA degradation machineries to degrade the viral mRNAs. Binds to a ZAP-responsive element (ZRE) present in the target viral mRNA, recruits cellular poly(A)-specific ribonuclease PARN to remove the poly(A) tail, and the 3'-5' exoribonuclease complex exosome to degrade the RNA body from the 3'-end. It also recruits the decapping complex DCP1-DCP2 through RNA helicase p72 (DDX17) to remove the cap structure of the viral mRNA to initiate its degradation from the 5'-end. Its target viruses belong to families which include retroviridae: human immunodeficiency virus type 1 (HIV-1) and moloney and murine leukemia virus (MoMLV), filoviridae: ebola virus (EBOV) and marburg virus (MARV), togaviridae: sindbis virus (SINV) and Ross river virus (RRV). Specifically targets the multiply spliced but not unspliced or singly spliced HIV-1 mRNAs for degradation. Isoform 1 is a more potent viral inhibitor than isoform 2. Isoform 2 acts as a positive regulator of DDX58/RIG-I signaling resulting in activation of the downstream effector IRF3 leading to the expression of type I IFNs and IFN stimulated genes (ISGs). {ECO:0000269|PubMed:21102435}. PTM: Phosphorylation at Ser-273 is essential for sequential phosphorylation of Ser-269, Ser-265, Ser-262 and Ser-257 by GSK3-beta. Phosphorylation by GSK3-beta enhances its antiviral activity (By similarity). {ECO:0000250|UniProtKB:Q8K3Y6}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8K3Y6}. Nucleus {ECO:0000250|UniProtKB:Q8K3Y6}. Note=Localizes in the cytoplasm at steady state, but shuttles between nucleus and cytoplasm in a XPO1-dependent manner. {ECO:0000250|UniProtKB:Q8K3Y6}. SUBUNIT: Homodimer or homooligomer. Homooligomerization is essential for its antiviral activity (By similarity). Interacts with EXOSC5 (By similarity). Interacts (via N-terminal domain) with DDX17 in an RNA-independent manner (By similarity). Interacts with EXOSC3, EXOSC7, DCP2 and DCP1A (By similarity). Interacts with PARN in an RNA-independent manner (By similarity). Interacts with XRN1 in an RNA-dependent manner (By similarity). Interacts (via N-terminal domain) with DHX30 (via N-terminus) in an RNA-independent manner (By similarity). Isoform 2 interacts (via zinc-fingers) with DDX58/RIG-I in an RNA-dependent manner (By similarity). {ECO:0000250}. DOMAIN: The N-terminal domain is sufficient to bind to viral RNAs and promote their degradation. The second and fourth zinc fingers are involved in binding to specific viral RNAs. Contains a divergent PARP homology ADP-ribosyltransferase domain which lacks the structural requirements for NAD[+] binding. It is therefore inactive. {ECO:0000250|UniProtKB:Q7Z2W4}. +Q8BIY3 ZC12D_MOUSE Probable ribonuclease ZC3H12D (EC 3.1.-.-) (MCP-induced protein 4) (Transformed follicular lymphoma homolog) (Zinc finger CCCH domain-containing protein 12D) 533 59,340 Chain (1); Frameshift (2); Region (1); Sequence conflict (1); Zinc finger (1) FUNCTION: May regulate cell growth likely by suppressing RB1 phosphorylation (By similarity). May function as RNase and regulate the levels of target RNA species (Potential). In association with ZC3H12A enhances the degradation of interleukin IL-6 mRNA level in activated macrophages (PubMed:26134560). Serve as a tumor suppressor in certain leukemia cells (By similarity). Overexpression inhibits the G1 to S phase progression through suppression of RB1 phosphorylation (By similarity). {ECO:0000250|UniProtKB:A2A288, ECO:0000269|PubMed:26134560}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A2A288}. Cytoplasm, P-body {ECO:0000250|UniProtKB:A2A288}. Note=Colocalizes with ZC3H12A in GW bodies (GWBs). {ECO:0000250|UniProtKB:A2A288}. SUBUNIT: Interacts with ZC3H12A. {ECO:0000250|UniProtKB:A2A288}. TISSUE SPECIFICITY: Expressed at low levels in bone marrow derived macrophages. {ECO:0000269|PubMed:18178554}. +A2A5K6 ZN335_MOUSE Zinc finger protein 335 (NRC-interacting factor 1) (NIF-1) 1337 145,603 Chain (1); Compositional bias (1); Cross-link (1); Modified residue (3); Sequence conflict (16); Zinc finger (13) FUNCTION: Component or associated component of some histone methyltransferase complexes may regulate transcription through recruitment of those complexes on gene promoters. Enhances ligand-dependent transcriptional activation by nuclear hormone receptors. Plays an important role in neural progenitor cell proliferation and self-renewal through the regulation of specific genes involved brain development, including REST. Also controls the expression of genes involved in somatic development and regulates, for instance, lymphoblast proliferation. {ECO:0000269|PubMed:23178126}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23178126}. SUBUNIT: Interacts with NCOA6; may enhance ligand-dependent transcriptional activation by nuclear hormone receptors (By similarity). Interacts with CNOT6 (By similarity). Interacts with CNOT9; the interaction is direct (By similarity). Part of a complex composed at least of ASCL2, EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; this complex may have a histone H3-specific methyltransferase activity (By similarity). Interacts with members of histone H3'Lys4'(H3K4) methyltransferase complexes ASCL2, CXXC1, KMT2A/MLL1, SETD1A (By similarity). Interacts with RBBP5 and WDR5. {ECO:0000250, ECO:0000269|PubMed:23178126}. TISSUE SPECIFICITY: Expressed at low levels in cerebral cortex, hippocampus and cerebellum (at protein level). {ECO:0000269|PubMed:23178126}. +Q6KAS7 ZN521_MOUSE Zinc finger protein 521 (Ecotropic viral integration site 3 protein) 1311 147,666 Alternative sequence (1); Chain (1); Cross-link (1); Erroneous initiation (2); Modified residue (3); Sequence conflict (3); Zinc finger (30) FUNCTION: Transcription factor that can both act as an activator or a repressor depending on the context. Involved in BMP signaling and in the regulation of the immature compartment of the hematopoietic system. Associates with SMADs in response to BMP2 leading to activate transcription of BMP target genes. Acts as a transcriptional repressor via its interaction with EBF1, a transcription factor involved specification of B-cell lineage; this interaction preventing EBF1 to bind DNA and activate target genes. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12393497}. SUBUNIT: Interacts with EBF1. Interacts with SMAD1 and SMAD4 (By similarity). {ECO:0000250}. DOMAIN: Uses different DNA- and protein-binding zinc fingers to regulate the distinct BMP-Smad and hematopoietic system. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. Expressed in all B-cell stages. {ECO:0000269|PubMed:12393497}. DISEASE: Note=Defects in Znf521 are a cause of B-cell lymphomas. Znf521 gene is a frequent target of retroviral integration in murine B-cell lymphomas. Involved in most B-cell tumors in the AKXD-27 strain. Viral insertion causes overexpression resulting in the up-regulation of EBF1-target gene expression. Misexpression initiates tumorigenesis by perturbing B-cell development via an interaction with EBF1. {ECO:0000269|PubMed:12393497, ECO:0000269|PubMed:15580294}. +Q8CHP0 ZC3H3_MOUSE Zinc finger CCCH domain-containing protein 3 (Smad-interacting CPSF-like factor) 950 103,224 Chain (1); Compositional bias (1); Modified residue (6); Zinc finger (5) FUNCTION: Required for the export of polyadenylated mRNAs from the nucleus (By similarity). Enhances ACVR1B-induced SMAD-dependent transcription. Binds to single-stranded DNA but not to double-stranded DNA in vitro. Involved in RNA cleavage (PubMed:16115198). {ECO:0000250|UniProtKB:Q8IXZ2, ECO:0000269|PubMed:16115198}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16115198}. SUBUNIT: Interacts with SMAD1, SMAD3, SMAD4, CPSF2 and CPSF3. {ECO:0000269|PubMed:16115198}. +Q8BYK8 ZC3H6_MOUSE Zinc finger CCCH domain-containing protein 6 1177 131,250 Alternative sequence (2); Chain (1); Coiled coil (2); Compositional bias (1); Erroneous initiation (1); Modified residue (1); Sequence conflict (4); Zinc finger (3) +Q99LH4 ZN672_MOUSE Zinc finger protein 672 468 52,154 Chain (1); Sequence conflict (1); Zinc finger (14) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q9QYZ4 SMOK1_MOUSE Sperm motility kinase 1 (EC 2.7.11.1) 484 54,794 Active site (1); Binding site (1); Chain (1); Domain (2); Nucleotide binding (1) FUNCTION: May play a role in sperm motility, especially in the regulation of flagellar function. {ECO:0000269|PubMed:10647005}. TISSUE SPECIFICITY: Testis-specific. Expressed in the testis from 22 days postpartum (22 dpp). {ECO:0000269|PubMed:10647005}. +P61807 SNN_MOUSE Stannin 88 9,501 Chain (1); Modified residue (2); Topological domain (2); Transmembrane (1) TRANSMEM 11 31 Helical. {ECO:0000255}. TOPO_DOM 1 10 Mitochondrial intermembrane. {ECO:0000250}.; TOPO_DOM 32 88 Cytoplasmic. {ECO:0000250}. FUNCTION: Plays a role in the toxic effects of organotins (By similarity). Plays a role in endosomal maturation (PubMed:27015288). {ECO:0000250|UniProtKB:O75324, ECO:0000269|PubMed:27015288}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250|UniProtKB:O75324}. +P62315 SMD1_MOUSE Small nuclear ribonucleoprotein Sm D1 (Sm-D1) (Sm-D autoantigen) (snRNP core protein D1) 119 13,282 Chain (1); Compositional bias (1); Cross-link (1); Region (1) FUNCTION: Plays role in pre-mRNA splicing as core component of the SMN-Sm complex that mediates spliceosomal snRNP assembly and as component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Component of both the pre-catalytic spliceosome B complex and activated spliceosome C complexes. Is also a component of the minor U12 spliceosome. May act as a charged protein scaffold to promote snRNP assembly or strengthen snRNP-snRNP interactions through non-specific electrostatic contacts with RNA. {ECO:0000250|UniProtKB:P62314}. PTM: Methylated on arginine residues by PRMT5 and PRMT7; probable asymmetric dimethylation which is required for assembly and biogenesis of snRNPs. {ECO:0000250|UniProtKB:P62314}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P62314}. Nucleus {ECO:0000250|UniProtKB:P62314}. Note=SMN-mediated assembly into core snRNPs occurs in the cytosol before SMN-mediated transport to the nucleus to be included in spliceosomes. {ECO:0000250|UniProtKB:P62314}. SUBUNIT: Core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Most spliceosomal snRNPs contain a common set of Sm proteins, SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. Component of the U1 snRNP. The U1 snRNP is composed of the U1 snRNA and the 7 core Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG, and at least three U1 snRNP-specific proteins SNRNP70/U1-70K, SNRPA/U1-A and SNRPC/U1-C. Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39, plus LSM2, LSM3, LSM4, LSM5, LSM6, LSM7 and LSM8. Component of the U11/U12 snRNPs that are part of the U12-type spliceosome. Part of the SMN-Sm complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8, STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG; catalyzes core snRNPs assembly. Forms a 6S pICln-Sm complex composed of CLNS1A/pICln, SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG; ring-like structure where CLNS1A/pICln mimics additional Sm proteins and which is unable to assemble into the core snRNP. {ECO:0000250|UniProtKB:P62314}. +Q99JR8 SMRD2_MOUSE SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2 (60 kDa BRG-1/Brm-associated factor subunit B) (BRG1-associated factor 60B) (BAF60B) 531 59,085 Alternative sequence (1); Chain (1); Compositional bias (1); Cross-link (1); Domain (1); Erroneous initiation (1); Modified residue (4) FUNCTION: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. Critical regulator of myeloid differentiation, controlling granulocytopoiesis and the expression of genes involved in neutrophil granule formation. {ECO:0000250|UniProtKB:Q92925}. PTM: Ubiquitinated through a signaling process involving RAC1 and the RING finger protein UNKL. {ECO:0000250|UniProtKB:Q92925}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92925}. SUBUNIT: Component of the multiprotein chromatin-remodeling complexes SWI/SNF: SWI/SNF-A (BAF), SWI/SNF-B (PBAF) and related complexes. The canonical complex contains a catalytic subunit (either SMARCA4/BRG1/BAF190A or SMARCA2/BRM/BAF190B), and at least SMARCE1, ACTL6A/BAF53, SMARCC1/BAF155, SMARCC2/BAF170, and SMARCB1/SNF5/BAF47. Other subunits specific to each of the complexes may also be present permitting several possible combinations developmentally and tissue specific. Component of the BAF complex, which includes at least actin (ACTB), ARID1A/BAF250A, ARID1B/BAF250B, SMARCA2/BRM, SMARCA4/BRG1, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57, SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C. In muscle cells, the BAF complex also contains DPF3. Component of the SWI/SNF-B (PBAF) chromatin remodeling complex, at least composed of SMARCA4/BRG1, SMARCB1/BAF47/SNF5, ACTL6A/BAF53A or ACTL6B/BAF53B, SMARCE1/BAF57, SMARCD1/BAF60A, SMARCD2/BAF60B, perhaps SMARCD3/BAF60C, SMARCC1/BAF155, SMARCC2/BAF170, PBRM1/BAF180, ARID2/BAF200 and actin (ACTB). Interacts with UNKL. Interacts with CEBPE. {ECO:0000250|UniProtKB:Q92925}. +C0HKC9 SMK3B_MOUSE Sperm motility kinase 3B (EC 2.7.11.1) 504 56,487 Active site (1); Binding site (1); Chain (1); Domain (2); Nucleotide binding (1) FUNCTION: May play a role in sperm motility, especially in the regulation of flagellar function. {ECO:0000269|PubMed:10647005}. TISSUE SPECIFICITY: Testis-specific. Expressed in the testis from 22 days postpartum (22 dpp). {ECO:0000269|PubMed:10647005}. +P56726 SMO_MOUSE Smoothened homolog (SMO) 793 87,450 Chain (1); Disulfide bond (8); Domain (1); Glycosylation (3); Region (2); Sequence conflict (3); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 238 258 Helical; Name=1. {ECO:0000255}.; TRANSMEM 266 286 Helical; Name=2. {ECO:0000255}.; TRANSMEM 319 339 Helical; Name=3. {ECO:0000255}.; TRANSMEM 363 383 Helical; Name=4. {ECO:0000255}.; TRANSMEM 407 427 Helical; Name=5. {ECO:0000255}.; TRANSMEM 456 476 Helical; Name=6. {ECO:0000255}.; TRANSMEM 529 549 Helical; Name=7. {ECO:0000255}. TOPO_DOM 33 237 Extracellular. {ECO:0000255}.; TOPO_DOM 259 265 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 287 318 Extracellular. {ECO:0000255}.; TOPO_DOM 340 362 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 384 406 Extracellular. {ECO:0000255}.; TOPO_DOM 428 455 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 477 528 Extracellular. {ECO:0000255}.; TOPO_DOM 550 793 Cytoplasmic. {ECO:0000255}. FUNCTION: G protein-coupled receptor that probably associates with the patched protein (PTCH) to transduce the hedgehog's proteins signal. Binding of sonic hedgehog (SHH) to its receptor patched is thought to prevent normal inhibition by patched of smoothened (SMO) (By similarity). Required for the accumulation of KIF7, GLI2 and GLI3 in the cilia. Interacts with DLG5 at the ciliary base to induce the accumulation of KIF7 and GLI2 at the ciliary tip for GLI2 activation (PubMed:25644602). {ECO:0000250|UniProtKB:Q99835, ECO:0000269|PubMed:25644602}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Cell projection, cilium {ECO:0000269|PubMed:21659505, ECO:0000269|PubMed:25644602}. SUBUNIT: Homodimer (By similarity). Interacts with ARRB2 (PubMed:15618519). Interacts with BBS5 and BBS7; the interactions are indicative for the association of SMO with the BBsome complex to facilitate ciliary localization of SMO (PubMed:22072986). Interacts with KIF7, DLG5 and SDCBP (PubMed:25644602). Interacts with GAS8/DRC4 (PubMed:21659505). {ECO:0000250|UniProtKB:Q99835, ECO:0000269|PubMed:15618519, ECO:0000269|PubMed:21659505, ECO:0000269|PubMed:22072986, ECO:0000269|PubMed:25644602}. +Q8CI12 SMTL2_MOUSE Smoothelin-like protein 2 456 49,523 Chain (1); Coiled coil (1); Domain (1); Modified residue (10) +Q6P5D8 SMHD1_MOUSE Structural maintenance of chromosomes flexible hinge domain-containing protein 1 (SMC hinge domain-containing protein 1) (EC 3.6.1.-) 2007 225,648 Chain (1); Cross-link (1); Domain (1); Erroneous initiation (1); Frameshift (1); Initiator methionine (1); Modified residue (6); Mutagenesis (3); Region (1); Sequence conflict (2) FUNCTION: Non-canonical member of the structural maintenance of chromosomes (SMC) protein family that plays a key role in epigenetic silencing by regulating chromatin architecture (PubMed:26091879, PubMed:29887375). Promotes heterochromatin formation in both autosomes and chromosome X, probably by mediating the merge of chromatin compartments (PubMed:23754746, PubMed:23819640, PubMed:26391951, PubMed:28587678, PubMed:29887375). Plays a key role in chromosome X inactivation in females by promoting the spreading of heterochromatin (PubMed:18425126, PubMed:22841499, PubMed:26391951, PubMed:29887375). Recruited to inactivated chromosome X by Xist RNA and acts by mediating the merge of chromatin compartments: promotes random chromatin interactions that span the boundaries of existing structures, leading to create a compartment-less architecture typical of inactivated chromosome X (PubMed:29887375). Required to facilitate Xist RNA spreading (PubMed:29887375). Also required for silencing of a subset of clustered autosomal loci in somatic cells, such as the DUX4 locus (PubMed:23754746, PubMed:23819640, PubMed:28587678). Has ATPase activity; may participate in structural manipulation of chromatin in an ATP-dependent manner as part of its role in gene expression regulation (PubMed:26391951, PubMed:27059856). Also plays a role in DNA repair: localizes to sites of DNA double-strand breaks in response to DNA damage to promote the repair of DNA double-strand breaks (By similarity). Acts by promoting non-homologous end joining (NHEJ) and inhibiting homologous recombination (HR) repair (By similarity). Required during preimplantation development, probably acts by regulating chromatin architecture (PubMed:29900695). {ECO:0000250|UniProtKB:A6NHR9, ECO:0000269|PubMed:18425126, ECO:0000269|PubMed:22841499, ECO:0000269|PubMed:23754746, ECO:0000269|PubMed:23819640, ECO:0000269|PubMed:26091879, ECO:0000269|PubMed:26391951, ECO:0000269|PubMed:27059856, ECO:0000269|PubMed:28587678, ECO:0000269|PubMed:29887375, ECO:0000269|PubMed:29900695}. PTM: Sumoylated with SUMO1. {ECO:0000269|PubMed:23213215}. SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:18425126, ECO:0000269|PubMed:26391951, ECO:0000269|PubMed:29887375}. Note=Recruited to inactivated chromosome X in females by Xist RNA (PubMed:29887375). Localizes at sites of DNA damage at double-strand breaks (DSBs) (By similarity). {ECO:0000250|UniProtKB:A6NHR9, ECO:0000269|PubMed:29887375}. SUBUNIT: Homodimer; homodimerizes via its SMC hinge domain (PubMed:26391951, PubMed:26733688, PubMed:27059856). Interacts with LRIF1 (PubMed:26391951). {ECO:0000269|PubMed:26391951, ECO:0000269|PubMed:26733688, ECO:0000269|PubMed:27059856}. DOMAIN: Atypical member of the structural maintenance of chromosomes (SMC) protein family (PubMed:26733688, PubMed:27059856). Like other members of the SMC family, has ATPase activity, which is probably necessary for its engagement with chromatin, and a SMC hinge domain (PubMed:26733688, PubMed:27059856). However, the SMC hinge domain adopts an unconventional homodimeric arrangement augmented by an intermolecular coiled coil formed between the two monomers. This suggests that protein may assemble as a head-to-head parallel dimer without adopting a hairpin shape at the hinge domain, unlike the dimeric arrangement conventionally found in other members of the SMC protein family (PubMed:26733688). The SMC hinge domain binds DNA and RNA (PubMed:26091879). {ECO:0000269|PubMed:26091879, ECO:0000269|PubMed:26733688, ECO:0000269|PubMed:27059856}. TISSUE SPECIFICITY: During embryogenesis, specifically expressed in immature olfactory sensory neurons. {ECO:0000269|PubMed:28067911}. +O35182 SMAD6_MOUSE Mothers against decapentaplegic homolog 6 (MAD homolog 6) (Mothers against DPP homolog 6) (Mad homolog 7) (SMAD family member 6) (SMAD 6) (Smad6) 495 53,714 Chain (1); Compositional bias (4); Cross-link (1); Domain (2); Metal binding (4); Modified residue (5); Mutagenesis (1); Sequence conflict (1) FUNCTION: Binds to regulatory elements in target promoter regions (By similarity). May block the BMP-SMAD1 signaling pathway by competing with SMAD4 for receptor-activated SMAD1-binding (By similarity). Acts as a mediator of TGF-beta and BMP antiflammatory activity. Suppresses IL1R-TLR signaling through its direct interaction with PEL1, preventing NF-kappa-B activation, nuclear transport and NF-kappa-B-mediated expression of proinflammatory genes. {ECO:0000250, ECO:0000269|PubMed:16951688}. PTM: Monoubiquitinated at Lys-174 by the E2/E3 hybrid ubiquitin-protein ligase UBE2O, leading to reduced binding affinity for the activated BMP type I receptor ACVR1/ALK2, thereby enhancing BMP7 and regulating adipocyte differentiation (By similarity). Ubiquitinated by WWP1 (PubMed:15221015). Ubiquitinated by RNF165, promoting proteasomal degradation, leading to enhance the BMP-Smad signaling (PubMed:23610558). {ECO:0000250|UniProtKB:O43541, ECO:0000269|PubMed:15221015, ECO:0000269|PubMed:23610558}.; PTM: Arginine methylation by PRMT1, which is recruited by BMPR2, initiates BMP-Induced signaling and induces dissociation from the BMPR1B receptor at the cell surface leading to derepress downstream Smad1/Smad5 signaling. {ECO:0000269|PubMed:23747011}.; PTM: Phosphorylated by BMP type 1 receptor kinase and by PRKX. {ECO:0000250|UniProtKB:O43541}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with NEDD4L. Interacts with WWP1. Interacts with STAMBP and PRKX (By similarity). Interacts with RNF111 and AXIN1. Interacts with TGF-beta type I receptor superfamily members, including ACVR1B, BMPR1B and TGFBR1. In response to BMP2 treatment, interacts with SMAD1; this interaction may inhibit SMAD1-binding to SMAD4. Interacts with HOXC8 and HOXC9 (By similarity). Interacts with PELI1; this interaction interferes with PELI1 complex formation with TRAF6, IRAK1, IRAK4 and MYD88 in response to IL1B and hence negatively regulates IL1R-TLR signaling. {ECO:0000250, ECO:0000269|PubMed:14657019, ECO:0000269|PubMed:15221015, ECO:0000269|PubMed:15496141, ECO:0000269|PubMed:16951688}. TISSUE SPECIFICITY: Ubiquitous in various organs, with higher levels in lung. +Q9CZ28 SNF8_MOUSE Vacuolar-sorting protein SNF8 (ESCRT-II complex subunit VPS22) 258 28,886 Chain (1); Coiled coil (1); Modified residue (1) FUNCTION: Component of the endosomal sorting complex required for transport II (ESCRT-II), which is required for multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs. The MVB pathway mediates delivery of transmembrane proteins into the lumen of the lysosome for degradation. The ESCRT-II complex is probably involved in the recruitment of the ESCRT-III complex. The ESCRT-II complex may also play a role in transcription regulation by participating in derepression of transcription by RNA polymerase II, possibly via its interaction with ELL. Required for degradation of both endocytosed EGF and EGFR, but not for the EGFR ligand-mediated internalization. Required for the exosomal release of SDCBP, CD63 and syndecan (By similarity). {ECO:0000250|UniProtKB:Q96H20}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Endosome membrane {ECO:0000250}. Nucleus {ECO:0000305}. Late endosome membrane {ECO:0000250}. Note=Recruited to the endosome membrane to participate in vesicle formation. {ECO:0000250}. SUBUNIT: Component of the endosomal sorting complex required for transport II (ESCRT-II), composed of SNF8, VPS25 and VPS36. SNF8 is essential for the stability of the ESCRT-II complex. ESCRT-II interacts with ELL. Interacts with TSG101 (via the C-terminal domain). Interacts with RILPL1 (via the N-terminal domain); which recruits ESCRT-II to the endosome membranes. Interacts with 14-3-3 proteins (By similarity). {ECO:0000250|UniProtKB:Q96H20}. +Q91WL6 SNX11_MOUSE Sorting nexin-11 271 30,431 Binding site (3); Chain (1); Domain (1); Region (1) FUNCTION: Phosphoinositide-binding protein involved in protein sorting and membrane trafficking in endosomes. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Endosome {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. DOMAIN: The PX domain mediates interaction with membranes enriched in phosphatidylinositol 3-phosphate. {ECO:0000250}. +Q9JLY0 SOCS6_MOUSE Suppressor of cytokine signaling 6 (SOCS-6) (Cytokine-inducible SH2 protein 4) (CIS-4) (Suppressor of cytokine signaling 4) (SOCS-4) 533 59,077 Chain (1); Domain (2); Sequence conflict (4) Protein modification; protein ubiquitination. FUNCTION: SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. May be a substrate recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Regulates KIT degradation by ubiquitination of the tyrosine-phosphorylated receptor (By similarity). {ECO:0000250, ECO:0000269|PubMed:16643902}. SUBUNIT: Interacts with KIT (phosphorylated) (By similarity). Interacts with RBCK1. Interacts with phosphorylated IRS4. Interacts with PIM3. {ECO:0000250, ECO:0000269|PubMed:12052866, ECO:0000269|PubMed:16643902, ECO:0000269|PubMed:21099329}. DOMAIN: The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin ligase complexes. {ECO:0000250}. +Q9JKT2 TR119_MOUSE Taste receptor type 2 member 119 (T2R119) (Taste receptor type 2 member 19) (T2R19) 335 37,735 Chain (1); Glycosylation (2); Sequence conflict (2); Topological domain (8); Transmembrane (7) TRANSMEM 8 28 Helical; Name=1. {ECO:0000255}.; TRANSMEM 44 64 Helical; Name=2. {ECO:0000255}.; TRANSMEM 82 102 Helical; Name=3. {ECO:0000255}.; TRANSMEM 125 145 Helical; Name=4. {ECO:0000255}.; TRANSMEM 177 197 Helical; Name=5. {ECO:0000255}.; TRANSMEM 225 245 Helical; Name=6. {ECO:0000255}.; TRANSMEM 257 277 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 7 Extracellular. {ECO:0000255}.; TOPO_DOM 29 43 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 65 81 Extracellular. {ECO:0000255}.; TOPO_DOM 103 124 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 146 176 Extracellular. {ECO:0000255}.; TOPO_DOM 198 224 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 246 256 Extracellular. {ECO:0000255}.; TOPO_DOM 278 335 Cytoplasmic. {ECO:0000255}. FUNCTION: Gustducin-coupled receptor implicated in the perception of bitter compounds in the oral cavity and the gastrointestinal tract. Signals through PLCB2 and the calcium-regulated cation channel TRPM5. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed in subsets of taste receptor cells of the tongue and palate epithelium and exclusively in gustducin-positive cells. Expressed in 15% taste bud cells in circumvallate and foliate papillae but only in 2% in fungiform papillae. Expressed in the gastro and duodenal tissue. Not expressed in colon, liver, heart and kidney. {ECO:0000269|PubMed:11854532}. +Q8BVL3 SNX17_MOUSE Sorting nexin-17 470 52,797 Binding site (4); Chain (1); Domain (2); Modified residue (7); Region (2); Sequence conflict (1) FUNCTION: Critical regulator of endosomal recycling of numerous receptors, channels, and other transmembrane proteins. Binds to NPxY sequences in the cytoplasmic tails of target cargos. Plays a role in the sorting of endocytosed LRP1 and APP, and prevents their degradation. Required for maintenance of normal cell surface levels of APP and LRP1. Recycles internalized integrins ITGB1, ITGB5 and their associated alpha subunits, preventing them from lysosomal degradation. Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)). {ECO:0000269|PubMed:12169628, ECO:0000269|PubMed:16052210, ECO:0000269|PubMed:18276590}. SUBCELLULAR LOCATION: Cytoplasm. Early endosome. Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. SUBUNIT: Monomer. Interacts with HRAS. Interacts with ITGB1 and ITGB5 (via NPxY motif). Interacts with KRIT1 (via N-terminus) (By similarity). Interacts with the C-termini of P-selectin, PTC, LDLR, VLDLR, LRP1 and LRP8. Interacts with APP (via cytoplasmic YXNPXY motif). Interacts with KIF1B. {ECO:0000250, ECO:0000269|PubMed:12169628, ECO:0000269|PubMed:16052210, ECO:0000269|PubMed:18276590, ECO:0000269|PubMed:19967056}. DOMAIN: The PX domain mediates specific binding to phosphatidylinositol 3-phosphate (PtdIns(P3)). Required for association with endosomes (By similarity). {ECO:0000250}.; DOMAIN: The PTB-like F3 module within the FERM-like domain mediates cargo recognition via their NPxY sequences, while the F1 module (Ras-associating) is responsible for interaction with membrane-bound HRAS. {ECO:0000250}. TISSUE SPECIFICITY: Detected in brain neurons (at protein level). Broadly expressed, with highest levels in brain and placenta, and lowest levels in colon, intestine and liver. {ECO:0000269|PubMed:12169628, ECO:0000269|PubMed:18276590}. +Q7TQB0 TR134_MOUSE Taste receptor type 2 member 134 (T2R134) (Taste receptor type 2 member 34) (T2R34) 298 34,628 Chain (1); Glycosylation (1); Sequence conflict (5); Topological domain (8); Transmembrane (7) TRANSMEM 7 27 Helical; Name=1. {ECO:0000255}.; TRANSMEM 56 76 Helical; Name=2. {ECO:0000255}.; TRANSMEM 97 117 Helical; Name=3. {ECO:0000255}.; TRANSMEM 129 149 Helical; Name=4. {ECO:0000255}.; TRANSMEM 177 197 Helical; Name=5. {ECO:0000255}.; TRANSMEM 230 250 Helical; Name=6. {ECO:0000255}.; TRANSMEM 258 278 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 6 Extracellular. {ECO:0000255}.; TOPO_DOM 28 55 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 77 96 Extracellular. {ECO:0000255}.; TOPO_DOM 118 128 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 150 176 Extracellular. {ECO:0000255}.; TOPO_DOM 198 229 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 251 257 Extracellular. {ECO:0000255}.; TOPO_DOM 279 298 Cytoplasmic. {ECO:0000255}. FUNCTION: Putative taste receptor which may play a role in the perception of bitterness. {ECO:0000303|PubMed:12734386}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. +Q8BXB6 SO2B1_MOUSE Solute carrier organic anion transporter family member 2B1 (Solute carrier family 21 member 9) 683 74,531 Chain (1); Disulfide bond (3); Domain (1); Glycosylation (4); Modified residue (3); Topological domain (13); Transmembrane (12) TRANSMEM 42 61 Helical; Name=1. {ECO:0000255}.; TRANSMEM 81 101 Helical; Name=2. {ECO:0000255}.; TRANSMEM 108 132 Helical; Name=3. {ECO:0000255}.; TRANSMEM 178 207 Helical; Name=4. {ECO:0000255}.; TRANSMEM 227 247 Helical; Name=5. {ECO:0000255}.; TRANSMEM 266 290 Helical; Name=6. {ECO:0000255}.; TRANSMEM 356 377 Helical; Name=7. {ECO:0000255}.; TRANSMEM 398 421 Helical; Name=8. {ECO:0000255}.; TRANSMEM 426 449 Helical; Name=9. {ECO:0000255}.; TRANSMEM 554 576 Helical; Name=10. {ECO:0000255}.; TRANSMEM 586 611 Helical; Name=11. {ECO:0000255}.; TRANSMEM 645 662 Helical; Name=12. {ECO:0000255}. TOPO_DOM 1 41 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 62 80 Extracellular. {ECO:0000255}.; TOPO_DOM 102 107 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 133 177 Extracellular. {ECO:0000255}.; TOPO_DOM 208 226 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 248 265 Extracellular. {ECO:0000255}.; TOPO_DOM 291 355 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 378 397 Extracellular. {ECO:0000255}.; TOPO_DOM 422 425 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 450 553 Extracellular. {ECO:0000255}.; TOPO_DOM 577 585 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 612 644 Extracellular. {ECO:0000255}.; TOPO_DOM 663 683 Cytoplasmic. {ECO:0000255}. FUNCTION: Mediates the Na(+)-independent transport of organic anions such as taurocholate, the prostaglandins PGD2, PGE1, PGE2, leukotriene C4, thromboxane B2 and iloprost. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q9CRB0 SNX24_MOUSE Sorting nexin-24 169 19,653 Binding site (4); Chain (1); Domain (1); Modified residue (3) FUNCTION: May be involved in several stages of intracellular trafficking. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. DOMAIN: The PX domain mediates specific binding to membranes enriched in phosphatidylinositol 3-phosphate (PtdIns(P3)). {ECO:0000250}. +Q8K078 SO4A1_MOUSE Solute carrier organic anion transporter family member 4A1 (Organic anion-transporting polypeptide E) (OATP-E) (Sodium-independent organic anion transporter E) (Solute carrier family 21 member 12) 723 77,669 Alternative sequence (2); Chain (1); Disulfide bond (3); Domain (1); Erroneous initiation (1); Glycosylation (2); Modified residue (3); Sequence conflict (1); Topological domain (13); Transmembrane (12) TRANSMEM 103 123 Helical; Name=1. {ECO:0000255}.; TRANSMEM 143 163 Helical; Name=2. {ECO:0000255}.; TRANSMEM 170 194 Helical; Name=3. {ECO:0000255}.; TRANSMEM 225 255 Helical; Name=4. {ECO:0000255}.; TRANSMEM 275 295 Helical; Name=5. {ECO:0000255}.; TRANSMEM 310 334 Helical; Name=6. {ECO:0000255}.; TRANSMEM 381 402 Helical; Name=7. {ECO:0000255}.; TRANSMEM 423 446 Helical; Name=8. {ECO:0000255}.; TRANSMEM 451 473 Helical; Name=9. {ECO:0000255}.; TRANSMEM 583 605 Helical; Name=10. {ECO:0000255}.; TRANSMEM 615 640 Helical; Name=11. {ECO:0000255}.; TRANSMEM 674 691 Helical; Name=12. {ECO:0000255}. TOPO_DOM 1 102 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 124 142 Extracellular. {ECO:0000255}.; TOPO_DOM 164 169 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 195 224 Extracellular. {ECO:0000255}.; TOPO_DOM 256 274 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 296 309 Extracellular. {ECO:0000255}.; TOPO_DOM 335 380 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 403 422 Extracellular. {ECO:0000255}.; TOPO_DOM 447 450 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 474 582 Extracellular. {ECO:0000255}.; TOPO_DOM 606 614 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 641 673 Extracellular. {ECO:0000255}.; TOPO_DOM 692 723 Cytoplasmic. {ECO:0000255}. FUNCTION: Mediates the Na(+)-independent transport of organic anions such as the thyroid hormone T3 (triiodo-L-thyronine) and of taurocholate. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q6P069 SORCN_MOUSE Sorcin 198 21,627 Alternative sequence (1); Calcium binding (2); Chain (1); Domain (4); Modified residue (1); Sequence conflict (1) FUNCTION: Calcium-binding protein that modulates excitation-contraction coupling in the heart. Contributes to calcium homeostasis in the heart sarcoplasmic reticulum. Modulates the activity of RYR2 calcium channels. {ECO:0000269|PubMed:12824171}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12824171}. Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:12824171}; Peripheral membrane protein {ECO:0000269|PubMed:12824171}; Cytoplasmic side {ECO:0000269|PubMed:12824171}. Note=Relocates to the sarcoplasmic reticulum membrane in response to elevated calcium levels. SUBUNIT: Homodimer. Interacts with GCA, RYR2 and ANXA7 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Detected in cardiac myocytes. {ECO:0000269|PubMed:12824171}. +O88908 SOAT2_MOUSE Sterol O-acyltransferase 2 (EC 2.3.1.26) (Acyl-coenzyme A:cholesterol acyltransferase 2) (ACAT-2) (Cholesterol acyltransferase 2) 525 60,597 Active site (1); Chain (1); Sequence conflict (8); Topological domain (6); Transmembrane (5) TRANSMEM 123 141 Helical. {ECO:0000255}.; TRANSMEM 161 179 Helical. {ECO:0000255}.; TRANSMEM 204 222 Helical. {ECO:0000255}.; TRANSMEM 344 366 Helical. {ECO:0000255}.; TRANSMEM 479 497 Helical. {ECO:0000255}. TOPO_DOM 1 122 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 142 160 Lumenal. {ECO:0000255}.; TOPO_DOM 180 203 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 223 343 Lumenal. {ECO:0000255}.; TOPO_DOM 367 478 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 498 525 Lumenal. {ECO:0000255}. FUNCTION: Plays a role in lipoprotein assembly and dietary cholesterol absorption. In addition to its acyltransferase activity, it may act as a ligase. May provide cholesteryl esters for lipoprotein secretion from hepatocytes and intestinal mucosa. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000269|PubMed:11071899}. SUBUNIT: May form homo- or heterodimers. {ECO:0000250}. +Q3TL54 TR43A_MOUSE Tripartite motif-containing protein 43A 445 52,125 Chain (1); Domain (1); Sequence conflict (1); Zinc finger (2) +Q06831 SOX4_MOUSE Transcription factor SOX-4 440 45,044 Beta strand (1); Chain (1); Compositional bias (1); DNA binding (1); Helix (3); Sequence conflict (5) FUNCTION: Transcriptional activator that binds with high affinity to the T-cell enhancer motif 5'-AACAAAG-3' motif. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with UBE2I. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in lymphocytes and in molar and incisor tooth germs. +Q3UHV4 TR5OS_MOUSE Putative uncharacterized protein TRPC5OS homolog 110 12,052 Chain (1) +Q7TT00 SP20H_MOUSE Transcription factor SPT20 homolog (p38-interacting protein) (p38IP) 530 59,519 Alternative sequence (3); Chain (1); Modified residue (4) FUNCTION: Required for MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) activation during gastrulation. Required for down-regulation of E-cadherin during gastrulation by regulating E-cadherin protein level downstream from NCK-interacting kinase (NIK) and independently of the regulation of transcription by FGF signaling and Snail. Required for starvation-induced ATG9A trafficking during autophagy. {ECO:0000269|PubMed:16751104}. SUBUNIT: Interacts with ATG9A (By similarity). Interacts with MAPK14. {ECO:0000250, ECO:0000269|PubMed:16751104}. TISSUE SPECIFICITY: Ubiquitously expressed throughout development. {ECO:0000269|PubMed:16751104}. +Q5SQF8 SP30L_MOUSE Histone deacetylase complex subunit SAP30L (Sin3 corepressor complex subunit SAP30L) (Sin3-associated protein p30-like) 182 20,745 Chain (1); Cross-link (4); Disulfide bond (2); Erroneous initiation (1); Modified residue (3); Motif (1); Region (1); Zinc finger (1) FUNCTION: Functions as transcription repressor, probably via its interaction with histone deacetylase complexes. Involved in the functional recruitment of the class 1 Sin3-histone deacetylase complex (HDAC) to the nucleolus. Binds DNA, apparently without sequence-specificity, and bends bound double-stranded DNA. Binds phosphoinositol phosphates (phosphoinositol 3-phosphate, phosphoinositol 4-phosphate and phosphoinositol 5-phosphate) via the same basic sequence motif that mediates DNA binding and nuclear import. {ECO:0000250|UniProtKB:Q9HAJ7}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9HAJ7}. SUBUNIT: Interacts with components of the histone deacetylase complex SIN3A, HDAC1 and HDAC2. Binds histones and nucleosomes. Interacts with FEZ1. {ECO:0000250|UniProtKB:Q9HAJ7}. DOMAIN: The zinc-finger domain mediates direct interaction with DNA and phosphoinositol phosphates (phosphoinositol 3-phosphate, phosphoinositol 4-phosphate and phosphoinositol 5-phosphate). In vitro oxydation causes reversible disulfide bond formation between Cys residues in the zinc-finger domain and reversible loss of zinc ion binding. {ECO:0000250|UniProtKB:Q9HAJ7}. +Q3TIT8 SPX3_MOUSE Sugar phosphate exchanger 3 (Solute carrier family 37 member 3) 494 54,553 Chain (1); Glycosylation (1); Sequence conflict (5); Transmembrane (12) TRANSMEM 10 30 Helical. {ECO:0000255}.; TRANSMEM 81 101 Helical. {ECO:0000255}.; TRANSMEM 113 133 Helical. {ECO:0000255}.; TRANSMEM 146 166 Helical. {ECO:0000255}.; TRANSMEM 177 197 Helical. {ECO:0000255}.; TRANSMEM 209 229 Helical. {ECO:0000255}.; TRANSMEM 297 317 Helical. {ECO:0000255}.; TRANSMEM 333 353 Helical. {ECO:0000255}.; TRANSMEM 357 377 Helical. {ECO:0000255}.; TRANSMEM 386 406 Helical. {ECO:0000255}.; TRANSMEM 428 448 Helical. {ECO:0000255}.; TRANSMEM 457 477 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8NCC5}; Multi-pass membrane protein {ECO:0000255}. +D3Z752 SPXN_MOUSE Spexin (NPQ) (Neuropeptide Q) (Spexin hormone) [Cleaved into: Spexin-1; Spexin-2] 116 13,004 Chain (1); Modified residue (1); Peptide (2); Propeptide (3); Signal peptide (1); Site (3) FUNCTION: Plays a role as a central modulator of cardiovascular and renal function and nociception. Plays also a role in energy metabolism and storage. Inhibits adrenocortical cell proliferation with minor stimulation on corticosteroid release (By similarity). {ECO:0000250}.; FUNCTION: Spexin-1: Intracerebroventricular administration of the peptide induces an increase in arterial blood pressure, a decrease in both heart rate and renal excretion and delayed natriuresis. Intraventricular administration of the peptide induces antinociceptive activity. Also induces contraction of muscarinic-like stomach smooth muscles. Acts as a ligand for galanin receptors GALR2 and GALR3 (By similarity). Intraperitoneal administration of the peptide induces a reduction in food consumption and body weight. Inhibits long chain fatty acid uptake into adipocytes (PubMed:24550067). {ECO:0000250, ECO:0000269|PubMed:24550067}.; FUNCTION: Spexin-2: Intracerebroventricular administration of the peptide induces a decrease in heart rate, but no change in arterial pressure, and an increase in urine flow rate. Intraventricular administration of the peptide induces antinociceptive activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24550067}. Secreted, extracellular space {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250}. Note=Secreted via the classical ER/Golgi-dependent pathway into the extracellular medium largely as a full-length protein without the signal peptide, and not as a hydrolyzed and amidated peptide. Localized extracellularly surrounding the villous trophoblastic cells (By similarity). Detected in the serum. {ECO:0000250}. +Q99MY0 SPZ1_MOUSE Spermatogenic leucine zipper protein 1 (BHLH-Zip transcription factor SPZ1) (Spermatogenic Zip 1) 378 43,091 Chain (1); Coiled coil (1); Modified residue (2); Region (4); Sequence conflict (2) FUNCTION: Transcription factor that binds to the DNA sequence 5'-CANNTG-3'(E box) and the G-box motif. Directly binds to a guanine-rich region of the PCNA promoter and up-regulates its expression which in turn induces cell transformation and tumor formation. May play an important role in the regulation of cell proliferation and differentiation during spermatogenesis. {ECO:0000269|PubMed:11165476, ECO:0000269|PubMed:14980513, ECO:0000269|PubMed:15899793}. PTM: Phosphorylated by MAPK1/ERK2 and MAPK3/ERK1. {ECO:0000269|PubMed:15899793}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15226296}. Nucleus {ECO:0000269|PubMed:11165476, ECO:0000269|PubMed:15226296}. SUBUNIT: Interacts with PPP1CC isoform gamma-2. This interaction can prevent SPZ1 binding to the E-box and inhibits PPP1CC activity. {ECO:0000269|PubMed:15226296}. TISSUE SPECIFICITY: Expressed specifically in the testis and epidydimis. In the testis expressed in both germ cells and somatic cells (Sertoli and Leydig cells). Expressed in several tumor cell lines. {ECO:0000269|PubMed:11165476, ECO:0000269|PubMed:14980513, ECO:0000269|PubMed:15899793}. +Q3ULG3 SRARP_MOUSE Steroid receptor-associated and regulated protein 163 17,055 Chain (1) FUNCTION: May regulate the transcriptional function of androgen and estrogen receptors. {ECO:0000250|UniProtKB:Q8NEQ6}. SUBUNIT: Interacts with 14-3-3 proteins. {ECO:0000250|UniProtKB:Q8NEQ6}. +A1L0T3 SRB4D_MOUSE Scavenger receptor cysteine-rich domain-containing group B protein (Four scavenger receptor cysteine-rich domains-containing protein) (S4D-SRCRB) 586 61,916 Chain (1); Disulfide bond (12); Domain (4); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q62417 SRBS1_MOUSE Sorbin and SH3 domain-containing protein 1 (Ponsin) (SH3 domain protein 5) (SH3P12) (c-Cbl-associated protein) (CAP) 1290 143,070 Alternative sequence (10); Chain (1); Domain (4); Erroneous initiation (1); Modified residue (35); Sequence conflict (3) FUNCTION: Plays a role in tyrosine phosphorylation of CBL by linking CBL to the insulin receptor. Required for insulin-stimulated glucose transport. Involved in formation of actin stress fibers and focal adhesions. {ECO:0000269|PubMed:11001060, ECO:0000269|PubMed:9447983, ECO:0000269|PubMed:9461600}. PTM: O-glycosylated. {ECO:0000269|PubMed:16452088}. SUBCELLULAR LOCATION: Cell junction, adherens junction. Cell membrane. Cytoplasm, cytoskeleton. Cell junction, focal adhesion {ECO:0000250}. Nucleus. Nucleus matrix. Note=Colocalized with PXN at focal adhesions during myogenic differentiation (By similarity). Colocalizes with actin stress fibers. Also detected at the plasma membrane and in neuronal intranuclear inclusions. Colocalizes with the Ten-1 ICD form of TENM1 in the nucleus. {ECO:0000250}. SUBUNIT: Interacts (via SH3 domain 2) with PXN (By similarity). Interacts with the long isoform of AFDN and with VCL. AFDN and VCL bind to SORBS1 in a competitive manner and do not form a ternary complex. Interacts with ABL1, CBL, CBLB and INPPL1/SHIP2 through the third SH3 domain. Interaction with ABL1 occurs only after insulin stimulation while this has no effect on the interaction with INPPL1. Interacts with the insulin receptor but dissociates from it following insulin stimulation. Also interacts with SCA7, PTK2/FAK1 and flotillin. Interacts (via third SH3 domain) with the Ten-1 ICD form of TENM1; the interaction induces the translocation of SORBS1 to the nucleus. Interacts with INSM1. {ECO:0000250, ECO:0000269|PubMed:10085297, ECO:0000269|PubMed:11001060, ECO:0000269|PubMed:12079283, ECO:0000269|PubMed:12842890, ECO:0000269|PubMed:15777793, ECO:0000269|PubMed:9447983, ECO:0000269|PubMed:9461600}. TISSUE SPECIFICITY: Expressed in all tissues tested: heart, brain, spleen, lung, liver, muscle, kidney and testis. Expressed in 3T3-L1 adipocytes but not in 3T3-L1 fibroblasts. {ECO:0000269|PubMed:10085297, ECO:0000269|PubMed:9447983}. +Q9WTN3 SRBP1_MOUSE Sterol regulatory element-binding protein 1 (SREBP-1) (Sterol regulatory element-binding transcription factor 1) [Cleaved into: Processed sterol regulatory element-binding protein 1] 1134 120,537 Alternative sequence (2); Chain (2); Compositional bias (2); Domain (1); Modified residue (8); Mutagenesis (5); Region (3); Sequence conflict (5); Site (3); Topological domain (3); Transmembrane (2) TRANSMEM 478 498 Helical. {ECO:0000255}.; TRANSMEM 537 557 Helical. {ECO:0000255}. TOPO_DOM 1 477 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 499 536 Lumenal. {ECO:0000255}.; TOPO_DOM 558 1134 Cytoplasmic. {ECO:0000255}. FUNCTION: Transcriptional activator required for lipid homeostasis. Regulates transcription of the LDL receptor gene as well as the fatty acid and to a lesser degree the cholesterol synthesis pathway. Binds to the sterol regulatory element 1 (SRE-1) (5'-ATCACCCCAC-3'). Has dual sequence specificity binding to both an E-box motif (5'-ATCACGTGA-3') and to SRE-1 (5'-ATCACCCCAC-3'). Isoform SREBP-1A is much more active than isoform SREBP-1C in stimulating transcription from SRE-1-containing promoters. {ECO:0000269|PubMed:11782483, ECO:0000269|PubMed:12855691, ECO:0000269|PubMed:17290224, ECO:0000269|PubMed:9329978, ECO:0000269|PubMed:9784493}. PTM: At low cholesterol the SCAP/SREBP complex is recruited into COPII vesicles for export from the ER. In the Golgi complex SREBPs are cleaved sequentially by site-1 and site-2 protease. The first cleavage by site-1 protease occurs within the luminal loop, the second cleavage by site-2 protease occurs within the first transmembrane domain and releases the transcription factor from the Golgi membrane. Apoptosis triggers cleavage by the cysteine proteases caspase-3 and caspase-7.; PTM: Phosphorylated by AMPK, leading to suppress protein processing and nuclear translocation, and repress target gene expression. Phosphorylation at Ser-389 by SIK1 represses activity possibly by inhibiting DNA-binding. {ECO:0000269|PubMed:19244231, ECO:0000269|PubMed:21459323}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21459323}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:21459323}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000269|PubMed:21459323}; Multi-pass membrane protein {ECO:0000255}. Note=Moves from the endoplasmic reticulum to the Golgi in the absence of sterols (PubMed:21459323). {ECO:0000269|PubMed:21459323}.; SUBCELLULAR LOCATION: Processed sterol regulatory element-binding protein 1: Nucleus {ECO:0000269|PubMed:21459323}. SUBUNIT: Forms a tight complex with SCAP in the ER membrane. Efficient DNA binding of the soluble transcription factor fragment requires dimerization with another bHLH protein. Interacts with LMNA. Interacts with CEBPA, the interaction produces a transcriptional synergy (PubMed:17290224). {ECO:0000269|PubMed:11929849, ECO:0000269|PubMed:17290224}. TISSUE SPECIFICITY: Isoform SREBP-1C predominates in liver, adrenal gland, brain and adipose tissue, whereas isoform SREBP-1A predominates in spleen. Isoform SREBP-1A and isoform SREBP-1C are found in kidney, thymus, testis, muscle, jejunum, and ileum. +Q7TQ48 SRCA_MOUSE Sarcalumenin 910 99,184 Alternative sequence (1); Chain (1); Domain (1); Glycosylation (3); Modified residue (1); Region (6); Signal peptide (1) FUNCTION: May be involved in the regulation of calcium transport. SUBCELLULAR LOCATION: Sarcoplasmic reticulum lumen {ECO:0000250}. Note=Associated through calcium with the membrane. {ECO:0000250}. +Q9QWI6 SRCN1_MOUSE SRC kinase signaling inhibitor 1 (SNAP-25-interacting protein) (SNIP) (p130Cas-associated protein) (p140Cap) 1250 134,859 Alternative sequence (2); Chain (1); Coiled coil (2); Compositional bias (1); Frameshift (1); Modified residue (40); Region (1); Sequence conflict (6) FUNCTION: Acts as a negative regulator of SRC by activating CSK which inhibits SRC activity and downstream signaling, leading to impaired cell spreading and migration. Regulates dendritic spine morphology. Involved in calcium-dependent exocytosis. May play a role in neurotransmitter release or synapse maintenance (By similarity). {ECO:0000250}. PTM: Tyrosine-phosphorylated in response to EGF and to cell adhesion to integrin ligands. {ECO:0000250|UniProtKB:Q9C0H9}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell projection, axon {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cell junction, synapse {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250}. Note=Localized to the perinuclear region, lamellopodia, cortical actin and actin stress fibers but not to focal adhesions. Strongly expressed in axons and dendrites of the CA1 and CA3 hippocampal regions and of the dentate gyrus. Detected in both presynapses and postsynapses and in postsynaptic density fractions (By similarity). {ECO:0000250}. SUBUNIT: Interacts with the N-terminal coiled-coil region of SNAP25. Interacts with BCAR1/p130Cas and SRC through its C-terminal domain. Interacts with CSK, CTTN, SORBS3/vinexin, SYP and MAPRE3/EB3 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed predominantly in central nervous system with high levels detected in cortex, cerebellum, midbrain and spinal cord (at protein level). Also expressed in testis and epithelial-rich tissues such as mammary gland, lung and kidney. {ECO:0000269|PubMed:14657239, ECO:0000269|PubMed:19146815}. +Q8BV57 SRCRL_MOUSE Soluble scavenger receptor cysteine-rich domain-containing protein SSC5D (Scavenger receptor cysteine-rich domain-containing protein LOC284297 homolog) 1371 144,637 Chain (1); Disulfide bond (15); Domain (5); Glycosylation (4); Sequence conflict (3); Signal peptide (1) FUNCTION: Binds to extracellular matrix proteins. Binds to pathogen-associated molecular patterns (PAMPs) present on the cell walls of Gram-positive and Gram-negative bacteria and fungi, behaving as a pattern recognition receptor (PRR). Induces bacterial and fungal aggregation and subsequent inhibition of PAMP-induced cytokine release. Does not possess intrinsic bactericidal activity. May play a role in the innate defense and homeostasis of certain epithelial surfaces. {ECO:0000269|PubMed:21217009}. PTM: Partially N- and O-glycosylated. {ECO:0000269|PubMed:21217009}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21217009}. Cytoplasm {ECO:0000269|PubMed:21217009}. SUBUNIT: Interacts with LGALS1 and laminin. {ECO:0000269|PubMed:21217009}. TISSUE SPECIFICITY: Detected throughout the gastrointestinal and genitourinary tracts, in serosal salivary gland, the exocrine part of pancreas and testis, as well as in a few tubular structures in kidney. Not detected in lung and heart (at protein level). Strongly expressed in testis, kidney and pancreas, with lower levels detected in bone marrow, spleen, lung, liver, colon, stomach and skeletal muscle. Very low levels or no expression detected in thymus, esophagus, jejunum, ileum, duodenum, ovary, uterus, heart, trachea, brain, cerebellum and bladder. {ECO:0000269|PubMed:21217009}. +Q9JM73 SRF_MOUSE Serum response factor (SRF) 504 51,247 Chain (1); Compositional bias (3); DNA binding (1); Domain (1); Glycosylation (5); Modified residue (9); Region (1) FUNCTION: SRF is a transcription factor that binds to the serum response element (SRE), a short sequence of dyad symmetry located 300 bp to the 5' of the site of transcription initiation of some genes (such as FOS) (PubMed:24732378). Together with MRTFA transcription coactivator, controls expression of genes regulating the cytoskeleton during development, morphogenesis and cell migration (PubMed:12732141, PubMed:19350017, PubMed:24732378). The SRF-MRTFA complex activity responds to Rho GTPase-induced changes in cellular globular actin (G-actin) concentration, thereby coupling cytoskeletal gene expression to cytoskeletal dynamics (PubMed:24732378). Required for cardiac differentiation and maturation (PubMed:15169892). {ECO:0000269|PubMed:12732141, ECO:0000269|PubMed:15169892, ECO:0000269|PubMed:19350017, ECO:0000269|PubMed:24732378}. PTM: Phosphorylated by PRKDC. {ECO:0000250|UniProtKB:P11831}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251, ECO:0000269|PubMed:19350017}. SUBUNIT: Binds DNA as a multimer, probably a dimer (PubMed:15492011, PubMed:16782067). Interacts with MRTFA, forming the SRF-MRTFA nuclear complex which binds the 5'-CArG-3' consensus motif (CArG box) on DNA via SRF (PubMed:12732141, PubMed:19350017). Forms a nuclear ternary complex with MRTFA and SCAI (PubMed:19350017). Interacts with MRTFB (By similarity). Interacts with MLLT7/FOXO4, NKX3A and SSRP1 (By similarity). Interacts with ARID2 (PubMed:16782067). Interacts with SRFBP1 (PubMed:15492011). Interacts with LPXN (By similarity). Interacts with OLFM2; the interaction promotes dissociation of SRF from the transcriptional repressor HEY2, facilitates binding of SRF to target genes and promotes smooth muscle differentiation (By similarity). {ECO:0000250|UniProtKB:P11831, ECO:0000269|PubMed:12732141, ECO:0000269|PubMed:15492011, ECO:0000269|PubMed:16782067, ECO:0000269|PubMed:19350017}. +Q812A2 SRGP3_MOUSE SLIT-ROBO Rho GTPase-activating protein 3 (srGAP3) (Rho GTPase-activating protein 14) (WAVE-associated Rac GTPase-activating protein) (WRP) 1099 124,420 Chain (1); Coiled coil (2); Domain (3); Erroneous initiation (2); Frameshift (1); Modified residue (6); Sequence caution (2); Sequence conflict (3) FUNCTION: GTPase-activating protein for RAC1 and perhaps CDC42, but not for RhoA small GTPase. May attenuate RAC1 signaling in neurons (By similarity). {ECO:0000250}. SUBUNIT: Homodimer (Probable). Forms a heterooligomer with SRGAP1 and SRGAP2 through its F-BAR domain. Interacts with WASF1. Probably interacts with ROBO1. Interacts with FASLG (By similarity). {ECO:0000250, ECO:0000305}. DOMAIN: The F-BAR domain mediates oligomerization, binds membranes, and induces plasma membrane protrusions. {ECO:0000250}. +Q8BTI8 SRRM2_MOUSE Serine/arginine repetitive matrix protein 2 2703 294,840 Alternative sequence (2); Chain (1); Coiled coil (1); Compositional bias (6); Cross-link (3); Erroneous initiation (1); Modified residue (265); Region (1); Sequence conflict (17) FUNCTION: Involved in pre-mRNA splicing. May function at or prior to the first catalytic step of splicing at the catalytic center of the spliceosome. May do so by stabilizing the catalytic center or the position of the RNA substrate. Binds to RNA (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}. SUBUNIT: Component of the active spliceosome. Found in a pre-mRNA splicing complex with SFRS4, SFRS5, SNRP70, SNRPA1, SRRM1 and SRRM2. Identified in the spliceosome C complex (By similarity). {ECO:0000250}. +Q9Z0G2 SRPK3_MOUSE SRSF protein kinase 3 (EC 2.7.11.1) (Muscle-specific serine kinase 1) (MSSK-1) (Serine/arginine-rich protein-specific kinase 3) (SR-protein-specific kinase 3) (Serine/threonine-protein kinase 23) 565 62,365 Active site (1); Binding site (1); Chain (1); Compositional bias (1); Domain (1); Modified residue (2); Nucleotide binding (1) FUNCTION: Serine/arginine-rich protein-specific kinase which specifically phosphorylates its substrates at serine residues located in regions rich in arginine/serine dipeptides, known as RS domains. Phosphorylates the SR splicing factor SRSF1 and the lamin-B receptor (LBR) in vitro. Required for normal muscle development. {ECO:0000269|PubMed:16140986}. TISSUE SPECIFICITY: Exclusively expressed in skeletal and heart muscle. {ECO:0000269|PubMed:16140986}. +Q99MR6 SRRT_MOUSE Serrate RNA effector molecule homolog (Arsenite-resistance protein 2) 875 100,452 Alternative sequence (2); Chain (1); Compositional bias (3); Cross-link (1); Erroneous initiation (2); Initiator methionine (1); Modified residue (15); Sequence conflict (1) FUNCTION: Acts as a mediator between the cap-binding complex (CBC) and the primary microRNAs (miRNAs) processing machinery during cell proliferation. Contributes to the stability and delivery of capped primary miRNA transcripts to the primary miRNA processing complex containing DGCR8 and DROSHA, thereby playing a role in RNA-mediated gene silencing (RNAi) by miRNAs. Binds capped RNAs (m7GpppG-capped RNA); however interaction is probably mediated via its interaction with NCBP1/CBP80 component of the CBC complex. Involved in cell cycle progression at S phase. Does not directly confer arsenite resistance but rather modulates arsenic sensitivity. Independently of its activity on miRNAs, necessary and sufficient to promote neural stem cell self-renewal. Does so by directly binding SOX2 promoter and positively regulating its transcription. {ECO:0000269|PubMed:19632182, ECO:0000269|PubMed:22198669}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm. Cytoplasm. Note=Predominantly nuclear. Shuttles between the nucleus and the cytoplasm in a CRM1-dependent way. SUBUNIT: Interacts with CASP8AP2 and ERBB4 (By similarity). Interacts with NCBP1/CBP80 and DROSHA (PubMed:19632182). Interacts with LUZP4 (By similarity). Interacts with NCBP2/CBP20 and NCBP3 (By similarity). {ECO:0000250|UniProtKB:Q9BXP5, ECO:0000269|PubMed:19632182}. TISSUE SPECIFICITY: Widely expressed, with a preference for proliferating cells. Highly expressed in hematopoietic tissues and reduced or absent expression in parenchymal organs like liver and kidney. In the brain, expressed in the subventricular zone by niche astrocytes, ependymal cells and neural stem cells. In this cerebral context, expressed in slowly dividing cells. {ECO:0000269|PubMed:18086880, ECO:0000269|PubMed:19632182, ECO:0000269|PubMed:22198669}. +Q8CD78 SRTM1_MOUSE Serine-rich and transmembrane domain-containing protein 1 107 11,392 Chain (1); Compositional bias (1); Transmembrane (1) TRANSMEM 43 63 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +A0A1B0GSN8 SRTM2_MOUSE Serine-rich and transmembrane domain-containing 2 89 10,093 Chain (1); Glycosylation (1); Transmembrane (1) TRANSMEM 38 58 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. +Q9D975 SRXN1_MOUSE Sulfiredoxin-1 (EC 1.8.98.2) (Neoplastic progression protein 3) 136 14,149 Chain (1); Disulfide bond (1); Modified residue (2); Nucleotide binding (1); Sequence conflict (1) FUNCTION: Contributes to oxidative stress resistance by reducing cysteine-sulfinic acid formed under exposure to oxidants in the peroxiredoxins PRDX1, PRDX2, PRDX3 and PRDX4. Does not act on PRDX5 or PRDX6. May catalyze the reduction in a multi-step process by acting both as a specific phosphotransferase and a thioltransferase. {ECO:0000269|PubMed:15448164}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +Q3TWW8 SRSF6_MOUSE Serine/arginine-rich splicing factor 6 (Pre-mRNA-splicing factor SRP55) (Splicing factor, arginine/serine-rich 6) 339 39,025 Chain (1); Compositional bias (2); Cross-link (1); Domain (2); Modified residue (9); Sequence conflict (4) FUNCTION: Plays a role in constitutive splicing and modulates the selection of alternative splice sites. Plays a role in the alternative splicing of MAPT/Tau exon 10. Binds to alternative exons of TNC pre-mRNA and promotes the expression of alternatively spliced TNC. Plays a role in wound healing and in the regulation of keratinocyte differentiation and proliferation via its role in alternative splicing (By similarity). {ECO:0000250}. PTM: Extensively phosphorylated on serine residues in the RS domain. Phosphorylated by DYRK1A, probably in the RS domain. Phosphorylation by DYRK1A modulates alternative splice site selection and inhibits the expression of MAPT/Tau exon 10 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12549914}. Nucleus speckle {ECO:0000250|UniProtKB:Q13247}. SUBUNIT: Binds SREK1/SFRS12. Interacts with DYRK1A (By similarity). {ECO:0000250}. +Q9CYR0 SSBP_MOUSE Single-stranded DNA-binding protein, mitochondrial (Mt-SSB) (MtSSB) 152 17,319 Chain (1); Domain (1); Modified residue (4); Transit peptide (1) FUNCTION: This protein binds preferentially and cooperatively to ss-DNA. Probably involved in mitochondrial DNA replication. Associates with mitochondrial DNA (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Mitochondrion matrix, mitochondrion nucleoid {ECO:0000250}. SUBUNIT: Homotetramer. Interacts with MPG/AAG, through inhibition of its glycosylase activity it potentially prevents formation of DNA breaks in ssDNA, ensuring that base removal primarily occurs in dsDNA. {ECO:0000250}. +Q8BWF0 SSDH_MOUSE Succinate-semialdehyde dehydrogenase, mitochondrial (EC 1.2.1.24) (Aldehyde dehydrogenase family 5 member A1) (NAD(+)-dependent succinic semialdehyde dehydrogenase) 523 55,968 Active site (2); Binding site (4); Chain (1); Disulfide bond (1); Modified residue (15); Nucleotide binding (2); Site (1); Transit peptide (1) Amino-acid degradation; 4-aminobutanoate degradation. FUNCTION: Catalyzes one step in the degradation of the inhibitory neurotransmitter gamma-aminobutyric acid (GABA). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. SUBUNIT: Homotetramer. {ECO:0000250}. +Q91YU8 SSF1_MOUSE Suppressor of SWI4 1 homolog (Ssf-1) (Peter Pan homolog) 470 52,756 Chain (1); Domain (1); Modified residue (4); Sequence conflict (1) FUNCTION: May have a role in cell growth. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. +Q5SW75 SSH2_MOUSE Protein phosphatase Slingshot homolog 2 (EC 3.1.3.16) (EC 3.1.3.48) (SSH-like protein 2) (SSH-2L) (mSSH-2L) 1423 158,230 Active site (1); Alternative sequence (4); Chain (1); Domain (1); Erroneous gene model prediction (3); Modified residue (10); Mutagenesis (1); Sequence caution (1); Sequence conflict (2) FUNCTION: Protein phosphatase which regulates actin filament dynamics. Dephosphorylates and activates the actin binding/depolymerizing factor cofilin, which subsequently binds to actin filaments and stimulates their disassembly. Inhibitory phosphorylation of cofilin is mediated by LIMK1, which may also be dephosphorylated and inactivated by this protein. {ECO:0000269|PubMed:14531860}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:14531860}. Cell junction, focal adhesion {ECO:0000269|PubMed:14531860}. Note=Colocalizes with filamentous actin in the cytoplasm and the cell periphery. Also localizes to focal adhesions. SUBUNIT: Interacts with filamentous actin. {ECO:0000269|PubMed:14531860}. TISSUE SPECIFICITY: Expressed in brain, heart, liver, skeletal muscle, testis and thymus. Also expressed at lower levels in kidney, small intestine and spleen. {ECO:0000269|PubMed:14531860}. +Q8K330 SSH3_MOUSE Protein phosphatase Slingshot homolog 3 (EC 3.1.3.16) (EC 3.1.3.48) (SSH-like protein 3) (SSH-3L) (mSSH-3L) 649 72,227 Active site (1); Alternative sequence (1); Chain (1); Domain (1); Initiator methionine (1); Modified residue (4); Mutagenesis (1); Sequence conflict (1) FUNCTION: Protein phosphatase which may play a role in the regulation of actin filament dynamics. Can dephosphorylate and activate the actin binding/depolymerizing factor cofilin, which subsequently binds to actin filaments and stimulates their disassembly. {ECO:0000269|PubMed:14531860}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:14531860}. Nucleus {ECO:0000269|PubMed:14531860}. SUBUNIT: Does not bind to, or colocalize with, filamentous actin. TISSUE SPECIFICITY: Expressed in brain, small intestine and testis. Also expressed at lower levels in heart, kidney, liver, spleen and thymus. {ECO:0000269|PubMed:14531860}. +Q3UN54 SSLP1_MOUSE Secreted seminal-vesicle Ly-6 protein 1 (SSLP-1) 99 11,155 Chain (1); Disulfide bond (5); Glycosylation (2); Signal peptide (1) PTM: Glycosylated. {ECO:0000269|PubMed:16940290}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16940290}. SUBUNIT: Monomer. {ECO:0000269|PubMed:16940290}. TISSUE SPECIFICITY: Predominantly expressed in the seminal vesicles. {ECO:0000269|PubMed:16940290}. +Q9JJ94 SSNA1_MOUSE Sjoegren syndrome nuclear autoantigen 1 homolog 119 13,557 Chain (1); Coiled coil (1); Initiator methionine (1); Modified residue (1) SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. +Q62147 SSPN_MOUSE Sarcospan (K-ras oncogene-associated protein) (Kirsten-Ras-associated protein) 216 23,859 Chain (1); Sequence conflict (1); Topological domain (5); Transmembrane (4) TRANSMEM 27 47 Helical. {ECO:0000255}.; TRANSMEM 60 80 Helical. {ECO:0000255}.; TRANSMEM 96 116 Helical. {ECO:0000255}.; TRANSMEM 167 187 Helical. {ECO:0000255}. TOPO_DOM 1 26 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 48 59 Extracellular. {ECO:0000255}.; TOPO_DOM 81 95 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 117 166 Extracellular. {ECO:0000255}.; TOPO_DOM 188 216 Cytoplasmic. {ECO:0000255}. FUNCTION: Component of the dystrophin-glycoprotein complex (DGC), a complex that spans the muscle plasma membrane and forms a link between the F-actin cytoskeleton and the extracellular matrix. Preferentially associates with the sarcoglycan subcomplex of the DGC (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane, sarcolemma {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Also found in myotendinous junctions and in the postsynaptic membrane of neuromuscular junctions. {ECO:0000250}. +P30875 SSR2_MOUSE Somatostatin receptor type 2 (SS-2-R) (SS2-R) (SS2R) (SRIF-1) 369 41,222 Alternative sequence (1); Chain (1); Disulfide bond (1); Glycosylation (4); Lipidation (1); Modified residue (5); Sequence conflict (2); Topological domain (8); Transmembrane (7) TRANSMEM 44 67 Helical; Name=1. {ECO:0000255}.; TRANSMEM 79 103 Helical; Name=2. {ECO:0000255}.; TRANSMEM 119 138 Helical; Name=3. {ECO:0000255}.; TRANSMEM 162 181 Helical; Name=4. {ECO:0000255}.; TRANSMEM 208 229 Helical; Name=5. {ECO:0000255}.; TRANSMEM 254 278 Helical; Name=6. {ECO:0000255}.; TRANSMEM 289 303 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 43 Extracellular. {ECO:0000255}.; TOPO_DOM 68 78 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 104 118 Extracellular. {ECO:0000255}.; TOPO_DOM 139 161 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 182 207 Extracellular. {ECO:0000255}.; TOPO_DOM 230 253 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 279 288 Extracellular. {ECO:0000255}.; TOPO_DOM 304 369 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for somatostatin-14 and -28. This receptor is coupled via pertussis toxin sensitive G proteins to inhibition of adenylyl cyclase. In addition it stimulates phosphotyrosine phosphatase and PLC via pertussis toxin insensitive as well as sensitive G proteins. Inhibits calcium entry by suppressing voltage-dependent calcium channels. Acts as the functionally dominant somatostatin receptor in pancreatic alpha- and beta-cells where it mediates the inhibitory effect of somatostatin-14 on hormone secretion. Inhibits cell growth through enhancement of MAPK1 and MAPK2 phosphorylation and subsequent up-regulation of CDKN1B. Stimulates neuronal migration and axon outgrowth and may participate in neuron development and maturation during brain development. Mediates negative regulation of insulin receptor signaling through PTPN6. Inactivates SSTR3 receptor function following heterodimerization. {ECO:0000269|PubMed:8104154, ECO:0000269|PubMed:9507021}. PTM: Phosphorylated on serine and threonine residues in response to agonist stimulation, leading to receptor desensitization and rapid internalization. Phosphorylated to a greater extent on serine than threonine residues. Threonine phosphorylation is required for arrestin binding and receptor endocytosis but is not necessary for desensitization (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8104154}; Multi-pass membrane protein {ECO:0000269|PubMed:8104154}. Cytoplasm {ECO:0000250}. Note=Located mainly at the cell surface under basal conditions. Agonist stimulation results in internalization to the cytoplasm (By similarity). {ECO:0000250}. SUBUNIT: Homodimer and heterodimer with SSTR3 and SSTR5. Heterodimerization with SSTR3 inactivates SSTR3 receptor function. Heterodimerization with SSTR5 is enhanced by agonist stimulation of SSTR2 and increases SSTR2 cell growth inhibition activity. Following agonist stimulation, homodimers dissociate into monomers which is required for receptor internalization. Interacts with beta-arrestin; this interaction is necessary for receptor internalization and is destabilized by heterodimerization with SSTR5 which results in increased recycling of SSTR2 to the cell surface. Interacts (via C-terminus) with SHANK1 (via PDZ domain) (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Cerebrum and kidney. +P30935 SSR3_MOUSE Somatostatin receptor type 3 (SS-3-R) (SS3-R) (SS3R) (SSR-28) 428 47,216 Chain (1); Compositional bias (1); Disulfide bond (1); Glycosylation (2); Modified residue (4); Sequence conflict (8); Topological domain (8); Transmembrane (7) TRANSMEM 46 71 Helical; Name=1. {ECO:0000255}.; TRANSMEM 82 103 Helical; Name=2. {ECO:0000255}.; TRANSMEM 119 140 Helical; Name=3. {ECO:0000255}.; TRANSMEM 163 182 Helical; Name=4. {ECO:0000255}.; TRANSMEM 207 232 Helical; Name=5. {ECO:0000255}.; TRANSMEM 267 288 Helical; Name=6. {ECO:0000255}.; TRANSMEM 303 325 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 45 Extracellular. {ECO:0000255}.; TOPO_DOM 72 81 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 104 118 Extracellular. {ECO:0000255}.; TOPO_DOM 141 162 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 183 206 Extracellular. {ECO:0000255}.; TOPO_DOM 233 266 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 289 302 Extracellular. {ECO:0000255}.; TOPO_DOM 326 428 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for somatostatin-14 and -28. This receptor is coupled via pertussis toxin sensitive G proteins to inhibition of adenylyl cyclase. {ECO:0000269|PubMed:1328199}. PTM: Phosphorylated. Phosphorylation increases upon somatostatin binding (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Internalized into endoplasmic vesicles upon somatostatin-stimulation. {ECO:0000250}. SUBUNIT: Homodimer and heterodimer with SSTR2. Heterodimerization with SSTR2 inactivates SSTR3 receptor function (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: In the brain, primarily observed in the forebrain. Moderate levels found throughout laminae 2-6 of the neocortex and allocortex, and high levels in lamina 2 of the piriform and entorhinal cortices. High levels also present in the cornu ammonis fields of the hippocampus. In the amygdala, highly expressed in the nucleus of the lateral olfactory tract with expression also detected in the rostral portions of the basal magnocellular and lateral nuclei. In the diencephalon, moderate levels observed in the ventromedial and arcuate nuclei of the hypothalamus. In the midbrain, moderate levels found in the lateral portion of the substantia nigra pars reticulata. {ECO:0000269|PubMed:1328199}. +O08858 SSR5_MOUSE Somatostatin receptor type 5 (SS-5-R) (SS5-R) (SS5R) 362 40,008 Chain (1); Disulfide bond (1); Erroneous initiation (1); Glycosylation (3); Lipidation (1); Sequence conflict (14); Topological domain (8); Transmembrane (7) TRANSMEM 36 63 Helical; Name=1. {ECO:0000255}.; TRANSMEM 74 99 Helical; Name=2. {ECO:0000255}.; TRANSMEM 111 132 Helical; Name=3. {ECO:0000255}.; TRANSMEM 155 175 Helical; Name=4. {ECO:0000255}.; TRANSMEM 196 220 Helical; Name=5. {ECO:0000255}.; TRANSMEM 247 272 Helical; Name=6. {ECO:0000255}.; TRANSMEM 283 307 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 35 Extracellular. {ECO:0000255}.; TOPO_DOM 64 73 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 100 110 Extracellular. {ECO:0000255}.; TOPO_DOM 133 154 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 176 195 Extracellular. {ECO:0000255}.; TOPO_DOM 221 246 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 273 282 Extracellular. {ECO:0000255}.; TOPO_DOM 308 362 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for somatostatin-28. The activity of this receptor is mediated by G proteins which inhibit adenylyl cyclase. Increases cell growth inhibition activity of SSTR2 following heterodimerization. PTM: Palmitoylated at Cys-319 by ZDHHC5, but not ZDHHC8. Palmitoylation creates an additional intracellular loop which is thought to be important for efficient coupling to G-proteins and may target the protein to lipid rafts. {ECO:0000269|PubMed:21820437}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21820437}; Multi-pass membrane protein {ECO:0000269|PubMed:21820437}. SUBUNIT: Heterodimer with SSTR2. Heterodimerization with SSTR2 increases cell growth inhibition activity of SSTR2 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in adult brain but not in liver, heart, spleen, or kidney. {ECO:0000269|PubMed:9300821}. +Q9CY50 SSRA_MOUSE Translocon-associated protein subunit alpha (TRAP-alpha) (Signal sequence receptor subunit alpha) (SSR-alpha) 286 32,065 Chain (1); Glycosylation (2); Modified residue (3); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 208 228 Helical. {ECO:0000255}. TOPO_DOM 22 207 Lumenal. {ECO:0000255}.; TOPO_DOM 229 286 Cytoplasmic. {ECO:0000255}. FUNCTION: TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins. May be involved in the recycling of the translocation apparatus after completion of the translocation process or may function as a membrane-bound chaperone facilitating folding of translocated proteins. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Heterotetramer of TRAP-alpha, TRAP-beta, TRAP-delta and TRAP-gamma. Interacts with palmitoylated calnexin (CALX), the interaction is required for efficient folding of glycosylated proteins (By similarity). {ECO:0000250}. DOMAIN: Shows a remarkable charge distribution with the N-terminus being highly negatively charged, and the cytoplasmic C-terminus positively charged. +Q9CPW5 SSRB_MOUSE Translocon-associated protein subunit beta (TRAP-beta) (Signal sequence receptor subunit beta) (SSR-beta) 183 20,019 Chain (1); Glycosylation (2); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 147 167 Helical. {ECO:0000255}. TOPO_DOM 18 146 Lumenal. {ECO:0000255}.; TOPO_DOM 168 183 Cytoplasmic. {ECO:0000255}. FUNCTION: TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Heterotetramer of TRAP-alpha, TRAP-beta, TRAP-delta and TRAP-gamma. Interacts with TMEM173/STING (By similarity). {ECO:0000250}. +Q62186 SSRD_MOUSE Translocon-associated protein subunit delta (TRAP-delta) (Signal sequence receptor subunit delta) (SSR-delta) 172 18,937 Chain (1); Cross-link (1); Disulfide bond (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 144 164 Helical. {ECO:0000255}. TOPO_DOM 24 143 Lumenal. {ECO:0000255}.; TOPO_DOM 165 172 Cytoplasmic. {ECO:0000255}. FUNCTION: TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Heterotetramer of TRAP-alpha, TRAP-beta, TRAP-delta and TRAP-gamma. {ECO:0000250}. +Q8K558 TRML1_MOUSE Trem-like transcript 1 protein (TLT-1) (Triggering receptor expressed on myeloid cells-like protein 1) 317 33,522 Alternative sequence (1); Chain (1); Compositional bias (1); Disulfide bond (2); Domain (1); Lipidation (1); Modified residue (1); Motif (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 176 196 Helical. {ECO:0000255}. TOPO_DOM 21 175 Extracellular. {ECO:0000255}.; TOPO_DOM 197 317 Cytoplasmic. {ECO:0000255}. FUNCTION: Cell surface receptor that may play a role in the innate and adaptive immune response. {ECO:0000269|PubMed:12393607}. PTM: Phosphorylated on tyrosine residues. {ECO:0000269|PubMed:12393607}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15100151}; Single-pass type I membrane protein {ECO:0000269|PubMed:15100151}. Cytoplasm {ECO:0000269|PubMed:15100151}. Note=Sequestered in cytoplasmic vesicles in resting platelets. Transported to the cell surface after stimulation by thrombin. Soluble fragments can be released into the serum by proteolysis. {ECO:0000250|UniProtKB:Q86YW5}. SUBUNIT: When phosphorylated, interacts with PTPN11 (By similarity). When phosphorylated, interacts with PTPN6. {ECO:0000250, ECO:0000269|PubMed:12393607}. TISSUE SPECIFICITY: Highly expressed in bone marrow leukocytes, splenic megakaryocytes and platelets. Detected in brain, liver and in peritoneal monocytes. {ECO:0000269|PubMed:12393607, ECO:0000269|PubMed:15100151}. +P13675 SSTY1_MOUSE Y-linked testis-specific protein 1 232 26,796 Chain (1) TISSUE SPECIFICITY: Expressed in testis (at protein level). {ECO:0000269|PubMed:14667817}. +Q9CY97 SSU72_MOUSE RNA polymerase II subunit A C-terminal domain phosphatase SSU72 (CTD phosphatase SSU72) (EC 3.1.3.16) 194 22,517 Alternative sequence (1); Chain (1); Coiled coil (1); Sequence conflict (1) FUNCTION: Protein phosphatase that catalyzes the dephosphorylation of the C-terminal domain of RNA polymerase II. Plays a role in RNA processing and termination. Plays a role in pre-mRNA polyadenylation via its interaction with SYMPK. {ECO:0000269|PubMed:15659578}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Predominantly in the cytosol. {ECO:0000250}. SUBUNIT: Interacts with GTF2B (via C-terminus); this interaction is inhibited by SYMPK. Interacts with RB1. Interacts with CD226. Interacts with SYMPK. {ECO:0000250|UniProtKB:Q9NP77}. TISSUE SPECIFICITY: Highly expressed in the brain. Expressed at low level in most tissues. {ECO:0000269|PubMed:15659578}. +Q562D6 TRMO_MOUSE tRNA (adenine(37)-N6)-methyltransferase (EC 2.1.1.-) (tRNA methyltransferase O) 431 47,559 Alternative sequence (2); Chain (1); Domain (1); Sequence conflict (1) FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase responsible for the addition of the methyl group in the formation of N6-methyl-N6-threonylcarbamoyladenosine at position 37 (m(6)t(6)A37) of the tRNA anticodon loop of tRNA(Ser)(GCU). The methyl group of m(6)t(6)A37 may improve the efficiency of the tRNA decoding ability. May bind to tRNA. {ECO:0000250|UniProtKB:P28634, ECO:0000250|UniProtKB:Q9BU70}. +B1AUS7 SSXA1_MOUSE Protein SSXA1 (Synovial sarcoma, X member A1) 101 11,929 Chain (1); Domain (1) FUNCTION: Could act as a modulator of transcription. {ECO:0000305}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21725589}. TISSUE SPECIFICITY: Specifically expressed in testis (at protein level). Not detected in other tissues tested (at protein level). {ECO:0000269|PubMed:21725589}. +Q62280 SSXT_MOUSE Protein SSXT (Protein SYT) (Synovial sarcoma-associated Ss18-alpha) 418 45,864 Chain (1); Compositional bias (2); Initiator methionine (1); Modified residue (1); Motif (4); Region (1); Repeat (2); Sequence conflict (2) FUNCTION: Appears to function synergistically with RBM14 as a transcriptional coactivator. Component of SWI/SNF chromatin remodeling subcomplex GBAF that carries out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. {ECO:0000250|UniProtKB:Q15532}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15532}. SUBUNIT: Interacts with MLLT10 (By similarity). Component of the multiprotein chromatin-remodeling complexes SWI/SNF: SWI/SNF-A (BAF), SWI/SNF-B (PBAF) and related complexes. The canonical complex contains a catalytic subunit (either SMARCA4/BRG1/BAF190A or SMARCA2/BRM/BAF190B) and at least SMARCE1, ACTL6A/BAF53, SMARCC1/BAF155, SMARCC2/BAF170, and SMARCB1/SNF5/BAF47. Other subunits specific to each of the complexes may also be present permitting several possible combinations developmentally and tissue specific. Component of the SWI/SNF (GBAF) subcomplex, which includes at least BICRA or BICRAL (mutually exclusive), BRD9, SS18, the core BAF subunits, SMARCA2/BRM, SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, SMARCC1/BAF155, and SMARCD1/BAF60A (PubMed:29374058). {ECO:0000250|UniProtKB:Q15532, ECO:0000269|PubMed:29374058}. +Q8C3L1 SSUH2_MOUSE Protein SSUH2 homolog (Protein ssu-2 homolog) 340 38,544 Chain (1); Mutagenesis (1); Sequence conflict (2) FUNCTION: Plays a role in odontogenesis. {ECO:0000269|PubMed:27680507}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y2M2}. Nucleus {ECO:0000250|UniProtKB:Q9Y2M2}. TISSUE SPECIFICITY: Widely expressed, with highest levels in the liver, intestine, tongue and underjaw. {ECO:0000269|PubMed:27680507}. +Q80VR3 ST1C1_MOUSE Sulfotransferase 1C1 (ST1C1) (EC 2.8.2.-) (Phenol sulfotransferase) 304 35,797 Active site (1); Binding site (3); Chain (1); Nucleotide binding (3); Region (1); Sequence conflict (1) FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of drugs, xenobiotic compounds, hormones, and neurotransmitters. May be involved in the activation of carcinogenic hydroxylamines. Shows activity towards p-nitrophenol and N-hydroxy-2-acetylamino-fluorene (N-OH-2AAF). Also shows activity towards cinnamyl alcohol at pH 6.4 but not at pH 5.5, and towards a number of phenolic odorants including eugenol, guaiacol and 2-naphthol. {ECO:0000269|PubMed:9560327}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8641270}. TISSUE SPECIFICITY: Expressed only in olfactory tissue. Detected in sustentacular cells in the dorso-medial portion of the nasal cavity. {ECO:0000269|PubMed:8641270, ECO:0000269|PubMed:9560327}. +Q8BG48 ST17B_MOUSE Serine/threonine-protein kinase 17B (EC 2.7.11.1) (DAP kinase-related apoptosis-inducing protein kinase 2) 372 41,983 Active site (1); Binding site (1); Chain (1); Domain (1); Nucleotide binding (1); Sequence conflict (1) FUNCTION: Acts as a positive regulator of apoptosis. Phosphorylates myosin light chains (By similarity). {ECO:0000250}. PTM: Autophosphorylated. {ECO:0000250|UniProtKB:Q9UEE5}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cell membrane {ECO:0000250}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250}. Note=Colocalizes with STK17B at the plasma membrane. {ECO:0000250}. SUBUNIT: Interacts with CHP1; the interaction induces CHP1 to translocate from the Golgi to the nucleus. {ECO:0000250}. +P52840 ST1A1_MOUSE Sulfotransferase 1A1 (ST1A1) (EC 2.8.2.1) (Aryl sulfotransferase) (Phenol sulfotransferase) (Phenol/aryl sulfotransferase) (mSTp1) (ST1A4) (Sulfokinase) 291 33,974 Active site (1); Binding site (3); Chain (1); Modified residue (1); Nucleotide binding (3); Region (1) FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of catecholamines, phenolic drugs and neurotransmitters. Has also estrogen sulfotransferase activity. responsible for the sulfonation and activation of minoxidil. Is Mediates the metabolic activation of carcinogenic N-hydroxyarylamines to DNA binding products and could so participate as modulating factor of cancer risk (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +Q9JMD3 STA10_MOUSE START domain-containing protein 10 (StARD10) (PCTP-like protein) (PCTP-L) (Serologically defined colon cancer antigen 28 homolog) (StAR-related lipid transfer protein 10) 291 32,951 Chain (1); Domain (1); Modified residue (8) FUNCTION: Phospholipid transfer protein that preferentially selects lipid species containing a palmitoyl or stearoyl chain on the sn-1 and an unsaturated fatty acyl chain (18:1 or 18:2) on the sn-2 position. Able to transfer phosphatidylcholine (PC) and phosphatidyetanolamline (PE) between membranes (By similarity). May play metabolic roles in sperm maturation or fertilization. {ECO:0000250, ECO:0000269|PubMed:10819773}. PTM: Phosphorylation at Ser-284 by CK2 negatively regulates lipid transfer activity, possibly by decreasing membrane association. {ECO:0000250}. SUBCELLULAR LOCATION: Cell projection, cilium, flagellum {ECO:0000269|PubMed:10819773}. Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}. Note=Mainly cytosolic (By similarity). In testis was predominantly detected at the flagella of elongated spermatids, with a strong signal also found at the tail of epididymal sperm. {ECO:0000250}. TISSUE SPECIFICITY: Testis, kidney, liver, and intestine with the highest level in the testis. +Q7TSE6 ST38L_MOUSE Serine/threonine-protein kinase 38-like (EC 2.7.11.1) (NDR2 protein kinase) (Nuclear Dbf2-related kinase 2) 464 53,772 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Domain (2); Initiator methionine (1); Modified residue (4); Nucleotide binding (1); Region (1); Sequence conflict (1) FUNCTION: Involved in the regulation of structural processes in differentiating and mature neuronal cells. {ECO:0000269|PubMed:15308672, ECO:0000269|PubMed:21730291}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15308672}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15308672}. Membrane {ECO:0000269|PubMed:15308672}. Note=Associated with the actin cytoskeleton. Co-localizes with STK24/MST3 in the membrane. SUBUNIT: Homodimeric S100B binds two molecules of STK38L. Interacts with MOB1 and MOB2 (By similarity). Interacts with MICAL1; leading to inhibit the protein kinase activity by antagonizing activation by MST1/STK4. {ECO:0000250, ECO:0000269|PubMed:21730291}. TISSUE SPECIFICITY: Highly expressed in the large and small intestine, stomach and testis. High levels also present in the brain, in particular the neurocortex, basal forebrain, hippocampus, the amygdala, cerebellum and brainstem. {ECO:0000269|PubMed:15037617, ECO:0000269|PubMed:15308672}. +Q8R4Y4 STAB1_MOUSE Stabilin-1 (Fasciclin, EGF-like, laminin-type EGF-like and link domain-containing scavenger receptor 1) (FEEL-1) 2571 276,257 Alternative sequence (2); Chain (1); Disulfide bond (60); Domain (26); Glycosylation (31); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 2476 2496 Helical. {ECO:0000255}. TOPO_DOM 26 2475 Extracellular. {ECO:0000255}.; TOPO_DOM 2497 2571 Cytoplasmic. {ECO:0000255}. FUNCTION: Acts as a scavenger receptor for acetylated low density lipoprotein. Binds to both Gram-positive and Gram-negative bacteria and may play a role in defense against bacterial infection. When inhibited in endothelial tube formation assays, there is a marked decrease in cell-cell interactions, suggesting a role in angiogenesis. Involved in the delivery of newly synthesized CHID1/SI-CLP from the biosynthetic compartment to the endosomal/lysosomal system (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Interacts with CHID1. {ECO:0000250}. +Q8R4U0 STAB2_MOUSE Stabilin-2 (Fasciclin, EGF-like, laminin-type EGF-like and link domain-containing scavenger receptor 2) (FEEL-2) [Cleaved into: Short form stabilin-2] 2559 277,532 Chain (2); Disulfide bond (65); Domain (27); Glycosylation (29); Modified residue (1); Region (1); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 2465 2485 Helical. {ECO:0000255}. TOPO_DOM 29 2464 Extracellular. {ECO:0000255}.; TOPO_DOM 2486 2559 Cytoplasmic. {ECO:0000255}. FUNCTION: Phosphatidylserine receptor that enhances the engulfment of apoptotic cells. Hyaluronan receptor that binds to and mediates endocytosis of hyaluronic acid (HA). Acts also, in different species, as a primary systemic scavenger receptor for heparin (Hep), chondroitin sulfate (CS), dermatan sulfate (DS), nonglycosaminoglycan (GAG), acetylated low-density lipoprotein (AcLDL), pro-collagen propeptides and advanced glycation end products (AGE). May serve to maintain tissue integrity by supporting extracellular matrix turnover or it may contribute to maintaining fluidity of bodily liquids by resorption of hyaluronan. Counter receptor which plays an important role in lymphocyte recruitment in the hepatic vasculature. Binds to both Gram-positive and Gram-negative bacteria and may play a role in defense against bacterial infection. The proteolytically processed short form also functions as an endocytosis receptor for heparin internalisation as well as HA and CS. {ECO:0000269|PubMed:15572036, ECO:0000269|PubMed:18230608}. PTM: Glycosylated. {ECO:0000250}.; PTM: Proteolytically processed to yield a smaller protein. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8WWQ8}. Cell membrane {ECO:0000269|PubMed:15572036}; Single-pass type I membrane protein {ECO:0000269|PubMed:15572036}. SUBUNIT: Interacts with heparin, alpha-M/beta-2 integrin (ITGAM and ITGB2), and thymosin beta 4 (TMSB4X) (By similarity). Interacts with GULP1. Associates with clathrin and adapter protein AP-2; in liver sinusoidal endothelial cells (LSECs). {ECO:0000250, ECO:0000269|PubMed:15572036, ECO:0000269|PubMed:18230608}. DOMAIN: Recognizes phosphatidyl serine via its epidermal growth factor-like domains. TISSUE SPECIFICITY: Expressed in endothelial sinuses of liver, lymph nodes, bone marrow, spleen and in specialised structures of eye, heart, brain and kidney. Expression is detected in corneal and lens epithelium, in mesenchymal cells of the heart valves, in the ependymal cells lining the ventricles in the brain, and in the prismatic epithelial cells covering the renal papillae. {ECO:0000269|PubMed:12473645, ECO:0000269|PubMed:14598175}. +O70576 STAG3_MOUSE Cohesin subunit SA-3 (SCC3 homolog 3) (Stromal antigen 3) (Stromalin-3) 1240 141,167 Chain (1); Compositional bias (1); Domain (1); Modified residue (1); Sequence conflict (4) FUNCTION: Meiosis specific component of cohesin complex. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The meiosis-specific cohesin complex probably replaces mitosis specific cohesin complex when it dissociates from chromatin during prophase I. {ECO:0000269|PubMed:11483963, ECO:0000269|PubMed:24597867}. PTM: Phosphorylated. {ECO:0000269|PubMed:22346761}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00750, ECO:0000269|PubMed:22346761}. Chromosome {ECO:0000269|PubMed:22346761}. Chromosome, centromere {ECO:0000269|PubMed:22346761}. Note=Associates with chromatin. In prophase I stage of meiosis, it is found along the axial elements of synaptonemal complexes. In late-pachytene-diplotene, the bulk of protein dissociates from the chromosome arms probably because of phosphorylation by PLK1, except at centromeres, where cohesin complexes remain. It however remains chromatin associated at the centromeres up to metaphase I. During anaphase I, it probably dissociates from centromeres, allowing chromosomes segregation. SUBUNIT: Component of the meiosis-specific cohesin complex, which also contains the SMC1 (SMC1A or SMC1B) and SMC3 heterodimer. Such complex likely contains RAD21, or the meiosis-specific related protein REC8 (By similarity). Interacts with CCDC79/TERB1; recruiting cohesin to telomeres to develop structural rigidity. {ECO:0000250, ECO:0000269|PubMed:11483963, ECO:0000269|PubMed:24413433}. TISSUE SPECIFICITY: Testis specific. +Q8BLA8 TRPA1_MOUSE Transient receptor potential cation channel subfamily A member 1 (Ankyrin-like with transmembrane domains protein 1) 1125 128,467 Chain (1); Coiled coil (1); Disulfide bond (4); Glycosylation (2); Intramembrane (1); Region (1); Repeat (14); Topological domain (8); Transmembrane (6) INTRAMEM 905 925 Pore-forming. {ECO:0000250|UniProtKB:O75762}. TRANSMEM 722 742 Helical; Name=1. {ECO:0000250|UniProtKB:O75762}.; TRANSMEM 768 788 Helical; Name=2. {ECO:0000250|UniProtKB:O75762}.; TRANSMEM 807 827 Helical; Name=3. {ECO:0000250|UniProtKB:O75762}.; TRANSMEM 833 853 Helical; Name=4. {ECO:0000250|UniProtKB:O75762}.; TRANSMEM 877 897 Helical; Name=5. {ECO:0000250|UniProtKB:O75762, ECO:0000255}.; TRANSMEM 938 959 Helical; Name=6. {ECO:0000250|UniProtKB:O75762}. TOPO_DOM 1 721 Cytoplasmic. {ECO:0000250|UniProtKB:O75762}.; TOPO_DOM 743 767 Extracellular. {ECO:0000250|UniProtKB:O75762}.; TOPO_DOM 789 806 Cytoplasmic. {ECO:0000250|UniProtKB:O75762}.; TOPO_DOM 828 832 Extracellular. {ECO:0000250|UniProtKB:O75762}.; TOPO_DOM 854 876 Cytoplasmic. {ECO:0000250|UniProtKB:O75762}.; TOPO_DOM 898 904 Extracellular. {ECO:0000250|UniProtKB:O75762}.; TOPO_DOM 926 937 Extracellular. {ECO:0000250|UniProtKB:O75762}.; TOPO_DOM 960 1125 Cytoplasmic. {ECO:0000250|UniProtKB:O75762}. FUNCTION: Receptor-activated non-selective cation channel involved in detection of pain and possibly also in cold perception and inner ear function. Has a central role in the pain response to endogenous inflammatory mediators and to a diverse array of volatile irritants, such as mustard oil, cinnamaldehyde, garlic and acrolein, an irritant from tears gas and vehicule exhaust fumes. Acts also as a ionotropic cannabinoid receptor by being activated by delta(9)-tetrahydrocannabinol (THC), the psychoactive component of marijuana. Is also activated by menthol (in vitro) (By similarity). May be a component for the mechanosensitive transduction channel of hair cells in inner ear, thereby participating in the perception of sounds. Probably operated by a phosphatidylinositol second messenger system. {ECO:0000250|UniProtKB:O75762, ECO:0000269|PubMed:12654248, ECO:0000269|PubMed:15046718, ECO:0000269|PubMed:15483558, ECO:0000269|PubMed:15843607, ECO:0000269|PubMed:16564016}. PTM: TRPA1 activation by electrophiles occurs though covalent modification of specific cysteine residues in the N-terminal cytoplasmic domain. {ECO:0000269|PubMed:22207754}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12654248, ECO:0000269|PubMed:15046718, ECO:0000269|PubMed:15483558, ECO:0000269|PubMed:15843607}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Homotetramer (PubMed:21908607). Interacts with TMEM100 (PubMed:25640077). {ECO:0000269|PubMed:21908607, ECO:0000269|PubMed:25640077}. DOMAIN: C-terminal helices from the four subunits associate to form atypical coiled coil structure; this region is probably involved in binding the inositol polyphosphates that are required for optimal channel activity (in vitro). {ECO:0000250|UniProtKB:O75762}.; DOMAIN: The ANK repeat domain consists of a convex stem structure followed by a crescent-shaped structure that surrounds the protein core. {ECO:0000250|UniProtKB:O75762}. TISSUE SPECIFICITY: Expressed in inner ear (at protein level). Specifically expressed in a subset of nociceptive neurons. Expressed in the same neurons that TRPV1. In contrast, it is not expressed in neurons expressing TRPM8. Expressed in the superior cervical ganglion. {ECO:0000269|PubMed:12654248, ECO:0000269|PubMed:15194861, ECO:0000269|PubMed:15483558, ECO:0000269|PubMed:15843607}. +Q8BZ71 STAC3_MOUSE SH3 and cysteine-rich domain-containing protein 3 360 41,000 Chain (1); Compositional bias (1); Domain (2); Mutagenesis (3); Zinc finger (1) FUNCTION: Required for normal excitation-contraction coupling in skeletal muscle and for normal muscle contraction in response to membrane depolarization (PubMed:23818578, PubMed:27621462, PubMed:29467163). Required for normal Ca(2+) release from the sarcplasmic reticulum, which ultimately leads to muscle contraction (PubMed:23818578). Probably functions via its effects on muscle calcium channels. Increases CACNA1S channel activity, in addition to its role in enhancing the expression of CACNA1S at the cell membrane (PubMed:27621462). Has a redundant role in promoting the expression of the calcium channel CACNA1S at the cell membrane (PubMed:25548159, PubMed:27621462, PubMed:29467163). Slows down the inactivation rate of the calcium channel CACNA1C (PubMed:25548159, PubMed:29363593). {ECO:0000269|PubMed:23818578, ECO:0000269|PubMed:25548159, ECO:0000269|PubMed:27621462, ECO:0000269|PubMed:29363593, ECO:0000269|PubMed:29467163}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28112192, ECO:0000269|PubMed:29467163}. Cell membrane, sarcolemma {ECO:0000269|PubMed:23818578, ECO:0000269|PubMed:28112192, ECO:0000269|PubMed:29363593, ECO:0000269|PubMed:29467163, ECO:0000305|PubMed:25548159}; Peripheral membrane protein {ECO:0000269|PubMed:29363593, ECO:0000269|PubMed:29467163, ECO:0000305|PubMed:25548159}; Cytoplasmic side {ECO:0000269|PubMed:29363593, ECO:0000269|PubMed:29467163, ECO:0000305|PubMed:25548159}. Cell membrane, sarcolemma, T-tubule {ECO:0000269|PubMed:23818578, ECO:0000269|PubMed:28112192, ECO:0000269|PubMed:29363593}. Note=Co-localizes with CACNA1S and CACNA1C on T-tubules. {ECO:0000269|PubMed:23818578, ECO:0000269|PubMed:28112192, ECO:0000269|PubMed:29363593}. SUBUNIT: Interacts (via SH3 domains) with the calcium channels CACNA1S and CACNA1C (PubMed:28112192, PubMed:29467163, PubMed:29363593). Component of a calcium channel complex with CACNA1S and CACNB1 (PubMed:28112192). Component of a calcium channel complex with CACNA1C and CACNB1 (PubMed:28112192). {ECO:0000269|PubMed:28112192, ECO:0000269|PubMed:29363593, ECO:0000269|PubMed:29467163}. TISSUE SPECIFICITY: Dected in skeletal muscle, including soleus, extensor digitorum longus, tibialis anterior, quadriceps and gastronemicus. Detected in tongue. {ECO:0000269|PubMed:23626854, ECO:0000269|PubMed:23818578}. +Q9EPQ7 STAR5_MOUSE StAR-related lipid transfer protein 5 (START domain-containing protein 5) (StARD5) 213 23,922 Chain (1); Domain (1) FUNCTION: May be involved in the intracellular transport of sterols or other lipids. May bind cholesterol or other sterols. TISSUE SPECIFICITY: Expressed in most tissues, with highest levels in liver and in kidney. +P59096 STAR6_MOUSE StAR-related lipid transfer protein 6 (START domain-containing protein 6) (StARD6) 233 26,223 Chain (1); Domain (1) FUNCTION: May be involved in the intracellular transport of sterols or other lipids. May bind cholesterol or other sterols (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Testis. +Q9WVL2 STAT2_MOUSE Signal transducer and activator of transcription 2 923 105,417 Chain (1); Domain (1); Erroneous gene model prediction (2); Modified residue (2); Sequence conflict (3) FUNCTION: Signal transducer and activator of transcription that mediates signaling by type I IFNs (IFN-alpha and IFN-beta). Following type I IFN binding to cell surface receptors, Jak kinases (TYK2 and JAK1) are activated, leading to tyrosine phosphorylation of STAT1 and STAT2. The phosphorylated STATs dimerize, associate with IRF9/ISGF3G to form a complex termed ISGF3 transcription factor, that enters the nucleus. ISGF3 binds to the IFN stimulated response element (ISRE) to activate the transcription of interferon stimulated genes, which drive the cell in an antiviral state. Acts as a regulator of mitochondrial fission by modulating the phosphorylation of DNM1L at 'Ser-616' and 'Ser-637' which activate and inactivate the GTPase activity of DNM1L respectively. {ECO:0000250|UniProtKB:P52630}. PTM: Tyrosine phosphorylated in response to IFN-alpha. {ECO:0000250}.; PTM: 'Lys-48'-linked ubiquitination by DCST1 leads to STAT2 proteasomal degradation. {ECO:0000250|UniProtKB:P52630}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P52630}. Nucleus {ECO:0000250|UniProtKB:P52630}. Note=Translocated into the nucleus upon activation by IFN-alpha/beta. {ECO:0000250|UniProtKB:P52630}. SUBUNIT: Heterodimer with STAT1 upon IFN-alpha/beta induced phosphorylation. The heterodimer STAT1:STAT2 forms the interferon-stimulated gene factor 3 complex (ISGF3) with IRF9; interacts with IRF9 in the cytoplasm (PubMed:17332413). Interacts with CRSP2 and CRSP6 (By similarity). Can form a homodimer upon IFN-alpha induced phosphorylation. Interacts with IFNAR1 and IFNAR2. Interacts with ARL2BP (PubMed:18234692). Interacts with E3 ubiquitin ligase DCST1; the interaction results in STAT2 ubiquitin-mediated proteasomal degradation (By similarity). {ECO:0000250|UniProtKB:P52630, ECO:0000269|PubMed:17332413, ECO:0000269|PubMed:18234692}. TISSUE SPECIFICITY: Found in the brain, lung, heart, spleen, liver, kidney, muscle and the testis. +Q5DQR4 STB5L_MOUSE Syntaxin-binding protein 5-like (Lethal(2) giant larvae protein homolog 4) (Tomosyn-2) 1185 131,844 Alternative sequence (6); Chain (1); Domain (1); Modified residue (10); Repeat (14) FUNCTION: May play a role in vesicle trafficking and exocytosis. {ECO:0000305}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Cell membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=Cytoplasmic, and associated with vesicular membranes and the plasma membrane. {ECO:0000305}. TISSUE SPECIFICITY: Detected in hippocampus and cerebellum. {ECO:0000269|PubMed:15659226}. +O55183 STC1_MOUSE Stanniocalcin-1 (STC-1) 247 27,480 Chain (1); Disulfide bond (6); Glycosylation (1); Propeptide (1); Signal peptide (1) FUNCTION: Stimulates renal phosphate reabsorption, and could therefore prevent hypercalcemia. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in many tissues. +Q8CJ67 STAU2_MOUSE Double-stranded RNA-binding protein Staufen homolog 2 570 62,535 Alternative sequence (7); Beta strand (3); Chain (1); Domain (4); Helix (3); Modified residue (8); Motif (2); Mutagenesis (4); Region (1) FUNCTION: RNA-binding protein required for the microtubule-dependent transport of neuronal RNA from the cell body to the dendrite. As protein synthesis occurs within the dendrite, the localization of specific mRNAs to dendrites may be a prerequisite for neurite outgrowth and plasticity at sites distant from the cell body (By similarity). {ECO:0000250|UniProtKB:Q68SB1}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15166236}. Nucleus {ECO:0000269|PubMed:15166236}. Nucleus, nucleolus {ECO:0000269|PubMed:15166236}. Endoplasmic reticulum {ECO:0000269|PubMed:15166236}. Note=Shuttles between the nucleolus, nucleus and the cytoplasm. Nuclear export of isoform 1 is independent of XPO1/CRM1 and requires the exportin XPO5. Nuclear export of isoform 2 and isoform 3 can occur by both XPO1/CRM1-dependent and XPO1/CRM1-independent pathways. May also be found in large cytoplasmic ribonucleoprotein (RNP) granules which are present in the actin rich regions of myelinating processes and associated with microtubules, polysomes and the endoplasmic reticulum. Also recruited to stress granules (SGs) upon inhibition of translation or oxidative stress. These structures are thought to harbor housekeeping mRNAs when translation is aborted. SUBUNIT: Interacts with microtubules. Isoform 2 and isoform 3 may also interact with ribosomes, and this association is independent of translation (By similarity). Identified in a mRNP complex, at least composed of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1. Interacts with the exportin XPO5. This requires RNA and RAN bound to GTP. Interacts with TRIM71 (via NHL repeats) in an RNA-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q68SB1, ECO:0000250|UniProtKB:Q9NUL3, ECO:0000269|PubMed:15166236}. DOMAIN: The DRBM 3 domain appears to be the major RNA-binding determinant. This domain also mediates interaction with XPO5 and is required for XPO1/CRM1-independent nuclear export. {ECO:0000269|PubMed:12140260, ECO:0000269|PubMed:15166236}. TISSUE SPECIFICITY: Expressed in brain and neurons, where isoform 2 and isoform 3 appear to be the most abundant. Expressed at the neuromuscular junction of the extensor digitorum longus, tibialis anterior and soleus muscles. Expression at neuromuscular junctions is most pronounced in slow-twitch muscle. Also weakly expressed in heart, kidney, ovary and testis. {ECO:0000269|PubMed:12140260, ECO:0000269|PubMed:12859680}. +P83093 STIM2_MOUSE Stromal interaction molecule 2 746 83,925 Calcium binding (1); Chain (1); Coiled coil (1); Compositional bias (1); Domain (2); Erroneous initiation (1); Glycosylation (1); Modified residue (10); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 219 235 Helical. {ECO:0000255}. TOPO_DOM 15 218 Extracellular. {ECO:0000255}.; TOPO_DOM 236 746 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a role in mediating store-operated Ca(2+) entry (SOCE), a Ca(2+) influx following depletion of intracellular Ca(2+) stores. Functions as a highly sensitive Ca(2+) sensor in the endoplasmic reticulum which activates both store-operated and store-independent Ca(2+)-influx. Regulates basal cytosolic and endoplasmic reticulum Ca(2+) concentrations. Upon mild variations of the endoplasmic reticulum Ca(2+) concentration, translocates from the endoplasmic reticulum to the plasma membrane where it probably activates the Ca(2+) release-activated Ca(2+) (CRAC) channels ORAI1, ORAI2 and ORAI3. May inhibit STIM1-mediated Ca(2+) influx (By similarity). {ECO:0000250}. PTM: Glycosylated. {ECO:0000250}.; PTM: Phosphorylated predominantly on Ser residues. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Dynamically translocates from a uniform endoplasmic reticulum distribution to punctual endoplasmic reticulum-plasma membrane junctions in response to decrease in endoplasmic reticulum Ca(2+) concentration. {ECO:0000250}. SUBUNIT: Oligomer with STIM1. Interacts with ORAI1 (By similarity). {ECO:0000250}. +Q3UF25 STIMA_MOUSE Store-operated calcium entry regulator STIMATE (STIM-activating enhancer encoded by TMEM110) (Transmembrane protein 110) 288 32,500 Chain (1); Motif (1); Region (1); Sequence conflict (8); Topological domain (2); Transmembrane (5) TRANSMEM 29 49 Helical. {ECO:0000255}.; TRANSMEM 69 89 Helical. {ECO:0000255}.; TRANSMEM 102 122 Helical. {ECO:0000255}.; TRANSMEM 156 176 Helical. {ECO:0000255}.; TRANSMEM 194 214 Helical. {ECO:0000255}. TOPO_DOM 1 28 Cytoplasmic. {ECO:0000250|UniProtKB:Q86TL2}.; TOPO_DOM 215 288 Cytoplasmic. {ECO:0000250|UniProtKB:Q86TL2}. FUNCTION: Acts as a regulator of store-operated Ca(2+) entry (SOCE) at junctional sites that connect the endoplasmic reticulum (ER) and plasma membrane (PM), called ER-plasma membrane (ER-PM) junction or cortical ER. SOCE is a Ca(2+) influx following depletion of intracellular Ca(2+) stores. Acts by interacting with STIM1, promoting STIM1 conformational switch. Involved in STIM1 relocalization to ER-PM junctions. Contributes to the maintenance and reorganization of store-dependent ER-PM junctions. {ECO:0000250|UniProtKB:Q86TL2}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q86TL2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q86TL2}. Note=Colocalizes with STIM1 at ER-plasma membrane (ER-PM) junctions, also called cortical endoplasmic reticulum (ER), in store-depleted calcium cells. May translocate to ER-PM junctions in a STIM1-dependent manner in store-depleted cells. {ECO:0000250|UniProtKB:Q86TL2}. SUBUNIT: Homooligomer. Interacts with STIM1. {ECO:0000250|UniProtKB:Q86TL2}. DOMAIN: The GXXXG motif may mediate oligomerization. The C-terminus is necessary for its localization at ER-plasma membrane (ER-PM) junctions as well as for the store-dependent rearrangement of ER-PM junctions. {ECO:0000250|UniProtKB:Q86TL2}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:26322679}. +Q924X7 STK33_MOUSE Serine/threonine-protein kinase 33 (EC 2.7.11.1) 491 54,459 Active site (1); Binding site (1); Chain (1); Domain (1); Modified residue (1); Nucleotide binding (1); Sequence conflict (1) FUNCTION: Serine/threonine protein kinase which phosphorylates VIME. May play a specific role in the dynamic behavior of the intermediate filament cytoskeleton by phosphorylation of VIME. {ECO:0000269|PubMed:18811945}. PTM: Autophosphorylated. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:16176263}. SUBUNIT: Interacts with VIME. {ECO:0000269|PubMed:18811945}. TISSUE SPECIFICITY: Highly expressed in testis, particularly in cells from the spermatogenic epithelia. Significant expression is detected in lung epithelia, alveolar macrophages, horizontal cells in the retina and in embryonic organs such as heart, brain and spinal cord. Also expressed in pituitary gland, kidney, pancreas, trachea and thyroid gland. {ECO:0000269|PubMed:16176263}. +Q80ZW0 STK35_MOUSE Serine/threonine-protein kinase 35 (Serine/threonine-protein kinase 35 L1) (EC 2.7.11.1) 539 59,459 Active site (1); Binding site (1); Chain (1); Compositional bias (2); Domain (1); Erroneous initiation (5); Frameshift (1); Nucleotide binding (1); Sequence conflict (8) PTM: Autophosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Nucleus, nucleolus. Cytoplasm. Note=When associated with PDLIM1, it is mostly found in cytoplasm, localized to actin stress fibers. {ECO:0000250}. SUBUNIT: Interacts with PDLIM1/CLP-36. {ECO:0000250}. +Q08535 SECR_MOUSE Secretin 133 14,914 Modified residue (2); Peptide (1); Propeptide (2); Signal peptide (1) FUNCTION: Stimulates formation of NaHCO(3)-rich pancreatic juice and secretion of NaHCO(3)-rich bile and inhibits HCl production by the stomach. SUBCELLULAR LOCATION: Secreted. +Q8VHC3 SELM_MOUSE Selenoprotein M (SelM) 145 16,378 Active site (2); Beta strand (6); Chain (1); Cross-link (1); Erroneous termination (1); Helix (5); Non-standard residue (1); Sequence conflict (1); Signal peptide (1); Turn (1) FUNCTION: May function as a thiol-disulfide oxidoreductase that participates in disulfide bond formation. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:11839807}. Endoplasmic reticulum {ECO:0000305|PubMed:11839807}. Golgi apparatus {ECO:0000305|PubMed:11839807}. Note=Localized to perinuclear structures corresponding to Golgi and endoplasmic reticulum. TISSUE SPECIFICITY: Widely expressed. Highly expressed in brain. {ECO:0000269|PubMed:11839807}. +P01831 THY1_MOUSE Thy-1 membrane glycoprotein (Thy-1 antigen) (CD antigen CD90) 162 18,080 Chain (1); Disulfide bond (2); Domain (1); Glycosylation (3); Lipidation (1); Modified residue (1); Natural variant (1); Propeptide (1); Signal peptide (1) FUNCTION: May play a role in cell-cell or cell-ligand interactions during synaptogenesis and other events in the brain. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. +Q80UJ9 SETMR_MOUSE Histone-lysine N-methyltransferase SETMAR (EC 2.1.1.43) (SET domain without mariner transposase fusion protein) 309 34,417 Binding site (2); Chain (1); Domain (3); Metal binding (16); Region (2); Sequence conflict (2) FUNCTION: Histone methyltransferase that methylates 'Lys-4' and 'Lys-36' of histone H3, 2 specific tags for epigenetic transcriptional activation. Specifically mediates dimethylation of H3 'Lys-36'. {ECO:0000250|UniProtKB:Q53H47}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q53H47}. Chromosome {ECO:0000250|UniProtKB:Q53H47}. DOMAIN: In the pre-SET domain, Cys residues bind 3 zinc ions that are arranged in a triangular cluster; some of these Cys residues contribute to the binding of two zinc ions within the cluster. {ECO:0000250|UniProtKB:Q53H47}. +Q1W617 SHRM4_MOUSE Protein Shroom4 1475 163,238 Alternative sequence (1); Chain (1); Coiled coil (1); Compositional bias (3); Domain (2); Erroneous initiation (1); Modified residue (3) FUNCTION: Probable regulator of cytoskeletal architecture that plays an important role in development. May regulate cellular and cytoskeletal architecture by modulating the spatial distribution of myosin II. {ECO:0000269|PubMed:17009331}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17009331}. Note=Shows partial colocalization with the cytoplasmic pool of F-actin. SUBUNIT: Interacts directly with F-actin. {ECO:0000269|PubMed:17009331}. TISSUE SPECIFICITY: Detected in most adult tissues examined. Expressed in brain, lung, heart, liver, kidney, muscle and ovary. Expressed throughout the brain, with high expression in the brain stem and cerebellum and weaker expression in the hypothalamus, the hippocampus and the olfactory bulb. Expressed in wide range of cell types during developpment, including vascular endothelium and the polarized epithelium of the neural tube and kidney. {ECO:0000269|PubMed:16249884, ECO:0000269|PubMed:17009331}. +Q8CG80 SHF_MOUSE SH2 domain-containing adapter protein F 238 26,893 Alternative sequence (1); Chain (1); Domain (1); Modified residue (2); Sequence conflict (1) FUNCTION: Adapter protein which may play a role in the regulation of apoptosis in response to PDGF. {ECO:0000250|UniProtKB:Q7M4L6}. PTM: May become phosphorylated upon binding to PDGFRA. {ECO:0000250|UniProtKB:Q7M4L6}. SUBUNIT: Interacts with phosphorylated 'Tyr-720' of PDGFRA via its SH2 domain. {ECO:0000250|UniProtKB:Q7M4L6}. +Q9QZS8 SH2D3_MOUSE SH2 domain-containing protein 3C (Cas/HEF1-associated signal transducer) (SH2 domain-containing Eph receptor-binding protein 1) 854 94,323 Alternative sequence (1); Chain (1); Domain (2); Modified residue (6); Mutagenesis (1) FUNCTION: Eph receptor-binding protein which may be a positive regulator of TCR signaling. Binding to BCAR1 is required to induce membrane ruffling and promote EGF-dependent cell migration. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10692442}. Membrane {ECO:0000269|PubMed:10692442}; Peripheral membrane protein {ECO:0000269|PubMed:10692442}. Note=Associated with the membrane when EGF-stimulated. Found at ruffling membranes. SUBUNIT: Interacts (via C-terminus) with BCAR1/CAS (By similarity). Interacts with PTK2B. Isoform 2 interacts with NEDD9/HEF1. {ECO:0000250, ECO:0000269|PubMed:10692442, ECO:0000269|PubMed:12486027}. DOMAIN: The C-terminal Cdc25-homology/Ras-GEF domain adopts a closed conformation rendering it incapable of carrying out canonical exchange factor function, this closed conformation is required for interaction with BCAR1. {ECO:0000250}. TISSUE SPECIFICITY: Isoform 2 is ubiquitously expressed. Isoform 1 is expressed in hematopoietic cells from spleen, lymph node and thymus. {ECO:0000269|PubMed:10542222, ECO:0000269|PubMed:10692442, ECO:0000269|PubMed:12486027}. +Q8R3V5 SHLB2_MOUSE Endophilin-B2 (SH3 domain-containing GRB2-like protein B2) 400 44,503 Alternative sequence (2); Chain (1); Coiled coil (1); Domain (2); Erroneous initiation (1); Modified residue (3); Region (1); Sequence caution (1); Sequence conflict (2) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homodimer, and heterodimer with SH3GLB1. {ECO:0000250}. +Q9D5J6 SHPK_MOUSE Sedoheptulokinase (SHK) (EC 2.7.1.14) (Carbohydrate kinase-like protein) 476 51,303 Chain (1); Mutagenesis (4) FUNCTION: Acts as a modulator of macrophage activation through control of glucose metabolism. {ECO:0000269|PubMed:18775706, ECO:0000269|PubMed:22682222}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22682222}. +Q3UEN2 SHLD2_MOUSE Shieldin complex subunit 2 (Protein FAM35A) (RINN1-REV7-interacting novel NHEJ regulator 2) 891 99,090 Chain (1); Region (2); Sequence conflict (1) FUNCTION: Component of the shieldin complex, which plays an important role in repair of DNA double-stranded breaks (DSBs). During G1 and S phase of the cell cycle, the complex functions downstream of TP53BP1 to promote non-homologous end joining (NHEJ) and suppress DNA end resection. Mediates various NHEJ-dependent processes including immunoglobulin class-switch recombination, and fusion of unprotected telomeres. {ECO:0000250|UniProtKB:Q86V20}. SUBCELLULAR LOCATION: Chromosome {ECO:0000250|UniProtKB:Q86V20}. SUBUNIT: Component of the shieldin complex, consisting of SHLD1, SHLD2, SHLD3 and MAD2L2/REV7. Within the complex, SHLD2 forms a scaffold which interacts with a SHLD3-MAD2L2 subcomplex via its N-terminus, and with SHLD1 via its C-terminus. Interacts with TP53BP1. Interacts with RIF1. {ECO:0000250|UniProtKB:Q86V20}. +Q3UH99 SHSA6_MOUSE Protein shisa-6 (Cystine-knot AMPAR modulating protein of 52 kDa) (CKAMP52) (Shisa family member 6) 525 58,426 Alternative sequence (1); Chain (1); Compositional bias (1); Glycosylation (2); Modified residue (5); Motif (1); Mutagenesis (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 181 201 Helical. {ECO:0000255}. TOPO_DOM 31 180 Extracellular. {ECO:0000255}.; TOPO_DOM 202 525 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in maintenance of high-frequency synaptic transmission at hippocampal CA3-CA1 synapses. Regulates AMPA-type glutamate receptor (AMPAR) immobilization at postsynaptic density keeping the channels in an activated state in the presence of glutamate and preventing synaptic depression (PubMed:26931375). May play a role in self-renewal and differentiation of spermatogonial stem cells by inhibiting canonical Wnt signaling pathway (PubMed:28196692). {ECO:0000269|PubMed:26931375, ECO:0000269|PubMed:28196692}. PTM: N-glycosylated. {ECO:0000269|PubMed:26931375}. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000269|PubMed:26931375}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Component of the postsynaptic hippocampal AMPA-type glutamate receptor (AMPAR) complex, at least composed of pore forming AMPAR subunits GRIA1, GRIA2 and GRIA3 and AMPAR auxiliary proteins SHISA6 and SHISA7 (PubMed:26931375, PubMed:29199957). Interacts (via PDZ-binding motif) with DLG4/PSD-95 (via PDZ domain); the interaction is direct (PubMed:26931375). {ECO:0000269|PubMed:26931375, ECO:0000269|PubMed:29199957}. DOMAIN: The PDZ-binding motif interacts with PDZ-domain of scaffolding protein DLG4. {ECO:0000269|PubMed:26931375}. TISSUE SPECIFICITY: Highly expressed in cerebellum and hippocampal neurons: CA1 stratum oriens and stratum radiatum, CA3 stratum oriens and stratum lucidum, and the dentate gyrus polymorphic layer (PubMed:26931375). Expressed in other brain structures including olfactory bulb, cortex, amigdala and midbrain (at protein level) (PubMed:26623514, PubMed:26931375). Also expressed in a subset of spermatogonial stem cells (PubMed:28196692). Also expressed in eye, heart, kidney, lung, muscle and spleen. Isoform 2: Specifically expressed in hippocampus (PubMed:26931375). {ECO:0000269|PubMed:26623514, ECO:0000269|PubMed:26931375, ECO:0000269|PubMed:28196692}. +Q9CZV2 SHLD3_MOUSE Shieldin complex subunit 3 (REV7-interacting novel NHEJ regulator 1) 255 29,675 Chain (1); Region (1); Sequence conflict (7) FUNCTION: Component of the shieldin complex, which plays an important role in repair of DNA double-stranded breaks (DSBs). During G1 and S phase of the cell cycle, the complex functions downstream of TP53BP1 to promote non-homologous end joining (NHEJ) and suppress DNA end resection. Mediates various NHEJ-dependent processes including immunoglobulin class-switch recombination, and fusion of unprotected telomeres. {ECO:0000250|UniProtKB:Q6ZNX1}. SUBCELLULAR LOCATION: Chromosome {ECO:0000250|UniProtKB:Q6ZNX1}. Note=Recruited to sites of chromosomal double-stranded breaks during G1 and S phase of the cell cycle. {ECO:0000250|UniProtKB:Q6ZNX1}. SUBUNIT: Component of the shieldin complex, consisting of SHLD1, SHLD2, SHLD3 and MAD2L2/REV7. Within the complex, SHLD2 forms a scaffold which interacts with a SHLD3-MAD2L2 subcomplex via its N-terminus, and with SHLD1 via its C-terminus. {ECO:0000250|UniProtKB:Q6ZNX1}. +Q8C3Q5 SHSA7_MOUSE Protein shisa-7 (Cystine-knot AMPAR modulating protein of 59 kDa) (CKAMP59) (Shisa family member 7) 558 58,334 Alternative sequence (1); Chain (1); Compositional bias (1); Erroneous initiation (1); Glycosylation (1); Modified residue (2); Motif (1); Mutagenesis (1); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 190 210 Helical. {ECO:0000255}. TOPO_DOM 23 189 Extracellular. {ECO:0000255}.; TOPO_DOM 211 558 Cytoplasmic. {ECO:0000255}. FUNCTION: Regulator of long-term synaptic potentiation specifically involved in the formation and retrieval of hippocampus-dependent contextual fear memory. Probably regulates induction and maintenance of long-term potentiation at Schaffer collaterals/CA3-CA1 excitatory synapses by affecting the recruitment of AMPA-type glutamate receptor (AMPAR) at postsynaptic density. {ECO:0000269|PubMed:29199957}. PTM: N-glycosylated. {ECO:0000269|PubMed:29199957}. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000269|PubMed:29199957}; Single-pass type I membrane protein {ECO:0000305|PubMed:29199957}. SUBUNIT: Component of the postsynaptic hippocampal AMPA-type glutamate receptor (AMPAR) complex, at least composed of pore forming AMPAR subunits GRIA1, GRIA2 and GRIA3 and AMPAR auxiliary proteins SHISA6 and SHISA7 (PubMed:29199957). Interacts (via PDZ-binding motif) with DLG4/PSD-95 (via PDZ domain); the interaction is direct (PubMed:29199957). {ECO:0000269|PubMed:29199957}. DOMAIN: The PDZ-binding motif interacts with PDZ-domain of scaffolding protein DLG4. {ECO:0000269|PubMed:29199957}. TISSUE SPECIFICITY: Mainly expressed in neurons (PubMed:29199957). Highly expressed in brain structures including cortex, striatum, olfactory bulb, amygdala hippocampus CA1-3 and dentate gyrus (at protein level) (PubMed:26623514, PubMed:29199957). {ECO:0000269|PubMed:26623514, ECO:0000269|PubMed:29199957}. +J3QNX5 SHSA8_MOUSE Protein shisa-8 (Cystine-knot AMPAR modulating protein of 39 kDa) (CKAMP39) (Shisa family member 8) 399 42,462 Chain (1); Glycosylation (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 137 157 Helical. {ECO:0000255}. TOPO_DOM 37 136 Extracellular. {ECO:0000305}.; TOPO_DOM 158 399 Cytoplasmic. {ECO:0000305}. FUNCTION: May regulate trafficking and current kinetics of AMPA-type glutamate receptor (AMPAR) at synapses. {ECO:0000269|PubMed:26623514}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Interacts with AMPAR subunits GRIA1 and GRIA2. {ECO:0000305|PubMed:26623514}. TISSUE SPECIFICITY: Brain-specific. Highly expressed in cerebellum and olfactory bulb. {ECO:0000269|PubMed:26623514}. +P97497 SHBG_MOUSE Sex hormone-binding globulin (SHBG) (Sex steroid-binding protein) (SBP) (Testis-specific androgen-binding protein) (ABP) 403 44,816 Chain (1); Disulfide bond (2); Domain (2); Glycosylation (3); Signal peptide (1) FUNCTION: Functions as an androgen transport protein, but may also be involved in receptor mediated processes. Each dimer binds one molecule of steroid. Specific for 5-alpha-dihydrotestosterone, testosterone, and 17-beta-estradiol. Regulates the plasma metabolic clearance rate of steroid hormones by controlling their plasma concentration (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=In testis, it is synthesized by the Sertoli cells, secreted into the lumen of the seminiferous tubule and transported to the epididymis. {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +Q0VBP7 SHSL1_MOUSE Protein shisa-like-1 198 22,482 Chain (1); Erroneous initiation (1); Glycosylation (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 97 117 Helical. {ECO:0000255}. TOPO_DOM 25 96 Extracellular. {ECO:0000255}.; TOPO_DOM 118 198 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q7TMX5 SHQ1_MOUSE Protein SHQ1 homolog 569 63,458 Alternative sequence (1); Chain (1); Domain (1); Sequence conflict (2) FUNCTION: Required for the quantitative accumulation of H/ACA ribonucleoproteins (RNPs), including telomerase, probably through the stabilization of DKC1, from the time of its synthesis until its association with NOP10, NHP2, and NAF1 at the nascent H/ACA RNA. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Note=May at least partially shuttle between cytosol and nucleoplasm. {ECO:0000250}. SUBUNIT: Directly interacts with DKC1 alone, but not in the context of the core trimer composed of DKC1, NOP10 and NHP2, nor in the presence of NAF1. Does not interact with NAF1 (By similarity). {ECO:0000250}. +Q3TQI7 TLS1_MOUSE Telomere length and silencing protein 1 homolog 289 33,544 Chain (1); Modified residue (5); Sequence conflict (1) FUNCTION: Involved in the regulation of telomeric heterochromatin assembly and control of telomere length. {ECO:0000250|UniProtKB:Q10148}. +P43345 TLX1_MOUSE T-cell leukemia homeobox protein 1 (Homeobox TLX-1) (Homeobox protein Hox-11) 332 34,644 Chain (1); DNA binding (1); Modified residue (1) FUNCTION: Controls the genesis of the spleen. Binds to the DNA sequence 5'-GGCGGTAAGTGG-3'. {ECO:0000269|PubMed:7908720}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: Expressed in various embryonic tissues, including branchial arches, some component of the nervous system and spleen. +Q61663 TLX2_MOUSE T-cell leukemia homeobox protein 2 (Enteric neuron homeobox protein) (Homeobox TLX-2) (Homeobox protein Hox-11L1) (Hox11L.1) (PMUR10F) 284 30,361 Chain (1); Compositional bias (1); DNA binding (1) FUNCTION: Transcription activator that binds DNA elements with the consensus sequence 5'-CGGTAATTGG-3'. Binds DNA via its homeobox. Required for normal cell death of enteric neurons in the gastrointestinal tract. Required for normal development of the enteric nervous system, and for proper development of normal motility of the gastrointestinal tract. {ECO:0000269|PubMed:10869550, ECO:0000269|PubMed:17560225, ECO:0000269|PubMed:19697050}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q923E4 SIR1_MOUSE NAD-dependent protein deacetylase sirtuin-1 (EC 3.5.1.-) (Regulatory protein SIR2 homolog 1) (SIR2-like protein 1) (SIR2alpha) (Sir2) (mSIR2a) [Cleaved into: SirtT1 75 kDa fragment (75SirT1)] 737 80,372 Active site (1); Alternative sequence (1); Binding site (1); Chain (2); Compositional bias (2); Domain (1); Initiator methionine (1); Metal binding (4); Modified residue (16); Motif (4); Mutagenesis (15); Nucleotide binding (4); Region (4) FUNCTION: NAD-dependent protein deacetylase that links transcriptional regulation directly to intracellular energetics and participates in the coordination of several separated cellular functions such as cell cycle, response to DNA damage, metabolism, apoptosis and autophagy (PubMed:11250901, PubMed:11672522, PubMed:12651913, PubMed:12887892, PubMed:12960381, PubMed:15175761, PubMed:15220471, PubMed:15632193, PubMed:15744310, PubMed:15788402, PubMed:16098828, PubMed:16366736, PubMed:16790548, PubMed:16892051, PubMed:17098745, PubMed:17347648, PubMed:17620057, PubMed:17901049, PubMed:17936707, PubMed:18004385, PubMed:18296641, PubMed:18371449, PubMed:18477450, PubMed:18662546, PubMed:18662547, PubMed:18687677, PubMed:19299583, PubMed:19356714, PubMed:20817729, PubMed:21176092, PubMed:21187328, PubMed:21189328, PubMed:21622680, PubMed:23160044, PubMed:20167603, PubMed:28883095). Can modulate chromatin function through deacetylation of histones and can promote alterations in the methylation of histones and DNA, leading to transcriptional repression (By similarity). Deacetylates a broad range of transcription factors and coregulators, thereby regulating target gene expression positively and negatively (By similarity). Serves as a sensor of the cytosolic ratio of NAD(+)/NADH which is altered by glucose deprivation and metabolic changes associated with caloric restriction (By similarity). Is essential in skeletal muscle cell differentiation and in response to low nutrients mediates the inhibitory effect on skeletal myoblast differentiation which also involves 5'-AMP-activated protein kinase (AMPK) and nicotinamide phosphoribosyltransferase (NAMPT) (PubMed:12887892, PubMed:18477450). Component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes (By similarity). The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus (PubMed:18004385). Deacetylates 'Lys-266' of SUV39H1, leading to its activation (By similarity). Inhibits skeletal muscle differentiation by deacetylating PCAF and MYOD1 (PubMed:12887892). Deacetylates H2A and 'Lys-26' of HIST1H1E (By similarity). Deacetylates 'Lys-16' of histone H4 (in vitro) (By similarity). Involved in NR0B2/SHP corepression function through chromatin remodeling: Recruited to LRH1 target gene promoters by NR0B2/SHP thereby stimulating histone H3 and H4 deacetylation leading to transcriptional repression (By similarity). Proposed to contribute to genomic integrity via positive regulation of telomere length; however, reports on localization to pericentromeric heterochromatin are conflicting (PubMed:21187328). Proposed to play a role in constitutive heterochromatin (CH) formation and/or maintenance through regulation of the available pool of nuclear SUV39H1 (By similarity). Upon oxidative/metabolic stress decreases SUV39H1 degradation by inhibiting SUV39H1 polyubiquitination by MDM2 (By similarity). This increase in SUV39H1 levels enhances SUV39H1 turnover in CH, which in turn seems to accelerate renewal of the heterochromatin which correlates with greater genomic integrity during stress response (By similarity). Deacetylates 'Lys-382' of p53/TP53 and impairs its ability to induce transcription-dependent proapoptotic program and modulate cell senescence (PubMed:11672522, PubMed:12960381). Deacetylates TAF1B and thereby represses rDNA transcription by the RNA polymerase I (PubMed:11250901). Deacetylates MYC, promotes the association of MYC with MAX and decreases MYC stability leading to compromised transformational capability (By similarity). Deacetylates FOXO3 in response to oxidative stress thereby increasing its ability to induce cell cycle arrest and resistance to oxidative stress but inhibiting FOXO3-mediated induction of apoptosis transcriptional activity; also leading to FOXO3 ubiquitination and protesomal degradation (By similarity). Appears to have a similar effect on MLLT7/FOXO4 in regulation of transcriptional activity and apoptosis (By similarity). Deacetylates DNMT1; thereby impairs DNMT1 methyltransferase-independent transcription repressor activity, modulates DNMT1 cell cycle regulatory function and DNMT1-mediated gene silencing (By similarity). Deacetylates RELA/NF-kappa-B p65 thereby inhibiting its transactivating potential and augments apoptosis in response to TNF-alpha (By similarity). Deacetylates HIF1A, KAT5/TIP60, RB1 and HIC1 (PubMed:17620057). Deacetylates FOXO1, which increases its DNA binding ability and enhances its transcriptional activity leading to increased gluconeogenesis in liver (PubMed:15220471, PubMed:15788402). Inhibits E2F1 transcriptional activity and apoptotic function, possibly by deacetylation (PubMed:16892051). Involved in HES1- and HEY2-mediated transcriptional repression (By similarity). In cooperation with MYCN seems to be involved in transcriptional repression of DUSP6/MAPK3 leading to MYCN stabilization by phosphorylation at 'Ser-62' (By similarity). Deacetylates MEF2D (By similarity). Required for antagonist-mediated transcription suppression of AR-dependent genes which may be linked to local deacetylation of histone H3 (By similarity). Represses HNF1A-mediated transcription (PubMed:21176092). Required for the repression of ESRRG by CREBZF (By similarity). Deacetylates NR1H3 and NR1H2 and deacetylation of NR1H3 at 'Lys-434' positively regulates transcription of NR1H3:RXR target genes, promotes NR1H3 proteosomal degradation and results in cholesterol efflux; a promoter clearing mechanism after reach round of transcription is proposed (PubMed:17936707). Involved in lipid metabolism (By similarity). Implicated in regulation of adipogenesis and fat mobilization in white adipocytes by repression of PPARG which probably involves association with NCOR1 and SMRT/NCOR2 (PubMed:15175761). Deacetylates p300/EP300 and PRMT1 (PubMed:15632193, PubMed:28883095). Deacetylates ACSS2 leading to its activation, and HMGCS1 deacetylation (PubMed:16790548). Involved in liver and muscle metabolism (By similarity). Through deacteylation and activation of PPARGC1A is required to activate fatty acid oxidation in skeletel muscle under low-glucose conditions and is involved in glucose homeostasis (PubMed:15744310, PubMed:17347648). Involved in regulation of PPARA and fatty acid beta-oxidation in liver (PubMed:19356714). Involved in positive regulation of insulin secretion in pancreatic beta cells in response to glucose; the function seems to imply transcriptional repression of UCP2 (PubMed:16098828, PubMed:16366736, PubMed:17901049). Proposed to deacetylate IRS2 thereby facilitating its insulin-induced tyrosine phosphorylation (PubMed:17901049). Deacetylates SREBF1 isoform SREBP-1C thereby decreasing its stability and transactivation in lipogenic gene expression (By similarity). Involved in DNA damage response by repressing genes which are involved in DNA repair, such as XPC and TP73, deacetylating XRCC6/Ku70, and faciliting recruitment of additional factors to sites of damaged DNA, such as SIRT1-deacetylated NBN can recruit ATM to initiate DNA repair and SIRT1-deacetylated XPA interacts with RPA2 (By similarity). Also involved in DNA repair of DNA double-strand breaks by homologous recombination and specifically single-strand annealing independently of XRCC6/Ku70 and NBN. Transcriptional suppression of XPC probably involves an E2F4:RBL2 suppressor complex and protein kinase B (AKT) signaling (By similarity). Transcriptional suppression of TP73 probably involves E2F4 and PCAF (By similarity). Deacetylates WRN thereby regulating its helicase and exonuclease activities and regulates WRN nuclear translocation in response to DNA damage (By similarity). Deacetylates APEX1 at 'Lys-6' and 'Lys-7' and stimulates cellular AP endonuclease activity by promoting the association of APEX1 to XRCC1 (By similarity). Increases p53/TP53-mediated transcription-independent apoptosis by blocking nuclear translocation of cytoplasmic p53/TP53 and probably redirecting it to mitochondria (By similarity). Deacetylates XRCC6/Ku70 at 'Lys-537' and 'Lys-540' causing it to sequester BAX away from mitochondria thereby inhibiting stress-induced apoptosis (By similarity). Is involved in autophagy, presumably by deacetylating ATG5, ATG7 and MAP1LC3B/ATG8 (PubMed:18296641, PubMed:21189328). Deacetylates AKT1 which leads to enhanced binding of AKT1 and PDK1 to PIP3 and promotes their activation (By similarity). Proposed to play role in regulation of STK11/LBK1-dependent AMPK signaling pathways implicated in cellular senescence which seems to involve the regulation of the acetylation status of STK11/LBK1 (PubMed:18687677). Can deacetylate STK11/LBK1 and thereby increase its activity, cytoplasmic localization and association with STRAD; however, the relevance of such activity in normal cells is unclear (By similarity). In endothelial cells is shown to inhibit STK11/LBK1 activity and to promote its degradation (By similarity). Deacetylates SMAD7 at 'Lys-64' and 'Lys-70' thereby promoting its degradation (PubMed:17098745). Deacetylates CIITA and augments its MHC class II transactivation and contributes to its stability (By similarity). Deacetylates MECOM/EVI1 (By similarity). Deacetylates PML at 'Lys-487' and this deacetylation promotes PML control of PER2 nuclear localization (By similarity). During the neurogenic transition, repress selective NOTCH1-target genes through histone deacetylation in a BCL6-dependent manner and leading to neuronal differentiation (By similarity). Regulates the circadian expression of several core clock genes, including ARNTL/BMAL1, RORC, PER2 and CRY1 and plays a critical role in maintaining a controlled rhythmicity in histone acetylation, thereby contributing to circadian chromatin remodeling (PubMed:18662546, PubMed:18662547, PubMed:19299583). Deacetylates ARNTL/BMAL1 and histones at the circadian gene promoters in order to facilitate repression by inhibitory components of the circadian oscillator (PubMed:18662546, PubMed:18662547, PubMed:19299583). Deacetylates PER2, facilitating its ubiquitination and degradation by the proteosome (PubMed:18662546). Protects cardiomyocytes against palmitate-induced apoptosis (PubMed:21622680). Deacetylates XBP1 isoform 2; deacetylation decreases protein stability of XBP1 isoform 2 and inhibits its transcriptional activity (By similarity). Deacetylates PCK1 and directs its activity toward phosphoenolpyruvate production promoting gluconeogenesis (PubMed:30193097). Involved in the CCAR2-mediated regulation of PCK1 and NR1D1 (By similarity). Deacetylates CTNB1 at 'Lys-49' (By similarity). In POMC (pro-opiomelanocortin) neurons, required for leptin-induced activation of PI3K signaling (PubMed:20620997). {ECO:0000250|UniProtKB:Q96EB6, ECO:0000269|PubMed:11250901, ECO:0000269|PubMed:11672522, ECO:0000269|PubMed:12651913, ECO:0000269|PubMed:12887892, ECO:0000269|PubMed:12960381, ECO:0000269|PubMed:15175761, ECO:0000269|PubMed:15220471, ECO:0000269|PubMed:15632193, ECO:0000269|PubMed:15744310, ECO:0000269|PubMed:15788402, ECO:0000269|PubMed:16098828, ECO:0000269|PubMed:16366736, ECO:0000269|PubMed:16790548, ECO:0000269|PubMed:16892051, ECO:0000269|PubMed:17098745, ECO:0000269|PubMed:17347648, ECO:0000269|PubMed:17620057, ECO:0000269|PubMed:17901049, ECO:0000269|PubMed:17936707, ECO:0000269|PubMed:18004385, ECO:0000269|PubMed:18296641, ECO:0000269|PubMed:18371449, ECO:0000269|PubMed:18477450, ECO:0000269|PubMed:18662546, ECO:0000269|PubMed:18662547, ECO:0000269|PubMed:18687677, ECO:0000269|PubMed:19299583, ECO:0000269|PubMed:19356714, ECO:0000269|PubMed:20167603, ECO:0000269|PubMed:20620997, ECO:0000269|PubMed:20817729, ECO:0000269|PubMed:21176092, ECO:0000269|PubMed:21187328, ECO:0000269|PubMed:21189328, ECO:0000269|PubMed:21622680, ECO:0000269|PubMed:23160044, ECO:0000269|PubMed:28883095, ECO:0000269|PubMed:30193097}.; FUNCTION: Isoform 2: Deacetylates 'Lys-382' of p53/TP53, however with lower activity than isoform 1. In combination, the two isoforms exert an additive effect. Isoform 2 regulates p53/TP53 expression and cellular stress response and is in turn repressed by p53/TP53 presenting a SIRT1 isoform-dependent auto-regulatory loop. {ECO:0000250|UniProtKB:Q96EB6}.; FUNCTION: SirtT1 75 kDa fragment: Catalytically inactive 75SirT1 may be involved in regulation of apoptosis. May be involved in protecting chondrocytes from apoptotic death by associating with cytochrome C and interfering with apoptosome assembly. {ECO:0000250|UniProtKB:Q96EB6}. PTM: Phosphorylated. Phosphorylated by STK4/MST1, resulting in inhibition of SIRT1-mediated p53/TP53 deacetylation. Phosphorylation by MAPK8/JNK1 at Ser-46 and Thr-522 leads to increased nuclear localization and enzymatic activity. Phosphorylation at Thr-522 by DYRK1A and DYRK3 activates deacetylase activity and promotes cell survival (PubMed:20167603). Phosphorylation by mammalian target of rapamycin complex 1 (mTORC1) at Ser-46 inhibits deacetylation activity. Phosphorylated by CaMK2, leading to increased p53/TP53 and NF-kappa-B p65/RELA deacetylation activity (By similarity). {ECO:0000250, ECO:0000269|PubMed:20167603}.; PTM: Proteolytically cleaved by cathepsin B upon TNF-alpha treatment to yield catalytic inactive but stable SirtT1 75 kDa fragment (75SirT1). {ECO:0000250|UniProtKB:Q96EB6}.; PTM: S-nitrosylated by GAPDH, leading to inhibit the NAD-dependent protein deacetylase activity. {ECO:0000269|PubMed:20972425}. SUBCELLULAR LOCATION: Nucleus, PML body {ECO:0000250|UniProtKB:Q96EB6}. Cytoplasm {ECO:0000269|PubMed:17197703, ECO:0000269|PubMed:17901049}. Nucleus {ECO:0000269|PubMed:17197703, ECO:0000269|PubMed:17901049, ECO:0000269|PubMed:18004385, ECO:0000269|PubMed:18662546, ECO:0000269|PubMed:20955178}. Note=Colocalizes in the nucleus with XBP1 isoform 2. Recruited to the nuclear bodies via its interaction with PML. Colocalized with APEX1 in the nucleus. May be found in nucleolus, nuclear euchromatin, heterochromatin and inner membrane (By similarity). Shuttles between nucleus and cytoplasm (PubMed:17197703). {ECO:0000250|UniProtKB:Q96EB6, ECO:0000269|PubMed:17197703}.; SUBCELLULAR LOCATION: SirtT1 75 kDa fragment: Cytoplasm {ECO:0000250|UniProtKB:Q96EB6}. Mitochondrion {ECO:0000250|UniProtKB:Q96EB6}. SUBUNIT: Interacts with XBP1 isoform 2 (By similarity). Found in a complex with PCAF and MYOD1 Component of the eNoSC complex, composed of SIRT1, SUV39H1 and RRP8. Interacts with HES1, HEY2 and PML. Interacts with RPS19BP1/AROS. Interacts with CCAR2 (via N-terminus); the interaction disrupts the interaction between SIRT1 and p53/TP53. Interacts with SETD7; the interaction induces the dissociation of SIRT1 from p53/TP53 and increases p53/TP53 activity. Interacts with MYCN, NR1I2, CREBZF, TSC2, TLE1, FOS, JUN, NR0B2, PPARG, NCOR, IRS1, IRS2 and NMNAT1. Interacts with HNF1A; the interaction occurs under nutrient restriction. Interacts with SUZ12; the interaction mediates the association with the PRC4 histone methylation complex which is specific as an association with PCR2 and PCR3 complex variants is not found. Interacts with FOXO1; the interaction deacetylates FOXO1, enhances its DNA-binding ability and increases its transcriptional activity. Interacts with BCL6; leads to a epigenetic repression of specific target genes. Interacts with CLOCK, ARNTL/BMAL1 and PER2. Interacts with PPARA; the interaction seems to be modulated by NAD(+) levels. Interacts with NR1H3 and this interaction is inhibited in the presence of CCAR2. Interacts with CHEK2 and p53/TP53. Exhibits a preferential interaction with sumoylated CCAR2 over its unmodified form (By similarity). Interacts with PACS2 (By similarity). {ECO:0000250|UniProtKB:Q96EB6, ECO:0000269|PubMed:11672522, ECO:0000269|PubMed:12887892, ECO:0000269|PubMed:15175761, ECO:0000269|PubMed:15220471, ECO:0000269|PubMed:16269335, ECO:0000269|PubMed:16892051, ECO:0000269|PubMed:17901049, ECO:0000269|PubMed:18662546, ECO:0000269|PubMed:18662547, ECO:0000269|PubMed:19299583, ECO:0000269|PubMed:19356714, ECO:0000269|PubMed:19478080, ECO:0000269|PubMed:20668652, ECO:0000269|PubMed:21176092, ECO:0000269|PubMed:22510882, ECO:0000269|PubMed:23160044}. TISSUE SPECIFICITY: Widely expressed. Weakly expressed in liver and skeletal muscle. {ECO:0000269|PubMed:12482959}. +Q3U0Y2 TM35B_MOUSE Transmembrane protein 35B (ZMYM6 neighbor protein) 150 16,223 Chain (1); Sequence conflict (1); Signal peptide (1); Transmembrane (3) TRANSMEM 62 82 Helical. {ECO:0000255}.; TRANSMEM 84 104 Helical. {ECO:0000255}.; TRANSMEM 111 131 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q3TMP8 TM38A_MOUSE Trimeric intracellular cation channel type A (TRIC-A) (TRICA) (27 kDa sarcoplasmic reticulum protein) (Mitsugumin-33A) (SPR-27) (Transmembrane protein 38A) 298 33,309 Binding site (2); Chain (1); Compositional bias (1); Sequence conflict (3); Topological domain (8); Transmembrane (7) TRANSMEM 19 39 Helical;Name=1. {ECO:0000255}.; TRANSMEM 52 72 Helical;Name=2. {ECO:0000255}.; TRANSMEM 86 106 Helical;Name=3. {ECO:0000255}.; TRANSMEM 145 165 Helical;Name=4. {ECO:0000255}.; TRANSMEM 179 199 Helical;Name=5. {ECO:0000255}.; TRANSMEM 210 230 Helical;Name=6. {ECO:0000255}.; TRANSMEM 235 255 Helical;Name=7. {ECO:0000255}. TOPO_DOM 1 18 Lumenal. {ECO:0000305}.; TOPO_DOM 40 51 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 73 85 Lumenal. {ECO:0000305}.; TOPO_DOM 107 144 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 166 178 Lumenal. {ECO:0000305}.; TOPO_DOM 200 209 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 231 234 Lumenal. {ECO:0000305}.; TOPO_DOM 256 298 Cytoplasmic. {ECO:0000305}. FUNCTION: Monovalent cation channel required for maintenance of rapid intracellular calcium release. May act as a potassium counter-ion channel that functions in synchronization with calcium release from intracellular stores. {ECO:0000269|PubMed:17611541}. SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane {ECO:0000250|UniProtKB:A5A6S6}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A5A6S6}. Nucleus membrane {ECO:0000250|UniProtKB:A5A6S6}. SUBUNIT: Homotrimer; trimerization probably requires binding to phosphatidylinositol 4,5-bisphosphate (PIP2). {ECO:0000250|UniProtKB:A5A6S6, ECO:0000250|UniProtKB:Q9NA73}. TISSUE SPECIFICITY: Expressed at high levels in heart and striated muscle. Also detected in brain, lung and kidney. {ECO:0000269|PubMed:17611541}. +Q69ZZ6 TMCC1_MOUSE Transmembrane and coiled-coil domains protein 1 649 71,642 Alternative sequence (3); Chain (1); Coiled coil (2); Erroneous initiation (2); Modified residue (3); Topological domain (2); Transmembrane (2) TRANSMEM 588 608 Helical. {ECO:0000255}.; TRANSMEM 621 641 Helical. {ECO:0000255}. TOPO_DOM 1 587 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 642 649 Cytoplasmic. {ECO:0000255}. FUNCTION: Endoplasmic reticulum membrane protein that promotes endoplasmic reticulum-associated endosome fission. Localizes to contact sites between the endoplasmic reticulum and endosomes and acts by promoting recruitment of the endoplasmic reticulum to endosome tubules for fission. Endosome membrane fission of early and late endosomes is essential to separate regions destined for lysosomal degradation from carriers to be recycled to the plasma membrane. {ECO:0000250|UniProtKB:O94876}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O94876}; Multi-pass membrane protein {ECO:0000255}. Note=Specifically localizes to contact sites between the endoplasmic reticulum and endosomes that are spatially and temporally linked to endosome fission. {ECO:0000250|UniProtKB:O94876}. SUBUNIT: May form homodimers and heterodimers with TMCC2 or TMCC3 via the coiled-coil domains. Interacts with ribosomal proteins RPL4 and RPS6. {ECO:0000250|UniProtKB:O94876}. +Q8R104 SIR3_MOUSE NAD-dependent protein deacetylase sirtuin-3 (EC 3.5.1.-) (Regulatory protein SIR2 homolog 3) (SIR2-like protein 3) (mSIR2L3) 334 36,615 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Domain (1); Metal binding (4); Modified residue (1); Nucleotide binding (4); Sequence conflict (4); Transit peptide (1) FUNCTION: NAD-dependent protein deacetylase (PubMed:23835326, PubMed:17923681, PubMed:18794531, PubMed:21172655). Activates or deactivates mitochondrial target proteins by deacetylating key lysine residues (PubMed:23835326, PubMed:17923681, PubMed:18794531, PubMed:21172655). Known targets include ACSS1, IDH, GDH, PDHA1, SOD2, LCAD, SDHA and the ATP synthase subunit ATP5PO (PubMed:16790548, PubMed:18794531, PubMed:21172655). Contributes to the regulation of the cellular energy metabolism (PubMed:23835326). Important for regulating tissue-specific ATP levels (PubMed:18794531, PubMed:24252090). In response to metabolic stress, deacetylates transcription factor FOXO3 and recruits FOXO3 and mitochondrial RNA polymerase POLRMT to mtDNA to promote mtDNA transcription (PubMed:23283301). {ECO:0000269|PubMed:16790548, ECO:0000269|PubMed:17923681, ECO:0000269|PubMed:18794531, ECO:0000269|PubMed:21172655, ECO:0000269|PubMed:21858060, ECO:0000269|PubMed:23283301, ECO:0000269|PubMed:23835326, ECO:0000269|PubMed:24252090}. SUBCELLULAR LOCATION: Isoform L: Mitochondrion matrix {ECO:0000269|PubMed:19241369, ECO:0000269|PubMed:19333382, ECO:0000269|PubMed:23283301}.; SUBCELLULAR LOCATION: Isoform S: Cytoplasm {ECO:0000269|PubMed:11056054}. SUBUNIT: Upon metabolic stress, forms a complex composed of FOXO3, SIRT3 and mitochondrial RNA polymerase POLRMT; the complex is recruited to mtDNA in a SIRT3-dependent manner (PubMed:23283301). Also forms a complex composed of FOXO3, SIRT3, TFAM and POLRMT (By similarity). Interacts with NDUFA9, ACSS1, IDH2 and GDH (By similarity). Interacts with PCCA (PubMed:23438705). {ECO:0000250|UniProtKB:Q9NTG7, ECO:0000269|PubMed:23283301, ECO:0000269|PubMed:23438705}. TISSUE SPECIFICITY: Strongly expressed in liver and kidney (PubMed:11056054). Expressed in skeletal muscles (at protein level) (PubMed:23283301, PubMed:23835326). Weakly expressed in lung (PubMed:11056054). {ECO:0000269|PubMed:11056054, ECO:0000269|PubMed:23283301, ECO:0000269|PubMed:23835326}. +Q8R310 TMCC3_MOUSE Transmembrane and coiled-coil domain protein 3 477 53,722 Alternative sequence (1); Chain (1); Coiled coil (3); Modified residue (2); Transmembrane (2) TRANSMEM 409 429 Helical. {ECO:0000255}.; TRANSMEM 450 470 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9ULS5}; Multi-pass membrane protein {ECO:0000255}. Note=Concentrates in discrete patches along peripheral endoplasmic reticulum tubules. {ECO:0000250|UniProtKB:Q9ULS5}. SUBUNIT: May form homodimers and heterodimers with TMCC2 or TMCC3 via the coiled-coil domains. Interacts with ribosomal proteins RPL4 and RPS6. {ECO:0000250|UniProtKB:Q9ULS5}. +Q9CPS8 SMAKA_MOUSE Small membrane A-kinase anchor protein (Small membrane AKAP) (smAKAP) 106 11,926 Chain (1); Initiator methionine (1); Lipidation (2); Modified residue (2); Region (1) FUNCTION: Binds to type I regulatory subunits of protein kinase A (PKA-RI) and may anchor/target them to the plasma membrane. {ECO:0000250}. PTM: May be palmitoylated at Cys-3. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. SUBUNIT: Interacts with PKA type I regulatory subunits PRKAR1A and PRKAR1B. Also binds to type II regulatory subunits, but at a tenfold lower affinity (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed, with very low levels in spleen and liver. {ECO:0000269|PubMed:23115245}. +A2A5Z6 SMUF2_MOUSE E3 ubiquitin-protein ligase SMURF2 (EC 2.3.2.26) (HECT-type E3 ubiquitin transferase SMURF2) (SMAD ubiquitination regulatory factor 2) (SMAD-specific E3 ubiquitin-protein ligase 2) 748 86,175 Active site (1); Alternative sequence (2); Chain (1); Compositional bias (1); Domain (5); Sequence conflict (1) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Interacts with SMAD1 and SMAD7 in order to trigger their ubiquitination and proteasome-dependent degradation. In addition, interaction with SMAD7 activates autocatalytic degradation, which is prevented by interaction with SCYE1. Forms a stable complex with the TGF-beta receptor-mediated phosphorylated SMAD2 and SMAD3. In this way, SMAD2 may recruit substrates, such as SNON, for ubiquitin-mediated degradation. Enhances the inhibitory activity of SMAD7 and reduces the transcriptional activity of SMAD2. Coexpression of SMURF2 with SMAD1 results in considerable decrease in steady-state level of SMAD1 protein and a smaller decrease of SMAD2 level. {ECO:0000250|UniProtKB:Q9HAU4}. PTM: Auto-ubiquitinated and ubiquitinated in the presence of RNF11 and UBE2D1. Ubiquitinated by the SCF(FBXL15) complex, leading to its degradation by the proteasome (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9HAU4}. Cytoplasm {ECO:0000250|UniProtKB:Q9HAU4}. Cell membrane {ECO:0000250|UniProtKB:Q9HAU4}. Membrane raft {ECO:0000250|UniProtKB:Q9HAU4}. Note=Cytoplasmic in the presence of SMAD7. Colocalizes with CAV1, SMAD7 and TGF-beta receptor in membrane rafts. Interacts with STAMBP and RNF11. {ECO:0000250}. SUBUNIT: Interacts (via WW domains) with SMAD1. Interacts (via WW domains) with SMAD2 (via PY-motif). Interacts (via WW domains) with SMAD3 (via PY-motif). Interacts with SMAD6. Interacts with SMAD7 (via PY-motif) and TGFBR1; SMAD7 recruits SMURF2 to the TGF-beta receptor and regulates its degradation. Does not interact with SMAD4; SMAD4 lacks a PY-motif. Interacts with AIMP1 (By similarity). Interacts with NDFIP1 and NDFIP2; this interaction activates the E3 ubiquitin-protein ligase (By similarity). {ECO:0000250|UniProtKB:Q9HAU4}. DOMAIN: The second and third WW domains are responsible for interaction with the PY-motif of R-SMAD (SMAD1, SMAD2 and SMAD3). {ECO:0000250}.; DOMAIN: The C2 domain is involved in autoinhibition of the catalytic activity by interacting with the HECT domain. {ECO:0000250}. +C0HKC8 SMK3A_MOUSE Sperm motility kinase 3A (EC 2.7.11.1) 504 56,487 Active site (1); Binding site (1); Chain (1); Domain (2); Nucleotide binding (1) FUNCTION: May play a role in sperm motility, especially in the regulation of flagellar function. {ECO:0000269|PubMed:10647005}. TISSUE SPECIFICITY: Testis-specific. Expressed in the testis from 22 days postpartum (22 dpp). {ECO:0000269|PubMed:10647005}. +P62317 SMD2_MOUSE Small nuclear ribonucleoprotein Sm D2 (Sm-D2) (snRNP core protein D2) 118 13,527 Chain (1); Cross-link (2); Initiator methionine (1); Modified residue (3); Sequence conflict (1) FUNCTION: Plays role in pre-mRNA splicing as core component of the SMN-Sm complex that mediates spliceosomal snRNP assembly and as component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Component of both the pre-catalytic spliceosome B complex and activated spliceosome C complexes. Is also a component of the minor U12 spliceosome. {ECO:0000250|UniProtKB:P62316}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P62316}. Nucleus {ECO:0000250|UniProtKB:P62316}. Note=SMN-mediated assembly into core snRNPs occurs in the cytosol before SMN-mediated transport to the nucleus to be included in spliceosomes. {ECO:0000250|UniProtKB:P62316}. SUBUNIT: Core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Most spliceosomal snRNPs contain a common set of Sm proteins, SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. Component of the U1 snRNP. The U1 snRNP is composed of the U1 snRNA and the 7 core Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG, and at least three U1 snRNP-specific proteins SNRNP70/U1-70K, SNRPA/U1-A and SNRPC/U1-C. Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39, plus LSM2, LSM3, LSM4, LSM5, LSM6, LSM7 and LSM8. Component of the U11/U12 snRNPs that are part of the U12-type spliceosome. Part of the SMN-Sm complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8, STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG; catalyzes core snRNPs assembly. Forms a 6S pICln-Sm complex composed of CLNS1A/pICln, SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG; ring-like structure where CLNS1A/pICln mimics additional Sm proteins and which is unable to assemble into the core snRNP. {ECO:0000250|UniProtKB:P62316}. +Q8VCQ6 SMS1_MOUSE Phosphatidylcholine:ceramide cholinephosphotransferase 1 (EC 2.7.8.27) (Protein Mob) (Sphingomyelin synthase 1) (Transmembrane protein 23) 419 49,317 Active site (3); Alternative sequence (3); Beta strand (1); Chain (1); Domain (1); Helix (4); Modified residue (1); Sequence conflict (2); Topological domain (1); Transmembrane (5); Turn (2) TRANSMEM 142 162 Helical. {ECO:0000255}.; TRANSMEM 190 210 Helical. {ECO:0000255}.; TRANSMEM 221 241 Helical. {ECO:0000255}.; TRANSMEM 282 302 Helical. {ECO:0000255}.; TRANSMEM 310 330 Helical. {ECO:0000255}. TOPO_DOM 331 419 Cytoplasmic. {ECO:0000255}. FUNCTION: Sphingomyelin synthases synthesize the sphingolipid, sphingomyelin, through transfer of the phosphatidyl head group, phosphatidylcholine, on to the primary hydroxyl of ceramide. The reaction is bidirectional depending on the respective levels of the sphingolipid and ceramide. Golgi apparatus SMS1 directly and specifically recognizes the choline head group on the substrate, requiring two fatty chains on the choline-P donor molecule in order to be recognized efficiently as a substrate. Major form in macrophages. Required for cell growth in certain cell types (By similarity). Suppresses BAX-mediated apoptosis and also prevents cell death in response to stimuli such as hydrogen peroxide, osmotic stress, elevated temperature and exogenously supplied sphingolipids. May protect against cell death by reversing the stress-inducible increase in levels of proapoptotic ceramide. {ECO:0000250, ECO:0000269|PubMed:16879426, ECO:0000269|PubMed:22580896}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Isoform 1 is widely expressed, isoform 2 shows a more narrow distribution and isoform 3 is detected only in testis and heart. {ECO:0000269|PubMed:16226406}. +Q3UKJ7 SMU1_MOUSE WD40 repeat-containing protein SMU1 (Smu-1 suppressor of mec-8 and unc-52 protein homolog) [Cleaved into: WD40 repeat-containing protein SMU1, N-terminally processed] 513 57,544 Alternative sequence (1); Chain (2); Cross-link (1); Domain (2); Frameshift (1); Initiator methionine (1); Modified residue (2); Region (1); Repeat (7); Sequence conflict (4) FUNCTION: Involved in pre-mRNA splicing as a component of the spliceosome (By similarity). Regulates alternative splicing of the HSPG2 pre-mRNA (By similarity). Required for normal accumulation of IK (By similarity). Required for normal mitotic spindle assembly and normal progress through mitosis (By similarity). {ECO:0000250|UniProtKB:Q2TAY7, ECO:0000250|UniProtKB:Q76B40}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q99M63}. Nucleus {ECO:0000250|UniProtKB:Q76B40}. Nucleus speckle {ECO:0000250|UniProtKB:Q76B40}. Note=Colocalizes with SRSF1 in nuclear speckles. {ECO:0000250|UniProtKB:Q76B40}. SUBUNIT: Component of the spliceosome B complex. Interacts with IK. {ECO:0000250|UniProtKB:Q2TAY7}. DOMAIN: The WD repeats assemble into a seven-bladed WD propeller. {ECO:0000250|UniProtKB:G5EEG7}. +Q70E20 SNED1_MOUSE Sushi, nidogen and EGF-like domain-containing protein 1 (Secreted protein SST-3) (Stromal nidogen extracellular matrix protein) 1403 151,581 Alternative sequence (1); Chain (1); Disulfide bond (47); Domain (20); Erroneous initiation (1); Glycosylation (3); Sequence conflict (5); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Expressed in lung. {ECO:0000269|PubMed:15162516}. +Q8C080 SNX16_MOUSE Sorting nexin-16 344 38,817 Binding site (3); Chain (1); Coiled coil (1); Domain (1); Modified residue (1); Sequence conflict (1) FUNCTION: May be involved in several stages of intracellular trafficking. Plays a role in protein transport from early to late endosomes. Plays a role in protein transport to the lysosome. Promotes degradation of EGFR after EGF signaling (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Late endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm {ECO:0000250}. Lysosome {ECO:0000250}. SUBUNIT: Homooligomer. Interacts with EGFR (By similarity). {ECO:0000250}. DOMAIN: The PX domain mediates interaction with membranes enriched in phosphatidylinositol 3-phosphate. {ECO:0000250}. +Q4VAA7 SNX33_MOUSE Sorting nexin-33 (SH3 and PX domain-containing protein 3) 574 65,315 Chain (1); Compositional bias (1); Domain (3); Modified residue (2); Sequence conflict (3) FUNCTION: Plays a role in the reorganization of the cytoskeleton, endocytosis and cellular vesicle trafficking via its interactions with membranes, WASL, DNM1 and DNM2. Acts both during interphase and at the end of mitotic cell divisions. Required for efficient progress through mitosis and cytokinesis. Required for normal formation of the cleavage furrow at the end of mitosis. Modulates endocytosis of cell-surface proteins, such as APP and PRNP; this then modulates the secretion of APP and PRNP peptides. Promotes membrane tubulation (in vitro). May promote the formation of macropinosomes (By similarity). {ECO:0000250}. PTM: Phosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Primarily detected in the cytosol. A minor proportion is membrane-bound (By similarity). {ECO:0000250}. SUBUNIT: Homodimer (via BAR domain). Interacts with ADAM15. Interacts with FASLG. Interacts (via SH3 domain) with DNM1 and DNM2. Interacts with WASL (By similarity). {ECO:0000250}. DOMAIN: The PX and BAR domains mediate association with membranes and are required for membrane tubulation. {ECO:0000250}. TISSUE SPECIFICITY: Detected in brain (at protein level). {ECO:0000269|PubMed:18353773}. +Q6PHU5 SORT_MOUSE Sortilin (Neurotensin receptor 3) (NTR3) (mNTR3) 825 91,200 Alternative sequence (1); Beta strand (52); Chain (1); Compositional bias (1); Disulfide bond (8); Glycosylation (6); Helix (9); Modified residue (3); Motif (1); Propeptide (1); Region (3); Repeat (9); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (5) TRANSMEM 755 775 Helical. {ECO:0000255}. TOPO_DOM 74 754 Extracellular. {ECO:0000255}.; TOPO_DOM 776 825 Cytoplasmic. {ECO:0000255}. FUNCTION: Functions as a sorting receptor in the Golgi compartment and as a clearance receptor on the cell surface. Required for protein transport from the Golgi apparatus to the lysosomes by a pathway that is independent of the mannose-6-phosphate receptor (M6PR). Also required for protein transport from the Golgi apparatus to the endosomes. Promotes neuronal apoptosis by mediating endocytosis of the proapoptotic precursor forms of BDNF (proBDNF) and NGFB (proNGFB). Also acts as a receptor for neurotensin. May promote mineralization of the extracellular matrix during osteogenic differentiation by scavenging extracellular LPL. Probably required in adipocytes for the formation of specialized storage vesicles containing the glucose transporter SLC2A4/GLUT4 (GLUT4 storage vesicles, or GSVs). These vesicles provide a stable pool of SLC2A4 and confer increased responsiveness to insulin. May also mediate transport from the endoplasmic reticulum to the Golgi. {ECO:0000269|PubMed:10594043, ECO:0000269|PubMed:15236332, ECO:0000269|PubMed:15236333, ECO:0000269|PubMed:15372498, ECO:0000269|PubMed:15992544, ECO:0000269|PubMed:19407813, ECO:0000269|PubMed:21102451}. PTM: The N-terminal propeptide is cleaved by furin and possibly other homologous proteases. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Endosome membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Golgi apparatus, Golgi stack membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Nucleus membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Cell membrane; Single-pass type I membrane protein; Extracellular side. Lysosome membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Localized to membranes of the endoplasmic reticulum, endosomes, Golgi stack, lysosomes and nucleus. A small fraction of the protein is also localized to the plasma membrane. Interaction with NRADD promotes localization at the cell membrane in neurons; this promotes interaction with NGFR. Also found in SLC2A4/GLUT4 storage vesicles (GSVs) in adipocytes. Localization to the plasma membrane in adipocytes is enhanced by insulin. SUBUNIT: Interacts with the cytosolic adapter proteins GGA1 and GGA2. Interacts with numerous ligands including the receptor-associated protein LRPAP1/RAP, NTS and GM2A. Forms a complex with NGFR which binds specifically to the precursor forms of NGFB (proNGFB) and BDNF (proBDNF). Interacts with the Trk receptors NTRK1, NTRK2 and NTRK3; may regulate their anterograde axonal transport and signaling (By similarity). Interacts with LPL (PubMed:10085125). Interacts with PSAP (PubMed:15236332). Interacts with SLC2A4 (PubMed:15992544). Interacts with NRADD and NGFR (PubMed:19407813). Interaction with NRADD protects against degradation in the lysosome. Interacts with CLN5 (By similarity). {ECO:0000250|UniProtKB:Q99523, ECO:0000269|PubMed:10085125, ECO:0000269|PubMed:15236332, ECO:0000269|PubMed:15992544, ECO:0000269|PubMed:19407813}. DOMAIN: The N-terminal propeptide may facilitate precursor transport within the Golgi stack. Intrachain binding of the N-terminal propeptide and the extracellular domain may also inhibit premature ligand binding (By similarity). {ECO:0000250}.; DOMAIN: The extracellular domain may be shed following protease cleavage in some cell types. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the brain, particularly the piriform cortex, the cerebral cortex and the hippocampus. {ECO:0000269|PubMed:10064893}. +Q8R3L5 SO3A1_MOUSE Solute carrier organic anion transporter family member 3A1 (MJAM) (Organic anion-transporting polypeptide D) (OATP-D) (Sodium-independent organic anion transporter D) (Solute carrier family 21 member 11) 710 76,763 Alternative sequence (2); Chain (1); Compositional bias (1); Disulfide bond (3); Domain (1); Glycosylation (7); Modified residue (1); Sequence conflict (11); Topological domain (13); Transmembrane (12) TRANSMEM 41 60 Helical; Name=1. {ECO:0000255}.; TRANSMEM 80 100 Helical; Name=2. {ECO:0000255}.; TRANSMEM 107 131 Helical; Name=3. {ECO:0000255}.; TRANSMEM 175 203 Helical; Name=4. {ECO:0000255}.; TRANSMEM 223 243 Helical; Name=5. {ECO:0000255}.; TRANSMEM 262 286 Helical; Name=6. {ECO:0000255}.; TRANSMEM 345 366 Helical; Name=7. {ECO:0000255}.; TRANSMEM 387 410 Helical; Name=8. {ECO:0000255}.; TRANSMEM 415 438 Helical; Name=9. {ECO:0000255}.; TRANSMEM 540 562 Helical; Name=10. {ECO:0000255}.; TRANSMEM 572 597 Helical; Name=11. {ECO:0000255}.; TRANSMEM 631 648 Helical; Name=12. {ECO:0000255}. TOPO_DOM 1 40 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 61 79 Extracellular. {ECO:0000255}.; TOPO_DOM 101 106 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 132 174 Extracellular. {ECO:0000255}.; TOPO_DOM 204 222 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 244 261 Extracellular. {ECO:0000255}.; TOPO_DOM 287 344 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 367 386 Extracellular. {ECO:0000255}.; TOPO_DOM 411 414 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 439 539 Extracellular. {ECO:0000255}.; TOPO_DOM 563 571 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 598 630 Extracellular. {ECO:0000255}.; TOPO_DOM 649 705 Cytoplasmic. {ECO:0000255}. FUNCTION: Mediates the Na(+)-independent transport of organic anions. Mediates transport of prostaglandins (PG) E1 and E2, thyroxine (T4), deltorphin II, BQ-123 and vasopressin. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Widely expressed. +Q9JLC4 SORC1_MOUSE VPS10 domain-containing receptor SorCS1 (mSorCS) 1167 129,631 Alternative sequence (3); Chain (1); Domain (1); Frameshift (1); Glycosylation (8); Repeat (5); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1099 1119 Helical. {ECO:0000255}. TOPO_DOM 34 1098 Lumenal. {ECO:0000255}.; TOPO_DOM 1120 1167 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. TISSUE SPECIFICITY: Isoform 1 is highly expressed in brain, and at lower levels in heart, liver and kidney. Detected in newborn brain and in adult olfactory bulb and cerebral cortex. Isoform 2 is highly expressed in liver, and at lower levels in heart, brain, kidney and testis. +Q8BGD4 SO4C1_MOUSE Solute carrier organic anion transporter family member 4C1 (Oatp-R) (Solute carrier family 21 member 20) 722 78,412 Chain (1); Compositional bias (1); Disulfide bond (3); Domain (1); Modified residue (6); Topological domain (13); Transmembrane (12) TRANSMEM 102 122 Helical; Name=1. {ECO:0000255}.; TRANSMEM 142 162 Helical; Name=2. {ECO:0000255}.; TRANSMEM 169 193 Helical; Name=3. {ECO:0000255}.; TRANSMEM 219 249 Helical; Name=4. {ECO:0000255}.; TRANSMEM 270 290 Helical; Name=5. {ECO:0000255}.; TRANSMEM 307 331 Helical; Name=6. {ECO:0000255}.; TRANSMEM 377 398 Helical; Name=7. {ECO:0000255}.; TRANSMEM 419 442 Helical; Name=8. {ECO:0000255}.; TRANSMEM 447 470 Helical; Name=9. {ECO:0000255}.; TRANSMEM 579 601 Helical; Name=10. {ECO:0000255}.; TRANSMEM 611 636 Helical; Name=11. {ECO:0000255}.; TRANSMEM 671 688 Helical; Name=12. {ECO:0000255}. TOPO_DOM 1 101 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 123 141 Extracellular. {ECO:0000255}.; TOPO_DOM 163 168 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 194 218 Extracellular. {ECO:0000255}.; TOPO_DOM 250 269 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 291 306 Extracellular. {ECO:0000255}.; TOPO_DOM 332 376 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 399 418 Extracellular. {ECO:0000255}.; TOPO_DOM 443 446 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 471 578 Extracellular. {ECO:0000255}.; TOPO_DOM 602 610 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 637 670 Extracellular. {ECO:0000255}.; TOPO_DOM 689 722 Cytoplasmic. {ECO:0000255}. FUNCTION: Organic anion transporter, capable of transporting pharmacological substances such as digoxin, ouabain, thyroxine, methotrexate and cAMP. May participate in the regulation of membrane transport of ouabain. Involved in the uptake of the dipeptidyl peptidase-4 inhibitor sitagliptin and hence may play a role in its transport into and out of renal proximal tubule cells. May be involved in the first step of the transport pathway of digoxin and various compounds into the urine in the kidney. May be involved in sperm maturation by enabling directed movement of organic anions and compounds within or between cells. This ion-transporting process is important to maintain the strict epididymal homeostasis necessary for sperm maturation. May have a role in secretory functions since seminal vesicle epithelial cells are assumed to secrete proteins involved in decapacitation by modifying surface proteins to facilitate the acquisition of the ability to fertilize the egg. {ECO:0000250|UniProtKB:Q6ZQN7, ECO:0000269|PubMed:16641146}. SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000250|UniProtKB:Q71MB6}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q71MB6}. Note=Detected at the basolateral membrane of the proximal tubule cell in the kidney. {ECO:0000250|UniProtKB:Q71MB6}. TISSUE SPECIFICITY: Strongly expressed in initial segment of epididymis and seminal vesicles. {ECO:0000269|PubMed:16641146}. +Q8R2Y9 SOSB1_MOUSE SOSS complex subunit B1 (Nucleic acid-binding protein 2) (Oligonucleotide/oligosaccharide-binding fold-containing protein 2B) (Sensor of single-strand DNA complex subunit B1) (Sensor of ssDNA subunit B1) (SOSS-B1) (Single-stranded DNA-binding protein 1) 212 22,628 Chain (1); Compositional bias (1); DNA binding (1); Modified residue (1) FUNCTION: Component of the SOSS complex, a multiprotein complex that functions downstream of the MRN complex to promote DNA repair and G2/M checkpoint. In the SOSS complex, acts as a sensor of single-stranded DNA that binds to single-stranded DNA, in particular to polypyrimidines. The SOSS complex associates with DNA lesions and influences diverse endpoints in the cellular DNA damage response including cell-cycle checkpoint activation, recombinational repair and maintenance of genomic stability. Required for efficient homologous recombination-dependent repair of double-strand breaks (DSBs) and ATM-dependent signaling pathways (By similarity). {ECO:0000250}. PTM: Phosphorylated by ATM in response to DNA damage. Phosphorylation prevents degradation by the proteasome, hence stabilization of the protein and accumulation within cells (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Localizes to nuclear foci following DNA damage. Foci formation is not cell-cycle dependent. Partial colocalization with RAD51 after ionizing radiation treatment (By similarity). {ECO:0000250}. SUBUNIT: Component of the SOSS complex, composed of SOSS-B (SOSS-B1/NABP2 or SOSS-B2/NABP1), SOSS-A/INTS3 and SOSS-C/INIP. SOSS complexes containing SOSS-B1/NABP2 are more abundant than complexes containing SOSS-B2/NABP1. Directly interacts with ATM, SOSS-A/INTS3 and RAD51. Interacts with INTS7 (By similarity). {ECO:0000250}. +P35710 SOX5_MOUSE Transcription factor SOX-5 763 84,090 Alternative sequence (3); Chain (1); Coiled coil (2); DNA binding (1); Helix (4); Modified residue (7); Sequence conflict (2) FUNCTION: Binds specifically to the DNA sequence 5'-AACAAT-3'. Activates transcription of COL2A1 and AGC1 in vitro. {ECO:0000269|PubMed:9755172}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Forms homodimers and heterodimers with SOX6. {ECO:0000269|PubMed:9755172}. TISSUE SPECIFICITY: Isoform 1 is found in the embryo and in adult testis. Isoform 2 is expressed in chondrocytes and, to a lesser extent, in brain. Isoform 3 is testis-specific. {ECO:0000269|PubMed:1396566, ECO:0000269|PubMed:9714725, ECO:0000269|PubMed:9755172}. +Q9D826 SOX_MOUSE Peroxisomal sarcosine oxidase (PSO) (EC 1.5.3.1) (EC 1.5.3.7) (L-pipecolate oxidase) (L-pipecolic acid oxidase) 390 43,847 Chain (1); Modified residue (3); Motif (1); Nucleotide binding (1); Sequence conflict (3) FUNCTION: Metabolizes sarcosine, L-pipecolic acid and L-proline. {ECO:0000250}. SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. TISSUE SPECIFICITY: Kidney and liver. +Q6PFR5 TRA2A_MOUSE Transformer-2 protein homolog alpha (TRA-2 alpha) (TRA2-alpha) (Transformer-2 protein homolog A) 281 32,316 Chain (1); Compositional bias (2); Cross-link (1); Domain (1); Initiator methionine (1); Modified residue (14); Region (1) FUNCTION: Sequence-specific RNA-binding protein which participates in the control of pre-mRNA splicing. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Binds to A3 enhancer proteins SRp75, SRp55, SRp40 and SRp30. {ECO:0000250}. +P62996 TRA2B_MOUSE Transformer-2 protein homolog beta (TRA-2 beta) (TRA2-beta) (Silica-induced gene 41 protein) (SIG-41) (Splicing factor, arginine/serine-rich 10) (Transformer-2 protein homolog B) 288 33,666 Alternative sequence (2); Chain (1); Compositional bias (2); Cross-link (1); Domain (1); Initiator methionine (1); Modified residue (20); Region (1) FUNCTION: Sequence-specific RNA-binding protein which participates in the control of pre-mRNA splicing. Can either activate or suppress exon inclusion. Acts additively with RBMX to promote exon 7 inclusion of the survival motor neuron SMN2. Activates the splicing of MAPT/Tau exon 10. Alters pre-mRNA splicing patterns by antagonizing the effects of splicing regulators, like RBMX. Binds to the AG-rich SE2 domain in the SMN exon 7 RNA. Binds to pre-mRNA (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Found in a pre-mRNA exonic splicing enhancer (ESE) complex with TRA2B/SFRS10, SNRNP70, SNRPA1 and SRRM1. Binds to A3 enhancer proteins SFRS4, SFRS5, SFRS6 and SFRS9. Interacts with CPSF6, RBMY1A1, RNPS1, SAFB/SAFB1, RBMX and phosphorylated SFRS13A (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. Highly expressed in uterus and brain. {ECO:0000269|PubMed:8674539}. +Q811W0 SOX21_MOUSE Transcription factor SOX-21 276 28,610 Chain (1); DNA binding (1); Sequence conflict (4) FUNCTION: May play a role as an activator of transcription of OPRM1. Overexpression of SOX21 can up-regulate the OPRM1 distal promoter activity in mor-expressing neuronal cells. {ECO:0000269|PubMed:12446692}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}. +Q3TXT3 SOSSC_MOUSE SOSS complex subunit C (INTS3- and NABP-interacting protein) (Sensor of single-strand DNA complex subunit C) (Sensor of ssDNA subunit C) (SOSS-C) (Single-stranded DNA-binding protein-interacting protein 1) (SSB-interacting protein 1) 104 11,411 Alternative sequence (1); Chain (1); Erroneous gene model prediction (1); Erroneous initiation (2); Initiator methionine (1); Modified residue (2) FUNCTION: Component of the SOSS complex, a multiprotein complex that functions downstream of the MRN complex to promote DNA repair and G2/M checkpoint. The SOSS complex associates with single-stranded DNA at DNA lesions and influences diverse endpoints in the cellular DNA damage response including cell-cycle checkpoint activation, recombinational repair and maintenance of genomic stability. Required for efficient homologous recombination-dependent repair of double-strand breaks (DSBs) and ATM-dependent signaling pathways (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Localizes to nuclear foci following DNA damage. {ECO:0000250}. SUBUNIT: Component of the SOSS complex, composed of SOSS-B (SOSS-B1/NABP2 or SOSS-B2/NABP1), SOSS-A/INTS3 and SOSS-C/INIP. SOSS complexes containing SOSS-B1/NABP2 are more abundant than complexes containing SOSS-B2/NABP1. Interacts with INTS3; the interaction is direct (By similarity). {ECO:0000250}. +Q04887 SOX9_MOUSE Transcription factor SOX-9 507 56,077 Chain (1); Compositional bias (2); DNA binding (1); Helix (3); Sequence conflict (1) FUNCTION: Transcriptional regulator that plays a role in chondrocytes differentiation and skeletal development (PubMed:20940257, PubMed:28263186). Binds to the COL2A1 promoter and activates COL2A1 expression, as part of a complex with ZNF219 (PubMed:20940257). {ECO:0000269|PubMed:20940257, ECO:0000269|PubMed:28263186}. PTM: Ubiquitinated. Ubiquitination leads to proteasomal degradation and is negatively regulated by DDRGK1. {ECO:0000250|UniProtKB:P48436}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267, ECO:0000269|PubMed:20940257}. SUBUNIT: Interacts (via C-terminus) with ZNF219 (PubMed:20940257). Interacts with DDRGK1 (By similarity). {ECO:0000250|UniProtKB:P48436, ECO:0000269|PubMed:20940257}. +P70302 STIM1_MOUSE Stromal interaction molecule 1 685 77,567 Calcium binding (1); Chain (1); Coiled coil (1); Compositional bias (3); Domain (2); Glycosylation (2); Modified residue (18); Motif (1); Region (1); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 214 234 Helical. {ECO:0000255}. TOPO_DOM 23 213 Extracellular. {ECO:0000255}.; TOPO_DOM 235 685 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a role in mediating store-operated Ca(2+) entry (SOCE), a Ca(2+) influx following depletion of intracellular Ca(2+) stores. Acts as Ca(2+) sensor in the endoplasmic reticulum via its EF-hand domain. Upon Ca(2+) depletion, translocates from the endoplasmic reticulum to the plasma membrane where it activates the Ca(2+) release-activated Ca(2+) (CRAC) channel subunit ORAI1. Involved in enamel formation. Activated following interaction with STIMATE, leading to promote STIM1 conformational switch. {ECO:0000250|UniProtKB:Q13586}. PTM: Glycosylation is required for cell surface expression. {ECO:0000250|UniProtKB:Q13586}.; PTM: Phosphorylated predominantly on Ser residues. {ECO:0000250|UniProtKB:Q13586}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q13586}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q13586}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q13586}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q13586}. Sarcoplasmic reticulum {ECO:0000250|UniProtKB:Q13586}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q13586}. Note=Translocates from the endoplasmic reticulum to the cell membrane in response to a depletion of intracellular Ca(2+) and is detected at punctae corresponding to junctions between the endoplasmic reticulum and the cell membrane. Associated with the microtubule network at the growing distal tip of microtubules. Colocalizes with ORAI1 at the cell membrane. Colocalizes preferentially with CASQ1 at endoplasmic reticulum in response to a depletion of intracellular calcium (By similarity). {ECO:0000250|UniProtKB:Q13586}. SUBUNIT: Monomer in the presence of Ca(2+). It oligomerizes in absence of Ca(2+). Forms homooligomers and heterooligomers with STIM2. Interacts (via the transmembrane region and the SOAR/CAD domain) with SPPL3; the interaction promotes the binding of STIM1 to ORAI1. Interacts with ORAI1. Interacts with MAPRE1; probably required for targeting to the growing microtubule plus ends. Interacts with CRACR2A/EFCAB4B; the interaction is direct and takes place in absence of Ca(2+). Forms a complex with CRACR2A/EFCAB4B and ORAI1 at low concentration of Ca(2+), the complex dissociates at elevated Ca(2+) concentrations. Interacts with SARAF, promoting a slow inactivation of STIM1-dependent SOCE activity, possibly by facilitating the deoligomerization of STIM1. Interacts with ASPH. Interacts with SLC35G1; intracellular Ca(2+)-dependent. May interact with ATP1A1, ATP2A2, ATP2B1, ATP2B4, KPNB1 and XPO1; through SLC35G1. Interacts with TMEM203. Interacts with STIMATE, promoting STIM1 conformational switch (By similarity). Interacts with TMEM178A (PubMed:26644563). Interacts with CASQ1 (via C-terminal end and preferentially with the monomeric form); this interaction increases in response to a depletion of intracellular calcium, decreases both STIM1 aggregation and clustering, interaction of STIM1 with ORAI1 and store-operated Ca(2+) entry (SOCE) activity (By similarity). Interacts with ADCY8 (By similarity). {ECO:0000250|UniProtKB:Q13586, ECO:0000269|PubMed:26644563}. DOMAIN: The microtubule tip localization signal (MtLS) motif; mediates interaction with MAPRE1 and targeting to the growing microtubule plus ends. {ECO:0000250|UniProtKB:Q13586}.; DOMAIN: The STIM1 Orai1-activating region/CRAC-activating domain (SOAR/CAD) mediates interaction with ORAI1 to activate the channel. {ECO:0000250|UniProtKB:Q13586}. TISSUE SPECIFICITY: Expressed in maturation-stage ameloblasts (at protein level). Expressed in all tissues examined and in many cell types, including bone marrow stroma, fibroblast, B-cell precursors, lymphoma and erythroleukemia. {ECO:0000269|PubMed:24621671, ECO:0000269|PubMed:8707854}. +Q9Z2W1 STK25_MOUSE Serine/threonine-protein kinase 25 (EC 2.7.11.1) (Ste20-like kinase) (Sterile 20/oxidant stress-response kinase 1) (SOK-1) (Ste20/oxidant stress response kinase 1) 426 48,158 Active site (1); Binding site (1); Chain (1); Domain (1); Modified residue (2); Nucleotide binding (1); Sequence conflict (1) FUNCTION: Oxidant stress-activated serine/threonine kinase that may play a role in the response to environmental stress. Targets to the Golgi apparatus where it appears to regulate protein transport events, cell adhesion, and polarity complexes important for cell migration (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus {ECO:0000250}. Note=Localizes to the Golgi apparatus. {ECO:0000250}. SUBUNIT: Homodimer. Interacts with CTTNBP2NL. {ECO:0000250}. +Q60864 STIP1_MOUSE Stress-induced-phosphoprotein 1 (STI1) (mSTI1) (Hsc70/Hsp90-organizing protein) (Hop) 543 62,582 Chain (1); Cross-link (4); Domain (2); Modified residue (12); Motif (1); Repeat (9); Sequence conflict (7) FUNCTION: Acts as a co-chaperone for HSP90AA1. Mediates the association of the molecular chaperones HSPA8/HSC70 and HSP90. {ECO:0000250|UniProtKB:O35814, ECO:0000250|UniProtKB:P31948}. PTM: In vitro kinase assay failed to detect phosphorylation by MAPKAPK2. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8999875}. Nucleus {ECO:0000269|PubMed:8999875}. SUBUNIT: Probably forms a complex composed of chaperones HSP90 and HSP70, co-chaperones STIP1/HOP, CDC37, PPP5C, PTGES3/p23, TSC1 and client protein TSC2 (By similarity). Forms a complex with HSPA8/HSC70, HSPCA/HSP-86 and HSPCB/HSP-84 (PubMed:8999875). Interacts with PACRG. Interacts with METTL21B. Interacts with HSP90/HSP90AA1; the interaction dissociates the PPP5C:HSP90AA1 interaction. Interacts with FLCN, FNIP1 and FNIP2. Interacts with HSPA8/HSC70 (By similarity). Interacts with HSP90AB1; upon SMYD2-dependent HSP90AB1 methylation (By similarity). {ECO:0000250|UniProtKB:O35814, ECO:0000250|UniProtKB:P31948, ECO:0000269|PubMed:8999875}. DOMAIN: The TPR 1 repeat interacts with the C-terminal of HSC70. The TPR 4, 5 and 6 repeats (also called TPR2A domain) and TPR 7, 8 and 9 repeats (also called TPR2B domain) interact with HSP90 (By similarity). {ECO:0000250}. +Q6P3A1 STMD1_MOUSE Stathmin domain-containing protein 1 279 31,413 Chain (1); Domain (1); Initiator methionine (1); Lipidation (1) +Q99JB2 STML2_MOUSE Stomatin-like protein 2, mitochondrial (SLP-2) (mslp2) 353 38,385 Chain (1); Coiled coil (1); Modified residue (6); Sequence conflict (2); Transit peptide (1) FUNCTION: Mitochondrial protein that probably regulates the biogenesis and the activity of mitochondria. Stimulates cardiolipin biosynthesis, binds cardiolipin-enriched membranes where it recruits and stabilizes some proteins including prohibitin and may therefore act in the organization of functional microdomains in mitochondrial membranes. Through regulation of the mitochondrial function may play a role into several biological processes including cell migration, cell proliferation, T-cell activation, calcium homeostasis and cellular response to stress. May play a role in calcium homeostasis through negative regulation of calcium efflux from mitochondria. Required for mitochondrial hyperfusion a pro-survival cellular response to stress which results in increased ATP production by mitochondria. May also regulate the organization of functional domains at the plasma membrane and play a role in T-cell activation through association with the T-cell receptor signaling complex and its regulation. {ECO:0000269|PubMed:19360003, ECO:0000269|PubMed:23028053}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22623988}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9UJZ1}. Mitochondrion {ECO:0000269|PubMed:22623988}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9UJZ1}; Lipid-anchor {ECO:0000250|UniProtKB:Q9UJZ1}. Mitochondrion intermembrane space {ECO:0000250|UniProtKB:Q9UJZ1}. Membrane raft {ECO:0000250|UniProtKB:Q9UJZ1}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9UJZ1}. Note=Behaves as an integral membrane protein of the mitochondrion despite the absence of a detectable transmembrane domain. Also associates with the actin cytoskeleton and membrane rafts in activated T-cells. A minor pool is associated with the plasma membrane and is enriched at the immunological synapse in activated T-cells. {ECO:0000250|UniProtKB:Q9UJZ1}. SUBUNIT: Forms homooligomers (By similarity). Interacts with MFN2; may form heterooligomers (By similarity). Interacts with PHB and PHB2; recruits them to cardiolipin-enriched mitochondrial membranes and stabilizes them (By similarity). Interacts with CACNA2D2. {ECO:0000250, ECO:0000269|PubMed:16928863}. +Q9JHN8 STK19_MOUSE Serine/threonine-protein kinase 19 (EC 2.7.11.1) (Protein RP1) 254 28,104 Chain (1) FUNCTION: Seems to be a protein kinase. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: The N-terminus interacts with BAG1. {ECO:0000250}. +Q499E5 STOX2_MOUSE Storkhead-box protein 2 926 102,757 Alternative sequence (3); Chain (1); Erroneous initiation (1); Sequence conflict (7) +Q9DAG5 STPG4_MOUSE Protein STPG4 (Gonad-specific expression gene protein) (GSE) (Sperm-tail PG-rich repeat-containing protein 4) 247 27,632 Chain (1) FUNCTION: Maternal factor that plays a role in epigenetic chromatin reprogramming during early development of the zygote (PubMed:23560077). Involved in the regulation of gametic DNA demethylation by inducing the conversion of the modified genomic base 5-methylcytosine (5mC) into 5-hydroxymethylcytosine (5hmC) (PubMed:23560077). {ECO:0000269|PubMed:23560077}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16571911}. Nucleus {ECO:0000269|PubMed:16571911, ECO:0000269|PubMed:23560077}. Note=Localizes in female and male zygote pronucleus (PubMed:23560077, PubMed:16571911). Associates preferentially with the paternal chromatin during zygote development (PubMed:23560077). {ECO:0000269|PubMed:23560077}. SUBUNIT: Interacts with histone H3 (PubMed:23560077). Interacts with histone H4 (PubMed:23560077). {ECO:0000269|PubMed:23560077}. TISSUE SPECIFICITY: Expressed in ovary and testis (PubMed:16571911). Expressed in spermatocytes I in the pachytene stage, round spermatids, and elongated spermatids (PubMed:16571911). Expressed in the germinal vesicle (GV) stage and stage 2 meiosis (MII) oocytes and pre-implantation embryos until blastocyst stage (at protein level) (PubMed:16571911, PubMed:23560077). {ECO:0000269|PubMed:16571911, ECO:0000269|PubMed:23560077}. +P11378 STP2_MOUSE Nuclear transition protein 2 (TP-2) (TP2) 117 13,117 Chain (1); Erroneous initiation (1); Metal binding (8); Modified residue (1); Motif (1); Sequence conflict (4) FUNCTION: Plays a key role in the replacement of histones to protamine in the elongating spermatids of mammals (PubMed:15163613, PubMed:15189834, PubMed:15083521, PubMed:28366643). In condensing spermatids, loaded onto the nucleosomes, where it promotes the recruitment and processing of protamines, which are responsible for histone eviction (PubMed:28366643). The histone H2AFB1-HIST1H2BA/TH2B dimer is required for loading of TNP2 onto chromatin (PubMed:28366643). {ECO:0000269|PubMed:15083521, ECO:0000269|PubMed:15163613, ECO:0000269|PubMed:15189834, ECO:0000269|PubMed:28366643}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15163613}. Chromosome {ECO:0000269|PubMed:28366643}. Note=Loaded onto the nucleosomes of condensing spermatids (PubMed:28366643). Inclusion of the H2AFB1-HIST1H2BA/TH2B dimer into chromatin opens the nucleosomes, releasing the nucleosomal DNA ends and allowing the invasion of nucleosomes by transition protein TNP2 (PubMed:28366643). Nuclear import is ATP-dependent and nucleolar localization requires the protein to be phosphorylated (By similarity). {ECO:0000250|UniProtKB:P11101, ECO:0000269|PubMed:28366643}. +Q9DCI3 STR3N_MOUSE STARD3 N-terminal-like protein (MLN64 N-terminal domain homolog) 235 26,811 Chain (1); Domain (1); Modified residue (5); Motif (1); Sequence conflict (2); Topological domain (5); Transmembrane (4) TRANSMEM 54 74 Helical. {ECO:0000255|PROSITE-ProRule:PRU00770}.; TRANSMEM 98 118 Helical. {ECO:0000255|PROSITE-ProRule:PRU00770}.; TRANSMEM 123 143 Helical. {ECO:0000255|PROSITE-ProRule:PRU00770}.; TRANSMEM 151 171 Helical. {ECO:0000255|PROSITE-ProRule:PRU00770}. TOPO_DOM 1 53 Cytoplasmic. {ECO:0000250|UniProtKB:O95772}.; TOPO_DOM 75 97 Extracellular. {ECO:0000255}.; TOPO_DOM 119 122 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 144 150 Extracellular. {ECO:0000255}.; TOPO_DOM 172 235 Cytoplasmic. {ECO:0000250|UniProtKB:O95772}. FUNCTION: Tethering protein that creates contact site between the endoplasmic reticulum and late endosomes: localizes to late endosome membranes and contacts the endoplasmic reticulum via interaction with VAPA and VAPB. {ECO:0000250|UniProtKB:O95772}. SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250|UniProtKB:O95772}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to contact sites between the endoplasmic reticulum and late endosomes: associates with the endoplasmic reticulum membrane via interaction with VAPA and VAPB. {ECO:0000250|UniProtKB:O95772}. SUBUNIT: Homodimer. Interacts (via the MENTAL domain) with STARD3NL. Interacts (via FFAT motif) with VAPA. Interacts (via FFAT motif) with VAPB. {ECO:0000250|UniProtKB:O95772}. DOMAIN: The FFAT motif mediates interaction with VAPA and VAPB. {ECO:0000250|UniProtKB:Q14849}.; DOMAIN: The MENTAL domain anchors the protein in endosome membranes and exposes the START domain in the cytosol (By similarity). It binds cholesterol and mediates homotypic as well as heterotypic interactions between STARD3 and STARD3NL (By similarity). {ECO:0000250|UniProtKB:O95772, ECO:0000250|UniProtKB:Q14849}. +Q8VIM6 STRC_MOUSE Stereocilin 1809 196,347 Chain (1); Compositional bias (1); Glycosylation (15); Sequence conflict (4); Signal peptide (1) FUNCTION: Essential to the formation of horizontal top connectors between outer hair cell stereocilia. {ECO:0000269|PubMed:21165971}. SUBCELLULAR LOCATION: Cell surface. Cell projection, kinocilium. Cell projection, stereocilium. TISSUE SPECIFICITY: Strongly expressed in the inner ear, detected in the testis, and barely detected in the eye. Detected in the six sensory areas of the inner ear by immunofluorescence. Expressed only in the sensory hair cells and associated with the stereocilia, the stiff microvilli forming the structure for mechanoreception of sound stimulation. {ECO:0000269|PubMed:11687802, ECO:0000269|PubMed:21165971}. +Q9ERG2 STRN3_MOUSE Striatin-3 (Cell cycle autoantigen SG2NA) (S/G2 antigen) 796 87,150 Chain (1); Coiled coil (1); Compositional bias (1); Modified residue (7); Region (2); Repeat (6) FUNCTION: Binds calmodulin in a calcium dependent manner. May function as scaffolding or signaling protein (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein. SUBUNIT: Interacts with protein phosphatase 2A (PP2A). Interacts with CDC42BPB. {ECO:0000250|UniProtKB:Q13033}. TISSUE SPECIFICITY: Mainly expressed in the brain and muscles but is also detected at low levels in various tissues such as kidney, spleen and lung. {ECO:0000269|PubMed:10748158}. +P46978 STT3A_MOUSE Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A (Oligosaccharyl transferase subunit STT3A) (STT3-A) (EC 2.4.99.18) (B5) (Integral membrane protein 1) 705 80,598 Binding site (5); Chain (1); Glycosylation (3); Metal binding (3); Motif (5); Region (1); Site (1); Topological domain (14); Transmembrane (13) TRANSMEM 18 38 Helical. {ECO:0000255}.; TRANSMEM 120 138 Helical. {ECO:0000250|UniProtKB:P39007}.; TRANSMEM 141 158 Helical. {ECO:0000250|UniProtKB:P39007}.; TRANSMEM 170 189 Helical. {ECO:0000250|UniProtKB:P39007}.; TRANSMEM 192 206 Helical. {ECO:0000250|UniProtKB:P39007}.; TRANSMEM 212 228 Helical. {ECO:0000250|UniProtKB:P39007}.; TRANSMEM 234 259 Helical. {ECO:0000250|UniProtKB:P39007}.; TRANSMEM 268 287 Helical. {ECO:0000250|UniProtKB:P39007}.; TRANSMEM 301 321 Helical. {ECO:0000255}.; TRANSMEM 357 379 Helical. {ECO:0000250|UniProtKB:P39007}.; TRANSMEM 386 402 Helical. {ECO:0000250|UniProtKB:P39007}.; TRANSMEM 407 428 Helical. {ECO:0000250|UniProtKB:P39007}.; TRANSMEM 454 473 Helical. {ECO:0000250|UniProtKB:P39007}. TOPO_DOM 1 17 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 39 119 Lumenal. {ECO:0000305}.; TOPO_DOM 139 140 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 159 169 Lumenal. {ECO:0000305}.; TOPO_DOM 190 191 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 207 211 Lumenal. {ECO:0000305}.; TOPO_DOM 229 233 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 260 267 Lumenal. {ECO:0000305}.; TOPO_DOM 288 300 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 322 356 Lumenal. {ECO:0000305}.; TOPO_DOM 380 385 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 403 406 Lumenal. {ECO:0000305}.; TOPO_DOM 429 453 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 474 705 Lumenal. {ECO:0000305}. Protein modification; protein glycosylation. FUNCTION: Catalytic subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. This subunit contains the active site and the acceptor peptide and donor lipid-linked oligosaccharide (LLO) binding pockets (By similarity). STT3A is present in the majority of OST complexes and mediates cotranslational N-glycosylation of most sites on target proteins, while STT3B-containing complexes are required for efficient post-translational glycosylation and mediate glycosylation of sites that have been skipped by STT3A (By similarity). {ECO:0000250|UniProtKB:F1PJP5, ECO:0000250|UniProtKB:P39007, ECO:0000250|UniProtKB:P46977}. SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:12887896, ECO:0000269|PubMed:15781470}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:15781470}; Multi-pass membrane protein {ECO:0000269|PubMed:15781470}. SUBUNIT: Component of the oligosaccharyltransferase (OST) complex. OST exists in two different complex forms which contain common core subunits RPN1, RPN2, OST48, OST4, DAD1 and TMEM258, either STT3A or STT3B as catalytic subunits, and form-specific accessory subunits. STT3A complex assembly occurs through the formation of 3 subcomplexes. Subcomplex 1 contains RPN1 and TMEM258, subcomplex 2 contains the STT3A-specific subunits STT3A, DC2/OSTC, and KCP2 as well as the core subunit OST4, and subcomplex 3 contains RPN2, DAD1, and OST48. The STT3A complex can form stable complexes with the Sec61 complex or with both the Sec61 and TRAP complexes. {ECO:0000250|UniProtKB:F1PJP5}. DOMAIN: Despite low primary sequence conservation between eukaryotic catalytic subunits and bacterial and archaeal single subunit OSTs (ssOST), structural comparison revealed several common motifs at spatially equivalent positions, like the DXD motif 1 on the external loop 1 and the DXD motif 2 on the external loop 2 involved in binding of the metal ion cofactor and the carboxamide group of the acceptor asparagine, the conserved Glu residue of the TIXE/SVSE motif on the external loop 5 involved in catalysis, as well as the WWDYG and the DK/MI motifs in the globular domain that define the binding pocket for the +2 Ser/Thr of the acceptor sequon. In bacterial ssOSTs, an Arg residue was found to interact with a negatively charged side chain at the -2 position of the sequon. This Arg is conserved in bacterial enzymes and correlates with an extended sequon requirement (Asp-X-Asn-X-Ser/Thr) for bacterial N-glycosylation. {ECO:0000250|UniProtKB:P39007}. +Q9D0I4 STX17_MOUSE Syntaxin-17 301 33,221 Chain (1); Coiled coil (1); Domain (1); Initiator methionine (1); Modified residue (4); Motif (1); Region (1); Sequence conflict (1); Topological domain (3); Transmembrane (2) TRANSMEM 228 248 Helical. {ECO:0000255}.; TRANSMEM 254 274 Helical. {ECO:0000255}. TOPO_DOM 2 227 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 249 253 Lumenal. {ECO:0000255}.; TOPO_DOM 275 301 Cytoplasmic. {ECO:0000255}. FUNCTION: SNAREs, soluble N-ethylmaleimide-sensitive factor-attachment protein receptors, are essential proteins for fusion of cellular membranes. SNAREs localized on opposing membranes assemble to form a trans-SNARE complex, an extended, parallel four alpha-helical bundle that drives membrane fusion. STX17 is a SNARE of the autophagosome involved in autophagy through the direct control of autophagosome membrane fusion with the lysosome membrane. May also play a role in the early secretory pathway where it may maintain the architecture of the endoplasmic reticulum-Golgi intermediate compartment/ERGIC and Golgi and/or regulate transport between the endoplasmic reticulum, the ERGIC and the Golgi (By similarity). {ECO:0000250|UniProtKB:P56962}. PTM: Dephosphorylation by PTPN2; regulates exit from the endoplasmic reticulum (By similarity). Phosphorylated at Tyr-156 probably by ABL1 (PubMed:23006999). {ECO:0000250|UniProtKB:Q9Z158, ECO:0000269|PubMed:23006999}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P56962}; Multi-pass membrane protein {ECO:0000255}. Smooth endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9Z158}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:P56962}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:27628032}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250|UniProtKB:Q9Z158}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9Z158}. Note=Has a hairpin-like insertion into membranes. Localizes to the completed autophagosome membrane upon cell starvation (By similarity). May also localize to the mitochondria (By similarity). {ECO:0000250|UniProtKB:P56962}. SUBUNIT: Forms a SNARE complex composed of VAMP8, SNAP29 and STX17 involved in fusion of autophagosome with lysosome (By similarity). May interact with VTI1B (By similarity). Probably interacts with BET1, SCFD1 and SEC22B (By similarity). Interacts with PTPN2 and ABL1; involved in STX17 phosphorylation (By similarity). Interacts with COPB1 (By similarity). Interacts with TMED9 and TMED10; the interaction is direct (By similarity). Interacts with VAMP7 (PubMed:23217709). {ECO:0000250|UniProtKB:P56962, ECO:0000250|UniProtKB:Q9Z158, ECO:0000269|PubMed:23217709}. +Q8CDJ8 STON1_MOUSE Stonin-1 (Stoned B-like factor) 730 81,793 Chain (1); Domain (2); Sequence conflict (3) FUNCTION: May be involved in the endocytic machinery. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}. Note=Some fraction is membrane-associated. {ECO:0000250}. +Q8K1E0 STX5_MOUSE Syntaxin-5 355 39,713 Alternative sequence (1); Chain (1); Coiled coil (1); Domain (1); Erroneous initiation (2); Motif (1); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 334 354 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 1 333 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 355 355 Vesicular. {ECO:0000255}. FUNCTION: Mediates endoplasmic reticulum to Golgi transport. Together with p115/USO1 and GM130/GOLGA2, involved in vesicle tethering and fusion at the cis-Golgi membrane to maintain the stacked and inter-connected structure of the Golgi apparatus. {ECO:0000250|UniProtKB:Q08851}. SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q08851}; Single-pass type IV membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q08851}. Note=Localizes throughout the Golgi apparatus, but most abundant in the cis-most cisternae. {ECO:0000250|UniProtKB:Q08851}. SUBUNIT: Part of a ternary complex containing STX5A, NSFL1C and VCP. Part of a unique SNARE complex composed of the Golgi SNAREs GOSR1, GOSR2, YKT6 and VTI1A (PubMed:9705316). Interacts with COG4 (By similarity). Interacts with GM130/GOLGA2 (By similarity). Interacts (via IxM motif) with SEC24C and SEC24D; mediates STX5 packaging into COPII-coated vesicles (By similarity). {ECO:0000250|UniProtKB:Q08851, ECO:0000250|UniProtKB:Q13190, ECO:0000269|PubMed:9705316}. +O70439 STX7_MOUSE Syntaxin-7 261 29,821 Chain (1); Coiled coil (1); Domain (1); Helix (1); Initiator methionine (1); Modified residue (9); Topological domain (2); Transmembrane (1) TRANSMEM 239 259 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 2 238 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 260 261 Vesicular. {ECO:0000255}. FUNCTION: May be involved in protein trafficking from the plasma membrane to the early endosome (EE) as well as in homotypic fusion of endocytic organelles. Mediates the endocytic trafficking from early endosomes to late endosomes and lysosomes (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. SUBUNIT: Interacts with VPS11, VPS16 and VPS18. Interacts with VPS33A (By similarity). Forms a SNARE complex with VTI1B, STX8 and VAMP8 which functions in the homotypic fusion of late endosomes. Component of the SNARE complex composed of STX7, STX8, VAMP7 and VTI1B that is required for heterotypic fusion of late endosomes with lysosomes. {ECO:0000250, ECO:0000269|PubMed:11786915, ECO:0000269|PubMed:15363411}. +Q6J9G1 STYK1_MOUSE Tyrosine-protein kinase STYK1 (EC 2.7.10.2) (Novel oncogene with kinase domain) (mNOK) (Serine/threonine/tyrosine kinase 1) 429 48,121 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Domain (1); Nucleotide binding (1); Sequence conflict (3); Transmembrane (1) TRANSMEM 30 50 Helical. {ECO:0000255}. FUNCTION: Probable tyrosine protein-kinase, which has strong transforming capabilities on a variety of cell lines including NIH 3T3 fibroblasts and on athymic nude mice. When overexpressed, it can also induce tumor cell invasion as well as metastasis in distant organs. May act by activating both MAP kinase and phosphatidylinositol 3'-kinases (PI3K) pathways. {ECO:0000269|PubMed:15150103}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Highly expressed in colon and small intestine. Weakly or not expressed in spleen, skeletal muscle, liver, kidney, heart and brain. Expressed in transformed kidney cell lines (COS-1 and HEK293T). {ECO:0000269|PubMed:15150103}. +Q9Z2I9 SUCB1_MOUSE Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial (EC 6.2.1.5) (ATP-specific succinyl-CoA synthetase subunit beta) (A-SCS) (Succinyl-CoA synthetase beta-A chain) (SCS-betaA) 463 50,114 Binding site (2); Chain (1); Domain (1); Metal binding (2); Modified residue (12); Nucleotide binding (1); Region (1); Site (2); Transit peptide (1) Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1. FUNCTION: ATP-specific succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit. {ECO:0000255|HAMAP-Rule:MF_03220}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03220}. SUBUNIT: Heterodimer of an alpha and a beta subunit. The beta subunit determines specificity for ATP. {ECO:0000255|HAMAP-Rule:MF_03220}. +Q9R244 TRPC2_MOUSE Short transient receptor potential channel 2 (TrpC2) (Transient receptor protein 2) (TRP-2) (mTrp2) 1172 130,531 Alternative sequence (4); Chain (1); Compositional bias (1); Repeat (3); Sequence conflict (12); Topological domain (7); Transmembrane (6) TRANSMEM 660 680 Helical. {ECO:0000255}.; TRANSMEM 703 723 Helical. {ECO:0000255}.; TRANSMEM 739 759 Helical. {ECO:0000255}.; TRANSMEM 790 810 Helical. {ECO:0000255}.; TRANSMEM 834 854 Helical. {ECO:0000255}.; TRANSMEM 900 920 Helical. {ECO:0000255}. TOPO_DOM 1 659 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 681 702 Extracellular. {ECO:0000255}.; TOPO_DOM 724 738 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 760 789 Extracellular. {ECO:0000255}.; TOPO_DOM 811 833 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 855 899 Extracellular. {ECO:0000255}.; TOPO_DOM 921 1172 Cytoplasmic. {ECO:0000255}. FUNCTION: Thought to form a receptor-activated non-selective calcium permeant cation channel. Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. May also be activated by intracellular calcium store depletion. Plays a role in mediating responsivity to pheromones that elicit aggressive and mating behaviors. Required for response to the Esp1 pheromone which enhances female sexual receptive behavior and to the Esp22 pheromone which inhibits adult male mating behavior. {ECO:0000269|PubMed:11823606, ECO:0000269|PubMed:11972034, ECO:0000269|PubMed:20596023, ECO:0000269|PubMed:24089208}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Isoform 3 is ubiquitously expressed at low levels. Isoform 4 is expressed exclusively in vomeronasal organ. +Q9QX29 TRPC5_MOUSE Short transient receptor potential channel 5 (TrpC5) (Capacitative calcium entry channel 2) (CCE2) (Transient receptor protein 5) (TRP-5) (mTRP5) (Trp-related protein 5) 975 111,458 Chain (1); Compositional bias (1); Glycosylation (1); Region (1); Repeat (4); Topological domain (7); Transmembrane (6) TRANSMEM 331 351 Helical. {ECO:0000255}.; TRANSMEM 399 419 Helical. {ECO:0000255}.; TRANSMEM 438 458 Helical. {ECO:0000255}.; TRANSMEM 471 491 Helical. {ECO:0000255}.; TRANSMEM 513 533 Helical. {ECO:0000255}.; TRANSMEM 604 624 Helical. {ECO:0000255}. TOPO_DOM 1 330 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 352 398 Extracellular. {ECO:0000255}.; TOPO_DOM 420 437 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 459 470 Extracellular. {ECO:0000255}.; TOPO_DOM 492 512 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 534 603 Extracellular. {ECO:0000255}.; TOPO_DOM 625 975 Cytoplasmic. {ECO:0000255}. FUNCTION: Thought to form a receptor-activated non-selective calcium permeant cation channel. Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Has also been shown to be calcium-selective. May also be activated by intracellular calcium store depletion. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Homotetramer and heterotetramer with TRPC1 and/or TRPC4 (By similarity). Interacts (via C-terminus) with CABP1. Interacts with NHERF (By similarity). Interacts with MX1 and RNF24 (By similarity). Interacts with SESTD1 (via the spectrin 1 repeat) (By similarity). Interacts with TRPC4AP. {ECO:0000250, ECO:0000269|PubMed:15895247, ECO:0000269|PubMed:20458742}. TISSUE SPECIFICITY: Expressed almost exclusively in brain, in mitral cells of the olfactory bulb, in lateral cerebellar nuclei and in pyramidal neurons of the hippocampus. Very low levels detected in liver kidney, testis, and uterus. {ECO:0000269|PubMed:9687496}. +Q9WVC5 TRPC7_MOUSE Short transient receptor potential channel 7 (TrpC7) (Transient receptor protein 7) (TRP-7) (mTRP7) 862 99,475 Chain (1); Glycosylation (1); Modified residue (1); Repeat (4); Topological domain (7); Transmembrane (6) TRANSMEM 352 372 Helical. {ECO:0000255}.; TRANSMEM 384 404 Helical. {ECO:0000255}.; TRANSMEM 466 486 Helical. {ECO:0000255}.; TRANSMEM 538 558 Helical. {ECO:0000255}.; TRANSMEM 582 602 Helical. {ECO:0000255}.; TRANSMEM 652 672 Helical. {ECO:0000255}. TOPO_DOM 1 351 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 373 383 Extracellular. {ECO:0000255}.; TOPO_DOM 405 465 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 487 537 Extracellular. {ECO:0000255}.; TOPO_DOM 559 581 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 603 651 Extracellular. {ECO:0000255}.; TOPO_DOM 673 862 Cytoplasmic. {ECO:0000255}. FUNCTION: Thought to form a receptor-activated non-selective calcium permeant cation channel. Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Activated by diacylglycerol (DAG). May also be activated by intracellular calcium store depletion. PTM: Phosphorylation by PRKG1 at Thr-15 negatively regulates TRPC7 activity. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Nucleus envelope {ECO:0000250}. SUBUNIT: Interacts with MX1 and RNF24. Interacts (via ANK-repeat domains) with PRKG1. {ECO:0000250}. +Q99MT6 SUCR1_MOUSE Succinate receptor 1 (G-protein coupled receptor 91) 317 36,765 Chain (1); Disulfide bond (1); Glycosylation (1); Sequence conflict (3); Topological domain (8); Transmembrane (7) TRANSMEM 24 47 Helical; Name=1. {ECO:0000255}.; TRANSMEM 56 76 Helical; Name=2. {ECO:0000255}.; TRANSMEM 102 119 Helical; Name=3. {ECO:0000255}.; TRANSMEM 134 157 Helical; Name=4. {ECO:0000255}.; TRANSMEM 181 204 Helical; Name=5. {ECO:0000255}.; TRANSMEM 229 246 Helical; Name=6. {ECO:0000255}.; TRANSMEM 278 294 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 23 Extracellular. {ECO:0000255}.; TOPO_DOM 48 55 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 77 101 Extracellular. {ECO:0000255}.; TOPO_DOM 120 133 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 158 180 Extracellular. {ECO:0000255}.; TOPO_DOM 205 228 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 247 277 Extracellular. {ECO:0000255}.; TOPO_DOM 295 317 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for succinate. {ECO:0000269|PubMed:15141213}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Predominantly expressed in the kidney (proximal and distal tubules and the juxtaglomerular apparatus). Weakly expressed in liver, spleen and small intestine. {ECO:0000269|PubMed:11273702, ECO:0000269|PubMed:15141213}. +Q9Z0P7 SUFU_MOUSE Suppressor of fused homolog 484 53,957 Alternative sequence (3); Chain (1); Cross-link (2); Modified residue (7); Region (1); Sequence conflict (2) FUNCTION: Negative regulator in the hedgehog/smoothened signaling pathway (PubMed:16155214, PubMed:16459298). Down-regulates GLI1-mediated transactivation of target genes (PubMed:11960000). Part of a corepressor complex that acts on DNA-bound GLI1 (PubMed:11960000). May also act by linking GLI1 to BTRC and thereby targeting GLI1 to degradation by the proteasome (By similarity). Sequesters GLI1, GLI2 and GLI3 in the cytoplasm, this effect is overcome by binding of STK36 to both SUFU and a GLI protein (PubMed:10531011, PubMed:16459298). Negative regulator of beta-catenin signaling (PubMed:11477086). Regulates the formation of either the repressor form (GLI3R) or the activator form (GLI3A) of the full-length form of GLI3 (GLI3FL) (PubMed:10531011, PubMed:20360384). GLI3FL is complexed with SUFU in the cytoplasm and is maintained in a neutral state (PubMed:10531011, PubMed:20360384). Without the Hh signal, the SUFU-GLI3 complex is recruited to cilia, leading to the efficient processing of GLI3FL into GLI3R (PubMed:10531011, PubMed:20360384). When Hh signaling is initiated, SUFU dissociates from GLI3FL and the latter translocates to the nucleus, where it is phosphorylated, destabilized, and converted to a transcriptional activator (GLI3A) (PubMed:10531011, PubMed:20360384). Required for normal embryonic development (PubMed:16155214, PubMed:16459298). Required for the proper formation of hair follicles and the control of epidermal differentiation (PubMed:16155214, PubMed:16459298, PubMed:23034632). {ECO:0000250|UniProtKB:Q9UMX1, ECO:0000269|PubMed:10531011, ECO:0000269|PubMed:11477086, ECO:0000269|PubMed:11960000, ECO:0000269|PubMed:16155214, ECO:0000269|PubMed:16459298, ECO:0000269|PubMed:20360384, ECO:0000269|PubMed:23034632}. PTM: Polyubiquitinated at Lys-257 by the SCF(FBXL17) complex, leading to its subsequent degradation and allowing the release of GLI1 for proper hedgehog/smoothened signal transduction. Ubiquitination is impaired by phosphorylation at Ser-342, Ser-346, Ser-352 and Thr-353. {ECO:0000250|UniProtKB:Q9UMX1}.; PTM: Phosphorylation at Ser-342, Ser-346, Ser-352 and Thr-353 prevents ubiquitination by the SCF(FBXL17) complex. {ECO:0000250|UniProtKB:Q9UMX1}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10531011, ECO:0000269|PubMed:16459298}. Nucleus {ECO:0000269|PubMed:10531011}. SUBUNIT: May form homodimers (By similarity). Interacts with ULK3; inactivating the protein kinase activity of ULK3. Interacts with RAB23 (By similarity). Part of a DNA-bound corepressor complex containing SAP18, GLI1 and SIN3 (PubMed:11960000). Part of a complex containing CTNNB1 (PubMed:11477086). Binds BTRC, GLI2, GLI3, SAP18 and STK36 (PubMed:20360384, PubMed:23034632). Binds both free and DNA-bound GLI1 (PubMed:10531011). Interacts with KIF7 (PubMed:19592253). Interacts with GLI3FL and this interaction regulates the formation of either repressor or activator forms of GLI3 (PubMed:20360384). Its association with GLI3FL is regulated by Hh signaling and dissociation of the SUFU-GLI3 interaction requires the presence of the ciliary motor KIF3A (PubMed:20360384). {ECO:0000250|UniProtKB:Q9UMX1, ECO:0000269|PubMed:10531011, ECO:0000269|PubMed:11477086, ECO:0000269|PubMed:11960000, ECO:0000269|PubMed:19592253, ECO:0000269|PubMed:20360384, ECO:0000269|PubMed:23034632}. TISSUE SPECIFICITY: Widely expressed in adult and fetal tissues. {ECO:0000269|PubMed:10531011, ECO:0000269|PubMed:11557033}. +Q8CH02 SUGP1_MOUSE SURP and G-patch domain-containing protein 1 (Splicing factor 4) 643 72,649 Beta strand (2); Chain (1); Compositional bias (2); Domain (1); Helix (9); Modified residue (7); Motif (1); Repeat (2); Sequence conflict (2); Turn (2) FUNCTION: Plays a role in pre-mRNA splicing. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Component of the spliceosome. {ECO:0000250}. +Q8R0F3 SUMF1_MOUSE Formylglycine-generating enzyme (FGE) (EC 1.8.3.7) (C-alpha-formylglycine-generating enzyme 1) (Sulfatase-modifying factor 1) 372 40,659 Chain (1); Disulfide bond (3); Erroneous initiation (2); Glycosylation (1); Metal binding (10); Region (1); Sequence conflict (1); Signal peptide (1) Protein modification; sulfatase oxidation. FUNCTION: Oxidase that catalyzes the conversion of cysteine to 3-oxoalanine on target proteins, using molecular oxygen and an unidentified reducing agent. 3-oxoalanine modification, which is also named formylglycine (fGly), occurs in the maturation of arylsulfatases and some alkaline phosphatases that use the hydrated form of 3-oxoalanine as a catalytic nucleophile. Known substrates include GALNS, ARSA, STS and ARSE. {ECO:0000250|UniProtKB:Q8NBK3}. PTM: N-glycosylated. Contains high-mannose-type oligosaccharides. {ECO:0000250|UniProtKB:Q8NBK3}. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:Q8NBK3}. SUBUNIT: Monomer, homodimer and heterodimer with SUMF2. {ECO:0000250|UniProtKB:Q8NBK3}. +P61957 SUMO2_MOUSE Small ubiquitin-related modifier 2 (SUMO-2) (SMT3 homolog 2) (Ubiquitin-like protein SMT3B) (Smt3B) 95 10,871 Beta strand (4); Chain (1); Cross-link (9); Domain (1); Helix (1); Modified residue (1); Propeptide (1); Turn (2) FUNCTION: Ubiquitin-like protein that can be covalently attached to proteins as a monomer or as a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by an E3 ligase such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Polymeric SUMO2 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. Plays a role in the regulation of sumoylation status of SETX (By similarity). {ECO:0000250|UniProtKB:P61956}. PTM: Polymeric chains can be formed through Lys-11 cross-linking. Polymeric SUMO2 chains undergo 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination by RNF4 (By similarity). {ECO:0000250}.; PTM: Cleavage of precursor form by SENP1 or SENP2 is necessary for function. {ECO:0000250}.; PTM: Monoubiquitinated N-terminally by UBE2W, which primes it for RNF4-dependent polyubiquitination by the UBE2V1-UBE2N heterodimer. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus, PML body {ECO:0000250}. SUBUNIT: Interacts with SAE2 and UBE2I. Interacts with ZNF451. Identified in a complex with ZNF451 and UBE2I/UBC9, where one ZNF451 interacts with one UBE2I/UBC9 and two SUMO2 chains, one bound to the UBE2I/UBC9 active site and the other to another region of the same UBE2I/UBC9 molecule. Covalently attached to a number of proteins. Interacts with PELP1. Interacts with USP25; the interaction sumoylates USP25. Interacts with SIMC1, CASP8AP2, RNF111 AND SOBP (via SIM domains). Interacts with MTA1. {ECO:0000250|UniProtKB:P61956}. +Q8BJS4 SUN2_MOUSE SUN domain-containing protein 2 (Protein unc-84 homolog B) (Sad1/unc-84 protein-like 2) 731 81,605 Alternative sequence (2); Beta strand (10); Chain (1); Coiled coil (2); Disulfide bond (1); Domain (1); Glycosylation (1); Helix (11); Modified residue (7); Mutagenesis (3); Region (2); Sequence conflict (4); Topological domain (2); Transmembrane (1) TRANSMEM 227 247 Helical. {ECO:0000255}. TOPO_DOM 1 226 Nuclear. {ECO:0000250}.; TOPO_DOM 248 731 Perinuclear space. FUNCTION: As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning. Specifically, SYNE2 and SUN2 assemble in arrays of transmembrane actin-associated nuclear (TAN) lines which are bound to F-actin cables and couple the nucleus to retrograde actin flow during actin-dependent nuclear movement. Required for interkinetic nuclear migration (INM) and essential for nucleokinesis and centrosome-nucleus coupling during radial neuronal migration in the cerebral cortex and during glial migration. Required for nuclear migration in retinal photoreceptor progenitors implicating association with cytoplasmic dynein-dynactin and kinesin motor complexes, and probably B-type lamins; SUN1 and SUN2 seem to act redundantly. The SUN1/2:KASH5 LINC complex couples telomeres to microtubules during meiosis; SUN1 and SUN2 seem to act at least partial redundantly. Anchors chromosome movement in the prophase of meiosis and is involved in selective gene expression of coding and non-coding RNAs needed for gametogenesis. Required for telomere attachment to nuclear envelope and gametogenesis. May also function on endocytic vesicles as a receptor for Rab5-GDP and participate in the activation of Rab5. {ECO:0000269|PubMed:16380439, ECO:0000269|PubMed:19509342, ECO:0000269|PubMed:19843581, ECO:0000269|PubMed:19874786, ECO:0000269|PubMed:20724637, ECO:0000269|PubMed:21177258, ECO:0000269|PubMed:23071752, ECO:0000269|PubMed:24586178, ECO:0000305}. PTM: The disulfid bond with SYNE2 is required for stability of the SUN2:SYNE2/KASH2 LINC complex under tensile forces though not required for the interaction. The disulfid bond is proposed to be conserved in LINC complexes involved in force transmission. {ECO:0000250|UniProtKB:Q9UH99}. SUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000269|PubMed:19933576}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9UH99}. Nucleus envelope {ECO:0000269|PubMed:17132086, ECO:0000269|PubMed:19843581, ECO:0000269|PubMed:19874786, ECO:0000269|PubMed:19933576}. Endosome membrane {ECO:0000250|UniProtKB:Q9UH99}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9UH99}. Note=Colocalizes with KASH5 at sites of telomere attachment in meiocytes. {ECO:0000269|PubMed:24586178}. SUBUNIT: Core component of the LINC complex which is composed of inner nuclear membrane SUN domain-containing proteins coupled to outer nuclear membrane KASH domain-containing nesprins. SUN and KASH domain-containing proteins seem to bind each other promiscuously; however, differentially expression of LINC complex constituents is giving rise to specific assemblies. At least SUN1/2-containing core LINC complexes are proposed to be hexameric composed of three protomers of each KASH and SUN domain-containing protein. Interacts with SYNE2; the SUN2:SYNE2/KASH2 LINC complex is a heterohexamer; the homotrimeric cloverleave-like conformation of the SUN domain is a prerequisite for LINC complex formation in which three separate SYNE2/KASH2 peptides bind at the interface of adjacent SUN domains. Component of a probable SUN2:KASH5 LINC complex. Interacts with SYNE1 and SYNE3; probably forming respective LINC complexes. Interacts with A-type lamin. Interaction with lamins B1 and C is hardly detectable. Interacts with EMD. Interacts with RAB5A. Interacts with TMEM43 and TMEM201. {ECO:0000250|UniProtKB:Q9UH99, ECO:0000269|PubMed:21177258, ECO:0000269|PubMed:22349700, ECO:0000269|PubMed:23071752, ECO:0000305|PubMed:24586178}. DOMAIN: The proximal coiled coil domain mediates trimerization required for binding to nesprins. The distal coiled coil domain is proposed to dynamically regulate the oligomeric state by locking the SUN domain in an inactive confirmation (PubMed:26688217). The coiled coil domains are proposed to be involved in load-bearing and force transmission from the cytoskeleton (By similarity). {ECO:0000250|UniProtKB:Q9UH99, ECO:0000269|PubMed:26688217}.; DOMAIN: The SUN domain may play a role in the nuclear anchoring and/or migration. {ECO:0000269|PubMed:19933576}. TISSUE SPECIFICITY: Highly expressed in heart, placenta and muscle. {ECO:0000269|PubMed:12393179}. +Q8R086 SUOX_MOUSE Sulfite oxidase, mitochondrial (EC 1.8.3.1) 546 60,756 Binding site (5); Chain (1); Domain (1); Erroneous initiation (1); Metal binding (3); Modified residue (1); Region (5); Sequence conflict (1); Transit peptide (1) Energy metabolism; sulfur metabolism. SUBCELLULAR LOCATION: Mitochondrion intermembrane space. SUBUNIT: Homodimer. +Q8R080 GTSE1_MOUSE G2 and S phase-expressed protein 1 (GTSE-1) (Protein B99) 741 78,751 Chain (1); Compositional bias (1); Modified residue (21); Sequence conflict (5) FUNCTION: May be involved in p53-induced cell cycle arrest in G2/M phase by interfering with microtubule rearrangements that are required to enter mitosis. Overexpression delays G2/M phase progression. PTM: Phosphorylated in mitosis. {ECO:0000269|PubMed:10984615}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Note=Associated with microtubules. +Q9DAN6 GTSF1_MOUSE Gametocyte-specific factor 1 (Protein FAM112B) 167 19,083 Chain (1); Modified residue (1); Zinc finger (2) FUNCTION: Required for spermatogenesis and is involved in the suppression of retrotransposon transcription in male germ cells. {ECO:0000269|PubMed:19735653}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17919994, ECO:0000269|PubMed:19735653}. TISSUE SPECIFICITY: Expressed abundantly in adult testis, at moderate levels in unfertilized eggs and ovaries and weakly in embryonic stem cells. {ECO:0000269|PubMed:17919994}. +Q9WV38 GTR5_MOUSE Solute carrier family 2, facilitated glucose transporter member 5 (Fructose transporter) (Glucose transporter type 5, small intestine) (GLUT-5) 501 55,409 Binding site (4); Chain (1); Glycosylation (1); Modified residue (1); Region (2); Sequence conflict (7); Topological domain (13); Transmembrane (12) TRANSMEM 18 38 Helical; Name=1. {ECO:0000250|UniProtKB:P43427}.; TRANSMEM 68 90 Helical; Name=2. {ECO:0000250|UniProtKB:P43427}.; TRANSMEM 98 118 Helical; Name=3. {ECO:0000250|UniProtKB:P43427}.; TRANSMEM 126 148 Helical; Name=4. {ECO:0000250|UniProtKB:P43427}.; TRANSMEM 161 181 Helical; Name=5. {ECO:0000250|UniProtKB:P43427}.; TRANSMEM 192 212 Helical; Name=6. {ECO:0000250|UniProtKB:P43427}.; TRANSMEM 277 297 Helical; Name=7. {ECO:0000250|UniProtKB:P43427}.; TRANSMEM 313 333 Helical; Name=8. {ECO:0000250|UniProtKB:P43427}.; TRANSMEM 342 362 Helical; Name=9. {ECO:0000250|UniProtKB:P43427}.; TRANSMEM 371 393 Helical; Name=10. {ECO:0000250|UniProtKB:P43427}.; TRANSMEM 412 432 Helical; Name=11. {ECO:0000250|UniProtKB:P43427}.; TRANSMEM 439 459 Helical; Name=12. {ECO:0000250|UniProtKB:P43427}. TOPO_DOM 1 17 Cytoplasmic. {ECO:0000250|UniProtKB:P43427}.; TOPO_DOM 39 67 Extracellular. {ECO:0000250|UniProtKB:P43427}.; TOPO_DOM 91 97 Cytoplasmic. {ECO:0000250|UniProtKB:P43427}.; TOPO_DOM 119 125 Extracellular. {ECO:0000250|UniProtKB:P43427}.; TOPO_DOM 149 160 Cytoplasmic. {ECO:0000250|UniProtKB:P43427}.; TOPO_DOM 182 191 Extracellular. {ECO:0000250|UniProtKB:P43427}.; TOPO_DOM 213 276 Cytoplasmic. {ECO:0000250|UniProtKB:P43427}.; TOPO_DOM 298 312 Extracellular. {ECO:0000250|UniProtKB:P43427}.; TOPO_DOM 334 341 Cytoplasmic. {ECO:0000250|UniProtKB:P43427}.; TOPO_DOM 363 370 Extracellular. {ECO:0000250|UniProtKB:P43427}.; TOPO_DOM 394 411 Cytoplasmic. {ECO:0000250|UniProtKB:P43427}.; TOPO_DOM 433 438 Extracellular. {ECO:0000250|UniProtKB:P43427}.; TOPO_DOM 460 501 Cytoplasmic. {ECO:0000250|UniProtKB:P43427}. FUNCTION: Functions as a fructose transporter that has only low activity with other monosaccharides (PubMed:12031501, PubMed:19091748). Can mediate the uptake of deoxyglucose, but with low efficiency (By similarity). Essential for fructose uptake in the small intestine (PubMed:19091748, PubMed:26071406). Plays a role in the regulation of salt uptake and blood pressure in response to dietary fructose. Required for the development of high blood pressure in response to high dietary fructose intake (PubMed:19091748). {ECO:0000250|UniProtKB:P43427, ECO:0000269|PubMed:12031501, ECO:0000269|PubMed:19091748, ECO:0000269|PubMed:26071406}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:18496516, ECO:0000269|PubMed:19091748, ECO:0000269|PubMed:26071406}; Multi-pass membrane protein {ECO:0000269|PubMed:18496516}. Cell membrane {ECO:0000269|PubMed:12031501, ECO:0000269|PubMed:19091748}; Multi-pass membrane protein {ECO:0000305}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P43427}. Note=Localized on the apical membrane of jejunum villi, but also on lateral plasma membranes of the villi (PubMed:18496516, PubMed:26071406). Transport to the cell membrane is dependent on RAB11A (PubMed:26071406). {ECO:0000269|PubMed:18496516, ECO:0000269|PubMed:26071406}. TISSUE SPECIFICITY: Detected at the apical membrane of villi in the jejunum (PubMed:18496516, PubMed:19091748, PubMed:26071406). Detected in jejunum mucosa (PubMed:26071406). Detected in epididymis and whole testis (at protein level) (PubMed:18417103). Detected in small intestine, kidney and testis (PubMed:12031501, PubMed:18417103, PubMed:19091748). Detected in cochlea, but not in inner or outer cochlear hair cells (PubMed:18417103). {ECO:0000269|PubMed:12031501, ECO:0000269|PubMed:18417103, ECO:0000269|PubMed:18496516, ECO:0000269|PubMed:19091748}. +Q32M07 KAD8_MOUSE Adenylate kinase 8 (AK 8) (EC 2.7.4.3) (EC 2.7.4.6) (ATP-AMP transphosphorylase 8) 479 55,073 Binding site (4); Chain (1); Nucleotide binding (5); Region (6); Sequence conflict (1) FUNCTION: Nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. Has highest activity toward AMP, and weaker activity toward dAMP, CMP and dCMP. Also displays broad nucleoside diphosphate kinase activity. {ECO:0000250|UniProtKB:Q96MA6}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q96MA6}. +P43081 GUC1A_MOUSE Guanylyl cyclase-activating protein 1 (GCAP 1) (Guanylate cyclase activator 1A) 202 22,986 Calcium binding (3); Chain (1); Domain (4); Initiator methionine (1); Lipidation (1); Modified residue (1); Sequence conflict (3) FUNCTION: Stimulates retinal guanylyl cyclase when free calcium ions concentration is low and inhibits guanylyl cyclase when free calcium ions concentration is elevated. This Ca(2+)-sensitive regulation of retinal guanylyl cyclase is a key event in recovery of the dark state of rod photoreceptors following light exposure. {ECO:0000250|UniProtKB:P46065}. SUBCELLULAR LOCATION: Membrane; Lipid-anchor. DOMAIN: Binds three calcium ions (via EF-hands 2, 3 and 4) when calcium levels are high. Binds Mg(2+) when calcium levels are low. {ECO:0000250|UniProtKB:P46065}. TISSUE SPECIFICITY: Retina; rod and cone outer segments. +P33680 GUC2A_MOUSE Guanylin (Guanylate cyclase activator 2A) 116 12,467 Disulfide bond (3); Peptide (1); Propeptide (1); Signal peptide (1) FUNCTION: Endogenous activator of intestinal guanylate cyclase. It stimulates this enzyme through the same receptor binding region as the heat-stable enterotoxins. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Localized in both crypts and villi in the small intestine and to superficial epithelial cells in the colon. +Q5SDA5 GUC2F_MOUSE Retinal guanylyl cyclase 2 (EC 4.6.1.2) 1108 124,425 Chain (1); Disulfide bond (3); Domain (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 470 490 Helical. {ECO:0000255}. TOPO_DOM 51 469 Extracellular. {ECO:0000255}.; TOPO_DOM 491 1108 Cytoplasmic. {ECO:0000255}. FUNCTION: Probably plays a specific functional role in the rods and/or cones of photoreceptors. It may be the enzyme involved in the resynthesis of cGMP required for recovery of the dark state after phototransduction (By similarity). {ECO:0000250}. PTM: There are 9 conserved cysteine residues in sensory guanylate cyclases, 6 in the extracellular domain, which may be involved in intra- or interchain disulfide bonds. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. DOMAIN: The protein kinase domain is predicted to be catalytically inactive. +Q8C3X4 GUF1_MOUSE Translation factor Guf1, mitochondrial (EC 3.6.5.-) (Elongation factor 4 homolog) (EF-4) (GTPase Guf1) (Ribosomal back-translocase) 651 72,463 Alternative sequence (1); Chain (1); Domain (1); Nucleotide binding (3); Transit peptide (1) FUNCTION: Promotes mitochondrial protein synthesis. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Binds to mitochondrial ribosomes in a GTP-dependent manner. {ECO:0000255|HAMAP-Rule:MF_03137}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03137}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03137}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03137}. +Q8C0P0 GWL_MOUSE Serine/threonine-protein kinase greatwall (GW) (GWL) (EC 2.7.11.1) (Microtubule-associated serine/threonine-protein kinase-like) (MAST-L) 865 95,975 Active site (1); Alternative sequence (2); Binding site (1); Chain (1); Domain (2); Erroneous initiation (2); Erroneous termination (1); Modified residue (15); Nucleotide binding (1); Sequence conflict (17) FUNCTION: Serine/threonine kinase that plays a key role in M phase by acting as a regulator of mitosis entry and maintenance. Acts by promoting the inactivation of protein phosphatase 2A (PP2A) during M phase: does not directly inhibit PP2A but acts by mediating phosphorylation and subsequent activation of ARPP19 and ENSA at 'Ser-62' and 'Ser-67', respectively. ARPP19 and ENSA are phosphatase inhibitors that specifically inhibit the PPP2R2D (PR55-delta) subunit of PP2A. Inactivation of PP2A during M phase is essential to keep cyclin-B1-CDK1 activity high. Following DNA damage, it is also involved in checkpoint recovery by being inhibited (By similarity). {ECO:0000250, ECO:0000269|PubMed:21156286}. PTM: Phosphorylation at Thr-727 by CDK1 during M phase activates its kinase activity. Maximum phosphorylation occurs in prometaphase (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Nucleus. Note=During interphase is mainly nuclear, upon nuclear envelope breakdown localizes at the cytoplasm and during mitosis at the centrosomes. {ECO:0000250}. +Q9CQ70 H2AB1_MOUSE Histone H2A-Bbd type 1 (H2A Barr body-deficient) (H2A.Bbd) (Histone H2A-like 2) (H2A.L.2) (H2AL2) (Histone H2Alike 2) (Testis-specific expressed gene 1 protein) (TSEG-1) 111 12,843 Chain (1); Sequence conflict (1) FUNCTION: Atypical histone H2A which replaces conventional H2A during late spermatogenesis and is involved in the replacement of histones to protamine in male germ cells (PubMed:28366643). Core component of nucleosome: nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template (PubMed:19506029). Nucleosomes containing H2AFB1 only wrap 130 bp of DNA, compared to 147 bp for classical nucleosomes (PubMed:19506029). In condensing spermatids, the heterodimer between H2AFB1 and HIST1H2BA/TH2B is loaded onto the nucleosomes and promotes loading of transition proteins (TNP1 and TNP2) onto the nucleosomes (PubMed:28366643). Inclusion of the H2AFB1-HIST1H2BA/TH2B dimer into chromatin opens the nucleosomes, releasing the nucleosomal DNA ends and allowing the invasion of nucleosomes by transition proteins (TNP1 and TNP2) (PubMed:28366643). Then, transition proteins drive the recruitment and processing of protamines, which are responsible for histone eviction (PubMed:28366643). {ECO:0000269|PubMed:19506029, ECO:0000269|PubMed:28366643}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17261847}. Chromosome {ECO:0000269|PubMed:17261847}. Note=Specifically localizes to the pericentric regions in condensing spermatids (PubMed:17261847). {ECO:0000269|PubMed:17261847}. SUBUNIT: The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers (PubMed:19506029). Incorporated into nucleosomes during late spermatogenesis (PubMed:19506029). Interacts with HIST1H2BA/TH2B; preferentially dimerizes with HIST1H2BA/TH2B to form nucleosomes (PubMed:17261847, PubMed:28366643). {ECO:0000269|PubMed:17261847, ECO:0000269|PubMed:19506029, ECO:0000269|PubMed:28366643}. TISSUE SPECIFICITY: Highly expressed in adult testis, mainly in spermatocytes (PubMed:20008104, PubMed:20188161, PubMed:17261847). {ECO:0000269|PubMed:17261847, ECO:0000269|PubMed:20008104, ECO:0000269|PubMed:20188161}. +Q8BFU2 H2A3_MOUSE Histone H2A type 3 130 14,121 Chain (1); Cross-link (3); Initiator methionine (1); Modified residue (23) FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. PTM: Deiminated on Arg-4 in granulocytes upon calcium entry. {ECO:0000250|UniProtKB:P0C0S8}.; PTM: Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM27 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is involved in the initiation of both imprinted and random X inactivation. Ubiquitinated H2A is enriched in inactive X chromosome chromatin. Ubiquitination of H2A functions downstream of methylation of 'Lys-27' of histone H3 (H3K27me). H2AK119Ub by RNF2/RING2 can also be induced by ultraviolet and may be involved in DNA repair. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties by the E2 ligase UBE2N and the E3 ligases RNF8 and RNF168, leading to the recruitment of repair proteins to sites of DNA damage. Ubiquitination at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) in response to DNA damage is initiated by RNF168 that mediates monoubiquitination at these 2 sites, and 'Lys-63'-linked ubiquitin are then conjugated to monoubiquitin; RNF8 is able to extend 'Lys-63'-linked ubiquitin chains in vitro. Deubiquitinated by USP51 at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) after damaged DNA is repaired (By similarity). H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination (H2AK13Ub and H2AK15Ub) are distinct events. {ECO:0000250|UniProtKB:P0C0S8, ECO:0000269|PubMed:15509584, ECO:0000269|PubMed:15525528, ECO:0000269|PubMed:24352239}.; PTM: Phosphorylation on Ser-2 (H2AS1ph) is enhanced during mitosis. Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses transcription. Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1. Phosphorylation at Thr-121 (H2AT120ph) by DCAF1 is present in the regulatory region of many tumor suppresor genes and down-regulates their transcription. {ECO:0000250|UniProtKB:P0C0S8}.; PTM: Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage. {ECO:0000269|PubMed:16699504}.; PTM: Glutamine methylation at Gln-105 (H2AQ104me) by FBL is specifically dedicated to polymerase I. It is present at 35S ribosomal DNA locus and impairs binding of the FACT complex. {ECO:0000269|PubMed:24352239}.; PTM: Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes. {ECO:0000269|PubMed:21925322}.; PTM: Hydroxybutyrylation of histones is induced by starvation. {ECO:0000269|PubMed:27105115}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}. SUBUNIT: The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. +Q8CGP0 H2B3B_MOUSE Histone H2B type 3-B 126 13,908 Chain (1); Cross-link (4); Erroneous initiation (2); Initiator methionine (1); Modified residue (52) FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. PTM: Monoubiquitination at Lys-35 (H2BK34Ub) by the MSL1/MSL2 dimer is required for histone H3 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) methylation and transcription activation at specific gene loci, such as HOXA9 and MEIS1 loci. Similarly, monoubiquitination at Lys-121 (H2BK120Ub) by the RNF20/40 complex gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation. It also functions cooperatively with the FACT dimer to stimulate elongation by RNA polymerase II. H2BK120Ub also acts as a regulator of mRNA splicing: deubiquitination by USP49 is required for efficient cotranscriptional splicing of a large set of exons (By similarity). {ECO:0000250|UniProtKB:P33778}.; PTM: Phosphorylated on Ser-15 (H2BS14ph) by STK4/MST1 during apoptosis; which facilitates apoptotic chromatin condensation. Also phosphorylated on Ser-15 in response to DNA double strand breaks (DSBs), and in correlation with somatic hypermutation and immunoglobulin class-switch recombination. Phosphorylation at Ser-37 (H2BS36ph) by AMPK in response to stress promotes transcription. {ECO:0000269|PubMed:15197225, ECO:0000269|PubMed:16039583, ECO:0000269|PubMed:20647423}.; PTM: Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes. {ECO:0000269|PubMed:21925322}.; PTM: Hydroxybutyrylation of histones is induced by starvation. {ECO:0000269|PubMed:27105115}. SUBCELLULAR LOCATION: Nucleus. Chromosome. SUBUNIT: The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. +P10854 H2B1M_MOUSE Histone H2B type 1-M (H2B 291B) 126 13,936 Chain (1); Cross-link (4); Glycosylation (1); Initiator methionine (1); Modified residue (53) FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. PTM: Monoubiquitination at Lys-35 (H2BK34Ub) by the MSL1/MSL2 dimer is required for histone H3 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) methylation and transcription activation at specific gene loci, such as HOXA9 and MEIS1 loci. Similarly, monoubiquitination at Lys-121 (H2BK120Ub) by the RNF20/40 complex gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation. It also functions cooperatively with the FACT dimer to stimulate elongation by RNA polymerase II. H2BK120Ub also acts as a regulator of mRNA splicing: deubiquitination by USP49 is required for efficient cotranscriptional splicing of a large set of exons (By similarity). {ECO:0000250|UniProtKB:P33778}.; PTM: Phosphorylated on Ser-15 (H2BS14ph) by STK4/MST1 during apoptosis; which facilitates apoptotic chromatin condensation. Also phosphorylated on Ser-15 in response to DNA double strand breaks (DSBs), and in correlation with somatic hypermutation and immunoglobulin class-switch recombination. Phosphorylation at Ser-37 (H2BS36ph) by AMPK in response to stress promotes transcription. {ECO:0000269|PubMed:15197225, ECO:0000269|PubMed:16039583, ECO:0000269|PubMed:20647423}.; PTM: GlcNAcylation at Ser-113 promotes monoubiquitination of Lys-121. It fluctuates in response to extracellular glucose, and associates with transcribed genes (By similarity). {ECO:0000250|UniProtKB:P62807}.; PTM: Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes. {ECO:0000269|PubMed:21925322}.; PTM: ADP-ribosylated on Ser-7 in response to DNA damage. {ECO:0000250|UniProtKB:Q99879}.; PTM: Hydroxybutyrylation of histones is induced by starvation. {ECO:0000269|PubMed:27105115}. SUBCELLULAR LOCATION: Nucleus. Chromosome. SUBUNIT: The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. +P84228 H32_MOUSE Histone H3.2 136 15,388 Beta strand (1); Chain (1); Erroneous initiation (2); Lipidation (1); Modified residue (87) FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. PTM: Acetylation is generally linked to gene activation. Acetylation on Lys-10 (H3K9ac) impairs methylation at Arg-9 (H3R8me2s). Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac) favors methylation at Arg-18 (H3R17me). Acetylation at Lys-123 (H3K122ac) by EP300/p300 plays a central role in chromatin structure: localizes at the surface of the histone octamer and stimulates transcription, possibly by promoting nucleosome instability. {ECO:0000269|PubMed:11751582, ECO:0000269|PubMed:12498683, ECO:0000269|PubMed:13678296, ECO:0000269|PubMed:15485929, ECO:0000269|PubMed:15616592, ECO:0000269|PubMed:17194708}.; PTM: Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by PADI4 impairs methylation and represses transcription. {ECO:0000269|PubMed:11751582, ECO:0000269|PubMed:12498683, ECO:0000269|PubMed:15339660, ECO:0000269|PubMed:15485929, ECO:0000269|PubMed:15616592}.; PTM: Asymmetric dimethylation at Arg-18 (H3R17me2a) by CARM1 is linked to gene activation. Symmetric dimethylation at Arg-9 (H3R8me2s) by PRMT5 is linked to gene repression. Asymmetric dimethylation at Arg-3 (H3R2me2a) by PRMT6 is linked to gene repression and is mutually exclusive with H3 Lys-5 methylation (H3K4me2 and H3K4me3). H3R2me2a is present at the 3' of genes regardless of their transcription state and is enriched on inactive promoters, while it is absent on active promoters (By similarity). {ECO:0000250}.; PTM: Methylation at Lys-5 (H3K4me), Lys-37 (H3K36me) and Lys-80 (H3K79me) are linked to gene activation. Methylation at Lys-5 (H3K4me) facilitates subsequent acetylation of H3 and H4. Methylation at Lys-80 (H3K79me) is associated with DNA double-strand break (DSB) responses and is a specific target for TP53BP1. Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are linked to gene repression. Methylation at Lys-10 (H3K9me) is a specific target for HP1 proteins (CBX1, CBX3 and CBX5) and prevents subsequent phosphorylation at Ser-11 (H3S10ph) and acetylation of H3 and H4. Methylation at Lys-5 (H3K4me) and Lys-80 (H3K79me) require preliminary monoubiquitination of H2B at 'Lys-120'. Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are enriched in inactive X chromosome chromatin. Monomethylation at Lys-57 (H3K56me1) by EHMT2/G9A in G1 phase promotes interaction with PCNA and is required for DNA replication. {ECO:0000269|PubMed:10464286, ECO:0000269|PubMed:11856369, ECO:0000269|PubMed:13678296, ECO:0000269|PubMed:15485929, ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:15735677, ECO:0000269|PubMed:15870105, ECO:0000269|PubMed:17189264, ECO:0000269|PubMed:17194708}.; PTM: Phosphorylated at Thr-4 (H3T3ph) by HASPIN during prophase and dephosphorylated during anaphase. Phosphorylation at Ser-11 (H3S10ph) by AURKB is crucial for chromosome condensation and cell-cycle progression during mitosis and meiosis. In addition phosphorylation at Ser-11 (H3S10ph) by RPS6KA4 and RPS6KA5 is important during interphase because it enables the transcription of genes following external stimulation, like mitogens, stress, growth factors or UV irradiation and result in the activation of genes, such as c-fos and c-jun. Phosphorylation at Ser-11 (H3S10ph), which is linked to gene activation, prevents methylation at Lys-10 (H3K9me) but facilitates acetylation of H3 and H4. Phosphorylation at Ser-11 (H3S10ph) by AURKB mediates the dissociation of HP1 proteins (CBX1, CBX3 and CBX5) from heterochromatin. Phosphorylation at Ser-11 (H3S10ph) is also an essential regulatory mechanism for neoplastic cell transformation. Phosphorylated at Ser-29 (H3S28ph) by MAP3K20 isoform 1, RPS6KA5 or AURKB during mitosis or upon ultraviolet B irradiation. Phosphorylation at Thr-7 (H3T6ph) by PRKCB is a specific tag for epigenetic transcriptional activation that prevents demethylation of Lys-5 (H3K4me) by LSD1/KDM1A. At centromeres, specifically phosphorylated at Thr-12 (H3T11ph) from prophase to early anaphase, by DAPK3 and PKN1. Phosphorylation at Thr-12 (H3T11ph) by PKN1 is a specific tag for epigenetic transcriptional activation that promotes demethylation of Lys-10 (H3K9me) by KDM4C/JMJD2C. Phosphorylation at Tyr-42 (H3Y41ph) by JAK2 promotes exclusion of CBX5 (HP1 alpha) from chromatin. {ECO:0000269|PubMed:10464286, ECO:0000269|PubMed:11441012, ECO:0000269|PubMed:11856369, ECO:0000269|PubMed:13678296, ECO:0000269|PubMed:15485929, ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:15684425, ECO:0000269|PubMed:15735677, ECO:0000269|PubMed:15870105, ECO:0000269|PubMed:17194708}.; PTM: Ubiquitinated by the CUL4-DDB-RBX1 complex in response to ultraviolet irradiation. This may weaken the interaction between histones and DNA and facilitate DNA accessibility to repair proteins (By similarity). Monoubiquitinated by RAG1 in lymphoid cells, monoubiquitination is required for V(D)J recombination. {ECO:0000250, ECO:0000269|PubMed:20122409}.; PTM: Lysine deamination at Lys-5 (H3K4all) to form allysine is mediated by LOXL2. Allysine formation by LOXL2 only takes place on H3K4me3 and results in gene repression (By similarity). {ECO:0000250}.; PTM: Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes. {ECO:0000269|PubMed:21925322}.; PTM: Butyrylation of histones marks active promoters and competes with histone acetylation. It is present during late spermatogenesis. {ECO:0000269|PubMed:27105113}.; PTM: Hydroxybutyrylation of histones is induced by starvation. It is linked to gene activation and may replace histone acetylation on the promoter of specific genes in response to fasting. {ECO:0000269|PubMed:27105115}.; PTM: Succinylation at Lys-80 (H3K79succ) by KAT2A takes place with a maximum frequency around the transcription start sites of genes. It gives a specific tag for epigenetic transcription activation. {ECO:0000250|UniProtKB:Q71DI3}.; PTM: Serine ADP-ribosylation constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage. Serine ADP-ribosylation at Ser-11 (H3S10ADPr) is mutually exclusive with phosphorylation at Ser-11 (H3S10ph) and impairs acetylation at Lys-10 (H3K9ac). {ECO:0000250|UniProtKB:P68431}. SUBCELLULAR LOCATION: Nucleus. Chromosome. SUBUNIT: The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. During nucleosome assembly the chaperone ASF1A interacts with the histone H3-H4 heterodimer (By similarity). {ECO:0000250|UniProtKB:Q71DI3}. +P14432 HA1T_MOUSE H-2 class I histocompatibility antigen, TLA(B) alpha chain (MHC thymus leukemia antigen) 384 43,479 Beta strand (18); Chain (1); Disulfide bond (2); Domain (1); Frameshift (1); Glycosylation (4); Helix (7); Natural variant (3); Region (4); Sequence conflict (18); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (2) TRANSMEM 315 334 Helical. {ECO:0000255}. TOPO_DOM 27 314 Extracellular. {ECO:0000255}.; TOPO_DOM 335 384 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in the presentation of foreign antigens to the immune system. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2-microglobulin). TISSUE SPECIFICITY: TL antigens are only expressed on thymocytes, activated T-lymphocytes and on some thymic leukemias. +P01896 HA1Z_MOUSE H-2 class I histocompatibility antigen, alpha chain (Clone PH-2D-2) (Fragment) 185 20,454 Chain (1); Domain (1); Glycosylation (2); Non-terminal residue (1); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 119 139 Helical. {ECO:0000255}. TOPO_DOM <1 118 Extracellular. {ECO:0000255}.; TOPO_DOM 140 185 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in the presentation of foreign antigens to the immune system. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2-microglobulin). +Q9QYK5 H6ST1_MOUSE Heparan-sulfate 6-O-sulfotransferase 1 (HS6ST-1) (mHS6ST-1) (EC 2.8.2.-) 411 48,302 Active site (1); Binding site (7); Chain (1); Coiled coil (1); Compositional bias (1); Erroneous initiation (2); Glycosylation (2); Region (4); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 20 37 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 19 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 38 411 Lumenal. {ECO:0000255}. FUNCTION: 6-O-sulfation enzyme which catalyzes the transfer of sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to position 6 of the N-sulfoglucosamine residue (GlcNS) of heparan sulfate. Critical for normal neuronal development where it may play a role in neuron branching. May also play a role in limb development. May prefer iduronic acid. {ECO:0000269|PubMed:10644753}. PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in fetal brain and liver. {ECO:0000269|PubMed:10644753}. +Q80UW0 H6ST2_MOUSE Heparan-sulfate 6-O-sulfotransferase 2 (HS6ST-2) (mHS6ST-2) (EC 2.8.2.-) 612 69,198 Active site (1); Alternative sequence (2); Binding site (7); Chain (1); Erroneous initiation (1); Glycosylation (8); Region (4); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 5 27 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 4 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 28 612 Lumenal. {ECO:0000255}. FUNCTION: 6-O-sulfation enzyme which catalyzes the transfer of sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to position 6 of the N-sulfoglucosamine residue (GlcNS) of heparan sulfate. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. +P04224 HA22_MOUSE H-2 class II histocompatibility antigen, E-K alpha chain 255 29,121 Beta strand (14); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (1); Helix (2); Region (3); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (3) TRANSMEM 217 242 Helical. {ECO:0000255}. TOPO_DOM 26 216 Extracellular. {ECO:0000255}.; TOPO_DOM 243 255 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +P14439 HA23_MOUSE H-2 class II histocompatibility antigen, E-U alpha chain 255 29,108 Chain (1); Disulfide bond (1); Domain (1); Glycosylation (1); Region (3); Sequence conflict (6); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 218 238 Helical. {ECO:0000255}. TOPO_DOM 26 217 Extracellular. {ECO:0000255}.; TOPO_DOM 239 255 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +P14434 HA2B_MOUSE H-2 class II histocompatibility antigen, A-B alpha chain (IAalpha) 256 28,093 Beta strand (14); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (1); Helix (2); Region (3); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (4) TRANSMEM 219 244 Helical. {ECO:0000255}. TOPO_DOM 24 218 Extracellular. {ECO:0000255}.; TOPO_DOM 245 256 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +P23150 HA2J_MOUSE H-2 class II histocompatibility antigen, I-E alpha chain (Fragment) 254 28,013 Chain (1); Disulfide bond (1); Domain (1); Glycosylation (2); Non-terminal residue (1); Region (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 217 242 Helical. {ECO:0000255}. TOPO_DOM 25 216 Extracellular. {ECO:0000255}.; TOPO_DOM 243 254 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q9QY80 HACD1_MOUSE Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 1 (EC 4.2.1.134) (3-hydroxyacyl-CoA dehydratase 1) (HACD1) (Protein-tyrosine phosphatase-like member A) 281 32,327 Active site (2); Chain (1); Glycosylation (1); Topological domain (7); Transmembrane (6) TRANSMEM 69 88 Helical. {ECO:0000255}.; TRANSMEM 108 124 Helical. {ECO:0000255}.; TRANSMEM 135 152 Helical. {ECO:0000255}.; TRANSMEM 159 173 Helical. {ECO:0000255}.; TRANSMEM 197 214 Helical. {ECO:0000255}.; TRANSMEM 245 262 Helical. {ECO:0000255}. TOPO_DOM 1 68 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 89 107 Lumenal. {ECO:0000255}.; TOPO_DOM 125 134 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 153 158 Lumenal. {ECO:0000255}.; TOPO_DOM 174 196 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 215 244 Lumenal. {ECO:0000255}.; TOPO_DOM 263 281 Cytoplasmic. {ECO:0000255}. Lipid metabolism; fatty acid biosynthesis. FUNCTION: Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. Thereby, it participates in the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. {ECO:0000250|UniProtKB:B0YJ81}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:B0YJ81}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:B0YJ81}; Multi-pass membrane protein {ECO:0000250|UniProtKB:B0YJ81}. SUBUNIT: May interact with enzymes of the ELO family (including ELOVL1); with those enzymes that mediate condensation, the first of the four steps of the reaction cycle responsible for fatty acids elongation, may be part of a larger fatty acids elongase complex. {ECO:0000250|UniProtKB:B0YJ81}. TISSUE SPECIFICITY: Expressed at high levels in heart, skeletal muscle and testis, weak expression in kidney and liver. {ECO:0000269|PubMed:10644438}. +Q9D3B1 HACD2_MOUSE Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 2 (EC 4.2.1.134) (3-hydroxyacyl-CoA dehydratase 2) (HACD2) (Protein-tyrosine phosphatase-like member B) 254 28,402 Active site (2); Chain (1); Compositional bias (1); Glycosylation (1); Initiator methionine (1); Modified residue (1); Sequence conflict (3); Topological domain (7); Transmembrane (6) TRANSMEM 42 60 Helical. {ECO:0000255}.; TRANSMEM 80 97 Helical. {ECO:0000255}.; TRANSMEM 108 125 Helical. {ECO:0000255}.; TRANSMEM 131 146 Helical. {ECO:0000255}.; TRANSMEM 170 187 Helical. {ECO:0000255}.; TRANSMEM 218 235 Helical. {ECO:0000255}. TOPO_DOM 2 41 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 61 79 Lumenal. {ECO:0000255}.; TOPO_DOM 98 107 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 126 130 Lumenal. {ECO:0000255}.; TOPO_DOM 147 169 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 188 217 Lumenal. {ECO:0000255}.; TOPO_DOM 236 254 Cytoplasmic. {ECO:0000255}. Lipid metabolism; fatty acid biosynthesis. FUNCTION: Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. Thereby, it participates in the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. {ECO:0000250|UniProtKB:Q6Y1H2}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q6Y1H2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q6Y1H2}. SUBUNIT: May interact with enzymes of the ELO family (including ELOVL1); with those enzymes that mediate condensation, the first of the four steps of the reaction cycle responsible for fatty acids elongation, may be part of a larger fatty acids elongase complex. Interacts with BCAP31. {ECO:0000250|UniProtKB:Q6Y1H2}. +Q9JKS5 HABP4_MOUSE Intracellular hyaluronan-binding protein 4 (IHABP-4) (IHABP4) (Hyaluronic acid-binding protein 4) 411 45,924 Chain (1); Coiled coil (2); Cross-link (6); Modified residue (7); Sequence caution (1); Sequence conflict (4) FUNCTION: RNA-binding protein that plays a role in the regulation of transcription, pre-mRNA splicing and mRNA translation. Negatively regulates DNA-binding activity of the transcription factor MEF2C in myocardial cells in response to mechanical stress. Plays a role in pre-mRNA splicing regulation. Binds (via C-terminus) to poly(U) RNA. Involved in mRNA translation regulation, probably at the initiation step. Seems to play a role in PML-nuclear bodies formation (By similarity). {ECO:0000250|UniProtKB:A1L1K8, ECO:0000250|UniProtKB:Q5JVS0}. PTM: Phosphorylated by phorbol 12-myristate 13-acetate (PMA)-activated PKC isoforms at Thr-352 and Thr-373. {ECO:0000250|UniProtKB:Q5JVS0}.; PTM: Methylated. Methylation is decreased by phorbol 12-myristate 13-acetate (PMA)-activated PKC, in vitro. {ECO:0000250|UniProtKB:Q5JVS0}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5JVS0}. Cytoplasm {ECO:0000250|UniProtKB:Q5JVS0}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q5JVS0}. Cytoplasm, sarcoplasm {ECO:0000250|UniProtKB:A1L1K8}. Nucleus, Nuclear body {ECO:0000250|UniProtKB:Q5JVS0}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q5JVS0}. Nucleus speckle {ECO:0000250|UniProtKB:Q5JVS0}. Nucleus, Cajal body {ECO:0000250|UniProtKB:Q5JVS0}. Nucleus, gem {ECO:0000250|UniProtKB:Q5JVS0}. Note=Transported into the nuclear compartment in activated leukocytes. Inhibition of methylation alters its distribution between the nuclear and cytoplasmic compartments. Methylation may be required for its localization in subnuclear structures, such as nucleoli, nuclear speckles, Cajal bodies and Gemini of coiled bodies (gems). Colocalizes with FMR1, FXR1 and FXR2 in cytoplasmic stress granules. In myocardial cells, localization at the sarcoplasm is reduced in response to mechanical stress. {ECO:0000250|UniProtKB:A1L1K8, ECO:0000250|UniProtKB:Q5JVS0}. SUBUNIT: Associates with polysomes. Interacts with FMR1. Interacts with FXR1 and FXR2. Interacts with CHD3 (via C-terminus). Interacts (via C-terminus) with RACK1. Interacts with p53/TP53 (By similarity). Interacts (via N-terminus) with SRSF9; this interaction is direct (PubMed:19523114). Interacts with SYNCRIP; this interaction is direct. Interacts with MEF2C (via N-terminus); this interaction decreases DNA-binding activity of MEF2C in myocardial cells in response to mechanical stress. Interacts with PRMT1 (via N-terminus) (By similarity). Interacts with SPIN1 (PubMed:23894536). {ECO:0000250|UniProtKB:Q5JVS0, ECO:0000269|PubMed:19523114, ECO:0000269|PubMed:23894536}. DOMAIN: The C-terminal region is necessary for nucleus and cytoplasmic localization. The N-terminal region is necessary for nucleus and nuclear bodies localization. Regions containing Arg-Gly-Gly repeats (RGG/RXR-box) may be preferentially methylated by PRMT1. {ECO:0000250|UniProtKB:Q5JVS0}. TISSUE SPECIFICITY: Expressed in adult heart, brain, liver, kidney, testis, and in various embryonic tissues, but not in adult spleen, lung or skeletal muscle. {ECO:0000269|PubMed:10887182}. +Q61645 HAIR_MOUSE Lysine-specific demethylase hairless (EC 1.14.11.-) 1182 127,193 Chain (1); Compositional bias (1); Domain (1); Metal binding (3); Motif (2); Sequence conflict (1); Zinc finger (1) FUNCTION: Histone demethylase that specifically demethylates both mono- and dimethylated 'Lys-9' of histone H3. May act as a transcription regulator controlling hair biology (via targeting of collagens), neural activity, and cell cycle (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. DOMAIN: Contains two Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs. The LXXLL motifs are essential for the association with nuclear receptors (By similarity). {ECO:0000250}.; DOMAIN: The JmjC domain and the C6-type zinc-finger are required for the demethylation activity. {ECO:0000250}. TISSUE SPECIFICITY: Expressed predominantly in brain, hair follicles and interfollicular epidermis. No expression in dermis. DISEASE: Note=Defects in Hr are the cause of a number of pleiotropic effects including structural abnormalities of epithelial cells in the hair follicles, hair loss towards the end of the first hair growth cycle, and the failure of subsequent hair growth cycles. Older mice carrying a hr mutation have been reported to possess altered ratios of T-cell-dependent B-cell responses. Mice homozygous for hr mutation are uniquely sensitive to UV and chemically induced skin tumors. +Q9JIY2 HAKAI_MOUSE E3 ubiquitin-protein ligase Hakai (EC 2.3.2.27) (Casitas B-lineage lymphoma-transforming sequence-like protein 1) (c-Cbl-like protein 1) (E-cadherin binding protein E7) (RING-type E3 ubiquitin transferase Hakai) 491 54,444 Alternative sequence (5); Beta strand (3); Chain (1); Compositional bias (1); Frameshift (1); Helix (3); Modified residue (3); Region (1); Turn (4); Zinc finger (2) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination of several tyrosine-phosphorylated Src substrates, including CDH1, CTTN and DOK1 (PubMed:11836526, PubMed:22252131). Targets CDH1 for endocytosis and degradation (PubMed:11836526). Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing (PubMed:29535189, PubMed:29547716). Its function in the WMM complex is unknown (PubMed:29535189, PubMed:29547716). {ECO:0000269|PubMed:11836526, ECO:0000269|PubMed:22252131, ECO:0000269|PubMed:29535189, ECO:0000269|PubMed:29547716}. PTM: Phosphorylated on tyrosine residues. {ECO:0000269|PubMed:11836526}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q75N03}. Nucleus, nucleoplasm {ECO:0000269|PubMed:29547716}. Cytoplasm {ECO:0000269|PubMed:29547716}. Note=Mainly nuclear with some fraction located in the cytoplasm (PubMed:29547716). ZC3H13 is required to anchor component of the MACOM subcomplex, such as VIRMA, in the nucleus (PubMed:29547716). {ECO:0000269|PubMed:29547716}. SUBUNIT: Homodimer (PubMed:22252131). Interacts with tyrosine-phosphorylated SRC substrates (PubMed:11836526, PubMed:22252131). Component of the WMM complex, a N6-methyltransferase complex composed of a catalytic subcomplex, named MAC, and of an associated subcomplex, named MACOM (PubMed:29535189, PubMed:29547716). The MAC subcomplex is composed of METTL3 and METTL14 (PubMed:29535189, PubMed:29547716). The MACOM subcomplex is composed of WTAP, ZC3H13, CBLL1/HAKAI, VIRMA, and, in some cases of RBM15 (RBM15 or RBM15B) (PubMed:29535189, PubMed:29547716). Also component of a MACOM-like complex, named WTAP complex, composed of WTAP, ZC3H13, CBLL1, VIRMA, RBM15, BCLAF1 and THRAP3 (By similarity). {ECO:0000250|UniProtKB:Q75N03, ECO:0000269|PubMed:11836526, ECO:0000269|PubMed:22252131, ECO:0000269|PubMed:29535189, ECO:0000269|PubMed:29547716}. DOMAIN: The HYB domain forms a phosphotyrosine-binding pocket upon dimerization, and mediates as well the recognition of its flanking acidic amino acids. {ECO:0000269|PubMed:22252131}. TISSUE SPECIFICITY: Detected in heart, brain, spleen, lung, liver, skeletal muscle, kidney and testis. {ECO:0000269|PubMed:11836526}. +Q8BR93 HARB1_MOUSE Putative nuclease HARBI1 (EC 3.1.-.-) (Harbinger transposase-derived nuclease) 349 38,713 Alternative sequence (4); Chain (1); Domain (1); Metal binding (4); Sequence conflict (1) FUNCTION: Transposase-derived protein that may have nuclease activity (Potential). Does not have transposase activity (By similarity). {ECO:0000250, ECO:0000305}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Interaction with NAIF1 promotes translocation to the nucleus. {ECO:0000250}. SUBUNIT: Interacts with NAIF1. {ECO:0000250}. TISSUE SPECIFICITY: Detected in adult brain, eye, nerve tissue and lung. Detected in embryo. {ECO:0000269|PubMed:15169610}. +Q9Z0R0 HASP_MOUSE Serine/threonine-protein kinase haspin (EC 2.7.11.1) (Germ cell-specific gene 2 protein) (Haploid germ cell-specific nuclear protein kinase) 754 84,181 Active site (2); Binding site (1); Chain (1); Domain (1); Modified residue (2); Nucleotide binding (4); Sequence conflict (4) FUNCTION: Serine/threonine-protein kinase that phosphorylates histone H3 at 'Thr-3' (H3T3ph) during mitosis. May act through H3T3ph to both position and modulate activation of AURKB and other components of the chromosomal passenger complex (CPC) at centromeres to ensure proper chromatid cohesion, metaphase alignment and normal progression through the cell cycle. {ECO:0000250|UniProtKB:Q8TF76}. PTM: Autophosphorylated on both serine and threonine residues (By similarity). Strongly phosphorylated during mitosis but this does not appear to significantly affect its intrinsic kinase activity. Phosphorylation by AURKB is required for full activity toward histone H3 at 'Ser-3' in mitosis (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q8TF76}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10358056}. Chromosome {ECO:0000250|UniProtKB:Q8TF76}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q8TF76}. Note=Nuclear during interphase and associates with the chromosomes and spindle apparatus during mitosis. {ECO:0000250|UniProtKB:Q8TF76}. TISSUE SPECIFICITY: Expressed in germ cells within the testis of adults and of embryos from day 24 onwards. Also present in adult thymus and weakly expressed in spleen, lung and whole embryo. {ECO:0000269|PubMed:10358056, ECO:0000269|PubMed:11311556, ECO:0000269|PubMed:7957958}. +Q8BHX1 HAUS1_MOUSE HAUS augmin-like complex subunit 1 (Coiled-coil domain-containing protein 5) 278 31,379 Chain (1); Coiled coil (3); Sequence conflict (1) FUNCTION: Contributes to mitotic spindle assembly, maintenance of centrosome integrity and completion of cytokinesis as part of the HAUS augmin-like complex. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. Note=Localizes with the spindle poles in mitotic cells. In interphase, localized at the centrosome and diffusely in the cytoplasm (By similarity). {ECO:0000250}. SUBUNIT: Component of the HAUS augmin-like complex. The complex interacts with the gamma-tubulin ring complex and this interaction is required for spindle assembly. Associates with microtubules. The interaction with microtubules is strong during mitosis, while it is weak or absent during interphase. It is unclear whether this interaction is direct or indirect (By similarity). {ECO:0000250}. +Q9CQS9 HAUS2_MOUSE HAUS augmin-like complex subunit 2 (Centrosomal protein of 27 kDa) (Cep27) 234 26,839 Alternative sequence (1); Chain (1); Coiled coil (2); Sequence conflict (1) FUNCTION: Contributes to mitotic spindle assembly, maintenance of centrosome integrity and completion of cytokinesis as part of the HAUS augmin-like complex. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Localizes to interphase centrosomes and to mitotic spindle microtubules. {ECO:0000250}. SUBUNIT: Component of the HAUS augmin-like complex. The complex interacts with the gamma-tubulin ring complex and this interaction is required for spindle assembly (By similarity). {ECO:0000250}. +Q8BFT2 HAUS4_MOUSE HAUS augmin-like complex subunit 4 363 42,197 Chain (1); Sequence conflict (6) FUNCTION: Contributes to mitotic spindle assembly, maintenance of centrosome integrity and completion of cytokinesis as part of the HAUS augmin-like complex. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Localizes to interphase centrosomes and to mitotic spindle microtubules. {ECO:0000250}. SUBUNIT: Component of the HAUS augmin-like complex. The complex interacts with the gamma-tubulin ring complex and this interaction is required for spindle assembly (By similarity). {ECO:0000250}. +P04230 HB21_MOUSE H-2 class II histocompatibility antigen, E-B beta chain 264 30,166 Beta strand (14); Chain (1); Disulfide bond (2); Domain (1); Glycosylation (1); Helix (5); Region (2); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (2) TRANSMEM 226 246 Helical. {ECO:0000255}. TOPO_DOM 27 225 Extracellular. {ECO:0000255}.; TOPO_DOM 247 264 Cytoplasmic. {ECO:0000255}. PTM: Ubiquitinated in immature dendritic cells leading to down-regulation of MHC class II. {ECO:0000269|PubMed:17051151, ECO:0000269|PubMed:17174123}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +P01915 HB22_MOUSE H-2 class II histocompatibility antigen, E-D beta chain 264 30,049 Chain (1); Disulfide bond (2); Domain (1); Glycosylation (1); Region (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 226 248 Helical. {ECO:0000255}. TOPO_DOM 32 225 Extracellular. {ECO:0000255}.; TOPO_DOM 249 264 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +P04231 HB23_MOUSE H-2 class II histocompatibility antigen, E-S beta chain (Fragment) 232 26,647 Chain (1); Disulfide bond (2); Domain (1); Glycosylation (1); Non-terminal residue (1); Region (2); Topological domain (2); Transmembrane (1) TRANSMEM 194 216 Helical. {ECO:0000255}. TOPO_DOM <1 193 Extracellular. {ECO:0000255}.; TOPO_DOM 217 232 Cytoplasmic. {ECO:0000255}. PTM: Ubiquitinated in immature dendritic cells leading to down-regulation of MHC class II. {ECO:0000269|PubMed:17051151, ECO:0000269|PubMed:17174123}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +P14483 HB2A_MOUSE H-2 class II histocompatibility antigen, A beta chain 265 30,128 Beta strand (13); Chain (1); Disulfide bond (2); Domain (1); Glycosylation (1); Helix (6); Region (3); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (3) TRANSMEM 227 247 Helical. {ECO:0000255}. TOPO_DOM 28 226 Extracellular. {ECO:0000255}.; TOPO_DOM 248 265 Cytoplasmic. {ECO:0000255}. PTM: Ubiquitinated in immature dendritic cells leading to down-regulation of MHC class II. {ECO:0000269|PubMed:17051151, ECO:0000269|PubMed:17174123}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +P01921 HB2D_MOUSE H-2 class II histocompatibility antigen, A-D beta chain 265 29,954 Beta strand (14); Chain (1); Disulfide bond (2); Domain (1); Glycosylation (1); Helix (6); Region (3); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (2) TRANSMEM 227 247 Helical. {ECO:0000255}. TOPO_DOM 28 226 Extracellular. {ECO:0000255}.; TOPO_DOM 248 265 Cytoplasmic. {ECO:0000255}. PTM: Ubiquitinated in immature dendritic cells leading to down-regulation of MHC class II. {ECO:0000269|PubMed:17051151, ECO:0000269|PubMed:17174123}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +P06342 HB2Q_MOUSE H-2 class II histocompatibility antigen, A-Q beta chain 265 29,950 Chain (1); Disulfide bond (2); Domain (1); Glycosylation (1); Region (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 228 247 Helical. {ECO:0000255}. TOPO_DOM 28 227 Extracellular. {ECO:0000255}.; TOPO_DOM 248 265 Cytoplasmic. {ECO:0000255}. PTM: Ubiquitinated in immature dendritic cells leading to down-regulation of MHC class II. {ECO:0000269|PubMed:17051151, ECO:0000269|PubMed:17174123}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +P06345 HB2S_MOUSE H-2 class II histocompatibility antigen, A-S beta chain 263 29,788 Chain (1); Disulfide bond (2); Domain (1); Glycosylation (1); Region (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 225 245 Helical. {ECO:0000255}. TOPO_DOM 28 224 Extracellular. {ECO:0000255}.; TOPO_DOM 246 263 Cytoplasmic. {ECO:0000255}. PTM: Ubiquitinated in immature dendritic cells leading to down-regulation of MHC class II. {ECO:0000269|PubMed:17051151, ECO:0000269|PubMed:17174123}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +P01942 HBA_MOUSE Hemoglobin subunit alpha (Alpha-globin) (Hemoglobin alpha chain) 142 15,085 Beta strand (1); Chain (1); Helix (9); Initiator methionine (1); Metal binding (2); Modified residue (17); Natural variant (5); Turn (2) FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues. SUBUNIT: Heterotetramer of two alpha chains and two beta chains. TISSUE SPECIFICITY: Red blood cells. +P04443 HBB0_MOUSE Hemoglobin subunit beta-H0 (Beta-H0-globin) (Hemoglobin beta-H0 chain) 147 16,384 Chain (1); Metal binding (2); Sequence conflict (4) FUNCTION: This is a minor early embryonic beta chain. SUBUNIT: Heterotetramer of two alpha chains and two beta chains. TISSUE SPECIFICITY: Red blood cells. +A2CG49 KALRN_MOUSE Kalirin (EC 2.7.11.1) (Protein Duo) (Serine/threonine-protein kinase with Dbl- and pleckstrin homology domain) 2964 337,000 Active site (1); Alternative sequence (18); Beta strand (5); Binding site (1); Chain (1); Compositional bias (1); Disulfide bond (1); Domain (10); Helix (1); Modified residue (8); Nucleotide binding (1); Repeat (9); Sequence conflict (5) FUNCTION: Promotes the exchange of GDP by GTP. Activates specific Rho GTPase family members, thereby inducing various signaling mechanisms that regulate neuronal shape, growth, and plasticity, through their effects on the actin cytoskeleton. Induces lamellipodia independent of its GEF activity (By similarity). {ECO:0000250|UniProtKB:P97924}. PTM: Autophosphorylated. {ECO:0000250|UniProtKB:O60229}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O60229, ECO:0000250|UniProtKB:P97924}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O60229, ECO:0000250|UniProtKB:P97924}. SUBUNIT: Interacts with the C-terminal of peptidylglycine alpha-amidating monooxygenase (PAM) and with the huntingtin-associated protein 1 (HAP1). Interacts with FASLG (By similarity). {ECO:0000250}. DOMAIN: The two GEF domains catalyze nucleotide exchange for RAC1 and RhoA which are bound by DH1 and DH2 respectively. The two GEF domains appear to play differing roles in neuronal development and axonal outgrowth. SH3 1 binds to the first GEF domain inhibiting GEF activity only when in the presence of a PXXP peptide, suggesting that the SH3 domain/peptide interaction mediates binding to GEF1. CRK1 SH3 domain binds to and inhibits GEF1 activity (By similarity). {ECO:0000250|UniProtKB:P97924}. +Q8BX02 KANK2_MOUSE KN motif and ankyrin repeat domain-containing protein 2 (Ankyrin repeat domain-containing protein 25) 843 90,245 Alternative sequence (2); Chain (1); Coiled coil (2); Modified residue (10); Region (2); Repeat (5); Sequence conflict (2) FUNCTION: Involved in transcription regulation by sequestering in the cytoplasm nuclear receptor coactivators such as NCOA1, NCOA2 and NCOA3 (By similarity). Involved in regulation of caspase-independent apoptosis by sequestering the proapoptotic factor AIFM1 in mitochondria (By similarity). Pro-apoptotic stimuli can induce its proteasomal degradation allowing the translocation of AIFM1 to the nucleus to induce apoptosis (By similarity). Involved in the negative control of vitamin D receptor signaling pathway (By similarity). Involved in actin stress fibers formation through its interaction with ARHGDIA and the regulation of the Rho signaling pathway (PubMed:25961457). May thereby play a role in cell adhesion and migration, regulating for instance podocytes migration during development of the kidney (PubMed:25961457). Through the Rho signaling pathway may also regulate cell proliferation (PubMed:16024821). {ECO:0000250|UniProtKB:Q63ZY3, ECO:0000269|PubMed:16024821, ECO:0000269|PubMed:25961457}. PTM: Phosphorylated by casein kinase II upon estrogen stimulation (By similarity). Phosphorylation induces the release by KANK2 of NCOA1 and its translocation to the nucleus where NCOA1 can activate gene transcription (By similarity). {ECO:0000250|UniProtKB:Q63ZY3}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q63ZY3}. Mitochondrion {ECO:0000250|UniProtKB:Q63ZY3}. SUBUNIT: Interacts (non-phosphorylated form) with NCOA1; NCOA2 AND NCOA3 (By similarity). Interacts with AIFM1 (By similarity). Interacts with ARHGDIA; the interaction is direct and may regulate the interaction of ARHGDIA with RHOA, RAC1 and CDC42 (By similarity). {ECO:0000250|UniProtKB:Q63ZY3}. TISSUE SPECIFICITY: Widely expressed with highest levels in liver and skeletal muscle. {ECO:0000269|PubMed:20720434}. +Q8R316 HBP1_MOUSE HMG box-containing protein 1 (HMG box transcription factor 1) (High mobility group box transcription factor 1) 516 57,645 Alternative sequence (1); Beta strand (7); Chain (1); Compositional bias (3); DNA binding (1); Domain (1); Erroneous initiation (1); Helix (4); Mutagenesis (2); Turn (4) FUNCTION: Transcriptional repressor that binds to the promoter region of target genes. Plays a role in the regulation of the cell cycle and of the Wnt pathway. Binds preferentially to the sequence 5'-TTCATTCATTCA-3'. Binding to the H1F0 promoter is enhanced by interaction with RB1. Disrupts the interaction between DNA and TCF4 (By similarity). {ECO:0000250|UniProtKB:O60381, ECO:0000269|PubMed:9178770}. PTM: Ubiquitinated by the CTLH E3 ubiquitin-protein ligase complex, leading to subsequent proteasomal degradation. {ECO:0000250|UniProtKB:O60381}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267, ECO:0000269|PubMed:15235594}. SUBUNIT: Binds TCF4 (By similarity). Binds RB1 (PubMed:9178770). Binds the second PAH repeat of SIN3A (PubMed:15235594). {ECO:0000250|UniProtKB:O60381, ECO:0000269|PubMed:15235594, ECO:0000269|PubMed:9178770}. +Q6P9J5 KANK4_MOUSE KN motif and ankyrin repeat domain-containing protein 4 (Ankyrin repeat domain-containing protein 38) 1016 110,404 Chain (1); Coiled coil (1); Compositional bias (2); Modified residue (1); Repeat (5); Sequence conflict (1) FUNCTION: May be involved in the control of cytoskeleton formation by regulating actin polymerization. {ECO:0000250|UniProtKB:Q5T7N3}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q5T7N3}. +Q80TG1 KANL1_MOUSE KAT8 regulatory NSL complex subunit 1 (NSL complex protein NSL1) (Non-specific lethal 1 homolog) 1036 113,179 Alternative sequence (6); Chain (1); Coiled coil (1); Cross-link (2); Modified residue (7); Region (2); Sequence conflict (1) FUNCTION: As part of the NSL complex it is involved in acetylation of nucleosomal histone H4 on several lysine residues and therefore may be involved in the regulation of transcription. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q7Z3B3}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q7Z3B3}. SUBUNIT: Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, KAT8/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Component of the NSL complex at least composed of MOF/KAT8, KANSL1, KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT, WDR5 and HCFC1. Interacts with KAT8; the interaction is direct (By similarity). {ECO:0000250}. +P12849 KAP1_MOUSE cAMP-dependent protein kinase type I-beta regulatory subunit 381 43,224 Binding site (4); Chain (1); Disulfide bond (2); Modified residue (6); Motif (1); Nucleotide binding (2); Region (1) FUNCTION: Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. {ECO:0000250}. PTM: The pseudophosphorylation site binds to the substrate-binding region of the catalytic chain, resulting in the inhibition of its activity. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. SUBUNIT: The inactive holoenzyme is composed of two regulatory chains and two catalytic chains. Activation by cAMP releases the two active catalytic monomers and the regulatory dimer. Interacts with PRKX; regulates this cAMP-dependent protein kinase (By similarity). Interacts with smAKAP; this interaction may target PRKAR1B to the plasma membrane (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Four types of regulatory chains are found: I-alpha, I-beta, II-alpha, and II-beta. Their expression varies among tissues and is in some cases constitutive and in others inducible. +P12367 KAP2_MOUSE cAMP-dependent protein kinase type II-alpha regulatory subunit 401 45,389 Beta strand (12); Binding site (4); Chain (1); Helix (14); Initiator methionine (1); Modified residue (8); Nucleotide binding (2); Region (1) FUNCTION: Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. Type II regulatory chains mediate membrane association by binding to anchoring proteins, including the MAP2 kinase. PTM: Phosphorylated by the activated catalytic chain. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Colocalizes with PJA2 in the cytoplasm and the cell membrane. {ECO:0000250}. SUBUNIT: The inactive form of the enzyme is composed of two regulatory chains and two catalytic chains. Activation by cAMP produces two active catalytic monomers and a regulatory dimer that binds four cAMP molecules. Interacts with AKAP4. Interacts with CBFA2T3 (By similarity). Interacts with the phosphorylated form of PJA2 (By similarity). Interacts with MYRIP. This interaction may link PKA to components of the exocytosis machinery, thus facilitating exocytosis, including insulin release (By similarity). Forms a complex composed of PRKAR2A, GSK3B and GSKIP through GSKIP interaction; facilitates PKA-induced phosphorylation and regulates GSK3B activity (By similarity). Interacts with ADCY8; inhibits adenylate cyclase activity through PKA phosphorylation (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P13861}. TISSUE SPECIFICITY: Four types of regulatory chains are found: I-alpha, I-beta, II-alpha, and II-beta. Their expression varies among tissues and is in some cases constitutive and in others inducible. +P05132 KAPCA_MOUSE cAMP-dependent protein kinase catalytic subunit alpha (PKA C-alpha) (EC 2.7.11.11) 351 40,571 Active site (1); Alternative sequence (1); Beta strand (9); Binding site (1); Chain (1); Domain (2); Helix (17); Initiator methionine (1); Lipidation (1); Modified residue (8); Mutagenesis (3); Nucleotide binding (3); Sequence conflict (2); Turn (6) FUNCTION: Phosphorylates a large number of substrates in the cytoplasm and the nucleus. Regulates the abundance of compartmentalized pools of its regulatory subunits through phosphorylation of PJA2 which binds and ubiquitinates these subunits, leading to their subsequent proteolysis. Phosphorylates CDC25B, ABL1, NFKB1, CLDN3, PSMC5/RPT6, PJA2, RYR2, RORA and VASP. RORA is activated by phosphorylation. Required for glucose-mediated adipogenic differentiation increase and osteogenic differentiation inhibition from osteoblasts. Involved in the regulation of platelets in response to thrombin and collagen; maintains circulating platelets in a resting state by phosphorylating proteins in numerous platelet inhibitory pathways when in complex with NF-kappa-B (NFKB1 and NFKB2) and I-kappa-B-alpha (NFKBIA), but thrombin and collagen disrupt these complexes and free active PRKACA stimulates platelets and leads to platelet aggregation by phosphorylating VASP. Prevents the antiproliferative and anti-invasive effects of alpha-difluoromethylornithine in breast cancer cells when activated. RYR2 channel activity is potentiated by phosphorylation in presence of luminal Ca(2+), leading to reduced amplitude and increased frequency of store overload-induced Ca(2+) release (SOICR) characterized by an increased rate of Ca(2+) release and propagation velocity of spontaneous Ca(2+) waves, despite reduced wave amplitude and resting cytosolic Ca(2+). PSMC5/RPT6 activation by phosphorylation stimulates proteasome. Negatively regulates tight junctions (TJs) in ovarian cancer cells via CLDN3 phosphorylation. NFKB1 phosphorylation promotes NF-kappa-B p50-p50 DNA binding. Involved in embryonic development by down-regulating the Hedgehog (Hh) signaling pathway that determines embryo pattern formation and morphogenesis. Prevents meiosis resumption in prophase-arrested oocytes via CDC25B inactivation by phosphorylation. May also regulate rapid eye movement (REM) sleep in the pedunculopontine tegmental (PPT). Phosphorylates APOBEC3G and AICDA. Phosphorylates HSF1; this phosphorylation promotes HSF1 nuclear localization and transcriptional activity upon heat shock (By similarity). Isoform 2 phosphorylates and activates ABL1 in sperm flagellum to promote spermatozoa capacitation (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P17612, ECO:0000269|PubMed:19223768, ECO:0000269|PubMed:19560455}. PTM: Autophosphorylated. Phosphorylation is enhanced by vitamin K(2) (By similarity). Phosphorylated on threonine and serine residues. Phosphorylation on Thr-198 is required for full activity. {ECO:0000250, ECO:0000269|PubMed:8395513, ECO:0000269|PubMed:9707564}.; PTM: Asn-3 is partially deaminated to Asp-3 giving rise to 2 major isoelectric variants, called CB and CA respectively.; PTM: When myristoylated, Ser-11 is autophosphorylated probably in conjunction with deamidation of Asn-3. {ECO:0000269|PubMed:11141074, ECO:0000269|PubMed:8395513}.; PTM: Phosphorylated at Tyr-331 by activated receptor tyrosine kinases EGFR and PDGFR; this increases catalytic efficienncy. {ECO:0000269|PubMed:21866565}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18367160}. Cell membrane {ECO:0000250}. Nucleus {ECO:0000250}. Mitochondrion {ECO:0000269|PubMed:18367160}. Membrane {ECO:0000250|UniProtKB:P17612}; Lipid-anchor {ECO:0000250|UniProtKB:P17612}. Note=Translocates into the nucleus (monomeric catalytic subunit) (By similarity). The inactive holoenzyme is found in the cytoplasm. Distributed throughout the cytoplasm in meiotically incompetent oocytes. Associated to mitochondrion as meiotic competence is acquired. Aggregates around the germinal vesicles (GV) at the immature GV stage oocytes. Colocalizes with HSF1 in nuclear stress bodies (nSBs) upon heat shock (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P17612}.; SUBCELLULAR LOCATION: Isoform 2: Cell projection, cilium, flagellum {ECO:0000269|PubMed:27105888}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:27105888}. Note=Expressed in the midpiece region of the sperm flagellum (By similarity). Colocalizes with MROH2B and TCP11 on the acrosome and tail regions in round spermatids and spermatozoa regardless of the capacitation status of the sperm (PubMed:27105888). {ECO:0000250, ECO:0000269|PubMed:27105888}. SUBUNIT: A number of inactive tetrameric holoenzymes are produced by the combination of homo- or heterodimers of the different regulatory subunits associated with two catalytic subunits. Protein kinase A holoenzyme is comprised of two catalytic (C) and two regulatory (R) subunits which keep the enzyme in an inhibited state before activation by cyclic-AMP. cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP and two free monomeric catalytic subunits. The cAMP-dependent protein kinase catalytic subunit binds PJA2. Both isoforms 1 and 2 forms activate cAMP-sensitive PKAI and PKAII holoenzymes by interacting with regulatory subunit (R) of PKA, PRKAR1A/PKR1 and PRKAR2A/PKR2, respectively. Interacts with NFKB1, NFKB2 and NFKBIA in platelets; these interactions are disrupted by thrombin and collagen. Binds to ABL1 in spermatozoa and with CDC25B in oocytes. Interacts with APOBEC3G and AICDA (By similarity). Interacts with RAB13; downstream effector of RAB13 involved in tight junction assembly (By similarity). Found in a complex at least composed of MROH2B isoform 2, PRKACA isoform 2 and TCP11 (PubMed:27105888). Interacts with MROH2B isoform 2 (PubMed:27105888). Interacts with HSF1 (By similarity). Isoform 2 interacts with TCP11 (PubMed:27105888). {ECO:0000250, ECO:0000250|UniProtKB:P17612, ECO:0000269|PubMed:22323819}. TISSUE SPECIFICITY: Isoform 2 is sperm specific. +P68181 KAPCB_MOUSE cAMP-dependent protein kinase catalytic subunit beta (PKA C-beta) (EC 2.7.11.11) 351 40,708 Active site (1); Alternative sequence (5); Binding site (1); Chain (1); Domain (2); Initiator methionine (1); Lipidation (1); Modified residue (8); Nucleotide binding (1) FUNCTION: Mediates cAMP-dependent signaling triggered by receptor binding to GPCRs. PKA activation regulates diverse cellular processes such as cell proliferation, the cell cycle, differentiation and regulation of microtubule dynamics, chromatin condensation and decondensation, nuclear envelope disassembly and reassembly, as well as regulation of intracellular transport mechanisms and ion flux (PubMed:9368018). Regulates the abundance of compartmentalized pools of its regulatory subunits through phosphorylation of PJA2 which binds and ubiquitinates these subunits, leading to their subsequent proteolysis. Phosphorylates GPKOW which regulates its ability to bind RNA (By similarity). {ECO:0000250|UniProtKB:P22694, ECO:0000269|PubMed:9368018}. PTM: Asn-3 is deaminated to Asp in more than 25% of the proteins, giving rise to 2 major isoelectric variants, called CB and CA respectively (0.4 pH unit change). Deamidation proceeds via the so-called beta-aspartyl shift mechanism and yields either 'D-Asp-2' (major) or 'D-isoAsp-2' (minor), in addition to L-isomers. Deamidation occurs after the addition of myristate. The Asn-3 form reaches a significantly larger nuclear/cytoplasmic ratio than the 'Asp-2' form (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Membrane {ECO:0000250|UniProtKB:P22694}; Lipid-anchor {ECO:0000250|UniProtKB:P22694}. Nucleus {ECO:0000250}. Note=Translocates into the nucleus (monomeric catalytic subunit). The inactive holoenzyme is found in the cytoplasm. {ECO:0000250}. SUBUNIT: A number of inactive tetrameric holoenzymes are produced by the combination of homo- or heterodimers of the different regulatory subunits associated with two catalytic subunits. cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP and two free monomeric catalytic subunits. The cAMP-dependent protein kinase catalytic subunit binds PJA2. Interacts with GPKOW. {ECO:0000250|UniProtKB:P05132, ECO:0000250|UniProtKB:P22694}. TISSUE SPECIFICITY: Isoform 1 is found in all tissues examined, with the highest expression in the brain and very low levels in the testis. Isoform 2 is strongly expressed in the brain, in the prelimbic and insular cortex. Isoform 3 is also found only in the brain, but at very low levels. {ECO:0000269|PubMed:9368018}. +Q8C131 HCAR1_MOUSE Hydroxycarboxylic acid receptor 1 (G-protein coupled receptor 81) 343 38,927 Chain (1); Disulfide bond (1); Glycosylation (1); Sequence conflict (2); Topological domain (8); Transmembrane (7) TRANSMEM 22 42 Helical; Name=1. {ECO:0000255}.; TRANSMEM 50 70 Helical; Name=2. {ECO:0000255}.; TRANSMEM 91 111 Helical; Name=3. {ECO:0000255}.; TRANSMEM 132 152 Helical; Name=4. {ECO:0000255}.; TRANSMEM 183 203 Helical; Name=5. {ECO:0000255}.; TRANSMEM 221 241 Helical; Name=6. {ECO:0000255}.; TRANSMEM 260 280 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 21 Extracellular. {ECO:0000255}.; TOPO_DOM 43 49 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 71 90 Extracellular. {ECO:0000255}.; TOPO_DOM 112 131 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 153 182 Extracellular. {ECO:0000255}.; TOPO_DOM 204 220 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 242 259 Extracellular. {ECO:0000255}.; TOPO_DOM 281 343 Cytoplasmic. {ECO:0000255}. FUNCTION: Acts as a receptor for L-lactate and mediates its anti-lipolytic effect through a G(i)-protein-mediated pathway. {ECO:0000269|PubMed:18174606, ECO:0000269|PubMed:19047060}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Highly expressed in subcutaneous fat and omental fat and detectable in lower levels in brain and many other tissues. High levels detected in epididymal and subcutaneous fat with slightly lower in omental fat, low levels are detected in the brain, skeletal muscle, kidney, liver and the pancreas (at protein level). {ECO:0000269|PubMed:18174606, ECO:0000269|PubMed:19047060}. +Q9EP66 HCAR2_MOUSE Hydroxycarboxylic acid receptor 2 (G-protein coupled receptor 109) (G-protein coupled receptor 109A) (G-protein coupled receptor HM74) (Niacin receptor 1) (Nicotinic acid receptor) (Protein PUMA-G) 360 41,401 Chain (1); Disulfide bond (1); Modified residue (1); Topological domain (8); Transmembrane (7) TRANSMEM 31 51 Helical; Name=1. {ECO:0000255}.; TRANSMEM 61 81 Helical; Name=2. {ECO:0000255}.; TRANSMEM 99 119 Helical; Name=3. {ECO:0000255}.; TRANSMEM 141 161 Helical; Name=4. {ECO:0000255}.; TRANSMEM 190 210 Helical; Name=5. {ECO:0000255}.; TRANSMEM 227 247 Helical; Name=6. {ECO:0000255}.; TRANSMEM 271 291 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 30 Extracellular. {ECO:0000255}.; TOPO_DOM 52 60 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 82 98 Extracellular. {ECO:0000255}.; TOPO_DOM 120 140 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 162 189 Extracellular. {ECO:0000255}.; TOPO_DOM 211 226 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 248 270 Extracellular. {ECO:0000255}.; TOPO_DOM 292 360 Cytoplasmic. {ECO:0000255}. FUNCTION: Acts as a high affinity receptor for both nicotinic acid (also known as niacin) and (D)-beta-hydroxybutyrate and mediates increased adiponectin secretion and decreased lipolysis through G(i)-protein-mediated inhibition of adenylyl cyclase. This pharmacological effect requires nicotinic acid doses that are much higher than those provided by a normal diet. Mediates nicotinic acid-induced apoptosis in mature neutrophils. Receptor activation by nicotinic acid results in reduced cAMP levels which may affect activity of cAMP-dependent protein kinase A and phosphorylation of target proteins, leading to neutrophil apoptosis. {ECO:0000269|PubMed:15929991}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed in lungs, spleen, heart, skeletal muscle and adipose tissue. {ECO:0000269|PubMed:11745392, ECO:0000269|PubMed:12646212}. +O08756 HCD2_MOUSE 3-hydroxyacyl-CoA dehydrogenase type-2 (EC 1.1.1.35) (17-beta-hydroxysteroid dehydrogenase 10) (17-beta-HSD 10) (EC 1.1.1.51) (3-hydroxy-2-methylbutyryl-CoA dehydrogenase) (EC 1.1.1.178) (3-hydroxyacyl-CoA dehydrogenase type II) (Endoplasmic reticulum-associated amyloid beta-peptide-binding protein) (Mitochondrial ribonuclease P protein 2) (Mitochondrial RNase P protein 2) (Type II HADH) 261 27,419 Active site (1); Binding site (1); Chain (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (10); Nucleotide binding (1) FUNCTION: Mitochondrial dehydrogenase that catalyzes the beta-oxidation at position 17 of androgens and estrogens and has 3-alpha-hydroxysteroid dehydrogenase activity with androsterone (By similarity). Catalyzes the third step in the beta-oxidation of fatty acids (By similarity). Carries out oxidative conversions of 7-alpha-OH and 7-beta-OH bile acids (By similarity). Also exhibits 20-beta-OH and 21-OH dehydrogenase activities with C21 steroids (By similarity). By interacting with intracellular amyloid-beta, it may contribute to the neuronal dysfunction associated with Alzheimer disease (AD) (By similarity). Essential for structural and functional integrity of mitochondria (PubMed:20077426). {ECO:0000250|UniProtKB:Q99714, ECO:0000269|PubMed:20077426}.; FUNCTION: In addition to mitochondrial dehydrogenase activity, moonlights as a component of mitochondrial ribonuclease P, a complex that cleaves tRNA molecules in their 5'-ends. Together with HSD17B10/MRPP2, forms a subcomplex of the mitochondrial ribonuclease P, named MRPP1-MRPP2 subcomplex, which displays functions that are independent of the ribonuclease P activity. The MRPP1-MRPP2 subcomplex catalyzes the formation of N(1)-methylguanine and N(1)-methyladenine at position 9 (m1G9 and m1A9, respectively) in tRNAs; HSD17B10/MRPP2 acting as a non-catalytic subunit. The MRPP1-MRPP2 subcomplex also acts as a tRNA maturation platform: following 5'-end cleavage by the mitochondrial ribonuclease P complex, the MRPP1-MRPP2 subcomplex enhances the efficiency of 3'-processing catalyzed by ELAC2, retains the tRNA product after ELAC2 processing and presents the nascent tRNA to the mitochondrial CCA tRNA nucleotidyltransferase TRNT1 enzyme. {ECO:0000250|UniProtKB:Q99714}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q99714}. SUBUNIT: Homotetramer. Component of mitochondrial ribonuclease P, a complex composed of TRMT10C/MRPP1, HSD17B10/MRPP2 and MRPP31. Interacts with TRMT10C/MRPP1; forming the MRPP1-MRPP2 subcomplex of the mitochondrial ribonuclease P complex. {ECO:0000250|UniProtKB:Q99714}. +O88703 HCN2_MOUSE Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2 (Brain cyclic nucleotide-gated channel 2) (BCNG-2) (Hyperpolarization-activated cation channel 1) (HAC-1) 863 94,722 Beta strand (10); Chain (1); Compositional bias (2); Glycosylation (1); Helix (11); Intramembrane (1); Modified residue (11); Mutagenesis (22); Nucleotide binding (3); Region (1); Sequence conflict (2); Topological domain (8); Transmembrane (6) INTRAMEM 387 408 Pore-forming; Name=Segment H5. {ECO:0000255}. TRANSMEM 189 209 Helical; Name=Segment S1. {ECO:0000255}.; TRANSMEM 214 234 Helical; Name=Segment S2. {ECO:0000255}.; TRANSMEM 262 282 Helical; Name=Segment S3. {ECO:0000255}.; TRANSMEM 291 311 Helical; Voltage-sensor; Name=Segment S4. {ECO:0000255}.; TRANSMEM 343 363 Helical; Name=Segment S5. {ECO:0000255}.; TRANSMEM 414 434 Helical; Name=Segment S6. {ECO:0000255}. TOPO_DOM 1 188 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 210 213 Extracellular. {ECO:0000255}.; TOPO_DOM 235 261 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 283 290 Extracellular. {ECO:0000255}.; TOPO_DOM 312 342 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 364 386 Extracellular. {ECO:0000255}.; TOPO_DOM 409 413 Extracellular. {ECO:0000255}.; TOPO_DOM 435 863 Cytoplasmic. {ECO:0000255}. FUNCTION: Hyperpolarization-activated ion channel exhibiting weak selectivity for potassium over sodium ions. Contributes to the native pacemaker currents in heart (If) and in neurons (Ih). Can also transport ammonium in the distal nephron. Produces a large instantaneous current. {ECO:0000269|PubMed:10962006, ECO:0000269|PubMed:11096117, ECO:0000269|PubMed:11741901, ECO:0000269|PubMed:12034718, ECO:0000269|PubMed:12193608, ECO:0000269|PubMed:12968185, ECO:0000269|PubMed:17562314, ECO:0000269|PubMed:23103389}. PTM: Phosphorylation at Ser-641 by PRKG2 shifts the voltage-dependence to more negative voltages, hence counteracting the stimulatory effect of cGMP on gating. {ECO:0000269|PubMed:21347269}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10962006, ECO:0000269|PubMed:11096117, ECO:0000269|PubMed:12034718, ECO:0000269|PubMed:12193608, ECO:0000269|PubMed:17562314, ECO:0000269|PubMed:23103389}; Multi-pass membrane protein {ECO:0000269|PubMed:10962006, ECO:0000269|PubMed:11096117, ECO:0000269|PubMed:12034718, ECO:0000269|PubMed:12193608, ECO:0000269|PubMed:17562314, ECO:0000269|PubMed:23103389}. SUBUNIT: Homotetramer. Heterotetramer with HCN1. The potassium channel is composed of a homo- or heterotetrameric complex of pore-forming subunits. Forms an obligate 4:4 complex with accessory subunit PEX5L. Interacts with KCNE2. {ECO:0000269|PubMed:11420311, ECO:0000269|PubMed:12034718, ECO:0000269|PubMed:12193608, ECO:0000269|PubMed:12968185, ECO:0000269|PubMed:17562314, ECO:0000269|PubMed:18367452, ECO:0000269|PubMed:19525958, ECO:0000269|PubMed:22550182}. DOMAIN: The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position. TISSUE SPECIFICITY: Highly expressed in brain. Detected at low levels in heart, in ventricle, atrium and in sinoatrial node (SAN). {ECO:0000269|PubMed:9630217}. +Q9JHD2 KAT2A_MOUSE Histone acetyltransferase KAT2A (EC 2.3.1.48) (General control of amino acid synthesis protein 5-like 2) (Histone acetyltransferase GCN5) (MmGCN5) (Histone succinyltransferase KAT2A) (EC 2.3.1.-) (Lysine acetyltransferase 2A) 830 93,394 Active site (1); Binding site (1); Chain (1); Cross-link (3); Domain (2); Initiator methionine (1); Modified residue (1); Region (3); Sequence conflict (2) FUNCTION: Protein lysine acyltransferase that can act both as a acetyltransferase and succinyltransferase, depending on the context (PubMed:28424240). Acts as a histone lysine succinyltransferase: catalyzes succinylation of histone H3 on 'Lys-79' (H3K79succ), with a maximum frequency around the transcription start sites of genes (By similarity). Succinylation of histones gives a specific tag for epigenetic transcription activation (By similarity). Association with the 2-oxoglutarate dehydrogenase complex, which provides succinyl-CoA, is required for histone succinylation (By similarity). In different complexes, functions either as an acetyltransferase (HAT) or as a succinyltransferase: in the SAGA and ATAC complexes, acts as a histone acetyltransferase (By similarity). Has significant histone acetyltransferase activity with core histones, but not with nucleosome core particles (By similarity). Acetylation of histones gives a specific tag for epigenetic transcription activation (PubMed:28424240). Involved in long-term memory consolidation and synaptic plasticity: acts by promoting expression of a hippocampal gene expression network linked to neuroactive receptor signaling (PubMed:25024434). Acts as a positive regulator of T-cell activation: upon TCR stimulation, recruited to the IL2 promoter following interaction with NFATC2 and catalyzes acetylation of histone H3 at Lys-9 (H3K9ac), leading to promote IL2 expression (PubMed:28424240). Also acetylates non-histone proteins, such as CEBPB, PLK4 and TBX5 (PubMed:17301242). Involved in heart and limb development by mediating acetylation of TBX5, acetylation regulating nucleocytoplasmic shuttling of TBX5 (By similarity). Acts as a negative regulator of centrosome amplification by mediating acetylation of PLK4 (By similarity). {ECO:0000250|UniProtKB:Q92830, ECO:0000269|PubMed:17301242, ECO:0000269|PubMed:25024434, ECO:0000269|PubMed:28424240}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92830}. Chromosome {ECO:0000269|PubMed:28424240}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q92830}. Note=Mainly localizes to the nucleus. Also localizes to centrosomes in late G1 and around the G1/S transition, coinciding with the onset of centriole formation. {ECO:0000250|UniProtKB:Q92830}. SUBUNIT: Interacts with EP300, CREBBP and ADA2 (By similarity). Component of the TFTC-HAT complex, at least composed of TAF5L, TAF6L, TAF3, TADA3L, SUPT3H/SPT3, TAF2/TAFII150, TAF4/TAFII135, TAF5/TAFII100, KAT2A/GCN5L2, TAF10 and TRRAP (By similarity). Component of the STAGA transcription coactivator-HAT complex, at least composed of SUPT3H, KAT2A, SUPT7L, TAF5L, TAF6L, TADA3L, TAD1L, TAF10, TAF12, TRRAP and TAF9 (By similarity). The STAGA core complex is associated with a subcomplex required for histone deubiquitination composed of ATXN7L3, ENY2 and USP22 (By similarity). Component of the ADA2A-containing complex (ATAC), composed of KAT14, KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1 (By similarity). In the complex, it probably interacts directly with KAT14, MBIP and WDR5 (By similarity). Interacts with PML (PubMed:22886304). Interacts with CEBPB (PubMed:17301242). Interacts with TACC1, TACC2 and TACC3 (By similarity). Interacts with RELA (PubMed:25024434). Interacts with NFATC2 (PubMed:28424240). Interacts with TBX5 (By similarity). Interacts with PLK4 (By similarity). Associates with the 2-oxoglutarate dehydrogenase complex (By similarity). {ECO:0000250|UniProtKB:Q92830, ECO:0000269|PubMed:17301242, ECO:0000269|PubMed:22886304, ECO:0000269|PubMed:25024434, ECO:0000269|PubMed:28424240}. DOMAIN: Loop3 is required for substrate specificity and adopts different structural conformations in succinyl-CoA-bound and acetyl-CoA-bound forms. Tyr-638 has an important role in the selective binding of succinyl-CoA over acetyl-CoA. {ECO:0000250|UniProtKB:Q92830}. TISSUE SPECIFICITY: In brain, highly expressed in the hippocampal CA1 region (at protein level) (PubMed:25024434). Also expressed in the hippocampal subregions CA3 and the dentate gyrus as well as in the cortex and prefrontal cortex (PubMed:25024434). Expressed at low level in the cerebellum (PubMed:25024434). {ECO:0000269|PubMed:25024434}. +Q71RI9 KAT3_MOUSE Kynurenine--oxoglutarate transaminase 3 (EC 2.6.1.7) (Cysteine-S-conjugate beta-lyase 2) (EC 4.4.1.13) (Kynurenine aminotransferase 3) (Kynurenine aminotransferase III) (KATIII) (Kynurenine--glyoxylate transaminase) (EC 2.6.1.63) (Kynurenine--oxoglutarate transaminase III) 455 51,126 Alternative sequence (1); Beta strand (15); Binding site (4); Chain (1); Helix (23); Modified residue (3); Turn (8) FUNCTION: Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). May catalyze the beta-elimination of S-conjugates and Se-conjugates of L-(seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond (By similarity). Has transaminase activity towards L-kynurenine, tryptophan, phenylalanine, serine, cysteine, methionine, histidine, glutamine and asparagine with glyoxylate as an amino group acceptor (in vitro). Has lower activity with 2-oxoglutarate as amino group acceptor (in vitro). {ECO:0000250, ECO:0000269|PubMed:19029248}. SUBUNIT: Homodimer. {ECO:0000269|PubMed:19029248}. TISSUE SPECIFICITY: Widely expressed, with higher expression levels in liver, kidney, heart and neuroendocrine tissues. {ECO:0000269|PubMed:16376499}. +Q5SVQ0 KAT7_MOUSE Histone acetyltransferase KAT7 (EC 2.3.1.48) (Histone acetyltransferase binding to ORC1) (Lysine acetyltransferase 7) (MOZ, YBF2/SAS3, SAS2 and TIP60 protein 2) (MYST-2) 613 70,641 Active site (1); Alternative sequence (3); Binding site (2); Chain (1); Compositional bias (1); Cross-link (2); Domain (1); Modified residue (19); Region (2); Sequence conflict (2); Zinc finger (2) FUNCTION: Component of the HBO1 complex which has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3 and is responsible for the bulk of histone H4 acetylation in vivo. Involved in H3K14 (histone H3 lysine 14) acetylation and cell proliferation (PubMed:23319590). Through chromatin acetylation it may regulate DNA replication and act as a coactivator of TP53-dependent transcription. Acts as a coactivator of the licensing factor CDT1. Specifically represses AR-mediated transcription. {ECO:0000250|UniProtKB:O95251, ECO:0000269|PubMed:23319590}. PTM: Phosphorylation at Ser-59 by PLK1 during mitosis seems important for prereplicative complex formation and DNA replication licensing, and requires prior phosphorylation at Thr-87 and Thr-90 by CDK1. Phosphorylated by MAP2K1, which accelerates its degradation (PubMed:23319590). {ECO:0000250|UniProtKB:O95251, ECO:0000269|PubMed:23319590}.; PTM: Autoacetylation at Lys-434 is required for proper function. {ECO:0000250|UniProtKB:Q9H7Z6}.; PTM: Ubiquitinated at Lys-340, leading to proteasomal degradation. {ECO:0000250|UniProtKB:O95251}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:O95251}. Cytoplasm, cytosol {ECO:0000269|PubMed:23319590}. Nucleus {ECO:0000269|PubMed:23319590}. Note=Associates with replication origins specifically during the G1 phase of the cell cycle. {ECO:0000250|UniProtKB:O95251}. SUBUNIT: Component of the HBO1 complex composed at least of ING4 or ING5, KAT7/HBO1, MEAF6, and one of JADE1, JADE2 and JADE3 (By similarity). Interacts with MCM2 and ORC1 (By similarity). Interacts with the androgen receptor (AR) in the presence of dihydrotestosterone (By similarity). Interacts with CDT1. Interacts with FBXW15, MAP2K1 and CUL1 (PubMed:23319590). {ECO:0000250|UniProtKB:O95251, ECO:0000269|PubMed:23319590}. DOMAIN: The C2HC MYST-type zinc finger is required for interaction with MCM2 and ORC1. {ECO:0000250|UniProtKB:O95251}.; DOMAIN: The N-terminus is involved in transcriptional repression, while the C-terminus mediates AR-interaction. {ECO:0000250}. +Q9D5U5 HDHD1_MOUSE Pseudouridine-5'-phosphatase (EC 3.1.3.96) (Haloacid dehalogenase-like hydrolase domain-containing protein 1) (Haloacid dehalogenase-like hydrolase domain-containing protein 1A) (Pseudouridine-5'-monophosphatase) (5'-PsiMPase) 234 26,161 Active site (2); Chain (1); Metal binding (2); Sequence conflict (5) FUNCTION: Dephosphorylates pseudouridine 5'-phosphate, a potential intermediate in rRNA degradation. Pseudouridine is then excreted intact in urine. {ECO:0000250|UniProtKB:Q08623}. +Q9Z2V5 HDAC6_MOUSE Histone deacetylase 6 (HD6) (EC 3.5.1.98) (Histone deacetylase mHDA2) 1149 125,787 Active site (2); Chain (1); Compositional bias (1); Metal binding (12); Modified residue (9); Region (4); Sequence conflict (7); Zinc finger (1) FUNCTION: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes (By similarity). Plays a central role in microtubule-dependent cell motility via deacetylation of tubulin. {ECO:0000250, ECO:0000269|PubMed:19893491, ECO:0000269|PubMed:22819792}.; FUNCTION: In addition to its protein deacetylase activity, plays a key role in the degradation of misfolded proteins: when misfolded proteins are too abundant to be degraded by the chaperone refolding system and the ubiquitin-proteasome, mediates the transport of misfolded proteins to a cytoplasmic juxtanuclear structure called aggresome. Probably acts as an adapter that recognizes polyubiquitinated misfolded proteins and target them to the aggresome, facilitating their clearance by autophagy (By similarity). {ECO:0000250}. PTM: Phosphorylated by AURKA. {ECO:0000250}.; PTM: Ubiquitinated. Its polyubiquitination however does not lead to its degradation (By similarity). {ECO:0000250}.; PTM: Sumoylated in vitro. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Perikaryon. Cell projection, dendrite. Cell projection, axon. Note=It is mainly cytoplasmic, where it is associated with microtubules. SUBUNIT: Interacts with BBIP10, DDIT3/CHOP, F-actin and HDAC11. Interacts with SIRT2 (via both phosphorylated, unphosphorylated, active or inactive forms); the interaction is necessary for the complex to interact with alpha-tubulin. Under proteasome impairment conditions, interacts with UBD via its histone deacetylase 1 and UBP-type zinc-finger regions (By similarity). Interacts with CBFA2T3, CYLD and ZMYND15. Interacts with RIPOR2; this interaction occurs during early myogenic differentiation and prevents HDAC6 to deacetylate tubulin (By similarity). Interacts with DYSF; this interaction occurs during early myogenic differentiation (By similarity). {ECO:0000250|UniProtKB:Q9UBN7, ECO:0000269|PubMed:11533236, ECO:0000269|PubMed:19893491, ECO:0000269|PubMed:20675388}. TISSUE SPECIFICITY: Expressed in neurons of the cortex. Expressed in Purkinje cells. Detected in keratinocytes (at protein level). {ECO:0000269|PubMed:16933150, ECO:0000269|PubMed:19893491}. +P42859 HD_MOUSE Huntingtin (Huntington disease protein homolog) (HD protein homolog) 3119 344,690 Alternative sequence (1); Chain (1); Compositional bias (6); Modified residue (13); Motif (1); Region (1); Repeat (5); Sequence conflict (46) FUNCTION: May play a role in microtubule-mediated transport or vesicle function. PTM: Phosphorylation at Ser-1159 and Ser-1179 by CDK5 in response to DNA damage in nuclei of neurons protects neurons against polyglutamine expansion as well as DNA damage mediated toxicity. {ECO:0000250|UniProtKB:P42858}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P42858}. Nucleus {ECO:0000250|UniProtKB:P42858}. Note=Shuttles between cytoplasm and nucleus in a Ran GTPase-independent manner. {ECO:0000250|UniProtKB:P42858}. SUBUNIT: Interacts with PFN1 (By similarity). Interacts through its N-terminus with PRPF40A (By similarity). Interacts with PQBP1 (By similarity). Interacts with SETD2 (By similarity). Interacts with SH3GLB1 (PubMed:12456676). Interacts with SYVN (By similarity). Interacts with TPR; the interaction is inhibited by forms of Huntingtin with expanded polyglutamine stretch (By similarity). Interacts with ZDHHC13 (via ANK repeats) (PubMed:26198635). Interacts with ZDHHC17 (via ANK repeats) (PubMed:26198635). Interacts with F8A1/F8A2/F8A3 (By similarity). {ECO:0000250|UniProtKB:P42858, ECO:0000269|PubMed:12456676, ECO:0000269|PubMed:26198635}. DOMAIN: The N-terminal Gln-rich and Pro-rich domain has great conformational flexibility and is likely to exist in a fluctuating equilibrium of alpha-helical, random coil, and extended conformations. {ECO:0000250|UniProtKB:P42858}. TISSUE SPECIFICITY: The highest level is seen throughout the brain, but it is also found in the stomach, heart, testis, adipose tissue, muscle, spleen, liver, and kidney. +Q69ZR2 HECD1_MOUSE E3 ubiquitin-protein ligase HECTD1 (EC 2.3.2.26) (HECT domain-containing protein 1) (HECT-type E3 ubiquitin transferase HECTD1) (Protein open mind) 2618 290,086 Active site (1); Chain (1); Compositional bias (3); Domain (2); Modified residue (7); Mutagenesis (1); Region (1); Repeat (4); Sequence conflict (2) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates (PubMed:22431752). Mediates 'Lys-63'-linked polyubiquitination of HSP90AA1 which leads to its intracellular localization and reduced secretion (PubMed:22431752). Negatively regulating HSP90AA1 secretion in cranial mesenchyme cells impairs their emigration and is consequently essential for the correct development of the cranial neural folds and neural tube closure (PubMed:17442300, PubMed:22431752). {ECO:0000269|PubMed:17442300, ECO:0000269|PubMed:22431752}. SUBUNIT: Interacts with IGSF1 (By similarity). Interacts (via N-terminus) with HSP90AA1 (PubMed:22431752). {ECO:0000250|UniProtKB:Q9ULT8, ECO:0000269|PubMed:22431752}. +Q8CDU6 HECD2_MOUSE Probable E3 ubiquitin-protein ligase HECTD2 (EC 2.3.2.26) (HECT domain-containing protein 2) (HECT-type E3 ubiquitin transferase HECTD2) 774 87,773 Active site (1); Chain (1); Domain (1); Erroneous initiation (1); Modified residue (1); Sequence conflict (2) Protein modification; protein ubiquitination. FUNCTION: Probable E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. {ECO:0000250|UniProtKB:Q69ZR2}. +Q8BQM4 HEAT3_MOUSE HEAT repeat-containing protein 3 679 74,305 Chain (1); Compositional bias (1); Modified residue (3); Repeat (2); Sequence conflict (2) +Q6I6G8 HECW2_MOUSE E3 ubiquitin-protein ligase HECW2 (EC 2.3.2.26) (HECT, C2 and WW domain-containing protein 2) (HECT-type E3 ubiquitin transferase HECW2) (NEDD4-like E3 ubiquitin-protein ligase 2) 1578 176,235 Active site (1); Alternative sequence (1); Chain (1); Coiled coil (1); Domain (4); Modified residue (4); Region (1); Sequence conflict (1) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination of TP73. Acts to stabilize TP73 and enhance activation of transcription by TP73. Involved in the regulation of mitotic metaphase/anaphase transition. {ECO:0000250|UniProtKB:Q9P2P5}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9P2P5}. SUBUNIT: Interacts with TP73 (By similarity). Interacts with FZR1 (By similarity). {ECO:0000250|UniProtKB:Q9P2P5}. +E9Q7X6 HEG1_MOUSE Protein HEG homolog 1 1337 141,899 Alternative sequence (3); Chain (1); Compositional bias (1); Disulfide bond (6); Domain (2); Erroneous initiation (1); Glycosylation (1); Modified residue (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1205 1225 Helical. {ECO:0000255}. TOPO_DOM 32 1204 Extracellular. {ECO:0000255}.; TOPO_DOM 1226 1337 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor component of the CCM signaling pathway which is a crucial regulator of heart and vessel formation and integrity. May be acting by stabilizing endothelial cell junctions. {ECO:0000269|PubMed:19151727}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Cell junction {ECO:0000269|PubMed:19151727}. SUBUNIT: Interacts with CCM2 and KRIT1; KRIT1 markedly facilitates interaction with CCM2. {ECO:0000269|PubMed:19151727}. +Q60848 HELLS_MOUSE Lymphocyte-specific helicase (EC 3.6.4.-) (Proliferation-associated SNF2-like protein) 821 95,126 Alternative sequence (1); Chain (1); Coiled coil (1); Domain (2); Erroneous initiation (1); Modified residue (2); Motif (1); Nucleotide binding (1); Sequence conflict (2) FUNCTION: Plays an essential role in normal development and survival. Involved in regulation of the expansion or survival of lymphoid cells. Required for de novo or maintenance DNA methylation. May control silencing of the imprinted CDKN1C gene through DNA methylation. May play a role in formation and organization of heterochromatin, implying a functional role in the regulation of transcription and mitosis. {ECO:0000269|PubMed:10781083, ECO:0000269|PubMed:11325543, ECO:0000269|PubMed:11357197, ECO:0000269|PubMed:11711429, ECO:0000269|PubMed:14517253, ECO:0000269|PubMed:14612388, ECO:0000269|PubMed:15105378, ECO:0000269|PubMed:15647320, ECO:0000269|PubMed:8647447}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10781083, ECO:0000269|PubMed:14517253, ECO:0000269|PubMed:14612388}. Note=Closely associated with pericentric heterochromatin. TISSUE SPECIFICITY: Highly expressed in thymus, bone marrow, and testis. Not detected in heart, brain, liver, kidney, skeletal muscle, spleen, peripheral blood lymphocytes, small intestine, colon, prostate or ovary. {ECO:0000269|PubMed:11325543, ECO:0000269|PubMed:11357197, ECO:0000269|PubMed:9878251}. +Q4VAH7 HECA2_MOUSE HEPACAM family member 2 (Mitotic kinetics regulator) 463 51,421 Chain (1); Disulfide bond (2); Domain (2); Glycosylation (4); Signal peptide (1); Topological domain (1); Transmembrane (1) TRANSMEM 353 373 Helical. {ECO:0000255}. TOPO_DOM 374 463 Cytoplasmic. {ECO:0000255}. FUNCTION: Required during prometaphase for centrosome maturation. Following poly-ADP-ribosylation (PARsylation) by TNKS, translocates from the Golgi apparatus to mitotic centrosomes and plays a key role in the formation of robust microtubules for prompt movement of chromosomes: anchors AKAP9/CG-NAP, a scaffold protein of the gamma-tubulin ring complex and promotes centrosome maturation (By similarity). {ECO:0000250}. PTM: Poly-ADP-ribosylated (PARsylated) by tankyrase TNKS during late G2 and prophase, leading to translocation to mitotic centrosomes. {ECO:0000250}.; PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:A8MVW5}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:A8MVW5}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:A8MVW5}. Midbody {ECO:0000250|UniProtKB:A8MVW5}. Note=In interphase, localizes to the Golgi apparatus. Localizes to centrosomes and spindles during prophase, prometaphase, and metaphase of mitosis, and to midbodies at telophase. Translocation to mitotic centrosomes is the result of poly-ADP-ribosylation (PARsylation). {ECO:0000250|UniProtKB:A8MVW5}. +Q6NVF4 HELB_MOUSE DNA helicase B (EC 3.6.4.12) 1074 121,471 Chain (1); Compositional bias (1); Erroneous initiation (1); Modified residue (5); Motif (1); Mutagenesis (2); Sequence conflict (2) FUNCTION: 5'-3' DNA helicase involved in DNA damage response by acting as an inhibitor of DNA end resection (PubMed:26774285). Recruitment to single-stranded DNA (ssDNA) following DNA damage leads to inhibit the nucleases catalyzing resection, such as EXO1, BLM and DNA2, possibly via the 5'-3' ssDNA translocase activity of HELB (PubMed:26774285). As cells approach S phase, DNA end resection is promoted by the nuclear export of HELB following phosphorylation (PubMed:26774285). Acts independently of TP53BP1 (PubMed:26774285). Unwinds duplex DNA with 5'-3' polarity. Has single-strand DNA-dependent ATPase and DNA helicase activities. Prefers ATP and dATP as substrates. During S phase, may facilitate cellular recovery from replication stress (PubMed:11557815, PubMed:7596831, PubMed:7794903). {ECO:0000269|PubMed:11557815, ECO:0000269|PubMed:26774285, ECO:0000269|PubMed:7596831, ECO:0000269|PubMed:7794903}. PTM: Phosphorylated at Ser-942 by CDK2 during the G1/S transition, resulting in its nuclear export into the cytoplasm. As S phase progresses, its exclusion from the nucleus promotes the activation of long-range resection. {ECO:0000250|UniProtKB:Q8NG08}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26774285}. Cytoplasm {ECO:0000269|PubMed:26774285}. Chromosome {ECO:0000250|UniProtKB:Q8NG08}. Note=Predominantly nuclear. Phosphorylation at Ser-942 by CDK2 during the G1/S transition results in its nuclear export into the cytoplasm as cells approach and progress through S phase. Following DNA damage, recruited to sites of double-strand breaks by the RPA complex. {ECO:0000250|UniProtKB:Q8NG08}. SUBUNIT: Binds to RPA1; this interaction promotes HELB recruitment to chromatin following DNA damage. Interacts with at least two subunits of the DNA polymerase alpha complex. Interacts with CDC45. Interacts with TOPB1. {ECO:0000250|UniProtKB:Q8NG08}. +Q9D3R6 KATL2_MOUSE Katanin p60 ATPase-containing subunit A-like 2 (Katanin p60 subunit A-like 2) (EC 5.6.1.1) (p60 katanin-like 2) 539 61,153 Alternative sequence (5); Chain (1); Domain (1); Nucleotide binding (1) FUNCTION: Severs microtubules in vitro in an ATP-dependent manner. This activity may promote rapid reorganization of cellular microtubule arrays. {ECO:0000255|HAMAP-Rule:MF_03025}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03025}. Cytoplasm {ECO:0000250|UniProtKB:Q8IYT4}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q8IYT4}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q8IYT4}. Note=Localizes within the cytoplasm, partially overlapping with microtubules in interphase and to the mitotic spindle and spindle poles during mitosis. {ECO:0000250|UniProtKB:Q8IYT4}. +Q9CR56 KBRS2_MOUSE NF-kappa-B inhibitor-interacting Ras-like protein 2 (I-kappa-B-interacting Ras-like protein 2) (Kappa B-Ras protein 2) (KappaB-Ras2) 191 21,494 Chain (1); Motif (1); Nucleotide binding (3); Region (1); Sequence conflict (1) FUNCTION: Atypical Ras-like protein that acts as a potent regulator of NF-kappa-B activity by preventing the degradation of NF-kappa-B inhibitor beta (NFKBIB) by most signals, explaining why NFKBIB is more resistant to degradation. May act by blocking phosphorylation of NFKBIB and nuclear localization of p65/RELA NF-kappa-B subunit. It is unclear whether it acts as a GTPase. Both GTP- and GDP-bound forms block phosphorylation of NFKBIB (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with both NF-kappa-B inhibitor alpha (NFKBIA) and beta (NFKBIB) in vitro. However, it probably only interacts with NFKBIB in vivo (By similarity). {ECO:0000250}. DOMAIN: In contrast to other members of the Ras family, the members of the KappaB-Ras subfamily do not contain the conserved Gly and Gln residues in positions 13 and 65, which are replaced by Ala and Leu residues, respectively, and are therefore similar to the constitutively active forms of oncogenic forms of Ras. This suggests that members of this family are clearly different from other small GTPases proteins. +Q8BHI4 KBTB3_MOUSE Kelch repeat and BTB domain-containing protein 3 (BTB and kelch domain-containing protein 3) 607 69,551 Chain (1); Domain (2); Repeat (5); Sequence conflict (1) +Q8BNW9 KBTBB_MOUSE Kelch repeat and BTB domain-containing protein 11 633 67,946 Chain (1); Domain (1); Erroneous initiation (1); Modified residue (6); Repeat (4); Sequence conflict (2) +Q9D618 KBTBC_MOUSE Kelch repeat and BTB domain-containing protein 12 (Kelch domain-containing protein 6) 625 71,191 Alternative sequence (2); Chain (1); Domain (2); Repeat (4); Sequence conflict (1) +Q8C828 KBTBD_MOUSE Kelch repeat and BTB domain-containing protein 13 458 49,769 Chain (1); Domain (1); Erroneous initiation (1); Repeat (5) Protein modification; protein ubiquitination. FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex. {ECO:0000250}. PTM: Autoubiquitinated. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Component of the BCR(KBTBD13) E3 ubiquitin ligase complex, at least composed of CUL3 and KBTBD13 and RBX1. Interacts with CUL3 (By similarity). {ECO:0000250}. DOMAIN: The BCB domain mediates the interaction with CUL3. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in skeletal muscle, heart and lung. {ECO:0000269|PubMed:21109227}. +P63143 KCAB1_MOUSE Voltage-gated potassium channel subunit beta-1 (EC 1.1.1.-) (K(+) channel subunit beta-1) (Kv-beta-1) 401 44,723 Active site (1); Binding site (5); Chain (1); Nucleotide binding (4); Sequence conflict (8) FUNCTION: Cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits (PubMed:10454353). Modulates action potentials via its effect on the pore-forming alpha subunits (PubMed:10454353). Promotes expression of the pore-forming alpha subunits at the cell membrane, and thereby increases channel activity (PubMed:8824288). Mediates closure of delayed rectifier potassium channels by physically obstructing the pore via its N-terminal domain and increases the speed of channel closure for other family members (By similarity). Promotes the closure of KCNA1, KCNA2 and KCNA5 channels (By similarity). Accelerates KCNA4 channel closure (By similarity). Accelerates the closure of heteromeric channels formed by KCNA1 and KCNA4 (By similarity). Accelerates the closure of heteromeric channels formed by KCNA2, KCNA5 and KCNA6 (By similarity). Enhances KCNB1 and KCNB2 channel activity (PubMed:8824288). Binds NADPH; this is required for efficient down-regulation of potassium channel activity (By similarity). Has NADPH-dependent aldoketoreductase activity (By similarity). Oxidation of the bound NADPH strongly decreases N-type inactivation of potassium channel activity (By similarity). {ECO:0000250|UniProtKB:P63144, ECO:0000250|UniProtKB:Q14722, ECO:0000269|PubMed:10454353, ECO:0000269|PubMed:8824288}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14722}. Membrane {ECO:0000250|UniProtKB:P63144}; Peripheral membrane protein {ECO:0000250|UniProtKB:P63144}; Cytoplasmic side {ECO:0000250|UniProtKB:P63144}. Cell membrane {ECO:0000250|UniProtKB:Q14722}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q14722}; Cytoplasmic side {ECO:0000250|UniProtKB:Q14722}. Note=Recruited to the cytoplasmic side of the cell membrane via its interaction with pore-forming potassium channel alpha subunits. {ECO:0000250|UniProtKB:Q14722}. SUBUNIT: Homotetramer (By similarity). Interaction with tetrameric potassium channel alpha subunits gives rise to a heterooctamer (Probable). Identified in potassium channel complexes containing KCNA1, KCNA2, KCNA4, KCNA5, KCNA6, KCNAB1 and KCNAB2 (By similarity). Interacts with KCNA1 (By similarity). Interacts with the dimer formed by GNB1 and GNG2; this enhances KCNA1 binding (By similarity). Interacts with KCNA4 (By similarity). Interacts with KCNB2 and KCNA5 (PubMed:8824288). Interacts with SQSTM1 (By similarity). Part of a complex containing KCNA1, KCNA4 and LGI1; interaction with LGI1 inhibits down-regulation of KCNA1 channel activity (By similarity). {ECO:0000250|UniProtKB:P63144, ECO:0000250|UniProtKB:Q14722, ECO:0000269|PubMed:8824288, ECO:0000305}. DOMAIN: The N-terminal domain of the beta subunit mediates closure of delayed rectifier potassium channels by physically obstructing the pore. {ECO:0000250|UniProtKB:P63144}. TISSUE SPECIFICITY: Detected in brain, in hippocampus and striatum (at protein level) (PubMed:10454353). Predominantly expressed in brain. No expression found in heart, skeletal muscle or kidney. In the late embryonic and early neonatal brain, highly expressed in hippocampus, cerebral cortex, caudate putamen, colliculus and cerebellum. {ECO:0000269|PubMed:10454353, ECO:0000269|PubMed:9468385}. +P62482 KCAB2_MOUSE Voltage-gated potassium channel subunit beta-2 (EC 1.1.1.-) (K(+) channel subunit beta-2) (Kv-beta-2) (Neuroimmune protein F5) 367 41,021 Active site (1); Binding site (5); Chain (1); Modified residue (8); Mutagenesis (1); Nucleotide binding (4); Sequence conflict (4) FUNCTION: Cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits (PubMed:8576199). Contributes to the regulation of nerve signaling, and prevents neuronal hyperexcitability (PubMed:11825900, PubMed:21209188). Promotes expression of the pore-forming alpha subunits at the cell membrane, and thereby increases channel activity (By similarity). Promotes potassium channel closure via a mechanism that does not involve physical obstruction of the channel pore (PubMed:8576199). Modulates the functional properties of KCNA4 (By similarity). Modulates the functional properties of KCNA5 (PubMed:8576199). Enhances KCNB2 channel activity (PubMed:8824288). Modulates the functional properties of KCNA5 (PubMed:8576199). Binds NADPH and has NADPH-dependent aldoketoreductase activity (By similarity). Has broad substrate specificity and can catalyze the reduction of methylglyoxal, 9,10-phenanthrenequinone, prostaglandin J2, 4-nitrobenzaldehyde, 4-nitroacetophenone and 4-oxo-trans-2-nonenal (in vitro) (By similarity). {ECO:0000250|UniProtKB:P62483, ECO:0000269|PubMed:11825900, ECO:0000269|PubMed:21209188, ECO:0000269|PubMed:8576199, ECO:0000269|PubMed:8824288}. PTM: Phosphorylated by PRKCZ; may be regulated by incorporation in a complex composed of PRKCZ and SQSTM1. {ECO:0000250|UniProtKB:P62483}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P62483}. Membrane {ECO:0000269|PubMed:21357749, ECO:0000269|PubMed:8576199}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell membrane {ECO:0000250|UniProtKB:P62483}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell projection, axon {ECO:0000269|PubMed:11825900}. Cell junction, synapse, synaptosome {ECO:0000269|PubMed:21357749}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P62483}. Note=Recruited to the cytoplasmic side of the cell membrane via its interaction with pore-forming potassium channel alpha subunits. Associates with microtubules when unphosphorylated. {ECO:0000250|UniProtKB:P62483}. SUBUNIT: Homotetramer (By similarity). Interaction with tetrameric potassium channel alpha subunits gives rise to a heterooctamer (By similarity). Identified in potassium channel complexes containing KCNA1, KCNA2, KCNA4, KCNA5, KCNA6, KCNAB1 and KCNAB2 (By similarity). Interacts with KCNA1 (By similarity). Interacts with KCNA2 (By similarity). Interacts with KCNA4 and KCND3 (By similarity). Interacts (in unphosphorylated form) with MAPRE1 (By similarity). Interacts with KCNA5 (PubMed:8576199, PubMed:8824288). Interacts with KCNB2 (PubMed:8824288). Forms a ternary complex with SQSTM1 and PRKCZ (By similarity). {ECO:0000250|UniProtKB:P62483, ECO:0000250|UniProtKB:Q13303, ECO:0000269|PubMed:8576199, ECO:0000269|PubMed:8824288}. DOMAIN: In contrast to KCNAB1, the shorter N-terminal domain of KCNAB2 cannot mediate closure of delayed rectifier potassium channels by physically obstructing the pore. {ECO:0000250|UniProtKB:Q13303}. TISSUE SPECIFICITY: Detected in brain (PubMed:21357749). Detected at basket cell terminals in cerebellum and in the juxtaparanodal region of nodes of Ranvier (at protein level) (PubMed:11825900). Strongest expression in brain and eye. Highest levels in brain detected in brainstem and diencephalon. Strong expression also detected in lung and heart. Moderate expression in kidney, T-lymphocytes and skeletal muscle. {ECO:0000269|PubMed:11825900, ECO:0000269|PubMed:1573677, ECO:0000269|PubMed:21357749, ECO:0000269|PubMed:8824288}. +P97382 KCAB3_MOUSE Voltage-gated potassium channel subunit beta-3 (K(+) channel subunit beta-3) (Kv-beta-3) 249 27,749 Chain (1) FUNCTION: Accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. Alters the functional properties of Kv2.2 but not Kv2.1. {ECO:0000269|PubMed:8824288}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. SUBUNIT: Forms heteromultimeric complex with alpha subunits. DOMAIN: Alteration of functional properties of alpha subunit is mediated through N-terminal domain of beta subunit. {ECO:0000305}. TISSUE SPECIFICITY: Strong expression in brain, with highest levels in neocortical and allocortical regions, hippocampus, olfactory bulb and cerebellum. Also strong in kidney. Weak expression in lung, skeletal muscle and heart. {ECO:0000269|PubMed:8824288}. +P22907 HEM3_MOUSE Porphobilinogen deaminase (PBG-D) (EC 2.5.1.61) (Hydroxymethylbilane synthase) (HMBS) (Pre-uroporphyrinogen synthase) 361 39,344 Alternative sequence (1); Chain (1); Erroneous gene model prediction (1); Initiator methionine (1); Modified residue (5); Sequence conflict (10) Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4. FUNCTION: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. +Q9QYK9 KCC1B_MOUSE Calcium/calmodulin-dependent protein kinase type 1B (EC 2.7.11.17) (CaM kinase I beta) (CaM kinase IB) (CaM-KI beta) (CaMKI-beta) (Pregnancy up-regulated non-ubiquitously-expressed CaM kinase homolog) 343 38,519 Active site (1); Binding site (1); Chain (1); Domain (1); Erroneous initiation (1); Modified residue (1); Nucleotide binding (1); Region (1) FUNCTION: Calcium/calmodulin-dependent protein kinase belonging to a proposed calcium-triggered signaling cascade. In vitro phosphorylates CREB1 and SYN1/synapsin I. Phosphorylates and activates CAMK1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10537072}. Nucleus {ECO:0000269|PubMed:10537072}. TISSUE SPECIFICITY: Expressed at highest levels in adult brain, and expressed in embryo. In the adult brain detected at high levels in the anterior olfactory nuclei, piriform cortex, septal nuclei, bed nuclei of the stria terminalis, hippocampal pyramidal cells, dentate granule cells, amygdala, hypothalamic nuclei, parabrachial nucleus, and nucleus of the solitary tract. Expressed at lower levels in adult ovary and heart and at very low levels in testis, lung and muscle. {ECO:0000269|PubMed:10537072, ECO:0000269|PubMed:10673339}. +Q8BW96 KCC1D_MOUSE Calcium/calmodulin-dependent protein kinase type 1D (EC 2.7.11.17) (CaM kinase I delta) (CaM-KI delta) (CaMKI delta) (CaM kinase ID) (CaMKI-like protein kinase) (CKLiK) (mCKLiK) 385 42,919 Active site (1); Alternative sequence (2); Binding site (1); Chain (1); Cross-link (1); Domain (1); Modified residue (2); Motif (1); Mutagenesis (3); Nucleotide binding (1); Region (2); Sequence conflict (2) FUNCTION: Calcium/calmodulin-dependent protein kinase that operates in the calcium-triggered CaMKK-CaMK1 signaling cascade and, upon calcium influx, activates CREB-dependent gene transcription, regulates calcium-mediated granulocyte function and respiratory burst and promotes basal dendritic growth of hippocampal neurons. In neutrophil cells, required for cytokine-induced proliferative responses and activation of the respiratory burst. Activates the transcription factor CREB1 in hippocampal neuron nuclei. May play a role in apoptosis of erythroleukemia cells. In vitro, phosphorylates transcription factor CREM isoform Beta (By similarity). Isoform 1 but not isoform 2 activates CREB1. {ECO:0000250, ECO:0000269|PubMed:14980499, ECO:0000269|PubMed:18400360}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Predominantly cytoplasmic. Nuclear upon activation. {ECO:0000250}. DOMAIN: The autoinhibitory domain overlaps with the calmodulin binding region and interacts in the inactive folded state with the catalytic domain as a pseudosubstrate. {ECO:0000250}. TISSUE SPECIFICITY: Expressed ubiquitously with high levels in brain and low levels in kidney. Isoform 2 is highly expressed in brain compared to other tissues. In hematopoietic cell lines predominant expression was detected in T and EC cells. {ECO:0000269|PubMed:14980499}. +P11798 KCC2A_MOUSE Calcium/calmodulin-dependent protein kinase type II subunit alpha (CaM kinase II subunit alpha) (CaMK-II subunit alpha) (EC 2.7.11.17) 478 54,115 Active site (1); Alternative sequence (3); Beta strand (7); Binding site (1); Chain (1); Domain (1); Helix (5); Modified residue (9); Mutagenesis (3); Nucleotide binding (1); Region (2); Sequence conflict (3); Turn (1) FUNCTION: Calcium/calmodulin-dependent protein kinase that functions autonomously after Ca(2+)/calmodulin-binding and autophosphorylation, and is involved in synaptic plasticity, neurotransmitter release and long-term potentiation. Member of the NMDAR signaling complex in excitatory synapses, it regulates NMDAR-dependent potentiation of the AMPAR and therefore excitatory synaptic transmission (By similarity). Regulates dendritic spine development. Also regulates the migration of developing neurons (By similarity). Phosphorylates the transcription factor FOXO3 to activate its transcriptional activity (PubMed:23805378). {ECO:0000250|UniProtKB:P11275, ECO:0000250|UniProtKB:Q9UQM7, ECO:0000269|PubMed:23805378}. PTM: Autophosphorylation of Thr-286 following activation by Ca(2+)/calmodulin. Phosphorylation of Thr-286 locks the kinase into an activated state. {ECO:0000269|PubMed:28130356}. SUBCELLULAR LOCATION: Isoform Alpha KAP: Cytoplasm {ECO:0000305|PubMed:8524307}.; SUBCELLULAR LOCATION: Cell junction, synapse {ECO:0000250|UniProtKB:P11275}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250|UniProtKB:P11275}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:Q9UQM7}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9UQM7}. Note=Postsynaptic lipid rafts. {ECO:0000250|UniProtKB:P11275}. SUBUNIT: There are 4 genes encoding calcium/calmodulin-dependent protein kinase type II chains: CAMK2A, CAMK2B, CAMK2G and CAMK2D. The corresponding proteins assemble into homo- or heteromultimeric holoenzymes composed of 12 subunits with two hexameric rings stacked one on top of the other (By similarity). Interacts with BAALC. Interacts with MPDZ. Interacts with SYN1. Interacts with CAMK2N2. Interacts with SYNGAP1. Interacts with SYNPO2 (By similarity). Interacts with SHANK3. Interacts with GRIN2B. Interacts with CACNB2. Interacts with LRRC7. Interacts with GRM5 (By similarity). {ECO:0000250|UniProtKB:P11275, ECO:0000250|UniProtKB:Q9UQM7}. TISSUE SPECIFICITY: Isoform Alpha CaMKII is expressed in brain while isoform Alpha KAP is expressed in skeletal muscle. {ECO:0000269|PubMed:8524307}. +Q80ZA0 ITL1B_MOUSE Intelectin-1b (Intelectin-2) 313 35,070 Binding site (1); Chain (1); Disulfide bond (4); Domain (1); Glycosylation (1); Lipidation (1); Metal binding (11); Propeptide (1); Region (1); Signal peptide (1) FUNCTION: May play a protective role in the innate immune response to parasite infection. {ECO:0000305}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8WWA0}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q8WWA0}. Secreted {ECO:0000250|UniProtKB:Q8WWA0}. TISSUE SPECIFICITY: Expressed in the globlet and Paneth cells of the small intestine of infected mice. Expressed in the ileum of uninfected mice. +Q8VC88 GRAN_MOUSE Grancalcin 220 24,663 Calcium binding (2); Chain (1); Domain (4); Sequence conflict (2) FUNCTION: Calcium-binding protein that may play a role in the adhesion of neutrophils to fibronectin. May play a role in the formation of focal adhesions. {ECO:0000269|PubMed:16934789}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P28676}. Cytoplasmic granule membrane {ECO:0000250|UniProtKB:P28676}; Peripheral membrane protein {ECO:0000250|UniProtKB:P28676}; Cytoplasmic side {ECO:0000250|UniProtKB:P28676}. Note=Primarily cytosolic in the absence of calcium or magnesium ions. Relocates to granules and other membranes in response to elevated calcium and magnesium levels. {ECO:0000250|UniProtKB:P28676}. SUBUNIT: Homodimer. Interacts with SRI and LCP1 (By similarity). {ECO:0000250}. +O89051 ITM2B_MOUSE Integral membrane protein 2B (Immature BRI2) (imBRI2) (Protein E25B) (Transmembrane protein BRI) (Bri) [Cleaved into: BRI2, membrane form (Mature BRI2) (mBRI2); BRI2 intracellular domain (BRI2 ICD); BRI2C, soluble form; Bri23 peptide (Bri2-23) (ABri23) (C-terminal peptide) (P23 peptide)] 266 30,260 Chain (4); Disulfide bond (3); Domain (1); Glycosylation (1); Peptide (1); Region (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 55 75 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 54 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 76 266 Lumenal. {ECO:0000255}. FUNCTION: Plays a regulatory role in the processing of the amyloid-beta A4 precursor protein (APP) and acts as an inhibitor of the amyloid-beta peptide aggregation and fibrils deposition. Plays a role in the induction of neurite outgrowth. Functions as a protease inhibitor by blocking access of secretases to APP cleavage sites (By similarity). {ECO:0000250}.; FUNCTION: Mature BRI2 (mBRI2) functions as a modulator of the amyloid-beta A4 precursor protein (APP) processing leading to a strong reduction in the secretion of secretase-processed amyloid-beta protein 40 and amyloid-beta protein 42. {ECO:0000250}.; FUNCTION: Bri23 peptide prevents aggregation of APP amyloid-beta protein 42 into toxic oligomers. {ECO:0000250}. PTM: The ectodomain C-terminal part of the imBRI2 is processed by furin producing a secreted Bri23 peptide and a mature BRI2, membrane form (mBRI2). The remaining part of the ectodomain of mBRI2 containing the BRICHOS domain is cleaved by ADAM10 and is secreted (BRI2C, soluble form). The membrane-bound N-terminal fragment (BRI2C, membrane form) is further proteolytically processed by SPPL2A and SPPL2B through regulated intramembrane proteolysis producing a secreted C-peptide and a BRI2 intracellular domain (BRI2 ICD) released in the cytosol. Shedding by ADAM10 facilitates intramembrane cleavage but is not absolutely required for BRI2 ICD generation (By similarity). {ECO:0000250}.; PTM: Glycosylation at Asn-170 is important for cell surface localization, but doesn't affect furin- and ADAM10-induced proteolytic processing. {ECO:0000250}. SUBCELLULAR LOCATION: Integral membrane protein 2B: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9Y287}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9Y287}. Note=Immature BRI2 (imBRI2) is cleaved by furin in the Golgi into mBRI2 and a Bri23 peptide. mBRI2 is transported to the plasma membrane and Bri23 peptide is secreted. {ECO:0000250|UniProtKB:Q9Y287}.; SUBCELLULAR LOCATION: BRI2, membrane form: Cell membrane {ECO:0000250|UniProtKB:Q9Y287}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9Y287}. Endosome membrane {ECO:0000250|UniProtKB:Q9Y287}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9Y287}. Note=Mature BRI2 (mBRI2) needs to be transported from the endoplasmic reticulum compartment to the cell membrane in order to be able to inhibit APP processing. {ECO:0000250|UniProtKB:Q9Y287}.; SUBCELLULAR LOCATION: Bri23 peptide: Secreted {ECO:0000250|UniProtKB:Q9Y287}. Note=Detected in the cerebral spinal fluid (CSF). {ECO:0000250|UniProtKB:Q9Y287}.; SUBCELLULAR LOCATION: BRI2C, soluble form: Secreted {ECO:0000250|UniProtKB:Q9Y287}. SUBUNIT: Homodimer; disulfide-linked. Interacts with SPPL2A and SPPL2B. Interacts with APP. Mature BRI2 (mBRI2) interacts with the APP amyloid-beta A4 protein; the interaction occurs at the cell surface and in the endocytic compartments and enable alpha- and beta-secretase-induced APP cleavage inhibition. Mature BRI2 (mBRI2) interacts with the APP C99; the interaction occurs in the endocytic compartments and enable gamma-secretase-induced C99 cleavage inhibition. May form heterodimers with Bri23 peptide and APP amyloid-beta protein 40 (By similarity). {ECO:0000250}. +O89100 GRAP2_MOUSE GRB2-related adaptor protein 2 (Adapter protein GRID) (GADS protein) (GRB-2-like protein) (GRB2L) (GRB-2-related monocytic adapter protein) (MONA) (Monocytic adapter) (GRBLG) (Growth factor receptor-binding protein) (Hematopoietic cell-associated adaptor protein GrpL) 322 36,810 Beta strand (14); Chain (1); Domain (3); Helix (3); Modified residue (5); Turn (1) FUNCTION: Interacts with SLP-76 to regulate NF-AT activation. Binds to tyrosine-phosphorylated shc. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Endosome {ECO:0000250}. SUBUNIT: Interacts with phosphorylated LAT and LAX1 upon TCR activation. Interacts with SHB. Interacts with PTPN23 (By similarity). Interacts with phosphorylated LIME1 upon TCR activation. {ECO:0000250, ECO:0000269|PubMed:14610044}. +Q9JLM9 GRB14_MOUSE Growth factor receptor-bound protein 14 (GRB14 adapter protein) 538 60,573 Chain (1); Domain (3); Initiator methionine (1); Modified residue (3) FUNCTION: Adapter protein which modulates coupling of cell surface receptor kinases with specific signaling pathways. Binds to, and suppresses signals from, the activated insulin receptor (INSR). Potent inhibitor of insulin-stimulated MAPK3 phosphorylation. Plays a critical role regulating PDPK1 membrane translocation in response to insulin stimulation and serves as an adapter protein to recruit PDPK1 to activated insulin receptor, thus promoting PKB/AKT1 phosphorylation and transduction of the insulin signal (By similarity). {ECO:0000250}. PTM: Phosphorylated on serine residues. Phosphorylated on tyrosine residues by TEK/TIE2 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14449}. Endosome membrane {ECO:0000250|UniProtKB:Q14449}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q14449}. Note=Upon insulin stimulation, translocates to the plasma membrane. {ECO:0000250|UniProtKB:Q14449}. SUBUNIT: Interacts with the cytoplasmic domain of the autophosphorylated insulin receptor, through the SH2 domain. Interacts with GRB14 (via BPS domain); this interaction protects the tyrosines in the activation loop on INSR from dephosphorylation (By similarity). Binds to the ankyrin repeat region of TNKS2 via its N-terminus. Interacts with activated NRAS (By similarity). Interacts (via SH2 domain) with TEK/TIE2 (tyrosine phosphorylated). {ECO:0000250, ECO:0000269|PubMed:10521483}. DOMAIN: The PH domain binds relatively non-specifically and with low affinity to several phosphoinositides, the best binder being PI(3,4,5)P3. {ECO:0000250}. +Q9Z2W9 GRIA3_MOUSE Glutamate receptor 3 (GluR-3) (AMPA-selective glutamate receptor 3) (GluR-C) (GluR-K3) (Glutamate receptor ionotropic, AMPA 3) (GluA3) 888 100,527 Beta strand (6); Binding site (3); Chain (1); Disulfide bond (2); Erroneous initiation (1); Glycosylation (5); Helix (7); Intramembrane (2); Lipidation (2); Modified residue (2); Region (2); Sequence conflict (6); Signal peptide (1); Topological domain (5); Transmembrane (3); Turn (2) INTRAMEM 597 612 Helical; Pore-forming. {ECO:0000250}.; INTRAMEM 613 615 {ECO:0000250}. TRANSMEM 547 567 Helical. {ECO:0000250}.; TRANSMEM 622 642 Helical. {ECO:0000250}.; TRANSMEM 818 838 Helical; Name=M4. {ECO:0000250}. TOPO_DOM 23 546 Extracellular. {ECO:0000250}.; TOPO_DOM 568 596 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 616 621 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 643 817 Extracellular. {ECO:0000250}.; TOPO_DOM 839 888 Cytoplasmic. {ECO:0000250}. FUNCTION: Receptor for glutamate that functions as ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. In the presence of CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of glutamate (By similarity). {ECO:0000250}. PTM: Palmitoylated. Depalmitoylated upon glutamate stimulation. Cys-615 palmitoylation leads to Golgi retention and decreased cell surface expression. In contrast, Cys-841 palmitoylation does not affect cell surface expression but regulates stimulation-dependent endocytosis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Interaction with CNIH2 and CNIH3 promotes cell surface expression. {ECO:0000250}. SUBUNIT: Homotetramer or heterotetramer of pore-forming glutamate receptor subunits. Tetramers may be formed by the dimerization of dimers. Interacts with PRKCABP, GRIP1 and GRIP2 (By similarity). Found in a complex with GRIA1, GRIA2, GRIA4, CNIH2, CNIH3, CACNG2, CACNG3, CACNG4, CACNG5, CACNG7 and CACNG8. Interacts with CACNG5 (By similarity). {ECO:0000250}. DOMAIN: The M4 transmembrane segment mediates tetramerization and is required for cell surface expression. {ECO:0000250}. +Q14BI2 GRM2_MOUSE Metabotropic glutamate receptor 2 (mGluR2) 872 95,887 Binding site (4); Chain (1); Disulfide bond (8); Glycosylation (5); Region (2); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 569 589 Helical; Name=1. {ECO:0000255}.; TRANSMEM 605 625 Helical; Name=2. {ECO:0000255}.; TRANSMEM 634 651 Helical; Name=3. {ECO:0000255}.; TRANSMEM 680 700 Helical; Name=4. {ECO:0000255}.; TRANSMEM 727 747 Helical; Name=5. {ECO:0000255}.; TRANSMEM 761 781 Helical; Name=6. {ECO:0000255}.; TRANSMEM 799 819 Helical; Name=7. {ECO:0000255}. TOPO_DOM 19 568 Extracellular. {ECO:0000255}.; TOPO_DOM 590 604 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 626 633 Extracellular. {ECO:0000255}.; TOPO_DOM 652 679 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 701 726 Extracellular. {ECO:0000255}.; TOPO_DOM 748 760 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 782 798 Extracellular. {ECO:0000255}.; TOPO_DOM 820 872 Cytoplasmic. {ECO:0000255}. FUNCTION: G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Signaling inhibits adenylate cyclase activity. May mediate suppression of neurotransmission or may be involved in synaptogenesis or synaptic stabilization. {ECO:0000269|PubMed:18297054, ECO:0000269|PubMed:23129762}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell junction, synapse. Cell projection, dendrite. SUBUNIT: Interacts with GRASP (By similarity). Interacts with HTR2A. {ECO:0000250, ECO:0000269|PubMed:18297054}. TISSUE SPECIFICITY: Detected in neurons in brain cortex (at protein level). {ECO:0000269|PubMed:18297054, ECO:0000269|PubMed:23129762}. +O70291 GRK4_MOUSE G protein-coupled receptor kinase 4 (EC 2.7.11.16) (G protein-coupled receptor kinase GRK4) 574 66,928 Active site (1); Binding site (1); Chain (1); Domain (3); Modified residue (2); Nucleotide binding (1); Region (1); Sequence conflict (1) FUNCTION: Specifically phosphorylates the activated forms of G protein-coupled receptors. PTM: Palmitoylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cell cortex {ECO:0000250}. SUBUNIT: Interacts with DRD3. {ECO:0000250}. +Q5FWH3 GRHL3_MOUSE Grainyhead-like protein 3 homolog (Transcription factor CP2-like 4) 603 67,816 Chain (1); Region (1) FUNCTION: Transcription factor playing important roles in primary neurulation and in the differentiation of stratified epithelia of both ectodermal and endodermal origin. Binds directly to the consensus DNA sequence 5'-AACCGGTT-3' acting as an activator and repressor on distinct target genes. Essential for epidermal differentiation and barrier formation at the end of embryogenesis with TGM3 as critical direct target (PubMed:21081122, PubMed:20654612, PubMed:25347468). Exhibits functional redundancy with GRHL2 in epidermal morphogenetic events such as eyelid fusion and epidermal wound repair (PubMed:21081122). Despite being dispensable during normal epidermal homeostasis in the adulthood, is again required for barrier repair after immune-mediated epidermal damage, regulates distinct gene batteries in embryonic epidermal differentiation and adult epidermal barrier reformation after injury (PubMed:25347468). Plays unique and cooperative roles with GRHL2 in establishing distinct zones of primary neurulation. Essential for spinal closure, functions cooperatively with GRHL2 in closure 2 (forebrain/midbrain boundary) and posterior neuropore closure (PubMed:14608380, PubMed:20654612). Also required for proper development of the oral periderm (PubMed:24360809). No genetic interaction with GRHL1, no functional cooperativity due to diverse target gene selectivity (PubMed:21081122). {ECO:0000269|PubMed:14608380, ECO:0000269|PubMed:16949565, ECO:0000269|PubMed:20654612, ECO:0000269|PubMed:21081122, ECO:0000269|PubMed:24360809, ECO:0000269|PubMed:25347468}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21081122}. SUBUNIT: Homodimer, also forms heterodimers with GRHL1 and GRHL2 (By similarity). Interacts with LMO4 (PubMed:16949565). {ECO:0000250|UniProtKB:Q8TE85, ECO:0000269|PubMed:16949565}. +Q68ED2 GRM7_MOUSE Metabotropic glutamate receptor 7 (mGluR7) 915 102,219 Binding site (4); Chain (1); Disulfide bond (8); Glycosylation (4); Modified residue (1); Region (1); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 591 615 Helical; Name=1. {ECO:0000255}.; TRANSMEM 628 648 Helical; Name=2. {ECO:0000255}.; TRANSMEM 655 675 Helical; Name=3. {ECO:0000255}.; TRANSMEM 703 723 Helical; Name=4. {ECO:0000255}.; TRANSMEM 754 775 Helical; Name=5. {ECO:0000255}.; TRANSMEM 789 810 Helical; Name=6. {ECO:0000255}.; TRANSMEM 826 850 Helical; Name=7. {ECO:0000255}. TOPO_DOM 35 590 Extracellular. {ECO:0000255}.; TOPO_DOM 616 627 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 649 654 Extracellular. {ECO:0000255}.; TOPO_DOM 676 702 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 724 753 Extracellular. {ECO:0000255}.; TOPO_DOM 776 788 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 811 825 Extracellular. {ECO:0000255}.; TOPO_DOM 851 915 Cytoplasmic. {ECO:0000255}. FUNCTION: G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with PICK1. {ECO:0000250}. +Q9QUG9 GRP2_MOUSE RAS guanyl-releasing protein 2 (Calcium and DAG-regulated guanine nucleotide exchange factor I) (CalDAG-GEFI) (F25B3.3 kinase-like protein) 608 69,446 Alternative sequence (3); Calcium binding (2); Chain (1); Domain (4); Erroneous initiation (1); Modified residue (5); Sequence conflict (16); Zinc finger (1) FUNCTION: Functions as a calcium- and DAG-regulated nucleotide exchange factor specifically activating Rap through the exchange of bound GDP for GTP. May also activates other GTPases such as RRAS, RRAS2, NRAS, KRAS but not HRAS. Functions in aggregation of platelets and adhesion of T-lymphocytes and neutrophils probably through inside-out integrin activation. May function in the muscarinic acetylcholine receptor M1/CHRM1 signaling pathway. {ECO:0000269|PubMed:10777492, ECO:0000269|PubMed:10913189, ECO:0000269|PubMed:11278453, ECO:0000269|PubMed:11432821, ECO:0000269|PubMed:12239348, ECO:0000269|PubMed:15334074, ECO:0000269|PubMed:16357324, ECO:0000269|PubMed:17492052, ECO:0000269|PubMed:9789079}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell junction, synapse, synaptosome {ECO:0000250}. Cell projection, ruffle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=Found both in the cytosol and associated with membranes. Enriched at juxtamembrane areas and membrane ruffles. Localizes to the cell bodies and axons of striatal neurons. {ECO:0000250}. SUBUNIT: Forms a signaling complex with RAP1 and BRAF. Interacts with F-actin (By similarity). Interacts with RAP1. {ECO:0000250, ECO:0000269|PubMed:15334074}. DOMAIN: The N-terminal Ras-GEF domain mediates association with F-actin. {ECO:0000250}. TISSUE SPECIFICITY: Detected in megakaryocytes, platelet and neutrophils but not in lymphocytes (at protein level). Isoform 1 and isoform 3 are detected in brain basal glanglia, heart, lung, spleen, liver and kidney interstitial cells. {ECO:0000269|PubMed:10835426, ECO:0000269|PubMed:11278453, ECO:0000269|PubMed:15334074}. +Q99LP6 GRPE1_MOUSE GrpE protein homolog 1, mitochondrial (Mt-GrpE#1) 217 24,307 Chain (1); Modified residue (6); Transit peptide (1) FUNCTION: Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. Seems to control the nucleotide-dependent binding of mitochondrial HSP70 to substrate proteins (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. SUBUNIT: Probable component of the PAM complex at least composed of a mitochondrial HSP70 protein, GRPEL1 or GRPEL2, TIMM44, TIMM16/PAM16 and TIMM14/DNAJC19. Binds to HSP70, HSC70 and HSJ1B (By similarity). {ECO:0000250}. +P12850 GROA_MOUSE Growth-regulated alpha protein (C-X-C motif chemokine 1) (Platelet-derived growth factor-inducible protein KC) (Secretory protein N51) [Cleaved into: KC(5-72) (Hematopoietic synergistic factor) (HSF) (KC-T)] 96 10,254 Chain (2); Disulfide bond (2); Signal peptide (1) FUNCTION: Has chemotactic activity for neutrophils. Contributes to neutrophil activation during inflammation (By similarity). Hematoregulatory chemokine, which, in vitro, suppresses hematopoietic progenitor cell proliferation. KC(5-72) shows a highly enhanced hematopoietic activity. {ECO:0000250, ECO:0000269|PubMed:10725737}. PTM: The N-terminal processed form KC(5-72) is produced by proteolytic cleavage after secretion from bone marrow stromal cells. {ECO:0000269|PubMed:10725737}. SUBCELLULAR LOCATION: Secreted. +Q9D8T2 GSDMD_MOUSE Gasdermin-D (Gasdermin domain-containing protein 1) [Cleaved into: Gasdermin-D, N-terminal (GSDMD-NT); Gasdermin-D, C-terminal (GSDMD-CT)] 487 53,238 Beta strand (4); Chain (3); Helix (12); Modified residue (1); Mutagenesis (16); Site (2); Turn (1) FUNCTION: Gasdermin-D, N-terminal: Promotes pyroptosis in response to microbial infection and danger signals. Produced by the cleavage of gasdermin-D by inflammatory caspases CASP1 or CASP4 in response to canonical, as well as non-canonical (such as cytosolic LPS) inflammasome activators (PubMed:26611636, PubMed:26375259, PubMed:26375003, PubMed:27418190, PubMed:27385778, PubMed:27383986). After cleavage, moves to the plasma membrane where it strongly binds to membrane inner leaflet lipids, including monophosphorylated phosphatidylinositols, such as phosphatidylinositol 4-phosphate, bisphosphorylated phosphatidylinositols, such as phosphatidylinositol (4,5)-bisphosphate, as well as phosphatidylinositol (3,4,5)-trisphosphate, and more weakly to phosphatidic acid and phosphatidylserine. Homooligomerizes within the membrane and forms pores of 10 - 15 nanometers (nm) of inner diameter, allowing the release of mature IL1B and triggering pyroptosis. Exhibits bactericidal activity. Gasdermin-D, N-terminal released from pyroptotic cells into the extracellular milieu rapidly binds to and kills both Gram-negative and Gram-positive bacteria, without harming neighboring mammalian cells, as it does not disrupt the plasma membrane from the outside due to lipid-binding specificity. Under cell culture conditions, also active against intracellular bacteria, such as Listeria monocytogenes. Strongly binds to bacterial and mitochondrial lipids, including cardiolipin. Does not bind to phosphatidylethanolamine or phosphatidylcholine (PubMed:27383986). {ECO:0000269|PubMed:26375003, ECO:0000269|PubMed:26375259, ECO:0000269|PubMed:26611636, ECO:0000269|PubMed:27383986, ECO:0000269|PubMed:27385778, ECO:0000269|PubMed:27418190}. PTM: Cleavage at Asp-276 by CASP1 (mature and uncleaved precursor forms) or CASP4 relieves autoinhibition and is sufficient to initiate pyroptosis (PubMed:26375259, PubMed:26611636). Cleavage at Asp-88 by CASP3 (By similarity). {ECO:0000250|UniProtKB:P57764, ECO:0000269|PubMed:26375259, ECO:0000269|PubMed:26611636}. SUBCELLULAR LOCATION: Gasdermin-D: Cytoplasm, cytosol {ECO:0000269|PubMed:27383986, ECO:0000269|PubMed:27418190}. Inflammasome {ECO:0000269|PubMed:26611636}. Note=In response to a canonical inflammasome stimulus, such as nigericin, recruited to NLRP3 inflammasone with similar kinetics to that of uncleaved CASP1 precursor. {ECO:0000269|PubMed:26611636}.; SUBCELLULAR LOCATION: Gasdermin-D, N-terminal: Cell membrane {ECO:0000269|PubMed:27383986, ECO:0000269|PubMed:27418190}. Secreted {ECO:0000269|PubMed:27383986}. Note=Released in the extracellular milieu following pyroptosis. {ECO:0000269|PubMed:27383986}. SUBUNIT: In response to a canonical inflammasome stimulus, such as nigericin, recruited to NLRP3 inflammasone with similar kinetics to that of uncleaved CASP1 precursor. Although this recruitment is also observed in the absence of PYCARD, it is more efficient in its presence (PubMed:26611636). Gasdermin-D, N-terminal forms disulfide-linked homooligomers (16-mers) in a Ca(+2)-independent manner. Oligomerization occurs in the presence of membranes; remains monomeric in the cytosol (PubMed:27383986). {ECO:0000269|PubMed:26611636, ECO:0000269|PubMed:27383986}. DOMAIN: Intramolecular interactions between N- and C-terminal domains may be important for autoinhibition in the absence of cleavage by inflammatory caspases CASP1 or CASP4. The intrinsic pyroptosis-inducing activity is carried by gasdermin-D, N-terminal, that is released upon cleavage by inflammatory caspases. {ECO:0000269|PubMed:26375003, ECO:0000269|PubMed:26375259, ECO:0000269|PubMed:26611636}. +Q9D9J7 IZUM1_MOUSE Izumo sperm-egg fusion protein 1 (Oocyte binding/fusion factor) (OBF) (Sperm-specific protein izumo) 397 44,885 Beta strand (10); Chain (1); Disulfide bond (5); Domain (1); Glycosylation (1); Helix (10); Modified residue (1); Mutagenesis (7); Region (1); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (2) TRANSMEM 320 340 Helical. {ECO:0000255}. TOPO_DOM 22 319 Extracellular. {ECO:0000255}.; TOPO_DOM 341 397 Cytoplasmic. {ECO:0000255}. FUNCTION: Essential sperm cell-surface protein required for fertilization by acting as a ligand for IZUMO1R/JUNO receptor on egg (PubMed:15759005, PubMed:24739963, PubMed:27309808). The IZUMO1:IZUMO1R/JUNO interaction is a necessary adhesion event between sperm and egg that is required for fertilization but is not sufficient for cell fusion (PubMed:15759005, PubMed:24739963, PubMed:27309808). The ligand-receptor interaction probably does not act as a membrane 'fusogen' (PubMed:15759005, PubMed:24739963, PubMed:27309808). {ECO:0000269|PubMed:15759005, ECO:0000269|PubMed:24739963, ECO:0000269|PubMed:27309808}. PTM: N-glycosylated. Glycosylation is not essential for fusion and for proper protein trafficking in sperm. {ECO:0000269|PubMed:18952059}.; PTM: Phosphorylated (PubMed:19658160, PubMed:27624483). The cytoplasmic C-terminus is phosphorylated and undergoes phosphorylation changes during epididymal transit (PubMed:27624483). {ECO:0000269|PubMed:19658160, ECO:0000269|PubMed:27624483}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25209248, ECO:0000269|PubMed:27309808, ECO:0000305|PubMed:19658160}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, acrosome membrane {ECO:0000269|PubMed:20421979, ECO:0000269|PubMed:27309808}; Single-pass type I membrane protein {ECO:0000255}. Note=Localizes initially to the acrosome membrane of the sperm head (both outer and inner acrosomal membranes). During the acrosome reaction, translocates to the plasma membrane. {ECO:0000269|PubMed:27624483}. SUBUNIT: Monomer, homodimer and homooligomer; depending on the context (PubMed:19658160, PubMed:26568141, PubMed:29954238). Interacts with IZUMO1R/JUNO (PubMed:25209248, PubMed:24739963, PubMed:27309808). IZUMO1 and IZUMO1R/JUNO form a complex with 1:1 stoichiometry (By similarity). In gamete recognition, IZUMO1R/JUNO first binds to monomeric IZUMO1 (PubMed:26568141, PubMed:29954238). The weak, but specific interaction with IZUMO1R/JUNO induces IZUMO1 homodimerization (PubMed:26568141, PubMed:29954238). The process follows a tight binding phase where IZUMO1 bends the entire structure towards the sperm membrane side through a thiol-disulfide exchange reaction (PubMed:26568141, PubMed:29954238). The molecule no longer binds to IZUMO1R/JUNO and instead binds to a putative second oocyte receptor (PubMed:26568141, PubMed:29954238). Interacts with ACE3 (PubMed:20421979). {ECO:0000250|UniProtKB:Q8IYV9, ECO:0000269|PubMed:19658160, ECO:0000269|PubMed:20421979, ECO:0000269|PubMed:24739963, ECO:0000269|PubMed:25209248, ECO:0000269|PubMed:26568141, ECO:0000269|PubMed:27309808, ECO:0000269|PubMed:29954238}. DOMAIN: The extracellular domain assumes a distinct boomerang shape when not bound to IZUMO1R/JUNO (By similarity). Interaction with IZUMO1R/JUNO triggers a conformation change, so that the IZUMO1 extracellular domain assumes an upright conformation (By similarity). {ECO:0000250|UniProtKB:Q8IYV9}.; DOMAIN: The cytoplasmic C-terminus region is not essential for fertilization (PubMed:27624483). It is however required for protein stability (PubMed:27624483). {ECO:0000269|PubMed:27624483}. TISSUE SPECIFICITY: Sperm-specific (at protein level) (PubMed:15759005, PubMed:19658160, PubMed:20421979). Detectable on sperm surface only after the acrosome reaction (PubMed:15759005). {ECO:0000269|PubMed:15759005, ECO:0000269|PubMed:19658160, ECO:0000269|PubMed:20421979}. +D3Z7H4 GSG1L_MOUSE Germ cell-specific gene 1-like protein (GSG1-like protein) 322 35,889 Chain (1); Modified residue (1); Topological domain (5); Transmembrane (4) TRANSMEM 9 29 Helical. {ECO:0000255}.; TRANSMEM 123 143 Helical. {ECO:0000255}.; TRANSMEM 164 184 Helical. {ECO:0000255}.; TRANSMEM 208 228 Helical. {ECO:0000255}. TOPO_DOM 1 8 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 30 122 Extracellular. {ECO:0000255}.; TOPO_DOM 144 163 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 185 207 Extracellular. {ECO:0000255}.; TOPO_DOM 229 322 Cytoplasmic. {ECO:0000255}. FUNCTION: As a component of the inner core of AMPAR complexes, modifies AMPA receptor (AMPAR) gating. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22632720}; Multi-pass membrane protein {ECO:0000269|PubMed:22632720}. Cell junction, synapse {ECO:0000250}. SUBUNIT: Component of the inner core of AMPAR complexes. AMPAR complexes consist of an inner core made of 4 pore-forming GluA/GRIA proteins (GRIA1, GRIA2, GRIA3 and GRIA4) and 4 major auxiliary subunits arranged in a twofold symmetry. One of the two pairs of distinct binding sites is occupied either by CNIH2, CNIH3 or CACNG2, CACNG3. The other harbors CACNG2, CACNG3, CACNG4, CACNG8 or GSG1L. This inner core of AMPAR complexes is complemented by outer core constituents binding directly to the GluA/GRIA proteins at sites distinct from the interaction sites of the inner core constituents. Outer core constituents include at least PRRT1, PRRT2, CKAMP44/SHISA9, FRRS1L and NRN1. The proteins of the inner and outer core serve as a platform for other, more peripherally associated AMPAR constituents. Alone or in combination, these auxiliary subunits control the gating and pharmacology of the AMPAR complexes and profoundly impact their biogenesis and protein processing. {ECO:0000269|PubMed:22632720}. TISSUE SPECIFICITY: Expressed in the brain, including hippocampus (at protein level). {ECO:0000269|PubMed:22632720}. +Q8R1W2 GSG1_MOUSE Germ cell-specific gene 1 protein (Germ cell-associated protein 1) 324 36,108 Alternative sequence (4); Chain (1); Erroneous initiation (1); Frameshift (1); Sequence conflict (1); Transmembrane (4) TRANSMEM 15 35 Helical. {ECO:0000255}.; TRANSMEM 127 147 Helical. {ECO:0000255}.; TRANSMEM 164 184 Helical. {ECO:0000255}.; TRANSMEM 208 228 Helical. {ECO:0000255}. FUNCTION: May cause the redistribution of PAPOLB from the cytosol to the endoplasmic reticulum. {ECO:0000269|PubMed:18325338}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18325338}; Multi-pass membrane protein {ECO:0000269|PubMed:18325338}. Note=Colocalizes with PAPOLB in the endoplasmic reticulum. SUBUNIT: Interacts with PAPOLB. {ECO:0000269|PubMed:18325338}. TISSUE SPECIFICITY: Expressed in spermatogenic cells (at protein level). Expressed in germ cells within the testis from day 21 onwards. {ECO:0000269|PubMed:18325338, ECO:0000269|PubMed:7957958}. +O09172 GSH0_MOUSE Glutamate--cysteine ligase regulatory subunit (GCS light chain) (Gamma-ECS regulatory subunit) (Gamma-glutamylcysteine synthetase regulatory subunit) (Glutamate--cysteine ligase modifier subunit) 274 30,535 Chain (1); Modified residue (2) Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 1/2. SUBUNIT: Heterodimer of a catalytic heavy chain and a regulatory light chain. +Q9D4P7 GSTT4_MOUSE Glutathione S-transferase theta-4 (EC 2.5.1.18) (GST class-theta-4) 240 28,099 Binding site (1); Chain (1); Domain (2); Region (2) FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. {ECO:0000250|UniProtKB:P30711}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P30711}. +P10649 GSTM1_MOUSE Glutathione S-transferase Mu 1 (EC 2.5.1.18) (GST 1-1) (GST class-mu 1) (Glutathione S-transferase GT8.7) (pmGT10) 218 25,970 Binding site (2); Chain (1); Domain (2); Initiator methionine (1); Mass spectrometry (1); Modified residue (3); Region (4) FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Homodimer. +Q9R0Y5 KAD1_MOUSE Adenylate kinase isoenzyme 1 (AK 1) (EC 2.7.4.3) (EC 2.7.4.6) (ATP-AMP transphosphorylase 1) (ATP:AMP phosphotransferase) (Adenylate monophosphate kinase) (Myokinase) 194 21,540 Alternative sequence (1); Binding site (7); Chain (1); Erroneous gene model prediction (1); Modified residue (2); Nucleotide binding (3); Region (2) FUNCTION: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Also possesses broad nucleoside diphosphate kinase activity. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism (By similarity). May provide a mechanism to buffer the adenylate energy charge for sperm motility. {ECO:0000250, ECO:0000269|PubMed:16790685}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03171}. SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03171}. DOMAIN: Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis. {ECO:0000255|HAMAP-Rule:MF_03171}. +Q07133 H1T_MOUSE Histone H1t (Testicular H1 histone) 208 21,540 Chain (1); Domain (1); Initiator methionine (1); Modified residue (6); Sequence conflict (3); Site (1) FUNCTION: Testis-specific histone H1 that forms less compacted chromatin compared to other H1 histone subtypes. Formation of more relaxed chromatin may be required to promote chromatin architecture required for proper chromosome regulation during meiosis, such as homologous recombination. Histones H1 act as linkers that bind to nucleosomes and compact polynucleosomes into a higher-order chromatin configuration. {ECO:0000250|UniProtKB:P22492}. PTM: Phosphorylated in early spermatids. {ECO:0000269|PubMed:19043117}.; PTM: Citrullination at Arg-56 (H1R54ci) by PADI4 takes place within the DNA-binding site of H1 and results in its displacement from chromatin and global chromatin decondensation, thereby promoting pluripotency and stem cell maintenance. {ECO:0000250|UniProtKB:P43275}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome {ECO:0000305}. TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:8241275}. +C0HKE9 H2A1P_MOUSE Histone H2A type 1-P 130 14,135 Chain (1); Cross-link (3); Initiator methionine (1); Modified residue (24) FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. PTM: Deiminated on Arg-4 in granulocytes upon calcium entry. {ECO:0000250|UniProtKB:P0C0S8}.; PTM: Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM27 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is involved in the initiation of both imprinted and random X inactivation. Ubiquitinated H2A is enriched in inactive X chromosome chromatin. Ubiquitination of H2A functions downstream of methylation of 'Lys-27' of histone H3 (H3K27me). H2AK119Ub by RNF2/RING2 can also be induced by ultraviolet and may be involved in DNA repair. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties by the E2 ligase UBE2N and the E3 ligases RNF8 and RNF168, leading to the recruitment of repair proteins to sites of DNA damage. Ubiquitination at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) in response to DNA damage is initiated by RNF168 that mediates monoubiquitination at these 2 sites, and 'Lys-63'-linked ubiquitin are then conjugated to monoubiquitin; RNF8 is able to extend 'Lys-63'-linked ubiquitin chains in vitro. Deubiquitinated by USP51 at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) after damaged DNA is repaired (By similarity). H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination (H2AK13Ub and H2AK15Ub) are distinct events. {ECO:0000250|UniProtKB:P0C0S8, ECO:0000269|PubMed:15509584, ECO:0000269|PubMed:15525528, ECO:0000269|PubMed:24352239}.; PTM: Phosphorylation on Ser-2 (H2AS1ph) is enhanced during mitosis. Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses transcription. Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1. Phosphorylation at Thr-121 (H2AT120ph) by DCAF1 is present in the regulatory region of many tumor suppresor genes and down-regulates their transcription. {ECO:0000250|UniProtKB:P0C0S8, ECO:0000269|PubMed:7217105}.; PTM: Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage. {ECO:0000269|PubMed:16699504}.; PTM: Glutamine methylation at Gln-105 (H2AQ104me) by FBL is specifically dedicated to polymerase I. It is present at 35S ribosomal DNA locus and impairs binding of the FACT complex. {ECO:0000269|PubMed:24352239}.; PTM: Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes. {ECO:0000269|PubMed:21925322}.; PTM: Hydroxybutyrylation of histones is induced by starvation. {ECO:0000269|PubMed:27105115}. SUBCELLULAR LOCATION: Nucleus. Chromosome. SUBUNIT: The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. +Q8R1M2 H2AJ_MOUSE Histone H2A.J (H2a/j) 129 14,045 Chain (1); Initiator methionine (1); Modified residue (4) FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. PTM: Monoubiquitination of Lys-120 (H2AXK119ub) gives a specific tag for epigenetic transcriptional repression. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties (By similarity). {ECO:0000250}.; PTM: Glutamine methylation at Gln-105 (H2AQ104me) by FBL is specifically dedicated to polymerase I. It is present at 35S ribosomal DNA locus and impairs binding of the FACT complex (By similarity). {ECO:0000250}.; PTM: Phosphorylation on Ser-2 (H2AS1ph) is enhanced during mitosis. Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses transcription. Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1. Phosphorylation at Thr-121 (H2AT120ph) by DCAF1 is present in the regulatory region of many tumor suppresor genes and down-regulates their transcription (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}. SUBUNIT: The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. +Q5M8Q2 H2AL1_MOUSE Histone H2A-like 1 (H2A.L.1) (H2AL1) (Histone H2Alike 1) 105 12,122 Chain (1) FUNCTION: Atypical histone H2A which can replace conventional H2A in some nucleosomes and may play a role during spermatogenesis. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. {ECO:0000305|PubMed:17261847}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17261847}. Chromosome {ECO:0000269|PubMed:17261847}. Note=Specifically localizes to the pericentric regions in condensing spermatids (PubMed:17261847). {ECO:0000269|PubMed:17261847}. SUBUNIT: The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. May be incorporated into a proportion of nucleosomes, replacing one or more H2A molecules. Interacts with HIST1H2BA/TH2B; preferentially dimerizes with HIST1H2BA/TH2B to form nucleosomes (PubMed:17261847). {ECO:0000269|PubMed:17261847}. TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:17261847}. +Q3THW5 H2AV_MOUSE Histone H2A.V (H2A.F/Z) 128 13,509 Chain (1); Initiator methionine (1); Modified residue (3); Sequence conflict (2) FUNCTION: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. May be involved in the formation of constitutive heterochromatin. May be required for chromosome segregation during cell division (By similarity). {ECO:0000250}. PTM: Monoubiquitination of Lys-122 gives a specific tag for epigenetic transcriptional repression. {ECO:0000250}.; PTM: Acetylated on Lys-5, Lys-8 and Lys-12 during interphase. Acetylation disappears at mitosis. {ECO:0000269|PubMed:16204459}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}. SUBUNIT: The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. H2A or its variant H2AFV forms a heterodimer with H2B (By similarity). {ECO:0000250}. +Q9QZQ8 H2AY_MOUSE Core histone macro-H2A.1 (Histone macroH2A1) (mH2A1) (H2A.y) (H2A/y) 372 39,735 Alternative sequence (2); Chain (1); Compositional bias (1); Cross-link (6); Domain (2); Modified residue (8) FUNCTION: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes where it represses transcription. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Involved in stable X chromosome inactivation. Inhibits the binding of transcription factors, including NF-kappa-B, and interferes with the activity of remodeling SWI/SNF complexes (By similarity). Inhibits histone acetylation by EP300 and recruits class I HDACs, which induces a hypoacetylated state of chromatin (By similarity) (PubMed:16107708). {ECO:0000250|UniProtKB:O75367, ECO:0000269|PubMed:16107708}.; FUNCTION: Isoform 1: Binds ADP-ribose and O-acetyl-ADP-ribose, and may be involved in ADP-ribose-mediated chromatin modulation (By similarity). Increases the expression of genes involved in redox metabolism, including SOD3 (PubMed:23022728). {ECO:0000250|UniProtKB:O75367, ECO:0000269|PubMed:23022728}.; FUNCTION: Isoform 2: Represses SOD3 gene expression. {ECO:0000269|PubMed:23022728}. PTM: Monoubiquitinated at either Lys-116 or Lys-117. May also be polyubiquitinated. Ubiquitination is mediated by the CUL3/SPOP E3 complex and does not promote proteasomal degradation. Instead, it is required for enrichment in inactive X chromosome chromatin (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15564378, ECO:0000269|PubMed:9634239}. Chromosome {ECO:0000269|PubMed:15564378, ECO:0000269|PubMed:9634239}. Note=Enriched in inactive X chromosome chromatin and in senescence-associated heterochromatin (PubMed:9634239). In quiescent lymphocytes, associated with centromeric constitutive heterochromatin (PubMed:15564378). {ECO:0000269|PubMed:15564378, ECO:0000269|PubMed:9634239}. SUBUNIT: The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. Interacts with SPOP. Part of a complex consisting of H2AFY, CUL3 and SPOP. Interacts with HDAC1 and HDAC2 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed, with high levels in testis. Present in liver, kidney and adrenal gland (at protein level). In the liver, present in hepatocytes and at a lesser extent in cells of the bile ducts. In the kidney, expressed in proximal and distal convoluted tubules and in straight proximal tubules. In the adrenal gland, present in inner cells of the cortex and medulla. {ECO:0000269|PubMed:10471737, ECO:0000269|PubMed:11262398}. +Q64475 H2B1B_MOUSE Histone H2B type 1-B (h2B-143) 126 13,952 Chain (1); Cross-link (4); Glycosylation (1); Initiator methionine (1); Modified residue (52) FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. PTM: Monoubiquitination at Lys-35 (H2BK34Ub) by the MSL1/MSL2 dimer is required for histone H3 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) methylation and transcription activation at specific gene loci, such as HOXA9 and MEIS1 loci. Similarly, monoubiquitination at Lys-121 (H2BK120Ub) by the RNF20/40 complex gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation. It also functions cooperatively with the FACT dimer to stimulate elongation by RNA polymerase II. H2BK120Ub also acts as a regulator of mRNA splicing: deubiquitination by USP49 is required for efficient cotranscriptional splicing of a large set of exons (By similarity). {ECO:0000250|UniProtKB:P33778}.; PTM: Phosphorylated on Ser-15 (H2BS14ph) by STK4/MST1 during apoptosis; which facilitates apoptotic chromatin condensation. Also phosphorylated on Ser-15 in response to DNA double strand breaks (DSBs), and in correlation with somatic hypermutation and immunoglobulin class-switch recombination. Phosphorylation at Ser-37 (H2BS36ph) by AMPK in response to stress promotes transcription. {ECO:0000269|PubMed:15197225, ECO:0000269|PubMed:16039583, ECO:0000269|PubMed:20647423}.; PTM: GlcNAcylation at Ser-113 promotes monoubiquitination of Lys-121. It fluctuates in response to extracellular glucose, and associates with transcribed genes (By similarity). {ECO:0000250|UniProtKB:P62807}.; PTM: Hydroxybutyrylation of histones is induced by starvation. {ECO:0000269|PubMed:27105115}.; PTM: Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes. {ECO:0000269|PubMed:21925322}. SUBCELLULAR LOCATION: Nucleus. Chromosome. SUBUNIT: The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. +Q64524 H2B2E_MOUSE Histone H2B type 2-E (H2b 613) 126 13,993 Chain (1); Cross-link (4); Initiator methionine (1); Modified residue (52) FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. PTM: Monoubiquitination at Lys-35 (H2BK34Ub) by the MSL1/MSL2 dimer is required for histone H3 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) methylation and transcription activation at specific gene loci, such as HOXA9 and MEIS1 loci. Similarly, monoubiquitination at Lys-121 (H2BK120Ub) by the RNF20/40 complex gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation. It also functions cooperatively with the FACT dimer to stimulate elongation by RNA polymerase II. H2BK120Ub also acts as a regulator of mRNA splicing: deubiquitination by USP49 is required for efficient cotranscriptional splicing of a large set of exons (By similarity). {ECO:0000250|UniProtKB:P33778}.; PTM: Phosphorylated on Ser-15 (H2BS14ph) by STK4/MST1 during apoptosis; which facilitates apoptotic chromatin condensation. Also phosphorylated on Ser-15 in response to DNA double strand breaks (DSBs), and in correlation with somatic hypermutation and immunoglobulin class-switch recombination. Phosphorylation at Ser-37 (H2BS36ph) by AMPK in response to stress promotes transcription. {ECO:0000269|PubMed:15197225, ECO:0000269|PubMed:16039583, ECO:0000269|PubMed:20647423}.; PTM: Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes. {ECO:0000269|PubMed:21925322}.; PTM: Hydroxybutyrylation of histones is induced by starvation. {ECO:0000269|PubMed:27105115}. SUBCELLULAR LOCATION: Nucleus. Chromosome. SUBUNIT: The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. +P10853 H2B1F_MOUSE Histone H2B type 1-F/J/L (H2B 291A) 126 13,936 Chain (1); Cross-link (4); Glycosylation (1); Initiator methionine (1); Modified residue (52) FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. PTM: Monoubiquitination at Lys-35 (H2BK34Ub) by the MSL1/MSL2 dimer is required for histone H3 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) methylation and transcription activation at specific gene loci, such as HOXA9 and MEIS1 loci. Similarly, monoubiquitination at Lys-121 (H2BK120Ub) by the RNF20/40 complex gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation. It also functions cooperatively with the FACT dimer to stimulate elongation by RNA polymerase II. H2BK120Ub also acts as a regulator of mRNA splicing: deubiquitination by USP49 is required for efficient cotranscriptional splicing of a large set of exons (By similarity). {ECO:0000250|UniProtKB:P33778}.; PTM: Phosphorylated on Ser-15 (H2BS14ph) by STK4/MST1 during apoptosis; which facilitates apoptotic chromatin condensation. Also phosphorylated on Ser-15 in response to DNA double strand breaks (DSBs), and in correlation with somatic hypermutation and immunoglobulin class-switch recombination. Phosphorylation at Ser-37 (H2BS36ph) by AMPK in response to stress promotes transcription. {ECO:0000269|PubMed:15197225, ECO:0000269|PubMed:16039583, ECO:0000269|PubMed:20647423}.; PTM: GlcNAcylation at Ser-113 promotes monoubiquitination of Lys-121. It fluctuates in response to extracellular glucose, and associates with transcribed genes (By similarity). {ECO:0000250|UniProtKB:P62807}.; PTM: Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes. {ECO:0000269|PubMed:21925322}.; PTM: Hydroxybutyrylation of histones is induced by starvation. {ECO:0000269|PubMed:27105115}. SUBCELLULAR LOCATION: Nucleus. Chromosome. SUBUNIT: The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. +Q8CGP1 H2B1K_MOUSE Histone H2B type 1-K 126 13,920 Chain (1); Cross-link (4); Glycosylation (1); Initiator methionine (1); Modified residue (52) FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. PTM: Monoubiquitination at Lys-35 (H2BK34Ub) by the MSL1/MSL2 dimer is required for histone H3 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) methylation and transcription activation at specific gene loci, such as HOXA9 and MEIS1 loci. Similarly, monoubiquitination at Lys-121 (H2BK120Ub) by the RNF20/40 complex gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation. It also functions cooperatively with the FACT dimer to stimulate elongation by RNA polymerase II. H2BK120Ub also acts as a regulator of mRNA splicing: deubiquitination by USP49 is required for efficient cotranscriptional splicing of a large set of exons (By similarity). {ECO:0000250|UniProtKB:P33778}.; PTM: Phosphorylated on Ser-15 (H2BS14ph) by STK4/MST1 during apoptosis; which facilitates apoptotic chromatin condensation. Also phosphorylated on Ser-15 in response to DNA double strand breaks (DSBs), and in correlation with somatic hypermutation and immunoglobulin class-switch recombination. Phosphorylation at Ser-37 (H2BS36ph) by AMPK in response to stress promotes transcription. {ECO:0000269|PubMed:15197225, ECO:0000269|PubMed:16039583, ECO:0000269|PubMed:20647423}.; PTM: GlcNAcylation at Ser-113 promotes monoubiquitination of Lys-121. It fluctuates in response to extracellular glucose, and associates with transcribed genes (By similarity). {ECO:0000250|UniProtKB:P62807}.; PTM: Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes. {ECO:0000269|PubMed:21925322}.; PTM: Hydroxybutyrylation of histones is induced by starvation. {ECO:0000269|PubMed:27105115}. SUBCELLULAR LOCATION: Nucleus. Chromosome. SUBUNIT: The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. +Q8CGP2 H2B1P_MOUSE Histone H2B type 1-P 126 13,992 Alternative sequence (1); Chain (1); Cross-link (4); Initiator methionine (1); Modified residue (52); Sequence conflict (2) FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. PTM: Monoubiquitination at Lys-35 (H2BK34Ub) by the MSL1/MSL2 dimer is required for histone H3 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) methylation and transcription activation at specific gene loci, such as HOXA9 and MEIS1 loci. Similarly, monoubiquitination at Lys-121 (H2BK120Ub) by the RNF20/40 complex gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation. It also functions cooperatively with the FACT dimer to stimulate elongation by RNA polymerase II. H2BK120Ub also acts as a regulator of mRNA splicing: deubiquitination by USP49 is required for efficient cotranscriptional splicing of a large set of exons (By similarity). {ECO:0000250|UniProtKB:P33778}.; PTM: Phosphorylated on Ser-15 (H2BS14ph) by STK4/MST1 during apoptosis; which facilitates apoptotic chromatin condensation. Also phosphorylated on Ser-15 in response to DNA double strand breaks (DSBs), and in correlation with somatic hypermutation and immunoglobulin class-switch recombination. Phosphorylation at Ser-37 (H2BS36ph) by AMPK in response to stress promotes transcription. {ECO:0000269|PubMed:15197225, ECO:0000269|PubMed:16039583, ECO:0000269|PubMed:20647423}.; PTM: Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes. {ECO:0000269|PubMed:21925322}.; PTM: Hydroxybutyrylation of histones is induced by starvation. {ECO:0000269|PubMed:27105115}. SUBCELLULAR LOCATION: Nucleus. Chromosome. SUBUNIT: The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. +P62806 H4_MOUSE Histone H4 103 11,367 Beta strand (3); Chain (1); Cross-link (7); DNA binding (1); Helix (4); Initiator methionine (1); Modified residue (57); Sequence conflict (3) FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. PTM: Acetylation at Lys-6 (H4K5ac), Lys-9 (H4K8ac), Lys-13 (H4K12ac) and Lys-17 (H4K16ac) occurs in coding regions of the genome but not in heterochromatin. {ECO:0000250|UniProtKB:P62805}.; PTM: Citrullination at Arg-4 (H4R3ci) by PADI4 impairs methylation. {ECO:0000269|PubMed:15145825, ECO:0000269|PubMed:16699504}.; PTM: Monomethylation and asymmetric dimethylation at Arg-4 (H4R3me1 and H4R3me2a, respectively) by PRMT1 favors acetylation at Lys-9 (H4K8ac) and Lys-13 (H4K12ac). Demethylation is performed by JMJD6. Symmetric dimethylation on Arg-4 (H4R3me2s) by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage (By similarity). {ECO:0000250|UniProtKB:P62805}.; PTM: Monomethylated, dimethylated or trimethylated at Lys-21 (H4K20me1, H4K20me2, H4K20me3). Monomethylation is performed by SET8. Trimethylation is performed by KMT5B and KMT5C and induces gene silencing (By similarity). {ECO:0000250|UniProtKB:P62805}.; PTM: Phosphorylated by PAK2 at Ser-48 (H4S47ph). This phosphorylation increases the association of H3.3-H4 with the histone chaperone HIRA, thus promoting nucleosome assembly of H3.3-H4 and inhibiting nucleosome assembly of H3.1-H4 (By similarity). {ECO:0000250|UniProtKB:P62805}.; PTM: Ubiquitinated by the CUL4-DDB-RBX1 complex in response to ultraviolet irradiation. This may weaken the interaction between histones and DNA and facilitate DNA accessibility to repair proteins. Monoubiquitinated at Lys-92 of histone H4 (H4K91ub1) in response to DNA damage. The exact role of H4K91ub1 in DNA damage response is still unclear but it may function as a licensing signal for additional histone H4 post-translational modifications such as H4 Lys-21 methylation (H4K20me) (By similarity). {ECO:0000250|UniProtKB:P62805}.; PTM: Sumoylated, which is associated with transcriptional repression. {ECO:0000250|UniProtKB:P62805}.; PTM: Butyrylation of histones marks active promoters and competes with histone acetylation. It is present during late spermatogenesis. {ECO:0000269|PubMed:27105113}.; PTM: Hydroxybutyrylation of histones is induced by starvation. {ECO:0000269|PubMed:27105115}.; PTM: Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes. {ECO:0000269|PubMed:21925322}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}. SUBUNIT: The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. {ECO:0000269|PubMed:11101893}. +B1B213 H60C_MOUSE Histocompatibility antigen 60c 197 22,340 Chain (1); Glycosylation (3); Lipidation (1); Propeptide (1); Signal peptide (1) FUNCTION: Ligand for the KLRK1 immunosurveillance receptor. Binding to KLRK1 stimulates cell lysis in vitro. {ECO:0000269|PubMed:18209064}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18209064}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:18209064}. TISSUE SPECIFICITY: Expressed in skin, and weakly in large intestine. {ECO:0000269|PubMed:18209064}. +P01897 HA1L_MOUSE H-2 class I histocompatibility antigen, L-D alpha chain 362 40,711 Beta strand (20); Chain (1); Disulfide bond (2); Domain (1); Erroneous initiation (1); Glycosylation (3); Helix (6); Modified residue (2); Region (4); Sequence conflict (12); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (5) TRANSMEM 310 331 Helical. {ECO:0000255}. TOPO_DOM 25 309 Extracellular. {ECO:0000255}.; TOPO_DOM 332 362 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in the presentation of foreign antigens to the immune system. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2-microglobulin). +P01895 HA1Y_MOUSE H-2 class I histocompatibility antigen, alpha chain (Clone PAG64) (Fragment) 298 33,850 Alternative sequence (1); Chain (1); Disulfide bond (2); Domain (1); Glycosylation (2); Modified residue (2); Natural variant (3); Non-terminal residue (1); Topological domain (2); Transmembrane (1) TRANSMEM 245 265 Helical. {ECO:0000255}. TOPO_DOM <1 244 Extracellular. {ECO:0000255}.; TOPO_DOM 266 298 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in the presentation of foreign antigens to the immune system. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2-microglobulin). +P04228 HA2D_MOUSE H-2 class II histocompatibility antigen, A-D alpha chain 256 28,243 Beta strand (14); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (1); Helix (2); Region (3); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (3) TRANSMEM 219 244 Helical. {ECO:0000255}. TOPO_DOM 24 218 Extracellular. {ECO:0000255}.; TOPO_DOM 245 256 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +P14435 HA2F_MOUSE H-2 class II histocompatibility antigen, A-F alpha chain 233 25,930 Chain (1); Disulfide bond (1); Domain (1); Glycosylation (1); Region (3); Topological domain (2); Transmembrane (1) TRANSMEM 196 221 Helical. {ECO:0000255}. TOPO_DOM 1 195 Extracellular. {ECO:0000255}.; TOPO_DOM 222 233 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +P14436 HA2R_MOUSE H-2 class II histocompatibility antigen, A-R alpha chain 233 25,900 Chain (1); Disulfide bond (1); Domain (1); Glycosylation (1); Region (3); Topological domain (2); Transmembrane (1) TRANSMEM 196 221 Helical. {ECO:0000255}. TOPO_DOM 1 195 Extracellular. {ECO:0000255}.; TOPO_DOM 222 233 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +P14437 HA2S_MOUSE H-2 class II histocompatibility antigen, A-S alpha chain 233 25,801 Chain (1); Disulfide bond (1); Domain (1); Glycosylation (1); Region (3); Topological domain (2); Transmembrane (1) TRANSMEM 196 221 Helical. {ECO:0000255}. TOPO_DOM 1 195 Extracellular. {ECO:0000255}.; TOPO_DOM 222 233 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +P14438 HA2U_MOUSE H-2 class II histocompatibility antigen, A-U alpha chain (Fragment) 227 25,136 Beta strand (12); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (1); Helix (2); Non-terminal residue (1); Region (3); Topological domain (2); Transmembrane (1); Turn (3) TRANSMEM 190 215 Helical. {ECO:0000255}. TOPO_DOM <1 189 Extracellular. {ECO:0000255}.; TOPO_DOM 216 227 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q8K0D2 HABP2_MOUSE Hyaluronan-binding protein 2 (EC 3.4.21.-) (Plasma hyaluronan-binding protein) [Cleaved into: Hyaluronan-binding protein 2 50 kDa heavy chain; Hyaluronan-binding protein 2 50 kDa heavy chain alternate form; Hyaluronan-binding protein 2 27 kDa light chain; Hyaluronan-binding protein 2 27 kDa light chain alternate form] 558 62,357 Active site (3); Alternative sequence (1); Chain (4); Disulfide bond (17); Domain (5); Erroneous initiation (1); Signal peptide (1); Site (3) FUNCTION: Cleaves the alpha-chain at multiple sites and the beta-chain between 'Lys-53' and 'Lys-54' but not the gamma-chain of fibrinogen and therefore does not initiate the formation of the fibrin clot and does not cause the fibrinolysis directly. It does not cleave (activate) prothrombin and plasminogen but converts the inactive single chain urinary plasminogen activator (pro-urokinase) to the active two chain form. Activates coagulation factor VII (By similarity). {ECO:0000250}. PTM: Proteolytic cleavage at Gly-23 or Met-27 can give rise to the 50 kDa heavy chain and cleavage at Arg-311 or Lys-317 can give rise to the 27 kDa light chain. The heavy chain can undergo further proteolytic cleavage at Arg-168 or Arg-169 to give rise to 2 inactive 26 kDa fragments and the light chain can undergo further proteolytic cleavage at Arg-478 to give rise to inactive 17 kDa and 8 kDa fragments. SUBCELLULAR LOCATION: Secreted. Note=Secreted as an inactive single-chain precursor and is then activated to a heterodimeric form. SUBUNIT: Heterodimer; disulfide-linked. Heterodimer of a 50 kDa heavy and a 27 kDa light chain linked by a disulfide bond. TISSUE SPECIFICITY: Liver and kidney. {ECO:0000269|PubMed:9401717}. +Q9DB32 HAGHL_MOUSE Hydroxyacylglutathione hydrolase-like protein (EC 3.1.2.-) 283 31,490 Alternative sequence (2); Chain (1); Metal binding (8) FUNCTION: Hydrolase acting on ester bonds. {ECO:0000305}. +Q9QXE0 HACL1_MOUSE 2-hydroxyacyl-CoA lyase 1 (EC 4.1.-.-) (2-hydroxyphytanoyl-CoA lyase) (2-HPCL) (Phytanoyl-CoA 2-hydroxylase 2) 581 63,660 Binding site (1); Chain (1); Metal binding (2); Modified residue (5); Motif (1); Region (1); Sequence conflict (1) Lipid metabolism; fatty acid metabolism. FUNCTION: Catalyzes a carbon-carbon cleavage reaction; cleaves a 2-hydroxy-3-methylacyl-CoA into formyl-CoA and a 2-methyl-branched fatty aldehyde. {ECO:0000250}. SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}. SUBUNIT: Homotetramer. {ECO:0000250}. +Q9WU19 HAOX1_MOUSE Hydroxyacid oxidase 1 (HAOX1) (EC 1.1.3.15) (Glycolate oxidase) (GOX) 370 41,001 Active site (1); Binding site (9); Chain (1); Domain (1); Modified residue (3); Motif (1); Nucleotide binding (1) Organic acid metabolism; glycolate degradation; 3-phospho-D-glycerate from glycolate: step 1/4. FUNCTION: Has 2-hydroxyacid oxidase activity. Most active on the 2-carbon substrate glycolate, but is also active on 2-hydroxy fatty acids, with high activity towards 2-hydroxy palmitate and 2-hydroxy octanoate (By similarity). {ECO:0000250, ECO:0000269|PubMed:9891009}. SUBCELLULAR LOCATION: Peroxisome. TISSUE SPECIFICITY: Liver. {ECO:0000269|PubMed:9891009}. +Q9NYQ2 HAOX2_MOUSE Hydroxyacid oxidase 2 (HAOX2) (EC 1.1.3.15) ((S)-2-hydroxy-acid oxidase, peroxisomal) (Medium chain alpha-hydroxy acid oxidase) (Medium-chain L-2-hydroxy acid oxidase) 353 38,700 Active site (1); Binding site (8); Chain (1); Domain (1); Modified residue (1); Motif (1); Nucleotide binding (1); Sequence conflict (1) FUNCTION: Has 2-hydroxyacid oxidase activity. Most active on medium-chain substrates. SUBCELLULAR LOCATION: Peroxisome. SUBUNIT: Homotetramer or homooctamer. {ECO:0000250}. TISSUE SPECIFICITY: Pancreas. +O35668 HAP1_MOUSE Huntingtin-associated protein 1 (HAP-1) 628 70,116 Alternative sequence (1); Chain (1); Coiled coil (2); Compositional bias (4); Domain (1); Modified residue (1); Region (4) FUNCTION: Originally identified as neuronal protein that specifically associates with HTT/huntingtin and the binding is enhanced by an expanded polyglutamine repeat within HTT possibly affecting HAP1 interaction properties. Both HTT and HAP1 are involved in intracellular trafficking and HAP1 is proposed to link HTT to motor proteins and/or transport cargos. Seems to play a role in vesicular transport within neurons and axons such as from early endosomes to late endocytic compartments and to promote neurite outgrowth. The vesicular transport function via association with microtubule-dependent transporters can be attenuated by association with mutant HTT. Involved in the axonal transport of BDNF and its activity-dependent secretion; the function seems to involve HTT, DCTN1 and a complex with SORT1. Involved in APP trafficking and seems to facilitate APP anterograde transport and membrane insertion thereby possibly reducing processing into amyloid beta. Involved in delivery of gamma-aminobutyric acid (GABA(A)) receptors to synapses; the function is dependent on kinesin motor protein KIF5 and is disrupted by HTT with expanded polyglutamine repeat. Involved in regulation of autophagosome motility by promoting efficient retrograde axonal transport. Seems to be involved in regulation of membrane receptor recycling and degradation, and respective signal transduction, including GABA(A) receptors, tyrosine kinase receptors, EGFR, IP3 receptor and androgen receptor. Among others suggested to be involved in control of feeding behavior (involving hypothalamic GABA(A) receptors), cerebellar and brainstem development (involving AHI1 and NTRK1/TrkA), postnatal neurogenesis (involving hypothalamic NTRK2/TrkB regulating the number of Npyr1-expressing cells), and ITPR1/InsP3R1-mediated Ca(2+) release (involving HTT and possibly the effect of mutant HTT). Via association with DCTN1/dynactin p150-glued and HTT/huntingtin involved in cytoplasmic retention of REST in neurons. May be involved in ciliogenesiss; however, reports are conflicting: PubMed:21985783 reports that Hap1 is required for ciliogenesis in primary cortical neurons and proposes that HTT interacts with PCM1 through HAP1; PubMed:23532844 reports that mice with disrupted Hap1 display normal cilium formation and function. Involved in regulation of exocytosis. Isoform A but not isoform B seems to be involved in formation of cytoplasmic inclusion bodies (STBs). In case of anomalous expression of TBP, can sequester a subset of TBP into STBs; sequestration is enhanced by an expanded polyglutamine repeat within TBP. {ECO:0000269|PubMed:12890790, ECO:0000269|PubMed:15379999, ECO:0000269|PubMed:17868456, ECO:0000269|PubMed:18636121, ECO:0000269|PubMed:21985783, ECO:0000269|PubMed:24355921, ECO:0000269|PubMed:24366265, ECO:0000269|PubMed:24453320}. PTM: Isoform A is phosphorylated on Thr-598. {ECO:0000250|UniProtKB:P54256}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell projection, axon {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Lysosome {ECO:0000269|PubMed:24453320}. Endoplasmic reticulum {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250}. Mitochondrion {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:24453320}. Note=Localizes to large nonmembrane-bound cytoplasmic bodies found in various types of neurons, called stigmoid bodies (STBs); STB formation is regulated by the ratio of isoform A to isoform B. Localization to neuronal processes and neurite tips is decreased by YWHAZ. In the nucleus localizes to nuclear rods (By similarity). {ECO:0000250}. SUBUNIT: Self-associates. Interacts with HTT/huntingtin; enhanced by an expanded polyglutamine repeat within HTT. Isoform A interacts with DCTN1; decreased in presence of HTT with expanded polyglutamine repeat; decreased by phosphorylation of Hap1 isoform A at Thr-598. Isoform A interacts with KLC2; decreased by phosphorylation of Hap1 isoform A at Thr-598. Isoform A interacts with ITPR1 and APP. Isoform A interacts with AR; decreased by an expanded polyglutamine repeat within AR. Isoform A interacts with YWHAZ; enhanced by phosphorylation of Hap1 isoform A at Thr-598. Isoform A interacts with BDNF and SORT1; probably forming a complex involved in proBDNF trafficking, degradation and processing. Interacts with TBP, AHI1, HGS and KALRN. Interacts with KIF5A, KIF5B, KIF5C and GABRB3; indicative for an HAP1:KIF5 complex transporting a GABA(A) receptor as cargo. Interacts with ATXN3; in STBs. Interacts with NTRK2; HAP1 stabilizes association of NTRK2 with SORT1 preventing NTRK2 degradation. Interacts with CCDC113. {ECO:0000250|UniProtKB:P54257, ECO:0000269|PubMed:17868456, ECO:0000269|PubMed:18636121, ECO:0000269|PubMed:23532844, ECO:0000269|PubMed:23658157}. +Q3UHX2 HAP28_MOUSE 28 kDa heat- and acid-stable phosphoprotein (PDGF-associated protein) (PAP) (PDGFA-associated protein 1) (PAP1) 181 20,605 Chain (1); Cross-link (1); Modified residue (11) PTM: Phosphorylated by several kinases in vitro. In vivo, can be phosphorylated by CK2. +Q8BY71 HAT1_MOUSE Histone acetyltransferase type B catalytic subunit (EC 2.3.1.48) (Histone acetyltransferase 1) 416 49,278 Active site (1); Chain (1); Initiator methionine (1); Modified residue (4); Region (4); Site (1) FUNCTION: Acetylates soluble but not nucleosomal histone H4 at 'Lys-5' (H4K5ac) and 'Lys-12' (H4K12ac) and, to a lesser extent, acetylates histone H2A at 'Lys-5' (H2AK5ac). Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG. May be involved in nucleosome assembly during DNA replication and repair as part of the histone H3.1 and H3.3 complexes. {ECO:0000250|UniProtKB:O14929}. SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000250}. SUBUNIT: Catalytic subunit of the type B histone acetyltransferase (HAT) complex, composed of RBBP7 and HAT1. Interacts with histones H4 and H2A. The interaction is dependent of the ability of RBBP7 to bind to the N-terminus of histones. Component of the histone H3.1 and H3.3 complexes. {ECO:0000250|UniProtKB:O14929}. +Q9D786 HAUS5_MOUSE HAUS augmin-like complex subunit 5 619 69,572 Alternative sequence (2); Chain (1); Coiled coil (3); Erroneous initiation (2); Modified residue (1); Sequence conflict (6) FUNCTION: Contributes to mitotic spindle assembly, maintenance of centrosome integrity and completion of cytokinesis as part of the HAUS augmin-like complex. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Localizes to interphase centrosomes and to mitotic spindle microtubules. {ECO:0000250}. SUBUNIT: Component of the HAUS augmin-like complex. The complex interacts with the gamma-tubulin ring complex and this interaction is required for spindle assembly (By similarity). {ECO:0000250}. +Q5QNS5 HAVR1_MOUSE Hepatitis A virus cellular receptor 1 homolog (HAVcr-1) (Kidney injury molecule 1) (KIM-1) (T cell immunoglobulin and mucin domain-containing protein 1) (TIMD-1) (T cell membrane protein 1) (T-cell immunoglobulin mucin receptor 1) (TIM-1) (CD antigen CD365) 305 33,361 Alternative sequence (1); Beta strand (9); Chain (1); Compositional bias (1); Disulfide bond (3); Domain (1); Glycosylation (1); Helix (2); Natural variant (4); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 238 258 Helical. {ECO:0000255}. TOPO_DOM 22 237 Extracellular. {ECO:0000255}.; TOPO_DOM 259 305 Cytoplasmic. {ECO:0000255}. FUNCTION: May play a role in T-helper cell development and the regulation of asthma and allergic diseases. Receptor for TIMD4. May play a role in kidney injury and repair (By similarity). {ECO:0000250, ECO:0000269|PubMed:15793576}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed by stimulated T-cells. Expressed during primary antigen stimulation. {ECO:0000269|PubMed:11725301}. +Q8VIM0 HAVR2_MOUSE Hepatitis A virus cellular receptor 2 homolog (HAVcr-2) (T-cell immunoglobulin and mucin domain-containing protein 3) (TIMD-3) (T-cell immunoglobulin mucin receptor 3) (TIM-3) (T-cell membrane protein 3) (CD antigen CD366) 281 30,934 Alternative sequence (1); Beta strand (10); Binding site (4); Chain (1); Compositional bias (1); Disulfide bond (3); Domain (1); Glycosylation (4); Helix (2); Metal binding (3); Modified residue (1); Mutagenesis (8); Region (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 194 214 Helical. {ECO:0000255}. TOPO_DOM 20 193 Extracellular. {ECO:0000255}.; TOPO_DOM 215 281 Cytoplasmic. {ECO:0000255}. FUNCTION: Cell surface receptor implicated in modulating innate and adaptive immune responses. Generally accepted to have an inhibiting function. Reports on stimulating functions suggest that the activity may be influenced by the cellular context and/or the respective ligand (PubMed:18006747). Regulates macrophage activation (PubMed:11823861). Inhibits T-helper type 1 lymphocyte (Th1)-mediated auto- and alloimmune responses and promotes immunological tolerance (PubMed:14556006, PubMed:18006747). In CD8+ cells attenuates TCR-induced signaling, specifically by blocking NF-kappaB and NFAT promoter activities resulting in the loss of IL-2 secretion. The function may implicate its association with LCK proposed to impair phosphorylation of TCR subunits (By similarity). In contrast, shown to activate TCR-induced signaling in T-cells probably implicating ZAP70, LCP2, LCK and FYN (PubMed:21807895). Expressed on Treg cells can inhibit Th17 cell responses (By similarity). Receptor for LGALS9. Binding to LGALS9 is believed to result in suppression of T-cell responses; the resulting apoptosis of antigen-specific cells may implicate HAVCR2 phosphorylation and disruption of its association with BAG6 (PubMed:22863785). Binding to LGALS9 is proposed to be involved in innate immune response to intracellular pathogens. Expressed on Th1 cells interacts with LGALS9 expressed on Mycobacterium tuberculosis-infected macrophages to stimulate antibactericidal activity including IL-1 beta secretion and to restrict intracellular bacterial growth (PubMed:20937702). However, the function as receptor for LGALS9 has been challenged (By similarity). Also reported to enhance CD8+ T-cell responses to an acute infection such as by Listeria monocytogenes (PubMed:24567532). Receptor for phosphatidylserine (PtSer); PtSer-binding is calcium-dependent (PubMed:20083673). May recognize PtSer on apoptotic cells leading to their phagocytosis. Mediates the engulfment of apoptotic cells by dendritic cells (PubMed:19224762). Expressed on T-cells, promotes conjugation but not engulfment of apoptotic cells (PubMed:20083673). Expressed on dendritic cells (DCs) positively regulates innate immune response and in synergy with Toll-like receptors promotes secretion of TNF-alpha (PubMed:18006747). In tumor-imfiltrating DCs suppresses nucleic acid-mediated innate immune repsonse by interaction with HMGB1 and interfering with nucleic acid-sensing and trafficking of nucleid acids to endosomes (PubMed:22842346). Can enhance mast cell production of Th2 cytokines Il-4, IL-6 and IL-13 (PubMed:17620455). Expressed on natural killer (NK) cells acts as a coreceptor to enhance IFN-gamma production in response to LGALS9. In contrast, shown to suppress NK cell-mediated cytotoxicity (By similarity). Negatively regulates NK cell function in LPS-induced endotoxic shock (PubMed:25337993). {ECO:0000250|UniProtKB:Q8TDQ0, ECO:0000269|PubMed:11823861, ECO:0000269|PubMed:14556006, ECO:0000269|PubMed:17620455, ECO:0000269|PubMed:18006747, ECO:0000269|PubMed:19224762, ECO:0000269|PubMed:20083673, ECO:0000269|PubMed:20937702, ECO:0000269|PubMed:21807895, ECO:0000269|PubMed:22842346, ECO:0000269|PubMed:24567532, ECO:0000269|PubMed:25337993, ECO:0000305|PubMed:22863785}. PTM: Phosphorylated on tyrosine residues; modestly increased after TCR/CD28 stimulation. Can be phosphorylated in the cytoplasmatic domain by FYN (PubMed:21807895). Phosphorylation at Tyr-256 is increased by stimulation with ligand LGALS9 (By similarity). {ECO:0000250|UniProtKB:Q8TDQ0, ECO:0000269|PubMed:21807895}.; PTM: N-glycosylated. {ECO:0000269|PubMed:21807895}. SUBCELLULAR LOCATION: Isoform 1: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Cell junction {ECO:0000250|UniProtKB:Q8TDQ0}. Note=Localizes to the immunological synapse between CD8+ T-cells and target cells. {ECO:0000250|UniProtKB:Q8TDQ0}.; SUBCELLULAR LOCATION: Isoform 2: Secreted {ECO:0000269|PubMed:14556006}. SUBUNIT: Interacts with HMGB1; impairs HMGB1 binding to B-DNA and likely HMGB1-mediated innate immume response (PubMed:22842346). Interacts with BAG6 (PubMed:22863785). Interacts (phosphorylated) with PIK3R1 and PIK3R2. Interacts (not dependent on its phosphorylation status) with FYN (PubMed:21807895). Interacts (in basal state T-cells) with VAV1; AKT1/2, LCP2, ZAP70, SYK, PIK3R1, FYN, SH3BP2 and SH2D2A. Interacts (in activated T-cells) with LCK and PLCG (By similarity). {ECO:0000250|UniProtKB:Q8TDQ0, ECO:0000269|PubMed:21807895, ECO:0000269|PubMed:22842346, ECO:0000269|PubMed:22863785}. DOMAIN: The Ig-like V-type (immunoglobulin-like) domain mediates binding to PtSer involving a Ca(2+) ion. {ECO:0000269|PubMed:20083673}. TISSUE SPECIFICITY: Expressed in T-helper type 1 lymphocytes. Not expressed by naive T-cells but up-regulated as they differentiate into T-helper-1 cells. Also expressed by differentiated type 1 CD8+ cytotoxic T-cells. Expressed on peritoneal exudate macrophages, monocytes, and splenic dendritic cells (DCs). Expression on natural killer (NK) cells is inversely associated with IFN-gamma production during the initial 24 h of LPS-induced endotoxic shock. Expressed on mast cells. {ECO:0000269|PubMed:11823861, ECO:0000269|PubMed:14556006, ECO:0000269|PubMed:17620455, ECO:0000269|PubMed:19224762, ECO:0000269|PubMed:24567532, ECO:0000269|PubMed:25337993}. +O35387 HAX1_MOUSE HCLS1-associated protein X-1 (HS1-associating protein X-1) (HAX-1) (HS1-binding protein 1) (HSP1BP-1) 280 31,654 Chain (1); Compositional bias (1); Initiator methionine (1); Modified residue (3); Region (9); Site (1) FUNCTION: Recruits the Arp2/3 complex to the cell cortex and regulates reorganization of the cortical actin cytoskeleton via its interaction with KCNC3 and the Arp2/3 complex. Slows down the rate of inactivation of KCNC3 channels. Promotes GNA13-mediated cell migration. Involved in the clathrin-mediated endocytosis pathway. May be involved in internalization of ABC transporters such as ABCB11. May inhibit CASP9 and CASP3. Promotes cell survival. May regulate intracellular calcium pools. {ECO:0000250|UniProtKB:O00165}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16814492}. Endoplasmic reticulum {ECO:0000269|PubMed:10760273}. Nucleus membrane {ECO:0000305|PubMed:16814492}. Cytoplasmic vesicle {ECO:0000269|PubMed:10760273, ECO:0000269|PubMed:16814492}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:O00165}. Cell membrane {ECO:0000250|UniProtKB:O00165}; Peripheral membrane protein {ECO:0000250|UniProtKB:O00165}; Cytoplasmic side {ECO:0000250|UniProtKB:O00165}. Sarcoplasmic reticulum {ECO:0000250|UniProtKB:Q7TSE9}. Cytoplasm, P-body {ECO:0000250|UniProtKB:O00165}. Cytoplasm {ECO:0000250|UniProtKB:O00165}. Nucleus {ECO:0000250|UniProtKB:O00165}. Note=Predominantly cytoplasmic. Also detected in the nucleus when nuclear export is inhibited (in vitro). {ECO:0000250|UniProtKB:O00165}. SUBUNIT: Interacts with ABCB1, ABCB4 and ABCB11 (By similarity). Directly associates with HCLS1/HS1, through binding to its N-terminal region (By similarity). Interacts with CTTN (PubMed:10760273). Interacts with PKD2(PubMed:10760273). Interacts with GNA13. Interacts with CASP9. Interacts with ITGB6. Interacts with PLN and ATP2A2; these interactions are inhibited by calcium. Interacts with GRB7. Interacts (via C-terminus) with XIAP/BIRC4 (via BIR 2 domain and BIR 3 domain) and this interaction blocks ubiquitination of XIAP/BIRC4. Interacts with TPC2. Interacts with KCNC3 (PubMed:26997484). Interacts with XPO1 (By similarity). {ECO:0000250|UniProtKB:O00165, ECO:0000250|UniProtKB:Q7TSE9, ECO:0000269|PubMed:10760273}. TISSUE SPECIFICITY: Ubiquitous, with highest levels in kidney and liver (at protein level). {ECO:0000269|PubMed:16814492}. +P20040 HB24_MOUSE H-2 class II histocompatibility antigen, E-Q beta chain (E-W17) 264 30,205 Chain (1); Disulfide bond (2); Domain (1); Glycosylation (1); Region (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 226 246 Helical. {ECO:0000255}. TOPO_DOM 27 225 Extracellular. {ECO:0000255}.; TOPO_DOM 247 264 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +P06346 HB2F_MOUSE H-2 class II histocompatibility antigen, A-F beta chain (Fragment) 252 28,602 Chain (1); Disulfide bond (2); Domain (1); Glycosylation (1); Non-terminal residue (1); Region (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 214 234 Helical. {ECO:0000255}. TOPO_DOM 17 213 Extracellular. {ECO:0000255}.; TOPO_DOM 235 252 Cytoplasmic. {ECO:0000255}. PTM: Ubiquitinated in immature dendritic cells leading to down-regulation of MHC class II. {ECO:0000269|PubMed:17051151, ECO:0000269|PubMed:17174123}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +P06343 HB2K_MOUSE H-2 class II histocompatibility antigen, A-K beta chain 263 29,967 Beta strand (14); Chain (1); Disulfide bond (2); Domain (1); Glycosylation (1); Helix (7); Region (3); Sequence conflict (8); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (2) TRANSMEM 225 245 Helical. {ECO:0000255}. TOPO_DOM 28 224 Extracellular. {ECO:0000255}.; TOPO_DOM 246 263 Cytoplasmic. {ECO:0000255}. PTM: Ubiquitinated in immature dendritic cells leading to down-regulation of MHC class II. {ECO:0000269|PubMed:17051151, ECO:0000269|PubMed:17174123}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +P06344 HB2U_MOUSE H-2 class II histocompatibility antigen, A-U beta chain 263 30,041 Beta strand (14); Chain (1); Disulfide bond (2); Domain (1); Glycosylation (1); Helix (4); Region (3); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (5) TRANSMEM 225 245 Helical. {ECO:0000255}. TOPO_DOM 28 224 Extracellular. {ECO:0000255}.; TOPO_DOM 246 263 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q8BK58 HBAP1_MOUSE HSPB1-associated protein 1 (27 kDa heat shock protein-associated protein 1) (Protein associated with small stress protein 1) 483 54,395 Chain (1); Domain (1); Region (1); Sequence conflict (1) FUNCTION: May play a role in cellular stress response. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with CRYAB and HSPB1. {ECO:0000269|PubMed:10751411}. +P02088 HBB1_MOUSE Hemoglobin subunit beta-1 (Beta-1-globin) (Hemoglobin beta-1 chain) (Hemoglobin beta-major chain) 147 15,840 Chain (1); Helix (9); Initiator methionine (1); Metal binding (2); Modified residue (8); Natural variant (5); Sequence conflict (5); Turn (1) FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues. SUBUNIT: Heterotetramer of two alpha chains and two beta chains. TISSUE SPECIFICITY: Red blood cells. +P02089 HBB2_MOUSE Hemoglobin subunit beta-2 (Beta-2-globin) (Hemoglobin beta-2 chain) (Hemoglobin beta-minor chain) 147 15,878 Chain (1); Initiator methionine (1); Metal binding (2); Modified residue (9); Natural variant (1) FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues. SUBUNIT: Heterotetramer of two alpha chains and two beta chains. TISSUE SPECIFICITY: Red blood cells. +P04444 HBBZ_MOUSE Hemoglobin subunit beta-H1 (Beta-H1-globin) (Hemoglobin beta-H1 chain) (Protein Z) 147 16,494 Chain (1); Metal binding (2) FUNCTION: This is an embryonic beta-type chain. SUBUNIT: Heterotetramer of two alpha chains and two beta chains. TISSUE SPECIFICITY: Red blood cells. +Q06186 HBEGF_MOUSE Proheparin-binding EGF-like growth factor [Cleaved into: Heparin-binding EGF-like growth factor (HB-EGF) (HBEGF)] 208 22,808 Chain (2); Disulfide bond (3); Domain (1); Glycosylation (1); Propeptide (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 161 184 Helical. {ECO:0000255}. TOPO_DOM 24 160 Extracellular. {ECO:0000255}.; TOPO_DOM 185 208 Cytoplasmic. {ECO:0000255}. FUNCTION: Growth factor that mediates its effects via EGFR, ERBB2 and ERBB4. Required for normal cardiac valve formation and normal heart function. Promotes smooth muscle cell proliferation. May be involved in macrophage-mediated cellular proliferation. It is mitogenic for fibroblasts, but not endothelial cells. It is able to bind EGF receptor/EGFR with higher affinity than EGF itself and is a far more potent mitogen for smooth muscle cells than EGF. Also acts as a diphtheria toxin receptor. PTM: O-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Heparin-binding EGF-like growth factor: Secreted, extracellular space. Note=Mature HB-EGF is released into the extracellular space and probably binds to a receptor.; SUBCELLULAR LOCATION: Proheparin-binding EGF-like growth factor: Cell membrane; Single-pass type I membrane protein. SUBUNIT: Interacts with FBLN1 (By similarity). Interacts with EGFR and ERBB4. {ECO:0000250}. TISSUE SPECIFICITY: Most abundant in kidney, skeletal muscle, lung, spleen, brain and heart. +P02104 HBE_MOUSE Hemoglobin subunit epsilon-Y2 (Epsilon-Y2-globin) (Hemoglobin epsilon-Y2 chain) 147 16,137 Chain (1); Initiator methionine (1); Metal binding (2); Modified residue (1); Natural variant (4) FUNCTION: Hemoglobin epsilon chain is a beta-type chain found in early embryos. TISSUE SPECIFICITY: High expression in yolk sac blood islands, fetal liver, and embryonic erythrocytes. Very low levels in adult liver and spleen. +Q8BN78 KAISO_MOUSE Transcriptional regulator Kaiso (Zinc finger and BTB domain-containing protein 33) 671 74,050 Chain (1); Cross-link (14); Domain (1); Modified residue (1); Motif (1); Mutagenesis (1); Region (5); Sequence conflict (3); Zinc finger (3) FUNCTION: Transcriptional regulator with bimodal DNA-binding specificity. Binds to methylated CpG dinucleotides in the consensus sequence 5'-CGCG-3' and also binds to the non-methylated consensus sequence 5'-CTGCNA-3' also known as the consensus kaiso binding site (KBS). May recruit the N-CoR repressor complex to promote histone deacetylation and the formation of repressive chromatin structures in target gene promoters. Contributes to the repression of target genes of the Wnt signaling pathway. May also activate transcription of a subset of target genes by the recruitment of CTNND2. Represses expression of MMP7 in conjunction with transcriptional corepressors CBFA2T3, CBFA2T2 and RUNX1T1 (By similarity). {ECO:0000250|UniProtKB:Q86T24, ECO:0000269|PubMed:15138284, ECO:0000269|PubMed:15282317, ECO:0000269|PubMed:15564377, ECO:0000269|PubMed:15817151}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10207085, ECO:0000269|PubMed:15282317, ECO:0000269|PubMed:15564377}. SUBUNIT: Interacts with NCOR1 (By similarity). Self-associates. Interacts with CTNND1, and this interaction inhibits binding to both methylated and non-methylated DNA. Interacts with CTNND2. Interacts with KPNA2/RCH1, which may mediate nuclear import of this protein. Interacts with CBFA2T3 (By similarity). {ECO:0000250|UniProtKB:Q86T24, ECO:0000269|PubMed:10207085, ECO:0000269|PubMed:12087177, ECO:0000269|PubMed:15282317, ECO:0000269|PubMed:15564377}. TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver, lung, neuromuscular junctions, skeletal muscle, spleen and testis. {ECO:0000269|PubMed:10207085, ECO:0000269|PubMed:15282317}. +Q5DTI6 KAL1L_MOUSE KAT8 regulatory NSL complex subunit 1-like protein 991 112,525 Alternative sequence (6); Chain (1); Cross-link (1); Erroneous initiation (2); Modified residue (2); Sequence conflict (20) PTM: Acetylated on lysine residues by KAT8 upon ionizing radiation-induced DNA damage; deacetylated by HDAC3. {ECO:0000250}. +Q9Z1P7 KANK3_MOUSE KN motif and ankyrin repeat domain-containing protein 3 (Ankyrin repeat domain-containing protein 47) 791 84,186 Chain (1); Coiled coil (1); Compositional bias (2); Modified residue (7); Repeat (5) FUNCTION: May be involved in the control of cytoskeleton formation by regulating actin polymerization. +Q8BQR4 KANL2_MOUSE KAT8 regulatory NSL complex subunit 2 (NSL complex protein NSL2) (Non-specific lethal 2 homolog) 486 54,173 Alternative sequence (3); Chain (1); Cross-link (1); Erroneous initiation (1); Erroneous translation (1); Frameshift (1); Modified residue (6); Sequence conflict (1) FUNCTION: As part of the NSL complex it is involved in acetylation of nucleosomal histone H4 on several lysine residues and therefore may be involved in the regulation of transcription. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the NSL complex at least composed of MOF/KAT8, KANSL1, KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT, WDR5 and HCFC1. {ECO:0000250}. +Q69ZS7 HBS1L_MOUSE HBS1-like protein 682 75,100 Alternative sequence (3); Chain (1); Domain (1); Erroneous initiation (1); Helix (5); Modified residue (6); Nucleotide binding (3); Region (5); Sequence conflict (4); Turn (1) TISSUE SPECIFICITY: Detected in embryos. {ECO:0000269|PubMed:9872408}. +A2RSY1 KANL3_MOUSE KAT8 regulatory NSL complex subunit 3 (NSL complex protein NSL3) (Non-specific lethal 3 homolog) 903 96,135 Alternative sequence (2); Chain (1); Compositional bias (1); Erroneous initiation (1); Modified residue (4) FUNCTION: As part of the NSL complex it is involved in acetylation of nucleosomal histone H4 on several lysine residues and therefore may be involved in the regulation of transcription. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the NSL complex at least composed of MOF/KAT8, KANSL1, KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT, WDR5 and HCFC1. {ECO:0000250}. +Q9DBC7 KAP0_MOUSE cAMP-dependent protein kinase type I-alpha regulatory subunit [Cleaved into: cAMP-dependent protein kinase type I-alpha regulatory subunit, N-terminally processed] 381 43,185 Binding site (4); Chain (2); Disulfide bond (2); Initiator methionine (1); Modified residue (8); Motif (1); Nucleotide binding (2); Region (1) FUNCTION: Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. {ECO:0000250}. PTM: The pseudophosphorylation site binds to the substrate-binding region of the catalytic chain, resulting in the inhibition of its activity. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. SUBUNIT: The inactive holoenzyme is composed of two regulatory chains and two catalytic chains. Activation by cAMP releases the two active catalytic monomers and the regulatory dimer. PRKAR1A also interacts with RFC2; the complex may be involved in cell survival. Interacts with AKAP4. Interacts with RARA; the interaction occurs in the presence of cAMP or FSH and regulates RARA transcriptional activity. Interacts with the phosphorylated form of PJA2. Interacts with PRKX; regulates this cAMP-dependent protein kinase (By similarity). Interacts with CBFA2T3. Interacts with smAKAP; this interaction may target PRKAR1A to the plasma membrane. Interacts with AICDA (By similarity). {ECO:0000250}. +P31324 KAP3_MOUSE cAMP-dependent protein kinase type II-beta regulatory subunit 416 46,167 Beta strand (13); Binding site (4); Chain (1); Helix (11); Modified residue (3); Nucleotide binding (2); Region (1); Sequence conflict (1) FUNCTION: Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. Type II regulatory chains mediate membrane association by binding to anchoring proteins, including the MAP2 kinase. PTM: Phosphorylated by the activated catalytic chain. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Colocalizes with PJA2 in the cytoplasm and at the cell membrane. {ECO:0000250}. SUBUNIT: The inactive form of the enzyme is composed of two regulatory chains and two catalytic chains. Activation by cAMP produces two active catalytic monomers and a regulatory dimer that binds four cAMP molecules. Interacts with the phosphorylated form of PJA2 (By similarity). Forms a complex composed of PRKAR2B, GSK3B and GSKIP through GSKIP interaction; facilitates PKA-induced phosphorylation and regulates GSK3B activity (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P31323}. TISSUE SPECIFICITY: Four types of regulatory chains are found: I-alpha, I-beta, II-alpha, and II-beta. Their expression varies among tissues and is in some cases constitutive and in others inducible. +Q9D968 HCFC2_MOUSE Host cell factor 2 (HCF-2) (C2 factor) 241 26,178 Beta strand (8); Chain (1); Domain (2); Helix (1) SUBUNIT: Binds KMT2A/MLL1. Component of the MLL1/MLL complex, at least composed of KMT2A/MLL1, ASH2L, RBBP5, DPY30, WDR5, MEN1, HCFC1 and HCFC2. +O88704 HCN1_MOUSE Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 1 (Brain cyclic nucleotide-gated channel 1) (BCNG-1) (Hyperpolarization-activated cation channel 2) (HAC-2) 910 102,432 Beta strand (8); Chain (1); Compositional bias (3); Frameshift (1); Glycosylation (1); Helix (10); Intramembrane (1); Motif (1); Mutagenesis (6); Nucleotide binding (3); Region (1); Sequence conflict (2); Topological domain (8); Transmembrane (6) INTRAMEM 334 355 Pore-forming; Name=Segment H5. {ECO:0000250|UniProtKB:O60741}. TRANSMEM 132 153 Helical; Name=Segment S1. {ECO:0000250|UniProtKB:O60741}.; TRANSMEM 163 183 Helical; Name=Segment S2. {ECO:0000250|UniProtKB:O60741}.; TRANSMEM 205 225 Helical; Name=Segment S3. {ECO:0000250|UniProtKB:O60741}.; TRANSMEM 250 270 Helical; Voltage-sensor; Name=Segment S4. {ECO:0000250|UniProtKB:O60741}.; TRANSMEM 285 307 Helical; Name=Segment S5. {ECO:0000250|UniProtKB:O60741}.; TRANSMEM 361 381 Helical; Name=Segment S6. {ECO:0000250|UniProtKB:O60741}. TOPO_DOM 1 131 Cytoplasmic. {ECO:0000250|UniProtKB:O60741}.; TOPO_DOM 154 162 Extracellular. {ECO:0000250|UniProtKB:O60741}.; TOPO_DOM 184 204 Cytoplasmic. {ECO:0000250|UniProtKB:O60741}.; TOPO_DOM 226 249 Extracellular. {ECO:0000250|UniProtKB:O60741}.; TOPO_DOM 271 284 Cytoplasmic. {ECO:0000250|UniProtKB:O60741}.; TOPO_DOM 308 333 Extracellular. {ECO:0000250|UniProtKB:O60741}.; TOPO_DOM 356 360 Extracellular. {ECO:0000250|UniProtKB:O60741}.; TOPO_DOM 382 910 Cytoplasmic. {ECO:0000250|UniProtKB:O60741}. FUNCTION: Hyperpolarization-activated ion channel exhibiting weak selectivity for potassium over sodium ions. Contributes to the native pacemaker currents in heart (If) and in neurons (Ih). May mediate responses to sour stimuli. {ECO:0000269|PubMed:11459060, ECO:0000269|PubMed:11675786, ECO:0000269|PubMed:12034718, ECO:0000269|PubMed:22006928, ECO:0000269|PubMed:9630217}. PTM: N-glycosylated. {ECO:0000269|PubMed:9405696}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11459060, ECO:0000269|PubMed:22006928, ECO:0000269|PubMed:9630217}; Multi-pass membrane protein {ECO:0000269|PubMed:11459060, ECO:0000269|PubMed:22006928, ECO:0000269|PubMed:9630217}. SUBUNIT: Homotetramer. Heterotetramer with HCN2. The potassium channel is composed of a homo- or heterotetrameric complex of pore-forming subunits. Interacts with KCNE2. Interacts with the SH3 domain of CSK (PubMed:9405696). {ECO:0000269|PubMed:11420311, ECO:0000269|PubMed:12034718, ECO:0000269|PubMed:12089064, ECO:0000269|PubMed:22006928, ECO:0000269|PubMed:9405696}. DOMAIN: The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position. {ECO:0000250|UniProtKB:O60741}. TISSUE SPECIFICITY: Predominantly expressed in brain. Highly expressed in apical dendrites of pyramidal neurons in the cortex, in the layer corresponding to the stratum lacunosum-moleculare in the hippocampus and in axons of basket cells in the cerebellum. Expressed in a subset of elongated cells in taste buds. {ECO:0000269|PubMed:11675786, ECO:0000269|PubMed:9405696}. +O88705 HCN3_MOUSE Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 3 (Hyperpolarization-activated cation channel 3) (HAC-3) 779 86,641 Chain (1); Glycosylation (1); Intramembrane (1); Modified residue (1); Nucleotide binding (3); Region (2); Topological domain (8); Transmembrane (6) INTRAMEM 297 318 Pore-forming; Name=Segment H5. {ECO:0000255}. TRANSMEM 97 117 Helical; Name=Segment S1. {ECO:0000255}.; TRANSMEM 124 144 Helical; Name=Segment S2. {ECO:0000255}.; TRANSMEM 171 191 Helical; Name=Segment S3. {ECO:0000255}.; TRANSMEM 201 221 Helical; Voltage-sensor; Name=Segment S4. {ECO:0000255}.; TRANSMEM 253 273 Helical; Name=Segment S5. {ECO:0000255}.; TRANSMEM 329 349 Helical; Name=Segment S6. {ECO:0000255}. TOPO_DOM 1 96 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 118 123 Extracellular. {ECO:0000255}.; TOPO_DOM 145 170 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 192 200 Extracellular. {ECO:0000255}.; TOPO_DOM 222 252 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 274 296 Extracellular. {ECO:0000255}.; TOPO_DOM 319 328 Extracellular. {ECO:0000255}.; TOPO_DOM 350 779 Cytoplasmic. {ECO:0000255}. FUNCTION: Hyperpolarization-activated potassium channel. May also facilitate the permeation of sodium ions. {ECO:0000269|PubMed:15923185}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15923185, ECO:0000269|PubMed:23382386}; Multi-pass membrane protein {ECO:0000269|PubMed:15923185}. SUBUNIT: Homotetramer. The potassium channel is probably composed of a homo- or heterotetrameric complex of pore-forming subunits (By similarity). Interacts with KCTD3 and PEX5L (PubMed:23382386). {ECO:0000250|UniProtKB:Q9UL51, ECO:0000269|PubMed:23382386}. DOMAIN: The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position. TISSUE SPECIFICITY: Detected in hypothalamus, amygdala, olfactory bulb, hippocampus and retina (at protein level). Highly expressed in brain and heart, in particular in ventricle, atrium and in sinoatrial node (SAN). Detected at low levels in skeletal muscle and lung. {ECO:0000269|PubMed:15923185, ECO:0000269|PubMed:23382386, ECO:0000269|PubMed:9630217}. +O70507 HCN4_MOUSE Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 4 (Brain cyclic nucleotide-gated channel 3) (BCNG-3) 1186 127,414 Chain (1); Compositional bias (1); Glycosylation (1); Intramembrane (1); Modified residue (3); Nucleotide binding (2); Region (1); Topological domain (8); Transmembrane (6) INTRAMEM 465 486 Pore-forming; Name=Segment H5. {ECO:0000255}. TRANSMEM 267 287 Helical; Name=Segment S1. {ECO:0000255}.; TRANSMEM 294 314 Helical; Name=Segment S2. {ECO:0000255}.; TRANSMEM 341 361 Helical; Name=Segment S3. {ECO:0000255}.; TRANSMEM 369 389 Helical; Voltage-sensor; Name=Segment S4. {ECO:0000255}.; TRANSMEM 421 441 Helical; Name=Segment S5. {ECO:0000255}.; TRANSMEM 497 517 Helical; Name=Segment S6. {ECO:0000255}. TOPO_DOM 1 266 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 288 293 Extracellular. {ECO:0000255}.; TOPO_DOM 315 340 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 362 368 Extracellular. {ECO:0000255}.; TOPO_DOM 390 420 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 442 464 Extracellular. {ECO:0000255}.; TOPO_DOM 487 496 Extracellular. {ECO:0000255}.; TOPO_DOM 518 1186 Cytoplasmic. {ECO:0000255}. FUNCTION: Hyperpolarization-activated ion channel with very slow activation and inactivation exhibiting weak selectivity for potassium over sodium ions. Contributes to the native pacemaker currents in heart (If) that regulate the rhythm of heart beat. May contribute to the native pacemaker currents in neurons (Ih) (By similarity). May mediate responses to sour stimuli. {ECO:0000250, ECO:0000269|PubMed:11675786}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11675786}; Multi-pass membrane protein {ECO:0000269|PubMed:11675786}. SUBUNIT: Homotetramer. The potassium channel is composed of a homo- or heterotetrameric complex of pore-forming subunits (By similarity). {ECO:0000250}. DOMAIN: The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position. TISSUE SPECIFICITY: Detected in a subset of elongated cells in taste buds. {ECO:0000269|PubMed:11675786}. +Q80VJ8 KASH5_MOUSE Protein KASH5 (Coiled-coil domain-containing protein 155) (KASH domain-containing protein 5) 648 72,444 Chain (1); Coiled coil (1); Compositional bias (2); Erroneous initiation (1); Mutagenesis (2); Sequence conflict (5); Topological domain (2); Transmembrane (1) TRANSMEM 607 627 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 1 606 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 628 648 Perinuclear space. {ECO:0000255}. FUNCTION: As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning. Required for telomere attachment to nuclear envelope in the prophase of meiosis and for rapid telomere prophase movements implicating a SUN1/2:KASH5 LINC complex in which SUN1 and SUN2 seem to act at least partial redundantly. Required for homologue pairing during meiotic prophase in spermatocytes and probably oocytes. Essential for male and female gametogenesis. Recruits cytoplasmic dynein to telomere attachment sites at the nuclear envelope in spermatocytes. In oocytes is involved in meiotic resumption and spindle formation. {ECO:0000269|PubMed:24062341, ECO:0000269|PubMed:25892231, ECO:0000269|PubMed:26842404}. SUBCELLULAR LOCATION: Nucleus outer membrane {ECO:0000269|PubMed:24062341, ECO:0000269|PubMed:26842404}; Single-pass type IV membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Nucleus {ECO:0000269|PubMed:22826121}. Chromosome, telomere {ECO:0000269|PubMed:22826121}. Note=Localized exclusively at telomeres from the leptotene to diplotene stages. Colocalizes with SUN2 at sites of telomere attachment in meiocytes. At oocyte MI stage localized around the spindle, at MII stage localized to the spindle poles. {ECO:0000269|PubMed:24586178, ECO:0000269|PubMed:26842404}. SUBUNIT: Core component the LINC complex which is composed of inner nuclear membrane SUN domain-containing proteins coupled to outer nuclear membrane KASH domain-containing nesprins. SUN and KASH domain-containing proteins seem to bind each other promiscuously; however, differentially expression of LINC complex constituents is giving rise to specific assemblies. At least SUN1/2-containing core LINC complexes are proposed to be hexameric composed of three protomers of each KASH and SUN domain-containing protein. Interacts (via the last 22 AA) with SUN1; this interaction mediates its telomere localization by forming a SUN1:KASH5 LINC complex. Component of a probable SUN2:KASH5 LINC complex. Self-associates. Interacts with DYNC1H1, DCTN1, DYNC1I1/2 and PAFAH1B1; suggesting the association with the dynein-dynactin motor complex. {ECO:0000250|UniProtKB:Q8WXH0, ECO:0000269|PubMed:22826121, ECO:0000269|PubMed:24062341, ECO:0000305, ECO:0000305|PubMed:24586178}. DOMAIN: The C-terminal 22 AA is required and sufficient for localization to telomeres at the nuclear envelope. TISSUE SPECIFICITY: Restricted to the testis and the early ootidogenesis ovary. Expressed in spermatocytes and oocytes (at protein level). {ECO:0000269|PubMed:22826121, ECO:0000269|PubMed:24062341, ECO:0000269|PubMed:26842404}. +Q6P3E7 HDA10_MOUSE Polyamine deacetylase HDAC10 (EC 3.5.1.48) (EC 3.5.1.62) (Histone deacetylase 10) (HD10) 666 72,109 Active site (1); Chain (1); Region (1); Sequence conflict (1) FUNCTION: Polyamine deacetylase (PDAC), which acts preferentially on N(8)-acetylspermidine, and also on acetylcadaverine and acetylputrescine. Exhibits attenuated catalytic activity toward N(1),N(8)-diacetylspermidine and very low activity, if any, toward N(1)-acetylspermidine. Histone deacetylase activity has been observed in vitro. Has also been shown to be involved in MSH2 deacetylation. The physiological relevance of protein/histone deacetylase activity is unclear and could be very weak. May play a role in the promotion of late stages of autophagy, possibly autophagosome-lysosome fusion and/or lysosomal exocytosis in neuroblastoma cells. May play a role in homologous recombination. May promote DNA mismatch repair. {ECO:0000250|UniProtKB:Q969S8}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q969S8}. Nucleus {ECO:0000250|UniProtKB:Q969S8}. Note=Excluded from nucleoli. {ECO:0000250|UniProtKB:Q969S8}. SUBUNIT: Interacts with HDAC3. Interacts with HDAC2 and NCOR2/SMRT. Interacts with HSPA8/HSC70. Interacts with MSH2. {ECO:0000250|UniProtKB:Q969S8}. TISSUE SPECIFICITY: widely expressed. {ECO:0000269|PubMed:11677242}. +Q9D1N2 HDBP1_MOUSE Glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1 (GPI-HBP1) (GPI-anchored HDL-binding protein 1) (High density lipoprotein-binding protein 1) 228 24,566 Chain (1); Compositional bias (2); Disulfide bond (5); Domain (1); Glycosylation (1); Lipidation (1); Mutagenesis (2); Propeptide (1); Signal peptide (1) FUNCTION: Plays a key role in the lipolytic processing of chylomicrons. Required for the transport of lipoprotein lipase LPL into the capillary lumen and across endothelial cells. {ECO:0000269|PubMed:17403372, ECO:0000269|PubMed:17620854, ECO:0000269|PubMed:20620994}. PTM: Glycosylation of Asn-76 is critical for cell surface localization and the binding of chylomicrons and lipoprotein lipase. {ECO:0000269|PubMed:18340083}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:20620994}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:20620994}. Basolateral cell membrane {ECO:0000269|PubMed:20620994}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:20620994}. Cell membrane {ECO:0000269|PubMed:20620994}; Peripheral membrane protein {ECO:0000269|PubMed:20620994}; Extracellular side {ECO:0000269|PubMed:20620994}. SUBUNIT: Mostly monomer, but also homodimer and homooligomer (PubMed:25387803). Interacts with high affinity with high-density lipoprotein (HDL) (PubMed:12496272). Only monomer interacts with lipoprotein lipase (LPL) (PubMed:25387803, PubMed:17403372). Interacts with chylomicrons and APOA5 (By similarity). {ECO:0000250|UniProtKB:Q8IV16, ECO:0000269|PubMed:12496272, ECO:0000269|PubMed:17403372, ECO:0000269|PubMed:25387803}. TISSUE SPECIFICITY: Highly expressed on the luminal surface of capillary endothelium in heart, adipose tissue and skeletal muscle. Not detected in capillaries of the brain. Expressed at lower levels in lung and liver. {ECO:0000269|PubMed:12496272, ECO:0000269|PubMed:17403372}. +O09106 HDAC1_MOUSE Histone deacetylase 1 (HD1) (EC 3.5.1.98) 482 55,075 Active site (1); Chain (1); Cross-link (10); Modified residue (10); Region (1) FUNCTION: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Deacetylates SP proteins, SP1 and SP3, and regulates their function. Component of the BRG1-RB1-HDAC1 complex, which negatively regulates the CREST-mediated transcription in resting neurons. Upon calcium stimulation, HDAC1 is released from the complex and CREBBP is recruited, which facilitates transcriptional activation. Deacetylates TSHZ3 and regulates its transcriptional repressor activity. Deacetylates 'Lys-310' in RELA and thereby inhibits the transcriptional activity of NF-kappa-B. Deacetylates NR1D2 and abrogates the effect of KAT5-mediated relieving of NR1D2 transcription repression activity. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. Involved in CIART-mediated transcriptional repression of the circadian transcriptional activator: CLOCK-ARNTL/BMAL1 heterodimer. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex or CRY1 through histone deacetylation. {ECO:0000269|PubMed:15226430, ECO:0000269|PubMed:15542849, ECO:0000269|PubMed:17707228, ECO:0000269|PubMed:21960634, ECO:0000269|PubMed:24736997}. PTM: Sumoylated on Lys-444 and Lys-476; which promotes enzymatic activity. Desumoylated by SENP1. {ECO:0000250|UniProtKB:Q13547}.; PTM: Phosphorylation on Ser-421 and Ser-423 promotes enzymatic activity and interactions with NuRD and SIN3 complexes. Phosphorylated by CDK5. {ECO:0000250|UniProtKB:Q13547}.; PTM: Ubiquitinated by CHFR and KCTD11, leading to its degradation by the proteasome. {ECO:0000250|UniProtKB:Q13547}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21454521}. SUBUNIT: Part of the core histone deacetylase (HDAC) complex composed of HDAC1, HDAC2, RBBP4 and RBBP7. The core complex associates with MTA2, MBD2, MBD3, MTA1L1, CHD3 and CHD4 to form the nucleosome remodeling and histone deacetylation (NuRD) complex, or with SIN3, SAP18 and SAP30 to form the SIN3 HDAC complex. Component of a BHC histone deacetylase complex that contains HDAC1, HDAC2, HMG20B/BRAF35, KDM1A, RCOR1/CoREST and PHF21A/BHC80. The BHC complex may also contain ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I. Component of a mSin3A corepressor complex that contains SIN3A, SAP130, SUDS3/SAP45, ARID4B/SAP180, HDAC1 and HDAC2. Found in a trimeric complex with APBB1 and TSHZ3; the interaction between HDAC1 and APBB1 is mediated by TSHZ3. Component of a RCOR/GFI/KDM1A/HDAC complex. Part of a complex composed of TRIM28, HDAC1, HDAC2 and EHMT2. Part of a complex containing at least CDYL, MIER1, MIER2, HDAC1 and HDAC2. The large PER complex involved in the histone deacetylation is composed of at least HDAC1, PER2, SFPQ and SIN3A. Associates with the 9-1-1 complex; interacts with HUS1. Found in a complex with DNMT3A and HDAC7. Interacts with the non-histone region of H2AFY. Interacts with TRIM28; the interaction recruits HDAC1 to E2F1 and inhibits its acetylation. Interacts with SP1; the interaction deacetylates SP1 and regulates its transcriptional activity. Interacts with SP3; the interaction deacetylates SP3 and regulates its transcriptional activity. In vitro, C(18) ceramides increase this interaction and the subsequent SP3 deacetylation and SP3-mediated repression of the TERT promoter. Interacts with TSHZ3 (via N-terminus); the interaction is direct. Interacts with APEX1; the interaction is not dependent on the acetylated status of APEX1. Interacts with DNTTIP1 (By similarity). Identified in a histone deacetylase complex that contains DNTTIP1, HDAC1 and ELMSAN1; this complex assembles into a tetramer that contains four copies of each protein chain (By similarity). Interacts with C10orf90/FATS (via its N-terminal); the interaction prevents binding of HDAC1 to CDKN1A/p21 and facilitates the acetylation and stabilization of CDKN1A/p21. Interacts with CDKN1A/p21. Interacts with CDK5 complexed to CDK5R1 (p25). Interacts directly with GFI1 and GFI1B. Interacts with NR1D2 (via C-terminus). Interacts with TSC22D3 isoform 1; this interaction affects HDAC1 activity on MYOG promoter and thus inhibits MYOD1 transcriptional activity. Interacts with BAZ2A/TIP5, BANP, BCL6, BCOR, BHLHE40/DEC1, BRMS1, BRMS1L, CBFA2T3, CHFR, CIART, CRY1, DAXX, DDIT3/CHOP, DDX5, DNMT1, E4F1, EP300, HCFC1, HDAC9, INSM1, NFE4, NR4A2/NURR1, MIER1, KDM4A, KDM5B, KLF1, MINT, NRIP1, PCAF, PHB2, PRDM6, PRDM16, RB1, RERE, SAMSN1, SAP30L, SETDB1, SMAD3, SMARCA4/BRG1, SMYD2, SUV39H1, TGIF, TGIF2, TRAF6, UHRF1, UHRF2, ZMYND15, ZNF431 and ZNF541. Interacts with KDM5A. Interacts with CCAR2 (By similarity). Interacts with PPHLN1 (By similarity). Found in a complex with YY1, SIN3A and GON4L (PubMed:21454521). Interacts with CHD4 (By similarity). Found in a complex composed of at least SINHCAF, SIN3A, HDAC1, SAP30, RBBP4, OGT and TET1 (PubMed:28554894). Interacts with SIN3A (PubMed:28554894). Interacts with DHX36; this interaction occurs in a RNA-dependent manner (By similarity). Interacts with ZBTB7A (By similarity). Interacts with SMAD4; positively regulated by ZBTB7A (By similarity). Interacts with PACS2 (By similarity). {ECO:0000250|UniProtKB:Q13547, ECO:0000269|PubMed:10615135, ECO:0000269|PubMed:10984530, ECO:0000269|PubMed:11022042, ECO:0000269|PubMed:11533236, ECO:0000269|PubMed:11788710, ECO:0000269|PubMed:11909966, ECO:0000269|PubMed:12198165, ECO:0000269|PubMed:12398767, ECO:0000269|PubMed:12616525, ECO:0000269|PubMed:14645126, ECO:0000269|PubMed:15060175, ECO:0000269|PubMed:15140878, ECO:0000269|PubMed:15226430, ECO:0000269|PubMed:15542849, ECO:0000269|PubMed:15711539, ECO:0000269|PubMed:16085498, ECO:0000269|PubMed:16107708, ECO:0000269|PubMed:16166625, ECO:0000269|PubMed:16537907, ECO:0000269|PubMed:16611996, ECO:0000269|PubMed:16805913, ECO:0000269|PubMed:17707228, ECO:0000269|PubMed:18849567, ECO:0000269|PubMed:19144721, ECO:0000269|PubMed:20124407, ECO:0000269|PubMed:20154723, ECO:0000269|PubMed:20478393, ECO:0000269|PubMed:20675388, ECO:0000269|PubMed:21177534, ECO:0000269|PubMed:21454521, ECO:0000269|PubMed:21960634, ECO:0000269|PubMed:22242125, ECO:0000269|PubMed:24227653, ECO:0000269|PubMed:24413057, ECO:0000269|PubMed:24736997, ECO:0000269|PubMed:28554894, ECO:0000269|PubMed:9702189}. TISSUE SPECIFICITY: Widely expressed with higher levels in thymus and testis and lower levels in liver. Present in muscle (at protein level). {ECO:0000269|PubMed:15711539}. +O88895 HDAC3_MOUSE Histone deacetylase 3 (HD3) (EC 3.5.1.98) 424 48,364 Active site (1); Alternative sequence (1); Chain (1); Modified residue (1); Region (1) FUNCTION: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4), and some other non-histone substrates. Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Participates in the BCL6 transcriptional repressor activity by deacetylating the H3 'Lys-27' (H3K27) on enhancer elements, antagonizing EP300 acetyltransferase activity and repressing proximal gene expression. Probably participates in the regulation of transcription through its binding to the zinc-finger transcription factor YY1; increases YY1 repression activity. Required to repress transcription of the POU1F1 transcription factor. Acts as a molecular chaperone for shuttling phosphorylated NR2C1 to PML bodies for sumoylation (PubMed:23911289). Contributes, together with XBP1 isoform 1, to the activation of NFE2L2-mediated HMOX1 transcription factor gene expression in a PI(3)K/mTORC2/Akt-dependent signaling pathway leading to endothelial cell (EC) survival under disturbed flow/oxidative stress (By similarity). {ECO:0000250|UniProtKB:O15379, ECO:0000269|PubMed:23911289}. PTM: Sumoylated in vitro. {ECO:0000269|PubMed:19204783}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O15379}. Cytoplasm {ECO:0000250|UniProtKB:O15379}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:O15379}. Note=Colocalizes with XBP1 and AKT1 in the cytoplasm. Predominantly expressed in the nucleus in the presence of CCAR2 (By similarity). {ECO:0000250|UniProtKB:O15379}. SUBUNIT: Interacts with HDAC7 and HDAC9. Forms a heterologous complex at least with YY1. Interacts with DAXX, HDAC10 and DACH1. Found in a complex with NCOR1 and NCOR2. Component of the N-Cor repressor complex, at least composed of NCOR1, NCOR2, HDAC3, TBL1X, TBL1R, CORO2A and GPS2. Interacts with BCOR, MJD2A/JHDM3A, NRIP1, PRDM6 and SRY. Interacts with BTBD14B. Interacts with GLIS2. Interacts (via the DNA-binding domain) with NR2C1; the interaction recruits phosphorylated NR2C1 to PML bodies for sumoylation. Component of the Notch corepressor complex. Interacts with CBFA2T3 and NKAP. Interacts with APEX1; the interaction is not dependent on the acetylated status of APEX1. Interacts with and deacetylates MAPK14. Interacts with ZMYND15. Interacts with SMRT/NCOR2 and BCL6 on DNA enhancer elements. Interacts with INSM1 (PubMed:10984530, PubMed:11022042, PubMed:11533236, PubMed:12130660, PubMed:15711539, PubMed:16326862, PubMed:16537907, PubMed:19204783, PubMed:20675388). Interacts with XBP1 isoform 1; the interaction occurs in endothelial cell (EC) under disturbed flow. Interacts (via C-terminus) with CCAR2 (via N-terminus). Interacts with and deacetylates MEF2D (By similarity). Interacts with BEND3 (By similarity). Interacts with NKAPL (PubMed:25875095). Interacts with DHX36; this interaction occurs in a RNA-dependent manner (By similarity). {ECO:0000250|UniProtKB:O15379, ECO:0000269|PubMed:10984530, ECO:0000269|PubMed:11022042, ECO:0000269|PubMed:11533236, ECO:0000269|PubMed:12130660, ECO:0000269|PubMed:15711539, ECO:0000269|PubMed:16326862, ECO:0000269|PubMed:16537907, ECO:0000269|PubMed:19204783, ECO:0000269|PubMed:20675388, ECO:0000269|PubMed:25875095}. +Q2TUM3 KCNRG_MOUSE Potassium channel regulatory protein (Potassium channel regulator) (Protein CLLD4) 264 29,417 Alternative sequence (2); Chain (1); Domain (1) FUNCTION: Inhibits potassium fluxes in cells. May regulate Kv1 family channel proteins by retaining a fraction of channels in endomembranes (By similarity). {ECO:0000250|UniProtKB:Q8N5I3}. SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:Q8N5I3}. SUBUNIT: Can form homooligomers. Interacts with KCNA1 (via cytoplasmic N-terminal domain) and KCNA4. {ECO:0000250|UniProtKB:Q8N5I3}. +Q7TSH7 KCNF1_MOUSE Potassium voltage-gated channel subfamily F member 1 (Voltage-gated potassium channel subunit Kv5.1) 493 55,647 Chain (1); Intramembrane (1); Motif (1); Topological domain (4); Transmembrane (6) INTRAMEM 358 378 Pore-forming; Name=Segment H5. {ECO:0000255}. TRANSMEM 184 204 Helical; Name=Segment S1. {ECO:0000255}.; TRANSMEM 224 244 Helical; Name=Segment S2. {ECO:0000255}.; TRANSMEM 250 270 Helical; Name=Segment S3. {ECO:0000255}.; TRANSMEM 290 310 Helical; Voltage-sensor; Name=Segment S4. {ECO:0000255}.; TRANSMEM 325 345 Helical; Name=Segment S5. {ECO:0000255}.; TRANSMEM 386 406 Helical; Name=Segment S6. {ECO:0000255}. TOPO_DOM 1 183 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 245 249 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 311 324 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 407 493 Cytoplasmic. {ECO:0000255}. FUNCTION: Putative voltage-gated potassium channel. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Heteromultimer with KCNG3, KCNG4 and KCNV2. Interacts with DLG1 (By similarity). {ECO:0000250}. DOMAIN: The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position. {ECO:0000250}. +P48545 KCNJ5_MOUSE G protein-activated inward rectifier potassium channel 4 (GIRK-4) (Cardiac inward rectifier) (CIR) (Heart KATP channel) (Inward rectifier K(+) channel Kir3.4) (KATP-1) (Potassium channel, inwardly rectifying subfamily J member 5) 419 47,669 Chain (1); Intramembrane (2); Modified residue (1); Motif (1); Sequence conflict (10); Site (1); Topological domain (4); Transmembrane (2) INTRAMEM 136 147 Helical; Pore-forming; Name=H5. {ECO:0000250}.; INTRAMEM 148 154 Pore-forming. {ECO:0000250}. TRANSMEM 87 111 Helical; Name=M1. {ECO:0000250}.; TRANSMEM 164 185 Helical; Name=M2. {ECO:0000250}. TOPO_DOM 1 86 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 112 135 Extracellular. {ECO:0000250}.; TOPO_DOM 155 163 Extracellular. {ECO:0000250}.; TOPO_DOM 186 419 Cytoplasmic. {ECO:0000250}. FUNCTION: This potassium channel is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by external barium. {ECO:0000269|PubMed:7499385}. SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P48544}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: May associate with GIRK1 and GIRK2 to form a G-protein-activated heteromultimer pore-forming unit. The resulting inward current is much larger. {ECO:0000250|UniProtKB:P48548}. TISSUE SPECIFICITY: Predominantly atrial and pancreatic expression. +O89109 KCNN4_MOUSE Intermediate conductance calcium-activated potassium channel protein 4 (SK4) (SKCa 4) (SKCa4) (IK1) (KCa3.1) (KCa4) 425 47,784 Chain (1); Compositional bias (1); Intramembrane (1); Modified residue (1); Region (1); Sequence conflict (1); Transmembrane (6) INTRAMEM 239 259 Pore-forming; Name=Segment H5. {ECO:0000255}. TRANSMEM 30 50 Helical; Name=Segment S1. {ECO:0000255}.; TRANSMEM 59 79 Helical; Name=Segment S2. {ECO:0000255}.; TRANSMEM 105 121 Helical; Name=Segment S3. {ECO:0000255}.; TRANSMEM 141 161 Helical; Name=Segment S4. {ECO:0000255}.; TRANSMEM 205 225 Helical; Name=Segment S5. {ECO:0000255}.; TRANSMEM 263 283 Helical; Name=Segment S6. {ECO:0000255}. FUNCTION: Forms a voltage-independent potassium channel that is activated by intracellular calcium (PubMed:9705284). Activation is followed by membrane hyperpolarization which promotes calcium influx. Required for maximal calcium influx and proliferation during the reactivation of naive T-cells (PubMed:20884616). Plays a role in the late stages of EGF-induced macropinocytosis (By similarity). {ECO:0000250|UniProtKB:O15554, ECO:0000269|PubMed:20884616, ECO:0000269|PubMed:9705284}. PTM: Phosphorylation at His-356 by NDKB activates the channel, and conversely it's dephosphorylation by PHPT1 inhibits the channel. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O15554}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O15554}. SUBUNIT: Heterotetramer of potassium channel proteins (Probable). Interacts with MTMR6 (By similarity). {ECO:0000250, ECO:0000305}. +O88454 KCNK4_MOUSE Potassium channel subfamily K member 4 (TWIK-related arachidonic acid-stimulated potassium channel protein) (TRAAK) 398 43,052 Alternative sequence (2); Chain (1); Disulfide bond (1); Glycosylation (2); Intramembrane (4); Region (2); Topological domain (7); Transmembrane (4) INTRAMEM 89 103 Helical; Name=Pore helix 1. {ECO:0000250|UniProtKB:Q9NYG8}.; INTRAMEM 104 110 {ECO:0000250|UniProtKB:Q9NYG8}.; INTRAMEM 201 214 Helical; Name=Pore helix 2. {ECO:0000250|UniProtKB:Q9NYG8}.; INTRAMEM 215 220 {ECO:0000250|UniProtKB:Q9NYG8}. TRANSMEM 4 24 Helical. {ECO:0000250|UniProtKB:Q9NYG8}.; TRANSMEM 119 151 Helical. {ECO:0000250|UniProtKB:Q9NYG8}.; TRANSMEM 174 195 Helical. {ECO:0000250|UniProtKB:Q9NYG8}.; TRANSMEM 235 261 Helical. {ECO:0000250|UniProtKB:Q9NYG8}. TOPO_DOM 1 3 Cytoplasmic. {ECO:0000250|UniProtKB:Q9NYG8}.; TOPO_DOM 25 88 Extracellular. {ECO:0000250|UniProtKB:Q9NYG8}.; TOPO_DOM 111 118 Extracellular. {ECO:0000250|UniProtKB:Q9NYG8}.; TOPO_DOM 152 173 Cytoplasmic. {ECO:0000250|UniProtKB:Q9NYG8}.; TOPO_DOM 196 200 Extracellular. {ECO:0000250|UniProtKB:Q9NYG8}.; TOPO_DOM 221 234 Extracellular. {ECO:0000250|UniProtKB:Q9NYG8}.; TOPO_DOM 262 398 Cytoplasmic. {ECO:0000250|UniProtKB:Q9NYG8}. FUNCTION: Voltage-insensitive potassium channel (PubMed:9628867). Channel opening is triggered by mechanical forces that deform the membrane. Channel opening is triggered by raising the intracellular pH to basic levels (By similarity). The channel is inactive at 24 degrees Celsius (in vitro); raising the temperature to 37 degrees Celsius increases the frequency of channel opening, with a further increase in channel activity when the temperature is raised to 42 degrees Celsius (By similarity). Plays a role in the sensory perception of pain caused by pressure (PubMed:19279663). Plays a role in the perception of pain caused by heat (PubMed:19279663). {ECO:0000250|UniProtKB:G3V8V5, ECO:0000269|PubMed:19279663, ECO:0000269|PubMed:9628867}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9NYG8}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9628867}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250|UniProtKB:Q9NYG8}. DOMAIN: Channel opening is brought about by a conformation change that involves buckling of the second transmembrane helix and affects the position and orientation of the fourth transmembrane helix. {ECO:0000250|UniProtKB:Q9NYG8}. TISSUE SPECIFICITY: Expressed in brain, spinal cord and eye. Not detected in heart, skeletal muscle, liver, lungs, kidney and testis. {ECO:0000269|PubMed:9628867}. +Q9Z0V2 KCND2_MOUSE Potassium voltage-gated channel subfamily D member 2 (Voltage-gated potassium channel subunit Kv4.2) 630 70,577 Chain (1); Erroneous initiation (1); Frameshift (1); Intramembrane (2); Metal binding (3); Modified residue (9); Motif (2); Mutagenesis (4); Region (5); Sequence conflict (2); Topological domain (8); Transmembrane (6) INTRAMEM 358 369 Helical; Name=Pore helix. {ECO:0000250|UniProtKB:P63142}.; INTRAMEM 370 377 {ECO:0000250|UniProtKB:P63142}. TRANSMEM 183 204 Helical; Name=Segment S1. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 229 250 Helical; Name=Segment S2. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 262 279 Helical; Name=Segment S3. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 287 306 Helical; Voltage-sensor; Name=Segment S4. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 322 343 Helical; Name=Segment S5. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 385 413 Helical; Name=Segment S6. {ECO:0000250|UniProtKB:P63142}. TOPO_DOM 1 182 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 205 228 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 251 261 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 280 286 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 307 321 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 344 357 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 378 384 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 414 630 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}. FUNCTION: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain, but also in rodent heart. Mediates the major part of the dendritic A-type current I(SA) in brain neurons (PubMed:10818150, PubMed:17122039, PubMed:18045912, PubMed:18187474, PubMed:20371829, PubMed:22815518). This current is activated at membrane potentials that are below the threshold for action potentials. It regulates neuronal excitability, prolongs the latency before the first spike in a series of action potentials, regulates the frequency of repetitive action potential firing, shortens the duration of action potentials and regulates the back-propagation of action potentials from the neuronal cell body to the dendrites (PubMed:10818150, PubMed:17122039, PubMed:22815518). Contributes to the regulation of the circadian rhythm of action potential firing in suprachiasmatic nucleus neurons, which regulates the circadian rhythm of locomotor activity (PubMed:22815518). Functions downstream of the metabotropic glutamate receptor GRM5 and plays a role in neuronal excitability and in nociception mediated by activation of GRM5 (PubMed:18045912). Mediates the transient outward current I(to) in rodent heart left ventricle apex cells, but not in human heart, where this current is mediated by another family member (PubMed:9734479, PubMed:10601491, PubMed:11909823, PubMed:23713033). Forms tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane (PubMed:9734479, PubMed:22311982). Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCND2 and KCND3; channel properties depend on the type of pore-forming alpha subunits that are part of the channel (PubMed:11909823). In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes (PubMed:11909823). Interaction with specific isoforms of the regulatory subunits KCNIP1, KCNIP2, KCNIP3 or KCNIP4 strongly increases expression at the cell surface and thereby increases channel activity; it modulates the kinetics of channel activation and inactivation, shifts the threshold for channel activation to more negative voltage values, shifts the threshold for inactivation to less negative voltages and accelerates recovery after inactivation (By similarity). Likewise, interaction with DPP6 or DPP10 promotes expression at the cell membrane and regulates both channel characteristics and activity (PubMed:22311982). {ECO:0000250|UniProtKB:Q63881, ECO:0000269|PubMed:10601491, ECO:0000269|PubMed:10818150, ECO:0000269|PubMed:11909823, ECO:0000269|PubMed:17122039, ECO:0000269|PubMed:18187474, ECO:0000269|PubMed:20371829, ECO:0000269|PubMed:22311982, ECO:0000269|PubMed:23713033, ECO:0000269|PubMed:9734479}. PTM: Phosphorylation at Ser-438 in response to MAPK activation is increased in stimulated dendrites. Interaction with KCNIP2 and DPP6 propomtes phosphorylation by PKA at Ser-552. Phosphorylation at Ser-552 has no effect on interaction with KCNIP3, but is required for the regulation of channel activity by KCNIP3. Phosphorylation at Ser-552 leads to KCND2 internalization (By similarity). Phosphorylated by MAPK in response to signaling via the metabotropic glutamate receptor GRM5 (PubMed:18045912). Phosphorylation at Ser-616 is required for the down-regulation of neuronal A-type currents in response to signaling via GRM5 (PubMed:18045912). {ECO:0000250|UniProtKB:Q63881, ECO:0000269|PubMed:18045912}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16009497, ECO:0000269|PubMed:17122053, ECO:0000269|PubMed:22098631, ECO:0000269|PubMed:22311982, ECO:0000269|PubMed:9734479}; Multi-pass membrane protein {ECO:0000305}. Cell projection, dendrite {ECO:0000269|PubMed:11040264, ECO:0000269|PubMed:17122053, ECO:0000269|PubMed:22098631}. Cell junction, synapse {ECO:0000269|PubMed:16009497, ECO:0000269|PubMed:17122053}. Perikaryon {ECO:0000269|PubMed:11040264, ECO:0000269|PubMed:16009497, ECO:0000269|PubMed:17122053, ECO:0000269|PubMed:22098631}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000269|PubMed:16009497}. Cell projection, dendritic spine {ECO:0000269|PubMed:17122053}. Cell junction {ECO:0000250|UniProtKB:Q63881}. Membrane, caveola {ECO:0000250|UniProtKB:Q63881}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:Q63881}. Note=In neurons, primarily detected on dendrites, dendritic spines and on the neuron cell body, but not on axons (PubMed:17122053, PubMed:22098631). Localized preferentially at the dendrites of pyramidal cells in the hippocampus CA1 layer. Detected at GABAergic synapses (PubMed:16009497). Detected at cell junctions that are distinct from synaptic cell contacts (By similarity). Detected in lipid rafts (By similarity). Detected primarily at the endoplasmic reticulum or Golgi when expressed by itself (By similarity). Interaction with KCNIP1, KCNIP2, KCNIP3 or KCNIP4 promotes expression at the cell membrane (PubMed:22311982). Interaction with DPP6 or DPP10 promotes expression at the cell membrane (By similarity). Internalized from the cell membrane by clathrin-dependent endocytosis in response to activation of AMPA-selective glutamate receptors and PKA-mediated phosphorylation at Ser-552. Redistributed from dendritic spines to the main dendritic shaft in response to activation of AMPA-selective glutamate receptors and activation of PKA (By similarity). {ECO:0000250|UniProtKB:Q63881, ECO:0000269|PubMed:17122053, ECO:0000269|PubMed:22098631, ECO:0000269|PubMed:22311982}. SUBUNIT: Homotetramer or heterotetramer with KCND3 or KCND1 (PubMed:9734479, PubMed:11909823, PubMed:19713751, PubMed:20943905). Associates with the regulatory subunits KCNIP1, KCNIP2, KCNIP3 and KCNIP4 (PubMed:11909823, PubMed:19713751, PubMed:20943905). In vivo, probably exists as heteromeric complex containing variable proportions of KCND1, KCND2, KCND3, KCNIP1, KCNIP2, KCNIP3, KCNIP4, DPP6 and DPP10 (PubMed:19713751). The tetrameric channel can associate with up to four regulatory subunits, such as KCNIP2 or KCNIP4 (By similarity). Interaction with four KCNIP4 chains does not reduce interaction with DPP10 (By similarity). Interacts with DLG1 (By similarity). Interacts with DLG4 (By similarity). Interacts with NCS1/FREQ (PubMed:11606724). Probably part of a complex consisting of KCNIP1, KCNIP2 isoform 3 and KCND2 (By similarity). Interacts with FLNA and FLNC (By similarity). Interacts with DPP6 and DPP10 (PubMed:19713751, PubMed:22311982). Identified in a complex with cAMP-dependent protein kinase (PKA), CAV3, AKAP6 and KCND3 in cardiac myocytes (By similarity). {ECO:0000250|UniProtKB:Q63881, ECO:0000250|UniProtKB:Q9NZV8, ECO:0000269|PubMed:11909823, ECO:0000269|PubMed:19713751, ECO:0000269|PubMed:20943905, ECO:0000269|PubMed:22311982, ECO:0000269|PubMed:9734479}. DOMAIN: The transmembrane segment S4 functions as voltage-sensor and is characterized by a series of positively charged amino acids at every third position. Channel opening and closing is effected by a conformation change that affects the position and orientation of the voltage-sensor paddle formed by S3 and S4 within the membrane. A transmembrane electric field that is positive inside would push the positively charged S4 segment outwards, thereby opening the pore, while a field that is negative inside would pull the S4 segment inwards and close the pore. Changes in the position and orientation of S4 are then transmitted to the activation gate formed by the inner helix bundle via the S4-S5 linker region. {ECO:0000250|UniProtKB:P63142}.; DOMAIN: The N-terminal cytoplasmic region can mediate N-type inactivation by physically blocking the channel (By similarity). This probably does not happen in vivo, where the N-terminal region mediates interaction with regulatory subunits, such as KCNIP1 and KCNIP2 (By similarity). The zinc binding sites in the N-terminal domain are important for tetramerization and assembly of a functional channel complex (By similarity). Most likely, the channel undergoes closed-state inactivation, where a subtle conformation change would render the protein less sensitive to activation. {ECO:0000250|UniProtKB:Q63881, ECO:0000250|UniProtKB:Q9NZV8, ECO:0000305|PubMed:18357523}.; DOMAIN: The C-terminal cytoplasmic region is important for normal expression at the cell membrane and modulates the voltage-dependence of channel activation and inactivation. It is required for interaction with KCNIP2, and probably other family members as well. {ECO:0000250|UniProtKB:Q63881}. TISSUE SPECIFICITY: Detected in hippocampus, thalamus, medial habenular nucleus, striatum, amygdala, brain cortex and cerebellum (PubMed:11040264, PubMed:17122039, PubMed:18187474, PubMed:20371829, PubMed:22612819). Detected in hippocampus CA1 and CA3 layer, in stratum oriens, stratum radiatum and stratum lacunosum-moleculare and in dentate gyrus (PubMed:16009497, PubMed:22098631). Detected in dorsal horn neurons; colocalizes with GRM5 (PubMed:18045912). C-terminally phosphorylated forms are detected in the stratum radiatum and in basilar dendrites in stratum oriens in hippocampus CA1 and on cell bodies in hippocampus CA3 layers, with lower levels in stratum lacunosum-moleculare (PubMed:11040264). In contrast, N-terminally phosphorylated forms are detected in stratum lacunosum moleculare in the hippocampus CA1 layer (PubMed:11040264). Both C-terminally and N-terminally phosphorylated forms are observed on cell bodies and neuronal processes in the amygdala (PubMed:11040264). C-terminally phosphorylated forms are detected in the dentate gyrus molecular layer, while N-terminally phosphorylated forms are detected in the hilus of the dentate gyrus (PubMed:11040264). Both N-terminally and C-terminally phosphorylated forms are detected in the somatosensory cortex (PubMed:11040264). C-terminally phosphorylated forms are detected in the cerebellum granular layers (PubMed:11040264). Detected in heart ventricle myocytes (at protein level) (PubMed:9734479, PubMed:11909823, PubMed:16293790, PubMed:23713033). Detected in brain and heart (PubMed:16293790). {ECO:0000269|PubMed:11040264, ECO:0000269|PubMed:11909823, ECO:0000269|PubMed:16009497, ECO:0000269|PubMed:16293790, ECO:0000269|PubMed:17122039, ECO:0000269|PubMed:17122053, ECO:0000269|PubMed:18045912, ECO:0000269|PubMed:18187474, ECO:0000269|PubMed:22098631, ECO:0000269|PubMed:22612819, ECO:0000269|PubMed:23713033, ECO:0000269|PubMed:9734479}. +Q6PCM1 KDM3A_MOUSE Lysine-specific demethylase 3A (EC 1.14.11.-) (JmjC domain-containing histone demethylation protein 2A) (Jumonji domain-containing protein 1A) 1323 147,847 Alternative sequence (2); Chain (1); Domain (1); Erroneous initiation (1); Metal binding (3); Modified residue (4); Motif (1); Sequence conflict (4); Zinc finger (1) FUNCTION: Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. Preferentially demethylates mono- and dimethylated H3 'Lys-9' residue, with a preference for dimethylated residue, while it has weak or no activity on trimethylated H3 'Lys-9'. Demethylation of Lys residue generates formaldehyde and succinate. Involved in hormone-dependent transcriptional activation, by participating in recruitment to androgen-receptor target genes, resulting in H3 'Lys-9' demethylation and transcriptional activation (By similarity). Involved in spermatogenesis by regulating expression of target genes such as PRM1 and TNP1 which are required for packaging and condensation of sperm chromatin (PubMed:17943087). Involved in obesity resistance through regulation of metabolic genes such as PPARA and UCP1. {ECO:0000250, ECO:0000269|PubMed:17943087, ECO:0000269|PubMed:19194461}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17943087}. Nucleus {ECO:0000269|PubMed:17943087}. Note=Nuclear in round spermatids. When spermatids start to elongate, localizes to the cytoplasm where it forms distinct foci which disappear in mature spermatozoa. DOMAIN: The JmjC domain and the C6-type zinc-finger are required for the demethylation activity. {ECO:0000250}.; DOMAIN: Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs are known to mediate the association with nuclear receptors. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in testis (at protein level). Also expressed at high levels in tissues responsive to sympathetic nerve activity such as brown adipose tissue and skeletal muscle. {ECO:0000269|PubMed:17943087}. +Q6P1G2 KDM2B_MOUSE Lysine-specific demethylase 2B (EC 1.14.11.27) (F-box and leucine-rich repeat protein 10) (F-box protein FBL10) (F-box/LRR-repeat protein 10) (JmjC domain-containing histone demethylation protein 1B) ([Histone-H3]-lysine-36 demethylase 1B) 1309 149,733 Alternative sequence (5); Binding site (2); Chain (1); Coiled coil (1); Compositional bias (1); Cross-link (2); Domain (2); Metal binding (3); Modified residue (10); Repeat (6); Sequence conflict (1); Zinc finger (2) FUNCTION: Histone demethylase that demethylates 'Lys-4' and 'Lys-36' of histone H3, thereby playing a central role in histone code. Preferentially demethylates trimethylated H3 'Lys-4' and dimethylated H3 'Lys-36' residue while it has weak or no activity for mono- and tri-methylated H3 'Lys-36'. Preferentially binds the transcribed region of ribosomal RNA and represses the transcription of ribosomal RNA genes which inhibits cell growth and proliferation. May also serve as a substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. {ECO:0000250|UniProtKB:Q8NHM5}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. SUBUNIT: Directly interacts with SKP1 and CUL1. {ECO:0000250}. DOMAIN: The JmjC domain mediates demethylation activity. It is also required for repression of ribosomal RNA genes (By similarity). {ECO:0000250}. +Q9Z0V1 KCND3_MOUSE Potassium voltage-gated channel subfamily D member 3 (Voltage-gated potassium channel subunit Kv4.3) 655 73,462 Alternative sequence (3); Chain (1); Intramembrane (1); Metal binding (3); Modified residue (4); Motif (1); Region (2); Topological domain (4); Transmembrane (6) INTRAMEM 360 380 Pore-forming; Name=Segment H5. {ECO:0000255}. TRANSMEM 182 202 Helical; Name=Segment S1. {ECO:0000255}.; TRANSMEM 222 242 Helical; Name=Segment S2. {ECO:0000255}.; TRANSMEM 257 277 Helical; Name=Segment S3. {ECO:0000255}.; TRANSMEM 287 307 Helical; Voltage-sensor; Name=Segment S4. {ECO:0000255}.; TRANSMEM 321 341 Helical; Name=Segment S5. {ECO:0000255}.; TRANSMEM 382 402 Helical; Name=Segment S6. {ECO:0000255}. TOPO_DOM 1 181 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 243 256 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 308 320 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 403 655 Cytoplasmic. {ECO:0000255}. FUNCTION: Pore-forming (alpha) subunit of voltage-gated rapidly inactivating A-type potassium channels. May contribute to I(To) current in heart and I(Sa) current in neurons. Channel properties are modulated by interactions with other alpha subunits and with regulatory subunits. PTM: Regulated through phosphorylation at Ser-569 by CaMK2D. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q62897}; Multi-pass membrane protein {ECO:0000255}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:Q62897}; Multi-pass membrane protein {ECO:0000255}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q62897}. Note=Interaction with palmitoylated KCNIP2 and KCNIP3 enhances cell surface expression. {ECO:0000250|UniProtKB:Q62897}. SUBUNIT: Homotetramer or heterotetramer with KCND1 and/or KCND2. Associates with the regulatory subunits KCNIP1, KCNIP2, KCNIP3 and KCNIP4. Interacts with DLG1, KCNE1, KCNE2, SCN1B and KCNAB1 (By similarity). {ECO:0000250}. DOMAIN: The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position. +P41230 KDM5C_MOUSE Lysine-specific demethylase 5C (EC 1.14.11.-) (Histone demethylase JARID1C) (Jumonji/ARID domain-containing protein 1C) (Protein SmcX) (Protein Xe169) 1554 175,313 Alternative sequence (2); Chain (1); Cross-link (6); Domain (3); Metal binding (3); Modified residue (6); Sequence conflict (10); Zinc finger (2) FUNCTION: Histone demethylase that specifically demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-9', H3 'Lys-27', H3 'Lys-36', H3 'Lys-79' or H4 'Lys-20'. Demethylates trimethylated and dimethylated but not monomethylated H3 'Lys-4'. Participates in transcriptional repression of neuronal genes by recruiting histone deacetylases and REST at neuron-restrictive silencer elements (By similarity). Represses the CLOCK-ARNTL/BMAL1 heterodimer-mediated transcriptional activation of the core clock component PER2. {ECO:0000250|UniProtKB:P41229, ECO:0000269|PubMed:21960634}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355, ECO:0000255|PROSITE-ProRule:PRU00537}. SUBUNIT: Part of two distinct complexes, one containing E2F6, and the other containing REST. {ECO:0000250|UniProtKB:P41229}. DOMAIN: The first PHD-type zinc finger domain recognizes and binds H3-K9Me3. {ECO:0000250}.; DOMAIN: Both the JmjC domain and the JmjN domain are required for enzymatic activity. {ECO:0000250}. +Q62240 KDM5D_MOUSE Lysine-specific demethylase 5D (EC 1.14.11.-) (Histocompatibility Y antigen) (H-Y) (Histone demethylase JARID1D) (Jumonji/ARID domain-containing protein 1D) (Protein SmcY) 1548 177,018 Alternative sequence (5); Binding site (4); Chain (1); Cross-link (5); Domain (3); Metal binding (3); Modified residue (5); Sequence conflict (3); Zinc finger (3) FUNCTION: Histone demethylase that specifically demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-9', H3 'Lys-27', H3 'Lys-36', H3 'Lys-79' or H4 'Lys-20'. Demethylates trimethylated and dimethylated but not monomethylated H3 'Lys-4'. May play a role in spermatogenesis. Involved in transcriptional repression of diverse metastasis-associated genes; in this function seems to cooperate with ZMYND8. Suppresses prostate cancer cell invasion. Regulates androgen receptor (AR) transcriptional activity by demethylating H3K4me3 active transcription marks (By similarity). {ECO:0000250|UniProtKB:Q9BY66, ECO:0000269|PubMed:3951555, ECO:0000269|PubMed:7544442}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BY66, ECO:0000255|PROSITE-ProRule:PRU00355, ECO:0000255|PROSITE-ProRule:PRU00537}. SUBUNIT: Interacts withPCGF6, MSH5, ZMYND8, AR. {ECO:0000250|UniProtKB:Q9BY66}. DOMAIN: The JmjC domain is required for enzymatic activity. {ECO:0000250|UniProtKB:Q9BY66}. +O70546 KDM6A_MOUSE Lysine-specific demethylase 6A (EC 1.14.11.-) (Histone demethylase UTX) (Ubiquitously transcribed TPR protein on the X chromosome) (Ubiquitously transcribed X chromosome tetratricopeptide repeat protein) 1401 154,355 Alternative sequence (1); Chain (1); Compositional bias (2); Domain (1); Metal binding (7); Modified residue (5); Region (1); Repeat (8); Sequence caution (1); Sequence conflict (2) FUNCTION: Histone demethylase that specifically demethylates 'Lys-27' of histone H3, thereby playing a central role in histone code. Demethylates trimethylated and dimethylated but not monomethylated H3 'Lys-27'. Plays a central role in regulation of posterior development, by regulating HOX gene expression. Demethylation of 'Lys-27' of histone H3 is concomitant with methylation of 'Lys-4' of histone H3, and regulates the recruitment of the PRC1 complex and monoubiquitination of histone H2A (By similarity). Plays a demethylase-independent role in chromatin remodeling to regulate T-box family member-dependent gene expression (PubMed:21095589). {ECO:0000250|UniProtKB:O15550, ECO:0000269|PubMed:21095589}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Component of the MLL2/3 complex (also named ASCOM complex), at least composed of KMT2D/MLL2 or KMT2C/MLL3, ASH2L, RBBP5, WDR5, NCOA6, DPY30, KDM6A (or KDM6B), PAXIP1/PTIP, PAGR1 and alpha- and beta-tubulin (By similarity). Interacts with TLE1 (PubMed:9854018). Interacts with SUPT6H (PubMed:23503590). Interacts with SMARCA4 (PubMed:21095589). {ECO:0000250|UniProtKB:O15550, ECO:0000269|PubMed:21095589, ECO:0000269|PubMed:23503590, ECO:0000269|PubMed:9854018}. TISSUE SPECIFICITY: Expressed in brain, heart and spleen. +Q69Z36 MEX3B_MOUSE RNA-binding protein MEX3B (RING finger and KH domain-containing protein 3) 601 61,781 Chain (1); Compositional bias (1); Domain (2); Erroneous initiation (1); Modified residue (3); Zinc finger (1) FUNCTION: RNA-binding protein. May be involved in post-transcriptional regulatory mechanisms (By similarity). {ECO:0000250}. PTM: Phosphorylation at Ser-494 creates a docking site for 14-3-3, which stabilizes the protein and modulates its ability to bind RNA. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, P-body {ECO:0000250}. Cytoplasmic granule {ECO:0000250}. Note=Predominantly expressed in the cytoplasm and shuttles between the cytoplasm and the nucleus through the CRM1 export pathway. Localization to P-bodies is dependent on 14-3-3 (By similarity). {ECO:0000250}. DOMAIN: Binds RNA through its KH domains. {ECO:0000250}. +Q6PDE8 MF13A_MOUSE Transmembrane protein 180 (Major facilitator superfamily domain-containing 13A) 519 57,898 Chain (1); Frameshift (1); Glycosylation (1); Transmembrane (11) TRANSMEM 9 29 Helical. {ECO:0000255}.; TRANSMEM 52 72 Helical. {ECO:0000255}.; TRANSMEM 101 123 Helical. {ECO:0000255}.; TRANSMEM 127 149 Helical. {ECO:0000255}.; TRANSMEM 164 184 Helical. {ECO:0000255}.; TRANSMEM 194 214 Helical. {ECO:0000255}.; TRANSMEM 266 286 Helical. {ECO:0000255}.; TRANSMEM 306 326 Helical. {ECO:0000255}.; TRANSMEM 332 354 Helical. {ECO:0000255}.; TRANSMEM 401 421 Helical. {ECO:0000255}.; TRANSMEM 468 488 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +P70187 MF14A_MOUSE Hippocampus abundant transcript 1 protein (Major facilitator superfamily domain-containing 14A) 490 53,000 Chain (1); Compositional bias (1); Glycosylation (2); Modified residue (1); Sequence conflict (2); Topological domain (13); Transmembrane (12) TRANSMEM 41 61 Helical; Name=1. {ECO:0000255}.; TRANSMEM 75 95 Helical; Name=2. {ECO:0000255}.; TRANSMEM 104 124 Helical; Name=3. {ECO:0000255}.; TRANSMEM 127 147 Helical; Name=4. {ECO:0000255}.; TRANSMEM 161 181 Helical; Name=5. {ECO:0000255}.; TRANSMEM 189 209 Helical; Name=6. {ECO:0000255}.; TRANSMEM 244 264 Helical; Name=7. {ECO:0000255}.; TRANSMEM 285 305 Helical; Name=8. {ECO:0000255}.; TRANSMEM 314 334 Helical; Name=9. {ECO:0000255}.; TRANSMEM 338 358 Helical; Name=10. {ECO:0000255}.; TRANSMEM 380 400 Helical; Name=11. {ECO:0000255}.; TRANSMEM 428 448 Helical; Name=12. {ECO:0000255}. TOPO_DOM 1 40 Extracellular. {ECO:0000255}.; TOPO_DOM 62 74 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 96 103 Extracellular. {ECO:0000255}.; TOPO_DOM 125 126 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 148 160 Extracellular. {ECO:0000255}.; TOPO_DOM 182 188 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 210 243 Extracellular. {ECO:0000255}.; TOPO_DOM 265 284 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 306 313 Extracellular. {ECO:0000255}.; TOPO_DOM 335 337 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 359 379 Extracellular. {ECO:0000255}.; TOPO_DOM 401 427 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 449 490 Extracellular. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in various tissues. {ECO:0000269|PubMed:9299464}. +Q8CIA9 MF14B_MOUSE Hippocampus abundant transcript-like protein 1 (Major facilitator superfamily domain-containing 14B) 507 55,087 Chain (1); Erroneous initiation (3); Glycosylation (2); Topological domain (13); Transmembrane (12) TRANSMEM 52 72 Helical. {ECO:0000255}.; TRANSMEM 85 105 Helical. {ECO:0000255}.; TRANSMEM 114 134 Helical. {ECO:0000255}.; TRANSMEM 137 157 Helical. {ECO:0000255}.; TRANSMEM 171 191 Helical. {ECO:0000255}.; TRANSMEM 199 219 Helical. {ECO:0000255}.; TRANSMEM 258 278 Helical. {ECO:0000255}.; TRANSMEM 284 304 Helical. {ECO:0000255}.; TRANSMEM 324 344 Helical. {ECO:0000255}.; TRANSMEM 348 368 Helical. {ECO:0000255}.; TRANSMEM 390 410 Helical. {ECO:0000255}.; TRANSMEM 431 451 Helical. {ECO:0000255}. TOPO_DOM 1 51 Extracellular. {ECO:0000255}.; TOPO_DOM 73 84 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 106 113 Extracellular. {ECO:0000255}.; TOPO_DOM 135 136 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 158 170 Extracellular. {ECO:0000255}.; TOPO_DOM 192 198 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 220 257 Extracellular. {ECO:0000255}.; TOPO_DOM 279 283 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 305 323 Extracellular. {ECO:0000255}.; TOPO_DOM 345 347 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 369 389 Extracellular. {ECO:0000255}.; TOPO_DOM 411 430 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 452 507 Extracellular. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8VCV9 MF4B1_MOUSE Sodium-dependent glucose transporter 1A (Major facilitator superfamily domain-containing protein 4B1) 425 45,686 Chain (1); Compositional bias (1); Erroneous initiation (2); Sequence conflict (1); Transmembrane (11) TRANSMEM 35 55 Helical. {ECO:0000255}.; TRANSMEM 61 81 Helical. {ECO:0000255}.; TRANSMEM 84 104 Helical. {ECO:0000255}.; TRANSMEM 123 143 Helical. {ECO:0000255}.; TRANSMEM 183 203 Helical. {ECO:0000255}.; TRANSMEM 228 248 Helical. {ECO:0000255}.; TRANSMEM 271 291 Helical. {ECO:0000255}.; TRANSMEM 294 314 Helical. {ECO:0000255}.; TRANSMEM 320 340 Helical. {ECO:0000255}.; TRANSMEM 355 375 Helical. {ECO:0000255}.; TRANSMEM 382 402 Helical. {ECO:0000255}. FUNCTION: May function as a sodium-dependent glucose transporter. Potential channels for urea in the inner medulla of kidney. {ECO:0000250|UniProtKB:Q80T22}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:Q80T22}; Multi-pass membrane protein {ECO:0000250}. +Q9D8I5 MF4B2_MOUSE Sodium-dependent glucose transporter 1B (Major facilitator superfamily domain-containing protein 4B2) 366 39,507 Chain (1); Compositional bias (1); Glycosylation (2); Transmembrane (10) TRANSMEM 13 33 Helical. {ECO:0000255}.; TRANSMEM 36 56 Helical. {ECO:0000255}.; TRANSMEM 75 95 Helical. {ECO:0000255}.; TRANSMEM 136 156 Helical. {ECO:0000255}.; TRANSMEM 185 205 Helical. {ECO:0000255}.; TRANSMEM 224 244 Helical. {ECO:0000255}.; TRANSMEM 247 267 Helical. {ECO:0000255}.; TRANSMEM 273 293 Helical. {ECO:0000255}.; TRANSMEM 308 328 Helical. {ECO:0000255}.; TRANSMEM 335 355 Helical. {ECO:0000255}. FUNCTION: May function as a sodium-dependent glucose transporter. Potential channels for urea in the inner medulla of kidney. {ECO:0000250|UniProtKB:Q80T22}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:Q80T22}; Multi-pass membrane protein {ECO:0000250}. +Q3UN21 MF4B3_MOUSE Sodium-dependent glucose transporter 1C (Major facilitator superfamily domain-containing protein 4B3) 355 38,419 Chain (1); Compositional bias (1); Glycosylation (2); Transmembrane (9) TRANSMEM 36 56 Helical. {ECO:0000255}.; TRANSMEM 66 86 Helical. {ECO:0000255}.; TRANSMEM 127 147 Helical. {ECO:0000255}.; TRANSMEM 172 192 Helical. {ECO:0000255}.; TRANSMEM 215 235 Helical. {ECO:0000255}.; TRANSMEM 238 258 Helical. {ECO:0000255}.; TRANSMEM 264 284 Helical. {ECO:0000255}.; TRANSMEM 299 319 Helical. {ECO:0000255}.; TRANSMEM 326 346 Helical. {ECO:0000255}. FUNCTION: May function as a sodium-dependent glucose transporter. Potential channels for urea in the inner medulla of kidney. {ECO:0000250|UniProtKB:Q80T22}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:Q80T22}; Multi-pass membrane protein {ECO:0000250}. +P55002 MFAP2_MOUSE Microfibrillar-associated protein 2 (MFAP-2) (Microfibril-associated glycoprotein 1) (MAGP) (MAGP-1) 183 20,578 Chain (1); Compositional bias (1); Disulfide bond (3); Domain (1); Modified residue (4); Signal peptide (1) FUNCTION: Component of the elastin-associated microfibrils. PTM: Forms intermolecular disulfide bonds either with other MAGP-1 molecules or with other components of the microfibrils. May form transglutaminase cross-links.; PTM: O-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SUBUNIT: Forms a ternary complex with BGN and ELN. Interacts with FBN1 (via N-terminal domain) and FBN2. {ECO:0000250|UniProtKB:P27424}. +Q9QZJ6 MFAP5_MOUSE Microfibrillar-associated protein 5 (MFAP-5) (Microfibril-associated glycoprotein 2) (MAGP-2) 164 18,538 Chain (1); Glycosylation (1); Motif (1); Sequence conflict (2); Signal peptide (1) FUNCTION: May play a role in hematopoiesis. In the cardiovascular system, could regulate growth factors or participate in cell signaling in maintaining large vessel integrity (PubMed:23963447). Component of the elastin-associated microfibrils (By similarity). {ECO:0000250|UniProtKB:Q13361, ECO:0000269|PubMed:23963447}. PTM: Forms intermolecular disulfide bonds either with other MAGP-2 molecules or with other components of the microfibrils. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. SUBUNIT: Interacts with TGFB2 (PubMed:23963447). Interacts with BMP2. Interacts with FBN1 (via N-terminal domain) and FBN2 (By similarity). {ECO:0000250|UniProtKB:Q28022, ECO:0000269|PubMed:23963447}. +Q6PDC8 MFD4A_MOUSE Major facilitator superfamily domain-containing protein 4A (Major facilitator superfamily domain-containing protein 4) 510 56,183 Alternative sequence (3); Chain (1); Erroneous initiation (1); Transmembrane (12) TRANSMEM 19 39 Helical. {ECO:0000255}.; TRANSMEM 53 73 Helical. {ECO:0000255}.; TRANSMEM 82 102 Helical. {ECO:0000255}.; TRANSMEM 107 127 Helical. {ECO:0000255}.; TRANSMEM 139 159 Helical. {ECO:0000255}.; TRANSMEM 218 238 Helical. {ECO:0000255}.; TRANSMEM 303 323 Helical. {ECO:0000255}.; TRANSMEM 345 365 Helical. {ECO:0000255}.; TRANSMEM 380 400 Helical. {ECO:0000255}.; TRANSMEM 401 421 Helical. {ECO:0000255}.; TRANSMEM 434 454 Helical. {ECO:0000255}.; TRANSMEM 462 482 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q6PCP5 MFF_MOUSE Mitochondrial fission factor 291 32,931 Alternative sequence (3); Chain (1); Coiled coil (1); Modified residue (10); Topological domain (2); Transmembrane (1) TRANSMEM 272 289 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 1 271 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 290 291 Mitochondrial intermembrane. {ECO:0000255}. FUNCTION: Plays a role in mitochondrial and peroxisomal fission. Promotes the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface. May be involved in regulation of synaptic vesicle membrane dynamics by recruitment of DNM1L to clathrin-containing vesicles. {ECO:0000269|PubMed:23283981}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Peroxisome {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250}. SUBUNIT: Homodimer. Interacts with DNM1L (By similarity). {ECO:0000250}. +Q80U63 MFN2_MOUSE Mitofusin-2 (EC 3.6.5.-) (Hypertension-related protein 1) (Mitochondrial assembly regulatory factor) (HSG protein) (Transmembrane GTPase MFN2) 757 86,188 Alternative sequence (2); Binding site (2); Chain (1); Coiled coil (2); Domain (1); Erroneous initiation (1); Modified residue (3); Nucleotide binding (2); Region (8); Sequence conflict (17); Topological domain (3); Transmembrane (2) TRANSMEM 605 625 Helical; Name=1. {ECO:0000255}.; TRANSMEM 627 647 Helical; Name=2. {ECO:0000255}. TOPO_DOM 1 604 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 626 626 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 648 757 Cytoplasmic. {ECO:0000255}. FUNCTION: Mitochondrial outer membrane GTPase that mediates mitochondrial clustering and fusion (PubMed:12527753, PubMed:23921378, PubMed:23620051). Mitochondria are highly dynamic organelles, and their morphology is determined by the equilibrium between mitochondrial fusion and fission events. Overexpression induces the formation of mitochondrial networks. Membrane clustering requires GTPase activity and may involve a major rearrangement of the coiled coil domains (By similarity). Plays a central role in mitochondrial metabolism and may be associated with obesity and/or apoptosis processes. Plays an important role in the regulation of vascular smooth muscle cell proliferation (By similarity). Involved in the clearance of damaged mitochondria via selective autophagy (mitophagy). Is required for PRKN recruitment to dysfunctional mitochondria (PubMed:23620051). Involved in the control of unfolded protein response (UPR) upon ER stress including activation of apoptosis and autophagy during ER stress (PubMed:23921556). Acts as an upstream regulator of EIF2AK3 and suppresses EIF2AK3 activation under basal conditions (PubMed:23921556). {ECO:0000250|UniProtKB:O95140, ECO:0000250|UniProtKB:Q8R500, ECO:0000269|PubMed:12527753, ECO:0000269|PubMed:23620051, ECO:0000269|PubMed:23921378, ECO:0000269|PubMed:23921556}. PTM: Phosphorylated by PINK1. {ECO:0000269|PubMed:23620051}.; PTM: Ubiquitinated by non-degradative ubiquitin by PRKN, promoting mitochondrial fusion; deubiquitination by USP30 inhibits mitochondrial fusion. {ECO:0000269|PubMed:23620051, ECO:0000269|PubMed:24513856}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:O95140}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O95140}. Note=Colocalizes with BAX during apoptosis. {ECO:0000250|UniProtKB:O95140}. SUBUNIT: Forms homomultimers and heteromultimers with MFN1 (PubMed:12527753). Oligomerization is essential for mitochondrion fusion (Probable). Interacts with VAT1 (By similarity). Interacts with STOML2; may form heterooligomers (By similarity). Interacts (phosphorylated) with PRKN (PubMed:23620051). Interacts with EIF2AK3 (By similarity). {ECO:0000250|UniProtKB:O95140, ECO:0000250|UniProtKB:Q8R500, ECO:0000269|PubMed:23620051, ECO:0000269|PubMed:23921556, ECO:0000305}. DOMAIN: A helix bundle is formed by helices from the N-terminal and the C-terminal part of the protein. The GTPase domain cannot be expressed by itself, without the helix bundle. Rearrangement of the helix bundle and/or of the coiled coil domains may bring membranes from adjacent mitochondria into close contact, and thereby play a role in mitochondrial fusion. {ECO:0000250|UniProtKB:Q8IWA4}. TISSUE SPECIFICITY: Ubiquitous. Expression is markedly reduced in ApoE-knockout mouse atherosclerotic arteries. {ECO:0000269|PubMed:11950885, ECO:0000269|PubMed:15322553}. +O09008 MFNG_MOUSE Beta-1,3-N-acetylglucosaminyltransferase manic fringe (EC 2.4.1.222) (O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase) 321 36,200 Active site (1); Beta strand (12); Binding site (2); Chain (1); Disulfide bond (3); Glycosylation (2); Helix (15); Metal binding (2); Topological domain (2); Transmembrane (1); Turn (4) TRANSMEM 8 27 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 7 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 28 321 Lumenal. {ECO:0000255}. FUNCTION: Glycosyltransferase that initiates the elongation of O-linked fucose residues attached to EGF-like repeats in the extracellular domain of Notch molecules. Modulates NOTCH1 activity by modifying O-fucose residues at specific EGF-like domains resulting in inhibition of NOTCH1 activation by JAG1 and enhancement of NOTCH1 activation by DLL1 via an increase in its binding to DLL1. {ECO:0000269|PubMed:28089369}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. +Q9DCY0 KEG1_MOUSE Glycine N-acyltransferase-like protein Keg1 (EC 2.3.1.13) (Acyl-CoA:glycine N-acyltransferase protein Keg1) (Kidney-expressed gene 1 protein) 295 33,723 Chain (1); Modified residue (16) FUNCTION: Acyltransferase which transfers the acyl group to the N-terminus of glycine. Can conjugate a multitude of substrates to form a variety of N-acylglycines (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Note=Also localizes in regions surrounding the centrosome. The centrosomal localization is dependent on microtubules (By similarity). {ECO:0000250}. SUBUNIT: Binds to microtubules. {ECO:0000250}. +Q9EQF2 KELL_MOUSE Kell blood group glycoprotein homolog (EC 3.4.24.-) (CD antigen CD238) 713 80,866 Active site (2); Chain (1); Disulfide bond (1); Glycosylation (8); Metal binding (3); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 29 48 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 28 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 49 713 Extracellular. {ECO:0000255}. FUNCTION: Zinc endopeptidase with endothelin-3-converting enzyme activity. Cleaves EDN1, EDN2 and EDN3 (By similarity). {ECO:0000250, ECO:0000269|PubMed:11132157}. PTM: N-glycosylated. {ECO:0000269|PubMed:11132157}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Spans the erythrocyte membrane, and is attached to the underlying cytoskeleton. {ECO:0000250}. SUBUNIT: Heterodimer with XK; disulfide-linked. {ECO:0000269|PubMed:11132157}. TISSUE SPECIFICITY: Highly expressed in spleen. Weaker expression in testis and heart. {ECO:0000269|PubMed:11132157}. +Q8K4H1 KFA_MOUSE Kynurenine formamidase (KFA) (KFase) (EC 3.5.1.9) (Arylformamidase) (N-formylkynurenine formamidase) (FKF) 305 34,229 Active site (3); Alternative sequence (1); Chain (1); Erroneous initiation (1); Motif (1); Mutagenesis (3); Sequence conflict (2) Amino-acid degradation; L-tryptophan degradation via kynurenine pathway; L-kynurenine from L-tryptophan: step 2/2. FUNCTION: Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-kynurenine, the second step in the kynurenine pathway of tryptophan degradation. Kynurenine may be further oxidized to nicotinic acid, NAD(H) and NADP(H). Required for elimination of toxic metabolites. {ECO:0000255|HAMAP-Rule:MF_03014, ECO:0000269|PubMed:12007602}. PTM: The N-terminus is blocked. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000255|HAMAP-Rule:MF_03014, ECO:0000269|PubMed:12411446}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03014, ECO:0000269|PubMed:12411446}. Note=Predominantly cytosolic. Some fraction is nuclear. SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03014}. DOMAIN: The main chain amide nitrogen atoms of the second glycine and its adjacent residue in the HGGXW motif define the oxyanion hole, and stabilize the oxyanion that forms during the nucleophilic attack by the catalytic serine during substrate cleavage. {ECO:0000255|HAMAP-Rule:MF_03014}. TISSUE SPECIFICITY: Highly expressed in liver. Expressed in kidney. Weakly or not expressed in other tissues. {ECO:0000269|PubMed:12411446}. +Q91VS7 MGST1_MOUSE Microsomal glutathione S-transferase 1 (Microsomal GST-1) (EC 2.5.1.18) (Microsomal GST-I) 155 17,552 Binding site (6); Chain (1); Modified residue (3); Sequence conflict (2); Site (1); Topological domain (5); Transmembrane (4) TRANSMEM 10 33 Helical. {ECO:0000250}.; TRANSMEM 63 96 Helical. {ECO:0000250}.; TRANSMEM 100 123 Helical. {ECO:0000250}.; TRANSMEM 129 148 Helical. {ECO:0000250}. TOPO_DOM 3 9 Lumenal. {ECO:0000250}.; TOPO_DOM 34 62 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 97 99 Lumenal. {ECO:0000250}.; TOPO_DOM 124 128 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 149 155 Lumenal. {ECO:0000250}. FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. {ECO:0000250}. PTM: Acetylation of Lys-42 and Lys-55 is observed in liver mitochondria from fasted mice but not from fed mice.; PTM: Peroxynitrite induces nitration at Tyr-93 which activates the enzyme. {ECO:0000250}. SUBCELLULAR LOCATION: Microsome {ECO:0000250}. Mitochondrion outer membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Homotrimer; The trimer binds only one molecule of glutathione. {ECO:0000250}. +Q9CPU4 MGST3_MOUSE Microsomal glutathione S-transferase 3 (Microsomal GST-3) (EC 2.5.1.18) (Microsomal GST-III) 153 16,958 Chain (1); Lipidation (1); Sequence conflict (1); Transmembrane (3) TRANSMEM 9 29 Helical. {ECO:0000255}.; TRANSMEM 71 91 Helical. {ECO:0000255}.; TRANSMEM 120 140 Helical. {ECO:0000255}. FUNCTION: Also functions as a glutathione peroxidase. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Microsome membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Microsome membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. +Q812G0 MGT4A_MOUSE Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A (EC 2.4.1.145) (N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase IVa) (GlcNAc-T IVa) (GnT-IVa) (N-acetylglucosaminyltransferase IVa) (UDP-N-acetylglucosamine: alpha-1,3-D-mannoside beta-1,4-N-acetylglucosaminyltransferase IVa) [Cleaved into: Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A soluble form] 535 61,480 Alternative sequence (1); Chain (2); Coiled coil (1); Glycosylation (2); Modified residue (1); Sequence conflict (3); Topological domain (2); Transmembrane (1) TRANSMEM 7 27 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 28 535 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Glycosyltransferase that participates in the transfer of N-acetylglucosamine (GlcNAc) to the core mannose residues of N-linked glycans. Catalyzes the formation of the GlcNAcbeta1-4 branch on the GlcNAcbeta1-2Manalpha1-3 arm of the core structure of N-linked glycans. Essential for the production of tri- and tetra-antennary N-linked sugar chains. Involved in glucose transport by mediating SLC2A2/GLUT2 glycosylation, thereby controlling cell-surface expression of SLC2A2 in pancreatic beta cells. {ECO:0000269|PubMed:16377570}. SUBCELLULAR LOCATION: Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A soluble form: Secreted {ECO:0000250}. +Q812F8 MGT4B_MOUSE Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase B (EC 2.4.1.145) (N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase IVb) (GlcNAc-T IVb) (GnT-IVb) (N-acetylglucosaminyltransferase IVb) (UDP-N-acetylglucosamine: alpha-1,3-D-mannoside beta-1,4-N-acetylglucosaminyltransferase IVb) 548 63,302 Chain (1); Coiled coil (1); Erroneous initiation (2); Glycosylation (2); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 8 28 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 7 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 29 548 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Glycosyltransferase that participates in the transfer of N-acetylglucosamine (GlcNAc) to the core mannose residues of N-linked glycans. Catalyzes the formation of the GlcNAcbeta1-4 branch on the GlcNAcbeta1-2Manalpha1-3 arm of the core structure of N-linked glycans. Essential for the production of tri- and tetra-antennary N-linked sugar chains. Has lower affinities for donors or acceptors than MGAT4A, suggesting that, under physiological conditions, it is not the main contributor in N-glycan biosynthesis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. +Q3TCX3 KHDC4_MOUSE KH homology domain-containing protein 4 (Brings lots of money 7) (Pre-mRNA splicing factor protein Khdc4) 612 64,563 Alternative sequence (6); Chain (1); Compositional bias (1); Domain (2); Erroneous initiation (1); Modified residue (2); Region (1); Sequence conflict (5) FUNCTION: RNA-binding protein involved in pre-mRNA splicing. Interacts with the PRP19C/Prp19 complex/NTC/Nineteen complex which is part of the spliceosome. Involved in regulating splice site selection. Binds preferentially RNA with A/C rich sequences and poly-C stretches. {ECO:0000250|UniProtKB:Q7Z7F0}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q7Z7F0}. Cytoplasm {ECO:0000250|UniProtKB:Q7Z7F0}. SUBUNIT: Interacts with PRPF19. Isoform 2: Interacts with U2AF65. {ECO:0000250|UniProtKB:Q7Z7F0}. DOMAIN: The C-terminal part is necessary for the interaction with the PRP19C/Prp19 complex/NTC/Nineteen complex. {ECO:0000250|UniProtKB:Q7Z7F0}.; DOMAIN: The KH domains mediate RNA-binding. {ECO:0000250|UniProtKB:Q7Z7F0}. +Q60749 KHDR1_MOUSE KH domain-containing, RNA-binding, signal transduction-associated protein 1 (GAP-associated tyrosine phosphoprotein p62) (Src-associated in mitosis 68 kDa protein) (Sam68) (p21 Ras GTPase-activating protein-associated p62) (p68) 443 48,371 Chain (1); Compositional bias (7); Cross-link (5); Domain (1); Modified residue (44); Mutagenesis (4); Region (3); Sequence conflict (6) FUNCTION: Recruited and tyrosine phosphorylated by several receptor systems, for example the T-cell, leptin and insulin receptors. Once phosphorylated, functions as an adapter protein in signal transduction cascades by binding to SH2 and SH3 domain-containing proteins. Role in G2-M progression in the cell cycle. Represses CBP-dependent transcriptional activation apparently by competing with other nuclear factors for binding to CBP. Also acts as a putative regulator of mRNA stability and/or translation rates and mediates mRNA nuclear export. Positively regulates the association of constitutive transport element (CTE)-containing mRNA with large polyribosomes and translation initiation. May not be involved in the nucleocytoplasmic export of unspliced (CTE)-containing RNA species. RNA-binding protein that plays a role in the regulation of alternative splicing and influences mRNA splice site selection and exon inclusion. Binds to RNA containing 5'-[AU]UAA-3' as a bipartite motif spaced by more than 15 nucleotides. Binds poly(A). In cooperation with HNRNPA1 modulates alternative splicing of BCL2L1 by promoting splicing toward isoform Bcl-X(S), and of SMN1 (By similarity). Can regulate CD44 alternative splicing in a Ras pathway-dependent manner. Can regulate alternative splicing of NRXN1 and NRXN3 in the laminin G-like domain 6 containing the evolutionary conserved neurexin alternative spliced segment 4 (AS4) involved in neurexin selective targeting to postsynaptic partners. In a neuronal activity-dependent manner cooperates synergistically with KHDRBS2/SLIM-1 in regulation of NRXN1 exon skipping at AS4. The cooperation with KHDRBS2/SLIM-1 is antagonistic for regulation of NXRN3 alternative splicing at AS4 (PubMed:12478298, PubMed:22196734, PubMed:24469635). {ECO:0000250|UniProtKB:O75525, ECO:0000269|PubMed:12478298, ECO:0000269|PubMed:12496368, ECO:0000269|PubMed:22196734, ECO:0000269|PubMed:24469635, ECO:0000269|PubMed:7512695, ECO:0000269|PubMed:9315629}. PTM: Tyrosine phosphorylated by several non-receptor tyrosine kinases including LCK, FYN and JAK3. Also tyrosine phosphorylated by the non-receptor tyrosine kinase SRMS in an EGF-dependent manner (By similarity). Phosphorylation by PTK6 negatively regulates its RNA binding ability. Phosphorylation by PTK6 at Tyr-440 dictates the nuclear localization of KHDRBS1. Phosphorylation by MAPK1 at Ser-58, Thr-71 and Thr-84 regulates CD44 alternative splicing by promoting CD44 exon v5 inclusion. {ECO:0000250|UniProtKB:Q07666, ECO:0000269|PubMed:12478298, ECO:0000269|PubMed:7512695}.; PTM: Acetylated. Positively correlates with ability to bind RNA (By similarity). {ECO:0000250|UniProtKB:Q07666}.; PTM: Arginine methylation is required for nuclear localization. Inhibits interaction with Src-like SH3 domains, but not interaction with WW domains of WBP4/FBP21 AND FNBP4/FBP30 (By similarity). {ECO:0000250|UniProtKB:Q07666}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12496368}. Cytoplasm {ECO:0000250|UniProtKB:Q07666}. Membrane {ECO:0000269|PubMed:12496368}. Note=Predominantly located in the nucleus but also located partially in the cytoplasm. {ECO:0000250|UniProtKB:Q07666}. SUBUNIT: Self-associates to form homooligomers when bound to RNA, oligomerization appears to be limited when binding to proteins (PubMed:9315629). Interacts with KHDRBS3/SLIM-2 and KHDRBS2/SLIM-1; heterooligomer formation of KHDRBS family proteins may modulate RNA substrate specificity (PubMed:10077576, PubMed:24469635). Interacts with RASA1, FYN, GRB2, PLCG1, SRC, RBMY1A1, CBP, PRMT1 (PubMed:7799925, PubMed:7512695, PubMed:10077576, PubMed:10823932, PubMed:12496368, PubMed:12529443). Interacts with PTK6 (via SH3 and SH2 domains). Forms a complex with ILF2, ILF3, YLPM1, RBMX, NCOA5 and PPP1CA. Binds WBP4/FBP21 (via WW domains), FNBP4/FBP30 (via WW domains). Interacts (via Arg/Gly-rich-flanked Pro-rich regions) with FYN (via the SH3 domain). Interacts with APC, HNRNPA1 (By similarity). Interacts with the non-receptor tyrosine kinase SRMS; the interaction leads to phosphorylation of KHDRBS1 (By similarity). Interacts with ZBTB7A; negatively regulates KHDRBS1 splicing activity toward BCL2L1 (By similarity). {ECO:0000250|UniProtKB:Q07666, ECO:0000250|UniProtKB:Q91V33, ECO:0000269|PubMed:10077576, ECO:0000269|PubMed:12496368, ECO:0000269|PubMed:12529443, ECO:0000269|PubMed:24469635, ECO:0000269|PubMed:7512695, ECO:0000269|PubMed:7799925, ECO:0000269|PubMed:9315629}. DOMAIN: The KH domain is required for binding to RNA. {ECO:0000269|PubMed:9315629}.; DOMAIN: The Pro-rich domains are flanked by Arg/Gly-rich motifs which can be asymmetric dimethylated on arginine residues to give the DMA/Gly-rich regions. Selective methylation on these motifs can modulate protein-protein interactions (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: In adult cerebellum expressed in most neuronal cell populations, specifically in cerebellar granule cells of the internal granular layer, ROR(alpha)-positive Purkinje cells, internal granular layer and molecuar layer interneurons (at protein level). {ECO:0000269|PubMed:22196734}. +Q9WU01 KHDR2_MOUSE KH domain-containing, RNA-binding, signal transduction-associated protein 2 (Sam68-like mammalian protein 1) (SLM-1) (mSLM-1) 349 38,866 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (1); Modified residue (2); Sequence conflict (1) FUNCTION: RNA-binding protein that plays a role in the regulation of alternative splicing and influences mRNA splice site selection and exon inclusion (By similarity). Binds both poly(A) and poly(U) homopolymers. Phosphorylation by PTK6 inhibits its RNA-binding ability. Induces an increased concentration-dependent incorporation of exon in CD44 pre-mRNA by direct binding to purine-rich exonic enhancer (By similarity). Can regulate alternative splicing of neurexins NRXN1-3 in the laminin G-like domain 6 containing the evolutionary conserved neurexin alternative spliced segment 4 (AS4) involved in neurexin selective targeting to postsynaptic partners. Regulates cell-type specific alternative splicing of NRXN1 at AS4 and acts synergystically with SAM68 in exon skipping. In contrast acts antagonistically with SAM68 in NRXN3 exon skipping at AS4 (PubMed:22196734, PubMed:24469635). Its phosphorylation by FYN inhibits its ability to regulate splice site selection (By similarity). May function as an adapter protein for Src kinases during mitosis (PubMed:10077576). {ECO:0000250|UniProtKB:Q920F3, ECO:0000269|PubMed:10077576, ECO:0000269|PubMed:15471878, ECO:0000269|PubMed:22196734, ECO:0000269|PubMed:24469635}. PTM: Methylated. {ECO:0000250|UniProtKB:Q5VWX1}.; PTM: Tyrosine phosphorylated by FYN, PTK6 and SRC. Tyrosine phosphorylated by SRC during mitosis. {ECO:0000269|PubMed:10077576, ECO:0000269|PubMed:15471878}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10077576, ECO:0000269|PubMed:15471878}. SUBUNIT: Self-associates to form homooligomers (By similarity). Interacts with KHDRBS1/SAM68; heterooligomer formation of KHDRBS family proteins may modulate RNA substrate specificity (PubMed:10077576). Interacts with RBMX, SAFB, SFRS9 and YTHDC1 (By similarity). Interacts with FYN and PLCG1 (via SH3 domain). Interacts (phosphorylated) with FYN, GRB2, PLCG1 and RASA1 (via SH2 domain) (PubMed:10077576). {ECO:0000250|UniProtKB:Q5VWX1, ECO:0000250|UniProtKB:Q920F3, ECO:0000269|PubMed:10077576}. TISSUE SPECIFICITY: Expressed in heart, skin, brain, colon, spleen, kidney, cervix and testis. In adult cerebellum expressed predominantly in Purkinje cells and in the hippocampus is abundantly expressed in glutamatergic dentate granule cells and in specific inhibitory Schaffer collateral-associated and path-associated interneurons; expression is restricted to neuronal subpopulations largely non-overlapping with expression of KHDRBS3/SLM-2 (at protein level). {ECO:0000269|PubMed:15471878, ECO:0000269|PubMed:22196734}. +P97328 KHK_MOUSE Ketohexokinase (EC 2.7.1.3) (Hepatic fructokinase) 298 32,750 Binding site (6); Chain (1); Nucleotide binding (1); Sequence conflict (1) Carbohydrate metabolism; fructose metabolism. FUNCTION: Catalyzes the phosphorylation of the ketose sugar fructose to fructose-1-phosphate. {ECO:0000250|UniProtKB:P50053}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P50053}. +Q8K273 MMGT1_MOUSE Membrane magnesium transporter 1 (ER membrane protein complex subunit 5) (Transmembrane protein 32) 131 14,677 Chain (1); Modified residue (1); Topological domain (3); Transmembrane (2) TRANSMEM 5 25 Helical. {ECO:0000255}.; TRANSMEM 45 65 Helical. {ECO:0000255}. TOPO_DOM 1 4 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 26 44 Lumenal. {ECO:0000305}.; TOPO_DOM 66 131 Cytoplasmic. {ECO:0000305}. FUNCTION: Mediates Mg(2+) transport. {ECO:0000269|PubMed:18057121}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8N4V1}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:18057121}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000269|PubMed:18057121}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Component of the ER membrane protein complex (EMC). {ECO:0000250|UniProtKB:Q8N4V1}. TISSUE SPECIFICITY: Abundant in heart muscle and kidney with lower levels in liver and brain and very little expression in intestine or colon. In kidney, highest levels in distal convoluted tubule. {ECO:0000269|PubMed:18057121}. +Q8R3L0 MMGT2_MOUSE Membrane magnesium transporter 2 123 13,922 Chain (1); Topological domain (3); Transmembrane (2) TRANSMEM 2 22 Helical. {ECO:0000255}.; TRANSMEM 41 61 Helical. {ECO:0000255}. TOPO_DOM 1 1 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 23 40 Lumenal. {ECO:0000305}.; TOPO_DOM 62 123 Cytoplasmic. {ECO:0000305}. FUNCTION: Mediates Mg(2+) transport. {ECO:0000269|PubMed:18057121}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:18057121}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000269|PubMed:18057121}; Multi-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: High expression levels in brain and kidney with lower levels in heart, colon and liver. Very low levels in intestine. In kidney, highest levels in distal convoluted tubule. {ECO:0000269|PubMed:18057121}. +Q99KR3 LACB2_MOUSE Endoribonuclease LACTB2 (Beta-lactamase-like protein 2) (EC 3.1.27.-) 288 32,754 Chain (1); Metal binding (10); Modified residue (4) FUNCTION: Endoribonuclease; cleaves preferentially 3' to purine-pyrimidine dinucleotide motifs in single-stranded RNA. The cleavage product contains a free 3' -OH group. Has no activity with double-stranded RNA or DNA. Required for normal mitochondrial function and cell viability. {ECO:0000250|UniProtKB:Q53H82}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:Q53H82}. SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q53H82}. +P33435 MMP13_MOUSE Collagenase 3 (EC 3.4.24.-) (Matrix metalloproteinase-13) (MMP-13) 472 54,182 Active site (1); Beta strand (11); Chain (1); Disulfide bond (1); Glycosylation (3); Helix (3); Metal binding (30); Modified residue (1); Motif (1); Propeptide (1); Region (2); Repeat (4); Signal peptide (1); Turn (1) FUNCTION: Plays a role in the degradation of extracellular matrix proteins including fibrillar collagen, fibronectin, TNC and ACAN. Cleaves triple helical collagens, including type I, type II and type III collagen, but has the highest activity with soluble type II collagen. Can also degrade collagen type IV, type XIV and type X. May also function by activating or degrading key regulatory proteins, such as TGFB1 and CTGF. Plays a role in wound healing, tissue remodeling, cartilage degradation, bone development, bone mineralization and ossification. Required for normal embryonic bone development and ossification. Plays a role in the healing of bone fractures via endochondral ossification. Plays a role in wound healing, probably by a mechanism that involves proteolytic activation of TGFB1 and degradation of CTGF. Plays a role in keratinocyte migration during wound healing. May play a role in cell migration and in tumor cell invasion. {ECO:0000269|PubMed:15539485, ECO:0000269|PubMed:15563592, ECO:0000269|PubMed:17987127, ECO:0000269|PubMed:19590036, ECO:0000269|PubMed:22880047}. PTM: The proenzyme is activated by removal of the propeptide; this cleavage can be effected by other matrix metalloproteinases, such as MMP2, MMP3 and MMP14 and may involve several cleavage steps. Cleavage can also be autocatalytic, after partial maturation by another protease or after treatment with 4-aminophenylmercuric acetate (APMA) (in vitro) (By similarity). {ECO:0000250}.; PTM: N-glycosylated. {ECO:0000250}.; PTM: Tyrosine phosphorylated by PKDCC/VLK. {ECO:0000250|UniProtKB:P45452}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000305}. Secreted. DOMAIN: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme (By similarity). {ECO:0000250}.; DOMAIN: The C-terminal region binds to collagen. {ECO:0000250}. TISSUE SPECIFICITY: Detected in epidermal cells and stromal fibroblasts in wounded skin, but not in normal skin (at protein level). Detected in embryonic hypertrophic chondrocytes and newly recruited bone cells at primary ossification centers. After adult bone fracture, detected in periosteum and in chondrocytes in the cartilage. Detected in immature and mature osteoblasts in the fracture callus. Detected in calvaria from neonates. Detected in wounded skin, but not in normal skin. {ECO:0000269|PubMed:15563592, ECO:0000269|PubMed:17987127, ECO:0000269|PubMed:19590036}. +O54732 MMP15_MOUSE Matrix metalloproteinase-15 (MMP-15) (EC 3.4.24.-) (Membrane-type matrix metalloproteinase 2) (MT-MMP 2) (MTMMP2) (Membrane-type-2 matrix metalloproteinase) (MT2-MMP) (MT2MMP) 657 74,666 Active site (1); Chain (1); Compositional bias (1); Disulfide bond (1); Glycosylation (2); Metal binding (4); Motif (1); Propeptide (1); Repeat (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 615 635 Helical. {ECO:0000255}. TOPO_DOM 128 614 Extracellular. {ECO:0000255}.; TOPO_DOM 636 657 Cytoplasmic. {ECO:0000255}. FUNCTION: Endopeptidase that degrades various components of the extracellular matrix. May activate progelatinase A. PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}; Extracellular side {ECO:0000305}. DOMAIN: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme. +Q9EPL6 MMP1B_MOUSE Interstitial collagenase B (EC 3.4.24.7) (Matrix metalloproteinase-1b) (MMP-1b) (Mcol-B) 463 53,492 Active site (1); Chain (1); Disulfide bond (1); Glycosylation (1); Metal binding (17); Motif (1); Propeptide (1); Region (1); Repeat (4); Signal peptide (1) SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000305}. DOMAIN: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme. +Q8K3F2 MMP21_MOUSE Matrix metalloproteinase-21 (MMP-21) (EC 3.4.24.-) 568 65,454 Active site (1); Chain (1); Disulfide bond (1); Glycosylation (1); Metal binding (4); Motif (1); Mutagenesis (3); Propeptide (1); Repeat (4); Signal peptide (1) FUNCTION: Plays a specialized role in the generation of left-right asymmetry during embryogenesis (PubMed:26437028). May act as a negative regulator of the NOTCH-signaling pathway. Cleaves alpha-1-antitrypsin (By similarity). {ECO:0000250|UniProtKB:Q8N119, ECO:0000269|PubMed:26437028, ECO:0000269|PubMed:26437029}. PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. DOMAIN: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme. +Q9R0S2 MMP24_MOUSE Matrix metalloproteinase-24 (MMP-24) (EC 3.4.24.-) (Matrix metalloproteinase-21) (MMP-21) (Membrane-type matrix metalloproteinase 5) (MT-MMP 5) (MTMMP5) (Membrane-type-5 matrix metalloproteinase) (MT5-MMP) (MT5MMP) [Cleaved into: Processed matrix metalloproteinase-24] 618 70,460 Active site (1); Chain (2); Compositional bias (1); Disulfide bond (1); Metal binding (4); Motif (2); Mutagenesis (3); Propeptide (1); Repeat (4); Sequence conflict (9); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 576 596 Helical. {ECO:0000255}. TOPO_DOM 42 575 Extracellular. {ECO:0000255}.; TOPO_DOM 597 618 Cytoplasmic. {ECO:0000255}. FUNCTION: Metalloprotease that mediates cleavage of N-cadherin (CDH2) and acts as a regulator of neuro-immune interactions and neural stem cell quiescence (PubMed:19805319, PubMed:24952463). Involved in cell-cell interactions between nociceptive neurites and mast cells, possibly by mediating cleavage of CDH2, thereby acting as a mediator of peripheral thermal nociception and inflammatory hyperalgesia (PubMed:19805319). Key regulator of neural stem cells quiescence by mediating cleavage of CDH2, affecting CDH2-mediated anchorage of neural stem cells to ependymocytes in the adult subependymal zone, leading to modulate their quiescence (PubMed:24952463). May play a role in axonal growth (PubMed:11714638). Able to activate progelatinase A. May also be a proteoglycanase involved in degradation of proteoglycans, such as dermatan sulfate and chondroitin sulfate proteoglycans. Cleaves partially fibronectin, but not collagen type I, nor laminin (PubMed:10622708). {ECO:0000269|PubMed:10622708, ECO:0000269|PubMed:11714638, ECO:0000269|PubMed:19805319, ECO:0000269|PubMed:24952463}. PTM: Cleaved by a furin endopeptidase in the trans-Golgi network. SUBCELLULAR LOCATION: Matrix metalloproteinase-24: Cell membrane; Single-pass type I membrane protein. Golgi apparatus, trans-Golgi network membrane; Single-pass type I membrane protein. Note=Recycled back to the plasma membrane through the trans-Golgi network via interaction with APBA3. {ECO:0000269|PubMed:14990567}.; SUBCELLULAR LOCATION: Processed matrix metalloproteinase-24: Secreted, extracellular space, extracellular matrix. Note=Also shed from cell surface as soluble proteinase, by a proteolytic cleavage. {ECO:0000269|PubMed:11470782}. SUBUNIT: Interacts with GRIP1 and GRIP2 (By similarity). Interacts (via PDZ-binding motif) with APBA3 (via PDZ domain). {ECO:0000250, ECO:0000269|PubMed:14990567}. DOMAIN: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.; DOMAIN: The PDZ-binding motif (also named EWV motif) is required for interaction with PDZ domains of APBA3 and recycling through the trans-Golgi network. {ECO:0000269|PubMed:14990567}. TISSUE SPECIFICITY: Mainly expressed in neuronal cells of both central and peripheral nervous systems. Expressed by CGRP-containing peptidergic nociceptors in dorsal root ganglia (PubMed:19805319). Expressed in adult neural stem cell and ependymocytes (PubMed:24952463). Expressed at low level in testis. {ECO:0000269|PubMed:11714638, ECO:0000269|PubMed:19805319, ECO:0000269|PubMed:24952463}. +Q3U435 MMP25_MOUSE Matrix metalloproteinase-25 (MMP-25) (EC 3.4.24.-) 615 68,496 Active site (1); Chain (1); Compositional bias (2); Disulfide bond (1); Lipidation (1); Metal binding (4); Motif (1); Propeptide (2); Repeat (4); Transmembrane (1) TRANSMEM 53 73 Helical. {ECO:0000255}. FUNCTION: May activate progelatinase A. {ECO:0000250}. PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}. DOMAIN: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme. +P33434 MMP2_MOUSE 72 kDa type IV collagenase (EC 3.4.24.24) (72 kDa gelatinase) (Gelatinase A) (Matrix metalloproteinase-2) (MMP-2) [Cleaved into: PEX] 662 74,102 Active site (1); Alternative sequence (1); Chain (2); Disulfide bond (7); Domain (3); Glycosylation (2); Metal binding (22); Motif (1); Propeptide (1); Region (4); Repeat (4); Signal peptide (1) FUNCTION: Ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. As well as degrading extracellular matrix proteins, can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. Also cleaves KISS at a Gly-|-Leu bond. Appears to have a role in myocardial cell death pathways. Contributes to myocardial oxidative stress by regulating the activity of GSK3beta. Cleaves GSK3beta in vitro. Involved in the formation of the fibrovascular tissues (By similarity). {ECO:0000250}.; FUNCTION: PEX, the C-terminal non-catalytic fragment of MMP2, posseses anti-angiogenic and anti-tumor properties and inhibits cell migration and cell adhesion to FGF2 and vitronectin. Ligand for integrin alpha-v/beta-3 on the surface of blood vessels (By similarity). {ECO:0000250}.; FUNCTION: Isoform 2: Mediates the proteolysis of CHUK/IKKA and initiates a primary innate immune response by inducing mitochondrial-nuclear stress signaling with activation of the pro-inflammatory NF-kappaB, NFAT and IRF transcriptional pathways. {ECO:0000269|PubMed:22509276}. PTM: Phosphorylation on multiple sites modulates enzymatic activity. Phosphorylated by PKC in vitro (By similarity). {ECO:0000250}.; PTM: The propeptide is processed by MMP14 (MT-MMP1) and MMP16 (MT-MMP3) (By similarity). Autocatalytic cleavage in the C-terminal produces the anti-angiogenic peptide, PEX. This processing appears to be facilitated by binding integrinv/beta3 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Isoform 1: Secreted, extracellular space, extracellular matrix {ECO:0000250}. Membrane {ECO:0000250}. Nucleus {ECO:0000250}. Note=Colocalizes with integrin alphaV/beta3 at the membrane surface in angiogenic blood vessels and melanomas. Found in mitochondria, along microfibrils, and in nuclei of cardiomyocytes (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Mitochondrion. SUBUNIT: Interacts (via the C-terminal hemopexin-like domains-containing region) with the integrin alpha-V/beta-3; the interaction promotes vascular invasion in angiogenic vessels and melamoma cells. Interacts (via the C-terminal PEX domain) with TIMP2 (via the C-terminal); the interaction inhibits the degradation activity. Interacts with GSK3B (By similarity). {ECO:0000250}. DOMAIN: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme. +P28862 MMP3_MOUSE Stromelysin-1 (SL-1) (EC 3.4.24.17) (EMS-2) (Matrix metalloproteinase-3) (MMP-3) (Transin-1) 477 53,845 Active site (1); Chain (1); Disulfide bond (1); Erroneous initiation (1); Metal binding (24); Motif (1); Propeptide (1); Repeat (4); Sequence conflict (1); Signal peptide (1) FUNCTION: Can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates procollagenase. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000305}. DOMAIN: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme. +Q10738 MMP7_MOUSE Matrilysin (EC 3.4.24.23) (Matrin) (Matrix metalloproteinase-7) (MMP-7) (Pump-1 protease) (Uterine metalloproteinase) 264 29,755 Active site (1); Chain (1); Metal binding (18); Motif (1); Propeptide (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Degrades casein, gelatins of types I, III, IV, and V, and fibronectin. Activates procollagenase (By similarity). {ECO:0000250}.; FUNCTION: May play a role in tissue reorganization. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000305}. DOMAIN: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme. +O70138 MMP8_MOUSE Neutrophil collagenase (EC 3.4.24.34) (Collagenase 2) (Matrix metalloproteinase-8) (MMP-8) 465 53,126 Active site (1); Chain (1); Disulfide bond (1); Glycosylation (2); Metal binding (21); Motif (1); Propeptide (1); Repeat (4); Sequence conflict (4); Signal peptide (1) FUNCTION: Can degrade fibrillar type I, II, and III collagens. May play a role in the degradation of collagen fibers during uterine involution. SUBCELLULAR LOCATION: Cytoplasmic granule. Secreted, extracellular space, extracellular matrix. Note=Stored in intracellular granules and released during inflammatory conditions. DOMAIN: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme. TISSUE SPECIFICITY: Neutrophils. Expressed in uterus. Low levels in kidney and muscle. +Q9EP89 LACTB_MOUSE Serine beta-lactamase-like protein LACTB, mitochondrial (EC 3.4.-.-) 551 60,705 Active site (1); Chain (1); Modified residue (4); Transit peptide (1) FUNCTION: Mitochondrial serine protease that acts as a regulator of mitochondrial lipid metabolism (By similarity). Acts by decreasing protein levels of PISD, a mitochondrial enzyme that converts phosphatidylserine (PtdSer) to phosphatidylethanolamine (PtdEtn), thereby affecting mitochondrial lipid metabolism (By similarity). It is unclear whether it acts directly by mediating proteolysis of PISD or by mediating proteolysis of another lipid metabolism protein (By similarity). Acts as a tumor suppressor that has the ability to inhibit proliferation of multiple types of cancer cells: probably by promoting decreased levels of PISD, thereby affecting mitochondrial lipid metabolism (PubMed:28329758). {ECO:0000250|UniProtKB:P83111, ECO:0000269|PubMed:28329758}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P83111}. TISSUE SPECIFICITY: Expressed predominantly in liver. {ECO:0000269|PubMed:11707067}. +P57016 LAD1_MOUSE Ladinin-1 (Lad-1) (Linear IgA disease antigen homolog) (LADA) 528 58,864 Chain (1); Compositional bias (1); Modified residue (11); Region (1); Repeat (6) FUNCTION: Anchoring filament protein which is a component of the basement membrane zone. {ECO:0000269|PubMed:9119369}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000269|PubMed:9119369}. TISSUE SPECIFICITY: Expressed in kidney, lung and keratinocytes followed by liver, spleen and brain. Not expressed in testis, skeletal and heart muscle and in fibroblasts. {ECO:0000269|PubMed:9119369}. +B2RPV6 MMRN1_MOUSE Multimerin-1 1210 136,106 Alternative sequence (1); Chain (1); Coiled coil (3); Disulfide bond (6); Domain (3); Glycosylation (16); Sequence conflict (6); Signal peptide (1) FUNCTION: Carrier protein for platelet (but not plasma) factor V/Va. Plays a role in the storage and stabilization of factor V in platelets. Upon release following platelet activation, may limit platelet and plasma factor Va-dependent thrombin generation. Ligand for integrin alpha-IIb/beta-3 and integrin alpha-V/beta-3 on activated platelets, and may function as an extracellular matrix or adhesive protein (By similarity). {ECO:0000250|UniProtKB:Q13201}. PTM: Extensively N-glycosylated. {ECO:0000250|UniProtKB:Q13201}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. SUBUNIT: Multimeric. Composed of varying sized, disulfide-linked multimers, the smallest of which is a homotrimer. Proteolysis of the promultimerin in the N-terminal region, leads to the mature p155 form that is stored in platelets. Interacts with factor V/Va (By similarity). {ECO:0000250|UniProtKB:Q13201}. +Q61790 LAG3_MOUSE Lymphocyte activation gene 3 protein (LAG-3) (CD antigen CD223) 521 56,978 Chain (1); Disulfide bond (4); Domain (4); Glycosylation (5); Region (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 443 463 Helical. {ECO:0000255}. TOPO_DOM 23 442 Extracellular. {ECO:0000255}.; TOPO_DOM 464 521 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in lymphocyte activation. Binds to HLA class-II antigens (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. +Q9CR70 LAGE3_MOUSE EKC/KEOPS complex subunit Lage3 (ITBA2 protein homolog) (L antigen family member 3) 148 15,824 Chain (1) FUNCTION: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. LAGE3 functions as a dimerization module for the complex. {ECO:0000250|UniProtKB:Q14657}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14657}. Nucleus {ECO:0000250|UniProtKB:Q14657}. SUBUNIT: Component of the EKC/KEOPS complex composed of at least GON7, TP53RK, TPRKB, OSGEP and LAGE3; the whole complex dimerizes. {ECO:0000250|UniProtKB:Q14657}. +B1AUR6 MMS22_MOUSE Protein MMS22-like (Methyl methanesulfonate-sensitivity protein 22-like) 1238 140,582 Alternative sequence (2); Chain (1); Erroneous initiation (2) FUNCTION: Component of the MMS22L-TONSL complex, a complex that stimulates the recombination-dependent repair of stalled or collapsed replication forks. The MMS22L-TONSL complex is required to maintain genome integrity during DNA replication by promoting homologous recombination-mediated repair of replication fork-associated double-strand breaks. It may act by mediating the assembly of RAD51 filaments on ssDNA (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Localizes to DNA damage sites, accumulates at stressed replication forks. {ECO:0000250}. SUBUNIT: Component of the MMS22L-TONSL complex, a complex at least composed of MMS22L and TONSL/NFKBIL2. {ECO:0000250}. +Q9EQ20 MMSA_MOUSE Methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial (MMSDH) (Malonate-semialdehyde dehydrogenase [acylating]) (EC 1.2.1.18) (EC 1.2.1.27) (Aldehyde dehydrogenase family 6 member A1) 535 57,916 Active site (1); Binding site (1); Chain (1); Modified residue (25); Nucleotide binding (2); Sequence conflict (3); Transit peptide (1) FUNCTION: Plays a role in valine and pyrimidine metabolism. Binds fatty acyl-CoA (By similarity). {ECO:0000250}. PTM: Acetylation of Lys-55; Lys-117 and Lys-331 is observed in liver mitochondria from fasted mice but not from fed mice. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. SUBUNIT: Homotetramer. {ECO:0000250}. +Q60675 LAMA2_MOUSE Laminin subunit alpha-2 (Laminin M chain) (Laminin-12 subunit alpha) (Laminin-2 subunit alpha) (Laminin-4 subunit alpha) (Merosin heavy chain) 3118 343,815 Beta strand (71); Chain (1); Coiled coil (2); Disulfide bond (68); Domain (27); Frameshift (1); Glycosylation (29); Helix (4); Region (1); Sequence conflict (27); Signal peptide (1); Turn (2) FUNCTION: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane. Note=Major component. SUBUNIT: Laminin is a complex glycoprotein, consisting of three different polypeptide chains (alpha, beta, gamma), which are bound to each other by disulfide bonds into a cross-shaped molecule comprising one long and three short arms with globules at each end. Alpha-2 is a subunit of laminin-2 (laminin-211 or merosin), laminin-4 (laminin-221 or S-merosin) and laminin-12 (laminin-213). Interacts with FBLN1, FBLN2 and NID2. {ECO:0000269|PubMed:10022829}. DOMAIN: The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure.; DOMAIN: Domains VI, IV and G are globular. DISEASE: Note=Defects in Lama2 are a cause of murine muscular dystrophy (dy2J). +Q61789 LAMA3_MOUSE Laminin subunit alpha-3 (Epiligrin subunit alpha) (Kalinin subunit alpha) (Laminin-5 subunit alpha) (Laminin-6 subunit alpha) (Laminin-7 subunit alpha) (Nicein subunit alpha) 3330 366,227 Alternative sequence (2); Chain (1); Coiled coil (5); Disulfide bond (54); Domain (23); Frameshift (1); Glycosylation (13); Motif (1); Region (5); Sequence conflict (29); Signal peptide (1) FUNCTION: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components.; FUNCTION: Laminin-5 is thought to be involved in (1) cell adhesion via integrin alpha-3/beta-1 in focal adhesion and integrin alpha-6/beta-4 in hemidesmosomes, (2) signal transduction via tyrosine phosphorylation of pp125-FAK and p80, (3) differentiation of keratinocytes. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane. Note=Major component. SUBUNIT: Laminin is a complex glycoprotein, consisting of three different polypeptide chains (alpha, beta, gamma), which are bound to each other by disulfide bonds into a cross-shaped molecule comprising one long and three short arms with globules at each end. Alpha-3 is a subunit of laminin-5 (laminin-332 or epiligrin/kalinin/nicein), laminin-6 (laminin-311 or K-laminin) and laminin-7 (laminin-321 or KS-laminin). DOMAIN: The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure.; DOMAIN: Domains IV and G are globular. TISSUE SPECIFICITY: Basal membrane of the upper alimentary tract and urinary and nasal epithelia, salivary glands and teeth (both variants). Isoform A is predominantly expressed in skin, hair follicles and developing neurons of the trigeminal ganglion. Isoform B was found in bronchi, alveoli, stomach, intestinal crypts, whisker pads, CNS, telencephalic neuroectoderm, thalamus, Rathke pouch and periventricular subependymal germinal layer. +P02469 LAMB1_MOUSE Laminin subunit beta-1 (Laminin B1 chain) (Laminin-1 subunit beta) (Laminin-10 subunit beta) (Laminin-12 subunit beta) (Laminin-2 subunit beta) (Laminin-6 subunit beta) (Laminin-8 subunit beta) 1786 197,090 Beta strand (21); Chain (1); Coiled coil (3); Disulfide bond (54); Domain (15); Erroneous initiation (1); Glycosylation (12); Helix (9); Modified residue (3); Region (3); Sequence conflict (8); Signal peptide (1); Turn (8) FUNCTION: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Involved in the organization of the laminar architecture of the cerebral cortex (By similarity). It is probably required for the integrity of the basement membrane/glia limitans that serves as an anchor point for the endfeet of radial glial cells and as a physical barrier to migrating neurons (By similarity). Radial glial cells play a central role in cerebral cortical development, where they act both as the proliferative unit of the cerebral cortex and a scaffold for neurons migrating toward the pial surface (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane. Note=Major component. SUBUNIT: Laminin is a complex glycoprotein, consisting of three different polypeptide chains (alpha, beta, gamma), which are bound to each other by disulfide bonds into a cross-shaped molecule comprising one long and three short arms with globules at each end. Beta-1 is a subunit of laminin-1 (laminin-111 or EHS laminin), laminin-2 (laminin-211 or merosin), laminin-6 (laminin-311 or K-laminin), laminin-8 (laminin-411), laminin-10 (laminin-511) and laminin-12 (laminin-213). TISSUE SPECIFICITY: Widely expressed in the embryo. High levels are detected in the cerebellar basement membrane, at postnatal day 7. {ECO:0000269|PubMed:23472759}. +Q8C4X7 MNARL_MOUSE Major intrinsically disordered NOTCH2-binding receptor 1-like homolog (Membrane integral NOTCH2-associated receptor 2) 193 21,854 Alternative sequence (1); Chain (1); Modified residue (1); Sequence conflict (1); Transmembrane (1) TRANSMEM 172 192 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q61087 LAMB3_MOUSE Laminin subunit beta-3 (Epiligrin subunit bata) (Kalinin B1 chain) (Kalinin subunit beta) (Laminin-5 subunit beta) (Nicein subunit beta) 1168 128,900 Chain (1); Coiled coil (3); Disulfide bond (27); Domain (7); Glycosylation (3); Region (3); Sequence conflict (12); Signal peptide (1) FUNCTION: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane. SUBUNIT: Laminin is a complex glycoprotein, consisting of three different polypeptide chains (alpha, beta, gamma), which are bound to each other by disulfide bonds into a cross-shaped molecule comprising one long and three short arms with globules at each end. Beta-3 is a subunit of laminin-5 (laminin-332 or epiligrin/kalinin/nicein). Interacts with ECM1 (By similarity). {ECO:0000250}. DOMAIN: The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure.; DOMAIN: Domain VI is globular. TISSUE SPECIFICITY: Found in the basement membranes (major component). +P02468 LAMC1_MOUSE Laminin subunit gamma-1 (Laminin B2 chain) (Laminin-1 subunit gamma) (Laminin-10 subunit gamma) (Laminin-11 subunit gamma) (Laminin-2 subunit gamma) (Laminin-3 subunit gamma) (Laminin-4 subunit gamma) (Laminin-6 subunit gamma) (Laminin-7 subunit gamma) (Laminin-8 subunit gamma) (Laminin-9 subunit gamma) (S-laminin subunit gamma) (S-LAM gamma) 1607 177,298 Beta strand (33); Chain (1); Coiled coil (1); Disulfide bond (42); Domain (14); Glycosylation (14); Helix (13); Modified residue (2); Region (1); Sequence conflict (11); Signal peptide (1); Turn (8) FUNCTION: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane. SUBUNIT: Laminin is a complex glycoprotein, consisting of three different polypeptide chains (alpha, beta, gamma), which are bound to each other by disulfide bonds into a cross-shaped molecule comprising one long and three short arms with globules at each end. Gamma-1 is a subunit of laminin-1 (laminin-111 or EHS laminin), laminin-2 (laminin-211 or merosin), laminin-3 (laminin-121 or S-laminin), laminin-4 (laminin-221 or S-merosin), laminin-6 (laminin-311 or K-laminin), laminin-7 (laminin-321 or KS-laminin), laminin-8 (laminin-411), laminin-9 (laminin-421), laminin-10 (laminin-511) and laminin-11 (laminin-521). DOMAIN: The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure.; DOMAIN: Domains VI and IV are globular. TISSUE SPECIFICITY: Found in the basement membranes (major component). +Q7TST5 LAMP3_MOUSE Lysosome-associated membrane glycoprotein 3 (LAMP-3) (Lysosomal-associated membrane protein 3) (DC-lysosome-associated membrane glycoprotein) (DC LAMP) (CD antigen CD208) 411 45,129 Chain (1); Disulfide bond (2); Glycosylation (1); Sequence conflict (7); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 377 397 Helical. {ECO:0000255|PROSITE-ProRule:PRU00740}. TOPO_DOM 22 376 Lumenal. {ECO:0000255}.; TOPO_DOM 398 411 Cytoplasmic. {ECO:0000255|PROSITE-ProRule:PRU00740}. FUNCTION: May play a role in dendritic cell function and in adaptive immunity. {ECO:0000250}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q9UQV4}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q9UQV4}; Single-pass type I membrane protein {ECO:0000255}. Note=During dendritic cell maturation, detected on cytoplasmic vesicles (the MHC II compartment) that contain MHC II proteins, LAMP1, LAMP2 and LAMP3. Detected on lysosomes in mature dendritic cells. {ECO:0000250|UniProtKB:Q9UQV4}. SUBUNIT: Monomer. {ECO:0000250}. +O89112 LANC1_MOUSE Glutathione S-transferase LANCL1 (EC 2.5.1.18) (40 kDa erythrocyte membrane protein) (p40) (LanC-like protein 1) 399 45,341 Binding site (1); Chain (1); Initiator methionine (1); Metal binding (3); Modified residue (2); Mutagenesis (1); Region (1) FUNCTION: Functions as glutathione transferase (PubMed:25158856). Catalyzes conjugation of the glutathione (GSH) to artificial substrates 1-chloro-2,4-dinitrobenzene (CDNB) and p-nitrophenyl acetate (PubMed:25158856). Mitigates neuronal oxidative stress during normal postnatal development and in response to oxidative stresses probably through GSH antioxidant defense mechanism (PubMed:25158856). May play a role in EPS8 signaling. Binds glutathione (By similarity). {ECO:0000250|UniProtKB:O43813, ECO:0000269|PubMed:25158856}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O43813}. Cell membrane {ECO:0000250|UniProtKB:O43813}; Peripheral membrane protein {ECO:0000250|UniProtKB:O43813}. SUBUNIT: Interacts with the C-terminal of STOM (By similarity). Interacts with the EPS8 SH3 domain. Interaction with EPS8 is inhibited by glutathione binding (By similarity). {ECO:0000250|UniProtKB:O43813}. TISSUE SPECIFICITY: Detected in spinal cord (at protein level). Ubiquitous. Strongly expressed in brain, testis, alveolar macrophages and epithelial cells of the lung, kidney and intestine (PubMed:17305318, PubMed:9714732). Expression in brain increases during the first postnatal month and remaining high in adult (PubMed:25158856). {ECO:0000269|PubMed:17305318, ECO:0000269|PubMed:25158856, ECO:0000269|PubMed:9714732}. +Q91XQ6 LAP4B_MOUSE Lysosomal-associated transmembrane protein 4B 227 25,395 Chain (1); Region (1); Transmembrane (4) TRANSMEM 26 46 Helical. {ECO:0000255}.; TRANSMEM 72 92 Helical. {ECO:0000255}.; TRANSMEM 100 120 Helical. {ECO:0000255}.; TRANSMEM 153 173 Helical. {ECO:0000255}. FUNCTION: Required for optimal lysosomal function. Blocks EGF-stimulated EGFR intraluminal sorting and degradation. Conversely by binding with the phosphatidylinositol 4,5-bisphosphate, regulates its PIP5K1C interaction, inhibits HGS ubiquitination and relieves LAPTM4B inhibition of EGFR degradation. Recruits SLC3A2 and SLC7A5 (the Leu transporter) to the lysosome, promoting entry of leucine and other essential amino acid (EAA) into the lysosome, stimulating activation of proton-transporting vacuolar (V)-ATPase protein pump (V-ATPase) and hence mTORC1 activation. Plays a role as negative regulator of TGFB1 production in regulatory T cells. Binds ceramide and facilitates its exit from late endosome in order to control cell death pathways. {ECO:0000250|UniProtKB:Q86VI4}. PTM: Undergoes proteolytic cleavage following delivery to the lysosomes. {ECO:0000250|UniProtKB:Q86VI4}.; PTM: Ubiquitinated by NEDD4. {ECO:0000250|UniProtKB:Q86VI4}. SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250|UniProtKB:Q86VI4}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q86VI4}. Late endosome membrane {ECO:0000250|UniProtKB:Q86VI4}. Cell membrane {ECO:0000250|UniProtKB:Q86VI4}. Cell projection {ECO:0000250|UniProtKB:Q86VI4}. Lysosome membrane {ECO:0000250|UniProtKB:Q86VI4}. Endosome membrane {ECO:0000250|UniProtKB:Q86VI4}. Endosome, multivesicular body membrane {ECO:0000250|UniProtKB:Q86VI4}. Endosome, multivesicular body lumen {ECO:0000250|UniProtKB:Q86VI4}. SUBUNIT: Homooligomer; upon reaching the lysosomes. Interacts with MCOLN1. Interacts with NEDD4; may play a role in the lysosomal sorting of LAPTM4B; enhances HGS association with NEDD4; mediates inhibition of EGFR degradation. Interacts with PIP5K1C; promotes SNX5 association with LAPTM4B; kinase activity of PIP5K1C is required; interaction is regulated by phosphatidylinositol 4,5-bisphosphate generated by PIP5K1C. Interacts with HGS; promotes HGS ubiquitination. Interacts with SNX5. Interacts with SLC3A2 AND SLC7A5; recruits SLC3A2 and SLC7A5 to lysosomes to promote leucine uptake into these organelles and is required for mTORC1 activation. Interacts with LRRC32; decreases TGFB1 production in regulatory T cells. Interacts with BECN1; competes with EGFR for LAPTM4B binding; regulates EGFR activity. Interacts with EGFR; positively correlates with EGFR activation. {ECO:0000250|UniProtKB:Q86VI4}. +Q6A0A2 LAR4B_MOUSE La-related protein 4B (La ribonucleoprotein domain family member 4B) (La ribonucleoprotein domain family member 5) (La-related protein 5) 741 81,627 Alternative sequence (2); Chain (1); Domain (2); Erroneous initiation (1); Modified residue (21); Sequence conflict (3) FUNCTION: Stimulates mRNA translation. {ECO:0000250|UniProtKB:Q92615}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q92615}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs in response to arsenite treatment. {ECO:0000250|UniProtKB:Q92615}. SUBUNIT: Interacts with PABPC1. Interacts with RACK1. Associates with polysomes via the 40S ribosomal subunit. {ECO:0000250|UniProtKB:Q92615}. +Q61168 LAPM5_MOUSE Lysosomal-associated transmembrane protein 5 (Lysosomal-associated multitransmembrane protein 5) (Retinoic acid-inducible E3 protein) 261 29,602 Chain (1); Compositional bias (1); Modified residue (1); Sequence conflict (3); Transmembrane (5) TRANSMEM 21 41 Helical. {ECO:0000255}.; TRANSMEM 65 85 Helical. {ECO:0000255}.; TRANSMEM 92 112 Helical. {ECO:0000255}.; TRANSMEM 133 153 Helical. {ECO:0000255}.; TRANSMEM 183 203 Helical. {ECO:0000255}. FUNCTION: May have a special functional role during embryogenesis and in adult hematopoietic cells. {ECO:0000269|PubMed:8661146}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:8661146}; Multi-pass membrane protein {ECO:0000269|PubMed:8661146}. SUBUNIT: Binds to ubiquitin. TISSUE SPECIFICITY: Preferentially expressed in adult hematopoietic tissues. High levels in lymphoid and myeloid tissues. {ECO:0000269|PubMed:8661146}. +A2BE28 LAS1L_MOUSE Ribosomal biogenesis protein LAS1L (Protein LAS1 homolog) 776 89,414 Alternative sequence (1); Chain (1); Modified residue (3) FUNCTION: Involved in the biogenesis of the 60S ribosomal subunit. Required for maturation of the 28S rRNA (By similarity). Functions as a component of the Five Friends of Methylated CHTOP (5FMC) complex; the 5FMC complex is recruited to ZNF148 by methylated CHTOP, leading to desumoylation of ZNF148 and subsequent transactivation of ZNF148 target genes. {ECO:0000250, ECO:0000269|PubMed:22872859}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000269|PubMed:22872859}. Cytoplasm {ECO:0000269|PubMed:22872859}. Note=Localizes mainly to the granular component, the region implicated in the later steps of rRNA processing and subunit assembly and export (By similarity). Mainly found in the nucleoplasm, with low levels detected in the cytoplasmic and chromatin fractions. {ECO:0000250}. SUBUNIT: Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10 (By similarity). Component of the 5FMC complex, at least composed of PELP1, LAS1L, TEX10, WDR18 and SENP3; the complex interacts with methylated CHTOP and ZNF148. {ECO:0000250, ECO:0000269|PubMed:22872859}. +Q61792 LASP1_MOUSE LIM and SH3 domain protein 1 (LASP-1) (Metastatic lymph node gene 50 protein) (MLN 50) 263 29,994 Chain (1); Compositional bias (2); Domain (2); Modified residue (10); Repeat (2) FUNCTION: Plays an important role in the regulation of dynamic actin-based, cytoskeletal activities. Agonist-dependent changes in LASP1 phosphorylation may also serve to regulate actin-associated ion transport activities, not only in the parietal cell but also in certain other F-actin-rich secretory epithelial cell types (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Associated with the F-actin rich cortical cytoskeleton. {ECO:0000250}. SUBUNIT: Interacts with F-actin. Interacts with KBTBD10 (By similarity). Interacts with ANKRD54. {ECO:0000250, ECO:0000269|PubMed:19064729}. +Q7TSJ6 LATS2_MOUSE Serine/threonine-protein kinase LATS2 (EC 2.7.11.1) (Kinase phosphorylated during mitosis protein) (Large tumor suppressor homolog 2) (Serine/threonine-protein kinase kpm) 1042 115,472 Active site (1); Binding site (1); Chain (1); Domain (3); Frameshift (1); Helix (3); Modified residue (5); Motif (1); Nucleotide binding (1); Sequence conflict (4) FUNCTION: Negative regulator of YAP1 in the Hippo signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. Acts as a tumor suppressor which plays a critical role in centrosome duplication, maintenance of mitotic fidelity and genomic stability. Negatively regulates G1/S transition by down-regulating cyclin E/CDK2 kinase activity. Negative regulator of the androgen receptor. Phosphorylates SNAI1 in the nucleus leading to its nuclear retention and stabilization, which enhances its epithelial-mesenchymal transition and tumor cell invasion/migration activities. This tumor-promoting activity is independent of its effects upon YAP1 or WWTR1/TAZ (By similarity). {ECO:0000250, ECO:0000269|PubMed:15343267}. PTM: Autophosphorylated and phosphorylated during M-phase and the G1/S-phase of the cell cycle. Phosphorylated and activated by STK3/MST2 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:15343267}. Cytoplasm {ECO:0000269|PubMed:15343267}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:15343267}. Nucleus {ECO:0000250}. Note=Colocalizes with AURKA at the centrosomes during interphase, early prophase and cytokinesis (By similarity). Migrates to the spindle poles during mitosis, and to the midbody during cytokinesis. Translocates to the nucleus upon mitotic stress by nocodazole treatment (By similarity). {ECO:0000250}. SUBUNIT: Interacts with and is phosphorylated by AURKA. Binds to AR (By similarity). Interacts with AJUBA during mitosis and this complex regulates organization of the spindle apparatus through recruitment of gamma-tubulin to the centrosome. Interacts (via PPxY motif) with YAP1 (via WW domains). Interacts with MOB1A and MOB1B (By similarity). Interacts with LIMD1, WTIP and AJUBA (By similarity). Interacts with SNAI1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed at high levels in ovary and testis and at lower levels in all other tissues examined. {ECO:0000269|PubMed:10673337}. +Q8C351 LAYN_MOUSE Layilin 381 43,269 Alternative sequence (2); Beta strand (1); Chain (1); Disulfide bond (2); Domain (1); Glycosylation (1); Modified residue (2); Region (4); Repeat (5); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 236 256 Helical. {ECO:0000255}. TOPO_DOM 25 235 Extracellular. {ECO:0000255}.; TOPO_DOM 257 381 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for hyaluronate. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Colocalizes with TLN1 at the membrane ruffles. {ECO:0000250}. SUBUNIT: Interacts with TLN1 (By similarity). Interacts with NF2 and RDX. {ECO:0000250, ECO:0000269|PubMed:15913605}. DOMAIN: The C-terminal domain interacts with the N-terminal domain of RDX. +O54957 LAT_MOUSE Linker for activation of T-cells family member 1 (36 kDa phospho-tyrosine adapter protein) (pp36) (p36-38) 242 26,015 Chain (1); Lipidation (2); Modified residue (12); Region (3); Topological domain (2); Transmembrane (1) TRANSMEM 5 28 Helical; Signal-anchor for type III membrane protein. {ECO:0000255}. TOPO_DOM 1 4 Extracellular. {ECO:0000255}.; TOPO_DOM 29 242 Cytoplasmic. {ECO:0000255}. FUNCTION: Required for TCR (T-cell antigen receptor)- and pre-TCR-mediated signaling, both in mature T-cells and during their development. Involved in FCGR3 (low affinity immunoglobulin gamma Fc region receptor III)-mediated signaling in natural killer cells and FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Couples activation of these receptors and their associated kinases with distal intracellular events such as mobilization of intracellular calcium stores, PKC activation, MAPK activation or cytoskeletal reorganization through the recruitment of PLCG1, GRB2, GRAP2, and other signaling molecules. {ECO:0000269|PubMed:10843385}. PTM: Phosphorylated on tyrosines by ZAP70 upon TCR activation, or by SYK upon other immunoreceptor activation; which leads to the recruitment of multiple signaling molecules. Is one of the most prominently tyrosine-phosphorylated proteins detected following TCR engagement. May be dephosphorylated by PTPRJ. Phosphorylated by ITK leading to the recruitment of VAV1 to LAT-containing complexes (By similarity). {ECO:0000250}.; PTM: Palmitoylation of Cys-27 and Cys-30 is required for raft targeting and efficient phosphorylation. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type III membrane protein. Note=Present in lipid rafts. SUBUNIT: When phosphorylated, interacts directly with the PIK3R1 subunit of phosphoinositide 3-kinase and the SH2 domains of GRB2, GRAP, GRAP2, PLCG1 and PLCG2. Interacts indirectly with CBL, SOS, VAV, and LCP2. Interacts with SHB and SKAP2. Interacts with FCGR1A (By similarity). Interacts with CLNK. Interacts with GRB2, PLCG1 and THEMIS upon TCR activation in thymocytes. {ECO:0000250, ECO:0000269|PubMed:11463797, ECO:0000269|PubMed:22561606}. TISSUE SPECIFICITY: Expressed in T-cells and mast cells. {ECO:0000269|PubMed:10843385}. +Q9Z127 LAT1_MOUSE Large neutral amino acids transporter small subunit 1 (4F2 light chain) (4F2 LC) (4F2LC) (L-type amino acid transporter 1) (Solute carrier family 7 member 5) 512 55,872 Chain (1); Glycosylation (2); Modified residue (1); Sequence conflict (3); Transmembrane (12) TRANSMEM 51 71 Helical. {ECO:0000255}.; TRANSMEM 85 105 Helical. {ECO:0000255}.; TRANSMEM 121 141 Helical. {ECO:0000255}.; TRANSMEM 147 167 Helical. {ECO:0000255}.; TRANSMEM 174 194 Helical. {ECO:0000255}.; TRANSMEM 200 220 Helical. {ECO:0000255}.; TRANSMEM 248 268 Helical. {ECO:0000255}.; TRANSMEM 279 299 Helical. {ECO:0000255}.; TRANSMEM 324 344 Helical. {ECO:0000255}.; TRANSMEM 398 418 Helical. {ECO:0000255}.; TRANSMEM 436 456 Helical. {ECO:0000255}.; TRANSMEM 463 483 Helical. {ECO:0000255}. FUNCTION: Sodium-independent, high-affinity transport of large neutral amino acids such as phenylalanine, tyrosine, leucine, arginine and tryptophan, when associated with SLC3A2/4F2hc. Involved in cellular amino acid uptake. Acts as an amino acid exchanger. Involved in the transport of L-DOPA across the blood-brain barrier, and that of thyroid hormones triiodothyronine (T3) and thyroxine (T4) across the cell membrane. Plays a role in neuronal cell proliferation (neurogenesis) in brain. Involved in the uptake of methylmercury (MeHg) when administered as the L-cysteine or D,L-homocysteine complexes, and hence plays a role in metal ion homeostasis and toxicity. Involved in the cellular activity of small molecular weight nitrosothiols, via the stereoselective transport of L-nitrosocysteine (L-CNSO) across the transmembrane. Mediates blood-to-retina L-leucine transport across the inner blood-retinal barrier which in turn may play a key role in maintaining large neutral amino acids as well as neurotransmitters in the neural retina. Acts as the major transporter of tyrosine in fibroblasts. When associated with LAPTM4B, recruits SLC3A2 and SLC7A5 to lysosomes to promote leucine uptake into these organelles and is required for mTORC1 activation (By similarity). {ECO:0000250|UniProtKB:Q01650, ECO:0000269|PubMed:11011012, ECO:0000269|PubMed:11117468, ECO:0000269|PubMed:9915839}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:9915839}. Apical cell membrane {ECO:0000269|PubMed:9915839}; Multi-pass membrane protein {ECO:0000269|PubMed:9915839}. Note=Located to the plasma membrane by SLC3A2/4F2hc. Expressed in both luminal and abluminal membranes of brain capillary endothelial cells (By similarity). Localized to the apical membrane of placental syncytiophoblastic cells (By similarity). {ECO:0000250}. SUBUNIT: Disulfide-linked heterodimer with the amino acid transport protein SLC3A2/4F2hc (PubMed:9915839). Interacts with LAPTM4B; recruits SLC3A2 and SLC7A5 to lysosomes to promote leucine uptake into these organelles and is required for mTORC1 activation (By similarity). {ECO:0000250|UniProtKB:Q01650, ECO:0000269|PubMed:9915839}. TISSUE SPECIFICITY: Predominantly expressed in the microvessels in the brain parenchyma of the central nervous system. Also detected in the subfornical organ, the subcommissural organ, ventromedial nucleus of the hypothalamus, subgranular zone of the dentate gyrus in hippocampus, ependymal layer of the lateral ventricles, and the olfactory bulb. Very strong expression also seen in testis, ovary, and placenta with weaker expression in spleen, skin, brain, thymus, stomach, lung, heart, kidney, small intestine, uterus and skeletal muscle. {ECO:0000269|PubMed:10574970, ECO:0000269|PubMed:11011012, ECO:0000269|PubMed:11117468, ECO:0000269|PubMed:9915839}. +Q8BHB3 LAX1_MOUSE Lymphocyte transmembrane adapter 1 (Linker for activation of X cells) (Membrane-associated adapter protein LAX) 407 44,838 Chain (1); Modified residue (4); Sequence conflict (7); Topological domain (2); Transmembrane (1) TRANSMEM 34 54 Helical; Signal-anchor for type III membrane protein. {ECO:0000255}. TOPO_DOM 1 33 Extracellular. {ECO:0000255}.; TOPO_DOM 55 407 Cytoplasmic. {ECO:0000255}. FUNCTION: Negatively regulates TCR (T-cell antigen receptor)-mediated signaling in T-cells and BCR (B-cell antigen receptor)-mediated signaling in B-cells. {ECO:0000269|PubMed:15843560}. PTM: Phosphorylated on tyrosines upon TCR or BCR activation; which leads to the recruitment of GRB2, PIK3R1 and GRAP2. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. SUBUNIT: When phosphorylated, interacts with GRB2, PIK3R1 and GRAP2. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in T-cells and B-cells. {ECO:0000269|PubMed:15843560}. +Q8C0X0 LCA5L_MOUSE Lebercilin-like protein (Leber congenital amaurosis 5-like protein) 730 81,290 Alternative sequence (2); Chain (1); Coiled coil (1); Frameshift (1); Sequence conflict (4) +Q9CX60 LBH_MOUSE Protein LBH (Limb bud and heart-expressed protein) 105 12,138 Chain (1); Domain (1); Modified residue (1); Sequence conflict (1) FUNCTION: Modulates the activity of key transcription factors involved in cardiogenesis. {ECO:0000269|PubMed:11336496, ECO:0000269|PubMed:15958514}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11336496}. Cytoplasm {ECO:0000250}. TISSUE SPECIFICITY: Expressed at highest levels in heart, and at lower levels in brain, spleen, lung, liver and kidney. {ECO:0000269|PubMed:11336496}. +P16301 LCAT_MOUSE Phosphatidylcholine-sterol acyltransferase (EC 2.3.1.43) (Lecithin-cholesterol acyltransferase) (Phospholipid-cholesterol acyltransferase) 438 49,747 Active site (3); Chain (1); Compositional bias (1); Disulfide bond (2); Glycosylation (5); Sequence conflict (1); Signal peptide (1); Site (1) FUNCTION: Central enzyme in the extracellular metabolism of plasma lipoproteins. Synthesized mainly in the liver and secreted into plasma where it converts cholesterol and phosphatidylcholines (lecithins) to cholesteryl esters and lysophosphatidylcholines on the surface of high and low density lipoproteins (HDLs and LDLs) (PubMed:19065001). The cholesterol ester is then transported back to the liver. Also produced in the brain by primary astrocytes, and esterifies free cholesterol on nascent APOE-containing lipoproteins secreted from glia and influences cerebral spinal fluid (CSF) APOE- and APOA1 levels (PubMed:19065001). Together with APOE and the cholesterol transporter ABCA1, plays a key role in the maturation of glial-derived, nascent lipoproteins (PubMed:19065001). Required for remodeling high-density lipoprotein particles into their spherical forms (PubMed:19065001). Has a preference for plasma 16:0-18:2 or 18:O-18:2 phosphatidylcholines (PubMed:8820107). {ECO:0000250|UniProtKB:P04180, ECO:0000269|PubMed:11809774, ECO:0000269|PubMed:11893779, ECO:0000269|PubMed:15654758, ECO:0000269|PubMed:19065001, ECO:0000269|PubMed:8820107}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19065001, ECO:0000269|PubMed:8820107}. Note=Secreted into blood plasma (PubMed:8820107). Produced in astrocytes and secreted into cerebral spinal fluid (CSF) (By similarity). {ECO:0000250, ECO:0000269|PubMed:8820107}. TISSUE SPECIFICITY: Detected in blood plasma (PubMed:8820107). Produced and secreted by astrocytes (at protein level) (PubMed:19065001). Abundantly expressed in liver, brain and testis with highest levels in liver. In the brain, found in cerebellum, cerebral cortex, hippocampus and brain stem. Located to neurons and neuroglia. {ECO:0000269|PubMed:19065001, ECO:0000269|PubMed:2600083}. +Q810Z1 LCN10_MOUSE Epididymal-specific lipocalin-10 182 20,652 Chain (1); Disulfide bond (1); Glycosylation (2); Modified residue (1); Signal peptide (1) FUNCTION: May play a role in male fertility. May act as a retinoid carrier protein within the epididymis. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. TISSUE SPECIFICITY: Expressed in epididymis. {ECO:0000269|PubMed:15363845}. +Q6JVL5 LCN12_MOUSE Epididymal-specific lipocalin-12 193 22,341 Chain (1); Disulfide bond (1); Glycosylation (2); Signal peptide (1) FUNCTION: Binds all-trans retinoic acid and may act as a retinoid carrier protein within the epididymis. May play a role in male fertility (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in epididymis. {ECO:0000269|PubMed:15363845}. +A2AJB7 LCN5_MOUSE Epididymal-specific lipocalin-5 (Epididymal retinoic acid-binding protein) (E-RABP) (mE-RABP) (Epididymal secretory protein 10) (MEP 10) [Cleaved into: Epididymal-specific lipocalin-5, major form; Epididymal-specific lipocalin-5, minor form] 192 21,013 Alternative sequence (3); Chain (2); Disulfide bond (1); Erroneous initiation (1); Signal peptide (1) FUNCTION: Associates with spermatozoa in the epididymal fluid but does not bind tightly to them. Binds both all-trans and 13-cis retinoic acid. May act as a retinoid carrier protein which is required for epididymal function and/or sperm maturation. {ECO:0000269|PubMed:1591332, ECO:0000269|PubMed:1591333}. PTM: 2 different forms with differently processed N-termini exist. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1591332, ECO:0000269|PubMed:2393684}. Note=Synthesized by the mid and distal caput of the epididymis and secreted into the epididymal lumen. {ECO:0000269|PubMed:1591332, ECO:0000269|PubMed:2393684}. TISSUE SPECIFICITY: Epididymal fluid of the caudal and corpus regions (at protein level). {ECO:0000269|PubMed:14595821}. +Q3U285 LCORL_MOUSE Ligand-dependent nuclear receptor corepressor-like protein (LCoR-like protein) (Mblk1-related protein 1) (Transcription factor MLR1) 600 66,695 Alternative sequence (7); Chain (1); Compositional bias (1); Cross-link (4); DNA binding (1); Domain (1); Sequence conflict (2) FUNCTION: May act as transcription activator that binds DNA elements with the sequence 5'-CCCTATCGATCGATCTCTACCT-3'. May play a role in spermatogenesis. {ECO:0000269|PubMed:12560079}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00320}. TISSUE SPECIFICITY: Expressed predominantly in the spermatocytes of the testis. Also found in the kidney, liver and heart. {ECO:0000269|PubMed:12560079}. +Q8BVA5 LDAH_MOUSE Lipid droplet-associated hydrolase (EC 3.1.1.-) (Lipid droplet-associated serine hydrolase) (mLDAH) 326 37,374 Active site (3); Alternative sequence (4); Chain (1); Mutagenesis (1); Sequence conflict (2) FUNCTION: Serine lipid hydrolase associated with lipid droplets. Highly expressed in macrophage-rich areas in atherosclerotic lesions, suggesting that it could promote cholesterol ester turnover in macrophages. {ECO:0000305|PubMed:24357060}. SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:23525007, ECO:0000269|PubMed:24357060}. Endoplasmic reticulum {ECO:0000269|PubMed:23525007}. Note=Localizes to the endoplasmic reticulum in absence of lipid droplets and translocates to lipid droplets upon lipid storage induction. {ECO:0000269|PubMed:23525007}. TISSUE SPECIFICITY: Highly expressed in macrophage-rich areas in atherosclerotic lesions. {ECO:0000269|PubMed:24357060}. +Q8K1F9 LCTL_MOUSE Lactase-like protein (Klotho/lactase-phlorizin hydrolase-related protein) 566 64,826 Alternative sequence (2); Chain (1); Erroneous initiation (1); Glycosylation (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 541 561 Helical. {ECO:0000255}. TOPO_DOM 21 540 Extracellular. {ECO:0000255}.; TOPO_DOM 562 566 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305|PubMed:12084582}; Single-pass membrane protein {ECO:0000305|PubMed:12084582}. TISSUE SPECIFICITY: Kidney and skin. {ECO:0000269|PubMed:12084582}. +P52189 KCNJ4_MOUSE Inward rectifier potassium channel 4 (Inward rectifier K(+) channel Kir2.3) (IRK-3) (Potassium channel, inwardly rectifying subfamily J member 4) 445 49,899 Chain (1); Compositional bias (3); Intramembrane (2); Motif (2); Mutagenesis (4); Sequence conflict (6); Site (1); Topological domain (4); Transmembrane (2) INTRAMEM 120 131 Helical; Pore-forming; Name=H5. {ECO:0000250}.; INTRAMEM 132 138 Pore-forming. {ECO:0000250}. TRANSMEM 56 80 Helical; Name=M1. {ECO:0000250}.; TRANSMEM 148 169 Helical; Name=M2. {ECO:0000250}. TOPO_DOM 1 55 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 81 119 Extracellular. {ECO:0000250}.; TOPO_DOM 139 147 Extracellular. {ECO:0000250}.; TOPO_DOM 170 445 Cytoplasmic. {ECO:0000250}. FUNCTION: Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by extracellular barium and cesium (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein. Cytoplasmic vesicle membrane. Note=TAX1BP3 binding promotes dissociation of KCNJ4 from LIN7 family members and KCNJ4 internalization. SUBUNIT: Homomultimeric and heteromultimeric association with KCNJ2 and KCNJ12. Association, via its PDZ-recognition domain, with LIN7A, LIN7B, LIN7C, DLG1, DLG2, DLG4, CASK and APBA1 plays a key role in its localization and trafficking (By similarity). Interacts with TAX1BP3. TAX1BP3 competes with LIN7 family members for KCNJ4 binding. {ECO:0000250, ECO:0000269|PubMed:11997254, ECO:0000269|PubMed:16855024}. TISSUE SPECIFICITY: Highly expressed in the forebrain, moderately in skeletal muscle. Im olfactory bulb, specifically expressed at the postsynaptic membrane of dendritic spines of granule cells. {ECO:0000269|PubMed:11997254}. +P16056 MET_MOUSE Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met) 1379 153,549 Active site (1); Binding site (1); Chain (1); Disulfide bond (10); Domain (5); Glycosylation (10); Modified residue (13); Nucleotide binding (1); Region (2); Sequence conflict (4); Signal peptide (1); Site (2); Topological domain (2); Transmembrane (1) TRANSMEM 932 954 Helical. {ECO:0000255}. TOPO_DOM 25 931 Extracellular. {ECO:0000255}.; TOPO_DOM 955 1379 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to hepatocyte growth factor/HGF ligand. Regulates many physiological processes including proliferation, scattering, morphogenesis and survival. Ligand binding at the cell surface induces autophosphorylation of MET on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with the PI3-kinase subunit PIK3R1, PLCG1, SRC, GRB2, STAT3 or the adapter GAB1. Recruitment of these downstream effectors by MET leads to the activation of several signaling cascades including the RAS-ERK, PI3 kinase-AKT, or PLCgamma-PKC. The RAS-ERK activation is associated with the morphogenetic effects while PI3K/AKT coordinates prosurvival effects. During embryonic development, MET signaling plays a role in gastrulation, development and migration of muscles and neuronal precursors, angiogenesis and kidney formation. In adults, participates in wound healing as well as organ regeneration and tissue remodeling. Promotes also differentiation and proliferation of hematopoietic cells (By similarity). May regulate cortical bone osteogenesis (PubMed:26637977). {ECO:0000250, ECO:0000269|PubMed:26637977, ECO:0000269|PubMed:7651534}. PTM: Autophosphorylated in response to ligand binding on Tyr-1232 and Tyr-1233 in the kinase domain leading to further phosphorylation of Tyr-1347 and Tyr-1354 in the C-terminal multifunctional docking site. Dephosphorylated by PTPRJ at Tyr-1347 and Tyr-1363 (By similarity). Dephosphorylated by PTPN1 and PTPN2 (By similarity). {ECO:0000250}.; PTM: Ubiquitinated. Ubiquitination by CBL regulates MET endocytosis, resulting in decreasing plasma membrane receptor abundance, and in endosomal degradation and/or recycling of internalized receptors. {ECO:0000250|UniProtKB:P08581}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Heterodimer made of an alpha chain (50 kDa) and a beta chain (145 kDa) which are disulfide linked (By similarity). Binds PLXNB1 (By similarity). Interacts when phosphorylated with downstream effectors including STAT3, PIK3R1, SRC, PCLG1, GRB2 and GAB1 (By similarity). When phosphorylated at Tyr-1354, interacts with INPPL1/SHIP2 (By similarity). Interacts with RANBP9 and RANBP10 (By similarity). Interacts with INPP5D/SHIP1 (PubMed:11896575). Interacts with SPSB1, SPSB2, SPSB4 and probably SPSB3. SPSB1 binding occurs in the presence and in the absence of HGF, however HGF treatment has a positive effect on this interaction (PubMed:16369487). Interacts with MUC20; prevents interaction with GRB2 and suppresses hepatocyte growth factor-induced cell proliferation (PubMed:15314156). Interacts with GRB10 (By similarity). Interacts with PTPN1 and PTPN2. Interacts with HSP90AA1 and HSP90AB1; the interaction suppresses MET kinase activity (By similarity). {ECO:0000250|UniProtKB:P08581, ECO:0000269|PubMed:11896575, ECO:0000269|PubMed:15314156, ECO:0000269|PubMed:16369487}. DOMAIN: The kinase domain is involved in SPSB1 binding. {ECO:0000250}.; DOMAIN: The beta-propeller Sema domain mediates binding to HGF. {ECO:0000250}. DISEASE: Note=Activation of Met after rearrangement with the TPR (translocated promoter) locus of chromosome 1 produces an oncogenic protein. +P21956 MFGM_MOUSE Lactadherin (MFGM) (Milk fat globule-EGF factor 8) (MFG-E8) (SED1) (Sperm surface protein SP47) (MP47) 463 51,241 Alternative sequence (1); Beta strand (13); Chain (1); Disulfide bond (9); Domain (4); Glycosylation (4); Motif (1); Sequence conflict (13); Signal peptide (1); Turn (1) FUNCTION: Contributes to phagocytic removal of apoptotic cells in many tissues. Specific ligand for the alpha-v/beta-3 and alpha-v/beta-5 receptors. Also binds to phosphatidylserine-enriched cell surfaces in a receptor-independent manner. Zona pellucida-binding protein which may play a role in gamete interaction (By similarity). Plays an important role in the maintenance of intestinal epithelial homeostasis and the promotion of mucosal healing. Promotes VEGF-dependent neovascularization. {ECO:0000250, ECO:0000269|PubMed:15834428, ECO:0000269|PubMed:18008006}. PTM: N-glycosylated. Isoform 1 also exists in both an O-glycosylated and a non-O-glycosylated form. {ECO:0000269|PubMed:9920772}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:2122462}; Peripheral membrane protein {ECO:0000269|PubMed:2122462}. Secreted {ECO:0000269|PubMed:2122462}. DOMAIN: The F5/8 type C 2 domain mediates high-affinity binding to phosphatidylserine-containing membranes. TISSUE SPECIFICITY: Mammary epithelial cell surfaces and spermatozoan. Isoform 2 is present in brain, heart, kidney and spleen and at low levels in lung, liver, small intestine and testis. {ECO:0000269|PubMed:2122462, ECO:0000269|PubMed:9920772}. +Q811U4 MFN1_MOUSE Mitofusin-1 (EC 3.6.5.-) (Transmembrane GTPase MFN1) 741 83,726 Binding site (2); Chain (1); Coiled coil (2); Domain (1); Erroneous initiation (2); Helix (1); Nucleotide binding (2); Region (8); Sequence conflict (9); Topological domain (3); Transmembrane (2) TRANSMEM 585 605 Helical; Name=1. {ECO:0000255}.; TRANSMEM 609 629 Helical; Name=2. {ECO:0000255}. TOPO_DOM 1 584 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 606 608 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 630 741 Cytoplasmic. {ECO:0000255}. FUNCTION: Mitochondrial outer membrane GTPase that mediates mitochondrial clustering and fusion (PubMed:12527753, PubMed:23921378, PubMed:24513856, PubMed:15297672). Membrane clustering requires GTPase activity (By similarity). It may involve a major rearrangement of the coiled coil domains (PubMed:15297672). Mitochondria are highly dynamic organelles, and their morphology is determined by the equilibrium between mitochondrial fusion and fission events (PubMed:12527753). Overexpression induces the formation of mitochondrial networks (in vitro). Has low GTPase activity (By similarity). {ECO:0000250|UniProtKB:Q8IWA4, ECO:0000269|PubMed:12527753, ECO:0000269|PubMed:15297672, ECO:0000269|PubMed:23921378, ECO:0000269|PubMed:24513856}. PTM: Ubiquitinated by MARCH5 (By similarity). When mitochondria are depolarized and dysfunctional, it is ubiquitinated by a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex that contains FBXO7 and PRKN. Ubiquitinated by non-degradative ubiquitin by PRKN, promoting mitochondrial fusion; deubiquitination by USP30 inhibits mitochondrial fusion (PubMed:24513856). {ECO:0000250|UniProtKB:Q8IWA4, ECO:0000269|PubMed:24513856}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:12759376}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Homodimer, also in the absence of bound GTP (By similarity). Forms higher oligomers in the presence of a transition state GTP analog (By similarity). Forms homomultimers and heteromultimers with MFN2 (PubMed:12527753). Oligomerization is essential for mitochondrion fusion (PubMed:15297672). Component of a high molecular weight multiprotein complex (By similarity). Interacts with VAT1 (By similarity). {ECO:0000250|UniProtKB:Q8IWA4, ECO:0000250|UniProtKB:Q8R4Z9, ECO:0000269|PubMed:12527753, ECO:0000269|PubMed:15297672}. DOMAIN: A helix bundle is formed by helices from the N-terminal and the C-terminal part of the protein. The GTPase domain cannot be expressed by itself, without the helix bundle. Rearrangement of the helix bundle and/or of the coiled coil domains may bring membranes from adjacent mitochondria into close contact, and thereby play a role in mitochondrial fusion. {ECO:0000250|UniProtKB:Q8IWA4}. TISSUE SPECIFICITY: Detected in adult heart (PubMed:12759376). Detected in embryos (at protein level) (PubMed:12527753). Widely expressed (PubMed:11950885). {ECO:0000269|PubMed:11950885, ECO:0000269|PubMed:12527753, ECO:0000269|PubMed:12759376}. +Q9CWE0 MFR1L_MOUSE Mitochondrial fission regulator 1-like 289 31,726 Alternative sequence (1); Chain (1); Modified residue (9); Sequence conflict (3) +Q64520 KGUA_MOUSE Guanylate kinase (EC 2.7.4.8) (GMP kinase) 198 21,918 Active site (3); Beta strand (7); Binding site (2); Chain (1); Domain (1); Helix (9); Nucleotide binding (1); Turn (3) FUNCTION: Essential for recycling GMP and indirectly, cGMP. SUBUNIT: Monomer. {ECO:0000250}. +Q9R226 KHDR3_MOUSE KH domain-containing, RNA-binding, signal transduction-associated protein 3 (RNA-binding protein Etoile) (Sam68-like mammalian protein 2) (SLM-2) 346 38,807 Chain (1); Compositional bias (2); Cross-link (1); Domain (1); Mutagenesis (2); Region (1); Sequence conflict (1) FUNCTION: RNA-binding protein that plays a role in the regulation of alternative splicing and influences mRNA splice site selection and exon inclusion. Binds preferentially to the 5'-[AU]UAAA-3' motif in vitro (PubMed:19457263). Binds optimally to RNA containing 5'-[AU]UAA-3' as a bipartite motif spaced by more than 15 nucleotides (By similarity). Binds poly(A). RNA-binding abilities are down-regulated by tyrosine kinase PTK6 (PubMed:15471878). Involved in splice site selection of vascular endothelial growth factor (By similarity). In vitro regulates CD44 alternative splicing by direct binding to purine-rich exonic enhancer (By similarity). Can regulate alternative splicing of neurexins NRXN1-3 in the laminin G-like domain 6 containing the evolutionary conserved neurexin alternative spliced segment 4 (AS4) involved in neurexin selective targeting to postsynaptic partners such as neuroligins and LRRTM family members. High concentrations in forebrain structures block splicing inclusion of NRXN1-3 AS4 exons while low concentrations favor their inclusion. Targeted, cell-type specific splicing regulation of NRXN1 at AS4 is involved in neuronal glutamatergic synapse function and plasticity and is linked to behavioral aspects (PubMed:22196734, PubMed:23637638, PubMed:24469635, PubMed:27174676). Regulates expression of KHDRBS2/SLIM-1 in defined neuron populations in the hippocampus by modifying its alternative splicing resulting in a transcript predicted to undergo nonsense-mediated decay (PubMed:25505328). Can bind FABP9 mRNA (PubMed:19916944). May play a role as a negative regulator of cell growth. Inhibits cell proliferation. {ECO:0000250|UniProtKB:O75525, ECO:0000250|UniProtKB:Q9JLP1, ECO:0000269|PubMed:15471878, ECO:0000269|PubMed:19457263, ECO:0000269|PubMed:19916944, ECO:0000269|PubMed:22196734, ECO:0000269|PubMed:23637638, ECO:0000269|PubMed:24469635, ECO:0000269|PubMed:27174676}. PTM: Phosphorylated on tyrosine residues by PTK6. {ECO:0000269|PubMed:15471878}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10332027, ECO:0000269|PubMed:15471878}. Note=Localized in a compartment adjacent to the nucleolus, but distinct from the peri-nucleolar one. SUBUNIT: Self-associates to form homooligomers; dimerization increases RNA affinity (By similarity). Interacts with KHDRBS2/SLM-1 (By similarity). Interacts with KHDRBS1/SAM68; heterooligomer formation of KHDRBS family proteins may modulate RNA substrate specificity (PubMed:10077576). Interacts with the splicing regulatory proteins SFRS9, SAFB and YTHDC1. Interacts with HNRPL, RBMX, RBMY1A1, p85 subunit of PI3-kinase, SERPINB5 (By similarity). {ECO:0000250|UniProtKB:O75525, ECO:0000250|UniProtKB:Q9JLP1, ECO:0000269|PubMed:10077576, ECO:0000305}. DOMAIN: The proline-rich site binds the SH3 domain of the p85 subunit of PI3-kinase. {ECO:0000250|UniProtKB:O75525}. TISSUE SPECIFICITY: Highly expressed in testis and brain. In adult cerebellum expressed predominantly in internal granular layer interneurons and in hippocampus is exclusively expressed in CA neurons; expression is restricted to neuronal subpopulations largely non-overlapping with expression of KHDRBS2/SLM-1. {ECO:0000269|PubMed:10332027, ECO:0000269|PubMed:15471878, ECO:0000269|PubMed:23637638, ECO:0000269|PubMed:24469635}. +Q9EQW7 KI13A_MOUSE Kinesin-like protein KIF13A 1749 195,813 Beta strand (12); Chain (1); Coiled coil (4); Domain (2); Helix (1); Modified residue (8); Nucleotide binding (1); Sequence conflict (2); Turn (1) FUNCTION: Plus end-directed microtubule-dependent motor protein involved in intracellular transport and regulating various processes such as mannose-6-phosphate receptor (M6PR) transport to the plasma membrane, endosomal sorting during melanosome biogenesis and cytokinesis. During melanosome maturation, required for delivering melanogenic enzymes from recycling endosomes to nascent melanosomes by creating peripheral recycling endosomal subdomains in melanocytes. Also required for the abcission step in cytokinesis: mediates translocation of ZFYVE26, and possibly TTC19, to the midbody during cytokinesis (By similarity). Mediates the transport of M6PR-containing vesicles from trans-Golgi network to the plasma membrane via direct interaction with the AP-1 complex. {ECO:0000250, ECO:0000269|PubMed:11106728}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:11106728}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000305|PubMed:11106728}. Midbody {ECO:0000250}. Endosome membrane {ECO:0000250}. Note=Recruited to the midbody during cytokinesis. {ECO:0000250}. SUBUNIT: Interacts with AP1G1 and AP1G2. Interacts with ZFYVE26 (By similarity). Interacts with AP2B1. {ECO:0000250, ECO:0000269|PubMed:11106728}. +Q91WD7 KI18A_MOUSE Kinesin-like protein KIF18A 886 100,935 Chain (1); Coiled coil (1); Cross-link (4); Domain (1); Modified residue (3); Nucleotide binding (1) FUNCTION: Microtubule-depolymerizing kinesin which plays a role in chromosome congression by reducing the amplitude of preanaphase oscillations and slowing poleward movement during anaphase, thus suppressing chromosome movements. May stabilize the CENPE-BUB1B complex at the kinetochores during early mitosis and maintains CENPE levels at kinetochores during chromosome congression (By similarity). {ECO:0000250}. PTM: Glycosylated. {ECO:0000250}.; PTM: Ubiquitinated. {ECO:0000250}. SUBCELLULAR LOCATION: Cell projection, ruffle {ECO:0000250}. Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. SUBUNIT: Interacts with CENPE and ESR1. {ECO:0000250}. +P97329 KI20A_MOUSE Kinesin-like protein KIF20A (Kinesin-like protein 174) (Rab6-interacting kinesin-like protein) (Rabkinesin-6) 887 99,876 Chain (1); Coiled coil (1); Domain (1); Helix (1); Initiator methionine (1); Modified residue (11); Nucleotide binding (1); Region (1) FUNCTION: Mitotic kinesin required for chromosome passenger complex (CPC)-mediated cytokinesis. Following phosphorylation by PLK1, involved in recruitment of PLK1 to the central spindle (By similarity). Interacts with guanosine triphosphate (GTP)-bound forms of RAB6A and RAB6B. May act as a motor required for the retrograde RAB6 regulated transport of Golgi membranes and associated vesicles along microtubules. Has a microtubule plus end-directed motility. {ECO:0000250, ECO:0000269|PubMed:9438855}. PTM: Phosphorylated by PLK1 at Ser-527 during mitosis, creating a docking site for PLK1 and recruiting PLK1 at central spindle. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000305|PubMed:9438855}. TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in spleen and testis. {ECO:0000269|PubMed:9438855}. +P33173 KIF1A_MOUSE Kinesin-like protein KIF1A (Axonal transporter of synaptic vesicles) 1695 191,725 Beta strand (17); Chain (1); Coiled coil (4); Domain (3); Helix (16); Modified residue (14); Nucleotide binding (1); Turn (4) FUNCTION: Motor for anterograde axonal transport of synaptic vesicle precursors. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Note=Expressed in distal regions of neurites. {ECO:0000250}. SUBUNIT: Monomer. Interacts with PPFIA1 and PPFIA4 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed almost exclusively in adult brain tissue (mainly in the cerebellum and cerebrum) within a single type of neuronal cell. Within the neuronal cell levels are concentrated around the axon, with smaller amounts in the perinuclear and synaptic regions. +Q61771 KIF3B_MOUSE Kinesin-like protein KIF3B (Microtubule plus end-directed kinesin motor 3B) [Cleaved into: Kinesin-like protein KIF3B, N-terminally processed] 747 85,288 Chain (2); Coiled coil (1); Compositional bias (3); Domain (1); Initiator methionine (1); Modified residue (2); Nucleotide binding (1); Region (1) FUNCTION: Involved in tethering the chromosomes to the spindle pole and in chromosome movement. Microtubule-based anterograde translocator for membranous organelles. Plus end-directed microtubule sliding activity in vitro (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. Cell projection, cilium {ECO:0000269|PubMed:25243405}. SUBUNIT: Interacts with the SMC3 subunit of the cohesin complex (By similarity). Heterodimer of KIF3A and KIF3B (PubMed:7559760). Interacts directly with IFT20 (PubMed:12821668). {ECO:0000250|UniProtKB:O15066, ECO:0000269|PubMed:12821668, ECO:0000269|PubMed:7559760}. +O35071 KIF1C_MOUSE Kinesin-like protein KIF1C 1100 122,434 Chain (1); Coiled coil (4); Compositional bias (1); Domain (2); Modified residue (9); Nucleotide binding (1) FUNCTION: Motor required for the retrograde transport of Golgi vesicles to the endoplasmic reticulum. Has a microtubule plus end-directed motility (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. SUBUNIT: Monomer. {ECO:0000305}. +Q91ZV0 MIA2_MOUSE Melanoma inhibitory activity protein 2 (CTAGE family member 5 ER export factor) 1396 156,461 Alternative sequence (3); Chain (1); Coiled coil (2); Compositional bias (1); Domain (1); Glycosylation (2); Intramembrane (1); Mutagenesis (1); Region (2); Sequence conflict (2); Signal peptide (1); Topological domain (3); Transmembrane (1) INTRAMEM 605 625 {ECO:0000255}. TRANSMEM 629 649 Helical. {ECO:0000255}. TOPO_DOM 23 604 Lumenal. {ECO:0000305}.; TOPO_DOM 626 628 Lumenal. {ECO:0000305}.; TOPO_DOM 650 1396 Cytoplasmic. {ECO:0000305}. FUNCTION: Plays a role in the transport of cargos that are too large to fit into COPII-coated vesicles and require specific mechanisms to be incorporated into membrane-bound carriers and exported from the endoplasmic reticulum. Plays a role in the secretion of lipoproteins, pre-chylomicrons and pre-VLDLs, by participating in their export from the endoplasmic reticulum (By similarity). Thereby, may play a role in cholesterol and triglyceride homeostasis (PubMed:21807889). Required for collagen VII (COL7A1) secretion by loading COL7A1 into transport carriers and recruiting PREB/SEC12 at the endoplasmic reticulum exit sites (By similarity). {ECO:0000250|UniProtKB:Q96PC5, ECO:0000269|PubMed:21807889}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21807889}; Single-pass membrane protein {ECO:0000305|PubMed:21807889}. Note=Localizes to endoplasmic reticulum exit sites (ERES), also known as transitional endoplasmic reticulum (tER). {ECO:0000269|PubMed:21807889}. SUBUNIT: Interacts with MIA3 (By similarity). Interacts with the COPII coat subunits SEC23A, SEC23B and maybe SEC24C (By similarity) (PubMed:21807889). Interacts with PREB; recruits PREB to endoplasmic reticulum exit sites. Interacts with APOB (By similarity). {ECO:0000250|UniProtKB:Q96PC5, ECO:0000269|PubMed:21807889}. DOMAIN: The proline-rich domain (PRD) contains repeated PPP motifs. A single PPP motif is necessary and sufficient to mediate interaction with the COPII coat subunits SEC23A and SEC23B (PubMed:21807889). The coiled coil domains mediate interaction with MIA3. The first coiled coil domain mediates interaction with PREB (By similarity). {ECO:0000250|UniProtKB:Q96PC5, ECO:0000269|PubMed:21807889}. TISSUE SPECIFICITY: Isoform 1 is expressed in liver (at protein level) (PubMed:12586826, PubMed:21807889). Isoform 2 is highly expressed in liver and weakly in testis (PubMed:12586826). {ECO:0000269|PubMed:12586826, ECO:0000269|PubMed:21807889}. +Q9WV04 KIF9_MOUSE Kinesin-like protein KIF9 790 89,898 Chain (1); Coiled coil (2); Domain (1); Modified residue (1); Nucleotide binding (2); Sequence conflict (2) SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. +Q9R008 KIME_MOUSE Mevalonate kinase (MK) (EC 2.7.1.36) 395 41,877 Active site (1); Binding site (4); Chain (1); Metal binding (2); Nucleotide binding (1) Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate: step 1/3. FUNCTION: Catalyzes the phosphorylation of mevalonate to mevalonate 5-phosphate, a key step in isoprenoid and cholesterol biosynthesis. {ECO:0000250|UniProtKB:Q03426}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P17256}. Peroxisome {ECO:0000250|UniProtKB:P17256}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q03426}. +O88448 KLC2_MOUSE Kinesin light chain 2 (KLC 2) 599 66,662 Chain (1); Coiled coil (1); Helix (11); Modified residue (8); Repeat (6); Turn (1) FUNCTION: Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. The light chain may function in coupling of cargo to the heavy chain or in the modulation of its ATPase activity. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. SUBUNIT: Oligomeric complex composed of two heavy chains and two light chains. +A2APT9 KLD7A_MOUSE Kelch domain-containing protein 7A 773 83,590 Chain (1); Compositional bias (1); Erroneous initiation (1); Frameshift (1); Glycosylation (2); Modified residue (2); Repeat (5); Sequence conflict (2); Transmembrane (1) TRANSMEM 23 40 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q9D2D9 KLD8B_MOUSE Kelch domain-containing protein 8B 354 37,592 Chain (1); Repeat (8) FUNCTION: Involved in pinching off the separated nuclei at the cleavage furrow and in cytokinesis. Required for mitotic integrity and maintenance of chromosomal stability. Protects cells against mitotic errors, centrosomal amplification, micronucleus formation and aneuploidy. Plays a key role of midbody function involving abscission of the daughter cells during cytokinesis and appropriate chromosomal and nuclear segregation into the daughter cells. {ECO:0000250|UniProtKB:Q8IXV7}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8IXV7}. Midbody {ECO:0000250|UniProtKB:Q8IXV7}. Note=In mitotic cells, concentrates in the midbody of the cytoplasmic bridge linking daughter cells as they are about to separate during cytokinesis. {ECO:0000250|UniProtKB:Q8IXV7}. +Q8K1S5 KLF11_MOUSE Krueppel-like factor 11 (TGFB-inducible early growth response protein 2b) (Transforming growth factor-beta-inducible early growth response protein 3) (TGFB-inducible early growth response protein 3) (TIEG-3) 502 54,054 Chain (1); Frameshift (1); Sequence conflict (5); Zinc finger (3) FUNCTION: Transcription factor. Activates the epsilon- and gamma-globin gene promoters and, to a much lower degree, the beta-globin gene and represses promoters containing SP1-like binding sites inhibiting cell growth (By similarity). Represses transcription of SMAD7 which enhances TGF-beta signaling. Induces apoptosis. {ECO:0000250|UniProtKB:O14901, ECO:0000269|PubMed:14697507, ECO:0000269|PubMed:18189266}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O14901}. SUBUNIT: Interacts with SIN3A. {ECO:0000250|UniProtKB:O14901}. +Q4G5Y1 KLDC2_MOUSE Kelch domain-containing protein 2 (Endothelial differentiation inhibitory protein TNG) 406 45,909 Chain (1); Repeat (6); Sequence conflict (3) FUNCTION: Represses CREB3-mediated transcription by interfering with CREB3-DNA binding. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Directly interacts with CREB3, but not with CREB1, ATF4, ATF6, JUN, FOS, CEBPA. {ECO:0000250}. +O35738 KLF12_MOUSE Krueppel-like factor 12 (Transcriptional repressor AP-2rep) 402 44,105 Chain (1); Modified residue (2); Sequence conflict (4); Zinc finger (3) FUNCTION: Confers strong transcriptional repression to the AP-2-alpha gene. Binds to a regulatory element (A32) in the AP-2-alpha gene promoter. SUBCELLULAR LOCATION: Nucleus. +Q9JJZ6 KLF13_MOUSE Krueppel-like factor 13 (Basic transcription element-binding protein 3) (BTE-binding protein 3) (Erythroid transcription factor FKLF-2) (RANTES factor of late activated T-lymphocytes 1) (RFLAT-1) (Transcription factor BTEB3) 289 31,136 Chain (1); Compositional bias (3); Modified residue (5); Sequence conflict (3); Zinc finger (3) FUNCTION: Transcription factor that activates expression from GC-rich minimal promoter regions, including genes in the cells of the erythroid lineage. SUBCELLULAR LOCATION: Nucleus. TISSUE SPECIFICITY: Ubiquitous. +Q69ZK5 KLH14_MOUSE Kelch-like protein 14 (Protein interactor of Torsin-1A) (Printor) (Protein interactor of torsinA) 630 70,953 Chain (1); Domain (2); Repeat (6); Sequence conflict (6) SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}. Note=In neurons, located in cell bodies, as well as in neurites. {ECO:0000269|PubMed:19535332}. SUBUNIT: Interacts with TOR1A. {ECO:0000269|PubMed:19535332}. TISSUE SPECIFICITY: Expressed in the brain, primarily in neurons. In the cerebral cortex, mostly expressed in layers I and II (at protein level). Also observed in some neurons of the corpus striatum (at protein level). Expressed at high levels in the hippocampus, including in pyramidal cells of the CA1 and CA3 layers (at protein level). In the cerebellum, expression in Purkinje cells is higher than in granular cells (at protein level). Also detected in the medial septum, ventral pallidum, thalamus, hypothalamus, amygdala, inferior colliculi, locus caeruleus, peripyramidal nucleus, raphe nucleus, reticular formation, spinal trigeminal nucleus, and vestibular nuclei (at protein level). Low expression, if any, in glial cells (at protein level). Not observed in the corpus callosum. {ECO:0000269|PubMed:19535332}. +P46099 KLF1_MOUSE Krueppel-like factor 1 (Erythroid krueppel-like transcription factor) (EKLF) 358 37,757 Chain (1); Compositional bias (1); Cross-link (1); Erroneous initiation (1); Modified residue (4); Mutagenesis (9); Sequence conflict (4); Zinc finger (3) FUNCTION: Transcription regulator of erythrocyte development. Binds to the CACCC box in the beta-globin gene promoter and activates transcription. Probably serves as a general switch factor for erythroid development. When sumoylated, acts as a transcriptional repressor by promoting interaction with CDH2/MI2beta and also represses megakaryocytic differentiation. {ECO:0000269|PubMed:11259590, ECO:0000269|PubMed:15542849, ECO:0000269|PubMed:17938210, ECO:0000269|PubMed:9722526}. PTM: Acetylated; can be acetylated on both Lys-270 and Lys-288. Acetylation on Lys-270 (by CBP) appears to be the major site affecting EKLF transactivation activity. {ECO:0000269|PubMed:11259590}.; PTM: Sumoylated; sumoylation, promoted by PIAS1, leads to repression of megakaryocyte differentiation. Also promotes the interaction with the CDH4 subunit of the NuRD repression complex. {ECO:0000269|PubMed:17938210}.; PTM: Phosphorylated primarily on serine residues in the transactivation domain. Phosphorylation on Thr-23 is critical for the transactivation activity. {ECO:0000269|PubMed:9722526}. SUBCELLULAR LOCATION: Nucleus. Note=Colocalizes with SUMO1 in nuclear speckles. SUBUNIT: Interacts with CBP and EP300; the interactions enhance the transactivation activity. Interacts with PCAF; the interaction does not acetylate EKLF and inhibits its transactivation activity (By similarity). Interacts with CDH4; the interaction is SUMO-dependent and leads to transcriptional repression. {ECO:0000250, ECO:0000269|PubMed:15542849, ECO:0000269|PubMed:17938210}. TISSUE SPECIFICITY: Erythroid-specific. Only expressed in bone marrow and spleen. +Q6TDP3 KLH17_MOUSE Kelch-like protein 17 (Actinfilin) 640 69,732 Chain (1); Compositional bias (1); Domain (2); Region (2); Repeat (6) Protein modification; protein ubiquitination. FUNCTION: Substrate-recognition component of some cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex. The BCR(KLHL17) mediates the ubiquitination and subsequenct degradation of GLUR6. May play a role in the actin-based neuronal function (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250}. Cell junction, synapse {ECO:0000250}. Note=Postsynaptic density. {ECO:0000250}. SUBUNIT: Interacts with F-actin; the interaction disruptes the F-actin structures and leads to marked changes of neuronal morphology. Component of a complex, composed of PDZK1, SYNGAP1, KLHL17 and NMDA receptors. Interacts directly with PDZK1 (via PDZ1 domain); the interaction is important for integrity of actin cytoskeleton structures in neurons. Interacts with DLG4 and SYNGAP1. Interacts (via kelch repeats) with GRIK2 (via C-terminus); the interaction targets GRIK2 for degradation via ubiquitin-proteasome pathway. Interacts with GRIK1. Interacts with (via BTB domain) CUL3; the interaction regulates surface GRIK2 expression (By similarity). {ECO:0000250}. +Q8VCK5 KLH20_MOUSE Kelch-like protein 20 (Kelch-like ECT2-interacting protein) 604 67,412 Chain (1); Domain (2); Erroneous initiation (1); Repeat (6) Protein modification; protein ubiquitination. FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex involved in interferon response and anterograde Golgi to endosome transport. The BCR(KLHL20) E3 ubiquitin ligase complex mediates the ubiquitination of DAPK1, leading to its degradation by the proteasome, thereby acting as a negative regulator of apoptosis. The BCR(KLHL20) E3 ubiquitin ligase complex also specifically mediates 'Lys-33'-linked ubiquitination. Involved in anterograde Golgi to endosome transport by mediating 'Lys-33'-linked ubiquitination of CORO7, promoting interaction between CORO7 and EPS15, thereby facilitating actin polymerization and post-Golgi trafficking. Also acts as a regulator of endothelial migration during angiogenesis by controlling the activation of Rho GTPases. The BCR(KLHL20) E3 ubiquitin ligase complex acts as a regulator of neurite outgrowth by mediating ubiquitination and degradation of PDZ-RhoGEF/ARHGEF11 (By similarity). {ECO:0000250|UniProtKB:Q9Y2M5}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000250}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Cell projection, axon {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Note=Localizes in the perinuclear region in normal conditions. Following IFN-alpha or IFN-gamma treatment, it is relocalized and sequestrated to the PML nuclear bodies, preventing DAPK1 ubiquitination (By similarity). {ECO:0000250}. SUBUNIT: Component of the BCR(KLHL20) E3 ubiquitin ligase complex, at least composed of CUL3, KLHL20 and RBX1. Interacts with PDZ-RhoGEF/ARHGEF11, DAPK1, PML and CORO7. Interacts with F-actin. Interacts with IFN-gamma (IFNG) (By similarity). Interacts (via kelch repeats) with IVNS1ABP (via kelch repeats); this interaction blocks the assembly of CUL3-KLHL20 complex (By similarity). {ECO:0000250|UniProtKB:Q9Y2M5}. +Q8R124 KLH36_MOUSE Kelch-like protein 36 613 69,950 Chain (1); Domain (2); Erroneous initiation (1); Repeat (6); Sequence conflict (1) Protein modification; protein ubiquitination. FUNCTION: Probable substrate-specific adapter of an E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000250}. SUBUNIT: Interacts with CUL3. {ECO:0000250}. +Q8BSF5 KLH38_MOUSE Kelch-like protein 38 581 65,651 Chain (1); Domain (2); Repeat (6) +Q6GQU2 KLH23_MOUSE Kelch-like protein 23 558 63,840 Chain (1); Domain (2); Repeat (6); Sequence conflict (1) +O08584 KLF6_MOUSE Krueppel-like factor 6 (Core promoter element-binding protein) 283 31,877 Chain (1); Erroneous initiation (1); Zinc finger (3) FUNCTION: Transcriptional activator. Binds a GC box motif. Could play a role in B-cell growth and development (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. DOMAIN: The acidic N-terminal part may favor interaction with the basic domain of transcription factors. TISSUE SPECIFICITY: Highly expressed in placenta. +Q8R2P1 KLH25_MOUSE Kelch-like protein 25 (Ectoderm-neural cortex protein 2) (ENC-2) 589 65,826 Chain (1); Domain (2); Repeat (6) Protein modification; protein ubiquitination. FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex required for translational homeostasis. The BCR(KLHL25) ubiquitin ligase complex acts by mediating ubiquitination of hypophosphorylated EIF4EBP1 (4E-BP1): ubiquitination and subsequent degradation of hypophosphorylated EIF4EBP1 (4E-BP1) probably serves as a homeostatic mechanism to maintain translation and prevent eIF4E inhibition when eIF4E levels are low. The BCR(KLHL25) complex does not target EIF4EBP1 (4E-BP1) when it is hyperphosphorylated or associated with eIF4E. {ECO:0000269|PubMed:22578813}. SUBUNIT: Component of the BCR(KLHL25) E3 ubiquitin ligase complex, at least composed of CUL3, KLHL25 and RBX1. Interacts with EIF4EBP1 (when hypophosphorylated) (By similarity). {ECO:0000250}. +Q8BGY4 KLH26_MOUSE Kelch-like protein 26 606 67,031 Alternative sequence (2); Chain (1); Domain (2); Erroneous initiation (1); Initiator methionine (1); Modified residue (2); Repeat (6) +Q9CR40 KLH28_MOUSE Kelch-like protein 28 (BTB/POZ domain-containing protein 5) 571 64,125 Alternative sequence (1); Chain (1); Domain (1); Repeat (6) +Q9D5V2 KLH10_MOUSE Kelch-like protein 10 608 68,977 Chain (1); Domain (1); Modified residue (1); Repeat (6); Sequence conflict (2) Protein modification; protein ubiquitination. FUNCTION: May be a substrate-specific adapter of a CUL3-based E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins during spermatogenesis. Required for male fertility. {ECO:0000269|PubMed:15136734, ECO:0000269|PubMed:16162871}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15136734}. SUBUNIT: Self-associates (By similarity). Interacts with CUL3; indicative for the participation in an E3 ubiquitin ligase complex. {ECO:0000250, ECO:0000269|PubMed:16162871}. TISSUE SPECIFICITY: Testis specific. {ECO:0000269|PubMed:15136734}. +Q9JI74 KLHL1_MOUSE Kelch-like protein 1 751 82,892 Chain (1); Compositional bias (1); Domain (1); Repeat (6); Sequence conflict (6) FUNCTION: May play a role in organizing the actin cytoskeleton of the brain cells. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. TISSUE SPECIFICITY: Highly expressed in brain. +Q9QYN3 KLK11_MOUSE Kallikrein-11 (EC 3.4.21.-) (Hippostasin) (Serine protease 20) 276 30,754 Active site (3); Alternative sequence (1); Chain (1); Disulfide bond (5); Domain (1); Glycosylation (4); Propeptide (1); Signal peptide (1) FUNCTION: Possible multifunctional protease. Efficiently cleaves 'bz-Phe-Arg-4-methylcoumaryl-7-amide', a kallikrein substrate, and weakly cleaves other substrates for kallikrein and trypsin (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Expressed in brain and prostate (isoform 1) and prostate (isoform 2). {ECO:0000269|PubMed:11072088}. +O35082 KLOT_MOUSE Klotho (EC 3.2.1.31) [Cleaved into: Klotho peptide] 1014 116,398 Alternative sequence (2); Chain (2); Glycosylation (6); Region (2); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 983 1003 Helical. {ECO:0000255}. TOPO_DOM 35 982 Extracellular. {ECO:0000255}.; TOPO_DOM 1004 1014 Cytoplasmic. {ECO:0000255}. FUNCTION: May have weak glycosidase activity towards glucuronylated steroids. However, it lacks essential active site Glu residues at positions 241 and 874, suggesting it may be inactive as a glycosidase in vivo. May be involved in the regulation of calcium and phosphorus homeostasis by inhibiting the synthesis of active vitamin D. Essential factor for the specific interaction between FGF23 and FGFR1.; FUNCTION: The Klotho peptide generated by cleavage of the membrane-bound isoform may be an anti-aging circulating hormone which would extend life span by inhibiting insulin/IGF1 signaling. PTM: N-glycosylated. {ECO:0000269|PubMed:15135068}. SUBCELLULAR LOCATION: Isoform 1: Cell membrane {ECO:0000269|PubMed:10631108, ECO:0000269|PubMed:12204354, ECO:0000269|PubMed:15135068, ECO:0000269|PubMed:9363890}; Single-pass type I membrane protein {ECO:0000305|PubMed:9363890}. Apical cell membrane {ECO:0000269|PubMed:15665504}; Single-pass type I membrane protein {ECO:0000305|PubMed:15665504}. Note=Isoform 1 shedding leads to a soluble peptide. {ECO:0000269|PubMed:16123266}.; SUBCELLULAR LOCATION: Isoform 2: Secreted {ECO:0000269|PubMed:10631108, ECO:0000269|PubMed:15135068}.; SUBCELLULAR LOCATION: Klotho peptide: Secreted {ECO:0000269|PubMed:16123266}. SUBUNIT: Homodimer. Interacts with FGF23 and FGFR1. {ECO:0000269|PubMed:15135068, ECO:0000269|PubMed:17086194}. DOMAIN: Contains 2 glycosyl hydrolase 1 regions. However, the first region lacks the essential Glu active site residue at position 241, and the second one lacks the essential Glu active site residue at position 874. TISSUE SPECIFICITY: Membrane-bound protein is present in distal renal tubules, inner ear, ependymal cells of brain choroid plexus, elongating spermatids and mature oocytes (at protein level). Soluble peptide is present in serum (100 pM) and cerebrospinal fluid. Expressed strongly in kidney, moderately in brain choroid plexus, and at low levels in pituitary, placenta, skeletal muscle, urinary bladder, aorta, pancreas, testis, ovary, colon, thyroid gland and adipocytes. {ECO:0000269|PubMed:10631108, ECO:0000269|PubMed:11411791, ECO:0000269|PubMed:12204354, ECO:0000269|PubMed:15135068, ECO:0000269|PubMed:15665504, ECO:0000269|PubMed:16123266, ECO:0000269|PubMed:9363890, ECO:0000269|PubMed:9537505}. +Q91YA2 KPSH1_MOUSE Serine/threonine-protein kinase H1 (EC 2.7.11.1) (Protein serine kinase H1) (PSK-H1) 424 48,095 Active site (1); Binding site (1); Chain (1); Domain (1); Initiator methionine (1); Lipidation (2); Modified residue (2); Nucleotide binding (1); Sequence conflict (1) FUNCTION: May be a SFC-associated serine kinase (splicing factor compartment-associated serine kinase) with a role in intranuclear SR protein (non-snRNP splicing factors containing a serine/arginine-rich domain) trafficking and pre-mRNA processing. {ECO:0000250}. PTM: Autophosphorylated on serine residues. {ECO:0000250}.; PTM: Myristoylated. Required for membrane association. Prerequisite for palmitoylation to occur (By similarity). {ECO:0000250}.; PTM: Palmitoylated. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Nucleus speckle {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Localized in the brefeldin A- sensitive Golgi compartment, at centrosomes, in the nucleus with a somewhat speckle-like presence, membrane-associated to the endoplasmic reticulum (ER) and the plasma membrane (PM), and more diffusely in the cytoplasm. Found to concentrate in splicing factor compartments (SFCs) within the nucleus of interphase cells. The acylation-negative form may be only cytoplasmic and nuclear. Acylation seems to allow the sequestering to the intracellular membranes. Myristoylation may mediate targeting to the intracellular non-Golgi membranes and palmitoylation may mediate the targeting to the Golgi membranes. Dual acylation is required to stabilize the interaction with Golgi membranes (By similarity). {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +Q9Z287 KR121_MOUSE Keratin-associated protein 12-1 130 13,119 Chain (1); Region (1); Repeat (14) FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins (By similarity). {ECO:0000250|UniProtKB:P59990}. SUBUNIT: Interacts with hair keratins. {ECO:0000250|UniProtKB:P59990}. TISSUE SPECIFICITY: Expressed only in the head and back skin of a 3 day old mouse. Not expressed in adult skin. {ECO:0000269|PubMed:9878246}. +Q9D7P0 KRA33_MOUSE Keratin-associated protein 3-3 99 10,531 Chain (1); Initiator methionine (1); Modified residue (1); Region (1); Repeat (3) FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins. {ECO:0000305}. SUBUNIT: Interacts with hair keratins. {ECO:0000305}. +Q99N43 KREM1_MOUSE Kremen protein 1 (Dickkopf receptor) (Kringle domain-containing transmembrane protein 1) (Kringle-containing protein marking the eye and the nose) 473 51,673 Chain (1); Disulfide bond (8); Domain (3); Glycosylation (6); Mutagenesis (5); Region (1); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 393 413 Helical. {ECO:0000255}. TOPO_DOM 21 392 Extracellular. {ECO:0000255}.; TOPO_DOM 414 473 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for Dickkopf proteins. Cooperates with DKK1/2 to inhibit Wnt/beta-catenin signaling by promoting the endocytosis of Wnt receptors LRP5 and LRP6 (PubMed:12050670). In the absence of DKK1, potentiates Wnt-beta-catenin signaling by maintaining LRP5 or LRP6 at the cell membrane (By similarity). Can trigger apoptosis in a Wnt-independent manner and this apoptotic activity is inhibited upon binding of the ligand DKK1 (PubMed:26206087). Plays a role in limb development; attenuates Wnt signaling in the developing limb to allow normal limb patterning and can also negatively regulate bone formation (PubMed:18505822). Modulates cell fate decisions in the developing cochlea with an inhibitory role in hair cell fate specification (PubMed:27550540). {ECO:0000250|UniProtKB:Q90Y90, ECO:0000269|PubMed:12050670, ECO:0000269|PubMed:18505822, ECO:0000269|PubMed:26206087, ECO:0000269|PubMed:27550540}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27550540}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Forms a ternary complex with DKK1 and LRP6 (PubMed:12050670). Interacts with LRP6 in a DKK1-dependent manner. Interacts with DKK1 and RSPO1 (via FU repeats) (By similarity). {ECO:0000250|UniProtKB:Q96MU8, ECO:0000269|PubMed:12050670}. TISSUE SPECIFICITY: In the adult, widely expressed with high levels in heart, lung, kidney, skeletal muscle and testis. {ECO:0000269|PubMed:11267660}. +Q6NXZ1 KRBA1_MOUSE Protein KRBA1 1043 111,257 Alternative sequence (3); Chain (1); Coiled coil (1); Compositional bias (1); Erroneous initiation (1); Modified residue (4); Sequence conflict (4) +P27812 KRBBA_MOUSE Killer cell lectin-like receptor subfamily B member 1B allele A (CD161 antigen-like family member B) (Lymphocyte antigen 55b) (Ly-55b) (NKR-P1 34) (Natural killer cell surface protein NKR-P1B allele SJL/BALB) (NKR-P1B) (CD antigen CD161b) 223 25,158 Chain (1); Disulfide bond (2); Domain (1); Motif (2); Mutagenesis (3); Natural variant (2); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 44 63 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 43 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 64 223 Extracellular. {ECO:0000255}. "FUNCTION: Receptor for CLEC2D/OCIL. Ligand-binding contributes to inhibition of cytotoxic natural killer (NK) cells. May mediate MHC class I-independent ""missing-self"" recognition of allografts, tumor cells and virus-infected cells. {ECO:0000269|PubMed:10229823, ECO:0000269|PubMed:10229828, ECO:0000269|PubMed:14990792}." SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. SUBUNIT: Homodimer; disulfide-linked. Interacts with tyrosine kinase LCK. Binds PTPN6/SHP-1 in a phosphorylation-dependent manner. {ECO:0000269|PubMed:10229828, ECO:0000269|PubMed:14990792, ECO:0000269|PubMed:15814704}. DOMAIN: Contains 1 copy of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). The phosphorylated ITIM motif can bind the SH2 domain of several SH2-containing phosphatases leading to down-regulation of cell activation. {ECO:0000269|PubMed:15814704}. TISSUE SPECIFICITY: Expressed in NK cells and a subset of T-cells. +Q99JB4 KRBBB_MOUSE Killer cell lectin-like receptor subfamily B member 1B allele B (CD161 antigen-like family member B) (Inhibitory receptor NKR-P1B) (Lymphocyte antigen 55d) (Ly-55d) (NKR-P1D) (Natural killer cell surface protein NKR-P1B allele B6) (CD antigen CD161b) 223 25,027 Beta strand (7); Chain (1); Disulfide bond (2); Domain (1); Helix (2); Motif (2); Sequence conflict (19); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 44 64 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 43 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 65 223 Extracellular. {ECO:0000255}. "FUNCTION: Receptor for CLEC2D/OCIL. Ligand-binding contributes to inhibition of cytotoxic natural killer (NK) cells. May mediate MHC class I-independent ""missing-self"" recognition of allografts, tumor cells and virus-infected cells. {ECO:0000269|PubMed:12858173, ECO:0000269|PubMed:14990792}." SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. SUBUNIT: Homodimer; disulfide-linked. Interacts with tyrosine kinase LCK. Binds PTPN6/SHP-1 in a phosphorylation-dependent manner. {ECO:0000269|PubMed:12858173, ECO:0000269|PubMed:14990792}. DOMAIN: Contains 1 copy of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). The phosphorylated ITIM motif can bind the SH2 domain of several SH2-containing phosphatases leading to down-regulation of cell activation. {ECO:0000269|PubMed:11685472}. TISSUE SPECIFICITY: Expressed in NK cells and a subset of T-cells. {ECO:0000269|PubMed:9390275}. +Q99JT5 KRCC1_MOUSE Lysine-rich coiled-coil protein 1 256 30,718 Chain (1); Coiled coil (1); Compositional bias (1) +B1AQ75 KRT36_MOUSE Keratin, type I cuticular Ha6 (Keratin-36) (K36) (Keratin-5) (MHRa-1) (Type I keratin 48 kDa) 473 52,790 Chain (1); Domain (1); Frameshift (1); Region (7); Sequence conflict (5); Site (1) SUBUNIT: Heterotetramer of two type I and two type II keratins. {ECO:0000269|PubMed:1385239}. TISSUE SPECIFICITY: In skin, only expressed in the suprabasal cells of tail scale epidermis. Suprabasally expressed in stratified squamous epithelia and also in the posterior unit of the complex filiform papillae of tongue. Expressed in rare anatomical sites in which an orthokeratinized stratum corneum would be too soft and a hard keratinized structure would be too rigid to meet the functional requirement of the respective epithelia. {ECO:0000269|PubMed:1385239}. +Q9ERE2 KRT81_MOUSE Keratin, type II cuticular Hb1 (Keratin-81) (K81) (Type II hair keratin Hb1) 481 52,863 Chain (1); Cross-link (1); Domain (1); Region (7) SUBUNIT: Heterotetramer of two type I and two type II keratins. {ECO:0000305}. TISSUE SPECIFICITY: Expressed in dorsal skin. {ECO:0000269|PubMed:12399393}. +Q9Z2T6 KRT85_MOUSE Keratin, type II cuticular Hb5 (Keratin-85) (K85) (Type II hair keratin Hb5) (Type-II keratin Kb25) 507 55,759 Chain (1); Cross-link (1); Domain (1); Region (7); Sequence conflict (3) SUBUNIT: Heterotetramer of two type I and two type II keratins. +P18653 KS6A1_MOUSE Ribosomal protein S6 kinase alpha-1 (S6K-alpha-1) (EC 2.7.11.1) (90 kDa ribosomal protein S6 kinase 1) (p90-RSK 1) (p90RSK1) (p90S6K) (MAP kinase-activated protein kinase 1a) (MAPK-activated protein kinase 1a) (MAPKAP kinase 1a) (MAPKAPK-1a) (Ribosomal S6 kinase 1) (RSK-1) 724 81,595 Active site (2); Binding site (2); Chain (1); Domain (3); Modified residue (9); Nucleotide binding (2) FUNCTION: Serine/threonine-protein kinase that acts downstream of ERK (MAPK1/ERK2 and MAPK3/ERK1) signaling and mediates mitogenic and stress-induced activation of the transcription factors CREB1, ETV1/ER81 and NR4A1/NUR77, regulates translation through RPS6 and EIF4B phosphorylation, and mediates cellular proliferation, survival, and differentiation by modulating mTOR signaling and repressing pro-apoptotic function of BAD and DAPK1. In fibroblast, is required for EGF-stimulated phosphorylation of CREB1, which results in the subsequent transcriptional activation of several immediate-early genes. In response to mitogenic stimulation (EGF and PMA), phosphorylates and activates NR4A1/NUR77 and ETV1/ER81 transcription factors and the cofactor CREBBP. Upon insulin-derived signal, acts indirectly on the transcription regulation of several genes by phosphorylating GSK3B at 'Ser-9' and inhibiting its activity. Phosphorylates RPS6 in response to serum or EGF via an mTOR-independent mechanism and promotes translation initiation by facilitating assembly of the pre-initiation complex. In response to insulin, phosphorylates EIF4B, enhancing EIF4B affinity for the EIF3 complex and stimulating cap-dependent translation. Is involved in the mTOR nutrient-sensing pathway by directly phosphorylating TSC2 at 'Ser-1798', which potently inhibits TSC2 ability to suppress mTOR signaling, and mediates phosphorylation of RPTOR, which regulates mTORC1 activity and may promote rapamycin-sensitive signaling independently of the PI3K/AKT pathway. Mediates cell survival by phosphorylating the pro-apoptotic proteins BAD and DAPK1 and suppressing their pro-apoptotic function. Promotes the survival of hepatic stellate cells by phosphorylating CEBPB in response to the hepatotoxin carbon tetrachloride (CCl4). Mediates induction of hepatocyte prolifration by TGFA through phosphorylation of CEBPB (PubMed:10635333). Is involved in cell cycle regulation by phosphorylating the CDK inhibitor CDKN1B, which promotes CDKN1B association with 14-3-3 proteins and prevents its translocation to the nucleus and inhibition of G1 progression (By similarity). Phosphorylates EPHA2 at 'Ser-897', the RPS6KA-EPHA2 signaling pathway controls cell migration (By similarity). {ECO:0000250|UniProtKB:Q15418, ECO:0000250|UniProtKB:Q63531, ECO:0000269|PubMed:10635333}. PTM: Activated by phosphorylation at Ser-221 by PDPK1. Autophosphorylated on Ser-369, as part of the activation process. May be phosphorylated at Thr-348 and Ser-352 by MAPK1/ERK2 and MAPK3/ERK1 (By similarity). {ECO:0000250}.; PTM: N-terminal myristoylation results in an activated kinase in the absence of added growth factors. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. SUBUNIT: Forms a complex with either MAPK1/ERK2 or MAPK3/ERK1 in quiescent cells. Transiently dissociates following mitogenic stimulation. Interacts with ETV1/ER81 and FGFR1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Intestine, thymus, and lung. +Q9WUT3 KS6A2_MOUSE Ribosomal protein S6 kinase alpha-2 (S6K-alpha-2) (EC 2.7.11.1) (90 kDa ribosomal protein S6 kinase 2) (p90-RSK 2) (p90RSK2) (MAP kinase-activated protein kinase 1c) (MAPK-activated protein kinase 1c) (MAPKAP kinase 1c) (MAPKAPK-1c) (Protein-tyrosine kinase Mpk-9) (Ribosomal S6 kinase 3) (RSK-3) (pp90RSK3) 733 83,157 Active site (2); Binding site (2); Chain (1); Domain (3); Modified residue (2); Nucleotide binding (2); Sequence conflict (1) FUNCTION: Serine/threonine-protein kinase that acts downstream of ERK (MAPK1/ERK2 and MAPK3/ERK1) signaling and mediates mitogenic and stress-induced activation of transcription factors, regulates translation, and mediates cellular proliferation, survival, and differentiation. May function as tumor suppressor in epithelial ovarian cancer cells (By similarity). {ECO:0000250}. PTM: Activated by phosphorylation at Ser-218 by PDPK1. Autophosphorylated on Ser-377, as part of the activation process. May be phosphorylated at Thr-356 and Ser-360 by MAPK1/ERK2 and MAPK3/ERK1 (By similarity). {ECO:0000250}.; PTM: N-terminal myristoylation results in an activated kinase in the absence of added growth factors. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. SUBUNIT: Forms a complex with either MAPK1/ERK2 or MAPK3/ERK1 in quiescent cells. Transiently dissociates following mitogenic stimulation (By similarity). Interacts with FBXO5; cooperate to induce the metaphase arrest of early blastomeres; increases and stabilizes interaction of FBXO5 with CDC20 (PubMed:15526037). {ECO:0000250, ECO:0000269|PubMed:15526037}. +Q8C050 KS6A5_MOUSE Ribosomal protein S6 kinase alpha-5 (S6K-alpha-5) (EC 2.7.11.1) (90 kDa ribosomal protein S6 kinase 5) (Nuclear mitogen- and stress-activated protein kinase 1) (RSK-like protein kinase) (RLSK) 863 96,583 Active site (2); Alternative sequence (1); Binding site (2); Chain (1); Domain (3); Modified residue (14); Nucleotide binding (2); Sequence conflict (3) FUNCTION: Serine/threonine-protein kinase that is required for the mitogen or stress-induced phosphorylation of the transcription factors CREB1 and ATF1 and for the regulation of the transcription factors RELA, STAT3 and ETV1/ER81, and that contributes to gene activation by histone phosphorylation and functions in the regulation of inflammatory genes (By similarity)(PubMed:11553624, PubMed:11909979, PubMed:16806820). Phosphorylates CREB1 and ATF1 in response to mitogenic or stress stimuli such as UV-C irradiation, epidermal growth factor (EGF) and anisomycin (PubMed:11909979). Plays an essential role in the control of RELA transcriptional activity in response to TNF and upon glucocorticoid, associates in the cytoplasm with the glucocorticoid receptor NR3C1 and contributes to RELA inhibition and repression of inflammatory gene expression (PubMed:12628924, PubMed:16806820). In skeletal myoblasts is required for phosphorylation of RELA at 'Ser-276' during oxidative stress (PubMed:12628924). In erythropoietin-stimulated cells, is necessary for the 'Ser-727' phosphorylation of STAT3 and regulation of its transcriptional potential (PubMed:11553624). Phosphorylates ETV1/ER81 at 'Ser-191' and 'Ser-216', and thereby regulates its ability to stimulate transcription, which may be important during development and breast tumor formation (By similarity). Directly represses transcription via phosphorylation of 'Ser-1' of histone H2A (By similarity). Phosphorylates 'Ser-10' of histone H3 in response to mitogenics, stress stimuli and EGF, which results in the transcriptional activation of several immediate early genes, including proto-oncogenes c-fos/FOS and c-jun/JUN (PubMed:15870105, PubMed:16517600). May also phosphorylate 'Ser-28' of histone H3 (PubMed:11441012, PubMed:15870105). Mediates the mitogen- and stress-induced phosphorylation of high mobility group protein 1 (HMGN1/HMG14) (By similarity). In lipopolysaccharide-stimulated primary macrophages, acts downstream of the Toll-like receptor TLR4 to limit the production of pro-inflammatory cytokines (PubMed:18690222). Functions probably by inducing transcription of the MAP kinase phosphatase DUSP1 and the anti-inflammatory cytokine interleukin 10 (IL10), via CREB1 and ATF1 transcription factors (PubMed:18690222). Plays a role in neuronal cell death by mediating the downstream effects of excitotoxic injury (PubMed:12807421). Phosphorylates TRIM7 at 'Ser-106' in response to growth factor signaling via the MEK/ERK pathway, thereby stimulating its ubiquitin ligase activity (By similarity). {ECO:0000250|UniProtKB:O75582, ECO:0000269|PubMed:11441012, ECO:0000269|PubMed:11553624, ECO:0000269|PubMed:11909979, ECO:0000269|PubMed:12628924, ECO:0000269|PubMed:12807421, ECO:0000269|PubMed:15870105, ECO:0000269|PubMed:16517600, ECO:0000269|PubMed:16806820, ECO:0000269|PubMed:18690222}. PTM: Ser-375 and Thr-645 phosphorylation is required for kinase activity. Ser-375 and Ser-211 are autophosphorylated by the C-terminal kinase domain, and their phosphorylation is essential for the catalytic activity of the N-terminal kinase domain. Phosphorylated at Ser-359, Thr-645 and Thr-764 by MAPK1/ERK2, MAPK3/ERK1 and MAPK14/p38-alpha. Autophosphorylated at Ser-814, Ser-816 and Ser-822 by the N-terminal kinase domain (By similarity). {ECO:0000250}.; PTM: Ubiquitinated. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Forms a complex with either MAPK1/ERK2 or MAPK3/ERK1 in quiescent cells which transiently dissociates following mitogenic stimulation. Also associates with MAPK14/p38-alpha. Activated RPS6KA5 associates with and phosphorylates the NF-kappa-B p65 subunit RELA. Interacts with CREBBP and EP300 (By similarity). {ECO:0000250}. +Q7TPS0 KS6A6_MOUSE Ribosomal protein S6 kinase alpha-6 (S6K-alpha-6) (EC 2.7.11.1) 764 86,571 Active site (2); Alternative sequence (2); Binding site (2); Chain (1); Domain (3); Frameshift (1); Modified residue (4); Nucleotide binding (2); Sequence conflict (6) FUNCTION: Constitutively active serine/threonine-protein kinase that exhibits growth-factor-independent kinase activity and that may participate in p53/TP53-dependent cell growth arrest signaling and play an inhibitory role during embryogenesis. {ECO:0000269|PubMed:15121846}. PTM: Phosphorylated at Ser-252, Ser-392, and Ser-409 in serum-starved cells. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol. Nucleus. Note=Predominantly cytosolic. {ECO:0000250}. SUBUNIT: Forms a complex with MAPK3/ERK1 but not with MAPK9 or MAPK14 in serum-starved cells. {ECO:0000250}. +Q9Z1M4 KS6B2_MOUSE Ribosomal protein S6 kinase beta-2 (S6K-beta-2) (S6K2) (EC 2.7.11.1) (70 kDa ribosomal protein S6 kinase 2) (p70 ribosomal S6 kinase beta) (p70 S6 kinase beta) (p70 S6K-beta) (p70 S6KB) 485 53,538 Active site (1); Binding site (1); Chain (1); Compositional bias (1); Domain (2); Modified residue (5); Motif (1); Nucleotide binding (1) FUNCTION: Phosphorylates specifically ribosomal protein S6. PTM: Phosphorylated and activated by MTOR. Phosphorylation by PKC within the NLS in response to mitogenic stimuli causes cytoplasmic retention. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. +P48025 KSYK_MOUSE Tyrosine-protein kinase SYK (EC 2.7.10.2) (Spleen tyrosine kinase) 629 71,376 Active site (1); Beta strand (1); Binding site (1); Chain (1); Domain (3); Modified residue (32); Mutagenesis (2); Nucleotide binding (1); Region (2); Sequence conflict (2) FUNCTION: Non-receptor tyrosine kinase which mediates signal transduction downstream of a variety of transmembrane receptors including classical immunoreceptors like the B-cell receptor (BCR). Regulates several biological processes including innate and adaptive immunity, cell adhesion, osteoclast maturation, platelet activation and vascular development. Assembles into signaling complexes with activated receptors at the plasma membrane via interaction between its SH2 domains and the receptor tyrosine-phosphorylated ITAM domains. The association with the receptor can also be indirect and mediated by adapter proteins containing ITAM or partial hemITAM domains. The phosphorylation of the ITAM domains is generally mediated by SRC subfamily kinases upon engagement of the receptor. More rarely signal transduction via SYK could be ITAM-independent. Direct downstream effectors phosphorylated by SYK include VAV1, PLCG1, PI-3-kinase, LCP2 and BLNK. Initially identified as essential in B-cell receptor (BCR) signaling, it is necessary for the maturation of B-cells most probably at the pro-B to pre-B transition. Activated upon BCR engagement, it phosphorylates and activates BLNK an adapter linking the activated BCR to downstream signaling adapters and effectors. It also phosphorylates and activates PLCG1 and the PKC signaling pathway. It also phosphorylates BTK and regulates its activity in B-cell antigen receptor (BCR)-coupled signaling. In addition to its function downstream of BCR plays also a role in T-cell receptor signaling. Plays also a crucial role in the innate immune response to fungal, bacterial and viral pathogens. It is for instance activated by the membrane lectin CLEC7A. Upon stimulation by fungal proteins, CLEC7A together with SYK activates immune cells inducing the production of ROS. Also activates the inflammasome and NF-kappa-B-mediated transcription of chemokines and cytokines in presence of pathogens. Regulates neutrophil degranulation and phagocytosis through activation of the MAPK signaling cascade. Also mediates the activation of dendritic cells by cell necrosis stimuli. Also involved in mast cells activation. Involved in interleukin-3/IL3-mediated signaling pathway in basophils (PubMed:19098920). Also functions downstream of receptors mediating cell adhesion. Relays for instance, integrin-mediated neutrophils and macrophages activation and P-selectin receptor/SELPG-mediated recruitment of leukocytes to inflammatory loci. Plays also a role in non-immune processes. It is for instance involved in vascular development where it may regulate blood and lymphatic vascular separation. It is also required for osteoclast development and function. Functions in the activation of platelets by collagen, mediating PLCG2 phosphorylation and activation. May be coupled to the collagen receptor by the ITAM domain-containing FCER1G. Also activated by the membrane lectin CLEC1B that is required for activation of platelets by PDPN/podoplanin. Involved in platelet adhesion being activated by ITGB3 engaged by fibrinogen. Together with CEACAM20, enhances production of the cytokine CXCL8/IL-8 via the NFKB pathway and may thus have a role in the intestinal immune response (PubMed:26195794). {ECO:0000269|PubMed:11672534, ECO:0000269|PubMed:11940607, ECO:0000269|PubMed:12522250, ECO:0000269|PubMed:15845454, ECO:0000269|PubMed:15956283, ECO:0000269|PubMed:16174766, ECO:0000269|PubMed:17086186, ECO:0000269|PubMed:17353363, ECO:0000269|PubMed:19098920, ECO:0000269|PubMed:19124738, ECO:0000269|PubMed:19219027, ECO:0000269|PubMed:19339971, ECO:0000269|PubMed:19797524, ECO:0000269|PubMed:26195794, ECO:0000269|PubMed:9171347}. PTM: Autophosphorylated. Phosphorylated on tyrosine residues by LYN following receptors engagement. Phosphorylation on Tyr-317 creates a binding site for CBL, an adapter protein that serves as a negative regulator of BCR-stimulated calcium ion signaling. Phosphorylation at Tyr-342 creates a binding site for VAV1 (By similarity). Phosphorylation on Tyr-342 and Tyr-346 enhances the phosphorylation and activation of phospholipase C-gamma and the early phase of calcium ion mobilization via a phosphoinositide 3-kinase-independent pathway (By similarity). Phosphorylation on Ser-291 is very common, it peaks 5 minutes after BCR stimulation, and creates a binding site for YWHAG (By similarity). Phosphorylation at Tyr-624 creates a binding site for BLNK (By similarity). Dephosphorylated by PTPN6 (By similarity). {ECO:0000250}.; PTM: Ubiquitinated by CBLB after BCR activation; which promotes proteasomal degradation. {ECO:0000269|PubMed:12771181}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:15845454}. Cytoplasm, cytosol {ECO:0000305|PubMed:15845454}. Cytoplasmic vesicle, phagosome {ECO:0000269|PubMed:15845454}. SUBUNIT: Interacts with LYN; phosphorylates SYK. Interacts with RHOH (phosphorylated); regulates mast cells activation. Interacts with NFAM1 (phosphorylated); probably involved in BCR signaling. Interacts with VAV1 (via SH2 domain); phosphorylates VAV1 upon BCR activation (By similarity). Interacts with GAB2 (phosphorylated); probably involved in IgE Fc receptor signaling. Interacts (via its SH2 domains) with CD79A (via its phosphorylated ITAM domain); the interaction stimulates SYK autophosphorylation and activation. Interacts (via SH2 domains) with FCER1G (via ITAM domain); activates SYK and mediates neutrophils and macrophages integrin-mediated activation. Interaction with FCER1G in basophils triggers IL3-induced IL4 production (PubMed:19098920). Interacts with ITGB2 and FGR; involved in ITGB2 downstream signaling. Interacts with ITGB3; upon activation by ITGB3 promotes platelet adhesion (By similarity). Interacts (via SH2 domains) with TYROBP (via ITAM domain); involved in neutrophils and macrophages integrin-mediated activation. Interacts with MSN and SELPLG; mediates the selectin-dependent activation of SYK by SELPLG (By similarity). Interacts with BLNK (via SH2 domain). Interacts (via the second SH2 domain) with USP25 (via C-terminus); phosphorylates USP25 and regulates USP25 intracellular levels (By similarity). Interacts (via SH2 domains) with CLEC1B (dimer) (By similarity). Interacts with CLEC7A; participates in leukocyte activation in presence of fungal pathogens. Interacts (phosphorylated) with SLA; may regulate SYK through CBL recruitment (By similarity). Interacts with YWHAG; attenuates BCR-induced membrane translocation and activation of SYK (By similarity). Interacts (via SH2 domains) with GCSAM; the interaction increases after B-cell receptor stimulation, resulting in enhanced SYK autophosphorylation and activity (By similarity). Interacts with TNS2; leading to the phosphorylation of SYK (By similarity). Interacts with FLNA (via filamin repeat 5); docks SYK to the plasma membrane (By similarity). Interacts with CEACAM1; lipopolysaccharide activated neutrophils induce phosphorylation of SYK resulting in the formation of a complex including TLR4 and the phosphorylated form of SYK and CEACAM1, which in turn, recruits PTPN6 that dephosphorylates SYK, reducing the production of reactive oxygen species (ROS) and lysosome disruption, leading to a reduction of the inflammasome activity (PubMed:22496641). Interacts (via SH2 domains) with CEACAM20 (phosphorylated form); the interaction further enhances CEACAM20 phosphorylation (PubMed:26195794). {ECO:0000250|UniProtKB:P43405, ECO:0000269|PubMed:19098920, ECO:0000269|PubMed:22496641, ECO:0000269|PubMed:26195794}. DOMAIN: The SH2 domains mediate the interaction of SYK with the phosphorylated ITAM domains of transmembrane proteins. Some proteins like CLEC1B have a partial ITAM domain (also called hemITAM) containing a single YxxL motif. The interaction with SYK requires CLEC1B homodimerization (By similarity). {ECO:0000250}. +Q8K274 KT3K_MOUSE Ketosamine-3-kinase (EC 2.7.1.-) (Fructosamine-3-kinase-related protein) 309 34,468 Chain (1); Modified residue (1); Sequence conflict (1) FUNCTION: Phosphorylates psicosamines and ribulosamines, but not fructosamines, on the third carbon of the sugar moiety. Protein-bound psicosamine 3-phosphates and ribulosamine 3-phosphates are unstable and decompose under physiological conditions. Thus phosphorylation leads to deglycation. {ECO:0000269|PubMed:14633848}. +Q5RL79 KTAP2_MOUSE Keratinocyte-associated protein 2 (KCP-2) (Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit KCP2) (Oligosaccharyl transferase subunit KCP2) 136 14,675 Chain (1); Erroneous initiation (1); Modified residue (1); Motif (1); Topological domain (4); Transmembrane (3) TRANSMEM 6 23 Helical. {ECO:0000255}.; TRANSMEM 35 55 Helical. {ECO:0000255}.; TRANSMEM 76 108 Helical. {ECO:0000255}. TOPO_DOM 1 5 Lumenal. {ECO:0000255}.; TOPO_DOM 24 34 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 56 75 Lumenal. {ECO:0000255}.; TOPO_DOM 109 136 Cytoplasmic. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. May be involved in N-glycosylation of APP (amyloid-beta precursor protein). Can modulate gamma-secretase cleavage of APP by enhancing endoprotelysis of PSEN1. {ECO:0000250|UniProtKB:Q8N6L1}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8N6L1}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8N6L1}. SUBUNIT: Component of the oligosaccharyltransferase (OST) complex. OST exists in two different complex forms which contain common core subunits RPN1, RPN2, OST48, OST4, DAD1 and TMEM258, either STT3A or STT3B as catalytic subunits, and form-specific accessory subunits. STT3A complex assembly occurs through the formation of 3 subcomplexes. Subcomplex 1 contains RPN1 and TMEM258, subcomplex 2 contains the STT3A-specific subunits STT3A, DC2/OSTC, and KCP2 as well as the core subunit OST4, and subcomplex 3 contains RPN2, DAD1, and OST48. The STT3A complex can form stable complexes with the Sec61 complex or with both the Sec61 and TRAP complexes (By similarity). Interacts with PSEN1 and NCSTN; indicative for an association with the gamma-secretase complex (By similarity). {ECO:0000250|UniProtKB:P86229, ECO:0000250|UniProtKB:Q8N6L1}. +Q9CWJ3 KTBL1_MOUSE KATNB1-like protein 1 (Katanin p80 subunit B-like 1) 299 34,035 Chain (1); Modified residue (1); Motif (1) FUNCTION: Regulates microtubule-severing activity of KATNAL1 in a concentration-dependent manner in vitro. {ECO:0000250|UniProtKB:Q9H079}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H079}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q9H079}. Note=Localizes to the spindle poles only during mitosis. Sequestered to the nucleus during interphase. {ECO:0000250|UniProtKB:Q9H079}. SUBUNIT: Interacts with KATNA1 and KATNAL1; these interactions are competed by KATNB1 which has a higher affinity for them. {ECO:0000250|UniProtKB:Q9H079}. +Q80SY4 MIB1_MOUSE E3 ubiquitin-protein ligase MIB1 (EC 2.3.2.27) (DAPK-interacting protein 1) (DIP-1) (Mind bomb homolog 1) (RING-type E3 ubiquitin transferase MIB1) 1006 110,088 Chain (1); Coiled coil (1); Domain (2); Erroneous initiation (2); Modified residue (1); Repeat (9); Sequence caution (2); Sequence conflict (3); Zinc finger (4) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination of Delta receptors, which act as ligands of Notch proteins. Positively regulates the Delta-mediated Notch signaling by ubiquitinating the intracellular domain of Delta, leading to endocytosis of Delta receptors. Involved in ubiquitination of centriolar satellite CEP131, CEP290 and PCM1 proteins and hence inhibits primary cilium formation in proliferating cells. Mediates 'Lys-63'-linked polyubiquitination of TBK1, which probably participates in kinase activation (By similarity). Probably mediates ubiquitination and subsequent proteasomal degradation of DAPK1, thereby antagonizing anti-apoptotic effects of DAPK1 to promote TNF-induced apoptosis. {ECO:0000250, ECO:0000269|PubMed:12351649}. PTM: Ubiquitinated; this modification is inhibited in response to cellular stress, such as ultraviolet light (UV) radiation or heat shock (By similarity). Ubiquitinated; possibly via autoubiquitination. {ECO:0000250, ECO:0000269|PubMed:12351649, ECO:0000269|PubMed:15824097}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000250}. Cytoplasm. Cell membrane. Note=Displaced from centriolar satellites in response to cellular stress, such as ultraviolet light (UV) radiation or heat shock (By similarity). Localizes to the plasma membrane. {ECO:0000250}. SUBUNIT: Interacts with CEP131 and PCM1. {ECO:0000250}. TISSUE SPECIFICITY: Detected in all tissues tested. Present in embryo, embryonic stem cells, bladder, skeletal muscle, bladder, uterus, testis, stomach, colon, ileum, trachea, lung, aorta, kidney, spleen, liver and vas deferens (at protein level). Highly expressed in testis. {ECO:0000269|PubMed:12351649, ECO:0000269|PubMed:15824097}. +Q8R516 MIB2_MOUSE E3 ubiquitin-protein ligase MIB2 (EC 2.3.2.27) (Dystrophin-like protein) (Dyslike) (Mind bomb homolog 2) (Mind bomb-2) (RING-type E3 ubiquitin transferase MIB2) (Skeletrophin) 973 105,961 Alternative sequence (5); Chain (1); Domain (2); Frameshift (2); Modified residue (1); Mutagenesis (2); Repeat (9); Sequence conflict (14); Zinc finger (3) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination of Delta receptors, which act as ligands of Notch proteins. Positively regulates the Delta-mediated Notch signaling by ubiquitinating the intracellular domain of Delta, leading to endocytosis of Delta receptors. {ECO:0000269|PubMed:15824097}. PTM: Ubiquitinated. Possibly via autoubiquitination. {ECO:0000269|PubMed:15824097}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15824097}. Endosome {ECO:0000269|PubMed:15824097}. Note=Colocalizes with endosomal compartments. SUBUNIT: Interacts with actin monomer. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in brain, heart, liver and kidney. {ECO:0000269|PubMed:15824097}. +Q78IK4 MIC27_MOUSE MICOS complex subunit Mic27 (Apolipoprotein O-like) (Protein FAM121A) 265 29,261 Chain (1); Modified residue (1); Topological domain (3); Transit peptide (1); Transmembrane (2) TRANSMEM 111 129 Helical. {ECO:0000255}.; TRANSMEM 138 155 Helical. {ECO:0000255}. TOPO_DOM 28 110 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 130 137 Mitochondrial matrix. {ECO:0000255}.; TOPO_DOM 156 265 Mitochondrial intermembrane. {ECO:0000255}. FUNCTION: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. Specifically binds to cardiolipin (in vitro) but not to the precursor lipid phosphatidylglycerol. Plays a crucial role in crista junction formation and mitochondrial function. {ECO:0000250|UniProtKB:Q6UXV4}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q6UXV4}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q6UXV4}. Mitochondrion {ECO:0000250|UniProtKB:Q6UXV4}. SUBUNIT: Component of the mitochondrial contact site and cristae organizing system (MICOS) complex, composed of at least MINOS1/MIC10, CHCHD3/MIC19, CHCHD6/MIC25, APOOL/MIC27, IMMT/MIC60, APOO/MIC23/MIC26 and QIL1/MIC13. This complex was also known under the names MINOS or MitOS complex. The MICOS complex associates with mitochondrial outer membrane proteins SAMM50, MTX1 and MTX2 (together described as components of the mitochondrial outer membrane sorting assembly machinery (SAM) complex) and DNAJC11, mitochondrial inner membrane protein TMEM11 and with HSPA9. The MICOS and SAM complexes together with DNAJC11 are part of a large protein complex spanning both membranes termed the mitochondrial intermembrane space bridging (MIB) complex. Interacts with MINOS1/MIC10, IMMT/MIC60 and APOO/MIC23/MIC26. {ECO:0000250|UniProtKB:Q6UXV4}. +Q8CAQ8 MIC60_MOUSE MICOS complex subunit Mic60 (Mitochondrial inner membrane protein) (Mitofilin) 757 83,900 Alternative sequence (6); Chain (1); Coiled coil (3); Erroneous initiation (1); Frameshift (1); Modified residue (9); Sequence conflict (2); Topological domain (2); Transit peptide (1); Transmembrane (1) TRANSMEM 46 65 Helical. {ECO:0000255}. TOPO_DOM 34 45 Mitochondrial matrix. {ECO:0000255}.; TOPO_DOM 66 757 Mitochondrial intermembrane. {ECO:0000255}. FUNCTION: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. Plays an important role in the maintenance of the MICOS complex stability and the mitochondrial cristae morphology. {ECO:0000250|UniProtKB:Q16891}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q16891}; Single-pass membrane protein {ECO:0000255}. Mitochondrion {ECO:0000250|UniProtKB:Q16891}. SUBUNIT: Component of the mitochondrial contact site and cristae organizing system (MICOS) complex, composed of at least MINOS1/MIC10, CHCHD3/MIC19, CHCHD6/MIC25, APOOL/MIC27, IMMT/MIC60, APOO/MIC23/MIC26 and QIL1/MIC13. This complex was also known under the names MINOS or MitOS complex. The MICOS complex associates with mitochondrial outer membrane proteins SAMM50, MTX1 and MTX2 (together described as components of the mitochondrial outer membrane sorting assembly machinery (SAM) complex) and DNAJC11, mitochondrial inner membrane protein TMEM11 and with HSPA9. The MICOS and SAM complexes together with DNAJC11 are part of a large protein complex spanning both membranes termed the mitochondrial intermembrane space bridging (MIB) complex. Interacts with QIL1/MIC13, MINOS1/MIC10, CHCHD3/MIC19, CHCHD6/MIC25, SAMM50 and TMEM11. Interacts with APOO/MIC23/MIC26 and APOOL/MIC27 (By similarity). Interacts with HSPA1A/HSPA1B and OPA1, preferentially with the soluble OPA1 form. {ECO:0000250|UniProtKB:Q16891, ECO:0000269|PubMed:21081504}. +Q8CJ19 MICA3_MOUSE [F-actin]-monooxygenase MICAL3 (EC 1.14.13.225) (Molecule interacting with CasL protein 3) (MICAL-3) 1993 223,721 Alternative sequence (6); Binding site (4); Chain (1); Coiled coil (1); Compositional bias (1); Domain (3); Erroneous initiation (1); Metal binding (8); Modified residue (20); Nucleotide binding (2); Region (1); Sequence conflict (2) FUNCTION: Monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). Seems to act as Rab effector protein and play a role in vesicle trafficking. Involved in exocytic vesicles tethering and fusion: the monooxygenase activity is required for this process and implicates RAB8A associated with exocytotic vesicles. Required for cytokinesis. Contributes to stabilization and/or maturation of the intercellular bridge independently of its monooxygenase activity. Promotes recruitment of Rab8 and ERC1 to the intercellular bridge, and together these proteins are proposed to function in timely abscission. {ECO:0000250|UniProtKB:Q7RTP6}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q7RTP6}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q7RTP6}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q7RTP6}. Nucleus {ECO:0000250|UniProtKB:Q7RTP6}. Midbody {ECO:0000250|UniProtKB:Q7RTP6}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q7RTP6}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q7RTP6}. Note=Mainly localizes in the nucleus. {ECO:0000250|UniProtKB:Q7RTP6}. SUBUNIT: Interacts with RAB1B, RAB8A, RAB10, RAB13 and RAB15 (in their GTP-bound forms); binding to RAB1B is of low affinity compared to other Rab proteins; at least in case of RAB8A can bind 2 molecules of RAB8A simultaneously through a high and a low affinity binding site, respectively. Interacts with ERC1 and RAB8A; may bridge ERC1 with RAB8A. Interacts with KIF23 and ERC1; enhances the interaction between KIF23 and ERC1. Interacts with NINL. {ECO:0000250|UniProtKB:Q7RTP6}. DOMAIN: The bivalent Mical/EHBP Rab binding (bMERB) domain, mediates binding to predominantly Rab8, Rab10, Rab10, Rab13 and Rab15 (in their GTP-bound forms). {ECO:0000250|UniProtKB:Q7RTP6}. +Q8CD10 MICU2_MOUSE Calcium uptake protein 2, mitochondrial (EF-hand domain-containing family member A1) 432 49,476 Chain (1); Compositional bias (1); Disulfide bond (1); Domain (4); Modified residue (1); Mutagenesis (2); Sequence conflict (2); Transit peptide (1) FUNCTION: Key regulator of mitochondrial calcium uniporter (MCU) required to limit calcium uptake by MCU when cytoplasmic calcium is low (PubMed:23409044, PubMed:24560927). MICU1 and MICU2 form a disulfide-linked heterodimer that stimulate and inhibit MCU activity, depending on the concentration of calcium (PubMed:24560927). MICU2 acts as a gatekeeper of MCU that senses calcium level via its EF-hand domains: prevents channel opening at resting Ca(2+), avoiding energy dissipation and cell-death triggering (PubMed:24560927). {ECO:0000269|PubMed:23409044, ECO:0000269|PubMed:24560927}. SUBCELLULAR LOCATION: Mitochondrion intermembrane space {ECO:0000269|PubMed:23409044}. SUBUNIT: Heterodimer; disulfide-linked; heterodimerizes with MICU1 (PubMed:23409044, PubMed:24560927). Interacts with MCU (PubMed:23409044). The heterodimer formed with MICU1 associates with MCU at low calcium concentration and dissociates from MCU at high calcium level (By similarity). Component of the uniplex complex, composed of MCU, MCUB, MICU1, MICU2 and EMRE/SMDT1. {ECO:0000250|UniProtKB:Q8IYU8, ECO:0000269|PubMed:23409044, ECO:0000269|PubMed:24560927}. DOMAIN: The EF-hand domains have high affinity for calcium and act as sensors of mitochondrial matrix calcium levels (PubMed:24560927). It is unclear which EF-hand binds calcium as none of the 4 EF-hand domains seem to contain a canonical calcium-binding site. {ECO:0000269|PubMed:24560927}. TISSUE SPECIFICITY: Predominantly expressed in stomach, intestine, skeletal muscle, kidney, heart, testis, prostate and uterus. {ECO:0000269|PubMed:23409044}. +Q3UHF3 MIER3_MOUSE Mesoderm induction early response protein 3 (Mi-er3) 551 61,521 Alternative sequence (2); Chain (1); Domain (2); Erroneous initiation (1); Modified residue (7); Sequence conflict (3) FUNCTION: Transcriptional repressor. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00512, ECO:0000255|PROSITE-ProRule:PRU00624}. +P34884 MIF_MOUSE Macrophage migration inhibitory factor (MIF) (EC 5.3.2.1) (Delayed early response protein 6) (DER6) (Glycosylation-inhibiting factor) (GIF) (L-dopachrome isomerase) (L-dopachrome tautomerase) (EC 5.3.3.12) (Phenylpyruvate tautomerase) 115 12,504 Active site (1); Beta strand (6); Binding site (3); Chain (1); Helix (6); Initiator methionine (1); Modified residue (2); Mutagenesis (1) FUNCTION: Pro-inflammatory cytokine. Involved in the innate immune response to bacterial pathogens. The expression of MIF at sites of inflammation suggests a role as mediator in regulating the function of macrophages in host defense. Counteracts the anti-inflammatory activity of glucocorticoids. Has phenylpyruvate tautomerase and dopachrome tautomerase activity (in vitro), but the physiological substrate is not known. It is not clear whether the tautomerase activity has any physiological relevance, and whether it is important for cytokine activity (By similarity). {ECO:0000250|UniProtKB:P14174}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17526494, ECO:0000269|PubMed:8234256}. Cytoplasm {ECO:0000250|UniProtKB:P14174}. Note=Does not have a cleavable signal sequence and is secreted via a specialized, non-classical pathway. Secreted by macrophages upon stimulation by bacterial lipopolysaccharide (LPS), or by M.tuberculosis antigens (By similarity). {ECO:0000250|UniProtKB:P14174}. SUBUNIT: Homotrimer. Interacts with BNIPL (By similarity). Interacts with the CD74 extracellular domain. Interacts with COPS5 and with the CXCR2 extracellular domain. {ECO:0000250|UniProtKB:P14174, ECO:0000269|PubMed:16780921, ECO:0000269|PubMed:19188446}. +Q4QQM5 MIGA1_MOUSE Mitoguardin 1 (Protein FAM73A) 600 67,536 Alternative sequence (3); Chain (1); Compositional bias (1); Frameshift (1); Modified residue (2); Sequence conflict (1); Transmembrane (2) TRANSMEM 15 32 Helical. {ECO:0000255}.; TRANSMEM 38 58 Helical. {ECO:0000255}. FUNCTION: Regulator of mitochondrial fusion (PubMed:26711011). Acts by forming homo- and heterodimers at the mitochondrial outer membrane and facilitating the formation of PLD6/MitoPLD dimers. May act by regulating phospholipid metabolism via PLD6/MitoPLD (By similarity). {ECO:0000250|UniProtKB:Q8NAN2, ECO:0000269|PubMed:26711011}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q8NAN2}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Homodimer and heterodimer; forms heterodimers with MIGA2. Interacts with PLD6/MitoPLD. {ECO:0000250|UniProtKB:Q8NAN2}. +Q8BK03 MIGA2_MOUSE Mitoguardin 2 (Protein FAM73B) 593 65,548 Alternative sequence (2); Chain (1); Compositional bias (2); Erroneous initiation (1); Modified residue (7); Transmembrane (2) TRANSMEM 11 31 Helical. {ECO:0000255}.; TRANSMEM 42 62 Helical. {ECO:0000255}. FUNCTION: Regulator of mitochondrial fusion (PubMed:26711011). Acts by forming homo- and heterodimers at the mitochondrial outer membrane and facilitating the formation of PLD6/MitoPLD dimers. May act by regulating phospholipid metabolism via PLD6/MitoPLD (By similarity). {ECO:0000250|UniProtKB:Q7L4E1, ECO:0000269|PubMed:26711011}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q7L4E1}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Homodimer and heterodimer; forms heterodimers with MIGA1. Interacts with PLD6/MitoPLD. {ECO:0000250|UniProtKB:Q7L4E1}. +A2A7Y5 MIIP_MOUSE Migration and invasion-inhibitory protein (Invasion-inhibitory protein 45) (IIp45) 387 42,828 Alternative sequence (1); Chain (1); Erroneous initiation (2); Modified residue (1); Sequence caution (1) FUNCTION: Inhibits glioma cells invasion and down-regulates adhesion- and motility-associated genes such as NFKB2 and ICAM1. Exhibits opposing effects to IGFBP2 on cell invasion (By similarity). {ECO:0000250}. SUBUNIT: Interacts with IGFBP2. {ECO:0000250}. +Q62000 MIME_MOUSE Mimecan (Osteoglycin) 298 34,012 Chain (1); Compositional bias (1); Disulfide bond (1); Glycosylation (1); Repeat (7); Signal peptide (1) FUNCTION: Induces bone formation in conjunction with TGF-beta-1 or TGF-beta-2. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. +Q9QZ26 KCNE5_MOUSE Potassium voltage-gated channel subfamily E regulatory beta subunit 5 (MinK-like protein) (Potassium voltage-gated channel subfamily E member 1-like protein) 143 14,968 Chain (1); Glycosylation (2); Topological domain (1); Transmembrane (1) TRANSMEM 61 81 Helical. {ECO:0000255}. TOPO_DOM 82 143 Cytoplasmic. {ECO:0000255}. FUNCTION: Potassium channel ancillary subunit that is essential for generation of some native K(+) currents by virtue of formation of heteromeric ion channel complex with voltage-gated potassium (Kv) channel pore-forming alpha subunits. Functions as an inhibitory beta-subunit of the repolarizing cardiac potassium ion channel KCNQ1. {ECO:0000250|UniProtKB:Q9UJ90}. SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9UJ90}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9UJ90}. SUBUNIT: Interacts with KCNQ1; impairs KCNQ1 localization in lipid rafts and only conducts current upon strong and continued depolarization. {ECO:0000250|UniProtKB:Q9UJ90}. TISSUE SPECIFICITY: Detected in embryonal dorsal root and nerve ganglia, in the somites and in myoepicardial layer of the developing heart wall. Detected at lower levels in the central nervous system (CNS) and in developing limb. {ECO:0000269|PubMed:10493825}. +Q50H33 KCTD8_MOUSE BTB/POZ domain-containing protein KCTD8 476 52,768 Alternative sequence (2); Chain (1); Domain (1); Modified residue (3); Sequence conflict (7) FUNCTION: Auxiliary subunit of GABA-B receptors that determine the pharmacology and kinetics of the receptor response. Increases agonist potency and markedly alter the G-protein signaling of the receptors by accelerating onset and promoting desensitization. {ECO:0000269|PubMed:20400944}. SUBCELLULAR LOCATION: Cell junction, synapse, presynaptic cell membrane {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000250}. SUBUNIT: Interacts as a tetramer with GABRB1 and GABRB2. {ECO:0000269|PubMed:20400944}. +Q9Z351 KCNQ2_MOUSE Potassium voltage-gated channel subfamily KQT member 2 (KQT-like 2) (Potassium channel subunit alpha KvLQT2) (Voltage-gated potassium channel subunit Kv7.2) 759 84,450 Alternative sequence (19); Chain (1); Intramembrane (1); Modified residue (10); Motif (1); Mutagenesis (3); Region (1); Sequence conflict (5); Topological domain (8); Transmembrane (6) INTRAMEM 265 285 Pore-forming; Name=Segment H5. {ECO:0000255}. TRANSMEM 92 112 Helical; Name=Segment S1. {ECO:0000255}.; TRANSMEM 123 143 Helical; Name=Segment S2. {ECO:0000255}.; TRANSMEM 167 187 Helical; Name=Segment S3. {ECO:0000255}.; TRANSMEM 198 221 Helical; Voltage-sensor; Name=Segment S4. {ECO:0000255}.; TRANSMEM 232 252 Helical; Name=Segment S5. {ECO:0000255}.; TRANSMEM 292 312 Helical; Name=Segment S6. {ECO:0000255}. TOPO_DOM 1 91 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 113 122 Extracellular. {ECO:0000255}.; TOPO_DOM 144 166 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 188 197 Extracellular. {ECO:0000255}.; TOPO_DOM 222 231 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 253 264 Extracellular. {ECO:0000255}.; TOPO_DOM 286 291 Extracellular. {ECO:0000255}.; TOPO_DOM 313 759 Cytoplasmic. {ECO:0000255}. FUNCTION: Associates with KCNQ3 to form a potassium channel with essentially identical properties to the channel underlying the native M-current, a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons as well as the responsiveness to synaptic inputs. Therefore, it is important in the regulation of neuronal excitability. {ECO:0000269|PubMed:12223552}. PTM: KCNQ2/KCNQ3 heteromeric current can be increased by intracellular cyclic AMP, an effect that depends on phosphorylation of Ser-52 in the N-terminal region. {ECO:0000250|UniProtKB:O43526}.; PTM: KCNQ2/KCNQ3 are ubiquitinated by NEDD4L. Ubiquitination leads to protein degradation. Degradation induced by NEDD4L is inhibited by USP36. {ECO:0000250|UniProtKB:O43526}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12223552}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Heterotetramer with KCNQ3; form the heterotetrameric M potassium channel (By similarity). Interacts with calmodulin; the interaction is calcium-independent, constitutive and participates to the proper assembly of a functional heterotetrameric M channel (PubMed:12223552). May associate with KCNE2 (By similarity). Interacts with IQCJ-SCHIP1 (PubMed:27979964). {ECO:0000250|UniProtKB:O43526, ECO:0000269|PubMed:12223552, ECO:0000269|PubMed:27979964}. DOMAIN: The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position. {ECO:0000250}. TISSUE SPECIFICITY: Exclusively expressed in the brain. Expressed in every neuron-containing regions of the central nervous system examined, such as the cerebellum, cerebral cortex, occipital pole, substantia nigra, amygdala, caudate nucleus, hippocampus and thalamus. Also detected in the cochlea. +Q8C0N1 KIF2B_MOUSE Kinesin-like protein KIF2B 668 75,469 Chain (1); Coiled coil (2); Domain (1); Modified residue (2); Nucleotide binding (1) FUNCTION: Plus end-directed microtubule-dependent motor required for spindle assembly and chromosome movement during mitosis. Has microtubule depolymerization activity. Plays a role in chromosome congression. {ECO:0000250|UniProtKB:Q8N4N8}. PTM: Phosphorylation at Thr-125 by PLK1 is required for activity in the correction of kinetochore-microtubules attachment errors, while phosphorylation at Ser-204 also by PLK1 is required for the kinetochore localization and activity in prometaphase. {ECO:0000250|UniProtKB:Q8N4N8}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q8N4N8}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q8N4N8}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q8N4N8}. Note=Association with kinetochore is transient. {ECO:0000250|UniProtKB:Q8N4N8}. +Q9R088 KITM_MOUSE Thymidine kinase 2, mitochondrial (EC 2.7.1.21) (Mt-TK) 270 31,209 Active site (1); Binding site (5); Chain (1); Nucleotide binding (1); Sequence conflict (4); Transit peptide (1) FUNCTION: Phosphorylates thymidine, deoxycytidine, and deoxyuridine in the mitochondrial matrix. In non-replicating cells, where cytosolic dNTP synthesis is down-regulated, mtDNA synthesis depends solely on TK2 and DGUOK. Widely used as target of antiviral and chemotherapeutic agents. {ECO:0000250|UniProtKB:O00142}. SUBCELLULAR LOCATION: Mitochondrion. SUBUNIT: Homodimer. TISSUE SPECIFICITY: Found in most tissues; highly expressed in liver. +Q8VBY2 KKCC1_MOUSE Calcium/calmodulin-dependent protein kinase kinase 1 (CaM-KK 1) (CaM-kinase kinase 1) (CaMKK 1) (EC 2.7.11.17) (CaM-kinase IV kinase) (Calcium/calmodulin-dependent protein kinase kinase alpha) (CaM-KK alpha) (CaM-kinase kinase alpha) (CaMKK alpha) 505 55,838 Active site (1); Binding site (1); Chain (1); Domain (1); Modified residue (8); Nucleotide binding (1); Region (3); Sequence conflict (4) FUNCTION: Calcium/calmodulin-dependent protein kinase that belongs to a proposed calcium-triggered signaling cascade involved in a number of cellular processes. Phosphorylates CAMK1, CAMK1D, CAMK1G and CAMK4. Involved in regulating cell apoptosis. Promotes cell survival by phosphorylating AKT1/PKB that inhibits pro-apoptotic BAD/Bcl2-antagonist of cell death. {ECO:0000269|PubMed:12637513}. PTM: Appears to be autophosphorylated in a Ca(2+)/calmodulin-dependent manner. Phosphorylated at multiple sites by PRCAKA/PKA. Phosphorylation of Ser-458 is blocked upon binding to Ca(2+)/calmodulin. In vitro, phosphorylated by CAMK1 and CAMK4 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Interacts with CAMK4 and calmodulin. {ECO:0000250}. DOMAIN: The autoinhibitory domain overlaps with the calmodulin binding region and may be involved in intrasteric autoinhibition.; DOMAIN: The RP domain (arginine/proline-rich) is involved in the recognition of CAMKI and CAMK4 as substrates. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. Differentially expressed in various brain regions. {ECO:0000269|PubMed:12654522}. +Q3UXL4 KIZ_MOUSE Centrosomal protein kizuna (Polo-like kinase 1 substrate 1) 695 76,542 Chain (1); Coiled coil (2); Erroneous gene model prediction (1); Modified residue (4) FUNCTION: Centrosomal protein required for establishing a robust mitotic centrosome architecture that can endure the forces that converge on the centrosomes during spindle formation. Required for stabilizing the expanded pericentriolar material around the centriole. {ECO:0000250|UniProtKB:Q2M2Z5}. PTM: Phosphorylation at Thr-391 by PLK1 is not needed for centrosomal localization or pericentriolar material expansion but is indispensable for spindle-pole stabilization. {ECO:0000250|UniProtKB:Q2M2Z5}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q2M2Z5}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q2M2Z5}. Note=Localizes to centrosomes throughout the cell cycle. After centrosome duplication, it usually remains associated only with the mother centrosome, containing the older mature centriole and particles surrounding it. During prophase, additional particles accumulate around both separating centrosomes. Does not accumulate at the microtubule minus ends, but instead localizes to the centrosomes and centrosome- surrounding area in a microtubule-independent and dependent manner, respectively. {ECO:0000250|UniProtKB:Q2M2Z5}. SUBUNIT: Interacts with AKAP9, CEP72, ODF2, PCNT and TUBGCP2. {ECO:0000250|UniProtKB:Q2M2Z5}. +Q9DBS5 KLC4_MOUSE Kinesin light chain 4 (KLC 4) (Kinesin-like protein 8) 619 68,613 Chain (1); Coiled coil (1); Initiator methionine (1); Modified residue (7); Repeat (7) FUNCTION: Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. The light chain may function in coupling of cargo to the heavy chain or in the modulation of its ATPase activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. SUBUNIT: Oligomeric complex composed of two heavy chains and two light chains. {ECO:0000250}. +Q9CZ49 KLH35_MOUSE Kelch-like protein 35 574 62,372 Chain (1); Domain (2); Repeat (6); Sequence conflict (1) +Q60793 KLF4_MOUSE Krueppel-like factor 4 (Epithelial zinc finger protein EZF) (Gut-enriched krueppel-like factor) 483 51,880 Beta strand (4); Chain (1); Compositional bias (1); Cross-link (1); Erroneous initiation (2); Helix (4); Modified residue (1); Region (2); Sequence conflict (4); Turn (2); Zinc finger (3) FUNCTION: Transcription factor; can act both as activator and as repressor. Binds the 5'-CACCC-3' core sequence. Binds to the promoter region of its own gene and can activate its own transcription. Regulates the expression of key transcription factors during embryonic development. Plays an important role in maintaining embryonic stem cells, and in preventing their differentiation. Required for establishing the barrier function of the skin and for postnatal maturation and maintenance of the ocular surface. Involved in the differentiation of epithelial cells and may also function in skeletal and kidney development. Contributes to the down-regulation of p53/TP53 transcription (By similarity). {ECO:0000250, ECO:0000269|PubMed:10431239, ECO:0000269|PubMed:10556311, ECO:0000269|PubMed:15358627, ECO:0000269|PubMed:16954384, ECO:0000269|PubMed:17060454, ECO:0000269|PubMed:19816951, ECO:0000269|PubMed:20071344}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10431239, ECO:0000269|PubMed:24161396}. SUBUNIT: Interacts with MUC1 (via the C-terminal domain) (By similarity). Interacts with POU5F1/OCT4 and SOX2 (PubMed:19816951). Interacts with MEIS2 isoform MeisD and PBX1 isoform PBX1a (By similarity). Interacts with ZNF296 (PubMed:24161396). {ECO:0000250|UniProtKB:O43474, ECO:0000269|PubMed:19816951, ECO:0000269|PubMed:24161396}. TISSUE SPECIFICITY: Highest expression in the colon. Lower levels in testis, lung and small intestine. +Q8BFQ9 KLH42_MOUSE Kelch-like protein 42 (Cullin-3-binding protein 9) (Ctb9) (Kelch domain-containing protein 5) 493 55,599 Chain (1); Domain (1); Repeat (6) Protein modification; protein ubiquitination. FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex required for mitotic progression and cytokinesis. The BCR(KLHL42) E3 ubiquitin ligase complex mediates the ubiquitination and subsequent degradation of KATNA1. Involved in microtubule dynamics throughout mitosis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Predominantly in mitotic cells. Localized diffusely in the cytoplasm during the interphase. During metaphase is localized throughout the cell and more widely dispersed than the microtubules. In anaphase cells is localized between the two sets of separated chromosomes as well as at the spindle poles (By similarity). During telophase is localized arround the nuclei of the two daughter cells. Not detected at the midbody region during cytokinesis. {ECO:0000250}. SUBUNIT: Component of the BCR(KLHL42) E3 ubiquitin ligase complex, at least composed of CUL3 and KLHL42. Interacts (via the BTB domain) with CUL3. Interacts (via the kelch domains) with KATNA1 (By similarity). {ECO:0000250}. +Q80T74 KLH29_MOUSE Kelch-like protein 29 (Kelch repeat and BTB domain-containing protein 9) 875 94,359 Chain (1); Domain (1); Erroneous initiation (3); Repeat (6) +Q8C3F7 KLH30_MOUSE Kelch-like protein 30 581 64,605 Chain (1); Domain (2); Frameshift (1); Repeat (6) +Q6ZPT1 KLHL9_MOUSE Kelch-like protein 9 617 69,400 Chain (1); Domain (2); Erroneous initiation (1); Repeat (6) Protein modification; protein ubiquitination. FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex required for mitotic progression and cytokinesis. The BCR(KLHL9-KLHL13) E3 ubiquitin ligase complex mediates the ubiquitination of AURKB and controls the dynamic behavior of AURKB on mitotic chromosomes and thereby coordinates faithful mitotic progression and completion of cytokinesis (By similarity). {ECO:0000250}. SUBUNIT: Component of the BCR(KLHL9-KLHL13) E3 ubiquitin ligase complex, at least composed of CUL3, KLHL9, KLHL13 and RBX1. Interacts with AURKB (By similarity). {ECO:0000250}. +Q8JZP3 KLHL2_MOUSE Kelch-like protein 2 593 65,983 Chain (1); Domain (1); Erroneous initiation (1); Repeat (6) FUNCTION: Promotes growth of cell projections in oligodendrocyte precursors. Responsible for degradative ubiquitination of the WNK kinases WNK1, WNK3 and WNK4 (By similarity). Component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex that mediates the ubiquitination of target proteins, such as NPTXR, leading most often to their proteasomal degradation. Plays a role in the reorganization of the actin cytoskeleton. {ECO:0000250, ECO:0000269|PubMed:21549840}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:21549840}. Cell projection, ruffle {ECO:0000269|PubMed:21549840}. Cell projection {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Cytoplasm, cytosol {ECO:0000269|PubMed:21549840}. Note=A proportion colocalizes with the actin cytoskeleton (By similarity). When over-expressed, colocalizes with NPTXR in perinuclear aggresomes. {ECO:0000250}. SUBUNIT: Binds actin. Interacts with KLHL12. Interacts (via N-terminus) with FYN (via SH3 domain) (By similarity). Component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex. Interacts with NPTXR and CUL3. {ECO:0000250, ECO:0000269|PubMed:21549840}. +Q8BZM0 KLH12_MOUSE Kelch-like protein 12 (CUL3-interacting protein 1) 568 63,246 Alternative sequence (1); Chain (1); Domain (2); Region (1); Repeat (6) Protein modification; protein ubiquitination. FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a negative regulator of Wnt signaling pathway and ER-Golgi transport. The BCR(KLHL12) complex is involved in ER-Golgi transport by regulating the size of COPII coats, thereby playing a key role in collagen export, which is required for embryonic stem (ES) cells division: BCR(KLHL12) acts by mediating monoubiquitination of SEC31 (SEC31A or SEC31B). The BCR(KLHL12) complex is also involved in neural crest specification: in response to cytosolic calcium increase, interacts with the heterodimer formed with PEF1 and PDCD6/ALG-2, leading to bridge together the BCR(KLHL12) complex and SEC31 (SEC31A or SEC31B), promoting monoubiquitination of SEC31 and subsequent collagen export. As part of the BCR(KLHL12) complex, also acts as a negative regulator of the Wnt signaling pathway by mediating ubiquitination and subsequent proteolysis of DVL3. The BCR(KLHL12) complex also mediates polyubiquitination of DRD4 and PEF1, without leading to degradation of these proteins. {ECO:0000250|UniProtKB:Q53G59}. PTM: Ubiquitinated by the SCF(FBXL17) complex, leading to its degradation by the proteaseome: ubiquitination by the SCF(FBXL17) complex takes place when aberrant BTB domain dimers are formed. {ECO:0000250|UniProtKB:Q53G59}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle {ECO:0000250|UniProtKB:Q53G59}. SUBUNIT: Component of the BCR(KLHL12) E3 ubiquitin ligase complex, at least composed of CUL3 and KLHL12 and RBX1. This complex interacts with DVL3 upon activation of the Wnt signaling pathway by WNT3A. Interacts with DRD4, KLHL2 and SEC31A. Interacts with PEF1 and PDCD6/ALG-2; interaction takes place in response to cytosolic calcium increase and leads to bridge together the BCR(KLHL12) complex and SEC31 (SEC31A or SEC31B). {ECO:0000250|UniProtKB:Q53G59}. DOMAIN: The BTB domain is required for interaction with CUL3. {ECO:0000250}. +Q8CGR5 KLK14_MOUSE Kallikrein-14 (EC 3.4.21.-) (Glandular kallikrein KLK14) (mGK14) (Kallikrein related-peptidase 14) 250 27,016 Active site (3); Chain (1); Disulfide bond (4); Domain (1); Propeptide (1); Signal peptide (1) FUNCTION: Serine-type endopeptidase with a dual trypsin-like and chymotrypsin-like substrate specificity. May activate/inactivate the proteinase-activated receptors F2R, F2RL1 and F2RL3 and other kallikreins including KLK1, KLK3, KLK5 and KLK11. May function in seminal clot liquefaction through direct cleavage of the semenogelin SEMG1 and SEMG2 and activation of KLK3. May function through desmoglein DSG1 cleavage in epidermal desquamation a process by which the most superficial corneocytes are shed from the skin surface. May be involved in several aspects of tumor progression including growth, invasion and angiogenesis (By similarity). {ECO:0000250}. PTM: Proteolytic cleavage of the activation peptide produces the active enzyme. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250}. +Q6V595 KLHL6_MOUSE Kelch-like protein 6 619 70,191 Chain (1); Domain (2); Erroneous initiation (1); Repeat (6); Sequence conflict (7) FUNCTION: Involved in B-lymphocyte antigen receptor signaling and germinal center formation. {ECO:0000269|PubMed:16166635}. TISSUE SPECIFICITY: Expressed in embryonic blood vessel endothelial cells but not in the vasculature of adult organs. In adults, detected at high levels in hematopoietic and lymphoid organs. {ECO:0000269|PubMed:16166635}. +P15947 KLK1_MOUSE Kallikrein-1 (EC 3.4.21.35) (Glandular kallikrein K1) (KAL-B) (Renal kallikrein) (Tissue kallikrein-6) (mGK-6) 261 28,775 Active site (3); Chain (1); Disulfide bond (5); Domain (1); Glycosylation (1); Propeptide (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin. +Q60682 KLRA8_MOUSE Killer cell lectin-like receptor 8 (Lymphocyte antigen 49h) (Ly-49h) (T-cell surface glycoprotein Ly-49H) 266 31,393 Alternative sequence (1); Chain (1); Disulfide bond (4); Domain (1); Glycosylation (2); Helix (1); Topological domain (2); Transmembrane (1) TRANSMEM 45 66 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 44 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 67 266 Extracellular. {ECO:0000255}. FUNCTION: Receptor on natural killer (NK) cells for class I MHC. SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. SUBUNIT: Homodimer; disulfide-linked. +P27814 KLRBC_MOUSE Killer cell lectin-like receptor subfamily B member 1C (CD161 antigen-like family member C) (Lymphocyte antigen 55c) (Ly-55c) (NK1.1) (NKR-P1.9) (NKR-P1C) (Natural killer cell surface protein P1-40) (NKR-P1 40) (CD antigen CD161c) 223 25,077 Alternative sequence (1); Chain (1); Disulfide bond (3); Domain (1); Glycosylation (3); Motif (1); Mutagenesis (2); Topological domain (2); Transmembrane (1) TRANSMEM 46 66 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 45 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 67 223 Extracellular. {ECO:0000255}. FUNCTION: Plays a stimulatory role on natural killer (NK) cells cytotoxicity. Activation by cross-linking of the receptor induces Ca(2+) mobilization and interferon-gamma production. {ECO:0000269|PubMed:12813047, ECO:0000269|PubMed:15814704}. SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. SUBUNIT: Homodimer; disulfide-linked. Interacts with tyrosine kinase LCK. {ECO:0000269|PubMed:15814704}. TISSUE SPECIFICITY: Expressed in natural killer cells. +Q8VD98 KLRBF_MOUSE Killer cell lectin-like receptor subfamily B member 1F (CD161 antigen-like family member F) (Natural killer cell surface protein NKR-P1F) (CD antigen CD161f) 217 24,681 Chain (1); Disulfide bond (2); Domain (1); Glycosylation (1); Motif (1); Sequence conflict (3); Topological domain (2); Transmembrane (1) TRANSMEM 46 66 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 45 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 67 217 Extracellular. {ECO:0000255}. FUNCTION: Binds CLEC2I/Clr-g leading to activation of natural killer cells or costimulation of IL-2 production and proliferation of T-cells in response to antigen stimulation. May contribute to the formation of the immunological synapse between T-cells and antigen-presenting dendritic cells. {ECO:0000269|PubMed:12858173, ECO:0000269|PubMed:15963483, ECO:0000269|PubMed:16143319}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Highly expressed in dendritic cells. Detectable in natural killer cells. {ECO:0000269|PubMed:15963483}. +B2KG20 KLRI1_MOUSE Killer cell lectin-like receptor subfamily I member 1 248 28,642 Chain (1); Disulfide bond (3); Domain (1); Glycosylation (3); Motif (2); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 81 101 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 80 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 102 248 Extracellular. {ECO:0000305}. FUNCTION: Lectin-like receptor for natural killer (NK) cells. Heterodimer formation with KLRE1 mediates inhibition of NK cell cytolytic activity. {ECO:0000269|PubMed:18713988}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18713988}; Single-pass type II membrane protein {ECO:0000255}. SUBUNIT: Heterodimer with KLRE1. Interacts with PTPN6. {ECO:0000250|UniProtKB:Q5DT39}. DOMAIN: Contains 2 copies of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). The phosphorylated ITIM motif can bind the SH2 domain of several SH2-containing phosphatases leading to down-regulation of cell activation. {ECO:0000250|UniProtKB:P27812}. TISSUE SPECIFICITY: Expressed in natural killer (NK) cells. {ECO:0000269|PubMed:15650876}. +Q9CR58 KMCP1_MOUSE Kidney mitochondrial carrier protein 1 (Solute carrier family 25 member 30) 291 32,282 Chain (1); Initiator methionine (1); Modified residue (1); Repeat (3); Sequence conflict (1); Transmembrane (6) TRANSMEM 9 26 Helical; Name=1. {ECO:0000255}.; TRANSMEM 71 89 Helical; Name=2. {ECO:0000255}.; TRANSMEM 106 124 Helical; Name=3. {ECO:0000255}.; TRANSMEM 164 183 Helical; Name=4. {ECO:0000255}.; TRANSMEM 204 224 Helical; Name=5. {ECO:0000255}.; TRANSMEM 264 283 Helical; Name=6. {ECO:0000255}. FUNCTION: Probable transporter. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:15809292}; Multi-pass membrane protein {ECO:0000269|PubMed:15809292}. SUBUNIT: Interacts with VDAC1. {ECO:0000250|UniProtKB:Q5SVS4}. TISSUE SPECIFICITY: Present in kidney (at protein level). Expressed predominantly within the kidney cortex in the proximal and distal tubules and at lower levels in the testis and white adipose tissue. {ECO:0000269|PubMed:15809292}. +Q91WN4 KMO_MOUSE Kynurenine 3-monooxygenase (EC 1.14.13.9) (Kynurenine 3-hydroxylase) 479 54,532 Alternative sequence (1); Binding site (10); Chain (1); Nucleotide binding (2); Transmembrane (2) TRANSMEM 385 404 Helical. {ECO:0000255|HAMAP-Rule:MF_03018}.; TRANSMEM 425 445 Helical. {ECO:0000255|HAMAP-Rule:MF_03018}. Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 1/3. FUNCTION: Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic acid, a neurotoxic NMDA receptor antagonist and potential endogenous inhibitor of NMDA receptor signaling in axonal targeting, synaptogenesis and apoptosis during brain development. Quinolinic acid may also affect NMDA receptor signaling in pancreatic beta cells, osteoblasts, myocardial cells, and the gastrointestinal tract. {ECO:0000255|HAMAP-Rule:MF_03018, ECO:0000269|PubMed:26752518}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000255|HAMAP-Rule:MF_03018}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03018}. DOMAIN: Transmembrane domains are required for enzymatic activity. {ECO:0000250|UniProtKB:O15229}. TISSUE SPECIFICITY: Expressed by organs containing secondary lymphoid tissue, such as the lung, spleen, mesenteric lymph node, thymus and peripheral lymph nodes. {ECO:0000269|PubMed:26752518}. +Q6Q783 KMT5C_MOUSE Histone-lysine N-methyltransferase KMT5C (EC 2.1.1.43) (Lysine-specific methyltransferase 5C) (Suppressor of variegation 4-20 homolog 2) (Su(var)4-20 homolog 2) (Suv4-20h2) 468 53,159 Beta strand (7); Chain (1); Domain (1); Erroneous initiation (2); Helix (11); Region (1); Turn (4) FUNCTION: Histone methyltransferase that specifically trimethylates 'Lys-20' of histone H4. H4 'Lys-20' trimethylation represents a specific tag for epigenetic transcriptional repression. Mainly functions in pericentric heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin in these regions. KMT5C is targeted to histone H3 via its interaction with RB1 family proteins (RB1, RBL1 and RBL2). {ECO:0000269|PubMed:15145825}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15145825}. Chromosome {ECO:0000269|PubMed:15145825}. Note=Associated with pericentric heterochromatin. CBX1 and CBX5 are required for the localization to pericentric heterochromatin. SUBUNIT: Interacts with HP1 proteins CBX1, CBX3 and CBX5. Interacts with RB1 family proteins RB1, RBL1 and RBL2. {ECO:0000269|PubMed:15145825, ECO:0000269|PubMed:15750587, ECO:0000269|PubMed:16612004}. +O08677 KNG1_MOUSE Kininogen-1 [Cleaved into: Kininogen-1 heavy chain; Bradykinin; Kininogen-1 light chain] 661 73,102 Alternative sequence (3); Chain (3); Compositional bias (1); Disulfide bond (9); Domain (3); Glycosylation (4); Modified residue (1); Peptide (1); Sequence conflict (1); Signal peptide (1) FUNCTION: (1) Kininogens are inhibitors of thiol proteases; (2) HMW-kininogen plays an important role in blood coagulation by helping to position optimally prekallikrein and factor XI next to factor XII; (3) HMW-kininogen inhibits the thrombin- and plasmin-induced aggregation of thrombocytes; (4) the active peptide bradykinin that is released from HMW-kininogen shows a variety of physiological effects: (4A) influence in smooth muscle contraction, (4B) induction of hypotension, (4C) natriuresis and diuresis, (4D) decrease in blood glucose level, (4E) it is a mediator of inflammation and causes (4E1) increase in vascular permeability, (4E2) stimulation of nociceptors (4E3) release of other mediators of inflammation (e.g. prostaglandins), (4F) it has a cardioprotective effect (directly via bradykinin action, indirectly via endothelium-derived relaxing factor action); (5) LMW-kininogen inhibits the aggregation of thrombocytes; (6) LMW-kininogen is in contrast to HMW-kininogen not involved in blood clotting (By similarity). {ECO:0000250}. PTM: Bradykinin is released from kininogen by plasma kallikrein.; PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000250|UniProtKB:P01042}. SUBCELLULAR LOCATION: Secreted, extracellular space. SUBUNIT: Isoform LMW interacts with CRISP3. {ECO:0000269|PubMed:20116414}. TISSUE SPECIFICITY: Plasma. +Q66JQ7 KNL1_MOUSE Kinetochore scaffold 1 (Cancer susceptibility candidate gene 5 protein homolog) (Kinetochore-null protein 1) (Protein CASC5) 1612 179,337 Chain (1); Modified residue (8); Motif (1); Region (1); Repeat (2); Sequence conflict (3) FUNCTION: Performs two crucial functions during mitosis: it is essential for spindle-assembly checkpoint signaling and for correct chromosome alignment. Directly links spindle checkpoint proteins BUB1 and BUB1B to kinetochores. Part of the MIS12 complex, which may be fundamental for kinetochore formation and proper chromosome segregation during mitosis. Acts in coordination with CENPK to recruit the NDC80 complex to the outer kinetochore (By similarity). {ECO:0000250|UniProtKB:Q8NG31}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8NG31}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q8NG31}. Note=Weakly expressed in interphase nuclei. Expression increases from prophase to late anaphase, but greatly diminishes from the telophase and cytokinesis to early G1 phase of cell cycle (By similarity). {ECO:0000250|UniProtKB:Q8NG31}. SUBUNIT: Interacts with DSN1, MIS12, BUB1, BUB1B, NSL1 and ZWINT. {ECO:0000250|UniProtKB:Q8NG31}. +Q9Z2Q2 KNOP1_MOUSE Lysine-rich nucleolar protein 1 (Testis-specific gene 118 protein) 478 53,846 Alternative sequence (2); Chain (1); Compositional bias (2); Cross-link (13); Erroneous initiation (1); Modified residue (6); Region (1); Sequence conflict (4) SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:10430019, ECO:0000269|PubMed:15833274}. SUBUNIT: Interacts with ZNF106. {ECO:0000269|PubMed:15833274}. TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:15833274}. +Q8BWJ3 KPB2_MOUSE Phosphorylase b kinase regulatory subunit alpha, liver isoform (Phosphorylase kinase alpha L subunit) 1235 138,492 Chain (1); Erroneous initiation (1); Lipidation (1); Modified residue (6); Region (2) Glycan biosynthesis; glycogen metabolism. FUNCTION: Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I. The alpha chain may bind calmodulin. PTM: Although the final Cys may be farnesylated, the terminal tripeptide is probably not removed, and the C-terminus is not methylated. {ECO:0000250|UniProtKB:P18688}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. SUBUNIT: Hexadecamer of 4 heterotetramers, each composed of alpha, beta, gamma, and delta subunits. Alpha (PHKA1 or PHKA2) and beta (PHKB) are regulatory subunits, gamma (PHKG1 or PHKG2) is the catalytic subunit, and delta is calmodulin (By similarity). {ECO:0000250}. +Q02956 KPCZ_MOUSE Protein kinase C zeta type (EC 2.7.11.13) (nPKC-zeta) 592 67,682 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Domain (3); Modified residue (3); Nucleotide binding (1); Region (1); Sequence conflict (3); Zinc finger (1) FUNCTION: Calcium- and diacylglycerol-independent serine/threonine-protein kinase that functions in phosphatidylinositol 3-kinase (PI3K) pathway and mitogen-activated protein (MAP) kinase cascade, and is involved in NF-kappa-B activation, mitogenic signaling, cell proliferation, cell polarity, inflammatory response and maintenance of long-term potentiation (LTP). Upon lipopolysaccharide (LPS) treatment in macrophages, or following mitogenic stimuli, functions downstream of PI3K to activate MAP2K1/MEK1-MAPK1/ERK2 signaling cascade independently of RAF1 activation. Required for insulin-dependent activation of AKT3, but may function as an adapter rather than a direct activator. Upon insulin treatment may act as a downstream effector of PI3K and contribute to the activation of translocation of the glucose transporter SLC2A4/GLUT4 and subsequent glucose transport in adipocytes. In EGF-induced cells, binds and activates MAP2K5/MEK5-MAPK7/ERK5 independently of its kinase activity and can activate JUN promoter through MEF2C. Through binding with SQSTM1/p62, functions in interleukin-1 signaling and activation of NF-kappa-B with the specific adapters RIPK1 and TRAF6. Participates in TNF-dependent transactivation of NF-kappa-B by phosphorylating and activating IKBKB kinase, which in turn leads to the degradation of NF-kappa-B inhibitors. In migrating astrocytes, forms a cytoplasmic complex with PARD6A and is recruited by CDC42 to function in the establishment of cell polarity along with the microtubule motor and dynein. In association with FEZ1, stimulates neuronal differentiation in PC12 cells. In the inflammatory response, is required for the T-helper 2 (Th2) differentiation process, including interleukin production, efficient activation of JAK1 and the subsequent phosphorylation and nuclear translocation of STAT6. May be involved in development of allergic airway inflammation (asthma), a process dependent on Th2 immune response. In the NF-kappa-B-mediated inflammatory response, can relieve SETD6-dependent repression of NF-kappa-B target genes by phosphorylating the RELA subunit at 'Ser-311'. In vein endothelial cells treated with the oxidant peroxynitrite, phosphorylates STK11 leading to nuclear export of STK11, subsequent inhibition of PI3K/Akt signaling, and increased apoptosis. Phosphorylates VAMP2 in vitro (By similarity). {ECO:0000250|UniProtKB:Q05513, ECO:0000269|PubMed:15987782, ECO:0000269|PubMed:21131967}.; FUNCTION: Isoform 2: Involved in late synaptic long term potentiation phase in CA1 hippocampal cells and long term memory maintenance. {ECO:0000269|PubMed:27187150}. PTM: CDH5 is required for its phosphorylation at Thr-410. Phosphorylated by protein kinase PDPK1; phosphorylation is inhibited by the apoptotic C-terminal cleavage product of PKN2. Phosphorylation at Thr-410 by PI3K activates the kinase (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q05513}. Endosome {ECO:0000250|UniProtKB:Q05513}. Cell junction {ECO:0000250|UniProtKB:Q05513}. Membrane {ECO:0000250|UniProtKB:P09217}; Peripheral membrane protein {ECO:0000305}. Note=In the retina, localizes in the terminals of the rod bipolar cells (By similarity). Associated with endosomes (By similarity). Presence of KRIT1, CDH5 and RAP1B is required for its localization to the cell junction (By similarity). Colocalizes with VAMP2 and WDFY2 in intracellular vesicles (PubMed:17313651). Transiently translocates to the membrane of CA1 hippocampal cells in response to the induction of long term potentiation (By similarity). {ECO:0000250|UniProtKB:P09217, ECO:0000250|UniProtKB:Q05513, ECO:0000269|PubMed:17313651}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm {ECO:0000250|UniProtKB:P09217}. SUBUNIT: Interacts directly with SQSTM1. Forms a ternary complex with SQSTM1 and KCNAB2. Forms another ternary complex with SQSTM1 and GABRR3. Forms a complex with SQSTM1 and MAP2K5 (By similarity). Interacts with PARD6A, PARD6B and PARD6G. Part of a complex with PARD3, PARD6A or PARD6B or PARD6G and CDC42 or RAC1. Interacts with ADAP1/CENTA1. Interacts (via the protein kinase domain) with WWC1. Forms a tripartite complex with WWC1 and DDR1, but predominantly in the absence of collagen. Interacts with PDPK1 (via N-terminal region) (By similarity). Interacts with WDFY2 (via WD repeats 1-3) (PubMed:16792529). Interacts with VAMP2 (PubMed:17313651). Forms a complex with WDFY2 and VAMP2 (PubMed:17313651). {ECO:0000250|UniProtKB:P09217, ECO:0000269|PubMed:16792529, ECO:0000269|PubMed:17313651}. DOMAIN: The C1 domain does not bind the diacylglycerol (DAG).; DOMAIN: The PB1 domain mediate mutually exclusive interactions with SQSTM1 and PARD6B. {ECO:0000250}. TISSUE SPECIFICITY: Isoform 1: In brain, highly expressed in cerebellar granule neurons and cerebellar astrocytes (at protein level) (PubMed:1487145, PubMed:12932816). Expressed at low levels in testes, lung and kidney (PubMed:1487145, PubMed:23283171). Isoform 2: Specifically expressed in brain where it localizes to cerebellar granule neurons (at protein level) (PubMed:12932816, PubMed:23283171). {ECO:0000269|PubMed:12932816, ECO:0000269|PubMed:1487145, ECO:0000269|PubMed:23283171}. +P28867 KPCD_MOUSE Protein kinase C delta type (EC 2.7.11.13) (Tyrosine-protein kinase PRKCD) (EC 2.7.10.2) (nPKC-delta) [Cleaved into: Protein kinase C delta type regulatory subunit; Protein kinase C delta type catalytic subunit (Sphingosine-dependent protein kinase-1) (SDK1)] 674 77,547 Active site (1); Alternative sequence (1); Beta strand (4); Binding site (1); Chain (3); Domain (3); Helix (1); Modified residue (18); Nucleotide binding (1); Sequence conflict (10); Site (5); Turn (2); Zinc finger (2) FUNCTION: Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays contrasting roles in cell death and cell survival by functioning as a pro-apoptotic protein during DNA damage-induced apoptosis, but acting as an anti-apoptotic protein during cytokine receptor-initiated cell death, is involved in tumor suppression, is required for oxygen radical production by NADPH oxidase and acts as positive or negative regulator in platelet functional responses. Negatively regulates B cell proliferation and also has an important function in self-antigen induced B cell tolerance induction. Upon DNA damage, activates the promoter of the death-promoting transcription factor BCLAF1/Btf to trigger BCLAF1-mediated p53/TP53 gene transcription and apoptosis. In response to oxidative stress, interact with and activate CHUK/IKKA in the nucleus, causing the phosphorylation of p53/TP53. In the case of ER stress or DNA damage-induced apoptosis, can form a complex with the tyrosine-protein kinase ABL1 which trigger apoptosis independently of p53/TP53. In cytosol can trigger apoptosis by activating MAPK11 or MAPK14, inhibiting AKT1 and decreasing the level of X-linked inhibitor of apoptosis protein (XIAP), whereas in nucleus induces apoptosis via the activation of MAPK8 or MAPK9. Upon ionizing radiation treatment, is required for the activation of the apoptosis regulators BAX and BAK, which trigger the mitochondrial cell death pathway. Can phosphorylate MCL1 and target it for degradation which is sufficient to trigger for BAX activation and apoptosis. Is required for the control of cell cycle progression both at G1/S and G2/M phases. Mediates phorbol 12-myristate 13-acetate (PMA)-induced inhibition of cell cycle progression at G1/S phase by up-regulating the CDK inhibitor CDKN1A/p21 and inhibiting the cyclin CCNA2 promoter activity. In response to UV irradiation can phosphorylate CDK1, which is important for the G2/M DNA damage checkpoint activation. Can protect glioma cells from the apoptosis induced by TNFSF10/TRAIL, probably by inducing increased phosphorylation and subsequent activation of AKT1. Can also act as tumor suppressor upon mitogenic stimulation with PMA or TPA. In N-formyl-methionyl-leucyl-phenylalanine (fMLP)-treated cells, is required for NCF1 (p47-phox) phosphorylation and activation of NADPH oxidase activity, and regulates TNF-elicited superoxide anion production in neutrophils, by direct phosphorylation and activation of NCF1 or indirectly through MAPK1/3 (ERK1/2) signaling pathways. May also play a role in the regulation of NADPH oxidase activity in eosinophil after stimulation with IL5, leukotriene B4 or PMA. In collagen-induced platelet aggregation, acts a negative regulator of filopodia formation and actin polymerization by interacting with and negatively regulating VASP phosphorylation. Downstream of PAR1, PAR4 and CD36/GP4 receptors, regulates differentially platelet dense granule secretion; acts as a positive regulator in PAR-mediated granule secretion, whereas it negatively regulates CD36/GP4-mediated granule release. Phosphorylates MUC1 in the C-terminal and regulates the interaction between MUC1 and beta-catenin. The catalytic subunit phosphorylates 14-3-3 proteins (YWHAB, YWHAZ and YWHAH) in a sphingosine-dependent fashion. Phosphorylates ELAVL1 in response to angiotensin-2 treatment (By similarity). {ECO:0000250|UniProtKB:Q05655, ECO:0000269|PubMed:11976686, ECO:0000269|PubMed:11976687, ECO:0000269|PubMed:18025218, ECO:0000269|PubMed:19917613, ECO:0000269|PubMed:9705322}. PTM: Autophosphorylated and/or phosphorylated at Thr-505, within the activation loop; phosphorylation at Thr-505 is not a prerequisite for enzymatic activity. Autophosphorylated at Ser-299. Upon TNFSF10/TRAIL treatment, phosphorylated at Tyr-155; phosphorylation is required for its translocation to the endoplasmic reticulum and cleavage by caspase-3. Phosphorylated at Tyr-311, Tyr-332 and Tyr-565; phosphorylation of Tyr-311 and Tyr-565 following thrombin stimulation potentiates its kinase activity. Phosphorylated by protein kinase PDPK1; phosphorylation is inhibited by the apoptotic C-terminal cleavage product of PKN2 (By similarity). {ECO:0000250}.; PTM: Proteolytically cleaved into a catalytic subunit and a regulatory subunit by caspase-3 during apoptosis which results in kinase activation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q05655}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q05655}. Nucleus {ECO:0000250|UniProtKB:Q05655}. Cell membrane {ECO:0000250|UniProtKB:Q05655}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q05655}. SUBUNIT: Interacts with PDPK1 (via N-terminal region) (By similarity). Interacts with RAD9A (By similarity). Interacts with CDCP1 (By similarity). Interacts with MUC1 (By similarity). Interacts with VASP (By similarity). Interacts with CAVIN3 (PubMed:9054438). Interacts with PRKD2 (via N-terminus and zing-finger domain 1 and 2) in response to oxidative stress; the interaction is independent of PRKD2 tyrosine phosphorylation (By similarity). {ECO:0000250|UniProtKB:Q05655, ECO:0000269|PubMed:9054438}. DOMAIN: The C1 domain, containing the phorbol ester/DAG-type region 1 (C1A) and 2 (C1B), is the diacylglycerol sensor.; DOMAIN: The C2 domain is a non-calcium binding domain. It binds proteins containing phosphotyrosine in a sequence-specific manner (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Isoform 1 is highly expressed in developing pro- and pre-B-cells and moderately in mature T-cells. Isoform 2 is highly expressed in testis and ovary and at a lower level in thymocytes, brain and kidney. +P16054 KPCE_MOUSE Protein kinase C epsilon type (EC 2.7.11.13) (nPKC-epsilon) 737 83,561 Active site (1); Binding site (1); Chain (1); Domain (3); Modified residue (16); Motif (1); Mutagenesis (3); Nucleotide binding (1); Zinc finger (2) FUNCTION: Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays essential roles in the regulation of multiple cellular processes linked to cytoskeletal proteins, such as cell adhesion, motility, migration and cell cycle, functions in neuron growth and ion channel regulation, and is involved in immune response, cancer cell invasion and regulation of apoptosis. Mediates cell adhesion to the extracellular matrix via integrin-dependent signaling, by mediating angiotensin-2-induced activation of integrin beta-1 (ITGB1) in cardiac fibroblasts. Phosphorylates MARCKS, which phosphorylates and activates PTK2/FAK, leading to the spread of cardiomyocytes. Involved in the control of the directional transport of ITGB1 in mesenchymal cells by phosphorylating vimentin (VIM), an intermediate filament (IF) protein. In epithelial cells, associates with and phosphorylates keratin-8 (KRT8), which induces targeting of desmoplakin at desmosomes and regulates cell-cell contact. Phosphorylates IQGAP1, which binds to CDC42, mediating epithelial cell-cell detachment prior to migration. During cytokinesis, forms a complex with YWHAB, which is crucial for daughter cell separation, and facilitates abscission by a mechanism which may implicate the regulation of RHOA. In cardiac myocytes, regulates myofilament function and excitation coupling at the Z-lines, where it is indirectly associated with F-actin via interaction with COPB1. During endothelin-induced cardiomyocyte hypertrophy, mediates activation of PTK2/FAK, which is critical for cardiomyocyte survival and regulation of sarcomere length. Plays a role in the pathogenesis of dilated cardiomyopathy via persistent phosphorylation of troponin I (TNNI3). Involved in nerve growth factor (NFG)-induced neurite outgrowth and neuron morphological change independently of its kinase activity, by inhibition of RHOA pathway, activation of CDC42 and cytoskeletal rearrangement. May be involved in presynaptic facilitation by mediating phorbol ester-induced synaptic potentiation. Phosphorylates gamma-aminobutyric acid receptor subunit gamma-2 (GABRG2), which reduces the response of GABA receptors to ethanol and benzodiazepines and may mediate acute tolerance to the intoxicating effects of ethanol. Upon PMA treatment, phosphorylates the capsaicin- and heat-activated cation channel TRPV1, which is required for bradykinin-induced sensitization of the heat response in nociceptive neurons. Is able to form a complex with PDLIM5 and N-type calcium channel, and may enhance channel activities and potentiates fast synaptic transmission by phosphorylating the pore-forming alpha subunit CACNA1B (CaV2.2). Downstream of TLR4, plays an important role in the lipopolysaccharide (LPS)-induced immune response by phosphorylating and activating TICAM2/TRAM, which in turn activates the transcription factor IRF3 and subsequent cytokines production. In differentiating erythroid progenitors, is regulated by EPO and controls the protection against the TNFSF10/TRAIL-mediated apoptosis, via BCL2. May be involved in the regulation of the insulin-induced phosphorylation and activation of AKT1. {ECO:0000269|PubMed:11746497, ECO:0000269|PubMed:12407104, ECO:0000269|PubMed:15949469, ECO:0000269|PubMed:16270034, ECO:0000269|PubMed:16445938, ECO:0000269|PubMed:16757566, ECO:0000269|PubMed:18604201}. PTM: Phosphorylation on Thr-566 by PDPK1 triggers autophosphorylation on Ser-729 (By similarity). Phosphorylation in the hinge domain at Ser-350 by MAPK11 or MAPK14, Ser-346 by GSK3B and Ser-368 by autophosphorylation is required for interaction with YWHAB. {ECO:0000250, ECO:0000269|PubMed:17611075, ECO:0000269|PubMed:18237277, ECO:0000269|PubMed:18604201}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:17611075}. Nucleus {ECO:0000269|PubMed:17611075}. Note=Translocated to plasma membrane in epithelial cells stimulated by HGF (By similarity). Associated with the Golgi at the perinuclear site in pre-passage fibroblasts. In passaging cells, translocated to the cell periphery. Translocated to the nucleus in PMA-treated cells. {ECO:0000250}. SUBUNIT: Forms a ternary complex with TRIM63 and GN2BL1. Can form a complex with PDLIM5 and N-type calcium channel. Interacts with COPB1, DGKQ and STAT3 (By similarity). Interacts with YWHAB. Interacts with HSP90AB1; promotes functional activation in a heat shock-dependent manner (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q02156, ECO:0000269|PubMed:11746497, ECO:0000269|PubMed:18604201}. DOMAIN: The C1 domain, containing the phorbol ester/DAG-type region 1 (C1A) and 2 (C1B), is the diacylglycerol sensor and the C2 domain is a non-calcium binding domain. +P63318 KPCG_MOUSE Protein kinase C gamma type (PKC-gamma) (EC 2.7.11.13) 697 78,358 Active site (1); Binding site (1); Chain (1); Domain (3); Metal binding (14); Modified residue (14); Nucleotide binding (1); Zinc finger (2) FUNCTION: Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays diverse roles in neuronal cells and eye tissues, such as regulation of the neuronal receptors GRIA4/GLUR4 and GRIN1/NMDAR1, modulation of receptors and neuronal functions related to sensitivity to opiates, pain and alcohol, mediation of synaptic function and cell survival after ischemia, and inhibition of gap junction activity after oxidative stress. Binds and phosphorylates GRIA4/GLUR4 glutamate receptor and regulates its function by increasing plasma membrane-associated GRIA4 expression. In primary cerebellar neurons treated with the agonist 3,5-dihyidroxyphenylglycine, functions downstream of the metabotropic glutamate receptor GRM5/MGLUR5 and phosphorylates GRIN1/NMDAR1 receptor which plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. May be involved in the regulation of hippocampal long-term potentiation (LTP), but may be not necessary for the process of synaptic plasticity. May be involved in desensitization of mu-type opioid receptor-mediated G-protein activation in the spinal cord, and may be critical for the development and/or maintenance of morphine-induced reinforcing effects in the limbic forebrain. May modulate the functionality of mu-type-opioid receptors by participating in a signaling pathway which leads to the phosphorylation and degradation of opioid receptors. May also contribute to chronic morphine-induced changes in nociceptive processing. Plays a role in neuropathic pain mechanisms and contributes to the maintenance of the allodynia pain produced by peripheral inflammation. Plays an important role in initial sensitivity and tolerance to ethanol, by mediating the behavioral effects of ethanol as well as the effects of this drug on the GABA(A) receptors. During and after cerebral ischemia modulate neurotransmission and cell survival in synaptic membranes, and is involved in insulin-induced inhibition of necrosis, an important mechanism for minimizing ischemic injury. Required for the elimination of multiple climbing fibers during innervation of Purkinje cells in developing cerebellum. Is activated in lens epithelial cells upon hydrogen peroxide treatment, and phosphorylates connexin-43 (GJA1/CX43), resulting in disassembly of GJA1 gap junction plaques and inhibition of gap junction activity which could provide a protective effect against oxidative stress. Phosphorylates p53/TP53 and promotes p53/TP53-dependent apoptosis in response to DNA damage. Involved in the phase resetting of the cerebral cortex circadian clock during temporally restricted feeding. Stabilizes the core clock component ARNTL/BMAL1 by interfering with its ubiquitination, thus suppressing its degradation, resulting in phase resetting of the cerebral cortex clock (PubMed:23185022). {ECO:0000269|PubMed:11246146, ECO:0000269|PubMed:11278552, ECO:0000269|PubMed:11356858, ECO:0000269|PubMed:11731061, ECO:0000269|PubMed:17904530, ECO:0000269|PubMed:23185022, ECO:0000269|PubMed:8269509, ECO:0000269|PubMed:9323205}. PTM: Autophosphorylation on Thr-674 appears to regulate motor functions of junctophilins, JPH3 and JPH4. {ECO:0000269|PubMed:17904530}.; PTM: Ubiquitinated. {ECO:0000250|UniProtKB:P05129}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17904530}. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:17904530, ECO:0000269|PubMed:18473171}; Peripheral membrane protein. Cell junction, synapse, synaptosome {ECO:0000269|PubMed:18473171}. Cell projection, dendrite {ECO:0000250|UniProtKB:P63319}. Note=Translocates to synaptic membranes on stimulation. {ECO:0000269|PubMed:18473171}. SUBUNIT: Interacts with CDCP1 and GRIA4 (By similarity). Interacts with TP53INP1 and p53/TP53 (By similarity). Interacts with ARNTL/BMAL1. {ECO:0000250|UniProtKB:P05129, ECO:0000250|UniProtKB:P63319, ECO:0000269|PubMed:23185022}. TISSUE SPECIFICITY: Expressed in the cerebellum, cerebral cortex and hippocampus (at protein level). Highly expressed in Purkinje cells. {ECO:0000269|PubMed:17904530, ECO:0000269|PubMed:23185022}. +Q8BGV8 MID51_MOUSE Mitochondrial dynamics protein MID51 (Mitochondrial dynamics protein of 51 kDa homolog) (Mitochondrial elongation factor 1) (Smith-Magenis syndrome chromosomal region candidate gene 7 protein-like) 463 51,184 Beta strand (12); Binding site (6); Chain (1); Helix (16); Modified residue (4); Mutagenesis (6); Region (3); Sequence conflict (1); Topological domain (2); Transmembrane (1); Turn (3) TRANSMEM 24 46 Helical. {ECO:0000255}. TOPO_DOM 1 23 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 47 463 Cytoplasmic. {ECO:0000255}. FUNCTION: Mitochondrial outer membrane protein which regulates mitochondrial fission. Promotes the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface independently of the mitochondrial fission FIS1 and MFF proteins. Regulates DNM1L GTPase activity and DNM1L oligomerization. Binds ADP and can also bind GDP, although with lower affinity. Does not bind CDP, UDP, ATP, AMP or GTP. Inhibits DNM1L GTPase activity in the absence of bound ADP. Requires ADP to stimulate DNM1L GTPase activity and the assembly of DNM1L into long, oligomeric tubules with a spiral pattern, as opposed to the ring-like DNM1L oligomers observed in the absence of bound ADP. Does not require ADP for its function in recruiting DNM1L. {ECO:0000269|PubMed:23283981, ECO:0000269|PubMed:24508339}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:24508339}; Single-pass membrane protein {ECO:0000269|PubMed:24508339}. SUBUNIT: Homodimer. Interacts with DNM1L. {ECO:0000269|PubMed:24508339}. +Q0P557 MIEAP_MOUSE Mitochondria-eating protein (Spermatogenesis-associated protein 18) 537 60,398 Alternative sequence (2); Chain (1); Coiled coil (2); Compositional bias (1); Modified residue (9); Sequence conflict (1) FUNCTION: Key regulator of mitochondrial quality that mediates the repairing or degradation of unhealthy mitochondria in response to mitochondrial damage. Mediator of mitochondrial protein catabolic process (also named MALM) by mediating the degradation of damaged proteins inside mitochondria by promoting the accumulation in the mitochondrial matrix of hydrolases that are characteristic of the lysosomal lumen. Also involved in mitochondrion degradation of damaged mitochondria by promoting the formation of vacuole-like structures (named MIV), which engulf and degrade unhealthy mitochondria by accumulating lysosomes. May have a role in spermatogenesis, especially in cell differentiation from late elongate spermatids to mature spermatozoa (By similarity). The physical interaction of SPATA18/MIEAP, BNIP3 and BNIP3L/NIX at the mitochondrial outer membrane regulates the opening of a pore in the mitochondrial double membrane in order to mediate the translocation of lysosomal proteins from the cytoplasm to the mitochondrial matrix (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8TC71}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q8TC71}. Note=Localizes to the cytoplasm under normal conditions. Relocalizes to mitochondrion outer membrane following cellular stress. Colocalizes with BNIP3 and BNIP3L at the mitochondrion outer membrane. {ECO:0000250|UniProtKB:Q8TC71}. SUBUNIT: Interacts (via coiled-coil domains) with BNIP3L (via BH3 domain). Interacts (via coiled-coil domains) with BNIP3 (via BH3 domain). {ECO:0000250}. TISSUE SPECIFICITY: In testis, expressed primarily in spermatids. {ECO:0000269|PubMed:21300779}. +Q9CQ86 MIEN1_MOUSE Migration and invasion enhancer 1 115 12,295 Chain (1); Disulfide bond (1); Initiator methionine (1); Lipidation (1); Modified residue (1); Mutagenesis (2); Propeptide (1) FUNCTION: Increases cell migration by inducing filopodia formation at the leading edge of migrating cells. Plays a role in regulation of apoptosis, possibly through control of CASP3. May be involved in a redox-related process (By similarity). {ECO:0000250}. PTM: Isoprenylation facilitates association with the plasma membrane and enhances the migratory phenotype of cells by inducing increased filopodia formation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:17503775}. Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Concentrates at the leading edge of migrating cells. Localizes outside membrane raft regions (By similarity). {ECO:0000250}. SUBUNIT: Interacts with GPX1. {ECO:0000269|PubMed:17503775}. TISSUE SPECIFICITY: Widely expressed with highest levels in kidney followed by brain and testis. {ECO:0000269|PubMed:17503775}. +Q3TN34 MILK2_MOUSE MICAL-like protein 2 (Junctional Rab13-binding protein) (Molecule interacting with CasL-like 2) (MICAL-L2) 1009 108,288 Chain (1); Coiled coil (1); Domain (3); Modified residue (7); Region (5); Sequence conflict (1) FUNCTION: Effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecules transport to the plasma membrane and actin cytoskeleton reorganization. Regulates the endocytic recycling of occludins, claudins and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. In parallel, may regulate actin cytoskeleton reorganization directly through interaction with F-actin or indirectly through actinins and filamins. Most probably involved in the processes of epithelial cell differentiation, cell spreading and neurite outgrowth. {ECO:0000269|PubMed:16525024, ECO:0000269|PubMed:18094055, ECO:0000269|PubMed:20008558, ECO:0000269|PubMed:23100251, ECO:0000269|PubMed:23890175}. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. Cell junction, tight junction. Recycling endosome. Cell projection {ECO:0000250}. Cytoplasm, cytoskeleton. Cytoplasm, cytosol. SUBUNIT: Interacts with RAB13 (GTP-bound form); competes with RAB8A and is involved in tight junctions assembly. Interacts with RAB8A; competes with RAB13 and is involved in E-cadherin endocytic recycling. Interacts with RAB8B. Interacts (preferentially in opened conformation) with ACTN1 and ACTN4; stimulated by RAB13 activation. Interacts (via calponin-homology (CH) domain) with the filamins FLNA, FLNB and FLNC (via actin-binding domain). {ECO:0000269|PubMed:16525024, ECO:0000269|PubMed:18094055, ECO:0000269|PubMed:18332111, ECO:0000269|PubMed:20008558, ECO:0000269|PubMed:23100251, ECO:0000269|PubMed:23890175}. DOMAIN: Probably exists in a closed and an open conformation due to interaction of the C-terminal coiled-coil domain with an N-terminal region including the calponin-homology (CH) and the LIM zinc-binding domain. The conformational change is regulated by RAB13. {ECO:0000269|PubMed:20008558, ECO:0000269|PubMed:23100251, ECO:0000269|PubMed:23890175}. TISSUE SPECIFICITY: Detected in brain, lung, liver and kidney (at protein level). {ECO:0000269|PubMed:16525024}. +Q8BG40 KTNB1_MOUSE Katanin p80 WD40 repeat-containing subunit B1 (Katanin p80 subunit B1) (p80 katanin) 658 72,639 Chain (1); Helix (9); Modified residue (1); Mutagenesis (8); Region (4); Repeat (6); Sequence conflict (2); Turn (2) FUNCTION: Participates in a complex which severs microtubules in an ATP-dependent manner. May act to target the enzymatic subunit of this complex to sites of action such as the centrosome. Microtubule severing may promote rapid reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. Microtubule release from the mitotic spindle poles may allow depolymerization of the microtubule end proximal to the spindle pole, leading to poleward microtubule flux and poleward motion of chromosome. The function in regulating microtubule dynamics at spindle poles seems to depend on the association of the katanin KATNA1:KATNB1 complex with ASPM which recruits it to microtubules. Reversely KATNA1:KATNB1 can enhance ASPM blocking activity on microtubule minus-end growth. Microtubule release within the cell body of neurons may be required for their transport into neuronal processes by microtubule-dependent motor proteins. This transport is required for axonal growth. {ECO:0000255|HAMAP-Rule:MF_03022, ECO:0000269|PubMed:28436967}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03022}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03022}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000255|HAMAP-Rule:MF_03022}. Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03022}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9BVA0}. Note=Predominantly cytoplasmic. Localized to the interphase centrosome and mitotic spindle poles (By similarity). Localizes within the cytoplasm, partially overlapping with microtubules, in interphase and to the mitotic spindle and spindle poles during mitosis (By similarity). {ECO:0000250|UniProtKB:Q9BVA0, ECO:0000255|HAMAP-Rule:MF_03022}. SUBUNIT: Interacts with KATNA1. This interaction enhances the microtubule binding and severing activity of KATNA1 and also targets this activity to the centrosome (PubMed:16203747). This interaction is weakly competed by KATNBL1 which has a lower affinity for it (By similarity). Interacts with ASPM; the katanin complex formation KATNA1:KATNB1 is required for the association of ASPM (PubMed:28436967). Interacts with dynein, microtubules, NDEL1 and PAFAH1B1 (PubMed:16203747). Interacts with KATNAL1; this interaction is weakly competed by KATNBL1 which has a lower affinity for it (By similarity). Interacts with CAMSAP2 and CAMSAP3; leading to regulate the length of CAMSAP-decorated microtubule stretches (By similarity). {ECO:0000250|UniProtKB:Q9BVA0, ECO:0000255|HAMAP-Rule:MF_03022, ECO:0000269|PubMed:16203747, ECO:0000269|PubMed:28436967}. +Q9JM52 MINK1_MOUSE Misshapen-like kinase 1 (EC 2.7.11.1) (GCK family kinase MiNK) (MAPK/ERK kinase kinase kinase 6) (MEK kinase kinase 6) (MEKKK 6) (Misshapen/NIK-related kinase) (Mitogen-activated protein kinase kinase kinase kinase 6) 1308 147,295 Active site (1); Alternative sequence (2); Binding site (1); Chain (1); Compositional bias (4); Domain (2); Modified residue (12); Nucleotide binding (1); Region (1); Sequence conflict (8) FUNCTION: Serine/threonine kinase which acts as a negative regulator of Ras-related Rap2-mediated signal transduction to control neuronal structure and AMPA receptor trafficking. Required for normal synaptic density, dendrite complexity, as well as surface AMPA receptor expression in hippocampal neurons. Can activate the JNK and MAPK14/p38 pathways and mediates stimulation of the stress-activated protein kinase MAPK14/p38 MAPK downstream of the Raf/ERK pathway. Phosphorylates: TANC1 upon stimulation by RAP2A, MBP and SMAD1. Has an essential function in negative selection of thymocytes, perhaps by coupling NCK1 to activation of JNK1. {ECO:0000269|PubMed:10708748, ECO:0000269|PubMed:15608642}. PTM: Autophosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250}. Cell projection, axon {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. SUBUNIT: Interacts with RAP2A and TANC1 (By similarity). Interacts with NCK1. {ECO:0000250, ECO:0000269|PubMed:15608642}. TISSUE SPECIFICITY: Appears to be ubiquitous, expressed in all tissue types examined. Highly expressed in the brain, moderately expressed in kidney and spleen, low levels present in heart and skeletal muscle. Isoform 2 is more abundant in the brain than isoform 1. {ECO:0000269|PubMed:10708748}. +Q9Z2L6 MINP1_MOUSE Multiple inositol polyphosphate phosphatase 1 (EC 3.1.3.62) (2,3-bisphosphoglycerate 3-phosphatase) (2,3-BPG phosphatase) (EC 3.1.3.80) (Inositol (1,3,4,5)-tetrakisphosphate 3-phosphatase) (Ins(1,3,4,5)P(4) 3-phosphatase) 481 54,537 Active site (1); Chain (1); Frameshift (1); Glycosylation (2); Motif (1); Mutagenesis (1); Sequence conflict (3); Signal peptide (1) FUNCTION: Acts as a 2,3-bisphosphoglycerate 3-phosphatase, by mediating the dephosphorylation of 2,3-bisphosphoglycerate (2,3-BPG) to produce phospho-D-glycerate without formation of 3-phosphoglycerate (By similarity). Acts as a phosphoinositide 5- and phosphoinositide 6-phosphatase and regulates cellular levels of inositol pentakisphosphate (InsP5) and inositol hexakisphosphate (InsP6). May play a role in bone development (endochondral ossification). May play a role in the transition of chondrocytes from proliferation to hypertrophy (By similarity). {ECO:0000250|UniProtKB:F1NPQ2, ECO:0000250|UniProtKB:Q9UNW1, ECO:0000269|PubMed:10938126}. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:O35217}. Cell membrane {ECO:0000305|PubMed:10938126}. Note=Also attached to the plasma membrane in erythrocytes. {ECO:0000305}. TISSUE SPECIFICITY: Widely expressed with highest levels in kidney, intestine, thymus and liver. +Q62504 MINT_MOUSE Msx2-interacting protein (SMART/HDAC1-associated repressor protein) (SPEN homolog) 3644 398,754 Alternative sequence (4); Chain (1); Coiled coil (5); Compositional bias (7); DNA binding (1); Domain (6); Erroneous initiation (1); Erroneous termination (1); Frameshift (1); Modified residue (48); Natural variant (4); Region (2); Sequence conflict (33) FUNCTION: May serve as a nuclear matrix platform that organizes and integrates transcriptional responses. In osteoblasts, supports transcription activation: synergizes with RUNX2 to enhance FGFR2-mediated activation of the osteocalcin FGF-responsive element (OCFRE). Has also been shown to be an essential corepressor protein, which probably regulates different key pathways, such as the Notch pathway. Negative regulator of the Notch pathway via its interaction with RBPSUH, which prevents the association between NOTCH1 and RBPSUH, and therefore suppresses the transactivation activity of Notch signaling. Blocks the differentiation of precursor B-cells into marginal zone B-cells. Probably represses transcription via the recruitment of large complexes containing histone deacetylase proteins. May bind both to DNA and RNA. {ECO:0000269|PubMed:10451362, ECO:0000269|PubMed:12594956, ECO:0000269|PubMed:15131132, ECO:0000269|PubMed:20484411}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10451362, ECO:0000269|PubMed:15131132}. Note=Associates with chromatin. SUBUNIT: Interacts with NCOR2, HDAC1, HDAC2, RBBP4, MBD3 and MTA1L1. Interacts with the nuclear receptors RAR and PPARD. Interacts with RAR in absence of ligand. Binds to the steroid receptor RNA coactivator SRA (By similarity). Interacts with MSX2. Interacts with RBPSUH; this interaction may prevent the interaction between RBPSUH and NOTCH1. Binds to HIPK3. {ECO:0000250, ECO:0000269|PubMed:10451362, ECO:0000269|PubMed:20484411}. DOMAIN: The RID domain mediates the interaction with nuclear receptors.; DOMAIN: The SPOC domain, which mediates the interaction with NCOR2, is essential for the repressive activity. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in testis. Expressed at lower level in brain, lung, spleen, liver and kidney. Weakly expressed in cardiac and skeletal muscles and ovary. In spleen, it is expressed in follicular B-cells, while it is weakly expressed in marginal zone B-cells. {ECO:0000269|PubMed:10451362, ECO:0000269|PubMed:12374742, ECO:0000269|PubMed:12594956}. +Q6PDI6 MINY2_MOUSE Ubiquitin carboxyl-terminal hydrolase MINDY-2 (EC 3.4.19.12) (Deubiquitinating enzyme MINDY-2) (Protein FAM63B) 601 65,637 Active site (2); Alternative sequence (3); Chain (1); Compositional bias (1); Erroneous initiation (1); Frameshift (1); Modified residue (2); Region (1); Sequence caution (1); Sequence conflict (5); Site (3) FUNCTION: Hydrolase that can remove 'Lys-48'-linked conjugated ubiquitin from proteins. Can also bind to polyubiquitin chains of different linkage types, including 'Lys-6', 'Lys-11', 'Lys-29', 'Lys-33' and 'Lys-63'. May play a regulatory role at the level of protein turnover. {ECO:0000250|UniProtKB:Q8NBR6}. +Q3UQI9 MINY4_MOUSE Probable ubiquitin carboxyl-terminal hydrolase MINDY-4 (EC 3.4.19.12) (Probable deubiquitinating enzyme MINDY-4) 744 82,937 Active site (2); Alternative sequence (1); Chain (1); Modified residue (4) FUNCTION: Probable hydrolase that can remove 'Lys-48'-linked conjugated ubiquitin from proteins. {ECO:0000250|UniProtKB:Q8NBR6}. +Q9QXN5 MIOX_MOUSE Inositol oxygenase (EC 1.13.99.1) (Aldehyde reductase-like 6) (Myo-inositol oxygenase) (MI oxygenase) (Renal-specific oxidoreductase) 285 33,164 Beta strand (3); Binding site (2); Chain (1); Helix (15); Metal binding (7); Modified residue (1); Region (3); Sequence conflict (1); Turn (3) Polyol metabolism; myo-inositol degradation into D-glucuronate; D-glucuronate from myo-inositol: step 1/1. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. TISSUE SPECIFICITY: Kidney specific. Renal proximal tubules. {ECO:0000269|PubMed:10944187}. +P01647 KV5AE_MOUSE Ig kappa chain V-V region HP 124E1 108 11,965 Beta strand (9); Chain (1); Disulfide bond (1); Helix (1); Non-terminal residue (1); Region (7); Turn (1) +P01648 KV5AF_MOUSE Ig kappa chain V-V region HP 91A3 108 11,961 Beta strand (10); Chain (1); Disulfide bond (1); Helix (1); Non-terminal residue (1); Region (7); Turn (1) +P01649 KV5AG_MOUSE Ig kappa chain V-V regions (Anti-arsonate antibodies) 108 12,057 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (7) +P01650 KV5AH_MOUSE Ig kappa chain V-V region UPC 61 108 11,809 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (7) +P01651 KV5AI_MOUSE Ig kappa chain V-V region EPC 109 108 11,876 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (7) +P01652 KV5AK_MOUSE Ig kappa chain V-V region J606 108 11,810 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (7) +P01642 KV5A9_MOUSE Ig kappa chain V-V region L7 (Fragment) 115 12,615 Beta strand (9); Chain (1); Disulfide bond (1); Helix (1); Non-terminal residue (1); Region (6); Signal peptide (1); Turn (1) +P01643 KV5AA_MOUSE Ig kappa chain V-V region MOPC 173 108 11,819 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (7) +Q9D2Y4 MLKL_MOUSE Mixed lineage kinase domain-like protein 472 54,317 Alternative sequence (1); Beta strand (11); Binding site (1); Chain (1); Coiled coil (2); Domain (1); Helix (19); Modified residue (5); Mutagenesis (8); Nucleotide binding (1); Region (1); Turn (2) FUNCTION: Pseudokinase that plays a key role in TNF-induced necroptosis, a programmed cell death process. Activated following phosphorylation by RIPK3, leading to homotrimerization, localization to the plasma membrane and execution of programmed necrosis characterized by calcium influx and plasma membrane damage. Does not have protein kinase activity (PubMed:23835476, PubMed:24012422, PubMed:24019532). Binds to highly phosphorylated inositol phosphates such as inositolhexakisphosphate (InsP6) which is essential for its necroptotic function (By similarity). {ECO:0000250|UniProtKB:Q8NB16, ECO:0000269|PubMed:23835476, ECO:0000269|PubMed:24012422, ECO:0000269|PubMed:24019532}. PTM: Phosphorylation by RIPK3 induces a conformational switch that is required for necroptosis. It also induces homotrimerization and localization to the plasma membrane. {ECO:0000269|PubMed:24012422, ECO:0000269|PubMed:24095729}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8NB16}. Cell membrane {ECO:0000250|UniProtKB:Q8NB16}. Note=Localizes to the cytoplasm and translocates to the plasma membrane on necroptosis induction. {ECO:0000250|UniProtKB:Q8NB16}. SUBUNIT: Homooligomer (By similarity). Homotrimer; forms homotrimers on necroptosis induction. Upon TNF-induced necrosis, forms in complex with PGAM5, RIPK1 and RIPK3. Within this complex, may play a role in the proper targeting of RIPK1/RIPK3 to its downstream effector PGAM5 (By similarity). Interacts with RIPK3; the interaction is direct. {ECO:0000250|UniProtKB:Q8NB16, ECO:0000269|PubMed:22265413, ECO:0000269|PubMed:23612963, ECO:0000269|PubMed:24012422, ECO:0000269|PubMed:24095729}. DOMAIN: The coiled coil region 2 is responsible for homotrimerization. {ECO:0000250}.; DOMAIN: The protein kinase domain is catalytically inactive but contains an unusual pseudoactive site with an interaction between Lys-219 and Gln-343 residues. Upon phosphorylation by RIPK3, undergoes an active conformation (PubMed:24012422, PubMed:24095729). {ECO:0000269|PubMed:24012422, ECO:0000269|PubMed:24095729}. TISSUE SPECIFICITY: Highly expressed in thymus, colon, intestine, liver, spleen and lung. Expressed at much lower level in skeletal muscle, heart and kidney. Not detected in brain. {ECO:0000269|PubMed:23835476}. +Q80Y17 L2GL1_MOUSE Lethal(2) giant larvae protein homolog 1 (LLGL) (Mgl-1) (Mlgl) 1036 112,618 Chain (1); Modified residue (5); Repeat (14); Sequence conflict (3) FUNCTION: Cortical cytoskeleton protein found in a complex involved in maintaining cell polarity and epithelial integrity. Involved in the regulation of mitotic spindle orientation, proliferation, differentiation and tissue organization of neuroepithelial cells. Involved in axonogenesis through RAB10 activation thereby regulating vesicular membrane trafficking toward the axonal plasma membrane. PTM: Phosphorylated by PRKCI on at least one of the following Ser residues: Ser 654, Ser-658, Ser-662, Ser-669 and Ser-672. Phosphorylation is important for appropriated cell polarization. {ECO:0000269|PubMed:12629547}. SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000250}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}. Cell projection, axon {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Localized to the lateral membrane during the polarization and formation cell-cell contacts. Enriched in developping axons (By similarity). {ECO:0000250}. SUBUNIT: Associated with nonmuscle myosin II heavy chain. Interacts with PRKCI/aPKC, PARD6B/Par-6 and PARD6A (By similarity). Interacts with STX4A. Interacts with RAB10 (GDP-bound form); the interaction is direct and promotes RAB10 association with membranes and activation through competition with the Rab inhibitor GDI1. Interacts with DCAF1 (By similarity). {ECO:0000250}. +Q8C4N4 LAAT1_MOUSE Lysosomal amino acid transporter 1 homolog (PQ-loop repeat-containing protein 2) 293 32,200 Alternative sequence (1); Chain (1); Domain (2); Glycosylation (2); Motif (1); Topological domain (8); Transmembrane (7) TRANSMEM 38 58 Helical. {ECO:0000255}.; TRANSMEM 72 92 Helical. {ECO:0000255}.; TRANSMEM 97 117 Helical. {ECO:0000255}.; TRANSMEM 128 148 Helical. {ECO:0000255}.; TRANSMEM 183 203 Helical. {ECO:0000255}.; TRANSMEM 215 235 Helical. {ECO:0000255}.; TRANSMEM 255 275 Helical. {ECO:0000255}. TOPO_DOM 1 37 Lumenal. {ECO:0000255}.; TOPO_DOM 59 71 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 93 96 Lumenal. {ECO:0000255}.; TOPO_DOM 118 127 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 149 182 Lumenal. {ECO:0000255}.; TOPO_DOM 204 214 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 236 254 Lumenal. {ECO:0000255}.; TOPO_DOM 276 293 Cytoplasmic. {ECO:0000255}. FUNCTION: Amino acid transporter that specifically mediates the pH-dependent export of the cationic amino acids arginine, histidine and lysine from lysosomes. {ECO:0000250}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. DOMAIN: The di-leucine motif mediates lysosomal localization. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:23169667}. +P01843 LAC1_MOUSE Ig lambda-1 chain C region 105 11,575 Beta strand (9); Chain (1); Disulfide bond (2); Domain (1); Helix (2); Non-terminal residue (1); Sequence conflict (6); Turn (2) +O08609 MLX_MOUSE Max-like protein X (Max-like bHLHZip protein) (Protein BigMax) (Transcription factor-like protein 4) 298 33,339 Alternative sequence (2); Chain (1); Domain (1); Modified residue (6); Region (1) FUNCTION: Transcription regulator. Forms a sequence-specific DNA-binding protein complex with MAD1, MAD4, MNT, WBSCR14 and MLXIP which recognizes the core sequence 5'-CACGTG-3'. The TCFL4-MAD1, TCFL4-MAD4, TCFL4-WBSCR14 complexes are transcriptional repressors. Plays a role in transcriptional activation of glycolytic target genes. Involved in glucose-responsive gene regulation. {ECO:0000269|PubMed:10593926, ECO:0000269|PubMed:11073985, ECO:0000269|PubMed:16644671}. SUBCELLULAR LOCATION: Isoform Alpha: Cytoplasm {ECO:0000250|UniProtKB:Q9UH92}. Note=Found predominantly in the cytoplasm. {ECO:0000250|UniProtKB:Q9UH92}.; SUBCELLULAR LOCATION: Isoform Beta: Cytoplasm {ECO:0000250|UniProtKB:Q9UH92}. Note=Found predominantly in the cytoplasm. {ECO:0000250|UniProtKB:Q9UH92}.; SUBCELLULAR LOCATION: Isoform Gamma: Nucleus {ECO:0000250|UniProtKB:Q9UH92}. Note=Found predominantly in the nucleus. {ECO:0000250|UniProtKB:Q9UH92}. SUBUNIT: Efficient DNA binding requires dimerization with another bHLH protein. Binds DNA as a heterodimer with MAD1, MAD4, MNT, WBSCR14 and MLXIP. Can also bind DNA as a homodimer. TISSUE SPECIFICITY: Expressed in all tissues examined: stomach, duodenum, jejunum, ileum, colon, liver, pancreas, salivary gland, kidney, spleen, lung, heart, skeletal muscle, brain, ovary and testis. {ECO:0000269|PubMed:8973301}. +Q8C7H1 MMAA_MOUSE Methylmalonic aciduria type A homolog, mitochondrial (EC 3.6.-.-) 415 45,932 Binding site (1); Chain (1); Nucleotide binding (2); Sequence conflict (1); Transit peptide (1) Cofactor biosynthesis; adenosylcobalamin biosynthesis. FUNCTION: GTPase, binds and hydrolyzes GTP. Involved in intracellular vitamin B12 metabolism, mediates the transport of cobalamin (Cbl) into mitochondria for the final steps of adenosylcobalamin (AdoCbl) synthesis. Functions as a G-protein chaperone that assists AdoCbl cofactor delivery from MMAB to the methylmalonyl-CoA mutase (MMUT) and reactivation of the enzyme during catalysis. {ECO:0000250|UniProtKB:Q8IVH4}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q8IVH4}. SUBUNIT: Homodimer. Interacts with MMUT (the apoenzyme form); the interaction is GTP dependent. {ECO:0000250|UniProtKB:Q8IVH4}. +Q99LS1 MMAD_MOUSE Methylmalonic aciduria and homocystinuria type D homolog, mitochondrial (CblD) 296 32,995 Beta strand (8); Chain (1); Helix (4); Modified residue (1); Transit peptide (1); Turn (2) FUNCTION: Involved in cobalamin metabolism. Plays a role in regulating the biosynthesis of two coenzymes, methylcobalamin and adenosylcobalamin. Plays a role in regulating the proportion of methylcobalamin and adenosylcobalamin. Promotes oxidation of cob(II)alamin bound to MMACHC. {ECO:0000250|UniProtKB:Q9H3L0}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H3L0}. Mitochondrion {ECO:0000250|UniProtKB:Q9H3L0}. SUBUNIT: Heterodimer with MMACHC. {ECO:0000250|UniProtKB:Q9H3L0}. +Q9JLI3 MMEL1_MOUSE Membrane metallo-endopeptidase-like 1 (EC 3.4.24.11) (NEP2(m)) (Neprilysin II) (NEPII) (Neprilysin-2) (NEP2) (NL2) (Neprilysin-like 1) (NL-1) (Neprilysin-like peptidase) (NEPLP) (Soluble secreted endopeptidase) [Cleaved into: Membrane metallo-endopeptidase-like 1, soluble form (Neprilysin-2 secreted) (NEP2(s))] 765 88,700 Active site (2); Alternative sequence (2); Binding site (1); Chain (2); Coiled coil (1); Disulfide bond (5); Erroneous initiation (1); Glycosylation (5); Metal binding (3); Mutagenesis (1); Sequence conflict (6); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 20 40 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 19 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 41 765 Lumenal. {ECO:0000255}. FUNCTION: Metalloprotease involved in sperm function, possibly by modulating the processes of fertilization and early embryonic development. Degrades a broad variety of small peptides with a preference for peptides shorter than 3 kDa containing neutral bulky aliphatic or aromatic amino acid residues. Shares the same substrate specificity with MME and cleaves peptides at the same amide bond. {ECO:0000269|PubMed:10542292, ECO:0000269|PubMed:11278416}. PTM: N-glycosylated. {ECO:0000269|PubMed:10542292, ECO:0000269|PubMed:10749671}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10542292}; Single-pass type II membrane protein {ECO:0000269|PubMed:10542292}. Secreted {ECO:0000269|PubMed:10542292}. Note=A secreted form produced by proteolytic cleavage also exists. TISSUE SPECIFICITY: Highly expressed in testis. Also expressed in ovary. Weakly or not expressed in brain, lung, heart, liver, kidney, adrenal gland and intestine. {ECO:0000269|PubMed:10542292}. +Q9EQR3 KCNN1_MOUSE Small conductance calcium-activated potassium channel protein 1 (SK1) (SKCa 1) (SKCa1) (KCa2.1) 537 59,330 Alternative sequence (5); Chain (1); Compositional bias (1); Intramembrane (1); Natural variant (3); Region (2); Transmembrane (5) INTRAMEM 314 334 Pore-forming; Name=Segment H5. {ECO:0000255}. TRANSMEM 108 128 Helical; Name=Segment S1. {ECO:0000255}.; TRANSMEM 137 157 Helical; Name=Segment S2. {ECO:0000255}.; TRANSMEM 176 196 Helical; Name=Segment S3. {ECO:0000255}.; TRANSMEM 225 245 Helical; Name=Segment S4. {ECO:0000255}.; TRANSMEM 274 294 Helical; Name=Segment S5. {ECO:0000255}. FUNCTION: Forms a voltage-independent potassium channel activated by intracellular calcium. Activation is followed by membrane hyperpolarization. Thought to regulate neuronal excitability by contributing to the slow component of synaptic afterhyperpolarization. The channel is blocked by apamin (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SUBUNIT: Heterooligomer. The complex is composed of 4 channel subunits each of which binds to a calmodulin subunit which regulates the channel activity through calcium-binding (By similarity). Interacts with calmodulin. {ECO:0000250, ECO:0000269|PubMed:11267657}. TISSUE SPECIFICITY: Highest expression in brain and liver with lower levels in heart, testis, kidney and colon. In colon, detected in smooth muscle cells. Expressed in atrial and ventricular myocytes with higher levels in atrial myocytes. {ECO:0000269|PubMed:11557517, ECO:0000269|PubMed:16055520}. +Q5M956 KCTD1_MOUSE BTB/POZ domain-containing protein KCTD1 257 29,405 Alternative sequence (1); Chain (1); Domain (1); Modified residue (2) FUNCTION: May repress the transcriptional activity of AP-2 family members, including TFAP2A, TFAP2B and TFAP2C to various extent. {ECO:0000250}. PTM: Sumoylated. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Can form homodimers. Interacts with TFAP2A, TFAP2B and TFAP2C via the BTB domain (By similarity). {ECO:0000250}. +Q8CEZ0 KCTD2_MOUSE BTB/POZ domain-containing protein KCTD2 266 30,145 Chain (1); Domain (1); Initiator methionine (1); Modified residue (1) +Q8BFX3 KCTD3_MOUSE BTB/POZ domain-containing protein KCTD3 815 88,862 Alternative sequence (2); Chain (1); Domain (1); Modified residue (4); Region (1); Repeat (5) FUNCTION: Accessory subunit of potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 3 (HCN3) upregulating its cell-surface expression and current density without affecting its voltage dependence and kinetics. {ECO:0000269|PubMed:23382386}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23382386}. SUBUNIT: Interacts with HCN3. {ECO:0000269|PubMed:23382386}. TISSUE SPECIFICITY: Brain (at protein level). Expressed in the liver kidney, and heart. {ECO:0000269|PubMed:23382386}. +O54982 KCNU1_MOUSE Potassium channel subfamily U member 1 (Calcium-activated potassium channel subunit alpha-3) (Calcium-activated potassium channel, subfamily M subunit alpha-3) (Pore-forming subunit of the sperm-specific alkalization activated K(+) current) (KSper) (Slowpoke homolog 3) (mSlo3) (pH-sensitive maxi potassium channel) 1121 126,870 Chain (1); Domain (1); Intramembrane (1); Motif (1); Mutagenesis (1); Region (4); Topological domain (9); Transmembrane (7) INTRAMEM 260 282 Pore-forming; Name=P region. {ECO:0000255}. TRANSMEM 25 45 Helical; Name=Segment S0. {ECO:0000255}.; TRANSMEM 102 122 Helical; Name=Segment S1. {ECO:0000255}.; TRANSMEM 138 158 Helical; Name=Segment S2. {ECO:0000255}.; TRANSMEM 166 186 Helical; Name=Segment S3. {ECO:0000255}.; TRANSMEM 189 209 Helical; Voltage-sensor; Name=Segment S4. {ECO:0000255}.; TRANSMEM 227 247 Helical; Name=Segment S5. {ECO:0000255}.; TRANSMEM 291 311 Helical; Name=Segment S6. {ECO:0000255}. TOPO_DOM 1 24 Extracellular. {ECO:0000255}.; TOPO_DOM 46 101 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 123 137 Extracellular. {ECO:0000255}.; TOPO_DOM 159 165 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 187 188 Extracellular. {ECO:0000255}.; TOPO_DOM 210 226 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 248 259 Extracellular. {ECO:0000255}.; TOPO_DOM 283 290 Extracellular. {ECO:0000255}.; TOPO_DOM 312 1121 Cytoplasmic. {ECO:0000255}. FUNCTION: Testis-specific potassium channel activated by both intracellular pH and membrane voltage that mediates export of K(+). Represents the primary spermatozoan K(+) current. In contrast to KCNMA1/SLO1, it is not activated by Ca(2+) or Mg(2+). Critical for fertility. May play an important role in sperm osmoregulation required for the acquisition of normal morphology and motility when faced with osmotic challenges, such as those experienced after mixing with seminal fluid and entry into the vagina. {ECO:0000269|PubMed:11696614, ECO:0000269|PubMed:11723163, ECO:0000269|PubMed:15201331, ECO:0000269|PubMed:16940554, ECO:0000269|PubMed:16940555, ECO:0000269|PubMed:21427226, ECO:0000269|PubMed:23129643, ECO:0000269|PubMed:9452476}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22084117}; Multi-pass membrane protein {ECO:0000269|PubMed:22084117}. SUBUNIT: Homotetramer; which constitutes the calcium-activated potassium channel. May interact with LRRC52; this interaction may change some channel gating properties, such as shifting gating to more negative potentials at a given pH. DOMAIN: The S4 segment, which is characterized by a series of positively charged amino acids at every third position, is part of the voltage-sensor. {ECO:0000250}.; DOMAIN: The pore-forming domain (also referred as P region) is imbedded into the membrane, and forms the selectivity filter of the pore. It contains the signature sequence of potassium channels that displays selectivity to potassium (By similarity). {ECO:0000250}.; DOMAIN: The RCK N-terminal domain mediates the homotetramerization, thereby promoting the assembly of monomers into functional potassium channel. {ECO:0000250}.; DOMAIN: The C-terminal cytosolic region confers the pH-dependence. TISSUE SPECIFICITY: Testis-specific. Mainly expressed in spermatocytes. {ECO:0000269|PubMed:21427226, ECO:0000269|PubMed:9452476}. +Q8BNL5 KCTD6_MOUSE BTB/POZ domain-containing protein KCTD6 237 27,624 Chain (1); Domain (1); Region (3); Sequence conflict (1) Protein modification; protein ubiquitination. FUNCTION: Probable substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex mediating the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes the ubiquitination of HDAC1; the function seems to depend on KCTD11:KCTD6 oligomerization. Can function as antagonist of the Hedgehog pathway by affecting the nuclear transfer of transcription factor GLI1; the function probably occurs via HDAC1 down-regulation, keeping GLI1 acetylated and inactive. Inhibits cell growth and tumorigenicity of medulloblastoma (MDB). Involved in regulating protein levels of ANK1 isoform Mu7 probably implicating CUL3-dependent proteasomal degradation. {ECO:0000250|UniProtKB:Q8NC69}. SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, M line {ECO:0000250|UniProtKB:Q8NC69}. Note=Colocalizes with ANK1 isoform Mu7 at the M line in differentiated skeletal muscle cells and heart. {ECO:0000250|UniProtKB:Q8NC69}. SUBUNIT: Homopentamer. Interacts with KCTD11; KCTD6 and KCTD11 may associate in heteropentameric assemblies. Interacts (via BTB domain) with CUL3; initially a 4:4 stoichiometry has been reported, however, electron microscopy revealed pentameric states with a five-pointed pinwheel shape. The interaction with CUL3 is indicative for a participation in a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex. Interacts with HDAC1; probably indirect as the interaction is requiring the presence of KCTD11. Interacts with USP21 (preferentially catalytic inactive form). Interacts with ANK1 isoform Mu7; detected in striated muscle. {ECO:0000250|UniProtKB:Q8NC69}. TISSUE SPECIFICITY: Highly expressed in cerebellum and brain. {ECO:0000269|PubMed:21472142}. +A6H8H5 KCNB2_MOUSE Potassium voltage-gated channel subfamily B member 2 (Voltage-gated potassium channel subunit Kv2.2) 907 102,336 Chain (1); Glycosylation (1); Intramembrane (2); Modified residue (1); Motif (1); Sequence conflict (1); Topological domain (8); Transmembrane (6) INTRAMEM 369 380 Helical; Name=Pore helix. {ECO:0000250|UniProtKB:P63142}.; INTRAMEM 381 388 {ECO:0000250|UniProtKB:P63142}. TRANSMEM 191 212 Helical; Name=Segment S1. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 233 254 Helical; Name=Segment S2. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 266 284 Helical; Name=Segment S3. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 297 317 Helical; Voltage-sensor; Name=Segment S4. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 333 354 Helical; Name=Segment S5. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 396 424 Helical; Name=Segment S6. {ECO:0000250|UniProtKB:P63142}. TOPO_DOM 1 190 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 213 232 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 255 265 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 285 296 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 318 332 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 355 368 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 389 395 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 425 907 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}. FUNCTION: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain and smooth muscle cells. Channels open or close in response to the voltage difference across the membrane, letting potassium ions pass in accordance with their electrochemical gradient. Homotetrameric channels mediate a delayed-rectifier voltage-dependent outward potassium current that display rapid activation and slow inactivation in response to membrane depolarization. Can form functional homotetrameric and heterotetrameric channels that contain variable proportions of KCNB1; channel properties depend on the type of alpha subunits that are part of the channel. Can also form functional heterotetrameric channels with other alpha subunits that are non-conducting when expressed alone, such as KCNS1 and KCNS2, creating a functionally diverse range of channel complexes. In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes, making it difficult to assign currents observed in intact tissues to any particular potassium channel family member. Contributes to the delayed-rectifier voltage-gated potassium current in cortical pyramidal neurons and smooth muscle cells. {ECO:0000250|UniProtKB:Q63099}. PTM: Phosphorylated. {ECO:0000250|UniProtKB:Q63099}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q63099}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q63099}. Perikaryon {ECO:0000250|UniProtKB:Q63099}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q63099}. Note=Localized uniformly throughout cell bodies and dendrites. Colocalizes with KCNB1 to high-density somatodendritic clusters on cortical pyramidal neurons. {ECO:0000250|UniProtKB:Q63099}. SUBUNIT: Homotetramer or heterotetramer with KCNB1. Heterotetramer with KCNS1 and KCNS2. {ECO:0000250|UniProtKB:Q63099}. DOMAIN: The transmembrane segment S4 functions as voltage-sensor and is characterized by a series of positively charged amino acids at every third position. Channel opening and closing is effected by a conformation change that affects the position and orientation of the voltage-sensor paddle formed by S3 and S4 within the membrane. A transmembrane electric field that is positive inside would push the positively charged S4 segment outwards, thereby opening the pore, while a field that is negative inside would pull the S4 segment inwards and close the pore. Changes in the position and orientation of S4 are then transmitted to the activation gate formed by the inner helix bundle via the S4-S5 linker region. {ECO:0000250|UniProtKB:P63142}. +Q8BJK1 KCTD7_MOUSE BTB/POZ domain-containing protein KCTD7 289 33,080 Chain (1); Domain (1); Frameshift (1); Sequence conflict (3) FUNCTION: May be involved in the control of excitability of cortical neurons. {ECO:0000269|PubMed:21710140}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. SUBUNIT: Interacts with CUL3. {ECO:0000269|PubMed:21710140}. TISSUE SPECIFICITY: High expression in brain, particularly in post-mitotic neurons. Expressed in the mitral cells of the olfactory bulbs, the hippocampus, the deep layers of the cerebral cortex and Purkinje cells of the cerebellum. Not detected in astrocytes or microglial cells. Also expressed in heart, liver, spleen and kidney. {ECO:0000269|PubMed:21710140, ECO:0000269|PubMed:22693283, ECO:0000269|PubMed:22748208}. +P97414 KCNQ1_MOUSE Potassium voltage-gated channel subfamily KQT member 1 (IKs producing slow voltage-gated potassium channel subunit alpha KvLQT1) (KQT-like 1) (Voltage-gated potassium channel subunit Kv7.1) 668 74,514 Alternative sequence (2); Chain (1); Coiled coil (1); Erroneous initiation (1); Glycosylation (1); Intramembrane (1); Modified residue (3); Motif (1); Region (3); Sequence conflict (2); Topological domain (8); Transmembrane (6) INTRAMEM 299 319 Pore-forming; Name=Segment H5. {ECO:0000255}. TRANSMEM 121 141 Helical; Name=Segment S1. {ECO:0000255}.; TRANSMEM 147 167 Helical; Name=Segment S2. {ECO:0000255}.; TRANSMEM 196 216 Helical; Name=Segment S3. {ECO:0000255}.; TRANSMEM 225 247 Helical; Voltage-sensor; Name=Segment S4. {ECO:0000255}.; TRANSMEM 261 281 Helical; Name=Segment S5. {ECO:0000255}.; TRANSMEM 331 351 Helical; Name=Segment S6. {ECO:0000255}. TOPO_DOM 1 120 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 142 146 Extracellular. {ECO:0000255}.; TOPO_DOM 168 195 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 217 224 Extracellular. {ECO:0000255}.; TOPO_DOM 248 260 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 282 298 Extracellular. {ECO:0000255}.; TOPO_DOM 320 330 Extracellular. {ECO:0000255}.; TOPO_DOM 352 668 Cytoplasmic. {ECO:0000255}. FUNCTION: Potassium channel that plays an important role in a number of tissues, including heart, inner ear, stomach and colon (By similarity) (PubMed:16314573, PubMed:11120752, PubMed:15004216). Associates with KCNE beta subunits that modulates current kinetics (By similarity) (PubMed:17597584, PubMed:15004216). Induces a voltage-dependent by rapidly activating and slowly deactivating potassium-selective outward current (By similarity) (PubMed:8900282). Promotes also a delayed voltage activated potassium current showing outward rectification characteristic (By similarity). During beta-adrenergic receptor stimulation participates in cardiac repolarization by associating with KCNE1 to form the I(Ks) cardiac potassium current that increases the amplitude and slows down the activation kinetics of outward potassium current I(Ks) (By similarity) (PubMed:15004216, PubMed:17597584). Muscarinic agonist oxotremorine-M strongly suppresses KCNQ1/KCNE1 current (By similarity). When associated with KCNE3, forms the potassium channel that is important for cyclic AMP-stimulated intestinal secretion of chloride ions (By similarity). This interaction with KCNE3 is reduced by 17beta-estradiol, resulting in the reduction of currents (By similarity). During conditions of increased substrate load, maintains the driving force for proximal tubular and intestinal sodium ions absorption, gastric acid secretion, and cAMP-induced jejunal chloride ions secretion (PubMed:16314573). Allows the provision of potassium ions to the luminal membrane of the secretory canaliculus in the resting state as well as during stimulated acid secretion (PubMed:19491250). When associated with KCNE2, forms an heterooligomer complex leading to currents with an apparently instantaneous activation, a rapid deactivation process and a linear current-voltage relationship and decreases the amplitude of the outward current (By similarity). When associated with KCNE4, inhibits voltage-gated potassium channel activity (By similarity). When associated with KCNE5, this complex only conducts current upon strong and continued depolarization (By similarity). Also forms a heterotetramer with KCNQ5; has a voltage-gated potassium channel activity (By similarity). Binds with phosphatidylinositol 4,5-bisphosphate (By similarity). {ECO:0000250|UniProtKB:P51787, ECO:0000250|UniProtKB:Q9Z0N7, ECO:0000269|PubMed:11120752, ECO:0000269|PubMed:15004216, ECO:0000269|PubMed:16314573, ECO:0000269|PubMed:17597584, ECO:0000269|PubMed:19491250, ECO:0000269|PubMed:8900282}. PTM: Phosphorylation at Ser-27 by PKA; increases delayed rectifier potassium channel activity of the KCNQ1-KCNE1 complex through a macromolecular complex that includes PKA, PP1, and the targeting protein AKAP9. {ECO:0000250|UniProtKB:P51787}.; PTM: Ubiquitinated by NEDD4L; promotes internalization. The ubiquitinylated form is internalized through a clathrin-mediated endocytosis by interacting with AP2M1 and is recycled back to the cell membrane via RAB4A and RAB11A. {ECO:0000250|UniProtKB:P51787}.; PTM: Deubiquitinated by USP2; counteracts the NEDD4L-specific down-regulation of I(Ks) and restores the membrane localization. {ECO:0000250|UniProtKB:P51787}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P51787}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P51787}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P51787}. Early endosome {ECO:0000250|UniProtKB:P51787}. Membrane raft {ECO:0000250|UniProtKB:P51787}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P51787}. Basolateral cell membrane {ECO:0000250|UniProtKB:P51787}. Note=Colocalized with KCNE3 at the plasma membrane. Upon 17beta-oestradiol treatment, colocalizes with RAB5A at early endosome. Heterotetramer with KCNQ5 is highly retained at the endoplasmic reticulum and is localized outside of lipid raft microdomains. During the early stages of epithelial cell polarization induced by the calcium switch it removed from plasma membrane to the endoplasmic reticulum where it retained and it is redistributed to the basolateral cell surface in a PI3K-dependent manner at a later stage. {ECO:0000250|UniProtKB:P51787}. SUBUNIT: Tetramer (By similarity). Heterotetramer with KCNE1; form the native cardiac channel I(Ks) which increases the amplitude and slows down the activation kinetics of outward potassium current and targets to the membrane raft (By similarity) (PubMed:8900282). Interacts (via C-terminus) with CALM; forms a heterotetramer in a calcium-independent manner. Interacts with AKAP9; targets protein kinase A (PKA) catalytic and regulatory subunits and protein phosphatase 1 (PP1) to the KCNQ1-KCNE1 complex, allowing PKA-mediated phosphorylation and increase of delayed rectifier potassium channel activity. Interacts with KCNE2; form an heterooligomer complex that targets to the membrane raft and leading to currents with an apparently instantaneous activation, a rapid deactivation process and a linear current-voltage relationship and decreases the amplitude of the outward current. Interacts with AP2M1; mediates estrogen-induced internalization via clathrin-coated vesicles. Interacts with NEDD4L; promotes internalization and decreases I(Ks) currents. Interacts with USP2; counteracts the NEDD4L-specific down-regulation of I(Ks) and restore plasma membrane localization. Heterotetramer with KCNQ5; has a voltage-gated potassium channel activity. Interacts with KCNE3; alters membrane raft localization. Interacts with KCNE4; impairs KCNQ1 localization in lipid rafts and inhibits voltage-gated potassium channel activity. Interacts with KCNE5; impairs KCNQ1 localization in lipid rafts and only conducts current upon strong and continued depolarization (By similarity). {ECO:0000250|UniProtKB:P51787, ECO:0000269|PubMed:8900282}. DOMAIN: The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position. {ECO:0000250|UniProtKB:P51787}.; DOMAIN: The coiled-coil domain mediates tetramerization. {ECO:0000250|UniProtKB:P51787}.; DOMAIN: The segment S6 is involved in the inhibition of voltage-gated potassium channel activity by KCNE4. {ECO:0000250|UniProtKB:P51787}.; DOMAIN: The C-terminal assembly domain promotes self-interactiona; allows functional channel. {ECO:0000250|UniProtKB:P51787}. TISSUE SPECIFICITY: Expressed in heart, kidney and salivary glands. Detected in the cochlea. Almost undetectable in brain, skeletal muscle and liver. Widely expressed in embryonic and neonatal tissues. {ECO:0000269|PubMed:9618174}. +Q9JK97 KCNQ4_MOUSE Potassium voltage-gated channel subfamily KQT member 4 (KQT-like 4) (Potassium channel subunit alpha KvLQT4) (Voltage-gated potassium channel subunit Kv7.4) 696 77,057 Chain (1); Coiled coil (1); Intramembrane (1); Motif (1); Region (1); Sequence conflict (4); Topological domain (8); Transmembrane (6) INTRAMEM 271 292 Pore-forming; Name=Segment H5. {ECO:0000255}. TRANSMEM 98 118 Helical; Name=Segment S1. {ECO:0000255}.; TRANSMEM 132 152 Helical; Name=Segment S2. {ECO:0000255}.; TRANSMEM 173 193 Helical; Name=Segment S3. {ECO:0000255}.; TRANSMEM 202 224 Helical; Voltage-sensor; Name=Segment S4. {ECO:0000255}.; TRANSMEM 238 258 Helical; Name=Segment S5. {ECO:0000255}.; TRANSMEM 297 317 Helical; Name=Segment S6. {ECO:0000255}. TOPO_DOM 1 97 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 119 131 Extracellular. {ECO:0000255}.; TOPO_DOM 153 172 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 194 201 Extracellular. {ECO:0000255}.; TOPO_DOM 225 237 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 259 270 Extracellular. {ECO:0000255}.; TOPO_DOM 293 296 Extracellular. {ECO:0000255}.; TOPO_DOM 318 695 Cytoplasmic. {ECO:0000255}. FUNCTION: Probably important in the regulation of neuronal excitability. May underlie a potassium current involved in regulating the excitability of sensory cells of the cochlea. SUBCELLULAR LOCATION: Basal cell membrane; Multi-pass membrane protein. Note=Situated at the basal membrane of cochlear outer hair cells. SUBUNIT: Homotetramer. May form heteromultimers with KCNQ3 (By similarity). Interacts with HSP90AB1; promotes cell surface expression of KCNQ4 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P56696}. DOMAIN: The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position. {ECO:0000250}.; DOMAIN: The A-domain tail carries the major determinants of channel assembly specificity. Its coiled-coil region is Four-stranded (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: In the inner ear expressed in the outer sensory hair cells of the cochlea and in type I hair cells of the vestibular organs. Also expressed in the postsynaptic membrane of the calyx nerve endings innervating type I cells. In the brain expressed in neurons of many, but not all, nuclei of the central auditory pathway. Absent from most other brain regions. {ECO:0000269|PubMed:10760300}. +A2A9F4 KDF1_MOUSE Keratinocyte differentiation factor 1 397 43,496 Chain (1); Compositional bias (2); Frameshift (1); Modified residue (1) FUNCTION: Plays a role in the regulation of the epidermis formation during early development. Required both as an inhibitor of basal cell proliferation and a promoter of differentiation of basal progenitor cell progeny. {ECO:0000269|PubMed:24075906}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24075906}. Cell junction {ECO:0000269|PubMed:24075906}. Note=Localized at cell borders in single layered keratinocytes. Localized at cell borders in the basal and spinous layers but is more diffusely localized in the granular layer. Colocalized with actin near the cell membrane, especially in cellular protrusions. +Q64507 KRA51_MOUSE Keratin-associated protein 5-1 (Ultra high sulfur serine protein 1) (UHS-Ser-1) 230 21,782 Alternative sequence (1); Chain (1); Region (1); Repeat (14); Sequence conflict (1) FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated protein (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins. {ECO:0000305}. SUBUNIT: Interacts with hair keratins. {ECO:0000305}. TISSUE SPECIFICITY: Expressed during the active phases of the hair cycle in the medulla and the inner root sheath of the forming hair. Also expressed in the upper layers of the epidermis of skin. {ECO:0000269|PubMed:2250030}. +Q9D5Z7 KRA52_MOUSE Keratin-associated protein 5-2 189 17,234 Chain (1); Region (1); Repeat (8) FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated protein (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins. {ECO:0000305}. SUBUNIT: Interacts with hair keratins. {ECO:0000305}. +Q9D226 KRA53_MOUSE Keratin-associated protein 5-3 196 17,777 Chain (1); Compositional bias (2); Region (1); Repeat (2) FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated protein (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins. {ECO:0000305}. SUBUNIT: Interacts with hair keratins. {ECO:0000305}. +Q8VDQ9 KRI1_MOUSE Protein KRI1 homolog 704 82,057 Chain (1); Compositional bias (1); Erroneous initiation (1); Modified residue (13); Sequence caution (1) +Q6S5J6 KRIT1_MOUSE Krev interaction trapped protein 1 (Krev interaction trapped 1) (Cerebral cavernous malformations 1 protein homolog) 736 83,982 Alternative sequence (3); Chain (1); Domain (1); Region (3); Repeat (4); Sequence conflict (6) FUNCTION: Component of the CCM signaling pathway which is a crucial regulator of heart and vessel formation and integrity. Negative regulator of angiogenesis. Inhibits endothelial proliferation, apoptosis, migration, lumen formation and sprouting angiogenesis in primary endothelial cells. Promotes AKT phosphorylation in a NOTCH-dependent and independent manner, and inhibits ERK1/2 phosphorylation indirectly through activation of the DELTA-NOTCH cascade. Acts in concert with CDH5 to establish and maintain correct endothelial cell polarity and vascular lumen and these effects are mediated by recruitment and activation of the Par polarity complex and RAP1B. Required for the localization of phosphorylated PRKCZ, PARD3, TIAM1 and RAP1B to the cell junction, and cell junction stabilization. Plays a role in integrin signaling via its interaction with ITGB1BP1; this prevents the interaction between ITGB1 and ITGB1BP1. Microtubule-associated protein that binds to phosphatidylinositol 4,5-bisphosphate (PIP2)-containing membranes in a GTP-bound RAP1-dependent manner (By similarity). Plays an important role in the maintenance of the intracellular reactive oxygen species (ROS) homeostasis to prevent oxidative cellular damage. Regulates the homeostasis of intracellular ROS through an antioxidant pathway involving FOXO1 and SOD2. Facilitates the down-regulation of cyclin-D1 (CCND1) levels required for cell transition from proliferative growth to quiescence by preventing the accumulation of intracellular ROS through the modulation of FOXO1 and SOD2 levels. {ECO:0000250|UniProtKB:O00522, ECO:0000269|PubMed:20332120, ECO:0000269|PubMed:20616044, ECO:0000269|PubMed:20668652}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell junction {ECO:0000250}. Note=KRIT1 and CDH5 reciprocally regulate their localization to endothelial cell-cell junctions. Association with RAP1 relocalizes KRIT1 from microtubules to cell junction membranes. Translocates from the cytoplasm along microtubules to the cell membrane in an ITGB1BP1-dependent manner (By similarity). {ECO:0000250}. SUBUNIT: Found in a complex, at least composed of ITGB1BP1, KRIT1 and RAP1A. Interacts (via C-terminus FERM domain) with RAP1A (active GTP-bound form preferentially); the interaction does not induce the opening conformation of KRIT1. Interacts (via N-terminus NPXY motif) with ITGB1BP1; the interaction induces the opening conformation of KRIT1 and competes with ITGB1 for ITGB1BP1 interaction. Associates (via N-terminus and C-terminus regions) with microtubules; the interaction is inhibited in presence of ITGB1BP1 and active GTP-bound RAP1A. Interacts (via FERM domain) with RAP1B. Interacts with CDH5. Interacts with RAP1A (By similarity). Interacts with HEG1 and CCM2; greatly facilitates CCM2-binding to HEG1 (PubMed:19151727). {ECO:0000250|UniProtKB:O00522, ECO:0000269|PubMed:19151727}. DOMAIN: The FERM domain mediates binding to RAP1A and RAP1B and is necessary for binding to phosphatidylinositol 4,5-bisphosphate (PIP2). {ECO:0000250|UniProtKB:O00522}.; DOMAIN: The N-terminal domain has structural similarity to the nudix hydrolase domain, despite the absence of a nudix box and low sequence similarity with nudix hydrolase domains. The N-terminus and the C-terminus part associate together via the NPAY binding motif and adopt a lose conformation that is disrupted by ITGB1BP1, but not by RAP1A. {ECO:0000250|UniProtKB:O00522}.; DOMAIN: Contains 4 ANK repeats that precede the FERM domain. {ECO:0000250|UniProtKB:O00522}. TISSUE SPECIFICITY: Expressed in heart, brain, spleen, lung, thymus, kidney and testis. Isoform 2 was more frequently expressed in the thymus than isoform 1. {ECO:0000269|PubMed:12172908, ECO:0000269|PubMed:14697511}. +Q99M74 KRT82_MOUSE Keratin, type II cuticular Hb2 (Keratin-82) (K82) (Type II hair keratin Hb2) (Type-II keratin Kb22) 516 57,140 Chain (1); Domain (1); Region (7); Sequence conflict (1) SUBUNIT: Heterotetramer of two type I and two type II keratins. {ECO:0000250}. +Q99M73 KRT84_MOUSE Keratin, type II cuticular Hb4 (65 kDa type II keratin) (Keratin-84) (K84) (Type II hair keratin Hb4) (Type-II keratin Kb24) 603 64,983 Chain (1); Domain (1); Region (7); Sequence conflict (2) SUBUNIT: Heterotetramer of two type I and two type II keratins. {ECO:0000250}. TISSUE SPECIFICITY: In skin, only expressed in the suprabasal cells of tail scale epidermis. Suprabasally expressed in stratified squamous epithelia and also in the posterior unit of the complex filiform papillae of tongue. Expressed in rare anatomical sites in which an orthokeratinized stratum corneum would be too soft and a hard keratinized structure would be too rigid to meet the functional requirement of the respective epithelia. {ECO:0000269|PubMed:1385239}. +P97861 KRT86_MOUSE Keratin, type II cuticular Hb6 (Keratin-86) (K86) (Type II hair keratin Hb6) (Type-II keratin Kb26) 486 53,251 Chain (1); Cross-link (1); Domain (1); Region (7) SUBUNIT: Heterotetramer of two type I and two type II keratins. +Q6IMF0 KRT87_MOUSE Keratin, type II cuticular 87 (Keratin-87) (K87) 495 54,629 Chain (1); Domain (1); Region (7); Sequence conflict (1) SUBUNIT: Heterotetramer of two type I and two type II keratins. {ECO:0000305}. +Q9Z2B9 KS6A4_MOUSE Ribosomal protein S6 kinase alpha-4 (S6K-alpha-4) (EC 2.7.11.1) (90 kDa ribosomal protein S6 kinase 4) (Nuclear mitogen- and stress-activated protein kinase 2) (RSK-like protein kinase) (RLSK) 773 85,652 Active site (2); Binding site (2); Chain (1); Domain (3); Modified residue (12); Nucleotide binding (2); Sequence conflict (2) FUNCTION: Serine/threonine-protein kinase that is required for the mitogen or stress-induced phosphorylation of the transcription factors CREB1 and ATF1 and for the regulation of the transcription factor RELA, and that contributes to gene activation by histone phosphorylation and functions in the regulation of inflammatory genes. Phosphorylates CREB1 and ATF1 in response to mitogenic or stress stimuli such as UV-C irradiation, epidermal growth factor (EGF) and anisomycin. Plays an essential role in the control of RELA transcriptional activity in response to TNF. Phosphorylates 'Ser-10' of histone H3 in response to mitogenics, stress stimuli and EGF, which results in the transcriptional activation of several immediate early genes, including proto-oncogenes c-fos/FOS and c-jun/JUN. May also phosphorylate 'Ser-28' of histone H3. Mediates the mitogen- and stress-induced phosphorylation of high mobility group protein 1 (HMGN1/HMG14). In lipopolysaccharide-stimulated primary macrophages, acts downstream of the Toll-like receptor TLR4 to limit the production of pro-inflammatory cytokines. Functions probably by inducing transcription of the MAP kinase phosphatase DUSP1 and the anti-inflammatory cytokine interleukin 10 (IL10), via CREB1 and ATF1 transcription factors (By similarity). {ECO:0000250, ECO:0000269|PubMed:11909979, ECO:0000269|PubMed:16517600, ECO:0000269|PubMed:18690222}. PTM: Ser-343 and Thr-568 phosphorylation is required for kinase activity. Ser-343 and Ser-196 are autophosphorylated by the C-terminal kinase domain, and their phosphorylation is essential for the catalytic activity of the N-terminal kinase domain. Phosphorylated at Ser-343, Thr-568 and Thr-687 by MAPK1/ERK2, MAPK3/ERK1 and MAPK14/p38-alpha. Autophosphorylated at Ser-737 and Ser-745 by the N-terminal kinase domain (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Forms a complex with either MAPK1/ERK2 or MAPK3/ERK1 in quiescent cells which transiently dissociates following mitogenic stimulation. Also associates with MAPK14/p38-alpha. Activated RPS6KA4 associates with and phosphorylates the NF-kappa-B p65 subunit RELA (By similarity). {ECO:0000250}. +Q3UVC0 KSR2_MOUSE Kinase suppressor of Ras 2 (EC 2.7.11.1) 959 108,572 Active site (1); Binding site (2); Chain (1); Compositional bias (2); Domain (1); Metal binding (8); Modified residue (4); Nucleotide binding (1); Zinc finger (1) FUNCTION: Location-regulated scaffold connecting MEK to RAF. Has very low protein kinase activity and can phosphorylate MAP2K1 at several Ser and Thr residues with very low efficiency (in vitro). Interaction with BRAF enhances KSR2-mediated phosphorylation of MAP2K1 (in vitro). Blocks MAP3K8 kinase activity and MAP3K8-mediated signaling. Acts as a negative regulator of MAP3K3-mediated activation of ERK, JNK and NF-kappa-B pathways, inhibiting MAP3K3-mediated interleukin-8 production (By similarity). {ECO:0000250}. PTM: Phosphorylated on Ser-484 by MARK3. {ECO:0000250|UniProtKB:Q61097}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q61097}. Membrane {ECO:0000250|UniProtKB:Q61097}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q61097}. SUBUNIT: Interacts with MAP2K1, forming a heterodimer that can dimerize to form a heterotetramer. Interacts with MAP3K8, MAPK, RAS and RAF. Interacts with BRAF; this increases the low intrinsic protein kinase activity of KSR2 (By similarity). {ECO:0000250}. DOMAIN: The protein kinase domain is predicted to be catalytically inactive and seems to have very low intrinsic kinase activity. This low kinase activity can be increased by interaction with BRAF (By similarity). {ECO:0000255|PROSITE-ProRule:PRU00159}. +Q8BSK8 KS6B1_MOUSE Ribosomal protein S6 kinase beta-1 (S6K-beta-1) (S6K1) (EC 2.7.11.1) (70 kDa ribosomal protein S6 kinase 1) (P70S6K1) (p70-S6K 1) (Ribosomal protein S6 kinase I) (S6K) (p70 ribosomal S6 kinase alpha) (p70 S6 kinase alpha) (p70 S6K-alpha) (p70 S6KA) 525 59,146 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Domain (2); Modified residue (9); Motif (1); Nucleotide binding (1); Region (1); Sequence conflict (1) FUNCTION: Serine/threonine-protein kinase that acts downstream of mTOR signaling in response to growth factors and nutrients to promote cell proliferation, cell growth and cell cycle progression. Regulates protein synthesis through phosphorylation of EIF4B, RPS6 and EEF2K, and contributes to cell survival by repressing the pro-apoptotic function of BAD. Under conditions of nutrient depletion, the inactive form associates with the EIF3 translation initiation complex. Upon mitogenic stimulation, phosphorylation by the mammalian target of rapamycin complex 1 (mTORC1) leads to dissociation from the EIF3 complex and activation. The active form then phosphorylates and activates several substrates in the pre-initiation complex, including the EIF2B complex and the cap-binding complex component EIF4B. Also controls translation initiation by phosphorylating a negative regulator of EIF4A, PDCD4, targeting it for ubiquitination and subsequent proteolysis. Promotes initiation of the pioneer round of protein synthesis by phosphorylating POLDIP3/SKAR. In response to IGF1, activates translation elongation by phosphorylating EEF2 kinase (EEF2K), which leads to its inhibition and thus activation of EEF2. Also plays a role in feedback regulation of mTORC2 by mTORC1 by phosphorylating RICTOR, resulting in the inhibition of mTORC2 and AKT1 signaling. Mediates cell survival by phosphorylating the pro-apoptotic protein BAD and suppressing its pro-apoptotic function. Phosphorylates mitochondrial RMP leading to dissociation of a RMP:PPP1CC complex. The free mitochondrial PPP1CC can then dephosphorylate RPS6KB1 at Thr-412, which is proposed to be a negative feedback mechanism for the RPS6KB1 anti-apoptotic function. Mediates TNF-alpha-induced insulin resistance by phosphorylating IRS1 at multiple serine residues, resulting in accelerated degradation of IRS1. In cells lacking functional TSC1-2 complex, constitutively phosphorylates and inhibits GSK3B. May be involved in cytoskeletal rearrangement through binding to neurabin. Phosphorylates and activates the pyrimidine biosynthesis enzyme CAD, downstream of MTOR (By similarity) (PubMed:11493700, PubMed:11500364, PubMed:15060135, PubMed:18952604). Following activation by mTORC1, phosphorylates EPRS and thereby plays a key role in fatty acid uptake by adipocytes and also most probably in interferon-gamma-induced translation inhibition (PubMed:28178239). {ECO:0000250|UniProtKB:P23443, ECO:0000269|PubMed:11493700, ECO:0000269|PubMed:11500364, ECO:0000269|PubMed:15060135, ECO:0000269|PubMed:18952604, ECO:0000269|PubMed:28178239}. PTM: Phosphorylation at Thr-412 is regulated by mTORC1. The phosphorylation at this site is maintained by an agonist-dependent autophosphorylation mechanism. Activated by phosphorylation at Thr-252 by PDPK1. Dephosphorylation by PPP1CC at Thr-412 in mitochondrion (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell junction, synapse, synaptosome {ECO:0000250}. Mitochondrion outer membrane {ECO:0000269|PubMed:11493700}. Mitochondrion {ECO:0000250}. Note=Colocalizes with URI1 at mitochondrion. {ECO:0000250}. SUBUNIT: Interacts with PPP1R9A/neurabin-1. Interacts with RPTOR. Interacts with IRS1. Interacts with EIF3B and EIF3C. Interacts with TRAF4. Interacts with POLDIP3. Interacts (via N-terminus) with IER5. {ECO:0000250|UniProtKB:P23443, ECO:0000250|UniProtKB:P67999}. DOMAIN: The autoinhibitory domain is believed to block phosphorylation within the AGC-kinase C-terminal domain and the activation loop. {ECO:0000250}.; DOMAIN: The TOS (TOR signaling) motif is essential for activation by mTORC1. {ECO:0000250}. +Q9CRB9 MIC19_MOUSE MICOS complex subunit Mic19 (Coiled-coil-helix-coiled-coil-helix domain-containing protein 3) 227 26,335 Chain (1); Disulfide bond (2); Domain (1); Initiator methionine (1); Lipidation (1); Modified residue (7); Motif (2); Mutagenesis (1) FUNCTION: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. Has also been shown to function as a transcription factor which binds to the BAG1 promoter and represses BAG1 transcription. Plays an important role in the maintenance of the MICOS complex stability and the mitochondrial cristae morphology. {ECO:0000250|UniProtKB:Q9NX63, ECO:0000269|PubMed:21081504}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:21081504}; Lipid-anchor {ECO:0000269|PubMed:21081504}; Intermembrane side {ECO:0000269|PubMed:21081504}. Cytoplasm {ECO:0000250|UniProtKB:Q9NX63}. Nucleus {ECO:0000250|UniProtKB:Q9NX63}. Mitochondrion {ECO:0000250|UniProtKB:Q9NX63}. SUBUNIT: Component of the mitochondrial contact site and cristae organizing system (MICOS) complex, composed of at least MINOS1/MIC10, CHCHD3/MIC19, CHCHD6/MIC25, APOOL/MIC27, IMMT/MIC60, APOO/MIC23/MIC26 and QIL1/MIC13. This complex was also known under the names MINOS or MitOS complex. The MICOS complex associates with mitochondrial outer membrane proteins SAMM50, MTX1 and MTX2 (together described as components of the mitochondrial outer membrane sorting assembly machinery (SAM) complex) and DNAJC11, mitochondrial inner membrane protein TMEM11 and with HSPA9. The MICOS and SAM complexes together with DNAJC11 are part of a large protein complex spanning both membranes termed the mitochondrial intermembrane space bridging (MIB) complex (By similarity). Interacts with HSPA1A/HSPA1B and OPA1, preferentially with the soluble OPA1 form. {ECO:0000250|UniProtKB:Q9NX63, ECO:0000269|PubMed:21081504}. +Q91VN4 MIC25_MOUSE MICOS complex subunit Mic25 (Coiled-coil-helix-coiled-coil-helix domain-containing protein 6) 273 29,852 Chain (1); Coiled coil (1); Disulfide bond (2); Domain (1); Frameshift (1); Initiator methionine (1); Lipidation (1); Modified residue (3); Motif (2); Sequence conflict (3) FUNCTION: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. {ECO:0000250|UniProtKB:Q9BRQ6}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9BRQ6}; Lipid-anchor {ECO:0000250|UniProtKB:Q9BRQ6}. Mitochondrion {ECO:0000250|UniProtKB:Q9BRQ6}. SUBUNIT: Component of the mitochondrial contact site and cristae organizing system (MICOS) complex, composed of at least MINOS1/MIC10, CHCHD3/MIC19, CHCHD6/MIC25, APOOL/MIC27, IMMT/MIC60, APOO/MIC23/MIC26 and QIL1/MIC13. This complex was also known under the names MINOS or MitOS complex. The MICOS complex associates with mitochondrial outer membrane proteins SAMM50, MTX1 and MTX2 (together described as components of the mitochondrial outer membrane sorting assembly machinery (SAM) complex) and DNAJC11, mitochondrial inner membrane protein TMEM11 and with HSPA9. The MICOS and SAM complexes together with DNAJC11 are part of a large protein complex spanning both membranes termed the mitochondrial intermembrane space bridging (MIB) complex. Interacts with DISC1. Interacts with IMMT/MIC60. {ECO:0000250|UniProtKB:Q9BRQ6}. +Q9DCZ4 MIC26_MOUSE MICOS complex subunit Mic26 (Apolipoprotein O) (MICOS complex subunit Mic23) (Protein FAM121B) 198 22,604 Alternative sequence (2); Chain (1); Glycosylation (1); Signal peptide (1); Transmembrane (1) TRANSMEM 108 128 Helical. {ECO:0000255}. FUNCTION: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. Plays a crucial role in crista junction formation and mitochondrial function (By similarity). Can induce cardiac lipotoxicity by enhancing mitochondrial respiration and fatty acid metabolism in cardiac myoblasts (PubMed:24743151). Promotes cholesterol efflux from macrophage cells. Detected in HDL, LDL and VLDL. Secreted by a microsomal triglyceride transfer protein (MTTP)-dependent mechanism, probably as a VLDL-associated protein that is subsequently transferred to HDL (By similarity). {ECO:0000250|UniProtKB:Q9BUR5, ECO:0000269|PubMed:24743151}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9BUR5}; Single-pass membrane protein {ECO:0000255}. Mitochondrion {ECO:0000269|PubMed:24743151}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9BUR5}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9BUR5}. Note=Exists in three distinct forms: a glycosylated and secreted form, an ER/Golgi-resident form and a non-glycosylated mitochondrial form. {ECO:0000250|UniProtKB:Q9BUR5}. SUBUNIT: Component of the mitochondrial contact site and cristae organizing system (MICOS) complex, composed of at least MINOS1/MIC10, CHCHD3/MIC19, CHCHD6/MIC25, APOOL/MIC27, IMMT/MIC60, APOO/MIC23/MIC26 and QIL1/MIC13. This complex was also known under the names MINOS or MitOS complex. The MICOS complex associates with mitochondrial outer membrane proteins SAMM50, MTX1 and MTX2 (together described as components of the mitochondrial outer membrane sorting assembly machinery (SAM) complex) and DNAJC11, mitochondrial inner membrane protein TMEM11 and with HSPA9. The MICOS and SAM complexes together with DNAJC11 are part of a large protein complex spanning both membranes termed the mitochondrial intermembrane space bridging (MIB) complex. Interacts with IMMT/MIC60. Interacts with MINOS1/MIC10 and APOOL/MIC27. {ECO:0000250|UniProtKB:Q9BUR5}. +Q8VDP3 MICA1_MOUSE [F-actin]-monooxygenase MICAL1 (EC 1.14.13.225) (Molecule interacting with CasL protein 1) (MICAL-1) (mMical1) (NEDD9-interacting protein with calponin homology and LIM domains) 1048 116,785 Alternative sequence (2); Beta strand (21); Binding site (4); Chain (1); Coiled coil (3); Domain (3); Helix (29); Metal binding (8); Modified residue (4); Nucleotide binding (2); Region (1); Sequence conflict (1); Turn (9) FUNCTION: Monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2) (By similarity). Acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. Also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L; acts by antagonizing STK38 and STK38L activation by MST1/STK4. Involved in regulation of lamina-specific connectivity in the nervous system such as the development of lamina-restricted hippocampal connections. Through redox regulation of the actin cytoskeleton controls the intracellular distribution of secretory vesicles containing L1/neurofascin/NgCAM family proteins in neurons, thereby regulating their cell surface levels. May act as Rab effector protein and play a role in vesicle trafficking. {ECO:0000250|UniProtKB:Q8TDZ2, ECO:0000269|PubMed:21730291, ECO:0000269|PubMed:23911929, ECO:0000269|PubMed:25007825, ECO:0000269|PubMed:26935886}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8TDZ2}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q8TDZ2}. SUBUNIT: Associates with the SH3 domain of NEDD9. Interacts with VIM and PLXNA3. Interacts with RAB1B, RAB8A, RAB10, RAB13 and RAB15 (in their GTP-bound forms); binding to RAB1B is of low affinity compared to other Rab proteins; at least in case of RAB8A and RAB10 can bind 2 molecules of the Rab proteins simultaneously (By similarity). Interacts with STK38 and STK38L. {ECO:0000250, ECO:0000250|UniProtKB:Q8TDZ2, ECO:0000269|PubMed:16275925, ECO:0000269|PubMed:18094055, ECO:0000269|PubMed:21730291}. DOMAIN: The C-terminal coiled coil part contains the plexin-interacting region.; DOMAIN: The bivalent Mical/EHBP Rab binding (bMERB) domain, mediates binding to predominantly Rab8, Rab10, Rab10, Rab13 and Rab15 (in their GTP-bound forms). {ECO:0000250|UniProtKB:Q8TDZ2}. TISSUE SPECIFICITY: Expressed in the postnatal and adult hippocampus; found in dentate gyrus, the polymorphic layer, cornu ammonis (CA) 1-3 and in mossy fibers of the striatum lucidum. In adult hippocampus strongly expressed in CA3 pyramidial neurons. {ECO:0000269|PubMed:25007825}. +Q8BML1 MICA2_MOUSE [F-actin]-monooxygenase MICAL2 (EC 1.14.13.225) (Molecule interacting with CasL protein 2) (MICAL-2) (mMical2) 960 110,072 Alternative sequence (3); Binding site (4); Chain (1); Domain (2); Erroneous initiation (1); Metal binding (8); Modified residue (2); Motif (1); Nucleotide binding (2); Region (1) FUNCTION: Nuclear monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization (PubMed:23911929, PubMed:23927065). In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2) (By similarity). Acts as a key regulator of the SRF signaling pathway elicited by nerve growth factor and serum: mediates oxidation and subsequent depolymerization of nuclear actin, leading to increase MKL1/MRTF-A presence in the nucleus and promote SRF:MKL1/MRTF-A-dependent gene transcription. Does not activate SRF:MKL1/MRTF-A through RhoA (By similarity). {ECO:0000250|UniProtKB:O94851, ECO:0000250|UniProtKB:Q8TDZ2, ECO:0000269|PubMed:23911929, ECO:0000269|PubMed:23927065}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O94851}. SUBUNIT: Interacts with PLXNA4 (PubMed:12110185). Interacts with RAB1B (By similarity). {ECO:0000250|UniProtKB:O94851, ECO:0000269|PubMed:12110185}. +Q9D5U9 MICLK_MOUSE MICAL C-terminal-like protein (Mical-cL) (ERK2-binding testicular protein 1) (Ebitein-1) 680 75,324 Alternative sequence (3); Chain (1); Coiled coil (2); Compositional bias (1); Domain (1); Erroneous initiation (1); Modified residue (1); Mutagenesis (1); Region (1); Sequence conflict (2) FUNCTION: May cooperate with MAPK1/ERK2 via an intracellular signal transduction pathway in the morphogenetic development of round spermatids to spermatozoa. May act as Rab effector protein and play a role in vesicle trafficking. {ECO:0000250|UniProtKB:Q6ZW33, ECO:0000269|PubMed:18241670}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18241670}. SUBUNIT: Interacts with MAPK1/ERK2. Interacts with RAB1B, RAB35, RAB8A, RAB10, RAB13 and RAB15 (in their GTP-bound forms); binding to RAB1B and RAB35 is of low affinity compared to other Rab proteins; binding to RAB1B and RAB35 is of low affinity compared to other Rab proteins; at least in case of RAB8A may bind 2 molecules of RAB8A simultaneously through a high and a low affinity binding site, respectively. {ECO:0000250|UniProtKB:Q6ZW33, ECO:0000269|PubMed:18241670, ECO:0000269|PubMed:18590835}. DOMAIN: The C-terminal RAB-binding domain (RBD), also described as bivalent Mical/EHBP Rab binding (bMERB) domain, mediates binding to predominantly Rab8, Rab10, Rab10, Rab13 and Rab15 (in their GTP-bound forms). {ECO:0000250|UniProtKB:Q6ZW33}. TISSUE SPECIFICITY: Expressed only in testis (at protein level). {ECO:0000269|PubMed:18241670}. +Q5NCS9 MID49_MOUSE Mitochondrial dynamics protein MID49 (Mitochondrial dynamics protein of 49 kDa homolog) (Mitochondrial elongation factor 2) (Smith-Magenis syndrome chromosomal region candidate gene 7 protein homolog) 454 49,624 Beta strand (13); Chain (1); Helix (14); Topological domain (2); Transmembrane (1); Turn (6) TRANSMEM 23 43 Helical. {ECO:0000255}. TOPO_DOM 1 22 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 44 454 Cytoplasmic. {ECO:0000255}. FUNCTION: Mitochondrial outer membrane protein which regulates mitochondrial fission. Promotes the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface independently of the mitochondrial fission FIS1 and MFF proteins. Regulates DNM1L GTPase activity. {ECO:0000269|PubMed:23283981, ECO:0000269|PubMed:24508339}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:24508339}; Single-pass membrane protein {ECO:0000269|PubMed:24508339}. Note=Colocalizes with DNM1L at mitochondrial membrane. Forms foci and rings around mitochondria. SUBUNIT: Interacts with DNM1L. {ECO:0000250}. +Q5UAK0 MIER1_MOUSE Mesoderm induction early response protein 1 (Early response 1) (Er1) (Mi-er1) 511 57,908 Alternative sequence (4); Chain (1); Compositional bias (1); Cross-link (2); Domain (2); Erroneous initiation (1); Modified residue (11) FUNCTION: Transcriptional repressor regulating the expression of a number of genes including SP1 target genes. Probably functions through recruitment of HDAC1 a histone deacetylase involved in chromatin silencing. {ECO:0000269|PubMed:16147882}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00512, ECO:0000255|PROSITE-ProRule:PRU00624}. SUBUNIT: Interacts with HDAC1. Part of a complex containing at least CDYL, MIER1, MIER2, HDAC1 and HDAC2. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed. Isoform 1 is only expressed in testis. {ECO:0000269|PubMed:16147882}. +Q3U3N0 MIER2_MOUSE Mesoderm induction early response protein 2 (Mi-er2) 541 59,268 Alternative sequence (3); Chain (1); Domain (2); Erroneous initiation (1); Modified residue (1) FUNCTION: Transcriptional repressor. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00512, ECO:0000255|PROSITE-ProRule:PRU00624}. SUBUNIT: Part of a complex containing at least CDYL, MIER1, MIER2, HDAC1 and HDAC2. {ECO:0000250}. +P97930 KTHY_MOUSE Thymidylate kinase (EC 2.7.4.9) (dTMP kinase) 212 23,915 Alternative sequence (1); Chain (1); Initiator methionine (1); Modified residue (1); Nucleotide binding (1); Sequence conflict (2) Pyrimidine metabolism; dTTP biosynthesis. FUNCTION: Catalyzes the conversion of dTMP to dTDP. +Q8BGT6 MILK1_MOUSE MICAL-like protein 1 (Molecule interacting with Rab13) (MIRab13) 870 94,079 Alternative sequence (3); Chain (1); Coiled coil (2); Compositional bias (1); Domain (3); Erroneous initiation (1); Modified residue (12); Motif (2); Region (2); Sequence conflict (1) FUNCTION: Probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. On endosome membranes, may act as a downstream effector of Rab proteins recruiting cytosolic proteins to regulate membrane tubulation. May be involved in a late step of receptor-mediated endocytosis regulating for instance endocytosed-EGF receptor trafficking. Alternatively, may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. May indirectly play a role in neurite outgrowth. {ECO:0000269|PubMed:23572513}. SUBCELLULAR LOCATION: Recycling endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Late endosome membrane {ECO:0000250}. Note=Localization to late endosomes is actin-dependent. Association to tubular recycling endosomes is regulated by RAB35 and ARF6 (By similarity). {ECO:0000250}. SUBUNIT: Homooligomer (Probable). Interacts (via NPF1 motif) with EHD1 (via EH domain); the interaction is direct and probably recruits EHD1 to membranes. Interacts with EHD3 (via EH domain). Interacts with RAB35 (GTP-bound form); the interaction is direct and probably recruits MICALL1 to membranes. Interacts with ACAP2; the interaction is indirect through RAB35. Interacts with RAB8A (GTP-bound form); regulates RAB8A association with recycling endosomes. Interacts with RAB13 (GTP-bound form). Interacts with ARF6 (GTP-bound form). Interacts with PACSIN2 (via the SH3 domain). Interacts with DPYSL2. {ECO:0000269|PubMed:18094055, ECO:0000269|PubMed:23572513, ECO:0000305}. DOMAIN: Probably exists in a closed and an opened conformation due to interaction of the C-terminal RAB-binding domain (RBD), also described as bivalent Mical/EHBP Rab binding (bMERB) domain, with the N-terminal calponin-homology (CH) domain. The conformational change is regulated by RAB13 and may modulate MICALL1 interactions with functional partners (By similarity). {ECO:0000250}. +Q3TB92 MILR1_MOUSE Allergin-1 (Allergy inhibitory receptor 1) (Mast cell antigen 32) (MCA-32) (Mast cell Ag-32) (Mast cell immunoglobulin-like receptor 1) 246 27,366 Alternative sequence (1); Chain (1); Disulfide bond (1); Domain (1); Erroneous initiation (1); Glycosylation (1); Modified residue (2); Motif (2); Mutagenesis (2); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 151 171 Helical. {ECO:0000255}. TOPO_DOM 34 150 Extracellular. {ECO:0000255}.; TOPO_DOM 172 246 Cytoplasmic. {ECO:0000255}. FUNCTION: Immunoglobulin-like receptor which plays an inhibitory role in degranulation of mast cells. Negatively regulates IgE-mediated mast cell activation and suppresses the type I immediate hypersensitivity reaction. {ECO:0000269|PubMed:20526344}. PTM: N-glycosylated. {ECO:0000269|PubMed:20526344}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20526344}; Single-pass type I membrane protein {ECO:0000269|PubMed:20526344}.; SUBCELLULAR LOCATION: Isoform 2: Secreted {ECO:0000305}. SUBUNIT: Monomer (Probable). Interacts (tyrosine-phosphorylated) with PTPN6, PTPN11 and INPP5D. {ECO:0000269|PubMed:20526344, ECO:0000305}. TISSUE SPECIFICITY: Expressed in myeloid cells (dendritic cells, macrophages and neutrophils but not in T-cells, B-cells or natural killer cells) and mast cells (at protein level). {ECO:0000269|PubMed:20526344}. +Q9D1R2 KTI12_MOUSE Protein KTI12 homolog 351 38,445 Chain (1); Erroneous initiation (1); Modified residue (4); Nucleotide binding (1) +Q8BPI1 KTU_MOUSE Protein kintoun (Dynein assembly factor 2, axonemal) 814 88,327 Alternative sequence (1); Chain (1); Erroneous initiation (5); Modified residue (2); Sequence conflict (3) FUNCTION: Required for cytoplasmic pre-assembly of axonemal dyneins, thereby playing a central role in motility in cilia and flagella. Involved in pre-assembly of dynein arm complexes in the cytoplasm before intraflagellar transport loads them for the ciliary compartment. {ECO:0000255|HAMAP-Rule:MF_03069}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03069}. Note=Localizes in the apical cytoplasm around the gamma-tubulin-positive pericentriolar region, not in the cilia. {ECO:0000255|HAMAP-Rule:MF_03069}. SUBUNIT: Interacts with DNAI2 and HSPA1A (PubMed:19052621). Interacts with CFAP300. Interacts with DNAAF4. Interacts with PIH1D3 (By similarity). {ECO:0000255|HAMAP-Rule:MF_03069, ECO:0000269|PubMed:19052621}. TISSUE SPECIFICITY: Expressed in nearly all organs of adult, with higher expression in tissues known to have motile cilia and flagella, such as brain and testis. {ECO:0000269|PubMed:19052621}. +A6H611 MIPEP_MOUSE Mitochondrial intermediate peptidase (MIP) (EC 3.4.24.59) 711 80,852 Active site (1); Chain (1); Metal binding (3); Modified residue (1); Sequence conflict (5); Transit peptide (1) FUNCTION: Cleaves proteins, imported into the mitochondrion, to their mature size. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. +Q9D9F8 MIPO1_MOUSE Mirror-image polydactyly gene 1 protein homolog 279 31,751 Chain (1); Coiled coil (2) +Q149C2 MIPT3_MOUSE TRAF3-interacting protein 1 (Intraflagellar transport protein 54 homolog) (Microtubule-interacting protein associated with TRAF3) (MIP-T3) 625 71,037 Chain (1); Coiled coil (1); Compositional bias (1); Helix (8); Modified residue (2); Mutagenesis (1); Region (2); Sequence caution (1); Sequence conflict (3); Turn (2) FUNCTION: Plays an inhibitory role on IL13 signaling by binding to IL13RA1. Involved in suppression of IL13-induced STAT6 phosphorylation, transcriptional activity and DNA-binding. Recruits TRAF3 and DISC1 to the microtubules (By similarity). Involved in epithelial morphogenesis and in the regulation of microtubule cytoskeleton organization. Is a negative regulator of microtubule stability, acting through the control of MAP4 levels (PubMed:26487268). Involved in ciliogenesis (PubMed:21945076). {ECO:0000250|UniProtKB:Q8TDR0, ECO:0000269|PubMed:21945076, ECO:0000269|PubMed:26487268}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q8TDR0}. Cell projection, cilium {ECO:0000269|PubMed:19253336}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:21945076}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:21945076}. Note=Microtubules. In the cilium, it is observed at the ciliary base, ciliary transition zone and ciliary tip. {ECO:0000250|UniProtKB:Q8TDR0}. SUBUNIT: Interacts with IL13RA1. Binds to microtubules, TRAF3 and DISC1 (By similarity). Component of the IFT complex B, at least composed of IFT20, IFT22, HSPB11/IFT25, IFT27, IFT46, IFT52, TRAF3IP1/IFT54, IFT57, IFT74, IFT80, IFT81, and IFT88. Interacts with IFT88. Interacts with MAP4 (PubMed:26487268). {ECO:0000250, ECO:0000269|PubMed:19253336, ECO:0000269|PubMed:26487268}. +P51180 MIP_MOUSE Lens fiber major intrinsic protein (Aquaporin-0) (MIP26) (MP26) 263 28,193 Chain (1); Intramembrane (4); Modified residue (3); Motif (3); Natural variant (1); Region (1); Sequence conflict (3); Site (1); Topological domain (7); Transmembrane (6) INTRAMEM 62 67 {ECO:0000250}.; INTRAMEM 68 78 Helical. {ECO:0000250}.; INTRAMEM 177 183 {ECO:0000250}.; INTRAMEM 184 194 Helical. {ECO:0000250}. TRANSMEM 9 32 Helical. {ECO:0000250}.; TRANSMEM 39 61 Helical. {ECO:0000250}.; TRANSMEM 85 107 Helical. {ECO:0000250}.; TRANSMEM 127 147 Helical. {ECO:0000250}.; TRANSMEM 160 176 Helical. {ECO:0000250}.; TRANSMEM 201 219 Helical. {ECO:0000250}. TOPO_DOM 1 8 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 33 38 Extracellular. {ECO:0000250}.; TOPO_DOM 79 84 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 108 126 Extracellular. {ECO:0000250}.; TOPO_DOM 148 159 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 195 200 Extracellular. {ECO:0000250}.; TOPO_DOM 220 263 Cytoplasmic. {ECO:0000250}. FUNCTION: Water channel. Channel activity is down-regulated by CALM when cytoplasmic Ca(2+) levels are increased. May be responsible for regulating the osmolarity of the lens. Interactions between homotetramers from adjoining membranes may stabilize cell junctions in the eye lens core. {ECO:0000250|UniProtKB:Q6J8I9}. PTM: Subject to partial proteolytic cleavage in the eye lens core. Partial proteolysis promotes interactions between tetramers from adjoining membranes (By similarity). {ECO:0000250}.; PTM: Fatty acylated at Met-1 and Lys-238. The acyl modifications, in decreasing order of ion abundance, are: oleoyl (C18:1) > palmitoyl (C16:0) > stearoyl (C18:0) > eicosenoyl (C20:1) > dihomo-gamma-linolenoyl (C20:3) > palmitoleoyl (C16:1) > eicosadienoyl (C20:2). {ECO:0000250|UniProtKB:P30301}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P30301}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q6J8I9}. Cell junction, gap junction {ECO:0000250|UniProtKB:P30301}. SUBUNIT: Homotetramer. Homooctamer formed by head-to-head interaction between homotetramers from adjoining membranes. Interacts with CALM; one CALM molecule interacts with the cytoplasmic domains of two aquaporins, leading to channel closure. {ECO:0000250|UniProtKB:P06624}. DOMAIN: Aquaporins contain two tandem repeats each containing two membrane-spanning helices and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA). Each tandem repeat contains a loop and a short helix that enter and leave the lipid bilayer on the same side (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Major component of lens fiber gap junctions. DISEASE: Note=Defects in Mip are a cause of autosomal dominant cataract. The cataract Fraser mutation (Cat-Fr or Shrivelled) is a transposon-induced splicing error that substitutes a long terminal repeat sequence for the C-terminus of Mip. The lens opacity mutation (LOP) is an AA substitution that inhibits targeting of Mip to the cell-membrane. +P01626 KV2A1_MOUSE Ig kappa chain V-II region MOPC 167 112 12,349 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (7) +P01629 KV2A4_MOUSE Ig kappa chain V-II region 2S1.3 112 12,221 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (7) +P03977 KV3A4_MOUSE Ig kappa chain V-III region 50S10.1 111 12,042 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (7) +P01657 KV3A5_MOUSE Ig kappa chain V-III region PC 2413 111 11,949 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (7) +P01658 KV3A6_MOUSE Ig kappa chain V-III region MOPC 321 132 14,525 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (7); Signal peptide (1) +P01659 KV3A7_MOUSE Ig kappa chain V-III region TEPC 124 112 12,340 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (7) +P01660 KV3A8_MOUSE Ig kappa chain V-III region PC 3741/TEPC 111 111 12,099 Beta strand (11); Chain (1); Disulfide bond (1); Helix (1); Non-terminal residue (1); Region (7); Turn (1) +P01661 KV3A9_MOUSE Ig kappa chain V-III region MOPC 63 131 14,291 Beta strand (10); Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (7); Signal peptide (1); Turn (1) +P01666 KV3AE_MOUSE Ig kappa chain V-III region PC 7183 111 11,952 Beta strand (10); Chain (1); Disulfide bond (1); Helix (1); Non-terminal residue (1); Region (7); Turn (1) +P01669 KV3AH_MOUSE Ig kappa chain V-III region PC 7769 111 12,011 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (7) +P01670 KV3AI_MOUSE Ig kappa chain V-III region PC 6684 111 12,040 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (7) +P01680 KV4A1_MOUSE Ig kappa chain V-IV region S107B 129 13,834 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (7); Signal peptide (1) +P01633 KV5A1_MOUSE Ig kappa chain V19-17 (Ig kappa chain V-V region MPC11) 149 16,434 Chain (1); Non-terminal residue (1); Region (7); Repeat (2); Signal peptide (1) +P01634 KV5A2_MOUSE Ig kappa chain V-V region MOPC 21 136 14,902 Beta strand (9); Chain (1); Helix (1); Non-terminal residue (1); Region (7); Signal peptide (1); Turn (1) +P01638 KV5A6_MOUSE Ig kappa chain V-V region L6 (Fragment) 115 12,986 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (6); Signal peptide (1) +P01639 KV5A7_MOUSE Ig kappa chain V-V region MOPC 41 130 14,311 Chain (1); Disulfide bond (1); Natural variant (1); Non-terminal residue (1); Region (7); Signal peptide (1) +P01646 KV5AD_MOUSE Ig kappa chain V-V region HP 123E6 108 11,989 Beta strand (10); Chain (1); Disulfide bond (1); Helix (1); Non-terminal residue (1); Region (7); Turn (1) +P01676 KV6A2_MOUSE Ig kappa chain V-VI region XRPC 24 107 11,584 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (7) +P01677 KV6A3_MOUSE Ig kappa chain V-VI region TEPC 601/TEPC 191 107 11,568 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (7) +P01678 KV6A4_MOUSE Ig kappa chain V-VI region SAPC 10 107 11,554 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (7) +P01679 KV6A5_MOUSE Ig kappa chain V-VI region J539 107 11,502 Beta strand (8); Chain (1); Disulfide bond (1); Helix (1); Non-terminal residue (1); Region (7); Turn (1) +P04940 KV6A6_MOUSE Ig kappa chain V-VI region NQ2-17.4.1 107 11,561 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (7) FUNCTION: Anti-2-phenyl oxazolone (PHOX) Antibody. +P04941 KV6A7_MOUSE Ig kappa chain V-VI region NQ2-48.2.2 107 11,557 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (7) FUNCTION: Anti-2-phenyl oxazolone (PHOX) Antibody. +P04943 KV6A9_MOUSE Ig kappa chain V-VI region NQ6-8.3.1 107 11,573 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (7) FUNCTION: Anti-2-phenyl oxazolone (PHOX) Antibody. +Q8VHK5 MLC1_MOUSE Membrane protein MLC1 382 41,596 Chain (1); Compositional bias (1); Modified residue (3); Transmembrane (8) TRANSMEM 58 78 Helical. {ECO:0000255}.; TRANSMEM 88 107 Helical. {ECO:0000255}.; TRANSMEM 117 137 Helical. {ECO:0000255}.; TRANSMEM 148 168 Helical. {ECO:0000255}.; TRANSMEM 205 225 Helical. {ECO:0000255}.; TRANSMEM 234 254 Helical. {ECO:0000255}.; TRANSMEM 263 283 Helical. {ECO:0000255}.; TRANSMEM 309 329 Helical. {ECO:0000255}. FUNCTION: Regulates the response of astrocytes to hypo-osmosis by promoting calcium influx. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cell membrane {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. SUBUNIT: Interacts with ATP1B1. Part of a complex containing ATP1B1, TRPV4, AQP4 and HEPACAM. {ECO:0000250}. +Q9QWV4 MLF1_MOUSE Myeloid leukemia factor 1 (Hematopoietic lineage switch 7) (Myelodysplasia-myeloid leukemia factor 1) 267 30,432 Chain (1); Modified residue (4); Mutagenesis (2); Region (1); Sequence conflict (2) FUNCTION: Involved in lineage commitment of primary hemopoietic progenitors by restricting erythroid formation and enhancing myeloid formation. Interferes with erythropoietin-induced erythroid terminal differentiation by preventing cells from exiting the cell cycle through suppression of CDKN1B/p27Kip1 levels. Suppresses COP1 activity via CSN3 which activates p53 and induces cell cycle arrest. Binds DNA and affects the expression of a number of genes so may function as a transcription factor in the nucleus. {ECO:0000269|PubMed:10523300, ECO:0000269|PubMed:15122318}. PTM: Phosphorylation is required for binding to YWHAZ. {ECO:0000269|PubMed:12176995}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10523300}. Nucleus {ECO:0000269|PubMed:10523300}. Cell projection, cilium {ECO:0000269|PubMed:27914912}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:27914912}. Note=Shuttles between the cytoplasm and nucleus. {ECO:0000269|PubMed:17008314}. SUBUNIT: Interacts with CENPU (By similarity). Also interacts with NRBP1/MADM, YWHAZ/14-3-3-zeta and HNRPUL2/MANP. NRBP1 recruits a serine kinase which phosphorylates both itself and MLF1. Phosphorylated MLF1 then binds to YWHAZ and is retained in the cytoplasm. Retained in the nucleus by binding to HNRPUL2. Binds to COPS3/CSN3 which is required for suppression of COP1 and activation of p53. {ECO:0000250, ECO:0000269|PubMed:12176995, ECO:0000269|PubMed:17008314}. TISSUE SPECIFICITY: Highly expressed in skeletal muscle, heart, testis. Also found in lung, but not in spleen, thymus, bone marrow, liver and kidney. {ECO:0000269|PubMed:10393836}. +Q99KX1 MLF2_MOUSE Myeloid leukemia factor 2 (Myelodysplasia-myeloid leukemia factor 2) 247 28,055 Chain (1); Modified residue (3) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. +Q80XH1 KXDL1_MOUSE KxDL motif-containing protein 1 177 19,977 Chain (1); Modified residue (1) FUNCTION: As part of the BORC complex may play a role in lysosomes movement and localization at the cell periphery. Associated with the cytosolic face of lysosomes, the BORC complex may recruit ARL8B and couple lysosomes to microtubule plus-end-directed kinesin motor (By similarity). May also be involved in the biogenesis of lysosome-related organelles such as melanosomes (PubMed:22554196). {ECO:0000250|UniProtKB:Q9BQD3, ECO:0000269|PubMed:22554196}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q9BQD3}. SUBUNIT: Component of the BLOC-one-related complex (BORC) which is composed of BLOC1S1, BLOC1S2, BORCS5, BORCS6, BORCS7, BORCS8, KXD1 and SNAPIN (By similarity). Associates with the BLOC-1 complex. Interacts with BLOC1S1. Interacts with DTNBP1/BLOC1S7 (via coiled-coil domain) (PubMed:22554196). {ECO:0000250|UniProtKB:Q9BQD3, ECO:0000269|PubMed:22554196}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:22554196}. +Q9CV60 MLN_MOUSE Myoregulin 46 5,175 Chain (1); Erroneous gene model prediction (1); Erroneous initiation (1); Mutagenesis (5); Topological domain (2); Transmembrane (1) TRANSMEM 22 42 Helical. {ECO:0000255}. TOPO_DOM 1 21 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 43 46 Lumenal. {ECO:0000305}. FUNCTION: Inhibits the activity of ATP2A1/SERCA1 ATPase in sarcoplasmic reticulum by decreasing the apparent affinity of the ATPase for Ca(2+), thereby acting as a key regulator of skeletal muscle activity. Its high expression in adult skeletal muscle, suggests that it constitutes the predominant regulator of ATP2A1/SERCA1 in adult skeletal muscle. {ECO:0000269|PubMed:25640239, ECO:0000269|PubMed:26816378}. SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:25640239}; Single-pass membrane protein {ECO:0000305|PubMed:25640239}. SUBUNIT: Interacts with ATP2A1/SERCA1. {ECO:0000269|PubMed:25640239}. TISSUE SPECIFICITY: Specifically expressed in all skeletal muscles. Not expressed in cardiac or smooth muscles. {ECO:0000269|PubMed:25640239}. +Q91VR7 MLP3A_MOUSE Microtubule-associated proteins 1A/1B light chain 3A (Autophagy-related protein LC3 A) (Autophagy-related ubiquitin-like modifier LC3 A) (MAP1 light chain 3-like protein 1) (MAP1A/MAP1B light chain 3 A) (MAP1A/MAP1B LC3 A) (Microtubule-associated protein 1 light chain 3 alpha) 121 14,272 Chain (1); Lipidation (1); Modified residue (1); Propeptide (1); Region (1); Sequence conflict (1); Site (1) FUNCTION: Ubiquitin-like modifier involved in formation of autophagosomal vacuoles (autophagosomes). Whereas LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation. {ECO:0000250|UniProtKB:Q9H492}. PTM: The precursor molecule is cleaved by ATG4B to form the cytosolic form, LC3-I. This is activated by APG7L/ATG7, transferred to ATG3 and conjugated to phospholipid to form the membrane-bound form, LC3-II. {ECO:0000269|PubMed:12207896, ECO:0000269|PubMed:14530254}.; PTM: Phosphorylation at Ser-12 by PKA inhibits conjugation to phosphatidylethanolamine (PE). Interaction with MAPK15 reduces the inhibitory phosphorylation and increases autophagy activity. {ECO:0000250|UniProtKB:Q9H492}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Endomembrane system; Lipid-anchor. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:Q9H492}. Note=LC3-II binds to the autophagic membranes. {ECO:0000250}. SUBUNIT: 3 different light chains, LC1, LC2 and LC3, can associate with MAP1A and MAP1B proteins (By similarity). Interacts with TP53INP1 and TP53INP2. Directly interacts with SQSTM1; this interaction leads to MAP1LC3A recruitment to inclusion bodies containing polyubiquitinated protein aggregates and to inclusion body degradation by autophagy. Interacts with ATG13. Interacts with ULK1. Interacts with TBC1D5. Found in a complex with UBQLN1 and UBQLN2. Interacts with UBQLN4 (via STI1 1 and 2 domains). Interacts with UBQLN1 in the presence of UBQLN4. Interacts with TRIM5. Interacts with MEFV. Interacts with RETREG1, RETREG2 and RETREG3 (By similarity). {ECO:0000250|UniProtKB:Q9H492}. +Q9CQV6 MLP3B_MOUSE Microtubule-associated proteins 1A/1B light chain 3B (Autophagy-related protein LC3 B) (Autophagy-related ubiquitin-like modifier LC3 B) (MAP1 light chain 3-like protein 2) (MAP1A/MAP1B light chain 3 B) (MAP1A/MAP1B LC3 B) (Microtubule-associated protein 1 light chain 3 beta) 125 14,617 Beta strand (4); Chain (1); Helix (5); Lipidation (1); Modified residue (1); Propeptide (1); Sequence conflict (1); Site (1); Turn (1) FUNCTION: Ubiquitin-like modifier involved in formation of autophagosomal vacuoles (autophagosomes). Plays a role in mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Whereas LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation. Promotes primary ciliogenesis by removing OFD1 from centriolar satellites via the autophagic pathway. {ECO:0000250|UniProtKB:Q9GZQ8}. PTM: The precursor molecule is cleaved by ATG4B to form the cytosolic form, LC3-I. This is activated by APG7L/ATG7, transferred to ATG3 and conjugated to phospholipid to form the membrane-bound form, LC3-II. {ECO:0000250|UniProtKB:Q9GZQ8}.; PTM: Phosphorylation at Ser-12 by PKA inhibits conjugation to phosphatidylethanolamine (PE) (By similarity). Interaction with MAPK15 reduces the inhibitory phosphorylation and increases autophagy activity (By similarity). {ECO:0000250|UniProtKB:Q9GZQ8}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Endomembrane system; Lipid-anchor. Cytoplasmic vesicle, autophagosome membrane; Lipid-anchor. Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:Q9GZQ8}. Note=LC3-II binds to the autophagic membranes (By similarity). Localizes also to discrete punctae along the ciliary axoneme. {ECO:0000250}. SUBUNIT: 3 different light chains, LC1, LC2 and LC3, can associate with MAP1A and MAP1B proteins (By similarity). Interacts at microtubules with CABP1 (via EF-hands 1 and 2) but not with calmodulin. Interacts with FYCO1 (via C-terminus). Interacts with TP53INP1 and TP53INP2 (By similarity). Interacts with TBC1D25 (PubMed:21383079). Directly interacts with SQSTM1; this interaction leads to MAP1LC3B recruitment to inclusion bodies containing polyubiquitinated protein aggregates and to inclusion body degradation by autophagy. Interacts with ATG4B, MAPK15 and BNIP3. Interacts with MAPB1, KEAP1, PCM1, OFD1, CEP131, and TECPR2. Interacts with TBC1D5. Found in a complex with UBQLN1 and UBQLN2. Interacts with UBQLN4 (via STI1 1 and 2 domains). Interacts with UBQLN1 in the presence of UBQLN4. Interacts with ATG13. Interacts with RETREG1, RETREG2 and RETREG3 (By similarity). Interacts with PLCL1; the interaction inhibits autophagosome formation (PubMed:23399561). Interacts with TRIM16. Interacts with CRY1 and PER2 (PubMed:29937374). {ECO:0000250|UniProtKB:Q9GZQ8, ECO:0000269|PubMed:21383079, ECO:0000269|PubMed:23399561, ECO:0000269|PubMed:29937374}. +P97457 MLRS_MOUSE Myosin regulatory light chain 2, skeletal muscle isoform (Fast skeletal myosin light chain 2) (MLC2F) 169 18,955 Calcium binding (1); Chain (1); Domain (3); Initiator methionine (1); Modified residue (7) SUBUNIT: Myosin is a hexamer of 2 heavy chains and 4 light chains. +P51667 MLRV_MOUSE Myosin regulatory light chain 2, ventricular/cardiac muscle isoform (MLC-2) (MLC-2v) (Myosin light chain 2, slow skeletal/ventricular muscle isoform) (MLC-2s/v) 166 18,864 Calcium binding (1); Chain (1); Domain (3); Initiator methionine (1); Modified residue (5); Mutagenesis (3); Sequence conflict (3) FUNCTION: Contractile protein that plays a role in heart development and function (PubMed:10409661). Following phosphorylation, plays a role in cross-bridge cycling kinetics and cardiac muscle contraction by increasing myosin lever arm stiffness and promoting myosin head diffusion; as a consequence of the increase in maximum contraction force and calcium sensitivity of contraction force. These events altogether slow down myosin kinetics and prolong duty cycle resulting in accumulated myosins being cooperatively recruited to actin binding sites to sustain thin filament activation as a means to fine-tune myofilament calcium sensitivity to force (By similarity) (PubMed:22426213, PubMed:16908724, PubMed:10409661). During cardiogenesis plays an early role in cardiac contractility by promoting cardiac myofibril assembly (PubMed:9422794). {ECO:0000250|UniProtKB:P08733, ECO:0000269|PubMed:10409661, ECO:0000269|PubMed:16908724, ECO:0000269|PubMed:22426213, ECO:0000269|PubMed:9422794}. PTM: N-terminus is methylated by METTL11A/NTM1. {ECO:0000269|PubMed:20668449}.; PTM: Phosphorylated by MYLK3 and MYLK2; promotes cardiac muscle contraction and function. Dephosphorylated by PPP1CB complexed to PPP1R12B (By similarity). The phosphorylated form in adult is expressed as gradients across the heart from endocardium (low phosphorylation) to epicardium (high phosphorylation); regulates cardiac torsion and workload distribution (PubMed:22426213). {ECO:0000250|UniProtKB:P08733, ECO:0000269|PubMed:22426213, ECO:0000269|PubMed:23095280}. SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, A band {ECO:0000250|UniProtKB:P08733}. SUBUNIT: Myosin is a hexamer of 2 heavy chains and 4 light chains (By similarity). Interacts with MYOC (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P10916}. TISSUE SPECIFICITY: Abundantly expressed in both cardiac and slow skeletal muscle (PubMed:1379240). In the adult heart, the phosphorylated form is highly expressed in epicardium and weakly in endocardium (PubMed:22426213). {ECO:0000269|PubMed:1379240, ECO:0000269|PubMed:22426213}. +Q3TJ91 L2GL2_MOUSE Lethal(2) giant larvae protein homolog 2 (Lethal giant larvae-like protein 2) 1027 114,323 Chain (1); Modified residue (3); Repeat (14); Sequence conflict (12) FUNCTION: Part of a complex with GPSM2/LGN, PRKCI/aPKC and PARD6B/Par-6, which may ensure the correct organization and orientation of bipolar spindles for normal cell division. This complex plays roles in the initial phase of the establishment of epithelial cell polarity (By similarity). {ECO:0000250}. PTM: Phosphorylated at Ser-653 by PRKCI. Phosphorylation is enhanced during cell polarization induced by calcium. Phosphorylation may occur during the cell-cell contact-induced cell polarization and may contribute to the segregation of LLGL2 from the PRKCI/aPKC and PARD6B/Par-6 complex (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Localized in the perinuclear structure and faintly at the cell-cell contacts sites in the interphase. Localized at the cell periphery during metaphase. Cortical localization in mitotic cells (By similarity). {ECO:0000250}. SUBUNIT: Interacts with GPSM2/LGN, PRKCI/aPKC and PARD6B/Par-6. The complex is enhanced during mitosis. Interacts with DCAF1 (By similarity). {ECO:0000250}. +Q91YP0 L2HDH_MOUSE L-2-hydroxyglutarate dehydrogenase, mitochondrial (EC 1.1.99.2) (Duranin) 464 50,899 Chain (1); Modified residue (2); Sequence conflict (5); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. +P11627 L1CAM_MOUSE Neural cell adhesion molecule L1 (N-CAM-L1) (NCAM-L1) (CD antigen CD171) 1260 140,969 Chain (1); Disulfide bond (6); Domain (11); Glycosylation (21); Modified residue (7); Motif (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1124 1146 Helical. {ECO:0000255}. TOPO_DOM 20 1123 Extracellular. {ECO:0000255}.; TOPO_DOM 1147 1260 Cytoplasmic. {ECO:0000255}. FUNCTION: Neural cell adhesion molecule involved in the dynamics of cell adhesion and in the generation of transmembrane signals at tyrosine kinase receptors. During brain development, critical in multiple processes, including neuronal migration, axonal growth and fasciculation, and synaptogenesis. In the mature brain, plays a role in the dynamics of neuronal structure and function, including synaptic plasticity. {ECO:0000250|UniProtKB:P32004}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q05695}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q05695}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q05695}. Note=Colocalized with SHTN1 in close apposition with actin filaments in filopodia and lamellipodia of axonalne growth cones of hippocampal neurons. {ECO:0000250|UniProtKB:Q05695}. SUBUNIT: Interacts with SHTN1; the interaction occurs in axonal growth cones. {ECO:0000250|UniProtKB:Q05695}. TISSUE SPECIFICITY: Expressed in the brain, including in the molecular layer of the cerebellar cortex, the fiber-rich layers of the hippocampus (alveus, and strata lacunosum moleculare, radiatum, and oriens), the nerve fiber layer and the inner and outer plexiform layers of the retina, and in the molecular layer of the olfactory bulb (at protein level). {ECO:0000269|PubMed:12514225}. +Q9D071 MMS19_MOUSE MMS19 nucleotide excision repair protein homolog (MET18 homolog) (MMS19-like protein) 1031 113,089 Alternative sequence (3); Chain (1); Initiator methionine (1); Modified residue (2); Repeat (4); Sequence conflict (3) FUNCTION: Key component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into apoproteins specifically involved in DNA metabolism and genomic integrity. In the CIA complex, MMS19 acts as an adapter between early-acting CIA components and a subset of cellular target Fe/S proteins such as ERCC2/XPD, FANCJ and RTEL1, thereby playing a key role in nucleotide excision repair (NER), homologous recombination-mediated double-strand break DNA repair, DNA replication and RNA polymerase II (POL II) transcription. As a CIA complex component and in collaboration with CIAO1 and CIAO2, binds to and facilitates the assembly of most cytosolic-nuclear Fe/S proteins. As part of the mitotic spindle-associated MMXD complex, plays a role in chromosome segregation, probably by facilitating iron-sulfur cluster assembly into ERCC2/XPD. Indirectly acts as a transcriptional coactivator of estrogen receptor (ER), via its role in iron-sulfur insertion into some component of the TFIIH-machinery. {ECO:0000250|UniProtKB:Q96T76}. PTM: Ubiquitinated; undergoes 'Lys-48'-linked polyubiquitination. {ECO:0000250|UniProtKB:Q96T76}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96T76}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q96T76}. SUBUNIT: Component of the CIA complex. In the CIA complex, interacts directly with CIAO2B and CIAO3. Component of the MMXD complex, composed of CIAO1, ERCC2, CIAO2B, MMS19 and SLC25A5. Interacts with CIAO2B; the interaction is direct. Interacts with ERCC2/XPD; the interaction is direct. Interacts with ERCC3/XPB and NCOA3/RAC3. Interacts with RTEL1; the interaction mediates the association of RTEL1 with the CIA complex. Interacts with BRIP1. {ECO:0000250|UniProtKB:Q96T76}. TISSUE SPECIFICITY: Ubiquitously expressed with higher expression in testis. {ECO:0000269|PubMed:11328871}. +Q8BG84 LAIR1_MOUSE Leukocyte-associated immunoglobulin-like receptor 1 (LAIR-1) (mLAIR1) (CD antigen CD305) 263 29,793 Alternative sequence (5); Beta strand (9); Chain (1); Disulfide bond (1); Domain (1); Erroneous translation (2); Frameshift (1); Glycosylation (2); Helix (2); Modified residue (2); Motif (2); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (2) TRANSMEM 145 165 Helical. {ECO:0000255}. TOPO_DOM 22 144 Extracellular. {ECO:0000255}.; TOPO_DOM 166 263 Cytoplasmic. {ECO:0000255}. FUNCTION: Functions as an inhibitory receptor that plays a constitutive negative regulatory role on cytolytic function of natural killer (NK) cells, B-cells and T-cells. Activation by Tyr phosphorylation results in recruitment and activation of the phosphatases PTPN6 and PTPN11. It also reduces the increase of intracellular calcium evoked by B-cell receptor ligation. May also play its inhibitory role independently of SH2-containing phosphatases. Modulates cytokine production in CD4+ T-cells, down-regulating IL2 and IFNG production while inducing secretion of transforming growth factor beta. Down-regulates also IgG and IgE production in B-cells as well as IL8, IL10 and TNF secretion. Inhibits proliferation and induces apoptosis in myeloid leukemia cell lines as well as prevents nuclear translocation of NF-kappa-B p65 subunit/RELA and phosphorylation of I-kappa-B alpha/CHUK in these cells. Inhibits the differentiation of peripheral blood precursors towards dendritic cells (By similarity). {ECO:0000250, ECO:0000269|PubMed:15100296}. PTM: Phosphorylation at Tyr-228 and Tyr-257 activates it. May be phosphorylated by LCK (By similarity). {ECO:0000250}.; PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Interacts with SH2 domains of tyrosine-protein phosphatases PTPN6 and PTPN11. The interaction with PTPN6 is constitutive. Interacts with the SH2 domain of CSK. Binds with high affinity to extracellular matrix collagens, the interaction is functionally important (By similarity). {ECO:0000250}. DOMAIN: ITIM (immunoreceptor tyrosine-based inhibitor motif) motif is a cytoplasmic motif present in 2 copies in the intracellular part of LAIR1. When phosphorylated, ITIM motif can bind the SH2 domain of several SH2-containing phosphatases, leading to down-regulation of cell activation. {ECO:0000269|PubMed:15100296}. TISSUE SPECIFICITY: Expressed in lymphoid organs and in cell lines of hemopoietic origin. {ECO:0000269|PubMed:15100296}. +P29752 LALBA_MOUSE Alpha-lactalbumin (Lactose synthase B protein) 143 16,260 Beta strand (6); Calcium binding (1); Chain (1); Disulfide bond (4); Glycosylation (1); Helix (9); Signal peptide (1); Turn (2) FUNCTION: Regulatory subunit of lactose synthase, changes the substrate specificity of galactosyltransferase in the mammary gland making glucose a good acceptor substrate for this enzyme. This enables LS to synthesize lactose, the major carbohydrate component of milk. In other tissues, galactosyltransferase transfers galactose onto the N-acetylglucosamine of the oligosaccharide chains in glycoproteins. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Lactose synthase (LS) is heterodimer of a catalytic component, beta1,4-galactosyltransferase (beta4Gal-T1) and a regulatory component, alpha-lactalbumin (LA). {ECO:0000269|PubMed:11419947, ECO:0000269|PubMed:11485999, ECO:0000269|PubMed:12927542}. TISSUE SPECIFICITY: Mammary gland specific. Secreted in milk. +Q99LX5 MMTA2_MOUSE Multiple myeloma tumor-associated protein 2 homolog 260 29,299 Chain (1); Compositional bias (1); Cross-link (3); Modified residue (5) +D3YWE6 MN1_MOUSE Transcriptional activator MN1 1297 134,072 Chain (1); Compositional bias (4); Modified residue (5) FUNCTION: Transcriptional activator which specifically regulates expression of TBX22 in the posterior region of the developing palate (PubMed:18948418). Required during later stages of palate development for normal growth and medial fusion of the palatal shelves (PubMed:18948418). Promotes maturation and normal function of calvarial osteoblasts, including expression of the osteoclastogenic cytokine TNFSF11/RANKL (PubMed:19386590). Necessary for normal development of the membranous bones of the skull (PubMed:15870292). May play a role in tumor suppression (By similarity). {ECO:0000250|UniProtKB:Q10571, ECO:0000269|PubMed:15870292, ECO:0000269|PubMed:18948418, ECO:0000269|PubMed:19386590}. TISSUE SPECIFICITY: Detected in brain, heart, tibia, and calvarial osteoclasts. {ECO:0000269|PubMed:19386590}. +Q8K3V7 MNAR1_MOUSE Major intrinsically disordered Notch2-binding receptor 1 (Membrane integral NOTCH2-associated receptor 1) (Protein DD1) (Ubiquitination and mTOR signaling protein) 917 102,792 Alternative sequence (1); Chain (1); Erroneous initiation (1); Modified residue (1); Topological domain (2); Transmembrane (1) TRANSMEM 893 913 Helical. {ECO:0000255}. TOPO_DOM 1 892 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 914 917 Extracellular. {ECO:0000305}. FUNCTION: Intrinsically disordered protein which may negatively regulate mTOR signaling pathway by stabilizing the mTOR complex component DEPTOR. Negatively regulates angiogenesis. Negatively regulates cell growth (By similarity). Negatively regulates neurite outgrowth in hippocampal neurons (By similarity). {ECO:0000250|UniProtKB:D3ZJ47, ECO:0000250|UniProtKB:Q9UPX6}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9UPX6}; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:Q9UPX6}. SUBUNIT: Interacts with NOTCH2; this interaction increases MINAR1 stability. Interacts (via N-terminus) with DEPTOR (via PDZ domain); this interaction may stabilize DEPTOR protein by impairing its ubiquitination. {ECO:0000250|UniProtKB:Q9UPX6}. TISSUE SPECIFICITY: Expressed in brain and in islets of Langerhans. +Q61292 LAMB2_MOUSE Laminin subunit beta-2 (Laminin-11 subunit beta) (Laminin-14 subunit beta) (Laminin-15 subunit beta) (Laminin-3 subunit beta) (Laminin-4 subunit beta) (Laminin-7 subunit beta) (Laminin-9 subunit beta) (S-laminin subunit beta) (S-LAM beta) 1799 196,579 Chain (1); Coiled coil (3); Disulfide bond (54); Domain (15); Glycosylation (7); Modified residue (1); Region (3); Sequence conflict (11); Signal peptide (1) FUNCTION: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. {ECO:0000269|PubMed:7885444}.; FUNCTION: Laminin-3 (S-laminin) regulates the formation of motor nerve terminals. {ECO:0000269|PubMed:7885444}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane. SUBUNIT: Laminin is a complex glycoprotein, consisting of three different polypeptide chains (alpha, beta, gamma), which are bound to each other by disulfide bonds into a cross-shaped molecule comprising one long and three short arms with globules at each end. Beta-2 is a subunit of laminin-3 (laminin-121 or S-laminin), laminin-4 (laminin-221 or S-merosin), laminin-7 (laminin-321 or KS-laminin), laminin-9 (laminin-421), laminin-11 (laminin-521), laminin-14 (laminin-423) and laminin-15 (laminin-523). DOMAIN: The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure.; DOMAIN: Domains VI and IV are globular. TISSUE SPECIFICITY: Neuromuscular synapse and kidney glomerulus. +Q8K396 MND1_MOUSE Meiotic nuclear division protein 1 homolog 205 23,849 Chain (1); Coiled coil (1); Initiator methionine (1); Modified residue (1); Sequence conflict (1) FUNCTION: Required for proper homologous chromosome pairing and efficient cross-over and intragenic recombination during meiosis. Stimulates both DMC1- and RAD51-mediated homologous strand assimilation, which is required for the resolution of meiotic double-strand breaks. {ECO:0000269|PubMed:15834424, ECO:0000269|PubMed:16675459, ECO:0000269|PubMed:17426123, ECO:0000269|PubMed:17639081}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Heterodimer with PSMC3IP/HOP2. MND1-PSMC3IP interacts with DMC1 and RAD51 and binds to ssDNA and dsDNA showing no preference for either form of DNA. {ECO:0000269|PubMed:15834424, ECO:0000269|PubMed:16675459}. +D0QMC3 MNDAL_MOUSE Myeloid cell nuclear differentiation antigen-like protein 538 60,526 Chain (1); Compositional bias (1); Domain (2); Natural variant (16) FUNCTION: Suppresses cell growth when expressed ectopically. {ECO:0000269|PubMed:19654412}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19654412}. TISSUE SPECIFICITY: Highest expression observed in spleen and thymus with moderate levels in bone marrow, lung, skin and heart, low levels in muscle, liver and intestine and little or no expression in brain and pancreas. {ECO:0000269|PubMed:19654412}. +Q9R0B6 LAMC3_MOUSE Laminin subunit gamma-3 (Laminin-12 subunit gamma) (Laminin-14 subunit gamma) (Laminin-15 subunit gamma) 1581 172,322 Chain (1); Coiled coil (5); Disulfide bond (40); Domain (14); Glycosylation (10); Region (1); Sequence conflict (10); Signal peptide (1) FUNCTION: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane. SUBUNIT: Laminin is a complex glycoprotein, consisting of three different polypeptide chains (alpha, beta, gamma), which are bound to each other by disulfide bonds into a cross-shaped molecule comprising one long and three short arms with globules at each end. Gamma-3 is a subunit of laminin-12 (laminin-213), laminin-14 (laminin-423) and laminin-15 (laminin-523). DOMAIN: The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure.; DOMAIN: Domain IV is globular. TISSUE SPECIFICITY: Strongly expressed in capillaries and arterioles of kidney as well as in interstitial Leydig cells of testis. +Q9D387 LAMP5_MOUSE Lysosome-associated membrane glycoprotein 5 (Brain and dendritic cell-associated LAMP) (Brain-associated LAMP-like protein) (BAD-LAMP) (Lysosome-associated membrane protein 5) (LAMP-5) 280 31,721 Chain (1); Erroneous initiation (2); Frameshift (1); Glycosylation (4); Mutagenesis (1); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 236 256 Helical. {ECO:0000255}. TOPO_DOM 30 235 Extracellular. {ECO:0000255}.; TOPO_DOM 257 280 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a role in short-term synaptic plasticity in a subset of GABAergic neurons in the brain. {ECO:0000269|PubMed:27272053}. PTM: Glycosylated. {ECO:0000269|PubMed:17215451}. SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:17215451}; Single-pass type I membrane protein {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:17215451}; Single-pass type I membrane protein {ECO:0000269|PubMed:17215451}. Cell projection, dendrite {ECO:0000269|PubMed:17215451}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:27272053}; Single-pass type I membrane protein {ECO:0000305}. Cell projection, growth cone membrane {ECO:0000269|PubMed:17215451}; Single-pass type I membrane protein {ECO:0000305}. Early endosome membrane {ECO:0000269|PubMed:17215451}; Single-pass type I membrane protein {ECO:0000269|PubMed:17215451}. Recycling endosome {ECO:0000269|PubMed:17215451}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q9UJQ1}; Single-pass type I membrane protein {ECO:0000305}. Endosome membrane {ECO:0000250|UniProtKB:Q9UJQ1}; Single-pass type I membrane protein {ECO:0000305}. Note=Recycles from the vesicles of the endocytic recycling compartment (ERC) to the plasma membrane (PubMed:17215451). Colocalizes with UNC93B1 in large endosomal intracellular vesicles (By similarity). Accumulates in the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) before its disappearance upon activation by CpG dinucleotides (By similarity). Associates with cortical membranes (By similarity). Localizes mostly in cytoplasmic vesicles of neuronal cell body (PubMed:17215451). Localizes to synaptic vesicles in a subset of GABAergic neurons (PubMed:27272053). {ECO:0000250|UniProtKB:Q9UJQ1, ECO:0000269|PubMed:27272053}. TISSUE SPECIFICITY: In brain, strongly expressed in the globus pallidus/ventral pallidum complex, the substantia nigra pars reticulata and the entopeduncular nucleus (at protein level) (PubMed:27272053). Expressed in the external plexiform layer of the olfactory bulb (at protein level). May be weakly expressed in neocortex and striatum (at protein level) (PubMed:27272053). Highly expressed in brain; not detected in other tissues tested (PubMed:17215451). Detected in the cingulate cortex, cortical plate and caudate putamen (PubMed:17215451). In neocortex, specifically expressed in neurons of layers II/III and V (PubMed:17215451). {ECO:0000269|PubMed:17215451, ECO:0000269|PubMed:27272053}. +Q61033 LAP2A_MOUSE Lamina-associated polypeptide 2, isoforms alpha/zeta (Thymopoietin isoforms alpha/zeta) (TP alpha/zeta) 693 75,168 Alternative sequence (2); Beta strand (3); Chain (1); Coiled coil (1); Domain (2); Helix (7); Modified residue (24); Motif (1); Region (1); Sequence conflict (7); Turn (1) FUNCTION: May be involved in the structural organization of the nucleus and in the post-mitotic nuclear assembly. Plays an important role, together with LMNA, in the nuclear anchorage of RB1 (By similarity). {ECO:0000250}. PTM: Phosphorylated in a mitose-specific manner. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}. Note=Expressed diffusely throughout the nucleus. {ECO:0000250}. SUBUNIT: Homooligomer. Interacts with LMNA, BANF1 and RB1 and with chromosomes. Associates directly or indirectly with lamins at specific cell-cycle stages (By similarity). Interacts with CMTM6 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P42166}. DOMAIN: The N-terminal part contains two structurally independent, non-interacting domains: LEM-like (also called LAP2-N or LEM-D) and LEM (also called LAP2-C or LEM-B). LEM-like binds DNA while LEM interacts with BANF1 (By similarity). {ECO:0000250}.; DOMAIN: The C-terminal domain forms a four-stranded coiled coil. {ECO:0000269|PubMed:17562312}. +O88559 MEN1_MOUSE Menin 611 67,501 Alternative sequence (1); Chain (1); Erroneous initiation (1); Modified residue (3); Region (1); Sequence conflict (7) FUNCTION: Essential component of a MLL/SET1 histone methyltransferase (HMT) complex, a complex that specifically methylates 'Lys-4' of histone H3 (H3K4). Functions as a transcriptional regulator. Binds to the TERT promoter and represses telomerase expression. Plays a role in TGFB1-mediated inhibition of cell-proliferation, possibly regulating SMAD3 transcriptional activity. Represses JUND-mediated transcriptional activation on AP1 sites, as well as that mediated by NFKB subunit RELA. Positively regulates HOXC8 and HOXC6 gene expression (By similarity). May be involved in normal hematopoiesis through the activation of HOXA9 expression. May be involved in DNA repair. {ECO:0000250, ECO:0000269|PubMed:16415155}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9824159}. Note=May be perinuclear in testis. {ECO:0000269|PubMed:9824159}. SUBUNIT: Component of the MLL-HCF complex, at least composed of KMT2A/MLL1, MEN1, ASH2L, RBBP5, DPY30, WDR5, HCFC1 and HCFC2 (By similarity). Component of the menin-associated histone methyltransferase complex, at least composed of KMT2B/MLL4, MEN1, ASH2L, RBBP5, DPY30 and WDR5 (By similarity). Interacts with POLR2B (By similarity). Interacts with POLR2A phosphorylated at 'Ser-5', but not with the unphosphorylated, nor 'Ser-2' phosphorylated POLR2A forms (By similarity). Interacts with FANCD2 and DBF4 (By similarity). Interacts with SMAD3, but not with SMAD2, nor SMAD4 (By similarity). Directly interacts with NFKB1, NFKB2 and RELA (By similarity). Interacts with JUND. {ECO:0000250, ECO:0000269|PubMed:9989505}. TISSUE SPECIFICITY: Widely expressed, with high levels in hippocampus, cerebral cortex, testis and thymus (at protein level). Also expressed at high levels in pancreatic islets, ovary and bone marrow. In the brain, highest expression in hippocampus pyramidal nerve cells (at protein level). In the testis, may be expressed in spermatogonia (at protein level). Low expression, if any, in skeletal muscle. {ECO:0000269|PubMed:10341092, ECO:0000269|PubMed:10524203, ECO:0000269|PubMed:9824159}. +Q3UV74 ITB2L_MOUSE Integrin beta-2-like protein (Protein pactolus) 738 81,547 Alternative sequence (4); Beta strand (8); Chain (1); Disulfide bond (22); Domain (2); Glycosylation (12); Helix (10); Natural variant (1); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 672 692 Helical. {ECO:0000255}. TOPO_DOM 23 671 Extracellular. {ECO:0000255}.; TOPO_DOM 693 738 Cytoplasmic. {ECO:0000255}. FUNCTION: During inflammatory stimulation, plays a role in retaining Cxcl13-expressing cells at the site of the inflammatory response. {ECO:0000269|PubMed:16836649}. PTM: N-glycosylated. {ECO:0000269|PubMed:11461913}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11461913, ECO:0000269|PubMed:14662885, ECO:0000269|PubMed:9535848}; Single-pass type I membrane protein {ECO:0000269|PubMed:11461913, ECO:0000269|PubMed:14662885, ECO:0000269|PubMed:9535848}. Note=In unactivated neutrophils, the majority of the protein is contained in intracellular granules and is released to the cell surface following inflammatory activation or induction of necrotic or apoptotic cell death. {ECO:0000269|PubMed:11461913, ECO:0000269|PubMed:14662885, ECO:0000269|PubMed:9535848}. SUBUNIT: Monomer and homodimer (Probable). Unlike integrin beta chains, no alpha chain partner has yet been found. {ECO:0000269|PubMed:11461913, ECO:0000269|PubMed:17523188, ECO:0000305}. TISSUE SPECIFICITY: Expressed predominantly in maturing and mature neutrophils. {ECO:0000269|PubMed:11461913}. +Q62469 ITA2_MOUSE Integrin alpha-2 (CD49 antigen-like family member B) (Collagen receptor) (Platelet membrane glycoprotein Ia) (GPIa) (VLA-2 subunit alpha) (CD antigen CD49b) 1178 128,955 Calcium binding (3); Chain (1); Disulfide bond (6); Domain (1); Glycosylation (9); Motif (2); Repeat (7); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1130 1151 Helical. {ECO:0000255}. TOPO_DOM 27 1129 Extracellular. {ECO:0000255}.; TOPO_DOM 1152 1178 Cytoplasmic. {ECO:0000255}. FUNCTION: Integrin alpha-2/beta-1 is a collagen receptor, being responsible for adhesion of platelets and other cells to collagens, modulation of collagen and collagenase gene expression, force generation and organization of newly synthesized extracellular matrix. It is also a receptor for laminins, collagen C-propeptides and E-cadherin. Mice homozygous for a null mutation in the alpha-2 die very early in embryogenesis. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Heterodimer of an alpha and a beta subunit. Alpha-2 associates with beta-1. Interacts with HPS5 and RAB21. {ECO:0000269|PubMed:16754960}. DOMAIN: The integrin I-domain (insert) is a VWFA domain. Integrins with I-domains do not undergo protease cleavage. +Q62470 ITA3_MOUSE Integrin alpha-3 (CD49 antigen-like family member C) (Galactoprotein B3) (GAPB3) (VLA-3 subunit alpha) (CD antigen CD49c) [Cleaved into: Integrin alpha-3 heavy chain; Integrin alpha-3 light chain] 1053 116,745 Alternative sequence (2); Chain (3); Disulfide bond (9); Glycosylation (13); Lipidation (1); Repeat (7); Sequence conflict (6); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 994 1021 Helical. {ECO:0000255}. TOPO_DOM 33 993 Extracellular. {ECO:0000255}.; TOPO_DOM 1022 1053 Cytoplasmic. {ECO:0000255}. FUNCTION: Integrin alpha-3/beta-1 is a receptor for fibronectin, laminin, collagen, epiligrin, thrombospondin and CSPG4. Integrin alpha-3/beta-1 provides a docking site for FAP (seprase) at invadopodia plasma membranes in a collagen-dependent manner and hence may participate in the adhesion, formation of invadopodia and matrix degradation processes, promoting cell invasion. Alpha-3/beta-1 may mediate with LGALS3 the stimulation by CSPG4 of endothelial cells migration. {ECO:0000250|UniProtKB:P26006}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Cell projection, invadopodium membrane {ECO:0000250|UniProtKB:P26006}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, filopodium membrane {ECO:0000250|UniProtKB:P26006}; Single-pass type I membrane protein {ECO:0000255}. Note=Enriched preferentially at invadopodia, cell membrane protrusions that correspond to sites of cell invasion, in a collagen-dependent manner. {ECO:0000250|UniProtKB:P26006}. SUBUNIT: Heterodimer of an alpha and a beta subunit. The alpha subunit is composed of a heavy and a light chain linked by a disulfide bond. Alpha-3 associates with beta-1. Interacts with HPS5. Interacts with FAP (seprase); the interaction occurs at the cell surface of invadopodia membrane in a collagen-dependent manner. {ECO:0000250|UniProtKB:P26006}. TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in heart and brain. Only isoform 1 is detected in lung. {ECO:0000269|PubMed:1946438}. +Q69ZQ2 ISY1_MOUSE Pre-mRNA-splicing factor ISY1 homolog 285 32,989 Chain (1); Compositional bias (1); Erroneous initiation (1); Helix (2); Modified residue (2); Sequence conflict (1); Turn (2) FUNCTION: May play a role in pre-mRNA splicing as component of the spliceosome. {ECO:0000250|UniProtKB:Q9ULR0}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9ULR0}. SUBUNIT: Identified in the spliceosome C complex. Component of the XAB2 complex, a multimeric protein complex composed of XAB2, PRPF19, AQR, ZNF830, ISY1, and PPIE. Identified in a pentameric intron-binding (IB) complex composed of AQR, XAB2, ISY1, ZNF830 and PPIE that is incorporated into the spliceosome as a preassembled complex. The IB complex does not contain PRPF19. {ECO:0000250|UniProtKB:Q9ULR0}. +O54890 ITB3_MOUSE Integrin beta-3 (Platelet membrane glycoprotein IIIa) (GPIIIa) (CD antigen CD61) 787 86,738 Beta strand (1); Chain (1); Disulfide bond (28); Domain (1); Glycosylation (5); Modified residue (4); Region (4); Repeat (4); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 718 740 Helical. {ECO:0000255}. TOPO_DOM 26 717 Extracellular. {ECO:0000255}.; TOPO_DOM 741 787 Cytoplasmic. {ECO:0000255}. FUNCTION: Integrin alpha-V/beta-3 (ITGAV:ITGB3) is a receptor for cytotactin, fibronectin, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin, vitronectin and von Willebrand factor. Integrin alpha-IIB/beta-3 (ITGA2B:ITGB3) is a receptor for fibronectin, fibrinogen, plasminogen, prothrombin, thrombospondin and vitronectin. Integrins alpha-IIB/beta-3 and alpha-V/beta-3 recognize the sequence R-G-D in a wide array of ligands. Integrin alpha-IIB/beta-3 recognizes the sequence H-H-L-G-G-G-A-K-Q-A-G-D-V in fibrinogen gamma chain. Following activation integrin alpha-IIB/beta-3 brings about platelet/platelet interaction through binding of soluble fibrinogen. This step leads to rapid platelet aggregation which physically plugs ruptured endothelial surfaces. Fibrinogen binding enhances SELP expression in activated platelets (PubMed:19332769). ITGAV:ITGB3 binds to fractalkine (CX3CL1) and acts as its coreceptor in CX3CR1-dependent fractalkine signaling. ITGAV:ITGB3 binds to NRG1 (via EGF domain) and this binding is essential for NRG1-ERBB signaling. ITGAV:ITGB3 binds to FGF1 and this binding is essential for FGF1 signaling. ITGAV:ITGB3 binds to FGF2 and this binding is essential for FGF2 signaling (By similarity). ITGAV:ITGB3 binds to IGF1 and this binding is essential for IGF1 signaling (By similarity). ITGAV:ITGB3 binds to IGF2 and this binding is essential for IGF2 signaling (By similarity). ITGAV:ITGB3 binds to IL1B and this binding is essential for IL1B signaling (By similarity). ITGAV:ITGB3 binds to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational changes and enhanced ligand binding to site 1 (By similarity). ITGAV:ITGB3 acts as a receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell adhesion to FBN1 (By similarity). {ECO:0000250|UniProtKB:P05106, ECO:0000269|PubMed:19332769}. PTM: Phosphorylated on tyrosine residues in response to thrombin-induced platelet aggregation. Probably involved in outside-in signaling. {ECO:0000250|UniProtKB:P05106}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P05106}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P05106}. Cell projection, lamellipodium membrane {ECO:0000250|UniProtKB:P05106}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:P05106}. SUBUNIT: Heterodimer of an alpha and a beta subunit (By similarity). Beta-3 (ITGB3) associates with either alpha-IIB (ITGA2B) or alpha-V (ITGAV). Interacts with FLNB and COMP (By similarity). Interacts with PDIA6 following platelet stimulation (By similarity). Interacts with SYK; upon activation by ITGB3 promotes platelet adhesion (By similarity). Interacts with MYO10 (By similarity). Interacts with DAB2 (PubMed:12606711). Interacts with FERMT2 (PubMed:18483218). Integrin ITGAV:ITGB3 interacts with FBLN5 (via N-terminus) (PubMed:11805835). Interacts with EMP2; regulates the levels of the heterodimer ITGA5:ITGB3 integrin expression on the plasma membrane (By similarity). ITGAV:ITGB3 interacts with CCN3 (By similarity). ITGAV:ITGB3 interacts with AGRA2 (By similarity). ITGAV:ITGB3 is found in a ternary complex with CX3CR1 and CX3CL1. ITGAV:ITGB3 is found in a ternary complex with NRG1 and ERBB3. ITGAV:ITGB3 is found in a ternary complex with FGF1 and FGFR1. ITGAV:ITGB3 interacts with FGF2; it is likely that FGF2 can simultaneously bind ITGAV:ITGB3 and FGF receptors (By similarity). ITGAV:ITGB3 binds to IL1B (By similarity). ITGAV:ITGB3 is found in a ternary complex with IGF1 and IGF1R (By similarity). ITGAV:ITGB3 interacts with IGF2 (By similarity). ITGAV:ITGB3 interacts with FBN1 (By similarity). ITGAV:ITGB3 interacts with CD9, CD81 and CD151 (via second extracellular domain) (By similarity). Interacts (via the allosteric site (site 2)) with CXCL12 in a CXCR4-independent manner (By similarity). Interacts with MXRA8/DICAM; the interaction inhibits ITGAV:ITGB3 heterodimer formation (PubMed:22492581). {ECO:0000250|UniProtKB:P05106, ECO:0000269|PubMed:11805835, ECO:0000269|PubMed:12606711, ECO:0000269|PubMed:18483218, ECO:0000269|PubMed:22492581}. +Q00651 ITA4_MOUSE Integrin alpha-4 (CD49 antigen-like family member D) (Integrin alpha-IV) (Lymphocyte Peyer patch adhesion molecules subunit alpha) (LPAM subunit alpha) (VLA-4 subunit alpha) (CD antigen CD49d) 1039 115,696 Calcium binding (3); Chain (1); Disulfide bond (9); Glycosylation (12); Modified residue (1); Motif (2); Repeat (7); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 984 1007 Helical. {ECO:0000255}. TOPO_DOM 41 983 Extracellular. {ECO:0000255}.; TOPO_DOM 1008 1039 Cytoplasmic. {ECO:0000255}. FUNCTION: Integrins alpha-4/beta-1 (VLA-4 or LPAM-2) and alpha-4/beta-7 (LPAM-1) are receptors for fibronectin. They recognize one or more domains within the alternatively spliced CS-1 and CS-5 regions of fibronectin. They are also receptors for VCAM1. Integrin alpha-4/beta-1 recognizes the sequence Q-I-D-S in VCAM1. Integrin alpha-4/beta-7 is also a receptor for MADCAM1. It recognizes the sequence L-D-T in MADCAM1. On activated endothelial cells integrin VLA-4 triggers homotypic aggregation for most VLA-4-positive leukocyte cell lines. It may also participate in cytolytic T-cell interactions with target cells. ITGA4:ITGB1 binds to fractalkine (CX3CL1) and may act as its coreceptor in CX3CR1-dependent fractalkine signaling. ITGA4:ITGB1 binds to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational changes and enhanced ligand binding to site 1. {ECO:0000250|UniProtKB:P13612}. PTM: Phosphorylation on Ser-1028 inhibits PXN binding. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Heterodimer of an alpha and a beta subunit. The alpha subunit can sometimes be cleaved into two non-covalently associated fragments. Alpha-4 associates with either beta-1 or beta-7. Alpha-4 interacts with PXN, LPXN, and TGFB1I1/HIC5. Interacts with CSPG4 through CSPG4 chondroitin sulfate glycosaminoglycan. Interacts with JAML; integrin alpha-4/beta-1 may regulate leukocyte to endothelial cells adhesion by controlling JAML homodimerization. ITGA4:ITGB1 is found in a ternary complex with CX3CR1 and CX3CL1 (By similarity). {ECO:0000250|UniProtKB:P13612}. DOMAIN: The SG1 motif is involved in binding to chondroitin sulfate glycosaminoglycan and cell adhesion. {ECO:0000250}. TISSUE SPECIFICITY: Peyer patch homing cells. +Q0VBD0 ITB8_MOUSE Integrin beta-8 767 84,519 Chain (1); Disulfide bond (20); Domain (2); Glycosylation (6); Region (1); Repeat (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 682 702 Helical. {ECO:0000255}. TOPO_DOM 22 681 Extracellular. {ECO:0000305}.; TOPO_DOM 703 767 Cytoplasmic. {ECO:0000305}. FUNCTION: Integrin alpha-V:beta-8 (ITGAV:ITGB8) is a receptor for fibronectin (By similarity). It recognizes the sequence R-G-D in its ligands (By similarity). Integrin alpha-V:beta-6 (ITGAV:ITGB6) mediates R-G-D-dependent release of transforming growth factor beta-1 (TGF-beta-1) from regulatory Latency-associated peptide (LAP), thereby playing a key role in TGF-beta-1 activation on the surface of activated regulatory T-cells (Tregs) (PubMed:25127859). Required during vasculogenesis (PubMed:12050137, PubMed:16251442). {ECO:0000250|UniProtKB:P26012, ECO:0000269|PubMed:12050137, ECO:0000269|PubMed:16251442, ECO:0000269|PubMed:25127859}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P26012}; Single-pass type I membrane protein {ECO:0000255}. SUBUNIT: Heterodimer of an alpha and a beta subunit (PubMed:25127859). Beta-8 (ITGB8) associates with alpha-V (ITGAV) to form ITGAV:ITGB8 (PubMed:25127859). ITGAV:ITGB8 interacts with TGFB1 (PubMed:25127859). {ECO:0000269|PubMed:25127859}. +Q61739 ITA6_MOUSE Integrin alpha-6 (CD49 antigen-like family member F) (VLA-6) (CD antigen CD49f) [Cleaved into: Integrin alpha-6 heavy chain; Integrin alpha-6 light chain] 1091 122,159 Alternative sequence (1); Calcium binding (3); Chain (3); Disulfide bond (9); Glycosylation (8); Lipidation (1); Modified residue (1); Motif (1); Repeat (7); Sequence conflict (6); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1012 1037 Helical. {ECO:0000255}. TOPO_DOM 24 1011 Extracellular. {ECO:0000255}.; TOPO_DOM 1038 1091 Cytoplasmic. {ECO:0000255}. FUNCTION: Integrin alpha-6/beta-1 (ITGA6:ITGB1) is a receptor for laminin on platelets (PubMed:8081870). Integrin alpha-6/beta-1 (ITGA6:ITGB1) is present in oocytes and is involved in sperm-egg fusion (PubMed:10634791). Integrin alpha-6/beta-4 (ITGA6:ITGB4) is a receptor for laminin in epithelial cells and it plays a critical structural role in the hemidesmosome (PubMed:8673141). ITGA6:ITGB4 binds to NRG1 (via EGF domain) and this binding is essential for NRG1-ERBB signaling (By similarity). ITGA6:ITGB4 binds to IGF1 and this binding is essential for IGF1 signaling (By similarity). ITGA6:ITGB4 binds to IGF2 and this binding is essential for IGF2 signaling (By similarity). {ECO:0000250|UniProtKB:P23229, ECO:0000269|PubMed:10634791, ECO:0000269|PubMed:8081870, ECO:0000269|PubMed:8673141}. PTM: Isoforms containing segment A, but not segment B, are the major targets for PMA-induced phosphorylation. Phosphorylation occurs on 'Ser-1064' of isoform alpha-6X1A. Phosphorylation is not required for the induction of integrin alpha-6A/beta-1 high affinity but may reduce the affinity for ligand (By similarity). {ECO:0000250|UniProtKB:P23229}.; PTM: Palmitoylation by DHHC3 enhances stability and cell surface expression. {ECO:0000250|UniProtKB:P23229}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P23229}; Single-pass type I membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:P23229}; Lipid-anchor {ECO:0000250|UniProtKB:P23229}. SUBUNIT: Heterodimer of an alpha and a beta subunit (PubMed:8081870). The alpha subunit is composed of a heavy and a light chain linked by a disulfide bond (PubMed:8081870). Alpha-6 associates with either beta-1(ITGB1) or beta-4 (ITGB4) to form ITGA6:ITGB1 and ITGA6:ITGB4, respectively (PubMed:8081870, PubMed:10634791). ITGA6:ITGB1 is found in a complex with CD9; interaction takes place in oocytes and is involved in sperm-egg fusion (PubMed:10634791). ITGA6:ITGB4 is found in a ternary complex with NRG1 and ERBB3 (By similarity). ITGA6:ITGB4 is found in a ternary complex with IGF1 and IGF1R (By similarity). ITGA6:ITGB4 interacts with IGF2 (By similarity). Interacts with ADAM9 (PubMed:10825303). Interacts with RAB21 (By similarity). {ECO:0000250|UniProtKB:P23229, ECO:0000269|PubMed:10634791, ECO:0000269|PubMed:10825303, ECO:0000269|PubMed:8081870}. +Q61738 ITA7_MOUSE Integrin alpha-7 [Cleaved into: Integrin alpha-7 heavy chain; Integrin alpha-7 light chain] 1179 129,329 Alternative sequence (3); Calcium binding (3); Chain (3); Compositional bias (1); Disulfide bond (9); Glycosylation (5); Motif (1); Region (1); Repeat (10); Sequence conflict (25); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1077 1102 Helical. {ECO:0000255}. TOPO_DOM 34 1076 Extracellular. {ECO:0000255}.; TOPO_DOM 1103 1179 Cytoplasmic. {ECO:0000255}. FUNCTION: Integrin alpha-7/beta-1 is the primary laminin receptor on skeletal myoblasts and adult myofibers. During myogenic differentiation, it may induce changes in the shape and mobility of myoblasts, and facilitate their localization at laminin-rich sites of secondary fiber formation. Involved in the maintenance of the myofibers cytoarchitecture as well as for their anchorage, viability and functional integrity. Mice carrying a ITGA7 null allele are viable and fertile, but show progressive muscular dystrophy starting soon after birth, but with a distinct variability in different muscle types. Required to promote contractile phenotype acquisition in differentiated airway smooth muscle (ASM) cells. Acts as Schwann cell receptor for laminin-2. Acts as a receptor of COMP and mediates its effect on vascular smooth muscle cells (VSMCs) maturation (By similarity). {ECO:0000250, ECO:0000269|PubMed:9354797}. PTM: ADP-ribosylated on at least two sites of the extracellular domain in skeletal myotubes (in vitro).; PTM: No proteolytic cleavage to produce the 70 kDa form is seen due to the presence of a Gly instead of an arginine residue at position 647. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Heterodimer of an alpha and a beta subunit. The alpha subunit is composed of a heavy and a light chain linked by a disulfide bond. Alpha-7 associates with beta-1. Interacts with COMP. Interacts (via C-terminus intracellular tail region) with CIB1; the interaction is stabilized/increased in a calcium- and magnesium-dependent manner (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Isoforms containing segment X2 are found in adult heart, lung and skeletal muscle. Isoforms containing segment X1 are expressed in adult heart, lung and in proliferating skeletal myoblasts but not in adult skeletal muscle. Isoforms containing segment a are exclusively found in skeletal muscle. Isoforms containing segment B are widely expressed. In muscle fibers isoforms containing segment A and B are expressed at myotendinous and neuromuscular junctions; isoforms containing segment C are expressed at neuromuscular junctions and at extrasynaptic sites. {ECO:0000269|PubMed:8626012}. +B2RRL2 JERKL_MOUSE Jerky protein homolog-like 523 59,710 Chain (1); DNA binding (2); Domain (3); Erroneous initiation (1); Frameshift (1); Sequence conflict (3) SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00320, ECO:0000255|PROSITE-ProRule:PRU00583}. +Q8BVL9 JKIP1_MOUSE Janus kinase and microtubule-interacting protein 1 (GABA-B receptor-binding protein) (Multiple alpha-helices and RNA-linker protein 1) (Marlin-1) 626 73,139 Chain (1); Coiled coil (3); Modified residue (2); Region (2); Sequence conflict (1) FUNCTION: Associates with microtubules and may play a role in the microtubule-dependent transport of the GABA-B receptor. May play a role in JAK1 signaling and regulate microtubule cytoskeleton rearrangements. {ECO:0000269|PubMed:17532644}. PTM: Phosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Colocalizes with the microtubule network. Localizes to the cell body and neurites of hippocampal neurons where it accumulates in granules. Localizes to the tail and to a lower extent to the head of sperm cells (By similarity). {ECO:0000250}. SUBUNIT: Homodimer (By similarity). Interacts with JAK1 and TYK2 (By similarity). Forms a complex with GABBR1 and KIF5B/kinesin-1. {ECO:0000250, ECO:0000269|PubMed:14718537, ECO:0000269|PubMed:17532644}. +Q62315 JARD2_MOUSE Protein Jumonji (Jumonji/ARID domain-containing protein 2) 1234 137,445 Alternative sequence (1); Chain (1); Domain (3); Erroneous gene model prediction (1); Frameshift (1); Helix (7); Modified residue (3); Motif (2); Mutagenesis (1); Sequence conflict (2) FUNCTION: Regulator of histone methyltransferase complexes that plays an essential role in embryonic development, including heart and liver development, neural tube fusion process and hematopoiesis. Acts by modulating histone methyltransferase activity and promoting the recruitment of histone methyltransferase complexes to their target genes. Binds DNA and mediates the recruitment of the PRC2 complex to target genes in embryonic stem cells. Does not have histone demethylase activity but regulates activity of various histone methyltransferase complexes. In embryonic stem cells, it associates with the PRC2 complex and inhibits trimethylation of 'Lys-27' of histone H3 (H3K27me3) by the PRC2 complex, thereby playing a key role in differentiation of embryonic stem cells and normal development. In cardiac cells, it is required to repress expression of cyclin-D1 (CCND1) by activating methylation of 'Lys-9' of histone H3 (H3K9me) by the GLP1/EHMT1 and G9a/EHMT2 histone methyltransferases. Also acts as a transcriptional repressor of ANF via its interaction with GATA4 and NKX2-5. Participates in the negative regulation of cell proliferation signaling. {ECO:0000269|PubMed:10807864, ECO:0000269|PubMed:10913339, ECO:0000269|PubMed:12852854, ECO:0000269|PubMed:12890668, ECO:0000269|PubMed:15542826, ECO:0000269|PubMed:15870077, ECO:0000269|PubMed:19010785, ECO:0000269|PubMed:20064375, ECO:0000269|PubMed:20064376, ECO:0000269|PubMed:20075857}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355, ECO:0000255|PROSITE-ProRule:PRU00537, ECO:0000269|PubMed:10807864, ECO:0000269|PubMed:10913339, ECO:0000269|PubMed:20064375, ECO:0000269|PubMed:20064376}. Note=Colocalizes with the PRC2 complex on chromatin. SUBUNIT: Associates with the PRC2 complex, which includes EED, EZH1, EZH2, SUZ12, RBBP4 and AEBP2; JARID2 is probably not a core component of the PRC2 complex and associates to PRC2 via its interaction with SUZ12. Associates with a histone methyltransferase complex containing GLP1/EHMT1 and G9a/EHMT2. Interacts with SUZ12; the interaction is direct. Interacts with GATA4 (via the N-terminal region). Interacts with NKX2-5 (via the C-terminal region). Interacts with RB1. Interacts with ZNF496. Interacts with ESRRB (PubMed:26523946). {ECO:0000269|PubMed:15542826, ECO:0000269|PubMed:15870077, ECO:0000269|PubMed:17521633, ECO:0000269|PubMed:20064375, ECO:0000269|PubMed:26523946}. DOMAIN: The ARID domain is required to target the PRC2 complex to its target genes.; DOMAIN: The GSGFP motif is required for the interaction with SUZ12. TISSUE SPECIFICITY: Widely expressed in embryos. In adults, expressed at high levels in heart, skeletal muscle, brain and thymus. {ECO:0000269|PubMed:10807864}. +Q60722 ITF2_MOUSE Transcription factor 4 (TCF-4) (Class A helix-loop-helix transcription factor ME2) (Immunoglobulin transcription factor 2) (ITF-2) (MITF-2) (SL3-3 enhancer factor 2) (SEF-2) 670 71,625 Alternative sequence (3); Chain (1); Compositional bias (1); Domain (1); Modified residue (5); Region (3); Sequence conflict (3) FUNCTION: Transcription factor that binds to the immunoglobulin enhancer Mu-E5/KE5-motif. Involved in the initiation of neuronal differentiation. Activates transcription by binding to the E box (5'-CANNTG-3'). Isoform 2 inhibits MYOD1 activation of the cardiac alpha-actin promoter. Binds to the E-box present in the somatostatin receptor 2 initiator element (SSTR2-INR) to activate transcription. May have a regulatory function in developmental processes as well as during neuronal plasticity. {ECO:0000269|PubMed:18214987}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Efficient DNA binding requires dimerization with another bHLH protein. Isoform 2 seems to form inactive heterodimers with MYOD1. Interacts with HIVEP2. Interacts with NEUROD2. Interacts with AGBL1 (By similarity). Interacts with BHLHA9. {ECO:0000250|UniProtKB:P15884, ECO:0000269|PubMed:10207097, ECO:0000269|PubMed:18214987}. TISSUE SPECIFICITY: Expressed in the cerebral cortex, Purkinje and granule cell layers of the cerebellum, olfactory neuroepithelium, pyramidal cells of hippocampal layers CA1-CA4, and in the granular cells of the dentate gyrus. +Q9D8B7 JAM3_MOUSE Junctional adhesion molecule C (JAM-C) (JAM-2) (Junctional adhesion molecule 3) (JAM-3) [Cleaved into: Soluble form of JAM-C (sJAM-C)] 310 34,838 Beta strand (1); Chain (2); Disulfide bond (2); Domain (2); Glycosylation (2); Lipidation (2); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 242 262 Helical. {ECO:0000255}. TOPO_DOM 30 241 Extracellular. {ECO:0000255}.; TOPO_DOM 263 310 Cytoplasmic. {ECO:0000255}. FUNCTION: Mediates cell-cell adhesion. Functions as counter-receptor for JAM2 (PubMed:15372036). Functions as a counter-receptor for ITGAM, mediating leukocyte-platelet interactions and is involved in the regulation of transepithelial migration of polymorphonuclear neutrophils (PMN) (By similarity). Plays a role in angiogenesis (PubMed:15994945). May play a role in the regulation of cell migration (By similarity). Required for normal polarization and acrosome formation in developing spermatids, and for normal male fertility (PubMed:15372036). {ECO:0000250|UniProtKB:Q9BX67, ECO:0000269|PubMed:15372036, ECO:0000269|PubMed:15994945}.; FUNCTION: Soluble form of JAM-C: Promotes chemotaxis of vascular endothelial cells and stimulates angiogenesis. {ECO:0000269|PubMed:20592283}. PTM: Proteolytically cleaved from endothelial cells surface into a soluble form by ADAM10 and ADAM17; the release of soluble JAM3 is increased by proinflammatory factors. {ECO:0000250|UniProtKB:Q9BX67}.; PTM: N-glycosylated. {ECO:0000269|PubMed:11053409}.; PTM: S-palmitoylated by ZDHHC7. S-palmitoylation promotes expression at tight junctions. {ECO:0000250|UniProtKB:Q9BX67}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11053409, ECO:0000269|PubMed:11739175}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9BX67}. Cell junction {ECO:0000269|PubMed:11053409}. Cell junction, desmosome {ECO:0000250|UniProtKB:Q9BX67}. Cell junction, tight junction {ECO:0000269|PubMed:11053409, ECO:0000269|PubMed:11739175}. Note=Detected in the acrosome region in developing spermatids (PubMed:28617811). In epithelial cells, it is expressed at desmosomes but not at tight junctions. Localizes at the cell surface of endothelial cells; treatment of endothelial cells with vascular endothelial growth factor stimulates recruitment of JAM3 to cell-cell contacts (By similarity). {ECO:0000250|UniProtKB:Q9BX67, ECO:0000269|PubMed:28617811}.; SUBCELLULAR LOCATION: Soluble form of JAM-C: Secreted {ECO:0000250|UniProtKB:Q9BX67}. SUBUNIT: Interacts with GORASP2 (PubMed:28617811). Interacts with JAM2 (PubMed:15372036). Interacts with ITGAM (By similarity). {ECO:0000250|UniProtKB:Q9BX67, ECO:0000269|PubMed:15372036, ECO:0000269|PubMed:28617811}. TISSUE SPECIFICITY: Colocalizes with Jam2 near the lumen of seminiferous tubulues. Detected at junctional plaques that correspond to cell-cell contacts between spermatids and Sertoli cells (PubMed:15372036, PubMed:28617811). Detected on endothelial cells, in brain vessels and kidney glomeruli (at protein level) (PubMed:11053409, PubMed:11739175). Detected in heart, lung, liver, kidney, testis, thymus, lymph node and Peyer patch (PubMed:11053409, PubMed:11739175). Endothelial cells (PubMed:11739175). {ECO:0000269|PubMed:11053409, ECO:0000269|PubMed:11739175, ECO:0000269|PubMed:15372036, ECO:0000269|PubMed:28617811}. +Q62120 JAK2_MOUSE Tyrosine-protein kinase JAK2 (EC 2.7.10.2) (Janus kinase 2) (JAK-2) 1129 130,235 Active site (1); Binding site (1); Chain (1); Domain (4); Modified residue (11); Mutagenesis (8); Nucleotide binding (1); Region (1); Sequence conflict (7) FUNCTION: Non-receptor tyrosine kinase involved in various processes such as cell growth, development, differentiation or histone modifications. Mediates essential signaling events in both innate and adaptive immunity. In the cytoplasm, plays a pivotal role in signal transduction via its association with type I receptors such as growth hormone (GHR), prolactin (PRLR), leptin (LEPR), erythropoietin (EPOR), thrombopoietin (THPO); or type II receptors including IFN-alpha, IFN-beta, IFN-gamma and multiple interleukins. Following ligand-binding to cell surface receptors, phosphorylates specific tyrosine residues on the cytoplasmic tails of the receptor, creating docking sites for STATs proteins. Subsequently, phosphorylates the STATs proteins once they are recruited to the receptor. Phosphorylated STATs then form homodimer or heterodimers and translocate to the nucleus to activate gene transcription. For example, cell stimulation with erythropoietin (EPO) during erythropoiesis leads to JAK2 autophosphorylation, activation, and its association with erythropoietin receptor (EPOR) that becomes phosphorylated in its cytoplasmic domain. Then, STAT5 (STAT5A or STAT5B) is recruited, phosphorylated and activated by JAK2. Once activated, dimerized STAT5 translocates into the nucleus and promotes the transcription of several essential genes involved in the modulation of erythropoiesis. Part of a signaling cascade that is activated by increased cellular retinol and that leads to the activation of STAT5 (STAT5A or STAT5B). In addition, JAK2 mediates angiotensin-2-induced ARHGEF1 phosphorylation. Plays a role in cell cycle by phosphorylating CDKN1B. Cooperates with TEC through reciprocal phosphorylation to mediate cytokine-driven activation of FOS transcription. In the nucleus, plays a key role in chromatin by specifically mediating phosphorylation of 'Tyr-41' of histone H3 (H3Y41ph), a specific tag that promotes exclusion of CBX5 (HP1 alpha) from chromatin. {ECO:0000269|PubMed:11779507, ECO:0000269|PubMed:20098430, ECO:0000269|PubMed:21368206, ECO:0000269|PubMed:21423214, ECO:0000269|PubMed:8343951, ECO:0000269|PubMed:8702638, ECO:0000269|PubMed:9473212, ECO:0000269|PubMed:9590173, ECO:0000269|PubMed:9590174}. PTM: Autophosphorylated, leading to regulate its activity. Leptin promotes phosphorylation on tyrosine residues, including phosphorylation on Tyr-813 (PubMed:16824542, PubMed:17565041). Autophosphorylation on Tyr-119 in response to EPO down-regulates its kinase activity (PubMed:17024180). Autophosphorylation on Tyr-868, Tyr-966 and Tyr-972 in response to growth hormone (GH) are required for maximal kinase activity (PubMed:20304997). Also phosphorylated by TEC (PubMed:9473212). Phosphorylated on tyrosine residues in response to interferon gamma signaling (By similarity). Phosphorylated on tyrosine residues in response to a signaling cascade that is activated by increased cellular retinol (PubMed:21368206). {ECO:0000250|UniProtKB:O60674, ECO:0000269|PubMed:16824542, ECO:0000269|PubMed:17024180, ECO:0000269|PubMed:17565041, ECO:0000269|PubMed:20304997, ECO:0000269|PubMed:21368206, ECO:0000269|PubMed:21726629, ECO:0000269|PubMed:8343951, ECO:0000269|PubMed:9473212}. SUBCELLULAR LOCATION: Endomembrane system; Peripheral membrane protein. Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Interacts with IL23R, SKB1 and STAM2 (By similarity). Interacts with EPOR (PubMed:8343951, PubMed:11779507). Interacts with LYN (PubMed:9573010). Interacts with SIRPA (PubMed:10842184). Interacts with SH2B1 (PubMed:17565041, PubMed:16824542). Interacts with TEC (PubMed:9473212). Interacts with IFNGR2 (via intracellular domain) (By similarity). Interacts with LEPR (Isoform B) (PubMed:11923481). Interacts with HSP90AB1; promotes functional activation in a heat shock-dependent manner. Interacts with STRA6 (By similarity). {ECO:0000250|UniProtKB:O60674, ECO:0000269|PubMed:10842184, ECO:0000269|PubMed:11779507, ECO:0000269|PubMed:11923481, ECO:0000269|PubMed:16824542, ECO:0000269|PubMed:17565041, ECO:0000269|PubMed:7775438, ECO:0000269|PubMed:8343951, ECO:0000269|PubMed:9473212, ECO:0000269|PubMed:9573010}. DOMAIN: Possesses 2 protein kinase domains. The second one probably contains the catalytic domain, while the presence of slight differences suggest a different role for protein kinase 1. TISSUE SPECIFICITY: Ubiquitously expressed throughout most tissues. +Q60677 ITAE_MOUSE Integrin alpha-E (Integrin alpha M290) (CD antigen CD103) [Cleaved into: Integrin alpha-E light chain; Integrin alpha-E heavy chain] 1167 128,906 Calcium binding (3); Chain (3); Compositional bias (1); Disulfide bond (7); Domain (1); Glycosylation (17); Motif (1); Region (1); Repeat (7); Sequence conflict (8); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1115 1137 Helical. {ECO:0000255}. TOPO_DOM 20 1114 Extracellular. {ECO:0000255}.; TOPO_DOM 1138 1167 Cytoplasmic. {ECO:0000255}. FUNCTION: Integrin alpha-E/beta-7 is a receptor for E-cadherin. It mediates adhesion of intra-epithelial T-lymphocytes to epithelial cell monolayers. Mice expressing a null mutation of the alpha-E subunit gene exhibit a marked reduction in the numbers of intraepithelial lymphocytes in the gut and in the development of gut-associated lymphoid aggregates, supporting a specific role for this integrin in mediating retention of lymphocytes in the intestinal wall. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Heterodimer of an alpha and a beta subunit. The alpha subunit is composed of a heavy and a light chains linked by a disulfide bond. Alpha-E associates with beta-7. DOMAIN: The integrin I-domain (insert) is a VWFA domain. Integrins with I-domains do not undergo protease cleavage. +Q3LS21 KCNK9_MOUSE Potassium channel subfamily K member 9 (Acid-sensitive potassium channel protein TASK-3) (TWIK-related acid-sensitive K(+) channel 3) 402 44,911 Chain (1); Glycosylation (1); Intramembrane (2); Topological domain (7); Transmembrane (4) INTRAMEM 89 101 Pore-forming; Name=Pore-forming 1. {ECO:0000255}.; INTRAMEM 195 207 Pore-forming; Name=Pore-forming 2. {ECO:0000255}. TRANSMEM 9 29 Helical. {ECO:0000255}.; TRANSMEM 108 128 Helical. {ECO:0000255}.; TRANSMEM 159 179 Helical. {ECO:0000255}.; TRANSMEM 219 239 Helical. {ECO:0000255}. TOPO_DOM 1 8 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 30 88 Extracellular. {ECO:0000255}.; TOPO_DOM 102 107 Extracellular. {ECO:0000255}.; TOPO_DOM 129 158 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 180 194 Extracellular. {ECO:0000255}.; TOPO_DOM 208 218 Extracellular. {ECO:0000255}.; TOPO_DOM 240 402 Cytoplasmic. {ECO:0000255}. FUNCTION: pH-dependent, voltage-insensitive, background potassium channel protein. {ECO:0000250|UniProtKB:Q9NPC2}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9NPC2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9NPC2}. SUBUNIT: Homodimer. Heterodimer with KCNK1. {ECO:0000250|UniProtKB:Q9NPC2}. +Q61923 KCNA6_MOUSE Potassium voltage-gated channel subfamily A member 6 (MK1.6) (Voltage-gated potassium channel subunit Kv1.6) 529 58,674 Chain (1); Intramembrane (2); Lipidation (1); Modified residue (2); Motif (2); Region (1); Topological domain (8); Transmembrane (6) INTRAMEM 410 421 Helical; Name=Pore helix. {ECO:0000250|UniProtKB:P63142}.; INTRAMEM 422 429 {ECO:0000250|UniProtKB:P63142}. TRANSMEM 172 193 Helical; Name=Segment S1. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 263 284 Helical; Name=Segment S2. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 296 316 Helical; Name=Segment S3. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 338 358 Helical; Voltage-sensor; Name=Segment S4. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 374 395 Helical; Name=Segment S5. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 437 465 Helical; Name=Segment S6. {ECO:0000250|UniProtKB:P63142}. TOPO_DOM 1 171 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 194 262 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 285 295 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 317 337 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 359 373 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 396 409 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 430 436 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 466 529 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}. FUNCTION: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes. Forms tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient (By similarity). The channel alternates between opened and closed conformations in response to the voltage difference across the membrane (By similarity). Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNA1, KCNA2, KCNA4, KCNA6, and possibly other family members as well; channel properties depend on the type of alpha subunits that are part of the channel (By similarity). Channel properties are modulated by cytoplasmic beta subunits that regulate the subcellular location of the alpha subunits and promote rapid inactivation (By similarity). Homotetrameric channels display rapid activation and slow inactivation (By similarity). {ECO:0000250|UniProtKB:P17658, ECO:0000250|UniProtKB:P17659}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P17658}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Homotetramer and heterotetramer of potassium channel proteins (Probable). Interacts with KCNAB1 and KCNAB2 (By similarity). {ECO:0000250|UniProtKB:P17659, ECO:0000305}. DOMAIN: The N-terminus may be important in determining the rate of inactivation of the channel while the tail may play a role in modulation of channel activity and/or targeting of the channel to specific subcellular compartments.; DOMAIN: The transmembrane segment S4 functions as voltage-sensor and is characterized by a series of positively charged amino acids at every third position. Channel opening and closing is effected by a conformation change that affects the position and orientation of the voltage-sensor paddle formed by S3 and S4 within the membrane. A transmembrane electric field that is positive inside would push the positively charged S4 segment outwards, thereby opening the pore, while a field that is negative inside would pull the S4 segment inwards and close the pore. Changes in the position and orientation of S4 are then transmitted to the activation gate formed by the inner helix bundle via the S4-S5 linker region. {ECO:0000250|UniProtKB:P63142}. +P35561 KCNJ2_MOUSE Inward rectifier potassium channel 2 (Inward rectifier K(+) channel Kir2.1) (IRK-1) (Potassium channel, inwardly rectifying subfamily J member 2) 428 48,389 Beta strand (14); Chain (1); Helix (4); Initiator methionine (1); Intramembrane (2); Lipidation (1); Modified residue (1); Motif (2); Mutagenesis (1); Site (1); Topological domain (4); Transmembrane (2); Turn (4) INTRAMEM 129 140 Helical; Pore-forming; Name=H5. {ECO:0000250}.; INTRAMEM 141 147 Pore-forming. {ECO:0000250}. TRANSMEM 82 106 Helical; Name=M1. {ECO:0000250}.; TRANSMEM 157 178 Helical; Name=M2. {ECO:0000250}. TOPO_DOM 2 81 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 107 128 Extracellular. {ECO:0000250}.; TOPO_DOM 148 156 Extracellular. {ECO:0000250}.; TOPO_DOM 179 428 Cytoplasmic. {ECO:0000250}. FUNCTION: Probably participates in establishing action potential waveform and excitability of neuronal and muscle tissues. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by extracellular barium and cesium. PTM: S-nitrosylation increases the open probability and inward rectifying currents. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Membrane; Lipid-anchor {ECO:0000250|UniProtKB:P63252}. SUBUNIT: Homomultimeric and heteromultimeric association with KCNJ4/Kir2.3. Association, via its PDZ-recognition domain, with LIN7A, LIN7B, LIN7C, DLG1, CASK and APBA1 plays a key role in its localization and trafficking (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Prominently expressed in the central nervous system. Also found in other excitable tissues such as heart and skeletal muscle. +O35174 KCNS2_MOUSE Potassium voltage-gated channel subfamily S member 2 (Delayed-rectifier K(+) channel alpha subunit 2) (Voltage-gated potassium channel subunit Kv9.2) 477 54,289 Chain (1); Intramembrane (2); Motif (1); Topological domain (8); Transmembrane (6) INTRAMEM 362 373 Helical; Name=Pore helix. {ECO:0000250|UniProtKB:P63142}.; INTRAMEM 374 381 {ECO:0000250|UniProtKB:P63142}. TRANSMEM 185 206 Helical; Name=Segment S1. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 226 248 Helical; Name=Segment S2. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 260 280 Helical; Name=Segment S3. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 291 311 Helical; Voltage-sensor; Name=Segment S4. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 327 348 Helical; Name=Segment S5. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 389 417 Helical; Name=Segment S6. {ECO:0000250|UniProtKB:P63142}. TOPO_DOM 1 184 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 207 225 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 249 259 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 281 290 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 312 326 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 349 361 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 382 388 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 418 477 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}. FUNCTION: Potassium channel subunit that does not form functional channels by itself. Can form functional heterotetrameric channels with KCNB1 and KCNB2; modulates the delayed rectifier voltage-gated potassium channel activation and deactivation rates of KCNB1 and KCNB2 (PubMed:9305895). {ECO:0000269|PubMed:9305895}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9305895}; Multi-pass membrane protein {ECO:0000305}. Note=May not reach the plasma membrane but remain in an intracellular compartment in the absence of KCNB1 or KCNB2 (PubMed:9305895). {ECO:0000269|PubMed:9305895}. SUBUNIT: Heterotetramer with KCNB1 and KCNB2 (PubMed:9305895). Does not form homomultimers (PubMed:9305895). {ECO:0000269|PubMed:9305895}. DOMAIN: The transmembrane segment S4 functions as voltage-sensor and is characterized by a series of positively charged amino acids at every third position. Channel opening and closing is effected by a conformation change that affects the position and orientation of the voltage-sensor paddle formed by S3 and S4 within the membrane. A transmembrane electric field that is positive inside would push the positively charged S4 segment outwards, thereby opening the pore, while a field that is negative inside would pull the S4 segment inwards and close the pore. Changes in the position and orientation of S4 are then transmitted to the activation gate formed by the inner helix bundle via the S4-S5 linker region. {ECO:0000250|UniProtKB:P63142}. TISSUE SPECIFICITY: Detected in brain, but not in the other tissues tested. Expression was highest in the olfactory bulb, cerebral cortex, hippocampus, habenula, basolateral amygdaloid nuclei and cerebellum (PubMed:9305895). {ECO:0000269|PubMed:9305895}. +Q9DBP5 KCY_MOUSE UMP-CMP kinase (EC 2.7.4.14) (Deoxycytidylate kinase) (CK) (dCMP kinase) (Nucleoside-diphosphate kinase) (EC 2.7.4.6) (Uridine monophosphate/cytidine monophosphate kinase) (UMP/CMP kinase) (UMP/CMPK) 196 22,165 Binding site (6); Chain (1); Cross-link (1); Erroneous initiation (7); Modified residue (5); Nucleotide binding (3); Region (2) FUNCTION: Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and CMP as phosphate acceptors. Also displays broad nucleoside diphosphate kinase activity. {ECO:0000255|HAMAP-Rule:MF_03172}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03172}. Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03172}. Note=Predominantly nuclear. {ECO:0000255|HAMAP-Rule:MF_03172}. SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03172}. DOMAIN: Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis. {ECO:0000255|HAMAP-Rule:MF_03172}. +Q9WVJ0 KCNH3_MOUSE Potassium voltage-gated channel subfamily H member 3 (Ether-a-go-go-like potassium channel 2) (ELK channel 2) (mElk2) (Voltage-gated potassium channel subunit Kv12.2) 1095 118,244 Chain (1); Compositional bias (1); Domain (2); Glycosylation (3); Intramembrane (1); Motif (1); Nucleotide binding (1); Sequence conflict (19); Topological domain (8); Transmembrane (6) INTRAMEM 465 485 Pore-forming; Name=Segment H5. {ECO:0000255}. TRANSMEM 229 249 Helical; Name=Segment S1. {ECO:0000255}.; TRANSMEM 260 280 Helical; Name=Segment S2. {ECO:0000255}.; TRANSMEM 303 323 Helical; Name=Segment S3. {ECO:0000255}.; TRANSMEM 332 352 Helical; Voltage-sensor; Name=Segment S4. {ECO:0000255}.; TRANSMEM 362 382 Helical; Name=Segment S5. {ECO:0000255}.; TRANSMEM 491 511 Helical; Name=Segment S6. {ECO:0000255}. TOPO_DOM 1 228 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 250 259 Extracellular. {ECO:0000255}.; TOPO_DOM 281 302 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 324 331 Extracellular. {ECO:0000255}.; TOPO_DOM 353 361 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 383 464 Extracellular. {ECO:0000255}.; TOPO_DOM 486 490 Extracellular. {ECO:0000255}.; TOPO_DOM 512 1095 Cytoplasmic. {ECO:0000255}. FUNCTION: Pore-forming (alpha) subunit of voltage-gated potassium channel. Elicits an outward current with fast inactivation. Channel properties may be modulated by cAMP and subunit assembly. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SUBUNIT: The potassium channel is probably composed of a homo- or heterotetrameric complex of pore-forming alpha subunits that can associate with modulating beta subunits. DOMAIN: The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position. TISSUE SPECIFICITY: Detected in brain, but not in other tissues. +Q8R1C0 KCNC4_MOUSE Potassium voltage-gated channel subfamily C member 4 (Voltage-gated potassium channel subunit Kv3.4) 628 68,655 Chain (1); Glycosylation (2); Modified residue (4); Motif (1); Region (1); Topological domain (4); Transmembrane (6) TRANSMEM 231 251 Helical; Name=Segment S1. {ECO:0000255}.; TRANSMEM 282 302 Helical; Name=Segment S2. {ECO:0000255}.; TRANSMEM 317 337 Helical; Name=Segment S3. {ECO:0000255}.; TRANSMEM 349 368 Helical; Voltage-sensor; Name=Segment S4. {ECO:0000255}.; TRANSMEM 385 405 Helical; Name=Segment S5. {ECO:0000255}.; TRANSMEM 456 476 Helical; Name=Segment S6. {ECO:0000255}. TOPO_DOM 1 230 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 303 316 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 369 384 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 477 628 Cytoplasmic. {ECO:0000255}. FUNCTION: This protein mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient (By similarity). {ECO:0000250}. PTM: Phosphorylation of serine residues in the inactivation gate inhibits rapid channel closure. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SUBUNIT: Homotetramer (Probable). Heterotetramer of potassium channel proteins (By similarity). {ECO:0000250, ECO:0000305}. DOMAIN: The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position. {ECO:0000250}.; DOMAIN: The tail may be important in modulation of channel activity and/or targeting of the channel to specific subcellular compartments. {ECO:0000250}. +Q03719 KCND1_MOUSE Potassium voltage-gated channel subfamily D member 1 (Voltage-gated potassium channel subunit Kv4.1) (mShal) 651 71,698 Chain (1); Glycosylation (1); Intramembrane (1); Metal binding (3); Modified residue (2); Motif (1); Region (2); Topological domain (4); Transmembrane (6) INTRAMEM 365 385 Pore-forming; Name=Segment H5. {ECO:0000255}. TRANSMEM 185 205 Helical; Name=Segment S1. {ECO:0000255}.; TRANSMEM 227 247 Helical; Name=Segment S2. {ECO:0000255}.; TRANSMEM 262 282 Helical; Name=Segment S3. {ECO:0000255}.; TRANSMEM 292 312 Helical; Voltage-sensor; Name=Segment S4. {ECO:0000255}.; TRANSMEM 326 346 Helical; Name=Segment S5. {ECO:0000255}.; TRANSMEM 387 407 Helical; Name=Segment S6. {ECO:0000255}. TOPO_DOM 1 184 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 248 261 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 313 325 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 408 651 Cytoplasmic. {ECO:0000255}. FUNCTION: Pore-forming (alpha) subunit of voltage-gated rapidly inactivating A-type potassium channels. May contribute to I(To) current in the heart and I(Sa) current in neurons. Channel properties are modulated by subunit assembly. {ECO:0000269|PubMed:2034678}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Cell projection, dendrite {ECO:0000250}. SUBUNIT: Homotetramer or heterotetramer with KCND2 and/or KCND3. Associates with the regulatory subunits KCNIP1, KCNIP2, KCNIP3 and KCNIP4. Interacts with DPP10 (By similarity). {ECO:0000250}. DOMAIN: The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position. +P07310 KCRM_MOUSE Creatine kinase M-type (EC 2.7.3.2) (Creatine kinase M chain) (Creatine phosphokinase M-type) (CPK-M) (M-CK) 381 43,045 Binding site (4); Chain (1); Domain (2); Modified residue (8); Nucleotide binding (2) FUNCTION: Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Dimer of identical or non-identical chains, which can be either B (brain type) or M (muscle type). With MM being the major form in skeletal muscle and myocardium, MB existing in myocardium, and BB existing in many tissues, especially brain. {ECO:0000250|UniProtKB:P12277}. +Q6P8J7 KCRS_MOUSE Creatine kinase S-type, mitochondrial (EC 2.7.3.2) (Basic-type mitochondrial creatine kinase) (Mib-CK) (Sarcomeric mitochondrial creatine kinase) (S-MtCK) 419 47,473 Binding site (4); Chain (1); Domain (2); Modified residue (2); Nucleotide binding (2); Region (1); Transit peptide (1) FUNCTION: Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Intermembrane side {ECO:0000250}. SUBUNIT: Exists as an octamer composed of four CKMT2 homodimers. {ECO:0000250}. +Q61595 KTN1_MOUSE Kinectin 1327 152,592 Alternative sequence (5); Chain (1); Coiled coil (1); Compositional bias (1); Glycosylation (3); Modified residue (4); Sequence conflict (8); Topological domain (2); Transmembrane (1) TRANSMEM 9 29 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 8 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 30 1327 Lumenal. {ECO:0000255}. FUNCTION: Receptor for kinesin thus involved in kinesin-driven vesicle motility. Accumulates in integrin-based adhesion complexes (IAC) upon integrin aggregation by fibronectin (By similarity). {ECO:0000250|UniProtKB:Q86UP2}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15316074}; Single-pass type II membrane protein {ECO:0000269|PubMed:15316074}. Note=Vesicle membrane protein anchored to the endoplasmic reticulum (By similarity). Some isoforms containing the inserts at residues 1007-1035 and 1154-1177 are detected in neurite processes. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in all tissues examined including 12-day embryo, adult heart, brain, ovary, kidney, lung, small intestine, spleen, thymus and pancreas. {ECO:0000269|PubMed:8912005}. +Q76LS9 MINY1_MOUSE Ubiquitin carboxyl-terminal hydrolase MINDY-1 (EC 3.4.19.12) (Deubiquitinating enzyme MINDY-1) (NF-E2 inducible protein) (Protein FAM63A) 468 51,226 Active site (2); Alternative sequence (3); Chain (1); Compositional bias (1); Modified residue (2); Region (1); Sequence caution (1); Sequence conflict (2); Site (3) FUNCTION: Hydrolase that can specifically remove 'Lys-48'-linked conjugated ubiquitin from proteins. Has exodeubiquitinase activity and has a preference for long polyubiquitin chains. May play a regulatory role at the level of protein turnover. {ECO:0000250|UniProtKB:Q8N5J2}. +Q9CV28 MINY3_MOUSE Ubiquitin carboxyl-terminal hydrolase MINDY-3 (EC 3.4.19.12) (Deubiquitinating enzyme MINDY-3) (Protein CARP) 444 49,612 Active site (2); Alternative sequence (1); Chain (1); Modified residue (1) FUNCTION: Hydrolase that can remove 'Lys-48'-linked conjugated ubiquitin from proteins. {ECO:0000250|UniProtKB:Q9H8M7}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H8M7}. SUBUNIT: Interacts with COPS5. {ECO:0000250|UniProtKB:Q9H8M7}. +Q8VE19 MIO_MOUSE GATOR complex protein MIOS 875 98,335 Chain (1); Modified residue (2); Repeat (7); Sequence conflict (1) FUNCTION: As a component of the GATOR subcomplex GATOR2, functions within the amino acid-sensing branch of the TORC1 signaling pathway. Indirectly activates mTORC1 and the TORC1 signaling pathway through the inhibition of the GATOR1 subcomplex. It is negatively regulated by the upstream amino acid sensors SESN2 and CASTOR1. {ECO:0000250|UniProtKB:Q9NXC5}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q9NXC5}. SUBUNIT: Within the GATOR complex, component of the GATOR2 subcomplex, made of MIOS, SEC13, SEH1L, WDR24 and WDR59. The GATOR complex strongly interacts with RRAGA/RRAGC and RRAGB/RRAGC heterodimers. The GATOR2 complex interacts with CASTOR2 and CASTOR1; the interaction is negatively regulated by arginine. The GATOR2 complex interacts with the sestrins SESN1, SESN2 and SESN3; the interaction is negatively regulated by amino acids. {ECO:0000250|UniProtKB:Q9NXC5}. +P01632 KV1A1_MOUSE Ig kappa chain V-I region S107A 114 12,717 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (7) FUNCTION: Anti-phosphocholine antibody. +P01627 KV2A2_MOUSE Ig kappa chain V-II region VKappa167 120 13,280 Chain (1); Disulfide bond (1); Region (6); Signal peptide (1) +P01628 KV2A3_MOUSE Ig kappa chain V-II region MOPC 511 113 12,496 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (7) +P03976 KV2A5_MOUSE Ig kappa chain V-II region 17S29.1 113 12,390 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (7) FUNCTION: Anti-streptococcal group A carbohydrate antibody. +P01630 KV2A6_MOUSE Ig kappa chain V-II region 7S34.1 113 12,496 Beta strand (9); Chain (1); Disulfide bond (1); Helix (1); Non-terminal residue (1); Region (7); Turn (1) +P01631 KV2A7_MOUSE Ig kappa chain V-II region 26-10 113 12,273 Beta strand (11); Chain (1); Disulfide bond (1); Helix (1); Non-terminal residue (1); Region (7); Turn (1) +P01654 KV3A1_MOUSE Ig kappa chain V-III region PC 2880/PC 1229 111 11,980 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (7) +P01655 KV3A2_MOUSE Ig kappa chain V-III region PC 7132 112 12,054 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (7) +P01656 KV3A3_MOUSE Ig kappa chain V-III region MOPC 70 111 11,904 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (7) +P01662 KV3AA_MOUSE Ig kappa chain V-III region ABPC 22/PC 9245 111 12,041 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (7) +P01663 KV3AB_MOUSE Ig kappa chain V-III region PC 4050 111 12,005 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (7) +P01664 KV3AC_MOUSE Ig kappa chain V-III region CBPC 101 111 11,964 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (7) +P01665 KV3AD_MOUSE Ig kappa chain V-III region PC 7043 111 12,002 Beta strand (10); Chain (1); Disulfide bond (1); Helix (1); Non-terminal residue (1); Region (7); Turn (1) +P01667 KV3AF_MOUSE Ig kappa chain V-III region PC 6308 111 12,071 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (7) +P01668 KV3AG_MOUSE Ig kappa chain V-III region PC 7210 110 11,950 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (7) +P01671 KV3AJ_MOUSE Ig kappa chain V-III region PC 7175 111 12,010 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (7) +P01672 KV3AK_MOUSE Ig kappa chain V-III region PC 7940 111 12,039 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (7) +P01673 KV3AL_MOUSE Ig kappa chain V-III region PC 2485/PC 4039 111 11,987 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (7) +P01674 KV3AM_MOUSE Ig kappa chain V-III region PC 2154 108 11,699 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (7) +P01635 KV5A3_MOUSE Ig kappa chain V-V region K2 (Fragment) 115 12,581 Beta strand (9); Chain (1); Disulfide bond (1); Helix (1); Non-terminal residue (1); Region (6); Signal peptide (1); Turn (1) +P01636 KV5A4_MOUSE Ig kappa chain V-V region MOPC 149 108 12,030 Beta strand (10); Chain (1); Disulfide bond (1); Helix (1); Non-terminal residue (1); Region (7); Turn (1) +P01637 KV5A5_MOUSE Ig kappa chain V-V region T1 128 14,386 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (7); Signal peptide (1) +P01641 KV5A8_MOUSE Ig kappa chain V-V region MOPC 173B 117 12,955 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (6); Signal peptide (1) +P01653 KV5AL_MOUSE Ig kappa chain V-V region W3082 108 11,850 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (7) +P04946 KV5AM_MOUSE Ig kappa chain V-V region NQ5-89.4 108 11,870 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (7) FUNCTION: Anti-2-phenyl oxazolone (PHOX) Antibody. +P01644 KV5AB_MOUSE Ig kappa chain V-V region HP R16.7 108 11,910 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (7) +P01645 KV5AC_MOUSE Ig kappa chain V-V region HP 93G7 108 11,954 Beta strand (9); Chain (1); Disulfide bond (1); Helix (1); Non-terminal residue (1); Region (7); Turn (1) +P01675 KV6A1_MOUSE Ig kappa chain V-VI region XRPC 44 107 11,627 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (7); Sequence conflict (1) +P04944 KV6AA_MOUSE Ig kappa chain V-VI region NQ5-78.2.6 107 11,613 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (7) FUNCTION: Anti-2-phenyl oxazolone (PHOX) Antibody. +P04945 KV6AB_MOUSE Ig kappa chain V-VI region NQ2-6.1 108 11,713 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (7) +P84750 KVM5_MOUSE Ig kappa chain V region Mem5 (Fragment) 121 13,251 Beta strand (9); Chain (1); Disulfide bond (1); Domain (1); Helix (1); Non-terminal residue (1); Region (7) FUNCTION: Anti-influenza H3N2 neuraminidase antibody. {ECO:0000269|PubMed:12414967}. SUBCELLULAR LOCATION: Secreted. +Q6ZQI3 MLEC_MOUSE Malectin 291 32,342 Binding site (5); Chain (1); Compositional bias (1); Erroneous initiation (1); Glycosylation (1); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 269 289 Helical. {ECO:0000255}. TOPO_DOM 31 268 Lumenal. {ECO:0000255}.; TOPO_DOM 290 291 Cytoplasmic. {ECO:0000255}. FUNCTION: Carbohydrate-binding protein with a strong ligand preference for Glc2-N-glycan. May play a role in the early steps of protein N-glycosylation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. +Q9JK91 MLH1_MOUSE DNA mismatch repair protein Mlh1 (MutL protein homolog 1) 760 84,670 Binding site (2); Chain (1); Modified residue (1); Nucleotide binding (2); Region (1); Sequence conflict (3) FUNCTION: Heterodimerizes with Pms2 to form MutL alpha, a component of the post-replicative DNA mismatch repair system (MMR). DNA repair is initiated by MutS alpha (Msh2-Msh6) or MutS beta (MSH2-MSH3) binding to a dsDNA mismatch, then MutL alpha is recruited to the heteroduplex. Assembly of the MutL-MutS-heteroduplex ternary complex in presence of RFC and PCNA is sufficient to activate endonuclease activity of Pms2. It introduces single-strand breaks near the mismatch and thus generates new entry points for the exonuclease EXO1 to degrade the strand containing the mismatch. DNA methylation would prevent cleavage and therefore assure that only the newly mutated DNA strand is going to be corrected. MutL alpha (Mlh1-Pms2) interacts physically with the clamp loader subunits of DNA polymerase III, suggesting that it may play a role to recruit the DNA polymerase III to the site of the MMR. Also implicated in DNA damage signaling, a process which induces cell cycle arrest and can lead to apoptosis in case of major DNA damages. Heterodimerizes with Mlh3 to form MutL gamma which plays a role in meiosis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P40692}. Chromosome {ECO:0000250|UniProtKB:P40692}. Note=Recruited to chromatin in a MCM9-dependent manner. {ECO:0000250|UniProtKB:P40692}. SUBUNIT: Component of the DNA mismatch repair (MMR) complex composed at least of MSH2, MSH3, MSH6, PMS1 and MLH1. Heterodimer of MLH1 and PMS2 (MutL alpha), MLH1 and PMS1 (MutL beta) or MLH1 and MLH3 (MutL gamma). Forms a ternary complex with MutS alpha (MSH2-MSH6) or MutS beta (MSH2-MSH3). Part of the BRCA1-associated genome surveillance complex (BASC), which contains BRCA1, MSH2, MSH6, MLH1, ATM, BLM, PMS2 and the RAD50-MRE11-NBS1 protein complex. This association could be a dynamic process changing throughout the cell cycle and within subnuclear domains. Interacts with MCM9; the interaction recruits MLH1 to chromatin. Interacts MCM8. Interacts with PMS2. Interacts with MBD4. Interacts with EXO1. Interacts with MTMR15/FAN1. {ECO:0000250|UniProtKB:P40692}. +Q5FW52 MLIP_MOUSE Muscular LMNA-interacting protein (Cardiac Isl1-interacting protein) (CIP) (Muscular-enriched A-type laminin-interacting protein) 269 29,466 Alternative sequence (1); Chain (1); Compositional bias (1); Modified residue (2); Region (1); Sequence conflict (2) FUNCTION: Required for precocious cardiac adaptation to stress through integrated regulation of the AKT/mTOR pathways and FOXO1. Regulates cardiac homeostasis and plays an important role in protection against cardiac hypertrophy (PubMed:26359501, PubMed:22343712, PubMed:26436652). Acts as a transcriptional cofactor, represses transactivator activity of ISL1 and MYOCD (PubMed:22343712). {ECO:0000269|PubMed:22343712, ECO:0000269|PubMed:26359501, ECO:0000269|PubMed:26436652}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21498514, ECO:0000269|PubMed:22343712, ECO:0000269|PubMed:26436652}. Nucleus envelope {ECO:0000269|PubMed:21498514}. Nucleus, PML body {ECO:0000269|PubMed:21498514}. Cell membrane, sarcolemma {ECO:0000269|PubMed:26359501}; Peripheral membrane protein {ECO:0000269|PubMed:26359501}; Cytoplasmic side {ECO:0000269|PubMed:26359501}. SUBUNIT: Interacts with LMNA (PubMed:21498514, PubMed:26436652). Interacts with ISL1 (via N-terminal domain); the interaction represses ISL1 transactivator activity (PubMed:22343712). {ECO:0000269|PubMed:21498514, ECO:0000269|PubMed:22343712, ECO:0000269|PubMed:26436652}. TISSUE SPECIFICITY: Ubiquitous but more abundantly expressed in heart, skeletal and smooth muscle (at protein level). In brain, expressed by a subpopulation of cells within the hippocampus and cortex. In heart, expressed by ventricular cardiomyocytes. Expression is higly reduced in hypertrophic hearts (PubMed:26359501, PubMed:22343712, PubMed:26436652). {ECO:0000269|PubMed:21498514, ECO:0000269|PubMed:22343712, ECO:0000269|PubMed:26359501, ECO:0000269|PubMed:26436652}. +Q9QVP4 MLRA_MOUSE Myosin regulatory light chain 2, atrial isoform (MLC-2a) (MLC2a) (Myosin light chain 2a) (Myosin regulatory light chain 7) 175 19,450 Calcium binding (1); Chain (1); Domain (3); Initiator methionine (1); Modified residue (3); Sequence conflict (3) SUBUNIT: Myosin is a hexamer of 2 heavy chains and 4 light chains. TISSUE SPECIFICITY: Predominantly expressed in adult atrial muscle. {ECO:0000269|PubMed:8207020}. +Q9CXF0 KYNU_MOUSE Kynureninase (EC 3.7.1.3) (L-kynurenine hydrolase) 464 52,325 Binding site (8); Chain (1); Erroneous initiation (2); Modified residue (2); Region (1) Amino-acid degradation; L-kynurenine degradation; L-alanine and anthranilate from L-kynurenine: step 1/1. Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 2/3. FUNCTION: Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively. Has a preference for the L-3-hydroxy form. Also has cysteine-conjugate-beta-lyase activity. {ECO:0000255|HAMAP-Rule:MF_03017}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000255|HAMAP-Rule:MF_03017}. SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03017}. +Q8C8H8 KY_MOUSE Kyphoscoliosis peptidase (EC 3.4.-.-) 661 75,090 Active site (3); Alternative sequence (1); Chain (1); Sequence conflict (3) FUNCTION: Probable cytoskeleton-associated protease required for normal muscle growth. Involved in function, maturation and stabilization of the neuromuscular junction. May act by cleaving muscle-specific proteins such as FLNC. {ECO:0000269|PubMed:11136708, ECO:0000269|PubMed:15385448}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, myofibril, sarcomere, Z line. SUBUNIT: Interacts with IGFN1 and FLNC. {ECO:0000269|PubMed:15385448, ECO:0000269|PubMed:20206623}. TISSUE SPECIFICITY: Specifically expressed in skeletal and cardiac muscle. {ECO:0000269|PubMed:11136708}. +Q8R1F0 L10K_MOUSE Leydig cell tumor 10 kDa protein homolog 94 10,197 Chain (1) FUNCTION: May have a potential role in hypercalcemia of malignancy. {ECO:0000250}. +Q2VPU4 MLXIP_MOUSE MLX-interacting protein (Transcriptional activator MondoA) 917 100,804 Alternative sequence (2); Chain (1); Domain (1); Initiator methionine (1); Modified residue (5); Region (4); Sequence conflict (1) FUNCTION: Binds DNA as a heterodimer with MLX and activates transcription. Binds to the canonical E box sequence 5'-CACGTG-3'. Plays a role in transcriptional activation of glycolytic target genes. Involved in glucose-responsive gene regulation. {ECO:0000250|UniProtKB:Q9HAP2, ECO:0000269|PubMed:11073985, ECO:0000269|PubMed:16644671}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11073985}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:11073985}. Mitochondrion outer membrane {ECO:0000269|PubMed:11073985}. Note=Predominantly cytoplasmic but shuttles between cytoplasm and nucleus when associated with MLX. Also associates with the outer mitochondrial membrane and may shuttle between the outer mitochondrial membrane and the nucleus. {ECO:0000250|UniProtKB:Q9HAP2, ECO:0000269|PubMed:11073985}. SUBUNIT: Efficient DNA binding requires dimerization with another bHLH protein. Binds DNA as a homodimer or a heterodimer with MLX. {ECO:0000269|PubMed:11073985}. +Q99MZ3 MLXPL_MOUSE Carbohydrate-responsive element-binding protein (ChREBP) (MLX interactor) (MLX-interacting protein-like) (Williams-Beuren syndrome chromosomal region 14 protein homolog) 864 94,875 Alternative sequence (7); Chain (1); Compositional bias (1); Domain (1); Helix (1); Modified residue (9); Region (1); Sequence conflict (8) FUNCTION: Transcriptional repressor. Binds to the canonical and non-canonical E box sequences 5'-CACGTG-3'. PTM: Phosphorylation at Ser-566 by AMPK inactivates the DNA-binding activity. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}. SUBUNIT: Binds DNA as a heterodimer with TCFL4/MLX. TISSUE SPECIFICITY: Expressed in the ventricular and intermediate zones of the developing spinal cord of E12.5 embryos. In later embryos expressed in a variety of tissues. +P01844 LAC2_MOUSE Ig lambda-2 chain C region 104 11,255 Beta strand (9); Chain (1); Disulfide bond (2); Domain (1); Helix (2); Non-terminal residue (1) +Q9D273 MMAB_MOUSE Corrinoid adenosyltransferase (EC 2.5.1.17) (Cob(II)alamin adenosyltransferase) (Cob(II)yrinic acid a,c-diamide adenosyltransferase) (Cobinamide/cobalamin adenosyltransferase) (Methylmalonic aciduria type B homolog) 237 26,273 Alternative sequence (1); Binding site (2); Chain (1); Modified residue (4); Nucleotide binding (3); Transit peptide (1) Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 2/7. FUNCTION: Adenosyltransferase involved in intracellular vitamin B12 metabolism. Generates adenosylcobalamin (AdoCbl) and directly delivers the cofactor to MUT in a transfer taht is stimulated by ATP-binding to MMAB and gated by MMAA. {ECO:0000250|UniProtKB:Q96EY8}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q96EY8}. SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:Q96EY8}. +P01845 LAC3_MOUSE Ig lambda-3 chain C region 104 11,371 Chain (1); Disulfide bond (2); Domain (1); Non-terminal residue (1) +Q9CZD0 MMAC_MOUSE Methylmalonic aciduria and homocystinuria type C protein homolog (EC 1.16.1.-) (CblC) (Cyanocobalamin reductase (cyanide-eliminating)) 279 31,648 Binding site (3); Chain (1); Erroneous initiation (2); Frameshift (1); Modified residue (3); Region (2); Sequence conflict (4) Cofactor biosynthesis; adenosylcobalamin biosynthesis. FUNCTION: Catalyzes the reductive dealkylation of cyanocobalamin to cob(II)alamin, using FAD or FMN as cofactor and NADPH as cosubstrate. Can also catalyze the glutathione-dependent reductive demethylation of methylcobalamin, and, with much lower efficiency, the glutathione-dependent reductive demethylation of adenosylcobalamin. Under anaerobic conditions cob(I)alamin is the first product; it is highly reactive and is converted to aquocob(II)alamin in the presence of oxygen. Binds cyanocobalamin, adenosylcobalamin, methylcobalamin and other, related vitamin B12 derivatives. {ECO:0000250|UniProtKB:Q9Y4U1}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y4U1}. SUBUNIT: Monomer in the absence of bound substrate. Homodimer; dimerization is triggered by binding to FMN or adenosylcobalamin. Heterodimer with MMADHC. {ECO:0000250|UniProtKB:Q9Y4U1}. TISSUE SPECIFICITY: Detected in liver and kidney (at protein level) (PubMed:21697092). Detected in embryos (PubMed:24889031). {ECO:0000269|PubMed:21697092, ECO:0000269|PubMed:24889031}. +O55123 MMP10_MOUSE Stromelysin-2 (SL-2) (EC 3.4.24.22) (Matrix metalloproteinase-10) (MMP-10) (Transin-2) 476 53,911 Active site (1); Chain (1); Disulfide bond (1); Metal binding (8); Motif (1); Propeptide (1); Repeat (4); Signal peptide (1) FUNCTION: Can degrade fibronectin, gelatins of type I, III, IV, and V; weakly collagens III, IV, and V. Activates procollagenase. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000305}. DOMAIN: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme. TISSUE SPECIFICITY: Expressed in small intestine. Weak levels in heart and lung. +Q8BZT9 LACC1_MOUSE Laccase domain-containing protein 1 430 47,514 Chain (1); Mutagenesis (2) FUNCTION: Central regulator of the metabolic function and bioenergetic state of macrophages. In macrophages, promotes flux through de novo lipogenesis to concomitantly drive high levels of both fatty-acid oxidation and glycolysis. {ECO:0000269|PubMed:27478939}. SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:Q8IV20}. SUBUNIT: Interacts with FASN. {ECO:0000250|UniProtKB:Q8IV20}. +Q02853 MMP11_MOUSE Stromelysin-3 (SL-3) (ST3) (EC 3.4.24.-) (Matrix metalloproteinase-11) (MMP-11) 492 55,441 Active site (1); Beta strand (12); Chain (1); Disulfide bond (1); Helix (3); Metal binding (12); Motif (1); Propeptide (1); Repeat (4); Signal peptide (1) FUNCTION: May play an important role in the progression of epithelial malignancies. PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000305}. DOMAIN: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme. TISSUE SPECIFICITY: Specifically expressed in the mammary gland during apoptosis. +P34960 MMP12_MOUSE Macrophage metalloelastase (MME) (EC 3.4.24.65) (Matrix metalloproteinase-12) (MMP-12) 473 54,971 Active site (1); Chain (1); Disulfide bond (1); Erroneous initiation (2); Glycosylation (3); Metal binding (23); Motif (1); Propeptide (1); Repeat (4); Sequence conflict (31); Signal peptide (1) FUNCTION: May be involved in tissue injury and remodeling. Has significant elastolytic activity. Can accept large and small amino acids at the P1' site, but has a preference for leucine. Aromatic or hydrophobic residues are preferred at the P1 site, with small hydrophobic residues (preferably alanine) occupying P3 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. DOMAIN: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme. +P53690 MMP14_MOUSE Matrix metalloproteinase-14 (MMP-14) (EC 3.4.24.80) (MMP-X1) (MT-MMP) (Membrane-type matrix metalloproteinase 1) (MT-MMP 1) (MTMMP1) (Membrane-type-1 matrix metalloproteinase) (MT1-MMP) (MT1MMP) 582 65,919 Active site (1); Chain (1); Disulfide bond (1); Metal binding (4); Modified residue (1); Motif (1); Propeptide (1); Repeat (4); Sequence conflict (13); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 542 562 Helical. {ECO:0000255}. TOPO_DOM 112 541 Extracellular. {ECO:0000255}.; TOPO_DOM 563 582 Cytoplasmic. {ECO:0000255}. FUNCTION: Endopeptidase that degrades various components of the extracellular matrix such as collagen. Activates progelatinase A. Essential for pericellular collagenolysis and modeling of skeletal and extraskeletal connective tissues during development (PubMed:10520996). May be involved in actin cytoskeleton reorganization by cleaving PTK7 (By similarity). Acts as a positive regulator of cell growth and migration via activation of MMP15. Involved in the formation of the fibrovascular tissues (By similarity). Cleaves ADGRB1 to release vasculostatin-40 which inhibits angiogenesis (By similarity). {ECO:0000250|UniProtKB:P50281, ECO:0000269|PubMed:10520996}. PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}.; PTM: Tyrosine phosphorylated by PKDCC/VLK. {ECO:0000250|UniProtKB:P50281}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}; Extracellular side {ECO:0000305}. Melanosome {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Forms a complex with BST2 and localizes to the cytoplasm. {ECO:0000250}. SUBUNIT: Interacts (via C-terminal cytoplasmic tail) with BST2. Interacts with DLL1; inhibits DLL1-induced Notch signaling. {ECO:0000250|UniProtKB:P50281}. DOMAIN: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme. TISSUE SPECIFICITY: Highly expressed in placenta, kidney, heart, lung, embryonic skeletal and periskeletal tissues. +Q9WTR0 MMP16_MOUSE Matrix metalloproteinase-16 (MMP-16) (EC 3.4.24.-) (Membrane-type matrix metalloproteinase 3) (MT-MMP 3) (MTMMP3) (Membrane-type-3 matrix metalloproteinase) (MT3-MMP) (MT3MMP) 607 69,571 Active site (1); Chain (1); Disulfide bond (1); Glycosylation (1); Metal binding (16); Motif (1); Propeptide (1); Repeat (4); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 565 585 Helical. {ECO:0000255}. TOPO_DOM 120 564 Extracellular. {ECO:0000255}.; TOPO_DOM 586 607 Cytoplasmic. {ECO:0000255}. FUNCTION: Endopeptidase that degrades various components of the extracellular matrix, such as collagen type III and fibronectin. Activates progelatinase A. Involved in the matrix remodeling of blood vessels. It has no effect on type I, II, IV and V collagen. However, upon interaction with CSPG4, it may be involved in degradation and invasion of type I collagen by melanoma cells (By similarity). {ECO:0000250}. PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}; Extracellular side {ECO:0000305}. Note=Localized at the cell surface of melanoma cells. {ECO:0000250}. SUBUNIT: Interacts with CSPG4 through CSPG4 chondroitin sulfate glycosaminoglycan. {ECO:0000250}. DOMAIN: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme. +Q9R0S3 MMP17_MOUSE Matrix metalloproteinase-17 (MMP-17) (EC 3.4.24.-) (Membrane-type matrix metalloproteinase 4) (MT-MMP 4) (MTMMP4) (Membrane-type-4 matrix metalloproteinase) (MT4-MMP) (MT4MMP) 578 64,333 Active site (1); Chain (1); Disulfide bond (1); Glycosylation (2); Lipidation (1); Metal binding (4); Motif (1); Mutagenesis (1); Propeptide (2); Repeat (4); Sequence conflict (2); Signal peptide (1) FUNCTION: Endopeptidase that degrades various components of the extracellular matrix, such as fibrin. May be involved in the activation of membrane-bound precursors of growth factors or inflammatory mediators, such as tumor necrosis factor-alpha. May also be involved in tumoral process. Not obvious if able to proteolytically activate progelatinase A. Does not hydrolyze collagen types I, II, III, IV and V, gelatin, fibronectin, laminin, decorin nor alpha1-antitrypsin. {ECO:0000269|PubMed:10799478}. PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor; Extracellular side. Secreted, extracellular space, extracellular matrix. DOMAIN: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme. TISSUE SPECIFICITY: Expressed by monocytes and macrophages. +Q9JHI0 MMP19_MOUSE Matrix metalloproteinase-19 (MMP-19) (EC 3.4.24.-) (Matrix metalloproteinase RASI) 527 59,122 Active site (1); Chain (1); Compositional bias (1); Disulfide bond (1); Glycosylation (4); Lipidation (1); Metal binding (4); Motif (1); Propeptide (2); Repeat (4); Signal peptide (1) FUNCTION: Endopeptidase that degrades various components of the extracellular matrix, such as aggrecan and cartilage oligomeric matrix protein (comp), during development, haemostasis and pathological conditions (arthritic disease). May also play a role in neovascularization or angiogenesis (By similarity). Hydrolyzes collagen type IV, laminin, nidogen, nascin-C isoform, fibronectin, and type I gelatin (By similarity). {ECO:0000250}. PTM: Activated by autolytic cleavage after Lys-98. {ECO:0000250}.; PTM: Tyrosine phosphorylated by PKDCC/VLK. {ECO:0000250|UniProtKB:Q99542}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}; Extracellular side {ECO:0000305}. Secreted, extracellular space, extracellular matrix {ECO:0000305}. DOMAIN: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme. TISSUE SPECIFICITY: Highly expressed in the liver. Expressed in the arterial tunica media of large blood vessels. +Q9EPL5 MMP1A_MOUSE Interstitial collagenase A (EC 3.4.24.7) (Matrix metalloproteinase-1a) (MMP-1a) (Mcol-A) 464 53,488 Active site (1); Chain (1); Disulfide bond (1); Glycosylation (2); Metal binding (19); Motif (1); Propeptide (1); Region (1); Repeat (4); Signal peptide (1) FUNCTION: Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X (By similarity). Able to degrade synthetic peptides and type I and II fibrillar collagen. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000305}. DOMAIN: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme. +P57748 MMP20_MOUSE Matrix metalloproteinase-20 (MMP-20) (EC 3.4.24.-) (Enamel metalloproteinase) (Enamelysin) 482 54,373 Active site (1); Chain (1); Disulfide bond (1); Metal binding (21); Motif (1); Propeptide (1); Repeat (4); Signal peptide (1) FUNCTION: Degrades amelogenin, the major protein component of the enamel matrix and two of the macromolecules characterizing the cartilage extracellular matrix: aggrecan and the cartilage oligomeric matrix protein (COMP). May play a central role in tooth enamel formation. Cleaves aggrecan at the '360-Asn-|-Phe-361' site. {ECO:0000250|UniProtKB:O60882}. PTM: Autoactivates at least at the 106-Asn-|-Tyr-107 site. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. DOMAIN: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme. TISSUE SPECIFICITY: Expressed specifically in the enamel organ. +O88676 MMP23_MOUSE Matrix metalloproteinase-23 (MMP-23) (EC 3.4.24.-) (Cysteine array matrix metalloproteinase) (CA-MMP) (CAMP metalloproteinase) [Cleaved into: Matrix metalloproteinase-23, soluble form] 391 44,451 Active site (1); Alternative sequence (1); Chain (2); Compositional bias (1); Disulfide bond (4); Domain (2); Glycosylation (4); Metal binding (3); Propeptide (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 19 39 Helical. {ECO:0000255}. TOPO_DOM 1 18 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 40 391 Lumenal. {ECO:0000255}. FUNCTION: Protease. May regulate the surface expression of some potassium channels by retaining them in the endoplasmic reticulum (By similarity). {ECO:0000250}. PTM: N-glycosylated. {ECO:0000250}.; PTM: Proteolytic cleavage might yield an active form. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Membrane {ECO:0000269|PubMed:10471791}; Single-pass type II membrane protein {ECO:0000269|PubMed:10471791}. Note=A secreted form produced by proteolytic cleavage may also exist. {ECO:0000250}. DOMAIN: The ShKT domain associates with, and blocks several potassium channels in the nanomolar to low micromolar range. The relative affinity is Kv1.6 > Kv1.3 > Kv1.1 = Kv3.2 > Kv1.4 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed at relatively high level in heart, lung and spleen. Not detected in brain, liver, skeletal muscle, kidney and testis. {ECO:0000269|PubMed:10471791}. +P41245 MMP9_MOUSE Matrix metalloproteinase-9 (MMP-9) (EC 3.4.24.35) (92 kDa gelatinase) (92 kDa type IV collagenase) (Gelatinase B) (GELB) 730 80,535 Active site (1); Chain (1); Disulfide bond (7); Domain (3); Glycosylation (3); Metal binding (21); Motif (1); Natural variant (3); Propeptide (1); Repeat (4); Sequence conflict (3); Signal peptide (1) FUNCTION: Could play a role in bone osteoclastic resorption. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments (By similarity). {ECO:0000250}. PTM: N- and O-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000305}. SUBUNIT: Exists as monomer or homodimer; disulfide-linked. Exists also as heterodimer with LCN2. Interacts with ECM1. {ECO:0000250|UniProtKB:P14780}. DOMAIN: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme. +A6H6E2 MMRN2_MOUSE Multimerin-2 943 105,206 Alternative sequence (1); Chain (1); Coiled coil (3); Compositional bias (1); Disulfide bond (3); Domain (2); Frameshift (1); Glycosylation (12); Sequence conflict (1); Signal peptide (1) FUNCTION: Inhibits endothelial cells motility and acts as a negative regulator of angiogenesis; it downregulates KDR activation by binding VEGFA. {ECO:0000250}. PTM: N- and O-glycosylated. {ECO:0000250|UniProtKB:Q9H8L6}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q9H8L6}. SUBUNIT: Heteromer of p110, p125, p140 and p200 subunits; disulfide-linked. Interacts with VEGFA. {ECO:0000250}. +P19137 LAMA1_MOUSE Laminin subunit alpha-1 (Laminin A chain) (Laminin-1 subunit alpha) (Laminin-3 subunit alpha) (S-laminin subunit alpha) (S-LAM alpha) 3083 338,148 Beta strand (72); Chain (1); Coiled coil (3); Disulfide bond (67); Domain (27); Glycosylation (16); Helix (6); Modified residue (1); Motif (1); Region (1); Sequence conflict (10); Signal peptide (1); Turn (1) FUNCTION: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. PTM: Tyrosine phosphorylated by PKDCC/VLK. {ECO:0000250|UniProtKB:P25391}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane. Note=Major component. SUBUNIT: Laminin is a complex glycoprotein, consisting of three different polypeptide chains (alpha, beta, gamma), which are bound to each other by disulfide bonds into a cross-shaped molecule comprising one long and three short arms with globules at each end. Alpha-1 is a subunit of laminin-1 (laminin-111 or EHS laminin) and laminin-3 (laminin-121 or S-laminin). DOMAIN: The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure.; DOMAIN: Domains VI, IV and G are globular. +P97927 LAMA4_MOUSE Laminin subunit alpha-4 (Laminin-14 subunit alpha) (Laminin-8 subunit alpha) (Laminin-9 subunit alpha) 1816 201,819 Chain (1); Coiled coil (4); Disulfide bond (19); Domain (9); Glycosylation (18); Motif (1); Region (1); Sequence conflict (20); Signal peptide (1) FUNCTION: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane. Note=Major component. SUBUNIT: Laminin is a complex glycoprotein, consisting of three different polypeptide chains (alpha, beta, gamma), which are bound to each other by disulfide bonds into a cross-shaped molecule comprising one long and three short arms with globules at each end. Alpha-4 is a subunit of laminin-8 (laminin-411), laminin-9 (laminin-421) and laminin-14 (laminin-423). DOMAIN: The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure.; DOMAIN: Domain G is globular. TISSUE SPECIFICITY: Strongly expressed in peripheral nerves, cardiac muscle, fat, dermis, lung stroma, aortic endothelium, endocardium and endothelium of blood vessels in skin and brain. +Q61001 LAMA5_MOUSE Laminin subunit alpha-5 (Laminin-10 subunit alpha) (Laminin-11 subunit alpha) (Laminin-15 subunit alpha) 3718 404,054 Beta strand (15); Chain (1); Coiled coil (4); Disulfide bond (88); Domain (30); Glycosylation (26); Helix (8); Motif (2); Region (2); Sequence conflict (7); Signal peptide (1); Turn (3) FUNCTION: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Alpha-5 may be the major laminin alpha chain of adult epithelial and/or endothelial basal laminae. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane. Note=Major component. SUBUNIT: Laminin is a complex glycoprotein, consisting of three different polypeptide chains (alpha, beta, gamma), which are bound to each other by disulfide bonds into a cross-shaped molecule comprising one long and three short arms with globules at each end. Alpha-5 is a subunit of laminin-10 (laminin-511), laminin-11 (laminin-521) and laminin-15 (laminin-523). DOMAIN: The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure.; DOMAIN: Domains VI, IV and G are globular. TISSUE SPECIFICITY: In adult, high levels in heart, lung, and kidney; lower in brain, muscle and testis; very low in liver, gut and skin. Expressed in many tissues in embryonic day 11. +Q61092 LAMC2_MOUSE Laminin subunit gamma-2 (Epiligrin subunit gamma) (Kalinin subunit gamma) (Kalinin/nicein/epiligrin 100 kDa subunit) (Laminin B2t chain) (Laminin-5 subunit gamma) (Nicein subunit gamma) 1191 130,161 Chain (1); Coiled coil (4); Disulfide bond (26); Domain (10); Glycosylation (5); Motif (1); Mutagenesis (6); Region (1); Signal peptide (1) FUNCTION: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane. Note=Major component. SUBUNIT: Laminin is a complex glycoprotein, consisting of three different polypeptide chains (alpha, beta, gamma), which are bound to each other by disulfide bonds into a cross-shaped molecule comprising one long and three short arms with globules at each end. Gamma-2 is a subunit of laminin-5 (laminin-332 or epiligrin/kalinin/nicein). Binds to fibulin-1, fibulin-1c, fibulin-2 and nidogen. DOMAIN: The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure.; DOMAIN: Domain IV is globular. TISSUE SPECIFICITY: Epithelial cells of many tissues, particularly high levels in tongue, hair follicles and kidney. Basement membranes of the collecting tubules of kidney and pancreas. +P17047 LAMP2_MOUSE Lysosome-associated membrane glycoprotein 2 (LAMP-2) (Lysosome-associated membrane protein 2) (CD107 antigen-like family member B) (Lysosomal membrane glycoprotein type B) (LGP-B) (CD antigen CD107b) 415 45,681 Alternative sequence (2); Beta strand (13); Chain (1); Disulfide bond (4); Glycosylation (16); Helix (1); Region (4); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (3) TRANSMEM 380 404 Helical. {ECO:0000255|PROSITE-ProRule:PRU00740}. TOPO_DOM 26 379 Lumenal. {ECO:0000255}.; TOPO_DOM 405 415 Cytoplasmic. {ECO:0000255|PROSITE-ProRule:PRU00740}. FUNCTION: Plays an important role in chaperone-mediated autophagy, a process that mediates lysosomal degradation of proteins in response to various stresses and as part of the normal turnover of proteins with a long biological half-live (PubMed:10972293). Functions by binding target proteins, such as GAPDH and MLLT11, and targeting them for lysosomal degradation (By similarity). Required for the fusion of autophagosomes with lysosomes during autophagy (PubMed:27628032). Cells that lack LAMP2 express normal levels of VAMP8, but fail to accumulate STX17 on autophagosomes, which is the most likely explanation for the lack of fusion between autophagosomes and lysosomes (PubMed:27628032). Required for normal degradation of the contents of autophagosomes (PubMed:10972293, PubMed:12221139). Plays a role in lysosomal protein degradation in response to starvation (PubMed:27628032). Required for efficient MHCII-mediated presentation of exogenous antigens via its function in lysosomal protein degradation; antigenic peptides generated by proteases in the endosomal/lysosomal compartment are captured by nascent MHCII subunits. Is not required for efficient MHCII-mediated presentation of endogenous antigens (By similarity). {ECO:0000250|UniProtKB:P13473, ECO:0000250|UniProtKB:P17046, ECO:0000269|PubMed:10972293, ECO:0000269|PubMed:12221139, ECO:0000269|PubMed:27628032}. PTM: Extensively N-glycosylated. Contains a minor proportion of O-linked glycans. {ECO:0000269|PubMed:2142158}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P13473}; Single-pass type I membrane protein {ECO:0000255|PROSITE-ProRule:PRU00740}. Endosome membrane {ECO:0000250|UniProtKB:P13473}; Single-pass type I membrane protein {ECO:0000255|PROSITE-ProRule:PRU00740}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:12221139}. Lysosome membrane {ECO:0000269|PubMed:11082038, ECO:0000269|PubMed:2142158}; Single-pass type I membrane protein {ECO:0000255|PROSITE-ProRule:PRU00740}. Note=This protein shuttles between lysosomes, endosomes, and the plasma membrane. SUBUNIT: Monomer. Forms large homooligomers. Interacts (via its cytoplasmic region) with HSPA8. Interacts with HSP90 in the lysosome lumen; this enhances LAMP2 stability (By similarity). Interacts with MLLT11 (By similarity). {ECO:0000250|UniProtKB:P13473, ECO:0000250|UniProtKB:P17046}. TISSUE SPECIFICITY: Detected in liver and kidney (at protein level). Detected in liver and kidney. {ECO:0000269|PubMed:10972293}. +Q9JJK2 LANC2_MOUSE LanC-like protein 2 (Testis-specific adriamycin sensitivity protein) 450 50,777 Chain (1); Initiator methionine (1); Lipidation (1); Modified residue (1); Region (1) FUNCTION: Necessary for abscisic acid (ABA) binding on the cell membrane and activation of the ABA signaling pathway in granulocytes. {ECO:0000250|UniProtKB:Q9NS86}. PTM: Myristoylated. Essential for membrane association. {ECO:0000250|UniProtKB:Q9NS86}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NS86}. Cytoplasm {ECO:0000250|UniProtKB:Q9NS86}. Cell membrane {ECO:0000250|UniProtKB:Q9NS86}. Note=Localizes to the juxta-nuclear vesicles. Associates with the cortical actin cytoskeleton. Cholesterol depletion by methyl-beta-cyclodextrin causes partial dissociation from the cell membrane in vitro and an enhanced cell detachment from the matrix in vivo. {ECO:0000250|UniProtKB:Q9NS86}. SUBUNIT: Interacts with an array of inositol phospholipids such as phosphatidylinositol 3-phosphate (PI3P), phosphatidylinositol 4-phosphate (PI4P) and phosphatidylinositol 5-phosphate (PI5P). PIP-binding enhances membrane association. {ECO:0000250|UniProtKB:Q9NS86}. +Q8CD19 LANC3_MOUSE LanC-like protein 3 420 46,475 Alternative sequence (1); Chain (1); Frameshift (1); Sequence conflict (1) +Q8BN59 LARP6_MOUSE La-related protein 6 (Acheron) (Achn) (La ribonucleoprotein domain family member 6) 492 54,873 Chain (1); Domain (2); Initiator methionine (1); Modified residue (3); Motif (2); Sequence conflict (3) FUNCTION: Regulates the coordinated translation of type I collagen alpha-1 and alpha-2 mRNAs, CO1A1 and CO1A2. Stabilizes mRNAs through high-affinity binding of a stem-loop structure in their 5' UTR. This regulation requires VIM and MYH10 filaments, and the helicase DHX9 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Shuttles between the nucleus and the cytoplasm. {ECO:0000250}. SUBUNIT: Interacts (via the HTH domain) with VIM/vimentin. Interacts (via C-terminus) with non-muscle myosin MYH10. Interacts (via C-terminus) with DHX9 (By similarity). {ECO:0000250}. DOMAIN: The RRM domain mediates the association with collagen mRNAs stem-loops. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in numerous tissues. Highest expression in heart and brain, intermediate in kidney, skeletal muscle and testis, lowest expression in testis (at protein level). {ECO:0000269|PubMed:17383118}. +Q8CGA3 LAT4_MOUSE Large neutral amino acids transporter small subunit 4 (L-type amino acid transporter 4) (Solute carrier family 43 member 2) 568 62,430 Chain (1); Glycosylation (1); Modified residue (3); Sequence conflict (2); Transmembrane (12) TRANSMEM 20 40 Helical. {ECO:0000255}.; TRANSMEM 90 110 Helical. {ECO:0000255}.; TRANSMEM 120 140 Helical. {ECO:0000255}.; TRANSMEM 143 163 Helical. {ECO:0000255}.; TRANSMEM 177 197 Helical. {ECO:0000255}.; TRANSMEM 207 227 Helical. {ECO:0000255}.; TRANSMEM 319 341 Helical. {ECO:0000255}.; TRANSMEM 365 385 Helical. {ECO:0000255}.; TRANSMEM 434 454 Helical. {ECO:0000255}.; TRANSMEM 461 481 Helical. {ECO:0000255}.; TRANSMEM 489 509 Helical. {ECO:0000255}.; TRANSMEM 515 535 Helical. {ECO:0000255}. FUNCTION: Sodium-, chloride-, and pH-independent, high affinity transport of large neutral amino acids. {ECO:0000269|PubMed:15659399}. PTM: Glycosylated. {ECO:0000269|PubMed:15659399}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:15659399}; Multi-pass membrane protein {ECO:0000269|PubMed:15659399}. TISSUE SPECIFICITY: Expressed in intestine, kidney, brain and adipose tissue, heart and testis. In the kidney, is detected in epithelial cells of the distal tubule and collecting duct. In the intestine, is expressed mainly in crypt cells of the intestinal microvilli and epithelial cells in the base of the villus. {ECO:0000269|PubMed:15659399}. +Q9Z1M7 LARG1_MOUSE LARGE xylosyl- and glucuronyltransferase 1 (EC 2.4.-.-) (Acetylglucosaminyltransferase-like 1A) (Glycosyltransferase-like protein) [Includes: Xylosyltransferase LARGE (EC 2.4.2.-); Beta-1,3-glucuronyltransferase LARGE (EC 2.4.1.-)] 756 87,964 Chain (1); Coiled coil (1); Erroneous initiation (1); Frameshift (1); Glycosylation (4); Metal binding (4); Region (2); Sequence conflict (4); Topological domain (2); Transmembrane (1) TRANSMEM 11 31 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 10 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 32 756 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Bifunctional glycosyltransferase with both xylosyltransferase and beta-1,3-glucuronyltransferase activities involved in the biosynthesis of the phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-3-N-acetylglucosamine-beta-4-(phosphate-6-)mannose), a carbohydrate structure present in alpha-dystroglycan (DAG1) (PubMed:23125099, PubMed:23135544). Phosphorylated O-mannosyl trisaccharid is required for binding laminin G-like domain-containing extracellular proteins with high affinity and plays a key role in skeletal muscle function and regeneration (PubMed:15184894, PubMed:24132234). LARGE elongates the glucuronyl-beta-1,4-xylose-beta disaccharide primer structure initiated by B3GNT1/B4GAT1 by adding repeating units [-3-Xylose-alpha-1,3-GlcA-beta-1-] to produce a heteropolysaccharide (By similarity). {ECO:0000250|UniProtKB:O95461, ECO:0000269|PubMed:15184894, ECO:0000269|PubMed:23125099, ECO:0000269|PubMed:23135544, ECO:0000269|PubMed:24132234, ECO:0000269|PubMed:25138275}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:O95461}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:O95461}. SUBUNIT: Interacts with DAG1 (via the N-terminal domain of alpha-DAG1); the interaction increases binding of DAG1 to laminin. Interacts with B3GNT1/B4GAT1. {ECO:0000250|UniProtKB:O95461, ECO:0000269|PubMed:15210115}. TISSUE SPECIFICITY: Ubiquitous. Highest expression in heart, diaphragm and brain, where it is especially found in cerebral cortex, hippocampus, and trigeminal ganglion. {ECO:0000269|PubMed:15958417}. DISEASE: Note=Defects in Large are the cause of myodystrophy (myd), an autosomal recessive neuromuscular phenotype, probably due to abnormal post-translational modification of alpha-dystroglycan. {ECO:0000269|PubMed:11381262}. +Q5XPT3 LARG2_MOUSE LARGE xylosyl- and glucuronyltransferase 2 (EC 2.4.-.-) (Glycosyltransferase-like 1B) [Includes: Xylosyltransferase LARGE2 (EC 2.4.2.-); Beta-1,3-glucuronyltransferase LARGE2 (EC 2.4.1.-)] 690 79,514 Alternative sequence (3); Chain (1); Erroneous translation (1); Glycosylation (3); Metal binding (4); Region (2); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 9 29 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 8 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 30 690 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Bifunctional glycosyltransferase with both xylosyltransferase and beta-1,3-glucuronyltransferase activities involved in the biosynthesis of the phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-3-N-acetylglucosamine-beta-4-(phosphate-6-)mannose), a carbohydrate structure present in alpha-dystroglycan (DAG1). Phosphorylated O-mannosyl trisaccharid is required for binding laminin G-like domain-containing extracellular proteins with high affinity. Elongates the glucuronyl-beta-1,4-xylose-beta disaccharide primer structure by adding repeating units [-3-Xylose-alpha-1,3-GlcA-beta-1-] to produce a heteropolysaccharide. Has a higher activity toward alpha-dystroglycan than LARGE (PubMed:15958417). {ECO:0000269|PubMed:15958417, ECO:0000269|PubMed:23125099, ECO:0000269|PubMed:23135544, ECO:0000269|PubMed:25138275}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:15958417}; Single-pass type II membrane protein {ECO:0000305}. SUBUNIT: Interacts with B3GNT1/B4GAT1. {ECO:0000250|UniProtKB:Q8N3Y3}. TISSUE SPECIFICITY: Highly expressed in the testis and kidney, but weakly expressed in the heart and brain. Expressed during embryogenesis from 7 dpc. {ECO:0000269|PubMed:15958417}. +Q8BYR2 LATS1_MOUSE Serine/threonine-protein kinase LATS1 (EC 2.7.11.1) (Large tumor suppressor homolog 1) (WARTS protein kinase) 1129 126,258 Active site (1); Binding site (1); Chain (1); Domain (3); Modified residue (7); Motif (2); Nucleotide binding (1); Region (1); Sequence conflict (3) FUNCTION: Negative regulator of YAP1 in the Hippo signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS1 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. Acts as a tumor suppressor which plays a critical role in maintenance of ploidy through its actions in both mitotic progression and the G1 tetraploidy checkpoint. Negatively regulates G2/M transition by down-regulating CDK1 kinase activity. Involved in the control of p53 expression. Affects cytokinesis by regulating actin polymerization through negative modulation of LIMK1. May also play a role in endocrine function. Plays a role in mammary gland epithelial cells differentiation, both through the Hippo signaling pathway and the intracellular estrogen receptor signaling pathway by promoting the degradation of ESR1. {ECO:0000250|UniProtKB:O95835, ECO:0000269|PubMed:9988269}. PTM: Autophosphorylated and phosphorylated during M-phase of the cell cycle. Phosphorylated by STK3/MST2 at Ser-908 and Thr-1078, which results in its activation. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Localizes to the centrosomes throughout interphase but migrates to the mitotic apparatus, including spindle pole bodies, mitotic spindle, and midbody, during mitosis. {ECO:0000250}. SUBUNIT: Complexes with CDK1 in early mitosis. LATS1-associated CDK1 has no mitotic cyclin partner and no apparent kinase activity. Binds phosphorylated ZYX, locating this protein to the mitotic spindle and suggesting a role for actin regulatory proteins during mitosis. Binds to and colocalizes with LIMK1 at the actomyosin contractile ring during cytokinesis. Interacts (via PPxY motif 2) with YAP1 (via WW domains). Interacts with MOB1A and MOB1B. Interacts with LIMD1, WTIP and AJUBA. Interacts with ESR1, DCAF1 and DCAF13; probably recruits DCAF1 and DCAF13 to ESR1 to promote ESR1 ubiquitination and ubiquitin-mediated proteasomal degradation. Interacts with STK3/MST2; this interaction is inhibited in the presence of DLG5. Interacts with SCRIB in the presence of DLG5. {ECO:0000250|UniProtKB:O95835}. +A3KMN5 LARGN_MOUSE Protein Largen (Proline-rich protein 16) 304 32,836 Alternative sequence (1); Chain (1); Coiled coil (1); Compositional bias (1) FUNCTION: Regulator of cell size that promotes cell size increase independently of mTOR and Hippo signaling pathways. Acts by stimulating the translation of specific mRNAs, including those encoding proteins affecting mitochondrial functions. Increases mitochondrial mass and respiration (Probable). {ECO:0000305|PubMed:24656129}. +Q9QXW9 LAT2_MOUSE Large neutral amino acids transporter small subunit 2 (L-type amino acid transporter 2) (mLAT2) (Solute carrier family 7 member 8) 531 57,873 Chain (1); Modified residue (5); Transmembrane (12) TRANSMEM 39 59 Helical. {ECO:0000255}.; TRANSMEM 71 91 Helical. {ECO:0000255}.; TRANSMEM 112 132 Helical. {ECO:0000255}.; TRANSMEM 154 174 Helical. {ECO:0000255}.; TRANSMEM 188 208 Helical. {ECO:0000255}.; TRANSMEM 230 250 Helical. {ECO:0000255}.; TRANSMEM 267 287 Helical. {ECO:0000255}.; TRANSMEM 309 329 Helical. {ECO:0000255}.; TRANSMEM 361 381 Helical. {ECO:0000255}.; TRANSMEM 387 407 Helical. {ECO:0000255}.; TRANSMEM 421 441 Helical. {ECO:0000255}.; TRANSMEM 446 466 Helical. {ECO:0000255}. FUNCTION: Sodium-independent, high-affinity transport of small and large neutral amino acids such as alanine, serine, threonine, cysteine, phenylalanine, tyrosine, leucine, arginine and tryptophan, when associated with SLC3A2/4F2hc. Acts as an amino acid exchanger. Has higher affinity for L-phenylalanine than LAT1 but lower affinity for glutamine and serine. L-alanine is transported at physiological concentrations. Plays a role in basolateral (re)absorption of neutral amino acids. Involved in the uptake of methylmercury (MeHg) when administered as the L-cysteine or D,L-homocysteine complexes, and hence plays a role in metal ion homeostasis and toxicity. Involved in the cellular activity of small molecular weight nitrosothiols, via the stereoselective transport of L-nitrosocysteine (L-CNSO) across the transmembrane. Plays an essential role in the reabsorption of neutral amino acids from the epithelial cells to the bloodstream in the kidney. {ECO:0000269|PubMed:10574970}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Basolateral cell membrane {ECO:0000269|PubMed:10574970}; Multi-pass membrane protein {ECO:0000269|PubMed:10574970}. Note=Localized to the cytoplasm when expressed alone (By similarity). When coexpressed with SLC3A2/4F2hc, is localized to the plasma membrane. Colocalized with SLC3A2/4F2hc at the basolateral membrane of kidney cortex proximal tubules and small intestine epithelia of the villi. {ECO:0000250}. SUBUNIT: Disulfide-linked heterodimer with the amino acid transport protein SLC3A2/4F2hc. {ECO:0000269|PubMed:10574970}. TISSUE SPECIFICITY: Strongly expressed in kidney and small intestine. Moderately present in placenta, ovary and brain. {ECO:0000269|PubMed:10574970}. +Q8C129 LCAP_MOUSE Leucyl-cystinyl aminopeptidase (Cystinyl aminopeptidase) (EC 3.4.11.3) (Oxytocinase) (OTase) 1025 117,304 Active site (1); Binding site (1); Chain (1); Glycosylation (17); Metal binding (3); Modified residue (4); Motif (2); Region (2); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 110 131 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 109 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 132 1025 Extracellular. {ECO:0000255}. FUNCTION: Release of an N-terminal amino acid, cleave before cysteine, leucine as well as other amino acids. Degrades peptide hormones such as oxytocin, vasopressin and angiotensin III, and plays a role in maintaining homeostasis during pregnancy. May be involved in the inactivation of neuronal peptides in the brain. Cleaves Met-enkephalin and dynorphin. Binds angiotensin IV and may be the angiotensin IV receptor in the brain (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Endomembrane system {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Localized mainly in intracellular vesicles together with GLUT4. Relocalizes to the plasma membrane in response to insulin. The dileucine internalization motif and/or the interaction with tankyrases may be involved in intracellular sequestration (By similarity). {ECO:0000250}. SUBUNIT: Homodimer. Binds tankyrases 1 and 2 (By similarity). {ECO:0000250}. +Q9D9P8 LCFC1_MOUSE LLLL and CFNLAS motif-containing protein 1 (MSSP-binding protein CTM-1) 108 12,138 Chain (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +P52955 LBX1_MOUSE Transcription factor LBX1 (Ladybird homeobox protein homolog 1) 282 30,262 Chain (1); Compositional bias (2); DNA binding (1); Erroneous initiation (1); Sequence conflict (2) FUNCTION: Transcription factor required for the development of GABAergic interneurons in the dorsal horn of the spinal cord and migration and further development of hypaxial muscle precursor cells for limb muscles, diaphragm and hypoglossal cord. {ECO:0000269|PubMed:10603359, ECO:0000269|PubMed:12062039, ECO:0000269|PubMed:16234809}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Interacts with SKOR1 which acts as a transcriptional corepressor. {ECO:0000269|PubMed:15528197}. TISSUE SPECIFICITY: Expressed in the dorsal part of the spinal cord and hindbrain and in presumptive myogenic cells in lateral regions of differentiating somites. {ECO:0000269|PubMed:8645601}. +Q9WUN8 LBX2_MOUSE Transcription factor LBX2 (Ladybird homeobox protein homolog 2) 195 20,917 Chain (1); DNA binding (1); Sequence conflict (1) FUNCTION: Putative transcription factor. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. TISSUE SPECIFICITY: Expressed in the developing urogenital system, eye and brain. {ECO:0000269|PubMed:10473138}. +Q7TNC4 LC7L2_MOUSE Putative RNA-binding protein Luc7-like 2 (CGI-74 homolog) 392 46,583 Alternative sequence (3); Chain (1); Coiled coil (1); Compositional bias (1); Modified residue (3); Sequence conflict (3) FUNCTION: May bind to RNA via its Arg/Ser-rich domain. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:17656373}. Nucleus, nucleoplasm {ECO:0000269|PubMed:17656373}. Note=Colocalizes with SCNM1 and SNRNP70 in nuclear speckles. {ECO:0000269|PubMed:17656373}. SUBUNIT: Interacts with SCNM1. {ECO:0000269|PubMed:17656373}. TISSUE SPECIFICITY: All isoforms are expressed in brain, kidney, heart, thymus, stomach, skeletal muscle, testis and spinal cord. {ECO:0000269|PubMed:17656373}. +Q3UN02 LCLT1_MOUSE Lysocardiolipin acyltransferase 1 (EC 2.3.1.-) (EC 2.3.1.51) (Acyl-CoA:lysocardiolipin acyltransferase 1) 376 44,400 Chain (1); Glycosylation (1); Modified residue (1); Motif (1); Transmembrane (4) TRANSMEM 9 29 Helical. {ECO:0000255}.; TRANSMEM 48 68 Helical. {ECO:0000255}.; TRANSMEM 309 329 Helical. {ECO:0000255}.; TRANSMEM 336 356 Helical. {ECO:0000255}. Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3. FUNCTION: Acyl-CoA:lysocardiolipin acyltransferase. Possesses both lysophosphatidylinositol acyltransferase (LPIAT) and lysophosphatidylglycerol acyltransferase (LPGAT) activities. Recognizes both monolysocardiolipin and dilysocardiolipin as substrates with a preference for linoleoyl-CoA and oleoyl-CoA as acyl donors. Acts as a remodeling enzyme for cardiolipin, a major membrane polyglycerophospholipid. Converts lysophosphatidic acid (LPA) into phosphatidic acid (PA) with a relatively low activity. Required for establishment of the hematopoietic and endothelial lineages. {ECO:0000269|PubMed:15152008, ECO:0000269|PubMed:17675553}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15152008}; Multi-pass membrane protein {ECO:0000269|PubMed:15152008}. DOMAIN: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed with highest expression in heart, liver and E12.5 aorta-gonad-mesonephros and lower levels in the E16 fetal liver and adult bone marrow. In bone marrow, highest levels are found in B-cells compared with whole bone marrow, T-cells, erythrocytes, and granulocytes. {ECO:0000269|PubMed:15152008, ECO:0000269|PubMed:16620771, ECO:0000269|PubMed:17675553}. +Q6ZPI3 LCOR_MOUSE Ligand-dependent corepressor (LCoR) (Mblk1-related protein 2) 433 47,125 Chain (1); Cross-link (2); DNA binding (1); Domain (1); Erroneous initiation (1); Frameshift (1); Modified residue (3); Motif (2); Sequence conflict (2) FUNCTION: Repressor of ligand-dependent transcription activation by various nuclear repressors. Repressor of ligand-dependent transcription activation by ESR1, ESR2, NR3C1, PGR, RARA, RARB, RARG, RXRA and VDR (By similarity). May act as transcription activator that binds DNA elements with the sequence 5'-CCCTATCGATCGATCTCTACCT-3'. {ECO:0000250, ECO:0000269|PubMed:12560079}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00320}. SUBUNIT: Interacts with ESR1 and ESR2 in the presence of estradiol. Interacts with CTBP1, HDAC3 and HDAC6. Component of a large corepressor complex that contains about 20 proteins, including CTBP1, CTBP2, HDAC1 and HDAC2 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Detected in heart and kidney. {ECO:0000269|PubMed:12560079}. +Q60787 LCP2_MOUSE Lymphocyte cytosolic protein 2 (SH2 domain-containing leukocyte protein of 76 kDa) (SLP-76 tyrosine phosphoprotein) (SLP76) 533 60,238 Chain (1); Domain (2); Helix (1); Modified residue (4); Sequence conflict (1) FUNCTION: Involved in T-cell antigen receptor mediated signaling. {ECO:0000269|PubMed:10660534}. PTM: Phosphorylated after T-cell receptor activation by ZAP70, ITK and TXK, which leads to the up-regulation of Th1 preferred cytokine IL-2. SYK-dependent phosphorylation is required for recruitment of PI3K signaling components (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. SUBUNIT: Interacts with SHB. Interacts with PRAM1 (By similarity). Interacts with SLA (PubMed:10662792). Interacts with GRB2 (PubMed:7706237). Interacts with CBLB (PubMed:10646608). Interacts (via SH2 domain) with CD6 (via tyrosine phosphorylated C-terminus) (PubMed:16914752, PubMed:24584089). Interacts with FYB1 and the phosphorylated form of FYB2 (By similarity). {ECO:0000250|UniProtKB:Q13094, ECO:0000269|PubMed:10646608, ECO:0000269|PubMed:10662792, ECO:0000269|PubMed:16914752, ECO:0000269|PubMed:24584089, ECO:0000269|PubMed:7706237}. DOMAIN: The SH2 domain mediates interaction with SHB. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in spleen, thymus, and peripheral blood leukocytes. +P16125 LDHB_MOUSE L-lactate dehydrogenase B chain (LDH-B) (EC 1.1.1.27) (LDH heart subunit) (LDH-H) 334 36,572 Active site (1); Binding site (5); Chain (1); Initiator methionine (1); Modified residue (8); Nucleotide binding (1) Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Homotetramer. +P00342 LDHC_MOUSE L-lactate dehydrogenase C chain (LDH-C) (EC 1.1.1.27) (LDH testis subunit) (LDH-X) 332 35,912 Active site (1); Beta strand (17); Binding site (5); Chain (1); Helix (12); Initiator methionine (1); Modified residue (1); Nucleotide binding (1); Sequence conflict (11); Turn (6) Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1. FUNCTION: Possible role in sperm motility. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Homotetramer. Interacts with RABL2/RABL2A; binds preferentially to GTP-bound RABL2. {ECO:0000269|PubMed:23055941}. TISSUE SPECIFICITY: Expressed within the midpiece of sperm tail (at protein level). {ECO:0000269|PubMed:23055941}. +P35951 LDLR_MOUSE Low-density lipoprotein receptor (LDL receptor) 862 94,947 Chain (1); Disulfide bond (29); Domain (10); Glycosylation (3); Modified residue (3); Motif (1); Region (2); Repeat (6); Sequence conflict (8); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 791 812 Helical. {ECO:0000255}. TOPO_DOM 22 790 Extracellular. {ECO:0000250|UniProtKB:P01131}.; TOPO_DOM 813 862 Cytoplasmic. {ECO:0000269|PubMed:11247302}. FUNCTION: Binds LDL, the major cholesterol-carrying lipoprotein of plasma, and transports it into cells by endocytosis. In order to be internalized, the receptor-ligand complexes must first cluster into clathrin-coated pits. {ECO:0000250|UniProtKB:P01130}. PTM: N- and O-glycosylated. {ECO:0000250|UniProtKB:P01130}.; PTM: Ubiquitinated by MYLIP leading to degradation. {ECO:0000250|UniProtKB:P01130}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P01130}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P01131}. Membrane, clathrin-coated pit {ECO:0000269|PubMed:11247302}. Golgi apparatus {ECO:0000250|UniProtKB:P01130}. Early endosome {ECO:0000250|UniProtKB:P01130}. Late endosome {ECO:0000250|UniProtKB:P01130}. Lysosome {ECO:0000250|UniProtKB:P01130}. Note=Rapidly endocytosed upon ligand binding. {ECO:0000269|PubMed:12169628}. SUBUNIT: Interacts (via NPXY motif) with DAB2 (via PID domain); the interaction is impaired by tyrosine phosphorylation of the NPXY motif (PubMed:11247302). Interacts (via NPXY motif) with LDLRAP1 (via PID domain) (By similarity). Interacts with ARRB1 (By similarity). Interacts with SNX17 (PubMed:12169628). Interacts with the full-length immature form of PCSK9 (via C-terminus) (By similarity). {ECO:0000250|UniProtKB:P01130, ECO:0000269|PubMed:11247302, ECO:0000269|PubMed:12169628}. DOMAIN: The NPXY motif mediates the interaction with the clathrin adapter DAB2 and with LDLRAP1 which are involved in receptor internalization. A few residues outside the motif also play a role in the interaction. {ECO:0000269|PubMed:11247302}. +Q8BTN6 LENG9_MOUSE Leukocyte receptor cluster member 9 485 52,613 Chain (1); Sequence conflict (3); Zinc finger (1) +Q8R1P5 KCNKD_MOUSE Potassium channel subfamily K member 13 (Tandem pore domain halothane-inhibited potassium channel 1) (THIK-1) 405 44,926 Chain (1); Glycosylation (2); Intramembrane (2); Topological domain (3); Transmembrane (4) INTRAMEM 95 115 Pore-forming; Name=Pore-forming 1. {ECO:0000255}.; INTRAMEM 224 244 Pore-forming; Name=Pore-forming 2. {ECO:0000255}. TRANSMEM 20 40 Helical. {ECO:0000255}.; TRANSMEM 125 145 Helical. {ECO:0000255}.; TRANSMEM 194 214 Helical. {ECO:0000255}.; TRANSMEM 263 283 Helical. {ECO:0000255}. TOPO_DOM 1 19 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 146 193 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 284 405 Cytoplasmic. {ECO:0000255}. FUNCTION: Potassium channel displaying weak inward rectification in symmetrical K(+) solution. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Homodimer. {ECO:0000305}. +A2BDX4 KCNG1_MOUSE Potassium voltage-gated channel subfamily G member 1 (Voltage-gated potassium channel subunit Kv6.1) 514 58,176 Chain (1); Intramembrane (2); Motif (1); Topological domain (8); Transmembrane (6) INTRAMEM 412 423 Helical; Name=Pore helix. {ECO:0000250|UniProtKB:P63142}.; INTRAMEM 424 431 {ECO:0000250|UniProtKB:P63142}. TRANSMEM 225 246 Helical; Name=Segment S1. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 268 289 Helical; Name=Segment S2. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 301 321 Helical; Name=Segment S3. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 339 359 Helical; Voltage-sensor; Name=Segment S4. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 375 396 Helical; Name=Segment S5. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 439 467 Helical; Name=Segment S6. {ECO:0000250|UniProtKB:P63142}. TOPO_DOM 1 224 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 247 267 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 290 300 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 322 338 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 360 374 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 397 411 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 432 438 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 468 514 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}. FUNCTION: Potassium channel subunit that does not form functional channels by itself. Can form functional heterotetrameric channels with KCNB1; modulates the delayed rectifier voltage-gated potassium channel activation and deactivation rates of KCNB1. {ECO:0000250|UniProtKB:D4AD53}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:D4AD53}; Multi-pass membrane protein {ECO:0000250|UniProtKB:D4AD53}. SUBUNIT: Heterotetramer with KCNB1. {ECO:0000250|UniProtKB:D4AD53}. DOMAIN: The transmembrane segment S4 functions as voltage-sensor and is characterized by a series of positively charged amino acids at every third position. Channel opening and closing is effected by a conformation change that affects the position and orientation of the voltage-sensor paddle formed by S3 and S4 within the membrane. A transmembrane electric field that is positive inside would push the positively charged S4 segment outwards, thereby opening the pore, while a field that is negative inside would pull the S4 segment inwards and close the pore. Changes in the position and orientation of S4 are then transmitted to the activation gate formed by the inner helix bundle via the S4-S5 linker region. {ECO:0000250|UniProtKB:P63142}. +O35219 KCNH2_MOUSE Potassium voltage-gated channel subfamily H member 2 (Ether-a-go-go-related gene potassium channel 1) (ERG-1) (Eag-related protein 1) (Ether-a-go-go-related protein 1) (MERG) (Voltage-gated potassium channel subunit Kv11.1) 1162 126,886 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (2); Glycosylation (1); Intramembrane (1); Modified residue (11); Motif (1); Natural variant (4); Nucleotide binding (1); Topological domain (8); Transmembrane (6) INTRAMEM 614 634 Pore-forming; Name=Segment H5. {ECO:0000255}. TRANSMEM 406 426 Helical; Name=Segment S1. {ECO:0000255}.; TRANSMEM 453 473 Helical; Name=Segment S2. {ECO:0000255}.; TRANSMEM 498 518 Helical; Name=Segment S3. {ECO:0000255}.; TRANSMEM 523 543 Helical; Voltage-sensor; Name=Segment S4. {ECO:0000255}.; TRANSMEM 550 570 Helical; Name=Segment S5. {ECO:0000255}.; TRANSMEM 641 661 Helical; Name=Segment S6. {ECO:0000255}. TOPO_DOM 1 405 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 427 452 Extracellular. {ECO:0000255}.; TOPO_DOM 474 497 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 519 522 Extracellular. {ECO:0000255}.; TOPO_DOM 544 549 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 571 613 Extracellular. {ECO:0000255}.; TOPO_DOM 635 640 Extracellular. {ECO:0000255}.; TOPO_DOM 662 1162 Cytoplasmic. {ECO:0000255}. FUNCTION: Pore-forming (alpha) subunit of voltage-gated inwardly rectifying potassium channel. Channel properties are modulated by cAMP and subunit assembly. Mediates the rapidly activating component of the delayed rectifying potassium current in heart (IKr) (By similarity). {ECO:0000250|UniProtKB:Q12809}. PTM: Phosphorylated on serine and threonine residues. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q12809}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: The potassium channel is probably composed of a homo- or heterotetrameric complex of pore-forming alpha subunits that can associate with modulating beta subunits. Interacts with DNAJB12 and DNAJB14; chaperones DNAJB12 and DNAJB14 promote tetramerization (By similarity). Heteromultimer with KCNH6/ERG2 and KCNH7/ERG3 (By similarity). Interacts with ALG10B (By similarity). Heteromultimer with KCNE1 and KCNE2. Interacts with CANX. The core-glycosylated, but not the fully glycosylated form interacts with RNF207. Interacts with NDFIP1 and NDFIP2 (By similarity). {ECO:0000250|UniProtKB:O08962, ECO:0000250|UniProtKB:Q12809}. DOMAIN: The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position. TISSUE SPECIFICITY: Isoform 1 is expressed in heart, brain and testis and at low levels in lung. Isoform 3 is expressed predominantly in heart. The expression of isoform 2 is low in all tissues tested. +P30275 KCRU_MOUSE Creatine kinase U-type, mitochondrial (EC 2.7.3.2) (Acidic-type mitochondrial creatine kinase) (Mia-CK) (Ubiquitous mitochondrial creatine kinase) (U-MtCK) 418 47,004 Binding site (4); Chain (1); Domain (2); Modified residue (6); Nucleotide binding (2); Region (1); Transit peptide (1) FUNCTION: Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side. SUBUNIT: Exists as an octamer composed of four MTCK homodimers. +P59997 KDM2A_MOUSE Lysine-specific demethylase 2A (EC 1.14.11.27) (F-box and leucine-rich repeat protein 11) (F-box/LRR-repeat protein 11) (JmjC domain-containing histone demethylation protein 1A) ([Histone-H3]-lysine-36 demethylase 1A) 1161 132,680 Alternative sequence (4); Beta strand (13); Binding site (2); Chain (1); Cross-link (1); Domain (2); Frameshift (1); Helix (21); Metal binding (3); Modified residue (14); Repeat (6); Sequence conflict (5); Turn (4); Zinc finger (2) FUNCTION: Histone demethylase that specifically demethylates 'Lys-36' of histone H3, thereby playing a central role in histone code. Preferentially demethylates dimethylated H3 'Lys-36' residue while it has weak or no activity for mono- and tri-methylated H3 'Lys-36'. May also recognize and bind to some phosphorylated proteins and promote their ubiquitination and degradation. Required to maintain the heterochromatic state. Associates with centromeres and represses transcription of small non-coding RNAs that are encoded by the clusters of satellite repeats at the centromere. Required to sustain centromeric integrity and genomic stability, particularly during mitosis. {ECO:0000250|UniProtKB:Q9Y2K7}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}. Note=Punctate expression throughout the nucleoplasm and enriched in the perinucleolar region. Specifically nucleates at CpG islands where it's presence results in chromatin depleted in H3K36me2 (By similarity). {ECO:0000250}. SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex. Interacts with CBX5/HP1A; the interaction promotes CBX5 localization to chromatin (By similarity). {ECO:0000250}. DOMAIN: The JmjC domain mediates demethylation activity and is required for satellite silencing. {ECO:0000250}.; DOMAIN: The CXXC zinc finger preferentially recognizes nonmethylated CpG DNA, and binding is blocked when the CpG DNA is methylated. {ECO:0000250}. +P0C7A0 KHD1B_MOUSE KH homology domain-containing protein 1B 126 14,836 Chain (1); Domain (1); Frameshift (1) +Q80U38 KHNYN_MOUSE Protein KHNYN (KH and NYN domain-containing protein) 671 74,565 Chain (1); Compositional bias (1); Erroneous initiation (1); Frameshift (1); Modified residue (1); Sequence conflict (2) +P83555 KI3L1_MOUSE Killer cell immunoglobulin-like receptor 3DL1 (CD antigen CD158e) 432 48,618 Chain (1); Disulfide bond (3); Domain (3); Glycosylation (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 336 356 Helical. {ECO:0000255}. TOPO_DOM 22 335 Extracellular. {ECO:0000255}.; TOPO_DOM 357 432 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor on natural killer (NK) cells. Inhibits the activity of NK cells thus preventing cell lysis. {ECO:0000250|UniProtKB:P43629, ECO:0000269|PubMed:12594244}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. +B1AVY7 KI16B_MOUSE Kinesin-like protein KIF16B 1312 150,058 Chain (1); Coiled coil (3); Compositional bias (1); Domain (3); Modified residue (6); Nucleotide binding (1); Sequence caution (1) FUNCTION: Plus end-directed microtubule-dependent motor protein involved in endosome transport and receptor recycling and degradation. Regulates the plus end motility of early endosomes and the balance between recycling and degradation of receptors such as EGF receptor (EGFR) and FGF receptor (FGFR). Regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. {ECO:0000269|PubMed:21238925}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Early endosome membrane {ECO:0000250}. Note=It is unclear whether association with endosomes is mediated via phosphatidylinositol 3-phosphate (PtdIns(3)P)-binding or via its interaction with RAB14. SUBUNIT: Interacts with PTPN21 (By similarity). Interacts with RAB14. {ECO:0000250, ECO:0000269|PubMed:21238925}. DOMAIN: The PX domain mediates binding to phosphatidylinositol 3-phosphate (PtdIns(3)P), phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2), phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) and phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3). Does not bind phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) (By similarity). {ECO:0000250}. +Q6PFD6 KI18B_MOUSE Kinesin-like protein KIF18B 834 91,936 Chain (1); Coiled coil (1); Domain (1); Modified residue (6); Motif (1); Nucleotide binding (1); Sequence conflict (1) FUNCTION: In complex with KIF2C, constitutes the major microtubule plus-end depolymerizing activity in mitotic cells. Its major role may be to transport KIF2C and/or MAPRE1 along microtubules (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000305}. Note=Present predominantly in the nucleus and to a lesser extent in the cytoplasm of interphase cells. During mitosis, found to be closely associated with astral microtubule plus ends emanating from the spindle pole during prometaphase and metaphase (By similarity). {ECO:0000250}. SUBUNIT: Interacts with MAPRE1; this interaction is required for efficient accumulation at microtubule plus ends. Interacts with KIF2C at microtubule tips; this interaction increases the affinity of both partners for microtubule plus ends and is required for robust microtubule depolymerization. KIF2C phosphorylation by AURKA or AURKB strongly reduces KIF18B-binding. {ECO:0000250}. +Q9QXL2 KI21A_MOUSE Kinesin-like protein KIF21A 1672 186,536 Alternative sequence (5); Chain (1); Coiled coil (3); Domain (1); Helix (2); Modified residue (12); Nucleotide binding (1); Repeat (7); Sequence conflict (3) FUNCTION: Microtubule-binding motor protein probably involved in neuronal axonal transport. In vitro, has a plus-end directed motor activity. {ECO:0000269|PubMed:10225949}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10225949}. Cell projection, dendrite {ECO:0000269|PubMed:10225949}. Cell projection, axon {ECO:0000269|PubMed:10225949}. Note=In neurons, localized to axons and dendrites. TISSUE SPECIFICITY: Widely expressed, with highest expression in brain. {ECO:0000269|PubMed:10225949}. +Q5SXA9 KIBRA_MOUSE Protein KIBRA (Kidney and brain protein) (KIBRA) (WW domain-containing protein 1) 1104 124,110 Chain (1); Coiled coil (2); Compositional bias (3); Domain (3); Erroneous initiation (2); Modified residue (11); Motif (1); Region (2); Sequence conflict (2) FUNCTION: Probable regulator of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a pivotal role in tumor suppression by restricting proliferation and promoting apoptosis. Along with NF2 can synergistically induce the phosphorylation of LATS1 and LATS2 and can probably function in the regulation of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway. Acts as a transcriptional coactivator of ESR1 which plays an essential role in DYNLL1-mediated ESR1 transactivation. Regulates collagen-stimulated activation of the ERK/MAPK cascade. Modulates directional migration of podocytes. Acts as a substrate for PRKCZ and may be associated with memory performance (By similarity). Regulates collagen-stimulated activation of the ERK/MAPK cascade. {ECO:0000250, ECO:0000269|PubMed:18190796}. PTM: Phosphorylation at Ser-542 and Ser-923 by CDK1 in response to spindle damage stress regulates mitotic exit, these two sites are dephosphorylated by CDC14B. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18190796}. Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000250}. Cell projection, ruffle membrane {ECO:0000250}. Note=Colocalizes with PRKCZ in the perinuclear region. {ECO:0000250}. SUBUNIT: Homodimer. Interacts with DDN. Interacts with DYNLL1 and histone H3. The interaction with DYNLL1 is mandatory for the recruitment and transactivation functions of ESR1 or DYNLL1 to the target chromatin and the interaction with histone H3 ensures proper regulatory interaction of WWC1-DYNLL1-ESR1 complexes with target chromatin. Interacts (via WW domains) with DDR1 (via PPxY motif) in a collagen-regulated manner. Interacts with PRKCZ (via the protein kinase domain). Forms a tripartite complex with DDR1 and PRKCZ, but predominantly in the absence of collagen. Interacts (via the ADDV motif) with PATJ (via PDZ domain 8). Interacts (via WW domains) with SYNPO (via PPxY motifs). Interacts with NF2 and SNX4 (By similarity). {ECO:0000250}. DOMAIN: The C2-domain mediates homodimerization. {ECO:0000250}. TISSUE SPECIFICITY: Mammary epithelium. {ECO:0000269|PubMed:18190796}. +Q52KG5 KI26A_MOUSE Kinesin-like protein KIF26A 1881 196,313 Chain (1); Coiled coil (1); Domain (1); Modified residue (3); Nucleotide binding (1); Sequence conflict (16) FUNCTION: Atypical kinesin that plays a key role in enteric neuron development. Acts by repressing a cell growth signaling pathway in the enteric nervous system development, possibly via its interaction with GRB2 that prevents GRB2-binding to SHC, thereby attenating the GDNF-Ret signaling. Binds to microtubules but lacks microtubule-based motility due to the absence of ATPase activity. {ECO:0000269|PubMed:19914172}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. SUBUNIT: Interacts with GRB2 (via SH2 domain). {ECO:0000269|PubMed:19914172}. TISSUE SPECIFICITY: Expressed in several neuronal populations. {ECO:0000269|PubMed:19914172}. +Q7TNC6 KI26B_MOUSE Kinesin-like protein KIF26B 2112 225,511 Chain (1); Compositional bias (3); Domain (1); Erroneous initiation (2); Modified residue (2); Mutagenesis (2); Nucleotide binding (1); Sequence conflict (4) FUNCTION: Essential for embryonic kidney development. Plays an important role in the compact adhesion between mesenchymal cells adjacent to the ureteric buds, possibly by interacting with MYH10. This could lead to the establishment of the basolateral integrity of the mesenchyme and the polarized expression of ITGA8, which maintains the GDNF expression required for further ureteric bud attraction. Although it seems to lack ATPase activity it is constitutively associated with microtubules. {ECO:0000269|PubMed:20439720, ECO:0000269|PubMed:22768111}. PTM: Phosphorylation at Thr-1859 and Ser-1962 by CDKs, mainly CDK2 and CDK5, enhances the interaction with NEDD4, polyubiquitination, and subsequent proteasomal degradation. Phosphorylation occurs upon loss of interaction with microtubules. {ECO:0000269|PubMed:22768111}.; PTM: Polyubiquitinated by NEDD4, resulting in proteasomal degradation. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20439720}. Cytoplasm, cytoskeleton {ECO:0000305|PubMed:20439720}. SUBUNIT: Interacts with MYH10. {ECO:0000269|PubMed:20439720}. TISSUE SPECIFICITY: In newborn kidney, specifically expressed in the mesenchyme. {ECO:0000269|PubMed:20439720}. +Q3UBZ5 MI4GD_MOUSE MIF4G domain-containing protein 222 25,493 Alternative sequence (2); Chain (1); Domain (1); Sequence conflict (3) FUNCTION: Functions in replication-dependent translation of histone mRNAs which differ from other eukaryotic mRNAs in that they do not end with a poly-A tail but a stem-loop. May participate in circularizing those mRNAs specifically enhancing their translation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Interacts with EIF4G1, EIF4G2 and SLBP; probably tethered by SLBP to the 3'-end of mRNAs ending with the histone stem-loop, it also interacts with EIF4G1 which is bound to their 5'-end. {ECO:0000250}. +O35066 KIF3C_MOUSE Kinesin-like protein KIF3C 796 89,973 Chain (1); Coiled coil (1); Compositional bias (1); Domain (1); Helix (1); Nucleotide binding (1); Region (1); Sequence conflict (2) FUNCTION: Microtubule-based anterograde translocator for membranous organelles. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. SUBUNIT: Heterodimer of KIF3A and KIF3C. {ECO:0000250}. +L0N7N1 KIF14_MOUSE Kinesin-like protein KIF14 1674 186,445 Beta strand (15); Chain (1); Coiled coil (2); Domain (2); Helix (11); Modified residue (4); Nucleotide binding (1); Region (3); Turn (1) FUNCTION: Microtubule motor protein that binds to microtubules with high affinity through each tubulin heterodimer and has an ATPase activity (PubMed:24949858). Plays a role in many processes like cell division, cytokinesis and also in cell proliferation and apoptosis (By similarity). During cytokinesis, targets to central spindle and midbody through its interaction with PRC1 and CIT respectively (By similarity). Regulates cell growth through regulation of cell cycle progression and cytokinesis. During cell cycle progression acts through SCF-dependent proteasomal ubiquitin-dependent protein catabolic process which controls CDKN1B degradation, resulting in positive regulation of cyclins, including CCNE1, CCND1 and CCNB1 (By similarity). During late neurogenesis, regulates the cerebellar and cerebral cortex development and olfactory bulb development through regulation of apoptosis, cell proliferation and cell division (PubMed:23308235, PubMed:24931760). Also is required for chromosome congression and alignment during mitotic cell cycle process (By similarity). Regulates cell spreading, focal adhesion dynamics, and cell migration through its interaction with RADIL resulting in regulation of RAP1A-mediated inside-out integrin activation by tethering RADIL on microtubules (By similarity). {ECO:0000250|UniProtKB:Q15058, ECO:0000269|PubMed:23308235, ECO:0000269|PubMed:24931760, ECO:0000269|PubMed:24949858}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15058}. Cytoplasm {ECO:0000250|UniProtKB:Q15058}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q15058}. Midbody {ECO:0000250|UniProtKB:Q15058}. Note=Nuclear localization observed during interphase. Nuclear localization triggered by entry into mitosis. Cytoplasmic in interphase. Cytoplasmic in metaphase cells. From prophase to metaphase, accumulates at the developing spindle poles and their associated microtubules. During anaphase, accumulates at the spindle midzone. Localization to the central spindle and midbody during anaphase is dependent upon PRC1 and CIT presence. In cells ready to undergo abscission, concentrates at the contractile ring. {ECO:0000250|UniProtKB:Q15058}. SUBUNIT: Directly interacts with PRC1 within a complex also containing KIF4A, KIF20A and KIF23; targets to the central spindle. Directly interacts with CIT depending on the activation state of the kinase (stronger interaction with the kinase-dead form); targets to the midbody. Interacts with ARRB2; the interaction is detected in the nucleus upon OR1D2 stimulation (By similarity). Interacts with AKT1; the interaction is detected in the plasma membrane upon INS stimulation and promotes AKT1 phosphorylation. Interacts with SVIL; at midbody during cytokinesis. Interacts with RADIL (via PDZ domain); recruits RADIL to the microtubule network restricting RADIL from interaction with activated RAP1A. {ECO:0000250|UniProtKB:Q15058}. DOMAIN: The kinesin motor domain binds to microtubules with high affinity and has a robust ATPase activity but a very slow motility. The kinesin motor domain protects microtubules from cold depolymerization. Binds to each tubulin heterodimer resulting in a microtubule complexes. Binds at the tubulin intradimer interface, at the crest of the protofilament, and orients slightly toward the next protofilament. {ECO:0000269|PubMed:24949858}. +Q3V300 KIF22_MOUSE Kinesin-like protein KIF22 660 73,190 Chain (1); Coiled coil (1); Cross-link (1); Domain (1); Modified residue (5); Nucleotide binding (1); Sequence conflict (3) FUNCTION: Kinesin family member that is involved in spindle formation and the movements of chromosomes during mitosis and meiosis. Binds to microtubules and to DNA. Plays a role in congression of laterally attached chromosomes in NDC80-depleted cells. {ECO:0000250|UniProtKB:Q14807, ECO:0000250|UniProtKB:Q9I869}. PTM: Ubiquitinated; mediated by SIAH1 and leading to its subsequent proteasomal degradation. {ECO:0000250|UniProtKB:Q14807}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q14807}. Cytoplasm, cytoskeleton {ECO:0000305}. SUBUNIT: Interacts with FAM83D and SIAH1. {ECO:0000250|UniProtKB:Q14807}. +Q99PW8 KIF17_MOUSE Kinesin-like protein KIF17 (MmKIF17) 1038 116,373 Chain (1); Coiled coil (2); Domain (1); Nucleotide binding (1) FUNCTION: Transports vesicles containing N-methyl-D-aspartate (NMDA) receptor 2B along microtubules. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. Cell projection, cilium {ECO:0000269|PubMed:25243405}. SUBUNIT: Interacts with LIN-10 PDZ domain. Interacts with PIWIL1. Interacts with TBATA. {ECO:0000269|PubMed:16787948, ECO:0000269|PubMed:17196196}. TISSUE SPECIFICITY: Neuron specific. +Q6NWW5 KIF24_MOUSE Kinesin-like protein KIF24 1356 150,207 Alternative sequence (1); Chain (1); Domain (2); Erroneous initiation (1); Erroneous termination (1); Modified residue (9); Nucleotide binding (1); Sequence conflict (1) FUNCTION: Microtubule-dependent motor protein that acts as a negative regulator of ciliogenesis by mediating recruitment of CCP110 to mother centriole in cycling cells, leading to restrict nucleation of cilia at centrioles. Mediates depolymerization of microtubules of centriolar origin, possibly to suppress aberrant cilia formation. Following activation by NEK2 involved in disassembly of primary cilium during G2/M phase but does not disassemble fully formed ciliary axonemes. As cilium assembly and disassembly is proposed to coexist in a dynamic equilibrium may suppress nascent cilium assembly and, potentially, ciliar re-assembly in cells that have already disassembled their cilia ensuring the completion of cilium removal in the later stages of the cell cycle (By similarity). {ECO:0000250|UniProtKB:Q5T7B8}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q5T7B8}. Note=Primarily localizes to the mother centriole/basal body and is either absent at daughter centriole. {ECO:0000250|UniProtKB:Q5T7B8}. SUBUNIT: Interacts with CCP110, CEP97, TALPID3. {ECO:0000250|UniProtKB:Q5T7B8}. TISSUE SPECIFICITY: Expressed in brain, spinal cord, and small intestine. {ECO:0000269|PubMed:11416179}. +D3YXS5 KIF28_MOUSE Kinesin-like protein KIF28P (Kinesin-like protein 6) 1028 114,827 Chain (1); Coiled coil (1); Domain (2); Nucleotide binding (1) FUNCTION: Microtubule-dependent motor protein required for mitochondrion morhology and transport of mitochondria in neuronal cells. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. +P28740 KIF2A_MOUSE Kinesin-like protein KIF2A (Kinesin-2) 705 79,756 Alternative sequence (3); Chain (1); Coiled coil (1); Domain (1); Modified residue (7); Nucleotide binding (1); Region (1); Sequence conflict (3) FUNCTION: Plus end-directed microtubule-dependent motor required for normal brain development. May regulate microtubule dynamics during axonal growth. Required for normal progression through mitosis. Required for normal congress of chromosomes at the metaphase plate. Required for normal spindle dynamics during mitosis. Promotes spindle turnover. Implicated in formation of bipolar mitotic spindles. Has microtubule depolymerization activity (By similarity). {ECO:0000250, ECO:0000269|PubMed:12887924, ECO:0000269|PubMed:9774330}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9774330}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:9774330}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:9774330}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Lysosome {ECO:0000269|PubMed:9774330}. Note=Localized to the spindle microtubules and spindle poles from prophase to metaphase. Efficient targeting to spindle microtubules and spindle poles requires the kinase activity of PLK1. Recruited to mitotic spindles by interaction with PSRC1 (By similarity). Associated with lysosomes in NIH3T3 cells. {ECO:0000250}. SUBUNIT: Interacts with AURKA, PSRC1 and PLK1. {ECO:0000250}. TISSUE SPECIFICITY: Highest level in lung. High level in ovary, moderate levels in heart, kidney, placenta, skeletal muscle and spleen (at protein level). Pancreas and spleen express a shorter isoform (at protein level). Expressed in the flagellum of elongated spermatids and sperm in the testis lumen (at protein level) (PubMed:24339785). Isoform 1 expressed in neuronal cells. Isoform 2 expressed in astrocytes and fibroblasts. {ECO:0000269|PubMed:24339785, ECO:0000269|PubMed:9774330}. +Q922S8 KIF2C_MOUSE Kinesin-like protein KIF2C (Mitotic centromere-associated kinesin) (MCAK) 721 81,085 Beta strand (14); Binding site (1); Chain (1); Coiled coil (1); Domain (1); Helix (16); Modified residue (12); Motif (1); Mutagenesis (3); Nucleotide binding (1); Region (2); Turn (2) FUNCTION: In complex with KIF18B, constitutes the major microtubule plus-end depolymerizing activity in mitotic cells (PubMed:14980225). Regulates the turnover of microtubules at the kinetochore and functions in chromosome segregation during mitosis. Plays a role in chromosome congression and is required for the lateral to end-on conversion of the chromosome-microtubule attachment (By similarity). {ECO:0000250|UniProtKB:Q99661, ECO:0000269|PubMed:14980225}. PTM: Phosphorylation by AURKB, regulates association with centromeres and kinetochores and the microtubule depolymerization activity. {ECO:0000250|UniProtKB:Q99661}.; PTM: Ubiquitinated. {ECO:0000250|UniProtKB:Q99661}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q99661}. Nucleus {ECO:0000250|UniProtKB:P70096}. Chromosome, centromere {ECO:0000250|UniProtKB:Q99661}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q99661}. Note=Associates with the microtubule network at the growing distal tip (the plus-end) of microtubules, probably through interaction with MTUS2/TIP150 and MAPRE1. Association with microtubule plus ends is also mediated by interaction with KIF18B. Centromeric localization requires the presence of BUB1 and SGO2. {ECO:0000250|UniProtKB:P70096, ECO:0000250|UniProtKB:Q99661}. SUBUNIT: Interacts with CENPH. Interacts with MTUS2/TIP150; the interaction is direct. Interacts with MAPRE1; the interaction is direct, regulated by phosphorylation and is probably required for targeting to growing microtubule plus ends. Interacts with KIF18B at microtubule tips; this interaction increases the affinity of both partners for microtubule plus ends and is required for robust microtubule depolymerization. Phosphorylation by AURKA or AURKB strongly reduces KIF18B-binding. {ECO:0000250|UniProtKB:Q99661}. DOMAIN: The microtubule tip localization signal (MtLS) motif; mediates interaction with MAPRE1 and targeting to the growing microtubule plus ends. {ECO:0000250|UniProtKB:Q99661}. +P28741 KIF3A_MOUSE Kinesin-like protein KIF3A (Microtubule plus end-directed kinesin motor 3A) 701 80,170 Chain (1); Coiled coil (1); Compositional bias (2); Domain (1); Helix (1); Modified residue (1); Nucleotide binding (1); Region (2); Sequence conflict (2) FUNCTION: Microtubule-based anterograde translocator for membranous organelles. Plus end-directed microtubule sliding activity in vitro. Plays a role in primary cilia formation (PubMed:21670265). Plays a role in centriole cohesion and subdistal appendage organization and function. Regulates the formation of the subdistal appendage via recruitement of DCTN1 to the centriole. Also required for ciliary basal feet formation and microtubule anchoring to mother centriole (PubMed:23386061). {ECO:0000269|PubMed:21670265, ECO:0000269|PubMed:23386061}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305|PubMed:21670265}. Cell projection, cilium {ECO:0000269|PubMed:21670265}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:23386061}. Note=Localizes to the subdistal appendage region of the centriole. {ECO:0000269|PubMed:23386061}. SUBUNIT: Heterodimer of KIF3A and KIF3B (PubMed:7559760). Interacts with PIFO (PubMed:20643351). Interacts with CLN3 (By similarity). Interacts with DCTN1 (PubMed:23386061). {ECO:0000250|UniProtKB:Q9Y496, ECO:0000269|PubMed:20643351, ECO:0000269|PubMed:23386061, ECO:0000269|PubMed:7559760}. TISSUE SPECIFICITY: Expressed almost exclusively in adult brain tissue (mainly in the cerebellar granular layer) within a single type of neuronal cell. +Q61768 KINH_MOUSE Kinesin-1 heavy chain (Conventional kinesin heavy chain) (Ubiquitous kinesin heavy chain) (UKHC) 963 109,551 Chain (1); Coiled coil (1); Cross-link (1); Domain (1); Initiator methionine (1); Modified residue (4); Nucleotide binding (1); Region (1); Sequence conflict (16) FUNCTION: Microtubule-dependent motor required for normal distribution of mitochondria and lysosomes. May be involved in the mechanisms of growth arrest induced by exposure to DNA-damaging drugs or by cellular senescence (PubMed:9657148). Can induce formation of neurite-like membrane protrusions in non-neuronal cells in a ZFYVE27-dependent manner (PubMed:21976701). Regulates centrosome and nuclear positioning during mitotic entry. During the G2 phase of the cell cycle in a BICD2-dependent manner, antagonizes dynein function and drives the separation of nuclei and centrosomes. Required for anterograde axonal transportation of MAPK8IP3/JIP3 which is essential for MAPK8IP3/JIP3 function in axon elongation (By similarity). {ECO:0000250|UniProtKB:P33176, ECO:0000250|UniProtKB:Q2PQA9, ECO:0000269|PubMed:21976701, ECO:0000269|PubMed:9657148}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q2PQA9}. Note=Uniformly distributed between soma and neurites in hippocampal neurons. {ECO:0000250|UniProtKB:Q2PQA9}. SUBUNIT: Oligomer composed of two heavy chains and two light chains. Interacts with GRIP1 and PPP1R42 (PubMed:11986669, PubMed:19886865). Interacts with SYBU (By similarity). Interacts with JAKMIP1 (PubMed:17532644). Interacts with PLEKHM2. Interacts with ECPAS (By similarity). Interacts with ZFYVE27 (PubMed:21976701). Found in a complex with OGT, RHOT1, RHOT2 and TRAK1 (By similarity). {ECO:0000250|UniProtKB:P33176, ECO:0000269|PubMed:11986669, ECO:0000269|PubMed:17532644, ECO:0000269|PubMed:19886865, ECO:0000269|PubMed:21976701}. DOMAIN: Composed of three structural domains: a large globular N-terminal domain which is responsible for the motor activity of kinesin (it hydrolyzes ATP and binds microtubule), a central alpha-helical coiled coil domain that mediates the heavy chain dimerization; and a small globular C-terminal domain which interacts with other proteins (such as the kinesin light chains), vesicles and membranous organelles. +Q9CR64 KISHA_MOUSE Protein kish-A (Transmembrane protein 167) (Transmembrane protein 167A) 72 8,074 Alternative sequence (1); Chain (1); Glycosylation (1); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 54 71 Helical. {ECO:0000255}. TOPO_DOM 27 53 Extracellular. {ECO:0000255}.; TOPO_DOM 72 72 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in the early part of the secretory pathway. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. +Q6Y4S4 KISS1_MOUSE Metastasis-suppressor KiSS-1 (Kisspeptin-1) [Cleaved into: Metastin (Kisspeptin-52); Kisspeptin-10 (Metastin45-54)] 130 14,117 Alternative sequence (1); Chain (1); Disulfide bond (1); Erroneous initiation (1); Modified residue (2); Peptide (2); Region (1); Signal peptide (1) FUNCTION: Metastasis suppressor protein. May regulate events downstream of cell-matrix adhesion, perhaps involving cytoskeletal reorganization. Generates a C-terminally amidated peptide, metastin which functions as the endogenous ligand of the G-protein coupled receptor GPR54. Activation of the receptor inhibits cell proliferation and cell migration, key characteristics of tumor metastasis. The receptor is also essential for normal gonadotropin-released hormone physiology and for puberty. The hypothalamic KiSS1/GPR54 system is a pivotal factor in central regulation of the gonadotropic axis at puberty and in adulthood. Intracerebroventricular administration induces an increase in serum LH and FSH levels in prepubertal male and female as well as in adult animals. {ECO:0000269|PubMed:15217982, ECO:0000269|PubMed:15375028, ECO:0000269|PubMed:15486019, ECO:0000269|PubMed:15637288}. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Weak in all tissue types with highest levels in lung and 15- 17-day embryos. Expressed in areas of the hypothalamus implicated in the neuroendocrine regulation of gonadotropin secretion, including the anteroventral periventricular nucleus, the periventricular nucleus, and the arcuate nucleus. {ECO:0000269|PubMed:12359743, ECO:0000269|PubMed:15217982}. +Q91V45 KISSR_MOUSE KiSS-1 receptor (KiSS-1R) (G-protein coupled receptor 54) (G-protein coupled receptor OT7T175) (mOT7T175) (Kisspeptins receptor) (Metastin receptor) 396 43,061 Chain (1); Disulfide bond (1); Glycosylation (3); Sequence conflict (1); Topological domain (8); Transmembrane (7) TRANSMEM 44 66 Helical; Name=1. {ECO:0000255}.; TRANSMEM 79 101 Helical; Name=2. {ECO:0000255}.; TRANSMEM 117 138 Helical; Name=3. {ECO:0000255}.; TRANSMEM 158 180 Helical; Name=4. {ECO:0000255}.; TRANSMEM 204 224 Helical; Name=5. {ECO:0000255}.; TRANSMEM 261 283 Helical; Name=6. {ECO:0000255}.; TRANSMEM 306 330 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 43 Extracellular. {ECO:0000255}.; TOPO_DOM 67 78 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 102 116 Extracellular. {ECO:0000255}.; TOPO_DOM 139 157 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 181 203 Extracellular. {ECO:0000255}.; TOPO_DOM 225 260 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 284 305 Extracellular. {ECO:0000255}.; TOPO_DOM 331 396 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for metastin (kisspeptin-52 or kp-52), a C-terminally amidated peptide of KiSS1. KiSS1 is a metastasis suppressor protein. Activation of the receptor inhibits cell proliferation and cell migration, key characteristics of tumor metastasis. The receptor is essential for normal gonadotropin-released hormone physiology and for puberty. The hypothalamic KiSS1/KISS1R system is a pivotal factor in central regulation of the gonadotropic axis at puberty and in adulthood. Analysis of the transduction pathways activated by the receptor identifies coupling to phospholipase C and intracellular calcium release through pertussis toxin-insensitive G(q) proteins. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Highest level in the heart and 15- and 17-day embryos. Low level in other tissues. Colocalized with gonadotropin-releasing hormone (GnRH) neurons in the hypothalamus. {ECO:0000269|PubMed:11414709, ECO:0000269|PubMed:12359743, ECO:0000269|PubMed:15665093}. +P04184 KITH_MOUSE Thymidine kinase, cytosolic (EC 2.7.1.21) 233 25,776 Active site (1); Binding site (2); Chain (1); Erroneous initiation (1); Initiator methionine (1); Metal binding (4); Modified residue (3); Natural variant (1); Nucleotide binding (3); Region (1); Sequence conflict (5) PTM: Phosphorylated on Ser-13 in mitosis. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Homotetramer. {ECO:0000250}. +Q8C078 KKCC2_MOUSE Calcium/calmodulin-dependent protein kinase kinase 2 (CaM-KK 2) (CaM-kinase kinase 2) (CaMKK 2) (EC 2.7.11.17) (Calcium/calmodulin-dependent protein kinase kinase beta) (CaM-KK beta) (CaM-kinase kinase beta) (CaMKK beta) 588 64,618 Active site (1); Alternative sequence (7); Binding site (1); Chain (1); Compositional bias (1); Domain (1); Initiator methionine (1); Modified residue (10); Nucleotide binding (1); Region (3); Sequence conflict (4) FUNCTION: Calcium/calmodulin-dependent protein kinase belonging to a proposed calcium-triggered signaling cascade involved in a number of cellular processes. Phosphorylates CAMK1, CAMK4 and CAMK1D (By similarity). Efficiently phosphorylates 5'-AMP-activated protein kinase (AMPK) trimer, including that consisting of PRKAA1, PRKAB1 and PRKAG1. This phosphorylation is stimulated in response to Ca(2+) signals (By similarity). May play a role in neurite growth. Isoform 2 may promote neurite elongation, while isoform 1 may promoter neurite branching (By similarity). May be involved in hippocampal activation of CREB1. {ECO:0000250, ECO:0000269|PubMed:14586002}. PTM: Autophosphorylated and phosphorylated by PKA. Each isoform may show a different pattern of phosphorylation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell projection {ECO:0000250}. Note=Predominantly nuclear in unstimulated cells. Found in the cytoplasm and neurites after forskolin induction. {ECO:0000250}. SUBUNIT: Interacts with calmodulin. {ECO:0000250}. DOMAIN: The autoinhibitory domain overlaps with the calmodulin binding region and may be involved in intrasteric autoinhibition.; DOMAIN: The RP domain (arginine/proline-rich) is involved in the recognition of CAMKI and CAMK4 as substrates. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in all tissues tested. A differential expression pattern compared to CAMKK1 is observed in the brain. {ECO:0000269|PubMed:12654522}. +P05532 KIT_MOUSE Mast/stem cell growth factor receptor Kit (SCFR) (EC 2.7.10.1) (Proto-oncogene c-Kit) (Tyrosine-protein kinase Kit) (CD antigen CD117) 979 109,343 Active site (1); Alternative sequence (3); Beta strand (25); Binding site (2); Chain (1); Disulfide bond (5); Domain (6); Glycosylation (8); Helix (2); Metal binding (3); Modified residue (16); Mutagenesis (5); Natural variant (5); Nucleotide binding (2); Region (1); Sequence conflict (4); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 528 548 Helical. {ECO:0000255}. TOPO_DOM 25 527 Extracellular. {ECO:0000255}.; TOPO_DOM 549 979 Cytoplasmic. {ECO:0000255}. FUNCTION: Tyrosine-protein kinase that acts as cell-surface receptor for the cytokine KITLG/SCF and plays an essential role in the regulation of cell survival and proliferation, hematopoiesis, stem cell maintenance, gametogenesis, mast cell development, migration and function, and in melanogenesis. In response to KITLG/SCF binding, KIT can activate several signaling pathways. Phosphorylates PIK3R1, PLCG1, SH2B2/APS and CBL. Activates the AKT1 signaling pathway by phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase. Activated KIT also transmits signals via GRB2 and activation of RAS, RAF1 and the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. Promotes activation of STAT family members STAT1, STAT3, STAT5A and STAT5B. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. KIT signaling is modulated by protein phosphatases, and by rapid internalization and degradation of the receptor. Activated KIT promotes phosphorylation of the protein phosphatases PTPN6/SHP-1 and PTPRU, and of the transcription factors STAT1, STAT3, STAT5A and STAT5B. Promotes phosphorylation of PIK3R1, CBL, CRK (isoform Crk-II), LYN, MAPK1/ERK2 and/or MAPK3/ERK1, PLCG1, SRC and SHC1. {ECO:0000269|PubMed:1698611, ECO:0000269|PubMed:1714377, ECO:0000269|PubMed:18725415, ECO:0000269|PubMed:21037083, ECO:0000269|PubMed:7509796, ECO:0000269|PubMed:9528781, ECO:0000269|PubMed:9722617}. PTM: Ubiquitinated by SOCS6. KIT is rapidly ubiquitinated after autophosphorylation induced by KITLG/SCF binding, leading to internalization and degradation (By similarity). {ECO:0000250}.; PTM: Autophosphorylated on tyrosine residues. KITLG/SCF binding promotes autophosphorylation of isoform 1 and isoform 2. Isoform 1 shows low levels of tyrosine phosphorylation in the absence of added KITLG/SCF, while isoform 2 requires stimulation by KITLG/SCF for phosphorylation (in vitro). Phosphorylation of Tyr-573 is required for interaction with PTPN6/SHP-1. Phosphorylation of Tyr-571 is required for interaction with PTPN11/SHP-2. Phosphorylated tyrosine residues are important for interaction with specific binding partners. {ECO:0000269|PubMed:1714377, ECO:0000269|PubMed:7527401}. SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Isoform 2: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Isoform 3: Cytoplasm. Note=Detected in the cytoplasm of spermatozoa, especially in the equatorial and subacrosomal region of the sperm head. {ECO:0000250}. SUBUNIT: Monomer in the absence of bound KITLG/SCF. Homodimer in the presence of bound KITLG/SCF, forming a heterotetramer with two KITLG/SCF molecules. Interacts (via phosphorylated tyrosine residues) with the adapter proteins GRB2 and GRB7 (via SH2 domain), and SH2B2/APS. Interacts (via C-terminus) with MPDZ (via the tenth PDZ domain). Interacts (via phosphorylated tyrosine residues) with the protein phosphatases PTPN6/SHP-1 (via SH2 domain), PTPN11/SHP-2 (via SH2 domain) and PTPRU. Interacts with DOK1 and TEC (By similarity). Interacts with the protein kinase FES/FPS. Interacts with PLCG1. Interacts (via phosphorylated tyrosine residues) with PIK3R1 and PIK3 catalytic subunit. Interacts (KITLG/SCF-bound) with IL1RL1. Interacts with IL1RAP (independent of stimulation with KITLG/SCF). A mast cell-specific KITLG/SCF-induced interleukin-33 signaling complex contains IL1RL1, IL1RAP, KIT and MYD88. {ECO:0000250|UniProtKB:P10721, ECO:0000269|PubMed:1698611, ECO:0000269|PubMed:1714377, ECO:0000269|PubMed:17255936, ECO:0000269|PubMed:17595334, ECO:0000269|PubMed:20200353, ECO:0000269|PubMed:7509796, ECO:0000269|PubMed:7527401, ECO:0000269|PubMed:9528781}. TISSUE SPECIFICITY: Isoform 1 and isoform 2 are detected in bone marrow cells, spermatogonia and spermatocytes, but not in round spermatids, elongating spermatids and spermatozoa. Isoform 3 is detected in round spermatids, elongating spermatids and spermatozoa, but not in spermatogonia and spermatocytes (at protein level). Isoform 1 is widely expressed and detected in fetal liver and bone marrow. Isoform 3 is detected in bone marrow cells enriched in hematopoietic stem cells. {ECO:0000269|PubMed:1378413, ECO:0000269|PubMed:18447649, ECO:0000269|PubMed:7527401}. DISEASE: Note=Defects in Kit are the cause of the white-spotting phenotype (W). White-spotting variants induces severe effects on pigmentation, gametogenesis and hematopoiesis. Mice homozygous for W42 die perinatally of macrocytic anemia. +O88447 KLC1_MOUSE Kinesin light chain 1 (KLC 1) 541 61,450 Beta strand (2); Chain (1); Coiled coil (1); Helix (13); Modified residue (5); Repeat (6); Turn (1) FUNCTION: Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. The light chain may function in coupling of cargo to the heavy chain or in the modulation of its ATPase activity. SUBCELLULAR LOCATION: Cell projection, growth cone {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000305}. SUBUNIT: Oligomeric complex composed of two heavy chains and two light chains. Interacts with SPAG9 (PubMed:15767678). Interacts with ATCAY; may link mitochondria to KLC1 and regulate mitochondria localization into neuron projections (PubMed:19861499). Interacts (via TPR repeats) with TOR1A; the interaction associates TOR1A with the kinesin oligomeric complex. Interacts with BORCS5 (By similarity). Interacts with MAPK8IP3/JIP3 and NTRK2/TRKB; interaction with NTRK2/TRKB is mediated by MAPK8IP3/JIP3 (By similarity). {ECO:0000250|UniProtKB:P37285, ECO:0000250|UniProtKB:Q07866, ECO:0000269|PubMed:15767678, ECO:0000269|PubMed:19861499}. +Q91XA8 KLD8A_MOUSE Kelch domain-containing protein 8A 350 38,817 Chain (1); Repeat (7) +O89091 KLF10_MOUSE Krueppel-like factor 10 (GDNF-inducible factor) (Transcription factor GIF) (mGIF) (Transforming growth factor-beta-inducible early growth response protein 1) (TGFB-inducible early growth response protein 1) (TIEG-1) 479 51,756 Chain (1); Modified residue (2); Zinc finger (3) FUNCTION: Transcriptional repressor which binds to the consensus sequence 5'-GGTGTG-3'. May play a role in the cell cycle regulation (By similarity). Plays a role in the regulation of the circadian clock; binds to the GC box sequence in the promoter of the core clock component ARTNL/BMAL1 and represses its transcriptional activity. Regulates the circadian expression of genes involved in lipogenesis, gluconeogenesis, and glycolysis in the liver. Represses the expression of PCK2, a rate-limiting step enzyme of gluconeogenesis. {ECO:0000250|UniProtKB:Q13118, ECO:0000269|PubMed:20070857, ECO:0000269|PubMed:20385766}. PTM: Ubiquitinated; mediated by SIAH1 and leading to its subsequent proteasomal degradation. {ECO:0000250|UniProtKB:Q13118}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20070857}. +Q80YG3 KLDC1_MOUSE Kelch domain-containing protein 1 406 46,830 Chain (1); Repeat (6) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +Q921I2 KLDC4_MOUSE Kelch domain-containing protein 4 584 64,860 Chain (1); Modified residue (1); Repeat (6); Sequence conflict (1) +Q3USL1 KLDC9_MOUSE Kelch domain-containing protein 9 350 38,185 Chain (1); Repeat (3) SUBUNIT: Interacts with CCNA1. {ECO:0000250}. +P58334 KLF16_MOUSE Krueppel-like factor 16 (Basic transcription element-binding protein 4) (BTE-binding protein 4) (Dopamine receptor-regulating factor) (Transcription factor BTEB4) 251 25,652 Chain (1); Compositional bias (3); Modified residue (2); Zinc finger (3) FUNCTION: Transcription factor that binds GC and GT boxes in the D1A, D2 and D3 dopamine receptor promoters and displaces Sp1 and Sp3 from these sequences. It modulates dopaminergic transmission in the brain by repressing or activating transcription from several different promoters depending on cellular context. SUBCELLULAR LOCATION: Nucleus. DOMAIN: The Ala/Pro-rich domain may contain discrete activation and repression subdomains and also can mediate protein-protein interactions. TISSUE SPECIFICITY: High expression in brain; olfactory tubercle, olfactory bulb, nucleus accumbens, striatum, hippocampal CA1 region, amygdala, dentate gyrus and frontal cortex. Moderate expression in hippocampal CA2-3 regions, piriform cortex, septum, and distinct thalamic nuclei. Low expression in the cerebellum. +Q8CFA7 KLF17_MOUSE Krueppel-like factor 17 (Germ cell-specific zinc finger protein) (Zinc finger protein 393) 341 38,076 Chain (1); Sequence conflict (2); Zinc finger (3) FUNCTION: Transcription repressor that binds to the promoter of target genes and prevents their expression. Acts as a negative regulator of epithelial-mesenchymal transition and metastasis in breast cancer. Specifically binds the 5'-CACCC-3' sequence in the promoter of ID1, a key metastasis regulator in breast cancer, and repress its expression. May be a germ cell-specific transcription factor that plays important roles in spermatid differentiation and oocyte development. {ECO:0000269|PubMed:19801974}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: Exclusively expressed in testis and ovary. Localized to step 3-8 spermatids in testis and growing oocytes in ovary. {ECO:0000269|PubMed:12351194}. +A2AAX3 KLH15_MOUSE Kelch-like protein 15 604 69,745 Alternative sequence (4); Chain (1); Domain (2); Repeat (5) Protein modification; protein ubiquitination. FUNCTION: Substrate-specific adapter for CUL3 E3 ubiquitin-protein ligase complex. Acts as an adapter for CUL3 to target the serine/threonine-protein phosphatase 2A (PP2A) subunit PPP2R5B for ubiquitination and subsequent proteasomal degradation, thus promoting exchange with other regulatory subunits and regulating PP2A holoenzyme composition. Acts as an adapter for CUL3 to target the DNA-end resection factor RBBP8/CtIP for ubiquitination and subsequent proteasomal degradation. Through the regulation of RBBP8/CtIP protein turnover, plays a key role in DNA damage response, favoring DNA double-strand repair through error-prone non-homologous end joining (NHEJ) over error-free, RBBP8-mediated homologous recombination (HR). {ECO:0000250|UniProtKB:Q96M94}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96M94}. SUBUNIT: Homodimer. Dimerization does not affect PPP2R5B-binding, but is required for its proteasomal degradation. Interacts with CUL3. Directly interacts with PPP2R5B; this interaction leads to PPP2R5B proteasomal degradation. Interacts with RBBP8/CtIP; this interaction leads to RBBP8 proteasomal degradation. {ECO:0000250|UniProtKB:Q96M94}. +Q60980 KLF3_MOUSE Krueppel-like factor 3 (Basic krueppel-like factor) (CACCC-box-binding protein BKLF) (TEF-2) 344 38,561 Beta strand (2); Chain (1); Compositional bias (1); Cross-link (5); Helix (2); Modified residue (8); Motif (1); Mutagenesis (5); Region (1); Turn (1); Zinc finger (3) FUNCTION: Binds to the CACCC box of erythroid cell-expressed genes. May play a role in hematopoiesis. {ECO:0000269|PubMed:15684403, ECO:0000269|PubMed:8657145}. PTM: Sumoylated with SUMO1. Sumoylation is enhanced by PIAS1, PIAS2alpha and PIAS2beta, and PIAS4, but not by Pc2. Enhances transcriptional repression, but has no effect on DNA binding. Sumoylation on Lys-197 is the major site. {ECO:0000269|PubMed:15684403}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Monomer. {ECO:0000269|PubMed:12736264}. TISSUE SPECIFICITY: In 8.5 day embryos, expressed in midbrain, anterior hindbrain and ventral forebrain. In 9 day embryos, expressed throughout ventral anterior half of embryo including midbrain-hindbrain junction, ventral midbrain, diencephalon and forebrain. At 10.5 days, distribution is more widespread with expression also found in developing limb buds. Widely expressed in the adult. {ECO:0000269|PubMed:8657145}. +Q3U410 KLH21_MOUSE Kelch-like protein 21 597 66,547 Chain (1); Domain (2); Erroneous initiation (1); Repeat (6); Sequence conflict (2) Protein modification; protein ubiquitination. FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex required for efficient chromosome alignment and cytokinesis. The BCR(KLHL21) E3 ubiquitin ligase complex regulates localization of the chromosomal passenger complex (CPC) from chromosomes to the spindle midzone in anaphase and mediates the ubiquitination of AURKB. Ubiquitination of AURKB by BCR(KLHL21) E3 ubiquitin ligase complex may not lead to its degradation by the proteasome (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Localizes to the spindle midzone and targets CUL3 to this region. {ECO:0000250}. SUBUNIT: Component of the BCR(KLHL21) E3 ubiquitin ligase complex, at least composed of CUL3, KLHL21 and RBX1. {ECO:0000250}. +Q9D783 KLH40_MOUSE Kelch-like protein 40 (Kelch repeat and BTB domain-containing protein 5) 621 69,589 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (2); Repeat (5); Sequence conflict (1) FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a key regulator of skeletal muscle development (PubMed:25940086). The BCR(KLHL40) complex acts by mediating ubiquitination and degradation of TFDP1, thereby regulating the activity of the E2F:DP transcription factor complex (PubMed:25940086). Promotes stabilization of LMOD3 by acting as a negative regulator of LMOD3 ubiquitination; the molecular process by which it negatively regulates ubiquitination of LMOD3 is however unclear (PubMed:24960163). {ECO:0000269|PubMed:24960163, ECO:0000269|PubMed:25940086}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25940086}. Cytoplasm, myofibril, sarcomere, A band {ECO:0000269|PubMed:24960163}. Cytoplasm, myofibril, sarcomere, I band {ECO:0000269|PubMed:24960163}. SUBUNIT: Component of the BCR(KLHL40) E3 ubiquitin ligase complex, at least composed of CUL3, KLHL40 and RBX1 (PubMed:24361185). Interacts with LMOD3 (PubMed:24960163). {ECO:0000269|PubMed:24361185, ECO:0000269|PubMed:24960163}. TISSUE SPECIFICITY: Specifically expressed in skeletal muscles in embryonic, neonatal and adults (PubMed:24960163, PubMed:25940086). Expressed in various types of muscles, including extensor digitorum longus, gastrocnemius, soleus, diaphragm, masseter and heart (at protein level). Not detected in brain, liver and lung (at protein level). {ECO:0000269|PubMed:23746549, ECO:0000269|PubMed:24960163, ECO:0000269|PubMed:25940086}. +Q8BRG6 KLH24_MOUSE Kelch-like protein 24 (Kainate receptor-interacting protein for GluR6) (KRIP6) 600 68,364 Chain (1); Domain (2); Erroneous initiation (3); Repeat (6); Sequence conflict (3) FUNCTION: Controls KRT14 levels during keratinocytes differentiation (PubMed:27798626). As part of the BCR(KLHL24) E3 ubiquitin ligase complex, mediates ubiquitination of KRT14 (By similarity). Specifically reduces kainate receptor-mediated currents in hippocampal neurons, most probably by modulating channel properties (By similarity). {ECO:0000250|UniProtKB:Q56A24, ECO:0000250|UniProtKB:Q6TFL4, ECO:0000269|PubMed:27798626}. PTM: Autoubiquitinated. Autoubiquitination leads to proteasomal degradation and is necessary to control KLHL24 levels. {ECO:0000250|UniProtKB:Q6TFL4}. SUBCELLULAR LOCATION: Perikaryon {ECO:0000250|UniProtKB:Q6TFL4}. Cell projection, axon {ECO:0000250|UniProtKB:Q56A24}. Cytoplasm {ECO:0000250|UniProtKB:Q56A24, ECO:0000250|UniProtKB:Q6TFL4}. Cell junction, desmosome {ECO:0000250|UniProtKB:Q6TFL4}. Cell junction, adherens junction {ECO:0000250|UniProtKB:Q6TFL4}. SUBUNIT: Forms homodimers. Interacts with GRIK2 (By similarity). Component of the BCR(KLHL24) E3 ubiquitin ligase complex, composed of CUL3, RBX1 and KLHL24. Interacts with CUL3. Interacts with KRT14 (By similarity). {ECO:0000250|UniProtKB:Q56A24, ECO:0000250|UniProtKB:Q6TFL4}. TISSUE SPECIFICITY: Expressed in the brain. {ECO:0000269|PubMed:27798626}. +A2AUC9 KLH41_MOUSE Kelch-like protein 41 (Kelch repeat and BTB domain-containing protein 10) 606 68,190 Chain (1); Domain (2); Modified residue (1); Repeat (5); Sequence conflict (1) FUNCTION: Involved in skeletal muscle development and differentiation. Regulates proliferation and differentiation of myoblasts and plays a role in myofibril assembly by promoting lateral fusion of adjacent thin fibrils into mature, wide myofibrils. Required for pseudopod elongation in transformed cells. {ECO:0000269|PubMed:18178185, ECO:0000269|PubMed:21368295, ECO:0000269|PubMed:22562206}. PTM: Ubiquitinated by E3 ubiquitin ligase complex formed by CUL3 and RBX1 and probably targeted for proteasome-independent degradation. Quinone-induced oxidative stress increases its ubiquitination. {ECO:0000250|UniProtKB:O60662}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18178185, ECO:0000269|PubMed:22562206}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:18178185}. Cell projection, pseudopodium {ECO:0000250|UniProtKB:Q9ER30}. Cell projection, ruffle {ECO:0000250|UniProtKB:Q9ER30}. Cytoplasm, myofibril, sarcomere, M line {ECO:0000269|PubMed:22562206}. Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:24268659}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:24268659}. Note=Predominantly cytoplasmic but can colocalize with F-actin at the membrane ruffle-like structures at the tips of transformation-specific pseudopodia. SUBUNIT: Interacts with NRAP. Part of a complex that contains CUL3, RBX1 and KLHL41. Interacts with LASP1. {ECO:0000250|UniProtKB:O60662, ECO:0000250|UniProtKB:Q9ER30}. TISSUE SPECIFICITY: Skeletal muscle. Localized between laterally fusing myofibrils in skeletal muscle (at protein level). Expressed at a lower level in the heart compared to skeletal muscle. {ECO:0000269|PubMed:18178185, ECO:0000269|PubMed:22562206}. +Q99JB0 KLF7_MOUSE Krueppel-like factor 7 301 33,337 Chain (1); Motif (1); Sequence conflict (1); Zinc finger (3) FUNCTION: Transcriptional activator. Binds specifically to an Ikaros core binding element that is crucial for in vivo NTRK1/TrkA enhancer function. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. DOMAIN: The acidic N-terminal part may favor interaction with the basic domain of transcription factors. TISSUE SPECIFICITY: Expressed primarily in the nervous system. +O35739 KLF9_MOUSE Krueppel-like factor 9 (Basic transcription element-binding protein 1) (BTE-binding protein 1) (GC-box-binding protein 1) (Transcription factor BTEB1) 244 27,170 Chain (1); Compositional bias (1); Modified residue (1); Zinc finger (3) FUNCTION: Transcription factor that binds to GC box promoter elements. Selectively activates mRNA synthesis from genes containing tandem repeats of GC boxes but represses genes with a single GC box. Acts as an epidermal circadian transcription factor regulating keratinocyte proliferation. {ECO:0000250|UniProtKB:Q13886}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13886}. +Q8BUL5 KLHL7_MOUSE Kelch-like protein 7 586 65,938 Chain (1); Domain (2); Repeat (6); Sequence conflict (1) Protein modification; protein ubiquitination. FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex. The BCR(KLHL7) complex acts by mediating ubiquitination and subsequent degradation of substrate proteins. Probably mediates 'Lys-48'-linked ubiquitination (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8IXQ5}. Cytoplasm {ECO:0000250|UniProtKB:Q8IXQ5}. Note=Colocalizes with CUL3 in punctate structures at the perinuclear region of the cytoplasm. {ECO:0000250|UniProtKB:Q8IXQ5}. SUBUNIT: Homodimer. Component of the BCR(KLHL7) E3 ubiquitin ligase complex, at least composed of CUL3 and KLHL7 and RBX1 (By similarity). {ECO:0000250}. +P59280 KLHL8_MOUSE Kelch-like protein 8 629 69,788 Chain (1); Domain (2); Initiator methionine (1); Modified residue (1); Repeat (6); Sequence conflict (1) Protein modification; protein ubiquitination. FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex required for The BCR(KLHL8) ubiquitin ligase complex mediates ubiquitination and degradation of RAPSN. {ECO:0000250}. SUBUNIT: Component of the BCR(KLHL8) E3 ubiquitin ligase complex, at least composed of CUL3, KLHL8 and RBX1. Interacts with RAPSN (By similarity). {ECO:0000250}. +Q60660 KLRA2_MOUSE Killer cell lectin-like receptor 2 (Lymphocyte antigen 49b) (Ly-49b) (T-cell surface glycoprotein Ly-49B) 288 33,607 Chain (1); Disulfide bond (4); Domain (1); Glycosylation (4); Topological domain (2); Transmembrane (1) TRANSMEM 46 66 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 45 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 67 288 Extracellular. {ECO:0000255}. FUNCTION: Receptor on natural killer (NK) cells for class I MHC. SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. SUBUNIT: Homodimer; disulfide-linked. +Q64329 KLRA3_MOUSE Killer cell lectin-like receptor 3 (5E6) (Lymphocyte antigen 49c) (Ly-49c) (Nk2.1) (T-cell surface glycoprotein Ly-49C) 266 31,311 Beta strand (8); Chain (1); Disulfide bond (4); Domain (1); Glycosylation (5); Helix (3); Mutagenesis (19); Natural variant (27); Region (6); Sequence conflict (5); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 49 69 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 48 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 70 266 Extracellular. {ECO:0000255}. FUNCTION: Receptor on natural killer (NK) cells for class I MHC. {ECO:0000269|PubMed:8976165}. SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:14595439, ECO:0000269|PubMed:18426793}. +Q60652 KLRA5_MOUSE Killer cell lectin-like receptor 5 (Lymphocyte antigen 49e) (Ly-49e) (T-cell surface glycoprotein Ly-49E) 266 30,843 Chain (1); Disulfide bond (4); Domain (1); Glycosylation (3); Topological domain (2); Transmembrane (1) TRANSMEM 45 66 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 44 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 67 266 Extracellular. {ECO:0000255}. FUNCTION: Receptor on natural killer (NK) cells for class I MHC. SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:11254682}. TISSUE SPECIFICITY: Mostly expressed in NK cells, but also observed on NK T and memory T-cells. {ECO:0000269|PubMed:11254682}. +Q60653 KLRA6_MOUSE Killer cell lectin-like receptor 6 (Lymphocyte antigen 49f) (Ly-49f) (T-cell surface glycoprotein Ly-49F) 266 31,269 Chain (1); Disulfide bond (4); Domain (1); Glycosylation (2); Topological domain (2); Transmembrane (1) TRANSMEM 45 66 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 44 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 67 266 Extracellular. {ECO:0000255}. FUNCTION: Receptor on natural killer (NK) cells for class I MHC. SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. SUBUNIT: Homodimer; disulfide-linked. +Q60654 KLRA7_MOUSE Killer cell lectin-like receptor 7 (Lymphocyte antigen 49g) (Ly-49g) (T-cell surface glycoprotein Ly-49G) 280 32,522 Alternative sequence (2); Beta strand (6); Chain (1); Disulfide bond (4); Domain (1); Glycosylation (2); Helix (2); Sequence conflict (1); Topological domain (2); Transmembrane (1); Turn (3) TRANSMEM 45 66 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 44 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 67 280 Extracellular. {ECO:0000255}. FUNCTION: Receptor on natural killer (NK) cells for class I MHC. SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:18426793}. +Q0ZUP1 KLRB1_MOUSE Killer cell lectin-like receptor subfamily B member 1 (Killer cell lectin-like receptor subfamily B member 1G) (Natural killer cell surface protein NKR-P1G) (Natural killer lectin-like receptor 1E) 214 23,909 Chain (1); Disulfide bond (2); Domain (1); Topological domain (2); Transmembrane (1) TRANSMEM 43 63 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 42 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 64 214 Extracellular. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000255}. +P27811 KLRBA_MOUSE Killer cell lectin-like receptor subfamily B member 1A (NKR-P1A) (CD161 antigen-like family member A) (Lymphocyte antigen 55A) (Ly-55A) (NKR-P1.7) (Natural killer cell surface protein P1-2) (NKR-P1 2) (CD antigen CD161a) 227 25,782 Beta strand (8); Chain (1); Disulfide bond (3); Domain (1); Helix (3); Motif (1); Sequence conflict (16); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 46 66 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 45 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 67 227 Extracellular. {ECO:0000255}. FUNCTION: Plays a stimulatory role on natural killer (NK) cell cytotoxicity. {ECO:0000269|PubMed:16751398}. SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. SUBUNIT: Homodimer; disulfide-linked. Interacts with tyrosine kinase LCK (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in natural killer cells. +Q61955 KLK8_MOUSE Kallikrein-8 (mK8) (EC 3.4.21.118) (Neuropsin) (NP) (Serine protease 19) 260 28,524 Active site (3); Beta strand (16); Chain (1); Disulfide bond (6); Domain (1); Glycosylation (1); Helix (3); Mass spectrometry (2); Propeptide (1); Signal peptide (1); Turn (1) FUNCTION: Serine protease which is capable of degrading a number of proteins such as casein, fibrinogen, kininogen, fibronectin and collagen type IV. Also cleaves L1CAM in response to increased neural activity. Induces neurite outgrowth and fasciculation of cultured hippocampal neurons. Plays a role in the formation and maturation of orphan and small synaptic boutons in the Schaffer-collateral pathway, regulates Schaffer-collateral long-term potentiation in the hippocampus and is required for memory acquisition and synaptic plasticity. Involved in skin desquamation and keratinocyte proliferation. Plays a role in the secondary phase of pathogenesis following spinal cord injury. {ECO:0000269|PubMed:10762375, ECO:0000269|PubMed:11880192, ECO:0000269|PubMed:12944500, ECO:0000269|PubMed:16308352, ECO:0000269|PubMed:16537644, ECO:0000269|PubMed:17182622, ECO:0000269|PubMed:17629414, ECO:0000269|PubMed:9556608}. SUBCELLULAR LOCATION: Secreted. Cytoplasm. Note=Shows a cytoplasmic distribution in the keratinocytes. SUBUNIT: Interacts with SPINK9. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the limbic system of mouse brain and is localized at highest concentration in pyramidal neurons of the hippocampal CA1-3 subfields. Also detected in spinal cord gray matter and in keratinized stratified epithelia of epidermis, hair, tongue, palate, nasal cavity, pharynges, esophagus and forestomach. In skin and mucus membranes, expressed in stratum spinosum and stratum granulosum. Expressed during estrus in vaginal epithelial cells but not stromal cells. Within the vaginal epithelium, expressed in prickle cells, granular cells and parakeratotic cells but not in basal cells. Not expressed in uterus. Expressed in the keratinocytes. {ECO:0000269|PubMed:12354676, ECO:0000269|PubMed:17629414, ECO:0000269|PubMed:17761692, ECO:0000269|PubMed:7623137, ECO:0000269|PubMed:8602273, ECO:0000269|PubMed:9620300, ECO:0000269|PubMed:9749739}. +Q8CJC7 KLRE1_MOUSE Killer cell lectin-like receptor subfamily E member 1 226 26,265 Chain (1); Disulfide bond (3); Domain (1); Glycosylation (1); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 69 89 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 68 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 90 226 Extracellular. {ECO:0000305}. FUNCTION: Lectin-like receptor for natural killer (NK) cells (PubMed:14707119, PubMed:15069013, PubMed:18713988). Can either inhibit or activate NK cell cytotoxic activity, depending on its binding partner (PubMed:14707119, PubMed:15069013, PubMed:18713988). Heterodimer formation with KLRI1 mediates NK cell inhibition whereas heterodimer formation with KLRI2 mediates NK cell activation (PubMed:18713988). Plays a role in allogeneic recognition by the immune system (PubMed:14707119, PubMed:15069013). {ECO:0000269|PubMed:14707119, ECO:0000269|PubMed:15069013, ECO:0000269|PubMed:18713988}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12782717, ECO:0000269|PubMed:14707119, ECO:0000269|PubMed:15069013, ECO:0000269|PubMed:18713988}; Single-pass type II membrane protein {ECO:0000255}. SUBUNIT: Heterodimer; with KLRI1 or KLRI2. {ECO:0000269|PubMed:14707119, ECO:0000269|PubMed:18713988}. TISSUE SPECIFICITY: Expressed in natural killer (NK) cells (at protein level) (PubMed:12782717, PubMed:14707119, PubMed:12715246). Also detected in natural killer T (NKT) cells (at protein level) (PubMed:14707119, PubMed:12715246). Has little or no expression in T cells (at protein level) (PubMed:14707119, PubMed:12715246). {ECO:0000269|PubMed:12715246, ECO:0000269|PubMed:12782717, ECO:0000269|PubMed:14707119}. +Q5DT36 KLRI2_MOUSE Killer cell lectin-like receptor subfamily I member 2 248 28,848 Chain (1); Disulfide bond (3); Domain (1); Glycosylation (3); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 80 100 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 79 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 101 248 Extracellular. {ECO:0000305}. FUNCTION: Lectin-like receptor for natural killer (NK) cells. Heterodimer formation with KLRE1 mediates NK cell cytolytic activity. {ECO:0000250|UniProtKB:Q5DT37}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q5DT37}; Single-pass type II membrane protein {ECO:0000255}. SUBUNIT: Heterodimer with KLRE1. {ECO:0000250|UniProtKB:Q5DT37}. TISSUE SPECIFICITY: Expressed in natural killer (NK) cells. {ECO:0000269|PubMed:15650876}. +P55200 KMT2A_MOUSE Histone-lysine N-methyltransferase 2A (Lysine N-methyltransferase 2A) (EC 2.1.1.43) (ALL-1) (Myeloid/lymphoid or mixed-lineage leukemia) (Myeloid/lymphoid or mixed-lineage leukemia protein 1) (Zinc finger protein HRX) [Cleaved into: MLL cleavage product N320 (N-terminal cleavage product of 320 kDa) (p320); MLL cleavage product C180 (C-terminal cleavage product of 180 kDa) (p180)] 3966 429,649 Alternative sequence (1); Binding site (4); Chain (3); Compositional bias (13); Cross-link (1); DNA binding (3); Domain (5); Erroneous initiation (1); Metal binding (4); Modified residue (29); Motif (1); Natural variant (1); Region (3); Sequence conflict (19); Site (3); Zinc finger (6) FUNCTION: Histone methyltransferase that plays an essential role in early development and hematopoiesis. Catalytic subunit of the MLL1/MLL complex, a multiprotein complex that mediates both methylation of 'Lys-4' of histone H3 (H3K4me) complex and acetylation of 'Lys-16' of histone H4 (H4K16ac). In the MLL1/MLL complex, it specifically mediates H3K4me, a specific tag for epigenetic transcriptional activation. Has weak methyltransferase activity by itself, and requires other component of the MLL1/MLL complex to obtain full methyltransferase activity. Has no activity toward histone H3 phosphorylated on 'Thr-3', less activity toward H3 dimethylated on 'Arg-8' or 'Lys-9', while it has higher activity toward H3 acetylated on 'Lys-9'. Binds to unmethylated CpG elements in the promoter of target genes and helps maintain them in the nonmethylated state. Required for transcriptional activation of HOXA9 (By similarity). Promotes PPP1R15A-induced apoptosis. Plays a critical role in the control of circadian gene expression and is essential for the transcriptional activation mediated by the CLOCK-ARNTL/BMAL1 heterodimer. Establishes a permissive chromatin state for circadian transcription by mediating a rhythmic methylation of 'Lys-4' of histone H3 (H3K4me) and this histone modification directs the circadian acetylation at H3K9 and H3K14 allowing the recruitment of CLOCK-ARNTL/BMAL1 to chromatin (PubMed:21113167). {ECO:0000250|UniProtKB:Q03164, ECO:0000269|PubMed:21113167}. PTM: Proteolytic cleavage by TASP1 generates MLL cleavage product N320 and MLL cleavage product C180, which reassemble through a non-covalent association. 2 cleavage sites exist, cleavage site 1 (CS1) and cleavage site 2 (CS2), to generate MLL cleavage products N320 and C180. CS2 is the major site. {ECO:0000250|UniProtKB:Q03164}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q03164}.; SUBCELLULAR LOCATION: MLL cleavage product N320: Nucleus {ECO:0000250|UniProtKB:Q03164}.; SUBCELLULAR LOCATION: MLL cleavage product C180: Nucleus {ECO:0000250|UniProtKB:Q03164}. Note=Localizes to a diffuse nuclear pattern when not associated with MLL cleavage product N320. {ECO:0000250|UniProtKB:Q03164}. SUBUNIT: MLL cleavage product N320 heterodimerizes with MLL cleavage product C180 (via SET and FYRC domains). Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, HCFC2, WDR5, DPY30 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MEN1, MGA, KAT8/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Interacts with WDR5; the interaction is direct (PubMed:21335234). Interaction with WDR5 is required for stable interaction with ASH2L and RBBP5, and thereby also for optimal histone methyltransferase activity. Interacts with KAT8/MOF; the interaction is direct. Interacts with SBF1 and PPP1R15A. Interacts with ZNF335 (By similarity). Interacts with CLOCK and ARNTL/BMAL1 in a circadian manner (PubMed:21113167). Interacts with PPIE; this results in decreased histone H3 methyltransferase activity. Interacts with CREBBP (By similarity). {ECO:0000250|UniProtKB:Q03164, ECO:0000269|PubMed:21113167, ECO:0000269|PubMed:21335234}. DOMAIN: The 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors. {ECO:0000250|UniProtKB:Q03164}.; DOMAIN: The SET domain structure is atypical and is not in an optimal position to have methyltransferase activity. It requires other components of the MLL1/MLL complex, such as ASH2L or RBBP5, to order the active site and obtain optimal histone methyltransferase activity. {ECO:0000250|UniProtKB:Q03164}.; DOMAIN: The CXXC-type zinc finger binds to DNA sequence elements containing nonmethylated CpG dinucleotides. {ECO:0000250|UniProtKB:Q03164}.; DOMAIN: The third PHD-type zinc-finger binds both trimethylated histone H3K4me3 and PPIE; histone and PPIE bind to distinct surfaces. Nevertheless, PPIE binding and histone binding are mutually inhibitory. Isomerization of a peptidylproline bond in the linker between the third PHD-type zinc-finger and the bromo domain disrupts the interaction between the bromo domain and the third PHD-type zinc-finger, and thereby facilitates interaction with PPIE. {ECO:0000250|UniProtKB:Q03164}. +O08550 KMT2B_MOUSE Histone-lysine N-methyltransferase 2B (Lysine N-methyltransferase 2B) (EC 2.1.1.43) (Myeloid/lymphoid or mixed-lineage leukemia protein 4 homolog) (Trithorax homolog 2) (WW domain-binding protein 7) (WBP-7) 2713 294,821 Binding site (4); Chain (1); Compositional bias (5); Cross-link (2); DNA binding (3); Domain (4); Initiator methionine (1); Metal binding (4); Modified residue (18); Region (1); Sequence caution (1); Sequence conflict (2); Zinc finger (6) FUNCTION: Histone methyltransferase. Methylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Plays a central role in beta-globin locus transcription regulation by being recruited by NFE2 (By similarity). Plays an important role in controlling bulk H3K4me during oocyte growth and preimplantation development. Required during the transcriptionally active period of oocyte growth for the establishment and/or maintenance of bulk H3K4 trimethylation (H3K4me3), global transcriptional silencing that preceeds resumption of meiosis, oocyte survival and normal zygotic genome activation. {ECO:0000250, ECO:0000269|PubMed:20808952}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the menin-associated histone methyltransferase complex, at least composed of KMT2B/MLL4, ASH2L, RBBP5, WDR5, DPY30, MEN1; the complex interacts with POLR2A and POLR2B via MEN1. Interacts with NFE2. Interacts with KDM6B. {ECO:0000250}. +Q3UG20 KMT2E_MOUSE Inactive histone-lysine N-methyltransferase 2E (Inactive lysine N-methyltransferase 2E) (Myeloid/lymphoid or mixed-lineage leukemia protein 5 homolog) 1868 204,543 Alternative sequence (1); Chain (1); Coiled coil (1); Compositional bias (1); Domain (1); Erroneous initiation (2); Frameshift (1); Glycosylation (2); Metal binding (8); Modified residue (5); Motif (1); Sequence caution (4); Sequence conflict (8); Zinc finger (1) FUNCTION: Associates with chromatin regions downstream of transcriptional start sites of active genes and thus regulates gene transcription (By similarity). Chromatin interaction is mediated via the binding to tri-methylated histone H3 at 'Lys-4' (H3K4me3) (By similarity). Key regulator of hematopoiesis involved in terminal myeloid differentiation and in the regulation of hematopoietic stem cell (HSCs) self-renewal by a mechanism that involves DNA methylation (PubMed:18854576, PubMed:18952892, PubMed:18818388). Also acts as an important cell cycle regulator, participating in cell cycle regulatory network machinery at multiple cell cycle stages including G1/S transition, S phase progression and mitotic entry (PubMed:19264965). Recruited to E2F1 responsive promoters by HCFC1 where it stimulates tri-methylation of histone H3 at 'Lys-4' and transcriptional activation and thereby facilitates G1 to S phase transition (By similarity). During myoblast differentiation, required to suppress inappropriate expression of S-phase-promoting genes and maintain expression of determination genes in quiescent cells (PubMed:19264965). {ECO:0000250|UniProtKB:Q8IZD2, ECO:0000269|PubMed:18818388, ECO:0000269|PubMed:18854576, ECO:0000269|PubMed:18952892, ECO:0000269|PubMed:19264965}. PTM: Ubiquitinated. Deubiquitinated by USP7. {ECO:0000250|UniProtKB:Q8IZD2}.; PTM: O-glycosylated at Ser-435 and Thr-440 in the SET domain by OGT which probably prevents KMT2E proteosomal-mediated degradation. {ECO:0000250|UniProtKB:Q8IZD2}. SUBCELLULAR LOCATION: Chromosome {ECO:0000250|UniProtKB:Q8IZD2}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q8IZD2}. Nucleus speckle {ECO:0000250|UniProtKB:Q8IZD2}. Note=Absent from the nucleolus. Localizes to chromosome during interphase and to centrosomes during mitosis. Dissociation from mitotic chromosome is likely due to histone H3 phosphorylation on 'Thr-3' and 'Thr-6'. {ECO:0000250|UniProtKB:Q8IZD2}. SUBUNIT: Component of a complex composed of KMT2E, OGT and USP7; the complex stabilizes KMT2E, preventing KMT2E ubiquitination and proteosomal-mediated degradation. Interacts (via N-terminus) with OGT (via TRP repeats). Interacts with deubiquitinating enzyme USP7 (via MATH domain). Interacts (via HBM motif) with HCFC1 (via Kelch domain). Interacts with E2F1; the interaction is probably indirect and is mediated via HCFC1. {ECO:0000250|UniProtKB:Q8IZD2}. DOMAIN: The PHD-type domain binds specifically histone H3 tri-methylated at 'Lys-4' (H3K4me3), thus promoting binding to chromatin. {ECO:0000250|UniProtKB:Q8IZD2}.; DOMAIN: The SET domain does not bind the methyl group donor S-adenosyl-L-methionine and histone 3 H3K4 peptide as a large loop prevents the docking of the 'Lys-4' side chain. {ECO:0000250|UniProtKB:Q8IZD2}.; DOMAIN: The C-terminus domain is responsible for the localization to the centrosome during mitosis. {ECO:0000250|UniProtKB:Q8IZD2}. +Q2YDW7 KMT5A_MOUSE N-lysine methyltransferase KMT5A (EC 2.1.1.-) (H4-K20-HMTase KMT5A) (Histone-lysine N-methyltransferase KMT5A) (EC 2.1.1.43) (Lysine-specific methylase 5A) (PR/SET domain-containing protein 07) (PR-Set7) (PR/SET07) (SET domain-containing protein 8) 349 38,845 Binding site (1); Chain (1); Compositional bias (1); Domain (1); Frameshift (1); Modified residue (3); Region (2); Sequence conflict (2) FUNCTION: Protein-lysine N-methyltransferase that monomethylates both histones and non-histone proteins. Specifically monomethylates 'Lys-20' of histone H4 (H4K20me1). H4K20me1 is enriched during mitosis and represents a specific tag for epigenetic transcriptional repression. Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. Required for cell proliferation, probably by contributing to the maintenance of proper higher-order structure of DNA during mitosis. Involved in chromosome condensation and proper cytokinesis. Nucleosomes are preferred as substrate compared to free histones. Mediates monomethylation of p53/TP53 at 'Lys-382', leading to repress p53/TP53-target genes. Plays a negative role in TGF-beta response regulation and a positive role in cell migration (By similarity). {ECO:0000250}. PTM: Acetylated at Lys-129; does not change methyltransferase activity. Deacetylated at Lys-129 by SIRT2; does not change methyltransferase activity (By similarity). {ECO:0000250}.; PTM: Ubiquitinated and degraded by the DCX(DTL) complex. {ECO:0000305}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000269|PubMed:23468428}. Note=Specifically localizes to mitotic chromosomes. Associates with silent chromatin on euchromatic arms. Not associated with constitutive heterochromatin (By similarity). Colocalized with SIRT2 at mitotic foci. Associates with chromosomes during mitosis; association is increased in a H(2)O(2)-induced oxidative stress-dependent manner. {ECO:0000250}. SUBUNIT: Interacts with L3MBTL1. Interacts with SIRT2 (phosphorylated form); the interaction is direct, stimulates KMT5A-mediated methyltransferase activity at histone H4 'Lys-20' (H4K20me1) and is increased in a H(2)O(2)-induced oxidative stress-dependent manner (By similarity). {ECO:0000250}. DOMAIN: Although the SET domain contains the active site of enzymatic activity, both sequences upstream and downstream of the SET domain are required for methyltransferase activity. {ECO:0000250}. +Q3U8K7 KMT5B_MOUSE Histone-lysine N-methyltransferase KMT5B (EC 2.1.1.43) (Lysine-specific methyltransferase 5B) (Suppressor of variegation 4-20 homolog 1) (Su(var)4-20 homolog 1) (Suv4-20h1) 883 98,580 Alternative sequence (5); Beta strand (6); Chain (1); Cross-link (1); Domain (1); Erroneous initiation (3); Erroneous termination (1); Helix (12); Sequence conflict (11); Turn (3) FUNCTION: Histone methyltransferase that specifically trimethylates 'Lys-20' of histone H4. H4 'Lys-20' trimethylation represents a specific tag for epigenetic transcriptional repression. Mainly functions in pericentric heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin in these regions. KMT5B is targeted to histone H3 via its interaction with RB1 family proteins (RB1, RBL1 and RBL2). Plays a role in myogenesis by regulating the expression of target genes, such as EID3. {ECO:0000269|PubMed:15145825, ECO:0000269|PubMed:23720823}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15145825}. Chromosome {ECO:0000269|PubMed:15145825}. Note=Associated with pericentric heterochromatin. CBX1 and CBX5 are required for the localization to pericentric heterochromatin. SUBUNIT: Interacts with HP1 proteins CBX1, CBX3 and CBX5. Interacts with RB1 family proteins RB1, RBL1 and RBL2. Interacts (via C-terminus) with FRG1. {ECO:0000269|PubMed:15145825, ECO:0000269|PubMed:15750587, ECO:0000269|PubMed:16612004, ECO:0000269|PubMed:23720823}. +Q307W7 KNCN_MOUSE Kinocilin 124 12,809 Chain (1); Transmembrane (2) TRANSMEM 13 33 Helical. {ECO:0000255}.; TRANSMEM 40 60 Helical. {ECO:0000255}. FUNCTION: May play a role in stabilizing dense microtubular networks or in vesicular trafficking. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Preferentially expressed in the inner ear and testis. Localizes mainly in the kinocilium of sensory cells in the inner ear. Also present in the manchette of the spermatids, a transient structure enriched in interconnected microtubules (at protein level). +Q0KK55 KNDC1_MOUSE Kinase non-catalytic C-lobe domain-containing protein 1 (KIND domain-containing protein 1) (Protein very KIND) (v-KIND) (Ras-GEF domain-containing family member 2) 1742 191,313 Alternative sequence (3); Chain (1); Coiled coil (1); Domain (4); Frameshift (1); Modified residue (2); Mutagenesis (5); Sequence conflict (17) FUNCTION: RAS-Guanine nucleotide exchange factor (GEF) that controls the negative regulation of neuronal dendrite growth by mediating a signaling pathway linking RAS and MAP2 (PubMed:17984326, PubMed:21385318). May be involved in cellular senescence (By similarity). {ECO:0000250|UniProtKB:Q76NI1, ECO:0000269|PubMed:17984326, ECO:0000269|PubMed:21385318}. SUBCELLULAR LOCATION: Cell projection, dendrite {ECO:0000269|PubMed:17984326}. Perikaryon {ECO:0000269|PubMed:17984326}. SUBUNIT: Interacts (via KIND2) with MAP2; the interaction enhances MAP2 phosphorylation and localizes KNDC1 to dendrites. {ECO:0000269|PubMed:17984326}. TISSUE SPECIFICITY: Highly expressed in the brain and at low levels in the ovary. In the brain it is most prominently expressed in the cerebellum where it is restricted to the granular Purkinje cell layer. {ECO:0000269|PubMed:16099729, ECO:0000269|PubMed:17984326}. +Q8C3Y4 KNTC1_MOUSE Kinetochore-associated protein 1 2207 250,358 Chain (1); Erroneous initiation (1); Sequence conflict (1) FUNCTION: Essential component of the mitotic checkpoint, which prevents cells from prematurely exiting mitosis. Required for the assembly of the dynein-dynactin and MAD1-MAD2 complexes onto kinetochores. Its function related to the spindle assembly machinery is proposed to depend on its association in the mitotic RZZ complex (By similarity). {ECO:0000250|UniProtKB:P50748}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P50748}. Nucleus {ECO:0000250|UniProtKB:P50748}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:P50748}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P50748}. SUBUNIT: Interacts with ZW10. This interaction is required for stable association with the kinetochore. Component of the RZZ complex composed of KNTC1/ROD, ZW10 and ZWILCH (By similarity). {ECO:0000250|UniProtKB:P50748}. +P23298 KPCL_MOUSE Protein kinase C eta type (EC 2.7.11.13) (PKC-L) (nPKC-eta) 683 77,919 Active site (1); Binding site (1); Chain (1); Domain (3); Modified residue (6); Nucleotide binding (1); Sequence conflict (1); Zinc finger (2) FUNCTION: Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that is involved in the regulation of cell differentiation in keratinocytes and pre-B cell receptor, mediates regulation of epithelial tight junction integrity and foam cell formation, and is required for glioblastoma proliferation and apoptosis prevention in MCF-7 cells. In keratinocytes, binds and activates the tyrosine kinase FYN, which in turn blocks epidermal growth factor receptor (EGFR) signaling and leads to keratinocyte growth arrest and differentiation. Associates with the cyclin CCNE1-CDK2-CDKN1B complex and inhibits CDK2 kinase activity, leading to RB1 dephosphorylation and thereby G1 arrest in keratinocytes. In association with RALA activates actin depolymerization, which is necessary for keratinocyte differentiation. In the pre-B cell receptor signaling, functions downstream of BLNK by up-regulating IRF4, which in turn activates L chain gene rearrangement. Regulates epithelial tight junctions (TJs) by phosphorylating occludin (OCLN) on threonine residues, which is necessary for the assembly and maintenance of TJs. In association with PLD2 and via TLR4 signaling, is involved in lipopolysaccharide (LPS)-induced RGS2 down-regulation and foam cell formation. Upon PMA stimulation, mediates glioblastoma cell proliferation by activating the mTOR pathway, the PI3K/AKT pathway and the ERK1-dependent phosphorylation of ELK1. Involved in the protection of glioblastoma cells from irradiation-induced apoptosis by preventing caspase-9 activation. In camptothecin-treated MCF-7 cells, regulates NF-kappa-B upstream signaling by activating IKBKB, and confers protection against DNA damage-induced apoptosis. Promotes oncogenic functions of ATF2 in the nucleus while blocking its apoptotic function at mitochondria. Phosphorylates ATF2 which promotes its nuclear retention and transcriptional activity and negatively regulates its mitochondrial localization. {ECO:0000269|PubMed:11106751, ECO:0000269|PubMed:18780722, ECO:0000269|PubMed:21346190}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11106751, ECO:0000269|PubMed:21346190}. Note=Associates with cell membrane during keratinocytes differentiation. SUBUNIT: Interacts with DGKQ (By similarity). Interacts with FYN and RALA. {ECO:0000250, ECO:0000269|PubMed:11106751, ECO:0000269|PubMed:21346190}. DOMAIN: The C1 domain, containing the phorbol ester/DAG-type region 1 (C1A) and 2 (C1B), is the diacylglycerol sensor and the C2 domain is a non-calcium binding domain. TISSUE SPECIFICITY: Predominantly expressed in lung and skin. +Q02111 KPCT_MOUSE Protein kinase C theta type (EC 2.7.11.13) (nPKC-theta) 707 81,573 Active site (1); Beta strand (3); Binding site (1); Chain (1); Domain (3); Helix (1); Modified residue (7); Nucleotide binding (1); Turn (2); Zinc finger (2) FUNCTION: Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that mediates non-redundant functions in T-cell receptor (TCR) signaling, including T-cells activation, proliferation, differentiation and survival, by mediating activation of multiple transcription factors such as NF-kappa-B, JUN, NFATC1 and NFATC2. In TCR-CD3/CD28-co-stimulated T-cells, is required for the activation of NF-kappa-B and JUN, which in turn are essential for IL2 production, and participates in the calcium-dependent NFATC1 and NFATC2 transactivation. Mediates the activation of the canonical NF-kappa-B pathway (NFKB1) by direct phosphorylation of CARD11 on several serine residues, inducing CARD11 association with lipid rafts and recruitment of the BCL10-MALT1 complex, which then activates IKK complex, resulting in nuclear translocation and activation of NFKB1. May also play an indirect role in activation of the non-canonical NF-kappa-B (NFKB2) pathway. In the signaling pathway leading to JUN activation, acts by phosphorylating the mediator STK39/SPAK and may not act through MAP kinases signaling. Plays a critical role in TCR/CD28-induced NFATC1 and NFATC2 transactivation by participating in the regulation of reduced inositol 1,4,5-trisphosphate generation and intracellular calcium mobilization. After costimulation of T-cells through CD28 can phosphorylate CBLB and is required for the ubiquitination and subsequent degradation of CBLB, which is a prerequisite for the activation of TCR. During T-cells differentiation, plays an important role in the development of T-helper 2 (Th2) cells following immune and inflammatory responses, and, in the development of inflammatory autoimmune diseases, is necessary for the activation of IL17-producing Th17 cells. May play a minor role in Th1 response. Upon TCR stimulation, mediates T-cell protective survival signal by phosphorylating BAD, thus protecting T-cells from BAD-induced apoptosis, and by up-regulating BCL-X(L)/BCL2L1 levels through NF-kappa-B and JUN pathways. In platelets, regulates signal transduction downstream of the ITGA2B, CD36/GP4, F2R/PAR1 and F2RL3/PAR4 receptors, playing a positive role in 'outside-in' signaling and granule secretion signal transduction. May relay signals from the activated ITGA2B receptor by regulating the uncoupling of WASP and WIPF1, thereby permitting the regulation of actin filament nucleation and branching activity of the Arp2/3 complex. May mediate inhibitory effects of free fatty acids on insulin signaling by phosphorylating IRS1, which in turn blocks IRS1 tyrosine phosphorylation and downstream activation of the PI3K/AKT pathway. Phosphorylates MSN (moesin) in the presence of phosphatidylglycerol or phosphatidylinositol. Phosphorylates PDPK1 at 'Ser-504' and 'Ser-532' and negatively regulates its ability to phosphorylate PKB/AKT1. {ECO:0000269|PubMed:10746729, ECO:0000269|PubMed:12782715, ECO:0000269|PubMed:1508194, ECO:0000269|PubMed:15263025, ECO:0000269|PubMed:16493044, ECO:0000269|PubMed:19047061}. PTM: Autophosphorylation at Thr-219 is required for targeting to the TCR and cellular function of PRKCQ upon antigen receptor ligation. Following TCR stimulation, phosphorylated at Tyr-90 and Ser-685 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein. Note=In resting T-cells, mostly localized in cytoplasm. In response to TCR stimulation, associates with lipid rafts and then localizes in the immunological synapse (By similarity). {ECO:0000250}. SUBUNIT: Interacts with GLRX3 (via N-terminus). Interacts with ECT2. Part of a membrane raft complex composed at least of BCL10, CARD11, MALT1 and IKBKB (By similarity). {ECO:0000250}. DOMAIN: The C1 domain, containing the phorbol ester/DAG-type region 1 (C1A) and 2 (C1B), is the diacylglycerol sensor and the C2 domain is a non-calcium binding domain. TISSUE SPECIFICITY: T-lymphocytes and skeletal muscle. {ECO:0000269|PubMed:10746729, ECO:0000269|PubMed:1508194}. +Q8BZ03 KPCD2_MOUSE Serine/threonine-protein kinase D2 (EC 2.7.11.13) (nPKC-D2) 875 96,542 Active site (1); Binding site (1); Chain (1); Domain (2); Modified residue (19); Motif (1); Mutagenesis (2); Nucleotide binding (1); Sequence conflict (5); Zinc finger (2) FUNCTION: Serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of cell proliferation via MAPK1/3 (ERK1/2) signaling, oxidative stress-induced NF-kappa-B activation, inhibition of HDAC7 transcriptional repression, signaling downstream of T-cell antigen receptor (TCR) and cytokine production, and plays a role in Golgi membrane trafficking, angiogenesis, secretory granule release and cell adhesion (PubMed:17226786, PubMed:20819079). May potentiate mitogenesis induced by the neuropeptide bombesin by mediating an increase in the duration of MAPK1/3 (ERK1/2) signaling, which leads to accumulation of immediate-early gene products including FOS that stimulate cell cycle progression (PubMed:17226786). In response to oxidative stress, is phosphorylated at Tyr-438 and Tyr-718 by ABL1, which leads to the activation of PRKD2 without increasing its catalytic activity, and mediates activation of NF-kappa-B (By similarity). In response to the activation of the gastrin receptor CCKBR, is phosphorylated at Ser-244 by CSNK1D and CSNK1E, translocates to the nucleus, phosphorylates HDAC7, leading to nuclear export of HDAC7 and inhibition of HDAC7 transcriptional repression of NR4A1/NUR77 (By similarity). Upon TCR stimulation, is activated independently of ZAP70, translocates from the cytoplasm to the nucleus and is required for interleukin-2 (IL2) promoter up-regulation. During adaptive immune responses, is required in peripheral T-lymphocytes for the production of the effector cytokines IL2 and IFNG after TCR engagement and for optimal induction of antibody responses to antigens (PubMed:20819079). In epithelial cells stimulated with lysophosphatidic acid (LPA), is activated through a PKC-dependent pathway and mediates LPA-stimulated interleukin-8 (IL8) secretion via a NF-kappa-B-dependent pathway (By similarity). During TCR-induced T-cell activation, interacts with and is activated by the tyrosine kinase LCK, which results in the activation of the NFAT transcription factors (By similarity). In the trans-Golgi network (TGN), regulates the fission of transport vesicles that are on their way to the plasma membrane and in polarized cells is involved in the transport of proteins from the TGN to the basolateral membrane (By similarity). Plays an important role in endothelial cell proliferation and migration prior to angiogenesis, partly through modulation of the expression of KDR/VEGFR2 and FGFR1, two key growth factor receptors involved in angiogenesis (By similarity). In secretory pathway, is required for the release of chromogranin-A (CHGA)-containing secretory granules from the TGN (By similarity). Downstream of PRKCA, plays important roles in angiotensin-2-induced monocyte adhesion to endothelial cells (By similarity). {ECO:0000250|UniProtKB:Q9BZL6, ECO:0000269|PubMed:17226786, ECO:0000269|PubMed:20819079}. PTM: Phosphorylation of Ser-873 correlates with the activation status of the kinase. Ser-707 is probably phosphorylated by PKC. Phosphorylation at Ser-244 by CSNK1D and CSNK1E promotes nuclear localization and substrate targeting. Phosphorylation at Ser-244, Ser-707 and Ser-711 is required for nuclear localization. Phosphorylated at Tyr-438 by ABL1 in response to oxidative stress. Phosphorylated at Tyr-718 by ABL1 specifically in response to oxidative stress; requires prior phosphorylation at Ser-707 or/and Ser-711. {ECO:0000250|UniProtKB:Q9BZL6}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BZL6}. Cell membrane {ECO:0000250|UniProtKB:Q15139}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q9BZL6}. Note=Translocation to the cell membrane is required for kinase activation. Accumulates in the nucleus upon CK1-mediated phosphorylation after activation of G-protein-coupled receptors. Nuclear accumulation is regulated by blocking nuclear export of active PRKD2 rather than by increasing import. {ECO:0000250|UniProtKB:Q9BZL6}. SUBUNIT: Interacts (via C-terminus) with LCK. Interacts (via N-terminus and zing-finger domain 1 and 2) with PRKCD in response to oxidative stress; the interaction is independent of PRKD2 tyrosine phosphorylation. {ECO:0000250|UniProtKB:Q9BZL6}. +Q8K1Y2 KPCD3_MOUSE Serine/threonine-protein kinase D3 (EC 2.7.11.13) (Protein kinase C nu type) (nPKC-nu) 889 100,078 Active site (1); Binding site (1); Chain (1); Domain (2); Modified residue (17); Nucleotide binding (1); Zinc finger (2) FUNCTION: Converts transient diacylglycerol (DAG) signals into prolonged physiological effects, downstream of PKC. Involved in resistance to oxidative stress (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}. Note=Translocation to the cell membrane is required for kinase activation. {ECO:0000250}. +B2RUR4 KPRP_MOUSE Keratinocyte proline-rich protein 657 71,740 Chain (1); Compositional bias (2); Erroneous initiation (1); Modified residue (1) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q7TQM5}. +Q8VCX6 KPTN_MOUSE KICSTOR complex protein kaptin 430 47,545 Chain (1) FUNCTION: As part of the KICSTOR complex functions in the amino acid-sensing branch of the TORC1 signaling pathway. Recruits, in an amino acid-independent manner, the GATOR1 complex to the lysosomal membranes and allows its interaction with GATOR2 and the RAG GTPases. Functions upstream of the RAG GTPases and is required to negatively regulate mTORC1 signaling in absence of amino acids. In absence of the KICSTOR complex mTORC1 is constitutively localized to the lysosome and activated. The KICSTOR complex is also probably involved in the regulation of mTORC1 by glucose. {ECO:0000250|UniProtKB:Q9Y664}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q9Y664}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q9Y664}. Cell projection, stereocilium {ECO:0000250|UniProtKB:A0A1D5PJB7}. Note=Localization to lysosomes is amino acid-independent (By similarity). Colocalizes with F-actin (By similarity). {ECO:0000250|UniProtKB:Q9Y664}. SUBUNIT: Part of the KICSTOR complex composed of KPTN, ITFG2, C12orf66 and SZT2. SZT2 probably serves as a link between the other three proteins in the KICSTOR complex and mediates the direct interaction with the GATOR1 complex. May associate with F-actin filaments. {ECO:0000250|UniProtKB:Q9Y664}. +P52480 KPYM_MOUSE Pyruvate kinase PKM (EC 2.7.1.40) (Pyruvate kinase muscle isozyme) 531 57,845 Alternative sequence (1); Binding site (9); Chain (1); Cross-link (4); Metal binding (6); Modified residue (25); Region (4); Sequence conflict (18); Site (2) Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5. FUNCTION: Glycolytic enzyme that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. Stimulates POU5F1-mediated transcriptional activation (By similarity). {ECO:0000250}. PTM: ISGylated. {ECO:0000269|PubMed:16139798}.; PTM: Under hypoxia, hydroxylated by EGLN3. {ECO:0000250}.; PTM: Acetylation at Lys-305 is stimulated by high glucose concentration, it decreases enzyme activity and promotes its lysosomal-dependent degradation via chaperone-mediated autophagy. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P14618}. Nucleus {ECO:0000250|UniProtKB:P14618}. Note=Translocates to the nucleus in response to different apoptotic stimuli. Nuclear translocation is sufficient to induce cell death that is caspase independent, isoform-specific and independent of its enzymatic activity. {ECO:0000250|UniProtKB:P14618}. SUBUNIT: Monomer and homotetramer. Exists as a monomer in the absence of fructose 1,6 bi-phosphate (FBP), and reversibly associates to form a homotetramer in the presence of FBP. The monomeric form binds T3. Tetramer formation induces pyruvate kinase activity. FBP stimulates the formation of tetramers from dimers. Interacts with HERC1, POU5F1 and PML. Interacts (isoform M2) with EGLN3; the interaction hydroxylates PKM under hypoxia and enhances binding to HIF1A. Interacts (isoform M2) with HIF1A; the interaction is enhanced by binding of EGLN3, promoting enhanced transcription activity under hypoxia (By similarity). Interacts (isoform M2, but not isoform M1) with TRIM35; this interaction prevents FGFR1-dependent tyrosine phosphorylation (By similarity). Interacts with JMJD8 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P14618}. TISSUE SPECIFICITY: Embryonic stem cells and embryonal carcinoma cells. {ECO:0000269|PubMed:18191611}. +Q925H2 KR191_MOUSE Keratin-associated protein 19-1 (Keratin-associated protein 16-9) (Keratin-associated protein 16.9) 87 8,850 Chain (1); Region (1) FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins. {ECO:0000305}. SUBUNIT: Interacts with hair keratins. {ECO:0000250}. TISSUE SPECIFICITY: Strong expression in narrowly defined pattern restricted to the lower and middle cortical regions of the hair shaft in both developing and cycling hair. During hair follicle regression (catagen), expression levels decrease until expression is no longer detectable in follicles at resting stage (telogen). {ECO:0000269|PubMed:15385554}. +Q925I0 KR192_MOUSE Keratin-associated protein 19-2 (Keratin-associated protein 16-1) (Keratin-associated protein 16.1) 141 13,738 Chain (1); Region (1) FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins. {ECO:0000305}. SUBUNIT: Interacts with hair keratins. {ECO:0000250}. TISSUE SPECIFICITY: Strong expression in narrowly defined pattern restricted to the lower and middle cortical regions of the hair shaft in both developing and cycling hair. During hair follicle regression (catagen), expression levels decrease until expression is no longer detectable in follicles at resting stage (telogen). {ECO:0000269|PubMed:15385554}. +Q925H7 KR194_MOUSE Keratin-associated protein 19-4 (Keratin-associated protein 16-4) (Keratin-associated protein 16.4) 84 8,626 Chain (1); Region (1) FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins. {ECO:0000305}. SUBUNIT: Interacts with hair keratins. {ECO:0000250}. TISSUE SPECIFICITY: Strong expression in narrowly defined pattern restricted to the lower and middle cortical regions of the hair shaft in both developing and cycling hair. During hair follicle regression (catagen), expression levels decrease until expression is no longer detectable in follicles at resting stage (telogen). {ECO:0000269|PubMed:15385554}. +O08632 KR195_MOUSE Keratin-associated protein 19-5 (Glycine tyrosine-rich hair protein) (High-glycine tyrosine keratin type 1 alpha) (HGTp type 1 alpha) (Keratin-associated protein 8-2) 62 6,688 Chain (1); Region (1) FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins. {ECO:0000305}. SUBUNIT: Interacts with hair keratins. {ECO:0000305}. TISSUE SPECIFICITY: Expressed in skin during two hair growth cycles. Expression restricted to the cortical cells of hair follicles, appearing first in the cortical cells processing the flat nuclei located a few cells above the dermal papilla. {ECO:0000269|PubMed:9374545}. +Q925H4 KR211_MOUSE Keratin-associated protein 21-1 (Keratin-associated protein 16-7) (Keratin-associated protein 16.7) 128 12,539 Chain (1); Region (1); Sequence conflict (3) FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins. {ECO:0000305}. SUBUNIT: Interacts with hair keratins. {ECO:0000250}. TISSUE SPECIFICITY: Strong expression in narrowly defined pattern restricted to the lower and middle cortical regions of the hair shaft in both developing and cycling hair. During hair follicle regression (catagen), expression levels decrease until expression is no longer detectable in follicles at resting stage (telogen). {ECO:0000269|PubMed:15385554, ECO:0000269|PubMed:17151017}. +Q9D7N2 KR261_MOUSE Keratin-associated protein 26-1 215 22,448 Chain (1) FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins (By similarity). {ECO:0000250}. SUBUNIT: Interacts with hair keratins. {ECO:0000250}. +A2A5X4 KR291_MOUSE Keratin-associated protein 29-1 (Keratin-associated protein 29.2) 342 35,045 Chain (1); Region (1); Repeat (5) +O08640 KRA14_MOUSE Keratin-associated protein 14 (Anagen-specific protein KAP13) (mKAP13) (Pubertal mammary gland-specific protein 1) 167 17,919 Chain (1); Frameshift (2); Region (1); Repeat (2) FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins. {ECO:0000305}. SUBUNIT: Interacts with hair keratins. {ECO:0000305}. TISSUE SPECIFICITY: Expressed at high levels in skin where it is found predominantly in the keratogenous zone of hair follicle cortical cells and at lower levels in the epithelium of the developing mammary gland. {ECO:0000269|PubMed:10446281, ECO:0000269|PubMed:9287118, ECO:0000269|PubMed:9804342}. +Q9D3I6 KRA71_MOUSE Keratin-associated protein 7-1 (High glycine-tyrosine keratin-associated protein 7.1) 87 9,516 Chain (1); Region (1) FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins. SUBUNIT: Interacts with hair keratins. +O08633 KRA81_MOUSE Keratin-associated protein 8-1 (HGTp type I F) (High-glycine/tyrosine protein keratin) (HGT keratin) 61 6,697 Chain (1); Region (1); Sequence conflict (1) FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins. SUBUNIT: Interacts with hair keratins. TISSUE SPECIFICITY: Expression restricted exclusively to the cortical cells of hair follicles. +Q6VV64 KCNKI_MOUSE Potassium channel subfamily K member 18 (Two-pore-domain potassium channel TRESK) 394 44,403 Chain (1); Glycosylation (1); Intramembrane (2); Modified residue (2); Mutagenesis (6); Region (2); Sequence conflict (4); Topological domain (3); Transmembrane (4) INTRAMEM 114 140 Pore-forming; Name=Pore-forming 1. {ECO:0000255}.; INTRAMEM 326 340 Pore-forming; Name=Pore-forming 2. {ECO:0000255}. TRANSMEM 32 52 Helical. {ECO:0000255}.; TRANSMEM 142 162 Helical. {ECO:0000255}.; TRANSMEM 293 313 Helical. {ECO:0000255}.; TRANSMEM 347 367 Helical. {ECO:0000255}. TOPO_DOM 1 31 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 163 292 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 368 394 Cytoplasmic. {ECO:0000255}. FUNCTION: Outward rectifying potassium channel. Produces rapidly activating outward rectifier K(+) currents. May function as background potassium channel that sets the resting membrane potential. Channel activity is directly activated by calcium signal. Activated by the G(q)-protein coupled receptor pathway. The calcium signal robustly activates the channel via calcineurin, whereas the anchoring of 14-3-3/YWHAH interferes with the return of the current to the resting state after activation. Inhibited also by arachidonic acid and other naturally occurring unsaturated free fatty acids. Channel activity is also enhanced by volatile anesthetics, such as isoflurane. Appears to be the primary target of hydroxy-alpha-sanshool, an ingredient of Schezuan pepper. May be involved in the somatosensory function with special respect to pain sensation. {ECO:0000269|PubMed:14981085, ECO:0000269|PubMed:16192517, ECO:0000269|PubMed:18568022}. PTM: Phosphorylation of Ser-264 is required for the binding of 14-3-3eta/YWHAH. Calcineurin-mediated dephosphorylation of Ser-276 enhances channel activity. {ECO:0000269|PubMed:14981085, ECO:0000269|PubMed:18397886}.; PTM: N-glycosylated. {ECO:0000269|PubMed:20006580}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20006580}; Multi-pass membrane protein {ECO:0000269|PubMed:20006580}. SUBUNIT: Interacts with calcineurin. Interacts with YWHAH, in a phosphorylation-dependent manner. {ECO:0000269|PubMed:16569637, ECO:0000269|PubMed:18397886}. TISSUE SPECIFICITY: Detected in brain cortex, cerebellum, dorsal root ganglion, spinal cord and testis. High expression in trigeminal ganglion, also expressed in autonomic nervous system ganglia such as the stellate ganglion and paravertebral sympathetic ganglia. Expressed in all adult spinal cord and brain regions, with slightly higher expression in thalamus, hypothalamus, hippocampus and posterior corte (at protein level). In non-neuronal tissues, substantial expression found in lung and heart and weal expression in liver, testis, kidney, small intestine and spleen. {ECO:0000269|PubMed:14981085, ECO:0000269|PubMed:16192517, ECO:0000269|PubMed:17962323, ECO:0000269|PubMed:20871611}. +P59053 KCNG3_MOUSE Potassium voltage-gated channel subfamily G member 3 (Voltage-gated potassium channel subunit Kv10.1) (Voltage-gated potassium channel subunit Kv6.3) 433 49,247 Alternative sequence (1); Chain (1); Intramembrane (2); Motif (1); Topological domain (8); Transmembrane (6) INTRAMEM 358 369 Helical; Name=Pore helix. {ECO:0000250|UniProtKB:P63142}.; INTRAMEM 370 377 {ECO:0000250|UniProtKB:P63142}. TRANSMEM 166 187 Helical; Name=Segment S1. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 218 239 Helical; Name=Segment S2. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 251 271 Helical; Name=Segment S3. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 282 302 Helical; Voltage-sensor; Name=Segment S4. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 318 339 Helical; Name=Segment S5. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 385 413 Helical; Name=Segment S6. {ECO:0000250|UniProtKB:P63142}. TOPO_DOM 1 165 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 188 217 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 240 250 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 272 281 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 303 317 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 340 357 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 378 384 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 414 433 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}. FUNCTION: Potassium channel subunit that does not form functional channels by itself. Can form functional heterotetrameric channels with KCNB1; modulates the delayed rectifier voltage-gated potassium channel activation and deactivation rates of KCNB1. {ECO:0000250|UniProtKB:Q8TAE7}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8TAE7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8TAE7}. Cytoplasm {ECO:0000250|UniProtKB:Q8TAE7}. Note=Has to be associated with KCNB1 or possibly another partner to get inserted in the plasma membrane. Colocalizes with KCNB1 at the plasma membrane. Remains intracellular in the absence of KCNB1. {ECO:0000250|UniProtKB:Q8TAE7}. SUBUNIT: Heterotetramer with KCNB1. Does not form homomultimers. {ECO:0000250|UniProtKB:Q8TAE7}. DOMAIN: The transmembrane segment S4 functions as voltage-sensor and is characterized by a series of positively charged amino acids at every third position. Channel opening and closing is effected by a conformation change that affects the position and orientation of the voltage-sensor paddle formed by S3 and S4 within the membrane. A transmembrane electric field that is positive inside would push the positively charged S4 segment outwards, thereby opening the pore, while a field that is negative inside would pull the S4 segment inwards and close the pore. Changes in the position and orientation of S4 are then transmitted to the activation gate formed by the inner helix bundle via the S4-S5 linker region. {ECO:0000250|UniProtKB:P63142}. +Q80UN1 KCTD9_MOUSE BTB/POZ domain-containing protein KCTD9 339 36,994 Chain (1); Domain (5); Modified residue (1); Sequence conflict (2) Protein modification; protein ubiquitination. FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex, which mediates the ubiquitination of target proteins, leading to their degradation by the proteasome. {ECO:0000250|UniProtKB:Q7L273}. SUBUNIT: Forms pentamers. Component of a complex mades of five KCTD9 and five CUL3 subunits. {ECO:0000250|UniProtKB:Q7L273}. +Q3U492 KCP_MOUSE Kielin/chordin-like protein (Cysteine-rich BMP regulator 2) (Cysteine-rich motor neuron 2 protein) (CRIM-2) (Kielin/chordin-like protein 1) (KCP-1) 1550 166,628 Alternative sequence (2); Chain (1); Coiled coil (1); Disulfide bond (1); Domain (20); Glycosylation (1); Sequence conflict (4); Signal peptide (1) FUNCTION: Enhances bone morphogenetic protein (BMP) signaling in a paracrine manner. In contrast, it inhibits both the activin-A and TGFB1-mediated signaling pathways. {ECO:0000269|PubMed:15793581}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15793581}. SUBUNIT: Interacts with BMP7 and, by doing so, enhances binding to the type I receptors that contains cytoplasmic serine-/threonine protein kinase domains. Also able to interact with activin-A and TGFB1. {ECO:0000269|PubMed:15793581, ECO:0000269|PubMed:16738323}. TISSUE SPECIFICITY: Weakly expressed in embryonic kidney and brain. Not expressed in adult tissues and several cell lines. {ECO:0000269|PubMed:15793581}. +Q04447 KCRB_MOUSE Creatine kinase B-type (EC 2.7.3.2) (B-CK) (Creatine kinase B chain) (Creatine phosphokinase B-type) (CPK-B) 381 42,713 Binding site (9); Chain (1); Domain (2); Modified residue (7); Nucleotide binding (2); Sequence conflict (2) FUNCTION: Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Dimer of identical or non-identical chains, which can be either B (brain type) or M (muscle type). With MM being the major form in skeletal muscle and myocardium, MB existing in myocardium, and BB existing in many tissues, especially brain. {ECO:0000250|UniProtKB:P12277}. +Q6ZPY7 KDM3B_MOUSE Lysine-specific demethylase 3B (EC 1.14.11.-) (JmjC domain-containing histone demethylation protein 2B) (Jumonji domain-containing protein 1B) 1562 170,875 Alternative sequence (2); Chain (1); Compositional bias (1); Cross-link (1); Domain (1); Erroneous initiation (1); Frameshift (1); Initiator methionine (1); Metal binding (3); Modified residue (12); Motif (1); Sequence conflict (3); Zinc finger (1) FUNCTION: Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. Demethylation of Lys residue generates formaldehyde and succinate May have tumor suppressor activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. DOMAIN: Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs are known to mediate the association with nuclear receptors. {ECO:0000250}. +Q8BW72 KDM4A_MOUSE Lysine-specific demethylase 4A (EC 1.14.11.-) (JmjC domain-containing histone demethylation protein 3A) (Jumonji domain-containing protein 2A) 1064 120,334 Alternative sequence (2); Binding site (7); Chain (1); Domain (4); Erroneous initiation (1); Initiator methionine (1); Metal binding (7); Modified residue (2); Region (1); Sequence conflict (4); Zinc finger (3) FUNCTION: Histone demethylase that specifically demethylates 'Lys-9' and 'Lys-36' residues of histone H3, thereby playing a central role in histone code (PubMed:24953653). Does not demethylate histone H3 'Lys-4', H3 'Lys-27' nor H4 'Lys-20'. Demethylates trimethylated H3 'Lys-9' and H3 'Lys-36' residue, while it has no activity on mono- and dimethylated residues. Demethylation of Lys residue generates formaldehyde and succinate. Participates in transcriptional repression of ASCL2 and E2F-responsive promoters via the recruitment of histone deacetylases and NCOR1, respectively (By similarity). {ECO:0000250|UniProtKB:O75164, ECO:0000269|PubMed:24953653}. PTM: Ubiquitinated by RNF8 and RNF168, leading to its degradation (PubMed:24953653). Degradation promotes accessibility of H4K20me2 mark for DNA repair protein TP53BP1, which is then recruited (By similarity). {ECO:0000250|UniProtKB:O75164, ECO:0000269|PubMed:24953653}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00537}. SUBUNIT: Interacts with histone deacetylase proteins HDAC1, HDAC2 and HDAC3. Interacts with RB and NCOR1 (By similarity). {ECO:0000250|UniProtKB:O75164}. DOMAIN: The 2 Tudor domains recognize and bind methylated histone H3 'Lys-4' residue (H3K4me). Double Tudor domain has an interdigitated structure and the unusual fold is required for its ability to bind methylated histone tails. Trimethylated H3 'Lys-4' (H3K4me3) is bound in a cage of 3 aromatic residues, 2 of which are from the Tudor domain 2, while the binding specificity is determined by side-chain interactions involving residues from the Tudor domain 1. The Tudor domains are also able to bind trimethylated histone H3 'Lys-9' (H3K9me3), di- and trimethylated H4 'Lys-20' (H4K20me2 and H4K20me3). Has high affinity for H4K20me2, blocking recruitment of proteins such as TP53BP1 (By similarity). {ECO:0000250|UniProtKB:O75164}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:16024779}. +Q8CIG3 KDM1B_MOUSE Lysine-specific histone demethylase 1B (EC 1.-.-.-) (Flavin-containing amine oxidase domain-containing protein 1) (Lysine-specific histone demethylase 2) 826 92,633 Alternative sequence (2); Binding site (2); Chain (1); Domain (1); Erroneous initiation (1); Frameshift (1); Metal binding (12); Modified residue (3); Mutagenesis (1); Nucleotide binding (2); Region (6); Zinc finger (1) FUNCTION: Histone demethylase that demethylates 'Lys-4' of histone H3, a specific tag for epigenetic transcriptional activation, thereby acting as a corepressor. Required for de novo DNA methylation of a subset of imprinted genes during oogenesis. Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed. Demethylates both mono- and di-methylated 'Lys-4' of histone H3. Has no effect on tri-methylated 'Lys-4', mono-, di- or tri-methylated 'Lys-9', mono-, di- or tri-methylated 'Lys-27', mono-, di- or tri-methylated 'Lys-36' of histone H3, or on mono-, di- or tri-methylated 'Lys-20' of histone H4. {ECO:0000269|PubMed:19407342, ECO:0000269|PubMed:19727073}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19727073}. SUBUNIT: Interacts with its cofactor GLYR1 at nucleosomes; this interaction stimulates H3K4me1 and H3K4me2 demethylation (By similarity). Does not form a complex with RCOR1/CoREST. {ECO:0000250|UniProtKB:Q8NB78}. DOMAIN: The SWIRM domain may act as an anchor site for a histone tail. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in growing oocytes and in intestinal gland. {ECO:0000269|PubMed:19727073}. +Q3UXZ9 KDM5A_MOUSE Lysine-specific demethylase 5A (EC 1.14.11.-) (Histone demethylase JARID1A) (Jumonji/ARID domain-containing protein 1A) (Retinoblastoma-binding protein 2) (RBBP-2) 1690 192,216 Binding site (4); Chain (1); Compositional bias (1); Cross-link (2); Domain (3); Erroneous initiation (1); Metal binding (3); Modified residue (12); Motif (1); Region (1); Sequence conflict (6); Zinc finger (4) FUNCTION: Histone demethylase that specifically demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-9', H3 'Lys-27', H3 'Lys-36', H3 'Lys-79' or H4 'Lys-20'. Demethylates trimethylated and dimethylated but not monomethylated H3 'Lys-4' (PubMed:17320161, PubMed:17320163). Regulates specific gene transcription through DNA-binding on 5'-CCGCCC-3' motif. May stimulate transcription mediated by nuclear receptors. Involved in transcriptional regulation of Hox proteins during cell differentiation (By similarity). May participate in transcriptional repression of cytokines such as CXCL12. Plays a role in the regulation of the circadian rhythm and in maintaining the normal periodicity of the circadian clock. In a histone demethylase-independent manner, acts as a coactivator of the CLOCK-ARNTL/BMAL1-mediated transcriptional activation of PER1/2 and other clock-controlled genes and increases histone acetylation at PER1/2 promoters by inhibiting the activity of HDAC1 (PubMed:21960634). Seems to act as a transcriptional corepressor for some genes such as MT1F and to favor the proliferation of cancer cells (By similarity). {ECO:0000250|UniProtKB:P29375, ECO:0000269|PubMed:17320161, ECO:0000269|PubMed:17320163, ECO:0000269|PubMed:21960634}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:P29375}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355, ECO:0000255|PROSITE-ProRule:PRU00537, ECO:0000269|PubMed:20064375}. Note=Occupies promoters of genes involved in RNA metabolism and mitochondrial function. {ECO:0000269|PubMed:20064375}. SUBUNIT: Interacts with RB1, ESR1, MYC, MYCN and LMO2 (By similarity). Interacts with SUZ12; the interaction is direct (PubMed:20064375). Interacts with HDAC1, ARNTL/BMAL1 and CLOCK (PubMed:21960634). Interacts (via PHD-type 1 zinc finger) with histone H3 unmodified at 'Lys-4' and (via PHD-type 3 zinc finger) with histone H3 di- and trimethylated at 'Lys-4' (By similarity). {ECO:0000250|UniProtKB:P29375, ECO:0000269|PubMed:20064375, ECO:0000269|PubMed:21960634}. DOMAIN: The GSGFP motif is required for the interaction with SUZ12 (PubMed:20064375). The ARID domain specifically binds to the CCGCCC motif and is required for the lysine-specific histone demethylase activity. The PHD-type 3 zinc finger is required for the interaction with histone H3 di- and trimethylated at 'Lys-4' (By similarity). {ECO:0000250|UniProtKB:P29375, ECO:0000269|PubMed:20064375}. +Q8BMK1 METL2_MOUSE Methyltransferase-like protein 2 (EC 2.1.1.-) 389 43,912 Alternative sequence (1); Chain (1); Sequence conflict (2) FUNCTION: Probable S-adenosyl-L-methionine-dependent methyltransferase that mediates 3-methylcytidine modification of some tRNAs. {ECO:0000250}. +Q3U034 METL4_MOUSE Methyltransferase-like protein 4 (EC 2.1.1.-) 471 53,306 Chain (1) FUNCTION: Probable methyltransferase. {ECO:0000250}. +Q8K1A0 METL5_MOUSE Methyltransferase-like protein 5 (EC 2.1.1.-) 209 23,662 Chain (1); Frameshift (1) FUNCTION: Probable methyltransferase. {ECO:0000250}. +O35367 KERA_MOUSE Keratocan (KTN) (Keratan sulfate proteoglycan keratocan) 351 40,404 Chain (1); Disulfide bond (3); Domain (1); Glycosylation (4); Repeat (10); Signal peptide (1) FUNCTION: May be important in developing and maintaining corneal transparency and for the structure of the stromal matrix. PTM: Binds keratan sulfate chains. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. TISSUE SPECIFICITY: Selectively expressed in cornea of adult where it is detected in keratocytes but not in scleral cells. In embryo, first detected in periocular mesenchymal cells migrating toward developing cornea on E13.5; expression gradually restricted to corneal stromal cells on E14.5 to E18.5. Detected in scleral cells of E15.5 but not in E18.5 embryos. +Q9D074 MGRN1_MOUSE E3 ubiquitin-protein ligase MGRN1 (EC 2.3.2.27) (Mahogunin RING finger protein 1) (RING-type E3 ubiquitin transferase MGRN1) 532 58,477 Alternative sequence (3); Chain (1); Initiator methionine (1); Lipidation (1); Modified residue (5); Motif (1); Mutagenesis (2); Sequence conflict (3); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase. Mediates TSG101 monoubiquitination at multiple sites. Plays a role in the regulation of endosome-to-lysosome trafficking. Impairs MC1R- and MC4R-signaling by competing with GNAS-binding to MCRs and inhibiting agonist-induced cAMP production. Does not inhibit ADRB2-signaling. Does not promote MC1R ubiquitination (By similarity). Acts also as a negative regulator of hedgehog signaling (PubMed:29290584). {ECO:0000250, ECO:0000269|PubMed:12560552, ECO:0000269|PubMed:19703557, ECO:0000269|PubMed:29290584}. PTM: Autoubiquitinated in vitro. {ECO:0000269|PubMed:12560552}. SUBCELLULAR LOCATION: Early endosome {ECO:0000269|PubMed:19422019, ECO:0000269|PubMed:19524515}. Note=The endosomal localization is dependent on the interaction with TSG101. {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 1: Cytoplasm. Cell membrane {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 5: Cytoplasm. Nucleus. Note=In the cytoplasm, predominantly localized to the perinuclear region and discrete vesicular structures. In the nucleus, broadly distributed, but excluded from nucleoli. SUBUNIT: Interacts with MC1R and MC4R (By similarity). Interacts with TSG101. Interacts with mislocalized cytosolically exposed PRNP; this interaction alters MGRN1 subcellular location and causes lysosomal enlargement. {ECO:0000250, ECO:0000269|PubMed:19524515, ECO:0000269|PubMed:19703557}. DOMAIN: The RING finger is required for ubiquitin ligase activity. TISSUE SPECIFICITY: Widely expressed, with highest levels in brain, heart, kidney and liver. In the CNS, especially prominent in the Purkinje cells of the cerebellum. In the skin, expressed in the basal layer of the epidermis and hair follicles, primarily in the outer root sheath. Isoforms 1, 3, 4 and 5 are equally expressed in the liver. Isoforms 1, 3 and 4 are most abundant in brain, kidney and heart, respectively. {ECO:0000269|PubMed:12438443, ECO:0000269|PubMed:12560552, ECO:0000269|PubMed:17083490, ECO:0000269|PubMed:19524515}. +P0C605 KGP1_MOUSE cGMP-dependent protein kinase 1 (cGK 1) (cGK1) (EC 2.7.11.12) (cGMP-dependent protein kinase I) (cGKI) 671 76,350 Active site (1); Alternative sequence (1); Binding site (3); Chain (1); Coiled coil (1); Disulfide bond (1); Domain (2); Initiator methionine (1); Modified residue (3); Nucleotide binding (5); Region (5) FUNCTION: Serine/threonine protein kinase that acts as key mediator of the nitric oxide (NO)/cGMP signaling pathway. GMP binding activates PRKG1, which phosphorylates serines and threonines on many cellular proteins. Numerous protein targets for PRKG1 phosphorylation are implicated in modulating cellular calcium, but the contribution of each of these targets may vary substantially among cell types. Proteins that are phosphorylated by PRKG1 regulate platelet activation and adhesion, smooth muscle contraction, cardiac function, gene expression, feedback of the NO-signaling pathway, and other processes involved in several aspects of the CNS like axon guidance, hippocampal and cerebellar learning, circadian rhythm and nociception. Smooth muscle relaxation is mediated through lowering of intracellular free calcium, by desensitization of contractile proteins to calcium, and by decrease in the contractile state of smooth muscle or in platelet activation. Regulates intracellular calcium levels via several pathways: phosphorylates MRVI1/IRAG and inhibits IP3-induced Ca(2+) release from intracellular stores, phosphorylation of KCNMA1 (BKCa) channels decreases intracellular Ca(2+) levels, which leads to increased opening of this channel. PRKG1 phosphorylates the canonical transient receptor potential channel (TRPC) family which inactivates the associated inward calcium current. Another mode of action of NO/cGMP/PKGI signaling involves PKGI-mediated inactivation of the Ras homolog gene family member A (RhoA). Phosphorylation of RHOA by PRKG1 blocks the action of this protein in myriad processes: regulation of RHOA translocation; decreasing contraction; controlling vesicle trafficking, reduction of myosin light chain phosphorylation resulting in vasorelaxation. Activation of PRKG1 by NO signaling alters also gene expression in a number of tissues. In smooth muscle cells, increased cGMP and PRKG1 activity influence expression of smooth muscle-specific contractile proteins, levels of proteins in the NO/cGMP signaling pathway, down-regulation of the matrix proteins osteopontin and thrombospondin-1 to limit smooth muscle cell migration and phenotype. Regulates vasodilator-stimulated phosphoprotein (VASP) functions in platelets and smooth muscle. {ECO:0000269|PubMed:10209042, ECO:0000269|PubMed:11055988, ECO:0000269|PubMed:19156199, ECO:0000269|PubMed:9606187, ECO:0000269|PubMed:9920894}. PTM: Autophosphorylation increases kinase activity. {ECO:0000250}.; PTM: 65 kDa monomer is produced by proteolytic cleavage. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Colocalized with TRPC7 in the plasma membrane. {ECO:0000250}. SUBUNIT: Isoform alpha: parallel homodimer or heterodimer and also heterotetramer. Interacts directly with PPP1R12A. Non-covalent dimer of dimer of PRKG1-PRKG1 and PPP1R12A-PPP1R12A. This interaction targets PRKG1 to stress fibers to mediate smooth muscle cell relaxation and vasodilation in responses to rises in cGMP (By similarity). Isoform beta: antiparallel homodimer. Part of cGMP kinase signaling complex at least composed of ACTA2/alpha-actin, CNN1/calponin H1, PLN/phospholamban, PRKG1 and ITPR1 (By similarity). Interacts with MRVI1. Forms a stable complex with ITPR1, MRVI1, and isoform beta of PRKG1 (By similarity). Interacts with TRPC7 (via ankyrin repeat domain) (By similarity). Isoform alpha interacts with RGS2 (By similarity). Interacts with GTF2I (By similarity). {ECO:0000250}. DOMAIN: Composed of an N-terminal leucine-zipper domain followed by an autoinhibitory domain, which mediate homodimer formation and inhibit kinase activity, respectively. Next, two cGMP-binding domains are followed by the catalytic domain at the C-terminus. Binding of cGMP to cGMP-binding domains results in a conformational change that activates kinase activity by removing the autoinhibitory domain from the catalytic cleft leaving the catalytic domain free to phosphorylate downstream substrates. Isoforms alpha and beta have identical cGMP-binding and catalytic domains but differ in their leucine zipper and autoinhibitory sequences and therefore differ in their dimerization substrates and kinase enzyme activity (By similarity). {ECO:0000250}.; DOMAIN: Heterotetramerization is mediated by the interaction between a coiled-coil of PRKG1 and the leucine/isoleucine zipper of PPP1R12A/MBS, the myosin-binding subunit of the myosin phosphatase. {ECO:0000250}. TISSUE SPECIFICITY: Detected in cerebellum, hippocampus, dorsomedial hypothalamus, medulla, subcommissural organ, cerebral cortex, amygdala, habenulae, various hypothalamic regions, olfactory bulb, pituitary gland, and retina. Isoform alpha is prominent in the cerebellum and medulla, whereas isoform Beta is predominant in the cortex, hippocampus, hypothalamus, and olfactory bulb. {ECO:0000269|PubMed:16154279}. +Q61410 KGP2_MOUSE cGMP-dependent protein kinase 2 (cGK 2) (cGK2) (EC 2.7.11.12) (cGMP-dependent protein kinase II) (cGKII) 762 87,085 Active site (1); Binding site (4); Chain (1); Domain (2); Initiator methionine (1); Lipidation (1); Modified residue (4); Nucleotide binding (5); Region (2) FUNCTION: Crucial regulator of intestinal secretion and bone growth (PubMed:8953039). Phosphorylates and activates CFTR on the plasma membrane. Plays a key role in intestinal secretion by regulating cGMP-dependent translocation of CFTR in jejunum (By similarity). Acts downstream of NMDAR to activate the plasma membrane accumulation of GRIA1/GLUR1 in synapse and increase synaptic plasticity. Phosphorylates GRIA1/GLUR1 at Ser-863 (By similarity). Acts as regulator of gene expression and activator of the extracellular signal-regulated kinases MAPK3/ERK1 AND MAPK1/ERK2 in mechanically stimulated osteoblasts. Under fluid shear stress, mediates ERK activation and subsequent induction of FOS, FOSL1/FRA1, FOSL2/FRA2 and FOSB that play a key role in the osteoblast anabolic response to mechanical stimulation (PubMed:19282289). {ECO:0000250|UniProtKB:Q64595, ECO:0000269|PubMed:19282289, ECO:0000269|PubMed:8953039}. PTM: Myristoylation mediates membrane localization. {ECO:0000250}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:Q13237}; Lipid-anchor {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:19282289}; Lipid-anchor {ECO:0000255}. SUBUNIT: Interacts with GRIA1/GLUR1. {ECO:0000250|UniProtKB:Q64595}. +Q9D4R2 MGT4D_MOUSE Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase-like protein MGAT4D (N-acetylglucosaminyltransferase MGAT1 inhibitory protein) (GlcNAcT-I inhibitory protein) (GnT1IP) 373 43,300 Alternative sequence (1); Chain (1); Compositional bias (1); Glycosylation (3); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 6 26 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 5 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 27 373 Lumenal. {ECO:0000255}. FUNCTION: Isoform 2: May play a role in male spermatogenesis. In vitro acts as inhibitor of MGAT1 activity causing cell surface proteins to carry mainly high mannose N-glycans. The function is mediated by its lumenal domain and occurs specifically in the Golgi. A catalytic glucosyltransferase activity is not detected. May be involved in regulation of Sertoli-germ cell interactions during specific stages of spermatogenesis. {ECO:0000269|PubMed:20805325, ECO:0000269|PubMed:26371870}. PTM: Isoform 2 is N-glycosylated; consisting of high-mannose and/or hybrid glycans. {ECO:0000269|PubMed:20805325}. SUBCELLULAR LOCATION: Isoform 2: Endoplasmic reticulum membrane {ECO:0000269|PubMed:20805325}; Single-pass type II membrane protein {ECO:0000305|PubMed:20805325}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000269|PubMed:20805325}; Single-pass type II membrane protein {ECO:0000305|PubMed:20805325}. Golgi apparatus membrane {ECO:0000269|PubMed:20805325}; Single-pass type II membrane protein {ECO:0000305|PubMed:20805325}.; SUBCELLULAR LOCATION: Isoform 1: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q4V8F8}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q4V8F8}. SUBUNIT: Isoform 2 self-associates; specifically in the endoplasmic reticulum prior to its translocation to the Golgi. Isoform 1 and isoform 2 interact with MGAT1, MGAT3 and MAN2A2; isoform 2 interacts specifically with MGAT1 in the Golgi. {ECO:0000269|PubMed:20805325, ECO:0000269|PubMed:26371870}. TISSUE SPECIFICITY: Isoform 1 and isoform 2 are specifically expressed in testis. Isoform 2 is expressed in spermatocytes but not in spermatids. Isoform 1 is expressed in spermatids. {ECO:0000269|PubMed:20805325}. +Q4KL78 KHD1C_MOUSE KH homology domain-containing protein 1C 166 19,664 Chain (1); Domain (1) +E9PVX6 KI67_MOUSE Proliferation marker protein Ki-67 (Antigen identified by monoclonal antibody Ki-67 homolog) (Antigen KI-67 homolog) (Antigen Ki67 homolog) 3177 350,864 Alternative sequence (1); Chain (1); Cross-link (13); Domain (2); Frameshift (2); Modified residue (98); Nucleotide binding (1); Repeat (15); Sequence conflict (10) FUNCTION: Required to maintain individual mitotic chromosomes dispersed in the cytoplasm following nuclear envelope disassembly (PubMed:27362226). Associates with the surface of the mitotic chromosome, the perichromosomal layer, and covers a substantial fraction of the chromosome surface (PubMed:27362226). Prevents chromosomes from collapsing into a single chromatin mass by forming a steric and electrostatic charge barrier: the protein has a high net electrical charge and acts as a surfactant, dispersing chromosomes and enabling independent chromosome motility (PubMed:27362226). Binds DNA, with a preference for supercoiled DNA and AT-rich DNA (By similarity). Does not contribute to the internal structure of mitotic chromosomes (PubMed:26949251). May play a role in chromatin organization (PubMed:26949251). It is however unclear whether it plays a direct role in chromatin organization or whether it is an indirect consequence of its function in maintaining mitotic chromosomes dispersed. {ECO:0000250|UniProtKB:P46013, ECO:0000269|PubMed:26949251, ECO:0000269|PubMed:27362226, ECO:0000305}. PTM: Phosphorylated. Hyperphosphorylated in mitosis. Hyperphosphorylated form does not bind DNA. {ECO:0000250|UniProtKB:P46013}. SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:12355204, ECO:0000269|PubMed:8834799}. Nucleus {ECO:0000269|PubMed:12355204, ECO:0000269|PubMed:8834799}. Nucleus, nucleolus {ECO:0000269|PubMed:12355204, ECO:0000269|PubMed:8834799}. Note=Associates with the surface of the mitotic chromosome, the perichromosomal layer, and covers a substantial fraction of the mitotic chromosome surface (PubMed:8834799, PubMed:12355204). Associates with satellite DNA in G1 phase (By similarity). Binds tightly to chromatin in interphase, chromatin-binding decreases in mitosis when it associates with the surface of the condensed chromosomes (By similarity). Predominantly localized in the G1 phase in the perinucleolar region, in the later phases it is also detected throughout the nuclear interior, being predominantly localized in the nuclear matrix (By similarity). {ECO:0000250|UniProtKB:P46013, ECO:0000269|PubMed:12355204, ECO:0000269|PubMed:8834799}. SUBUNIT: Interacts with KIF15. Interacts (via the FHA domain) with NIFK. Interacts with PPP1CC. Part of a complex composed at least of ASCL2, EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; this complex may have a histone H3-specific methyltransferase activity. {ECO:0000250|UniProtKB:P46013}. TISSUE SPECIFICITY: Mainly present in proliferating cells (at protein level). {ECO:0000269|PubMed:8834799}. +Q80WE4 KI20B_MOUSE Kinesin-like protein KIF20B (Kinesin family member 20B) (Kinesin-related motor interacting with PIN1) (M-phase phosphoprotein 1) (MPP1) 1774 203,514 Alternative sequence (4); Chain (1); Coiled coil (4); Domain (1); Frameshift (2); Modified residue (8); Mutagenesis (2); Nucleotide binding (1); Region (2); Sequence conflict (2) FUNCTION: Plus-end-directed motor enzyme that is required for completion of cytokinesis (By similarity). Required for proper midbody organization and abscission in polarized cortical stem cells (PubMed:24173802). Plays a role in the regulation of neuronal polarization by mediating the transport of specific cargos. Participates in the mobilization of SHTN1 and in the accumulation of PIP3 in the growth cone of primary hippocampal neurons in a tubulin and actin-dependent manner (PubMed:23864681). In the developing telencephalon, cooperates with SHTN1 to promote both the transition from the multipolar to the bipolar stage and the radial migration of cortical neurons from the ventricular zone toward the superficial layer of the neocortex (PubMed:23864681). Involved in cerebral cortex growth (PubMed:24173802). Acts as an oncogene for promoting bladder cancer cells proliferation, apoptosis inhibition and carcinogenic progression (By similarity). {ECO:0000250|UniProtKB:Q96Q89, ECO:0000269|PubMed:23864681, ECO:0000269|PubMed:24173802}. PTM: Phosphorylated during mitosis by CDK1. {ECO:0000250|UniProtKB:Q96Q89}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24173802}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:23864681}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q96Q89}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q96Q89}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q96Q89}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:24173802}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q96Q89}. Midbody {ECO:0000269|PubMed:23864681, ECO:0000269|PubMed:24173802}. Cell projection, axon {ECO:0000269|PubMed:23864681}. Cell projection, growth cone {ECO:0000269|PubMed:23864681}. Note=Localizes mainly in the nucleus during interphase although it is also detected in the cytoplasm without clear association with microtubules (By similarity). Localized to the central spindle during cytokinetic furrowing and with the midbody during abscission (PubMed:24173802). A 2-3 fold expression increase is seen as cells progress from G1 to G2/M phase. During prophase and metaphase it is found throughout the cytoplasm and at anaphase accumulates at the midplan of the cell and forms a distinct band extending across the spindle midzone. At anaphase it is concentrated in the midbody (By similarity). Colocalized partially along microtubules in primary neurons (PubMed:23864681). Colocalized with SHTN1 along microtubules to the tip of the growing cone in primary hippocampal neurons (PubMed:23864681). Localized in midbodies between dividing radial progenitors in the ventricular zone (PubMed:23864681). Colocalized with PRC1 in the nucleus of bladder carcinoma cells at the interphase. Colocalized with PRC1 in bladder carcinoma cells at prophase, metaphase, early anaphase, at the midzone in late anaphase and at the contractile ring in telophase (By similarity). {ECO:0000250|UniProtKB:Q96Q89, ECO:0000269|PubMed:23864681, ECO:0000269|PubMed:24173802}. SUBUNIT: Oligomerizes (via kinesin motor domain). Associates with microtubules. Interacts (via C-terminal globular tail region) with PIN1 (via WW domain). Interacts with PRC1 (By similarity). Interacts with SHTN1 (via N-terminus); the interaction is direct and promotes the association of SHTN1 to microtubules in primary neurons (PubMed:23864681). Associates with microtubules (PubMed:23864681). {ECO:0000250|UniProtKB:Q96Q89, ECO:0000269|PubMed:23864681}. TISSUE SPECIFICITY: Expressed in the brain (at protein level) (PubMed:24173802). {ECO:0000269|PubMed:24173802}. +Q60575 KIF1B_MOUSE Kinesin-like protein KIF1B 1816 204,081 Alternative sequence (4); Chain (1); Coiled coil (4); Domain (3); Initiator methionine (1); Modified residue (12); Nucleotide binding (1); Region (1); Sequence conflict (7) FUNCTION: Motor for anterograde transport of mitochondria. Has a microtubule plus end-directed motility. SUBCELLULAR LOCATION: Cytoplasmic vesicle. Cytoplasm, cytoskeleton. Mitochondrion {ECO:0000250}. Note=Colocalizes with synaptophysin at synaptic cytoplasmic transport vesicles in the neurites of hippocampal neurons. {ECO:0000250}. SUBUNIT: Monomer. Interacts with KBP. Interacts (via C-terminus end of the kinesin-motor domain) with CHP1; the interaction occurs in a calcium-dependent manner (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed almost exclusively in adult brain tissue (mainly in the cerebellum and cerebrum) within a single type of neuronal cell. +Q6P9L6 KIF15_MOUSE Kinesin-like protein KIF15 (Kinesin-like protein 2) (Kinesin-like protein 7) 1387 160,120 Chain (1); Coiled coil (1); Domain (1); Modified residue (4); Nucleotide binding (1); Sequence conflict (2) FUNCTION: Plus-end directed kinesin-like motor enzyme involved in mitotic spindle assembly. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Detected during the interphase in the cytoplasm as finely punctuate pattern and irregularly shaped dots. Localizes at the spindle poles and microtubules prior to anaphase. Localizes at the central spindle at anaphase. Localizes at the sites of invaginating cell membranes, a position that corresponds to the location of the contractile actomyosin ring of dividing cells. Colocalizes with actin in interphase. Colocalizes in dendrites and in growth cone of axons with microtubules. Colocalizes with TPX2 in mitosis (By similarity). {ECO:0000250}. SUBUNIT: Interacts with MKI67 and TPX2. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain (neurons in the external germinal layer of the cerebellum and in ventricular zones) (at protein level). Expressed in spleen and testis. {ECO:0000269|PubMed:14618103, ECO:0000269|PubMed:9275178}. +E9Q5G3 KIF23_MOUSE Kinesin-like protein KIF23 953 108,776 Chain (1); Coiled coil (1); Cross-link (12); Domain (1); Modified residue (10); Motif (1); Nucleotide binding (1); Sequence conflict (1) FUNCTION: Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Essential for cytokinesis in Rho-mediated signaling. Required for the localization of ECT2 to the central spindle. Plus-end-directed motor enzyme that moves antiparallel microtubules in vitro (By similarity). {ECO:0000250}. PTM: Ubiquitinated. Deubiquitinated by USP8/UBPY (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Midbody, Midbody ring {ECO:0000269|PubMed:19020301}. Note=Localizes to the interzone of mitotic spindles (By similarity). Detected at the midbody during later stages of mitotic cytokinesis. {ECO:0000250}. SUBUNIT: Heterotetramer of two molecules each of RACGAP1 and KIF23. Found in the centralspindlin complex composed of RACGAP1 and KIF23. Interacts with RACGAP1; the interaction is direct. Interacts with ECT2 and PRC1. Interacts with ANXA11 during cytokinesis. Interacts with BIRC6/bruce and USP8/UBPY (By similarity). Interacts with ARF6, forming heterodimers and heterotetramers. {ECO:0000250, ECO:0000269|PubMed:22522702}. TISSUE SPECIFICITY: Detected in testis and ovary from newborn mice (at protein level). Detected in brain, spinal cord and small intestine. {ECO:0000269|PubMed:11416179, ECO:0000269|PubMed:19020301}. +Q8VEA4 MIA40_MOUSE Mitochondrial intermembrane space import and assembly protein 40 (Coiled-coil-helix-coiled-coil-helix domain-containing protein 4) 139 15,525 Chain (1); Compositional bias (1); Disulfide bond (3); Domain (1); Motif (2) FUNCTION: Functions as chaperone and catalyzes the formation of disulfide bonds in substrate proteins, such as COX17, COX19 and MICU1. Required for the import and folding of small cysteine-containing proteins (small Tim) in the mitochondrial intermembrane space (IMS). Precursor proteins to be imported into the IMS are translocated in their reduced form into the mitochondria. The oxidized form of CHCHD4/MIA40 forms a transient intermolecular disulfide bridge with the reduced precursor protein, resulting in oxidation of the precursor protein that now contains an intramolecular disulfide bond and is able to undergo folding in the IMS. Reduced CHCHD4/MIA40 is then reoxidized by GFER/ERV1 via a disulfide relay system. Mediates formation of disulfide bond in MICU1 in the IMS, promoting formation of the MICU1-MICU2 heterodimer that regulates mitochondrial calcium uptake. {ECO:0000250|UniProtKB:Q8N4Q1}. PTM: Forms intrachain disulfide bridges, but exists in different redox states. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion intermembrane space {ECO:0000250|UniProtKB:Q8N4Q1}. Mitochondrion {ECO:0000250|UniProtKB:Q8N4Q1}. SUBUNIT: Monomer. Can form homooligomers. Interacts with GFER and forms transient disulfide bonds with GFER. Interacts with MICU1. Interacts with COX19 forming transient intermolecular disulfide bridges. {ECO:0000250|UniProtKB:Q8N4Q1}. DOMAIN: The CHCH domain contains a conserved twin Cys-X(9)-Cys motif which is required for import and stability of MIA40 in mitochondria. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. Present at high level in liver and kidney, followed by lung, brain, heart and spleen (at protein level). {ECO:0000269|PubMed:16185709}. +Q7M6Z4 KIF27_MOUSE Kinesin-like protein KIF27 1394 158,956 Alternative sequence (2); Chain (1); Coiled coil (6); Compositional bias (1); Domain (1); Modified residue (8); Nucleotide binding (1); Sequence conflict (1) FUNCTION: Plays an essential role in motile ciliogenesis. {ECO:0000269|PubMed:19305393}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305|PubMed:19305393}. Cell projection, cilium {ECO:0000269|PubMed:19305393}. Note=Localizes to centrioles and basal bodies. SUBUNIT: Interacts with STK36. {ECO:0000269|PubMed:19305393}. +Q8K339 KIN17_MOUSE DNA/RNA-binding protein KIN17 (Binding to curved DNA) (KIN, antigenic determinant of recA protein) 391 44,722 Chain (1); Coiled coil (2); Modified residue (2); Region (3); Zinc finger (1) FUNCTION: Involved in DNA replication and the cellular response to DNA damage. May participate in DNA replication factories and create a bridge between DNA replication and repair mediated by high molecular weight complexes. May play a role in illegitimate recombination and regulation of gene expression. May participate in mRNA processing. Binds, in vitro, to double-stranded DNA. Also shown to bind preferentially to curved DNA in vitro and in vivo. Binds via its C-terminal domain to RNA in vitro. {ECO:0000250|UniProtKB:O60870, ECO:0000269|PubMed:15252136, ECO:0000269|PubMed:1923796, ECO:0000269|PubMed:8670903, ECO:0000269|PubMed:8954809}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15252136}. Cytoplasm {ECO:0000269|PubMed:15252136}. Note=During S phase, strongly associated with the nuclear matrix, and to chromosomal DNA in the presence of DNA damage. Also shows cytoplasmic localization in elongated spermatids. {ECO:0000250|UniProtKB:O60870, ECO:0000269|PubMed:15252136}. SUBUNIT: Associated with DNA polymerase alpha, RFC1 and cyclin A, in multiprotein DNA replication complexes. Also associates with replication origins at the G1/S phase boundary and throughout the S phase in vivo (By similarity). {ECO:0000250}. DOMAIN: The C-terminal domain (268-393) is organized into 2 subdomains that bear structural similarities to SH3-like domains. Both subdomains adopt a similar 5-stranded beta-barrel-like fold and are connected to each other by a short linker of 5 residues. The 5 beta-sheets are packed at approximately right angles against each other. A highly conserved groove formed at the interface between the 2 subdomains, comprised of Lys residues 302 and 391 and other positively charged residues, may possibly be the site of RNA-binding (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in transformed mouse AtT20 neuroendocrine cells. Expressed at a lower level in testis, kidney, skeletal muscle, liver, lung, spleen, brain and heart and kidney. In testis, expressed at much higher levels in proliferating cells than in differentiating cells. Not detected in embryo. {ECO:0000269|PubMed:15252136, ECO:0000269|PubMed:1923796, ECO:0000269|PubMed:8954809}. +Q80W68 KIRR1_MOUSE Kin of IRRE-like protein 1 (Kin of irregular chiasm-like protein 1) (Nephrin-like protein 1) 789 87,176 Alternative sequence (2); Chain (1); Disulfide bond (5); Domain (5); Erroneous initiation (1); Frameshift (1); Glycosylation (4); Modified residue (6); Motif (1); Mutagenesis (2); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 532 552 Helical. {ECO:0000255}. TOPO_DOM 48 531 Extracellular. {ECO:0000255}.; TOPO_DOM 553 789 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a significant role in the normal development and function of the glomerular permeability. Is a signaling protein that needs the presence of TEC kinases to fully trans-activate the transcription factor AP-1. {ECO:0000269|PubMed:11416156}. PTM: Phosphorylation probably regulates the interaction with NPHS2. Phosphorylated at Tyr-637 and Tyr-638 by FYN, leading to GRB2 binding (By similarity). {ECO:0000250}.; PTM: N-glycosylated. {ECO:0000269|PubMed:12660326, ECO:0000269|PubMed:19349973}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Predominantly located at podocyte slit diaphragm. SUBUNIT: Interacts with TJP1/ZO-1 and with NPHS2/podocin (via the C-terminus). Interacts with NPHS1/nephrin (via the Ig-like domains); this interaction is dependent on KIRREL1 glycosylation. Homodimer (via the Ig-like domains). Interacts when tyrosine-phosphorylated with GRB2 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Abundantly expressed in kidney. Specifically expressed in podocytes of kidney glomeruli. {ECO:0000269|PubMed:12865409}. +Q7TSU7 KIRR2_MOUSE Kin of IRRE-like protein 2 (Kin of irregular chiasm-like protein 2) 700 74,529 Alternative sequence (1); Chain (1); Disulfide bond (5); Domain (5); Glycosylation (3); Modified residue (4); Motif (1); Mutagenesis (3); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 508 528 Helical. {ECO:0000255}. TOPO_DOM 20 507 Extracellular. {ECO:0000255}.; TOPO_DOM 529 700 Cytoplasmic. {ECO:0000255}. FUNCTION: May regulate basal insulin secretion. {ECO:0000269|PubMed:26324709}. PTM: N-glycosylated. {ECO:0000269|PubMed:26324709}.; PTM: Phosphorylated at Ser-548 or Ser-549; due to site ambiguity, the exact position of the serine phosphorylation could not be determined. Phosphorylation at residues Tyr-631 and/or Tyr-632. FYN mediates tyrosine phosphorylation in pancreatic beta-cells. {ECO:0000269|PubMed:26324709}.; PTM: The extracellular domain is cleaved leading to the generation of a soluble fragment and a membrane-bound C-terminal fragment, which is further cleaved by gamma-secretase. {ECO:0000269|PubMed:26324709}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26324709}; Single-pass type I membrane protein {ECO:0000305}. Note=Localized along the sites of the cell contacts (PubMed:26324709). Colocalizes with E-Cadherin and beta-catenin (PubMed:26324709). {ECO:0000269|PubMed:26324709}. SUBUNIT: Homodimer (PubMed:26324709). Interacts with NPHS2/podocin (via the C-terminus). Interacts with NPHS1 (via the Ig-like domains). Interacts wit FYN (PubMed:26324709). {ECO:0000269|PubMed:12424224, ECO:0000269|PubMed:19887377, ECO:0000269|PubMed:26324709}. TISSUE SPECIFICITY: Highly expressed in beta-cells of the pancreatic islets. Expression is seen in podocytes of kidney glomeruli, and in the cerebellum and hindbrain at E12.5, in the spinal cord at E10.5, and in the retina and hypothalamus at E13.5. {ECO:0000269|PubMed:12424224, ECO:0000269|PubMed:12837264, ECO:0000269|PubMed:19887377}. +Q8BR86 KIRR3_MOUSE Kin of IRRE-like protein 3 (Kin of irregular chiasm-like protein 3) (Nephrin-like protein 2) (mKirre) [Cleaved into: Processed kin of IRRE-like protein 3] 778 85,405 Alternative sequence (5); Chain (2); Compositional bias (1); Disulfide bond (5); Domain (5); Glycosylation (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 536 556 Helical. {ECO:0000255}. TOPO_DOM 22 535 Extracellular. {ECO:0000255}.; TOPO_DOM 557 778 Cytoplasmic. {ECO:0000255}. FUNCTION: Synaptic adhesion molecule required for the formation of target-specific synapses (PubMed:23637329, PubMed:26575286). Required for formation of target-specific synapses at hippocampal mossy fiber synapses. Required for formation of mossy fiber filopodia, the synaptic structures connecting dentate granule and GABA neurons. Probably acts as a homophilic adhesion molecule that promotes trans-cellular interactions and stabilize mossy fiber filipodia contact and subsequent synapse formation (PubMed:26575286). Required for the coalescence of vomeronasal sensory neuron axons (PubMed:23637329). May be involved in the hematopoietic supportive capacity of stroma cells; the secreted extracellular domain is directly responsible for supporting hematopoietic stem cells (PubMed:12665856). {ECO:0000269|PubMed:12665856, ECO:0000269|PubMed:23637329, ECO:0000269|PubMed:26575286}. PTM: Undergoes proteolysis by a metalloprotease and gives rise to a soluble form. {ECO:0000269|PubMed:12665856, ECO:0000269|PubMed:15843475}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12665856}; Single-pass type I membrane protein {ECO:0000269|PubMed:12665856}. Cell projection, axon {ECO:0000269|PubMed:26575286}. Cell projection, dendrite {ECO:0000269|PubMed:26575286}.; SUBCELLULAR LOCATION: Processed kin of IRRE-like protein 3: Secreted {ECO:0000269|PubMed:12665856}. SUBUNIT: Homodimer; mediates homophilic interactions to promote cell adhesion (PubMed:26575286). Interacts with NPHS1; forms heterodimers with NPHS1 (PubMed:15843475, PubMed:18752272). Interacts with NPHS2/podocin (via the C-terminus) (By similarity). Interacts with CASK. Interacts (via extracellular region) with MAP1B. Interacts (via extracellular region) with MYO16. Interacts (via intracellular region) with ATP1B1. Interacts (via intracellular region) with SHMT2. Interacts (via intracellular region) with UFC1 (By similarity). {ECO:0000250|UniProtKB:Q8IZU9, ECO:0000269|PubMed:15843475, ECO:0000269|PubMed:18752272, ECO:0000269|PubMed:26575286}. TISSUE SPECIFICITY: Expressed mainly in adult brain, bone marrow and stromal cells (PubMed:12665856). Expressed in diverse regions of the brain, including the cortex, hippocampus, striatum, olfactory bulb and cerebellum (PubMed:15908127, PubMed:26283919). In brain, expressed in pontine nucleus neurons (at protein level) (PubMed:21241806). In hippocampus, produced in both the dentate granule neurons and the GABAergic neurons, but not the CA3 neurons (PubMed:26575286). Expressed in subpopulations of vomeronasal sensory neurons (PubMed:23637329). Expressed in a subset of neurons in dorsal root ganglia (PubMed:18752272). {ECO:0000269|PubMed:12665856, ECO:0000269|PubMed:15908127, ECO:0000269|PubMed:18752272, ECO:0000269|PubMed:21241806, ECO:0000269|PubMed:23637329, ECO:0000269|PubMed:26283919, ECO:0000269|PubMed:26575286}. +Q80X45 KISHB_MOUSE Protein kish-B (Transmembrane protein 167B) 74 8,308 Chain (1); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 53 73 Helical. {ECO:0000255}. TOPO_DOM 23 52 Extracellular. {ECO:0000255}.; TOPO_DOM 74 74 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in the early part of the secretory pathway. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. +Q9QWT9 KIFC1_MOUSE Kinesin-like protein KIFC1 674 74,153 Alternative sequence (2); Chain (1); Coiled coil (1); Domain (1); Frameshift (1); Modified residue (4); Nucleotide binding (1); Sequence conflict (33) FUNCTION: Minus end-directed microtubule-dependent motor required for bipolar spindle formation (PubMed:16638812). May contribute to movement of early endocytic vesicles (PubMed:17360972). Regulates cilium formation and structure (PubMed:23807208). {ECO:0000269|PubMed:16638812, ECO:0000269|PubMed:17360972, ECO:0000269|PubMed:23807208}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16638812, ECO:0000269|PubMed:17360972, ECO:0000269|PubMed:23807208}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:16638812, ECO:0000269|PubMed:17360972}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:16638812, ECO:0000269|PubMed:17360972}. Early endosome {ECO:0000269|PubMed:16638812, ECO:0000269|PubMed:17360972}. Note=Associated with nucleus during interphase, centrosomes in early and spindle in later mitosis. {ECO:0000269|PubMed:16638812, ECO:0000269|PubMed:17360972}. SUBUNIT: Binds NUBP1 and NUBP2 (PubMed:16638812). Interacts with PPP1R42 (PubMed:18237440). {ECO:0000269|PubMed:16638812, ECO:0000269|PubMed:18237440}. TISSUE SPECIFICITY: Highly expressed in E14 embryos, spleen and NIH3T3 cells. Also expressed in testis, brain, lung, kidney and cultured astrocytes. Very low levels in skeletal muscle and heart. {ECO:0000269|PubMed:16638812, ECO:0000269|PubMed:9115736}. +O08672 KIFC2_MOUSE Kinesin-like protein KIFC2 792 85,686 Chain (1); Coiled coil (1); Compositional bias (1); Domain (1); Nucleotide binding (1); Sequence conflict (3) FUNCTION: May play a role in microtubule-dependent retrograde axonal transport. May function as the motor for the transport of multivesicular body (MVB)-like organelles in dendrites. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. TISSUE SPECIFICITY: Present in axons and dendrites of neurons in the central and peripheral nervous systems. +O35231 KIFC3_MOUSE Kinesin-like protein KIFC3 824 92,556 Alternative sequence (2); Chain (1); Coiled coil (2); Domain (1); Erroneous initiation (2); Modified residue (2); Nucleotide binding (1); Sequence conflict (9) FUNCTION: Minus-end microtubule-dependent motor protein. Involved in apically targeted transport. Required for zonula adherens maintenance. {ECO:0000269|PubMed:11581287}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11581287}. Cytoplasmic vesicle membrane {ECO:0000305|PubMed:11581287}; Peripheral membrane protein {ECO:0000305|PubMed:11581287}. Cell junction, adherens junction {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Note=Localizes along zonula adherens only at mature cell-cell contacts (By similarity). Apical cell membrane. On membrane organelles immediately beneath the apical plasma membrane of renal tubular epithelial cells. Localized in the distal tubules and loops of Henle in the kidney, but not in the proximal tubules or the glomeruli, with stronger staining in the apical area of these epithelial cells. {ECO:0000250}. SUBUNIT: Interacts with annexin XIIIB. {ECO:0000269|PubMed:11581287}. TISSUE SPECIFICITY: Predominant expression in the kidney, testis and ovary. Also expressed in brain, heart, liver, lung and uterus. {ECO:0000269|PubMed:11581287}. +Q91W40 KLC3_MOUSE Kinesin light chain 3 508 56,006 Chain (1); Coiled coil (1); Compositional bias (2); Modified residue (4); Repeat (5); Sequence conflict (1) FUNCTION: Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:28003339, ECO:0000305|PubMed:11319135}. Note=In elongating spermatid tail midpiece, localized in outer dense fibers (ODFs) and associates with mitochondria (By similarity). Also localizes to the manchette in elongating spermatids (PubMed:28003339). {ECO:0000250|UniProtKB:Q68G30, ECO:0000269|PubMed:28003339}. SUBUNIT: Oligomer composed of two heavy chains and two light chains (By similarity). Associates with microtubulin in an ATP-dependent manner (By similarity). Interacts with KIF5C. Interacts with ODF1 (By similarity). Interacts with LRGUK (PubMed:28003339). {ECO:0000250|UniProtKB:Q68G30, ECO:0000269|PubMed:28003339}. DOMAIN: The heptad repeat (HR) motif is sufficient for interaction with kinesin heavy (KHL) chains and ODF1. The TPR region is involved in mitochondrial binding (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in postmeiotic male germ cells (at protein level). Expressed in spleen, intestine, brain, ovary, testis, spermatocytes and spermatids. {ECO:0000269|PubMed:11319135}. +Q6PAR0 KLD10_MOUSE Kelch domain-containing protein 10 439 49,012 Alternative sequence (2); Chain (1); Compositional bias (1); Erroneous initiation (2); Frameshift (1); Modified residue (1); Region (1); Repeat (6); Sequence conflict (4) FUNCTION: Participates in the oxidative stress-induced cell death through MAP3K5 activation. Inhibits PPP5C phosphatase activity on MAP3K5. {ECO:0000269|PubMed:23102700}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm {ECO:0000269|PubMed:23102700}. SUBUNIT: Interacts with CUL2, ELOB and ELOC; may be the substrate recognition component of an E3 ubiquitin ligase complex. Interacts (via the 6 Kelch repeats) with PPP5C. {ECO:0000269|PubMed:23102700}. +Q8VEM9 KLDC3_MOUSE Kelch domain-containing protein 3 (Protein Peas) (Testis intracellular mediator protein) 382 43,082 Chain (1); Natural variant (1); Repeat (5); Sequence conflict (4) FUNCTION: May be involved in meiotic recombination process. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12606021}. Note=Also found in meiotic chromatin. TISSUE SPECIFICITY: Expressed specifically in testis, particularly in pachytene spermatocytes. {ECO:0000269|PubMed:12606021}. +Q19A41 KLF14_MOUSE Krueppel-like factor 14 325 35,091 Chain (1); Zinc finger (3) SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +Q9EPW2 KLF15_MOUSE Krueppel-like factor 15 (Cardiovascular Krueppel-like factor) 415 44,253 Chain (1); Zinc finger (3) FUNCTION: Transcriptional regulator that binds to the GA element of the CLCNKA promoter (By similarity). Binds to the KCNIP2 promoter and regulates KCNIP2 circadian expression in the heart. Is a repressor of CTGF expression, involved in the control of cardiac fibrosis. Is also involved in the control of cardiac hypertrophy acting through the inhibition of MEF2A, GATA4 and MYOCD activity. Is a negative regulator of TP53 acetylation. Inhibits NF-kappa-B activation through repression of EP300-dependent RELA acetylation (By similarity). Involved in podocyte differentiation. {ECO:0000250, ECO:0000269|PubMed:17438289, ECO:0000269|PubMed:18586263, ECO:0000269|PubMed:20375365, ECO:0000269|PubMed:20566642, ECO:0000269|PubMed:22367544, ECO:0000269|PubMed:22493483, ECO:0000269|PubMed:23999430}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with MYOCD. Interacts with EP300 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in aortic smooth muscle cells. {ECO:0000269|PubMed:23999430}. +Q80TF4 KLH13_MOUSE Kelch-like protein 13 (BTB and kelch domain-containing protein 2) 654 73,787 Alternative sequence (4); Chain (1); Domain (2); Erroneous initiation (1); Repeat (6) Protein modification; protein ubiquitination. FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex required for mitotic progression and cytokinesis. The BCR(KLHL9-KLHL13) E3 ubiquitin ligase complex mediates the ubiquitination of AURKB and controls the dynamic behavior of AURKB on mitotic chromosomes and thereby coordinates faithful mitotic progression and completion of cytokinesis (By similarity). {ECO:0000250}. SUBUNIT: Component of the BCR(KLHL9-KLHL13) E3 ubiquitin ligase complex, at least composed of CUL3, KLHL9, KLHL13 and RBX1. Interacts with AURKB (By similarity). {ECO:0000250}. +Q60843 KLF2_MOUSE Krueppel-like factor 2 (Lung krueppel-like factor) 354 37,657 Chain (1); Compositional bias (3); Modified residue (3); Mutagenesis (2); Region (1); Sequence conflict (1); Zinc finger (3) FUNCTION: Transcription factor that binds to the CACCC box in the promoter of target genes such as HBB/beta globin or NOV and activates their transcription. {ECO:0000250|UniProtKB:Q9Y5W3}. PTM: Ubiquitinated. Polyubiquitination involves WWP1 and leads to proteasomal degradation of this protein. {ECO:0000269|PubMed:15003522}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with WWP1. {ECO:0000269|PubMed:11375995, ECO:0000269|PubMed:15003522}. TISSUE SPECIFICITY: Predominant expression in the lungs and spleen. +Q8BWA5 KLH31_MOUSE Kelch-like protein 31 (Kelch repeat and BTB domain-containing protein 1) (Kelch-like protein KLHL) 634 70,181 Chain (1); Domain (2); Initiator methionine (1); Modified residue (1); Repeat (6) FUNCTION: Transcriptional repressor in MAPK/JNK signaling pathway to regulate cellular functions. Overexpression inhibits the transcriptional activities of both the TPA-response element (TRE) and serum response element (SRE) (By similarity). {ECO:0000250}. PTM: N-terminus is methylated by METTL11A/NTM1. {ECO:0000269|PubMed:20668449}. +Q99JN2 KLH22_MOUSE Kelch-like protein 22 634 71,687 Alternative sequence (1); Chain (1); Domain (1); Initiator methionine (1); Modified residue (5); Repeat (6); Sequence conflict (2) Protein modification; protein ubiquitination. FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex required for chromosome alignment and localization of PLK1 at kinetochores. The BCR(KLHL22) ubiquitin ligase complex mediates monoubiquitination of PLK1, leading to PLK1 dissociation from phosphoreceptor proteins and subsequent removal from kinetochores, allowing silencing of the spindle assembly checkpoint (SAC) and chromosome segregation. Monoubiquitination of PLK1 does not lead to PLK1 degradation (By similarity). The BCR(KLHL22) ubiquitin ligase complex is also responsible for the amino acid-stimulated 'Lys-48' polyubiquitination and proteasomal degradation of DEPDC5. Through the degradation of DEPDC5, releases the GATOR1 complex-mediated inhibition of the TORC1 pathway. It is therefore an amino acid-dependent activator within the amino acid-sensing branch of the TORC1 pathway, indirectly regulating different cellular processes including cell growth and autophagy (PubMed:29769719). {ECO:0000250|UniProtKB:Q53GT1, ECO:0000269|PubMed:29769719}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q53GT1}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q53GT1}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q53GT1}. Nucleus {ECO:0000250|UniProtKB:Q53GT1}. Lysosome {ECO:0000250|UniProtKB:Q53GT1}. Note=Mainly cytoplasmic in prophase and prometaphase. Associates with the mitotic spindle as the cells reach chromosome bi-orientation. Localizes to the centrosomes shortly before cells enter anaphase After anaphase onset, predominantly associates with the polar microtubules connecting the 2 opposing centrosomes and gradually diffuses into the cytoplasm during telophase. Localizes to the nucleus upon amino acid starvation. Relocalizes to the cytosol and associates with lysosomes when amino acids are available. {ECO:0000250|UniProtKB:Q53GT1}. SUBUNIT: Component of the BCR(KLHL22) E3 ubiquitin ligase complex, at least composed of CUL3, KLHL22 and RBX1. Interacts with PLK1. Interacts with DEPDC5 (via DEP domain); the interaction depends on amino acid availability. Interacts with YWHAE; required for the nuclear localization of KLHL22 upon amino acid starvation. {ECO:0000250|UniProtKB:Q53GT1}. +Q9Z0Z7 KLF5_MOUSE Krueppel-like factor 5 (Basic transcription element-binding protein 2) (BTE-binding protein 2) (Intestinal-enriched krueppel-like factor) (Transcription factor BTEB2) 446 49,754 Chain (1); Cross-link (4); Region (1); Sequence conflict (1); Zinc finger (3) FUNCTION: Transcription factor that binds to GC box promoter elements. Activates the transcription of these genes. PTM: Ubiquitinated (By similarity). Polyubiquitination involves WWP1 and leads to proteasomal degradation of this protein. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with WWP1. {ECO:0000250}. TISSUE SPECIFICITY: Highest expression in digestive track. +Q8BLM0 KLF8_MOUSE Krueppel-like factor 8 355 38,845 Chain (1); Cross-link (1); Zinc finger (3) FUNCTION: Transcriptional repressor and activator. Binds to CACCC-boxes promoter elements. Also binds the GT-box of cyclin D1 promoter and mediates cell cycle progression at G(1) phase as a downstream target of focal adhesion kinase (FAK) (By similarity). {ECO:0000250}. PTM: Sumoylation at Lys-64 represses transcriptional activity and reduces cell cycle progression into the G(1) phase. Has no effect on subcellular location. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with corepressor CtBP2. Interacts with PIAS1, PIAS2, AND PIAS4; the interaction with each ligase sumoylates KLF8 (By similarity). {ECO:0000250}. +Q8CE33 KLH11_MOUSE Kelch-like protein 11 709 80,429 Alternative sequence (1); Chain (1); Domain (2); Frameshift (1); Modified residue (1); Repeat (5); Signal peptide (1) FUNCTION: Component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex that mediates the ubiquitination of target proteins, leading most often to their proteasomal degradation. {ECO:0000250}. SUBUNIT: Homodimer. Interacts with CUL3. Component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex (By similarity). {ECO:0000250}. +E0CZ16 KLHL3_MOUSE Kelch-like protein 3 587 64,922 Alternative sequence (1); Chain (1); Domain (2); Modified residue (4); Repeat (6) Protein modification; protein ubiquitination. FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a regulator of ion transport in the distal nephron (PubMed:25831548, PubMed:28052936). The BCR(KLHL3) complex acts by mediating ubiquitination of WNK4, an inhibitor of potassium channel KCNJ1, leading to WNK4 degradation (By similarity). The BCR(KLHL3) complex also mediates ubiquitination and degradation of CLDN8, a tight-junction protein required for paracellular chloride transport in the kidney (PubMed:25831548). {ECO:0000250|UniProtKB:Q9UH77, ECO:0000269|PubMed:25831548, ECO:0000269|PubMed:28052936}. PTM: Phosphorylation at Ser-433 by PKA decreases the interaction with WNK4, Leading to inhibit WNK4 degradation by the BCR(KLHL3) complex. Phosphorylation at Ser-433 is increased by insulin. {ECO:0000250|UniProtKB:Q9UH77}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9UH77}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9UH77}. SUBUNIT: Homodimer. Component of the BCR(KLHL3) E3 ubiquitin ligase complex, at least composed of CUL3 and KLHL3 and RBX1 (By similarity). Interacts with SLC12A3 (By similarity). Interacts with WNK1 and WNK4 (By similarity). Interacts with CLDN8 (PubMed:25831548). {ECO:0000250|UniProtKB:Q9UH77, ECO:0000269|PubMed:25831548}. TISSUE SPECIFICITY: Present at high level in brain and kidney (at protein level) (PubMed:28052936). Weakly expressed in other tissues (PubMed:28052936). In kidney, predominantly localizes to the distal convoluted tubule (DCT) and collecting duct, with apical localization in the DCT (at protein level) (PubMed:22266938, PubMed:22406640). {ECO:0000269|PubMed:22266938, ECO:0000269|PubMed:22406640, ECO:0000269|PubMed:28052936}. +Q99N32 KLOTB_MOUSE Beta-klotho (BKL) (BetaKlotho) (Klotho beta-like protein) 1043 120,189 Alternative sequence (2); Chain (1); Erroneous initiation (1); Glycosylation (12); Region (2); Topological domain (2); Transmembrane (1) TRANSMEM 995 1015 Helical. {ECO:0000255}. TOPO_DOM 1 994 Extracellular. {ECO:0000255}.; TOPO_DOM 1016 1043 Cytoplasmic. {ECO:0000255}. FUNCTION: Contributes to the transcriptional repression of cholesterol 7-alpha-hydroxylase (CYP7A1), the rate-limiting enzyme in bile acid synthesis. Probably inactive as a glycosidase. Increases the ability of FGFR1 and FGFR4 to bind FGF21. {ECO:0000269|PubMed:16075061, ECO:0000269|PubMed:17452648}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type III membrane protein {ECO:0000305}. SUBUNIT: Interacts with FGF19; this interaction is direct. Interacts (via C-terminus) with FGF21; this interaction is direct (By similarity). Interacts with FGFR1 and FGFR4. {ECO:0000250, ECO:0000269|PubMed:17452648}. DOMAIN: Contains 2 glycosyl hydrolase 1 regions. However, the first region lacks the essential Glu active site residue at position 241, and the second one lacks the essential Glu active site residue at position 887. These domains are therefore predicted to be inactive. TISSUE SPECIFICITY: Present in liver, muscle and white adipose tissue, but not in kidney (at protein level). Expressed in liver and pancreas, and at lower levels in skin, stomach, skeletal muscle, small intestine and lung. {ECO:0000269|PubMed:11044614, ECO:0000269|PubMed:16075061, ECO:0000269|PubMed:17452648}. +Q9Z0M1 KLK4_MOUSE Kallikrein-4 (EC 3.4.21.-) (Enamel matrix serine proteinase 1) (Kallikrein-like protein 1) (Serine protease 17) 255 27,488 Active site (3); Chain (1); Disulfide bond (4); Domain (1); Glycosylation (2); Metal binding (2); Propeptide (1); Sequence conflict (2); Signal peptide (1) FUNCTION: Has a major role in enamel formation. Required during the maturation stage of tooth development for clearance of enamel proteins and normal structural patterning of the crystalline matrix. {ECO:0000269|PubMed:19578120}. PTM: N-glycosylated. The N-glycan structures are of complex diantennary or triantennary type, which may be further modified with up to 2 sialic acid residues. {ECO:0000269|PubMed:22243251}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +P20937 KLRA1_MOUSE T-cell surface glycoprotein YE1/48 (Lymphocyte antigen 49a) (Ly-49a) (T lymphocyte antigen A1) 262 30,498 Beta strand (7); Chain (1); Disulfide bond (4); Domain (1); Glycosylation (3); Helix (4); Motif (1); Sequence conflict (5); Topological domain (2); Transmembrane (1) TRANSMEM 45 66 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 44 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 67 262 Extracellular. {ECO:0000305}. FUNCTION: Receptor on natural killer (NK) cells for H-2d alleles. Inhibits the activity of NK cells thus preventing cell lysis. SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:10604468}. TISSUE SPECIFICITY: High, in T-lymphoma lines, very low in normal lymphocytes. +Q60651 KLRA4_MOUSE Killer cell lectin-like receptor 4 (Lymphocyte antigen 49d) (Ly-49d) (T-cell surface glycoprotein Ly-49D) 263 30,872 Alternative sequence (1); Chain (1); Disulfide bond (4); Domain (1); Glycosylation (4); Natural variant (9); Topological domain (2); Transmembrane (1) TRANSMEM 45 65 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 44 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 66 263 Extracellular. {ECO:0000255}. FUNCTION: Receptor on natural killer (NK) cells for class I MHC. SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. SUBUNIT: Homodimer; disulfide-linked. +Q91VE3 KLK7_MOUSE Kallikrein-7 (EC 3.4.21.117) (Serine protease 6) (Stratum corneum chymotryptic enzyme) (Thymopsin) 249 27,257 Active site (3); Beta strand (14); Chain (1); Disulfide bond (6); Helix (5); Propeptide (1); Region (1); Sequence conflict (1); Signal peptide (1); Site (1); Turn (1) FUNCTION: May catalyze the degradation of intercellular cohesive structures in the cornified layer of the skin in the continuous shedding of cells from the skin surface. Specific for amino acid residues with aromatic side chains in the P1 position. Cleaves insulin A chain at '14-Tyr-|-Gln-15' and insulin B chain at '6-Leu-|-Cys-7', '16-Tyr-|-Leu-17', '25-Phe-|-Tyr-26' and '26-Tyr-|-Thr-27'. Could play a role in the activation of precursors to inflammatory cytokines. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. TISSUE SPECIFICITY: Expressed in skin and, at lower levels, in lung, kidney, brain, heart and spleen. In skin, expressed in high suprabasal keratinocytes and in the luminal parts of hair follicles. Not detected in liver and skeletal muscle. {ECO:0000269|PubMed:10469296}. +O54707 KLRD1_MOUSE Natural killer cells antigen CD94 (Killer cell lectin-like receptor subfamily D member 1) (CD antigen CD94) 179 20,808 Chain (1); Disulfide bond (5); Domain (1); Glycosylation (2); Natural variant (1); Topological domain (2); Transmembrane (1) TRANSMEM 11 31 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 10 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 32 179 Extracellular. {ECO:0000255}. FUNCTION: Plays a role as a receptor for the recognition of MHC class I HLA-E molecules by NK cells and some cytotoxic T-cells. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. SUBUNIT: Can form disulfide-bonded heterodimer with NKG2 family members. {ECO:0000250}. +P26262 KLKB1_MOUSE Plasma kallikrein (EC 3.4.21.34) (Fletcher factor) (Kininogenin) (Plasma prekallikrein) [Cleaved into: Plasma kallikrein heavy chain; Plasma kallikrein light chain] 638 71,383 Active site (3); Beta strand (14); Chain (2); Disulfide bond (18); Domain (5); Glycosylation (5); Helix (7); Sequence conflict (1); Signal peptide (1) FUNCTION: The enzyme cleaves Lys-Arg and Arg-Ser bonds. It activates, in a reciprocal reaction, factor XII after its binding to a negatively charged surface. It also releases bradykinin from HMW kininogen and may also play a role in the renin-angiotensin system by converting prorenin into renin. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Forms a heterodimer with SERPINA5. The zymogen is activated by factor XIIa, which cleaves the molecule into a light chain, which contains the active site, and a heavy chain, which associates with HMW kininogen. These chains are linked by one or more disulfide bonds (By similarity). {ECO:0000250}. +O88713 KLRG1_MOUSE Killer cell lectin-like receptor subfamily G member 1 (Mast cell function-associated antigen 2F1) 188 21,396 Beta strand (6); Chain (1); Disulfide bond (3); Domain (1); Glycosylation (2); Helix (2); Motif (1); Mutagenesis (4); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 34 56 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 33 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 57 188 Extracellular. {ECO:0000255}. FUNCTION: Plays an inhibitory role on natural killer (NK) cells and T-cell functions upon binding to their non-MHC ligands. May mediate missing self recognition by binding to a highly conserved site on classical cadherins, enabling it to monitor expression of E-cadherin/CDH1, N-cadherin/CDH2 and R-cadherin/CDH4 on target cells. {ECO:0000269|PubMed:19604491}. PTM: Phosphorylated in response to monoclonal antibody G63 binding and antigenic stimulation. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19604491}; Single-pass type II membrane protein {ECO:0000269|PubMed:19604491}. SUBUNIT: Forms a monomer and homodimer; disulfide-linked (By similarity). Interacts (via ITIM motif) with PTPN11 and INPP5D. {ECO:0000250, ECO:0000269|PubMed:17307799, ECO:0000269|PubMed:19604491}. DOMAIN: Contains 1 copy of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is involved in modulation of cellular responses. Upon phosphorylation of ITIM motif KLRG1 associates with the two phosphatases, PTPN11 and INPP5D. TISSUE SPECIFICITY: Expressed specifically on natural killer (NK) cells and activated CD8 T-cells. Not detected in spleen, thymus, lymph node, testis, brain or kidney. Not detected on mast cell lines, bone marrow-derived mast cells, or peritoneal mast cells. {ECO:0000269|PubMed:9862378, ECO:0000269|PubMed:9862665}. +Q3UM83 KLRG2_MOUSE Killer cell lectin-like receptor subfamily G member 2 387 41,831 Chain (1); Disulfide bond (2); Domain (1); Modified residue (1); Sequence conflict (1); Transmembrane (1) TRANSMEM 241 261 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +P01794 HVM25_MOUSE Ig heavy chain V region HPCG14 123 13,807 Chain (1); Domain (1); Non-terminal residue (1) +P01797 HVM28_MOUSE Ig heavy chain V-III region U61 113 12,671 Chain (1); Disulfide bond (1); Domain (1); Non-terminal residue (1) +P09026 HXB3_MOUSE Homeobox protein Hox-B3 (Homeobox protein Hox-2.7) (Homeobox protein MH-23) 433 44,353 Chain (1); Compositional bias (1); DNA binding (1); Motif (1); Sequence conflict (9) FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. SUBCELLULAR LOCATION: Nucleus. +P52792 HXK4_MOUSE Glucokinase (EC 2.7.1.2) (Hexokinase type IV) (HK IV) (Hexokinase-4) (HK4) (Hexokinase-D) 465 52,089 Alternative sequence (1); Binding site (5); Chain (1); Domain (1); Nucleotide binding (4); Region (5); Sequence conflict (2) FUNCTION: Catalyzes the initial step in utilization of glucose by the beta-cell and liver at physiological glucose concentration. Pancreatic glucokinase plays an important role in modulating insulin secretion. Hepatic glucokinase helps to facilitate the uptake and conversion of glucose by acting as an insulin-sensitive determinant of hepatic glucose usage. {ECO:0000250|UniProtKB:P35557}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24187134}. Nucleus {ECO:0000250|UniProtKB:P35557}. Note=Under low glucose concentrations, GCK associates with GKRP and the inactive complex is recruited to the hepatocyte nucleus. {ECO:0000250|UniProtKB:P35557}. SUBUNIT: Monomer. Interacts with MIDN; the interaction occurs preferentially at low glucose levels and results in inhibition of GCK activity. {ECO:0000250|UniProtKB:P17712, ECO:0000250|UniProtKB:P35557}. TISSUE SPECIFICITY: Isoform 1: Pancreas, anterior pituitary. Isoform 2: Liver. +Q9CXX0 HYLS1_MOUSE Hydrolethalus syndrome protein 1 homolog 307 35,141 Chain (1); Erroneous initiation (1); Frameshift (1) FUNCTION: Plays a role in ciliogenesis. {ECO:0000250|UniProtKB:A0A1L8ER70, ECO:0000250|UniProtKB:Q95X94}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96M11}. Cell projection, cilium {ECO:0000250|UniProtKB:A0A1L8ER70, ECO:0000250|UniProtKB:Q95X94}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:A0A1L8ER70, ECO:0000250|UniProtKB:Q95X94}. TISSUE SPECIFICITY: Expressed in hippocampus and dentate gyrus of 3-month adult brain. {ECO:0000269|PubMed:15843405}. +Q9Z2B1 I18RA_MOUSE Interleukin-18 receptor accessory protein (IL-18 receptor accessory protein) (IL-18RAcP) (Accessory protein-like) (AcPL) (CD218 antigen-like family member B) (IL-1R accessory protein-like) (IL-1RAcPL) (Interleukin-18 receptor accessory protein-like) (Interleukin-18 receptor beta) (IL-18R-beta) (IL-18Rbeta) (CD antigen CD218b) 614 70,094 Chain (1); Disulfide bond (5); Domain (3); Glycosylation (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 357 377 Helical. {ECO:0000255}. TOPO_DOM 20 356 Extracellular. {ECO:0000255}.; TOPO_DOM 378 614 Cytoplasmic. {ECO:0000255}. FUNCTION: Within the IL18 receptor complex, does not mediate IL18-binding, but involved in IL18-dependent signal transduction, leading to NF-kappa-B and JNK activation (PubMed:11046021, PubMed:15843532, PubMed:9792649). May play a role in IL18-mediated IFNG synthesis from T-helper 1 (Th1) cells (By similarity). {ECO:0000250|UniProtKB:O95256, ECO:0000269|PubMed:11046021, ECO:0000269|PubMed:15843532, ECO:0000269|PubMed:9792649}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O95256}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Forms a ternary complex with IL18 and IL18R1. Within this complex, IL18R1 is involved in ligand-binding and IL18RAP in signaling leading to NF-kappa-B and JNK activation. {ECO:0000250|UniProtKB:O95256}. +Q60837 I12R1_MOUSE Interleukin-12 receptor subunit beta-1 (IL-12 receptor subunit beta-1) (IL-12R subunit beta-1) (IL-12R-beta-1) (IL-12 receptor beta component) (CD antigen CD212) 738 81,788 Chain (1); Compositional bias (1); Disulfide bond (1); Domain (5); Glycosylation (13); Motif (2); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 566 591 Helical. {ECO:0000255}. TOPO_DOM 20 565 Extracellular. {ECO:0000255}.; TOPO_DOM 592 738 Cytoplasmic. {ECO:0000255}. FUNCTION: Functions as an interleukin receptor which binds interleukin-12 with low affinity and is involved in IL12 transduction. Associated with IL12RB2 it forms a functional, high affinity receptor for IL12. Associates also with IL23R to form the interleukin-23 receptor which functions in IL23 signal transduction probably through activation of the Jak-Stat signaling cascade. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Dimer or oligomer; disulfide-linked. Interacts with IL12RB2 to form the high affinity IL12 receptor. Heterodimer with IL23R; in presence of IL23. The heterodimer forms the IL23 receptor (By similarity). {ECO:0000250}. DOMAIN: The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.; DOMAIN: The box 1 motif is required for JAK interaction and/or activation. +Q9CR04 HYPM_MOUSE Huntingtin-interacting protein M (Huntingtin yeast partner M) 117 13,492 Chain (1) SUBUNIT: May interact with the N-terminus of HD. {ECO:0000250}. +Q3UTA9 I4E1B_MOUSE Eukaryotic translation initiation factor 4E type 1B (Oocyte-specific eukaryotic translation initiation factor 4E-like) 244 27,985 Alternative sequence (2); Chain (1); Region (7) FUNCTION: Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures. {ECO:0000250}. SUBUNIT: EIF4F is a multi-subunit complex, the composition of which varies with external and internal environmental conditions. It is composed of at least EIF4A, EIF4E AND EIF4G (By similarity). {ECO:0000250}. +Q60819 I15RA_MOUSE Interleukin-15 receptor subunit alpha (IL-15 receptor subunit alpha) (IL-15R-alpha) (IL-15RA) (CD antigen CD215) [Cleaved into: Soluble interleukin-15 receptor subunit alpha (sIL-15 receptor subunit alpha) (sIL-15R-alpha) (sIL-15RA)] 263 28,061 Alternative sequence (7); Beta strand (5); Chain (2); Disulfide bond (2); Domain (1); Glycosylation (1); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 206 226 Helical. {ECO:0000255}. TOPO_DOM 33 205 Extracellular. {ECO:0000255}.; TOPO_DOM 227 263 Cytoplasmic. {ECO:0000255}. FUNCTION: High-affinity receptor for interleukin-15. Can signal both in cis and trans where IL15R from one subset of cells presents IL15 to neighboring IL2RG-expressing cells. Signal transduction involves SYK (By similarity). {ECO:0000250, ECO:0000269|PubMed:12734349, ECO:0000269|PubMed:17947230}. PTM: Phosphorylated by activated SYK. {ECO:0000250}.; PTM: N-glycosylated and O-glycosylated. {ECO:0000250}.; PTM: A soluble form (sIL-15RA) arises from proteolytic shedding of the membrane-anchored receptor. The cleavage involves ADAM17/TACE. It also binds IL15 and thus interferes with IL15 binding to the membrane receptor (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: Soluble interleukin-15 receptor subunit alpha: Secreted, extracellular space {ECO:0000250}. SUBUNIT: The interleukin-15 receptor IL15R is a heterotrimer of IL15RA, IL2RB and IL2RG. IL15RA also self-associates. Interacts with SYK (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12885940, ECO:0000269|PubMed:7641685}. +Q6PHB0 I20RA_MOUSE Interleukin-20 receptor subunit alpha (IL-20 receptor subunit alpha) (IL-20R-alpha) (IL-20RA) (IL-20R1) 546 61,978 Chain (1); Disulfide bond (2); Domain (2); Glycosylation (5); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 254 274 Helical. {ECO:0000255}. TOPO_DOM 33 253 Extracellular. {ECO:0000255}.; TOPO_DOM 275 546 Cytoplasmic. {ECO:0000255}. FUNCTION: The IL20RA/IL20RB dimer is a receptor for IL19, IL20 and IL24. The IL20RA/IL10RB dimer is a receptor for IL26 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Heterodimer with IL20RB and heterodimer with IL10RB. {ECO:0000250}. +P47876 IBP1_MOUSE Insulin-like growth factor-binding protein 1 (IBP-1) (IGF-binding protein 1) (IGFBP-1) 272 29,570 Chain (1); Disulfide bond (5); Domain (2); Modified residue (6); Motif (1); Sequence conflict (3); Signal peptide (1) FUNCTION: IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. Promotes cell migration (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Binds equally well IGF1 and IGF2. +Q60943 I17RA_MOUSE Interleukin-17 receptor A (IL-17 receptor A) (IL-17RA) (CD antigen CD217) 864 97,808 Chain (1); Compositional bias (1); Disulfide bond (5); Domain (1); Glycosylation (7); Modified residue (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 323 343 Helical. {ECO:0000255}. TOPO_DOM 32 322 Extracellular. {ECO:0000255}.; TOPO_DOM 344 864 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for IL17A (PubMed:17911633, PubMed:20554964, PubMed:8777726). Receptor for IL17F (PubMed:17911633, PubMed:20554964). Binds to IL17A with higher affinity than to IL17F (PubMed:17911633). Binds IL17A and IL17F homodimers as part of a heterodimeric complex with IL17RC (By similarity). Also binds heterodimers formed by IL17A and IL17F as part of a heterodimeric complex with IL17RC (By similarity). Receptor for IL17C as part of a heterodimeric complex with IL17RE (PubMed:21993848, PubMed:21993849, PubMed:21982598). Activation of IL17RA leads to induction of expression of inflammatory chemokines and cytokines such as CXCL1, CXCL8/IL8 and IL6 (By similarity). {ECO:0000250|UniProtKB:Q96F46, ECO:0000269|PubMed:17911633, ECO:0000269|PubMed:20554964, ECO:0000269|PubMed:21982598, ECO:0000269|PubMed:21993848, ECO:0000269|PubMed:21993849, ECO:0000269|PubMed:8777726}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17911633}; Single-pass type I membrane protein {ECO:0000255}. SUBUNIT: Forms heterodimers with IL17RE; the heterodimer binds IL17C (PubMed:21993848). Forms heterodimers with IL17RC; the heterodimer binds IL17A and IL17F homodimers as well as the heterodimer formed by IL17A and IL17F (PubMed:20554964). {ECO:0000269|PubMed:20554964, ECO:0000269|PubMed:21993848}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:21993848}. +Q8BMF3 MAON_MOUSE NADP-dependent malic enzyme, mitochondrial (NADP-ME) (EC 1.1.1.40) (Malic enzyme 3) 604 67,098 Active site (2); Binding site (3); Chain (1); Metal binding (3); Modified residue (1); Sequence conflict (2); Site (1); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. +Q9Z2E1 MBD2_MOUSE Methyl-CpG-binding domain protein 2 (Methyl-CpG-binding protein MBD2) 414 43,501 Alternative sequence (2); Chain (1); Compositional bias (2); Domain (1); Modified residue (2); Sequence conflict (5) FUNCTION: Binds CpG islands in promoters where the DNA is methylated at position 5 of cytosine within CpG dinucleotides. Binds hemimethylated DNA as well. Recruits histone deacetylases and DNA methyltransferases. Acts as transcriptional repressor and plays a role in gene silencing. Functions as a scaffold protein, targeting GATAD2A and GATAD2B to chromatin to promote repression (By similarity). May enhance the activation of some unmethylated cAMP-responsive promoters (By similarity). Selectively represses transcription activity of methylated rRNA promoters. {ECO:0000250, ECO:0000269|PubMed:14610093, ECO:0000269|PubMed:9774669}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Nuclear, in discrete foci. Detected at replication foci in late S phase (By similarity). {ECO:0000250}. SUBUNIT: Heterodimer with MBD3. Component of the MeCP1 complex that contains HDAC1 and HDAC2. Binds DNMT1, MIZF, GPN1, SIN3A, GATAD2A/p66-alpha and GATAD2B/p66-beta (By similarity). Interacts with DHX9 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in brain, heart, kidney, lung, skeletal muscle, spleen and testis. Detected at lower levels in embryonic stem cells. {ECO:0000269|PubMed:9774669}. +Q9Z2D7 MBD4_MOUSE Methyl-CpG-binding domain protein 4 (EC 3.2.2.-) (Methyl-CpG-binding protein MBD4) (Mismatch-specific DNA N-glycosylase) 554 62,578 Active site (1); Beta strand (3); Chain (1); Domain (1); Helix (13); Modified residue (2); Sequence conflict (1); Turn (1) FUNCTION: Mismatch-specific DNA N-glycosylase involved in DNA repair. Has thymine glycosylase activity and is specific for G:T mismatches within methylated and unmethylated CpG sites. Can also remove uracil or 5-fluorouracil in G:U mismatches. Has no lyase activity. Was first identified as methyl-CpG-binding protein. {ECO:0000269|PubMed:9774669}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9774669}. Note=Nuclear, in discrete foci. SUBUNIT: Interacts with MLH1. {ECO:0000250}. +Q3TY92 MBD6_MOUSE Methyl-CpG-binding domain protein 6 (Methyl-CpG-binding protein MBD6) 1003 100,990 Chain (1); Compositional bias (2); Domain (1); Sequence conflict (1) FUNCTION: Binds to heterochromatin. Does not interact with either methylated or unmethylated DNA (in vitro) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}. Note=Associated with pericentric heterochromatin in about 25% of the cells. {ECO:0000250}. DOMAIN: The MBD domain is necessary for chromocentric localization. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. Expressed at highest levels in adult testis and brain. {ECO:0000269|PubMed:20700456}. +Q7TT79 MCPH1_MOUSE Microcephalin 822 90,373 Chain (1); Domain (3); Erroneous initiation (1); Modified residue (4); Sequence conflict (1) FUNCTION: Implicated in chromosome condensation and DNA damage induced cellular responses. May play a role in neurogenesis and regulation of the size of the cerebral cortex (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. SUBUNIT: Interacts with CDC27 and maybe other components of the APC/C complex. Interacts with histone variant H2AFX under DNA damage conditions (By similarity). {ECO:0000250}. DOMAIN: BRCT domain 1 is required to prevent abnormal chromosome condensation. It binds directly to the SWI-SNF chromatin remodeling complex (By similarity). {ECO:0000250}.; DOMAIN: BRCT domains 2 and 3 recognize phosphoserine/phosphothreonine marks on proteins with high selectivity, and mediate interaction with phosphorylated CDC27. They also mediate the dual recognition of phosphoserine and phosphotyrosine in the C-terminal tail of histone H2AFX (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: High levels of expression are found in the developing forebrain and, in particular, in the walls of the lateral ventricles. {ECO:0000269|PubMed:12046007}. +Q9D8C4 IN35_MOUSE Interferon-induced 35 kDa protein homolog (IFP 35) (Ifi-35) 286 31,876 Chain (1); Region (1); Sequence conflict (1) SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Nuclear following IFN treatment. {ECO:0000250}. SUBUNIT: Homodimer. Also interacts with B-ATF (By similarity). {ECO:0000250}. +Q9ESK4 ING2_MOUSE Inhibitor of growth protein 2 (Inhibitor of growth 1-like protein) (p33ING2) 281 32,978 Beta strand (3); Binding site (4); Chain (1); Coiled coil (1); Cross-link (1); Helix (2); Metal binding (8); Region (1); Sequence caution (1); Sequence conflict (8); Turn (1); Zinc finger (1) FUNCTION: Seems to be involved in p53/TP53 activation and p53/TP53-dependent apoptotic pathways, probably by enhancing acetylation of p53/TP53. Component of a mSin3A-like corepressor complex, which is probably involved in deacetylation of nucleosomal histones. ING2 activity seems to be modulated by binding to phosphoinositides (PtdInsPs) (By similarity). {ECO:0000250}. PTM: Sumoylation enhances its association with SIN3A and is required for binding to some target gene promoters, this is the case for TMEM71. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Predominantly cytoplasmic. Localized to chromatin and nuclear matrix. Upon reduced PtdIns(5)P levels seems to be released from chromatin and, at least partially, translocated to the cytoplasm (By similarity). {ECO:0000250}. SUBUNIT: Interacts with H3K4me3 and to a lesser extent with H3K4me2. Component of a mSin3A-like complex at least consisting of SIN3A, HDAC1, HDAC2, RBBP4/RbAp48, RBBP7/RbAp46, SAP30 and ING2. {ECO:0000250}. DOMAIN: The PHD-type zinc finger mediates the binding to H3K4me3. {ECO:0000250}.; DOMAIN: The polybasic region (PBR) is responsive to the binding to phosphoinositides (PtdInsPs), including phosphatidylinositol 5-phosphate (PtdIns(5)P). {ECO:0000250}. +Q6PKN7 INCA1_MOUSE Protein INCA1 (Inhibitor of CDK interacting with cyclin A1) 231 26,477 Alternative sequence (1); Chain (1); Modified residue (1); Motif (1); Region (1) FUNCTION: Binds to CDK2-bound cyclins and inhibits the kinase activity of CDK2; binding to cyclins is critical for its function as CDK inhibitor. Inhibits cell growth and proliferation and may play a role in cell cycle control (PubMed:21540187). Required for ING5-mediated regulation of S-phase progression, enhancement of Fas-induced apoptosis and inhibition of cell growth (PubMed:21750715). {ECO:0000269|PubMed:21540187, ECO:0000269|PubMed:21750715}. PTM: Phosphorylated when part of a complex with CCNA1 and CDK2. {ECO:0000250|UniProtKB:Q0VD86}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q0VD86}. Cytoplasm {ECO:0000250|UniProtKB:Q0VD86}. SUBUNIT: Interacts with CCNA1 (PubMed:21540187). Identified in a complex with CCNA1 and CDK2 (By similarity). Interacts with ZNF16; the interaction inhibits INCA1 activity and induces the cell cycle process (By similarity). Interacts with SPACA9 (By similarity). Interacts with CCNA2, CCNB1 and CCNE1 (By similarity). Interacts with the CCNA1/CDK2 complex (PubMed:21540187). Interacts with ING5, DAZAP2, RNF26, USP15, SPOUT1, DPH7, TRIM26 and RAB5C (By similarity). {ECO:0000250|UniProtKB:Q0VD86, ECO:0000269|PubMed:21540187}. +Q8VEK6 ING3_MOUSE Inhibitor of growth protein 3 (p47ING3) 421 46,847 Binding site (4); Chain (1); Compositional bias (1); Cross-link (4); Erroneous initiation (3); Metal binding (8); Modified residue (2); Sequence conflict (1); Zinc finger (1) FUNCTION: Component of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when directly recruited to sites of DNA damage. Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AFZ from the nucleosome (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with H3K4me3 and to a lesser extent with H3K4me2 (By similarity). Component of the NuA4 histone acetyltransferase complex which contains the catalytic subunit KAT5/TIP60 and the subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6. The NuA4 complex interacts with MYC. HTATTIP/TIP60, EPC1, and ING3 together constitute a minimal HAT complex termed Piccolo NuA4. Component of a SWR1-like complex (By similarity). {ECO:0000250}. DOMAIN: The PHD-type zinc finger mediates the binding to H3K4me3. {ECO:0000250}. +Q80XH2 IMPG2_MOUSE Interphotoreceptor matrix proteoglycan 2 (Sialoprotein associated with cones and rods proteoglycan) (Spacrcan) 1243 138,102 Alternative sequence (1); Chain (1); Disulfide bond (6); Domain (4); Erroneous initiation (1); Frameshift (1); Glycosylation (15); Mutagenesis (6); Region (5); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1107 1127 Helical. {ECO:0000255}. TOPO_DOM 28 1106 Extracellular. {ECO:0000255}.; TOPO_DOM 1128 1243 Cytoplasmic. {ECO:0000255}. FUNCTION: Chondroitin sulfate- and hyaluronan-binding proteoglycan involved in the organization of interphotoreceptor matrix; may participate in the maturation and maintenance of the light-sensitive photoreceptor outer segment. Binds heparin. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in the retina and pineal gland. {ECO:0000269|PubMed:12589770}. +Q8C0D7 ING4_MOUSE Inhibitor of growth protein 4 (p29ING4) 249 28,528 Alternative sequence (8); Beta strand (1); Binding site (4); Chain (1); Coiled coil (1); Frameshift (1); Metal binding (8); Modified residue (8); Motif (1); Sequence conflict (2); Turn (2); Zinc finger (1) FUNCTION: Component of the HBO1 complex which has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3 and is responsible for the bulk of histone H4 acetylation in vivo. Through chromatin acetylation it may function in DNA replication. May inhibit tumor progression by modulating the transcriptional output of signaling pathways which regulate cell proliferation. Can suppress brain tumor angiogenesis through transcriptional repression of RELA/NFKB3 target genes when complexed with RELA. May also specifically suppress loss of contact inhibition elicited by activated oncogenes such as MYC. Represses hypoxia inducible factor's (HIF) activity by interacting with HIF prolyl hydroxylase 2 (EGLN1) (By similarity). Can enhance apoptosis induced by serum starvation in mammary epithelial cell line HC11 (PubMed:11888890). {ECO:0000250|UniProtKB:Q9UNL4, ECO:0000269|PubMed:11888890}. PTM: Citrullination by PADI4 within the nuclear localization signal disrupts the interaction with p53 and increases susceptibility to degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11888890}. SUBUNIT: Homodimer. Interacts with H3K4me3 and to a lesser extent with H3K4me2, the interaction augments HBO1 acetylation activity on H3 tails. Component of the HBO1 complex composed at least of ING4 or ING5, KAT7/HBO1, MEAF6, and one of JADE1, JADE2 and JADE3. Interacts with EP300, RELA and TP53; these interactions may be indirect. Interacts with EGLN1 (By similarity). Isoform 3, isoform 4 and isoform 5 interact with BCL2A1. {ECO:0000250|UniProtKB:Q9UNL4, ECO:0000269|PubMed:11888890}. DOMAIN: The PHD-type zinc finger mediates the binding to H3K4me3. {ECO:0000250}.; DOMAIN: The N-terminal coiled-coil domain mediates homodimerization. {ECO:0000250}. TISSUE SPECIFICITY: Isoform 2, isoform 3, isoform 4 and isoform 5 are expressed in the mammary gland, ovary, spleen and muscle. {ECO:0000269|PubMed:11888890}. +P11034 MCPT1_MOUSE Mast cell protease 1 (mMCP-1) (EC 3.4.21.-) 246 27,013 Active site (3); Chain (1); Disulfide bond (3); Domain (1); Glycosylation (1); Propeptide (1); Signal peptide (1) FUNCTION: Has a chymotrypsin-like activity. SUBCELLULAR LOCATION: Secreted. Cytoplasmic granule. Note=Secretory granules. TISSUE SPECIFICITY: Mucosal mast cells. +P15119 MCPT2_MOUSE Mast cell protease 2 (mMCP-2) (EC 3.4.21.-) 244 26,732 Active site (3); Chain (1); Disulfide bond (3); Domain (1); Glycosylation (1); Propeptide (1); Sequence conflict (5); Signal peptide (1) TISSUE SPECIFICITY: Mucosal mast cells. +Q04999 INHBB_MOUSE Inhibin beta B chain (Activin beta-B chain) 411 45,211 Chain (1); Disulfide bond (5); Glycosylation (1); Propeptide (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Inhibins and activins inhibit and activate, respectively, the secretion of follitropin by the pituitary gland. Inhibins/activins are involved in regulating a number of diverse functions such as hypothalamic and pituitary hormone secretion, gonadal hormone secretion, germ cell development and maturation, erythroid differentiation, insulin secretion, nerve cell survival, embryonic axial development or bone growth, depending on their subunit composition. Inhibins appear to oppose the functions of activins. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Homo- or heterodimer; disulfide-linked. Inhibin A is a dimer of alpha and beta-A. Inhibin B is a dimer of alpha and beta-B. Activin A is a homodimer of beta-A. Activin B is a homodimer of beta-B. Activin AB is a dimer of beta-A and beta-B. Interacts with FST and FSTL3 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Uterus, testis, ovary, lung, kidney, brain, CJ7 embryonic stem cells, and possibly in liver. +Q04997 INHA_MOUSE Inhibin alpha chain 366 39,550 Chain (1); Disulfide bond (4); Glycosylation (2); Propeptide (2); Sequence conflict (3); Signal peptide (1); Site (2) FUNCTION: Inhibins and activins inhibit and activate, respectively, the secretion of follitropin by the pituitary gland. Inhibins/activins are involved in regulating a number of diverse functions such as hypothalamic and pituitary hormone secretion, gonadal hormone secretion, germ cell development and maturation, erythroid differentiation, insulin secretion, nerve cell survival, embryonic axial development or bone growth, depending on their subunit composition. Inhibins appear to oppose the functions of activins. Inhibin deficient mice are viable but are acutely sensitive to development of gonadal sex-cord stromal tumors. {ECO:0000269|PubMed:1448148, ECO:0000269|PubMed:8090730, ECO:0000269|PubMed:8701077}. PTM: Proteolytic processing yields a number of bioactive forms, consisting either solely of the mature alpha chain, of the most N-terminal propeptide linked through a disulfide bond to the mature alpha chain, or of the entire proprotein. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Dimeric, linked by one or more disulfide bonds. Inhibin A is a dimer of alpha and beta-A. Inhibin B is a dimer of alpha and beta-B. +Q80VY2 INKA2_MOUSE PAK4-inhibitor INKA2 (Induced in neural crest by AP2-alpha protein-related homolog) (MInca-r) 300 33,233 Alternative sequence (1); Chain (1); Region (1); Sequence conflict (1) FUNCTION: Inhibitor of the serine/threonine-protein kinase PAK4. Acts by binding PAK4 in a substrate-like manner, inhibiting the protein kinase activity. {ECO:0000250|UniProtKB:Q96EL1}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NTI7}. SUBUNIT: Interacts with PAK4. {ECO:0000250|UniProtKB:Q9NTI7}. DOMAIN: The Inka box (also named iBox or inca box) binds and inhibits PAK4 by binding a substrate-like manner. {ECO:0000250|UniProtKB:Q96EL1}. TISSUE SPECIFICITY: Enriched in the nervous system. {ECO:0000269|PubMed:26292052}. +A2A863 ITB4_MOUSE Integrin beta-4 (CD antigen CD104) 1818 201,650 Alternative sequence (2); Chain (1); Disulfide bond (23); Domain (7); Glycosylation (5); Modified residue (10); Motif (2); Region (3); Repeat (4); Sequence conflict (27); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 713 733 Helical. {ECO:0000255}. TOPO_DOM 29 712 Extracellular. {ECO:0000255}.; TOPO_DOM 734 1818 Cytoplasmic. {ECO:0000255}. FUNCTION: Integrin alpha-6/beta-4 is a receptor for laminin. It plays a critical structural role in the hemidesmosome of epithelial cells. Is required for the regulation of keratinocyte polarity and motility. ITGA6:ITGB4 binds to NRG1 (via EGF domain) and this binding is essential for NRG1-ERBB signaling. ITGA6:ITGB4 binds to IGF1 and this binding is essential for IGF1 signaling. ITGA6:ITGB4 binds to IGF2 and this binding is essential for IGF2 signaling. {ECO:0000250|UniProtKB:P16144}. PTM: Palmitoylated by DHHC3 at several cysteines of the membrane-proximal region, enhancing stability and cell surface expression. Palmitoylation also promotes secundary association with tertaspanins (By similarity). {ECO:0000250|UniProtKB:P16144}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Cell junction, hemidesmosome {ECO:0000250}. Note=Colocalizes with DST at the leading edge of migrating keratinocytes. {ECO:0000250}. SUBUNIT: Heterodimer of an alpha and a beta subunit. Beta-4 associates with alpha-6. Interacts (via cytoplasmic region) with COL17A1 (via cytoplasmic region). Interacts (via cytoplasmic region) with DST isoform 3 (via N-terminus). Interacts (via cytoplasmic domain) with DST (via N-terminus). Interacts with RAC1. ITGA6:ITGB4 is found in a ternary complex with NRG1 and ERBB3. ITGA6:ITGB4 is found in a ternary complex with IGF1 and IGF1R. ITGA6:ITGB4 interacts with IGF2. {ECO:0000250|UniProtKB:P16144}. DOMAIN: The fibronectin type-III-like domains bind BPAG1 and plectin and probably also recruit BP230. {ECO:0000250}. +P26011 ITB7_MOUSE Integrin beta-7 (Integrin beta-P) (M290 IEL antigen) 806 87,411 Chain (1); Disulfide bond (26); Domain (1); Glycosylation (8); Region (1); Repeat (4); Sequence conflict (5); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 725 745 Helical. {ECO:0000255}. TOPO_DOM 20 724 Extracellular. {ECO:0000255}.; TOPO_DOM 746 806 Cytoplasmic. {ECO:0000255}. FUNCTION: Integrin alpha-4/beta-7 (Peyer patches-specific homing receptor LPAM-1) is involved in adhesive interactions of leukocytes. It is a receptor for fibronectin and recognizes one or more domains within the alternatively spliced CS-1 region of fibronectin. Integrin alpha-4/beta-7 is also a receptor for MADCAM1 and VCAM1. It recognizes the sequence L-D-T in MADCAM1. Integrin alpha-E/beta-7 is a receptor for E-cadherin. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Heterodimer of an alpha and a beta subunit. Beta-7 associates with either alpha-4 or alpha-E. Interacts with FLNA (via filamin repeats 4, 9, 12, 17, 19, 21, and 23). {ECO:0000250|UniProtKB:P26010}. +Q8C863 ITCH_MOUSE E3 ubiquitin-protein ligase Itchy (EC 2.3.2.26) (HECT-type E3 ubiquitin transferase Itchy homolog) 864 98,994 Active site (1); Alternative sequence (2); Beta strand (19); Chain (1); Compositional bias (1); Domain (6); Erroneous initiation (1); Helix (21); Initiator methionine (1); Modified residue (7); Mutagenesis (10); Region (2); Turn (3) Protein modification; protein ubiquitination. FUNCTION: Acts as an E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates (PubMed:15358865, PubMed:16446428, PubMed:17592138, PubMed:18628966, PubMed:20392206, PubMed:25632008). It catalyzes 'Lys-29'-, 'Lys-48'- and 'Lys-63'-linked ubiquitin conjugation (By similarity). Involved in the control of inflammatory signaling pathways (By similarity). Is an essential component of a ubiquitin-editing protein complex, comprising also TNFAIP3, TAX1BP1 and RNF11, that ensures the transient nature of inflammatory signaling pathways (By similarity). Promotes the association of the complex after TNF stimulation (By similarity). Once the complex is formed, TNFAIP3 deubiquitinates 'Lys-63' polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-48'-polyubiquitin chains (By similarity). This leads to RIPK1 proteasomal degradation and consequently termination of the TNF- or LPS-mediated activation of NFKB1 (By similarity). Ubiquitinates RIPK2 by 'Lys-63'-linked conjugation and influences NOD2-dependent signal transduction pathways (By similarity). Regulates the transcriptional activity of several transcription factors involved in immune response (PubMed:15358865, PubMed:11828324). Ubiquitinates NFE2 by 'Lys-63' linkages and is implicated in the control of the development of hematopoietic lineages (By similarity). Mediates JUN ubiquitination and degradation (PubMed:15358865). Mediates JUNB ubiquitination and degradation (PubMed:11828324, PubMed:15358865). Critical regulator of type 2 helper T (Th2) cell cytokine production by inducing JUNB ubiquitination and degradation (PubMed:11828324). Involved in the negative regulation of MAVS-dependent cellular antiviral responses (By similarity). Ubiquitinates MAVS through 'Lys-48'-linked conjugation resulting in MAVS proteasomal degradation (By similarity). Following ligand stimulation, regulates sorting of Wnt receptor FZD4 to the degradative endocytic pathway probably by modulating PI42KA activity (By similarity). Ubiquitinates PI4K2A and negatively regulates its catalytic activity (By similarity). Ubiquitinates chemokine receptor CXCR4 and regulates sorting of CXCR4 to the degradative endocytic pathway following ligand stimulation by ubiquitinating endosomal sorting complex required for transport ESCRT-0 components HGS and STAM (By similarity). Targets DTX1 for lysosomal degradation and controls NOTCH1 degradation, in the absence of ligand, through 'Lys-29'-linked polyubiquitination (PubMed:18628966). Ubiquitinates SNX9 (By similarity). Ubiquitinates MAP3K7 through 'Lys-48'-linked conjugation (PubMed:25632008). Involved in the regulation of apoptosis and reactive oxygen species levels through the ubiquitination and proteasomal degradation of TXNIP (By similarity). Mediates the antiapoptotic activity of epidermal growth factor through the ubiquitination and proteasomal degradation of p15 BID (PubMed:20392206). Ubiquitinates BRAT1 and this ubiquitination is enhanced in the presence of NDFIP1 (By similarity). {ECO:0000250|UniProtKB:Q96J02, ECO:0000269|PubMed:11828324, ECO:0000269|PubMed:15358865, ECO:0000269|PubMed:16446428, ECO:0000269|PubMed:18628966, ECO:0000269|PubMed:20392206, ECO:0000269|PubMed:25632008}. PTM: On T-cell activation, phosphorylation by the JNK cascade on serine and threonine residues surrounding the PRR domain accelerates the ubiquitination and degradation of JUN and JUNB. The increased ITCH catalytic activity due to phosphorylation by JNK1 may occur due to a conformational change disrupting the interaction between the PRR/WW motifs domain and the HECT domain and, thus exposing the HECT domain. Phosphorylation by FYN reduces interaction with JUNB and negatively controls JUN ubiquitination and degradation. {ECO:0000269|PubMed:15358865, ECO:0000269|PubMed:16446428, ECO:0000269|PubMed:18628966, ECO:0000269|PubMed:20392206}.; PTM: Monoubiquitinated. Autopolyubiquitinated with 'Lys-63' linkages which does not lead to protein degradation. {ECO:0000250|UniProtKB:Q96J02}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q96J02}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q96J02}; Cytoplasmic side {ECO:0000250|UniProtKB:Q96J02}. Cytoplasm {ECO:0000250|UniProtKB:Q96J02}. Nucleus {ECO:0000250|UniProtKB:Q96J02}. Early endosome membrane {ECO:0000250|UniProtKB:Q96J02}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q96J02}; Cytoplasmic side {ECO:0000250|UniProtKB:Q96J02}. Endosome membrane {ECO:0000250|UniProtKB:Q96J02}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q96J02}; Cytoplasmic side {ECO:0000250|UniProtKB:Q96J02}. Note=May be recruited to exosomes by NDFIP1. Localizes to plasma membrane upon CXCL12 stimulation where it co-localizes with CXCL4. Localization to early endosomes is increased upon CXCL12 stimulation where it co-localizes with DTX3L and CXCL4. {ECO:0000250|UniProtKB:Q96J02}. SUBUNIT: Monomer. Interacts (via WW domains) with OCNL (PubMed:11782481). Interacts (via WW domains) with NOTCH1 (PubMed:10940313, PubMed:18628966). Interacts (via WW domains) JUN (PubMed:11828324). Interacts with JUNB; the interaction promotes ITCH-mediated ubiquitination and degradation of JUNB (PubMed:11828324). Interacts with FYN; the interaction phosphorylates ITCH on Tyr-381 decreasing binding of JUNB (By similarity). Interacts (via WW domain 2) with N4BP1; the interaction inhibits the E3 ubiquitin-protein ligase activity (PubMed:17592138). Interacts with NDFIP1 and NDFIP2; the interaction with NDFIP proteins activates the E3 ubiquitin-protein ligase and may induce its recruitment to exosomes (PubMed:11748237, PubMed:17137798, PubMed:25632008). Interacts with ARHGEF7 (By similarity). Interacts with RNF11 (By similarity). Interacts (via the WW 1 domain) with NFE2 (via the PXY motif 1); the interaction promotes 'Lys-63'-linked ubiquitination of NFE2, retains it in the cytoplasm and prevents its transactivation activity (By similarity). Interacts (via WW domains) with CXCR4 (via C-terminus); the interaction depends on CXCR4 phosphorylation (By similarity). Found in a complex with E3 ligase DTX3L and ESCRT-0 components HGS and STAM (By similarity). Interacts with DTX3L (via C-terminus); the interaction is increased upon CXCL12 stimulation and inhibits ITCH catalytic activity (the interaction is direct) (By similarity). Interacts with HGS (By similarity). Interacts (via WW domains) with PCBP2 within a complex containing ITCH, MAVS and PCBP2 (By similarity). Interacts (via WW domains) with TXNIP (via C-terminus) (By similarity). Interacts with p15 BID (PubMed:20392206). Interacts with ERBB4 (By similarity).Interacts with DTX1 (By similarity). Interacts with SPART (By similarity). Interacts with SNX9 and SNX18 (By similarity). Interacts (via its WW domains) with ATN1 (By similarity). Interacts (via WW domains) with SGK3 (By similarity). Interacts with CBLC (By similarity). Interacts with OTUD7B (By similarity). Interacts (via WW domain 1,2 and 3) with PI4K2A; the interaction inhibits PI4K2A catalytic activity and promotes ITCH catalytic activity (PubMed:23146885). Interacts with ARRDC4 (By similarity). Part of a complex containing ITCH, NDFIP1 and MAP3K7 (PubMed:25632008). Interacts with UBE2L3; the interaction is mediated by NDFIP1 (PubMed:25632008). Interacts with MAPK8/JNK1 (PubMed:16446428). Interacts (via WW domains) with ARRDC1 (via PPxY motifs); the interaction is direct and participates to the recruitment of the ubiquitin-protein ligase ITCH to the NOTCH1 receptor (By similarity). Interacts (via WW domains) with ARRDC2 (By similarity). Interacts (via WW domains) with ARRDC3 (By similarity). {ECO:0000250|UniProtKB:Q96J02, ECO:0000269|PubMed:10940313, ECO:0000269|PubMed:11748237, ECO:0000269|PubMed:11782481, ECO:0000269|PubMed:11828324, ECO:0000269|PubMed:16446428, ECO:0000269|PubMed:17137798, ECO:0000269|PubMed:17592138, ECO:0000269|PubMed:20392206, ECO:0000269|PubMed:23146885, ECO:0000269|PubMed:25632008}.; SUBUNIT: (Microbial infection) Interacts with Epstein-Barr virus LMP2A. {ECO:0000269|PubMed:17437719}. DOMAIN: The WW domains mediate interaction with PPxY motif-containing proteins. {ECO:0000250|UniProtKB:Q96J02}. TISSUE SPECIFICITY: Detected in uterus (at protein level) (PubMed:23146885). Widely expressed (PubMed:9462742). {ECO:0000269|PubMed:23146885, ECO:0000269|PubMed:9462742}. DISEASE: Note=Defects in Itch are the cause of the itchy phenotype which is an inflammatory and immunological condition characterized by inflammation in the lung and stomach, hyperplasia in lymphoid and hematopoietic cells and constant itching in the skin. {ECO:0000269|PubMed:9462742}. +Q6IE82 JADE3_MOUSE Protein Jade-3 (Jade family PHD finger protein 3) (PHD finger protein 16) 823 93,455 Chain (1); Frameshift (1); Modified residue (11); Zinc finger (3) FUNCTION: Component of the HBO1 complex which has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3 and is responsible for the bulk of histone H4 acetylation in vivo. {ECO:0000250}. SUBUNIT: Component of the HBO1 complex composed at least of ING4 or ING5, MYST2/HBO1, MEAF6, and one of JADE1, JADE2 and JADE3. {ECO:0000250}. +Q58A65 JIP4_MOUSE C-Jun-amino-terminal kinase-interacting protein 4 (JIP-4) (JNK-interacting protein 4) (JNK-associated leucine-zipper protein) (JLP) (JNK/SAPK-associated protein 2) (JSAP2) (Mitogen-activated protein kinase 8-interacting protein 4) (Sperm-associated antigen 9) 1321 146,219 Alternative sequence (6); Chain (1); Coiled coil (3); Domain (2); Erroneous gene model prediction (1); Erroneous initiation (1); Modified residue (30); Sequence conflict (5) FUNCTION: The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. {ECO:0000269|PubMed:12391307, ECO:0000269|PubMed:15767678}. PTM: Phosphorylated by MAPK8 and MAPK14. {ECO:0000269|PubMed:15767678}. SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region. Note=Perinuclear distribution in response to stress signals such as UV radiation. SUBUNIT: Homodimer. The homodimer interacts with ARF6, forming a heterotetramer (By similarity). Homooligomer. Interacts with MAX, MAPK8, MAPK14, MAPK10, MAPK14, MAP3K3, MYC, KNS2, and MAP2K4. Interaction with KNS2 is important in the formation of ternary complex with MAPK8. {ECO:0000250, ECO:0000269|PubMed:12391307, ECO:0000269|PubMed:15767678, ECO:0000269|PubMed:15987681}. TISSUE SPECIFICITY: Isoform 6 is highly expressed in brain, kidney, liver, heart. {ECO:0000269|PubMed:15767678}. +P52332 JAK1_MOUSE Tyrosine-protein kinase JAK1 (EC 2.7.10.2) (Janus kinase 1) (JAK-1) 1153 133,367 Active site (1); Binding site (1); Chain (1); Domain (4); Modified residue (5); Nucleotide binding (1); Sequence conflict (4) FUNCTION: Tyrosine kinase of the non-receptor type, involved in the IFN-alpha/beta/gamma signal pathway. Kinase partner for the interleukin (IL)-2 receptor as well as interleukin (IL)-10 receptor. {ECO:0000250|UniProtKB:P23458}. PTM: Ubiquitinated by RNF125; leading to its degradation by the proteasome. {ECO:0000250|UniProtKB:P23458}.; PTM: Autophosphorylated. Phosphorylated on tyrosine residues in response to interferon gamma signaling. Dephosphorylation of Tyr-1034 and Tyr-1034 by PTPN2 negatively regulates cytokine-mediated signaling. {ECO:0000250|UniProtKB:P23458}. SUBCELLULAR LOCATION: Endomembrane system; Peripheral membrane protein. Note=Wholly intracellular, possibly membrane associated. SUBUNIT: Interacts with IL31RA. Interacts with IFNAR2. Interacts with IFNGR1. Interacts with JAKMIP1. Interacts with SHB. Interacts (via N-terminus) with IL2RB and IL10RA (via its cytoplasmic domain) (By similarity). Interacts with FER (PubMed:12738762). {ECO:0000250|UniProtKB:P23458, ECO:0000269|PubMed:12738762}. DOMAIN: The FERM domain mediates interaction with JAKMIP1. {ECO:0000250}.; DOMAIN: Possesses two phosphotransferase domains. The second one probably contains the catalytic domain, while the presence of slight differences suggest a different role for domain 1. {ECO:0000250}. +Q8BI36 JKAMP_MOUSE JNK1/MAPK8-associated membrane protein (JKAMP) (JNK1-associated membrane protein) (JAMP) (Medulloblastoma antigen MU-MB-50.4 homolog) 311 35,248 Alternative sequence (1); Chain (1); Glycosylation (1); Mutagenesis (1); Sequence conflict (2); Topological domain (8); Transmembrane (7) TRANSMEM 58 78 Helical. {ECO:0000255}.; TRANSMEM 88 108 Helical. {ECO:0000255}.; TRANSMEM 150 170 Helical. {ECO:0000255}.; TRANSMEM 189 209 Helical. {ECO:0000255}.; TRANSMEM 211 231 Helical. {ECO:0000255}.; TRANSMEM 251 271 Helical. {ECO:0000255}.; TRANSMEM 278 298 Helical. {ECO:0000255}. TOPO_DOM 1 57 Lumenal. {ECO:0000255}.; TOPO_DOM 79 87 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 109 149 Lumenal. {ECO:0000255}.; TOPO_DOM 171 188 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 210 210 Lumenal. {ECO:0000255}.; TOPO_DOM 232 250 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 272 277 Lumenal. {ECO:0000255}.; TOPO_DOM 299 311 Cytoplasmic. {ECO:0000255}. FUNCTION: May be a regulator of the duration of MAPK8 activity in response to various stress stimuli. Facilitates degradation of misfolded endoplasmic reticulum (ER) luminal proteins through the recruitment of components of the proteasome and endoplasmic reticulum-associated degradation (ERAD) system. {ECO:0000269|PubMed:16166642}. PTM: Ubiquitinated by RNF5 via 'Lys-63'-linked ubiquitin linkage in a UBE2N-dependent manner. Ubiquitination decreases association with components of the proteasome and ERAD. {ECO:0000269|PubMed:19269966}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16166642, ECO:0000269|PubMed:18784250}; Multi-pass membrane protein {ECO:0000269|PubMed:16166642, ECO:0000269|PubMed:18784250}. SUBUNIT: Interacts with RNF5 and MAPK8, but not with MAPK9. Binding to MAPK8 occurs before and after exposure to stress, such as UV irradiation. After exposure to stress, interacts with phosphorylated MAPK8. Competes with DUSP10 for MAPK8 binding. Associates with multiple components of the proteasome and with ERAD regulatory proteins, including AMFR/GP78, CANX, PSMC1, PSMC2, PSMC3/TBP1, PSMC5, PSMC6, PSMD8, SEC61-ALPHA and UFD1. {ECO:0000269|PubMed:16166642, ECO:0000269|PubMed:18784250, ECO:0000269|PubMed:19269966}. TISSUE SPECIFICITY: Expressed in numerous tissues, including brain, spleen, thymus, liver, kidney and testis. Elevated expression in medulloblastoma. {ECO:0000269|PubMed:16166642}. +Q9ERE9 JIP2_MOUSE C-Jun-amino-terminal kinase-interacting protein 2 (JIP-2) (JNK-interacting protein 2) (Islet-brain-2) (IB-2) (JNK MAP kinase scaffold protein 2) (Mitogen-activated protein kinase 8-interacting protein 2) 830 89,900 Chain (1); Compositional bias (6); Domain (2); Erroneous termination (1); Modified residue (3); Region (2); Sequence conflict (1) FUNCTION: The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. JIP2 inhibits IL1 beta-induced apoptosis in insulin-secreting cells (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13387}. Note=Accumulates in cell surface projections. {ECO:0000250|UniProtKB:Q13387}. SUBUNIT: Forms homo-or heterooligomeric complexes. Binds specific components of the JNK signaling pathway namely JNK1, JNK2, JNK3, MAP2K7, MAP3K10, MAP3K11, MAP3K12 and MAPK13 (By similarity). Also binds the proline-rich domain-containing splice variant of apolipoprotein E receptor 2 (ApoER2). Binds the TPR motif-containing C-terminal of kinesin light chain. Binds the cytoplasmic tails of LRP1 and LRP2 (Megalin). Interacts with DCLK2. Interacts with FGF13; enables the interaction with MAPK13 and may regulate the MAPK8IP2 scaffolding activity. Interacts with TIAM1 and TIAM2 (PubMed:10827199, PubMed:11378392, PubMed:16628014, PubMed:19893486). Interacts with SH3RF2 (By similarity). {ECO:0000250|UniProtKB:G3V9M2, ECO:0000250|UniProtKB:Q13387, ECO:0000269|PubMed:10827199, ECO:0000269|PubMed:11378392, ECO:0000269|PubMed:16628014, ECO:0000269|PubMed:19893486}. TISSUE SPECIFICITY: Highly expressed in brain. Expressed in all neurons. Also expressed in testis, primarily in the epididymal epidermis. +Q3TA59 JMJD8_MOUSE JmjC domain-containing protein 8 (Jumonji domain-containing protein 8) 271 30,666 Chain (1); Domain (1); Erroneous initiation (1); Frameshift (1); Glycosylation (3); Sequence conflict (1); Signal peptide (1) FUNCTION: Functions as a positive regulator of TNF-induced NF-kappaB signaling (By similarity). Regulates angiogenesis and cellular metabolism through interaction with PKM (PubMed:27199445). {ECO:0000250|UniProtKB:Q96S16, ECO:0000269|PubMed:27199445}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q96S16}. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:Q96S16}. Cytoplasm {ECO:0000250|UniProtKB:Q96S16}. SUBUNIT: Oligomer. Dimer. Interacts with PKM; regulates angiogenesis and metabolism. {ECO:0000250|UniProtKB:Q96S16}. +P97825 JUPI1_MOUSE Jupiter microtubule associated homolog 1 (Hematological and neurological expressed 1 protein) [Cleaved into: Jupiter microtubule associated homolog 1, N-terminally processed] 154 16,081 Chain (2); Initiator methionine (1); Modified residue (11) FUNCTION: Modulates negatively AKT-mediated GSK3B signaling. Induces CTNNB1 'Ser-33' phosphorylation and degradation through the suppression of the inhibitory 'Ser-9' phosphorylation of GSK3B, which represses the function of the APC:CTNNB1:GSK3B complex and the interaction with CDH1/E-cadherin in adherent junctions (By similarity). Plays a role in the regulation of cell cycle and cell adhesion (PubMed:25450365). Has an inhibitory role on AR-signaling pathway through the induction of receptor proteosomal degradation (By similarity). {ECO:0000250|UniProtKB:Q9UK76, ECO:0000269|PubMed:25450365}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UK76}. Cytoplasm {ECO:0000250|UniProtKB:Q9UK76}. SUBUNIT: Interacts with the complex composed, at least, of APC, CTNNB1 and GSK3B; the interaction takes place with the inactive form of GSK3B (phosphorylated at 'Ser-9'). {ECO:0000250|UniProtKB:Q9UK76}. TISSUE SPECIFICITY: Expressed in yolk sac, fetal brain, brain, spleen and bone marrow. {ECO:0000269|PubMed:9271675}. +P24063 ITAL_MOUSE Integrin alpha-L (CD11 antigen-like family member A) (Leukocyte adhesion glycoprotein LFA-1 alpha chain) (LFA-1A) (Leukocyte function-associated molecule 1 alpha chain) (Lymphocyte antigen 15) (Ly-15) (CD antigen CD11a) 1163 128,328 Calcium binding (3); Chain (1); Disulfide bond (8); Domain (1); Glycosylation (15); Motif (1); Repeat (7); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1088 1108 Helical. {ECO:0000255}. TOPO_DOM 24 1087 Extracellular. {ECO:0000255}.; TOPO_DOM 1109 1163 Cytoplasmic. {ECO:0000255}. FUNCTION: Integrin alpha-L/beta-2 is a receptor for ICAM1, ICAM2, ICAM3 and ICAM4 (PubMed:2051027). Integrin alpha-L/beta-2 is also a receptor for F11R (By similarity). Involved in a variety of immune phenomena including leukocyte-endothelial cell interaction, cytotoxic T-cell mediated killing, and antibody dependent killing by granulocytes and monocytes. Contributes to natural killer cell cytotoxicity. Involved in leukocyte adhesion and transmigration of leukocytes including T-cells and neutrophils (PubMed:16234355, PubMed:24158516). Required for generation of common lymphoid progenitor cells in bone marrow, indicating the role in lymphopoiesis (PubMed:25108025). Integrin alpha-L/beta-2 in association with ICAM3, contributes to apoptotic neutrophil phagocytosis by macrophages. {ECO:0000250|UniProtKB:P20701, ECO:0000269|PubMed:16234355, ECO:0000269|PubMed:2051027, ECO:0000269|PubMed:24158516, ECO:0000269|PubMed:25108025}. PTM: In resting T-cells, up to 40% of surface ITGAL is constitutively phosphorylated. Phosphorylation causes conformational changes needed for ligand binding and is necessary for the activation by some physiological agents. {ECO:0000250|UniProtKB:P20701}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P20701}; Single-pass type I membrane protein {ECO:0000255}. SUBUNIT: Heterodimer of an alpha and a beta subunit. Alpha-L associates with beta-2. Interacts with THBD. {ECO:0000250|UniProtKB:P20701}. DOMAIN: The integrin I-domain (insert) is a VWFA domain. Integrins with I-domains do not undergo protease cleavage. The I-domain is necessary and sufficient for interaction with ICAM1 and F11R. {ECO:0000250|UniProtKB:P20701}. TISSUE SPECIFICITY: Leukocytes. {ECO:0000269|PubMed:24158516, ECO:0000269|PubMed:25108025}. +Q62137 JAK3_MOUSE Tyrosine-protein kinase JAK3 (EC 2.7.10.2) (Janus kinase 3) (JAK-3) 1100 122,641 Active site (1); Alternative sequence (2); Binding site (1); Chain (1); Domain (4); Frameshift (2); Modified residue (6); Mutagenesis (1); Nucleotide binding (1); Region (1); Sequence conflict (36) FUNCTION: Non-receptor tyrosine kinase involved in various processes such as cell growth, development, or differentiation. Mediates essential signaling events in both innate and adaptive immunity and plays a crucial role in hematopoiesis during T-cells development. In the cytoplasm, plays a pivotal role in signal transduction via its association with type I receptors sharing the common subunit gamma such as IL2R, IL4R, IL7R, IL9R, IL15R and IL21R. Following ligand binding to cell surface receptors, phosphorylates specific tyrosine residues on the cytoplasmic tails of the receptor, creating docking sites for STATs proteins. Subsequently, phosphorylates the STATs proteins once they are recruited to the receptor. Phosphorylated STATs then form homodimer or heterodimers and translocate to the nucleus to activate gene transcription. For example, upon IL2R activation by IL2, JAK1 and JAK3 molecules bind to IL2R beta (IL2RB) and gamma chain (IL2RG) subunits inducing the tyrosine phosphorylation of both receptor subunits on their cytoplasmic domain. Then, STAT5A AND STAT5B are recruited, phosphorylated and activated by JAK1 and JAK3. Once activated, dimerized STAT5 translocates to the nucleus and promotes the transcription of specific target genes in a cytokine-specific fashion. {ECO:0000269|PubMed:9016869}. PTM: Autophosphorylated, leading to regulate its activity. IL2 promotes phosphorylation on tyrosine residues, including autophosphorylation on Tyr-781 (By similarity). Dephosphorylation of Tyr-976 and Tyr-977 by PTPN2 negatively regulates cytokine-mediated signaling (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with STAM2 and MYO18A. Interacts with SHB (By similarity). {ECO:0000250}. DOMAIN: Possesses two phosphotransferase domains. The second one contains the catalytic domain, while the presence of a pseudokinase domain is required for suppression of basal activity of JAK3. TISSUE SPECIFICITY: In contrast with the ubiquitous expression of the other JAKs, JAK3 is predominantly expressed in hematopoietic tissues. {ECO:0000269|PubMed:8605329}. +Q5PR69 K1211_MOUSE Uncharacterized protein KIAA1211 1207 132,286 Alternative sequence (1); Chain (1); Compositional bias (3); Modified residue (12); Sequence conflict (4) +Q8C753 K0556_MOUSE Protein KIAA0556 1610 179,609 Alternative sequence (5); Chain (1); Coiled coil (1); Compositional bias (1); Erroneous initiation (2); Modified residue (2); Sequence conflict (4) FUNCTION: May influence the stability of microtubules (MT), possibly through interaction with the MT-severing katanin complex. {ECO:0000250|UniProtKB:O60303}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:O60303}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:O60303}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O60303}. Note=When overexpressed, localizes to the cytoplasm where it associates with acetylated alpha-tubulin. {ECO:0000250|UniProtKB:O60303}. SUBUNIT: Interacts with microtubules. Interacts with 4 subunits of the katanin complex: KATNA1, KATNAL1, KATNB1 and KATNBL1. {ECO:0000250|UniProtKB:O60303}. +Q3UPC7 K0825_MOUSE Uncharacterized protein KIAA0825 homolog 1272 145,556 Alternative sequence (2); Chain (1); Erroneous initiation (1); Erroneous termination (1); Frameshift (2); Sequence conflict (5) +Q3UE31 K0930_MOUSE Uncharacterized protein KIAA0930 homolog 404 45,960 Chain (1); Erroneous initiation (2); Modified residue (10); Sequence conflict (1) +Q80TK0 K1107_MOUSE AP2-interacting clathrin-endocytosis protein (APache) 1239 134,060 Chain (1); Frameshift (1); Sequence conflict (6) FUNCTION: Involved in clathrin-mediated endocytosis at the synapse. Plays a role in neuronal development and in synaptic vesicle recycling in mature neurons, a process required for normal synaptic transmission. {ECO:0000269|PubMed:29262337}. SUBCELLULAR LOCATION: Cell projection, axon {ECO:0000269|PubMed:29262337}. Cell junction, synapse, presynaptic cell membrane {ECO:0000269|PubMed:29262337}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:D4A0X3}. Note=In primary cultures, mainly present at axonal and presynaptic terminal levels of mature neurons. In immature neurons, localizes to the cell body and growing processes, including axons. {ECO:0000269|PubMed:29262337}. SUBUNIT: Interacts (via N-terminus) with adaptor protein complex AP-2 subunits alpha (AP2A1) and beta (AP2B1). {ECO:0000269|PubMed:29262337}. TISSUE SPECIFICITY: Neuron-specific protein. Primarily expressed in brain, with the highest levels in the cerebral cortex, hippocampus, and striatum (at protein level). Not detected in glial cells. {ECO:0000269|PubMed:29262337}. +P19001 K1C19_MOUSE Keratin, type I cytoskeletal 19 (Cytokeratin-19) (CK-19) (Keratin-19) (K19) 403 44,542 Chain (1); Domain (1); Modified residue (17); Region (8); Site (2) FUNCTION: Involved in the organization of myofibers. Together with KRT8, helps to link the contractile apparatus to dystrophin at the costameres of striated muscle (By similarity). {ECO:0000250}. SUBUNIT: Heterotetramer of two type I and two type II keratins. Interacts with PNN and the actin-binding domain of DMD (By similarity). {ECO:0000250}. DOMAIN: This keratin differs from all other IF proteins in lacking the C-terminal tail domain. +Q99PS0 K1C23_MOUSE Keratin, type I cytoskeletal 23 (Cytokeratin-23) (CK-23) (Keratin-23) (K23) 422 48,027 Chain (1); Domain (1); Region (7) SUBUNIT: Heterotetramer of two type I and two type II keratins. {ECO:0000250}. +Q8VCW2 K1C25_MOUSE Keratin, type I cytoskeletal 25 (Cytokeratin-25) (CK-25) (Keratin-25) (K25) (Type I inner root sheath-specific keratin-K25irs1) (mIRSa1) 446 48,921 Chain (1); Compositional bias (1); Domain (1); Modified residue (1); Mutagenesis (2); Region (7) FUNCTION: Essential for the proper assembly of type I and type II keratin protein complexes and formation of keratin intermediate filaments in the inner root sheath (irs) (PubMed:14996088, PubMed:17920809). Plays a role in the cytoskeleton organization (By similarity). {ECO:0000250|UniProtKB:Q7Z3Z0, ECO:0000269|PubMed:14996088, ECO:0000269|PubMed:17920809}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14996088}. SUBUNIT: Heterodimer of a type I and a type II keratin (PubMed:14996088). Heterodimer with type II keratin KRT5 leading to the formation of keratin intermediate filament (KIF) network. Interacts with KRT6A to form filaments (By similarity). {ECO:0000250|UniProtKB:Q7Z3Z0, ECO:0000269|PubMed:14996088, ECO:0000305}. +P00757 K1KB4_MOUSE Kallikrein 1-related peptidase-like b4 (7S nerve growth factor alpha chain) (Alpha-NGF) 256 28,548 Beta strand (14); Chain (1); Disulfide bond (4); Domain (1); Helix (5); Metal binding (2); Natural variant (1); Region (1); Sequence conflict (2); Signal peptide (1) PTM: The presence of Gln-24 prevents cleavage of the activation peptide, which remains attached at the amino end of the mature alpha chain. SUBUNIT: 7S nerve growth factor is composed of two alpha chains, a beta dimer composed of identical chains, and two gamma chains. +Q9Z320 K1C27_MOUSE Keratin, type I cytoskeletal 27 (Cytokeratin-27) (CK-27) (Keratin complex-1, acidic, gene C29) (Keratin-27) (K27) (Type I inner root sheath-specific keratin-K25irs3) 448 49,105 Chain (1); Compositional bias (1); Domain (1); Mutagenesis (1); Region (7) FUNCTION: Essential for the proper assembly of type I and type II keratin protein complexes and formation of keratin intermediate filaments in the inner root sheath (irs). {ECO:0000269|PubMed:14996088, ECO:0000269|PubMed:17920809}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14996088}. SUBUNIT: Heterotetramer of two type I and two type II keratins. Interacts with KRT6A to form filaments. {ECO:0000269|PubMed:14996088, ECO:0000305}. TISSUE SPECIFICITY: Expressed in skin. Expressed in the Henle layer and cuticle of the irs in hair follicle bulb. In the hair follicle, expression was observed in all layers of the irs but was stronger in the Henle layer and cuticle than the Huxley layer until the Henle layer differentiated (at protein level). {ECO:0000269|PubMed:10087197, ECO:0000269|PubMed:14996088}. +A6BLY7 K1C28_MOUSE Keratin, type I cytoskeletal 28 (Cytokeratin-28) (CK-28) (Keratin-25D) (K25D) (Keratin-28) (K28) (Type I inner root sheath-specific keratin-K25irs4) 462 50,346 Chain (1); Compositional bias (1); Domain (1); Region (7) FUNCTION: Essential for the proper assembly of types I and II keratin protein complexes and the formation of keratin intermediate filaments in the inner root sheath (irs). {ECO:0000269|PubMed:14996088, ECO:0000269|PubMed:17920809}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14996088}. SUBUNIT: Heterotetramer of two type I and two type II keratins. {ECO:0000305}. TISSUE SPECIFICITY: In the hair follicle and bulb, uniformly expressed in all three layers of the inner root sheath (the Henle layer, the Huxley layer and the cuticle) and observed in matrix cells (at protein level). {ECO:0000269|PubMed:14996088}. +Q9Z331 K2C6B_MOUSE Keratin, type II cytoskeletal 6B (Cytokeratin-6B) (CK-6B) (Keratin-6-beta) (mK6-beta) (Keratin-6B) (K6B) 562 60,322 Chain (1); Domain (1); Region (7); Site (1) SUBUNIT: Heterodimer of a type I and a type II keratin. KRT6 isomers associate with KRT16 and/or KRT17. {ECO:0000269|PubMed:8636216}. TISSUE SPECIFICITY: Expressed in adult epithelia including the tongue, esophagus/trachea, eye and skin. Localized preferentially to the suprabasal layers of thickened epidermis in injured and chemically treated skin. {ECO:0000269|PubMed:9790766}. +P07744 K2C4_MOUSE Keratin, type II cytoskeletal 4 (Cytokeratin-4) (CK-4) (Cytoskeletal 57 kDa keratin) (Keratin-4) (K4) (Type-II keratin Kb4) 525 56,283 Chain (1); Compositional bias (2); Domain (1); Erroneous initiation (1); Modified residue (1); Region (7); Sequence conflict (5); Site (1) SUBUNIT: Heterotetramer of two type I and two type II keratins. Keratin-4 is generally associated with keratin-13. TISSUE SPECIFICITY: Expressed in the dorsal and ventral epithelium of the tongue. Highest expression levels are detected in the suprabasal layer with low levels detected in the basal cell layer. Within the suprabasal layer expression is highest in the spinous cells, decreases in the granular cells and is not detected in the stratum corneum. {ECO:0000269|PubMed:2418416}. +Q9JM71 K1B27_MOUSE Kallikrein 1-related peptidase b27 (EC 3.4.21.-) (Glandular kallikrein K27) (mGK-27) (Tissue kallikrein 27) (mKlk27) 263 28,742 Active site (3); Chain (1); Disulfide bond (5); Domain (1); Glycosylation (2); Mutagenesis (1); Propeptide (1); Signal peptide (1) FUNCTION: Serine protease with chymotrypsin-like cleavage specificity. Shows activity towards casein, gelatin, IGFBP3 and fibronectin but not towards laminin or collagens I and IV. Does not hydrolyze kininogin to release Lys-bradykinin. TISSUE SPECIFICITY: Expressed in testis and submaxillary gland. Not expressed in heart, brain, spleen, lung, liver, muscle, kidney and ovary. In the testis, expression localized specifically to Leydig cells in the interstitial tissues. {ECO:0000269|PubMed:11082197}. +Q61423 KCNA4_MOUSE Potassium voltage-gated channel subfamily A member 4 (Voltage-gated potassium channel subunit Kv1.4) 654 73,470 Chain (1); Compositional bias (6); Glycosylation (1); Intramembrane (2); Modified residue (2); Motif (2); Region (1); Sequence conflict (3); Topological domain (8); Transmembrane (6) INTRAMEM 513 524 Helical; Name=Pore helix. {ECO:0000250|UniProtKB:P63142}.; INTRAMEM 525 532 {ECO:0000250|UniProtKB:P63142}. TRANSMEM 306 327 Helical; Name=Segment S1. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 372 393 Helical; Name=Segment S2. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 405 425 Helical; Name=Segment S3. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 441 461 Helical; Voltage-sensor; Name=Segment S4. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 477 498 Helical; Name=Segment S5. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 540 568 Helical; Name=Segment S6. {ECO:0000250|UniProtKB:P63142}. TOPO_DOM 1 305 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 328 371 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 394 404 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 426 440 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 462 476 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 499 512 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 533 539 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 569 654 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}. FUNCTION: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes. Forms tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane (PubMed:8020965). Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNA1, KCNA2, KCNA4, KCNA5, and possibly other family members as well; channel properties depend on the type of alpha subunits that are part of the channel (By similarity). Channel properties are modulated by cytoplasmic beta subunits that regulate the subcellular location of the alpha subunits and promote rapid inactivation. In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes, making it difficult to assign currents observed in intact tissues to any particular potassium channel family member. Homotetrameric KCNA4 forms a potassium channel that opens in response to membrane depolarization, followed by rapid spontaneous channel closure (PubMed:8020965). Likewise, a heterotetrameric channel formed by KCNA1 and KCNA4 shows rapid inactivation (By similarity). {ECO:0000250|UniProtKB:P15385, ECO:0000269|PubMed:8020965}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8020965}; Multi-pass membrane protein {ECO:0000255}. Cell projection, axon {ECO:0000250|UniProtKB:P15385}. SUBUNIT: Homotetramer and heterotetramer of potassium channel proteins (By similarity). Interacts with KCNAB1 and KCNAB2 (By similarity). Binds PDZ domains of DLG1, DLG2 and DLG4 (By similarity). Interacts with SIGMAR1 (By similarity). Detected in a complex with KCNA1 (By similarity). Interacts with KCNA2 (By similarity). Part of a complex containing KCNA1, KCNAB1 and LGI1 (By similarity). Interacts (via cytoplasmic N-terminal domain) with KCNRG (By similarity). {ECO:0000250|UniProtKB:P15385, ECO:0000250|UniProtKB:P22459}. DOMAIN: The N-terminus may be important in determining the rate of inactivation of the channel while the tail may play a role in modulation of channel activity and/or targeting of the channel to specific subcellular compartments. {ECO:0000250|UniProtKB:Q28527}.; DOMAIN: The transmembrane segment S4 functions as voltage-sensor and is characterized by a series of positively charged amino acids at every third position. Channel opening and closing is effected by a conformation change that affects the position and orientation of the voltage-sensor paddle formed by S3 and S4 within the membrane. A transmembrane electric field that is positive inside would push the positively charged S4 segment outwards, thereby opening the pore, while a field that is negative inside would pull the S4 segment inwards and close the pore. Changes in the position and orientation of S4 are then transmitted to the activation gate formed by the inner helix bundle via the S4-S5 linker region. {ECO:0000250|UniProtKB:P63142}. +P63250 KCNJ3_MOUSE G protein-activated inward rectifier potassium channel 1 (GIRK-1) (Inward rectifier K(+) channel Kir3.1) (Potassium channel, inwardly rectifying subfamily J member 3) 501 56,573 Beta strand (15); Chain (1); Glycosylation (1); Helix (7); Intramembrane (2); Modified residue (2); Motif (1); Site (1); Topological domain (4); Transmembrane (2); Turn (4) INTRAMEM 130 141 Helical; Pore-forming; Name=H5. {ECO:0000250}.; INTRAMEM 142 148 Pore-forming. {ECO:0000250}. TRANSMEM 81 105 Helical; Name=M1. {ECO:0000250}.; TRANSMEM 158 179 Helical; Name=M2. {ECO:0000250}. TOPO_DOM 1 80 Cytoplasmic.; TOPO_DOM 106 129 Extracellular. {ECO:0000250}.; TOPO_DOM 149 157 Extracellular. {ECO:0000250}.; TOPO_DOM 180 501 Cytoplasmic. FUNCTION: This potassium channel is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. This receptor plays a crucial role in regulating the heartbeat. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SUBUNIT: Associates with GIRK2, GIRK3 or GIRK4 to form a G-protein activated heteromultimer pore-forming unit. The resulting inward current is much larger (By similarity). {ECO:0000250}. +Q9WTW3 KCNE4_MOUSE Potassium voltage-gated channel subfamily E member 4 (MinK-related peptide 3) (Minimum potassium ion channel-related peptide 3) (Potassium channel subunit beta MiRP3) 170 18,639 Chain (1); Glycosylation (2); Topological domain (1); Transmembrane (1) TRANSMEM 36 56 Helical. {ECO:0000255}. TOPO_DOM 57 170 Cytoplasmic. {ECO:0000255}. FUNCTION: Ancillary protein that assembles as a beta subunit with a voltage-gated potassium channel complex of pore-forming alpha subunits. Modulates the gating kinetics and enhances stability of the channel complex. Associated with KCNQ1/KVLTQ1 inhibits potassium current (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Interacts with KCNQ1; impairs KCNQ1 localization in lipid rafts and inhibits voltage-gated potassium channel activity. {ECO:0000250|UniProtKB:Q8WWG9}. +P58391 KCNN3_MOUSE Small conductance calcium-activated potassium channel protein 3 (SK3) (SKCa 3) (SKCa3) (KCa2.3) 732 81,333 Chain (1); Compositional bias (4); Intramembrane (1); Modified residue (1); Region (1); Sequence conflict (4); Transmembrane (6) INTRAMEM 495 515 Pore-forming; Name=Segment H5. {ECO:0000255}. TRANSMEM 289 309 Helical; Name=Segment S1. {ECO:0000255}.; TRANSMEM 316 336 Helical; Name=Segment S2. {ECO:0000255}.; TRANSMEM 367 387 Helical; Name=Segment S3. {ECO:0000255}.; TRANSMEM 406 426 Helical; Name=Segment S4. {ECO:0000255}.; TRANSMEM 455 475 Helical; Name=Segment S5. {ECO:0000255}.; TRANSMEM 524 544 Helical; Name=Segment S6. {ECO:0000255}. FUNCTION: Forms a voltage-independent potassium channel activated by intracellular calcium. Activation is followed by membrane hyperpolarization. Thought to regulate neuronal excitability by contributing to the slow component of synaptic afterhyperpolarization. The channel is blocked by apamin (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SUBUNIT: Heterooligomer. The complex is composed of 4 channel subunits each of which binds to a calmodulin subunit which regulates the channel activity through calcium-binding (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed at low levels in atrial and ventricular myocytes (at protein level). {ECO:0000269|PubMed:16055520}. +Q9D7X1 KCTD4_MOUSE BTB/POZ domain-containing protein KCTD4 259 29,978 Chain (1); Domain (1); Sequence conflict (2) +Q14B80 KCNC2_MOUSE Potassium voltage-gated channel subfamily C member 2 (Shaw-like potassium channel) (Voltage-gated potassium channel Kv3.2) 642 70,503 Chain (1); Compositional bias (1); Glycosylation (2); Modified residue (1); Motif (1); Topological domain (4); Transmembrane (6) TRANSMEM 234 254 Helical; Name=Segment S1. {ECO:0000255}.; TRANSMEM 287 307 Helical; Name=Segment S2. {ECO:0000255}.; TRANSMEM 318 338 Helical; Name=Segment S3. {ECO:0000255}.; TRANSMEM 350 372 Helical; Voltage-sensor; Name=Segment S4. {ECO:0000255}.; TRANSMEM 386 406 Helical; Name=Segment S5. {ECO:0000255}.; TRANSMEM 457 477 Helical; Name=Segment S6. {ECO:0000255}. TOPO_DOM 1 233 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 308 317 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 373 385 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 478 642 Cytoplasmic. {ECO:0000255}. FUNCTION: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain. Contributes to the regulation of the fast action potential repolarization and in sustained high-frequency firing in neurons of the central nervous system (PubMed:10561420, PubMed:10414303, PubMed:11124984, PubMed:10903572, PubMed:11506885, PubMed:15317859, PubMed:15917463, PubMed:17761775, PubMed:21414897). Homotetramer channels mediate delayed-rectifier voltage-dependent potassium currents that activate rapidly at high-threshold voltages and inactivate slowly (PubMed:10414303). Forms tetrameric channels through which potassium ions pass in accordance with their electrochemical gradient. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane (By similarity). Can form functional homotetrameric and heterotetrameric channels that contain variable proportions of KCNC1, and possibly other family members as well; channel properties depend on the type of alpha subunits that are part of the channel (PubMed:10531438, PubMed:12000114). Channel properties may be modulated by either the association with ancillary subunits, such as KCNE1, KCNE2 and KCNE3 or indirectly by nitric oxide (NO) through a cGMP- and PKG-mediated signaling cascade, slowing channel activation and deactivation of delayed rectifier potassium channels (By similarity). Contributes to fire sustained trains of very brief action potentials at high frequency in thalamocortical and suprachiasmatic nucleus (SCN) neurons, in hippocampal and neocortical interneurons and in retinal ganglion cells (PubMed:10561420, PubMed:10903572, PubMed:11506885, PubMed:17761775). Sustained maximal action potential firing frequency in inhibitory hippocampal interneurons is negatively modulated by histamine H2 receptor activation in a cAMP- and protein kinase (PKA) phosphorylation-dependent manner (PubMed:10903572). Plays a role in maintaining the fidelity of synaptic transmission in neocortical GABAergic interneurons by generating action potential (AP) repolarization at nerve terminals, thus reducing spike-evoked calcium influx and GABA neurotransmitter release (PubMed:15917463). Required for long-range synchronization of gamma oscillations over distance in the neocortex (PubMed:22539821). Contributes to the modulation of the circadian rhythm of spontaneous action potential firing in suprachiasmatic nucleus (SCN) neurons in a light-dependent manner (PubMed:21414897). {ECO:0000250|UniProtKB:P22462, ECO:0000269|PubMed:10531438, ECO:0000269|PubMed:10561420, ECO:0000269|PubMed:10903572, ECO:0000269|PubMed:11124984, ECO:0000269|PubMed:12000114, ECO:0000269|PubMed:15317859, ECO:0000269|PubMed:15917463, ECO:0000269|PubMed:17761775, ECO:0000269|PubMed:21414897, ECO:0000269|PubMed:22539821, ECO:0000305|PubMed:10414303, ECO:0000305|PubMed:11506885}. PTM: Phosphorylated by PKA in cortical synaptosomes. cAMP-dependent phosphorylation inhibits channel activity (By similarity). Histamine H2 receptor- and PKA-induced phosphorylation extends action potential spike duration, reduces action potential spike amplitude, sustains maximum firing frequency in hippocampal interneurons; also reduces the incidence of high-frequency oscillations in hippocampal CA3 pyramidal cell layers (PubMed:10903572). {ECO:0000250|UniProtKB:P63142, ECO:0000269|PubMed:10903572}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10531438, ECO:0000269|PubMed:10561420, ECO:0000269|PubMed:10903572, ECO:0000269|PubMed:11124984, ECO:0000269|PubMed:15317859, ECO:0000269|PubMed:15917463, ECO:0000269|PubMed:17761775, ECO:0000269|PubMed:21414897, ECO:0000269|PubMed:22539821}; Multi-pass membrane protein {ECO:0000255}. Membrane {ECO:0000269|PubMed:12000114}; Multi-pass membrane protein {ECO:0000255}. Perikaryon {ECO:0000269|PubMed:10531438, ECO:0000269|PubMed:10903572, ECO:0000269|PubMed:12000114, ECO:0000269|PubMed:15317859, ECO:0000269|PubMed:15852012}. Cell projection, axon {ECO:0000269|PubMed:10903572}. Cell projection, dendrite {ECO:0000269|PubMed:10531438, ECO:0000269|PubMed:10903572, ECO:0000269|PubMed:12000114, ECO:0000269|PubMed:15317859}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000269|PubMed:10531438}. Cell junction, synapse, presynaptic cell membrane {ECO:0000269|PubMed:10531438}. Cell junction, synapse, synaptosome {ECO:0000250|UniProtKB:P22462}. Cell junction, synapse {ECO:0000250|UniProtKB:P22462}. Apical cell membrane {ECO:0000250|UniProtKB:P22462}. Basolateral cell membrane {ECO:0000250|UniProtKB:P22462}. Note=Colocalizes with parvalbumin in globus pallidus neurons. Localizes in thalamocortical axons and synapses (By similarity). Localizes on the surface of cell somata, proximal dendrites and axonal membranes (PubMed:12000114, PubMed:10903572). Also detected throughout the neuropil (PubMed:12000114). Localized in starburst cell somata and proximal dendrite processes (PubMed:15317859). Colocalized with GABA in presynaptic terminals (PubMed:10531438). Clustered in patches in somatic and proximal dendritic membrane as well as in axons and presnypatic terminals of GABAergic interneurons; some of these patches are found near postsynaptic sites (PubMed:10531438). {ECO:0000250|UniProtKB:P22462, ECO:0000269|PubMed:10531438, ECO:0000269|PubMed:10903572, ECO:0000269|PubMed:12000114, ECO:0000269|PubMed:15317859}. SUBUNIT: Homotetramer and heterotetramer with other channel-forming alpha subunits, such as KCNC1 (PubMed:10531438). Interacts with KCNC1 (PubMed:10531438, PubMed:12000114). Homotetramer or heterotetramer channel activity is regulated by association with modulating ancillary subunits such as KCNE1, KCNE2 and KCNE3, creating a functionally diverse range of channel complexes. Interacts with KCNE1, KCNE2 and KCNE3 (By similarity). {ECO:0000250|UniProtKB:P22462, ECO:0000269|PubMed:10531438, ECO:0000269|PubMed:12000114}. DOMAIN: The transmembrane segment S4 functions as voltage-sensor and is characterized by a series of positively charged amino acids at every third position. Channel opening and closing is effected by a conformation change that affects the position and orientation of the voltage-sensor paddle formed by S3 and S4 within the membrane. A transmembrane electric field that is positive inside would push the positively charged S4 segment outwards, thereby opening the pore, while a field that is negative inside would pull the S4 segment inwards and close the pore. Changes in the position and orientation of S4 are then transmitted to the activation gate formed by the inner helix bundle via the S4-S5 linker region. {ECO:0000250|UniProtKB:P63142}. TISSUE SPECIFICITY: Weakly expressed in the brain at postnatal age day 7 (P7) and increased at P60 (PubMed:21912965). Not detectable in newborn hippocampus. Expressed weakly at P7 in the early developing hippocampus, increasing progressively and reaching a plateau of expression at P14 that is maintained throughout P51. Expressed in paravalbumin- and somatostain-containing inhibitory interneurons of the hippocampus; in the CA1/CA3 stratum oriens-alveus and stratum pyramidale and in cells within the hilus and subgranular layer of the dentate gyrus (DG) (PubMed:12000114, PubMed:10903572). Strongly expressed in parvalbumin (PV)-containing fast-spiking GABAergic inhibitor interneurons in deep cortical layers V and VI (PubMed:10531438). Also expressed in non-fast-spiking calbindin (CB)- and/or somatostatin (SOM)-containing interneurons in deep cortical layers V and VI (PubMed:10531438). Expressed in starburst amacrine cells of the retina in the inner nuclear layer (INL) and ganglion cell layer (GCL) (PubMed:15317859). Expressed in the suprachiasmatic nucleus (SCN) (at protein level) (PubMed:15852012, PubMed:21414897). Expressed in the early developing brain, increasing progressively until P14 (PubMed:21912965). {ECO:0000269|PubMed:10531438, ECO:0000269|PubMed:10903572, ECO:0000269|PubMed:12000114, ECO:0000269|PubMed:15317859, ECO:0000269|PubMed:15852012, ECO:0000269|PubMed:21414897, ECO:0000269|PubMed:21912965}. +Q63959 KCNC3_MOUSE Potassium voltage-gated channel subfamily C member 3 (KSHIIID) (Voltage-gated potassium channel subunit Kv3.3) 769 82,143 Alternative sequence (1); Chain (1); Compositional bias (6); Glycosylation (3); Modified residue (8); Motif (1); Mutagenesis (2); Region (1); Sequence conflict (8); Topological domain (4); Transmembrane (6) TRANSMEM 291 309 Helical; Name=Segment S1. {ECO:0000255}.; TRANSMEM 351 370 Helical; Name=Segment S2. {ECO:0000255}.; TRANSMEM 380 398 Helical; Name=Segment S3. {ECO:0000255}.; TRANSMEM 412 434 Helical; Voltage-sensor; Name=Segment S4. {ECO:0000255}.; TRANSMEM 448 469 Helical; Name=Segment S5. {ECO:0000255}.; TRANSMEM 518 539 Helical; Name=Segment S6. {ECO:0000255}. TOPO_DOM 1 290 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 371 379 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 435 447 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 540 769 Cytoplasmic. {ECO:0000255}. FUNCTION: Voltage-gated potassium channel that plays an important role in the rapid repolarization of fast-firing brain neurons. The channel opens in response to the voltage difference across the membrane, forming a potassium-selective channel through which potassium ions pass in accordance with their electrochemical gradient. The channel displays rapid activation and inactivation kinetics (PubMed:18539595, PubMed:26997484, PubMed:24218544). It plays a role in the regulation of the frequency, shape and duration of action potentials in Purkinje cells (PubMed:15217387, PubMed:18448641, PubMed:24218544). Required for normal survival of cerebellar neurons, probably via its role in regulating the duration and frequency of action potentials that in turn regulate the activity of voltage-gated Ca(2+) channels and cellular Ca(2+) homeostasis (PubMed:24218544). Required for normal motor function (PubMed:16923152, PubMed:18448641). Plays a role in the reorganization of the cortical actin cytoskeleton and the formation of actin veil structures in neuronal growth cones via its interaction with HAX1 and the Arp2/3 complex (PubMed:26997484). {ECO:0000269|PubMed:15217387, ECO:0000269|PubMed:16923152, ECO:0000269|PubMed:18448641, ECO:0000269|PubMed:18539595, ECO:0000269|PubMed:24218544, ECO:0000269|PubMed:26997484}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q14003}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15217387, ECO:0000269|PubMed:18448641, ECO:0000269|PubMed:18539595, ECO:0000269|PubMed:24218544, ECO:0000269|PubMed:26997484}; Multi-pass membrane protein {ECO:0000255}. Cell junction, synapse, presynaptic cell membrane {ECO:0000269|PubMed:26997484}; Multi-pass membrane protein {ECO:0000255}. Perikaryon {ECO:0000269|PubMed:15217387}. Cell projection, axon {ECO:0000269|PubMed:15217387}. Cell projection, dendrite {ECO:0000269|PubMed:15217387}. Cell projection, dendritic spine membrane {ECO:0000250|UniProtKB:Q01956}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q14003}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q14003}. Note=Detected on Purkinje cell dendritic spines (By similarity). Detected at presynaptic calices of Held (PubMed:26997484). Colocalizes with the cortical actin cytoskeleton and the Arp2/3 complex (By similarity). {ECO:0000250|UniProtKB:Q01956, ECO:0000250|UniProtKB:Q14003}. SUBUNIT: Homotetramer. Heterotetramer with KCNC1 (By similarity). Interacts (via C-terminus) with HAX1. Identified in a complex with ACTR3, a subunit of the Arp2/3 complex; this interaction is indirect and depends on the presence of HAX1. Interaction with HAX1 modulates channel gating (PubMed:26997484). {ECO:0000250|UniProtKB:Q14003, ECO:0000269|PubMed:26997484}. DOMAIN: The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position. {ECO:0000305}.; DOMAIN: The cytoplasmic N-terminus mediates N-type inactivation. {ECO:0000269|PubMed:18539595}.; DOMAIN: The C-terminal cytoplasmic tail contributes to the regulation of channel inactivation and to the interaction with HAX1 and the Arp2/3 complex. {ECO:0000269|PubMed:26997484}. TISSUE SPECIFICITY: Detected on Purkinje cells in the dentate, interposed and medial nucleus in cerebellum (PubMed:15217387, PubMed:18448641). Detected in brainstem (PubMed:18539595). Detected at calyces of Held in the auditory brain stem (at protein level) (PubMed:26997484). Isoform KV3.3B is highly enriched in the brain, particularly in the cerebellum, where its expression is confined to Purkinje cells and deep cerebellar nuclei. Isoform KV3.3A is not expressed in cerebellum. {ECO:0000269|PubMed:15217387, ECO:0000269|PubMed:18448641, ECO:0000269|PubMed:18539595, ECO:0000269|PubMed:26997484, ECO:0000269|PubMed:8301351}. +Q9D306 MGT4C_MOUSE Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase C (EC 2.4.1.145) (N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase IVc) (GnT-IVc) (N-acetylglucosaminyltransferase IVc) (UDP-N-acetylglucosamine: alpha-1,3-D-mannoside beta-1,4-N-acetylglucosaminyltransferase IVc) 478 56,250 Chain (1); Glycosylation (2); Topological domain (2); Transmembrane (1) TRANSMEM 26 43 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 25 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 44 478 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Glycosyltransferase that participates in the transfer of N-acetylglucosamine (GlcNAc) to the core mannose residues of N-linked glycans. Catalyzes the formation of the GlcNAcbeta1-4 branch on the GlcNAcbeta1-2Manalpha1-3 arm of the core structure of N-linked glycans. Essential for the production of tri- and tetra-antennary N-linked sugar chains. Does not catalyze the transfer of GlcNAc to the Manalpha1-6 arm to form GlcNAcBeta1-4Manalpha1-6 linkage ('GnT-VI' activity) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. +A6H684 MGT4E_MOUSE Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase-like protein MGAT4E (EC 2.4.1.-) 439 49,986 Alternative sequence (1); Chain (1); Compositional bias (1); Erroneous initiation (2); Frameshift (1); Sequence conflict (10) Protein modification; protein glycosylation. FUNCTION: Glycosyltransferase-like protein that may participate in the transfer of N-acetylglucosamine (GlcNAc) to the core mannose residues of N-linked glycans. {ECO:0000250}. +Q8R4G6 MGT5A_MOUSE Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase A (EC 2.4.1.155) (Alpha-mannoside beta-1,6-N-acetylglucosaminyltransferase) (GlcNAc-T V) (GNT-V) (Mannoside acetylglucosaminyltransferase 5) (N-acetylglucosaminyl-transferase V) [Cleaved into: Secreted alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase A (Secreted beta-1,6-N-acetylglucosaminyltransferase V) (Secreted GNT-V)] 740 84,551 Binding site (2); Chain (2); Disulfide bond (9); Glycosylation (6); Region (2); Topological domain (2); Transmembrane (1) TRANSMEM 14 30 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 13 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 31 740 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Catalyzes the addition of N-acetylglucosamine (GlcNAc) in beta 1-6 linkage to the alpha-linked mannose of biantennary N-linked oligosaccharides (PubMed:10700233, PubMed:14561752, PubMed:22715095). Catalyzes an important step in the biosynthesis of branched, complex-type N-glycans, such as those found on EGFR, TGFR (TGF-beta receptor) and CDH2 (PubMed:12122020, PubMed:10700233, PubMed:14561752, PubMed:15459394, PubMed:22715095). Via its role in the biosynthesis of complex N-glycans, plays an important role in the activation of cellular signaling pathways, reorganization of the actin cytoskeleton, cell-cell adhesion and cell migration (PubMed:10700233, PubMed:14561752, PubMed:15459394). MGAT5-dependent EGFR N-glycosylation enhances the interaction between EGFR and LGALS3 and thereby prevents rapid EGFR endocytosis and prolongs EGFR signaling (PubMed:15459394). Required for efficient interaction between TGFB1 and its receptor (PubMed:15459394). Enhances activation of intracellular signaling pathways by several types of growth factors, including FGF2, PDGF, IGF, TGFB1 and EGF (PubMed:15459394). MGAT5-dependent CDH2 N-glycosylation inhibits CDH2-mediated homotypic cell-cell adhesion and contributes to the regulation of downstream signaling pathways (PubMed:14561752). Promotes cell migration (PubMed:14561752, PubMed:15459394). Contributes to the regulation of the inflammatory response (PubMed:11217864, PubMed:15459394). MGAT5-dependent TCR N-glycosylation enhances the interaction between TCR and LGALS3, limits agonist-induced TCR clustering, and thereby dampens TCR-mediated responses to antigens (PubMed:11217864). Required for normal leukocyte evasation and accumulation at sites of inflammation (PubMed:15459394). Inhibits attachment of monocytes to the vascular endothelium and subsequent monocyte diapedesis (By similarity). {ECO:0000250|UniProtKB:Q09328, ECO:0000269|PubMed:10700233, ECO:0000269|PubMed:11217864, ECO:0000269|PubMed:12122020, ECO:0000269|PubMed:14561752, ECO:0000269|PubMed:15459394, ECO:0000269|PubMed:22715095}.; FUNCTION: Secreted alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase A: Promotes proliferation of umbilical vein endothelial cells and angiogenesis, at least in part by promoting the release of the growth factor FGF2 from the extracellular matrix. {ECO:0000250|UniProtKB:Q09328}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q09328}.; PTM: A secreted form is released from the membrane after cleavage by gamma-secretase. {ECO:0000250|UniProtKB:Q09328}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:P97259}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q09328}. Perikaryon {ECO:0000269|PubMed:10700233}.; SUBCELLULAR LOCATION: Secreted alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase A: Secreted {ECO:0000250|UniProtKB:Q09328}. TISSUE SPECIFICITY: Detected in cerebellum. {ECO:0000269|PubMed:10700233}. +Q765H6 MGT5B_MOUSE Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase B (EC 2.4.1.-) (EC 2.4.1.155) (Alpha-mannoside beta-1,6-N-acetylglucosaminyltransferase B) (GlcNAc-T Vb) (GNT-Vb) (Mannoside acetylglucosaminyltransferase 5B) (N-acetylglucosaminyl-transferase Vb) (N-acetylglucosaminyltransferase IX) (GNT-IX) 792 89,473 Alternative sequence (3); Chain (1); Disulfide bond (9); Glycosylation (2); Topological domain (2); Transmembrane (1) TRANSMEM 25 45 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 24 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 46 792 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Glycosyltransferase that acts on alpha-linked mannose of N-glycans and O-mannosyl glycans. Catalyzes the transfer of N-acetylglucosamine (GlcNAc) to the beta 1-6 linkage of the mannose residue of GlcNAc-beta1,2-Man-alpha on both the alpha1,3- and alpha1,6-linked mannose arms in the core structure of N-glycan (By similarity). Also acts on the GlcNAc-beta1,2-Man-alpha1-Ser/Thr moiety, forming a 2,6-branched structure in brain O-mannosyl glycan (PubMed:22715095). Plays an active role in modulating integrin and laminin-dependent adhesion and migration of neuronal cells via its activity in the O-mannosyl glycan pathway. {ECO:0000250|UniProtKB:Q3V5L5, ECO:0000269|PubMed:22715095}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:16413118}; Single-pass type II membrane protein {ECO:0000269|PubMed:16413118}. TISSUE SPECIFICITY: Present in brain (at protein level) (PubMed:16413118). Predominantly expressed in hippocampus, superficial layers of the brain cortex, striatum, nucleus accumbens, a subset of nuclei in the thalamus, inferior colliculus, brain stem and cerebellum (PubMed:16413118, PubMed:22715095). {ECO:0000269|PubMed:16413118, ECO:0000269|PubMed:22715095}. +Q9CWU5 KHDC3_MOUSE KH domain-containing protein 3 (Protein Filia) 440 47,995 Alternative sequence (3); Beta strand (5); Chain (1); Compositional bias (1); Domain (1); Helix (6); Region (1) FUNCTION: Required for maintenance of euploidy during cleavage-stage embryogenesis. Ensures proper spindle assembly by regulating the localization of AURKA via RHOA signaling and of PLK1 via a RHOA-independent process. Required for the localization of MAD2L1 to kinetochores to enable spindle assembly checkpoint function. Capable of binding RNA. {ECO:0000269|PubMed:19376971, ECO:0000269|PubMed:22276159}. SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000269|PubMed:18057100, ECO:0000269|PubMed:18804437}. Note=Located throughout the cell cortex of ovulated eggs in a complex with NLRP5. After fertilization, restricted to the apical cortex and excluded from regions of cell-cell contact. {ECO:0000269|PubMed:18057100}. SUBUNIT: Component of the subcortical maternal complex (SCMC) which is essential for progression of zygotes beyond the first embryonic cell division. The complex also contains NLRP5, OOEP and TLE6. Within the complex, interacts with NLRP5. {ECO:0000269|PubMed:18057100, ECO:0000269|PubMed:18804437}. DOMAIN: Contains 1 atypical KH domain, which is still capable of binding RNA. {ECO:0000269|PubMed:22276159}. TISSUE SPECIFICITY: Detected in ovary, but not in testis or somatic tissues. In the ovary, expressed in growing oocytes. {ECO:0000269|PubMed:18057100}. +Q3UWR2 KHD1A_MOUSE KH homology domain-containing protein 1A (Nur77 downstream gene 1 protein) 166 19,690 Chain (1); Domain (1); Sequence conflict (2) FUNCTION: Has pro-apoptotic activity. {ECO:0000269|PubMed:14657025}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14657025}. +Q99PT9 KIF19_MOUSE Kinesin-like protein KIF19 997 111,559 Beta strand (15); Chain (1); Coiled coil (2); Domain (1); Helix (12); Nucleotide binding (1); Sequence conflict (1); Turn (2) FUNCTION: Plus end-directed microtubule-dependent motor protein that regulates the length of motile cilia by mediating depolymerization of microtubules at ciliary tips. {ECO:0000269|PubMed:23168168}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305|PubMed:23168168}. Cell projection, cilium {ECO:0000269|PubMed:23168168}. Note=Localizes to cilia tips. TISSUE SPECIFICITY: Strongly expressed in the oviduct and trachea. Expressed in testis, lung, ovary and brain. {ECO:0000269|PubMed:11416179, ECO:0000269|PubMed:23168168}. +Q9QXL1 KI21B_MOUSE Kinesin-like protein KIF21B (Kinesin-like protein KIF6) 1668 186,180 Chain (1); Coiled coil (2); Domain (1); Modified residue (7); Mutagenesis (1); Nucleotide binding (1); Region (1); Repeat (7); Sequence conflict (1) FUNCTION: Plus-end directed microtubule-dependent motor protein which displays processive activity (PubMed:27117409, PubMed:10225949). Is involved in regulation of microtubule dynamics, synapse function and neuronal morphology, including dendritic tree branching and spine formation (PubMed:27117409). Plays a role in lerning and memory (PubMed:27117409). Involved in delivery of gamma-aminobutyric acid (GABA(A)) receptor to cell surface (PubMed:25172774). {ECO:0000269|PubMed:10225949, ECO:0000269|PubMed:25172774, ECO:0000269|PubMed:27117409}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10225949}. Cell projection, dendrite {ECO:0000269|PubMed:10225949, ECO:0000269|PubMed:24086586, ECO:0000269|PubMed:25172774, ECO:0000269|PubMed:27117409}. Cell projection, growth cone {ECO:0000269|PubMed:24086586}. Cell projection, axon {ECO:0000269|PubMed:10225949}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:F1M5N7}. SUBUNIT: Interacts with TRIM3; the interaction positively affects motility of KIF21B (PubMed:24086586). Interacts with GABARAP and GABA(A) receptor subunits: GABRG2, GABRA1 and GABRA2 (By similarity). May interact with GABA(A) receptor subunits: GABRB2 and GABRB3 (By similarity). {ECO:0000250|UniProtKB:F1M5N7, ECO:0000269|PubMed:24086586}. TISSUE SPECIFICITY: Expressed in brain (at protein level) (PubMed:27117409, PubMed:25172774). Expressed in spleen and at lower levels in testes (PubMed:10225949). {ECO:0000269|PubMed:10225949, ECO:0000269|PubMed:25172774, ECO:0000269|PubMed:27117409}. +Q6P9P6 KIF11_MOUSE Kinesin-like protein KIF11 (Kinesin-related motor protein Eg5) 1052 118,027 Chain (1); Coiled coil (2); Cross-link (1); Domain (1); Modified residue (3); Nucleotide binding (1); Sequence conflict (6) FUNCTION: Motor protein required for establishing a bipolar spindle during mitosis. Required in non-mitotic cells for transport of secretory proteins from the Golgi complex to the cell surface. {ECO:0000250|UniProtKB:P52732}. PTM: Phosphorylated exclusively on serine during S phase, but on both serine and Thr-925 during mitosis, so controlling the association of KIF11 with the spindle apparatus (probably during early prophase). {ECO:0000250|UniProtKB:P52732}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P52732}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:P52732}. SUBUNIT: Interacts with the thyroid hormone receptor in the presence of thyroid hormone. Component of a large chromatin remodeling complex, at least composed of MYSM1, PCAF, RBM10 and KIF11/TRIP5. {ECO:0000250|UniProtKB:P52732}. +Q9D2Z8 KIF12_MOUSE Kinesin-like protein KIF12 642 70,706 Chain (1); Coiled coil (1); Compositional bias (1); Domain (1); Modified residue (3); Nucleotide binding (1); Sequence conflict (1) SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. +P33174 KIF4_MOUSE Chromosome-associated kinesin KIF4 (Chromokinesin) 1231 139,519 Beta strand (17); Chain (1); Coiled coil (1); Domain (1); Helix (13); Modified residue (7); Nucleotide binding (1); Region (1); Sequence conflict (3); Turn (5) FUNCTION: Required for mitotic chromosomal positioning and bipolar spindle stabilization. {ECO:0000269|PubMed:7929562}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:7929562}. Chromosome {ECO:0000269|PubMed:7929562}. Cytoplasm, cytoskeleton {ECO:0000305|PubMed:7929562}. Note=Associated with mitotic chromosomes. TISSUE SPECIFICITY: Expressed in pyramidal cells in juvenile hippocampus, granular cells in juvenile cerebellar cortex and in adult spleen. {ECO:0000269|PubMed:7929562}. +P33175 KIF5A_MOUSE Kinesin heavy chain isoform 5A (Kinesin heavy chain neuron-specific 1) (Neuronal kinesin heavy chain) (NKHC) 1027 117,019 Chain (1); Coiled coil (1); Domain (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (2); Mutagenesis (1); Nucleotide binding (1); Region (4); Sequence conflict (5) FUNCTION: Microtubule-dependent motor required for slow axonal transport of neurofilament proteins (NFH, NFM and NFL) (PubMed:12682084). Can induce formation of neurite-like membrane protrusions in non-neuronal cells in a ZFYVE27-dependent manner. The ZFYVE27-KIF5A complex contributes to the vesicular transport of VAPA, VAPB, SURF4, RAB11A, RAB11B and RTN3 proteins in neurons (PubMed:21976701). Required for anterograde axonal transportation of MAPK8IP3/JIP3 which is essential for MAPK8IP3/JIP3 function in axon elongation (By similarity). {ECO:0000250|UniProtKB:Q6QLM7, ECO:0000269|PubMed:12682084, ECO:0000269|PubMed:21976701}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Cytoplasm, cytoskeleton. Note=Concentrated in the cell body of the neurons, particularly in the perinuclear region. SUBUNIT: Oligomer composed of two heavy chains and two light chains. Interacts with GRIP1 (PubMed:11986669). Interacts with FMR1 (via C-terminus); this interaction is increased in a mGluR-dependent manner (PubMed:18539120). Interacts with BORCS5 (By similarity). Interacts with ZFYVE27 (PubMed:21976701, PubMed:24251978). Interacts with VAPA, VAPB, SURF4, RAB11A (GDP-bound form), RAB11B (GDP-bound form) and RTN3 in a ZFYVE27-dependent manner (PubMed:21976701). Interacts with BICD2 (By similarity). {ECO:0000250|UniProtKB:Q12840, ECO:0000269|PubMed:11986669, ECO:0000269|PubMed:18539120, ECO:0000269|PubMed:21976701, ECO:0000269|PubMed:24251978}. DOMAIN: Composed of three structural domains: a large globular N-terminal domain which is responsible for the motor activity of kinesin (it hydrolyzes ATP and binds microtubule), a central alpha-helical coiled coil domain that mediates the heavy chain dimerization; and a small globular C-terminal domain which interacts with other proteins (such as the kinesin light chains), vesicles and membranous organelles. +P28738 KIF5C_MOUSE Kinesin heavy chain isoform 5C (Kinesin heavy chain neuron-specific 2) 956 109,275 Beta strand (17); Chain (1); Coiled coil (1); Domain (1); Helix (11); Modified residue (1); Nucleotide binding (1); Region (2); Sequence caution (1); Sequence conflict (2); Turn (5) FUNCTION: Involved in synaptic transmission (By similarity). Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. Mediates dendritic trafficking of mRNAs (PubMed:19608740). Required for anterograde axonal transportation of MAPK8IP3/JIP3 which is essential for MAPK8IP3/JIP3 function in axon elongation (By similarity). {ECO:0000250|UniProtKB:O60282, ECO:0000250|UniProtKB:P56536, ECO:0000269|PubMed:19608740}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. Cell projection, dendrite {ECO:0000250|UniProtKB:O60282}. Note=Abundant in distal regions of dendrites. {ECO:0000250|UniProtKB:O60282}. SUBUNIT: Oligomer composed of two heavy chains and two light chains (PubMed:15286375). Interacts with GRIP1 (PubMed:11986669). Interacts with KLC3 and TRAK1 (By similarity). Interacts with ZFYVE27 (PubMed:21976701). {ECO:0000250|UniProtKB:O60282, ECO:0000250|UniProtKB:P56536, ECO:0000269|PubMed:11986669, ECO:0000269|PubMed:15286375, ECO:0000269|PubMed:21976701}. DOMAIN: Composed of three structural domains: a large globular N-terminal domain which is responsible for the motor activity of kinesin (it hydrolyzes ATP and binds microtubule), a central alpha-helical coiled coil domain that mediates the heavy chain dimerization; and a small globular C-terminal domain which interacts with other proteins (such as the kinesin light chains), vesicles and membranous organelles. +B7ZNG0 KIF7_MOUSE Kinesin-like protein KIF7 1348 151,624 Alternative sequence (1); Chain (1); Coiled coil (3); Compositional bias (1); Domain (1); Modified residue (1); Mutagenesis (1); Nucleotide binding (1); Region (2); Sequence conflict (1) FUNCTION: Essential for hedgehog signaling regulation: acts as both a negative and positive regulator of sonic hedgehog (Shh) and Indian hedgehog (Ihh) pathways, acting downstream of SMO, through both SUFU-dependent and -independent mechanisms. Involved in the regulation of microtubular dynamics. Required for proper organization of the ciliary tip and control of ciliary localization of SUFU-GLI2 complexes. Required for localization of GLI3 to cilia in response to Shh. Negatively regulates Shh signaling by preventing inappropriate activation of the transcriptional activator GLI2 in the absence of ligand. Positively regulates Shh signaling by preventing the processing of the transcription factor GLI3 into its repressor form. In keratinocytes, promotes the dissociation of SUFU-GLI2 complexes, GLI2 nuclear translocation and Shh signaling activation. Involved in the regulation of epidermal differentiation and chondrocyte development. {ECO:0000269|PubMed:19549984, ECO:0000269|PubMed:19592253, ECO:0000269|PubMed:19666503, ECO:0000269|PubMed:21795282, ECO:0000269|PubMed:23034632, ECO:0000269|PubMed:24952464}. PTM: Polyubiquitinated by UBR3. {ECO:0000269|PubMed:27195754}. SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000269|PubMed:19666503, ECO:0000269|PubMed:24952464, ECO:0000269|PubMed:25644602}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:25644602}. Note=Localizes to the cilium tip. SUBUNIT: Can form homodimers and interacts with microtubules (PubMed:24952464). Interacts with GLI1 and SMO (By similarity). Interacts with GLI2, GLI3 and SUFU (PubMed:19549984). Interacts with NPHP1 (By similarity). Interacts with SMO and DLG5 (via PDZ4 or guanylate kinase-like domain) (PubMed:25644602). {ECO:0000250|UniProtKB:Q2M1P5, ECO:0000269|PubMed:19549984, ECO:0000269|PubMed:24952464, ECO:0000269|PubMed:25644602}. TISSUE SPECIFICITY: Expressed in heart, lung, liver, kidney, testis, spleen and cerebellum. {ECO:0000269|PubMed:21633164}. +P70188 KIFA3_MOUSE Kinesin-associated protein 3 (KAP-3) (KAP3) 793 91,291 Alternative sequence (1); Chain (1); Modified residue (1); Repeat (5) FUNCTION: Involved in tethering the chromosomes to the spindle pole and in chromosome movement. Binds to the tail domain of the KIF3A/KIF3B heterodimer to form a heterotrimeric KIF3 complex and may regulate the membrane binding of this complex. PTM: Phosphorylated on tyrosine residues by SRC in vitro; this reduces the binding affinity of the protein for RAP1GDS1. {ECO:0000250}. SUBUNIT: Interacts with SMC3 subunit of the cohesin complex (By similarity). Heterotrimer of KIFAP3, KIF3A and KIF3B. Interacts with RAP1GDS1/SMG GDS. {ECO:0000250}. +Q9JJR9 NRIP3_MOUSE Nuclear receptor-interacting protein 3 240 26,879 Chain (1); Sequence conflict (1) +Q91W63 NRK1_MOUSE Nicotinamide riboside kinase 1 (NRK 1) (NmR-K 1) (EC 2.7.1.22) (Nicotinic acid riboside kinase 1) (EC 2.7.1.173) (Ribosylnicotinamide kinase 1) (RNK 1) (Ribosylnicotinic acid kinase 1) 195 22,303 Active site (1); Binding site (2); Chain (1); Metal binding (2); Nucleotide binding (3); Region (3) Cofactor biosynthesis; NAD(+) biosynthesis. FUNCTION: Catalyzes the phosphorylation of nicotinamide riboside (NR) and nicotinic acid riboside (NaR) to form nicotinamide mononucleotide (NMN) and nicotinic acid mononucleotide (NaMN). {ECO:0000250|UniProtKB:Q9NWW6}. SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9NWW6}. +P0DI97 NRX1B_MOUSE Neurexin-1-beta (Neurexin I-beta) 468 50,223 Chain (1); Compositional bias (3); Domain (1); Metal binding (4); Mutagenesis (2); Region (1); Signal peptide (1); Transmembrane (1) TRANSMEM 393 413 Helical. {ECO:0000255}. FUNCTION: Neuronal cell surface protein that may be involved in cell recognition and cell adhesion by forming intracellular junctions through binding to neuroligins. May play a role in formation or maintenance of synaptic junctions. May mediate intracellular signaling. May play a role in angiogenesis (By similarity). {ECO:0000250}. PTM: Highly O-glycosylated and minor N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Cell junction, synapse. Note=Localized on the pre-synaptic membrane. {ECO:0000250}. SUBUNIT: The cytoplasmic C-terminal region binds to CASK. Binds NLGN1, NLGN2 and NLGN3, DAG1 (alpha-dystroglycan) and alpha-latrotoxin. Binding to neuroligins is calcium-dependent, and the binding preference ranks as follow: NLGN1 > NLGN4 >> NLGN3 > NLGN2 (By similarity). Interacts with CBLN2 and more weakly with CBLN4 (PubMed:22220752). Interacts with CBLN1; interaction is CBLN1 hexamer form-dependent; CBLN1-binding is calcium-independent; isoform 1b does not interact with CBLN1 (PubMed:21410790, PubMed:22220752). {ECO:0000250|UniProtKB:Q63373, ECO:0000269|PubMed:21410790, ECO:0000269|PubMed:22220752}. +Q9CZ44 NSF1C_MOUSE NSFL1 cofactor p47 (p97 cofactor p47) 370 40,710 Alternative sequence (3); Chain (1); Compositional bias (1); Domain (2); Modified residue (8); Motif (2); Sequence conflict (1) FUNCTION: Reduces the ATPase activity of VCP. Necessary for the fragmentation of Golgi stacks during mitosis and for VCP-mediated reassembly of Golgi stacks after mitosis. May play a role in VCP-mediated formation of transitional endoplasmic reticulum (tER). Inhibits the activity of CTSL (in vitro). Together with UBXN2B/p37, regulates the centrosomal levels of kinase AURKA/Aurora A during mitotic progression by promoting AURKA removal from centrosomes in prophase. Also, regulates spindle orientation during mitosis. {ECO:0000250|UniProtKB:O35987, ECO:0000250|UniProtKB:Q9UNZ2}. PTM: Phosphorylated during mitosis. Phosphorylation inhibits interaction with Golgi membranes and is required for the fragmentation of the Golgi stacks during mitosis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O35987}. Golgi apparatus, Golgi stack {ECO:0000250|UniProtKB:O35987}. Chromosome {ECO:0000250|UniProtKB:O35987}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:O35987}. Note=Predominantly nuclear in interphase cells. Bound to the axial elements of sex chromosomes in pachytene spermatocytes. A small proportion of the protein is cytoplasmic, associated with Golgi stacks. Localizes to centrosome during mitotic prophase and metaphase. {ECO:0000250|UniProtKB:O35987}. SUBUNIT: Part of a ternary complex containing STX5A, NSFL1C and VCP. NSFL1C forms a homotrimer that binds to one end of a VCP homohexamer. The complex binds to membranes enriched in phosphatidylethanolamine-containing lipids and promotes Golgi membrane fusion. Interaction with VCIP135 leads to dissociation of the complex via ATP hydrolysis by VCP. Binds ubiquitin and mono-ubiquitinated proteins via its N-terminal UBA-like domain when bound to VCP (By similarity). {ECO:0000250}. +E0CYR6 NT8F7_MOUSE N-acetyltransferase family 8 member 7 (EC 2.3.1.48) 227 26,101 Chain (1); Compositional bias (1); Domain (1); Transmembrane (2) TRANSMEM 36 56 Helical. {ECO:0000255}.; TRANSMEM 58 78 Helical. {ECO:0000255}. FUNCTION: Has histone acetyltransferase activity in vitro, with specificity for histone H4. {ECO:0000269|PubMed:25123547}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. +O35595 PTC2_MOUSE Protein patched homolog 2 (PTC2) 1182 128,586 Chain (1); Domain (1); Glycosylation (2); Topological domain (13); Transmembrane (12) TRANSMEM 58 78 Helical. {ECO:0000255}.; TRANSMEM 395 414 Helical. {ECO:0000255}.; TRANSMEM 429 449 Helical. {ECO:0000255}.; TRANSMEM 458 478 Helical. {ECO:0000255}.; TRANSMEM 502 522 Helical. {ECO:0000255}.; TRANSMEM 532 552 Helical. {ECO:0000255}.; TRANSMEM 687 707 Helical. {ECO:0000255}.; TRANSMEM 964 984 Helical. {ECO:0000255}.; TRANSMEM 992 1012 Helical. {ECO:0000255}.; TRANSMEM 1014 1034 Helical. {ECO:0000255}.; TRANSMEM 1065 1085 Helical. {ECO:0000255}.; TRANSMEM 1087 1107 Helical. {ECO:0000255}. TOPO_DOM 1 57 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 79 394 Extracellular. {ECO:0000255}.; TOPO_DOM 415 428 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 450 457 Extracellular. {ECO:0000255}.; TOPO_DOM 479 501 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 523 531 Extracellular. {ECO:0000255}.; TOPO_DOM 553 686 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 708 963 Extracellular. {ECO:0000255}.; TOPO_DOM 985 991 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1013 1013 Extracellular. {ECO:0000255}.; TOPO_DOM 1035 1064 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1086 1086 Extracellular. {ECO:0000255}.; TOPO_DOM 1108 1182 Cytoplasmic. {ECO:0000255}. FUNCTION: May have a role in epidermal development. May act as a receptor for Sonic hedgehog (SHH). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed in epithelial cells of the developing hair, tooth and whisker. +Q64697 PTCA_MOUSE Protein tyrosine phosphatase receptor type C-associated protein (PTPRC-associated protein) (CD45-associated protein) (CD45-AP) (LSM-1) 197 20,371 Chain (1); Erroneous initiation (1); Modified residue (2); Sequence conflict (1); Transmembrane (1) TRANSMEM 33 53 Helical. {ECO:0000255}. PTM: Phosphorylated on tyrosine residues. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. SUBUNIT: Interacts with CD45/PTPRC. TISSUE SPECIFICITY: Leukocyte-specific. Expressed in B- and T-cell lines, in spleen, thymus, and bone marrow of adult mice, and in embryos. +Q8R3K3 PTCD2_MOUSE Pentatricopeptide repeat-containing protein 2, mitochondrial 381 43,844 Chain (1); Frameshift (1); Modified residue (1); Repeat (1); Sequence caution (1) FUNCTION: Involved in mitochondrial RNA maturation and mitochondrial respiratory chain function. {ECO:0000269|PubMed:18729827}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:18729827}. TISSUE SPECIFICITY: High expression in heart and liver and low expression in kidney, brain and testis. {ECO:0000269|PubMed:18729827}. +Q9JK30 ORC3_MOUSE Origin recognition complex subunit 3 (Origin recognition complex subunit Latheo) 715 82,342 Alternative sequence (1); Chain (1); Modified residue (2); Sequence conflict (6) FUNCTION: Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. The specific DNA sequences that define origins of replication have not been identified yet. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication (By similarity). Binds histone H3 and H4 trimethylation marks H3K9me3, H3K27me3 and H4K20me3 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Component of ORC, a complex composed of at least 6 subunits: ORC1, ORC2, ORC3, ORC4, ORC5 and ORC6. ORC is regulated in a cell-cycle dependent manner. It is sequentially assembled at the exit from anaphase of mitosis and disassembled as cells enter S phase (By similarity). {ECO:0000250}. +Q14C51 PTCD3_MOUSE Pentatricopeptide repeat domain-containing protein 3, mitochondrial (28S ribosomal protein S39, mitochondrial) (MRP-S39) 685 77,796 Chain (1); Erroneous initiation (1); Modified residue (1); Repeat (10); Sequence conflict (5); Transit peptide (1) FUNCTION: Mitochondrial RNA-binding protein that has a role in mitochondrial translation. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. SUBUNIT: Component of the mitochondrial ribosome small subunit (28S) which comprises a 12S rRNA and about 30 distinct proteins. Associated with the 12S mitochondrial rRNA (12S mt-rRNA) (By similarity). {ECO:0000250}. +Q9WUJ8 ORC6_MOUSE Origin recognition complex subunit 6 262 29,188 Chain (1); Cross-link (1); Modified residue (1) FUNCTION: Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. The specific DNA sequences that define origins of replication have not been identified yet. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of ORC, a complex composed of at least 6 subunits: ORC1, ORC2, ORC3, ORC4, ORC5 and ORC6. ORC is regulated in a cell-cycle dependent manner. It is sequentially assembled at the exit from anaphase of mitosis and disassembled as cells enter S phase (By similarity). Interacts with DBF4. {ECO:0000250, ECO:0000269|PubMed:12614612}. +O55241 OREX_MOUSE Orexin (Hypocretin) (Hcrt) [Cleaved into: Orexin-A (Hypocretin-1) (Hcrt1); Orexin-B (Hypocretin-2) (Hcrt2)] 130 13,503 Disulfide bond (2); Modified residue (3); Peptide (2); Propeptide (1); Signal peptide (1) FUNCTION: Neuropeptides that play a significant role in the regulation of food intake and sleep-wakefulness, possibly by coordinating the complex behavioral and physiologic responses of these complementary homeostatic functions. A broader role in the homeostatic regulation of energy metabolism, autonomic function, hormonal balance and the regulation of body fluids, is also suggested. Orexin-A binds to both OX1R and OX2R with a high affinity, whereas orexin-B binds only to OX2R with a similar high affinity. PTM: Specific enzymatic cleavages at paired basic residues yield the different active peptides. SUBCELLULAR LOCATION: Rough endoplasmic reticulum {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Cell junction, synapse {ECO:0000250}. Note=Associated with perikaryal rough endoplasmic reticulum as well as cytoplasmic large granular vesicles at synapses. {ECO:0000250}. TISSUE SPECIFICITY: Restricted to neuronal cell bodies of the dorsal and lateral hypothalamus. +Q8K2C7 OS9_MOUSE Protein OS-9 672 76,108 Alternative sequence (1); Binding site (5); Chain (1); Compositional bias (1); Disulfide bond (3); Domain (1); Glycosylation (1); Sequence conflict (2); Signal peptide (1) FUNCTION: Lectin which functions in endoplasmic reticulum (ER) quality control and ER-associated degradation (ERAD). May bind terminally misfolded non-glycosylated proteins as well as improperly folded glycoproteins, retain them in the ER, and possibly transfer them to the ubiquitination machinery and promote their degradation. Possible targets include TRPV4 (By similarity). {ECO:0000250}. PTM: Intramolecular disulfide bonds. {ECO:0000250}.; PTM: N-glycosylated. {ECO:0000269|PubMed:19084021}. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250}. SUBUNIT: Probably part of the HRD1 ubiquitin ligase complex composed at least of SYVN1/HRD1 and SEL1L with which it interacts directly. Through this complex it may interact with ERLEC1 and HSPA5. Interacts with DERL2. Interacts with HSP90B1, CREB3 and SYVN1 (By similarity). Interacts (via C-terminus) with CPNE6 (via second C2 domain); this interaction occurs in a calcium-dependent manner in vitro (PubMed:10403379). {ECO:0000250|UniProtKB:Q13438, ECO:0000269|PubMed:10403379}. +Q8VBT3 OSCAR_MOUSE Osteoclast-associated immunoglobulin-like receptor (Osteoclast-associated receptor) (mOSCAR) (Ocl178) 265 28,726 Alternative sequence (1); Chain (1); Disulfide bond (1); Domain (2); Glycosylation (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 232 248 Helical. {ECO:0000255}. TOPO_DOM 19 231 Extracellular. {ECO:0000255}.; TOPO_DOM 249 265 Cytoplasmic. {ECO:0000255}. FUNCTION: Regulator of osteoclastogenesis which plays an important bone-specific function in osteoclast differentiation. {ECO:0000269|PubMed:11805147}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Specifically expressed in preosteoclasts or mature osteoclasts. {ECO:0000269|PubMed:11805147}. +Q8BHW2 OSCP1_MOUSE Protein OSCP1 379 43,232 Chain (1); Frameshift (1) FUNCTION: May be involved in drug clearance in the placenta. {ECO:0000250}. SUBCELLULAR LOCATION: Basal cell membrane {ECO:0000250}. TISSUE SPECIFICITY: Predominantly expressed in testis. {ECO:0000269|PubMed:16006562}. +Q9D722 OSER1_MOUSE Oxidative stress-responsive serine-rich protein 1 (Oxidative stress-responsive protein 1) (Peroxide-inducible transcript 1 protein) 291 32,011 Chain (1); Compositional bias (1); Modified residue (1); Natural variant (1); Sequence conflict (3) +Q8BWU5 OSGEP_MOUSE Probable tRNA N6-adenosine threonylcarbamoyltransferase (EC 2.3.1.234) (N6-L-threonylcarbamoyladenine synthase) (t(6)A synthase) (O-sialoglycoprotein endopeptidase) (t(6)A37 threonylcarbamoyladenosine biosynthesis protein Osgep) (tRNA threonylcarbamoyladenosine biosynthesis protein Osgep) 335 36,301 Binding site (4); Chain (1); Metal binding (4); Region (1); Sequence conflict (2) FUNCTION: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. OSGEP likely plays a direct catalytic role in this reaction, but requires other protein(s) of the complex to fulfill this activity. {ECO:0000255|HAMAP-Rule:MF_03180}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03180}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03180}. SUBUNIT: Component of the EKC/KEOPS complex composed of at least GON7, TP53RK, TPRKB, OSGEP and LAGE3; the whole complex dimerizes. {ECO:0000250|UniProtKB:Q9NPF4, ECO:0000255|HAMAP-Rule:MF_03180}. TISSUE SPECIFICITY: Widely expressed at low level. Expressed at intermediate level in lung. Weakly expressed in testis, skeletal muscle, kidney, liver, spleen, brain and heart. {ECO:0000269|PubMed:12200116}. +Q8BXR9 OSBL6_MOUSE Oxysterol-binding protein-related protein 6 (ORP-6) (OSBP-related protein 6) 959 108,920 Alternative sequence (1); Chain (1); Domain (1); Initiator methionine (1); Modified residue (4); Sequence conflict (1) FUNCTION: Weakly binds 25-hydroxycholesterol. {ECO:0000250|UniProtKB:Q9BZF3}. SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000269|PubMed:14593528}. Cytoplasm, cytosol {ECO:0000269|PubMed:14593528}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:14593528}; Peripheral membrane protein {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:14593528}; Peripheral membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in skin, respiratory epithelium, small intestine epithelium, pancreas, striated muscle, brain, spinal ganglia, and nervous plexus of the intestine (at protein level). {ECO:0000269|PubMed:14593528}. +Q62130 PTN14_MOUSE Tyrosine-protein phosphatase non-receptor type 14 (EC 3.1.3.48) (Protein-tyrosine phosphatase PTP36) 1189 135,042 Active site (1); Binding site (1); Chain (1); Compositional bias (3); Domain (2); Modified residue (8); Region (1); Sequence conflict (2) FUNCTION: Protein tyrosine phosphatase which may play a role in the regulation of lymphangiogenesis, cell-cell adhesion, cell-matrix adhesion, cell migration, cell growth and also regulates TGF-beta gene expression, thereby modulating epithelial-mesenchymal transition. Mediates beta-catenin dephosphorylation at adhesion junctions. Acts as a negative regulator of the oncogenic property of YAP, a downstream target of the hippo pathway, in a cell density-dependent manner. May function as a tumor suppressor. {ECO:0000269|PubMed:20826270}. PTM: Ubiquitinated by the ECS (Elongin BC-CUL2/5-SOCS-box protein)/LRR1 E3 ligase complex and subsequently targeted to proteasomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Nucleus {ECO:0000250}. Note=Translocation into the nucleus is associated with induction of cell proliferation. Partially colocalized with actin filaments at the plasma membrane. {ECO:0000250}. SUBUNIT: Interacts with FLT4; the interaction is enhanced by stimulation with VEGFC. Interacts (via PPxY motifs) with YAP1 (via WW domains); this interaction leads to the cytoplasmic sequestration of YAP1 and inhibits its transcriptional coactivator activity. {ECO:0000250}. TISSUE SPECIFICITY: Thymus; in cells of both hematopoietic and non-hematopoietic origins. +Q61152 PTN18_MOUSE Tyrosine-protein phosphatase non-receptor type 18 (EC 3.1.3.48) (Fetal liver phosphatase 1) (FLP-1) (PTP-K1) 453 50,202 Active site (1); Binding site (2); Chain (1); Domain (1); Modified residue (2); Region (1); Sequence conflict (8) FUNCTION: May be involved in growth and differentiation of hematopoietic cells. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8977243}. Cytoplasm {ECO:0000269|PubMed:8977243}. SUBUNIT: Interacts with PSTPIP1. {ECO:0000269|PubMed:9265651}. TISSUE SPECIFICITY: Highest expression in bone marrow. Also expressed in kidney, lung, ovary, spleen, thymus and lymph node. {ECO:0000269|PubMed:8695832, ECO:0000269|PubMed:8875997, ECO:0000269|PubMed:8977243}. +Q62136 PTN21_MOUSE Tyrosine-protein phosphatase non-receptor type 21 (EC 3.1.3.48) (Protein-tyrosine phosphatase PTP-RL10) 1176 133,491 Active site (1); Binding site (2); Chain (1); Compositional bias (2); Domain (2); Modified residue (10); Region (1) FUNCTION: May be involved in the regulation of growth and differentiation of liver cells. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. TISSUE SPECIFICITY: Liver. +Q9WVG7 OSR1_MOUSE Protein odd-skipped-related 1 266 29,584 Chain (1); Modified residue (1); Zinc finger (3) FUNCTION: Transcription factor that plays a role in the regulation of embryonic heart and urogenital development. {ECO:0000269|PubMed:16223478}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q06180 PTN2_MOUSE Tyrosine-protein phosphatase non-receptor type 2 (Protein-tyrosine phosphatase PTP-2) (EC 3.1.3.48) (MPTP) 406 47,360 Active site (1); Alternative sequence (1); Binding site (2); Chain (1); Domain (1); Modified residue (10); Mutagenesis (1); Region (3) FUNCTION: Non-receptor type tyrosine-specific phosphatase that dephosphorylates receptor protein tyrosine kinases including INSR, EGFR, CSF1R, PDGFR. Also dephosphorylates non-receptor protein tyrosine kinases like JAK1, JAK2, JAK3, Src family kinases, STAT1, STAT3 and STAT6 either in the nucleus or the cytoplasm. Negatively regulates numerous signaling pathways and biological processes like hematopoiesis, inflammatory response, cell proliferation and differentiation, and glucose homeostasis. Plays a multifaceted and important role in the development of the immune system. Functions in T-cell receptor signaling through dephosphorylation of FYN and LCK to control T-cells differentiation and activation. Dephosphorylates CSF1R, negatively regulating its downstream signaling and macrophage differentiation. Negatively regulates cytokine (IL2/interleukin-2 and interferon)-mediated signaling through dephosphorylation of the cytoplasmic kinases JAK1, JAK3 and their substrate STAT1, that propagate signaling downstream of the cytokine receptors. Also regulates the IL6/interleukin-6 and IL4/interleukin-4 cytokine signaling through dephosphorylation of STAT3 and STAT6 respectively. In addition to the immune system, it is involved in anchorage-dependent, negative regulation of EGF-stimulated cell growth. Activated by the integrin ITGA1/ITGB1, it dephosphorylates EGFR and negatively regulates EGF signaling. Dephosphorylates PDGFRB and negatively regulates platelet-derived growth factor receptor-beta signaling pathway and therefore cell proliferation. Negatively regulates tumor necrosis factor-mediated signaling downstream via MAPK through SRC dephosphorylation. May also regulate the hepatocyte growth factor receptor signaling pathway through dephosphorylation of the hepatocyte growth factor receptor MET. Plays also an important role in glucose homeostasis. For instance, negatively regulates the insulin receptor signaling pathway through the dephosphorylation of INSR and control gluconeogenesis and liver glucose production through negative regulation of the IL6 signaling pathways. May also bind DNA. {ECO:0000269|PubMed:11498795, ECO:0000269|PubMed:11909529, ECO:0000269|PubMed:12138178, ECO:0000269|PubMed:14966296, ECO:0000269|PubMed:15696169, ECO:0000269|PubMed:16705167, ECO:0000269|PubMed:17210636, ECO:0000269|PubMed:20484139, ECO:0000269|PubMed:22080863, ECO:0000269|PubMed:9271584}. PTM: Isoform 2: Specifically phosphorylated in a cell cycle-dependent manner by cyclin-dependent kinases CDK1 and CDK2. Probably activated through phosphorylation by PKR. {ECO:0000250|UniProtKB:P17706}. SUBCELLULAR LOCATION: Isoform 1: Endoplasmic reticulum {ECO:0000250}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250}. Note=Targeted to the endoplasmic reticulum by its C-terminal hydrophobic region. {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 2: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Predominantly localizes to chromatin. Able to shuttle between the nucleus and the cytoplasm and to dephosphorylate plasma membrane receptors. Recruited by activated ITGA1 at the plasma membrane (By similarity). {ECO:0000250}. SUBUNIT: Interacts with RMDN3. Isoform 1 interacts with TMED9. Isoform 1 interacts with STX17; dephosphorylates STX17. Interacts with ITGA1 (via cytoplasmic domain); activates the phosphatase activity towards EGFR. Interacts with TRAF2; probably involved in tumor necrosis factor-mediated signaling. Interacts with MET (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed. The highest expression levels were found in ovary, testis, thymus and kidney. {ECO:0000269|PubMed:20484139, ECO:0000269|PubMed:9271584}. +A2ALK8 PTN3_MOUSE Tyrosine-protein phosphatase non-receptor type 3 (EC 3.1.3.48) 913 103,896 Active site (1); Binding site (2); Chain (1); Domain (3); Modified residue (6); Region (1) FUNCTION: May act at junctions between the membrane and the cytoskeleton. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. +P86547 OSTC2_MOUSE Osteocalcin-2 (Bone Gla protein 2) (BGP2) (Gamma-carboxyglutamic acid-containing protein 2) 95 10,459 Chain (1); Disulfide bond (1); Domain (1); Metal binding (5); Propeptide (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Constitutes 1-2% of the total bone protein. It binds strongly to apatite and calcium. PTM: Gamma-carboxyglutamate residues are formed by vitamin K dependent carboxylation. These residues are essential for the binding of calcium. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Bone. +P29351 PTN6_MOUSE Tyrosine-protein phosphatase non-receptor type 6 (EC 3.1.3.48) (70Z-SHP) (Hematopoietic cell protein-tyrosine phosphatase) (PTPTY-42) (Protein-tyrosine phosphatase 1C) (PTP-1C) (SH-PTP1) (SHP-1) 595 67,559 Active site (1); Alternative sequence (3); Binding site (2); Chain (1); Domain (3); Modified residue (6); Natural variant (2); Region (1); Sequence conflict (3) FUNCTION: Modulates signaling by tyrosine phosphorylated cell surface receptors such as KIT and the EGF receptor/EGFR. The SH2 regions may interact with other cellular components to modulate its own phosphatase activity against interacting substrates. Together with MTUS1, induces UBE2V2 expression upon angiotensin II stimulation. Plays a key role in hematopoiesis. {ECO:0000269|PubMed:9528781}. PTM: Phosphorylated on tyrosine residues. Phosphorylation at Tyr-564 enhances phosphatase activity (By similarity). Binding of KITLG/SCF to KIT increases tyrosine phosphorylation. {ECO:0000250, ECO:0000269|PubMed:1385421, ECO:0000269|PubMed:9528781}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}. Note=In neurons, translocates into the nucleus after treatment with angiotensin II. Shuttles between the cytoplasm and nucleus via its association with PDPK1 (By similarity). {ECO:0000250}. SUBUNIT: Monomer. Interacts with MTUS1 (By similarity). Interacts with MILR1 (tyrosine-phosphorylated) (PubMed:20526344). Interacts with KIT (PubMed:9528781). Interacts with SIRPA/PTPNS1 (PubMed:9712903). Interacts with FCRL2 and FCRL4 (By similarity). Interacts with CD84 (By similarity). Interacts with CD300LF (PubMed:14662855). Interacts with CDK2 (By similarity). Interacts with KIR2DL1; the interaction is enhanced by ARRB2 (By similarity). Interacts (via SH2 1 domain) with ROS1; the interaction is direct and promotes ROS1 dephosphorylation (By similarity). Interacts with EGFR; inhibits EGFR-dependent activation of MAPK/ERK (By similarity). Interacts with LYN (By similarity). Interacts with the tyrosine phosphorylated form of PDPK1 (By similarity). Interacts with CEACAM1 (via cytoplasmic domain); this interaction depends on the monomer/dimer equilibrium and is phosphorylation-dependent (PubMed:19948503, PubMed:9867848). Interacts with MPIG6B (via ITIM motif) (PubMed:23112346). Interacts with KLRI1 and KLRI2 (By similarity). {ECO:0000250|UniProtKB:P29350, ECO:0000250|UniProtKB:P81718, ECO:0000269|PubMed:19948503, ECO:0000269|PubMed:20526344, ECO:0000269|PubMed:23112346, ECO:0000269|PubMed:9528781, ECO:0000269|PubMed:9712903, ECO:0000269|PubMed:9867848}. DOMAIN: The N-terminal SH2 domain functions as an auto-inhibitory domain, blocking the catalytic domain in the ligand-free close conformation. {ECO:0000250}. TISSUE SPECIFICITY: Expressed predominantly in hematopoietic cells. {ECO:0000269|PubMed:1932742}. DISEASE: Note=Defects in Ptpn6 are the cause of the motheaten (me) or viable motheaten (mev) phenotypes. Mice homozygous for the recessive allelic mutations develop severe defects in hematopoiesis. +P86546 OSTCN_MOUSE Osteocalcin (Bone Gla protein) (BGP) (Gamma-carboxyglutamic acid-containing protein) 95 10,549 Chain (1); Disulfide bond (1); Domain (1); Metal binding (5); Modified residue (3); Propeptide (1); Signal peptide (1) FUNCTION: Constitutes 1-2% of the total bone protein. It binds strongly to apatite and calcium. PTM: Gamma-carboxyglutamate residues are formed by vitamin K dependent carboxylation. These residues are essential for the binding of calcium. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Bone. +Q78XF5 OSTC_MOUSE Oligosaccharyltransferase complex subunit OSTC 149 16,815 Chain (1); Erroneous initiation (1); Topological domain (4); Transmembrane (3) TRANSMEM 33 53 Helical. {ECO:0000255}.; TRANSMEM 84 104 Helical. {ECO:0000255}.; TRANSMEM 118 138 Helical. {ECO:0000255}. TOPO_DOM 1 32 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 54 83 Extracellular. {ECO:0000255}.; TOPO_DOM 105 117 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 139 149 Extracellular. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. May be involved in N-glycosylation of APP (amyloid-beta precursor protein). Can modulate gamma-secretase cleavage of APP by enhancing endoprotelysis of PSEN1. {ECO:0000250|UniProtKB:Q9NRP0}. SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9NRP0}. Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Component of the oligosaccharyltransferase (OST) complex. OST exists in two different complex forms which contain common core subunits RPN1, RPN2, OST48, OST4, DAD1 and TMEM258, either STT3A or STT3B as catalytic subunits, and form-specific accessory subunits. STT3A complex assembly occurs through the formation of 3 subcomplexes. Subcomplex 1 contains RPN1 and TMEM258, subcomplex 2 contains the STT3A-specific subunits STT3A, DC2/OSTC, and KCP2 as well as the core subunit OST4, and subcomplex 3 contains RPN2, DAD1, and OST48. The STT3A complex can form stable complexes with the Sec61 complex or with both the Sec61 and TRAP complexes (By similarity). Interacts with PSEN1 and NCSTN; indicative for an association with the gamma-secretase complex (By similarity). {ECO:0000250|UniProtKB:P86218, ECO:0000250|UniProtKB:Q9NRP0}. +Q91VU8 PTOV1_MOUSE Prostate tumor-overexpressed gene 1 protein homolog 416 46,865 Chain (1); Modified residue (1); Region (1) FUNCTION: May activate transcription. Required for nuclear translocation of FLOT1. Promotes cell proliferation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000250}. Note=Translocates from the cytoplasm to the nucleus at the onset of S-phase. Also localizes to lipid rafts. {ECO:0000250}. SUBUNIT: May interact with CREBBP. Interacts with FLOT1 (By similarity). {ECO:0000250}. +P58389 PTPA_MOUSE Serine/threonine-protein phosphatase 2A activator (EC 5.2.1.8) (PP2A, subunit B', PR53 isoform) (Phosphotyrosyl phosphatase activator) (PTPA) (Serine/threonine-protein phosphatase 2A regulatory subunit 4) (Serine/threonine-protein phosphatase 2A regulatory subunit B') 323 36,710 Chain (1); Initiator methionine (1); Modified residue (1); Nucleotide binding (3); Sequence conflict (2) FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for serine/threonine-protein phosphatase 2A (PP2A) modulating its activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a proposed direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2A(i)) in presence of ATP and Mg(2+). Reversibly stimulates the variable phosphotyrosyl phosphatase activity of PP2A core heterodimer PP2A(D) in presence of ATP and Mg(2+) (in vitro). The phosphotyrosyl phosphatase activity is dependent of an ATPase activity of the PP2A(D):PPP2R4 complex. Is involved in apoptosis; the function appears to be independent from PP2A (By similarity). {ECO:0000250, ECO:0000269|PubMed:12952889}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Associates with PP2A heterodimeric core enzyme PP2A(D), composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant regulatory subunit (PR65 or subunit A) (By similarity). Interacts with PPP2CB (PubMed:12952889). {ECO:0000250|UniProtKB:Q15257, ECO:0000269|PubMed:12952889}. +Q6NZK8 PTPC1_MOUSE Protein tyrosine phosphatase domain-containing protein 1 (EC 3.1.3.-) 747 83,934 Active site (1); Alternative sequence (3); Chain (1); Domain (1); Erroneous initiation (2); Modified residue (3); Sequence conflict (1) FUNCTION: May play roles in cilia formation and/or maintenance. {ECO:0000269|PubMed:21289087}. +P18052 PTPRA_MOUSE Receptor-type tyrosine-protein phosphatase alpha (Protein-tyrosine phosphatase alpha) (R-PTP-alpha) (EC 3.1.3.48) (LCA-related phosphatase) (PTPTY-28) 829 93,698 Active site (2); Alternative sequence (2); Beta strand (24); Binding site (2); Chain (1); Domain (2); Glycosylation (8); Helix (15); Modified residue (3); Region (1); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (7) TRANSMEM 143 166 Helical. {ECO:0000255}. TOPO_DOM 20 142 Extracellular. {ECO:0000255}.; TOPO_DOM 167 829 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. TISSUE SPECIFICITY: Widely expressed. Highest expression in brain and kidney. {ECO:0000269|PubMed:1932742, ECO:0000269|PubMed:2162042, ECO:0000269|PubMed:2166945}. +P06800 PTPRC_MOUSE Receptor-type tyrosine-protein phosphatase C (EC 3.1.3.48) (Leukocyte common antigen) (L-CA) (Lymphocyte antigen 5) (Ly-5) (T200) (CD antigen CD45) 1293 144,837 Active site (2); Alternative sequence (2); Binding site (2); Chain (1); Domain (4); Erroneous initiation (4); Frameshift (1); Glycosylation (16); Modified residue (11); Region (1); Sequence caution (1); Sequence conflict (11); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 567 588 Helical. {ECO:0000255}. TOPO_DOM 26 566 Extracellular. {ECO:0000255}.; TOPO_DOM 589 1293 Cytoplasmic. {ECO:0000255}. FUNCTION: Protein tyrosine-protein phosphatase required for T-cell activation through the antigen receptor. Acts as a positive regulator of T-cell coactivation upon binding to DPP4. The first PTPase domain has enzymatic activity, while the second one seems to affect the substrate specificity of the first one. Upon T-cell activation, recruits and dephosphorylates SKAP1 and FYN (By similarity). Dephosphorylates LYN, and thereby modulates LYN activity. {ECO:0000250, ECO:0000269|PubMed:10415030}. PTM: Heavily N- and O-glycosylated. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P08575}; Single-pass type I membrane protein {ECO:0000255}. Membrane raft {ECO:0000250|UniProtKB:P08575}. Note=Colocalized with DPP4 in membrane rafts. {ECO:0000250|UniProtKB:P08575}. SUBUNIT: Interacts with SKAP1. Interacts with DPP4; the interaction is enhanced in a interleukin-12-dependent manner in activated lymphocytes (By similarity). Binds GANAB and PRKCSH. {ECO:0000250, ECO:0000269|PubMed:9148925}. DOMAIN: The first PTPase domain interacts with SKAP1. {ECO:0000250}. +Q64487 PTPRD_MOUSE Receptor-type tyrosine-protein phosphatase delta (Protein-tyrosine phosphatase delta) (R-PTP-delta) (EC 3.1.3.48) 1912 214,410 Active site (2); Alternative sequence (9); Beta strand (41); Binding site (2); Chain (1); Disulfide bond (3); Domain (13); Erroneous initiation (1); Glycosylation (4); Helix (2); Mutagenesis (5); Region (3); Sequence conflict (22); Signal peptide (1); Site (2); Topological domain (2); Transmembrane (1); Turn (2) TRANSMEM 1267 1287 Helical. {ECO:0000255}. TOPO_DOM 21 1266 Extracellular. {ECO:0000255}.; TOPO_DOM 1288 1912 Cytoplasmic. {ECO:0000255}. FUNCTION: Can bidirectionally induce pre- and post-synaptic differentiation of neurons by mediating interaction with IL1RAP and IL1RAPL1 trans-synaptically (PubMed:25908590). Involved in pre-synaptic differentiation through interaction with SLITRK2 (PubMed:25989451). {ECO:0000269|PubMed:25908590, ECO:0000269|PubMed:25989451}. PTM: A cleavage occurs, separating the extracellular domain from the transmembrane segment. This process called 'ectodomain shedding' is thought to be involved in receptor desensitization, signal transduction and/or membrane localization (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Interacts with PPFIA1, PPFIA2 and PPFIA3 (By similarity). Interacts (via extracellular domain) with SLITRK4 (via LRR 1 and 2 repeats) (PubMed:25989451). Interacts with SLITRK2; induces presynaptic differentiation (PubMed:25989451). Interacts (via the second immunoglobilin domain) with IL1RAPL1 (via the first immunoglobilin domain); induces pre- and postsynaptic differentiation of neurons and synapse formation. Isoform G, isoform H, isoform I, isoform J, and isoform K do not interact with IL1RAPL1 (PubMed:25908590, PubMed:21940441). Interacts (via the third immunoglobilin domain) with IL1RAP (via the first immunoglobilin domain); induces pre- and postsynaptic differentiation of neurons (PubMed:25908590). {ECO:0000250|UniProtKB:P23468, ECO:0000269|PubMed:21940441, ECO:0000269|PubMed:25908590, ECO:0000269|PubMed:25989451}. TISSUE SPECIFICITY: Brain, kidney, heart, and some B-cell lines. +E9Q0N2 PTPRH_MOUSE Receptor-type tyrosine-protein phosphatase H (R-PTP-H) (EC 3.1.3.48) (Stomach cancer-associated protein tyrosine phosphatase 1) (SAP-1) 971 106,952 Active site (1); Chain (1); Domain (7); Frameshift (1); Glycosylation (7); Modified residue (2); Mutagenesis (4); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 605 625 Helical. {ECO:0000255}. TOPO_DOM 28 604 Extracellular. {ECO:0000305}.; TOPO_DOM 626 971 Cytoplasmic. {ECO:0000305}. FUNCTION: Protein phosphatase that may contribute to contact inhibition of cell growth and motility by mediating the dephosphorylation of focal adhesion-associated substrates and thus negatively regulating integrin-promoted signaling processes. Induces apoptotic cell death by at least two distinct mechanisms: inhibition of cell survival signaling mediated by PI 3-kinase, Akt, and ILK and activation of a caspase-dependent proapoptotic pathway. Inhibits the basal activity of LCK and its activation in response to TCR stimulation and TCR-induced activation of MAP kinase and surface expression of CD69. Inhibits TCR-induced tyrosine phosphorylation of LAT and ZAP70. Inhibits both basal activity of DOK1 and its CD2-induced tyrosine phosphorylation. Induces dephosphorylation of BCAR1, focal adhesion kinase and SRC. Reduces migratory activity of Jurkat cells (By similarity). Reduces tyrosine phosphorylation of CEACAM20 and thereby contributes to suppress the intestinal immune response (PubMed:26195794). {ECO:0000250|UniProtKB:Q9HD43, ECO:0000269|PubMed:26195794}. SUBCELLULAR LOCATION: Cell projection, microvillus membrane {ECO:0000269|PubMed:19170756, ECO:0000269|PubMed:26195794}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasm {ECO:0000250|UniProtKB:Q9HD43}. Apical cell membrane {ECO:0000269|PubMed:19170756, ECO:0000269|PubMed:26195794}; Single-pass type I membrane protein {ECO:0000305}. Note=Colocalizes with CEACAM20 at the apical brush border of intestinal cells. {ECO:0000269|PubMed:26195794}. SUBUNIT: Homodimer; disulfide-linked (By similarity). Interacts with LCK (By similarity). Interacts (phosphorylated form) with GRB2 (via SH2 domain) (PubMed:20398064). Interacts (phosphorylated form) with FYN (via SH2 domain) (PubMed:20398064). Interacts (via extracellular domain) with CEACAM20 (via extracellular domain); the interaction dephosphorylates CEACAM20 (PubMed:26195794). {ECO:0000250|UniProtKB:Q9HD43, ECO:0000269|PubMed:20398064, ECO:0000269|PubMed:26195794}. TISSUE SPECIFICITY: Expressed strongly in the intestinal tract, with particularly high levels in the duodenum and jejunum (at protein level). Also expressed at low level in the testis (at protein level). Not detected in other tissues tested (at protein level). {ECO:0000269|PubMed:19170756}. +Q64455 PTPRJ_MOUSE Receptor-type tyrosine-protein phosphatase eta (Protein-tyrosine phosphatase eta) (R-PTP-eta) (EC 3.1.3.48) (HPTP beta-like tyrosine phosphatase) (Protein-tyrosine phosphatase receptor type J) (R-PTP-J) (Susceptibility to colon cancer 1) (CD antigen CD148) 1238 136,769 Active site (1); Binding site (2); Chain (1); Domain (9); Glycosylation (37); Modified residue (1); Mutagenesis (2); Region (1); Sequence conflict (11); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 877 897 Helical. {ECO:0000255}. TOPO_DOM 29 876 Extracellular. {ECO:0000255}.; TOPO_DOM 898 1238 Cytoplasmic. {ECO:0000255}. FUNCTION: Tyrosine phosphatase which dephosphorylates or contributes to the dephosphorylation of CTNND1, FLT3, PDGFRB, MET, RET, KDR, LYN, SRC, MAPK1, MAPK3, EGFR, TJP1, OCLN, PIK3R1 and PIK3R2. Plays a role in cell adhesion, migration, proliferation and differentiation. Involved in vascular development. May be involved in the mechanism of contact inhibition of cell growth. Regulator of macrophage adhesion and spreading. Positively affects cell-matrix adhesion. Positive regulator of platelet activation and thrombosis. Negative regulator of cell proliferation. Negative regulator of PDGF-stimulated cell migration; through dephosphorylation of PDGFR. Positive regulator of endothelial cell survival, as well as of VEGF-induced SRC and AKT activation; through KDR dephosphorylation. Negative regulator of EGFR signaling pathway; through EGFR dephosphorylation. Enhances the barrier function of epithelial junctions during reassembly. Negatively regulates T-cell receptor (TCR) signaling. Upon T-cell TCR activation, it is up-regulated and excluded from the immunological synapses, while upon T-cell-antigen presenting cells (APC) disengagement, it is no longer excluded and can dephosphorylate PLCG1 and LAT to down-regulate prolongation of signaling. {ECO:0000269|PubMed:12588999, ECO:0000269|PubMed:12771128, ECO:0000269|PubMed:12833140, ECO:0000269|PubMed:12913111, ECO:0000269|PubMed:18249142, ECO:0000269|PubMed:19246339, ECO:0000269|PubMed:19268662}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Cell projection, ruffle membrane. Cell junction. Note=After T-cell stimulation, it is temporarily excluded from immunological synapses. Found at cell borders. SUBUNIT: Monomer. Interacts with CTNNB1 (phosphorylated) and JUP (phosphorylated). Interacts with FLT3 (phosphorylated). Interacts with GAB1 and GRB2 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed at high levels in brain, kidney, spleen and intestine, and at lower levels in liver, lung, thymus and heart. Expressed at a high level in the myeloid cell line FDC-P2, and at a lower level in the pre-B lymphoid cell line WEHI-231 and the T hybridoma cell line HB21.7.31. Not expressed in the fibroblast cell line NIH3T3 or the erythroid cell line F5-5. Expressed in macrophages. {ECO:0000269|PubMed:8483328, ECO:0000269|PubMed:8549806, ECO:0000269|PubMed:9823776}. +E9Q612 PTPRO_MOUSE Receptor-type tyrosine-protein phosphatase O (R-PTP-O) (EC 3.1.3.48) (Glomerular epithelial protein 1) (Protein tyrosine phosphatase U2) (PTP-U2) (PTPase U2) 1226 138,589 Active site (1); Binding site (2); Chain (1); Domain (7); Glycosylation (9); Modified residue (2); Mutagenesis (1); Region (1); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 833 853 Helical. {ECO:0000255}. TOPO_DOM 30 832 Extracellular. {ECO:0000255}.; TOPO_DOM 854 1226 Cytoplasmic. {ECO:0000255}. FUNCTION: Possesses tyrosine phosphatase activity. Plays a role in regulating the glomerular pressure/filtration rate relationship through an effect on podocyte structure and function. {ECO:0000269|PubMed:11086029}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Interacts (phosphorylated form) with FYN and GRB2. {ECO:0000269|PubMed:20398064}. +Q4ZJM7 OTOL1_MOUSE Otolin-1 482 49,601 Chain (1); Domain (4); Glycosylation (2); Modified residue (11); Sequence conflict (3); Signal peptide (1) FUNCTION: Collagen-like protein specifically expressed in the inner ear, which provides an organic scaffold for otoconia, a calcium carbonate structure in the saccule and utricle of the ear (PubMed:21655225, PubMed:24748133, PubMed:29076638). Acts as a scaffold for biomineralization: sequesters calcium and forms interconnecting fibrils between otoconia that are incorporated into the calcium crystal structure (PubMed:21655225, PubMed:24748133, PubMed:29076638). Together with OC90, modulates calcite crystal morphology and growth kinetics (PubMed:24748133). {ECO:0000269|PubMed:21655225, ECO:0000269|PubMed:24748133, ECO:0000269|PubMed:29076638}. PTM: Not N-glycosylated. {ECO:0000269|PubMed:20856818}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:20856818}. Note=Localized in both the surrounding otoconial matrix and otoconia. {ECO:0000269|PubMed:20856818}. SUBUNIT: Homooligomer; disulfide-linked; probably forms homotrimers (PubMed:20856818, PubMed:24748133, PubMed:29076638). Interacts with OC90 (PubMed:17300776, PubMed:20856818, PubMed:21655225). Interacts with CBLN1 (PubMed:20856818). {ECO:0000269|PubMed:17300776, ECO:0000269|PubMed:20856818, ECO:0000269|PubMed:21655225, ECO:0000269|PubMed:24748133, ECO:0000269|PubMed:29076638}. DOMAIN: The C1q domain mediates calcium-binding. {ECO:0000269|PubMed:29076638}. TISSUE SPECIFICITY: Expressed in the organic matrix of otoconia (at protein level) (PubMed:17300776, PubMed:22841569). Expressed in neonatal sensory epithelium of vestibular utricle and saccule and also in otoconia (PubMed:21655225). {ECO:0000269|PubMed:17300776, ECO:0000269|PubMed:21655225, ECO:0000269|PubMed:22841569}. +Q62132 PTPRR_MOUSE Receptor-type tyrosine-protein phosphatase R (R-PTP-R) (EC 3.1.3.48) (Phosphotyrosine phosphatase 13) (Protein-tyrosine-phosphatase SL) 656 74,036 Active site (1); Alternative sequence (3); Beta strand (10); Binding site (2); Chain (1); Domain (1); Erroneous initiation (1); Glycosylation (1); Helix (13); Modified residue (2); Mutagenesis (4); Region (1); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (2) TRANSMEM 227 247 Helical. {ECO:0000255}. TOPO_DOM 24 226 Extracellular. {ECO:0000255}.; TOPO_DOM 248 656 Cytoplasmic. {ECO:0000255}. FUNCTION: Sequesters mitogen-activated protein kinases (MAPKs) such as MAPK1, MAPK3 and MAPK14 in the cytoplasm in an inactive form. The MAPKs bind to a dephosphorylated kinase interacting motif, phosphorylation of which by the protein kinase A complex releases the MAPKs for activation and translocation into the nucleus. Isoform gamma may have a role in patterning and cellular proliferation of skeletal elements in the precartilaginous/cartilaginous skeleton. {ECO:0000269|PubMed:10601328, ECO:0000269|PubMed:10949045}. SUBCELLULAR LOCATION: Isoform Alpha: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Isoform Beta: Cytoplasm. Note=Locates to the areas within the cytoplasm.; SUBCELLULAR LOCATION: Isoform Gamma: Cytoplasm. Note=Locates to the areas within the cytoplasm. SUBUNIT: Interacts with MAPKs. {ECO:0000269|PubMed:10601328}. TISSUE SPECIFICITY: Expressed in the heart, brain, spleen, lung, liver, skeletal muscle, kidney and testis. Isoform alpha is expressed throughout the granular layer of the cerebellar but not within the Purkinje cells, also in the villi of the ileum and jejunum and both the villi and crypts of the duodenum. Isoform beta is expressed only in the Purkinje cells. Isoform gamma is expressed throughout the brain, the villi and crypts of the duodenum, jejunum and ileum and expressed at low levels in the proximal colon. {ECO:0000269|PubMed:10705342, ECO:0000269|PubMed:10949045, ECO:0000269|PubMed:7832766, ECO:0000269|PubMed:7836467}. +Q99M80 PTPRT_MOUSE Receptor-type tyrosine-protein phosphatase T (R-PTP-T) (EC 3.1.3.48) (RPTPmam4) (Receptor-type tyrosine-protein phosphatase rho) (RPTP-rho) (mRPTPrho) 1454 163,012 Active site (2); Alternative sequence (4); Binding site (2); Chain (1); Disulfide bond (1); Domain (8); Glycosylation (10); Modified residue (1); Region (1); Sequence conflict (18); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 771 791 Helical. {ECO:0000255}. TOPO_DOM 30 770 Extracellular. {ECO:0000255}.; TOPO_DOM 792 1454 Cytoplasmic. {ECO:0000255}. FUNCTION: May be involved in both signal transduction and cellular adhesion in the CNS. May have specific signaling roles in the tyrosine phosphorylation/dephosphorylation pathway in the anterior compartment of the adult cerebellar cortex. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. TISSUE SPECIFICITY: Expression is restricted to the CNS. Distributed throughout the brain and spinal cord. {ECO:0000269|PubMed:9486824}. +B1AUH1 PTPRU_MOUSE Receptor-type tyrosine-protein phosphatase U (R-PTP-U) (EC 3.1.3.48) (Ftp-1) (Pancreatic carcinoma phosphatase 2) (PCP-2) (Protein-tyrosine phosphatase-lamda) (PTP-lambda) (PTPlambda) (Receptor-type protein-tyrosine phosphatase psi) (R-PTP-psi) 1446 162,494 Active site (2); Alternative sequence (1); Binding site (2); Chain (1); Disulfide bond (1); Domain (8); Erroneous termination (1); Glycosylation (3); Modified residue (4); Region (2); Sequence caution (2); Sequence conflict (6); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 750 770 Helical. {ECO:0000255}. TOPO_DOM 19 749 Extracellular. {ECO:0000255}.; TOPO_DOM 771 1446 Cytoplasmic. {ECO:0000255}. FUNCTION: Tyrosine-protein phosphatase which dephosphorylates CTNNB1. Regulates CTNNB1 function both in cell adhesion and signaling. May function in cell proliferation and migration and play a role in the maintenance of epithelial integrity. May play a role in megakaryocytopoiesis (By similarity). {ECO:0000250}. PTM: The extracellular domain is proteolytically processed through cleavage within the fibronectin type-III 4 domain. In addition to the 190 kDa full-length protein, proteolytic products of 100 kDa, 80 kDa and 73 kDa are observed (By similarity). {ECO:0000250}.; PTM: N-glycosylated. {ECO:0000250}.; PTM: Phosphorylated on tyrosine residues upon activation of KIT with stem cell factor (SCF). The 73 kDa proteolytic product is not phosphorylated (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction {ECO:0000250}. Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Forms homooligomeric complexes which mediate cell homotypic adhesion (Probable). Interacts (via the cytoplasmic juxtamembrane domain) with CTNNB1; may mediate interaction with the cadherin/catenin adhesion complex. Interacts with KIT (By similarity). May interact with AP3B1 (By similarity). {ECO:0000250, ECO:0000305}. TISSUE SPECIFICITY: Transcripts of different sizes are differentially expressed in a subset of tissues. Detected in brain, lung, skeletal muscle, heart, kidney and placenta. In brain; expressed in olfactory bulb, cerebral cortex, hippocampus and cerebellum. {ECO:0000269|PubMed:15040814, ECO:0000269|PubMed:9054423, ECO:0000269|PubMed:9272866}. +Q7TQI3 OTUB1_MOUSE Ubiquitin thioesterase OTUB1 (EC 3.4.19.12) (Deubiquitinating enzyme OTUB1) (OTU domain-containing ubiquitin aldehyde-binding protein 1) (Otubain-1) (Ubiquitin-specific-processing protease OTUB1) 271 31,270 Active site (3); Binding site (5); Chain (1); Domain (1); Initiator methionine (1); Modified residue (2); Region (6); Sequence conflict (1) FUNCTION: Hydrolase that can specifically remove compared to 'Lys-48'-linked conjugated ubiquitin from proteins and plays an important regulatory role at the level of protein turnover by preventing degradation. Regulator of T-cell anergy, a phenomenon that occurs when T-cells are rendered unresponsive to antigen rechallenge and no longer respond to their cognate antigen. Acts via its interaction with RNF128/GRAIL. Surprisingly, it regulates RNF128-mediated ubiquitination, but does not deubiquitinate polyubiquitinated RNF128. Deubiquitinates estrogen receptor alpha (ESR1). Mediates deubiquitination of 'Lys-48'-linked polyubiquitin chains, but not 'Lys-63'-linked polyubiquitin chains. Not able to cleave di-ubiquitin. Also capable of removing NEDD8 from NEDD8 conjugates, but with a much lower preference compared to 'Lys-48'-linked ubiquitin. {ECO:0000269|PubMed:14661020}.; FUNCTION: Plays a key non-catalytic role in DNA repair regulation by inhibiting activity of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of 'Lys-63'-linked histone H2A and H2AX at DNA damage sites. Inhibits RNF168 independently of ubiquitin thioesterase activity by binding and inhibiting UBE2N/UBC13, the E2 partner of RNF168, thereby limiting spreading of 'Lys-63'-linked histone H2A and H2AX marks. Inhibition occurs by binding to free ubiquitin: free ubiquitin acts as an allosteric regulator that increases affinity for UBE2N/UBC13 and disrupts interaction with UBE2V1. The OTUB1-UBE2N/UBC13-free ubiquitin complex adopts a configuration that mimics a cleaved 'Lys48'-linked di-ubiquitin chain (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with RNF128. Forms a ternary complex with RNF128 and USP8. Interacts with FUS, ESR1 and RACK1. Interacts with UBE2N/UBC13 (By similarity). {ECO:0000250}. +Q9CQX0 OTUB2_MOUSE Ubiquitin thioesterase OTUB2 (EC 3.4.19.12) (Deubiquitinating enzyme OTUB2) (OTU domain-containing ubiquitin aldehyde-binding protein 2) (Otubain-2) (Ubiquitin-specific-processing protease OTUB2) 234 27,300 Active site (4); Chain (1); Domain (1); Site (1) FUNCTION: Hydrolase that can remove conjugated ubiquitin from proteins in vitro and may therefore play an important regulatory role at the level of protein turnover by preventing degradation. Mediates deubiquitination of 'Lys-11'-,'Lys-48'- and 'Lys-63'-linked polyubiquitin chains, with a preference for 'Lys-63'-linked polyubiquitin chains (By similarity). {ECO:0000250}. +Q8CIV7 OVOL2_MOUSE Transcription factor Ovo-like 2 (mOvo2) (Zinc finger OVO2) (Zinc finger protein 339) (Zinc finger protein mOVO) 274 30,685 Alternative sequence (3); Chain (1); Modified residue (1); Sequence conflict (2); Zinc finger (4) FUNCTION: Zinc-finger transcription repressor factor (PubMed:15225875, PubMed:23319585). Plays a critical role in maintaining the identity of epithelial lineages by suppressing epithelial-to mesenchymal transition (EMT) mainly through the repression of ZEB1, an EMT inducer (PubMed:24735878, PubMed:24735879). Positively regulates neuronal differentiation (PubMed:16423343, PubMed:23319585). Suppresses cell cycling and terminal differentiation of keratinocytes by directly repressing MYC and NOTCH1 (By similarity). Important for the correct development of primordial germ cells in embryos (PubMed:28059165). {ECO:0000250|UniProtKB:Q9BRP0, ECO:0000269|PubMed:15225875, ECO:0000269|PubMed:16423343, ECO:0000269|PubMed:23319585, ECO:0000269|PubMed:24735878, ECO:0000269|PubMed:24735879, ECO:0000269|PubMed:28059165}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9468311}. TISSUE SPECIFICITY: Expressed highly in testis, specifically in spermatocytes. Expressed also in skin and at lower levels in the ovary. {ECO:0000269|PubMed:12213202, ECO:0000269|PubMed:15225875, ECO:0000269|PubMed:9468311}. +P58308 OX2R_MOUSE Orexin receptor type 2 (Ox-2-R) (Ox2-R) (Ox2R) (Hypocretin receptor type 2) 460 52,461 Alternative sequence (1); Binding site (1); Chain (1); Disulfide bond (1); Glycosylation (3); Region (1); Sequence conflict (2); Site (1); Topological domain (8); Transmembrane (7) TRANSMEM 55 75 Helical; Name=1. {ECO:0000250|UniProtKB:O43614}.; TRANSMEM 89 110 Helical; Name=2. {ECO:0000250|UniProtKB:O43614}.; TRANSMEM 128 150 Helical; Name=3. {ECO:0000250|UniProtKB:O43614}.; TRANSMEM 171 191 Helical; Name=4. {ECO:0000250|UniProtKB:O43614}.; TRANSMEM 223 243 Helical; Name=5. {ECO:0000250|UniProtKB:O43614}.; TRANSMEM 305 326 Helical; Name=6. {ECO:0000250|UniProtKB:O43614}.; TRANSMEM 343 366 Helical; Name=7. {ECO:0000250|UniProtKB:O43614}. TOPO_DOM 1 54 Extracellular. {ECO:0000250|UniProtKB:O43614}.; TOPO_DOM 76 88 Cytoplasmic. {ECO:0000250|UniProtKB:O43614}.; TOPO_DOM 111 127 Extracellular. {ECO:0000250|UniProtKB:O43614}.; TOPO_DOM 151 170 Cytoplasmic. {ECO:0000250|UniProtKB:O43614}.; TOPO_DOM 192 222 Extracellular. {ECO:0000250|UniProtKB:O43614}.; TOPO_DOM 244 304 Cytoplasmic. {ECO:0000250|UniProtKB:O43614}.; TOPO_DOM 327 342 Extracellular. {ECO:0000250|UniProtKB:O43614}.; TOPO_DOM 367 460 Cytoplasmic. {ECO:0000250|UniProtKB:O43614}. FUNCTION: Nonselective, high-affinity receptor for both orexin-A and orexin-B neuropeptides. Triggers an increase in cytoplasmic Ca(2+) levels in response to orexin-A binding. {ECO:0000250|UniProtKB:O43614}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O43614}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O43614}. DOMAIN: The N-terminal region is required for orexin signaling. {ECO:0000250|UniProtKB:O43614}. TISSUE SPECIFICITY: Widely expressed. Isoform 2 not detected in skeletal muscle and kidney. {ECO:0000269|PubMed:15256537}. +Q922Z0 OXDD_MOUSE D-aspartate oxidase (DASOX) (DDO) (EC 1.4.3.1) 341 37,546 Binding site (5); Chain (1); Motif (1); Nucleotide binding (5); Sequence conflict (2) FUNCTION: Selectively catalyzes the oxidative deamination of D-aspartate and its N-methylated derivative, N-methyl D-aspartate. {ECO:0000250}. SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}. +Q8VE38 OXND1_MOUSE Oxidoreductase NAD-binding domain-containing protein 1 (EC 1.-.-.-) 311 34,727 Alternative sequence (1); Chain (1); Domain (1); Nucleotide binding (1); Sequence conflict (2); Signal peptide (1) +Q9D404 OXSM_MOUSE 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial (EC 2.3.1.41) (Beta-ketoacyl-ACP synthase) 459 48,628 Chain (1); Modified residue (5); Transit peptide (1) Lipid metabolism; fatty acid biosynthesis. FUNCTION: May play a role in the biosynthesis of lipoic acid as well as longer chain fatty acids required for optimal mitochondrial function. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. +Q4KMM3 OXR1_MOUSE Oxidation resistance protein 1 (Protein C7) 866 95,912 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (3); Erroneous initiation (3); Modified residue (11); Region (1); Sequence conflict (9) FUNCTION: May be involved in protection from oxidative damage. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Nucleus, nucleolus {ECO:0000269|PubMed:11237729}. Note=According to PubMed:11237729 it is nucleolar. TISSUE SPECIFICITY: Highly expressed in brain and testis. {ECO:0000269|PubMed:11237729}. +Q8BQN6 OZF_MOUSE Zinc finger protein OZF (Only zinc finger protein) (Zinc finger protein 146) 292 33,093 Chain (1); Cross-link (6); Erroneous initiation (1); Region (1); Zinc finger (10) SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Binds DNA. Interacts with SUMO conjugating enzyme UBC9/UBE2I. Interacts with the telomeric protein TERF2IP (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in heart, brain, liver, lung, skeletal muscle and kidney, and at much lower level in spleen and testicle. Expressed in lactating mammary gland. {ECO:0000269|PubMed:10449921, ECO:0000269|PubMed:12437081}. +P48759 PTX3_MOUSE Pentraxin-related protein PTX3 (Pentaxin-related protein PTX3) (Tumor necrosis factor-inducible gene 14 protein) (TSG-14) 381 41,812 Chain (1); Disulfide bond (7); Domain (1); Glycosylation (1); Sequence conflict (8); Signal peptide (1) FUNCTION: Plays a role in the regulation of innate resistance to pathogens, inflammatory reactions, possibly clearance of self-components and female fertility. {ECO:0000269|PubMed:9407058}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Homooctamer; disulfide-linked (By similarity). Binds to C1q. {ECO:0000250, ECO:0000269|PubMed:9407058}. +Q3UR32 P2RX3_MOUSE P2X purinoceptor 3 (P2X3) (ATP receptor) (Purinergic receptor) 397 44,437 Binding site (3); Chain (1); Disulfide bond (5); Glycosylation (4); Nucleotide binding (2); Sequence conflict (1); Topological domain (3); Transmembrane (2) TRANSMEM 21 43 Helical; Name=1. {ECO:0000250|UniProtKB:P56373}.; TRANSMEM 323 341 Helical; Name=2. {ECO:0000250|UniProtKB:P56373}. TOPO_DOM 1 20 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 44 322 Extracellular. {ECO:0000305}.; TOPO_DOM 342 397 Cytoplasmic. {ECO:0000305}. FUNCTION: Receptor for ATP that acts as a ligand-gated cation channel (By similarity). Plays a role in sensory perception (PubMed:15961431, PubMed:16322458). Required for normal perception of pain (PubMed:15961431). Required for normal taste perception (PubMed:16322458). {ECO:0000250|UniProtKB:P56373, ECO:0000269|PubMed:15961431, ECO:0000269|PubMed:16322458}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P56373}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P56373}. SUBUNIT: Homotrimer (By similarity). Functional P2XRs are organized as homomeric and heteromeric trimers (By similarity). {ECO:0000250|UniProtKB:P49654, ECO:0000250|UniProtKB:P56373}. +Q8BFU7 P2Y10_MOUSE Putative P2Y purinoceptor 10 (P2Y10) 328 37,244 Chain (1); Disulfide bond (1); Erroneous gene model prediction (1); Glycosylation (2); Sequence conflict (2); Topological domain (8); Transmembrane (7) TRANSMEM 28 48 Helical; Name=1. {ECO:0000255}.; TRANSMEM 57 77 Helical; Name=2. {ECO:0000255}.; TRANSMEM 92 112 Helical; Name=3. {ECO:0000255}.; TRANSMEM 138 158 Helical; Name=4. {ECO:0000255}.; TRANSMEM 183 203 Helical; Name=5. {ECO:0000255}.; TRANSMEM 234 254 Helical; Name=6. {ECO:0000255}.; TRANSMEM 278 298 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 27 Extracellular. {ECO:0000255}.; TOPO_DOM 49 56 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 78 91 Extracellular. {ECO:0000255}.; TOPO_DOM 113 137 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 159 182 Extracellular. {ECO:0000255}.; TOPO_DOM 204 233 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 255 277 Extracellular. {ECO:0000255}.; TOPO_DOM 299 328 Cytoplasmic. {ECO:0000255}. FUNCTION: Putative receptor for purines coupled to G-proteins. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q9D8I2 P2Y13_MOUSE P2Y purinoceptor 13 (P2Y13) (G-protein coupled receptor 86) 337 38,727 Chain (1); Disulfide bond (1); Glycosylation (3); Sequence conflict (2); Topological domain (8); Transmembrane (7) TRANSMEM 32 52 Helical; Name=1. {ECO:0000255}.; TRANSMEM 61 81 Helical; Name=2. {ECO:0000255}.; TRANSMEM 102 122 Helical; Name=3. {ECO:0000255}.; TRANSMEM 145 165 Helical; Name=4. {ECO:0000255}.; TRANSMEM 194 214 Helical; Name=5. {ECO:0000255}.; TRANSMEM 238 258 Helical; Name=6. {ECO:0000255}.; TRANSMEM 282 302 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 31 Extracellular. {ECO:0000255}.; TOPO_DOM 53 60 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 82 101 Extracellular. {ECO:0000255}.; TOPO_DOM 123 144 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 166 193 Extracellular. {ECO:0000255}.; TOPO_DOM 215 237 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 259 281 Extracellular. {ECO:0000255}.; TOPO_DOM 303 337 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for ADP. Coupled to G(i)-proteins. May play a role in hematopoiesis and the immune system (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q9ESG6 P2Y14_MOUSE P2Y purinoceptor 14 (P2Y14) (G-protein coupled receptor 105) (UDP-glucose receptor) 338 38,861 Chain (1); Disulfide bond (1); Glycosylation (2); Topological domain (8); Transmembrane (7) TRANSMEM 30 50 Helical; Name=1. {ECO:0000255}.; TRANSMEM 56 76 Helical; Name=2. {ECO:0000255}.; TRANSMEM 97 117 Helical; Name=3. {ECO:0000255}.; TRANSMEM 140 160 Helical; Name=4. {ECO:0000255}.; TRANSMEM 189 209 Helical; Name=5. {ECO:0000255}.; TRANSMEM 235 255 Helical; Name=6. {ECO:0000255}.; TRANSMEM 279 299 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 29 Extracellular. {ECO:0000255}.; TOPO_DOM 51 55 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 77 96 Extracellular. {ECO:0000255}.; TOPO_DOM 118 139 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 161 188 Extracellular. {ECO:0000255}.; TOPO_DOM 210 234 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 256 278 Extracellular. {ECO:0000255}.; TOPO_DOM 300 338 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for UDP-glucose coupled to G-proteins. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +P35383 P2RY2_MOUSE P2Y purinoceptor 2 (P2Y2) (ATP receptor) (P2U purinoceptor 1) (P2U1) (Purinergic receptor) 373 42,175 Chain (1); Disulfide bond (1); Glycosylation (2); Mutagenesis (6); Sequence conflict (8); Topological domain (8); Transmembrane (7) TRANSMEM 33 59 Helical; Name=1. {ECO:0000255}.; TRANSMEM 71 93 Helical; Name=2. {ECO:0000255}.; TRANSMEM 111 129 Helical; Name=3. {ECO:0000255}.; TRANSMEM 153 172 Helical; Name=4. {ECO:0000255}.; TRANSMEM 195 220 Helical; Name=5. {ECO:0000255}.; TRANSMEM 247 269 Helical; Name=6. {ECO:0000255}.; TRANSMEM 288 309 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 32 Extracellular. {ECO:0000255}.; TOPO_DOM 60 70 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 94 110 Extracellular. {ECO:0000255}.; TOPO_DOM 130 152 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 173 194 Extracellular. {ECO:0000255}.; TOPO_DOM 221 246 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 270 287 Extracellular. {ECO:0000255}.; TOPO_DOM 310 373 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for ATP and UTP coupled to G-proteins that activate a phosphatidylinositol-calcium second messenger system. The affinity range is UTP = ATP > ATP-gamma-S >> 2-methylthio-ATP = ADP. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Spleen, testis, kidney, liver, lung, heart and brain. +Q9ERK9 P2RY6_MOUSE P2Y purinoceptor 6 (P2Y6) 328 36,721 Chain (1); Disulfide bond (1); Glycosylation (2); Topological domain (8); Transmembrane (7) TRANSMEM 28 48 Helical; Name=1. {ECO:0000255}.; TRANSMEM 63 83 Helical; Name=2. {ECO:0000255}.; TRANSMEM 102 122 Helical; Name=3. {ECO:0000255}.; TRANSMEM 145 165 Helical; Name=4. {ECO:0000255}.; TRANSMEM 195 215 Helical; Name=5. {ECO:0000255}.; TRANSMEM 237 257 Helical; Name=6. {ECO:0000255}.; TRANSMEM 281 303 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 27 Extracellular. {ECO:0000255}.; TOPO_DOM 49 62 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 84 101 Extracellular. {ECO:0000255}.; TOPO_DOM 123 144 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 166 194 Extracellular. {ECO:0000255}.; TOPO_DOM 216 236 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 258 280 Extracellular. {ECO:0000255}.; TOPO_DOM 304 328 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for extracellular UTP > ADP = 2-methylthio-ATP > ADP-beta-S > ATP = ATP-gamma-S. The activity of this receptor is mediated by G proteins which activate a phosphatidylinositol-calcium second messenger system. Functionally coupled to phospholipase C (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q6P2K6 P4R3A_MOUSE Serine/threonine-protein phosphatase 4 regulatory subunit 3A (SMEK homolog 1) 820 93,842 Alternative sequence (1); Chain (1); Domain (1); Erroneous initiation (1); Modified residue (10) FUNCTION: Regulatory subunit of serine/threonine-protein phosphatase 4. May regulate the activity of PPP4C at centrosomal microtubule organizing centers. The PPP4C-PPP4R2-PPP4R3A PP4 complex specifically dephosphorylates H2AFX phosphorylated on 'Ser-140' (gamma-H2AFX) generated during DNA replication and required for DNA DSB repair (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Nucleus {ECO:0000250}. Note=In interphase localized in the cytoplasm and in the nucleus (with higher levels). During metaphase located in pericentriolar regions (By similarity). {ECO:0000250}. SUBUNIT: Serine/threonine-protein phosphatase 4 (PP4) occurs in different assemblies of the catalytic and one or more regulatory subunits. Component of the PP4 complex PPP4C-PPP4R2-PPP4R3A. Interacts with PPP4C; the interaction requires PPP4R2 (By similarity). {ECO:0000250}. +Q3V0Y1 P4R3C_MOUSE Protein PPP4R3C (SMEK homolog 3) 813 95,416 Chain (1); Sequence conflict (1) +Q4QQM4 P5I11_MOUSE Tumor protein p53-inducible protein 11 (Transformation related protein 53 inducible protein 11) (p53-induced gene 11 protein) 189 20,911 Chain (1); Compositional bias (1); Frameshift (1); Modified residue (1); Topological domain (5); Transmembrane (4) TRANSMEM 64 84 Helical. {ECO:0000255}.; TRANSMEM 109 129 Helical. {ECO:0000255}.; TRANSMEM 131 151 Helical. {ECO:0000255}.; TRANSMEM 156 176 Helical. {ECO:0000255}. TOPO_DOM 1 63 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 85 108 Extracellular. {ECO:0000255}.; TOPO_DOM 130 130 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 152 155 Extracellular. {ECO:0000255}.; TOPO_DOM 177 189 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q80U58 PUM2_MOUSE Pumilio homolog 2 1066 114,314 Alternative sequence (3); Chain (1); Compositional bias (3); Domain (1); Erroneous initiation (1); Helix (33); Modified residue (14); Region (9); Repeat (8); Sequence conflict (7); Turn (4) FUNCTION: Sequence-specific RNA-binding protein that acts as a post-transcriptional repressor by binding the 3'-UTR of mRNA targets. Binds to an RNA consensus sequence, the Pumilio Response Element (PRE), 5'-UGUANAUA-3', that is related to the Nanos Response Element (NRE). Mediates post-transcriptional repression of transcripts via different mechanisms: acts via direct recruitment of the CCR4-POP2-NOT deadenylase leading to translational inhibition and mRNA degradation. Also mediates deadenylation-independent repression by promoting accessibility of miRNAs. Acts as a post-transcriptional repressor of E2F3 mRNAs by binding to its 3'-UTR and facilitating miRNA regulation. Plays a role in cytoplasmic sensing of viral infection. Represses a program of genes necessary to maintain genomic stability such as key mitotic, DNA repair and DNA replication factors. Its ability to repress those target mRNAs is regulated by the lncRNA NORAD (non-coding RNA activated by DNA damage) which, due to its high abundance and multitude of PUMILIO binding sites, is able to sequester a significant fraction of PUM1 and PUM2 in the cytoplasm. May regulate DCUN1D3 mRNA levels. May support proliferation and self-renewal of stem cells. Binds specifically to miRNA MIR199A precursor, with PUM1, regulates miRNA MIR199A expression at a postranscriptional level (By similarity). {ECO:0000250|UniProtKB:Q8TB72}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:19861488}. Cytoplasmic granule {ECO:0000269|PubMed:19861488}. Cytoplasm, perinuclear region {ECO:0000250}. Note=The cytoplasmic granules are stress granules which are a dense aggregation in the cytosol composed of proteins and RNAs that appear when the cell is under stress. Colocalizes with NANOS1 and SNAPIN in the perinuclear region of germ cells (By similarity). Colocalizes with NANOS3 in the stress granules (PubMed:19861488). {ECO:0000250|UniProtKB:Q8TB72, ECO:0000269|PubMed:19861488}. SUBUNIT: Homodimer; homodimerizes in vitro. Interacts with DAZ, DAZL and NANOS1 via its pumilio repeats. Interacts with NANOS3 (By similarity). Interacts with SNAPIN. Recruits the CCR4-POP2-NOT deadenylase leading to translational inhibition and mRNA degradation. Interacts with DDX20. In case of viral infection, interacts with DHX58 (By similarity). {ECO:0000250|UniProtKB:Q8TB72}. DOMAIN: The pumilio repeats mediate the association with RNA by packing together to form a right-handed superhelix that approximates a half donut. RNA-binding occurs on the concave side of the surface (PubMed:19540345). PUM2 is composed of 8 pumilio repeats of 36 residues; each repeat binds a single nucleotide in its RNA target. Residues at positions 12 and 16 of the pumilio repeat bind each RNA base via hydrogen bonding or van der Waals contacts with the Watson-Crick edge, while the amino acid at position 13 makes a stacking interaction. The recognition of RNA by pumilio repeats is base specific: cysteine and glutamine at position 12 and 16, respectively, bind adenine; asparagine and glutamine bind uracil; and serine and glutamate bind guanine (By similarity). {ECO:0000250|UniProtKB:Q14671, ECO:0000269|PubMed:19540345}. TISSUE SPECIFICITY: Widely expressed. Expressed in embryonic stem cells, heart, kidney, lung, skin, intestine, spleen and thymus. Expressed at intermediate level in brain and liver. Weakly or not expressed in muscles and stomach. Expressed at various stages of myeloid and lymphoid cell development. In the testis expressed in the spermatogoni, spermatocytes, spermatids and Sertoli cells. {ECO:0000269|PubMed:11780640, ECO:0000269|PubMed:12667987, ECO:0000269|PubMed:18089289}. +P47713 PA24A_MOUSE Cytosolic phospholipase A2 (cPLA2) (Phospholipase A2 group IVA) [Includes: Phospholipase A2 (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase); Lysophospholipase (EC 3.1.1.5)] 748 85,222 Active site (2); Chain (1); Cross-link (2); Domain (2); Metal binding (9); Modified residue (9); Region (1) FUNCTION: Selectively hydrolyzes arachidonyl phospholipids in the sn-2 position releasing arachidonic acid. Together with its lysophospholipid activity, it is implicated in the initiation of the inflammatory response. PTM: Activated by phosphorylation at both Ser-505 and Ser-726. {ECO:0000269|PubMed:10978317}. SUBCELLULAR LOCATION: Cytoplasm. Cytoplasmic vesicle. Note=Translocates to membrane vesicles in a calcium-dependent fashion. DOMAIN: The N-terminal C2 domain associates with lipid membranes upon calcium binding. It modulates enzyme activity by presenting the active site to its substrate in response to elevations of cytosolic Ca(2+) (By similarity). {ECO:0000250}. +P0C871 PA24B_MOUSE Cytosolic phospholipase A2 beta (cPLA2-beta) (EC 3.1.1.4) (Phospholipase A2 group IVB) 782 88,448 Active site (2); Chain (1); Domain (2); Erroneous gene model prediction (1); Sequence conflict (4) FUNCTION: Calcium-dependent phospholipase A2 that selectively hydrolyzes glycerophospholipids in the sn-2 position with a preference for arachidonoyl phospholipids. Has a much weaker activity than PLA2G4A (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Translocates to membrane vesicles in a calcium-dependent fashion. {ECO:0000250}. DOMAIN: The N-terminal C2 domain associates with lipid membranes upon calcium binding. It modulates enzyme activity by presenting the active site to its substrate in response to elevations of cytosolic Ca(2+) (By similarity). {ECO:0000250}. +Q64GA5 PA24C_MOUSE Cytosolic phospholipase A2 gamma (cPLA2-gamma) (EC 3.1.1.4) (Phospholipase A2 group IVC) 597 67,882 Active site (2); Alternative sequence (1); Chain (1); Domain (1) FUNCTION: Has a preference for arachidonic acid at the sn-2 position of phosphatidylcholine as compared with palmitic acid. {ECO:0000250|UniProtKB:Q9UP65}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:15950603}. Nucleus envelope {ECO:0000269|PubMed:15950603}. Cytoplasm, cell cortex {ECO:0000269|PubMed:15950603}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:15950603}. Note=In germinal vesicle stage oocytes and early embryos, shows mainly uniform nuclear and cortical expression. During germinal vesicle breakdown, found in intensely stained foci which accumulate near the dissolving nuclear envelope. Also localizes to spindle poles at metaphase II. {ECO:0000269|PubMed:15950603}. TISSUE SPECIFICITY: Highly expressed in ovary, where it localizes to oocytes in preantral and antral stage follicles (at protein level). Not detected in other tissues tested. {ECO:0000269|PubMed:15950603}. +Q50L42 PA24E_MOUSE Cytosolic phospholipase A2 epsilon (cPLA2-epsilon) (EC 3.1.1.4) (Phospholipase A2 group IVE) 875 100,157 Active site (2); Alternative sequence (3); Chain (1); Domain (2); Modified residue (1); Sequence conflict (1) FUNCTION: Calcium-dependent phospholipase A2 that selectively hydrolyzes glycerophospholipids in the sn-2 position. {ECO:0000269|PubMed:15866882}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:15866882}. Lysosome membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Translocates to lysosomal membranes in a calcium-dependent fashion. DOMAIN: The N-terminal C2 domain associates with lipid membranes upon calcium binding. It modulates enzyme activity by presenting the active site to its substrate in response to elevations of cytosolic Ca(2+) (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Predominantly expressed in heart, skeletal muscle, testis and thyroid. Expressed at lower level in brain and stomach. {ECO:0000269|PubMed:15866882}. +Q50L41 PA24F_MOUSE Cytosolic phospholipase A2 zeta (cPLA2-zeta) (EC 3.1.1.4) (Phospholipase A2 group IVF) 855 96,364 Active site (2); Chain (1); Domain (2); Erroneous initiation (1); Sequence conflict (10) FUNCTION: Calcium-dependent phospholipase A2 that selectively hydrolyzes glycerophospholipids in the sn-2 position. Has higher enzyme activity for phosphatidylethanolamine than phosphatidylcholine. {ECO:0000269|PubMed:15866882}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:15866882}. Lysosome membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Translocates to lysosomal membranes in a calcium-dependent fashion. DOMAIN: The N-terminal C2 domain associates with lipid membranes upon calcium binding. It modulates enzyme activity by presenting the active site to its substrate in response to elevations of cytosolic Ca(2+) (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Strongly expressed in thyroid, expressed at intermediate level in stomach and at very low level in large intestine and prostate. {ECO:0000269|PubMed:15866882}. +P50580 PA2G4_MOUSE Proliferation-associated protein 2G4 (IRES-specific cellular trans-acting factor 45 kDa) (ITAF45) (Mpp1) (Proliferation-associated protein 1) (Protein p38-2G4) 394 43,699 Alternative sequence (1); Beta strand (13); Chain (1); Cross-link (1); Helix (10); Initiator methionine (1); Modified residue (6); Mutagenesis (1); Region (4); Sequence conflict (2); Turn (1) FUNCTION: May play a role in a ERBB3-regulated signal transduction pathway. Seems be involved in growth regulation. Acts a corepressor of the androgen receptor (AR) and is regulated by the ERBB3 ligand neuregulin-1/heregulin (HRG). Inhibits transcription of some E2F1-regulated promoters, probably by recruiting histone acetylase (HAT) activity. Binds RNA. Associates with 28S, 18S and 5.8S mature rRNAs, several rRNA precursors and probably U3 small nucleolar RNA. May be involved in regulation of intermediate and late steps of rRNA processing. May be involved in ribosome assembly (By similarity). Mediates cap-independent translation of specific viral IRESs (internal ribosomal entry site). Together with PTBP1 is required for the translation initiation on the foot-and-mouth disease virus (FMDV) IRES. Regulates cell proliferation, differentiation, and survival. Isoform 1 suppresses apoptosis whereas isoform 2 promotes cell differentiation (By similarity). {ECO:0000250|UniProtKB:Q6AYD3, ECO:0000250|UniProtKB:Q9UQ80, ECO:0000269|PubMed:10950867, ECO:0000269|PubMed:17690690}. PTM: Phosphorylated on serine and threonine residues. Phosphorylation is enhanced by HRG treatment. Basal phosphorylation is PKC-dependent and HRG-induced phosphorylation is predominantly PKC-independent. Phosphorylation at Ser-361 by PKC/PRKCD regulates its nucleolar localization. {ECO:0000250|UniProtKB:Q9UQ80}.; PTM: Isoform 2 is polyubiquitinated, leading to proteasomal degradation and phosphorylation by PKC/PRKCD enhances polyubiquitination. {ECO:0000250|UniProtKB:Q9UQ80}. SUBCELLULAR LOCATION: Isoform 1: Cytoplasm {ECO:0000250|UniProtKB:Q9UQ80}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9UQ80}. Note=Phosphorylation at Ser-361 by PKC/PRKCD regulates its nucleolar localization. {ECO:0000250|UniProtKB:Q9UQ80}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm {ECO:0000269|PubMed:7556453}. SUBUNIT: Isoform 2 interacts with the cytoplasmic domain of non-phosphorylated ERBB3; the interaction requires PKC activity. Interacts with AR. Treatment with HRG leads to dissociation from ERBB3 and increases association with AR. Interacts with nucleolin/NCL. Component of a ribonucleoprotein complex containing at least PA2G4, NCL, TOP1, PABPC2, RPLP0, acetylated histone H1 (HIST1H1A or H1F1), histone H1 2/4, RPL4, RPL8, RPL15, RPL18, RPL18A, RPL21, RPL11, RPL12, RPL28, RPL27, RPLP2 and RPL24. Interacts with HDAC2. Interacts with RB1; the interaction is enhanced upon PA2G4 dephosphorylation (By similarity). Interacts with AKT1 (By similarity). Isoform 1 and isoform 2 interact with RNF20 (By similarity). Isoform 2 interacts with HUWE1. Interacts with DNAJC21 (By similarity). {ECO:0000250|UniProtKB:Q6AYD3, ECO:0000250|UniProtKB:Q9UQ80}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15064750}. +P48076 PA2GC_MOUSE Group IIC secretory phospholipase A2 (GIIC sPLA2) (sPLA2-IIC) (EC 3.1.1.4) (14 kDa phospholipase A2) (PLA2-8) (Phosphatidylcholine 2-acylhydrolase 2C) 150 16,983 Active site (2); Chain (1); Disulfide bond (8); Glycosylation (1); Metal binding (4); Sequence conflict (2); Signal peptide (1) FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Testis PA2 may be important in the production of prostaglandins, by the release of arachidonic acid, which in turn are necessary for the contractions of the seminiferous tubules and the testicular capsule; they also seem to decrease sperm transit time through the male reproductive tract. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Testis specific. +Q9WVF6 PA2GD_MOUSE Group IID secretory phospholipase A2 (GIID sPLA2) (sPLA2-IID) (EC 3.1.1.4) (PLA2IID) (Phosphatidylcholine 2-acylhydrolase 2D) (Secretory-type PLA, stroma-associated homolog) 144 16,164 Active site (2); Alternative sequence (1); Chain (1); Disulfide bond (7); Glycosylation (1); Metal binding (4); Signal peptide (1) FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. L-alpha-1-palmitoyl-2-linoleoyl phosphatidylethanolamine is more efficiently hydrolyzed than the other phospholipids examined. SUBCELLULAR LOCATION: Isoform 1: Secreted {ECO:0000305}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm {ECO:0000305}. TISSUE SPECIFICITY: Expressed in several tissues including pancreas, spleen, thymus, skin, lung, and ovary. +Q9QXX3 PA2GX_MOUSE Group 10 secretory phospholipase A2 (EC 3.1.1.4) (Group X secretory phospholipase A2) (GX sPLA2) (sPLA2-X) (Phosphatidylcholine 2-acylhydrolase 10) 151 17,005 Active site (2); Chain (1); Disulfide bond (8); Metal binding (4); Propeptide (1); Sequence conflict (1); Signal peptide (1) FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Has a powerful potency for releasing arachidonic acid from cell membrane phospholipids. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Expressed in various tissues including the lung, thymus, and spleen. +P29341 PABP1_MOUSE Polyadenylate-binding protein 1 (PABP-1) (Poly(A)-binding protein 1) 636 70,671 Chain (1); Compositional bias (1); Domain (5); Modified residue (18); Region (1); Sequence conflict (1) FUNCTION: Binds the poly(A) tail of mRNA, including that of its own transcript. May be involved in cytoplasmic regulatory processes of mRNA metabolism such as pre-mRNA splicing. Its function in translational initiation regulation can either be enhanced by PAIP1 or repressed by PAIP2. Can probably bind to cytoplasmic RNA sequences other than poly(A) in vivo. Involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. Involved in regulation of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons; for the recognition of premature termination codons (PTC) and initiation of NMD a competitive interaction between UPF1 and PABPC1 with the ribosome-bound release factors is proposed (By similarity). By binding to long poly(A) tails, may protect them from uridylation by ZCCHC6/ZCCHC11 and hence contribute to mRNA stability (By similarity). {ECO:0000250|UniProtKB:P11940}. PTM: Phosphorylated by MAPKAPK2. {ECO:0000250|UniProtKB:P11940}.; PTM: Methylated by CARM1. Arg-493 is dimethylated, probably to asymmetric dimethylarginine (By similarity). {ECO:0000250|UniProtKB:P11940}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P11940}. Nucleus {ECO:0000250|UniProtKB:P11940}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Shuttles between the cytoplasm and the nucleus (By similarity). {ECO:0000250|UniProtKB:P11940}. SUBUNIT: Component of a multi subunit autoregulatory ribonucleoprotein complex (ARC), at least composed of IGF2BP1, PABPC1 and CSDE1. Identified in a mRNP complex, at least composed of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Directly interacts with IGF2BP1. Part of a complex associated with the FOS mCRD domain and consisting of HNRPD, SYNCRIP, PAIP1 and CSDE1/UNR. Interacts with the PABPC1-interacting motif-1 (PAM1) and -2 (PAM2) of PAIP1 and PAIP2. Interacts with PAIP1 with a 1:1 stoichiometry and with PAIP2 with a 1:2 stoichiometry. Identified in the spliceosome C complex. Interacts with NFX1. Interacts with AGO1, AGO2, GSPT1 and GSPT2. Interacts with LARP1 and LARP4B. May interact with SETX (By similarity). The interaction with CSDE1 is direct and RNA-independent (PubMed:15314026). Found in a mRNP complex with YBX2 (PubMed:10076007). Interacts with TENT2/GLD2 (PubMed:17927953). Interacts with PIWIL1 (PubMed:19020299). Interacts (via the second and third RRM domains and the C-terminus) with PAIP2B (via central acidic portion and C-terminus). Interacts with LARP1. Interacts with RYDEN (By similarity). Found in a complex with RYDEN and LARP1. Interacts with LARP4 (By similarity). Interacts with ZFC3H1 in a RNase-sensitive manner (By similarity). Interacts with TRIM71 (via NHL repeats) in an RNA-dependent manner (By similarity). Interacts with TENT5C; the interaction has no effect on TENT5C poly(A) polymerase function (By similarity). {ECO:0000250|UniProtKB:P11940, ECO:0000269|PubMed:10076007, ECO:0000269|PubMed:15314026, ECO:0000269|PubMed:17927953, ECO:0000269|PubMed:19020299}. DOMAIN: The RNA-binding domains RRM1 and RRM2 and the C-terminus (last 138 amino acids) regions interact respectively with the PABPC1-interacting motif-1 (PAM1) and -2 (PAM2) of PAIP1, respectively. {ECO:0000250|UniProtKB:P11940}.; DOMAIN: The RNA-binding domains RRM2 and RRM3 and the C-terminus (last 138 amino acids) regions interact with the PABPC1-interacting motif-1 (PAM1) and -2 (PAM2) of PAIP2, respectively. {ECO:0000250|UniProtKB:P11940}. +Q8CCS6 PABP2_MOUSE Polyadenylate-binding protein 2 (PABP-2) (Poly(A)-binding protein 2) (Nuclear poly(A)-binding protein 1) (Poly(A)-binding protein II) (PABII) (Polyadenylate-binding nuclear protein 1) 302 32,297 Alternative sequence (2); Chain (1); Coiled coil (1); Compositional bias (1); Domain (1); Initiator methionine (1); Modified residue (24); Region (4) FUNCTION: Involved in the 3'-end formation of mRNA precursors (pre-mRNA) by the addition of a poly(A) tail of 200-250 nt to the upstream cleavage product. Stimulates poly(A) polymerase (PAPOLA) conferring processivity on the poly(A) tail elongation reaction and controls also the poly(A) tail length. Increases the affinity of poly(A) polymerase for RNA. Is also present at various stages of mRNA metabolism including nucleocytoplasmic trafficking and nonsense-mediated decay (NMD) of mRNA. Cooperates with SKIP to synergistically activate E-box-mediated transcription through MYOD1 and may regulate the expression of muscle-specific genes. Binds to poly(A) and to poly(G) with high affinity. May protect the poly(A) tail from degradation. Subunit of the trimeric poly(A) tail exosome targeting (PAXT) complex, a complex that directs a subset of long and polyadenylated poly(A) RNAs for exosomal degradation. The RNA exosome is fundamental for the degradation of RNA in eukaryotic nuclei. Substrate targeting is facilitated by its cofactor MTREX, which links to RNA-binding protein adapters (By similarity). {ECO:0000250|UniProtKB:Q28165, ECO:0000250|UniProtKB:Q86U42}. PTM: Arginine dimethylation is asymmetric and involves PRMT1 and PRMT3. It does not influence the RNA binding properties (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q86U42}. Nucleus {ECO:0000250|UniProtKB:Q86U42}. Nucleus speckle {ECO:0000250|UniProtKB:Q86U42}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Shuttles between the nucleus and the cytoplasm but predominantly found in the nucleus. Its nuclear import may involve the nucleocytoplasmic transport receptor transportin and a RAN-GTP-sensitive import mechanism. It is exported to the cytoplasm by a carrier-mediated pathway that is independent of mRNA traffic. Nucleus; nuclear speckle (By similarity). Colocalizes with SKIP and poly(A) RNA in nuclear speckles (By similarity). {ECO:0000250|UniProtKB:Q28165, ECO:0000250|UniProtKB:Q86U42}. SUBUNIT: Monomer and homooligomer. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Binds RNA as a monomer and oligomerizes when bound to poly(A). Interacts with PAPOLA, but only in presence of oligo(A) RNA. Interacts with NUDT21/CPSF5 and transportin. Associates in a ternary complex with CPSF4 and NS/NS1 and interaction with NS/NS1, blocks nuclear export of host cell mRNAs. Associates in a single complex with SKIP and MYOD1 and interacts with SKIP in differentiated myocytes. May interact with SETX (By similarity). Interacts (via RRM domain and C-terminal arginine-rich region) with ZFP36 (via hypophosphorylated form); this interaction occurs in the nucleus in a RNA-independent manner, decreases in presence of single-stranded poly(A) RNA-oligomer and in a p38-dependent-manner and may down-regulated RNA poly(A) polymerase activity (PubMed:22844456). Component of the poly(A) tail exosome targeting (PAXT) complex composed of PABPN1, ZFC3H1 and MTREX. Interacts with ZFC3H1 in a RNase-insensitive manner (By similarity). {ECO:0000250|UniProtKB:Q86U42, ECO:0000269|PubMed:22844456}. DOMAIN: The RRM domain is essential for specific adenine bases recognition in the poly(A) tail but not sufficient for poly(A) binding. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9434149}. +Q5SUR0 PUR4_MOUSE Phosphoribosylformylglycinamidine synthase (FGAM synthase) (FGAMS) (EC 6.3.5.3) (Formylglycinamide ribonucleotide amidotransferase) (FGAR amidotransferase) (FGAR-AT) (Formylglycinamide ribotide amidotransferase) 1337 144,629 Active site (3); Binding site (2); Chain (1); Domain (1); Metal binding (4); Modified residue (3); Nucleotide binding (2); Sequence conflict (2) Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 1/2. FUNCTION: Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +Q9DBQ7 PACE1_MOUSE Protein-associating with the carboxyl-terminal domain of ezrin (Ezrin-binding protein PACE-1) (SCY1-like protein 3) 735 81,333 Alternative sequence (3); Chain (1); Domain (1); Erroneous termination (1); Erroneous translation (1); Initiator methionine (1); Lipidation (1); Modified residue (2); Region (1); Repeat (4); Sequence conflict (2) FUNCTION: May play a role in regulating cell adhesion/migration complexes in migrating cells. PTM: May be myristoylated; myristoylation may target it to Golgi compartment. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Note=Colocalized with EZR/VIL2, actin and CD44 in lamellipodia. {ECO:0000250}. SUBUNIT: Interacts with EZR/VIL2 C-terminal domain. {ECO:0000250}. DOMAIN: The protein kinase domain is predicted to be catalytically inactive. +Q8K3V4 PADI6_MOUSE Protein-arginine deiminase type-6 (EC 3.5.3.15) (Arginine deiminase-like protein) (Egg and embryo abundant PAD) (ePAD) (Peptidylarginine deiminase VI) (Protein-arginine deiminase type VI) 682 76,778 Chain (1); Modified residue (2); Sequence conflict (4) FUNCTION: Catalyzes the deimination of arginine residues of proteins (By similarity). May be involved in cytoskeletal reorganization in the egg and early embryo (PubMed:17587491). {ECO:0000250, ECO:0000269|PubMed:17587491}. PTM: Phosphorylation at Ser-2, possibly by RSK-type kinases, and Ser-434 creates binding sites for 14-3-3 proteins. {ECO:0000250|UniProtKB:Q6TGC4}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12654293}. Nucleus {ECO:0000269|PubMed:12654293}. Note=Predominantly cytoplasmic (oocyte cytoplasmic sheets), also nuclear. TISSUE SPECIFICITY: Expressed at very high levels in oocytes. Weakly expressed in testis. Expressed in primordial, primary, secondary and Graafian follicles, and in immature oocytes, mature eggs and blastocyst (at protein level). {ECO:0000269|PubMed:12654293}. +Q8K212 PACS1_MOUSE Phosphofurin acidic cluster sorting protein 1 (PACS-1) 961 104,829 Chain (1); Coiled coil (1); Compositional bias (4); Initiator methionine (1); Modified residue (14); Sequence conflict (1) FUNCTION: Coat protein that is involved in the localization of trans-Golgi network (TGN) membrane proteins that contain acidic cluster sorting motifs. Controls the endosome-to-Golgi trafficking of furin and mannose-6-phosphate receptor by connecting the acidic-cluster-containing cytoplasmic domain of these molecules with the adapter-protein complex-1 (AP-1) of endosomal clathrin-coated membrane pits (By similarity). {ECO:0000250|UniProtKB:O88588, ECO:0000250|UniProtKB:Q6VY07}. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:O88588}. Note=Localizes in the perinuclear region, probably the TGN. {ECO:0000250|UniProtKB:O88588}. SUBUNIT: Associates with AP-1 and AP-3 but not with AP-2 complexes (By similarity). Interacts with FURIN (PubMed:9695949). Forms a ternary complex with FURIN and AP-1 (By similarity). Interacts with PKD2 (via acidic region) (PubMed:15692563). {ECO:0000250|UniProtKB:Q6VY07, ECO:0000269|PubMed:15692563, ECO:0000269|PubMed:9695949}. +Q9CQX4 PAF15_MOUSE PCNA-associated factor (HCV NS5A-transactivated protein 9 homolog) (PCNA-associated factor of 15 kDa) (PAF15) (p15PAF) (PCNA-clamp-associated factor) 110 11,993 Chain (1); Cross-link (2); Modified residue (3); Motif (4); Sequence conflict (2) FUNCTION: PCNA-binding protein that acts as a regulator of DNA repair during DNA replication. Following DNA damage, the interaction with PCNA is disrupted, facilitating the interaction between monoubiquitinated PCNA and the translesion DNA synthesis DNA polymerase eta (POLH) at stalled replisomes, facilitating the bypass of replication-fork-blocking lesions. Also acts as a regulator of centrosome number (By similarity). {ECO:0000250}. PTM: Monoubiquitinated at Lys-15 and Lys-24 during normal S phase, promoting its association with PCNA. Also diubiquitinated at these 2 sites. Following DNA damage, monoubiquitin chains at Lys-15 and Lys-24 are probably extended, leading to disrupt the interaction with PCNA. Polyubiquitinated by the APC/C complex at the mitotic exit, leading to its degradation by the proteasome (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15004}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q15004}. Note=Following DNA damage, localizes to DNA damage sites. Colocalizes with centrosomes in perinuclear region. {ECO:0000250|UniProtKB:Q15004}. SUBUNIT: Interacts (when monoubiquitinated at Lys-15 and Lys-24) with PCNA. Interacts with isoform 2/p33ING1b of ING1. Interacts with BRCA1 (By similarity). {ECO:0000250}. DOMAIN: The PIP-box mediates the interaction with PCNA. {ECO:0000250}.; DOMAIN: The KEN box is required for the association with the APC/C complex. {ECO:0000250}.; DOMAIN: The D-box (destruction box) mediates the interaction with APC/C proteins, and acts as a recognition signal for degradation via the ubiquitin-proteasome pathway. {ECO:0000250}.; DOMAIN: The initiation motif is required for efficient chain initiation by the APC/C complex E2 ligase UBE2C. It determines the rate of substrate's degradation without affecting its affinity for the APC/C, a mechanism used by the APC/C to control the timing of substrate proteolysis during the cell cycle (By similarity). {ECO:0000250}. +Q60963 PAFA_MOUSE Platelet-activating factor acetylhydrolase (PAF acetylhydrolase) (EC 3.1.1.47) (1-alkyl-2-acetylglycerophosphocholine esterase) (2-acetyl-1-alkylglycerophosphocholine esterase) (LDL-associated phospholipase A2) (LDL-PLA(2)) (PAF 2-acylhydrolase) 440 49,258 Active site (3); Chain (1); Frameshift (1); Glycosylation (3); Sequence conflict (3); Signal peptide (1) FUNCTION: Modulates the action of platelet-activating factor (PAF) by hydrolyzing the sn-2 ester bond to yield the biologically inactive lyso-PAF. Has a specificity for substrates with a short residue at the sn-2 position. It is inactive against long-chain phospholipids. SUBCELLULAR LOCATION: Secreted, extracellular space. TISSUE SPECIFICITY: Plasma. +P10601 PAHO_MOUSE Pancreatic prohormone (Pancreatic polypeptide) (PP) [Cleaved into: Pancreatic hormone (PH); C-terminal peptide] 100 11,020 Modified residue (1); Peptide (2); Signal peptide (1) FUNCTION: Pancreatic hormone is synthesized in pancreatic islets of Langerhans and acts as a regulator of pancreatic and gastrointestinal functions. PTM: No icosapeptide-like peptide is cleaved from the C-terminal. SUBCELLULAR LOCATION: Secreted. +P22777 PAI1_MOUSE Plasminogen activator inhibitor 1 (PAI) (PAI-1) (Endothelial plasminogen activator inhibitor) (Serpin E1) 402 45,170 Beta strand (14); Chain (1); Glycosylation (3); Helix (12); Sequence conflict (1); Signal peptide (1); Site (1); Turn (4) FUNCTION: Serine protease inhibitor. Inhibits TMPRSS7. Is a primary inhibitor of tissue-type plasminogen activator (PLAT) and urokinase-type plasminogen activator (PLAU). As PLAT inhibitor, it is required for fibrinolysis down-regulation and is responsible for the controlled degradation of blood clots. As PLAU inhibitor, it is involved in the regulation of cell adhesion and spreading. Acts as a regulator of cell migration, independently of its role as protease inhibitor. It is required for stimulation of keratinocyte migration during cutaneous injury repair (By similarity). Involved in cellular and replicative senescence (PubMed:16862142). Plays a role in alveolar type 2 cells senescence in the lung (PubMed:28722352). Is involved in the regulation of cementogenic differentiation of periodontal ligament stem cells, and regulates odontoblast differentiation and dentin formation during odontogenesis (By similarity). {ECO:0000250|UniProtKB:P05121, ECO:0000269|PubMed:16862142, ECO:0000269|PubMed:28722352}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P05121}. SUBUNIT: Forms a heterodimer with TMPRSS7. Interacts with VTN. Binds LRP1B; binding is followed by internalization and degradation. Interacts with PPP1CB. {ECO:0000250|UniProtKB:P05121}. +Q91W45 PAI2B_MOUSE Polyadenylate-binding protein-interacting protein 2B (PABP-interacting protein 2B) (PAIP-2B) (Poly(A)-binding protein-interacting protein 2B) 136 15,472 Chain (1); Erroneous initiation (1); Sequence conflict (1) FUNCTION: Inhibits translation of capped and polyadenylated mRNAs by displacing PABPC1 from the poly(A) tail. {ECO:0000250|UniProtKB:Q9ULR5}. PTM: Ubiquitinated in vitro. {ECO:0000250|UniProtKB:Q9ULR5}. SUBUNIT: Interacts (via central acidic portion and C-terminus) with PABPC1 (via the second and third RRM domains and the C-terminus). {ECO:0000250|UniProtKB:Q9ULR5}. TISSUE SPECIFICITY: Expressed at very high levels in pancreas, at high levels in testis and at moderately high levels in brain, heart and lung (at protein level). {ECO:0000269|PubMed:16804161}. +Q9CY58 PAIRB_MOUSE Plasminogen activator inhibitor 1 RNA-binding protein (PAI1 RNA-binding protein 1) (PAI-RBP1) (SERPINE1 mRNA-binding protein 1) 407 44,714 Alternative sequence (4); Chain (1); Cross-link (6); Modified residue (26); Sequence conflict (2) FUNCTION: May play a role in the regulation of mRNA stability. Binds to the 3'-most 134 nt of the SERPINE1/PAI1 mRNA, a region which confers cyclic nucleotide regulation of message decay. Seems to play a role in PML-nuclear bodies formation. {ECO:0000250|UniProtKB:Q8NC51}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8NC51}. Nucleus {ECO:0000250|UniProtKB:Q8NC51}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8NC51}. SUBUNIT: Interacts with SPIN1 (PubMed:23894536). Interacts with CHD3 and TDRD3. Interacts with ZDHHC17 (via ANK repeats) (By similarity). {ECO:0000250|UniProtKB:Q8NC51, ECO:0000269|PubMed:23894536}. +O88643 PAK1_MOUSE Serine/threonine-protein kinase PAK 1 (EC 2.7.11.1) (Alpha-PAK) (CDC42/RAC effector kinase PAK-A) (p21-activated kinase 1) (PAK-1) (p65-PAK) 545 60,737 Active site (1); Binding site (1); Chain (1); Domain (2); Initiator methionine (1); Modified residue (24); Nucleotide binding (1); Region (3) FUNCTION: Protein kinase involved in intracellular signaling pathways downstream of integrins and receptor-type kinases that plays an important role in cytoskeleton dynamics, in cell adhesion, migration, proliferation, apoptosis, mitosis, and in vesicle-mediated transport processes. Can directly phosphorylate BAD and protects cells against apoptosis. Activated by interaction with CDC42 and RAC1. Functions as GTPase effector that links the Rho-related GTPases CDC42 and RAC1 to the JNK MAP kinase pathway. Phosphorylates and activates MAP2K1, and thereby mediates activation of downstream MAP kinases. Involved in the reorganization of the actin cytoskeleton, actin stress fibers and of focal adhesion complexes. Phosphorylates the tubulin chaperone TBCB and thereby plays a role in the regulation of microtubule biogenesis and organization of the tubulin cytoskeleton. Plays a role in the regulation of insulin secretion in response to elevated glucose levels. Part of a ternary complex that contains PAK1, DVL1 and MUSK that is important for MUSK-dependent regulation of AChR clustering during the formation of the neuromuscular junction (NMJ). Activity is inhibited in cells undergoing apoptosis, potentially due to binding of CDC2L1 and CDC2L2. Phosphorylates MYL9/MLC2. Phosphorylates RAF1 at 'Ser-338' and 'Ser-339' resulting in: activation of RAF1, stimulation of RAF1 translocation to mitochondria, phosphorylation of BAD by RAF1, and RAF1 binding to BCL2. Phosphorylates SNAI1 at 'Ser-246' promoting its transcriptional repressor activity by increasing its accumulation in the nucleus. In podocytes, promotes NR3C2 nuclear localization. Required for atypical chemokine receptor ACKR2-induced phosphorylation of LIMK1 and cofilin (CFL1) and for the up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. In synapses, seems to mediate the regulation of F-actin cluster formation performed by SHANK3, maybe through CFL1 phosphorylation and inactivation. Plays a role in RUFY3-mediated facilitating gastric cancer cells migration and invasion. {ECO:0000269|PubMed:10611223, ECO:0000269|PubMed:12165471, ECO:0000269|PubMed:12176334, ECO:0000269|PubMed:22669945, ECO:0000269|PubMed:23633677}. PTM: Autophosphorylated in trans, meaning that in a dimer, one kinase molecule phosphorylates the other one. Activated by autophosphorylation at Thr-423 in response to a conformation change, triggered by interaction with GTP-bound CDC42 or RAC1. Activated by phosphorylation at Thr-423 by BRSK2 and by PDPK1. Phosphorylated by JAK2 in response to PRL; this increases PAK1 kinase activity. Phosphorylated at Ser-21 by PKB/AKT; this reduces interaction with NCK1 and association with focal adhesion sites (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13153}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q13153}. Cell membrane {ECO:0000250|UniProtKB:Q13153}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q13153}. Cell projection, invadopodium {ECO:0000250|UniProtKB:Q13153}. Note=Recruited to the cell membrane by interaction with CDC42 and RAC1 (By similarity). Recruited to focal adhesions upon activation. Colocalized with CIB1 within membrane ruffles during cell spreading upon readhesion to fibronectin. Colocalizes with RUFY3, F-actin and other core migration components in invadopodia at the cell periphery (By similarity). {ECO:0000250|UniProtKB:P35465, ECO:0000250|UniProtKB:Q13153}. SUBUNIT: Homodimer in its autoinhibited state. Active as monomer. Component of cytoplasmic complexes, which also contains PXN, ARHGEF6 and GIT1. Interacts with NISCH (PubMed:15229651). Interacts with DVL1; mediates the formation of a DVL1, MUSK and PAK1 ternary complex involved in AChR clustering (By similarity). Binds to the caspase-cleaved p110 isoform of CDC2L1 and CDC2L2, p110C, but not the full-length proteins (By similarity). Interacts with ARHGEF7 (By similarity). Interacts tightly with GTP-bound but not GDP-bound CDC42/P21 and RAC1. Probably found in a ternary complex composed of DSCAM, PAK1 and RAC1. Interacts with DSCAM (via cytoplasmic domain); the interaction is direct and enhanced in presence of RAC1 (PubMed:15169762). Interacts with SCRIB (PubMed:18716323). Interacts with PDPK1 (By similarity). Interacts (via kinase domain) with RAF1 (By similarity). Interacts with NCK1 and NCK2 (By similarity). Interacts with TBCB (By similarity). Interacts with CRIPAK (By similarity). Interacts with BRSK2 (PubMed:22669945). Interacts with SNAI1 (By similarity). Interacts with CIB1 (via N-terminal region); the interaction is direct, promotes PAK1 activity and occurs in a calcium-dependent manner (By similarity). Interacts with INPP5K (PubMed:22751929). {ECO:0000250|UniProtKB:P35465, ECO:0000250|UniProtKB:Q13153, ECO:0000269|PubMed:15169762, ECO:0000269|PubMed:15229651, ECO:0000269|PubMed:18716323, ECO:0000269|PubMed:22751929}. +Q8CIN4 PAK2_MOUSE Serine/threonine-protein kinase PAK 2 (EC 2.7.11.1) (Gamma-PAK) (p21-activated kinase 2) (PAK-2) [Cleaved into: PAK-2p27; PAK-2p34] 524 57,930 Active site (1); Binding site (1); Chain (3); Domain (2); Initiator methionine (1); Modified residue (19); Motif (1); Nucleotide binding (1); Region (2); Site (1) FUNCTION: Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell motility, cell cycle progression, apoptosis or proliferation. Acts as downstream effector of the small GTPases CDC42 and RAC1. Activation by the binding of active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Full-length PAK2 stimulates cell survival and cell growth. Phosphorylates MAPK4 and MAPK6 and activates the downstream target MAPKAPK5, a regulator of F-actin polymerization and cell migration. Phosphorylates JUN and plays an important role in EGF-induced cell proliferation. Phosphorylates many other substrates including histone H4 to promote assembly of H3.3 and H4 into nucleosomes, BAD, ribosomal protein S6, or MBP. Additionally, associates with ARHGEF7 and GIT1 to perform kinase-independent functions such as spindle orientation control during mitosis. On the other hand, apoptotic stimuli such as DNA damage lead to caspase-mediated cleavage of PAK2, generating PAK-2p34, an active p34 fragment that translocates to the nucleus and promotes cellular apoptosis involving the JNK signaling pathway. Caspase-activated PAK2 phosphorylates MKNK1 and reduces cellular translation (By similarity). {ECO:0000250, ECO:0000269|PubMed:11278362}. PTM: Full-length PAK2 is autophosphorylated when activated by CDC42/p21. Following cleavage, both peptides, PAK-2p27 and PAK-2p34, become highly autophosphorylated. Autophosphorylation of PAK-2p27 can occur in the absence of any effectors and is dependent on phosphorylation of Thr-402, because PAK-2p27 is acting as an exogenous substrate (By similarity). {ECO:0000250}.; PTM: During apoptosis proteolytically cleaved by caspase-3 or caspase-3-like proteases to yield active PAK-2p34. {ECO:0000250}.; PTM: Ubiquitinated, leading to its proteasomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Serine/threonine-protein kinase PAK 2: Cytoplasm. Note=MYO18A mediates the cellular distribution of the PAK2-ARHGEF7-GIT1 complex to the inner surface of the cell membrane. {ECO:0000250}.; SUBCELLULAR LOCATION: PAK-2p34: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Note=Interaction with ARHGAP10 probably changes PAK-2p34 location to cytoplasmic perinuclear region. {ECO:0000250}. SUBUNIT: Interacts tightly with GTP-bound but not GDP-bound CDC42/p21 and RAC1. Interacts with SH3MD4. Interacts with SCRIB. Interacts with ARHGEF7 and GIT1. PAK-2p34 interacts with ARHGAP10. Interacts with RAC1 (By similarity). {ECO:0000250|UniProtKB:Q13177}. +Q0VB07 PGRP4_MOUSE Peptidoglycan recognition protein 4 (Peptidoglycan recognition protein I-beta) (PGLYRPIbeta) (PGRP-I-beta) (Peptidoglycan recognition protein intermediate beta) 374 41,190 Binding site (1); Chain (1); Disulfide bond (3); Domain (2); Glycosylation (3); Region (2); Sequence conflict (1); Signal peptide (1) FUNCTION: Pattern receptor that binds to murein peptidoglycans (PGN) of Gram-positive bacteria. Has bactericidal activity towards Gram-positive bacteria. May kill Gram-positive bacteria by interfering with peptidoglycan biosynthesis. Binds also to Gram-negative bacteria, and has bacteriostatic activity towards Gram-negative bacteria. Plays a role in innate immunity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Homodimer; disulfide-linked. Heterodimer with PGLYRP3; disulfide-linked (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15177568}. +Q99L02 PGR1A_MOUSE PAXIP1-associated glutamate-rich protein 1A (PAXIP1-associated protein 1) (PTIP-associated protein 1) 253 27,723 Chain (1); Compositional bias (1); Modified residue (4); Region (2) FUNCTION: Its association with the histone methyltransferase MLL2/MLL3 complex is suggesting a role in epigenetic transcriptional activation. However, in association with PAXIP1/PTIP is proposed to function at least in part independently of the MLL2/MLL3 complex. Proposed to be recruited by PAXIP1 to sites of DNA damage where the PAGR1:PAXIP1 complex is required for cell survival in response to DNA damage independently of the MLL2/MLL3 complex (PubMed:19124460). However, its function in DNA damage has been questioned (PubMed:26744420). During immunoglobulin class switching in activated B-cells is involved in transcription regulation of downstream switch regions at the immunoglobulin heavy-chain (Igh) locus independently of the MLL2/MLL3 complex (PubMed:26744420). Involved in both estrogen receptor-regulated gene transcription and estrogen-stimulated G1/S cell-cycle transition (By similarity). Acts as transcriptional cofactor for nuclear hormone receptors. Inhibits the induction properties of several steroid receptors such as NR3C1, AR and PPARG; the mechanism of inhibition appears to be gene-dependent (By similarity). May be involved in the regulation of the BMP pathway in extraembryonic development (PubMed:24633704). {ECO:0000250|UniProtKB:Q9BTK6, ECO:0000269|PubMed:19124460, ECO:0000269|PubMed:26744420, ECO:0000305, ECO:0000305|PubMed:24633704}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26744420}. SUBUNIT: Component of the KMT2 family MLL2/MLL3 complex, at least composed of the histone methyltransferases KMT2D and/or KMT2C, the common subunits ASH2L, RBBP5, WDR5 and DPY30, and the complex type-specific subunits PAXIP1/PTIP, PAGR1, NCOA6 and KDM6A; PAXIP1 is required for the association with the MLL2/MLL3 complex (By similarity). Forms a constitutive complex with PAXIP1/PTIP independently of the MLL2/MLL3 complex (PubMed:19124460, PubMed:26744420). Interacts with NCOA1, ESR1, NR3C1, AR (By similarity). {ECO:0000250|UniProtKB:Q9BTK6, ECO:0000269|PubMed:19124460, ECO:0000269|PubMed:26744420}. +Q9JHK4 PGTA_MOUSE Geranylgeranyl transferase type-2 subunit alpha (EC 2.5.1.60) (Geranylgeranyl transferase type II subunit alpha) (Rab geranyl-geranyltransferase subunit alpha) (Rab GG transferase alpha) (Rab GGTase alpha) (Rab geranylgeranyltransferase subunit alpha) 567 64,989 Alternative sequence (2); Chain (1); Modified residue (1); Repeat (11) FUNCTION: Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of Rab proteins with the C-terminal sequence -XXCC, -XCXC and -CCXX, such as RAB1A, RAB3A, RAB5A and RAB7A. {ECO:0000269|PubMed:10737774}. SUBUNIT: Heterotrimer composed of RABGGTA, RABGGTB and CHM; within this trimer, RABGGTA and RABGGTB form the catalytic component B, while CHM (component A) mediates peptide substrate binding. The Rab GGTase dimer (RGGT) interacts with CHM (component A) prior to Rab protein binding; the association is stabilized by geranylgeranyl pyrophosphate (GGpp). The CHM:RGGT:Rab complex is destabilized by GGpp (By similarity). {ECO:0000250}. DISEASE: Note=Defects in Rabggta are the cause of the gunmetal (gm) phenotype. Mice homozygous for gm have prolonged bleeding, thrombocytopenia and reduced platelet alpha- and delta-granule contents. {ECO:0000269|PubMed:10737774}. +Q8BUY9 PGTB1_MOUSE Geranylgeranyl transferase type-1 subunit beta (EC 2.5.1.59) (Geranylgeranyl transferase type I subunit beta) (GGTase-I-beta) (Type I protein geranyl-geranyltransferase subunit beta) 377 42,354 Chain (1); Metal binding (3); Region (3); Repeat (4) FUNCTION: Catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to a cysteine at the fourth position from the C-terminus of proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. Known substrates include RAC1, RAC2, RAP1A and RAP1B (By similarity). {ECO:0000250}. SUBUNIT: Heterodimer of FNTA and PGGT1B. PGGT1B mediates interaction with substrate peptides (By similarity). {ECO:0000250}. +O35691 PININ_MOUSE Pinin 725 82,436 Chain (1); Coiled coil (4); Compositional bias (5); Cross-link (15); Initiator methionine (1); Modified residue (17); Region (1); Sequence conflict (9) FUNCTION: Transcriptional activator binding to the E-box 1 core sequence of the E-cadherin promoter gene; the core-binding sequence is 5'CAGGTG-3'. Capable of reversing CTBP1-mediated transcription repression. Auxiliary component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Participates in the regulation of alternative pre-mRNA splicing. Associates to spliced mRNA within 60 nt upstream of the 5'-splice sites. Component of the PSAP complex which binds RNA in a sequence-independent manner and is proposed to be recruited to the EJC prior to or during the splicing process and to regulate specific excision of introns in specific transcription subsets. Involved in the establishment and maintenance of epithelia cell-cell adhesion (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}. Cell junction, desmosome {ECO:0000250}. Note=Cell-cell contact area, predominantly desmosome of intercellular adherens junction. Not a nucleocytoplasmic shuttling protein (By similarity). {ECO:0000250}. SUBUNIT: Found in a mRNA splicing-dependent exon junction complex (EJC). Found in a complex with SR proteins. Found in a mRNP complex with RNPS1. Component of the PSAP complex consisting of RNPS1, SAP18 and PNN. Interacts with PNISR, CTBP1, CTBP2, KRT8, KRT18, KRT19, PS1D/PNO40, PPIG, RNPS1, SFRS4 and SRRM2. Identified in the spliceosome C complex (By similarity). {ECO:0000250}. +Q62070 PIM2_MOUSE Serine/threonine-protein kinase pim-2 (EC 2.7.11.1) 370 40,060 Active site (1); Alternative sequence (3); Binding site (1); Chain (1); Domain (1); Nucleotide binding (1) FUNCTION: Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation. Exerts its oncogenic activity through: the regulation of MYC transcriptional activity, the regulation of cell cycle progression, the regulation of cap-dependent protein translation and through survival signaling by phosphorylation of a pro-apoptotic protein, BAD. Phosphorylation of MYC leads to an increase of MYC protein stability and thereby an increase of transcriptional activity. The stabilization of MYC exerted by PIM2 might explain partly the strong synergism between these 2 oncogenes in tumorigenesis. Regulates cap-dependent protein translation in a mammalian target of rapamycin complex 1 (mTORC1)-independent manner and in parallel to the PI3K-Akt pathway. Mediates survival signaling through phosphorylation of BAD, which induces release of the anti-apoptotic protein Bcl-X(L)/BCL2L1. Promotes cell survival in response to a variety of proliferative signals via positive regulation of the I-kappa-B kinase/NF-kappa-B cascade; this process requires phosphorylation of MAP3K8/COT. Promotes growth factor-independent proliferation by phosphorylation of cell cycle factors such as CDKN1A and CDKN1B. Involved in the positive regulation of chondrocyte survival and autophagy in the epiphyseal growth plate. {ECO:0000269|PubMed:12869584, ECO:0000269|PubMed:12954615, ECO:0000269|PubMed:15199164, ECO:0000269|PubMed:15548703, ECO:0000269|PubMed:15705789, ECO:0000269|PubMed:17476689, ECO:0000269|PubMed:18438430, ECO:0000269|PubMed:9294606}. PTM: Autophosphorylated. {ECO:0000269|PubMed:12869584, ECO:0000269|PubMed:12954615, ECO:0000269|PubMed:15548703}. SUBUNIT: Interacts with MYC. {ECO:0000269|PubMed:18438430}. TISSUE SPECIFICITY: Widely expressed, with highest expression in spleen, thymus and brain. Expressed in epiphyseal chondrocytes. {ECO:0000269|PubMed:17476689, ECO:0000269|PubMed:9294606}. +Q99MQ3 PINK1_MOUSE Serine/threonine-protein kinase PINK1, mitochondrial (EC 2.7.11.1) (BRPK) (PTEN-induced putative kinase protein 1) 580 63,181 Active site (1); Binding site (1); Chain (1); Domain (1); Modified residue (2); Nucleotide binding (1); Sequence conflict (6); Topological domain (2); Transit peptide (1); Transmembrane (1) TRANSMEM 94 110 Helical. {ECO:0000255}. TOPO_DOM 78 93 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 111 580 Cytoplasmic. {ECO:0000255}. FUNCTION: Protects against mitochondrial dysfunction during cellular stress by phosphorylating mitochondrial proteins (PubMed:24652937). Involved in the clearance of damaged mitochondria via selective autophagy (mitophagy) by mediating activation and translocation of PRKN (PubMed:24784582). Targets PRKN to dysfunctional depolarized mitochondria through the phosphorylation of MFN2 (By similarity). Activates PRKN in 2 steps: (1) by mediating phosphorylation at 'Ser-65' of PRKN and (2) mediating phosphorylation of ubiquitin, converting PRKN to its fully-active form (PubMed:24784582). Required for ubiquinone reduction by mitochondrial complex I by mediating phosphorylation of complex I subunit NDUFA10 (PubMed:24652937). {ECO:0000250|UniProtKB:Q9BXM7, ECO:0000269|PubMed:24652937, ECO:0000269|PubMed:24784582}. PTM: Autophosphorylated. {ECO:0000250|UniProtKB:Q9BXM7}.; PTM: Two shorter forms of 55 kDa and 48 kDa seem to be produced by proteolytic cleavage and localize mainly in cytosol. {ECO:0000250|UniProtKB:Q9BXM7}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q9BXM7}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9BXM7}. Mitochondrion inner membrane {ECO:0000269|PubMed:24652937}; Single-pass membrane protein {ECO:0000255}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9BXM7}. SUBUNIT: Interacts with PRKN and FBXO7 (By similarity). Forms a complex with PRKN and PARK7 (PubMed:19229105). {ECO:0000250|UniProtKB:Q9BXM7}. TISSUE SPECIFICITY: High levels expressed in testis, lower levels in brain, heart, lung, liver and kidney. {ECO:0000269|PubMed:14607334}. +Q9CQD7 PINLY_MOUSE phospholipase A2 inhibitor and Ly6/PLAUR domain-containing protein 212 22,819 Chain (1); Disulfide bond (7); Domain (1); Sequence conflict (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q7TN88 PK1L2_MOUSE Polycystic kidney disease protein 1-like 2 (PC1-like 2 protein) (Polycystin-1L2) 2461 271,977 Chain (1); Compositional bias (1); Disulfide bond (2); Domain (6); Glycosylation (11); Region (1); Signal peptide (1); Transmembrane (11) TRANSMEM 1346 1366 Helical. {ECO:0000255}.; TRANSMEM 1554 1574 Helical. {ECO:0000255}.; TRANSMEM 1596 1616 Helical. {ECO:0000255}.; TRANSMEM 1816 1836 Helical. {ECO:0000255}.; TRANSMEM 1863 1883 Helical. {ECO:0000255}.; TRANSMEM 1940 1960 Helical. {ECO:0000255}.; TRANSMEM 2186 2206 Helical. {ECO:0000255}.; TRANSMEM 2222 2242 Helical. {ECO:0000255}.; TRANSMEM 2273 2293 Helical. {ECO:0000255}.; TRANSMEM 2315 2335 Helical. {ECO:0000255}.; TRANSMEM 2380 2400 Helical. {ECO:0000255}. FUNCTION: May function as an ion-channel regulator. May function as a G-protein-coupled receptor (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: May interact via its C-terminus with GNAS and GNAI1. {ECO:0000250}. +Q2EG98 PK1L3_MOUSE Polycystic kidney disease protein 1-like 3 (PC1-like 3 protein) (Polycystin-1L3) 2201 241,253 Alternative sequence (11); Chain (1); Compositional bias (1); Disulfide bond (2); Domain (3); Glycosylation (6); Mutagenesis (2); Region (1); Sequence conflict (16); Signal peptide (1); Topological domain (13); Transmembrane (12) TRANSMEM 1084 1104 Helical. {ECO:0000255}.; TRANSMEM 1294 1314 Helical. {ECO:0000255}.; TRANSMEM 1331 1351 Helical. {ECO:0000255}.; TRANSMEM 1544 1564 Helical. {ECO:0000255}.; TRANSMEM 1586 1606 Helical. {ECO:0000255}.; TRANSMEM 1667 1687 Helical. {ECO:0000255}.; TRANSMEM 1856 1876 Helical. {ECO:0000255}.; TRANSMEM 1903 1923 Helical. {ECO:0000255}.; TRANSMEM 1945 1965 Helical. {ECO:0000255}.; TRANSMEM 2033 2053 Helical. {ECO:0000255}.; TRANSMEM 2061 2078 Helical. {ECO:0000255}.; TRANSMEM 2099 2119 Helical. {ECO:0000255}. TOPO_DOM 25 1083 Extracellular. {ECO:0000255}.; TOPO_DOM 1105 1293 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1315 1330 Extracellular. {ECO:0000255}.; TOPO_DOM 1352 1543 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1565 1585 Extracellular. {ECO:0000255}.; TOPO_DOM 1607 1666 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1688 1855 Extracellular. {ECO:0000255}.; TOPO_DOM 1877 1902 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1924 1944 Extracellular. {ECO:0000255}.; TOPO_DOM 1966 2032 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 2054 2060 Extracellular. {ECO:0000255}.; TOPO_DOM 2079 2098 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 2120 2201 Extracellular. {ECO:0000255}. FUNCTION: Component of a calcium channel. May act as a sour taste receptor by forming a calcium channel with PKD1L3 in gustatory cells; however, its contribution to sour taste perception is unclear in vivo and may be indirect. {ECO:0000269|PubMed:16805797, ECO:0000269|PubMed:16891422, ECO:0000269|PubMed:16929298, ECO:0000269|PubMed:21098668, ECO:0000269|PubMed:21625513}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16891422, ECO:0000269|PubMed:21185261}; Multi-pass membrane protein {ECO:0000269|PubMed:16891422, ECO:0000269|PubMed:21185261}. Note=Interaction with PKD2L1 is required for localization to the cell membrane. SUBUNIT: Calcium channels are probably composed of 3 subunit of PKD2L1 and 1 subunit of PKD1L3. TISSUE SPECIFICITY: Expressed in a subset of taste receptor cells distinct from those involved in bitter, sweet and umami taste. Expressed in circumvallate and foliate taste buds, but not in surrounding non-gustatory lingual epithelium cells. Expressed in testis. {ECO:0000269|PubMed:16805797, ECO:0000269|PubMed:16891422, ECO:0000269|PubMed:16929298}. +Q9ERS4 PKHA3_MOUSE Pleckstrin homology domain-containing family A member 3 (PH domain-containing family A member 3) (Phosphatidylinositol-four-phosphate adapter protein 1) (FAPP-1) (Phosphoinositol 4-phosphate adapter protein 1) 297 33,423 Chain (1); Domain (1); Modified residue (1) FUNCTION: Involved in Golgi to cell surface membrane traffic. Induces membrane tubulation. Binds preferentially to phosphatidylinositol 4-phosphate (PtdIns4P) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. SUBUNIT: Interacts with GTP-bound ARF1. {ECO:0000250}. DOMAIN: The PH domain of FAPPS binds the small GTPase ARF1 and phosphatidylinositol-4-phosphate (PtdIns4P) with high selectivity, and is required for recruitment of FAPPs to the trans-Golgi network (TGN). {ECO:0000250}. +Q8BFY0 PIRT_MOUSE Phosphoinositide-interacting protein 135 15,264 Chain (1); Mutagenesis (2); Transmembrane (2) TRANSMEM 54 74 Helical. {ECO:0000255}.; TRANSMEM 92 112 Helical. {ECO:0000255}. FUNCTION: Regulatory subunit of TRPV1, a molecular sensor of noxious heat and capsaicin. Positively regulates TRPV1 channel activity via phosphatidylinositol 4,5-bisphosphate (PIP2). Binds various phosphoinositide, including phosphatidylinositol 4,5-bisphosphate (PIP2), but not phosphatidylinositol (PI). {ECO:0000269|PubMed:18455988}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Interacts with TRPV1. {ECO:0000269|PubMed:18455988}. TISSUE SPECIFICITY: Strongly expressed in most dorsal root ganglia (DRG) and trigeminal neurons. Expressed by most peptidergic (CGRP+) and non-peptidergic (IB4+) DRG neurons. Weakly expressed in other parts of the peripheral nervous system (PNS) including sympathetic and enteric neurons. Not expressed in the spinal cord. {ECO:0000269|PubMed:18455988}. +Q80ZA4 PKHL1_MOUSE Fibrocystin-L (Polycystic kidney and hepatic disease 1-like protein 1) (PKHD1-like protein 1) (Protein D86) 4249 464,732 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (17); Glycosylation (4); Repeat (10); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 4223 4243 Helical. {ECO:0000255}. TOPO_DOM 21 4222 Extracellular. {ECO:0000255}.; TOPO_DOM 4244 4249 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q9D711 PIR_MOUSE Pirin (EC 1.13.11.24) (Probable quercetin 2,3-dioxygenase PIR) (Probable quercetinase) 290 32,066 Chain (1); Metal binding (4); Sequence conflict (1) Flavonoid metabolism; quercetin degradation. FUNCTION: Transcriptional coregulator of NF-kappa-B which facilitates binding of NF-kappa-B proteins to target kappa-B genes in a redox-state-dependent manner. May be required for efficient terminal myeloid maturation of hematopoietic cells. Has quercetin 2,3-dioxygenase activity (in vitro) (By similarity). {ECO:0000250, ECO:0000269|PubMed:20010624}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Predominantly localized in dot-like subnuclear structures. {ECO:0000250}. SUBUNIT: May interact with NF1/CTF1. Interacts with BCL3. Identified in a complex comprised of PIR, BLC3, NFKB1 and target DNA (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Weakly expressed in bone marrow. {ECO:0000269|PubMed:20010624}. +Q7TSI1 PKHM1_MOUSE Pleckstrin homology domain-containing family M member 1 (PH domain-containing family M member 1) 1074 118,535 Chain (1); Domain (3); Modified residue (4); Motif (1); Mutagenesis (2); Region (1); Sequence conflict (2); Zinc finger (1) FUNCTION: Proposed to act as a multivalent adapter protein that regulates Rab7-dependent and HOPS complex-dependent fusion events in the endolysosomal system and couples autophagic and the endocytic trafficking pathways. Required for late stages of endolysosomal maturation, facilitating both endocytosis-mediated degradation of growth factor receptors and autophagosome clearance. Seems to be involved in the terminal maturation of autophagosomes and to mediate autophagosome-lysosome fusion (PubMed:25498145). Positively regulates lysosome peripheral distribution and ruffled border formation in osteoclasts (PubMed:27777970). May be involved in negative regulation of endocytic transport from early endosome to late endosome/lysosome implicating its association with Rab7 (By similarity). May have a role in sialyl-lex-mediated transduction of apoptotic signals (By similarity). Involved in bone resorption (PubMed:27777970). {ECO:0000250|UniProtKB:Q5PQS0, ECO:0000250|UniProtKB:Q9Y4G2, ECO:0000269|PubMed:25498145, ECO:0000269|PubMed:27777970, ECO:0000305}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Endosome membrane {ECO:0000250|UniProtKB:Q9Y4G2}. Lysosome {ECO:0000250|UniProtKB:Q9Y4G2}. Lysosome membrane {ECO:0000250|UniProtKB:Q9Y4G2}. Note=Localizes to the external membrane of autolysosomes. {ECO:0000250|UniProtKB:Q9Y4G2}. SUBUNIT: Interacts with VPS41, VPS11 and VPS39; indicative for an association with the HOPS complex; the interaction with VPS41 seems to require RAB7A. Interacts with GABARAP, GABARAPL, GABARAPL2, MAP1LC3A, MAP1LC3B and MAP1LC3C (By similarity). Interacts with PAFAH1B1; detected in osteoblasts (PubMed:22073305). Interacts (via N- and C-terminus) with NDEL1 (PubMed:27777970). Interacts (via C-terminus) with MAP3K7 (PubMed:27777970). Interacts (via N- and C-terminus) with FAM98A (PubMed:27777970). Interacts (via C-terminus) with DEF8; this interaction is weak but increased in a RAB7A-dependent manner (PubMed:27777970). Interacts (via N- and C-terminus) with RAB7A (GTP-bound form) (PubMed:27777970). May interact with sialyl-lex positive protein (By similarity). {ECO:0000250|UniProtKB:Q9Y4G2, ECO:0000269|PubMed:22073305, ECO:0000269|PubMed:27777970}. DOMAIN: The LIR (LC3-interacting region) motif mediates the interaction with ATG8 family proteins GABARAP, GABARAPL, GABARAPL2, and LC3A/B/C. {ECO:0000250|UniProtKB:Q9Y4G2}. +O35904 PK3CD_MOUSE Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform (PI3-kinase subunit delta) (PI3K-delta) (PI3Kdelta) (PtdIns-3-kinase subunit delta) (EC 2.7.1.153) (Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit delta) (PtdIns-3-kinase subunit p110-delta) (p110delta) 1043 119,712 Alternative sequence (2); Beta strand (32); Chain (1); Domain (5); Helix (43); Modified residue (2); Mutagenesis (1); Sequence conflict (3); Turn (8) Phospholipid metabolism; phosphatidylinositol phosphate biosynthesis. FUNCTION: Phosphoinositide-3-kinase (PI3K) that phosphorylates PftdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Mediates immune responses. Plays a role in B-cell development, proliferation, migration, and function. Required for B-cell receptor (BCR) signaling. Mediates B-cell proliferation response to anti-IgM, anti-CD40 and IL4 stimulation. Promotes cytokine production in response to TLR4 and TLR9. Required for antibody class switch mediated by TLR9. Involved in the antigen presentation function of B-cells. Involved in B-cell chemotaxis in response to CXCL13 and sphingosine 1-phosphate (S1P). Required for proliferation, signaling and cytokine production of naive, effector and memory T-cells. Required for T-cell receptor (TCR) signaling. Mediates TCR signaling events at the immune synapse. Activation by TCR leads to antigen-dependent memory T-cell migration and retention to antigenic tissues. Together with PIK3CG participates in T-cell development. Contributes to T-helper cell expansion and differentiation. Required for T-cell migration mediated by homing receptors SELL/CD62L, CCR7 and S1PR1 and antigen dependent recruitment of T-cells. Together with PIK3CG is involved in natural killer (NK) cell development and migration towards the sites of inflammation. Participates in NK cell receptor activation. Have a role in NK cell maturation and cytokine production. Together with PIK3CG is involved in neutrophil chemotaxis and extravasation. Together with PIK3CG participates in neutrophil respiratory burst. Have important roles in mast-cell development and mast cell mediated allergic response. Involved in stem cell factor (SCF)-mediated proliferation, adhesion and migration. Required for allergen-IgE-induced degranulation and cytokine release. The lipid kinase activity is required for its biological function. {ECO:0000269|PubMed:12130661, ECO:0000269|PubMed:12235209, ECO:0000269|PubMed:15496927, ECO:0000269|PubMed:16116162, ECO:0000269|PubMed:18259608, ECO:0000269|PubMed:18809712, ECO:0000269|PubMed:19297623}. PTM: Autophosphorylation on Ser-1038 results in the almost complete inactivation of the lipid kinase activity. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Heterodimer of a catalytic subunit PIK3CD and a p85 regulatory subunit (PIK3R1, PIK3R2 or PIK3R3). Interacts with ERAS and HRAS. {ECO:0000269|PubMed:12774123}. TISSUE SPECIFICITY: Isoform 1 is expressed in spleen and lung (at protein level). Isoform 1 is expressed predominantly in leukocytes. {ECO:0000269|PubMed:22020336}. +P47932 REL1_MOUSE Prorelaxin 1 [Cleaved into: Relaxin B chain; Relaxin A chain] 185 20,571 Disulfide bond (3); Peptide (2); Propeptide (1); Signal peptide (1) FUNCTION: Relaxin is an ovarian hormone that acts with estrogen to produce dilatation of the birth canal in many mammals. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Heterodimer of a B chain and an A chain linked by two disulfide bonds. +Q8BLJ3 PLCX3_MOUSE PI-PLC X domain-containing protein 3 321 36,314 Active site (2); Chain (1); Domain (1); Sequence conflict (1) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q63HM9}. TISSUE SPECIFICITY: Widely expressed, with highest levels in brain, followed by heart atrium. Not detected in small intestine, nor stomach. {ECO:0000269|PubMed:22732399}. +Q8BVZ1 PLIN5_MOUSE Perilipin-5 (Lipid droplet-associated protein PAT-1) (Lipid storage droplet protein 5) (Myocardial LD protein) 463 50,474 Alternative sequence (1); Chain (1); Modified residue (3); Region (4) FUNCTION: Lipid droplet-associated protein that maintains the balance between lipogenesis and lipolysis and also regulates fatty acid oxidation in oxidative tissues. Recruits mitochondria to the surface of lipid droplets and is involved in lipid droplet homeostasis by regulating both the storage of fatty acids in the form of triglycerides and the release of fatty acids for mitochondrial fatty acid oxidation. In lipid droplet triacylglycerol hydrolysis, plays a role as a scaffolding protein for three major key lipolytic players: ABHD5, PNPLA2 and LIPE. Reduces the triacylglycerol hydrolase activity of PNPLA2 by recruiting and sequestering PNPLA2 to lipid droplets. Phosphorylation by PKA enables lipolysis probably by promoting release of ABHD5 from the perilipin scaffold and by facilitating interaction of ABHD5 with PNPLA2. Also increases lipolysis through interaction with LIPE and upon PKA-mediated phosphorylation of LIPE. {ECO:0000269|PubMed:17130488, ECO:0000269|PubMed:19064991, ECO:0000269|PubMed:21393244, ECO:0000269|PubMed:21885430, ECO:0000269|PubMed:22532565, ECO:0000269|PubMed:22675471, ECO:0000269|PubMed:23345411}. PTM: Phosphorylated by PKA. Phosphorylated on serine in skeletal muscle at rest or with lipolytic stimulation. {ECO:0000269|PubMed:21393244}. SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:16571721, ECO:0000269|PubMed:17130488, ECO:0000269|PubMed:17234449, ECO:0000269|PubMed:19717842, ECO:0000269|PubMed:23345411}. Cytoplasm {ECO:0000269|PubMed:17234449, ECO:0000269|PubMed:19717842}. Mitochondrion {ECO:0000250|UniProtKB:M0R7Z9}. Note=Lipid droplet surface-associated (PubMed:17234449, PubMed:17130488, PubMed:16571721). Exchanges between lipid droplets and the cytoplasm (PubMed:19717842). {ECO:0000269|PubMed:16571721, ECO:0000269|PubMed:17130488, ECO:0000269|PubMed:17234449, ECO:0000269|PubMed:19717842}. SUBUNIT: Homooligomer. Interacts with PNPLA2; prevents interaction of PNPLA2 with ABHD5. Interacts with ABHD5; targets ABHD5 to lipid droplets and promotes interaction of ABHD5 with PNPLA2. Interacts with LIPE. {ECO:0000269|PubMed:19064991, ECO:0000269|PubMed:19717842, ECO:0000269|PubMed:21148142, ECO:0000269|PubMed:21393244}. TISSUE SPECIFICITY: Highly expressed in oxidative tissues, including heart, liver, brown adipose tissue (BAT) and slow-twitch fibers of skeletal muscle. Lower expression in epididymal white adipose tissue and anterior tibialis and quadriceps. Expressed in adrenal glands. Isoform 2 has the highest expression in heart. {ECO:0000269|PubMed:16571721, ECO:0000269|PubMed:17130488, ECO:0000269|PubMed:17234449}. +Q8BG07 PLD4_MOUSE Phospholipase D4 (PLD 4) (EC 3.1.4.4) (Choline phosphatase 4) (Phosphatidylcholine-hydrolyzing phospholipase D4) 503 56,154 Active site (6); Alternative sequence (1); Chain (1); Domain (2); Frameshift (1); Sequence conflict (7); Transmembrane (1) TRANSMEM 37 57 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +O35621 PMM1_MOUSE Phosphomannomutase 1 (PMM 1) (EC 5.4.2.8) 262 29,775 Active site (2); Binding site (7); Chain (1); Initiator methionine (1); Metal binding (3); Modified residue (2) Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2. FUNCTION: Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions. In addition, may be responsible for the degradation of glucose-1,6-bisphosphate in ischemic brain. {ECO:0000269|PubMed:18927083}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16847318}. SUBUNIT: Homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Present in brain, where it is restricted to neuronal cell bodies. Present at lower levels in pancreas, liver, lung, gonads, uterus, adrenal glands and pituitary (at protein level). Undetectable in intestine. {ECO:0000269|PubMed:16847318}. +P48453 PP2BB_MOUSE Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform (EC 3.1.3.16) (CAM-PRP catalytic subunit) (Calmodulin-dependent calcineurin A subunit beta isoform) (CNA beta) 525 59,173 Active site (1); Alternative sequence (1); Chain (1); Compositional bias (1); Initiator methionine (1); Metal binding (7); Modified residue (2); Motif (1); Region (5); Sequence conflict (2) FUNCTION: Calcium-dependent, calmodulin-stimulated protein phosphatase which plays an essential role in the transduction of intracellular Ca(2+)-mediated signals. Dephosphorylates and activates transcription factor NFATC1. Dephosphorylates and inactivates transcription factor ELK1. Dephosphorylates DARPP32. {ECO:0000250|UniProtKB:P16298}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P16298}. SUBUNIT: Forms a complex composed of a calmodulin-dependent catalytic subunit (also known as calcineurin A) and a regulatory Ca(2+)-binding subunit (also known as calcineurin B). There are three catalytic subunits, each encoded by a separate gene (PPP3CA, PPP3CB, and PPP3CC) and two regulatory subunits which are also encoded by separate genes (PPP3R1 and PPP3R2). In response to an increase in Ca(2+) intracellular levels, forms a complex composed of PPP3CB/calcineurin A, calcineurin B and calmodulin. Interacts (via calcineurin B binding domain) with regulatory subunit PPP3R1/calcineurin B. Interacts (via calmodulin-binding domain) with calmodulin; the interaction depends on calmodulin binding to Ca(2+). {ECO:0000250|UniProtKB:P16298}. DOMAIN: The poly-Pro domain may confer substrate specificity. {ECO:0000250|UniProtKB:P16298}.; DOMAIN: The autoinhibitory domain prevents access to the catalytic site. {ECO:0000250|UniProtKB:P16298}.; DOMAIN: The autoinhibitory segment prevents access to the substrate binding site. {ECO:0000250|UniProtKB:P16298}.; DOMAIN: Possible isomerization of Pro-318 within the SAPNY motif triggers a conformation switch which affects the organization and thus accessibility of the active site and the substrate binding region (PxIxIF motif). The trans- to cis-transition may favor calcineurin A activation and substrate binding. The reverse cis- to trans-transition may be enhanced by peptidyl-prolyl isomerases such as PPIA. {ECO:0000250|UniProtKB:Q08209}. TISSUE SPECIFICITY: Two isoforms in Ehrlich ascites tumor (EAT) is demonstrated by polymerase chain reaction specific primers to the catalytic and calmodulin-binding domain, respectively. Isoform 1 is of medium abundance in EAT cells. {ECO:0000269|PubMed:1328240}. +P48455 PP2BC_MOUSE Serine/threonine-protein phosphatase 2B catalytic subunit gamma isoform (EC 3.1.3.16) (CAM-PRP catalytic subunit) (Calcineurin, testis-specific catalytic subunit) (Calmodulin-dependent calcineurin A subunit gamma isoform) 513 58,699 Active site (1); Chain (1); Metal binding (7); Motif (1); Region (5) FUNCTION: Calcium-dependent, calmodulin-stimulated protein phosphatase which plays an essential role in the transduction of intracellular Ca(2+)-mediated signals. Dephosphorylates and activates transcription factor NFATC1. Dephosphorylates and inactivates transcription factor ELK1. Dephosphorylates DARPP32. {ECO:0000250|UniProtKB:P48454}. SUBUNIT: Forms a complex composed of a calmodulin-dependent catalytic subunit (also known as calcineurin A) and a regulatory Ca(2+)-binding subunit (also known as calcineurin B). There are three catalytic subunits, each encoded by a separate gene (PPP3CA, PPP3CB, and PPP3CC) and two regulatory subunits which are also encoded by separate genes (PPP3R1 and PPP3R2). In response to an increase in Ca(2+) intracellular levels, forms a complex composed of PPP3CC/calcineurin A, calcineurin B and calmodulin. Interacts (via calmodulin-binding domain) with calmodulin; the interaction depends on calmodulin binding to Ca(2+). {ECO:0000250|UniProtKB:P16298, ECO:0000250|UniProtKB:P48454}. DOMAIN: The autoinhibitory domain prevents access to the catalytic site. {ECO:0000250|UniProtKB:P16298}.; DOMAIN: The autoinhibitory segment prevents access to the substrate binding site. {ECO:0000250|UniProtKB:P16298}.; DOMAIN: Possible isomerization of Pro-305 within the SAPNY motif triggers a conformation switch which affects the organization and thus accessibility of the active site and the substrate binding region (PxIxIF motif). The trans- to cis-transition may favor calcineurin A activation and substrate binding. The reverse cis- to trans-transition may be enhanced by peptidyl-prolyl isomerases such as PPIA. {ECO:0000250|UniProtKB:Q08209}. TISSUE SPECIFICITY: Testis. +Q8BVT6 PP2D1_MOUSE Protein phosphatase 2C-like domain-containing protein 1 620 70,630 Chain (1); Domain (1) +Q9D0B8 RIBC1_MOUSE RIB43A-like with coiled-coils protein 1 379 44,962 Chain (1); Coiled coil (2) +Q9D4Q1 RIBC2_MOUSE RIB43A-like with coiled-coils protein 2 309 37,323 Chain (1); Coiled coil (1) +P97470 PP4C_MOUSE Serine/threonine-protein phosphatase 4 catalytic subunit (PP4C) (Pp4) (EC 3.1.3.16) (Protein phosphatase X) (PP-X) 307 35,080 Active site (1); Chain (1); Frameshift (1); Initiator methionine (1); Metal binding (7); Modified residue (2); Sequence conflict (1) FUNCTION: Protein phosphatase that is involved in many processes such as microtubule organization at centrosomes, maturation of spliceosomal snRNPs, apoptosis, DNA repair, tumor necrosis factor (TNF)-alpha signaling, activation of c-Jun N-terminal kinase MAPK8, regulation of histone acetylation, DNA damage checkpoint signaling, NF-kappa-B activation and cell migration. The PPP4C-PPP4R1 PP4 complex may play a role in dephosphorylation and regulation of HDAC3. The PPP4C-PPP4R2-PPP4R3A PP4 complex specifically dephosphorylates H2AFX phosphorylated on Ser-140 (gamma-H2AFX) generated during DNA replication and required for DNA double strand break repair (By similarity). Dephosphorylates NDEL1 at CDK1 phosphorylation sites and negatively regulates CDK1 activity in interphase. In response to DNA damage, catalyzes RPA2 dephosphorylation, an essential step for DNA repair since it allows the efficient RPA2-mediated recruitment of RAD51 to chromatin (By similarity). {ECO:0000250, ECO:0000269|PubMed:18347064}. PTM: Methylation at the C-terminal Leu-307 is critical for interactions with regulatory subunits and functions in DNA repair. {ECO:0000250|UniProtKB:P60510}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. SUBUNIT: Serine/threonine-protein phosphatase 4 (PP4) occurs in different assemblies of the catalytic and one or more regulatory subunits. Component of the PP4 complexes PPP4C-PPP4R1, PPP4C-PPP4R2, PPP4C-PPP4R2-PPP4R3A, PPP4C-PPP4R2-PPP4R3B and PPP4C-PPP4R4. The PPP4C-PPP4R2 complex appears to be a tetramer composed of 2 molecules of PPP4C and 2 molecules of PPP4R2. Interacts with REL, NFKB1/p50 and RELA. Interacts with SMN1 AND GEMIN4. Interacts with IRS4 (phosphorylated). Interacts with SMEK1/PPP4R3A; the interaction requires PP4R2. Interacts with HDAC3 (By similarity). {ECO:0000250}. +Q69ZJ7 RIC1_MOUSE RAB6A-GEF complex partner protein 1 (Protein RIC1 homolog) 1422 158,829 Alternative sequence (4); Chain (1); Modified residue (7); Repeat (2); Transmembrane (1) TRANSMEM 1266 1286 Helical. {ECO:0000255}. FUNCTION: The RIC1-RGP1 complex acts as a guanine nucleotide exchange factor (GEF), which activates RAB6A by exchanging bound GDP for free GTP and may thereby required for efficient fusion of endosome-derived vesicles with the Golgi compartment. The RIC1-RGP1 complex participates in the recycling of mannose-6-phosphate receptors. Required for phosphorylation and localization of GJA1. {ECO:0000250|UniProtKB:Q4ADV7}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q4ADV7}. Membrane {ECO:0000250|UniProtKB:Q4ADV7}; Single-pass membrane protein {ECO:0000255}. SUBUNIT: Forms a complex with RGP1; the interaction enhances RAB6A GTPase activity. Interacts (via central domain) with RGP1. Interacts with RAB6A; the interaction is direct with a preference for RAB6A-GDP. Interacts (via C-terminus domain) with RAB33B; the interaction is direct with a preference for RAB33B-GTP. Interacts with GJA1. {ECO:0000250|UniProtKB:Q4ADV7}. +Q8R3Q2 PP6R2_MOUSE Serine/threonine-protein phosphatase 6 regulatory subunit 2 (SAPS domain family member 2) 923 100,460 Chain (1); Compositional bias (1); Frameshift (1); Modified residue (3); Sequence conflict (3) FUNCTION: Regulatory subunit of protein phosphatase 6 (PP6). May function as a scaffolding PP6 subunit. Involved in the PP6-mediated dephosphorylation of NFKBIE opposing its degradation in response to TNF-alpha. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Protein phosphatase 6 (PP6) holoenzyme is proposed to be a heterotrimeric complex formed by the catalytic subunit, a SAPS domain-containing subunit (PP6R) and an ankyrin repeat-domain containing regulatory subunit (ARS). Interacts with PPP6C and NFKBIE. Interacts with ANKRD28 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Strongest expression in bladder and lower levels found in heart and pancreas. Very weak expression observed in all other tissues tested. {ECO:0000269|PubMed:16769727}. +Q922D4 PP6R3_MOUSE Serine/threonine-protein phosphatase 6 regulatory subunit 3 (SAPS domain family member 3) 844 94,653 Alternative sequence (5); Chain (1); Erroneous initiation (1); Modified residue (9) FUNCTION: Regulatory subunit of protein phosphatase 6 (PP6). May function as a scaffolding PP6 subunit. May have an important role in maintaining immune self-tolerance (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}. SUBUNIT: Protein phosphatase 6 (PP6) holoenzyme is proposed to be a heterotrimeric complex formed by the catalytic subunit, a SAPS domain-containing subunit (PP6R) and an ankyrin repeat-domain containing regulatory subunit (ARS). Interacts with PPP6C and ANKRD28 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Strongest expression observed in lung, spleen, bladder and liver and weaker levels present in brain, heart, kidney, skeletal muscle and pancreas. {ECO:0000269|PubMed:16769727}. +P52760 RIDA_MOUSE 2-iminobutanoate/2-iminopropanoate deaminase (EC 3.5.99.10) (Heat-responsive protein 12) (Reactive intermediate imine deaminase A homolog) (Translation inhibitor L-PSP ribonuclease) (EC 3.1.-.-) 135 14,255 Chain (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (5) FUNCTION: Catalyzes the hydrolytic deamination of enamine/imine intermediates that form during the course of normal metabolism. May facilitate the release of ammonia from these potentially toxic reactive metabolites, reducing their impact on cellular components. It may act on enamine/imine intermediates formed by several types of pyridoxal-5'-phosphate-dependent dehydratases including L-threonine dehydratase. {ECO:0000250|UniProtKB:P52758}.; FUNCTION: May also function as an endoribonuclease, cleaving mRNA phosphodiester bonds of single-stranded RNA (By similarity). Thereby, may inhibit protein translation (By similarity). {ECO:0000250|UniProtKB:P52758, ECO:0000250|UniProtKB:P52759}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P52758}. Nucleus {ECO:0000250|UniProtKB:P52758}. Peroxisome {ECO:0000250|UniProtKB:P52759}. Mitochondrion {ECO:0000250|UniProtKB:P52759}. Note=Mostly cytoplasmic but, in less differentiated cells occasionally nuclear. {ECO:0000250|UniProtKB:P52758}. SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:P52758}. TISSUE SPECIFICITY: Expressed predominantly in liver and kidney. Lower levels in lung and brain. {ECO:0000269|PubMed:9141440}. +Q8BP40 PPA6_MOUSE Lysophosphatidic acid phosphatase type 6 (EC 3.1.3.2) (Acid phosphatase 6, lysophosphatidic) (Acid phosphatase-like protein 1) (PACPL1) 418 47,625 Active site (2); Alternative sequence (2); Chain (1); Frameshift (2); Region (1); Sequence conflict (7); Transit peptide (1) FUNCTION: Hydrolyzes lysophosphatidic acid (LPA) containing a medium length fatty acid chain to the corresponding monoacylglycerol. Has highest activity with lysophosphatidic acid containing myristate (C14:0), monounsaturated oleate (C18:1) or palmitate (C16:0), and lower activity with C18:0 and C6:0 lysophosphatidic acid (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. +P24638 PPAL_MOUSE Lysosomal acid phosphatase (LAP) (EC 3.1.3.2) 423 48,509 Active site (2); Chain (1); Disulfide bond (3); Glycosylation (10); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 382 402 Helical. {ECO:0000255}. TOPO_DOM 31 381 Lumenal. {ECO:0000255}.; TOPO_DOM 403 423 Cytoplasmic. {ECO:0000255}. PTM: The membrane-bound form is converted to the soluble form by sequential proteolytic processing. First, the C-terminal cytoplasmic tail is removed. Cleavage by a lysosomal protease releases the soluble form in the lysosome lumen (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:P11117}; Single-pass membrane protein {ECO:0000255}; Lumenal side {ECO:0000250|UniProtKB:P11117}. Lysosome lumen {ECO:0000250|UniProtKB:P11117}. Note=The soluble form arises by proteolytic processing of the membrane-bound form. {ECO:0000250|UniProtKB:P11117}. +Q5ND29 RILP_MOUSE Rab-interacting lysosomal protein 369 41,139 Chain (1); Coiled coil (1); Domain (2); Erroneous initiation (1); Modified residue (3); Region (1) FUNCTION: Rab effector playing a role in late endocytic transport to degradative compartments. Involved in the regulation of lysosomal morphology and distribution. Induces recruitment of dynein-dynactin motor complexes to Rab7A-containing late endosome and lysosome compartments. Promotes centripetal migration of phagosomes and the fusion of phagosomes with the late endosomes and lysosomes. {ECO:0000250|UniProtKB:Q96NA2}. SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250|UniProtKB:Q96NA2}. Lysosome membrane {ECO:0000250|UniProtKB:Q96NA2}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:Q96NA2}. Note=Associated with late endosomal, lysosomal and phagosomal membranes. The interaction with RAB7A is necessary for its recruitment to phagosomes. {ECO:0000250|UniProtKB:Q96NA2}. SUBUNIT: Homodimer. Interacts with RAB7A. Interacts with RAB34 (By similarity). Identified in a complex with MREG and DCTN1; interacts directly with MREG (PubMed:22275436). Interacts with CLN3 (By similarity). {ECO:0000250|UniProtKB:Q96NA2, ECO:0000269|PubMed:22275436}. +Q7TNF8 RIMB1_MOUSE Peripheral-type benzodiazepine receptor-associated protein 1 (PRAX-1) (Peripheral benzodiazepine receptor-interacting protein) (PBR-IP) (RIMS-binding protein 1) (RIM-BP1) (TSPO-associated protein 1) 1846 199,929 Alternative sequence (5); Chain (1); Compositional bias (3); Domain (6); Sequence conflict (1) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Mitochondrion {ECO:0000250}. Note=Preferentially expressed in the mitochondria in the presence of TSPO. {ECO:0000250}. SUBUNIT: Interacts with RIMS1, RIMS2 and TSPO. {ECO:0000250}. DOMAIN: The SH3 and proline-rich domain is required for the interaction with TSPO and the second SH3 domain mediates binding to a proline-rich motif in RIMS1 and RIMS2. {ECO:0000250}. TISSUE SPECIFICITY: Predominantly expressed in the brain. {ECO:0000269|PubMed:9915832}. +Q80U40 RIMB2_MOUSE RIMS-binding protein 2 (RIM-BP2) 1072 118,342 Alternative sequence (1); Chain (1); Domain (6); Modified residue (5); Sequence conflict (4) FUNCTION: Plays a role in the synaptic transmission as bifunctional linker that interacts simultaneously with RIMS1, RIMS2, CACNA1D and CACNA1B. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Cell junction, synapse {ECO:0000250}. Note=Synaptic plasma membrane. {ECO:0000250}. SUBUNIT: Interacts with RIMS1, RIMS2, CACNA1D and CACNA1B, and potentially with other Ca(2+) channel alpha-1 isoforms. {ECO:0000250}. DOMAIN: The SH3 domains mediate binding to a proline-rich motif in RIMS1, RIMS2, CACNA1D and CACNA1B. {ECO:0000250}. +Q6PFX8 RIMKA_MOUSE N-acetylaspartylglutamate synthase A (NAAG synthetase A) (NAAGS) (EC 6.3.2.41) (N-acetylaspartylglutamylglutamate synthase A) (EC 6.3.2.42) (Ribosomal protein S6 modification-like protein A) 380 41,504 Binding site (2); Chain (1); Domain (1); Metal binding (4); Modified residue (1); Nucleotide binding (1); Sequence conflict (1) FUNCTION: Catalyzes the synthesis of N-acetyl-L-aspartyl-L-glutamate (NAAG) and N-acetyl-L-aspartyl-L-glutamyl-L-glutamate. {ECO:0000269|PubMed:20657015, ECO:0000269|PubMed:21454531}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. TISSUE SPECIFICITY: Highly expressed in spinal cord and brain. {ECO:0000269|PubMed:21454531}. +P24823 PPBN_MOUSE Alkaline phosphatase, germ cell type (EC 3.1.3.1) (Alkaline phosphatase 5) (Alkaline phosphatase, placental-like) (Embryonic alkaline phosphatase) (EAP) (Embryonic-type alkaline phosphatase) 529 57,202 Active site (1); Chain (1); Disulfide bond (2); Glycosylation (3); Lipidation (1); Metal binding (10); Propeptide (1); Sequence conflict (3); Signal peptide (1) SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P05187}. TISSUE SPECIFICITY: Embryo and testis. +Q8C167 PPCEL_MOUSE Prolyl endopeptidase-like (EC 3.4.21.-) (Prolylendopeptidase-like) 725 83,194 Active site (3); Alternative sequence (4); Chain (1); Erroneous initiation (1); Modified residue (1) FUNCTION: Probable serine peptidase whose precise substrate specificity remains unclear. Does not cleave peptides after a arginine or lysine residue. May play a role in the regulation of synaptic vesiscle exocytosis. {ECO:0000250|UniProtKB:Q4J6C6}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q4J6C6}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q4J6C6}. +P53808 PPCT_MOUSE Phosphatidylcholine transfer protein (PC-TP) (START domain-containing protein 2) (StARD2) (StAR-related lipid transfer protein 2) 214 24,785 Binding site (3); Chain (1); Domain (1); Modified residue (2); Sequence conflict (2) FUNCTION: Catalyzes the transfer of phosphatidylcholine between membranes. Binds a single lipid molecule. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10500206}. SUBUNIT: Interacts with ACOT13/THEM2. {ECO:0000269|PubMed:17704541}. TISSUE SPECIFICITY: Abundant in liver of pups but levels in liver decrease 10-fold about 2 weeks after birth. In adult, highly expressed in epididymis, testis, kidney and bone-marrow derived mast cells. {ECO:0000269|PubMed:10500206}. +O35655 PPE1_MOUSE Serine/threonine-protein phosphatase with EF-hands 1 (PPEF-1) (EC 3.1.3.16) (DRES10) (Protein phosphatase with EF calcium-binding domain) (PPEF) 650 75,058 Active site (1); Calcium binding (3); Chain (1); Domain (4); Metal binding (7); Region (1) FUNCTION: May have a role in the recovery or adaptation response of photoreceptors. May have a role in diverse sensory neurons and in development. TISSUE SPECIFICITY: In the embryo it is almost exclusively expressed in the peripheral nervous system, within sensory neurons of cranial and dorsal root ganglia. Otherwise found in fetal inner ear and a small group of neurons in the midbrain/pons junction. +Q9CR37 PPDPF_MOUSE Pancreatic progenitor cell differentiation and proliferation factor (Exocrine differentiation and proliferation factor) 115 12,260 Chain (1); Modified residue (1) FUNCTION: Probable regulator of exocrine pancreas development. {ECO:0000250}. +P24369 PPIB_MOUSE Peptidyl-prolyl cis-trans isomerase B (PPIase B) (EC 5.2.1.8) (CYP-S1) (Cyclophilin B) (Rotamase B) (S-cyclophilin) (SCYLP) 216 23,713 Chain (1); Domain (1); Erroneous initiation (2); Modified residue (4); Motif (1); Signal peptide (1) FUNCTION: PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. {ECO:0000250|UniProtKB:P23284}. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:P23284}. Melanosome {ECO:0000250|UniProtKB:P23284}. SUBUNIT: Interacts with DYM. Interacts with CALR, CANX and CLGN (By similarity). {ECO:0000250}. +Q9D868 PPIH_MOUSE Peptidyl-prolyl cis-trans isomerase H (PPIase H) (EC 5.2.1.8) (Rotamase H) 188 20,464 Alternative sequence (1); Chain (1); Domain (1); Initiator methionine (1); Modified residue (1) FUNCTION: PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. Participates in pre-mRNA splicing. May play a role in the assembly of the U4/U5/U6 tri-snRNP complex, one of the building blocks of the spliceosome. May act as a chaperone. {ECO:0000250|UniProtKB:O43447}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Colocalizes with spliceosomal snRNPs. A small proportion may also be cytoplasmic (By similarity). {ECO:0000250}. SUBUNIT: Interacts directly with PRPF4. Part of a heteromeric complex containing PPIH, PRPF3 and PRPF4 that is stable in the absence of RNA. Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39. Heterodimer with PRPF18. Heterodimer with PRPF18 (By similarity). {ECO:0000250}. +Q9D6L8 PPIL3_MOUSE Peptidyl-prolyl cis-trans isomerase-like 3 (PPIase) (EC 5.2.1.8) (CYP10L) (Cyclophilin-like protein PPIL3) (Rotamase PPIL3) 161 18,128 Alternative sequence (1); Chain (1); Domain (1); Initiator methionine (1); Modified residue (2); Sequence conflict (3) FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. May be involved in pre-mRNA splicing (By similarity). {ECO:0000250}. SUBUNIT: Identified in the spliceosome C complex. {ECO:0000250}. +P49443 PPM1A_MOUSE Protein phosphatase 1A (EC 3.1.3.16) (Protein phosphatase 2C isoform alpha) (PP2C-alpha) (Protein phosphatase IA) 382 42,433 Chain (1); Domain (1); Initiator methionine (1); Lipidation (1); Metal binding (5); Modified residue (2) FUNCTION: Enzyme with a broad specificity. Negatively regulates TGF-beta signaling through dephosphorylating SMAD2 and SMAD3, resulting in their dissociation from SMAD4, nuclear export of the SMADs and termination of the TGF-beta-mediated signaling (By similarity). Dephosphorylates PRKAA1 and PRKAA2. Plays an important role in the termination of TNF-alpha-mediated NF-kappa-B activation through dephosphorylating and inactivating IKBKB/IKKB. {ECO:0000250, ECO:0000269|PubMed:23088624}. PTM: N-myristoylation is essential for the recognition of its substrates for dephosphorylation. {ECO:0000269|PubMed:23088624}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P35813}. Cytoplasm, cytosol {ECO:0000269|PubMed:22781750, ECO:0000269|PubMed:23088624}. Membrane {ECO:0000269|PubMed:23088624}; Lipid-anchor {ECO:0000269|PubMed:23088624}. Note=Weakly associates at the membrane and N-myristoylation mediates the membrane localization. {ECO:0000269|PubMed:23088624}. SUBUNIT: Monomer (By similarity). Interacts with SMAD2; the interaction dephosphorylates SMAD2 in its C-terminal SXS motif resulting in disruption of the SMAD2/SMAD4 complex, SMAD2 nuclear export and termination of the TGF-beta-mediated signaling. Interacts with SMAD2; the interaction dephosphorylates SMAD2 in its C-terminal SXS motif resulting in disruption of the SMAD2/SMAD4 complex, SMAD2 nuclear export and termination of the TGF-beta-mediated signaling (By similarity). Interacts with the phosphorylated form of IKBKB/IKKB (By similarity). {ECO:0000250}. +P36993 PPM1B_MOUSE Protein phosphatase 1B (EC 3.1.3.16) (Protein phosphatase 2C isoform beta) (PP2C-beta) 390 42,795 Alternative sequence (3); Chain (1); Cross-link (1); Domain (1); Initiator methionine (1); Lipidation (1); Metal binding (5); Modified residue (1); Sequence caution (1) FUNCTION: Enzyme with a broad specificity. Dephosphorylates PRKAA1 and PRKAA2. Inhibits TBK1-mediated antiviral signaling by dephosphorylating it at 'Ser-172'. Plays an important role in the termination of TNF-alpha-mediated NF-kappa-B activation through dephosphorylating and inactivating IKBKB/IKKB. {ECO:0000269|PubMed:23088624}. PTM: Isgylation negatively regulates its activity. {ECO:0000250}.; PTM: N-myristoylation is essential for the recognition of its substrates for dephosphorylation. {ECO:0000269|PubMed:23088624}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:22781750, ECO:0000269|PubMed:23088624}. Membrane {ECO:0000269|PubMed:23088624}; Lipid-anchor {ECO:0000269|PubMed:23088624}. Note=Weakly associates at the membrane and N-myristoylation mediates the membrane localization. {ECO:0000269|PubMed:23088624}. SUBUNIT: Monomer. Interacts with PAK6 (By similarity). Interacts with the phosphorylated form of IKBKB/IKKB (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Isoform 1: Expressed ubiquitously. Isoform 2: Expressed exclusively in testis and intestine. Isoform 3: Expressed exclusively in brain and intestine. Isoform 4: Expressed exclusively in testis and intestine. +Q9QZ67 PPM1D_MOUSE Protein phosphatase 1D (EC 3.1.3.16) (Protein phosphatase 2C isoform delta) (PP2C-delta) (Protein phosphatase magnesium-dependent 1 delta) (p53-induced protein phosphatase 1) 598 65,723 Chain (1); Domain (1); Metal binding (5); Modified residue (1); Region (1); Sequence conflict (1) FUNCTION: Involved in the negative regulation of p53 expression. Required for the relief of p53-dependent checkpoint mediated cell cycle arrest. Binds to and dephosphorylates 'Ser-15' of TP53 and 'Ser-345' of CHEK1 which contributes to the functional inactivation of these proteins. Mediates MAPK14 dephosphorylation and inactivation (By similarity). Is also an important regulator of global heterochromatin silencing and critical in maintaining genome integrity (PubMed:24135283). {ECO:0000250|UniProtKB:O15297, ECO:0000269|PubMed:24135283}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O15297}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:O15297}. SUBUNIT: Interacts with CHEK1 and CHEK2; dephosphorylates them. Interacts with MAPK14. {ECO:0000250|UniProtKB:O15297}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:10756097}. +Q8CGA0 PPM1F_MOUSE Protein phosphatase 1F (EC 3.1.3.16) (Ca(2+)/calmodulin-dependent protein kinase phosphatase) (CaM-kinase phosphatase) (CaMKPase) 452 49,611 Chain (1); Compositional bias (1); Domain (1); Metal binding (5); Modified residue (1) FUNCTION: Dephosphorylates and concomitantly deactivates CaM-kinase II activated upon autophosphorylation, and CaM-kinases IV and I activated upon phosphorylation by CaM-kinase kinase. Promotes apoptosis (By similarity). {ECO:0000250}. SUBUNIT: Associates with FEM1B. {ECO:0000250}. +Q3UYC0 PPM1H_MOUSE Protein phosphatase 1H (EC 3.1.3.16) 513 56,380 Alternative sequence (2); Chain (1); Domain (1); Erroneous initiation (3); Modified residue (8); Sequence conflict (6) FUNCTION: Dephosphorylates CDKN1B at 'Thr-187', thus removing a signal for proteasomal degradation. {ECO:0000250|UniProtKB:Q9ULR3}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9ULR3}. Cytoplasm {ECO:0000250|UniProtKB:Q9ULR3}. +Q8BXN7 PPM1K_MOUSE Protein phosphatase 1K, mitochondrial (EC 3.1.3.16) (Protein phosphatase 2C isoform kappa) (PP2C-kappa) 372 40,918 Chain (1); Domain (1); Metal binding (3); Modified residue (1); Transit peptide (1) FUNCTION: Regulates the mitochondrial permeability transition pore and is essential for cellular survival and development. {ECO:0000269|PubMed:17374715}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:17374715}. TISSUE SPECIFICITY: Highly expressed in the heart, kidney, brain and liver and to a lesser extent in testis, lung, spleen and adipose tissue. Very low amount in muscle (at protein level). Also expressed in the thymus (at protein level) and the diaphragm. Significantly reduced in hypertrophied hearts. {ECO:0000269|PubMed:17336929, ECO:0000269|PubMed:17374715}. +Q60676 PPP5_MOUSE Serine/threonine-protein phosphatase 5 (PP5) (EC 3.1.3.16) (Protein phosphatase T) (PPT) 499 56,877 Active site (1); Binding site (4); Chain (1); Initiator methionine (1); Metal binding (7); Modified residue (1); Region (3); Repeat (3); Sequence conflict (3) FUNCTION: Serine/threonine-protein phosphatase that dephosphorylates a myriad of proteins involved in different signaling pathways including the kinases CSNK1E, ASK1/MAP3K5, PRKDC and RAF1, the nuclear receptors NR3C1, PPARG, ESR1 and ESR2, SMAD proteins and TAU/MAPT. Implicated in wide ranging cellular processes, including apoptosis, differentiation, DNA damage response, cell survival, regulation of ion channels or circadian rhythms, in response to steroid and thyroid hormones, calcium, fatty acids, TGF-beta as well as oxidative and genotoxic stresses. Participates in the control of DNA damage response mechanisms such as checkpoint activation and DNA damage repair through, for instance, the regulation ATM/ATR-signaling and dephosphorylation of PRKDC and TP53BP1. Inhibits ASK1/MAP3K5-mediated apoptosis induced by oxidative stress. Plays a positive role in adipogenesis, mainly through the dephosphorylation and activation of PPARG transactivation function. Also dephosphorylates and inhibits the anti-adipogenic effect of NR3C1. Regulates the circadian rhythms, through the dephosphorylation and activation of CSNK1E. May modulate TGF-beta signaling pathway by the regulation of SMAD3 phosphorylation and protein expression levels. Dephosphorylates and may play a role in the regulation of TAU/MAPT. Through their dephosphorylation, may play a role in the regulation of ions channels such as KCNH2. {ECO:0000269|PubMed:17376776, ECO:0000269|PubMed:21994940, ECO:0000269|PubMed:22526606}. PTM: Activated by at least two different proteolytic cleavages producing a 56 kDa and a 50 kDa form. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21994940}. Cytoplasm {ECO:0000269|PubMed:21994940}. Cell membrane {ECO:0000250|UniProtKB:P53041}. Note=Predominantly nuclear. But also present in the cytoplasm. Translocates from the cytoplasm to the plasma membrane in a RAC1-dependent manner. {ECO:0000250|UniProtKB:P53041}. SUBUNIT: Probably forms a complex composed of chaperones HSP90 and HSP70, co-chaperones STIP1/HOP, CDC37, PPP5C, PTGES3/p23, TSC1 and client protein TSC2 (By similarity). Probably forms a complex composed of chaperones HSP90 and HSP70, co-chaperones CDC37, PPP5C, TSC1 and client protein TSC2, CDK4, AKT, RAF1 and NR3C1; this complex does not contain co-chaperones STIP1/HOP and PTGES3/p23 (By similarity). Part of a complex with HSP90/HSP90AA1 and steroid receptors (PubMed:9195923). Interacts (via TPR repeats) with HSP90AA1 (via TPR repeat-binding motif) or HSPA1A/HSPA1B; the interaction is direct and activates the phosphatase activity (By similarity). Dissociates from HSPA1A/HSPA1B and HSP90AA1 in response to arachidonic acid (By similarity). Interacts with CPNE1 (via VWFA domain) (PubMed:12522145). Interacts with CDC16, CDC27 (By similarity). Interacts with KLHDC10 (via the 6 Kelch repeats); inhibits the phosphatase activity on MAP3K5 (By similarity). Interacts with ATM and ATR; both interactions are induced by DNA damage and enhance ATM and ATR kinase activity (By similarity). Interacts with RAD17; reduced by DNA damage (By similarity). Interacts with nuclear receptors such as NR3C1/GCR and PPARG (activated by agonist); regulates their transactivation activities (PubMed:9195923, PubMed:21994940). Interacts (via TPR repeats) with S100 proteins S100A1, S100A2, S100A6, S100B and S100P; the interactions are calcium-dependent, strongly activate PPP5C phosphatase activity and compete with HSP90AA1 and MAP3K5 interactions (By similarity). Interacts with SMAD2 and SMAD3 but not with SMAD1; decreases SMAD3 phosphorylation and protein levels (By similarity). Interacts (via TPR repeats) with CRY1 and CRY2; the interaction with CRY2 downregulates the phosphatase activity on CSNK1E (By similarity). Interacts (via TPR repeats) with the active form of RAC1, GNA12 or GNA13; these interactions activate the phosphatase activity and translocate PPP5C to the cell membrane (By similarity). Interacts with FLCN (By similarity). {ECO:0000250|UniProtKB:P53041, ECO:0000269|PubMed:12522145, ECO:0000269|PubMed:21994940, ECO:0000269|PubMed:9195923}. TISSUE SPECIFICITY: Expressed in liver (at protein level) and brain, enriched in suprachiasmatic nuclei. {ECO:0000269|PubMed:16790549}. +Q9ERT9 PPR1A_MOUSE Protein phosphatase 1 regulatory subunit 1A (Protein phosphatase inhibitor 1) (I-1) (IPP-1) 171 18,718 Chain (1); Modified residue (6); Region (3) FUNCTION: Inhibitor of protein-phosphatase 1. This protein may be important in hormonal control of glycogen metabolism. Hormones that elevate intracellular cAMP increase I-1 activity in many tissues. I-1 activation may impose cAMP control over proteins that are not directly phosphorylated by PKA. Following a rise in intracellular calcium, I-1 is inactivated by calcineurin (or PP2B). Does not inhibit type-2 phosphatases. PTM: Phosphorylation of Thr-35 is required for activity. {ECO:0000250}. SUBUNIT: Interacts with PPP1R15A. {ECO:0000250}. +Q148A4 PPR32_MOUSE Protein phosphatase 1 regulatory subunit 32 (Protein IIIG9) 427 47,809 Chain (1); Sequence conflict (1) SUBUNIT: Interacts with PPP1CA. {ECO:0000250}. +Q8BRJ4 PPR3E_MOUSE Protein phosphatase 1 regulatory subunit 3E 279 30,575 Chain (1); Domain (1); Erroneous translation (1); Modified residue (3); Motif (1); Region (2); Sequence conflict (1) FUNCTION: Acts as a glycogen-targeting subunit for PP1. PP1 is involved in glycogen metabolism and contributes to the activation of glycogen synthase leading to an increase in glycogen synthesis. {ECO:0000269|PubMed:15752363}. DOMAIN: The CBM21 domain is known to be involved in the localization to glycogen and is characteristic of some regulatory subunit of phosphatase complexes. +Q6NZN1 PPRC1_MOUSE Peroxisome proliferator-activated receptor gamma coactivator-related protein 1 (PGC-1-related coactivator) (PRC) 1644 175,074 Alternative sequence (6); Chain (1); Compositional bias (3); Domain (1); Erroneous initiation (1); Modified residue (5); Region (2); Sequence conflict (10) FUNCTION: Acts as a coactivator during transcriptional activation of nuclear genes related to mitochondrial biogenesis and cell growth. Involved in the transcription coactivation of CREB and NRF1 target genes (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11340167}. Note=Colocalizes with NRF1. SUBUNIT: Interacts with CREB1 and NRF1. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in liver, heart, skeletal muscle, kidney and white and brown adipose tissues. {ECO:0000269|PubMed:11340167}. +Q8C6U2 PQLC3_MOUSE PQ-loop repeat-containing protein 3 202 22,739 Chain (1); Sequence conflict (1); Signal peptide (1); Transmembrane (4) TRANSMEM 33 53 Helical. {ECO:0000255}.; TRANSMEM 64 84 Helical. {ECO:0000255}.; TRANSMEM 94 114 Helical. {ECO:0000255}.; TRANSMEM 171 191 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q91VU7 PUS7_MOUSE Pseudouridylate synthase 7 homolog (EC 5.4.99.-) 660 74,793 Active site (1); Alternative sequence (1); Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (2); Modified residue (2) FUNCTION: Pseudouridylate synthase that catalyzes pseudouridylation of RNAs. Acts as a regulator of protein synthesis in embryonic stem cells by mediating pseudouridylation of RNA fragments derived from tRNAs (tRFs): pseudouridylated tRFs inhibit translation by targeting the translation initiation complex. Also catalyzes pseudouridylation of mRNAs: mediates pseudouridylation of mRNAs with the consensus sequence 5'-UGUAG-3'. In addition to mRNAs and tRNAs, binds other types of RNAs, such as snRNAs, Y RNAs and vault RNAs, suggesting that it can catalyze pseudouridylation of many RNA types. {ECO:0000250|UniProtKB:Q96PZ0}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96PZ0}. +Q9ET01 PYGL_MOUSE Glycogen phosphorylase, liver form (EC 2.4.1.1) 850 97,463 Binding site (1); Chain (1); Initiator methionine (1); Modified residue (8); Sequence conflict (1); Site (3) FUNCTION: Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties (By similarity). {ECO:0000250}. PTM: Phosphorylation of Ser-15 converts phosphorylase B (unphosphorylated) to phosphorylase A. {ECO:0000250}. SUBUNIT: Homodimer. Dimers associate into a tetramer to form the enzymatically active phosphorylase A. Interacts with PPP1R3B (By similarity). {ECO:0000250}. +Q9WUB3 PYGM_MOUSE Glycogen phosphorylase, muscle form (EC 2.4.1.1) (Myophosphorylase) 842 97,286 Binding site (1); Chain (1); Initiator methionine (1); Modified residue (10); Site (3) FUNCTION: Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties. PTM: Phosphorylation of Ser-15 converts phosphorylase B (unphosphorylated) to phosphorylase A. {ECO:0000250}. SUBUNIT: Homodimer. Dimers associate into a tetramer to form the enzymatically active phosphorylase A (By similarity). {ECO:0000250}. +Q3V3Q4 PYDC3_MOUSE Pyrin domain-containing protein 3 (Interferon-activable protein 204-like) (Ifi-204-like) 588 63,866 Chain (1); Domain (1) +Q8BH73 QPCTL_MOUSE Glutaminyl-peptide cyclotransferase-like protein (EC 2.3.2.5) (Golgi-resident glutaminyl-peptide cyclotransferase) (isoQC) (gQC) 383 42,692 Active site (2); Alternative sequence (1); Chain (1); Compositional bias (1); Metal binding (3); Sequence conflict (2); Transmembrane (1) TRANSMEM 33 53 Helical. {ECO:0000255}. FUNCTION: Responsible for the biosynthesis of pyroglutamyl peptides. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Detected in thalamus, hippocampus, brain cortex, cerebellum, kidney, lung and liver, and at low levels in heart and spleen. {ECO:0000269|PubMed:18486145}. +Q9CYK2 QPCT_MOUSE Glutaminyl-peptide cyclotransferase (EC 2.3.2.5) (Glutaminyl cyclase) (QC) (Glutaminyl-tRNA cyclotransferase) 362 41,119 Active site (2); Alternative sequence (1); Beta strand (14); Chain (1); Disulfide bond (1); Glycosylation (2); Helix (16); Metal binding (3); Sequence conflict (7); Signal peptide (1); Turn (3) FUNCTION: Responsible for the biosynthesis of pyroglutamyl peptides. Has a bias against acidic and tryptophan residues adjacent to the N-terminal glutaminyl residue and a lack of importance of chain length after the second residue (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +Q3UA37 QRIC1_MOUSE Glutamine-rich protein 1 777 86,556 Chain (1); Compositional bias (1); Cross-link (2); Domain (1); Modified residue (3) +Q6ZWV7 RL35_MOUSE 60S ribosomal protein L35 123 14,553 Chain (1); Cross-link (1); Modified residue (3) FUNCTION: Component of the large ribosomal subunit. {ECO:0000250|UniProtKB:P42766}. SUBUNIT: Component of the large ribosomal subunit. {ECO:0000250|UniProtKB:P42766}. +D3Z423 R212B_MOUSE RING finger protein 212B 297 32,990 Chain (1); Coiled coil (1); Zinc finger (1) +Q148R9 R9BP_MOUSE Regulator of G-protein signaling 9-binding protein (RGS9-anchoring protein) 237 25,177 Chain (1); Coiled coil (1); Region (1); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 213 233 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 1 212 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 234 237 Extracellular. {ECO:0000255}. FUNCTION: Regulator of G protein-coupled receptor (GPCR) signaling in phototransduction. Participates in the recovery phase of visual transduction via its interaction with RGS9-1 isoform. Acts as a membrane-anchor that mediates the targeting of RGS9-1 to the photoreceptor outer segment, where phototransduction takes place. Enhances the ability of RGS9-1 to stimulate G protein GTPase activity, allowing the visual signal to be terminated on the physiologically time scale. It also controls the proteolytic stability of RGS9-1, probably by protecting it from degradation. {ECO:0000269|PubMed:12560335, ECO:0000269|PubMed:14625292, ECO:0000269|PubMed:16908407, ECO:0000269|PubMed:16939221}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12119397}; Single-pass type IV membrane protein {ECO:0000269|PubMed:12119397}. SUBUNIT: Specifically interacts with isoform RGS9-1 of RGS9. Interaction is decreased when RGS9-1 is phosphorylated at 'Ser-475'. Component of the RGS9-1-Gbeta5 complex composed of RGS9-1, Gbeta5 (GNB5) and RGS9BP. {ECO:0000269|PubMed:12119397, ECO:0000269|PubMed:12499365, ECO:0000269|PubMed:14614075, ECO:0000269|PubMed:16908407}. TISSUE SPECIFICITY: Predominantly expressed in photoreceptors of the retina. Weakly expressed in other areas of the central nervous system. {ECO:0000269|PubMed:12119397, ECO:0000269|PubMed:14664818}. +P35282 RAB21_MOUSE Ras-related protein Rab-21 (Rab-12) 222 24,106 Chain (1); Initiator methionine (1); Lipidation (2); Modified residue (2); Motif (1); Mutagenesis (2); Nucleotide binding (4); Propeptide (1) FUNCTION: Regulates integrin internalization and recycling, but does not influence the traffic of endosomally translocated receptors in general (PubMed:16754960). As a result, may regulate cell adhesion and migration (PubMed:16754960). During the mitosis of adherent cells, controls the endosomal trafficking of integrins which is required for the successful completion of cytokinesis (PubMed:18804435). Involved in neurite growth (By similarity). Following SBF2/MTMT13-mediated activation in response to starvation-induced autophagy, binds to and regulates SNARE protein VAMP8 endolysosomal transport required for SNARE-mediated autophagosome-lysosome fusion (By similarity). {ECO:0000250|UniProtKB:Q6AXT5, ECO:0000250|UniProtKB:Q9UL25, ECO:0000269|PubMed:16754960, ECO:0000269|PubMed:18804435}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16754960}; Lipid-anchor {ECO:0000305}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:19745841}. Golgi apparatus membrane {ECO:0000269|PubMed:16754960}. Early endosome membrane {ECO:0000269|PubMed:16754960}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:16754960}. Cleavage furrow {ECO:0000269|PubMed:18804435}. Note=Colocalizes with ANKRD27 and VAMP7 in neurites (PubMed:19745841). During mitosis, in mid-telophase, localized in the ingressing cleavage furrow (PubMed:18804435). In late telophase, detected at the opposite poles of the daughter cells, in vesicles at the base of lamellipodia formed by the separating daughter cells (PubMed:18804435). {ECO:0000269|PubMed:18804435, ECO:0000269|PubMed:19745841}. SUBUNIT: Interacts with the cytoplasmic tail of integrins ITGA1, ITGA2, ITGA5, ITGA6, ITGA11 and ITGB1; this interaction is dependent upon its GDP/GTP cycle (PubMed:16754960). Interacts with RABGEF1 (via VPS9 domain) (By similarity). Interacts with ANKRD27 (By similarity). Interacts with VAMP7 (By similarity). Interacts (in GTP-bound form) with VAMP8 in response to starvation; the interaction probably regulates VAMP8 endolysosomal trafficking (By similarity). {ECO:0000250|UniProtKB:Q9UL25, ECO:0000269|PubMed:16754960}. +P35290 RAB24_MOUSE Ras-related protein Rab-24 (Rab-16) 203 23,144 Chain (1); Lipidation (2); Motif (1); Mutagenesis (4); Nucleotide binding (4); Sequence conflict (1) FUNCTION: May be involved in autophagy-related processes. PTM: Isoprenylation is inefficient compared to other Rab family members. {ECO:0000269|PubMed:10660536}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10660536, ECO:0000269|PubMed:12323076}. Membrane {ECO:0000269|PubMed:10660536, ECO:0000269|PubMed:12323076}; Lipid-anchor {ECO:0000305}. Note=Only about 20% is recovered in the particulate fraction. {ECO:0000269|PubMed:10660536}. SUBUNIT: Unlike other Rab family members, does not interact with GDP dissociation inhibitors (GDIs), including ARHGDIA and ARHGDIB. TISSUE SPECIFICITY: Widely expressed, with highest expression in brain. {ECO:0000269|PubMed:8126105}. +P53994 RAB2A_MOUSE Ras-related protein Rab-2A 212 23,548 Chain (1); Initiator methionine (1); Lipidation (2); Modified residue (1); Motif (1); Nucleotide binding (4); Region (1) FUNCTION: Required for protein transport from the endoplasmic reticulum to the Golgi complex. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate compartment membrane; Lipid-anchor. Melanosome {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Golgi apparatus membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. SUBUNIT: Interacts with PRKCI. {ECO:0000250}. +P59279 RAB2B_MOUSE Ras-related protein Rab-2B 216 24,198 Chain (1); Lipidation (2); Motif (1); Nucleotide binding (4) FUNCTION: Required for protein transport from the endoplasmic reticulum to the Golgi complex. {ECO:0000305}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000305}. Golgi apparatus membrane {ECO:0000305}. +Q921E2 RAB31_MOUSE Ras-related protein Rab-31 194 21,331 Chain (1); Erroneous initiation (1); Lipidation (2); Modified residue (1); Motif (1); Nucleotide binding (3); Sequence conflict (1) FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. Required for the integrity and for normal function of the Golgi apparatus and the trans-Golgi network. Plays a role in insulin-stimulated translocation of GLUT4 to the cell membrane. Plays a role in the maturation of phagosomes that engulf pathogens, such as S.aureus and Mycobacterium (By similarity). Plays a role in M6PR transport from the trans-Golgi network to endosomes. Plays a role in the internalization of EGFR from the cell membrane into endosomes. {ECO:0000250, ECO:0000269|PubMed:19345684, ECO:0000269|PubMed:22460790}. SUBCELLULAR LOCATION: Early endosome {ECO:0000250|UniProtKB:Q13636}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q13636}. Golgi apparatus, trans-Golgi network membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle, phagosome {ECO:0000250|UniProtKB:Q13636}. Cytoplasmic vesicle, phagosome membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Rapidly recruited to phagosomes containing S.aureus or M.tuberculosis. {ECO:0000250|UniProtKB:Q13636}. SUBUNIT: Interacts with OCRL. Interacts (in GDP-bound form) with RIN3 and GAPVD1, which function as guanine exchange factors (GEF). Interacts with EGFR (By similarity). Interacts with NGFR. Interacts (in GTP-bound form) with EEA1. {ECO:0000250, ECO:0000269|PubMed:22460790}. TISSUE SPECIFICITY: Detected in brain astrocytes (at protein level). {ECO:0000269|PubMed:19725050}. +Q9CZE3 RAB32_MOUSE Ras-related protein Rab-32 223 25,068 Chain (1); Initiator methionine (1); Lipidation (2); Modified residue (2); Motif (1); Mutagenesis (2); Nucleotide binding (3); Region (1); Sequence conflict (3) FUNCTION: Acts as an A-kinase anchoring protein by binding to the type II regulatory subunit of protein kinase A and anchoring it to the mitochondrion. Also involved in synchronization of mitochondrial fission. Plays a role in the maturation of phagosomes that engulf pathogens, such as S.aureus and Mycobacterium (By similarity). Plays an important role in the control of melanin production and melanosome biogenesis (By similarity). In concert with RAB38, regulates the proper trafficking of melanogenic enzymes TYR, TYRP1 and DCT/TYRP2 to melanosomes in melanocytes (PubMed:26620560). {ECO:0000250|UniProtKB:Q13637, ECO:0000269|PubMed:26620560}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q13637}. Mitochondrion outer membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Cytoplasmic vesicle, phagosome {ECO:0000250|UniProtKB:Q13637}. Cytoplasmic vesicle, phagosome membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Melanosome {ECO:0000269|PubMed:26620560}. Melanosome membrane {ECO:0000250|UniProtKB:Q13637}. Note=Recruited to phagosomes containing S.aureus or M.tuberculosis. The BLOC-3 complex, a heterodimer of HPS1 and HPS4 promotes its membrane localization. {ECO:0000250|UniProtKB:Q13637}. SUBUNIT: Interacts with ANKRD27 (PubMed:19403694, PubMed:21187289). A decreased interaction with ANKRD27 seen in the presence of SGSM2 (By similarity). {ECO:0000250|UniProtKB:Q13637, ECO:0000269|PubMed:19403694, ECO:0000269|PubMed:21187289}. TISSUE SPECIFICITY: Widely expressed with highest levels in liver. Strong expression also found in melanocyte, platelet, mast cell and fibroblast cell lines. {ECO:0000269|PubMed:14499590}. +Q9D823 RL37_MOUSE 60S ribosomal protein L37 97 11,078 Chain (1); Metal binding (4); Modified residue (3); Sequence conflict (1); Zinc finger (1) FUNCTION: Binds to the 23S rRNA. {ECO:0000250}. +P35278 RAB5C_MOUSE Ras-related protein Rab-5C 216 23,413 Beta strand (6); Chain (1); Helix (7); Lipidation (2); Motif (1); Nucleotide binding (5); Turn (1) FUNCTION: Protein transport. Probably involved in vesicular traffic (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Early endosome membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Melanosome {ECO:0000250}. SUBUNIT: Interacts with EEA1 and INCA1. {ECO:0000250|UniProtKB:P51148}. +Q0PD08 RAB42_MOUSE Ras-related protein Rab-42 215 23,568 Chain (1); Lipidation (2); Nucleotide binding (5) SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P62820}; Lipid-anchor {ECO:0000250|UniProtKB:P62820}. +Q8CB87 RAB44_MOUSE Ras-related protein Rab-44 973 106,328 Chain (1); Coiled coil (1); Domain (1); Erroneous initiation (2); Lipidation (2); Nucleotide binding (3) SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. +P55258 RAB8A_MOUSE Ras-related protein Rab-8A (Oncogene c-mel) 207 23,668 Beta strand (6); Chain (1); Helix (4); Lipidation (1); Modified residue (3); Motif (1); Nucleotide binding (6); Propeptide (1); Sequence conflict (1); Turn (1) FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab is involved in polarized vesicular trafficking and neurotransmitter release. Together with RAB11A, RAB3IP, the exocyst complex, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis. Together with MYO5B and RAB11A participates in epithelial cell polarization. Plays an important role in ciliogenesis (By similarity). Together with MICALL2, may also regulate adherens junction assembly (PubMed:18094055). May play a role in insulin-induced transport to the plasma membrane of the glucose transporter GLUT4 and therefore play a role in glucose homeostasis (By similarity). Involved in autophagy (By similarity). {ECO:0000250|UniProtKB:P35280, ECO:0000250|UniProtKB:P61006, ECO:0000269|PubMed:18094055}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18094055}; Lipid-anchor {ECO:0000269|PubMed:18094055}; Cytoplasmic side {ECO:0000269|PubMed:18094055}. Golgi apparatus {ECO:0000250|UniProtKB:P61006}. Recycling endosome membrane {ECO:0000269|PubMed:18094055}. Cell projection, cilium {ECO:0000250|UniProtKB:P61006}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:P61006}; Lipid-anchor {ECO:0000250|UniProtKB:P61006}; Cytoplasmic side {ECO:0000250|UniProtKB:P61006}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:23807208}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:19625297, ECO:0000269|PubMed:23807208}. Midbody {ECO:0000250|UniProtKB:P61006}. Note=Colocalizes with OPTN at the Golgi complex and in vesicular structures close to the plasma membrane. In the GDP-bound form, present in the perinuclear region. Shows a polarized distribution to distal regions of cell protrusions in the GTP-bound form. Colocalizes with PARD3, PRKCI, EXOC5, OCLN, PODXL and RAB11A in apical membrane initiation sites (AMIS) during the generation of apical surface and lumenogenesis. Localizes to tubular recycling endosome. Recruited to phagosomes containing S.aureus or Mycobacterium. {ECO:0000250|UniProtKB:P61006}. SUBUNIT: Interacts (GTP-bound form) with MICALL1; regulates RAB8A association with recycling endosomes. Interacts with MICALL2; competes with RAB13 and is involved in E-cadherin endocytic recycling. Interacts (GTP-bound form) with MICAL1, MICALCL, MICAL3 and EHBP1L1; two molecules of RAB8A can bind to one molecule of the effector protein; ternary complexes of RAB8A, RAB13 and either MICAL1 or EHBP1L1 are possible. Interacts (GTP-bound form) with EHBP1. Interacts with EHD1. Interacts with MAP4K2 and SYTL4. Interacts with SGSM1 and SGSM3. Interacts with RABIF, RIMS2, RPH3A and RPH3A. Interacts with OPTN. Interacts with RAB3IP. Interacts with MYO5B. Interacts with PIFO. Interacts with BIRC6/bruce. Interacts with OCRL. Interacts with AHI1 (PubMed:19625297). Interacts with DCDC1 (By similarity). {ECO:0000250|UniProtKB:P61006, ECO:0000269|PubMed:12578829, ECO:0000269|PubMed:12590134, ECO:0000269|PubMed:16541104, ECO:0000269|PubMed:17509819, ECO:0000269|PubMed:18094055, ECO:0000269|PubMed:19625297, ECO:0000269|PubMed:20643351, ECO:0000269|PubMed:8643544}. +Q9JJI8 RL38_MOUSE 60S ribosomal protein L38 70 8,204 Chain (1); Cross-link (2); Modified residue (2) +Q9R0M6 RAB9A_MOUSE Ras-related protein Rab-9A (Sid 99) 201 22,910 Beta strand (5); Binding site (2); Chain (1); Helix (9); Initiator methionine (1); Lipidation (2); Modified residue (4); Motif (1); Nucleotide binding (3); Turn (2) FUNCTION: Involved in the transport of proteins between the endosomes and the trans-Golgi network (By similarity). Involved in the recruitment of SGSM2 to melanosomes and is required for the proper trafficking of melanogenic enzymes TYR, TYRP1 and DCT/TYRP2 to melanosomes in melanocytes (PubMed:26620560). {ECO:0000250|UniProtKB:P24408, ECO:0000269|PubMed:26620560}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P51151}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P51151}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P51151}. Late endosome {ECO:0000250|UniProtKB:P51151}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:P51151}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle, phagosome {ECO:0000250|UniProtKB:P51151}. Cytoplasmic vesicle membrane. Melanosome {ECO:0000269|PubMed:26620560}. Note=Colocalizes with OSBPL1A at the late endosome. Recruited to phagosomes containing S.aureus or M.tuberculosis. {ECO:0000250|UniProtKB:P51151}. SUBUNIT: Interacts (preferentially in its GTP-bound form) with GCC2 (via its GRIP domain) (By similarity). Interacts (GTP-bound form) with SGSM1; the GDP-bound form has much lower affinity for SGSM1 (PubMed:25220469). Interacts with SGSM2 (PubMed:26620560). The GTP-bound form but not the GDP-bound form interacts with HPS4 (PubMed:26620560, PubMed:20048159). The GTP-bound form but not the GDP-bound form interacts with BLOC-3 complex (heterodimer of HPS1 and HPS4) but does not interact with HPS1 alone (By similarity). {ECO:0000250|UniProtKB:P51151, ECO:0000269|PubMed:20048159, ECO:0000269|PubMed:25220469, ECO:0000269|PubMed:26620560}. +Q8BHH2 RAB9B_MOUSE Ras-related protein Rab-9B 201 22,704 Binding site (1); Chain (1); Lipidation (2); Modified residue (1); Motif (1); Nucleotide binding (5) FUNCTION: Involved in the transport of proteins between the endosomes and the trans Golgi network. {ECO:0000250|UniProtKB:P24408}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Recruited to phagosomes containing S.aureus or Mycobacterium. {ECO:0000250}. SUBUNIT: Interacts (GTP-bound form) with SGSM1; the GDP-bound form has much lower affinity for SGSM1 (PubMed:25220469). The GTP-bound form but not the GDP-bound form interacts with HPS4 and the BLOC-3 complex (heterodimer of HPS1 and HPS4) but does not interact with HPS1 alone (By similarity). {ECO:0000250|UniProtKB:Q9NP90, ECO:0000305|PubMed:25220469}. +Q91YQ1 RAB7L_MOUSE Ras-related protein Rab-7L1 (Rab-7-like protein 1) 204 23,089 Chain (1); Lipidation (2); Motif (1); Nucleotide binding (5) FUNCTION: Rab GTPase key regulator in vesicle trafficking. Essential for maintaining the integrity of endosome-trans-Golgi network structure. Together with LRRK2, plays a role in the retrograde trafficking pathway for recycling proteins, such as mannose 6 phosphate receptor (M6PR), between lysosomes and the Golgi apparatus in a retromer-dependent manner. Regulates also neuronal process morphology in the intact central nervous system (CNS) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q5R7A4}; Lipid-anchor {ECO:0000250|UniProtKB:Q5R7A4}; Cytoplasmic side {ECO:0000250|UniProtKB:Q5R7A4}. Cytoplasm {ECO:0000250|UniProtKB:O14966}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O14966}. Golgi apparatus {ECO:0000250|UniProtKB:O14966}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:O14966}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O14966}. Note=Colocalizes with GM130 at the Golgi apparatus (By similarity). Colocalizes with LRRK2 at dynamic tubules emerging from and retracting to the Golgi apparatus (By similarity). Colocalizes with TGN46 at the trans-Golgi network (TGN) (By similarity). {ECO:0000250|UniProtKB:O14966, ECO:0000250|UniProtKB:Q63481}. SUBUNIT: Interacts with LRRK2. {ECO:0000269|PubMed:23395371}. +Q05144 RAC2_MOUSE Ras-related C3 botulinum toxin substrate 2 (Protein EN-7) (p21-Rac2) 192 21,441 Chain (1); Lipidation (1); Modified residue (2); Motif (1); Nucleotide binding (3); Propeptide (1); Sequence conflict (1) FUNCTION: Plasma membrane-associated small GTPase which cycles between an active GTP-bound and inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses, such as secretory processes, phagocytose of apoptotic cells and epithelial cell polarization. Augments the production of reactive oxygen species (ROS) by NADPH oxidase. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Note=Membrane-associated when activated. {ECO:0000250}. SUBUNIT: Interacts with DOCK2, which may activate it. Interacts with S100A8 and calprotectin (S100A8/9) (By similarity). Found in a complex with SH3RF1, MAP3K7/TAK1, MAP2K7/MKK7, MAPK8IP1/JIP1, MAPK8/JNK1 and MAPK9/JNK2 (PubMed:27084103). {ECO:0000250|UniProtKB:P15153, ECO:0000269|PubMed:27084103}. +Q8BGE9 RL3R1_MOUSE Relaxin-3 receptor 1 (RLN3 receptor 1) (G protein-coupled receptor SALPR homolog) (Relaxin family peptide receptor 3) 472 51,573 Chain (1); Compositional bias (2); Disulfide bond (1); Glycosylation (2); Topological domain (8); Transmembrane (7) TRANSMEM 82 102 Helical; Name=1. {ECO:0000255}.; TRANSMEM 120 140 Helical; Name=2. {ECO:0000255}.; TRANSMEM 157 177 Helical; Name=3. {ECO:0000255}.; TRANSMEM 216 236 Helical; Name=4. {ECO:0000255}.; TRANSMEM 271 291 Helical; Name=5. {ECO:0000255}.; TRANSMEM 299 319 Helical; Name=6. {ECO:0000255}.; TRANSMEM 333 353 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 81 Extracellular. {ECO:0000255}.; TOPO_DOM 103 119 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 141 156 Extracellular. {ECO:0000255}.; TOPO_DOM 178 215 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 237 270 Extracellular. {ECO:0000255}.; TOPO_DOM 292 298 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 320 332 Extracellular. {ECO:0000255}.; TOPO_DOM 354 472 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for RNL3/relaxin-3. Binding of the ligand inhibit cAMP accumulation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q6NXW6 RAD17_MOUSE Cell cycle checkpoint protein RAD17 688 77,391 Chain (1); Compositional bias (1); Modified residue (5); Nucleotide binding (1); Region (1); Sequence conflict (7) FUNCTION: Essential for sustained cell growth, maintenance of chromosomal stability, and ATR-dependent checkpoint activation upon DNA damage. Has a weak ATPase activity required for binding to chromatin. Participates in the recruitment of the RAD1-RAD9-HUS1 complex and RHNO1 onto chromatin, and in CHEK1 activation. May also serve as a sensor of DNA replication progression, and may be involved in homologous recombination (By similarity). Essential for embryonic development. May be involved in homologous recombination. {ECO:0000250, ECO:0000269|PubMed:15297881}. PTM: Phosphorylated. Phosphorylation on Ser-647 and Ser-657 is cell cycle-regulated, enhanced by genotoxic stress, and required for activation of checkpoint signaling. {ECO:0000269|PubMed:11687627, ECO:0000269|PubMed:14500819, ECO:0000269|PubMed:17376776}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Phosphorylated form redistributes to discrete nuclear foci upon DNA damage. {ECO:0000250}. SUBUNIT: Part of a DNA-binding complex containing RFC2, RFC3, RFC4 and RFC5. Interacts with RAD1 and RAD9 within the RAD1-RAD9-HUS1 complex. Interacts with RAD9B, POLE, SNU13 and MCM7. DNA damage promotes interaction with ATR or ATM and disrupts interaction with the RAD1-RAD9-HUS1 complex (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous at low levels. Highly expressed in testis, where it is expressed in spermatogonia, spermatocytes and spermatids, but absent in mature spermatozoa (at protein level). {ECO:0000269|PubMed:10232579, ECO:0000269|PubMed:10480350, ECO:0000269|PubMed:9933569}. +O08603 RAE1B_MOUSE Retinoic acid early-inducible protein 1-beta (RAE-1-beta) 253 28,625 Beta strand (8); Chain (1); Disulfide bond (2); Glycosylation (5); Helix (3); Lipidation (1); Propeptide (1); Signal peptide (1); Turn (2) FUNCTION: Acts as a ligand for KLRK1. {ECO:0000269|PubMed:10894171, ECO:0000269|PubMed:11248803, ECO:0000269|PubMed:11557981}. PTM: Glycosylated. {ECO:0000269|PubMed:8982867}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10894171, ECO:0000269|PubMed:8982867}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:10894171, ECO:0000269|PubMed:8982867}. TISSUE SPECIFICITY: Expressed predominantly in embryonic brain. {ECO:0000269|PubMed:8982867}. +O08604 RAE1C_MOUSE Retinoic acid early-inducible protein 1-gamma (RAE-1-gamma) 253 28,508 Beta strand (7); Chain (1); Disulfide bond (2); Glycosylation (5); Helix (5); Lipidation (1); Propeptide (1); Signal peptide (1); Turn (3) FUNCTION: Acts as a ligand for KLRK1. {ECO:0000269|PubMed:10894171}. PTM: Glycosylated. {ECO:0000269|PubMed:8982867}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10894171, ECO:0000269|PubMed:8982867}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:10894171, ECO:0000269|PubMed:8982867}. TISSUE SPECIFICITY: Expressed predominantly in embryonic brain. {ECO:0000269|PubMed:8982867}. +Q9CZQ6 RAE1E_MOUSE Retinoic acid early-inducible protein 1-epsilon (RAE-1-epsilon) 251 28,284 Chain (1); Disulfide bond (2); Glycosylation (5); Lipidation (1); Propeptide (1); Signal peptide (1) FUNCTION: Acts as a ligand for KLRK1. {ECO:0000269|PubMed:11567106, ECO:0000269|PubMed:16086018}. PTM: Glycosylated. {ECO:0000250|UniProtKB:O08603}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. +O88667 RAD_MOUSE GTP-binding protein RAD 308 33,279 Chain (1); Modified residue (2); Mutagenesis (1); Nucleotide binding (2); Region (1) FUNCTION: May play an important role in cardiac antiarrhythmia via the strong suppression of voltage-gated L-type Ca(2+) currents. Regulates voltage-dependent L-type calcium channel subunit alpha-1C trafficking to the cell membrane. Inhibits cardiac hypertrophy through the calmodulin-dependent kinase II (CaMKII) pathway. Inhibits phosphorylation and activation of CAMK2D. {ECO:0000269|PubMed:17525370, ECO:0000269|PubMed:18056528}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17525370}. SUBUNIT: Interacts with Calmodulin preferentially in the inactive, GDP-bound form. Interacts with CAMK2D (By similarity). Interacts with CACNB2. Interaction with CACNB2 regulates the trafficking of CACNA1C to the cell membrane. {ECO:0000250, ECO:0000269|PubMed:17525370}. +P15919 RAG1_MOUSE V(D)J recombination-activating protein 1 (RAG-1) [Includes: Endonuclease RAG1 (EC 3.1.-.-); E3 ubiquitin-protein ligase RAG1 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase RAG1)] 1040 119,185 Beta strand (19); Chain (1); Cross-link (1); DNA binding (1); Helix (38); Metal binding (19); Mutagenesis (42); Sequence conflict (1); Site (1); Turn (5); Zinc finger (2) FUNCTION: Catalytic component of the RAG complex, a multiprotein complex that mediates the DNA cleavage phase during V(D)J recombination. V(D)J recombination assembles a diverse repertoire of immunoglobulin and T-cell receptor genes in developing B and T-lymphocytes through rearrangement of different V (variable), in some cases D (diversity), and J (joining) gene segments. In the RAG complex, RAG1 mediates the DNA-binding to the conserved recombination signal sequences (RSS) and catalyzes the DNA cleavage activities by introducing a double-strand break between the RSS and the adjacent coding segment. RAG2 is not a catalytic component but is required for all known catalytic activities. DNA cleavage occurs in 2 steps: a first nick is introduced in the top strand immediately upstream of the heptamer, generating a 3'-hydroxyl group that can attack the phosphodiester bond on the opposite strand in a direct transesterification reaction, thereby creating 4 DNA ends: 2 hairpin coding ends and 2 blunt, 5'-phosphorylated ends. The chromatin structure plays an essential role in the V(D)J recombination reactions and the presence of histone H3 trimethylated at 'Lys-4' (H3K4me3) stimulates both the nicking and haipinning steps. The RAG complex also plays a role in pre-B cell allelic exclusion, a process leading to expression of a single immunoglobulin heavy chain allele to enforce clonality and monospecific recognition by the B-cell antigen receptor (BCR) expressed on individual B-lymphocytes. The introduction of DNA breaks by the RAG complex on one immunoglobulin allele induces ATM-dependent repositioning of the other allele to pericentromeric heterochromatin, preventing accessibility to the RAG complex and recombination of the second allele. In addition to its endonuclease activity, RAG1 also acts as an E3 ubiquitin-protein ligase that mediates monoubiquitination of histone H3. Histone H3 monoubiquitination is required for the joining step of V(D)J recombination. Mediates polyubiquitination of KPNA1. {ECO:0000269|PubMed:10601032, ECO:0000269|PubMed:10678172, ECO:0000269|PubMed:12629039, ECO:0000269|PubMed:14671314, ECO:0000269|PubMed:17028591, ECO:0000269|PubMed:19118899, ECO:0000269|PubMed:19396172, ECO:0000269|PubMed:19448632, ECO:0000269|PubMed:19524534, ECO:0000269|PubMed:20122409, ECO:0000269|PubMed:22157821, ECO:0000269|PubMed:2598259, ECO:0000269|PubMed:8521468, ECO:0000269|PubMed:9094713}. PTM: Autoubiquitinated in the presence of CDC34/UBCH3. {ECO:0000269|PubMed:14671314, ECO:0000269|PubMed:19118899}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00820, ECO:0000269|PubMed:8284210}. SUBUNIT: Homodimer. Component of the RAG complex composed of core components RAG1 and RAG2, and associated component HMGB1 or HMGB2. Interacts with DCAF1, leading to recruitment of the CUL4A-RBX1-DDB1-DCAF1/VPRBP complex to ubiquitinate proteins and limit error-prone repair during V(D)J recombination. {ECO:0000269|PubMed:19396172, ECO:0000269|PubMed:22157821, ECO:0000269|PubMed:8521468, ECO:0000269|PubMed:9094713, ECO:0000269|PubMed:9184213, ECO:0000269|PubMed:9228952}. DOMAIN: The RING-type zinc finger mediates the E3 ubiquitin-protein ligase activity. {ECO:0000269|PubMed:19396172}.; DOMAIN: The NBD (nonamer binding) DNA-binding domain mediates the specific binding to the nonamer RSS motif by forming a tightly interwoven homodimer that binds and synapses 2 nonamer elements, with each NBD making contact with both DNA molecules. Each RSS is composed of well-conserved heptamer (consensus 5'-CACAGTG-3') and nonamer (consensus 5'-ACAAAAACC-3') sequences separated by a spacer of either 12 bp or 23 bp. {ECO:0000255|PROSITE-ProRule:PRU00820, ECO:0000269|PubMed:19396172}. TISSUE SPECIFICITY: Maturing lymphoid cells and central nervous system. +Q6WBX7 RAD9B_MOUSE Cell cycle checkpoint control protein RAD9B (DNA repair exonuclease rad9 homolog B) (mRAD9B) 403 44,840 Chain (1); Modified residue (2) SUBUNIT: Interacts with HUS1, HUS1B, RAD1, RAD9A and RAD17. {ECO:0000250}. +Q9CQY2 RAMAC_MOUSE RNA guanine-N7 methyltransferase activating subunit (Protein FAM103A1) (RNA guanine-7 methyltransferase activating subunit) (RNMT-activating mRNA cap methylating subunit) (RNMT-activating mRNA cap methyltransferase subunit) (RNMT-activating mini protein) (RAM) 119 14,556 Chain (1); Compositional bias (1); Modified residue (3); Motif (1); Region (2); Sequence conflict (1) FUNCTION: Regulatory subunit of the mRNA-capping methyltransferase RNMT:RAMAC complex that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs. Promotes the recruitment of the methyl donor, S-adenosyl-L-methionine, to RNMT. Regulates RNMT expression by a post-transcriptional stabilizing mechanism. Binds RNA. {ECO:0000250|UniProtKB:Q9BTL3}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BTL3}. SUBUNIT: Interacts with RNMT; this interaction enhances mRNA binding and cap methyltransferase activity. {ECO:0000250|UniProtKB:Q9BTL3}. +Q8BHL4 RAI3_MOUSE Retinoic acid-induced protein 3 (G-protein coupled receptor family C group 5 member A) (Retinoic acid-induced gene 1 protein) (RAIG-1) 356 40,101 Chain (1); Erroneous initiation (1); Glycosylation (1); Modified residue (6); Sequence conflict (1); Topological domain (8); Transmembrane (7) TRANSMEM 36 56 Helical; Name=1. {ECO:0000255}.; TRANSMEM 69 89 Helical; Name=2. {ECO:0000255}.; TRANSMEM 102 122 Helical; Name=3. {ECO:0000255}.; TRANSMEM 132 152 Helical; Name=4. {ECO:0000255}.; TRANSMEM 179 199 Helical; Name=5. {ECO:0000255}.; TRANSMEM 215 235 Helical; Name=6. {ECO:0000255}.; TRANSMEM 245 265 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 35 Extracellular. {ECO:0000305}.; TOPO_DOM 57 68 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 90 101 Extracellular. {ECO:0000305}.; TOPO_DOM 123 131 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 153 178 Extracellular. {ECO:0000305}.; TOPO_DOM 200 214 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 236 244 Extracellular. {ECO:0000305}.; TOPO_DOM 266 356 Cytoplasmic. {ECO:0000305}. FUNCTION: Orphan receptor. Could be involved in modulating differentiation and maintaining homeostasis of epithelial cells. This retinoic acid-inducible GPCR provides evidence for a possible interaction between retinoid and G-protein signaling pathways. Functions as a negative modulator of EGFR signaling (PubMed:25744720). Acts as a lung tumor suppressor (PubMed:18000218). {ECO:0000269|PubMed:18000218, ECO:0000269|PubMed:25744720}. PTM: Phosphorylated in two conserved double-tyrosine motifs, TYR-318/TYR-321 and TYR-346/TYR-349 by EGFR. TYR-318 and TYR-321 are the preferred residues responsible for EGFR-mediated GPRC5A phosphorylation. {ECO:0000250|UniProtKB:Q8NFJ5}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18000218}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Interacts (via its transmembrane domain) with EGFR (PubMed:25744720). {ECO:0000269|PubMed:25744720}. TISSUE SPECIFICITY: Expressed predominantly in normal fetal and adult lung. Almost undetectable or expressed at very low levels in other tissues. {ECO:0000269|PubMed:18000218}. +Q3U0S6 RAIN_MOUSE Ras-interacting protein 1 (Rain) 961 103,559 Chain (1); Compositional bias (1); Domain (2); Modified residue (7); Sequence conflict (2) FUNCTION: Required for the proper formation of vascular structures that develop via both vasculogenesis and angiogenesis. Acts as a critical and vascular-specific regulator of GTPase signaling, cell architecture, and adhesion, which is essential for endothelial cell morphogenesis and blood vessel tubulogenesis. Regulates the activity of Rho GTPases in part by recruiting ARHGAP29 and suppressing RhoA signaling and dampening ROCK and MYH9 activities in endothelial cells. May act as effector for Golgi-bound HRAS and other Ras-like proteins. May promote HRAS-mediated transformation. Negative regulator of amino acid starvation-induced autophagy (By similarity). {ECO:0000250, ECO:0000269|PubMed:19272373, ECO:0000269|PubMed:21396893}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}. Golgi apparatus, Golgi stack {ECO:0000250}. Note=Associated with perinuclear vesicles. Is recruited to Golgi stacks by activated HRAS (By similarity). {ECO:0000250}. SUBUNIT: Interacts with Ras family members that have been activated by GTP binding. Interacts with HRAS, RAP1A, RAP2, RRAS, RAF1 and RRAS2 (By similarity). Interacts with MYH9 and ARHGAP29. {ECO:0000250, ECO:0000269|PubMed:21396893}. TISSUE SPECIFICITY: Detected in kidney, heart, skeletal muscle, small intestine and lung. {ECO:0000269|PubMed:15031288}. +Q9WUP0 RAMP2_MOUSE Receptor activity-modifying protein 2 189 21,017 Chain (1); Disulfide bond (2); Glycosylation (4); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 160 180 Helical. {ECO:0000255}. TOPO_DOM 45 159 Extracellular. {ECO:0000255}.; TOPO_DOM 181 189 Cytoplasmic. {ECO:0000255}. FUNCTION: Transports the calcitonin gene-related peptide type 1 receptor (CALCRL) to the plasma membrane. Acts as a receptor for adrenomedullin (AM) together with CALCRL. {ECO:0000269|PubMed:10854696}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Heterodimer of CALCRL and RAMP2. TISSUE SPECIFICITY: Ubiquitous. Expressed predominantly in embryonic brain, lung and gut and in adult heart, lung, skeletal muscle and brain. {ECO:0000269|PubMed:10777702, ECO:0000269|PubMed:10854696}. +P62827 RAN_MOUSE GTP-binding nuclear protein Ran (GTPase Ran) (Ras-like protein TC4) (Ras-related nuclear protein) 216 24,423 Binding site (1); Chain (1); Cross-link (3); Initiator methionine (1); Modified residue (8); Mutagenesis (3); Nucleotide binding (4); Region (1); Sequence conflict (3); Site (1) FUNCTION: GTPase involved in nucleocytoplasmic transport, participating both to the import and the export from the nucleus of proteins and RNAs. Switches between a cytoplasmic GDP- and a nuclear GTP-bound state by nucleotide exchange and GTP hydrolysis. Nuclear import receptors such as importin beta bind their substrates only in the absence of GTP-bound RAN and release them upon direct interaction with GTP-bound RAN, while export receptors behave in the opposite way. Thereby, RAN controls cargo loading and release by transport receptors in the proper compartment and ensures the directionality of the transport. Interaction with RANBP1 induces a conformation change in the complex formed by XPO1 and RAN that triggers the release of the nuclear export signal of cargo proteins. RAN (GTP-bound form) triggers microtubule assembly at mitotic chromosomes and is required for normal mitotic spindle assembly and chromosome segregation. Required for normal progress through mitosis. The complex with BIRC5/survivin plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. Acts as a negative regulator of the kinase activity of VRK1 and VRK2. Enhances AR-mediated transactivation. {ECO:0000250|UniProtKB:P62826}. PTM: Acetylation by KAT5 at Lys-134 is increased during mitosis, impairs RANGRF binding and enhances RCC1 binding. {ECO:0000250|UniProtKB:P62826}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18347012, ECO:0000269|PubMed:25946333}. Nucleus envelope {ECO:0000269|PubMed:25946333}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P62826}. Cytoplasm {ECO:0000269|PubMed:18347012}. Melanosome {ECO:0000250|UniProtKB:P62826}. Note=Predominantly nuclear during interphase. Becomes dispersed throughout the cytoplasm during mitosis (By similarity). Identified by mass spectrometry in melanosome fractions from stage I to stage IV (By similarity). {ECO:0000250|UniProtKB:P62826}. SUBUNIT: Monomer. Interacts with RANGAP1, which promotes RAN-mediated GTP hydrolysis. Interacts with KPNB1. Interaction with KPNB1 inhibits RANGAP1-mediated stimulation of GTPase activity. Interacts with RCC1 which promotes the exchange of RAN-bound GDP by GTP. Interaction with KPNB1 inhibits RCC1-mediated exchange of RAN-bound GDP by GTP. Interacts (GTP-bound form) with TNPO1; the interaction is direct. Interacts with KPNB1 and with TNPO1; both inhibit RAN GTPase activity (By similarity). Interacts (via C-terminus) with RANBP1, which alleviates the inhibition of RAN GTPase activity (PubMed:7891706, PubMed:9428644). Interacts with RANGRF, which promotes the release of bound guanine nucleotide (PubMed:10811801). RANGRF and RCC1 compete for an overlapping binding site on RAN. Identified in a complex with KPNA2 and CSE1L; interaction with RANBP1 mediates dissociation of RAN from this complex. Interaction with both RANBP1 and KPNA2 promotes dissociation of the complex between RAN and KPNB1. Identified in a complex composed of RAN, RANGAP1 and RANBP1. Identified in a complex that contains TNPO1, RAN and RANBP1. Identified in a nuclear export complex with XPO1. Found in a nuclear export complex with RANBP3 and XPO1. Interacts with RANBP2/NUP358. Interaction with RANBP1 or RANBP2 induces a conformation change in the complex formed by XPO1 and RAN that triggers the release of the nuclear export signal of cargo proteins. Component of a nuclear export receptor complex composed of KPNB1, RAN, SNUPN and XPO1 (By similarity). Found in a nuclear export complex with RAN, XPO5 and pre-miRNA (By similarity). Interacts (GTP-bound form) with XPO5 (By similarity). Part of a complex consisting of RANBP9, RAN, DYRK1B and COPS5 (By similarity). Interacts with RANBP9 and RANBP10 (PubMed:18347012). Interacts in its GTP-bound form with BIRC5/survivin at S and M phases of the cell cycle. Interacts with TERT; the interaction requires hydrogen peroxide-mediated phosphorylation of TERT and transports TERT to the nucleus. Interacts with MAD2L2. Interacts with VRK1 and VRK3. Interacts with VRK2 (By similarity). Interacts with NEMP1 and KPNB1 (PubMed:25946333). Interacts (GDP-bound form) with NUTF2; regulates RAN nuclear import. Interacts with CAPG; mediates CAPG nuclear import. Interacts with NUP153. Interacts with the AR N-terminal poly-Gln region; the interaction with AR is inversely correlated with the poly-Gln length (By similarity). Interacts with MYCBP2, which promotes RAN-mediated GTP hydrolysis (PubMed:26304119). {ECO:0000250|UniProtKB:P62825, ECO:0000250|UniProtKB:P62826, ECO:0000269|PubMed:10811801, ECO:0000269|PubMed:18347012, ECO:0000269|PubMed:25946333, ECO:0000269|PubMed:26304119, ECO:0000269|PubMed:7891706, ECO:0000269|PubMed:9428644}. TISSUE SPECIFICITY: Expressed in a variety of tissues, including testis. {ECO:0000269|PubMed:7849398}. +P61226 RAP2B_MOUSE Ras-related protein Rap-2b 183 20,504 Chain (1); Lipidation (3); Modified residue (1); Motif (1); Mutagenesis (3); Nucleotide binding (3); Propeptide (1) FUNCTION: Small GTP-binding protein which cycles between a GDP-bound inactive and a GTP-bound active form. Involved in EGFR and CHRM3 signaling pathways through stimulation of PLCE1. May play a role in cytoskeletal rearrangements and regulate cell spreading through activation of the effector TNIK. May regulate membrane vesiculation in red blood cells. {ECO:0000269|PubMed:19061864}. PTM: Palmitoylated. Unlike RAP2A and RAP2C, palmitoylation of RAP2B is not required for association with recycling endosome membranes and activation of TNIK. {ECO:0000269|PubMed:19061864}. SUBCELLULAR LOCATION: Recycling endosome membrane {ECO:0000269|PubMed:19061864}; Lipid-anchor {ECO:0000269|PubMed:19061864}; Cytoplasmic side {ECO:0000269|PubMed:19061864}. Note=Associated with red blood cells-released vesicles. {ECO:0000250}. SUBUNIT: Interacts with PLCE1. Interacts with SGSM1, SGSM2 and SGSM3 (By similarity). The GTP-bound form of RAP2B interacts with RUNDC3A. {ECO:0000250, ECO:0000269|PubMed:9523700}. DOMAIN: The effector domain mediates the interaction with RUNDC3A. {ECO:0000269|PubMed:9523700}. +P49769 PSN1_MOUSE Presenilin-1 (PS-1) (EC 3.4.23.-) (Protein S182) [Cleaved into: Presenilin-1 NTF subunit; Presenilin-1 CTF subunit; Presenilin-1 CTF12 (PS1-CTF12)] 467 52,640 Active site (2); Alternative sequence (2); Chain (3); Modified residue (6); Motif (1); Natural variant (5); Region (3); Site (4); Topological domain (10); Transmembrane (9) TRANSMEM 83 103 Helical. {ECO:0000250|UniProtKB:P49768}.; TRANSMEM 133 153 Helical. {ECO:0000250|UniProtKB:P49768}.; TRANSMEM 167 189 Helical. {ECO:0000250|UniProtKB:P49768}.; TRANSMEM 195 216 Helical. {ECO:0000250|UniProtKB:P49768}.; TRANSMEM 221 241 Helical. {ECO:0000250|UniProtKB:P49768}.; TRANSMEM 249 272 Helical. {ECO:0000250|UniProtKB:P49768}.; TRANSMEM 381 401 Helical. {ECO:0000250|UniProtKB:P49768}.; TRANSMEM 408 428 Helical. {ECO:0000250|UniProtKB:P49768}.; TRANSMEM 433 453 Helical. {ECO:0000250|UniProtKB:P49768}. TOPO_DOM 1 82 Cytoplasmic. {ECO:0000250|UniProtKB:P49768}.; TOPO_DOM 104 132 Lumenal. {ECO:0000250|UniProtKB:P49768}.; TOPO_DOM 154 166 Cytoplasmic. {ECO:0000250|UniProtKB:P49768}.; TOPO_DOM 190 194 Lumenal. {ECO:0000250|UniProtKB:P49768}.; TOPO_DOM 217 220 Cytoplasmic. {ECO:0000250|UniProtKB:P49768}.; TOPO_DOM 242 248 Lumenal. {ECO:0000250|UniProtKB:P49768}.; TOPO_DOM 273 380 Cytoplasmic. {ECO:0000250|UniProtKB:P49768}.; TOPO_DOM 402 407 Lumenal. {ECO:0000250|UniProtKB:P49768}.; TOPO_DOM 429 432 Cytoplasmic. {ECO:0000250|UniProtKB:P49768}.; TOPO_DOM 454 467 Lumenal. {ECO:0000250|UniProtKB:P49768}. FUNCTION: Catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (amyloid-beta precursor protein). Requires the presence of the other members of the gamma-secretase complex for protease activity (By similarity). Plays a role in Notch and Wnt signaling cascades and regulation of downstream processes via its role in processing key regulatory proteins, and by regulating cytosolic CTNNB1 levels (PubMed:10421573, PubMed:11517342). Stimulates cell-cell adhesion via its interaction with CDH1; this stabilizes the complexes between CDH1 (E-cadherin) and its interaction partners CTNNB1 (beta-catenin), CTNND1 and JUP (gamma-catenin) (PubMed:11226248). Under conditions of apoptosis or calcium influx, cleaves CDH1 (PubMed:11953314). This promotes the disassembly of the complexes between CDH1 and CTNND1, JUP and CTNNB1, increases the pool of cytoplasmic CTNNB1, and thereby negatively regulates Wnt signaling (PubMed:11226248). Required for normal embryonic brain and skeleton development, and for normal angiogenesis (PubMed:9160754, PubMed:10421573, PubMed:12834865). Mediates the proteolytic cleavage of EphB2/CTF1 into EphB2/CTF2 (PubMed:17428795). {ECO:0000250|UniProtKB:P49768, ECO:0000269|PubMed:10421573, ECO:0000269|PubMed:11226248, ECO:0000269|PubMed:11517342, ECO:0000269|PubMed:11953314, ECO:0000269|PubMed:12834865, ECO:0000269|PubMed:17428795, ECO:0000269|PubMed:9160754}. PTM: Heterogeneous proteolytic processing generates N-terminal (NTF) and C-terminal (CTF) fragments of approximately 35 and 20 kDa, respectively. During apoptosis, the C-terminal fragment (CTF) is further cleaved by caspase-3 to produce the fragment, PS1-CTF12. {ECO:0000250|UniProtKB:P49768}.; PTM: After endoproteolysis, the C-terminal fragment (CTF) is phosphorylated on serine residues by PKA and/or PKC. Phosphorylation on Ser-346 inhibits endoproteolysis. {ECO:0000250|UniProtKB:P49768}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P49768}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P49768}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P49768}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P49768}. Cytoplasmic granule {ECO:0000250|UniProtKB:P49768}. Cell membrane {ECO:0000269|PubMed:10421573, ECO:0000269|PubMed:11517342}. Cytoplasmic vesicle {ECO:0000269|PubMed:10421573, ECO:0000305|PubMed:11517342}. Note=Translocates with bound NOTCH1 from the endoplasmic reticulum and/or Golgi to the cell surface. Colocalizes with CDH1/2 at sites of cell-cell contact. Colocalizes with CTNNB1 in the endoplasmic reticulum and the proximity of the plasma membrane. Also present in azurophil granules of neutrophils. Colocalizes with UBQLN1 in the cell membrane and in cytoplasmic juxtanuclear structures called aggresomes. {ECO:0000250|UniProtKB:P49768}. SUBUNIT: Homodimer. The functional gamma-secretase complex is composed of at least four polypeptides: a presenilin homodimer (PSEN1 or PSEN2), nicastrin (NCSTN), APH1 (APH1A or APH1B) and PEN2. Such minimal complex is sufficient for secretase activity. Other components which are associated with the complex include SLC25A64, SLC5A7, PHB and PSEN1 isoform 3. Predominantly heterodimer of a N-terminal (NTF) and a C-terminal (CTF) endoproteolytical fragment. Associates with proteolytic processed C-terminal fragments C83 and C99 of the amyloid precursor protein (APP). Associates with NOTCH1. Associates with cadherin/catenin adhesion complexes through direct binding to CDH1 or CDH2 (PubMed:11226248). Interaction with CDH1 stabilizes the complex and stimulates cell-cell aggregation. Interaction with CDH2 is essential for trafficking of CDH2 from the endoplasmic reticulum to the plasma membrane. Interacts with CTNND2, CTNNB1, CTNND1, JUP, HERPUD1, FLNA, FLNB, MTCH1, PKP4 and PARL. Interacts through its N-terminus with isoform 3 of GFAP (By similarity). Interacts with DOCK3 (PubMed:10854253). Interacts with isoform 1 and isoform 3 of UBQLN1 (By similarity). {ECO:0000250|UniProtKB:P49768, ECO:0000269|PubMed:10854253, ECO:0000269|PubMed:11226248}. DOMAIN: The PAL motif is required for normal active site conformation. {ECO:0000250|UniProtKB:P49768}. TISSUE SPECIFICITY: Detected in embryonic brain (PubMed:10421573). Detected in adult skin epidermis (at protein level) (PubMed:11517342). {ECO:0000269|PubMed:10421573, ECO:0000269|PubMed:11517342}. +P62889 RL30_MOUSE 60S ribosomal protein L30 115 12,784 Chain (1); Cross-link (1); Modified residue (3) +P70698 PYRG1_MOUSE CTP synthase 1 (EC 6.3.4.2) (CTP synthetase 1) (UTP--ammonia ligase 1) 591 66,682 Active site (3); Chain (1); Domain (1); Modified residue (9); Sequence conflict (4) Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2. FUNCTION: This enzyme is involved in the de novo synthesis of CTP, a precursor of DNA, RNA and phospholipids. Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as a source of nitrogen. This enzyme and its product, CTP, play a crucial role in the proliferation of activated lymphocytes and therefore in immunity. {ECO:0000250|UniProtKB:P17812}. +P62900 RL31_MOUSE 60S ribosomal protein L31 125 14,463 Chain (1); Modified residue (7) +Q66JV4 R12BB_MOUSE RNA-binding protein 12B-B (RNA-binding motif protein 12B-B) 834 96,450 Alternative sequence (1); Chain (1); Domain (4); Erroneous initiation (1); Modified residue (1); Sequence conflict (2) +Q8C551 R51A1_MOUSE RAD51-associated protein 1 (RAB22) (RAD51-interacting protein) 337 36,227 Chain (1); Modified residue (5); Region (1); Sequence conflict (12) FUNCTION: May participate in a common DNA damage response pathway associated with the activation of homologous recombination and double-strand break repair. Functionally cooperates with PALB2 in promoting of D-loop formation by RAD51. Binds to single and double stranded DNA, and is capable of aggregating DNA. Also binds RNA (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9192668}. Note=Colocalizes with RAD51 to multiple nuclear foci. SUBUNIT: Interacts (via C-terminal region) with RAD51; the interaction is direct (By similarity). Interacts with RAD51 and PALB2. {ECO:0000250, ECO:0000269|PubMed:9192668}. TISSUE SPECIFICITY: Most abundantly expressed in testis. Also expressed in spleen, thymus and bone marrow. Not detected in heart, kidney or liver. {ECO:0000269|PubMed:9192668}. +Q924H5 RA51C_MOUSE DNA repair protein RAD51 homolog 3 (R51H3) (RAD51 homolog C) (RAD51-like protein 2) 366 40,675 Alternative sequence (1); Chain (1); Modified residue (1); Motif (1); Nucleotide binding (1); Region (2); Sequence conflict (4) FUNCTION: Essential for the homologous recombination (HR) pathway of DNA repair. Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA breaks arising during DNA replication or induced by DNA-damaging agents. Part of the RAD21 paralog protein complexes BCDX2 and CX3 which act at different stages of the BRCA1-BRCA2-dependent HR pathway. Upon DNA damage, BCDX2 seems to act downstream of BRCA2 recruitment and upstream of RAD51 recruitment; CX3 seems to act downstream of RAD51 recruitment; both complexes bind predominantly to the intersection of the four duplex arms of the Holliday junction (HJ) and to junction of replication forks. The BCDX2 complex was originally reported to bind single-stranded DNA, single-stranded gaps in duplex DNA and specifically to nicks in duplex DNA. The BCDX2 subcomplex RAD51B:RAD51C exhibits single-stranded DNA-dependent ATPase activity suggesting an involvement in early stages of the HR pathway. Involved in RAD51 foci formation in response to DNA damage suggesting an involvement in early stages of HR probably in the invasion step. Has an early function in DNA repair in facilitating phosphorylation of the checkpoint kinase CHEK2 and thereby transduction of the damage signal, leading to cell cycle arrest and HR activation. Participates in branch migration and HJ resolution and thus is important for processing HR intermediates late in the DNA repair process; the function may be linked to the CX3 complex. Part of a PALB2-scaffolded HR complex containing BRCA2 and which is thought to play a role in DNA repair by HR. Protects RAD51 from ubiquitin-mediated degradation that is enhanced following DNA damage. Plays a role in regulating mitochondrial DNA copy number under conditions of oxidative stress in the presence of RAD51 and XRCC3. Contributes to DNA cross-link resistance, sister chromatid cohesion and genomic stability. Involved in maintaining centrosome number in mitosis. {ECO:0000269|PubMed:20471405}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Mitochondrion {ECO:0000250}. Note=DNA damage induces an increase in nuclear levels. Accumulates in DNA damage induced nuclear foci or RAD51C foci which is formed during the S or G2 phase of cell cycle. Accumulation at DNA lesions requires the presence of NBN/NBS1, ATM and RPA (By similarity). {ECO:0000250}. SUBUNIT: Part of the Rad21 paralog protein complexes BCDX2 and CX3; the complexes have a ring-like structure arranged into a flat disc around a central channel. The BCDX2 complex consits of RAD51B, RAD51C, RAD51D and XRCC2; the CX3 complex consists of RAD51C and XRCC3. The BCDX2 subcomplex RAD51B:RAD51C interacts with RAD51. Interacts with SWSAP1; involved in homologous recombination repair. Interacts directly with PALB2 which may serve as a scaffold for a HR complex containing PALB2, BRCA2, RAD51C, RAD51 and XRCC3 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the heart, brain, spleen, lung, liver, kidney and testis but not detected in skeletal muscle. {ECO:0000269|PubMed:11410366}. +O35719 RA51B_MOUSE DNA repair protein RAD51 homolog 2 (R51H2) (RAD51 homolog B) (RAD51-like protein 1) 350 38,152 Alternative sequence (2); Chain (1); Nucleotide binding (1); Region (1); Sequence conflict (1) FUNCTION: Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA breaks arising during DNA replication or induced by DNA-damaging agents. May promote the assembly of presynaptic RAD51 nucleoprotein filaments. Binds single-stranded DNA and double-stranded DNA and has DNA-dependent ATPase activity. Part of the RAD21 paralog protein complex BCDX2 which acts in the BRCA1-BRCA2-dependent HR pathway. Upon DNA damage, BCDX2 acts downstream of BRCA2 recruitment and upstream of RAD51 recruitment. BCDX2 binds predominantly to the intersection of the four duplex arms of the Holliday junction and to junction of replication forks. The BCDX2 complex was originally reported to bind single-stranded DNA, single-stranded gaps in duplex DNA and specifically to nicks in duplex DNA. The BCDX2 subcomplex RAD51B:RAD51C exhibits single-stranded DNA-dependent ATPase activity suggesting an involvement in early stages of the HR pathway (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Part of the BCDX2 complex consisting of RAD51B, RAD51C, RAD51D and XRCC2; the complex has a ring-like structure arranged into a flat disc around a central channel. The BCDX2 subcomplex RAD51B:RAD51C interacts with RAD51. Interacts with SWSAP1; involved in homologous recombination repair (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in a wide range of tissues. +Q9WTL2 RAB25_MOUSE Ras-related protein Rab-25 213 23,473 Chain (1); Lipidation (2); Modified residue (1); Motif (1); Nucleotide binding (4); Propeptide (1); Sequence conflict (2) FUNCTION: Involved in the regulation of cell survival. Promotes invasive migration of cells in which it functions to localize and maintain integrin alpha-V/beta-1 at the tips of extending pseudopodia. Involved in the regulation of epithelial morphogenesis through the control of CLDN4 expression and localization at tight junctions (PubMed:22696678). May selectively regulate the apical recycling pathway. Together with MYO5B regulates transcytosis (By similarity). {ECO:0000250|UniProtKB:E2RQ15, ECO:0000250|UniProtKB:P46629, ECO:0000250|UniProtKB:P57735, ECO:0000269|PubMed:22696678}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell projection, pseudopodium membrane {ECO:0000250|UniProtKB:P57735}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:P57735}. Note=Colocalizes with integrin alpha-V/beta-1 in vesicles at the pseudopodial tips. {ECO:0000250|UniProtKB:P57735}. SUBUNIT: Interacts with RAB11FIP1, RAB11FIP2, RAB11FIP3 and RAB11FIP4. Interacts (via the hypervariable C-terminal region) with ITGB1 (via the cytoplasmic region); the interaction is GTP-dependent. Interacts with ITGAV. Associates with the integrin alpha-V/beta-1 heterodimer. {ECO:0000250|UniProtKB:P57735}. +Q99KL7 RAB28_MOUSE Ras-related protein Rab-28 221 24,728 Chain (1); Initiator methionine (1); Lipidation (1); Modified residue (3); Motif (1); Nucleotide binding (4); Propeptide (1) SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm, cytoskeleton, cilium basal body. Note=Expressed in the basal body and ciliary rootlet of the photoreceptors. {ECO:0000250}. +Q9DD03 RAB13_MOUSE Ras-related protein Rab-13 202 22,770 Chain (1); Lipidation (1); Modified residue (2); Motif (1); Nucleotide binding (3); Propeptide (1) FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab is involved in endocytic recycling and regulates the transport to the plasma membrane of transmembrane proteins like the tight junction protein OCLN/occludin. Thereby, it regulates the assembly and the activity of tight junctions. Moreover, it may also regulate tight junction assembly by activating the PKA signaling pathway and by reorganizing the actin cytoskeleton through the activation of the downstream effectors PRKACA and MICALL2 respectively. Through its role in tight junction assembly, may play a role in the establishment of Sertoli cell barrier. Plays also a role in angiogenesis through regulation of endothelial cells chemotaxis. Also involved in neurite outgrowth. Has also been proposed to play a role in post-Golgi membrane trafficking from the TGN to the recycling endosome. Finally, it has been involved in insulin-induced transport to the plasma membrane of the glucose transporter GLUT4 and therefore may play a role in glucose homeostasis. {ECO:0000269|PubMed:21543326}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P51153}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P51153}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell junction, tight junction {ECO:0000250|UniProtKB:P51153}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:P51153}. Recycling endosome membrane {ECO:0000250|UniProtKB:P51153}. Cell projection, lamellipodium {ECO:0000269|PubMed:21543326}. Note=Tight junctions or associated with vesicles scattered throughout the cytoplasm in cells lacking tight junctions (By similarity). Relocalizes to the leading edge of lamellipodia in migrating endothelial cells (PubMed:21543326). {ECO:0000250|UniProtKB:P51153, ECO:0000269|PubMed:21543326}. SUBUNIT: Interacts (GTP-bound form) with MICALL2; competes with RAB8A and is involved in tight junctions assembly. Interacts (GTP-bound form) with MICALL1. Interacts (GTP-bound form) with MICAL1, MICAL3, MICALCL, EHBP1 and EHBP1L1; ternary complexes of RAB8A, RAB13 and either MICAL1 or EHBP1L1 are possible. Interacts with PRKACA; downstream effector of RAB13 involved in tight junction assembly. Interacts with GRB2; may recruit RAB13 to the leading edge of migrating endothelial cells where it can activate RHOA. Interacts (isoprenylated form) with PDE6D; dissociates RAB13 from membranes. Interacts with BICDL2/BICDR2. Interacts with LEPROT and LEPROTL1. {ECO:0000250|UniProtKB:P51153, ECO:0000269|PubMed:16525024, ECO:0000269|PubMed:20360680, ECO:0000269|PubMed:21543326}. +Q9CZT8 RAB3B_MOUSE Ras-related protein Rab-3B 219 24,757 Chain (1); Initiator methionine (1); Lipidation (2); Modified residue (4); Motif (1); Nucleotide binding (5) FUNCTION: Protein transport. Probably involved in vesicular traffic (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Golgi apparatus {ECO:0000269|PubMed:18396146}. Note=Colocalizes with GAS8/DRC4 in the Golgi apparatus. {ECO:0000269|PubMed:18396146}. SUBUNIT: Interacts with RIMS1, RIMS2, RPH3A and RPH3AL (PubMed:12578829). The GTP-bound form interacts with GAS8/DRC4 (via coiled-coil domains) (PubMed:18396146). {ECO:0000269|PubMed:12578829, ECO:0000269|PubMed:18396146}. TISSUE SPECIFICITY: Abundantly expressed in testis, lung and brain. {ECO:0000269|PubMed:18396146}. +Q68EF0 RAB3I_MOUSE Rab-3A-interacting protein (Rab3A-interacting protein) (Rabin-3) (SSX2-interacting protein) 428 47,133 Chain (1); Coiled coil (1); Modified residue (5) FUNCTION: Guanine nucleotide exchange factor (GEF) which may activate RAB8A and RAB8B. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. Mediates the release of GDP from RAB8A and RAB8B but not from RAB3A or RAB5. Modulates actin organization and promotes polarized transport of RAB8A-specific vesicles to the cell surface. Together with RAB11A, RAB8A, the exocyst complex, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Note=Predominantly cytoplasmic but a small proportion colocalizes with SSX2 in the nucleus. Activation of protein kinase C results in redistribution to the periphery of lamellipodia. In the cytoskeleton, localizes to cortical actin (By similarity). {ECO:0000250}. SUBUNIT: Interacts with the N-terminal region of SSX2. Interacts with the GDP-bound forms of RAB3A, RAB3D, RAB8A and RAB8B. Interacts with DCDC1. {ECO:0000250|UniProtKB:Q96QF0}. +P35279 RAB6A_MOUSE Ras-related protein Rab-6A (Rab-6) 208 23,590 Alternative sequence (1); Chain (1); Initiator methionine (1); Lipidation (2); Modified residue (3); Motif (1); Mutagenesis (4); Nucleotide binding (4) FUNCTION: Protein transport. Regulator of membrane traffic from the Golgi apparatus towards the endoplasmic reticulum (ER). Involved in COPI-independent retrograde transport from the Golgi to the ER (By similarity). {ECO:0000250|UniProtKB:P20340}. PTM: Prenylated. {ECO:0000250|UniProtKB:P20340}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:P20340}; Lipid-anchor {ECO:0000250|UniProtKB:P20340}. Note=BICD2 facilitates its targeting to Golgi apparatus membrane. {ECO:0000250|UniProtKB:P20340}. SUBUNIT: Interacts with RIC1 and RGP1; the interactions are direct with a preference for RAB6A-GDP. Interacts with VSP52 and RABGAP1. Interacts with GCC2 (via its GRIP domain). Interacts with RAB6IP1 (via its RUN 1 domain). Interacts with RAB6KIFL. Interacts with BICD1. Interacts with BICD2. Interacts with TMF1. Interacts (GTP-bound) with DYNLRB1; the interaction is direct (By similarity). Interacts with SCYL1BP1. Interacts with BICDL1; leads to its accumulation in the pericentrosomal region. Interacts with PIFO. Interacts (GTP-bound) with APBA1/MINT1 isoform 3, also called Mint1_826. {ECO:0000250|UniProtKB:P20340, ECO:0000269|PubMed:18997784, ECO:0000269|PubMed:20360680, ECO:0000269|PubMed:20643351, ECO:0000269|PubMed:23737971}. +Q8CG50 RAB43_MOUSE Ras-related protein Rab-43 210 23,263 Chain (1); Lipidation (2); Modified residue (2); Motif (1); Nucleotide binding (4) FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. The low intrinsic GTPase activity of RAB43 is activated by USP6NL. Involved in retrograde transport from the endocytic pathway to the Golgi apparatus. Involved in the transport of Shiga toxin from early and recycling endosomes to the trans-Golgi network. Required for the structural integrity of the Golgi complex. Plays a role in the maturation of phagosomes that engulf pathogens, such as S.aureus and Mycobacterium. SUBCELLULAR LOCATION: Cytoplasmic vesicle, phagosome {ECO:0000250|UniProtKB:Q86YS6}. Cytoplasmic vesicle, phagosome membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Golgi apparatus {ECO:0000250|UniProtKB:Q86YS6}. Golgi apparatus, trans-Golgi network membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q86YS6}. Note=Recruited to phagosomes containing S.aureus or M.tuberculosis. {ECO:0000250|UniProtKB:Q86YS6}. +P62821 RAB1A_MOUSE Ras-related protein Rab-1A (YPT1-related protein) 205 22,678 Chain (1); Initiator methionine (1); Lipidation (2); Modified residue (3); Motif (1); Nucleotide binding (5) FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. RAB1A regulates vesicular protein transport from the endoplasmic reticulum (ER) to the Golgi compartment and on to the cell surface, and plays a role in IL-8 and growth hormone secretion. Regulates the level of CASR present at the cell membrane. Plays a role in cell adhesion and cell migration, via its role in protein trafficking. Plays a role in autophagosome assembly and cellular defense reactions against pathogenic bacteria (By similarity). Plays a role in microtubule-dependent protein transport by early endosomes and in anterograde melanosome transport. {ECO:0000250, ECO:0000269|PubMed:20639577, ECO:0000269|PubMed:22854043}. PTM: Phosphorylated by CDK1 kinase during mitosis. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:P62820}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P62820}. Early endosome {ECO:0000250|UniProtKB:P62820}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P62820}. Membrane {ECO:0000250|UniProtKB:P62820}. Melanosome {ECO:0000269|PubMed:22854043}. Note=Alternates between membrane-associated and cytosolic forms. {ECO:0000250|UniProtKB:P62820}. SUBUNIT: May interact with YIPF5 (By similarity). Interacts with C9orf72; the interaction mediates recruitment of RAB1A to the ATG1/ULK1 kinase complex (PubMed:24549040). Interacts with GDI1; this promotes dissociation from membranes (By similarity). {ECO:0000250|UniProtKB:P62820, ECO:0000250|UniProtKB:P62822, ECO:0000269|PubMed:24549040}. +P61028 RAB8B_MOUSE Ras-related protein Rab-8B 207 23,603 Chain (1); Lipidation (1); Modified residue (3); Motif (1); Nucleotide binding (3); Propeptide (1) FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab may be involved in polarized vesicular trafficking and neurotransmitter release. May participate in cell junction dynamics in Sertoli cells (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Recruited to phagosomes containing S.aureus or Mycobacterium. {ECO:0000250}. SUBUNIT: Associated with actin, delta-catenin and alpha and beta tubulins (By similarity). Interacts with OTOF. Interacts with PEX5R (By similarity). Interacts with RAB3IP (By similarity). Interacts with VIM (By similarity). Interacts with CDH1 (By similarity). Interacts with MICALL2. {ECO:0000250, ECO:0000269|PubMed:18094055, ECO:0000269|PubMed:18772196}. +Q5U3K5 RABL6_MOUSE Rab-like protein 6 (GTP-binding protein Parf) (Rab-like protein 1) (RBEL1) 725 79,831 Chain (1); Modified residue (14); Nucleotide binding (3); Region (2); Sequence conflict (2) FUNCTION: May enhance cellular proliferation. May reduce growth inhibitory activity of CDKN2A (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Cytoplasm {ECO:0000250|UniProtKB:Q3YEC7}. Note=Predominantly cytoplasmic. {ECO:0000250|UniProtKB:Q3YEC7}. +Q8VEA8 RAB7B_MOUSE Ras-related protein Rab-7b 199 22,502 Alternative sequence (1); Chain (1); Lipidation (2); Modified residue (1); Motif (1); Nucleotide binding (5); Sequence conflict (1) FUNCTION: Controls vesicular trafficking from endosomes to the trans-Golgi network (TGN). Acts as a negative regulator of TLR9 signaling and can suppress TLR9-triggered TNFA, IL6, and IFNB production in macrophages by promoting TLR9 lysosomal degradation. Also negatively regulates TLR4 signaling in macrophages by promoting lysosomal degradation of TLR4. Promotes megakaryocytic differentiation by increasing NF-kappa-B-dependent IL6 production and subsequently enhancing the association of STAT3 with GATA1. Not involved in the regulation of the EGF- and EGFR degradation pathway. {ECO:0000269|PubMed:17395780, ECO:0000269|PubMed:19587007}. SUBCELLULAR LOCATION: Late endosome {ECO:0000269|PubMed:19587007}. Lysosome {ECO:0000269|PubMed:17395780, ECO:0000269|PubMed:19587007}. Golgi apparatus {ECO:0000250|UniProtKB:Q96AH8}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q96AH8}. Cytoplasmic vesicle, phagosome {ECO:0000250|UniProtKB:Q96AH8}. Cytoplasmic vesicle, phagosome membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Recruited to phagosomes containing S.aureus or Mycobacterium. {ECO:0000250|UniProtKB:Q96AH8}. +P22935 RABP2_MOUSE Cellular retinoic acid-binding protein 2 (Cellular retinoic acid-binding protein II) (CRABP-II) 138 15,746 Chain (1); Cross-link (1); Motif (1); Region (1) FUNCTION: Transports retinoic acid to the nucleus. Regulates the access of retinoic acid to the nuclear retinoic acid receptors. {ECO:0000269|PubMed:10490651}. PTM: Sumoylated in response to retinoic acid binding, sumoylation is critical for dissociation from ER and subsequent nuclear translocation. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10490651}. Endoplasmic reticulum {ECO:0000250}. Nucleus {ECO:0000269|PubMed:10490651}. Note=Upon ligand binding, a conformation change exposes a nuclear localization motif and the protein is transported into the nucleus. SUBUNIT: Interacts with importin alpha (By similarity). Interacts with RXR and RARA. {ECO:0000250}. DOMAIN: Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior. {ECO:0000250}. TISSUE SPECIFICITY: Embryo and skin of adult mouse. +P63001 RAC1_MOUSE Ras-related C3 botulinum toxin substrate 1 (p21-Rac1) 192 21,450 Binding site (1); Chain (1); Cross-link (1); Lipidation (1); Modified residue (1); Motif (1); Mutagenesis (1); Nucleotide binding (4); Propeptide (1) FUNCTION: Plasma membrane-associated small GTPase which cycles between active GTP-bound and inactive GDP-bound states. In its active state, binds to a variety of effector proteins to regulate cellular responses such as secretory processes, phagocytosis of apoptotic cells, epithelial cell polarization, neurons adhesion, migration and differentiation, and growth-factor induced formation of membrane ruffles. Rac1 p21/rho GDI heterodimer is the active component of the cytosolic factor sigma 1, which is involved in stimulation of the NADPH oxidase activity in macrophages. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. Stimulates PKN2 kinase activity. In concert with RAB7A, plays a role in regulating the formation of RBs (ruffled borders) in osteoclasts. In glioma cells, promotes cell migration and invasion. Required for atypical chemokine receptor ACKR2-induced LIMK1-PAK1-dependent phosphorylation of cofilin (CFL1) and for up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. In podocytes, promotes nuclear shuttling of NR3C2; this modulation is required for a proper kidney functioning. In synapses, seems to mediate the regulation of F-actin cluster formation performed by SHANK3. {ECO:0000250|UniProtKB:P63000, ECO:0000269|PubMed:19007770, ECO:0000269|PubMed:19029984}. PTM: GTP-bound active form is ubiquitinated by HACE1, leading to its degradation by the proteasome. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P63000}; Lipid-anchor {ECO:0000250|UniProtKB:P63000}; Cytoplasmic side {ECO:0000250|UniProtKB:P63000}. Melanosome {ECO:0000250|UniProtKB:P63000}. Cytoplasm {ECO:0000250|UniProtKB:P63000}. Cell projection, lamellipodium {ECO:0000269|PubMed:22959435}. Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine (By similarity). Found in the ruffled border (a late endosomal-like compartment in the plasma membrane) of bone-resorbing osteoclasts (By similarity). Localizes to the lamellipodium in a SH3RF1-dependent manner. {ECO:0000250|UniProtKB:P63000, ECO:0000269|PubMed:22959435}. SUBUNIT: Interacts with the GEF proteins PREX1, FARP1, FARP2, DOCK1, DOCK2 and DOCK7, which promote the exchange between GDP and GTP, and therefore activate it. Part of a quaternary complex containing PARD3, some PARD6 protein (PARD6A, PARD6B or PARD6G) and some atypical PKC protein (PRKCI or PRKCZ), which plays a central role in epithelial cell polarization. Found in a trimeric complex composed of DOCK1 and ELMO1, which plays a central role in phagocytosis of apoptotic cells. Interacts with RALBP1 via its effector domain. Interacts with BAIAP2, BAIAP2L1, PLXNB1, CYFIP1/SRA-1 and DEF6. Probably found in a ternary complex composed of DSCAM, PAK1 and RAC1. Interacts with DSCAM; the interaction requires PAK1. Interacts with TBC1D2. Interacts with UNKL. Interacts with USP6. Interacts with SPATA13. Interacts with ITGB4. Interacts with the GTP-bound form of RAB7A. Interacts with ARHGEF2. Interacts with ARHGEF16; mediates activation of RAC1 by EPHA2. Interacts with NOXA1. Interacts with S100A8 and calprotectin (S100A8/9). Interacts with ARHGDIA; the interaction is induced by SEMA5A, mediated through PLXNB3 and inactivates and stabilizes RAC1. Interacts with PACSIN2. Interacts with ITGB1BP1 (By similarity). Interacts with the GEF protein RASGRF2, which promotes the exchange between GDP and GTP, and therefore activates it. Interacts with PARD6A, PARD6B and PARD6G in a GTP-dependent manner. Part of a complex with MAP2K3, MAP3K3 and CCM2. Interacts with NISCH. Interacts with PIP5K1A. Interacts (GTP-bound form preferentially) with PKN2 (via the REM repeats); the interaction stimulates autophosphorylation and phosphorylation of PKN2. Interacts with SRGAP2. Interacts with PLXNB3. Interacts (when active) with PPP5C (via TPR repeats); activates PPP5C phosphatase activity and translocates PPP5C to the cell membrane. Interacts with RAPH1 (via Ras associating and PH domains) (By similarity). Interacts with MTSS1L (via IMD domain); this interaction may be important to potentiate PDGF-induced RAC1 activation. Interacts (GTP-bound form) with SH3RF3. Interacts with PAK2 (By similarity). Interacts (GTP-bound form) with SH3RF1 (PubMed:22959435). Found in a complex with SH3RF1, MAPK8IP1/JIP1, MAP3K11/MLK3, MAP2K7/MKK7 and MAPK8/JNK1 (PubMed:23963642). Interacts (both active GTP- or inactive GDP-bound forms) with SH3RF2 (By similarity). {ECO:0000250|UniProtKB:P63000, ECO:0000250|UniProtKB:Q6RUV5, ECO:0000269|PubMed:10679324, ECO:0000269|PubMed:10934474, ECO:0000269|PubMed:10934475, ECO:0000269|PubMed:14634666, ECO:0000269|PubMed:16002401, ECO:0000269|PubMed:17403031, ECO:0000269|PubMed:19737524, ECO:0000269|PubMed:20696765, ECO:0000269|PubMed:20974804, ECO:0000269|PubMed:22959435, ECO:0000269|PubMed:23963642, ECO:0000269|PubMed:9707409}. DOMAIN: The effector region mediates interaction with DEF6. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:1905006}. +Q9JM13 RABX5_MOUSE Rab5 GDP/GTP exchange factor (Rabex-5) 491 56,869 Chain (1); Coiled coil (1); Domain (1); Modified residue (7); Region (1); Zinc finger (1) FUNCTION: Rab effector protein acting as linker between gamma-adaptin, RAB4A or RAB5A. Involved in endocytic membrane fusion and membrane trafficking of recycling endosomes. Stimulates nucleotide exchange on RAB5A (By similarity). Can act as a ubiquitin ligase (By similarity). {ECO:0000250}. PTM: Monoubiquitinated. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Early endosome {ECO:0000250}. Recycling endosome {ECO:0000250}. SUBUNIT: Heterodimer with RABEP1. The heterodimer binds RAB4A and RAB5A that have been activated by GTP-binding. Binds TSC2, GGA1, GGA2, GGA3, AP1G1 and AP1G2 (By similarity). Interacts with RAB21, and with 100-fold lower affinity also with RAB22 (By similarity). Interacts with ubiquitinated EGFR (By similarity). Interacts with RGS14; the interaction is GTP-dependent. {ECO:0000250, ECO:0000269|PubMed:10926822}. TISSUE SPECIFICITY: Expressed in the white matter tracts of the cerebellum, the fimbria hippocampi and the corpus callosum. {ECO:0000269|PubMed:10926822}. +P60764 RAC3_MOUSE Ras-related C3 botulinum toxin substrate 3 (p21-Rac3) 192 21,379 Chain (1); Lipidation (1); Modified residue (1); Motif (1); Nucleotide binding (3); Propeptide (1) FUNCTION: Plasma membrane-associated small GTPase which cycles between an active GTP-bound and inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses, such as cell spreading and the formation of actin-based protusions including lamellipodia and membrane ruffles. Promotes cell adhesion and spreading on fibrinogen in a CIB1 and alpha-IIb/beta3 integrin-mediated manner (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Endomembrane system {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000250}. Cytoplasm, cytoskeleton. Note=Membrane-associated when activated. Colocalizes with NRBP to endomembranes and at the cell periphery in lamellipodia. Colocalized with CIB1 in the perinuclear area and at the cell periphery (By similarity). {ECO:0000250}. SUBUNIT: Interacts with the GEF protein DOCK7, which promotes the exchange between GDP and GTP, and therefore activates it. Interacts with C1D. Interacts (via C-terminal region) with CIB1; the interaction induces their association with the cytoskeleton upon alpha-IIb/beta3 integrin-mediated adhesion (By similarity). {ECO:0000250}. +Q61550 RAD21_MOUSE Double-strand-break repair protein rad21 homolog (Pokeweed agglutinin-binding protein 29) (PW29) (SCC1 homolog) 635 72,083 Chain (1); Compositional bias (2); Cross-link (3); Modified residue (8); Region (2); Sequence conflict (6); Site (3) FUNCTION: Cleavable component of the cohesin complex, involved in chromosome cohesion during cell cycle, in DNA repair, and in apoptosis. Plays a role in apoptosis, via its cleavage by caspase-3/CASP3 or caspase-7/CASP7 during early steps of apoptosis: the C-terminal 64 kDa cleavage product may act as a nuclear signal to initiate cytoplasmic events involved in the apoptotic pathway (By similarity). The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At metaphase-anaphase transition, this protein is cleaved by separase/ESPL1 and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis. {ECO:0000250}. PTM: Cleaved by separase/ESPL1 at the onset of anaphase. Cleaved by caspase-3 and caspase-7 at the beginning of apoptosis. The cleavage by ESPL1 and caspase-3 take place at different sites (By similarity). {ECO:0000250}.; PTM: Phosphorylated; becomes hyperphosphorylated in M phase of cell cycle. The large dissociation of cohesin from chromosome arms during prophase may be partly due to its phosphorylation by PLK (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O60216}. Chromosome {ECO:0000250|UniProtKB:O60216}. Chromosome, centromere {ECO:0000250|UniProtKB:O60216}. Note=Associates with chromatin. Before prophase it is scattered along chromosome arms. During prophase, most of cohesin complexes dissociate from chromatin probably because of phosphorylation by PLK, except at centromeres, where cohesin complexes remain. At anaphase, it is cleaved by separase/ESPL1, leading to the dissociation of the complex from chromosomes, allowing chromosome separation. Once cleaved by caspase-3, the C-terminal 64 kDa cleavage product translocates to the cytoplasm, where it may trigger apoptosis. {ECO:0000250|UniProtKB:O60216}. SUBUNIT: Cohesin complexes are composed of the SMC1 (SMC1A or SMC1B) and SMC3 heterodimer attached via their hinge domain, RAD21 which link them, and one STAG protein (STAG1, STAG2 or STAG3), which interacts with RAD21. Found in a complex with SMC1A, SMC3, CDCA5, PDS5A/SCC-112 and PDS5B/APRIN. Interacts with PDS5B and WAPL; the interaction is direct. Interacts with DDX11. Found in a cohesin complex with SMC1A, SMC3 and STAG1 (By similarity). Interacts with SMC1A and SMC3 (PubMed:10375619). {ECO:0000250|UniProtKB:O60216, ECO:0000269|PubMed:10375619}. DOMAIN: The C-terminal part associates with the head of SMC1A, while the N-terminal part binds to the head of SMC3. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed with highest levels in testis, brain, kidney, heart and thymus. Lowest levels in skeletal muscle. {ECO:0000269|PubMed:8812457}. +Q9QWZ1 RAD1_MOUSE Cell cycle checkpoint protein RAD1 (mRAD1) (EC 3.1.11.2) (DNA repair exonuclease rad1 homolog) (Rad1-like DNA damage checkpoint protein) 280 31,610 Alternative sequence (1); Chain (1); Sequence conflict (8) FUNCTION: Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair. The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex. Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3'-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage activity on substrates with double, nick, or gap flaps of distinct sequences and lengths; and DNA ligase I (LIG1) on long-patch base excision repair substrates. The 9-1-1 complex is necessary for the recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring during the S phase. Isoform 1 possesses 3'->5' double stranded DNA exonuclease activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the toroidal 9-1-1 (RAD9-RAD1-HUS1) complex, composed of RAD9A, RAD1 and HUS1. The 9-1-1 complex associates with LIG1, POLB, FEN1, RAD17, HDAC1, RPA1 and RPA2. The 9-1-1 complex associates with the RAD17-RFC complex. RAD1 interacts with POLB, FEN1, HUS1, HUS1B, RAD9A and RAD9B. Interacts with DNAJC7 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in testis, uterus, bladder, spleen, ovaries, lung, brain and muscle (at protein level). Expressed in brain, testis, kidney, heart, liver and lung. {ECO:0000269|PubMed:9660799, ECO:0000269|PubMed:9716408, ECO:0000269|PubMed:9828137}. +Q8CES1 PMIS2_MOUSE Transmembrane protein PMIS2 (Protein missing in infertile spermatozoa 2) 96 11,040 Chain (1); Sequence conflict (2); Transmembrane (2) TRANSMEM 31 51 Helical. {ECO:0000255}.; TRANSMEM 76 96 Helical. {ECO:0000255}. FUNCTION: May play a role in spermatozoa mobility. {ECO:0000269|PubMed:22621904}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Specifically expressed in testis. {ECO:0000269|PubMed:22621904}. +Q8CJH3 PLXB1_MOUSE Plexin-B1 2119 231,376 Chain (1); Coiled coil (1); Compositional bias (1); Disulfide bond (10); Domain (4); Glycosylation (7); Sequence conflict (2); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 1475 1495 Helical. {ECO:0000255}. TOPO_DOM 20 1474 Extracellular. {ECO:0000255}.; TOPO_DOM 1496 2119 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for SEMA4D. Plays a role in RHOA activation and subsequent changes of the actin cytoskeleton. Plays a role in axon guidance, invasive growth and cell migration. {ECO:0000269|PubMed:19788569}. PTM: Phosphorylated on tyrosine residues by ERBB2 and MET upon SEMA4D binding. {ECO:0000250}.; PTM: Proteolytic processing favors heterodimerization with PLXNB2 and SEMA4D binding. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SUBUNIT: Monomer, and heterodimer with PLXNB2 after proteolytic processing. Binds RAC1 that has been activated by GTP binding. Interaction with SEMA4D promotes binding of cytoplasmic ligands. Interacts with RRAS, ARHGEF11, ARHGEF12, ERBB2, MET, MST1R, RND1, RHOD, NRP1 and NRP2 (By similarity). Binds PLXNA1. {ECO:0000250, ECO:0000269|PubMed:12559962}. TISSUE SPECIFICITY: Detected in brain, heart, lung, liver, kidney, stomach, testis, uterus and placenta. {ECO:0000269|PubMed:12559962}. +Q91X88 PMGT1_MOUSE Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1 (POMGnT1) (EC 2.4.1.-) 660 75,110 Alternative sequence (3); Binding site (5); Chain (1); Compositional bias (1); Disulfide bond (4); Metal binding (2); Modified residue (1); Nucleotide binding (3); Region (5); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 38 58 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 37 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 59 660 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Participates in O-mannosyl glycosylation by catalyzing the addition of N-acetylglucosamine to O-linked mannose on glycoproteins. Catalyzes the synthesis of the GlcNAc(beta1-2)Man(alpha1-)O-Ser/Thr moiety on alpha-dystroglycan and other O-mannosylated proteins, providing the necessary basis for the addition of further carbohydrate moieties. Is specific for alpha linked terminal mannose. {ECO:0000250|UniProtKB:Q8WZA1}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q8WZA1}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q8WZA1}. SUBUNIT: Interacts with DAG1 (via O-linked mannose moiety). Interacts (via transmembrane domain) with FKTN; the interaction is direct and is required for normal location in Golgi membranes. {ECO:0000250|UniProtKB:Q8WZA1}. DOMAIN: The stem domain mediates specific interaction with beta-linked N-acetylglucosamine moieties of O-glycosylated proteins. It also interacts with its product, N-acetyl-beta-D-glucosaminyl-(1->2)-O-alpha-D-mannosylprotein. {ECO:0000250|UniProtKB:Q8WZA1}. TISSUE SPECIFICITY: Expressed at basal body and daughter centriole of photoreceptor cells (at protein level). {ECO:0000269|PubMed:26908613}. +Q9WVQ0 PMFBP_MOUSE Polyamine-modulated factor 1-binding protein 1 (PMF-1-binding protein) (Sperm tail-associated protein) 1022 119,401 Chain (1); Coiled coil (5) FUNCTION: Required for normal spermatogenesis (PubMed:30032984, PubMed:30298696). It functions as a scaffold protein that attaches the sperm head-tail connecting piece to the nuclear envelope, thus maintaining sperm head and tail integrity (PubMed:30032984). May also be involved in the general organization of cellular cytoskeleton. {ECO:0000269|PubMed:11468771, ECO:0000269|PubMed:30032984, ECO:0000269|PubMed:30298696}. SUBCELLULAR LOCATION: Cell projection, cilium, flagellum {ECO:0000269|PubMed:11468771, ECO:0000269|PubMed:30032984, ECO:0000269|PubMed:30298696}. Note=Localized at the sperm head-tail connecting piece (PubMed:30032984, PubMed:30298696). During spermatogenesis, it is first observed in the cytoplasm of round spermatids, it later appears in the implantation fossa region of the sperm nucleus during sperm head elongation and differentiation, and finally it localizes to the head-tail connecting piece (PubMed:30032984). {ECO:0000269|PubMed:30032984, ECO:0000269|PubMed:30298696}. TISSUE SPECIFICITY: Expressed in the testis. {ECO:0000269|PubMed:11468771, ECO:0000269|PubMed:30032984}. +Q60953 PML_MOUSE Protein PML 885 98,242 Alternative sequence (1); Chain (1); Coiled coil (1); Compositional bias (1); Cross-link (12); Erroneous initiation (1); Metal binding (8); Modified residue (16); Motif (1); Region (2); Sequence conflict (4); Zinc finger (3) FUNCTION: Functions via its association with PML-nuclear bodies (PML-NBs) in a wide range of important cellular processes, including tumor suppression, transcriptional regulation, apoptosis, senescence, DNA damage response, and viral defense mechanisms. Acts as the scaffold of PML-NBs allowing other proteins to shuttle in and out, a process which is regulated by SUMO-mediated modifications and interactions. Positively regulates p53/TP53 by acting at different levels (by promoting its acetylation and phosphorylation and by inhibiting its MDM2-dependent degradation). Regulates phosphorylation of ITPR3 and plays a role in the regulation of calcium homeostasis at the endoplasmic reticulum. Regulates RB1 phosphorylation and activity. Acts as both a negative regulator of PPARGC1A acetylation and a potent activator of PPAR signaling and fatty acid oxidation. Regulates translation of HIF1A by sequestering MTOR, and thereby plays a role in neoangiogenesis and tumor vascularization. Regulates PER2 nuclear localization and circadian function. Cytoplasmic PML is involved in the regulation of the TGF-beta signaling pathway. Required for normal development of the brain cortex during embryogenesis. Plays a role in granulopoiesis or monopoiesis of myeloid progenitor cells. May play a role regulating stem and progenitor cell fate in tissues as diverse as blood, brain and breast. Shows antiviral activity towards lymphocytic choriomeningitis virus (LCMV) and the vesicular stomatitis virus (VSV). {ECO:0000269|PubMed:10637504, ECO:0000269|PubMed:11907221, ECO:0000269|PubMed:12439746, ECO:0000269|PubMed:14976551, ECO:0000269|PubMed:15195100, ECO:0000269|PubMed:15356634, ECO:0000269|PubMed:16915281, ECO:0000269|PubMed:19136970, ECO:0000269|PubMed:21030605, ECO:0000269|PubMed:21427174, ECO:0000269|PubMed:21779477, ECO:0000269|PubMed:22274616, ECO:0000269|PubMed:22886304, ECO:0000269|PubMed:23279884, ECO:0000269|PubMed:9488655, ECO:0000269|PubMed:9806545}. PTM: Ubiquitinated; mediated by RNF4, RNF111, UHRF1, UBE3A/E6AP, BCR(KLHL20) E3 ubiquitin ligase complex, SIAH1 or SIAH2 and leading to subsequent proteasomal degradation. 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination by RNF4 is polysumoylation-dependent (By similarity). Ubiquitination by RNF111 is polysumoylation-dependent (PubMed:23530056). Ubiquitination by BCR(KLHL20) E3 ubiquitin ligase complex requires CDK1/2-mediated phosphorylation at Ser-528 which in turn is recognized by prolyl-isopeptidase PIN1 and PIN1-catalyzed isomerization further potentiates PML interaction with KLHL20 (By similarity). {ECO:0000250|UniProtKB:P29590, ECO:0000269|PubMed:23530056}.; PTM: Sumoylation regulates PML's: stability in response to extracellular or intracellular stimuli, transcription directly and indirectly, through sequestration of or dissociation of the transcription factors from PML-NBs, ability to regulate apoptosis and its anti-viral activities. It is also essential for: maintaining proper PML nuclear bodies (PML-NBs) structure and normal function, recruitment of components of PML-NBs, the turnover and retention of PML in PML-NBs and the integrity of PML-NBs. Undergoes 'Lys-11'-linked sumoylation. Sumoylation on all three sites (Lys-70, Lys-165 and Lys-500) is required for nuclear body formation. Sumoylation on Lys-165 is a prerequisite for sumoylation on Lys-70. Lys-70 and Lys-165 are sumoylated by PISA1 and PIAS2. PIAS1-mediated sumoylation of PML promotes its interaction with CSNK2A1/CK2 and phosphorylation at Ser-575 which in turn triggers its ubiquitin-mediated degradation. Sumoylation at Lys-500 by RANBP2 is essential for the proper assembly of PML-NBs. Desumoylated by SENP1, SENP2, SENP3, SENP5 and SENP6 (By similarity). {ECO:0000250|UniProtKB:P29590}.; PTM: Phosphorylation is a major regulatory mechanism that controls PML protein abundance and the number and size of PML nuclear bodies (PML-NBs). Phosphorylated in response to DNA damage, probably by ATR. HIPK2-mediated phosphorylation at Ser-17, Ser-45 and Ser-47 leads to increased accumulation of PML protein and its sumoylation and is required for the maximal pro-apoptotic activity of PML after DNA damage. MAPK1- mediated phosphorylations at Ser-404, Ser-515 and Ser-540 and CDK1/2-mediated phosphorylation at Ser-528 promote PIN1-dependent PML degradation. CK2-mediated phosphorylation at Ser-575 primes PML ubiquitination via an unidentified ubiquitin ligase (By similarity). {ECO:0000250|UniProtKB:P29590}.; PTM: Acetylation at Lys-497 is essential for its nuclear localization. Deacetylated at Lys-497 by SIRT1 and this deacetylation promotes PML control of PER2 nuclear localization (By similarity). {ECO:0000250|UniProtKB:P29590}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus, nucleoplasm. Cytoplasm. Nucleus, PML body. Nucleus, nucleolus {ECO:0000250}. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Early endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Detected in the nucleolus after DNA damage. Acetylation at Lys-497 is essential for its nuclear localization. Within the nucleus, most of PML is expressed in the diffuse nuclear fraction of the nucleoplasm and only a small fraction is found in the matrix-associated nuclear bodies (PML-NBs). The transfer of PML from the nucleoplasm to PML-NBs depends on its phosphorylation and sumoylation. The B1 box and the RING finger are also required for the localization in PML-NBs. Also found in specific membrane structures termed mitochondria-associated membranes (MAMs) which connect the endoplasmic reticulum (ER) and the mitochondria (By similarity). {ECO:0000250}. SUBUNIT: Key component of PML bodies. PML bodies are formed by the interaction of PML homodimers (via SUMO-binding motif) with sumoylated PML, leading to the assembly of higher oligomers. Several types of PML bodies have been observed. PML bodies can form hollow spheres that can sequester target proteins inside. Interacts (via SUMO-binding motif) with sumoylated proteins. Interacts (via C-terminus) with p53/TP53. Recruits p53/TP53 and CHEK2 into PML bodies, which promotes p53/TP53 phosphorylation at 'Ser-20' and prevents its proteasomal degradation. Interacts with MDM2, and sequesters MDM2 in the nucleolus, thereby preventing ubiquitination of p53/TP53. Interaction with PML-RARA oncoprotein and certain viral proteins causes disassembly of PML bodies and abolishes the normal PML function. Interacts with TERT, SIRT1, TOPBP1, TRIM27 and TRIM69. Interacts with ELF4 (via C-terminus). Interacts with Lassa virus Z protein and rabies virus phosphoprotein. Interacts (in the cytoplasm) with TGFBR1, TGFBR2 and PKM. Interacts (via the coiled-coil domain and when sumoylated) with SATB1. Interacts with UBE2I; the interaction is enhanced by arsenic binding. Interacts with SMAD2, SMAD3, DAXX, RPL11, HIPK2 and MTOR. Interacts with ITPR3, PPP1A and RB1. Interacts with RNF4, NLRP3, MAGEA2, RBL2, PER2, E2F4 and MAPK7/BMK1. Interacts with CSNK2A1 and CSNK2A3. Interacts with ANKRD2; the interaction is direct. Interacts with PPARGC1A AND KAT2A. Interacts (via SUMO-interacting motif) with sumoylated MORC3 (By similarity). Interacts with TRIM16. {ECO:0000250|UniProtKB:P29590, ECO:0000269|PubMed:10779416, ECO:0000269|PubMed:12837286, ECO:0000269|PubMed:14645235, ECO:0000269|PubMed:15195100, ECO:0000269|PubMed:16915281, ECO:0000269|PubMed:19136970, ECO:0000269|PubMed:21030605, ECO:0000269|PubMed:22274616, ECO:0000269|PubMed:22886304}. DOMAIN: The coiled-coil domain mediates a strong homo/multidimerization activity essential for core assembly of PML-NBs. {ECO:0000250}.; DOMAIN: Binds arsenic via the RING-type zinc finger. {ECO:0000250}.; DOMAIN: The Sumo interaction motif (SIM) is required for efficient ubiquitination, recruitment of proteasome components within PML-NBs and PML degradation in response to arsenic trioxide. {ECO:0000250}. +B2RXZ1 PNDC1_MOUSE Poly(A)-specific ribonuclease PNLDC1 (EC 3.1.13.4) (PARN-like domain-containing protein 1) (Poly(A)-specific ribonuclease domain-containing protein 1) 531 61,292 Chain (1); Metal binding (4); Transmembrane (1) TRANSMEM 506 526 Helical. {ECO:0000255}. FUNCTION: 3'-exoribonuclease that has a preference for poly(A) tails of mRNAs, thereby efficiently degrading poly(A) tails (PubMed:27515512). Exonucleolytic degradation of the poly(A) tail is often the first step in the decay of eukaryotic mRNAs and is also used to silence certain maternal mRNAs translationally during oocyte maturation and early embryonic development (PubMed:27515512). May act as a regulator of multipotency in embryonic stem cells (PubMed:27515512). {ECO:0000269|PubMed:27515512}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:27515512}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8NA58}. Note=Localizes mainly in the endoplasmic reticulum. {ECO:0000269|PubMed:27515512}. TISSUE SPECIFICITY: Specifically expressed in embryonic stem cells (PubMed:27515512). Highly expressed in testis (PubMed:26919431, PubMed:27515512). {ECO:0000269|PubMed:26919431, ECO:0000269|PubMed:27515512}. +Q9ESG9 PMYT1_MOUSE Membrane-associated tyrosine- and threonine-specific cdc2-inhibitory kinase (EC 2.7.11.1) (Myt1 kinase) 490 54,053 Active site (1); Binding site (1); Chain (1); Compositional bias (1); Domain (1); Metal binding (2); Modified residue (8); Motif (1); Nucleotide binding (1); Region (2); Sequence conflict (4) FUNCTION: Acts as a negative regulator of entry into mitosis (G2 to M transition) by phosphorylation of the CDK1 kinase specifically when CDK1 is complexed to cyclins. Mediates phosphorylation of CDK1 predominantly on 'Thr-14'. Also involved in Golgi fragmentation. May be involved in phosphorylation of CDK1 on 'Tyr-15' to a lesser degree, however tyrosine kinase activity is unclear and may be indirect. May be a downstream target of Notch signaling pathway during eye development (By similarity). {ECO:0000250}. PTM: Autophosphorylated. Phosphorylated by CDC2-CCNB1 complexes on undefined serine and threonine residues. The phosphorylation by CDC2-CCNB1 complexes may inhibit the catalytic activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. SUBUNIT: Interacts with CDC2-CCNB1 complex. Can also interact with PIN1 when phosphorylated by CDC2-CCNB1 (By similarity). {ECO:0000250}. DOMAIN: The membrane-association motif is essential for the localization to membrane of Golgi stack. According to some authors, it is a transmembrane domain; the existence of a transmembrane region of such is however unsure (By similarity). {ECO:0000250}. +Q8K1R3 PNPT1_MOUSE Polyribonucleotide nucleotidyltransferase 1, mitochondrial (EC 2.7.7.8) (3'-5' RNA exonuclease OLD35) (PNPase old-35) (Polynucleotide phosphorylase 1) (PNPase 1) (Polynucleotide phosphorylase-like protein) 783 85,683 Alternative sequence (2); Beta strand (1); Chain (1); Domain (2); Frameshift (1); Helix (3); Modified residue (5); Sequence conflict (5); Transit peptide (1); Turn (1) FUNCTION: RNA-binding protein implicated in numerous RNA metabolic processes. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'-to-5' direction. Mitochondrial intermembrane factor with RNA-processing exoribonulease activity. Component of the mitochondrial degradosome (mtEXO) complex, that degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality in an ATP-dependent manner. Required for correct processing and polyadenylation of mitochondrial mRNAs. Plays a role as a cytoplasmic RNA import factor that mediates the translocation of small RNA components, like the 5S RNA, the RNA subunit of ribonuclease P and the mitochondrial RNA-processing (MRP) RNA, into the mitochondrial matrix. Plays a role in mitochondrial morphogenesis and respiration; regulates the expression of the electron transport chain (ETC) components at the mRNA and protein levels. In the cytoplasm, shows a 3'-to-5' exoribonuclease mediating mRNA degradation activity; degrades c-myc mRNA upon treatment with IFNB1/IFN-beta, resulting in a growth arrest in melanoma cells. Regulates the stability of specific mature miRNAs in melanoma cells; specifically and selectively degrades miR-221, preferentially. Plays also a role in RNA cell surveillance by cleaning up oxidized RNAs. Binds to the RNA subunit of ribonuclease P, MRP RNA and miR-221 microRNA. {ECO:0000269|PubMed:20691904}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Mitochondrion {ECO:0000250}. Mitochondrion intermembrane space {ECO:0000269|PubMed:16966381}; Peripheral membrane protein {ECO:0000269|PubMed:16966381}. SUBUNIT: Homotrimer; in free form. Homooligomer. Component of the mitochondrial degradosome (mtEXO) complex which is a heteropentamer containing 2 copies of SUPV3L1 and 3 copies of PNPT1. Interacts with TCL1A; the interaction has no effect on PNPT1 exonuclease activity (By similarity). {ECO:0000250}. +P97428 RGS16_MOUSE Regulator of G-protein signaling 16 (RGS16) (A28-RGS14P) (Retinal-specific RGS) (RGS-r) (Retinally abundant regulator of G-protein signaling) 201 22,691 Chain (1); Domain (1); Helix (9); Lipidation (2); Modified residue (2); Sequence conflict (4); Turn (2) FUNCTION: Regulates G protein-coupled receptor signaling cascades (PubMed:9079700). Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form (PubMed:10373502). Plays an important role in the phototransduction cascade by regulating the lifetime and effective concentration of activated transducin alpha (PubMed:8917514). May regulate extra and intracellular mitogenic signals. {ECO:0000269|PubMed:10373502, ECO:0000269|PubMed:8917514, ECO:0000305}. PTM: Palmitoylated on Cys-2 and/or Cys-12. {ECO:0000269|PubMed:10373502}.; PTM: Phosphorylated. Phosphorylation at Tyr-167 by EGFR enhances GTPase accelerating (GAP) activity toward GNAI1. {ECO:0000250|UniProtKB:O15492}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10373502}; Lipid-anchor {ECO:0000269|PubMed:10373502}. SUBUNIT: Interacts with GNAI1 and GNAQ (By similarity). Interacts with GNAI3, GNAI3 and GNAO1 (PubMed:9079700, PubMed:18434540). {ECO:0000250|UniProtKB:O15492, ECO:0000269|PubMed:18434540, ECO:0000269|PubMed:9079700}. TISSUE SPECIFICITY: Retinal; also predominantly expressed in the liver and pituitary. +Q63934 PO4F2_MOUSE POU domain, class 4, transcription factor 2 (Brain-specific homeobox/POU domain protein 3B) (Brain-3B) (Brn-3B) (Brn-3.2) 411 43,173 Alternative sequence (1); Chain (1); Compositional bias (3); DNA binding (1); Domain (1); Motif (2); Mutagenesis (1); Region (2); Sequence conflict (1) FUNCTION: Tissue-specific DNA-binding transcription factor involved in the development and differentiation of target cells (PubMed:7904822, PubMed:8995448, PubMed:8972215, PubMed:10357904, PubMed:10414983, PubMed:11163266, PubMed:17668438, PubMed:25775587). Functions either as activator or repressor by modulating the rate of target gene transcription through RNA polymerase II enzyme in a promoter-dependent manner (PubMed:7904822, PubMed:7935408, PubMed:8065921, PubMed:7852360, PubMed:7797498, PubMed:8662774, PubMed:9694219, PubMed:10526314, PubMed:15733064, PubMed:17145718, PubMed:18368538). Binds to the consensus octamer motif 5'-AT[A/T]A[T/A]T[A/T]A-3' of promoter of target genes (PubMed:7904822, PubMed:8290353, PubMed:9111308, PubMed:10414983, PubMed:16152597, PubMed:17668438, PubMed:24643061). Plays a fundamental role in the gene regulatory network essential for retinal ganglion cell (RGC) differentiation (PubMed:8632990, PubMed:10357904, PubMed:25775587). Binds to an octamer site to form a ternary complex with ISL1; cooperates positively with ISL1 and ISL2 to potentiate transcriptional activation of RGC target genes being involved in RGC fate commitment in the developing retina and RGC axon formation and pathfinding (PubMed:8995448, PubMed:9261145, PubMed:8972215, PubMed:10357904, PubMed:11163266, PubMed:24643061, PubMed:25775587). Inhibits DLX1 and DLX2 transcriptional activities preventing DLX1- and DLX2-mediated ability to promote amacrine cell fate specification (PubMed:21875655). In cooperation with TP53 potentiates transcriptional activation of BAX promoter activity increasing neuronal cell apoptosis (PubMed:17145718). Negatively regulates BAX promoter activity in the absence of TP53 (PubMed:17145718). Acts as a transcriptional coactivator via its interaction with the transcription factor ESR1 by enhancing its effect on estrogen response element (ERE)-containing promoter (PubMed:9448000). Antagonizes the transcriptional stimulatory activity of POU4F1 by preventing its binding to an octamer motif (PubMed:7935408, PubMed:8065921, PubMed:8537352, PubMed:7852360, PubMed:8662774). Involved in TNFSF11-mediated terminal osteoclast differentiation (PubMed:17668438). {ECO:0000269|PubMed:10357904, ECO:0000269|PubMed:10414983, ECO:0000269|PubMed:10526314, ECO:0000269|PubMed:11163266, ECO:0000269|PubMed:15733064, ECO:0000269|PubMed:16152597, ECO:0000269|PubMed:17145718, ECO:0000269|PubMed:17668438, ECO:0000269|PubMed:18368538, ECO:0000269|PubMed:21875655, ECO:0000269|PubMed:24643061, ECO:0000269|PubMed:25775587, ECO:0000269|PubMed:7797498, ECO:0000269|PubMed:7852360, ECO:0000269|PubMed:7904822, ECO:0000269|PubMed:7935408, ECO:0000269|PubMed:8065921, ECO:0000269|PubMed:8290353, ECO:0000269|PubMed:8537352, ECO:0000269|PubMed:8632990, ECO:0000269|PubMed:8662774, ECO:0000269|PubMed:8972215, ECO:0000269|PubMed:8995448, ECO:0000269|PubMed:9111308, ECO:0000269|PubMed:9261145, ECO:0000269|PubMed:9448000, ECO:0000269|PubMed:9694219}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17668438}. Nucleus speckle {ECO:0000250|UniProtKB:Q12837}. Cytoplasm {ECO:0000269|PubMed:17668438}. SUBUNIT: Isoform 2: Interacts with POU4F1 isoform 1; this interaction inhibits both POU4F1 DNA-binding and transcriptional activities (PubMed:8537352). Isoform 2: Interacts (C-terminus) with ESR1 (via DNA-binding domain); this interaction increases the estrogen receptor ESR1 transcriptional activity in a DNA- and ligand 17-beta-estradiol-independent manner (PubMed:9448000). Isoform 2: Interacts (via C-terminus) with TP53 (via N-terminus) (PubMed:17145718). Interacts with DLX1 (via homeobox DNA-binding domain); this interaction suppresses DLX1-mediated transcriptional activity in postnatal retina enhancing retinal ganglion cell (RGC) differentiation (PubMed:21875655). Interacts with DLX2 (via homeobox DNA-binding domain); this interaction enhances RGC differentiation (PubMed:21875655). Isoform 1: Interacts (via C-terminus) with ISL1 (via C-terminus) (PubMed:24643061). Isoform 1: Interacts with ISL2 (PubMed:24643061). Isoform 1: Interacts with LHX2 (PubMed:24643061). {ECO:0000269|PubMed:17145718, ECO:0000269|PubMed:21875655, ECO:0000269|PubMed:24643061, ECO:0000269|PubMed:8537352, ECO:0000269|PubMed:9448000}. DOMAIN: The N-terminal transcriptional activation region is sufficient to induce transcriptional activity. {ECO:0000269|PubMed:15733064, ECO:0000269|PubMed:8995448}.; DOMAIN: The POU-specific domain and POU homeodomain regions are necessary for DNA-binding activity and transcriptional repression. {ECO:0000269|PubMed:15733064, ECO:0000269|PubMed:8995448}.; DOMAIN: The polyhistidine motif acts as a targeting signal to nuclear speckles. {ECO:0000250|UniProtKB:Q12837}. TISSUE SPECIFICITY: Expressed in retinal ganglion cells (RGCs) (PubMed:21875655, PubMed:23805044). Expressed in mature osteoclasts (PubMed:17668438). Expressed in cells of layers of the superior colliculus and the adjacent periaqueductal gray (at protein level) (PubMed:7691107). Expressed in the brain, peripheral sensory nervous system and retina (PubMed:7904822). Expressed in the optical, intermediate, and deep gray areas of the superior colliculus, the dorsal column of the mesencephalic and pontine central gray, and the lateral interpeduncular nucleus of the brain (PubMed:7904822). Expressed predominantly in postmitotic, terminally differentiated neurons (PubMed:7904822). Expressed in ganglion cell layer (GCL) of the retina (PubMed:7691107, PubMed:23805044). {ECO:0000269|PubMed:17668438, ECO:0000269|PubMed:21875655, ECO:0000269|PubMed:23805044, ECO:0000269|PubMed:7691107, ECO:0000269|PubMed:7904822}. +P58873 RHBL3_MOUSE Rhomboid-related protein 3 (EC 3.4.21.105) (Ventrhoid transmembrane protein) 404 45,266 Active site (2); Chain (1); Domain (2); Transmembrane (7) TRANSMEM 164 184 Helical. {ECO:0000255}.; TRANSMEM 227 247 Helical. {ECO:0000255}.; TRANSMEM 250 270 Helical. {ECO:0000255}.; TRANSMEM 274 294 Helical. {ECO:0000255}.; TRANSMEM 305 324 Helical. {ECO:0000255}.; TRANSMEM 338 358 Helical. {ECO:0000255}.; TRANSMEM 371 391 Helical. {ECO:0000255}. FUNCTION: May be involved in regulated intramembrane proteolysis and the subsequent release of functional polypeptides from their membrane anchors. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9CTN4 RHBT3_MOUSE Rho-related BTB domain-containing protein 3 (EC 3.6.1.-) 611 69,208 Chain (1); Domain (2); Erroneous initiation (1); Region (2); Sequence caution (1); Sequence conflict (1) FUNCTION: Rab9-regulated ATPase required for endosome to Golgi transport. Involved in transport vesicle docking at the Golgi complex, possibly by participating in release M6PRBP1/TIP47 from vesicles to permit their efficient docking and fusion at the Golgi. Specifically binds Rab9, but not other Rab proteins. Has low intrinsic ATPase activity due to autoinhibition, which is relieved by Rab9 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250}. SUBUNIT: Interacts with RAB9A and RAB9B (at lower level compared to RAB9A-binding). Interacts with M6PRBP1/TIP47 (By similarity). {ECO:0000250}. +Q6PIX5 RHDF1_MOUSE Inactive rhomboid protein 1 (iRhom1) (Epidermal growth factor receptor-related protein) (Rhomboid family member 1) 856 97,292 Alternative sequence (2); Chain (1); Erroneous gene model prediction (1); Erroneous initiation (2); Glycosylation (1); Modified residue (5); Sequence conflict (4); Topological domain (8); Transmembrane (7) TRANSMEM 413 433 Helical. {ECO:0000255}.; TRANSMEM 657 677 Helical. {ECO:0000255}.; TRANSMEM 693 713 Helical. {ECO:0000255}.; TRANSMEM 716 736 Helical. {ECO:0000255}.; TRANSMEM 748 768 Helical. {ECO:0000255}.; TRANSMEM 774 794 Helical. {ECO:0000255}.; TRANSMEM 805 825 Helical. {ECO:0000255}. TOPO_DOM 1 412 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 434 656 Lumenal. {ECO:0000255}.; TOPO_DOM 678 692 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 714 715 Lumenal. {ECO:0000255}.; TOPO_DOM 737 747 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 769 773 Lumenal. {ECO:0000255}.; TOPO_DOM 795 804 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 826 856 Lumenal. {ECO:0000255}. FUNCTION: Rhomboid protease-like protein which has no protease activity but regulates the secretion of several ligands of the epidermal growth factor receptor. Indirectly activates the epidermal growth factor receptor signaling pathway and may thereby regulate sleep, cell survival, proliferation and migration (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q96CC6}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q96CC6}; Multi-pass membrane protein {ECO:0000255}. Note=Predominantly localized in the endoplasmic reticulum membrane. {ECO:0000250|UniProtKB:Q96CC6}. SUBUNIT: Homodimer, or homooligomer. Interacts with TGFA and HBEGF (By similarity). Interacts with EGF; may retain EGF in the endoplasmic reticulum and regulates its degradation through the endoplasmic reticulum-associated degradation (ERAD). {ECO:0000250, ECO:0000269|PubMed:21439629}. TISSUE SPECIFICITY: Expressed in the duodenum, as well as in fetal liver and head. {ECO:0000269|PubMed:8318735}. +Q62009 POSTN_MOUSE Periostin (PN) (Osteoblast-specific factor 2) (OSF-2) 838 93,144 Alternative sequence (3); Chain (1); Disulfide bond (3); Domain (5); Glycosylation (1); Sequence conflict (2); Signal peptide (1) FUNCTION: Induces cell attachment and spreading and plays a role in cell adhesion (PubMed:10404027). Enhances incorporation of BMP1 in the fibronectin matrix of connective tissues, and subsequent proteolytic activation of lysyl oxidase LOX (PubMed:20181949). {ECO:0000269|PubMed:10404027, ECO:0000269|PubMed:20181949}. PTM: Gamma-carboxylation is controversial. Gamma-carboxyglutamated; gamma-carboxyglutamate residues are formed by vitamin K dependent carboxylation; these residues may be required for binding to calcium (PubMed:18450759). According to a more recent report in human, does not contain vitamin K-dependent gamma-carboxyglutamate residues (By similarity). {ECO:0000250|UniProtKB:Q15063, ECO:0000269|PubMed:18450759}. SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:20181949}. Secreted {ECO:0000269|PubMed:10404027, ECO:0000269|PubMed:18450759}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:10404027}. Note=Colocalizes with BMP1 in the Golgi (PubMed:20181949). {ECO:0000269|PubMed:20181949}. SUBUNIT: Interacts with BMP1 and fibronectin (PubMed:20181949). {ECO:0000269|PubMed:20181949}. TISSUE SPECIFICITY: Preferentially expressed in periosteum and periodontal ligament (PubMed:10404027). Also expressed in the developing and adult heart (PubMed:11335131). {ECO:0000269|PubMed:10404027, ECO:0000269|PubMed:11335131}. +Q80WQ6 RHDF2_MOUSE Inactive rhomboid protein 2 (iRhom2) (Rhomboid family member 2) (Rhomboid veinlet-like protein 6) (Rhomboid-related protein) 827 93,434 Chain (1); Modified residue (6); Sequence conflict (1); Topological domain (8); Transmembrane (7) TRANSMEM 382 402 Helical. {ECO:0000255}.; TRANSMEM 628 648 Helical. {ECO:0000255}.; TRANSMEM 664 684 Helical. {ECO:0000255}.; TRANSMEM 687 707 Helical. {ECO:0000255}.; TRANSMEM 719 739 Helical. {ECO:0000255}.; TRANSMEM 745 765 Helical. {ECO:0000255}.; TRANSMEM 774 794 Helical. {ECO:0000255}. TOPO_DOM 1 381 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 403 627 Lumenal. {ECO:0000255}.; TOPO_DOM 649 663 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 685 686 Lumenal. {ECO:0000255}.; TOPO_DOM 708 718 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 740 744 Lumenal. {ECO:0000255}.; TOPO_DOM 766 773 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 795 827 Lumenal. {ECO:0000255}. FUNCTION: Rhomboid protease-like protein which has no protease activity but regulates the secretion of several ligands of the epidermal growth factor receptor. Indirectly activates the epidermal growth factor receptor signaling pathway and may thereby regulate sleep, cell survival, proliferation and migration. {ECO:0000269|PubMed:21439629}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21439629}; Multi-pass membrane protein {ECO:0000269|PubMed:21439629}. SUBUNIT: Interacts with EGF. {ECO:0000269|PubMed:21439629}. +Q921J2 RHEB_MOUSE GTP-binding protein Rheb (Ras homolog enriched in brain) 184 20,451 Beta strand (6); Binding site (1); Chain (1); Helix (5); Lipidation (1); Metal binding (2); Modified residue (2); Motif (1); Mutagenesis (2); Nucleotide binding (4); Propeptide (1) FUNCTION: Activates the protein kinase activity of mTORC1, and thereby plays a role in the regulation of apoptosis. Stimulates the phosphorylation of S6K1 and EIF4EBP1 through activation of mTORC1 signaling. Has low intrinsic GTPase activity. {ECO:0000269|PubMed:24648513, ECO:0000305}. PTM: Farnesylation is important for efficiently activating mTORC1-mediated signaling. {ECO:0000250|UniProtKB:Q62639}.; PTM: Phosphorylation by MAPKAPK5 impairs GTP-binding and inactivation. {ECO:0000269|PubMed:21336308}. SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250|UniProtKB:Q15382}; Lipid-anchor {ECO:0000250|UniProtKB:Q15382}; Cytoplasmic side {ECO:0000250|UniProtKB:Q15382}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q15382}; Lipid-anchor {ECO:0000250|UniProtKB:Q15382}; Cytoplasmic side {ECO:0000250|UniProtKB:Q15382}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q15382}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q15382}; Lipid-anchor {ECO:0000250|UniProtKB:Q15382}; Cytoplasmic side {ECO:0000250|UniProtKB:Q15382}. SUBUNIT: Binds to mTORC1 in a guanyl nucleotide-independent manner. Interacts directly with MTOR, MLST8 and RPTOR. Interacts with TSC2 (By similarity). Interacts (when prenylated) with PDE6D; this promotes release from membranes (By similarity). {ECO:0000250|UniProtKB:Q15382}. +Q9R0Z9 RHG07_MOUSE Rho GTPase-activating protein 7 (Deleted in liver cancer 1 protein homolog) (DLC-1) (Rho-type GTPase-activating protein 7) (START domain-containing protein 12) (StARD12) (StAR-related lipid transfer protein 12) 1092 123,367 Alternative sequence (1); Chain (1); Compositional bias (2); Domain (3); Erroneous initiation (1); Modified residue (4); Region (2); Sequence conflict (10) FUNCTION: Functions as a GTPase-activating protein for the small GTPases RHOA, RHOB, RHOC and CDC42, terminating their downstream signaling. This induces morphological changes and detachment through cytoskeletal reorganization, playing a critical role in biological processes such as cell migration and proliferation. Also functions in vivo as an activator of the phospholipase PLCD1. Active DLC1 increases cell migration velocity but reduces directionality (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell junction, focal adhesion {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Colocalizes with EF1A1 at actin-rich regions in the cell periphery. {ECO:0000250}. SUBUNIT: Interacts with EF1A1, facilitates EF1A1 distribution to the membrane periphery and ruffles upon growth factor stimulation and suppresses cell migration. {ECO:0000250}. DOMAIN: The SAM domain mediates interaction with EF1A1, and functions as an autoinhibitory regulator of RhoGAP Activity. {ECO:0000250}.; DOMAIN: The polybasic cluster is required for activation and mediates binding to phosphatidylinositol-4,5-bisphosphate (PI(4,5)P(2)) containing membranes. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed with the highest levels in heart, liver and lung. +Q9CXP4 RHG08_MOUSE Rho GTPase-activating protein 8 (Rho-type GTPase-activating protein 8) 425 48,972 Chain (1); Domain (2); Erroneous initiation (1); Sequence conflict (2) FUNCTION: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in skeletal muscle, lung and testis, and at lower levels in kidney, stomach and colon. Not detected in heart, liver, spleen, breast, brain, neonatal head or pancreas. {ECO:0000269|PubMed:15225876}. +Q8C0D4 RHG12_MOUSE Rho GTPase-activating protein 12 (Rho-type GTPase-activating protein 12) 838 95,352 Chain (1); Domain (5); Modified residue (9); Sequence conflict (5) FUNCTION: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. {ECO:0000250}. +Q811M1 RHG15_MOUSE Rho GTPase-activating protein 15 (ArhGAP15) (Rho-type GTPase-activating protein 15) 481 55,339 Alternative sequence (5); Chain (1); Domain (2); Erroneous initiation (1); Modified residue (5); Sequence conflict (1) FUNCTION: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. Has activity toward RAC1. Overexpression results in an increase in actin stress fibers and cell contraction (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. DOMAIN: The PH domain is required for localization to the membrane. {ECO:0000250}. +Q3UIA2 RHG17_MOUSE Rho GTPase-activating protein 17 (Neuron-associated developmentally-regulated protein) (Nadrin) (Rho-type GTPase-activating protein 17) 846 92,202 Alternative sequence (3); Chain (1); Compositional bias (2); Domain (2); Modified residue (9); Motif (1); Sequence conflict (6) FUNCTION: Rho GTPase-activating protein involved in the maintenance of tight junction by regulating the activity of CDC42, thereby playing a central role in apical polarity of epithelial cells. Specifically acts as a GTPase activator for the CDC42 GTPase by converting it to an inactive GDP-bound state. The complex formed with AMOT acts by regulating the uptake of polarity proteins at tight junctions, possibly by deciding whether tight junction transmembrane proteins are recycled back to the plasma membrane or sent elsewhere. Participates in the Ca(2+)-dependent regulation of exocytosis, possibly by catalyzing GTPase activity of Rho family proteins and by inducing the reorganization of the cortical actin filaments. Acts as a GTPase activator in vitro for RAC1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell junction, tight junction {ECO:0000250}. Note=Associates with membranes and concentrates at sites of cell-cell contact. {ECO:0000250}. SUBUNIT: Component of a complex whose core is composed of ARHGAP17, AMOT, MPP5/PALS1, PATJ and PARD3/PAR3. Interacts with SLC9A3R1, FNBP1, TRIP10, CAPZA (CAPZA1, CAPZA2 or CAPZA3), CAPZB, CD2AP and SH3KBP1/CIN85 (By similarity). {ECO:0000250}. DOMAIN: The BAR domain mediates the interaction with the coiled coil domain of AMOT, leading to its recruitment to tight junctions. {ECO:0000250}. +Q8K0Q5 RHG18_MOUSE Rho GTPase-activating protein 18 (Rho-type GTPase-activating protein 18) 663 74,930 Chain (1); Domain (1); Modified residue (6); Sequence conflict (2) FUNCTION: Rho GTPase activating protein that suppresses F-actin polymerization by inhibiting Rho. Rho GTPase activating proteins act by converting Rho-type GTPases to an inactive GDP-bound state. Plays a key role in tissue tension and 3D tissue shape by regulating cortical actomyosin network formation. Acts downstream of YAP1 and inhibits actin polymerization, which in turn reduces nuclear localization of YAP1. Regulates cell shape, spreading, and migration (By similarity). {ECO:0000250|UniProtKB:Q8N392}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8N392}. SUBUNIT: Interacts with MPHOSPH6. {ECO:0000250|UniProtKB:Q8N392}. TISSUE SPECIFICITY: Widely expressed: expressed in most organs, except small intestine. {ECO:0000269|PubMed:21865595}. +B2RQE8 RHG42_MOUSE Rho GTPase-activating protein 42 (Rho-type GTPase-activating protein 42) 841 94,636 Chain (1); Coiled coil (1); Compositional bias (1); Domain (4); Modified residue (7) FUNCTION: May influence blood pressure by functioning as a GTPase-activating protein for RHOA in vascular smooth muscle. {ECO:0000269|PubMed:24335996}. TISSUE SPECIFICITY: Highly and selectively expressed in smooth muscle cells. {ECO:0000269|PubMed:24335996}. +Q91VC7 PP14A_MOUSE Protein phosphatase 1 regulatory subunit 14A (17 kDa PKC-potentiated inhibitory protein of PP1) (Protein kinase C-potentiated inhibitor protein of 17 kDa) (CPI-17) 147 16,649 Chain (1); Modified residue (5); Region (1); Sequence conflict (2) FUNCTION: Inhibitor of PPP1CA. Has over 1000-fold higher inhibitory activity when phosphorylated, creating a molecular switch for regulating the phosphorylation status of PPP1CA substrates and smooth muscle contraction (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +Q62084 PP14B_MOUSE Protein phosphatase 1 regulatory subunit 14B (Phosphatase holoenzyme inhibitor 1) (PHI-1) (Phospholipase C-beta-3 neighbouring gene protein) 147 15,957 Chain (1); Coiled coil (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (5); Mutagenesis (1) FUNCTION: Inhibitor of PPP1CA. Has over 50-fold higher inhibitory activity when phosphorylated. {ECO:0000269|PubMed:10606530, ECO:0000269|PubMed:12144526}. PTM: Phosphorylated primarily on Thr-57 by PKC (in vitro). An unknown Ser is also phosphorylated by PKC (in vitro). {ECO:0000269|PubMed:10606530, ECO:0000269|PubMed:12144526}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. TISSUE SPECIFICITY: Ubiquitous. Highly expressed in testis. Detected at low levels in the other tissues tested. Highly expressed in cardiac muscle, bladder and aorta (at protein level). {ECO:0000269|PubMed:10606530, ECO:0000269|PubMed:8670283}. +Q80Y19 RHGBA_MOUSE Rho GTPase-activating protein 11A (Rho-type GTPase-activating protein 11A) 987 108,436 Chain (1); Domain (1); Erroneous initiation (1); Modified residue (13); Sequence conflict (4) +Q8R3G1 PP1R8_MOUSE Nuclear inhibitor of protein phosphatase 1 (NIPP-1) (Protein phosphatase 1 regulatory inhibitor subunit 8) 351 38,528 Beta strand (10); Chain (1); Compositional bias (2); Domain (1); Modified residue (7); Motif (2); Region (7); Turn (1) FUNCTION: Inhibitor subunit of the major nuclear protein phosphatase-1 (PP-1). It has RNA-binding activity but does not cleave RNA and may target PP-1 to RNA-associated substrates. May also be involved in pre-mRNA splicing. Binds DNA and might act as a transcriptional repressor. Essential for cell proliferation and early embryonic development. {ECO:0000269|PubMed:15199142, ECO:0000269|PubMed:15501817}. PTM: May be inactivated by phosphorylation on Ser-199 or Ser-204. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus speckle {ECO:0000250}. Note=Mainly, but not exclusively, nuclear. SUBUNIT: Interacts with phosphorylated CDC5L, SF3B1 and MELK. Part of the spliceosome. Interacts with PPP1CA, PPP1CB and PPP1CC (By similarity). Interacts with EED. Part of a complex consisting of PPP1R8, EED, HDAC2 and PP-1. {ECO:0000250, ECO:0000269|PubMed:12788942, ECO:0000269|PubMed:18253837}. DOMAIN: Has a basic N- and C-terminal and an acidic central domain. {ECO:0000269|PubMed:18253837}.; DOMAIN: The FHA domain mediates interactions with threonine-phosphorylated MELK. {ECO:0000269|PubMed:18253837}. +Q62159 RHOC_MOUSE Rho-related GTP-binding protein RhoC (Silica-induced gene 61 protein) (SIG-61) 193 22,006 Chain (1); Lipidation (1); Modified residue (1); Motif (1); Nucleotide binding (3); Propeptide (1); Sequence conflict (1) FUNCTION: Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Serves as a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Regulates apical junction formation in bronchial epithelial cells. {ECO:0000269|PubMed:20974804}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cleavage furrow {ECO:0000250}. Note=Translocates to the equatorial region before furrow formation in a ECT2-dependent manner. {ECO:0000250}. SUBUNIT: Interacts with RTKN (PubMed:8662891). Interacts with AKAP13. Interacts with DIAPH1 (By similarity). Interacts with PKN2 (PubMed:20974804). Interacts with ROCK1 and ROCK2. Interacts with ARHGDIA. Interacts with RIPOR1 (By similarity). {ECO:0000250|UniProtKB:P08134, ECO:0000269|PubMed:20974804, ECO:0000269|PubMed:8662891}. +Q8BYP3 RHOF_MOUSE Rho-related GTP-binding protein RhoF 211 23,577 Chain (1); Lipidation (1); Modified residue (2); Motif (1); Nucleotide binding (3); Propeptide (1) FUNCTION: Plasma membrane-associated small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. Causes the formation of thin, actin-rich surface projections called filopodia. Functions cooperatively with CDC42 and Rac to generate additional structures, increasing the diversity of actin-based morphology (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm, cytoskeleton. +P84096 RHOG_MOUSE Rho-related GTP-binding protein RhoG (Sid 10750) 191 21,309 Chain (1); Lipidation (1); Modified residue (3); Motif (1); Nucleotide binding (3); Propeptide (1) FUNCTION: Required for the formation of membrane ruffles during macropinocytosis. Plays a role in cell migration and is required for the formation of cup-like structures during trans-endothelial migration of leukocytes (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. SUBUNIT: Interacts with ARHGEF26. Interacts with ARHGEF16 (By similarity). {ECO:0000250}. +P63330 PP2AA_MOUSE Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform (PP2A-alpha) (EC 3.1.3.16) 309 35,608 Active site (1); Chain (1); Metal binding (7); Modified residue (2); Mutagenesis (2); Sequence conflict (2) FUNCTION: PP2A is the major phosphatase for microtubule-associated proteins (MAPs). PP2A can modulate the activity of phosphorylase B kinase casein kinase 2, mitogen-stimulated S6 kinase, and MAP-2 kinase. Cooperates with SGO2 to protect centromeric cohesin from separase-mediated cleavage in oocytes specifically during meiosis I. Activates RAF1 by dephosphorylating it at 'Ser-259' (By similarity). {ECO:0000250, ECO:0000269|PubMed:18084284}. PTM: Reversibly methyl esterified on Leu-309 by leucine carboxyl methyltransferase 1 (Lcmt1) and protein phosphatase methylesterase 1 (Ppme1). Carboxyl methylation influences the affinity of the catalytic subunit for the different regulatory subunits, thereby modulating the PP2A holoenzyme's substrate specificity, enzyme activity and cellular localization. {ECO:0000269|PubMed:10441131}.; PTM: Phosphorylation of either threonine (by autophosphorylation-activated protein kinase) or tyrosine results in inactivation of the phosphatase. Auto-dephosphorylation has been suggested as a mechanism for reactivation. {ECO:0000269|PubMed:7510677}.; PTM: Polyubiquitinated, leading to its degradation by the proteasome (By similarity). May be monoubiquitinated by NOSIP. {ECO:0000250|UniProtKB:P67775, ECO:0000269|PubMed:25546391}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18084284}. Nucleus {ECO:0000250}. Chromosome, centromere {ECO:0000269|PubMed:18084284}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. Note=In prometaphase cells, but not in anaphase cells, localizes at centromeres. During mitosis, also found at spindle poles (By similarity). Centromeric localization requires the presence of SGO2. {ECO:0000250}. SUBUNIT: PP2A consists of a common heterodimeric core enzyme, composed of PPP2CA a 36 kDa catalytic subunit (subunit C) and PPP2R1A a 65 kDa constant regulatory subunit (PR65 or subunit A), that associates with a variety of regulatory subunits. Proteins that associate with the core dimer include three families of regulatory subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa variable regulatory subunit, viral proteins, and cell signaling molecules. Interacts with NXN; the interaction is direct. Interacts with TP53, SGO1 and SGO2. Interacts with AXIN1; the interaction dephosphorylates AXIN1 (By similarity). Interacts with PIM3; this interaction promotes dephosphorylation, ubiquitination and proteasomal degradation of PIM3 (By similarity). Interacts with RAF1. Interacts with GSK3B (via C2 domain) (By similarity). Interaction with IGBP1 protects unassembled PPP2CA from degradative ubiquitination (By similarity). Interacts with KCTD20 (PubMed:24156551). Interacts with BTBD10 (PubMed:18160256). Interacts with MFHAS1; retains PPP2CA into the cytoplasm and excludes it from the nucleus (By similarity). Interacts with FAM122A (By similarity). Interacts with ADCY8; interaction is phosphatase activity-dependent; antagonizes interaction between ADCY8 and calmodulin (PubMed:16258073). {ECO:0000250|UniProtKB:P67775, ECO:0000269|PubMed:16258073, ECO:0000269|PubMed:18160256, ECO:0000269|PubMed:24156551}. +P62715 PP2AB_MOUSE Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform (PP2A-beta) (EC 3.1.3.16) 309 35,575 Active site (1); Chain (1); Metal binding (7); Modified residue (2); Mutagenesis (3) FUNCTION: PP2A can modulate the activity of phosphorylase B kinase casein kinase 2, mitogen-stimulated S6 kinase, and MAP-2 kinase. PTM: Reversibly methyl esterified on Leu-309 by leucine carboxyl methyltransferase 1 (Lcmt1) and protein phosphatase methylesterase 1 (Ppme1). Carboxyl methylation influences the affinity of the catalytic subunit for the different regulatory subunits, thereby modulating the PP2A holoenzyme's substrate specificity, enzyme activity and cellular localization (By similarity). {ECO:0000250}.; PTM: Phosphorylation of either threonine (by autophosphorylation-activated protein kinase) or tyrosine results in inactivation of the phosphatase. Auto-dephosphorylation has been suggested as a mechanism for reactivation (By similarity). {ECO:0000250}.; PTM: May be monoubiquitinated by NOSIP. {ECO:0000269|PubMed:25546391}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}. Chromosome, centromere {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. Note=In prometaphase cells, but not in anaphase cells, localizes at centromeres. During mitosis, also found at spindle poles (By similarity). {ECO:0000250}. SUBUNIT: PP2A consists of a common heterodimeric core enzyme (composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant regulatory subunit (PR65) (subunit A)) that associates with a variety of regulatory subunits. Proteins that associate with the core dimer include three families of regulatory subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa variable regulatory subunit, viral proteins, and cell signaling molecules. Binds PPME1. May indirectly interact with SGO1, most probably through regulatory B56 subunits. Found in a complex with at least ARL2, PPP2CB, PPP2R1A, PPP2R2A, PPP2R5E and TBCD. Interacts with TBCD. Interacts with CTTNBP2NL. Interacts with PTPA. {ECO:0000250|UniProtKB:P62714, ECO:0000250|UniProtKB:Q0P594}. +P63328 PP2BA_MOUSE Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform (EC 3.1.3.16) (CAM-PRP catalytic subunit) (Calmodulin-dependent calcineurin A subunit alpha isoform) (CNA alpha) 521 58,644 Active site (1); Alternative sequence (1); Beta strand (15); Chain (1); Helix (16); Initiator methionine (1); Metal binding (7); Modified residue (4); Motif (1); Mutagenesis (5); Region (6); Site (1); Turn (6) FUNCTION: Calcium-dependent, calmodulin-stimulated protein phosphatase which plays an essential role in the transduction of intracellular Ca(2+)-mediated signals (PubMed:7791792, PubMed:26794871). Many of the substrates contain a PxIxIT motif and/or a LxVP motif (By similarity). In response to increased Ca(2+) levels, dephosphorylates and activates phosphatase SSH1 which results in cofilin dephosphorylation (By similarity). In response to increased Ca(2+) levels following mitochondrial depolarization, dephosphorylates DNM1L inducing DNM1L translocation to the mitochondrion (By similarity). Dephosphorylates heat shock protein HSPB1 (By similarity). Dephosphorylates and activates transcription factor NFATC1 (By similarity). Dephosphorylates and inactivates transcription factor ELK1 (By similarity). Dephosphorylates DARPP32 (By similarity). {ECO:0000250|UniProtKB:P48452, ECO:0000250|UniProtKB:Q08209, ECO:0000269|PubMed:26794871, ECO:0000269|PubMed:7791792}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q08209}. Cell membrane {ECO:0000250|UniProtKB:Q08209}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q08209}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P63329}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:P63329}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:Q08209}. Note=Colocalizes with ACTN1 and MYOZ2 at the Z line in heart and skeletal muscle. Recruited to the cell membrane by scaffold protein AKAP5 following L-type Ca(2+)-channel activation. {ECO:0000250|UniProtKB:P63329, ECO:0000250|UniProtKB:Q08209}. SUBUNIT: Forms a complex composed of a calmodulin-dependent catalytic subunit (also known as calcineurin A) and a regulatory Ca(2+)-binding subunit (also known as calcineurin B) (PubMed:26794871). There are three catalytic subunits, each encoded by a separate gene (PPP3CA, PPP3CB, and PPP3CC) and two regulatory subunits which are also encoded by separate genes (PPP3R1 and PPP3R2). In response to an increase in Ca(2+) intracellular levels, forms a complex composed of PPP3CA/calcineurin A, calcineurin B and calmodulin (By similarity). Interacts (via calcineurin B binding domain) with regulatory subunit PPP3R1/calcineurin B (PubMed:26794871). Interacts (via calmodulin-binding domain) with calmodulin; the interaction depends on calmodulin binding to Ca(2+) (By similarity). Forms a complex composed of MYOZ2 and ACTN1 (PubMed:11114196). Within the complex interacts with MYOZ2 (PubMed:11114196). Interacts with MYOZ1 (PubMed:11114196). Interacts with MYOZ3 (By similarity). Interacts with CIB1; the interaction increases upon cardiomyocyte hypertrophy (PubMed:20639889). Interacts with CHP1 and CHP2 (By similarity). Interacts with CRTC2 (By similarity). Interacts with DNM1L; the interaction dephosphorylates DNM1L and promotes its translocation to mitochondria (By similarity). Interacts with CMYA5; this interaction represses calcineurin activity in muscle (PubMed:21427212). Interacts (constitutively active form) with SYNPO2 (By similarity). Interacts with scaffold protein AKAP5 (via IAIIIT motif); the interaction recruits PPP3CA to the plasma membrane following L-type Ca(2+)-channel activation (By similarity). Interacts with NFATC2 (By similarity). Interacts with RCAN3 (By similarity). Interacts with PPIA (By similarity). Interacts with RCAN1 (PubMed:12809556). {ECO:0000250|UniProtKB:P48452, ECO:0000250|UniProtKB:P63329, ECO:0000250|UniProtKB:Q08209, ECO:0000269|PubMed:11114196, ECO:0000269|PubMed:12809556, ECO:0000269|PubMed:20639889, ECO:0000269|PubMed:21427212, ECO:0000269|PubMed:26794871}. DOMAIN: The autoinhibitory domain prevents access to the catalytic site. {ECO:0000269|PubMed:26794871}.; DOMAIN: The autoinhibitory segment prevents access to the substrate binding site. {ECO:0000269|PubMed:26794871}.; DOMAIN: Possible isomerization of Pro-309 within the SAPNY motif triggers a conformation switch which affects the organization and thus accessibility of the active site and the substrate binding region (PxIxIF motif). The trans- to cis-transition may favor calcineurin A activation and substrate binding. The reverse cis- to trans-transition may be enhanced by peptidyl-prolyl isomerases such as PPIA. {ECO:0000250|UniProtKB:Q08209}. +Q3TWL2 PP4P1_MOUSE Type 1 phosphatidylinositol 4,5-bisphosphate 4-phosphatase (Type 1 PtdIns-4,5-P2 4-Ptase) (EC 3.1.3.78) (PtdIns-4,5-P2 4-Ptase I) (Transmembrane protein 55B) 284 30,047 Active site (1); Chain (1); Compositional bias (1); Modified residue (1); Motif (1); Transmembrane (2) TRANSMEM 219 239 Helical. {ECO:0000255}.; TRANSMEM 246 266 Helical. {ECO:0000255}. FUNCTION: Catalyzes the hydrolysis of the 4-position phosphate of phosphatidylinositol 4,5-bisphosphate. Does not hydrolyze phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 3,4-bisphosphate, inositol 3,5-bisphosphate, inositol 3,4-bisphosphate, phosphatidylinositol 5-monophosphate, phosphatidylinositol 4-monophosphate and phosphatidylinositol 3-monophosphate (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Lysosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q9CZX7 PP4P2_MOUSE Type 2 phosphatidylinositol 4,5-bisphosphate 4-phosphatase (Type 2 PtdIns-4,5-P2 4-Ptase) (EC 3.1.3.78) (PtdIns-4,5-P2 4-Ptase II) (Transmembrane protein 55A) 257 28,038 Active site (1); Chain (1); Modified residue (2); Motif (1); Transmembrane (2) TRANSMEM 192 212 Helical. {ECO:0000255}.; TRANSMEM 227 247 Helical. {ECO:0000255}. FUNCTION: Catalyzes the hydrolysis of the 4-position phosphate of phosphatidylinositol 4,5-bisphosphate. Does not hydrolyze phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 3,4-bisphosphate, inositol 3,5-bisphosphate, inositol 3,4-bisphosphate, phosphatidylinositol 5-monophosphate, phosphatidylinositol 4-monophosphate and phosphatidylinositol 3-monophosphate (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Lysosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q8K2V1 PP4R1_MOUSE Serine/threonine-protein phosphatase 4 regulatory subunit 1 951 106,298 Alternative sequence (1); Chain (1); Modified residue (1); Repeat (12); Sequence conflict (4) FUNCTION: Regulatory subunit of serine/threonine-protein phosphatase 4. May play a role in regulation of cell division in renal glomeruli. The PPP4C-PPP4R1 PP4 complex may play a role in dephosphorylation and regulation of HDAC3 (By similarity). {ECO:0000250}. SUBUNIT: Serine/threonine-protein phosphatase 4 (PP4) occurs in different assemblies of the catalytic and one or more regulatory subunits. Component of the PP4 complex PPP4C-PPP4R1. Interacts with HDAC3 (By similarity). {ECO:0000250}. +Q0VGB7 PP4R2_MOUSE Serine/threonine-protein phosphatase 4 regulatory subunit 2 417 46,479 Chain (1); Compositional bias (1); Modified residue (2); Sequence conflict (5) FUNCTION: Regulatory subunit of serine/threonine-protein phosphatase 4 (PP4). May regulate the activity of PPP4C at centrosomal microtubule organizing centers. Its interaction with the SMN complex leads to enhance the temporal localization of snRNPs, suggesting a role of PPP4C in maturation of spliceosomal snRNPs. The PPP4C-PPP4R2-PPP4R3A PP4 complex specifically dephosphorylates H2AFX phosphorylated on 'Ser-140' (gamma-H2AFX) generated during DNA replication and required for DNA double strand break repair (By similarity). Mediates RPA2 dephosphorylation by recruiting PPP4C to RPA2 in a DNA damage-dependent manner. RPA2 dephosphorylation is required for the efficient RPA2-mediated recruitment of RAD51 to chromatin following double strand breaks, an essential step for DNA repair (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Nucleus {ECO:0000250}. Note=Ionizing radiation induces relocalization to nuclear foci and colocalization with RPA2. {ECO:0000250}. SUBUNIT: Serine/threonine-protein phosphatase 4 (PP4) occurs in different assemblies of the catalytic and one or more regulatory subunits. Component of the PP4 complexes PPP4C-PPP4R2, PPP4C-PPP4R2-PPP4R3A and PPP4C-PPP4R2-PPP4R3B. The PPP4C-PPP4R2 complex appears to be a tetramer composed of 2 molecules of PPP4C and 2 molecules of PPP4R2. Interacts with DDX20/GEMIN3 and GEMIN4 (By similarity). Interacts with RPA2; this DNA damage-dependent interaction recruits PPP4C leading to RPA2 dephosphorylation (By similarity). {ECO:0000250}. +Q8C0Y0 PP4R4_MOUSE Serine/threonine-protein phosphatase 4 regulatory subunit 4 875 99,481 Alternative sequence (3); Chain (1); Coiled coil (1); Modified residue (2); Repeat (2); Sequence caution (1); Sequence conflict (3) FUNCTION: Putative regulatory subunit of serine/threonine-protein phosphatase 4. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Serine/threonine-protein phosphatase 4 (PP4) occurs in different assemblies of the catalytic and one or more regulatory subunits. Component of the PP4 complex PPP4C-PPP4R4 (By similarity). {ECO:0000250}. +Q8BPM6 RIC3_MOUSE Protein RIC-3 (Resistant to inhibitor of cholinesterase 3) 367 40,283 Alternative sequence (3); Chain (1); Coiled coil (1); Compositional bias (1); Cross-link (1); Modified residue (1); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 96 116 Helical. {ECO:0000255}. TOPO_DOM 32 95 Lumenal. {ECO:0000255}.; TOPO_DOM 117 367 Cytoplasmic. {ECO:0000255}. FUNCTION: Promotes functional expression of homomeric alpha-7 and alpha-8 nicotinic acetylcholine receptors at the cell surface. May also promote functional expression of homomeric serotoninergic 5-HT3 receptors, and of heteromeric acetylcholine receptors alpha-3/beta-2, alpha-3/beta-4, alpha-4/beta-2 and alpha-4/beta-4. {ECO:0000269|PubMed:19812337}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19812337}; Single-pass membrane protein {ECO:0000269|PubMed:19812337}. SUBUNIT: Monomer and homodimer. Interacts with CHRNA7, CHRNA3, CHRNA4, CHRNB2, CHRNB4 and HTR3A (By similarity). {ECO:0000250}. DOMAIN: The coiled-coil domain mediates transient homodimerization with other acetylcholine receptor-bound RIC3 molecules, promoting stepwise ACHR homomeric assembly at the membrane. TISSUE SPECIFICITY: Expressed in brain, with highest levels in hippocampus, cerebellum and superior colliculus. {ECO:0000269|PubMed:12821669}. +Q7TSI3 PP6R1_MOUSE Serine/threonine-protein phosphatase 6 regulatory subunit 1 (SAPS domain family member 1) 856 94,527 Chain (1); Compositional bias (1); Modified residue (10); Region (1); Sequence caution (1); Sequence conflict (2) FUNCTION: Regulatory subunit of protein phosphatase 6 (PP6). May function as a scaffolding PP6 subunit. Involved in the PP6-mediated dephosphorylation of NFKBIE opposing its degradation in response to TNF-alpha (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Protein phosphatase 6 (PP6) holoenzyme is proposed to be a heterotrimeric complex formed of the catalytic subunit, a SAPS domain-containing subunit (PP6R) and an ankyrin repeat-domain containing regulatory subunit (ARS). Interacts with PPP6C and NFKBIE. Interacts with ANKRD28, ANKRD44 and ANKRD52 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous with highest expression in lung, spleen and bladder. {ECO:0000269|PubMed:16769727}. +Q3TIR3 RIC8A_MOUSE Synembryn-A (Protein Ric-8A) 530 59,847 Chain (1); Modified residue (7); Sequence conflict (3) FUNCTION: Guanine nucleotide exchange factor (GEF), which can activate some, but not all, G-alpha proteins. Able to activate GNAI1, GNAO1 and GNAQ, but not GNAS by exchanging bound GDP for free GTP. Involved in regulation of microtubule pulling forces during mitotic movement of chromosomes by stimulating G(i)-alpha protein, possibly leading to release G(i)-alpha-GTP and NuMA proteins from the NuMA-GPSM2-G(i)-alpha-GDP complex. Also acts as an activator for G(q)-alpha (GNAQ) protein by enhancing the G(q)-coupled receptor-mediated ERK activation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Colocalizes with GNAI1 and RGS14 at the plasma membrane (By similarity). Colocalizes with RIC8A in CA2 hippocampal neurons. {ECO:0000250, ECO:0000269|PubMed:21158412}. SUBUNIT: Interacts with GDP-bound G alpha proteins GNAI1, GNAO1 and GNAQ, and with GNA13 with lower affinity. Does not interact with G-alpha proteins when they are in complex with subunits beta and gamma. Interacts (via C-terminus) with RGS14; the interaction stimulates the dissociation of the complex between RGS14 and the active GTP-bound form of GNAI1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in neurons and neurites of the CA1 and CA2 subregions of the hippocampus (at protein level). In adult brain, it is expressed in the neocortex, hippocampus and cerebellum as well as in the pineal gland and ependymal layer. {ECO:0000269|PubMed:12971991, ECO:0000269|PubMed:21158412}. +Q80XE1 RIC8B_MOUSE Synembryn-B (Protein Ric-8B) 520 58,683 Alternative sequence (1); Chain (1); Modified residue (2) FUNCTION: Guanine nucleotide exchange factor (GEF), which can activate some, but not all, G-alpha proteins by exchanging bound GDP for free GTP (By similarity). Able to potentiate G(olf)-alpha-dependent cAMP accumulation suggesting that it may be an important component for odorant signal transduction. {ECO:0000250, ECO:0000269|PubMed:15829631}. SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000250}. Note=Localizes to the cell cortex. {ECO:0000250}. SUBUNIT: Interacts with GDP-bound G alpha proteins GNAI1, GNAL, GNAS and GNAQ. Does not interact with G-alpha proteins when they are in complex with subunits beta and gamma. {ECO:0000269|PubMed:15829631}. TISSUE SPECIFICITY: Predominantly expressed in the mature olfactory sensory neurons and also in a few regions in the brain. {ECO:0000269|PubMed:15829631}. +Q6QI06 RICTR_MOUSE Rapamycin-insensitive companion of mTOR (AVO3 homolog) (mAVO3) (Protein pianissimo) 1708 191,570 Alternative sequence (1); Chain (1); Modified residue (19); Region (1); Sequence conflict (4) FUNCTION: Subunit of mTORC2, which regulates cell growth and survival in response to hormonal signals. mTORC2 is activated by growth factors, but, in contrast to mTORC1, seems to be nutrient-insensitive. mTORC2 seems to function upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors. mTORC2 promotes the serum-induced formation of stress-fibers or F-actin. mTORC2 plays a critical role in AKT1 'Ser-473' phosphorylation, which may facilitate the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1 which is a prerequisite for full activation. mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422'. mTORC2 also modulates the phosphorylation of PRKCA on 'Ser-657'. Plays an essential role in embryonic growth and development. {ECO:0000269|PubMed:16221682, ECO:0000269|PubMed:16962653, ECO:0000269|PubMed:16962829, ECO:0000269|PubMed:17141160}. PTM: Phosphorylated by MTOR; when part of mTORC2. Phosphorylated at Thr-1135 by RPS6KB1; phosphorylation of RICTOR inhibits mTORC2 and AKT1 signaling (By similarity). {ECO:0000250}. SUBUNIT: Part of the mammalian target of rapamycin complex 2 (mTORC2) which contains MTOR, MLST8, PRR5, RICTOR, MAPKAP1 and DEPTOR (PubMed:15467718, PubMed:16962829, PubMed:16962653). Contrary to mTORC1, mTORC2 does not bind to and is not sensitive to FKBP12-rapamycin. Binds directly to MTOR and PRR5 within the TORC2 complex. Interacts with CCDC28B. Interacts with NBN. Interacts with PRR5L (By similarity). {ECO:0000250|UniProtKB:Q6R327, ECO:0000269|PubMed:15467718, ECO:0000269|PubMed:16962653, ECO:0000269|PubMed:16962829}. +Q05117 PPA5_MOUSE Tartrate-resistant acid phosphatase type 5 (TR-AP) (EC 3.1.3.2) (Tartrate-resistant acid ATPase) (TrATPase) (Type 5 acid phosphatase) 327 36,807 Chain (1); Disulfide bond (1); Glycosylation (2); Metal binding (8); Signal peptide (1) FUNCTION: May play a role in the process of bone resorption. The osteoclastic trap acts on nucleotide tri- and diphosphates with higher affinity, compared with other substrates. SUBCELLULAR LOCATION: Lysosome. SUBUNIT: Exists either as monomer or, after proteolytic processing, as a dimer of two chains linked by disulfide bond(s). TISSUE SPECIFICITY: Characteristic constituent of osteoclasts. +Q6PR54 RIF1_MOUSE Telomere-associated protein RIF1 (Rap1-interacting factor 1 homolog) (mRif1) 2419 266,228 Alternative sequence (2); Chain (1); Erroneous initiation (1); Modified residue (38); Region (1); Sequence caution (2); Sequence conflict (32) FUNCTION: Key regulator of TP53BP1 that plays a key role in the repair of double-strand DNA breaks (DSBs) in response to DNA damage: acts by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs (PubMed:23333305, PubMed:23306437, PubMed:23306439). In response to DNA damage, interacts with ATM-phosphorylated TP53BP1 (PubMed:23333305, PubMed:23306437, PubMed:23306439). Interaction with TP53BP1 leads to dissociate the interaction between NUDT16L1/TIRR and TP53BP1, thereby unmasking the tandem Tudor-like domain of TP53BP1 and allowing recruitment to DNA DSBs (By similarity). Once recruited to DSBs, RIF1 and TP53BP1 act by promoting NHEJ-mediated repair of DSBs (PubMed:23333305, PubMed:23306437). In the same time, RIF1 and TP53BP1 specifically counteract the function of BRCA1 by blocking DSBs resection via homologous recombination (HR) during G1 phase (PubMed:23333305, PubMed:23306437). Also required for immunoglobulin class-switch recombination (CSR) during antibody genesis, a process that involves the generation of DNA DSBs (PubMed:23333305, PubMed:23333306, PubMed:23306439). Promotes NHEJ of dysfunctional telomeres (PubMed:23333305). {ECO:0000250|UniProtKB:Q5UIP0, ECO:0000269|PubMed:23306437, ECO:0000269|PubMed:23306439, ECO:0000269|PubMed:23333305, ECO:0000269|PubMed:23333306}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15042697}. Chromosome {ECO:0000269|PubMed:23306437, ECO:0000269|PubMed:23306439, ECO:0000269|PubMed:23333305}. Chromosome, telomere {ECO:0000269|PubMed:15042697}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q5UIP0}. Note=Exhibits ATM- and TP53BP1-dependent localization to uncapped or aberrant telomeres and to DNA double strand breaks (DSBs). Following interaction with TP53BP1, recruited to sites of DNA damage, such as DSBs (PubMed:23333305, PubMed:23306437, PubMed:23306439). Localizes to microtubules of the midzone of the mitotic spindle during anaphase, and to condensed chromosomes in telophase (By similarity). While the majority of the protein appears nuclear and distinct from normal telomere structures, a small fraction may bind to telomeres in embryonic stem cells (PubMed:15042697). {ECO:0000250|UniProtKB:Q5UIP0, ECO:0000269|PubMed:15042697, ECO:0000269|PubMed:23306437, ECO:0000269|PubMed:23306439, ECO:0000269|PubMed:23333305}. SUBUNIT: Interacts with TP53BP1 (when phosphorylated by ATM) (PubMed:23333305, PubMed:23306437, PubMed:23306439). May interact with TRF2 (PubMed:15042697). Interacts with SHLD2 (By similarity). {ECO:0000250|UniProtKB:Q5UIP0, ECO:0000269|PubMed:23306437, ECO:0000269|PubMed:23306439, ECO:0000269|PubMed:23333305, ECO:0000305|PubMed:15042697}. TISSUE SPECIFICITY: Expressed in Sertoli cells, prospermatagonia, early primary spermatocytes, and in oocytes at all stages of their growth. Expressed in embryonic stem (ES) and embryonic germ (EG) cells: expression is lost upon differentiation. {ECO:0000269|PubMed:15042697}. +Q9D358 PPAC_MOUSE Low molecular weight phosphotyrosine protein phosphatase (LMW-PTP) (LMW-PTPase) (EC 3.1.3.48) (Low molecular weight cytosolic acid phosphatase) (EC 3.1.3.2) 158 18,192 Active site (3); Alternative sequence (1); Beta strand (4); Chain (1); Helix (8); Initiator methionine (1); Modified residue (3); Natural variant (3); Turn (1) FUNCTION: Acts on tyrosine phosphorylated proteins, low-MW aryl phosphates and natural and synthetic acyl phosphates. {ECO:0000250|UniProtKB:P11064}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with the SH3 domain of SPTAN1. Interacts with EPHA2; dephosphorylates EPHA2. Interacts with EPHB1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed with highest levels in brain and liver and lowest levels in muscle. {ECO:0000269|PubMed:9824304}. +Q8CFV9 RIFK_MOUSE Riboflavin kinase (EC 2.7.1.26) (ATP:riboflavin 5'-phosphotransferase) (Flavokinase) (KOI-4) 155 17,437 Active site (1); Binding site (10); Chain (1); Metal binding (1) Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (ATP route): step 1/1. FUNCTION: Catalyzes the phosphorylation of riboflavin (vitamin B2) to form flavin-mononucleotide (FMN), hence rate-limiting enzyme in the synthesis of FAD. Essential for TNF-induced reactive oxygen species (ROS) production. Through its interaction with both TNFRSF1A and CYBA, physically and functionally couples TNFRSF1A to NADPH oxidase. TNF-activation of RFK may enhance the incorporation of FAD in NADPH oxidase, a critical step for the assembly and activation of NADPH oxidase (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Monomer (By similarity). Directly interacts with TNFRSF1A death domain; this interaction may be supported by TRADD. In the absence of TNFRSF1A, interacts with TRADD. Independently of TNFRSF1A, interacts with the NADPH oxidase subunit CYBA. {ECO:0000250, ECO:0000269|PubMed:19641494}. +Q8CE08 PPAP_MOUSE Prostatic acid phosphatase (EC 3.1.3.2) (5'-nucleotidase) (5'-NT) (EC 3.1.3.5) (Ecto-5'-nucleotidase) (Fluoride-resistant acid phosphatase) (FRAP) (Thiamine monophosphatase) (TMPase) 381 43,717 Active site (2); Alternative sequence (1); Binding site (4); Chain (1); Disulfide bond (3); Glycosylation (3); Sequence conflict (8); Signal peptide (1); Site (4) FUNCTION: A non-specific tyrosine phosphatase that dephosphorylates a diverse number of substrates under acidic conditions (pH 4-6) including alkyl, aryl, and acyl orthophosphate monoesters and phosphorylated proteins. Has lipid phosphatase activity and inactivates lysophosphatidic acid in seminal plasma (By similarity). {ECO:0000250}.; FUNCTION: Isoform 2: the cellular form also has ecto-5'-nucleotidase activity in dorsal root ganglion (DRG) neurons. Generates adenosine from AMP which acts as a pain suppressor. {ECO:0000269|PubMed:18940592}. SUBCELLULAR LOCATION: Isoform 1: Secreted {ECO:0000305|PubMed:17638863}.; SUBCELLULAR LOCATION: Isoform 2: Cell membrane {ECO:0000269|PubMed:17638863}; Single-pass type I membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:17638863}; Single-pass type I membrane protein {ECO:0000255}. Note=Appears to shuttle between the cell membrane and intracellular vesicles. Colocalizes with FLOT1 at cell membrane and in intracellular vesicles (PubMed:17638863). Colocalizes with LAMP2 on the lysosome membrane (By similarity). {ECO:0000250|UniProtKB:P15309, ECO:0000269|PubMed:17638863}. SUBUNIT: Homodimer; dimer formation is required for phosphatase activity. {ECO:0000250}. TISSUE SPECIFICITY: Isoform 1 is expressed in salivary gland, thymus and thyroid gland. Isoform 2 is widely expressed in prostate lobes, brain, kidney, liver, lung, muscle, placenta, salivary gland, spleen, thyroid and thymus. Locates to Schwann cells and fibroblasts. Expressed in peptidergic and non-peptidergic nociceptive (pain-sensing) neurons. Preferentially expressed in non-peptidergic doral root ganglia neurons. {ECO:0000269|PubMed:17638863, ECO:0000269|PubMed:18940592, ECO:0000269|PubMed:20084276}. +P23204 PPARA_MOUSE Peroxisome proliferator-activated receptor alpha (PPAR-alpha) (Nuclear receptor subfamily 1 group C member 1) 468 52,347 Chain (1); DNA binding (1); Domain (1); Mutagenesis (4); Region (1); Sequence conflict (1); Site (1); Zinc finger (2) FUNCTION: Ligand-activated transcription factor. Key regulator of lipid metabolism. Activated by the endogenous ligand 1-palmitoyl-2-oleoyl-sn-glycerol-3-phosphocholine (16:0/18:1-GPC). Activated by oleylethanolamide, a naturally occurring lipid that regulates satiety. Receptor for peroxisome proliferators such as hypolipidemic drugs and fatty acids. Regulates the peroxisomal beta-oxidation pathway of fatty acids. Functions as transcription activator for the ACOX1 and P450 genes. Transactivation activity requires heterodimerization with RXRA and is antagonized by NR2C2. May be required for the propagation of clock information to metabolic pathways regulated by PER2. {ECO:0000269|PubMed:12955147, ECO:0000269|PubMed:19646743, ECO:0000269|PubMed:20159955}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407, ECO:0000269|PubMed:20159955}. SUBUNIT: Heterodimer; with RXRA. This heterodimerization is required for DNA binding and transactivation activity. Interacts with NCOA3 coactivator. Interacts with CITED2; the interaction stimulates its transcriptional activity. Also interacts with PPARBP in vitro. Interacts with AKAP13, LPIN1, PRDM16 and coactivator NCOA6. Interacts with ASXL1 and ASXL2. Interacts with PER2. Interacts with SIRT1; the interaction seems to be modulated by NAD(+) levels (By similarity). {ECO:0000250|UniProtKB:Q07869, ECO:0000269|PubMed:10788465, ECO:0000269|PubMed:16950137, ECO:0000269|PubMed:18719582, ECO:0000269|PubMed:20159955, ECO:0000269|PubMed:9325263, ECO:0000269|PubMed:9627117}. TISSUE SPECIFICITY: Highly expressed in liver, kidney and heart. Very weakly expressed in brain and testis. DISEASE: Note=Peroxisome proliferators are a diverse group of chemicals that include hypolipidaemic drugs, herbicides and industrial plasticisers. Administration of these chemicals to rodents results in the dramatic proliferation of hepatic peroxisomes as well as liver hyperplasia. +Q3V0F0 RIMB3_MOUSE RIMS-binding protein 3 (RIM-BP3) 1606 177,278 Chain (1); Coiled coil (3); Domain (5); Erroneous initiation (2); Modified residue (2) FUNCTION: Component of the manchette, a microtubule-based structure which plays a key role in sperm head morphogenesis during late stages of sperm development (PubMed:19091768, PubMed:28003339). Important for male fertility (PubMed:19091768). {ECO:0000269|PubMed:19091768, ECO:0000269|PubMed:28003339}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19091768, ECO:0000269|PubMed:28003339}. Note=In elongating spermatids, localizes to the manchette. {ECO:0000269|PubMed:19091768, ECO:0000269|PubMed:28003339}. SUBUNIT: Interacts with FASLG (By similarity). Interacts with LRGUK (via guanylate kinase-like domain) (PubMed:28003339). Interacts (via C-terminus) with HOOK1 (via coiled-coil region) (PubMed:19091768). {ECO:0000250|UniProtKB:A6NJZ7, ECO:0000269|PubMed:19091768, ECO:0000269|PubMed:28003339}. TISSUE SPECIFICITY: Specifically expressed in testis, where it localizes to postmeiotic germ cells (at protein level). {ECO:0000269|PubMed:19091768}. +P35396 PPARD_MOUSE Peroxisome proliferator-activated receptor delta (PPAR-delta) (Nuclear hormone receptor 1) (NUC1) (Nuclear receptor subfamily 1 group C member 2) (Peroxisome proliferator-activated receptor beta) (PPAR-beta) 440 49,715 Chain (1); DNA binding (1); Domain (1); Erroneous initiation (1); Sequence conflict (1); Zinc finger (2) FUNCTION: Ligand-activated transcription factor. Receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. Has a preference for poly-unsaturated fatty acids, such as gamma-linoleic acid and eicosapentanoic acid. Once activated by a ligand, the receptor binds to promoter elements of target genes. Regulates the peroxisomal beta-oxidation pathway of fatty acids. Functions as transcription activator for the acyl-CoA oxidase gene. Decreases expression of NPC1L1 once activated by a ligand (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Heterodimer with the retinoid X receptor. TISSUE SPECIFICITY: Heart, adrenal and intestine. +Q80WS1 RIMKB_MOUSE Beta-citrylglutamate synthase B (EC 6.3.1.17) (N-acetyl-aspartylglutamate synthetase B) (NAAG synthetase B) (NAAGS) (EC 6.3.2.41) (Ribosomal protein S6 modification-like protein B) 387 42,528 Alternative sequence (4); Binding site (2); Chain (1); Domain (1); Erroneous initiation (1); Metal binding (4); Nucleotide binding (1) FUNCTION: Catalyzes the synthesis of beta-citryl-L-glutamate and N-acetyl-L-aspartyl-L-glutamate. Beta-citryl-L-glutamate is synthesized more efficiently than N-acetyl-L-aspartyl-L-glutamate. {ECO:0000269|PubMed:20643647, ECO:0000269|PubMed:20657015}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20643647}. TISSUE SPECIFICITY: Strongly expressed in brain and testis. Expressed in eyes, thymus, lung, kidney, skeletal muscle, spleen, skin and heart. Expressed in neurons of the neocortex, the gray matter and Purkinje cells. {ECO:0000269|PubMed:20643647}. +P37238 PPARG_MOUSE Peroxisome proliferator-activated receptor gamma (PPAR-gamma) (Nuclear receptor subfamily 1 group C member 3) 505 57,598 Alternative sequence (1); Chain (1); DNA binding (1); Domain (1); Glycosylation (1); Modified residue (1); Mutagenesis (2); Region (1); Sequence conflict (5); Zinc finger (2) FUNCTION: Nuclear receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. Once activated by a ligand, the nuclear receptor binds to DNA specific PPAR response elements (PPRE) and modulates the transcription of its target genes, such as acyl-CoA oxidase. It therefore controls the peroxisomal beta-oxidation pathway of fatty acids. Key regulator of adipocyte differentiation and glucose homeostasis. ARF6 acts as a key regulator of the tissue-specific adipocyte P2 (aP2) enhancer. Acts as a critical regulator of gut homeostasis by suppressing NF-kappa-B-mediated proinflammatory responses. Plays a role in the regulation of cardiovascular circadian rhythms by regulating the transcription of ARNTL/BMAL1 in the blood vessels (PubMed:19041764). {ECO:0000269|PubMed:18719582, ECO:0000269|PubMed:19041764, ECO:0000269|PubMed:21035761, ECO:0000269|PubMed:21994940, ECO:0000269|PubMed:23525231}. PTM: O-GlcNAcylation at Thr-84 reduces transcriptional activity in adipocytes. {ECO:0000269|PubMed:22226965}.; PTM: Phosphorylated in basal conditions and dephosphorylated when treated with the ligand. May be dephosphorylated by PPP5C. The phosphorylated Ser-112 form is recognized by PER2 and repressed, dephosphorylation at Ser-112 induces adipogenic activity. Ser-112 phosphorylation levels are reduced by 65% in brown adipose tissue compared to white adipose tissue. {ECO:0000269|PubMed:21035761, ECO:0000269|PubMed:21994940}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407, ECO:0000269|PubMed:20498072, ECO:0000269|PubMed:23525231}. Cytoplasm {ECO:0000250}. Note=Redistributed from the nucleus to the cytosol through a MAP2K1/MEK1-dependent manner (By similarity). NOCT enhances its nuclear translocation. {ECO:0000250}. SUBUNIT: Heterodimer with other nuclear receptors, such as RXRA. The heterodimer with the retinoic acid receptor RXRA is called adipocyte-specific transcription factor ARF6. Interacts with NCOA6 coactivator, leading to a strong increase in transcription of target genes. Interacts with coactivator PPARBP, leading to a mild increase in transcription of target genes. Interacts with NOCA7 in a ligand-inducible manner. Interacts with NCOA1 and NCOA2 LXXLL motifs. Interacts with ASXL1, ASXL2, DNTTIP2, FAM120B, MAP2K1/MEK1, NR0B2, PDPK1, PRDM16, PRMT2 and TGFB1I1. Interacts (when activated by agonist) with PPP5C. Interacts with HELZ2 and THRAP3; the interaction stimulates the transcriptional activity of PPARG. Interacts with PER2, the interaction is ligand dependent and blocks PPARG recruitment to target promoters. Interacts with NOCT. Interacts with FOXO1 (acetylated form). Interacts with ACTN4 (By similarity). Interacts (when in the liganded conformation) with GPS2 (PubMed:25519902). {ECO:0000250|UniProtKB:P37231, ECO:0000269|PubMed:10788465, ECO:0000269|PubMed:15687259, ECO:0000269|PubMed:17595322, ECO:0000269|PubMed:18719582, ECO:0000269|PubMed:19037106, ECO:0000269|PubMed:20498072, ECO:0000269|PubMed:21035761, ECO:0000269|PubMed:21994940, ECO:0000269|PubMed:23525231, ECO:0000269|PubMed:25519902, ECO:0000269|PubMed:7838715, ECO:0000269|PubMed:7926726, ECO:0000269|PubMed:9325263}. TISSUE SPECIFICITY: Highest expression in white and brown adipose tissue. Also found in liver, skeletal muscle, heart, adrenal gland, spleen, kidney and intestine. Isoform 2 is more abundant than isoform 1 in adipose tissue. {ECO:0000269|PubMed:21035761, ECO:0000269|PubMed:7838715}. +Q8VDG5 PPCS_MOUSE Phosphopantothenate--cysteine ligase (EC 6.3.2.5) (Phosphopantothenoylcysteine synthetase) (PPC synthetase) 311 33,794 Alternative sequence (1); Chain (1); Initiator methionine (1); Modified residue (1) Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 2/5. FUNCTION: Catalyzes the first step in the biosynthesis of coenzyme A from vitamin B5, where cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine. {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +Q9QUR6 PPCE_MOUSE Prolyl endopeptidase (PE) (EC 3.4.21.26) (Post-proline cleaving enzyme) 710 80,752 Active site (3); Chain (1); Modified residue (2) FUNCTION: Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long. SUBCELLULAR LOCATION: Cytoplasm. +O35385 PPE2_MOUSE Serine/threonine-protein phosphatase with EF-hands 2 (PPEF-2) (EC 3.1.3.16) 757 86,645 Active site (1); Calcium binding (2); Chain (1); Domain (4); Metal binding (7); Region (1) FUNCTION: May play a role in phototransduction. May dephosphorylate photoactivated rhodopsin. May function as a calcium sensing regulator of ionic currents, energy production or synaptic transmission. TISSUE SPECIFICITY: Detected in retina, more specifically in photoreceptors. +P17742 PPIA_MOUSE Peptidyl-prolyl cis-trans isomerase A (PPIase A) (EC 5.2.1.8) (Cyclophilin A) (Cyclosporin A-binding protein) (Rotamase A) (SP18) [Cleaved into: Peptidyl-prolyl cis-trans isomerase A, N-terminally processed] 164 17,971 Chain (2); Cross-link (3); Domain (1); Glycosylation (1); Initiator methionine (1); Modified residue (10); Sequence conflict (2) FUNCTION: PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. {ECO:0000250|UniProtKB:P62937}. PTM: Acetylation at Lys-125 markedly inhibits catalysis of cis to trans isomerization. PPIA acetylation also antagonizes the immunosuppressive effects of cyclosporine by inhibiting the sequential steps of cyclosporine binding and calcineurin inhibition (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Secreted {ECO:0000250}. Note=Secretion occurs in response to oxidative stress in vascular smooth muscle through a vesicular secretory pathway that involves actin remodeling and myosin II activation, and mediates ERK1/2 activation. {ECO:0000250}. SUBUNIT: Interacts with protein phosphatase PPP3CA/calcineurin A (By similarity). Interacts with PRPF19 isoform 2 (via N-terminus). {ECO:0000250|UniProtKB:P62937, ECO:0000269|PubMed:16352598}. +Q925F3 R144A_MOUSE E3 ubiquitin-protein ligase RNF144A (EC 2.3.2.31) (RING finger protein 144A) (UbcM4-interacting protein 4) (Ubiquitin-conjugating enzyme 7-interacting protein 4) 292 32,845 Active site (1); Chain (1); Erroneous initiation (1); Metal binding (20); Region (1); Transmembrane (1); Zinc finger (3) TRANSMEM 250 270 Helical. {ECO:0000255}. Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates the ubiquitination and degradation of the DNA damage kinase PRKDC. {ECO:0000250|UniProtKB:P50876}. PTM: Autoubiquitinated. {ECO:0000250|UniProtKB:P50876}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P50876}; Single-pass membrane protein {ECO:0000305}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P50876}. SUBUNIT: Interacts with UBE2L3. {ECO:0000269|PubMed:10431818}. DOMAIN: Members of the RBR family are atypical E3 ligases. They interact with the E2 conjugating enzyme UBE2L3 and function like HECT-type E3 enzymes: they bind E2s via the first RING domain, but require an obligate trans-thiolation step during the ubiquitin transfer, requiring a conserved cysteine residue in the second RING domain. {ECO:0000250|UniProtKB:O60260}. +Q80YR9 R12BA_MOUSE RNA-binding protein 12B-A (RNA-binding motif protein 12B-A) 836 96,596 Chain (1); Domain (4); Modified residue (2); Sequence caution (1); Sequence conflict (3) +Q8K0S5 R4RL1_MOUSE Reticulon-4 receptor-like 1 (Nogo receptor-like 2) (Nogo-66 receptor homolog 2) (Nogo-66 receptor-related protein 3) (NgR3) 445 49,836 Chain (1); Domain (2); Lipidation (1); Propeptide (1); Repeat (8); Signal peptide (1); Transmembrane (1) TRANSMEM 424 444 Helical. {ECO:0000255}. FUNCTION: Cell surface receptor that plays a functionally redundant role in postnatal brain development and in regulating axon regeneration in the adult central nervous system (PubMed:22406547, PubMed:27339102). Contributes to normal axon migration across the brain midline and normal formation of the corpus callosum (PubMed:27339102). Protects motoneurons against apoptosis; protection against apoptosis is probably mediated by MAG (PubMed:26335717). Plays a role in inhibiting neurite outgrowth and axon regeneration via its binding to neuronal chondroitin sulfate proteoglycans (PubMed:22406547). Binds heparin (PubMed:22406547). Like other family members, plays a role in restricting the number dendritic spines and the number of synapses that are formed during brain development (PubMed:22325200). Signaling mediates activation of Rho and downstream reorganization of the actin cytoskeleton (PubMed:22325200). {ECO:0000269|PubMed:22325200, ECO:0000269|PubMed:22406547, ECO:0000269|PubMed:26335717, ECO:0000269|PubMed:27339102}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12839991}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q80WD0}. Membrane raft {ECO:0000250|UniProtKB:Q86UN2}. Perikaryon {ECO:0000250|UniProtKB:Q80WD0}. Cell projection {ECO:0000250|UniProtKB:Q80WD0}. Note=Localized to the surface of neurons, including axons. {ECO:0000250|UniProtKB:Q80WD0}. SUBUNIT: Identified in a complex that contains RTN4R, RTN4RL1 and NGFR; the interaction depends on the presence of chondroitin sulfate proteoglycans (PubMed:22406547). Does not interact with MAG, OMG and RTN4 (PubMed:12839991). {ECO:0000269|PubMed:12839991, ECO:0000269|PubMed:22406547}. TISSUE SPECIFICITY: Detected in brain (at protein level) (PubMed:22406547). Detected in retina ganglion cell layer and inner nuclear layer (PubMed:22406547). {ECO:0000269|PubMed:22406547}. +Q7M6Z0 R4RL2_MOUSE Reticulon-4 receptor-like 2 (Nogo receptor-like 3) (Nogo-66 receptor homolog 1) (Nogo-66 receptor-related protein 2) (NgR2) 420 46,075 Chain (1); Disulfide bond (4); Domain (2); Erroneous translation (1); Glycosylation (3); Lipidation (1); Propeptide (1); Region (1); Repeat (8); Signal peptide (1) FUNCTION: Cell surface receptor that plays a functionally redundant role in the inhibition of neurite outgrowth mediated by MAG (By similarity). Plays a functionally redundant role in postnatal brain development (PubMed:27339102). Contributes to normal axon migration across the brain midline and normal formation of the corpus callosum (PubMed:27339102). Does not seem to play a significant role in regulating axon regeneration in the adult central nervous system (PubMed:22406547). Protects motoneurons against apoptosis; protection against apoptosis is probably mediated by MAG (PubMed:26335717). Like other family members, plays a role in restricting the number dendritic spines and the number of synapses that are formed during brain development (PubMed:22325200). Signaling mediates activation of Rho and downstream reorganization of the actin cytoskeleton (PubMed:22325200). {ECO:0000250|UniProtKB:Q80WD1, ECO:0000269|PubMed:22325200, ECO:0000269|PubMed:22406547, ECO:0000269|PubMed:26335717, ECO:0000269|PubMed:27339102}. PTM: Undergoes zinc metalloproteinase-mediated ectodomain shedding in neuroblastoma cells; is released both as a full-length ectodomain and an N-terminal fragment containing the leucine-rich repeat (LRR) region of the protein. {ECO:0000250|UniProtKB:Q86UN3}.; PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q86UN3}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q86UN3}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q86UN3}. Membrane raft {ECO:0000250|UniProtKB:Q80WD1}. Cell projection, dendrite {ECO:0000269|PubMed:22325200}. Cell projection, axon {ECO:0000269|PubMed:22325200}. Perikaryon {ECO:0000250|UniProtKB:Q80WD1}. Note=Localized to the surface of neurons, including axons. Detected close to synapses, but is excluded from synapses. {ECO:0000269|PubMed:22325200}. SUBUNIT: Interaction with MAG is controversial, and may be indirect (Probable). Interacts with MAG. Does not interact with OMG and RTN4 (By similarity). {ECO:0000250|UniProtKB:Q80WD1, ECO:0000305}. TISSUE SPECIFICITY: Detected in brain (PubMed:22406547). Detected in hippocampus neurons (at protein level) (PubMed:22325200). {ECO:0000269|PubMed:22325200, ECO:0000269|PubMed:22406547}. +Q8BQP9 R7BP_MOUSE Regulator of G-protein signaling 7-binding protein (R7 family-binding protein) 257 29,023 Chain (1); Frameshift (1); Lipidation (2); Motif (1); Mutagenesis (6); Sequence conflict (6) FUNCTION: Regulator of G protein-coupled receptor (GPCR) signaling. Regulatory subunit of the R7-Gbeta5 complexes that acts by controlling the subcellular location of the R7-Gbeta5 complexes. When palmitoylated, it targets the R7-Gbeta5 complexes to the plasma membrane, leading to inhibit G protein alpha subunits. When it is unpalmitoylated, the R7-Gbeta5 complexes undergo a nuclear/cytoplasmic shuttling. May also act by controlling the proteolytic stability of R7 proteins, probably by protecting them from degradation. {ECO:0000269|PubMed:15897264, ECO:0000269|PubMed:16574655, ECO:0000269|PubMed:16867977, ECO:0000269|PubMed:17158100}. PTM: Palmitoylation regulates the cell membrane and nuclear shuttling and the regulation of GPCR signaling. Upon depalmitoylation, it is targeted into the nucleus. {ECO:0000269|PubMed:15897264, ECO:0000269|PubMed:16574655}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15897264, ECO:0000269|PubMed:16574655, ECO:0000269|PubMed:16867977}. Cytoplasm {ECO:0000269|PubMed:15897264, ECO:0000269|PubMed:16574655}. Cell membrane {ECO:0000269|PubMed:15897264, ECO:0000269|PubMed:16574655, ECO:0000269|PubMed:16867977}; Lipid-anchor {ECO:0000269|PubMed:15897264, ECO:0000269|PubMed:16867977}. Note=Shuttling between the plasma membrane, the cytoplasm and the nucleus is regulated by palmitoylation (PubMed:15897264). {ECO:0000269|PubMed:15897264}. SUBUNIT: Interacts with 'R7' family proteins RGS6, RGS7, RGS9 and RGS11. Component of some R7-Gbeta5 complex composed of some R7 protein (RGS6, RGS7, RGS9 or RGS11), Gbeta5 (GNB5) and RGS7BP. {ECO:0000269|PubMed:15632198, ECO:0000269|PubMed:15897264}. DOMAIN: The nuclear localization signal is both required for nuclear localization and palmitoylation. {ECO:0000269|PubMed:16867977}. TISSUE SPECIFICITY: Specifically expressed in the central nervous system including the retina but not in other non-neuronal tissues (at protein level). {ECO:0000269|PubMed:15632198, ECO:0000269|PubMed:15897264}. +O55230 RA51D_MOUSE DNA repair protein RAD51 homolog 4 (R51H3) (RAD51 homolog D) (RAD51-like protein 3) 329 35,260 Chain (1); Nucleotide binding (1); Region (3) FUNCTION: Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA breaks arising during DNA replication or induced by DNA-damaging agents. Bind to single-stranded DNA (ssDNA) and has DNA-dependent ATPase activity. Part of the Rad21 paralog protein complex BCDX2 which acts in the BRCA1-BRCA2-dependent HR pathway. Upon DNA damage, BCDX2 acts downstream of BRCA2 recruitment and upstream of RAD51 recruitment. BCDX2 binds predominantly to the intersection of the four duplex arms of the Holliday junction and to junction of replication forks. The BCDX2 complex was originally reported to bind single-stranded DNA, single-stranded gaps in duplex DNA and specifically to nicks in duplex DNA. Involved in telomere maintenance. The BCDX2 subcomplex XRCC2:RAD51D can stimulate Holliday junction resolution by BLM (By similarity). {ECO:0000250, ECO:0000269|PubMed:15109494}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, telomere {ECO:0000269|PubMed:15109494}. SUBUNIT: Part of the BCDX2 complex consisting of RAD51B, RAD51C, RAD51D and XRCC2; the complex has a ring-like structure arranged into a flat disc around a central channel. In the absence of DNA, the BCDX2 subcomplex XRCC2:RAD51D formed a multimeric ring structure; in the presence of single-stranded DNA it formed a filamentous structure with the ssDNA. Interacts with SWSAP1 and ZSWIM7; involved in homologous recombination repair. Interacts with BLM; required for stimulation of BLM activity by the BCDX2 subcomplex XRCC2:RAD51D (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in brain followed by testis. Also expressed in heart, liver, kidney, spleen, lung and skeletal muscle. +Q6PHN9 RAB35_MOUSE Ras-related protein Rab-35 201 23,025 Chain (1); Lipidation (2); Modified residue (2); Motif (1); Mutagenesis (2); Nucleotide binding (5) FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab is involved in the process of endocytosis and is an essential rate-limiting regulator of the fast recycling pathway back to the plasma membrane. During cytokinesis, required for the postfurrowing terminal steps, namely for intercellular bridge stability and abscission, possibly by controlling phosphatidylinositol 4,5-bis phosphate (PIP2) and SEPT2 localization at the intercellular bridge. May indirectly regulate neurite outgrowth. Together with TBC1D13 may be involved in regulation of insulin-induced glucose transporter SLC2A4/GLUT4 translocation to the plasma membrane in adipocytes. {ECO:0000269|PubMed:20159556, ECO:0000269|PubMed:22762500, ECO:0000269|PubMed:23572513}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q15286}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:Q15286}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:Q15286}. Endosome {ECO:0000250|UniProtKB:Q15286}. Melanosome {ECO:0000250|UniProtKB:Q15286}. Note=Present on sorting endosomes and recycling endosome tubules. Tends to be enriched in PIP2-positive cell membrane domains. During mitosis, associated with the plasma membrane and present at the ingressing furrow during early cytokinesis as well as at the intercellular bridge later during cytokinesis. Identified in stage I to stage IV melanosomes. {ECO:0000250|UniProtKB:Q15286}. SUBUNIT: Interacts with DENND1A and DENND1B; in a nucleotide-dependent manner (PubMed:20159556, PubMed:26774822). Interacts with DENND1C; weak interaction which is nucleotide-independent (By similarity). Interacts (GTP-bound form) with ACAP2 and MICALL1; the interaction is direct and probably recruits ACAP2 and MICALL1 to membranes (PubMed:23572513). Interacts with EHD1; the interaction is indirect through MICALL1 and probably recruits EHD1 to membranes (PubMed:23572513). {ECO:0000250|UniProtKB:Q15286, ECO:0000269|PubMed:23572513}. +Q64008 RAB34_MOUSE Ras-related protein Rab-34 (Ras-related homolog) (Ras-related protein Rab-39) (Ras-related protein Rah) 259 29,101 Chain (1); Lipidation (2); Modified residue (2); Motif (1); Mutagenesis (2); Nucleotide binding (3); Sequence conflict (3) FUNCTION: Protein transport. Plays a role in the maturation of phagosomes that engulf pathogens, such as S.aureus and Mycobacterium. Plays a role in the fusion of phagosomes with lysosomes (By similarity). Involved in the redistribution of lysosomes to the peri-Golgi region (PubMed:12475955). Acts also as a positive regulator of hedgehog signaling and regulates ciliary function (PubMed:29290584). {ECO:0000250|UniProtKB:Q9BZG1, ECO:0000269|PubMed:12475955, ECO:0000269|PubMed:29290584}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12475955}. Golgi apparatus {ECO:0000269|PubMed:12475955}. Cytoplasmic vesicle, phagosome {ECO:0000250|UniProtKB:Q9BZG1}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:Q9BZG1}; Lipid-anchor {ECO:0000250|UniProtKB:Q9BZG1}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9BZG1}. Cell projection, cilium {ECO:0000269|PubMed:29290584}. Note=Recruited to phagosomes containing S.aureus or Mycobacterium. {ECO:0000250|UniProtKB:Q9BZG1}. SUBUNIT: Interacts with RILP. {ECO:0000269|PubMed:12475955}. +P35276 RAB3D_MOUSE Ras-related protein Rab-3D 219 24,416 Chain (1); Initiator methionine (1); Lipidation (2); Modified residue (3); Motif (1); Nucleotide binding (5) FUNCTION: Protein transport. Probably involved in vesicular traffic (By similarity). May be involved in the insulin-induced exocytosis of glut4-containing vesicles in adipocytes. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. SUBUNIT: Interacts with RIMS1, RIMS2, RPH3A, RPH3AL and RAB3IP. {ECO:0000269|PubMed:11431472, ECO:0000269|PubMed:12578829}. TISSUE SPECIFICITY: Predominantly expressed in the adipocyte tissue, but is also expressed in several other organs including skin, spleen, heart and lung. +P61294 RAB6B_MOUSE Ras-related protein Rab-6B 208 23,462 Binding site (1); Chain (1); Lipidation (2); Modified residue (1); Motif (1); Nucleotide binding (3) FUNCTION: Seems to have a role in retrograde membrane traffic at the level of the Golgi complex. May function in retrograde transport in neuronal cells (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9NRW1}; Lipid-anchor {ECO:0000305}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250|UniProtKB:Q9NRW1}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q9NRW1}. Note=Colocalizes with BICD1 at vesicular structures that align along microtubules. {ECO:0000250|UniProtKB:Q9NRW1}. SUBUNIT: Interacts with RAB6KIFL. Interacts (GTP-bound) with BICD1 (via C-terminus); the interaction is direct. Interacts (GDP-bound) with DYNLRB1 (By similarity). Interacts with BICDL1/BICDR1; leads to its accumulation in the pericentrosomal region. Interacts (GTP-bound) with APBA1/MINT1 isoform 3, also called Mint1_826 (By similarity). {ECO:0000250}. +Q91ZR1 RAB4B_MOUSE Ras-related protein Rab-4B 213 23,629 Chain (1); Initiator methionine (1); Lipidation (2); Modified residue (4); Motif (1); Nucleotide binding (4); Sequence conflict (2) FUNCTION: Protein transport. Probably involved in vesicular traffic (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. +P51150 RAB7A_MOUSE Ras-related protein Rab-7a 207 23,490 Beta strand (7); Chain (1); Helix (8); Initiator methionine (1); Lipidation (2); Modified residue (3); Motif (1); Nucleotide binding (5); Sequence conflict (1); Turn (2) FUNCTION: Key regulator in endo-lysosomal trafficking. Governs early-to-late endosomal maturation, microtubule minus-end as well as plus-end directed endosomal migration and positioning, and endosome-lysosome transport through different protein-protein interaction cascades. Plays a central role, not only in endosomal traffic, but also in many other cellular and physiological events, such as growth-factor-mediated cell signaling, nutrient-transportor mediated nutrient uptake, neurotrophin transport in the axons of neurons and lipid metabolism. Also involved in regulation of some specialized endosomal membrane trafficking, such as maturation of melanosomes, pathogen-induced phagosomes (or vacuoles) and autophagosomes. Plays a role in the maturation and acidification of phagosomes that engulf pathogens, such as S.aureus and Mycobacteria. Plays a role in the fusion of phagosomes with lysosomes. Plays important roles in microbial pathogen infection and survival, as well as in participating in the life cycle of viruses. Microbial pathogens possess survival strategies governed by RAB7A, sometimes by employing RAB7A function (e.g. Salmonella) and sometimes by excluding RAB7A function (e.g. Mycobacterium). In concert with RAC1, plays a role in regulating the formation of RBs (ruffled borders) in osteoclasts. Controls the endosomal trafficking and neurite outgrowth signaling of NTRK1/TRKA. Regulates the endocytic trafficking of the EGF-EGFR complex by regulating its lysosomal degradation (By similarity). Involved in the ADRB2-stimulated lipolysis through lipophagy, a cytosolic lipase-independent autophagic pathway (PubMed:23708524). Required for the exosomal release of SDCBP, CD63 and syndecan (By similarity). {ECO:0000250|UniProtKB:P51149, ECO:0000269|PubMed:23708524}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:P51149}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Late endosome membrane {ECO:0000250|UniProtKB:P51149}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Lysosome membrane {ECO:0000250|UniProtKB:P51149}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Melanosome membrane {ECO:0000250|UniProtKB:P51149}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:P51149}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Lipid droplet {ECO:0000269|PubMed:23708524}. Endosome membrane {ECO:0000250|UniProtKB:P51149}. Note=Colocalizes with OSBPL1A at the late endosome (By similarity). Found in the ruffled border (a late endosomal-like compartment in the plasma membrane) of bone-resorbing osteoclasts (By similarity). Recruited to phagosomes containing S.aureus or Mycobacterium (By similarity). Lipid droplet localization is increased upon ADRB2 stimulation (PubMed:23708524). {ECO:0000250|UniProtKB:P51149, ECO:0000269|PubMed:23708524}. SUBUNIT: Interacts with NTRK1/TRKA (By similarity), RILP (By similarity), PSMA7 (By similarity), RNF115 (PubMed:12972561) and FYCO1 (By similarity). Interacts with the PIK3C3/VPS34-PIK3R4 complex (By similarity). The GTP-bound form interacts with OSBPL1A and RAC1 (By similarity). Interacts with CLN3 (By similarity). Interacts with CHM, the substrate-binding subunit of the Rab geranylgeranyltransferase complex (By similarity). Interacts with C9orf72 (PubMed:24549040). Does not interact with HPS4 and the BLOC-3 complex (heterodimer of HPS1 and HPS4) (PubMed:20048159). Interacts with CLN5 (By similarity). Interacts with PLEKHM1 (via N- and C-terminus) (PubMed:27777970). Interacts with RUFY4 (By similarity). {ECO:0000250|UniProtKB:P09527, ECO:0000250|UniProtKB:P51149, ECO:0000269|PubMed:12972561, ECO:0000269|PubMed:20048159, ECO:0000269|PubMed:24549040, ECO:0000269|PubMed:27777970}. TISSUE SPECIFICITY: Widely expressed. High expression in liver, heart and kidney. Found in sensory and motor neurons. {ECO:0000269|PubMed:12545426}. +Q91WG2 RABE2_MOUSE Rab GTPase-binding effector protein 2 (Rabaptin-5beta) 554 62,132 Alternative sequence (2); Chain (1); Coiled coil (2); Compositional bias (2); Modified residue (2) FUNCTION: Plays a role in membrane trafficking and in homotypic early endosome fusion. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Early endosome {ECO:0000250}. SUBUNIT: Heterodimer with RABGEF1. The dimer binds RAB5A that has been activated by GTP-binding (By similarity). {ECO:0000250}. +Q9QXK2 RAD18_MOUSE E3 ubiquitin-protein ligase RAD18 (EC 2.3.2.27) (Postreplication repair protein RAD18) (mRAD18Sc) (RING-type E3 ubiquitin transferase RAD18) 509 57,412 Chain (1); Domain (1); Modified residue (6); Motif (1); Sequence conflict (2); Zinc finger (2) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase involved in postreplication repair of UV-damaged DNA. Postreplication repair functions in gap-filling of a daughter strand on replication of damaged DNA. Associates to the E2 ubiquitin conjugating enzyme UBE2B to form the UBE2B-RAD18 ubiquitin ligase complex involved in mono-ubiquitination of DNA-associated PCNA on 'Lys-164'. Has ssDNA binding activity. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NS91}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9NS91}. Note=Associates with chromatin. Colocalizes with SLF1 in the nucleus and to centrosomes. Relocalizes with SLF1 to nuclear foci in response to DNA damage. Accumulates with the SLF1-SLF2 and SMC5-SMC6 complexes at replication-coupled DNA interstrand repair and DNA double-strand breaks (DSBs) sites on chromatin in a ubiquitin-dependent manner. {ECO:0000250|UniProtKB:Q9NS91}. SUBUNIT: Homodimer. Interacts with UBE2A and UBE2B, one homodimer binding one molecule of UBE2B. Interacts with HLTF. Interacts with SHPRH. Interacts with SPRTN; leading to enhance chromatin association of RAD18 and RAD18-mediated PCNA ubiquitination and translesion DNA synthesis. Interacts (via C-terminus and phosphorylated form) with SLF1 (via BRCT domains); this interaction is required for efficient repair of UV-induced DNA damage. Interacts with SLF2. Interacts with SMC5; this interaction is increased in a SLF1 or SLF2-dependent manner. {ECO:0000250|UniProtKB:Q9NS91}. TISSUE SPECIFICITY: Expressed in thymus, spleen, brain, and ovary. +Q99P51 RASF3_MOUSE Ras association domain-containing protein 3 232 26,749 Chain (1); Domain (2); Initiator methionine (1); Modified residue (1); Sequence conflict (1) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Localized to microtubules in vascular endothelial cells. {ECO:0000250}. +P08556 RASN_MOUSE GTPase NRas (Transforming protein N-Ras) 189 21,199 Chain (1); Lipidation (2); Modified residue (1); Motif (1); Nucleotide binding (3); Propeptide (1); Region (1); Sequence conflict (1) FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. PTM: Palmitoylated by the ZDHHC9-GOLGA7 complex. Depalmitoylated by ABHD17A, ABHD17B and ABHD17C. A continuous cycle of de- and re-palmitoylation regulates rapid exchange between plasma membrane and Golgi. {ECO:0000250|UniProtKB:P01111}.; PTM: Acetylation at Lys-104 prevents interaction with guanine nucleotide exchange factors (GEFs). {ECO:0000250|UniProtKB:P01116}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P01111}; Lipid-anchor {ECO:0000250|UniProtKB:P01111}; Cytoplasmic side {ECO:0000250|UniProtKB:P01111}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P01111}; Lipid-anchor {ECO:0000250|UniProtKB:P01111}. Note=Shuttles between the plasma membrane and the Golgi apparatus. {ECO:0000250|UniProtKB:P01111}. SUBUNIT: Interacts (active GTP-bound form preferentially) with RGS14. Interacts (active GTP-bound form) with RASSF7 (By similarity). {ECO:0000250}. +Q5EBH1 RASF5_MOUSE Ras association domain-containing protein 5 (New ras effector 1) (Regulator for cell adhesion and polarization enriched in lymphoid tissues) (RAPL) 413 46,714 Alternative sequence (2); Beta strand (6); Chain (1); Domain (2); Erroneous initiation (1); Helix (9); Modified residue (3); Mutagenesis (10); Sequence conflict (2); Turn (3); Zinc finger (1) FUNCTION: Potental tumor suppressor. Seems to be involved in lymphocyte adhesion by linking RAP1A activation upon T-cell receptor or chemokine stimulation to integrin activation. Isoform 2 stimulates lymphocyte polarization and the patch-like distribution of ITGAL/LFA-1, resulting in an enhanced adhesion to ICAM1. Together with RAP1A may participate in regulation of microtubule growth. The association of isoform 2 with activated RAP1A is required for directional movement of endothelial cells during wound healing (By similarity). May be involved in regulation of Ras apoptotic function. The RASSF5-STK4/MST1 complex may mediate HRAS and KRAS induced apoptosis. {ECO:0000250, ECO:0000269|PubMed:11864565}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Isoform 2 is mainly located in the perinuclear region of unstimulated primary T-cells. Upon stimulation translocates to the leading edge and colocalizes with ITGAL/LFA-1 in the peripheral zone of the immunological synapse. Isoform 2 is localized to growing microtubules in vascular endothelial cells and is dissociated from microtubules by activated RAP1A (By similarity). {ECO:0000250}. SUBUNIT: Interacts directly with activated HRAS; a RASSF5-STK4/MST1 complex probably associates with activated HRAS. Interacts with KRAS. Probably interacts with Ras-like GTPases RRAS, RRAS2, MRAS, RAP1B, RAP2A and RALA. Can self-associate. Interacts with RSSF1 isoform A. The RSSF1 isoform A-RSSF5 heterodimer probably mediates the association of RSSF1 with HRAS. Isoform 2 interacts with activated RAP1A and ITGAL/LFA-1. Binds STK4/MST1, inhibiting STK4/MST1 autoactivation (By similarity). {ECO:0000250}. +P46638 RB11B_MOUSE Ras-related protein Rab-11B 218 24,489 Chain (1); Initiator methionine (1); Lipidation (2); Modified residue (3); Motif (1); Mutagenesis (2); Nucleotide binding (4); Propeptide (1) FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab plays a role in endocytic recycling, regulating apical recycling of several transmembrane proteins including cystic fibrosis transmembrane conductance regulator/CFTR, epithelial sodium channel/ENaC, potassium voltage-gated channel, and voltage-dependent L-type calcium channel. May also regulate constitutive and regulated secretion, like insulin granule exocytosis. Required for melanosome transport and release from melanocytes. Also regulates V-ATPase intracellular transport in response to extracellular acidosis. {ECO:0000269|PubMed:10942597, ECO:0000269|PubMed:19335615, ECO:0000269|PubMed:21291502, ECO:0000269|PubMed:22129970}. PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}. SUBCELLULAR LOCATION: Recycling endosome membrane {ECO:0000305|PubMed:10942597}; Lipid-anchor {ECO:0000305|PubMed:10942597}; Cytoplasmic side {ECO:0000305|PubMed:10942597}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Recruited to phagosomes containing S.aureus. {ECO:0000250}. SUBUNIT: Interacts with KCNMA1 (PubMed:22935415). Interacts with RAB11FIP1, RAB11FIP2, RAB11FIP3 and RAB11FIP4. May interact with TBC1D14. Interacts with ATP6V1E1. Interacts with PI4KB (By similarity). Interacts (GDP-bound form) with ZFYVE27. Interacts (GDP-bound form) with KIF5A in a ZFYVE27-dependent manner (By similarity). Interacts with RELCH (PubMed:29514919). {ECO:0000250|UniProtKB:Q15907, ECO:0000269|PubMed:22935415, ECO:0000269|PubMed:29514919}. TISSUE SPECIFICITY: Abundantly expressed in brain, heart and testis. Also detected in kidney and pancreatic islets. {ECO:0000269|PubMed:19335615}. +P35285 RB22A_MOUSE Ras-related protein Rab-22A (Rab-22) (Rab-14) 194 21,802 Beta strand (6); Chain (1); Helix (7); Lipidation (2); Motif (1); Mutagenesis (1); Nucleotide binding (4); Sequence conflict (1); Turn (1) FUNCTION: Plays a role in endocytosis and intracellular protein transport (PubMed:19759177, PubMed:27718357). Mediates trafficking of TF from early endosomes to recycling endosomes. Required for NGF-mediated endocytosis of NTRK1, and subsequent neurite outgrowth. Binds GTP and GDP and has low GTPase activity. Alternates between a GTP-bound active form and a GDP-bound inactive form (By similarity). {ECO:0000250|UniProtKB:Q9UL26, ECO:0000269|PubMed:19759177, ECO:0000269|PubMed:27718357}. SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:27718357}; Lipid-anchor {ECO:0000305}. Cell membrane {ECO:0000250|UniProtKB:P51154}; Lipid-anchor {ECO:0000305}. Early endosome {ECO:0000269|PubMed:19759177, ECO:0000269|PubMed:27718357}. Late endosome {ECO:0000250|UniProtKB:P51154}. Cell projection, ruffle {ECO:0000250|UniProtKB:Q9UL26}. Cytoplasmic vesicle {ECO:0000269|PubMed:27718357}. Cytoplasmic vesicle, phagosome {ECO:0000250|UniProtKB:Q9UL26}. Cytoplasmic vesicle, phagosome membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Recruited to phagosomes containing S.aureus or M.tuberculosis. {ECO:0000250|UniProtKB:Q9UL26}. SUBUNIT: Binds EEA1 (By similarity). Interacts (in its GTP-bound form) with RINL (By similarity). Interacts directly with ZFYVE20 (PubMed:16034420). Interacts (in its GTP-bound form) with RABGEF1 (PubMed:19759177). {ECO:0000250|UniProtKB:P51154, ECO:0000250|UniProtKB:Q9UL26, ECO:0000269|PubMed:16034420, ECO:0000269|PubMed:19759177}. TISSUE SPECIFICITY: Detected in brain and heart, and at lower levels in lung and spleen. {ECO:0000269|PubMed:8126105}. +Q60972 RBBP4_MOUSE Histone-binding protein RBBP4 (Chromatin assembly factor 1 subunit C) (CAF-1 subunit C) (Chromatin assembly factor I p48 subunit) (CAF-I 48 kDa subunit) (CAF-I p48) (Nucleosome-remodeling factor subunit RBAP48) (Retinoblastoma-binding protein 4) (RBBP-4) (Retinoblastoma-binding protein p48) 425 47,656 Chain (1); Cross-link (3); Frameshift (1); Initiator methionine (1); Modified residue (5); Repeat (6); Sequence conflict (1) FUNCTION: Core histone-binding subunit that may target chromatin assembly factors, chromatin remodeling factors and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA. Component of several complexes which regulate chromatin metabolism. These include the chromatin assembly factor 1 (CAF-1) complex, which is required for chromatin assembly following DNA replication and DNA repair; the core histone deacetylase (HDAC) complex, which promotes histone deacetylation and consequent transcriptional repression; the nucleosome remodeling and histone deacetylase complex (the NuRD complex), which promotes transcriptional repression by histone deacetylation and nucleosome remodeling; and the PRC2/EED-EZH2 complex, which promotes repression of homeotic genes during development; and the NURF (nucleosome remodeling factor) complex (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Binds directly to helix 1 of the histone fold of histone H4, a region that is not accessible when H4 is in chromatin. Subunit of the chromatin assembly factor 1 (CAF-1) complex, which is composed of RBBP4, CHAF1B and CHAF1A. Subunit of the core histone deacetylase (HDAC) complex, which is composed of HDAC1, HDAC2, RBBP4 and RBBP7. The core HDAC complex associates with SIN3A, ARID4B/SAP180, SAP18, SAP30, SAP130, SUDS3/SAP45 and possibly ARID4A/RBP1 and ING1 to form the SIN3 HDAC complex. The core HDAC complex may also associate with MTA2, MBD3, CHD3 and CHD4 to form the nucleosome remodeling and histone deacetylase complex (the NuRD complex). The NuRD complex may also interact with MBD3L1 and MBD3L2. Component of the PRC2/EED-EZH1 complex, which includes EED, EZH1, SUZ12, RBBP4 and AEBP2. Interacts with MTA1. Subunit of the PRC2/EED-EZH2 complex, which is composed of at least EED, EZH2, RBBP4, RBBP7 and SUZ12. The PRC2/EED-EZH2 complex may also associate with HDAC1. Component of the PRC2/EED-EZH1 complex, which includes EED, EZH1, SUZ12, RBBP4 and AEBP2. Part of the nucleosome remodeling factor (NURF) complex which consists of SMARCA1; BPTF; RBBP4 and RBBP7. Interacts with the viral protein-binding domain of the retinoblastoma protein (RB1). Interacts with SPEN/MINT. Interacts with BRCA1 (By similarity). Interacts with CREBBP, and this interaction may be enhanced by the binding of phosphorylated CREB1 to CREBBP. Interacts with SAP30, SUV39H1 and HDAC7. Component of the DREAM complex (also named LINC complex) at least composed of E2F4, E2F5, LIN9, LIN37, LIN52, LIN54, MYBL1, MYBL2, RBL1, RBL2, RBBP4, TFDP1 and TFDP2. The complex exists in quiescent cells where it represses cell cycle-dependent genes. It dissociates in S phase when LIN9, LIN37, LIN52 and LIN54 form a subcomplex that binds to MYBL2. Found in a complex composed of at least SINHCAF, SIN3A, HDAC1, SAP30, RBBP4, OGT and TET1 (PubMed:28554894). {ECO:0000250|UniProtKB:Q09028, ECO:0000269|PubMed:10866654, ECO:0000269|PubMed:10984530, ECO:0000269|PubMed:11788710, ECO:0000269|PubMed:19026780, ECO:0000269|PubMed:28554894, ECO:0000269|PubMed:9702189}. TISSUE SPECIFICITY: Higher levels in brain, thymus, lung, spleen, kidney, testis, and ovary/uterus; lower levels in heart, liver, and muscle. {ECO:0000269|PubMed:7503932}. +Q99P58 RB27B_MOUSE Ras-related protein Rab-27B 218 24,560 Beta strand (6); Chain (1); Disulfide bond (1); Helix (6); Initiator methionine (1); Lipidation (2); Modified residue (2); Motif (1); Mutagenesis (3); Nucleotide binding (4); Sequence conflict (3); Turn (3) FUNCTION: Plays a role in NTRK2/TRKB axonal anterograde transport by facilitating the associaton of NTRK2/TRKB with KLC1. May be involved in targeting uroplakins to urothelial apical membranes. {ECO:0000250|UniProtKB:Q8HZJ5, ECO:0000250|UniProtKB:Q99P74}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. SUBUNIT: Interacts with SYTL2, SYTL4, MYRIP and MLPH. Interacts with RPH3A and RPH3A. {ECO:0000269|PubMed:11956164, ECO:0000269|PubMed:12221080, ECO:0000269|PubMed:12578829, ECO:0000269|PubMed:16716193, ECO:0000269|PubMed:18940604}. TISSUE SPECIFICITY: Expressed abundantly in the stomach and is predominantly localized at the apical region of gastric-surface mucus cells. Also expressed in the brain and spleen. {ECO:0000269|PubMed:16716193}. +Q8BX09 RBBP5_MOUSE Retinoblastoma-binding protein 5 (RBBP-5) 538 59,098 Alternative sequence (2); Chain (1); Cross-link (1); Modified residue (6); Repeat (6); Sequence conflict (2) FUNCTION: As part of the MLL1/MLL complex, involved in mono-, di- and trimethylation at 'Lys-4' of histone H3. Histone H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. In embryonic stem (ES) cells, plays a crucial role in the differentiation potential, particularly along the neural lineage, regulating gene induction and H3 'Lys-4' methylation at key developmental loci, including that mediated by retinoic acid. Does not affect ES cell self-renewal. {ECO:0000269|PubMed:21335234}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the SET1 complex, at least composed of the catalytic subunit (SETD1A or SETD1B), WDR5, WDR82, RBBP5, ASH2L/ASH2, CXXC1/CFP1, CFC1 and DPY30 (By similarity). Interacts with WDR82 and SETD1A (By similarity). Part of a complex composed at least of ASCL2, EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; this complex may have a histone H3-specific methyltransferase activity (By similarity). Core component of several methyltransferase-containing complexes including MLL1/MLL, MLL2/3 (also named ASCOM complex) and MLL4/WBP7. Each complex is at least composed of ASH2L, RBBP5, DPY30, WDR5, one or more specific histone methyltransferases (KMT2A/MLL1, KMT2D/MLL2, KMT2C/MLL3 and KMT2B/MLL4), and the facultative components PAGR1, BAP18, CHD8, E2F6, HCFC1, HCFC2, HSP70, INO80C, KDM6A, KANSL1, LAS1L, MAX, MCRS1, MEN1, MGA, MYST1/MOF, NCOA6, PAXIP1/PTIP, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9, TEX10 and alpha- and beta-tubulin. Interacts with ZNF335. {ECO:0000250, ECO:0000269|PubMed:21335234, ECO:0000269|PubMed:23178126}. +P97950 RB33A_MOUSE Ras-related protein Rab-33A (Small GTP-binding protein S10) 237 26,541 Chain (1); Lipidation (2); Modified residue (1); Nucleotide binding (3) SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. TISSUE SPECIFICITY: Expressed predominantly in brain. Weak expression in ovary. +Q8BHC1 RB39B_MOUSE Ras-related protein Rab-39B 213 24,636 Chain (1); Lipidation (2); Modified residue (2); Motif (1); Nucleotide binding (3) FUNCTION: Small GTPases Rab involved in autophagy. The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (By similarity). May be involved in vesicular trafficking (PubMed:20159109). Plays a role in synapse formation. May regulate the homeostasis of SNCA/alpha-synuclein (PubMed:25434005). Together with PICK1 proposed to ensure selectively GRIA2 exit from the endoplasmic reticulum to the Golgi and to regulate AMPAR compostion at the post-synapses and thus synaptic transmission (PubMed:25784538). {ECO:0000250|UniProtKB:Q96DA2, ECO:0000269|PubMed:20159109, ECO:0000269|PubMed:25434005}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q96DA2}; Lipid-anchor {ECO:0000250|UniProtKB:Q96DA2}; Cytoplasmic side {ECO:0000250|UniProtKB:Q96DA2}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q96DA2}; Lipid-anchor {ECO:0000250|UniProtKB:Q96DA2}; Cytoplasmic side {ECO:0000250|UniProtKB:Q96DA2}. Golgi apparatus {ECO:0000269|PubMed:20159109}. Note=Partial colocalization with markers that cycle from the cell surface to the trans-Golgi network. {ECO:0000269|PubMed:20159109}. SUBUNIT: Interacts (in GTP-bound form) with PICK1 (via PDZ domain); a PICK1 homodimer may allow simultaneous association of RAB39B and GRIA2 to PICK1 which is involved in GRIA2 trafficking. {ECO:0000269|PubMed:25784538}. TISSUE SPECIFICITY: Specifically expressed in neuron and neuronal precursors in the brain. Expression is high in all regions of the brain with highest levels observed in the hippocampus. {ECO:0000269|PubMed:20159109}. +Q80UJ7 RB3GP_MOUSE Rab3 GTPase-activating protein catalytic subunit (RAB3 GTPase-activating protein 130 kDa subunit) (Rab3-GAP p130) (Rab3-GAP) 981 110,198 Chain (1); Erroneous initiation (1); Modified residue (7); Sequence conflict (12) FUNCTION: Probable catalytic subunit of a GTPase activating protein that has specificity for Rab3 subfamily (RAB3A, RAB3B, RAB3C and RAB3D). Rab3 proteins are involved in regulated exocytosis of neurotransmitters and hormones. Specifically converts active Rab3-GTP to the inactive form Rab3-GDP. Required for normal eye and brain development. May participate in neurodevelopmental processes such as proliferation, migration and differentiation before synapse formation, and non-synaptic vesicular release of neurotransmitters (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=In neurons, it is enriched in the synaptic soluble fraction. {ECO:0000250}. SUBUNIT: The Rab3 GTPase-activating complex is a heterodimer composed of RAB3GAP and RAB3-GAP150. The Rab3 GTPase-activating complex interacts with DMXL2. Interacts with LMAN1. {ECO:0000250|UniProtKB:P69735, ECO:0000250|UniProtKB:Q15042}. TISSUE SPECIFICITY: In the eye, it is highly expressed within the lens, particularly in the anterior lens epithelium and in a ring corresponding to the equatorial region where anterior cells are differentiating into lens fibers. Also highly expressed in the retina. {ECO:0000269|PubMed:15696165}. +Q9ESK9 RBCC1_MOUSE RB1-inducible coiled-coil protein 1 (Coiled-coil-forming protein 1) (FAK family kinase-interacting protein of 200 kDa) (FIP200) (LaXp180) 1588 182,350 Chain (1); Coiled coil (2); Compositional bias (1); Erroneous initiation (1); Modified residue (15); Motif (1); Sequence conflict (7) FUNCTION: Involved in autophagy (PubMed:23262492, PubMed:19258318). Regulates early events but also late events of autophagosome formation through direct interaction with Atg16L1 (PubMed:23392225, PubMed:23285000, PubMed:19258318). Required for the formation of the autophagosome-like double-membrane structure that surrounds the Salmonella-containing vacuole (SCV) during S.typhimurium infection and subsequent xenophagy (PubMed:21525242). Involved in repair of DNA damage caused by ionizing radiation, which subsequently improves cell survival by decreasing apoptosis (PubMed:21807966). Inhibits PTK2/FAK1 and PTK2B/PYK2 kinase activity, affecting their downstream signaling pathways (By similarity). Plays a role as a modulator of TGF-beta-signaling by restricting substrate specificity of RNF111 (PubMed:21795712). Functions as a DNA-binding transcription factor (PubMed:12095676). Is a potent regulator of the RB1 pathway through induction of RB1 expression (PubMed:15968549). Plays a crucial role in muscular differentiation (PubMed:15968549). Plays an indispensable role in fetal hematopoiesis and in the regulation of neuronal homeostasis (PubMed:19940130, PubMed:21088496). {ECO:0000250|UniProtKB:Q8TDY2, ECO:0000269|PubMed:12095676, ECO:0000269|PubMed:15968549, ECO:0000269|PubMed:19258318, ECO:0000269|PubMed:19940130, ECO:0000269|PubMed:21088496, ECO:0000269|PubMed:21525242, ECO:0000269|PubMed:21795712, ECO:0000269|PubMed:21807966, ECO:0000269|PubMed:23262492, ECO:0000269|PubMed:23285000, ECO:0000269|PubMed:23392225}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12095676}. Cytoplasm, cytosol {ECO:0000269|PubMed:19258318}. Cytoplasm {ECO:0000250|UniProtKB:Q8TDY2}. Preautophagosomal structure {ECO:0000269|PubMed:19258318}. Lysosome {ECO:0000250|UniProtKB:Q8TDY2}. Note=Under starvation conditions, is localized to puncate structures primarily representing the isolation membrane that sequesters a portion of the cytoplasm resulting in the formation of an autophagosome. {ECO:0000269|PubMed:19258318}. SUBUNIT: Part of a complex containing ATG13/KIAA0652, ULK1 and RB1CC1 (PubMed:19258318). This complex associates with ATG101 (By similarity). Interacts with PTK2/FAK1 and PTK2B/PYK2 (By similarity). Interacts with GABARAP and GABARAPL1 (By similarity). Interacts with ATG16L1; the interaction is required for ULK1 complex-dependent autophagy (PubMed:23392225, PubMed:23262492). Interacts with RNF111, SKI and SMAD7 (PubMed:21795712). Interacts with COP1 in the cytoplasm of proliferating cells in response to UV stimulation (By similarity). Interacts with TP53 (By similarity). Interacts with C9orf72 (By similarity). Interacts with WDR45B (PubMed:28561066). {ECO:0000250|UniProtKB:Q8TDY2, ECO:0000269|PubMed:19258318, ECO:0000269|PubMed:21795712, ECO:0000269|PubMed:23262492, ECO:0000269|PubMed:23392225, ECO:0000269|PubMed:28561066}. TISSUE SPECIFICITY: Expressed abundantly in heart and testis, and moderately in kidney, liver and skeletal muscles. Very low expression levels in lung and spleen. Colocalizes with RB1 in various tissues. {ECO:0000269|PubMed:12095676}. +Q6P3B9 RBFA_MOUSE Putative ribosome-binding factor A, mitochondrial 350 39,317 Chain (1); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}. +P47962 RL5_MOUSE 60S ribosomal protein L5 297 34,401 Chain (1); Cross-link (2); Initiator methionine (1); Modified residue (7) FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. As part of the 5S RNP/5S ribonucleoprotein particle it is an essential component of the LSU, required for its formation and the maturation of rRNAs. It also couples ribosome biogenesis to p53/TP53 activation. As part of the 5S RNP it accumulates in the nucleoplasm and inhibits MDM2, when ribosome biogenesis is perturbed, mediating the stabilization and the activation of TP53. Interacts with RRP1B. {ECO:0000250|UniProtKB:P46777}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P46777}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P46777}. SUBUNIT: Component of the large ribosomal subunit (LSU). Part of a LSU subcomplex, the 5S RNP which is composed of the 5S RNA, RPL5 and RPL11. Interacts with NVL in an ATP-dependent manner. {ECO:0000250|UniProtKB:P46777}. +Q64700 RBL2_MOUSE Retinoblastoma-like protein 2 (130 kDa retinoblastoma-associated protein) (p130) (Retinoblastoma-related protein 2) (RBR-2) (pRb2) 1135 127,485 Chain (1); Compositional bias (4); Modified residue (20); Region (4); Sequence conflict (13) FUNCTION: Key regulator of entry into cell division. Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation. Recruits and targets histone methyltransferases KMT5B and KMT5C, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-20' trimethylation. Probably acts as a transcription repressor by recruiting chromatin-modifying enzymes to promoters. Potent inhibitor of E2F-mediated trans-activation, associates preferentially with E2F5. Binds to cyclins A and E. Binds to and may be involved in the transforming capacity of the adenovirus E1A protein. May act as a tumor suppressor. {ECO:0000269|PubMed:15750587}. PTM: During G0 and early G1 phase of the cell cycle, phosphorylated on Ser-636 and on 5 sites within the domain B. Phosphorylation on Ser-669 in G1 leads to its ubiquitin-dependent proteolysis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with AATF and RINT1. Component of the DREAM complex (also named LINC complex) at least composed of E2F4, E2F5, LIN9, LIN37, LIN52, LIN54, MYBL1, MYBL2, RBL1, RBL2, RBBP4, TFDP1 and TFDP2. The complex exists in quiescent cells where it represses cell cycle-dependent genes. It dissociates in S phase when LIN9, LIN37, LIN52 and LIN54 form a subcomplex that binds to MYBL2. Interacts with USP4 (By similarity). Interacts with KMT5B, KMT5C and USP4. Interacts with PML (By similarity). {ECO:0000250}. +Q8BGC4 PTGR3_MOUSE Prostaglandin reductase-3 (PTGR-3) (EC 1.3.1.48) (15-oxoprostaglandin 13-reductase) (Zinc-binding alcohol dehydrogenase domain-containing protein 2) 377 40,529 Binding site (8); Chain (1); Modified residue (2); Nucleotide binding (1) FUNCTION: Functions as 15-oxo-prostaglandin 13-reductase and acts on 15-keto-PGE1, 15-keto-PGE2, 15-keto-PGE1-alpha and 15-keto-PGE2-alpha with highest efficienty towards 15-keto-PGE2-alpha. Overexpression represses transcriptional activity of PPARG and inhibits adipocyte differentiation. {ECO:0000269|PubMed:23821743}. SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:19091015}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:23821743}. +P42669 PURA_MOUSE Transcriptional activator protein Pur-alpha (Purine-rich single-stranded DNA-binding protein alpha) 321 34,884 Chain (1); Compositional bias (2); Initiator methionine (1); Modified residue (2) FUNCTION: This is a probable transcription activator that specifically binds the purine-rich single strand of the PUR element located upstream of the c-Myc gene. May play a role in the initiation of DNA replication and in recombination. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Homodimer, heterodimer with PURB and heterotrimer with PURB and YBX1/Y-box protein 1 (PubMed:10318844). Interacts with FMR1; this interaction occurs in association with polyribosome (PubMed:12147688). {ECO:0000269|PubMed:10318844, ECO:0000269|PubMed:12147688}. +Q9CYH2 PXL2A_MOUSE Peroxiredoxin-like 2A (Peroxiredoxin-like 2 activated in M-CSF stimulated monocytes) (Protein PAMM) (Redox-regulatory protein FAM213A) 218 24,395 Active site (2); Chain (1); Region (1) FUNCTION: Involved in redox regulation of the cell (By similarity). Acts as an antioxidant (By similarity). Inhibits TNFSF11-induced NFKB1 and JUN activation and osteoclast differentiation (By similarity). May affect bone resorption and help to maintain bone mass (By similarity). Acts as a negative regulator of macrophage-mediated inflammation by inhibiting macrophage production of inflammatory cytokines, probably through suppression of the MAPK signaling pathway (PubMed:26438880). {ECO:0000250|UniProtKB:Q9BRX8, ECO:0000269|PubMed:26438880}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BRX8}. Secreted {ECO:0000269|PubMed:26438880}. Note=Secreted from mature adipocytes but not from preadipocytes. {ECO:0000250|UniProtKB:Q9BRX8}. TISSUE SPECIFICITY: Expressed in kidney, liver, skin, and brain (PubMed:19951071). Widely expressed with highest levels detected in adipose tissue (PubMed:26438880). {ECO:0000269|PubMed:19951071, ECO:0000269|PubMed:26438880}. +Q9DB60 PXL2B_MOUSE Prostamide/prostaglandin F synthase (Prostamide/PG F synthase) (Prostamide/PGF synthase) (EC 1.11.1.20) (Peroxiredoxin-like 2B) 201 21,670 Chain (1); Modified residue (1); Mutagenesis (2) FUNCTION: Catalyzes the reduction of prostaglandin-ethanolamide H(2) (prostamide H(2)) to prostamide F(2alpha) with NADPH as proton donor. Also able to reduce prostaglandin H(2) to prostaglandin F(2alpha). {ECO:0000269|PubMed:18006499}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:18006499}. TISSUE SPECIFICITY: Mainly present in brain and spinal cord. In spinal cord, present in the superficial layer of the dorsal horn, in motor neurons of the ventral horn and in glia of the white matter of the spinal cord. In brain, expressed preferentially in the white matter bundles of the entire CNS of adult with less marked expression in neuronal cell bodies. Colocalizes with MBP in myelin sheaths but not in axons. Localizes to myelin sheaths (at protein level). {ECO:0000269|PubMed:18006499, ECO:0000269|PubMed:20950588}. +P42925 PXMP2_MOUSE Peroxisomal membrane protein 2 (22 kDa peroxisomal membrane protein) 194 22,266 Chain (1); Sequence conflict (4); Topological domain (4); Transmembrane (4) TRANSMEM 31 51 Helical. {ECO:0000255}.; TRANSMEM 75 95 Helical. {ECO:0000255}.; TRANSMEM 114 134 Helical. {ECO:0000255}.; TRANSMEM 173 193 Helical. {ECO:0000255}. TOPO_DOM 1 30 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 52 74 Peroxisomal. {ECO:0000255}.; TOPO_DOM 96 113 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 135 172 Peroxisomal. {ECO:0000255}. FUNCTION: Seems to be involved in pore-forming activity and may contribute to the unspecific permeability of the peroxisomal membrane. SUBCELLULAR LOCATION: Peroxisome membrane; Multi-pass membrane protein. SUBUNIT: Interacts with PEX19 and SIVA1. {ECO:0000250}. +Q8CHP5 PYM1_MOUSE Partner of Y14 and mago (PYM homolog 1 exon junction complex-associated factor) (Protein wibg homolog) 203 22,690 Alternative sequence (1); Chain (1); Coiled coil (2); Modified residue (4); Region (2); Sequence conflict (3) FUNCTION: Key regulator of the exon junction complex (EJC), a multiprotein complex that associates immediately upstream of the exon-exon junction on mRNAs and serves as a positional landmark for the intron exon structure of genes and directs post-transcriptional processes in the cytoplasm such as mRNA export, nonsense-mediated mRNA decay (NMD) or translation. Acts as an EJC disassembly factor, allowing translation-dependent EJC removal and recycling by disrupting mature EJC from spliced mRNAs. Its association with the 40S ribosomal subunit probably prevents a translation-independent disassembly of the EJC from spliced mRNAs, by restricting its activity to mRNAs that have been translated. Interferes with NMD and enhances translation of spliced mRNAs, probably by antagonizing EJC functions (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BRP8}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9BRP8}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9BRP8}. Note=Shuttles between the nucleus and the cytoplasm. Nuclear export is mediated by XPO1/CRM1. {ECO:0000250|UniProtKB:Q9BRP8}. SUBUNIT: Interacts (via N-terminus) with MAGOH and RBM8A; the interaction is direct. Associates (eIF2A-like region) with the 40S ribosomal subunit and the 48S preinitiation complex (By similarity). {ECO:0000250}. DOMAIN: The eIF2A-like region shares sequence similarity with eIF2A and mediates the interaction with the 40S ribosomal subunit and the 48S preinitiation complex. {ECO:0000250}. +Q3TMV7 PYRD1_MOUSE Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 1 (EC 1.8.1.-) 498 55,592 Chain (1); Modified residue (1); Sequence conflict (7) FUNCTION: Probable FAD-dependent oxidoreductase; involved in the cellular oxidative stress response (By similarity). Required for normal sarcomere structure and muscle fiber integrity (By similarity). {ECO:0000250|UniProtKB:Q6PBT5, ECO:0000250|UniProtKB:Q8WU10}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:30169133}. Cytoplasm {ECO:0000269|PubMed:30169133}. Cytoplasm, myofibril, sarcomere {ECO:0000250|UniProtKB:Q8WU10}. +Q9D1G1 RAB1B_MOUSE Ras-related protein Rab-1B 201 22,187 Chain (1); Lipidation (2); Modified residue (3); Motif (1); Nucleotide binding (5); Region (1) FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. RAB1B regulates vesicular transport between the endoplasmic reticulum and successive Golgi compartments. Plays a role in the initial events of the autophagic vacuole development which take place at specialized regions of the endoplasmic reticulum. {ECO:0000250|UniProtKB:Q9H0U4}. PTM: Prenylated; by GGTase II, only after interaction of the substrate with Rab escort protein 1 (REP1). {ECO:0000250|UniProtKB:Q9H0U4}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H0U4}. Membrane {ECO:0000250|UniProtKB:Q9H0U4}; Lipid-anchor {ECO:0000250|UniProtKB:Q9H0U4}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9H0U4}. Preautophagosomal structure membrane {ECO:0000250|UniProtKB:Q9H0U4}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Targeted by REP1 to membranes of specific subcellular compartments including endoplasmic reticulum, Golgi apparatus, and intermediate vesicles between these two compartments. In the GDP-form, colocalizes with GDI in the cytoplasm. {ECO:0000250|UniProtKB:Q9H0U4}. SUBUNIT: Interacts with MICAL1 and MICAL2. Interacts (GTP-bound form) with MICALCL, MICAL1 and MILCAL3. Interacts with GDI1; the interaction requires the GDP-bound state. Interacts with CHM/REP1; the interaction requires the GDP-bound form and is necessary for prenylation by GGTase II. {ECO:0000250|UniProtKB:Q9H0U4}. +O35551 RABE1_MOUSE Rab GTPase-binding effector protein 1 (Rabaptin-5) (Rabaptin-5alpha) 862 99,524 Alternative sequence (7); Chain (1); Coiled coil (2); Erroneous initiation (1); Initiator methionine (1); Modified residue (7); Sequence conflict (5) FUNCTION: Rab effector protein acting as linker between gamma-adaptin, RAB4A and RAB5A. Involved in endocytic membrane fusion and membrane trafficking of recycling endosomes. Involved in KCNH1 channels trafficking to and from the cell membrane. Stimulates RABGEF1 mediated nucleotide exchange on RAB5A. Mediates the traffic of PKD1:PKD2 complex from the endoplasmic reticulum through the Golgi to the cilium (PubMed:25405894). {ECO:0000250|UniProtKB:Q15276, ECO:0000269|PubMed:25405894}. PTM: Proteolytic cleavage by caspases in apoptotic cells causes loss of endosome fusion activity. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Early endosome {ECO:0000250}. Recycling endosome {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. SUBUNIT: Heterodimer with RABGEF1. The heterodimer binds RAB4A and RAB5A that have been activated by GTP-binding. Binds TSC2, GGA2, GGA3, AP1G1 and AP1G2 (By similarity). Interacts with ECPAS (By similarity). Interacts with KCNH1 (PubMed:22841712). Interacts with PKD1 (via C-terminal domain) and GGA1; the interactions recruit PKD1:PKD2 complex to GGA1 and ARL3 at trans-Golgi network (PubMed:25405894). Interacts with KCNH1 (By similarity). {ECO:0000250|UniProtKB:O35550, ECO:0000250|UniProtKB:Q15276, ECO:0000269|PubMed:22841712, ECO:0000269|PubMed:25405894}. +Q8VCH5 RABEK_MOUSE Rab9 effector protein with kelch motifs 380 41,119 Chain (1); Repeat (6) FUNCTION: Rab9 effector required for endosome to trans-Golgi network (TGN) transport. {ECO:0000250}. PTM: Phosphorylated on Ser residues most probably by PIP5K3. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Endosome membrane. Note=Interaction with PIP5K3 and subsequent phosphorylation recruits it to the endosomal membrane. {ECO:0000250}. SUBUNIT: Interacts with PIP5K3. Interacts with RAB9 in its GTP-bound conformation (By similarity). {ECO:0000250}. +Q7TQP4 RL3R2_MOUSE Relaxin-3 receptor 2 (RLN3 receptor 2) (G-protein coupled receptor 100) (Insulin-like peptide INSL5 receptor) (Relaxin family peptide receptor 4) 414 45,460 Chain (1); Compositional bias (1); Disulfide bond (1); Glycosylation (2); Sequence conflict (1); Topological domain (8); Transmembrane (7) TRANSMEM 44 64 Helical; Name=1. {ECO:0000255}.; TRANSMEM 78 98 Helical; Name=2. {ECO:0000255}.; TRANSMEM 117 137 Helical; Name=3. {ECO:0000255}.; TRANSMEM 156 176 Helical; Name=4. {ECO:0000255}.; TRANSMEM 210 230 Helical; Name=5. {ECO:0000255}.; TRANSMEM 256 276 Helical; Name=6. {ECO:0000255}.; TRANSMEM 294 316 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 43 Extracellular. {ECO:0000255}.; TOPO_DOM 65 77 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 99 116 Extracellular. {ECO:0000255}.; TOPO_DOM 138 155 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 177 209 Extracellular. {ECO:0000255}.; TOPO_DOM 231 255 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 277 293 Extracellular. {ECO:0000255}.; TOPO_DOM 317 414 Cytoplasmic. {ECO:0000255}. FUNCTION: High affinity receptor for INSL5. Also acts as receptor for RLN3/relaxin-3, as well as bradykinin and kallidin. Binding of the ligand inhibit cAMP accumulation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Detected only in bone marrow. +Q08297 RAD51_MOUSE DNA repair protein RAD51 homolog 1 (RAD51 homolog A) 339 36,971 Chain (1); Cross-link (2); Domain (1); Initiator methionine (1); Modified residue (3); Motif (1); Nucleotide binding (1); Region (1) FUNCTION: Plays an important role in homologous strand exchange, a key step in DNA repair through homologous recombination (HR) (PubMed:15834424). Binds to single and double-stranded DNA and exhibits DNA-dependent ATPase activity. Catalyzes the recognition of homology and strand exchange between homologous DNA partners to form a joint molecule between a processed DNA break and the repair template. Binds to single-stranded DNA in an ATP-dependent manner to form nucleoprotein filaments which are essential for the homology search and strand exchange. Part of a PALB2-scaffolded HR complex containing BRCA2 and RAD51C and which is thought to play a role in DNA repair by HR. Plays a role in regulating mitochondrial DNA copy number under conditions of oxidative stress in the presence of RAD51C and XRCC3. Also involved in interstrand cross-link repair (By similarity). {ECO:0000250|UniProtKB:Q06609, ECO:0000269|PubMed:15834424}. PTM: Ubiquitinated by the SCF(FBH1) E3 ubiquitin ligase complex, regulating RAD51 subcellular location and preventing its association with DNA. Ubiquitinated by RFWD3 in response to DNA damage: ubiquitination leads to degradation by the proteasome, promoting homologous recombination. {ECO:0000250|UniProtKB:Q06609}.; PTM: Phosphorylated. Phosphorylation of Thr-309 by CHEK1 may enhance association with chromatin at sites of DNA damage and promote DNA repair by homologous recombination. Phosphorylation by ABL1 inhibits function. {ECO:0000250|UniProtKB:Q06609}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q06609}. Cytoplasm {ECO:0000250|UniProtKB:Q06609}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q06609}. Mitochondrion matrix {ECO:0000250|UniProtKB:Q06609}. Chromosome {ECO:0000250|UniProtKB:Q06609}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q06609}. Note=Colocalizes with RAD51AP1 and RPA2 to multiple nuclear foci upon induction of DNA damage. DNA damage induces an increase in nuclear levels. Together with FIGNL1, redistributed in discrete nuclear DNA damage-induced foci after ionizing radiation (IR) or camptothecin (CPT) treatment. Accumulated at sites of DNA damage in a SPIDR-dependent manner. Recruited at sites of DNA damage in a MCM9-MCM8-dependent manner. {ECO:0000250|UniProtKB:Q06609}. SUBUNIT: Forms linear homooligomers, giving rise to a RAD51 nucleoprotein filament, which is essential for strand-pairing reactions during DNA recombination. Interacts with BRCA1 and either directly or indirectly with p53. Interacts with XRCC3, RAD54L and RAD54B. Interacts with the BCDX2 subcomplex RAD51C:RAD51B. Interacts directly with PALB2 which may serve as a scaffold for a HR complex containing PALB2, BRCA2, RAD51C, RAD51 and XRCC3. Interacts with RAD51AP1 and RAD51AP2. Interacts with CHEK1, and this may require prior phosphorylation of CHEK1 (By similarity). Interacts with the MND1-PSMC3IP heterodimer (PubMed:15834424). Found in a complex, at least composed of BLM, RAD51 and SPIDR; the complex formation is mediated by SPIDR. Interacts with SPIDR; the interaction is direct and recruits RAD51 to DNA damage sites. Interacts with FIGNL1 (via N-terminal one-half region); the interaction is direct. Interacts with RAD51AP1 (via C-terminal region); the interaction is direct (By similarity). Interacts with NABP2, RPA1, PALB2 and RAD51. Interacts with SWI5/C9orf119, and at lower level with SFR1/MEIR5 (PubMed:20976249). Interacts with hyperphosphorylated RPA2; this interaction is necessary for efficient recruitment to chromatin in response to DNA damage. Interacts with SWSAP1; involved in homologous recombination repair. Interacts with PARPBP, BRCA2 and RECQL5; these interactions interfere with the formation of the RAD51-DNA homologous recombination structure. Interacts with POLQ; POLQ acts as an inhibitor of homology-recombination repair (HR) pathway by limiting RAD51 accumulation at resected ends. Interacts with POLN (By similarity). Interacts with FBH1 (PubMed:24108124). Interacts with RFWD3 (By similarity). Interacts with the MCM8-MCM9 complex; the interaction recruits RAD51 to DNA damage sites (By similarity). {ECO:0000250|UniProtKB:Q06609, ECO:0000269|PubMed:15834424, ECO:0000269|PubMed:20976249, ECO:0000269|PubMed:24108124}. TISSUE SPECIFICITY: Expressed in ovary and testis. Expressed in the brain. {ECO:0000269|PubMed:22305526}. +P70388 RAD50_MOUSE DNA repair protein RAD50 (mRad50) (EC 3.6.-.-) 1312 153,488 Alternative sequence (4); Chain (1); Coiled coil (5); Compositional bias (1); Domain (1); Metal binding (2); Modified residue (3); Mutagenesis (1); Nucleotide binding (1); Sequence conflict (5) FUNCTION: Component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis. The complex possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by MRE11. RAD50 may be required to bind DNA ends and hold them in close proximity. This could facilitate searches for short or long regions of sequence homology in the recombining DNA templates, and may also stimulate the activity of DNA ligases and/or restrict the nuclease activity of MRE11 to prevent nucleolytic degradation past a given point. The complex may also be required for DNA damage signaling via activation of the ATM kinase. In telomeres the MRN complex may modulate t-loop formation (By similarity). {ECO:0000250, ECO:0000269|PubMed:10377422, ECO:0000269|PubMed:12208847}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92878}. Chromosome, telomere {ECO:0000250|UniProtKB:Q92878}. Chromosome {ECO:0000250|UniProtKB:Q92878}. Note=Localizes to discrete nuclear foci after treatment with genotoxic agents. {ECO:0000250|UniProtKB:Q92878}. SUBUNIT: Component of the MRN complex composed of two heterodimers RAD50/MRE11 associated with a single NBN. As part of the MRN complex, interacts with MCM8 and MCM9; the interaction recruits the complex to DNA repair sites. Component of the BASC complex, at least composed of BRCA1, MSH2, MSH6, MLH1, ATM, BLM, RAD50, MRE11 and NBN. Found in a complex with TERF2. Interacts with RINT1. Interacts with BRCA1 via its N-terminal domain. Interacts with DCLRE1C/Artemis. Interacts with MRNIP. {ECO:0000250|UniProtKB:Q92878}. DOMAIN: The zinc-hook, which separates the large intramolecular coiled coil regions, contains 2 Cys residues that coordinate one molecule of zinc with the help of the 2 Cys residues of the zinc-hook of another RAD50 molecule, thereby forming a V-shaped homodimer. The two heads of the homodimer, which constitute the ATP-binding domain, interact with the MRE11 homodimer (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: In adult, it is expressed at very low level in most tissues, except in heart, lung and aorta. Expressed at high level in testis. {ECO:0000269|PubMed:8910585}. +P43352 RAD52_MOUSE DNA repair protein RAD52 homolog 420 46,910 Chain (1); DNA binding (1); Modified residue (3); Region (1); Sequence conflict (7) FUNCTION: Involved in double-stranded break repair. Plays a central role in genetic recombination and DNA repair by promoting the annealing of complementary single-stranded DNA and by stimulation of the RAD51 recombinase (By similarity). {ECO:0000250}. PTM: Phosphorylated upon DNA damage by ABL1, and probably by ATM or ATR. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: The full-length protein forms heptameric rings. Interacts with ABL1. Interacts with RPA2; the interaction is direct and associates RAD52 with the RPA complex (By similarity). {ECO:0000250}. +P70270 RAD54_MOUSE DNA repair and recombination protein RAD54-like (EC 3.6.4.-) (RAD54 homolog) (mHR54) (mRAD54) 747 84,694 Chain (1); Domain (2); Modified residue (1); Motif (1); Nucleotide binding (1); Region (1); Sequence conflict (3) FUNCTION: Involved in DNA repair and mitotic recombination. Functions in the recombinational DNA repair (RAD52) pathway. Dissociates RAD51 from nucleoprotein filaments formed on dsDNA. Could be involved in the turnover of RAD51 protein-dsDNA filaments (By similarity). Deficient mice also show significantly shorter telomeres than wild-type controls, indicating that the protein activity plays an essential role in telomere length maintenance in mammals. Deficiency also resulted in an increased frequency of end-to-end chromosome fusions involving telomeres compared to the controls, suggesting a putative role in telomere capping. Non-homologous end joining (NHEJ) and homologous recombination (HR) represent the two major pathways of DNA double-strand break (DSB) repair in eukaryotic cells. LIG4 and RAD54L cooperate to support cellular proliferation, repair spontaneous DSBs, and prevent chromosome and single chromatid aberrations. {ECO:0000250, ECO:0000269|PubMed:10209103, ECO:0000269|PubMed:10757799, ECO:0000269|PubMed:12218123, ECO:0000269|PubMed:12531026, ECO:0000269|PubMed:12548566, ECO:0000269|PubMed:12897131, ECO:0000269|PubMed:15175260, ECO:0000269|PubMed:9108475}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Interacts (via N-terminus) with RAD51. {ECO:0000250}. TISSUE SPECIFICITY: Hardly detectable in most tissues. Dramatically increased in thymus, spleen and testis. {ECO:0000269|PubMed:8805304}. +O08602 RAE1A_MOUSE Retinoic acid early-inducible protein 1-alpha (RAE-1-alpha) 253 28,616 Chain (1); Disulfide bond (2); Glycosylation (5); Lipidation (1); Propeptide (1); Signal peptide (1) FUNCTION: Acts as a ligand for KLRK1. {ECO:0000269|PubMed:10894171}. PTM: Glycosylated. {ECO:0000269|PubMed:8982867}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10894171, ECO:0000269|PubMed:8982867}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:10894171, ECO:0000269|PubMed:8982867}. TISSUE SPECIFICITY: Expressed predominantly in embryonic brain. {ECO:0000269|PubMed:8982867}. +Q9QXG2 RAE1_MOUSE Rab proteins geranylgeranyltransferase component A 1 (Choroideremia protein homolog) (Rab escort protein 1) (REP-1) 665 73,977 Chain (1); Sequence conflict (1) FUNCTION: Substrate-binding subunit of the Rab geranylgeranyltransferase (GGTase) complex. Binds unprenylated Rab proteins and presents the substrate peptide to the catalytic component B composed of RABGGTA and RABGGTB, and remains bound to it after the geranylgeranyl transfer reaction. The component A is thought to be regenerated by transferring its prenylated Rab back to the donor membrane. Besides, a pre-formed complex consisting of CHM and the Rab GGTase dimer (RGGT or component B) can bind to and prenylate Rab proteins; this alternative pathway is proposed to be the predominant pathway for Rab protein geranylgeranylation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. SUBUNIT: Monomer. Heterotrimer composed of RABGGTA, RABGGTB and CHM; within this trimer, RABGGTA and RABGGTB form the catalytic component B, while CHM (component A) mediates Rab protein binding. Can associate with the Rab GGTase dimer (RGGT or component B) prior to Rab protein binding; the association is stabilized by geranylgeranyl pyrophosphate (GGpp). The CHM:RGGT:Rab complex is destabilized by GGpp. Interacts with RAB1A, RAB1B, RAB7A and RAB27A and mediates their prenylation (By similarity). {ECO:0000250}. +Q9Z0F6 RAD9A_MOUSE Cell cycle checkpoint control protein RAD9A (mRAD9) (EC 3.1.11.2) (DNA repair exonuclease rad9 homolog A) (Rad9-like protein) 389 42,059 Chain (1); Modified residue (6); Region (2) FUNCTION: Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair. The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex. Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3'-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage activity on substrates with double, nick, or gap flaps of distinct sequences and lengths; and DNA ligase I (LIG1) on long-patch base excision repair substrates. The 9-1-1 complex is necessary for the recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring during the S phase. RAD9A possesses 3'->5' double stranded DNA exonuclease activity (By similarity). {ECO:0000250}. PTM: Constitutively phosphorylated on serine and threonine amino acids in absence of DNA damage. Hyperphosphorylated by PRKCD and ABL1 upon DNA damage. Its phosphorylation by PRKCD may be required for the formation of the 9-1-1 complex (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the toroidal 9-1-1 (RAD9-RAD1-HUS1) complex, composed of RAD9A, RAD1 and HUS1. The 9-1-1 complex associates with LIG1, POLB, FEN1, RAD17, HDAC1, RPA1 and RPA2. The 9-1-1 complex associates with the RAD17-RFC complex. RAD9A interacts with BCL2L1, FEN1, PRKCD, RAD9B, HUS1, RAD1, ABL1, RPA1 and RPA2. Interacts with DNAJC7 and RHNO1 (By similarity). Interacts with ATAD5. {ECO:0000250, ECO:0000269|PubMed:15983387}. TISSUE SPECIFICITY: Expressed in heart, brain, spleen, lung, liver, skeletal muscle, kidney and testis. {ECO:0000269|PubMed:9766521}. +P21784 RAG2_MOUSE V(D)J recombination-activating protein 2 (RAG-2) 527 59,074 Beta strand (39); Chain (1); Compositional bias (1); Helix (6); Metal binding (8); Mutagenesis (19); Turn (5); Zinc finger (1) FUNCTION: Core component of the RAG complex, a multiprotein complex that mediates the DNA cleavage phase during V(D)J recombination. V(D)J recombination assembles a diverse repertoire of immunoglobulin and T-cell receptor genes in developing B and T-lymphocytes through rearrangement of different V (variable), in some cases D (diversity), and J (joining) gene segments. DNA cleavage by the RAG complex occurs in 2 steps: a first nick is introduced in the top strand immediately upstream of the heptamer, generating a 3'-hydroxyl group that can attack the phosphodiester bond on the opposite strand in a direct transesterification reaction, thereby creating 4 DNA ends: 2 hairpin coding ends and 2 blunt, 5'-phosphorylated ends. The chromatin structure plays an essential role in the V(D)J recombination reactions and the presence of histone H3 trimethylated at 'Lys-4' (H3K4me3) stimulates both the nicking and haipinning steps. The RAG complex also plays a role in pre-B cell allelic exclusion, a process leading to expression of a single immunoglobulin heavy chain allele to enforce clonality and monospecific recognition by the B-cell antigen receptor (BCR) expressed on individual B-lymphocytes. The introduction of DNA breaks by the RAG complex on one immunoglobulin allele induces ATM-dependent repositioning of the other allele to pericentromeric heterochromatin, preventing accessibility to the RAG complex and recombination of the second allele. In the RAG complex, RAG2 is not the catalytic component but is required for all known catalytic activities mediated by RAG1. It probably acts as a sensor of chromatin state that recruits the RAG complex to H3K4me3. {ECO:0000269|PubMed:16111638, ECO:0000269|PubMed:19448632, ECO:0000269|PubMed:19524534, ECO:0000269|PubMed:2360047, ECO:0000269|PubMed:8521468, ECO:0000269|PubMed:9094713}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Component of the RAG complex composed of core components RAG1 and RAG2, and associated component HMGB1 or HMGB2. {ECO:0000269|PubMed:15964836, ECO:0000269|PubMed:18025461, ECO:0000269|PubMed:9094713, ECO:0000269|PubMed:9184213}. DOMAIN: The atypical PHD-type zinc finger recognizes and binds histone H3 trimethylated on 'Lys-4' (H3K4me3). The presence Tyr-445 instead of a carboxylate in classical PHD-type zinc fingers results in an enhanced binding to H3K4me3 in presence of dimethylated on 'Arg-2' (H3R2me2) rather than inhibited. The atypical PHD-type zinc finger also binds various phosphoinositides, such as phosphatidylinositol 3,4-bisphosphate binding (PtdIns(3,4)P2), phosphatidylinositol 3,5-bisphosphate binding (PtdIns(3,5)P2), phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) and phosphatidylinositol 3,4,5-trisphosphate binding (PtdIns(3,4,5)P3). {ECO:0000269|PubMed:18025461, ECO:0000269|PubMed:18033247}. TISSUE SPECIFICITY: Maturing lymphoid cells. +Q99N57 RAF1_MOUSE RAF proto-oncogene serine/threonine-protein kinase (EC 2.7.11.1) (Proto-oncogene c-RAF) (cRaf) (Raf-1) 648 72,917 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Domain (2); Metal binding (8); Modified residue (22); Nucleotide binding (1); Region (1); Sequence conflict (2); Zinc finger (1) FUNCTION: Serine/threonine-protein kinase that acts as a regulatory link between the membrane-associated Ras GTPases and the MAPK/ERK cascade, and this critical regulatory link functions as a switch determining cell fate decisions including proliferation, differentiation, apoptosis, survival and oncogenic transformation. RAF1 activation initiates a mitogen-activated protein kinase (MAPK) cascade that comprises a sequential phosphorylation of the dual-specific MAPK kinases (MAP2K1/MEK1 and MAP2K2/MEK2) and the extracellular signal-regulated kinases (MAPK3/ERK1 and MAPK1/ERK2). The phosphorylated form of RAF1 (on residues Ser-338 and Ser-339, by PAK1) phosphorylates BAD/Bcl2-antagonist of cell death at 'Ser-75'. Phosphorylates adenylyl cyclases: ADCY2, ADCY5 and ADCY6, resulting in their activation. Phosphorylates PPP1R12A resulting in inhibition of the phosphatase activity. Phosphorylates TNNT2/cardiac muscle troponin T. Can promote NF-kB activation and inhibit signal transducers involved in motility (ROCK2), apoptosis (MAP3K5/ASK1 and STK3/MST2), proliferation and angiogenesis (RB1). Can protect cells from apoptosis also by translocating to the mitochondria where it binds BCL2 and displaces BAD/Bcl2-antagonist of cell death. Plays a role in the oncogenic transformation of epithelial cells via repression of the TJ protein, occludin (OCLN) by inducing the up-regulation of a transcriptional repressor SNAI2/SLUG, which induces down-regulation of OCLN. Restricts caspase activation in response to selected stimuli, notably Fas stimulation, pathogen-mediated macrophage apoptosis, and erythroid differentiation (By similarity). Regulates Rho signaling and migration, and is required for normal wound healing. {ECO:0000250, ECO:0000269|PubMed:15753127}. PTM: Phosphorylation at Thr-269, Ser-338, Tyr-341, Thr-491 and Ser-494 results in its activation. Phosphorylation at Ser-29, Ser-43, Ser-289, Ser-296, Ser-301 and Ser-642 by MAPK1/ERK2 results in its inactivation. Phosphorylation at Ser-259 induces the interaction with YWHAZ and inactivates kinase activity. Dephosphorylation of Ser-259 by the complex containing protein phosphatase 1, SHOC2 and M-Ras/MRAS relieves inactivation, leading to stimulate RAF1 activity. Phosphorylation at Ser-338 by PAK1 and PAK5 and Ser-339 by PAK1 is required for its mitochondrial localization (By similarity). Phosphorylation at Ser-621 in response to growth factor treatment stabilizes the protein, possibly by preventing proteasomal degradation. Phosphorylation at Ser-289, Ser-296, Ser-301, Ser-338 and Ser-621 are somehow linked to the methylation potential of cells. Treatment of cells with HGF in the presence of the methylation inhibitor 5'-methylthioadenosine (MTA) results in increased phosphorylation at Ser-338 and Ser-621 and decreased phosphorylation at Ser-296, Ser-301 and Ser-338. Dephosphorylation at SER-338 by PPP5C results in a decreased of activity (By similarity). {ECO:0000250}.; PTM: Methylated at Arg-563 in response to EGF treatment. This modification leads to destabilization of the protein, possibly through proteasomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Mitochondrion {ECO:0000250}. Nucleus {ECO:0000269|PubMed:19298812}. Note=Colocalizes with RGS14 and BRAF in both the cytoplasm and membranes. Phosphorylation at Ser-259 impairs its membrane accumulation. Recruited to the cell membrane by the active Ras protein. Phosphorylation at Ser-338 and Ser-339 by PAK1 is required for its mitochondrial localization (By similarity). Retinoic acid-induced Ser-621 phosphorylated form of RAF1 is predominantly localized at the nucleus. {ECO:0000250}. SUBUNIT: Monomer (By similarity). Homodimer (By similarity). Heterodimerizes with BRAF and this heterodimer possesses a highly increased kinase activity compared to the respective homodimers or monomers (By similarity). Heterodimerization is mitogen-regulated and enhanced by 14-3-3 proteins (By similarity). MAPK1/ERK2 activation can induce a negative feedback that promotes the dissociation of the heterodimer (By similarity). Forms a multiprotein complex with Ras (M-Ras/MRAS), SHOC2 and protein phosphatase 1 (PPP1CA, PPP1CB and PPP1CC) (By similarity). Interacts with Ras proteins; the interaction is antagonized by RIN1 (By similarity). Weakly interacts with RIT1 (By similarity). Interacts (via N-terminus) with RGS14 (via RBD domains); the interaction mediates the formation of a ternary complex with BRAF, a ternary complex inhibited by GNAI1 (By similarity). Probably forms a complex composed of chaperones HSP90 and HSP70, co-chaperones CDC37, PPP5C, TSC1 and client protein TSC2, CDK4, AKT, RAF1 and NR3C1; this complex does not contain co-chaperones STIP1/HOP and PTGES3/p23 (By similarity). Interacts with STK3/MST2; the interaction inhibits its pro-apoptotic activity (By similarity). Interacts (when phosphorylated at Ser-259) with YWHAZ (unphosphorylated at 'Thr-232') (By similarity). Interacts with MAP2K1/MEK1 and MAP2K2/MEK2 (By similarity). Interacts with MAP3K5/ASF1 (via N-terminus) and this interaction inhibits the proapoptotic function of MAP3K5/ASK1 (By similarity). Interacts with PAK1 (via kinase domain) (By similarity). The Ser-338 and Ser-339 phosphorylated form (by PAK1) interacts with BCL2 (By similarity). Interacts with PEBP1/RKIP and this interaction is enhanced if RAF1 is phosphorylated on residues Ser-338, Ser-339, Tyr-340 and Tyr-341 (By similarity). Interacts with ADCY2, ADCY5, ADCY6, DGKH, RCAN1/DSCR1, PPP1R12A, PKB/AKT1, SPRY2, SPRY4, CNKSR1/CNK1, KSR2 and PHB/prohibitin (By similarity). The phosphorylated form interacts with PIN1 (PubMed:15664191). Interacts with PPP2CA, PPP2R1B and ROCK2 (PubMed:15753127, PubMed:15664191). In its active form, interacts with PRMT5 (By similarity). Interacts with FAM83B; displaces 14-3-3 proteins from RAF1 and activates RAF1 (By similarity). Interacts with PDE8A; the interaction promotes RAF1 activity (By similarity). Interacts with MFHAS1 (By similarity). {ECO:0000250|UniProtKB:P04049, ECO:0000250|UniProtKB:P11345, ECO:0000269|PubMed:15664191, ECO:0000269|PubMed:15753127}. TISSUE SPECIFICITY: Present in all tissues tested: testis, ovary, small intestine, colon, peripheral blood leukocytes, fetal liver, bone marrow, thymus, lymph node and spleen, and the cell lines melanoma G-361, lung carcinoma A-549, colorectal adenocarcinoma SW480, Burkitt's lymphoma Raji and lymphoblastic leukemia MOLT-4. In skeletal muscle, isoform 1 is more abundant than isoform 2. {ECO:0000269|PubMed:11597136, ECO:0000269|PubMed:1886707}. +Q8CB96 RASF4_MOUSE Ras association domain-containing protein 4 322 36,934 Alternative sequence (3); Chain (1); Domain (2); Frameshift (1); Modified residue (1); Sequence conflict (3) FUNCTION: Potential tumor suppressor. May act as a KRAS effector protein. May promote apoptosis and cell cycle arrest. SUBUNIT: Interacts directly with activated KRAS in a GTP-dependent manner. {ECO:0000250}. +Q80UQ2 RASF6_MOUSE Ras association domain-containing protein 6 353 41,252 Alternative sequence (2); Chain (1); Domain (2); Erroneous initiation (1); Modified residue (2) FUNCTION: Involved in the induction of apoptosis. May act as a Ras effector protein. May suppress the serum-induced basal levels of NF-kappa-B. {ECO:0000269|PubMed:17404571}. SUBUNIT: Interacts with MOAP1. Interaction with activated KRAS is still a matter of debate: interaction has been shown in the mouse (PubMed:17404571), but not in human (PubMed:17367779). Lack of interaction with MRAS, NRAS nor RRAS2 has also been reported (PubMed:17367779). {ECO:0000269|PubMed:17404571}. +Q9DD19 RASF7_MOUSE Ras association domain-containing protein 7 359 39,247 Chain (1); Coiled coil (2); Compositional bias (2); Domain (1); Sequence conflict (3) FUNCTION: Negatively regulates stress-induced JNK activation and apoptosis by promoting MAP2K7 phosphorylation and inhibiting its ability to activate JNK. Following prolonged stress, anti-apoptotic effect stops because of degradation of RASSF7 protein via the ubiquitin-proteasome pathway. Required for the activation of AURKB and chromosomal congression during mitosis where it stimulates microtubule polymerization (By similarity). {ECO:0000250}. PTM: Polyubiquitinated and degraded by the proteasome upon prolonged stress stimuli. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Note=Colocalizes with gamma-tubulin. {ECO:0000250}. SUBUNIT: Interacts with MAP2K7 and GTP-bound NRAS. {ECO:0000250}. +Q8K342 RASF9_MOUSE Ras association domain-containing protein 9 (PAM COOH-terminal interactor protein 1) (P-CIP1) (Peptidylglycine alpha-amidating monooxygenase COOH-terminal interactor) 435 49,582 Chain (1); Coiled coil (1); Domain (1); Sequence conflict (3) FUNCTION: May play a role in regulating vesicuar trafficking in cells. {ECO:0000250}. SUBCELLULAR LOCATION: Endosome. Note=Accumulates on perinuclear endosomes. {ECO:0000250}. SUBUNIT: Interacts with PAM. {ECO:0000250}. +Q8BL43 RASFA_MOUSE Ras association domain-containing protein 10 508 57,333 Chain (1); Coiled coil (2); Compositional bias (1); Domain (1); Erroneous initiation (1); Frameshift (1); Sequence caution (1); Sequence conflict (1) FUNCTION: Plays an important role in regulating embryonic neurogenesis. {ECO:0000269|PubMed:29490266}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. TISSUE SPECIFICITY: Expressed in neural progenitor cells (at protein level). {ECO:0000269|PubMed:29490266}. +P62492 RB11A_MOUSE Ras-related protein Rab-11A (Rab-11) 216 24,394 Chain (1); Initiator methionine (1); Lipidation (2); Modified residue (2); Motif (1); Nucleotide binding (5); Propeptide (1); Sequence conflict (1) FUNCTION: The small GTPases Rab areR key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab regulates endocytic recycling. Acts as a major regulator of membrane delivery during cytokinesis. Together with MYO5B and RAB8A participates in epithelial cell polarization. Together with RAB3IP, RAB8A, the exocyst complex, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis. Together with MYO5B participates in CFTR trafficking to the plasma membrane and TF (Transferrin) recycling in nonpolarized cells. Required in a complex with MYO5B and RAB11FIP2 for the transport of NPC1L1 to the plasma membrane. Participates in the sorting and basolateral transport of CDH1 from the Golgi apparatus to the plasma membrane. Regulates the recycling of FCGRT (receptor of Fc region of monomeric Ig G) to basolateral membranes (By similarity). May also play a role in melanosome transport and release from melanocytes. {ECO:0000250, ECO:0000269|PubMed:21291502}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P62491}; Lipid-anchor {ECO:0000305}. Recycling endosome membrane {ECO:0000269|PubMed:29514919}; Lipid-anchor {ECO:0000305}. Cleavage furrow {ECO:0000250|UniProtKB:P62491}. Cytoplasmic vesicle, phagosome {ECO:0000250|UniProtKB:P62491}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P62491}. Note=Translocates with RAB11FIP2 from the vesicles of the endocytic recycling compartment (ERC) to the plasma membrane. Localizes to the cleavage furrow. Colocalizes with PARD3, PRKCI, EXOC5, OCLN, PODXL and RAB8A in apical membrane initiation sites (AMIS) during the generation of apical surface and lumenogenesis. Recruited to phagosomes containing S.aureus or M.tuberculosis. {ECO:0000250|UniProtKB:P62491}. SUBUNIT: Interacts with RAB11FIP1, RAB11FIP2, RAB11FIP3 (via its C-terminus) and RAB11FIP4 (By similarity). Interacts with EVI5; EVI5 and RAB11FIP3 may be mutually exclusive and compete for binding RAB11A (By similarity). Interacts with RIP11 and STXBP6. Interacts (GDP-bound form) with ZFYVE27 (By similarity). Interacts with SGSM1, SGSM2, SGSM3 and VIPAS39 (PubMed:17509819, PubMed:20190753). Interacts with EXOC6 in a GTP-dependent manner (PubMed:15292201). Interacts with BIRC6/bruce (By similarity). May interact with TBC1D14 (By similarity). Interacts with UNC119; in a cell cycle-dependent manner (By similarity). GDP-bound and nucleotide-free forms interact with SH3BP5 (PubMed:26506309). Interacts (GDP-bound form) with KIF5A in a ZFYVE27-dependent manner (By similarity). Interacts (GDP-bound form) with RELCH (PubMed:29514919). Found in a complex composed of RELCH, OSBP1 and RAB11A (PubMed:29514919). {ECO:0000250|UniProtKB:P62491, ECO:0000269|PubMed:15292201, ECO:0000269|PubMed:17509819, ECO:0000269|PubMed:26506309, ECO:0000269|PubMed:29514919}. +Q6PHZ5 RB15B_MOUSE Putative RNA-binding protein 15B (RNA-binding motif protein 15B) 887 97,076 Beta strand (6); Chain (1); Compositional bias (1); Cross-link (2); Domain (4); Erroneous initiation (1); Helix (2); Modified residue (8); Motif (1); Region (1); Sequence caution (1) FUNCTION: RNA-binding protein that acts as a key regulator of N6-methyladenosine (m6A) methylation of RNAs, thereby regulating different processes, such as alternative splicing of mRNAs and X chromosome inactivation mediated by Xist RNA. Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing. Plays a key role in m6A methylation, possibly by binding target RNAs and recruiting the WMM complex. Involved in random X inactivation mediated by Xist RNA: acts by binding Xist RNA and recruiting the WMM complex, which mediates m6A methylation, leading to target YTHDC1 reader on Xist RNA and promoting transcription repression activity of Xist. Functions in the regulation of alternative or illicit splicing, possibly by regulating m6A methylation. Inhibits pre-mRNA splicing. Also functions as a mRNA export factor by acting as a cofactor for the nuclear export receptor NXF1. {ECO:0000250|UniProtKB:Q8NDT2}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q8NDT2}. Nucleus speckle {ECO:0000250|UniProtKB:Q8NDT2}. Nucleus envelope {ECO:0000250|UniProtKB:Q8NDT2}. Note=Colocalizes with BMLF1 in the nucleus. Localized in the nucleoplasm with a granular staining pattern and excluded from the nucleoli. {ECO:0000250|UniProtKB:Q8NDT2}. SUBUNIT: Component of the WMM complex, a N6-methyltransferase complex composed of a catalytic subcomplex, named MAC, and of an associated subcomplex, named MACOM. The MAC subcomplex is composed of METTL3 and METTL14. The MACOM subcomplex is composed of WTAP, ZC3H13, CBLL1/HAKAI, VIRMA, and, in some cases of RBM15 (RBM15 or RBM15B). May interact with NCOR2. Interacts with NXF1, the interaction is required to promote mRNA export. {ECO:0000250|UniProtKB:Q8NDT2}. +Q8BQC8 RBAK_MOUSE RB-associated KRAB zinc finger protein (RB-associated KRAB repressor) (Zinc finger protein 769) 711 81,675 Chain (1); Cross-link (5); Domain (1); Region (2); Zinc finger (15) FUNCTION: May repress E2F-dependent transcription. May promote AR-dependent transcription. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with AR (By similarity). May also interact with other nuclear hormone receptors such as NR3C1/GR (By similarity). Interacts with RB1. {ECO:0000250, ECO:0000269|PubMed:10702291}. +O35963 RB33B_MOUSE Ras-related protein Rab-33B 229 25,767 Beta strand (8); Chain (1); Helix (9); Lipidation (2); Modified residue (1); Mutagenesis (2); Nucleotide binding (4); Turn (1) FUNCTION: Protein transport. Acts, in coordination with RAB6A, to regulate intra-Golgi retrograde trafficking (By similarity). It is involved in autophagy, acting as a modulator of autophagosome formation. {ECO:0000250, ECO:0000269|PubMed:18448665}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:18448665, ECO:0000269|PubMed:9512502}; Lipid-anchor {ECO:0000305}. Golgi apparatus, cis-Golgi network {ECO:0000269|PubMed:18448665}. Note=Under starvation conditions punctate RAB33B-positive structures are often observed in the cytoplasm (PubMed:18448665). {ECO:0000269|PubMed:18448665}. SUBUNIT: Interacts with RIC1 (via C-terminus domain); the interaction is direct with a preference for RAB33B-GTP. Interacts with RGP1 (By similarity). Interacts with ATG16L; the interaction is important for autophagosome formation (PubMed:18448665). {ECO:0000250|UniProtKB:Q9H082, ECO:0000269|PubMed:18448665}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9512502}. +Q60973 RBBP7_MOUSE Histone-binding protein RBBP7 (Histone acetyltransferase type B subunit 2) (Nucleosome-remodeling factor subunit RBAP46) (Retinoblastoma-binding protein 7) (RBBP-7) (Retinoblastoma-binding protein p46) 425 47,790 Chain (1); Cross-link (5); Initiator methionine (1); Modified residue (8); Repeat (7) FUNCTION: Core histone-binding subunit that may target chromatin remodeling factors, histone acetyltransferases and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA. Component of several complexes which regulate chromatin metabolism. These include the type B histone acetyltransferase (HAT) complex, which is required for chromatin assembly following DNA replication; the core histone deacetylase (HDAC) complex, which promotes histone deacetylation and consequent transcriptional repression; the nucleosome remodeling and histone deacetylase complex (the NuRD complex), which promotes transcriptional repression by histone deacetylation and nucleosome remodeling; and the PRC2/EED-EZH2 complex, which promotes repression of homeotic genes during development; and the NURF (nucleosome remodeling factor) complex (By similarity). {ECO:0000250|UniProtKB:Q16576}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Binds directly to helix 1 of the histone fold of histone H4, a region that is not accessible when H4 is in chromatin. Subunit of the type B histone acetyltransferase (HAT) complex, composed of RBBP7 and HAT1. Subunit of the core histone deacetylase (HDAC) complex, which is composed of HDAC1, HDAC2, RBBP4 and RBBP7. The core HDAC complex associates with SIN3A, ARID4B/SAP180, SAP18, SAP30, SAP130, SUDS3/SAP45 and possibly ARID4A/RBP1 and ING1 to form the SIN3 HDAC complex. The core HDAC complex may also associate with MTA2, MBD3, CHD3 and CHD4 to form the nucleosome remodeling and histone deacetylase complex (the NuRD complex). The NuRD complex may also interact with MBD3L1 and MBD3L2. Interacts with MTA1. Subunit of the PRC2/EED-EZH2 complex, which is composed of at least EED, EZH2, RBBP4, RBBP7 and SUZ12. The PRC2/EED-EZH2 complex may also associate with HDAC1. Part of the nucleosome remodeling factor (NURF) complex which consists of SMARCA1; BPTF; RBBP4 and RBBP7. Interacts with the viral protein-binding domain of the retinoblastoma protein (RB1). Interacts with CREBBP, and this interaction may be enhanced by the binding of phosphorylated CREB1 to CREBBP. Interacts with CENPA (By similarity). Interacts with BRCA1, HDAC7 and SUV39H1. {ECO:0000250|UniProtKB:Q16576, ECO:0000269|PubMed:10984530, ECO:0000269|PubMed:11788710, ECO:0000269|PubMed:20144788}. TISSUE SPECIFICITY: Higher levels in brain, thymus, lung, spleen, kidney, testis, and ovary/uterus; lower levels in heart, liver, and muscle. {ECO:0000269|PubMed:7503932}. +O88851 RBBP9_MOUSE Putative hydrolase RBBP9 (EC 3.-.-.-) (B5T-overexpressed gene protein) (Protein BOG) (Retinoblastoma-binding protein 9) (RBBP-9) 186 20,912 Active site (3); Chain (1); Frameshift (2); Modified residue (2); Region (1); Sequence conflict (1) FUNCTION: May play a role in the transformation process due to its capacity to confer resistance to the growth-inhibitory effects of TGF-beta1 through interaction with retinoblastoma and the subsequent displacement of E2F-1. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. +Q8VHP8 RB40B_MOUSE Ras-related protein Rab-40B (SOCS box-containing protein RAR) 278 31,063 Chain (1); Domain (1); Lipidation (2); Nucleotide binding (3) Protein modification; protein ubiquitination. FUNCTION: May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. DOMAIN: The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin ligase complexes. {ECO:0000250}. +Q8VHQ4 RB40C_MOUSE Ras-related protein Rab-40C (SOCS box-containing protein RAR3) 281 31,348 Chain (1); Domain (1); Lipidation (2); Nucleotide binding (3) Protein modification; protein ubiquitination. FUNCTION: Probable substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. SUBUNIT: Component of the probable SCF-like ECS(RAB40C) E3 ubiquitin-protein ligase complex which contains CUL5, RNF7/RBX2, Elongin BC complex and RAB40C. Interacts with CUL5, RNF7, ELOB and ELOC (By similarity). {ECO:0000250}. DOMAIN: The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin ligase complexes. {ECO:0000250}. +Q99MI1 RB6I2_MOUSE ELKS/Rab6-interacting/CAST family member 1 (ERC-1) (CAZ-associated structural protein 2) (CAST2) (Rab6-interacting protein 2) 1120 128,331 Alternative sequence (7); Chain (1); Coiled coil (2); Domain (1); Modified residue (12); Sequence caution (1); Sequence conflict (2) FUNCTION: Regulatory subunit of the IKK complex. Probably recruits IkappaBalpha/NFKBIA to the complex (By similarity). May be involved in the organization of the cytomatrix at the nerve terminals active zone (CAZ) which regulates neurotransmitter release. May be involved in vesicle trafficking at the CAZ. May be involved in Rab-6 regulated endosomes to Golgi transport. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein. Golgi apparatus membrane; Peripheral membrane protein. Note=In neurons, localized closed to presynaptic membrane. Recruited on Golgi membranes by RAB6A in a GTP-dependent manner. SUBUNIT: Interacts with the GTB-bound forms of RAB6A isoform 1 and isoform 2 and with RAB6B. The interaction was strongest with RAB6B, followed by RAB6A isoform 2 and weakest with RAB6A isoform 1. Part of a complex with CHUK, IKBKB and IKBKG. Interacts with CHUK, IKBKB and IKBKG. The interaction with IKBKG is independent of CHUK and IKBKB. Interacts with NFKBIA (By similarity). Isoform 2 interacts through its C-terminus with the PDZ domains of RIMS1 and RIMS2. Interacts with ERC2/CAST1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11929610}. +A6H6A9 RBG1L_MOUSE Rab GTPase-activating protein 1-like 815 92,404 Alternative sequence (8); Chain (1); Domain (2); Erroneous initiation (1); Frameshift (1); Modified residue (3); Mutagenesis (2); Sequence caution (1); Sequence conflict (5); Site (2) FUNCTION: GTP-hydrolysis activating protein (GAP) for small GTPase RAB22A, converting active RAB22A-GTP to the inactive form RAB22A-GDP (By similarity). Plays a role in endocytosis and intracellular protein transport. Recruited by ANK2 to phosphatidylinositol 3-phosphate (PI3P)-positive early endosomes, where it inactivates RAB22A, and promotes polarized trafficking to the leading edge of the migrating cells. Part of the ANK2/RABGAP1L complex which is required for the polarized recycling of fibronectin receptor ITGA5 ITGB1 to the plasma membrane that enables continuous directional cell migration (PubMed:27718357). {ECO:0000250|UniProtKB:Q5R372, ECO:0000269|PubMed:27718357}. SUBCELLULAR LOCATION: Early endosome {ECO:0000269|PubMed:27718357}. Golgi apparatus {ECO:0000250|UniProtKB:Q5R372}. Note=Colocalizes on endosomes partially with EEA1 (By similarity). Colocalizes and cotransports on motile vesicles with ANK2 (PubMed:27718357). {ECO:0000250|UniProtKB:Q5R372, ECO:0000269|PubMed:27718357}. SUBUNIT: Interacts (via Rab-GAP TBC domain) with ANK2 (via death domain). {ECO:0000269|PubMed:27718357}. DOMAIN: The arginine and glutamine fingers are critical for the GTPase-activating mechanism, they pull out Rab's 'switch 2' glutamine and insert in Rab's active site. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in embryonic heart and liver, and in hemopoietic cells (PubMed:10585558). Expressed in the corpus callosum in the central nervous system (CNS) and costameres in skeletal muscle at postnatal day (PND) 30 (PubMed:27718357). {ECO:0000269|PubMed:10585558, ECO:0000269|PubMed:27718357}. +O89086 RBM3_MOUSE RNA-binding protein 3 (RNA-binding motif protein 3) 153 16,605 Chain (1); Compositional bias (1); Domain (1); Modified residue (10) FUNCTION: Cold-inducible mRNA binding protein that enhances global protein synthesis at both physiological and mild hypothermic temperatures. Reduces the relative abundance of microRNAs, when overexpressed. Enhances phosphorylation of translation initiation factors and active polysome formation. {ECO:0000269|PubMed:15684048}. PTM: Arg-103 is dimethylated, probably to asymmetric dimethylarginine. {ECO:0000250}.; PTM: Phosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Note=Localizes in mRNA granules in dentrites. {ECO:0000250}. SUBUNIT: Interacts with RPL4. Associates with the 60S ribosomal subunits in an RNA-independent manner. +Q91WT8 RBM47_MOUSE RNA-binding protein 47 (RNA-binding motif protein 47) 590 64,062 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (3); Modified residue (4); Sequence conflict (1) SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +Q8VE92 RBM4B_MOUSE RNA-binding protein 4B (RNA-binding motif protein 30) (RNA-binding motif protein 4B) (RNA-binding protein 30) 357 39,991 Chain (1); Compositional bias (2); Domain (2); Region (1); Zinc finger (1) FUNCTION: Required for the translational activation of PER1 mRNA in response to circadian clock. Binds directly to the 3'-UTR of the PER1 mRNA. {ECO:0000269|PubMed:17264215}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. SUBUNIT: Interacts with TNPO3, which may mediate nuclear import of the protein. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the suprachiasmatic nucleus (SCN) (at protein level). Expressed in the suprachiasmatic nucleus (SCN). {ECO:0000269|PubMed:17264215}. +Q69Z61 PWP2A_MOUSE PWWP domain-containing protein 2A 730 79,388 Alternative sequence (3); Chain (1); Compositional bias (3); Cross-link (1); Domain (1); Erroneous gene model prediction (1); Erroneous initiation (1); Frameshift (1); Modified residue (2); Region (1); Sequence conflict (4) FUNCTION: H2A.Z-specific chromatin binding protein which may play an important role in the neural crest stem cell migration and differentiation during early development. Also required for proper mitosis progression. {ECO:0000250|UniProtKB:Q96N64}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96N64}. SUBUNIT: Interacts with H2A.Z/H2AFZ. {ECO:0000250|UniProtKB:Q96N64}. +Q8BX57 PXK_MOUSE PX domain-containing protein kinase-like protein (Modulator of Na,K-ATPase) (MONaKA) 582 65,231 Alternative sequence (4); Chain (1); Domain (3); Frameshift (2); Sequence caution (1); Sequence conflict (15) FUNCTION: Binds to and modulates brain Na,K-ATPase subunits ATP1B1 and ATP1B3 and may thereby participate in the regulation of electrical excitability and synaptic transmission. May not display kinase activity. {ECO:0000250|UniProtKB:Q7Z7A4, ECO:0000269|PubMed:16135750}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16135750}. Cell membrane {ECO:0000269|PubMed:16135750}; Peripheral membrane protein {ECO:0000269|PubMed:16135750}. Note=Also associates with the plasma membrane. DOMAIN: The protein kinase domain is predicted to be catalytically inactive. TISSUE SPECIFICITY: Isoform 1 is present in all tissues examined. Isoform 2 is found in all tissues except skeletal muscle and very low levels in spleen. Both isoforms are widely expressed throughout the nervous system however levels of isoform 2 are higher in purified hippocampal and cortical neurons whereas glial cells express more isoform 1 than isoform 2. {ECO:0000269|PubMed:16135750}. +Q9JJW0 PXMP4_MOUSE Peroxisomal membrane protein 4 (24 kDa peroxisomal intrinsic membrane protein) 212 24,196 Chain (1); Glycosylation (1); Transmembrane (2) TRANSMEM 97 117 Helical. {ECO:0000255}.; TRANSMEM 153 173 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with PEX19. {ECO:0000250}. +P62911 RL32_MOUSE 60S ribosomal protein L32 135 15,860 Chain (1); Cross-link (1); Modified residue (2) +Q61838 PZP_MOUSE Pregnancy zone protein (Alpha-2-macroglobulin) (Alpha-2-M) [Cleaved into: Alpha-2-macroglobulin 165 kDa subunit; Alpha-2-macroglobulin 35 kDa subunit] 1495 165,853 Chain (3); Cross-link (1); Disulfide bond (12); Frameshift (1); Glycosylation (11); Region (1); Sequence conflict (22); Signal peptide (1) FUNCTION: Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region, a thioester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Highest expression in liver, medium expression in ovary, heart and stomach. Low expression in lung, kidney and uterus. Protein found in plasma. {ECO:0000269|PubMed:15355875}. +Q69ZS0 PZRN3_MOUSE E3 ubiquitin-protein ligase PDZRN3 (EC 2.3.2.27) (PDZ domain-containing RING finger protein 3) (RING-type E3 ubiquitin transferase PDZRN3) (Semaphorin cytoplasmic domain-associated protein 3) (Protein SEMACAP3) 1063 119,401 Alternative sequence (2); Chain (1); Coiled coil (1); Compositional bias (1); Domain (2); Erroneous termination (1); Modified residue (1); Mutagenesis (2); Sequence conflict (11); Zinc finger (2) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase. Plays an important role in regulating the surface level of MUSK on myotubes. Mediates the ubiquitination of MUSK, promoting its endocytosis and lysosomal degradation. Might contribute to terminal myogenic differentiation. {ECO:0000269|PubMed:17118964, ECO:0000269|PubMed:17576800}. PTM: Auto-ubiquitinated. {ECO:0000269|PubMed:17576800}. SUBCELLULAR LOCATION: Cell junction, synapse {ECO:0000269|PubMed:17576800}. Cytoplasm {ECO:0000250|UniProtKB:E7FDW2}. Note=Localizes to the postsynaptic region of neuromuscular junctions. {ECO:0000269|PubMed:17576800}. SUBUNIT: Interacts with NLGN1 and EFNB2 (By similarity). Interacts with UBE2D2 and with MUSK via the first PDZ domain. In myotubes, the interaction between PDZRN3 and MUSK is enhanced upon agrin stimulation. {ECO:0000250, ECO:0000269|PubMed:17576800}. DOMAIN: The RING-type zinc finger domain is required for E3 ligase activity. {ECO:0000269|PubMed:17576800}. TISSUE SPECIFICITY: Highly expressed in skeletal and cardiac muscle and at lower levels in spinal cord and brain (at protein level). Also expressed in kidney and lung. In muscles, concentrated at the neuromuscular junction (NMJ). {ECO:0000269|PubMed:17576800}. +Q9CZ13 QCR1_MOUSE Cytochrome b-c1 complex subunit 1, mitochondrial (Complex III subunit 1) (Core protein I) (Ubiquinol-cytochrome-c reductase complex core protein 1) 480 52,852 Chain (1); Modified residue (7); Sequence conflict (2); Transit peptide (1) FUNCTION: This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. This protein may mediate formation of the complex between cytochromes c and c1 (By similarity). {ECO:0000250}. PTM: Acetylation of Lys-138 is observed in liver mitochondria from fasted mice but not from fed mice. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}. SUBUNIT: The bc1 complex contains 11 subunits: 3 respiratory subunits (cytochrome b, cytochrome c1 and Rieske/UQCRFS1), 2 core proteins (UQCRC1/QCR1 and UQCRC2/QCR2) and 6 low-molecular weight proteins (UQCRH/QCR6, UQCRB/QCR7, UQCRQ/QCR8, UQCR10/QCR9, UQCR11/QCR10 and a cleavage product of Rieske/UQCRFS1). {ECO:0000250}. +P99028 QCR6_MOUSE Cytochrome b-c1 complex subunit 6, mitochondrial (Complex III subunit 6) (Complex III subunit VIII) (Cytochrome c1 non-heme 11 kDa protein) (Mitochondrial hinge protein) (Ubiquinol-cytochrome c reductase complex 11 kDa protein) 89 10,435 Chain (1); Compositional bias (1); Disulfide bond (2); Modified residue (2); Transit peptide (1) FUNCTION: This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. This protein may mediate formation of the complex between cytochromes c and c1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P00127}. SUBUNIT: The bc1 complex contains 11 subunits: 3 respiratory subunits (cytochrome b, cytochrome c1 and Rieske/UQCRFS1), 2 core proteins (UQCRC1/QCR1 and UQCRC2/QCR2) and 6 low-molecular weight proteins (UQCRH/QCR6, UQCRB/QCR7, UQCRQ/QCR8, UQCR10/QCR9, UQCR11/QCR10 and a cleavage product of Rieske/UQCRFS1). {ECO:0000250}. +Q9CQ69 QCR8_MOUSE Cytochrome b-c1 complex subunit 8 (Complex III subunit 8) (Complex III subunit VIII) (Ubiquinol-cytochrome c reductase complex 9.5 kDa protein) (Ubiquinol-cytochrome c reductase complex ubiquinone-binding protein QP-C) 82 9,768 Chain (1); Modified residue (3) FUNCTION: This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. This subunit, together with cytochrome b, binds to ubiquinone. SUBCELLULAR LOCATION: Mitochondrion inner membrane. SUBUNIT: The bc1 complex contains 11 subunits: 3 respiratory subunits (cytochrome b, cytochrome c1 and Rieske/UQCRFS1), 2 core proteins (UQCRC1/QCR1 and UQCRC2/QCR2) and 6 low-molecular weight proteins (UQCRH/QCR6, UQCRB/QCR7, UQCRQ/QCR8, UQCR10/QCR9, UQCR11/QCR10 and a cleavage product of Rieske/UQCRFS1). {ECO:0000250}. +Q8R1I1 QCR9_MOUSE Cytochrome b-c1 complex subunit 9 (Complex III subunit 9) (Complex III subunit X) (Cytochrome c1 non-heme 7 kDa protein) (Ubiquinol-cytochrome c reductase complex 7.2 kDa protein) 64 7,446 Chain (1) FUNCTION: This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. This subunit interacts with cytochrome c1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}. SUBUNIT: The bc1 complex contains 11 subunits: 3 respiratory subunits (cytochrome b, cytochrome c1 and Rieske/UQCRFS1), 2 core proteins (UQCRC1/QCR1 and UQCRC2/QCR2) and 6 low-molecular weight proteins (UQCRH/QCR6, UQCRB/QCR7, UQCRQ/QCR8, UQCR10/QCR9, UQCR11/QCR10 and a cleavage product of Rieske/UQCRFS1). {ECO:0000250}. +Q9QYS9 QKI_MOUSE Protein quaking (MqkI) (qkI) 341 37,671 Alternative sequence (8); Chain (1); Domain (1); Helix (3); Modified residue (5); Motif (2); Mutagenesis (11); Region (2); Sequence conflict (1); Site (6) FUNCTION: RNA-binding protein that plays a central role in myelinization (PubMed:10864952, PubMed:11917126). Also required for visceral endoderm function and blood vessel development (PubMed:11892011, PubMed:16470614). Binds to the 5'-NACUAAY-N(1,20)-UAAY-3' RNA core sequence (PubMed:16041388). Acts by regulating pre-mRNA splicing, mRNA export, mRNA stability and protein translation, as well as cellular processes including apoptosis, cell cycle, glial cell fate and development (PubMed:10535969, PubMed:12467586, PubMed:11297509, PubMed:11917126, PubMed:15568022). Required to protect and promote stability of mRNAs such as MBP and CDKN1B which promotes oligodendrocyte differentiation (PubMed:10535969, PubMed:15568022). Participates in mRNA transport by regulating the nuclear export of MBP mRNA (PubMed:12467586). May also play a role in smooth muscle development (PubMed:14706070). {ECO:0000269|PubMed:10535969, ECO:0000269|PubMed:10864952, ECO:0000269|PubMed:11297509, ECO:0000269|PubMed:11892011, ECO:0000269|PubMed:11917126, ECO:0000269|PubMed:12467586, ECO:0000269|PubMed:14706070, ECO:0000269|PubMed:15568022, ECO:0000269|PubMed:16041388, ECO:0000269|PubMed:16470614}.; FUNCTION: Isoform 1 is involved in regulation of mRNA splicing of MAG pre-mRNA by acting as a negative regulator of MAG exon 12 alternative splicing. {ECO:0000269|PubMed:11917126}.; FUNCTION: Isoform 3 can induce apoptosis, while heterodimerization with other isoforms results in nuclear translocation of isoform 3 and suppression of apoptosis. {ECO:0000269|PubMed:11297509}.; FUNCTION: Isoform 4 acts as a translational repressor for GLI1. {ECO:0000269|PubMed:16198329}. PTM: Methylated by PRMT1. {ECO:0000269|PubMed:12529443}.; PTM: Tyrosine phosphorylated at its C-terminus, probably by FYN. Phosphorylation leads to decreased mRNA-binding affinity, affecting transport and/or stabilization of MBP mRNA. The level of Tyr phosphorylation in the developing myelin is highest in the first postnatal week (P7). During the vigorous accumulation of MBP mRNA between P7 and P20, phosphorylation in the developing myelin drastically declines. By the end of the fourth postnatal week (P28), phosphorylation is reduced approximately 90%. {ECO:0000269|PubMed:12682013, ECO:0000269|PubMed:15528192}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus.; SUBCELLULAR LOCATION: Isoform 1: Cytoplasm. Nucleus. Note=Isoform 1 localizes predominantly in the nucleus and at lower levels in cytoplasm. It shuttles between the cytoplasm and the nucleus.; SUBCELLULAR LOCATION: Isoform 3: Cytoplasm. Nucleus. Note=Isoform 3 localizes predominantly in the cytoplasm and at much lower levels in nucleus.; SUBCELLULAR LOCATION: Isoform 4: Cytoplasm. Nucleus. Note=Isoform 4 localizes both in the cytoplasm and nucleus. SUBUNIT: Homodimer. Does not require RNA to homodimerize (PubMed:10506177, PubMed:11297509, PubMed:9671495). Able to heterodimerize with BICC1 (PubMed:9315629). {ECO:0000269|PubMed:10506177, ECO:0000269|PubMed:11297509, ECO:0000269|PubMed:9315629, ECO:0000269|PubMed:9671495}. DOMAIN: The KH domain and the Qua2 region are involved in RNA binding. {ECO:0000250|UniProtKB:Q96PU8}. TISSUE SPECIFICITY: Highly expressed in myelin-forming cells. Expressed in oligodendrocytes and astrocytes in the central nervous system as well as Schwann cells in the peripheral nervous system. Also expressed in the yolk sac endoderm, adjacent to the mesodermal site of developing blood islands, where the differentiation of blood and endothelial cells first occurs (at protein level). Expressed in brain, lung, heart and testis. {ECO:0000269|PubMed:8589716, ECO:0000269|PubMed:8987822, ECO:0000269|PubMed:9778149}. DISEASE: Note=Defects in Qki are the cause of quakingviable (qkv). Qkv is a spontaneous mutation resulting in hypomyelinization of the central and peripheral nervous systems. Mutant mice develop normally until postnatal day 10 when they display rapid tremors or 'quaking' that is especially pronounced in hindlimbs and experience convulsive tonic-clonic seizures as they mature (PubMed:8589716). Mice with qkv specifically lack isoform 3 and isoform 4 in myelin-forming cells, while isoform 1 is lacking in oligodendrocytes of severely affected tracts (PubMed:12888522). Mice with qkv also lack the PRKN gene product, suggesting that the absence of PRKN may also affect the phenotype (PubMed:15014970). {ECO:0000269|PubMed:12888522, ECO:0000269|PubMed:15014970, ECO:0000269|PubMed:8589716}. +Q921W4 QORL1_MOUSE Quinone oxidoreductase-like protein 1 (EC 1.-.-.-) (Quinone oxidoreductase homolog 1) (QOH-1) (Zeta-crystallin homolog) 348 38,725 Alternative sequence (2); Chain (1); Sequence conflict (1) +P83861 QRFPR_MOUSE Pyroglutamylated RF-amide peptide receptor (AQ27) (G-protein coupled receptor 103) (Orexigenic neuropeptide QRFP receptor) (SP9155) 433 49,245 Chain (1); Glycosylation (2); Topological domain (8); Transmembrane (7) TRANSMEM 47 67 Helical; Name=1. {ECO:0000255}.; TRANSMEM 82 102 Helical; Name=2. {ECO:0000255}.; TRANSMEM 121 141 Helical; Name=3. {ECO:0000255}.; TRANSMEM 163 183 Helical; Name=4. {ECO:0000255}.; TRANSMEM 213 233 Helical; Name=5. {ECO:0000255}.; TRANSMEM 272 292 Helical; Name=6. {ECO:0000255}.; TRANSMEM 314 334 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 46 Extracellular. {ECO:0000255}.; TOPO_DOM 68 81 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 103 120 Extracellular. {ECO:0000255}.; TOPO_DOM 142 162 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 184 212 Extracellular. {ECO:0000255}.; TOPO_DOM 234 271 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 293 313 Extracellular. {ECO:0000255}.; TOPO_DOM 335 433 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for the orexigenic neuropeptide QRFP. The activity of this receptor is mediated by G proteins that modulate adenylate cyclase activity and intracellular calcium levels (By similarity). {ECO:0000250|UniProtKB:Q96P65}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed widely in the brain with high levels in the cortex and hypothalamus, and moderate levels in the brain stem, caudate nucleus, midbrain hippocampus, thalamus, trigeminal ganglia and spinal cord. Particularly strong expression detected in the mitral cell layer of the olfactory bulb, accessory olfactory bulb, island of Calleja and nucleus of the solitary tract. In peripheral tissues, expressed at moderate levels in the eye, liver, kidney, pituitary gland, testis and thymus. {ECO:0000269|PubMed:12714592, ECO:0000269|PubMed:16648250}. +Q8BND5 QSOX1_MOUSE Sulfhydryl oxidase 1 (mSOx) (EC 1.8.3.2) (Quiescin Q6) (Skin sulfhydryl oxidase) 748 82,785 Active site (2); Alternative sequence (6); Beta strand (17); Binding site (7); Chain (1); Disulfide bond (4); Domain (2); Glycosylation (2); Helix (25); Nucleotide binding (1); Sequence conflict (3); Signal peptide (1); Transmembrane (1); Turn (5) TRANSMEM 711 731 Helical. {ECO:0000255}. FUNCTION: Catalyzes the oxidation of sulfhydryl groups in peptide and protein thiols to disulfides with the reduction of oxygen to hydrogen peroxide. May contribute to disulfide bond formation in a variety of secreted proteins (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Isoform 1: Golgi apparatus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 2: Secreted. Note=Found in the extracellular medium of quiescent cells but not in proliferating cells.; SUBCELLULAR LOCATION: Isoform 3: Secreted. Note=Found in the extracellular medium of quiescent cells but not in proliferating cells.; SUBCELLULAR LOCATION: Isoform 4: Secreted. Note=Found in the extracellular medium of quiescent cells but not in proliferating cells. SUBUNIT: Monomer. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the seminal vesicles and skin. {ECO:0000269|PubMed:12354420}. +Q3TMX7 QSOX2_MOUSE Sulfhydryl oxidase 2 (EC 1.8.3.2) (Quiescin Q6-like protein 1) 692 77,775 Active site (2); Alternative sequence (3); Binding site (7); Chain (1); Disulfide bond (4); Domain (2); Glycosylation (4); Nucleotide binding (1); Signal peptide (1); Transmembrane (1) TRANSMEM 656 676 Helical. {ECO:0000255}. FUNCTION: Catalyzes the oxidation of sulfhydryl groups in peptide and protein thiols to disulfides with the reduction of oxygen to hydrogen peroxide. May contribute to disulfide bond formation in a variety of secreted proteins (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. +B8ZXI1 QTRT2_MOUSE Queuine tRNA-ribosyltransferase accessory subunit 2 (Queuine tRNA-ribosyltransferase domain-containing protein 1) 415 46,288 Alternative sequence (1); Beta strand (17); Chain (1); Erroneous initiation (4); Helix (17); Metal binding (4); Turn (3) FUNCTION: Non-catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). {ECO:0000255|HAMAP-Rule:MF_03043, ECO:0000269|PubMed:19414587}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03043, ECO:0000269|PubMed:19414587}. Mitochondrion outer membrane {ECO:0000255|HAMAP-Rule:MF_03043, ECO:0000269|PubMed:19414587}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03043, ECO:0000269|PubMed:19414587}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03043, ECO:0000269|PubMed:19414587}. Note=May associate with the mitochondrion outer membrane. {ECO:0000255|HAMAP-Rule:MF_03043, ECO:0000269|PubMed:19414587}. SUBUNIT: Heterodimer of a catalytic subunit QTRT1 and an accessory subunit QTRT2. {ECO:0000255|HAMAP-Rule:MF_03043, ECO:0000269|PubMed:19414587}. TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver, lung, skeletal muscle, spleen and testis. {ECO:0000269|PubMed:19414587}. +O55142 RL35A_MOUSE 60S ribosomal protein L35a 110 12,554 Chain (1); Modified residue (3) FUNCTION: Required for the proliferation and viability of hematopoietic cells. Plays a role in 60S ribosomal subunit formation. The protein was found to bind to both initiator and elongator tRNAs and consequently was assigned to the P site or P and A site. {ECO:0000250}. +Q69Z89 RADIL_MOUSE Ras-associating and dilute domain-containing protein 1099 120,355 Alternative sequence (4); Chain (1); Domain (4); Erroneous initiation (1); Frameshift (1); Modified residue (7); Sequence conflict (2) FUNCTION: Downstream effector of Rap required for cell adhesion and migration of neural crest precursors during development. {ECO:0000269|PubMed:17704304}. SUBUNIT: Interacts with RAP1A; in a GTP-dependent manner. Does not interact with members of the Ras family. Interacts (via PDZ domain) with KIF14; is recruited to the microtubule network restricting its interaction with activated RAP1A (By similarity). {ECO:0000250|UniProtKB:Q96JH8}. +P26043 RADI_MOUSE Radixin (ESP10) 583 68,543 Beta strand (14); Binding site (1); Chain (1); Compositional bias (2); Domain (1); Helix (12); Modified residue (2); Region (1); Sequence conflict (3); Turn (4) FUNCTION: Probably plays a crucial role in the binding of the barbed end of actin filaments to the plasma membrane. PTM: Phosphorylated by tyrosine-protein kinases. Phosphorylation by ROCK2 suppresses the head-to-tail association of the N-terminal and C-terminal halves resulting in an opened conformation which is capable of actin and membrane-binding. {ECO:0000269|PubMed:8479753, ECO:0000269|PubMed:9456324}. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Cleavage furrow. Cell projection, microvillus {ECO:0000269|PubMed:9472040}. Note=Highly concentrated in the undercoat of the cell-to-cell adherens junction and the cleavage furrow in the interphase and mitotic phase, respectively. SUBUNIT: Interacts with CPNE1 (via VWFA domain) and CPNE4 (via VWFA domain) (PubMed:12522145). Binds SLC9A3R1 (By similarity). Interacts with LAYN (PubMed:15913605). Interacts with NHERF1 and NHERF2 (PubMed:16615918). Interacts with MME/NEP (PubMed:17459884). Interacts with ICAM2 (PubMed:12554651, PubMed:9472040). Interacts with SPN and CD44 (PubMed:9472040). {ECO:0000250|UniProtKB:P35241, ECO:0000269|PubMed:12522145, ECO:0000269|PubMed:12554651, ECO:0000269|PubMed:15913605, ECO:0000269|PubMed:16615918, ECO:0000269|PubMed:17459884, ECO:0000269|PubMed:9472040}. DOMAIN: The N-terminal domain interacts with the C-terminal domain of LAYN. An interdomain interaction between its N-terminal and C-terminal domains inhibits its ability to bind LAYN. In the presence of acidic phospholipids, the interdomain interaction is inhibited and this enhances binding to LAYN. +Q9JI58 RAE1D_MOUSE Retinoic acid early-inducible protein 1-delta (RAE-1-delta) 249 27,884 Chain (1); Disulfide bond (2); Glycosylation (4); Lipidation (1); Propeptide (1); Signal peptide (1) FUNCTION: Acts as a ligand for KLRK1. {ECO:0000269|PubMed:10894171}. PTM: Glycosylated. {ECO:0000269|PubMed:10894171}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10894171}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:10894171}. +Q8C779 RADX_MOUSE RPA-related protein RADX 850 96,847 Alternative sequence (1); Chain (1); DNA binding (1); Sequence conflict (3) FUNCTION: Single-stranded DNA-binding protein recruited to replication forks to maintain genome stability. Prevents fork collapse by antagonizing the accumulation of RAD51 at forks to ensure the proper balance of fork remodeling and protection without interfering with the capacity of cells to complete homologous recombination of double-strand breaks. {ECO:0000250|UniProtKB:Q6NSI4}. SUBCELLULAR LOCATION: Chromosome {ECO:0000250|UniProtKB:Q6NSI4}. Note=Recruited to replication forks. {ECO:0000250|UniProtKB:Q6NSI4}. +Q8C570 RAE1L_MOUSE mRNA export factor (Rae1 protein homolog) (mRNA-associated protein mrnp 41) 368 40,965 Chain (1); Modified residue (1); Repeat (7); Sequence conflict (1) FUNCTION: Plays a role in mitotic bipolar spindle formation. Binds mRNA. May function in nucleocytoplasmic transport and in directly or indirectly attaching cytoplasmic mRNPs to the cytoskeleton. {ECO:0000250|UniProtKB:P78406}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P78406}. Nucleus {ECO:0000250|UniProtKB:P78406}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:P78406}. Note=Recruited from interphase nuclei to spindle MTs during mitosis. {ECO:0000250|UniProtKB:P78406}. SUBUNIT: Interacts with NUMA1 (via N-terminal end of the coiled-coil domain); this interaction promotes spindle formation in mitosis (By similarity). Interacts with NUP98 (PubMed:10209021). Interacts with MYCBP2 (By similarity). {ECO:0000250|UniProtKB:P78406, ECO:0000269|PubMed:10209021}. +Q9QZD5 RAE2_MOUSE Rab proteins geranylgeranyltransferase component A 2 (Choroideremia-like protein) (Rab escort protein 2) (REP-2) 621 70,010 Chain (1); Sequence conflict (2) FUNCTION: Substrate-binding subunit (component A) of the Rab geranylgeranyltransferase (GGTase) complex. Binds unprenylated Rab proteins and presents the substrate peptide to the catalytic component B. The component A is thought to be regenerated by transferring its prenylated Rab back to the donor membrane. Less effective than CHM in supporting prenylation of Rab3 family (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. SUBUNIT: Monomer. Heterotrimer composed of RABGGTA, RABGGTB and CHML; within this trimer, RABGGTA and RABGGTB form the catalytic component B, while CHML (component A) mediates Rab protein binding. Interacts with RAB1A, RAB7A and RAB27A, but has much lower affinity for RAB1A, RAB7A and RAB27A than CHM (By similarity). {ECO:0000250}. +Q8BTF8 RALYL_MOUSE RNA-binding Raly-like protein 293 32,452 Alternative sequence (2); Chain (1); Coiled coil (1); Domain (1); Sequence conflict (1) +Q61818 RAI1_MOUSE Retinoic acid-induced protein 1 1889 201,571 Alternative sequence (2); Chain (1); Compositional bias (4); Cross-link (5); Modified residue (14); Motif (2); Sequence conflict (7); Zinc finger (2) FUNCTION: Transcriptional regulator of the circadian clock components: CLOCK, ARNTL/BMAL1, ARNTL2/BMAL2, PER1/3, CRY1/2, NR1D1/2 and RORA/C. Positively regulates the transcriptional activity of CLOCK a core component of the circadian clock. Regulates transcription through chromatin remodeling by interacting with other proteins in chromatin as well as proteins in the basic transcriptional machinery. May be important for embryonic and postnatal development. May be involved in neuronal differentiation. {ECO:0000269|PubMed:15746153, ECO:0000269|PubMed:22578325}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=In neurons, localized to neurites. TISSUE SPECIFICITY: Detected in all tissues examined with strong expression in the thymus and brain. Expressed in epithelial cells involved in organogenesis. No expression was seen in the corpus callosum of the brain. {ECO:0000269|PubMed:7476016}. +Q9QVY8 RAI2_MOUSE Retinoic acid-induced protein 2 (3f8) 529 57,123 Chain (1); Compositional bias (1); Sequence conflict (2) +Q9WTJ5 RAMP1_MOUSE Receptor activity-modifying protein 1 148 16,892 Chain (1); Disulfide bond (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 118 138 Helical. {ECO:0000255}. TOPO_DOM 27 117 Extracellular. {ECO:0000255}.; TOPO_DOM 139 148 Cytoplasmic. {ECO:0000255}. FUNCTION: Transports the calcitonin gene-related peptide type 1 receptor (CALCRL) to the plasma membrane. Acts as a receptor for calcitonin-gene-related peptide (CGRP) together with CALCRL. {ECO:0000269|PubMed:10854696, ECO:0000269|PubMed:12147211}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Heterodimer of CALCRL and RAMP1. TISSUE SPECIFICITY: Expressed predominantly in the thymus, skeletal muscle, embryonic and adult brain, embryonic and adult lung, and colon. {ECO:0000269|PubMed:10777702, ECO:0000269|PubMed:10854696, ECO:0000269|PubMed:12147211}. +P27659 RL3_MOUSE 60S ribosomal protein L3 (J1 protein) 403 46,110 Chain (1); Cross-link (9); Modified residue (7); Sequence conflict (1) FUNCTION: The L3 protein is a component of the large subunit of cytoplasmic ribosomes. {ECO:0000250|UniProtKB:P39023}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Cytoplasm. SUBUNIT: Component of the large ribosomal subunit. Interacts with METTL18. Interacts with DHX33 (PubMed:26100019). {ECO:0000250|UniProtKB:P39023, ECO:0000269|PubMed:26100019}. +P69566 RANB9_MOUSE Ran-binding protein 9 (RanBP9) (B-cell antigen receptor Ig beta-associated protein 1) (IBAP-1) (Ran-binding protein M) (RanBPM) 653 71,012 Alternative sequence (2); Chain (1); Compositional bias (2); Domain (3); Modified residue (3); Region (2); Sequence conflict (1) FUNCTION: May act as scaffolding protein, and as adapter protein to couple membrane receptors to intracellular signaling pathways. Acts as a mediator of cell spreading and actin cytoskeleton rearrangement. Core component of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1. May be involved in signaling of ITGB2/LFA-1 and other integrins. Enhances HGF-MET signaling by recruiting Sos and activating the Ras pathway. Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but not affect estrogen-induced transactivation. Stabilizes TP73 isoform Alpha, probably by inhibiting its ubiquitination, and increases its proapoptotic activity. Inhibits the kinase activity of DYRK1A and DYRK1B. Inhibits FMR1 binding to RNA. {ECO:0000250|UniProtKB:Q96S59}. PTM: Phosphorylated in response to stress. {ECO:0000250|UniProtKB:Q96S59}.; PTM: Ubiquitinated. Polyubiquitination targets the protein for rapid degradation via the ubiquitin system (By similarity). {ECO:0000250|UniProtKB:Q96S59}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18710924}. Cell membrane {ECO:0000305|PubMed:18710924}; Peripheral membrane protein {ECO:0000305|PubMed:18710924}; Cytoplasmic side {ECO:0000305|PubMed:18710924}. Nucleus {ECO:0000269|PubMed:18710924}. Note=Predominantly cytoplasmic (PubMed:18710924). A phosphorylated form is associated with the plasma membrane (By similarity). Perinuclear in spermatids (PubMed:14648869). {ECO:0000250|UniProtKB:Q96S59, ECO:0000269|PubMed:14648869, ECO:0000269|PubMed:18710924}. SUBUNIT: Part of a complex consisting of RANBP9, MKLN1 and GID8. Identified in the CTLH complex that contains GID4, RANBP9 and/or RANBP10, MKLN1, MAEA, RMND5A (or alternatively its paralog RMND5B), GID8, ARMC8, WDR26 and YPEL5. Within this complex, MAEA, RMND5A (or alternatively its paralog RMND5B), GID8, WDR26, and RANBP9 and/or RANBP10 form the catalytic core, while GID4, MKLN1, ARMC8 and YPEL5 have ancillary roles. Interacts with GTP-bound Ran, AR, CDC2L1/p110C, CALB1, S100A7, USP11, SOS1 or SOS2, GID8, and FMR1. Interacts with the Dyrk kinases HIPK2, DYRK1A, and DYRK1B. Interacts with TP73 isoform Alpha but not with TP53. Interacts with the HGF receptor MET and the integrins ITGB1 and ITGB2, but not with ITGAL. Part of a complex consisting of RANBP9, RAN, DYRK1B and COPS5. Directly interacts with RANBP10. Interacts with YPEL5 (By similarity). Interacts with MKLN1 (PubMed:18710924). Interacts with DDX4 (PubMed:14648869). Interacts with NGFR (PubMed:12963025). Interacts with Tex19.1 and, probably, Tex19.2 (PubMed:28254886). {ECO:0000250|UniProtKB:Q96S59, ECO:0000269|PubMed:12963025, ECO:0000269|PubMed:14648869, ECO:0000269|PubMed:18710924, ECO:0000269|PubMed:28254886}. DOMAIN: The SPRY domain mediates the interaction with MET, AR, and CDC2L1. {ECO:0000250|UniProtKB:Q96S59}. TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in maturating spermatocytes. {ECO:0000269|PubMed:14648869, ECO:0000269|PubMed:14722085}. +P63321 RALA_MOUSE Ras-related protein Ral-A 206 23,553 Chain (1); Lipidation (1); Modified residue (1); Motif (1); Nucleotide binding (3); Propeptide (1) FUNCTION: Multifunctional GTPase involved in a variety of cellular processes including gene expression, cell migration, cell proliferation, oncogenic transformation and membrane trafficking. Accomplishes its multiple functions by interacting with distinct downstream effectors. Acts as a GTP sensor for GTP-dependent exocytosis of dense core vesicles. Key regulator of LPAR1 signaling and competes with GRK2 for binding to LPAR1 thus affecting the signaling properties of the receptor. Required for anchorage-independent proliferation of transformed cells (By similarity). The RALA-exocyst complex regulates integrin-dependent membrane raft exocytosis and growth signaling (PubMed:20005108). During mitosis, supports the stabilization and elongation of the intracellular bridge between dividing cells. Cooperates with EXOC2 to recruit other components of the exocyst to the early midbody (By similarity). {ECO:0000250|UniProtKB:P11233, ECO:0000269|PubMed:20005108}. PTM: Prenylation is essential for membrane localization. {ECO:0000250|UniProtKB:P11233}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P11233}; Lipid-anchor {ECO:0000250|UniProtKB:P11233}; Cytoplasmic side. Cleavage furrow {ECO:0000250|UniProtKB:P11233}. Midbody, Midbody ring {ECO:0000250|UniProtKB:P11233}. Note=Predominantly at the cell surface in the absence of LPA. In the presence of LPA, colocalizes with LPAR1 and LPAR2 in endocytic vesicles. {ECO:0000250|UniProtKB:P11233}. SUBUNIT: Interacts (via effector domain) with RALBP1 (By similarity). Interacts with EXOC2/Sec5 and EXOC8/Exo84; binding to EXOC2 and EXOC8 is mutually exclusive (By similarity). Interacts with Clostridium exoenzyme C3 (By similarity). Interacts with RALGPS1 (By similarity). Interacts with LPAR1 and LPAR2. Interacts with GRK2 in response to LPAR1 activation. RALA and GRK2 binding to LPAR1 is mutually exclusive (By similarity). Interacts with CDC42 (By similarity). {ECO:0000250|UniProtKB:P11233, ECO:0000250|UniProtKB:P63322}. +Q80ZJ1 RAP2A_MOUSE Ras-related protein Rap-2a 183 20,642 Alternative sequence (1); Chain (1); Lipidation (3); Modified residue (1); Motif (1); Mutagenesis (5); Nucleotide binding (3); Propeptide (1) FUNCTION: Small GTP-binding protein which cycles between a GDP-bound inactive and a GTP-bound active form. In its active form interacts with and regulates several effectors including MAP4K4, MINK1 and TNIK. Part of a signaling complex composed of NEDD4, RAP2A and TNIK which regulates neuronal dendrite extension and arborization during development. More generally, it is part of several signaling cascades and may regulate cytoskeletal rearrangements, cell migration, cell adhesion and cell spreading. {ECO:0000269|PubMed:12133960, ECO:0000269|PubMed:18701680, ECO:0000269|PubMed:19061864}. PTM: Ubiquitinated; undergoes 'Lys-63' monoubiquitination and diubiquitination by NEDD4. Multiple lysine residues are probably modified. Ubiquitination requires TNIK, prevents interaction with effectors and inactivates RAP2A. {ECO:0000269|PubMed:20159449}.; PTM: Palmitoylated. Palmitoylation is required for association with recycling endosome membranes and activation of TNIK. {ECO:0000269|PubMed:19061864}. SUBCELLULAR LOCATION: Midbody {ECO:0000250}. Recycling endosome membrane {ECO:0000269|PubMed:19061864}; Lipid-anchor {ECO:0000269|PubMed:19061864}; Cytoplasmic side {ECO:0000269|PubMed:19061864}. Note=Localizes to midbody at telophase. May also localize to the Golgi and the gelatinase-containing granules of neutrophils. {ECO:0000250}. SUBUNIT: Interacts with PLCE1. Interacts with ARHGAP29, SGSM1, SGSM2 and SGSM3. Interacts (GTP-bound form preferentially) with MAP4K4. Interacts with MINK1. Interacts with cytoskeletal actin (By similarity). Interacts (GTP-bound form) with RUNDC3A. Interacts (GTP-bound form preferentially) with TNIK (via the CNH domain); the interaction is direct and recruits RAP2A to the E3 ubiquitin ligase NEDD4. Interacts with RGS14; the interaction is GTP-dependent. {ECO:0000250, ECO:0000269|PubMed:10926822, ECO:0000269|PubMed:20159449, ECO:0000269|PubMed:9523700}. DOMAIN: The effector domain mediates the interaction with RUNDC3A. {ECO:0000269|PubMed:9523700}. TISSUE SPECIFICITY: Expressed in granular layer of the cerebellum, forebrain, striatum, layer V of the cortex, olfactory cortex, tubercules, subthalamic and hippocampus, particularly in the CA2 region, to a lesser extent in the CA1 region and the external layer of the dentate gyrus. Expressed in neurons. {ECO:0000269|PubMed:10926822}. +Q8BU31 RAP2C_MOUSE Ras-related protein Rap-2c 183 20,745 Chain (1); Lipidation (3); Modified residue (1); Motif (1); Mutagenesis (3); Nucleotide binding (3); Propeptide (1); Sequence conflict (1) FUNCTION: Small GTP-binding protein which cycles between a GDP-bound inactive and a GTP-bound active form. May play a role in cytoskeletal rearrangements and regulate cell spreading through activation of the effector TNIK. May play a role in SRE-mediated gene transcription. {ECO:0000269|PubMed:19061864}. PTM: Palmitoylated. Palmitoylation is required for association with recycling endosome membranes and activation of TNIK. {ECO:0000269|PubMed:19061864}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Recycling endosome membrane {ECO:0000269|PubMed:19061864}; Lipid-anchor {ECO:0000269|PubMed:19061864}; Cytoplasmic side {ECO:0000269|PubMed:19061864}. +P12672 RAPSN_MOUSE 43 kDa receptor-associated protein of the synapse (RAPsyn) (43 kDa postsynaptic protein) (Acetylcholine receptor-associated 43 kDa protein) 412 46,393 Chain (1); Initiator methionine (1); Lipidation (1); Modified residue (2); Repeat (7); Sequence conflict (1); Zinc finger (1) FUNCTION: Postsynaptic protein required for clustering of nicotinic acetylcholine receptors (nAChRs) at the neuromuscular junction. It may link the receptor to the underlying postsynaptic cytoskeleton, possibly by direct association with actin or spectrin (By similarity). {ECO:0000250}. PTM: Ubiquitinated by the BCR(KLHL8) complex, leading to its degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell junction, synapse, postsynaptic cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Note=Cytoplasmic surface of postsynaptic membranes. DOMAIN: A cysteine-rich region homologous to part of the regulatory domain of protein kinase C may be important in interactions of this protein with the lipid bilayer. +P62984 RL40_MOUSE Ubiquitin-60S ribosomal protein L40 (Ubiquitin A-52 residue ribosomal protein fusion product 1) [Cleaved into: Ubiquitin; 60S ribosomal protein L40 (CEP52)] 128 14,728 Beta strand (3); Binding site (2); Chain (2); Cross-link (7); Domain (1); Helix (3); Modified residue (3); Site (1) FUNCTION: Ubiquitin: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling. {ECO:0000269|PubMed:19754430}.; FUNCTION: 60S ribosomal protein L40: Component of the 60S subunit of the ribosome. {ECO:0000269|PubMed:19754430}. PTM: Ubiquitin: Phosphorylated at Ser-65 by PINK1 during mitophagy. Phosphorylated ubiquitin specifically binds and activates parkin (PRKN), triggering mitophagy. Phosphorylation does not affect E1-mediated E2 charging of ubiquitin but affects discharging of E2 enzymes to form polyubiquitin chains. It also affects deubiquitination by deubiquitinase enzymes such as USP30. {ECO:0000250|UniProtKB:P62987}.; PTM: Ubiquitin: Mono-ADP-ribosylated at the C-terminus by PARP9, a component of the PPAR9-DTX3L complex. ADP-ribosylation requires processing by E1 and E2 enzymes and prevents ubiquitin conjugation to substrates such as histones. {ECO:0000250|UniProtKB:P62987}. SUBCELLULAR LOCATION: Ubiquitin: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.; SUBCELLULAR LOCATION: 60S ribosomal protein L40: Cytoplasm {ECO:0000250}. SUBUNIT: Ribosomal protein L40 is part of the 60S ribosomal subunit. Interacts with UBQLN1 (via UBA domain). {ECO:0000250|UniProtKB:P62987}. +P11416 RARA_MOUSE Retinoic acid receptor alpha (RAR-alpha) (Nuclear receptor subfamily 1 group B member 1) 462 50,735 Alternative sequence (1); Chain (1); Cross-link (3); DNA binding (1); Domain (1); Modified residue (5); Mutagenesis (8); Natural variant (2); Region (3); Sequence conflict (3); Zinc finger (2) FUNCTION: Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RXR/RAR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. In the absence of ligand, the RXR-RAR heterodimers associate with a multiprotein complex containing transcription corepressors that induce histone acetylation, chromatin condensation and transcriptional suppression. On ligand binding, the corepressors dissociate from the receptors and associate with the coactivators leading to transcriptional activation. RARA plays an essential role in the regulation of retinoic acid-induced germ cell development during spermatogenesis. Has a role in the survival of early spermatocytes at the beginning prophase of meiosis. In Sertoli cells, may promote the survival and development of early meiotic prophase spermatocytes. In concert with RARG, required for skeletal growth, matrix homeostasis and growth plate function. {ECO:0000269|PubMed:10660575, ECO:0000269|PubMed:15901285, ECO:0000269|PubMed:17205979, ECO:0000269|PubMed:17905941, ECO:0000269|PubMed:19078967, ECO:0000269|PubMed:19389355, ECO:0000269|PubMed:9230306}. PTM: Phosphorylated on serine and threonine residues. Phosphorylation does not change during cell cycle. Phosphorylation on Ser-77 is crucial for the N-terminal AF1 transcriptional activity. Under stress conditions, MAPK8 enhances phosphorylation on Thr-181, Ser-445 and Ser-461 leading to RARA ubiquitination and degradation. Phosphorylation by AKT1 inhibits the transactivation activity. On retinoic acid stimulation, phosphorylation on Ser-369 by RPS6KA5 promotes interaction with GTF2H3 and the CDK7-mediated phosphorylation of Ser-77. {ECO:0000269|PubMed:12079996, ECO:0000269|PubMed:19078967, ECO:0000269|PubMed:9230306}.; PTM: Sumoylated with SUMO2, mainly on Lys-399 which is also required for SENP6 binding. On all-trans retinoic acid (ATRA) binding, a confromational change may occur that allows sumoylation on two additional site, Lys-166 and Lys-171. Probably desumoylated by SENP6. Sumoylation levels determine nuclear localization and regulate ATRA-mediated transcriptional activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Nuclear localization depends on ligand binding, phosphorylation and sumoylation. Transloaction to the nucleus is dependent on activation of PKC and the downstream MAPK phosphorylation. SUBUNIT: Interacts with PRMT2 (By similarity). Interacts with LRIF1 (By similarity). Interacts with NCOA7 in a ligand-inducible manner. Interacts (via the ligand-binding domain) with PRAME; interaction is direct and ligand (retinoic acid)-dependent. Interacts with PRKAR1A; the interaction negatively. regulates RARA transcriptional activity. Interacts with NCOR1 and NCOR2; the interaction occurs in the absence of ligand and represses transcriptional activity. Interacts with NCOA3 and NCOA6 coactivators, leading to a strong increase of transcription of target genes. Interacts with CDK7; the interaction is enhanced by interaction with GTF2H3. Interacts with GTF2H3; the interaction requires prior phosphorylation on Ser-369 which then enhances interaction with CDK7. Interacts with ASXL1 and NCOA1. Interacts with ACTN4. {ECO:0000250|UniProtKB:P10276, ECO:0000269|PubMed:10788465, ECO:0000269|PubMed:17205979, ECO:0000269|PubMed:19078967, ECO:0000269|PubMed:9192892, ECO:0000269|PubMed:9230306}. DOMAIN: Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain. TISSUE SPECIFICITY: Expressed in Sertoli cells and germ cells. {ECO:0000269|PubMed:17905941}. +P62947 RL41_MOUSE 60S ribosomal protein L41 25 3,456 Chain (1) FUNCTION: Interacts with the beta subunit of protein kinase CKII and stimulates phosphorylation of DNA topoisomerase II alpha by CKII. {ECO:0000250}. +P22605 RARB_MOUSE Retinoic acid receptor beta (RAR-beta) (Nuclear receptor subfamily 1 group B member 2) 482 53,331 Alternative sequence (5); Beta strand (5); Chain (1); DNA binding (1); Domain (1); Helix (13); Modified residue (1); Region (2); Turn (4); Zinc finger (2) FUNCTION: Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RAR/RXR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. In the absence of ligand, acts mainly as an activator of gene expression due to weak binding to corepressors (By similarity). In concert with RARG, required for skeletal growth, matrix homeostasis and growth plate function. {ECO:0000250, ECO:0000269|PubMed:19389355}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Homodimer (By similarity). Heterodimer; with a RXR molecule. Binds DNA preferentially as a RAR/RXR heterodimer. Interacts weakly with NCOR2 (By similarity). {ECO:0000250}. DOMAIN: Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain. +P18911 RARG_MOUSE Retinoic acid receptor gamma (RAR-gamma) (Nuclear receptor subfamily 1 group B member 3) 458 50,891 Alternative sequence (2); Chain (1); Cross-link (2); DNA binding (1); Domain (1); Modified residue (1); Region (2); Sequence conflict (5); Zinc finger (2) FUNCTION: Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RAR/RXR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. In the absence of ligand, acts mainly as an activator of gene expression due to weak binding to corepressors (By similarity). Required for limb bud development. In concert with RARA or RARB, required for skeletal growth, matrix homeostasis and growth plate function. {ECO:0000250, ECO:0000269|PubMed:19389355, ECO:0000269|PubMed:8388780}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407, ECO:0000269|PubMed:15327771}. SUBUNIT: Homodimer (By similarity). Heterodimer with a RXR molecule (By similarity). Binds DNA preferentially as a RAR/RXR heterodimer (By similarity). Forms a complex with PUS1 and the SRA1 RNA in the nucleus. {ECO:0000250, ECO:0000269|PubMed:15327771}. DOMAIN: Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain. +Q9DD06 RARR2_MOUSE Retinoic acid receptor responder protein 2 (Chemerin) 162 18,350 Chain (1); Disulfide bond (3); Natural variant (1); Propeptide (1); Signal peptide (1) FUNCTION: Adipocyte-secreted protein (adipokine) that regulates adipogenesis, metabolism and inflammation through activation of the chemokine-like receptor 1 (CMKLR1). Its other ligands include G protein-coupled receptor 1 (GPR1) and chemokine receptor-like 2 (CCRL2). Positively regulates adipocyte differentiation, modulates the expression of adipocyte genes involved in lipid and glucose metabolism and might play a role in angiogenesis, a process essential for the expansion of white adipose tissue. Also acts as a proinflammatory adipokine, causing an increase in secretion of proinflammatory and prodiabetic adipokines, which further impair adipose tissue metabolic function and have negative systemic effects including impaired insulin sensitivity, altered glucose and lipid metabolism, and a decrease in vascular function in other tissues. Can have both pro- and anti-inflammatory properties depending on the modality of enzymatic cleavage by different classes of proteases. Acts as a chemotactic factor for leukocyte populations expressing CMKLR1, particularly immature plasmacytoid dendritic cells, but also immature myeloid DCs, macrophages and natural killer cells. Exerts an anti-inflammatory role by preventing TNF/TNFA-induced VCAM1 expression and monocytes adhesion in vascular endothelial cells. The effect is mediated via inhibiting activation of NF-kappa-B and CRK/p38 through stimulation of AKT1/NOS3 signaling and nitric oxide production. Exhibits an antimicrobial function in the skin. {ECO:0000269|PubMed:17635925, ECO:0000269|PubMed:18242188}. PTM: Secreted in an inactive precursor form, prochemerin, which is proteolytically processed by a variety of extracellular proteases to generate forms with differing levels of bioactivity. For example, the removal of six amino acids results in chemerin-156, which exhibits the highest activity, while removal of seven amino acids results in chemerin-155 which has slightly less activity. Some proteases are able to cleave at more than one site and chemerin forms may be sequentially processed by different enzymes to modulate activity levels. The coordinated expression and activity of chemerin-modifying enzymes is essential for regulating its bioactivation, inactivation and, consequently, biological function. Cathepsin G cleaves seven C-terminal amino acids from prochemerin (chemerin-155), elastase is able to cleave six (chemerin-156), eight (chemerin-154) or eleven (chemerin-151), plasmin cleaves five amino acids (chemerin-157), and tryptase cleaves five (chemerin-157) or eight (chemerin-154). Multiple cleavages might be required to fully activate chemerin, with an initial tryptase cleavage resulting in chemerin with low activity (chemerin-157), and a second cleavage by carboxypeptidase N or B producing highly active chemerin (chemerin-156) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17635925, ECO:0000269|PubMed:18242188}. TISSUE SPECIFICITY: Expressed in the differentiated adipocytes (at protein level). Abundantly expressed in the liver, adipose tissue including visceral, epididymal, and brown adipose tissue. {ECO:0000269|PubMed:17635925, ECO:0000269|PubMed:17767914, ECO:0000269|PubMed:18242188}. +P32883 RASK_MOUSE GTPase KRas (K-Ras 2) (Ki-Ras) (c-K-ras) (c-Ki-ras) [Cleaved into: GTPase KRas, N-terminally processed] 189 21,656 Alternative sequence (2); Chain (2); Initiator methionine (1); Lipidation (2); Modified residue (4); Motif (1); Mutagenesis (2); Nucleotide binding (4); Propeptide (1); Region (1) FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity (By similarity). Plays an important role in the regulation of cell proliferation (PubMed:6474169, PubMed:1352876). Plays a role in promoting oncogenic events by inducing transcriptional silencing of tumor suppressor genes (TSGs) in colorectal cancer (CRC) cells in a ZNF304-dependent manner (By similarity). {ECO:0000250|UniProtKB:P01116, ECO:0000269|PubMed:1352876, ECO:0000269|PubMed:6474169}. PTM: Acetylation at Lys-104 prevents interaction with guanine nucleotide exchange factors (GEFs). {ECO:0000250|UniProtKB:P01116}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P01116}; Lipid-anchor {ECO:0000250|UniProtKB:P01116}; Cytoplasmic side {ECO:0000250|UniProtKB:P01116}. Cytoplasm {ECO:0000250|UniProtKB:P01116}. SUBUNIT: Interacts with PHLPP. Interacts (active GTP-bound form preferentially) with RGS14 (By similarity). Interacts (when farnesylated) with PDE6D; this promotes dissociation from the cell membrane (By similarity). Interacts with SOS1 (By similarity). {ECO:0000250|UniProtKB:P01116, ECO:0000250|UniProtKB:P08644}. +Q9Z268 RASL1_MOUSE RasGAP-activating-like protein 1 (RAS protein activator like 1) (Ras GTPase-activating-like protein) 799 89,395 Chain (1); Compositional bias (1); Domain (4); Modified residue (1); Sequence conflict (1); Zinc finger (1) FUNCTION: Probable inhibitory regulator of the Ras-cyclic AMP pathway. Plays a role in dendrite formation by melanocytes. {ECO:0000250|UniProtKB:O95294}. +Q8C2K5 RASL3_MOUSE RAS protein activator like-3 1041 114,782 Alternative sequence (2); Chain (1); Coiled coil (2); Domain (3); Frameshift (1); Modified residue (13); Sequence conflict (3) FUNCTION: Functions as a Ras GTPase-activating protein. Plays an important role in the expansion and functions of natural killer T (NKT) cells in the liver by negatively regulating RAS activity and the down-stream ERK signaling pathway. {ECO:0000269|PubMed:25652366}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q86YV0}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q86YV0}. TISSUE SPECIFICITY: Predominantly expressed in hematopoietic tissues. +Q99MK9 RASF1_MOUSE Ras association domain-containing protein 1 (Protein 123F2) 340 38,789 Alternative sequence (2); Chain (1); Domain (2); Initiator methionine (1); Modified residue (2); Region (2); Zinc finger (1) FUNCTION: Potential tumor suppressor. Required for death receptor-dependent apoptosis. Mediates activation of Mediates activation of STK3/MST2 and STK4/MST1 during Fas-induced apoptosis by preventing their dephosphorylation. When associated with MOAP1, promotes BAX conformational change and translocation to mitochondrial membranes in response to TNF and TNFSF10 stimulation. Isoform A interacts with CDC20, an activator of the anaphase-promoting complex, APC, resulting in the inhibition of APC activity and mitotic progression. Inhibits proliferation by negatively regulating cell cycle progression at the level of G1/S-phase transition by regulating accumulation of cyclin D1 protein. Isoform C has been shown not to perform these roles, no function has been identified for this isoform. Isoform A disrupts interactions among MDM2, DAXX and USP7, thus contributing to the efficient activation of TP53 by promoting MDM2 self-ubiquitination in cell-cycle checkpoint control in response to DNA damage (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Isoform A: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. Note=Localizes to cytoplasmic microtubules during interphase, to bipolar centrosomes associated with microtubules during prophase, to spindle fibers and spindle poles at metaphase and anaphase, to the midzone during early telophase, and to the midbody in late telophase in cells. Colocalizes with MDM2 in the nucleus (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform C: Nucleus {ECO:0000250}. Note=Predominantly nuclear. {ECO:0000250}. SUBUNIT: Interacts with MAP1S and XPA. Binds to the N-terminal of CDC20 during prometaphase. Binds to STK3/MST2 and STK4/MST1. Isoform A interacts with MOAP1 and E4F1. Recruited to the TNFRSF1A and TNFRSF10A complexes in response to their respective cognate ligand, after internalization. Can self-associate. Isoform A interacts with RSSF5 and probably associates with HRAS via a RSSF1 isoform A-RSSF5 heterodimer. Part of a complex with MDM2, DAXX, RASSF1 and USP7. Isoform A interacts (via C-terminus) with DAXX (via N-terminus); the interaction is independent of MDM2 and TP53. Isoform A interacts (via N-terminus) with MDM2 (via C-terminus); the interaction is independent of TP53 (By similarity). {ECO:0000250}. +O08989 RASM_MOUSE Ras-related protein M-Ras (Muscle and microspikes Ras) (Ras-related protein R-Ras3) (X-Ras) 208 23,901 Beta strand (7); Chain (1); Compositional bias (1); Helix (10); Lipidation (1); Modified residue (1); Motif (1); Nucleotide binding (3); Propeptide (1) FUNCTION: May serve as an important signal transducer for a novel upstream stimuli in controlling cell proliferation. Weakly activates the MAP kinase pathway (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. SUBUNIT: Forms a multiprotein complex with SHOC2, Raf (RAF1) and protein phosphatase 1 (PPP1CA, PPP1CB and PPP1CC). Interacts (active GTP-bound form preferentially) with RGS14 (By similarity). Interacts with RGL3. {ECO:0000250, ECO:0000269|PubMed:11313946}. +Q64701 RBL1_MOUSE Retinoblastoma-like protein 1 (107 kDa retinoblastoma-associated protein) (p107) (pRb1) 1063 119,456 Alternative sequence (2); Chain (1); Modified residue (13); Region (4); Sequence conflict (4) FUNCTION: Key regulator of entry into cell division. Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation. Recruits and targets histone methyltransferases KMT5B and KMT5C, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-20' trimethylation. Probably acts as a transcription repressor by recruiting chromatin-modifying enzymes to promoters. Potent inhibitor of E2F-mediated trans-activation. Forms a complex with adenovirus E1A and with SV40 large T antigen. May bind and modulate functionally certain cellular proteins with which T and E1A compete for pocket binding. May act as a tumor suppressor. {ECO:0000269|PubMed:15750587}. PTM: Phosphorylated. SV40 large T antigen binds only to the unphosphorylated form, whereas the adenovirus E1A binds to both forms. Cell-cycle arrest properties are inactivated by phosphorylation on Thr-332, Ser-640, Ser-959 and Ser-970 by CDK4 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Interacts with AATF. Interacts with KDM5A. Component of the DREAM complex (also named LINC complex) at least composed of E2F4, E2F5, LIN9, LIN37, LIN52, LIN54, MYBL1, MYBL2, RBL1, RBL2, RBBP4, TFDP1 and TFDP2. The complex exists in quiescent cells where it represses cell cycle-dependent genes. It dissociates in S phase when LIN9, LIN37, LIN52 and LIN54 form a subcomplex that binds to MYBL2 (By similarity). Interacts with KMT5B, KMT5C and USP4. {ECO:0000250, ECO:0000269|PubMed:11571651, ECO:0000269|PubMed:15750587}. TISSUE SPECIFICITY: Highly expressed in fetal heart and liver. Expressed at low levels in all other fetal tissues except skeletal muscle. High levels in neonatal spleen and thymus with low levels in other tissues. In adult, highly expressed in testis. Barely detectable in other tissues. +E9Q9D5 RBL2A_MOUSE Rab-like protein 2A 223 25,610 Alternative sequence (3); Chain (1); Mutagenesis (1); Nucleotide binding (3); Sequence conflict (3) FUNCTION: Plays an essential role in male fertility, sperm intra-flagellar transport, and tail assembly. Binds, in a GTP-regulated manner, to a specific set of effector proteins including key proteins involved in cilia development and function and delivers them into the growing sperm tail. {ECO:0000269|PubMed:23055941}. SUBUNIT: Interacts with IFT27, IFT81, IFT172, ATP6V1E1, HK1, LDHC, MAPRE1 and HSPA2. {ECO:0000269|PubMed:23055941}. TISSUE SPECIFICITY: Isoform 2 is expressed in the testis and localizes to the mid-piece of the sperm tail (at protein level). Isoform 2 is expressed at higher levels in testis than isoform 1. Isoform 1 and isoform 2 are widely expressed and notably within other tissues containing motile cilia including the lung, trachea, brain, ovary and kidney. {ECO:0000269|PubMed:23055941}. +Q8BMG7 RBGPR_MOUSE Rab3 GTPase-activating protein non-catalytic subunit (Rab3 GTPase-activating protein 150 kDa subunit) (Rab3-GAP p150) (Rab3-GAP150) (Rab3-GAP regulatory subunit) 1366 152,535 Alternative sequence (1); Chain (1); Erroneous initiation (2); Modified residue (4); Sequence caution (1); Sequence conflict (7) FUNCTION: Regulatory subunit of a GTPase activating protein that has specificity for Rab3 subfamily (RAB3A, RAB3B, RAB3C and RAB3D). Rab3 proteins are involved in regulated exocytosis of neurotransmitters and hormones. Rab3 GTPase-activating complex specifically converts active Rab3-GTP to the inactive form Rab3-GDP. Required for normal eye and brain development. May participate in neurodevelopmental processes such as proliferation, migration and differentiation before synapse formation, and non-synaptic vesicular release of neurotransmitters (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=In neurons, it is enriched in the synaptic soluble fraction. {ECO:0000250}. SUBUNIT: The Rab3 GTPase-activating complex is a heterodimer composed of RAB3GAP and RAB3-GAP150. The Rab3 GTPase-activating complex interacts with DMXL2 (By similarity). Interacts with LMAN1 (By similarity). {ECO:0000250|UniProtKB:Q5U1Z0, ECO:0000250|UniProtKB:Q9H2M9}. +Q99J64 RBM43_MOUSE RNA-binding protein 43 (RNA-binding motif protein 43) 343 38,637 Chain (1); Domain (1) +Q91W59 RBMS1_MOUSE RNA-binding motif, single-stranded-interacting protein 1 (Single-stranded DNA-binding protein MSSP-1) 403 43,991 Alternative sequence (2); Chain (1); Domain (2); Erroneous initiation (1); Modified residue (1); Sequence conflict (1) FUNCTION: Single-stranded DNA binding protein that interacts with the region upstream of the MYC gene. Binds specifically to the DNA sequence motif 5'-[AT]CT[AT][AT]T-3'. Probably has a role in DNA replication. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. Expressed in all tissues except testis. {ECO:0000269|PubMed:10639566}. +Q6VN19 RBP10_MOUSE Ran-binding protein 10 (RanBP10) 620 67,188 Beta strand (14); Chain (1); Compositional bias (1); Domain (3); Erroneous initiation (2); Helix (4); Initiator methionine (1); Modified residue (9); Mutagenesis (1); Turn (5) FUNCTION: May act as an adapter protein to couple membrane receptors to intracellular signaling pathways (Probable). Core component of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1 (By similarity). Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but does not affect estrogen-induced transactivation (By similarity). Acts as a guanine nucleotide exchange factor (GEF) for RAN GTPase (PubMed:18347012). May play an essential role in hemostasis and in maintaining microtubule dynamics with respect to both platelet shape and function (PubMed:19801445). {ECO:0000250|UniProtKB:Q6VN20, ECO:0000269|PubMed:18347012, ECO:0000269|PubMed:19801445, ECO:0000305}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18347012}. Nucleus {ECO:0000269|PubMed:18347012}. Note=Predominantly cytoplasmic. Associates with cytoplasmic microtubules in mature megakaryocytes and platelets. SUBUNIT: May form homodimers. Identified in the CTLH complex that contains GID4, RANBP9 and/or RANBP10, MKLN1, MAEA, RMND5A (or alternatively its paralog RMND5B), GID8, ARMC8, WDR26 and YPEL5. Within this complex, MAEA, RMND5A (or alternatively its paralog RMND5B), GID8, WDR26, and RANBP9 and/or RANBP10 form the catalytic core, while GID4, MKLN1, ARMC8 and YPEL5 have ancillary roles. Interacts with RAN and RANBP9. Interacts with the HGF receptor MET. Interacts with AR (By similarity). Interacts with TUBB1 (PubMed:18347012). Interacts with YPEL5 (By similarity). May interact with TUBB5 (PubMed:18347012). Interacts with DDX4 (PubMed:27622290). {ECO:0000250|UniProtKB:Q6VN20, ECO:0000269|PubMed:18347012, ECO:0000269|PubMed:27622290}. DOMAIN: The SPRY domain mediates the interaction with MET. {ECO:0000250}. TISSUE SPECIFICITY: Expressed at highest levels in spleen and liver. Expressed in megakaryocytes and platelets (at protein level). {ECO:0000269|PubMed:18347012}. +D3Z4I3 RBM24_MOUSE RNA-binding protein 24 (RNA-binding motif protein 24) 236 24,822 Chain (1); Compositional bias (1); Domain (1); Region (1) FUNCTION: Multifunctional RNA-binding protein involved in the regulation of pre-mRNA splicing, mRNA stability and mRNA translation important for cell fate decision and differentiation (PubMed:25313962, PubMed:26844700). Plays a major role in pre-mRNA alternative splicing regulation. Mediates preferentially muscle-specific exon inclusion in numerous mRNAs important for striated cardiac and skeletal muscle cell differentiation (PubMed:25313962, PubMed:26844700). Binds to intronic splicing enhancer (ISE) composed of stretches of GU-rich motifs localized in flanking intron of exon that will be included by alternative splicing (PubMed:25313962). Involved in embryonic stem cell (ESC) transition to cardiac cell differentiation by promoting pre-mRNA alternative splicing events of several pluripotency and/or differentiation genes. Plays a role in the regulation of mRNA stability. Binds to 3'-untranslated region (UTR) AU-rich elements in target transcripts, such as CDKN1A and MYOG, leading to maintain their stabilities. Involved in myogenic differentiation by regulating MYOG levels. Binds to multiple regions in the mRNA 3'-UTR of TP63, hence inducing its destabilization. Promotes also the destabilization of the CHRM2 mRNA via its binding to a region in the coding sequence. Plays a role in the regulation of mRNA translation. Mediates repression of p53/TP53 mRNA translation through its binding to U-rich element in the 3'-UTR, hence preventing EIF4E from binding to p53/TP53 mRNA and translation initiation. Binds to a huge amount of mRNAs (By similarity). Required for embryonic heart development, sarcomer and M-band formation in striated muscles (PubMed:25313962, PubMed:29358667). {ECO:0000250|UniProtKB:Q9BX46, ECO:0000269|PubMed:25313962, ECO:0000269|PubMed:26844700, ECO:0000269|PubMed:29358667}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6GQD3}. Cytoplasm {ECO:0000269|PubMed:25217815}. SUBUNIT: Interacts with EIF4E; this interaction prevents EIF4E from binding to p53/TP53 mRNA and inhibits the assembly of translation initiation complex. {ECO:0000250|UniProtKB:Q9BX46}. DOMAIN: The RRM domain is necessary for mRNA stability and mRNA translation regulation. {ECO:0000250|UniProtKB:Q9BX46}. TISSUE SPECIFICITY: Expressed strongly in heart and skeletal muscles (PubMed:25313962). Weakly expressed in intestine, aorta, liver, lung, kidney, uterus and bladder (PubMed:25313962). {ECO:0000269|PubMed:25313962}. +Q91YE7 RBM5_MOUSE RNA-binding protein 5 (Putative tumor suppressor LUCA15) (RNA-binding motif protein 5) 815 92,311 Alternative sequence (1); Chain (1); Compositional bias (2); Domain (3); Modified residue (8); Region (2); Sequence conflict (4); Zinc finger (2) FUNCTION: Component of the spliceosome A complex. Regulates alternative splicing of a number of mRNAs. May modulate splice site pairing after recruitment of the U1 and U2 snRNPs to the 5' and 3' splice sites of the intron. May both positively and negatively regulate apoptosis by regulating the alternative splicing of several genes involved in this process, including FAS and CASP2/caspase-2. In the case of FAS, promotes production of a soluble form of FAS that inhibits apoptosis. In the case of CASP2/caspase-2, promotes production of a catalytically active form of CASP2/Caspase-2 that induces apoptosis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the spliceosome A complex (also known as the prespliceosome). Appears to dissociate from the spliceosome upon formation of the spliceosome B complex (also known as the precatalytic spliceosome), in which the heterotrimeric U4/U6.U5 snRNPs are bound. Interacts with U2AF2; this interaction is direct. Also interacts with ACIN1, PRPF8, SFRS3, SNRPB, SNRPN, SNRNP70 and SNRNP200; these interactions may be indirect (By similarity). {ECO:0000250}. +Q8VH51 RBM39_MOUSE RNA-binding protein 39 (Coactivator of activating protein 1 and estrogen receptors) (Coactivator of AP-1 and ERs) (RNA-binding motif protein 39) (RNA-binding region-containing protein 2) (Transcription coactivator CAPER) 530 59,407 Alternative sequence (2); Beta strand (5); Chain (1); Compositional bias (2); Cross-link (3); Domain (3); Helix (4); Initiator methionine (1); Modified residue (11); Region (4); Sequence conflict (2); Turn (2) FUNCTION: Transcriptional coactivator for steroid nuclear receptors ESR1/ER-alpha and ESR2/ER-beta, and JUN/AP-1. May be involved in pre-mRNA splicing process. {ECO:0000269|PubMed:11704680}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Interacts with NCOA6 and JUN (PubMed:11704680). Interacts with ESR1 and ESR2, in the presence of estradiol (E2) (PubMed:11704680). Interacts with RSRC1 (via Arg/Ser-rich domain) (By similarity). Interacts with SF3B1 (By similarity). Interacts with ZNF106 (via N-terminus) (PubMed:27418600). {ECO:0000250|UniProtKB:Q14498, ECO:0000269|PubMed:11704680, ECO:0000269|PubMed:27418600}. +Q8R1Q9 RBSK_MOUSE Ribokinase (RK) (EC 2.7.1.15) 323 34,119 Active site (1); Binding site (5); Chain (1); Metal binding (6); Nucleotide binding (2); Region (2) Carbohydrate metabolism; D-ribose degradation; D-ribose 5-phosphate from beta-D-ribopyranose: step 2/2. FUNCTION: Catalyzes the phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium. The resulting D-ribose-5-phosphate can then be used either for sythesis of nucleotides, histidine, and tryptophan, or as a component of the pentose phosphate pathway. {ECO:0000255|HAMAP-Rule:MF_03215}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03215}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03215}. SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03215}. +P25801 RBTN2_MOUSE Rhombotin-2 (Cysteine-rich protein TTG-2) (LIM domain only protein 2) (LMO-2) (T-cell translocation protein 2) 158 18,340 Beta strand (10); Chain (1); Domain (2); Helix (2); Turn (2) FUNCTION: Acts with TAL1/SCL to regulate red blood cell development. Also acts with LDB1 to maintain erythroid precursors in an immature state. {ECO:0000269|PubMed:9391090}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9391090}. SUBUNIT: Interacts with BEX2 and KDM5A (By similarity). Interacts via its LIM domains with ELF2 and LDB1. Also interacts with basic helix-loop-helix protein TAL1/SCL and can assemble in a complex with LMO2 and TAL1/SCL. {ECO:0000250, ECO:0000269|PubMed:12727888, ECO:0000269|PubMed:9001422, ECO:0000269|PubMed:9391090}. DOMAIN: The second LIM zinc-binding domain interacts with KDM5A. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in early mouse development in central nervous system, lung, kidney, liver and spleen but only very low levels occur in thymus. {ECO:0000269|PubMed:2034676}. +Q9JKK0 RCAN3_MOUSE Calcipressin-3 (Down syndrome candidate region 1-like protein 2) (Myocyte-enriched calcineurin-interacting protein 3) (MCIP3) (Regulator of calcineurin 3) 239 27,153 Chain (1); Region (1) FUNCTION: Inhibits calcineurin-dependent transcriptional responses by binding to the catalytic domain of calcineurin A. Could play a role during central nervous system development (By similarity). {ECO:0000250}. SUBUNIT: Interacts with protein phosphatase PPP3CA/calcineurin A. {ECO:0000250|UniProtKB:Q9UKA8}. +Q8CFE3 RCOR1_MOUSE REST corepressor 1 (Protein CoREST) 480 52,715 Chain (1); Coiled coil (2); Compositional bias (1); Cross-link (3); Domain (3); Erroneous initiation (1); Modified residue (3); Region (2); Sequence conflict (2) FUNCTION: Essential component of the BHC complex, a corepressor complex that represses transcription of neuron-specific genes in non-neuronal cells. The BHC complex is recruited at RE1/NRSE sites by REST and acts by deacetylating and demethylating specific sites on histones, thereby acting as a chromatin modifier. In the BHC complex, it serves as a molecular beacon for the recruitment of molecular machinery, including MeCP2 and SUV39H1, that imposes silencing across a chromosomal interval. Plays a central role in demethylation of Lys-4 of histone H3 by promoting demethylase activity of KDM1A on core histones and nucleosomal substrates. It also protects KDM1A from the proteasome. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development and controls hematopoietic differentiation. {ECO:0000269|PubMed:15907476, ECO:0000269|PubMed:17707228, ECO:0000269|PubMed:20346398}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00512, ECO:0000255|PROSITE-ProRule:PRU00624}. SUBUNIT: Component of a BHC histone deacetylase complex that contains HDAC1, HDAC2, HMG20B/BRAF35, KDM1A, RCOR1/CoREST and PHF21A/BHC80. The BHC complex may also contain ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I. Interacts with REST. Interacts with the SMARCE1/BAF57, suggesting that the BHC complex may recruit the ATP-dependent chromatin-remodeling SWI-SNF complex (By similarity). Interacts directly with GFI1 AND GFI1B in a RCOR/GFI/KDM1A/HDAC complex. Interacts with INMS1. {ECO:0000250, ECO:0000269|PubMed:17707228, ECO:0000269|PubMed:24227653}. DOMAIN: The SANT domains may bridge the nucleosomal substrates and the demethylase KDM1A. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the external germinal layer (EGL) and internal granular layer (IGL) of the cerebellum and in Purkinje cells (at protein level). {ECO:0000269|PubMed:20346398}. +Q99LJ7 RCBT2_MOUSE RCC1 and BTB domain-containing protein 2 (Chromosome condensation 1-like) (Regulator of chromosome condensation and BTB domain-containing protein 2) 551 60,164 Alternative sequence (1); Chain (1); Domain (1); Repeat (6); Sequence conflict (1) SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:22768142}. Note=Mainly found in the acrosomal cap region. {ECO:0000269|PubMed:22768142}. DOMAIN: The BTB domain might play a role in targeting to acrosomal vesicles. {ECO:0000269|PubMed:22768142}. TISSUE SPECIFICITY: Expressed in testis and heart (at protein level). {ECO:0000269|PubMed:22768142}. +O35698 RBY1A_MOUSE RNA-binding motif protein, Y chromosome, family 1 member A1 (RNA-binding motif protein 1) (Y chromosome RNA recognition motif 1) 380 43,216 Chain (1); Domain (1); Sequence conflict (1) FUNCTION: RNA-binding protein involved in pre-mRNA splicing. Required for sperm development. Acts additively with TRA2B to promote exon 7 inclusion of the survival motor neuron SMN. Binds non-specifically to mRNAs. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with splicing factor proteins SFRS3/SRP20, TRA2B/SFRS10, KHDRBS1/SAM68 and KHDRBS3. {ECO:0000269|PubMed:10823932}. TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:9499427}. +Q8BP92 RCN2_MOUSE Reticulocalbin-2 (Taipoxin-associated calcium-binding protein 49) (TCBP-49) 320 37,271 Calcium binding (6); Chain (1); Domain (6); Modified residue (1); Motif (1); Sequence conflict (2); Signal peptide (1) FUNCTION: Not known. Binds calcium (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138}. +Q9CQK3 RDM1_MOUSE RAD52 motif-containing protein 1 281 31,235 Chain (1); Domain (1); Region (2) FUNCTION: May confer resistance to the antitumor agent cisplatin. Binds to DNA and RNA (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Nucleus, nucleolus. Nucleus, Cajal body. Nucleus, PML body. Note=After treatment with proteasomal inhibitors and mild heat-shock stress is relocalized to the nucleolus as dot-like or irregular subnuclear structures. Colocalized with nuclear promyelocytic leukemia (PML) and Cajal bodies (CB); this association with nuclear bodies is enhanced in response to proteotoxic stress. Relocalized in nucleolar caps during transcriptional arrest (By similarity). {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. DOMAIN: C-terminal half contains cytoplasmic retention domains as well as determinants involved in its stress-induced nucleolar accumulation. {ECO:0000250}. +P22858 PTHR_MOUSE Parathyroid hormone-related protein (PTH-rP) (PTHrP) (Parathyroid hormone-like protein) (PLP) [Cleaved into: Osteostatin] 175 20,100 Chain (1); Motif (1); Peptide (1); Propeptide (1); Region (1); Signal peptide (1) FUNCTION: Neuroendocrine peptide which is a critical regulator of cellular and organ growth, development, migration, differentiation and survival and of epithelial calcium ion transport. Regulates endochondral bone development and epithelial-mesenchymal interactions during the formation of the mammary glands and teeth. Required for skeletal homeostasis. Promotes mammary mesenchyme differentiation and bud outgrowth by modulating mesenchymal cell responsiveness to BMPs. Upregulates BMPR1A expression in the mammary mesenchyme and this increases the sensitivity of these cells to BMPs and allows them to respond to BMP4 in a paracrine and/or autocrine fashion. BMP4 signaling in the mesenchyme, in turn, triggers epithelial outgrowth and augments MSX2 expression, which causes the mammary mesenchyme to inhibit hair follicle formation within the nipple sheath. {ECO:0000269|PubMed:17301089, ECO:0000269|PubMed:20501677}.; FUNCTION: Osteostatin is a potent inhibitor of osteoclastic bone resorption. {ECO:0000250}. PTM: There are several secretory forms, including osteostatin, arising from endoproteolytic cleavage of the initial translation product. Each of these secretory forms is believed to have one or more of its own receptors that mediates the normal paracrine, autocrine and endocrine actions (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Secreted {ECO:0000250}. SUBUNIT: PTHrP interacts with PTH1R (via N-terminal extracellular domain). {ECO:0000250}. +Q9D0P5 PYGO1_MOUSE Pygopus homolog 1 417 45,090 Beta strand (3); Chain (1); Compositional bias (2); Helix (3); Motif (1); Region (2); Turn (2); Zinc finger (1) FUNCTION: Involved in signal transduction through the Wnt pathway. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Interacts with BCL9 via The PHD-type zinc finger motiv, and thereby becomes part of the nuclear beta-catenin/TCF complex. Found in a complex with BCL9L, CDC73, CTNNB1 and PYGO1. Interacts with histone H3 mono-, di- or tri-methylated at 'Lys4' (H3K4me1, H3K4me2, H3K4me3); the interaction is enhanced by the interaction with BCL9 (By similarity). {ECO:0000250}. +Q9EPS2 PYY_MOUSE Peptide YY (PYY) (Peptide tyrosine tyrosine) [Cleaved into: Peptide YY(3-36) (PYY-II)] 98 11,064 Modified residue (2); Peptide (2); Propeptide (1); Sequence conflict (1); Signal peptide (1); Site (1) FUNCTION: This gut peptide inhibits exocrine pancreatic secretion, has a vasoconstrictory action and inhibitis jejunal and colonic mobility. PTM: The peptide YY form is cleaved at Pro-30 by the prolyl endopeptidase FAP (seprase) activity (in vitro) to generate peptide YY(3-36). {ECO:0000250|UniProtKB:P10082}. SUBCELLULAR LOCATION: Secreted. +Q62052 P_MOUSE P protein (Melanocyte-specific transporter protein) (Pink-eyed dilution protein) 833 91,869 Chain (1); Compositional bias (2); Glycosylation (3); Topological domain (13); Transmembrane (12) TRANSMEM 173 193 Helical. {ECO:0000255}.; TRANSMEM 326 346 Helical. {ECO:0000255}.; TRANSMEM 349 369 Helical. {ECO:0000255}.; TRANSMEM 382 402 Helical. {ECO:0000255}.; TRANSMEM 418 438 Helical. {ECO:0000255}.; TRANSMEM 502 522 Helical. {ECO:0000255}.; TRANSMEM 618 638 Helical. {ECO:0000255}.; TRANSMEM 640 660 Helical. {ECO:0000255}.; TRANSMEM 676 696 Helical. {ECO:0000255}.; TRANSMEM 719 739 Helical. {ECO:0000255}.; TRANSMEM 760 780 Helical. {ECO:0000255}.; TRANSMEM 811 831 Helical. {ECO:0000255}. TOPO_DOM 1 172 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 194 325 Extracellular. {ECO:0000255}.; TOPO_DOM 347 348 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 370 381 Extracellular. {ECO:0000255}.; TOPO_DOM 403 417 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 439 501 Extracellular. {ECO:0000255}.; TOPO_DOM 523 617 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 639 639 Extracellular. {ECO:0000255}.; TOPO_DOM 661 675 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 697 718 Extracellular. {ECO:0000255}.; TOPO_DOM 740 759 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 781 810 Extracellular. {ECO:0000255}.; TOPO_DOM 832 833 Cytoplasmic. {ECO:0000255}. FUNCTION: Could be involved in the transport of tyrosine, the precursor to melanin synthesis, within the melanocyte. Regulates the pH of melanosome and the melanosome maturation. One of the components of the mammalian pigmentary system. Seems to regulate the postranslational processing of tyrosinase, which catalyzes the limiting reaction in melanin synthesis. It can modulate intracellular glutathione metabolism. {ECO:0000269|PubMed:11310796}. SUBCELLULAR LOCATION: Melanosome membrane {ECO:0000269|PubMed:7991586}; Multi-pass membrane protein {ECO:0000269|PubMed:7991586}. TISSUE SPECIFICITY: Most abundant in melanocytes. Also present in neonatal and adult eye tissue presumably as a result of expression in the retinal pigmented epithelium and choroid body, known sites of melanogenesis in the eye. Small but detectable amounts also observed in fetal, neonatal and adult brain. Moderate amounts detected in adult testis and ovary. Not detected in heart, kidney, spleen, liver or thymus. {ECO:0000269|PubMed:1509264}. DISEASE: Note=Defects in Oca2 are a cause of hypopigmentation of the eyes, skin, and fur. The protein is missing or altered in six independent mutant alleles of the OCA2 locus, suggesting that disruption of this gene results in hypopigmentation phenotype that defines mutant OCA2 alleles. {ECO:0000269|PubMed:1509264}. +Q9CPX8 QCR10_MOUSE Cytochrome b-c1 complex subunit 10 (Complex III subunit 10) (Complex III subunit XI) (Ubiquinol-cytochrome c reductase complex 6.4 kDa protein) 56 6,539 Chain (1); Transmembrane (1) TRANSMEM 16 36 Helical. {ECO:0000255}. FUNCTION: This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. {ECO:0000250}.; FUNCTION: This protein may be closely linked to the iron-sulfur protein in the complex and function as an iron-sulfur protein binding factor. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}. SUBUNIT: The bc1 complex contains 11 subunits: 3 respiratory subunits (cytochrome b, cytochrome c1 and Rieske/UQCRFS1), 2 core proteins (UQCRC1/QCR1 and UQCRC2/QCR2) and 6 low-molecular weight proteins (UQCRH/QCR6, UQCRB/QCR7, UQCRQ/QCR8, UQCR10/QCR9, UQCR11/QCR10 and a cleavage product of Rieske/UQCRFS1). {ECO:0000250}. +Q9DB77 QCR2_MOUSE Cytochrome b-c1 complex subunit 2, mitochondrial (Complex III subunit 2) (Core protein II) (Ubiquinol-cytochrome-c reductase complex core protein 2) 453 48,235 Chain (1); Modified residue (4); Sequence conflict (2); Transit peptide (1) FUNCTION: This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. The core protein 2 is required for the assembly of the complex (By similarity). {ECO:0000250}. PTM: Acetylation of Lys-159 and Lys-250 is observed in liver mitochondria from fasted mice but not from fed mice. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Matrix side {ECO:0000250}. SUBUNIT: The bc1 complex contains 11 subunits: 3 respiratory subunits (cytochrome b, cytochrome c1 and Rieske/UQCRFS1), 2 core proteins (UQCRC1/QCR1 and UQCRC2/QCR2) and 6 low-molecular weight proteins (UQCRH/QCR6, UQCRB/QCR7, UQCRQ/QCR8, UQCR10/QCR9, UQCR11/QCR10 and a cleavage product of Rieske/UQCRFS1). {ECO:0000250}. +Q9D855 QCR7_MOUSE Cytochrome b-c1 complex subunit 7 (Complex III subunit 7) (Complex III subunit VII) (Ubiquinol-cytochrome c reductase complex 14 kDa protein) 111 13,527 Chain (1); Initiator methionine (1); Modified residue (10); Sequence conflict (2) FUNCTION: This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. This component is involved in redox-linked proton pumping (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane. SUBUNIT: The bc1 complex contains 11 subunits: 3 respiratory subunits (cytochrome b, cytochrome c1 and Rieske/UQCRFS1), 2 core proteins (UQCRC1/QCR1 and UQCRC2/QCR2) and 6 low-molecular weight proteins (UQCRH/QCR6, UQCRB/QCR7, UQCRQ/QCR8, UQCR10/QCR9, UQCR11/QCR10 and a cleavage product of Rieske/UQCRFS1). {ECO:0000250}. +Q3UNZ8 QORL2_MOUSE Quinone oxidoreductase-like protein 2 (EC 1.-.-.-) (Zeta-crystallin homolog 2) 350 37,809 Alternative sequence (2); Chain (1); Modified residue (4) +P47199 QOR_MOUSE Quinone oxidoreductase (EC 1.6.5.5) (NADPH:quinone reductase) (Zeta-crystallin) 331 35,269 Binding site (4); Chain (1); Initiator methionine (1); Modified residue (5); Nucleotide binding (3); Sequence conflict (2) FUNCTION: Does not have alcohol dehydrogenase activity. Binds NADP and acts through a one-electron transfer process. Orthoquinones, such as 1,2-naphthoquinone or 9,10-phenanthrenequinone, are the best substrates (in vitro). May act in the detoxification of xenobiotics. Interacts with (AU)-rich elements (ARE) in the 3'-UTR of target mRNA species and enhances their stability. NADPH binding interferes with mRNA binding (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homotetramer. {ECO:0000250}. +Q9D1R9 RL34_MOUSE 60S ribosomal protein L34 117 13,293 Chain (1); Cross-link (1); Modified residue (3) FUNCTION: Component of the large ribosomal subunit. {ECO:0000250|UniProtKB:P49207}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P49207}. Cytoplasm {ECO:0000250|UniProtKB:P49207}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q29223}. Note=Detected on cytosolic polysomes (By similarity). Detected in ribosomes that are associated with the rough endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:P49207, ECO:0000250|UniProtKB:Q29223}. SUBUNIT: Component of the large ribosomal subunit. {ECO:0000250|UniProtKB:P49207}. +Q8BKD6 R144B_MOUSE E3 ubiquitin-protein ligase RNF144B (EC 2.3.2.31) (IBR domain-containing protein 2) (RING finger protein 144B) 301 33,495 Active site (1); Chain (1); Erroneous initiation (1); Frameshift (1); Metal binding (20); Region (1); Sequence conflict (2); Transmembrane (1); Zinc finger (3) TRANSMEM 256 276 Helical. {ECO:0000255}. Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates such as LCMT2, thereby promoting their degradation. Induces apoptosis via a p53/TP53-dependent but caspase-independent mechanism. However, its overexpression also produces a decrease of the ubiquitin-dependent stability of BAX, a pro-apoptotic protein, ultimately leading to protection of cell death; But, it is not an anti-apoptotic protein per se (By similarity). {ECO:0000250}. PTM: Auto-ubiquitinated. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion membrane; Single-pass membrane protein. Cytoplasm. Note=Mostly cytosololic, accumulates in submitochondrial domains specifically upon apoptosis induction, in synchrony with BAX activation. {ECO:0000250}. SUBUNIT: Interacts with UBE2L3, UBE2L6 and LCMT2 as well as with BAX. {ECO:0000250}. DOMAIN: Members of the RBR family are atypical E3 ligases. They interact with the E2 conjugating enzyme UBE2L3 and function like HECT-type E3 enzymes: they bind E2s via the first RING domain, but require an obligate trans-thiolation step during the ubiquitin transfer, requiring a conserved cysteine residue in the second RING domain. {ECO:0000250|UniProtKB:O60260}. +Q8BJM3 R3HCL_MOUSE Coiled-coil domain-containing protein R3HCC1L (Growth inhibition and differentiation-related protein 88 homolog) (R3H and coiled-coil domain-containing protein 1-like) 775 84,481 Chain (1); Coiled coil (1); Modified residue (2); Region (1); Sequence conflict (10) SUBUNIT: May interact with the exon junction complex (EJC) composed at least of CASC3, EIF4A3, MAGOH and RBM8A. {ECO:0000250}. +Q80TM6 R3HD2_MOUSE R3H domain-containing protein 2 1044 114,583 Alternative sequence (4); Chain (1); Compositional bias (2); Domain (2); Erroneous initiation (2); Frameshift (1); Modified residue (9); Sequence conflict (4) SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q4VBF2 R3HD4_MOUSE R3H domain-containing protein 4 262 29,660 Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (2); Sequence conflict (1) SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q6PFE3 RA54B_MOUSE DNA repair and recombination protein RAD54B (EC 3.6.4.-) (RAD54 homolog B) 886 99,338 Chain (1); Domain (2); Modified residue (1); Motif (1); Nucleotide binding (1) FUNCTION: Involved in DNA repair and mitotic recombination. May play an active role in recombination processes in concert with other members of the RAD52 epistasis group. {ECO:0000269|PubMed:12548566}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Interacts with RAD51 through the NH2-terminal domain. {ECO:0000250}. +Q91V41 RAB14_MOUSE Ras-related protein Rab-14 215 23,897 Chain (1); Initiator methionine (1); Lipidation (2); Modified residue (2); Motif (1); Nucleotide binding (4) FUNCTION: Regulates, together with its guanine nucleotide exchange factor, DENND6A, the specific endocytic transport of ADAM10, N-cadherin/CDH2 shedding and cell-cell adhesion (By similarity). Involved in membrane trafficking between the Golgi complex and endosomes during early embryonic development. Regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. May act by modulating the kinesin KIF16B-cargo association to endosomes (By similarity). {ECO:0000250, ECO:0000269|PubMed:21238925}. SUBCELLULAR LOCATION: Recycling endosome {ECO:0000250|UniProtKB:P61106}. Early endosome membrane {ECO:0000250|UniProtKB:P61106}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P61106}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:P61106}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle, phagosome {ECO:0000250|UniProtKB:P61106}. Note=Recruited to recycling endosomes by DENND6A. Recruited to phagosomes containing S.aureus or M.tuberculosis. {ECO:0000250|UniProtKB:P61106}. SUBUNIT: Interacts with ZFYVE20 (By similarity). Interacts with KIF16B. {ECO:0000250, ECO:0000269|PubMed:21238925}. +P35292 RAB17_MOUSE Ras-related protein Rab-17 214 23,640 Chain (1); Lipidation (2); Modified residue (1); Motif (1); Mutagenesis (2); Nucleotide binding (3); Sequence conflict (2) FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab is involved in transcytosis, the directed movement of endocytosed material through the cell and its exocytosis from the plasma membrane at the opposite side. Mainly observed in epithelial cells, transcytosis mediates for instance, the transcellular transport of immunoglobulins from the basolateral surface to the apical surface. Most probably controls membrane trafficking through apical recycling endosomes in a post-endocytic step of transcytosis. Required for melanosome transport and release from melanocytes, it also regulates dendrite and dendritic spine development. May also play a role in cell migration. {ECO:0000269|PubMed:21291502, ECO:0000269|PubMed:22291024, ECO:0000269|PubMed:9490718, ECO:0000269|PubMed:9624171}. SUBCELLULAR LOCATION: Recycling endosome membrane {ECO:0000269|PubMed:21291502, ECO:0000269|PubMed:22291024, ECO:0000269|PubMed:9490718, ECO:0000269|PubMed:9624171}; Lipid-anchor {ECO:0000305|PubMed:9624171}; Cytoplasmic side {ECO:0000305|PubMed:9624171}. Melanosome {ECO:0000269|PubMed:21291502}. Cell projection, dendrite {ECO:0000269|PubMed:22291024}. Note=According to a report the protein is localized at the basolateral and apical plasma membrane of kidney epithelial cells (PubMed:8486736). It was later shown to localize to the apical recycling endosome in epithelial cells (PubMed:21291502). In neurons, localizes to the cell body and dendritic shaft and spine (PubMed:22291024). {ECO:0000269|PubMed:21291502, ECO:0000269|PubMed:22291024, ECO:0000269|PubMed:8486736}. TISSUE SPECIFICITY: Expressed in kidney, liver, and intestine mainly by epithelial cells. Expressed in hippocampus (at protein level). {ECO:0000269|PubMed:22291024, ECO:0000269|PubMed:8486736}. +O70579 PM34_MOUSE Peroxisomal membrane protein PMP34 (34 kDa peroxisomal membrane protein) (Solute carrier family 25 member 17) 307 34,413 Chain (1); Motif (1); Region (2); Repeat (3); Topological domain (7); Transmembrane (6) TRANSMEM 10 30 Helical; Name=1. {ECO:0000255}.; TRANSMEM 67 87 Helical; Name=2. {ECO:0000255}.; TRANSMEM 105 125 Helical; Name=3. {ECO:0000255}.; TRANSMEM 161 181 Helical; Name=4. {ECO:0000255}.; TRANSMEM 203 223 Helical; Name=5. {ECO:0000255}.; TRANSMEM 281 301 Helical; Name=6. {ECO:0000255}. TOPO_DOM 1 9 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 31 66 Lumenal. {ECO:0000255}.; TOPO_DOM 88 104 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 126 160 Lumenal. {ECO:0000255}.; TOPO_DOM 182 202 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 224 280 Lumenal. {ECO:0000255}.; TOPO_DOM 302 307 Cytoplasmic. {ECO:0000250}. FUNCTION: Peroxisomal transporter for multiple cofactors like coenzyme A (CoA), flavin adenine dinucleotide (FAD), flavin mononucleotide (FMN) and nucleotide adenosine monophosphate (AMP), and to a lesser extent for nicotinamide adenine dinucleotide (NAD(+)), adenosine diphosphate (ADP) and adenosine 3',5'-diphosphate (PAP). May catalyze the transport of free CoA, FAD and NAD(+) from the cytosol into the peroxisomal matrix by a counter-exchange mechanism. Inhibited by pyridoxal 5'-phosphate and bathophenanthroline in vitro (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Peroxisome membrane; Multi-pass membrane protein. SUBUNIT: Interacts (via N- and C-terminus peroxisomal targeting regions) with PEX19; the interaction occurs with the newly synthesized SLC25A17 in the cytosol. {ECO:0000250}. DOMAIN: The N- and C-terminal portions are exposed to the cytoplasm. A region between helical transmembrane domains (TM) 4 and 5 and TM1-TM3 or TM4-TM6 are necessary for the peroxisome-targeting activity (By similarity). Lacks a typical peroxisomal sorting signal. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in liver. +Q8BHT7 RGP1_MOUSE RAB6A-GEF complex partner protein 2 (Retrograde Golgi transport protein RGP1 homolog) 391 42,498 Chain (1); Erroneous initiation (1) FUNCTION: The RIC1-RGP1 complex acts as a guanine nucleotide exchange factor (GEF), which activates RAB6A by exchanging bound GDP for free GTP and may thereby required for efficient fusion of endosome-derived vesicles with the Golgi compartment. The RIC1-RGP1 complex participates in the recycling of mannose-6-phosphate receptors. {ECO:0000250|UniProtKB:Q92546}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q92546}. Membrane {ECO:0000250|UniProtKB:Q92546}. SUBUNIT: Forms a complex with RIC1; the interaction enhances RAB6A GTPase activity. Interacts with RIC1. Interacts with RAB6A; the interaction is direct with a preference for RAB6A-GDP. Interacts with RAB33B. {ECO:0000250|UniProtKB:Q92546}. +Q6GYP7 RGPA1_MOUSE Ral GTPase-activating protein subunit alpha-1 (GAP-related-interacting partner to E12) (GRIPE) (GTPase-activating RapGAP domain-like 1) (Tuberin-like protein 1) (p240) 2035 229,389 Alternative sequence (9); Chain (1); Coiled coil (1); Compositional bias (1); Domain (1); Erroneous initiation (1); Erroneous termination (1); Modified residue (16); Region (1); Sequence conflict (15) FUNCTION: Catalytic subunit of the heterodimeric RalGAP1 complex which acts as a GTPase activator for the Ras-like small GTPases RALA and RALB (By similarity). May interact with the HLH region of TCF3/isoform E12. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12200424}. Nucleus {ECO:0000269|PubMed:12200424}. Note=Translocated to the nucleus, when associated with TCF3/E12. SUBUNIT: Component of the heterodimeric RalGAP1 complex with RALGAPB. Heterodimerization is required for activity (By similarity). Interacts with the HLH region of TCF3/isoform E12. {ECO:0000250, ECO:0000269|PubMed:12200424}. TISSUE SPECIFICITY: Expressed during embryogenesis. Expressed in the adult brain, particularly in neurons of the cortex and hippocampus. {ECO:0000269|PubMed:12200424}. +Q80VM8 PNM8A_MOUSE Paraneoplastic antigen-like protein 8A (PNMA-like protein 1) 430 48,062 Chain (1) +Q9CQE5 RGS10_MOUSE Regulator of G-protein signaling 10 (RGS10) 181 21,151 Chain (1); Domain (1); Lipidation (1); Modified residue (2); Sequence conflict (1) FUNCTION: Regulates G protein-coupled receptor signaling cascades, including signaling downstream of the muscarinic acetylcholine receptor CHRM2. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. Modulates the activity of potassium channels that are activated in response to CHRM2 signaling. Activity on GNAZ is inhibited by palmitoylation of the G-protein. {ECO:0000250|UniProtKB:O43665}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:O43665}. Nucleus {ECO:0000250|UniProtKB:O43665}. Note=Forskolin treatment promotes phosphorylation and translocation to the nucleus. {ECO:0000250|UniProtKB:O43665}. SUBUNIT: Interacts with GNAZ, GNAI1 and GNAI3. Associates specifically with the activated, GTP-bound forms of GNAZ and GNAI3. {ECO:0000250|UniProtKB:O43665}. +Q9Z2H1 RGS11_MOUSE Regulator of G-protein signaling 11 443 51,075 Alternative sequence (1); Chain (1); Domain (3); Sequence conflict (3) FUNCTION: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. {ECO:0000250}. SUBUNIT: Heterodimer with Gbeta5 (By similarity). Interacts with RGS7BP, leading to regulate the subcellular location of the heterodimer formed with Gbeta5. {ECO:0000250, ECO:0000269|PubMed:15632198, ECO:0000269|PubMed:15897264}. +P97492 RGS14_MOUSE Regulator of G-protein signaling 14 (RGS14) (RAP1/RAP2-interacting protein) (RPIP1) 547 59,847 Beta strand (5); Chain (1); Domain (4); Helix (2); Modified residue (9); Mutagenesis (8); Region (1); Sequence conflict (2); Turn (3) FUNCTION: Regulates G protein-coupled receptor signaling cascades. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. Besides, modulates signal transduction via G protein alpha subunits by functioning as a GDP-dissociation inhibitor (GDI). Has GDI activity on G(i) alpha subunits GNAI1 and GNAI3, but not on GNAI2 and G(o) alpha subunit GNAO1. Has GAP activity on GNAI0, GNAI2 and GNAI3. May act as a scaffold integrating G protein and Ras/Raf MAPkinase signaling pathways. Inhibits platelet-derived growth factor (PDGF)-stimulated ERK1/ERK2 phosphorylation; a process depending on its interaction with HRAS and that is reversed by G(i) alpha subunit GNAI1. Acts as a positive modulator of microtubule polymerisation and spindle organization through a G(i)-alpha-dependent mechanism. Plays a role in cell division; required for completion of the first mitotic division of the embryo. Involved in visual memory processing capacity; when overexpressed in the V2 secondary visual cortex area. Involved in hippocampal-based learning and memory; acts as a suppressor of synaptic plasticity in CA2 neurons. Required for the nerve growth factor (NGF)-mediated neurite outgrowth. Involved in stress resistance. {ECO:0000269|PubMed:10926822, ECO:0000269|PubMed:15112653, ECO:0000269|PubMed:15525537, ECO:0000269|PubMed:15917656, ECO:0000269|PubMed:16246175, ECO:0000269|PubMed:20837545}. PTM: Phosphorylated by PKC. Phosphorylation is increased in presence of forskolin and may enhance the GDI activity on G(i) alpha subunit GNAI1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Nucleus, PML body. Cytoplasm. Membrane. Cell membrane {ECO:0000250}. Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cell projection, dendrite. Cell projection, dendritic spine. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density. Note=Localizes with spindle poles during metaphase. Shuttles between the nucleus and cytoplasm in a CRM1-dependent manner. Recruited from the cytosol to the plasma membrane by the inactive GDP-bound forms of G(i) alpha subunits GNAI1 and GNAI3. Recruited from the cytosol to membranes by the active GTP-bound form of HRAS. Colocalizes with G(i) alpha subunit GNAI1 and RIC8A at the plasma membrane. Colocalizes with BRAF and RAF1 in both the cytoplasm and membranes (By similarity). Associates with the perinuclear sheaths of microtubules (MTs) surrounding the pronuclei, prior to segregating to the anastral mitotic apparatus and subsequently the barrel- shaped cytoplasmic bridge between the nascent nuclei of the emerging 2-cell embryo. Localizes to a perinuclear compartment near the microtubule-organizing center (MTOC). Expressed in the nucleus during interphase and segregates to the centrosomes and astral MTs during mitosis. Shuttles between the nucleus and cytoplasm in a CRM1-dependent manner. Relocalizes to the nucleus in PML nuclear bodies in respons to heat stress. Colocalizes with RIC8A in CA2 hippocampal neurons. {ECO:0000250}. SUBUNIT: Interacts with GNAI1 and GNAI2 (PubMed:15112653, PubMed:17635935). Interacts with GNAI3 (By similarity). Interacts with GNAO1 (PubMed:10926822). Interacts (via RGS and GoLoco domains) with GNAI1; the interaction occurs in the centrosomes. Interaction with GNAI1 or GNAI3 (via active GTP- or inactive GDP-bound forms) prevents association of RGS14 with centrosomes or nuclear localization (By similarity). Interacts with RABGEF1; the interactions is GTP-dependent (PubMed:10926822, PubMed:15112653). Interacts with RAP2A; the interactions is GTP-dependent and does not alter its function on G(i) alpha subunits either as GAP or as GDI (PubMed:10926822, PubMed:15112653). Associates with microtubules (By similarity). Found in a complex with at least BRAF, HRAS, MAP2K1, MAPK3 and RGS14. Interacts with RIC8A (via C-terminus). Interacts (via RBD 1 domain) with HRAS (active GTP-bound form preferentially). Interacts (via RBD domains) with BRAF (via N-terminus); the interaction mediates the formation of a ternary complex with RAF1. Interacts (via RBD domains) with RAF1 (via N-terminus); the interaction mediates the formation of a ternary complex with BRAF. Interacts with KRAS (active GTP-bound form preferentially), MRAS (active GTP-bound form preferentially), NRAS (active GTP-bound form preferentially) and RRAS (active GTP-bound form preferentially) (By similarity). {ECO:0000250|UniProtKB:O08773, ECO:0000269|PubMed:10926822, ECO:0000269|PubMed:15112653, ECO:0000269|PubMed:17635935}. DOMAIN: The RGS domain is necessary for GTPase-activating protein (GAP) activity for G subunits and localization to the nucleus and centrosomes. {ECO:0000250}.; DOMAIN: The GoLoco domain is necessary for GDP-dissociation inhibitor (GDI) activity, translocation out of the nucleus and interaction with G(i) alpha subunits GNAI1, GNAI2 and GNAI3. {ECO:0000250}.; DOMAIN: The RBD domains are necessary for localization to the nucleus and centrosomes. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in pyramidal neurons of the CA1, CA2 and fasciola cinerea (FC) subregions of the hippocampus and in the olfactory cortex (at protein level). Expressed in brain, spleen, heart, liver, lung, kidney, skin and thymus (at protein level). Expressed in granular layer of the cerebellum, forbrain, striatum, layer V of the cortex, olfactory cortex, tubercules, subthalamic and hippocampus, particularly in the CA2 region, to a lesser extent in the CA1 region and the external layer of the dentate gyrus. Expressed in neurons. {ECO:0000269|PubMed:10926822, ECO:0000269|PubMed:15525537, ECO:0000269|PubMed:20837545, ECO:0000269|PubMed:21158412}. +Q99PG4 RGS18_MOUSE Regulator of G-protein signaling 18 (RGS18) 235 27,610 Chain (1); Domain (1); Modified residue (3) FUNCTION: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds to G(i) alpha-1, G(i) alpha-2, G(i) alpha-3 and G(q) alpha. SUBCELLULAR LOCATION: Cytoplasm. TISSUE SPECIFICITY: Expressed in bone marrow, spleen, fetal liver and lung. At very low levels expressed in heart. +Q9CX84 RGS19_MOUSE Regulator of G-protein signaling 19 (RGS19) 216 24,678 Chain (1); Compositional bias (1); Domain (1); Modified residue (3); Region (1); Sequence conflict (1) FUNCTION: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds to G-alpha subfamily 1 members, with the order G(i)a3 > G(i)a1 > G(o)a >> G(z)a/G(i)a2. Activity on G(z)-alpha is inhibited by phosphorylation and palmitoylation of the G-protein (By similarity). {ECO:0000250}. PTM: Fatty acylated. Heavily palmitoylated in the cysteine string motif (By similarity). {ECO:0000250}.; PTM: Phosphorylated, mainly on serine residues. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. SUBUNIT: Interacts with GIPC PDZ domain. {ECO:0000250}. +Q8K3Z9 PO121_MOUSE Nuclear envelope pore membrane protein POM 121 (Nucleoporin Nup121) (Pore membrane protein of 121 kDa) 1200 121,022 Chain (1); Compositional bias (7); Modified residue (15); Region (2); Sequence conflict (1); Site (1); Transmembrane (1) TRANSMEM 57 77 Helical. {ECO:0000255}. FUNCTION: Essential component of the nuclear pore complex (NPC). The repeat-containing domain may be involved in anchoring components of the pore complex to the pore membrane. When overexpressed in cells induces the formation of cytoplasmic annulate lamellae (AL) (By similarity). {ECO:0000250}. PTM: Proteolytically cleaved by caspase-3 during apoptosis. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nuclear pore complex {ECO:0000250}. Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=Stably associated with the NPC throughout interphase and the endoplasmic reticulum during metaphase. {ECO:0000250}. DOMAIN: Contains F-X-F-G repeats. +P31362 PO2F3_MOUSE POU domain, class 2, transcription factor 3 (Epoc-1) (Octamer-binding protein 11) (Oct-11) (Octamer-binding transcription factor 11) (OTF-11) 431 47,071 Chain (1); Compositional bias (1); DNA binding (1); Domain (1); Sequence conflict (3) FUNCTION: Transcription factor that binds to the octamer motif (5'-ATTTGCAT-3'). SUBCELLULAR LOCATION: Nucleus. TISSUE SPECIFICITY: Skin, thymus, stomach and testis. +P21952 PO3F1_MOUSE POU domain, class 3, transcription factor 1 (Octamer-binding protein 6) (Oct-6) (Octamer-binding transcription factor 6) (OTF-6) (POU domain transcription factor SCIP) 449 45,324 Chain (1); DNA binding (1); Domain (1); Helix (7); Sequence conflict (1) FUNCTION: Transcription factor that binds to the octamer motif (5'-ATTTGCAT-3'). Thought to be involved in early embryogenesis and neurogenesis. SUBCELLULAR LOCATION: Nucleus. TISSUE SPECIFICITY: Expressed in embryonal stem cells and in the developing brain. +Q80TC5 POGK_MOUSE Pogo transposable element with KRAB domain 607 69,598 Chain (1); Coiled coil (1); Cross-link (2); Domain (3); Erroneous initiation (3); Sequence conflict (1) SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q8BZH4 POGZ_MOUSE Pogo transposable element with ZNF domain 1409 154,910 Chain (1); Coiled coil (1); Compositional bias (1); Cross-link (9); Domain (2); Modified residue (10); Region (1); Sequence conflict (2); Zinc finger (9) FUNCTION: Plays a role in mitotic cell cycle progression and is involved in kinetochore assembly and mitotic sister chromatid cohesion. Probably through its association with CBX5 plays a role in mitotic chromosome segregation by regulating aurora kinase B/AURKB activation and AURKB and CBX5 dissociation from chromosome arms (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00583}. Chromosome {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Recruited to trimethylated 'Lys-9' of histone H3 (H3K9me3). {ECO:0000250}. SUBUNIT: Interacts with CBX1, CBX3, MAD2L2 and CHAMP1. Interacts with CBX5; POGZ competes with PXVXL motif-containing proteins such as INCENP and TRIM28 for interaction with CBX5. Interacts with PSIP1 isoform 1 (By similarity). {ECO:0000250}. +Q9QUT0 RHAG_MOUSE Ammonium transporter Rh type A (Erythrocyte membrane glycoprotein Rh50) (Rhesus blood group family type A glycoprotein) (Rh family type A glycoprotein) (Rh type A glycoprotein) (CD antigen CD241) 438 47,837 Chain (1); Glycosylation (4); Sequence conflict (1); Topological domain (13); Transmembrane (12) TRANSMEM 5 25 Helical. {ECO:0000255}.; TRANSMEM 62 82 Helical. {ECO:0000255}.; TRANSMEM 87 107 Helical. {ECO:0000255}.; TRANSMEM 122 142 Helical. {ECO:0000255}.; TRANSMEM 149 169 Helical. {ECO:0000255}.; TRANSMEM 179 199 Helical. {ECO:0000255}.; TRANSMEM 219 239 Helical. {ECO:0000255}.; TRANSMEM 250 270 Helical. {ECO:0000255}.; TRANSMEM 279 296 Helical. {ECO:0000255}.; TRANSMEM 301 321 Helical. {ECO:0000255}.; TRANSMEM 343 363 Helical. {ECO:0000255}.; TRANSMEM 373 393 Helical. {ECO:0000255}. TOPO_DOM 1 4 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 26 61 Extracellular. {ECO:0000255}.; TOPO_DOM 83 86 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 108 121 Extracellular. {ECO:0000255}.; TOPO_DOM 143 148 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 170 178 Extracellular. {ECO:0000255}.; TOPO_DOM 200 218 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 240 249 Extracellular. {ECO:0000255}.; TOPO_DOM 271 278 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 297 300 Extracellular. {ECO:0000255}.; TOPO_DOM 322 342 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 364 372 Extracellular. {ECO:0000255}.; TOPO_DOM 394 438 Cytoplasmic. {ECO:0000255}. FUNCTION: May be part of an oligomeric complex which is likely to have a transport or channel function in the erythrocyte membrane. Involved in ammonia transport across the erythrocyte membrane. Seems to act in monovalent cation transport. {ECO:0000250|UniProtKB:Q02094}. SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q02094}; Multi-pass membrane protein. SUBUNIT: Heterotetramer. {ECO:0000250}. +Q62086 PON2_MOUSE Serum paraoxonase/arylesterase 2 (PON 2) (EC 3.1.1.2) (EC 3.1.1.81) (Aromatic esterase 2) (A-esterase 2) (Serum aryldialkylphosphatase 2) 354 39,617 Active site (1); Chain (1); Disulfide bond (1); Glycosylation (3); Metal binding (8); Sequence conflict (8); Signal peptide (1) FUNCTION: Capable of hydrolyzing lactones and a number of aromatic carboxylic acid esters. {ECO:0000250}. PTM: Glycosylated. {ECO:0000250}.; PTM: The signal sequence is not cleaved. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. SUBUNIT: Homotrimer. {ECO:0000250}. +Q9ES83 POPD1_MOUSE Blood vessel epicardial substance (mBVES) (Popeye domain-containing protein 1) (Popeye protein 1) 358 41,016 Chain (1); Glycosylation (2); Modified residue (2); Mutagenesis (4); Region (2); Topological domain (4); Transmembrane (3) TRANSMEM 49 69 Helical. {ECO:0000255}.; TRANSMEM 71 91 Helical. {ECO:0000255}.; TRANSMEM 93 113 Helical. {ECO:0000255}. TOPO_DOM 1 48 Extracellular. {ECO:0000255}.; TOPO_DOM 70 70 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 92 92 Extracellular. {ECO:0000255}.; TOPO_DOM 114 358 Cytoplasmic. {ECO:0000255}. FUNCTION: Cell adhesion molecule involved in the establishment and/or maintenance of cell integrity. Involved in the formation and regulation of the tight junction (TJ) paracellular permeability barrier in epithelial cells (PubMed:16188940). Plays a role in VAMP3-mediated vesicular transport and recycling of different receptor molecules through its interaction with VAMP3 (PubMed:20057356). Plays a role in the regulation of cell shape and movement by modulating the Rho-family GTPase activity through its interaction with ARHGEF25/GEFT (PubMed:18541910). Induces primordial adhesive contact and aggregation of epithelial cells in a Ca(2+)-independent manner. Also involved in striated muscle regeneration and repair and in the regulation of cell spreading (PubMed:11839816). Important for the maintenance of cardiac function. Plays a regulatory function in heart rate dynamics mediated, at least in part, through cAMP-binding and, probably, by increasing cell surface expression of the potassium channel KCNK2 and enhancing current density (PubMed:26642364). Is a caveolae-associated protein important for the preservation of caveolae structural and functional integrity as well as for heart protection against ischemia injury (PubMed:24066022). {ECO:0000250|UniProtKB:Q8NE79, ECO:0000269|PubMed:10882522, ECO:0000269|PubMed:11839816, ECO:0000269|PubMed:16188940, ECO:0000269|PubMed:18541910, ECO:0000269|PubMed:20057356, ECO:0000269|PubMed:22354168, ECO:0000269|PubMed:24066022}. SUBCELLULAR LOCATION: Lateral cell membrane {ECO:0000250|UniProtKB:Q8NE79}. Cell junction, tight junction {ECO:0000269|PubMed:16188940}. Membrane {ECO:0000269|PubMed:22354168}; Multi-pass membrane protein {ECO:0000305}. Cell membrane, sarcolemma {ECO:0000269|PubMed:24066022}. Membrane, caveola {ECO:0000269|PubMed:24066022}. Note=Its movement from the cytoplasm to membrane is an early event occurring concurrently with cell-cell contact. Detected at cell-cell contact but never observed at the free surface of epithelial cells (By similarity). Colocalizes in epithelial cells with OCLN and TJP1 in an apical-lateral position within the z axis. Colocalizes with VAMP3 at the cell-cell contact in cardiac and skeletal muscle. {ECO:0000269|PubMed:16188940, ECO:0000269|PubMed:20057356}. SUBUNIT: Homodimer. Homodimerization requires the C-terminus cytoplasmic region (By similarity). Interacts (via the C-terminus cytoplasmic tail) with TJP1. Interacts (via the C-terminus cytoplasmic tail) with ARHGEF25/GEFT (via the DH domain). Interacts (via the C-terminus cytoplasmic tail) with VAMP3. Interacts with KCNK2; the interaction enhances KCNK2 surface expression and is inhibited by cAMP (PubMed:22354168, PubMed:26642364). Interacts with CAV3 (PubMed:24066022). {ECO:0000250|UniProtKB:Q9DG23, ECO:0000269|PubMed:16188940, ECO:0000269|PubMed:18541910, ECO:0000269|PubMed:20057356, ECO:0000269|PubMed:24066022, ECO:0000269|PubMed:26642364}. TISSUE SPECIFICITY: Expressed in epithelial cells, skeletal muscle, heart and intestinal smooth muscle (at protein level). Expressed in fetal and adult heart and skeletal muscle. {ECO:0000269|PubMed:10882522, ECO:0000269|PubMed:11839816, ECO:0000269|PubMed:16188940, ECO:0000269|PubMed:18541910}. +Q8BP97 RHBD3_MOUSE Rhomboid domain-containing protein 3 385 40,934 Alternative sequence (1); Chain (1); Domain (1); Transmembrane (5) TRANSMEM 13 33 Helical. {ECO:0000255}.; TRANSMEM 58 78 Helical. {ECO:0000255}.; TRANSMEM 95 115 Helical. {ECO:0000255}.; TRANSMEM 146 166 Helical. {ECO:0000255}.; TRANSMEM 168 188 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q62087 PON3_MOUSE Serum paraoxonase/lactonase 3 (EC 3.1.1.2) (EC 3.1.1.81) (EC 3.1.8.1) 354 39,351 Active site (1); Chain (1); Disulfide bond (1); Glycosylation (3); Metal binding (8); Modified residue (1); Sequence conflict (5); Signal peptide (1) FUNCTION: Has low activity towards the organophosphate paraxon and aromatic carboxylic acid esters. Rapidly hydrolyzes lactones such as statin prodrugs (e.g. lovastatin). Hydrolyzes aromatic lactones and 5- or 6-member ring lactones with aliphatic substituents but not simple lactones or those with polar substituents (By similarity). {ECO:0000250}. PTM: Glycosylated. {ECO:0000250}.; PTM: The signal sequence is not cleaved. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +Q9DAK3 RHBT1_MOUSE Rho-related BTB domain-containing protein 1 695 78,819 Chain (1); Domain (2); Nucleotide binding (3); Region (1); Sequence conflict (1) TISSUE SPECIFICITY: Highest expression in heart and testis. {ECO:0000269|PubMed:12426103}. +Q9DB28 POP5_MOUSE Ribonuclease P/MRP protein subunit POP5 (EC 3.1.26.5) 169 19,285 Chain (1); Frameshift (1); Modified residue (2); Sequence conflict (1) FUNCTION: Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. SUBUNIT: Component of nuclear RNase P and RNase MRP ribonucleoproteins. RNase P consists of an RNA moiety and at least 8 protein subunits; POP1, RPP14, RPP20/POP7, RPP25, RPP29/POP4, RPP30, RPP38 and RPP40. RNase MRP consists of an RNA moiety and at least 9 protein subunits; POP1, RPP14, RPP20/POP7, RPP25, RPP29/POP4, RPP30, RPP38, RPP40, POP5 and RPP21 (By similarity). {ECO:0000250}. +Q5FWK3 RHG01_MOUSE Rho GTPase-activating protein 1 (Rho-type GTPase-activating protein 1) 439 50,411 Chain (1); Domain (2); Modified residue (7); Motif (1); Sequence conflict (2); Site (1) FUNCTION: GTPase activator for the Rho, Rac and Cdc42 proteins, converting them to the putatively inactive GDP-bound state. Cdc42 seems to be the preferred substrate (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Found in a complex with XPO7, EIF4A1, ARHGAP1, VPS26A, VPS29, VPS35 and SFN. Interacts with BNIPL (By similarity). {ECO:0000250}. +P97393 RHG05_MOUSE Rho GTPase-activating protein 5 (Rho-type GTPase-activating protein 5) (p190-B) 1501 172,113 Chain (1); Compositional bias (1); Domain (7); Frameshift (1); Modified residue (9); Sequence conflict (17) FUNCTION: GTPase-activating protein for Rho family members. {ECO:0000250|UniProtKB:Q13017}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13017}. Cell membrane {ECO:0000250|UniProtKB:Q13017}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q13017}. Note=Also membrane-associated in a fibrillar pattern that colocalizes with the alpha5-beta1 integrin receptor (ITGA5/ITGB1) for fibronectin. {ECO:0000250|UniProtKB:Q13017}. SUBUNIT: May interact with RASA1/p120GAP. {ECO:0000250|UniProtKB:Q13017}. DOMAIN: The pG1 pseudoGTPase domain does not bind GTP. {ECO:0000250|UniProtKB:Q13017}. TISSUE SPECIFICITY: Expressed in spinal cord, cerebellum, kidney, testis and lung. {ECO:0000269|PubMed:9838117}. +O54834 RHG06_MOUSE Rho GTPase-activating protein 6 (Rho-type GTPase-activating protein 6) (Rho-type GTPase-activating protein RhoGAPX-1) 987 108,844 Alternative sequence (5); Chain (1); Domain (1); Erroneous initiation (2); Modified residue (14); Motif (1); Sequence conflict (15) FUNCTION: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. Could regulate the interactions of signaling molecules with the actin cytoskeleton. Promotes continuous elongation of cytoplasmic processes during cell motility and simultaneous retraction of the cell body changing the cell morphology (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. TISSUE SPECIFICITY: Expressed in retina and lung. +Q91WC1 POTE1_MOUSE Protection of telomeres protein 1 (mPot1) (POT1-like telomere end-binding protein) 640 70,863 Alternative sequence (2); Chain (1) FUNCTION: Component of the telomerase ribonucleoprotein (RNP) complex that is essential for the replication of chromosome termini. Is a component of the double-stranded telomeric DNA-binding TRF1 complex which is involved in the regulation of telomere length by cis-inhibition of telomerase. Also acts as a single-stranded telomeric DNA-binding protein and thus may act as a downstream effector of the TRF1 complex and may transduce information about telomere maintenance and/or length to the telomere terminus. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded TTAGGG repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways. Binds to two or more telomeric single-stranded 5'-TTAGGG-3' repeats (G-strand) and with high specificity to a minimal telomeric single-stranded 5'-TAGGGTTAG-3' sequence. Binds telomeric single-stranded sequences internally or at proximity of a 3'-end. Its activity is TERT dependent but it does not increase TERT activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, telomere {ECO:0000250}. Note=Colocalizes with telomeric DNA. {ECO:0000250}. SUBUNIT: Homodimer or homooligomer. Component of the shelterin complex (telosome) composed of TERF1, TERF2, TINF2, TERF2IP, ACD and POT1. Binds single-stranded telomeric DNA as a monomer. Associated component of the telomerase holoenzyme complex. Found in a complex with TERF1, TINF2 and TNKS1. Interacts with TNKS1. Forms heterodimers with ACD. Identified in a complex with ACD and single-stranded telomeric DNA. {ECO:0000250|UniProtKB:Q9NUX5}. +Q6IFT4 RHG20_MOUSE Rho GTPase-activating protein 20 (RA and RhoGAP domain-containing protein) (RARhoGAP) (Rho-type GTPase-activating protein 20) 1182 131,374 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (3); Modified residue (3) FUNCTION: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. {ECO:0000250}. +Q8BL80 RHG22_MOUSE Rho GTPase-activating protein 22 (Rho-type GTPase-activating protein 22) (p68RacGAP) 702 77,786 Alternative sequence (2); Chain (1); Coiled coil (1); Compositional bias (1); Domain (2); Frameshift (2); Modified residue (2); Mutagenesis (1); Sequence conflict (2) FUNCTION: Rho GTPase-activating protein involved in the signal transduction pathway that regulates endothelial cell capillary tube formation during angiogenesis. Acts as a GTPase activator for the RAC1 by converting it to an inactive GDP-bound state. Inhibits RAC1-dependent lamellipodia formation. May also play a role in transcription regulation via its interaction with VEZF1, by regulating activity of the endothelin-1 (EDN1) promoter. {ECO:0000269|PubMed:14966113}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14966113}. Nucleus {ECO:0000269|PubMed:14966113}. Note=Mainly cytoplasmic. Some fraction is nuclear. SUBUNIT: Interacts with VEZF1. TISSUE SPECIFICITY: Predominantly present in endothelial cells (at protein level). {ECO:0000269|PubMed:14966113}. +Q69ZH9 RHG23_MOUSE Rho GTPase-activating protein 23 (Rho-type GTPase-activating protein 23) 1483 161,832 Alternative sequence (1); Chain (1); Compositional bias (2); Cross-link (1); Domain (3); Erroneous initiation (1); Modified residue (11); Sequence conflict (1) FUNCTION: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. {ECO:0000250}. +Q8C4V1 RHG24_MOUSE Rho GTPase-activating protein 24 (Rho-type GTPase-activating protein 24) 747 84,100 Alternative sequence (3); Chain (1); Coiled coil (1); Domain (2); Erroneous initiation (1); Modified residue (10); Sequence conflict (1) FUNCTION: Rho GTPase-activating protein involved in cell polarity, cell morphology and cytoskeletal organization. Acts as a GTPase activator for the Rac-type GTPase by converting it to an inactive GDP-bound state. Controls actin remodeling by inactivating Rac downstream of Rho leading to suppress leading edge protrusion and promotes cell retraction to achieve cellular polarity. Able to suppress RAC1 and CDC42 activity in vitro. Overexpression induces cell rounding with partial or complete disruption of actin stress fibers and formation of membrane ruffles, lamellipodia, and filopodia. Isoform 2 is a vascular cell-specific GAP involved in modulation of angiogenesis (By similarity). {ECO:0000250}. PTM: Phosphorylated by ROCK, leading to activate the RacGAP activity. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell junction, adherens junction {ECO:0000250}. Cell junction, focal adhesion {ECO:0000250}. Cell projection {ECO:0000250}. Note=Localizes to actin stress fibers. In migrating cells, localizes to membrane lamellae and protusions (By similarity). {ECO:0000250}. SUBUNIT: Interacts with FLNA. {ECO:0000250}. DOMAIN: The coiled coil domain mediates the interaction with FLNA leading to its recruitment to lamellae. {ECO:0000250}. +Q8BYW1 RHG25_MOUSE Rho GTPase-activating protein 25 (Rho-type GTPase-activating protein 25) 648 73,383 Alternative sequence (2); Chain (1); Coiled coil (1); Domain (2); Erroneous initiation (1); Modified residue (5); Sequence conflict (2) FUNCTION: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. {ECO:0000250}. +Q6ZQ82 RHG26_MOUSE Rho GTPase-activating protein 26 (Rho-type GTPase-activating protein 26) 814 92,071 Chain (1); Compositional bias (1); Domain (3); Erroneous initiation (1); Sequence conflict (1) FUNCTION: GTPase-activating protein for RHOA and CDC42. {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Colocalizes with actin stress fibers and cortical actin structures. {ECO:0000250}. SUBUNIT: Binds to the C-terminus of PTK2/FAK1 (By similarity). Interacts with NYAP1, NYAP2 and MYO16. {ECO:0000250, ECO:0000269|PubMed:21946561}. +A2AB59 RHG27_MOUSE Rho GTPase-activating protein 27 (CIN85-associated multi-domain-containing Rho GTPase-activating protein 1) (Rho-type GTPase-activating protein 27) 869 97,049 Alternative sequence (1); Chain (1); Domain (6); Erroneous initiation (1); Modified residue (11) FUNCTION: Rho GTPase-activating protein which may be involved in clathrin-mediated endocytosis. GTPase activators for the Rho-type GTPases act by converting them to an inactive GDP-bound state. Has activity toward CDC42 and RAC1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. SUBUNIT: Interacts with SH3KBP1/CIN85. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. Highly expressed in kidney, lung, small intestine and thymus. {ECO:0000269|PubMed:15147912}. +Q8BN58 RHG28_MOUSE Rho GTPase-activating protein 28 (Rho-type GTPase-activating protein 28) 729 81,795 Alternative sequence (3); Chain (1); Domain (1); Erroneous initiation (1); Modified residue (2); Sequence conflict (7) FUNCTION: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. {ECO:0000250}. +Q8CGF1 RHG29_MOUSE Rho GTPase-activating protein 29 (Rho-type GTPase-activating protein 29) 1266 142,341 Alternative sequence (1); Chain (1); Coiled coil (1); Domain (2); Modified residue (12); Region (1); Sequence conflict (5); Zinc finger (1) FUNCTION: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. Has strong activity toward RHOA, and weaker activity toward RAC1 and CDC42. May act as a specific effector of RAP2A to regulate Rho (By similarity). In concert with RASIP1, suppresses RhoA signaling and dampens ROCK and MYH9 activities in endothelial cells and plays an essential role in blood vessel tubulogenesis. {ECO:0000250, ECO:0000269|PubMed:21396893}. SUBUNIT: Interacts with PTPN13/PTPL1. Interacts with RAP2A via its coiled coil domain (By similarity). Interacts with RASIP1. {ECO:0000250, ECO:0000269|PubMed:21396893}. +Q640N3 RHG30_MOUSE Rho GTPase-activating protein 30 (Rho-type GTPase-activating protein 30) 1101 120,114 Alternative sequence (1); Chain (1); Domain (1); Modified residue (3); Sequence conflict (8) FUNCTION: GTPase-activating protein (GAP) for RAC1 and RHOA, but not for CDC42. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasmic vesicle {ECO:0000250}. SUBUNIT: Interacts with RHOU in a GTP-independent manner. {ECO:0000250}. +A6X8Z5 RHG31_MOUSE Rho GTPase-activating protein 31 (Cdc42 GTPase-activating protein) 1425 155,276 Chain (1); Compositional bias (1); Domain (1); Modified residue (16); Mutagenesis (2); Sequence conflict (5) FUNCTION: Functions as a GTPase-activating protein (GAP) for RAC1 and CDC42. Required for cell spreading, polarized lamellipodia formation and cell migration. {ECO:0000269|PubMed:16860736, ECO:0000269|PubMed:9786927}. PTM: Phosphorylated on Thr-776 by GSK3; which reduces GAP activity. {ECO:0000269|PubMed:16024771, ECO:0000269|PubMed:17158447}. SUBCELLULAR LOCATION: Cell projection, lamellipodium. Cell junction, focal adhesion. SUBUNIT: Interacts with ITSN1, which inhibits GAP activity. Interacts with PARVA. Interacts with GTP-loaded RHOU (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed at highest levels in heart and lung. {ECO:0000269|PubMed:9786927}. +Q811P8 RHG32_MOUSE Rho GTPase-activating protein 32 (Brain-specific Rho GTPase-activating protein) (GAB-associated Cdc42/Rac GTPase-activating protein) (GC-GAP) (Rho-type GTPase-activating protein 32) (Rho/Cdc42/Rac GTPase-activating protein RICS) (RhoGAP involved in the beta-catenin-N-cadherin and NMDA receptor signaling) (p200RhoGAP) (p250GAP) 2089 229,719 Alternative sequence (1); Chain (1); Compositional bias (2); Domain (3); Modified residue (13); Mutagenesis (1); Region (2) FUNCTION: GTPase-activating protein (GAP) promoting GTP hydrolysis on RHOA, CDC42 and RAC1 small GTPases. May be involved in the differentiation of neuronal cells during the formation of neurite extensions. Involved in NMDA receptor activity-dependent actin reorganization in dendritic spines. May mediate cross-talks between Ras- and Rho-regulated signaling pathways in cell growth regulation. Isoform 2 has higher GAP activity. {ECO:0000269|PubMed:12454018, ECO:0000269|PubMed:12531901, ECO:0000269|PubMed:12819203, ECO:0000269|PubMed:16716191, ECO:0000269|PubMed:17272280}. PTM: Isoform 2 is phosphorylated on multiple tyrosine residues by FYN (By similarity). Phosphorylated tyrosine residues undergo dephosphorylation after stimulation of NMDA receptors. Phosphorylated in vitro by CaMK2 in the presence of calmodulin and calcium; which inhibits GAP activity. {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000269|PubMed:12531901, ECO:0000269|PubMed:27609886}. Cell projection, dendritic spine {ECO:0000269|PubMed:12531901}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:A7KAX9}. Endosome membrane {ECO:0000269|PubMed:17663722}. Golgi apparatus membrane {ECO:0000269|PubMed:17663722}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:17663722}. Membrane {ECO:0000250|UniProtKB:A7KAX9}. Note=Association to membrane via PX domain (By similarity). Associated with cortical actin in undifferentiated neuroblastoma cells, but localized to dendritic spine and postsynaptic density after differentiation (PubMed:12531901). Colocalizes with EGFR at the cell membrane upon EGF treatment (By similarity). Colocalizes with GAB2 at the cell membrane (By similarity). {ECO:0000250|UniProtKB:A7KAX9, ECO:0000269|PubMed:12531901}. SUBUNIT: Interacts with NTRK1 (via cytoplasmic domain); the interaction is independent of the phosphorylation state of NTRK1 (By similarity). Interacts with SHC3 (via SH2 domain) (By similarity). Interacts with RASA1 (via SH3 domain); the interaction is necessary for the Ras activation and cell transforming activities of ARHGAP32. Interacts with GAB1 and GAB2. Interacts with CRK and CRKL. Found in a complex with CRKL and BCAR1; upon EGF stimulation BCAR1 may be replaced by EGFR (By similarity). Interacts with NCK1 (via SH3 domain); NCK1 recruits phosphorylated BCAR1 to the complex. Isoform 2 interacts with FYN; the interaction appears to be dependent on tyrosine phosphorylation of ARHGAP32 (By similarity). Interacts with EGFR; the interaction requires EGF stimulation and is increased by SHC3. Interacts with CDC42; the interaction requires constitutively active CDC42. Interacts with CTNNB1, DLG4, CDH2 and GRIN2B (By similarity) (PubMed:12531901, PubMed:12857875, PubMed:16716191, PubMed:17272280, PubMed:17663722). Interacts with GPHN (PubMed:27609886). {ECO:0000250|UniProtKB:A7KAX9, ECO:0000269|PubMed:12531901, ECO:0000269|PubMed:12857875, ECO:0000269|PubMed:16716191, ECO:0000269|PubMed:17272280, ECO:0000269|PubMed:17663722, ECO:0000269|PubMed:27609886}. DOMAIN: The N-terminal PX domain interacts specifically with phosphatidylinositides. {ECO:0000269|PubMed:17663722}. TISSUE SPECIFICITY: Isoform 1 and isoform 2 are highly expressed in brain, specially in cortex, corpus striatum, hippocampus and thalamus. Low levels in cerebellum, colon, small intestine, and kidney. {ECO:0000269|PubMed:12454018, ECO:0000269|PubMed:12531901, ECO:0000269|PubMed:12819203, ECO:0000269|PubMed:12857875, ECO:0000269|PubMed:16716191, ECO:0000269|PubMed:17663722}. +Q91YM2 RHG35_MOUSE Rho GTPase-activating protein 35 (Glucocorticoid receptor DNA-binding factor 1) 1499 170,393 Binding site (3); Chain (1); Compositional bias (1); Domain (7); Modified residue (22); Mutagenesis (5); Nucleotide binding (4); Region (2) FUNCTION: Rho GTPase-activating protein (GAP). Binds several acidic phospholipids which inhibits the Rho GAP activity to promote the Rac GAP activity (PubMed:16971514). This binding is inhibited by phosphorylation by PRKCA (By similarity). Involved in cell differentiation as well as cell adhesion and migration, plays an important role in retinal tissue morphogenesis, neural tube fusion, midline fusion of the cerebral hemispheres and mammary gland branching morphogenesis (PubMed:11044403, PubMed:11283609, PubMed:18502760, PubMed:21945077). Transduces signals from p21-ras to the nucleus, acting via the ras GTPase-activating protein (GAP) (PubMed:16971514). Transduces SRC-dependent signals from cell-surface adhesion molecules, such as laminin, to promote neurite outgrowth. Regulates axon outgrowth, guidance and fasciculation (PubMed:11283609). Modulates Rho GTPase-dependent F-actin polymerization, organization and assembly, is involved in polarized cell migration and in the positive regulation of ciliogenesis and cilia elongation (PubMed:11044403, PubMed:26859289, PubMed:18502760). During mammary gland development, is required in both the epithelial and stromal compartments for ductal outgrowth (PubMed:21945077). Represses transcription of the glucocorticoid receptor by binding to the cis-acting regulatory sequence 5'-GAGAAAAGAAACTGGAGAAACTC-3'; this function is however unclear and would need additional experimental evidences (By similarity). {ECO:0000250|UniProtKB:Q9NRY4, ECO:0000269|PubMed:11044403, ECO:0000269|PubMed:11283609, ECO:0000269|PubMed:16971514, ECO:0000269|PubMed:18502760, ECO:0000269|PubMed:21945077, ECO:0000269|PubMed:26859289}. PTM: Phosphorylation of Tyr-1105 by PTK6 promotes the association with RASA1, inactivating RHOA while activating RAS. Phosphorylation at Tyr-308 by PDGFRA inhibits binding to GTF2I (By similarity). Phosphorylated by PRKCA at Ser-1221 and Thr-1226, induces relocalization from the cytoplasm to regions of plasma membrane ruffling and prevents the binding and substrate specificity regulation by phospholipids (PubMed:11044403). In brain, phosphorylated by FYN and SRC (PubMed:11283609). During focal adhesion formation, phosphorylated by MAPK1 and MAPK3 at the C-terminal region, probably at Ser-1451, Ser-1476, Thr-1480 and Ser-1483. Phosphorylation by MAPK1 and MAPK3 inhibits GAP function and localizes ARGHAP35 away from newly forming focal adhesions and stress fibers in cells spreading on fibronectin (By similarity). Phosphorylation at Ser-1476 and Thr-1480 by GSK3B requires priming by MAPK and inhibits RhoGAP activity and modulates polarized cell migration (PubMed:18502760). {ECO:0000250|UniProtKB:P81128, ECO:0000250|UniProtKB:Q9NRY4, ECO:0000269|PubMed:11044403, ECO:0000269|PubMed:11283609, ECO:0000269|PubMed:18502760}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:26859289}. Cytoplasm {ECO:0000269|PubMed:11044403}. Nucleus {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:11044403}. Note=In response to integrins and SDC4 and upon phosphorylation by PKC, relocalizes from the cytoplasm to regions of plasma membrane ruffling where it colocalizes with polymerized actin. {ECO:0000269|PubMed:11044403}. SUBUNIT: Interacts with the general transcription factor GTF2I, the interaction sequesters GTF2I in the cytoplasm (By similarity). Interacts with RASA1 (PubMed:16971514). {ECO:0000250, ECO:0000269|PubMed:16971514}. DOMAIN: N-terminal part (1-266) has GTPase activity. Required for proper cellular localization. Mutation of this region is a severely defective loss of function. Mutants have defective morphogenesis of neural retinal tissue, agenesis of the corpus callosum due to defectuous midline fusion of the cerebral hemispheres (PubMed:11044403). Mutants show defects in axon guidance and fasciculation (PubMed:11283609). {ECO:0000269|PubMed:11044403, ECO:0000269|PubMed:11283609}.; DOMAIN: The pG1 pseudoGTPase domain does not bind GTP. {ECO:0000250|UniProtKB:Q6NU25}. TISSUE SPECIFICITY: Expressed in the developing kidneys (PubMed:26859289). Expressed in all regions of the mature nervous system (at protein level) (PubMed:11044403). Detected in neutrophils (at protein level) (PubMed:20675588). {ECO:0000269|PubMed:11044403, ECO:0000269|PubMed:20675588, ECO:0000269|PubMed:26859289}. +Q9CW07 PP13G_MOUSE Protein phosphatase 1 regulatory subunit 3G 347 37,823 Chain (1); Domain (1); Frameshift (1); Modified residue (1) FUNCTION: Glycogen-targeting subunit for protein phosphatase 1 (PP1). Involved in the regulation of hepatic glycogenesis in a manner coupled to the fasting-feeding cycle and distinct from other glycogen-targeting subunits. {ECO:0000269|PubMed:21471512}. +P59281 RHG39_MOUSE Rho GTPase-activating protein 39 1107 125,206 Alternative sequence (1); Chain (1); Domain (4); Erroneous initiation (1); Initiator methionine (1); Modified residue (10); Sequence conflict (1) SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q8R4S0 PP14C_MOUSE Protein phosphatase 1 regulatory subunit 14C (Kinase-enhanced PP1 inhibitor) (PKC-potentiated PP1 inhibitory protein) 164 17,754 Chain (1); Compositional bias (4); Initiator methionine (1); Modified residue (5) FUNCTION: Inhibitor of the PP1 regulatory subunit PPP1CA. {ECO:0000269|PubMed:11812771}. PTM: The main inhibitory site appears to be Thr-72 (By similarity). Has over 600-fold higher inhibitory activity when phosphorylated, creating a molecular switch for regulating the phosphorylation status of PPP1CA substrates and smooth muscle contraction. {ECO:0000250, ECO:0000269|PubMed:11812771}. SUBCELLULAR LOCATION: Endomembrane system {ECO:0000269|PubMed:11812771}; Peripheral membrane protein {ECO:0000269|PubMed:11812771}. TISSUE SPECIFICITY: Detected in heart, muscle, spinal cord, hippocampus, hypothalamus, thalamus, midbrain, brain stem, cerebellum, brain cortex and olfactory bulb. {ECO:0000269|PubMed:11812771}. +Q7TT52 PP14D_MOUSE Protein phosphatase 1 regulatory subunit 14D (Gastrointestinal and brain-specific PP1-inhibitory protein 1) (GBPI-1) 146 16,817 Alternative sequence (1); Chain (1); Region (1) FUNCTION: Inhibitor of PPP1CA. Has inhibitory activity only when phosphorylated, creating a molecular switch for regulating the phosphorylation status of PPP1CA substrates and smooth muscle contraction (By similarity). {ECO:0000250}. PTM: Phosphorylated on several residues. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. TISSUE SPECIFICITY: Isoform 1 is detected in intestine, kidney, lung, spleen, stomach and brain. Isoform 2 is detected in testis. {ECO:0000269|PubMed:12974676}. +Q3UMT1 PP12C_MOUSE Protein phosphatase 1 regulatory subunit 12C (Protein phosphatase 1 myosin-binding subunit of 85 kDa) (Protein phosphatase 1 myosin-binding subunit p85) 782 84,685 Chain (1); Coiled coil (2); Compositional bias (1); Initiator methionine (1); Modified residue (8); Repeat (4); Sequence conflict (1) FUNCTION: Regulates myosin phosphatase activity. {ECO:0000250|UniProtKB:Q9BZL4}. PTM: Phosphorylation at Thr-560 is essential for its interaction with PPP1CB. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BZL4}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:Q9BZL4}. SUBUNIT: PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or PPP1CC, and one or several targeting or regulatory subunits. PPP1R12C mediates binding to myosin. Interacts via its N-terminus with PPP1CB. Interacts with IL16. Interacts with the coiled-coil domain of MPRIP. Interacts with NOD2 (By similarity). {ECO:0000250|UniProtKB:Q9BZL4, ECO:0000269|PubMed:15469989}. +P62137 PP1A_MOUSE Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (PP-1A) (EC 3.1.3.16) 330 37,540 Active site (1); Chain (1); Initiator methionine (1); Metal binding (7); Modified residue (7); Mutagenesis (2) FUNCTION: Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca(2+)/calmodulin dependent protein kinase II. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. Regulates NEK2 function in terms of kinase activity and centrosome number and splitting, both in the presence and absence of radiation-induced DNA damage. Regulator of neural tube and optic fissure closure, and enteric neural crest cell (ENCCs) migration during development. In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. May dephosphorylate CSNK1D and CSNK1E. Dephosphorylates CENPA (By similarity). Dephosphorylates the 'Ser-139' residue of ATG16L1 causing dissociation of ATG12-ATG5-ATG16L1 complex, thereby inhibiting autophagy (By similarity). {ECO:0000250|UniProtKB:P62136, ECO:0000269|PubMed:17609112, ECO:0000269|PubMed:21712997, ECO:0000269|PubMed:21930935, ECO:0000269|PubMed:22215812}. PTM: Phosphorylated. Dephosphorylated at Thr-320 in the presence of ionizing radiation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Note=Primarily nuclear and largely excluded from the nucleolus. Highly mobile in cells and can be relocalized through interaction with targeting subunits. NOM1 plays a role in targeting this protein to the nucleolus. In the presence of PPP1R8 relocalizes from the nucleus to nuclear speckles (By similarity). {ECO:0000250}. SUBUNIT: PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or PPP1CC, which is folded into its native form by inhibitor 2 and glycogen synthetase kinase 3, and then complexed to one or several targeting or regulatory subunits. PPP1R12A, PPP1R12B and PPP1R12C mediate binding to myosin. PPP1R3A (in skeletal muscle), PPP1R3B (in liver), PPP1R3C, PPP1R3D and PPP1R3F (in brain) mediate binding to glycogen. Interacts with PPP1R9A, PPP1R9B and PPP1R7. Interacts with PPP1R15A; the interaction mediates binding to EIF2S1. Interacts with YLPM1. Forms a complex with ILF2, ILF3, YLPM1, KHDRBS1, RBMX and NCOA5. Interacts with NOM1 and PPP1R8. Interacts with PPP1R16B. Interacts. with RPSA only in the presence of PPP1R16B. Component of the PTW/PP1 phosphatase complex, composed of PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA or PPP1CB or PPP1CC. Interacts with PPP1R10/PNUTS and PPP1R8. Interacts with WDR82 in the presence of PPP1R10/PNUTS. Interacts with PPP1R39. Interacts with TRIM28; the interaction dephosphorylates TRIM28 on 'Ser-824' and forms a complex at the p21 promoter site (By similarity). Interacts with PPP1R15B; the interaction mediates binding to EIF2S1. Part of a complex containing PPP1R15B, PP1 and NCK1/2. Interacts with NEK2. Interacts with FER; this promotes phosphorylation at Thr-320 (By similarity). Interacts with PHACTR4; which acts as an activator of PP1 activity. Interacts with BTBD10 (PubMed:18160256). Interacts with KCTD20 (PubMed:24156551). Interacts with FOXP3 (By similarity). Interacts with CENPA (By similarity). Interacts with ATG16L1 (By similarity). Found in a complex with PPP1CA, PPP1CC, SHC1 and PEAK1 (By similarity). {ECO:0000250|UniProtKB:P62136, ECO:0000250|UniProtKB:P62139, ECO:0000269|PubMed:14638860, ECO:0000269|PubMed:16835242, ECO:0000269|PubMed:17609112, ECO:0000269|PubMed:18160256, ECO:0000269|PubMed:24156551}. +P62141 PP1B_MOUSE Serine/threonine-protein phosphatase PP1-beta catalytic subunit (PP-1B) (EC 3.1.3.16) (EC 3.1.3.53) 327 37,187 Active site (1); Chain (1); Initiator methionine (1); Metal binding (7); Modified residue (2); Sequence conflict (5) FUNCTION: Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase (PP1) is essential for cell division, it participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. May dephosphorylate CSNK1D and CSNK1E. {ECO:0000269|PubMed:21712997, ECO:0000269|PubMed:21930935}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P62140}. Nucleus {ECO:0000250|UniProtKB:P62140}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P62140}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P62140}. Note=Highly mobile in cells and can be relocalized through interaction with targeting subunits. In the presence of PPP1R8 relocalizes from the nucleus to nuclear speckles. {ECO:0000250|UniProtKB:P62140}. SUBUNIT: PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or PPP1CC, which is folded into its native form by inhibitor 2 and glycogen synthetase kinase 3, and then complexed to one or several targeting or regulatory subunits. The targeting or regulatory subunits determine the substrate specificity of PP1. PPP1R12A, PPP1R12B and PPP1R12C mediate binding to myosin. PPP1R3A (in skeletal muscle), PPP1R3B (in liver), PPP1R3C, PPP1R3D and PPP1R3F (in brain) mediate binding to glycogen. Interacts with PPP1R7 and PPP1R12C. Interacts with PPP1R12A and NUAK1; the interaction is direct. Interacts with TRIM28; the interaction is weak (By similarity). Interacts with PPP1R15A; the interaction mediates binding to EIF2S1. Interacts with PPP1R16B. Component of the PTW/PP1 phosphatase complex, composed of PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA or PPP1CB or PPP1CC. Interacts with PPP1R8. Interacts with TRIM28; the interaction is weak (By similarity). Part of a complex containing PPP1R15B, PP1 and NCK1/2. Interacts with PPP1R15B; the interaction mediates binding to EIF2S1. Interacts with FOXP3 (By similarity). Interacts with RRP1B (By similarity). Interacts with SERPINE1 (By similarity). {ECO:0000250|UniProtKB:P62140, ECO:0000269|PubMed:14638860, ECO:0000269|PubMed:16835242}. +P63087 PP1G_MOUSE Serine/threonine-protein phosphatase PP1-gamma catalytic subunit (PP-1G) (EC 3.1.3.16) (Protein phosphatase 1C catalytic subunit) 323 36,984 Active site (1); Alternative sequence (1); Beta strand (15); Chain (1); Helix (11); Initiator methionine (1); Metal binding (7); Modified residue (3); Sequence conflict (3); Turn (4) FUNCTION: Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Dephosphorylates RPS6KB1. Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca(2+)/calmodulin dependent protein kinase II. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. May dephosphorylate CSNK1D and CSNK1E. {ECO:0000269|PubMed:21712997, ECO:0000269|PubMed:21930935}.; FUNCTION: Isoform 2: Required for normal male fertility. {ECO:0000269|PubMed:23082183}. PTM: Phosphorylated by NEK2. {ECO:0000250|UniProtKB:P36873}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P36873}. Nucleus {ECO:0000250|UniProtKB:P36873}. Cleavage furrow {ECO:0000250|UniProtKB:P36873}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P36873}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P36873}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:P36873}. Nucleus speckle {ECO:0000250|UniProtKB:P36873}. Midbody {ECO:0000250|UniProtKB:P36873}. Mitochondrion {ECO:0000250|UniProtKB:P36873}. Note=Colocalizes with SPZ1 in the nucleus (PubMed:15226296). Colocalizes with URI1 at mitochondrion. Rapidly exchanges between the nucleolar, nucleoplasmic and cytoplasmic compartments (By similarity). Highly mobile in cells and can be relocalized through interaction with targeting subunits (By similarity). In the presence of PPP1R8 relocalizes from the nucleolus to nuclear speckles (By similarity). Shows a dynamic targeting to specific sites throughout the cell cycle (By similarity). Highly concentrated in nucleoli of interphase cells and localizes at kinetochores early in mitosis (By similarity). Relocalization to chromosome-containing regions occurs at the transition from early to late anaphase (By similarity). Also accumulates at the cleavage furrow and midbody by telophase (By similarity). {ECO:0000250|UniProtKB:P36873, ECO:0000269|PubMed:15226296}. SUBUNIT: PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or PPP1CC, which is folded into its native form by inhibitor 2 and glycogen synthetase kinase 3, and then complexed to one or several targeting or regulatory subunits. PPP1R12A, PPP1R12B and PPP1R12C mediate binding to myosin. PPP1R3A (in skeletal muscle), PPP1R3B (in liver), PPP1R3C, PPP1R3D and PPP1R3F (in brain) mediate binding to glycogen. Interacts with PPP1R3B, PPP1R7 and CDCA2 (By similarity). Isoform 2 interacts with SPZ1. This interaction can prevent SPZ1 binding to the E-box and inhibits PPP1CC activity. PPP1R15A and PPP1R15B mediate binding to EIF2S1. Part of a complex containing PPP1R15B, PP1 and NCK1/2. Interacts with IKFZ1; the interaction targets PPP1CC to pericentromeric heterochromatin, dephosphorylates IKAROS, stabilizes it and prevents it from degradation. Interacts with NOM1 and PPP1R8. Component of the PTW/PP1 phosphatase complex, composed of PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA or PPP1CB or PPP1CC. Interacts with PPP1R8. Interacts with NEK2. Interacts with NEK2. Interacts with URI1; the interaction is phosphorylation-dependent and occurs in a growth factor-dependent manner (By similarity). Isoform 2 interacts with PPP1R42; the interaction is direct. Interacts with FOXP3 (By similarity). Isoform 2 interacts with TMEM225 (via RVxF motif) (PubMed:25605614). Isoform 2, but not isoform 1, interacts with Sh3glb1 testis-specific isoform 3; this interaction leads to the inhibition of phosphatase activity (PubMed:17381077). Interacts with MKI67 (By similarity). Interacts with RRP1B; this targets PPP1CC to the nucleolus (By similarity). Found in a complex with PPP1CA, PPP1CC, SHC1 and PEAK1 (By similarity). {ECO:0000250|UniProtKB:P36873, ECO:0000269|PubMed:14638860, ECO:0000269|PubMed:15226296, ECO:0000269|PubMed:16835242, ECO:0000269|PubMed:17381077, ECO:0000269|PubMed:19282287, ECO:0000269|PubMed:19886865, ECO:0000269|PubMed:25605614}. TISSUE SPECIFICITY: Isoform 1 is widely expressed (PubMed:9339378). Isoform 2 is highly enriched in testis, mainly restricted to meiotic and postmeiotic germ cells (PubMed:9339378). {ECO:0000269|PubMed:9339378}. +Q3UM45 PP1R7_MOUSE Protein phosphatase 1 regulatory subunit 7 (Protein phosphatase 1 regulatory subunit 22) 361 41,292 Chain (1); Domain (1); Frameshift (1); Initiator methionine (1); Modified residue (7); Repeat (11); Sequence conflict (3) FUNCTION: Regulatory subunit of protein phosphatase 1. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with PPP1CA, PPP1CB and PPP1CC/PPP1G. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed with high level in testis. Expression increases during puberty. Expressed in spermatids and probably also in spermatozoa. {ECO:0000269|PubMed:12972598}. +Q80W00 PP1RA_MOUSE Serine/threonine-protein phosphatase 1 regulatory subunit 10 (MHC class I region proline-rich protein CAT53) 888 94,372 Alternative sequence (1); Chain (1); Compositional bias (2); Cross-link (2); Domain (1); Modified residue (8); Motif (1); Mutagenesis (1); Region (5); Sequence conflict (4); Zinc finger (1) FUNCTION: Scaffold protein which mediates the formation of the PTW/PP1 phosphatase complex by providing a binding platform to each component of the complex. The PTW/PP1 phosphatase complex plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. Mediates interaction of WDR82 and PPP1CA. Inhibitor of PPP1CA and PPP1CC phosphatase activities. Has inhibitory activity on PPP1CA only when phosphorylated. Binds to mRNA, single-stranded DNA (ssDNA), poly(A) and poly(G) homopolymers. {ECO:0000269|PubMed:20516061}. PTM: Phosphorylated on Thr-398 by PKA within the region necessary for interaction with PPP1CA. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00649}. Note=Found in discrete nucleoplasmic bodies and within nucleoli (By similarity). Associates with chromatin during interphase, excluded from condensed chromosomes during early mitosis and is reloaded onto chromosomes at the late telophase. {ECO:0000250, ECO:0000269|PubMed:20516061}. SUBUNIT: Component of the PTW/PP1 phosphatase complex, composed of PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA or PPP1CB or PPP1CC. Interacts with PPP1CC (By similarity). Interacts with PPP1CA, WDR82 and TOX4. {ECO:0000250, ECO:0000269|PubMed:20516061}. +Q8K1L5 PP1RB_MOUSE E3 ubiquitin-protein ligase PPP1R11 (EC 2.3.2.27) (Protein phosphatase 1 regulatory subunit 11) (T-complex testis expressed protein 5) (Tctex-5) 131 14,544 Chain (1); Compositional bias (1); Initiator methionine (1); Modified residue (6); Region (2); Sequence conflict (2) Protein modification; protein ubiquitination. FUNCTION: Atypical E3 ubiquitin-protein ligase which ubiquitinates TLR2 at 'Lys-754' leading to its degradation by the proteasome. Plays a role in regulating inflammatory cytokine release and gram-positive bacterial clearance by functioning, in part, through the ubiquitination and degradation of TLR2 (PubMed:27805901). Inhibitor of protein phosphatase 1 (By similarity). {ECO:0000250|UniProtKB:O60927, ECO:0000269|PubMed:27805901}. PTM: Auto-ubiquitinated. {ECO:0000250|UniProtKB:O60927}. SUBUNIT: Interacts with TLR2 and UBE2D2. {ECO:0000269|PubMed:27805901}. TISSUE SPECIFICITY: Expressed in testis with high level during spermatogenesis. {ECO:0000269|PubMed:1718647}. +Q8K3A4 RHNO1_MOUSE RAD9, HUS1, RAD1-interacting nuclear orphan protein 1 235 26,820 Chain (1); Sequence conflict (3) FUNCTION: Plays a role in DNA damage response (DDR) signaling upon genotoxic stresses such as ionizing radiation (IR) during the S phase. Recruited to sites of DNA damage through interaction with the 9-1-1 cell-cycle checkpoint response complex and TOPBP1 in a ATR-dependent manner. Required for the progression of the G1 to S phase transition. Plays a role in the stimulation of CHEK1 phosphorylation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}. Note=Localizes to sites of DNA damage in a H2AX-independent manner. {ECO:0000250}. SUBUNIT: Interacts with RAD9A, RAD18, TOPBP1 and UBE2N. {ECO:0000250}. +Q9QUI0 RHOA_MOUSE Transforming protein RhoA 193 21,782 Beta strand (6); Chain (1); Compositional bias (1); Helix (9); Lipidation (1); Modified residue (2); Motif (1); Nucleotide binding (3); Propeptide (1); Sequence conflict (1); Turn (3) FUNCTION: Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Involved in a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Plays an essential role in cleavage furrow formation. May be an activator of PLCE1. Activated by ARHGEF2, which promotes the exchange of GDP for GTP. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization (By similarity). Required for the apical junction formation of keratinocyte cell-cell adhesion. Regulates KCNA2 potassium channel activity by reducing its location at the cell surface in response to CHRM1 activation; promotes KCNA2 endocytosis (PubMed:9635436). {ECO:0000250, ECO:0000269|PubMed:11777936, ECO:0000269|PubMed:20974804, ECO:0000269|PubMed:9635436}. PTM: Ubiquitinated by the BCR(KCTD13) and BCR(TNFAIP1) E3 ubiquitin ligase complexes, leading to its degradation by the proteasome, thereby regulating the actin cytoskeleton and synaptic transmission in neurons. {ECO:0000305|PubMed:29088697}.; PTM: Phosphorylation by PRKG1 at Ser-188 inactivates RHOA signaling (By similarity). Phosphorylation by SLK at Ser-188 in response to AGTR2 activation (By similarity). {ECO:0000250|UniProtKB:P61586, ECO:0000250|UniProtKB:P61589}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cleavage furrow {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Midbody {ECO:0000250}. Cell projection, lamellipodium {ECO:0000269|PubMed:11777936, ECO:0000269|PubMed:21543326}. Note=Translocates to the equatorial region before furrow formation in a ECT2-dependent manner. Localizes to the equatorial cell cortex (at the site of the presumptive furrow) in early anaphase in an activated form and in a myosin- and actin-independent manner (By similarity). Localized to cell-cell contacts in calcium-treated keratinocytes. {ECO:0000250}. SUBUNIT: Binds PRKCL1, ROCK1 and ROCK2. Interacts with ARHGEF2 and ARHGEF3. Interacts with PLCE1 and AKAP13. Interacts with DIAPH1. Interacts (in the constitutively activated, GTP-bound form) with DGKQ. Interacts with RACK1; enhances RHOA activation. Interacts with PKP4; the interaction is detected at the midbody. Interacts (GTP-bound form preferentially) with PKN2; the interaction stimulates autophosphorylation and phosphorylation of PKN2 (By similarity). Interacts with NET1, ARHGEF28 and RTKN. Interacts with ARHGDIA; this interaction inactivates and stabilizes RHOA. Interacts with ARHGDIB (By similarity). Interacts (GTP-bound form) with KCNA2 (via cytoplasmic N-terminal domain) (PubMed:9635436). Interacts (via GTP-bound form) with RIPOR1 (via N-terminus); this interaction links RHOA to STK24 and STK26 kinases (By similarity). Interacts with RIPOR2 (via active GTP- or inactive GDP-bound forms); this interaction is direct, blocks the loading of GTP to RHOA and decreases upon chemokine CCL19 stimulation in primary T lymphocytes (By similarity). {ECO:0000250|UniProtKB:P61586, ECO:0000269|PubMed:9635436}. +P62746 RHOB_MOUSE Rho-related GTP-binding protein RhoB 196 22,123 Chain (1); Lipidation (4); Modified residue (2); Motif (1); Nucleotide binding (3); Propeptide (1) FUNCTION: Mediates apoptosis in neoplastically transformed cells after DNA damage. Not essential for development but affects cell adhesion and growth factor signaling in transformed cells. Plays a negative role in tumorigenesis as deletion causes tumor formation. Involved in intracellular protein trafficking of a number of proteins. Targets PKN1 to endosomes and is involved in trafficking of the EGF receptor from late endosomes to lysosomes. Also required for stability and nuclear trafficking of AKT1/AKT which promotes endothelial cell survival during vascular development. Serves as a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Required for genotoxic stress-induced cell death in breast cancer cells. {ECO:0000269|PubMed:11353846, ECO:0000269|PubMed:11564874, ECO:0000269|PubMed:14597666}. PTM: Prenylation specifies the subcellular location of RHOB. The farnesylated form is localized to the plasma membrane while the geranylgeranylated form is localized to the endosome (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000269|PubMed:14597666}; Lipid-anchor {ECO:0000269|PubMed:14597666}. Cell membrane {ECO:0000269|PubMed:14597666}; Lipid-anchor {ECO:0000269|PubMed:14597666}. Nucleus {ECO:0000269|PubMed:14597666}. Cleavage furrow {ECO:0000250}. Note=Translocates to the equatorial region before furrow formation in a ECT2-dependent manner (By similarity). Late endosomal membrane (geranylgeranylated form). Plasma membrane (farnesylated form). Also detected at the nuclear margin and in the nucleus. {ECO:0000250}. SUBUNIT: Binds ROCK1 and ROCK2. Also binds PKN1/PRK1. Interacts with ARGGEF3 (By similarity). Interacts with RTKN (PubMed:8662891). Interacts with AKAP13. Interacts with RIPOR1 (By similarity). {ECO:0000250|UniProtKB:P62745, ECO:0000250|UniProtKB:P62747, ECO:0000269|PubMed:8662891}. +P97348 RHOD_MOUSE Rho-related GTP-binding protein RhoD 210 23,562 Chain (1); Lipidation (1); Modified residue (1); Motif (1); Nucleotide binding (3); Propeptide (1) FUNCTION: Involved in endosome dynamics. May coordinate membrane transport with the function of the cytoskeleton. Involved in the internalization and trafficking of activated tyrosine kinase receptors such as PDGFRB. Participates in the reorganization of actin cytoskeleton; the function seems to involve WHAMM and includes regulation of filopodia formation and actin filament bundling. Can modulate the effect of DAPK3 in reorganization of actin cytoskeleton and focal adhesion dissolution. {ECO:0000269|PubMed:23087206, ECO:0000269|PubMed:23454120, ECO:0000269|PubMed:24102721, ECO:0000269|PubMed:8945468}. SUBCELLULAR LOCATION: Cell membrane. Early endosome {ECO:0000269|PubMed:24102721}. Note=Colocalizes with RAB5 to early endosomes. {ECO:0000269|PubMed:24102721}. SUBUNIT: Interacts with PAK5. Interacts (in GTP-bound form) with DAPK3, FILIP1 and WHAMM. Interacts (independent of GTP-loaded status) with ANKFY1. {ECO:0000269|PubMed:23087206, ECO:0000269|PubMed:23454120, ECO:0000269|PubMed:24102721}. TISSUE SPECIFICITY: Widely expressed. +Q9D3G9 RHOH_MOUSE Rho-related GTP-binding protein RhoH 191 21,324 Chain (1); Lipidation (1); Modified residue (1); Motif (1); Mutagenesis (2); Nucleotide binding (3); Propeptide (1); Region (1) FUNCTION: Binds GTP but lacks intrinsic GTPase activity and is resistant to Rho-specific GTPase-activating proteins. Inhibits the activation of NF-kappa-B by TNF and IKKB and the activation of CRK/p38 by TNF. Inhibits activities of RAC1, RHOA and CDC42. Negatively regulates leukotriene production in neutrophils (By similarity). Negative regulator of hematopoietic progenitor cell proliferation, survival and migration. Critical regulator of thymocyte development and T-cell antigen receptor (TCR) signaling by mediating recruitment and activation of ZAP70. Required for phosphorylation of CD3Z, membrane translocation of ZAP70 and subsequent activation of the ZAP70-mediated pathways. Essential for efficient beta-selection and positive selection by promoting the ZAP70-dependent phosphorylation of the LAT signalosome during pre-TCR and TCR signaling. Crucial for thymocyte maturation during DN3 to DN4 transition and during positive selection. Plays critical roles in mast cell function by facilitating phosphorylation of SYK in Fc epsilon RI-mediated signal transduction. Essential for the phosphorylation of LAT, LCP2, PLCG1 and PLCG2 and for Ca(2+) mobilization in mast cells. {ECO:0000250, ECO:0000269|PubMed:15494435, ECO:0000269|PubMed:17028588, ECO:0000269|PubMed:17119112, ECO:0000269|PubMed:19124738}. PTM: Phosphorylated on tyrosine by LCK. Phosphorylated by FYN. Phosphorylation enhances the interactions with ZAP70 and SYK and is critical for its function in thymocyte development. {ECO:0000269|PubMed:17028588}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17028588}. Cell membrane {ECO:0000269|PubMed:17028588}; Lipid-anchor {ECO:0000269|PubMed:17028588}; Cytoplasmic side {ECO:0000269|PubMed:17028588}. Note=Colocalizes together with ZAP70 in the immunological synapse. SUBUNIT: Interacts with GDI1 and GDI2 (By similarity). Interacts with ZAP70 (via SH2 domains) and the interaction is enhanced by its phosphorylation by LCK. Interacts with SYK and the interaction is enhanced by its phosphorylation by FYN. {ECO:0000250, ECO:0000269|PubMed:17028588, ECO:0000269|PubMed:19124738}. DOMAIN: The region involved in interaction with ZAP70 is a non-canonical immunoreceptor tyrosine-based activation motif (ITAM). TISSUE SPECIFICITY: Expression is widespread in hematopoietic cells, including in bone marrow progenitor cells and in differentiated myeloid as well as lymphoid cells. Expressed at high levels in the thymus and mast cells, found in spleen and low-density bone marrow (LDBM) cells and is detected at a low level in neutrophils. In the thymus it is detected in thymocytes of the thymic cortex but not in non-lymphoid cells of fibrovascular and fibroadipose tissues. Expressed in T-cells, B-cells and mast cells. {ECO:0000269|PubMed:15494435, ECO:0000269|PubMed:19124738}. +Q9ER71 RHOJ_MOUSE Rho-related GTP-binding protein RhoJ (Tc10-like GTP-binding protein) 214 23,766 Alternative sequence (1); Chain (1); Lipidation (3); Modified residue (1); Motif (1); Nucleotide binding (5); Propeptide (1); Sequence conflict (1) FUNCTION: Plasma membrane-associated small GTPase specifically involved in angiogenesis (By similarity). Required for endothelial cell migration during vascular development via its interaction with GLUL (By similarity). Elicits the formation of F-actin-rich structures, thereby regulating endothelial cell migration (PubMed:10967094). {ECO:0000250|UniProtKB:Q9H4E5, ECO:0000269|PubMed:10967094}. PTM: Palmitoylated; regulates localization to the plasma membrane and may be mediated by GLUL. {ECO:0000250|UniProtKB:Q9H4E5}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9H4E5}; Lipid-anchor {ECO:0000250|UniProtKB:Q9H4E5}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9H4E5}. Note=Localization to the plasma membrane is regulated by GLUL. {ECO:0000250|UniProtKB:Q9H4E5}. SUBUNIT: Interacts with the CRIB domains of proteins such as Pak1 and Was/Wasp (PubMed:10967094). Interacts with GLUL (By similarity). {ECO:0000250|UniProtKB:Q9H4E5, ECO:0000269|PubMed:10967094}. TISSUE SPECIFICITY: Highly expressed in heart with moderate levels in lung and liver (PubMed:10967094). Very low levels detected in brain, spleen, skeletal muscle, kidney and testis (PubMed:10967094). {ECO:0000269|PubMed:10967094}. +Q8R527 RHOQ_MOUSE Rho-related GTP-binding protein RhoQ (Ras-like protein TC10) 205 22,645 Chain (1); Lipidation (1); Modified residue (1); Motif (1); Nucleotide binding (3); Propeptide (1); Sequence conflict (1) FUNCTION: Plasma membrane-associated small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses. Involved in epithelial cell polarization processes. May play a role in CFTR trafficking to the plasma membrane. Causes the formation of thin, actin-rich surface projections called filopodia (By similarity). {ECO:0000250}. PTM: May be post-translationally modified by both palmitoylation and polyisoprenylation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. SUBUNIT: Interacts with EXO70, CDC42EP1, CDC42EP2 and CDC42EP3 in a GTP-dependent manner (By similarity). Interacts with CDC42EP4, PARD6A, PARD6G (and probably PARD6B) in a GTP-dependent manner. Part of a quaternary complex containing PARD3, some PARD6 protein (PARD6A, PARD6B or PARD6G) and some atypical PKC protein (PRKCI or PRKCZ). Interacts with GOPC (By similarity). Interacts with ARHGAP33/TCGAP. {ECO:0000250, ECO:0000269|PubMed:10490598, ECO:0000269|PubMed:12773384}. +Q9EQT3 RHOU_MOUSE Rho-related GTP-binding protein RhoU (Rho GTPase-like protein ARHU) (Wnt-1 responsive Cdc42 homolog 1) (WRCH-1) 261 28,354 Chain (1); Lipidation (1); Nucleotide binding (3) FUNCTION: Acts upstream of PAK1 to regulate the actin cytoskeleton, adhesion turnover and increase cell migration. Stimulates quiescent cells to reenter the cell cycle. Has no detectable GTPase activity but its high intrinsic guanine nucleotide exchange activity suggests it is constitutively GTP-bound. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape (By similarity). {ECO:0000250}. PTM: Tyrosine phosphorylated by SRC in response to PTK2B/PYK2 activation. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q7L0Q8}; Lipid-anchor {ECO:0000250|UniProtKB:Q7L0Q8}; Cytoplasmic side {ECO:0000250|UniProtKB:Q7L0Q8}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q7L0Q8}; Lipid-anchor {ECO:0000250|UniProtKB:Q7L0Q8}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q7L0Q8}. Cell projection, podosome {ECO:0000250|UniProtKB:Q7L0Q8}. Note=Localizes to podosomes in SRC-transformed cells. {ECO:0000250|UniProtKB:Q7L0Q8}. SUBUNIT: Interacts with PAK3 (By similarity). Interacts with ARHGAP30 in a GTP-independent manner. In its GTP-loaded conformation, interacts with ARHGAP31. Interacts with PTK2B/PYK2 (By similarity). {ECO:0000250}. +Q8VDU1 RHOV_MOUSE Rho-related GTP-binding protein RhoV 236 26,148 Chain (1); Lipidation (1); Modified residue (1); Nucleotide binding (3) FUNCTION: Plays a role in the control of the actin cytoskeleton via activation of the JNK pathway. {ECO:0000250|UniProtKB:Q9Z1Y0}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9Z1Y0}; Lipid-anchor {ECO:0000250|UniProtKB:Q9Z1Y0}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9Z1Y0}. Endosome membrane {ECO:0000250|UniProtKB:Q9Z1Y0}; Lipid-anchor {ECO:0000250|UniProtKB:Q9Z1Y0}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9Z1Y0}. Note=Treatment with TNFA activates endosomal but not plasma membrane RHOV. {ECO:0000250|UniProtKB:Q9Z1Y0}. SUBUNIT: Interacts with PAK2. {ECO:0000250|UniProtKB:Q9Z1Y0}. +P52651 RHOX5_MOUSE Homeobox protein Rhox5 (Homeobox protein Pem) (Placenta and embryonic expression protein) (Reproductive homeobox on chromosome X 5) 210 23,045 Chain (1); DNA binding (1) FUNCTION: Transcription factor required for differentiation of embryonic stem cells (ESCs) into primordial germ cells. {ECO:0000269|PubMed:24074865}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q61085 RHPN1_MOUSE Rhophilin-1 (GTP-Rho-binding protein 1) 643 71,319 Chain (1); Domain (3); Modified residue (1); Sequence conflict (1) FUNCTION: Has no enzymatic activity. May serve as a target for Rho, and interact with some cytoskeletal component upon Rho binding or relay a Rho signal to other molecules. {ECO:0000269|PubMed:8571126}. SUBUNIT: Binds specifically to GTP-Rho. Interacts with ROPN1. {ECO:0000269|PubMed:10591629}. DOMAIN: The PDZ domain mediates interaction with ROPN1. {ECO:0000269|PubMed:10591629}. TISSUE SPECIFICITY: Highly expressed in testis. {ECO:0000269|PubMed:10591629}. +Q8BWR8 RHPN2_MOUSE Rhophilin-2 (GTP-Rho-binding protein 2) 686 76,957 Beta strand (4); Chain (1); Compositional bias (1); Domain (3); Helix (2); Modified residue (1); Region (1); Sequence conflict (2); Turn (1) FUNCTION: Binds specifically to GTP-Rho. May function in a Rho pathway to limit stress fiber formation and/or increase the turnover of F-actin structures in the absence of high levels of RhoA activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}. SUBUNIT: Interacts with GTP-bound RhoA and RhoB. Interacts with both GTP- and GDP-bound RhoA. Interacts with KRT18 (By similarity). {ECO:0000250}. +F6YCR7 RHX13_MOUSE Homeobox protein Rhox13 (Reproductive homeobox protein 13) 232 25,316 Chain (1); Compositional bias (2); DNA binding (1); Sequence conflict (1) FUNCTION: Probable transcription factor. {ECO:0000305}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|RuleBase:RU000682, ECO:0000269|PubMed:18675325}. +Q3KNY5 RIAD1_MOUSE RIIa domain-containing protein 1 119 13,797 Chain (1); Domain (1); Sequence caution (1) TISSUE SPECIFICITY: Abundant in tissues rich in highly ciliated cells, such as testis, trachea and olfactory epithelium. {ECO:0000269|PubMed:17971504}. +P54279 PMS2_MOUSE Mismatch repair endonuclease PMS2 (EC 3.1.-.-) (DNA mismatch repair protein PMS2) (PMS1 protein homolog 2) 859 95,225 Chain (1) FUNCTION: Component of the post-replicative DNA mismatch repair system (MMR). Heterodimerizes with MLH1 to form MutL alpha. DNA repair is initiated by MutS alpha (MSH2-MSH6) or MutS beta (MSH2-MSH3) binding to a dsDNA mismatch, then MutL alpha is recruited to the heteroduplex. Assembly of the MutL-MutS-heteroduplex ternary complex in presence of RFC and PCNA is sufficient to activate endonuclease activity of PMS2. It introduces single-strand breaks near the mismatch and thus generates new entry points for the exonuclease EXO1 to degrade the strand containing the mismatch. DNA methylation would prevent cleavage and therefore assure that only the newly mutated DNA strand is going to be corrected. MutL alpha (MLH1-PMS2) interacts physically with the clamp loader subunits of DNA polymerase III, suggesting that it may play a role to recruit the DNA polymerase III to the site of the MMR. Also implicated in DNA damage signaling, a process which induces cell cycle arrest and can lead to apoptosis in case of major DNA damages. {ECO:0000250|UniProtKB:P54278}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P54278}. SUBUNIT: Heterodimer of PMS2 and MLH1 (MutL alpha). Forms a ternary complex with MutS alpha (MSH2-MSH6) or MutS beta (MSH2-MSH3). Part of the BRCA1-associated genome surveillance complex (BASC), which contains BRCA1, MSH2, MSH6, MLH1, ATM, BLM, PMS2 and the RAD50-MRE11-NBS1 protein complex. This association could be a dynamic process changing throughout the cell cycle and within subnuclear domains. Interacts with MTMR15/FAN1. {ECO:0000250|UniProtKB:P54278}. +Q9CPV5 PMF1_MOUSE Polyamine-modulated factor 1 (PMF-1) 202 23,121 Alternative sequence (1); Chain (1); Coiled coil (1); Sequence conflict (4) FUNCTION: Part of the MIS12 complex which is required for normal chromosome alignment and segregation and for kinetochore formation during mitosis (By similarity). May act as a cotranscription partner of NFE2L2 involved in regulation of polyamine-induced transcription of SSAT. {ECO:0000250, ECO:0000269|PubMed:11583586}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Note=Associated with the kinetochore. {ECO:0000250}. SUBUNIT: Component of the MIS12 complex composed of MIS12, DSN1, NSL1 and PMF1. Interacts with COPS7A (By similarity). Interacts via its coiled-coil domain with the leucine-zipper domain of NFE2L2. The interaction with NFE2L2 is required for the transcriptional regulation of SSAT. {ECO:0000250, ECO:0000269|PubMed:11583586}. +Q8BHK0 PNMA2_MOUSE Paraneoplastic antigen Ma2 homolog 365 41,201 Chain (1); Compositional bias (1); Initiator methionine (1); Modified residue (1) SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the cerebrum, cerebellum and testis. {ECO:0000269|PubMed:19366867}. +Q9Z2M7 PMM2_MOUSE Phosphomannomutase 2 (PMM 2) (EC 5.4.2.8) 242 27,657 Active site (2); Binding site (6); Chain (1); Modified residue (1) Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2. FUNCTION: Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +P40935 PNMT_MOUSE Phenylethanolamine N-methyltransferase (PNMTase) (EC 2.1.1.28) (Noradrenaline N-methyltransferase) 295 32,544 Binding site (7); Chain (1); Region (3); Repeat (2) Catecholamine biosynthesis; (R)-adrenaline biosynthesis; (R)-adrenaline from (R)-noradrenaline: step 1/1. FUNCTION: Converts noradrenaline to adrenaline. TISSUE SPECIFICITY: Brain (pons and medulla oblongata), adrenal gland and retina. +Q8C1C8 PNMA1_MOUSE Paraneoplastic antigen Ma1 homolog 353 39,718 Chain (1); Compositional bias (1); Sequence conflict (1) SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. TISSUE SPECIFICITY: Predominantly expressed in testis. Very low levels in the brain, including in the piriform cortex, hippocampus and some subcortical nuclei. {ECO:0000269|PubMed:19366867}. +Q8K443 RGS13_MOUSE Regulator of G-protein signaling 13 (RGS13) 158 18,729 Chain (1); Domain (1) FUNCTION: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds to both G(i)-alpha and G(q)-alpha. +O54828 RGS9_MOUSE Regulator of G-protein signaling 9 (RGS9) 675 76,978 Alternative sequence (2); Beta strand (6); Chain (1); Domain (3); Helix (24); Sequence conflict (4); Turn (3) FUNCTION: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds to GNAT1. Involved in phototransduction; key element in the recovery phase of visual transduction. PTM: Retinal isoform 1 is light-dependent phosphorylated at 'Ser-475'. Phosphorylation is decreased by light exposition. Interaction with RGS9BP is decreased when isoform 1 is phosphorylated at 'Ser-475'. {ECO:0000269|PubMed:11292825}. SUBCELLULAR LOCATION: Isoform 1: Membrane; Peripheral membrane protein. Note=Isoform 1 is targeted to the membrane via its interaction with RGS9BP. SUBUNIT: Heterodimer with GNB5. Interacts with RGS7BP, leading to regulate the subcellular location of the heterodimer formed with GNB5 (PubMed:15632198, PubMed:15897264). Component of the RGS9-1-Gbeta5 complex composed of RGS9 (RGS9-1), Gbeta5 (GNB5) and RGS9BP (PubMed:12119397, PubMed:12499365, PubMed:14614075, PubMed:16908407). Interacts with PDE6G and GNAT1 (By similarity). {ECO:0000250|UniProtKB:O46469, ECO:0000305|PubMed:12119397, ECO:0000305|PubMed:12499365, ECO:0000305|PubMed:14614075, ECO:0000305|PubMed:15632198, ECO:0000305|PubMed:15897264, ECO:0000305|PubMed:16908407}. TISSUE SPECIFICITY: Isoform 1 is expressed in photoreceptor outer segments. Isoform 2 is expressed in brain striatum. +Q9QY81 PO210_MOUSE Nuclear pore membrane glycoprotein 210 (Nuclear pore protein gp210) (Nuclear envelope pore membrane protein POM 210) (POM210) (Nucleoporin Nup210) (Pore membrane protein of 210 kDa) 1886 204,101 Chain (1); Compositional bias (1); Domain (1); Glycosylation (12); Modified residue (6); Sequence conflict (17); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1809 1829 Helical. {ECO:0000255}. TOPO_DOM 27 1808 Lumenal. {ECO:0000305}.; TOPO_DOM 1830 1886 Cytoplasmic. {ECO:0000305}. FUNCTION: Nucleoporin essential for nuclear pore assembly and fusion, nuclear pore spacing, as well as structural integrity. PTM: N-glycosylated, but not all potential glycosylation sites may be used. Contains high-mannose type oligosaccharides (By similarity). {ECO:0000250}.; PTM: Phosphorylated at Ser-1880 in mitosis specifically; not phosphorylated in interphase. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nuclear pore complex {ECO:0000250}. Nucleus membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Forms dimers and possibly higher-order oligomers. {ECO:0000250}. +Q00196 PO2F2_MOUSE POU domain, class 2, transcription factor 2 (Lymphoid-restricted immunoglobulin octamer-binding protein NF-A2) (Octamer-binding protein 2) (Oct-2) (Octamer-binding transcription factor 2) (OTF-2) 463 49,439 Alternative sequence (7); Chain (1); Compositional bias (3); DNA binding (1); Domain (1); Erroneous initiation (1); Frameshift (1); Region (1); Sequence conflict (10) FUNCTION: Transcription factor that specifically binds to the octamer motif (5'-ATTTGCAT-3'). Regulates transcription in a number of tissues in addition to activating immunoglobulin gene expression. Modulates transcription transactivation by NR3C1, AR and PGR. Isoform OCT2.5 activates the U2 small nuclear RNA (snRNA) promoter. Isoforms OCT2.1, OCT2.2 and OCT2.3 activate octamer-containing promoters. Isoforms OCT2.4 and OCT2.5 repress some promoters and activate others. Isoform OCT2.7 is unable to bind to the octamer motif, but can still activate the beta-casein gene promoter at low levels. {ECO:0000269|PubMed:1281152, ECO:0000269|PubMed:17285328, ECO:0000269|PubMed:2011512, ECO:0000269|PubMed:7935477}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17285328}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-ProRule:PRU00530, ECO:0000269|PubMed:17285328}. Note=In alveolus epithelial cells of mammary glands, present in the nucleus and cytoplasm. In HC11 mammary epithelial cells, present in the nucleus and preinuclear regions. TISSUE SPECIFICITY: Highest in B-cells, but also present in brain (neuronal and glial cells), intestine, kidney, and testes. Isoform OCT2.1 is expressed at higher levels in B-cells than in neuronal cells. Isoform OCT2.2 is expressed in neuronal cell lines and brain, but not dorsal root ganglia. Isoform OCT2.3 is expressed at lower levels in neuronal cells than in B-cells. Isoform OCT2.4 is expressed in neuronal cell lines, and at lower levels in neuroblastoma and dorsal root ganglia. Isoform OCT2.5 is widely expressed in the developing nervous system but expression is confined to very specific regions in the adult brain, it is expressed at a lower level in B-cells. Isoform OCT2.6 is either absent in, or expressed at very low levels in neuronal cells and brain. Isoform OCT2.7 is expressed in all tissues tested: mammary gland, liver, spleen, lung, kidney intestine, uterus and ovary of a virgin mouse. Levels of isoform OCT2.7 are highest in spleen and lung. In mammary gland, expression is localized to the alveolus epithelial cells. {ECO:0000269|PubMed:1281152, ECO:0000269|PubMed:17285328}. +Q91X05 PODO_MOUSE Podocin 385 42,337 Chain (1); Lipidation (1); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 105 125 Helical. {ECO:0000255}. TOPO_DOM 1 104 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 126 385 Extracellular. {ECO:0000255}. FUNCTION: Plays a role in the regulation of glomerular permeability, acting probably as a linker between the plasma membrane and the cytoskeleton. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. SUBUNIT: Interacts with nephrin/NPHS1, KIRRL1 and CD2AP. Interacts with DDN. {ECO:0000269|PubMed:12424224, ECO:0000269|PubMed:17537921}. +Q8BHD1 POC1B_MOUSE POC1 centriolar protein homolog B (WD repeat-containing protein 51B) 476 53,504 Chain (1); Coiled coil (1); Repeat (7) FUNCTION: Plays an important role in centriole assembly and/or stability and ciliogenesis. Involved in early steps of centriole duplication, as well as in the later steps of centriole length control. Acts in concert with POC1A to ensure centriole integrity and proper mitotic spindle formation. Required for primary cilia formation, ciliary length and also cell proliferation. Required for retinal integrity. {ECO:0000250|UniProtKB:Q8TC44}. PTM: Phosphorylated in mitotic cells that may be mediated by CDK1. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:25044745}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:25044745}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q8TC44}. Note=Component of both mother and daughter centrioles. Localizes to the basal body and centriole adjacent to the connecting cilium of photoreceptors and in synapses of the outer plexiform layer. {ECO:0000269|PubMed:25044745}. SUBUNIT: Interacts with POC1A. Interacts with FAM161A. {ECO:0000250|UniProtKB:Q8TC44}. TISSUE SPECIFICITY: Expressed in the retina. {ECO:0000269|PubMed:25044745}. +P20263 PO5F1_MOUSE POU domain, class 5, transcription factor 1 (NF-A3) (Octamer-binding protein 3) (Oct-3) (Octamer-binding protein 4) (Oct-4) (Octamer-binding transcription factor 3) (OTF-3) 352 38,216 Beta strand (1); Binding site (2); Chain (1); Cross-link (1); DNA binding (1); Domain (1); Helix (8); Modified residue (5); Mutagenesis (17); Region (2); Sequence conflict (4); Turn (1) FUNCTION: Transcription factor that binds to the octamer motif (5'-ATTTGCAT-3') (PubMed:1972777, PubMed:1690859, PubMed:1967980, PubMed:17525163, PubMed:23376973). Forms a trimeric complex with SOX2 on DNA and controls the expression of a number of genes involved in embryonic development such as YES1, FGF4, UTF1 and ZFP206 (PubMed:17097055, PubMed:17496161, PubMed:19740739). Critical for early embryogenesis and for embryonic stem cell pluripotency (PubMed:1972777, PubMed:1690859, PubMed:17496161, PubMed:18662995, PubMed:19740739, PubMed:29153991, PubMed:23376973). {ECO:0000269|PubMed:1690859, ECO:0000269|PubMed:17097055, ECO:0000269|PubMed:17496161, ECO:0000269|PubMed:17525163, ECO:0000269|PubMed:18662995, ECO:0000269|PubMed:1967980, ECO:0000269|PubMed:1972777, ECO:0000269|PubMed:19740739, ECO:0000269|PubMed:23376973, ECO:0000269|PubMed:29153991}. PTM: Sumoylation enhances the protein stability, DNA binding and transactivation activity. Sumoylation is required for enhanced YES1 expression. {ECO:0000269|PubMed:17097055, ECO:0000269|PubMed:17496161, ECO:0000269|PubMed:17525163}.; PTM: Ubiquitinated; undergoes 'Lys-63'-linked polyubiquitination by WWP2 leading to proteasomal degradation. {ECO:0000269|PubMed:19997087, ECO:0000269|PubMed:23376973}.; PTM: ERK1/2-mediated phosphorylation at Ser-106 promotes nuclear exclusion and proteasomal degradation. Phosphorylation at Thr-228 and Ser-229 decrease DNA-binding and alters ability to activate transcription (By similarity). JNK1/2-mediated phosphorylation at Ser-347 promotes proteasomal degradation (PubMed:29153991). {ECO:0000250|UniProtKB:Q01860, ECO:0000269|PubMed:29153991}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q01860}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-ProRule:PRU00530, ECO:0000269|PubMed:17496161, ECO:0000269|PubMed:17525163, ECO:0000269|PubMed:29153991}. Note=Expressed in a diffuse and slightly punctuate pattern (By similarity). Colocalizes with MAPK8 and MAPK9 in the nucleus (PubMed:29153991). {ECO:0000250|UniProtKB:Q01860, ECO:0000269|PubMed:29153991}. SUBUNIT: Interacts with PKM. Interacts with WWP2 (By similarity). Interacts with UBE2I and ZSCAN10 (PubMed:17496161, PubMed:19740739). Interacts with PCGF1 (By similarity). Interacts with ESRRB; recruits ESRRB near the POU5F1-SOX2 element in the NANOG proximal promoter; the interaction is DNA independent (PubMed:18662995). Interacts with ZNF322 (PubMed:24550733). Interacts with MAPK8 and MAPK9; the interaction allows MAPK8 and MAPK9 to phosphorylate POU5F1 on Ser-347 (PubMed:29153991). Interacts (when phosphorylated on Ser-347) with FBXW8 (PubMed:29153991). Interacts with FBXW4 (PubMed:29153991). {ECO:0000250|UniProtKB:Q01860, ECO:0000269|PubMed:17496161, ECO:0000269|PubMed:18662995, ECO:0000269|PubMed:19740739, ECO:0000269|PubMed:24550733, ECO:0000269|PubMed:29153991}. DOMAIN: The POU-specific domain mediates interaction with PKM. {ECO:0000250|UniProtKB:Q01860}. TISSUE SPECIFICITY: Expressed the totipotent and pluripotent stem cells of the pregastrulation embryo. Also expressed in primordial germ cells and in the female germ line. Absent from adult tissues. {ECO:0000269|PubMed:1690859, ECO:0000269|PubMed:1972777}. +Q9DAC9 PO5F2_MOUSE POU domain, class 5, transcription factor 2 (Sperm 1 POU domain transcription factor) (SPRM-1) 329 36,411 Chain (1); DNA binding (1); Domain (1); Sequence conflict (1) FUNCTION: Transcription factor that binds preferentially to the octamer motif (5'-ATGTTAAT-3'). May exert a regulatory function in meiotic events that are required for terminal differentiation of male germ cell (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-ProRule:PRU00530}. TISSUE SPECIFICITY: In adult brain, expressed in the olfactory bulb, becoming specifically concentrated in the mitral cell layer. Also found in the pyramidal cell layer of the hippocampus, in the granule cell layer of the cerebellum and in the cortex. {ECO:0000269|PubMed:7908264}. +Q8VEK2 RHBD2_MOUSE Rhomboid domain-containing protein 2 (Rhomboid-like protein 7) 361 39,108 Alternative sequence (1); Chain (1); Mutagenesis (4); Sequence conflict (1); Transmembrane (5) TRANSMEM 19 39 Helical. {ECO:0000255}.; TRANSMEM 63 83 Helical. {ECO:0000255}.; TRANSMEM 100 120 Helical. {ECO:0000255}.; TRANSMEM 158 178 Helical. {ECO:0000255}.; TRANSMEM 182 202 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:23386608}; Multi-pass membrane protein {ECO:0000269|PubMed:23386608}. SUBUNIT: Might form homotrimers; these trimers are only formed in retina. {ECO:0000269|PubMed:23386608}. TISSUE SPECIFICITY: Widely expressed, including in retina and brain (at protein level), as well as in kidney, testis and ovary. Expressed in all layers of the retina, including inner segments of photoreceptor cells and ganglion cells (at protein level). {ECO:0000269|PubMed:23386608}. +Q8BUX5 RHBG_MOUSE Ammonium transporter Rh type B (Rhesus blood group family type B glycoprotein) (Rh family type B glycoprotein) (Rh type B glycoprotein) 455 49,543 Chain (1); Glycosylation (1); Region (1); Sequence conflict (2); Topological domain (13); Transmembrane (12) TRANSMEM 11 31 Helical. {ECO:0000255}.; TRANSMEM 59 79 Helical. {ECO:0000255}.; TRANSMEM 84 104 Helical. {ECO:0000255}.; TRANSMEM 122 142 Helical. {ECO:0000255}.; TRANSMEM 147 167 Helical. {ECO:0000255}.; TRANSMEM 176 198 Helical. {ECO:0000255}.; TRANSMEM 217 237 Helical. {ECO:0000255}.; TRANSMEM 249 269 Helical. {ECO:0000255}.; TRANSMEM 280 300 Helical. {ECO:0000255}.; TRANSMEM 302 322 Helical. {ECO:0000255}.; TRANSMEM 344 364 Helical. {ECO:0000255}.; TRANSMEM 391 411 Helical. {ECO:0000255}. TOPO_DOM 1 10 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 32 58 Extracellular. {ECO:0000255}.; TOPO_DOM 80 83 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 105 121 Extracellular. {ECO:0000255}.; TOPO_DOM 143 146 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 168 175 Extracellular. {ECO:0000255}.; TOPO_DOM 199 216 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 238 248 Extracellular. {ECO:0000255}.; TOPO_DOM 270 279 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 301 301 Extracellular. {ECO:0000255}.; TOPO_DOM 323 343 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 365 390 Extracellular. {ECO:0000255}.; TOPO_DOM 412 455 Cytoplasmic. {ECO:0000255}. FUNCTION: Functions as a specific ammonium transporter. {ECO:0000269|PubMed:15353405, ECO:0000269|PubMed:16131648}. PTM: N-glycosylated. {ECO:0000269|PubMed:11024028}. SUBCELLULAR LOCATION: Basolateral cell membrane; Multi-pass membrane protein. Cytoplasmic vesicle membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts (via C-terminus) with ANK2 and ANK3; required for targeting to the basolateral membrane. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in kidney by connecting segments and collecting tubules. Also expressed in liver by perivenous hepatocytes. Expressed in the forestomach and the fundus of the stomach. Expressed in duodenum, jejunum, ileum and colon at the level of villous (at protein level). Specifically expressed in kidney where it is restricted to the epithelial linings of the convoluted tubules and the loop of Henle. Also detected in ovary. Expressed by hepatocytes and dermal hair follicles and papillae. {ECO:0000269|PubMed:11024028, ECO:0000269|PubMed:12388412, ECO:0000269|PubMed:12730882, ECO:0000269|PubMed:15576624}. +Q8VC82 RHBL1_MOUSE Rhomboid-related protein 1 (RRP) (EC 3.4.21.105) (Rhomboid-like protein 1) 373 41,786 Active site (2); Chain (1); Transmembrane (7) TRANSMEM 131 151 Helical. {ECO:0000255}.; TRANSMEM 196 216 Helical. {ECO:0000255}.; TRANSMEM 219 239 Helical. {ECO:0000255}.; TRANSMEM 243 263 Helical. {ECO:0000255}.; TRANSMEM 275 294 Helical. {ECO:0000255}.; TRANSMEM 307 327 Helical. {ECO:0000255}.; TRANSMEM 340 360 Helical. {ECO:0000255}. FUNCTION: May be involved in regulated intramembrane proteolysis and the subsequent release of functional polypeptides from their membrane anchors. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +P52430 PON1_MOUSE Serum paraoxonase/arylesterase 1 (PON 1) (EC 3.1.1.2) (EC 3.1.1.81) (EC 3.1.8.1) (Aromatic esterase 1) (A-esterase 1) (Serum aryldialkylphosphatase 1) 355 39,565 Active site (1); Chain (1); Disulfide bond (1); Glycosylation (3); Metal binding (8); Sequence conflict (2); Signal peptide (1) FUNCTION: Hydrolyzes the toxic metabolites of a variety of organophosphorus insecticides. Capable of hydrolyzing a broad spectrum of organophosphate substrates and lactones, and a number of aromatic carboxylic acid esters. Mediates an enzymatic protection of low density lipoproteins against oxidative modification. {ECO:0000250|UniProtKB:P27169}. PTM: The signal sequence is not cleaved. {ECO:0000250|UniProtKB:P27169}. SUBCELLULAR LOCATION: Secreted, extracellular space. SUBUNIT: Homodimer. Interacts with CLU. {ECO:0000250|UniProtKB:P27169}. TISSUE SPECIFICITY: Plasma, liver, kidney, heart, brain, small intestine and lung. In the plasma, associated with HDL. +Q8BHC7 RHBL4_MOUSE Rhomboid-related protein 4 (RRP4) (EC 3.4.21.105) (Rhomboid domain-containing protein 1) (mRHBDD1) (Rhomboid-like protein 4) 315 35,776 Active site (2); Chain (1); Mutagenesis (3); Region (2); Sequence conflict (5); Topological domain (5); Transmembrane (4) TRANSMEM 22 42 Helical. {ECO:0000255}.; TRANSMEM 104 124 Helical. {ECO:0000255}.; TRANSMEM 146 166 Helical. {ECO:0000255}.; TRANSMEM 181 201 Helical. {ECO:0000255}. TOPO_DOM 1 21 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 43 103 Lumenal. {ECO:0000255}.; TOPO_DOM 125 145 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 167 180 Lumenal. {ECO:0000255}.; TOPO_DOM 202 315 Cytoplasmic. {ECO:0000255}. FUNCTION: Intramembrane-cleaving serine protease that cleaves single transmembrane or multi-pass membrane proteins in the hydrophobic plane of the membrane, luminal loops and juxtamembrane regions. Involved in regulated intramembrane proteolysis and the subsequent release of functional polypeptides from their membrane anchors. Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded membrane proteins. Required for the degradation process of some specific misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Functions in BIK, MPZ, PKD1, PTCRA, RHO, STEAP3 and TRAC processing. Involved in the regulation of exosomal secretion; inhibits the TSAP6-mediated secretion pathway. Involved in the regulation of apoptosis; modulates BIK-mediated apoptotic activity. Also plays a role in the regulation of spermatogenesis; inhibits apoptotic activity in spermatogonia. {ECO:0000269|PubMed:19358743, ECO:0000269|PubMed:22795130}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Mitochondrion {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:22795130}; Multi-pass membrane protein {ECO:0000269|PubMed:22795130}. SUBUNIT: Interacts with BIK and STEAP3 (By similarity). Interacts (via C-terminal domain) with VCP/P97. Interacts with ubiquitin and ubiquitinated proteins. {ECO:0000250, ECO:0000269|PubMed:22795130}. TISSUE SPECIFICITY: Expressed in testis (at protein level). Expressed in intestine, lung, brain, kidney, epididymis, stomach, muscle, spleen, liver, heart and testis. {ECO:0000269|PubMed:19358743}. +Q91V93 RHBT2_MOUSE Rho-related BTB domain-containing protein 2 (Deleted in breast cancer 2 gene protein homolog) 728 82,650 Chain (1); Domain (2); Nucleotide binding (3); Region (1); Sequence conflict (14) SUBUNIT: Interacts with HSP90AA1 and HSP90AB1. Interacts with CUL3. {ECO:0000250|UniProtKB:Q9BYZ6}. TISSUE SPECIFICITY: Expressed in most tissues, with highest expression in brain. {ECO:0000269|PubMed:12426103}. +Q9DCH2 POP7_MOUSE Ribonuclease P protein subunit p20 (RNaseP protein p20) (EC 3.1.26.5) 140 15,777 Chain (1) FUNCTION: Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP complex, which cleaves pre-rRNA sequences (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasmic granule {ECO:0000250}. Note=Under stress conditions colocalizes with SMN1 in punctuated cytoplasmic granules. {ECO:0000250}. SUBUNIT: Component of nuclear RNase P and RNase MRP complexes. RNase P consists of an RNA moiety and at least 8 protein subunits; POP1, RPP14, RPP20/POP7, RPP25, RPP29/POP4, RPP30, RPP38 and RPP40. RNase MRP consists of an RNA moiety and at least 9 protein subunits; POP1, RPP14, RPP20/POP7, RPP25, RPP29/POP4, RPP30, RPP38, RPP40, POP5 and RPP21. Interacts with RPP25 and SMN1. RPP20/POP7 is probably a dimer (By similarity). {ECO:0000250}. +Q9WUP4 PORED_MOUSE Polyprenol reductase (EC 1.3.1.94) (3-oxo-5-alpha-steroid 4-dehydrogenase 3) (EC 1.3.1.22) (Steroid 5-alpha-reductase 2-like) (Steroid 5-alpha-reductase 3) (S5AR 3) (SR type 3) 330 37,936 Alternative sequence (1); Chain (1); Sequence conflict (4); Topological domain (7); Transmembrane (6) TRANSMEM 17 37 Helical. {ECO:0000255}.; TRANSMEM 81 101 Helical. {ECO:0000255}.; TRANSMEM 133 153 Helical. {ECO:0000255}.; TRANSMEM 170 190 Helical. {ECO:0000255}.; TRANSMEM 207 227 Helical. {ECO:0000255}.; TRANSMEM 278 298 Helical. {ECO:0000255}. TOPO_DOM 1 16 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 38 80 Lumenal. {ECO:0000255}.; TOPO_DOM 102 132 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 154 169 Lumenal. {ECO:0000255}.; TOPO_DOM 191 206 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 228 277 Lumenal. {ECO:0000255}.; TOPO_DOM 299 330 Cytoplasmic. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Plays a key role in early steps of protein N-linked glycosylation by being required for the conversion of polyprenol into dolichol. Dolichols are required for the synthesis of dolichol-linked monosaccharides and the oligosaccharide precursor used for N-glycosylation. Acts as a polyprenol reductase that promotes the reduction of the alpha-isoprene unit of polyprenols into dolichols in a NADP-dependent mechanism. Also able to convert testosterone (T) into 5-alpha-dihydrotestosterone (DHT). {ECO:0000269|PubMed:20637498}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q91Z22 PORIM_MOUSE Porimin (Transmembrane protein 123) 195 20,178 Chain (1); Compositional bias (1); Glycosylation (6); Modified residue (1); Sequence conflict (6); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 153 173 Helical. {ECO:0000255}. TOPO_DOM 24 152 Extracellular. {ECO:0000255}.; TOPO_DOM 174 195 Cytoplasmic. {ECO:0000255}. FUNCTION: Implicated in oncotic cell death, characterized by cell swelling, organelle swelling, vacuolization and increased membrane permeability. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +P63032 RHES_MOUSE GTP-binding protein Rhes (Ras homolog enriched in striatum) 266 30,197 Chain (1); Lipidation (1); Modified residue (1); Motif (1); Nucleotide binding (3); Propeptide (1); Region (1); Sequence caution (1) FUNCTION: GTPase signaling protein that binds to and hydrolyzes GTP. Regulates signaling pathways involving G-proteins-coupled receptor and heterotrimeric proteins such as GNB1, GNB2 and GNB3. May be involved in selected striatal competencies, mainly locomotor activity and motor coordination. {ECO:0000269|PubMed:15199135, ECO:0000269|PubMed:18035555}. PTM: Farnesylated. Farnesylation is required for membrane targeting (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. SUBUNIT: Monomer (Potential). Interacts with PIK3CA and UBE2I. Interacts with GNB1, GNB2 and GNB3 (By similarity). {ECO:0000250, ECO:0000305}. TISSUE SPECIFICITY: Highly expressed in brain; prominently in the striatum and weakly in kidney, thyroid, lung, heart and testis. Not expressed in liver. Expressed in pancreatic cell lines and in a embryonic stem cell line. {ECO:0000269|PubMed:15199135, ECO:0000269|PubMed:16945334}. +Q6Y5D8 RHG10_MOUSE Rho GTPase-activating protein 10 (PH and SH3 domain-containing rhoGAP protein) (PS-GAP) (PSGAP) (Rho-type GTPase-activating protein 10) 786 89,366 Alternative sequence (3); Chain (1); Domain (4); Mutagenesis (1); Sequence conflict (23) FUNCTION: GTPase activator for the small GTPases RhoA and Cdc42 by converting them to an inactive GDP-bound state. Essential for PTKB2 regulation of cytoskeletal organization via Rho family GTPases. Inhibits PAK2 proteolytic fragment PAK-2p34 kinase activity and changes its localization from the nucleus to the perinuclear region. Stabilizes PAK-2p34 thereby increasing stimulation of cell death. {ECO:0000269|PubMed:11238453, ECO:0000269|PubMed:15471851}. PTM: Phosphorylated on tyrosine residues, probably involving PTK2B/PYK2. SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region. Cell membrane. Note=Association to cell membrane is dependent on PH domain. SUBUNIT: Interacts with PKN3 (By similarity). Interacts with caspase-activated PAK2 proteolytic fragment PAK-2p34; the interaction does not affect ARHGAP10 GTPase activation activity towards RHOA and CDC42. Interacts via its SH3 domain with PTK2/FAK1. Interacts with PTK2B/PYK2; the interaction negatively regulates ARHGAP10 GTPase-activating activity. {ECO:0000250, ECO:0000269|PubMed:11238453, ECO:0000269|PubMed:15471851}. TISSUE SPECIFICITY: High levels of expression in brain, testes, liver, heart and kidney. {ECO:0000269|PubMed:15471851}. +Q8BRH3 RHG19_MOUSE Rho GTPase-activating protein 19 (Rho-type GTPase-activating protein 19) 494 55,734 Alternative sequence (1); Chain (1); Domain (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (7); Sequence conflict (1) FUNCTION: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. {ECO:0000250}. +Q6DFV3 RHG21_MOUSE Rho GTPase-activating protein 21 (Rho GTPase-activating protein 10) (Rho-type GTPase-activating protein 21) 1944 215,743 Chain (1); Cross-link (1); Domain (3); Erroneous gene model prediction (3); Modified residue (26); Region (2); Sequence conflict (3) FUNCTION: Functions as a GTPase-activating protein (GAP) for RHOA and CDC42. Downstream partner of ARF1 which may control Golgi apparatus structure and function. Also required for CTNNA1 recruitment to adherens junctions (By similarity). {ECO:0000250}. PTM: Sumoylated with SUMO2 and SUMO3 in proliferating lymphocytes. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell junction {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Localization to the Golgi is dependent on interaction with GTP-bound ARF1. {ECO:0000250}. SUBUNIT: Interacts with CTNNA1 (By similarity). Interacts with GTP-bound ARF1 and probably ARF6. {ECO:0000250, ECO:0000269|PubMed:17347647}. +Q80YF9 RHG33_MOUSE Rho GTPase-activating protein 33 (Rho-type GTPase-activating protein 33) (Sorting nexin-26) (Tc10/CDC42 GTPase-activating protein) 1305 139,801 Chain (1); Compositional bias (6); Domain (3); Erroneous initiation (1); Modified residue (6); Sequence conflict (1) FUNCTION: May be involved in several stages of intracellular trafficking (By similarity). Could play an important role in the regulation of glucose transport by insulin. May act as a downstream effector of RHOQ/TC10 in the regulation of insulin-stimulated glucose transport. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12773384}. Note=Translocates to the plasma membrane in response to insulin in adipocytes. SUBUNIT: Specifically interacts with CDC42 and RHOQ/TC10 through its Rho-GAP domain. Interacts with NEK6 (By similarity). {ECO:0000250}. DOMAIN: The N-terminal PX domain interacts specifically with phosphatidylinositol 4,5-bisphosphate. TISSUE SPECIFICITY: Highly expressed in brain and testis. Also expressed in white adipose tissue (WAT) and muscle at a low level. {ECO:0000269|PubMed:12773384}. +B1AUC7 RHG36_MOUSE Rho GTPase-activating protein 36 590 66,600 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (1); Erroneous gene model prediction (2); Sequence conflict (4) FUNCTION: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. {ECO:0000250}. +E9Q6X9 RHG40_MOUSE Rho GTPase-activating protein 40 (Rho-type GTPase-activating protein 40) 672 74,333 Chain (1); Domain (1); Erroneous initiation (1) FUNCTION: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. {ECO:0000250}. +Q5SSM3 RHG44_MOUSE Rho GTPase-activating protein 44 (Rho-type GTPase-activating protein RICH2) (RhoGAP interacting with CIP4 homologs protein 2) (RICH-2) 814 88,994 Alternative sequence (5); Chain (1); Compositional bias (1); Domain (2); Erroneous gene model prediction (1); Frameshift (2); Modified residue (2); Motif (1); Mutagenesis (1); Region (1) FUNCTION: GTPase-activating protein (GAP) that stimulates the GTPase activity of Rho-type GTPases. Thereby, controls Rho-type GTPases cycling between their active GTP-bound and inactive GDP-bound states. May act as a GAP for CDC42 and RAC1. Endosomal recycling protein which, in association with SHANK3, is involved in synaptic plasticity. Promotes GRIA1 exocytosis from recycling endosomes and spine morphological changes associated to long-term potentiation. {ECO:0000269|PubMed:23739967}. SUBCELLULAR LOCATION: Cell projection, dendritic spine {ECO:0000269|PubMed:23739967}. Recycling endosome {ECO:0000269|PubMed:23739967}. Cell junction, synapse {ECO:0000250}. Note=In CA1 hippocampal synapses, detected at both presynaptic and postsynaptic sites. {ECO:0000250}. SUBUNIT: Interacts with BST2 (via cytoplasmic domain).Interacts (probably via PDZ-binding motif) with SHANK3 (via PDZ domain); the interaction takes place in dendritic spines and promotes GRIA1 exocytosis. {ECO:0000269|PubMed:23739967}. DOMAIN: Rho-GAP domain is required to promote GRIA1 exocytosis from recycling endosomes. Rho-GAP and BAR domains are necessary for the control of long-term potentiation in hippocampal neurons (PubMed:23739967). {ECO:0000269|PubMed:23739967}. TISSUE SPECIFICITY: Expressed in hippocampal neurons (at protein level). {ECO:0000269|PubMed:23739967}. +Q923M0 PP16A_MOUSE Protein phosphatase 1 regulatory subunit 16A (Myosin phosphatase targeting subunit 3) 524 57,530 Chain (1); Coiled coil (1); Lipidation (2); Modified residue (2); Propeptide (1); Repeat (5) FUNCTION: Inhibits protein phosphatase 1 activity toward phosphorylase, myosin light chain and myosin substrates. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. SUBUNIT: Binds PP1. TISSUE SPECIFICITY: Highly expressed in testis, followed by liver, heart, brain and lung. +Q8VHQ3 PP16B_MOUSE Protein phosphatase 1 regulatory inhibitor subunit 16B (CAAX box protein TIMAP) (TGF-beta-inhibited membrane-associated protein) 568 63,571 Chain (1); Coiled coil (1); Lipidation (2); Modified residue (6); Propeptide (1); Repeat (5) FUNCTION: Regulator of protein phosphatase 1 (PP1) that acts as a positive regulator of pulmonary endothelial cell (EC) barrier function. Protects the endothelial barrier from lipopolysaccharide (LPS)-induced vascular leakage (PubMed:21907835). Involved in the regulation of the PI3K/AKT signaling pathway (By similarity). Involved in the regulation of angiogenesis and endothelial cell proliferation through the control of ECE1 dephosphorylation, trafficking and activity (By similarity). Involved in the regulation of endothelial cell filopodia extension (By similarity). May be a downstream target for TGF-beta1 signaling cascade in endothelial cells (By similarity). Involved in PKA-mediated moesin dephosphorylation which is important in EC barrier protection against thrombin stimulation. Promotes the interaction of PPP1CA with RPSA/LAMR1 and in turn facilitates the dephosphorylation of RPSA/LAMR1 (By similarity). Involved in the dephosphorylation of EEF1A1 (By similarity). {ECO:0000250|UniProtKB:Q95N27, ECO:0000250|UniProtKB:Q96T49, ECO:0000269|PubMed:21907835}. PTM: Phosphorylated by PKA and, after PKA priming, by GSK3B. Phosphorylation by GSK3B reduces its association with PP1C and enhances PP1C activity. Dephosphorylation by its associated PP1C results in enhanced association with PP1C, but reduced PP1C activity (By similarity). {ECO:0000250|UniProtKB:Q95N27}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q96T49}. Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Nucleus {ECO:0000250|UniProtKB:Q96T49}. Cell projection {ECO:0000250|UniProtKB:Q96T49}. Note=Colocalizes with RPSA/LAMR1 in the cell membrane (By similarity). Localizes to the perinuclear region (By similarity). Colocalizes with PTEN at the tip of EC projections (By similarity). {ECO:0000250|UniProtKB:Q95N27, ECO:0000250|UniProtKB:Q96T49}. SUBUNIT: Interacts with PPP1CA, PPP1CB and MSN. Interacts (via its fourth ankyrin repeat) with the mature dimeric form of RPSA/LAMR1 (By similarity). Interacts with EEF1A1 (By similarity). Interacts with PTEN (By similarity). Interacts with ECE1 (By similarity). {ECO:0000250|UniProtKB:Q95N27, ECO:0000250|UniProtKB:Q96T49}. +D3YTS9 PPAT_MOUSE Testicular acid phosphatase (EC 3.1.3.2) (Acid phosphatase 4) 425 46,405 Active site (2); Chain (1); Disulfide bond (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 393 413 Helical. {ECO:0000255}. TOPO_DOM 28 392 Extracellular. {ECO:0000305}.; TOPO_DOM 414 425 Cytoplasmic. {ECO:0000305}. FUNCTION: May dephosphorylate receptor tyrosine-protein kinase ERBB4 and inhibits its ligand-induced proteolytic cleavage. May play a role in odontogenesis. {ECO:0000250|UniProtKB:Q9BZG2}. PTM: Glycosylated. {ECO:0000250|UniProtKB:Q9BZG2}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9BZG2}. +P24822 PPBI_MOUSE Intestinal-type alkaline phosphatase (IAP) (Intestinal alkaline phosphatase) (EC 3.1.3.1) (Alkaline phosphatase 3) 559 60,285 Active site (1); Chain (1); Compositional bias (2); Disulfide bond (2); Glycosylation (3); Lipidation (1); Metal binding (10); Propeptide (1); Signal peptide (1) SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}. SUBUNIT: Homodimer. TISSUE SPECIFICITY: Intestine and thymus. +Q9EPX2 PPN_MOUSE Papilin 1280 138,904 Chain (1); Disulfide bond (12); Domain (10); Sequence conflict (9); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q3TDD9 PPR21_MOUSE Protein phosphatase 1 regulatory subunit 21 (Coiled-coil domain-containing protein 128) (KLRAQ motif-containing protein 1) 780 88,338 Alternative sequence (2); Chain (1); Coiled coil (3); Modified residue (1); Sequence caution (1); Sequence conflict (9) SUBUNIT: Interacts with PPP1CA. {ECO:0000250}. +Q9D119 PPR27_MOUSE Protein phosphatase 1 regulatory subunit 27 (Dysferlin-interacting protein 1) 154 17,436 Chain (1); Repeat (2) FUNCTION: Inhibits phosphatase activity of protein phosphatase 1 (PP1) complexes. {ECO:0000250}. SUBUNIT: Interacts with DYSF and PPP1CA. {ECO:0000250}. +Q8BQ30 PPR18_MOUSE Phostensin (Protein phosphatase 1 F-actin cytoskeleton-targeting subunit) (Protein phosphatase 1 regulatory subunit 18) 594 65,630 Alternative sequence (1); Chain (1); Compositional bias (1); Erroneous initiation (1); Modified residue (9); Sequence conflict (1) FUNCTION: May target protein phosphatase 1 to F-actin cytoskeleton. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. SUBUNIT: Interacts with Protein phosphatase 1 (PP1). {ECO:0000250}. +Q8BKK4 PPR1C_MOUSE Protein phosphatase 1 regulatory subunit 1C 108 12,303 Alternative sequence (2); Chain (1); Sequence conflict (1) FUNCTION: May increase cell susceptibility to TNF-induced apoptosis. {ECO:0000250|UniProtKB:Q8WVI7}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +D3Z0R2 PPR36_MOUSE Protein phosphatase 1 regulatory subunit 36 411 47,354 Chain (1) FUNCTION: Inhibits phosphatase activity of protein phosphatase 1 (PP1) complexes. {ECO:0000250}. SUBUNIT: Interacts with PPP1CA. {ECO:0000250}. +Q8BKR5 PPR37_MOUSE Protein phosphatase 1 regulatory subunit 37 (Leucine-rich repeat-containing protein 68) 712 77,574 Chain (1); Compositional bias (2); Modified residue (3); Repeat (5) FUNCTION: Inhibits phosphatase activity of protein phosphatase 1 (PP1) complexes. {ECO:0000250}. SUBUNIT: Interacts with PPP1CA. {ECO:0000250}. +Q8C767 PPR3B_MOUSE Protein phosphatase 1 regulatory subunit 3B (Hepatic glycogen-targeting protein phosphatase 1 regulatory subunit GL) (Protein phosphatase 1 regulatory subunit 4) (PP1 subunit R4) (Protein phosphatase 1 subunit GL) (PTG) 284 32,433 Chain (1); Domain (1); Erroneous initiation (1); Modified residue (1); Motif (1) FUNCTION: Acts as a glycogen-targeting subunit for phosphatase PP1. Facilitates interaction of the PP1 with enzymes of the glycogen metabolism and regulates its activity. Suppresses the rate at which PP1 dephosphorylates (inactivates) glycogen phosphorylase and enhances the rate at which it activates glycogen synthase and therefore limits glycogen breakdown. Its activity is inhibited by PYGL, resulting in inhibition of the glycogen synthase and glycogen phosphorylase phosphatase activities of PP1. Dramatically increases basal and insulin-stimulated glycogen synthesis upon overexpression in hepatocytes (By similarity). {ECO:0000250}. SUBUNIT: Interacts with glycogen, PPP1CC catalytic subunit of PP1 and PYGL. Associates with glycogen particles. Forms complexes with debranching enzyme, glycogen phosphorylase, glycogen synthase and phosphorylase kinase which is necessary for its regulation of PP1 activity (By similarity). {ECO:0000250}. DOMAIN: The N-terminal region is required for binding to PP1, the central region is required for binding to glycogen and the C-terminal region is required for binding to PYGL. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in liver (at protein level). Expressed predominantly in liver. Expressed moderately in heart. Expressed weakly in prostate, stomach, thyroid, lung, kidney, spleen and skeletal muscle. {ECO:0000269|PubMed:11872655, ECO:0000269|PubMed:16949035}. +Q7TMB3 PPR3C_MOUSE Protein phosphatase 1 regulatory subunit 3C (Protein phosphatase 1 regulatory subunit 5) (PP1 subunit R5) (Protein targeting to glycogen) (PTG) 317 36,460 Chain (1); Domain (1); Erroneous initiation (1); Motif (1); Mutagenesis (4); Region (1); Sequence conflict (1) FUNCTION: Acts as a glycogen-targeting subunit for PP1 and regulates its activity. Activates glycogen synthase, reduces glycogen phosphorylase activity and limits glycogen breakdown. Dramatically increases basal and insulin-stimulated glycogen synthesis upon overexpression in a variety of cell types. {ECO:0000269|PubMed:10683377, ECO:0000269|PubMed:10862764, ECO:0000269|PubMed:10998419, ECO:0000269|PubMed:12727934, ECO:0000269|PubMed:12805359, ECO:0000269|PubMed:15322104, ECO:0000269|PubMed:16354703, ECO:0000269|PubMed:9045612, ECO:0000269|PubMed:9242697, ECO:0000269|PubMed:9756875}. PTM: Ubiquitinated by NHLRC1/malin in a EPM2A/laforin-dependent manner. {ECO:0000250}. SUBUNIT: Interacts with PPP1CC catalytic subunit of PP1 and associates with glycogen. Forms complexes with glycogen phosphorylase, glycogen synthase and phosphorylase kinase which is necessary for its regulation of PP1 activity. Also interacts with EPM2A/laforin. {ECO:0000250|UniProtKB:Q9UQK1, ECO:0000269|PubMed:9045612}. DOMAIN: The N-terminal region is required for binding to PP1, the central region is required for binding to glycogen and the C-terminal region is required for binding to glycogen phosphorylase, glycogen synthase and phosphorylase kinase. {ECO:0000269|PubMed:10938087}. +Q9JIG4 PPR3F_MOUSE Protein phosphatase 1 regulatory subunit 3F (R3F) 799 84,120 Alternative sequence (1); Chain (1); Domain (1); Erroneous initiation (3); Modified residue (4); Motif (1); Mutagenesis (1); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 773 793 Helical. {ECO:0000255}. TOPO_DOM 1 772 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 794 799 Extracellular. {ECO:0000255}. FUNCTION: Glycogen-targeting subunit for protein phosphatase 1 (PP1). {ECO:0000269|PubMed:21668450}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:21668450}; Single-pass membrane protein {ECO:0000269|PubMed:21668450}. TISSUE SPECIFICITY: Highly expressed in brain (at protein level). {ECO:0000269|PubMed:21668450}. +Q8R1Z4 PPR42_MOUSE Protein phosphatase 1 regulatory subunit 42 (Leucine-rich repeat-containing protein 67) (Testis leucine-rich repeat protein) (TLRR) 357 41,151 Alternative sequence (3); Chain (1); Domain (1); Repeat (7) FUNCTION: Regulates phosphatase activity of protein phosphatase 1 (PP1) complexes in the testis. {ECO:0000269|PubMed:21738792}. PTM: Phosphorylated; during the first round of spermatogenesis with a marginal increase at 21 days after birth. {ECO:0000269|PubMed:21738792}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Colocalizes with alpha tubulin to the manchette of developing spermatids. Detected to nuclear rim in pachytene spermatocytes. Detected at nuclear surface, opposite the acrosome in elongating spermatids. Detected at the microtubule- organizing center (MTOC). Localized to the centrosomal region of late-stage spermatids. SUBUNIT: Interacts with PPP1CC isoform gamma-2; the interaction is direct. Interacts with actin, dynein, KIF5B, KIFC1 and tubulin. Associates with microtubules. {ECO:0000269|PubMed:18237440, ECO:0000269|PubMed:19886865, ECO:0000269|PubMed:21738792}. TISSUE SPECIFICITY: Testis-specific. Expressed in spermatids (at protein level). Testis-specific. {ECO:0000269|PubMed:18237440}. +O35448 PPT2_MOUSE Lysosomal thioesterase PPT2 (PPT-2) (EC 3.1.2.-) 302 34,366 Active site (3); Chain (1); Disulfide bond (3); Glycosylation (5); Signal peptide (1) FUNCTION: Removes thioester-linked fatty acyl groups from various substrates including S-palmitoyl-CoA. Has the highest S-thioesterase activity for the acyl groups palmitic and myristic acid followed by other short- and long-chain acyl substrates. However, because of structural constraints, is unable to remove palmitate from peptides or proteins (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:14528005}. TISSUE SPECIFICITY: Expressed throughout the brain, primarily in neurons, and at lower levels in glial cells. {ECO:0000269|PubMed:11717424, ECO:0000269|PubMed:14528005}. +O35257 PR6A1_MOUSE Prolactin-6A1 (Placental prolactin-like protein B) (PLP-B) (PRL-like protein B) 230 26,621 Chain (1); Disulfide bond (2); Glycosylation (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000250}. TISSUE SPECIFICITY: Expressed in both placenta and decidual tissues. Detected first in deciduals cells early in gestation and in trophoblasts later in pregnancy. {ECO:0000269|PubMed:9389542, ECO:0000269|PubMed:9472921}. +O54831 PR7A2_MOUSE Prolactin-7A2 (Placental prolactin-like protein F) (PLP-F) (PRL-like protein F) 253 28,921 Chain (1); Compositional bias (1); Disulfide bond (2); Glycosylation (3); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000250}. TISSUE SPECIFICITY: Expression restricted to the placental tissue. Expressed only in the spongiotrophoblasts. {ECO:0000269|PubMed:9389541}. +Q8JZM2 PR15L_MOUSE Proline-rich protein 15-like protein (Protein ATAD4) 100 11,359 Chain (1); Erroneous termination (1) +Q99MW3 PRAL1_MOUSE Preferentially expressed antigen in melanoma-like protein 1 (Prame-like 1) 458 52,402 Chain (1); Repeat (9) FUNCTION: May play a role in acrosome development and also in sperm maturation and motility. {ECO:0000303|PubMed:23565261}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23565261}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:23565261}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:23565261}. Note=Located in the cytoplasm of spermatocytes and in the acrosomal vesicle region of round, elongating and elongated spermatids. Detected in the main piece of the flagellum in testicular spermatozoa. Detected also in the connecting piece, middle piece and cytoplasmic droplets of epididymal spermatozoa. {ECO:0000269|PubMed:23565261}. TISSUE SPECIFICITY: Specifically expressed in testis (at protein level). {ECO:0000269|PubMed:23565261}. +Q6BCL1 PRAM_MOUSE PML-RARA-regulated adapter molecule 1 (PRAM-1) 675 75,508 Chain (1); Compositional bias (1); Domain (1); Modified residue (1); Sequence conflict (1) FUNCTION: May be involved in integrin signaling in neutrophils. Binds to PtdIns(4)P. {ECO:0000269|PubMed:15572693}. PTM: May be phosphorylated on tyrosines. {ECO:0000250}. SUBUNIT: Interacts with SKAP2, LCP2 and DBNL. May interact with LYN (By similarity). Interacts with NEK6 (By similarity). {ECO:0000250}. DOMAIN: The SH3 domain binds to PtdIns(4)P. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in bone marrow and mature neutrophils. Weakly expressed in macrophages and mast cells. {ECO:0000269|PubMed:15572693}. +Q61171 PRDX2_MOUSE Peroxiredoxin-2 (EC 1.11.1.15) (Thiol-specific antioxidant protein) (TSA) (Thioredoxin peroxidase 1) (Thioredoxin-dependent peroxide reductase 1) 198 21,779 Active site (1); Chain (1); Disulfide bond (2); Domain (1); Initiator methionine (1); Modified residue (4); Sequence conflict (9) FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2). {ECO:0000250|UniProtKB:P32119}. PTM: The enzyme can be inactivated by further oxidation of the cysteine sulfenic acid (C(P)-SOH) to sulphinic acid (C(P)-SO2H) instead of its condensation to a disulfide bond. It can be reactivated by forming a transient disulfide bond with sulfiredoxin SRXN1, which reduces the cysteine sulfinic acid in an ATP- and Mg-dependent manner. {ECO:0000250|UniProtKB:P32119, ECO:0000250|UniProtKB:Q06830}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P32119}. SUBUNIT: Homodimer; disulfide-linked, upon oxidation. 5 homodimers assemble to form a ring-like decamer (By similarity). Interacts with TIPIN (PubMed:17141802). {ECO:0000250|UniProtKB:P32119, ECO:0000269|PubMed:17141802}. TISSUE SPECIFICITY: Widely expressed with highest levels in bone marrow. High levels also found in heart, brain, kidney and skeletal muscle. Lower levels in liver, lung and thymus. +Q99K43 PRC1_MOUSE Protein regulator of cytokinesis 1 603 70,290 Binding site (2); Chain (1); Coiled coil (5); Modified residue (5); Region (3); Sequence caution (1); Sequence conflict (1) FUNCTION: Key regulator of cytokinesis that cross-links antiparrallel microtubules at an average distance of 35 nM. Essential for controlling the spatiotemporal formation of the midzone and successful cytokinesis. Required for KIF14 localization to the central spindle and midbody. Required to recruit PLK1 to the spindle. Stimulates PLK1 phosphorylation of RACGAP1 to allow recruitment of ECT2 to the central spindle. Acts as an oncogene for promoting bladder cancer cells proliferation, apoptosis inhibition and carcinogenic progression. {ECO:0000250|UniProtKB:O43663}. PTM: Phosphorylation by CDK1 in early mitosis holds PRC1 in an inactive monomeric state, during the metaphase to anaphase transition, PRC1 is dephosphorylated, promoting interaction with KIF4A, which then translocates PRC1 along mitotic spindles to the plus ends of antiparallel interdigitating microtubules. Dephosphorylation also promotes MT-bundling activity by allowing dimerization. Phosphorylation by CDK1 prevents PLK1-binding: upon degradation of CDK1 at anaphase and dephosphorylation, it is then phosphorylated by PLK1, leading to cytokinesis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O43663}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. Midbody {ECO:0000250|UniProtKB:O43663}. Note=Predominantly localized to the nucleus of interphase cells. During mitosis becomes associated with the mitotic spindle poles, and localizes with the cell midbody during cytokinesis. Colocalized with KIF20B in the nucleus of bladder carcinoma cells at the interphase. Colocalized with KIF20B in bladder carcinoma cells at prophase, metaphase, early anaphase, at the midzone in late anaphase and at the contractile ring in telophase. {ECO:0000250|UniProtKB:O43663}. SUBUNIT: Homodimer. Interacts with the C-terminal Rho-GAP domain and the basic region of RACGAP1. The interaction with RACGAP1 inhibits its GAP activity towards CDC42 in vitro, which may be required for maintaining normal spindle morphology. Interacts separately via its N-terminal region with the C-terminus of CENPE, KIF4A and KIF23 during late mitosis. Interacts with KIF14 and KIF20A. Interacts with PLK1. Interacts with KIF20B. {ECO:0000250|UniProtKB:O43663}. DOMAIN: Microtubule binding occurs via a basic patch in the central spectrin-like domain and requires also the unstructured C-terminal domain. {ECO:0000250}. +Q60636 PRDM1_MOUSE PR domain zinc finger protein 1 (EC 2.1.1.-) (B lymphocyte-induced maturation protein 1) (Blimp-1) (Beta-interferon gene positive regulatory domain I-binding factor) (PR domain-containing protein 1) 856 95,836 Alternative sequence (4); Chain (1); Compositional bias (1); Cross-link (2); Domain (1); Erroneous initiation (1); Region (1); Sequence conflict (2); Zinc finger (4) FUNCTION: Transcription factor that mediates a transcriptional program in various innate and adaptive immune tissue-resident lymphocyte T cell types such as tissue-resident memory T (Trm), natural killer (trNK) and natural killer T (NKT) cells and negatively regulates gene expression of proteins that promote the egress of tissue-resident T-cell populations from non-lymphoid organs (PubMed:27102484). Plays a role in the development, retention and long-term establishment of adaptive and innate tissue-resident lymphocyte T cell types in non-lymphoid organs, such as the skin and gut, but also in other nonbarrier tissues like liver and kidney, and therefore may provide immediate immunological protection against reactivating infections or viral reinfection (PubMed:27102484). Binds specifically to the PRDI element in the promoter of the beta-interferon gene (By similarity). Drives the maturation of B-lymphocytes into Ig secreting cells (By similarity). Associates with the transcriptional repressor ZNF683 to chromatin at gene promoter regions (PubMed:27102484). {ECO:0000250|UniProtKB:O75626, ECO:0000269|PubMed:27102484}. PTM: Sumoylation at Lys-847 by PIAS1 augments transcriptional repressor activity, and is critical for plasma cell differentiation. {ECO:0000250|UniProtKB:O75626}.; PTM: Ubiquitinated by SCF(FBXO11), leading to its degradation by the proteasome. {ECO:0000250|UniProtKB:O75626}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8168136}. Cytoplasm {ECO:0000250|UniProtKB:O75626}. SUBUNIT: Interacts with PRMT5 (PubMed:16699504). Interacts with FBXO10 (By similarity). Interacts with FBXO11 (By similarity). {ECO:0000250|UniProtKB:O75626, ECO:0000269|PubMed:16699504}. TISSUE SPECIFICITY: Expressed in innate lymphocytes, including tissue-resident conventional natural killer (cNK) cells in liver (PubMed:27102484). Expressed also weakly in tissue-resident natural killer (trNK) and natural killer T (NKT) cells in liver (PubMed:27102484). Isoform 1 is detected in bone marrow, spleen and lymph node but not in brain, heart, kidney, liver, ovary or muscle. Weak expression detected in the lung. Isoform 3 is detected only in yolk sac. Isoform 4 is detected in embryo, yolk sac, placenta, splenocytes, and activated T-cells. {ECO:0000269|PubMed:11121475, ECO:0000269|PubMed:19737919, ECO:0000269|PubMed:27102484, ECO:0000269|PubMed:8168136}. +Q810F0 PRIMA_MOUSE Proline-rich membrane anchor 1 (PRiMA) 153 16,564 Alternative sequence (2); Chain (1); Domain (1); Glycosylation (1); Mutagenesis (5); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 93 113 Helical. {ECO:0000255}. TOPO_DOM 36 92 Extracellular. {ECO:0000255}.; TOPO_DOM 114 153 Cytoplasmic. {ECO:0000255}. FUNCTION: Required to anchor acetylcholinesterase (ACHE) to the basal lamina of the neuromuscular junction and to the membrane of neuronal synapses in brain. Also able to organize ACHE into tetramers. {ECO:0000269|PubMed:11804574}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Cell junction. Cell junction, synapse. Note=In the brain, PRIMA linked to ACHE is found in membrane rafts. SUBUNIT: Interacts with ACHE, probably through disulfide bonds. {ECO:0000269|PubMed:11804574}. DOMAIN: The proline-rich attachment domain (PRAD) binds the AChE catalytic subunits. {ECO:0000269|PubMed:11804574}. TISSUE SPECIFICITY: Predominantly expressed in the central nervous system, including in the brain. Also expressed in muscle, heart and kidney. Isoform 1 may be predominant in the cortex and striatum, while isoform 2 is more abundant in the cerebellum. {ECO:0000269|PubMed:11804574, ECO:0000269|PubMed:14622217}. +Q08501 PRLR_MOUSE Prolactin receptor (PRL-R) 608 68,241 Alternative sequence (4); Chain (1); Disulfide bond (2); Domain (2); Glycosylation (3); Metal binding (2); Motif (2); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 230 253 Helical. {ECO:0000250}. TOPO_DOM 20 229 Extracellular. {ECO:0000250}.; TOPO_DOM 254 608 Cytoplasmic. {ECO:0000250}. FUNCTION: This is a receptor for the anterior pituitary hormone prolactin. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Interacts with SMARCA1. Interacts with NEK3 and VAV2 and this interaction is prolactin-dependent. {ECO:0000250}. DOMAIN: The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.; DOMAIN: The box 1 motif is required for JAK interaction and/or activation. +B2RQC6 PYR1_MOUSE CAD protein [Includes: Glutamine-dependent carbamoyl-phosphate synthase (EC 6.3.5.5); Aspartate carbamoyltransferase (EC 2.1.3.2); Dihydroorotase (EC 3.5.2.3)] 2225 243,238 Active site (3); Alternative sequence (1); Binding site (5); Chain (1); Domain (4); Initiator methionine (1); Metal binding (18); Modified residue (11); Nucleotide binding (2); Region (8) Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3. Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3. Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. "FUNCTION: This protein is a ""fusion"" protein encoding four enzymatic activities of the pyrimidine pathway (GATase, CPSase, ATCase and DHOase). {ECO:0000250|UniProtKB:P27708}." PTM: Activated by MAP kinase (Erk1/2) phosphorylation just prior to the S phase of the cell cycle, when the demand for pyrimidine nucleotides is greatest, and down-regulated as the cells emerge from S phase by protein kinase A (PKA) phosphorylation. Phosphorylation at Ser-1859 by RPS6KB1 downstream of MTOR promotes oligomerization and stimulates dihydroorotase activity. Phosphorylation at Ser-1406 reduces sensitivy to feedback inhibition by UTP (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Cytosolic and unphosphorylated in resting cells, translocates to the nucleus in response to EGF stimulation, nuclear import promotes optimal cell growth. {ECO:0000250}. SUBUNIT: Homohexamer. Interacts with CIPC. {ECO:0000250|UniProtKB:P27708}. +P17932 RL32P_MOUSE Putative 60S ribosomal protein L32' 135 16,011 Chain (1) +Q8BW41 PMGT2_MOUSE Protein O-linked-mannose beta-1,4-N-acetylglucosaminyltransferase 2 (POMGnT2) (EC 2.4.1.312) (Extracellular O-linked N-acetylglucosamine transferase-like) (Glycosyltransferase-like domain-containing protein 2) 605 69,378 Alternative sequence (2); Chain (1); Domain (1); Erroneous termination (1); Glycosylation (2); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 5 25 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 4 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 26 580 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: O-linked mannose beta-1,4-N-acetylglucosaminyltransferase that transfers UDP-N-acetyl-D-glucosamine to the 4-position of the mannose to generate N-acetyl-D-glucosamine-beta-1,4-O-D-mannosylprotein (By similarity). Involved in the biosynthesis of the phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-3-N-acetylglucosamine-beta-4-(phosphate-6-)mannose), a carbohydrate structure present in alpha-dystroglycan (DAG1), which is required for binding laminin G-like domain-containing extracellular proteins with high affinity (PubMed:24256719). {ECO:0000250|UniProtKB:Q8NAT1, ECO:0000269|PubMed:24256719}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8NAT1}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q8NAT1}. TISSUE SPECIFICITY: Mainly expressed in the central nervous system. {ECO:0000269|PubMed:24256719}. +A2AJT4 PNISR_MOUSE Arginine/serine-rich protein PNISR (Serine/arginine-rich-splicing regulatory protein 130) (SRrp130) (Splicing factor, arginine/serine-rich 130) (Splicing factor, arginine/serine-rich 18) 805 92,115 Chain (1); Coiled coil (2); Compositional bias (4); Cross-link (3); Modified residue (10); Sequence conflict (1) SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}. SUBUNIT: Interacts with PNN. {ECO:0000250}. +Q64387 PNOC_MOUSE Prepronociceptin (N23K/N27K) [Cleaved into: Nocistatin; Nociceptin (Orphanin FQ) (PPNOC); Orphanin FQ2] 187 20,884 Alternative sequence (1); Peptide (3); Propeptide (2); Region (1); Repeat (3); Sequence conflict (1); Signal peptide (1) FUNCTION: Nociceptin: Ligand of the opioid receptor-like receptor OPRL1. It may act as a transmitter in the brain by modulating nociceptive and locomotor behavior. May be involved in neuronal differentiation and development. When administered intracerebroventricularly, nociceptin induces hyperalgesia and decreases locomotor activity.; FUNCTION: Nocistatin: Blocks nociceptin action in pain transmission by inhibiting nociceptin-induced hyperalgesia and allodynia. {ECO:0000250|UniProtKB:O62647}.; FUNCTION: Orphanin FQ2: Has potent analgesic activity. {ECO:0000269|PubMed:9601687}. PTM: Specific enzymatic cleavages at paired basic residues probably yield other active peptides besides nociceptin.; PTM: The N-terminal domain contains 6 conserved cysteines thought to be involved in disulfide bonding and/or processing. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Brain and spinal cord. Low levels in kidney and spleen. +P23492 PNPH_MOUSE Purine nucleoside phosphorylase (PNP) (EC 2.4.2.1) (Inosine phosphorylase) (Inosine-guanosine phosphorylase) 289 32,277 Binding site (6); Chain (1); Modified residue (1); Natural variant (5); Region (1) Purine metabolism; purine nucleoside salvage. FUNCTION: The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. {ECO:0000269|PubMed:1902950}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. SUBUNIT: Homotrimer. +Q91XF0 PNPO_MOUSE Pyridoxine-5'-phosphate oxidase (EC 1.4.3.5) (Pyridoxamine-phosphate oxidase) 261 30,114 Binding site (7); Chain (1); Erroneous initiation (1); Modified residue (2); Nucleotide binding (4); Region (2) Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1. Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxine 5'-phosphate: step 1/1. FUNCTION: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP). {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +Q9QZB0 RGS17_MOUSE Regulator of G-protein signaling 17 (RGS17) (Regulator of Gz-selective protein signaling 2) 210 24,345 Chain (1); Compositional bias (1); Domain (1); Modified residue (1) FUNCTION: Regulates G protein-coupled receptor signaling cascades, including signaling via muscarinic acetylcholine receptor CHRM2 and dopamine receptor DRD2 (By similarity). Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. Binds selectively to GNAZ and GNAI2 subunits, accelerates their GTPase activity and regulates their signaling activities. Negatively regulates mu-opioid receptor-mediated activation of the G-proteins. {ECO:0000250|UniProtKB:Q9UGC6, ECO:0000269|PubMed:15827571, ECO:0000269|PubMed:16900103}. PTM: N- and O-glycosylated in synapsomal membranes. {ECO:0000269|PubMed:15827571}.; PTM: Serine phosphorylated in synapsomal membranes. {ECO:0000269|PubMed:16900103}.; PTM: Sumoylated with SUMO1 and SUM02 in synaptosomes. The sumoylated forms act as a scaffold for sequestering mu-opioid receptor-activated G(alpha) subunits. {ECO:0000269|PubMed:16900103}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:15827571, ECO:0000269|PubMed:16900103}. Cell junction, synapse, synaptosome {ECO:0000269|PubMed:15827571, ECO:0000269|PubMed:16900103}. Nucleus {ECO:0000269|PubMed:16900103}. Cytoplasm {ECO:0000269|PubMed:16900103}. SUBUNIT: Interacts with GNAI1 and GNAQ (By similarity). Interacts with GNAZ and GNAI2 (PubMed:15827571, PubMed:16900103). Interacts with OPRM1 (PubMed:15827571). Forms a complex with mu-opioid receptors and G(alpha)z/i2 subunits, including GNAZ and GNAI2; the formation of this complex results in mu-opioid receptor desensitization (PubMed:15827571). {ECO:0000250|UniProtKB:Q9UGC6, ECO:0000269|PubMed:15827571, ECO:0000269|PubMed:16900103}. TISSUE SPECIFICITY: Detected in brain (at protein level) (PubMed:15827571, PubMed:16900103). Highly expressed in the hypothalamus, periaqueductal gray matter, and pons-medulla. Lower levels in the thalamus, cortex and spinal cord. Weak expression in the striatum and cerebellum. {ECO:0000269|PubMed:15827571, ECO:0000269|PubMed:16900103}. +P25425 PO2F1_MOUSE POU domain, class 2, transcription factor 1 (NF-A1) (Octamer-binding protein 1) (Oct-1) (Octamer-binding transcription factor 1) (OTF-1) 770 79,547 Alternative sequence (14); Chain (1); DNA binding (1); Domain (1); Modified residue (5); Sequence conflict (16) FUNCTION: Transcription factor that binds to the octamer motif (5'-ATTTGCAT-3') and activates the promoters of the genes for some small nuclear RNAs (snRNA) and of genes such as those for histone H2B and immunoglobulins. Modulates transcription transactivation by NR3C1, AR and PGR (By similarity). {ECO:0000250}. PTM: Phosphorylated by PRKDC. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with NR3C1, AR, PGR and HCFC1. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed. However, isoforms 4 and 5 are only expressed in lymphocytes. {ECO:0000269|PubMed:10023087, ECO:0000269|PubMed:11683265, ECO:0000269|PubMed:14729276, ECO:0000269|PubMed:7711063}. +Q8JZX3 POC1A_MOUSE POC1 centriolar protein homolog A (WD repeat-containing protein 51A) 405 45,125 Alternative sequence (2); Chain (1); Coiled coil (1); Repeat (7); Sequence conflict (4) FUNCTION: Plays an important role in centriole assembly and/or stability and ciliogenesis. Involved in early steps of centriole duplication, as well as in the later steps of centriole length control. Acts in concert with POC1B to ensure centriole integrity and proper mitotic spindle formation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. Note=Component of both mother and daughter centrioles. {ECO:0000250}. SUBUNIT: Interacts with POC1B. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed in embryonic and adult tissues. {ECO:0000269|PubMed:22840364}. +Q9DBS8 POC5_MOUSE Centrosomal protein POC5 (Protein of centriole 5) 558 60,956 Alternative sequence (2); Chain (1); Coiled coil (2); Frameshift (1); Modified residue (5); Repeat (3); Sequence conflict (2) FUNCTION: Essential for the assembly of the distal half of centrioles, required for centriole elongation. {ECO:0000250}. PTM: Hyperphosphorylated during recruitment to procentrioles in G2/M phase. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250}. Note=Localized to the distal portion of centrioles. {ECO:0000250}. SUBUNIT: Interacts with CETN2 and CETN3. {ECO:0000250}. +Q5K2P8 POLS2_MOUSE Polyserase-2 (EC 3.4.21.-) (Polyserine protease 2) (Serine protease 36) 849 91,852 Active site (3); Chain (1); Disulfide bond (11); Domain (3); Glycosylation (6); Propeptide (1); Signal peptide (1) FUNCTION: Serine protease. Hydrolyzes the peptides N-t-Boc-Gln-Ala-Arg-AMC and N-t-Boc-Gln-Gly-Arg-AMC and, to a lesser extent, N-t-Boc-Ala-Phe-Lys-AMC and N-t-Boc-Val-Leu-Lys-AMC. Has a preference for substrates with an Arg instead of a Lys residue in position P1 (By similarity). {ECO:0000250}. PTM: The 3 protease domains are not proteolytically cleaved. {ECO:0000250}.; PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. Note=Not attached to membranes. {ECO:0000250}. DOMAIN: The first serine protease domain is catalytically active, whereas the second domain lacks the essential His residue of the catalytic triad at position 363, and the third domain lacks the essential Asp residue of the catalytic triad at position 673. The second and third domains are therefore predicted to be inactive. +Q9ES82 POPD2_MOUSE Popeye domain-containing protein 2 (Popeye protein 2) 367 41,252 Chain (1); Glycosylation (2); Modified residue (1); Mutagenesis (1); Transmembrane (2) TRANSMEM 36 56 Helical. {ECO:0000255}.; TRANSMEM 77 97 Helical. {ECO:0000255}. FUNCTION: Important for the maintenance of cardiac function. Plays a regulatory function in heart rate dynamics mediated, at least in part, through cAMP-binding and, probably, by increasing cell surface expression of the potassium channel KCNK2 and enhancing current density. {ECO:0000250|UniProtKB:Q6JWV8, ECO:0000269|PubMed:22354168}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:Q9HBU9}. TISSUE SPECIFICITY: Expressed in the developing and adult heart, with high expression levels in the sinus and atrioventricular nodes. Also expressed in the bladder and skeletal muscle. {ECO:0000269|PubMed:10882522, ECO:0000269|PubMed:22354168}. +Q9ES81 POPD3_MOUSE Popeye domain-containing protein 3 (Popeye protein 3) 291 33,612 Chain (1); Glycosylation (1); Transmembrane (3) TRANSMEM 27 44 Helical. {ECO:0000255}.; TRANSMEM 48 70 Helical. {ECO:0000255}.; TRANSMEM 77 99 Helical. {ECO:0000255}. FUNCTION: May play a role in the maintenance of heart function mediated, at least in part, through cAMP-binding. {ECO:0000269|PubMed:10882522, ECO:0000269|PubMed:22354168}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in cardiac and skeletal muscle. {ECO:0000269|PubMed:10882522}. +A2AGA4 RHBL2_MOUSE Rhomboid-related protein 2 (RRP2) (EC 3.4.21.105) [Cleaved into: Rhomboid-related protein 2, N-terminal fragment (NTF); Rhomboid-related protein 2, C-terminal fragment (CTF)] 302 33,735 Active site (2); Chain (3); Mutagenesis (2); Transmembrane (7) TRANSMEM 71 91 Helical. {ECO:0000255}.; TRANSMEM 127 147 Helical. {ECO:0000255}.; TRANSMEM 158 178 Helical. {ECO:0000255}.; TRANSMEM 182 202 Helical. {ECO:0000255}.; TRANSMEM 211 231 Helical. {ECO:0000255}.; TRANSMEM 244 264 Helical. {ECO:0000255}.; TRANSMEM 277 297 Helical. {ECO:0000255}. FUNCTION: Involved in regulated intramembrane proteolysis and the subsequent release of functional polypeptides from their membrane anchors. Known substrate: EFNB3 (By similarity). {ECO:0000250}. PTM: Proteolytic processing of the proenzyme produces an N- and a C-terminal fragment. The processing is required for activation of the protease (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Rhomboid-related protein 2, C-terminal fragment: Cell membrane {ECO:0000250|UniProtKB:Q9NX52}; Multi-pass membrane protein {ECO:0000255}. +Q8CF94 RHD_MOUSE Blood group Rh(D) polypeptide (Erythrocyte membrane glycoprotein Rh30) (CD antigen CD240D) 418 45,877 Chain (1); Natural variant (1); Sequence conflict (10); Transmembrane (12) TRANSMEM 12 32 Helical. {ECO:0000255}.; TRANSMEM 43 63 Helical. {ECO:0000255}.; TRANSMEM 73 93 Helical. {ECO:0000255}.; TRANSMEM 112 131 Helical. {ECO:0000255}.; TRANSMEM 133 155 Helical. {ECO:0000255}.; TRANSMEM 166 186 Helical. {ECO:0000255}.; TRANSMEM 211 231 Helical. {ECO:0000255}.; TRANSMEM 241 261 Helical. {ECO:0000255}.; TRANSMEM 268 288 Helical. {ECO:0000255}.; TRANSMEM 290 310 Helical. {ECO:0000255}.; TRANSMEM 331 351 Helical. {ECO:0000255}.; TRANSMEM 368 388 Helical. {ECO:0000255}. FUNCTION: May be part of an oligomeric complex which is likely to have a transport or channel function in the erythrocyte membrane. {ECO:0000250}. PTM: Palmitoylated. {ECO:0000250|UniProtKB:Q02161}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q02161}; Multi-pass membrane protein {ECO:0000255}. +P09242 PPBT_MOUSE Alkaline phosphatase, tissue-nonspecific isozyme (AP-TNAP) (TNSALP) (EC 3.1.3.1) (Alkaline phosphatase 2) (Alkaline phosphatase liver/bone/kidney isozyme) 524 57,514 Active site (1); Chain (1); Disulfide bond (2); Glycosylation (5); Lipidation (1); Metal binding (10); Modified residue (1); Propeptide (1); Sequence conflict (1); Signal peptide (1) FUNCTION: This isozyme may play a role in skeletal mineralization. {ECO:0000250|UniProtKB:P05186}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:P05186}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P05186}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P05186}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P05186}. +P16675 PPGB_MOUSE Lysosomal protective protein (EC 3.4.16.5) (Carboxypeptidase C) (Carboxypeptidase L) (Cathepsin A) (Protective protein cathepsin A) (PPCA) (Protective protein for beta-galactosidase) [Cleaved into: Lysosomal protective protein 32 kDa chain; Lysosomal protective protein 20 kDa chain] 474 53,844 Active site (3); Chain (3); Disulfide bond (4); Glycosylation (2); Sequence conflict (1); Signal peptide (1) FUNCTION: Protective protein appears to be essential for both the activity of beta-galactosidase and neuraminidase, it associates with these enzymes and exerts a protective function necessary for their stability and activity. This protein is also a carboxypeptidase and can deamidate tachykinins. SUBCELLULAR LOCATION: Lysosome. SUBUNIT: Heterodimer of a 32 kDa chain and a 20 kDa chain; disulfide-linked. {ECO:0000250}. +Q8K2H1 PPHLN_MOUSE Periphilin-1 381 43,835 Alternative sequence (1); Chain (1); Compositional bias (1); Cross-link (6); Modified residue (10); Motif (1); Sequence conflict (1) FUNCTION: Component of the HUSH complex, a multiprotein complex that mediates epigenetic repression. The HUSH complex is recruited to genomic loci rich in H3K9me3 and is probably required to maintain transcriptional silencing by promoting recruitment of SETDB1, a histone methyltransferase that mediates further deposition of H3K9me3. In the HUSH complex, contributes to the maintenance of the complex at chromatin. Acts as a transcriptional corepressor and regulates the cell cycle, probably via the HUSH complex. May be involved in epithelial differentiation by contributing to epidermal integrity and barrier formation. {ECO:0000250|UniProtKB:Q8NEY8}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8NEY8}. Cytoplasm {ECO:0000250|UniProtKB:Q8NEY8}. Chromosome {ECO:0000250|UniProtKB:Q8NEY8}. Note=In undifferentiated keratinocytes expressed in speckle-type nuclear granules and at the nuclear membrane, but in the differentiated keratinocytes colocalized with periplakin at the cell periphery and at cell-cell junctions. Localizes to chromatin. {ECO:0000250|UniProtKB:Q8NEY8}. SUBUNIT: Homodimer. Component of the HUSH complex; at least composed of FAM208A/TASOR, PPHLN1 and MPHOSPH8. Interacts with SIN3A and HDAC1. Interacts with PPL. {ECO:0000250|UniProtKB:Q8NEY8}. TISSUE SPECIFICITY: Ubiquitously expressed. Strong expression in the developing somites and limbs, the embryonic nervous system and the adult brain. {ECO:0000269|PubMed:19621438}. +P30412 PPIC_MOUSE Peptidyl-prolyl cis-trans isomerase C (PPIase C) (EC 5.2.1.8) (Cyclophilin C) (Rotamase C) 212 22,794 Beta strand (11); Chain (1); Domain (1); Helix (3); Turn (4) FUNCTION: PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. {ECO:0000269|PubMed:1652374}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1652374}. TISSUE SPECIFICITY: Specifically expressed in kidney. {ECO:0000269|PubMed:1652374}. +Q9CR16 PPID_MOUSE Peptidyl-prolyl cis-trans isomerase D (PPIase D) (EC 5.2.1.8) (40 kDa peptidyl-prolyl cis-trans isomerase) (Cyclophilin-40) (CYP-40) (Rotamase D) 370 40,743 Chain (1); Domain (1); Modified residue (3); Region (2); Repeat (3) FUNCTION: PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. Proposed to act as a co-chaperone in HSP90 complexes such as in unligated steroid receptors heterocomplexes. Different co-chaperones seem to compete for association with HSP90 thus establishing distinct HSP90-co-chaperone-receptor complexes with the potential to exert tissue-specific receptor activity control. May have a preference for estrogen receptor complexes and is not found in glucocorticoid receptor complexes. May be involved in cytoplasmic dynein-dependent movement of the receptor from the cytoplasm to the nucleus. May regulate MYB by inhibiting its DNA-binding activity. Involved in regulation of AHR signaling by promoting the formation of the AHR:ARNT dimer; the function is independent of HSP90 but requires the chaperone activity region. Involved in regulation of UV radiation-induced apoptosis. {ECO:0000250|UniProtKB:Q08752, ECO:0000269|PubMed:18771283}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q08752}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q08752}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q08752}. SUBUNIT: Identified in ESR1 or NR3C1/GCR steroid receptor-chaperone complexes. Found in HSP90 chaperone complexes with kinase clients LCK or EIF2AK1. Two monomers associate with one HSP90 homodimer. Interacts with HSP90AA1. Interacts with HSP90AB1; PPID and FKBP4 compete for binding to HSP90AB1 and the interaction is mutually exclusive with the PPID:HSPA8 interaction. Interacts with HSPA8; PPID and STIP1 but not FKBP4 compete for binding to HSPA8 and the interaction is mutually exclusive with the PPID:HSP90AB1 interaction. Interacts with S100A1 and S100A2; the interactions dissociate the PPID:HSP90AA1 interaction. Interacts with S100A6. Interacts with MYB, ILF2, XRCC6, RACK1 and RPS3. Interacts with cytoplasmic dynein 1 intermediate chain (DYNC1I1 or DYNC1I2). {ECO:0000269|PubMed:9195923}. +A2AR02 PPIG_MOUSE Peptidyl-prolyl cis-trans isomerase G (PPIase G) (Peptidyl-prolyl isomerase G) (EC 5.2.1.8) (Cyclophilin G) (Rotamase G) 752 88,325 Chain (1); Compositional bias (6); Cross-link (2); Domain (1); Modified residue (19); Sequence conflict (1) FUNCTION: PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. May be implicated in the folding, transport, and assembly of proteins. May play an important role in the regulation of pre-mRNA splicing. {ECO:0000250|UniProtKB:Q13427}. SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000250|UniProtKB:Q13427}. Nucleus speckle {ECO:0000250|UniProtKB:Q13427}. Note=Colocalizes with splicing factors at nuclear speckles. {ECO:0000250|UniProtKB:Q13427}. SUBUNIT: Interacts with CLK1, PNN and with the phosphorylated C-terminal domain of RNA polymerase II. {ECO:0000250|UniProtKB:Q13427}. DOMAIN: The RS domain is required for the interaction with the phosphorylated C-terminal domain of RNA polymerase II. {ECO:0000250|UniProtKB:Q13427}. +Q9CXG3 PPIL4_MOUSE Peptidyl-prolyl cis-trans isomerase-like 4 (PPIase) (EC 5.2.1.8) (Cyclophilin-like protein PPIL4) (Rotamase PPIL4) 492 57,230 Chain (1); Compositional bias (1); Cross-link (7); Domain (2); Modified residue (4); Sequence conflict (2) FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +P97814 PPIP1_MOUSE Proline-serine-threonine phosphatase-interacting protein 1 (PEST phosphatase-interacting protein 1) 415 47,590 Chain (1); Coiled coil (2); Domain (2); Modified residue (2); Mutagenesis (2); Sequence conflict (1) FUNCTION: Involved in regulation of the actin cytoskeleton. May regulate WAS actin-bundling activity. Bridges the interaction between ABL1 and PTPN18 leading to ABL1 dephosphorylation. May play a role as a scaffold protein between PTPN12 and WAS and allow PTPN12 to dephosphorylate WAS. Has the potential to physically couple CD2 and CD2AP to WAS. Acts downstream of CD2 and CD2AP to recruit WAS to the T-cell:APC contact site so as to promote the actin polymerization required for synapse induction during T-cell activation. Down-regulates CD2-stimulated adhesion through the coupling of PTPN12 to CD2. Also has a role in innate immunity and the inflammatory response. Recruited to inflammasomes by MEFV. Induces formation of pyroptosomes, large supramolecular structures composed of oligomerized PYCARD dimers which form prior to inflammatory apoptosis. Binding to MEFV allows MEFV to bind to PYCARD and facilitates pyroptosome formation. Regulates endocytosis and cell migration in neutrophils. {ECO:0000269|PubMed:11163214, ECO:0000269|PubMed:11711533, ECO:0000269|PubMed:12530983, ECO:0000269|PubMed:9265651, ECO:0000269|PubMed:9488710}. PTM: Dephosphorylated on Tyr-344 by PTPN18, this event negatively regulates the association of PSTPIP1 with SH2 domain-containing proteins as tyrosine kinase. Phosphorylation of Tyr-344 is probably required for subsequent phosphorylation at other tyrosine residues. Phosphorylation is induced by activation of the EGFR and PDGFR in a ABL1 dependent manner. The phosphorylation regulates the interaction with WAS and with MEFV. {ECO:0000269|PubMed:11163214, ECO:0000269|PubMed:11711533, ECO:0000269|PubMed:9265651, ECO:0000269|PubMed:9488710}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11711533, ECO:0000269|PubMed:12530983}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:11711533}. Cell projection, lamellipodium {ECO:0000269|PubMed:9265651}. Cleavage furrow {ECO:0000269|PubMed:9265651}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9265651, ECO:0000269|PubMed:9488710}. Cell membrane {ECO:0000250|UniProtKB:O43586}; Peripheral membrane protein {ECO:0000250|UniProtKB:O43586}. Cell projection, uropodium {ECO:0000250|UniProtKB:O43586}. Note=Colocalized with PTPN12 in the cytoplasm and the perinuclear region (PubMed:11711533). During interphase, colocalizes with F-actin in the cortical cytoskeleton, lamellipodia, and stress fibers (PubMed:9265651). In dividing cells, colocalizes with the F-actin rich cytokinetic cleavage furrow (PubMed:9265651). Colocalized with CD2AP and WAS in the actin cytoskeleton within the cytoplasm (PubMed:12530983, PubMed:9488710). Colocalized with CD2, CD2AP and WAS at the site of T-cell:APC contact (PubMed:12530983). Mainly cytoplasmic in T cells. Colocalizes in cluster with CD2 near the cell surface membrane in activated T-cells. In monocytes, forms a branched filamentous network in the cytoplasm. In transfected cells, forms relatively straight filaments radiating out from the nucleus. Filament formation requires an intact tubulin cytoskeleton. In migrating neutrophils, colocalizes with PIP5K1C and DNM2 to the trailing edge of the uropod in a actin-dependent manner (By similarity). {ECO:0000250|UniProtKB:O43586, ECO:0000269|PubMed:11711533, ECO:0000269|PubMed:12530983, ECO:0000269|PubMed:9265651, ECO:0000269|PubMed:9488710}. SUBUNIT: Homodimer. Homotrimer. Interacts (via coiled-coil domain) with CD2AP, PTPN12 and PTPN18. Interacts (via SH3 domain) with ABL1 and WAS. Interacts (via SH3 and coiled-coil domains) with MEFV (via B-box zinc finger); the interaction allows binding of MEFV to PYCARD and facilitates formation of PYCARD pyroptosomes. Interacts with DNM2 and FASLG (By similarity). Interacts with CD2. {ECO:0000250, ECO:0000269|PubMed:11163214, ECO:0000269|PubMed:11711533, ECO:0000269|PubMed:12530983, ECO:0000269|PubMed:9265651, ECO:0000269|PubMed:9488710}. DOMAIN: The F-BAR domain is important for filament formation. The SH3 domain is not required for filament formation or localization to the uropod (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in adult lung and spleen, and weakly expressed in testis, muscle, kidney, brain and heart. Highly expressed in spleen and thymus, moderately in lung, brain and muscle, and weakly expressed in heart and liver (at protein level). {ECO:0000269|PubMed:11711533, ECO:0000269|PubMed:9265651}. +Q9D0W5 PPIL1_MOUSE Peptidyl-prolyl cis-trans isomerase-like 1 (PPIase) (EC 5.2.1.8) (Rotamase PPIL1) 166 18,237 Binding site (2); Chain (1); Domain (1); Modified residue (1); Region (4) FUNCTION: Involved in pre-mRNA splicing as component of the spliceosome. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. {ECO:0000250|UniProtKB:Q9Y3C6}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y3C6}. SUBUNIT: Identified in the spliceosome C complex. Interacts with SNW1. {ECO:0000250|UniProtKB:Q9Y3C6}. +Q8BU27 PPM1M_MOUSE Protein phosphatase 1M (EC 3.1.3.16) (Protein phosphatase 2C isoform eta) (PP2C-eta) (PP2CE) 406 45,273 Alternative sequence (1); Chain (1); Domain (1); Metal binding (5); Sequence conflict (4) SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14654243}. TISSUE SPECIFICITY: Widely expressed with highest levels in testis and lower levels in lung, kidney and brain. {ECO:0000269|PubMed:14654243}. +Q8BGL1 PPM1N_MOUSE Probable protein phosphatase 1N (EC 3.1.3.16) 404 43,201 Chain (1); Compositional bias (1); Domain (1); Metal binding (5) +Q8BVQ5 PPME1_MOUSE Protein phosphatase methylesterase 1 (PME-1) (EC 3.1.1.89) 386 42,256 Active site (3); Chain (1); Compositional bias (1); Erroneous initiation (1); Modified residue (3); Sequence conflict (3) FUNCTION: Demethylates proteins that have been reversibly carboxymethylated. Demethylates PPP2CB (in vitro) and PPP2CA. Binding to PPP2CA displaces the manganese ion and inactivates the enzyme (By similarity). {ECO:0000250}. PTM: Phosphorylated by SIK1 following increases in intracellular sodium, leading to dissociation from the protein phosphatase 2A (PP2A) complex and subsequent dephosphorylation of sodium/potassium-transporting ATPase ATP1A1. {ECO:0000250}. SUBUNIT: Binds PPP2CA and PPP2CB. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. Highly expressed in testis and brain. {ECO:0000269|PubMed:10318862}. +Q9CQR6 PPP6_MOUSE Serine/threonine-protein phosphatase 6 catalytic subunit (PP6C) (EC 3.1.3.16) 305 35,159 Active site (1); Chain (1); Metal binding (7); Modified residue (1) FUNCTION: A component of a signaling pathway regulating cell cycle progression in response to IL2 receptor stimulation. N-terminal domain restricts G1 to S phase progression in cancer cells, in part through control of cyclin D1. Downregulates MAP3K7 kinase activation of the IL1 signaling pathway by dephosphorylation of MAP3K7 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with IGBP1, MAP3K7, NFKBIE, PPP6R1, PPP6R2 and PPP6R3. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed in all tissues tested with strongest expression in lung, spleen, liver, kidney and brain. Weaker expression observed in bladder, pancreas, heart and skeletal muscle. {ECO:0000269|PubMed:16769727}. +Q9Z2E4 PPR17_MOUSE Protein phosphatase 1 regulatory subunit 17 (G substrate) 159 17,815 Chain (1); Modified residue (2); Mutagenesis (2) FUNCTION: Inhibits phosphatase activities of protein phosphatase 1 (PP1) and protein phosphatase 2A (PP2A) complexes. {ECO:0000269|PubMed:9920894}. PTM: Substrate for cGMP-dependent protein kinase (By similarity). Phosphorylation of Thr-72 and Thr-123 is required for its phosphatase activity. Phosphorylated by PRKG1 isoform alpha. {ECO:0000250, ECO:0000269|PubMed:9920894}. TISSUE SPECIFICITY: Expressed in Purkinje cells of the cerebellum, hippocampus, pons, medulla and eye. {ECO:0000269|PubMed:9920894}. +Q6A025 PPR26_MOUSE Protein phosphatase 1 regulatory subunit 26 1163 124,934 Chain (1); Erroneous initiation (1); Modified residue (1) FUNCTION: Inhibits phosphatase activity of protein phosphatase 1 (PP1) complexes. May positively regulate cell proliferation. {ECO:0000269|PubMed:16053918}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. SUBUNIT: Interacts with UTP20 and PPP1CA. {ECO:0000250}. +Q3TLH4 PRC2C_MOUSE Protein PRRC2C (BAT2 domain-containing protein 1) (HLA-B-associated transcript 2-like 2) (Proline-rich and coiled-coil-containing protein 2C) 2846 310,892 Alternative sequence (1); Chain (1); Coiled coil (2); Compositional bias (10); Cross-link (1); Frameshift (2); Modified residue (40); Sequence caution (6); Sequence conflict (14) +P04095 PR2C2_MOUSE Prolactin-2C2 (Mitogen-regulated protein 1) (Proliferin-1) 224 25,367 Alternative sequence (1); Chain (1); Disulfide bond (3); Glycosylation (4); Signal peptide (1) FUNCTION: May have a role in embryonic development. It is likely to provide a growth stimulus to target cells in maternal and fetal tissues during the development of the embryo at mid-gestation. May play a role during wound healing and in the hair follicle cycle as a growth factor and/or an angiogenesis factor. May play a role in microvilli formation and cell proliferation of neuroblastoma cells. {ECO:0000269|PubMed:11316781, ECO:0000269|PubMed:16876275}. PTM: N-glycosylated and sialylated. {ECO:0000269|PubMed:10537154}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10537154, ECO:0000269|PubMed:16876275}. Endoplasmic reticulum {ECO:0000269|PubMed:16876275}. TISSUE SPECIFICITY: Expressed in brain and cerebellum (PubMed:16876275). Expressed in placenta and hair follicles, with highest expression levels detected in the outer root sheath and no expression detected in bulb (PubMed:11316781, PubMed:10537154). Also expressed in body fluids such as plasma and amniotic fluid (PubMed:10537154). Expressed in embryonic fibroblasts and at low levels in keratinocytes (PubMed:11316781). Isoform 1: Expressed in brain and Neuro-2a cells (PubMed:16876275). Isoform 2: Expressed in brain (PubMed:16876275). {ECO:0000269|PubMed:10537154, ECO:0000269|PubMed:11316781, ECO:0000269|PubMed:16876275}. +B0QZF7 PRCA1_MOUSE Protein PROCA1 307 34,900 Chain (1); Compositional bias (1); Modified residue (6) +Q00LT2 PRCD_MOUSE Progressive rod-cone degeneration protein homolog 53 5,931 Chain (1); Signal peptide (1) FUNCTION: Involved in vision. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q00LT1}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q00LT1}. Golgi apparatus {ECO:0000250|UniProtKB:Q00LT1}. Secreted {ECO:0000250|UniProtKB:Q00LT1}. +Q810Y8 PRAL7_MOUSE Preferentially expressed antigen in melanoma-like protein 7 (Prame-like 7) 479 55,834 Chain (1); Frameshift (1); Repeat (9); Sequence caution (1); Sequence conflict (2) FUNCTION: Promotes maintenance and self-renewal of pluripotent embryonic stem cells (ESCs), downstream of LIF/STAT3 (PubMed:21425410). Maintains the pluripotency state of ESCs by repressing DNA methylation through the regulation of UHRF1 stability. Mediates the proteasomal degradation of UHRF1. Is required for the establishment of the blastocyst (PubMed:28604677). {ECO:0000269|PubMed:21425410, ECO:0000269|PubMed:28604677}. SUBUNIT: Interacts with UHRF1. {ECO:0000269|PubMed:28604677}. TISSUE SPECIFICITY: Seems to be specific to pluripotent tissues in the early embryo. Not detected in somatic tissues. {ECO:0000269|PubMed:12620990}. +Q80W14 PR40B_MOUSE Pre-mRNA-processing factor 40 homolog B (Huntingtin yeast partner C) (Huntingtin-interacting protein C) 870 99,300 Alternative sequence (4); Chain (1); Coiled coil (1); Compositional bias (1); Cross-link (2); Domain (8); Modified residue (4); Sequence conflict (1) FUNCTION: May be involved in pre-mRNA splicing. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}. SUBUNIT: Interacts with the N-terminus of HD. {ECO:0000250}. +E9Q3T6 PRD14_MOUSE PR domain zinc finger protein 14 (EC 2.1.1.-) (PR domain-containing protein 14) 561 63,374 Beta strand (13); Binding site (1); Chain (1); Domain (1); Helix (3); Mutagenesis (1); Region (1); Sequence conflict (2); Zinc finger (6) FUNCTION: Transcription factor that has both positive and negative roles on transcription (By similarity). Plays a role in cellular pluripotency. Essential for germ cell development at 2 levels: the reacquisition of potential pluripotency, including SOX2 up-regulation, and successful epigenetic reprogramming, characterized by EHMT1 repression. Its association with CBFA2T2 is required for the functions in pluripotency and germ cell formation. {ECO:0000250, ECO:0000269|PubMed:18622394, ECO:0000269|PubMed:26523391}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with CBFA2T2. {ECO:0000269|PubMed:26523391, ECO:0000269|PubMed:27281218}. TISSUE SPECIFICITY: Restricted to embryonic stem cells and primordial germ cells. Not detected in epiblast-derived stem cells. {ECO:0000269|PubMed:18622394, ECO:0000269|PubMed:20953172}. +Q9JII2 PR5A1_MOUSE Prolactin-5A1 (Placental prolactin-like protein L) (PLP-L) (PRL-like protein L) 230 26,556 Chain (1); Disulfide bond (1); Glycosylation (3); Sequence conflict (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +P35700 PRDX1_MOUSE Peroxiredoxin-1 (EC 1.11.1.15) (Macrophage 23 kDa stress protein) (Osteoblast-specific factor 3) (OSF-3) (Thioredoxin peroxidase 2) (Thioredoxin-dependent peroxide reductase 2) 199 22,176 Active site (1); Chain (1); Cross-link (3); Disulfide bond (2); Domain (1); Initiator methionine (1); Modified residue (9); Sequence conflict (1) FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2) (By similarity). Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation (PubMed:19766572). {ECO:0000250|UniProtKB:Q06830, ECO:0000269|PubMed:19766572}. PTM: Phosphorylated on Thr-90 during the M-phase, which leads to a decrease in enzymatic activity. {ECO:0000250|UniProtKB:Q06830}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q06830}. SUBUNIT: Homodimer; disulfide-linked, upon oxidation. 5 homodimers assemble to form a ring-like decamer (By similarity). Interacts with GDPD5; forms a mixed-disulfide with GDPD5 (By similarity). Interacts with SESN1 and SESN2 (By similarity). Interacts with FAM107A (PubMed:21969592). {ECO:0000250|UniProtKB:P0CB50, ECO:0000250|UniProtKB:Q06830, ECO:0000269|PubMed:21969592}. TISSUE SPECIFICITY: Found in various tissues; high concentration in liver. +Q9D1C3 PREY_MOUSE Protein preY, mitochondrial 112 12,506 Chain (1); Domain (1); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}. +P07978 PRM2_MOUSE Protamine-2 (Sperm histone P2) (Sperm protamine P2) [Cleaved into: PP2-A; PP2-C; PP2-D; PP2-B (Protamine mP2)] 107 13,638 Chain (4); Initiator methionine (1); Modified residue (3) FUNCTION: Protamines substitute for histones in the chromatin of sperm during the haploid phase of spermatogenesis. They compact sperm DNA into a highly condensed, stable and inactive complex. {ECO:0000269|PubMed:12620939, ECO:0000269|PubMed:28366643}. PTM: Proteolytic processing into mature chains is required for histone eviction during spermatogenesis (PubMed:28366643). Transition proteins (TNP1 and TNP2) are required for processing (PubMed:28366643). {ECO:0000269|PubMed:28366643}. SUBCELLULAR LOCATION: Nucleus. Chromosome {ECO:0000269|PubMed:28366643}. SUBUNIT: Interacts with TDRP. {ECO:0000269|PubMed:27069551}. TISSUE SPECIFICITY: Testis. +A2ADA5 PUSL1_MOUSE tRNA pseudouridine synthase-like 1 (EC 5.4.99.-) (tRNA pseudouridylate synthase-like 1) (tRNA-uridine isomerase-like 1) 291 31,993 Active site (1); Alternative sequence (6); Binding site (1); Chain (1) +Q9D1A0 PXL2C_MOUSE Peroxiredoxin-like 2C (AhpC/TSA antioxidant enzyme domain-containing protein 1) (Thioredoxin-like protein AAED1) 226 24,904 Chain (1) FUNCTION: May regulate positively ERK1/2 signaling and AKT1 activation leading to HIF1A up-regulation with an increased expression of glycolysis genes and enhanced glycolysis. {ECO:0000250|UniProtKB:Q7RTV5}. +O35435 PYRD_MOUSE Dihydroorotate dehydrogenase (quinone), mitochondrial (DHOdehase) (EC 1.3.5.2) (Dihydroorotate oxidase) 395 42,700 Active site (1); Binding site (8); Chain (1); Nucleotide binding (2); Region (3); Topological domain (2); Transit peptide (1); Transmembrane (1) TRANSMEM 11 30 Helical. {ECO:0000255}. TOPO_DOM 1 10 Mitochondrial matrix. {ECO:0000255}.; TOPO_DOM 31 395 Mitochondrial intermembrane. {ECO:0000255}. Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1. FUNCTION: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor. PTM: The uncleaved transit peptide is required for mitochondrial targeting and proper membrane integration. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. +B9EKX1 PTHD4_MOUSE Patched domain-containing protein 4 904 103,115 Chain (1); Domain (1); Erroneous initiation (1); Glycosylation (3); Transmembrane (12) TRANSMEM 41 61 Helical. {ECO:0000255}.; TRANSMEM 295 312 Helical. {ECO:0000255}.; TRANSMEM 323 343 Helical. {ECO:0000255}.; TRANSMEM 351 371 Helical. {ECO:0000255}.; TRANSMEM 394 414 Helical. {ECO:0000255}.; TRANSMEM 431 451 Helical. {ECO:0000255}.; TRANSMEM 523 543 Helical. {ECO:0000255}.; TRANSMEM 718 738 Helical. {ECO:0000255}.; TRANSMEM 744 764 Helical. {ECO:0000255}.; TRANSMEM 771 791 Helical. {ECO:0000255}.; TRANSMEM 823 843 Helical. {ECO:0000255}.; TRANSMEM 845 865 Helical. {ECO:0000255}. FUNCTION: Could act as a repressor of canonical hedgehog signaling by antagonizing the effects of SMO, as suggested by down-regulation of hedgehog target genes, including GLI1, PTCH1, and PTCH2 in PTCHD4-expressing cells. {ECO:0000250|UniProtKB:Q6ZW05}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +O35295 PURB_MOUSE Transcriptional activator protein Pur-beta (Purine-rich element-binding protein B) (Vascular actin single-stranded DNA-binding factor 2 p44 component) 324 33,901 Chain (1); Compositional bias (3); DNA binding (1); Initiator methionine (1); Modified residue (11) FUNCTION: Has capacity to bind repeated elements in single-stranded DNA such as the purine-rich single strand of the PUR element located upstream of the MYC gene. Participates in transcriptional and translational regulation of alpha-MHC expression in cardiac myocytes by binding to the purine-rich negative regulatory (PNR) element. Modulates constitutive liver galectin-3 gene transcription by binding to its promoter. May play a role in the dendritic transport of a subset of mRNAs (By similarity). Plays a role in the control of vascular smooth muscle (VSM) alpha-actin gene transcription as repressor in myoblasts and fibroblasts. {ECO:0000250, ECO:0000269|PubMed:11751932, ECO:0000269|PubMed:9334258}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Homodimer, heterodimer with PURA and heterotrimer with PURA and YBX1/Y-box protein 1. {ECO:0000269|PubMed:10318844}. +Q8BU03 PWP2_MOUSE Periodic tryptophan protein 2 homolog 919 102,910 Chain (1); Modified residue (5); Repeat (14); Sequence conflict (1) SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. +P70303 PYRG2_MOUSE CTP synthase 2 (EC 6.3.4.2) (CTP synthetase 2) (CTPsH) (UTP--ammonia ligase 2) 586 65,514 Active site (3); Alternative sequence (4); Chain (1); Domain (1); Modified residue (3) Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2. FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Constitutes the rate-limiting enzyme in the synthesis of cytosine nucleotides (By similarity). {ECO:0000250}. +Q80UG2 PLXA4_MOUSE Plexin-A4 1893 212,560 Chain (1); Disulfide bond (10); Domain (8); Erroneous initiation (1); Glycosylation (4); Modified residue (1); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1237 1257 Helical. {ECO:0000255}. TOPO_DOM 24 1236 Extracellular. {ECO:0000255}.; TOPO_DOM 1258 1893 Cytoplasmic. {ECO:0000255}. FUNCTION: Coreceptor for SEMA3A. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance in the developing nervous system. Class 3 semaphorins bind to a complex composed of a neuropilin and a plexin. The plexin modulates the affinity of the complex for specific semaphorins, and its cytoplasmic domain is required for the activation of down-stream signaling events in the cytoplasm. {ECO:0000269|PubMed:12591607, ECO:0000269|PubMed:18262512}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Interacts with NRP1 and NRP2. {ECO:0000269|PubMed:18262512}. TISSUE SPECIFICITY: Expressed in the developing nervous system. Widely expressed in both the central and peripheral nervous systems. Expressed in the peripheral ganglia, somatosensory, olfactory, visual, auditory and equilibrium systems. {ECO:0000269|PubMed:12591607}. +Q9R0M4 PODXL_MOUSE Podocalyxin (Podocalyxin-like protein 1) (PC) (PCLP-1) 503 53,389 Chain (1); Compositional bias (1); Glycosylation (8); Modified residue (3); Natural variant (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 405 425 Helical. {ECO:0000255}. TOPO_DOM 22 404 Extracellular. {ECO:0000255}.; TOPO_DOM 426 503 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in the regulation of both adhesion and cell morphology and cancer progression. Function as an anti-adhesive molecule that maintains an open filtration pathway between neighboring foot processes in the podocyte by charge repulsion. Acts as a pro-adhesive molecule, enhancing the adherence of cells to immobilized ligands, increasing the rate of migration and cell-cell contacts in an integrin-dependent manner. Induces the formation of apical actin-dependent microvilli. Involved in the formation of a preapical plasma membrane subdomain to set up initial epithelial polarization and the apical lumen formation during renal tubulogenesis. Plays a role in cancer development and aggressiveness by inducing cell migration and invasion through its interaction with the actin-binding protein EZR. Affects EZR-dependent signaling events, leading to increased activities of the MAPK and PI3K pathways in cancer cells. {ECO:0000269|PubMed:11435469, ECO:0000269|PubMed:17311105}. PTM: N- and O-linked glycosylated. Sialoglycoprotein (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:17311105}. Cell projection, microvillus {ECO:0000269|PubMed:17311105}. Membrane raft {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Cell projection, filopodium {ECO:0000250}. Cell projection, ruffle {ECO:0000250}. Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=In single attached epithelial cells is restricted to a preapical pole on the free plasma membrane whereas other apical and basolateral proteins are not yet polarized. Colocalizes with SLC9A3R2 at the apical plasma membrane during epithelial polarization. Colocalizes with SLC9A3R1 at the trans-Golgi network (transiently) and at the apical plasma membrane. Its association with the membrane raft is transient. Forms granular, punctuated pattern, forming patches, preferentially adopting a polar distribution, located on the migrating poles of the cell or forming clusters along the terminal ends of filipodia establishing contact with the endothelial cells. Colocalizes with the submembrane actin of lamellipodia, particularly associated with ruffles. Colocalizes with vinculin at protrusions of cells. Colocalizes with ITGB1. Colocalizes with EZR and SLC9A3R2 at the apical cell membrane of glomerular epithelium cells (By similarity). Colocalizes with actin filaments, EZR and SLC9A3R1 in a punctate pattern at the apical cell surface where microvilli form. Colocalizes with PARD3, PRKCI, EXOC5, OCLN, RAB11A and RAB8A in apical membrane initiation sites (AMIS) during the generation of apical surface and luminogenesis (By similarity). {ECO:0000250}. SUBUNIT: Monomer; when associated with the membrane raft. Oligomer; when integrated in the apical membrane. Found in a complex with EZR, PODXL and SLC9A3R2. Associates with the actin cytoskeleton through complex formation with EZR and SLC9A3R2. Interacts (via the C-terminal PDZ-binding motif DTHL) with SLC9A3R1 (via the PDZ domains); interaction is not detected in glomerular epithelium cells, take place early in the secretory pathway and is necessary for its apical membrane sorting. Interacts (via the C-terminal PDZ-binding motif DTHL) with SLC9A3R2 (via the PDZ 1 domain); interaction is detected in glomerular epithelium cells. Interacts with EZR (By similarity). {ECO:0000250}. DOMAIN: Both the O-glycan-rich domain of the extracellular domain and the C-terminus PDZ-binding motif (DTHL) in the cytoplasmic tail harbor an apical sorting signal. The cytoplasmic domain is necessary for the apical membrane targeting and renal tubulogenesis. The large highly anionic extracellular domain allows to maintain open filtration pathways between neighboring podocyte foot processes. The cytoplasmic C-terminus PDZ-binding motif (DTHL) is essential for interaction with SLC9A3R1 and for targeting SLC9A3R1 to the apical cell membrane. The extracellular domain is necessary for microvillus formation (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in liver cells and hematopoietic cells (at protein level). Glomerular epithelium cell (podocyte). {ECO:0000269|PubMed:11435469}. +Q7TQ62 PODN_MOUSE Podocan 611 68,718 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (1); Glycosylation (3); Repeat (20); Signal peptide (1) FUNCTION: Negatively regulates cell proliferation and cell migration, especially in smooth muscle cells. {ECO:0000250}. PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:12796502}. SUBUNIT: Binds to type I collagen. {ECO:0000250}. TISSUE SPECIFICITY: Kidney. Expressed in podocytes and likely vascular endothelial cells within the glomerulus. {ECO:0000269|PubMed:12796502}. +Q07916 PO6F1_MOUSE POU domain, class 6, transcription factor 1 (Octamer-binding transcription factor EMB) (Transcription regulatory protein MCP-1) 301 32,852 Alternative sequence (2); Chain (1); Compositional bias (1); DNA binding (1); Domain (1) FUNCTION: Transcription factor that binds preferentially to a variant of the octamer motif (5'-ATGATAAT-3'). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. TISSUE SPECIFICITY: Isoform C1 and isoform C2 are found in the brain, while isoform C7 is found in the testis. +Q8BJI4 PO6F2_MOUSE POU domain, class 6, transcription factor 2 691 73,309 Chain (1); Compositional bias (3); DNA binding (1); Domain (1) FUNCTION: Probable transcription factor likely to be involved in early steps in the differentiation of amacrine and ganglion cells. Recognizes and binds to the DNA sequence 5'-ATGCAAAT-3' (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-ProRule:PRU00530}. TISSUE SPECIFICITY: Expressed in kidney, heart, muscle, spleen and ovary, but not in lung. {ECO:0000269|PubMed:11284034}. +Q6R3M4 POLI_MOUSE DNA polymerase iota (EC 2.7.7.7) (Rad30 homolog B) 717 79,653 Active site (1); Alternative sequence (1); Beta strand (1); Binding site (2); Chain (1); Domain (1); Helix (5); Metal binding (2); Natural variant (10); Region (2); Sequence conflict (1); Turn (1) FUNCTION: Error-prone DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Favors Hoogsteen base-pairing in the active site. Inserts the correct base with high-fidelity opposite an adenosine template. Exhibits low fidelity and efficiency opposite a thymidine template, where it will preferentially insert guanosine. May play a role in hypermutation of immunogobulin genes. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but may not have lyase activity (By similarity). {ECO:0000250, ECO:0000269|PubMed:15026325}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Accumulates at replication forks after DNA damage. {ECO:0000250}. SUBUNIT: Interacts with POLH (By similarity). Interacts with REV1. {ECO:0000250, ECO:0000269|PubMed:14657033}. DOMAIN: The catalytic core consists of fingers, palm and thumb subdomains, but the fingers and thumb subdomains are much smaller than in high-fidelity polymerases; residues from five sequence motifs of the Y-family cluster around an active site cleft that can accommodate DNA and nucleotide substrates with relaxed geometric constraints, with consequently higher rates of misincorporation and low processivity. {ECO:0000250}. TISSUE SPECIFICITY: Detected in testis, and at very low levels in spleen, lung and brain. Detected in round spermatids, but not in prophase spermatocytes. {ECO:0000269|PubMed:10458907}. +Q9QUG2 POLK_MOUSE DNA polymerase kappa (EC 2.7.7.7) (DINB protein) (DINP) 852 96,003 Alternative sequence (2); Chain (1); Domain (1); Helix (1); Metal binding (2); Natural variant (7); Zinc finger (2) FUNCTION: DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls (PubMed:12432099). Depending on the context, it inserts the correct base, but causes frequent base transitions, transversions and frameshifts. Lacks 3'-5' proofreading exonuclease activity. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but does not have lyase activity (By similarity). {ECO:0000250|UniProtKB:Q9UBT6, ECO:0000269|PubMed:12432099}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UBT6}. Note=Detected throughout the nucleus and at replication foci. Recruited to DNA damage sites in response to ultraviolet irradiation: N6-methyladenosine (m6A)-containing mRNAs accumulate in the vicinity of DNA damage sites and their presence is required to recruit POLK. {ECO:0000250|UniProtKB:Q9UBT6}. SUBUNIT: Interacts with PCNA (By similarity). Interacts with REV1 (PubMed:14657033). {ECO:0000250|UniProtKB:Q9UBT6, ECO:0000269|PubMed:14657033}. DOMAIN: The catalytic core consists of fingers, palm and thumb subdomains, but the fingers and thumb subdomains are much smaller than in high-fidelity polymerases; residues from five sequence motifs of the Y-family cluster around an active site cleft that can accommodate DNA and nucleotide substrates with relaxed geometric constraints, with consequently higher rates of misincorporation and low processivity. TISSUE SPECIFICITY: Detected at low levels in heart, brain, lung, liver, kidney and testis. {ECO:0000269|PubMed:10620008}. +Q8R2R1 POMT1_MOUSE Protein O-mannosyl-transferase 1 (EC 2.4.1.109) (Dolichyl-phosphate-mannose--protein mannosyltransferase 1) 746 85,234 Chain (1); Domain (3); Frameshift (1); Glycosylation (3); Sequence conflict (4); Transmembrane (10) TRANSMEM 30 50 Helical. {ECO:0000255}.; TRANSMEM 90 110 Helical. {ECO:0000255}.; TRANSMEM 121 141 Helical. {ECO:0000255}.; TRANSMEM 144 164 Helical. {ECO:0000255}.; TRANSMEM 176 196 Helical. {ECO:0000255}.; TRANSMEM 228 248 Helical. {ECO:0000255}.; TRANSMEM 266 286 Helical. {ECO:0000255}.; TRANSMEM 597 617 Helical. {ECO:0000255}.; TRANSMEM 636 656 Helical. {ECO:0000255}.; TRANSMEM 660 680 Helical. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Transfers mannosyl residues to the hydroxyl group of serine or threonine residues. Coexpression of both POMT1 and POMT2 is necessary for enzyme activity, expression of either POMT1 or POMT2 alone is insufficient. Essentially dedicated to O-mannosylation of alpha-DAG1 and few other proteins but not of cadherins and protocaherins. {ECO:0000250|UniProtKB:Q9Y6A1}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q8BGQ4 POMT2_MOUSE Protein O-mannosyl-transferase 2 (EC 2.4.1.109) (Dolichyl-phosphate-mannose--protein mannosyltransferase 2) 820 92,386 Alternative sequence (3); Chain (1); Domain (3); Glycosylation (6); Transmembrane (10) TRANSMEM 124 144 Helical. {ECO:0000255}.; TRANSMEM 170 190 Helical. {ECO:0000255}.; TRANSMEM 216 236 Helical. {ECO:0000255}.; TRANSMEM 261 281 Helical. {ECO:0000255}.; TRANSMEM 301 321 Helical. {ECO:0000255}.; TRANSMEM 353 373 Helical. {ECO:0000255}.; TRANSMEM 659 679 Helical. {ECO:0000255}.; TRANSMEM 713 733 Helical. {ECO:0000255}.; TRANSMEM 735 755 Helical. {ECO:0000255}.; TRANSMEM 774 794 Helical. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Transfers mannosyl residues to the hydroxyl group of serine or threonine residues. Coexpression of both POMT1 and POMT2 is necessary for enzyme activity, expression of either POMT1 or POMT2 alone is insufficient. Essentially dedicated to O-mannosylation of alpha-DAG1 and few other proteins but not of cadherins and protocaherins. {ECO:0000250|UniProtKB:Q9UKY4}. PTM: N-glycosylated. {ECO:0000269|PubMed:12460945}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. Highly expressed in the acrosome of cap phase spermatids, in spermatocytes and liver. Isoform 1 seems to be testis-specific. {ECO:0000269|PubMed:12460945}. +Q6P3Y9 PONL1_MOUSE Podocan-like protein 1 559 62,519 Chain (1); Erroneous termination (1); Glycosylation (1); Repeat (20); Sequence conflict (5); Signal peptide (1) PTM: N-glycosylated. {ECO:0000269|PubMed:21672516}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:21672516}. TISSUE SPECIFICITY: Detected in bone where it is expressed in osteoblasts and newly formed bone matrix (at protein level). Also expressed weakly in osteoclasts (at protein level). Expressed strongly in calvaria, lung and femur, and weakly in kidney. {ECO:0000269|PubMed:21672516}. +Q9QXP0 RHCG_MOUSE Ammonium transporter Rh type C (Rhesus blood group family type C glycoprotein) (Rh family type C glycoprotein) (Rh type C glycoprotein) (Rhesus blood group-associated C glycoprotein) (Rhesus-associated C glycoprotein) 498 54,972 Chain (1); Glycosylation (1); Sequence conflict (3); Topological domain (13); Transmembrane (12) TRANSMEM 10 30 Helical. {ECO:0000255}.; TRANSMEM 62 82 Helical. {ECO:0000255}.; TRANSMEM 87 107 Helical. {ECO:0000255}.; TRANSMEM 125 145 Helical. {ECO:0000255}.; TRANSMEM 154 174 Helical. {ECO:0000255}.; TRANSMEM 180 200 Helical. {ECO:0000255}.; TRANSMEM 220 240 Helical. {ECO:0000255}.; TRANSMEM 252 272 Helical. {ECO:0000255}.; TRANSMEM 280 302 Helical. {ECO:0000255}.; TRANSMEM 305 325 Helical. {ECO:0000255}.; TRANSMEM 341 361 Helical. {ECO:0000255}.; TRANSMEM 396 416 Helical. {ECO:0000255}. TOPO_DOM 1 9 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 31 61 Extracellular. {ECO:0000255}.; TOPO_DOM 83 86 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 108 124 Extracellular. {ECO:0000255}.; TOPO_DOM 146 153 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 175 179 Extracellular. {ECO:0000255}.; TOPO_DOM 201 219 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 241 251 Extracellular. {ECO:0000255}.; TOPO_DOM 273 279 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 303 304 Extracellular. {ECO:0000255}.; TOPO_DOM 326 340 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 362 395 Extracellular. {ECO:0000255}.; TOPO_DOM 417 498 Cytoplasmic. {ECO:0000255}. FUNCTION: Functions as an electroneutral and bidirectional ammonium transporter. May regulate transepithelial ammonia secretion. {ECO:0000269|PubMed:16131648}. PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:12388412, ECO:0000269|PubMed:15576624}; Multi-pass membrane protein {ECO:0000269|PubMed:12388412, ECO:0000269|PubMed:15576624}. Note=Also detected at the basolateral membrane and in subapical vesicles. {ECO:0000250}. SUBUNIT: Homotrimer. TISSUE SPECIFICITY: Expressed in the forestomach and the fundus of the stomach. Expressed at the level of villous in duodenum, jejunum, ileum and colon. Expressed in kidney by connecting segments and collecting tubules (at protein level). Expressed in testis by seminiferous tubules. {ECO:0000269|PubMed:10852913, ECO:0000269|PubMed:12388412, ECO:0000269|PubMed:15576624}. +P51175 PPOX_MOUSE Protoporphyrinogen oxidase (PPO) (EC 1.3.3.4) 477 50,871 Binding site (3); Chain (1); Nucleotide binding (4); Sequence conflict (5) Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1. FUNCTION: Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX. {ECO:0000269|PubMed:8554330}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:3346226}; Peripheral membrane protein {ECO:0000269|PubMed:3346226}; Intermembrane side {ECO:0000269|PubMed:3346226}. SUBUNIT: Monomer. Homodimer (By similarity). {ECO:0000250}. +Q68FM6 PPR29_MOUSE Protein phosphatase 1 regulatory subunit 29 (Extracellular leucine-rich repeat and fibronectin type III domain-containing protein 2) (Leucine-rich repeat and fibronectin type-III domain-containing protein 6) (Leucine-rich repeat-containing protein 62) 823 90,029 Chain (1); Compositional bias (2); Domain (2); Glycosylation (6); Modified residue (3); Repeat (5); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 398 418 Helical. {ECO:0000255}. TOPO_DOM 23 397 Extracellular. {ECO:0000255}.; TOPO_DOM 419 823 Cytoplasmic. {ECO:0000255}. FUNCTION: Inhibits phosphatase activity of protein phosphatase 1 (PP1) complexes. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. SUBUNIT: Interacts with PPP1CA. {ECO:0000250}. +Q60829 PPR1B_MOUSE Protein phosphatase 1 regulatory subunit 1B (DARPP-32) (Dopamine- and cAMP-regulated neuronal phosphoprotein) 194 21,781 Alternative sequence (1); Chain (1); Modified residue (8) FUNCTION: Inhibitor of protein-phosphatase 1. PTM: Dopamine- and cyclic AMP-regulated neuronal phosphoprotein. {ECO:0000250}.; PTM: Phosphorylation of Thr-34 is required for activity. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. +Q9D8C8 PPR35_MOUSE Protein phosphatase 1 regulatory subunit 35 260 28,355 Chain (1); Compositional bias (1); Modified residue (2) FUNCTION: Inhibits PPP1CA phosphatase activity. {ECO:0000250}. SUBUNIT: Interacts with PPP1CA. {ECO:0000250}. +Q99MR9 PPR3A_MOUSE Protein phosphatase 1 regulatory subunit 3A (Protein phosphatase 1 glycogen-associated regulatory subunit) (Protein phosphatase type-1 glycogen targeting subunit) (RG1) 1089 121,435 Chain (1); Domain (1); Modified residue (7); Motif (1); Sequence conflict (1); Transmembrane (1) TRANSMEM 1047 1067 Helical. {ECO:0000255}. FUNCTION: Seems to act as a glycogen-targeting subunit for PP1. PP1 is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Plays an important role in glycogen synthesis but is not essential for insulin activation of glycogen synthase. {ECO:0000269|PubMed:11283248}. PTM: Phosphorylation at Ser-48 by ISPK stimulates the dephosphorylation of glycogen synthase and phosphorylase kinase. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with PPP1CC catalytic subunit of PP1, and associates with glycogen. {ECO:0000250}. DOMAIN: The CBM21 domain is known to be involved in the localization to glycogen and is characteristic of some regulatory subunit of phosphatase complexes. TISSUE SPECIFICITY: Skeletal muscle and heart. {ECO:0000269|PubMed:11361130}. +Q6NVE9 PPTC7_MOUSE Protein phosphatase PTC7 homolog (EC 3.1.3.16) (T-cell activation protein phosphatase 2C) (TA-PP2C) 310 33,048 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (1); Metal binding (4) +Q8CEC6 PPWD1_MOUSE Peptidylprolyl isomerase domain and WD repeat-containing protein 1 (EC 5.2.1.8) 646 73,385 Chain (1); Compositional bias (1); Domain (1); Initiator methionine (1); Modified residue (1); Repeat (4); Sequence conflict (5) FUNCTION: PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. May be involved in pre-mRNA splicing. {ECO:0000250|UniProtKB:Q96BP3}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96BP3}. Note=Associated with spliceosomal complexes. {ECO:0000250, ECO:0000250|UniProtKB:Q96BP3}. SUBUNIT: Identified in the spliceosome C complex. {ECO:0000250|UniProtKB:Q96BP3}. +O88531 PPT1_MOUSE Palmitoyl-protein thioesterase 1 (PPT-1) (EC 3.1.2.22) (Palmitoyl-protein hydrolase 1) 306 34,490 Active site (3); Chain (1); Disulfide bond (3); Erroneous initiation (1); Glycosylation (3); Sequence conflict (7); Signal peptide (1) FUNCTION: Removes thioester-linked fatty acyl groups such as palmitate from modified cysteine residues in proteins or peptides during lysosomal degradation. Prefers acyl chain lengths of 14 to 18 carbons. {ECO:0000250|UniProtKB:P45478}. PTM: Glycosylated. {ECO:0000269|PubMed:9685319}. SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:19941651, ECO:0000269|PubMed:9685319}. Secreted {ECO:0000269|PubMed:9685319}. SUBUNIT: Interacts with CLN5, ATP5F1A and ATP5F1B (PubMed:19941651). {ECO:0000269|PubMed:19941651}. TISSUE SPECIFICITY: Highest level in testis and kidney, lower in heart, brain and lung and lowest in skeletal muscle. {ECO:0000269|PubMed:10231585, ECO:0000269|PubMed:9685319}. +Q91VJ5 PQBP1_MOUSE Polyglutamine-binding protein 1 (PQBP-1) (38 kDa nuclear protein containing a WW domain) (Npw38) (Polyglutamine tract-binding protein 1) 263 30,597 Chain (1); Domain (1); Modified residue (1); Region (5); Repeat (14); Sequence conflict (5) FUNCTION: Intrinsically disordered protein that acts as a scaffold, and which is involved in different processes, such as pre-mRNA splicing, transcription regulation, innate immunity and neuron development (By similarity). Interacts with splicing-related factors via the intrinsically disordered region and regulates alternative splicing of target pre-mRNA species (PubMed:23512658). May suppress the ability of POU3F2 to transactivate the DRD1 gene in a POU3F2 dependent manner (By similarity). Can activate transcription directly or via association with the transcription machinery (By similarity). May be involved in ATXN1 mutant-induced cell death (By similarity). The interaction with ATXN1 mutant reduces levels of phosphorylated RNA polymerase II large subunit (By similarity). Involved in the assembly of cytoplasmic stress granule, possibly by participating to the transport of neuronal RNA granules (By similarity). Also acts as an innate immune sensor of infection by retroviruses, by detecting the presence of reverse-transcribed DNA in the cytosol (By similarity). Directly binds retroviral reverse-transcribed DNA in the cytosol and interacts with CGAS, leading to activate the cGAS-STING signaling pathway, triggering type-I interferon production (By similarity). {ECO:0000250|UniProtKB:O60828, ECO:0000269|PubMed:23512658}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23512658}. Nucleus speckle {ECO:0000269|PubMed:23512658}. Cytoplasmic granule {ECO:0000250|UniProtKB:O60828}. Note=Colocalizes with SRSF2 in nuclear speckles (PubMed:23512658). Colocalized with POU3F2. Colocalized with ATXN1 in nuclear inclusion bodies. Localizes to cytoplasmic stress granules (By similarity). {ECO:0000250|UniProtKB:O60828, ECO:0000269|PubMed:23512658}. SUBUNIT: Interacts with POU3F2/Brn-2, ATXN1, TXNL4A, HTT and AR. Interaction with ATXN1 correlates positively with the length of the polyglutamine tract. Interacts with RNA polymerase II large subunit in a phosphorylation-dependent manner. Forms a ternary complex with ATXN1 mutant and phosphorylated RNA polymerase II. Interacts (via C-terminus) with TXNL4A and CD2BP2. Interacts (via WW domain) with ATN1 and SF3B1, and may interact with additional splice factors. Interacts (via WW domain) with WBP11; Leading to reduce interaction between PQBP1 and TXNL4A. Interacts with CAPRIN1. Interacts with DDX1. Interacts with SFPQ. Interacts with KHSRP. {ECO:0000250|UniProtKB:O60828}. DOMAIN: The WW domain may play a role as a transcriptional activator directly or via association with the transcription machinery. The WW domain mediates interaction with WBP11, ATN1, SF3B1 and the C-terminal domain of the RNA polymerase II large subunit. {ECO:0000250|UniProtKB:O60828}.; DOMAIN: Except for the WW domain, the protein is intrinsically disordered. {ECO:0000250|UniProtKB:O60828}. TISSUE SPECIFICITY: Detected in brain cortex and hippocampus neurons (at protein level). Expressed in brain with high level in cerebellar cortex, hippocampus and olfactory bulb. {ECO:0000269|PubMed:10332029, ECO:0000269|PubMed:23512658}. +Q80XM9 PQLC1_MOUSE PQ-loop repeat-containing protein 1 271 30,580 Alternative sequence (4); Chain (1); Domain (2); Frameshift (1); Modified residue (1); Sequence conflict (5); Transmembrane (6) TRANSMEM 7 27 Helical. {ECO:0000255}.; TRANSMEM 49 69 Helical. {ECO:0000255}.; TRANSMEM 72 92 Helical. {ECO:0000255}.; TRANSMEM 145 165 Helical. {ECO:0000255}.; TRANSMEM 168 188 Helical. {ECO:0000255}.; TRANSMEM 232 252 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8CGZ9 PR7B1_MOUSE Prolactin-7B1 (Placental prolactin-like protein N) (PLP-N) (PRL-like protein N) 251 28,960 Chain (1); Disulfide bond (2); Glycosylation (2); Sequence conflict (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000250}. TISSUE SPECIFICITY: Expression restricted to placenta. Abundantly expressed in trophoblast cells of the junctional zone and trophoblasts migrating into the mesometrial decidua. {ECO:0000269|PubMed:12488360}. +P17564 PR15A_MOUSE Protein phosphatase 1 regulatory subunit 15A (Growth arrest and DNA damage-inducible protein GADD34) (Myeloid differentiation primary response protein MyD116) 657 71,840 Alternative sequence (1); Chain (1); Compositional bias (1); Intramembrane (1); Modified residue (4); Mutagenesis (1); Region (5); Repeat (5); Sequence conflict (3); Topological domain (2) INTRAMEM 22 39 Helical. {ECO:0000250|UniProtKB:O75807}. TOPO_DOM 1 21 Cytoplasmic. {ECO:0000250|UniProtKB:O75807}.; TOPO_DOM 40 657 Cytoplasmic. {ECO:0000250|UniProtKB:O75807}. FUNCTION: Recruits the serine/threonine-protein phosphatase PP1 to dephosphorylate the translation initiation factor eIF-2A/EIF2S1, thereby reversing the shut-off of protein synthesis initiated by stress-inducible kinases and facilitating recovery of cells from stress. Down-regulates the TGF-beta signaling pathway by promoting dephosphorylation of TGFB1 by PP1. May promote apoptosis by inducing TP53 phosphorylation on 'Ser-15'. In case of infection with vesicular stomatitis virus (VSV), impairs viral replication. {ECO:0000269|PubMed:11381086, ECO:0000269|PubMed:12606582, ECO:0000269|PubMed:12824288, ECO:0000269|PubMed:16478986, ECO:0000269|PubMed:17670836}. PTM: Phosphorylated at multiple Ser/Thr residues. Phosphorylated on tyrosine by LYN; which impairs its antiproliferative activity. Phosphorylation at Tyr-239 enhances proteasomal degradation, this position is dephosphorylated by PTPN2. {ECO:0000250|UniProtKB:O75807}.; PTM: Polyubiquitinated. Exhibits a rapid proteasomal degradation with a half-life under 1 hour, ubiquitination depends on endoplasmic reticulum association. {ECO:0000250|UniProtKB:O75807}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side {ECO:0000250|UniProtKB:O75807}. Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side {ECO:0000250|UniProtKB:O75807}. Note=Associates with membranes via an N-terminal amphipathic intramembrane region. {ECO:0000250|UniProtKB:O75807}. SUBUNIT: Interacts with KMT2A/MLL1. Interacts with SMARCB1. Interacts with SMAD7. Interacts with BAG1 (By similarity). Interacts with PCNA. Interacts with LYN. Interacts with PP1 and PPP1R1A. {ECO:0000250, ECO:0000269|PubMed:11381086, ECO:0000269|PubMed:11517336, ECO:0000269|PubMed:9023344, ECO:0000269|PubMed:9371605}. TISSUE SPECIFICITY: Expressed strongly in spleen and lung, moderately in thymus and muscle, and weakly in brain. {ECO:0000269|PubMed:12824288}. +Q4FK66 PR38A_MOUSE Pre-mRNA-splicing factor 38A 312 37,437 Alternative sequence (3); Chain (1); Coiled coil (1); Compositional bias (1); Modified residue (5); Region (1); Sequence conflict (1) FUNCTION: Involved in pre-mRNA splicing as a component of the spliceosome. {ECO:0000250|UniProtKB:Q8NAV1}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8NAV1}. SUBUNIT: Component of the spliceosome B complex. Interacts (via N-terminal interaction domain) with ZMAT2 AND MFAP1. {ECO:0000250|UniProtKB:Q8NAV1}. +P09586 PR3B1_MOUSE Prolactin-3B1 (Chorionic somatomammotropin hormone 2) (Placental lactogen II) (PL-II) 222 25,159 Chain (1); Disulfide bond (2); Sequence conflict (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted. +A2AJ77 PRD12_MOUSE PR domain zinc finger protein 12 (EC 2.1.1.-) (PR domain-containing protein 12) 365 40,303 Chain (1); Compositional bias (1); Domain (1); Zinc finger (3) FUNCTION: Involved in the positive regulation of histone H3-K9 dimethylation. {ECO:0000269|PubMed:26005867}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H4Q4}. +E9Q8T2 PRD15_MOUSE PR domain zinc finger protein 15 (EC 2.1.1.-) (PR domain-containing protein 15) 1174 132,870 Alternative sequence (1); Chain (1); Cross-link (1); Domain (1); Sequence conflict (2); Zinc finger (15) FUNCTION: Sequence-specific DNA-binding transcriptional regulator. Plays a role as a molecular node in a transcriptional network regulating embryonic development and cell fate decision. Stimulates the expression of upstream key transcriptional activators and repressors of the Wnt/beta-catenin and MAPK/ERK pathways, respectively, that are essential for naive pluripotency and self-renewal maintenance of embryonic stem cells (ESCs). Specifically promotes SPRY1 and RSPO1 transcription activation through recognition and direct binding of a specific DNA sequence in their promoter regions. Plays also a role in induced pluripotent stem cells (iPSCs) reprogramming. Involved in early embryo development. {ECO:0000269|PubMed:28740264}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28740264}. TISSUE SPECIFICITY: Expressed in embryonic stem cells (ESCs) (at protein level). {ECO:0000269|PubMed:28740264}. +Q3LAC4 PREX2_MOUSE Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 2 protein (P-Rex2) (PtdIns(3,4,5)-dependent Rac exchanger 2) (DEP domain-containing protein 2) 1598 181,717 Alternative sequence (2); Chain (1); Domain (6); Erroneous initiation (1); Frameshift (1); Sequence conflict (2) FUNCTION: Functions as a RAC1 guanine nucleotide exchange factor (GEF), activating Rac proteins by exchanging bound GDP for free GTP. Its activity is synergistically activated by phosphatidylinositol 3,4,5-trisphosphate and the beta gamma subunits of heterotrimeric G protein. Mediates the activation of RAC1 in a PI3K-dependent manner. May be an important mediator of Rac signaling, acting directly downstream of both G protein-coupled receptors and phosphoinositide 3-kinase (By similarity). {ECO:0000250}. SUBUNIT: Interacts with RAC1. {ECO:0000250}. DOMAIN: PH domain confers substrate specificity and recognition. Able to discriminate between RAC1, RHOA, and CDC42 (By similarity). {ECO:0000250}.; DOMAIN: DH domain alone was unable to confer substrate specificity and recognition. {ECO:0000250}. +Q3U5C7 PRIC1_MOUSE Prickle-like protein 1 832 94,131 Chain (1); Compositional bias (1); Domain (4); Lipidation (1); Modified residue (5); Propeptide (1) FUNCTION: Involved in the planar cell polarity pathway that controls convergent extension during gastrulation and neural tube closure (By similarity). Convergent extension is a complex morphogenetic process during which cells elongate, move mediolaterally, and intercalate between neighboring cells, leading to convergence toward the mediolateral axis and extension along the anteroposterior axis. Necessary for nuclear localization of REST. May serve as nuclear receptor (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Note=A smaller amount is detected in the cytosol. {ECO:0000250}. SUBUNIT: Interacts with REST. {ECO:0000250}. +Q9WVS6 PRKN_MOUSE E3 ubiquitin-protein ligase parkin (EC 2.3.2.31) (Parkin RBR E3 ubiquitin-protein ligase) 464 51,618 Active site (1); Alternative sequence (4); Beta strand (5); Chain (1); Domain (1); Helix (3); Metal binding (24); Modified residue (2); Region (4); Sequence conflict (2); Zinc finger (4) Protein modification; protein ubiquitination. FUNCTION: Functions within a multiprotein E3 ubiquitin ligase complex, catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins, such as BCL2, SYT11, CCNE1, GPR37, RHOT1/MIRO1, MFN1, MFN2, STUB1, SNCAIP, SEPT5, TOMM20, USP30, ZNF746 and AIMP2. Mediates monoubiquitination as well as 'Lys-6', 'Lys-11', 'Lys-48'-linked and 'Lys-63'-linked polyubiquitination of substrates depending on the context. Participates in the removal and/or detoxification of abnormally folded or damaged protein by mediating 'Lys-63'-linked polyubiquitination of misfolded proteins such as PARK7: 'Lys-63'-linked polyubiquitinated misfolded proteins are then recognized by HDAC6, leading to their recruitment to aggresomes, followed by degradation. Mediates 'Lys-63'-linked polyubiquitination of a 22 kDa O-linked glycosylated isoform of SNCAIP, possibly playing a role in Lewy-body formation. Mediates monoubiquitination of BCL2, thereby acting as a positive regulator of autophagy. Promotes the autophagic degradation of dysfunctional depolarized mitochondria (mitophagy) by promoting the ubiquitination of mitochondrial proteins such as TOMM20, RHOT1/MIRO1 and USP30. Preferentially assembles 'Lys-6'-, 'Lys-11'- and 'Lys-63'-linked polyubiquitin chains following mitochondrial damage, leading to mitophagy. Mediates 'Lys-48'-linked polyubiquitination of ZNF746, followed by degradation of ZNF746 by the proteasome; possibly playing a role in the regulation of neuron death. Limits the production of reactive oxygen species (ROS). Regulates cyclin-E during neuronal apoptosis. In collaboration with CHPF isoform 2, may enhance cell viability and protect cells from oxidative stress. Independently of its ubiquitin ligase activity, protects from apoptosis by the transcriptional repression of p53/TP53. May protect neurons against alpha synuclein toxicity, proteasomal dysfunction, GPR37 accumulation, and kainate-induced excitotoxicity. May play a role in controlling neurotransmitter trafficking at the presynaptic terminal and in calcium-dependent exocytosis. May represent a tumor suppressor gene. {ECO:0000250|UniProtKB:O60260, ECO:0000269|PubMed:15105460, ECO:0000269|PubMed:19801972, ECO:0000269|PubMed:22082830}. PTM: Auto-ubiquitinates in an E2-dependent manner leading to its own degradation. Also polyubiquitinated by RNF41 for proteasomal degradation. {ECO:0000250}.; PTM: S-nitrosylated. {ECO:0000269|PubMed:15105460}.; PTM: Phosphorylation at Ser-65 by PINK1 contributes to activate PRKN activity. It is however not sufficient and requires binding to phosphorylated ubiquitin as well. {ECO:0000250|UniProtKB:O60260}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Cytoplasm, cytosol {ECO:0000305|PubMed:10818204, ECO:0000305|PubMed:11122330}. Cell projection, dendrite {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250}. Mitochondrion {ECO:0000250}. Cell junction, synapse {ECO:0000250}. Note=Mainly localizes in the cytosol. Expressed in the endoplasmic reticulum, dendrites, some presynaptic terminals and in postsynaptic densities. Relocates to dysfunctional mitochondria that have lost the mitochondrial membrane potential; recruitment to mitochondria is PINK1-dependent (By similarity). {ECO:0000250}. SUBUNIT: Forms an E3 ubiquitin ligase complex with UBE2L3 or UBE2L6. Mediates 'Lys-63'-linked polyubiquitination by associating with UBE2V1. Part of a SCF-like complex, consisting of PRKN, CUL1 and FBXW7. Interacts with FBXO7; this promotes translocation to dysfunctional depolarized mitochondria (By similarity). Interacts with SNCAIP. Binds to the C2A and C2B domains of SYT11. Interacts and regulates the turnover of SEPT5. Part of a complex, including STUB1, HSP70 and GPR37. The amount of STUB1 in the complex increases during ER stress. STUB1 promotes the dissociation of HSP70 from PRKN and GPR37, thus facilitating PRKN-mediated GPR37 ubiquitination. HSP70 transiently associates with unfolded GPR37 and inhibits the E3 activity of PRKN, whereas, STUB1 enhances the E3 activity of PRKN through promotion of dissociation of HSP70 from PRKN-GPR37 complexes. Interacts with PSMD4 and PACRG. Interacts with LRKK2. Interacts with RANBP2. Interacts with SUMO1 but not SUMO2, which promotes nuclear localization and autoubiquitination. Interacts (via first RING-type domain) with AIMP2 (via N-terminus). Interacts with PSMA7 and RNF41. Interacts with PINK1. Interacts with CHPF, the interaction may facilitate PRKN transport into the mitochondria. Interacts with MFN2 (phosphorylated), promotes PRKN localization in dysfunctional depolarized mitochondria. Interacts with heat shock protein 70 family members, including HSPA1L, HSPA1A and HSPA8; interaction HSPA1L promotes translocation to damaged mitochondria (By similarity). Interacts with BAG4 and, to a lesser extent, BAG5; interaction with BAG4 inhibits translocation to damaged mitochondria. Interacts (when phosphorylated at Ser-65) with ubiquitin (phosphorylated); binding to phosphorylated ubiquitin is required to activate PRKN. Forms a complex with PINK1 and PARK7 (By similarity). {ECO:0000250|UniProtKB:O60260}. DOMAIN: The ubiquitin-like domain binds the PSMD4 subunit of 26S proteasomes. {ECO:0000250}.; DOMAIN: The RING-type 1 zinc finger domain is required to repress p53/TP53 transcription. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in all subdivisions of the brain. Highly expressed in brainstem, cranial nerve, pontine, cerebellar nuclei, indusium griseum, nuclei reticularis, strata oriens and laccunosum moleculare of the hippocampal CA2 region. Low levels were found in the telencephalon and diencephalon. Expressed in heart, liver, skeletal muscle, kidney and testis. {ECO:0000269|PubMed:10818204, ECO:0000269|PubMed:11122330, ECO:0000269|PubMed:11675120}. +Q9QUG3 PRND_MOUSE Prion-like protein doppel (Doppelganger) (Dpl) (PrPLP) 179 20,442 Beta strand (2); Chain (1); Disulfide bond (2); Glycosylation (2); Helix (6); Lipidation (1); Propeptide (1); Region (3); Sequence conflict (1); Signal peptide (1); Turn (1) FUNCTION: Required for normal acrosome reaction and for normal male fertility (PubMed:12110578, PubMed:15161660, PubMed:15007175). Can bind Cu(2+) (By similarity). {ECO:0000250|UniProtKB:Q9UKY0, ECO:0000269|PubMed:12110578, ECO:0000269|PubMed:15007175, ECO:0000269|PubMed:15161660}. PTM: N-glycosylated (PubMed:10525406, PubMed:10842180). N-glycosylated at two distinct sites (PubMed:10842180). {ECO:0000269|PubMed:10525406, ECO:0000269|PubMed:10842180}.; PTM: O-glycosylated. {ECO:0000250|UniProtKB:Q9UKY0}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10842180}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:10842180}. DOMAIN: A short helical region is required and sufficient for Cu(2+) binding. {ECO:0000250|UniProtKB:Q9UKY0}. TISSUE SPECIFICITY: Detected in testis (PubMed:10842180, PubMed:12110578, PubMed:15161660). Detected within seminiferous tubules, on round and elongated spermatids (at protein level) (PubMed:12110578). Not detected in brain (at protein level) (PubMed:10842180, PubMed:15161660). Detected in testis, and at low levels in heart (PubMed:10525406, PubMed:12110578). Expression in brain is very low and barely detectable (PubMed:10525406). {ECO:0000269|PubMed:10525406, ECO:0000269|PubMed:10842180, ECO:0000269|PubMed:12110578, ECO:0000269|PubMed:15161660}. +Q9CQW3 PROZ_MOUSE Vitamin K-dependent protein Z 399 44,304 Chain (1); Disulfide bond (9); Domain (4); Glycosylation (4); Modified residue (12); Propeptide (1); Signal peptide (1) FUNCTION: Appears to assist hemostasis by binding thrombin and promoting its association with phospholipid vesicles. Inhibits activity of the coagulation protease factor Xa in the presence of SERPINA10, calcium and phospholipids (By similarity). {ECO:0000250}. PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Plasma. +O54990 PROM1_MOUSE Prominin-1 (Antigen AC133 homolog) (Prominin-like protein 1) (CD antigen CD133) 867 97,113 Alternative sequence (7); Chain (1); Glycosylation (8); Modified residue (4); Sequence conflict (18); Signal peptide (1); Topological domain (6); Transmembrane (5) TRANSMEM 108 128 Helical. {ECO:0000255}.; TRANSMEM 159 179 Helical. {ECO:0000255}.; TRANSMEM 435 455 Helical. {ECO:0000255}.; TRANSMEM 488 508 Helical. {ECO:0000255}.; TRANSMEM 795 815 Helical. {ECO:0000255}. TOPO_DOM 20 107 Extracellular. {ECO:0000255}.; TOPO_DOM 129 158 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 180 434 Extracellular. {ECO:0000255}.; TOPO_DOM 456 487 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 509 794 Extracellular. {ECO:0000255}.; TOPO_DOM 816 867 Cytoplasmic. {ECO:0000255}. FUNCTION: May play a role in cell differentiation, proliferation and apoptosis. Binds cholesterol in cholesterol-containing plasma membrane microdomains and may play a role in the organization of the apical plasma membrane in epithelial cells. During early retinal development acts as a key regulator of disk morphogenesis (PubMed:19228982). Involved in regulation of MAPK and Akt signaling pathways. In neuroblastoma cells suppresses cell differentiation such as neurite outgrowth in a RET-dependent manner. {ECO:0000269|PubMed:19228982}. PTM: Acetylation at Lys-226, Lys-258 and Lys-265 by NAT8 and NAT8B may control PROM1 protein expression and its function in cell apoptosis. SUBCELLULAR LOCATION: Apical cell membrane; Multi-pass membrane protein. Cell projection, microvillus membrane; Multi-pass membrane protein. Cell projection, cilium, photoreceptor outer segment. Endoplasmic reticulum {ECO:0000250}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250}. Note=Found in extracellular membrane particles in various body fluids such as ventricular fluid of the developing brain and urine. SUBUNIT: Interacts with CDHR1 and with actin filaments. Interacts with NAT8 and NAT8B (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: In the submandibular gland, expressed on the apical side of epithelial cells. In the parotid gland, expressed in the intercalated ducts. In the sublingual gland, expressed in intercalated ducts. In the extraorbital lacrimal gland, expressed in the intercalated tubules and larger intralobular ducts. Expressed in the retina. Present in urine within small membrane particles (at protein level). In the embryo, expressed on the apical side of neuroepithelial cells and of other epithelia such as lung buds, gut and ureter buds. In the adult, expressed at the apical side of the kidney tubules and of the ependymal layer of the brain. Not expressed in gut, liver, lung, pituitary, adrenal, heart or spleen. Localized to the nascent disk membranes at the base of the rod outer segment in the retina (at protein level). {ECO:0000269|PubMed:12514187, ECO:0000269|PubMed:17874118, ECO:0000269|PubMed:18654668, ECO:0000269|PubMed:19228982}. +Q8K2Z2 PRP39_MOUSE Pre-mRNA-processing factor 39 (PRP39 homolog) 665 77,921 Alternative sequence (1); Chain (1); Compositional bias (1); Erroneous initiation (1); Modified residue (1); Repeat (7) FUNCTION: Involved in pre-mRNA splicing. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +Q99PV0 PRP8_MOUSE Pre-mRNA-processing-splicing factor 8 (Splicing factor Prp8) 2335 273,616 Chain (1); Domain (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (5); Region (7); Sequence conflict (2) FUNCTION: Functions as a scaffold that mediates the ordered assembly of spliceosomal proteins and snRNAs. Required for the assembly of the U4/U6-U5 tri-snRNP complex. Functions as scaffold that positions spliceosomal U2, U5 and U6 snRNAs at splice sites on pre-mRNA substrates, so that splicing can occur. Interacts with both the 5' and the 3' splice site. {ECO:0000250|UniProtKB:Q6P2Q9}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:15169873}. SUBUNIT: Part of the U5 snRNP complex. Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39. Component of the U5.U4atac/U6atac snRNP complexes in U12-dependent spliceosomes. Found in a mRNA splicing-dependent exon junction complex (EJC) with SRRM1. Interacts with U5 snRNP proteins SNRP116 and SNRNP40. Interacts with EFTUD2 and SNRNP200. Interacts (via the MPN (JAB/Mov34) domain) with PRPF3 ('Lys-63'-linked polyubiquitinated); may stabilize the U4/U6-U5 tri-snRNP complex. Interacts (via RNase H homology domain) with AAR2. {ECO:0000250|UniProtKB:Q6P2Q9}. DOMAIN: The MPN (JAB/Mov34) domain has structural similarity with deubiquitinating enzymes, but lacks the residues that would bind the catalytic metal ion. {ECO:0000250}.; DOMAIN: Contains a region with structural similarity to reverse transcripase, presenting the classical thumb, fingers and palm architecture, but lacks enzyme activity, since the essential metal-binding residues are not conserved. {ECO:0000250}.; DOMAIN: Contains a region with structural similarity to type-2 restriction endonucleases, but the residues that would bind catalytic metal ions in endonucleases are instead involved in hydrogen bonds that stabilize the protein structure. {ECO:0000250}.; DOMAIN: Contains a region with structural similarity to RNase H, but lacks RNase H activity. {ECO:0000250}. TISSUE SPECIFICITY: Strongly expressed in testis (preferentially in the outer cell layer), and moderately in ovary (preferentially in granulosa cells). {ECO:0000269|PubMed:11275560}. +Q9DAW6 PRP4_MOUSE U4/U6 small nuclear ribonucleoprotein Prp4 (U4/U6 snRNP 60 kDa protein) (WD splicing factor Prp4) 521 58,370 Chain (1); Modified residue (1); Repeat (7) FUNCTION: Plays role in pre-mRNA splicing as component of the U4/U6-U5 tri-snRNP complex that is involved in spliceosome assembly, and as component of the precatalytic spliceosome (spliceosome B complex). {ECO:0000250|UniProtKB:O43172}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O43172}. Nucleus speckle {ECO:0000250|UniProtKB:O43172}. SUBUNIT: Component of the precatalytic spliceosome (spliceosome B complex). Component of the U4/U6-U5 tri-snRNP complex, a building block of the precatalytic spliceosome (spliceosome B complex). The U4/U6-U5 tri-snRNP complex is composed of the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39, plus LSM2, LSM3, LSM4, LSM5, LSM6, LSM7 and LSM8. Interacts directly with PRPF18, PPIH and PRPF3. Part of a heteromeric complex containing PPIH, PRPF3 and PRPF4 that is stable in the absence of RNA. {ECO:0000250|UniProtKB:O43172}. +E9PUL5 PRRT2_MOUSE Proline-rich transmembrane protein 2 (Dispanin subfamily B member 3) (DSPB3) 346 35,924 Chain (1); Compositional bias (1); Intramembrane (1); Modified residue (9); Topological domain (3); Transmembrane (1) INTRAMEM 275 295 Helical. {ECO:0000255, ECO:0000305|PubMed:26797119}. TRANSMEM 324 344 Helical. {ECO:0000255, ECO:0000305|PubMed:26797119}. TOPO_DOM 1 274 Cytoplasmic. {ECO:0000255, ECO:0000305|PubMed:26797119}.; TOPO_DOM 296 323 Cytoplasmic. {ECO:0000255, ECO:0000305|PubMed:26797119}.; TOPO_DOM 345 346 Extracellular. {ECO:0000255, ECO:0000305|PubMed:26797119}. FUNCTION: As a component of the outer core of AMPAR complex, may be involved in synaptic transmission in the central nervous system. In hippocampal neurons, in presynaptic terminals, plays an important role in the final steps of neurotransmitter release, possibly by regulating Ca(2+)-sensing (PubMed:27052163). In the cerebellum, may inhibit SNARE complex formation and downregulate short-term facilitation (PubMed:29056747). {ECO:0000269|PubMed:27052163, ECO:0000269|PubMed:29056747}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26797119, ECO:0000269|PubMed:27172900}. Cell junction, synapse, presynaptic cell membrane {ECO:0000269|PubMed:27052163, ECO:0000269|PubMed:29056747}. Cell junction, synapse {ECO:0000269|PubMed:27052163, ECO:0000269|PubMed:29056747, ECO:0000305|PubMed:22632720}. Cell projection, axon {ECO:0000269|PubMed:29056747}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:D3ZFB6}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250|UniProtKB:D3ZFB6}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:D3ZFB6}. SUBUNIT: Component of the outer core of AMPAR complex (PubMed:22632720, PubMed:25915028). AMPAR complex consists of an inner core made of 4 pore-forming GluA/GRIA proteins (GRIA1, GRIA2, GRIA3 and GRIA4) and 4 major auxiliary subunits arranged in a twofold symmetry. One of the two pairs of distinct binding sites is occupied either by CNIH2, CNIH3 or CACNG2, CACNG3. The other harbors CACNG2, CACNG3, CACNG4, CACNG8 or GSG1L. This inner core of AMPAR complex is complemented by outer core constituents binding directly to the GluA/GRIA proteins at sites distinct from the interaction sites of the inner core constituents. Outer core constituents include at least PRRT1, PRRT2, CKAMP44/SHISA9, FRRS1L and NRN1. The proteins of the inner and outer core serve as a platform for other, more peripherally associated AMPAR constituents. Alone or in combination, these auxiliary subunits control the gating and pharmacology of the AMPAR complex and profoundly impact their biogenesis and protein processing (PubMed:22632720). Interacts with intersectin 1/ITSN1 (PubMed:26797119). Interacts with SNARE complex components, including SNAP25, STX1A, SYT1 and SYT2; this interaction may inhibit SNARE complex formation (PubMed:22832103, PubMed:27052163, PubMed:29056747). {ECO:0000269|PubMed:22632720, ECO:0000269|PubMed:22832103, ECO:0000269|PubMed:25915028, ECO:0000269|PubMed:26797119, ECO:0000269|PubMed:27052163, ECO:0000269|PubMed:29056747}. TISSUE SPECIFICITY: Neuron-specific expression throughout the brain, with the highest levels in the cerebellum, basal ganglia, hippocampus, substantia nigra, and neocortex (at protein level) (PubMed:22101681, PubMed:22243967, PubMed:22832103, PubMed:22632720, PubMed:25915028, PubMed:27052163, PubMed:27172900, PubMed:28007585, PubMed:29056747). Highly expressed also in spinal cord (at protein level) (PubMed:22101681, PubMed:22832103). Detected at very low levels in the heart, lung, kidney and skin (PubMed:22101681). {ECO:0000269|PubMed:22101681, ECO:0000269|PubMed:22243967, ECO:0000269|PubMed:22632720, ECO:0000269|PubMed:22832103, ECO:0000269|PubMed:25915028, ECO:0000269|PubMed:27052163, ECO:0000269|PubMed:27172900, ECO:0000269|PubMed:28007585, ECO:0000269|PubMed:29056747}. +Q8BHE0 PRR11_MOUSE Proline-rich protein 11 368 40,949 Chain (1); Compositional bias (1); Modified residue (5); Motif (4); Sequence conflict (2) FUNCTION: Plays a critical role in cell cycle progression. {ECO:0000250|UniProtKB:Q96HE9}. PTM: Ubiquitinated. Rapidly degraded by the proteasome; degradation may involve FBXW7-specific phosphorylated phosphodegron motifs. {ECO:0000250|UniProtKB:Q96HE9}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96HE9}. +P70195 PSB7_MOUSE Proteasome subunit beta type-7 (EC 3.4.25.1) (Macropain chain Z) (Multicatalytic endopeptidase complex chain Z) (Proteasome subunit Z) 277 29,891 Active site (1); Beta strand (12); Chain (1); Helix (4); Propeptide (1); Sequence conflict (2); Turn (1) FUNCTION: Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). Within the 20S core complex, PSMB7 displays a trypsin-like activity. {ECO:0000269|PubMed:16581775, ECO:0000269|PubMed:22341445}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q99436}. Nucleus {ECO:0000250|UniProtKB:Q99436}. SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is a barrel-shaped complex made of 28 subunits that are arranged in four stacked rings. The two outer rings are each formed by seven alpha subunits, and the two inner rings are formed by seven beta subunits. The proteolytic activity is exerted by three beta-subunits PSMB5, PSMB6 and PSMB7. {ECO:0000250|UniProtKB:Q99436, ECO:0000269|PubMed:16857966, ECO:0000269|PubMed:22341445}. +O35226 PSMD4_MOUSE 26S proteasome non-ATPase regulatory subunit 4 (26S proteasome regulatory subunit RPN10) (26S proteasome regulatory subunit S5A) (Multiubiquitin chain-binding protein) 376 40,704 Alternative sequence (7); Chain (1); Compositional bias (1); Cross-link (1); Domain (3); Modified residue (8); Region (1) FUNCTION: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. PSMD4 acts as an ubiquitin receptor subunit through ubiquitin-interacting motifs and selects ubiquitin-conjugates for destruction. Displays a preferred selectivity for longer polyubiquitin chains. {ECO:0000250|UniProtKB:P55036}. SUBUNIT: Component of the 19S proteasome regulatory particle complex. The 26S proteasome consists of a 20S core particle (CP) and two 19S regulatory subunits (RP). The regulatory particle is made of a lid composed of 9 subunits, a base containing 6 ATPases and few additional components including PSMD4 (PubMed:16857966). Interacts with NUB1. Interacts with SQSTM1. Interacts with UBQLN4. Interacts with UBE3A. Interacts with UBQLN1 (via ubiquitin-like domain). {ECO:0000250|UniProtKB:P55036, ECO:0000269|PubMed:16857966}. DOMAIN: The 2 UIM motifs are involved in the binding to a multi-ubiquitin chain in a cooperative way. {ECO:0000250}. TISSUE SPECIFICITY: Isoform Rpn10A is ubiquitous whereas isoform Rpn10E is mostly expressed in the embryonic brain. +P21841 PSPC_MOUSE Pulmonary surfactant-associated protein C (SP-C) (Pulmonary surfactant-associated proteolipid SPL(Val)) (SP5) 193 21,055 Chain (1); Disulfide bond (1); Domain (1); Lipidation (2); Propeptide (2) FUNCTION: Pulmonary surfactant associated proteins promote alveolar stability by lowering the surface tension at the air-liquid interface in the peripheral air spaces. SUBCELLULAR LOCATION: Secreted, extracellular space, surface film. +Q9JK23 PSMG1_MOUSE Proteasome assembly chaperone 1 (Down syndrome critical region protein 2 homolog) 289 33,104 Chain (1); Initiator methionine (1); Modified residue (5); Sequence conflict (2) FUNCTION: Chaperone protein which promotes assembly of the 20S proteasome as part of a heterodimer with PSMG2. The PSMG1-PSMG2 heterodimer binds to the PSMA5 and PSMA7 proteasome subunits, promotes assembly of the proteasome alpha subunits into the heteroheptameric alpha ring and prevents alpha ring dimerization (By similarity). {ECO:0000250|UniProtKB:O95456}. PTM: Degraded by the proteasome upon completion of 20S proteasome maturation. {ECO:0000250|UniProtKB:O95456}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O95456}. Endoplasmic reticulum {ECO:0000250|UniProtKB:O95456}. SUBUNIT: Forms a heterodimer with PSMG2. The PSMG1-PSMG2 heterodimer interacts directly with the PSMA5 and PSMA7 proteasome alpha subunits (By similarity). {ECO:0000250|UniProtKB:O95456}. TISSUE SPECIFICITY: Highly expressed in testis with moderate expression in brain, liver and kidney and low levels in heart, skeletal muscle and pancreas. {ECO:0000269|PubMed:10872820}. +Q9EST4 PSMG2_MOUSE Proteasome assembly chaperone 2 (CD40 ligand-activated specific transcript 3) (Tumor necrosis factor superfamily member 5-induced protein 1) 264 29,524 Alternative sequence (3); Chain (1); Modified residue (1); Sequence conflict (1) FUNCTION: Chaperone protein which promotes assembly of the 20S proteasome as part of a heterodimer with PSMG1. The PSMG1-PSMG2 heterodimer binds to the PSMA5 and PSMA7 proteasome subunits, promotes assembly of the proteasome alpha subunits into the heteroheptameric alpha ring and prevents alpha ring dimerization (By similarity). {ECO:0000250|UniProtKB:Q969U7}. PTM: Degraded by the proteasome upon completion of 20S proteasome maturation. {ECO:0000250|UniProtKB:Q969U7}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12147697}. SUBUNIT: Forms a heterodimer with PSMG1. The PSMG1-PSMG2 heterodimer interacts directly with the PSMA5 and PSMA7 proteasome alpha subunits (By similarity). {ECO:0000250|UniProtKB:Q969U7}. +Q9D0P7 PSRC1_MOUSE Proline/serine-rich coiled-coil protein 1 329 34,707 Chain (1); Coiled coil (1); Compositional bias (1); Modified residue (6); Region (1); Repeat (5); Sequence conflict (2) FUNCTION: Required for normal progression through mitosis. Required for normal congress of chromosomes at the metaphase plate, and for normal rate of chromosomal segregation during anaphase. Plays a role in the regulation of mitotic spindle dynamics. Increases the rate of turnover of microtubules on metaphase spindles, and contributes to the generation of normal tension across sister kinetochores. Recruits KIF2A and ANKRD53 to the mitotic spindle and spindle poles. May participate in p53/TP53-regulated growth suppression (By similarity). {ECO:0000250|UniProtKB:Q6PGN9}. PTM: Phosphorylated during mitosis. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12427559}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:12427559}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. Note=Detected at the mitotic spindle and spindle poles. Diffusely distributed throughout the cell during interphase (By similarity). {ECO:0000250}. SUBUNIT: Interacts with APC2 (PubMed:17310996). Interacts with KIF2A (By similarity). Interacts with ANKRD53; recruits ANKRD53 to the spindle during mitosis (By similarity). {ECO:0000250|UniProtKB:Q6PGN9, ECO:0000269|PubMed:17310996}. TISSUE SPECIFICITY: Highly expressed in heart, brain and lung. Weaker expression in kidney and testis. {ECO:0000269|PubMed:10618717}. +P97371 PSME1_MOUSE Proteasome activator complex subunit 1 (11S regulator complex subunit alpha) (REG-alpha) (Activator of multicatalytic protease subunit 1) (Proteasome activator 28 subunit alpha) (PA28a) (PA28alpha) 249 28,673 Beta strand (1); Chain (1); Helix (9); Sequence conflict (4) FUNCTION: Implicated in immunoproteasome assembly and required for efficient antigen processing. The PA28 activator complex enhances the generation of class I binding peptides by altering the cleavage pattern of the proteasome. SUBUNIT: Heterodimer of PSME1 and PSME2, which forms a hexameric ring. PSME1 can form homoheptamers (By similarity). {ECO:0000250}. +O09114 PTGDS_MOUSE Prostaglandin-H2 D-isomerase (EC 5.3.99.2) (Glutathione-independent PGD synthase) (Lipocalin-type prostaglandin-D synthase) (Prostaglandin-D2 synthase) (L-PGDS) (PGD2 synthase) (PGDS2) 189 21,066 Active site (1); Alternative sequence (1); Beta strand (12); Chain (1); Disulfide bond (1); Frameshift (1); Glycosylation (2); Helix (4); Modified residue (1); Mutagenesis (4); Signal peptide (1); Turn (3) FUNCTION: Catalyzes the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation. Involved in a variety of CNS functions, such as sedation, NREM sleep and PGE2-induced allodynia, and may have an anti-apoptotic role in oligodendrocytes. Binds small non-substrate lipophilic molecules, including biliverdin, bilirubin, retinal, retinoic acid and thyroid hormone, and may act as a scavenger for harmful hydrophopic molecules and as a secretory retinoid and thyroid hormone transporter. Possibly involved in development and maintenance of the blood-brain, blood-retina, blood-aqueous humor and blood-testis barrier. It is likely to play important roles in both maturation and maintenance of the central nervous system and male reproductive system. {ECO:0000269|PubMed:10781097, ECO:0000269|PubMed:11751991, ECO:0000269|PubMed:12077186, ECO:0000269|PubMed:17715133, ECO:0000269|PubMed:19546224, ECO:0000269|PubMed:19833210, ECO:0000269|PubMed:8922532, ECO:0000269|PubMed:9892701}. SUBCELLULAR LOCATION: Rough endoplasmic reticulum {ECO:0000250}. Nucleus membrane {ECO:0000250}. Golgi apparatus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Secreted {ECO:0000250}. Note=Detected on rough endoplasmic reticulum of arachnoid and menigioma cells. Localized to the nuclear envelope, Golgi apparatus, secretory vesicles and spherical cytoplasmic structures in arachnoid trabecular cells, and to circular cytoplasmic structures in meningeal macrophages and perivascular microglial cells. In oligodendrocytes, localized to the rough endoplasmic reticulum and nuclear envelope. In retinal pigment epithelial cells, localized to distinct cytoplasmic domains including the perinuclear region. Also secreted (By similarity). {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. DOMAIN: Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior. {ECO:0000269|PubMed:17715133, ECO:0000269|PubMed:19546224, ECO:0000269|PubMed:19833210}. TISSUE SPECIFICITY: Abundant in the brain and CNS, where it is expressed in tissues of the blood-brain barrier and secreted into the cerebro-spinal fluid. In the male reproductive system, it is expressed in the testis, efferent ducts and epididymis, and is secreted into the seminal fluid. In the eye, it is expressed in the pigmented epithelium of the retina and the nonpigmented epithelium of the ciliary body, and secreted into the aqueous humor. Low levels detected in various tissue fluids such as serum, normal urine, ascitic fluid and tear fluid. Also found in a number of other organs including the ear, heart and lung. {ECO:0000269|PubMed:11105911, ECO:0000269|PubMed:11751991, ECO:0000269|PubMed:8922532, ECO:0000269|PubMed:9892701}. +O09167 RL21_MOUSE 60S ribosomal protein L21 160 18,562 Chain (1) FUNCTION: Component of the large ribosomal subunit. {ECO:0000250|UniProtKB:P46778}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P46778}. Cytoplasm {ECO:0000250|UniProtKB:P46778}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P49666}. Note=Detected on cytosolic polysomes (By similarity). Detected in ribosomes that are associated with the rough endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:P46778, ECO:0000250|UniProtKB:P49666}. SUBUNIT: Component of the large ribosomal subunit. {ECO:0000250|UniProtKB:P46778}. +Q8BKG3 PTK7_MOUSE Inactive tyrosine-protein kinase 7 (Protein chuzhoi) (Protein-tyrosine kinase 7) (Pseudo tyrosine kinase receptor 7) (Tyrosine-protein kinase-like 7) 1062 117,532 Chain (1); Disulfide bond (7); Domain (8); Erroneous initiation (1); Glycosylation (10); Modified residue (1); Region (1); Sequence conflict (1); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 697 717 Helical. {ECO:0000255}. TOPO_DOM 23 696 Extracellular. {ECO:0000255}.; TOPO_DOM 718 1062 Cytoplasmic. {ECO:0000255}. FUNCTION: Inactive tyrosine kinase involved in Wnt signaling pathway. Component of both the non-canonical (also known as the Wnt/planar cell polarity signaling) and the canonical Wnt signaling pathway. Functions in cell adhesion, cell migration, cell polarity, proliferation, actin cytoskeleton reorganization and apoptosis. Has a role in embryogenesis, epithelial tissue organization and angiogenesis. {ECO:0000269|PubMed:15229603, ECO:0000269|PubMed:19439496, ECO:0000269|PubMed:20704721}. PTM: MMP14 cleaves PTK7 between Pro-613 and Leu-614 generating an N-terminal soluble (70 kDa) fragment and a membrane C-terminal (50 kDa) fragment. Proteolysis by MMP14 regulates PTK7 function in non-canonical Wnt signaling pathway. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. Cell junction {ECO:0000250}. Note=Colocalizes with MMP14 at cell junctions. Also localizes at the leading edge of migrating cells. SUBUNIT: Interacts with CTNNB1. {ECO:0000250}. DOMAIN: The protein kinase domain is predicted to be catalytically inactive. TISSUE SPECIFICITY: Expressed at high levels in lung and un-pregnant uterus among adult tissues, and in the tail, limbs, somites, gut and craniofacial regions among embryonic tissues. {ECO:0000269|PubMed:15019986}. +Q8R4E6 PURG_MOUSE Purine-rich element-binding protein gamma 350 39,938 Alternative sequence (1); Chain (1); Compositional bias (1); DNA binding (1); Modified residue (3); Sequence conflict (1) SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. TISSUE SPECIFICITY: Isoform 1 is expressed in testis. Isoform 2 is expressed in blastocyst and kidney. {ECO:0000269|PubMed:12034829}. +Q99LL5 PWP1_MOUSE Periodic tryptophan protein 1 homolog 501 55,587 Chain (1); Modified residue (6); Repeat (5); Sequence conflict (1) FUNCTION: Chromatin-associated factor that regulates transcription (By similarity). Regulates Pol I-mediated rRNA biogenesis and, probably, Pol III-mediated transcription (By similarity). Regulates the epigenetic status of rDNA (By similarity). {ECO:0000250|UniProtKB:Q13610}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13610}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q13610}. Chromosome {ECO:0000250|UniProtKB:Q13610}. Note=Associates with chromatin regions of rDNA. {ECO:0000250|UniProtKB:Q13610}. SUBUNIT: Associates with the RNA polymerase (Pol I) complex. Interacts with POLR1E. {ECO:0000250|UniProtKB:Q13610}. +Q61144 PSN2_MOUSE Presenilin-2 (PS-2) (EC 3.4.23.-) [Cleaved into: Presenilin-2 NTF subunit; Presenilin-2 CTF subunit] 448 49,983 Active site (2); Alternative sequence (2); Chain (2); Intramembrane (1); Modified residue (4); Motif (1); Sequence conflict (6); Topological domain (10); Transmembrane (8) INTRAMEM 414 434 Helical. {ECO:0000255}. TRANSMEM 88 108 Helical. {ECO:0000255}.; TRANSMEM 139 159 Helical. {ECO:0000255}.; TRANSMEM 167 187 Helical. {ECO:0000255}.; TRANSMEM 201 221 Helical. {ECO:0000255}.; TRANSMEM 224 244 Helical. {ECO:0000255}.; TRANSMEM 250 270 Helical. {ECO:0000255}.; TRANSMEM 359 379 Helical. {ECO:0000255}.; TRANSMEM 389 409 Helical. {ECO:0000255}. TOPO_DOM 1 87 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 109 138 Lumenal. {ECO:0000255}.; TOPO_DOM 160 166 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 188 200 Lumenal. {ECO:0000255}.; TOPO_DOM 222 223 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 245 249 Lumenal. {ECO:0000255}.; TOPO_DOM 271 358 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 380 388 Lumenal. {ECO:0000255}.; TOPO_DOM 410 413 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 435 448 Cytoplasmic. {ECO:0000255}. FUNCTION: Probable catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (amyloid-beta precursor protein). Requires the other members of the gamma-secretase complex to have a protease activity. May play a role in intracellular signaling and gene expression or in linking chromatin to the nuclear membrane. May function in the cytoplasmic partitioning of proteins (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Homodimer. Component of the gamma-secretase complex, a complex composed of a presenilin homodimer (PSEN1 or PSEN2), nicastrin (NCSTN), APH1 (APH1A or APH1B) and PEN2. Such minimal complex is sufficient for secretase activity, although other components may exist. Interacts with DOCK3. Interacts with HERPUD1, FLNA, FLNB and PARL (By similarity). {ECO:0000250}. DOMAIN: The PAL motif is required for normal active site conformation. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in the liver. +P26516 PSMD7_MOUSE 26S proteasome non-ATPase regulatory subunit 7 (26S proteasome regulatory subunit RPN8) (26S proteasome regulatory subunit S12) (Mov34 protein) (Proteasome subunit p40) 321 36,540 Chain (1); Compositional bias (1); Cross-link (1); Domain (1); Modified residue (4) FUNCTION: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. {ECO:0000250|UniProtKB:P51665}. SUBUNIT: Component of the 19S proteasome regulatory particle complex. The 26S proteasome consists of a 20S core particle (CP) and two 19S regulatory subunits (RP). The regulatory particle is made of a lid composed of 9 subunits including PSMD7, a base containing 6 ATPases and few additional components. Within the complex, PSMD7 interacts with subunit PSMD4 through their respective MPN domain. Interacts with TRIM5. {ECO:0000250|UniProtKB:P51665}. DISEASE: Note=Disruption of the Mov-34 locus is a recessive embryonic lethal mutation. {ECO:0000305|PubMed:2209467}. +Q9D9A7 PTG3L_MOUSE Putative protein PTGES3L (Prostaglandin E synthase 3-like) 131 15,652 Alternative sequence (1); Chain (1); Domain (1) +Q9D7S7 RL22L_MOUSE 60S ribosomal protein L22-like 1 122 14,467 Alternative sequence (1); Chain (1); Modified residue (3) +P67984 RL22_MOUSE 60S ribosomal protein L22 (Heparin-binding protein HBp15) 128 14,759 Chain (1); Compositional bias (1); Modified residue (3) +P62751 RL23A_MOUSE 60S ribosomal protein L23a 156 17,695 Chain (1); Cross-link (1); Initiator methionine (1); Modified residue (5) FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. Binds a specific region on the 26S rRNA (By similarity). May promote p53/TP53 degradation possibly through the stimulation of MDM2-mediated TP53 polyubiquitination (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P62750}. PTM: N-terminus is methylated by METTL11A/NTM1. {ECO:0000269|PubMed:20668449}.; PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}. SUBUNIT: Interacts with LYAR and GNL2. Interacts with MDM2; this interaction may promote MDM2-mediated p53/TP53 polyubiquitination. {ECO:0000250|UniProtKB:P62750}. +P28063 PSB8_MOUSE Proteasome subunit beta type-8 (EC 3.4.25.1) (Low molecular mass protein 7) (Macropain subunit C13) (Multicatalytic endopeptidase complex subunit C13) (Proteasome component C13) (Proteasome subunit beta-5i) 276 30,260 Active site (1); Beta strand (13); Chain (1); Erroneous initiation (1); Helix (5); Natural variant (2); Propeptide (1); Sequence conflict (3); Site (1); Turn (1) FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processing to generate class I binding peptides. May be involved in the inflammatory response pathway. Required for adipocyte differentiation. {ECO:0000269|PubMed:21881205, ECO:0000269|PubMed:22341445, ECO:0000269|PubMed:8066463}. PTM: Autocleaved. The resulting N-terminal Thr residue of the mature subunit is responsible for the nucleophile proteolytic activity. {ECO:0000250|UniProtKB:O35955}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}. Nucleus {ECO:0000250}. SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel. Component of the immunoproteasome, where it displaces the equivalent housekeeping subunit PSMB5. Component of the spermatoproteasome, a form of the proteasome specifically found in testis. Directly interacts with POMP. Interacts with TAP1. {ECO:0000269|PubMed:16857966, ECO:0000269|PubMed:22341445, ECO:0000269|PubMed:23706739}. TISSUE SPECIFICITY: Detected in liver (at protein level). Expressed in spleen, thymus, lung, liver, heart and, at a very low level, in kidney. Not expressed in brain nor testis. {ECO:0000269|PubMed:22341445, ECO:0000269|PubMed:8406612}. +Q9CZH3 PSMG3_MOUSE Proteasome assembly chaperone 3 (PAC-3) (mPAC3) 122 13,331 Chain (1); Modified residue (1) FUNCTION: Chaperone protein which promotes assembly of the 20S proteasome. May cooperate with PSMG1-PSMG2 heterodimers to orchestrate the correct assembly of proteasomes. {ECO:0000269|PubMed:17707236}. SUBUNIT: Homodimer. Interacts directly with alpha and beta subunits of the 20S proteasome but dissociates before the formation of half-proteasomes, probably upon recruitment of POMP (By similarity). Interacts with PSMG4. {ECO:0000250, ECO:0000269|PubMed:17707236}. +Q8VDQ1 PTGR2_MOUSE Prostaglandin reductase 2 (PRG-2) (EC 1.3.1.48) (15-oxoprostaglandin 13-reductase) (Zinc-binding alcohol dehydrogenase domain-containing protein 1) 351 38,015 Alternative sequence (2); Beta strand (15); Binding site (4); Chain (1); Helix (18); Mutagenesis (1); Nucleotide binding (3); Region (2); Sequence conflict (12); Turn (1) FUNCTION: Functions as 15-oxo-prostaglandin 13-reductase and acts on 15-keto-PGE1, 15-keto-PGE2, 15-keto-PGE1-alpha and 15-keto-PGE2-alpha with highest activity towards 15-keto-PGE2. Overexpression represses transcriptional activity of PPARG and inhibits adipocyte differentiation. {ECO:0000269|PubMed:17449869}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000269|PubMed:15229897, ECO:0000269|PubMed:19000823}. TISSUE SPECIFICITY: Widely expressed with highest levels in adipose tissues. {ECO:0000269|PubMed:17449869}. +P41593 PTH1R_MOUSE Parathyroid hormone/parathyroid hormone-related peptide receptor (PTH/PTHrP type I receptor) (PTH/PTHr receptor) (Parathyroid hormone 1 receptor) (PTH1 receptor) 591 66,372 Chain (1); Disulfide bond (3); Glycosylation (4); Motif (1); Sequence conflict (3); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 189 212 Helical; Name=1. {ECO:0000255}.; TRANSMEM 220 239 Helical; Name=2. {ECO:0000255}.; TRANSMEM 283 306 Helical; Name=3. {ECO:0000255}.; TRANSMEM 321 342 Helical; Name=4. {ECO:0000255}.; TRANSMEM 362 382 Helical; Name=5. {ECO:0000255}.; TRANSMEM 410 428 Helical; Name=6. {ECO:0000255}.; TRANSMEM 441 463 Helical; Name=7. {ECO:0000255}. TOPO_DOM 27 188 Extracellular. {ECO:0000255}.; TOPO_DOM 213 219 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 240 282 Extracellular. {ECO:0000255}.; TOPO_DOM 307 320 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 343 361 Extracellular. {ECO:0000255}.; TOPO_DOM 383 409 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 429 440 Extracellular. {ECO:0000255}.; TOPO_DOM 464 591 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for parathyroid hormone and for parathyroid hormone-related peptide (PubMed:8197183). The activity of this receptor is mediated by G proteins which activate adenylyl cyclase and also a phosphatidylinositol-calcium second messenger system. {ECO:0000250|UniProtKB:Q03431, ECO:0000269|PubMed:8197183}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q03431}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8197183}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Interacts (via N-terminal extracellular domain) with PTHLH and PTH (PubMed:8197183). Homodimer in the absence of bound ligand. Peptide hormone binding leads to dissociation of the homodimer. {ECO:0000250|UniProtKB:Q03431, ECO:0000305|PubMed:8197183}. TISSUE SPECIFICITY: Detected in kidney. {ECO:0000269|PubMed:8197183}. +Q91V95 PTH2R_MOUSE Parathyroid hormone 2 receptor (PTH2 receptor) 546 61,908 Chain (1); Glycosylation (4); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 144 167 Helical; Name=1. {ECO:0000255}.; TRANSMEM 175 194 Helical; Name=2. {ECO:0000255}.; TRANSMEM 236 258 Helical; Name=3. {ECO:0000255}.; TRANSMEM 274 295 Helical; Name=4. {ECO:0000255}.; TRANSMEM 314 334 Helical; Name=5. {ECO:0000255}.; TRANSMEM 362 380 Helical; Name=6. {ECO:0000255}.; TRANSMEM 392 414 Helical; Name=7. {ECO:0000255}. TOPO_DOM 27 143 Extracellular. {ECO:0000255}.; TOPO_DOM 168 174 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 195 235 Extracellular. {ECO:0000255}.; TOPO_DOM 259 273 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 296 313 Extracellular. {ECO:0000255}.; TOPO_DOM 335 361 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 381 391 Extracellular. {ECO:0000255}.; TOPO_DOM 415 546 Cytoplasmic. {ECO:0000255}. FUNCTION: This is a specific receptor for parathyroid hormone. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. PTH2R may be responsible for PTH effects in a number of physiological systems. It may play a significant role in pancreatic function. PTH2R presence in neurons indicates that it may function as a neurotransmitter receptor (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBUNIT: Binds to TIPF39/TIP39. +Q811G0 PTHB1_MOUSE Protein PTHB1 (Bardet-Biedl syndrome 9 protein homolog) (Parathyroid hormone-responsive B1 gene protein homolog) 885 99,057 Alternative sequence (4); Chain (1); Erroneous initiation (1); Region (2); Sequence conflict (2); Site (1) FUNCTION: The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor, which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane and binds to RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the Rab8-GTP localizes to the cilium and promotes docking and fusion of carrier vesicles to the base of the ciliary membrane. Required for proper BBSome complex assembly and its ciliary localization (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell projection, cilium membrane {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000250}. SUBUNIT: Part of BBSome complex, that contains BBS1, BBS2, BBS4, BBS5, BBS7, BBS8/TTC8, BBS9 and BBIP10. Interacts with LZTL1; the interaction mediates the association of LZTL1 with the BBsome complex and regulates BBSome ciliary trafficking. {ECO:0000269|PubMed:22072986}. +Q9JI38 PUS3_MOUSE tRNA pseudouridine(38/39) synthase (EC 5.4.99.45) (tRNA pseudouridine synthase 3) (tRNA pseudouridylate synthase 3) (tRNA-uridine isomerase 3) 481 55,546 Active site (1); Binding site (1); Chain (1); Initiator methionine (1); Modified residue (1); Sequence conflict (2) FUNCTION: Formation of pseudouridine at position 39 in the anticodon stem and loop of transfer RNAs. Also acts on position 38, but much less efficiently. {ECO:0000269|PubMed:11027153}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q3U4I7 PYRD2_MOUSE Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 2 (EC 1.-.-.-) 581 62,940 Chain (1); Nucleotide binding (1); Sequence caution (1); Sequence conflict (3) FUNCTION: Probable oxidoreductase. {ECO:0000250}. +Q8BLY1 SMOC1_MOUSE SPARC-related modular calcium-binding protein 1 (SPARC-related gene protein) (Secreted modular calcium-binding protein 1) (SMOC-1) 463 51,076 Alternative sequence (1); Calcium binding (2); Chain (1); Disulfide bond (9); Domain (5); Glycosylation (2); Sequence conflict (1); Signal peptide (1) FUNCTION: Probable regulator of osteoblast differentiation. Plays essential roles in both eye and limb development. {ECO:0000269|PubMed:21194678, ECO:0000269|PubMed:21750680}. PTM: Glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000250}. Note=In or around the basement membrane. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed in many tissues with a strongest signal in ovary. +Q5RKS2 SMIM7_MOUSE Small integral membrane protein 7 75 8,555 Chain (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 54 74 Helical. {ECO:0000255}. TOPO_DOM 18 53 Extracellular. {ECO:0000255}.; TOPO_DOM 75 75 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q99K82 SMOX_MOUSE Spermine oxidase (EC 1.5.3.16) (Polyamine oxidase 1) (PAO-1) (PAOh1) 555 61,852 Alternative sequence (12); Chain (1); Mutagenesis (1) Amine and polyamine degradation; spermine degradation. FUNCTION: Flavoenzyme which catalyzes the oxidation of spermine to spermidine. Can also use N(1)-acetylspermine and spermidine as substrates, with different affinity depending on the isoform (isozyme) and on the experimental conditions. Plays an important role in the regulation of polyamine intracellular concentration and has the potential to act as a determinant of cellular sensitivity to the antitumor polyamine analogs. May contribute to beta-alanine production via aldehyde dehydrogenase conversion of 3-amino-propanal. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14764092}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Nucleus. TISSUE SPECIFICITY: Widely expressed. Isoform 1 and isoform 2 are expressed at higher level in brain and skeletal muscle. Isoform 7 is found in brain and spleen, isoform 10 is widely expressed but found at lower level in heart, kidney, liver and lung. {ECO:0000269|PubMed:14764092}. +Q5RJH6 SMG7_MOUSE Protein SMG7 (EST1-like protein C) (SMG-7 homolog) 1138 126,841 Alternative sequence (3); Chain (1); Compositional bias (2); Erroneous initiation (1); Initiator methionine (1); Modified residue (5); Repeat (2); Sequence conflict (1) FUNCTION: Plays a role in nonsense-mediated mRNA decay. Recruits UPF1 to cytoplasmic mRNA decay bodies. Together with SMG5 is thought to provide a link to the mRNA degradation machinery involving exonucleolytic pathways, and to serve as an adapter for UPF1 to protein phosphatase 2A (PP2A), thereby triggering UPF1 dephosphorylation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Predominantly cytoplasmic, and nuclear. Shuttles between nucleus and cytoplasm (By similarity). {ECO:0000250}. SUBUNIT: Part of a complex that contains SMG5, SMG7, PPP2CA, a short isoform of UPF3A (isoform UPF3AS, but not isoform UPF3AL) and phosphorylated UPF1. {ECO:0000250}. +Q8BIZ6 SNIP1_MOUSE Smad nuclear-interacting protein 1 383 44,415 Chain (1); Coiled coil (1); Compositional bias (2); Cross-link (5); Domain (1); Modified residue (7); Sequence conflict (1) FUNCTION: Down-regulates NF-kappa-B signaling by competing with RELA for CREBBP/EP300 binding. Involved in the microRNA (miRNA) biogenesis. biogenesis. May be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA (By similarity). {ECO:0000250}. PTM: Degraded by the proteasome upon binding to the SMAD1/OAZ1/PSMB4 complex. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Binds SMAD4 and CREBBP/EP300. Binds the SMAD1/OAZ1/PSMB4 complex. Interacts with DROSHA and SMARCA4. Component of the SNARP complex which consists at least of SNIP1, SNW1, THRAP3, BCLAF1 and PNN (By similarity). {ECO:0000250}. +Q80ZJ7 SNX32_MOUSE Sorting nexin-32 (Sorting nexin-6B) 404 46,647 Chain (1); Coiled coil (1); Domain (1) FUNCTION: May be involved in several stages of intracellular trafficking. {ECO:0000250}. +Q7M722 TR114_MOUSE Taste receptor type 2 member 114 (T2R114) (mT2R46) 309 35,732 Chain (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 8 28 Helical; Name=1. {ECO:0000255}.; TRANSMEM 44 64 Helical; Name=2. {ECO:0000255}.; TRANSMEM 88 108 Helical; Name=3. {ECO:0000255}.; TRANSMEM 128 148 Helical; Name=4. {ECO:0000255}.; TRANSMEM 183 203 Helical; Name=5. {ECO:0000255}.; TRANSMEM 234 254 Helical; Name=6. {ECO:0000255}.; TRANSMEM 260 280 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 7 Extracellular. {ECO:0000255}.; TOPO_DOM 29 43 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 65 87 Extracellular. {ECO:0000255}.; TOPO_DOM 109 127 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 149 182 Extracellular. {ECO:0000255}.; TOPO_DOM 204 233 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 255 259 Extracellular. {ECO:0000255}.; TOPO_DOM 281 309 Cytoplasmic. {ECO:0000255}. FUNCTION: Putative taste receptor which may play a role in the perception of bitterness. {ECO:0000305}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q6P4T1 SNX19_MOUSE Sorting nexin-19 997 109,808 Beta strand (3); Binding site (2); Chain (1); Compositional bias (1); Domain (2); Erroneous initiation (1); Helix (6); Mutagenesis (3) FUNCTION: Plays a role in intracellular vesicle trafficking and exocytosis (PubMed:24843546). May play a role in maintaining insulin-containing dense core vesicles in pancreatic beta-cells and in preventing their degradation. May play a role in insulin secretion (PubMed:24843546). Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)) (PubMed:25148684). {ECO:0000269|PubMed:24843546, ECO:0000269|PubMed:25148684}. SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000305|PubMed:25148684}; Peripheral membrane protein {ECO:0000269|PubMed:25148684}; Cytoplasmic side {ECO:0000269|PubMed:25148684}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:25148684}; Peripheral membrane protein {ECO:0000269|PubMed:25148684}; Cytoplasmic side {ECO:0000269|PubMed:25148684}. SUBUNIT: Interacts with PTPRN. {ECO:0000250|UniProtKB:Q92543}. DOMAIN: The PX domain mediates specific binding to membranes enriched in phosphatidylinositol 3-phosphate (PtdIns(P3)). {ECO:0000269|PubMed:25148684}. +Q8BGT7 SPF30_MOUSE Survival of motor neuron-related-splicing factor 30 (30 kDa splicing factor SMNrp) (SMN-related protein) (Survival motor neuron domain-containing protein 1) 238 26,753 Chain (1); Domain (1); Modified residue (2); Motif (1) FUNCTION: Necessary for spliceosome assembly. Overexpression causes apoptosis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}. Nucleus, Cajal body {ECO:0000250}. Note=Detected in nuclear speckles containing snRNP and in Cajal (coiled) bodies. {ECO:0000250}. SUBUNIT: Associates with spliceosomes. Associates with U4/U5/U6 tri-snRNP and with U2 snRNP (By similarity). {ECO:0000250}. DOMAIN: The Tudor domain mediates association with dimethylarginines, which are common in snRNP proteins. {ECO:0000250}. +Q148B6 SPERI_MOUSE Speriolin (Spermatogenesis and centriole-associated protein 1) (Spermatogenic cell-specific Cdc20-binding protein) 480 51,418 Alternative sequence (1); Chain (1); Coiled coil (1); Mutagenesis (4); Region (1); Sequence conflict (3) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15280373}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:15280373, ECO:0000269|PubMed:20542897}. Note=Colocalizes with the centrosomal pericentrin protein PCNT1. Located in the connecting piece of sperm. {ECO:0000269|PubMed:20542897}. SUBUNIT: Found in a complex with CDC20, CDC27 and TUBG1. Interacts with CDC20. {ECO:0000269|PubMed:15280373}. TISSUE SPECIFICITY: Expressed in testis. Expressed in pachyten spermatocytes, spermatids and epididymal sperm (at protein level). {ECO:0000269|PubMed:15280373, ECO:0000269|PubMed:20542897}. +Q9CQC8 SPG21_MOUSE Maspardin (Acid cluster protein 33) (Spastic paraplegia 21 autosomal recessive Mast syndrome protein homolog) 308 34,952 Alternative sequence (1); Chain (1); Domain (1); Modified residue (1); Sequence conflict (2) FUNCTION: May play a role as a negative regulatory factor in CD4-dependent T-cell activation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with CD4. Interacts with ALDH16A1. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in cell lines FT.1 and in a L cell fibroblast derivative (at protein level). {ECO:0000269|PubMed:11113139}. +Q3ULF4 SPG7_MOUSE Paraplegin (EC 3.4.24.-) (Spastic paraplegia 7 protein) 781 85,996 Active site (1); Binding site (2); Chain (1); Erroneous initiation (2); Metal binding (3); Modified residue (1); Mutagenesis (1); Nucleotide binding (1); Propeptide (1); Region (1); Sequence conflict (4); Topological domain (3); Transit peptide (1); Transmembrane (2) TRANSMEM 145 165 Helical; Name=1. {ECO:0000255}.; TRANSMEM 249 269 Helical; Name=2. {ECO:0000255}. TOPO_DOM 106 144 Mitochondrial matrix. {ECO:0000305}.; TOPO_DOM 166 248 Mitochondrial intermembrane. {ECO:0000305}.; TOPO_DOM 270 781 Mitochondrial matrix. {ECO:0000305}. FUNCTION: ATP-dependent zinc metalloprotease. Plays a role in the formation and regulation of the mitochondrial permeability transition pore (mPTP) and its proteolytic activity is dispensable for this function (By similarity). {ECO:0000250|UniProtKB:Q9UQ90, ECO:0000305}. PTM: Upon import into the mitochondrion, the N-terminal transit peptide is cleaved by the mitochondrial-processing peptidase (MPP) to generate an intermediate form which undergoes a second proteolytic cleavage mediated by proteases AFG3L1 and/or AFG3L2 removing an additional N-terminal fragment to generate the proteolytically active mature form. {ECO:0000269|PubMed:19656850}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:19656850, ECO:0000269|PubMed:22563492}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Forms heterooligomers with AFG3L1 and AFG3L2 (PubMed:22563492, PubMed:17101804, PubMed:19656850). Component of the mitochondrial permeability transition pore complex (mPTPC), at least composed of SPG7, VDAC1 and PPIF (By similarity). Interacts with AFG3L2; the interaction is required for the efficient assembly of mitochondrial complex I (PubMed:22563492, PubMed:19656850). Interacts with AFG3L1 (PubMed:19656850). Interacts with MAIP1. Interacts with VDAC1 and PPIF (By similarity). {ECO:0000250|UniProtKB:Q9UQ90, ECO:0000269|PubMed:17101804, ECO:0000269|PubMed:19656850, ECO:0000269|PubMed:22563492}. TISSUE SPECIFICITY: Expressed in the brain and retina (at protein level). {ECO:0000269|PubMed:22563492}. +Q8CI15 SPHK1_MOUSE Sphingosine kinase 1 (SK 1) (SPK 1) (EC 2.7.1.91) 382 42,443 Active site (1); Alternative sequence (2); Binding site (4); Chain (1); Domain (1); Modified residue (2); Motif (2); Nucleotide binding (4); Region (1); Sequence conflict (1) FUNCTION: Catalyzes the phosphorylation of sphingosine to form sphingosine 1-phosphate (SPP), a lipid mediator with both intra- and extracellular functions. Also acts on D-erythro-sphingosine and to a lesser extent sphinganine, but not other lipids, such as D,L-threo-dihydrosphingosine, N,N-dimethylsphingosine, diacylglycerol, ceramide, or phosphatidylinositol. {ECO:0000250|UniProtKB:Q9NYA1}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NYA1}. Nucleus {ECO:0000250|UniProtKB:Q9NYA1}. Cell membrane {ECO:0000250|UniProtKB:Q9NYA1}. Note=Translocated from the cytoplasm to the plasma membrane in a CIB1-dependent manner. {ECO:0000250|UniProtKB:Q9NYA1}. SUBUNIT: Interacts with ACY1 (PubMed:15196915). Binds to calmodulin. Interacts with SPHKAP (By similarity). Interacts with CIB1, the interaction occurs in a calcium-dependent manner (By similarity). Interacts with TRAF2 (By similarity). {ECO:0000250|UniProtKB:Q9NYA1, ECO:0000269|PubMed:15196915}. +Q9R1R2 TRIM3_MOUSE Tripartite motif-containing protein 3 (RING finger protein 22) (RING finger protein HAC1) 744 80,774 Chain (1); Coiled coil (1); Initiator methionine (1); Modified residue (3); Region (1); Repeat (7); Zinc finger (2) FUNCTION: Probably involved in vesicular trafficking via its association with the CART complex. The CART complex is necessary for efficient transferrin receptor recycling but not for EGFR degradation (By similarity). Positively regulates motility of microtubule-dependent motor protein KIF21B (PubMed:24086586). {ECO:0000250|UniProtKB:O75382, ECO:0000269|PubMed:24086586}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Early endosome {ECO:0000250|UniProtKB:O75382}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:24086586}. Cell projection, dendrite {ECO:0000269|PubMed:24086586}. SUBUNIT: Associates with myosin-Vb (MYO5B) and alpha-actinin-4 (ACTN4) (By similarity). Component of the CART complex, at least composed of ACTN4, HGS/HRS, MYO5B and TRIM3 (By similarity). Interacts with ZFYVE28/LST2 (By similarity). Interacts with KIF21B (PubMed:24086586). {ECO:0000250|UniProtKB:O70277, ECO:0000250|UniProtKB:O75382, ECO:0000269|PubMed:24086586}. DOMAIN: The interaction with MYO5B is dependent upon its NHL repeats, which form a beta-propeller (NHL) domain containing six blades. {ECO:0000250}. +P17433 SPI1_MOUSE Transcription factor PU.1 (31 kDa-transforming protein) (SFFV proviral integration 1 protein) 272 31,349 Beta strand (5); Chain (1); DNA binding (1); Erroneous initiation (2); Helix (4); Modified residue (2); Turn (3) FUNCTION: Binds to the PU-box, a purine-rich DNA sequence (5'-GAGGAA-3') that can act as a lymphoid-specific enhancer. This protein is a transcriptional activator that may be specifically involved in the differentiation or activation of macrophages or B-cells. Also binds RNA and may modulate pre-mRNA splicing. {ECO:0000269|PubMed:8626664}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Binds DNA as a monomer. Interacts with RUNX1 and SPIB (By similarity). Interacts with CEBPD and NONO. Interacts with GFI1; the interaction represses SPI1 transcriptional activity. Interacts with CEBPE (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P17947, ECO:0000269|PubMed:17197705, ECO:0000269|PubMed:7594592, ECO:0000269|PubMed:8626664}. DISEASE: Note=Involved in murine acute Friend erythroleukemia. It is a target region for SFFV proviral insertion. {ECO:0000269|PubMed:2594367}. +Q99PJ2 TRIM8_MOUSE Probable E3 ubiquitin-protein ligase TRIM8 (EC 2.3.2.27) (Glioblastoma-expressed RING finger protein) (RING finger protein 27) (RING-type E3 ubiquitin transferase TRIM8) (Tripartite motif-containing protein 8) 551 61,602 Chain (1); Coiled coil (2); Sequence conflict (3); Zinc finger (3) Protein modification; protein ubiquitination. FUNCTION: Probable E3 ubiquitin-protein ligase which may promote proteasomal degradation of SOCS1. {ECO:0000269|PubMed:12163497}. SUBUNIT: Homodimer. Interacts with SOCS1 (via) SH2 domain and SOCS box. Interacts with HSP90AB1; prevents nucleus translocation of phosphorylated STAT3 and HSP90AB1 (PubMed:21689689). {ECO:0000269|PubMed:12163497, ECO:0000269|PubMed:21689689}. DOMAIN: The coiled coil domain is required for homodimerization. {ECO:0000250}.; DOMAIN: The region immediately C-terminal to the RING motif is sufficient to mediate the interaction with SOCS1. TISSUE SPECIFICITY: High expression in heart, liver, and thymus. Expressed in embryonic CNS, kidney, lens and gut. {ECO:0000269|PubMed:11331580, ECO:0000269|PubMed:12163497}. +Q8C7M3 TRIM9_MOUSE E3 ubiquitin-protein ligase TRIM9 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase TRIM9) (Tripartite motif-containing protein 9) 817 90,870 Alternative sequence (9); Chain (1); Coiled coil (1); Domain (3); Erroneous initiation (1); Modified residue (5); Sequence conflict (4); Zinc finger (3) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase which ubiquitinates itself in cooperation with an E2 enzyme UBE2D2/UBC4 and serves as a targeting signal for proteasomal degradation. May play a role in regulation of neuronal functions. May act as a regulator of synaptic vesicle exocytosis by controlling the availability of SNAP25 for the SNARE complex formation. {ECO:0000250|UniProtKB:Q9C026}. PTM: Auto-ubiquitinated. {ECO:0000250|UniProtKB:Q9C026}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20085810}. Cell projection, dendrite {ECO:0000269|PubMed:20085810}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250|UniProtKB:Q91ZY8}. Cell junction, synapse {ECO:0000250|UniProtKB:Q91ZY8}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q91ZY8}. Note=Enriched at synaptic terminals where it exists in a soluble form and a synaptic vesicle-associated form. Associated with the cytoskeleton (By similarity). Found in proximal dendrites of pyramidal neurons in the cerebral cortex and hippocampus, and Purkinje cells in the cerebellum (Ref.7). {ECO:0000250|UniProtKB:Q91ZY8, ECO:0000269|PubMed:20085810}. SUBUNIT: Interacts with SNAP25. {ECO:0000250|UniProtKB:Q91ZY8}. DOMAIN: The coiled coil domain mediates the interaction with the N-terminal t-SNARE domain of SNAP25. {ECO:0000250|UniProtKB:Q91ZY8}. TISSUE SPECIFICITY: Brain. Expression is higher in the cerebral cortex and hippocampus (at protein level). Its expression is mainly confined to the central nervous system. The developing neocortex, the dorsal thalamus, the midbrain, the basal area of the hindbrain and spinal cord show high level of expression during embryogenesis. In adult brain, it is detected in the Purkinje cells of the cerebellum, in the hippocampus, and in the cortex. {ECO:0000269|PubMed:11960705, ECO:0000269|PubMed:20085810}. +Q0KL02 TRIO_MOUSE Triple functional domain protein (EC 2.7.11.1) 3102 347,861 Active site (1); Alternative sequence (5); Binding site (1); Chain (1); Compositional bias (5); Disulfide bond (1); Domain (9); Erroneous initiation (1); Modified residue (8); Mutagenesis (2); Nucleotide binding (1); Repeat (6); Sequence conflict (1) FUNCTION: Guanine nucleotide exchange factor (GEF) for RHOA and RAC1 GTPases. Involved in coordinating actin remodeling, which is necessary for cell migration and growth (By similarity). In developing hippocampal neurons, limits dendrite formation, without affecting the establishment of axon polarity. Once dendrites are formed, involved in the control of synaptic function by regulating the endocytosis of AMPA-selective glutamate receptors (AMPARs) at CA1 excitatory synapses (By similarity). May act as a regulator of adipogenesis (PubMed:22666460). {ECO:0000250|UniProtKB:F1M0Z1, ECO:0000250|UniProtKB:O75962, ECO:0000269|PubMed:22666460}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16943433}. Note=Isoform 2 localizes to early endosomes. {ECO:0000269|PubMed:16943433}. SUBUNIT: Interacts with CARMIL1 (By similarity). Interacts with PTPRF/LAR (By similarity). Interacts with ANKRD26 (By similarity). {ECO:0000250|UniProtKB:O75962}. DOMAIN: The N-terminal DBL/GEF domain specifically catalyzes nucleotide exchange for RAC1, leading to the activation of Jun kinase and the production of membrane ruffles. The second DBL/GEF domain is an exchange factor for rhoa and induces the formation of stress fibers (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widespread in the brain, with more intense signals in the hippocampus, olfactory bulb, cortical layers and cerebellum. Isoform 2 is predominantly expressed in Purkinje neurons of brain. {ECO:0000269|PubMed:16943433}. +Q61142 SPIN1_MOUSE Spindlin-1 (30000 Mr metaphase complex) (SSEC P) (Spindlin1) 262 29,643 Alternative sequence (1); Binding site (3); Chain (1); Cross-link (3); Modified residue (4); Region (6) FUNCTION: Chromatin reader that specifically recognizes and binds histone H3 both trimethylated at 'Lys-4' and asymmetrically dimethylated at 'Arg-8' (H3K4me3 and H3R8me2a) and acts as an activator of Wnt signaling pathway downstream of PRMT2. In case of cancer, promotes cell cancer proliferation via activation of the Wnt signaling pathway (By similarity). Overexpression induces metaphase arrest and chromosomal instability (PubMed:18543248). Localizes to active rDNA loci and promotes the expression of rRNA genes. May play a role in cell-cycle regulation during the transition from gamete to embryo. Involved in oocyte meiotic resumption, a process that takes place before ovulation to resume meiosis of oocytes blocked in prophase I: may act by regulating maternal transcripts to control meiotic resumption (PubMed:23894536). {ECO:0000250|UniProtKB:Q9Y657, ECO:0000269|PubMed:18543248, ECO:0000269|PubMed:23894536}. PTM: Phosphorylated during oocyte meiotic maturation. {ECO:0000269|PubMed:9053325}.; PTM: Post-translationally modified during the first mitotic cell cycle. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9053325}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:9053325}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9Y657}. Note=Associates with the meiotic spindle. {ECO:0000269|PubMed:9053325}. SUBUNIT: Homodimer; may form higher-order oligomers. Interacts with TCF7L2/TCF4; the interaction is direct (By similarity). Interacts with HABP4 and SERBP1 (PubMed:23894536). Interacts with C11orf84/SPINDOC (By similarity). {ECO:0000250|UniProtKB:Q9Y657, ECO:0000269|PubMed:23894536}. DOMAIN: The 3 tudor-like domains (also named Spin/Ssty repeats) specifically recognize and bind methylated histones. H3K4me3 and H3R8me2a are recognized by tudor-like domains 2 and 1, respectively. {ECO:0000250|UniProtKB:Q9Y657}. TISSUE SPECIFICITY: Oocyte, egg, and very early embryo; not in the 8-, and 16-cell stage of the embryo. Isoform 1: Present in testis. Isoform 1 is more highly expressed in adult testes compared with newborn testes (at protein level). {ECO:0000269|PubMed:9053325}. +Q8VCC9 SPON1_MOUSE Spondin-1 (F-spondin) 807 90,821 Chain (1); Disulfide bond (17); Domain (8); Erroneous initiation (1); Glycosylation (2); Metal binding (3); Signal peptide (1) FUNCTION: Cell adhesion protein that promotes the attachment of spinal cord and sensory neuron cells and the outgrowth of neurites in vitro. May contribute to the growth and guidance of axons in both the spinal cord and the PNS (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. SUBUNIT: Binds to the central extracellular domain of APP and inhibits beta-secretase cleavage of APP. {ECO:0000250}. +Q9D2Q2 TRM44_MOUSE Probable tRNA (uracil-O(2)-)-methyltransferase (EC 2.1.1.211) (Methyltransferase-like protein 19) 713 79,836 Chain (1); Modified residue (2); Sequence conflict (1); Zinc finger (1) FUNCTION: Probable adenosyl-L-methionine (AdoMet)-dependent tRNA (uracil-O(2)-)-methyltransferase. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. +Q62266 SPR1A_MOUSE Cornifin-A (Small proline-rich protein 1A) (SPR1 A) (SPR1A) 144 15,765 Chain (1); Region (1); Repeat (13) FUNCTION: Cross-linked envelope protein of keratinocytes. It is a keratinocyte protein that first appears in the cell cytosol, but ultimately becomes cross-linked to membrane proteins by transglutaminase. All that results in the formation of an insoluble envelope beneath the plasma membrane. May participate widely in the construction of cell envelopes in cornifying epithelia characterized by either increased thickness or a requirement for extreme flexibility. SUBCELLULAR LOCATION: Cytoplasm. TISSUE SPECIFICITY: Expressed in fetal periderm, hair follicles and in the thickened epidermis of the lip and footpad. Also present in the epithelia of various tissues such as the penis, vagina, forestomach, tongue and esophagus. {ECO:0000269|PubMed:8601731}. +Q62267 SPR1B_MOUSE Cornifin-B (Small proline-rich protein 1B) (SPR1 B) (SPR1B) 153 16,636 Chain (1); Region (1); Repeat (14) FUNCTION: Cross-linked envelope protein of keratinocytes. It is a keratinocyte protein that first appears in the cell cytosol, but ultimately becomes cross-linked to membrane proteins by transglutaminase. All that results in the formation of an insoluble envelope beneath the plasma membrane. SUBCELLULAR LOCATION: Cytoplasm. TISSUE SPECIFICITY: Expressed in fetal periderm, hair follicles and in the thickened epidermis of the lip and footpad. Also present in the epithelia of various tissues such as the penis, vagina, forestomach, tongue and esophagus. +Q9CQK8 SPR2A_MOUSE Small proline-rich protein 2A1 (small proline-rich protein 2A) 83 9,408 Chain (1); Region (1); Repeat (5); Sequence conflict (1) FUNCTION: Cross-linked envelope protein of keratinocytes. It is a keratinocyte protein that first appears in the cell cytosol, but ultimately becomes cross-linked to membrane proteins by transglutaminase. All that results in the formation of an insoluble envelope beneath the plasma membrane (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +Q8BWU1 SPRN_MOUSE Shadow of prion protein (Protein shadoo) 147 14,591 Chain (1); Compositional bias (1); Glycosylation (1); Lipidation (1); Propeptide (1); Signal peptide (1) FUNCTION: Prion-like protein that has PrP(C)-like neuroprotective activity. May act as a modulator for the biological actions of normal and abnormal PrP. {ECO:0000269|PubMed:17703189}. PTM: N-glycosylated. {ECO:0000269|PubMed:17703189}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17703189}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:17703189}. TISSUE SPECIFICITY: Mainly expressed in brain (at protein level). In brain, it is highly expressed in the hippocampus and cerebellum and is also expressed at lower level in other areas of the brain including the cerebral cortex, the thalamus and the medulla. In hippocampus and cerebellum it is highly expressed in the cell bodies of pyramidal cells and Purkinje cells, respectively. {ECO:0000269|PubMed:17703189}. +Q8CGN8 SPRR4_MOUSE Small proline-rich protein 4 76 8,504 Chain (1) FUNCTION: Cross-linked envelope protein of keratinocytes. Involved in UV-induced cornification (By similarity). {ECO:0000250}. PTM: Cross-linked to membrane proteins by transglutaminase. {ECO:0000305}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Note=Translocates to the cell periphery of keratinocytes and is integrated into both rigid and fragile cornified envelopes. {ECO:0000250}. +Q9D552 SPT17_MOUSE Spermatogenesis-associated protein 17 (Spermatogenesis-related protein 11) 379 45,503 Alternative sequence (4); Chain (1); Domain (3) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15756417}. TISSUE SPECIFICITY: Strongly expressed in adult testis but weakly expressed in the spleen and thymus. Strongly expressed in round and elongating spermatids, and weakly or not expressed in spermatozoa. {ECO:0000269|PubMed:15756417}. +Q5SV06 SPT22_MOUSE Spermatogenesis-associated protein 22 358 40,163 Chain (1) FUNCTION: Meiosis-specific protein required for homologous recombination in meiosis I. {ECO:0000269|PubMed:22011390}. SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:24240703}. Note=Localizes on meiotic chromosome axes. Accumulates on resected DNA. Localization is dependent on MEIOB. SUBUNIT: Component of a multiprotein complex with MEIOB and SPATA22. TISSUE SPECIFICITY: Specifically expressed in gonadal germ cells, when male and female germ cells progress through prophase of meiosis I. {ECO:0000269|PubMed:22011390}. +Q9Z199 SPT4B_MOUSE Transcription elongation factor SPT4-B (DRB sensitivity-inducing factor small subunit 2) (DSIF small subunit 2) (Transcription elongation factor SPT4 2) 117 13,194 Chain (1); Region (1); Zinc finger (1) FUNCTION: Component of the DRB sensitivity-inducing factor complex (DSIF complex), which regulates mRNA processing and transcription elongation by RNA polymerase II. DSIF positively regulates mRNA capping by stimulating the mRNA guanylyltransferase activity of RNGTT/CAP1A. DSIF also acts cooperatively with the negative elongation factor complex (NELF complex) to enhance transcriptional pausing at sites proximal to the promoter. Transcriptional pausing may facilitate the assembly of an elongation competent RNA polymerase II complex. DSIF and NELF promote pausing by inhibition of the transcription elongation factor TFIIS/S-II. TFIIS/S-II binds to RNA polymerase II at transcription pause sites and stimulates the weak intrinsic nuclease activity of the enzyme. Cleavage of blocked transcripts by RNA polymerase II promotes the resumption of transcription from the new 3' terminus and may allow repeated attempts at transcription through natural pause sites (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with SUPT5H to form DSIF. DSIF interacts with the positive transcription elongation factor b complex (P-TEFb complex), which is composed of CDK9 and cyclin-T (CCNT1 or CCNT2). DSIF interacts with RNA polymerase II, and this interaction is reduced by phosphorylation of the C-terminal domain (CTD) of POLR2A by P-TEFb. DSIF also interacts with the NELF complex, which is composed of WHSC2/NELFA, COBRA1/NELFB, TH1L/NELFD and RDBP/NELFE, and this interaction occurs following prior binding of DSIF to RNA polymerase II. DSIF also interacts with HRMT1L2/PRMT1, HTATSF1/TATSF1, RNGTT/CAP1A, SKB1/PRMT5, SUPT6H, and can interact with PIN1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain, heart and liver. {ECO:0000269|PubMed:9776760}. +Q62383 SPT6H_MOUSE Transcription elongation factor SPT6 1726 199,086 Chain (1); Coiled coil (1); Compositional bias (1); Domain (2); Initiator methionine (1); Modified residue (21); Mutagenesis (1); Region (4); Sequence conflict (2) FUNCTION: Transcription elongation factor which binds histone H3 and plays a key role in the regulation of transcription elongation and mRNA processing. Enhances the transcription elongation by RNA polymerase II (RNAPII) and is also required for the efficient activation of transcriptional elongation by the HIV-1 nuclear transcriptional activator, Tat. Besides chaperoning histones in transcription, acts to transport and splice mRNA by forming a complex with IWS1 and the C-terminal domain (CTD) of the RNAPII subunit RPB1 (POLR2A). The SUPT6H:IWS1:CTD complex recruits mRNA export factors (ALYREF/THOC4, EXOSC10) as well as histone modifying enzymes (such as SETD2), to ensure proper mRNA splicing, efficient mRNA export and elongation-coupled H3K36 methylation, a signature chromatin mark of active transcription. SUPT6H via its association with SETD1A, regulates both class-switch recombination and somatic hypermutation through formation of H3K4me3 epigenetic marks on activation-induced cytidine deaminase (AICDA) target loci. Promotes the activation of the myogenic gene program by entailing erasure of the repressive H3K27me3 epigenetic mark through stabilization of the chromatin interaction of the H3K27 demethylase KDM6A. {ECO:0000269|PubMed:17234882, ECO:0000269|PubMed:21518874, ECO:0000269|PubMed:22843687, ECO:0000269|PubMed:23503590}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Interacts with RNA polymerase II and the DRB sensitivity-inducing factor complex (DSIF complex), which is composed of SUPT5H and SUPT4H1 or SUPT4H2 (By similarity). Interacts with PAAF1 (By similarity). Interacts with histone H2B and H3 (By similarity). Interacts (via SH2 domain) with POLR2A phosphorylated at 'Ser-2'. Interacts (via SH2 domain) with SETD1A. Interacts with IWS1, KDM6A and AICDA. {ECO:0000250, ECO:0000269|PubMed:17234882, ECO:0000269|PubMed:19141475, ECO:0000269|PubMed:21518874, ECO:0000269|PubMed:22843687, ECO:0000269|PubMed:23503590}. TISSUE SPECIFICITY: Ubiquitously expressed. +Q925E8 SPTSB_MOUSE Serine palmitoyltransferase small subunit B (Protein ADMP) (Small subunit of serine palmitoyltransferase B) (ssSPTb) 76 9,108 Chain (1); Topological domain (3); Transmembrane (2) TRANSMEM 12 29 Helical. {ECO:0000255}.; TRANSMEM 37 57 Helical. {ECO:0000255}. TOPO_DOM 1 11 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 30 36 Lumenal. {ECO:0000255}.; TOPO_DOM 58 76 Cytoplasmic. {ECO:0000255}. Lipid metabolism; sphingolipid metabolism. FUNCTION: Stimulates the activity of serine palmitoyltransferase (SPT). The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference, complexes with this subunit showing a clear preference for longer acyl-CoAs. The SPTLC1-SPTLC2-SPTSSB complex shows a strong preference for C18-CoA substrate, while the SPTLC1-SPTLC3-SPTSSB isozyme displays an ability to use a broader range of acyl-CoAs, without apparent preference (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Interacts with SPTLC1; the interaction is direct. Component of the serine palmitoyltransferase (SPT) complex, composed of SPTLC1, either SPTLC2 or SPTLC3, and either SPTSSA or SPTSSB (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expression is strong in hypogonadal (hpg) mouse prostate, weak in mature castrated mouse prostate and absent in normal intact or androgen-replaced hpg mouse prostates. {ECO:0000269|PubMed:15777716}. +P08032 SPTA1_MOUSE Spectrin alpha chain, erythrocytic 1 (Erythroid alpha-spectrin) 2415 279,865 Calcium binding (2); Chain (1); Domain (4); Modified residue (3); Repeat (20); Sequence conflict (13) FUNCTION: Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cell cortex. SUBUNIT: Composed of non-homologous chains, alpha and beta, which aggregate to form dimers, tetramers, and higher polymers. Interacts with FASLG (By similarity). {ECO:0000250}. +Q9D9T6 SPTA3_MOUSE Spermatogenesis-associated protein 3 (Testis and spermatogenesis cell-related protein 1) (mTSARG1) (Testis spermatocyte apoptosis-related protein 1) 193 20,947 Alternative sequence (5); Chain (1); Compositional bias (1); Sequence conflict (1) TISSUE SPECIFICITY: Strongly expressed in testis. Faintly expressed in epididymis, ovary, spleen, kidney, lung, heart, brain, epididymis, liver and skeletal muscle. {ECO:0000269|PubMed:12812072}. +Q62261 SPTB2_MOUSE Spectrin beta chain, non-erythrocytic 1 (Beta-II spectrin) (Embryonic liver fodrin) (Fodrin beta chain) 2363 274,223 Alternative sequence (3); Beta strand (9); Chain (1); Domain (3); Glycosylation (1); Helix (2); Initiator methionine (1); Modified residue (39); Region (3); Repeat (17); Sequence conflict (16) FUNCTION: Fodrin, which seems to be involved in secretion, interacts with calmodulin in a calcium-dependent manner and is thus candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. Endomembrane system {ECO:0000269|PubMed:15262991}. Cytoplasm, myofibril, sarcomere, M line {ECO:0000269|PubMed:15262991}. Note=Colocalizes with ANK2 in a distinct intracellular compartment of neonatal cardiomyocytes. {ECO:0000269|PubMed:15262991}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm {ECO:0000269|PubMed:9927192}. Cell membrane {ECO:0000269|PubMed:9927192}; Peripheral membrane protein; Cytoplasmic side. SUBUNIT: Interacts with ANK2 (PubMed:15262991). Interacts with CPNE4 (via VWFA domain) (PubMed:12522145). Like erythrocyte spectrin, the spectrin-like proteins are capable to form dimers which can further associate to tetramers (By similarity). Interacts with CAMSAP1 (By similarity). {ECO:0000250|UniProtKB:P85986, ECO:0000250|UniProtKB:Q01082, ECO:0000269|PubMed:12522145, ECO:0000269|PubMed:15262991}. TISSUE SPECIFICITY: Isoform 2 is present in brain, heart, kidney and liver (at protein level). {ECO:0000269|PubMed:15262991, ECO:0000269|PubMed:9927192}. +P97363 SPTC2_MOUSE Serine palmitoyltransferase 2 (EC 2.3.1.50) (Long chain base biosynthesis protein 2) (LCB 2) (Long chain base biosynthesis protein 2a) (LCB2a) (Serine-palmitoyl-CoA transferase 2) (SPT 2) 560 62,982 Chain (1); Modified residue (1); Transmembrane (1) TRANSMEM 65 85 Helical. {ECO:0000255}. Lipid metabolism; sphingolipid metabolism. FUNCTION: Serine palmitoyltransferase (SPT). The heterodimer formed with LCB1/SPTLC1 constitutes the catalytic core. The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference. The SPTLC1-SPTLC2-SPTSSA complex shows a strong preference for C16-CoA substrate, while the SPTLC1-SPTLC2-SPTSSB complex displays a preference for C18-CoA substrate (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:1317856}; Single-pass membrane protein {ECO:0000269|PubMed:1317856}. SUBUNIT: Heterodimer with SPTLC1. Component of the serine palmitoyltransferase (SPT) complex, composed of LCB1/SPTLC1, LCB2 (SPTLC2 or SPTLC3) and ssPT (SPTSSA or SPTSSB) (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in a variety of tissues. +Q8BG54 SPTC3_MOUSE Serine palmitoyltransferase 3 (EC 2.3.1.50) (Long chain base biosynthesis protein 2b) (LCB2b) (Long chain base biosynthesis protein 3) (LCB 3) (Serine-palmitoyl-CoA transferase 3) (SPT 3) 563 63,486 Chain (1); Frameshift (1); Modified residue (1); Transmembrane (1) TRANSMEM 59 79 Helical. {ECO:0000255}. Lipid metabolism; sphingolipid metabolism. FUNCTION: Serine palmitoyltransferase (SPT). The heterodimer formed with LCB1/SPTLC1 constitutes the catalytic core. The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference. The SPTLC1-SPTLC3-SPTSSA isozyme uses both C14-CoA and C16-CoA as substrates, while the SPTLC1-SPTLC3-SPTSSB has the ability to use a broader range of acyl-CoAs without apparent preference (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. SUBUNIT: Heterodimer with SPTLC1. Component of the serine palmitoyltransferase (SPT) complex, composed of LCB1/SPTLC1, LCB2 (SPTLC2 or SPTLC3) and ssPT (SPTSSA or SPTSSB) (By similarity). {ECO:0000250}. +Q3UHA3 SPTCS_MOUSE Spatacsin (Spastic paraplegia 11 protein homolog) 2430 273,934 Alternative sequence (2); Chain (1); Erroneous initiation (2); Modified residue (2); Sequence conflict (7) FUNCTION: May play a role in neurite plasticity by maintaining cytoskeleton stability and regulating synaptic vesicle transport. {ECO:0000269|PubMed:24794856}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:24794856}. Nucleus {ECO:0000250|UniProtKB:Q96JI7}. Cell projection, axon {ECO:0000269|PubMed:24794856}. Cell projection, dendrite {ECO:0000269|PubMed:24794856}. Cell junction, synapse {ECO:0000269|PubMed:24794856}. Note=Mainly cytoplasmic. {ECO:0000269|PubMed:24794856}. SUBUNIT: Interacts with AP5Z1, AP5B1, AP5S1 and ZFYVE26. {ECO:0000250|UniProtKB:Q96JI7}. TISSUE SPECIFICITY: Ubiquitously expressed at low level. Expressed in embryonic and adult cortical projection neurons. {ECO:0000269|PubMed:17322883, ECO:0000269|PubMed:24794856}. +O35423 SPYA_MOUSE Serine--pyruvate aminotransferase, mitochondrial (SPT) (EC 2.6.1.51) (Alanine--glyoxylate aminotransferase) (AGT) (EC 2.6.1.44) 414 45,912 Alternative sequence (1); Beta strand (12); Binding site (1); Chain (1); Helix (16); Modified residue (7); Motif (1); Sequence conflict (2); Transit peptide (1); Turn (5) FUNCTION: Dual metabolic roles of gluconeogenesis (in the mitochondria) and glyoxylate detoxification (in the peroxisomes). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. Peroxisome {ECO:0000250|UniProtKB:P21549}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P21549}. +Q3U213 SRAC1_MOUSE Protein SERAC1 (Serine active site-containing protein 1) 654 73,987 Alternative sequence (3); Chain (1); Compositional bias (2); Natural variant (6); Transmembrane (1) TRANSMEM 32 54 Helical. {ECO:0000255}. FUNCTION: Plays an important role in the phosphatidylglycerol remodeling that is essential for both mitochondrial function and intracellular cholesterol trafficking. May catalyze the remodeling of phosphatidylglycerol and be involved in the transacylation-acylation reaction to produce phosphatidylglycerol-36:1. May be involved in bis(monoacylglycerol)phosphate biosynthetic pathway (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Endoplasmic reticulum {ECO:0000250}. Mitochondrion {ECO:0000250}. Note=Localizes at the endoplasmic reticulum and at the endoplasmic reticulum-mitochondria interface. {ECO:0000250}. TISSUE SPECIFICITY: Testis. {ECO:0000269|PubMed:15722415}. +Q3U1N2 SRBP2_MOUSE Sterol regulatory element-binding protein 2 (SREBP-2) (Sterol regulatory element-binding transcription factor 2) [Cleaved into: Processed sterol regulatory element-binding protein 2] 1130 122,911 Alternative sequence (2); Chain (2); Compositional bias (3); Cross-link (1); Domain (1); Modified residue (1); Region (3); Sequence conflict (4); Site (3); Topological domain (3); Transmembrane (2) TRANSMEM 471 491 Helical. {ECO:0000255}.; TRANSMEM 523 543 Helical. {ECO:0000255}. TOPO_DOM 1 470 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 492 522 Lumenal. {ECO:0000255}.; TOPO_DOM 544 1130 Cytoplasmic. {ECO:0000255}. FUNCTION: Transcriptional activator required for lipid homeostasis. Regulates transcription of the LDL receptor gene as well as the cholesterol and to a lesser degree the fatty acid synthesis pathway. Binds the sterol regulatory element 1 (SRE-1) (5'-ATCACCCCAC-3') found in the flanking region of the LDRL and HMG-CoA synthase genes. {ECO:0000269|PubMed:9616204}. PTM: At low cholesterol the SCAP/SREBP complex is recruited into COPII vesicles for export from the ER. In the Golgi complex SREBPs are cleaved sequentially by site-1 and site-2 protease. The first cleavage by site-1 protease occurs within the luminal loop, the second cleavage by site-2 protease occurs within the first transmembrane domain and releases the transcription factor from the Golgi membrane. Apoptosis triggers cleavage by the cysteine proteases caspase-3 and caspase-7 (By similarity). {ECO:0000250|UniProtKB:Q12772}.; PTM: Phosphorylated by AMPK, leading to suppress protein processing and nuclear translocation, and repress target gene expression. {ECO:0000269|PubMed:21459323}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q12772}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q12772}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q12772}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q12772}. Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250|UniProtKB:Q12772}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q12772}. Note=Moves from the endoplasmic reticulum to the Golgi in the absence of sterols. {ECO:0000250|UniProtKB:Q12772}.; SUBCELLULAR LOCATION: Processed sterol regulatory element-binding protein 2: Nucleus {ECO:0000269|PubMed:29068315}. SUBUNIT: Forms a tight complex with SCAP in the ER membrane. Efficient DNA binding of the soluble transcription factor fragment requires dimerization with another bHLH protein (By similarity). Interacts with LMNA. Component of SCAP/SREBP complex composed of SREBF2, SCAP and RNF139; the complex hampers the interaction between SCAP and SEC24B, thereby reducing SREBF2 proteolytic processing. Interacts (via C-terminal domain) with RNF139 (By similarity). {ECO:0000250}. +Q3UTJ2 SRBS2_MOUSE Sorbin and SH3 domain-containing protein 2 (Arg-binding protein 2) (ArgBP2) (Arg/Abl-interacting protein 2) 1180 132,349 Alternative sequence (12); Chain (1); Compositional bias (2); Domain (4); Modified residue (37); Sequence conflict (2) FUNCTION: Adapter protein that plays a role in the assembling of signaling complexes, being a link between ABL kinases and actin cytoskeleton. Can form complex with ABL1 and CBL, thus promoting ubiquitination and degradation of ABL1 (By similarity). May play a role in the regulation of pancreatic cell adhesion, possibly by acting on WASF1 phosphorylation, enhancing phosphorylation by ABL1, as well as dephosphorylation by PTPN12 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O94875}. PTM: Ubiquitinated by CBL. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250}. Apical cell membrane {ECO:0000250|UniProtKB:O94875}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:O94875}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:O94875}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Found at the Z line sarcomeres, stress fibers, dense bodies and focal adhesion. In pancreatic acinar cells, localized preferentially to the apical membrane. Colocalized with vinculin and filamentous actin at focal adhesions and lamellipodia of pancreatic cells. {ECO:0000250, ECO:0000250|UniProtKB:O94875}. SUBUNIT: Interacts with ABL, CBL, DNM1, DNM2, FLOT1, AFDN, PTK2B/PYK2, SAPAP, SPTAN1, SYNJ1, SYNJ2, VCL/vinculin, WASF, ABL1/c-Abl, ABL2/v-Abl/Arg, ACTN, CBL and PALLD. Interacts with PTPN12 and WASF1 via its SH3 domains; this interaction may mediate the partial PTPN12 and WASF1 translocation to focal adhesion sites. {ECO:0000250, ECO:0000250|UniProtKB:O94875}. DOMAIN: The first 2 SH3 domains are required for WASF1-binding. All 3 SH3 domains can bind independently to PTPN12. {ECO:0000250|UniProtKB:O94875}. +Q497V5 SRBD1_MOUSE S1 RNA-binding domain-containing protein 1 982 110,281 Alternative sequence (2); Chain (1); Coiled coil (1); Cross-link (5); Domain (1); Modified residue (1) +Q5ND28 SREC_MOUSE Scavenger receptor class F member 1 (Acetyl LDL receptor) (Scavenger receptor expressed by endothelial cells 1 protein) (SREC-I) 820 87,464 Chain (1); Disulfide bond (12); Domain (6); Erroneous initiation (1); Glycosylation (1); Modified residue (2); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 423 443 Helical. {ECO:0000255}. TOPO_DOM 24 422 Extracellular. {ECO:0000255}.; TOPO_DOM 444 820 Cytoplasmic. {ECO:0000255}. FUNCTION: Mediates the binding and degradation of acetylated low density lipoprotein (Ac-LDL). Mediates heterophilic interactions, suggesting a function as adhesion protein (By similarity). Plays a role in the regulation of neurite-like outgrowth. {ECO:0000250, ECO:0000269|PubMed:15247299}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Heterophilic interaction with SREC2 via its extracellular domain. The heterophilic interaction is suppressed by the presence of ligand such as Ac-LDL (By similarity). Interacts with AVIL; the interaction occurs in embryonic dorsal root ganglions at 18 dpc and induces neurite-like outgrowth. {ECO:0000250, ECO:0000269|PubMed:15247299}. DOMAIN: The cytoplasmic domain is necessary for the regulation of neurite-like outgrowth. TISSUE SPECIFICITY: Expressed weakly in brain, spinal cord and dorsal root ganglions. {ECO:0000269|PubMed:15247299}. +Q9CZ91 SRFB1_MOUSE Serum response factor-binding protein 1 (SRF-dependent transcription regulation-associated protein) (p49/STRAP) 441 48,746 Chain (1); Coiled coil (2); Cross-link (2); Modified residue (4); Sequence conflict (14) FUNCTION: May be involved in regulating transcriptional activation of cardiac genes during the aging process. May play a role in biosynthesis and/or processing of SLC2A4 in adipose cells. {ECO:0000269|PubMed:15492011, ECO:0000269|PubMed:16647043}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:16647043}. SUBUNIT: Interacts with SRF. Forms complexes with SRF and SRF cofactors ARID2, MYOCD and NKX2-5. Interacts with the N-terminus of SLC2A4. {ECO:0000269|PubMed:15492011, ECO:0000269|PubMed:16647043, ECO:0000269|PubMed:16782067}. TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle, liver, kidney, testis and brain. Also expressed in white adipose tissue. Expression is up-regulated in cardiomyopathic heart. {ECO:0000269|PubMed:15492011, ECO:0000269|PubMed:16647043}. +Q91Z69 SRGP1_MOUSE SLIT-ROBO Rho GTPase-activating protein 1 (srGAP1) (Rho GTPase-activating protein 13) 1062 121,430 Beta strand (4); Chain (1); Coiled coil (2); Compositional bias (3); Domain (3); Erroneous initiation (1); Helix (1); Modified residue (7); Sequence conflict (3) FUNCTION: GTPase-activating protein for RhoA and Cdc42 small GTPases. Together with CDC42 seems to be involved in the pathway mediating the repulsive signaling of Robo and Slit proteins in neuronal migration. SLIT2, probably through interaction with ROBO1, increases the interaction of SRGAP1 with ROBO1 and inactivates CDC42 (By similarity). {ECO:0000250}. SUBUNIT: Homodimer (Probable). Forms a heterooligomer with SRGAP2 and SRGAP3 through its F-BAR domain. Interacts with CDC42 and RHOA. Interacts with FASLG (By similarity). Interacts (via SH3 domain) with ROBO1. {ECO:0000250, ECO:0000269|PubMed:16857672, ECO:0000305}. DOMAIN: The F-BAR domain mediates oligomerization, binds membranes, and constrains plasma membrane protrusions. {ECO:0000250}. +Q62270 SRMS_MOUSE Tyrosine-protein kinase Srms (EC 2.7.10.2) (PTK70) 496 55,758 Active site (1); Binding site (1); Chain (1); Domain (3); Modified residue (1); Nucleotide binding (1); Sequence conflict (4) FUNCTION: Non-receptor tyrosine-protein kinase which phosphorylates DOK1 on tyrosine residues. Also phosphorylates KHDRBS1/SAM68 and VIM on tyrosine residues. Phosphorylation of KHDRBS1 is EGF-dependent. {ECO:0000250|UniProtKB:Q9H3Y6}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H3Y6}. Note=Localizes to punctate cytoplasmic structures. {ECO:0000250|UniProtKB:Q9H3Y6}. SUBUNIT: Interacts (via the SH2 and SH3 domains) with DOK1. Interacts with KHDRBS1/SAM68 and VIM. {ECO:0000250|UniProtKB:Q9H3Y6}. DOMAIN: The N-terminal region regulates its kinase activity. {ECO:0000250|UniProtKB:Q9H3Y6}. TISSUE SPECIFICITY: Higher expression in liver, lung, thymus and skin than in brain, kidney, heart and spleen (PubMed:9226137). In skin, highly expressed in keratinocytes (PubMed:9226137). Abundant in lung, liver, spleen, kidney and testis and is also detected in the cerebrum (PubMed:7935409). {ECO:0000269|PubMed:7935409, ECO:0000269|PubMed:9226137}. +Q9D7A6 SRP19_MOUSE Signal recognition particle 19 kDa protein (SRP19) 144 16,191 Chain (1); Region (1) FUNCTION: Signal-recognition-particle assembly, binds directly to 7S RNA and mediates binding of the 54 kDa subunit of the SRP. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Signal recognition particle consists of a 7S RNA molecule of 300 nucleotides and six protein subunits: SRP72, SRP68, SRP54, SRP19, SRP14 and SRP9. +Q9Z120 TRMB_MOUSE tRNA (guanine-N(7)-)-methyltransferase (EC 2.1.1.33) (Methyltransferase-like protein 1) (tRNA (guanine(46)-N(7))-methyltransferase) (tRNA(m7G46)-methyltransferase) 268 30,603 Active site (1); Binding site (2); Chain (1); Modified residue (1); Region (3); Sequence conflict (3) tRNA modification; N(7)-methylguanine-tRNA biosynthesis. FUNCTION: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. {ECO:0000255|HAMAP-Rule:MF_03055}. PTM: Phosphorylation at Ser-21 inactivates its catalytic activity but does not affect the interaction with WDR4. {ECO:0000255|HAMAP-Rule:MF_03055}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03055}. SUBUNIT: Forms a complex with WDR4. {ECO:0000255|HAMAP-Rule:MF_03055}. +P14576 SRP54_MOUSE Signal recognition particle 54 kDa protein (SRP54) 504 55,721 Alternative sequence (2); Chain (1); Helix (4); Nucleotide binding (3); Region (2); Sequence conflict (1) FUNCTION: Binds to the signal sequence of presecretory protein when they emerge from the ribosomes and transfers them to TRAM (translocating chain-associating membrane protein). SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}. Cytoplasm. SUBUNIT: Interacts with RNPS1 (By similarity). Signal recognition particle consists of a 7S RNA molecule of 300 nucleotides and six protein subunits: SRP72, SRP68, SRP54, SRP19, SRP14 and SRP9. {ECO:0000250}. DOMAIN: Has a two domain structure: the G-domain binds GTP; the M-domain binds the 7S RNA in presence of SRP19 and also binds the signal sequence. +O54781 SRPK2_MOUSE SRSF protein kinase 2 (EC 2.7.11.1) (SFRS protein kinase 2) (Serine/arginine-rich protein-specific kinase 2) (SR-protein-specific kinase 2) [Cleaved into: SRSF protein kinase 2 N-terminal; SRSF protein kinase 2 C-terminal] 681 76,757 Active site (1); Binding site (1); Chain (3); Domain (1); Modified residue (13); Nucleotide binding (1); Sequence conflict (2); Site (2) FUNCTION: Serine/arginine-rich protein-specific kinase which specifically phosphorylates its substrates at serine residues located in regions rich in arginine/serine dipeptides, known as RS domains and is involved in the phosphorylation of SR splicing factors and the regulation of splicing. Promotes neuronal apoptosis by up-regulating cyclin-D1 (CCND1) expression. This is done by the phosphorylation of SRSF2, leading to the suppression of p53/TP53 phosphorylation thereby relieving the repressive effect of p53/TP53 on cyclin-D1 (CCND1) expression. Phosphorylates ACIN1, and redistributes it from the nuclear speckles to the nucleoplasm, resulting in cyclin A1 but not cyclin A2 up-regulation. Plays an essential role in spliceosomal B complex formation via the phosphorylation of DDX23/PRP28. {ECO:0000269|PubMed:19592491, ECO:0000269|PubMed:9446799}. PTM: Phosphorylation at Thr-485 by PKB/AKT1 enhances its stimulatory activity in triggering cyclin-D1 (CCND1) expression and promoting apoptosis in neurons, which can be blocked by YWHAB. It also enhances its protein kinase activity toward ACIN1 and SRSF2, promotes its nuclear translocation and prevents its proteolytic cleavage (By similarity). {ECO:0000250}.; PTM: Proteolytically cleaved at Asp-137 and Asp-401 by caspase-3 during apoptotic cell death. Cleavage at Asp-137 which is the major site of cleavage, produces a small N-terminal fragment that translocates into nucleus and promotes VP16-induced apoptosis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9446799}. Nucleus {ECO:0000269|PubMed:9446799}. Note=Shuttles between the nucleus and the cytoplasm. KAT5/TIP60 inhibits its nuclear translocation. Phosphorylation at Thr-492 by PKB/AKT1 promotes nuclear translocation (By similarity). {ECO:0000250}. SUBUNIT: Interacts with PKB/AKT1 in a phosphorylation-dependent manner. The phosphorylated form (by PKB/AKT1) interacts with YWHAB and YWHAE. Interaction with YWHAB suppresses its cleavage by caspases and inhibits the release of its N-terminal pro-apoptotic fragment. Interacts with SFN. Associates with U4/U6-U5 tri-small nuclear ribonucleoproteins (U4/U6-U5 tri-snRNPs) (By similarity). Interacts with ACIN1. {ECO:0000250, ECO:0000269|PubMed:18559500}. TISSUE SPECIFICITY: Expressed in testes, lung and brain. {ECO:0000269|PubMed:9446799}. +Q9QZX7 SRR_MOUSE Serine racemase (EC 5.1.1.18) (D-serine ammonia-lyase) (D-serine dehydratase) (EC 4.3.1.18) (L-serine ammonia-lyase) (L-serine dehydratase) (EC 4.3.1.17) 339 36,359 Active site (2); Alternative sequence (2); Binding site (3); Chain (1); Erroneous gene model prediction (1); Metal binding (3); Modified residue (3); Mutagenesis (2); Region (1); Sequence conflict (1) FUNCTION: Catalyzes the synthesis of D-serine from L-serine. D-serine is a key coagonist with glutamate at NMDA receptors. Has dehydratase activity towards both L-serine and D-serine. {ECO:0000269|PubMed:10557334, ECO:0000269|PubMed:12393813, ECO:0000269|PubMed:12515328, ECO:0000269|PubMed:15536068, ECO:0000269|PubMed:17293453}. PTM: S-nitrosylated, leading to decrease the enzyme activity. {ECO:0000269|PubMed:17293453}. SUBUNIT: Homodimer. {ECO:0000269|PubMed:12515328}. TISSUE SPECIFICITY: Detected in brain (at protein level). Brain. +Q62093 SRSF2_MOUSE Serine/arginine-rich splicing factor 2 (Protein PR264) (Putative myelin regulatory factor 1) (MRF-1) (Splicing component, 35 kDa) (Splicing factor SC35) (SC-35) (Splicing factor, arginine/serine-rich 2) 221 25,476 Chain (1); Compositional bias (2); Domain (1); Frameshift (1); Initiator methionine (1); Modified residue (13); Sequence conflict (4) FUNCTION: Necessary for the splicing of pre-mRNA. It is required for formation of the earliest ATP-dependent splicing complex and interacts with spliceosomal components bound to both the 5'- and 3'-splice sites during spliceosome assembly. It also is required for ATP-dependent interactions of both U1 and U2 snRNPs with pre-mRNA (By similarity). Can bind to the myelin basic protein (MBP) gene MB3 regulatory region and increase transcription of the mbp promoter in cells derived from the CNS. The phosphorylated form (by SRPK2) is required for cellular apoptosis in response to cisplatin treatment (By similarity). {ECO:0000250, ECO:0000269|PubMed:7527040}. PTM: Extensively phosphorylated on serine residues in the RS domain. Phosphorylated by SRPK2 and this causes its redistribution from the nuclear speckle to nucleoplasm and controls cell fate decision in response to cisplatin treatment. KAT5/TIP60 inhibits its phosphorylation by preventing SRPK2 nuclear translocation (By similarity). {ECO:0000250}.; PTM: Acetylation on Lys-52 by KAT5/TIP60 promotes its proteasomal degradation. This effect is counterbalanced by HDAC6, which positively controls SRSF2 protein level by deacetylating it and preventing its proteasomal degradation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Nucleus speckle {ECO:0000250}. Note=Phosphorylation by SRPK2 provokes its redistribution from the nuclear specke to nucleoplasm. {ECO:0000250}. SUBUNIT: Interacts with CCNL1 and CCNL2. Interacts with SCAF11. Interacts with ZRSR2/U2AF1-RS2. Interacts with CCDC55 (via C-terminus) (By similarity). In vitro, self-associates and binds SRSF1/SFRS1 (ASF/SF2), SNRNP70 and U2AF1 but not U2AF2. Binds SREK1/SFRS12. Interacts with BRDT. {ECO:0000250, ECO:0000269|PubMed:22570411}. TISSUE SPECIFICITY: Expressed in all the tissues examined; liver, kidney, spleen, heart, lung and brain. {ECO:0000269|PubMed:7527040}. +Q9R0U0 SRS10_MOUSE Serine/arginine-rich splicing factor 10 (FUS-interacting serine-arginine-rich protein 1) (Neural-salient serine/arginine-rich protein) (Neural-specific SR protein) (Splicing factor, arginine/serine-rich 13A) (TLS-associated protein with Ser-Arg repeats) (TASR) (TLS-associated protein with SR repeats) (TLS-associated serine-arginine protein) (TLS-associated SR protein) 262 31,301 Alternative sequence (3); Chain (1); Compositional bias (1); Domain (1); Modified residue (10); Sequence conflict (3) FUNCTION: Splicing factor that in its dephosphorylated form acts as a general repressor of pre-mRNA splicing. Seems to interfere with the U1 snRNP 5'-splice recognition of SNRNP70. Required for splicing repression in M-phase cells and after heat shock. Also acts as a splicing factor that specifically promotes exon skipping during alternative splicing. Interaction with YTHDC1, a RNA-binding protein that recognizes and binds N6-methyladenosine (m6A)-containing RNAs, prevents SRSF10 from binding to its mRNA-binding sites close to m6A-containing regions, leading to inhibit exon skipping during alternative splicing (By similarity). May be involved in regulation of alternative splicing in neurons (PubMed:10583508). {ECO:0000250|UniProtKB:O75494, ECO:0000269|PubMed:10583508}. PTM: Phosphorylated. Fully dephosphorylated in mitosis and partially dephosphorylated on heat shock. {ECO:0000250|UniProtKB:O75494}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:10583508}. SUBUNIT: The phosphorylated but not the dephosphorylated form interacts with TRA2B/SFRS10. The dephosphorylated form interacts with SNRNP70. Interacts with FUS C-terminus. Interacts with YTHDC1, leading to inhibit RNA-binding activity of SRSF10. {ECO:0000250|UniProtKB:O75494}. TISSUE SPECIFICITY: Widely expressed, with high levels in brain and testis. {ECO:0000269|PubMed:10583508}. +Q8BL97 SRSF7_MOUSE Serine/arginine-rich splicing factor 7 (Splicing factor, arginine/serine-rich 7) 267 30,818 Alternative sequence (4); Chain (1); Compositional bias (1); Cross-link (1); Domain (1); Modified residue (12); Region (2); Repeat (6); Sequence conflict (6); Zinc finger (1) FUNCTION: Required for pre-mRNA splicing. Represses the splicing of MAPT/Tau exon 10. May function as export adapter involved in mRNA nuclear export such as of histone H2A. Binds mRNA which is thought to be transferred to the NXF1-NXT1 heterodimer for export (TAP/NXF1 pathway); enhances NXF1-NXT1 RNA-binding activity. RNA-binding is semi-sequence specific (By similarity). {ECO:0000250}. PTM: Extensively phosphorylated on serine residues in the RS domain. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. SUBUNIT: Found in large molecular weight complexes containing CCNL1 and the p110 isoforms of either CDC2L1 or CDC2L2. Interacts with CCNL2 and CPSF6. Interacts with NXF1 (By similarity). {ECO:0000250}. +Q9D0B0 SRSF9_MOUSE Serine/arginine-rich splicing factor 9 (Splicing factor, arginine/serine-rich 9) 222 25,661 Beta strand (5); Chain (1); Compositional bias (2); Cross-link (1); Domain (2); Helix (2); Modified residue (9); Region (1); Sequence conflict (1); Turn (1) FUNCTION: Plays a role in constitutive splicing and can modulate the selection of alternative splice sites. Represses the splicing of MAPT/Tau exon 10 (By similarity). {ECO:0000250}. PTM: Extensively phosphorylated on serine residues in the RS domain. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with KHDRBS3/SLM-2 (PubMed:11118435). Interacts with HABP4. Interacts with NOL3/ARC/NOP30, NSEP1/YB-1/YB1, SAFB/SAFB1, SRSF6/SFRS6, TRA2B/SFRS10 and C1QBP. May also interact with DUSP11/PIR1 (By similarity). {ECO:0000250|UniProtKB:Q13242, ECO:0000269|PubMed:11118435}. +Q05738 SRY_MOUSE Sex-determining region Y protein (Testis-determining factor) 395 49,494 Chain (1); DNA binding (1); Modified residue (1); Mutagenesis (1); Natural variant (7); Region (6) FUNCTION: Transcriptional regulator that controls a genetic switch in male development. It is necessary and sufficient for initiating male sex determination by directing the development of supporting cell precursors (pre-Sertoli cells) as Sertoli rather than granulosa cells. In male adult brain involved in the maintenance of motor functions of dopaminergic neurons (By similarity). Involved in different aspects of gene regulation including promoter activation or repression. SRY HMG box recognizes DNA by partial intercalation in the minor groove. Promotes DNA bending. Also involved in pre-mRNA splicing (By similarity). Binds to the DNA consensus sequence 5'-[AT]AACAA[AT]-3'. {ECO:0000250, ECO:0000269|PubMed:15170344}. PTM: Phosphorylated on serine residues by PKA. Phosphorylation by PKA enhances its DNA-binding activity and stimulates transcription repression. {ECO:0000250}.; PTM: Acetylation of Lys-81 contributes to its nuclear localization and enhances its interaction with KPNB1. {ECO:0000269|PubMed:15297880}.; PTM: Poly-ADP-ribosylated by PARP1 (By similarity). ADP-ribosylation reduces its DNA-binding activity. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q05066}. Cytoplasm {ECO:0000269|PubMed:11535586, ECO:0000269|PubMed:15469996, ECO:0000269|PubMed:16488877}. Nucleus {ECO:0000250|UniProtKB:Q05066}. Note=Acetylation contributes to its nuclear localization and deacetylation by HDAC3 induces a cytoplasmic delocalization (By similarity). Colocalizes in the nucleus with ZNF208 isoform KRAB-O and tyrosine hydroxylase (TH) (PubMed:15469996). Colocalizes with SOX6 in speckles. Colocalizes with CAML in the nucleus (By similarity). {ECO:0000250|UniProtKB:Q05066, ECO:0000269|PubMed:15469996}. SUBUNIT: Interacts with KPNB1, ZNF208 isoform KRAB-O, PARP1 and SLC9A3R2. The interaction with KPNB1 is sensitive to dissociation by Ran in the GTP-bound form. Interaction with PARP1 impaired its DNA-binding activity. Interacts with CALM, EP300, HDAC3 and WT1 (By similarity). The interaction with EP300 modulates its DNA-binding activity (By similarity). {ECO:0000250}. DOMAIN: DNA binding and bending properties of the HMG domains of mouse and human SRY differ form each other. Mouse SRY shows less extensive minor groove contacts with DNA and a higher specificity of sequence recognition than human SRY. TISSUE SPECIFICITY: Expressed in the substantia nigra of the brain (at protein level). Expressed in diencephalon, cortex, the substantia nigra of the midbrain and the medial mammillary bodies of the hypothalamus of male, but not female. {ECO:0000269|PubMed:11085593, ECO:0000269|PubMed:15469996, ECO:0000269|PubMed:16488877}. +P56873 SSA27_MOUSE Sjoegren syndrome/scleroderma autoantigen 1 homolog (Autoantigen p27 homolog) (Protein C184L) 199 21,336 Chain (1); Initiator methionine (1); Modified residue (2) TISSUE SPECIFICITY: Expressed in the early postnatal brain. {ECO:0000269|PubMed:10512749}. +Q9CYZ8 SSBP2_MOUSE Single-stranded DNA-binding protein 2 (Sequence-specific single-stranded-DNA-binding protein 2) 361 37,846 Alternative sequence (1); Chain (1); Compositional bias (2); Domain (1); Modified residue (3) SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +Q9D032 SSBP3_MOUSE Single-stranded DNA-binding protein 3 (Lck-associated signal transducer) (Sequence-specific single-stranded-DNA-binding protein) 388 40,421 Alternative sequence (1); Chain (1); Compositional bias (2); Domain (1); Modified residue (10); Sequence conflict (3) FUNCTION: May be involved in transcription regulation of the alpha 2(I) collagen gene where it binds to the single-stranded polypyrimidine sequences in the promoter region. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +Q76I79 SSH1_MOUSE Protein phosphatase Slingshot homolog 1 (EC 3.1.3.16) (EC 3.1.3.48) (SSH-like protein 1) (SSH-1L) (mSSH-1L) 1042 115,297 Active site (1); Alternative sequence (1); Chain (1); Domain (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (6); Mutagenesis (1); Region (1); Sequence conflict (6) FUNCTION: Protein phosphatase which regulates actin filament dynamics. Dephosphorylates and activates the actin binding/depolymerizing factor cofilin, which subsequently binds to actin filaments and stimulates their disassembly. Inhibitory phosphorylation of cofilin is mediated by LIMK1, which may also be dephosphorylated and inactivated by this protein. {ECO:0000269|PubMed:14531860}. PTM: Phosphorylated. Inhibitory phosphorylation by PAK4 promotes binding to YWHAZ. Phosphorylation at Ser-970 is decreased by stimuli which promote actin reorganization and lamellipodia formation. Can be dephosphorylated and activated by PPP3CA/calcineurin A. Phosphorylation decreases immediately prior to telophase (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:14531860}. Cleavage furrow {ECO:0000250}. Midbody {ECO:0000250}. Note=Localized to the cleavage furrow and the midbody during cytokinesis (By similarity). Also colocalizes with F-actin in the cytoplasm and the cell periphery, which may allow local control of actin dynamics at sites of cell locomotion. {ECO:0000250}. SUBUNIT: Interacts with the 14-3-3 proteins YWHAB, YWHAG, YWHAQ, and YWHAZ. Interaction with 14-3-3 proteins inhibits phosphatase activity and also blocks recruitment to lamellipodia and stimulation by actin (By similarity). Interacts with actin and this stimulates phosphatase activity. Interacts with LIMK1. {ECO:0000250, ECO:0000269|PubMed:14531860, ECO:0000269|PubMed:15660133}. TISSUE SPECIFICITY: Expressed in brain, heart, kidney and thymus. Also expressed at lower levels in liver, skeletal muscle, small intestine and spleen. {ECO:0000269|PubMed:14531860}. +Q8CG65 SSPO_MOUSE SCO-spondin 4998 534,975 Chain (1); Disulfide bond (104); Domain (53); Glycosylation (43); Sequence conflict (8); Signal peptide (1) FUNCTION: Involved in the modulation of neuronal aggregation. May be involved in developmental events during the formation of the central nervous system (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250}. TISSUE SPECIFICITY: Subcommissural organ. {ECO:0000269|PubMed:12909363}. +P30873 SSR1_MOUSE Somatostatin receptor type 1 (SS-1-R) (SS1-R) (SS1R) (SRIF-2) 391 42,718 Chain (1); Disulfide bond (1); Glycosylation (3); Lipidation (1); Topological domain (8); Transmembrane (7) TRANSMEM 57 84 Helical; Name=1. {ECO:0000255}.; TRANSMEM 95 120 Helical; Name=2. {ECO:0000255}.; TRANSMEM 132 153 Helical; Name=3. {ECO:0000255}.; TRANSMEM 176 196 Helical; Name=4. {ECO:0000255}.; TRANSMEM 220 244 Helical; Name=5. {ECO:0000255}.; TRANSMEM 271 296 Helical; Name=6. {ECO:0000255}.; TRANSMEM 304 327 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 56 Extracellular. {ECO:0000255}.; TOPO_DOM 85 94 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 121 131 Extracellular. {ECO:0000255}.; TOPO_DOM 154 175 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 197 219 Extracellular. {ECO:0000255}.; TOPO_DOM 245 270 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 297 303 Extracellular. {ECO:0000255}.; TOPO_DOM 328 391 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for somatostatin with higher affinity for somatostatin-14 than -28. This receptor is coupled via pertussis toxin sensitive G proteins to inhibition of adenylyl cyclase. In addition it stimulates phosphotyrosine phosphatase and Na(+)/H(+) exchanger via pertussis toxin insensitive G proteins. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Jejunum and stomach. +P49660 SSR4_MOUSE Somatostatin receptor type 4 (SS-4-R) (SS4-R) (SS4R) 385 41,932 Chain (1); Disulfide bond (1); Glycosylation (1); Lipidation (1); Sequence conflict (5); Topological domain (8); Transmembrane (7) TRANSMEM 43 70 Helical; Name=1. {ECO:0000255}.; TRANSMEM 81 106 Helical; Name=2. {ECO:0000255}.; TRANSMEM 118 139 Helical; Name=3. {ECO:0000255}.; TRANSMEM 162 182 Helical; Name=4. {ECO:0000255}.; TRANSMEM 205 229 Helical; Name=5. {ECO:0000255}.; TRANSMEM 256 281 Helical; Name=6. {ECO:0000255}.; TRANSMEM 289 312 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 42 Extracellular. {ECO:0000255}.; TOPO_DOM 71 80 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 107 117 Extracellular. {ECO:0000255}.; TOPO_DOM 140 161 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 183 204 Extracellular. {ECO:0000255}.; TOPO_DOM 230 255 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 282 288 Extracellular. {ECO:0000255}.; TOPO_DOM 313 385 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for somatostatin-14. The activity of this receptor is mediated by G proteins which inhibits adenylyl cyclase. It is functionally coupled not only to inhibition of adenylate cyclase, but also to activation of both arachidonate release and mitogen-activated protein (MAP) kinase cascade. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q08943 SSRP1_MOUSE FACT complex subunit SSRP1 (Facilitates chromatin transcription complex subunit SSRP1) (Recombination signal sequence recognition protein 1) (Structure-specific recognition protein 1) (T160) 708 80,860 Alternative sequence (1); Chain (1); Compositional bias (5); Cross-link (3); DNA binding (1); Frameshift (1); Initiator methionine (1); Modified residue (18); Sequence conflict (6); Site (1) FUNCTION: Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II. The FACT complex is probably also involved in phosphorylation of 'Ser-392' of p53/TP53 via its association with CK2 (casein kinase II). Binds specifically to double-stranded DNA. Also acts as a transcriptional coactivator for p63/TP63. {ECO:0000269|PubMed:23364797}. PTM: Phosphorylated by CK2 following UV but not gamma irradiation. Phosphorylation inhibits its DNA-binding activity (By similarity). {ECO:0000250}.; PTM: Ubiquitinated. Polyubiquitinated following caspase cleavage resulting in degradation of the N-terminal ubiquitinated part of the cleaved protein (By similarity). {ECO:0000250}.; PTM: Sumoylated. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q05344}. Chromosome {ECO:0000250|UniProtKB:Q05344}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q05344}. Note=Colocalizes with RNA polymerase II on chromatin. Recruited to actively transcribed loci. {ECO:0000250|UniProtKB:Q05344}. SUBUNIT: Interacts with MYOG (via C-terminal region) (PubMed:23364797). Component of the FACT complex, a stable heterodimer of SSRP1 and SUPT16H. Also component of a CK2-SPT16-SSRP1 complex which forms following UV irradiation, composed of SSRP1, SUPT16H, CSNK2A1, CSNK2A2 and CSNK2B. Binds to histone H3-H4 tetramers, but not to intact nucleosomes. Identified in a centromere complex containing histones H2A, H2B and H4, and at least CENPA, CENPB, CENPC, CENPT, CENPN, HJURP, SUPT16H, SSRP1 and RSF1. Interacts with isoform gamma of TP63. Interacts with FYTTD1/UIF (By similarity). Interacts with SRF (By similarity). Interacts with NEK9 (By similarity). {ECO:0000250|UniProtKB:Q04931, ECO:0000250|UniProtKB:Q08945, ECO:0000269|PubMed:23364797}. +Q9DC77 SMPX_MOUSE Small muscular protein (Stretch-responsive skeletal muscle protein) (Chisel protein) 85 9,253 Chain (1); Modified residue (2); Sequence conflict (1) FUNCTION: Plays a role in the regulatory network through which muscle cells coordinate their structural and functional states during growth, adaptation, and repair. {ECO:0000269|PubMed:11381084}. TISSUE SPECIFICITY: Abundantly expressed in heart and skeletal muscle. Expression is increased by passive stretch. {ECO:0000269|PubMed:10598820, ECO:0000269|PubMed:11401441}. +Q9Z266 SNAPN_MOUSE SNARE-associated protein Snapin (Biogenesis of lysosome-related organelles complex 1 subunit 7) (BLOC-1 subunit 7) (Synaptosomal-associated protein 25-binding protein) (SNAP-associated protein) 136 14,904 Alternative sequence (2); Chain (1); Coiled coil (1); Initiator methionine (1); Modified residue (7); Mutagenesis (4); Region (1) FUNCTION: Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. Plays a role in intracellular vesicle trafficking and synaptic vesicle recycling. May modulate a step between vesicle priming, fusion and calcium-dependent neurotransmitter release through its ability to potentiate the interaction of synaptotagmin with the SNAREs and the plasma-membrane-associated protein SNAP25. Its phosphorylation state influences exocytotic protein interactions and may regulate synaptic vesicle exocytosis. May also have a role in the mechanisms of SNARE-mediated membrane fusion in non-neuronal cells (PubMed:16760431, PubMed:19546860, PubMed:21998198). As part of the BORC complex may play a role in lysosomes movement and localization at the cell periphery. Associated with the cytosolic face of lysosomes, the BORC complex may recruit ARL8B and couple lysosomes to microtubule plus-end-directed kinesin motor (By similarity). {ECO:0000250|UniProtKB:O95295, ECO:0000269|PubMed:16760431, ECO:0000269|PubMed:19546860, ECO:0000269|PubMed:21998198}. PTM: Phosphorylated by PKD, phosphorylation controls SNAPIN protein stability (By similarity). Phosphorylated by CSNK1D/CK1. {ECO:0000250, ECO:0000269|PubMed:11283605, ECO:0000269|PubMed:17101137}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12877659}; Peripheral membrane protein {ECO:0000269|PubMed:12877659}; Cytoplasmic side {ECO:0000269|PubMed:12877659}. Cytoplasm, cytosol {ECO:0000269|PubMed:12877659}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:12877659}. Golgi apparatus membrane {ECO:0000269|PubMed:17101137}. Lysosome membrane {ECO:0000250|UniProtKB:O95295}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:11283605}. Note=Colocalizes with NANOS1 and PUM2 in the perinuclear region of germ cells. {ECO:0000250|UniProtKB:O95295}. SUBUNIT: Component of the biogenesis of lysosome-related organelles complex 1 (BLOC-1) composed of BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. Octamer composed of one copy each BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. The BLOC-1 complex associates with the AP-3 protein complex and membrane protein cargos (PubMed:21998198). Component of the BLOC-one-related complex (BORC) which is composed of BLOC1S1, BLOC1S2, BORCS5, BORCS6, BORCS7, BORCS8, KXD1 and SNAPIN (By similarity). Associates with the SNARE complex. Interacts with CSNK1D, SNAP23 and STX4A but not with STX1A, VAMP2 and SYT1 (PubMed:12877659, PubMed:17101137). Interacts with SNAP25; the interaction with SNAP25 is increased by its phosphorylation (PubMed:10195194, PubMed:11283605). Interacts with CNTRL, NANOS1, PUM2 and RGS7. Interacts with TOR1A; the interaction is direct and associates SNAPIN with the CSN complex (By similarity). {ECO:0000250|UniProtKB:O95295, ECO:0000269|PubMed:10195194, ECO:0000269|PubMed:11283605, ECO:0000269|PubMed:12877659, ECO:0000269|PubMed:17101137, ECO:0000269|PubMed:21998198}. TISSUE SPECIFICITY: Strongly expressed in heart, brain, testis, kidney and liver; low expression in spleen, lung and skeletal muscle. In the testis, expressed in the seminiferous tubules. {ECO:0000269|PubMed:12877659, ECO:0000269|PubMed:19168546}. +Q9Z1L2 SNG4_MOUSE Synaptogyrin-4 233 25,795 Chain (1); Domain (1); Sequence conflict (3); Transmembrane (4) TRANSMEM 25 45 Helical. {ECO:0000255}.; TRANSMEM 66 86 Helical. {ECO:0000255}.; TRANSMEM 104 124 Helical. {ECO:0000255}.; TRANSMEM 145 165 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. +A2KF29 SMKTR_MOUSE Sperm motility kinase Tcr mutant form (SmokTcr) (Tcr) (EC 2.7.11.1) (Dominant negative form of Smok) (Responder protein Smok-Tcr) 484 54,619 Active site (1); Binding site (1); Chain (1); Domain (1); Nucleotide binding (1) FUNCTION: While the main function of Smoks is to control sperm motility, the role of Smok-Tcr, with reduced kinase activity, is to counterbalance a signaling impairment caused by the distorter/sterility loci, giving t-sperm an advantage in reaching the oocytes. Transmission ratio distortion also called segregation distortion is the name given to the phenomenon above-mentioned. Being associated with the T-complex, it allows males heterozygous for a complete t-haplotype to preferentially transmit the t-haplotype chromosome. {ECO:0000269|PubMed:10647005}. TISSUE SPECIFICITY: Testis-specific. Expressed in the testis from 22 days postpartum (22 dpp). Expressed late in spermiogenesis, only in Tcr-containing t-haplotypes. {ECO:0000269|PubMed:10647005}. +Q99LM3 SMTL1_MOUSE Smoothelin-like protein 1 (Calponin homology-associated smooth muscle protein) (CHASM) 459 49,525 Beta strand (2); Chain (1); Coiled coil (1); Domain (1); Helix (8); Modified residue (1); Mutagenesis (1); Region (1) FUNCTION: Plays a role in the regulation of contractile properties of both striated and smooth muscles. When unphosphorylated, may inhibit myosin dephosphorylation. Phosphorylation at Ser-301 reduces this inhibitory activity. {ECO:0000269|PubMed:18310078, ECO:0000269|PubMed:20634291}. PTM: Maximal phosphorylation of Ser-301 correlates with maximal relaxation of aorta in response to acetylcholine. {ECO:0000269|PubMed:15327999, ECO:0000269|PubMed:18310078, ECO:0000269|PubMed:20634291}. SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, I band. Cytoplasm, myofibril, sarcomere, M line. Nucleus. Note=Colocalizes with MYH2. In its unphosphorylated state, localizes to the cytoplasm. Phosphorylation at Ser-301 promotes translocation to the nucleus. SUBUNIT: Interacts with PPP1R12A. {ECO:0000269|PubMed:20634291}. TISSUE SPECIFICITY: Widely expressed, with highest expression in skeletal muscles (at protein level). Within striated muscles, significantly more expressed in soleus muscle compared with plantaris muscle or white vastus (at protein level). 30-40% lower expression in females than in males (at protein level). Expressed in type 2a fibers, but not detected in fast twitch type 2b muscle white vastus nor in oxidative type I/b heart muscle (at protein level). Expressed within myometrial cells of the uterus, as well as in the endometrial layer. In the aorta, confined to smooth muscle cells. Not detected in endothelial cells. {ECO:0000269|PubMed:18310078, ECO:0000269|PubMed:20634291}. +O35985 SMR2C_MOUSE Submaxillary gland androgen-regulated protein 2, isoform gamma (Salivary protein MSG2, isoform gamma) 143 16,158 Chain (1); Signal peptide (1) FUNCTION: May play a role in protection or detoxification. SUBCELLULAR LOCATION: Secreted. +Q80ZU4 SMI19_MOUSE Small integral membrane protein 19 107 12,283 Chain (1); Erroneous initiation (4); Transmembrane (1) TRANSMEM 25 43 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +O35716 SOCS1_MOUSE Suppressor of cytokine signaling 1 (SOCS-1) (JAK-binding protein) (JAB) (STAT-induced STAT inhibitor 1) (SSI-1) 212 23,715 Chain (1); Compositional bias (1); Domain (2); Mutagenesis (25); Region (3); Sequence conflict (2) Protein modification; protein ubiquitination. FUNCTION: SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. SOCS1 is involved in negative regulation of cytokines that signal through the JAK/STAT3 pathway. Through binding to JAKs, inhibits their kinase activity. In vitro, also suppresses Tec protein-tyrosine activity (By similarity). Appears to be a major regulator of signaling by interleukin 6 (IL6) and leukemia inhibitory factor (LIF). Regulates interferon-gamma mediated sensory neuron survival. Probable substrate recognition component of an ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Seems to recognize JAK2 (By similarity). SOCS1 appears to be a negative regulator in IGF1R signaling pathway (By similarity). {ECO:0000250|UniProtKB:O15524, ECO:0000269|PubMed:10064597, ECO:0000269|PubMed:15169905, ECO:0000269|PubMed:24880459}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O15524}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:O15524}. Note=Detected in perinuclear cytoplasmic vesicles upon interaction with FGFR3. {ECO:0000250|UniProtKB:O15524}. SUBUNIT: Interacts with multiple activated proteins of the tyrosine kinase signaling pathway including JAK family kinases, TEC, KIT, GRB2 and VAV. Binding to JAKs is mediated through the KIR and SH2 domain to a phosphorylated tyrosine residue within the JAK JH1 domain. Binds the SH3 domain of GRB2 via diproline determinants in the N-terminus, and the N-terminal regulatory domain of VAV. Interacts with the Elongin BC complex (ELOB and ELOC). Component of an ECS CBC(SOCS1) E3 ubiquitin-protein ligase complex which contains Elongin BC, CUL5, RBX1 and SOCS1. Interacts (via SH2 domain and SOCS box) with TRIM8. Interacts with CUL2. Interacts with AXL and FGFR3 (By similarity). Interacts with INSR. Interacts with TRIM8 (By similarity). {ECO:0000250|UniProtKB:O15524, ECO:0000269|PubMed:10051596, ECO:0000269|PubMed:12163497, ECO:0000269|PubMed:15169905, ECO:0000269|PubMed:9869640}. DOMAIN: The ESS and SH2 domains are required for JAK phosphotyrosine binding. Further interaction with the KIR domain is necessary for signal and kinase inhibition.; DOMAIN: The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin ligase complexes. The Elongin BC complex binding domain is also known as BC-box with the consensus [APST]-L-x(3)-C-x(3)-[AILV] and is part of the SOCS box. TISSUE SPECIFICITY: High expression in thymus. Lower expression in lung and spleen. Expressed in both Th1 and Th2 cells. {ECO:0000269|PubMed:12242343}. +P09671 SODM_MOUSE Superoxide dismutase [Mn], mitochondrial (EC 1.15.1.1) 222 24,603 Chain (1); Metal binding (4); Modified residue (11); Mutagenesis (1); Sequence conflict (4); Transit peptide (1) FUNCTION: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. PTM: Nitrated under oxidative stress. Nitration coupled with oxidation inhibits the catalytic activity (By similarity). {ECO:0000250|UniProtKB:P04179}.; PTM: Acetylation at Lys-122 decreases enzymatic activity. Deacetylated by SIRT3 upon exposure to ionizing radiations or after long fasting. {ECO:0000269|PubMed:21172655}.; PTM: Polyubiquitinated; leading to proteasomal degradation. Deubiquitinated by USP36 which increases protein stability. {ECO:0000250|UniProtKB:P04179}. SUBCELLULAR LOCATION: Mitochondrion matrix. SUBUNIT: Homotetramer. +Q91VH2 SNX9_MOUSE Sorting nexin-9 595 66,546 Beta strand (6); Binding site (4); Chain (1); Domain (3); Modified residue (4); Region (1); Turn (1) FUNCTION: Involved in endocytosis and intracellular vesicle trafficking, both during interphase and at the end of mitosis. Required for efficient progress through mitosis and cytokinesis. Required for normal formation of the cleavage furrow at the end of mitosis. Plays a role in endocytosis via clathrin-coated pits, but also clathrin-independent, actin-dependent fluid-phase endocytosis. Plays a role in macropinocytosis. Promotes internalization of TNFR. Promotes degradation of EGFR after EGF signaling. Stimulates the GTPase activity of DNM1. Promotes DNM1 oligomerization. Promotes activation of the Arp2/3 complex by WASL, and thereby plays a role in the reorganization of the F-actin cytoskeleton. Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate and promotes membrane tubulation. Has lower affinity for membranes enriched in phosphatidylinositol 3-phosphate (By similarity). {ECO:0000250}. PTM: Phosphorylated on tyrosine residues by TNK2. Phosphorylation promotes its activity in the degradation of EGFR (By similarity). {ECO:0000250}.; PTM: Ubiquitinated by ITCH. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Cell projection, ruffle {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Localized at sites of endocytosis at the cell membrane. Detected on newly formed macropinosomes. Transiently recruited to clathrin-coated pits at a late stage of clathrin-coated vesicle formation (By similarity). Colocalizes with the actin cytoskeleton at the cell membrane (By similarity). {ECO:0000250}. SUBUNIT: Homodimer, and homooligomer. Heterodimer with SNX18. Interacts with ITCH. Interacts (via SH3 domain) with TNK2, WASL and ARP3. Identified in a complex with TNK2 and clathrin heavy chains. Identified in a complex with the AP-2 complex, clathrin and DNM2. Interacts (via SH3 domain) with DNM1 and DNM2. Identified in an oligomeric complex containing DNM1 and SNX9 (By similarity). Interacts with ADAM9 and ADAM15 cytoplasmic tails. {ECO:0000250, ECO:0000269|PubMed:10531379}. DOMAIN: The PX domain mediates interaction with membranes enriched in phosphatidylinositol phosphate. Has high affinity for phosphatidylinositol 4,5-bisphosphate, but can also bind to membranes enriched in other phosphatidylinositol phosphates (By similarity). {ECO:0000250}. +P08228 SODC_MOUSE Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) 154 15,943 Beta strand (11); Chain (1); Disulfide bond (1); Helix (2); Initiator methionine (1); Lipidation (1); Metal binding (8); Modified residue (11); Sequence conflict (1); Turn (1) FUNCTION: Destroys radicals which are normally produced within the cells and which are toxic to biological systems. PTM: Palmitoylation helps nuclear targeting and decreases catalytic activity. {ECO:0000250}.; PTM: Succinylation, adjacent to copper catalytic site, probably inhibits activity. Desuccinylation by SIRT5 enhances activity. {ECO:0000250|UniProtKB:P00441}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000269|PubMed:20727846}. +Q9EP96 SO1A4_MOUSE Solute carrier organic anion transporter family member 1A4 (Sodium-independent organic anion-transporting polypeptide 2) (Solute carrier family 21 member 5) 670 73,965 Chain (1); Disulfide bond (3); Domain (1); Glycosylation (4); Modified residue (2); Topological domain (13); Transmembrane (12) TRANSMEM 21 40 Helical; Name=1. {ECO:0000255}.; TRANSMEM 60 80 Helical; Name=2. {ECO:0000255}.; TRANSMEM 87 111 Helical; Name=3. {ECO:0000255}.; TRANSMEM 156 184 Helical; Name=4. {ECO:0000255}.; TRANSMEM 204 224 Helical; Name=5. {ECO:0000255}.; TRANSMEM 243 267 Helical; Name=6. {ECO:0000255}.; TRANSMEM 312 333 Helical; Name=7. {ECO:0000255}.; TRANSMEM 354 377 Helical; Name=8. {ECO:0000255}.; TRANSMEM 382 405 Helical; Name=9. {ECO:0000255}.; TRANSMEM 514 536 Helical; Name=10. {ECO:0000255}.; TRANSMEM 546 571 Helical; Name=11. {ECO:0000255}.; TRANSMEM 606 623 Helical; Name=12. {ECO:0000255}. TOPO_DOM 1 20 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 41 59 Extracellular. {ECO:0000255}.; TOPO_DOM 81 86 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 112 155 Extracellular. {ECO:0000255}.; TOPO_DOM 185 203 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 225 242 Extracellular. {ECO:0000255}.; TOPO_DOM 268 311 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 334 353 Extracellular. {ECO:0000255}.; TOPO_DOM 378 381 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 406 513 Extracellular. {ECO:0000255}.; TOPO_DOM 537 545 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 572 605 Extracellular. {ECO:0000255}.; TOPO_DOM 624 670 Cytoplasmic. {ECO:0000255}. FUNCTION: Mediates the Na(+)-independent transport of organic anions such as taurocholate, cholate, 17-beta-glucuronosyl estradiol, estrone-3-sulfate, the cardiac glycosides ouabain and digoxin and thyroid hormones. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Highly expressed in brain and liver. Detected at very low levels in heart and lung. +Q64105 SPRE_MOUSE Sepiapterin reductase (SPR) (EC 1.1.1.153) 261 27,883 Beta strand (8); Binding site (5); Chain (1); Helix (11); Modified residue (5); Nucleotide binding (4); Region (1); Sequence conflict (1) FUNCTION: Catalyzes the final one or two reductions in tetra-hydrobiopterin biosynthesis to form 5,6,7,8-tetrahydrobiopterin. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Homodimer. {ECO:0000269|PubMed:9405351}. +P70663 SPRL1_MOUSE SPARC-like protein 1 (Extracellular matrix protein 2) (Matrix glycoprotein Sc1) 650 72,287 Calcium binding (1); Chain (1); Compositional bias (2); Disulfide bond (7); Domain (3); Glycosylation (3); Modified residue (8); Sequence conflict (11); Signal peptide (1) SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. TISSUE SPECIFICITY: Highest expression in brain. Moderate levels in heart, adrenal gland, epididymis and lung. Low levels in kidney, eye, liver, spleen, submandibular gland and testis. +Q6P6N5 SPRE3_MOUSE Sprouty-related, EVH1 domain-containing protein 3 (Spred-3) 408 42,794 Chain (1); Compositional bias (3); Domain (3); Modified residue (2); Sequence conflict (1) FUNCTION: Tyrosine kinase substrate that inhibits growth-factor-mediated activation of MAP kinase. PTM: Phosphorylated on tyrosine. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12646235}; Peripheral membrane protein {ECO:0000269|PubMed:12646235}. SUBUNIT: Interacts with Ras. {ECO:0000250}. TISSUE SPECIFICITY: Brain specific. {ECO:0000269|PubMed:12646235}. +Q3TD49 SPP2B_MOUSE Signal peptide peptidase-like 2B (SPP-like 2B) (SPPL2b) (EC 3.4.23.-) 578 63,824 Active site (2); Alternative sequence (2); Chain (1); Compositional bias (1); Domain (1); Glycosylation (2); Motif (1); Sequence conflict (6); Signal peptide (1); Topological domain (10); Transmembrane (9) TRANSMEM 169 189 Helical. {ECO:0000255}.; TRANSMEM 217 237 Helical. {ECO:0000255}.; TRANSMEM 240 260 Helical. {ECO:0000255}.; TRANSMEM 287 307 Helical. {ECO:0000255}.; TRANSMEM 313 333 Helical. {ECO:0000255}.; TRANSMEM 342 362 Helical. {ECO:0000255}.; TRANSMEM 406 426 Helical. {ECO:0000255}.; TRANSMEM 439 459 Helical. {ECO:0000255}.; TRANSMEM 464 484 Helical. {ECO:0000255}. TOPO_DOM 20 168 Lumenal. {ECO:0000250|UniProtKB:Q8TCT7}.; TOPO_DOM 190 216 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 238 239 Lumenal. {ECO:0000255}.; TOPO_DOM 261 286 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 308 312 Lumenal. {ECO:0000255}.; TOPO_DOM 334 341 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 363 405 Lumenal. {ECO:0000250|UniProtKB:Q8TCT7}.; TOPO_DOM 427 438 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 460 463 Lumenal. {ECO:0000255}.; TOPO_DOM 485 578 Cytoplasmic. {ECO:0000250|UniProtKB:Q8TCT7}. FUNCTION: Intramembrane-cleaving aspartic protease (I-CLiP) that cleaves type II membrane signal peptides in the hydrophobic plane of the membrane. Functions in ITM2B and TNF processing. Catalyzes the intramembrane cleavage of the anchored fragment of shed TNF-alpha (TNF), which promotes the release of the intracellular domain (ICD) for signaling to the nucleus. May play a role in the regulation of innate and adaptive immunity. {ECO:0000250|UniProtKB:Q8TCT7}. PTM: Glycosylated. {ECO:0000250|UniProtKB:Q8TCT7}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21896273}; Multi-pass membrane protein {ECO:0000305}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q8TCT7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8TCT7}. Lysosome membrane {ECO:0000250|UniProtKB:Q8TCT7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8TCT7}. Endosome membrane {ECO:0000250|UniProtKB:Q8TCT7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8TCT7}. Membrane {ECO:0000250|UniProtKB:Q8TCT7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8TCT7}; Lumenal side {ECO:0000250|UniProtKB:Q8TCT7}. Note=targeted through the entire secretory pathway to endosomes/lysosomes. {ECO:0000250|UniProtKB:Q8TCT7}. SUBUNIT: Monomer. Homodimer. Interacts with ITM2B and TNF. {ECO:0000250|UniProtKB:Q8TCT7}. DOMAIN: The PAL motif is required for normal active site conformation. The catalytic domains embedded in the membrane are in the opposite orientation to that of the presenilin protein family; therefore, it is predicted to cleave type II-oriented substrate peptides like the prototypic protease SPP. {ECO:0000250|UniProtKB:P49768}. +A2A6C4 SPP2C_MOUSE Signal peptide peptidase-like 2C (SPP-like 2C) (SPPL2c) (EC 3.4.23.-) (Intramembrane protease 5) (IMP-5) 690 76,266 Active site (2); Alternative sequence (2); Chain (1); Domain (1); Erroneous termination (1); Frameshift (1); Glycosylation (1); Motif (1); Sequence conflict (1); Signal peptide (1); Topological domain (10); Transmembrane (9) TRANSMEM 193 213 Helical. {ECO:0000255}.; TRANSMEM 261 283 Helical. {ECO:0000255}.; TRANSMEM 285 307 Helical. {ECO:0000255}.; TRANSMEM 329 349 Helical. {ECO:0000255}.; TRANSMEM 355 373 Helical. {ECO:0000255}.; TRANSMEM 385 405 Helical. {ECO:0000255}.; TRANSMEM 449 469 Helical. {ECO:0000255}.; TRANSMEM 483 503 Helical. {ECO:0000255}.; TRANSMEM 505 525 Helical. {ECO:0000255}. TOPO_DOM 29 192 Lumenal. {ECO:0000250|UniProtKB:Q8IUH8}.; TOPO_DOM 214 260 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 284 284 Lumenal. {ECO:0000255}.; TOPO_DOM 308 328 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 350 354 Lumenal. {ECO:0000255}.; TOPO_DOM 374 384 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 406 448 Lumenal. {ECO:0000250|UniProtKB:Q8IUH8}.; TOPO_DOM 470 482 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 504 504 Lumenal. {ECO:0000255}.; TOPO_DOM 526 690 Cytoplasmic. {ECO:0000250|UniProtKB:Q8IUH8}. FUNCTION: Intramembrane-cleaving aspartic protease (I-CLiP) that may be able to cleave type II membrane signal peptides in the hydrophobic plane of the membrane. {ECO:0000250}. PTM: Glycosylated. {ECO:0000250|UniProtKB:P49768}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8IUH8}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8IUH8}. Membrane {ECO:0000250|UniProtKB:Q8IUH8}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8IUH8}; Lumenal side {ECO:0000250|UniProtKB:Q8IUH8}. DOMAIN: The PAL motif is required for normal active site conformation. The catalytic domains embedded in the membrane are in the opposite orientation to that of the presenilin protein family; therefore, it is predicted to cleave type II-oriented substrate peptides like the prototypic protease SPP. {ECO:0000250|UniProtKB:P49768}. +G3X912 SPRTN_MOUSE SprT-like domain-containing protein Spartan (Protein with SprT-like domain at the N terminus) (Spartan) 497 55,317 Chain (1); Cross-link (4); Domain (1); Modified residue (2); Motif (2); Sequence conflict (2); Zinc finger (1) FUNCTION: Regulator of UV-induced DNA damage response: acts as a 'reader' of ubiquitinated PCNA that enhances RAD18-mediated PCNA ubiquitination and translesion DNA synthesis (TLS). Recruited to sites of UV damage and interacts with ubiquitinated PCNA and RAD18, the E3 ubiquitin ligase that monoubiquitinates PCNA. Facilitates chromatin association of RAD18 and is required for efficient PCNA monoubiquitination, promoting a feed-forward loop to enhance PCNA ubiquitination and translesion DNA synthesis. Acts as a regulator of TLS by recruiting VCP/p97 to sites of DNA damage, possibly leading to extraction of DNA polymerase eta (POLH) by VCP/p97 to prevent excessive translesion DNA synthesis and limit the incidence of mutations induced by DNA damage (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}. Note=Localizes to sites of UV damage via the PIP-box. Recruited to stalled replication forks at sites of replication stress (By similarity). {ECO:0000250}. SUBUNIT: Interacts with PCNA (when ubiquitinated). Interacts with RAD18. Interacts (via its SHP-box) with VCP/p97. Interacts with KCTD13 and POLD3 (By similarity). {ECO:0000250}. DOMAIN: The PIP-box mediates the interaction with PCNA, while the UBZ-type zinc finger mediates binding to 'Lys-48'- and 'Lys-63'-linked polyubiquitin. {ECO:0000250}. +Q80XC2 TRM61_MOUSE tRNA (adenine(58)-N(1))-methyltransferase catalytic subunit TRMT61A (EC 2.1.1.220) (mRNA methyladenosine-N(1)-methyltransferase catalytic subunit TRMT61A) (EC 2.1.1.-) (tRNA(m1A58)-methyltransferase subunit TRMT61A) (tRNA(m1A58)MTase subunit TRMT61A) 290 31,639 Binding site (5); Chain (1); Initiator methionine (1); Modified residue (2); Region (9); Sequence conflict (2) FUNCTION: Catalytic subunit of tRNA (adenine-N(1)-)-methyltransferase, which catalyzes the formation of N(1)-methyladenine at position 58 (m1A58) in initiator methionyl-tRNA. Catalytic subunit of mRNA N(1)-methyltransferase complex, which mediates methylation of adenosine residues at the N(1) position of a small subset of mRNAs: N(1) methylation takes place in tRNA T-loop-like structures of mRNAs and is only present at low stoichiometries. {ECO:0000250|UniProtKB:Q96FX7}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P46959}. SUBUNIT: Heterotetramer; composed of two copies of TRMT6 and two copies of TRMT61A. {ECO:0000250|UniProtKB:Q96FX7}. +Q91WK1 SPRY4_MOUSE SPRY domain-containing protein 4 207 23,275 Chain (1); Domain (1); Frameshift (1); Modified residue (3); Sequence conflict (1) +Q8BH69 SPS1_MOUSE Selenide, water dikinase 1 (EC 2.7.9.3) (Selenium donor protein 1) (Selenophosphate synthase 1) 392 42,907 Active site (1); Binding site (3); Chain (1); Initiator methionine (1); Modified residue (1); Nucleotide binding (3); Site (1) FUNCTION: Synthesizes selenophosphate from selenide and ATP. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Nucleus membrane {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +Q91WJ7 SPS2L_MOUSE SPATS2-like protein 558 61,669 Alternative sequence (1); Chain (1); Coiled coil (1); Initiator methionine (1); Modified residue (2) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. +Q80YT5 SPT20_MOUSE Spermatogenesis-associated protein 20 (Sperm-specific protein 411) (Ssp411) (Transcript increased in spermiogenesis 78 protein) 790 88,472 Chain (1); Modified residue (2) FUNCTION: May play a role in fertility regulation. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q8BHW6 SPT21_MOUSE Spermatogenesis-associated protein 21 681 75,541 Calcium binding (1); Chain (1); Compositional bias (1); Domain (1) FUNCTION: Involved in the differentiation of haploid spermatids. {ECO:0000250}. +Q80WQ4 TRM9B_MOUSE Probable tRNA methyltransferase 9B (Probable tRNA methyltransferase 9-like protein) (EC 2.1.1.-) 447 50,277 Alternative sequence (3); Chain (1); Erroneous initiation (1); Modified residue (1); Sequence conflict (3) FUNCTION: May modifie wobble uridines in specific arginine and glutamic acid tRNAs. Acts as a tumor suppressor by promoting the expression of LIN9 (By similarity). {ECO:0000250|UniProtKB:Q9P272}. +Q5DU57 SPT13_MOUSE Spermatogenesis-associated protein 13 (APC-stimulated guanine nucleotide exchange factor 2) (Asef2) 656 75,257 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (3); Modified residue (2); Region (2) FUNCTION: Acts as guanine nucleotide exchange factor (GEF) for RHOA, RAC1 and CDC42 GTPases. Regulates cell migration and adhesion assembly and disassembly through a RAC1, PI3K, RHOA and AKT1-dependent mechanism. Increases both RAC1 and CDC42 activity, but decreases the amount of active RHOA (By similarity). Required for MMP9 up-regulation via the JNK signaling pathway in colorectal tumor cells. Involved in tumor angiogenesis and may play a role in intestinal adenoma formation and tumor progression. {ECO:0000250, ECO:0000269|PubMed:19893577}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell projection, filopodium {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Cell projection, ruffle membrane {ECO:0000250}. Note=Accumulates in the lamellipodium and ruffle membrane in response to hepatocyte growth factor (HGF) treatment. {ECO:0000250}. SUBUNIT: Interacts (via ABR and SH3 domain) with APC. The binding of APC enhances its GEF activity by relieving it from an autoinhibitory conformation, in which the ABR and SH3 domains are associated with the C-terminal tail. Interacts (via C-terminal tail) with PPP1R9B (via C-terminus). Interacts with RAC1 (By similarity). {ECO:0000250}. DOMAIN: The C-terminal tail is required for its GEF activity. {ECO:0000250}. TISSUE SPECIFICITY: Expression is aberrantly enhanced in most colorectal tumors. {ECO:0000269|PubMed:19893577}. +Q8C5V0 SPT32_MOUSE Spermatogenesis-associated protein 32 (Acrosome expressed protein 2) 334 37,222 Chain (1); Modified residue (2) SUBUNIT: Interacts with syntaxin-1 and ACTB. {ECO:0000269|PubMed:18621766}. TISSUE SPECIFICITY: Highly expressed in the testis and weakly in the brain and heart. {ECO:0000269|PubMed:18621766}. +Q8C624 SPT33_MOUSE Spermatogenesis-associated protein 33 132 15,038 Chain (1); Modified residue (1) SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:23844118}. Nucleus {ECO:0000269|PubMed:23844118}. TISSUE SPECIFICITY: Predominantly expressed in testis (at protein level). {ECO:0000269|PubMed:23844118}. +Q9CVW4 SPT45_MOUSE Spermatogenesis-associated protein 45 97 11,413 Chain (1); Frameshift (1) +Q4FZF2 SPT46_MOUSE Spermatogenesis-associated protein 46 204 22,997 Chain (1); Compositional bias (1) FUNCTION: Play a role in spermiogenesis and fertilization. {ECO:0000269|PubMed:27488028}. SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:27488028}. Note=Located throughout the subacrosomal area (PubMed:27488028). {ECO:0000269|PubMed:27488028}. TISSUE SPECIFICITY: Testis-specific (PubMed:27488028). {ECO:0000269|PubMed:27488028}. +Q5NC83 SPT48_MOUSE Spermatogenesis-associated protein 48 (Post-meiotic spermatogenesis protein 1) 441 50,400 Alternative sequence (1); Chain (1); Sequence conflict (1) TISSUE SPECIFICITY: Testis specific. Expressed at the spermatid stage. {ECO:0000269|PubMed:22110678}. +Q8C636 SPT16_MOUSE Spermatogenesis-associated protein 16 571 65,006 Alternative sequence (1); Chain (1) FUNCTION: Involved in the formation of sperm acrosome, which implicated its potential role in spermatogenesis and sperm-egg fusion. {ECO:0000269|PubMed:16372119}. SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasmic vesicle, secretory vesicle, acrosome. Note=Shift from Golgi to sperm acrosome. TISSUE SPECIFICITY: Expressed in spermatocytes and round and elongated spermatids in the seminiferous tubules. {ECO:0000269|PubMed:12529416, ECO:0000269|PubMed:16372119}. +P16546 SPTN1_MOUSE Spectrin alpha chain, non-erythrocytic 1 (Alpha-II spectrin) (Fodrin alpha chain) 2472 284,597 Alternative sequence (1); Calcium binding (2); Chain (1); Domain (4); Modified residue (28); Repeat (20); Sequence conflict (6); Site (1) FUNCTION: Fodrin, which seems to be involved in secretion, interacts with calmodulin in a calcium-dependent manner and is thus candidate for the calcium-dependent movement of the cytoskeleton at the membrane. PTM: Phosphorylation of Tyr-1176 decreases sensitivity to cleavage by calpain in vitro. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cell cortex. Note=Expressed along the cell membrane in podocytes and presumptive tubule cells during glomerulogenesis and is expressed along lateral cell margins in tubule cells. {ECO:0000250}. SUBUNIT: Like erythrocyte spectrin, the spectrin-like proteins are capable of forming dimers which can further associate to tetramers. Interacts (via C-terminal spectrin repeats) with TRPC4. Interacts with CALM and EMD. Interacts with isoform 1 of ACP1. Identified in a complex with ACTN4, CASK, IQGAP1, MAGI2, NPHS1 and SPTBN1. Interacts with SHANK3 (via ANK repeats) (By similarity). {ECO:0000250}. +Q8R207 SPTSA_MOUSE Serine palmitoyltransferase small subunit A (Small subunit of serine palmitoyltransferase A) (ssSPTa) 71 8,452 Chain (1); Erroneous initiation (5); Sequence conflict (1); Topological domain (3); Transmembrane (2) TRANSMEM 13 29 Helical. {ECO:0000255}.; TRANSMEM 35 57 Helical. {ECO:0000255}. TOPO_DOM 1 12 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 30 34 Lumenal. {ECO:0000255}.; TOPO_DOM 58 71 Cytoplasmic. {ECO:0000255}. Lipid metabolism; sphingolipid metabolism. FUNCTION: Stimulates the activity of serine palmitoyltransferase (SPT). The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference. The SPTLC1-SPTLC2-SPTSSA complex shows a strong preference for C16-CoA substrate, while the SPTLC1-SPTLC3-SPTSSA isozyme uses both C14-CoA and C16-CoA as substrates, with a slight preference for C14-CoA (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Interacts with SPTLC1; the interaction is direct. Component of the serine palmitoyltransferase (SPT) complex, composed of SPTLC1, either SPTLC2 or SPTLC3, and either SPTSSA or SPTSSB (By similarity). {ECO:0000250}. +Q52KI8 SRRM1_MOUSE Serine/arginine repetitive matrix protein 1 (Plenty-of-prolines 101) 946 106,862 Alternative sequence (2); Chain (1); Compositional bias (5); Cross-link (7); Domain (1); Modified residue (74); Region (3); Sequence conflict (5) FUNCTION: Part of pre- and post-splicing multiprotein mRNP complexes. Involved in numerous pre-mRNA processing events. Promotes constitutive and exonic splicing enhancer (ESE)-dependent splicing activation by bridging together sequence-specific (SR family proteins, SFRS4, SFRS5 and TRA2B/SFRS10) and basal snRNP (SNRP70 and SNRPA1) factors of the spliceosome. Stimulates mRNA 3'-end cleavage independently of the formation of an exon junction complex. Binds both pre-mRNA and spliced mRNA 20-25 nt upstream of exon-exon junctions. Binds RNA and DNA with low sequence specificity and has similar preference for either double- or single-stranded nucleic acid substrates. {ECO:0000250|UniProtKB:Q8IYB3}. PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}.; PTM: Phosphorylated on multiple serine and threonine residues by DYRK3 during the G2-to-M transition, after the nuclear-envelope breakdown. Phosphorylation by DYRK3 promotes disassembly of nuclear speckles. {ECO:0000250|UniProtKB:Q8IYB3}. SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000255|PROSITE-ProRule:PRU00627}. Nucleus speckle {ECO:0000255|PROSITE-ProRule:PRU00627}. SUBUNIT: Identified in the spliceosome C complex. Found in a pre-mRNA splicing complex with SFRS4, SFRS5, SNRP70, SNRPA1, SRRM1 and SRRM2. Found in a pre-mRNA exonic splicing enhancer (ESE) complex with SNRP70, SNRPA1, SRRM1 and TRA2B/SFRS10. Found in a mRNA splicing-dependent exon junction complex (EJC) with DEK, PRPF8, NCBP1, RBM8A, RNPS1, SRRM1 and ALYREF/THOC4. Interacts with BAT1, CPSF1, RBM8A, RNPS1, and ALYREF/THOC4. Seems to be a compound of RNA export complexes that are released from speckles in a ATP-dependent manner. {ECO:0000250|UniProtKB:Q8IYB3}. +Q9R0M3 SRPX_MOUSE Sushi-repeat-containing protein SRPX (DRS protein) 464 51,574 Alternative sequence (1); Chain (1); Disulfide bond (7); Domain (4); Signal peptide (1) +Q8C8K3 SRS12_MOUSE Serine/arginine-rich splicing factor 12 (Splicing factor, arginine/serine-rich 13B) 266 29,664 Chain (1); Compositional bias (2); Sequence conflict (1) FUNCTION: Splicing factor that seems to antagonize SR proteins in pre-mRNA splicing regulation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +Q8BKA3 SRRM4_MOUSE Serine/arginine repetitive matrix protein 4 (Neural-specific serine/arginine repetitive splicing factor of 100 kDa) (Neural-specific SR-related protein of 100 kDa) (nSR100) 608 67,860 Alternative sequence (1); Chain (1); Compositional bias (3) FUNCTION: Splicing factor specifically required for neural cell differentiation. Acts in conjunction with nPTB/PTBP2 by binding directly to its regulated target transcripts and promotes neural-specific exon inclusion in many genes that function in neural cell differentiation. Required to promote the inclusion of neural-specific exon 10 in nPTB/PTBP2, leading to increased expression of neural-specific nPTB/PTBP2. Also promotes the inclusion of exon 16 in DAAM1 in neuron extracts (PubMed:19737518). Promotes alternative splicing of REST transcripts to produce a REST isoform (REST4) with greatly reduced repressive activity, thereby activating expression of REST targets in neural cells (PubMed:21884984). Plays an important role during embryonic development as well as in the proper functioning of the adult nervous system. Regulates alternative splicing events in genes with important neuronal functions (PubMed:25838543). {ECO:0000269|PubMed:19737518, ECO:0000269|PubMed:21884984, ECO:0000269|PubMed:25838543}. PTM: Phosphorylated. {ECO:0000269|PubMed:19737518}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19737518}. TISSUE SPECIFICITY: Specifically expressed in neuronal cells (at protein level). Expressed in adult nervous system and sensory organ tissues. {ECO:0000269|PubMed:19737518, ECO:0000269|PubMed:25838543}. +Q6PDM2 SRSF1_MOUSE Serine/arginine-rich splicing factor 1 (ASF/SF2) (Pre-mRNA-splicing factor SRp30a) (Splicing factor, arginine/serine-rich 1) 248 27,745 Alternative sequence (4); Beta strand (5); Chain (1); Compositional bias (2); Cross-link (2); Domain (2); Helix (3); Initiator methionine (1); Modified residue (19); Region (1); Sequence conflict (6) FUNCTION: Plays a role in preventing exon skipping, ensuring the accuracy of splicing and regulating alternative splicing. Interacts with other spliceosomal components, via the RS domains, to form a bridge between the 5'- and 3'-splice site binding components, U1 snRNP and U2AF. Can stimulate binding of U1 snRNP to a 5'-splice site-containing pre-mRNA. Binds to purine-rich RNA sequences, either the octamer, 5'-RGAAGAAC-3' (r=A or G) or the decamers, AGGACAGAGC/AGGACGAAGC. Binds preferentially to the 5'-CGAGGCG-3' motif in vitro. Three copies of the octamer constitute a powerful splicing enhancer in vitro, the ASF/SF2 splicing enhancer (ASE) which can specifically activate ASE-dependent splicing (By similarity). Specifically regulates alternative splicing of cardiac isoforms of CAMK2D, LDB3/CYPHER and TNNT2/CTNT during heart remodeling at the juvenile to adult transition. The inappropriate accumulation of a neonatal and neuronal isoform of CAMKD2 in the adult heart results in aberrant calcium handling and defective excitation-contraction coupling in cardiomyocytes. May function as export adapter involved in mRNA nuclear export through the TAP/NXF1 pathway. {ECO:0000250, ECO:0000269|PubMed:15652482}. PTM: Phosphorylated by CLK1, CLK2, CLK3 and CLK4. Phosphorylated by SRPK1 at multiple serines in its RS domain via a directional (C-terminal to N-terminal) and a dual-track mechanism incorporating both processive phosphorylation (in which the kinase stays attached to the substrate after each round of phosphorylation) and distributive phosphorylation steps (in which the kinase and substrate dissociate after each phosphorylation event). The RS domain of SRSF1 binds to a docking groove in the large lobe of the kinase domain of SRPK1 and this induces certain structural changes in SRPK1 and/or RRM 2 domain of SRSF1, allowing RRM 2 to bind the kinase and initiate phosphorylation. The cycles continue for several phosphorylation steps in a processive manner (steps 1-8) until the last few phosphorylation steps (approximately steps 9-12). During that time, a mechanical stress induces the unfolding of the beta-4 motif in RRM 2, which then docks at the docking groove of SRPK1. This also signals RRM 2 to begin to dissociate, which facilitates SRSF1 dissociation after phosphorylation is completed (By similarity). {ECO:0000250}.; PTM: Asymmetrically dimethylated at arginines, probably by PRMT1, methylation promotes localization to nuclear speckles. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q07955}. Nucleus speckle {ECO:0000250|UniProtKB:Q07955}. Note=In nuclear speckles. Shuttles between the nucleus and the cytoplasm. {ECO:0000250|UniProtKB:Q07955}. SUBUNIT: Consists of two polypeptides of p32 and p33. In vitro, self-associates and binds SRSF2, SNRNP70 and U2AF1 but not U2AF2. Binds SREK1/SFRS12. Interacts with SAFB/SAFB1. Interacts with PSIP1/LEDGF. Identified in the spliceosome C complex. Interacts with RSRC1 (via Arg/Ser-rich domain). Interacts with ZRSR2/U2AF1-RS2. Interacts with CCDC55 (via C-terminus). Interacts with SRPK1 and a sliding docking interaction is essential for its sequential and processive phosphorylation by SRPK1. Interacts with NXF1. Interacts with CCNL1, CCNL2 and CDK11B. Interacts with RRP1B. {ECO:0000250|UniProtKB:Q07955}. DOMAIN: The RRM 2 domain plays an important role in governing both the binding mode and the phosphorylation mechanism of the RS domain by SRPK1. RS domain and RRM 2 are uniquely positioned to initiate a highly directional (C-terminus to N-terminus) phosphorylation reaction in which the RS domain slides through an extended electronegative channel separating the docking groove of SRPK1 and the active site. RRM 2 binds toward the periphery of the active site and guides the directional phosphorylation mechanism. Both the RS domain and an RRM domain are required for nucleocytoplasmic shuttling (By similarity). {ECO:0000250}. +Q9DCF9 SSRG_MOUSE Translocon-associated protein subunit gamma (TRAP-gamma) (Signal sequence receptor subunit gamma) (SSR-gamma) 185 21,064 Alternative sequence (2); Chain (1); Modified residue (4); Topological domain (4); Transmembrane (4) TRANSMEM 28 48 Helical. {ECO:0000255}.; TRANSMEM 55 76 Helical. {ECO:0000255}.; TRANSMEM 136 157 Helical. {ECO:0000255}.; TRANSMEM 164 184 Helical. {ECO:0000255}. TOPO_DOM 1 27 Lumenal. {ECO:0000255}.; TOPO_DOM 49 54 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 77 135 Lumenal. {ECO:0000255}.; TOPO_DOM 158 163 Cytoplasmic. {ECO:0000255}. FUNCTION: TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Heterotetramer of TRAP-alpha, TRAP-beta, TRAP-delta and TRAP-gamma. +Q2LA85 TRML2_MOUSE Trem-like transcript 2 protein (TLT-2) (Triggering receptor expressed on myeloid cells-like protein 2) 329 37,075 Chain (1); Compositional bias (2); Disulfide bond (2); Domain (1); Glycosylation (1); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 271 291 Helical. {ECO:0000255}. TOPO_DOM 25 270 Extracellular. {ECO:0000255}.; TOPO_DOM 292 329 Cytoplasmic. {ECO:0000255}. FUNCTION: Cell surface receptor that may play a role in the innate and adaptive immune response. Acts as a counter-receptor for CD276 and interaction with CD276 on T-cells enhances T-cell activation (By similarity). {ECO:0000250, ECO:0000269|PubMed:16670310}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Interacts with CD276 and this interaction enhances T-cell activation. {ECO:0000250}. TISSUE SPECIFICITY: Detected in B-lymphocytes and macrophages. Detected in spleen, lymph nodes, blood, bone marrow and cells from the peritoneal cavity (at protein level). {ECO:0000269|PubMed:16670310}. +Q3LRV9 TRML4_MOUSE Trem-like transcript 4 protein (TLT-4) (Triggering receptor expressed on myeloid cells-like protein 3) (Triggering receptor expressed on myeloid cells-like protein 4) 263 29,355 Alternative sequence (2); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (1); Mutagenesis (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 201 221 Helical. {ECO:0000255}. TOPO_DOM 29 200 Extracellular. {ECO:0000305}.; TOPO_DOM 222 263 Cytoplasmic. {ECO:0000305}. FUNCTION: Positively regulates Toll-like receptor signaling via TLR7, TLR9 and TLR13 in neutrophils and splenic macrophages (PubMed:25848864). Regulates TLR7 signaling by controlling ligand-induced recruitment of TLR7 from the endoplasmic reticulum to endosomes and lysosomes (PubMed:25848864). Positively regulates Toll-like receptor TLR9-induced production of inflammatory cytokines but is dispensable for IFNB1 production (PubMed:25848864). Involved in the anti-viral response to several viruses including influenza virus, vesicular stomatitis virus and cytomegalovirus (PubMed:25848864). Binds to late apoptotic, and necrotic cells, but not living or early apoptotic cells, but is not essential for uptake of dying cells by dendritic cells (DCs) (PubMed:22210914, PubMed:19155473, PubMed:25848864). Does not bind nucleic acids (PubMed:25848864). May participate in antigen presentation (PubMed:22210914). {ECO:0000269|PubMed:19155473, ECO:0000269|PubMed:22210914, ECO:0000269|PubMed:25848864}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:19155473, ECO:0000305|PubMed:22210914}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Interacts with TYROBP/DAP12. {ECO:0000269|PubMed:19155473}. DOMAIN: The cytoplasmic tail appears to be dispensable for TLR7-mediated signaling. {ECO:0000269|PubMed:25848864}. TISSUE SPECIFICITY: Predominantly expressed in spleen, with highest levels on selected populations of macrophages, including red pulp macrophages, and on subsets of dendritic cells (DC), mostly on CD8alpha(+) DC (at protein level) (PubMed:19155473, PubMed:22210914, PubMed:25848864). Also expressed on blood and spleen Ly6C(low) monocytes (at protein level) (PubMed:22210914). Not expressed on lymphocytes or granulocytes (at protein level) (PubMed:19155473, PubMed:22210914). {ECO:0000269|PubMed:19155473, ECO:0000269|PubMed:22210914, ECO:0000269|PubMed:25848864}. +Q9QWG7 ST1B1_MOUSE Sulfotransferase family cytosolic 1B member 1 (ST1B1) (Sulfotransferase 1B1) (EC 2.8.2.-) (DOPA/tyrosine sulfotransferase) 299 34,901 Active site (1); Alternative sequence (1); Binding site (3); Chain (1); Nucleotide binding (3); Sequence conflict (3) FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of many hormones, neurotransmitters, drugs and xenobiotic compounds. Sulfonation increases the water solubility of most compounds, and therefore their renal excretion, but it can also result in bioactivation to form active metabolites. Sulfates L-DOPA and D-DOPA, tyrosine isomers such as DL-m-tyrosine, dopamine and thyroid hormones. {ECO:0000269|PubMed:9644246}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. TISSUE SPECIFICITY: Liver specific. {ECO:0000269|PubMed:9644246}. +P56677 ST14_MOUSE Suppressor of tumorigenicity 14 protein homolog (EC 3.4.21.109) (Epithin) (Serine protease 14) 855 94,655 Active site (3); Chain (1); Disulfide bond (18); Domain (8); Glycosylation (6); Modified residue (1); Topological domain (2); Transmembrane (1) TRANSMEM 56 76 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 55 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 77 855 Extracellular. {ECO:0000255}. FUNCTION: Degrades extracellular matrix. Exhibits trypsin-like activity as defined by cleavage of synthetic substrates with Arg or Lys as the P1 site (By similarity). Involved in the terminal differentiation of keratinocytes through prostasin (PRSS8) activation and filaggrin (FLG) processing (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. SUBUNIT: Interacts with CDCP1. May interact with TMEFF1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in intestine, kidney, lung, and thymus. Not expressed in skeletal muscle, liver, heart, testis and brain. +Q9D939 ST1C2_MOUSE Sulfotransferase 1C2 (ST1C2) (EC 2.8.2.-) 296 34,953 Active site (1); Binding site (3); Chain (1); Modified residue (2); Nucleotide binding (3); Region (1); Sequence conflict (2) FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of drugs, xenobiotic compounds, hormones, and neurotransmitters. {ECO:0000250}. SUBCELLULAR LOCATION: Lysosome {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in stomach and kidney. {ECO:0000269|PubMed:12164856}. +P0CC03 ST6B1_MOUSE Sulfotransferase 6B1 (ST6B1) (Thyroxine sulfotransferase) (EC 2.8.2.n2) 303 35,077 Active site (1); Binding site (3); Chain (1); Nucleotide binding (3); Sequence conflict (1) FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of thyroxine. Involved in the metabolism of thyroxine. {ECO:0000269|PubMed:19505954}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain, heart, kidney, thymus, lung, liver and testis. {ECO:0000269|PubMed:19505954}. +Q80ZI1 TRNP1_MOUSE TMF-regulated nuclear protein 1 223 23,086 Chain (1); Compositional bias (1) FUNCTION: DNA-binding factor that regulates the expression of a subset of genes and plays a key role in tangential, radial, and lateral expansion of the brain neocortex. Regulates neural stem cells proliferation and the production of intermediate neural progenitors and basal radial glial cells affecting the process of cerebral cortex gyrification. May control the proliferation rate of cells by regulating their progression through key cell-cycle transition points. {ECO:0000269|PubMed:16792503, ECO:0000269|PubMed:23622239}. PTM: Ubiquitinated, leading to its degradation by the proteasome. {ECO:0000269|PubMed:16792503}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23622239}. SUBUNIT: Interacts with TMF1; may regulate TRNP1 proteasomal degradation. {ECO:0000269|PubMed:16792503}. TISSUE SPECIFICITY: Expressed in brain and kidney (at protein level). Also detected in spleen and intestine. {ECO:0000269|PubMed:16792503, ECO:0000269|PubMed:23622239}. +Q8K1J6 TRNT1_MOUSE CCA tRNA nucleotidyltransferase 1, mitochondrial (EC 2.7.7.72) (mitochondrial tRNA nucleotidyl transferase, CCA-adding) (mt CCA-adding enzyme) (mt tRNA CCA-diphosphorylase) (mt tRNA CCA-pyrophosphorylase) (mt tRNA adenylyltransferase) 434 49,895 Active site (3); Alternative sequence (2); Chain (1); Modified residue (2); Sequence conflict (1); Transit peptide (1) FUNCTION: Adds and repairs the conserved 3'-CCA sequence necessary for the attachment of amino acids to the 3' terminus of tRNA molecules, using CTP and ATP as substrates. {ECO:0000250|UniProtKB:Q96Q11}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. SUBUNIT: Monomer and homodimer. {ECO:0000250}. +P50236 ST2A2_MOUSE Bile salt sulfotransferase 2 (EC 2.8.2.14) (Hydroxysteroid sulfotransferase) (ST) (Sulfotransferase 2A2) (ST2A2) 285 33,329 Active site (1); Binding site (5); Chain (1); Nucleotide binding (3); Sequence conflict (2) FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze sulfonation of hydroxysteroids and xenobiotics. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. +Q8BGW6 ST32A_MOUSE Serine/threonine-protein kinase 32A (EC 2.7.11.1) 398 46,509 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Domain (1); Initiator methionine (1); Lipidation (1); Nucleotide binding (1) SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor {ECO:0000250|UniProtKB:Q8WU08}. +Q8QZV4 ST32C_MOUSE Serine/threonine-protein kinase 32C (EC 2.7.11.1) 488 55,263 Active site (1); Binding site (1); Chain (1); Compositional bias (1); Domain (1); Modified residue (3); Nucleotide binding (1); Sequence conflict (1) +O35403 ST3A1_MOUSE Amine sulfotransferase (EC 2.8.2.3) (SULT-X2) (Sulfotransferase 3A1) (ST3A1) 293 35,181 Active site (1); Binding site (2); Chain (1); Nucleotide binding (3) FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the N-sulfonation of amines. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +P63046 ST4A1_MOUSE Sulfotransferase 4A1 (ST4A1) (EC 2.8.2.-) (Brain sulfotransferase-like protein) (mBR-STL) (Nervous system sulfotransferase) (NST) 284 33,054 Alternative sequence (1); Chain (1); Modified residue (3); Sequence conflict (1) FUNCTION: Atypical sulfotransferase family member with very low affinity for 3'-phospho-5'-adenylyl sulfate (PAPS) and very low catalytic activity towards L-triiodothyronine, thyroxine, estrone, p-nitrophenol, 2-naphthylamine, and 2-beta-naphthol. May have a role in the metabolism of drugs and neurotransmitters in the CNS. {ECO:0000269|PubMed:12039030}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain, cerebellum and hypothalamus. Not detected in pancreas, liver, lung, intestine, kidney, uterus, adrenal gland, thymus, spleen, epididymis, testicle, and heart. {ECO:0000269|PubMed:12039030}. +Q8K031 STAR8_MOUSE StAR-related lipid transfer protein 8 (START domain-containing protein 8) (StARD8) 1019 113,021 Chain (1); Compositional bias (2); Domain (2); Modified residue (6); Sequence conflict (7) FUNCTION: Accelerates GTPase activity of RHOA and CDC42, but not RAC1. Stimulates the hydrolysis of phosphatidylinositol 4,5-bisphosphate by PLCD1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000269|PubMed:17976533}. SUBUNIT: Binds both the SH2 and PTB domains of TNS1. {ECO:0000250}. +Q76N33 STALP_MOUSE AMSH-like protease (AMSH-LP) (EC 3.4.19.-) (AMSH family protein) (AMSH-FP) (STAM-binding protein-like 1) 436 49,640 Alternative sequence (1); Chain (1); Domain (1); Erroneous initiation (1); Metal binding (7); Modified residue (3); Motif (1); Sequence conflict (2); Site (1) FUNCTION: Zinc metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Does not cleave 'Lys-48'-linked polyubiquitin chains (By similarity). {ECO:0000250}. DOMAIN: The JAMM motif is essential for the protease activity. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed. Isoform 1 is widely expressed while isoform 2 is testis-specific. {ECO:0000269|PubMed:12943674}. +P70297 STAM1_MOUSE Signal transducing adapter molecule 1 (STAM-1) 548 59,771 Chain (1); Cross-link (1); Domain (4); Modified residue (4) FUNCTION: Involved in intracellular signal transduction mediated by cytokines and growth factors. Upon IL-2 and GM-CSL stimulation, it plays a role in signaling leading to DNA synthesis and MYC induction. May also play a role in T-cell development. Involved in down-regulation of receptor tyrosine kinase via multivesicular body (MVBs) when complexed with HGS (ESCRT-0 complex). The ESCRT-0 complex binds ubiquitin and acts as sorting machinery that recognizes ubiquitinated receptors and transfers them to further sequential lysosomal sorting/trafficking processes (By similarity). {ECO:0000250}. PTM: Phosphorylated on Tyr-198. Phosphorylated in response to IL2, IL3, IL4, IL7, CSF2/GM-CSF, EGF and PDGFB. Phosphorylated by activated PDGFRB (By similarity). {ECO:0000250|UniProtKB:Q92783}.; PTM: Ubiquitinated by ITCH. {ECO:0000250|UniProtKB:Q92783}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Early endosome membrane {ECO:0000250|UniProtKB:Q92783}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q92783}; Cytoplasmic side {ECO:0000250|UniProtKB:Q92783}. SUBUNIT: Component of the ESCRT-0 complex composed of STAM or STAM2 and HGS (PubMed:19278655). Probably part of a complex at least composed of HSG, STAM and EPS15 (By similarity). Found in a complex with HGS and E3 ligase ITCH and DTX3L (By similarity). Interacts with E3 ligase DTX3L; the interaction brings together STAM and HSG, promotes their recruitment to early endosomes and decreases STAM and HGS ubiquitination by ITCH (By similarity). Interacts with STAMBP/AMSH (By similarity). Interacts with PDGFRB (By similarity). Interacts with LITAF; the interaction is direct (By similarity). Identified in a complex with HGS and LITAF (By similarity). {ECO:0000250|UniProtKB:Q92783, ECO:0000269|PubMed:19278655}. DOMAIN: The VHS domain mediates high-avidity binding to Lys63-linked and Lys48-linked polyubiquitinated cargos. {ECO:0000250|UniProtKB:Q92783}. TISSUE SPECIFICITY: Ubiquitously expressed. Enriched expression in synaptic vesicles. {ECO:0000269|PubMed:8780729}. +P51557 STAR_MOUSE Steroidogenic acute regulatory protein, mitochondrial (StAR) (Luteinizing hormone-induced protein) (START domain-containing protein 1) (StARD1) 284 31,626 Chain (1); Compositional bias (1); Domain (1); Modified residue (2); Sequence conflict (1); Transit peptide (1) Steroid metabolism; cholesterol metabolism. FUNCTION: Plays a key role in steroid hormone synthesis by enhancing the metabolism of cholesterol into pregnenolone. Transporter that binds to and transport cholesterol through the intermembrane space of the mitochondrion (Probable). {ECO:0000305}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:7588255}. SUBUNIT: May interact with TSPO. {ECO:0000250}. TISSUE SPECIFICITY: Expressed within glia and neurons in discrete regions of the brain. {ECO:0000269|PubMed:12486153}. +O88811 STAM2_MOUSE Signal transducing adapter molecule 2 (STAM-2) (Hrs-binding protein) 523 57,455 Alternative sequence (3); Beta strand (5); Chain (1); Domain (4); Helix (1); Motif (1); Mutagenesis (2); Region (2) FUNCTION: Involved in intracellular signal transduction mediated by cytokines and growth factors. Upon IL-2 and GM-CSL stimulation, it plays a role in signaling leading to DNA synthesis and MYC induction. May also play a role in T-cell development. Involved in down-regulation of receptor tyrosine kinase via multivesicular body (MVBs) when complexed with HGS (ESCRT-0 complex). The ESCRT-0 complex binds ubiquitin and acts as sorting machinery that recognizes ubiquitinated receptors and transfers them to further sequential lysosomal sorting/trafficking processes (By similarity). {ECO:0000250, ECO:0000269|PubMed:12972556}. PTM: Phosphorylated in response to IL-2, GM-CSF, EGF and PDGF. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10651905, ECO:0000269|PubMed:12551915}. Early endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. SUBUNIT: Component of the ESCRT-0 complex composed of STAM or STAM2 and HGS. Part of a complex at least composed of HSG, STAM2 and EPS15. Interacts with JAK2 and JAK3. Interacts with ubiquitinated proteins and the deubiquitinating enzyme USP8/UBPY. Interacts (via the via the PxVxL motif) with CBX5; the interaction is direct. Interacts with VPS37C. Interacts with ubiquitin; the interaction is direct (By similarity). Interacts (via UIM domain) with UBQLN1 (via ubiquitin-like domain). {ECO:0000250|UniProtKB:O75886, ECO:0000269|PubMed:16159959}. DOMAIN: The VHS and UIM domains mediate the interaction with ubiquitinated proteins. {ECO:0000269|PubMed:10651905}.; DOMAIN: The SH3 domain mediates the interaction with USP8. {ECO:0000269|PubMed:10651905}.; DOMAIN: Contains one Pro-Xaa-Val-Xaa-Leu (PxVxL) motif, which is required for interaction with chromoshadow domains. This motif requires additional residues -7, -6, +4 and +5 of the central Val which contact the chromoshadow domain. {ECO:0000269|PubMed:10651905}. TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in testis. {ECO:0000269|PubMed:10651905}. +Q8R0L1 STAP2_MOUSE Signal-transducing adaptor protein 2 (STAP-2) 411 45,802 Alternative sequence (2); Chain (1); Coiled coil (1); Compositional bias (1); Domain (2); Modified residue (4) FUNCTION: Substrate of protein kinase PTK6 (By similarity). May play a regulatory role in the acute-phase response in systemic inflammation and may modulate STAT3 activity. {ECO:0000250, ECO:0000269|PubMed:12540842}. PTM: Phosphorylated on tyrosine. Phosphorylated by PTK6 at Tyr-250 modulates PTK6-mediated STAT3 activation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12540842}. Membrane {ECO:0000269|PubMed:12540842}; Peripheral membrane protein {ECO:0000269|PubMed:12540842}. Note=The translocation to the membranes occurs in response to EGF when the protein is overexpressed in fibroblastic cells. SUBUNIT: Interacts with PTK6 and CSF1R. {ECO:0000269|PubMed:12540842}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12540842}. +Q99JV5 STAR4_MOUSE StAR-related lipid transfer protein 4 (START domain-containing protein 4) (StARD4) 224 25,579 Beta strand (11); Chain (1); Domain (1); Helix (5); Natural variant (2); Turn (1) FUNCTION: May be involved in the intracellular transport of sterols or other lipids. May bind cholesterol or other sterols. TISSUE SPECIFICITY: Expressed in most tissues, with highest levels in liver and in kidney. +P42227 STAT3_MOUSE Signal transducer and activator of transcription 3 (Acute-phase response factor) 770 88,054 Alternative sequence (2); Beta strand (20); Chain (1); Domain (1); Helix (30); Initiator methionine (1); Modified residue (14); Motif (1); Mutagenesis (6); Sequence conflict (4); Turn (6) FUNCTION: Signal transducer and transcription activator that mediates cellular responses to interleukins, KITLG/SCF, LEP and other growth factors. Once activated, recruits coactivators, such as NCOA1 or MED1, to the promoter region of the target gene. May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4. Binds to the interleukin-6 (IL-6)-responsive elements identified in the promoters of various acute-phase protein genes. Activated by IL31 through IL31RA. Acts as a regulator of inflammatory response by regulating differentiation of naive CD4(+) T-cells into T-helper Th17 or regulatory T-cells (Treg): deacetylation and oxidation of lysine residues by LOXL3, leads to disrupt STAT3 dimerization and inhibit its transcription activity (By similarity). Involved in cell cycle regulation by inducing the expression of key genes for the progression from G1 to S phase, such as CCND1 (By similarity). Mediates the effects of LEP on melanocortin production, body energy homeostasis and lactation (PubMed:12594516). May play an apoptotic role by transctivating BIRC5 expression under LEP activation (PubMed:16825198). Cytoplasmic STAT3 represses macroautophagy by inhibiting EIF2AK2/PKR activity (By similarity). Plays a crucial role in basal beta cell functions, such as regulation of insulin secretion (PubMed:20215569). Plays an important role in host defense in methicillin-resistant S.aureus lung infection by regulating the expression of the antimicrobial lectin REG3G (PubMed:23401489). {ECO:0000250|UniProtKB:P40763, ECO:0000269|PubMed:11294897, ECO:0000269|PubMed:12594516, ECO:0000269|PubMed:16825198, ECO:0000269|PubMed:20215569, ECO:0000269|PubMed:23084476, ECO:0000269|PubMed:23401489}. PTM: Activated through tyrosine phosphorylation by BMX. Tyrosine phosphorylated in response to IL6, IL11, CNTF, LIF, KITLG/SCF, CSF1, EGF, PDGF, IFN-alpha, LEP and OSM. Activated KIT promotes phosphorylation on tyrosine residues and subsequent translocation to the nucleus. Tyrosine phosphorylated in response to constitutively activated FGFR1, FGFR2, FGFR3 and FGFR4. Phosphorylated on serine upon DNA damage, probably by ATM or ATR. Serine phosphorylation is important for the formation of stable DNA-binding STAT3 homodimers and maximal transcriptional activity. ARL2BP may participate in keeping the phosphorylated state of STAT3 within the nucleus. Tyrosine phosphorylated upon stimulation with EGF. Upon LPS challenge, phosphorylated within the nucleus by IRAK1 (By similarity). Upon UV-A treatment, phosphorylated on Ser-727 by RPS6KA5 (By similarity). Dephosphorylation on tyrosine residues by PTPN2 negatively regulates IL6/interleukin-6 signaling (By similarity). Phosphorylation at Tyr-705 by FER or PTK6 leads to an increase of its transcriptional activity. {ECO:0000250|UniProtKB:P40763, ECO:0000269|PubMed:10878010, ECO:0000269|PubMed:11294897, ECO:0000269|PubMed:11553624, ECO:0000269|PubMed:15004007, ECO:0000269|PubMed:16825198, ECO:0000269|PubMed:20595392, ECO:0000269|PubMed:21135090, ECO:0000269|PubMed:23401489, ECO:0000269|PubMed:7543024}.; PTM: Acetylated on lysine residues by CREBBP. Deacetylation by LOXL3 leads to disrupt STAT3 dimerization and inhibit STAT3 transcription activity. Oxidation of lysine residues to allysine on STAT3 preferentially takes place on lysine residues that are acetylated. {ECO:0000250|UniProtKB:P40763}.; PTM: Some lysine residues are oxidized to allysine by LOXL3, leading to disrupt STAT3 dimerization and inhibit STAT3 transcription activity. Oxidation of lysine residues to allysine on STAT3 preferentially takes place on lysine residues that are acetylated. {ECO:0000250|UniProtKB:P40763}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Predominantly present in the cytoplasm without stimuli. Upon leukemia inhibitory factor (LIF) stimulation, accumulates in the nucleus. The complex composed of BART and ARL2 plays an important role in the nuclear translocation and retention of STAT3 (By similarity). Shuttles between the nucleus and the cytoplasm. Translocated into the nucleus upon tyrosine phosphorylation and dimerization, in response to signaling by activated FGFR1, FGFR2, FGFR3 or FGFR4. Constitutive nuclear presence is independent of tyrosine phosphorylation. {ECO:0000250}. SUBUNIT: Forms a homodimer or a heterodimer with a related family member (at least STAT1). Interacts with IL31RA, NCOA1, PELP1, SIPAR, SOCS7, STATIP1 and TMF1. Interacts with IL23R in presence of IL23. Interacts (via SH2 domain) with NLK. Interacts with ARL2BP; the interaction is enhanced by LIF and JAK1 expression (By similarity). Interacts with KPNA4 and KPNA5; KPNA4 may be the primary mediator of nuclear import (By similarity). Interacts with CAV2; the interaction is increased on insulin-induced tyrosine phosphorylation of CAV2 and leads to STAT3 activation (By similarity). Interacts with ARL2BP; interaction is enhanced with ARL2. Interacts with NEK6 (By similarity). Binds to CDK9 when activated and nuclear. Interacts with BMX. Interacts with ZIPK/DAPK3. Interacts with PIAS3; the interaction occurs on stimulation by IL6, CNTF or OSM and inhibits the DNA binding activity of STAT3. In prostate cancer cells, interacts with STAT3 and promotes DNA binding activity of STAT3. Interacts with STMN3, antagonizing its microtubule-destabilizing activity. Interacts with the 'Lys-129' acetylated form of BIRC5/survivin. Interacts with FER. Interacts (via SH2 domain) with EIF2AK2/PKR (via the kinase catalytic domain) (By similarity). Interacts with FGFR4 (By similarity). Interacts with STAT3; the interaction is independent of STAT3 TYR-705 phosphorylation status (By similarity). Interacts with OCAD1 (PubMed:23972987). {ECO:0000250|UniProtKB:P40763, ECO:0000250|UniProtKB:P52631, ECO:0000269|PubMed:10878010, ECO:0000269|PubMed:10954736, ECO:0000269|PubMed:11553624, ECO:0000269|PubMed:15004007, ECO:0000269|PubMed:15919823, ECO:0000269|PubMed:16401721, ECO:0000269|PubMed:18234692, ECO:0000269|PubMed:20595392, ECO:0000269|PubMed:23972987, ECO:0000269|PubMed:9388184, ECO:0000269|Ref.18}. TISSUE SPECIFICITY: STAT3A is seen in the liver, spleen, and kidney. STAT3B is also detected in the liver, although in a much less abundant manner. Expressed in the lung and an increase in expression levels seen during methicillin-resistant S.aureus infection. {ECO:0000269|PubMed:23401489}. +Q8C7E7 STBD1_MOUSE Starch-binding domain-containing protein 1 (Genethonin-1) (Glycophagy cargo receptor stbd1) 338 36,127 Chain (1); Compositional bias (1); Domain (1); Modified residue (11); Motif (1); Topological domain (2); Transmembrane (1) TRANSMEM 7 23 Helical. {ECO:0000255}. TOPO_DOM 1 6 Extracellular. {ECO:0000255}.; TOPO_DOM 24 338 Cytoplasmic. {ECO:0000255}. FUNCTION: Acts as a cargo receptor for glycogen. Delivers its cargo to an autophagic pathway called glycophagy, resulting in the transport of glycogen to lysosomes. {ECO:0000250|UniProtKB:O95210, ECO:0000269|PubMed:20810658}. PTM: Ubiquitinated, which leads to proteasomal degradation. {ECO:0000250|UniProtKB:O95210}. SUBCELLULAR LOCATION: Preautophagosomal structure membrane {ECO:0000250|UniProtKB:Q5FVN1, ECO:0000305|PubMed:20810658}; Single-pass type III membrane protein {ECO:0000250|UniProtKB:O95210}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O95210}; Single-pass type III membrane protein {ECO:0000250|UniProtKB:O95210}. Cell membrane, sarcolemma, T-tubule {ECO:0000250|UniProtKB:O95210}. Note=Also detected near the junctional sarcoplasmic reticulum (By similarity). Concentrates at perinuclear structures (PubMed:20810658). {ECO:0000250|UniProtKB:O95210, ECO:0000269|PubMed:20810658}. SUBUNIT: Interacts with the ATG8 family proteins GABARAP and GABARAPL1 (By similarity). Interacts with several glycogen-associated proteins, such as GYS2 (liver glycogen synthase), GDE (glycogen debranching enzyme), GBE1 (glycogen branching enzyme 1) and EPM2A (Laforin) (By similarity). {ECO:0000250|UniProtKB:O95210}. DOMAIN: The LIR motif (LC3-interacting region) is required for the interaction with the ATG8 family protein GABARAPL1. {ECO:0000250|UniProtKB:O95210}.; DOMAIN: The C-terminal CBM20 domain is required for the interaction with glycogen. {ECO:0000269|PubMed:20810658}. TISSUE SPECIFICITY: Expressed at high level in glycogen-accumulating organs such as muscle and liver. Trace signals are also found in brain, kidney, and pancreas. {ECO:0000269|PubMed:20810658}. +Q9Z108 STAU1_MOUSE Double-stranded RNA-binding protein Staufen homolog 1 487 53,925 Chain (1); Domain (2); Modified residue (3) FUNCTION: Binds double-stranded RNA (regardless of the sequence) and tubulin. May play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Rough endoplasmic reticulum. Note=Localizes exclusively with the rough reticulum endoplasmic (RER). SUBUNIT: Binds tubulin. Identified in a mRNP complex, at least composed of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1. Binds with low affinity single-stranded RNA or DNA homopolymers. Interacts with CASC3 in an RNA-dependent manner (By similarity). {ECO:0000250}. DOMAIN: One of the DRDB could be involved in RER binding.; DOMAIN: The C-terminal contains the tubulin binding domain (TBD). +Q99JT2 STK26_MOUSE Serine/threonine-protein kinase 26 (EC 2.7.11.1) (Mammalian STE20-like protein kinase 4) (MST-4) (STE20-like kinase MST4) (Serine/threonine-protein kinase MST4) 416 46,614 Active site (1); Binding site (1); Chain (1); Domain (1); Initiator methionine (1); Modified residue (10); Nucleotide binding (1) FUNCTION: Mediator of cell growth. Modulates apoptosis. In association with STK24 negatively regulates Golgi reorientation in polarized cell migration upon RHO activation. {ECO:0000250|UniProtKB:Q9P289}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9P289}. Golgi apparatus {ECO:0000250|UniProtKB:Q9P289}. Note=Colocalized with RIPOR1 in the Golgi of serum-starved cells and relocated to cytoplasmic punctae, probably vesicular compartments, along with RIPOR1 upon serum stimulation in a Rho- and PDCD10-dependent manner. {ECO:0000250|UniProtKB:Q9P289}. SUBUNIT: Homodimer. Interacts with PDCD10. Interacts with GOLGA2. Interacts with CTTNBP2NL. Interacts with RIPOR1 (via C-terminus); this interaction occurs in a PDCD10-dependent and Rho-independent manner. Interacts with PDCD10; this interaction is required for the association of STK26 with RIPOR1. {ECO:0000250|UniProtKB:Q9P289}. +Q99MW1 STK31_MOUSE Serine/threonine-protein kinase 31 (EC 2.7.11.1) 1018 115,018 Binding site (1); Chain (1); Coiled coil (1); Domain (2); Nucleotide binding (1); Sequence conflict (4) TISSUE SPECIFICITY: Testis specific. Expressed only in male germ cells. +Q69ZM6 STK36_MOUSE Serine/threonine-protein kinase 36 (EC 2.7.11.1) (Fused homolog) 1316 144,180 Active site (1); Alternative sequence (4); Binding site (1); Chain (1); Compositional bias (2); Domain (1); Frameshift (1); Nucleotide binding (1); Sequence caution (1); Sequence conflict (5) FUNCTION: Serine/threonine protein kinase which plays an important role in the sonic hedgehog (Shh) pathway by regulating the activity of GLI transcription factors. Controls the activity of the transcriptional regulators GLI1, GLI2 and GLI3 by opposing the effect of SUFU and promoting their nuclear localization. GLI2 requires an additional function of STK36 to become transcriptionally active, but the enzyme does not need to possess an active kinase catalytic site for this to occur. Required for postnatal development, possibly by regulating the homeostasis of cerebral spinal fluid or ciliary function. Essential for construction of the central pair apparatus of motile cilia. {ECO:0000269|PubMed:16055717, ECO:0000269|PubMed:18600476, ECO:0000269|PubMed:19305393}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19305393}. Nucleus {ECO:0000250}. Note=Low levels also present in the nucleus. {ECO:0000250}. SUBUNIT: Interacts with SPAG16 and KIF27. {ECO:0000269|PubMed:19305393}. TISSUE SPECIFICITY: Weakly expressed in the heart and thymus, present at moderate to high levels in the lungs, pancreas, and kidneys and at higher levels in the brain and cerebellum. Very highly expressed in the testis. {ECO:0000269|PubMed:16055717, ECO:0000269|PubMed:18600476}. +P54227 STMN1_MOUSE Stathmin (Leukemia-associated gene protein) (Leukemia-associated phosphoprotein p18) (Metablastin) (Oncoprotein 18) (Op18) (Phosphoprotein p19) (pp19) (Prosolin) (Protein Pr22) (pp17) 149 17,274 Chain (1); Coiled coil (1); Domain (1); Initiator methionine (1); Modified residue (11) FUNCTION: Involved in the regulation of the microtubule (MT) filament system by destabilizing microtubules. Prevents assembly and promotes disassembly of microtubules. Phosphorylation at Ser-16 may be required for axon formation during neurogenesis (By similarity). Involved in the control of the learned and innate fear. {ECO:0000250, ECO:0000269|PubMed:16286011}. PTM: Many different phosphorylated forms are observed depending on specific combinations among the sites which can be phosphorylated. MAPK is responsible for the phosphorylation of stathmin in response to NGF (Probable). Phosphorylation at Ser-16 seems to be required for neuron polarization (By similarity). {ECO:0000250, ECO:0000305}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SUBUNIT: Binds to two alpha/beta-tubulin heterodimers. Interacts with KIST. {ECO:0000269|PubMed:7724523}. TISSUE SPECIFICITY: Highly expressed in the lateral nucleus of the amygdala. {ECO:0000269|PubMed:16286011}. +Q91VJ4 STK38_MOUSE Serine/threonine-protein kinase 38 (EC 2.7.11.1) (NDR1 protein kinase) (Nuclear Dbf2-related kinase 1) 465 54,174 Active site (1); Binding site (1); Chain (1); Domain (2); Initiator methionine (1); Modified residue (5); Nucleotide binding (1); Region (1) FUNCTION: Negative regulator of MAP3K1/2 signaling. Converts MAP3K2 from its phosphorylated form to its non-phosphorylated form and inhibits autophosphorylation of MAP3K2 (By similarity). {ECO:0000250, ECO:0000269|PubMed:21730291}. PTM: ISGylated. {ECO:0000250}.; PTM: Phosphorylated by STK3/MST2 and this is enhanced by MOBKL1B. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. SUBUNIT: Homodimeric S100B binds two molecules of STK38. Interacts with MOB1 and MOB2 (By similarity). Interacts with MAP3K1 and MAP3K2 (via the kinase catalytic domain) (By similarity). Forms a tripartite complex with MOBKL1B and STK3/MST2 (By similarity). Interacts with MICAL1; leading to inhibit the protein kinase activity by antagonizing activation by MST1/STK4 (PubMed:21730291). {ECO:0000250|UniProtKB:Q15208, ECO:0000269|PubMed:21730291}. TISSUE SPECIFICITY: Expressed at high levels in spleen, lung, thymus, brain and fat tissue. {ECO:0000269|PubMed:15037617}. +Q7TNL3 STK40_MOUSE Serine/threonine-protein kinase 40 (EC 2.7.11.1) (Serine/threonine-protein kinase lyk4) 435 48,932 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Domain (1); Erroneous initiation (1); Nucleotide binding (1); Sequence conflict (2) FUNCTION: May be a negative regulator of NF-kappa-B and p53-mediated gene transcription. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. +Q9WTK7 STK11_MOUSE Serine/threonine-protein kinase STK11 (EC 2.7.11.1) (Liver kinase B1 homolog) (LKB1) (mLKB1) 436 49,267 Active site (1); Alternative sequence (2); Binding site (1); Chain (1); Domain (1); Lipidation (2); Modified residue (17); Mutagenesis (8); Nucleotide binding (1); Propeptide (1); Region (1); Sequence conflict (1) FUNCTION: Tumor suppressor serine/threonine-protein kinase that controls the activity of AMP-activated protein kinase (AMPK) family members, thereby playing a role in various processes such as cell metabolism, cell polarity, apoptosis and DNA damage response. Acts by phosphorylating the T-loop of AMPK family proteins, thus promoting their activity: phosphorylates PRKAA1, PRKAA2, BRSK1, BRSK2, MARK1, MARK2, MARK3, MARK4, NUAK1, NUAK2, SIK1, SIK2, SIK3 and SNRK but not MELK. Also phosphorylates non-AMPK family proteins such as STRADA, PTEN and possibly p53/TP53. Acts as a key upstream regulator of AMPK by mediating phosphorylation and activation of AMPK catalytic subunits PRKAA1 and PRKAA2 and thereby regulates processes including: inhibition of signaling pathways that promote cell growth and proliferation when energy levels are low, glucose homeostasis in liver, activation of autophagy when cells undergo nutrient deprivation, and B-cell differentiation in the germinal center in response to DNA damage. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton. Required for cortical neuron polarization by mediating phosphorylation and activation of BRSK1 and BRSK2, leading to axon initiation and specification. Involved in DNA damage response: interacts with p53/TP53 and recruited to the CDKN1A/WAF1 promoter to participate in transcription activation. Able to phosphorylate p53/TP53; the relevance of such result in vivo is however unclear and phosphorylation may be indirect and mediated by downstream STK11/LKB1 kinase NUAK1. Also acts as a mediator of p53/TP53-dependent apoptosis via interaction with p53/TP53: translocates to the mitochondrion during apoptosis and regulates p53/TP53-dependent apoptosis pathways. In vein endothelial cells, inhibits PI3K/Akt signaling activity and thus induces apoptosis in response to the oxidant peroxynitrite. Regulates UV radiation-induced DNA damage response mediated by CDKN1A. In association with NUAK1, phosphorylates CDKN1A in response to UV radiation and contributes to its degradation which is necessary for optimal DNA repair (PubMed:25329316). {ECO:0000269|PubMed:16308421, ECO:0000269|PubMed:17482548, ECO:0000269|PubMed:17482549, ECO:0000269|PubMed:20864035, ECO:0000269|PubMed:25329316}.; FUNCTION: Isoform 2: Has a role in spermiogenesis. {ECO:0000269|PubMed:18774945}. PTM: Phosphorylated by ATM at Thr-366 following ionizing radiation (IR). Phosphorylation at Ser-431 by RPS6KA1 and/or some PKA is required to inhibit cell growth. Phosphorylation at Ser-431 is also required during neuronal polarization to mediate phosphorylation of BRSK1 and BRSK2. Phosphorylation by PKC/PRKCZ at Ser-428 promotes peroxynitrite-induced nuclear export of STK11, leading to PTEN activation and subsequent inhibition of AKT signaling. Phosphorylation by PKC/PRKCZ at Ser-399 in isoform 2 promotes metformin (or peroxynitrite)-induced nuclear export of STK11 and activation of AMPK. UV radiation-induced phosphorylation at Thr-366 mediates CDKN1A degradation. {ECO:0000269|PubMed:10642527, ECO:0000269|PubMed:11297520, ECO:0000269|PubMed:11853558, ECO:0000269|PubMed:12234250, ECO:0000269|PubMed:17482548, ECO:0000269|PubMed:17482549, ECO:0000269|PubMed:20864035, ECO:0000269|PubMed:25329316}.; PTM: Acetylated. Deacetylation at Lys-48 enhances cytoplasmic localization and kinase activity in vitro. {ECO:0000269|PubMed:18687677}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Membrane. Mitochondrion {ECO:0000250}. Note=Translocates to mitochondrion during apoptosis (By similarity). A small fraction localizes at membranes. Relocates to the cytoplasm when bound to STRAD (STRADA or STRADB) and CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta). PTEN promotes cytoplasmic localization (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 2: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Relocates to the cytoplasm when bound to STRAD (STRADA or STRADB) and CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta). {ECO:0000250}. SUBUNIT: Catalytic component of a trimeric complex composed of STK11/LKB1, STRAD (STRADA or STRADB) and CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta): the complex tethers STK11/LKB1 in the cytoplasm and stimulates its catalytic activity. Found in a ternary complex composed of SMAD4, STK11/LKB1 and STK11IP. Interacts with p53/TP53, SMAD4, STK11IP and WDR6. Interacts with NR4A1 (By similarity). Interacts with NISCH; this interaction may increase STK11 activity (By similarity). Interacts with PTEN, leading to PTEN phosphorylation (By similarity). Interacts with SIRT1; the interaction deacetylates STK11 (By similarity). Interacts with CDKN1A. {ECO:0000250|UniProtKB:Q15831, ECO:0000269|PubMed:17482548, ECO:0000269|PubMed:25329316}. TISSUE SPECIFICITY: Widely expressed. Isoform 2 is predominantly expressed in testis (at protein level). {ECO:0000269|PubMed:10642527, ECO:0000269|PubMed:18774945, ECO:0000269|PubMed:18854309}. +Q8CI66 STML1_MOUSE Stomatin-like protein 1 (SLP-1) 399 42,926 Chain (1); Domain (1); Modified residue (1); Motif (1); Sequence conflict (3); Topological domain (1); Transmembrane (1) TRANSMEM 58 78 Helical; Signal-anchor for type III membrane protein. {ECO:0000255}. TOPO_DOM 79 399 Cytoplasmic. {ECO:0000255}. FUNCTION: May play a role in cholesterol transfer to late endosomes (By similarity). May play a role in modulating membrane acid-sensing ion channels. Can specifically inhibit proton-gated current of ASIC1 isoform 1. Can increase inactivation speed of ASIC3. May be involved in regulation of proton sensing in dorsal root ganglions (PubMed:24247984). {ECO:0000250|UniProtKB:Q9UBI4, ECO:0000269|PubMed:24247984}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type III membrane protein {ECO:0000305}. Cytoplasmic vesicle {ECO:0000269|PubMed:24247984}. Cell membrane {ECO:0000269|PubMed:24247984}; Single-pass type III membrane protein {ECO:0000305}. Late endosome membrane {ECO:0000250|UniProtKB:Q9UBI4}. Membrane raft {ECO:0000250|UniProtKB:Q9UBI4}. SUBUNIT: Interacts with STOM; may redistribute STOM from the plasma membrane to late endosomes. {ECO:0000250|UniProtKB:Q9UBI4}. TISSUE SPECIFICITY: Expressed in dorsal root ganglion neurons. {ECO:0000269|PubMed:24247984}. +O88697 STK16_MOUSE Serine/threonine-protein kinase 16 (EC 2.7.11.1) (Embryo-derived protein kinase) (Edpk) (Myristoylated and palmitoylated serine/threonine-protein kinase) (MPSK) (Protein kinase Krct) (Protein kinase PKL12) (TGF-beta-stimulated factor 1) (TSF-1) (Tyrosine-protein kinase STK16) (EC 2.7.10.2) 305 34,382 Active site (1); Binding site (1); Chain (1); Domain (1); Initiator methionine (1); Lipidation (3); Modified residue (2); Nucleotide binding (1); Region (1); Sequence conflict (4) FUNCTION: Membrane-associated protein kinase that phosphorylates on serine and threonine residues. In vitro substrates include DRG1, ENO1 and EIF4EBP1. Also autophosphorylates (By similarity). May be involved in secretory vesicle trafficking or intracellular signaling. May have a role in regulating stromal-epithelial interactions that occur during ductal morphogenesis in the mammary gland. May be involved in TGF-beta signaling. Able to autophosphorylate on Tyr residue; it is however unclear whether it has tyrosine-protein kinase toward other proteins. {ECO:0000250, ECO:0000269|PubMed:9878782}. PTM: Mainly autophosphorylated on serine/threonine residues. Also autophosphorylated on Tyr-198 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:9712705}. Membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Note=Associates with Golgi and Golgi-derived vesicles. SUBUNIT: Monomer. Interacts with DRG1 (via its N-terminal); the interaction phosphorylates DRG1. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed at low levels. Relatively higher levels in testis, kidney and liver. {ECO:0000269|PubMed:9712705, ECO:0000269|PubMed:9878782}. +Q99KH8 STK24_MOUSE Serine/threonine-protein kinase 24 (EC 2.7.11.1) (Mammalian STE20-like protein kinase 3) (MST-3) (STE20-like kinase MST3) [Cleaved into: Serine/threonine-protein kinase 24 35 kDa subunit (Mammalian STE20-like protein kinase 3 N-terminal) (MST3/N); Serine/threonine-protein kinase 24 12 kDa subunit (Mammalian STE20-like protein kinase 3 C-terminal) (MST3/C)] 431 47,954 Active site (1); Binding site (1); Chain (3); Domain (1); Initiator methionine (1); Metal binding (2); Modified residue (4); Motif (2); Nucleotide binding (2); Site (1) FUNCTION: Serine/threonine-protein kinase that acts on both serine and threonine residues and promotes apoptosis in response to stress stimuli and caspase activation. Mediates oxidative-stress-induced cell death by modulating phosphorylation of JNK1-JNK2 (MAPK8 and MAPK9), p38 (MAPK11, MAPK12, MAPK13 and MAPK14) during oxidative stress. Plays a role in a staurosporine-induced caspase-independent apoptotic pathway by regulating the nuclear translocation of AIFM1 and ENDOG and the DNase activity associated with ENDOG. Phosphorylates STK38L on 'Thr-442' and stimulates its kinase activity. In association with STK26 negatively regulates Golgi reorientation in polarized cell migration upon RHO activation. Regulates also cellular migration with alteration of PTPN12 activity and PXN phosphorylation: phosphorylates PTPN12 and inhibits its activity and may regulate PXN phosphorylation through PTPN12. Acts as a key regulator of axon regeneration in the optic nerve and radial nerve (By similarity). {ECO:0000250|UniProtKB:Q9Y6E0}. PTM: Proteolytically processed by caspases during apoptosis. Proteolytic cleavage results in kinase activation, nuclear translocation of the truncated form (MST3/N) and the induction of apoptosis (By similarity). {ECO:0000250}.; PTM: Oxidative stress induces phosphorylation. Activated by autophosphorylation at Thr-178 and phosphorylation at this site is essential for its function. Manganese, magnesium and cobalt-dependent autophosphorylation is mainly on threonine residues while zinc-dependent autophosphorylation is on both serine and threonine residues (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Membrane {ECO:0000250}. Note=The truncated form (MST3/N) translocates to the nucleus. Colocalizes with STK38L in the membrane (By similarity). {ECO:0000250}. SUBUNIT: Monomer. Interacts with CTTNBP2NL. Interacts with RIPOR1 (via C-terminus); this interaction occurs in a PDCD10-dependent and Rho-independent manner. Interacts with PDCD10; this interaction is required for the association of STK24 with RIPOR1. {ECO:0000250|UniProtKB:Q9Y6E0}. +P58404 STRN4_MOUSE Striatin-4 (Zinedin) 760 81,645 Alternative sequence (1); Chain (1); Coiled coil (1); Modified residue (4); Region (2); Repeat (7); Sequence conflict (3) FUNCTION: Binds calmodulin in a calcium dependent manner. May function as scaffolding or signaling protein. SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein. Cell projection, dendritic spine {ECO:0000250}. Note=CTTNBP2-binding may regulate dendritic spine distribution. {ECO:0000250}. SUBUNIT: Interacts with CTTNBP2; this interaction may regulate dendritic spine distribution of STRN4. Activation of glutamate receptors weakens the interaction with CTTNBP2 (By similarity). Interacts with CTTNBP2NL (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Mainly expressed in brain but is also expressed at low levels in the kidney. +Q8C079 STRP1_MOUSE Striatin-interacting protein 1 (Protein FAM40A) 837 95,585 Alternative sequence (3); Chain (1); Compositional bias (1); Frameshift (1); Modified residue (5); Sequence conflict (2) FUNCTION: Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the cortical actin filament dynamics and cell shape (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Enriched on the plasma membrane. {ECO:0000250}. SUBUNIT: Component of striatin-interacting phosphatase and kinase (STRIPAK) complex (PubMed:18782753). Interacts with CDC42BPB. Interacts with CTTNBP2NL. {ECO:0000250|UniProtKB:Q5VSL9, ECO:0000269|PubMed:18782753}. +P63042 STMN4_MOUSE Stathmin-4 (Stathmin-like protein B3) (RB3) 189 22,087 Chain (1); Coiled coil (1); Domain (1); Lipidation (2); Modified residue (1) FUNCTION: Exhibits microtubule-destabilizing activity. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250}. Cell projection, growth cone {ECO:0000250}. Cell projection, axon {ECO:0000250}. +Q8K2X3 STN1_MOUSE CST complex subunit STN1 (Alpha-accessory factor of 44 kDa) (AAF-44) (AAF44) (Oligonucleotide/oligosaccharide-binding fold-containing protein 1) (Suppressor of cdc thirteen homolog) 378 43,486 Beta strand (4); Chain (1); DNA binding (1); Erroneous initiation (1); Helix (4); Initiator methionine (1); Mutagenesis (2); Region (3); Sequence conflict (1) FUNCTION: Component of the CST complex proposed to act as a specialized replication factor promoting DNA replication under conditions of replication stress or natural replication barriers such as the telomere duplex. The CST complex binds single-stranded DNA with high affinity in a sequence-independent manner, while isolated subunits bind DNA with low affinity by themselves. Initially the CST complex has been proposed to protect telomeres from DNA degradation (PubMed:19854130). However, the CST complex has been shown to be involved in several aspects of telomere replication. The CST complex inhibits telomerase and is involved in telomere length homeostasis; it is proposed to bind to newly telomerase-synthesized 3' overhangs and to terminate telomerase action implicating the association with the ACD:POT1 complex thus interfering with its telomerase stimulation activity. The CST complex is also proposed to be involved in fill-in synthesis of the telomeric C-strand probably implicating recruitment and activation of DNA polymerase alpha (PubMed:22748632). The CST complex facilitates recovery from many forms of exogenous DNA damage; seems to be involved in the re-initiation of DNA replication at repaired forks and/or dormant origins. Required for efficicient replication of the duplex region of the telomere. Promotes efficient replication of lagging-strand telomeres. Promotes general replication start following replication-fork stalling implicating new origin firing. May be in involved in C-strand fill-in during late S/G2 phase independent of its role in telomere duplex replication (By similarity). {ECO:0000250|UniProtKB:Q9H668, ECO:0000269|PubMed:19854130, ECO:0000269|PubMed:22748632}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19119139, ECO:0000269|PubMed:19854130}. Chromosome, telomere {ECO:0000269|PubMed:19854130}. SUBUNIT: Component of the CST complex, composed of TEN1/C17orf106, CTC1/C17orf68 and STN1; in the complex interacts directly with TEN1 and CTC1 (PubMed:19119139, PubMed:19854130). Interacts with ACD/TPP1 (PubMed:19648609). Interacts with POT1 and POLA1 (By similarity). {ECO:0000250|UniProtKB:Q9H668, ECO:0000269|PubMed:19119139, ECO:0000269|PubMed:19648609, ECO:0000269|PubMed:19854130}. +Q8VDS8 STX18_MOUSE Syntaxin-18 334 38,381 Alternative sequence (3); Chain (1); Domain (1); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 309 329 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 1 308 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 330 334 Lumenal. {ECO:0000255}. FUNCTION: Syntaxin that may be involved in targeting and fusion of Golgi-derived retrograde transport vesicles with the ER. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}. SUBUNIT: Component of a SNARE complex consisting of STX18, USE1L, BNIP1/SEC20L, and SEC22B. RINT1/TIP20L and ZW10 are associated with the complex through interaction with BNIP1/SEC20L. Interacts directly with USE1L and BNIP1/SEC20L (By similarity). {ECO:0000250}. +Q9D3G5 STX11_MOUSE Syntaxin-11 287 33,369 Chain (1); Coiled coil (1); Domain (1) FUNCTION: SNARE that acts to regulate protein transport between late endosomes and the trans-Golgi network. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. SUBUNIT: Interacts with the SNARE proteins SNAP-23 and VAMP. {ECO:0000250}. +Q9JKK1 STX6_MOUSE Syntaxin-6 255 28,997 Alternative sequence (1); Chain (1); Coiled coil (1); Domain (1); Initiator methionine (1); Modified residue (4); Topological domain (1); Transmembrane (1) TRANSMEM 235 255 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 2 234 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in intracellular vesicle trafficking. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. SUBUNIT: Identified in a complex containing STX6, STX12 and VAMP4 (By similarity). This complex also includes VTI1A (PubMed:9705316). Binds EEA1 (By similarity). Interacts with VPS45A and GOPC (By similarity). Interacts with MARCH2 and MARCH3 (By similarity). Interacts with UHRF1BP1L (via C-terminal coiled-coil domain) (By similarity). Interacts with BAIAP3; this interaction is increased in the presence of calcium (By similarity). {ECO:0000250|UniProtKB:O43752, ECO:0000250|UniProtKB:Q63635, ECO:0000269|PubMed:9705316}. +Q9ER00 STX12_MOUSE Syntaxin-12 274 31,195 Chain (1); Coiled coil (1); Domain (1); Initiator methionine (1); Modified residue (5); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 251 271 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 2 250 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 272 274 Vesicular. {ECO:0000255}. FUNCTION: SNARE that acts to regulate protein transport between late endosomes and the trans-Golgi network. The SNARE complex containing STX6, STX12, VAMP4 and VTI1A mediates vesicle fusion (in vitro) (By similarity). Through complex formation with GRIP1, GRIA2 and NSG1 controls the intracellular fate of AMPAR and the endosomal sorting of the GRIA2 subunit toward recycling and membrane targeting (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:G3V7P1}. SUBCELLULAR LOCATION: Endosome membrane; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:G3V7P1}. Golgi apparatus membrane; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:G3V7P1}. Endomembrane system {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Early endosome membrane {ECO:0000250|UniProtKB:G3V7P1}; Single-pass type IV membrane protein {ECO:0000305}. Recycling endosome membrane {ECO:0000250|UniProtKB:G3V7P1}; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:G3V7P1}. SUBUNIT: Associates with the BLOC-1 complex. Interacts with BLOC1S6. Interacts with NAPA and SNAP23. Identified in a complex containing STX6, STX12, VAMP4 and VTI1A (By similarity). Interacts with GRIPAP1 (PubMed:20098723). Forms a complex with GRIP1, GRIA2 and NSG1; controls the intracellular fate of AMPAR and the endosomal sorting of the GRIA2 subunit toward recycling and membrane targeting (By similarity). Interacts with NSG1 (PubMed:12070131). {ECO:0000250, ECO:0000250|UniProtKB:G3V7P1, ECO:0000269|PubMed:12070131, ECO:0000269|PubMed:20098723}. +O55101 SNG2_MOUSE Synaptogyrin-2 (Cellugyrin) 224 24,778 Chain (1); Domain (1); Modified residue (2); Natural variant (1); Sequence conflict (1); Transmembrane (4) TRANSMEM 31 51 Helical. {ECO:0000255}.; TRANSMEM 72 92 Helical. {ECO:0000255}.; TRANSMEM 105 125 Helical. {ECO:0000255}.; TRANSMEM 147 167 Helical. {ECO:0000255}. FUNCTION: May play a role in regulated exocytosis. In neuronal cells, modulates the localization of synaptophysin/SYP into synaptic-like microvesicles and may therefore play a role in the formation and/or the maturation of this vesicles. May also play a role in GLUT4 storage and transport to the plasma membrane. {ECO:0000250|UniProtKB:O54980}. PTM: May be tyrosine phosphorylated by Src. {ECO:0000250|UniProtKB:O54980}. SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:12928441}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:12928441}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to cytoplasmic vesicles associated with the recycling endosomes. {ECO:0000250|UniProtKB:O54980}. +O09044 SNP23_MOUSE Synaptosomal-associated protein 23 (SNAP-23) (Syndet) (Vesicle-membrane fusion protein SNAP-23) 210 23,261 Chain (1); Coiled coil (1); Domain (2); Lipidation (5); Modified residue (7); Mutagenesis (1); Sequence conflict (2); Site (2) FUNCTION: Essential component of the high affinity receptor for the general membrane fusion machinery and an important regulator of transport vesicle docking and fusion. {ECO:0000250}. PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type A (BoNT/A, botA) which hydrolyzes the 202-Thr-|-Arg-203 bond; the in vitro reaction is not highly efficient (PubMed:9886085). {ECO:0000269|PubMed:9886085}.; PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type E (BoNT/E) which hydrolyzes the 185-Arg-|-Ile-186 bond; the in vitro reaction is more efficient than that of BoNT/A (PubMed:9886085). {ECO:0000269|PubMed:9886085}. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Cell junction, synapse, synaptosome. Note=Mainly localized to the plasma membrane. SUBUNIT: Homotetramer (via coiled-coil domain), also forms heterotetramers with STX4 and VAMP3 (By similarity). Found in a complex with VAMP8 and STX1A (By similarity). Found in a complex with VAMP8 and STX4 in pancreas (PubMed:15363411). Interacts simultaneously with SNAPIN and SYN4 (By similarity). Interacts with STX1A (PubMed:9507000). Interacts with STX12 (PubMed:9507000). Interacts tightly to multiple syntaxins and synaptobrevins/VAMPs (By similarity). Interacts with ZDHHC13 (via ANK repeats) (PubMed:26198635). Interacts with ZDHHC17 (via ANK repeats) (PubMed:26198635). {ECO:0000250|UniProtKB:O00161, ECO:0000250|UniProtKB:O70377, ECO:0000269|PubMed:15363411, ECO:0000269|PubMed:26198635, ECO:0000269|PubMed:9507000}. TISSUE SPECIFICITY: Expressed in non-neuronal tissues. +Q2MH31 SMRP1_MOUSE Spermatid-specific manchette-related protein 1 (Ciliated bronchial epithelial protein 1) 260 29,939 Alternative sequence (2); Chain (1) FUNCTION: May be involved in differentiation or function of ciliated cells (By similarity). May play a role in spermatogenesis. {ECO:0000250, ECO:0000269|PubMed:18163442}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:18163442}. Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Localizes to the manchette in elongating spermatids. Predominantly perinuclear in bronchial epithelial cells but also detected in the nucleus in some primary epithelial cells and in a number of cell lines. SUBUNIT: Interacts with alpha-tubulin. {ECO:0000269|PubMed:18163442}. TISSUE SPECIFICITY: Isoforms 1 is testis-specific where it is expressed exclusively in germ cells (at protein level). Isoform 2 is testis-specific. Isoform 3 and isoform 4 are expressed in both lung and testis. {ECO:0000269|PubMed:18163442, ECO:0000269|PubMed:19213785}. +P28663 SNAB_MOUSE Beta-soluble NSF attachment protein (SNAP-beta) (Brain protein I47) (N-ethylmaleimide-sensitive factor attachment protein beta) 298 33,557 Chain (1) FUNCTION: Required for vesicular transport between the endoplasmic reticulum and the Golgi apparatus. SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein. SUBUNIT: Interacts with PRKCABP, and disrupts the interaction between GRIA2 and PRKCABP, leading to the internalization of GRIA2. {ECO:0000250}. TISSUE SPECIFICITY: Cerebral cortex, cerebellar cortex, hippocampus, and dentate gyrus, weakly expressed in the putamen, the thalamus and the brain stem. {ECO:0000269|PubMed:8455721}. +Q9CWZ7 SNAG_MOUSE Gamma-soluble NSF attachment protein (SNAP-gamma) (N-ethylmaleimide-sensitive factor attachment protein gamma) 312 34,732 Chain (1); Modified residue (3) FUNCTION: Required for vesicular transport between the endoplasmic reticulum and the Golgi apparatus. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. SUBUNIT: Binds RIP11 (By similarity). Interacts with VTI1A. {ECO:0000250, ECO:0000269|PubMed:9705316}. +O35253 SMAD7_MOUSE Mothers against decapentaplegic homolog 7 (MAD homolog 7) (Mothers against DPP homolog 7) (Mothers against decapentaplegic homolog 8) (MAD homolog 8) (Mothers against DPP homolog 8) (SMAD family member 7) (SMAD 7) (Smad7) 426 46,442 Alternative sequence (1); Chain (1); Compositional bias (3); Cross-link (2); Domain (2); Metal binding (4); Modified residue (3); Motif (1); Mutagenesis (2); Region (1); Sequence conflict (2) FUNCTION: Antagonist of signaling by TGF-beta (transforming growth factor) type 1 receptor superfamily members; has been shown to inhibit TGF-beta (Transforming growth factor) and activin signaling by associating with their receptors thus preventing SMAD2 access. Functions as an adapter to recruit SMURF2 to the TGF-beta receptor complex. Also acts by recruiting the PPP1R15A-PP1 complex to TGFBR1, which promotes its dephosphorylation. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator. {ECO:0000250|UniProtKB:O15105}. PTM: Phosphorylation on Ser-249 does not affect its stability, nuclear localization or inhibitory function in TGFB signaling; however it affects its ability to regulate transcription (PubMed:11278814). Phosphorylated by PDPK1 (By similarity). {ECO:0000250|UniProtKB:O15105, ECO:0000269|PubMed:11278814}.; PTM: Ubiquitinated by WWP1 (PubMed:15221015). Polyubiquitinated by RNF111, which is enhanced by AXIN1 and promotes proteasomal degradation (PubMed:14657019). In response to TGF-beta, ubiquitinated by SMURF1; which promotes its degradation (By similarity). Ubiquitinated by RNF165, promoting proteasomal degradation, leading to enhance the BMP-Smad signaling (PubMed:23610558). {ECO:0000250|UniProtKB:O15105, ECO:0000269|PubMed:14657019, ECO:0000269|PubMed:15221015, ECO:0000269|PubMed:23610558}.; PTM: Acetylation prevents ubiquitination and degradation mediated by SMURF1. {ECO:0000250|UniProtKB:O15105}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11278814, ECO:0000269|PubMed:15496141}. Cytoplasm {ECO:0000269|PubMed:11278814, ECO:0000269|PubMed:15496141}. Note=Interaction with NEDD4L or RNF111 induces translocation from the nucleus to the cytoplasm (PubMed:15496141). TGF-beta stimulates its translocation from the nucleus to the cytoplasm. PDPK1 inhibits its translocation from the nucleus to the cytoplasm in response to TGF-beta (By similarity). {ECO:0000250|UniProtKB:O15105, ECO:0000269|PubMed:15496141}. SUBUNIT: Interacts with COPS5. Interacts with STAMBP. Interacts with PPP1R15A (By similarity). Interacts with NEDD4L. Interacts with RNF111, AXIN1 and AXIN2. Interacts with ACVR1B, SMURF1, SMURF2 and TGFBR1; SMAD7 recruits SMURF1 and SMURF2 to the TGF-beta receptor and regulates its degradation (By similarity). Interacts with WWP1. Interacts with PDPK1 (via PH domain) (By similarity). Ubiquitinated by WWP1. {ECO:0000250, ECO:0000269|PubMed:14657019, ECO:0000269|PubMed:15221015, ECO:0000269|PubMed:15496141}. TISSUE SPECIFICITY: Ubiquitous in various organs, with higher levels in brain and kidney. +O55100 SNG1_MOUSE Synaptogyrin-1 234 25,653 Alternative sequence (1); Chain (1); Domain (1); Modified residue (1); Topological domain (5); Transmembrane (4) TRANSMEM 24 44 Helical. {ECO:0000255}.; TRANSMEM 72 92 Helical. {ECO:0000255}.; TRANSMEM 104 124 Helical. {ECO:0000255}.; TRANSMEM 149 169 Helical. {ECO:0000255}. TOPO_DOM 1 23 Cytoplasmic. {ECO:0000250|UniProtKB:Q62876}.; TOPO_DOM 45 71 Lumenal. {ECO:0000250|UniProtKB:Q62876}.; TOPO_DOM 93 103 Cytoplasmic. {ECO:0000250|UniProtKB:Q62876}.; TOPO_DOM 125 148 Lumenal. {ECO:0000250|UniProtKB:Q62876}.; TOPO_DOM 170 234 Cytoplasmic. {ECO:0000250|UniProtKB:Q62876}. FUNCTION: May play a role in regulated exocytosis. Modulates the localization of synaptophysin/SYP into synaptic-like microvesicles and may therefore play a role in synaptic-like microvesicle formation and/or maturation (By similarity). Involved in the regulation of short-term and long-term synaptic plasticity (PubMed:10595519). {ECO:0000250|UniProtKB:Q62876, ECO:0000269|PubMed:10595519}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q62876}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q62876}. Melanosome {ECO:0000250|UniProtKB:O43759}. +P97469 SNAI2_MOUSE Zinc finger protein SNAI2 (Neural crest transcription factor Slug) (Protein snail homolog 2) 269 30,003 Chain (1); Region (1); Zinc finger (5) FUNCTION: Transcriptional repressor that modulates both activator-dependent and basal transcription. Involved in the generation and migration of neural crest cells. Plays a role in mediating RAF1-induced transcriptional repression of the TJ protein, occludin (OCLN) and subsequent oncogenic transformation of epithelial cells. Represses BRCA2 expression by binding to its E2-box-containing silencer and recruiting CTBP1 and HDAC1 in breast cells. In epidermal keratinocytes, binds to the E-box in ITGA3 promoter and represses its transcription. Involved in the regulation of ITGB1 and ITGB4 expression and cell adhesion and proliferation in epidermal keratinocytes. Binds to E-box2 domain of BSG and activates its expression during TGFB1-induced epithelial-mesenchymal transition (EMT) in hepatocytes. Represses E-Cadherin/CDH1 transcription via E-box elements. Involved in osteoblast maturation. Binds to RUNX2 and SOC9 promoters and may act as a positive and negative transcription regulator, respectively, in osteoblasts. Binds to CXCL12 promoter via E-box regions in mesenchymal stem cells and osteoblasts. Plays an essential role in TWIST1-induced EMT and its ability to promote invasion and metastasis (By similarity). {ECO:0000250}. PTM: GSK3B-mediated phosphorylation results in cytoplasmic localization and degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O43623}. Cytoplasm {ECO:0000250}. Note=Observed in discrete foci in interphase nuclei. These nuclear foci do not overlap with the nucleoli, the SP100 and the HP1 heterochromatin or the coiled body, suggesting SNAI2 is associated with active transcription or active splicing regions (By similarity). {ECO:0000250}. SUBUNIT: Interacts (via SNAG domain) with LIMD1 (via LIM domains), WTIP (via LIM domains) and AJUBA (via LIM domains). Interacts (via zinc fingers) with KPNA2, KPNB1, and TNPO1. May interact (via zinc fingers) with IPO7 (By similarity). {ECO:0000250}. DOMAIN: Repression activity depends on the C-terminal DNA-binding zinc fingers and on the N-terminal repression domain. {ECO:0000250}. +Q80XS6 SMAG2_MOUSE Protein Smaug homolog 2 (Smaug 2) (mSmaug2) (Sterile alpha motif domain-containing protein 4B) 687 75,024 Chain (1); Domain (1); Modified residue (13) FUNCTION: Has transcriptional repressor activity. Overexpression inhibits the transcriptional activities of AP-1, p53/TP53 and CDKN1A (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. +O88816 SNAT_MOUSE Serotonin N-acetyltransferase (Serotonin acetylase) (EC 2.3.1.87) (Aralkylamine N-acetyltransferase) (AA-NAT) 205 23,069 Binding site (2); Chain (1); Domain (1); Modified residue (2); Region (3); Site (2) Aromatic compound metabolism; melatonin biosynthesis; melatonin from serotonin: step 1/2. FUNCTION: Controls the night/day rhythm of melatonin production in the pineal gland. Catalyzes the N-acetylation of serotonin into N-acetylserotonin, the penultimate step in the synthesis of melatonin. {ECO:0000250|UniProtKB:Q29495}. PTM: cAMP-dependent phosphorylation on both N-terminal Thr-29 and C-terminal Ser-203 regulates AANAT activity by promoting interaction with 14-3-3 proteins. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q16613}. SUBUNIT: Monomer (By similarity). Interacts with several 14-3-3 proteins, including YWHAB, YWHAE, YWHAG and YWHAZ, preferentially when phosphorylated at Thr-29 (By similarity). Phosphorylation on Ser-203 also allows binding to YWHAZ, but with lower affinity (By similarity). The interaction with YWHAZ considerably increases affinity for arylalkylamines and acetyl-CoA and protects the enzyme from dephosphorylation and proteasomal degradation. It may also prevent thiol-dependent inactivation (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in pineal gland at night. Expression in the retina has not been confirmed. Extrapineal expression could be strain-specific. {ECO:0000269|PubMed:9838107}. +Q9D3S3 SNX29_MOUSE Sorting nexin-29 818 91,387 Alternative sequence (1); Chain (1); Coiled coil (1); Domain (2); Modified residue (11); Sequence caution (1) +Q9CWK8 SNX2_MOUSE Sorting nexin-2 519 58,471 Binding site (4); Chain (1); Domain (2); Modified residue (8); Region (2); Sequence conflict (2) FUNCTION: Involved in several stages of intracellular trafficking. Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)) or phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Acts in part as component of the retromer membrane-deforming SNX-BAR subcomplex. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX-BAR subcomplex functions to deform the donor membrane into a tubular profile called endosome-to-TGN transport carrier (ETC). Can sense membrane curvature and has in vitro vesicle-to-membrane remodeling activity. Required for retrograde endosome-to-TGN transport of TGN38. Promotes KALRN- and RHOG-dependent but retromer-independent membrane remodeling such as lamellipodium formation; the function is dependent on GEF activity of KALRN (By similarity). {ECO:0000250|UniProtKB:O60749}. SUBCELLULAR LOCATION: Early endosome membrane; Peripheral membrane protein; Cytoplasmic side {ECO:0000250|UniProtKB:O60749}. Cell projection, lamellipodium. Note=Colocalized with SORT1 to tubular endosomal membrane structures called endosome-to-TGN transport carriers (ETCs) which are budding from early endosome vacuoles just before maturing into late endosome vacuoles. Colocalized with F-actin at the leading edge of lamellipodia in cells in a KALRN-dependent manner (By similarity). {ECO:0000250|UniProtKB:O60749}. SUBUNIT: Predominantly forms heterodimers with BAR domain-containing sorting nexins SNX5, SNX6 and SNX32; can self-associate to form homodimers. The heterodimers are proposed to self-assemble into helical arrays on the membrane to stabilize and expand local membrane curvature underlying endosomal tubule formation. Thought to be a component of the originally described retromer complex (also called SNX-BAR retromer) which is a pentamer containing the heterotrimeric retromer cargo-selective complex (CSC), also descibed as vacuolar protein sorting subcomplex (VPS), and a heterodimeric membrane-deforming subcomplex formed between SNX1 or SNX2 and SNX5 or SNX6 (also called SNX-BAR subcomplex); the respective CSC and SNX-BAR subcomplexes associate with low affinity. Interacts with SNX5, SNX6, SNX32, VPS26A, VPS29, VPS35, FNBP1, KALRN, RHOG (GDP-bound form) (By similarity). {ECO:0000250|UniProtKB:O60749}. DOMAIN: The BAR domain is able to sense membrane curvature upon dimerization. Membrane remodeling seems to implicate insertion of a N-terminal amphipatric helix (AH) in the membrane (By similarity). {ECO:0000250|UniProtKB:O60749}. +Q6P8X1 SNX6_MOUSE Sorting nexin-6 [Cleaved into: Sorting nexin-6, N-terminally processed] 406 46,649 Chain (2); Domain (2); Initiator methionine (1); Modified residue (4); Region (5); Sequence conflict (1) FUNCTION: Involved in several stages of intracellular trafficking. Interacts with membranes phosphatidylinositol 3,4-bisphosphate and/or phosphatidylinositol 4,5-bisphosphate (Probable). Acts in part as component of the retromer membrane-deforming SNX-BAR subcomplex. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX-BAR subcomplex functions to deform the donor membrane into a tubular profile called endosome-to-TGN transport carrier (ETC). Does not have in vitro vesicle-to-membrane remodeling activity (By similarity). Involved in retrograde endosome-to-TGN transport of lysosomal enzyme receptor IGF2R. May function as link between transport vesicles and dynactin. Negatively regulates retrograde transport of BACE1 from the cell surface to the trans-Golgi network. Involved in E-cadherin sorting and degradation; inhibits PIP5K1C-mediated E-cadherin degradation (By similarity). In association with GIT1 involved in EGFR degradation (PubMed:18523162). Promotes lysosomal degradation of CDKN1B (PubMed:20228253). May contribute to transcription regulation (By similarity). {ECO:0000250|UniProtKB:Q9UNH7, ECO:0000269|PubMed:18523162, ECO:0000269|PubMed:20228253}. PTM: In vitro phosphorylated by PIM1; not affecting PIM1-dependent nuclear translocation (By similarity). {ECO:0000250|UniProtKB:Q9UNH7}. SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000269|PubMed:20228253}; Peripheral membrane protein {ECO:0000269|PubMed:20228253}; Cytoplasmic side {ECO:0000269|PubMed:20228253}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q9UNH7}. Cytoplasm {ECO:0000250|UniProtKB:Q9UNH7}. Nucleus {ECO:0000250|UniProtKB:Q9UNH7}. Note=Interaction with SNX1 or SNX2 promotes location at endosome membranes (By similarity). Only a minor proportion is seen in the nucleus (By similarity). {ECO:0000250|UniProtKB:Q9UNH7}. SUBUNIT: Forms heterodimers with BAR domain-containing sorting nexins SNX1 and SNX2. The heterodimers are proposed to self-assemble into helical arrays on the membrane to stabilize and expand local membrane curvature underlying endosomal tubule formation. Thought to be a component of the originally described retromer complex (also called SNX-BAR retromer) which is a pentamer containing the heterotrimeric retromer cargo-selective complex (CSC), also descibed as vacuolar protein sorting subcomplex (VPS), and a heterodimeric membrane-deforming subcomplex formed between SNX1 or SNX2 and SNX5 or SNX6 (also called SNX-BAR subcomplex); the respective CSC and SNX-BAR subcomplexes associate with low affinity (By similarity). Interacts with SNX1, SNX2, VPS26A, VPS29, VPS35, TGFB receptors, BACE1, BRMS1, PIP5K1C. Interacts with DCTN1; the association with DCTN1 is involved in movement of retromer-c ontaining vesicles toward the TGN. Interacts with PIM1; translocating SNX6 to the nucleus (By similarity). Interacts with CDKN1B and GIT1 (PubMed:18523162, PubMed:20228253). {ECO:0000250|UniProtKB:Q9UNH7, ECO:0000269|PubMed:18523162, ECO:0000269|PubMed:20228253}. DOMAIN: The PX domain mediates interaction with membranes enriched in phosphatidylinositol 3,4-bisphosphate and/or phosphatidylinositol 4,5-bisphosphate. {ECO:0000250}.; DOMAIN: The BAR domain is able to sense membrane curvature upon dimerization. Membrane remodeling seems to implicate insertion of an amphipatric helix (AH) in the membrane (By similarity). {ECO:0000250|UniProtKB:Q9UNH7}. +O08712 TR11B_MOUSE Tumor necrosis factor receptor superfamily member 11B (Osteoclastogenesis inhibitory factor) (Osteoprotegerin) 401 45,923 Beta strand (12); Chain (1); Disulfide bond (9); Domain (2); Glycosylation (4); Natural variant (5); Repeat (4); Signal peptide (1); Site (1) FUNCTION: Acts as decoy receptor for TNFSF11/RANKL and thereby neutralizes its function in osteoclastogenesis. Inhibits the activation of osteoclasts and promotes osteoclast apoptosis in vitro. Bone homeostasis seems to depend on the local ratio between TNFSF11 and TNFRSF11B. May also play a role in preventing arterial calcification. May act as decoy receptor for TNFSF10/TRAIL and protect against apoptosis. TNFSF10/TRAIL binding blocks the inhibition of osteoclastogenesis. {ECO:0000269|PubMed:10952716}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Homodimer. Interacts with TNFSF10 and TNFSF11. {ECO:0000269|PubMed:23039992}. TISSUE SPECIFICITY: Highly expressed in liver, lung, stomach, intestines and calvaria. Highly expressed in decidua and placenta, and in embryo. +Q9ERB5 SO1C1_MOUSE Solute carrier organic anion transporter family member 1C1 (Organic anion transporter 2) (OATP2) (Organic anion transporter F) (OATP-F) (Organic anion-transporting polypeptide 14) (OATP-14) (Solute carrier family 21 member 14) (Thyroxine transporter) 715 78,320 Chain (1); Compositional bias (1); Disulfide bond (3); Domain (1); Glycosylation (3); Sequence conflict (1); Topological domain (13); Transmembrane (12) TRANSMEM 44 63 Helical; Name=1. {ECO:0000255}.; TRANSMEM 83 103 Helical; Name=2. {ECO:0000255}.; TRANSMEM 110 134 Helical; Name=3. {ECO:0000255}.; TRANSMEM 188 216 Helical; Name=4. {ECO:0000255}.; TRANSMEM 236 256 Helical; Name=5. {ECO:0000255}.; TRANSMEM 275 299 Helical; Name=6. {ECO:0000255}.; TRANSMEM 352 373 Helical; Name=7. {ECO:0000255}.; TRANSMEM 394 417 Helical; Name=8. {ECO:0000255}.; TRANSMEM 422 445 Helical; Name=9. {ECO:0000255}.; TRANSMEM 558 580 Helical; Name=10. {ECO:0000255}.; TRANSMEM 590 615 Helical; Name=11. {ECO:0000255}.; TRANSMEM 650 667 Helical; Name=12. {ECO:0000255}. TOPO_DOM 1 43 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 64 82 Extracellular. {ECO:0000255}.; TOPO_DOM 104 109 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 135 187 Extracellular. {ECO:0000255}.; TOPO_DOM 217 235 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 257 274 Extracellular. {ECO:0000255}.; TOPO_DOM 300 351 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 374 393 Extracellular. {ECO:0000255}.; TOPO_DOM 418 421 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 446 557 Extracellular. {ECO:0000255}.; TOPO_DOM 581 589 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 616 649 Extracellular. {ECO:0000255}.; TOPO_DOM 668 715 Cytoplasmic. {ECO:0000255}. FUNCTION: Mediates the Na(+)-independent high affinity transport of organic anions such as the thyroid hormones thyroxine (T4) and rT3. Other potential substrates, such as triiodothyronine (T3), estradiol-17-beta-glucuronide, estrone-3-sulfate and sulfobromophthalein (BSP) are transported with much lower efficiency (By similarity). May play a signifiant role in regulating T4 flux into and out of the brain (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18687783}; Multi-pass membrane protein {ECO:0000269|PubMed:18687783}. TISSUE SPECIFICITY: Highly expressed in cerebral microvessels (at protein level). Highly expressed in cerebral microvessels throughout the brain and in tanycytes of the third ventricle. {ECO:0000269|PubMed:18687783}. +Q04888 SOX10_MOUSE Transcription factor SOX-10 (Protein SOX-21) (Transcription factor SOX-M) 466 49,949 Chain (1); Compositional bias (1); DNA binding (1); Erroneous initiation (1); Frameshift (1); Modified residue (1); Natural variant (1); Sequence conflict (3) FUNCTION: Transcription factor that plays a central role in developing and mature glia (PubMed:24204311, PubMed:27532821). Specifically activates expression of myelin genes, during oligodendrocyte (OL) maturation, such as DUSP15 and MYRF, thereby playing a central role in oligodendrocyte maturation and CNS myelination (PubMed:24204311, PubMed:27532821). Once induced, MYRF cooperates with SOX10 to implement the myelination program (PubMed:24204311). Transcriptional activator of MITF, acting synergistically with PAX3 (By similarity). {ECO:0000250|UniProtKB:P56693, ECO:0000269|PubMed:24204311, ECO:0000269|PubMed:27532821}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19304657}. Nucleus {ECO:0000269|PubMed:19304657, ECO:0000269|PubMed:9560246}. Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side {ECO:0000269|PubMed:19304657}. SUBUNIT: Monomer (PubMed:27532821). Interacts with Armcx3 at the mitochondrial outer membrane surface (PubMed:19304657). Interacts with PAX3 (By similarity). {ECO:0000250|UniProtKB:P56693, ECO:0000269|PubMed:19304657, ECO:0000269|PubMed:27532821}. +Q04890 SOX12_MOUSE Transcription factor SOX-12 314 34,083 Chain (1); Compositional bias (4); DNA binding (1); Sequence conflict (1) FUNCTION: Binds to the sequence 5'-AACAAT-3'. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}. TISSUE SPECIFICITY: Expressed in embryonic molar and incisor teeth. {ECO:0000269|PubMed:8921394}. +Q80VJ2 SRA1_MOUSE Steroid receptor RNA activator 1 (Steroid receptor RNA activator protein) (SRAP) 232 25,557 Chain (1); Compositional bias (1); Erroneous initiation (5); Helix (6); Modified residue (1); Sequence caution (1); Sequence conflict (6); Turn (1) FUNCTION: Functional RNA which acts as a transcriptional coactivator that selectively enhances steroid receptor-mediated transactivation ligand-independently through a mechanism involving the modulating N-terminal domain (AF-1) of steroid receptors. Also mediates transcriptional coactivation of steroid receptors ligand-dependently through the steroid-binding domain (AF-2). Enhances cellular proliferation and differentiation and promotes apoptosis in vivo. May play a role in tumorigenesis (By similarity). {ECO:0000250|UniProtKB:Q9HD15}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9HD15}. Cytoplasm {ECO:0000250|UniProtKB:Q9HD15}. SUBUNIT: SRA1 RNA exists in a ribonucleoprotein complex containing NCOA1. The RNA also forms a complex with PUS1 and RARG in the nucleus. Interacts with AR. {ECO:0000250|UniProtKB:Q6QGW5, ECO:0000250|UniProtKB:Q9HD15, ECO:0000269|PubMed:15327771}. +P13609 SRGN_MOUSE Serglycin (Mastocytoma proteoglycan core protein) (Secretory granule proteoglycan core protein) (gp600) 152 16,711 Chain (1); Disulfide bond (1); Glycosylation (8); Propeptide (1); Region (1); Repeat (10); Signal peptide (1) FUNCTION: Plays a role in formation of mast cell secretory granules and mediates storage of various compounds in secretory vesicles. Required for storage of some proteases in both connective tissue and mucosal mast cells and for storage of granzyme B in T-lymphocytes. Plays a role in localizing neutrophil elastase in azurophil granules of neutrophils. Mediates processing of MMP2. Plays a role in cytotoxic cell granule-mediated apoptosis by forming a complex with granzyme B which is delivered to cells by perforin to induce apoptosis. Regulates the secretion of TNF-alpha and may also regulate protease secretion. Inhibits bone mineralization. {ECO:0000269|PubMed:15231821, ECO:0000269|PubMed:16046402, ECO:0000269|PubMed:16807245, ECO:0000269|PubMed:17010166, ECO:0000269|PubMed:17081126, ECO:0000269|PubMed:17147513, ECO:0000269|PubMed:17272511}. PTM: O-glycosylated; contains chondroitin sulfate and heparan sulfate. {ECO:0000269|PubMed:17010166, ECO:0000269|PubMed:7535771}. SUBCELLULAR LOCATION: Cytoplasmic granule {ECO:0000269|PubMed:16046402}. Secreted, extracellular space {ECO:0000269|PubMed:16046402}. Golgi apparatus {ECO:0000250|UniProtKB:P10124}. Note=Found in mast cell granules and in cytoplasmic granules of cytolytic T-lymphocytes from where it is secreted upon cell activation (PubMed:16046402). Secreted constitutively by endothelial cells and macrophages. Located to Golgi apparatus during neutrophil differentiation (By similarity). {ECO:0000250|UniProtKB:P10124, ECO:0000269|PubMed:16046402}. SUBUNIT: Binds to activated CD44 and to GZMB. +P49962 SRP09_MOUSE Signal recognition particle 9 kDa protein (SRP9) 86 10,194 Chain (1); Sequence conflict (1) FUNCTION: Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP. The complex of SRP9 and SRP14 is required for SRP RNA binding. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Signal recognition particle consists of a 7S RNA molecule of 300 nucleotides and six protein subunits: SRP72, SRP68, SRP54, SRP19, SRP14 and SRP9. {ECO:0000269|PubMed:9233785}. +P16254 SRP14_MOUSE Signal recognition particle 14 kDa protein (SRP14) 110 12,510 Beta strand (4); Chain (1); Helix (2); Modified residue (1) FUNCTION: Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP. The complex of SRP9 and SRP14 is required for SRP RNA binding. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Signal recognition particle consists of a 7S RNA molecule of 300 nucleotides and six protein subunits: SRP72, SRP68, SRP54, SRP19, SRP14 and SRP9. {ECO:0000269|PubMed:9233785}. +Q9DBG7 SRPRA_MOUSE Signal recognition particle receptor subunit alpha (SR-alpha) (Docking protein alpha) (DP-alpha) 636 69,623 Chain (1); Erroneous initiation (1); Modified residue (7); Nucleotide binding (3); Sequence conflict (1) FUNCTION: Component of the SRP (signal recognition particle) receptor. Ensures, in conjunction with the signal recognition particle, the correct targeting of the nascent secretory proteins to the endoplasmic reticulum membrane system (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Thought to be anchored in the membrane through an interaction with SR-beta, which contains a bona fide transmembrane domain. {ECO:0000250}. SUBUNIT: Heterodimer with SRPRB. {ECO:0000250}. +Q8R054 SRPX2_MOUSE Sushi repeat-containing protein SRPX2 468 53,140 Chain (1); Disulfide bond (6); Domain (4); Erroneous initiation (2); Sequence conflict (3); Signal peptide (1) FUNCTION: Acts as a ligand for the urokinase plasminogen activator surface receptor. Plays a role in angiogenesis by inducing endothelial cell migration and the formation of vascular network (cords). Involved in cellular migration and adhesion. Increases the phosphorylation levels of FAK. Interacts with and increases the mitogenic activity of HGF. Promotes synapse formation. Required for ultrasonic vocalizations. {ECO:0000269|PubMed:19667118, ECO:0000269|PubMed:24179158}. PTM: Contains chondroitin sulfate chains. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell surface {ECO:0000250}. Cell junction, synapse {ECO:0000250}. SUBUNIT: Forms homooligomers. Interacts with PLAUR (via the UPAR/Ly6 domains), ADAMTS4 and CTSB. Interacts with HGF; the interaction increases the mitogenic activity of HGF (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in angiogenic endothelial cells (at protein level). {ECO:0000269|PubMed:19667118}. +Q8K2M3 SRR1L_MOUSE SRR1-like protein (SRR1 domain-containing protein) 249 27,502 Alternative sequence (1); Chain (1); Sequence conflict (1) FUNCTION: May be involved in a circadian clock input pathway. {ECO:0000250}. +Q9JL10 SRTD1_MOUSE SERTA domain-containing protein 1 (CDK4-binding protein p34SEI1) (SEI-1) (Transcriptional regulator interacting with the PHD-bromodomain 1) (TRIP-Br1) 236 25,136 Chain (1); Domain (1); Sequence conflict (2) FUNCTION: Acts at E2F-responsive promoters as coregulator to integrate signals provided by PHD- and/or bromodomain-containing transcription factors. Stimulates E2F1/TFDP1 transcriptional activity. Renders the activity of cyclin D1/CDK4 resistant to the inhibitory effects of CDKN2A/p16INK4A. {ECO:0000269|PubMed:11331592}. PTM: Polyubiquitinated, which promotes proteasomal degradation. {ECO:0000250}. SUBUNIT: Interacts with the PHD-bromodomain of TIF1, TRIM28/TIF1B and p300/CBP. Interacts with E2F1 and TFDP1; modulates transactivation activity of TFDP1/E2F complexes. Also interacts with CDK4. {ECO:0000269|PubMed:11331592}. TISSUE SPECIFICITY: Detected at in testis, lung and, at lower levels, in muscle, liver, spleen, brain and heart. {ECO:0000269|PubMed:11331592}. +Q9JJG5 SRTD2_MOUSE SERTA domain-containing protein 2 (Transcriptional regulator interacting with the PHD-bromodomain 2) (TRIP-Br2) 309 33,312 Chain (1); Domain (1); Motif (1); Region (1); Sequence conflict (4) FUNCTION: Acts at E2F-responsive promoters as coregulator to integrate signals provided by PHD- and/or bromodomain-containing transcription factors. May act as coactivator as well as corepressor of E2F1-TFDP1 and E2F4-TFDP1 complexes on E2F consensus binding sites, which would activate or inhibit E2F-target genes expression. Modulates fat storage by down-regulating the expression of key genes involved in adipocyte lipolysis, thermogenesis and oxidative metabolism. {ECO:0000269|PubMed:23291629}. PTM: Polyubiquitinated, which promotes proteasomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Exported out of the nucleus via its NES in a XPO1-dependent manner. Once in the cytoplasm, is degraded by the proteasome (By similarity). {ECO:0000250}. SUBUNIT: Interacts with XPO1; which mediates nuclear export. Interacts with TFDP1; modulates transactivation activity of TFDP1/E2F complexes (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in white and brown adipose tissue. {ECO:0000269|PubMed:23291629}. +Q9ERC3 SRTD3_MOUSE SERTA domain-containing protein 3 (Replication protein-binding trans-activator) (RPA-binding trans-activator) 197 21,935 Chain (1); Domain (1) FUNCTION: Strong transcriptional coactivator. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with RPA2. {ECO:0000250}. +A7DTG3 SRTD4_MOUSE SERTA domain-containing protein 4 377 41,096 Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (1); Sequence conflict (1) TISSUE SPECIFICITY: Highly expressed in adult epidermal tissues and in digits. {ECO:0000269|PubMed:16546331}. +P84104 SRSF3_MOUSE Serine/arginine-rich splicing factor 3 (Pre-mRNA-splicing factor SRP20) (Protein X16) (Splicing factor, arginine/serine-rich 3) 164 19,330 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (1); Modified residue (3); Region (2); Repeat (2) FUNCTION: Splicing factor that specifically promotes exon-inclusion during alternative splicing. Interaction with YTHDC1, a RNA-binding protein that recognizes and binds N6-methyladenosine (m6A)-containing RNAs, promotes recruitment of SRSF3 to its mRNA-binding elements adjacent to m6A sites, leading to exon-inclusion during alternative splicing. Also functions as export adapter involved in mRNA nuclear export. Binds mRNA which is thought to be transferred to the NXF1-NXT1 heterodimer for export (TAP/NXF1 pathway); enhances NXF1-NXT1 RNA-binding activity. Involved in nuclear export of m6A-containing mRNAs via interaction with YTHDC1: interaction with YTHDC1 facilitates m6A-containing mRNA-binding to both SRSF3 and NXF1, promoting mRNA nuclear export. RNA-binding is semi-sequence specific. {ECO:0000250|UniProtKB:P84103}. PTM: Phosphorylated by CLK1, CLK2, CLK3 and CLK4. Extensively phosphorylated on serine residues in the RS domain. {ECO:0000269|PubMed:9307018}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P84103}. Nucleus speckle {ECO:0000250|UniProtKB:P84103}. Cytoplasm {ECO:0000250|UniProtKB:P84103}. Note=Recruited to nuclear speckles following interaction with YTHDC1. {ECO:0000250|UniProtKB:P84103}. SUBUNIT: Interacts with CPSF6. Interacts with RBMY1A1. Interacts with SREK1/SFRS12. Interacts with NXF1. Interacts with YTHDC1, leading to recruitment to RNA elements adjacent to m6A sites. {ECO:0000250|UniProtKB:P84103}. TISSUE SPECIFICITY: Highest expression in thymus and pre-B cell lines; high, in testis, brain and spleen; very low in heart and not detectable in liver and kidney. {ECO:0000269|PubMed:2030943}. +Q8VE97 SRSF4_MOUSE Serine/arginine-rich splicing factor 4 (Splicing factor, arginine/serine-rich 4) 489 55,979 Chain (1); Compositional bias (2); Domain (2); Erroneous initiation (1); Modified residue (8); Sequence conflict (3) FUNCTION: Plays a role in alternative splice site selection during pre-mRNA splicing. Represses the splicing of MAPT/Tau exon 10 (By similarity). {ECO:0000250}. PTM: Extensively phosphorylated on serine residues in the RS domain. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}. SUBUNIT: Found in a pre-mRNA splicing complex with SRSF4/SFRS4, SRSF5/SFRS5, SNRNP70, SNRPA1, SRRM1 and SRRM2. Interacts with PNN (By similarity). {ECO:0000250}. +O35326 SRSF5_MOUSE Serine/arginine-rich splicing factor 5 (Delayed-early protein HRS) (Pre-mRNA-splicing factor SRP40) (Splicing factor, arginine/serine-rich 5) 269 30,891 Chain (1); Compositional bias (2); Domain (2); Modified residue (7) FUNCTION: May be required for progression through G1 and entry into S phase of cell growth. May play a regulatory role in pre-mRNA splicing. Autoregulates its own expression. Plays a role in constitutive splicing and can modulate the selection of alternative splice sites (By similarity). {ECO:0000250}. PTM: Extensively phosphorylated on serine residues in the RS domain. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Found in a pre-mRNA splicing complex with SRSF4/SFRS4, SRSF5/SFRS5, SNRNP70, SNRPA1, SRRM1 and SRRM2 (By similarity). Interacts (via RS domain) with PHF5A (via N-terminus). {ECO:0000250, ECO:0000269|PubMed:18758164}. +Q8BV79 TRNK1_MOUSE TPR and ankyrin repeat-containing protein 1 (Lupus brain antigen 1) 2999 343,320 Alternative sequence (1); Chain (1); Compositional bias (2); Repeat (10); Sequence conflict (1) TISSUE SPECIFICITY: Expressed only in the brain. Detected in the hippocampus, hypothalamus and cingulate gyrus. {ECO:0000269|PubMed:9585807}. +Q9CZV5 ST65G_MOUSE STAGA complex 65 subunit gamma (SPTF-associated factor 65 gamma) (STAF65gamma) (Suppressor of Ty 7-like) 412 45,971 Chain (1); Cross-link (1); Modified residue (3) PTM: Sumoylated. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the STAGA transcription coactivator-HAT complex, at least composed of SUPT3H, SUPT7L, GCN5L2, TAF5L, TAF6L, TADA3L, TAD1L, TAF10, TAF12 and TAF9. {ECO:0000250}. +Q80TY4 ST18_MOUSE Suppression of tumorigenicity 18 protein 1045 114,750 Chain (1); Coiled coil (1); Erroneous initiation (2); Sequence conflict (5); Zinc finger (6) FUNCTION: Repressor that binds to DNA sequences containing a bipartite element consisting of a direct repeat of the sequence 5'-AAAGTTT-3' separated by 2-9 nucleotides. Represses basal transcription activity from target promoters (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +P52843 ST2A1_MOUSE Bile salt sulfotransferase 1 (EC 2.8.2.14) (Hydroxysteroid sulfotransferase) (ST) (Sulfotransferase 2A1) (ST2A1) 285 33,213 Active site (1); Binding site (5); Chain (1); Nucleotide binding (3) FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze sulfonation of hydroxysteroids and xenobiotics. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. +O35400 ST2B1_MOUSE Sulfotransferase family cytosolic 2B member 1 (ST2B1) (Sulfotransferase 2B1) (EC 2.8.2.2) (Alcohol sulfotransferase) (Hydroxysteroid sulfotransferase 2) 338 38,347 Active site (1); Alternative sequence (1); Binding site (5); Chain (1); Nucleotide binding (3); Sequence conflict (1) FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of many hormones, neurotransmitters, drugs and xenobiotic compounds. Sulfonation increases the water solubility of most compounds, and therefore their renal excretion, but it can also result in bioactivation to form active metabolites. Sulfates hydroxysteroids such as dehydroepiandrosterone. Isoform 1 is required for production of cholesterol sulfate essential for normal skin development whereas isoform 2 produces pregnenolone sulfate, an essential neurosteroid during development of the central nervous system. Plays a role in epidermal cholesterol metabolism and in the regulation of epidermal proliferation and differentiation. {ECO:0000250|UniProtKB:O00204}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Microsome {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:O00204}. TISSUE SPECIFICITY: Expressed at high levels in epididymis, intestine and uterus, and low levels in brain and hypothalamus. Isoform 2 is most prominent in the brain and spinal cord, with modest expression in the lung, skin and spleen. Isoform 1 is most prominently expressed in skin and small intestine, with modest expression in muscle and prostate. {ECO:0000269|PubMed:12639899, ECO:0000269|PubMed:9647753}. +Q99M96 ST7_MOUSE Suppressor of tumorigenicity 7 protein (mRay) 577 66,095 Alternative sequence (7); Chain (1); Erroneous initiation (1); Glycosylation (1); Modified residue (1); Sequence conflict (3); Transmembrane (4) TRANSMEM 15 35 Helical. {ECO:0000255}.; TRANSMEM 62 82 Helical. {ECO:0000255}.; TRANSMEM 512 532 Helical. {ECO:0000255}.; TRANSMEM 539 559 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9JJX8 ST32B_MOUSE Serine/threonine-protein kinase 32B (EC 2.7.11.1) 414 47,916 Active site (1); Binding site (1); Chain (1); Domain (1); Nucleotide binding (1); Sequence conflict (2) +P42232 STA5B_MOUSE Signal transducer and activator of transcription 5B 786 90,002 Chain (1); Domain (1); Modified residue (4); Mutagenesis (1); Natural variant (1); Sequence conflict (6) FUNCTION: Carries out a dual function: signal transduction and activation of transcription. Mediates cellular responses to the cytokine KITLG/SCF and other growth factors. Binds to the GAS element and activates PRL-induced transcription. Positively regulates hematopoietic/erythroid differentiation. {ECO:0000269|PubMed:7568026}. PTM: Tyrosine phosphorylated in response to signaling via activated KIT, resulting in translocation to the nucleus. Tyrosine phosphorylated in response to signaling via activated FLT3; wild-type FLT3 results in much weaker phosphorylation than constitutively activated mutant FLT3. Alternatively, can be phosphorylated by JAK2 (By similarity). Phosphorylation at Tyr-699 by PTK6 or HCK leads to an increase of its transcriptional activity (By similarity). {ECO:0000250|UniProtKB:P51692, ECO:0000269|PubMed:11773439, ECO:0000269|PubMed:21135090, ECO:0000269|PubMed:21262971}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20639532}. Nucleus {ECO:0000269|PubMed:20639532}. Note=Translocated into the nucleus in response to phosphorylation. SUBUNIT: Forms a homodimer or a heterodimer with a related family member. Binds NR3C1 (PubMed:9528750). Interacts with NCOA1 (By similarity). Interacts with SOCS7 (By similarity). Interacts (via SH2 domain) with INSR (PubMed:9428692). Interacts with CPEB3; this inhibits STAT5B-mediated transcriptional activation (PubMed:20639532). {ECO:0000250|UniProtKB:P51692, ECO:0000269|PubMed:20639532, ECO:0000269|PubMed:9428692, ECO:0000269|PubMed:9528750}. TISSUE SPECIFICITY: In the virgin, found in most tissues. Particularly abundant in muscle tissue of virgin and lactating females, and of males. {ECO:0000269|PubMed:7568026}. +Q9D3E6 STAG1_MOUSE Cohesin subunit SA-1 (SCC3 homolog 1) (Stromal antigen 1) 1258 144,440 Chain (1); Cross-link (1); Domain (1); Modified residue (5); Sequence caution (1); Sequence conflict (2) FUNCTION: Component of cohesin complex, a complex required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis (By similarity). {ECO:0000250}. PTM: Phosphorylated by PLK1. The large dissociation of cohesin from chromosome arms during prophase is partly due to its phosphorylation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00750}. Chromosome {ECO:0000250}. Note=Associates with chromatin. Before prophase it is scattered along chromosome arms. During prophase, most of cohesin complexes dissociate from chromatin probably because of phosphorylation by PLK1, except at centromeres, where cohesin complexes remain. At anaphase, the RAD21 subunit of cohesin is cleaved, leading to the dissociation of the complex from chromosomes, allowing chromosome separation (By similarity). {ECO:0000250}. SUBUNIT: Cohesin complexes are composed of a heterodimer between a SMC1 protein (SMC1A or SMC1B) and SMC3, which are attached via their hinge domain, and RAD21 which link them at their heads, and one STAG protein (STAG1, STAG2 or STAG3). In cohesin complexes, STAG1 is mutually exclusive with STAG2 and STAG3. Interacts directly with RAD21 in cohesin complex. Found in a cohesin complex with SMC1A, SMC3 and RAD21. {ECO:0000250|UniProtKB:Q8WVM7, ECO:0000250|UniProtKB:Q9DGN1}. +Q924W7 ST5_MOUSE Suppression of tumorigenicity 5 protein (DENN domain-containing protein 2B) 1134 126,861 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (3); Erroneous initiation (1); Modified residue (9) FUNCTION: Guanine nucleotide exchange factor (GEF) which may activate RAB9A and RAB9B. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. May be involved in cytoskeletal organization and tumorogenicity. Isoform 1 seems to be involved in a signaling transduction pathway leading to activation of MAPK1/ERK2. Isoform 3 may block ERK2 activation stimulated by ABL1. Isoform 3 may alter cell morphology and cell growth (By similarity). {ECO:0000250}. SUBUNIT: Isoform 1 interacts with the SH3 domain of ABL1. {ECO:0000250}. +Q8R1B0 STAC2_MOUSE SH3 and cysteine-rich domain-containing protein 2 (24b2/STAC2) (Src homology 3 and cysteine-rich domain-containing protein 2) 408 44,793 Chain (1); Compositional bias (1); Domain (2); Modified residue (1); Sequence conflict (2); Zinc finger (1) FUNCTION: Plays a redundant role in promoting the expression of calcium channel CACNA1S at the cell membrane, and thereby contributes to increased channel activity (PubMed:29467163). Slows down the inactivation rate of the calcium channel CACNA1C (PubMed:25548159, PubMed:29363593). {ECO:0000269|PubMed:25548159, ECO:0000269|PubMed:29363593, ECO:0000269|PubMed:29467163}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:28112192, ECO:0000269|PubMed:29467163}. Cell membrane {ECO:0000269|PubMed:25548159}; Peripheral membrane protein {ECO:0000305|PubMed:25548159}; Cytoplasmic side {ECO:0000305|PubMed:25548159}. Cell membrane, sarcolemma {ECO:0000269|PubMed:29467163}; Peripheral membrane protein {ECO:0000269|PubMed:29467163}; Cytoplasmic side {ECO:0000269|PubMed:29467163}. Note=Colocalizes with CACNA1C at the plasma membrane of transfected cells. {ECO:0000269|PubMed:25548159}. SUBUNIT: Interacts (via SH3 domains) with CACNA1S (PubMed:29467163). Interacts (via SH3 domains) with CACNA1C (PubMed:29363593). Has much lower affinity for CACNA1C than for CACNA1S (By similarity). {ECO:0000250|UniProtKB:Q6ZMT1, ECO:0000269|PubMed:29363593, ECO:0000269|PubMed:29467163}. TISSUE SPECIFICITY: Detected in cerebellum, forebrain and midbrain, and in the eye. {ECO:0000269|PubMed:23818578}. +P97306 STAC_MOUSE SH3 and cysteine-rich domain-containing protein (Src homology 3 and cysteine-rich domain-containing protein) 403 44,319 Chain (1); Domain (2); Zinc finger (1) FUNCTION: Promotes expression of the ion channel CACNA1H at the cell membrane, and thereby contributes to the regulation of channel activity (PubMed:27149520). Plays a minor and redundant role in promoting the expression of calcium channel CACNA1S at the cell membrane, and thereby contributes to increased channel activity (PubMed:29467163). Slows the rate of calcium-mediated inactivation of CACNA1C calcium channel activity (PubMed:29363593). {ECO:0000269|PubMed:27149520, ECO:0000269|PubMed:29363593, ECO:0000269|PubMed:29467163}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:28112192, ECO:0000269|PubMed:29467163}. Cell membrane {ECO:0000269|PubMed:29467163}; Peripheral membrane protein {ECO:0000269|PubMed:29467163}; Cytoplasmic side {ECO:0000269|PubMed:29467163}. Cell membrane, sarcolemma {ECO:0000269|PubMed:29363593}; Peripheral membrane protein {ECO:0000269|PubMed:29363593}; Cytoplasmic side {ECO:0000269|PubMed:29363593}. SUBUNIT: Interacts (via SH3 domains) with CACNA1S (PubMed:29467163). Interacts with CACNA1H (PubMed:27149520). Interacts with CACNA1C (Probable) (PubMed:29363593). {ECO:0000269|PubMed:27149520, ECO:0000269|PubMed:29363593, ECO:0000269|PubMed:29467163, ECO:0000305|PubMed:28112192}. TISSUE SPECIFICITY: Expressed predominantly in brain (PubMed:8954993, PubMed:23818578) Detected in brain neurons, more specifically in hippocampus, cerebellum and inferior olive (PubMed:8954993). Highly expressed in urinary bladder, and detected at lower levels in adrenal gland (PubMed:23818578). Detected at very low levels in heart, liver, lung and kidney (PubMed:8954993). {ECO:0000269|PubMed:23818578, ECO:0000269|PubMed:8954993}. +P42225 STAT1_MOUSE Signal transducer and activator of transcription 1 749 87,197 Chain (1); Coiled coil (1); Cross-link (3); Domain (1); Initiator methionine (1); Modified residue (14); Mutagenesis (2) FUNCTION: Signal transducer and transcription activator that mediates cellular responses to interferons (IFNs), cytokine KITLG/SCF and other cytokines and other growth factors. Following type I IFN (IFN-alpha and IFN-beta) binding to cell surface receptors, signaling via protein kinases leads to activation of Jak kinases (TYK2 and JAK1) and to tyrosine phosphorylation of STAT1 and STAT2. The phosphorylated STATs dimerize and associate with ISGF3G/IRF-9 to form a complex termed ISGF3 transcription factor, that enters the nucleus. ISGF3 binds to the IFN stimulated response element (ISRE) to activate the transcription of IFN-stimulated genes (ISG), which drive the cell in an antiviral state. In response to type II IFN (IFN-gamma), STAT1 is tyrosine- and serine-phosphorylated. It then forms a homodimer termed IFN-gamma-activated factor (GAF), migrates into the nucleus and binds to the IFN gamma activated sequence (GAS) to drive the expression of the target genes, inducing a cellular antiviral state. Becomes activated in response to KITLG/SCF and KIT signaling. May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4. {ECO:0000269|PubMed:11294897, ECO:0000269|PubMed:19088846, ECO:0000269|PubMed:22065572, ECO:0000269|PubMed:9344858}. PTM: Phosphorylated on tyrosine and serine residues in response to a variety of cytokines/growth hormones including IFN-alpha, IFN-gamma, PDGF and EGF. Activated KIT promotes phosphorylation on tyrosine residues and subsequent translocation to the nucleus. Upon EGF stimulation, phosphorylation on Tyr-701 (lacking in beta form) by JAK1, JAK2 or TYK2 promotes dimerization and subsequent translocation to the nucleus. Growth hormone (GH) activates STAT1 signaling only via JAK2. Tyrosine phosphorylated in response to constitutively activated FGFR1, FGFR2, FGFR3 and FGFR4. Phosphorylation on Ser-727 by several kinases including MAPK14, ERK1/2 and CAMKII on IFN-gamma stimulation, regulates STAT1 transcriptional activity. Phosphorylation on Ser-727 promotes sumoylation though increasing interaction with PIAS. Phosphorylation on Ser-727 by PRKCD induces apoptosis in response to DNA-damaging agents. Phosphorylated on tyrosine residues when PTK2/FAK1 is activated; most likely this is catalyzed by a SRC family kinase. Dephosphorylation on tyrosine residues by PTPN2 negatively regulates interferon-mediated signaling. Upon viral infection or IFN induction, phosphorylation on Ser-708 occurs much later than phosphorylation on Tyr-701 and is required for the binding of ISGF3 on the ISREs of a subset of IFN-stimulated genes IKBKE-dependent. Phosphorylation at Tyr-701 and Ser-708 are mutually exclusive, phosphorylation at Ser-708 requires previous dephosphorylation of Tyr-701. {ECO:0000269|PubMed:11294897, ECO:0000269|PubMed:12138178, ECO:0000269|PubMed:17332413, ECO:0000269|PubMed:19088846, ECO:0000269|PubMed:21135090, ECO:0000269|PubMed:22065572, ECO:0000269|PubMed:9344858}.; PTM: Sumoylated with SUMO1, SUMO2 and SUMO3. Sumoylation is enhanced by IFN-gamma-induced phosphorylation on Ser-727, and by interaction with PIAS proteins. Enhances the transactivation activity. {ECO:0000250|UniProtKB:P42224}.; PTM: ISGylated. {ECO:0000269|PubMed:16139798}.; PTM: Mono-ADP-ribosylated at Glu-657 and Glu-705 by PARP14; ADP-riboslyation prevents phosphorylation at Tyr-701. {ECO:0000250|UniProtKB:P42224}.; PTM: Monomethylated at Lys-525 by SETD2; monomethylation is necessary for phosphorylation at Tyr-701, translocation into the nucleus and activation of the antiviral defense. {ECO:0000250|UniProtKB:P42224}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11294897}. Nucleus {ECO:0000269|PubMed:11294897}. Note=Translocated into the nucleus upon tyrosine phosphorylation and dimerization, in response to IFN-gamma and signaling by activated FGFR1, FGFR2, FGFR3 or FGFR4. Monomethylation at Lys-525 is required for phosphorylation at Tyr-701 and translocation into the nucleus. Translocates into the nucleus in response to interferon-beta stimulation. {ECO:0000250|UniProtKB:P42224}. SUBUNIT: Homodimerizes upon IFN-gamma induced phosphorylation (By similarity). Heterodimer with STAT2 upon IFN-alpha/beta induced phosphorylation (By similarity). The heterodimer STAT1:STAT2 forms the interferon-stimulated gene factor 3 complex (ISGF3) with IRF9 (PubMed:17332413). Interacts (phosphorylated at Ser-727) with PIAS1; the interaction results in release of STAT1 from its target gene (By similarity). Interacts with IFNAR1 (By similarity). Interacts with IFNAR2 (By similarity). Found in a complex with NMI and CREBBP/CBP (By similarity). Interacts with NMI which is required for CREBBP/CBP recruitment to the complex (By similarity). Interacts with PTK2/FAK1 (By similarity). Interacts with SRC (PubMed:9344858). Interacts with ERBB4 (phosphorylated) (By similarity). Interacts with PARP9 and DTX3L independently of IFN-beta or IFN-gamma-mediated STAT1 'Tyr-701' phosphorylation (By similarity). Interacts with histone acetyltransferase EP300/p300 in response to INF-gamma stimulation (By similarity). Interacts with OTOP1 (PubMed:24379350). {ECO:0000250|UniProtKB:P42224, ECO:0000269|PubMed:17332413, ECO:0000269|PubMed:24379350, ECO:0000269|PubMed:9344858}. +Q8R1R3 STAR7_MOUSE StAR-related lipid transfer protein 7, mitochondrial (START domain-containing protein 7) (StARD7) 373 43,144 Chain (1); Coiled coil (1); Domain (1); Transit peptide (1) FUNCTION: May play a protective role in mucosal tissues by preventing exaggerated allergic responses. {ECO:0000269|PubMed:25980009}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}. TISSUE SPECIFICITY: Expressed in epithelial cells of airways, peripheral bronchioles and alveoli, as well as in the basal cell layer of the epidermis (at protein level). {ECO:0000269|PubMed:25980009}. +P42228 STAT4_MOUSE Signal transducer and activator of transcription 4 749 85,941 Chain (1); Domain (1); Helix (10); Modified residue (1); Sequence conflict (2) FUNCTION: Carries out a dual function: signal transduction and activation of transcription. PTM: Tyrosine phosphorylated. Serine phosphorylation is also required for maximal transcriptional activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Translocated into the nucleus in response to phosphorylation. SUBUNIT: Forms a homodimer or a heterodimer with a related family member (By similarity). Interacts with ARL2BP. {ECO:0000250, ECO:0000269|PubMed:18234692}. +P52633 STAT6_MOUSE Signal transducer and transcription activator 6 837 93,497 Chain (1); Domain (1); Initiator methionine (1); Modified residue (2); Motif (1); Sequence conflict (18) FUNCTION: Carries out a dual function: signal transduction and activation of transcription. Involved in IL4/interleukin-4- and IL3/interleukin-3-mediated signaling. {ECO:0000269|PubMed:17210636}. PTM: Tyrosine phosphorylated on Tyr-641 following stimulation by IL4/interleukin-4. Tyrosine phosphorylated following stimulation by IL3/interleukin-3. Dephosphorylation on tyrosine residues by PTPN2 negatively regulates the IL4/interleukin-4 mediated signaling. {ECO:0000269|PubMed:17210636}.; PTM: Mono-ADP-ribosylated by PARP14. {ECO:0000250|UniProtKB:P42226}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Translocated into the nucleus in response to phosphorylation. SUBUNIT: Forms a homodimer or a heterodimer with a related family member. Interacts with NCOA1 via its C-terminal LXXLL motif (By similarity). {ECO:0000250}. +O88452 STC2_MOUSE Stanniocalcin-2 (STC-2) 296 32,602 Chain (1); Glycosylation (1); Signal peptide (1) FUNCTION: Has an anti-hypocalcemic action on calcium and phosphate homeostasis. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}. TISSUE SPECIFICITY: Found in a variety of tissues including skeletal muscle, small intestine, kidney, liver and brain. +Q8CI59 STEA3_MOUSE Metalloreductase STEAP3 (EC 1.16.1.-) (Dudulin-2) (Protein nm1054) (Six-transmembrane epithelial antigen of prostate 3) (Tumor suppressor-activated pathway protein 6) 488 54,749 Alternative sequence (1); Binding site (8); Chain (1); Domain (1); Frameshift (1); Glycosylation (1); Metal binding (2); Modified residue (4); Mutagenesis (2); Nucleotide binding (3); Sequence conflict (9); Site (1); Topological domain (7); Transmembrane (6) TRANSMEM 208 228 Helical. {ECO:0000255}.; TRANSMEM 259 279 Helical. {ECO:0000255}.; TRANSMEM 305 325 Helical. {ECO:0000255}.; TRANSMEM 359 379 Helical. {ECO:0000255}.; TRANSMEM 391 411 Helical. {ECO:0000255}.; TRANSMEM 434 454 Helical. {ECO:0000255}. TOPO_DOM 1 207 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 229 258 Vesicular. {ECO:0000255}.; TOPO_DOM 280 304 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 326 358 Vesicular. {ECO:0000255}.; TOPO_DOM 380 390 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 412 433 Vesicular. {ECO:0000255}.; TOPO_DOM 455 488 Cytoplasmic. {ECO:0000255}. FUNCTION: Endosomal ferrireductase required for efficient transferrin-dependent iron uptake in erythroid cells. Participates in erythroid iron homeostasis by reducing Fe(3+) to Fe(2+). Also mediates reduction of Cu(2+) to Cu(1+), suggesting that it participates in copper homeostasis. Uses NADP(+) as acceptor. May play a role downstream of p53/TP53 to interface apoptosis and cell cycle progression. Indirectly involved in exosome secretion by facilitating the secretion of proteins such as TCTP. {ECO:0000269|PubMed:16227996, ECO:0000269|PubMed:16609065}. PTM: Proteolytically cleaved by RHBDL4/RHBDD1. RHBDL4/RHBDD1-induced cleavage occurs at multiple sites in a glycosylation-independent manner (By similarity). {ECO:0000250}.; PTM: Glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:16227996}; Multi-pass membrane protein {ECO:0000269|PubMed:16227996}. SUBUNIT: Homodimer. Interacts with BNIP3L, MYT1, RHBDL4/RHBDD1 and TCTP (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in fetal liver (the site of midgestational hematopoiesis). {ECO:0000269|PubMed:12606722, ECO:0000269|PubMed:16227996}. +Q923B6 STEA4_MOUSE Metalloreductase STEAP4 (EC 1.16.1.9) (Dudulin-4) (Six-transmembrane epithelial antigen of prostate 4) (Tumor necrosis factor-alpha-induced adipose-related protein) 470 52,994 Binding site (10); Chain (1); Domain (1); Frameshift (1); Metal binding (2); Nucleotide binding (3); Sequence conflict (15); Transmembrane (6) TRANSMEM 202 224 Helical. {ECO:0000250|UniProtKB:Q687X5}.; TRANSMEM 236 256 Helical. {ECO:0000250|UniProtKB:Q687X5}.; TRANSMEM 293 313 Helical. {ECO:0000250|UniProtKB:Q687X5}.; TRANSMEM 342 362 Helical. {ECO:0000250|UniProtKB:Q687X5}.; TRANSMEM 381 401 Helical. {ECO:0000250|UniProtKB:Q687X5}.; TRANSMEM 419 439 Helical. {ECO:0000250|UniProtKB:Q687X5}. FUNCTION: Integral membrane protein that functions as NADPH-dependent ferric-chelate reductase, using NADPH from one side of the membrane to reduce a Fe(3+) chelate that is bound on the other side of the membrane (PubMed:16609065). Mediates sequential transmembrane electron transfer from NADPH to FAD and onto heme, and finally to the Fe(3+) chelate (By similarity). Can also reduce Cu(2+) to Cu(1+) (PubMed:16609065). Plays a role in systemic metabolic homeostasis, integrating inflammatory and metabolic responses (PubMed:17482547). Associated with obesity and insulin-resistance (By similarity). Involved in inflammatory arthritis, through the regulation of inflammatory cytokines (PubMed:19660107). Inhibits anchorage-independent cell proliferation (By similarity). {ECO:0000250|UniProtKB:Q687X5, ECO:0000269|PubMed:16609065, ECO:0000269|PubMed:17482547, ECO:0000269|PubMed:19660107}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11443137, ECO:0000269|PubMed:16609065}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q687X5}. Golgi apparatus membrane {ECO:0000305|PubMed:11443137}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q687X5}. Early endosome membrane {ECO:0000269|PubMed:16609065}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q687X5}. SUBUNIT: Homotrimer. Interacts with PTK2/FAK1; the interaction may regulate PTK2 phosphorylation. {ECO:0000250|UniProtKB:Q687X5}. TISSUE SPECIFICITY: Expressed in white and brown adipose tissues cells, as well as in muscle and liver cells. Detected in joints and spleens of arthritic mice. {ECO:0000269|PubMed:14988015, ECO:0000269|PubMed:19660107}. +Q60988 STIL_MOUSE SCL-interrupting locus protein homolog 1262 138,757 Chain (1); Frameshift (1); Modified residue (3); Mutagenesis (7); Region (3); Sequence conflict (12) FUNCTION: Immediate-early gene. Plays an important role in embryonic development as well as in cellular growth and proliferation; its long-term silencing affects cell survival and cell cycle distribution as well as decreases CDK1 activity correlated with reduced phosphorylation of CDK1. Plays a role as a positive regulator of the sonic hedgehog pathway, acting downstream of PTCH1. Plays an important role in the regulation of centriole duplication. Required for the onset of procentriole formation and proper mitotic progression. During procentriole formation, is essential for the correct loading of SASS6 and CENPJ to the base of the procentriole to initiate procentriole assembly (By similarity). {ECO:0000250|UniProtKB:Q15468, ECO:0000269|PubMed:10385121, ECO:0000269|PubMed:11668681, ECO:0000269|PubMed:8825637}. PTM: Ubiquitinated. {ECO:0000250|UniProtKB:Q15468}.; PTM: Phosphorylated following the activation of the mitotic checkpoint. {ECO:0000305|PubMed:16024801}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q15468}. SUBUNIT: Homodimer (By similarity). Interacts with PIN1 via its WW domain. This interaction is dependent on Stil mitotic phosphorylation (PubMed:16024801). Interacts with CENPJ. Interacts with RBM14 and this interaction interferes with the interaction of STIL with CENPJ. Forms a complex with CENPJ and SASS6 (By similarity). {ECO:0000250|UniProtKB:Q15468, ECO:0000269|PubMed:16024801}. TISSUE SPECIFICITY: Ubiquitously expressed in adult and fetal tissues. Highly expressed in hematopoietic tissues such as thymus, bone marrow and spleen. {ECO:0000269|PubMed:1922059, ECO:0000269|PubMed:8825637}. +Q3TBT3 STING_MOUSE Stimulator of interferon genes protein (mSTING) (Endoplasmic reticulum interferon stimulator) (ERIS) (Mediator of IRF3 activation) (MMITA) (Transmembrane protein 173) 378 42,830 Alternative sequence (2); Beta strand (8); Binding site (1); Chain (1); Cross-link (1); Erroneous initiation (1); Erroneous termination (1); Frameshift (1); Helix (9); Modified residue (1); Mutagenesis (4); Region (4); Sequence conflict (10); Topological domain (5); Transmembrane (4); Turn (3) TRANSMEM 21 41 Helical; Name=1. {ECO:0000255}.; TRANSMEM 47 67 Helical; Name=2. {ECO:0000255}.; TRANSMEM 87 106 Helical; Name=3. {ECO:0000255}.; TRANSMEM 115 135 Helical; Name=4. {ECO:0000255}. TOPO_DOM 1 20 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 42 46 Extracellular. {ECO:0000255}.; TOPO_DOM 68 86 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 107 114 Extracellular. {ECO:0000255}.; TOPO_DOM 136 378 Cytoplasmic. {ECO:0000255}. FUNCTION: Facilitator of innate immune signaling that acts as a sensor of cytosolic DNA from bacteria and viruses and promotes the production of type I interferon (IFN-alpha and IFN-beta). Innate immune response is triggered in response to non-CpG double-stranded DNA from viruses and bacteria delivered to the cytoplasm. Acts by recognizing and binding cyclic di-GMP (c-di-GMP), a second messenger produced by bacteria, and cyclic GMP-AMP (cGAMP), a messenger produced in response to DNA virus in the cytosol: upon binding of c-di-GMP or cGAMP, autoinhibition is alleviated and TMEM173/STING is able to activate both NF-kappa-B and IRF3 transcription pathways to induce expression of type I interferon and exert a potent anti-viral state. May be involved in translocon function, the translocon possibly being able to influence the induction of type I interferons. May be involved in transduction of apoptotic signals via its association with the major histocompatibility complex class II (MHC-II). Mediates death signaling via activation of the extracellular signal-regulated kinase (ERK) pathway. Exhibits 2',3' phosphodiester linkage-specific ligand recognition. Can bind both 2'-3' linked cGAMP and 3'-3' linked cGAMP but is preferentially activated by 2'-3' linked cGAMP (PubMed:26300263). {ECO:0000269|PubMed:18559423, ECO:0000269|PubMed:18724357, ECO:0000269|PubMed:18818105, ECO:0000269|PubMed:19433799, ECO:0000269|PubMed:19776740, ECO:0000269|PubMed:23258412, ECO:0000269|PubMed:23722158, ECO:0000269|PubMed:26229117, ECO:0000269|PubMed:26300263, ECO:0000269|PubMed:26669264}. PTM: Phosphorylated on Ser-357 by TBK1, leading to activation and production of IFN-beta (By similarity). Phosphorylated on tyrosine residues upon MHC-II aggregation. {ECO:0000250|UniProtKB:Q86WV6, ECO:0000269|PubMed:18559423}.; PTM: Ubiquitinated. 'Lys-63'-linked ubiquitination mediated by TRIM56 at Lys-150 promotes homodimerization and recruitment of the antiviral kinase TBK1 and subsequent production of IFN-beta. 'Lys-48'-linked polyubiquitination at Lys-150 occurring after viral infection is mediated by RNF5 and leads to proteasomal degradation. 'Lys-11'-linked polyubiquitination at Lys-150 by RNF26 leads to stabilize TMEM173/STING: it protects TMEM173/STING from RNF5-mediated 'Lys-48'-linked polyubiquitination. {ECO:0000250|UniProtKB:Q86WV6}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19776740}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane {ECO:0000269|PubMed:18559423}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:18559423}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q86WV6}. Cytoplasm {ECO:0000250|UniProtKB:Q86WV6}. Note=In response to double-stranded DNA stimulation, relocalizes to perinuclear region, where the kinase TBK1 is recruited. SUBUNIT: Homodimer; 'Lys-63'-linked ubiquitination at Lys-150 is required for homodimerization (PubMed:18559423). Interacts with TBK1; when homodimer, leading to subsequent production of IFN-beta (By similarity). Interacts with DDX58/RIG-I, MAVS and SSR2. Interacts with RNF5. Associates with the MHC-II complex. Interacts with IFIT1 and IFIT2 (By similarity). Interacts with TRIM29; this interaction induces TMEM173/STING ubiquitination and subsequent degradation (By similarity). {ECO:0000250|UniProtKB:Q86WV6, ECO:0000269|PubMed:18559423}. DOMAIN: The c-di-GMP-binding domain (CBD) forms a homodimer via hydrophobic interactions and binds both the cyclic diguanylate monophosphate (c-di-GMP) and the cyclic GMP-AMP (cGAMP) messengers. In absence of c-di-GMP or cGAMP, the protein is autoinhibited by an intramolecular interaction between the CBD and the C-terminal tail (CTT). Binding of c-di-GMP or cGAMP to the CBD releases the autoinhibition by displacing the CTT, leading to activate both NF-kappa-B and IRF3 transcription pathways to induce expression of type I interferon. The N-terminal part of the CBD region was initially though to contain a fifth transmembrane region (TM5) but is part of the folded, soluble CBD (By similarity). {ECO:0000250|UniProtKB:Q86WV6}. TISSUE SPECIFICITY: Present in spleen and thymus tissue. Also present in dendritic cells (at protein level). {ECO:0000269|PubMed:18559423}. +O55098 STK10_MOUSE Serine/threonine-protein kinase 10 (EC 2.7.11.1) (Lymphocyte-oriented kinase) 966 111,906 Active site (1); Binding site (5); Chain (1); Coiled coil (1); Compositional bias (1); Domain (1); Modified residue (11); Nucleotide binding (1); Region (1); Sequence conflict (4) FUNCTION: Serine/threonine-protein kinase involved in regulation of lymphocyte migration. Phosphorylates MSN, and possibly PLK1. Involved in regulation of lymphocyte migration by mediating phosphorylation of ERM proteins such as MSN. Acts as a negative regulator of MAP3K1/MEKK1. May also act as a cell cycle regulator by acting as a polo kinase kinase: mediates phosphorylation of PLK1 in vitro; however such data require additional evidences in vivo. {ECO:0000269|PubMed:19255442}. PTM: Autophosphorylates following homodimerization, leading to activation of the protein. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. SUBUNIT: Homodimer; homodimerization is required for activation segment autophosphorylation. {ECO:0000250}. TISSUE SPECIFICITY: Expressed predominantly in lymphoid organs such as spleen, thymus, and bone marrow. +Q80YS9 STKL1_MOUSE Serine/threonine kinase-like domain-containing protein STKLD1 (Serine/threonine kinase-like domain-containing protein 1) (Sugen kinase 071) 662 74,843 Binding site (1); Chain (1); Domain (1); Frameshift (1); Nucleotide binding (1) DOMAIN: The protein kinase domain is predicted to be catalytically inactive. +Q8R3F9 STPAP_MOUSE Speckle targeted PIP5K1A-regulated poly(A) polymerase (Star-PAP) (EC 2.7.7.19) (RNA-binding motif protein 21) (RNA-binding protein 21) (U6 snRNA-specific terminal uridylyltransferase 1) (U6-TUTase) (EC 2.7.7.52) 869 94,603 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (2); Metal binding (2); Modified residue (2); Zinc finger (1) FUNCTION: Poly(A) polymerase that creates the 3'-poly(A) tail of specific pre-mRNAs. Localizes to nuclear speckles together with PIP5K1A and mediates polyadenylation of a select set of mRNAs, such as HMOX1. In addition to polyadenylation, it is also required for the 3'-end cleavage of pre-mRNAs: binds to the 3'UTR of targeted pre-mRNAs and promotes the recruitment and assembly of the CPSF complex on the 3'UTR of pre-mRNAs. In addition to adenylyltransferase activity, also has uridylyltransferase activity. However, the ATP ratio is higher than UTP in cells, suggesting that it functions primarily as a poly(A) polymerase. Acts as a specific terminal uridylyltransferase for U6 snRNA in vitro: responsible for a controlled elongation reaction that results in the restoration of the four 3'-terminal UMP-residues found in newly transcribed U6 snRNA. Not involved in replication-dependent histone mRNA degradation (By similarity). {ECO:0000250}. PTM: Phosphorylated by CK1 in the proline-rich (Pro-rich) region. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9H6E5}. Nucleus speckle {ECO:0000250|UniProtKB:Q9H6E5}. SUBUNIT: Associates with the cleavage and polyadenylation specificity factor (CPSF) complex. Interacts with CPSF1 and CPSF3; the interaction is direct. Interacts with PIP5K1A; interaction (By similarity). {ECO:0000250}. +Q9D2F5 STPG1_MOUSE O(6)-methylguanine-induced apoptosis 2 (MAPO2) (Sperm-tail PG-rich repeat-containing protein 1) 341 37,499 Chain (1); Modified residue (1); Repeat (7) FUNCTION: May positively contribute to the induction of apoptosis triggered by O(6)-methylguanine. {ECO:0000269|PubMed:23028632}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23028632}. Nucleus {ECO:0000269|PubMed:23028632}. +Q8C8J0 STPG2_MOUSE Sperm-tail PG-rich repeat-containing protein 2 561 62,698 Chain (1); Repeat (10) +Q9DBN1 STR6L_MOUSE Stimulated by retinoic acid gene 6 protein-like (STRA6-like protein) (Retinol-binding protein 4 receptor 2) (RBP4 receptor 2) 621 71,003 Alternative sequence (1); Chain (1); Glycosylation (1); Modified residue (1); Sequence conflict (5); Topological domain (11); Transmembrane (10) TRANSMEM 22 42 Helical. {ECO:0000255}.; TRANSMEM 54 74 Helical. {ECO:0000255}.; TRANSMEM 111 131 Helical. {ECO:0000255}.; TRANSMEM 138 158 Helical. {ECO:0000255}.; TRANSMEM 174 194 Helical. {ECO:0000255}.; TRANSMEM 259 279 Helical. {ECO:0000255}.; TRANSMEM 322 342 Helical. {ECO:0000255}.; TRANSMEM 384 404 Helical. {ECO:0000255}.; TRANSMEM 425 445 Helical. {ECO:0000255}.; TRANSMEM 477 497 Helical. {ECO:0000255}. TOPO_DOM 1 21 Extracellular. {ECO:0000305}.; TOPO_DOM 43 53 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 75 110 Extracellular. {ECO:0000305}.; TOPO_DOM 132 137 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 159 173 Extracellular. {ECO:0000305}.; TOPO_DOM 195 258 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 280 321 Extracellular. {ECO:0000305}.; TOPO_DOM 343 383 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 405 424 Extracellular. {ECO:0000305}.; TOPO_DOM 446 476 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 498 621 Extracellular. {ECO:0000305}. FUNCTION: Acts as a high-affinity cell-surface receptor for retinol-binding protein RBP4 and mediates RBP4-dependent retinol uptake in the liver. {ECO:0000269|PubMed:23105095}. PTM: Glycosylated. {ECO:0000269|PubMed:23105095}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23105095}; Multi-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Highly expressed in liver and small intestine. Also expressed in spleen, kidney, colon, stomach, placenta, adipose tissue and isolated adipocytes. {ECO:0000269|PubMed:23105095}. +Q9Z1Z2 STRAP_MOUSE Serine-threonine kinase receptor-associated protein (UNR-interacting protein) 350 38,442 Chain (1); Modified residue (4); Repeat (7); Sequence conflict (2) FUNCTION: The SMN complex plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus. STRAP plays a role in the cellular distribution of the SMN complex. Negatively regulates TGF-beta signaling but positively regulates the PDPK1 kinase activity by enhancing its autophosphorylation and by significantly reducing the association of PDPK1 with 14-3-3 protein (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Localized predominantly in the cytoplasm but also found in the nucleus. {ECO:0000250}. SUBUNIT: Part of the core SMN complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8 and STRAP/UNRIP. Part of the SMN-Sm complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8, STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG. Interacts directly with GEMIN6 and GEMIN7. Associates with the SMN complex in the cytoplasm but not in the nucleus. Also interacts with CSDE1/UNR and MAWBP. Interacts with PDPK1 (By similarity). {ECO:0000250}. +Q91WM1 STRBP_MOUSE Spermatid perinuclear RNA-binding protein 672 73,705 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (3); Modified residue (2) FUNCTION: Involved in spermatogenesis and sperm function. Plays a role in regulation of cell growth (By similarity). Binds to double-stranded DNA and RNA (By similarity). Binds most efficiently to poly(I:C) RNA than to poly(dI:dC) DNA (By similarity). Binds also to single-stranded poly(G) RNA (By similarity). Binds non-specifically to the mRNA PRM1 3'-UTR and adenovirus VA RNA. {ECO:0000250, ECO:0000269|PubMed:11336498, ECO:0000269|PubMed:7744952}. SUBCELLULAR LOCATION: Isoform 2: Cytoplasm, cytoskeleton. Note=Microtubule-associated that localizes to the manchette in developing spermatids. SUBUNIT: Interacts with EIF2AK2 (By similarity). Associates with microtubules; it is unsure whether such interaction is direct or indirect. {ECO:0000250, ECO:0000269|PubMed:9674995}. TISSUE SPECIFICITY: Isoform 2 is expressed in spermatocytes (at protein level). Expressed in testis, thymus, ovary, liver, kidney, heart, spleen and brain. Expressed in cortex, dentate gyrus and Purkinje cell layer and granule cells of the cerebellum. {ECO:0000269|PubMed:11336498, ECO:0000269|PubMed:7744952}. +Q3TDQ1 STT3B_MOUSE Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B (Oligosaccharyl transferase subunit STT3B) (STT3-B) (EC 2.4.99.18) (B6dom1 antigen) (Source of immunodominant MHC-associated peptides) 823 93,246 Binding site (5); Chain (1); Erroneous initiation (1); Glycosylation (4); Initiator methionine (1); Metal binding (3); Modified residue (6); Motif (5); Natural variant (1); Region (1); Sequence conflict (4); Site (1); Topological domain (14); Transmembrane (13) TRANSMEM 42 83 Helical. {ECO:0000250|UniProtKB:P39007}.; TRANSMEM 171 189 Helical. {ECO:0000250|UniProtKB:P39007}.; TRANSMEM 192 209 Helical. {ECO:0000250|UniProtKB:P39007}.; TRANSMEM 221 240 Helical. {ECO:0000250|UniProtKB:P39007}.; TRANSMEM 243 257 Helical. {ECO:0000250|UniProtKB:P39007}.; TRANSMEM 263 279 Helical. {ECO:0000250|UniProtKB:P39007}.; TRANSMEM 285 310 Helical. {ECO:0000250|UniProtKB:P39007}.; TRANSMEM 319 338 Helical. {ECO:0000250|UniProtKB:P39007}.; TRANSMEM 348 368 Helical. {ECO:0000255}.; TRANSMEM 408 430 Helical. {ECO:0000250|UniProtKB:P39007}.; TRANSMEM 437 453 Helical. {ECO:0000250|UniProtKB:P39007}.; TRANSMEM 458 479 Helical. {ECO:0000250|UniProtKB:P39007}.; TRANSMEM 524 549 Helical. {ECO:0000250|UniProtKB:P39007}. TOPO_DOM 2 41 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 84 170 Lumenal. {ECO:0000305}.; TOPO_DOM 190 191 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 210 220 Lumenal. {ECO:0000305}.; TOPO_DOM 241 242 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 258 262 Lumenal. {ECO:0000305}.; TOPO_DOM 280 284 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 311 318 Lumenal. {ECO:0000305}.; TOPO_DOM 339 347 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 369 407 Lumenal. {ECO:0000305}.; TOPO_DOM 431 436 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 454 457 Lumenal. {ECO:0000305}.; TOPO_DOM 480 523 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 550 823 Lumenal. {ECO:0000305}. Protein modification; protein glycosylation. FUNCTION: Catalytic subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. This subunit contains the active site and the acceptor peptide and donor lipid-linked oligosaccharide (LLO) binding pockets (By similarity). STT3B is present in a small subset of OST complexes and mediates both cotranslational and post-translational N-glycosylation of target proteins: STT3B-containing complexes are required for efficient post-translational glycosylation and while they are less competent than STT3A-containing complexes for cotranslational glycosylation, they have the ability to mediate glycosylation of some nascent sites that are not accessible for STT3A. STT3B-containing complexes also act post-translationally and mediate modification of skipped glycosylation sites in unfolded proteins. Plays a role in ER-associated degradation (ERAD) pathway that mediates ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins by mediating N-glycosylation of unfolded proteins, which are then recognized by the ERAD pathway and targeted for degradation (By similarity). {ECO:0000250|UniProtKB:E2RG47, ECO:0000250|UniProtKB:P39007, ECO:0000250|UniProtKB:Q8TCJ2}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8TCJ2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P39007}. SUBUNIT: Component of the oligosaccharyltransferase (OST) complex. OST exists in two different complex forms which contain common core subunits RPN1, RPN2, OST48, OST4, DAD1 and TMEM258, either STT3A or STT3B as catalytic subunits, and form-specific accessory subunits. OST can form stable complexes with the Sec61 complex or with both the Sec61 and TRAP complexes (By similarity). {ECO:0000250|UniProtKB:E2RG47}. DOMAIN: Despite low primary sequence conservation between eukaryotic catalytic subunits and bacterial and archaeal single subunit OSTs (ssOST), structural comparison revealed several common motifs at spatially equivalent positions, like the DXD motif 1 on the external loop 1 and the DXD motif 2 on the external loop 2 involved in binding of the metal ion cofactor and the carboxamide group of the acceptor asparagine, the conserved Glu residue of the TIXE/SVSE motif on the external loop 5 involved in catalysis, as well as the WWDYG and the DK/MI motifs in the globular domain that define the binding pocket for the +2 Ser/Thr of the acceptor sequon. In bacterial ssOSTs, an Arg residue was found to interact with a negatively charged side chain at the -2 position of the sequon. This Arg is conserved in bacterial enzymes and correlates with an extended sequon requirement (Asp-X-Asn-X-Ser/Thr) for bacterial N-glycosylation. {ECO:0000250|UniProtKB:P39007}. +Q9WV89 STXB4_MOUSE Syntaxin-binding protein 4 (Syntaxin 4-interacting protein) (STX4-interacting protein) (Synip) 557 61,689 Alternative sequence (7); Beta strand (7); Chain (1); Coiled coil (1); Domain (2); Helix (2); Modified residue (5); Mutagenesis (2) FUNCTION: Plays a role in the translocation of transport vesicles from the cytoplasm to the plasma membrane. Inhibits the translocation of SLC2A4 from intracellular vesicles to the plasma membrane by STX4A binding and preventing the interaction between STX4A and VAMP2. Stimulation with insulin disrupts the interaction with STX4A, leading to increased levels of SLC2A4 at the plasma membrane. May also play a role in the regulation of insulin release by pancreatic beta cells after stimulation by glucose. {ECO:0000269|PubMed:10394363, ECO:0000269|PubMed:12855681}. PTM: Phosphorylated on Ser-99 by PKB/AKT2 after insulin treatment. Phosphorylation on Ser-99 abolishes the interaction with STX4A. {ECO:0000269|PubMed:15753124}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10394363}. SUBUNIT: Interacts with STX4A. {ECO:0000269|PubMed:10394363}. TISSUE SPECIFICITY: Detected in skeletal muscle, heart, testis, adipocytes and pancreatic islet cells. {ECO:0000269|PubMed:10394363, ECO:0000269|PubMed:12855681}. +O88983 STX8_MOUSE Syntaxin-8 (Syntaxin-like protein 3I35) 236 26,925 Chain (1); Coiled coil (1); Domain (1); Modified residue (1); Topological domain (2); Transmembrane (1) TRANSMEM 216 232 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 1 215 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 233 236 Vesicular. {ECO:0000255}. FUNCTION: Vesicle trafficking protein that functions in the early secretory pathway, possibly by mediating retrograde transport from cis-Golgi membranes to the ER. {ECO:0000250}. PTM: Ubiquitinated by HECTD3. {ECO:0000269|PubMed:18821010}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Note=Preferentially associated with the early endosome. To a lesser extent, also present in late endosome, the plasma membrane and coated pits (By similarity). {ECO:0000250}. SUBUNIT: Forms a SNARE complex with STX7, VTI1B and VAMP8 which functions in the homotypic fusion of late endosomes. Part of the SNARE core complex containing STX7, VAMP8 and VTI1B. Interacts with VAMP8 (By similarity). Interacts with HECTD3. {ECO:0000250, ECO:0000269|PubMed:18821010}. +Q9QUQ5 TRPC4_MOUSE Short transient receptor potential channel 4 (TrpC4) (Capacitative calcium entry channel Trp4) (Receptor-activated cation channel TRP4) 974 111,575 Alternative sequence (1); Beta strand (9); Chain (1); Coiled coil (1); Helix (33); Modified residue (2); Region (4); Repeat (4); Sequence conflict (2); Topological domain (7); Transmembrane (6); Turn (8) TRANSMEM 330 350 Helical. {ECO:0000255}.; TRANSMEM 363 383 Helical. {ECO:0000255}.; TRANSMEM 437 457 Helical. {ECO:0000255}.; TRANSMEM 470 490 Helical. {ECO:0000255}.; TRANSMEM 512 532 Helical. {ECO:0000255}.; TRANSMEM 600 620 Helical. {ECO:0000255}. TOPO_DOM 1 329 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 351 362 Extracellular. {ECO:0000255}.; TOPO_DOM 384 436 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 458 469 Extracellular. {ECO:0000255}.; TOPO_DOM 491 511 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 533 599 Extracellular. {ECO:0000255}.; TOPO_DOM 621 974 Cytoplasmic. {ECO:0000255}. FUNCTION: Thought to form a receptor-activated non-selective calcium permeant cation channel. Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Acts as a cell-cell contact-dependent endothelial calcium entry channel. Has also been shown to be calcium-selective (By similarity). May also be activated by intracellular calcium store depletion. Trpc4 deficient mice lack a store-operated calcium entry in endothelial cells. {ECO:0000250, ECO:0000269|PubMed:11175743}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Homotetramer. Heterotetramer with TRPC1 and/or TRPC5 (By similarity). Isoform alpha but not isoform beta associates with inositol 1,4,5-trisphosphate receptor (ITPR) (By similarity). Interacts with NHERF. Interacts with MX1 and RNF24 (By similarity). Interacts (via CIRB domain) with SESTD1 (via the spectrin 1 repeat) and SPTBN5 (via C-terminus) (By similarity). Interacts with CDH5 and CTNNB1 (By similarity). Interacts (via protein 4.1-binding domain) with EPB41L2 (By similarity). Interacts with TRPC4AP. {ECO:0000250, ECO:0000269|PubMed:19070363, ECO:0000269|PubMed:20458742}. TISSUE SPECIFICITY: Abundantly expressed in brain (hippocampal CA1 pyramidal neurons, dentate gyrus granule cells, and cerebral cortical neurons, and in the septal nuclei and the mitral layer of olfactory bulb). Lower levels are detected in other tissues. +Q61143 TRPC6_MOUSE Short transient receptor potential channel 6 (TrpC6) (Calcium entry channel) (Transient receptor protein 6) (TRP-6) 930 106,681 Chain (1); Glycosylation (1); Modified residue (1); Repeat (4); Sequence conflict (8); Topological domain (7); Transmembrane (6) TRANSMEM 438 458 Helical. {ECO:0000255}.; TRANSMEM 487 507 Helical. {ECO:0000255}.; TRANSMEM 521 541 Helical. {ECO:0000255}.; TRANSMEM 592 612 Helical. {ECO:0000255}.; TRANSMEM 636 656 Helical. {ECO:0000255}.; TRANSMEM 706 726 Helical. {ECO:0000255}. TOPO_DOM 1 437 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 459 486 Extracellular. {ECO:0000255}.; TOPO_DOM 508 520 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 542 591 Extracellular. {ECO:0000255}.; TOPO_DOM 613 635 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 657 705 Extracellular. {ECO:0000255}.; TOPO_DOM 727 930 Cytoplasmic. {ECO:0000255}. FUNCTION: Thought to form a receptor-activated non-selective calcium permeant cation channel. Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Activated by diacylglycerol (DAG) in a membrane-delimited fashion, independently of protein kinase C. Seems not to be activated by intracellular calcium store depletion. {ECO:0000250|UniProtKB:Q9Y210}. PTM: Phosphorylated by FYN, leading to an increase of TRPC6 channel activity. {ECO:0000269|PubMed:14761972}.; PTM: N-glycosylated. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9Y210}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9Y210}. SUBUNIT: Homodimer; forms channel complex. Interacts with MX1 and RNF24. {ECO:0000250|UniProtKB:Q9Y210}. TISSUE SPECIFICITY: Lung and brain. +Q8VCI7 SWAP1_MOUSE ATPase SWSAP1 278 29,385 Chain (1); Erroneous initiation (1); Sequence conflict (1) FUNCTION: ATPase which is preferentially stimulated by single-stranded DNA and is involved in homologous recombination repair (HRR). Has a DNA-binding activity which is independent of its ATPase activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Interacts with ZSWIM7; they form a functional complex involved in homologous recombination repair and stabilize each other. Interacts with RAD51, RAD51B, RAD51C, RAD51D and XRCC3; involved in homologous recombination repair (By similarity). {ECO:0000250}. +Q80U70 SUZ12_MOUSE Polycomb protein Suz12 (Suppressor of zeste 12 protein homolog) 741 83,026 Chain (1); Compositional bias (2); Cross-link (6); Modified residue (4); Region (1); Sequence caution (1); Zinc finger (1) FUNCTION: Polycomb group (PcG) protein. Component of the PRC2/EED-EZH2 complex, which methylates 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene. The PRC2/EED-EZH2 complex may also serve as a recruiting platform for DNA methyltransferases, thereby linking two epigenetic repression systems (By similarity). Genes repressed by the PRC2/EED-EZH2 complex include HOXA7, HOXB6 and HOXC8. {ECO:0000250|UniProtKB:Q15022, ECO:0000269|PubMed:15385962, ECO:0000269|PubMed:15516932, ECO:0000269|PubMed:17339329}. PTM: Sumoylated, probably by PIAS2. {ECO:0000250|UniProtKB:Q15022}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16415857}. Chromosome {ECO:0000269|PubMed:16415857}. Note=Localizes to the inactive X chromosome in trophoblast stem cells. SUBUNIT: Interacts with histone H1 and PHF19 (By similarity). Interacts with CDYL (By similarity). Component of the PRC2/EED-EZH2 complex, which includes EED, EZH2, SUZ12, RBBP4 and RBBP7 and possibly AEBP2. The minimum components required for methyltransferase activity of the PRC2/EED-EZH2 complex are EED, EZH2 and SUZ12. Component of the PRC2/EED-EZH1 complex, which includes EED, EZH1, SUZ12, RBBP4 and AEBP2. The PRC2 complex may also interact with DNMT1, DNMT3A, DNMT3B and PHF1 via the EZH2 subunit and with SIRT1 via the SUZ12 subunit. Interacts with WDR77. Interacts with ARNTL/BMAL1. {ECO:0000250|UniProtKB:Q15022, ECO:0000269|PubMed:16712789, ECO:0000269|PubMed:19026780, ECO:0000269|PubMed:20144788, ECO:0000269|PubMed:23970558}. TISSUE SPECIFICITY: Expressed in embryonic stem cells. {ECO:0000269|PubMed:22226355}. +Q69ZS6 SV2C_MOUSE Synaptic vesicle glycoprotein 2C (Synaptic vesicle protein 2C) 727 82,291 Chain (1); Erroneous initiation (1); Glycosylation (5); Modified residue (4); Region (1); Topological domain (13); Transmembrane (12) TRANSMEM 155 175 Helical. {ECO:0000255}.; TRANSMEM 192 212 Helical. {ECO:0000255}.; TRANSMEM 227 247 Helical. {ECO:0000255}.; TRANSMEM 249 269 Helical. {ECO:0000255}.; TRANSMEM 281 301 Helical. {ECO:0000255}.; TRANSMEM 321 341 Helical. {ECO:0000255}.; TRANSMEM 438 458 Helical. {ECO:0000255}.; TRANSMEM 579 599 Helical. {ECO:0000255}.; TRANSMEM 610 630 Helical. {ECO:0000255}.; TRANSMEM 637 657 Helical. {ECO:0000255}.; TRANSMEM 671 693 Helical. {ECO:0000255}.; TRANSMEM 698 716 Helical. {ECO:0000255}. TOPO_DOM 1 154 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 176 191 Extracellular. {ECO:0000255}.; TOPO_DOM 213 226 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 248 248 Extracellular. {ECO:0000255}.; TOPO_DOM 270 280 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 302 320 Extracellular. {ECO:0000255}.; TOPO_DOM 342 437 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 459 578 Extracellular. {ECO:0000255, ECO:0000305|PubMed:16543415, ECO:0000305|PubMed:16545378}.; TOPO_DOM 600 609 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 631 636 Extracellular. {ECO:0000255}.; TOPO_DOM 658 670 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 694 697 Extracellular. {ECO:0000255}.; TOPO_DOM 717 727 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a role in the control of regulated secretion in neural and endocrine cells, enhancing selectively low-frequency neurotransmission. Positively regulates vesicle fusion by maintaining the readily releasable pool of secretory vesicles. {ECO:0000250|UniProtKB:Q9Z2I6}.; FUNCTION: (Microbial infection) Receptor for C.botulinum neurotoxin type A (BoNT/A, botA); the toxin binds Sv2c via extracellular loop 4 (PubMed:16543415). {ECO:0000269|PubMed:16543415, ECO:0000269|PubMed:16545378}.; FUNCTION: (Microbial infection) Possible receptor for C.botulinum neurotoxin type D (BoNT/D, botD) (PubMed:21483489). {ECO:0000269|PubMed:21483489}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9Z2I6}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q9Z2I6}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9Z2I6}. Note=Enriched in small synaptic vesicles and adrenal microsomes, not present in chromaffin granules. Associated with both insulin granules and synaptic-like microvesicles in insulin-secreting cells of the pancreas. {ECO:0000250|UniProtKB:Q9Z2I6}. SUBUNIT: Interacts with SYT1 in a calcium-dependent manner. {ECO:0000250|UniProtKB:Q9Z2I6}.; SUBUNIT: (Microbial infection) Interacts with C.botulinum neurotoxin type A (BoNT/A, botA). {ECO:0000269|PubMed:16545378, ECO:0000305|PubMed:16543415}.; SUBUNIT: (Microbial infection) Interacts with C.botulinum neurotoxin type D (BoNT/D, botD). {ECO:0000269|PubMed:21483489}. TISSUE SPECIFICITY: Expressed in specific subsets of conventional synapses in the retina (at protein level) (PubMed:12687700). Expressed in diaphragm motor nerve terminals (at protein level) (PubMed:16543415). Expressed in a subset of hippocampus neurons (at protein level) (PubMed:18815274, PubMed:21483489). {ECO:0000269|PubMed:12687700, ECO:0000269|PubMed:16543415, ECO:0000269|PubMed:18815274, ECO:0000269|PubMed:21483489}. +Q7TN37 TRPM4_MOUSE Transient receptor potential cation channel subfamily M member 4 (Calcium-activated non-selective cation channel 1) (Long transient receptor potential channel 4) (LTrpC-4) (LTrpC4) 1213 135,760 Alternative sequence (2); Beta strand (28); Binding site (3); Chain (1); Coiled coil (1); Disulfide bond (1); Helix (51); Intramembrane (1); Metal binding (4); Modified residue (4); Motif (1); Mutagenesis (5); Region (2); Sequence conflict (1); Topological domain (8); Transmembrane (6); Turn (6) INTRAMEM 960 980 Pore-forming. {ECO:0000269|PubMed:29211714}. TRANSMEM 779 799 Helical. {ECO:0000269|PubMed:29211714}.; TRANSMEM 811 831 Helical. {ECO:0000269|PubMed:29211714}.; TRANSMEM 860 880 Helical. {ECO:0000269|PubMed:29211714}.; TRANSMEM 883 906 Helical. {ECO:0000269|PubMed:29211714}.; TRANSMEM 927 947 Helical. {ECO:0000269|PubMed:29211714}.; TRANSMEM 1016 1036 Helical. {ECO:0000269|PubMed:29211714}. TOPO_DOM 1 778 Cytoplasmic. {ECO:0000269|PubMed:29211714}.; TOPO_DOM 800 810 Extracellular. {ECO:0000269|PubMed:29211714}.; TOPO_DOM 832 859 Cytoplasmic. {ECO:0000269|PubMed:29211714}.; TOPO_DOM 881 882 Extracellular. {ECO:0000269|PubMed:29211714}.; TOPO_DOM 907 926 Cytoplasmic. {ECO:0000269|PubMed:29211714}.; TOPO_DOM 948 959 Extracellular. {ECO:0000269|PubMed:29211714}.; TOPO_DOM 981 1015 Extracellular. {ECO:0000269|PubMed:29211714}.; TOPO_DOM 1037 1213 Cytoplasmic. {ECO:0000269|PubMed:29211714}. FUNCTION: Calcium-activated non selective (CAN) cation channel that mediates membrane depolarization. While it is activated by increase in intracellular Ca(2+), it is impermeable to it (PubMed:17188667, PubMed:29211714). Mediates transport of monovalent cations (Na(+) > K(+) > Cs(+) > Li(+)), leading to depolarize the membrane. It thereby plays a central role in cadiomyocytes, neurons from entorhinal cortex, dorsal root and vomeronasal neurons, endocrine pancreas cells, kidney epithelial cells, cochlea hair cells etc. Participates in T-cell activation by modulating Ca(2+) oscillations after T lymphocyte activation, which is required for NFAT-dependent IL2 production. Involved in myogenic constriction of cerebral arteries. Controls insulin secretion in pancreatic beta-cells. May also be involved in pacemaking or could cause irregular electrical activity under conditions of Ca(2+) overload. Affects T-helper 1 (Th1) and T-helper 2 (Th2) cell motility and cytokine production through differential regulation of calcium signaling and NFATC1 localization. Enhances cell proliferation through up-regulation of the beta-catenin signaling pathway (By similarity). Essential for the migration but not the maturation of dendritic cells (PubMed:18758465). {ECO:0000250|UniProtKB:Q8TD43, ECO:0000269|PubMed:17188667, ECO:0000269|PubMed:18758465, ECO:0000269|PubMed:29211714}. PTM: Phosphorylation by PKC leads to increase the sensitivity to Ca(2+). {ECO:0000250|UniProtKB:Q8TD43}.; PTM: Sumoylated. Desumoylated by SENP1. {ECO:0000250|UniProtKB:Q8TD43}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12893253, ECO:0000269|PubMed:29211714}; Multi-pass membrane protein {ECO:0000269|PubMed:29211714}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q8TD43}. Golgi apparatus {ECO:0000250|UniProtKB:Q8TD43}. SUBUNIT: Homotetramer. {ECO:0000269|PubMed:29211714}. TISSUE SPECIFICITY: Sino-atrial nodes (at protein level). Widely expressed. {ECO:0000269|PubMed:12799367, ECO:0000269|PubMed:12893253, ECO:0000269|PubMed:17188667}. +Q14CH7 SYAM_MOUSE Alanine--tRNA ligase, mitochondrial (EC 6.1.1.7) (Alanyl-tRNA synthetase) (AlaRS) 980 106,783 Binding site (6); Chain (1); Metal binding (4); Nucleotide binding (1); Sequence conflict (1); Transit peptide (1) FUNCTION: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain. {ECO:0000255|HAMAP-Rule:MF_03133}. SUBCELLULAR LOCATION: Mitochondrion. SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03133}. DOMAIN: Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs. {ECO:0000255|HAMAP-Rule:MF_03133}. +Q9DBX3 SUSD2_MOUSE Sushi domain-containing protein 2 820 90,641 Alternative sequence (2); Chain (1); Disulfide bond (9); Domain (4); Frameshift (1); Glycosylation (3); Helix (2); Sequence conflict (6); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 783 803 Helical. {ECO:0000255}. TOPO_DOM 23 782 Extracellular. {ECO:0000255}.; TOPO_DOM 804 820 Cytoplasmic. {ECO:0000255}. FUNCTION: May be a cytokine receptor for C10ORF99. May be a tumor suppressor; together with C10ORF99 has a growth inhibitory effect on colon cancer cells which includes G1 cell cycle arrest (By similarity). May play a role in breast tumorigenesis (PubMed:23131994). {ECO:0000250|UniProtKB:Q9UGT4, ECO:0000269|PubMed:23131994}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9UGT4}; Single-pass type I membrane protein {ECO:0000305}. +Q5DTW2 SMBT2_MOUSE Scm-like with four MBT domains protein 2 938 105,981 Alternative sequence (2); Chain (1); Domain (1); Erroneous initiation (1); Repeat (4) FUNCTION: Transcriptional repressor of HOXB13 gene. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with YY1. Interacts with methylated histones H3K9me2 and H4K20me2 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in testis and, at much lower levels, in ovary. {ECO:0000269|PubMed:18024232}. +Q8C1Q6 SMIM4_MOUSE Small integral membrane protein 4 (Small nucleolar RNA host gene 8) 80 9,746 Alternative sequence (3); Chain (1); Erroneous initiation (2); Transmembrane (1) TRANSMEM 20 41 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q04692 SMRCD_MOUSE SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD/H box 1 (EC 3.6.4.12) (ATP-dependent helicase SMARCAD1) (Enhancer trap locus homolog 1) (Etl-1) 1021 116,451 Alternative sequence (1); Chain (1); Cross-link (5); Domain (4); Erroneous initiation (2); Modified residue (15); Motif (3); Nucleotide binding (2); Sequence conflict (1) FUNCTION: DNA helicase that possesses intrinsic ATP-dependent nucleosome-remodeling activity and is both required for DNA repair and heterochromatin organization. Promotes DNA end resection of double-strand breaks (DSBs) following DNA damage: probably acts by weakening histone DNA interactions in nucleosomes flanking DSBs. Required for the restoration of heterochromatin organization after replication. Acts at replication sites to facilitate the maintenance of heterochromatin by directing H3 and H4 histones deacetylation, H3 'Lys-9' trimethylation (H3K9me3) and restoration of silencing (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18675275, ECO:0000269|PubMed:21549307, ECO:0000269|PubMed:8219362}. Chromosome {ECO:0000250}. Note=Colocalizes with PCNA at replication forks during S phase. Recruited to double-strand breaks (DSBs) sites of DNA damage (By similarity). {ECO:0000250}. SUBUNIT: Binds to DNA preferentially in the vicinity of transcriptional start sites. Interacts with MSH2 and TRIM28. Part of a complex composed of TRIM28, HDAC1, HDAC2 and EHMT2. Interacts with PCNA (By similarity). {ECO:0000250}. +Q9CUN6 SMUF1_MOUSE E3 ubiquitin-protein ligase SMURF1 (EC 2.3.2.26) (HECT-type E3 ubiquitin transferase SMURF1) (SMAD ubiquitination regulatory factor 1) (SMAD-specific E3 ubiquitin-protein ligase 1) 731 83,356 Active site (1); Chain (1); Compositional bias (1); Cross-link (2); Domain (4); Erroneous initiation (1); Modified residue (1); Sequence conflict (9) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that acts as a negative regulator of BMP signaling pathway (By similarity). Mediates ubiquitination and degradation of SMAD1 and SMAD5, 2 receptor-regulated SMADs specific for the BMP pathway (By similarity). Promotes ubiquitination and subsequent proteasomal degradation of TRAF family members and RHOA (By similarity). Promotes ubiquitination and subsequent proteasomal degradation of MAVS (PubMed:23087404). Plays a role in dendrite formation by melanocytes (By similarity). {ECO:0000250|UniProtKB:Q9HCE7, ECO:0000269|PubMed:23087404}. PTM: Auto-ubiquitinated in presence of NDFIP1. Ubiquitinated by the SCF(FBXL15) complex at Lys-355 and Lys-357, leading to its degradation by the proteasome. Lys-357 is the primary ubiquitination site. {ECO:0000250|UniProtKB:Q9HCE7}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. SUBUNIT: Interacts with TRAF4 (By similarity). Interacts (via HECT domain) with FBXL15 (via LRR repeats) (By similarity). Interacts with SMAD7 and TGFBR1; SMAD7 recruits SMURF1 to TGFBR1 and regulates TGF-beta receptor degradation (By similarity). Interacts with MAVS; the interaction is mediated by NDFIP1 (PubMed:23087404). {ECO:0000250|UniProtKB:Q9HCE7, ECO:0000269|PubMed:23087404}. DOMAIN: The C2 domain mediates membrane localization and substrate selection. {ECO:0000250}. +Q8R5A0 SMYD2_MOUSE N-lysine methyltransferase SMYD2 (EC 2.1.1.-) (Histone methyltransferase SMYD2) (EC 2.1.1.43) (SET and MYND domain-containing protein 2) 433 49,567 Beta strand (11); Binding site (2); Chain (1); Domain (1); Helix (20); Modified residue (1); Mutagenesis (1); Region (4); Sequence caution (1); Turn (7); Zinc finger (1) FUNCTION: Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. Specifically methylates histone H3 'Lys-4' (H3K4me) and dimethylates histone H3 'Lys-36' (H3K36me2). Shows even higher methyltransferase activity on p53/TP53. Monomethylates 'Lys-370' of p53/TP53, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity of p53/TP53. Monomethylates RB1 at 'Lys-860'. {ECO:0000269|PubMed:16805913}. SUBCELLULAR LOCATION: Cytoplasm, cytosol. Nucleus. SUBUNIT: Interacts (via MYND-type zinc finger) with EPB41L3. Interacts (via SET domain) with p53/TP53. Interacts with RB1 and HSP90AA1 (By similarity). Interacts with RNA polymerase II and HELZ. Interacts with SIN3A and HDAC1. {ECO:0000250, ECO:0000269|PubMed:16805913, ECO:0000269|PubMed:20305823}. TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle and brain tissue. During cardiac development, it is differentially expressed with highest expression in the neonatal heart while very low expression is detected at E12.5 and adult. Specifically expressed in cardiomyocytes (at protein level). {ECO:0000269|PubMed:20305823}. +Q6PHS6 SNX13_MOUSE Sorting nexin-13 957 110,819 Binding site (4); Chain (1); Domain (3) FUNCTION: May be involved in several stages of intracellular trafficking. Acts as a GAP for Galphas (By similarity). May play a role in endosome homeostasis. {ECO:0000250, ECO:0000269|PubMed:17077144}. SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. DOMAIN: The PX domain mediates interaction with membranes enriched in phosphatidylinositol 3-phosphate. {ECO:0000250}. +Q6P8Y7 SNX31_MOUSE Sorting nexin-31 439 50,862 Alternative sequence (1); Chain (1); Domain (1); Sequence conflict (1) FUNCTION: May be involved in protein trafficking. {ECO:0000250}. +O54928 SOCS5_MOUSE Suppressor of cytokine signaling 5 (SOCS-5) (Cytokine-inducible SH2-containing protein 5) 536 61,086 Chain (1); Domain (2); Helix (1); Region (1); Sequence conflict (1) Protein modification; protein ubiquitination. FUNCTION: SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. May be a substrate-recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Inhibits for instance EGF signaling by mediating the degradation of the EGF receptor/EGFR. Involved in the regulation of T-helper cell differentiation by inhibiting of the IL4 signaling pathway which promotes differentiation into the Th2 phenotype. Can also partially inhibit IL6 and LIF signaling. {ECO:0000269|PubMed:12242343}. PTM: Phosphorylated. Phosphorylation is induced by EGF (By similarity). {ECO:0000250}. SUBUNIT: Interacts with EGFR. Interacts with ELOB and ELOC; mediates EGFR ubiquitination and degradation (By similarity). Interacts with IL4R; inhibits IL4 signaling. {ECO:0000250, ECO:0000269|PubMed:12242343}. DOMAIN: The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin ligase complexes. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. Expressed in TH1 but not TH2 cells. {ECO:0000269|PubMed:12242343}. +O09164 SODE_MOUSE Extracellular superoxide dismutase [Cu-Zn] (EC-SOD) (EC 1.15.1.1) 251 27,392 Chain (1); Disulfide bond (2); Glycosylation (1); Metal binding (8); Propeptide (1); Signal peptide (1) FUNCTION: Protect the extracellular space from toxic effect of reactive oxygen intermediates by converting superoxide radicals into hydrogen peroxide and oxygen. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space. +Q91YY5 SO1A5_MOUSE Solute carrier organic anion transporter family member 1A5 (Organic anion-transporting polypeptide 3) (OATP-3) (Sodium-independent organic anion transporter 3) (Solute carrier family 21 member 7) 670 74,663 Chain (1); Disulfide bond (3); Domain (1); Glycosylation (4); Sequence conflict (4); Topological domain (13); Transmembrane (12) TRANSMEM 21 40 Helical; Name=1. {ECO:0000255}.; TRANSMEM 60 80 Helical; Name=2. {ECO:0000255}.; TRANSMEM 87 111 Helical; Name=3. {ECO:0000255}.; TRANSMEM 156 184 Helical; Name=4. {ECO:0000255}.; TRANSMEM 204 224 Helical; Name=5. {ECO:0000255}.; TRANSMEM 243 267 Helical; Name=6. {ECO:0000255}.; TRANSMEM 312 333 Helical; Name=7. {ECO:0000255}.; TRANSMEM 354 377 Helical; Name=8. {ECO:0000255}.; TRANSMEM 382 405 Helical; Name=9. {ECO:0000255}.; TRANSMEM 514 536 Helical; Name=10. {ECO:0000255}.; TRANSMEM 546 571 Helical; Name=11. {ECO:0000255}.; TRANSMEM 606 623 Helical; Name=12. {ECO:0000255}. TOPO_DOM 1 20 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 41 59 Extracellular. {ECO:0000255}.; TOPO_DOM 81 86 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 112 155 Extracellular. {ECO:0000255}.; TOPO_DOM 185 203 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 225 242 Extracellular. {ECO:0000255}.; TOPO_DOM 268 311 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 334 353 Extracellular. {ECO:0000255}.; TOPO_DOM 378 381 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 406 513 Extracellular. {ECO:0000255}.; TOPO_DOM 537 545 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 572 605 Extracellular. {ECO:0000255}.; TOPO_DOM 624 670 Cytoplasmic. {ECO:0000255}. FUNCTION: Mediates the Na(+)-independent transport of organic anions such as taurocholate and thyroid hormones. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q9D2Y5 SNX20_MOUSE Sorting nexin-20 313 36,028 Binding site (4); Chain (1); Domain (1); Modified residue (1); Mutagenesis (1); Sequence conflict (5) FUNCTION: May play a role in cellular vesicle trafficking (PubMed:25882846). Has been proposed to function as a sorting protein that targets SELPLG into endosomes, but has no effect on SELPLG internalization from the cell surface, nor on SELPLG-mediated cell-cell adhesion (PubMed:18196517). {ECO:0000269|PubMed:18196517, ECO:0000305|PubMed:25882846}. SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000269|PubMed:25882846}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q7Z614}; Cytoplasmic side {ECO:0000250|UniProtKB:Q7Z614}. Cell membrane {ECO:0000250|UniProtKB:Q7Z614}. Cytoplasm {ECO:0000250|UniProtKB:Q7Z614}. Nucleus {ECO:0000250|UniProtKB:Q7Z614}. SUBUNIT: Interacts with SELPLG (By similarity). Interaction with SELPLG is controversial and was not detected in PubMed:25882846. {ECO:0000250|UniProtKB:Q7Z614, ECO:0000269|PubMed:25882846}. DOMAIN: The PX domain binds phosphatidylinositol 3-phosphate which is necessary for localization to the endosomes. {ECO:0000269|PubMed:25882846}. +Q7TQA9 TR135_MOUSE Taste receptor type 2 member 135 (T2R135) (Taste receptor type 2 member 35) (T2R35) (mT2r38) 312 35,591 Chain (1); Erroneous gene model prediction (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 20 40 Helical; Name=1. {ECO:0000255}.; TRANSMEM 67 87 Helical; Name=2. {ECO:0000255}.; TRANSMEM 98 118 Helical; Name=3. {ECO:0000255}.; TRANSMEM 141 161 Helical; Name=4. {ECO:0000255}.; TRANSMEM 199 219 Helical; Name=5. {ECO:0000255}.; TRANSMEM 245 265 Helical; Name=6. {ECO:0000255}.; TRANSMEM 278 298 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 19 Extracellular. {ECO:0000255}.; TOPO_DOM 41 66 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 88 97 Extracellular. {ECO:0000255}.; TOPO_DOM 119 140 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 162 198 Extracellular. {ECO:0000255}.; TOPO_DOM 220 244 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 266 277 Extracellular. {ECO:0000255}.; TOPO_DOM 299 312 Cytoplasmic. {ECO:0000255}. FUNCTION: Putative taste receptor which may play a role in the perception of bitterness. {ECO:0000303|PubMed:12734386}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. +Q3ZT31 SNX25_MOUSE Sorting nexin-25 840 97,146 Chain (1); Coiled coil (1); Domain (3); Modified residue (1); Sequence caution (1); Sequence conflict (12) FUNCTION: May be involved in several stages of intracellular trafficking. {ECO:0000250}. SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. +Q7TQB9 TR143_MOUSE Taste receptor type 2 member 143 (T2R143) (Taste receptor type 2 member 43) (T2R43) (mT2R36) 293 34,045 Chain (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 7 27 Helical; Name=1. {ECO:0000255}.; TRANSMEM 56 76 Helical; Name=2. {ECO:0000255}.; TRANSMEM 80 100 Helical; Name=3. {ECO:0000255}.; TRANSMEM 128 148 Helical; Name=4. {ECO:0000255}.; TRANSMEM 182 202 Helical; Name=5. {ECO:0000255}.; TRANSMEM 228 248 Helical; Name=6. {ECO:0000255}.; TRANSMEM 265 285 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 6 Extracellular. {ECO:0000255}.; TOPO_DOM 28 55 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 77 79 Extracellular. {ECO:0000255}.; TOPO_DOM 101 127 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 149 181 Extracellular. {ECO:0000255}.; TOPO_DOM 203 227 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 249 264 Extracellular. {ECO:0000255}.; TOPO_DOM 286 293 Cytoplasmic. {ECO:0000255}. FUNCTION: Putative taste receptor which may play a role in the perception of bitterness. {ECO:0000303|PubMed:12734386}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. +Q8VI51 SORC3_MOUSE VPS10 domain-containing receptor SorCS3 1219 135,985 Chain (1); Domain (1); Glycosylation (7); Repeat (6); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1123 1143 Helical. {ECO:0000255}. TOPO_DOM 34 1122 Lumenal. {ECO:0000255}.; TOPO_DOM 1144 1219 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. +Q569Z6 TR150_MOUSE Thyroid hormone receptor-associated protein 3 (Thyroid hormone receptor-associated protein complex 150 kDa component) (Trap150) 951 108,178 Chain (1); Compositional bias (2); Cross-link (36); Initiator methionine (1); Modified residue (49); Nucleotide binding (1); Region (2) FUNCTION: Involved in pre-mRNA splicing. Remains associated with spliced mRNA after splicing which probably involves interactions with the exon junction complex (EJC). Can trigger mRNA decay which seems to be independent of nonsense-mediated decay involving premature stop codons (PTC) recognition. May be involved in nuclear mRNA decay. Involved in regulation of signal-induced alternative splicing. During splicing of PTPRC/CD45 is proposed to sequester phosphorylated SFPQ from PTPRC/CD45 pre-mRNA in resting T-cells. Involved in cyclin-D1/CCND1 mRNA stability probably by acting as component of the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. Involved in response to DNA damage. Is excluced from DNA damage sites in a manner that parallels transcription inhibition; the function may involve the SNARP complex. Initially thought to play a role in transcriptional coactivation through its association with the TRAP complex; however, it is not regarded as a stable Mediator complex subunit. Cooperatively with HELZ2, enhances the transcriptional activation mediated by PPARG, maybe through the stabilization of the PPARG binding to DNA in presence of ligand. May play a role in the terminal stage of adipocyte differentiation. Plays a role in the positive regulation of the circadian clock. Acts as a coactivator of the CLOCK-ARNTL/BMAL1 heterodimer and promotes its transcriptional activator activity and binding to circadian target genes (PubMed:24043798). {ECO:0000269|PubMed:23525231, ECO:0000269|PubMed:24043798}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23525231}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9Y2W1}. Nucleus speckle {ECO:0000250|UniProtKB:Q9Y2W1}. SUBUNIT: Associated with the large multiprotein complex TRAP (Mediator complex-like). Interacts with SFPQ; the interaction is dependent on SFPQ phosphorylation at 'Thr-687' and inhibits binding of SFPQ to an ESS1 exonic splicing silencer element-containing RNA. Interacts with NXF1. Component of the SNARP complex which consists at least of SNIP1, SNW1, THRAP3, BCLAF1 and PNN. Associated with spliced mRNP complexes. Interacts with HELZ2 and PPARG. Interacts with CLOCK and ARNTL/BMAL1 (By similarity). Component of a MACOM-like complex, named WTAP complex, composed of WTAP, ZC3H13, CBLL1, KIAA1429, RBM15, BCLAF1 and THRAP3 (By similarity). {ECO:0000250|UniProtKB:Q9Y2W1}. +Q7M6Y2 SOX11_MOUSE Transcription factor SOX-11 395 42,629 Chain (1); Compositional bias (2); DNA binding (1); Sequence conflict (8) FUNCTION: Transcriptional factor involved in the embryonic neurogenesis. May also have a role in tissue modeling during development. {ECO:0000250|UniProtKB:P35716}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267, ECO:0000269|PubMed:15456859}. TISSUE SPECIFICITY: Expression prominent in the periventricular cells of the central nervous system, also observed in a wide range of tissues involved in epithelial-mesenchymal interactions. +Q9CQN4 SOSD1_MOUSE Sclerostin domain-containing protein 1 (Ectodermal BMP inhibitor) (Ectodin) (Sclerostin-like protein) (Uterine sensitization-associated gene 1 protein) (USAG-1) 206 23,174 Chain (1); Disulfide bond (4); Domain (1); Glycosylation (2); Sequence conflict (2); Signal peptide (1) FUNCTION: May be involved in the onset of endometrial receptivity for implantation/sensitization for the decidual cell reaction. Enhances Wnt signaling and inhibits TGF-beta signaling (By similarity). Directly antagonizes activity of BMP2, BMP4, BMP6 and BMP7 in a dose-dependent manner. {ECO:0000250, ECO:0000269|PubMed:14623234}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14623234}. SUBUNIT: Interacts with BMP2, BMP4, BMP6 and BMP7 with high affinity. {ECO:0000269|PubMed:14623234}. TISSUE SPECIFICITY: Highly expressed in kidney at renal collecting ducts level and weakly in brain. {ECO:0000269|PubMed:14623234, ECO:0000269|PubMed:15020244}. +O35892 SP100_MOUSE Nuclear autoantigen Sp-100 (Nuclear dot-associated Sp100 protein) (Speckled 100 kDa) 482 54,727 Alternative sequence (1); Chain (1); Cross-link (1); Domain (2); Modified residue (8); Motif (1); Sequence conflict (9) FUNCTION: Together with PML, this tumor suppressor is a major constituent of the PML bodies, a subnuclear organelle involved in a large number of physiological processes including cell growth, differentiation and apoptosis. Functions as a transcriptional coactivator of ETS1 and ETS2. Under certain conditions, it may also act as a corepressor of ETS1 preventing its binding to DNA. Through the regulation of ETS1 it may play a role in angiogenesis, controlling endothelial cell motility and invasion. Through interaction with the MRN complex it may be involved in the regulation of telomeres lengthening. May also regulate TP53-mediated transcription and through CASP8AP2, regulate FAS-mediated apoptosis. May also play a role in infection by viruses through mechanisms that may involve chromatin and/or transcriptional regulation (By similarity). {ECO:0000250}. PTM: Sumoylated. Sumoylated with SUMO1. Sumoylation depends on a functional nuclear localization signal but is not necessary for nuclear import or nuclear body targeting. Sumoylation may stabilize the interaction with CBX5 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00185, ECO:0000255|PROSITE-ProRule:PRU00747}. Nucleus, PML body {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Accumulates in the cytoplasm upon FAS activation. {ECO:0000250}. SUBUNIT: Homodimer. Interacts with members of the HP1 family of nonhistone chromosomal protein, such as CBX5 and CBX3 via the PxVxL motif. Interacts with ETS1; the interaction is direct and modulates ETS1 transcriptional activity. Interacts with the MRN complex which is composed of two heterodimers RAD50/MRE11 associated with a single NBN; recruits the complex to PML-related bodies. Interacts with HIPK2; positively regulates TP53-dependent transcription. Interacts with CASP8AP2; may negatively regulate CASP8AP2 export from the nucleus to the cytoplasm (By similarity). {ECO:0000250}. DOMAIN: The HSR domain is important for the nuclear body targeting as well as for the dimerization. {ECO:0000250}.; DOMAIN: Contains one Pro-Xaa-Val-Xaa-Leu (PxVxL) motif, which is required for interaction with chromoshadow domains. This motif requires additional residues -7, -6, +4 and +5 of the central Val which contact the chromoshadow domain. +P43680 SOX18_MOUSE Transcription factor SOX-18 377 40,898 Chain (1); DNA binding (1); Domain (1); Helix (3); Sequence conflict (2) FUNCTION: Binds to the consensus sequence 5'-AACAAAG-3' and is able to trans-activate transcription via this site. SUBCELLULAR LOCATION: Nucleus. TISSUE SPECIFICITY: Expressed only in lung, heart and skeletal muscles. +Q62249 SOX19_MOUSE Protein SOX-19 (Fragment) 55 6,862 Chain (1); DNA binding (1); Non-terminal residue (2) SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}. +Q3UZZ6 ST1D1_MOUSE Sulfotransferase 1 family member D1 (ST1D1) (EC 2.8.2.-) (Amine N-sulfotransferase) (SULT-N) (Dopamine sulfotransferase Sult1d1) (Tyrosine-ester sulfotransferase) 295 35,083 Active site (1); Beta strand (6); Binding site (5); Chain (1); Frameshift (1); Helix (17); Mutagenesis (2); Nucleotide binding (3); Region (1); Sequence conflict (3); Turn (6) FUNCTION: Sulfotransferase with broad substrate specificity that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of catecholamines, such as dopamine, prostaglandins, leukotriene E4, drugs and xenobiotic compounds. Has sulfotransferase activity towards p-nitrophenol, 2-naphthylamine and minoxidil (in vitro). Sulfonation increases the water solubility of most compounds, and therefore their renal excretion, but it can also result in bioactivation to form active metabolites. {ECO:0000269|PubMed:15087475, ECO:0000269|PubMed:18977225, ECO:0000269|PubMed:19966186, ECO:0000269|PubMed:9647753, ECO:0000269|PubMed:9920733}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19966186}. TISSUE SPECIFICITY: Detected in kidney and liver. Detected in kidney collecting duct cells. {ECO:0000269|PubMed:19966186, ECO:0000269|PubMed:9647753}. +P49891 ST1E1_MOUSE Estrogen sulfotransferase, testis isoform (EC 2.8.2.4) (Sulfotransferase 1E1) (ST1E1) (Sulfotransferase, estrogen-preferring) 295 35,590 Active site (1); Beta strand (6); Binding site (3); Chain (1); Helix (17); Modified residue (1); Mutagenesis (6); Nucleotide binding (3); Region (1); Sequence conflict (1); Turn (6) FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of estradiol and estrone. May play a role in the regulation of estrogen receptor activity by metabolizing free estradiol. {ECO:0000269|PubMed:9765259}. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Testis and at very low level in the placenta. +Q8K4P7 ST7L_MOUSE Suppressor of tumorigenicity 7 protein-like (ST7-related protein) 559 63,368 Alternative sequence (2); Chain (1); Transmembrane (3) TRANSMEM 39 59 Helical. {ECO:0000255}.; TRANSMEM 83 103 Helical. {ECO:0000255}.; TRANSMEM 513 533 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:12060862}. +B7ZNG4 TROAP_MOUSE Tastin (Troap protein) (Trophinin-assisting protein) (Trophinin-associated protein) 668 71,959 Chain (1); Erroneous initiation (1); Modified residue (6); Sequence conflict (2) FUNCTION: Could be involved with bystin and trophinin in a cell adhesion molecule complex that mediates an initial attachment of the blastocyst to uterine epithelial cells at the time of the embryo implantation. {ECO:0000250|UniProtKB:Q12815}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q12815}. SUBUNIT: Directly binds bystin, and indirectly trophinin. {ECO:0000250|UniProtKB:Q12815}. +P42230 STA5A_MOUSE Signal transducer and activator of transcription 5A (Mammary gland factor) 793 90,831 Beta strand (17); Chain (1); Domain (1); Helix (18); Modified residue (5); Turn (6) FUNCTION: Carries out a dual function: signal transduction and activation of transcription. Mediates cellular responses to the cytokine KITLG/SCF and other growth factors. May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4. Binds to the GAS element and activates PRL-induced transcription. Regulates the expression of milk proteins during lactation. {ECO:0000269|PubMed:10508857, ECO:0000269|PubMed:16837552, ECO:0000269|PubMed:7720707}. PTM: ISGylated. {ECO:0000269|PubMed:22022510}.; PTM: Tyrosine phosphorylated in response to KITLG/SCF, IL2, IL3, IL7, IL15, CSF2/GMCSF, GH1, PRL, EPO and THPO (PubMed:16837552). Activated KIT promotes phosphorylation on tyrosine residues and subsequent translocation to the nucleus (PubMed:21135090). Tyrosine phosphorylated in response to constitutively activated FGFR1, FGFR2, FGFR3 and FGFR4 (By similarity). Tyrosine phosphorylation is required for DNA-binding activity and dimerization (PubMed:7720707). Serine phosphorylation is also required for maximal transcriptional activity (By similarity). Tyrosine phosphorylated in response to signaling via activated FLT3; wild-type FLT3 results in much weaker phosphorylation than constitutively activated mutant FLT3 (PubMed:11090077, PubMed:21262971). Alternatively, can be phosphorylated by JAK2 at Tyr-694 (By similarity). {ECO:0000250|UniProtKB:P40763, ECO:0000250|UniProtKB:P42229, ECO:0000250|UniProtKB:Q62771, ECO:0000269|PubMed:11090077, ECO:0000269|PubMed:16837552, ECO:0000269|PubMed:21135090, ECO:0000269|PubMed:21262971, ECO:0000269|PubMed:7720707}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16837552}. Nucleus {ECO:0000269|PubMed:16837552}. Note=Translocated into the nucleus in response to phosphorylation. SUBUNIT: Forms a homodimer or a heterodimer with a related family member. Interacts with NCOA1 and SOCS7 (By similarity). Binds NR3C1. Interacts with ERBB4. {ECO:0000250, ECO:0000269|PubMed:10508857, ECO:0000269|PubMed:16837552, ECO:0000269|PubMed:9528750}. TISSUE SPECIFICITY: In the virgin, found in most tissues except brain and muscle. During lactation, abundantly found in mammary tissue, as well as in other secretory organs such as salivary gland and seminal vesicle. +Q923Q2 STA13_MOUSE StAR-related lipid transfer protein 13 (START domain-containing protein 13) (StARD13) 1113 125,060 Chain (1); Domain (3); Modified residue (2); Sequence conflict (2) FUNCTION: May function as a GTPase-activating protein. SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein; Cytoplasmic side. Mitochondrion membrane; Peripheral membrane protein; Cytoplasmic side. Lipid droplet {ECO:0000250}. SUBUNIT: Homodimer. Interacts with TAX1BP1 (By similarity). {ECO:0000250}. +Q9CQ26 STABP_MOUSE STAM-binding protein (EC 3.4.19.-) (Associated molecule with the SH3 domain of STAM) 424 48,514 Chain (1); Compositional bias (1); Domain (1); Metal binding (7); Modified residue (3); Motif (1); Region (2); Site (1) FUNCTION: Zinc metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Does not cleave 'Lys-48'-linked polyubiquitin chains (By similarity). Plays a role in signal transduction for cell growth and MYC induction mediated by IL-2 and GM-CSF. Potentiates BMP (bone morphogenetic protein) signaling by antagonizing the inhibitory action of SMAD6 and SMAD7 (By similarity). Involved in the ubiquitin-dependent sorting and trafficking of receptors from endosomes to lysosome. Endosomal localization of STAMBP is required for efficient EGFR degradation but not for its internalization. Involved in the negative regulation of PI3K-AKT-mTOR and RAS-MAP signaling pathways (By similarity). {ECO:0000250}. PTM: Phosphorylated after BMP type I receptor activation. {ECO:0000250}.; PTM: Ubiquitinated by SMURF2 in the presence of RNF11. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Endosome {ECO:0000250}. SUBUNIT: Interacts with STAM. Interacts with SMAD6 and SMAD7. Interacts with CHMP3; the interaction appears to relieve the autoinhibition of CHMP3 (By similarity). Interacts with SMURF2 and RNF11; this interaction promotes ubiquitination (By similarity). {ECO:0000250|UniProtKB:O95630}. DOMAIN: The JAMM motif is essential for the protease activity. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain. {ECO:0000269|PubMed:11713295}. +O35638 STAG2_MOUSE Cohesin subunit SA-2 (SCC3 homolog 2) (Stromal antigen 2) 1231 141,281 Chain (1); Compositional bias (1); Domain (1); Frameshift (3); Modified residue (9); Sequence conflict (6) FUNCTION: Component of cohesin complex, a complex required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis (By similarity). {ECO:0000250}. PTM: Phosphorylated by PLK1. The large dissociation of cohesin from chromosome arms during prophase is partly due to its phosphorylation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Chromosome {ECO:0000250}. Chromosome, centromere {ECO:0000250}. Note=Associates with chromatin. Before prophase it is scattered along chromosome arms. During prophase, most of cohesin complexes dissociate from chromatin probably because of phosphorylation by PLK1, except at centromeres, where cohesin complexes remain. At anaphase, the RAD21 subunit of cohesin is cleaved, leading to the dissociation of the complex from chromosomes, allowing chromosome separation. In germ cells, cohesin complex dissociates from chromatin at prophase I, and may be replaced by a meiosis-specific cohesin complex (By similarity). {ECO:0000250}. SUBUNIT: Interacts directly with RAD21 in cohesin complex. Cohesin complexes are composed of a heterodimer between a SMC1 protein (SMC1A or SMC1B) and SMC3, which are attached via their hinge domain, and RAD21 which link them at their heads, and one STAG protein (STAG1, STAG2 or STAG3). In cohesin complexes, STAG2 is mutually exclusive with STAG1 and STAG3 (By similarity). {ECO:0000250}. +Q80TF6 STAR9_MOUSE StAR-related lipid transfer protein 9 (Kinesin-like protein Kif16a) (START domain-containing protein 9) (StARD9) 4561 500,243 Chain (1); Coiled coil (2); Compositional bias (2); Domain (3); Modified residue (1); Nucleotide binding (1); Sequence conflict (37) FUNCTION: Microtubule-dependent motor protein required for spindle pole assembly during mitosis. Required to stabilize the pericentriolar material (PCM) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250}. Nucleus {ECO:0000250}. Note=Localizes throughout the cytoplasm and nucleus during interphase. Localizes to the daughter centriole during mitosis. Disappears in cytokinesis (By similarity). {ECO:0000250}. SUBUNIT: Interacts with ATAD3A. {ECO:0000250}. +Q9JM90 STAP1_MOUSE Signal-transducing adaptor protein 1 (STAP-1) (Stem cell adaptor protein 1) 297 34,628 Alternative sequence (2); Chain (1); Domain (2); Modified residue (1) FUNCTION: May function as an adapter molecule downstream of KIT in the proliferation or differentiation of hematopoietic stem cells. {ECO:0000269|PubMed:10679268}. PTM: Phosphorylated on tyrosine by TEC. Phosphorylated on tyrosine by KIT. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000305}. Mitochondrion {ECO:0000250}. SUBUNIT: Interacts with URI1; the interaction is phosphorylation-dependent occurs in a growth-dependent manner (By similarity). Interacts with KIT and CSF1R. {ECO:0000250, ECO:0000269|PubMed:10679268}. TISSUE SPECIFICITY: Expression restricted to the bone marrow. {ECO:0000269|PubMed:10679268}. +Q61542 STAR3_MOUSE StAR-related lipid transfer protein 3 (Protein ES 64) (Protein MLN 64) (START domain-containing protein 3) (StARD3) 446 50,470 Chain (1); Domain (2); Modified residue (3); Motif (1); Topological domain (5); Transmembrane (4) TRANSMEM 53 73 Helical. {ECO:0000255|PROSITE-ProRule:PRU00770}.; TRANSMEM 96 116 Helical. {ECO:0000255|PROSITE-ProRule:PRU00770}.; TRANSMEM 122 142 Helical. {ECO:0000255|PROSITE-ProRule:PRU00770}.; TRANSMEM 150 170 Helical. {ECO:0000255|PROSITE-ProRule:PRU00770}. TOPO_DOM 1 52 Cytoplasmic. {ECO:0000250|UniProtKB:Q14849}.; TOPO_DOM 74 95 Extracellular. {ECO:0000255}.; TOPO_DOM 117 121 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 143 149 Extracellular. {ECO:0000255}.; TOPO_DOM 171 446 Cytoplasmic. {ECO:0000250|UniProtKB:Q14849}. FUNCTION: Sterol-binding protein that mediates cholesterol transport from the endoplasmic reticulum to endosomes (By similarity). Creates contact site between the endoplasmic reticulum and late endosomes: localizes to late endosome membranes and contacts the endoplasmic reticulum via interaction with VAPA and VAPB (By similarity). Acts as a lipid transfer protein that redirects sterol to the endosome at the expense of the cell membrane and favors membrane formation inside endosomes (By similarity). May also mediate cholesterol transport between other membranes, such as mitochondria membrane or cell membrane (By similarity). However, such results need additional experimental evidences; probably mainly mediates cholesterol transport from the endoplasmic reticulum to endosomes (By similarity). Does not activate transcriptional cholesterol sensing (By similarity). {ECO:0000250|UniProtKB:F7B909, ECO:0000250|UniProtKB:Q14849}. SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250|UniProtKB:Q14849}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to contact sites between the endoplasmic reticulum and late endosomes: associates with the endoplasmic reticulum membrane via interaction with VAPA and VAPB. {ECO:0000250|UniProtKB:Q14849}. SUBUNIT: Homodimer. Interacts (via the MENTAL domain) with STARD3NL. Interacts (via FFAT motif) with VAPA. Interacts (via FFAT motif) with VAPB. {ECO:0000250|UniProtKB:Q14849}. DOMAIN: The FFAT motif mediates interaction with VAPA and VAPB. {ECO:0000250|UniProtKB:Q14849}.; DOMAIN: The START domain mediates lipid-transfer between membranes. It contains a hydrophobic cavity able to accommodate one lipid molecule, thereby serving as a 'hydrophobic bridge' across the aqueous gap between donor and acceptor organelle membranes. {ECO:0000250|UniProtKB:Q14849}.; DOMAIN: The MENTAL domain anchors the protein in endosome membranes and exposes the START domain in the cytosol. It binds cholesterol and mediates homotypic as well as heterotypic interactions between STARD3 and STARD3NL. {ECO:0000250|UniProtKB:Q14849}. +Q9CWR7 STEA1_MOUSE Metalloreductase STEAP1 (EC 1.16.1.-) (Six-transmembrane epithelial antigen of prostate 1) 339 39,292 Binding site (4); Chain (1); Domain (1); Metal binding (2); Modified residue (1); Sequence conflict (1); Transmembrane (6) TRANSMEM 79 99 Helical. {ECO:0000255}.; TRANSMEM 109 129 Helical. {ECO:0000255}.; TRANSMEM 164 184 Helical. {ECO:0000255}.; TRANSMEM 218 238 Helical. {ECO:0000255}.; TRANSMEM 258 278 Helical. {ECO:0000255}.; TRANSMEM 283 303 Helical. {ECO:0000255}. FUNCTION: Metalloreductase that has the ability to reduce both Fe(3+) to Fe(2+) and Cu(2+) to Cu(1+). Uses NAD(+) as acceptor. {ECO:0000269|PubMed:16609065}. SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:16609065}; Multi-pass membrane protein {ECO:0000269|PubMed:16609065}. +Q8BWB6 STEA2_MOUSE Metalloreductase STEAP2 (EC 1.16.1.-) (Six-transmembrane epithelial antigen of prostate 2) 489 55,760 Binding site (8); Chain (1); Domain (1); Metal binding (2); Modified residue (1); Nucleotide binding (3); Transmembrane (6) TRANSMEM 207 227 Helical. {ECO:0000255}.; TRANSMEM 258 278 Helical. {ECO:0000255}.; TRANSMEM 304 324 Helical. {ECO:0000255}.; TRANSMEM 358 378 Helical. {ECO:0000255}.; TRANSMEM 392 412 Helical. {ECO:0000255}.; TRANSMEM 431 451 Helical. {ECO:0000255}. FUNCTION: Metalloreductase that has the ability to reduce both Fe(3+) to Fe(2+) and Cu(2+) to Cu(1+). Uses NAD(+) as acceptor. {ECO:0000269|PubMed:16609065}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endosome membrane {ECO:0000269|PubMed:16609065}; Multi-pass membrane protein {ECO:0000269|PubMed:16609065}. +P33242 STF1_MOUSE Steroidogenic factor 1 (SF-1) (STF-1) (Adrenal 4-binding protein) (Embryonal LTR-binding protein) (ELP) (Embryonal long terminal repeat-binding protein) (Fushi tarazu factor homolog 1) (Nuclear receptor subfamily 5 group A member 1) (Steroid hormone receptor Ad4BP) (Steroid hydroxylase positive regulator) 462 52,077 Alternative sequence (1); Beta strand (7); Binding site (3); Chain (1); Cross-link (2); DNA binding (1); Domain (1); Erroneous initiation (1); Helix (17); Modified residue (4); Mutagenesis (11); Natural variant (1); Sequence conflict (3); Turn (4); Zinc finger (2) FUNCTION: Transcriptional activator. Seems to be essential for sexual differentiation and formation of the primary steroidogenic tissues. Binds to the Ad4 site found in the promoter region of steroidogenic P450 genes such as CYP11A, CYP11B and CYP21B. Also regulates the AMH/Muellerian inhibiting substance gene as well as the AHCH and STAR genes. 5'-YCAAGGYC-3' and 5'-RRAGGTCA-3' are the consensus sequences for the recognition by NR5A1. The SFPQ-NONO-NR5A1 complex binds to the CYP17 promoter and regulates basal and cAMP-dependent transcriptional activity (By similarity). Transcription repressor of the Moloney leukemia virus long terminal repeat in undifferentiated murine embryonal carcinoma cells. Binds phosphatidylcholine and phospholipids with a phosphatidylinositol (PI) headgroup, in particular phosphatidyl(3,4)bisphosphate, phosphatidyl(3,5)bisphosphate and phosphatidyl(3,4,5)triphosphate. Activated by the phosphorylation of NR5A1 by HIPK3 leading to increased steroidogenic gene expression upon cAMP signaling pathway stimulation. {ECO:0000250, ECO:0000269|PubMed:17210646, ECO:0000269|PubMed:18988706}. PTM: Acetylation stimulates the transcriptional activity. {ECO:0000250}.; PTM: Sumoylation reduces CDK7-mediated phosphorylation on Ser-203. {ECO:0000250}.; PTM: Phosphorylated on Ser-203 by CDK7. This phosphorylation promotes transcriptional activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Binds DNA as a monomer (By similarity). Part of a complex consisting of SFPQ, NONO and NR5A1. Interacts with DGKQ and CDK7 (By similarity). Interacts with NR0B2, NCOA2 and PPARGC1A. Binds to and activated by HIPK3. {ECO:0000250, ECO:0000269|PubMed:15707893, ECO:0000269|PubMed:15721253, ECO:0000269|PubMed:17210646, ECO:0000269|PubMed:18988706, ECO:0000269|PubMed:8395013}. +Q9Z1W9 STK39_MOUSE STE20/SPS1-related proline-alanine-rich protein kinase (Ste-20-related kinase) (EC 2.7.11.1) (Serine/threonine-protein kinase 39) 556 60,320 Active site (1); Beta strand (8); Binding site (1); Chain (1); Compositional bias (2); Domain (1); Helix (17); Modified residue (8); Motif (2); Mutagenesis (2); Nucleotide binding (1); Region (1); Turn (8) FUNCTION: May act as a mediator of stress-activated signals. Mediates the inhibition of SLC4A4, SLC26A6 as well as CFTR activities by the WNK scaffolds, probably through phosphorylation (PubMed:21317537, PubMed:23542070). Phosphorylates RELT (PubMed:16530727). {ECO:0000269|PubMed:16530727, ECO:0000269|PubMed:21317537, ECO:0000269|PubMed:23542070}. PTM: Phosphorylated at Ser-321 by PRKCQ (PubMed:21733846). Autophosphorylation at Thr-243 positively regulates its activity (PubMed:16530727). {ECO:0000269|PubMed:16530727, ECO:0000269|PubMed:21733846}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}. Note=Nucleus when caspase-cleaved. {ECO:0000305}. SUBUNIT: The phosphorylated form forms a complex with WNK2 (PubMed:21733846). Interacts with RELT (PubMed:16530727). {ECO:0000269|PubMed:16530727, ECO:0000269|PubMed:21733846}. DOMAIN: PAPA box (proline-alanine repeats) may target the kinase to a specific subcellular location by facilitating interaction with intracellular proteins such as actin or actin-like proteins. +Q9JI10 STK3_MOUSE Serine/threonine-protein kinase 3 (EC 2.7.11.1) (Mammalian STE20-like protein kinase 2) (MST-2) (STE20-like kinase MST2) [Cleaved into: Serine/threonine-protein kinase 3 36kDa subunit (MST2/N); Serine/threonine-protein kinase 3 20kDa subunit (MST2/C)] 497 56,855 Active site (1); Alternative sequence (1); Binding site (1); Chain (3); Coiled coil (3); Compositional bias (3); Domain (2); Frameshift (1); Modified residue (9); Nucleotide binding (1); Site (1) FUNCTION: Stress-activated, pro-apoptotic kinase which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. Key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. STK3/MST2 and STK4/MST1 are required to repress proliferation of mature hepatocytes, to prevent activation of facultative adult liver stem cells (oval cells), and to inhibit tumor formation. Phosphorylates NKX2-1. Phosphorylates NEK2 and plays a role in centrosome disjunction by regulating the localization of NEK2 to centrosomes, and its ability to phosphorylate CROCC and CEP250. In conjunction with SAV1, activates the transcriptional activity of ESR1 through the modulation of its phosphorylation. Positively regulates RAF1 activation via suppression of the inhibitory phosphorylation of RAF1 on 'Ser-259'. Phosphorylates MOBKL1A and RASSF2. Phosphorylates MOBKL1B on 'Thr-74'. Acts cooperatively with MOBKL1B to activate STK38 (By similarity). {ECO:0000250|UniProtKB:Q13188, ECO:0000269|PubMed:20080689}. PTM: Phosphorylation at Thr-117 and Thr-390 by PKB/AKT1, leads to inhibition of its: cleavage, kinase activity, autophosphorylation at Thr-180, binding to RASSF1 and nuclear translocation, and increase in its binding to RAF1. {ECO:0000250}.; PTM: Proteolytically cleaved by caspase-3 during apoptosis. Proteolytic cleavage results in kinase activation and nuclear translocation of the truncated form (MST1/N). {ECO:0000269|PubMed:11278283}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=The caspase-cleaved form cycles between nucleus and cytoplasm. Phosphorylation at Thr-117 leads to inhibition of nuclear translocation (By similarity). {ECO:0000250}. SUBUNIT: Homodimer; mediated via the coiled-coil region. Interacts with NORE1, which inhibits autoactivation. Interacts with and stabilizes SAV1. Interacts with RAF1, which prevents dimerization and phosphorylation. Interacts with RASSF1. Interacts (via SARAH domain) with NEK2. Interacts with ESR1 only in the presence of SAV1. Interacts with PKB/AKT1. Forms a tripartite complex with MOBKL1B and STK38. Interacts with RASSF2 (via SARAH domain). Interacts with LATS1; this interaction is inhibited in the presence of DLG5. Interacts with MARK3 in the presence of DLG5 (By similarity). Interacts with DLG5 (via PDZ domain 3) (PubMed:28087714). {ECO:0000250|UniProtKB:Q13188, ECO:0000269|PubMed:28087714}. +Q6PE84 STML3_MOUSE Stomatin-like protein 3 (SLP-3) (Stomatin-related olfactory protein) 287 31,591 Chain (1); Erroneous initiation (2); Modified residue (2); Mutagenesis (4); Sequence conflict (1); Topological domain (1); Transmembrane (1) TRANSMEM 25 45 Helical; Signal-anchor for type III membrane protein. {ECO:0000255}. TOPO_DOM 46 287 Cytoplasmic. {ECO:0000255}. FUNCTION: Required for the function of many mechanoreceptors. Modulate mechanotransduction channels and acid-sensing ion channels (ASIC) proteins. Potentiates PIEZO1 and PIEZO2 function by increasing their sensitivity to mechanical stimulations. {ECO:0000269|PubMed:24662763}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12122055, ECO:0000269|PubMed:24662763}; Single-pass type III membrane protein {ECO:0000269|PubMed:12122055}. Note=Detected in lipid rafts, in apical dendrites and in olfactory cilia. SUBUNIT: Homodimer. Interacts with PIEZO1 and PIEZO2. {ECO:0000269|PubMed:24662763}. TISSUE SPECIFICITY: Expressed by all dorsal root ganglion neurons and is selectively expressed in neuronal tissues. Detected in olfactory epithelium. {ECO:0000269|PubMed:12122055, ECO:0000269|PubMed:17167420}. +O70491 STRA6_MOUSE Receptor for retinol uptake STRA6 (Retinoic acid-responsive protein) (Retinol-binding protein receptor STRA6) (Stimulated by retinoic acid gene 6 protein) 670 73,775 Chain (1); Glycosylation (2); Intramembrane (1); Modified residue (1); Region (1); Sequence conflict (1); Topological domain (11); Transmembrane (9) INTRAMEM 511 548 Helical. {ECO:0000250|UniProtKB:F1RAX4}. TRANSMEM 51 71 Helical. {ECO:0000250|UniProtKB:F1RAX4}.; TRANSMEM 98 118 Helical. {ECO:0000250|UniProtKB:F1RAX4}.; TRANSMEM 145 165 Helical. {ECO:0000250|UniProtKB:F1RAX4}.; TRANSMEM 169 189 Helical. {ECO:0000250|UniProtKB:F1RAX4}.; TRANSMEM 206 226 Helical. {ECO:0000250|UniProtKB:F1RAX4}.; TRANSMEM 297 317 Helical. {ECO:0000250|UniProtKB:F1RAX4}.; TRANSMEM 369 389 Helical. {ECO:0000250|UniProtKB:F1RAX4}.; TRANSMEM 424 444 Helical. {ECO:0000250|UniProtKB:F1RAX4}.; TRANSMEM 475 495 Helical. {ECO:0000250|UniProtKB:F1RAX4}. TOPO_DOM 1 50 Extracellular. {ECO:0000250|UniProtKB:F1RAX4}.; TOPO_DOM 72 97 Cytoplasmic. {ECO:0000250|UniProtKB:F1RAX4}.; TOPO_DOM 119 144 Extracellular. {ECO:0000250|UniProtKB:F1RAX4}.; TOPO_DOM 166 168 Cytoplasmic. {ECO:0000250|UniProtKB:F1RAX4}.; TOPO_DOM 190 205 Extracellular. {ECO:0000250|UniProtKB:F1RAX4}.; TOPO_DOM 227 296 Cytoplasmic. {ECO:0000250|UniProtKB:F1RAX4}.; TOPO_DOM 318 368 Extracellular. {ECO:0000250|UniProtKB:F1RAX4}.; TOPO_DOM 390 423 Cytoplasmic. {ECO:0000250|UniProtKB:F1RAX4}.; TOPO_DOM 445 474 Extracellular. {ECO:0000250|UniProtKB:F1RAX4}.; TOPO_DOM 496 510 Cytoplasmic. {ECO:0000250|UniProtKB:F1RAX4}.; TOPO_DOM 549 670 Cytoplasmic. {ECO:0000250|UniProtKB:F1RAX4}. FUNCTION: Functions as retinol transporter (PubMed:23839944, PubMed:24852372). Accepts all-trans retinol from the extracellular retinol-binding protein RBP4, facilitates retinol transport across the cell membrane, and then transfers retinol to the cytoplasmic retinol-binding protein RBP1. Retinol uptake is enhanced by LRAT, an enzyme that converts retinol to all-trans retinyl esters, the storage forms of vitamin A (By similarity). Contributes to the activation of a signaling cascade that depends on retinol transport and LRAT-dependent generation of retinol metabolites that then trigger activation of JAK2 and its target STAT5, and ultimately increase the expression of SOCS3 and inhibit cellular responses to insulin (PubMed:21368206, PubMed:23839944). Important for the homeostasis of vitamin A and its derivatives, such as retinoic acid and 11-cis-retinal (PubMed:22467576, PubMed:24852372). STRA6-mediated transport is particularly important in the eye, and under conditions of dietary vitamin A deficiency (PubMed:22467576, PubMed:23839944, PubMed:24852372). Does not transport retinoic acid (By similarity). {ECO:0000250|UniProtKB:Q9BX79, ECO:0000269|PubMed:21368206, ECO:0000269|PubMed:22467576, ECO:0000269|PubMed:23839944, ECO:0000269|PubMed:24852372}. PTM: Phosphorylated on tyrosine residues in response to RBP4 binding (PubMed:21368206). Phosphorylation requires the presence of LRAT, suggesting it may be triggered by the uptake of retinol that is then metabolized within the cell to retinoids that function as signaling molecules (By similarity). {ECO:0000250|UniProtKB:Q9BX79, ECO:0000269|PubMed:21368206}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9203140}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q0V8E7}. Note=In the retinal pigment epithelium localizes to the basolateral membrane (PubMed:22467576, PubMed:24852372). Plasma membrane of the basal pole of Sertoli cells, absent in plasma membrane of neighboring spermatogonia (PubMed:9203140). {ECO:0000250|UniProtKB:Q0V8E7, ECO:0000269|PubMed:22467576, ECO:0000269|PubMed:9203140}. SUBUNIT: Homodimer (By similarity). Interacts with JAK2 and STAT5. Interacts (via extracellular domains) with RBP4. Interacts (via cytoplasmic domains) with RBP1 (By similarity). {ECO:0000250|UniProtKB:F1RAX4, ECO:0000250|UniProtKB:Q9BX79}. DOMAIN: Contrary to predictions, contains nine transmembrane helices, with an extracellular N-terminus and a cytoplasmic C-terminus (By similarity). Besides, contains one long helix that dips into the membrane and then runs more or less parallel to the membrane surface (By similarity). {ECO:0000250|UniProtKB:F1RAX4, ECO:0000250|UniProtKB:Q0V8E7}. TISSUE SPECIFICITY: Widely expressed in the embryo (PubMed:9203140, PubMed:23839944). Detected in adult in the retinal pigment epithelium in the eye (PubMed:9203140, PubMed:22467576, PubMed:23839944, PubMed:24852372). In the adult, is highly expressed in cells that compose blood-organ barriers in the brain (choroid plexus and the brain microvascular), in testis (the basal layer of the seminiferous epithelium), in the yolk sac, and in the chorioallantoic placenta (PubMed:9203140, PubMed:23839944). Detected in white adipose tissue and skeletal muscle, but not in liver (at protein level) (PubMed:21368206). Widely expressed in adult, with high expression levels in the eye (PubMed:24852372). Detected in brain, cerebellum, testis, pituitary, pancreas, kidney, spleen, and female genital tract; and at very low levels in heart and lung (PubMed:9203140, PubMed:24852372). Not detected in liver (PubMed:9203140). {ECO:0000269|PubMed:21368206, ECO:0000269|PubMed:22467576, ECO:0000269|PubMed:23839944, ECO:0000269|PubMed:24852372, ECO:0000269|PubMed:9203140}. +O70166 STMN3_MOUSE Stathmin-3 (Hippocampus abundant transcript 3) (SCG10-like protein) (SCG10-related protein HiAT3) 180 20,954 Chain (1); Coiled coil (1); Domain (1); Lipidation (2); Modified residue (7) FUNCTION: Exhibits microtubule-destabilizing activity, which is antagonized by STAT3. {ECO:0000269|PubMed:16401721}. PTM: N-terminal palmitoylation promotes specific anchoring to the cytosolic leaflet of Golgi membranes and subsequent vesicular trafficking along dendrites and axons. Neuronal Stathmins are substrates for palmitoyltransferases ZDHHC3, ZDHHC7 and ZDHHC15 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus. Cell projection, growth cone. Cell projection, axon. SUBUNIT: Interacts with STAT3. {ECO:0000269|PubMed:16401721}. TISSUE SPECIFICITY: Neuron specific. +P50427 STS_MOUSE Steryl-sulfatase (EC 3.1.6.2) (Arylsulfatase C) (ASC) (Steroid sulfatase) (Steryl-sulfate sulfohydrolase) 624 66,591 Active site (2); Chain (1); Disulfide bond (4); Glycosylation (2); Metal binding (5); Modified residue (1); Signal peptide (1); Topological domain (3); Transmembrane (2) TRANSMEM 193 216 Helical. {ECO:0000250}.; TRANSMEM 221 242 Helical. {ECO:0000250}. TOPO_DOM 24 192 Lumenal. {ECO:0000250}.; TOPO_DOM 217 220 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 243 624 Lumenal. {ECO:0000250}. FUNCTION: Conversion of sulfated steroid precursors to estrogens during pregnancy. PTM: The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity. {ECO:0000250}. SUBCELLULAR LOCATION: Microsome membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=The sequence shows several membrane-spanning domains that could serve to anchor the protein in the microsomal membrane. SUBUNIT: Homodimer. +Q8R1Q0 STX19_MOUSE Syntaxin-19 (Syntaxin-9) 292 33,867 Chain (1); Compositional bias (1); Domain (1); Frameshift (1); Sequence conflict (1) FUNCTION: Plays a role in endosomal trafficking of the epidermal growth factor receptor (EGFR). {ECO:0000269|PubMed:16420529}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16420529}; Peripheral membrane protein {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:16420529}. SUBUNIT: Interacts with EGFR. {ECO:0000269|PubMed:16420529}. TISSUE SPECIFICITY: Expressed in stomach, lung and skin (at protein level). In stomach, strongly expressed in the mucosa of the fundus, in epithelial cells of gastric pits, and in gastric glands (at protein level). In skin, expressed in the epidermis, dermis, and epithelial layer of the hair bulb (at protein level). {ECO:0000269|PubMed:16420529}. +P54116 STOM_MOUSE Erythrocyte band 7 integral membrane protein (Protein 7.2b) (Stomatin) 284 31,375 Beta strand (4); Chain (1); Erroneous gene model prediction (1); Helix (5); Intramembrane (1); Lipidation (2); Modified residue (3); Mutagenesis (5); Region (3); Sequence conflict (7); Topological domain (2) INTRAMEM 32 52 {ECO:0000255}. TOPO_DOM 1 31 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 53 284 Cytoplasmic. {ECO:0000255}. FUNCTION: Regulates ion channel activity and transmembrane ion transport. Regulates ASIC2 and ASIC3 channel activity. {ECO:0000269|PubMed:15471860, ECO:0000269|PubMed:22850675}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P27105}; Peripheral membrane protein {ECO:0000250|UniProtKB:P27105}; Cytoplasmic side {ECO:0000250|UniProtKB:P27105}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P27105}. Cell membrane {ECO:0000250|UniProtKB:P27105}; Lipid-anchor {ECO:0000250|UniProtKB:P27105}; Cytoplasmic side {ECO:0000250|UniProtKB:P27105}. Membrane raft {ECO:0000250|UniProtKB:P27105}. Melanosome {ECO:0000250|UniProtKB:P27105}. Cytoplasmic vesicle {ECO:0000269|PubMed:10383825}. Note=Localizes to juxtanuclear structure probably derived from the Golgi apparatus. Colocalizes with cortical actin microfilaments at small plasma membrane protrusions. Associates with alpha-granular lipid rafts. Translocates from the alpha-granular lipid rafts to the cell membrane on thrombin activation and selectively enriched in released microvesicles. Identified by mass spectrometry in melanosome fractions from stage I to stage IV. {ECO:0000250|UniProtKB:P27105}. SUBUNIT: Interacts with LANCL1. Interacts with SLC2A1 and SLC4A1. Identified in large complexes with SLC40A1, SLC14A1, SLC29A1 and AQP1 (By similarity). Homodimer and higher order homooligomers. The homodimer is banana-shaped. Interacts with ASIC1, ASIC2 and ASIC3. Interacts with STOML1; may redistribute STOM from the plasma membrane to late endosomes. {ECO:0000250, ECO:0000250|UniProtKB:P27105, ECO:0000269|PubMed:15471860, ECO:0000269|PubMed:22850675}. TISSUE SPECIFICITY: Expressed in all sensory neurons of the dorsal root ganglia. In the CNS, expressed in many neurons of the spinal cord, medulla and pons. Expressed only in scattered neurons in the cortex, hippocampus, thalamus and basal ganglia. In the cerebellum, expressed in all Purkinje cells (at protein level). Widely expressed with high levels in heart, liver, skeletal muscle and testis and low levels in lung, brain and spleen. {ECO:0000269|PubMed:10383825, ECO:0000269|PubMed:7540886}. +O35526 STX1A_MOUSE Syntaxin-1A (Neuron-specific antigen HPC-1) 288 33,054 Chain (1); Coiled coil (1); Domain (1); Modified residue (4); Topological domain (2); Transmembrane (1) TRANSMEM 266 286 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 1 265 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 287 288 Extracellular. {ECO:0000255}. FUNCTION: Plays a role in hormone and neurotransmitter exocytosis (By similarity). Potentially involved in docking of synaptic vesicles at presynaptic active zones. May mediate Ca(2+)-regulation of exocytosis acrosomal reaction in sperm (PubMed:15774481). {ECO:0000250|UniProtKB:P32851, ECO:0000269|PubMed:15774481}. PTM: Phosphorylated by CK2. Phosphorylation at Ser-188 by DAPK1 significantly decreases its interaction with STXBP1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:18760330}; Single-pass type IV membrane protein {ECO:0000269|PubMed:18760330}. Cell junction, synapse, synaptosome {ECO:0000269|PubMed:18760330}. Cell membrane {ECO:0000250|UniProtKB:P32851}. Note=Colocalizes with KCNB1 at the cell membrane. {ECO:0000250|UniProtKB:P32851}. SUBUNIT: Interacts (via C-terminus) with KCNB1 (via C-terminus); the interaction increases in a calcium-dependent manner and induces a pore-independent enhancement of exocytosis in neuroendocrine cells, chromaffin cells, pancreatic beta cells and from the soma of dorsal root ganglia (DRG) neurons (By similarity). Part of the SNARE core complex containing SNAP25, VAMP2 and STX1A (PubMed:19196426). This complex binds to CPLX1 (By similarity). Interacts with VAPA and SYBU (By similarity). Binds STXBP6 (By similarity). Found in a complex with VAMP8 and SNAP23 (By similarity). Found in a ternary complex with STX1A and SNAP25 (By similarity). Interacts with SLC6A4 (By similarity). Binds SYTL4 (PubMed:12101244). Interacts with OTOF and LGI3 (PubMed:18760330, PubMed:17055430). Interacts with SYT6 and SYT8; the interaction is Ca(2+)-dependent (PubMed:15774481). Interacts with STXBP1 and DAPK1 (By similarity). Interacts with PLCL1 (via C2 domain) (PubMed:23341457). Interacts with PRRT2 (PubMed:29056747). Interacts with SEPT8 (By similarity). {ECO:0000250|UniProtKB:P32851, ECO:0000250|UniProtKB:Q16623, ECO:0000269|PubMed:12101244, ECO:0000269|PubMed:15774481, ECO:0000269|PubMed:17055430, ECO:0000269|PubMed:18760330, ECO:0000269|PubMed:19196426, ECO:0000269|PubMed:23341457, ECO:0000269|PubMed:29056747}. +Q0VBF8 STUM_MOUSE Protein stum homolog 141 15,005 Chain (1); Compositional bias (2); Modified residue (1); Transmembrane (2) TRANSMEM 51 71 Helical. {ECO:0000255}.; TRANSMEM 87 107 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +P61264 STX1B_MOUSE Syntaxin-1B 288 33,245 Chain (1); Coiled coil (1); Domain (1); Modified residue (2); Sequence conflict (13); Topological domain (1); Transmembrane (1) TRANSMEM 265 288 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 1 264 Cytoplasmic. {ECO:0000255}. FUNCTION: Potentially involved in docking of synaptic vesicles at presynaptic active zones (By similarity). May mediate Ca(2+)-regulation of exocytosis acrosomal reaction in sperm. {ECO:0000250, ECO:0000269|PubMed:15774481}. PTM: Phosphorylated by CK2. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}. SUBUNIT: Interacts with OTOF. Interacts with SYT6 and SYT8; the interaction is Ca(2+)-dependent. {ECO:0000269|PubMed:15774481, ECO:0000269|PubMed:17055430}. +Q00262 STX2_MOUSE Syntaxin-2 (Epimorphin) 289 33,178 Chain (1); Coiled coil (1); Domain (1); Topological domain (1); Transmembrane (1) TRANSMEM 266 289 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 1 265 Cytoplasmic. {ECO:0000255}. FUNCTION: Essential for epithelial morphogenesis. May mediate Ca(2+)-regulation of exocytosis acrosomal reaction in sperm. {ECO:0000269|PubMed:15774481, ECO:0000269|PubMed:7957204}. SUBCELLULAR LOCATION: Membrane; Single-pass type IV membrane protein. SUBUNIT: Interacts with SYT6 and SYT8; the interaction is Ca(2+)-dependent. {ECO:0000269|PubMed:15774481}. +Q8K400 STXB5_MOUSE Syntaxin-binding protein 5 (Lethal(2) giant larvae protein homolog 3) (Tomosyn-1) 1152 127,651 Alternative sequence (1); Chain (1); Compositional bias (2); Domain (1); Modified residue (12); Repeat (14); Sequence conflict (9) FUNCTION: Plays a regulatory role in calcium-dependent exocytosis and neurotransmitter release (By similarity). Inhibits membrane fusion between transport vesicles and the plasma membrane. May modulate the assembly of trans-SNARE complexes between transport vesicles and the plasma membrane. Competes with STXBP1 for STX1 binding. Inhibits translocation of GLUT4 from intracellular vesicles to the plasma membrane. {ECO:0000250, ECO:0000269|PubMed:12832401}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12832401}. Cell membrane {ECO:0000269|PubMed:12832401}; Peripheral membrane protein {ECO:0000269|PubMed:12832401}. Membrane {ECO:0000269|PubMed:12832401}; Peripheral membrane protein {ECO:0000269|PubMed:12832401}. Note=Cytoplasmic, and associated with vesicular membranes and the plasma membrane. SUBUNIT: Part of a complex that contains STX1, STXBP5, SNAP25 and SYT1 (By similarity). Interacts with STX1A and STX4A via its v-SNARE homology domain. Part of a complex that contains STXBP5, STX4A and SNAP23. {ECO:0000250, ECO:0000269|PubMed:12832401}. TISSUE SPECIFICITY: Detected in heart, spleen, lung, skeletal muscle, liver and kidney (at protein level). Detected in brain, particularly in the olfactory bulb and in hippocampus. Detected in the tenia tecta and in the piriform layer of the brain cortex. {ECO:0000269|PubMed:12832401, ECO:0000269|PubMed:15659226}. +O08599 STXB1_MOUSE Syntaxin-binding protein 1 (Protein unc-18 homolog 1) (Unc18-1) (Protein unc-18 homolog A) (Unc-18A) 594 67,569 Alternative sequence (1); Chain (1); Erroneous gene model prediction (1); Modified residue (5); Natural variant (1); Sequence conflict (4) FUNCTION: May participate in the regulation of synaptic vesicle docking and fusion, possibly through interaction with GTP-binding proteins. Essential for neurotransmission and binds syntaxin, a component of the synaptic vesicle fusion machinery probably in a 1:1 ratio. Can interact with syntaxins 1, 2, and 3 but not syntaxin 4. May play a role in determining the specificity of intracellular fusion reactions (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P61764}. Membrane; Peripheral membrane protein. SUBUNIT: Binds SYTL4. Interacts with STX1A. {ECO:0000250}. +Q8K007 SULF1_MOUSE Extracellular sulfatase Sulf-1 (mSulf-1) (EC 3.1.6.-) 870 100,923 Active site (1); Chain (1); Erroneous initiation (1); Glycosylation (10); Metal binding (5); Modified residue (1); Sequence caution (2); Sequence conflict (1); Signal peptide (1) FUNCTION: Exhibits arylsulfatase activity and highly specific endoglucosamine-6-sulfatase activity. It can remove sulfate from the C-6 position of glucosamine within specific subregions of intact heparin. Diminishes HSPG (heparan sulfate proteoglycans) sulfation, inhibits signaling by heparin-dependent growth factors, diminishes proliferation, and facilitates apoptosis in response to exogenous stimulation (By similarity). {ECO:0000250}. PTM: The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250}. Golgi apparatus, Golgi stack {ECO:0000250}. Cell surface {ECO:0000250}. Note=Also localized on the cell surface. {ECO:0000250}. +Q8CFG0 SULF2_MOUSE Extracellular sulfatase Sulf-2 (mSulf-2) (EC 3.1.6.-) 875 100,497 Active site (1); Chain (1); Erroneous initiation (1); Glycosylation (13); Metal binding (5); Modified residue (1); Sequence conflict (7); Signal peptide (1) FUNCTION: Exhibits arylsulfatase activity and highly specific endoglucosamine-6-sulfatase activity. It can remove sulfate from the C-6 position of glucosamine within specific subregions of intact heparin (By similarity). {ECO:0000250}. PTM: The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250}. Golgi apparatus, Golgi stack {ECO:0000250}. Cell surface {ECO:0000250}. Note=Also localized on the cell surface. {ECO:0000250}. +Q9D666 SUN1_MOUSE SUN domain-containing protein 1 (Protein unc-84 homolog A) (Sad1/unc-84 protein-like 1) 913 101,976 Alternative sequence (4); Beta strand (12); Chain (1); Coiled coil (2); Disulfide bond (1); Domain (1); Erroneous initiation (1); Helix (7); Modified residue (3); Region (4); Sequence conflict (8); Topological domain (2); Transmembrane (1) TRANSMEM 416 436 Helical. TOPO_DOM 1 415 Nuclear.; TOPO_DOM 437 913 Perinuclear space. FUNCTION: As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex involved in the connection between the nuclear lamina and the cytoskeleton (PubMed:20711465, PubMed:16380439, PubMed:24062341, PubMed:25892231, PubMed:26842404). The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning (PubMed:19874786). Required for interkinetic nuclear migration (INM) and essential for nucleokinesis and centrosome-nucleus coupling during radial neuronal migration in the cerebral cortex and during glial migration (PubMed:19874786). Involved in telomere attachment to nuclear envelope in the prophase of meiosis implicating a SUN1/2:KASH5 LINC complex in which SUN1 and SUN2 seem to act at least partial redundantly (PubMed:17543860, PubMed:19211677, PubMed:19509342, PubMed:24062341, PubMed:25892231, PubMed:26842404). Required for gametogenesis and involved in selective gene expression of coding and non-coding RNAs needed for gametogenesis (PubMed:17543860). Helps to define the distribution of nuclear pore complexes (NPCs) (PubMed:17724119). Required for efficient localization of SYNE4 in the nuclear envelope (PubMed:23348741). May be involved in nuclear remodeling during sperm head formation in spermatogenenis (PubMed:20711465). May play a role in DNA repair by suppressing non-homologous end joining repair to facilitate the repair of DNA cross-links (By similarity). {ECO:0000250|UniProtKB:O94901, ECO:0000269|PubMed:16380439, ECO:0000269|PubMed:17543860, ECO:0000269|PubMed:17724119, ECO:0000269|PubMed:19211677, ECO:0000269|PubMed:19509342, ECO:0000269|PubMed:19874786, ECO:0000269|PubMed:20711465, ECO:0000269|PubMed:23348741, ECO:0000269|PubMed:24062341, ECO:0000269|PubMed:25892231, ECO:0000269|PubMed:26842404}.; FUNCTION: Isoform 5 may be involved in nuclear remodeling during sperm head formation in spermatogenenis. A probable SUN1 isoform 5:SYNE3 LINC complex may tether spermatid nuclei to anterior cytoskeletal structures such as actin filaments present at membraneous junctions of spermatids and Sertoli cells. {ECO:0000305|PubMed:20711465}. PTM: The disulfid bond with KASH domain containing nesprins is required for stability of the respective LINC complexes under tensile forces. {ECO:0000250|UniProtKB:Q9UH99}. SUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000269|PubMed:11593002, ECO:0000269|PubMed:12036294, ECO:0000269|PubMed:16380439, ECO:0000269|PubMed:16648470, ECO:0000269|PubMed:17132086, ECO:0000269|PubMed:17724119, ECO:0000269|PubMed:18845190, ECO:0000269|PubMed:19841137, ECO:0000269|PubMed:19843581, ECO:0000269|PubMed:19874786, ECO:0000269|PubMed:23348741}; Single-pass type II membrane protein {ECO:0000269|PubMed:11593002, ECO:0000269|PubMed:12036294, ECO:0000269|PubMed:16380439, ECO:0000269|PubMed:16648470, ECO:0000269|PubMed:17132086, ECO:0000269|PubMed:17724119, ECO:0000269|PubMed:18845190, ECO:0000269|PubMed:19841137, ECO:0000269|PubMed:19843581, ECO:0000269|PubMed:19874786, ECO:0000269|PubMed:23348741}. Note=At oocyte MI stage localized around the spindle, at MII stage localized to the spindle poles. In round spermatids mainly localizes to the posterior pole of the nucleus. This localization is gradually disappearing during spermiogenesis. In elongated spermatids localizes to anterior regions outside the nucleus indicative for isoform 5. {ECO:0000269|PubMed:20711465, ECO:0000269|PubMed:26842404}.; SUBCELLULAR LOCATION: Isoform 5: Cytoplasmic vesicle, secretory vesicle, acrosome outer membrane {ECO:0000305|PubMed:20711465}. Note=Localized to the anterior pole of spermatids. {ECO:0000305|PubMed:20711465}. SUBUNIT: Core component of the LINC complex which is composed of inner nuclear membrane SUN domain-containing proteins coupled to outer nuclear membrane KASH domain-containing nesprins. SUN and KASH domain-containing proteins seem to bind each other promiscuously; however, differentially expression of LINC complex constituents is giving rise to specific assemblies. At least SUN1/2-containing core LINC complexes are proposed to be hexameric composed of three protomers of each KASH and SUN domain-containing protein. Interacts with CCDC155/KASH5 (via the last 22 amino acids); this interaction mediates CCDC155 telomere localization by forming a SUN1:KASH5 LINC complex. Isoform 5 is proposed to form a non-nuclear spermatogenesis-specific LINC complex with SYNE3 during sperm head formation. Interacts with SYNE2 and SYNE1; probably forming respective LINC complexes. Interacts with A-type lamin with a strong preference for unprocessed A-type lamin compared with the mature protein. Interaction with lamins B1 and C is hardly detectable. Interacts with NAT10. Interacts with EMD and TSNAX. Associates with the nuclear pore complex (NPC). Interacts with CCDC79/TERB1; promoting the accumulation of the LINC complex complexes at the telomere-nuclear envelope attachment sites. {ECO:0000250|UniProtKB:O94901, ECO:0000269|PubMed:12036294, ECO:0000269|PubMed:16380439, ECO:0000269|PubMed:16648470, ECO:0000269|PubMed:17132086, ECO:0000269|PubMed:18845190, ECO:0000269|PubMed:19843581, ECO:0000269|PubMed:19874786, ECO:0000269|PubMed:19933576, ECO:0000269|PubMed:22826121, ECO:0000269|PubMed:24413433}. DOMAIN: The coiled coil domains differentially mediate trimerization required for binding to nesprins and are proposed to dynamically regulate the oligomeric state by locking the SUN domain in an inactive confirmation. The coiled coil domains are proposed to be involved in load-bearing and force transmission from the cytoskeleton. {ECO:0000250|UniProtKB:Q8BJS4, ECO:0000250|UniProtKB:Q9UH99}.; DOMAIN: The SUN domain may play a role in the nuclear anchoring and/or migration. TISSUE SPECIFICITY: Widely expressed. Expressed in cochlear outer hair cells (at protein level). Seven isoforms are expressed in testis including testis-specific isoform 5. Isoform 5 is the only isoform expressed at the end of sperm differentiation. Six isoforms are expressed in muscle, heart and brain, four isoforms in kidney and three isoforms in liver. {ECO:0000269|PubMed:12036294, ECO:0000269|PubMed:16380439, ECO:0000269|PubMed:17132086, ECO:0000269|PubMed:23348741}. +Q8C0J6 SWAHC_MOUSE Ankyrin repeat domain-containing protein SOWAHC (Ankyrin repeat domain-containing protein 57) (Protein sosondowah homolog C) 512 54,938 Chain (1); Compositional bias (1); Modified residue (4); Repeat (2); Sequence conflict (5) +F2Z472 SVS3A_MOUSE Seminal vesicle secretory protein 3A (Seminal vesicle secretory protein III) (SVS III) 265 29,967 Alternative sequence (1); Chain (1); Region (1); Repeat (5); Sequence conflict (9); Signal peptide (1) FUNCTION: Component of the copulatory plug. {ECO:0000269|PubMed:11723121}. PTM: Glycosylated. {ECO:0000269|PubMed:11723121}.; PTM: Covalently cross-linked by transglutaminase, which is important for the formation of the gelatinous copulatory plug. Five repeats of Q-X-K-(S/T) in the central region of the protein serve as the transglutaminase substrate site(s). {ECO:0000269|PubMed:11723121}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11723121}. TISSUE SPECIFICITY: Highly expressed in the seminal vesicle where it is detected in luminal epithelium of the mucosa folds, and also in luminal fluid (at protein level). Not detected in other tissues tested. {ECO:0000269|PubMed:11723121}. +Q9JIS5 SV2A_MOUSE Synaptic vesicle glycoprotein 2A (Synaptic vesicle protein 2) (Synaptic vesicle protein 2A) (Calcium regulator SV2A) 742 82,647 Chain (1); Frameshift (1); Glycosylation (3); Modified residue (6); Region (1); Topological domain (13); Transmembrane (12) TRANSMEM 170 190 Helical. {ECO:0000255}.; TRANSMEM 206 226 Helical. {ECO:0000255}.; TRANSMEM 234 254 Helical. {ECO:0000255}.; TRANSMEM 263 283 Helical. {ECO:0000255}.; TRANSMEM 295 315 Helical. {ECO:0000255}.; TRANSMEM 335 355 Helical. {ECO:0000255}.; TRANSMEM 448 468 Helical. {ECO:0000255}.; TRANSMEM 599 619 Helical. {ECO:0000255}.; TRANSMEM 627 647 Helical. {ECO:0000255}.; TRANSMEM 652 672 Helical. {ECO:0000255}.; TRANSMEM 686 708 Helical. {ECO:0000255}.; TRANSMEM 713 731 Helical. {ECO:0000255}. TOPO_DOM 1 169 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 191 205 Extracellular. {ECO:0000255}.; TOPO_DOM 227 233 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 255 262 Extracellular. {ECO:0000255}.; TOPO_DOM 284 294 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 316 334 Extracellular. {ECO:0000255}.; TOPO_DOM 356 447 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 469 598 Extracellular. {ECO:0000255, ECO:0000305|PubMed:16543415}.; TOPO_DOM 620 626 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 648 651 Extracellular. {ECO:0000255}.; TOPO_DOM 673 685 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 709 712 Extracellular. {ECO:0000255}.; TOPO_DOM 732 742 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a role in the control of regulated secretion in neural and endocrine cells, enhancing selectively low-frequency neurotransmission. Positively regulates vesicle fusion by maintaining the readily releasable pool of secretory vesicles.; FUNCTION: (Microbial infection) Receptor for C.botulinum neurotoxin type A (BoNT/A, botA); the toxin probably binds via extracellular loop 4 (PubMed:16543415). {ECO:0000269|PubMed:16543415}.; FUNCTION: (Microbial infection) Possible receptor for C.botulinum neurotoxin type D (BoNT/D, botD); BoNT/D does not bind to extracellular loop 4 as do BoNT/A and BoNT/E (PubMed:21483489). {ECO:0000269|PubMed:21483489}.; FUNCTION: (Microbial infection) Receptor for C.botulinum neurotoxin type E (BoNT/E); the toxin probably binds via extracellular loop 4 (PubMed:18815274). It probably requires glycosylation of Asn-573 (PubMed:18815274). {ECO:0000269|PubMed:18815274, ECO:0000305|PubMed:18815274}. PTM: Phosphorylation by CK1 of the N-terminal cytoplasmic domain regulates interaction with SYT1. {ECO:0000250}.; PTM: N-glycosylated. {ECO:0000305|PubMed:18815274}. SUBCELLULAR LOCATION: Cell junction, synapse {ECO:0000269|PubMed:12209837}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q02563}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q02563}. Note=Enriched in chromaffin granules, not present in adrenal microsomes. Associated with both insulin granules and synaptic-like microvesicles in insulin-secreting cells of the pancreas (By similarity). Colocalizes with ATP2B1 at photoreceptor synaptic terminals. {ECO:0000250|UniProtKB:Q02563, ECO:0000269|PubMed:12209837}. SUBUNIT: Interacts with SYT1/synaptotagmin-1 in a calcium-dependent manner. Binds the adapter protein complex AP-2 (By similarity). {ECO:0000250}.; SUBUNIT: (Microbial infection) Interacts with C.botulinum neurotoxin type A (BoNT/A, botA). {ECO:0000269|PubMed:18815274, ECO:0000305|PubMed:16543415}. TISSUE SPECIFICITY: Expressed in conventional synapses and cone ribbon synapses in the retina (at protein level) (PubMed:12687700). Expressed in diaphragm motor nerve terminals (at protein level) (PubMed:16543415). Expressed in hippocampus neurons (at protein level) (PubMed:18815274). {ECO:0000269|PubMed:12687700, ECO:0000269|PubMed:16543415, ECO:0000269|PubMed:18815274}. +Q8BG39 SV2B_MOUSE Synaptic vesicle glycoprotein 2B (Synaptic vesicle protein 2B) 683 77,457 Chain (1); Glycosylation (3); Modified residue (3); Sequence conflict (1); Topological domain (13); Transmembrane (12) TRANSMEM 111 131 Helical. {ECO:0000255}.; TRANSMEM 149 169 Helical. {ECO:0000255}.; TRANSMEM 183 203 Helical. {ECO:0000255}.; TRANSMEM 206 226 Helical. {ECO:0000255}.; TRANSMEM 238 258 Helical. {ECO:0000255}.; TRANSMEM 278 298 Helical. {ECO:0000255}.; TRANSMEM 391 411 Helical. {ECO:0000255}.; TRANSMEM 536 556 Helical. {ECO:0000255}.; TRANSMEM 566 586 Helical. {ECO:0000255}.; TRANSMEM 593 613 Helical. {ECO:0000255}.; TRANSMEM 627 649 Helical. {ECO:0000255}.; TRANSMEM 654 672 Helical. {ECO:0000255}. TOPO_DOM 1 110 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 132 148 Extracellular. {ECO:0000255}.; TOPO_DOM 170 182 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 204 205 Extracellular. {ECO:0000255}.; TOPO_DOM 227 237 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 259 277 Extracellular. {ECO:0000255}.; TOPO_DOM 299 390 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 412 535 Extracellular. {ECO:0000255}.; TOPO_DOM 557 565 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 587 592 Extracellular. {ECO:0000255}.; TOPO_DOM 614 626 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 650 653 Extracellular. {ECO:0000255}.; TOPO_DOM 673 683 Cytoplasmic. {ECO:0000255}. FUNCTION: Probably plays a role in the control of regulated secretion in neural and endocrine cells. {ECO:0000305|PubMed:10624962}.; FUNCTION: (Microbial infection) Receptor for C.botulinum neurotoxin type A (BoNT/A, botA); the toxin probably binds via extracellular loop 4 (PubMed:16543415). {ECO:0000269|PubMed:16543415}.; FUNCTION: (Microbial infection) Possible receptor for C.botulinum neurotoxin type D (BoNT/D, botD) (PubMed:21483489). Not a receptor for C.botulinum neurotoxin type D (BoNT/D, botD) (PubMed:21632541). {ECO:0000269|PubMed:21632541}.; FUNCTION: (Microbial infection) Receptor for C.botulinum neurotoxin type E (BoNT/E); the toxin probably binds via extracellular loop 4 (PubMed:18815274). It probably requires glycosylation of Asn-516 (PubMed:18815274). {ECO:0000269|PubMed:18815274, ECO:0000305|PubMed:18815274}. PTM: N-glycosylated. {ECO:0000305|PubMed:18815274}.; PTM: The N-terminal cytoplasmic domain is phosphorylated by CK1. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q63564}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250|UniProtKB:Q63564}. Note=Associated with synaptic-like microvesicles but not with insulin-containing vesicles in insulin-secreting cells of the pancreas (By similarity). Localizes to microvesicles in the pinealocytes. Localizes to the acrosome in spermatids (By similarity). {ECO:0000250|UniProtKB:Q63564}. SUBUNIT: Interacts with SYT1 in a calcium-independent manner. Forms a complex with SYT1, syntaxin-1 and SNAP25. {ECO:0000269|PubMed:15466855}.; SUBUNIT: (Microbial infection) Interacts with C.botulinum neurotoxin type A (BoNT/A, botA). {ECO:0000269|PubMed:18815274, ECO:0000305|PubMed:16543415}.; SUBUNIT: (Microbial infection) Interacts with C.botulinum neurotoxin type D (BoNT/D, botD) (PubMed:21483489). No evidence for its interaction with BoNT/D has also been published (PubMed:21632541). {ECO:0000269|PubMed:21483489, ECO:0000269|PubMed:21632541}. TISSUE SPECIFICITY: Expressed in ribbon synapses of the retina (at protein level) (PubMed:12687700). Expressed in diaphragm motor nerve terminals (at protein level) (PubMed:16543415). Expressed in hippocampus neurons (at protein level) (PubMed:18815274). {ECO:0000269|PubMed:12687700, ECO:0000269|PubMed:16543415, ECO:0000269|PubMed:18815274}. +A2AVA0 SVEP1_MOUSE Sushi, von Willebrand factor type A, EGF and pentraxin domain-containing protein 1 (Polydom) 3567 387,457 Alternative sequence (2); Chain (1); Disulfide bond (94); Domain (47); Glycosylation (1); Sequence conflict (3); Signal peptide (1) FUNCTION: May play a role in the cell attachment process. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Present in stromal osteogenic cells. Expressed at much higher level in stromal osteogenic cells at low density compared to cells grown at higher densities (at protein level). Highly expressed in lung and placenta. Also expressed in bone and periosteum, but not in cartilage and skeletal muscle. Weakly or not expressed in other tissues. {ECO:0000269|PubMed:11062057, ECO:0000269|PubMed:16206243}. +Q61466 SMRD1_MOUSE SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1 (60 kDa BRG-1/Brm-associated factor subunit A) (BRG1-associated factor 60A) (BAF60A) (Protein D15KZ1) (SWI/SNF complex 60 kDa subunit) 515 58,245 Beta strand (4); Chain (1); Coiled coil (1); Compositional bias (1); Cross-link (1); Domain (1); Erroneous initiation (3); Frameshift (2); Helix (5); Modified residue (4); Region (3); Sequence conflict (8) FUNCTION: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner (By similarity). Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (PubMed:17640523). Has a strong influence on vitamin D-mediated transcriptional activity from an enhancer vitamin D receptor element (VDRE). May be a link between mammalian SWI-SNF-like chromatin remodeling complexes and the vitamin D receptor (VDR) heterodimer. Mediates critical interactions between nuclear receptors and the BRG1/SMARCA4 chromatin-remodeling complex for transactivation (By similarity). {ECO:0000250|UniProtKB:Q96GM5, ECO:0000269|PubMed:17640523}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Component of the multiprotein chromatin-remodeling complexes SWI/SNF: SWI/SNF-A (BAF), SWI/SNF-B (PBAF) and related complexes. The canonical complex contains a catalytic subunit (either SMARCA4/BRG1/BAF190A or SMARCA2/BRM/BAF190B), and at least SMARCE1, ACTL6A/BAF53, SMARCC1/BAF155, SMARCC2/BAF170, and SMARCB1/SNF5/BAF47. Other subunits specific to each of the complexes may also be present permitting several possible combinations developmentally and tissue specific (PubMed:8804307, PubMed:8895581). Component of the BAF complex, which includes at least actin (ACTB), ARID1A/BAF250A, ARID1B/BAF250B, SMARCA2/BRM, SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57, SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C (By similarity). In muscle cells, the BAF complex also contains DPF3. Component of neural progenitors-specific chromatin remodeling complex (npBAF complex) composed of at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, PHF10/BAF45A, ACTL6A/BAF53A and actin. Component of neuron-specific chromatin remodeling complex (nBAF complex) composed of at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, DPF1/BAF45B, DPF3/BAF45C, ACTL6B/BAF53B and actin (PubMed:17640523). Component of the SWI/SNF-B (PBAF) chromatin remodeling complex, at least composed of SMARCA4/BRG1, SMARCB1/BAF47/SNF5, ACTL6A/BAF53A or ACTL6B/BAF53B, SMARCE1/BAF57, SMARCD1/BAF60A, SMARCD2/BAF60B, perhaps SMARCD3/BAF60C, SMARCC1/BAF155, SMARCC2/BAF170, PBRM1/BAF180, ARID2/BAF200 and actin (ACTB) (By similarity). Component of SWI/SNF (GBAF) subcomplex, which includes at least BICRA or BICRAL (mutually exclusive), BRD9, SS18, SMARCA2/BRM, SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, SMARCC1/BAF155, and SMARCD1/BAF60A (PubMed:29374058). Specifically interacts with the VDR heterodimer complex. Interacts with ESR1, NR3C1, NR1H4, PGR, SMARCA4, SMARCC1 and SMARCC2 (By similarity). Interacts with DPF2. {ECO:0000250|UniProtKB:Q96GM5, ECO:0000269|PubMed:17640523, ECO:0000269|PubMed:29374058, ECO:0000269|PubMed:8804307, ECO:0000269|PubMed:8895581}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:2725507, ECO:0000269|PubMed:8804307}. +A0AUV4 SMKY_MOUSE Sperm motility kinase Y (EC 2.7.11.1) 508 57,058 Active site (1); Binding site (1); Chain (1); Domain (2); Nucleotide binding (1); Sequence conflict (1) FUNCTION: May play a role in sperm motility, especially in the regulation of flagellar function. {ECO:0000250}. +Q8VE18 SMG8_MOUSE Protein SMG8 (Protein smg-8 homolog) 991 109,667 Chain (1); Modified residue (6); Sequence conflict (3) FUNCTION: Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. Is recruited by release factors to stalled ribosomes together with SMG1 and SMG9 (forming the SMG1C protein kinase complex) and, in the SMG1C complex, is required to mediate the recruitment of SMG1 to the ribosome:SURF complex and to suppress SMG1 kinase activity until the ribosome:SURF complex locates the exon junction complex (EJC). Acts as a regulator of kinase activity (By similarity). {ECO:0000250}. PTM: Phosphorylated by SMG1. {ECO:0000250}. SUBUNIT: Component of the SMG1C complex composed of SMG1, SMG8 and SMG9; the recruitment of SMG8 to SMG1 N-terminus induces a large conformational change in the SMG1 C-terminal head domain containing the catalytic domain. Forms heterodimers with SMG9; this assembly form may represent a SMG1C intermediate form (By similarity). {ECO:0000250}. +Q61900 SMR3A_MOUSE Submaxillary gland androgen-regulated protein 3A (Salivary protein MSG1) (Submaxillary gland androgen-regulated protein 1) 147 15,544 Chain (1); Compositional bias (1); Region (1); Repeat (3); Signal peptide (1) FUNCTION: May play a role in protection or detoxification. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Secreted into saliva by submaxillary gland. +P97443 SMYD1_MOUSE Histone-lysine N-methyltransferase Smyd1 (EC 2.1.1.43) (CD8b-opposite) (SET and MYND domain-containing protein 1) (Zinc finger protein BOP) (m-BOP) 490 56,496 Alternative sequence (3); Beta strand (14); Binding site (1); Chain (1); Domain (1); Erroneous initiation (2); Helix (19); Metal binding (4); Natural variant (3); Region (3); Turn (6); Zinc finger (1) FUNCTION: Methylates histone H3 at 'Lys-4' (H3K4me). Acts as a transcriptional repressor. Essential for cardiomyocyte differentiation and cardiac morphogenesis. {ECO:0000269|PubMed:11923873, ECO:0000269|PubMed:20943667}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11923873}. Nucleus {ECO:0000269|PubMed:11923873}. SUBUNIT: Interacts with HDAC1, HDAC2 and HDAC3. Interacts (via MYND-type zinc finger) with NACA isoform skNAC. {ECO:0000269|PubMed:11923873, ECO:0000269|PubMed:20943667}. DOMAIN: The SET domain is split between the S-sequence (residues 1-49) and the core SET domain (residues 181-258), however the two segments still come together to form a conserved SET domain fold. TISSUE SPECIFICITY: Expressed in cardiac and skeletal muscle, lymphocytes and thymus. {ECO:0000269|PubMed:11923873, ECO:0000269|PubMed:9013956}. +Q9D4B1 SMS2_MOUSE Phosphatidylcholine:ceramide cholinephosphotransferase 2 (EC 2.7.8.27) (Sphingomyelin synthase 2) 365 42,248 Active site (3); Chain (1); Lipidation (4); Topological domain (1); Transmembrane (6) TRANSMEM 80 100 Helical. {ECO:0000255}.; TRANSMEM 128 148 Helical. {ECO:0000255}.; TRANSMEM 159 179 Helical. {ECO:0000255}.; TRANSMEM 219 239 Helical. {ECO:0000255}.; TRANSMEM 248 268 Helical. {ECO:0000255}.; TRANSMEM 273 290 Helical. {ECO:0000255}. TOPO_DOM 291 365 Cytoplasmic. {ECO:0000255}. FUNCTION: Sphingomyelin synthases synthesize the sphingolipid, sphingomyelin, through transfer of the phosphatidyl head group, phosphatidylcholine, on to the primary hydroxyl of ceramide. The reaction is bidirectional depending on the respective levels of the sphingolipid and ceramide. Plasma membrane SMS2 can also convert phosphatidylethanolamine (PE) to ceramide phosphatidylethanolamine (CPE). Major form in liver. Required for cell growth in certain cell types. Regulator of cell surface levels of ceramide, an important mediator of signal transduction and apoptosis. Regulation of sphingomyelin (SM) levels at the cell surface affects insulin sensitivity. {ECO:0000269|PubMed:19590047, ECO:0000269|PubMed:21844222, ECO:0000269|PubMed:22580896, ECO:0000269|PubMed:22849442}. PTM: Palmitoylated on Cys-331, Cys-332, Cys-343 and Cys-348; which plays an important role in plasma membrane localization. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Predominantly plasma membrane, some in Golgi apparatus. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in liver and macrophages. {ECO:0000269|PubMed:19590047}. +Q9CWR2 SMYD3_MOUSE Histone-lysine N-methyltransferase SMYD3 (EC 2.1.1.43) (SET and MYND domain-containing protein 3) (Zinc finger MYND domain-containing protein 1) 428 49,126 Binding site (4); Chain (1); Domain (1); Modified residue (1); Region (3); Sequence conflict (1); Zinc finger (1) FUNCTION: Histone methyltransferase. Specifically methylates 'Lys-4' of histone H3, inducing di- and tri-methylation, but not monomethylation. Also methylates 'Lys-5' of histone H4. Plays an important role in transcriptional activation as a member of an RNA polymerase complex. Binds DNA containing 5'-CCCTCC-3' or 5'-GAGGGG-3' sequences. {ECO:0000250|UniProtKB:Q9H7B4}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H7B4}. Nucleus {ECO:0000250|UniProtKB:Q9H7B4}. Note=Mainly cytoplasmic when cells are arrested at G0/G1. Accumulates in the nucleus at S phase and G2/M. {ECO:0000250|UniProtKB:Q9H7B4}. SUBUNIT: Interacts with HSPCA. Interacts with HELZ. Interacts with POLR2A; the interaction may be indirect and may be mediated by HELZ. Interacts with HSP90AA1; this interaction enhances SMYD3 histone-lysine N-methyltransferase. {ECO:0000250|UniProtKB:Q9H7B4}. +Q3UHD6 SNX27_MOUSE Sorting nexin-27 539 60,989 Alternative sequence (1); Chain (1); Domain (3); Erroneous initiation (1); Erroneous termination (1); Modified residue (2); Region (3) FUNCTION: Involved in the retrograde transport from endosome to plasma membrane, a trafficking pathway that promotes the recycling of internalized transmembrane proteins. Following internalization, endocytosed transmembrane proteins are delivered to early endosomes and recycled to the plasma membrane instead of being degraded in lysosomes. SNX27 specifically binds and directs sorting of a subset of transmembrane proteins containing a PDZ-binding motif at the C-terminus: following interaction with target transmembrane proteins, associates with the retromer complex, preventing entry into the lysosomal pathway, and promotes retromer-tubule based plasma membrane recycling. SNX27 also binds with the WASH complex. Interacts with membranes containing phosphatidylinositol-3-phosphate (PtdIns(3P)). May participate in establishment of natural killer cell polarity. Recruits CYTIP to early endosomes. {ECO:0000269|PubMed:23524343}. SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Note=Localizes to immunological synapse in T-cells. In T-cells, recruited from the cytosol to sorting endosomes by phosphoinositide-3-kinase products (By similarity). {ECO:0000250}. SUBUNIT: Core component of the SNX27-retromer, a multiprotein complex composed of SNX27, the WASH complex and the retromer complex. Interacts (via the FERM-like regions) with the WASH complex. Interacts with SNX1. Interacts with CYTIP. Interacts with DGKZ. Interacts with MCC (By similarity). Interacts (via PDZ domain) with a number of target transmembrane proteins (via PDZ-binding motif): ABCC4, ADRB2, ARHGEF7, GRIA1, GRIA2, GRIN1, GRIN2A GRIN2C, KCNJ6, KCNJ9 and SLC2A1/GLUT1. {ECO:0000250, ECO:0000269|PubMed:15466885, ECO:0000269|PubMed:23524343}. DOMAIN: The PDZ domain mediates binding to a subset of proteins containing a PDZ-binding motif at the C-terminus: the specificity for PDZ-binding motif is provided by the 2 residues located upstream of the canonical PDZ-binding motif. The PDZ domain also mediates binding to the retromer complex via direct interaction with VPS26 (VPS26A or VPS26B). {ECO:0000250}.; DOMAIN: The PX domain mediates binding to phosphatidylinositol 3-phosphate (PtdIns(3P)) and localization to early endosome membranes. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in cells of hematopoietic origin. {ECO:0000269|PubMed:17351151}. +Q91ZA6 SOCS4_MOUSE Suppressor of cytokine signaling 4 (SOCS-4) (Suppressor of cytokine signaling 7) (SOCS-7) 436 49,918 Chain (1); Domain (2); Sequence conflict (2) Protein modification; protein ubiquitination. FUNCTION: SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. Substrate-recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Inhibits EGF signaling by mediating the degradation of the Tyr-phosphorylated EGF receptor/EGFR (By similarity). {ECO:0000250}. DOMAIN: The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin ligase complexes. {ECO:0000250}. +Q91ZR2 SNX18_MOUSE Sorting nexin-18 (Sorting nexin-associated Golgi protein 1) 614 67,904 Binding site (4); Chain (1); Domain (3) FUNCTION: Involved in endocytosis and intracellular vesicle trafficking, both during interphase and at the end of mitosis. Required for efficient progress through mitosis and cytokinesis. Required for normal formation of the cleavage furrow at the end of mitosis (By similarity). Plays a role in endocytosis via clathrin-coated pits, but also clathrin-independent, actin-dependent fluid-phase endocytosis. Plays a role in macropinocytosis. Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate and promotes membrane tubulation. Stimulates the GTPase activity of DNM2. Promotes DNM2 location at the plasma membrane (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Localized at sites of endocytosis at the cell membrane. Detected on newly formed macropinosomes. Partially colocalized with clathrin and dynamin at the cell membrane. Transiently recruited to clathrin-coated pits at a late stage of clathrin-coated vesicle formation (By similarity). {ECO:0000250}. SUBUNIT: Heterodimer with SNX9. Interacts with ITCH. Interacts with dynamin, SYNJ1 and WASL. Interacts with the AP-1 complex (By similarity). {ECO:0000250}. DOMAIN: The PX domain mediates interaction with membranes enriched in phosphatidylinositol 4,5-bisphosphate. {ECO:0000250}. +Q7M718 TR124_MOUSE Taste receptor type 2 member 124 (T2R124) (mT2R50) 309 35,966 Chain (1); Glycosylation (3); Topological domain (8); Transmembrane (7) TRANSMEM 8 28 Helical; Name=1. {ECO:0000255}.; TRANSMEM 47 67 Helical; Name=2. {ECO:0000255}.; TRANSMEM 87 107 Helical; Name=3. {ECO:0000255}.; TRANSMEM 128 148 Helical; Name=4. {ECO:0000255}.; TRANSMEM 184 204 Helical; Name=5. {ECO:0000255}.; TRANSMEM 231 251 Helical; Name=6. {ECO:0000255}.; TRANSMEM 262 282 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 7 Extracellular. {ECO:0000255}.; TOPO_DOM 29 46 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 68 86 Extracellular. {ECO:0000255}.; TOPO_DOM 108 127 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 149 183 Extracellular. {ECO:0000255}.; TOPO_DOM 205 230 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 252 261 Extracellular. {ECO:0000255}.; TOPO_DOM 283 309 Cytoplasmic. {ECO:0000255}. FUNCTION: Putative taste receptor which may play a role in the perception of bitterness. {ECO:0000305}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q99PQ1 TR12A_MOUSE Tripartite motif-containing protein 12A 284 33,320 Chain (1); Coiled coil (1); Sequence conflict (1); Zinc finger (2) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11331580}. TISSUE SPECIFICITY: Expressed in embryonic CNS, liver, kidney, olfactory epithelium. {ECO:0000269|PubMed:11331580}. +Q9EPT5 SO2A1_MOUSE Solute carrier organic anion transporter family member 2A1 (Prostaglandin transporter) (PGT) (Solute carrier family 21 member 2) 643 70,147 Alternative sequence (2); Chain (1); Disulfide bond (3); Domain (1); Glycosylation (3); Mutagenesis (2); Sequence conflict (1); Topological domain (13); Transmembrane (12) TRANSMEM 33 52 Helical; Name=1. {ECO:0000255}.; TRANSMEM 72 92 Helical; Name=2. {ECO:0000255}.; TRANSMEM 99 123 Helical; Name=3. {ECO:0000255}.; TRANSMEM 168 196 Helical; Name=4. {ECO:0000255}.; TRANSMEM 216 236 Helical; Name=5. {ECO:0000255}.; TRANSMEM 255 279 Helical; Name=6. {ECO:0000255}.; TRANSMEM 321 342 Helical; Name=7. {ECO:0000255}.; TRANSMEM 363 386 Helical; Name=8. {ECO:0000255}.; TRANSMEM 391 414 Helical; Name=9. {ECO:0000255}.; TRANSMEM 518 540 Helical; Name=10. {ECO:0000255}.; TRANSMEM 550 575 Helical; Name=11. {ECO:0000255}.; TRANSMEM 610 628 Helical; Name=12. {ECO:0000255}. TOPO_DOM 1 32 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 53 71 Extracellular. {ECO:0000255}.; TOPO_DOM 93 98 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 124 167 Extracellular. {ECO:0000255}.; TOPO_DOM 197 215 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 237 254 Extracellular. {ECO:0000255}.; TOPO_DOM 280 320 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 343 362 Extracellular. {ECO:0000255}.; TOPO_DOM 387 390 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 415 517 Extracellular. {ECO:0000255}.; TOPO_DOM 541 549 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 576 609 Extracellular. {ECO:0000255}.; TOPO_DOM 629 643 Cytoplasmic. {ECO:0000255}. FUNCTION: May mediate the release of newly synthesized prostaglandins from cells, the transepithelial transport of prostaglandins, and the clearance of prostaglandins from the circulation. Transports PGD2, as well as PGE1, PGE2 and PGF2A. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Highly expressed in lung and liver. Detected at lower levels in kidney and skeletal muscle. +Q9JJL3 SO1B2_MOUSE Solute carrier organic anion transporter family member 1B2 (Liver-specific organic anion transporter 1) (LST-1) (SLC21A6) (Solute carrier family 21 member 10) 689 76,729 Alternative sequence (1); Chain (1); Disulfide bond (3); Domain (1); Glycosylation (3); Modified residue (4); Sequence conflict (2); Topological domain (13); Transmembrane (12) TRANSMEM 27 46 Helical; Name=1. {ECO:0000255}.; TRANSMEM 66 86 Helical; Name=2. {ECO:0000255}.; TRANSMEM 93 117 Helical; Name=3. {ECO:0000255}.; TRANSMEM 164 192 Helical; Name=4. {ECO:0000255}.; TRANSMEM 212 232 Helical; Name=5. {ECO:0000255}.; TRANSMEM 251 275 Helical; Name=6. {ECO:0000255}.; TRANSMEM 327 348 Helical; Name=7. {ECO:0000255}.; TRANSMEM 369 392 Helical; Name=8. {ECO:0000255}.; TRANSMEM 397 420 Helical; Name=9. {ECO:0000255}.; TRANSMEM 534 556 Helical; Name=10. {ECO:0000255}.; TRANSMEM 566 591 Helical; Name=11. {ECO:0000255}.; TRANSMEM 626 643 Helical; Name=12. {ECO:0000255}. TOPO_DOM 1 26 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 47 65 Extracellular. {ECO:0000255}.; TOPO_DOM 87 92 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 118 163 Extracellular. {ECO:0000255}.; TOPO_DOM 193 211 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 233 250 Extracellular. {ECO:0000255}.; TOPO_DOM 276 326 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 349 368 Extracellular. {ECO:0000255}.; TOPO_DOM 393 396 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 421 533 Extracellular. {ECO:0000255}.; TOPO_DOM 557 565 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 592 625 Extracellular. {ECO:0000255}.; TOPO_DOM 644 689 Cytoplasmic. {ECO:0000255}. FUNCTION: Mediates the Na(+)-independent uptake of organic anions such as taurochlate, bromosulfophthalein and steroid conjugates such as estrone-3-sulfate, 17-beta-glucuronosyl estradiol, dehydroepiandrosterone sulfate and prostaglandin E2. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Liver specific. +Q99P68 SOST_MOUSE Sclerostin 211 23,443 Beta strand (4); Chain (1); Disulfide bond (4); Domain (1); Glycosylation (2); Sequence conflict (2); Signal peptide (1); Turn (1) FUNCTION: Negative regulator of bone growth that acts through inhibition of Wnt signaling and bone formation. {ECO:0000250, ECO:0000269|PubMed:19419300}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. SUBUNIT: Interacts with LRP4 (via the extracellular domain); the interaction facilitates the inhibition of Wnt signaling. Interacts with LRP5 (via the first two YWTD-EGF repeat domains); the interaction inhibits Wnt-mediated signaling. Interacts with LRP6. {ECO:0000250}. +Q7TQA4 TR140_MOUSE Taste receptor type 2 member 140 (T2R140) (T2R13) (T2R8) (Taste receptor family B member 3) (mTRB3) (mTRB5) (Taste receptor type 2 member 40) (T2R40) (mT2r64) 312 35,555 Chain (1); Glycosylation (3); Sequence conflict (8); Topological domain (8); Transmembrane (7) TRANSMEM 10 30 Helical; Name=1. {ECO:0000255}.; TRANSMEM 47 67 Helical; Name=2. {ECO:0000255}.; TRANSMEM 91 111 Helical; Name=3. {ECO:0000255}.; TRANSMEM 134 154 Helical; Name=4. {ECO:0000255}.; TRANSMEM 185 205 Helical; Name=5. {ECO:0000255}.; TRANSMEM 230 250 Helical; Name=6. {ECO:0000255}.; TRANSMEM 265 285 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 9 Extracellular. {ECO:0000255}.; TOPO_DOM 31 46 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 68 90 Extracellular. {ECO:0000255}.; TOPO_DOM 112 133 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 155 184 Extracellular. {ECO:0000255}.; TOPO_DOM 206 229 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 251 264 Extracellular. {ECO:0000255}.; TOPO_DOM 286 312 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor that may play a role in the perception of bitterness and is gustducin-linked. May play a role in sensing the chemical composition of the gastrointestinal content. The activity of this receptor may stimulate alpha gustducin, mediate PLC-beta-2 activation and lead to the gating of TRPM5. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in subsets of taste receptor cells of the tongue and palate epithelium and exclusively in gustducin-positive cells. Expressed in 15% taste bud cells in circumvallate and foliate papillae but only in 2% in fungiform papillae. +Q61263 SOAT1_MOUSE Sterol O-acyltransferase 1 (EC 2.3.1.26) (Acyl-coenzyme A:cholesterol acyltransferase 1) (ACAT-1) (Cholesterol acyltransferase 1) 540 63,799 Active site (1); Chain (1); Disulfide bond (1); Modified residue (1); Sequence conflict (1); Topological domain (6); Transmembrane (5) TRANSMEM 141 159 Helical. {ECO:0000255}.; TRANSMEM 182 199 Helical. {ECO:0000255}.; TRANSMEM 225 243 Helical. {ECO:0000255}.; TRANSMEM 247 264 Helical. {ECO:0000255}.; TRANSMEM 502 517 Helical. {ECO:0000255}. TOPO_DOM 1 140 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 160 181 Lumenal. {ECO:0000255}.; TOPO_DOM 200 224 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 244 246 Lumenal. {ECO:0000255}.; TOPO_DOM 265 501 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 518 540 Lumenal. {ECO:0000255}. FUNCTION: Catalyzes the formation of fatty acid-cholesterol esters, which are less soluble in membranes than cholesterol. Plays a role in lipoprotein assembly and dietary cholesterol absorption. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000269|PubMed:11071899}. SUBUNIT: May form homo- or heterodimers. Interacts with UBIAD1. {ECO:0000250|UniProtKB:P35610}. +P15533 TR30A_MOUSE Tripartite motif-containing protein 30A (Down regulatory protein of interleukin-2 receptor) (Tripartite motif-containing protein 30) 496 57,330 Alternative sequence (2); Chain (1); Coiled coil (1); Domain (1); Erroneous initiation (1); Frameshift (1); Helix (1); Motif (1); Mutagenesis (1); Region (1); Sequence conflict (6); Turn (3); Zinc finger (2) FUNCTION: Trans-acting factor that regulates gene expression of interleukin 2 receptor alpha chain. May affect IL2R-alpha expression through cis-acting negative regulatory elements or through competition with proteins that bind to enhancer or activator sequences. Negatively regulates Toll-like receptor (TLR)-mediated activation of NFKB by promoting degradation of TAB2 and TAB3 and preventing TRAF6 autoubiquitination. Negatively regulates production of reactive oxygen species (ROS) which inhibits activation of the NLRP3 inflammasome complex. This, in turn, regulates activation of CASP1 and subsequent cleavage of IL1B and IL18. No activity detected against a range of retroviruses including a number of lentiviruses, gammaretroviruses and betaretroviruses. {ECO:0000269|PubMed:18345001, ECO:0000269|PubMed:19147168, ECO:0000269|PubMed:21048113}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. SUBUNIT: Homomultimer. Interacts with NR2C2/TAK1, TAB2 and TAB3. Does not interact with NLRP3, NLRC4 or TAB1. {ECO:0000269|PubMed:18345001, ECO:0000269|PubMed:21048113}. TISSUE SPECIFICITY: Highly expressed in spleen and lymph nodes (at protein level). {ECO:0000269|PubMed:18345001}. +Q99PP6 TR34A_MOUSE Tripartite motif-containing protein 34A 485 55,908 Alternative sequence (4); Chain (1); Coiled coil (1); Domain (1); Sequence conflict (1); Zinc finger (2) FUNCTION: May function as antiviral protein and may contribute to the defense against retroviral infections. {ECO:0000250|UniProtKB:Q9BYJ4}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BYJ4}. SUBUNIT: Homotrimer. Interacts (via B-box and SPRY domain) with TRIM5. {ECO:0000250|UniProtKB:Q9BYJ4}. +Q62247 SOX16_MOUSE Protein SOX-16 (Fragment) 57 6,932 Chain (1); DNA binding (1); Non-terminal residue (2) SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}. +Q8BIH0 SP130_MOUSE Histone deacetylase complex subunit SAP130 (130 kDa Sin3-associated polypeptide) (Sin3-associated polypeptide p130) 1057 111,228 Alternative sequence (3); Chain (1); Compositional bias (3); Cross-link (3); Erroneous initiation (1); Modified residue (7); Region (1); Sequence conflict (1) FUNCTION: Acts as a transcriptional repressor. May function in the assembly and/or enzymatic activity of the mSin3A corepressor complex or in mediating interactions between the complex and other regulatory complexes (By similarity). {ECO:0000250}. PTM: Acetylated. {ECO:0000250}.; PTM: Sumoylated with SUMO1. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of a mSin3A corepressor complex that contains SIN3A, SAP130, SUDS3/SAP45, ARID4B/SAP180, HDAC1 and HDAC2 (By similarity). Interacts (released by dead or dying cells) with CLEC4E. {ECO:0000250, ECO:0000269|PubMed:18776906}. DOMAIN: The N-terminus may interact with a transcriptional coactivator. {ECO:0000250}.; DOMAIN: The C-terminus may interact with HDAC-dependent and HDAC-independent corepressors. {ECO:0000250}. +Q920B9 SP16H_MOUSE FACT complex subunit SPT16 (Chromatin-specific transcription elongation factor 140 kDa subunit) (FACT 140 kDa subunit) (FACTp140) (Facilitates chromatin transcription complex subunit SPT16) 1047 119,825 Chain (1); Coiled coil (1); Compositional bias (2); Cross-link (3); Erroneous initiation (1); Initiator methionine (1); Modified residue (18); Sequence conflict (2) FUNCTION: Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II. The FACT complex is probably also involved in phosphorylation of 'Ser-392' of p53/TP53 via its association with CK2 (casein kinase II). {ECO:0000250|UniProtKB:Q9Y5B9, ECO:0000269|PubMed:23364797}. PTM: ADP-ribosylated. ADP-ribosylation by PARP1 is induced by genotoxic stress and correlates with dissociation of FACT from chromatin. SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Colocalizes with RNA polymerase II on chromatin. Recruited to actively transcribed loci. SUBUNIT: Interacts with MYOG (via C-terminal region) (PubMed:23364797). Component of the FACT complex, a stable heterodimer of SSRP1 and SUPT16H. Also component of a CK2-SPT16-SSRP1 complex which forms following UV irradiation, composed of SSRP1, SUPT16H, CSNK2A1, CSNK2A2 and CSNK2B. Interacts with NEK9. Binds to histone H2A-H2B. Identified in a centromere complex containing histones H2A, H2B and H4, and at least CENPA, CENPB, CENPC, CENPT, CENPN, HJURP, SUPT16H, SSRP1 and RSF1. Interacts with GTF2E2 (By similarity). {ECO:0000250|UniProtKB:Q9Y5B9, ECO:0000269|PubMed:23364797}. DOMAIN: The C-terminal Glu-rich acidic region is essential for FACT activity. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. Expressed in brain, liver, heart, kidneys, lungs, spleen, thymus, ovary, and testes, with highest levels of expression observed in thymus. {ECO:0000269|PubMed:11471063}. +P48432 SOX2_MOUSE Transcription factor SOX-2 319 34,454 Chain (1); Compositional bias (1); Cross-link (1); DNA binding (1); Helix (3); Modified residue (1); Mutagenesis (1); Sequence conflict (3) FUNCTION: Transcription factor that forms a trimeric complex with OCT4 on DNA and controls the expression of a number of genes involved in embryonic development such as YES1, FGF4, UTF1 and ZFP206. Critical for early embryogenesis and for embryonic stem cell pluripotency. May function as a switch in neuronal development. Downstream SRRT target that mediates the promotion of neural stem cell self-renewal. Keeps neural cells undifferentiated by counteracting the activity of proneural proteins and suppresses neuronal differentiation (By similarity). {ECO:0000250, ECO:0000269|PubMed:17097055, ECO:0000269|PubMed:22198669}. PTM: Sumoylation inhibits binding on DNA and negatively regulates the FGF4 transactivation. {ECO:0000269|PubMed:17097055}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267, ECO:0000269|PubMed:17097055}. SUBUNIT: Interacts with ZSCAN10. Interacts with SOX3 and FGFR1. {ECO:0000269|PubMed:17728342, ECO:0000269|PubMed:19740739}. TISSUE SPECIFICITY: Expressed in the brain and retina. A very low level expression is seen in the stomach and lung. Expressed in developing urogenital ridge. +Q4KL71 SP2A3_MOUSE Small proline-rich protein 2A3 83 9,408 Chain (1); Region (1); Repeat (5) FUNCTION: Cross-linked envelope protein of keratinocytes. It is a keratinocyte protein that first appears in the cell cytosol, but ultimately becomes cross-linked to membrane proteins by transglutaminase. All that results in the formation of an insoluble envelope beneath the plasma membrane (By similarity). {ECO:0000250|UniProtKB:P35324}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P35324}. +Q62445 SP4_MOUSE Transcription factor Sp4 782 81,906 Chain (1); Compositional bias (4); Modified residue (1); Sequence conflict (2); Zinc finger (3) FUNCTION: Binds to GT and GC boxes promoters elements. Probable transcriptional activator. Required for normal male reproductive behavior. SUBCELLULAR LOCATION: Nucleus. TISSUE SPECIFICITY: Expressed in many tissues. +Q91WP6 SPA3N_MOUSE Serine protease inhibitor A3N (Serpin A3N) 418 46,718 Beta strand (17); Chain (1); Glycosylation (3); Helix (12); Region (1); Sequence conflict (1); Signal peptide (1); Site (1); Turn (4) SUBCELLULAR LOCATION: Secreted {ECO:0000250}. DOMAIN: The reactive center loop (RCL) extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site within the RCL, establishing a covalent linkage between the serpin reactive site and the protease. The resulting inactive serpin-protease complex is highly stable (By similarity). Variability within the reactive center loop (RCL) sequences of Serpina3 paralogs may determine target protease specificity. {ECO:0000250}. TISSUE SPECIFICITY: Expressed at high levels in brain, heart, liver, lung, spleen, testis and thymus, and at low levels in bone marrow, kidney and skeletal muscle. {ECO:0000269|PubMed:15638460, ECO:0000269|PubMed:1718822}. +Q80ZX8 SPAG1_MOUSE Sperm-associated antigen 1 (Infertility-related sperm protein Spag-1) (TPR-containing protein involved in spermatogenesis) (TPIS) 901 100,670 Alternative sequence (2); Chain (1); Erroneous initiation (1); Modified residue (6); Nucleotide binding (1); Repeat (8); Sequence conflict (6) FUNCTION: May play a role in the cytoplasmic assembly of the ciliary dynein arms (By similarity). May play a role in fertilization. Binds GTP and has GTPase activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. TISSUE SPECIFICITY: Detected in cerebellum, tongue, esophagus, forestomach, sperm and testis. {ECO:0000269|PubMed:10527845}. +A0A1B0GSZ0 SPAR_MOUSE Small regulatory polypeptide of amino acid response 75 8,470 Chain (1); Topological domain (2); Transmembrane (1) TRANSMEM 4 24 Helical. {ECO:0000255}. TOPO_DOM 1 3 Lumenal. {ECO:0000250|UniProtKB:A0A1B0GVQ0}.; TOPO_DOM 25 75 Cytoplasmic. {ECO:0000250|UniProtKB:A0A1B0GVQ0}. FUNCTION: Negative regulator of amino acid sensing and mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels and amino acids (By similarity). Negatively regulates mTORC1 activation by inhibiting recruitment of mTORC1 to lysosomes upon stimulation with amino acids: acts by promoting the formation of a tightly bound supercomplex composed of the lysosomal V-ATPase, Ragulator and Rag GTPases, preventing recruitment of mTORC1 (By similarity). Acts as a regulator of muscle regeneration following injury by regulating mTORC1 activation (PubMed:28024296). {ECO:0000250|UniProtKB:A0A1B0GVQ0, ECO:0000269|PubMed:28024296}. SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250|UniProtKB:A0A1B0GVQ0}; Single-pass membrane protein {ECO:0000250|UniProtKB:A0A1B0GVQ0}. Lysosome membrane {ECO:0000250|UniProtKB:A0A1B0GVQ0}; Single-pass membrane protein {ECO:0000250|UniProtKB:A0A1B0GVQ0}. SUBUNIT: Interacts with components of the lysosomal V-ATPase complex (By similarity). Interacts with ATP6V0A1 (PubMed:28024296). Interacts with ATP6V0A2 (By similarity). {ECO:0000250|UniProtKB:A0A1B0GVQ0}. TISSUE SPECIFICITY: Expressed in the skeletal muscle. {ECO:0000269|PubMed:28024296}. +A2RRY8 SPAS1_MOUSE Spermatogenesis-associated serine-rich protein 1 (Dvl2-DEP domain-interacting protein) 269 30,169 Alternative sequence (2); Chain (1); Compositional bias (1); Modified residue (4); Sequence conflict (3) +Q8K3V1 SPAT4_MOUSE Spermatogenesis-associated protein 4 (Spermatogenesis-related gene 2 protein) (Testis and spermatogenesis cell-related protein 2) (Testis spermatocyte apoptosis-related gene 2 protein) 295 33,579 Chain (1); Domain (1) FUNCTION: May play a role in apoptosis regulation. {ECO:0000250|UniProtKB:Q8NEY3}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8NEY3}. TISSUE SPECIFICITY: Testis. {ECO:0000269|PubMed:12417927}. +Q80VP2 SPAT7_MOUSE Spermatogenesis-associated protein 7 homolog 582 65,655 Chain (1); Erroneous initiation (1) FUNCTION: Involved in photoreceptor cells maintenance (PubMed:25398945). It is required for recruitment and proper localization of RPGRIP1 to the photoreceptor connecting cilium (CC), as well as protein trafficking across the CC to the outer segments (PubMed:25398945). {ECO:0000269|PubMed:25398945}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q9P0W8}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q9P0W8}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9P0W8}. Note=Localizes to the microtubule network (By similarity). In the retinal photoreceptor cell layer, localizes at the connecting cilium (PubMed:25398945). {ECO:0000250|UniProtKB:Q9P0W8, ECO:0000269|PubMed:25398945}. SUBUNIT: Interacts with RPGRIP1 (PubMed:25398945). Found in a complex with CFAP410, NEK1 and SPATA7 (By similarity). Interacts with NEK1 (By similarity). {ECO:0000250|UniProtKB:Q9P0W8, ECO:0000269|PubMed:25398945}. TISSUE SPECIFICITY: Expressed in the retina (PubMed:19268277). Found in the photoreceptor cell layer, where localizes at the region between the inner segment and outer segment (PubMed:25398945). {ECO:0000269|PubMed:19268277, ECO:0000269|PubMed:25398945}. +Q9D9R3 SPAT9_MOUSE Spermatogenesis-associated protein 9 252 28,482 Alternative sequence (2); Chain (1); Compositional bias (1); Transmembrane (1) TRANSMEM 145 167 Helical. {ECO:0000255}. FUNCTION: May play at role in testicular development/spermatogenesis and may be an important factor in male infertility. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. +Q9D7P9 SPB12_MOUSE Serpin B12 423 47,835 Chain (1); Sequence conflict (1); Site (1) FUNCTION: Inhibits trypsin and plasmin, but not thrombin, coagulation factor Xa, or urokinase-type plasminogen activator. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +Q8VIG6 TRAIP_MOUSE E3 ubiquitin-protein ligase TRAIP (EC 2.3.2.27) (RING-type E3 ubiquitin transferase TRAIP) (TRAF-interacting protein) 470 53,149 Alternative sequence (2); Chain (1); Coiled coil (2); Mutagenesis (1); Region (1); Sequence conflict (4); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin ligase acting as a negative regulator of innate immune signaling. Inhibits activation of NF-kappa-B mediated by TNF. Negatively regulates TLR3/4- and RIG-I-mediated IRF3 activation and subsequent IFNB1 production and cellular antiviral response by promoting 'Lys-48'-linked polyubiquitination of TNK1 leading to its proteasomal degradation (By similarity) (PubMed:17544371, PubMed:22945920). Involved in response to genotoxic lesions during genome replication. Promotes H2AX and RPA2 phosphorylation after replication-associated DNA damage and assists fork progression at UV-induced replication-blocking lesions during S phase. Might also play a role in promoting translesion synthesis by mediating the assembly of 'Lys-63'-linked poly-ubiquitin chains on the Y-family polymerase POLN in order to facilitate bypass of DNA lesions and preserve genomic integrity. The function in translesion synthesis is controversial (By similarity). {ECO:0000250|UniProtKB:Q9BWF2, ECO:0000269|PubMed:17544371, ECO:0000269|PubMed:22945920}. PTM: Autoubiquitinated. {ECO:0000269|PubMed:17544371}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BWF2}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9BWF2}. Nucleus {ECO:0000250|UniProtKB:Q9BWF2}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9BWF2}. Note=In the nucleus, found in close proximity to PCNA, suggesting localization at replication foci. After UV irradiation, rapidly localizes to sites of DNA damage, where it colocalizes with phosphorylated histone H2AX (gamma-H2AX) and RPA2. {ECO:0000250|UniProtKB:Q9BWF2}. SUBUNIT: Interacts with POLK and POLN (By similarity). Binds TRAF1, TRAF2, TRAF3, TRAF5 and TRAF6 is part of the receptor-TRAF signaling complex. The C-terminus interacts with CYLD, however the interaction was not detected with the full-length protein (PubMed:17544371). {ECO:0000250, ECO:0000269|PubMed:17544371, ECO:0000269|PubMed:9104814}. TISSUE SPECIFICITY: Detected in testis and thymus, and at lower levels in spleen. +Q6PD31 TRAK1_MOUSE Trafficking kinesin-binding protein 1 (Protein Milton) 939 104,467 Alternative sequence (3); Chain (1); Coiled coil (2); Domain (1); Glycosylation (3); Modified residue (3); Region (2) FUNCTION: Involved in the regulation of endosome-to-lysosome trafficking, including endocytic trafficking of EGF-EGFR complexes and GABA-A receptors (By similarity). Involved in mitochondrial motility (PubMed:24995978). When O-glycosylated, abolishes mitochondrial motility. Crucial for recruiting OGT to the mitochondrial surface of neuronal processes (By similarity). TRAK1 and RHOT form an essential protein complex that links KIF5 to mitochondria for light chain-independent, anterograde transport of mitochondria (By similarity). {ECO:0000250|UniProtKB:Q960V3, ECO:0000250|UniProtKB:Q9UPV9, ECO:0000269|PubMed:24995978}. PTM: O-glycosylated (PubMed:24995978). Glycosylated by OGT; glycosylation in response to increased extracellular glucose levels is required for and leads to regulation of mitochondrial motility by OGT (By similarity). {ECO:0000250|UniProtKB:Q9UPV9, ECO:0000269|PubMed:24995978}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24995978}. Nucleus {ECO:0000250|UniProtKB:Q9UPV9}. Mitochondrion {ECO:0000250|UniProtKB:Q9UPV9}. Early endosome {ECO:0000250|UniProtKB:Q9UPV9}. Endosome {ECO:0000250|UniProtKB:Q9UPV9}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q9UPV9}. Cytoplasm, cell cortex {ECO:0000269|PubMed:24995978}. Note=Predominantly associated with early endosome. The localization to early endosomes depends on its interaction with HGS/HRS. Colocalizes with MGARP at the mitochondria. {ECO:0000250|UniProtKB:Q9UPV9}. SUBUNIT: Interacts with RHOT1 and RHOT2. Found in a complex with KIF5B, OGT, RHOT1 and RHOT2. Interacts with HGS (By similarity). Interacts with GABRA1 (PubMed:16380713). Interacts with KIF5C. Interacts with OGT; stable interaction is not required for glycosylation of this protein by OGT. Isoform 1 interacts with OGT (By similarity). {ECO:0000250|UniProtKB:Q9UPV9, ECO:0000269|PubMed:16380713}. TISSUE SPECIFICITY: Widely expressed with the greatest expression in brain, liver and kidney. Detected throughout the CNS, including the cortex, hippocamps, thalamus and various subcortical nuclei of the forebrain and midbrain, the granule of Purkinje layers of the cerebellum and the gray matter of the spinal cord. High level detected in lower moter neurons (at protein level). {ECO:0000269|PubMed:16380713}. DISEASE: Note=A spontaneous mutation (hyrt mice) causes a recessively transmitted form of hypertonia neurological dysfunction characterized by postural abnormalities, jerky movements and tremormutant. Hyrt mice have much lower levels of GABA(A) receptors in the CNS, particularly the lower motor neurons, than do wild-type mice, indicating that the hypertonicity of the mutants is likely to be caused by deficits in GABA-mediated motor neuron inhibition. {ECO:0000269|PubMed:16380713}. +Q91V04 TRAM1_MOUSE Translocating chain-associated membrane protein 1 374 43,039 Chain (1); Domain (1); Glycosylation (1); Modified residue (1); Mutagenesis (3); Topological domain (9); Transmembrane (8) TRANSMEM 30 50 Helical. {ECO:0000255}.; TRANSMEM 77 97 Helical. {ECO:0000255}.; TRANSMEM 122 142 Helical. {ECO:0000255}.; TRANSMEM 160 180 Helical. {ECO:0000255}.; TRANSMEM 193 213 Helical. {ECO:0000255}.; TRANSMEM 218 238 Helical. {ECO:0000255}.; TRANSMEM 252 272 Helical. {ECO:0000255}.; TRANSMEM 298 318 Helical. {ECO:0000255}. TOPO_DOM 1 29 Cytoplasmic. {ECO:0000305|PubMed:21237175}.; TOPO_DOM 51 76 Lumenal. {ECO:0000305|PubMed:21237175}.; TOPO_DOM 98 121 Cytoplasmic. {ECO:0000305|PubMed:21237175}.; TOPO_DOM 143 159 Lumenal. {ECO:0000305|PubMed:21237175}.; TOPO_DOM 181 192 Cytoplasmic. {ECO:0000305|PubMed:21237175}.; TOPO_DOM 214 217 Lumenal. {ECO:0000305|PubMed:21237175}.; TOPO_DOM 239 251 Cytoplasmic. {ECO:0000305|PubMed:21237175}.; TOPO_DOM 273 297 Lumenal. {ECO:0000305|PubMed:21237175}.; TOPO_DOM 319 374 Cytoplasmic. {ECO:0000305|PubMed:21237175}. FUNCTION: Stimulatory or required for the translocation of secretory proteins across the ER membrane. {ECO:0000250|UniProtKB:Q15629}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21237175}; Multi-pass membrane protein {ECO:0000255}. +Q9D083 SPC24_MOUSE Kinetochore protein Spc24 201 23,416 Alternative sequence (3); Chain (1); Coiled coil (1); Modified residue (1); Region (3) FUNCTION: Acts as a component of the essential kinetochore-associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity. Required for kinetochore integrity and the organization of stable microtubule binding sites in the outer plate of the kinetochore. The NDC80 complex synergistically enhances the affinity of the SKA1 complex for microtubules and may allow the NDC80 complex to track depolymerizing microtubules. {ECO:0000250|UniProtKB:Q8NBT2}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8NBT2}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q8NBT2}. Note=Localizes to kinetochores from late prophase to anaphase. Localizes specifically to the outer plate of the kinetochore. {ECO:0000250|UniProtKB:Q8NBT2}. SUBUNIT: Component of the NDC80 complex, which consists of NDC80/HEC1, CDCA1, SPBC24 and SPBC25. The NDC80 complex is formed by two subcomplexes composed of NDC80/HEC1-CDCA1 and SPBC24-SPBC25. Each subcomplex is formed by parallel interactions through the coiled-coil domains of individual subunits. Formation of a tetrameric complex is mediated by interactions between the C-terminal regions of both subunits of the NDC80/HEC1-CDCA1 subcomplex and the N-terminal regions of both subunits of the SPBC24-SPBC25 complex. The tetrameric NDC80 complex has an elongated rod-like structure with globular domains at either end (By similarity). {ECO:0000250}. +Q9D958 SPCS1_MOUSE Signal peptidase complex subunit 1 (EC 3.4.-.-) (Microsomal signal peptidase 12 kDa subunit) (SPase 12 kDa subunit) 161 18,186 Chain (1); Erroneous initiation (3); Sequence conflict (2); Topological domain (3); Transmembrane (2) TRANSMEM 86 106 Helical. {ECO:0000255}.; TRANSMEM 108 128 Helical. {ECO:0000255}. TOPO_DOM 1 85 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 107 107 Extracellular. {ECO:0000255}.; TOPO_DOM 129 161 Cytoplasmic. {ECO:0000255}. FUNCTION: Component of the microsomal signal peptidase complex which removes signal peptides from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum. {ECO:0000250}. SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Component of the microsomal signal peptidase complex which consists of five members: SEC11A, SEC11C, SPCS1, SPCS2 and SPCS3. {ECO:0000250}. +Q6P6M7 SPCS_MOUSE O-phosphoseryl-tRNA(Sec) selenium transferase (EC 2.9.1.2) (Selenocysteine synthase) (Sec synthase) (Selenocysteinyl-tRNA(Sec) synthase) (Sep-tRNA:Sec-tRNA synthase) (SepSecS) (UGA suppressor tRNA-associated protein) 504 55,326 Beta strand (16); Binding site (8); Chain (1); Helix (15); Modified residue (2); Mutagenesis (3); Region (2); Sequence conflict (1); Site (1); Turn (4) Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec) (archaeal/eukaryal route): step 2/2. FUNCTION: Converts O-phosphoseryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis. {ECO:0000250|UniProtKB:Q9HD40}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9HD40}. SUBUNIT: Homotetramer formed by a catalytic dimer and a non-catalytic dimer serving as a binding platform that orients tRNASec for catalysis. Each tetramer binds the CCA ends of two tRNAs which point to the active sites of the catalytic dimer (By similarity). {ECO:0000250|UniProtKB:Q9HD40, ECO:0000269|PubMed:18093968}. +Q6ZWQ7 SPCS3_MOUSE Signal peptidase complex subunit 3 (EC 3.4.-.-) (Microsomal signal peptidase 22/23 kDa subunit) (SPC22/23) (SPase 22/23 kDa subunit) 180 20,313 Chain (1); Glycosylation (1); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 12 32 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 11 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 33 180 Lumenal. {ECO:0000305}. FUNCTION: Component of the microsomal signal peptidase complex which removes signal peptides and other N-terminal peptides from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum. {ECO:0000250|UniProtKB:P61009}. SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250|UniProtKB:P61008}; Single-pass type II membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q12133}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q12133}. SUBUNIT: Component of the microsomal signal peptidase complex which consists of five members: SEC11A, SEC11C, SPCS1, SPCS2 and SPCS3. {ECO:0000250|UniProtKB:P61008}. +P15306 TRBM_MOUSE Thrombomodulin (TM) (Fetomodulin) (CD antigen CD141) 577 61,868 Chain (1); Disulfide bond (19); Domain (7); Glycosylation (5); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 518 541 Helical. {ECO:0000255}. TOPO_DOM 17 517 Extracellular. {ECO:0000255}.; TOPO_DOM 542 577 Cytoplasmic. {ECO:0000255}. FUNCTION: Thrombomodulin is a specific endothelial cell receptor that forms a 1:1 stoichiometric complex with thrombin. This complex is responsible for the conversion of protein C to the activated protein C (protein Ca). Once evolved, protein Ca scissions the activated cofactors of the coagulation mechanism, factor Va and factor VIIIa, and thereby reduces the amount of thrombin generated. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Interacts with ITGAL, ITGAM and ITGB2. {ECO:0000250|UniProtKB:P07204}. TISSUE SPECIFICITY: Endothelial cells are unique in synthesizing thrombomodulin. +Q9WTP3 SPDEF_MOUSE SAM pointed domain-containing Ets transcription factor (Prostate epithelium-specific Ets transcription factor) (Prostate-specific Ets) (Prostate-derived Ets factor) 325 36,356 Chain (1); DNA binding (1); Domain (1) FUNCTION: May function as an androgen-independent transactivator of the prostate-specific antigen (PSA) promoter. Binds to 5'-GGAT-3' DNA sequences. May play a role in the regulation of the prostate gland and/or prostate cancer development. Acts as a transcriptional activator for SERPINB5 promoter (By similarity). {ECO:0000250, ECO:0000269|PubMed:10675039}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Interacts with the DNA-binding domain of the androgen receptor. Interacts with NKX3-1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the accessory glands of sex organs including the prostate, seminal vesicle, coagulating gland in males, the oviduct in females, and in intestines. Expression is epithelial-specific. {ECO:0000269|PubMed:10675039}. +Q8BXJ2 TREF1_MOUSE Transcriptional-regulating factor 1 (Transcriptional-regulating protein 132) (Zinc finger transcription factor TReP-132) 1205 132,402 Alternative sequence (5); Chain (1); Compositional bias (3); Domain (2); Frameshift (1); Modified residue (6); Sequence conflict (9); Zinc finger (3) FUNCTION: Binds DNA and activates transcription of CYP11A1. Interaction with CREBBP and EP300 results in a synergistic transcriptional activation of CYP11A1. {ECO:0000250|UniProtKB:Q96PN7}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00512, ECO:0000255|PROSITE-ProRule:PRU00624}. SUBUNIT: Interacts with CREBBP and EP300. Interacts with DNTTIP1 and DNTT. {ECO:0000250|UniProtKB:Q96PN7}. TISSUE SPECIFICITY: Highly expressed in kidney, lung and brain. In the brain, expression was seen in the basal ganglia, hippocampus, piriform cortex, cerebral cortex, ventromedial nucleus of the hypothalamus and the dorsal and superior central nuclei of the raphe. {ECO:0000269|PubMed:12556907}. +Q9JKE1 TREM3_MOUSE Triggering receptor expressed on myeloid cells 3 (TREM-3) 183 20,452 Chain (1); Disulfide bond (1); Domain (1); Glycosylation (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 139 159 Helical. {ECO:0000255}. TOPO_DOM 20 138 Extracellular. {ECO:0000305}.; TOPO_DOM 160 183 Cytoplasmic. {ECO:0000305}. FUNCTION: Forms a receptor signaling complex with TYROBP/DAP12 which mediates activation of macrophages as part of the innate immune response. {ECO:0000269|PubMed:11754004}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11754004}; Single-pass type I membrane protein {ECO:0000255}. SUBUNIT: Interacts with TYROBP/DAP12. {ECO:0000269|PubMed:11754004}. TISSUE SPECIFICITY: Expressed in macrophages and in T-cells. {ECO:0000269|PubMed:11754004}. +Q8K4K2 TRIB3_MOUSE Tribbles homolog 3 (TRB-3) (Neuronal cell death-inducible putative kinase) 354 39,023 Chain (1); Domain (1); Region (1); Sequence conflict (4) FUNCTION: Disrupts insulin signaling by binding directly to Akt kinases and blocking their activation. May bind directly to and mask the 'Thr-308' phosphorylation site in AKT1. Binds to ATF4 and inhibits its transcriptional activation activity. Interacts with the NF-kappa-B transactivator p65 RELA and inhibits its phosphorylation and thus its transcriptional activation activity. Interacts with MAPK kinases and regulates activation of MAP kinases. May play a role in programmed neuronal cell death but does not appear to affect non-neuronal cells. Does not display kinase activity. Inhibits the transcriptional activity of DDIT3/CHOP and is involved in DDIT3/CHOP-dependent cell death during ER stress (By similarity). Can inhibit APOBEC3A editing of nuclear DNA. {ECO:0000250, ECO:0000269|PubMed:12749859, ECO:0000269|PubMed:12791994, ECO:0000269|PubMed:22977230}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12749859, ECO:0000269|PubMed:22977230}. SUBUNIT: Interacts with AKT1, AKT2, ATF4, MAP2K1 and MAP2K7. Interacts with DDIT3/CHOP and inhibits its interaction with EP300/P300 (By similarity). Interacts with APOBEC3C (By similarity). Interacts (via N-terminus) with APOBEC3A. {ECO:0000250, ECO:0000269|PubMed:12749859, ECO:0000269|PubMed:12791994, ECO:0000269|PubMed:22977230}. DOMAIN: The protein kinase domain is predicted to be catalytically inactive. TISSUE SPECIFICITY: Highly expressed in liver. Not detected in heart, brain, spleen, lung, skeletal muscle, kidney or testis. {ECO:0000269|PubMed:12749859}. +Q9ESN6 TRIM2_MOUSE Tripartite motif-containing protein 2 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRIM2) (Neural activity-related RING finger protein) (RING-type E3 ubiquitin transferase TRIM2) 744 81,445 Chain (1); Erroneous initiation (1); Modified residue (5); Repeat (7); Zinc finger (2) Protein modification; protein ubiquitination. FUNCTION: UBE2D1-dependent E3 ubiquitin-protein ligase that mediates the ubiquitination of NEFL and of phosphorylated BCL2L11. Plays a neuroprotective function. May play a role in neuronal rapid ischemic tolerance. {ECO:0000269|PubMed:18687884, ECO:0000269|PubMed:21478148}. PTM: RING-type zinc finger-dependent and UBE2D1-dependent autoubiquitination. {ECO:0000269|PubMed:18687884}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11432975}. SUBUNIT: Interacts with myosin V; myosin V may not be a substrate for ubiquitination. Interacts with NEFL. Interacts with phosphorylated BCL2L11. {ECO:0000269|PubMed:18687884, ECO:0000269|PubMed:21478148}. DOMAIN: The interaction with myosin V is dependent upon its NHL repeats, which form a beta-propeller (NHL) domain containing six blades. TISSUE SPECIFICITY: Highly expressed in the cerebellum, hippocampus, retina and spinal cord. In the cerebellum, strongest expression in Purkinje cells and in the deep cerebellar nuclei. In retina, high expression in the ganglionic cell layer, inner nuclear layer and inthe outer plexiform layer. Particularly high expression in the hippocampus, in pyramidal cells of CA1-CA3 hippocampal areas and ingranule cells of the dentate gyrus. {ECO:0000269|PubMed:11432975, ECO:0000269|PubMed:18687884}. +Q9D287 SPF27_MOUSE Pre-mRNA-splicing factor SPF27 (Breast carcinoma-amplified sequence 2 homolog) (DNA amplified in mammary carcinoma 1 protein) 225 26,131 Chain (1); Coiled coil (1); Compositional bias (1); Initiator methionine (1); Modified residue (2); Sequence conflict (3) FUNCTION: Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex. The PRP19-CDC5L complex may also play a role in the response to DNA damage (DDR). {ECO:0000250|UniProtKB:O75934}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:O75934}. SUBUNIT: Component of the PRP19-CDC5L splicing complex composed of a core complex comprising a homotetramer of PRPF19, CDC5L, PLRG1 and BCAS2, and at least three less stably associated proteins CTNNBL1, CWC15 and HSPA8. Interacts directly in the complex with PRPF19, CDC5L and PLRG1. {ECO:0000250|UniProtKB:O75934}. +Q3TFQ1 SPRY7_MOUSE SPRY domain-containing protein 7 (Chronic lymphocytic leukemia deletion region gene 6 protein homolog) (CLL deletion region gene 6 protein homolog) 196 21,681 Chain (1); Domain (1); Initiator methionine (1); Modified residue (1); Sequence conflict (5) +P97364 SPS2_MOUSE Selenide, water dikinase 2 (EC 2.7.9.3) (Selenium donor protein 2) (Selenophosphate synthase 2) 452 47,834 Active site (1); Chain (1); Compositional bias (2); Initiator methionine (1); Modified residue (2); Non-standard residue (1); Nucleotide binding (1); Site (1) FUNCTION: Synthesizes selenophosphate from selenide and ATP. +Q9D5L7 SPSB1_MOUSE SPRY domain-containing SOCS box protein 1 (SSB-1) 273 30,785 Alternative sequence (1); Chain (1); Domain (2); Modified residue (1); Sequence conflict (3) Protein modification; protein ubiquitination. FUNCTION: Substrate recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). Negatively regulates nitric oxide (NO) production and limits cellular toxicity in activated macrophages by mediating the ubiquitination and proteasomal degradation of NOS2 (By similarity). Acts as a bridge which links the NOS2 with the ECS E3 ubiquitin ligase complex components ELOC and CUL5 (By similarity). {ECO:0000250|UniProtKB:Q96BD6}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q96BD6}. Note=Exhibits a diffuse cytosolic localization. {ECO:0000250|UniProtKB:Q96BD6}. SUBUNIT: Component of the probable ECS(SPSB1) E3 ubiquitin-protein ligase complex which contains CUL5, RNF7/RBX2, Elongin BC complex and SPSB1 (By similarity). Interacts with CUL5, RNF7, ELOB and ELOC (By similarity). Directly interacts with MET tyrosine kinase domain in the presence and in the absence of HGF, however HGF treatment has a positive effect on this interaction (PubMed:16369487). When phosphorylated, interacts with RASA1 without affecting its stability (By similarity). Interacts (via B30.2/SPRY domain) with PAWR; this interaction is direct and occurs in association with the Elongin BC complex (PubMed:16369487, PubMed:16498413, PubMed:20561531).Interacts with EPHB2 (By similarity). Interacts with NOS2 (PubMed:20603330). {ECO:0000250|UniProtKB:Q96BD6, ECO:0000269|PubMed:16369487, ECO:0000269|PubMed:16498413, ECO:0000269|PubMed:20561531, ECO:0000269|PubMed:20603330}. DOMAIN: The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin ligase complexes (By similarity). Essential for its ability to link NOS2 and the ECS E3 ubiquitin ligase complex components ELOC and CUL5 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q96BD6}.; DOMAIN: The B30.2/SPRY domain is involved in MET and PAWR binding. {ECO:0000269|PubMed:16369487, ECO:0000269|PubMed:20561531}. +O88838 SPSB2_MOUSE SPRY domain-containing SOCS box protein 2 (SSB-2) (Gene-rich cluster protein C9) 264 28,938 Alternative sequence (1); Beta strand (15); Chain (1); Domain (2); Helix (5); Mutagenesis (14); Turn (3) Protein modification; protein ubiquitination. FUNCTION: Substrate recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:20603330). Negatively regulates nitric oxide (NO) production and limits cellular toxicity in activated macrophages by mediating the ubiquitination and proteasomal degradation of NOS2 (PubMed:20603330). Acts as a bridge which links NOS2 with the ECS E3 ubiquitin ligase complex components ELOC and CUL5 (By similarity). {ECO:0000250|UniProtKB:Q99619, ECO:0000269|PubMed:20603330}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q99619}. Note=Exhibits a diffuse cytosolic localization. {ECO:0000250|UniProtKB:Q99619}. SUBUNIT: Component of the probable ECS(SPSB2) E3 ubiquitin-protein ligase complex which contains CUL5, RNF7/RBX2, Elongin BC complex and SPSB2 (By similarity). Interacts with CUL5, RNF7, ELOB and ELOC (By similarity). Interacts with MET (PubMed:16369487). Interacts (via B30.2/SPRY domain) with PAWR; this interaction occurs in association with the Elongin BC complex (PubMed:16369487, PubMed:20561531). Interacts with NOS2. {ECO:0000250|UniProtKB:Q99619, ECO:0000269|PubMed:16369487, ECO:0000269|PubMed:20561531, ECO:0000269|PubMed:20603330}. DOMAIN: The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin ligase complexes (By similarity). Essential for its ability to link NOS2 and the ECS E3 ubiquitin ligase complex components ELOC and CUL5 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q99619}. +Q571F5 SPSB3_MOUSE SPRY domain-containing SOCS box protein 3 (SSB-3) 354 39,321 Alternative sequence (3); Chain (1); Domain (2); Erroneous initiation (1); Frameshift (1); Sequence conflict (2) Protein modification; protein ubiquitination. FUNCTION: May be a substrate recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000250}. SUBUNIT: Interacts with MET. {ECO:0000250}. DOMAIN: The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin ligase complexes. {ECO:0000250}. +Q8R5B6 SPSB4_MOUSE SPRY domain-containing SOCS box protein 4 (SSB-4) 273 30,286 Alternative sequence (1); Chain (1); Domain (2) Protein modification; protein ubiquitination. FUNCTION: Substrate recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). Negatively regulates nitric oxide (NO) production and limits cellular toxicity in activated macrophages by mediating the ubiquitination and proteasomal degradation of NOS2 (By similarity). Acts as a bridge which links NOS2 with the ECS E3 ubiquitin ligase complex components ELOC and CUL5 (By similarity). Diminishes EphB2-dependent cell repulsive responses by mediating the ubiquitination and degradation of the EphB2/CTF2 (By similarity). Regulates cellular clock function by mediating ubiquitination and proteasomal degradation of the circadian transcriptional repressor NR1D1 (By similarity). {ECO:0000250|UniProtKB:Q96A44}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q96A44}. Note=Exhibits a diffuse cytosolic localization. {ECO:0000250|UniProtKB:Q96A44}. SUBUNIT: Component of the probable ECS(SPSB4) E3 ubiquitin-protein ligase complex which contains CUL5, RNF7/RBX2, Elongin BC complex and SPSB4 (By similarity). Interacts with CUL5; RNF7; ELOB and ELOC (By similarity). Interacts with MET (PubMed:16369487). Interacts (via B30.2/SPRY domain) with PAWR; this interaction occurs in association with the Elongin BC complex (PubMed:16369487, PubMed:20561531). Interacts with NOS2 (PubMed:20603330). Interacts with EPHB2 (By similarity). {ECO:0000250|UniProtKB:Q96A44, ECO:0000269|PubMed:16369487, ECO:0000269|PubMed:20561531, ECO:0000269|PubMed:20603330}. DOMAIN: The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin ligase complexes (By similarity). Essential for its ability to link NOS2 and the ECS E3 ubiquitin ligase complex components ELOC and CUL5 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q96A44}. +Q9DA57 SPT25_MOUSE Spermatogenesis-associated protein 25 (Testis-specific gene 23 protein) 226 23,548 Chain (1); Sequence conflict (1); Transmembrane (1) TRANSMEM 153 173 Helical. {ECO:0000255}. FUNCTION: May play a role in spermatogenesis. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed strongly in testis, weakly in epididymis and not detected in other tissues. {ECO:0000269|PubMed:19240080}. +Q68FG3 SPT2_MOUSE Protein SPT2 homolog (SPT2 domain-containing protein 1) 682 74,818 Chain (1); Coiled coil (2); Compositional bias (3); Cross-link (2); Modified residue (3); Region (2); Sequence conflict (1) FUNCTION: Histone chaperone that stabilizes pre-existing histone tetramers and regulates replication-independent histone exchange on chromatin. Required for normal chromatin refolding in the coding region of transcribed genes, and for the suppression of spurious transcription. Binds DNA and histones and promotes nucleosome assembly (in vitro). Facilitates formation of tetrameric histone complexes containing histone H3 and H4 (By similarity). Modulates RNA polymerase 1-mediated transcription (By similarity). Binds DNA, with a preference for branched DNA species, such as Y-form DNA and Holliday junction DNA (By similarity). {ECO:0000250|UniProtKB:E1BUG7, ECO:0000250|UniProtKB:Q68D10}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:E1BUG7}. SUBUNIT: Interacts with histones. Interacts with a heterotetrameric complex formed by histone H3 and H4, especially when the histone tetramer is not bound to DNA. {ECO:0000250|UniProtKB:Q68D10}. DOMAIN: The acidic C-terminal domain mediates interaction with histone H3/H4 complexes. {ECO:0000250|UniProtKB:Q68D10}. +O55201 SPT5H_MOUSE Transcription elongation factor SPT5 (DRB sensitivity-inducing factor large subunit) (DSIF large subunit) 1082 120,664 Alternative sequence (1); Chain (1); Compositional bias (1); Cross-link (2); Domain (5); Erroneous initiation (1); Modified residue (20); Region (4); Repeat (19); Sequence conflict (8) FUNCTION: Component of the DRB sensitivity-inducing factor complex (DSIF complex), which regulates mRNA processing and transcription elongation by RNA polymerase II. DSIF positively regulates mRNA capping by stimulating the mRNA guanylyltransferase activity of RNGTT/CAP1A. DSIF also acts cooperatively with the negative elongation factor complex (NELF complex) to enhance transcriptional pausing at sites proximal to the promoter. Transcriptional pausing may facilitate the assembly of an elongation competent RNA polymerase II complex. DSIF and NELF promote pausing by inhibition of the transcription elongation factor TFIIS/S-II. TFIIS/S-II binds to RNA polymerase II at transcription pause sites and stimulates the weak intrinsic nuclease activity of the enzyme. Cleavage of blocked transcripts by RNA polymerase II promotes the resumption of transcription from the new 3' terminus and may allow repeated attempts at transcription through natural pause sites (By similarity). {ECO:0000250}. PTM: Methylated by PRMT1/HRMT1L2 and PRMT5/SKB1. Methylation negatively regulates interaction with P-TEFb and RNA polymerase II (By similarity). {ECO:0000250}.; PTM: Phosphorylated by CDK7 and CDK9. Phosphorylation by P-TEFb alleviates transcriptional pausing. Phosphorylation may also stimulate interaction with PIN1. Bulk phosphorylation occurs predominantly in mitosis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with SUPT4H1 to form DSIF. DSIF interacts with the positive transcription elongation factor b complex (P-TEFb complex), which is composed of CDK9 and cyclin-T (CCNT1 or CCNT2). DSIF interacts with RNA polymerase II, and this interaction is reduced by phosphorylation of the C-terminal domain (CTD) of POLR2A by P-TEFb. DSIF also interacts with the NELF complex, which is composed of NELFA, NELFB, NELFD and NELFE, and this interaction occurs following prior binding of DSIF to RNA polymerase II. Also interacts with PRMT1/HRMT1L2, HTATSF1/TATSF1, RNGTT/CAP1A, PRMT5/SKB1, SUPT6H, and can interact with PIN1. Component of a complex which is at least composed of HTATSF1/Tat-SF1, the P-TEFb complex components CDK9 and CCNT1, RNA polymerase II, SUPT5H, and NCL/nucleolin (By similarity). {ECO:0000250}. +P15508 SPTB1_MOUSE Spectrin beta chain, erythrocytic (Beta-I spectrin) 2128 245,250 Chain (1); Domain (2); Modified residue (12); Region (1); Repeat (17) FUNCTION: Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cell cortex. SUBUNIT: Composed of nonhomologous chains, alpha and beta, which aggregate to form dimers, tetramers, and higher polymers. +O35704 SPTC1_MOUSE Serine palmitoyltransferase 1 (EC 2.3.1.50) (Long chain base biosynthesis protein 1) (LCB 1) (Serine-palmitoyl-CoA transferase 1) (SPT 1) (SPT1) 473 52,535 Chain (1); Modified residue (1); Sequence conflict (7); Topological domain (2); Transmembrane (1) TRANSMEM 16 36 Helical. {ECO:0000255}. TOPO_DOM 1 15 Lumenal. {ECO:0000255}.; TOPO_DOM 37 473 Cytoplasmic. {ECO:0000255}. Lipid metabolism; sphingolipid metabolism. FUNCTION: Serine palmitoyltransferase (SPT). The heterodimer formed with SPTLC2 or SPTLC3 constitutes the catalytic core. The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference. The SPTLC1-SPTLC2-SPTSSA complex shows a strong preference for C16-CoA substrate, while the SPTLC1-SPTLC3-SPTSSA isozyme uses both C14-CoA and C16-CoA as substrates. The SPTLC1-SPTLC2-SPTSSB complex displays a strong preference for C18-CoA substrate, while the SPTLC1-SPTLC3-SPTSSB isozyme has the ability to use a broader range of acyl-CoAs (By similarity). {ECO:0000250}. PTM: Phosphorylation at Tyr-164 inhibits activity and promotes cell survival. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:1317856}; Single-pass membrane protein {ECO:0000269|PubMed:1317856}. SUBUNIT: Heterodimer with SPTLC2 or SPTLC3. Component of the serine palmitoyltransferase (SPT) complex, composed of SPTLC1, either SPTLC2 or SPTLC3, and either SPTSSA or SPTSSB. Interacts with SPTSSA and SPTSSB; the interaction is direct. Interacts with ORMDL3 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in a variety of tissues. Highest expression in brain, kidney and liver. +Q9QXV9 SPY1_MOUSE Protein sprouty homolog 1 (Spry-1) 313 34,004 Chain (1); Compositional bias (2); Domain (1); Modified residue (1) FUNCTION: May function as an antagonist of fibroblast growth factor (FGF) pathways and may negatively modulate respiratory organogenesis. SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein. Note=Found in the cytoplasm in unstimulated cells but is translocated to the membrane ruffles in cells stimulated with EGF (epidermal growth factor). DOMAIN: The Cys-rich domain is responsible for the localization of the protein to the membrane ruffles. TISSUE SPECIFICITY: Expressed in the embryo and adult tissues including heart, brain, lung, kidney, and skeletal muscle. +Q9QXV8 SPY2_MOUSE Protein sprouty homolog 2 (Spry-2) 315 34,623 Chain (1); Compositional bias (2); Domain (1); Sequence conflict (1); Site (1) FUNCTION: May function as an antagonist of fibroblast growth factor (FGF) pathways and may negatively modulate respiratory organogenesis. PTM: Cleaved at Pro-143 by the prolyl endopeptidase FAP (seprase) activity (in vitro). {ECO:0000250|UniProtKB:O43597}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell projection, ruffle membrane. Note=Associated with microtubules in unstimulated cells but is translocated to the membrane ruffles in cells stimulated ith EGF (epidermal growth factor). SUBUNIT: Interacts with RAF1. Part of a tripartite complex containing GAB1, METTL13 and SPRY2. Interacts with METTL13. {ECO:0000250|UniProtKB:O43597}. DOMAIN: The Cys-rich domain is responsible for the localization of the protein to the membrane ruffles. TISSUE SPECIFICITY: In adult, highly expressed in brain, lung, heart and at lower levels in skeletal muscle and kidney. In embryo, highly expressed in lung epithelial cells, primarily in the distal airways. +Q9WTP2 SPY4_MOUSE Protein sprouty homolog 4 (Spry-4) 300 32,523 Chain (1); Compositional bias (2); Domain (1); Modified residue (2); Sequence conflict (1) FUNCTION: Suppresses the insulin receptor and EGFR-transduced MAPK signaling pathway, but does not inhibit MAPK activation by a constitutively active mutant Ras. Probably impairs the formation of GTP-Ras (By similarity). Inhibits Ras-independent, but not Ras-dependent, activation of RAF1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein. Note=Found in the cytoplasm in unstimulated cells but is translocated to the membrane ruffles in cells stimulated with EGF (epidermal growth factor). SUBUNIT: Interacts with the C-terminus of TESK1. Interacts with RAF1. {ECO:0000250}. DOMAIN: The Cys-rich domain is responsible for the localization of the protein to the membrane ruffles. TISSUE SPECIFICITY: Expressed in the embryo and adult tissues including heart, brain, lung, kidney, and skeletal muscle. +Q64337 SQSTM_MOUSE Sequestosome-1 (STONE14) (Ubiquitin-binding protein p62) 442 48,163 Alternative sequence (1); Chain (1); Compositional bias (1); Cross-link (1); Domain (2); Helix (4); Initiator methionine (1); Modified residue (18); Motif (2); Mutagenesis (3); Region (7); Turn (2); Zinc finger (1) FUNCTION: Autophagy receptor required for selective macroautophagy (aggrephagy). Functions as a bridge between polyubiquitinated cargo and autophagosomes. Interacts directly with both the cargo to become degraded and an autophagy modifier of the MAP1 LC3 family. Required both for the formation and autophagic degradation of polyubiquitin-containing bodies, called ALIS (aggresome-like induced structures) and links ALIS to the autophagic machinery. Involved in midbody ring degradation (By similarity). May regulate the activation of NFKB1 by TNF-alpha, nerve growth factor (NGF) and interleukin-1. May play a role in titin/TTN downstream signaling in muscle cells. May regulate signaling cascades through ubiquitination. Adapter that mediates the interaction between TRAF6 and CYLD (PubMed:14960283, PubMed:18382763). May be involved in cell differentiation, apoptosis, immune response and regulation of K(+) channels. Involved in endosome organization by retaining vesicles in the perinuclear cloud: following ubiquitination by RNF26, attracts specific vesicle-associated adapters, forming a molecular bridge that restrains cognate vesicles in the perinuclear region and organizes the endosomal pathway for efficient cargo transport (By similarity). {ECO:0000250|UniProtKB:O08623, ECO:0000250|UniProtKB:Q13501, ECO:0000269|PubMed:14960283, ECO:0000269|PubMed:18382763}. PTM: Phosphorylated. May be phosphorylated by PRKCZ. Phosphorylated in vitro by TTN (By similarity). Phosphorylation at Ser-405 by ULK1 is stimulated by SESN2 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q13501}.; PTM: Ubiquitinated by RNF26: ubiquitinated SQSTM1 attracts specific vesicle-associated adapters, forming a molecular bridge that restrains cognate vesicles in the perinuclear region and organizes the endosomal pathway for efficient cargo transport. Deubiquitination by USP15 releases target vesicles for fast transport into the cell periphery. {ECO:0000250|UniProtKB:Q13501}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:16286508, ECO:0000269|PubMed:22792322}. Late endosome {ECO:0000269|PubMed:16286508}. Nucleus {ECO:0000269|PubMed:16286508}. Endoplasmic reticulum {ECO:0000269|PubMed:16286508}. Lysosome {ECO:0000250}. Cytoplasmic vesicle, autophagosome {ECO:0000250}. Nucleus, PML body {ECO:0000250|UniProtKB:Q13501}. Cytoplasm, myofibril, sarcomere. Note=In cardiac muscles, localizes to the sarcomeric band. May also localize to the hepatocellular carcinoma. Colocalizes with TRIM13 in the perinuclear endoplasmic reticulum (By similarity). Commonly found in inclusion bodies containing polyubiquitinated protein aggregates (By similarity). Co-localizes with TRIM5 in the cytoplasmic bodies (By similarity). When nuclear export is blocked by treatment with leptomycin B, accumulates in PML bodies (By similarity). {ECO:0000250|UniProtKB:Q13501}. SUBUNIT: Homooligomer or heterooligomer; may form homotypic arrays. Interacts directly with PRKCI and PRKCZ (Probable). Interacts with EBI3, LCK, RASA1, PRKCZ, PRKCI, NR2F2, NTRK1, NTRK2, NTRK3, NBR1, MAP2K5, TRIM13, TRIM55 and MAPKAPK5. Interacts with the proteasome subunits PSMD4 and PSMC2. Interacts with K63-polyubiquitinated MAPT/TAU. Interacts with IKBKB through PRKCZ and PRKCI. Interacts with NGFR through TRAF6 and bridges that complex to NTRK1. Forms a complex with MAP2K5 and PRKCZ or PRKCI. Component of a ternary complex with PAWR and PRKCZ. Upon TNF-alpha stimulation, interacts with RIPK1 probably bridging IKBKB to the TNF-R1 complex composed of TNF-R1/TNFRSF1A, TRADD and RIPK1. Forms a complex with AJUBA, PRKCZ and TRAF6. Forms ternary complexes with PRKCZ and KCNAB2 or PRKCZ and GABBR3. Interacts with KCNAB1, GABRR1, GABRR2 and GABRR3. Forms an NGF-induced complex with IKBKB, PRKCI and TRAF6. Identified in a heterotrimeric complex with ubiquitin and ZFAND5, where ZFAND5 and SQSTM1 both interact with the same ubiquitin molecule (By similarity). Interacts with TRAF6 and CYLD. Identified in a complex with TRAF6 and CYLD. Directly interacts with MAP1LC3A and MAP1LC3B, as well as with other MAP1 LC3 family members, including GABARAP, GABARAPL1 and GABARAPL2; these interactions are necessary for the recruitment MAP1 LC3 family members to inclusion bodies containing polyubiquitinated protein aggregates and for their degradation by autophagy (By similarity). Interacts with FHOD3 (By similarity). Interacts with TRMI5 (By similarity). Interacts with SESN1 (By similarity). Interacts with SESN2 (PubMed:25040165). Interacts with ULK1 (PubMed:25040165). Interacts with UBD (By similarity). Interacts with WDR81; the interaction is direct and regulates the interaction of SQSTM1 with ubiquitinated proteins (By similarity). Interacts with WDFY3; this interaction is required to recruit WDFY3 to cytoplasmic bodies and to PML bodies (By similarity). Interacts with TRIM23 (By similarity). Interacts with LRRC25. Interacts with TRIM50 (PubMed:22792322). Interacts with TRIM16 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q13501, ECO:0000269|PubMed:22792322, ECO:0000269|PubMed:25040165, ECO:0000305}. DOMAIN: The UBA domain binds specifically 'Lys-63'-linked polyubiquitin chains of polyubiquitinated substrates. Mediates the interaction with TRIM55. Both the UBA and PB1 domains are necessary and sufficient for the localization into the ubiquitin-containing inclusion bodies. {ECO:0000250|UniProtKB:Q13501}.; DOMAIN: The PB1 domain mediates homooligomerization and interactions with FHOD3, MAP2K5, NBR1, PRKCI, PRKCZ and WDR81. Both the PB1 and UBA domains are necessary and sufficient for the localization into the ubiquitin-containing inclusion bodies. {ECO:0000250|UniProtKB:Q13501}.; DOMAIN: The ZZ-type zinc finger mediates the interaction with RIPK1. {ECO:0000250|UniProtKB:Q13501}.; DOMAIN: The LIR (LC3-interacting region) motif mediates the interaction with ATG8 family proteins. {ECO:0000250|UniProtKB:Q13501}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10458914}. +Q9R112 SQOR_MOUSE Sulfide:quinone oxidoreductase, mitochondrial (SQOR) (EC 1.8.5.-) (Sulfide quinone oxidoreductase) 450 50,282 Active site (2); Chain (1); Modified residue (3); Nucleotide binding (1); Sequence conflict (5); Transit peptide (1) FUNCTION: Catalyzes the oxidation of hydrogen sulfide with the help of a quinone, such as ubiquinone, giving rise to thiosulfate and ultimately to sulfane (molecular sulfur) atoms. Requires an additional electron acceptor; can use sulfite, sulfide or cyanide (in vitro). {ECO:0000250|UniProtKB:Q9Y6N5}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9Y6N5}. +Q6NV83 SR140_MOUSE U2 snRNP-associated SURP motif-containing protein (140 kDa Ser/Arg-rich domain protein) (U2-associated protein SR140) 1029 118,261 Alternative sequence (2); Chain (1); Coiled coil (3); Compositional bias (5); Cross-link (9); Domain (2); Initiator methionine (1); Modified residue (13); Repeat (1); Sequence conflict (3) SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with ERBB4. {ECO:0000250}. +Q4V9W2 SR1IP_MOUSE Protein SREK1IP1 (SFRS12-interacting protein 1) (SREK1-interacting protein 1) 153 18,151 Alternative sequence (1); Chain (1); Compositional bias (1); Erroneous termination (1); Modified residue (3); Sequence caution (1); Sequence conflict (2); Zinc finger (1) FUNCTION: Possible splicing regulator involved in the control of cellular survival. {ECO:0000250}. SUBUNIT: Interacts with SREK1/SFRS12. {ECO:0000250}. +Q60598 SRC8_MOUSE Src substrate cortactin 546 61,250 Beta strand (5); Chain (1); Coiled coil (1); Cross-link (6); Domain (1); Helix (1); Modified residue (27); Mutagenesis (4); Repeat (7); Sequence conflict (2) FUNCTION: Contributes to the organization of the actin cytoskeleton and cell shape (PubMed:17403031). Plays a role in the formation of lamellipodia and in cell migration (By similarity). Plays a role in the regulation of neuron morphology, axon growth and formation of neuronal growth cones (By similarity). Through its interaction with CTTNBP2, involved in the regulation of neuronal spine density (PubMed:22262902). Plays a role in the invasiveness of cancer cells, and the formation of metastases (By similarity). Plays a role in focal adhesion assembly and turnover (By similarity). In complex with ABL1 and MYLK regulates cortical actin-based cytoskeletal rearrangement critical to sphingosine 1-phosphate (S1P)-mediated endothelial cell (EC) barrier enhancement (By similarity). Plays a role in intracellular protein transport and endocytosis, and in modulating the levels of potassium channels present at the cell membrane (PubMed:17959782). Plays a role in receptor-mediated endocytosis via clathrin-coated pits (By similarity). Required for stabilization of KCNH1 channels at the cell membrane (By similarity). {ECO:0000250|UniProtKB:Q14247, ECO:0000250|UniProtKB:Q66HL2, ECO:0000269|PubMed:17403031, ECO:0000269|PubMed:17959782, ECO:0000269|PubMed:22262902}. PTM: Phosphorylated by FER. Phosphorylated in response to FGR activation (PubMed:7693700). Phosphorylation by SRC promotes MYLK binding (By similarity). Phosphorylated on tyrosine residues in response to CHRM1 activation (By similarity). Phosphorylated by PTK2/FAK1 in response to cell adhesion (By similarity). Tyrosine phosphorylation in transformed cells may contribute to cellular growth regulation and transformation. Phosphorylated by PKN2 at both serine and threonine residues in a GTP-bound Rac1-dependent manner in hyaluronan-induced astrocytes and hence down-regulated CTTN ability to associate with filamentous actin. {ECO:0000250|UniProtKB:Q14247, ECO:0000250|UniProtKB:Q66HL2, ECO:0000269|PubMed:17403031, ECO:0000269|PubMed:22252131, ECO:0000269|PubMed:7693700}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell projection, lamellipodium. Cell projection, ruffle. Cytoplasm, cell cortex. Cell projection {ECO:0000250|UniProtKB:Q66HL2}. Cell projection, podosome {ECO:0000250|UniProtKB:Q01406}. Cell projection, dendritic spine {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cell membrane {ECO:0000250|UniProtKB:Q66HL2}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell junction {ECO:0000250|UniProtKB:Q66HL2}. Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:Q66HL2}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q66HL2}. Note=Colocalizes transiently with PTK2/FAK1 at focal adhesions (By similarity). Associated with membrane ruffles and lamellipodia. In the presence of CTTNBP2NL, colocalizes with stress fibers. In the presence of CTTNBP2, localizes at the cell cortex. In response to neuronal activation by glutamate, redistributes from dendritic spines to the dendritic shaft. Colocalizes with DNM2 at the basis of filopodia in hippocampus neuron growth zones (By similarity). {ECO:0000250|UniProtKB:Q14247, ECO:0000250|UniProtKB:Q66HL2}. SUBUNIT: Interacts with SHANK2 and SHANK3 (via its SH3 domain). Interacts with PLXDC2 and SRCIN1. Interacts with SAMSN1 (via SH3 domain). Interacts (via SH3 domain) with ASAP1 (via Pro-rich region). Interacts (via SH3 domain) with DNM2. Interacts with ACTN1 (By similarity). Interacts with FER. Forms a complex with ABL1 and MYLK (By similarity). Interacts with KCNA2 (via non-phosphorylated C-terminus). Interacts with FGD1. Identified in a complex containing FGFR4, NCAM1, CDH2, PLCG1, FRS2, SRC, SHC1, GAP43 and CTTN. Interacts with ABL2 (PubMed:22297987). Interacts with CTTNBP2NL; this interaction may target CTTN to stress fibers. Interacts with CTTNBP2; this interaction may target CTTN at the cell cortex or dendritic spines. Interacts with KCNH1 (By similarity). {ECO:0000250|UniProtKB:Q14247, ECO:0000250|UniProtKB:Q66HL2, ECO:0000269|PubMed:11433297, ECO:0000269|PubMed:12913069, ECO:0000269|PubMed:17959782, ECO:0000269|PubMed:22262902, ECO:0000269|PubMed:22297987, ECO:0000269|PubMed:23015759}. DOMAIN: The SH3 motif may mediate binding to the cytoskeleton. {ECO:0000305}. TISSUE SPECIFICITY: Expressed in most tissues, except in B-lymphocytes or plasma cells. +P59222 SREC2_MOUSE Scavenger receptor class F member 2 (Scavenger receptor expressed by endothelial cells 2 protein) (SREC-II) 833 87,871 Chain (1); Compositional bias (1); Disulfide bond (21); Domain (7); Glycosylation (4); Modified residue (7); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 434 454 Helical. {ECO:0000255}. TOPO_DOM 34 433 Extracellular. {ECO:0000255}.; TOPO_DOM 455 833 Cytoplasmic. {ECO:0000255}. FUNCTION: Probable adhesion protein, which mediates homophilic and heterophilic interactions. In contrast to SCARF1, it poorly mediates the binding and degradation of acetylated low density lipoprotein (Ac-LDL). SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Homophilic and heterophilic interaction via its extracellular domain. Interacts with SCARF1. The heterophilic interaction with SCARF1, which is stronger than the homophilic interaction with itself, is suppressed by the presence of SCARF1 ligand such as Ac-LDL. +Q8BZX4 SREK1_MOUSE Splicing regulatory glutamine/lysine-rich protein 1 (Serine/arginine-rich-splicing regulatory protein 86) (SRrp86) (Splicing factor, arginine/serine-rich 12) 494 56,763 Alternative sequence (1); Chain (1); Compositional bias (1); Cross-link (1); Domain (1); Modified residue (3); Sequence conflict (1) FUNCTION: Participates in the regulation of alternative splicing by modulating the activity of other splice facors. Inhibits the splicing activity of SFRS1, SFRS2 and SFRS6. Augments the splicing activity of SFRS3 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Homodimer. Binds SFRS1, SFRS2, SFRS3 and SFRS6. Interacts with the spliceosome. Interacts with SREK1IP1 (By similarity). {ECO:0000250}. +Q80YD6 SRGEF_MOUSE Secretion-regulating guanine nucleotide exchange factor (Deafness locus-associated putative guanine nucleotide exchange factor) (DelGEF) (Guanine nucleotide exchange factor-related protein) 464 49,226 Chain (1); Modified residue (1); Repeat (7); Sequence conflict (1) FUNCTION: Probable guanine nucleotide exchange factor (GEF), which may be involved in the secretion process. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Interacts with SEC5. The interaction occurs only in the presence of magnesium or manganese and is stimulated by dCTP or GTP (By similarity). {ECO:0000250}. +P05480 SRC_MOUSE Neuronal proto-oncogene tyrosine-protein kinase Src (EC 2.7.10.2) (Proto-oncogene c-Src) (pp60c-src) (p60-Src) 541 60,645 Active site (1); Beta strand (22); Binding site (1); Chain (1); Domain (3); Helix (20); Initiator methionine (1); Lipidation (1); Modified residue (7); Nucleotide binding (1); Sequence conflict (1); Turn (4) FUNCTION: Non-receptor protein tyrosine kinase which is activated following engagement of many different classes of cellular receptors including immune response receptors, integrins and other adhesion receptors, receptor protein tyrosine kinases, G protein-coupled receptors as well as cytokine receptors. Participates in signaling pathways that control a diverse spectrum of biological activities including gene transcription, immune response, cell adhesion, cell cycle progression, apoptosis, migration, and transformation. Due to functional redundancy between members of the SRC kinase family, identification of the specific role of each SRC kinase is very difficult. SRC appears to be one of the primary kinases activated following engagement of receptors and plays a role in the activation of other protein tyrosine kinase (PTK) families. Receptor clustering or dimerization leads to recruitment of SRC to the receptor complexes where it phosphorylates the tyrosine residues within the receptor cytoplasmic domains. Plays an important role in the regulation of cytoskeletal organization through phosphorylation of specific substrates such as AFAP1. Phosphorylation of AFAP1 allows the SRC SH2 domain to bind AFAP1 and to localize to actin filaments. Cytoskeletal reorganization is also controlled through the phosphorylation of cortactin (CTTN) (Probable). When cells adhere via focal adhesions to the extracellular matrix, signals are transmitted by integrins into the cell resulting in tyrosine phosphorylation of a number of focal adhesion proteins, including PTK2/FAK1 and paxillin (PXN) (By similarity). In addition to phosphorylating focal adhesion proteins, SRC is also active at the sites of cell-cell contact adherens junctions and phosphorylates substrates such as beta-catenin (CTNNB1), delta-catenin (CTNND1), and plakoglobin (JUP). Another type of cell-cell junction, the gap junction, is also a target for SRC, which phosphorylates connexin-43 (GJA1). SRC is implicated in regulation of pre-mRNA-processing and phosphorylates RNA-binding proteins such as KHDRBS1 (Probable). Also plays a role in PDGF-mediated tyrosine phosphorylation of both STAT1 and STAT3, leading to increased DNA binding activity of these transcription factors (PubMed:9344858). Involved in the RAS pathway through phosphorylation of RASA1 and RASGRF1. Plays a role in EGF-mediated calcium-activated chloride channel activation (By similarity). Required for epidermal growth factor receptor (EGFR) internalization through phosphorylation of clathrin heavy chain (CLTC and CLTCL1) at 'Tyr-1477'. Involved in beta-arrestin (ARRB1 and ARRB2) desensitization through phosphorylation and activation of GRK2, leading to beta-arrestin phosphorylation and internalization. Has a critical role in the stimulation of the CDK20/MAPK3 mitogen-activated protein kinase cascade by epidermal growth factor (Probable). Might be involved not only in mediating the transduction of mitogenic signals at the level of the plasma membrane but also in controlling progression through the cell cycle via interaction with regulatory proteins in the nucleus (By similarity). Plays an important role in osteoclastic bone resorption in conjunction with PTK2B/PYK2. Both the formation of a SRC-PTK2B/PYK2 complex and SRC kinase activity are necessary for this function. Recruited to activated integrins by PTK2B/PYK2, thereby phosphorylating CBL, which in turn induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function (PubMed:14739300). Promotes energy production in osteoclasts by activating mitochondrial cytochrome C oxidase (PubMed:12615910). Phosphorylates DDR2 on tyrosine residues, thereby promoting its subsequent autophosphorylation. Phosphorylates RUNX3 and COX2 on tyrosine residues, TNK2 on 'Tyr-284' and CBL on 'Tyr-738'. Enhances DDX58/RIG-I-elicited antiviral signaling. Phosphorylates PDPK1 at 'Tyr-9', 'Tyr-373' and 'Tyr-376'. Phosphorylates BCAR1 at 'Tyr-226'. Phosphorylates CBLC at multiple tyrosine residues, phosphorylation at 'Tyr-341' activates CBLC E3 activity. Involved in anchorage-independent cell growth (By similarity). Required for podosome formation (PubMed:21525037). {ECO:0000250|UniProtKB:P12931, ECO:0000269|PubMed:12615910, ECO:0000269|PubMed:14739300, ECO:0000269|PubMed:21525037, ECO:0000269|PubMed:8641341, ECO:0000269|PubMed:9344858, ECO:0000305|PubMed:11964124, ECO:0000305|PubMed:8672527, ECO:0000305|PubMed:9442882}. PTM: Myristoylated at Gly-2, and this is essential for targeting to membranes. {ECO:0000250}.; PTM: Dephosphorylated at Tyr-535 by PTPRJ (By similarity). Phosphorylated on Tyr-535 by c-Src kinase (CSK). The phosphorylated form is termed pp60c-src. Dephosphorylated by PTPRJ at Tyr-424. Normally maintained in an inactive conformation with the SH2 domain engaged with Tyr-535, the SH3 domain engaged with the SH2-kinase linker, and Tyr-424 dephosphorylated. Dephosphorylation of Tyr-535 as a result of protein tyrosine phosphatase (PTP) action disrupts the intramolecular interaction between the SH2 domain and Tyr-535, Tyr-424 can then become autophosphorylated, resulting in SRC activation. Phosphorylation of Tyr-535 by CSK allows this interaction to reform, resulting in SRC inactivation. CDK5-mediated phosphorylation at Ser-74 targets SRC to ubiquitin-dependent degradation and thus leads to cytoskeletal reorganization. Phosphorylated by PTK2/FAK1; this enhances kinase activity. Phosphorylated by PTK2B/PYK2; this enhances kinase activity (By similarity). {ECO:0000250}.; PTM: S-nitrosylation is important for activation of its kinase activity. {ECO:0000250}.; PTM: Ubiquitinated in response to CDK5-mediated phosphorylation. Ubiquitination mediated by CBLC requires SRC autophosphorylation at Tyr-424 and may lead to lysosomal degradation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12615910, ECO:0000269|PubMed:21525037}. Mitochondrion inner membrane {ECO:0000269|PubMed:12615910}. Nucleus {ECO:0000269|PubMed:12615910}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12615910}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P12931}. Note=Localizes to focal adhesion sites following integrin engagement. Localization to focal adhesion sites requires myristoylation and the SH3 domain. Colocalizes with PDLIM4 at the perinuclear region, but not at focal adhesions. {ECO:0000250|UniProtKB:P12931}. SUBUNIT: Interacts with CDCP1, PELP1, TGFB1I1 and TOM1L2 (By similarity). Interacts with DDEF1/ASAP1 via its SH3 domain (PubMed:9819391). Interacts with CCPG1 (PubMed:17000758). Interacts with the cytoplasmic domain of MUC1, phosphorylates it and increases binding of MUC1 with beta-catenin (By similarity). Interacts with RALGPS1 via its SH3 domain (By similarity). Interacts with CAV2 (tyrosine phosphorylated form) (By similarity). Interacts (via the SH3 domain and the protein kinase domain) with ARRB1; the interaction is independent of the phosphorylation state of SRC C-terminus (By similarity). Interacts with FCAMR and PXN (By similarity). Interacts with ARRB2 (PubMed:19122674). Interacts with ARRB1 (By similarity). Interacts with SRCIN1 (By similarity). Interacts with NDFIP2 and more weakly with NDFIP1 (By similarity). Interacts with PIK3CA and/or PIK3C2B, PTK2/FAK1, ESR1 (dimethylated on arginine) and FAK (PubMed:14739300). Interacts (via SH2 and SH3 domain) with TNK2 (By similarity). Interacts (via protein kinase domain) with the tyrosine phosphorylated form of RUNX3 (via runt domain) (By similarity). Interacts with TRAF3 (via RING-type zinc finger domain) (By similarity). Interacts with DDX58, MAVS and TBK1 (By similarity). Interacts (via SH2 domain) with RACK1; the interaction is enhanced by tyrosine phosphorylation of RACK1 and inhibits SRC activity (By similarity). Interacts (via SH2 domain) with the 'Tyr-402' phosphorylated form of PTK2B/PYK2 (PubMed:14739300). Interacts (via SH2 domain) with FLT3 (tyrosine phosphorylated) (PubMed:16684964). Identified in a complex containing FGFR4, NCAM1, CDH2, PLCG1, FRS2, SRC, SHC1, GAP43 and CTTN (PubMed:11433297). Interacts with EPHB1; activates the MAPK/ERK cascade to regulate cell migration (PubMed:12925710). Interacts with ERBB2 and STAT1 (PubMed:7542762, PubMed:9344858). Interacts with PDGFRA (tyrosine phosphorylated) (PubMed:14644164). Interacts with CSF1R (PubMed:7681396). Interacts (via SH2 domain) with the 'Tyr-9' phosphorylated form of PDPK1 (By similarity). Interacts with DDR2 (By similarity). Interacts with AMOTL2; this interaction regulates the translocation of phosphorylated SRC to peripheral cell-matrix adhesion sites (By similarity). Interacts with DDR1 and DAB2 (PubMed:20093046). Interacts with TRAP1 (By similarity). Interacts with CBLC; the interaction is enhanced when SRC is phosphorylated at 'Tyr-424' (By similarity). Interacts with ARHGEF5 (PubMed:21525037). Interacts (via cytoplasmic domain) with CEACAM1 (via SH2 domain); this interaction is regulated by trans-homophilic cell adhesion (By similarity). Interacts with MPP2 (By similarity). Interacts with PRR7 (By similarity). Interacts (via kinase domain and to a lesser extent the SH2 domain) directly with PDLIM4; this interaction results in PTPN13-mediated dephosphorylation of this protein leading to its inactivation (By similarity). {ECO:0000250|UniProtKB:P00523, ECO:0000250|UniProtKB:P12931, ECO:0000250|UniProtKB:Q9WUD9, ECO:0000269|PubMed:11433297, ECO:0000269|PubMed:12925710, ECO:0000269|PubMed:14644164, ECO:0000269|PubMed:14739300, ECO:0000269|PubMed:16684964, ECO:0000269|PubMed:17000758, ECO:0000269|PubMed:19122674, ECO:0000269|PubMed:20093046, ECO:0000269|PubMed:21525037, ECO:0000269|PubMed:7542762, ECO:0000269|PubMed:7681396, ECO:0000269|PubMed:9344858, ECO:0000269|PubMed:9819391}. +Q91Z67 SRGP2_MOUSE SLIT-ROBO Rho GTPase-activating protein 2 (srGAP2) (Formin-binding protein 2) (Formin-binding protein 27) (FBP-27) 1071 120,798 Chain (1); Coiled coil (2); Domain (3); Modified residue (14); Mutagenesis (2); Sequence conflict (5) FUNCTION: RAC1 GTPase activating protein (GAP) that binds and deforms membranes, and regulates actin dynamics to regulate cell migration and differentiation. Plays an important role in different aspects of neuronal morphogenesis and migration mainly during development of the cerebral cortex. This includes the biogenesis of neurites, where it is required for both axons and dendrites outgrowth, and the maturation of the dendritic spines. Also stimulates the branching of the leading process and negatively regulates neuron radial migration in the cerebral cortex. May play a role for cognition, learning and memory. In non-neuronal cells, it may also play a role in cell migration by regulating the formation of lamellipodia and filopodia. {ECO:0000269|PubMed:19737524, ECO:0000269|PubMed:22559944}. PTM: Methylation at Arg-927 is required for the stimulation of cell migration, dimerization and localization at the plasma membrane protrusions. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Cell projection, dendritic spine {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density. Cell junction, synapse, postsynaptic cell membrane. Cell projection, lamellipodium {ECO:0000250}. Cytoplasmic vesicle, phagosome. Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Recruited to actin-rich phagosomes during phagocytosis. Translocates from nucleus to cytoplasm during development (By similarity). {ECO:0000250}. SUBUNIT: Homodimer. Interacts with FASLG (By similarity). Interacts with PRMT5 (By similarity). Probably interacts with ROBO1 and ROBO2. Interacts with RAC1; specifically stimulates RAC1 GTPase activity. Interacts (via SH3 domain) with FMNL1 (activated by RAC1); regulates the actin filament severing activity of FMNL1. Interacts (via SH3 domain) with FMNL3. Interacts (via SH3 domain) with GPHN. {ECO:0000250, ECO:0000269|PubMed:19737524, ECO:0000269|PubMed:21148482, ECO:0000269|PubMed:22126966}. DOMAIN: The F-BAR domain mediates oligomerization, binds membranes, and induces plasma membrane protrusions. +Q8BMA6 SRP68_MOUSE Signal recognition particle subunit SRP68 (SRP68) (Signal recognition particle 68 kDa protein) 625 70,574 Chain (1); Compositional bias (1); Modified residue (3); Sequence conflict (2) FUNCTION: Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP68 binds the 7S RNA, SRP72 binds to this complex subsequently. This ribonucleoprotein complex might interact directly with the docking protein in the ER membrane and possibly participate in the elongation arrest function (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. SUBUNIT: Signal recognition particle consists of a 7S RNA molecule of 300 nucleotides and six protein subunits: SRP72, SRP68, SRP54, SRP19, SRP14 and SRP9. DOMAIN: The RNA-binding domain is located near the N-terminus. {ECO:0000250}. +P47758 SRPRB_MOUSE Signal recognition particle receptor subunit beta (SR-beta) 269 29,579 Beta strand (7); Binding site (2); Chain (1); Helix (7); Modified residue (2); Nucleotide binding (3); Sequence conflict (1); Transmembrane (1); Turn (1) TRANSMEM 35 55 Helical. {ECO:0000255}. FUNCTION: Component of the SRP (signal recognition particle) receptor. Ensures, in conjunction with the signal recognition particle, the correct targeting of the nascent secretory proteins to the endoplasmic reticulum membrane system. Has GTPase activity. May mediate the membrane association of SRPR. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. SUBUNIT: Heterodimer with SRPRA. {ECO:0000269|PubMed:16439358}. +O70551 SRPK1_MOUSE SRSF protein kinase 1 (EC 2.7.11.1) (SFRS protein kinase 1) (Serine/arginine-rich protein-specific kinase 1) (SR-protein-specific kinase 1) 648 73,088 Active site (1); Binding site (1); Chain (1); Domain (1); Modified residue (7); Nucleotide binding (1); Sequence conflict (4) FUNCTION: Serine/arginine-rich protein-specific kinase which specifically phosphorylates its substrates at serine residues located in regions rich in arginine/serine dipeptides, known as RS domains and is involved in the phosphorylation of SR splicing factors and the regulation of splicing. Plays a central role in the regulatory network for splicing, controlling the intranuclear distribution of splicing factors in interphase cells and the reorganization of nuclear speckles during mitosis. Can influence additional steps of mRNA maturation, as well as other cellular activities, such as chromatin reorganization in somatic and sperm cells and cell cycle progression. Phosphorylates SFRS2, ZRSR2, LBR and PRM1. Phosphorylates SRSF1 using a directional (C-terminal to N-terminal) and a dual-track mechanism incorporating both processive phosphorylation (in which the kinase stays attached to the substrate after each round of phosphorylation) and distributive phosphorylation steps (in which the kinase and substrate dissociate after each phosphorylation event). The RS domain of SRSF1 binds first to a docking groove in the large lobe of the kinase domain of SRPK1. This induces certain structural changes in SRPK1 and/or RRM2 domain of SRSF1, allowing RRM2 to bind the kinase and initiate phosphorylation. The cycles continue for several phosphorylation steps in a processive manner (steps 1-8) until the last few phosphorylation steps (approximately steps 9-12). During that time, a mechanical stress induces the unfolding of the beta-4 motif in RRM2, which then docks at the docking groove of SRPK1. This also signals RRM2 to begin to dissociate, which facilitates SRSF1 dissociation after phosphorylation is completed. Can mediate hepatitis B virus (HBV) core protein phosphorylation. It plays a negative role in the regulation of HBV replication through a mechanism not involving the phosphorylation of the core protein but by reducing the packaging efficiency of the pregenomic RNA (pgRNA) without affecting the formation of the viral core particles. Can induce splicing of exon 10 in MAPT/TAU (By similarity). {ECO:0000250, ECO:0000269|PubMed:10390541, ECO:0000269|PubMed:9446799}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Nucleus matrix {ECO:0000250}. Microsome {ECO:0000250}. Note=Shuttles between the nucleus and the cytoplasm. Inhibition of the Hsp90 ATPase activity, osmotic stress and interaction with HHV-1 ICP27 protein can induce its translocation to the nucleus. KAT5/TIP60 inhibits its nuclear translocation (By similarity). {ECO:0000250}. SUBUNIT: Monomer. Found in a multisubunit complex containing seven proteins, named toposome, which separates entangled circular chromatin DNA during chromosome segregation. Interacts with HHV-1 ICP27 protein. Interacts with DNAJC8 and AHSA1/AHA1 and this mediates formation of a complex with the Hsp70 /Hsp90 machinery. Binds to IGF2BP1, SYNCRIP, HNRNPA2B1 and HNRNPC. Interacts with SAFB/SAFB1 and SAFB2 which inhibits its activity (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Predominantly expressed in the testis but is also present at lower levels in heart, spleen, liver, brain, kidney, lung and skeletal muscle. Present in all germinal cells in the seminiferous tubules but not in mature spermatozoa. {ECO:0000269|PubMed:10390541, ECO:0000269|PubMed:9446799}. +Q80WV7 SRRM3_MOUSE Serine/arginine repetitive matrix protein 3 648 71,104 Alternative sequence (2); Chain (1); Compositional bias (3); Erroneous initiation (1); Sequence conflict (1) FUNCTION: May play a role in regulating breast cancer cell invasiveness. May be involved in RYBP-mediated breast cancer progression. {ECO:0000250|UniProtKB:A6NNA2}. +Q8BHY8 SNX14_MOUSE Sorting nexin-14 964 111,865 Chain (1); Domain (3); Erroneous initiation (2); Modified residue (1); Sequence conflict (1); Transmembrane (2) TRANSMEM 51 71 Helical. {ECO:0000255}.; TRANSMEM 76 96 Helical. {ECO:0000255}. FUNCTION: Plays a role in maintaining normal neuronal excitability and synaptic transmission. May be involved in several stages of intracellular trafficking (PubMed:24859318). Required for autophagosome clearance, possibly by mediating the fusion of lysosomes with autophagosomes. Binds phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2), a key component of late endosomes/lysosomes. Does not bind phosphatidylinositol 3-phosphate (PtdIns(3P)) (By similarity). {ECO:0000250|UniProtKB:Q9Y5W7, ECO:0000269|PubMed:24859318}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q9Y5W7}; Multi-pass membrane protein {ECO:0000305}. Late endosome membrane {ECO:0000250|UniProtKB:Q9Y5W7}; Multi-pass membrane protein {ECO:0000305}. Cell projection, dendrite {ECO:0000269|PubMed:24859318}. TISSUE SPECIFICITY: Expressed at high levels in the brain, testes, and lung and is present in diverse brain regions. Increases significantly during neuron development and maturation. {ECO:0000269|PubMed:24859318}. +Q8CFD4 SNX8_MOUSE Sorting nexin-8 459 52,059 Binding site (3); Chain (1); Domain (1); Erroneous initiation (2); Modified residue (2); Sequence conflict (2) FUNCTION: May be involved in several stages of intracellular trafficking. May play a role in intracellular protein transport from early endosomes to the trans-Golgi network (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Colocalizes with retromer components. {ECO:0000250}. +Q7TNE3 SPAG7_MOUSE Sperm-associated antigen 7 227 25,921 Chain (1); Domain (1); Initiator methionine (1); Modified residue (4); Motif (2); Sequence conflict (1) SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q9JJF2 SPAG4_MOUSE Sperm-associated antigen 4 protein (Outer dense fiber-associated protein SPAG4) (SUN domain-containing protein 4) 443 48,582 Alternative sequence (2); Chain (1); Coiled coil (1); Domain (1); Sequence conflict (2); Transmembrane (2) TRANSMEM 137 157 Helical. {ECO:0000255}.; TRANSMEM 168 188 Helical. {ECO:0000255}. FUNCTION: Involved in spermatogenesis. Required for sperm head formation but not required to establish and maintain general polarity of the sperm head. Required for anchoring and organization of the manchette. Required for targeting of SUN3 and probably SYNE1 through a probable SUN1:SYNE3 LINC complex to the nuclear envelope and involved in accurate posterior sperm head localization of the complex. May anchor SUN3 the nuclear envelope. Involved in maintenance of the nuclear envelope integrity. May assist the organization and assembly of outer dense fibers (ODFs), a specific structure of the sperm tail. {ECO:0000269|PubMed:26621829}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm, cytoskeleton {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 1: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O55034}. Nucleus envelope {ECO:0000269|PubMed:26621829}. Nucleus inner membrane {ECO:0000305}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:O55034}. Note=In spermatids, isoform 1 is localized in the transient manchette and in the axoneme of elongating spermatids and epididymal sperm (By similarity). Conflictingly is not found in axoneme but only associated with the manchette where cytoplasmic microtubules contact the nuclear envelope. Localizes at the posterior lateral side of round and elongating spermatids (PubMed:26621829). {ECO:0000250|UniProtKB:O55034, ECO:0000269|PubMed:26621829}. SUBUNIT: Self-associates. Interacts with ODF1. May associate with microtubules (By similarity). Interacts with SUN3 and SYNE1; suggesting the formation of a spermatogenesis-specific LINC complex; a SUN domain-based heterotrimer of SPAG4 and SUN3 may associate with SYNE1 (PubMed:26621829). Interacts with SEPT12 and LMNB1; during spermatogenesis (By similarity). {ECO:0000250|UniProtKB:O55034, ECO:0000250|UniProtKB:Q9NPE6, ECO:0000269|PubMed:26621829}. TISSUE SPECIFICITY: Isoform 1 is testis specific and is exclusively expressed in spermatids. {ECO:0000269|PubMed:10373309, ECO:0000269|PubMed:26621829}. +Q8K1K6 SPB10_MOUSE Serpin B10 397 45,115 Chain (1); Motif (1); Site (1) FUNCTION: Protease inhibitor that may play a role in the regulation of protease activities during hematopoiesis and apoptosis induced by TNF. May regulate protease activities in the cytoplasm and in the nucleus (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. +Q9CQV3 SPB11_MOUSE Serpin B11 388 43,482 Chain (1); Region (1); Sequence conflict (2); Site (1) FUNCTION: Inhibitor of serine proteases. Has moderate inhibitory activity for trypsin-like peptidases, but also some activity with cysteine peptidases, cathepsin L, K, and V, and the serine peptidase, tryptase gamma. {ECO:0000269|PubMed:17562709}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. TISSUE SPECIFICITY: Expressed in eye, lung, lymphocytes, thymus, stomach, uterus, heart, brain, liver, skeletal muscle, and in day 7, 15, and 17 embryos. {ECO:0000269|PubMed:17562709}. +Q9QYY8 SPAST_MOUSE Spastin (EC 5.6.1.1) 614 66,456 Alternative sequence (1); Chain (1); Domain (1); Intramembrane (1); Modified residue (4); Motif (3); Mutagenesis (2); Nucleotide binding (1); Region (10); Sequence conflict (4); Topological domain (2) INTRAMEM 55 75 Helical. {ECO:0000255|HAMAP-Rule:MF_03021}. TOPO_DOM 1 54 Cytoplasmic. {ECO:0000255|HAMAP-Rule:MF_03021}.; TOPO_DOM 76 614 Cytoplasmic. {ECO:0000255|HAMAP-Rule:MF_03021}. FUNCTION: ATP-dependent microtubule severing protein that specifically recognizes and cuts microtubules that are polyglutamylated (PubMed:19141076 PubMed:20530212). Preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold (By similarity). Severing activity is not dependent on tubulin acetylation or detyrosination (By similarity). Microtubule severing promotes reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation (By similarity). It is critical for the biogenesis and maintenance of complex microtubule arrays in axons, spindles and cilia (By similarity). SPAST is involved in abscission step of cytokinesis and nuclear envelope reassembly during anaphase in cooperation with the ESCRT-III complex (By similarity). Recruited at the midbody, probably by IST1, and participates in membrane fission during abscission together with the ESCRT-III complex (By similarity). Recruited to the nuclear membrane by IST1 and mediates microtubule severing, promoting nuclear envelope sealing and mitotic spindle disassembly during late anaphase (By similarity). Required for membrane traffic from the endoplasmic reticulum (ER) to the Golgi and endosome recycling (By similarity). Recruited by IST1 to endosomes and regulates early endosomal tubulation and recycling by mediating microtubule severing (By similarity). Probably plays a role in axon growth and the formation of axonal branches (PubMed:18234839). {ECO:0000250|UniProtKB:Q9UBP0, ECO:0000255|HAMAP-Rule:MF_03021, ECO:0000269|PubMed:18234839, ECO:0000269|PubMed:19141076, ECO:0000269|PubMed:20530212}.; FUNCTION: Isoform 1: Involved in lipid metabolism by regulating the size and distribution of lipid droplets. {ECO:0000250|UniProtKB:Q9UBP0}. SUBCELLULAR LOCATION: Membrane {ECO:0000255|HAMAP-Rule:MF_03021}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03021}. Endoplasmic reticulum {ECO:0000255|HAMAP-Rule:MF_03021}. Midbody {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, perinuclear region {ECO:0000255|HAMAP-Rule:MF_03021}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, spindle {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03021}. Note=Forms a intramembrane hairpin-like structure in the membrane. Localization to the centrosome is independent of microtubules. Localizes to the midbody of dividing cells, and this requires CHMP1B (By similarity). Enriched in the distal axons and branches of postmitotic neurons (By similarity). Evenly distributed along early axons and concentrates in the growth cone of the axons of late stage 3 neurons (PubMed:18234839). {ECO:0000255|HAMAP-Rule:MF_03021, ECO:0000269|PubMed:18234839}.; SUBCELLULAR LOCATION: Isoform 1: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9UBP0}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9UBP0}. Nucleus membrane {ECO:0000250|UniProtKB:Q9UBP0}. Lipid droplet {ECO:0000250|UniProtKB:Q9UBP0}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9UBP0}. Endosome {ECO:0000250|UniProtKB:Q9UBP0}. Note=Forms a intramembrane hairpin-like structure in the membrane. Recruited to nuclear membrane by IST1 during late anaphase. Localizes to endoplasmic reticulum tubular network. {ECO:0000250|UniProtKB:Q9UBP0}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm {ECO:0000250|UniProtKB:Q9UBP0}. Endosome {ECO:0000250|UniProtKB:Q9UBP0}. Nucleus membrane {ECO:0000250|UniProtKB:Q9UBP0}. Note=Constitutes the main endosomal form. Recruited to nuclear membrane by IST1 during late anaphase. {ECO:0000250|UniProtKB:Q9UBP0}. SUBUNIT: Homohexamer. Mostly monomeric, but assembles into hexameric structure for short periods of time. Oligomerization seems to be a prerequisite for catalytic activity. Binding to ATP in a cleft between two adjacent subunits stabilizes the homohexameric form. Binds to microtubules at least in part via the alpha-tubulin and beta-tubulin tails. The hexamer adopts a ring conformation through which microtubules pass prior to being severed. Does not interact strongly with tubulin heterodimers. Interacts (via MIT domain) with CHMP1B; the interaction is direct. Interacts with SSNA1. Interacts with ATL1. Interacts with RTN1. Interacts with ZFYVE27. Interacts with REEP1. Interacts (via MIT domain) with IST1. {ECO:0000255|HAMAP-Rule:MF_03021}. TISSUE SPECIFICITY: Expressed in brain, heart, liver, lung, skeletal muscle, spinal cord, spleen and testis. {ECO:0000269|PubMed:10610178, ECO:0000269|PubMed:16026783}. +Q9DBE9 SPB1_MOUSE pre-rRNA processing protein FTSJ3 (EC 2.1.1.-) (2'-O-ribose RNA methyltransferase SPB1 homolog) (Protein ftsJ homolog 3) (Putative rRNA methyltransferase 3) 838 95,532 Active site (1); Binding site (5); Chain (1); Coiled coil (1); Compositional bias (1); Cross-link (5); Modified residue (10); Sequence conflict (12) FUNCTION: Probable methyltransferase involved in the processing of the 34S pre-rRNA to 18S rRNA and in 40S ribosomal subunit formation. {ECO:0000255|HAMAP-Rule:MF_03163}. PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000255|HAMAP-Rule:MF_03163}. SUBUNIT: Interacts with NIP7. {ECO:0000255|HAMAP-Rule:MF_03163}. +Q9D695 SPB7_MOUSE Serpin B7 (Megsin) 380 43,050 Chain (1); Modified residue (1); Site (1) FUNCTION: Might function as an inhibitor of Lys-specific proteases. Might influence the maturation of megakaryocytes via its action as a serpin (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +O08800 SPB8_MOUSE Serpin B8 374 42,150 Chain (1); Site (1) FUNCTION: Has an important role in epithelial desmosome-mediated cell-cell adhesion. {ECO:0000250|UniProtKB:P50452}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +P15501 SPBP_MOUSE Prostatic spermine-binding protein (SBP) (Major prostatic secretory glycoprotein) (P25) 199 21,966 Chain (1); Domain (1); Glycosylation (1); Signal peptide (1) FUNCTION: This protein seems to be functional equivalent to rat prostatic spermine-binding protein, which is involved in polyamine binding. TISSUE SPECIFICITY: Prostate. +Q924Z5 TRAM2_MOUSE Translocating chain-associated membrane protein 2 370 43,183 Chain (1); Domain (1); Glycosylation (1); Topological domain (9); Transmembrane (8) TRANSMEM 23 43 Helical. {ECO:0000255}.; TRANSMEM 76 96 Helical. {ECO:0000255}.; TRANSMEM 120 140 Helical. {ECO:0000255}.; TRANSMEM 160 180 Helical. {ECO:0000255}.; TRANSMEM 192 209 Helical. {ECO:0000255}.; TRANSMEM 215 235 Helical. {ECO:0000255}.; TRANSMEM 251 271 Helical. {ECO:0000255}.; TRANSMEM 288 308 Helical. {ECO:0000255}. TOPO_DOM 1 22 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 44 75 Extracellular. {ECO:0000305}.; TOPO_DOM 97 119 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 141 159 Extracellular. {ECO:0000305}.; TOPO_DOM 181 191 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 210 214 Extracellular. {ECO:0000305}.; TOPO_DOM 236 250 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 272 287 Extracellular. {ECO:0000305}.; TOPO_DOM 309 370 Cytoplasmic. {ECO:0000305}. FUNCTION: Necessary for collagen type I synthesis. May couple the activity of the ER Ca(2+) pump SERCA2B with the activity of the translocon. This coupling may increase the local Ca(2+) concentration at the site of collagen synthesis, and a high Ca(2+) concentration may be necessary for the function of molecular chaperones involved in collagen folding. Required for proper insertion of the first transmembrane helix N-terminus of TM4SF20 into the ER lumen, may act as a ceramide sensor for regulated alternative translocation (RAT). {ECO:0000250|UniProtKB:Q15035}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Interacts with COL1A1 (By similarity). Interacts with SERCA2B. {ECO:0000250, ECO:0000269|PubMed:14749390}. +Q9D9W0 SPC1L_MOUSE Speriolin-like protein (Spermatogenesis and centriole-associated protein 1-like protein) 342 38,164 Chain (1); Modified residue (2) +Q9CQN1 TRAP1_MOUSE Heat shock protein 75 kDa, mitochondrial (HSP 75) (TNFR-associated protein 1) (Tumor necrosis factor type 1 receptor-associated protein) (TRAP-1) 706 80,209 Binding site (5); Chain (1); Modified residue (11); Transit peptide (1) FUNCTION: Chaperone that expresses an ATPase activity. Involved in maintaining mitochondrial function and polarization, downstream of PINK1 and mitochondrial complex I. Is a negative regulator of mitochondrial respiration able to modulate the balance between oxidative phosphorylation and aerobic glycolysis. The impact of TRAP1 on mitochondrial respiration is probably mediated by modulation of mitochondrial SRC and inhibition of SDHA. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Mitochondrion inner membrane {ECO:0000250}. Mitochondrion matrix {ECO:0000250}. SUBUNIT: Binds to the intracellular domain of tumor necrosis factor type 1 receptor. Binds to RB1. Interacts with SRC. Interacts with SDHA. {ECO:0000250}. +P70124 SPB5_MOUSE Serpin B5 (Maspin) (Peptidase inhibitor 5) (PI-5) 375 42,111 Chain (1); Glycosylation (3); Site (1) FUNCTION: Tumor suppressor. It blocks the growth, invasion, and metastatic properties of mammary tumors. As it does not undergo the S (stressed) to R (relaxed) conformational transition characteristic of active serpins, it exhibits no serine protease inhibitory activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space. SUBUNIT: Interacts with IRF6. {ECO:0000250}. +Q60854 SPB6_MOUSE Serpin B6 (Placental thrombin inhibitor) (Proteinase inhibitor 6) (PI-6) 378 42,599 Chain (1); Modified residue (3); Site (1) FUNCTION: Inhibitor of cathepsin G, kallikrein-8 and thrombin. May play an important role in the inner ear in the protection against leakage of lysosomal content during stress. May be involved in the regulation of serine proteinases present in the brain or extravasated from the blood. {ECO:0000269|PubMed:17761692}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17761692, ECO:0000269|PubMed:20451170}. SUBUNIT: Forms a complex with the monomeric form of beta-tryptase. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the inner ear hair cells, keratinocytes of hair follicles and epidermis in abdominal skin. {ECO:0000269|PubMed:17761692, ECO:0000269|PubMed:20451170}. +Q3UA16 SPC25_MOUSE Kinetochore protein Spc25 226 26,457 Alternative sequence (2); Chain (1); Coiled coil (1); Modified residue (1); Region (3) FUNCTION: Acts as a component of the essential kinetochore-associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity. Required for kinetochore integrity and the organization of stable microtubule binding sites in the outer plate of the kinetochore. The NDC80 complex synergistically enhances the affinity of the SKA1 complex for microtubules and may allow the NDC80 complex to track depolymerizing microtubules. {ECO:0000250|UniProtKB:Q9HBM1}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9HBM1}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q9HBM1}. Note=Localizes to kinetochores from late prophase to anaphase. Localizes specifically to the outer plate of the kinetochore. {ECO:0000250|UniProtKB:Q9HBM1}. SUBUNIT: Component of the NDC80 complex, which consists of NDC80/HEC1, CDCA1, SPBC24 and SPBC25. The NDC80 complex is formed by two subcomplexes composed of NDC80/HEC1-CDCA1 and SPBC24-SPBC25. Each subcomplex is formed by parallel interactions through the coiled-coil domains of individual subunits. Formation of a tetrameric complex is mediated by interactions between the C-terminal regions of both subunits of the NDC80/HEC1-CDCA1 subcomplex and the N-terminal regions of both subunits of the SPBC24-SPBC25 complex. The tetrameric NDC80 complex has an elongated rod-like structure with globular domains at either end (By similarity). {ECO:0000250}. +Q9CYN2 SPCS2_MOUSE Signal peptidase complex subunit 2 (EC 3.4.-.-) (Microsomal signal peptidase 25 kDa subunit) (SPase 25 kDa subunit) 226 24,978 Chain (1); Erroneous termination (1); Initiator methionine (1); Modified residue (3); Sequence conflict (2); Topological domain (3); Transmembrane (2) TRANSMEM 87 107 Helical. {ECO:0000255}.; TRANSMEM 112 132 Helical. {ECO:0000255}. TOPO_DOM 2 86 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 108 111 Lumenal. {ECO:0000255}.; TOPO_DOM 133 226 Cytoplasmic. {ECO:0000255}. FUNCTION: Component of the microsomal signal peptidase complex which removes signal peptides from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum. {ECO:0000250}. SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Component of the microsomal signal peptidase complex which consists of five members: SEC11A, SEC11C, SPCS1, SPCS2 and SPCS3. {ECO:0000250}. +P97473 TRBP2_MOUSE RISC-loading complex subunit TARBP2 (Protamine-1 RNA-binding protein) (PRM-1 RNA-binding protein) (TAR RNA-binding protein 2) 365 38,842 Chain (1); Domain (3); Modified residue (1); Region (4); Sequence conflict (5) FUNCTION: Required for formation of the RNA induced silencing complex (RISC). Component of the RISC loading complex (RLC), also known as the micro-RNA (miRNA) loading complex (miRLC), which is composed of DICER1, AGO2 and TARBP2. Within the RLC/miRLC, DICER1 and TARBP2 are required to process precursor miRNAs (pre-miRNAs) to mature miRNAs and then load them onto AGO2. AGO2 bound to the mature miRNA constitutes the minimal RISC and may subsequently dissociate from DICER1 and TARBP2. May also play a role in the production of short interfering RNAs (siRNAs) from double-stranded RNA (dsRNA) by DICER1 (By similarity). Binds in vitro to the PRM1 3'-UTR. Seems to act as a repressor of translation (PubMed:8649414). {ECO:0000255|HAMAP-Rule:MF_03034, ECO:0000269|PubMed:8649414}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03034, ECO:0000269|PubMed:8649414}. Cytoplasm, perinuclear region {ECO:0000255|HAMAP-Rule:MF_03034}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03034, ECO:0000269|PubMed:8649414}. SUBUNIT: Self-associates. Component of the RISC loading complex (RLC), or micro-RNA (miRNA) loading complex (miRLC), which is composed of DICER1, AGO2 and TARBP2. Note that the trimeric RLC/miRLC is also referred to as RISC. Interacts with EIF2AK2/PKR and inhibits its protein kinase activity. Interacts with DHX9 (By similarity). Interacts with DICER1 and PRKRA (PubMed:16142218, PubMed:17452327). Interacts with DICER1, AGO2, MOV10, EIF6 and RPL7A (60S ribosome subunit); they form a large RNA-induced silencing complex (RISC) (By similarity). {ECO:0000255|HAMAP-Rule:MF_03034, ECO:0000269|PubMed:16142218, ECO:0000269|PubMed:17452327}. +Q923A2 SPDLY_MOUSE Protein Spindly (Coiled-coil domain-containing protein 99) (Spindle apparatus coiled-coil domain-containing protein 1) 608 70,237 Chain (1); Coiled coil (1); Modified residue (4); Sequence conflict (1) FUNCTION: Required for the localization of dynein and dynactin to the mitotic kintochore. Dynein is believed to control the initial lateral interaction between the kinetochore and spindle microtubules and to facilitate the subsequent formation of end-on kinetochore-microtubule attachments mediated by the NDC80 complex. Also required for correct spindle orientation. Does not appear to be required for the removal of spindle assembly checkpoint (SAC) proteins from the kinetochore upon bipolar spindle attachment. Acts as an adapter protein linking the dynein motor complex to various cargos and converts dynein from a non-processive to a highly processive motor in the presence of dynactin. Facilitates the interaction between dynein and dynactin and activates dynein processivity (the ability to move along a microtubule for a long distance without falling off the track) (By similarity). {ECO:0000250|UniProtKB:Q96EA4, ECO:0000255|HAMAP-Rule:MF_03041}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03041}. Chromosome, centromere, kinetochore {ECO:0000255|HAMAP-Rule:MF_03041}. Nucleus. Cytoplasm, cytoskeleton, spindle pole {ECO:0000255|HAMAP-Rule:MF_03041}. Note=Localizes to the nucleus in interphase and to the kinetochore in early prometaphase. Relocalizes to the mitotic spindle pole before metaphase and is subsequently lost from the spindle poles after chromosome congression is completed. Removal of this protein from the kinetochore requires the dynein/dynactin complex. {ECO:0000255|HAMAP-Rule:MF_03041}. SUBUNIT: Interacts with KNTC1 and ZW10. These interactions appear weak and may be transient or indirect. Interacts with dynein intermediate chain and dynactin (DCTN1) (By similarity). {ECO:0000250|UniProtKB:Q96EA4, ECO:0000255|HAMAP-Rule:MF_03041}. +Q5IBH7 SPDYA_MOUSE Speedy protein A (Protein expressed in male leptotene and zygotene spermatocytes 465) (MLZ-465) (Rapid inducer of G2/M progression in oocytes A) (RINGO A) (mSpy/Ringo A) (Speedy-1) (Spy1) 310 36,115 Alternative sequence (2); Chain (1); Modified residue (2); Mutagenesis (5); Region (1); Sequence conflict (2) FUNCTION: Regulates the G1/S phase transition of the cell cycle by binding and activating CDK1 and CDK2 (PubMed:15611625). Contributes to CDK2 activation without promoting CDK2 phosphorylation, by inducing a conformation change of the CDK2 T-loop that obstructs the substrate-binding cleft prior to kinase activation. Interferes with CDKN1B-mediated inhibition of CDK2. Mediates cell survival during the DNA damage process through activation of CDK2 (By similarity). {ECO:0000250|UniProtKB:Q5MJ70, ECO:0000269|PubMed:15611625}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20339383}. SUBUNIT: Interacts with CDK1, CDK2 and CDKN1B/KIP1 (PubMed:15611625). Identified in a complex with CDK2 and CDKN1B/KIP1, where it interacts primarily with CDK2 (By similarity). {ECO:0000250|UniProtKB:Q5MJ70, ECO:0000269|PubMed:15611625}. DOMAIN: The C-terminus is required for CDK2-activation, but not CDK2-binding. {ECO:0000269|PubMed:15611625}. TISSUE SPECIFICITY: Expressed at a high level in testis. Also expressed in the adult ovary and in immature oocytes. {ECO:0000269|PubMed:11730327, ECO:0000269|PubMed:15611625, ECO:0000269|PubMed:20339383}. +Q9JKE2 TREM1_MOUSE Triggering receptor expressed on myeloid cells 1 (TREM-1) (CD antigen CD354) 230 25,409 Beta strand (9); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (1); Helix (3); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 203 223 Helical. {ECO:0000255}. TOPO_DOM 21 202 Extracellular. {ECO:0000255}.; TOPO_DOM 224 230 Cytoplasmic. {ECO:0000255}. FUNCTION: Stimulates neutrophil and monocyte-mediated inflammatory responses. Triggers release of pro-inflammatory chemokines and cytokines, as well as increased surface expression of cell activation markers. Amplifier of inflammatory responses that are triggered by bacterial and fungal infections and is a crucial mediator of septic shock (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Interacts with TYROBP/DAP12 (By similarity). Monomer. {ECO:0000250, ECO:0000269|PubMed:15561137}. +Q99NH8 TREM2_MOUSE Triggering receptor expressed on myeloid cells 2 (TREM-2) (Triggering receptor expressed on monocytes 2) 227 24,527 Alternative sequence (1); Chain (1); Disulfide bond (2); Domain (1); Frameshift (1); Glycosylation (2); Natural variant (1); Sequence conflict (7); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 172 192 Helical. {ECO:0000255}. TOPO_DOM 19 171 Extracellular. {ECO:0000255}.; TOPO_DOM 193 227 Cytoplasmic. {ECO:0000255}. FUNCTION: Forms a receptor signaling complex with TYROBP and triggers activation of the immune responses in macrophages and dendritic cells. May have a role in chronic inflammations and may stimulate production of constitutive rather than inflammatory chemokines and cytokines. {ECO:0000269|PubMed:11241283}. SUBCELLULAR LOCATION: Isoform 1: Cell membrane {ECO:0000250|UniProtKB:Q9NZC2}; Single-pass type I membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: Isoform 2: Secreted {ECO:0000305}. SUBUNIT: Monomer (By similarity). Interacts with TYROBP/DAP12 (PubMed:11241283). {ECO:0000250|UniProtKB:Q9NZC2, ECO:0000269|PubMed:11241283}. TISSUE SPECIFICITY: Expressed at higher levels in the CNS, heart and lung than in lymph nodes or in other non-lymphoid tissues such as kidney, liver and testis. In the CNS not all microglia express TREM2. Brain regions with an incomplete blood-brain barrier had the lowest percentages of TREM2 expressing microglia, whereas the lateral entorhinal and cingulate cortex had the highest percentages. {ECO:0000269|PubMed:11241283, ECO:0000269|PubMed:12472885}. +Q62361 TRH_MOUSE Pro-thyrotropin-releasing hormone (Pro-TRH) (Prothyroliberin) [Cleaved into: Thyrotropin-releasing hormone (TRH) (Protirelin) (TSH-releasing factor) (Thyroliberin) (Thyrotropin-releasing factor) (TRF)] 256 29,195 Chain (1); Modified residue (5); Peptide (5); Sequence conflict (3); Signal peptide (1) FUNCTION: Functions as a regulator of the biosynthesis of TSH in the anterior pituitary gland and as a neurotransmitter/ neuromodulator in the central and peripheral nervous systems. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Specifically expressed in hypothalamus and testis. {ECO:0000269|PubMed:1323011}. +Q9CYB0 TRI13_MOUSE E3 ubiquitin-protein ligase TRIM13 (EC 2.3.2.27) (Putative tumor suppressor RFP2) (RING-type E3 ubiquitin transferase TRIM13) (Ret finger protein 2) (Tripartite motif-containing protein 13) 407 46,958 Chain (1); Coiled coil (1); Sequence conflict (8); Transmembrane (1); Zinc finger (2) TRANSMEM 316 336 Helical. {ECO:0000255}. Protein modification; protein ubiquitination. FUNCTION: Endoplasmic reticulum (ER) membrane anchored E3 ligase involved in the retrotranslocation and turnover of membrane and secretory proteins from the ER through a set of processes named ER-associated degradation (ERAD). This process acts on misfolded proteins as well as in the regulated degradation of correctly folded proteins. Enhances ionizing radiation-induced p53/TP53 stability and apoptosis via ubiquitinating MDM2 and AKT1 and decreasing AKT1 kinase activity through MDM2 and AKT1 proteasomal degradation. Regulates ER stress-induced autophagy, and may act as a tumor suppressor. Plays also a role in innate immune response by stimulating NF-kappa-B activity in the TLR2 signaling pathway. Ubiquitinates TRAF6 via the 'Lys-29'-linked polyubiquitination chain resulting in NF-kappa-B activation. Participates as well in T-cell receptor-mediated NF-kappa-B activation. In the presence of TNF, modulates the IKK complex by regulating IKBKG/NEMO ubiquitination leading to the repression of NF-kappa-B. {ECO:0000250|UniProtKB:O60858}. PTM: Auto-ubiquitinated; requires the RING-type zinc finger. Auto-polyubiquitination leads to proteasomal degradation. {ECO:0000250|UniProtKB:O60858}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O60858}; Single-pass membrane protein {ECO:0000250|UniProtKB:O60858}. Note=Concentrates and colocalizes with p62/SQSTM1 and ZFYVE1 at the perinuclear endoplasmic reticulum. {ECO:0000250|UniProtKB:O60858}. SUBUNIT: Interacts (via C-terminal domain) with VCP. Interacts with AKT1; the interaction ubiquitinates AKT1 and leads to its proteasomal degradation. Interacts with MDM2; the interaction ubiquitinates AKT1 and leads to its proteasomal degradation. Interacts with p62/SQSTM1. Interacts with TRAF6. Interacts with IKBKG/NEMO. {ECO:0000250|UniProtKB:O60858}. DOMAIN: The coiled-coil domain is required for the induction of autophagy during endoplasmic reticulum (ER) stress. {ECO:0000250|UniProtKB:O60858}.; DOMAIN: The RING-type zinc finger is required for auto-polyubiquitination. {ECO:0000250|UniProtKB:O60858}.; DOMAIN: The C-terminal transmembrane domain is indispensable for the localization to the ER. {ECO:0000250|UniProtKB:O60858}. +Q8BVW3 TRI14_MOUSE Tripartite motif-containing protein 14 (PU.1-binding protein) 440 49,641 Alternative sequence (4); Chain (1); Domain (1); Erroneous initiation (1); Mutagenesis (1); Sequence conflict (2); Zinc finger (1) FUNCTION: Plays a role in the innate immune defense against viruses. Facilitates the type I IFN response by interacting with MAVS at the outer mitochondria membrane and thereby recruiting NF-kappa-B essential modulator IKBKG/NEMO to the MAVS signalosome, leading to the activation of both the IFN regulatory factor 3/IRF3 and NF-kappa-B pathways. Positively regulates the CGAS-induced type I interferon signaling pathway by stabilizing CGAS and inhibiting its autophagic degradation (PubMed:27666593). Inhibits the transcriptional activity of SPI1 in a dose-dependent manner (PubMed:14592421). {ECO:0000250|UniProtKB:Q14142, ECO:0000269|PubMed:14592421, ECO:0000269|PubMed:27666593}. PTM: Ubiquitinated. Undergoes 'Lys-63'-linked polyubiquitination; this modification allows IKBKG/NEMO recruitment to MAVS. {ECO:0000250|UniProtKB:Q14142}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q14142}. SUBUNIT: Interacts with MAVS. Interacts with WRNIP1 and PPP6C; these interactions positively regulate the RIG-I/DDX58 signaling pathway. Interacts with CGAS; this interaction stabilizes CGAS and promotes type I interferon production. Interacts with USP14; this interaction mediates the cleavage of 'Lys-48'-linked ubiquitination of CGAS (By similarity). Interacts with SPI1 (PubMed:14592421). {ECO:0000250|UniProtKB:Q14142, ECO:0000269|PubMed:14592421}. DOMAIN: The B-box zinc finger is responsible for inhibition of SPI1-mediated transcriptional activation. TISSUE SPECIFICITY: Expressed with high level in spleen, thymus, liver and testis. Expressed with low level in the brain, kidney, and skeletal muscle. Expressed in various differentiation stages of B-lymphocytes. {ECO:0000269|PubMed:14592421}. +Q99PP9 TRI16_MOUSE Tripartite motif-containing protein 16 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRIM16) (Estrogen-responsive B box protein) 556 62,943 Alternative sequence (3); Chain (1); Coiled coil (2); Domain (1); Modified residue (2); Sequence conflict (9); Zinc finger (2) FUNCTION: E3 ubiquitin ligase that plays an essential role in the organization of autophagic response and ubiquitination upon lysosomal and phagosomal damages. Plays a role in the stress-induced biogenesis and degradation of protein aggresomes by regulating the p62-KEAP1-NRF2 signaling and particularly by modulating the ubiquitination levels and thus stability of NRF2. Acts as a scaffold protein and facilitates autophagic degradation of protein aggregates by interacting with p62/SQSTM, ATG16L1 and LC3B/MAP1LC3B. In turn, protects the cell against oxidative stress-induced cell death as a consequence of endomembrane damage. {ECO:0000250|UniProtKB:O95361}. PTM: Phosphorylated by ULK1. {ECO:0000250|UniProtKB:O95361}.; PTM: Auto-ubiquitinates via its B-Boxes. {ECO:0000250|UniProtKB:O95361}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O95361}. SUBUNIT: Homodimerizes via its coiled-coil domain. Heterodimerizes with MID1, TRIM24 and PML. Interacts with Galectin-3/LGALS3 in a ULK1-dependent manner; this interaction mediates autophagy of damage endomembranes. Interacts with BECN1. Interacts with ATG16L1. Interacts with p62/SQSTM and LC3B/MAP1LC3B. {ECO:0000250|UniProtKB:O95361}. TISSUE SPECIFICITY: Widely expressed. Expressed in basal keratinocytes. +Q7TPM3 TRI17_MOUSE E3 ubiquitin-protein ligase TRIM17 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase TRIM17) (Tripartite motif-containing protein 17) 477 54,863 Chain (1); Coiled coil (1); Domain (1); Zinc finger (2) Protein modification; protein ubiquitination. FUNCTION: May function as a ubiquitin E3 ligase. {ECO:0000250|UniProtKB:Q9Y577}. PTM: Auto-ubiquitinated. {ECO:0000250|UniProtKB:Q9Y577}. SUBUNIT: Interacts (via coiled coil) with TRIM44 (via coiled coil). {ECO:0000250|UniProtKB:Q9Y577}. TISSUE SPECIFICITY: Almost exclusively in the testis. +Q8BGX0 TRI23_MOUSE E3 ubiquitin-protein ligase TRIM23 (EC 2.3.2.27) (ADP-ribosylation factor domain-containing protein 1) (GTP-binding protein ARD-1) (RING-type E3 ubiquitin transferase TRIM23) (Tripartite motif-containing protein 23) 574 63,931 Alternative sequence (2); Chain (1); Coiled coil (1); Nucleotide binding (3); Region (1); Sequence conflict (1); Zinc finger (2) Protein modification; protein ubiquitination. FUNCTION: Acts as an E3 ubiquitin-protein ligase. Plays an essential role in autophagy activation during viral infection. Mechanistically, activates TANK-binding kinase 1/TBK1 by facilitating its dimerization and ability to phosphorylate the selective autophagy receptor SQSTM1. In order to achieve this function, TRIM23 mediates 'Lys-27'-linked auto-ubiquitination of its ADP-ribosylation factor (ARF) domain to induce its GTPase activity and its recruitment to autophagosomes. {ECO:0000250|UniProtKB:P36406}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P36406}. Endomembrane system {ECO:0000250|UniProtKB:P36406}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P36406}. Lysosome membrane {ECO:0000250|UniProtKB:P36406}. Note=Membrane-associated with the Golgi complex and lysosomal structures. {ECO:0000250|UniProtKB:P36406}. SUBUNIT: Homodimer. Interacts with PSCD1. Interacts with UBE2D2. Interacts with TBK1 (via N-terminal kinase domain) and p62/SQSTM1. {ECO:0000250|UniProtKB:P36406}. DOMAIN: The RING-type zinc finger domain is responsible for E3 ubiquitin ligase activity. {ECO:0000250|UniProtKB:P36406}. +Q61510 TRI25_MOUSE E3 ubiquitin/ISG15 ligase TRIM25 (EC 6.3.2.n3) (Estrogen-responsive finger protein) (RING-type E3 ubiquitin transferase) (EC 2.3.2.27) (RING-type E3 ubiquitin transferase TRIM25) (Tripartite motif-containing protein 25) (Ubiquitin/ISG15-conjugating enzyme TRIM25) (Zinc finger protein 147) 634 71,726 Beta strand (13); Chain (1); Coiled coil (1); Cross-link (1); Domain (1); Helix (4); Modified residue (5); Sequence conflict (4); Turn (3); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: Functions as a ubiquitin E3 ligase and as an ISG15 E3 ligase. Involved in innate immune defense against viruses by mediating ubiquitination of DDX58 and IFIH1. Mediates 'Lys-63'-linked polyubiquitination of the DDX58 N-terminal CARD-like region which is crucial for triggering the cytosolic signal transduction that leads to the production of interferons in response to viral infection. Mediates 'Lys-63'-linked polyubiquitination of IFIH1. Promotes ISGylation of 14-3-3 sigma (SFN), an adapter protein implicated in the regulation of a large spectrum signaling pathway. Mediates estrogen action in various target organs. Mediates the ubiquitination and subsequent proteasomal degradation of ZFHX3. {ECO:0000250|UniProtKB:Q14258}. PTM: Auto-ISGylated. {ECO:0000250|UniProtKB:Q14258}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14258}. Note=Colocalized with DDX58 at cytoplasmic perinuclear bodies. {ECO:0000250|UniProtKB:Q14258}. SUBUNIT: Interacts (via SPRY domain) with DDX58 (via CARD domain). Interacts with ZFHX3. {ECO:0000250|UniProtKB:Q14258}. DOMAIN: The RING-type zinc finger is important for ISG15 E3 ligase activity and autoISGylation. AutoISGylation negatively regulates ISG15 E3 ligase activity. {ECO:0000250|UniProtKB:Q14258}.; DOMAIN: The C-terminal B30.2/SPRY domain interacts with the first N-terminal CARD domain of DDX58. {ECO:0000250|UniProtKB:Q14258}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:7592654}. +Q99PN3 TRI26_MOUSE Tripartite motif-containing protein 26 (EC 2.3.2.27) (Zinc finger protein 173) 545 62,809 Alternative sequence (2); Chain (1); Coiled coil (1); Compositional bias (1); Domain (1); Sequence conflict (5); Zinc finger (2) FUNCTION: E3 ubiquitin-protein ligase which regulates the IFN-beta production and antiviral response downstream of various DNA-encoded pattern-recognition receptors (PRRs). Promotes nuclear IRF3 ubiquitination and proteasomal degradation. Bridges together TBK1 and NEMO during the innate response to viral infection leading to the activation of TBK1. {ECO:0000250|UniProtKB:Q12899}. PTM: Autoubiquitinates upon viral infection. In turn, autoubiquitinated TRIM26 recruits NEMO and bridges TBK1-NEMO interaction. {ECO:0000250|UniProtKB:Q12899}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q12899}. Nucleus {ECO:0000250|UniProtKB:Q12899}. Note=Viral infection mediates TRIM26 nuclear translocation. {ECO:0000250|UniProtKB:Q12899}. SUBUNIT: Interacts with TBK1; this interaction bridges together TBK1 and NEMO in order to activate TBK1. Interacts with INCA1. {ECO:0000250|UniProtKB:Q12899}. +Q62158 TRI27_MOUSE Zinc finger protein RFP (EC 2.3.2.27) (RING-type E3 ubiquitin transferase TRIM27) (Ret finger protein) (Tripartite motif-containing protein 27) 513 58,513 Chain (1); Coiled coil (2); Domain (1); Erroneous initiation (1); Sequence conflict (5); Zinc finger (2) FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination of PIK3C2B and inhibits its activity; mediates the formation of 'Lys-48'-linked polyubiquitin chains; the function inhibits CD4 T-cell activation. Acts as a regulator of retrograde transport: together with MAGEL2, mediates the formation of 'Lys-63'-linked polyubiquitin chains at 'Lys-220' of WASHC1, leading to promote endosomal F-actin assembly. Has a transcriptional repressor activity. Induces apoptosis by activating Jun N-terminal kinase and p38 kinase and also increases caspase-3-like activity independently of mitochondrial events. May function in male germ cell development. Has DNA-binding activity and preferentially bound to double-stranded DNA. {ECO:0000250|UniProtKB:P14373}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P14373}. Cytoplasm {ECO:0000250|UniProtKB:P14373}. Nucleus, PML body {ECO:0000250}. Endosome {ECO:0000250}. Note=Nuclear or cytoplasmic depending on the cell type. Recruited to retromer-containing endosomes via interaction with MAGEL2 (By similarity). Colocalized with PML and EIF3S6 in nuclear bodies. {ECO:0000250, ECO:0000269|PubMed:10571821}. SUBUNIT: Homomultimerizes. Interacts with PML, EIF3S6, EPC1, CHD4 and EID1. Interacts with MAGED4, MAGEF1 and MAGEL2. {ECO:0000250|UniProtKB:P14373}. DOMAIN: The coiled-coil region mediates interaction with EPC1 and CHD4. The B box and coiled-coil domains mediate interaction with PML. The B box and the distal coiled-coil domains mediate homomultimerisation. The B30.2 domain mediates interaction with EIF3S6. TISSUE SPECIFICITY: Expressed strongly in testis. Low levels were detected in spleen, thymus, cerebrum and cerebellum. {ECO:0000269|PubMed:10571821, ECO:0000269|PubMed:1437549}. +Q8R2Q0 TRI29_MOUSE Tripartite motif-containing protein 29 587 65,820 Chain (1); Coiled coil (1); Erroneous initiation (1); Modified residue (7); Sequence conflict (1); Zinc finger (1) FUNCTION: Plays a crucial role in the regulation of macrophage activation in response to viral or bacterial infections within the respiratory tract. Mechanistically, TRIM29 interacts with IKBKG/NEMO in the lysosome where it induces its 'Lys-48' ubiquitination and subsequent degradation. In turn, the expression of type I interferons and the production of proinflammatory cytokines are inhibited. Additionally, induces the 'Lys-48' ubiquitination of TMEM173/STING in a similar way, leading to its degradation. {ECO:0000250|UniProtKB:Q14134}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14134}. Lysosome {ECO:0000250|UniProtKB:Q14134}. Note=Colocalizes with intermediate filaments. {ECO:0000250|UniProtKB:Q14134}. SUBUNIT: Interacts with VIM and HINT1. Interacts with IKBKG/NEMO. Interacts with TMEM173/STING. {ECO:0000250|UniProtKB:Q14134}. +Q8R0K2 TRI31_MOUSE E3 ubiquitin-protein ligase TRIM31 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase TRIM31) (Tripartite motif-containing protein 31) 507 57,127 Chain (1); Coiled coil (2); Domain (1); Zinc finger (2) Protein modification; protein ubiquitination. FUNCTION: May have E3 ubiquitin-protein ligase activity (By similarity). Regulator of Src-induced anchorage independent cell growth. {ECO:0000250, ECO:0000269|PubMed:19665990}. PTM: Auto-ubiquitinated (in vitro). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Mitochondrion {ECO:0000250}. Note=Predomintanly expressed in the cytoplasm but a fraction is associated with the mitochondria. {ECO:0000250}. SUBUNIT: Homodimer (By similarity). Interacts with isoform p52shc of SHC1. {ECO:0000250, ECO:0000269|PubMed:19665990}. TISSUE SPECIFICITY: Highly expressed in the gastrointestrinal tract, with high expression in the small intestine, moderate in the large intestine and weak in the stomach and esophagus. {ECO:0000269|PubMed:19665990}. +Q8CH72 TRI32_MOUSE E3 ubiquitin-protein ligase TRIM32 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase TRIM32) (Tripartite motif-containing protein 32) 655 72,057 Chain (1); Coiled coil (1); Compositional bias (1); Modified residue (3); Repeat (5); Sequence conflict (1); Zinc finger (2) Protein modification; protein ubiquitination. FUNCTION: Has an E3 ubiquitin ligase activity. Ubiquitinates DTNBP1 (dysbindin). May ubiquitinate BBS2 (By similarity). Ubiquitinates PIAS4/PIASY and promotes its degradation in keratinocytes treated with UVB and TNF-alpha. {ECO:0000250, ECO:0000269|PubMed:14578165, ECO:0000269|PubMed:16816390}. PTM: Ubiquitinated. {ECO:0000269|PubMed:14578165}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14578165, ECO:0000269|PubMed:16816390}. Note=Localized in cytoplasmic bodies, usually concentrated around the nucleus. SUBUNIT: Interacts with DTNBP1 (By similarity). It self-associates (By similarity). Interacts with PIAS4/PIASY upon treatment with UVB and TNF-alpha. {ECO:0000250, ECO:0000269|PubMed:16816390}. TISSUE SPECIFICITY: Ubiquitous. High expression in brain. +Q99PP7 TRI33_MOUSE E3 ubiquitin-protein ligase TRIM33 (EC 2.3.2.27) (Ectodermin homolog) (RING-type E3 ubiquitin transferase TRIM33) (Transcription intermediary factor 1-gamma) (TIF1-gamma) (Tripartite motif-containing protein 33) 1142 123,843 Alternative sequence (1); Chain (1); Coiled coil (1); Compositional bias (4); Cross-link (19); Domain (1); Modified residue (20); Region (2); Sequence conflict (1); Zinc finger (4) Protein modification; protein ubiquitination. FUNCTION: Acts as an E3 ubiquitin-protein ligase. Promotes SMAD4 ubiquitination, nuclear exclusion and degradation via the ubiquitin proteasome pathway (By similarity). May act as a transcriptional repressor (By similarity). Inhibits the transcriptional response to TGF-beta/BMP signaling cascade (By similarity). Plays a role in the control of cell proliferation (By similarity). Its association with SMAD2 and SMAD3 stimulates erythroid differentiation of hematopoietic stem/progenitor. Monoubiquitinates SMAD4 and acts as an inhibitor of SMAD4-dependent TGF-beta/BMP signaling cascade (Monoubiquitination of SMAD4 hampers its ability to form a stable complex with activated SMAD2/3 resulting in inhibition of TGF-beta/BMP signaling cascade) (By similarity). {ECO:0000250, ECO:0000269|PubMed:16751102}. PTM: Sumoylated with SUMO1. {ECO:0000269|PubMed:23213215}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15314655, ECO:0000269|PubMed:16751102}. Note=In discrete nuclear dots resembling nuclear bodies. SUBUNIT: Homooligomer and heterooligomer with TRIM24 and TRIM28 family members (By similarity). Interacts with SMAD4 in unstimulated cells (By similarity). Found in a complex with SMAD2 and SMAD3 upon addition of TGF-beta (By similarity). Interacts with SMAD2 and SMAD3 (By similarity). Interacts with SMAD4 under basal and induced conditions and, upon TGF-beta signaling, with activated SMAD2. Forms a ternary complex with SMAD4 and SMAD2 upon TGF-beta signaling (By similarity). {ECO:0000250|UniProtKB:Q9UPN9}. TISSUE SPECIFICITY: Ubiquitous with high level in testis. +Q8C006 TRI35_MOUSE Tripartite motif-containing protein 35 (Hemopoietic lineage switch protein 5) (Macrophage-derived apoptosis-inducing RBCC protein) (Protein MAIR) (Protein Nc8) 501 57,345 Alternative sequence (2); Chain (1); Coiled coil (1); Domain (1); Erroneous initiation (4); Frameshift (1); Modified residue (2); Sequence conflict (3); Zinc finger (2) FUNCTION: Reduces FGFR1-dependent tyrosine phosphorylation of PKM, inhibiting PKM-dependent lactate production, glucose metabolism, and cell growth (By similarity). Implicated in the cell death mechanism (PubMed:12692137, PubMed:14662771). {ECO:0000250|UniProtKB:Q9UPQ4, ECO:0000269|PubMed:12692137, ECO:0000269|PubMed:14662771}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12692137}. Nucleus. Note=Found predominantly in cytoplasm with a granular distribution. Found in punctuate nuclear bodies in transfected COS and HeLa cells. {ECO:0000269|PubMed:12692137}. SUBUNIT: Interacts with PKM isoform M2, but not isoform M1; this interaction reduces FGFR1-dependent tyrosine phosphorylation of PKM. {ECO:0000250|UniProtKB:Q9UPQ4}. DOMAIN: The RING finger domain and the coiled-coil region are required for the apoptosis-inducing activity. TISSUE SPECIFICITY: Widely expressed. Highly expressed in brain, heart, kidney, spleen, skeletal muscle, lung and thymus. Lower expression found in stomach, large intestine and bone marrow. {ECO:0000269|PubMed:12692137, ECO:0000269|PubMed:14662771}. +Q80WG7 TRI36_MOUSE E3 ubiquitin-protein ligase Trim36 (EC 2.3.2.27) (Acrosome RBCC protein) (Haprin) (RING-type E3 ubiquitin transferase TRIM36) (Tripartite motif-containing protein 36) 729 82,791 Chain (1); Coiled coil (1); Domain (3); Frameshift (1); Sequence conflict (3); Zinc finger (3) FUNCTION: E3 ubiquitin-protein ligase which mediates ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:19232519). Involved in chromosome segregation and cell cycle regulation (PubMed:19232519). May play a role in the acrosome reaction and fertilization (PubMed:12917430). {ECO:0000269|PubMed:12917430, ECO:0000269|PubMed:19232519}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NQ86}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:12917430}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19232519}. Note=Found in the acrosomal region of elongated spermatids and mature sperm (PubMed:12917430). Colocalizes with alpha-tubulin (PubMed:19232519). {ECO:0000269|PubMed:12917430, ECO:0000269|PubMed:19232519}. SUBUNIT: Interacts with CENPH. {ECO:0000269|PubMed:19232519}. TISSUE SPECIFICITY: Expressed in testis (PubMed:12917430). Strongly expressed in the neural tube region in 14.5 dpc embryos (PubMed:28087737). {ECO:0000269|PubMed:12917430, ECO:0000269|PubMed:28087737}. +Q3UWA4 TRI40_MOUSE Tripartite motif-containing protein 40 (Probable E3 NEDD8-protein ligase) 246 27,903 Chain (1); Coiled coil (1); Zinc finger (2) FUNCTION: May function as an E3 ubiquitin-protein ligase of the NEDD8 conjugation pathway. Promotes neddylation of IKBKG/NEMO, stabilizing NFKBIA, and inhibiting of NF-kappaB nuclear translocation and activity (By similarity). {ECO:0000250}. SUBUNIT: Interacts with NEDD8. {ECO:0000250}. +Q9D2H5 TRI42_MOUSE Tripartite motif-containing protein 42 723 82,953 Chain (1); Coiled coil (1); Compositional bias (1); Domain (2); Sequence conflict (1); Zinc finger (3) +Q6PFY8 TRI45_MOUSE Tripartite motif-containing protein 45 580 64,257 Alternative sequence (1); Chain (1); Coiled coil (1); Repeat (1); Sequence conflict (4); Zinc finger (3) FUNCTION: May act as a transcriptional repressor in mitogen-activated protein kinase signaling pathway. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. +Q7TNM2 TRI46_MOUSE Tripartite motif-containing protein 46 (Gene Y protein) (GeneY) (Tripartite, fibronectin type-III and C-terminal SPRY motif protein) 759 83,432 Alternative sequence (3); Chain (1); Coiled coil (1); Domain (3); Modified residue (2); Region (2); Sequence conflict (1); Zinc finger (3) FUNCTION: Microtubule-associated protein that is involved in the formation of parallel microtubule bundles linked by cross-bridges in the proximal axon. Required for the uniform orientation and maintenance of the parallel microtubule fascicles, which are important for efficient cargo delivery and trafficking in axons. Thereby also required for proper axon formation, the establishment of neuronal polarity and proper neuronal migration. {ECO:0000269|PubMed:26671463}. SUBCELLULAR LOCATION: Cell projection, axon {ECO:0000269|PubMed:26671463}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:26671463}. Note=Microtubule-associated. Localizes to the proximal part of the axon. {ECO:0000269|PubMed:26671463}. SUBUNIT: Interacts with TUBB3 and TUBA4A. {ECO:0000269|PubMed:26671463}. TISSUE SPECIFICITY: Expressed in the central nervous system, including pyramidal neurons and interneurons in the cortex and hippocampus and all neuronal cell types in the cerebral and cerebellar cortex, and in the peripheral nervous system, including the dorsal root ganglion neurons. {ECO:0000269|PubMed:26671463}. +Q8C0E3 TRI47_MOUSE E3 ubiquitin-protein ligase TRIM47 (EC 2.3.2.27) (Tripartite motif-containing protein 47) 641 69,912 Alternative sequence (1); Chain (1); Coiled coil (1); Compositional bias (1); Domain (1); Erroneous initiation (2); Modified residue (5); Sequence conflict (1); Zinc finger (2) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that mediates the ubiquitination and proteasomal degradation of CYLD. {ECO:0000269|PubMed:29291351}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96LD4}. Nucleus {ECO:0000250|UniProtKB:Q96LD4}. TISSUE SPECIFICITY: Expressed in hepatocytes, expression is increased in fatty livers. {ECO:0000269|PubMed:29291351}. +Q810I2 TRI50_MOUSE E3 ubiquitin-protein ligase TRIM50 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase TRIM50) (Tripartite motif-containing protein 50) 483 54,607 Chain (1); Coiled coil (2); Domain (1); Modified residue (1); Mutagenesis (1); Zinc finger (2) FUNCTION: E3 ubiquitin-protein ligase that ubiquitinates Beclin-1/BECN1 in a 'Lys-63'-dependent manner enhancing its binding to ULK1. In turn, promotes starvation-induced autophagy activation. Interacts also with p62/SQSTM1 protein and thereby induces the formation and the autophagy clearance of aggresome-associated polyubiquitinated proteins through HDAC6 interaction. {ECO:0000269|PubMed:22792322, ECO:0000269|PubMed:29604308}. PTM: Auto-ubiquitinated. {ECO:0000250|UniProtKB:Q86XT4}.; PTM: Acetylated by EP300 and KAT2B. HDAC6 drives TRIM50 deacetylation. Acetylation antagonizes with TRIM50 ubiquitination. {ECO:0000269|PubMed:24308962}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22792322, ECO:0000269|PubMed:24308962, ECO:0000269|PubMed:29604308}. Note=Localizes mainly into discrete cytoplasmic punctuate structures heterogeneous in size and shape containing polyubiquitinated proteins. {ECO:0000269|PubMed:22792322}. SUBUNIT: Can form dimers and trimers. Interacts with several E2 ubiquitin-conjugating enzymes, including UBE2L6, UBE2E1, UBE2E3. No interaction with UBE2H. Interacts with BECN1. Interacts with SQSTM1. {ECO:0000250|UniProtKB:Q86XT4, ECO:0000269|PubMed:22792322, ECO:0000269|PubMed:29604308}. TISSUE SPECIFICITY: Expressed in the stomach. {ECO:0000269|PubMed:18398435}. +Q922Y2 TRI59_MOUSE Tripartite motif-containing protein 59 (RING finger protein 1) 403 47,238 Chain (1); Coiled coil (1); Sequence conflict (10); Transmembrane (1); Zinc finger (2) TRANSMEM 329 349 Helical. {ECO:0000255}. FUNCTION: May serve as a multifunctional regulator for innate immune signaling pathways. {ECO:0000269|PubMed:22588174}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22588174}; Single-pass membrane protein {ECO:0000305}. SUBUNIT: Interacts with ECSIT (PubMed:22588174). {ECO:0000269|PubMed:22588174}. TISSUE SPECIFICITY: Moderately expressed in the spleen, brain and heart and very highly expressed in the testis (PubMed:12095697). {ECO:0000269|PubMed:12095697}. +Q8VI40 TRI60_MOUSE Tripartite motif-containing protein 60 (RING finger protein 33) 466 54,199 Chain (1); Coiled coil (1); Domain (1); Sequence conflict (1); Zinc finger (2) +Q38HM4 TRI63_MOUSE E3 ubiquitin-protein ligase TRIM63 (EC 2.3.2.27) (Muscle-specific RING finger protein 1) (MuRF-1) (MuRF1) (Muscle RING finger protein 1) (RING-type E3 ubiquitin transferase TRIM63) (Tripartite motif-containing protein 63) 350 39,491 Alternative sequence (2); Chain (1); Coiled coil (1); Domain (1); Region (1); Sequence conflict (2); Zinc finger (2) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin ligase. Mediates the ubiquitination and subsequent proteasomal degradation of CKM, GMEB1 and HIBADH. Regulates the proteasomal degradation of muscle proteins under amino acid starvation, where muscle protein is catabolized to provide other organs with amino acids. Inhibits de novo skeletal muscle protein synthesis under amino acid starvation. Regulates proteasomal degradation of cardiac troponin I/TNNI3 and probably of other sarcomeric-associated proteins. May play a role in striated muscle atrophy and hypertrophy by regulating an anti-hypertrophic PKC-mediated signaling pathway. May regulate the organization of myofibrils through TTN in muscle cells. {ECO:0000269|PubMed:15596539, ECO:0000269|PubMed:15601779, ECO:0000269|PubMed:18222470}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15601779}. Nucleus {ECO:0000269|PubMed:15601779}. Cytoplasm, myofibril, sarcomere, M line {ECO:0000250}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250}. Note=Localizes to the M- and Z-lines in skeletal muscle (By similarity). Colocalizes with TNNI3 in myocytes. {ECO:0000250}. SUBUNIT: Homodimer. Homooligomer and heterooligomer. Interacts with SUMO2, titin/TTN and GMEB1. Interacts with TRIM54 and probably with TRIM55 (By similarity). Interacts with TNNI3. Forms a ternary complex with RACK1 and PRKCE. Interacts with CKM. {ECO:0000250, ECO:0000269|PubMed:15596539, ECO:0000269|PubMed:15601779, ECO:0000269|PubMed:18222470}. DOMAIN: The RING-type zinc finger mediates interaction with SUMO2 and localization to the nucleus (By similarity). Also required for the E3 ubiquitin ligase activity. {ECO:0000250, ECO:0000269|PubMed:15601779}.; DOMAIN: The B box-type zinc finger mediates homodimerization. {ECO:0000250}. +Q8BFW4 TRI65_MOUSE Tripartite motif-containing protein 65 522 58,458 Alternative sequence (2); Chain (1); Coiled coil (1); Domain (1); Initiator methionine (1); Modified residue (2); Zinc finger (2) +Q924W6 TRI66_MOUSE Tripartite motif-containing protein 66 (Transcriptional intermediary factor 1 delta) 1242 136,766 Alternative sequence (2); Chain (1); Coiled coil (1); Compositional bias (1); Domain (1); Motif (1); Mutagenesis (2); Sequence conflict (4); Zinc finger (3) FUNCTION: May function as transcription repressor; The repressive effects are mediated, at least in part, by recruitment of deacetylase activity. May play a role as negative regulator of postmeiotic genes acting through CBX3 complex formation and centromere association. {ECO:0000269|PubMed:15322135}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15322135}. Note=Forms discrete foci within the centromeric chromocenter and surrounding nucleoplasm. SUBUNIT: Can form homodimers and heterodimers. Interacts with CBX5, CBX1 and CBX3 via PxVxL motif. {ECO:0000269|PubMed:15322135}. TISSUE SPECIFICITY: Predominant in testis, specifically in elongating spermatids. {ECO:0000269|PubMed:15322135}. +Q505D9 TRI67_MOUSE Tripartite motif-containing protein 67 768 82,760 Chain (1); Coiled coil (1); Compositional bias (4); Domain (3); Zinc finger (3) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Microtubule-associated. {ECO:0000250}. +Q8K243 TRI68_MOUSE E3 ubiquitin-protein ligase TRIM68 (EC 2.3.2.27) (RING finger protein 137) (RING-type E3 ubiquitin transferase TRIM68) (Tripartite motif-containing protein 68) 485 56,098 Chain (1); Coiled coil (1); Domain (1); Zinc finger (2) Protein modification; protein ubiquitination. FUNCTION: Functions as a ubiquitin E3 ligase. Acts as a coactivator of androgen receptor (AR) depending on its ubiquitin ligase activity. {ECO:0000250|UniProtKB:Q6AZZ1}. PTM: Auto-ubiquitinated. {ECO:0000250|UniProtKB:Q6AZZ1}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q6AZZ1}. Nucleus {ECO:0000250|UniProtKB:Q6AZZ1}. Note=Colocalized with AR in nucleus. {ECO:0000250|UniProtKB:Q6AZZ1}. SUBUNIT: Interacts with AR/androgen receptor (via ligand-binding domain). Interacts with KAT5/TIP60. {ECO:0000250|UniProtKB:Q6AZZ1}. DOMAIN: The RING domain is essential for ubiquitin E3 ligase activity. {ECO:0000250|UniProtKB:Q6AZZ1}. +Q80X56 TRI69_MOUSE E3 ubiquitin-protein ligase TRIM69 (EC 2.3.2.27) (RING finger B-box coiled-coil transcription factor) (RING finger protein 36) (RING-type E3 ubiquitin transferase TRIM69) (Testis-specific RING finger protein) (Tripartite motif-containing protein 69) 500 57,312 Chain (1); Coiled coil (1); Domain (1); Modified residue (1); Region (1); Sequence conflict (3); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: May have E3 ubiquitin-protein ligase activity. May play a role in apoptosis. {ECO:0000269|PubMed:12837286}. PTM: Phosphorylated. Phosphorylation is necessary for nuclear localization. {ECO:0000269|PubMed:12837286}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q86WT6}. Nucleus {ECO:0000250|UniProtKB:Q86WT6}. Nucleus speckle. SUBUNIT: Interacts with PML. {ECO:0000269|PubMed:12837286}. DOMAIN: The RING-type zinc finger domain is responsible for E3 ubiquitin ligase activity and for nuclear localization and aggregation. {ECO:0000250|UniProtKB:Q86WT6}. TISSUE SPECIFICITY: Expressed in spermatid. {ECO:0000269|PubMed:11578878}. +Q1XH17 TRI72_MOUSE Tripartite motif-containing protein 72 (Mitsugumin-53) (Mg53) 477 52,817 Chain (1); Coiled coil (2); Disulfide bond (1); Domain (1); Modified residue (2); Mutagenesis (16); Zinc finger (2) FUNCTION: Muscle-specific protein that plays a central role in cell membrane repair by nucleating the assembly of the repair machinery at injury sites. Specifically binds phosphatidylserine. Acts as a sensor of oxidation: upon membrane damage, entry of extracellular oxidative environment results in disulfide bond formation and homooligomerization at the injury site. This oligomerization acts as a nucleation site for recruitment of TRIM72-containing vesicles to the injury site, leading to membrane patch formation. Probably acts upstream of the Ca(2+)-dependent membrane resealing process. Required for transport of DYSF to sites of cell injury during repair patch formation. Regulates membrane budding and exocytosis. May be involved in the regulation of the mobility of KCNB1-containing endocytic vesicles. {ECO:0000269|PubMed:19029292, ECO:0000269|PubMed:19043407, ECO:0000269|PubMed:19202355, ECO:0000269|PubMed:19380584}. PTM: Disulfide bond formation at Cys-242 occurs in case of membrane damage that cause the entry of the oxidized milieu of the extracellular space, resulting in homooligomerization.; PTM: S-nitrosylation at Cys-144 stabilizes TRIM72 and protects against oxidation-induced protein degradation and cell death. {ECO:0000250|UniProtKB:Q6ZMU5}. SUBCELLULAR LOCATION: Cell membrane, sarcolemma. Cytoplasmic vesicle membrane. Note=Tethered to plasma membrane and cytoplasmic vesicles via its interaction with phosphatidylserine. SUBUNIT: Homooligomer; disulfide-linked. Interacts with DYSF and CAV3. {ECO:0000269|PubMed:19043407, ECO:0000269|PubMed:19380584}. TISSUE SPECIFICITY: Muscle-specific. Exclusively expressed in cardiac and skeletal muscle. {ECO:0000269|PubMed:19043407}. +Q3UWZ0 TRI75_MOUSE Tripartite motif-containing protein 75 467 53,385 Chain (1); Coiled coil (1); Domain (1); Zinc finger (2) +Q8K4K3 TRIB2_MOUSE Tribbles homolog 2 (TRB-2) 343 38,773 Chain (1); Domain (1); Sequence conflict (1) FUNCTION: Interacts with MAPK kinases and regulates activation of MAP kinases. Does not display kinase activity (By similarity). {ECO:0000250|UniProtKB:Q28283, ECO:0000250|UniProtKB:Q96RU8}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=May associate with the cytoskeleton. {ECO:0000250}. DOMAIN: The protein kinase domain is predicted to be catalytically inactive. +Q32MG2 SPERT_MOUSE Spermatid-associated protein (Protein nurit) 446 51,865 Alternative sequence (3); Chain (1); Coiled coil (3); Erroneous initiation (1); Modified residue (11); Sequence conflict (2) SUBUNIT: Homodimer. Binds to NEK1. TISSUE SPECIFICITY: Expression is restricted to the flower-like structure in spermatids. {ECO:0000269|PubMed:12204287}. +Q8JZX4 SPF45_MOUSE Splicing factor 45 (45 kDa-splicing factor) (RNA-binding motif protein 17) 405 45,304 Chain (1); Cross-link (7); Domain (2); Initiator methionine (1); Modified residue (12) FUNCTION: Splice factor that binds to the single-stranded 3'AG at the exon/intron border and promotes its utilization in the second catalytic step. Involved in the regulation of alternative splicing and the utilization of cryptic splice sites (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Binds SXL. Associates with the spliceosome. Interacts with SF3B1, SF1 and U2AF2 (By similarity). {ECO:0000250}. +Q8C5U4 SPEM2_MOUSE Uncharacterized protein SPEM2 503 56,934 Chain (1); Compositional bias (2); Transmembrane (1) TRANSMEM 26 46 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q5S003 SPG17_MOUSE Sperm-associated antigen 17 (Projection protein PF6 homolog) 2320 263,102 Chain (1); Coiled coil (1); Compositional bias (2); Erroneous initiation (1); Frameshift (2); Sequence caution (1); Sequence conflict (9) FUNCTION: Component of the central pair apparatus of ciliary axonemes. Plays a critical role in the function and structure of motile cilia (PubMed:23418344, PubMed:15827353). May play a role in endochondral bone formation, most likely because of a function in primary cilia of chondrocytes and osteoblasts (PubMed:26017218). {ECO:0000269|PubMed:15827353, ECO:0000269|PubMed:23418344, ECO:0000269|PubMed:26017218}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15827353}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:15827353}. Note=Detected in the cytoplasm of round spermatids and in condensing spermatids. Localized to the central pair of the sperm flagellar axoneme. Colocalizes with SPAG6 on microtubules. SUBUNIT: Interacts (via the C-terminus) with SPAG6; the interaction probably occurs on polymerized microtubules. {ECO:0000269|PubMed:15827353}. TISSUE SPECIFICITY: Highly expressed in testis, round spermatids, testicular sperm, epididymal sperm and in condensing spermatids (at protein level) (PubMed:15827353). Expressed in organs that contain cilia-bearing cells including brain, oviduct, lung, and uterus (PubMed:15827353). Expressed in articular cartilage and bone (PubMed:26017218). {ECO:0000269|PubMed:15827353, ECO:0000269|PubMed:26017218}. +Q9JIA7 SPHK2_MOUSE Sphingosine kinase 2 (SK 2) (SPK 2) (EC 2.7.1.91) 617 65,618 Active site (1); Binding site (4); Chain (1); Domain (1); Modified residue (3); Nucleotide binding (4); Region (2); Sequence conflict (3) FUNCTION: Catalyzes the phosphorylation of sphingosine to form sphingosine 1-phosphate (SPP), a lipid mediator with both intra- and extracellular functions. Also acts on D-erythro-dihydrosphingosine, D-erythro-sphingosine and L-threo-dihydrosphingosine. Binds phosphoinositides. {ECO:0000250|UniProtKB:Q9NRA0}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250}. +Q8C804 SPICE_MOUSE Spindle and centriole-associated protein 1 (Coiled-coil domain-containing protein 52) 860 95,645 Chain (1); Coiled coil (2); Modified residue (7); Sequence conflict (1) FUNCTION: Regulator required for centriole duplication, for proper bipolar spindle formation and chromosome congression in mitosis. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. SUBUNIT: Interacts with CEP120. {ECO:0000269|PubMed:20360068}. +Q6P3D7 SPIC_MOUSE Transcription factor Spi-C (Pu.1-related factor) (Prf) 242 27,942 Alternative sequence (2); Chain (1); DNA binding (1); Sequence conflict (2) FUNCTION: Controls the development of red pulp macrophages required for red blood cells recycling and iron homeostasis. Transcription factor that binds to the PU-box, a purine-rich DNA sequence (5'-GAGGA[AT]-3') that can act as a lymphoid-specific enhancer. Regulates VCAM1 gene expression. {ECO:0000269|PubMed:19037245}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Binds DNA as a monomer. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in lymphoid tissues, including spleen, bone marrow and thymus. According to PubMed:19037245, highly expressed in red pulp macrophages and, at lower, levels in B-cells, but not in other cells, including, monocytes, dendritic cells and other tissue macrophages. According to PubMed:10464163 expressed in pre- and mature B-cells but not in immature B-cells; according to PubMed:10187812 not expressed in pre- but predominantly in mature B-cells and at lower levels in macrophages. {ECO:0000269|PubMed:10187812, ECO:0000269|PubMed:10464163, ECO:0000269|PubMed:19037245}. +Q8BGX7 SPIDR_MOUSE DNA repair-scaffolding protein (Scaffolding protein involved in DNA repair) 933 103,297 Alternative sequence (3); Chain (1); Erroneous initiation (1); Frameshift (2); Region (1); Sequence conflict (3) FUNCTION: Plays a role in DNA double-strand break (DBS) repair via homologous recombination (HR). Serves as a scaffolding protein that helps to promote the recruitment of DNA-processing enzymes like the helicase BLM and recombinase RAD51 to site of DNA damage, and hence contributes to maintain genomic integrity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Together with BLM, is redistributed in discrete nuclear DNA damage-induced foci following hydroxyurea (HU) or camptothecin (CPT) treatment. {ECO:0000250}. SUBUNIT: Found in a complex, at least composed of BLM, RAD51 and SPIDR; the complex formation is mediated by SPIDR. Interacts (via C-terminal region) with BLM; the interaction is direct. Interacts with RAD51; the interaction is direct. Interacts (via the C-terminal region) with FIGNL1 (via N-terminal one-half region); the interaction is direct (By similarity). {ECO:0000250}. +Q6NVE3 SPI2C_MOUSE Spindlin-2C (Spindlin-like protein 2C) (SPIN-2) (SPIN-2C) 257 29,207 Binding site (3); Chain (1); Region (5) FUNCTION: May be involved in the regulation of cell cycle progression. Exhibits H3K4me3-binding activity. {ECO:0000250|UniProtKB:Q99865}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BPZ2}. SUBUNIT: Interacts with C11orf84/SPINDOC. {ECO:0000250|UniProtKB:Q99865}. +Q8BGE7 TRIM6_MOUSE Tripartite motif-containing protein 6 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase TRIM6) 488 56,152 Chain (1); Coiled coil (1); Domain (1); Zinc finger (2) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase which ubiquitinates MYC and inhibits its transcription activation activity, maintaining the pluripotency of embryonic stem cells (PubMed:22328504). Involved in the synthesis of unanchored K48-linked polyubiquitin chains which interact with and activate the serine/threonine kinase IKBKE, leading to phosphorylation of STAT1 and stimulation of an antiviral response (PubMed:24882218). {ECO:0000269|PubMed:22328504, ECO:0000269|PubMed:24882218}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22328504}. SUBUNIT: Homotrimer. Forms heteromultimers (via B30.2/SPRY domain) with TRIM5 (By similarity). Interacts with MYC (PubMed:22328504). Interacts (via SPRY domain) with IKBKE (By similarity). {ECO:0000250|UniProtKB:Q9C030, ECO:0000269|PubMed:22328504}. DOMAIN: The B-box zinc finger and the linker region between the coiled coil and B30.2/SPRY domains contribute to higher order self-association. {ECO:0000250|UniProtKB:Q9C030}. +Q923T7 TRIM7_MOUSE E3 ubiquitin-protein ligase TRIM7 (EC 2.3.2.27) (Glycogenin-interacting protein) (Tripartite motif-containing protein 7) 510 57,021 Alternative sequence (3); Chain (1); Coiled coil (1); Compositional bias (1); Domain (1); Modified residue (1); Zinc finger (2) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase (By similarity). Mediates 'Lys-63'-linked polyubiquitination and stabilization of the JUN coactivator RNF187 in response to growth factor signaling via the MEK/ERK pathway, thereby regulating JUN transactivation and cellular proliferation (By similarity). {ECO:0000250|UniProtKB:Q9C029}. PTM: Phosphorylated at Ser-106 by RPS6KA5/MSK1, which stimulates the ubiquitin ligase activity. {ECO:0000250|UniProtKB:Q9C029}. SUBUNIT: Forms homodimers, and heterodimers with GNIP2. Interacts with GYG. Interacts with RNF187 (via C-terminus). {ECO:0000250|UniProtKB:Q9C029}. DOMAIN: The B30.2 domain mediates interaction with GYG. {ECO:0000250|UniProtKB:Q9C029}.; DOMAIN: The coiled-coil region mediates homodimerization and heterodimerization. {ECO:0000250|UniProtKB:Q9C029}. +Q8BVP1 TRIML_MOUSE Probable E3 ubiquitin-protein ligase TRIML1 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase TRIML1) (Tripartite motif family-like protein 1) 470 53,787 Chain (1); Coiled coil (2); Domain (1); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: Probable E3 ubiquitin-protein ligase which plays an important role in blastocyst development. Involved in progression of blastocyst stage and subsequent embryo development. {ECO:0000269|PubMed:19156909}. SUBUNIT: Interacts with USP5. {ECO:0000269|PubMed:19156909}. TISSUE SPECIFICITY: Testis. {ECO:0000269|PubMed:19156909}. +Q8CEK3 SPIKL_MOUSE Serine protease inhibitor kazal-like protein, minor form (SPINKL, minor form) [Cleaved into: Serine protease inhibitor kazal-like protein, major form (SPINKL, major form)] 90 10,542 Chain (2); Domain (1); Glycosylation (1); Signal peptide (1) FUNCTION: Does not function as an inhibitor of trypsin, chymotrypsin, subtilisin or elastase. Binds sperm and enhances sperm motility. May act as a decapacitation factor, suppresses BSA-stimulated sperm capacitation and blocks sperm-oocyte interactions in vitro. {ECO:0000269|PubMed:18715980}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18715980}. TISSUE SPECIFICITY: Luminal fluid and mucosal folds of the seminal vesicles (at protein level). Not detected in brain, heart, lung, liver, kidney, stomach, small intestine, muscle, skin, thymus, placenta or bladder. {ECO:0000269|PubMed:18715980}. +Q9QXN3 TRIP4_MOUSE Activating signal cointegrator 1 (ASC-1) (Thyroid receptor-interacting protein 4) (TR-interacting protein 4) (TRIP-4) 581 66,197 Alternative sequence (2); Chain (1); Cross-link (2); Initiator methionine (1); Modified residue (3); Region (2); Sequence conflict (4); Zinc finger (1) FUNCTION: Transcription coactivator which associates with nuclear receptors, transcriptional coactivators including EP300, CREBBP and NCOA1, and basal transcription factors like TBP and TFIIA to facilitate nuclear receptors-mediated transcription. May thereby play an important role in establishing distinct coactivator complexes under different cellular conditions. Plays a role in thyroid hormone receptor and estrogen receptor transactivation (By similarity). Also involved in androgen receptor transactivation (PubMed:12077347). Plays a pivotal role in the transactivation of NF-kappa-B, SRF and AP1. Acts as a mediator of transrepression between nuclear receptor and either AP1 or NF-kappa-B. May play a role in the development of neuromuscular junction (By similarity). May play a role in late myogenic differentiation (PubMed:27008887). {ECO:0000250|UniProtKB:Q15650, ECO:0000269|PubMed:12077347, ECO:0000269|PubMed:12390891, ECO:0000269|PubMed:27008887}. PTM: Phosphorylated by NEK6. {ECO:0000250}.; PTM: Polyufmylated by the UFM1-conjugating system composed of the enzymes UBA5, UFC1 and UFL1. Deufmylated by the protease UFSP2. Ufmylation of TRIP4 is promoted by ligand-bound nuclear receptors that compete with UFSP2 for interaction with TRIP4. Nuclear receptors-induced ufmylation promotes the recruitment of additional transcriptional coactivators like EP300 and NCOA1 and therefore the assembly of a coactivator complex facilitating nuclear receptor-mediated transcription. {ECO:0000250|UniProtKB:Q15650, ECO:0000269|PubMed:21494687}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15650}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q15650}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q15650}. Note=Cytoplasmic under conditions of serum deprivation. Colocalizes with NEK6 in the centrosome. {ECO:0000250|UniProtKB:Q15650}. SUBUNIT: Interacts with the thyroid hormone receptor/TR (via the ligand-binding domain); this interaction requires the presence of thyroid hormone (By similarity). Interacts with the androgen receptor/AR; in an androgen, testosterone and dihydrotestosterone-dependent manner (By similarity). Interacts with ESR1 (estrogen ligand-bound); competes with UFSP2 (By similarity). Interacts with UFSP2; competes with ligand-bound ESR1 (By similarity). Interacts with DDRGK1 and UFL1; the interaction with DDRGK1 is direct (By similarity). Interacts with NCOA1 (By similarity). Interacts with EP300 (By similarity). Part of the ASC-1 complex, that contains TRIP4, ASCC1, ASCC2 and ASCC3 (PubMed:12077347). Interacts with NEK6 (By similarity). Interacts with CSRP1. {ECO:0000250, ECO:0000269|PubMed:12077347}. DOMAIN: The C4-type zinc finger mediates a competitive interaction with UFSP2 and ligand-bound nuclear receptors. It also mediates interaction with the transcriptional coactivators and the basal transcription machinery. {ECO:0000250|UniProtKB:Q15650}. TISSUE SPECIFICITY: Ubiquitously expressed (PubMed:12390891). Expressed in the spinal cord, brain, paraspinal ganglia, thyroid, and submandibular glands (PubMed:26924529). Expressed at low level in all the muscles (at protein level) but with higher expression in axial than in limb muscles (PubMed:27008887). {ECO:0000269|PubMed:12390891, ECO:0000269|PubMed:26924529, ECO:0000269|PubMed:27008887}. +Q9Z1Y4 TRIP6_MOUSE Thyroid receptor-interacting protein 6 (TR-interacting protein 6) (TRIP-6) (Zyxin-related protein 1) (ZRP-1) 480 50,934 Chain (1); Compositional bias (1); Domain (3); Modified residue (10); Mutagenesis (1); Region (1); Sequence conflict (1) FUNCTION: Relays signals from the cell surface to the nucleus to weaken adherens junction and promote actin cytoskeleton reorganization and cell invasiveness. Involved in lysophosphatidic acid-induced cell adhesion and migration. Acts as a transcriptional coactivator for NF-kappa-B and JUN, and mediates the transrepression of these transcription factors induced by glucocorticoid receptor (By similarity). {ECO:0000250}. PTM: Phosphorylation at Tyr-55 by SRC is required for enhancement of lysophosphatidic acid-induced cell migration. Tyr-55 is dephosphorylated by PTPN13 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q15654}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q15654}. Nucleus {ECO:0000250|UniProtKB:Q15654}. Cytoplasm {ECO:0000250|UniProtKB:Q15654}. Note=Shuttles between nucleus and cytoplasm. Colocalizes with actin. {ECO:0000250|UniProtKB:Q15654}. SUBUNIT: Specifically interacts with the ligand binding domain of the thyroid receptor (TR) in the presence of thyroid hormone (By similarity). Interacts (via the third LIM domain and C-terminus) with PTPN13 (via the second PDZ domain). Interacts (via the second LIM domain or via the third LIM domain plus C-terminus) with PDLIM4 (via PDZ domain). Found in a complex with PTPN13 and PDLIM4 (PubMed:10826496). Interacts with SVIL isoform 2. Interacts with LPAR2 but not other LPA receptors. Interacts with PRKAA2. Interacts with MAGI1. Interacts with SCRIB (By similarity). In case of infection, interacts with S.typhimurium protein sseI (PubMed:17095609). {ECO:0000250|UniProtKB:Q15654, ECO:0000269|PubMed:10826496, ECO:0000269|PubMed:17095609}. DOMAIN: The LIM zinc-binding domains mediate interaction with LPAR2. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in kidney, stomach, lung, heart and testis. Low expression levels in brain, colon, thymus, pancreas and skin. Not expressed in skeletal muscle. {ECO:0000269|PubMed:10826496}. +Q52KF3 SPIR1_MOUSE Protein spire homolog 1 598 68,450 Alternative sequence (2); Chain (1); Domain (3); Erroneous initiation (1); Modified residue (11); Region (1) FUNCTION: Acts as an actin nucleation factor, remains associated with the slow-growing pointed end of the new filament (PubMed:21620703, PubMed:21983562). Involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport (PubMed:21983562). Required for asymmetric spindle positioning and asymmetric cell division during oocyte meiosis (PubMed:21620703). Required for normal formation of the cleavage furrow and for polar body extrusion during female germ cell meiosis (PubMed:21620703). {ECO:0000269|PubMed:21620703, ECO:0000269|PubMed:21983562}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:21983562}. Cytoplasm, cytosol {ECO:0000269|PubMed:21620703, ECO:0000269|PubMed:21983562}. Cleavage furrow {ECO:0000269|PubMed:21620703}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q08AE8}. Cell membrane {ECO:0000269|PubMed:21620703, ECO:0000269|PubMed:21983562}; Peripheral membrane protein {ECO:0000269|PubMed:21620703, ECO:0000269|PubMed:21983562}; Cytoplasmic side {ECO:0000269|PubMed:21620703, ECO:0000269|PubMed:21983562}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:21983562}; Peripheral membrane protein {ECO:0000269|PubMed:21983562}; Cytoplasmic side {ECO:0000269|PubMed:21983562}. Note=Punctate spots in perinuclear region and cytoplasm, co-localised with Rab11 (PubMed:21983562). Detected at the cleavage furrow during asymmetric oocyte division and polar body extrusion (PubMed:21620703). {ECO:0000269|PubMed:21620703, ECO:0000269|PubMed:21983562}. SUBUNIT: Interacts with FMN2. {ECO:0000250|UniProtKB:Q08AE8}. DOMAIN: Binds to actin monomers via the WH2 domain. {ECO:0000250|UniProtKB:Q9U1K1}.; DOMAIN: The Spir-box targets binding to intracellular membrane structures. {ECO:0000250|UniProtKB:Q08AE8}. TISSUE SPECIFICITY: Expressed in the developing nervous system and in the adult brain, specifically the Purkinje cells of the cerebellum, in neuronal cells in the CA1, CA2 and CA3 fields of the hippocampus and granular layer of the dentate gyrus (PubMed:15053972). Detected in oocytes (PubMed:21620703). {ECO:0000269|PubMed:15053972, ECO:0000269|PubMed:21620703}. +Q8K1S6 SPIR2_MOUSE Protein spire homolog 2 (Spir-2) 718 80,210 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (4); Modified residue (4); Region (1) FUNCTION: Acts as an actin nucleation factor, remains associated with the slow-growing pointed end of the new filament (PubMed:21620703, PubMed:21983562). Involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport (PubMed:21983562). Required for asymmetric spindle positioning and asymmetric cell division during oocyte meiosis (PubMed:21620703). Required for normal formation of the cleavage furrow and for polar body extrusion during female germ cell meiosis (PubMed:21620703). Also acts in the nucleus: together with SPIRE1 and SPIRE2, promotes assembly of nuclear actin filaments in response to DNA damage in order to facilitate movement of chromatin and repair factors after DNA damage (By similarity). {ECO:0000250|UniProtKB:Q8WWL2, ECO:0000269|PubMed:21620703, ECO:0000269|PubMed:21983562}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:21983562}. Cytoplasm, cytosol {ECO:0000269|PubMed:21983562}. Cell membrane {ECO:0000269|PubMed:21983562}; Peripheral membrane protein {ECO:0000269|PubMed:21983562}; Cytoplasmic side {ECO:0000269|PubMed:21983562}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:21983562}; Peripheral membrane protein {ECO:0000269|PubMed:21983562}; Cytoplasmic side {ECO:0000269|PubMed:21983562}. Note=Detected at the cleavage furrow during asymmetric oocyte division and polar body extrusion. {ECO:0000269|PubMed:21620703}. DOMAIN: Binds to actin monomers via the WH2 domain. {ECO:0000250|UniProtKB:Q9U1K1}.; DOMAIN: The Spir-box targets binding to intracellular membrane structures. {ECO:0000250|UniProtKB:Q08AE8}. TISSUE SPECIFICITY: Detected in oocytes. {ECO:0000269|PubMed:21620703}. +Q3TX08 TRM1_MOUSE tRNA (guanine(26)-N(2))-dimethyltransferase (EC 2.1.1.216) (tRNA 2,2-dimethylguanosine-26 methyltransferase) (tRNA(guanine-26,N(2)-N(2)) methyltransferase) (tRNA(m(2,2)G26)dimethyltransferase) 663 72,350 Chain (1); Domain (1); Modified residue (3); Sequence conflict (4); Zinc finger (1) FUNCTION: Dimethylates a single guanine residue at position 26 of most tRNAs using S-adenosyl-L-methionine as donor of the methyl groups. {ECO:0000250}. +Q05AH6 SPNDC_MOUSE Spindlin interactor and repressor of chromatin-binding protein (SPIN1-docking protein) (SPIN-DOC) 381 41,245 Alternative sequence (2); Chain (1); Cross-link (5); Modified residue (6); Sequence conflict (2) FUNCTION: Negatively regulates the transcriptional activator activity of SPIN1 via inhibition of its histone methyl-binding ability. Represses the expression of a number of SPIN1-regulated genes and the SPIN1-mediated activation of the Wnt signaling pathway (PubMed:29061846). Can also inhibit the histone methyl-binding abilities of SPIN2A, SPIN2B, SPIN3 and SPIN4 (By similarity). {ECO:0000250|UniProtKB:Q9BUA3, ECO:0000269|PubMed:29061846}. SUBUNIT: Interacts with SPIN1, SPIN2A, SPIN2B, SPIN3 and SPIN4. Interacts with TCF7L2 in a SPIN1-dependent manner. {ECO:0000250|UniProtKB:Q9BUA3}. +Q8BNV1 TRM2A_MOUSE tRNA (uracil-5-)-methyltransferase homolog A (EC 2.1.1.-) (HpaII tiny fragments locus 9c protein) 574 63,301 Binding site (2); Chain (1); Coiled coil (1); Domain (1); Erroneous initiation (1); Modified residue (1); Sequence conflict (10) TISSUE SPECIFICITY: Widely expressed at low level. Expressed at higher level in proliferating cells. +Q91VM4 SPNS2_MOUSE Protein spinster homolog 2 549 58,196 Alternative sequence (2); Chain (1); Erroneous initiation (1); Transmembrane (11) TRANSMEM 141 161 Helical. {ECO:0000255}.; TRANSMEM 169 189 Helical. {ECO:0000255}.; TRANSMEM 202 222 Helical. {ECO:0000255}.; TRANSMEM 229 249 Helical. {ECO:0000255}.; TRANSMEM 261 281 Helical. {ECO:0000255}.; TRANSMEM 320 340 Helical. {ECO:0000255}.; TRANSMEM 364 384 Helical. {ECO:0000255}.; TRANSMEM 398 418 Helical. {ECO:0000255}.; TRANSMEM 422 442 Helical. {ECO:0000255}.; TRANSMEM 466 486 Helical. {ECO:0000255}.; TRANSMEM 507 527 Helical. {ECO:0000255}. FUNCTION: Sphingolipid transporter required for migration of myocardial precursors. Transports sphingosine 1-phosphate (S1P), a secreted lipid mediator that plays critical roles in cardiovascular, immunological, and neural development and function. Mediates the export of S1P from cells in the extraembryonic yolk syncytial layer (YSL), thereby regulating myocardial precursor migration (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9D232 SPNS3_MOUSE Protein spinster homolog 3 514 55,456 Alternative sequence (1); Chain (1); Sequence conflict (8); Transmembrane (12) TRANSMEM 54 74 Helical. {ECO:0000255}.; TRANSMEM 88 108 Helical. {ECO:0000255}.; TRANSMEM 116 136 Helical. {ECO:0000255}.; TRANSMEM 149 169 Helical. {ECO:0000255}.; TRANSMEM 176 196 Helical. {ECO:0000255}.; TRANSMEM 212 232 Helical. {ECO:0000255}.; TRANSMEM 264 284 Helical. {ECO:0000255}.; TRANSMEM 313 333 Helical. {ECO:0000255}.; TRANSMEM 347 367 Helical. {ECO:0000255}.; TRANSMEM 376 396 Helical. {ECO:0000255}.; TRANSMEM 415 435 Helical. {ECO:0000255}.; TRANSMEM 453 473 Helical. {ECO:0000255}. FUNCTION: Sphingolipid transporter. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8K1I3 SPP24_MOUSE Secreted phosphoprotein 24 (Spp-24) (Secreted phosphoprotein 2) 203 23,136 Chain (1); Disulfide bond (2); Modified residue (6); Sequence conflict (1); Signal peptide (1) FUNCTION: Could coordinate an aspect of bone turnover. {ECO:0000250}. PTM: Phosphorylation sites are present in the extracellular medium. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. +Q9Z0H3 SNF5_MOUSE SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1 (BRG1-associated factor 47) (BAF47) (Integrase interactor 1 protein) (SNF5 homolog) (mSNF5) 385 44,141 Alternative sequence (1); Chain (1); Cross-link (4); Modified residue (1); Region (4); Repeat (2) FUNCTION: Core component of the BAF (SWI/SNF) complex. This ATP-dependent chromatin-remodeling complex plays important roles in cell proliferation and differentiation, in cellular antiviral activities and inhibition of tumor formation. The BAF complex is able to create a stable, altered form of chromatin that constrains fewer negative supercoils than normal. This change in supercoiling would be due to the conversion of up to one-half of the nucleosomes on polynucleosomal arrays into asymmetric structures, termed altosomes, each composed of 2 histones octamers. Stimulates in vitro the remodeling activity of SMARCA4/BRG1/BAF190A. Plays a key role in cell-cycle control and causes cell cycle arrest in G0/G1. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth. {ECO:0000250|UniProtKB:Q12824, ECO:0000269|PubMed:17640523, ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Component of the multiprotein chromatin-remodeling complexes SWI/SNF: SWI/SNF-A (BAF), SWI/SNF-B (PBAF) and related complexes. The canonical complex contains a catalytic subunit (either SMARCA4/BRG1/BAF190A or SMARCA2/BRM/BAF190B) and at least SMARCE1, ACTL6A/BAF53, SMARCC1/BAF155, SMARCC2/BAF170, and SMARCB1/SNF5/BAF47. Other subunits specific to each of the complexes may also be present permitting several possible combinations developmentally and tissue specific (Probable). Component of the BAF complex, which includes at least actin (ACTB), ARID1A/BAF250A, ARID1B/BAF250B, SMARCA2/BRM, SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57 SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C (By similarity). In muscle cells, the BAF complex also contains DPF3. Component of neural progenitors-specific chromatin remodeling complex (npBAF complex) composed of at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, PHF10/BAF45A, ACTL6A/BAF53A and actin. Component of neuron-specific chromatin remodeling complex (nBAF complex) composed of at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, DPF1/BAF45B, DPF3/BAF45C, ACTL6B/BAF53B and actin (PubMed:17640523). Component of the SWI/SNF-B (PBAF) chromatin remodeling complex, at least composed of SMARCA4/BRG1, SMARCB1/BAF47/SNF5, ACTL6A/BAF53A or ACTL6B/BAF53B, SMARCE1/BAF57, SMARCD1/BAF60A, SMARCD2/BAF60B, perhaps SMARCD3/BAF60C, SMARCC1/BAF155, SMARCC2/BAF170, PBRM1/BAF180, ARID2/BAF200 and actin (PubMed:26601204). Binds to double-stranded DNA. Interacts with CEBPB (when not methylated) (PubMed:20111005). Interacts with PIH1D1. Interacts with MYK and MAEL (PubMed:16787967). Interacts with PPP1R15A (By similarity). Interacts with DPF2 (By similarity). {ECO:0000250|UniProtKB:Q12824, ECO:0000269|PubMed:16787967, ECO:0000269|PubMed:17640523, ECO:0000269|PubMed:20111005, ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}. DOMAIN: The N-terminal DNA-binding region is structurally similar to winged helix domains. {ECO:0000250|UniProtKB:Q12824}. +O35961 SMR2E_MOUSE Submaxillary gland androgen-regulated protein 2, isoform epsilon (Salivary protein MSG2, isoform epsilon) 40 4,678 Chain (1); Signal peptide (1) FUNCTION: May play a role in protection or detoxification. SUBCELLULAR LOCATION: Secreted. +P60879 SNP25_MOUSE Synaptosomal-associated protein 25 (SNAP-25) (Super protein) (SUP) (Synaptosomal-associated 25 kDa protein) 206 23,315 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (2); Lipidation (4); Modified residue (3); Mutagenesis (4); Region (2); Site (2) FUNCTION: t-SNARE involved in the molecular regulation of neurotransmitter release (PubMed:8243676, PubMed:8103915). May play an important role in the synaptic function of specific neuronal systems. Associates with proteins involved in vesicle docking and membrane fusion. Regulates plasma membrane recycling through its interaction with CENPF (PubMed:16672379). Modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1 in pancreatic beta cells (By similarity). {ECO:0000250|UniProtKB:P60881, ECO:0000269|PubMed:16672379, ECO:0000305|PubMed:8103915, ECO:0000305|PubMed:8243676}. PTM: Palmitoylated. Cys-85 appears to be the main site, and palmitoylation is required for membrane association. {ECO:0000269|PubMed:9349529}.; PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type A (BoNT/A, botA) which hydrolyzes the 197-Gln-|-Arg-198 bond and inhibits neurotransmitter release (PubMed:8243676, PubMed:8103915). {ECO:0000269|PubMed:8243676, ECO:0000305|PubMed:10413679, ECO:0000305|PubMed:8103915}.; PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type E (BoNT/E) which hydrolyzes the 180-Arg-|-Ile-181 bond and inhibits neurotransmitter release (PubMed:8243676, PubMed:8103915). {ECO:0000269|PubMed:8243676, ECO:0000305|PubMed:10413679, ECO:0000305|PubMed:8103915}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:16672379}. Cell membrane {ECO:0000269|PubMed:10413679, ECO:0000269|PubMed:9349529}; Lipid-anchor {ECO:0000269|PubMed:9349529}. Cell junction, synapse, synaptosome {ECO:0000269|PubMed:2592413}. Note=Colocalizes with KCNB1 at the cell membrane (By similarity). Membrane association requires palmitoylation (PubMed:9349529). Expressed throughout cytoplasm, concentrating at the perinuclear region (PubMed:16672379). {ECO:0000250|UniProtKB:P60881, ECO:0000269|PubMed:16672379, ECO:0000269|PubMed:9349529}. SUBUNIT: Part of the SNARE core complex containing SNAP25, VAMP2 and STX1A, this complex binds CPLX1 (PubMed:19196426). Found in a complex containing SYT1, SV2B and syntaxin-1 (PubMed:15466855). Found in a ternary complex with STX1A and VAMP8 (By similarity). Isoform 1 and isoform 2 interact with BLOC1S6 (PubMed:19546860). Interacts with CENPF (PubMed:16672379). Interacts with EQTN (PubMed:19285662). Interacts with HGS (By similarity). Interacts with KCNB1 (via N-terminus); reduces the voltage-dependent potassium channel KCNB1 activity in pancreatic beta cells (By similarity). Interacts with OTOF (PubMed:17055430). Interacts with RIMS1 (By similarity). Interacts with SNAPIN (PubMed:10195194). Interacts with STXBP6 (By similarity). Interacts with TRIM9 (By similarity). Interacts with ZDHHC13 (via ANK repeats) (PubMed:25253725). Interacts with ZDHHC17 (via ANK repeats) (PubMed:25253725). Associates with the BLOC-1 complex (PubMed:19546860). Interacts with HSC70 and with SYT9, forming a complex with DNAJC5 (PubMed:20847230). The interaction with SYT9 is inhibited in presence of calcium (PubMed:20847230). Interacts with PLCL1 (via C2 domain) (PubMed:23341457). Interacts with PRRT2; this interaction may impair the formation of the SNARE complex (PubMed:22832103, PubMed:27052163, PubMed:29056747). {ECO:0000250|UniProtKB:P60881, ECO:0000269|PubMed:10195194, ECO:0000269|PubMed:15466855, ECO:0000269|PubMed:16672379, ECO:0000269|PubMed:17055430, ECO:0000269|PubMed:19196426, ECO:0000269|PubMed:19285662, ECO:0000269|PubMed:19546860, ECO:0000269|PubMed:20847230, ECO:0000269|PubMed:22832103, ECO:0000269|PubMed:23341457, ECO:0000269|PubMed:25253725, ECO:0000269|PubMed:27052163, ECO:0000269|PubMed:29056747}. +Q8CE50 SNX30_MOUSE Sorting nexin-30 437 49,520 Chain (1); Domain (1); Modified residue (2); Sequence conflict (1) FUNCTION: May be involved in several stages of intracellular trafficking. {ECO:0000250}. +Q9DCG9 TR112_MOUSE Multifunctional methyltransferase subunit TRM112-like protein (tRNA methyltransferase 112 homolog) 125 14,141 Chain (1); Domain (1); Sequence conflict (2) FUNCTION: Acts as an activator of both rRNA/tRNA and protein methyltransferases (PubMed:26797129). Together with methyltransferase BUD23, methylates the N(7) position of a guanine in 18S rRNA (By similarity). The heterodimer with HEMK2/N6AMT1 catalyzes N5-methylation of ETF1 on 'Gln-185', using S-adenosyl L-methionine as methyl donor (PubMed:20606008, PubMed:26797129). The heterodimer with ALKBH8 catalyzes the methylation of 5-carboxymethyl uridine to 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in target tRNA species (By similarity). Involved in the pre-rRNA processing steps leading to small-subunit rRNA production (By similarity). {ECO:0000250|UniProtKB:Q9UI30, ECO:0000269|PubMed:20606008, ECO:0000269|PubMed:26797129}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9UI30}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9UI30}. Note=Localizes to a polarized perinuclear structure, overlapping partially with the Golgi and lysosomes. {ECO:0000250|UniProtKB:Q9UI30}. SUBUNIT: Heterodimer with BUD23; this heterodimerization is necessary for the metabolic stability and activity of the catalytic subunit BUD23 (By similarity). Heterodimer with N6AMT1/HEMK2 (PubMed:26797129). Heterodimer with ALKBH8 (By similarity). {ECO:0000250|UniProtKB:Q9UI30, ECO:0000269|PubMed:26797129}. +Q91WE1 SNX15_MOUSE Sorting nexin-15 337 37,742 Binding site (4); Chain (1); Domain (2); Modified residue (3) FUNCTION: May be involved in several stages of intracellular trafficking. Overexpression of SNX15 disrupts the normal trafficking of proteins from the plasma membrane to recycling endosomes or the TGN (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. SUBUNIT: Homodimer. Interacts with SNX1, SNX2 and SNX4 (By similarity). {ECO:0000250}. DOMAIN: The PX domain mediates interaction with membranes enriched in phosphatidylinositol 3-phosphate. {ECO:0000250}. +Q9CY18 SNX7_MOUSE Sorting nexin-7 387 45,000 Binding site (4); Chain (1); Domain (1) FUNCTION: May be involved in several stages of intracellular trafficking. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. +Q9QXZ6 SO1A1_MOUSE Solute carrier organic anion transporter family member 1A1 (Sodium-independent organic anion-transporting polypeptide 1) (OATP-1) (Solute carrier family 21 member 1) 670 74,396 Chain (1); Disulfide bond (3); Domain (1); Glycosylation (4); Modified residue (1); Topological domain (13); Transmembrane (12) TRANSMEM 21 40 Helical; Name=1. {ECO:0000255}.; TRANSMEM 60 80 Helical; Name=2. {ECO:0000255}.; TRANSMEM 87 111 Helical; Name=3. {ECO:0000255}.; TRANSMEM 156 184 Helical; Name=4. {ECO:0000255}.; TRANSMEM 204 224 Helical; Name=5. {ECO:0000255}.; TRANSMEM 243 267 Helical; Name=6. {ECO:0000255}.; TRANSMEM 312 333 Helical; Name=7. {ECO:0000255}.; TRANSMEM 354 377 Helical; Name=8. {ECO:0000255}.; TRANSMEM 382 405 Helical; Name=9. {ECO:0000255}.; TRANSMEM 514 536 Helical; Name=10. {ECO:0000255}.; TRANSMEM 546 571 Helical; Name=11. {ECO:0000255}.; TRANSMEM 606 623 Helical; Name=12. {ECO:0000255}. TOPO_DOM 1 20 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 41 59 Extracellular. {ECO:0000255}.; TOPO_DOM 81 86 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 112 155 Extracellular. {ECO:0000255}.; TOPO_DOM 185 203 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 225 242 Extracellular. {ECO:0000255}.; TOPO_DOM 268 311 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 334 353 Extracellular. {ECO:0000255}.; TOPO_DOM 378 381 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 406 513 Extracellular. {ECO:0000255}.; TOPO_DOM 537 545 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 572 605 Extracellular. {ECO:0000255}.; TOPO_DOM 624 670 Cytoplasmic. {ECO:0000255}. FUNCTION: Mediates the Na(+)-independent transport of organic anions such as taurocholate, prostaglandin E2 (PGE2), dehydroepiandrosterone sulfate (DHEAS), 17-beta-glucuronosyl estradiol, estrone-3-sulfate, sulfobromophthalein (BSP), ouabain and gadoxetate. SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Binds to PDZK1. Interaction with PDZK1 is required for expression on hepatocyte surface (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in liver, and at lower levels in kidney. Not detected in other tissues. +Q3UR97 SNX21_MOUSE Sorting nexin-21 363 40,308 Beta strand (1); Binding site (4); Chain (1); Domain (1); Helix (7); Mutagenesis (1); Turn (1) FUNCTION: Binds to membranes enriched in phosphatidylinositol 3-phosphate (PtdIns(P3)) and phosphatidylinositol 4,5-bisphosphate (PubMed:25882846). May be involved in several stages of intracellular trafficking. {ECO:0000269|PubMed:25882846, ECO:0000305}. SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000305|PubMed:25882846}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Early endosome membrane {ECO:0000269|PubMed:25882846}; Peripheral membrane protein {ECO:0000269|PubMed:25882846}; Cytoplasmic side {ECO:0000269|PubMed:25882846}. SUBUNIT: Monomer. {ECO:0000269|PubMed:25882846}. DOMAIN: The PX domain mediates specific binding to membranes enriched in phosphatidylinositol 3-phosphate (PtdIns(P3)). {ECO:0000269|PubMed:25882846}. +Q7TQA8 TR136_MOUSE Taste receptor type 2 member 136 (T2R136) (Taste receptor type 2 member 36) (T2R36) (mT2r52) 305 35,019 Chain (1); Erroneous gene model prediction (1); Topological domain (8); Transmembrane (7) TRANSMEM 10 30 Helical; Name=1. {ECO:0000255}.; TRANSMEM 47 67 Helical; Name=2. {ECO:0000255}.; TRANSMEM 70 90 Helical; Name=3. {ECO:0000255}.; TRANSMEM 100 120 Helical; Name=4. {ECO:0000255}.; TRANSMEM 128 148 Helical; Name=5. {ECO:0000255}.; TRANSMEM 177 197 Helical; Name=6. {ECO:0000255}.; TRANSMEM 224 244 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 9 Extracellular. {ECO:0000255}.; TOPO_DOM 31 46 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 68 69 Extracellular. {ECO:0000255}.; TOPO_DOM 91 99 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 121 127 Extracellular. {ECO:0000255}.; TOPO_DOM 149 176 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 198 223 Extracellular. {ECO:0000255}.; TOPO_DOM 245 305 Cytoplasmic. {ECO:0000255}. FUNCTION: Putative taste receptor which may play a role in the perception of bitterness. {ECO:0000303|PubMed:12734386}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. +Q9D8D0 TR13C_MOUSE Tumor necrosis factor receptor superfamily member 13C (B-cell maturation defect) (B-cell-activating factor receptor) (BAFF receptor) (BAFF-R) (BLyS receptor 3) (CD antigen CD268) 175 18,798 Alternative sequence (1); Chain (1); Disulfide bond (2); Glycosylation (1); Region (1); Repeat (1); Topological domain (2); Transmembrane (1) TRANSMEM 72 92 Helical; Signal-anchor for type III membrane protein. {ECO:0000255}. TOPO_DOM 1 71 Extracellular. {ECO:0000255}.; TOPO_DOM 93 175 Cytoplasmic. {ECO:0000255}. FUNCTION: B-cell receptor specific for TNFSF13B/TALL1/BAFF/BLyS. Promotes the survival of mature B-cells and the B-cell response. {ECO:0000269|PubMed:11747827}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type III membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Highly expressed in spleen and testis; detected at lower levels in lung and thymus. DISEASE: Note=Defects in Tnfrsf13c are a cause of severe B-cell deficiency. B-cell deficient strain A/WySnJ has a 4.7 kb insertion in the BAFFR gene leading to an altered C-terminus. The mutant RNA is not detectable. B-cell lymphopoiesis is normal, but the life span of peripheral B-cells is much reduced. {ECO:0000269|PubMed:11591325}. +Q9EPR5 SORC2_MOUSE VPS10 domain-containing receptor SorCS2 1159 128,902 Chain (1); Compositional bias (1); Domain (1); Glycosylation (7); Repeat (6); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1079 1099 Helical. {ECO:0000255}. TOPO_DOM 50 1078 Lumenal. {ECO:0000255}.; TOPO_DOM 1100 1159 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. TISSUE SPECIFICITY: Detected in brain, lung, testis and heart. +Q02384 SOS2_MOUSE Son of sevenless homolog 2 (SOS-2) (mSOS-2) 1333 153,127 Chain (1); Compositional bias (2); Domain (4); Modified residue (1); Sequence conflict (1) FUNCTION: Promotes the exchange of Ras-bound GDP by GTP. {ECO:0000250|UniProtKB:Q62245}. TISSUE SPECIFICITY: Expressed in most embryonic and adult tissues. +P40645 SOX6_MOUSE Transcription factor SOX-6 (SOX-LZ) 827 91,803 Alternative sequence (1); Chain (1); Coiled coil (1); Compositional bias (5); Cross-link (2); DNA binding (1); Modified residue (5); Sequence conflict (2) FUNCTION: Transcriptional activator. Binds specifically to the DNA sequence 5'-AACAAT-3'. Plays a key role in several developmental processes, including neurogenesis and skeleton formation. PTM: Sumoylation inhibits the transcriptional activity. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}. SUBUNIT: Interacts with DAZAP2. May interact with CENPK. {ECO:0000269|PubMed:14530442}. TISSUE SPECIFICITY: Highly expressed in testis. +P43267 SOX15_MOUSE Protein SOX-15 231 25,311 Chain (1); DNA binding (1); Modified residue (1); Natural variant (2); Sequence conflict (2) SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}. +P40646 SOX7_MOUSE Transcription factor SOX-7 (mSOX7) 380 41,489 Chain (1); DNA binding (1); Domain (1); Mutagenesis (1); Region (1) FUNCTION: Binds to and activates the CDH5 promoter, hence plays a role in the transcriptional regulation of genes expressed in the hemogenic endothelium and blocks further differentiation into blood precursors. May be required for the survival of both hematopoietic and endothelial precursors during specification. May play a role in skeletal myogenesis and up-regulate the expression of muscle markers, such as PAX3/PAX7 and Meox1. Competes with GATA4 for binding and activation of the FGF3 promoter. Represses Wnt/beta-catenin-stimulated transcription. Probably acts by targeting CTNNB1 to proteasomal degradation. Binds the DNA sequence 5'-AACAAT-3'. {ECO:0000269|PubMed:10320775, ECO:0000269|PubMed:11691915, ECO:0000269|PubMed:15082719, ECO:0000269|PubMed:19489079, ECO:0000269|PubMed:19801444, ECO:0000269|PubMed:22492353}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267, ECO:0000269|PubMed:11691915}. Cytoplasm {ECO:0000269|PubMed:11691915}. SUBUNIT: Interacts with CTNNB1/beta-catenin; this interaction may lead to the proteasomal degradation of active CTNNB1 and thus inhibition of Wnt/beta-catenin-stimulated transcription. {ECO:0000250}. TISSUE SPECIFICITY: Predominantly expressed in ovary, lung and heart. In the ovary, restricted to oocytes (at protein level). Present both in mesenchymal and epithelial cells in some adult tissues, including ear. {ECO:0000269|PubMed:10320775, ECO:0000269|PubMed:11691915}. +Q99JY4 TRABD_MOUSE TraB domain-containing protein 376 42,189 Chain (1); Modified residue (2); Sequence conflict (2) +P39428 TRAF1_MOUSE TNF receptor-associated factor 1 409 45,465 Chain (1); Coiled coil (1); Cross-link (2); Domain (1); Modified residue (1); Mutagenesis (1); Sequence conflict (1); Site (1) FUNCTION: Adapter molecule that regulates the activation of NF-kappa-B and JNK. Plays a role in the regulation of cell survival and apoptosis. The heterotrimer formed by TRAF1 and TRAF2 is part of a E3 ubiquitin-protein ligase complex that promotes ubiquitination of target proteins, such as MAP3K14. The TRAF1/TRAF2 complex recruits the antiapoptotic E3 protein-ubiquitin ligases BIRC2 and BIRC3 to TNFRSF1B/TNFR2 (By similarity). {ECO:0000250, ECO:0000269|PubMed:11672546, ECO:0000269|PubMed:18429822}. PTM: Polyubiquitinated by BIRC2 and/or BIRC3, leading to its subsequent proteasomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Homotrimer (By similarity). Heterotrimer with TRAF2 (PubMed:8069916). Interacts with TNFRSF1A/TNFR1, TNFRSF1B/TNFR2, TNFRSF4, TNFRSF5/CD40, TNFRSF8/CD30, TNFRSF9/CD137, TNFRSF11A/RANK, TNFRSF13C, TNFRSF18/AITR, TNFRSF17/BCMA, TNFRSF19/TROY, TNFRSF19L/RELT, XEDAR, EDAR, Epstein-Barr virus BNFL1/LMP-1, TANK/ITRAF, TRAIP and RIPK2 (PubMed:8069916, PubMed:9104814, PubMed:18429822). Interacts with BIRC2 and BIRC3 N-terminus; a single BIRC2 or BIRC3 molecule interacts with a heterotrimer formed by TRAF1 and TRAF2. Interacts with MAP3K14 (By similarity). Interacts with NFATC2IP, TRAFD1 and with HIVEP3 (PubMed:11804591, PubMed:16352630, PubMed:18849341). Interacts with GPS2 (PubMed:22424771). {ECO:0000250|UniProtKB:Q13077, ECO:0000269|PubMed:11804591, ECO:0000269|PubMed:16352630, ECO:0000269|PubMed:18429822, ECO:0000269|PubMed:18849341, ECO:0000269|PubMed:22424771, ECO:0000269|PubMed:8069916, ECO:0000269|PubMed:9104814}. DOMAIN: The coiled coil domain mediates homo- and hetero-oligomerization. {ECO:0000250}.; DOMAIN: The MATH/TRAF domain binds to receptor cytoplasmic domains.; DOMAIN: Cleavage by CASP8 liberates a C-terminal fragment that promotes apoptosis and inhibits the activation of NF-kappa-B in response to TNF signaling. {ECO:0000250}. +Q9ESX2 SP6_MOUSE Transcription factor Sp6 (Epiprofin) (Krueppel-like factor 14) 376 40,016 Chain (1); Zinc finger (3) FUNCTION: Promotes cell proliferation. {ECO:0000269|PubMed:14551215}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14551215}. TISSUE SPECIFICITY: Ubiquitous. Preferentially expressed by proliferating epithelial cells of teeth, hair follicles and limbs. {ECO:0000269|PubMed:14551215}. +Q8VI67 SP7_MOUSE Transcription factor Sp7 (C22) (Zinc finger protein osterix) 428 44,718 Chain (1); Cross-link (2); Sequence conflict (2); Zinc finger (3) FUNCTION: Transcriptional activator essential for osteoblast differentiation. Binds to SP1 and EKLF consensus sequences and to other G/C-rich sequences. {ECO:0000269|PubMed:11792318, ECO:0000269|PubMed:17510056}. PTM: Ubiquitination at leads to proteasomal degradation. SP7 is a short-live protein with an endogenous half-life of approximately 12 hours (By similarity). {ECO:0000250|UniProtKB:Q8TDD2}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11792318}. SUBUNIT: Interacts with RIOX1; the interaction is direct and inhibits transcription activator activity. {ECO:0000269|PubMed:19927124}. TISSUE SPECIFICITY: Osteoblast/chondrocyte specific. {ECO:0000269|PubMed:11792318}. +Q5I2A0 SPA3G_MOUSE Serine protease inhibitor A3G (Serpin A3G) (Serine protease inhibitor 2A) (Serpin 2A) 440 49,021 Chain (1); Region (1); Sequence conflict (3); Site (1) FUNCTION: Serine and cysteine protease inhibitor. Can inhibit lysosomal papain-like proteases including the cathepsins B, G, H, K, L and V. Ineffective against elastase, granzyme A, granzyme B, or caspases 3, 8 or 9. Inhibition of cytoplasmic cathepsin B following release from the lysosome may protect cells from apoptosis. This may facilitate the survival of progenitor T-cells and the subsequent development of long term memory CD8 T-cells. {ECO:0000269|PubMed:14517268, ECO:0000269|PubMed:15225607, ECO:0000269|PubMed:15311278}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. DOMAIN: The reactive center loop (RCL) extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site within the RCL, establishing a covalent linkage between the serpin reactive site and the protease. The resulting inactive serpin-protease complex is highly stable (By similarity). Variability within the reactive center loop (RCL) sequences of Serpina3 paralogs may determine target protease specificity. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in bone marrow (particularly hematopoietic stem cells), heart, kidney, liver, lung, skeletal muscle, spleen, testis, thymus and T-cells. {ECO:0000269|PubMed:11438738, ECO:0000269|PubMed:15638460, ECO:0000269|PubMed:8978283}. +Q8CIE0 SPA11_MOUSE Serpin A11 424 47,188 Chain (1); Glycosylation (4); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q7TMF5 SPA12_MOUSE Serpin A12 (Visceral adipose tissue-derived serine protease inhibitor) (Vaspin) (Visceral adipose-specific serpin) 413 47,634 Chain (1); Glycosylation (2); Region (1); Sequence conflict (4); Signal peptide (1); Site (1) FUNCTION: Adipokine that modulates insulin action by specifically inhibiting its target protease KLK7 in white adipose tissues. {ECO:0000269|PubMed:16030142, ECO:0000269|PubMed:23370777}. PTM: Glycosylation slightly decreases affinity for heparin, but otherwise has no significant effect on KLK7 inhibitory activity or thermal stability of the protein. {ECO:0000250|UniProtKB:Q8IW75}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23370777}. SUBUNIT: Forms a stable complex with KLK7. {ECO:0000250|UniProtKB:Q8IW75}. DOMAIN: The reactive center loop (RCL) extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site within the RCL, establishing a covalent linkage between the carboxyl group of the serpin reactive site and the serine hydroxyl of the protease. The resulting inactive serpin-protease complex is highly stable. {ECO:0000250|UniProtKB:Q8IW75}. TISSUE SPECIFICITY: Expressed in visceral adipose tissues. {ECO:0000269|PubMed:16030142}. +Q9D5A0 SPESP_MOUSE Sperm equatorial segment protein 1 399 44,702 Chain (1); Compositional bias (3); Glycosylation (1); Sequence conflict (2); Signal peptide (1) FUNCTION: Involved in fertilization ability of sperm. {ECO:0000269|PubMed:20375058, ECO:0000269|PubMed:25761597}. PTM: Glycosylated. In testis there are two predominant forms of 77- and 67-kDa and a form of 47-kDa, whereas in epididymal sperm from caput, corpus, and cauda there are two forms of 47- and 43-kDa. Testis forms contain complex carbohydrate residues. Epididymal sperm forms are N-glycosylated. Then undergoes significant glycosylation in the testis and that the majority of these glycoconjugates are removed by the time sperm reach the caput epididymis. {ECO:0000269|PubMed:25761597}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:20375058}. Note=Small proacrosomal granules (during the Golgi phase), enlarged acrosomal vesicles (during the cap phase), acrosome (during the elongating phase), equatorial segment of the acrosome (during the maturation phase) (By similarity). After acrosome reaction localizes to the equatorial segment region in both noncapacitated and capacitated, acrosome-reacted sperm (PubMed:25761597). {ECO:0000250|UniProtKB:Q6UW49, ECO:0000269|PubMed:25761597}. TISSUE SPECIFICITY: Testis specific. {ECO:0000269|PubMed:20375058}. +Q8K4N2 SPG11_MOUSE Sperm-associated antigen 11 71 8,116 Alternative sequence (2); Chain (1); Disulfide bond (3); Sequence conflict (1); Signal peptide (1) FUNCTION: May have antimicrobial activity. May also play a role sperm maturation, storage, and protection. {ECO:0000250|UniProtKB:Q8VBV2}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +Q5F289 SPEM1_MOUSE Spermatid maturation protein 1 310 35,062 Chain (1); Coiled coil (1); Compositional bias (1); Sequence conflict (2); Transmembrane (1) TRANSMEM 29 49 Helical. {ECO:0000255}. FUNCTION: Required for proper cytoplasm removal during spermatogenesis. {ECO:0000269|PubMed:17426145}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:17426145}. TISSUE SPECIFICITY: Testis-specific. Exclusively present in cytoplasm of steps 14-16 elongated spermatids (at protein level). {ECO:0000269|PubMed:17426145}. +Q8K450 SPG16_MOUSE Sperm-associated antigen 16 protein (Pf20 protein homolog) 639 71,473 Alternative sequence (5); Chain (1); Coiled coil (1); Repeat (7) FUNCTION: Necessary for sperm flagellar function. Plays a role in motile ciliogenesis. May help to recruit STK36 to the cilium or apical surface of the cell to initiate subsequent steps of construction of the central pair apparatus of motile cilia. {ECO:0000269|PubMed:19305393}. PTM: Phosphorylated by TSSK2. {ECO:0000305|PubMed:18367677}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12391165}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:12391165}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:12391165}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:12391165, ECO:0000269|PubMed:27682589}. Note=Detected on the sperm flagellum. Detected in the central apparatus of the axoneme. Colocalizes with SPAG6 on microtubules. {ECO:0000269|PubMed:12391165, ECO:0000269|PubMed:27682589}. SUBUNIT: Interacts with SPAG6 and STK36. {ECO:0000269|PubMed:12391165, ECO:0000269|PubMed:19305393}. TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:12391165, ECO:0000269|PubMed:27682589}. +O35906 SPIB_MOUSE Transcription factor Spi-B 267 29,365 Alternative sequence (2); Chain (1); DNA binding (1); Region (2) FUNCTION: Sequence specific transcriptional activator which binds to the PU-box, a purine-rich DNA sequence (5'-GAGGAA-3') that can act as a lymphoid-specific enhancer. Promotes development of plasmacytoid dendritic cells (pDCs), also known as type 2 DC precursors (pre-DC2) or natural interferon (IFN)-producing cells. These cells have the capacity to produce large amounts of interferon and block viral replication. Required for B-cell receptor (BCR) signaling, which is necessary for normal B-cell development and antigenic stimulation. {ECO:0000269|PubMed:10229183, ECO:0000269|PubMed:11313289, ECO:0000269|PubMed:11672537, ECO:0000269|PubMed:11980719, ECO:0000269|PubMed:12431391, ECO:0000269|PubMed:8691135, ECO:0000269|PubMed:9384589}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q01892}. SUBUNIT: Can form homotypic interactions. Interacts with IRF4. May also interact with CREBBP, EP300, SPI1/PU.1 related, JUN and TBP (By similarity). {ECO:0000250}. DOMAIN: The protein contains a weakly acidic N-terminal transactivation domain (TAD) followed by a second TAD rich in proline, serine and threonine. Each of these domains may be required for transcriptional activation of a subset of target genes (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the medulla of the thymus, the spleen and germinal centers of the lymph nodes. Expressed in B-cells and T-cells, expression increases during B-cell maturation and decreases during T-cell maturation. {ECO:0000269|PubMed:8691135}. +Q9JK88 SPI2_MOUSE Serpin I2 (Serine protease inhibitor 14) 405 45,776 Chain (1); Glycosylation (1); Sequence conflict (5); Signal peptide (1); Site (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Expressed in pancreas. +Q8K1L2 SPIN4_MOUSE Spindlin-4 249 28,508 Binding site (2); Chain (1); Region (6); Sequence conflict (1) FUNCTION: Exhibits H3K4me3-binding activity. {ECO:0000250|UniProtKB:Q56A73}. SUBUNIT: Interacts with C11orf84/SPINDOC. {ECO:0000250|UniProtKB:Q56A73}. +G5E870 TRIPC_MOUSE E3 ubiquitin-protein ligase TRIP12 (EC 2.3.2.26) (HECT-type E3 ubiquitin transferase TRIP12) (Thyroid receptor-interacting protein 12) (TR-interacting protein 12) (TRIP-12) 2025 224,128 Active site (1); Chain (1); Domain (2); Initiator methionine (1); Modified residue (20); Region (1) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase involved in ubiquitin fusion degradation (UFD) pathway and regulation of DNA repair. Part of the ubiquitin fusion degradation (UFD) pathway, a process that mediates ubiquitination of protein at their N-terminus, regardless of the presence of lysine residues in target proteins. In normal cells, mediates ubiquitination and degradation of isoform p19ARF/ARF of CDKN2A, a lysine-less tumor suppressor required for p53/TP53 activation under oncogenic stress. In cancer cells, however, isoform p19ARF/ARF and TRIP12 are located in different cell compartments, preventing isoform p19ARF/ARF ubiquitination and degradation. Does not mediate ubiquitination of isoform p16-INK4a of CDKN2A. Also catalyzes ubiquitination of NAE1 and SMARCE1, leading to their degradation. Ubiquitination and degradation of target proteins is regulated by interaction with proteins such as MYC, TRADD or SMARCC1, which disrupt the interaction between TRIP12 and target proteins. Acts as a key regulator of DNA damage response by acting as a suppressor of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of 'Lys-63'-linked histone H2A and H2AX at DNA damage sites, thereby acting as a guard against excessive spreading of ubiquitinated chromatin at damaged chromosomes. {ECO:0000250|UniProtKB:Q14669}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}. SUBUNIT: Interacts with MYC; leading to disrupt interaction with isoform p19ARF/ARF of CDKN2A. Interacts with TRADD; leading to disrupt interaction with isoform p19ARF/ARF of CDKN2A. Interacts with SMARCC1; leading to disrupt interaction with SMARCE1 (By similarity). {ECO:0000250}. +B2B9E1 TRIQK_MOUSE Triple QxxK/R motif-containing protein (Triple repetitive-sequence of QXXK/R protein homolog) 86 9,722 Chain (1); Transmembrane (1) TRANSMEM 51 71 Helical. {ECO:0000255}. FUNCTION: May play a role in cell growth and maintenance of cell morphology. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Expressed in heart, brain, spleen, lung, liver, skeletal muscle, kidney and testis. {ECO:0000269|PubMed:18828657}. +Q9D735 TRIR_MOUSE Telomerase RNA component interacting RNase (EC 3.1.13.-) (Exoribonuclease Trir) 173 18,377 Chain (1); Modified residue (1); Sequence conflict (1) FUNCTION: Exoribonuclease that is part of the telomerase RNA 3' end processing complex and which has the ability to all four unpaired RNA nucleotides from 5' end or 3' end with higher efficiency for purine bases (By similarity). {ECO:0000250|UniProtKB:Q9BQ61}. SUBUNIT: Part of the telomerase RNA 3' end complex which contains about 488 proteins (By similarity). {ECO:0000250|UniProtKB:Q9BQ61}. DOMAIN: The C-terminus contains a key domain which is responsible for the RNA digestion activity (By similarity). {ECO:0000250|UniProtKB:Q9BQ61}. +Q9R097 SPIT1_MOUSE Kunitz-type protease inhibitor 1 (Hepatocyte growth factor activator inhibitor type 1) (HAI-1) 507 56,591 Chain (1); Disulfide bond (8); Domain (4); Glycosylation (2); Sequence conflict (3); Signal peptide (1); Site (2) FUNCTION: Inhibitor of HGF activator. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Interacts with HGFAC. {ECO:0000250}. DOMAIN: This inhibitor contains two inhibitory domains. +Q9WU03 SPIT2_MOUSE Kunitz-type protease inhibitor 2 (Hepatocyte growth factor activator inhibitor type 2) (HAI-2) 252 27,914 Alternative sequence (3); Chain (1); Disulfide bond (6); Domain (2); Glycosylation (2); Signal peptide (1); Site (2); Topological domain (2); Transmembrane (1) TRANSMEM 198 218 Helical. {ECO:0000255}. TOPO_DOM 28 197 Extracellular. {ECO:0000255}.; TOPO_DOM 219 252 Cytoplasmic. {ECO:0000255}. FUNCTION: Inhibitor of HGF activator. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. DOMAIN: This inhibitor contains two inhibitory domains. TISSUE SPECIFICITY: Isoform 2 is more predominantly expressed than isoform 1. +Q9D263 SPIT4_MOUSE Kunitz-type protease inhibitor 4 (Epididymal trypsin inhibitor Spint4) 159 18,327 Chain (1); Disulfide bond (3); Domain (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Highly expressed in the epididymis, in the epithelial cells of the distal caput and early corpus. {ECO:0000269|PubMed:12920233}. +Q6NSW3 SPKAP_MOUSE A-kinase anchor protein SPHKAP (SPHK1-interactor and AKAP domain-containing protein) 1687 185,095 Alternative sequence (4); Chain (1); Frameshift (1); Modified residue (8); Region (1); Sequence conflict (16) FUNCTION: Anchoring protein that binds preferentially to the type I regulatory subunit of c-AMP-dependent protein kinase (PKA type I) and targets it to distinct subcellular compartments. May act as a converging factor linking cAMP and sphingosine signaling pathways. Plays a regulatory role in the modulation of SPHK1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Colocalizes with SPHK1 in the cytoplasm. {ECO:0000250}. SUBUNIT: Interacts (via the PKA-RII subunit binding domain) with the RI subunit of PKA. Interacts with SPHK1; the interaction greatly reduces SPHK1 activity (By similarity). {ECO:0000250}. DOMAIN: RII-binding site, predicted to form an amphipathic helix, could participate in protein-protein interactions with a complementary surface on the R-subunit dimer. {ECO:0000250}. +Q9CWH5 TRM11_MOUSE tRNA (guanine(10)-N2)-methyltransferase homolog (EC 2.1.1.-) (tRNA guanosine-2'-O-methyltransferase TRM11 homolog) 460 52,904 Alternative sequence (2); Chain (1); Initiator methionine (1); Modified residue (1) FUNCTION: Catalytic subunit of an S-adenosyl-L-methionine-dependent tRNA methyltransferase complex that mediates the methylation of the guanosine nucleotide at position 10 (m2G10) in tRNAs. {ECO:0000250}. +Q8BYH3 TRM13_MOUSE tRNA:m(4)X modification enzyme TRM13 homolog (EC 2.1.1.225) (Coiled-coil domain-containing protein 76) 481 54,261 Chain (1); Coiled coil (1); Zinc finger (1) FUNCTION: tRNA methylase which 2'-O-methylates cytidine(4) in tRNA(Pro) and tRNA(Gly)(GCC), and adenosine(4) in tRNA(His). {ECO:0000250|UniProtKB:Q12383}. +A2RSY6 TRM1L_MOUSE TRMT1-like protein (EC 2.1.1.-) 728 80,861 Alternative sequence (4); Chain (1); Cross-link (1); Domain (1); Erroneous initiation (1); Modified residue (3); Sequence conflict (7); Zinc finger (1) FUNCTION: May play a role in motor coordination and exploratory behavior. {ECO:0000269|PubMed:17198746}. TISSUE SPECIFICITY: Expressed in various neuronal structures during embryonic development, including spinal ganglia, trigeminal nerve and ganglion, olfactory and nasopharyngeal epithelium, nuclei of the metencephalon, thalamus and medulla oblongata. Also expressed in lung, esophagus, epiglottis, ependyma, vertebral column, spinal cord and brown adipose tissue. Expression persists in the adult brain with dynamically changing patterns in cortex and cerebellum. {ECO:0000269|PubMed:17198746}. +Q80W37 SPN1_MOUSE Snurportin-1 (RNA U transporter 1) 358 41,032 Chain (1); Domain (1); Modified residue (3); Region (4); Site (3) FUNCTION: Functions as an U snRNP-specific nuclear import adapter. Involved in the trimethylguanosine (m3G)-cap-dependent nuclear import of U snRNPs. Binds specifically to the terminal m3G-cap U snRNAs. {ECO:0000250|UniProtKB:O95149}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O95149}. Cytoplasm {ECO:0000250|UniProtKB:O95149}. Note=Nucleoplasmic shuttling protein. Its nuclear import involves the nucleocytoplasmic transport receptor importin beta. It is re-exported to the cytoplasm by the XPO1-dependent nuclear export receptor pathway. {ECO:0000250|UniProtKB:O95149}. SUBUNIT: Component of an import snRNP complex composed of KPNB1, SNUPN, SMN1 and ZNF259. Component of a nuclear export receptor complex composed of KPNB1, Ran, SNUPN and XPO1. Found in a trimeric export complex with SNUPN, Ran and XPO1. Interacts (via IBB domain) with KPNB1; the interaction is direct. Interacts with DDX20, IPO7, SMN1, SNRPB and XPO1. Interacts directly with XPO1. Its interaction with XPO1 and binding to m3G-cap U snRNPs appears to be mutually exclusive. {ECO:0000250|UniProtKB:O95149}. +Q9ESJ4 SPN90_MOUSE NCK-interacting protein with SH3 domain (54 kDa VacA-interacting protein) (VIP54) (90 kDa N-WASP-interacting protein) (90 kDa SH3 protein interacting with Nck) (SH3 adapter protein SPIN90) (WASP-interacting SH3-domain protein) (WISH) (Wiskott-Aldrich syndrome protein-binding protein) (N-WASP-binding protein) 714 78,572 Chain (1); Compositional bias (4); Domain (1); Modified residue (5); Motif (1) FUNCTION: Has an important role in stress fiber formation induced by active diaphanous protein homolog 1 (DRF1) (By similarity). Induces microspike formation, in vivo. In vitro, stimulates N-WASP-induced ARP2/3 complex activation in the absence of CDC42. May play an important role in the maintenance of sarcomere and/or in the assembly of myofibrils into sarcomeres. Implicated in regulation of actin polymerization and cell adhesion. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Colocalizes with DRF1 at membrane ruffles, and with Nck at Z-disks in mature cardiac myocytes. {ECO:0000250}. SUBUNIT: Associates with the intermediate filaments, vimentin and desmin (By similarity). Binds the first and third SH3 domains of NCK (By similarity). Binds the proline-rich domains of N-WASP through its SH3 domain. Similarly, binds diaphanous protein homolog 1 (DRF1) (By similarity). Binds the SH3 domains of GRB2 through its proline-rich domains. Interacts with FASLG (By similarity). {ECO:0000250}. +Q8R0G7 SPNS1_MOUSE Protein spinster homolog 1 528 56,709 Chain (1); Initiator methionine (1); Modified residue (2); Sequence conflict (7); Transmembrane (12) TRANSMEM 60 80 Helical. {ECO:0000255}.; TRANSMEM 98 118 Helical. {ECO:0000255}.; TRANSMEM 126 146 Helical. {ECO:0000255}.; TRANSMEM 160 180 Helical. {ECO:0000255}.; TRANSMEM 187 207 Helical. {ECO:0000255}.; TRANSMEM 218 238 Helical. {ECO:0000255}.; TRANSMEM 278 298 Helical. {ECO:0000255}.; TRANSMEM 323 343 Helical. {ECO:0000255}.; TRANSMEM 357 377 Helical. {ECO:0000255}.; TRANSMEM 381 401 Helical. {ECO:0000255}.; TRANSMEM 421 441 Helical. {ECO:0000255}.; TRANSMEM 465 485 Helical. {ECO:0000255}. FUNCTION: Sphingolipid transporter. May be involved in necrotic or autophagic cell death (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with BCL2 and BCL2L1. {ECO:0000250}. +Q8BQJ6 TRM2_MOUSE tRNA (uracil(54)-C(5))-methyltransferase homolog (EC 2.1.1.35) (TRM2 homolog) 493 55,476 Active site (2); Binding site (3); Chain (1); Sequence conflict (1) FUNCTION: Probable S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the formation of 5-methyl-uridine at position 54 (m5U54) in all tRNA. May also have a role in tRNA stabilization or maturation (By similarity). {ECO:0000250}. +Q9WTK8 SPO11_MOUSE Meiotic recombination protein SPO11 (EC 5.99.1.3) 396 44,570 Active site (1); Alternative sequence (4); Chain (1); Metal binding (2) FUNCTION: Isoform 1: Component of a topoisomerase 6 complex specifically required for meiotic recombination. Together with TOP6BL, mediates DNA cleavage that forms the double-strand breaks (DSB) that initiate meiotic recombination (PubMed:26917764). The complex promotes relaxation of negative and positive supercoiled DNA and DNA decatenation through cleavage and ligation cycles. Essential for the phosphorylation of SMC3, HORMAD1 and HORMAD2 (PubMed:22346761). {ECO:0000269|PubMed:22346761, ECO:0000269|PubMed:26917764}.; FUNCTION: Isoform 4: In contrast to isoform 1, does not mediate DNA cleavage that forms the double-strand breaks (DSB) that initiate meiotic recombination. {ECO:0000269|PubMed:22346761}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Isoform 1: Heterotetramer of SPO11 and 2 TOP6BL chains (Probable). Isoform 1: Interacts with TOP6BL (PubMed:26917764). Isoform 4: Does not interact with TOP6BL (PubMed:26917764). {ECO:0000269|PubMed:26917764, ECO:0000305}. TISSUE SPECIFICITY: High levels are found only in the testis where expression is restricted primarily to meiotic germ cells. Not expressed in spermatogonia. Highest levels are found in pachytene spermatocytes. Very low levels are found in thymus, brain and oocytes of embryonic ovary. Not detected in adult ovary (PubMed:10622720, PubMed:10855504). Isoform 1: Expressed early in meiosis, when most double-strand breaks (DSB) are formed (PubMed:21330546). {ECO:0000269|PubMed:10534401, ECO:0000269|PubMed:10622720, ECO:0000269|PubMed:10855504, ECO:0000269|PubMed:21330546}. +Q8BMS2 SPON2_MOUSE Spondin-2 (Mindin) 330 35,965 Chain (1); Disulfide bond (1); Domain (2); Glycosylation (1); Metal binding (5); Sequence conflict (1); Signal peptide (1); Site (1) FUNCTION: Cell adhesion protein that promotes adhesion and outgrowth of hippocampal embryonic neurons. Binds directly to bacteria and their components and functions as an opsonin for macrophage phagocytosis of bacteria. Binds bacterial lipopolysaccharide. Essential in the initiation of the innate immune response and represents a unique pattern-recognition molecule in the ECM for microbial pathogens. {ECO:0000269|PubMed:14691481}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:14691481}. SUBUNIT: Monomer. Interacts with integrin (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Detected in heart, lung, thymus, spleen and lymph node. {ECO:0000269|PubMed:14691481}. +Q2M2N2 SPOPL_MOUSE Speckle-type POZ protein-like (HIB homolog 2) 392 44,699 Alternative sequence (1); Chain (1); Domain (2); Erroneous initiation (1); Frameshift (1); Sequence conflict (1) Protein modification; protein ubiquitination. FUNCTION: Component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins, but with relatively low efficiency. Cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes containing homodimeric SPOPL or the heterodimer formed by SPOP and SPOPL are less efficient than ubiquitin ligase complexes containing only SPOP. May function to down-regulate the activity of cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes that contain SPOP (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Homodimer. Heterodimer with SPOP. Component of cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes containing homodimeric SPOPL or the heterodimer formed by SPOP and SPOPL. Interacts with CUL3 and H2AFY (By similarity). {ECO:0000250}. +Q6ZWS8 SPOP_MOUSE Speckle-type POZ protein (HIB homolog 1) (PDX-1 C-terminal-interacting factor 1) 374 42,132 Chain (1); Compositional bias (1); Domain (2); Region (4); Sequence conflict (1) Protein modification; protein ubiquitination. FUNCTION: Component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex that mediates the ubiquitination of target proteins, leading most often to their proteasomal degradation. The cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex containing homodimeric SPOP has higher ubiquitin ligase activity than the complex that contains the heterodimer formed by SPOP and SPOPL (By similarity). In complex with CUL3, involved in ubiquitination and proteasomal degradation of BRMS1, DAXX, PDX1/IPF1, GLI2 and GLI3. In complex with CUL3, involved in ubiquitination of H2AFY and BMI1; this does not lead to their proteasomal degradation. Inhibits transcriptional activation of PDX1/IPF1 targets, such as insulin, by promoting PDX1/IPF1 degradation. {ECO:0000250, ECO:0000269|PubMed:15121856, ECO:0000269|PubMed:16740475, ECO:0000269|PubMed:20463034, ECO:0000269|PubMed:20811152}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15121856}. Nucleus speckle {ECO:0000269|PubMed:15121856}. SUBUNIT: Homodimer and homooligomer. Heterodimer with SPOPL. Each dimer interacts with two CUL3 molecules. Part of cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes that contain CUL3 and homodimeric SPOP, or the heterodimer formed by SPOP and SPOPL, plus a target protein, such as H2AFY, PDX1/IPF1, BMI1, BRMS1 and DAXX (By similarity). Interacts with H2AFY, PDX1/IPF1, GLI2 and GLI3. {ECO:0000250, ECO:0000269|PubMed:12183056, ECO:0000269|PubMed:15121856, ECO:0000269|PubMed:20463034}. DOMAIN: The BTB (POZ) domain mediates dimerization and interaction with CUL3. {ECO:0000250}.; DOMAIN: The MATH domain mediates interaction with protein-ubiquitin ligase substrates, such as H2AFY and BMI1. TISSUE SPECIFICITY: Widely expressed, mainly in pancreas and in particular in adult pancreatic insulin-producing beta cells and in a subset of exocrine acinar and duct cells. +Q9JJF9 SPP2A_MOUSE Signal peptide peptidase-like 2A (SPP-like 2A) (SPPL2a) (EC 3.4.23.-) (Intramembrane protease 3) (IMP-3) (Presenilin-like protein 2) 523 58,129 Active site (2); Chain (1); Domain (1); Glycosylation (6); Motif (2); Mutagenesis (2); Sequence conflict (3); Signal peptide (1); Topological domain (10); Transmembrane (9) TRANSMEM 176 196 Helical. {ECO:0000255}.; TRANSMEM 225 245 Helical. {ECO:0000255}.; TRANSMEM 248 268 Helical. {ECO:0000255}.; TRANSMEM 289 309 Helical. {ECO:0000255}.; TRANSMEM 316 336 Helical. {ECO:0000255}.; TRANSMEM 345 365 Helical. {ECO:0000255}.; TRANSMEM 404 424 Helical. {ECO:0000255}.; TRANSMEM 441 461 Helical. {ECO:0000255}.; TRANSMEM 464 484 Helical. {ECO:0000255}. TOPO_DOM 26 175 Lumenal. {ECO:0000250|UniProtKB:Q8TCT8, ECO:0000255}.; TOPO_DOM 197 224 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 246 247 Lumenal. {ECO:0000255}.; TOPO_DOM 269 288 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 310 315 Lumenal. {ECO:0000255}.; TOPO_DOM 337 344 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 366 403 Lumenal. {ECO:0000250|UniProtKB:Q8TCT8}.; TOPO_DOM 425 440 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 462 463 Lumenal. {ECO:0000255}.; TOPO_DOM 485 523 Cytoplasmic. {ECO:0000250|UniProtKB:Q8TCT8}. FUNCTION: Intramembrane-cleaving aspartic protease (I-CLiP) that cleaves type II membrane signal peptides in the hydrophobic plane of the membrane. Functions in FASLG, ITM2B and TNF processing. Catalyzes the intramembrane cleavage of the anchored fragment of shed TNF-alpha (TNF), which promotes the release of the intracellular domain (ICD) for signaling to the nucleus. Also responsible for the intramembrane cleavage of Fas antigen ligand FASLG, which promotes the release of the intracellular FasL domain (FasL ICD). May play a role in the regulation of innate and adaptive immunity. {ECO:0000250|UniProtKB:Q8TCT8}. PTM: Glycosylated. {ECO:0000250|UniProtKB:P49768}. SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000269|PubMed:21896273}; Multi-pass membrane protein {ECO:0000305}. Lysosome membrane {ECO:0000269|PubMed:21896273}; Multi-pass membrane protein {ECO:0000305}. Membrane {ECO:0000250|UniProtKB:Q8TCT8}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8TCT8}; Lumenal side {ECO:0000250|UniProtKB:Q8TCT8}. Note=Colocalizes with palmitoylated and myristoylated proteins at the plasma membrane. {ECO:0000250}. SUBUNIT: Interacts with ITM2B. {ECO:0000250|UniProtKB:Q8TCT8}. DOMAIN: The PAL motif is required for normal active site conformation. The catalytic domains embedded in the membrane are in the opposite orientation to that of the presenilin protein family; therefore, it is predicted to cleave type II-oriented substrate peptides like the prototypic protease SPP (By similarity). The C-terminal tail is necessary for lysosomal transport (PubMed:21896273). {ECO:0000250|UniProtKB:P49768, ECO:0000269|PubMed:21896273}. +O70554 SPR2B_MOUSE Small proline-rich protein 2B 98 10,735 Chain (1); Region (1); Repeat (5); Sequence conflict (2) FUNCTION: Cross-linked envelope protein of keratinocytes. It is a keratinocyte protein that first appears in the cell cytosol, but ultimately becomes cross-linked to membrane proteins by transglutaminase. All that results in the formation of an insoluble envelope beneath the plasma membrane (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. TISSUE SPECIFICITY: Expressed in uterus. {ECO:0000269|PubMed:15232223}. +O70555 SPR2D_MOUSE Small proline-rich protein 2D 85 9,243 Chain (1); Region (1); Repeat (4) FUNCTION: Cross-linked envelope protein of keratinocytes. It is a keratinocyte protein that first appears in the cell cytosol, but ultimately becomes cross-linked to membrane proteins by transglutaminase. All that results in the formation of an insoluble envelope beneath the plasma membrane (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. TISSUE SPECIFICITY: Expressed in uterus. {ECO:0000269|PubMed:15232223}. +O70556 SPR2E_MOUSE Small proline-rich protein 2E 76 8,406 Chain (1); Region (1); Repeat (3) FUNCTION: Cross-linked envelope protein of keratinocytes. It is a keratinocyte protein that first appears in the cell cytosol, but ultimately becomes cross-linked to membrane proteins by transglutaminase. All that results in the formation of an insoluble envelope beneath the plasma membrane (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. TISSUE SPECIFICITY: Expressed in uterus. {ECO:0000269|PubMed:15232223}. +O70557 SPR2F_MOUSE Small proline-rich protein 2F 76 8,271 Chain (1); Region (1); Repeat (3) FUNCTION: Cross-linked envelope protein of keratinocytes. It is a keratinocyte protein that first appears in the cell cytosol, but ultimately becomes cross-linked to membrane proteins by transglutaminase. All that results in the formation of an insoluble envelope beneath the plasma membrane (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. TISSUE SPECIFICITY: Expressed in uterus. {ECO:0000269|PubMed:15232223}. +O70558 SPR2G_MOUSE Small proline-rich protein 2G 76 8,296 Chain (1); Region (1); Repeat (3) FUNCTION: Cross-linked envelope protein of keratinocytes. It is a keratinocyte protein that first appears in the cell cytosol, but ultimately becomes cross-linked to membrane proteins by transglutaminase. All that results in the formation of an insoluble envelope beneath the plasma membrane (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. TISSUE SPECIFICITY: Expressed in uterus. {ECO:0000269|PubMed:15232223}. +O70559 SPR2H_MOUSE Small proline-rich protein 2H 108 11,720 Chain (1); Region (1); Repeat (7) FUNCTION: Cross-linked envelope protein of keratinocytes. It is a keratinocyte protein that first appears in the cell cytosol, but ultimately becomes cross-linked to membrane proteins by transglutaminase. All that results in the formation of an insoluble envelope beneath the plasma membrane (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. TISSUE SPECIFICITY: Expressed weakly in uterus. {ECO:0000269|PubMed:15232223}. +O70560 SPR2I_MOUSE Small proline-rich protein 2I 76 8,356 Chain (1); Region (1); Repeat (3) FUNCTION: Cross-linked envelope protein of keratinocytes. It is a keratinocyte protein that first appears in the cell cytosol, but ultimately becomes cross-linked to membrane proteins by transglutaminase. All that results in the formation of an insoluble envelope beneath the plasma membrane (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. TISSUE SPECIFICITY: Not expressed in uterus. {ECO:0000269|PubMed:15232223}. +O70561 SPR2J_MOUSE Putative small proline-rich protein 2J 109 11,809 Chain (1); Region (1); Repeat (5); Sequence conflict (2) FUNCTION: Cross-linked envelope protein of keratinocytes. It is a keratinocyte protein that first appears in the cell cytosol, but ultimately becomes cross-linked to membrane proteins by transglutaminase. All that results in the formation of an insoluble envelope beneath the plasma membrane (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. TISSUE SPECIFICITY: Not expressed in uterus. {ECO:0000269|PubMed:15232223}. +O70562 SPR2K_MOUSE Small proline-rich protein 2K 68 7,499 Chain (1); Region (1); Repeat (4) FUNCTION: Cross-linked envelope protein of keratinocytes. It is a keratinocyte protein that first appears in the cell cytosol, but ultimately becomes cross-linked to membrane proteins by transglutaminase. All that results in the formation of an insoluble envelope beneath the plasma membrane (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. TISSUE SPECIFICITY: Not expressed in uterus. {ECO:0000269|PubMed:15232223}. +P07214 SPRC_MOUSE SPARC (Basement-membrane protein 40) (BM-40) (Osteonectin) (ON) (Secreted protein acidic and rich in cysteine) 302 34,450 Calcium binding (1); Chain (1); Compositional bias (1); Disulfide bond (7); Domain (3); Glycosylation (1); Signal peptide (1) FUNCTION: Appears to regulate cell growth through interactions with the extracellular matrix and cytokines. Binds calcium and copper, several types of collagen, albumin, thrombospondin, PDGF and cell membranes. There are two calcium binding sites; an acidic domain that binds 5 to 8 Ca(2+) with a low affinity and an EF-hand loop that binds a Ca(2+) ion with a high affinity. PTM: N-glycosylated. {ECO:0000269|PubMed:3427055}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000269|PubMed:3427055}. Note=In or around the basement membrane. +Q924S8 SPRE1_MOUSE Sprouty-related, EVH1 domain-containing protein 1 (Spred-1) 444 50,664 Alternative sequence (2); Chain (1); Domain (3); Initiator methionine (1); Modified residue (4); Sequence conflict (1) FUNCTION: Tyrosine kinase substrate that inhibits growth-factor-mediated activation of MAP kinase. Negatively regulates hematopoiesis of bone marrow. {ECO:0000269|PubMed:11493923, ECO:0000269|PubMed:15465815}. PTM: Phosphorylated on tyrosine. {ECO:0000269|PubMed:11493923}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11493923}; Peripheral membrane protein {ECO:0000269|PubMed:11493923}. Membrane, caveola {ECO:0000269|PubMed:11493923}; Peripheral membrane protein {ECO:0000269|PubMed:11493923}. Nucleus {ECO:0000269|PubMed:11493923}. Note=Localized in cholesterol-rich membrane raft/caveola fractions. {ECO:0000250}. SUBUNIT: Interacts with TAOK2 and TESK1 (By similarity). Homodimer and heterodimer. Interacts with CAV1. Able to interact with SPRED2 to form heterodimers (By similarity). Interacts with ras. {ECO:0000250, ECO:0000269|PubMed:11493923}. TISSUE SPECIFICITY: Expressed in brain. Weakly expressed in lung, heart, liver, kidney, intestine, spleen, testis, thymus, colon and ovary. Also expressed in embryonic tissues such as heart, lung, liver and brain. Highly expressed in IL3-dependent hematopoietic cell lines (Ba/F3 and MC/9) and bone marrow-derived mast cells (BMMC). {ECO:0000269|PubMed:11493923, ECO:0000269|PubMed:12646235, ECO:0000269|PubMed:15465815, ECO:0000269|PubMed:15580519}. +Q924S7 SPRE2_MOUSE Sprouty-related, EVH1 domain-containing protein 2 (Spred-2) 410 46,794 Chain (1); Domain (3); Modified residue (2) FUNCTION: Negatively regulates Ras signaling pathways and downstream activation of MAP kinases. {ECO:0000269|PubMed:11493923}. PTM: Phosphorylated on serine and threonine residues. Phosphorylated on tyrosine. Phosphorylation of Tyr-224 and Tyr-227 are required for ubiquitination. {ECO:0000250|UniProtKB:Q7Z698}.; PTM: Ubiquitinated; leading to degradation by the proteasome. {ECO:0000250|UniProtKB:Q7Z698}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11493923}; Peripheral membrane protein {ECO:0000269|PubMed:11493923}; Cytoplasmic side {ECO:0000269|PubMed:11493923}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:Q7Z698}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q7Z698}; Cytoplasmic side {ECO:0000250|UniProtKB:Q7Z698}. Cytoplasm {ECO:0000269|PubMed:11493923}. Note=Detected in the cytoplasm of the stratum spinosum cells, where it is associated with cytoplasmic vesicles that are supposed to be secretory granules. {ECO:0000250|UniProtKB:Q7Z698}. SUBUNIT: Homodimer and heterodimer. Able to interact with SPRED1 to form heterodimers (By similarity). Interacts with Ras (PubMed:11493923). May interact with ZDHHC13 (via ANK repeats) and ZDHHC17 (via ANK repeats) (PubMed:28882895). {ECO:0000250|UniProtKB:Q7Z698, ECO:0000269|PubMed:11493923, ECO:0000269|PubMed:28882895}. TISSUE SPECIFICITY: Predominantly expressed in lung, liver and testis. In testis, it is specially found in mature spermatids projecting into the lumen of the seminiferous. Strongly expressed in glandular epithelia. Also expressed in embryonic tissues such as heart, lung, liver and brain. {ECO:0000269|PubMed:11493923, ECO:0000269|PubMed:15580519}. +O09116 SPRR3_MOUSE Small proline-rich protein 3 (Cornifin beta) 238 25,241 Chain (1); Initiator methionine (1); Modified residue (1); Region (1); Repeat (21) FUNCTION: Cross-linked envelope protein of keratinocytes. SUBCELLULAR LOCATION: Cytoplasm. +Q9D0C4 TRM5_MOUSE tRNA (guanine(37)-N1)-methyltransferase (EC 2.1.1.228) (M1G-methyltransferase) (tRNA [GM37] methyltransferase) (tRNA methyltransferase 5 homolog) 501 56,794 Alternative sequence (1); Binding site (2); Chain (1); Region (2); Sequence conflict (1) FUNCTION: Involved in mitochondrial tRNA methylation (By similarity). Specifically methylates the N1 position of guanosine-37 in various tRNAs. Methylation is not dependent on the nature of the nucleoside 5' of the target nucleoside. This is the first step in the biosynthesis of wybutosine (yW), a modified base adjacent to the anticodon of tRNAs and required for accurate decoding. {ECO:0000250|UniProtKB:Q32P41, ECO:0000255|HAMAP-Rule:MF_03152}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-Rule:MF_03152}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03152}. Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03152}. Note=Predominantly in the mitochondria and in the nucleus. {ECO:0000255|HAMAP-Rule:MF_03152}. SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03152}. +Q9CUS9 SPPL3_MOUSE Signal peptide peptidase-like 3 (SPP-like 3) (EC 3.4.23.-) (Intramembrane protease 2) (IMP-2) (Presenilin-like protein 4) 384 42,261 Active site (2); Chain (1); Compositional bias (1); Erroneous initiation (1); Motif (1); Mutagenesis (2); Sequence conflict (2); Topological domain (10); Transmembrane (9) TRANSMEM 9 29 Helical. {ECO:0000255}.; TRANSMEM 74 94 Helical. {ECO:0000255}.; TRANSMEM 96 116 Helical. {ECO:0000255}.; TRANSMEM 139 159 Helical. {ECO:0000255}.; TRANSMEM 165 185 Helical. {ECO:0000255}.; TRANSMEM 191 211 Helical. {ECO:0000255}.; TRANSMEM 263 283 Helical. {ECO:0000255}.; TRANSMEM 312 332 Helical. {ECO:0000255}.; TRANSMEM 340 360 Helical. {ECO:0000255}. TOPO_DOM 1 8 Lumenal. {ECO:0000250|UniProtKB:Q8TCT6}.; TOPO_DOM 30 73 Cytoplasmic. {ECO:0000250|UniProtKB:Q8TCT6}.; TOPO_DOM 95 95 Lumenal. {ECO:0000255}.; TOPO_DOM 117 138 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 160 164 Lumenal. {ECO:0000255}.; TOPO_DOM 186 190 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 212 262 Lumenal. {ECO:0000250|UniProtKB:Q8TCT6}.; TOPO_DOM 284 311 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 333 339 Lumenal. {ECO:0000255}.; TOPO_DOM 361 384 Cytoplasmic. {ECO:0000250|UniProtKB:Q8TCT6}. FUNCTION: Intramembrane-cleaving aspartic protease (I-CLiP) that cleaves type II membrane protein substrates in or close to their luminal transmembrane domain boundaries. Acts like a sheddase by mediating the proteolytic release and secretion of active site-containing ectodomains of glycan-modifiying glycosidase and glycosyltransferase enzymes such as MGAT5, B4GAT1 and B4GALT1 (PubMed:25354954, PubMed:25827571). Plays a role in the regulation of cellular glycosylation processes (PubMed:25354954). Required to link T-cell antigen receptor (TCR) and calcineurin-NFAT signaling cascades in lymphocytes by promoting the association of STIM1 and ORAI1 during store-operated calcium entry (SOCE) in a protease-independent manner (PubMed:25384971). {ECO:0000269|PubMed:25354954, ECO:0000269|PubMed:25384971, ECO:0000269|PubMed:25827571}. PTM: Not glycosylated. {ECO:0000250|UniProtKB:Q8TCT6}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8TCT6}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8TCT6}. Golgi apparatus {ECO:0000250|UniProtKB:Q8TCT6}. Membrane {ECO:0000250|UniProtKB:Q8TCT6}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8TCT6}; Lumenal side {ECO:0000250|UniProtKB:Q8TCT6}. SUBUNIT: Monomer. Homodimer (By similarity). Interacts with STIM1 (via transmembrane region and SOAR/CAD domain); the interaction promotes the binding of STIM1 to ORAI1 (PubMed:25384971). {ECO:0000250|UniProtKB:Q8TCT6, ECO:0000269|PubMed:25384971}. DOMAIN: The first transmembrane domain may act as a type I signal anchor. The catalytic loops is exposed toward the lumen. The PAL motif is required for normal active site conformation. The catalytic domains embedded in the membrane are in the opposite orientation to that of the presenilin protein family. {ECO:0000250|UniProtKB:P49768, ECO:0000250|UniProtKB:Q8TCT6}. +Q8CE96 TRM6_MOUSE tRNA (adenine(58)-N(1))-methyltransferase non-catalytic subunit TRM6 (mRNA methyladenosine-N(1)-methyltransferase non-catalytic subunit TRM6) (tRNA(m1A58)-methyltransferase subunit TRM6) (tRNA(m1A58)MTase subunit TRM6) 497 55,518 Alternative sequence (3); Binding site (2); Chain (1); Erroneous initiation (1); Frameshift (1); Modified residue (1); Region (5); Sequence conflict (5) FUNCTION: Substrate-binding subunit of tRNA (adenine-N(1)-)-methyltransferase, which catalyzes the formation of N(1)-methyladenine at position 58 (m1A58) in initiator methionyl-tRNA. Together with the TRMT61A catalytic subunit, part of a mRNA N(1)-methyltransferase complex that mediates methylation of adenosine residues at the N(1) position of a small subset of mRNAs: N(1) methylation takes place in tRNA T-loop-like structures of mRNAs and is only present at low stoichiometries. {ECO:0000250|UniProtKB:Q9UJA5}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P41814}. SUBUNIT: Heterotetramer; composed of two copies of TRMT6 and two copies of TRMT61A. {ECO:0000250|UniProtKB:Q9UJA5}. +Q9DAQ9 SPT19_MOUSE Spermatogenesis-associated protein 19, mitochondrial (Spermatogenic cell-specific gene 1 protein) (Spergen-1) 154 18,057 Alternative sequence (2); Chain (1); Modified residue (2); Transit peptide (1) FUNCTION: May have a role in spermiogenesis. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:15139970}. TISSUE SPECIFICITY: Expressed specifically in adult testis. {ECO:0000269|PubMed:15139970}. +P97355 SPSY_MOUSE Spermine synthase (SPMSY) (EC 2.5.1.22) (Spermidine aminopropyltransferase) 366 41,313 Active site (1); Binding site (6); Chain (1); Domain (1); Initiator methionine (1); Modified residue (2); Region (1); Sequence conflict (2) Amine and polyamine biosynthesis; spermine biosynthesis; spermine from spermidine: step 1/1. FUNCTION: Catalyzes the production of spermine from spermidine and decarboxylated S-adenosylmethionine (dcSAM) (By similarity). Required for normal viability, growth and fertility. {ECO:0000250, ECO:0000269|PubMed:15459188}. SUBUNIT: Homodimer. Dimerization is mediated through the N-terminal domain and seems to be required for activity as deletion of the N-terminal domain causes complete loss of activity (By similarity). {ECO:0000250}. DOMAIN: Composed of 3 domains: the N-terminal domain has structural similarity to S-adenosylmethionine decarboxylase, the central domain is made up of four beta strands and the C-terminal domain is similar in structure to spermidine synthase. The N- and C-terminal domains are both required for activity (By similarity). {ECO:0000250}. +E9QAF0 SPT31_MOUSE Spermatogenesis-associated protein 31 (Acrosome-expressed protein 1) 1014 115,834 Chain (1); Sequence conflict (6); Transmembrane (1) TRANSMEM 22 42 Helical. {ECO:0000255}. FUNCTION: May play a role in spermatogenesis. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle, acrosome lumen {ECO:0000269|PubMed:20850414}. Note=Localizes to the inner and outer membranes as well as to the matrix of the acrosome. SUBUNIT: Interacts with ACTB and STX1A and/or STX1B. {ECO:0000269|PubMed:20850414}. +P63271 SPT4A_MOUSE Transcription elongation factor SPT4-A (DRB sensitivity-inducing factor small subunit 1) (DSIF small subunit 1) (Transcription elongation factor SPT4 1) 117 13,193 Chain (1); Initiator methionine (1); Modified residue (1); Region (1); Sequence conflict (1); Zinc finger (1) FUNCTION: Component of the DRB sensitivity-inducing factor complex (DSIF complex), which regulates mRNA processing and transcription elongation by RNA polymerase II. DSIF positively regulates mRNA capping by stimulating the mRNA guanylyltransferase activity of RNGTT/CAP1A. DSIF also acts cooperatively with the negative elongation factor complex (NELF complex) to enhance transcriptional pausing at sites proximal to the promoter. Transcriptional pausing may facilitate the assembly of an elongation competent RNA polymerase II complex. DSIF and NELF promote pausing by inhibition of the transcription elongation factor TFIIS/S-II. TFIIS/S-II binds to RNA polymerase II at transcription pause sites and stimulates the weak intrinsic nuclease activity of the enzyme. Cleavage of blocked transcripts by RNA polymerase II promotes the resumption of transcription from the new 3' terminus and may allow repeated attempts at transcription through natural pause sites (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with SUPT5H to form DSIF. DSIF interacts with the positive transcription elongation factor b complex (P-TEFb complex), which is composed of CDK9 and cyclin-T (CCNT1 or CCNT2). DSIF interacts with RNA polymerase II, and this interaction is reduced by phosphorylation of the C-terminal domain (CTD) of POLR2A by P-TEFb. DSIF also interacts with the NELF complex, which is composed of WHSC2/NELFA, COBRA1/NELFB, TH1L/NELFD and RDBP/NELFE, and this interaction occurs following prior binding of DSIF to RNA polymerase II. DSIF also interacts with HRMT1L2/PRMT1, HTATSF1/TATSF1, RNGTT/CAP1A, SKB1/PRMT5, SUPT6H, and can interact with PIN1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:8786137, ECO:0000269|PubMed:9776760}. +P62754 RS6_MOUSE 40S ribosomal protein S6 (Phosphoprotein NP33) 249 28,681 Chain (1); Cross-link (1); Modified residue (9) FUNCTION: May play an important role in controlling cell growth and proliferation through the selective translation of particular classes of mRNA. PTM: Ribosomal protein S6 is the major substrate of protein kinases in eukaryote ribosomes. The phosphorylation is stimulated by growth factors, tumor promoting agents, and mitogens. It is dephosphorylated at growth arrest. Phosphorylated at Ser-235 and Ser-236 by RPS6KA1 and RPS6KA3; phosphorylation at these sites facilitates the assembly of the preinitiation complex. {ECO:0000269|PubMed:1939282, ECO:0000269|PubMed:8440735}.; PTM: Specifically hydroxylated (with R stereochemistry) at C-3 of Arg-137 by KDM8. {ECO:0000250|UniProtKB:P62753}. +P62242 RS8_MOUSE 40S ribosomal protein S8 208 24,205 Chain (1); Cross-link (2); Initiator methionine (1); Lipidation (1); Modified residue (4); Sequence conflict (1) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250|UniProtKB:P62241}; Lipid-anchor {ECO:0000250|UniProtKB:P62241}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. {ECO:0000250}. SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. {ECO:0000250}. +Q6IMB1 RSLBA_MOUSE Ras-like protein family member 11A 242 27,067 Alternative sequence (1); Chain (1); Nucleotide binding (3); Region (1) FUNCTION: Regulator of rDNA transcription. Acts in cooperation UBF/UBTF and positively regulates RNA polymerase I transcription. {ECO:0000269|PubMed:20168301}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:20168301}. Note=Associates with rDNA transcription unit throughout the cell cycle. SUBUNIT: Interacts with UBF/UBTF. {ECO:0000269|PubMed:20168301}. +Q922H7 RSLBB_MOUSE Ras-like protein family member 11B 247 27,362 Alternative sequence (2); Chain (1); Nucleotide binding (3); Region (1); Sequence conflict (1) +Q62178 SEM4A_MOUSE Semaphorin-4A (Semaphorin-B) (Sema B) 760 83,421 Chain (1); Compositional bias (1); Disulfide bond (7); Domain (3); Glycosylation (4); Sequence conflict (5); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 683 703 Helical. {ECO:0000255}. TOPO_DOM 33 682 Extracellular. {ECO:0000255}.; TOPO_DOM 704 760 Cytoplasmic. {ECO:0000255}. FUNCTION: Cell surface receptor for PLXNB1, PLXNB2, PLXNB3 and PLXND1 that plays an important role in cell-cell signaling. Plays a role in priming antigen-specific T-cells, promotes differentiation of Th1 T-helper cells, and thereby contributes to adaptive immunity. Promotes phosphorylation of TIMD2. Inhibits angiogenesis. Promotes axon growth cone collapse. Inhibits axonal extension by providing local signals to specify territories inaccessible for growing axons. {ECO:0000269|PubMed:12374982, ECO:0000269|PubMed:15780988, ECO:0000269|PubMed:17318185, ECO:0000269|PubMed:20043131}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12374982, ECO:0000269|PubMed:15780988, ECO:0000269|PubMed:17318185, ECO:0000269|PubMed:20043131}; Single-pass type I membrane protein {ECO:0000269|PubMed:12374982, ECO:0000269|PubMed:15780988, ECO:0000269|PubMed:17318185, ECO:0000269|PubMed:20043131}. SUBUNIT: Interacts with PLXNB1, PLXNB2, PLXNB3 and PLXND1. Probable ligand for TIMD2. {ECO:0000269|PubMed:12374982, ECO:0000269|PubMed:17318185, ECO:0000269|PubMed:20043131}. +Q8C1B7 SEP11_MOUSE Septin-11 431 49,695 Alternative sequence (2); Binding site (3); Chain (1); Coiled coil (1); Domain (1); Initiator methionine (1); Modified residue (2); Nucleotide binding (2); Region (3); Sequence conflict (3) FUNCTION: Filament-forming cytoskeletal GTPase. May play a role in cytokinesis (Potential). May play a role in the cytoarchitecture of neurons, including dendritic arborization and dendritic spines, and in GABAergic synaptic connectivity (By similarity). {ECO:0000250, ECO:0000305}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17546647}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17546647}. Cell junction, synapse {ECO:0000269|PubMed:17546647}. Cell projection, dendritic spine {ECO:0000269|PubMed:17546647}. Cell projection, axon {ECO:0000250}. SUBUNIT: Septins polymerize into heterooligomeric protein complexes that form filaments, and can associate with cellular membranes, actin filaments and microtubules. GTPase activity is required for filament formation. Interacts with SEPT7, SEPT9 and SEPT12. Forms homooligomers (By similarity). {ECO:0000250}. +Q91ZX6 SENP2_MOUSE Sentrin-specific protease 2 (EC 3.4.22.-) (Axam2) (SUMO-1 protease 1) (SuPr-1) (SUMO-1/Smt3-specific isopeptidase 2) (Smt3ip2) (Sentrin/SUMO-specific protease SENP2) 588 67,579 Active site (3); Alternative sequence (2); Chain (1); Modified residue (3); Motif (3); Mutagenesis (1); Region (1); Sequence conflict (2) FUNCTION: Protease that catalyzes two essential functions in the SUMO pathway. The first is the hydrolysis of an alpha-linked peptide bond at the C-terminal end of the small ubiquitin-like modifier (SUMO) propeptides, SUMO1, SUMO2 and SUMO3 leading to the mature form of the proteins. The second is the deconjugation of SUMO1, SUMO2 and SUMO3 from targeted proteins, by cleaving an epsilon-linked peptide bond between the C-terminal glycine of the mature SUMO and the lysine epsilon-amino group of the target protein. May down-regulate CTNNB1 levels and thereby modulate the Wnt pathway. Deconjugates SUMO2 from MTA1 (By similarity). Plays a dynamic role in adipogenesis by desumoylating and promoting the stabilization of CEBPB (PubMed:20194620). Isoform 3 activates transcription. {ECO:0000250|UniProtKB:Q9EQE1, ECO:0000250|UniProtKB:Q9HC62, ECO:0000269|PubMed:11489887, ECO:0000269|PubMed:12419228, ECO:0000269|PubMed:20194620}. PTM: Polyubiquitinated; which leads to proteasomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Isoform 1: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q9HC62}. Nucleus membrane {ECO:0000250|UniProtKB:Q9HC62}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9HC62}; Nucleoplasmic side {ECO:0000250|UniProtKB:Q9HC62}. Note=Shuttles between cytoplasm and nucleus. {ECO:0000250|UniProtKB:Q9HC62}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Cytoplasmic vesicle. Note=Found in the cytoplasm and in cytoplasmic vesicles, together with axin. {ECO:0000269|PubMed:11489887}.; SUBCELLULAR LOCATION: Isoform 3: Nucleus, PML body {ECO:0000269|PubMed:12419228}. SUBUNIT: Binds to SUMO2 and SUMO3. Interacts with the C-terminal domain of NUP153 via its N-terminus. Interacts with MTA1 (By similarity). {ECO:0000250}. DOMAIN: The N-terminus is necessary and sufficient for nuclear envelope targeting. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in testis. Detected in brain, heart and thymus. {ECO:0000269|PubMed:12419228}. +O55131 SEPT7_MOUSE Septin-7 (CDC10 protein homolog) 436 50,550 Binding site (4); Chain (1); Coiled coil (1); Domain (1); Initiator methionine (1); Modified residue (8); Nucleotide binding (2); Region (4) FUNCTION: Filament-forming cytoskeletal GTPase. Required for normal organization of the actin cytoskeleton. Required for normal progress through mitosis. Involved in cytokinesis. Required for normal association of CENPE with the kinetochore. Plays a role in ciliogenesis and collective cell movements. Forms a filamentous structure with SEPT12, SEPT6, SEPT2 and probably SEPT4 at the sperm annulus which is required for the structural integrity and motility of the sperm tail during postmeiotic differentiation (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q16181}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17546647}. Chromosome, centromere, kinetochore {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Cleavage furrow {ECO:0000250}. Midbody {ECO:0000250}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q16181}. Note=Distributed throughout the cytoplasm in prometaphase cells. Associated with the spindle during metaphase. Associated with the central spindle and at the cleavage furrow in anaphase cells. Detected at the midbody in telophase (By similarity). Associated with actin stress fibers. Found in the sperm annulus (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q16181}. SUBUNIT: Septins polymerize into heterooligomeric protein complexes that form filaments, and associate with cellular membranes, actin filaments and microtubules. GTPase activity is required for filament formation. Filaments are assembled from asymmetrical heterotrimers, composed of SEPT2, SEPT6 and SEPT7 that associate head-to-head to form a hexameric unit. Within the trimer, directly interacts with SEPT6, while interaction with SEPT2 seems indirect. In the absence of SEPT6, forms homodimers. Interacts directly with CENPE and links CENPE to septin filaments composed of SEPT2, SEPT6 and SEPT7. Interacts with SEPT5, SEPT8, SEPT9 and SEPT11. Component of a septin core octomeric complex consisting of SEPT12, SEPT7, SEPT6 and SEPT2 or SEPT4 in the order 12-7-6-2-2-6-7-12 or 12-7-6-4-4-6-7-12 and located in the sperm annulus; the SEPT12:SEPT7 association is mediated by the respective GTP-binding domains (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q16181}. +P42208 SEPT2_MOUSE Septin-2 (Neural precursor cell expressed developmentally down-regulated protein 5) (NEDD-5) 361 41,526 Beta strand (12); Binding site (5); Chain (1); Domain (1); Helix (8); Modified residue (4); Mutagenesis (5); Nucleotide binding (2); Region (4); Site (1); Turn (2) FUNCTION: Filament-forming cytoskeletal GTPase. Forms a filamentous structure with SEPT12, SEPT6, SEPT2 and probably SEPT4 at the sperm annulus which is required for the structural integrity and motility of the sperm tail during postmeiotic differentiation (By similarity). Required for normal organization of the actin cytoskeleton. Plays a role in the biogenesis of polarized columnar-shaped epithelium by maintaining polyglutamylated microtubules, thus facilitating efficient vesicle transport, and by impeding MAP4 binding to tubulin. Required for the progression through mitosis. Forms a scaffold at the midplane of the mitotic splindle required to maintain CENPE localization at kinetochores and consequently chromosome congression. During anaphase, may be required for chromosome segregation and spindle elongation. Plays a role in ciliogenesis and collective cell movements (By similarity). In cilia, required for the integrity of the diffusion barrier at the base of the primary cilium that prevents diffusion of transmembrane proteins between the cilia and plasma membranes: probably acts by regulating the assembly of the tectonic-like complex (also named B9 complex) by localizing TMEM231 protein. {ECO:0000250, ECO:0000250|UniProtKB:Q15019, ECO:0000269|PubMed:20558667, ECO:0000269|PubMed:22179047, ECO:0000269|PubMed:9203580}. SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Cleavage furrow {ECO:0000250}. Midbody {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Cell projection, cilium membrane. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q15019}. Note=In metaphase cells, localized within the microtubule spindle. At the metaphase plate, in close apposition to the kinetochores of the congressed chromosomes. In cells undergoing cytokinesis, localized to the midbody, the ingressing cleavage furrow, and the central spindle (By similarity). In interphase and postmitotic cells, localised to fibrous or granular structures, depending on the growth state of the cell. Localizes at the base of the cilia near the morphological distinction between the cilia and plasma membranes. Found in the sperm annulus. {ECO:0000250, ECO:0000250|UniProtKB:Q15019}. SUBUNIT: Septins polymerize into heterooligomeric protein complexes that form filaments, and associate with cellular membranes, actin filaments and microtubules (By similarity). GTPase activity is required for filament formation (By similarity). Septin filaments are assembled from asymmetrical heterotrimers, composed of SEPT2, SEPT6 and SEPT7 that associate head-to-head to form a hexameric unit (By similarity). Interaction between SEPT2 and SEPT7 seems indirect (By similarity). Interacts also with SEPT9 and SEPT5 (PubMed:11739749). Interaction with SEPT4 not detected (PubMed:11739749). Component of a septin core octomeric complex consisting of SEPT12, SEPT7, SEPT6 and SEPT2 or SEPT4 in the order 12-7-6-2-2-6-7-12 or 12-7-6-4-4-6-7-12 and located in the sperm annulus (By similarity). Interacts with MAP4 (By similarity). Interacts with DZIP1L (By similarity). {ECO:0000250|UniProtKB:Q15019, ECO:0000269|PubMed:11739749}. TISSUE SPECIFICITY: Widely expressed. +Q5XK03 SERC4_MOUSE Serine incorporator 4 492 53,907 Chain (1); Frameshift (1); Sequence conflict (3); Transmembrane (10) TRANSMEM 59 79 Helical. {ECO:0000255}.; TRANSMEM 113 133 Helical. {ECO:0000255}.; TRANSMEM 148 168 Helical. {ECO:0000255}.; TRANSMEM 179 199 Helical. {ECO:0000255}.; TRANSMEM 219 239 Helical. {ECO:0000255}.; TRANSMEM 254 274 Helical. {ECO:0000255}.; TRANSMEM 281 301 Helical. {ECO:0000255}.; TRANSMEM 330 350 Helical. {ECO:0000255}.; TRANSMEM 421 441 Helical. {ECO:0000255}.; TRANSMEM 464 484 Helical. {ECO:0000255}. FUNCTION: Incorporates a polar amino acid serine into membranes and facilitates the synthesis of two serine-derived lipids, phosphatidylserine and sphingolipids. {ECO:0000250|UniProtKB:A6NH21}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +P97401 SFRP3_MOUSE Secreted frizzled-related protein 3 (sFRP-3) (Frezzled) (Fritz) (Frizzled-related protein 1) (FrzB-1) 323 36,011 Beta strand (3); Chain (1); Compositional bias (1); Disulfide bond (5); Domain (2); Glycosylation (1); Helix (7); Sequence conflict (1); Signal peptide (1); Turn (2) FUNCTION: Soluble frizzled-related proteins (sFRPS) function as modulators of Wnt signaling through direct interaction with Wnts. They have a role in regulating cell growth and differentiation in specific cell types. SFRP3/FRZB appears to be involved in limb skeletogenesis. Antagonist of Wnt8 signaling. Regulates chondrocyte maturation and long bone development (By similarity). {ECO:0000250, ECO:0000269|PubMed:9178261}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. SUBUNIT: Interacts with MYOC. {ECO:0000269|PubMed:19188438}. DOMAIN: The FZ domain is involved in binding with Wnt ligands. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in kidney, brain, testis. Weak expression in spleen and heart. {ECO:0000269|PubMed:9096311, ECO:0000269|PubMed:9178261}. +Q99NB9 SF3B1_MOUSE Splicing factor 3B subunit 1 (Pre-mRNA-splicing factor SF3b 155 kDa subunit) (SF3b155) (Spliceosome-associated protein 155) (SAP 155) 1304 145,816 Chain (1); Cross-link (4); Modified residue (42); Region (4); Repeat (11); Site (9) FUNCTION: Involved in pre-mRNA splicing as a component of the splicing factor SF3B complex. SF3B complex is required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA. May also be involved in the assembly of the 'E' complex. Belongs also to the minor U12-dependent spliceosome, which is involved in the splicing of rare class of nuclear pre-mRNA intron. {ECO:0000250|UniProtKB:O75533}. PTM: Phosphorylated. Phosphorylation occurs concomitantly with the splicing catalytic steps. Phosphorylation on Thr-244, Thr-248 and Thr-313 by cyclin-dependent kinases promotes interaction with PPP1R8 during mitosis (By similarity). {ECO:0000250}.; PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O75533}. SUBUNIT: Component of the B-WICH complex, at least composed of SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21. Identified in the spliceosome C complex. Component of the U11/U12 snRNPs that are part of the U12-type spliceosome. Component of splicing factor SF3B complex which is composed of at least eight subunits; SF3B1, SF3B2, SF3B3, SF3B4, SF3B5, SF3B6, PHF5A and DDX42. SF3B associates with the splicing factor SF3A and a 12S RNA unit to form the U2 small nuclear ribonucleoproteins complex (U2 snRNP). Interacts directly with the splicing factor U2AF. Within the SF3B complex interacts directly (via HEAT domain) with SF3B3, SF3B5 and (via HEAT domain) with PHF5A. Interacts directly with SF3B6. The SF3B complex composed of SF3B1, SF3B2, SF3B3, SF3B4, SF3B5, SF3B6 and PHF5A interacts with U2AF2. Phosphorylated form interacts with PPP1R8. Interacts with PQBP1. Interacts with RBM17. Interacts with RBM39. Interacts with SETX. Interacts with RBM15. Interacts with ZRSR1 (PubMed:29617656). {ECO:0000250|UniProtKB:O75533, ECO:0000269|PubMed:29617656}. TISSUE SPECIFICITY: Ubiquitous. +Q921M3 SF3B3_MOUSE Splicing factor 3B subunit 3 (Pre-mRNA-splicing factor SF3b 130 kDa subunit) (SF3b130) (Spliceosome-associated protein 130) (SAP 130) 1217 135,550 Alternative sequence (1); Chain (1); Modified residue (2); Region (6); Sequence conflict (3); Site (6) FUNCTION: Involved in pre-mRNA splicing as a component of the splicing factor SF3B complex, a constituent of the spliceosome. SF3B complex is required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA. May also be involved in the assembly of the 'E' complex. Belongs also to the minor U12-dependent spliceosome, which is involved in the splicing of rare class of nuclear pre-mRNA intron. {ECO:0000250|UniProtKB:Q15393}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15393}. SUBUNIT: Identified in the spliceosome A complex; remains associated with the spliceosome throughout the splicing process. Component of the spliceosome B complex. Identified in the spliceosome C complex. Identified in the spliceosome E complex. Component of the U11/U12 snRNPs that are part of the U12-type spliceosome. Component of splicing factor SF3B complex which is composed of at least eight subunits; SF3B1, SF3B2, SF3B3, SF3B4, SF3B5, SF3B6, PHF5A and DDX42. SF3B associates with the splicing factor SF3A and a 12S RNA unit to form the U2 small nuclear ribonucleoproteins complex (U2 snRNP). Interaction between SF3B3 and SF3B1 is tighter than the interaction between SF3B3 and SF3B2. Within the SF3B complex interacts directly with SF3B1 (via HEAT domain), SF3B5 and PHF5A. The SF3B complex composed of SF3B1, SF3B2, SF3B3, SF3B4, SF3B5, SF3B6 and PHF5A interacts with U2AF2. Associates with the STAGA transcription coactivator-HAT complex. Interacts with SUPT3H. Interacts with TAF3. {ECO:0000250|UniProtKB:Q15393}. DOMAIN: The core of the protein consists of three beta-propeller domains. {ECO:0000250|UniProtKB:Q15393}. +P35242 SFTPA_MOUSE Pulmonary surfactant-associated protein A (PSAP) (PSP-A) (SP-A) 248 26,157 Chain (1); Disulfide bond (3); Domain (2); Glycosylation (2); Metal binding (4); Modified residue (10); Signal peptide (1) FUNCTION: In presence of calcium ions, it binds to surfactant phospholipids and contributes to lower the surface tension at the air-liquid interface in the alveoli of the mammalian lung and is essential for normal respiration. Enhances the expression of MYO18A/SP-R210 on alveolar macrophages (PubMed:25965346). {ECO:0000269|PubMed:25965346}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. Secreted, extracellular space, surface film. SUBUNIT: Oligomeric complex of 6 set of homotrimers. {ECO:0000250|UniProtKB:Q8IWL2}. +P50404 SFTPD_MOUSE Pulmonary surfactant-associated protein D (PSP-D) (SP-D) (Lung surfactant protein D) 374 37,688 Chain (1); Coiled coil (1); Disulfide bond (2); Domain (2); Glycosylation (1); Modified residue (2); Signal peptide (1) FUNCTION: Contributes to the lung's defense against inhaled microorganisms, organic antigens and toxins. Interacts with compounds such as bacterial lipopolysaccharides, oligosaccharides and fatty acids and modulates leukocyte action in immune response. May participate in the extracellular reorganization or turnover of pulmonary surfactant. Binds strongly maltose residues and to a lesser extent other alpha-glucosyl moieties. PTM: S-nitrosylation at Cys-34 and Cys-39 alters the quaternary structure which results in a pro-inflammatory chemoattractive signaling activity with macrophages. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. Secreted, extracellular space, surface film. SUBUNIT: Oligomeric complex of 4 set of homotrimers. +Q8BP27 SFR1_MOUSE Swi5-dependent recombination DNA repair protein 1 homolog (Meiosis protein 5 homolog) 319 35,183 Alternative sequence (3); Chain (1); Coiled coil (1); Compositional bias (1); Frameshift (1); Modified residue (8); Sequence conflict (6) FUNCTION: Component of the SWI5-SFR1 complex, a complex required for double-strand break repair via homologous recombination (PubMed:20976249). Acts as a transcriptional modulator for ESR1. {ECO:0000250|UniProtKB:Q86XK3, ECO:0000269|PubMed:20976249}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20976249}. SUBUNIT: Component of the SWI5-SFR1 complex (PubMed:20976249). Interacts with RAD51; the interaction is weak (By similarity). {ECO:0000250|UniProtKB:Q86XK3, ECO:0000269|PubMed:20976249}. +Q925N2 SFXN2_MOUSE Sideroflexin-2 322 36,141 Chain (1); Modified residue (1); Sequence conflict (1); Transmembrane (5) TRANSMEM 99 119 Helical. {ECO:0000255}.; TRANSMEM 147 167 Helical. {ECO:0000255}.; TRANSMEM 174 194 Helical. {ECO:0000255}.; TRANSMEM 223 243 Helical. {ECO:0000255}.; TRANSMEM 266 286 Helical. {ECO:0000255}. FUNCTION: Potential iron transporter. SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain, heart, kidney, spleen, thymus, liver, stomach and skin. {ECO:0000269|PubMed:11274051}. +P98083 SHC1_MOUSE SHC-transforming protein 1 (SHC-transforming protein A) (Src homology 2 domain-containing-transforming protein C1) (SH2 domain protein C1) 579 62,608 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (2); Modified residue (8); Region (1) FUNCTION: Signaling adapter that couples activated growth factor receptors to signaling pathways. Participates in signaling downstream of the angiopoietin receptor TEK/TIE2, and plays a role in the regulation of endothelial cell migration and sprouting angiogenesis (By similarity). Participates in a signaling cascade initiated by activated KIT and KITLG/SCF. Isoform p47Shc and isoform p52Shc, once phosphorylated, couple activated receptor kinases to Ras via the recruitment of the GRB2/SOS complex and are implicated in the cytoplasmic propagation of mitogenic signals. Isoform p47Shc and isoform p52 may thus function as initiators of the Ras signaling cascade in various non-neuronal systems. Isoform p66Shc does not mediate Ras activation, but is involved in signal transduction pathways that regulate the cellular response to oxidative stress and life span. Isoform p66Shc acts as a downstream target of the tumor suppressor p53 and is indispensable for the ability of stress-activated p53 to induce elevation of intracellular oxidants, cytochrome c release and apoptosis. The expression of isoform p66Shc has been correlated with life span. {ECO:0000250, ECO:0000269|PubMed:12571362, ECO:0000269|PubMed:17272725}. PTM: Phosphorylated in response to FLT4 signaling (By similarity). Tyrosine phosphorylated by ligand-activated PDGFRB (By similarity). May be tyrosine phosphorylated by activated PTK2/FAK1 (By similarity). Tyrosine phosphorylated by TEK/TIE2 (By similarity). Tyrosine phosphorylated by activated PTK2B/PYK2 (By similarity). Dephosphorylation by PTPN2 may regulate interaction with GRB2 (By similarity). Phosphorylated by activated epidermal growth factor receptor. Phosphorylated in response to KIT signaling. Isoform p47Shc and isoform p52Shc are phosphorylated on tyrosine residues of the Pro-rich domain. Isoform p66Shc is phosphorylated on Ser-36 by PRKCB upon treatment with insulin, hydrogen peroxide or irradiation with ultraviolet light. FLT3 signaling promotes tyrosine phosphorylation of isoform p47Shc and isoform p52Shc. Also tyrosine phosphorylated by ligand-activated ALK. {ECO:0000250, ECO:0000269|PubMed:10080542, ECO:0000269|PubMed:9165038}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform p47Shc: Mitochondrion matrix {ECO:0000250}. Note=Targeting of isoform p47Shc to mitochondria is mediated by its first 32 amino acids, which behave as a bona fide mitochondrial targeting sequence. Isoform p52Shc and isoform p66Shc, that contain the same sequence but more internally located, display a different subcellular localization (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform p66Shc: Mitochondrion {ECO:0000269|PubMed:17272725}. Note=In case of oxidative conditions, phosphorylation at 'Ser-36' of isoform p66Shc, leads to mitochondrial accumulation. SUBUNIT: Interacts with CPNE3; this interaction may mediate the binding of CPNE3 with ERBB2 (By similarity). Interacts with the NPXY motif of tyrosine-phosphorylated IGF1R and INSR in vitro via the PID domain. Once activated, binds to GRB2. Interacts with tyrosine-phosphorylated DDR2 and CD3T. Interacts with the N-terminal region of APS. Interacts with GRB7 and KIT (By similarity). Interacts with PTK2/FAK1 (By similarity). Interacts with phosphorylated LRP1 and IRS4. Interacts with FLT4 (tyrosine-phosphorylated) (By similarity). Interacts with PDGFRB (tyrosine-phosphorylated). Interacts with ERBB4 (By similarity). Interacts with TEK/TIE2 (tyrosine-phosphorylated) (By similarity). Interacts with ALK, GAB2, TRIM31, INPP5D/SHIP1 and INPPL1/SHIP2. Interacts with PTPN6/SHP (tyrosine phosphorylated). Identified in a complex containing FGFR4, NCAM1, CDH2, PLCG1, FRS2, SRC, SHC1, GAP43 and CTTN. Interacts with EPHB1 and GRB2; activates the MAPK/ERK cascade to regulate cell migration. Interacts with the Trk receptors NTRK1, NTRK2 and NTRK3; in a phosphotyrosine-dependent manner. Interacts with CEACAM1; this interaction is CEACAM1-phosphorylation-dependent and mediates interaction with EGFR or INSR resulting in decrease coupling of SHC1 to the MAPK3/ERK1-MAPK1/ERK2 pathway (By similarity) (PubMed:15467833). Interacts (via PID domain) with PEAK1 (when phosphorylated at 'Tyr-1177') (By similarity). Found in a complex with PPP1CA, PPP1CC, SHC1 and PEAK1 (By similarity). {ECO:0000250|UniProtKB:P29353, ECO:0000250|UniProtKB:Q5M824, ECO:0000269|PubMed:10068665, ECO:0000269|PubMed:10080542, ECO:0000269|PubMed:10395202, ECO:0000269|PubMed:11433297, ECO:0000269|PubMed:12367511, ECO:0000269|PubMed:12925710, ECO:0000269|PubMed:15467833, ECO:0000269|PubMed:19665990, ECO:0000269|PubMed:8643691, ECO:0000269|PubMed:8654924, ECO:0000269|PubMed:9083021, ECO:0000269|PubMed:9099679, ECO:0000269|PubMed:9885561}. DOMAIN: In response to a variety of growth factors, isoform p47Shc and isoform p52 bind to phosphorylated receptors through their phosphotyrosine binding (PID) and/or SH2 domains. The PID and SH2 domains bind to specific phosphorylated tyrosine residues in the Asn-Pro-Xaa-Tyr(P) motif. Isoform p47Shc and isoform p52Shc are in turn phosphorylated on three tyrosine residues within the extended proline-rich domain. These phosphotyrosines act as docking site for GRB2 and thereby are involved in Ras activation. TISSUE SPECIFICITY: Widely expressed. Expressed in neural stem cells but absent in mature neurons. +Q9D413 SH2D6_MOUSE SH2 domain-containing protein 6 297 32,016 Alternative sequence (1); Chain (1); Domain (1); Erroneous initiation (1); Sequence conflict (1) +Q9CXH7 SGO1_MOUSE Shugoshin 1 (Shugoshin-like 1) 517 58,966 Alternative sequence (2); Chain (1); Coiled coil (2); Modified residue (2); Motif (2); Region (1); Sequence conflict (3) FUNCTION: Plays a central role in chromosome cohesion during mitosis by preventing premature dissociation of cohesin complex from centromeres after prophase, when most of cohesin complex dissociates from chromosomes arms. May act by preventing phosphorylation of the STAG2 subunit of cohesin complex at the centromere, ensuring cohesin persistence at centromere until cohesin cleavage by ESPL1/separase at anaphase. Essential for proper chromosome segregation during mitosis and this function requires interaction with PPP2R1A. Its phosphorylated form is necessary for chromosome congression and for the proper attachment of spindle microtubule to the kinetochore. Necessary for kinetochore localization of PLK1 and CENPF. May play a role in the tension sensing mechanism of the spindle-assembly checkpoint by regulating PLK1 kinetochore affinity. Involved in centromeric enrichment of AUKRB in prometaphase. {ECO:0000250|UniProtKB:Q5FBB7, ECO:0000269|PubMed:18084284, ECO:0000269|PubMed:18331714}. PTM: Ubiquitinated and degraded during mitotic exit by APC/C-Cdh1. {ECO:0000250}.; PTM: Phosphorylation by NEK2 is essential for chromosome congression in mitosis and for the proper attachment of spindle microtubule to the kinetochore. Phosphorylated by PLK1 and AUKRB (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5FBB7}. Chromosome, centromere {ECO:0000250|UniProtKB:Q5FBB7}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q5FBB7}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q5FBB7}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q5FBB7}. Note=Localizes to the inner centromere throughout prophase until metaphase and disappears at anaphase. Centromeric localization requires the presence of BUB1 and the interaction with PPP2R1A. Colocalizes with NEK2 at the kinetochore. Colocalizes with and SS18L1 at the kinetochore. Phosphorylation by AUKRB and the presence of BUB1 are required for localization to the kinetochore. Isoform 1 primarily localizes to kinetochores during G2 phase and mitotic prophase, metaphase, and anaphase and does not appear to be associated with kinetochores during late mitosis. Isoform 3 is found at the centrosome in interphase and at spindle poles in mitosis and its spindle pole localization is PLK1 dependent. Isoform 3 does not localize to kinetochores during any stages of the cell cycle. {ECO:0000250|UniProtKB:Q5FBB7}. SUBUNIT: Interacts with PPP2CA (or PPP2CB), PPP2R1B, PPP2R5A, PPP2R5B, PPP2R5C, PPP2R5D, PPP2R5E, SET, LRRC59, RBM10 (or RBM5), RPL10A, RPL28, RPL7, RPL7A and RPLP1. Interaction with protein phosphatase 2A occurs most probably through direct binding to the regulatory B56 subunits: PPP2R1B, PPP2R5A, PPP2R5B, PPP2R5C, PPP2R5D, PPP2R5E. Interacts with PPP2R1A and NEK2. Interacts with CDCA8 (By similarity). {ECO:0000250|UniProtKB:Q5FBB7}. TISSUE SPECIFICITY: Ubiquitously expressed in proliferating cells. Moderately expressed in the oocytes. {ECO:0000269|PubMed:18084284}. +Q6S5L9 SHC4_MOUSE SHC-transforming protein 4 (Rai-like protein) (RaLP) (SHC-transforming protein D) (mShcD) (Src homology 2 domain-containing-transforming protein C4) (SH2 domain protein C4) 626 68,519 Chain (1); Domain (2); Modified residue (1); Region (2) FUNCTION: Activates both Ras-dependent and Ras-independent migratory pathways in melanomas. Contributes to the early phases of agrin-induced tyrosine phosphorylation of CHRNB1. {ECO:0000269|PubMed:17452444}. PTM: Phosphorylated; the phosphorylation is enhanced by EGF. Phosphorylation at Tyr-422 is required for the interaction with GRB2 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane {ECO:0000269|PubMed:17452444}. Note=Colocalized with MUSK at the neuromuscular junction. SUBUNIT: Interacts (via PID domain) with phosphorylated MUSK (via NPXY motif); undergoes tyrosine phosphorylation downstream of activated MUSK. Interacts with GRB2; the interaction is dependent of Tyr-422 phosphorylation and increased by EGF (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in both brain and skeletal muscle; widely expressed in brain namely olfactory bulb, cortex, hippocampus, striatum, thalamus, and brain stem (at protein level). Only expressed in melanomas. Weakly expressed in normal melanocytes and benign nevi. Highly expressed at the transition from radial growth phase to vertical growth phase and metastatic melanomas, when tumor cells acquire migratory competence and invasive potential. {ECO:0000269|PubMed:17452444}. +Q8R0X7 SGPL1_MOUSE Sphingosine-1-phosphate lyase 1 (S1PL) (SP-lyase 1) (SPL 1) (mSPL) (EC 4.1.2.27) (Sphingosine-1-phosphate aldolase) 568 63,677 Chain (1); Modified residue (5); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 41 61 Helical; Signal-anchor for type III membrane protein. {ECO:0000255}. TOPO_DOM 1 40 Lumenal. {ECO:0000255}.; TOPO_DOM 62 568 Cytoplasmic. {ECO:0000255}. Lipid metabolism; sphingolipid metabolism. FUNCTION: Cleaves phosphorylated sphingoid bases (PSBs), such as sphingosine-1-phosphate, into fatty aldehydes and phosphoethanolamine. Elevates stress-induced ceramide production and apoptosis. {ECO:0000269|PubMed:9464245}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:28165339}; Single-pass type III membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Highest levels are found in liver, followed by kidney, lung, heart and brain. {ECO:0000269|PubMed:28165339, ECO:0000269|PubMed:9464245}. +Q8JZW5 SH2D5_MOUSE SH2 domain-containing protein 5 429 47,380 Chain (1); Domain (1); Erroneous initiation (1) FUNCTION: May be involved in synaptic plasticity regulation through the control of Rac-GTP levels. {ECO:0000303|PubMed:25331951}. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000269|PubMed:25331951}. SUBUNIT: Interacts with BCR. {ECO:0000269|PubMed:25331951}. TISSUE SPECIFICITY: Highly expressed in brain, particularly in Purkinjie cells in the cerebellum and the cornu ammonis of the hippocampus. {ECO:0000269|PubMed:25331951}. +Q80TE4 SI1L2_MOUSE Signal-induced proliferation-associated 1-like protein 2 (SIPA1-like protein 2) 1722 189,413 Alternative sequence (1); Chain (1); Coiled coil (1); Compositional bias (4); Domain (2); Modified residue (12); Sequence conflict (2) +Q8CA71 SHSA4_MOUSE Protein shisa-4 (Transmembrane protein 58) 197 21,483 Chain (1); Compositional bias (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 88 108 Helical. {ECO:0000255}. TOPO_DOM 28 87 Extracellular. {ECO:0000255}.; TOPO_DOM 109 197 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q9D7I0 SHSA5_MOUSE Protein shisa-5 (Scotin) 235 25,517 Alternative sequence (5); Chain (1); Compositional bias (3); Sequence caution (1); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 106 126 Helical. {ECO:0000255}. TOPO_DOM 27 105 Extracellular. {ECO:0000255}.; TOPO_DOM 127 235 Cytoplasmic. {ECO:0000255}. FUNCTION: Can induce apoptosis in a caspase-dependent manner and plays a role in p53/TP53-dependent apoptosis. {ECO:0000269|PubMed:12135983}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12135983}; Single-pass type I membrane protein {ECO:0000269|PubMed:12135983}. Nucleus membrane {ECO:0000269|PubMed:12135983}. SUBUNIT: Interacts with PDCD6; PDCD6 can stabilze SHISA5. {ECO:0000269|PubMed:17889823}. DOMAIN: The proline-rich region is required for endoplasmic reticulum localization. {ECO:0000269|PubMed:12135983}. TISSUE SPECIFICITY: Spleen and thymus. +Q6PDG5 SMRC2_MOUSE SWI/SNF complex subunit SMARCC2 (BRG1-associated factor 170) (BAF170) (SWI/SNF complex 170 kDa subunit) (SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily C member 2) 1213 132,604 Alternative sequence (1); Chain (1); Coiled coil (1); Compositional bias (5); Cross-link (7); Domain (2); Modified residue (9); Sequence conflict (1) FUNCTION: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. Can stimulate the ATPase activity of the catalytic subunit of these complexes. May be required for CoREST dependent repression of neuronal specific gene promoters in non-neuronal cells. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (PubMed:17640523). Critical regulator of myeloid differentiation, controlling granulocytopoiesis and the expression of genes involved in neutrophil granule formation (PubMed:28369036). {ECO:0000269|PubMed:17640523, ECO:0000269|PubMed:28369036, ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Component of the multiprotein chromatin-remodeling complexes SWI/SNF: SWI/SNF-A (BAF), SWI/SNF-B (PBAF) and related complexes. The canonical complex contains a catalytic subunit (either SMARCA4/BRG1/BAF190A or SMARCA2/BRM/BAF190B) and at least SMARCE1, ACTL6A/BAF53, SMARCC1/BAF155, SMARCC2/BAF170, and SMARCB1/SNF5/BAF47. Other subunits specific to each of the complexes may also be present permitting several possible combinations developmentally and tissue specific (Probable). Component of the BAF complex, which includes at least actin (ACTB), ARID1A/BAF250A, ARID1B/BAF250B, SMARCA2/BRM, SMARCA4/BRG1, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57, SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C. In muscle cells, the BAF complex also contains DPF3. Component of neural progenitors-specific chromatin remodeling complex (npBAF complex) composed of at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, PHF10/BAF45A, ACTL6A/BAF53A and actin. Component of neuron-specific chromatin remodeling complex (nBAF complex) composed of at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, DPF1/BAF45B, DPF3/BAF45C, ACTL6B/BAF53B and actin (PubMed:17640523). Component of the SWI/SNF-B (PBAF) chromatin remodeling complex, at least composed of SMARCA4/BRG1, SMARCB1/BAF47/SNF5, ACTL6A/BAF53A or ACTL6B/BAF53B, SMARCE1/BAF57, SMARCD1/BAF60A, SMARCD2/BAF60B, perhaps SMARCD3/BAF60C, SMARCC1/BAF155, SMARCC2/BAF170, PBRM1/BAF180, ARID2/BAF200 and actin (PubMed:22952240, PubMed:26601204). May also interact with the SIN3A histone deacetylase transcription repressor complex in conjunction with SMARCA2 and SMARCA4. Interacts with SMARD1 (By similarity). Interacts with KDM6B (PubMed:21095589). Interaction with RCOR1 (By similarity). Interacts with DPF2 (By similarity). {ECO:0000250|UniProtKB:Q8TAQ2, ECO:0000269|PubMed:17640523, ECO:0000269|PubMed:21095589, ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}. +Q8BKX6 SMG1_MOUSE Serine/threonine-protein kinase SMG1 (SMG-1) (EC 2.7.11.1) 3658 409,769 Alternative sequence (4); Chain (1); Domain (3); Erroneous initiation (1); Modified residue (6); Repeat (1); Sequence conflict (1) FUNCTION: Serine/threonine protein kinase involved in both mRNA surveillance and genotoxic stress response pathways. Recognizes the substrate consensus sequence [ST]-Q. Plays a central role in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons by phosphorylating UPF1/RENT1. Recruited by release factors to stalled ribosomes together with SMG8 and SMG9 (forming the SMG1C protein kinase complex), and UPF1 to form the transient SURF (SMG1-UPF1-eRF1-eRF3) complex. In EJC-dependent NMD, the SURF complex associates with the exon junction complex (EJC) through UPF2 and allows the formation of an UPF1-UPF2-UPF3 surveillance complex which is believed to activate NMD. Also acts as a genotoxic stress-activated protein kinase that displays some functional overlap with ATM. Can phosphorylate p53/TP53 and is required for optimal p53/TP53 activation after cellular exposure to genotoxic stress. Its depletion leads to spontaneous DNA damage and increased sensitivity to ionizing radiation (IR). May activate PRKCI but not PRKCZ (By similarity). {ECO:0000250}. PTM: Autophosphorylated. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. SUBUNIT: Component of the SMG1C complex composed of SMG1, SMG8 and SMG9; the recruitment of SMG8 to SMG1 N-terminus induces a large conformational change in the SMG1 C-terminal head domain containing the catalytic domain. Component of the transient SURF (SMG1-UPF1-eRF1-eRF3) complex. Interacts with PRKCI. Interacts with TELO2 and TTI1. Interacts with RUVBL1 and RUVBL2. +Q6ZPY2 SMG5_MOUSE Protein SMG5 (EST1-like protein B) (SMG-5 homolog) 1017 114,071 Alternative sequence (2); Chain (1); Coiled coil (1); Compositional bias (1); Domain (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (3); Natural variant (4) FUNCTION: Plays a role in nonsense-mediated mRNA decay. Does not have RNase activity by itself. Promotes dephosphorylation of UPF1. Together with SMG7 is thought provide a link to the mRNA degradation machinery involving exonucleolytic pathways, and to serve as an adapter for UPF1 to protein phosphatase 2A (PP2A), thereby triggering UPF1 dephosphorylation. Necessary for TERT activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Detected in cytoplasmic mRNA decay bodies. {ECO:0000250}. SUBUNIT: Interacts with TERT, PPP2CA and SMG1. Part of a complex that contains SMG1, SMG5, SMG7, PPP2CA, a short isoform of UPF3A (isoform UPF3AS, but not isoform UPF3AL) and phosphorylated UPF1. Not detected in complexes that contain unphosphorylated UPF1. +O09133 SMR2A_MOUSE Submaxillary gland androgen-regulated protein 2, isoform alpha (Salivary protein MSG2, isoform alpha) 150 16,630 Chain (1); Signal peptide (1) FUNCTION: May play a role in protection or detoxification. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +O35982 SMR2B_MOUSE Submaxillary gland androgen-regulated protein 2, isoform beta (Salivary protein MSG2, isoform beta) 41 4,885 Chain (1); Signal peptide (1) FUNCTION: May play a role in protection or detoxification. SUBCELLULAR LOCATION: Secreted. +Q921U8 SMTN_MOUSE Smoothelin 923 100,289 Alternative sequence (2); Chain (1); Coiled coil (2); Compositional bias (4); Domain (1); Initiator methionine (1); Modified residue (14); Sequence conflict (32) FUNCTION: Structural protein of the cytoskeleton. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Note=Exhibits a filamentous organization. {ECO:0000250}. +Q8R570 SNP47_MOUSE Synaptosomal-associated protein 47 (SNAP-47) (Synaptosomal-associated 47 kDa protein) 413 46,524 Alternative sequence (2); Chain (1); Domain (2); Frameshift (1); Sequence conflict (1) FUNCTION: May play a role in intracellular membrane fusion. {ECO:0000269|PubMed:16621800}. SUBCELLULAR LOCATION: Endomembrane system {ECO:0000269|PubMed:16621800}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16621800}. Note=Appears to be exclusively membrane-bound. In primary neurons, widely distributed in both cell bodies and neuronal processes. SUBUNIT: Associates with the BLOC-1 complex. Interacts with BLOC1S6 (By similarity). Forms a complex containing SNAP47, VAMP2 and STX1A. {ECO:0000250, ECO:0000269|PubMed:16621800}. TISSUE SPECIFICITY: Ubiquitously expressed with the most abundant expression in the brain. In brain, most highly expressed in the glomerular layer of the olfactory bulb, the cortex, striatum, hippocampus, and colliculi (at protein level). {ECO:0000269|PubMed:16621800}. +Q02085 SNAI1_MOUSE Zinc finger protein SNAI1 (Protein snail homolog 1) (Protein sna) 264 29,190 Chain (1); Compositional bias (1); Cross-link (3); Glycosylation (1); Modified residue (12); Motif (1); Region (4); Sequence conflict (1); Zinc finger (4) FUNCTION: Involved in induction of the epithelial to mesenchymal transition (EMT), formation and maintenance of embryonic mesoderm, growth arrest, survival and cell migration. Binds to 3 E-boxes of the E-cadherin gene promoter and to the promoters of CLDN7 and KRT8 and, in association with histone demethylase KDM1A which it recruits to the promoters, causes a decrease in dimethylated H3K4 levels and represses transcription. During EMT, involved with LOXL2 in negatively regulating pericentromeric heterochromatin transcription (PubMed:24239292). SNAI1 recruits LOXL2 to pericentromeric regions to oxidize histone H3 and repress transcription which leads to release of heterochromatin component CBX5/HP1A, enabling chromatin reorganization and acquisition of mesenchymal traits (PubMed:24239292). Associates with EGR1 and SP1 to mediate 12-O-tetradecanoylphorbol-13-acetate (TPA)-induced up-regulation of CDKN2B, possibly by binding to the CDKN2B promoter region 5'-TCACA-3'. In addition, may also activate the CDKN2B promoter by itself. {ECO:0000269|PubMed:10655586, ECO:0000269|PubMed:11689706, ECO:0000269|PubMed:24239292}. PTM: Phosphorylated by GSK3B. Once phosphorylated, it becomes a target for BTRC ubiquitination. Phosphorylation by CSNK1E, probably at Ser-104, provides the priming site for the subsequent phosphorylation by GSK3B, probably at Ser-100 and Ser-96. Phosphorylation by PAK1 may modulate its transcriptional activity by promoting increased accumulation in the nucleus. Phosphorylation at Ser-11 and Ser-104 positively regulates its function in induction of EMT and/or cell survival, respectively. Phosphorylation by LATS2, upon mitotic stress, oncogenic stress or Hippo pathway activation, occurs in the nucleus and promotes nuclear retention and stabilization of total cellular protein level (By similarity). {ECO:0000250}.; PTM: Ubiquitinated on Lys-98, Lys-137 and Lys-146 by FBXL14 and BTRC leading to degradation. BTRC-triggered ubiquitination requires previous GSK3B-mediated SNAI1 phosphorylation. Ubiquitination induced upon interaction with NOTCH1 or p53 is mediated by MDM2 (By similarity). {ECO:0000250}.; PTM: O-GlcNAcylation at Ser-112 is enhanced in hyperglycaemic conditions, it opposes phosphorylation by GSK3B, and stabilizes the protein. {ECO:0000250}.; PTM: ADP-ribosylation by PARP1 increases protein half-life and may be involved in TGFB-induced SNAI1 up-regulation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12832491}. Cytoplasm {ECO:0000269|PubMed:12832491}. Note=Once phosphorylated (probably on Ser-107, Ser-111, Ser-115 and Ser-119) it is exported from the nucleus to the cytoplasm where subsequent phosphorylation of the destruction motif and ubiquitination involving BTRC occurs. {ECO:0000250}. SUBUNIT: Interacts with LOXL2 and LOXL3 (By similarity). Interacts with FBXL14 and GSK3B. Interacts with BTRC; interaction occurs when it is phosphorylated on the destruction motif. Interacts (via SNAG domain) with LIMD1 (via LIM domains), WTIP (via LIM domains) and AJUBA (via LIM domains). Interacts (via N-terminal region) with CSNK2A1. Interacts with EGR1 upon TPA induction. Interacts (via N-terminal region) with LATS2; the interaction is dependent on LATS2 kinase activity but independent of SNAI1 Thr-203 phosphorylation. Interacts (via zinc fingers) with KPNB1 and TNPO1; the interactions mediate nuclear import. Interacts (via zinc fingers) with KPNA1; the interaction disrupts the transport complex with KPNB1 and prevents nuclear import increasing SNAI1 degradation in the cytoplasm. Interacts (via zinc fingers) with KPNA2; the interaction, in combination with KPNB1, mediates nuclear import. Interacts with KPNA4; this interaction mediates nuclear import. May interact (via zinc fingers) with IPO7. Interacts (via zinc fingers) with PARP1; the interaction requires SNAI1 to be poly-ADP-ribosylated and non-phosphorylated (active) by GSK3B. Interacts (via SNAG domain) with KDM1A; the interaction is necessary for the down-regulation of dimethylated H3K4 mark and promoter activity of E-cadherin/CDH1, CDN7 and KRT8. Interacts with TP53/p53 and (via zinc fingers) with NOTCH1 (via intracellular domain); the interactions induce SNAI1 degradation via MDM2-mediated ubiquitination and inhibit SNAI1-induced cell invasion. Interacts with MDM2; the interaction promotes SNAI1 ubiquitination. Interacts (via zinc fingers) with CSNK1E. Interacts with PAK1. {ECO:0000250, ECO:0000269|PubMed:18331720, ECO:0000269|PubMed:19386897, ECO:0000269|PubMed:19923321, ECO:0000269|PubMed:21577210}. TISSUE SPECIFICITY: While expression is completely absent from non-invasive cell lines, it is high in invasive and metastatic cell types. +Q7M711 TR113_MOUSE Taste receptor type 2 member 113 (T2R113) (mT2R58) 309 36,376 Chain (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 11 31 Helical; Name=1. {ECO:0000255}.; TRANSMEM 56 76 Helical; Name=2. {ECO:0000255}.; TRANSMEM 81 101 Helical; Name=3. {ECO:0000255}.; TRANSMEM 128 148 Helical; Name=4. {ECO:0000255}.; TRANSMEM 186 206 Helical; Name=5. {ECO:0000255}.; TRANSMEM 230 250 Helical; Name=6. {ECO:0000255}.; TRANSMEM 263 283 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 10 Extracellular. {ECO:0000255}.; TOPO_DOM 32 55 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 77 80 Extracellular. {ECO:0000255}.; TOPO_DOM 102 127 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 149 185 Extracellular. {ECO:0000255}.; TOPO_DOM 207 229 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 251 262 Extracellular. {ECO:0000255}.; TOPO_DOM 284 309 Cytoplasmic. {ECO:0000255}. FUNCTION: Putative taste receptor which may play a role in the perception of bitterness. {ECO:0000305}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +O70492 SNX3_MOUSE Sorting nexin-3 (SDP3 protein) 162 18,757 Binding site (4); Chain (1); Cross-link (1); Domain (1); Initiator methionine (1); Modified residue (3); Mutagenesis (4); Region (1) FUNCTION: Phosphoinositide-binding protein required for multivesicular body formation. Specifically binds phosphatidylinositol 3-phosphate (PtdIns(P3)). Also can bind phosphatidylinositol 4-phosphate (PtdIns(P4)), phosphatidylinositol 5-phosphate (PtdIns(P5)) and phosphatidylinositol 3,5-biphosphate (PtdIns(3,5)P2) (PubMed:19576982). Plays a role in protein transport between cellular compartments. Together with RAB7A facilitates endosome membrane association of the retromer cargo-selective subcomplex (CSC). May act in part as component of the SNX3-retromer complex which mediates the retrograde endosome-to-TGN transport of WLS distinct from the SNX-BAR retromer pathway (By similarity). Promotes stability and cell surface expression of epithelial sodium channel (ENAC) subunits SCNN1A and SCNN1G (PubMed:18632802). Not involved in EGFR degradation. Involved in the regulation of phagocytosis in dendritic cells possibly by regulating EEA1 recruitment to the nascent phagosomes (By similarity). Involved in iron homeostasis through regulation of endocytic recycling of the transferrin receptor Tfrc presuambly by delivering the transferrin:transferrin receptor complex to recycling endosomes; the function may involve the CSC retromer subcomplex (PubMed:23416069). Involved in regulation of neurite outgrowth in primary neurons (PubMed:19576982). {ECO:0000250|UniProtKB:O60493, ECO:0000269|PubMed:18632802, ECO:0000269|PubMed:23416069}. PTM: Ubiquitinated, leading to its proteasomal degradation. Deubiquitinated by USP10. {ECO:0000269|PubMed:18632802}. SUBCELLULAR LOCATION: Early endosome {ECO:0000269|PubMed:23416069}. Cytoplasmic vesicle, phagosome {ECO:0000250|UniProtKB:O60493}. Note=Colocalizes to clathrin-coated endosomal vesicles morphologically distinct from retromer-decorated non-branched endosomal tubule structures. Colocalizes with EEA1 on nascent phagosomes in dendritic cells but competes with EEA1 for binding to phagosomal membrane (By similarity). {ECO:0000250|UniProtKB:O60493, ECO:0000269|PubMed:23416069}. SUBUNIT: Interacts with VPS26A, VPS29 (By similarity). Interacts with VPS35; the interaction with VPS35 is direct (PubMed:23416069). The association with the retromer CSC subcomplex subunits is proposed to represent a functional distinct retromer variant described as SNX3-retromer complex (By similarity). Interacts with USP10 and SCNN1A (PubMed:18632802). Interacts with TRFC (PubMed:23416069). Interacts with SNX8; 2 molecules of SNX8 seems to associate with one molecule of SNX3. Interacts with PTPRU (By similarity). {ECO:0000250|UniProtKB:O60493, ECO:0000269|PubMed:18632802, ECO:0000269|PubMed:23416069}. DOMAIN: The PX domain mediates specific binding to phosphatidylinositol 3-phosphate (PtdIns(P3)). TISSUE SPECIFICITY: Highly expressed in developing red cells and hematopoietic tissues (PubMed:23416069). {ECO:0000269|PubMed:23416069}. +Q91XB0 TREX1_MOUSE Three-prime repair exonuclease 1 (EC 3.1.11.2) (3'-5' exonuclease TREX1) 314 33,675 Active site (1); Beta strand (9); Binding site (2); Chain (1); Helix (11); Metal binding (4); Modified residue (3); Mutagenesis (5); Region (5); Sequence conflict (2); Turn (2) FUNCTION: Major cellular 3'-to-5' DNA exonuclease which digests single-stranded DNA (ssDNA) and double-stranded DNA (dsDNA) with mismatched 3' termini. Prevents cell-intrinsic initiation of autoimmunity. Acts by metabolizing DNA fragments from endogenous retroelements, including L1, LTR and SINE elements. Unless degraded, these DNA fragments accumulate in the cytosol and activate the IFN-stimulatory DNA (ISD) response and innate immune signaling. Prevents chronic ATM-dependent checkpoint activation, by processing ssDNA polynucleotide species arising from the processing of aberrant DNA replication intermediates. Inefficiently degrades oxidized DNA, such as that generated upon antimicrobial reactive oxygen production or upon absorption of UV light. During GZMA-mediated cell death, contributes to DNA damage in concert with NME1. NME1 nicks one strand of DNA and TREX1 removes bases from the free 3' end to enhance DNA damage and prevent DNA end reannealing and rapid repair. {ECO:0000269|PubMed:10391904, ECO:0000269|PubMed:11279105, ECO:0000269|PubMed:15254239, ECO:0000269|PubMed:17293595, ECO:0000269|PubMed:17355961, ECO:0000269|PubMed:18045533, ECO:0000269|PubMed:18724932, ECO:0000269|PubMed:18780819, ECO:0000269|PubMed:23993650, ECO:0000269|PubMed:24218451}. PTM: Ubiquitinated, but not targeted to proteasomal degradation. Ubiquitination may be important for interaction with UBQLN1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytosol. Endoplasmic reticulum membrane; Peripheral membrane protein. Note=Retained in the cytoplasm through the C-terminal region. In response to DNA damage, translocates to the nucleus where it is specifically recruited to replication foci. Translocation to the nucleus also occurs during GZMA-mediated cell death. SUBUNIT: Homodimer. Interacts (via proline-rich region) with TCERG1/CA150 (via the second WW domain). Component of the SET complex, composed of at least ANP32A, APEX1, HMGB2, NME1, SET and TREX1. Within this complex, directly interacts with SET; this interaction does not result in TREX1 inhibition. Also interacts with NME1, but only following translocation to the nucleus. Directly interacts with UBQLN1 (via ubiquitin-like domain); the interaction may control TREX1 subcellular location. {ECO:0000269|PubMed:17293595, ECO:0000269|PubMed:17355961, ECO:0000269|PubMed:22071149}. TISSUE SPECIFICITY: Widely expressed with high expression levels detected in spleen, thymus and uterus. {ECO:0000269|PubMed:24218451}. +Q9R1A9 TREX2_MOUSE Three prime repair exonuclease 2 (EC 3.1.11.2) (3'-5' exonuclease TREX2) 236 25,955 Active site (1); Binding site (2); Chain (1); Metal binding (4); Region (1) FUNCTION: Exonuclease with a preference for double-stranded DNA with mismatched 3' termini. May play a role in DNA repair. {ECO:0000269|PubMed:10391904}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Homodimer. {ECO:0000250}. +Q921I1 TRFE_MOUSE Serotransferrin (Transferrin) (Beta-1 metal-binding globulin) (Siderophilin) 697 76,724 Binding site (8); Chain (1); Disulfide bond (18); Domain (2); Glycosylation (1); Metal binding (8); Modified residue (3); Sequence conflict (17); Signal peptide (1) FUNCTION: Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Monomer. TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma. {ECO:0000269|PubMed:2601714}. +P08071 TRFL_MOUSE Lactotransferrin (Lactoferrin) (EC 3.4.21.-) 707 77,838 Active site (2); Binding site (8); Chain (1); Disulfide bond (16); Domain (2); Glycosylation (2); Metal binding (8); Sequence conflict (8); Signal peptide (1) FUNCTION: Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate.; FUNCTION: Lactotransferrin is a major iron-binding and multifunctional protein found in exocrine fluids such as breast milk and mucosal secretions. Has antimicrobial activity. Antimicrobial properties may include bacteriostasis, which is related to its ability to sequester free iron and thus inhibit microbial growth, as well as direct bactericidal properties leading to the release of lipopolysaccharides from the bacterial outer membrane. May have anabolic, differentiating and anti-apoptotic effects on osteoblasts and may also inhibit osteoclastogenesis, possibly playing a role in the regulation of bone growth. May interfere with the lipopolysaccharide (LPS)-stimulated TLR4 signaling (By similarity). {ECO:0000250}.; FUNCTION: The lactotransferrin transferrin-like domain 1 functions as a serine protease of the peptidase S60 family that cuts arginine rich regions. This function contributes to the antimicrobial activity. Shows a preferential cleavage at -Arg-Ser-Arg-Arg-|- and -Arg-Arg-Ser-Arg-|-, and of Z-Phe-Arg-|-aminomethylcoumarin sites. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. Cytoplasmic granule {ECO:0000250}. Note=Secreted into most exocrine fluids by various endothelial cells. Stored in the secondary granules of neutrophils (By similarity). {ECO:0000250}. SUBUNIT: Monomer. Found in a complex with LTF, CLU, EPPIN and SEMG1 (By similarity). {ECO:0000250}. +Q9R0R1 TRFM_MOUSE Melanotransferrin (Membrane-bound transferrin-like protein p97) (MTf) (CD antigen CD228) 738 81,293 Binding site (4); Chain (1); Disulfide bond (6); Domain (2); Glycosylation (3); Lipidation (1); Metal binding (7); Modified residue (1); Propeptide (1); Signal peptide (1) FUNCTION: Involved in iron cellular uptake. Seems to be internalized and then recycled back to the cell membrane. Binds a single atom of iron per subunit. Could also bind zinc. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. +P21761 TRFR_MOUSE Thyrotropin-releasing hormone receptor (TRH-R) (Thyroliberin receptor) 393 44,559 Chain (1); Disulfide bond (1); Glycosylation (2); Topological domain (8); Transmembrane (7) TRANSMEM 29 51 Helical; Name=1. {ECO:0000255}.; TRANSMEM 62 83 Helical; Name=2. {ECO:0000255}.; TRANSMEM 100 121 Helical; Name=3. {ECO:0000255}.; TRANSMEM 145 168 Helical; Name=4. {ECO:0000255}.; TRANSMEM 194 215 Helical; Name=5. {ECO:0000255}.; TRANSMEM 267 288 Helical; Name=6. {ECO:0000255}.; TRANSMEM 297 319 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 28 Extracellular. {ECO:0000255}.; TOPO_DOM 52 61 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 84 99 Extracellular. {ECO:0000255}.; TOPO_DOM 122 144 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 169 193 Extracellular. {ECO:0000255}.; TOPO_DOM 216 266 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 289 296 Extracellular. {ECO:0000255}.; TOPO_DOM 320 393 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for thyrotropin-releasing hormone. Activity of this receptor is mediated by G proteins which activate a phosphatidylinositol-calcium second messenger system. {ECO:0000269|PubMed:11181534, ECO:0000269|PubMed:2175902}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11181534, ECO:0000269|PubMed:2175902}; Multi-pass membrane protein {ECO:0000255}. +Q8K093 TRHDE_MOUSE Thyrotropin-releasing hormone-degrading ectoenzyme (TRH-DE) (TRH-degrading ectoenzyme) (EC 3.4.19.6) (Pyroglutamyl-peptidase II) (PAP-II) (TRH-specific aminopeptidase) (Thyroliberinase) 1025 117,458 Active site (1); Chain (1); Disulfide bond (1); Glycosylation (12); Metal binding (3); Modified residue (1); Region (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 41 61 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 40 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 62 1025 Extracellular. {ECO:0000255}. FUNCTION: Specific inactivation of TRH after its release. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}. +Q9WUH5 TRI10_MOUSE Tripartite motif-containing protein 10 (Hematopoietic RING finger 1) (RING finger protein 9) 489 55,630 Chain (1); Coiled coil (1); Domain (1); Sequence conflict (5); Zinc finger (2) FUNCTION: Seems to play an important role in erythropoiesis. TISSUE SPECIFICITY: Expressed in embryonic liver. {ECO:0000269|PubMed:11331580}. +Q99PQ2 TRI11_MOUSE E3 ubiquitin-protein ligase TRIM11 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase TRIM11) (Tripartite motif-containing protein 11) 467 52,580 Alternative sequence (1); Chain (1); Coiled coil (1); Domain (1); Modified residue (1); Zinc finger (2) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that promotes the degradation of insoluble ubiquitinated proteins, including insoluble PAX6, poly-Gln repeat expanded HTT and poly-Ala repeat expanded ARX. Mediates PAX6 ubiquitination leading to proteasomal degradation, thereby modulating cortical neurogenesis. May also inhibit PAX6 transcriptional activity, possibly in part by preventing the binding of PAX6 to its consensus sequences. May contribute to the regulation of the intracellular level of HN (humanin) or HN-containing proteins through the proteasomal degradation pathway. Mediates MED15 ubiquitination leading to proteasomal degradation. May contribute to the innate restriction of retroviruses. Upon overexpression, reduces HIV-1 and murine leukemia virus infectivity, by suppressing viral gene expression. Antiviral activity depends on a functional E3 ubiquitin-protein ligase domain. May regulate TRIM5 turnover via the proteasome pathway, thus counteracting the TRIM5-mediated cross-species restriction of retroviral infection at early stages of the retroviral life cycle. {ECO:0000269|PubMed:12670303, ECO:0000269|PubMed:18248090, ECO:0000269|PubMed:18628401}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18628401}. Nucleus {ECO:0000269|PubMed:18628401}. Note=In the nucleus, colocalizes with PAX6. SUBUNIT: Binds cytoplasmic tail of integrin alpha-1 (By similarity). Interacts with MED15/ARC105; this interaction leads to MED15 ubiquitination and proteasomal degradation (By similarity). Interacts with the HN peptide. Interacts with PHOX2B. Interacts with PAX6. {ECO:0000250, ECO:0000269|PubMed:12670303, ECO:0000269|PubMed:18275850, ECO:0000269|PubMed:18628401}. DOMAIN: The coiled-coil domain and the B30.2 domain are both necessary for interaction with HN and PAX6. They are also involved in MED15-binding. {ECO:0000250}.; DOMAIN: The B30.2 domain may be involved cellular protein quality control by promoting the degradation of insoluble ubiquitinated proteins. {ECO:0000269|PubMed:18628401}. TISSUE SPECIFICITY: Expressed in embryonic central nervous system (CNS), kidney, thymus and gut. +O70583 TRI18_MOUSE E3 ubiquitin-protein ligase Midline-1 (EC 2.3.2.27) (Midin) (RING finger protein Midline-1) (RING-type E3 ubiquitin transferase Midline-1) (Tripartite motif-containing protein 18) 680 76,136 Alternative sequence (2); Chain (1); Coiled coil (1); Domain (3); Erroneous termination (1); Metal binding (8); Modified residue (3); Sequence conflict (6); Zinc finger (3) FUNCTION: Has E3 ubiquitin ligase activity towards IGBP1, promoting its monoubiquitination, which results in deprotection of the catalytic subunit of protein phosphatase PP2A, and its subsequent degradation by polyubiquitination. {ECO:0000250|UniProtKB:O15344}. PTM: Phosphorylated. {ECO:0000269|PubMed:11371618}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O15344}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O15344}. Note=Microtubule-associated. {ECO:0000250|UniProtKB:O15344}. SUBUNIT: Homodimer or heterodimer with MID2. Interacts with IGBP1. {ECO:0000250|UniProtKB:O15344}. TISSUE SPECIFICITY: Ubiquitously expressed in fetus and adult. At E9-E10.5, highest expression found in frontonasal processes, branchial arches and CNS. From E12.5 to E16.5, high levels found in rostral part of CNS. At E14.5, begins to be highly expressed in kidney and lung. At E16.5, highly expressed in the mucosa of the hindgut and cutaneous region of the stomach. {ECO:0000269|PubMed:9722948}. +Q6PCX9 TRI37_MOUSE E3 ubiquitin-protein ligase TRIM37 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase TRIM37) (Tripartite motif-containing protein 37) 961 107,660 Chain (1); Coiled coil (2); Compositional bias (2); Domain (1); Erroneous initiation (1); Modified residue (2); Sequence conflict (1); Zinc finger (2) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase required to prevent centriole reduplication (By similarity). Probably acts by ubiquitinating positive regulators of centriole reduplication (By similarity). Mediates monoubiquitination of 'Lys-119' of histone H2A (H2AK119Ub), a specific tag for epigenetic transcriptional repression: associates with some Polycomb group (PcG) multiprotein PRC2-like complex and mediates repression of target genes (PubMed:25470042). {ECO:0000250|UniProtKB:O94972, ECO:0000269|PubMed:25470042}. PTM: Auto-ubiquitinated. {ECO:0000250|UniProtKB:O94972}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O94972}. Peroxisome {ECO:0000250|UniProtKB:O94972}. Note=Found in vesicles of the peroxisome. Aggregates as aggresomes, a perinuclear region where certain misfolded or aggregated proteins are sequestered for proteasomal degradation. {ECO:0000250|UniProtKB:O94972}. SUBUNIT: Associates with the PRC2/EED-EZH2 complex. {ECO:0000250|UniProtKB:O94972}. TISSUE SPECIFICITY: Highly expressed in testis and brain. In embryonic tissues, expressed in epithelia, including ducts of the developing pancreas, epithelium of the midgut and nasal epithelium. In adult, detected in the central and peripheral nervous systems, including enteric ganglia, retina and the adrenal medulla (at protein level). {ECO:0000269|PubMed:16514549}. +Q9ESN2 TRI39_MOUSE E3 ubiquitin-protein ligase TRIM39 (EC 2.3.2.27) (RING finger protein 23) (RING-type E3 ubiquitin transferase TRIM39) (Testis-abundant finger protein) (Tripartite motif-containing protein 39) 488 56,369 Alternative sequence (3); Chain (1); Coiled coil (1); Domain (1); Sequence conflict (1); Zinc finger (2) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase. May facilitate apoptosis by inhibiting APC/C-Cdh1-mediated poly-ubiquitination and subsequent proteasome-mediated degradation of the pro-apoptotic protein MOAP1. {ECO:0000250|UniProtKB:Q9HCM9}. PTM: Autoubiquitinated. {ECO:0000250|UniProtKB:Q9HCM9}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9HCM9}. Mitochondrion {ECO:0000250|UniProtKB:Q9HCM9}. Note=Found predominantly in the cytosol. Partial shift from the cytosol to the mitochondria when colocalized with MOAP1. {ECO:0000250|UniProtKB:Q9HCM9}. SUBUNIT: Interacts with MOAP1. {ECO:0000250|UniProtKB:Q9HCM9}. +Q64674 SPEE_MOUSE Spermidine synthase (SPDSY) (EC 2.5.1.16) (Putrescine aminopropyltransferase) 302 33,995 Active site (1); Binding site (7); Chain (1); Domain (1); Modified residue (1); Region (2) Amine and polyamine biosynthesis; spermidine biosynthesis; spermidine from putrescine: step 1/1. FUNCTION: Catalyzes the production of spermidine from putrescine and decarboxylated S-adenosylmethionine (dcSAM). Has a strong preference for putrescine as substrate, and has very low activity towards 1,3-diaminopropane. Has extremely low activity towards spermidine (By similarity). {ECO:0000250}. SUBUNIT: Homodimer or homotetramer. {ECO:0000250}. +Q5NCC3 TRI41_MOUSE E3 ubiquitin-protein ligase TRIM41 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase TRIM41) (Tripartite motif-containing protein 41) 630 71,818 Chain (1); Coiled coil (1); Compositional bias (2); Cross-link (1); Domain (1); Modified residue (2); Zinc finger (2) Protein modification; protein ubiquitination. FUNCTION: Functions as an E3 ligase that catalyzes the ubiquitin-mediated degradation of protein kinase C. {ECO:0000250|UniProtKB:Q8WV44}. PTM: Auto-ubiquitinated. {ECO:0000250|UniProtKB:Q8WV44}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8WV44}. Nucleus {ECO:0000250|UniProtKB:Q8WV44}. SUBUNIT: Interacts with PRKCA. Interacts with NOD2 (By similarity). {ECO:0000250|UniProtKB:Q8WV44}. +Q9QXA7 TRI44_MOUSE Tripartite motif-containing protein 44 (Protein DIPB) (Protein Mc7) 346 38,272 Chain (1); Coiled coil (1); Compositional bias (1); Erroneous initiation (2); Modified residue (2); Sequence conflict (7); Zinc finger (1) FUNCTION: May play a role in the process of differentiation and maturation of neuronal cells (By similarity). May regulate the activity of TRIM17 (By similarity). Is a negative regulator of PAX6 expression (By similarity). {ECO:0000250|UniProtKB:Q96DX7}. SUBUNIT: Interacts (via coiled coil) with TRIM17 (via coiled coil). {ECO:0000250|UniProtKB:Q96DX7}. TISSUE SPECIFICITY: Expressed mainly in brain with high level in cerebral hemispheres and cerebellum. Lower expression in kidney, lung and spleen. In brain is detected in the hippocampus, thalamic and pretectal nuclei, substantia nigra, the dorsal part of the medulla, the cerebellum, in the olfactory nucleus, other cortical areas apart from hyppocampus and the striatum. Indeed expression is confined in neuronal somata namely in the CA3 region and dentate gyrus of the hyppocampus, caudate-putamen, parabranchial nucleus, olfactory nucleus, cortex, deep cerebellar nuclei and thalamus. Also highly expressed in the spleen. thymus and testis. {ECO:0000269|PubMed:19358823}. +Q9ERP3 TRI54_MOUSE Tripartite motif-containing protein 54 (Muscle-specific RING finger protein) (MuRF) (Muscle-specific RING finger protein 3) (MuRF-3) (MuRF3) (RING finger protein 30) 366 41,131 Chain (1); Coiled coil (1); Domain (1); Region (1); Zinc finger (2) FUNCTION: May bind and stabilize microtubules during myotubes formation. {ECO:0000269|PubMed:10953002}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10953002}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:10953002}. Note=Associates with microtubules. Localizes to the Z-lines in skeletal muscles. SUBUNIT: Homooligomer and heterooligomer. Interacts with TRIM63 and probably with TRIM55 (By similarity). Interacts with tubulin. {ECO:0000250, ECO:0000269|PubMed:10953002}. TISSUE SPECIFICITY: Selectively expressed in heart and skeletal muscle (at protein level). Also detected in lung and brain at much lower level. {ECO:0000269|PubMed:10953002}. +Q80VI1 TRI56_MOUSE E3 ubiquitin-protein ligase TRIM56 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase TRIM56) (Tripartite motif-containing protein 56) 734 79,513 Chain (1); Coiled coil (1); Compositional bias (2); Modified residue (1); Sequence conflict (1); Zinc finger (3) FUNCTION: E3 ubiquitin-protein ligase that plays a key role in innate antiviral immunity. In response to pathogen- and host-derived double-stranded DNA (dsDNA), targets TMEM173/STING to 'Lys-63'-linked ubiquitination, thereby promoting its homodimerization, a step required for the production of type I interferon IFN-beta. Independently of its E3 ubiquitin ligase activity, positive regulator of TLR3 signaling. Potentiates extracellular double stranded RNA (dsRNA)-induced expression of IFNB1 and interferon-stimulated genes ISG15, IFIT1/ISG56, CXCL10, OASL and CCL5/RANTES (By similarity). {ECO:0000250|UniProtKB:Q9BRZ2, ECO:0000269|PubMed:21074459}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21074459}. SUBUNIT: Interacts with TMEM173/STING (PubMed:21074459). Interacts with TICAM1 (By similarity). {ECO:0000250|UniProtKB:Q9BRZ2, ECO:0000269|PubMed:21074459}. +Q5NCC9 TRI58_MOUSE E3 ubiquitin-protein ligase TRIM58 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase TRIM58) (Tripartite motif-containing protein 58) 485 55,371 Chain (1); Coiled coil (1); Compositional bias (1); Domain (1); Zinc finger (2) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin ligase induced during late erythropoiesis. Directly binds and ubiquitinates the intermediate chain of the microtubule motor dynein (DYNC1LI1/DYNC1LI2), stimulating the degradation of the dynein holoprotein complex. May participate in the erythroblast enucleation process through regulation of nuclear polarization. {ECO:0000250|UniProtKB:Q8NG06}. DOMAIN: The RING finger is required for ubiquitin ligase activity. {ECO:0000250|UniProtKB:Q8NG06}. TISSUE SPECIFICITY: Expressed in erythroblasts. {ECO:0000269|PubMed:25241935}. +Q80V85 TRI62_MOUSE E3 ubiquitin-protein ligase TRIM62 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase TRIM62) (Tripartite motif-containing protein 62) 475 54,298 Chain (1); Coiled coil (1); Domain (1); Zinc finger (2) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin ligase whose activity is dependent on E2 ubiquitin-conjugating enzyme UBE2D2. {ECO:0000250|UniProtKB:Q9BVG3}. PTM: Polyubiquitinated, autoubiquitinated in the presence of UBE2D2. {ECO:0000250|UniProtKB:Q9BVG3}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BVG3}. SUBUNIT: Interacts with the ubiquitin-conjugating enzyme, UBE2D2. {ECO:0000250|UniProtKB:Q9BVG3}. DOMAIN: The RING finger is required for ubiquitin ligase activity. {ECO:0000250|UniProtKB:Q9BVG3}. +Q99JL1 SPEF1_MOUSE Sperm flagellar protein 1 (Calponin-homology and microtubule-associated protein) 234 26,839 Chain (1); Domain (1); Sequence conflict (3) FUNCTION: Microtubule-associated protein that promotes microtubule bundling and stabilizes microtubules against depolymerization in response to cold shock (PubMed:16206169). Microtubule-associated protein involved in the stabilization of microtubules along the axis of migration during radial intercalation. Promotes the establishment and stabilization of an axis of microtubules required for the active migration of cells into the outer epithelium (By similarity). {ECO:0000250|UniProtKB:Q0IH24, ECO:0000269|PubMed:16206169}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15979255}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:15979255}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q0IH24}. Note=Also found at the apical tip of cilia (By similarity). Present in the tails of developing and epididymal sperm, internal to the fibrous sheath and around the outer dense fibers of the sperm flagellum. {ECO:0000250}. TISSUE SPECIFICITY: Expressed predominantly in the seminiferous epithelium of adult testis (PubMed:15979255). Expressed in pillar cells of the organ of Corti (at protein level). Expressed in brain, kidney, lung and testis (PubMed:16206169). {ECO:0000269|PubMed:15979255, ECO:0000269|PubMed:16206169}. +Q8C9J3 SPEF2_MOUSE Sperm flagellar protein 2 (Protein KPL2) 1724 197,972 Alternative sequence (6); Chain (1); Coiled coil (4); Compositional bias (1); Domain (1); Region (1); Sequence conflict (1) FUNCTION: Required for correct axoneme development in spermatozoa (PubMed:21715716, PubMed:28619825). Important for normal development of the manchette and sperm head morphology (PubMed:28619825). Essential for male fertility (PubMed:21715716, PubMed:28619825). Plays a role in localization of the intraflagellar transport protein IFT20 to the manchette, suggesting function as an adapter for dynein-mediated protein transport during spermatogenesis. Also plays a role in bone growth where it seems to be required for normal osteoblast differentiation (PubMed:28619825). {ECO:0000269|PubMed:21715716, ECO:0000269|PubMed:28619825}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19889948}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19889948, ECO:0000269|PubMed:28619825}. Golgi apparatus {ECO:0000269|PubMed:19889948}. Note=Shows dynamic localization in developing spermatozoa (PubMed:19889948). Localizes to the manchette in step 10-12 elongating spermatids, where it is mainly found on the basal side below the perinuclear ring (PubMed:19889948, PubMed:28619825). Detected in the basal body and neck area of step 13-14 spermatids (PubMed:19889948). Localizes to the midpiece of the sperm tail in step 15-16 spermatids (PubMed:19889948). During the epididymal transport of spermatozoa, expression in the sperm tail reduces and becomes concentrated at the distal part of the midpiece (PubMed:19889948). Detected in the Golgi apparatus of late spermatocytes and round spermatids (PubMed:19889948). Detected in the cytoplasm of Sertoli cells (PubMed:19889948). {ECO:0000269|PubMed:19889948, ECO:0000269|PubMed:28619825}. SUBUNIT: Interacts (via C-terminus) with IFT20 (PubMed:19889948). Interacts with DYNC1I2 (PubMed:28619825). {ECO:0000269|PubMed:19889948, ECO:0000269|PubMed:28619825}. TISSUE SPECIFICITY: Highly expressed in testis, where it primarily localizes to late spermatocytes, round spermatids and elongating spermatids (at protein level) (PubMed:19889948, PubMed:29339787). Found in Sertoli cells of the testis (at protein level) (PubMed:19889948). Expressed at lower levels in epididymis (at protein level) (PubMed:19889948, PubMed:29339787). Detected in lung, brain, liver and kidney (PubMed:19889948, PubMed:29339787). Also detected in bone, cartilage, trachea, pituitary gland and eye (PubMed:29339787). Expressed in osteoblasts and chondrocytes (PubMed:29339787). {ECO:0000269|PubMed:19889948, ECO:0000269|PubMed:29339787}. +Q62407 SPEG_MOUSE Striated muscle-specific serine/threonine-protein kinase (EC 2.7.11.1) (Aortic preferentially expressed protein 1) (APEG-1) 3262 354,343 Active site (2); Alternative sequence (5); Binding site (1); Chain (1); Compositional bias (7); Disulfide bond (3); Domain (14); Frameshift (1); Modified residue (43); Nucleotide binding (1); Sequence conflict (1) FUNCTION: Isoform 3 may have a role in regulating the growth and differentiation of arterial smooth muscle cells. PTM: May be autophosphorylated. {ECO:0000269|PubMed:10973969}. SUBCELLULAR LOCATION: Isoform 3: Nucleus. SUBUNIT: Interacts with MTM1 (By similarity). Isoform 3 is found as a monomer or homodimer. {ECO:0000250|UniProtKB:Q15772}. TISSUE SPECIFICITY: Isoform 1 is preferentially expressed in striated muscle. Non-kinase form such as isoform 3 is predominantly expressed in the aorta. Isoform 3 appears to be expressed only in highly differentiated ASMC in normal vessel walls and down-regulated in dedifferentiated ASMC in vivo. In response to vascular injuries ASMC dedifferentiate and change from a quiescent and contractile phenotype to a proliferative and synthetic phenotype. This proliferation of vascular smooth muscle cells is one of the most prominent features of atherosclerosis. Isoform 1 and isoform 4 are expressed in cardiomyocytes of the developing heart. {ECO:0000269|PubMed:10973969, ECO:0000269|PubMed:19118250, ECO:0000269|PubMed:8663449}. +Q9D8Z2 TRIA1_MOUSE TP53-regulated inhibitor of apoptosis 1 (Protein 15E1.1) (WF-1) (p53-inducible cell-survival factor) (p53CSV) 76 8,756 Chain (1); Coiled coil (1); Disulfide bond (2); Domain (1); Modified residue (1); Motif (2); Sequence conflict (1); Site (2) FUNCTION: Involved in the modulation of the mitochondrial apoptotic pathway by ensuring the accumulation of cardiolipin (CL) in mitochondrial membranes. In vitro, the TRIAP1:PRELID1 complex mediates the transfer of phosphatidic acid (PA) between liposomes and probably functions as a PA transporter across the mitochondrion intermembrane space to provide PA for CL synthesis in the inner membrane. Likewise, the TRIAP1:PRELID3A complex mediates the transfer of phosphatidic acid (PA) between liposomes (in vitro) and probably functions as a PA transporter across the mitochondrion intermembrane space (in vivo). Mediates cell survival by inhibiting activation of caspase-9 which prevents induction of apoptosis. {ECO:0000250|UniProtKB:O43715}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O43715}. Mitochondrion {ECO:0000250|UniProtKB:O43715}. Mitochondrion intermembrane space {ECO:0000250|UniProtKB:O43715}. SUBUNIT: Monomer. Interacts with APAF1 and HSP70. Forms a complex with PRELID1 in the mitochondrion intermembrane space. Interacts with PRELID3A. {ECO:0000250|UniProtKB:O43715}. +Q8K4K4 TRIB1_MOUSE Tribbles homolog 1 (TRB-1) 372 41,281 Alternative sequence (1); Chain (1); Domain (1); Erroneous initiation (2); Motif (1); Sequence conflict (2) FUNCTION: Adapter protein involved in protein degradation by interacting with COP1 ubiquitin ligase (PubMed:23515163, PubMed:20410507). Promotes CEBPA degradation and inhibits its function (PubMed:20410507). Controls macrophage, eosinophil and neutrophil differentiation via the COP1-binding domain (PubMed:24003916, PubMed:23515163). Regulates myeloid cell differentiation by altering the expression of CEBPA in a COP1-dependent manner (PubMed:23515163). Interacts with MAPK kinases and regulates activation of MAP kinases, but has no kinase activity (By similarity). {ECO:0000250|UniProtKB:Q96RU8, ECO:0000269|PubMed:20410507, ECO:0000269|PubMed:23515163, ECO:0000269|PubMed:24003916}. SUBUNIT: Monomer. Interacts (via protein kinase domain) with CEBPA. Interacts with COP1. {ECO:0000250|UniProtKB:Q96RU8}. DOMAIN: The COP1-binding motif (355-360) is required for regulation activity (PubMed:24003916). {ECO:0000269|PubMed:24003916}.; DOMAIN: The C-terminus (351-372) is required for interaction with COP1 (By similarity). {ECO:0000250|UniProtKB:Q96RU8}.; DOMAIN: The protein kinase active site is incompatible with ATP binding and is inactive (By similarity). {ECO:0000250|UniProtKB:Q96RU8}. +Q9DBY4 TRIL_MOUSE TLR4 interactor with leucine rich repeats (Leucine-rich repeat-containing protein KIAA0644) 809 88,810 Chain (1); Domain (2); Frameshift (1); Glycosylation (3); Modified residue (1); Repeat (12); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 695 715 Helical. {ECO:0000255}. TOPO_DOM 26 694 Extracellular. {ECO:0000255}.; TOPO_DOM 716 809 Cytoplasmic. {ECO:0000255}. FUNCTION: Component of the TLR4 signaling complex. Mediate the innate immune response to bacterial lipopolysaccharide (LPS) leading to cytokine secretion (By similarity). {ECO:0000250}. PTM: N-glycolysaled. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Belongs to the lipopolysaccharide (LPS) receptor, a multi-protein complex containing at least CD14, MD-2 and TLR4. Interacts with TLR4; this interaction is greatly enhanced by LPS stimulation (By similarity). Interacts with LPS (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in brain, spinal cord and lung. {ECO:0000269|PubMed:19710467}. +Q9QUS6 TRIM1_MOUSE Probable E3 ubiquitin-protein ligase MID2 (EC 2.3.2.27) (Midline defect 2) (Midline-2) (RING-type E3 ubiquitin transferase MID2) (Tripartite motif-containing protein 1) 705 79,774 Chain (1); Coiled coil (1); Domain (3); Erroneous initiation (2); Zinc finger (3) Protein modification; protein ubiquitination. FUNCTION: May play a role in microtubule stabilization. {ECO:0000250|UniProtKB:Q9UJV3}. PTM: Phosphorylated on serine and threonine residues. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Note=Microtubule-associated. SUBUNIT: Homodimer or heterodimer with MID1. Interacts with IGBP1. {ECO:0000250|UniProtKB:Q9UJV3}. DOMAIN: The tripartite motif (RBCC; RING- and B box-type zinc fingers and coiled coil domains) mediates dimerization. {ECO:0000250|UniProtKB:Q9UJV3}.; DOMAIN: Associates with microtubules in a manner that is dependent on the C-terminal B30.2 domain. TISSUE SPECIFICITY: Low abundance in brain and lung, with even lower levels in heart, liver, and kidney. +P70178 SIX5_MOUSE Homeobox protein SIX5 (DM locus-associated homeodomain protein homolog) (Sine oculis homeobox homolog 5) 719 73,717 Chain (1); DNA binding (1) FUNCTION: Transcription factor that is thought to be involved in regulation of organogenesis. May be involved in determination and maintenance of retina formation. Binds a 5'-GGTGTCAG-3' motif present in the ARE regulatory element of ATP1A1. Binds a 5'-TCA[AG][AG]TTNC-3' motif present in the MEF3 element in the myogenin promoter, and in the IGFBP5 promoter (By similarity). Thought to be regulated by association with Dach and Eya proteins, and seems to be coactivated by EYA1, EYA2 and EYA3. {ECO:0000250, ECO:0000269|PubMed:10490620}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. SUBUNIT: Probably binds DNA dimer. Interacts with EYA3, and probably EYA1 and EYA2. {ECO:0000269|PubMed:10490620, ECO:0000269|PubMed:12215533}. +Q8BFU0 RSPO2_MOUSE R-spondin-2 (Cysteine-rich and single thrombospondin domain-containing protein 2) (Cristin-2) (mCristin-2) (Roof plate-specific spondin-2) 243 28,276 Beta strand (10); Chain (1); Disulfide bond (11); Domain (1); Erroneous termination (1); Glycosylation (1); Repeat (1); Signal peptide (1); Turn (1) FUNCTION: Activator of the canonical Wnt signaling pathway by acting as a ligand for LGR4-6 receptors. Upon binding to LGR4-6 (LGR4, LGR5 or LGR6), LGR4-6 associate with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increase expression of target genes. Also regulates the canonical Wnt/beta-catenin-dependent pathway and non-canonical Wnt signaling by acting as an inhibitor of ZNRF3, an important regulator of the Wnt signaling pathway. Probably also acts as a ligand for frizzled and LRP receptors (PubMed:21693646). During embryonic development, plays a crucial role in limb specification, amplifying the Wnt signaling pathway independently of LGR4-6 receptors, possibly by acting as a direct antagonistic ligand to RNF43 and ZNRF3, hence governing the number of limbs an embryo should form (By similarity). {ECO:0000250|UniProtKB:Q6UXX9, ECO:0000269|PubMed:21693646}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16543246}. SUBUNIT: Interacts with WNT1 (PubMed:16543246). Binds heparin (PubMed:16543246). Interacts with LGR4, LGR5 and LGR6 (PubMed:21693646). {ECO:0000269|PubMed:16543246, ECO:0000269|PubMed:21693646}. DOMAIN: The FU repeat is required for activation and stabilization of beta-catenin. {ECO:0000250}. +Q9DCA2 RT11_MOUSE 28S ribosomal protein S11, mitochondrial (MRP-S11) (S11mt) 191 20,208 Chain (1); Sequence conflict (3); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P82911}. SUBUNIT: Component of the mitochondrial ribosome small subunit (28S) which comprises a 12S rRNA and about 30 distinct proteins. {ECO:0000250|UniProtKB:P82911}. +Q8C6B2 RTKN_MOUSE Rhotekin 564 63,013 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (2); Modified residue (8); Sequence conflict (4) FUNCTION: Mediates Rho signaling to activate NF-kappa-B and may confer increased resistance to apoptosis to cells in gastric tumorigenesis. May play a novel role in the organization of septin structures (By similarity). {ECO:0000250}. SUBUNIT: Interacts via its C-terminal region with the TAX1BP3 PDZ domain. This interaction facilitates Rho-mediated activation of the c-Fos serum response element (SRE). Interacts with SEPT9 (By similarity). Specifically binds to GTP-bound RHOA, RHOB and RHOC and inhibits their GTPase activity. {ECO:0000250|UniProtKB:Q9BST9, ECO:0000269|PubMed:8662891}. TISSUE SPECIFICITY: Abundantly expressed in brain and kidney. Weakly expressed in lung, testis, skeletal muscle, heart and thymus. {ECO:0000269|PubMed:8662891}. +Q8QZY4 RTBDN_MOUSE Retbindin 247 26,559 Chain (1); Disulfide bond (4); Sequence conflict (3); Signal peptide (1) FUNCTION: Riboflavin-binding protein which might have a role in retinal flavin transport. {ECO:0000269|PubMed:25542898}. PTM: Not N-glycosylated. {ECO:0000269|PubMed:25542898}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, interphotoreceptor matrix {ECO:0000269|PubMed:25542898}. Cell membrane {ECO:0000269|PubMed:25542898}; Peripheral membrane protein {ECO:0000269|PubMed:25542898}. TISSUE SPECIFICITY: Expressed in the peripheral retina where it localizes to the inter-photoreceptor matrix (at protein level). May be produced by rod photoreceptors (at protein level). {ECO:0000269|PubMed:25542898}. +Q99P72 RTN4_MOUSE Reticulon-4 (Neurite outgrowth inhibitor) (Nogo protein) 1162 126,613 Alternative sequence (4); Chain (1); Compositional bias (2); Domain (1); Erroneous initiation (1); Erroneous termination (1); Helix (6); Modified residue (21); Sequence conflict (21); Topological domain (3); Transmembrane (2); Turn (2) TRANSMEM 989 1009 Helical. {ECO:0000255}.; TRANSMEM 1079 1099 Helical. {ECO:0000255}. TOPO_DOM 1 988 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1010 1078 Lumenal. {ECO:0000255}.; TOPO_DOM 1100 1162 Cytoplasmic. {ECO:0000255}. FUNCTION: Developmental neurite growth regulatory factor with a role as a negative regulator of axon-axon adhesion and growth, and as a facilitator of neurite branching. Regulates neurite fasciculation, branching and extension in the developing nervous system. Involved in down-regulation of growth, stabilization of wiring and restriction of plasticity in the adult CNS. Regulates the radial migration of cortical neurons via an RTN4R-LINGO1 containing receptor complex. May inhibit BACE1 activity and amyloid precursor protein processing. Induces the formation and stabilization of endoplasmic reticulum (ER) tubules. Regulates membrane morphogenesis in the ER by promoting tubular ER production. Influences NE expansion, nuclear pore complex formation and proper localization of inner nuclear membrane proteins (By similarity). {ECO:0000250|UniProtKB:Q9NQC3, ECO:0000269|PubMed:20093372, ECO:0000269|PubMed:20573699}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9NQC3}; Multi-pass membrane protein {ECO:0000255}. Note=Anchored to the membrane of the endoplasmic reticulum through 2 putative transmembrane domains. Localizes throughout the ER tubular network. Co-localizes with TMEM33 at the ER sheets. {ECO:0000250|UniProtKB:Q9NQC3}. SUBUNIT: Binds to RTN4R. Interacts with Bcl-xl and Bcl-2. Interacts in trans with CNTNAP1. Interacts with ATL1 (By similarity). Interacts with RTN4IP1. Interacts with TMEM170A and TMEM33 (By similarity). {ECO:0000250|UniProtKB:Q9NQC3, ECO:0000269|PubMed:12067236}. DOMAIN: Three regions, residues 59-172, 544-725 and the loop 66 amino acids, between the two transmembrane domains, known as Nogo-66 loop, appear to be responsible for the inhibitory effect on neurite outgrowth and the spreading of neurons. This Nogo-66 loop, mediates also the binding of RTN4 to its receptor (By similarity). {ECO:0000250}. +Q9CQE8 RTRAF_MOUSE RNA transcription, translation and transport factor protein 244 28,152 Chain (1); Modified residue (3) FUNCTION: RNA-binding protein involved in modulation of mRNA transcription by Polymerase II. Component of the tRNA-splicing ligase complex and is required for tRNA ligation. May be required for RNA transport. {ECO:0000250|UniProtKB:Q9Y224}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y224}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9Y224}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9Y224}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9Y224}. Note=May localize at the centrosome during mitosis. Shuttles between the cytosol and the nucleus: enters into the nucleus in case of active transcription while it accumulates in cytosol when transcription level is low (By similarity). {ECO:0000250}. SUBUNIT: Homodimer. Interacts with FAM98A (via N- and C-terminus). Interacts with NIN; which may prevent phosphorylation of NIN. Interacts with POLR2A. Component of a tRNA-splicing ligase complex. {ECO:0000250|UniProtKB:Q9Y224}. +Q62241 RU1C_MOUSE U1 small nuclear ribonucleoprotein C (U1 snRNP C) (U1-C) (U1C) 159 17,364 Chain (1); Compositional bias (1); Modified residue (3); Zinc finger (1) FUNCTION: Component of the spliceosomal U1 snRNP, which is essential for recognition of the pre-mRNA 5' splice-site and the subsequent assembly of the spliceosome. SNRPC/U1-C is directly involved in initial 5' splice-site recognition for both constitutive and regulated alternative splicing. The interaction with the 5' splice-site seems to precede base-pairing between the pre-mRNA and the U1 snRNA. Stimulates commitment or early (E) complex formation by stabilizing the base pairing of the 5' end of the U1 snRNA and the 5' splice-site region. {ECO:0000255|HAMAP-Rule:MF_03153}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03153}. SUBUNIT: Component of the U1 snRNP. The U1 snRNP is composed of the U1 snRNA and the 7 core Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP, and at least 3 U1 snRNP-specific proteins SNRNP70/U1-70K, SNRPA/U1-A and SNRPC/U1-C. SNRPC/U1-C interacts with U1 snRNA and the 5' splice-site region of the pre-mRNA. {ECO:0000255|HAMAP-Rule:MF_03153}. TISSUE SPECIFICITY: Widely expressed. In the testis, expressed in somatic and germinal testicular cells but not in elongated spermatids. +Q8BIJ7 RUFY1_MOUSE RUN and FYVE domain-containing protein 1 (Rab4-interacting protein) 712 80,376 Chain (1); Coiled coil (2); Domain (1); Erroneous initiation (1); Modified residue (3); Region (1); Sequence conflict (1); Zinc finger (1) FUNCTION: Binds phospholipid vesicles containing phosphatidylinositol 3-phosphate and participates in early endosomal trafficking. {ECO:0000269|PubMed:11172003, ECO:0000269|PubMed:16522682}. PTM: Phosphorylation on Tyr-393 and/or Tyr-404 is required for interaction with BMX and endosomal targeting. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Early endosome membrane; Peripheral membrane protein. SUBUNIT: Interacts with BMX. May interact with SSB (By similarity). Interacts with RAB4 and RAB5 that have been activated by GTP-binding. {ECO:0000250, ECO:0000269|PubMed:11172003}. DOMAIN: The FYVE-type zinc finger domain mediates interactions with phosphatidylinositol 3-phosphate in membranes of early endosomes and penetrates bilayers. The FYVE domain insertion into PtdIns(3)P-enriched membranes is substantially increased in acidic conditions (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Broadly expressed. {ECO:0000269|PubMed:11172003}. +Q9JI11 STK4_MOUSE Serine/threonine-protein kinase 4 (EC 2.7.11.1) (Mammalian STE20-like protein kinase 1) (MST-1) (STE20-like kinase MST1) [Cleaved into: Serine/threonine-protein kinase 4 37kDa subunit (MST1/N); Serine/threonine-protein kinase 4 18kDa subunit (MST1/C)] 487 55,541 Active site (1); Binding site (1); Chain (3); Coiled coil (1); Compositional bias (1); Domain (2); Modified residue (10); Nucleotide binding (1); Site (1) FUNCTION: Stress-activated, pro-apoptotic kinase which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. Key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. STK3/MST2 and STK4/MST1 are required to repress proliferation of mature hepatocytes, to prevent activation of facultative adult liver stem cells (oval cells), and to inhibit tumor formation. Phosphorylates 'Ser-14' of histone H2B (H2BS14ph) during apoptosis. Phosphorylates FOXO3 upon oxidative stress, which results in its nuclear translocation and cell death initiation. Phosphorylates MOBKL1A, MOBKL1B and RASSF2. Phosphorylates TNNI3 (cardiac Tn-I) and alters its binding affinity to TNNC1 (cardiac Tn-C) and TNNT2 (cardiac Tn-T). Phosphorylates FOXO1 on 'Ser-212' and regulates its activation and stimulates transcription of PMAIP1 in a FOXO1-dependent manner. Phosphorylates SIRT1 and inhibits SIRT1-mediated p53/TP53 deacetylation, thereby promoting p53/TP53 dependent transcription and apoptosis upon DNA damage. Acts as an inhibitor of PKB/AKT1. Phosphorylates AR on 'Ser-650' and suppresses its activity by intersecting with PKB/AKT1 signaling and antagonizing formation of AR-chromatin complexes (By similarity). {ECO:0000250|UniProtKB:Q13043, ECO:0000269|PubMed:20080689}. PTM: Autophosphorylated on serine and threonine residues. Phosphorylation at Thr-387 by PKB/AKT1, leads to inhibition of its: kinase activity, nuclear translocation and autophosphorylation at Thr-183. It also diminishes its cleavage by caspases and its ability to phosphorylate FOXO3 (By similarity). {ECO:0000250|UniProtKB:Q13043}.; PTM: Proteolytically cleaved by caspase-3 during apoptosis at Asp-326 resulting in a 37 kDa form. Proteolytic cleavage results in kinase activation and nuclear translocation of the truncated form (MST1/N). {ECO:0000269|PubMed:11278283}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=The caspase-cleaved form cycles between nucleus and cytoplasm. {ECO:0000250}. SUBUNIT: Homodimer; mediated via the coiled-coil region. Interacts with NORE1, which inhibits autoactivation. Interacts with and stabilizes SAV1. Interacts with RASSF1. Interacts with FOXO3. Interacts with RASSF2 (via SARAH domain). Interacts with AR, PKB/AKT1, TNNI3 and SIRT1. Interacts with MARK3 and SCRIB in the presence of DLG5 (By similarity). Interacts with DLG5 (via PDZ domain 3) (PubMed:28087714). {ECO:0000250|UniProtKB:Q13043, ECO:0000269|PubMed:28087714}. +B2RQL2 STOX1_MOUSE Storkhead-box protein 1 990 108,902 Chain (1); Erroneous initiation (1) FUNCTION: Involved in regulating the levels of reactive oxidative species and reactive nitrogen species and in mitochondrial homeostasis in the placenta (By similarity). Required for regulation of inner ear epithelial cell proliferation via the AKT signaling pathway (PubMed:25677106). Involved in cell cycle regulation by binding to the CCNB1 promoter, up-regulating its expression and promoting mitotic entry (By similarity). Induces phosphorylation of MAPT/tau (By similarity). {ECO:0000250|UniProtKB:Q6ZVD7, ECO:0000269|PubMed:25677106}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25677106}. Cytoplasm {ECO:0000269|PubMed:25677106}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q6ZVD7}. Note=In epithelial cells, diffusely expressed in the cytoplasm, particularly in peri-membrane cortical regions (PubMed:25677106). Concentrated at centrosomes during metaphase (By similarity). {ECO:0000250|UniProtKB:Q6ZVD7, ECO:0000269|PubMed:25677106}. TISSUE SPECIFICITY: Detected in sensory epithelial cells of the inner ear but not in adjacent surrounding tissue (at protein level). {ECO:0000269|PubMed:25677106}. +P10856 STP1_MOUSE Spermatid nuclear transition protein 1 (STP-1) (TP-1) 55 6,407 Chain (1); Modified residue (2) FUNCTION: Plays a key role in the replacement of histones to protamine in the elongating spermatids of mammals (PubMed:10781074, PubMed:15163613, PubMed:15189834, PubMed:15083521, PubMed:28366643). In condensing spermatids, loaded onto the nucleosomes, where it promotes the recruitment and processing of protamines, which are responsible for histone eviction (PubMed:28366643). The histone H2AFB1-HIST1H2BA/TH2B dimer is required for loading of TNP1 onto chromatin (PubMed:28366643). {ECO:0000269|PubMed:10781074, ECO:0000269|PubMed:15083521, ECO:0000269|PubMed:15163613, ECO:0000269|PubMed:15189834, ECO:0000269|PubMed:28366643}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15163613}. Chromosome {ECO:0000269|PubMed:28366643}. Note=Loaded onto the nucleosomes of condensing spermatids (PubMed:28366643). Inclusion of the H2AFB1-HIST1H2BA/TH2B dimer into chromatin opens the nucleosomes, releasing the nucleosomal DNA ends and allowing the invasion of nucleosomes by transition protein TNP1 (PubMed:28366643). {ECO:0000269|PubMed:28366643}. TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:3382664}. +A2RSX4 STPG3_MOUSE Protein STPG3 (Sperm-tail PG-rich repeat-containing protein 3) 306 34,690 Chain (1) +P70278 STRA8_MOUSE Stimulated by retinoic acid gene 8 protein 393 44,555 Chain (1); Coiled coil (1); Compositional bias (2); Motif (2); Sequence conflict (1) FUNCTION: Meiosis-inducer required for the transition into meiosis for both female and male germ cells. In female germ cells, required for premeiotic DNA replication and subsequent events in meiotic prophase. During spermatogenesis, next to its role in meiotic initiation, promotes (but is not required for) spermatogonial differentiation. Can associate with DNA (possibly in an indirect manner), and in vitro can activate DNA transcription. {ECO:0000269|PubMed:16461896, ECO:0000269|PubMed:17115059, ECO:0000269|PubMed:18799751, ECO:0000269|PubMed:18799790, ECO:0000269|PubMed:19805549, ECO:0000269|PubMed:25902548}. PTM: Phosphorylated in P19 EC cells. {ECO:0000269|PubMed:8896602}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19805549, ECO:0000269|PubMed:8896602}. Nucleus {ECO:0000269|PubMed:19805549}. Note=Shuttles between nucleus and cytoplasm. Nuclear export is XPO1-dependent. {ECO:0000269|PubMed:19805549}. SUBUNIT: Interacts with XPO1. {ECO:0000269|PubMed:19805549}. TISSUE SPECIFICITY: Expressed exclusively in premeiotic germ cells in both sexes. In females, is expressed in the embryonic ovary. In males, is expressed in pubertal and adult testes, in premeiotic spermatogenic cells. Expressed by some type A and B spermatogonia, preleptotene spermatocytes, and early leptotene spermatocytes (at protein level). Expression begins in late undifferentiated spermatogonia and persists during differentiating spermatogonia (at protein level). {ECO:0000269|PubMed:16461896, ECO:0000269|PubMed:18799790, ECO:0000269|PubMed:25902548, ECO:0000269|PubMed:8896602}. +Q3UUJ4 STRAA_MOUSE STE20-related kinase adapter protein alpha (STRAD alpha) (STE20-related adapter protein) 431 48,236 Alternative sequence (2); Chain (1); Domain (1); Modified residue (3) FUNCTION: Pseudokinase which, in complex with CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta), binds to and activates STK11/LKB1. Adopts a closed conformation typical of active protein kinases and binds STK11/LKB1 as a pseudosubstrate, promoting conformational change of STK11/LKB1 in an active conformation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250|UniProtKB:Q7RTN6}. SUBUNIT: Component of a trimeric complex composed of STK11/LKB1, STRAD (STRADA or STRADB) and CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta): the complex tethers STK11/LKB1 in the cytoplasm and stimulates its catalytic activity. {ECO:0000250}. DOMAIN: The protein kinase domain is predicted to be catalytically inactive. {ECO:0000255}. +Q8K4T3 STRAB_MOUSE STE20-related kinase adapter protein beta (STRAD beta) (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 2 protein homolog) (ILP-interacting protein homolog) (Polyploidy-associated protein kinase) (Pseudokinase ALS2CR2) 418 46,832 Alternative sequence (2); Binding site (1); Chain (1); Domain (1); Nucleotide binding (1); Sequence conflict (4) FUNCTION: Pseudokinase which, in complex with CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta), binds to and activates STK11/LKB1. Adopts a closed conformation typical of active protein kinases and binds STK11/LKB1 as a pseudosubstrate, promoting conformational change of STK11/LKB1 in an active conformation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. SUBUNIT: Component of a trimeric complex composed of STK11/LKB1, STRAD (STRADA or STRADB) and CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta): the complex tethers STK11/LKB1 in the cytoplasm and stimulates its catalytic activity. Interacts with BIRC4/XIAP. These two proteins are likely to coexist in a complex with TAK1, TRAF6, TAB1 and TAB2 (By similarity). {ECO:0000250}. DOMAIN: The protein kinase domain is predicted to be catalytically inactive. +O55106 STRN_MOUSE Striatin 780 85,966 Chain (1); Coiled coil (1); Compositional bias (1); Modified residue (6); Region (2); Repeat (6); Sequence conflict (1) FUNCTION: Binds calmodulin in a calcium dependent manner. May function as scaffolding or signaling protein. SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein. Cell projection, dendritic spine {ECO:0000250}. Note=CTTNBP2-binding may regulate dendritic spine distribution. {ECO:0000250}. SUBUNIT: Interacts with protein phosphatase 2A (PP2A) (Potential). Interacts with CTTNBP2; this interaction may regulate dendritic spine distribution of STRN. Activation of glutamate receptors weakens the interaction with CTTNBP2 (By similarity). {ECO:0000250, ECO:0000305}. TISSUE SPECIFICITY: Mainly expressed in brain but is also expressed at low levels in various tissues such as kidney, spleen, skeletal muscle and lung. {ECO:0000269|PubMed:10748158}. +Q8C9H6 STRP2_MOUSE Striatin-interacting proteins 2 (Protein FAM40B) 844 96,294 Alternative sequence (3); Chain (1); Modified residue (3); Sequence conflict (1) FUNCTION: Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Enriched in lamellipodia. {ECO:0000250}. SUBUNIT: Component of striatin-interacting phosphatase and kinase (STRIPAK) complex. Interacts with CTTNBP2NL (By similarity). {ECO:0000250}. +P55821 STMN2_MOUSE Stathmin-2 (Superior cervical ganglion-10 protein) (Protein SCG10) 179 20,828 Chain (1); Coiled coil (1); Domain (1); Lipidation (2); Modified residue (6); Region (2) FUNCTION: Regulator of microtubule stability. When phosphorylated by MAPK8, stabilizes microtubules and consequently controls neurite length in cortical neurons. In the developing brain, negatively regulates the rate of exit from multipolar stage and retards radial migration from the ventricular zone. {ECO:0000269|PubMed:21297631}. PTM: Sumoylated. {ECO:0000250}.; PTM: Phosphorylated mostly by MAPK8, but also by MAPK9 and MAPK10 in the developing brain cortex. {ECO:0000269|PubMed:16618812}.; PTM: N-terminal palmitoylation promotes specific anchoring to the cytosolic leaflet of Golgi membranes and subsequent vesicular trafficking along dendrites and axons. Neuronal Stathmins are substrates for palmitoyltransferases ZDHHC3, ZDHHC7 and ZDHHC15 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16618812}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16618812}. Cell projection, growth cone {ECO:0000269|PubMed:16618812}. Cell projection, axon {ECO:0000269|PubMed:16618812}. Membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Endosome {ECO:0000250}. Golgi apparatus {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Note=Colocalized with CIB1 in neurites of developing hippocampal primary neurons. Colocalized with CIB1 in the cell body, neuritis, growth cones of neurons and in neurites of developing hippocampal primary neurons. Colocalized with CIB1 to the leading edge of lamellipodia (By similarity). Associated with punctate structures in the perinuclear cytoplasm, axons, and growth cones of developing neurons. Exists in both soluble and membrane-bound forms. In the developing brain, mostly cytosolic. {ECO:0000250}. SUBUNIT: Interacts with ITM2C. Interacts with MAPK8. Interacts with KIF1BP. Interacts (via the N-terminal region) with CIB1 (via C-terminal region); the interaction is direct, occurs in a calcium-dependent manner and attenuates the neurite outgrowth inhibition of STMN2. {ECO:0000250}. TISSUE SPECIFICITY: Neuron specific. +P0DP99 STMP1_MOUSE Short transmembrane mitochondrial protein 1 47 5,400 Chain (1); Transmembrane (1) TRANSMEM 7 23 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000255}. +Q8BVI5 STX16_MOUSE Syntaxin-16 326 37,080 Chain (1); Domain (1); Erroneous initiation (1); Modified residue (2); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 303 323 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 1 302 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 324 326 Vesicular. {ECO:0000255}. FUNCTION: SNARE involved in vesicular transport from the late endosomes to the trans-Golgi network. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. SUBUNIT: Interacts with GCC2 (By similarity). Interacts with BAIAP3; this interaction is increased in the presence of calcium (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O14662}. +Q8BZ60 STON2_MOUSE Stonin-2 (Stoned B) 895 99,611 Chain (1); Domain (2); Modified residue (4); Motif (2) FUNCTION: Adapter protein involved in endocytic machinery. Involved in the synaptic vesicle recycling. May facilitate clathrin-coated vesicle uncoating (By similarity). {ECO:0000250}. PTM: Phosphorylated in vitro by PKD. {ECO:0000250}.; PTM: Neddylated; deneddylated via its interaction with the COP9 signalosome (CSN) complex through TOR1A and COPS4. {ECO:0000250}.; PTM: Ubiquitinated; leading to its degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}. Cell junction, synapse, synaptosome {ECO:0000250}. Note=Some fraction is membrane-associated. SUBUNIT: Interacts with the second C2 domain of synaptotagmins SYT1 and SYT2. Interacts with EPS15, EPS15R and ITSN1. Interacts indirectly with the AP-2 adapter complex. Interacts with TOR1A and COPS4; the interaction controls STON2 protein stability (By similarity). {ECO:0000250}. DOMAIN: The Asn-Pro-Phe (NPF) motifs, which are found in proteins involved in the endocytic pathway, mediate the interaction with the EH domain of SYT1, SYT2, EPS15, EPS15R and ITSN1. {ECO:0000250}. +Q64324 STXB2_MOUSE Syntaxin-binding protein 2 (MUSEC1) (Protein unc-18 homolog 2) (Munc18-2) (Unc18-2) (Protein unc-18 homolog B) (Unc-18B) 593 66,357 Chain (1) FUNCTION: Involved in intracellular vesicle trafficking and vesicle fusion with membranes. Contributes to the granule exocytosis machinery through interaction with soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins that regulate membrane fusion. Regulates cytotoxic granule exocytosis in natural killer (NK) cells (By similarity). {ECO:0000250}. SUBUNIT: Interacts with STX1A, STX2 and STX3. Interacts with STX11. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in testis, intestine, kidney, rat adipose tissue and 3T3-L1 cells. +Q60770 STXB3_MOUSE Syntaxin-binding protein 3 (MUNC-18-3) (Mammalian homolog of Unc-18c) (Munc-18c) (Protein unc-18 homolog 3) (Unc18-3) (Protein unc-18 homolog C) (Unc-18C) 592 67,942 Alternative sequence (2); Beta strand (20); Chain (1); Frameshift (1); Helix (26); Region (1); Sequence conflict (6); Turn (7) FUNCTION: Together with STX4 and VAMP2, may play a role in insulin-dependent movement of GLUT4 and in docking/fusion of intracellular GLUT4-containing vesicles with the cell surface in adipocytes. {ECO:0000269|PubMed:9045631}. PTM: Phosphorylated by PKC in platelets in response to thrombin stimulation; phosphorylation inhibits binding to STX4. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:9045631}. Note=In platelets, predominantly cytosolic. Low amounts membrane-associated (By similarity). {ECO:0000250}. SUBUNIT: Interacts with STX4. Interacts with DOC2B; the interaction is direct, occurs at the cell membrane, excludes interaction with STX4 and regulates glucose-stimulated insulin secretion. {ECO:0000269|PubMed:17548353, ECO:0000269|PubMed:9045631}. TISSUE SPECIFICITY: Ubiquitously expressed in all tissues tested. {ECO:0000269|PubMed:8824310}. +Q64704 STX3_MOUSE Syntaxin-3 289 33,243 Alternative sequence (4); Chain (1); Coiled coil (1); Domain (1); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 264 283 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 1 263 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 284 289 Extracellular. {ECO:0000255}. FUNCTION: Potentially involved in docking of synaptic vesicles at presynaptic active zones. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}. +Q8R3T5 STXB6_MOUSE Syntaxin-binding protein 6 210 23,671 Chain (1); Domain (1); Initiator methionine (1); Modified residue (1) FUNCTION: Forms non-fusogenic complexes with SNAP25 and STX1A and may thereby modulate the formation of functional SNARE complexes and exocytosis. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. SUBUNIT: Part of a ternary complex containing SNAP25 and STX1A that can be dissociated by NAPA and NSF. Interacts with STX4A (By similarity). {ECO:0000250}. +P70452 STX4_MOUSE Syntaxin-4 298 34,165 Chain (1); Coiled coil (1); Domain (1); Helix (1); Modified residue (6); Region (1); Sequence conflict (3); Topological domain (2); Transmembrane (1) TRANSMEM 275 295 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 1 274 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 296 298 Extracellular. {ECO:0000255}. FUNCTION: Plasma membrane t-SNARE that mediates docking of transport vesicles. Necessary for the translocation of SLC2A4 from intracellular vesicles to the plasma membrane. Together with STXB3 and VAMP2, may also play a role in docking/fusion of intracellular GLUT4-containing vesicles with the cell surface in adipocytes and in docking of synaptic vesicles at presynaptic active zones. {ECO:0000269|PubMed:10394363, ECO:0000269|PubMed:18827011, ECO:0000269|PubMed:9045631}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}. SUBUNIT: Interacts with STXBP6. Component of the SNARE complex composed of STX4, SNAP23 and VAMP7 that interacts with SYT7 during lysosomal exocytosis (By similarity). Found in a complex with VAMP8 and SNAP23. Detected in a complex with SNAP23 and STXBP4. Interacts with VAMP2. Interacts with SNAP23 and SNAPIN. Interacts with LLGL1. Interacts (via C-terminus) with CENPF. Interacts with DOC2B. Interacts with STXBP3; excludes interaction with DOC2B and SNAP25. Interacts with STXBP4; excludes interaction with VAMP2. {ECO:0000250, ECO:0000269|PubMed:10394363, ECO:0000269|PubMed:11809830, ECO:0000269|PubMed:12877659, ECO:0000269|PubMed:15363411, ECO:0000269|PubMed:17548353, ECO:0000269|PubMed:18827011, ECO:0000269|PubMed:19033398, ECO:0000269|PubMed:9045631}. +Q60969 STYX_MOUSE Serine/threonine/tyrosine-interacting protein (Inactive tyrosine-protein phosphatase Styx) (Phosphoserine/threonine/tyrosine interaction protein) 223 25,430 Alternative sequence (1); Chain (1); Domain (1); Modified residue (2); Motif (1); Mutagenesis (1); Sequence conflict (3) FUNCTION: Catalytically inactive phosphatase (PubMed:7592916). Acts as a nuclear anchor for MAPK1/MAPK3 (ERK1/ERK2) (By similarity). Modulates cell-fate decisions and cell migration by spatiotemporal regulation of MAPK1/MAPK3 (ERK1/ERK2) (By similarity). By binding to the F-box of FBXW7, prevents the assembly of FBXW7 into the SCF E3 ubiquitin-protein ligase complex, and thereby inhibits degradation of its substrates (By similarity). Plays a role in spermatogenesis (PubMed:11842224). {ECO:0000250|UniProtKB:Q8WUJ0, ECO:0000269|PubMed:11842224, ECO:0000269|PubMed:7592916}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8WUJ0}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8WUJ0}. Note=Predominantly localizes to the nucleus. {ECO:0000250|UniProtKB:Q8WUJ0}. SUBUNIT: Interacts with MAPK1; independently of MAPK1 phosphorylation status (By similarity). Interacts with CARHSP1/Crhsp-24 (PubMed:11842224). Interacts (via FQQ motif) with FBXW7 (via F-box domain); the interaction is direct and prevents FBXW7 interaction with SKP1, a component of the SCF(FBXW7) complex (By similarity). {ECO:0000250|UniProtKB:Q8WUJ0, ECO:0000269|PubMed:11842224}. TISSUE SPECIFICITY: Widely expressed with highest levels in muscle, testis and brain (PubMed:7592916). In testis, expression starts 13-14 days after birth and is limited to the seminiferous tubule and to round and elongating spermatids (PubMed:11842224). Expression is low in condensing spermatids and pachytene spermatocytes, and absent in spermatogonia, spermatozoa and somatic Sertoli cells (PubMed:11842224). {ECO:0000269|PubMed:11842224, ECO:0000269|PubMed:7592916}. +Q9WUM5 SUCA_MOUSE Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial (EC 6.2.1.4) (EC 6.2.1.5) (Succinyl-CoA synthetase subunit alpha) (SCS-alpha) 346 36,155 Active site (1); Binding site (2); Chain (1); Erroneous initiation (5); Modified residue (9); Region (2); Sequence conflict (5); Transit peptide (1) Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1. FUNCTION: Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and specificity for either ATP or GTP is provided by different beta subunits. {ECO:0000255|HAMAP-Rule:MF_03222}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03222}. SUBUNIT: Heterodimer of an alpha and a beta subunit. Different beta subunits determine nucleotide specificity. Together with the ATP-specific beta subunit SUCLA2, forms an ADP-forming succinyl-CoA synthetase (A-SCS). Together with the GTP-specific beta subunit SUCLG2 forms a GDP-forming succinyl-CoA synthetase (G-SCS). {ECO:0000255|HAMAP-Rule:MF_03222}. +Q9Z2I8 SUCB2_MOUSE Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial (EC 6.2.1.4) (GTP-specific succinyl-CoA synthetase subunit beta) (G-SCS) (GTPSCS) (Succinyl-CoA synthetase beta-G chain) (SCS-betaG) 433 46,840 Alternative sequence (1); Binding site (3); Chain (1); Domain (1); Metal binding (2); Modified residue (18); Nucleotide binding (1); Region (1); Sequence conflict (5); Site (2); Transit peptide (1) Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1. FUNCTION: GTP-specific succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit. {ECO:0000255|HAMAP-Rule:MF_03221}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03221}. SUBUNIT: Heterodimer of an alpha and a beta subunit. The beta subunit determines specificity for GTP. {ECO:0000255|HAMAP-Rule:MF_03221}. +Q61056 TRPC1_MOUSE Short transient receptor potential channel 1 (TrpC1) (Transient receptor protein 1) (TRP-1) (mTrp1) (Trp-related protein 1) 793 91,213 Alternative sequence (1); Chain (1); Erroneous initiation (3); Repeat (4); Topological domain (7); Transmembrane (6) TRANSMEM 387 407 Helical. {ECO:0000255}.; TRANSMEM 416 436 Helical. {ECO:0000255}.; TRANSMEM 496 516 Helical. {ECO:0000255}.; TRANSMEM 540 560 Helical. {ECO:0000255}.; TRANSMEM 587 607 Helical. {ECO:0000255}.; TRANSMEM 617 637 Helical. {ECO:0000255}. TOPO_DOM 1 386 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 408 415 Extracellular. {ECO:0000255}.; TOPO_DOM 437 495 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 517 539 Extracellular. {ECO:0000255}.; TOPO_DOM 561 586 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 608 616 Extracellular. {ECO:0000255}.; TOPO_DOM 638 793 Cytoplasmic. {ECO:0000255}. FUNCTION: Thought to form a receptor-activated non-selective calcium permeant cation channel. Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Seems to be also activated by intracellular calcium store depletion. PTM: Activation of PRKCA induces phosphorylation of TRPC1 and subsequent Ca2+ entry into cells. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Homotetramer and heterotetramer with TRPC4 and/or TRPC5 (By similarity). Interacts with TRPC3, TRPC4 and TRPC5 (By similarity). Interacts with ITPR3 (By similarity). Interacts with MX1 and RNF24 (By similarity). Interacts with FKBP4 (By similarity). Interacts with TRPC4AP. {ECO:0000250, ECO:0000269|PubMed:20458742}. +Q9QZC1 TRPC3_MOUSE Short transient receptor potential channel 3 (TrpC3) (Receptor-activated cation channel TRP3) (Transient receptor protein 3) (TRP-3) (mTrp3) (Trp-related protein 3) 836 95,672 Chain (1); Glycosylation (1); Repeat (4); Topological domain (7); Transmembrane (6) TRANSMEM 370 390 Helical. {ECO:0000255}.; TRANSMEM 419 439 Helical. {ECO:0000255}.; TRANSMEM 452 472 Helical. {ECO:0000255}.; TRANSMEM 524 544 Helical. {ECO:0000255}.; TRANSMEM 568 588 Helical. {ECO:0000255}.; TRANSMEM 638 658 Helical. {ECO:0000255}. TOPO_DOM 1 369 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 391 418 Extracellular. {ECO:0000255}.; TOPO_DOM 440 451 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 473 523 Extracellular. {ECO:0000255}.; TOPO_DOM 545 567 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 589 637 Extracellular. {ECO:0000255}.; TOPO_DOM 659 836 Cytoplasmic. {ECO:0000255}. FUNCTION: Thought to form a receptor-activated non-selective calcium permeant cation channel. Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Activated by diacylglycerol (DAG) in a membrane-delimited fashion, independently of protein kinase C, and by inositol 1,4,5-triphosphate receptors (ITPR) with bound IP3 (By similarity). May also be activated by internal calcium store depletion. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Interacts with TRPC1, ITPR1, ITPR3, MX1 and RNF24. Interacts with JPH2; the interaction is involved in maintaining Ca(2+) homeostasis in skeletal muscle and is mediated by JPH2 'Ser-165' phosphorylation (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Abundantly expressed in brain. Concentrated in cerebellar Purkinje cells and sparsely localized in cerebellar granule lyer, pontine nuclei and thalamus. Lower levels detected in other tissues. +Q7TNE1 SUCHY_MOUSE Succinate--hydroxymethylglutarate CoA-transferase (EC 2.8.3.13) (SuccinylCoA:glutarate-CoA transferase) 436 47,690 Active site (1); Chain (1); Modified residue (2); Sequence conflict (1); Transit peptide (1) FUNCTION: Catalyzes the succinyl-CoA-dependent conversion of glutarate to glutaryl-CoA. Can use different dicarboxylic acids as CoA acceptors, the preferred ones are glutarate, succinate, adipate, and 3-hydroxymethylglutarate (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. +Q8C341 SUCO_MOUSE SUN domain-containing ossification factor (Membrane protein CH1) (Protein osteopotentia) (SUN-like protein 1) 1250 139,169 Alternative sequence (1); Chain (1); Coiled coil (1); Domain (1); Glycosylation (5); Modified residue (1); Sequence conflict (2); Signal peptide (1); Transmembrane (1) TRANSMEM 1007 1027 Helical. {ECO:0000255}. FUNCTION: Required for bone modeling during late embryogenesis. Regulates type I collagen synthesis in osteoblasts during their postnatal maturation. {ECO:0000269|PubMed:20440000}. PTM: N-glycosylated. {ECO:0000269|PubMed:20440000}.; PTM: O-glycosylated. O-mannosylated by POMT1 and POMT2 and elongated by POMGNT1. {ECO:0000250|UniProtKB:Q9UBS9}. SUBCELLULAR LOCATION: Rough endoplasmic reticulum membrane {ECO:0000269|PubMed:20440000}; Single-pass type I membrane protein {ECO:0000269|PubMed:20440000}. TISSUE SPECIFICITY: Present in chondrocytes, osteoblasts, osteoclasts and osteocytes (at protein level). {ECO:0000269|PubMed:20440000}. +Q8CH09 SUGP2_MOUSE SURP and G-patch domain-containing protein 2 (Arginine/serine-rich-splicing factor 14) (Splicing factor, arginine/serine-rich 14) 1067 118,103 Chain (1); Compositional bias (1); Cross-link (1); Domain (1); Frameshift (1); Modified residue (8); Motif (1); Natural variant (1); Repeat (2); Sequence conflict (2) FUNCTION: May play a role in mRNA splicing. {ECO:0000305}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +P31266 SUH_MOUSE Recombining binding protein suppressor of hairless (J kappa-recombination signal-binding protein) (RBP-J kappa) 526 58,537 Alternative sequence (2); Beta strand (31); Chain (1); DNA binding (3); Domain (1); Helix (7); Modified residue (1); Turn (1) FUNCTION: Transcriptional regulator that plays a central role in Notch signaling, a signaling pathway involved in cell-cell communication that regulates a broad spectrum of cell-fate determinations (PubMed:7566092). Acts as a transcriptional repressor when it is not associated with Notch proteins. When associated with some NICD product of Notch proteins (Notch intracellular domain), it acts as a transcriptional activator that activates transcription of Notch target genes. Probably represses or activates transcription via the recruitment of chromatin remodeling complexes containing histone deacetylase or histone acetylase proteins, respectively. Specifically binds to the immunoglobulin kappa-type J segment recombination signal sequence. Binds specifically to methylated DNA. Binds to the oxygen responsive element of COX4I2 and activates its transcription under hypoxia conditions (4% oxygen) (By similarity). Negatively regulates the phagocyte oxidative burst in response to bacterial infection by repressing transcription of NADPH oxidase subunits (PubMed:26194095). {ECO:0000250|UniProtKB:Q06330, ECO:0000269|PubMed:26194095, ECO:0000269|PubMed:7566092}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm {ECO:0000250}. Note=Mainly nuclear, upon interaction with RITA1, translocates to the cytoplasm, down-regulating the Notch signaling pathway. {ECO:0000250}. SUBUNIT: Interacts with RITA1, leading to nuclear export, prevent the interaction between RBPJ and NICD product and subsequent down-regulation of the Notch signaling pathway (By similarity). Interacts with activated NOTCH1, NOTCH2 and NOTCH3. Interacts with MINT/SHARP. This interaction may mediate the recruitment of large corepressor complexes containing proteins such as HDAC1, HDAC2, NCOR2, SAP30, FHL1/KYOT2 and CIR1. Interacts with EP300, MAML1 and PTF1A. Interacts with SNW1. Interacts with CHCHD2 and CXXC5. Interacts with BEND6 (via BEN domain) (By similarity). Interacts with NKAPL (PubMed:25875095). Interacts with ZMIZ1 (By similarity). Interacts with RBM15 (PubMed:17283045). {ECO:0000250|UniProtKB:Q06330, ECO:0000269|PubMed:10640276, ECO:0000269|PubMed:11318877, ECO:0000269|PubMed:11604511, ECO:0000269|PubMed:17283045, ECO:0000269|PubMed:25875095, ECO:0000269|PubMed:7566092, ECO:0000269|PubMed:9418910}. +Q8BPG6 SUMF2_MOUSE Inactive C-alpha-formylglycine-generating enzyme 2 (Sulfatase-modifying factor 2) 308 34,737 Chain (1); Disulfide bond (1); Erroneous initiation (1); Glycosylation (1); Metal binding (8); Motif (1); Sequence conflict (2); Signal peptide (1) FUNCTION: Lacks formylglycine generating activity and is unable to convert newly synthesized inactive sulfatases to their active form. Inhibits the activation of sulfatases by SUMF1. {ECO:0000250|UniProtKB:Q8NBJ7}. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:Q8NBJ7}. SUBUNIT: Homodimer and heterodimer with SUMF1. {ECO:0000250|UniProtKB:Q8NBJ7}. DOMAIN: The non-canonical ER retention motif mediates retention of the protein in the endoplasmic reticulum. {ECO:0000250|UniProtKB:Q8NBJ7}. +P63166 SUMO1_MOUSE Small ubiquitin-related modifier 1 (SUMO-1) (SMT3 homolog 3) (Ubiquitin-homology domain protein PIC1) (Ubiquitin-like protein SMT3C) (Smt3C) 101 11,557 Chain (1); Cross-link (11); Domain (1); Initiator methionine (1); Modified residue (4); Propeptide (1); Site (1) FUNCTION: Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Covalently attached to the voltage-gated potassium channel KCNB1; this modulates the gating characteristics of KCNB1. Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development. Covalently attached to ZFHX3 (By similarity). {ECO:0000250|UniProtKB:P63165, ECO:0000269|PubMed:16990542}. PTM: Cleavage of precursor form by SENP1 or SENP2 is necessary for function. {ECO:0000250}.; PTM: Polymeric SUMO1 chains undergo polyubiquitination by RNF4. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus membrane. Nucleus speckle. Cytoplasm. Nucleus, PML body {ECO:0000250}. Cell membrane {ECO:0000250|UniProtKB:P63165}. Nucleus {ECO:0000250|UniProtKB:P63165}. Note=Recruited by BCL11A into the nuclear body. In the presence of ZFHX3, sequesterd to nuclear body (NB)-like dots in the nucleus some of which overlap or closely associate with PML body (By similarity). {ECO:0000250|UniProtKB:P63165, ECO:0000269|PubMed:18681895}. SUBUNIT: Interacts with USP25 (via ts SIM domain) the interaction weakly sumoylates USP25. Covalently attached to KCNB1; UBE2I increases cross-linking with KCNB1 and PIAS1 decreases cross-links with KCNB1 (By similarity). Interacts with SAE2, UBE2I, RANBP2, PIAS1 and PIAS2. Interacts with PRKN. Covalently attached to a number of proteins such as IKFZ1, PML, RANGAP1, HIPK2, SP100, p53, p73-alpha, MDM2, JUN, DNMT3B and TDG. Also interacts with HIF1A, HIPK2, HIPK3, CHD3, EXOSC9, RAD51 and RAD52. Interacts with SIMC1, CASP8AP2, RNF111 AND SOBP (via SIM domains). Interacts with BHLHE40/DEC1. Interacts with RWDD3. Interacts with UBE2I/UBC9 and this interaction is enhanced in the presence of RWDD3. Interacts with MTA1 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P63165}. TISSUE SPECIFICITY: Ubiquitous. +Q9Z172 SUMO3_MOUSE Small ubiquitin-related modifier 3 (SUMO-3) (SMT3 homolog 1) (Ubiquitin-like protein SMT3A) (Smt3A) 110 12,430 Alternative sequence (1); Chain (1); Cross-link (5); Domain (1); Propeptide (1) FUNCTION: Ubiquitin-like protein which can be covalently attached to target lysines either as a monomer or as a lysine-linked polymer. Does not seem to be involved in protein degradation and may function as an antagonist of ubiquitin in the degradation process. Plays a role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Covalent attachment to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by an E3 ligase such as PIAS1-4, RANBP2 or CBX4. Plays a role in the regulation of sumoylation status of SETX (By similarity). {ECO:0000250|UniProtKB:P55854}. PTM: Polymeric chains can be formed through Lys-11 cross-linking. {ECO:0000250}.; PTM: Cleavage of precursor form by SENP1, SENP2 or SENP5 is necessary for function. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Nucleus, PML body {ECO:0000269|PubMed:18644859}. SUBUNIT: Interacts with SAE2 and UBE2I. Covalently attached to a number of proteins. Interacts with USP25 (via ts SIM domain); the interaction sumoylates USP25 and inhibits its ubiquitin hydrolyzing activity (By similarity). Interacts with ARNTL/BMAL1. {ECO:0000250, ECO:0000269|PubMed:18644859}. +Q8BLS7 SWAHA_MOUSE Ankyrin repeat domain-containing protein SOWAHA (Ankyrin repeat domain-containing protein 43) (Protein sosondowah homolog A) 548 57,749 Chain (1); Compositional bias (2); Erroneous initiation (1); Frameshift (1); Modified residue (1); Repeat (2); Sequence conflict (2); Signal peptide (1) +Q9EQQ0 SUV92_MOUSE Histone-lysine N-methyltransferase SUV39H2 (EC 2.1.1.43) (Histone H3-K9 methyltransferase 2) (H3-K9-HMTase 2) (Suppressor of variegation 3-9 homolog 2) (Su(var)3-9 homolog 2) 477 54,098 Binding site (1); Chain (1); Domain (4); Erroneous gene model prediction (1); Metal binding (17); Modified residue (3); Region (2); Sequence conflict (5) FUNCTION: Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys-9' as substrate. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions. H3 'Lys-9' trimethylation is also required to direct DNA methylation at pericentric repeats. SUV39H1 is targeted to histone H3 via its interaction with RB1 and is involved in many processes, such as cell cycle regulation, transcriptional repression and regulation of telomere length. May participate in regulation of higher-order chromatin organization during spermatogenesis. Recruited by the large PER complex to the E-box elements of the circadian target genes such as PER2 itself or PER1, contributes to the conversion of local chromatin to a heterochromatin-like repressive state through H3 'Lys-9' trimethylation. {ECO:0000269|PubMed:11701123, ECO:0000269|PubMed:14690609, ECO:0000269|PubMed:14690610, ECO:0000269|PubMed:14702045, ECO:0000269|PubMed:24413057}. SUBCELLULAR LOCATION: Nucleus. Chromosome. Chromosome, centromere. Note=Associates with centromeric constitutive heterochromatin during most stages of spermato- and spermiogenesis. Predominantly accumulates at the sex chromosomes present at the XY body. SUBUNIT: Interacts with SMAD5. The large PER complex involved in the histone methylation is composed of at least PER2, CBX3, TRIM28, SUV39H1 and/or SUV39H2; CBX3 mediates the formation of the complex. DOMAIN: Although the SET domain contains the active site of enzymatic activity, both pre-SET and post-SET domains are required for methyltransferase activity. The SET domain also participates in stable binding to heterochromatin (By similarity). {ECO:0000250}.; DOMAIN: In the pre-SET domain, Cys residues bind 3 zinc ions that are arranged in a triangular cluster; some of these Cys residues contribute to the binding of two zinc ions within the cluster. {ECO:0000250}. TISSUE SPECIFICITY: Testis specific; predominant expression in type B spermatogonia and preleptotene spermatocytes. +Q925H1 TRPS1_MOUSE Zinc finger transcription factor Trps1 1281 141,035 Chain (1); Cross-link (28); Modified residue (8); Region (3); Zinc finger (8) FUNCTION: Transcriptional repressor. Binds specifically to GATA sequences and represses expression of GATA-regulated genes at selected sites and stages in vertebrate development. Regulates chondrocyte proliferation and differentiation. Executes multiple functions in proliferating chondrocytes, expanding the region of distal chondrocytes, activating proliferation in columnar cells and supporting the differentiation of columnar into hypertrophic chondrocytes. {ECO:0000269|PubMed:11285235, ECO:0000269|PubMed:19389374}. PTM: Sumoylated. Sumoylation in the repressor domain inhibits the transcription repression activity. Sumoylation on Lys-1201 is the major site. Appears to be sumoylated on multiple sites (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with RNF4; regulates TRPS1 repressor activity. Interacts specifically with the activator form of GLI3 (GLI3A) but not with the repressor form (GLI3R). {ECO:0000269|PubMed:12885770, ECO:0000269|PubMed:19389374}. TISSUE SPECIFICITY: In the embryo, expression is detected in both visceral and skeletal tissues. Found in the maxilla, mandible, snout, prospective phalanges and in the femoral head within the developing hip. Also expressed in the hair follicles. +Q9CUU3 SYCP2_MOUSE Synaptonemal complex protein 2 (SCP-2) (Synaptonemal complex lateral element protein) 1500 172,123 Beta strand (10); Chain (1); Coiled coil (1); Compositional bias (1); Helix (21); Modified residue (33); Sequence caution (1); Turn (1) FUNCTION: Major component of the axial/lateral elements of synaptonemal complexes (SCS) during meiotic prophase. Plays a role in the assembly of synaptonemal complexes (PubMed:16717126). Required for normal meiotic chromosome synapsis during oocyte and spermatocyte development and for normal male and female fertility (PubMed:16717126). Required for insertion of SYCP3 into synaptonemal complexes (PubMed:16717126). May be involved in the organization of chromatin by temporarily binding to DNA scaffold attachment regions. Requires SYCP3, but not SYCP1, in order to be incorporated into the axial/lateral elements. {ECO:0000269|PubMed:11463847, ECO:0000269|PubMed:16717126}. PTM: Phosphorylated. {ECO:0000269|PubMed:22346761}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16717126}. Chromosome {ECO:0000269|PubMed:16717126, ECO:0000269|PubMed:22346761}. Note=In axial/lateral elements of the tripartite segments of synaptonemal complexes. {ECO:0000269|PubMed:16717126}. SUBUNIT: Component of the lateral elements of synaptonemal complexes (PubMed:16717126). Heterodimer with SYCP3 (PubMed:16717126). Interacts with SMC1A and SMC3 (By similarity). Interacts with TEX11 (PubMed:18316482). {ECO:0000250|UniProtKB:O70608, ECO:0000269|PubMed:16717126, ECO:0000269|PubMed:18316482}. TISSUE SPECIFICITY: Detected in testis and spermatocytes (at protein level). {ECO:0000269|PubMed:16717126}. +Q80YV3 TRRAP_MOUSE Transformation/transcription domain-associated protein (Tra1 homolog) 2565 291,557 Chain (1); Cross-link (1); Domain (3); Modified residue (4); Motif (1); Region (1) FUNCTION: Adapter protein, which is found in various multiprotein chromatin complexes with histone acetyltransferase activity (HAT), which gives a specific tag for epigenetic transcription activation. Component of the NuA4 histone acetyltransferase complex which is responsible for acetylation of nucleosomal histones H4 and H2A. Plays a central role in MYC transcription activation, and also participates in cell transformation by MYC. Required for p53/TP53-, E2F1- and E2F4-mediated transcription activation. Probably acts by linking transcription factors such as E1A, MYC or E2F1 to HAT complexes such as STAGA thereby allowing transcription activation. Probably not required in the steps following histone acetylation in processes of transcription activation. May be required for the mitotic checkpoint and normal cell cycle progression. Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AFZ from the nucleosome. {ECO:0000269|PubMed:11544477}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with MYC, E2F1 and E2F4 transcription factors. Interacts directly with p53/TP53. Interacts with GCN5L2. Component of various HAT complexes. Component of the PCAF complex, at least composed of TADA2L/ADA2, SUPT3H, TADA3L/ADA3, TAF5L/PAF65-beta, TAF6L/PAF65-alpha, TAF10/TAFII30, TAF12/TAFII20, TAF9/TAFII31 and TRRAP. Component of the TFTC-HAT complex, at least composed of TAF5L, TAF6L, TADA3L, SUPT3H/SPT3, TAF2/TAFII150, TAF4/TAFII135, TAF5/TAFII100, GCN5L2/GCN5, TAF10 and TRRAP. Component of the NuA4 histone acetyltransferase complex which contains the catalytic subunit KAT5/TIP60 and the subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6. Component of the STAGA complex, at least composed of SUPT3H, GCN5L2, SUPT7L, TAF5L, TAF6L, TADA3L, TAD1L, TAF10, TAF12, TRRAP and TAF9. The STAGA core complex is associated with a subcomplex required for histone deubiquitination composed of ATXN7L3, ENY2 and USP22. Component of the BAF53 complex, at least composed of BAF53A, RUVBL1, SMARCA4/BRG1, and TRRAP, which preferentially acetylates histone H4 (and H2A) within nucleosomes. Interacts with NPAT (By similarity). Interaction with TELO2 AND TTI1. Component of a SWR1-like complex (By similarity). {ECO:0000250}. DOMAIN: The PI3K/PI4K domain is required for the recruitment of HAT complexes, and the MYC-dependent transactivation. Although it is strongly related to the PI3/PI4-kinase family, it lacks the typical motifs that constitute the catalytic site of PI3/PI4-kinase proteins, and lacks such activity (By similarity). {ECO:0000250}. +Q8C0D0 TRUB1_MOUSE Probable tRNA pseudouridine synthase 1 (EC 5.4.99.-) 338 36,348 Active site (1); Alternative sequence (2); Chain (1); Initiator methionine (1); Modified residue (1); Sequence conflict (2) FUNCTION: Pseudouridine synthase that catalyzes pseudouridylation of mRNAs. Mediates pseudouridylation of mRNAs with the consensus sequence 5'-GUUCNANNC-3', harboring a stem-loop structure. Constitutes the major pseudouridine synthase acting on mRNAs. {ECO:0000250|UniProtKB:Q8WWH5}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8WWH5}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8WWH5}. Note=Catalyzes pseudouridylation of mRNAs in the nucleus. {ECO:0000250|UniProtKB:Q8WWH5}. +Q91WG3 TRUB2_MOUSE Mitochondrial mRNA pseudouridine synthase Trub2 (EC 5.4.99.-) 331 36,807 Active site (1); Chain (1); Sequence conflict (1); Transit peptide (1) FUNCTION: Minor enzyme contributing to the isomerization of uridine to pseudouridine (pseudouridylation) of specific mitochondrial mRNAs (mt-mRNAs) such as COXI and COXIII mt-mRNAs. As a component of a functional protein-RNA module, consisting of RCC1L, NGRN, RPUSD3, RPUSD4, TRUB2, FASTKD2 and 16S mitochondrial ribosomal RNA (16S mt-rRNA), controls 16S mt-rRNA abundance and is required for intra-mitochondrial translation. {ECO:0000250|UniProtKB:O95900}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:O95900}. Note=Localizes to mitochondrial RNA granules, platforms for post-transcriptional RNA modification and ribosome assembly. {ECO:0000250|UniProtKB:O95900}. SUBUNIT: Forms a regulatory protein-RNA complex, consisting of RCC1L, NGRN, RPUSD3, RPUSD4, TRUB2, FASTKD2 and 16S mt-rRNA. {ECO:0000250|UniProtKB:O95900}. +P70281 SYCP3_MOUSE Synaptonemal complex protein 3 (SCP-3) 254 29,347 Chain (1); Coiled coil (1); Compositional bias (1); Modified residue (7); Motif (1); Region (4); Sequence conflict (2) FUNCTION: Component of the synaptonemal complexes (SCS), formed between homologous chromosomes during meiotic prophase (PubMed:11311943, PubMed:22761579). Required for centromere pairing during meiosis in male germ cells (PubMed:22761579). Required for normal meiosis during spermatogenesis and male fertility (PubMed:10678170). Plays a lesser role in female fertility (PubMed:10678170, PubMed:12004129). Required for efficient phosphorylation of HORMAD1 and HORMAD2 (PubMed:22346761). {ECO:0000269|PubMed:10678170, ECO:0000269|PubMed:11311943, ECO:0000269|PubMed:12004129, ECO:0000269|PubMed:22346761, ECO:0000269|PubMed:22761579}. PTM: Phosphorylated. {ECO:0000269|PubMed:22346761}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16717126}. Chromosome {ECO:0000269|PubMed:16717126, ECO:0000269|PubMed:22346761, ECO:0000269|PubMed:22761579, ECO:0000269|PubMed:24287868}. Chromosome, centromere {ECO:0000269|PubMed:22761579}. Note=It is present in early unpaired cores, in the lateral domains of the synaptonemal complex and in the chromosome cores when they separate at diplotene. It is found axial to the metaphase I chromosomes and in association with pairs of sister centromeres. The centromere-associated protein becomes dissociated from the centromeres at anaphase II and is not found in mitotic metaphase centromeres (By similarity). The phosphorylated form localizes preferentially to unsynapsed chromosomal regions (PubMed:22346761). {ECO:0000250|UniProtKB:Q60547, ECO:0000269|PubMed:22346761}. SUBUNIT: Component of the lateral elements of synaptonemal complexes (PubMed:16717126). Homotetramer; the tetrameric helix bundles assemble end to end into long homopolimeric fibers that exhibit a transversal striation with a periodicity of about 20 nm (in vitro) (By similarity). Interacts with SYCP2 (PubMed:16717126). {ECO:0000250|UniProtKB:Q8IZU3, ECO:0000269|PubMed:16717126}. DOMAIN: Composed of a long central coiled coil domain. The N-terminal and C-terminal regions interact with DNA. {ECO:0000250|UniProtKB:Q8IZU3}. TISSUE SPECIFICITY: Detected in oocytes (PubMed:16717126). Detected in spermatocytes and testis (at protein level) (PubMed:10678170, PubMed:16717126, PubMed:22761579). {ECO:0000269|PubMed:10678170, ECO:0000269|PubMed:16717126, ECO:0000269|PubMed:22761579, ECO:0000269|PubMed:24287868}. +Q61035 SYHC_MOUSE Histidine--tRNA ligase, cytoplasmic (EC 6.1.1.21) (Histidyl-tRNA synthetase) (HisRS) 509 57,432 Binding site (4); Chain (1); Domain (1); Initiator methionine (1); Modified residue (3); Region (2); Sequence conflict (2) FUNCTION: Cytoplasmic histidine--tRNA ligase. Plays a role in axon guidance. {ECO:0000250|UniProtKB:P12081}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P12081}. +Q8BIJ6 SYIM_MOUSE Isoleucine--tRNA ligase, mitochondrial (EC 6.1.1.5) (Isoleucyl-tRNA synthetase) (IleRS) 1012 112,804 Binding site (1); Chain (1); Modified residue (14); Motif (2); Sequence conflict (5); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. +Q9JLT4 TRXR2_MOUSE Thioredoxin reductase 2, mitochondrial (EC 1.8.1.9) (Thioredoxin reductase TR3) 524 56,603 Active site (1); Alternative sequence (4); Beta strand (22); Chain (1); Cross-link (1); Disulfide bond (1); Erroneous initiation (5); Helix (18); Modified residue (3); Non-standard residue (1); Nucleotide binding (1); Sequence conflict (1); Transit peptide (1); Turn (3) FUNCTION: Maintains thioredoxin in a reduced state. Implicated in the defenses against oxidative stress. May play a role in redox-regulated cell signaling.; FUNCTION: Involved in the control of reactive oxygen species levels and the regulation of mitochondrial redox homeostasis (By similarity). Maintains thioredoxin in a reduced state. May play a role in redox-regulated cell signaling (By similarity). {ECO:0000250|UniProtKB:Q9NNW7, ECO:0000250|UniProtKB:Q9Z0J5}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:10721726}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P38816}. TISSUE SPECIFICITY: Expressed in liver, heart, testis and kidney. {ECO:0000269|PubMed:10455115, ECO:0000269|PubMed:10500251, ECO:0000269|PubMed:10721726}. +Q99MD6 TRXR3_MOUSE Thioredoxin reductase 3 (EC 1.8.1.9) (Thioredoxin and glutathione reductase) (Thioredoxin reductase TR2) 652 71,319 Active site (1); Beta strand (4); Chain (1); Cross-link (1); Disulfide bond (1); Domain (1); Erroneous initiation (1); Erroneous termination (3); Frameshift (1); Helix (5); Modified residue (4); Mutagenesis (3); Non-standard residue (1); Nucleotide binding (1); Sequence caution (3); Sequence conflict (2); Turn (2) FUNCTION: Displays thioredoxin reductase, glutaredoxin and glutathione reductase activities. Catalyzes disulfide bond isomerization. Promotes disulfide bond formation between GPX4 and various sperm proteins and may play a role in sperm maturation by promoting formation of sperm structural components. {ECO:0000269|PubMed:11259642, ECO:0000269|PubMed:15901730}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11259642, ECO:0000269|PubMed:15901730}. Nucleus {ECO:0000269|PubMed:11259642, ECO:0000269|PubMed:15901730}. Microsome {ECO:0000269|PubMed:11259642, ECO:0000269|PubMed:15901730}. Endoplasmic reticulum. Note=Detected in cytoplasm and nucleus in late spermatids. {ECO:0000269|PubMed:11259642, ECO:0000269|PubMed:15901730}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O89049}. DOMAIN: The N-terminal glutaredoxin domain does not contain the C-X-X-C redox-active motif normally found in glutaredoxins but activity may be mediated through a single cysteine. The C-terminal Cys-Sec motif of one subunit of the homodimer may transfer electrons from the thiol-disulfide center to the glutaredoxin domain of the other subunit. {ECO:0000269|PubMed:11259642, ECO:0000269|PubMed:16262253}. TISSUE SPECIFICITY: Expressed preferentially in testis where it is found in spermatids and spermatocytes but not in sperm. In elongating spermatids, expressed at the site of mitochondrial sheath formation. Low levels in other tissues including heart, lung, liver, kidney, brain, muscle and prostate. {ECO:0000269|PubMed:10455115, ECO:0000269|PubMed:15901730, ECO:0000269|PubMed:20018845}. +Q99MN1 SYK_MOUSE Lysine--tRNA ligase (EC 2.7.7.-) (EC 6.1.1.6) (Lysyl-tRNA synthetase) (LysRS) 595 67,840 Binding site (6); Chain (1); Initiator methionine (1); Modified residue (9); Nucleotide binding (4) FUNCTION: Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA. When secreted, acts as a signaling molecule that induces immune response through the activation of monocyte/macrophages. Catalyzes the synthesis of the signaling molecule diadenosine tetraphosphate (Ap4A), and thereby mediates disruption of the complex between HINT1 and MITF and the concomitant activation of MITF transcriptional activity. {ECO:0000250|UniProtKB:Q15046}. PTM: Phosphorylated on a serine residue after mast cell stimulation with immunoglobulin E (IgE). {ECO:0000250|UniProtKB:Q5XIM7}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q15046}. Cytoplasm {ECO:0000250|UniProtKB:Q15046}. Nucleus {ECO:0000250|UniProtKB:Q15046}. Cell membrane {ECO:0000250|UniProtKB:Q15046}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q15046}. Secreted {ECO:0000250|UniProtKB:Q15046}. Note=Secretion is induced by TNF-alpha. Cytosolic in quiescent mast cells. Translocates into the nucleus in response to mast cell activation by immunoglobulin E. {ECO:0000250|UniProtKB:Q15046}. SUBUNIT: Homodimer (By similarity). Part of the multisynthetase complex (MSC), a multisubunit complex that groups tRNA ligases for Arg (RARS), Asp (DARS), Gln (QARS), Ile (IARS), Leu (LARS), Lys (KARS), Met (MARS) the bifunctional ligase for Glu and Pro (EPRS) and the auxiliary subunits AIMP1/p43, AIMP2/p38 and EEF1E1/p18 (PubMed:14975237). Interacts with AIMP2 (via N-terminus) and MITF (PubMed:14975237). Interacts with TARSL2 (By similarity). {ECO:0000250|UniProtKB:Q15046, ECO:0000269|PubMed:14975237}. DOMAIN: The N-terminal domain (1-65) is a functional tRNA-binding domain and is involved in the interaction with DARS, but has a repulsive role in the binding to EEF1A1. A central domain (208-259) is involved in homodimerization. The C-terminal domain (452-597) is not required for interaction with AIMP2 (By similarity). {ECO:0000250|UniProtKB:Q15046}. +Q3USQ7 SYN1L_MOUSE Synapse differentiation-inducing gene protein 1-like (Capucin) (Caudate and putamen-enriched protein) (Dispanin subfamily C member 1) (DSPC1) (Synapse differentiation-induced protein 2) (Transmembrane protein 90A) 237 25,524 Chain (1); Topological domain (3); Transmembrane (2) TRANSMEM 162 182 Helical. {ECO:0000255}.; TRANSMEM 205 225 Helical. {ECO:0000255}. TOPO_DOM 1 161 Extracellular. {ECO:0000255}.; TOPO_DOM 183 204 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 226 237 Extracellular. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Golgi apparatus, cis-Golgi network {ECO:0000269|PubMed:16359841}. TISSUE SPECIFICITY: Expression is restricted to the caudate-putamen. Down-regulated in R6/2 transgenic mice, a model for Huntington disease. {ECO:0000269|PubMed:16359841}. +Q6ZWR6 SYNE1_MOUSE Nesprin-1 (Enaptin) (KASH domain-containing protein 1) (KASH1) (Myocyte nuclear envelope protein 1) (Myne-1) (Nuclear envelope spectrin repeat protein 1) (Synaptic nuclear envelope protein 1) (Syne-1) 8799 1,009,926 Alternative sequence (8); Chain (1); Coiled coil (1); Compositional bias (1); Disulfide bond (2); Domain (3); Frameshift (1); Modified residue (12); Region (1); Repeat (74); Sequence conflict (6); Topological domain (2); Transmembrane (1) TRANSMEM 8749 8769 Helical; Anchor for type IV membrane protein. {ECO:0000255|PROSITE-ProRule:PRU00385}. TOPO_DOM 1 8748 Cytoplasmic. {ECO:0000255|PROSITE-ProRule:PRU00385}.; TOPO_DOM 8770 8799 Perinuclear space. {ECO:0000255|PROSITE-ProRule:PRU00385}. FUNCTION: Multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain the subcellular spatial organization. As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning. May be involved in nucleus-centrosome attachment. During interkinetic nuclear migration (INM) at G2 phase and nuclear migration in neural progenitors its LINC complex association with SUN1/2 and probably association with cytoplasmic dynein-dynactin motor complexes functions to pull the nucleus toward the centrosome; SYNE1 and SYNE2 seem to act redundantly in cerebellum, midbrain, brain stem, and other brain regions except cerebral cortex and hippocampus. Required for centrosome migration to the apical cell surface during early ciliogenesis. May be involved in nuclear remodeling during sperm head formation in spermatogenenis; a probable SUN3:SYNE1/KASH1 LINC complex may tether spermatid nuclei to posterior cytoskeletal structures such as the manchette. {ECO:0000250|UniProtKB:Q8NF91, ECO:0000269|PubMed:19596800, ECO:0000269|PubMed:19874786}. PTM: The disulfid bond with SUN1 or SUN2 is required for stability of the respective LINC complex under tensile forces. {ECO:0000250|UniProtKB:Q8WXH0}. SUBCELLULAR LOCATION: Nucleus outer membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Nucleus. Nucleus envelope. Cytoplasm, cytoskeleton. Cytoplasm, myofibril, sarcomere {ECO:0000250}. Note=The largest part of the protein is cytoplasmic, while its C-terminal part is associated with the nuclear envelope, most probably the outer nuclear membrane. In skeletal and smooth muscles, a significant amount is found in the sarcomeres (By similarity). {ECO:0000250}. SUBUNIT: Core component of LINC complexes which are composed of inner nuclear membrane SUN domain-containing proteins coupled to outer nuclear membrane KASH domain-containing nesprins. SUN and KASH domain-containing proteins seem to bind each other promiscuously; however, differentially expression of LINC complex constituents can give rise to specific assemblies. At least SUN1/2-containing core LINC complexes are proposed to be hexameric composed of three protomers of each KASH and SUN domain-containing protein. The SUN2:SYNE1/KASH1 LINC complex is a heterohexamer; the homotrimeric cloverleave-like conformation of the SUN domain is a prerequisite for LINC complex formation in which three separate SYNE1/KASH1 peptides bind at the interface of adjacent SUN domains. Self-associates. Interacts with SYNE3. Interacts with SUN3; proposed to form a spermatogenesis-specific LINC complex with SUN3 during sperm head formation. May interact with MUSK. Interacts with SPAG4/SUN4. Interacts with EMD and LMNA in vitro. Interacts with F-actin via its N-terminal domain. Interacts with DCTN1 and DYNC1I1/2; suggesting the association with the dynein-dynactin motor complex. {ECO:0000250|UniProtKB:Q8NF91, ECO:0000269|PubMed:10878022, ECO:0000269|PubMed:19874786, ECO:0000269|PubMed:22518138, ECO:0000269|PubMed:26621829}. DOMAIN: The KASH domain, which contains a transmembrane domain, mediates the nuclear envelope targeting and is involved in the binding to SUN1 and SUN2 through recognition of their SUN domains. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in C2F3 and CH310T1/2 cells, brain and skeletal muscle (at protein level). {ECO:0000269|PubMed:15093733, ECO:0000269|PubMed:22518138}. +Q61037 TSC2_MOUSE Tuberin (Tuberous sclerosis 2 protein homolog) 1814 202,071 Alternative sequence (8); Chain (1); Domain (1); Modified residue (21); Sequence conflict (17) FUNCTION: In complex with TSC1, this tumor suppressor inhibits the nutrient-mediated or growth factor-stimulated phosphorylation of S6K1 and EIF4EBP1 by negatively regulating mTORC1 signaling (By similarity). Acts as a GTPase-activating protein (GAP) for the small GTPase RHEB, a direct activator of the protein kinase activity of mTORC1 (By similarity). May also play a role in microtubule-mediated protein transport (PubMed:16707451). Also stimulates the intrinsic GTPase activity of the Ras-related proteins RAP1A and RAB5 (By similarity). {ECO:0000250|UniProtKB:P49815, ECO:0000250|UniProtKB:P49816, ECO:0000269|PubMed:16707451}. PTM: Phosphorylation at Ser-1388, Ser-1419 or Ser-1421 does not affect interaction with TSC1. Phosphorylation at Ser-939 and Thr-1465 by PKB/AKT1 is induced by growth factor stimulation. Phosphorylation by AMPK activates it and leads to negatively regulates the mTORC1 complex. Phosphorylated at Ser-1805 by RPS6KA1; phosphorylation inhibits TSC2 ability to suppress mTORC1 signaling. Phosphorylated by DAPK1. {ECO:0000250|UniProtKB:P49815}.; PTM: Ubiquitinated by the DCX(FBXW5) E3 ubiquitin-protein ligase complex, leading to its subsequent degradation. Ubiquitinated by MYCBP2 independently of its phosphorylation status leading to subsequent degradation; association with TSC1 protects from ubiquitination. {ECO:0000250|UniProtKB:P49815}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=At steady state found in association with membranes. {ECO:0000250}. SUBUNIT: Probably forms a complex composed of chaperones HSP90 and HSP70, co-chaperones STIP1/HOP, CDC37, PPP5C, PTGES3/p23, TSC1 and client protein TSC2. Probably forms a complex composed of chaperones HSP90 and HSP70, co-chaperones CDC37, PPP5C, TSC1 and client protein TSC2, CDK4, AKT, RAF1 and NR3C1; this complex does not contain co-chaperones STIP1/HOP and PTGES3/p23. Forms a complex containing HSP90AA1, TSC1 and TSC2; TSC1 is required to recruit TCS2 to the complex thereby stabilizing TSC2. Interacts with TSC1 and HERC1; the interaction with TSC1 stabilizes TSC2 and prevents the interaction with HERC1. May also interact with the adapter molecule RABEP1. The final complex may contain TSC2 and RABEP1 linked to RAB5. Interacts with HSPA1 and HSPA8. Interacts with DAPK1. Interacts with FBXW5. Interacts with NAA10 (via C-terminal domain). Interacts with RRAGA (polyubiquitinated). Interacts with WDR45B (By similarity). {ECO:0000250|UniProtKB:P49815}. TISSUE SPECIFICITY: Widely expressed. +Q8CII8 SYNE4_MOUSE Nesprin-4 (KASH domain-containing protein 4) (KASH4) (Nuclear envelope spectrin repeat protein 4) 388 42,024 Chain (1); Disulfide bond (2); Domain (1); Sequence conflict (3); Topological domain (2); Transmembrane (1) TRANSMEM 340 360 Helical; Anchor for type IV membrane protein. {ECO:0000255|PROSITE-ProRule:PRU00385}. TOPO_DOM 1 339 Cytoplasmic. {ECO:0000255|PROSITE-ProRule:PRU00385}.; TOPO_DOM 361 388 Perinuclear space. {ECO:0000255|PROSITE-ProRule:PRU00385}. FUNCTION: As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning (By similarity). Behaves as a kinesin cargo, providing a functional binding site for kinesin-1 at the nuclear envelope. Hence may contribute to the establishment of secretory epithelial morphology, by promoting kinesin-dependent apical migration of the centrosome and Golgi apparatus and basal localization of the nucleus. {ECO:0000250, ECO:0000269|PubMed:19164528}. PTM: The disulfid bond with SUN1 or SUN2 is required for stability of the respective LINC complex under tensile forces. {ECO:0000250|UniProtKB:Q8WXH0}. SUBCELLULAR LOCATION: Nucleus outer membrane {ECO:0000269|PubMed:19164528, ECO:0000269|PubMed:23348741}; Single-pass type IV membrane protein {ECO:0000269|PubMed:19164528, ECO:0000269|PubMed:23348741}. Note=Localization at the nucleus outer membrane location requires the presence of SUN1. SUBUNIT: Core component of LINC complexes which are composed of inner nuclear membrane SUN domain-containing proteins coupled to outer nuclear membrane KASH domain-containing nesprins. SUN and KASH domain-containing proteins seem to bind each other promiscuously; however, differentially expression of LINC complex constituents can give rise to specific assemblies. Probably part of a SUN1-containing LINC complex. Interacts with kinesins KIF5B and KLC1. {ECO:0000250, ECO:0000269|PubMed:19164528}. DOMAIN: The KASH domain, which contains a transmembrane domain, mediates the nuclear envelope targeting and is involved in the binding to SUN1 and SUN2 through recognition of their SUN domains. {ECO:0000269|PubMed:19164528}. TISSUE SPECIFICITY: Expressed in secretory epithelial cells, such as those found in exocrine pancreas, bulbourethral gland, mammary gland and salivary gland (at protein level). Also expressed in the cochlea, where it is restricted primarily to the 3 rows of outer hair cells and 1 row of inner hair cells (at protein level). Not detected in other cells of the cochlea, including Deiter's cells and pillar cells, nor in liver and kidney (at protein level). {ECO:0000269|PubMed:19164528, ECO:0000269|PubMed:23348741}. +Q8CC35 SYNPO_MOUSE Synaptopodin 929 99,552 Alternative sequence (2); Chain (1); Compositional bias (1); Erroneous initiation (2); Modified residue (28); Motif (2); Sequence conflict (1) FUNCTION: Actin-associated protein that may play a role in modulating actin-based shape and motility of dendritic spines and renal podocyte foot processes. Seems to be essential for the formation of spine apparatuses in spines of telencephalic neurons, which is involved in synaptic plasticity. {ECO:0000269|PubMed:12928494}. PTM: O-glycosylated. {ECO:0000269|PubMed:16452088}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9314539}. Cell junction, tight junction {ECO:0000269|PubMed:9314539}. Perikaryon {ECO:0000269|PubMed:9314539}. Cell projection, dendritic spine {ECO:0000269|PubMed:12928494, ECO:0000269|PubMed:9314539}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000269|PubMed:9314539}. Cell junction, synapse {ECO:0000269|PubMed:9314539}. Note=Localized at the tight junction of cells. In brain, localized to the postsynaptic densities and in the perikarya. Associated with dendritic spines of a subset of synapses (PubMed:9314539). {ECO:0000269|PubMed:9314539}. SUBUNIT: Interacts with BAIAP1. Interacts with actin. Interacts (via PPxY motifs) with WWC1 (via WW domains) (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain, namely in the olfactory bulb, cerebral cortex, striatum, and hippocampus, but not in the cerebellum. Also expressed in the podocytes of kidney glomeruli. In the hippocampus, mainly expressed in the principal cell layer of the dentate gyrus and Ammon's horn. {ECO:0000269|PubMed:12357430, ECO:0000269|PubMed:12928494, ECO:0000269|PubMed:9314539}. +Q5SV85 SYNRG_MOUSE Synergin gamma (AP1 subunit gamma-binding protein 1) (Gamma-synergin) 1306 139,616 Alternative sequence (4); Chain (1); Coiled coil (1); Domain (1); Erroneous gene model prediction (1); Modified residue (20); Motif (3); Region (1) FUNCTION: May play a role in endocytosis and/or membrane trafficking at the trans-Golgi network (TGN). May act by linking the adapter protein complex AP-1 to other proteins (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12808037}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:12808037}; Peripheral membrane protein {ECO:0000269|PubMed:12808037}. Note=Associated with membranes of the TGN, colocalizes with AP1G1 (By similarity). Associates with membranes via the adapter protein complex AP-1. {ECO:0000250}. SUBUNIT: Interacts with SCAMP1 via its EH-domain. Interacts with GGA1, GGA2 and GGA3. Interacts with the AP1G1 and AP1G2 subunits of the adapter protein complexes AP-1 (By similarity). {ECO:0000250}. DOMAIN: The DFXDF motifs mediate the interaction with gamma-appendage subunits AP1G1 and AP1G2. {ECO:0000250}. +Q9DA17 TSG13_MOUSE Testis-specific gene 13 protein 273 32,067 Chain (1) +O08859 TSG6_MOUSE Tumor necrosis factor-inducible gene 6 protein (TNF-stimulated gene 6 protein) (TSG-6) (Tumor necrosis factor alpha-induced protein 6) (TNF alpha-induced protein 6) 275 30,924 Chain (1); Disulfide bond (4); Domain (2); Glycosylation (2); Signal peptide (1) FUNCTION: Possibly involved in cell-cell and cell-matrix interactions during inflammation and tumorigenesis. {ECO:0000250}. SUBUNIT: Interacts with inter-alpha-inhibitor (I-alpha-I). Chondroitin sulfate may be required for the stability of the complex (By similarity). {ECO:0000250}. +Q9JJL0 TSGA8_MOUSE Testis-specific gene A8 protein (Haploid-specific alanine-rich acidic protein located on chromosome X) (Halap-x) 238 22,769 Chain (1); Compositional bias (1); Erroneous initiation (1); Region (2); Repeat (8) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10993819}. Nucleus, nucleoplasm {ECO:0000269|PubMed:10993819}. Note=Strongly expressed in the nucleus of round spermatids. As spermatids mature, nuclear expression declines and cytoplasmic expression increases. Elongating spermatids have mainly cytoplasmic expression. {ECO:0000269|PubMed:10993819}. TISSUE SPECIFICITY: Specifically expressed in testis (at protein level). {ECO:0000269|PubMed:10993819}. +Q5DTH5 TSH1_MOUSE Teashirt homolog 1 (Serologically defined colon cancer antigen 3 homolog) 1084 118,567 Chain (1); Compositional bias (1); DNA binding (1); Erroneous initiation (2); Frameshift (1); Modified residue (1); Sequence conflict (3); Zinc finger (5) FUNCTION: Probable transcriptional regulator involved in developmental processes. May act as a transcriptional repressor (Potential). {ECO:0000305}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Interacts (via homeobox domain) with APBB1 (via PID domain 1). {ECO:0000269|PubMed:19343227}. +Q68FE9 TSH2_MOUSE Teashirt homolog 2 (SDCCAG33-like protein) (Zinc finger protein 218) 1030 114,223 Chain (1); Coiled coil (1); Cross-link (12); DNA binding (1); Erroneous initiation (2); Modified residue (1); Sequence conflict (3); Zinc finger (5) FUNCTION: Probable transcriptional regulator involved in developmental processes. May act as a transcriptional repressor (Potential). {ECO:0000305}. PTM: Sumoylated. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Interacts (via homeobox domain) with APBB1 (via PID domain 1). {ECO:0000269|PubMed:19343227}. +Q8CGV9 TSH3_MOUSE Teashirt homolog 3 (Zinc finger protein 537) 1081 118,626 Chain (1); Coiled coil (1); Compositional bias (2); DNA binding (1); Frameshift (1); Modified residue (1); Sequence conflict (2); Zinc finger (5) FUNCTION: Transcriptional regulator involved in developmental processes. Function in association with APBB1, SET and HDAC factors as a transcriptional repressor, that inhibits the expression of CASP4. TSHZ3-mediated transcription repression involves the recruitment of histone deacetylases HDAC1 and HDAC2. Associates with chromatin in a region surrounding the CASP4 transcriptional start site(s). Regulates the development of neurons involved in both respiratory rhythm and airflow control. Promotes maintenance of nucleus ambiguus (nA) motoneurons, which govern upper airway function, and establishes a respiratory rhythm generator (RRG) activity compatible with survival at birth. Involved in the differentiation of the proximal uretic smooth muscle cells during developmental processes. Involved in the up-regulation of myocardin, that directs the expression of smooth muscle cells in the proximal ureter. Involved in the modulation of glutamatergic synaptic transmission and long-term synaptic potentiation (PubMed:27668656). {ECO:0000269|PubMed:18776146, ECO:0000269|PubMed:19745106, ECO:0000269|PubMed:20631175, ECO:0000269|PubMed:27668656}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. Cell projection, growth cone {ECO:0000250}. Note=Colocalizes with APBB1 in the nucleus. Colocalizes with APBB1 in axonal growth cone (By similarity). {ECO:0000250}. SUBUNIT: Interacts (via N-terminus) with HDAC1 and HDAC2; the interaction is direct. Found in a trimeric complex with APBB1 and HDAC1; the interaction between HDAC1 and APBB1 is mediated by TSHZ3 (By similarity). Interacts (via homeobox domain) with APBB1 (via PID domain 1). {ECO:0000250, ECO:0000269|PubMed:19343227}. TISSUE SPECIFICITY: Expressed in corticostriatal neurons. {ECO:0000269|PubMed:27668656}. +P12656 TSHB_MOUSE Thyrotropin subunit beta (Thyroid-stimulating hormone subunit beta) (TSH-B) (TSH-beta) (Thyrotropin beta chain) 138 15,373 Chain (1); Disulfide bond (6); Glycosylation (1); Propeptide (1); Signal peptide (1) FUNCTION: Indispensable for the control of thyroid structure and metabolism. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Heterodimer of a common alpha chain and a unique beta chain which confers biological specificity to thyrotropin, lutropin, follitropin and gonadotropin. +P47750 TSHR_MOUSE Thyrotropin receptor (Thyroid-stimulating hormone receptor) (TSH-R) 764 86,583 Chain (1); Disulfide bond (2); Glycosylation (5); Modified residue (1); Motif (1); Natural variant (1); Repeat (7); Sequence conflict (1); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 414 441 Helical; Name=1. {ECO:0000255}.; TRANSMEM 451 473 Helical; Name=2. {ECO:0000255}.; TRANSMEM 495 517 Helical; Name=3. {ECO:0000255}.; TRANSMEM 538 560 Helical; Name=4. {ECO:0000255}.; TRANSMEM 581 602 Helical; Name=5. {ECO:0000255}.; TRANSMEM 626 649 Helical; Name=6. {ECO:0000255}.; TRANSMEM 661 682 Helical; Name=7. {ECO:0000255}. TOPO_DOM 22 413 Extracellular. {ECO:0000255}.; TOPO_DOM 442 450 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 474 494 Extracellular. {ECO:0000255}.; TOPO_DOM 518 537 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 561 580 Extracellular. {ECO:0000255}.; TOPO_DOM 603 625 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 650 660 Extracellular. {ECO:0000255}.; TOPO_DOM 683 764 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for the thyroid-stimulating hormone (TSH) or thyrotropin. Also acts as a receptor for the heterodimeric glycoprotein hormone (GPHA2:GPHB5) or thyrostimulin. The activity of this receptor is mediated by G proteins which activate adenylate cyclase. Plays a central role in controlling thyroid cell metabolism. {ECO:0000250|UniProtKB:P16473, ECO:0000250|UniProtKB:P21463}. PTM: Glycosylated. {ECO:0000250|UniProtKB:P16473}.; PTM: Sulfated. Sulfation on Tyr-385 plays a role in thyrotropin receptor binding and activation. {ECO:0000250|UniProtKB:P16473}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P16473}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P16473}. Basolateral cell membrane {ECO:0000250|UniProtKB:P16473}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P16473}. SUBUNIT: Interacts with heterodimer GPHA2:GPHB5; this interaction stimulates cAMP production. Interacts (via the PDZ-binding motif) with SCRIB; regulates TSHR trafficking and function. {ECO:0000250|UniProtKB:P16473}. DISEASE: Note=Defects in Tshr are the cause of hyt/hyt hypothyroidism, an autosomal recessive, fetal-onset, severe hypothyroidism related to TSH hyporesponsiveness and associated with elevated TSH. {ECO:0000305|PubMed:8170469}. +Q9D1D1 TSN11_MOUSE Tetraspanin-11 (Tspan-11) 253 28,072 Chain (1); Glycosylation (1); Transmembrane (4) TRANSMEM 19 39 Helical. {ECO:0000255}.; TRANSMEM 63 83 Helical. {ECO:0000255}.; TRANSMEM 93 113 Helical. {ECO:0000255}.; TRANSMEM 220 240 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8QZY6 TSN14_MOUSE Tetraspanin-14 (Tspan-14) (Transmembrane 4 superfamily member 14) 270 30,674 Chain (1); Glycosylation (1); Region (1); Topological domain (5); Transmembrane (4) TRANSMEM 18 38 Helical. {ECO:0000255}.; TRANSMEM 62 82 Helical. {ECO:0000255}.; TRANSMEM 93 113 Helical. {ECO:0000255}.; TRANSMEM 233 253 Helical. {ECO:0000255}. TOPO_DOM 1 17 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 39 61 Extracellular. {ECO:0000305}.; TOPO_DOM 83 92 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 114 232 Extracellular. {ECO:0000305}.; TOPO_DOM 254 270 Cytoplasmic. {ECO:0000305}. FUNCTION: Regulates maturation and trafficking of the transmembrane metalloprotease ADAM10 (PubMed:26668317, PubMed:23035126). Negatively regulates ADAM10-mediated cleavage of GP6 (PubMed:26668317). Promotes ADAM10-mediated cleavage of CDH5 (PubMed:23035126). {ECO:0000269|PubMed:23035126, ECO:0000269|PubMed:26668317}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8NG11}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Interacts with ADAM10; the interaction promotes ADAM10 maturation and cell surface expression. {ECO:0000269|PubMed:23035126, ECO:0000269|PubMed:26668317}. +Q9D7W4 TSN17_MOUSE Tetraspanin-17 (Tspan-17) (F-box only protein 23) (Tetraspan protein SB134) (Transmembrane 4 superfamily member 17) 270 30,126 Chain (1); Glycosylation (2); Sequence conflict (1); Topological domain (5); Transmembrane (4) TRANSMEM 20 40 Helical. {ECO:0000255}.; TRANSMEM 64 84 Helical. {ECO:0000255}.; TRANSMEM 95 115 Helical. {ECO:0000255}.; TRANSMEM 235 255 Helical. {ECO:0000255}. TOPO_DOM 1 19 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 41 63 Extracellular. {ECO:0000255}.; TOPO_DOM 85 94 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 116 234 Extracellular. {ECO:0000255}.; TOPO_DOM 256 270 Cytoplasmic. {ECO:0000255}. FUNCTION: Regulates ADAM10 maturation. {ECO:0000269|PubMed:23035126}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Interacts with ADAM10. {ECO:0000269|PubMed:23035126, ECO:0000269|PubMed:26668317}. +Q80WR1 TSN18_MOUSE Tetraspanin-18 (Tspan-18) 248 27,801 Chain (1); Glycosylation (1); Topological domain (5); Transmembrane (4) TRANSMEM 14 34 Helical. {ECO:0000255}.; TRANSMEM 50 70 Helical. {ECO:0000255}.; TRANSMEM 84 104 Helical. {ECO:0000255}.; TRANSMEM 224 244 Helical. {ECO:0000255}. TOPO_DOM 1 13 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 35 49 Extracellular. {ECO:0000255}.; TOPO_DOM 71 83 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 105 223 Extracellular. {ECO:0000255}.; TOPO_DOM 245 248 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q99J59 TSN1_MOUSE Tetraspanin-1 (Tspan-1) 240 26,356 Chain (1); Erroneous gene model prediction (2); Glycosylation (1); Transmembrane (4) TRANSMEM 12 32 Helical. {ECO:0000255}.; TRANSMEM 53 73 Helical. {ECO:0000255}.; TRANSMEM 89 109 Helical. {ECO:0000255}.; TRANSMEM 211 231 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q922J6 TSN2_MOUSE Tetraspanin-2 (Tspan-2) 221 24,181 Chain (1); Glycosylation (1); Sequence conflict (1); Topological domain (5); Transmembrane (4) TRANSMEM 14 34 Helical. {ECO:0000255}.; TRANSMEM 55 75 Helical. {ECO:0000255}.; TRANSMEM 91 111 Helical. {ECO:0000255}.; TRANSMEM 189 209 Helical. {ECO:0000255}. TOPO_DOM 1 13 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 35 54 Extracellular. {ECO:0000255}.; TOPO_DOM 76 90 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 112 188 Extracellular. {ECO:0000255}.; TOPO_DOM 210 221 Cytoplasmic. {ECO:0000255}. FUNCTION: May play a role in signalling in oligodendrocytes in the early stages of their terminal differentiation into myelin-forming glia and may also function in stabilizing the mature sheath. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9CQ88 TSN31_MOUSE Tetraspanin-31 (Tspan-31) (Sarcoma-amplified sequence homolog) 210 22,694 Chain (1); Glycosylation (3); Topological domain (5); Transmembrane (4) TRANSMEM 13 33 Helical. {ECO:0000255}.; TRANSMEM 45 65 Helical. {ECO:0000255}.; TRANSMEM 73 93 Helical. {ECO:0000255}.; TRANSMEM 174 194 Helical. {ECO:0000255}. TOPO_DOM 1 12 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 34 44 Extracellular. {ECO:0000255}.; TOPO_DOM 66 72 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 94 173 Extracellular. {ECO:0000255}.; TOPO_DOM 195 210 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q8R3S2 TSN33_MOUSE Tetraspanin-33 (Tspan-33) (Penumbra) (mPen) (Proerythroblast new membrane) 283 31,550 Alternative sequence (1); Chain (1); Glycosylation (1); Topological domain (5); Transmembrane (4) TRANSMEM 25 45 Helical. {ECO:0000255}.; TRANSMEM 65 85 Helical. {ECO:0000255}.; TRANSMEM 97 117 Helical. {ECO:0000255}.; TRANSMEM 236 256 Helical. {ECO:0000255}. TOPO_DOM 1 24 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 46 64 Extracellular. {ECO:0000255}.; TOPO_DOM 86 96 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 118 235 Extracellular. {ECO:0000255}.; TOPO_DOM 257 283 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays an important role in normal erythropoiesis (PubMed:17158226). It has a role in the differentiation of erythroid progenitors (PubMed:17158226). Regulates maturation and trafficking of the transmembrane metalloprotease ADAM10 (PubMed:23035126). Negatively regulates ligand-induced Notch activity probably by regulating ADAM10 activity (By similarity). {ECO:0000250|UniProtKB:Q86UF1, ECO:0000269|PubMed:17158226, ECO:0000269|PubMed:23035126}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q86UF1}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Homodimer; disulfide-linked (PubMed:17158226). Interacts with ADAM10 (PubMed:26668317, PubMed:23035126). {ECO:0000269|PubMed:17158226, ECO:0000269|PubMed:23035126, ECO:0000269|PubMed:26668317}. TISSUE SPECIFICITY: Predominantly expressed in erythroblasts. {ECO:0000269|PubMed:17158226, ECO:0000269|PubMed:23035126}. +O70401 TSN6_MOUSE Tetraspanin-6 (Tspan-6) (Transmembrane 4 superfamily member 6) 245 27,333 Chain (1); Glycosylation (1); Topological domain (5); Transmembrane (4) TRANSMEM 20 40 Helical. {ECO:0000255}.; TRANSMEM 60 80 Helical. {ECO:0000255}.; TRANSMEM 94 114 Helical. {ECO:0000255}.; TRANSMEM 209 229 Helical. {ECO:0000255}. TOPO_DOM 1 19 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 41 59 Extracellular. {ECO:0000255}.; TOPO_DOM 81 93 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 115 208 Extracellular. {ECO:0000255}.; TOPO_DOM 230 245 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. +P35441 TSP1_MOUSE Thrombospondin-1 (Glycoprotein G) 1170 129,647 Chain (1); Disulfide bond (30); Domain (8); Glycosylation (4); Motif (1); Region (1); Repeat (8); Sequence conflict (1); Signal peptide (1) FUNCTION: Adhesive glycoprotein that mediates cell-to-cell and cell-to-matrix interactions. Binds heparin. May play a role in dentinogenesis and/or maintenance of dentin and dental pulp. Ligand for CD36 mediating antiangiogenic properties (By similarity). Plays a role in ER stress response, via its interaction with the activating transcription factor 6 alpha (ATF6) which produces adaptive ER stress response factors. {ECO:0000250, ECO:0000269|PubMed:22682248}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P07996}. Cell surface {ECO:0000250|UniProtKB:P07996}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P07996}. Endoplasmic reticulum {ECO:0000269|PubMed:22682248}. Sarcoplasmic reticulum {ECO:0000269|PubMed:22682248}. Note=Secreted by thrombin-activated platelets and binds to the cell surface in the presence of extracellular Ca(2+) (By similarity). Incorporated into the extracellular matrix of fibroblasts (By similarity). Also detected in the endoplasmic reticulum and sarcoplasmic reticulum where it plays a role in the ER stress response (PubMed:22682248). {ECO:0000250|UniProtKB:P07996, ECO:0000269|PubMed:22682248}. SUBUNIT: Homotrimer; disulfide-linked (By similarity). Can bind to fibrinogen, fibronectin, laminin, type V collagen and integrins alpha-V/beta-1, alpha-V/beta-3 and alpha-IIb/beta-3. Binds heparin. Interacts (via the TSP type I repeats) with CD36; the interaction conveys an antiangiogenic effect. Interacts (via the TSP type I repeats) with HRG; the interaction blocks the antiangiogenic effect of THBS1 with CD36 (By similarity). Interacts with ATF6 (via lumenal domain). {ECO:0000250, ECO:0000269|PubMed:22682248}. +Q03350 TSP2_MOUSE Thrombospondin-2 1172 129,882 Chain (1); Disulfide bond (29); Domain (8); Glycosylation (7); Motif (1); Region (1); Repeat (8); Sequence conflict (2); Signal peptide (1) FUNCTION: Adhesive glycoprotein that mediates cell-to-cell and cell-to-matrix interactions. Ligand for CD36 mediating antiangiogenic properties. {ECO:0000269|PubMed:15748999}. SUBUNIT: Homotrimer; disulfide-linked. Can bind to fibrinogen, fibronectin, laminin and type V collagen (By similarity). Interacts (via the TSP type I repeats) with CD36; the interaction conveys an antiangiogenic effect. Interacts (via the TSP type I repeats) with HRG; the interaction blocks the antiangiogenic effect of THBS2 with CD36. Can bind to fibrinogen, fibronectin, laminin. {ECO:0000250, ECO:0000269|PubMed:15748999}. +Q05895 TSP3_MOUSE Thrombospondin-3 956 104,119 Chain (1); Disulfide bond (23); Domain (5); Glycosylation (4); Repeat (8); Sequence conflict (7); Signal peptide (1) FUNCTION: Adhesive glycoprotein that mediates cell-to-cell and cell-to-matrix interactions. Can bind to fibrinogen, fibronectin, laminin and type V collagen. SUBUNIT: Oligomer; disulfide-linked. TISSUE SPECIFICITY: Brain, lung and cartilage. +Q9Z1T2 TSP4_MOUSE Thrombospondin-4 963 106,366 Chain (1); Disulfide bond (23); Domain (6); Glycosylation (3); Motif (2); Repeat (8); Sequence conflict (2); Signal peptide (1) FUNCTION: Adhesive glycoprotein that mediates cell-to-cell and cell-to-matrix interactions and is involved in various processes including cellular proliferation, migration, adhesion and attachment, inflammatory response to CNS injury, regulation of vascular inflammation and adaptive responses of the heart to pressure overload and in myocardial function and remodeling. Binds to structural extracellular matrix (ECM) proteins and modulates the ECM in response to tissue damage, contributing to cardioprotective and adaptive ECM remodeling. Plays a role in ER stress response, via its interaction with the activating transcription factor 6 alpha (ATF6) which produces adaptive ER stress response factors and protects myocardium from pressure overload. May contribute to spinal presynaptic hypersensitivity and neuropathic pain states after peripheral nerve injury. May play a role in regulating protective astrogenesis from the subventricular zone (SVZ) niche after injury in a NOTCH1-dependent manner. {ECO:0000269|PubMed:20884877, ECO:0000269|PubMed:22034490, ECO:0000269|PubMed:22362893, ECO:0000269|PubMed:22682248, ECO:0000269|PubMed:22745497, ECO:0000269|PubMed:23615612}. SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:22682248}. Sarcoplasmic reticulum {ECO:0000269|PubMed:22682248}. Secreted {ECO:0000269|PubMed:22682248}. Secreted, extracellular space {ECO:0000269|PubMed:22682248}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:22362893, ECO:0000269|PubMed:22682248}. SUBUNIT: Homopentamer; disulfide-linked. Interacts with PTBP3 (By similarity). Interacts (via EGF-like 3; calcium-binding domain) with ATF6 and facilitates its processing, activation and nuclear translocation. Interacts with NOTCH1. {ECO:0000250, ECO:0000269|PubMed:22682248, ECO:0000269|PubMed:23615612}. TISSUE SPECIFICITY: Heart. Up-regulated in the heart in response to ischemic injury and pathology (at protein level). Astrocytes; expressed at high levels in subventricular zone (SVZ)-derived astrocytes and at low levels in cortical astrocytes. In response to peripheral nerve injury, significantly up-regulated in the dorsal spinal cord (at protein level). {ECO:0000269|PubMed:22362893, ECO:0000269|PubMed:22745497, ECO:0000269|PubMed:23615612}. +P50637 TSPO_MOUSE Translocator protein (Mitochondrial benzodiazepine receptor) (PKBS) (Peripheral-type benzodiazepine receptor) (PBR) 169 18,841 Beta strand (1); Chain (1); Helix (12); Mutagenesis (3); Sequence conflict (4); Topological domain (6); Transmembrane (5); Turn (2) TRANSMEM 6 26 Helical; Name=1.; TRANSMEM 47 67 Helical; Name=2.; TRANSMEM 80 100 Helical; Name=3.; TRANSMEM 106 126 Helical; Name=4.; TRANSMEM 135 155 Helical; Name=5. TOPO_DOM 1 5 Mitochondrial intermembrane. {ECO:0000269|PubMed:24653034}.; TOPO_DOM 27 46 Cytoplasmic. {ECO:0000269|PubMed:24653034}.; TOPO_DOM 68 79 Mitochondrial intermembrane. {ECO:0000269|PubMed:24653034}.; TOPO_DOM 101 105 Cytoplasmic. {ECO:0000269|PubMed:24653034}.; TOPO_DOM 127 134 Mitochondrial intermembrane. {ECO:0000269|PubMed:24653034}.; TOPO_DOM 156 169 Cytoplasmic. {ECO:0000269|PubMed:24653034}. FUNCTION: Can bind protoporphyrin IX and may play a role in the transport of porphyrins and heme (By similarity). Was initially identified as peripheral-type benzodiazepine receptor; can also bind isoquinoline carboxamides. Promotes the transport of cholesterol across mitochondrial membranes and may play a role in lipid metabolism (PubMed:9832438, PubMed:24814875), but its precise physiological role is controversial. According to some reports, it is not required for steroid hormone biosynthesis (PubMed:24174323, PubMed:24936060). {ECO:0000250, ECO:0000269|PubMed:24174323, ECO:0000269|PubMed:24814875, ECO:0000269|PubMed:24936060, ECO:0000269|PubMed:8114671, ECO:0000269|PubMed:9832438}. SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Membrane; Multi-pass membrane protein. SUBUNIT: Interacts with TSPOAP1. Interacts with MOST-1. May interact with STAR. {ECO:0000250}. TISSUE SPECIFICITY: Detected in liver (at protein level). Ubiquitous. {ECO:0000269|PubMed:24174323, ECO:0000269|PubMed:24936060}. +P13438 TSP_MOUSE Trophoblast-specific protein alpha 124 13,948 Chain (1); Signal peptide (1) FUNCTION: It may be a growth factor/hormone, perhaps involved in interaction between the maternal and fetal systems in maintenance of pregnancy. SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000305}. +Q5HZH2 TSR3_MOUSE Ribosome biogenesis protein TSR3 homolog 323 35,334 Chain (1); Modified residue (1); Sequence conflict (1) FUNCTION: Probable pre-rRNA processing protein involved in ribosome biogenesis. {ECO:0000255|HAMAP-Rule:MF_03146}. +Q9JHE7 TSSC4_MOUSE Protein TSSC4 317 33,569 Alternative sequence (2); Chain (1); Modified residue (6) TISSUE SPECIFICITY: Expressed in placenta. Widely expressed in embryo and newborn. {ECO:0000269|PubMed:10915772}. +Q61241 TSSK1_MOUSE Testis-specific serine/threonine-protein kinase 1 (TSK-1) (TSK1) (TSSK-1) (Testis-specific kinase 1) (EC 2.7.11.1) (Serine/threonine-protein kinase 22A) 365 41,589 Active site (1); Binding site (1); Chain (1); Domain (1); Modified residue (1); Nucleotide binding (1); Sequence conflict (3) FUNCTION: Testis-specific serine/threonine-protein kinase required during spermatid development (PubMed:20053632, PubMed:23599433). Phosphorylates 'Ser-281' of TSKS (PubMed:20053632). Involved in the late stages of spermatogenesis, during the reconstruction of the cytoplasm (PubMed:20053632). During spermatogenesis, required for the transformation of a ring-shaped structure around the base of the flagellum originating from the chromatoid body (PubMed:20053632). {ECO:0000269|PubMed:20053632, ECO:0000269|PubMed:23599433}. PTM: Autophosphorylated. {ECO:0000250|UniProtKB:Q9BXA7}.; PTM: Ubiquitinated; HSP90 activity negatively regulates ubiquitination and degradation. {ECO:0000269|PubMed:23599433}. SUBCELLULAR LOCATION: Cytoplasm. Cytoplasmic vesicle, secretory vesicle, acrosome. Cell projection, cilium, flagellum. Note=In spermatozoa, present in the sperm head and in the flagellum. SUBUNIT: Interacts with TSSK2 (PubMed:10781952). Interacts with HSP90; this interaction stabilizes TSSK1 (PubMed:23599433). {ECO:0000269|PubMed:10781952, ECO:0000269|PubMed:23599433}. TISSUE SPECIFICITY: Testis-specific. Expressed only in postmeiotic spermatids at the final stages of cytodifferentiation in the seminiferous tubules (at protein level). Not detected in released sperms in the lumen of the seminiferous tubules and the epididymis. {ECO:0000269|PubMed:20729278, ECO:0000269|PubMed:9412477, ECO:0000269|PubMed:9651519}. +Q925K9 TSSK6_MOUSE Testis-specific serine/threonine-protein kinase 6 (TSK-6) (TSSK-6) (Testis-specific kinase 6) (EC 2.7.11.1) (Serine/threonine-protein kinase SSTK) (Small serine/threonine kinase) 273 30,287 Active site (1); Binding site (1); Chain (1); Domain (1); Nucleotide binding (1); Sequence conflict (1) FUNCTION: Required for sperm production and function. Plays a role in DNA condensation during postmeiotic chromatin remodeling. {ECO:0000269|PubMed:15870294}. PTM: Autophosphorylated. {ECO:0000250|UniProtKB:Q9BXA6}.; PTM: Ubiquitinated; HSP90 activity negatively regulates ubiquitination and degradation. {ECO:0000269|PubMed:23599433}. SUBUNIT: Interacts with HSP90; this interaction stabilizes and activates TSSK6 (PubMed:23599433). Interacts with the heat shock proteins HSPCB, HSPA8 and HSPA1A. These interactions appear to be required for TSSK6 kinase activity. Interacts with TSACC; this interaction is direct and recruits TSACC to HSP90, which is essential for kinase activity (By similarity). {ECO:0000250|UniProtKB:Q9BXA6, ECO:0000269|PubMed:23599433}. TISSUE SPECIFICITY: Expressed in the testis, localized to the heads of elongating spermatids. {ECO:0000269|PubMed:15870294}. +Q9D6E4 TTC9B_MOUSE Tetratricopeptide repeat protein 9B (TPR repeat protein 9B) 239 25,909 Chain (1); Compositional bias (1); Erroneous initiation (1); Modified residue (2); Repeat (2) +P26687 TWST1_MOUSE Twist-related protein 1 (M-twist) 206 21,198 Chain (1); Compositional bias (1); Domain (1); Mutagenesis (10); Region (1); Sequence conflict (2) FUNCTION: Acts as a transcriptional regulator. Inhibits myogenesis by sequestrating E proteins, inhibiting trans-activation by MEF2, and inhibiting DNA-binding by MYOD1 through physical interaction. This interaction probably involves the basic domains of both proteins. Also represses expression of proinflammatory cytokines such as TNFA and IL1B. Regulates cranial suture patterning and fusion. Activates transcription as a heterodimer with E proteins. Regulates gene expression differentially, depending on dimer composition. Homodimers induce expression of FGFR2 and POSTN while heterodimers repress FGFR2 and POSTN expression and induce THBS1 expression. Heterodimerization is also required for osteoblast differentiation. Represses the activity of the circadian transcriptional activator: NPAS2-ARNTL/BMAL1 heterodimer. {ECO:0000269|PubMed:12553906, ECO:0000269|PubMed:14645221, ECO:0000269|PubMed:16502419, ECO:0000269|PubMed:17893140, ECO:0000269|PubMed:9343420}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Efficient DNA binding requires dimerization with another bHLH protein. Homodimer or heterodimer with E proteins such as TCF3. ID1 binds preferentially to TCF3 but does not interact efficiently with TWIST1 so ID1 levels control the amount of TCF3 available to dimerize with TWIST1 and thus determine the type of dimer formed. {ECO:0000269|PubMed:16502419, ECO:0000269|PubMed:17893140}. TISSUE SPECIFICITY: Subset of mesodermal cells. {ECO:0000269|PubMed:1840517}. +P46096 SYT1_MOUSE Synaptotagmin-1 (Synaptotagmin I) (SytI) (p65) 421 47,418 Beta strand (18); Chain (1); Compositional bias (1); Domain (2); Glycosylation (1); Helix (5); Lipidation (5); Metal binding (14); Modified residue (5); Region (1); Topological domain (2); Transmembrane (1); Turn (3) TRANSMEM 58 79 Helical. {ECO:0000255}. TOPO_DOM 1 57 Vesicular. {ECO:0000255}.; TOPO_DOM 80 421 Cytoplasmic. {ECO:0000255}. FUNCTION: May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse (PubMed:7961887). It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca(2+)-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca(2+)-independent manner; these are neurexins, syntaxin and AP2. Plays a role in dendrite formation by melanocytes (By similarity). {ECO:0000250|UniProtKB:P21579, ECO:0000269|PubMed:7961887}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:P21707}; Single-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:23345244}; Single-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, chromaffin granule membrane {ECO:0000250|UniProtKB:P21707}; Single-pass membrane protein {ECO:0000250|UniProtKB:P21707}. Cytoplasm {ECO:0000250|UniProtKB:P21707}. Note=Synaptic vesicles and chromaffin granules. {ECO:0000250|UniProtKB:P21707}. SUBUNIT: Homotetramer (Probable). Interacts with SCAMP5, STON2, SV2A, SV2B, SV2C and RIMS1 (By similarity). Forms a complex with SV2B, syntaxin 1 and SNAP25. Interacts with PRRT2 (PubMed:27052163). {ECO:0000250, ECO:0000269|PubMed:15466855, ECO:0000269|PubMed:27052163, ECO:0000305}. DOMAIN: The first C2 domain mediates Ca(2+)-dependent phospholipid binding. {ECO:0000250|UniProtKB:P21707}.; DOMAIN: The second C2 domain mediates interaction with SV2A and probably with STN2. {ECO:0000250|UniProtKB:P21707}. +Q99N50 SYTL2_MOUSE Synaptotagmin-like protein 2 (Exophilin-4) 950 106,806 Alternative sequence (6); Chain (1); Compositional bias (1); Domain (3); Mutagenesis (5) FUNCTION: Isoform 11 acts as a RAB27A effector protein and plays a role in cytotoxic granule exocytosis in lymphocytes. Required for cytotoxic granule docking at the immunologic synapse. Isoform 1 may play a role in melanosome transport and vesicle trafficking. It controls melanosome distribution in the cell periphery and regulates melanocyte morphology. Isoform 1 acts as a positive mediator of mucus secretion by the surface mucus cells of the stomach. Mediates basal mucus secretion by gastric surface cells by promoting the proper granule biognesis and docking of mucus granules with the apical plasma membrane. {ECO:0000269|PubMed:15543135, ECO:0000269|PubMed:16716193, ECO:0000269|PubMed:18266782}. PTM: Isoform 1 is highly susceptible to proteolytic degradation and is stabilized by the interaction with RAB27A. SUBCELLULAR LOCATION: Isoform 1: Melanosome membrane {ECO:0000269|PubMed:15543135}; Peripheral membrane protein {ECO:0000269|PubMed:15543135}. Note=Bound to melanosomes. Isoform 1 is localized mainly on peripheral melanosomes but not on less mature melanosomes around the nucleus. {ECO:0000269|PubMed:15543135}.; SUBCELLULAR LOCATION: Isoform 11: Cell membrane {ECO:0000269|PubMed:11243866, ECO:0000269|PubMed:17182843, ECO:0000269|PubMed:18266782}. Note=In the pancreatic alpha cells distributed in both peripheral and anterior regions. Localizes on the glucagon granules in the cell periphery. {ECO:0000269|PubMed:17182843}. SUBUNIT: Monomer. Binds NRXN1. Binds RAB27A that has been activated by GTP-binding. Interacts with RAB27B. {ECO:0000269|PubMed:11243866, ECO:0000269|PubMed:11773082, ECO:0000269|PubMed:16716193, ECO:0000269|PubMed:17182843, ECO:0000269|PubMed:18266782}. DOMAIN: The RabBD domain mediates interaction with RAB27A. {ECO:0000250}.; DOMAIN: The C2 1 domain mediates localization to the cell membrane. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in brain, lung, kidney, testis and in embryos after day 7. Detected at lower levels in skeletal muscle. Expressed in pancreatic alpha cells. Isoform 6 is highly expressed in brain, but not detectable in the other tissues tested. Isoform 1 is expressed abundantly in the stomach and is predominantly localized at the apical region of gastric-surface mucus cells. Isoform 11 is expressed in cytotoxic T-lymphocytes (CTL). {ECO:0000269|PubMed:11327731, ECO:0000269|PubMed:16716193, ECO:0000269|PubMed:17182843, ECO:0000269|PubMed:18266782}. +P09926 SURF2_MOUSE Surfeit locus protein 2 (Surf-2) 257 30,355 Chain (1); Modified residue (2) +P70279 SURF6_MOUSE Surfeit locus protein 6 355 41,235 Chain (1); Modified residue (3); Motif (2) FUNCTION: Binds to both DNA and RNA in vitro, with a stronger binding capacity for RNA. May represent a nucleolar constitutive protein involved in ribosomal biosynthesis or assembly. {ECO:0000269|PubMed:9548374}. PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:8639267, ECO:0000269|PubMed:9548374}. Note=Granular component of the nucleolus. TISSUE SPECIFICITY: Expressed in all tissues tested, including heart, brain, spleen, lung, liver, muscle, kidney and testis. +Q8BFT9 SVOP_MOUSE Synaptic vesicle 2-related protein (SV2-related protein) 548 60,769 Chain (1); Modified residue (3); Sequence conflict (2); Topological domain (13); Transmembrane (12) TRANSMEM 88 108 Helical. {ECO:0000255}.; TRANSMEM 123 143 Helical. {ECO:0000255}.; TRANSMEM 157 177 Helical. {ECO:0000255}.; TRANSMEM 181 201 Helical. {ECO:0000255}.; TRANSMEM 210 230 Helical. {ECO:0000255}.; TRANSMEM 239 259 Helical. {ECO:0000255}.; TRANSMEM 317 337 Helical. {ECO:0000255}.; TRANSMEM 374 394 Helical. {ECO:0000255}.; TRANSMEM 402 422 Helical. {ECO:0000255}.; TRANSMEM 425 445 Helical. {ECO:0000255}.; TRANSMEM 458 478 Helical. {ECO:0000255}.; TRANSMEM 490 510 Helical. {ECO:0000255}. TOPO_DOM 1 87 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 109 122 Vesicular. {ECO:0000255}.; TOPO_DOM 144 156 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 178 180 Vesicular. {ECO:0000255}.; TOPO_DOM 202 209 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 231 238 Vesicular. {ECO:0000255}.; TOPO_DOM 260 316 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 338 373 Vesicular. {ECO:0000255}.; TOPO_DOM 395 401 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 423 424 Vesicular. {ECO:0000255}.; TOPO_DOM 446 457 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 479 489 Vesicular. {ECO:0000255}.; TOPO_DOM 511 548 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +P30933 SVS5_MOUSE Seminal vesicle secretory protein 5 (SVS protein F) (Seminal vesicle secretory protein V) (SVS V) 122 13,019 Chain (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted, extracellular space. TISSUE SPECIFICITY: Testis. +Q6A028 SWP70_MOUSE Switch-associated protein 70 (SWAP-70) 585 68,996 Chain (1); Coiled coil (1); Compositional bias (1); Domain (1); Erroneous initiation (1); Sequence conflict (3) FUNCTION: Phosphatidylinositol 3,4,5-trisphosphate-dependent guanine nucleotide exchange factor (GEF) which, independently of RAS, transduces signals from tyrosine kinase receptors to RAC. It also mediates signaling of membrane ruffling. Regulates the actin cytoskeleton as an effector or adapter protein in response to agonist stimulated phosphatidylinositol (3,4)-bisphosphate production and cell protrusion (By similarity). {ECO:0000250}. PTM: Tyrosine-phosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10382743}. Cell membrane {ECO:0000250|UniProtKB:Q9UH65}. Nucleus {ECO:0000269|PubMed:10382743, ECO:0000269|PubMed:9642267}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q9UH65}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9UH65}. Note=Localizes predominantly to the nucleus in activated cells. Only a small amount can be detected in the cytoplasm. {ECO:0000269|PubMed:10382743}. SUBUNIT: The SWAP complex consists of NPM1, NCL, PARP1 and SWAP70. {ECO:0000269|PubMed:9642267}. DOMAIN: The PH domain is essential for phosphatidylinositol 3,4,5-trisphosphate binding. {ECO:0000250}. TISSUE SPECIFICITY: Spleen. Expressed only in B-cells that have been induced to switch to various Ig isotypes. {ECO:0000269|PubMed:10382743, ECO:0000269|PubMed:9642267}. +Q9DBQ9 SWT1_MOUSE Transcriptional protein SWT1 907 103,168 Alternative sequence (3); Chain (1); Compositional bias (1); Domain (1); Frameshift (1); Sequence conflict (2) +Q62209 SYCP1_MOUSE Synaptonemal complex protein 1 (SCP-1) 993 115,935 Chain (1); Coiled coil (3); Compositional bias (2); Erroneous initiation (1); Modified residue (1); Motif (4); Region (2); Sequence conflict (5) FUNCTION: Major component of the transverse filaments of synaptonemal complexes, formed between homologous chromosomes during meiotic prophase (PubMed:16717126). Required for normal assembly of the central element of the synaptonemal complexes (PubMed:15937223). Required for normal centromere pairing during meiosis (PubMed:22761579). Required for normal meiotic chromosome synapsis during oocyte and spermatocyte development and for normal male and female fertility (PubMed:15937223). {ECO:0000269|PubMed:15937223, ECO:0000269|PubMed:16717126, ECO:0000269|PubMed:22761579}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16717126}. Chromosome {ECO:0000269|PubMed:15937223, ECO:0000269|PubMed:16717126, ECO:0000269|PubMed:22761579}. Chromosome, centromere {ECO:0000269|PubMed:22761579}. Note=In tripartite segments of synaptonemal complexes, between lateral elements in the nucleus. Its N-terminus is found towards the center of the synaptonemal complex while the C-terminus extends well into the lateral domain of the synaptonemal complex (By similarity). Only rarely detected at centromeres during leptotene and zygotene. Detected at centromeres during mid-diplotene, when it is no longer present along chromosome arms. No longer detected at centromeres at later stages of meiosis (PubMed:22761579). {ECO:0000250|UniProtKB:Q03410, ECO:0000269|PubMed:22761579}. SUBUNIT: Structural component of synaptonemal complexes (PubMed:15937223, PubMed:16717126, PubMed:22761579). Homotetramer that consists of an N-terminal four-helical bundle that bifurcates into two elongated C-terminal dimeric coiled coils. This tetrameric building block potentially self-assembles into a supramolecular zipper-like lattice to mediate meiotic chromosome synapsis. Self-assembly is likely initiated by local proton density at chromosome axis, which is predicted to trigger antiparallel back to back assembly of adjacent C-terminal ends into tetrameric structures that anchor to chromosomal DNA. Then the N-terminal ends are predicted to undergo cooperative antiparallel head to head assembly at the midline of synaptonemal complexes central element to form a zipper-like lattice between properly aligned homologous chromosomes (By similarity). The nascent synapsis generated by SYCP1 is stabilized through interaction with central element proteins SYCE1 and SYCE2 (PubMed:15944401). {ECO:0000250|UniProtKB:Q15431, ECO:0000269|PubMed:15937223, ECO:0000269|PubMed:15944401, ECO:0000269|PubMed:16717126, ECO:0000269|PubMed:22761579}. DOMAIN: The molecule is in a coiled coil structure that is formed by 4 polypeptide chains. The N-terminal region exhibits a prominent seven-residues periodicity. {ECO:0000250|UniProtKB:Q15431}. TISSUE SPECIFICITY: Detected in testis (PubMed:15937223). Detected in spermatocytes (at protein level) (PubMed:22761579). {ECO:0000269|PubMed:15937223, ECO:0000269|PubMed:22761579}. +P69744 TRPV5_MOUSE Transient receptor potential cation channel subfamily V member 5 (TrpV5) (Calcium transport protein 2) (CaT2) (Epithelial calcium channel 1) (ECaC1) (Osm-9-like TRP channel 3) (OTRPC3) 723 82,218 Chain (1); Frameshift (1); Intramembrane (1); Metal binding (1); Modified residue (2); Mutagenesis (2); Region (3); Repeat (6); Sequence conflict (1); Topological domain (6); Transmembrane (6) INTRAMEM 517 537 Pore-forming. {ECO:0000250|UniProtKB:Q9XSM3}. TRANSMEM 321 341 Helical. {ECO:0000250|UniProtKB:Q9XSM3}.; TRANSMEM 379 401 Helical. {ECO:0000250|UniProtKB:Q9XSM3}.; TRANSMEM 413 435 Helical. {ECO:0000250|UniProtKB:Q9XSM3}.; TRANSMEM 442 462 Helical. {ECO:0000250|UniProtKB:Q9XSM3}.; TRANSMEM 486 506 Helical. {ECO:0000250|UniProtKB:Q9XSM3}.; TRANSMEM 550 570 Helical. {ECO:0000250|UniProtKB:Q9XSM3}. TOPO_DOM 1 320 Cytoplasmic. {ECO:0000250|UniProtKB:Q9XSM3}.; TOPO_DOM 342 378 Extracellular. {ECO:0000250|UniProtKB:Q9XSM3}.; TOPO_DOM 402 412 Extracellular. {ECO:0000250|UniProtKB:Q9XSM3}.; TOPO_DOM 436 441 Cytoplasmic. {ECO:0000250|UniProtKB:Q9XSM3}.; TOPO_DOM 463 485 Extracellular. {ECO:0000250|UniProtKB:Q9XSM3}.; TOPO_DOM 571 723 Cytoplasmic. {ECO:0000250|UniProtKB:Q9XSM3}. FUNCTION: Constitutively active calcium selective cation channel thought to be involved in Ca(2+) reabsorption in kidney and intestine (PubMed:12077127, PubMed:14679186). Required for normal Ca(2+) reabsorption in the kidney distal convoluted tubules (PubMed:14679186). The channel is activated by low internal calcium level and the current exhibits an inward rectification. A Ca(2+)-dependent feedback regulation includes fast channel inactivation and slow current decay (PubMed:12077127). Heteromeric assembly with TRPV6 seems to modify channel properties. TRPV5-TRPV6 heteromultimeric concatemers exhibit voltage-dependent gating (By similarity). {ECO:0000250|UniProtKB:Q9XSM3, ECO:0000269|PubMed:12077127, ECO:0000269|PubMed:14679186}. PTM: Glycosylated. {ECO:0000250|UniProtKB:Q9NQA5}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:12660155}; Multi-pass membrane protein {ECO:0000269|PubMed:12660155}. Note=Colocalized with S100A10 and ANAX2 along the apical domain of kidney distal tubular cells. {ECO:0000269|PubMed:12660155}. SUBUNIT: Homotetramer and probably heterotetramer with TRPV6. Interacts with TRPV6 (PubMed:12574114). Interacts with S100A10 and probably with the ANAX2-S100A10 heterotetramer. The interaction with S100A10 is required for the trafficking to the plasma membrane (PubMed:12660155). Interacts with calmodulin (PubMed:15123711). Interacts with BSPRY, which results in its inactivation (PubMed:16380433). {ECO:0000269|PubMed:12574114, ECO:0000269|PubMed:12660155, ECO:0000269|PubMed:15123711, ECO:0000269|PubMed:16380433}. TISSUE SPECIFICITY: Detected in kidney cortex (at protein level). {ECO:0000269|PubMed:14679186}. +Q8BU30 SYIC_MOUSE Isoleucine--tRNA ligase, cytoplasmic (EC 6.1.1.5) (Isoleucyl-tRNA synthetase) (IRS) (IleRS) 1262 144,271 Binding site (1); Chain (1); Modified residue (3); Motif (2); Sequence conflict (1) FUNCTION: Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA. {ECO:0000269|PubMed:12060739}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P41252}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P41252}. SUBUNIT: Part of a multisubunit complex that groups tRNA ligases for Arg (RARS), Asp (DARS), Gln (QARS), Ile (IARS), Leu (LARS), Lys (KARS), Met (MARS) the bifunctional ligase for Glu and Pro (EPRS) and the auxiliary subunits AIMP1/p43, AIMP2/p38 and EEF1E1/p18. {ECO:0000269|PubMed:12060739}. +Q9JMH6 TRXR1_MOUSE Thioredoxin reductase 1, cytoplasmic (TR) (EC 1.8.1.9) (Thioredoxin reductase TR1) 613 67,084 Active site (1); Alternative sequence (1); Chain (1); Compositional bias (1); Cross-link (1); Disulfide bond (1); Erroneous termination (3); Modified residue (2); Non-standard residue (1); Nucleotide binding (1); Sequence conflict (3) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10721726}. SUBUNIT: Homodimer. {ECO:0000250}. +P07146 TRY2_MOUSE Anionic trypsin-2 (EC 3.4.21.4) (Anionic trypsin II) (Pretrypsinogen II) (Serine protease 2) 246 26,204 Active site (3); Chain (1); Disulfide bond (6); Domain (1); Metal binding (4); Propeptide (1); Signal peptide (1); Site (1) SUBCELLULAR LOCATION: Secreted, extracellular space. +P21845 TRYB2_MOUSE Tryptase beta-2 (Tryptase-2) (EC 3.4.21.59) (Mast cell protease 6) (mMCP-6) 276 30,927 Active site (3); Alternative sequence (2); Chain (1); Disulfide bond (4); Domain (1); Glycosylation (1); Modified residue (1); Propeptide (1); Signal peptide (1) FUNCTION: Tryptase is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type. Plays a role in innate immunity. {ECO:0000269|PubMed:17456473}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Released from the secretory granules upon mast cell activation. {ECO:0000250}. SUBUNIT: Homotetramer. The active tetramer is converted to inactive monomers at neutral and acidic pH in the absence of heparin. Low concentrations of inactive monomers become active monomers at pH 6.0 in the presence of heparin. When the concentration of active monomers is higher, they convert to active monomers and then to active tetramers. These monomers are active and functionally distinct from the tetrameric enzyme. In contrast to the hidden active sites in the tetrameric form, the active site of the monomeric form is accessible for macromolecular proteins and inhibitors eg: fibrinogen which is a substrate for the monomeric but not for the tetrameric form. The monomeric form forms a complex with SERPINB6 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: During embryogenesis, detected primarily in skin. {ECO:0000269|PubMed:16777228}. +Q9D6K5 SYJ2B_MOUSE Synaptojanin-2-binding protein (Activin receptor-interacting protein 2) (Activin receptor-interacting protein 4) (Mitochondrial outer membrane protein 25) 145 15,815 Alternative sequence (4); Chain (1); Domain (1); Erroneous initiation (1); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 118 138 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 1 117 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 139 145 Mitochondrial intermembrane. {ECO:0000255}. FUNCTION: Isoform 1 regulates endocytosis of activin type 2 receptor kinases through the Ral/RALBP1-dependent pathway and may be involved in suppression of activin-induced signal transduction. Isoform 2 and isoform 3 show a stimulatory affect on activin-induced signal transduction and enhance activin type 2 expression at the cell surface. {ECO:0000269|PubMed:11882656, ECO:0000269|PubMed:16648306}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q9WVJ4}; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:Q9WVJ4}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9WVJ4}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:11882656}. SUBUNIT: Binds (via the PDZ domain) to isoform 2A of SYNJ2 (via the unique motif in the C-terminus) (By similarity). Interacts (via C-terminus) with RALBP1. Interacts (via PDZ domain) with ACVR2A (via C-terminus) and ACVR2B (via C-terminus). Forms a ternary complex with ACVR2A and RALBP1 (PubMed:11882656, PubMed:16648306). Interacts with MAPK12 (By similarity). Interacts with DLL1; enhances DLL1 protein stability, and promotes notch signaling in endothelial cells (By similarity). {ECO:0000250|UniProtKB:P57105, ECO:0000250|UniProtKB:Q9WVJ4, ECO:0000269|PubMed:11882656, ECO:0000269|PubMed:16648306}. TISSUE SPECIFICITY: Isoform 1 and isoform 2 are widely expressed, notably in brain, heart, lung, liver, kidney, skeletal muscle, ovary and testis. Isoform 3 is detected only in heart, spleen and testis. {ECO:0000269|PubMed:11882656, ECO:0000269|PubMed:16648306}. +Q9QUL7 TRYG1_MOUSE Tryptase gamma (EC 3.4.21.-) (Transmembrane tryptase) [Cleaved into: Tryptase gamma light chain; Tryptase gamma heavy chain] 311 32,656 Active site (3); Chain (3); Disulfide bond (5); Domain (1); Glycosylation (2); Signal peptide (1); Transmembrane (1) TRANSMEM 277 297 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in many tissues. +Q925I4 TS1R2_MOUSE Taste receptor type 1 member 2 (G-protein coupled receptor 71) (Sweet taste receptor T1R2) 843 95,736 Chain (1); Glycosylation (9); Natural variant (2); Sequence conflict (4); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 571 591 Helical; Name=1. {ECO:0000255}.; TRANSMEM 607 627 Helical; Name=2. {ECO:0000255}.; TRANSMEM 643 663 Helical; Name=3. {ECO:0000255}.; TRANSMEM 683 703 Helical; Name=4. {ECO:0000255}.; TRANSMEM 732 752 Helical; Name=5. {ECO:0000255}.; TRANSMEM 765 785 Helical; Name=6. {ECO:0000255}.; TRANSMEM 790 810 Helical; Name=7. {ECO:0000255}. TOPO_DOM 20 570 Extracellular. {ECO:0000255}.; TOPO_DOM 592 606 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 628 642 Extracellular. {ECO:0000255}.; TOPO_DOM 664 682 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 704 731 Extracellular. {ECO:0000255}.; TOPO_DOM 753 764 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 786 789 Extracellular. {ECO:0000255}.; TOPO_DOM 811 843 Cytoplasmic. {ECO:0000255}. FUNCTION: Putative taste receptor. TAS1R2/TAS1R3 recognizes diverse natural and synthetic sweeteners. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBUNIT: Forms heterodimers with TAS1R3. TISSUE SPECIFICITY: Expressed mainly in circumvallate and foliate taste papillae. {ECO:0000269|PubMed:11319557}. +Q8VDC0 SYLM_MOUSE Probable leucine--tRNA ligase, mitochondrial (EC 6.1.1.4) (Leucyl-tRNA synthetase) (LeuRS) 902 101,480 Binding site (1); Chain (1); Modified residue (2); Motif (2); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. +Q499X9 SYMM_MOUSE Methionine--tRNA ligase, mitochondrial (EC 6.1.1.10) (Methionyl-tRNA synthetase 2) (Mitochondrial methionyl-tRNA synthetase) (MtMetRS) 586 65,805 Binding site (1); Chain (1); Erroneous initiation (1); Motif (2); Sequence conflict (1); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. +O88935 SYN1_MOUSE Synapsin-1 (Synapsin I) 706 74,097 Alternative sequence (3); Chain (1); Glycosylation (11); Modified residue (24); Region (5); Sequence conflict (1) FUNCTION: Neuronal phosphoprotein that coats synaptic vesicles, binds to the cytoskeleton, and is believed to function in the regulation of neurotransmitter release. Regulation of neurotransmitter release. The complex formed with NOS1 and CAPON proteins is necessary for specific nitric-oxide functions at a presynaptic level. PTM: Substrate of at least four different protein kinases. It is probable that phosphorylation plays a role in the regulation of synapsin-1 in the nerve terminal (By similarity). {ECO:0000250}.; PTM: Phosphorylation at Ser-9 dissociates synapsins from synaptic vesicles. {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, synapse {ECO:0000269|PubMed:11571277}. Golgi apparatus {ECO:0000269|PubMed:11571277}. SUBUNIT: Homodimer. Interacts with CAPON. Forms a ternary complex with NOS1 (By similarity). Isoform Ib interacts with PRNP. {ECO:0000250, ECO:0000269|PubMed:11571277}. DOMAIN: The A region binds phospholipids with a preference for negatively charged species. {ECO:0000250}. +Q9EPM5 SYNCI_MOUSE Syncoilin (Syncoilin intermediate filament 1) (Syncoilin-1) 470 53,630 Alternative sequence (3); Chain (1); Domain (1); Modified residue (2); Region (7); Sequence conflict (4) FUNCTION: Atypical type III intermediate filament (IF) protein that may play a supportive role in the efficient coupling of mechanical stress between the myofibril and fiber exterior. May facilitate lateral force transmission during skeletal muscle contraction. Does not form homofilaments nor heterofilaments with other IF proteins. {ECO:0000269|PubMed:11694502, ECO:0000269|PubMed:18367591}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:11053421, ECO:0000269|PubMed:11694502, ECO:0000269|PubMed:17629480}. Note=In skeletal muscle, colocalizes with DES and DTNA, and is localized at the myotendinous and neuromuscular junctions, sarcolemma and Z-lines. In myotubes, detected in a punctate cytoplasmic pattern. {ECO:0000269|PubMed:11053421, ECO:0000269|PubMed:11694502, ECO:0000269|PubMed:17629480}. SUBUNIT: May link the dystrophin-associated glycoprotein complex (DAPC) to intracellular desmin (DES) filaments. Interacts with DES and DTNA. {ECO:0000269|PubMed:11053421, ECO:0000269|PubMed:11694502}. TISSUE SPECIFICITY: Detected strongly in skeletal muscle and heart and weakly in lung (at protein level). Highly expressed in skeletal muscle and lung and weakly in lung and testis. {ECO:0000269|PubMed:11053421}. +A2ANU3 SYNG1_MOUSE Synapse differentiation-inducing gene protein 1 (SynDIG1) (Dispanin subfamily C member 2) (DSPC2) (Transmembrane protein 90B) 258 28,456 Chain (1); Compositional bias (1); Intramembrane (1); Modified residue (1); Topological domain (3); Transmembrane (1) INTRAMEM 229 249 Helical. {ECO:0000255}. TRANSMEM 182 202 Helical. {ECO:0000255}. TOPO_DOM 1 181 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 203 228 Extracellular. {ECO:0000255}.; TOPO_DOM 250 258 Extracellular. {ECO:0000255}. FUNCTION: May regulate AMPA receptor content at nascent synapses, and have a role in postsynaptic development and maturation. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20152115}; Single-pass type II membrane protein {ECO:0000269|PubMed:20152115}. Early endosome membrane {ECO:0000269|PubMed:20152115}; Single-pass type II membrane protein {ECO:0000269|PubMed:20152115}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000269|PubMed:20152115}. Cell junction, synapse {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cell projection, dendritic spine {ECO:0000250}. Note=Shuttles between the cell surface and early endosome membrane. SUBUNIT: Homodimer. Interacts with GRIA1 and GRIA2. {ECO:0000269|PubMed:20152115}. TISSUE SPECIFICITY: Brain-specific. Expressed in Purkinje neurons in cerebellum. Also detected in the hippocampus. Found at excitatory synapses and postsynaptic cells. {ECO:0000269|PubMed:12408845, ECO:0000269|PubMed:20152115}. +Q8CHC4 SYNJ1_MOUSE Synaptojanin-1 (EC 3.1.3.36) (Synaptic inositol 1,4,5-trisphosphate 5-phosphatase 1) 1574 172,617 Chain (1); Compositional bias (2); Domain (2); Erroneous initiation (1); Modified residue (10) FUNCTION: Phosphatase that acts on various phosphoinositides, including phosphatidylinositol 4-phosphate, phosphatidylinositol (4,5)-bisphosphate and phosphatidylinositol (3,4,5)-trisphosphate (By similarity). Has a role in clathrin-mediated endocytosis (By similarity). Hydrolyzes PIP2 bound to actin regulatory proteins resulting in the rearrangement of actin filaments downstream of tyrosine kinase and ASH/GRB2 (By similarity). {ECO:0000250|UniProtKB:O18964, ECO:0000250|UniProtKB:O43426}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O18964}. SUBUNIT: Interacts with ASH/GRB2. Interacts with PACSIN1, PACSIN2 and PACSIN3 (PubMed:11082044). Binds AMPH, SH3GL1, SH3GL2 and SH3GL3. Interacts with MYO1E (via SH3 domain). Interacts with BIN1 and DNM1 (By similarity). {ECO:0000250|UniProtKB:Q62910, ECO:0000269|PubMed:11082044}. DOMAIN: Binds to EPS15 (a clathrin coat-associated protein) via a C-terminal domain containing three Asn-Pro-Phe (NPF) repeats. {ECO:0000250}.; DOMAIN: The C-terminal proline-rich region mediates binding to a variety of SH3 domain-containing proteins including AMPH, SH3GL1, SH3GL2, SH3GL3 and GRB2. +Q6ZWQ0 SYNE2_MOUSE Nesprin-2 (KASH domain-containing protein 2) (KASH2) (Nuclear envelope spectrin repeat protein 2) (Nucleus and actin connecting element protein) (Protein NUANCE) (Synaptic nuclear envelope protein 2) (Syne-2) 6874 782,725 Alternative sequence (4); Chain (1); Coiled coil (1); Compositional bias (2); Disulfide bond (2); Domain (3); Modified residue (9); Mutagenesis (2); Region (2); Repeat (56); Topological domain (2); Transmembrane (1) TRANSMEM 6824 6844 Helical; Anchor for type IV membrane protein. {ECO:0000255|PROSITE-ProRule:PRU00385}. TOPO_DOM 1 6823 Cytoplasmic. {ECO:0000255|PROSITE-ProRule:PRU00385}.; TOPO_DOM 6845 6874 Perinuclear space. {ECO:0000255|PROSITE-ProRule:PRU00385}. FUNCTION: Multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain the subcellular spatial organization. As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning. Specifically, SYNE2 and SUN2 assemble in arrays of transmembrane actin-associated nuclear (TAN) lines which are bound to F-actin cables and couple the nucleus to retrograde actin flow during actin-dependent nuclear movement. May be involved in nucleus-centrosome attachment. During interkinetic nuclear migration (INM) at G2 phase and nuclear migration in neural progenitors its LINC complex association with SUN1/2 and probable association with cytoplasmic dynein-dynactin motor complexes functions to pull the nucleus toward the centrosome; SYNE1 and SYNE2 seem to act redundantly in cerebellum, midbrain, brain stem, and other brain regions except cerebral cortex and hippocampus. During INM at G1 phase mediates respective LINC complex association with kinesin to push the nucleus away from the centrosome. Involved in nuclear migration in retinal photoreceptor progenitors. Required for centrosome migration to the apical cell surface during early ciliogenesis. {ECO:0000250|UniProtKB:Q8WXH0, ECO:0000269|PubMed:18477613, ECO:0000269|PubMed:19596800, ECO:0000269|PubMed:19874786, ECO:0000269|PubMed:20724637, ECO:0000269|PubMed:21177258, ECO:0000269|PubMed:23071752}. PTM: The disulfid bond with SUN2 is required for stability of the SUN2:SYNE2/KASH2 LINC complex under tensile forces though not required for the interaction. {ECO:0000250|UniProtKB:Q8WXH0}. SUBCELLULAR LOCATION: Nucleus outer membrane; Single-pass type IV membrane protein; Cytoplasmic side. Sarcoplasmic reticulum membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Cell membrane; Single-pass membrane protein. Cytoplasm, cytoskeleton. Mitochondrion {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Note=Different isoform patterns are found in the different compartments of the cell. The isoforms having the C-terminal transmembrane span can be found in several organellar membranes like the nuclear envelope, the sarcoplasmic reticulum of myoblasts, or the lamellipodia and focal adhesions at the cell membrane. The largest part of the outer nuclear membrane-associated protein is cytoplasmic, while its C-terminal part is associated with the nuclear envelope, most probably the outer nuclear membrane. Remains associated with the nuclear envelope during its breakdown in mitotic cells. Shorter soluble isoforms can be found in the cytoplasm and within the nucleus (By similarity). {ECO:0000250}. SUBUNIT: Core component of LINC complexes which are composed of inner nuclear membrane SUN domain-containing proteins coupled to outer nuclear membrane KASH domain-containing nesprins. SUN and KASH domain-containing proteins seem to bind each other promiscuously; however, some LINC complex constituents are tissue- or cell type-specific. At least SUN1/2-containing core LINC complexes are proposed to be hexameric composed of three protomers of each KASH and SUN domain-containing protein. The SUN2:SYNE2/KASH2 complex is a heterohexamer; the homotrimeric cloverleave-like conformation of the SUN domain is a prerequisite for LINC complex formation in which three separate SYNE2/KASH2 peptides bind at the interface of adjacent SUN domains. Interacts with EMD, LMNA, MKS3 and F-actin via its N-terminal domain. Interacts with DCTN1 and DYNC1I1/2; suggesting the association with the dynein-dynactin motor complex. Associates with kinesin motor complexes. Interacts with TMEM67. {ECO:0000250|UniProtKB:Q8WXH0, ECO:0000269|PubMed:19596800, ECO:0000269|PubMed:19874786, ECO:0000269|PubMed:20724637, ECO:0000269|PubMed:21177258, ECO:0000269|PubMed:23071752}. DOMAIN: The KASH domain, which contains a transmembrane domain, mediates the nuclear envelope targeting and is involved in the binding to SUN1 and SUN2 through recognition of their SUN domains. {ECO:0000250}. TISSUE SPECIFICITY: C-terminal isoforms are highly expressed in the brain, hert and skeletal muscle. Isoform 1 (Nesprin-2 Giant) is most prevalent in the brain, skin, kidney and skeletal muscle. {ECO:0000269|PubMed:18477613}. +Q91YE8 SYNP2_MOUSE Synaptopodin-2 (Myopodin) 1087 116,527 Alternative sequence (2); Chain (1); Compositional bias (4); Domain (1); Modified residue (24); Motif (2); Mutagenesis (2); Region (9); Sequence conflict (2) FUNCTION: Has an actin-binding and actin-bundling activity (PubMed:11673475). Can induce the formation of F-actin networks. At the sarcomeric Z lines is proposed to act as adapter protein that links nascent myofibers to the sarcolemma via ZYX and may play a role in early assembly and stabilization of the Z lines. Involved in autophagosome formation. May play a role in chaperone-assisted selective autophagy (CASA) involved in Z lines maintenance in striated muscle under mechanical tension; may link the client-processing CASA chaperone machinery to a membrane-tethering and fusion complex providing autophagosome membranes. Involved in regulation of cell migration. May be a tumor suppressor (By similarity). {ECO:0000250|UniProtKB:D4A702, ECO:0000250|UniProtKB:Q9UMS6, ECO:0000269|PubMed:11673475}. PTM: Phosphorylated by PKA, and by CaMK2 at multiple sites. Dephosphorylated by calcineurin at Ser-555 and Thr-602; abrogating interaction with YWHAB and impairing nuclear import. {ECO:0000269|PubMed:17923693}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11673475, ECO:0000269|PubMed:16309678, ECO:0000269|PubMed:17923693}. Cytoplasm {ECO:0000269|PubMed:11673475, ECO:0000269|PubMed:17923693}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:11673475}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q9UMS6}. Note=Shuttles between the nucleus and the cytoplasm in a differentiation-dependent and stress-induced fashion. In undifferentiated myoblasts strongly expressed in the nucleus, after induction of myotube differentiation is located to both nucleus and cytoplasm along acting filaments, and in differentiated myotubes is located at the Z lines. Upon stress redistributes from cytoplasm of myoblasts and myotubes to the nucleus. Nuclear import is KPNA2-dependent and promoted by phosphorylation by PKA and/or CaMK2, and inhibition of calcineurin. The nuclear export is XPO1-dependent (PubMed:11673475, PubMed:15883195, PubMed:17923693). {ECO:0000250|UniProtKB:Q9UMS6, ECO:0000269|PubMed:11673475, ECO:0000269|PubMed:17923693}. SUBUNIT: May self-associate in muscle cells under oxidative stress (By similarity). Binds F-actin (PubMed:11673475). Interacts with ACTN2; ACTN2 is proposed to anchor SYOP2 at Z lines in mature myocytes. Interacts with AKAP6, PPP3CA and CAMK2A. Interacts (phosphorylated form) with YWHAB; YWHAB competes with ACTN2 for interaction with SYNPO2 (PubMed:15883195, PubMed:17923693). Interacts with KPNA2; mediating nuclear import of SYNOP2; dependent on interaction with YWHAB (PubMed:15883195). Interacts with IPO13; may be implicated in SYNOP2 nuclear import (By similarity). Interacts with ZYX, FLNC, ILK. Interacts with BAG3 (via WW 1 domain). May associate with the CASA complex consisting of HSPA8, HSPB8 and BAG3. Interacts with VPS18 (By similarity). {ECO:0000250|UniProtKB:D4A702, ECO:0000250|UniProtKB:Q9UMS6, ECO:0000269|PubMed:11673475, ECO:0000269|PubMed:15883195, ECO:0000269|PubMed:17923693}. DOMAIN: The PPPY motif interacts with the WW domain 1 of BAG3. {ECO:0000250|UniProtKB:Q9UMS6}. TISSUE SPECIFICITY: Expressed in skeletal muscle, heart, colon, stomach, uterus and lung. Expression is restricted to muscle cell layers in colon, uterus and stomach. {ECO:0000269|PubMed:11673475}. +Q8CA03 TSCOT_MOUSE Thymic stromal cotransporter protein (Solute carrier family 46 member 2) 479 52,083 Chain (1); Glycosylation (2); Sequence conflict (4); Topological domain (13); Transmembrane (12) TRANSMEM 24 44 Helical; Name=1. {ECO:0000255}.; TRANSMEM 81 101 Helical; Name=2. {ECO:0000255}.; TRANSMEM 111 131 Helical; Name=3. {ECO:0000255}.; TRANSMEM 141 161 Helical; Name=4. {ECO:0000255}.; TRANSMEM 175 195 Helical; Name=5. {ECO:0000255}.; TRANSMEM 208 228 Helical; Name=6. {ECO:0000255}.; TRANSMEM 282 302 Helical; Name=7. {ECO:0000255}.; TRANSMEM 322 342 Helical; Name=8. {ECO:0000255}.; TRANSMEM 349 369 Helical; Name=9. {ECO:0000255}.; TRANSMEM 372 392 Helical; Name=10. {ECO:0000255}.; TRANSMEM 408 428 Helical; Name=11. {ECO:0000255}.; TRANSMEM 442 462 Helical; Name=12. {ECO:0000255}. TOPO_DOM 1 23 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 45 80 Extracellular. {ECO:0000255}.; TOPO_DOM 102 110 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 132 140 Extracellular. {ECO:0000255}.; TOPO_DOM 162 174 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 196 207 Extracellular. {ECO:0000255}.; TOPO_DOM 229 281 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 303 321 Extracellular. {ECO:0000255}.; TOPO_DOM 343 348 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 370 371 Extracellular. {ECO:0000255}.; TOPO_DOM 393 407 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 429 441 Extracellular. {ECO:0000255}.; TOPO_DOM 463 479 Cytoplasmic. {ECO:0000255}. FUNCTION: May act as a transporter. {ECO:0000250}. PTM: Glycosylated. {ECO:0000269|PubMed:10706709}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed on cortical epithelial cells in the thymus. Mainly expressed in the thymic cortex and is highly enriched in SCID thymus. Also expressed in lymph nodes, heart, fetal liver, brain, spleen, intestine and kidney, but not in adult liver, skin, skeletal muscle and lung. {ECO:0000269|PubMed:10706709, ECO:0000269|PubMed:10978518}. +Q70IV5 SYNEM_MOUSE Synemin (Desmuslin) 1561 173,209 Alternative sequence (3); Chain (1); Domain (1); Modified residue (12); Region (10); Sequence conflict (36) FUNCTION: Type-VI intermediate filament (IF) which plays an important cytoskeletal role within the muscle cell cytoskeleton. It forms heteropolymeric IFs with desmin and/or vimentin, and via its interaction with cytoskeletal proteins alpha-dystrobrevin, dystrophin, talin-1, utrophin and vinculin, is able to link these heteropolymeric IFs to adherens-type junctions, such as to the costameres, neuromuscular junctions, and myotendinous junctions within striated muscle cells (By similarity). {ECO:0000250, ECO:0000269|PubMed:15265691}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17356066}. Cell junction, adherens junction {ECO:0000250|UniProtKB:O15061}. Note=There are at least two distinct SYNM subpopulations, one in which SYMN interacts with DES within the Z-lines, and another in which it interacts with both DTNA and DES at the costamere. {ECO:0000250|UniProtKB:O15061, ECO:0000269|PubMed:17356066}. SUBUNIT: Interacts with DES, DMD, DTNA, TLN1, UTRN and VCL (By similarity). Isoform 1 and isoform 2 interact with GFAP and VIM. {ECO:0000250|UniProtKB:O15061, ECO:0000269|PubMed:17356066}. TISSUE SPECIFICITY: Isoform 2 and isoform 3 are detected in adult skeletal muscle, heart and bladder, whereas isoform 1 is only detected in adult bladder (at protein level). {ECO:0000269|PubMed:15265691}. +Q6NY15 TSG10_MOUSE Testis-specific gene 10 protein 697 81,262 Alternative sequence (2); Chain (1); Modified residue (1); Region (1); Sequence conflict (6) FUNCTION: Plays a role in spermatogenesis (PubMed:14585816). When overexpressed, prevents nuclear localization of HIF1A (PubMed:16777103). {ECO:0000269|PubMed:14585816, ECO:0000269|PubMed:16777103}. PTM: Processed into N-terminal 27-kDa and C-terminal 55-kDa fragments. {ECO:0000269|PubMed:14585816}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Z220}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q9BZW7}. Note=In mature spermatozoa, localizes to the centriole and midpiece (By similarity). The 27-kDa peptide associates with the fibrous sheath in mature spermatozoa and localizes to the principal piece of sperm tail, while the 55-kDa peptide localizes to the midpiece (PubMed:16643851, PubMed:16777103). Detected in the cytoplasm of almost all spermatogonial cells within the seminiferous tubules (By similarity). {ECO:0000250|UniProtKB:Q9BZW7, ECO:0000250|UniProtKB:Q9Z220, ECO:0000269|PubMed:16643851, ECO:0000269|PubMed:16777103}. SUBUNIT: Interacts with HIF1A. {ECO:0000269|PubMed:16777103}. TISSUE SPECIFICITY: Predominantly expressed in testis, in spermatozoa (at protein level) (PubMed:14585816, PubMed:16643851). Not detected in Leydig cells (PubMed:16643851). The N-terminal 27-kDa fragment is also detected in liver, while the C-terminal 55-kDa fragment is also found retina, brain and kidney (at protein level) (PubMed:16643851). {ECO:0000269|PubMed:14585816, ECO:0000269|PubMed:16643851}. +Q9JHH2 TSN32_MOUSE Tetraspanin-32 (Tspan-32) (AML1-regulated transmembrane protein 1) (Protein Phemx) 256 28,906 Alternative sequence (5); Chain (1); Sequence conflict (2); Transmembrane (4) TRANSMEM 15 35 Helical. {ECO:0000255}.; TRANSMEM 61 81 Helical. {ECO:0000255}.; TRANSMEM 90 110 Helical. {ECO:0000255}.; TRANSMEM 203 223 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed exclusively in hematopoietic tissues. Expression detected in spleen, thymus, bone marrow and peripheral blood leukocytes but not in heart, brain, lung, liver, kidney or testis. {ECO:0000269|PubMed:10950922}. +Q9QY33 TSN3_MOUSE Tetraspanin-3 (Tspan-3) (OSP-associated protein 1) (OAP-1) (Tetraspanin TM4-A) (Transmembrane 4 superfamily member 8) 253 28,049 Chain (1); Glycosylation (4); Sequence conflict (2); Topological domain (5); Transmembrane (4) TRANSMEM 12 32 Helical. {ECO:0000255}.; TRANSMEM 51 71 Helical. {ECO:0000255}.; TRANSMEM 86 106 Helical. {ECO:0000255}.; TRANSMEM 213 233 Helical. {ECO:0000255}. TOPO_DOM 1 11 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 33 50 Extracellular. {ECO:0000255}.; TOPO_DOM 72 85 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 107 212 Extracellular. {ECO:0000255}.; TOPO_DOM 234 253 Cytoplasmic. {ECO:0000255}. FUNCTION: Regulates the proliferation and migration of oligodendrocytes, a process essential for normal myelination and repair. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Interacts with claudin-11/CLDN11 and integrins. {ECO:0000269|PubMed:11309411}. +Q8BWB1 SYP2L_MOUSE Synaptopodin 2-like protein 975 102,953 Chain (1); Compositional bias (2); Domain (1); Modified residue (35) FUNCTION: Actin-associated protein that may play a role in modulating actin-based shape. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. +Q9DCK3 TSN4_MOUSE Tetraspanin-4 (Tspan-4) (Transmembrane 4 superfamily member 7) 238 26,054 Chain (1); Glycosylation (2); Topological domain (5); Transmembrane (4) TRANSMEM 14 34 Helical. {ECO:0000255}.; TRANSMEM 56 76 Helical. {ECO:0000255}.; TRANSMEM 86 106 Helical. {ECO:0000255}.; TRANSMEM 202 222 Helical. {ECO:0000255}. TOPO_DOM 1 13 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 35 55 Extracellular. {ECO:0000255}.; TOPO_DOM 77 85 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 107 201 Extracellular. {ECO:0000255}.; TOPO_DOM 223 238 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SUBUNIT: Forms a complex with integrins. {ECO:0000250}. +O09117 SYPL1_MOUSE Synaptophysin-like protein 1 (Pantophysin) 261 28,899 Alternative sequence (1); Chain (1); Domain (1); Erroneous initiation (1); Glycosylation (3); Sequence conflict (2); Topological domain (5); Transmembrane (4) TRANSMEM 34 54 Helical. {ECO:0000255}.; TRANSMEM 118 138 Helical. {ECO:0000255}.; TRANSMEM 152 172 Helical. {ECO:0000255}.; TRANSMEM 215 235 Helical. {ECO:0000255}. TOPO_DOM 1 33 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 55 117 Vesicular. {ECO:0000255}.; TOPO_DOM 139 151 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 173 214 Vesicular. {ECO:0000255}.; TOPO_DOM 236 261 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:8707851}; Multi-pass membrane protein {ECO:0000269|PubMed:8707851}. Melanosome {ECO:0000250}. Note=Cytoplasmic transport vesicles. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:8707851}. +Q8CFI5 SYPM_MOUSE Probable proline--tRNA ligase, mitochondrial (EC 6.1.1.15) (Prolyl-tRNA synthetase) (ProRS) 475 53,518 Chain (1); Sequence conflict (3); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000305}. +Q8R3G9 TSN8_MOUSE Tetraspanin-8 (Tspan-8) 235 25,582 Chain (1); Glycosylation (1); Topological domain (5); Transmembrane (4) TRANSMEM 13 33 Helical. {ECO:0000255}.; TRANSMEM 53 73 Helical. {ECO:0000255}.; TRANSMEM 85 105 Helical. {ECO:0000255}.; TRANSMEM 204 224 Helical. {ECO:0000255}. TOPO_DOM 1 12 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 34 52 Extracellular. {ECO:0000255}.; TOPO_DOM 74 84 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 106 203 Extracellular. {ECO:0000255}.; TOPO_DOM 225 235 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q62348 TSN_MOUSE Translin (EC 3.1.-.-) (Component 3 of promoter of RISC) (C3PO) (Testis/brain RNA-binding protein) (TB-RBP) 228 26,201 Beta strand (1); Chain (1); Helix (10); Modified residue (3); Region (2); Turn (2) FUNCTION: DNA-binding protein that specifically recognizes consensus sequences at the breakpoint junctions in chromosomal translocations, mostly involving immunoglobulin (Ig)/T-cell receptor gene segments. Seems to recognize single-stranded DNA ends generated by staggered breaks occurring at recombination hot spots. {ECO:0000269|PubMed:15491149}.; FUNCTION: Exhibits both single-stranded and double-stranded endoribonuclease activity. May act as an activator of RNA-induced silencing complex (RISC) by facilitating endonucleolytic cleavage of the siRNA passenger strand. {ECO:0000269|PubMed:15491149}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus. SUBUNIT: Ring-shaped heterooctamer of six TSN and two TSNAX subunits, DNA/RNA binding occurs inside the ring. {ECO:0000269|PubMed:12079346}. +Q8BLH5 TSP50_MOUSE Probable threonine protease PRSS50 (EC 3.4.25.-) (Serine protease 50) (Testis-specific protease-like protein 50) 439 48,676 Active site (3); Chain (1); Disulfide bond (4); Domain (1); Glycosylation (3); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 416 436 Helical. {ECO:0000255}. TOPO_DOM 48 415 Extracellular. {ECO:0000255}.; TOPO_DOM 437 439 Cytoplasmic. {ECO:0000255}. FUNCTION: May be involved in proteolysis through its threonine endopeptidase activity. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q9CRZ8 TSPO2_MOUSE Translocator protein 2 (Peripheral-type benzodiazepine receptor-like protein 1) 162 18,286 Chain (1); Transmembrane (5) TRANSMEM 3 23 Helical. {ECO:0000255}.; TRANSMEM 44 64 Helical. {ECO:0000255}.; TRANSMEM 79 99 Helical. {ECO:0000255}.; TRANSMEM 103 123 Helical. {ECO:0000255}.; TRANSMEM 129 149 Helical. {ECO:0000255}. FUNCTION: Binds cholesterol and mediates its redistribution during erythropoiesis which may play a role in erythrocyte maturation. {ECO:0000269|PubMed:19729679}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19729679}; Multi-pass membrane protein {ECO:0000269|PubMed:19729679}. DOMAIN: The C-terminal region mediates cholesterol-binding. TISSUE SPECIFICITY: Expressed in liver, bone marrow and spleen. In spleen, detected in red pulp but not in white pulp. {ECO:0000269|PubMed:19729679}. +Q64356 SVS6_MOUSE Seminal vesicle secretory protein 6 (SVSP99) (Seminal vesicle protein 6) (Seminal vesicle secretory protein VI) (SVS VI) 99 11,482 Chain (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted, extracellular space. TISSUE SPECIFICITY: Testis. +Q91YD4 TRPM2_MOUSE Transient receptor potential cation channel subfamily M member 2 (Long transient receptor potential channel 2) (LTrpC-2) (LTrpC2) (Transient receptor potential channel 7) (TrpC7) 1506 172,202 Chain (1); Domain (1); Motif (1); Mutagenesis (1); Sequence conflict (1); Topological domain (7); Transmembrane (6) TRANSMEM 751 771 Helical. {ECO:0000255}.; TRANSMEM 793 813 Helical. {ECO:0000255}.; TRANSMEM 870 890 Helical. {ECO:0000255}.; TRANSMEM 894 914 Helical. {ECO:0000255}.; TRANSMEM 934 954 Helical. {ECO:0000255}.; TRANSMEM 1025 1045 Helical. {ECO:0000255}. TOPO_DOM 1 750 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 772 792 Extracellular. {ECO:0000255}.; TOPO_DOM 814 869 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 891 893 Extracellular. {ECO:0000255}.; TOPO_DOM 915 933 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 955 1024 Extracellular. {ECO:0000255}.; TOPO_DOM 1046 1506 Cytoplasmic. {ECO:0000255}. FUNCTION: Nonselective, voltage-independent cation channel that mediates Na(+) and Ca(2+) influx, leading to increased cytoplasmic Ca(2+) levels (PubMed:11804595, PubMed:19454650, PubMed:21753080, PubMed:22493272). Extracellular calcium passes through the channel and increases channel activity by binding to the cytoplasmic domain and stabilizing the channel in an open conformation (By similarity). Also contributes to Ca(2+) release from intracellular stores in response to ADP-ribose (PubMed:21753080). Plays a role in numerous processes that involve signaling via intracellular Ca(2+) levels (PubMed:21753080). Besides, mediates the release of lysosomal Zn(2+) stores in response to reactive oxygen species, leading to increased cytosolic Zn(2+) levels (By similarity). Activated by moderate heat (35 to 40 degrees Celsius) (PubMed:27533035, PubMed:27562954). Activated by intracellular ADP-ribose, beta-NAD (NAD(+)) and similar compounds, and by oxidative stress caused by reactive oxygen or nitrogen species (PubMed:19454650, PubMed:21753080, PubMed:22493272). The precise physiological activators are under debate; the true, physiological activators may be ADP-ribose and ADP-ribose-2'-phosphate. Activation by ADP-ribose and beta-NAD is strongly increased by moderate heat (35 to 40 degrees Celsius) (By similarity). Likewise, reactive oxygen species lower the threshold for activation by moderate heat (37 degrees Celsius) (PubMed:22493272, PubMed:25817999). Plays a role in mediating behavorial and physiological responses to moderate heat and thereby contributes to body temperature homeostasis (PubMed:27533035, PubMed:27562954). Plays a role in insulin secretion, a process that requires increased cytoplasmic Ca(2+) levels (PubMed:20921208, PubMed:25817999). Required for normal IFNG and cytokine secretion and normal innate immune immunity in response to bacterial infection (PubMed:21709234). Required for normal phagocytosis and cytokine release by macrophages exposed to zymosan (in vitro) (PubMed:22493272). Plays a role in dendritic cell differentiation and maturation, and in dendritic cell chemotaxis via its role in regulating cytoplasmic Ca(2+) levels (PubMed:21753080). Plays a role in the regulation of the reorganization of the actin cytoskeleton and filopodia formation in response to reactive oxygen species via its function in increasing cytoplasmic Ca(2+) and Zn(2+) levels (By similarity). Confers susceptibility to cell death following oxidative stress (PubMed:25562606). {ECO:0000250|UniProtKB:O94759, ECO:0000269|PubMed:11804595, ECO:0000269|PubMed:19454650, ECO:0000269|PubMed:21753080, ECO:0000269|PubMed:22493272, ECO:0000269|PubMed:25562606, ECO:0000269|PubMed:25817999, ECO:0000269|PubMed:27533035, ECO:0000269|PubMed:27562954}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11804595, ECO:0000269|PubMed:19454650, ECO:0000269|PubMed:21753080, ECO:0000269|PubMed:22493272}; Multi-pass membrane protein {ECO:0000255}. Perikaryon {ECO:0000250|UniProtKB:E9PTA2}. Cell projection {ECO:0000250|UniProtKB:E9PTA2}. Cytoplasmic vesicle {ECO:0000269|PubMed:21753080}. Lysosome {ECO:0000269|PubMed:21753080}. Note=Detected at the cell membrane and in intracellular vesicles in cortical neurons. Detected on neuronal cell bodies and neurites (By similarity). Detected on the cell membrane in polymorphonuclear neutrophils (PubMed:21753080). Detected on cytoplasmic vesicles and lysosomes in immature bone marrow dendritic cells (PubMed:21753080). {ECO:0000250|UniProtKB:E9PTA2, ECO:0000269|PubMed:21753080}. DOMAIN: The cytosolic nudix box binds ADP-ribose and is required for channel activation by ADP-ribose. {ECO:0000250|UniProtKB:O94759}. TISSUE SPECIFICITY: Detected in the preoptic area of the hypothalamus, a brain area involved in body temperature control (PubMed:27562954). Detected in beta-cells in pancreas islets (at protein level) (PubMed:16601673, PubMed:20921208). Detected in brain cortex, striatum, hippocampus CA1, CA2 and CA3 layers, and in the Purkinje cell layer in cerebellum (PubMed:15708008). Widely expressed, with highest levels in lung, spleen, eye and brain (PubMed:11804595). Detected in dendritic cells and in polymorphonuclear neutrophils (PubMed:21753080). {ECO:0000269|PubMed:11804595, ECO:0000269|PubMed:15708008, ECO:0000269|PubMed:16601673, ECO:0000269|PubMed:20921208, ECO:0000269|PubMed:21753080, ECO:0000269|PubMed:27562954}. +Q8R4D5 TRPM8_MOUSE Transient receptor potential cation channel subfamily M member 8 (Long transient receptor potential channel 6) (LTrpC-6) (LTrpC6) (Transient receptor potential p8) (Trp-p8) 1104 127,710 Chain (1); Coiled coil (1); Glycosylation (1); Mutagenesis (6); Topological domain (7); Transmembrane (6) TRANSMEM 692 712 Helical; Name=1. {ECO:0000255}.; TRANSMEM 735 755 Helical; Name=2. {ECO:0000255}.; TRANSMEM 760 780 Helical; Name=3. {ECO:0000255}.; TRANSMEM 795 815 Helical; Name=4. {ECO:0000255}.; TRANSMEM 830 850 Helical; Name=5. {ECO:0000255}.; TRANSMEM 959 979 Helical; Name=6. {ECO:0000255}. TOPO_DOM 1 691 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 713 734 Extracellular. {ECO:0000255}.; TOPO_DOM 756 759 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 781 794 Extracellular. {ECO:0000255}.; TOPO_DOM 816 829 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 851 958 Extracellular. {ECO:0000255}.; TOPO_DOM 980 1104 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor-activated non-selective cation channel involved in detection of sensations such as coolness, by being activated by cold temperature below 25 degrees Celsius. Activated by icilin, eucalyptol, menthol, cold and modulation of intracellular pH. Involved in menthol sensation. Permeable for monovalent cations sodium, potassium, and cesium and divalent cation calcium. Temperature sensing is tightly linked to voltage-dependent gating. Activated upon depolarization, changes in temperature resulting in graded shifts of its voltage-dependent activation curves. The chemical agonists menthol functions as a gating modifier, shifting activation curves towards physiological membrane potentials. Temperature sensitivity arises from a tenfold difference in the activation energies associated with voltage-dependent opening and closing. {ECO:0000269|PubMed:11893340, ECO:0000269|PubMed:15190109}. PTM: N-glycosylation is not essential for but facilitates cell surface expression, multimerization, association with lipid rafts and ion channel activity. {ECO:0000269|PubMed:17015441, ECO:0000269|PubMed:19176480}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Membrane raft. Note=Localizes to membrane rafts but is also located in the cell membrane outside of these regions where channel response to cold is enhanced compared to membrane rafts. SUBUNIT: Interacts (via N-terminus and C-terminus domains) with TCAF1; the interaction stimulates TRPM8 channel activity. Interacts (via N-terminus and C-terminus domains) with TCAF2; the interaction inhibits TRPM8 channel activity (By similarity). Homotetramer. {ECO:0000250|UniProtKB:Q7Z2W7, ECO:0000269|PubMed:17015441}. DOMAIN: The coiled coil region is required for multimerization. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in dorsal root and trigeminal ganglia. Specifically expressed in a subset of pain- and temperature-sensing neurons. Not expressed in heavily myelinated neurons. Not expressed in neurons expressing TRPA1 or TRPV1. {ECO:0000269|PubMed:11893340, ECO:0000269|PubMed:12654248}. +Q8K3A2 TRPT1_MOUSE tRNA 2'-phosphotransferase 1 (mTPT1) (EC 2.7.1.160) 249 27,354 Chain (1); Erroneous initiation (1); Modified residue (1) FUNCTION: Catalyzes the last step of tRNA splicing, the transfer of the splice junction 2'-phosphate from ligated tRNA to NAD to produce ADP-ribose 1''-2'' cyclic phosphate. {ECO:0000269|PubMed:9826666}. +Q704Y3 TRPV1_MOUSE Transient receptor potential cation channel subfamily V member 1 (TrpV1) (Osm-9-like TRP channel 1) (OTRPC1) (Vanilloid receptor 1) 839 94,976 Alternative sequence (1); Binding site (6); Chain (1); Erroneous gene model prediction (3); Glycosylation (1); Metal binding (1); Modified residue (8); Motif (1); Mutagenesis (4); Nucleotide binding (2); Region (4); Repeat (6); Sequence conflict (1); Site (1); Topological domain (7); Transmembrane (6) TRANSMEM 434 454 Helical. {ECO:0000250|UniProtKB:O35433}.; TRANSMEM 473 498 Helical. {ECO:0000250|UniProtKB:O35433}.; TRANSMEM 512 532 Helical. {ECO:0000250|UniProtKB:O35433}.; TRANSMEM 537 557 Helical. {ECO:0000250|UniProtKB:O35433}.; TRANSMEM 573 600 Helical. {ECO:0000250|UniProtKB:O35433}.; TRANSMEM 659 687 Helical. {ECO:0000250|UniProtKB:O35433}. TOPO_DOM 1 433 Cytoplasmic. {ECO:0000250|UniProtKB:O35433}.; TOPO_DOM 455 472 Extracellular. {ECO:0000250|UniProtKB:O35433}.; TOPO_DOM 499 511 Cytoplasmic. {ECO:0000250|UniProtKB:O35433}.; TOPO_DOM 533 536 Extracellular. {ECO:0000250|UniProtKB:O35433}.; TOPO_DOM 558 572 Cytoplasmic. {ECO:0000250|UniProtKB:O35433}.; TOPO_DOM 601 658 Extracellular. {ECO:0000250|UniProtKB:O35433}.; TOPO_DOM 688 839 Cytoplasmic. {ECO:0000250|UniProtKB:O35433}. FUNCTION: Ligand-activated non-selective calcium permeant cation channel involved in detection of noxious chemical and thermal stimuli (PubMed:15194687, PubMed:15489017). Seems to mediate proton influx and may be involved in intracellular acidosis in nociceptive neurons. Involved in mediation of inflammatory pain and hyperalgesia (PubMed:10764638). Sensitized by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases, which involves PKC isozymes and PCL. Activation by vanilloids, like capsaicin, and temperatures higher than 42 degrees Celsius, exhibits a time- and Ca(2+)-dependent outward rectification, followed by a long-lasting refractory state. Mild extracellular acidic pH (6.5) potentiates channel activation by noxious heat and vanilloids, whereas acidic conditions (pH <6) directly activate the channel. Can be activated by endogenous compounds, including 12-hydroperoxytetraenoic acid and bradykinin. Acts as ionotropic endocannabinoid receptor with central neuromodulatory effects. Triggers a form of long-term depression (TRPV1-LTD) mediated by the endocannabinoid anandamine in the hippocampus and nucleus accumbens by affecting AMPA receptors endocytosis (By similarity). {ECO:0000250|UniProtKB:O35433, ECO:0000269|PubMed:10764638, ECO:0000269|PubMed:15194687, ECO:0000269|PubMed:15489017}. PTM: Phosphorylation by PKA reverses capsaicin-induced dephosphorylation at multiple sites probably including Ser-117 as a major phosphorylation site. Phosphorylation by CAMKII seems to regulate binding to vanilloids. Phosphorylated and modulated by PRKCE, PRKCM and probably PRKCZ. Dephosphorylation by calcineurin seems to lead to receptor desensitization and phosphorylation by CAMKII recovers activity. {ECO:0000250|UniProtKB:O35433}. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane {ECO:0000250|UniProtKB:O35433}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O35433}. Cell projection, dendritic spine membrane {ECO:0000250|UniProtKB:O35433}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O35433}. Cell membrane {ECO:0000250|UniProtKB:O35433}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O35433}. Note=Mostly, but not exclusively expressed in postsynaptic dendritic spines. {ECO:0000250|UniProtKB:O35433}. SUBUNIT: Homotetramer. May also form a heteromeric channel with TRPV3 (By similarity). Interacts with CALM, PRKCM and CSK (By similarity). Interacts with PRKCG and NTRK1, probably by forming a trimeric complex (By similarity). Interacts with PIRT (PubMed:18455988). Interacts with the Scolopendra mutilans RhTx toxin (PubMed:26420335). Interacts with TMEM100 (PubMed:25640077). Interacts with PACS2 (By similarity). {ECO:0000250|UniProtKB:O35433, ECO:0000250|UniProtKB:Q8NER1, ECO:0000269|PubMed:18455988, ECO:0000269|PubMed:25640077, ECO:0000269|PubMed:26420335}. DOMAIN: The association domain (AD) is necessary for self-association. {ECO:0000250}. TISSUE SPECIFICITY: Detected in neurons in the root ganglia (at protein level). Detected in dorsal root ganglia. {ECO:0000269|PubMed:10764638}. +Q68FL6 SYMC_MOUSE Methionine--tRNA ligase, cytoplasmic (EC 6.1.1.10) (Methionyl-tRNA synthetase) (MetRS) 902 101,431 Binding site (1); Chain (1); Domain (2); Modified residue (2); Motif (2) FUNCTION: Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA. {ECO:0000250|UniProtKB:P56192}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P56192}. SUBUNIT: Monomer. Part of a multisubunit complex that groups tRNA ligases for Arg (RARS), Asp (DARS), Gln (QARS), Ile (IARS), Leu (LARS), Lys (KARS), Met (MARS) the bifunctional ligase for Glu and Pro (EPRS) and the auxiliary subunits AIMP1/p43, AIMP2/p38 and EEF1E1/p18. Forms a linear complex that contains MARS, EEF1E1, EPRS and AIMP2 that is at the core of the multisubunit complex. {ECO:0000269|PubMed:12060739}. +Q80X82 SYMPK_MOUSE Symplekin 1284 142,284 Chain (1); Cross-link (4); Modified residue (7); Motif (1); Region (1); Repeat (5) FUNCTION: Scaffold protein that functions as a component of a multimolecular complex involved in histone mRNA 3'-end processing. Specific component of the tight junction (TJ) plaque, but might not be an exclusively junctional component. May have a house-keeping rule. Is involved in pre-mRNA polyadenylation. Enhances SSU72 phosphatase activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell junction, tight junction {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell junction {ECO:0000250|UniProtKB:Q92797}. Nucleus, nucleoplasm {ECO:0000250}. Note=Cytoplasmic face of adhesion plaques (major) and nucleoplasm (minor) (in cells with TJ). Nucleoplasm (in cells without TJ). Nuclear bodies of heat-stressed cells. Colocalizes with HSF1 in nuclear stress bodies upon heat shock. {ECO:0000250|UniProtKB:Q92797}. SUBUNIT: Found in a heat-sensitive complex at least composed of several cleavage and polyadenylation specific and cleavage stimulation factors. Interacts with CPSF2, CPSF3 and CSTF2. Interacts (via N-terminus) with HSF1; this interaction is direct and occurs upon heat shock. Interacts with SSU72. {ECO:0000250|UniProtKB:Q92797}. DOMAIN: The HEAT repeats have been determined based on 3D-structure analysis of the D.melanogaster ortholog and are not detected by sequence-based prediction programs. +Q80VC6 TSAP1_MOUSE tRNA selenocysteine 1-associated protein 1 (SECp43) (tRNA selenocysteine-associated protein 1) 287 32,423 Chain (1); Compositional bias (1); Domain (2); Sequence conflict (1) FUNCTION: Involved in the early steps of selenocysteine biosynthesis and tRNA(Sec) charging to the later steps resulting in the cotranslational incorporation of selenocysteine into selenoproteins. Stabilizes the SECISBP2, EEFSEC and tRNA(Sec) complex. May be involved in the methylation of tRNA(Sec). Enhances efficiency of selenoproteins synthesis. {ECO:0000269|PubMed:16230358, ECO:0000269|PubMed:16508009}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Abundant in the nucleus. {ECO:0000250}. SUBUNIT: Found in a complex with tRNA(Sec) (By similarity). Interacts with SEPSECS (By similarity). Component of the tRNA(Sec) complex composed at least of EEFSEC, SECISBP2, SEPHS1, SEPSECS, TRNAU1AP and tRNA(Sec). Associates with mRNP and/or polysomes. {ECO:0000250, ECO:0000269|PubMed:16230358, ECO:0000269|PubMed:16508009}. +Q64332 SYN2_MOUSE Synapsin-2 (Synapsin II) 586 63,373 Alternative sequence (2); Chain (1); Compositional bias (2); Modified residue (3); Region (6) FUNCTION: Neuronal phosphoprotein that coats synaptic vesicles, binds to the cytoskeleton, and is believed to function in the regulation of neurotransmitter release. May play a role in noradrenaline secretion by sympathetic neurons. {ECO:0000269|PubMed:22673524}. PTM: Phosphorylation at Ser-10 dissociates synapsins from synaptic vesicles (By similarity). Phosphorylation at Ser-426 by MAPK1/ERK2 and/or MAPK3/ERK1 may play a role in noradrenaline secretion by sympathetic neurons. {ECO:0000250, ECO:0000269|PubMed:22673524}. SUBCELLULAR LOCATION: Cell junction, synapse. SUBUNIT: Interacts with CAPON. {ECO:0000250}. DOMAIN: The A region binds phospholipids with a preference for negatively charged species. {ECO:0000250}. TISSUE SPECIFICITY: Expressed exclusively in neuronal cells. Isoform IIb is enriched in sympathetic cervical ganglion. {ECO:0000269|PubMed:8034599}. +Q8JZP2 SYN3_MOUSE Synapsin-3 (Synapsin III) 579 63,315 Chain (1); Modified residue (8); Region (5); Sequence conflict (2) FUNCTION: May be involved in the regulation of neurotransmitter release and synaptogenesis. Binds ATP with high affinity and ADP with a lower affinity. This is consistent with a catalytic role of the C-domain in which ADP would be dissociated by cellular ATP after bound ATP was hydrolyzed (By similarity). {ECO:0000250}. PTM: Phosphorylation at Ser-9 dissociates synapsins from synaptic vesicles. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Peripheral membrane protein localized to the cytoplasmic surface of synaptic vesicles. {ECO:0000250}. SUBUNIT: Interacts with CAPON. {ECO:0000250}. DOMAIN: The A region binds phospholipids with a preference for negatively charged species. {ECO:0000250}. +Q5G5D5 SYNA_MOUSE Syncytin-A [Cleaved into: Surface protein (SU); Transmembrane protein (TM)] 617 68,657 Chain (3); Disulfide bond (3); Glycosylation (3); Motif (2); Mutagenesis (1); Region (1); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 545 565 Helical. {ECO:0000255}. TOPO_DOM 18 544 Extracellular. {ECO:0000305}.; TOPO_DOM 566 617 Cytoplasmic. {ECO:0000305}. FUNCTION: This endogenous retroviral envelope protein has retained its original fusogenic properties (PubMed:15644441, PubMed:17762178, PubMed:18077339, PubMed:19564597, PubMed:27589388). Together with Synb, participates in trophoblast fusion and the formation of a syncytium during placenta morphogenesis (PubMed:19564597). Syna is essential for placental development and is specifically required for formation of syncytiotrophoblast layer I (SynT-I) (PubMed:19564597). Promotes muscle myoblast fusion (PubMed:27589388). Does not have immunosuppressive activity (PubMed:18077339). {ECO:0000269|PubMed:15644441, ECO:0000269|PubMed:17762178, ECO:0000269|PubMed:18077339, ECO:0000269|PubMed:19564597, ECO:0000269|PubMed:27589388}. PTM: Synthesized as a inactive precursor that is heavily N-glycosylated and processed likely by furin in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires the minimal sequence [KR]-X-[KR]-R. {ECO:0000250|UniProtKB:Q9UQF0}.; PTM: The CXXC motif is highly conserved across a broad range of retroviral envelope proteins. It is thought to participate in the formation of a labile disulfide bond possibly with the CX6CC motif present in the transmembrane protein. Isomerization of the intersubunit disulfide bond to an SU intrachain disulfide bond is thought to occur upon receptor recognition in order to allow membrane fusion. {ECO:0000250|UniProtKB:Q9UQF0}. SUBCELLULAR LOCATION: Transmembrane protein: Cell membrane {ECO:0000305|PubMed:17762178}; Single-pass membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: Surface protein: Cell membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=The surface protein is not anchored to the membrane, but localizes to the extracellular surface through its binding to TM. {ECO:0000250|UniProtKB:Q9UQF0}. SUBUNIT: The mature protein consists of a trimer of SU-TM heterodimers (Probable). The SU-TM heterodimers are attached by a labile interchain disulfide bond (By similarity). {ECO:0000250|UniProtKB:Q9UQF0, ECO:0000305|PubMed:17105734}. TISSUE SPECIFICITY: Highly expressed in placenta where it localizes to syncytiotrophoblasts of the labyrinthine zona (PubMed:15644441). Specifically localizes to syncytiotrophoblast layer I (SynT-I) (PubMed:18448564). Also detected at very low levels in hippocampus, brain, testis and ovary (PubMed:15644441). {ECO:0000269|PubMed:15644441}. +Q8BI41 SYNB_MOUSE Syncytin-B [Cleaved into: Surface protein (SU); Transmembrane protein (TM)] 618 69,514 Chain (3); Disulfide bond (3); Glycosylation (4); Motif (2); Mutagenesis (1); Region (2); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 546 566 Helical. {ECO:0000255}. TOPO_DOM 18 545 Extracellular. {ECO:0000305}.; TOPO_DOM 567 618 Cytoplasmic. {ECO:0000305}. FUNCTION: This endogenous retroviral envelope protein has retained its original fusogenic properties (PubMed:15644441, PubMed:18077339, PubMed:22032925, PubMed:27589388). Together with Syna, participates in trophoblast fusion and the formation of a syncytium during placenta morphogenesis (PubMed:22032925). Synb is specifically involved in formation of syncytiotrophoblast layer II (SynT-II) (PubMed:22032925). Promotes myoblast fusion, and may play a role in regeneration of damaged muscle tissue in males (PubMed:27589388). May have immunosuppressive activity (PubMed:18077339). {ECO:0000269|PubMed:15644441, ECO:0000269|PubMed:18077339, ECO:0000269|PubMed:22032925}. PTM: Synthesized as a inactive precursor that is heavily N-glycosylated and processed likely by furin in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires the minimal sequence [KR]-X-[KR]-R. {ECO:0000250|UniProtKB:Q9UQF0}.; PTM: The CXXC motif is highly conserved across a broad range of retroviral envelope proteins. It is thought to participate in the formation of a labile disulfide bond possibly with the CX6CC motif present in the transmembrane protein. Isomerization of the intersubunit disulfide bond to an SU intrachain disulfide bond is thought to occur upon receptor recognition in order to allow membrane fusion. {ECO:0000250|UniProtKB:Q9UQF0}. SUBCELLULAR LOCATION: Surface protein: Cell membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=The surface protein is not anchored to the membrane, but localizes to the extracellular surface through its binding to TM. {ECO:0000250|UniProtKB:Q9UQF0}.; SUBCELLULAR LOCATION: Transmembrane protein: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000255}. SUBUNIT: The mature protein consists of a trimer of SU-TM heterodimers (Probable). The SU-TM heterodimers are attached by a labile interchain disulfide bond (By similarity). {ECO:0000250|UniProtKB:Q9UQF0, ECO:0000305}. TISSUE SPECIFICITY: Highly expressed in placenta where it localizes to syncytiotrophoblasts of the labyrinthine zona (PubMed:15644441). Specifically localizes to syncytiotrophoblast layer II (SynT-II) (PubMed:18448564). Also detected at very low levels in ovary (PubMed:15644441). {ECO:0000269|PubMed:15644441, ECO:0000269|PubMed:18448564}. +Q9EP53 TSC1_MOUSE Hamartin (Tuberous sclerosis 1 protein homolog) 1161 128,746 Alternative sequence (3); Chain (1); Coiled coil (3); Compositional bias (4); Modified residue (7); Region (1) FUNCTION: In complex with TSC2, inhibits the nutrient-mediated or growth factor-stimulated phosphorylation of S6K1 and EIF4EBP1 by negatively regulating mTORC1 signaling (By similarity). Implicated as a tumor suppressor. Involved in microtubule-mediated protein transport, but this seems to be due to unregulated mTOR signaling (PubMed:16707451). Acts as a co-chaperone for HSP90AA1 facilitating HSP90AA1 chaperoning of protein clients such as kinases, TSC2 and glucocorticoid receptor NR3C1 (PubMed:29127155). Increases ATP binding to HSP90AA1 and inhibits HSP90AA1 ATPase activity (PubMed:29127155). Competes with the activating co-chaperone AHSA1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins (By similarity). Recruits TSC2 to HSP90AA1 and stabilizes TSC2 by preventing the interaction between TSC2 and ubiquitin ligase HERC1 (By similarity). {ECO:0000250|UniProtKB:Q92574, ECO:0000269|PubMed:16707451, ECO:0000269|PubMed:29127155}. PTM: Phosphorylation at Ser-502 does not affect interaction with TSC2. {ECO:0000250|UniProtKB:Q92574}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q92574}. Membrane {ECO:0000250|UniProtKB:Q92574}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q92574}. Note=At steady state found in association with membranes. {ECO:0000250|UniProtKB:Q92574}. SUBUNIT: Probably forms a complex composed of chaperones HSP90 and HSP70, co-chaperones STIP1/HOP, CDC37, PPP5C, PTGES3/p23, TSC1 and client protein TSC2 (By similarity). Forms a complex composed of chaperones HSP90 and HSP70, co-chaperones CDC37, PPP5C, TSC1 and client protein TSC2, CDK4, AKT, RAF1 and NR3C1; this complex does not contain co-chaperones STIP1/HOP and PTGES3/p23 (By similarity). Forms a complex containing HSP90AA1, TSC1 and TSC2; TSC1 is required to recruit TCS2 to the complex (By similarity). Interacts (via C-terminus) with the closed form of HSP90AA1 (via the middle domain and TPR repeat-binding motif) (PubMed:29127155). Interacts with TSC2; the interaction stabilizes TSC2 and prevents TSC2 self-aggregation (By similarity). Interacts with DOCK7 (By similarity). Interacts with FBXW5 (By similarity). Interacts with TBC1D7 (By similarity). Interacts with WDR45B (By similarity). {ECO:0000250|UniProtKB:Q92574, ECO:0000269|PubMed:29127155}. DOMAIN: The putative coiled-coil domain is necessary for interaction with TSC2. {ECO:0000250|UniProtKB:Q92574}. +Q8BP47 SYNC_MOUSE Asparagine--tRNA ligase, cytoplasmic (EC 6.1.1.22) (Asparaginyl-tRNA synthetase) (AsnRS) 559 64,279 Chain (1); Erroneous initiation (2); Modified residue (4); Sequence conflict (5) SUBCELLULAR LOCATION: Cytoplasm. +Q9D2G5 SYNJ2_MOUSE Synaptojanin-2 (EC 3.1.3.36) (Synaptic inositol 1,4,5-trisphosphate 5-phosphatase 2) 1434 158,480 Alternative sequence (8); Chain (1); Compositional bias (1); Domain (2); Erroneous initiation (1); Frameshift (1); Modified residue (1); Natural variant (5); Region (1); Sequence caution (1); Sequence conflict (2) FUNCTION: Inositol 5-phosphatase which may be involved in distinct membrane trafficking and signal transduction pathways. May mediate the inhibitory effect of Rac1 on endocytosis (By similarity). {ECO:0000250, ECO:0000269|PubMed:9442075}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O55207}. Cell membrane {ECO:0000250|UniProtKB:O55207}. Cell projection, axon {ECO:0000250|UniProtKB:O55207}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O55207}. Membrane raft {ECO:0000250|UniProtKB:O55207}. Note=Localizes at nerve terminals in brain and at bundles of microtubules surrounding the nucleus in the elongating spermatids corresponding to the manchette. Translocates from the cytoplasm to membrane ruffles in a RAC1-dependent manner. {ECO:0000250|UniProtKB:O55207}. SUBUNIT: Binds GRB2 and OMP25. {ECO:0000250}. DOMAIN: The C-terminal proline-rich region mediates binding to the SH3 domain-containing protein GRB2. TISSUE SPECIFICITY: Ubiquitously expressed, with the highest levels in heart and brain. Detected in cortex, cerebellum and olfactory bulb. Expressed in the testis. {ECO:0000269|PubMed:15722415, ECO:0000269|PubMed:9442075}. +Q8BGV0 SYNM_MOUSE Probable asparagine--tRNA ligase, mitochondrial (EC 6.1.1.22) (Asparaginyl-tRNA synthetase) (AsnRS) 477 53,962 Chain (1); Modified residue (1); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:Q96I59}. Mitochondrion {ECO:0000250|UniProtKB:Q96I59}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q96I59}. TISSUE SPECIFICITY: Expressed in brain and inner ear, including the cochlear epithelium and organ of Corti. {ECO:0000269|PubMed:25807530}. +Q4FZC9 SYNE3_MOUSE Nesprin-3 (KASH domain-containing protein 3) (KASH3) (Nuclear envelope spectrin repeat protein 3) 975 112,035 Alternative sequence (2); Chain (1); Disulfide bond (2); Domain (1); Frameshift (1); Repeat (2); Topological domain (2); Transmembrane (1) TRANSMEM 926 946 Helical; Anchor for type IV membrane protein. {ECO:0000255|PROSITE-ProRule:PRU00385}. TOPO_DOM 1 925 Cytoplasmic. {ECO:0000255|PROSITE-ProRule:PRU00385}.; TOPO_DOM 947 975 Perinuclear space. {ECO:0000255|PROSITE-ProRule:PRU00385}. FUNCTION: As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning. Probable anchoring protein which tethers the nucleus to the cytoskeleton by binding PLEC which can associate with the intermediate filament system. Plays a role in the regulation of aortic epithelial cell morphology, and is required for flow-induced centrosome polarization and directional migration in aortic endothelial cells (By similarity). {ECO:0000250, ECO:0000269|PubMed:16330710}. PTM: The disulfid bond with SUN1 or SUN2 is required for stability of the respective LINC complex under tensile forces. {ECO:0000250|UniProtKB:Q8WXH0}. SUBCELLULAR LOCATION: Nucleus outer membrane; Single-pass type IV membrane protein. Nucleus envelope. Rough endoplasmic reticulum. SUBUNIT: Core component of LINC complexes which are composed of inner nuclear membrane SUN domain-containing proteins coupled to outer nuclear membrane KASH domain-containing nesprins. SUN and KASH domain-containing proteins seem to bind each other promiscuously; however, differentially expression of LINC complex constituents can give rise to specific assemblies. Interacts with SUN1 and SUN2; probably forming respective LINC complexes. Interacts with PLEC (via actin-binding domain). Interacts with DST. Interacts with SYNE1. Interacts (via KASH domain) with TOR1A (ATP-bound); the interaction is required for SYNE3 nuclear envelope localization. {ECO:0000269|PubMed:16330710, ECO:0000269|PubMed:18638474, ECO:0000269|PubMed:18827015, ECO:0000269|PubMed:22518138}. DOMAIN: The KASH domain is involved in the binding to SUN1 and SUN2 through recognition of their SUN domains. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:16330710}. +J3S6Y1 TSEAR_MOUSE Thrombospondin-type laminin G domain and EAR repeat-containing protein (TSP-EAR) 670 75,098 Alternative sequence (3); Chain (1); Domain (1); Erroneous initiation (1); Glycosylation (1); Repeat (7); Sequence conflict (1); Signal peptide (1) FUNCTION: May play a role in development or function of the auditory system. {ECO:0000250|UniProtKB:Q8WU66}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22678063}. Cell surface {ECO:0000269|PubMed:22678063}. Cell projection, stereocilium {ECO:0000269|PubMed:22678063}. Note=Secreted protein which may bind to the cell surface via a membrane receptor. {ECO:0000269|PubMed:22678063}. TISSUE SPECIFICITY: In the organ of Corti, expression at postnatal day 1 (P1) is restricted to the basal region of the stereocilia of inner and outer hair cells (at protein level). Expressed in the organ of Corti at P1 and P7, in cochlear ganglion, stria vascularis and vestibular ends at P7, and in inferior colliculus, remaining brainstem, cerebellum, brain hemispheres and retina at P1, P7 and in the adult. Also detected in adult liver, lung, kidney, intestine and testis but not in heart or skeletal muscle. {ECO:0000269|PubMed:22678063}. +Q8BGN8 SYNPR_MOUSE Synaptoporin 265 29,228 Alternative sequence (1); Chain (1); Domain (1); Glycosylation (2); Modified residue (1); Region (1); Repeat (5); Sequence conflict (1); Topological domain (5); Transmembrane (4) TRANSMEM 5 25 Helical. {ECO:0000255}.; TRANSMEM 82 102 Helical. {ECO:0000255}.; TRANSMEM 115 135 Helical. {ECO:0000255}.; TRANSMEM 178 198 Helical. {ECO:0000255}. TOPO_DOM 1 4 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 26 81 Vesicular. {ECO:0000255}.; TOPO_DOM 103 114 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 136 177 Vesicular. {ECO:0000255}.; TOPO_DOM 199 265 Cytoplasmic. {ECO:0000255}. FUNCTION: Intrinsic membrane protein of small synaptic vesicles. Probable vesicular channel protein (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell junction, synapse, synaptosome {ECO:0000250}. +O54887 TSKS_MOUSE Testis-specific serine kinase substrate (Testis-specific kinase substrate) (STK22 substrate 1) 585 63,505 Chain (1); Frameshift (1); Modified residue (3); Sequence conflict (4) FUNCTION: May play a role in testicular physiology, most probably in the process of spermatogenesis or spermatid development. PTM: Phosphorylated on serine residue(s) by STK22A/TSSK1 and STK22B/TSSK2. {ECO:0000269|PubMed:18533145, ECO:0000269|PubMed:9412477}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Cytoplasmic vesicle, secretory vesicle, acrosome. Note=Concentrates in spermatid centrioles during flagellogenesis. Associates with acrosomal vesicle in sperm. In elongating spermatids, accumulates in a ring-shaped structure originating from the chromatoid body. TISSUE SPECIFICITY: Testis specific. {ECO:0000269|PubMed:9412477}. +Q8CBR6 TSK_MOUSE Tsukushin (Tsukushi) (Leucine-rich repeat-containing protein 54) 354 38,362 Chain (1); Domain (1); Erroneous initiation (2); Glycosylation (3); Repeat (10); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q9JIE6 TSLP_MOUSE Thymic stromal lymphopoietin (Thymic stroma-derived lymphopoietin) 140 16,152 Chain (1); Disulfide bond (3); Glycosylation (3); Helix (7); Signal peptide (1); Site (1) FUNCTION: Cytokine that induces the release of T-cell-attracting chemokines from monocytes and, in particular, enhances the maturation of CD11c(+) dendritic cells. Can induce allergic inflammation by directly activating mast cells (By similarity). {ECO:0000250, ECO:0000269|PubMed:10974033}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10974033}. SUBUNIT: Interacts with a receptor composed of CRLF2 and IL7R. Binding of TSLP to CRLF2/TSLPR is a mechanistic prerequisite for recruitment of IL7R to the high-affinity ternary complex. {ECO:0000269|PubMed:24632570}. +Q8VCF5 TSN10_MOUSE Tetraspanin-10 (Tspan-10) (Oculospanin) 331 35,182 Chain (1); Glycosylation (1); Topological domain (4); Transmembrane (3) TRANSMEM 77 97 Helical. {ECO:0000255}.; TRANSMEM 121 141 Helical. {ECO:0000255}.; TRANSMEM 153 173 Helical. {ECO:0000255}. TOPO_DOM 1 76 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 98 120 Extracellular. {ECO:0000305}.; TOPO_DOM 142 152 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 174 331 Extracellular. {ECO:0000305}. FUNCTION: Regulates maturation of the transmembrane metalloprotease ADAM10. {ECO:0000269|PubMed:23035126}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Interacts with ADAM10. {ECO:0000269|PubMed:23035126, ECO:0000269|PubMed:26668317}. +Q8BKT6 TSN12_MOUSE Tetraspanin-12 (Tspan-12) (Transmembrane 4 superfamily member 12) 305 35,408 Alternative sequence (1); Chain (1); Lipidation (3); Sequence conflict (1); Topological domain (5); Transmembrane (4) TRANSMEM 13 33 Helical. {ECO:0000255}.; TRANSMEM 60 80 Helical. {ECO:0000255}.; TRANSMEM 90 110 Helical. {ECO:0000255}.; TRANSMEM 225 245 Helical. {ECO:0000255}. TOPO_DOM 1 12 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 34 59 Extracellular. {ECO:0000255}.; TOPO_DOM 81 89 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 111 224 Extracellular. {ECO:0000255}.; TOPO_DOM 246 305 Cytoplasmic. {ECO:0000255}. FUNCTION: Regulator of cell surface receptor signal transduction. Acts as a regulator of membrane proteinases such as ADAM10 and MMP14/MT1-MMP. Activates ADAM10-dependent cleavage activity of amyloid precursor protein (APP). Activates MMP14/MT1-MMP-dependent cleavage activity (By similarity). Plays a central role in retinal vascularization by regulating norrin (NDP) signal transduction. Acts in concert with norrin (NDP) to promote FZD4 multimerization and subsequent activation of FZD4, leading to promote accumulation of beta-catenin (CTNNB1) and stimulate LEF/TCF-mediated transcriptional programs. Suprisingly, it only activate the norrin (NDP)-dependent activation of FZD4, while it does not activate the Wnt-dependent activation of FZD4, suggesting the existence of a Wnt-independent signaling that also promote accumulation the beta-catenin (CTNNB1). {ECO:0000250, ECO:0000269|PubMed:19837033}. PTM: Palmitoylated; required for interaction with ADAM10. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:19837033}; Multi-pass membrane protein {ECO:0000305|PubMed:19837033}. SUBUNIT: Interacts (when palmitoylated) with ADAM10. Interacts with MMP14/MT1-MMP (By similarity). Component of a complex, at least composed of TSPAN12, FZD4 and norrin (NDP). {ECO:0000250, ECO:0000269|PubMed:19837033}. TISSUE SPECIFICITY: Expressed in the neonatal retinal vasculature but not other retinal tissues. Also detected in the neonatal meningeal vasculature and in nonvascular cell types, such as the smooth muscle cells in the neonatal intestine. {ECO:0000269|PubMed:19837033}. +Q9D8C2 TSN13_MOUSE Tetraspanin-13 (Tspan-13) (Transmembrane 4 superfamily member 13) 204 22,219 Chain (1); Glycosylation (2); Modified residue (1); Sequence conflict (2); Topological domain (5); Transmembrane (4) TRANSMEM 20 40 Helical. {ECO:0000255}.; TRANSMEM 45 65 Helical. {ECO:0000255}.; TRANSMEM 73 93 Helical. {ECO:0000255}.; TRANSMEM 168 188 Helical. {ECO:0000255}. TOPO_DOM 1 19 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 41 44 Extracellular. {ECO:0000255}.; TOPO_DOM 66 72 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 94 167 Extracellular. {ECO:0000255}.; TOPO_DOM 189 204 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +F7BWT7 TSN15_MOUSE Tetraspanin-15 (Tspan-15) (Transmembrane 4 superfamily member 15) 294 33,071 Alternative sequence (1); Chain (1); Erroneous initiation (1); Glycosylation (3); Sequence conflict (2); Topological domain (5); Transmembrane (4) TRANSMEM 24 44 Helical. {ECO:0000255}.; TRANSMEM 63 83 Helical. {ECO:0000255}.; TRANSMEM 95 115 Helical. {ECO:0000255}.; TRANSMEM 236 256 Helical. {ECO:0000255}. TOPO_DOM 1 23 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 45 62 Extracellular. {ECO:0000255}.; TOPO_DOM 84 94 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 116 235 Extracellular. {ECO:0000255}.; TOPO_DOM 257 294 Cytoplasmic. {ECO:0000255}. FUNCTION: Regulates maturation and trafficking of the transmembrane metalloprotease ADAM10 (PubMed:23035126, PubMed:26668317). Promotes ADAM10-mediated cleavage of (CDH2) (PubMed:26668317). Negatively regulates ligand-induced Notch activity probably by regulating ADAM10 activity (By similarity). {ECO:0000250|UniProtKB:O95858, ECO:0000269|PubMed:23035126, ECO:0000269|PubMed:26668317}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O95858}; Multi-pass membrane protein {ECO:0000305}. Late endosome membrane {ECO:0000250|UniProtKB:O95858}. SUBUNIT: Interacts with ADAM10; the interaction influences ADAM10 substrate specificity. {ECO:0000269|PubMed:23035126, ECO:0000269|PubMed:26668317}. +P62080 TSN5_MOUSE Tetraspanin-5 (Tspan-5) (Tetraspan NET-4) (Transmembrane 4 superfamily member 9) 268 30,337 Chain (1); Glycosylation (4); Sequence conflict (1); Topological domain (5); Transmembrane (4) TRANSMEM 18 38 Helical. {ECO:0000255}.; TRANSMEM 62 82 Helical. {ECO:0000255}.; TRANSMEM 93 113 Helical. {ECO:0000255}.; TRANSMEM 233 253 Helical. {ECO:0000255}. TOPO_DOM 1 17 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 39 61 Extracellular. {ECO:0000255}.; TOPO_DOM 83 92 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 114 232 Extracellular. {ECO:0000255}.; TOPO_DOM 254 268 Cytoplasmic. {ECO:0000255}. FUNCTION: Regulates ADAM10 maturation and trafficking to the cell surface (PubMed:23035126). Promotes ADAM10-mediated cleavage of CD44 (By similarity). {ECO:0000250|UniProtKB:P62079, ECO:0000269|PubMed:23035126}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P62079}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Interacts with ADAM10. {ECO:0000269|PubMed:23035126, ECO:0000269|PubMed:26668317}. +O89104 SYPL2_MOUSE Synaptophysin-like protein 2 (Mitsugumin-29) (Mg29) 264 29,224 Chain (1); Domain (1); Glycosylation (1); Topological domain (5); Transmembrane (4) TRANSMEM 34 54 Helical. {ECO:0000255}.; TRANSMEM 117 137 Helical. {ECO:0000255}.; TRANSMEM 151 171 Helical. {ECO:0000255}.; TRANSMEM 214 234 Helical. {ECO:0000255}. TOPO_DOM 1 33 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 55 116 Vesicular. {ECO:0000255}.; TOPO_DOM 138 150 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 172 213 Vesicular. {ECO:0000255}.; TOPO_DOM 235 264 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in communication between the T-tubular and junctional sarcoplasmic reticulum (SR) membranes. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Note=Triad junction, the junctional complex between the transverse tubule and the sarcoplasmic reticulum. TISSUE SPECIFICITY: Expressed abundantly in skeletal muscle and at lower levels in the kidney. {ECO:0000269|PubMed:9708916}. +Q62283 TSN7_MOUSE Tetraspanin-7 (Tspan-7) (Cell surface glycoprotein A15) (PE31) (TALLA homolog) (Transmembrane 4 superfamily member 2) (CD antigen CD231) 249 27,544 Chain (1); Erroneous initiation (2); Glycosylation (5); Sequence conflict (1); Topological domain (5); Transmembrane (4) TRANSMEM 17 40 Helical. {ECO:0000255}.; TRANSMEM 57 75 Helical. {ECO:0000255}.; TRANSMEM 87 112 Helical. {ECO:0000255}.; TRANSMEM 214 234 Helical. {ECO:0000255}. TOPO_DOM 1 16 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 41 56 Extracellular. {ECO:0000255}.; TOPO_DOM 76 86 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 113 213 Extracellular. {ECO:0000255}.; TOPO_DOM 235 249 Cytoplasmic. {ECO:0000255}. FUNCTION: May be involved in cell proliferation and cell motility. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. +Q8BJU2 TSN9_MOUSE Tetraspanin-9 (Tspan-9) (Tetraspan NET-5) 239 26,738 Chain (1); Glycosylation (1); Topological domain (5); Transmembrane (4) TRANSMEM 14 34 Helical. {ECO:0000255}.; TRANSMEM 56 76 Helical. {ECO:0000255}.; TRANSMEM 86 106 Helical. {ECO:0000255}.; TRANSMEM 204 224 Helical. {ECO:0000255}. TOPO_DOM 1 13 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 35 55 Extracellular. {ECO:0000255}.; TOPO_DOM 77 85 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 107 203 Extracellular. {ECO:0000255}.; TOPO_DOM 225 239 Cytoplasmic. {ECO:0000255}. PTM: Glycosylated. {ECO:0000269|PubMed:18795891}. SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:18795891}; Multi-pass membrane protein {ECO:0000305|PubMed:18795891}. Note=Colocalizes with GP6 in tetraspanin microdomains on the platelet surface. SUBUNIT: Found in a complex with GP6. {ECO:0000269|PubMed:18795891}. TISSUE SPECIFICITY: Strongly expressed in megakaryocytes, platelets and lung. Weakly expressed in bone marrow, brain and kidney (at protein level). {ECO:0000269|PubMed:18795891}. +Q9QZE7 TSNAX_MOUSE Translin-associated protein X (Translin-associated factor X) 290 32,926 Chain (1); Cross-link (1); Metal binding (2); Region (1) FUNCTION: Acts in combination with TSN as an endonuclease involved in the activation of the RNA-induced silencing complex (RISC). Possible role in spermatogenesis (By similarity). {ECO:0000250}. PTM: Sumoylated with SUMO1. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}. Golgi apparatus {ECO:0000269|PubMed:15314092}. Nucleus {ECO:0000250}. Note=Expressed in the cytoplasm in the presence of TSN (By similarity). Accumulate in the Golgi complex of mid-late pachytene spermatocytes. {ECO:0000250}. SUBUNIT: Ring-shaped heterooctamer of six TSN and two TSNAX subunits. Interacts with GOLGA3, TSNAXIP1, SUN1 and AKAP9. Interacts with the homodimeric form of C1D following gamma-radiation. Interacts with TSN and C1D in a mutually exclusive manner (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Detected in heart, brain, lung, liver, kidney and testis. {ECO:0000269|PubMed:10790540}. +Q62277 SYPH_MOUSE Synaptophysin (BM89 antigen) (Major synaptic vesicle protein p38) 314 34,025 Chain (1); Domain (1); Glycosylation (1); Modified residue (4); Region (1); Sequence conflict (1); Topological domain (5); Transmembrane (4) TRANSMEM 26 49 Helical. {ECO:0000255}.; TRANSMEM 108 131 Helical. {ECO:0000255}.; TRANSMEM 139 162 Helical. {ECO:0000255}.; TRANSMEM 201 224 Helical. {ECO:0000255}. TOPO_DOM 1 25 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 50 107 Vesicular. {ECO:0000255}.; TOPO_DOM 132 138 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 163 200 Vesicular. {ECO:0000255}.; TOPO_DOM 225 314 Cytoplasmic. {ECO:0000255}. FUNCTION: Possibly involved in structural functions as organizing other membrane components or in targeting the vesicles to the plasma membrane (By similarity). Involved in the regulation of short-term and long-term synaptic plasticity. {ECO:0000250, ECO:0000269|PubMed:10595519}. PTM: Ubiquitinated; mediated by SIAH1 or SIAH2 and leading to its subsequent proteasomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:24995978}; Multi-pass membrane protein {ECO:0000255}. Cell junction, synapse, synaptosome {ECO:0000250|UniProtKB:P08247}. SUBUNIT: Homohexamer or homotetramer. Interacts with SRCIN1 (By similarity). Interacts with VAMP2; the interaction is inhibit by interaction of VAPM2 with SEPT8 (PubMed:19196426). {ECO:0000250|UniProtKB:P08247, ECO:0000269|PubMed:19196426}. DOMAIN: The calcium-binding activity is thought to be localized in the cytoplasmic tail of the protein. +Q9D2E1 TSSK3_MOUSE Testis-specific serine/threonine-protein kinase 3 (TSK-3) (TSSK-3) (Testis-specific kinase 3) (EC 2.7.11.1) (Serine/threonine-protein kinase 22C) 268 30,209 Active site (1); Binding site (1); Chain (1); Domain (1); Frameshift (1); Nucleotide binding (1) FUNCTION: May be involved in a signaling pathway during male germ cell development or mature sperm function. PTM: Autophosphorylated. {ECO:0000250}. TISSUE SPECIFICITY: Developmentally expressed in testicular germ cells. In adult testis, expression was detected in round and condensing spermatids, but not in meiotic pachytene spermatocytes. Not expressed in brain, ovary, kidney, liver or early embryonic cells. {ECO:0000269|PubMed:10781952}. +Q8C1R0 TSSK5_MOUSE Testis-specific serine/threonine-protein kinase 5 (TSK-5) (TSSK-5) (Testis-specific kinase 5) (EC 2.7.11.1) 372 42,234 Active site (1); Binding site (1); Chain (1); Domain (1); Frameshift (1); Nucleotide binding (1) FUNCTION: May be involved in a signaling pathway during male germ cell development or mature sperm function. {ECO:0000250|UniProtKB:Q61241}. PTM: Autophosphorylated. {ECO:0000250|UniProtKB:Q9BXA7}. +Q9D0B5 TSTD3_MOUSE Thiosulfate sulfurtransferase/rhodanese-like domain-containing protein 3 (Rhodanese domain-containing protein 3) 157 17,271 Active site (1); Chain (1); Domain (1); Modified residue (1) +O88852 TSYL1_MOUSE Testis-specific Y-encoded-like protein 1 (TSPY-like protein 1) 379 42,994 Chain (1); Cross-link (1) SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9H0U9}. TISSUE SPECIFICITY: Highly expressed in testis, ovary, liver, spleen, brain, kidney, prostate, lung, and heart. Low expression in liver. {ECO:0000269|PubMed:9730615}. +Q7TQI8 TSYL2_MOUSE Testis-specific Y-encoded-like protein 2 (TSPY-like protein 2) (CASK-interacting nucleosome assembly protein) (Differentially-expressed nucleolar TGF-beta1 target protein) 677 77,671 Chain (1); Compositional bias (4); Cross-link (3); Modified residue (5); Sequence conflict (7) FUNCTION: Part of the CASK/TBR1/TSPYL2 transcriptional complex which modulates gene expression in response to neuronal synaptic activity, probably by facilitating nucleosome assembly. May inhibit cell proliferation by inducing p53-dependent CDKN1A expression. {ECO:0000269|PubMed:15066269}. PTM: Phosphorylation at Thr-333 impairs function on cell proliferation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Enriched in transcriptionally active regions of chromatin in neurons. SUBUNIT: Interacts with histones. Interacts with CASK. Part of a complex containing CASK, TBR1 and TSPYL2. {ECO:0000269|PubMed:15066269}. TISSUE SPECIFICITY: Present at high levels in the pituitary gland and at moderate levels in adrenal gland, brain, testis and ovary. In brain, expressed both in mature neurons and progenitor cells (at protein level). {ECO:0000269|PubMed:12112471, ECO:0000269|PubMed:15241014, ECO:0000269|PubMed:16374801}. +Q8VD63 TSYL4_MOUSE Testis-specific Y-encoded-like protein 4 (TSPY-like protein 4) 406 44,811 Chain (1) +Q69ZB3 TSYL5_MOUSE Testis-specific Y-encoded-like protein 5 (TSPY-like protein 5) 406 44,303 Chain (1); Erroneous initiation (1) FUNCTION: Involved in modulation of cell growth and cellular response to gamma radiation probably via regulation of the Akt signaling pathway. Involved in regulation of p53/TP53. Suppresses p53/TP53 protein levels and promotes its ubiquitination; the function is dependent on USP7 and independent on MDM2. Proposed to displace p53/TP53 from interaction with USP7 (By similarity). {ECO:0000250}. SUBUNIT: Interacts with USP7. {ECO:0000250}. +Q9CY00 TT30B_MOUSE Tetratricopeptide repeat protein 30B (TPR repeat protein 30B) 664 76,096 Chain (1); Coiled coil (1); Compositional bias (1); Repeat (8); Sequence conflict (1) FUNCTION: Required for polyglutamylation of axonemal tubulin. Plays a role in anterograde intraflagellar transport (IFT), the process by which cilia precursors are transported from the base of the cilium to the site of their incorporation at the tip. {ECO:0000250}. SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000250}. +Q8BYY4 TT39B_MOUSE Tetratricopeptide repeat protein 39B (TPR repeat protein 39B) 617 70,293 Alternative sequence (4); Chain (1); Repeat (3) FUNCTION: Regulates high density lipoprotein (HDL) cholesterol metabolism by promoting the ubiquitination and degradation of the oxysterols receptors LXR (NR1H2 and NR1H3). {ECO:0000269|PubMed:27383786}. TISSUE SPECIFICITY: High expression in lung and spleen. Low lower expression in liver and small intestine. Weak expression in heart, brain, kidney, adipose, and adrenal gland. {ECO:0000269|PubMed:27383786}. +Q6PCN3 TTBK1_MOUSE Tau-tubulin kinase 1 (EC 2.7.11.1) 1308 141,613 Active site (1); Binding site (1); Chain (1); Compositional bias (2); Domain (1); Modified residue (2); Nucleotide binding (1) FUNCTION: Serine/threonine kinase which is able to phosphorylate TAU on serine, threonine and tyrosine residues. Induces aggregation of TAU (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the brain. Strong expression in the cortical layers, the CA1 layers of the hippocampus and the granular layer of the cerebellum. Also expressed in the large cortical pyramidal cells in the temporal cortex, the CA1 pyramidal neurons and the cerebellum granular neurons. {ECO:0000269|PubMed:16923168}. +O88196 TTC3_MOUSE E3 ubiquitin-protein ligase TTC3 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase TTC3) (TPR repeat protein D) (Mtprd) 1979 223,931 Alternative sequence (5); Chain (1); Compositional bias (3); Erroneous initiation (3); Modified residue (4); Repeat (4); Sequence caution (2); Sequence conflict (14); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that mediates the ubiquitination and subsequent degradation of phosphorylated Akt (AKT1, AKT2 and AKT3) in the nucleus. Acts as a terminal regulator of Akt signaling after activation; its phosphorylation by Akt, which is a prerequisite for ubiquitin ligase activity, suggests the existence of a regulation mechanism required to control Akt levels after activation. Catalyzes the formation of 'Lys-48'-polyubiquitin chains. May play a role in neuronal differentiation inhibition via its interaction with CIT. {ECO:0000250|UniProtKB:P53804}. PTM: Phosphorylation on Ser-378 by Akt is required for ubiquitin ligase activity. {ECO:0000250|UniProtKB:P53804}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P53804}. SUBUNIT: Interacts (when phosphorylated on Ser-378) with AKT1, AKT2 and AKT3 (when phosphorylated). Interacts with CIT. {ECO:0000250|UniProtKB:P53804}. +Q8R3H9 TTC4_MOUSE Tetratricopeptide repeat protein 4 (TPR repeat protein 4) 386 44,339 Chain (1); Modified residue (3); Repeat (3) +Q99LG4 TTC5_MOUSE Tetratricopeptide repeat protein 5 (TPR repeat protein 5) (Stress-responsive activator of p300) 440 48,795 Beta strand (9); Chain (1); Helix (21); Modified residue (2); Repeat (6); Sequence conflict (7); Turn (2) FUNCTION: Adapter protein involved in p53/TP53 response that acts by regulating and mediating the assembly of multi-protein complexes. Required to facilitate the interaction between JMY and p300/EP300 and increase p53/TP53-dependent transcription and apoptosis. Prevents p53/TP53 degradation by MDM2. {ECO:0000269|PubMed:10518217, ECO:0000269|PubMed:15448695}. PTM: Phosphorylation at Ser-203 enhances protein stability, regulates nuclear accumulation and association with p300/EP300. {ECO:0000269|PubMed:15448695, ECO:0000269|PubMed:22362889}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15448695}. Cytoplasm {ECO:0000269|PubMed:15448695}. Note=Phosphorylation at Ser-203 results in nuclear localization, while unphosphorylated protein localizes to the cytoplasm. SUBUNIT: Interacts with JMY and p300/EP300. {ECO:0000269|PubMed:10518217}. +E9Q6P5 TTC7B_MOUSE Tetratricopeptide repeat protein 7B (TPR repeat protein 7B) 843 94,203 Chain (1); Modified residue (9); Repeat (11) FUNCTION: Component of a complex required to localize phosphatidylinositol 4-kinase (PI4K) to the plasma membrane. The complex acts as a regulator of phosphatidylinositol 4-phosphate (PtdIns(4)P) synthesis. In the complex, plays a central role in bridging PI4KA to EFR3B and FAM126A, via direct interactions. {ECO:0000250|UniProtKB:Q86TV6}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q86TV6}. Cell membrane {ECO:0000250|UniProtKB:Q86TV6}. Note=Localizes to the cytosol and is recruited to the plasma membrane following interaction with EFR3 (EFR3A or EFR3B). {ECO:0000250|UniProtKB:Q86TV6}. SUBUNIT: Component of a phosphatidylinositol 4-kinase (PI4K) complex, composed of PI4KA, EFR3 (EFR3A or EFR3B), TTC7 (TTC7A or TTC7B) and FAM126 (FAM126A or FAM126B). Interacts with PI4KA, interaction is direct. Interacts with EFR3 (EFR3A or EFR3B), interaction is direct. Interacts with FAM126 (FAM126A or FAM126B), interaction is direct. Association with the PI4K complex is strongly reduced by TMEM150A. {ECO:0000250|UniProtKB:Q86TV6}. +Q8VD72 TTC8_MOUSE Tetratricopeptide repeat protein 8 (TPR repeat protein 8) (Bardet-Biedl syndrome 8 protein homolog) 515 58,440 Alternative sequence (1); Chain (1); Repeat (8) FUNCTION: The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor, which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane and binds to RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the Rab8-GTP localizes to the cilium and promotes docking and fusion of carrier vesicles to the base of the ciliary membrane. The BBSome complex, together with the LTZL1, controls SMO ciliary trafficking and contributes to the sonic hedgehog (SHH) pathway regulation. Required for proper BBSome complex assembly and its ciliary localization (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q8TAM2}. Cell projection, cilium membrane {ECO:0000250|UniProtKB:Q8TAM2}. Cytoplasm {ECO:0000250|UniProtKB:Q8TAM2}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000250|UniProtKB:Q8TAM2}. Cell projection, cilium {ECO:0000269|PubMed:25243405}. SUBUNIT: Part of BBSome complex, that contains BBS1, BBS2, BBS4, BBS5, BBS7, BBS8/TTC8, BBS9 and BBIP10. Interacts with PCM1. Interacts with CCDC28B. Interacts with PKD1. {ECO:0000250|UniProtKB:Q8TAM2, ECO:0000269|PubMed:22072986}. TISSUE SPECIFICITY: Isoform 1 is retina-specific whereas isoform 2 is ubiquitously expressed. {ECO:0000269|PubMed:20451172}. +Q5NC05 TTF2_MOUSE Transcription termination factor 2 (EC 3.6.4.-) (RNA polymerase II termination factor) (Transcription release factor 2) 1138 125,530 Chain (1); Domain (2); Modified residue (3); Motif (1); Nucleotide binding (1); Sequence conflict (10) FUNCTION: DsDNA-dependent ATPase which acts as a transcription termination factor by coupling ATP hydrolysis with removal of RNA polymerase II from the DNA template. May contribute to mitotic transcription repression. May also be involved in pre-mRNA splicing (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Cytoplasmic during interphase. Relocates to the nucleus as cells enter mitosis (By similarity). {ECO:0000250}. SUBUNIT: Interacts with CDC5L. Part of the spliceosome (By similarity). {ECO:0000250}. +Q9DA32 SUN5_MOUSE SUN domain-containing protein 5 (Sperm-associated antigen 4-like protein) 373 42,653 Alternative sequence (1); Chain (1); Coiled coil (1); Domain (1); Mutagenesis (6); Sequence conflict (6); Topological domain (2); Transmembrane (1) TRANSMEM 104 120 Helical. {ECO:0000255}. TOPO_DOM 1 103 Nuclear. {ECO:0000255}.; TOPO_DOM 121 373 Perinuclear space. {ECO:0000255}. FUNCTION: Plays an essential role in anchoring sperm head to the tail. Is responsible for the attachment of the coupling apparatus to the sperm nuclear envelope. {ECO:0000269|PubMed:28945193, ECO:0000305|PubMed:21711156}. PTM: Highly glycosylated in the Golgi apparatus during spermiogenesis. {ECO:0000269|PubMed:25775128}. SUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000269|PubMed:21159740, ECO:0000269|PubMed:25775128, ECO:0000269|PubMed:28945193, ECO:0000269|PubMed:29298896}; Single-pass membrane protein {ECO:0000269|PubMed:21159740}. Golgi apparatus {ECO:0000269|PubMed:25775128}. Note=During spermiogenesis, traffics through the Golgi apparatus before reaching the round spermatid inner membrane of the nuclear envelope and later migrates to the coupling apparatus of the sperm during sperm head elongation and differentiation. In mature spermatozoa, is localized to the coupling apparatus of the sperm head and tail in the implementation fossa. {ECO:0000269|PubMed:21159740, ECO:0000269|PubMed:25775128, ECO:0000269|PubMed:28945193}. SUBUNIT: Probable homotrimer (Probable). Interacts with DNAJB13 (PubMed:29298896). {ECO:0000269|PubMed:29298896, ECO:0000305|PubMed:25775128}. TISSUE SPECIFICITY: Testis-specific, abundantly expressed in spermatocytes and round spermatids. {ECO:0000269|PubMed:15552040, ECO:0000269|PubMed:21711156}. +Q2TV84 TRPM1_MOUSE Transient receptor potential cation channel subfamily M member 1 (Long transient receptor potential channel 1) (LTrpC1) (Melastatin-1) 1622 183,527 Alternative sequence (8); Chain (1); Coiled coil (1); Sequence conflict (7); Topological domain (9); Transmembrane (8) TRANSMEM 791 811 Helical. {ECO:0000255}.; TRANSMEM 876 896 Helical. {ECO:0000255}.; TRANSMEM 898 918 Helical. {ECO:0000255}.; TRANSMEM 943 963 Helical. {ECO:0000255}.; TRANSMEM 974 994 Helical. {ECO:0000255}.; TRANSMEM 1007 1027 Helical. {ECO:0000255}.; TRANSMEM 1100 1120 Helical. {ECO:0000255}.; TRANSMEM 1151 1171 Helical. {ECO:0000255}. TOPO_DOM 1 790 Extracellular. {ECO:0000255}.; TOPO_DOM 812 875 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 897 897 Extracellular. {ECO:0000255}.; TOPO_DOM 919 942 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 964 973 Extracellular. {ECO:0000255}.; TOPO_DOM 995 1006 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1028 1099 Extracellular. {ECO:0000255}.; TOPO_DOM 1121 1150 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1172 1622 Extracellular. {ECO:0000255}. FUNCTION: Cation channel essential for the depolarizing photoresponse of retinal ON bipolar cells. It is part of the GRM6 signaling cascade. Calcium channel which may play a role in metastasis suppression. May act as a spontaneously active, calcium-permeable plasma membrane channel. {ECO:0000269|PubMed:19861548, ECO:0000269|PubMed:19966281, ECO:0000269|PubMed:9537257}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000255, ECO:0000305}; Multi-pass membrane protein {ECO:0000255, ECO:0000305}. TISSUE SPECIFICITY: Expressed in the retina where it localizes on dendritic tips of ON bipolar cells. Not detected in brain, lung, liver, heart, kidney, spleen or small intestine. Also expressed at high levels in poorly metastatic variants of B16 melanoma and at much reduced levels in highly metastatic variants of B16 melanoma. {ECO:0000269|PubMed:19861548, ECO:0000269|PubMed:19966281, ECO:0000269|PubMed:9537257}. +Q8CIR4 TRPM6_MOUSE Transient receptor potential cation channel subfamily M member 6 (EC 2.7.11.1) (Channel kinase 2) (Melastatin-related TRP cation channel 6) 2028 232,888 Active site (1); Binding site (5); Chain (1); Domain (1); Intramembrane (1); Metal binding (4); Modified residue (1); Nucleotide binding (1); Topological domain (8); Transmembrane (6) INTRAMEM 1019 1039 Pore-forming. {ECO:0000255}. TRANSMEM 748 768 Helical. {ECO:0000255}.; TRANSMEM 848 868 Helical. {ECO:0000255}.; TRANSMEM 911 931 Helical. {ECO:0000255}.; TRANSMEM 946 966 Helical. {ECO:0000255}.; TRANSMEM 979 999 Helical. {ECO:0000255}.; TRANSMEM 1054 1074 Helical. {ECO:0000255}. TOPO_DOM 1 747 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 769 847 Extracellular. {ECO:0000255}.; TOPO_DOM 869 910 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 932 945 Extracellular. {ECO:0000255}.; TOPO_DOM 967 978 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1000 1018 Extracellular. {ECO:0000255}.; TOPO_DOM 1040 1053 Extracellular. {ECO:0000255}.; TOPO_DOM 1075 2028 Cytoplasmic. {ECO:0000255}. FUNCTION: Essential ion channel and kinase. Crucial for magnesium homeostasis. Has an important role in epithelial magnesium transport and in the active magnesium absorption in the gut and kidney (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9BX84}; Multi-pass membrane protein. SUBUNIT: Forms heterodimers with TRPM7. Interacts (via kinase domain) with RACK1 (By similarity). {ECO:0000250}. +Q923J1 TRPM7_MOUSE Transient receptor potential cation channel subfamily M member 7 (EC 2.7.11.1) (Channel-kinase 1) (Long transient receptor potential channel 7) (LTrpC-7) (LTrpC7) (Transient receptor potential-phospholipase C-interacting kinase) (TRP-PLIK) 1863 212,399 Active site (1); Beta strand (26); Binding site (5); Chain (1); Coiled coil (1); Domain (1); Helix (53); Intramembrane (1); Metal binding (4); Modified residue (19); Mutagenesis (3); Nucleotide binding (1); Sequence conflict (6); Topological domain (8); Transmembrane (6); Turn (16) INTRAMEM 1036 1056 Pore-forming. {ECO:0000255}. TRANSMEM 756 776 Helical. {ECO:0000255}.; TRANSMEM 856 876 Helical. {ECO:0000255}.; TRANSMEM 919 939 Helical. {ECO:0000255}.; TRANSMEM 963 983 Helical. {ECO:0000255}.; TRANSMEM 996 1016 Helical. {ECO:0000255}.; TRANSMEM 1075 1095 Helical. {ECO:0000255}. TOPO_DOM 1 755 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 777 855 Extracellular. {ECO:0000255}.; TOPO_DOM 877 918 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 940 962 Extracellular. {ECO:0000255}.; TOPO_DOM 984 995 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1017 1035 Extracellular. {ECO:0000255}.; TOPO_DOM 1057 1074 Extracellular. {ECO:0000255}.; TOPO_DOM 1096 1863 Cytoplasmic. {ECO:0000255}. FUNCTION: Essential ion channel and serine/threonine-protein kinase. Divalent cation channel permeable to calcium and magnesium. Has a central role in magnesium ion homeostasis and in the regulation of anoxic neuronal cell death. Involved in TNF-induced necroptosis downstream of MLKL by mediating calcium influx. The kinase activity is essential for the channel function. May be involved in a fundamental process that adjusts plasma membrane divalent cation fluxes according to the metabolic state of the cell. Phosphorylates annexin A1 (ANXA1). {ECO:0000269|PubMed:11385574}. PTM: Autophosphorylated. {ECO:0000269|PubMed:11161216, ECO:0000269|PubMed:22222377}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Forms heterodimers with TRPM6. Interacts with PLCB1 (By similarity). Homodimer. {ECO:0000250, ECO:0000269|PubMed:11389851}. TISSUE SPECIFICITY: Found to be expressed in brain and skeletal muscle, with stronger signals in kidney, heart, liver and spleen. {ECO:0000269|PubMed:11161216}. +Q9D5V6 SYAP1_MOUSE Synapse-associated protein 1 (BSD domain-containing signal transducer and Akt interactor protein) (BSTA) 365 41,350 Chain (1); Domain (1); Modified residue (4); Sequence conflict (1) FUNCTION: Plays a role in adipocyte differentiation by promoting mTORC2-mediated phosphorylation of AKT1 at 'Ser-473' after growth factor stimulation (PubMed:23300339). {ECO:0000269|PubMed:23300339}. PTM: Phosphorylated (PubMed:23300339). Phosphorylation increases in a mTORC2-mediated manner in response to epidermal growth factor (EGF) stimulation (PubMed:23300339). {ECO:0000269|PubMed:23300339}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:27344443}. Golgi apparatus {ECO:0000269|PubMed:27344443}. Perikaryon {ECO:0000269|PubMed:27344443}. Cell projection, axon {ECO:0000269|PubMed:27344443}. Cell projection, dendrite {ECO:0000269|PubMed:27344443}. Cell projection, growth cone {ECO:0000269|PubMed:27344443}. Cell junction, synapse, presynaptic cell membrane {ECO:0000269|PubMed:27344443}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000269|PubMed:27344443}. Membrane {ECO:0000250|UniProtKB:Q96A49}. Note=Localizes to cholinergic neuromuscular junctions and in actin-rich growth cone regions (PubMed:27344443). Membrane-associated in a epidermal growth factor (EGF)-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q96A49, ECO:0000269|PubMed:27344443}. SUBUNIT: Interacts (via phosphorylated form and BSD domain) with AKT1; this interaction is enhanced in a mTORC2-mediated manner in response to epidermal growth factor (EGF) stimulation and activates AKT1 (PubMed:23300339). {ECO:0000269|PubMed:23300339}. TISSUE SPECIFICITY: Expressed in the liver, kidney, skeletal muscle and in white and brown adipose tissues (PubMed:23300339, PubMed:27344443). Expressed in the cortex, cerebellum, thalamus, hippocampus, braistem, olfactory bulb, spinal cord and striatum of the brain (PubMed:27344443). Expressed in most neuropil regions containing glutamatergic synaptic terminals (PubMed:27344443). Expressed in the CA1, CA2 and CA3 perikarya of the hippocampus (PubMed:27344443). Expressed in neurons and Purkinje cells (at the protein level) (PubMed:27344443). {ECO:0000269|PubMed:23300339, ECO:0000269|PubMed:27344443}. +Q8K424 TRPV3_MOUSE Transient receptor potential cation channel subfamily V member 3 (TrpV3) 791 90,663 Beta strand (2); Chain (1); Helix (16); Intramembrane (1); Repeat (3); Sequence conflict (1); Topological domain (6); Transmembrane (6); Turn (1) INTRAMEM 621 637 Pore-forming. {ECO:0000255}. TRANSMEM 440 460 Helical. {ECO:0000255}.; TRANSMEM 488 508 Helical. {ECO:0000255}.; TRANSMEM 524 544 Helical. {ECO:0000255}.; TRANSMEM 546 566 Helical. {ECO:0000255}.; TRANSMEM 590 610 Helical. {ECO:0000255}.; TRANSMEM 650 670 Helical. {ECO:0000255}. TOPO_DOM 1 439 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 461 487 Extracellular. {ECO:0000255}.; TOPO_DOM 509 523 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 545 545 Extracellular. {ECO:0000255}.; TOPO_DOM 567 589 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 671 791 Cytoplasmic. {ECO:0000255}. FUNCTION: Putative receptor-activated non-selective calcium permeant cation channel. It is activated by innocuous (warm) temperatures and shows an increased response at noxious temperatures greater than 39 degrees Celsius. Activation exhibits an outward rectification. May associate with TRPV1 and may modulate its activity. Is a negative regulator of hair growth and cycling: TRPV3-coupled signaling suppresses keratinocyte proliferation in hair follicles and induces apoptosis and premature hair follicle regression (catagen) (By similarity). {ECO:0000250, ECO:0000269|PubMed:12016205}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: May form a heteromeric channel with TRPV1. Interacts with TRPV1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in keratinocytes and hair follicles. {ECO:0000269|PubMed:12016205}. +Q91WD2 TRPV6_MOUSE Transient receptor potential cation channel subfamily V member 6 (TrpV6) (Calcium transport protein 1) (CaT1) (Epithelial calcium channel 2) (ECaC2) 767 87,387 Chain (1); Glycosylation (1); Helix (15); Intramembrane (1); Metal binding (1); Modified residue (2); Motif (1); Mutagenesis (6); Region (3); Repeat (6); Sequence caution (2); Sequence conflict (1); Topological domain (8); Transmembrane (6); Turn (1) INTRAMEM 565 584 Pore-forming. {ECO:0000250|UniProtKB:Q9R186}. TRANSMEM 367 387 Helical. {ECO:0000250|UniProtKB:Q9R186}.; TRANSMEM 425 447 Helical. {ECO:0000250|UniProtKB:Q9R186}.; TRANSMEM 463 482 Helical. {ECO:0000250|UniProtKB:Q9R186}.; TRANSMEM 489 508 Helical. {ECO:0000250|UniProtKB:Q9R186}.; TRANSMEM 529 551 Helical. {ECO:0000250|UniProtKB:Q9R186}.; TRANSMEM 596 616 Helical. {ECO:0000250|UniProtKB:Q9R186}. TOPO_DOM 1 366 Cytoplasmic. {ECO:0000250|UniProtKB:Q9R186}.; TOPO_DOM 388 424 Extracellular. {ECO:0000250|UniProtKB:Q9R186}.; TOPO_DOM 448 462 Cytoplasmic. {ECO:0000250|UniProtKB:Q9R186}.; TOPO_DOM 483 488 Extracellular. {ECO:0000250|UniProtKB:Q9R186}.; TOPO_DOM 509 528 Cytoplasmic. {ECO:0000250|UniProtKB:Q9R186}.; TOPO_DOM 552 564 Extracellular. {ECO:0000250|UniProtKB:Q9R186}.; TOPO_DOM 585 595 Extracellular. {ECO:0000250|UniProtKB:Q9R186}.; TOPO_DOM 617 767 Cytoplasmic. {ECO:0000250|UniProtKB:Q9R186}. FUNCTION: Calcium selective cation channel that mediates Ca(2+) uptake in various tissues, including the intestine (PubMed:12765696, PubMed:12601087, PubMed:12574114, PubMed:14736889, PubMed:15123711, PubMed:17129178). Important for normal Ca(2+) ion homeostasis in the body, including bone and skin (PubMed:17129178, PubMed:22878123). The channel is activated by low internal calcium level, probably including intracellular calcium store depletion, and the current exhibits an inward rectification. Inactivation includes both a rapid Ca(2+)-dependent and a slower Ca(2+)-calmodulin-dependent mechanism; the latter may be regulated by phosphorylation (PubMed:15123711). In vitro, is slowly inhibited by Mg(2+) in a voltage-independent manner (PubMed:12601087). Heteromeric assembly with TRPV5 seems to modify channel properties. TRPV5-TRPV6 heteromultimeric concatemers exhibit voltage-dependent gating (PubMed:12574114). {ECO:0000269|PubMed:12574114, ECO:0000269|PubMed:12601087, ECO:0000269|PubMed:12660155, ECO:0000269|PubMed:12765696, ECO:0000269|PubMed:14736889, ECO:0000269|PubMed:15123711, ECO:0000269|PubMed:17129178, ECO:0000269|PubMed:22878123}. PTM: Glycosylated. {ECO:0000269|PubMed:12574114, ECO:0000269|PubMed:12765696, ECO:0000269|PubMed:17129178}.; PTM: Phosphorylation at Tyr-201 and Tyr-202 by SRC leads to an increased calcium influx through the channel. Probably dephosphorylated at these sites by PTPN1 (By similarity). {ECO:0000250|UniProtKB:Q9H1D0, ECO:0000250|UniProtKB:Q9R186}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12574114, ECO:0000269|PubMed:12601087, ECO:0000269|PubMed:12660155, ECO:0000269|PubMed:12765696, ECO:0000269|PubMed:14736889}; Multi-pass membrane protein {ECO:0000269|PubMed:12660155}. SUBUNIT: Interacts with TCAF1 and TCAF2 (By similarity). Homotetramer and probably heterotetramer with TRPV5 (PubMed:12574114). Interacts with TRPV5 (PubMed:12574114). Interacts with S100A10 and probably with the ANAX2-S100A10 heterotetramer. The interaction with S100A10 is required for the trafficking to the plasma membrane (PubMed:12660155). Interacts with calmodulin (PubMed:12765696, PubMed:15123711). Interacts with BSPRY (PubMed:16380433). {ECO:0000250|UniProtKB:Q9H1D0, ECO:0000269|PubMed:12574114, ECO:0000269|PubMed:12660155, ECO:0000269|PubMed:12765696, ECO:0000269|PubMed:15123711, ECO:0000269|PubMed:16380433}. TISSUE SPECIFICITY: Detected in intestine (at protein level) (PubMed:17129178). Abundantly expressed in pancreas and placenta, and to a much lesser extent in stomach and kidney (PubMed:12765696). Detected in kidney and duodenum (PubMed:17129178, PubMed:20399919). {ECO:0000269|PubMed:12765696, ECO:0000269|PubMed:17129178, ECO:0000269|PubMed:20399919}. +F6SEU4 SYGP1_MOUSE Ras/Rap GTPase-activating protein SynGAP (Neuronal RasGAP) (Synaptic Ras GTPase-activating protein 1) (Synaptic Ras-GAP 1) 1340 148,238 Chain (1); Domain (3); Helix (2); Modified residue (27); Motif (1) FUNCTION: Major constituent of the PSD essential for postsynaptic signaling. Inhibitory regulator of the Ras-cAMP pathway. Member of the NMDAR signaling complex in excitatory synapses, it may play a role in NMDAR-dependent control of AMPAR potentiation, AMPAR membrane trafficking and synaptic plasticity. Regulates AMPAR-mediated miniature excitatory postsynaptic currents. Exhibits dual GTPase-activating specificity for Ras and Rap. May be involved in certain forms of brain injury, leading to long-term learning and memory deficits (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell junction, synapse {ECO:0000250}. Note=Mostly in excitatory glutamatergic synapses (By similarity). receptor activation or SYNGAP1/MPDZ complex disruption. Phosphorylation by PLK2 promotes its activity (By similarity). {ECO:0000250}. SUBUNIT: Interacts KLHL17, CAMK2A and CAMK2B. Interacts with MPDZ (By similarity). {ECO:0000250}. DOMAIN: The C2 domain is required for RapGAP activity. {ECO:0000250}. +Q8BML9 SYQ_MOUSE Glutamine--tRNA ligase (EC 6.1.1.18) (Glutaminyl-tRNA synthetase) (GlnRS) 775 87,677 Binding site (3); Chain (1); Initiator methionine (1); Modified residue (4); Nucleotide binding (4); Sequence conflict (4) FUNCTION: Glutamine--tRNA ligase. Plays a critical role in brain development. {ECO:0000250|UniProtKB:P47897}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P47897}. Cytoplasm {ECO:0000250|UniProtKB:P47897}. SUBUNIT: Monomer. Part of a multisubunit complex that groups tRNA ligases for Arg (RARS), Asp (DARS), Gln (QARS), Ile (IARS), Leu (LARS), Lys (KARS), Met (MARS) the bifunctional ligase for Glu and Pro (EPRS) and the auxiliary subunits AIMP1/p43, AIMP2/p38 and EEF1E1/p18 (PubMed:12060739). Interacts with RARS. Part of a complex composed of RARS, QARS and AIMP1 (By similarity). {ECO:0000250|UniProtKB:P47897, ECO:0000269|PubMed:12060739}. +Q9D0I9 SYRC_MOUSE Arginine--tRNA ligase, cytoplasmic (EC 6.1.1.19) (Arginyl-tRNA synthetase) (ArgRS) 660 75,674 Binding site (4); Chain (1); Modified residue (1); Motif (1); Region (3); Sequence conflict (10) FUNCTION: Forms part of a macromolecular complex that catalyzes the attachment of specific amino acids to cognate tRNAs during protein synthesis (PubMed:12060739). Modulates the secretion of AIMP1 and may be involved in generation of the inflammatory cytokine EMAP2 from AIMP1. {ECO:0000250|UniProtKB:P54136, ECO:0000269|PubMed:12060739}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P54136}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P54136}. SUBUNIT: Interacts (via N-terminus) with AIMP1 (via N-terminus); this stimulates its catalytic activity. Interacts (via N-terminus) with LARS2 (via C-terminus). Monomer (By similarity). Part of a multisubunit complex that groups tRNA ligases for Arg (RARS), Asp (DARS), Gln (QARS), Ile (IARS), Leu (LARS), Lys (KARS), Met (MARS) the bifunctional ligase for Glu and Pro (EPRS) and the auxiliary subunits AIMP1/p43, AIMP2/p38 and EEF1E1/p18 (PubMed:12060739). Interacts with QARS. Part of a complex composed of RARS, QARS and AIMP1 (By similarity). {ECO:0000250|UniProtKB:P54136, ECO:0000269|PubMed:12060739}. DOMAIN: The alpha-helical N-terminus (residues 1-72) mediates interaction with AIMP1 and thereby contributes to the assembly of the multisynthetase complex. {ECO:0000250|UniProtKB:P54136}. +Q3U186 SYRM_MOUSE Probable arginine--tRNA ligase, mitochondrial (EC 6.1.1.19) (Arginyl-tRNA synthetase) (ArgRS) 578 65,336 Binding site (4); Chain (1); Modified residue (1); Motif (1); Region (1); Sequence conflict (2); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. +Q62187 TTF1_MOUSE Transcription termination factor 1 (TTF-1) (RNA polymerase I termination factor) (Transcription termination factor I) (TTF-I) (mTFF-I) 859 97,723 Chain (1); Compositional bias (1); Cross-link (1); Domain (2); Modified residue (7); Region (1); Sequence conflict (5) FUNCTION: Multifunctional nucleolar protein that terminates ribosomal gene transcription, mediates replication fork arrest and regulates RNA polymerase I transcription on chromatin. Plays a dual role in rDNA regulation, being involved in both activation and silencing of rDNA transcription. Interaction with BAZ2A/TIP5 recovers DNA-binding activity. {ECO:0000269|PubMed:15292447, ECO:0000269|PubMed:7720715, ECO:0000269|PubMed:9049305, ECO:0000269|PubMed:9267035}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:7720715}. Nucleus, nucleolus {ECO:0000269|PubMed:7720715}. SUBUNIT: Oligomer. The oligomeric structure enables to interact simultaneously with two separatee DNA fragments (PubMed:9092622). Interacts with BAZ2A/TIP5 (PubMed:15292447). Interacts with CAVIN1 (PubMed:9582279, PubMed:27528195). {ECO:0000269|PubMed:15292447, ECO:0000269|PubMed:27528195, ECO:0000269|PubMed:9092622, ECO:0000269|PubMed:9582279}. DOMAIN: The N-terminal region (NRD) inhibits DNA-binding via its interaction with the C-terminal region. +Q91V83 TTI1_MOUSE TELO2-interacting protein 1 homolog 1085 120,814 Chain (1); Modified residue (2); Sequence conflict (2) FUNCTION: Regulator of the DNA damage response (DDR). Part of the TTT complex that is required to stabilize protein levels of the phosphatidylinositol 3-kinase-related protein kinase (PIKK) family proteins. The TTT complex is involved in the cellular resistance to DNA damage stresses, like ionizing radiation (IR), ultraviolet (UV) and mitomycin C (MMC). Together with the TTT complex and HSP90 may participate in the proper folding of newly synthesized PIKKs. Promotes assembly, stabilizes and maintains the activity of mTORC1 and mTORC2 complexes, which regulate cell growth and survival in response to nutrient and hormonal signals (By similarity). {ECO:0000250}. PTM: Phosphorylated at Ser-823 by CK2 following growth factor deprivation, leading to its subsequent ubiquitination by the SCF(FBXO9) complex. Phosphorylation by CK2 only takes place when TELO2 is bound to mTORC1, not mTORC2; leading to selective ubiquitination of mTORC1-associated protein (By similarity). {ECO:0000250}.; PTM: Ubiquitinated by the SCF(FBXO9) complex following phosphorylation by CK2 in response to growth factor deprivation, leading to its degradation by the proteasome. Only mTORC1-associated protein is ubiquitinated and degraded, leading to selective inactivation of mTORC1 to restrain cell growth and protein translation, while mTORC2 is activated due to the relief of feedback inhibition by mTORC1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Component of the TTT complex composed of TELO2, TTI1 and TTI2. Interacts with ATM, ATR, MTOR, PRKDC, SMG1, TELO2, TRRAP AND TTI2. Component of the mTORC1 and mTORC2 complexes. Interacts with WAC; WAC positively regulates MTOR activity by promoting the assembly of the TTT complex and the RUVBL complex composed of RUVBL1 and RUVBL2 into the TTT-RUVBL complex which leads to the dimerization of the mTORC1 complex and its subsequent activation. {ECO:0000250|UniProtKB:O43156}. +Q8BGV4 TTI2_MOUSE TELO2-interacting protein 2 512 56,702 Chain (1); Sequence conflict (2) FUNCTION: Regulator of the DNA damage response (DDR). Part of the TTT complex that is required to stabilize protein levels of the phosphatidylinositol 3-kinase-related protein kinase (PIKK) family proteins. The TTT complex is involved in the cellular resistance to DNA damage stresses, like ionizing radiation (IR), ultraviolet (UV) and mitomycin C (MMC). Together with the TTT complex and HSP90 may participate in the proper folding of newly synthesized PIKKs (By similarity). {ECO:0000250}. SUBUNIT: Component of the TTT complex composed of TELO2, TTI1 and TTI2. Interacts with TELO2 and TTI1. Interacts with WAC; WAC positively regulates MTOR activity by promoting the assembly of the TTT complex and the RUVBL complex composed of RUVBL1 and RUVBL2 into the TTT-RUVBL complex which leads to the dimerization of the mTORC1 complex and its subsequent activation. {ECO:0000250|UniProtKB:Q6NXR4}. +P35761 TTK_MOUSE Dual specificity protein kinase TTK (EC 2.7.12.1) (ESK) (PYT) 856 96,211 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Domain (1); Modified residue (8); Nucleotide binding (1) FUNCTION: Essential for chromosome alignment by enhancing AURKB activity (via direct CDCA8 phosphorylation) at the centromere, and for the mitotic checkpoint (By similarity). Phosphorylates proteins on serine, threonine, and tyrosine. Probably associated with cell proliferation. May play some role in the control of cell proliferation or differentiation and could be involved in modulating different levels of signal transduction pathways. {ECO:0000250}. PTM: Autophosphorylated. SUBUNIT: Interacts with TPR; the interactions occurs in a microtubule-independent manner. {ECO:0000250}. TISSUE SPECIFICITY: Present in rapidly proliferating cell lines; high levels in testis, bone marrow, spleen and thymus. Low levels in brain, heart, lung and kidney. +Q3UDE2 TTL12_MOUSE Tubulin--tyrosine ligase-like protein 12 639 74,043 Binding site (2); Chain (1); Domain (1); Nucleotide binding (1); Sequence conflict (1) TISSUE SPECIFICITY: Widely expressed with highest levels in brain, kidney, liver, lung, muscle and testis. {ECO:0000269|PubMed:17499049}. +A4Q9F6 TTL13_MOUSE Tubulin polyglutamylase TTLL13 (EC 6.-.-.-) (Tubulin--tyrosine ligase-like protein 13) 804 93,463 Binding site (2); Chain (1); Coiled coil (3); Domain (1); Frameshift (1); Nucleotide binding (1); Region (1) FUNCTION: Polyglutamylase which preferentially modifies alpha-tubulin. Involved in the side-chain elongation step of the polyglutamylation reaction rather than in the initiation step. {ECO:0000269|PubMed:17499049}. DOMAIN: The flexible c-MTBD (cationic microtubule binding domain) region mediates binding to microtubules. It is positively charged and becomes ordered when bound to microtubules: it interacts with a negatively charged patch on tubulin. The presence of positive charges in the c-MTBD region is essential for proper binding. {ECO:0000250|UniProtKB:A6NNM8, ECO:0000250|UniProtKB:Q6ZT98}. TISSUE SPECIFICITY: Widely expressed with highest levels in heart and testis. {ECO:0000269|PubMed:17499049}. +Q91V51 TTLL1_MOUSE Probable tubulin polyglutamylase TTLL1 (EC 6.-.-.-) (Tubulin polyglutamylase complex subunit 3) (PGs3) (Tubulin--tyrosine ligase-like protein 1) (p49) 423 49,110 Binding site (2); Chain (1); Domain (1); Nucleotide binding (1); Sequence conflict (2) FUNCTION: Catalytic subunit of the neuronal tubulin polyglutamylase complex. Modifies alpha- and beta-tubulin, generating side chains of glutamate on the gamma-carboxyl groups of specific glutamate residues within the C-terminal tail of alpha- and beta-tubulin. {ECO:0000269|PubMed:15890843}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. SUBUNIT: Part of the neuronal tubulin polyglutamylase complex which contains TPGS1, TPGS2, TTLL1, LRRC49 and NICN1. TISSUE SPECIFICITY: Widely expressed with highest levels in brain, heart and kidney. {ECO:0000269|PubMed:17499049}. +A4Q9E5 TTLL3_MOUSE Tubulin monoglycylase TTLL3 (EC 6.3.2.-) (Tubulin--tyrosine ligase-like protein 3) 927 104,428 Alternative sequence (5); Binding site (2); Chain (1); Domain (1); Nucleotide binding (1); Sequence conflict (2) FUNCTION: Monoglycylase which modifies alpha- and beta-tubulin, generating side chains of glycine on the gamma-carboxyl groups of specific glutamate residues within the C-terminal tail of alpha- and beta-tubulin. Involved in the side-chain initiation step of the glycylation reaction by adding a single glycine chain to generate monoglycine side chains. Not involved in elongation step of the polyglycylation reaction. {ECO:0000269|PubMed:19524510}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305|PubMed:19524510}. Cell projection, cilium {ECO:0000305|PubMed:19524510}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000305|PubMed:19524510}. TISSUE SPECIFICITY: Widely expressed with highest levels in brain and testis. {ECO:0000269|PubMed:17499049}. +Q8CHB8 TTLL5_MOUSE Tubulin polyglutamylase TTLL5 (EC 6.-.-.-) (Tubulin--tyrosine ligase-like protein 5) 1328 147,715 Alternative sequence (1); Binding site (2); Chain (1); Domain (1); Erroneous initiation (2); Frameshift (1); Nucleotide binding (1); Region (1); Sequence conflict (7) FUNCTION: Polyglutamylase which preferentially modifies alpha-tubulin. Involved in the side-chain initiation step of the polyglutamylation reaction rather than in the elongation step. Required for CCSAP localization to both spindle and cilia microtubules. Increases the effects of NCOA2 in glucocorticoid receptor-mediated repression and induction and in androgen receptor-mediated induction. {ECO:0000269|PubMed:17499049}. SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000269|PubMed:17499049}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:17499049}. Nucleus {ECO:0000250|UniProtKB:Q6EMB2}. Cytoplasm {ECO:0000250, ECO:0000250|UniProtKB:Q6EMB2}. Note=In osteosarcoma cells, found in both cytoplasm and nucleus in the absence of steroid but located exclusively in the nucleus in the presence of steroid (By similarity). Localized to the base of the connecting cilium between the basal body and the adjacent daughter centriole of the cilium. {ECO:0000250|UniProtKB:Q6EMB2}. SUBUNIT: Interacts with the transcriptional coactivators NCOA1/SRC-1 and NCOA2/TIF2. {ECO:0000250|UniProtKB:Q6EMB2}. DOMAIN: The flexible c-MTBD (cationic microtubule binding domain) region mediates binding to microtubules. It is positively charged and becomes ordered when bound to microtubules: it interacts with a negatively charged patch on tubulin. The presence of positive charges in the c-MTBD region is essential for proper binding. {ECO:0000250|UniProtKB:Q6EMB2, ECO:0000250|UniProtKB:Q6ZT98}. TISSUE SPECIFICITY: Widely expressed with highest levels in brain, kidney, liver, spleen and testis. {ECO:0000269|PubMed:17499049}. +A4Q9F0 TTLL7_MOUSE Tubulin polyglutamylase TTLL7 (EC 6.-.-.-) (Tubulin--tyrosine ligase-like protein 7) (mTTLL7) 912 105,501 Alternative sequence (2); Binding site (2); Chain (1); Domain (1); Mutagenesis (1); Nucleotide binding (1); Region (1); Sequence conflict (1); Site (2) FUNCTION: Polyglutamylase which preferentially modifies beta-tubulin (PubMed:16901895, PubMed:17499049, PubMed:19152315). Mediates both ATP-dependent initiation and elongation of polyglutamylation of microtubules (PubMed:16901895, PubMed:19152315). Required for neurite growth; responsible for the strong increase in tubulin polyglutamylation during postnatal neuronal maturation (PubMed:16901895). {ECO:0000269|PubMed:16901895, ECO:0000269|PubMed:17499049, ECO:0000269|PubMed:19152315}. SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000269|PubMed:16901895, ECO:0000269|PubMed:17499049}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:16901895, ECO:0000269|PubMed:17499049}. Cell projection, dendrite {ECO:0000269|PubMed:16901895, ECO:0000269|PubMed:17499049}. Perikaryon {ECO:0000269|PubMed:16901895, ECO:0000269|PubMed:17499049}. Note=In cells with primary cilia, found in both cilia and basal bodies. In neuronal cells, found in dendrites and perikaryon. {ECO:0000269|PubMed:16901895, ECO:0000269|PubMed:17499049}. SUBUNIT: Interacts with both alpha- and beta-tubulin (via C-terminal tubulin tails). {ECO:0000250|UniProtKB:Q6ZT98}. DOMAIN: The enzyme uses its core to engage the disordered anionic tails of alpha- and beta-tubulin and the flexible c-MTBD (cationic microtubule binding domain) region to bind the microtubule and position itself for beta-tail modification. The c-MTBD region is positively charged and becomes ordered when bound to microtubules: it interacts with a negatively charged patch on alpha-tubulin. The presence of positive charges in the c-MTBD region is essential for proper binding. {ECO:0000250|UniProtKB:Q6ZT98}. TISSUE SPECIFICITY: Widely expressed with highest levels in brain, testis and trachea. In brain, highly expressed in hippocampus, thalamus, olfactory bulb and cerebellum. {ECO:0000269|PubMed:16901895, ECO:0000269|PubMed:17499049}. +A4Q9F1 TTLL8_MOUSE Protein monoglycylase TTLL8 (EC 6.3.2.-) (Tubulin--tyrosine ligase-like protein 8) 832 94,915 Binding site (2); Chain (1); Domain (1); Erroneous initiation (2); Frameshift (1); Nucleotide binding (1) FUNCTION: Monoglycylase which modifies both tubulin and non-tubulin proteins, generating side chains of glycine on the gamma-carboxyl groups of specific glutamate residues of target proteins. Monoglycylates tubulin, with a preference for alpha-tubulin toward beta-tubulin. Has the ability to modify non-tubulin proteins such as ANP32A, ANP32B, SET and NCL. Involved in the side-chain initiation step of the glycylation reaction by adding a single glycine chain to generate monoglycine side chains. Not involved in elongation step of the polyglycylation reaction. {ECO:0000269|PubMed:19427864, ECO:0000269|PubMed:19524510}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305|PubMed:19524510}. Cell projection, cilium {ECO:0000305|PubMed:19524510}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000305|PubMed:19524510}. TISSUE SPECIFICITY: Widely expressed with highest levels in testis. {ECO:0000269|PubMed:17499049}. +A2APC3 TTLL9_MOUSE Probable tubulin polyglutamylase TTLL9 (EC 6.-.-.-) (Tubulin--tyrosine ligase-like protein 9) 461 54,107 Alternative sequence (1); Binding site (2); Chain (1); Domain (1); Erroneous gene model prediction (2); Nucleotide binding (1); Sequence conflict (1) FUNCTION: Probable tubulin polyglutamylase that forms polyglutamate side chains on tubulin. Probably acts when complexed with other proteins (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:17499049}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17499049}. +Q8C5C9 TTMP_MOUSE TPA-induced transmembrane protein homolog 218 24,709 Chain (1); Erroneous initiation (1); Sequence conflict (3); Transmembrane (1) TRANSMEM 66 86 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q9D3D0 TTPAL_MOUSE Alpha-tocopherol transfer protein-like 343 38,836 Alternative sequence (2); Chain (1); Domain (1); Erroneous initiation (4) FUNCTION: May act as a protein that binds a hydrophobic ligand. {ECO:0000305}. +P26638 SYSC_MOUSE Serine--tRNA ligase, cytoplasmic (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase) 512 58,389 Binding site (5); Chain (1); Modified residue (4); Motif (1); Nucleotide binding (3); Region (1); Sequence conflict (3) Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1. FUNCTION: Catalyzes the attachment of serine to tRNA(Ser) in a two-step reaction: serine is first activated by ATP to form Ser-AMP and then transferred to the acceptor end of tRNA(Ser). Is probably also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec). In the nucleus, binds to the VEGFA core promoter and prevents MYC binding and transcriptional activation by MYC. Recruits SIRT2 to the VEGFA promoter, promoting deacetylation of histone H4 at 'Lys-16' (H4K16). Thereby, inhibits the production of VEGFA and sprouting angiogenesis mediated by VEGFA. {ECO:0000250|UniProtKB:P49591}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P49591}. Nucleus {ECO:0000250|UniProtKB:P49591}. Note=Predominantly cytoplasmic, but a minor proportion is also found in the nucleus. {ECO:0000250|UniProtKB:P49591}. SUBUNIT: Homodimer. The tRNA molecule may bind across the dimer. Interacts with SIRT2. {ECO:0000250|UniProtKB:P49591}. DOMAIN: Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding. {ECO:0000250|UniProtKB:P49591}. +Q91YR1 TWF1_MOUSE Twinfilin-1 (Protein A6) 350 40,079 Beta strand (12); Chain (1); Domain (2); Helix (13); Initiator methionine (1); Modified residue (5); Natural variant (1); Sequence conflict (2); Turn (2) FUNCTION: Actin-binding protein involved in motile and morphological processes. Inhibits actin polymerization, likely by sequestering G-actin. By capping the barbed ends of filaments, it also regulates motility. Seems to play an important role in clathrin-mediated endocytosis and distribution of endocytic organelles. {ECO:0000269|PubMed:10669753, ECO:0000269|PubMed:15282541, ECO:0000269|PubMed:16511569, ECO:0000269|PubMed:9249064}. PTM: Phosphorylated on serine and threonine residues. {ECO:0000250|UniProtKB:Q12792}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10669753}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10669753}. Note=Diffuse cytoplasmic localization with perinuclear and G-actin-rich cortical actin structures sublocalization. Also found at membrane ruffles and cell-cell contacts. SUBUNIT: Interacts with G-actin; ADP-actin form and capping protein (CP) (PubMed:12807912, PubMed:15282541, PubMed:16511569). May also be able to interact with TWF2 and phosphoinositides, PI(4,5)P2 (PubMed:12807912). When bound to PI(4,5)P2, it is down-regulated (PubMed:12807912). Interacts with ACTG1 (By similarity). {ECO:0000250|UniProtKB:Q12792, ECO:0000269|PubMed:10669753, ECO:0000269|PubMed:12807912, ECO:0000269|PubMed:15282541, ECO:0000269|PubMed:16511569}. TISSUE SPECIFICITY: Widely expressed with highest levels in brain, liver and kidney. Also expressed in heart, lung and testis. Not detected in spleen or skeletal muscle. {ECO:0000269|PubMed:10669753, ECO:0000269|PubMed:12807912, ECO:0000269|PubMed:9249064}. +Q9Z0P5 TWF2_MOUSE Twinfilin-2 (A6-related protein) (mA6RP) (Twinfilin-1-like protein) 349 39,471 Alternative sequence (1); Chain (1); Domain (2); Initiator methionine (1); Modified residue (4); Sequence conflict (2) FUNCTION: Actin-binding protein involved in motile and morphological processes. Inhibits actin polymerization, likely by sequestering G-actin. By capping the barbed ends of filaments, it also regulates motility. Seems to play an important role in clathrin-mediated endocytosis and distribution of endocytic organelles. May play a role in regulating the mature length of the middle and short rows of stereocilia. {ECO:0000269|PubMed:18837697, ECO:0000269|PubMed:19955359}. PTM: Phosphorylated on both serine/threonine and tyrosine. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19955359}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10406962}. Cell projection, stereocilium {ECO:0000269|PubMed:19774077, ECO:0000269|PubMed:19955359}. Note=Perinuclear and G-actin-rich cortical actin structure sublocalization. Isoform 2 found also along myofibrils in cardiomyocytes (PubMed:18837697). Localized in cochlea hair cells to the tips of the middle and short rows of stereocilia (PubMed:19955359). {ECO:0000269|PubMed:18837697, ECO:0000269|PubMed:19955359}. SUBUNIT: Interacts with G-actin; ADP-actin form and capping protein (CP). Isoform 2 interacts (via its N-terminal ADF-H domain) with G-actin (ADP-bound form) with significantly higher affinity than isoform 1. May also be able to interact with TWF1 and phosphoinositides, PI(4,5)P2. When bound to PI(4,5)P2, it is down-regulated. Interacts with MYO7A. {ECO:0000269|PubMed:12807912, ECO:0000269|PubMed:18837697, ECO:0000269|PubMed:19774077}. TISSUE SPECIFICITY: Isoform 1 is ubiquitously expressed (at protein level). Isoform 2 expression is restricted to heart and skeletal muscle where it is the predominant form. {ECO:0000269|PubMed:10406962, ECO:0000269|PubMed:18837697}. +Q9D030 TWST2_MOUSE Twist-related protein 2 (Dermis-expressed protein 1) (Dermo-1) 160 18,140 Chain (1); Domain (1); Mutagenesis (1); Sequence conflict (1) FUNCTION: Binds to the E-box consensus sequence 5'-CANNTG-3' as a heterodimer and inhibits transcriptional activation by MYOD1, MYOG, MEF2A and MEF2C. Also represses expression of proinflammatory cytokines such as TNFA and IL1B. Involved in postnatal glycogen storage and energy metabolism. Inhibits the premature or ectopic differentiation of preosteoblast cells during osteogenesis, possibly by changing the internal signal transduction response of osteoblasts to external growth factors (By similarity). {ECO:0000250, ECO:0000269|PubMed:11809751, ECO:0000269|PubMed:12553906, ECO:0000269|PubMed:7589808}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:11809751}. Cytoplasm {ECO:0000269|PubMed:11809751}. Note=Mainly nuclear during embryonic development. Cytoplasmic in adult tissues. SUBUNIT: Efficient DNA binding requires dimerization with another bHLH protein. Forms a heterodimer with TCF3/E12. Also interacts with MEF2C. {ECO:0000269|PubMed:7589808}. DOMAIN: The C-terminal and HLH domains are essential for transcriptional repression. {ECO:0000269|PubMed:11809751}. TISSUE SPECIFICITY: Expressed at low levels in sclerotome and dermatome of somites, and in limb buds at 10.5 dpc. Accumulates predominantly in dermatome, prevertebrae and derivatives of branchial arches by 13 dpc. Also expressed near surface of embryo and in chondrogenic cells. In adult, expressed at low levels in skin, bladder, uterus, aorta and heart. {ECO:0000269|PubMed:7589808}. +Q920M7 SYT17_MOUSE Synaptotagmin-17 (Protein B/K) (Synaptotagmin XVII) (SytXVII) 470 53,293 Chain (1); Compositional bias (1); Domain (2); Modified residue (2); Sequence conflict (1) FUNCTION: Plays a role in dendrite formation by melanocytes. {ECO:0000250|UniProtKB:Q9BSW7}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11716773}; Peripheral membrane protein {ECO:0000269|PubMed:11716773}. +Q9EQT6 SYT13_MOUSE Synaptotagmin-13 (Synaptotagmin XIII) (SytXIII) 426 46,870 Chain (1); Domain (2); Erroneous initiation (1); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 7 29 Helical. {ECO:0000255}. TOPO_DOM 1 6 Vesicular. {ECO:0000255}.; TOPO_DOM 30 426 Cytoplasmic. {ECO:0000255}. FUNCTION: May be involved in transport vesicle docking to the plasma membrane. SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:11171101}; Single-pass membrane protein {ECO:0000269|PubMed:11171101}. SUBUNIT: Interacts with NRXN1. {ECO:0000269|PubMed:11171101}. DOMAIN: The first C2 domain/C2A does not mediate Ca(2+)-dependent phospholipid binding.; DOMAIN: The second C2 domain/C2B domain binds phospholipids regardless of whether calcium is present. TISSUE SPECIFICITY: Expressed in brain, heart, spleen, lung and testis. {ECO:0000269|PubMed:11171101}. +Q7TN84 SYT14_MOUSE Synaptotagmin-14 (Synaptotagmin XIV) (SytXIV) 555 62,044 Chain (1); Domain (2); Topological domain (2); Transmembrane (1) TRANSMEM 25 47 Helical; Signal-anchor for type III membrane protein. {ECO:0000255}. TOPO_DOM 1 24 Extracellular. {ECO:0000255}.; TOPO_DOM 48 555 Cytoplasmic. {ECO:0000255}. FUNCTION: May be involved in the trafficking and exocytosis of secretory vesicles in non-neuronal tissues. Is Ca(2+)-independent. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type III membrane protein {ECO:0000305}. SUBUNIT: Homodimer. Can also form heterodimers (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in heart and testis. Expressed in brain (especially in the cerebellum). {ECO:0000269|PubMed:12801916, ECO:0000269|PubMed:21835308}. +Q1H9T6 TZAP_MOUSE Telomere zinc finger-associated protein (TZAP) (Krueppel-related zinc finger protein 3 homolog) (Zinc finger and BTB domain-containing protein 48) 681 76,800 Alternative sequence (1); Beta strand (9); Chain (1); Cross-link (2); Domain (1); Erroneous gene model prediction (1); Helix (11); Sequence conflict (4); Turn (4); Zinc finger (11) FUNCTION: Telomere-binding protein that acts as a regulator of telomere length. Directly binds the telomeric double-stranded 5'-TTAGGG-3' repeat. Preferentially binds to telomeres that have a low concentration of shelterin complex and acts as a regulator of telomere length by initiating telomere trimming, a process that prevents the accumulation of aberrantly long telomeres. Also acts as a transcription regulator that binds to promoter regions. Regulates expression of a small subset of genes, including MTFP1. Regulates expression the J and/or S elements in MHC II promoter. Acts as a negative regulator of cell proliferation by specifically activating expression of ARF, a tumor suppressor isoform of CDKN2A. {ECO:0000250|UniProtKB:P10074}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P10074}. Chromosome, telomere {ECO:0000250|UniProtKB:P10074}. Note=Directly binds the telomeric double-stranded 5'-TTAGGG-3' repeat. According to a report, preferentially binds to long telomeres that have a low concentration of shelterin complex, competing with the telomeric repeat binding factors TERF1 and TERF2. According to another report, binds telomeres regardless of their length. {ECO:0000250|UniProtKB:P10074}. SUBUNIT: Interacts with EP300. {ECO:0000250|UniProtKB:P10074}. DOMAIN: The C2H2-type zinc fingers mediate binding to the telomeric double-stranded 5'-TTAGGG-3' repeats. The last C2H2-type zinc finger is required for telomeric-binding. {ECO:0000250|UniProtKB:P10074}. +Q5SS91 SUN3_MOUSE SUN domain-containing protein 3 (Sad1/unc-84 domain-containing protein 1) 320 36,758 Alternative sequence (1); Chain (1); Coiled coil (1); Domain (1); Topological domain (2); Transmembrane (1) TRANSMEM 7 29 Helical. {ECO:0000255}. TOPO_DOM 1 6 Nuclear. {ECO:0000305}.; TOPO_DOM 30 320 Perinuclear space. {ECO:0000305}. FUNCTION: As a probable component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning. May be involved in nuclear remodeling during sperm head formation in spermatogenenis. A probable SUN3:SYNE1 LINC complex may tether spermatid nuclei to posterior cytoskeletal structures such as the manchette. {ECO:0000305|PubMed:20711465}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Nucleus envelope {ECO:0000269|PubMed:20711465}. Nucleus inner membrane {ECO:0000305}. Note=Localized to spermatid nucleus posterior pole lateral regions excluding the implantation fossa during entire sperm head elongation. {ECO:0000269|PubMed:20711465}. SUBUNIT: Self-associates. Interacts with SYNE1 and SPAG4/SUN4. Proposed to form a spermatogenesis-specific LINC complex with SYNE1 during sperm head formation possibly implicating a SUN domain-based heterotrimer with SPAG4/SUN4 associating with SYNE1. Can interact with SYNE3; the interaction is questioned by missing colocalization in spermatids. {ECO:0000269|PubMed:20711465, ECO:0000269|PubMed:26621829}. TISSUE SPECIFICITY: Specifically expressed in testis (at protein level). {ECO:0000269|PubMed:20711465}. +Q8BZW2 SWAHB_MOUSE Ankyrin repeat domain-containing protein SOWAHB (Ankyrin repeat domain-containing protein 56) (Protein sosondowah homolog B) 760 83,542 Chain (1); Modified residue (3); Repeat (2) +Q8BY98 SWAHD_MOUSE Ankyrin repeat domain-containing protein SOWAHD (Ankyrin repeat domain-containing protein 58) (Protein sosondowah homolog D) 327 36,297 Chain (1); Repeat (3) +Q64310 SURF4_MOUSE Surfeit locus protein 4 269 30,381 Chain (1); Motif (1); Transmembrane (5) TRANSMEM 65 85 Helical. {ECO:0000255}.; TRANSMEM 92 112 Helical. {ECO:0000255}.; TRANSMEM 179 199 Helical. {ECO:0000255}.; TRANSMEM 203 223 Helical. {ECO:0000255}.; TRANSMEM 242 262 Helical. {ECO:0000255}. FUNCTION: May play a role in the maintenance of the architecture of the endoplasmic reticulum-Golgi intermediate compartment and of the Golgi. {ECO:0000250|UniProtKB:O15260}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O15260}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:O15260}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:O15260, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Note=Cycles between the endoplasmic reticulum and the Golgi. {ECO:0000250|UniProtKB:O15260}. SUBUNIT: Found in a complex composed at least of SURF4, TMED2 and TMED10. May interact with LMAN1 (By similarity). Interacts with ZFYVE27 and with KIF5A in a ZFYVE27-dependent manner (PubMed:21976701). {ECO:0000250|UniProtKB:O15260, ECO:0000269|PubMed:21976701}. DOMAIN: The di-lysine motif confers endoplasmic reticulum localization for type I membrane proteins. {ECO:0000250|UniProtKB:O15260}. +Q3UZP4 SVIP_MOUSE Small VCP/p97-interacting protein 77 8,364 Chain (1); Initiator methionine (1); Lipidation (1); Modified residue (1); Region (1) SUBCELLULAR LOCATION: Smooth endoplasmic reticulum membrane; Peripheral membrane protein. Golgi apparatus membrane; Peripheral membrane protein. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Membrane {ECO:0000250|UniProtKB:Q8NHG7}; Lipid-anchor {ECO:0000250|UniProtKB:Q8NHG7}. SUBUNIT: Interacts with VCP. {ECO:0000250|UniProtKB:Q8NHG7}. +Q9CXK4 SWET1_MOUSE Sugar transporter SWEET1 (MmSWEET1) (RAG1-activating protein 1) (Solute carrier family 50 member 1) 221 24,649 Chain (1); Domain (2); Region (1); Sequence conflict (1); Transmembrane (7) TRANSMEM 3 23 Helical; Name=1. {ECO:0000255}.; TRANSMEM 43 63 Helical; Name=2. {ECO:0000255}.; TRANSMEM 68 88 Helical; Name=3. {ECO:0000255}.; TRANSMEM 102 122 Helical; Name=4. {ECO:0000255}.; TRANSMEM 129 149 Helical; Name=5. {ECO:0000255}.; TRANSMEM 160 180 Helical; Name=6. {ECO:0000255}.; TRANSMEM 186 206 Helical; Name=7. {ECO:0000255}. FUNCTION: Mediates sugar transport across membranes (By similarity). May regulate the expression of RAG1 a gene involved in V(D)J recombination. {ECO:0000250, ECO:0000269|PubMed:8630032}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=May also localize to the endoplasmic reticulum. {ECO:0000250}. SUBUNIT: Interacts with TRPV2; the interaction probably occurs intracellularly and depends on TRPV2 N-glycosylation. {ECO:0000250}. TISSUE SPECIFICITY: Expressed at high levels in lung, placenta, spleen and thymus, at intermediate levels in brain, heart, kidney and testis, and at low levels in bone marrow, liver and lymph node. Within the thymus expression is highest in non-lymphoid cells. {ECO:0000269|PubMed:8630032}. +Q8K3D3 SWI5_MOUSE DNA repair protein SWI5 homolog (Protein SAE3 homolog) 89 10,261 Alternative sequence (1); Chain (1); Coiled coil (1); Modified residue (1) FUNCTION: Component of the SWI5-SFR1 complex, a complex required for double-strand break repair via homologous recombination. {ECO:0000269|PubMed:20976249}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20976249}. SUBUNIT: Component of the SWI5-SFR1 complex. Interacts with RAD51. {ECO:0000269|PubMed:20976249}. +O54864 SUV91_MOUSE Histone-lysine N-methyltransferase SUV39H1 (EC 2.1.1.43) (Histone H3-K9 methyltransferase 1) (H3-K9-HMTase 1) (Position-effect variegation 3-9 homolog) (Suppressor of variegation 3-9 homolog 1) (Su(var)3-9 homolog 1) 412 47,754 Alternative sequence (3); Binding site (1); Chain (1); Domain (4); Frameshift (1); Metal binding (17); Modified residue (2); Region (4); Sequence conflict (1) FUNCTION: Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys-9' as substrate. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions. H3 'Lys-9' trimethylation is also required to direct DNA methylation at pericentric repeats. SUV39H1 is targeted to histone H3 via its interaction with RB1 and is involved in many processes, such as repression of MYOD1-stimulated differentiation, regulation of the control switch for exiting the cell cycle and entering differentiation, repression by the PML-RARA fusion protein, BMP-induced repression, repression of switch recombination to IgA and regulation of telomere length. Component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus. Recruited by the PER complex to the E-box elements of the circadian target genes such as PER2 itself or PER1, contributes to the conversion of local chromatin to a heterochromatin-like repressive state through H3 'Lys-9' trimethylation. {ECO:0000269|PubMed:11701123, ECO:0000269|PubMed:12867029, ECO:0000269|PubMed:14690609, ECO:0000269|PubMed:14690610, ECO:0000269|PubMed:14702045, ECO:0000269|PubMed:18004385, ECO:0000269|PubMed:24413057}. PTM: Phosphorylated on serine residues, and to a lesser degree, on threonine residues. {ECO:0000250}.; PTM: Acetylated at Lys-266, leading to inhibition of enzyme activity. SIRT1-mediated deacetylation relieves this inhibition (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Nucleus lamina {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Chromosome, centromere. Note=Associates with centromeric constitutive heterochromatin. SUBUNIT: Interacts with CCAR2 and GFI1B. Component of the eNoSC complex, composed of SIRT1, SUV39H1 and RRP8 (By similarity). Interacts with H3 and H4 histones. Interacts with DNMT3B, CBX1, CBX4, MBD1, RUNX1, RUNX3, MYOD1, SMAD5 and RB1. Interacts with SBF1 through the SET domain. Interacts with HDAC1 and HDAC2 through the N-terminus and associates with the core histone deacetylase complex composed of HDAC1, HDAC2, RBBP4 and RBBP7. Interacts (via SET domain) with MECOM; enhances MECOM transcriptional repression activity. Interacts with LMNA; the interaction increases stability of SUV39H1. The large PER complex involved in the histone methylation is composed of at least PER2, CBX3, TRIM28, SUV39H1 and/or SUV39H2; CBX3 mediates the formation of the complex. {ECO:0000250, ECO:0000269|PubMed:10202156, ECO:0000269|PubMed:11788710, ECO:0000269|PubMed:12867029, ECO:0000269|PubMed:18619962, ECO:0000269|PubMed:23695662}. DOMAIN: Although the SET domain contains the active site of enzymatic activity, both pre-SET and post-SET domains are required for methyltransferase activity. The SET domain also participates in stable binding to heterochromatin.; DOMAIN: In the pre-SET domain, Cys residues bind 3 zinc ions that are arranged in a triangular cluster; some of these Cys residues contribute to the binding of two zinc ions within the cluster. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10202156, ECO:0000269|PubMed:11094092}. +Q9JJH7 TRPM5_MOUSE Transient receptor potential cation channel subfamily M member 5 (Long transient receptor potential channel 5) (LTrpC-5) (LTrpC5) (MLSN1- and TRP-related gene 1 protein) 1158 130,844 Alternative sequence (4); Chain (1); Coiled coil (1); Frameshift (2); Mutagenesis (3); Sequence conflict (4); Topological domain (7); Transmembrane (6) TRANSMEM 646 666 Helical. {ECO:0000255}.; TRANSMEM 733 753 Helical. {ECO:0000255}.; TRANSMEM 811 831 Helical. {ECO:0000255}.; TRANSMEM 835 855 Helical. {ECO:0000255}.; TRANSMEM 872 892 Helical. {ECO:0000255}.; TRANSMEM 954 974 Helical. {ECO:0000255}. TOPO_DOM 1 645 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 667 732 Extracellular. {ECO:0000255}.; TOPO_DOM 754 810 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 832 834 Extracellular. {ECO:0000255}.; TOPO_DOM 856 871 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 893 953 Extracellular. {ECO:0000255}.; TOPO_DOM 975 1158 Cytoplasmic. {ECO:0000255}. FUNCTION: Voltage-modulated Ca(2+)-activated, monovalent cation channel (VCAM) that mediates a transient membrane depolarization and plays a central role in taste transduction. Monovalent-specific, non-selective cation channel that mediates the transport of Na(+), K(+) and Cs(+) ions equally well. Activated directly by increases in intracellular Ca(2+), but is impermeable to it. Gating is voltage-dependent and displays rapid activation and deactivation kinetics upon channel stimulation even during sustained elevations in Ca(2+). Also activated by a fast intracellular Ca(2+) increase in response to inositol 1,4,5-triphosphate-producing receptor agonists. The channel is blocked by extracellular acidification. External acidification has 2 effects, a fast reversible block of the current and a slower irreversible enhancement of current inactivation. Is a highly temperature-sensitive, heat activated channel showing a steep increase of inward currents at temperatures between 15 and 35 degrees Celsius. Heat activation is due to a shift of the voltage-dependent activation curve to negative potentials. Activated by arachidonic acid in vitro. May be involved in perception of bitter, sweet and umami tastes. May also be involved in sensing semiochemicals. {ECO:0000269|PubMed:12842017, ECO:0000269|PubMed:14657398, ECO:0000269|PubMed:15731110, ECO:0000269|PubMed:16355226, ECO:0000269|PubMed:16436689, ECO:0000269|PubMed:16935556, ECO:0000269|PubMed:17267604, ECO:0000269|PubMed:17522321}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8TD43, ECO:0000255}. TISSUE SPECIFICITY: Strongly expressed in liver, heart, testis, brain and kidney. Detected in fetal liver, kidney, spleen, brain, heart and lung, and in adult skin, eyes, spleen, stomach, small intestine, colon, lung, bladder, pancreas and thymus. Biallelically expressed at all stages and tissues examined. Also expressed in subsets of taste receptor cells of the tongue, in olfactory sensory neurons of the main olfactory epithelium and in the vomeronasal organ. {ECO:0000269|PubMed:10903843, ECO:0000269|PubMed:12368808, ECO:0000269|PubMed:17267604, ECO:0000269|PubMed:17610722}. +Q8BGE4 SUSD6_MOUSE Sushi domain-containing protein 6 (Drago) 302 31,978 Chain (1); Disulfide bond (2); Domain (1); Signal peptide (1); Transmembrane (1) TRANSMEM 120 140 Helical. {ECO:0000255}. FUNCTION: May play a role in growth-suppressive activity and cell death. May be involved in the production of chemokine molecules in umbilical vein endothelial cells (HUVECs) cultured in THP1 monocyte LPS-induced medium (By similarity). Plays a role in preventing tumor onset (PubMed:24652652). {ECO:0000250|UniProtKB:Q92537, ECO:0000269|PubMed:24652652}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. +Q9WTR1 TRPV2_MOUSE Transient receptor potential cation channel subfamily V member 2 (TrpV2) (Growth factor-regulated calcium channel) (GRC) (Osm-9-like TRP channel 2) (OTRPC2) 756 85,965 Chain (1); Glycosylation (1); Intramembrane (1); Modified residue (4); Region (1); Repeat (6); Sequence conflict (1); Topological domain (6); Transmembrane (6) INTRAMEM 568 604 Pore-forming. {ECO:0000255}. TRANSMEM 388 408 Helical. {ECO:0000255}.; TRANSMEM 429 449 Helical. {ECO:0000255}.; TRANSMEM 456 476 Helical. {ECO:0000255}.; TRANSMEM 491 511 Helical. {ECO:0000255}.; TRANSMEM 533 553 Helical. {ECO:0000255}.; TRANSMEM 617 637 Helical. {ECO:0000255}. TOPO_DOM 1 387 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 409 428 Extracellular. {ECO:0000255}.; TOPO_DOM 450 455 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 477 490 Extracellular. {ECO:0000255}.; TOPO_DOM 512 532 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 638 756 Cytoplasmic. {ECO:0000255}. FUNCTION: Calcium-permeable, non-selective cation channel with an outward rectification. Seems to be regulated, at least in part, by IGF-I, PDGF and neuropeptide head activator. May transduce physical stimuli in mast cells. Activated by temperatures higher than 52 degrees Celsius; is not activated by vanilloids and acidic pH. {ECO:0000269|PubMed:10559903, ECO:0000269|PubMed:11707512}. PTM: N-glycosylated. {ECO:0000269|PubMed:10559903}.; PTM: Phosphorylated by PKA. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cytoplasm. Melanosome {ECO:0000250}. Note=Translocates from the cytoplasm to the plasma membrane upon ligand stimulation. SUBUNIT: Homotetramer (Probable). Interacts with a cAMP-dependent protein kinase type II regulatory subunit (PRKAR2A or PRKAR2B) and ACBD3. Interacts with SLC50A1; the interaction probably occurs intracellularly and depends on TRPV2 N-glycosylation (By similarity). {ECO:0000250, ECO:0000305}. TISSUE SPECIFICITY: Abundantly expressed in spleen, placenta, skeleton muscle, lung and brain. {ECO:0000269|PubMed:10559903}. +Q02844 TRYB1_MOUSE Tryptase (EC 3.4.21.59) (Mast cell protease 7) (mMCP-7) (Tryptase alpha/beta-1) 273 30,337 Active site (3); Alternative sequence (2); Chain (1); Disulfide bond (4); Domain (1); Glycosylation (2); Propeptide (1); Signal peptide (1) FUNCTION: Tryptase is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type. May play a role in innate immunity (By similarity). {ECO:0000250|UniProtKB:P21845}. +Q61187 TS101_MOUSE Tumor susceptibility gene 101 protein (ESCRT-I complex subunit TSG101) 391 44,124 Chain (1); Coiled coil (1); Domain (2); Initiator methionine (1); Modified residue (2); Motif (1); Region (1) FUNCTION: Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Binds to ubiquitinated cargo proteins and is required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies (MVBs). Mediates the association between the ESCRT-0 and ESCRT-I complex. Required for completion of cytokinesis; the function requires CEP55. May be involved in cell growth and differentiation. Acts as a negative growth regulator. Required for the exosomal release of SDCBP, CD63 and syndecan (By similarity). It may also play a role in the extracellular release of microvesicles that differ from the exosomes (By similarity). {ECO:0000250|UniProtKB:Q99816}. PTM: Monoubiquitinated at multiple sites by LRSAM1 and by MGRN1. Ubiquitination inactivates it, possibly by regulating its shuttling between an active membrane-bound protein and an inactive soluble form. Ubiquitination by MGRN1 requires the presence of UBE2D1. {ECO:0000250|UniProtKB:Q99816}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q99816}. Early endosome membrane {ECO:0000250|UniProtKB:Q99816}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q99816}; Cytoplasmic side {ECO:0000250|UniProtKB:Q99816}. Late endosome membrane {ECO:0000250|UniProtKB:Q99816}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q99816}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q99816}. Midbody, Midbody ring {ECO:0000250|UniProtKB:Q99816}. Nucleus {ECO:0000250|UniProtKB:Q99816}. Note=Mainly cytoplasmic. Membrane-associated when active and soluble when inactive. Nuclear localization is cell cycle-dependent. Interaction with CEP55 is required for localization to the midbody during cytokinesis. {ECO:0000250|UniProtKB:Q99816}. SUBUNIT: Component of the ESCRT-I complex (endosomal sorting complex required for transport I) which consists of TSG101, VPS28, a VPS37 protein (VPS37A to -D) and MVB12A or MVB12B in a 1:1:1:1 stoichiometry. Interacts with VPS37A, VPS37B and VPS37C. Component of an ESCRT-I complex (endosomal sorting complex required for transport I) which consists of TSG101, VPS28, VPS37A and UBAP1 in a 1:1:1:1 stoichiometry. Interacts with DMAP1 (PubMed:10888872). Interacts with GMCL (PubMed:12927808). Interacts with ubiquitin, stathmin and AATF (By similarity). Interacts with HGS; the interaction mediates the association with the ESCRT-0 complex (PubMed:12802020). Interacts with GGA1 and GGA3. Interacts (via UEV domain) with PDCD6IP/AIP1. Interacts with VPS28, SNF8 and VPS36. Self-associates. Interacts with MVB12A; the association appears to be mediated by the TSG101-VPS37 binary subcomplex. Interacts with VPS37D. Interacts with LRSAM1. Interacts with CEP55; the interaction is required for cytokinesis (By similarity). Interacts with PDCD6. Interacts with LITAF (By similarity). Interacts with murine leukemia virus Gag polyprotein (via PSAP motif) (PubMed:15908698). Interacts with MGRN1 (PubMed:19703557). Interacts with ARRDC1; recruits TSG101 to the plasma membrane (By similarity). {ECO:0000250|UniProtKB:Q6IRE4, ECO:0000250|UniProtKB:Q99816, ECO:0000269|PubMed:10888872, ECO:0000269|PubMed:12802020, ECO:0000269|PubMed:12927808, ECO:0000269|PubMed:15908698, ECO:0000269|PubMed:19703557}. DOMAIN: The UEV domain is required for the interaction of the complex with ubiquitin.; DOMAIN: The coiled coil domain may interact with stathmin. TISSUE SPECIFICITY: Ubiquitous. Higher expression in brain and mammary gland. Lower expression in liver and tumoral tissues. +Q99PG6 TS1R1_MOUSE Taste receptor type 1 member 1 (G-protein coupled receptor 70) 842 93,426 Chain (1); Glycosylation (7); Natural variant (7); Sequence conflict (6); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 569 589 Helical; Name=1. {ECO:0000255}.; TRANSMEM 605 625 Helical; Name=2. {ECO:0000255}.; TRANSMEM 641 661 Helical; Name=3. {ECO:0000255}.; TRANSMEM 682 702 Helical; Name=4. {ECO:0000255}.; TRANSMEM 726 746 Helical; Name=5. {ECO:0000255}.; TRANSMEM 763 783 Helical; Name=6. {ECO:0000255}.; TRANSMEM 790 810 Helical; Name=7. {ECO:0000255}. TOPO_DOM 20 568 Extracellular. {ECO:0000255}.; TOPO_DOM 590 604 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 626 640 Extracellular. {ECO:0000255}.; TOPO_DOM 662 681 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 703 725 Extracellular. {ECO:0000255}.; TOPO_DOM 747 762 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 784 789 Extracellular. {ECO:0000255}.; TOPO_DOM 811 842 Cytoplasmic. {ECO:0000255}. FUNCTION: Putative taste receptor. TAS1R1/TAS1R3 responds to the umami taste stimulus (the taste of monosodium glutamate) and also to most of the 20 standard L-amino acids, but not to their D-enantiomers or other compounds. Sequence differences within and between species can significantly influence the selectivity and specificity of taste responses. {ECO:0000269|PubMed:11894099}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBUNIT: Forms heterodimers with TAS1R3. TISSUE SPECIFICITY: Expressed strongly only in fungiform papillae. {ECO:0000269|PubMed:11319557}. +Q925D8 TS1R3_MOUSE Taste receptor type 1 member 3 (Saccharin preference protein) (Sweet taste receptor T1R3) 858 94,561 Chain (1); Glycosylation (10); Natural variant (9); Sequence conflict (1); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 573 593 Helical; Name=1. {ECO:0000255}.; TRANSMEM 611 631 Helical; Name=2. {ECO:0000255}.; TRANSMEM 645 665 Helical; Name=3. {ECO:0000255}.; TRANSMEM 688 708 Helical; Name=4. {ECO:0000255}.; TRANSMEM 736 756 Helical; Name=5. {ECO:0000255}.; TRANSMEM 768 788 Helical; Name=6. {ECO:0000255}.; TRANSMEM 797 817 Helical; Name=7. {ECO:0000255}. TOPO_DOM 21 572 Extracellular. {ECO:0000255}.; TOPO_DOM 594 610 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 632 644 Extracellular. {ECO:0000255}.; TOPO_DOM 666 687 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 709 735 Extracellular. {ECO:0000255}.; TOPO_DOM 757 767 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 789 796 Extracellular. {ECO:0000255}.; TOPO_DOM 818 858 Cytoplasmic. {ECO:0000255}. FUNCTION: Putative taste receptor. TAS1R1/TAS1R3 responds to the umami taste stimulus (the taste of monosodium glutamate) and also to most of the 20 standard L-amino acids, but not to their D-enantiomers or other compounds. TAS1R2/TAS1R3 recognizes diverse natural and synthetic sweeteners. TAS1R3 is essential for the recognition and response to the disaccharide trehalose. Sequence differences within and between species can significantly influence the selectivity and specificity of taste responses. {ECO:0000269|PubMed:11894099, ECO:0000269|PubMed:12892531}. PTM: The Thr-60 variant is predicted to introduce a novel N-linked glycosylation site at Asn-58. The addition of even a short carbohydrate group at Asn-58 is predicted to disrupt one of the contact surfaces required for stability of a dimer. Therefore a Thr-60 variant N-glycosylated at Asn-58 is predicted to be precluded from forming homodimers or heterodimers. {ECO:0000269|PubMed:11326277}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBUNIT: Forms homodimers or heterodimers with TAS1R1 and TAS1R2. TISSUE SPECIFICITY: Expressed in circumvallate, foliate and fungiform taste papillae as well as in taste buds on the palate. Also expressed in testis. Not expressed in brain, heart, kidney, liver or spleen. The topographic distribution in various taste papillae is different from those of other T1R members. {ECO:0000269|PubMed:11319557, ECO:0000269|PubMed:11322794, ECO:0000269|PubMed:11326277, ECO:0000269|PubMed:11331418}. +Q9DA44 TSACC_MOUSE TSSK6-activating co-chaperone protein 124 13,476 Chain (1) FUNCTION: Co-chaperone that facilitates HSP-mediated activation of TSSK6. {ECO:0000250}. SUBUNIT: Interacts with HSP70. Associates with HSP90. Interacts with TSSK6; this interaction is direct and recruits TSACC to HSP90 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: In testis, expressed in the inner luminal layer of the seminiferous tubules. {ECO:0000269|PubMed:20829357}. +P09925 SURF1_MOUSE Surfeit locus protein 1 306 34,798 Chain (1); Sequence conflict (3); Transmembrane (2) TRANSMEM 68 86 Helical. {ECO:0000255}.; TRANSMEM 280 300 Helical. {ECO:0000255}. FUNCTION: Component of the MITRAC (mitochondrial translation regulation assembly intermediate of cytochrome c oxidase complex) complex, that regulates cytochrome c oxidase assembly. {ECO:0000250|UniProtKB:Q15526}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Component of the MITRAC (mitochondrial translation regulation assembly intermediate of cytochrome c oxidase complex) complex, the core components of this complex being COA3/MITRAC12 and COX14. Interacts with COA3. {ECO:0000250|UniProtKB:Q15526}. +P18419 SVS4_MOUSE Seminal vesicle secretory protein 4 (Seminal vesicle protein 2) (Seminal vesicle secretory protein IV) (SVS IV) 113 12,515 Chain (1); Compositional bias (1); Sequence conflict (4); Signal peptide (1) SUBCELLULAR LOCATION: Secreted, extracellular space. TISSUE SPECIFICITY: Testis. +Q8CGC7 SYEP_MOUSE Bifunctional glutamate/proline--tRNA ligase (Bifunctional aminoacyl-tRNA synthetase) [Includes: Glutamate--tRNA ligase (EC 6.1.1.17) (Glutamyl-tRNA synthetase) (GluRS); Proline--tRNA ligase (EC 6.1.1.15) (Prolyl-tRNA synthetase) (ProRS)] 1512 170,079 Binding site (5); Chain (1); Compositional bias (1); Domain (3); Metal binding (4); Modified residue (18); Motif (2); Mutagenesis (2); Nucleotide binding (4); Region (4); Sequence caution (1); Sequence conflict (5) FUNCTION: Multifunctional protein which is primarily part of the aminoacyl-tRNA synthetase multienzyme complex, also know as multisynthetase complex, that catalyzes the attachment of the cognate amino acid to the corresponding tRNA in a two-step reaction: the amino acid is first activated by ATP to form a covalent intermediate with AMP and is then transferred to the acceptor end of the cognate tRNA (By similarity). The phosphorylation of EPRS, induced by interferon-gamma, dissociates the protein from the aminoacyl-tRNA synthetase multienzyme complex and recruits it to the GAIT complex that binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin), suppressing their translation. Interferon-gamma can therefore redirect, in specific cells, the EPRS function from protein synthesis to translation inhibition (PubMed:23071094). Also functions as an effector of the mTORC1 signaling pathway by promoting, through SLC27A1, the uptake of long-chain fatty acid by adipocytes. Thereby, it also plays a role in fat metabolism and more indirectly influences lifespan (PubMed:28178239). {ECO:0000250|UniProtKB:P07814, ECO:0000269|PubMed:23071094, ECO:0000269|PubMed:28178239}. PTM: Phosphorylated at Ser-999 by RPS6KB1; triggers EPRS release from the aminoacyl-tRNA synthetase multienzyme complex. In monocytes, the IFN-gamma-induced phosphorylation at Ser-999 releases EPRS from the aminoacyl-tRNA synthetase multienzyme complex, allowing its association with the GAIT complex. Phosphorylation at Ser-999 is specifically required for the RPL13A-mediated interaction of the GAIT complex with eIF4G (By similarity). Phosphorylation at Ser-999 by RPS6KB1, is also induced by insulin through activation of the mTORC1 signaling pathway and promotes the interaction of EPRS with SLC27A1 (PubMed:28178239). {ECO:0000250|UniProtKB:P07814, ECO:0000269|PubMed:28178239}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P07814}. Membrane {ECO:0000269|PubMed:28178239}; Peripheral membrane protein {ECO:0000305|PubMed:28178239}. Note=Translocates from cytosol to membranes upon phosphorylation at Ser-999. {ECO:0000305|PubMed:28178239}. SUBUNIT: Homodimer. Part of the aminoacyl-tRNA synthetase multienzyme complex, also know as multisynthetase complex, that is composed of the tRNA ligases for Arg (RARS), Asp (DARS), Gln (QARS), Ile (IARS), Leu (LARS), Lys (KARS), Met (MARS) the bifunctional ligase for Glu and Pro (EPRS) and the auxiliary subunits AIMP1/p43, AIMP2/p38 and EEF1E1/p18. Forms a linear complex that contains MARS, EEF1E1, EPRS and AIMP2 that is at the core of the multisubunit complex (PubMed:12060739). Interacts with TARSL2 (By similarity). Interacts with DUS2L (By similarity). Component of the GAIT complex which is composed of EPRS, RPL13A and GAPDH (PubMed:23071094). Interacts (phosphorylated at Ser-999) with SLC27A1; mediates the translocation of SLC27A1 from the cytoplasm to the plasma membrane thereby increasing the uptake of long-chain fatty acids (PubMed:28178239). {ECO:0000250|UniProtKB:P07814, ECO:0000269|PubMed:12060739, ECO:0000269|PubMed:23071094, ECO:0000269|PubMed:28178239}. DOMAIN: The WHEP-TRS domains are involved in RNA binding. {ECO:0000250|UniProtKB:Q7SIA2}. +P07309 TTHY_MOUSE Transthyretin (Prealbumin) 147 15,776 Beta strand (9); Binding site (2); Chain (1); Glycosylation (1); Helix (1); Modified residue (2); Region (1); Signal peptide (1); Turn (2) FUNCTION: Thyroid hormone-binding protein. Probably transports thyroxine from the bloodstream to the brain. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Homotetramer. Dimer of dimers. In the homotetramer, subunits assemble around a central channel that can accommodate two ligand molecules. Interacts with RBP4 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Detected in plasma (at protein level). Detected in liver. +A4Q9E4 TTLL2_MOUSE Probable tubulin polyglutamylase TTLL2 (EC 6.-.-.-) (Tubulin--tyrosine ligase-like protein 2) 540 62,109 Binding site (2); Chain (1); Domain (1); Nucleotide binding (1) FUNCTION: Probable tubulin polyglutamylase that forms polyglutamate side chains on tubulin. Probably acts when complexed with other proteins. {ECO:0000269|PubMed:17499049}. TISSUE SPECIFICITY: Widely expressed with highest levels in brain, kidney, liver and testis. {ECO:0000269|PubMed:17499049}. +Q80UG8 TTLL4_MOUSE Tubulin polyglutamylase TTLL4 (EC 6.-.-.-) (Tubulin--tyrosine ligase-like protein 4) 1193 132,530 Binding site (2); Chain (1); Compositional bias (3); Domain (1); Modified residue (1); Nucleotide binding (1); Region (1) FUNCTION: Glutamylase which preferentially modifies beta-tubulin and non-tubulin proteins, such as NAP1L1, NAP1L4 and CGAS (PubMed:17499049, PubMed:21074048, PubMed:20530212). Involved in the side-chain initiation step of the polyglutamylation reaction rather than in the elongation step (PubMed:17499049, PubMed:21074048). Involved in formation of short side-chains (PubMed:20530212). Mediates initiation of polyglutamylation of nucleosome assembly proteins NAP1L1 and NAP1L4 (PubMed:17499049). Also acts as a monoglutamylase: generates monoglutamylation of CGAS, leading to impair the nucleotidyltransferase activity of CGAS (PubMed:26829768). {ECO:0000269|PubMed:17499049, ECO:0000269|PubMed:20530212, ECO:0000269|PubMed:21074048, ECO:0000269|PubMed:26829768}. SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000269|PubMed:17499049}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:17499049}. Note=Located in cilia. In some cells, also found in basal bodies. {ECO:0000269|PubMed:17499049}. DOMAIN: The flexible c-MTBD (cationic microtubule binding domain) region mediates binding to microtubules. It is positively charged and becomes ordered when bound to microtubules: it interacts with a negatively charged patch on tubulin. The presence of positive charges in the c-MTBD region is essential for proper binding. {ECO:0000250|UniProtKB:Q14679, ECO:0000250|UniProtKB:Q6ZT98}. TISSUE SPECIFICITY: Widely expressed with highest levels in testis. {ECO:0000269|PubMed:17499049}. +Q8BWP5 TTPA_MOUSE Alpha-tocopherol transfer protein (Alpha-TTP) 278 32,014 Beta strand (7); Binding site (4); Chain (1); Domain (1); Helix (18); Mutagenesis (3); Turn (3) FUNCTION: Binds alpha-tocopherol, enhances its transfer between separate membranes, and stimulates its release from liver cells. Binds both phosphatidylinol 3,4-bisphosphate and phosphatidylinol 4,5-bisphosphate; the resulting conformation change is important for the release of the bound alpha-tocopherol. {ECO:0000269|PubMed:23599266}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Monomer and homotetramer. Phosphatidylinol 4,5-bisphosphate binding induces the formation of homotetramers. Phosphatidylinol 3,4-bisphosphate is less efficient in inducing tetramerization. {ECO:0000269|PubMed:23599266}. +Q6P5F7 TTYH3_MOUSE Protein tweety homolog 3 (mTTY3) 524 57,714 Alternative sequence (2); Chain (1); Erroneous termination (1); Glycosylation (3); Modified residue (3); Sequence conflict (1); Topological domain (6); Transmembrane (5) TRANSMEM 43 63 Helical; Name=1. {ECO:0000255}.; TRANSMEM 87 107 Helical; Name=2. {ECO:0000255}.; TRANSMEM 212 232 Helical; Name=3. {ECO:0000255}.; TRANSMEM 237 257 Helical; Name=4. {ECO:0000255}.; TRANSMEM 387 407 Helical; Name=5. {ECO:0000255}. TOPO_DOM 1 42 Extracellular. {ECO:0000255}.; TOPO_DOM 64 86 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 108 211 Extracellular. {ECO:0000255}.; TOPO_DOM 233 236 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 258 386 Extracellular. {ECO:0000255}.; TOPO_DOM 408 524 Cytoplasmic. {ECO:0000255}. FUNCTION: Probable large-conductance Ca(2+)-activated chloride channel. May play a role in Ca(2+) signal transduction (By similarity). {ECO:0000250}. PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Expressed in excitable tissues. Expressed in the brain, heart, skeletal muscle, colon, spleen, kidney and peripheral blood leukocytes. Also expressed in fat, the pancreas, thymus, and uterus. {ECO:0000269|PubMed:15010458}. +P50586 TUB_MOUSE Tubby protein 505 55,362 Alternative sequence (1); Beta strand (17); Chain (1); Compositional bias (2); Erroneous initiation (1); Helix (7); Mutagenesis (2); Turn (2) FUNCTION: Functions in signal transduction from heterotrimeric G protein-coupled receptors. Binds to membranes containing phosphatidylinositol 4,5-bisphosphate. Can bind DNA (in vitro). May contribute to the regulation of transcription in the nucleus. Could be involved in the hypothalamic regulation of body weight. Contribute to stimulation of phagocytosis of apoptotic retinal pigment epithelium (RPE) cells and macrophages (By similarity). {ECO:0000250, ECO:0000269|PubMed:10591637, ECO:0000269|PubMed:11375483}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Secreted. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Note=Binds phospholipid and is anchored to the plasma membrane through binding phosphatidylinositol 4,5-bisphosphate. Is released upon activation of phospholipase C. Translocates from the plasma membrane to the nucleus upon activation of guanine nucleotide-binding protein G(q) subunit alpha. Does not have a cleavable signal peptide and is secreted by a non-conventional pathway. SUBUNIT: Interacts with GNAQ. Interacts with TULP1. {ECO:0000269|PubMed:11375483, ECO:0000269|PubMed:19837063}. DISEASE: Note=Defects in Tub are the cause of maturity-onset obesity, insulin resistance and sensory deficits. +O08970 TUFT1_MOUSE Tuftelin 390 44,576 Alternative sequence (2); Chain (1); Coiled coil (2) FUNCTION: Involved in the mineralization and structural organization of enamel. {ECO:0000250|UniProtKB:P27628}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P27628}. Note=Secreted at a very early stage of enamel formation, concentrated at the dentin-enamel junction and tightly bound to the surface of the growing crystallites. {ECO:0000250|UniProtKB:P27628}. SUBUNIT: Interacts with TFIP11. May form oligomers. {ECO:0000269|PubMed:10806191}. TISSUE SPECIFICITY: Ameloblasts, and also non-odontogenic tissues including kidney, lung, liver and testis. {ECO:0000269|PubMed:9839784}. +Q9WVF8 TUSC2_MOUSE Tumor suppressor candidate 2 (Fusion 1 protein) (Fus-1 protein) (PDGFA-associated protein 2) 110 12,136 Chain (1); Initiator methionine (1); Lipidation (1); Modified residue (1) PTM: Myristoylation is required for tumor suppressor activity. {ECO:0000250}. +Q9R0N6 SYT8_MOUSE Synaptotagmin-8 (Synaptotagmin VIII) (SytVIII) 395 44,093 Alternative sequence (2); Chain (1); Domain (2); Topological domain (2); Transmembrane (1) TRANSMEM 45 65 Helical; Signal-anchor for type III membrane protein. {ECO:0000255}. TOPO_DOM 1 44 Extracellular. {ECO:0000255}.; TOPO_DOM 66 395 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in the trafficking and exocytosis of secretory vesicles in non-neuronal tissues. Mediates Ca(2+)-regulation of exocytosis acrosomal reaction in sperm. May mediate Ca(2+)-regulation of exocytosis in insulin secreted cells. {ECO:0000269|PubMed:11751263, ECO:0000269|PubMed:15774481, ECO:0000269|PubMed:7791877}. SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Single-pass type III membrane protein. Cytoplasmic vesicle, secretory vesicle, acrosome. SUBUNIT: Homodimer or homooligomer. Homodimerization and homooligomerization do not depend on Ca(2+). Interacts with SYNCRIP isoform 2 C-terminus. Binds inositol 1,3,4,5-tetrakisphosphate (IP4). Binds to AP2 in a Ca(2+)-independent manner. Interacts with STX1A, STX1B and STX2; the interaction is Ca(2+)-dependent. {ECO:0000269|PubMed:10734137, ECO:0000269|PubMed:15774481, ECO:0000269|PubMed:7791877, ECO:0000269|PubMed:9575177}. DOMAIN: The first C2 domain/C2A does not mediate Ca(2+)-dependent phospholipid binding.; DOMAIN: The second C2 domain/C2B is responsible for SYNCRIP and inositol 1,3,4,5-tetrakisphosphate (IP4)-binding. TISSUE SPECIFICITY: Ubiquitous. Detected in testis and brain. Expressed in primary neurons, neuroendocrine and endocrine cells. {ECO:0000269|PubMed:11751263, ECO:0000269|PubMed:16386321}. +Q99N42 TYPH_MOUSE Thymidine phosphorylase (TP) (EC 2.4.2.4) (TdRPase) 471 49,336 Binding site (4); Chain (1); Modified residue (1) Pyrimidine metabolism; dTMP biosynthesis via salvage pathway; dTMP from thymine: step 1/2. FUNCTION: Catalyzes the reversible phosphorolysis of thymidine. The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis (By similarity). {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +A2RSX7 TYW5_MOUSE tRNA wybutosine-synthesizing protein 5 (EC 1.14.11.42) (tRNA(Phe) (7-(3-amino-3-carboxypropyl)wyosine(37)-C(2))-hydroxylase) 315 36,633 Alternative sequence (2); Binding site (3); Chain (1); Domain (1); Metal binding (3); Sequence conflict (1) tRNA modification; wybutosine-tRNA(Phe) biosynthesis. FUNCTION: tRNA hydroxylase that acts as a component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA. Catalyzes the hydroxylation of 7-(a-amino-a-carboxypropyl)wyosine (yW-72) into undermodified hydroxywybutosine (OHyW*). OHyW* being further transformed into hydroxywybutosine (OHyW) by LCMT2/TYW4. OHyW is a derivative of wybutosine found in higher eukaryotes (By similarity). {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +E9Q9U0 U17PB_MOUSE Ubiquitin carboxyl-terminal hydrolase 17-like protein B (USP17-B) (EC 3.4.19.12) (Deubiquitinating enzyme 1A) 468 52,114 Active site (2); Alternative sequence (1); Chain (1); Domain (1); Mutagenesis (1); Sequence conflict (8) FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes. {ECO:0000269|PubMed:14583620}. PTM: Ubiquitinated. {ECO:0000269|PubMed:14583620}. TISSUE SPECIFICITY: Detected in brain, heart, liver, lung, kidney, ovary and spleen. {ECO:0000269|PubMed:14583620}. +G5E8G2 U17PD_MOUSE Ubiquitin carboxyl-terminal hydrolase 17-like protein D (EC 3.4.19.12) (Deubiquitinating enzyme 2A) 545 61,450 Active site (2); Chain (1); Domain (1); Mutagenesis (1); Sequence conflict (6) FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes that may include cell proliferation, progression through the cell cycle, apoptosis, cell migration, and the cellular response to viral infection. {ECO:0000269|PubMed:11468161}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6R6M4}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q6R6M4}. TISSUE SPECIFICITY: Detected in T-cell, myeloid, and embryonic stem cell lines. {ECO:0000269|PubMed:11468161}. +Q9Z1Q9 SYVC_MOUSE Valine--tRNA ligase (EC 6.1.1.9) (Protein G7a) (Valyl-tRNA synthetase) (ValRS) 1263 140,215 Binding site (1); Chain (1); Domain (1); Initiator methionine (1); Modified residue (4); Motif (2); Sequence conflict (4) SUBUNIT: Forms high-molecular-mass aggregates with elongation factor 1. {ECO:0000250}. +Q99MX7 T121B_MOUSE Transmembrane protein 121B (Cat eye syndrome critical region protein 6 homolog) 572 58,158 Chain (1); Compositional bias (7); Modified residue (3) +Q9WUF1 V1R49_MOUSE Vomeronasal type-1 receptor 49 (Vomeronasal receptor VRi2) (Vomeronasal type-1 receptor B2) 310 35,523 Chain (1); Disulfide bond (1); Glycosylation (2); Topological domain (8); Transmembrane (7) TRANSMEM 13 33 Helical; Name=1. {ECO:0000255}.; TRANSMEM 51 71 Helical; Name=2. {ECO:0000255}.; TRANSMEM 94 114 Helical; Name=3. {ECO:0000255}.; TRANSMEM 136 156 Helical; Name=4. {ECO:0000255}.; TRANSMEM 191 211 Helical; Name=5. {ECO:0000255}.; TRANSMEM 239 259 Helical; Name=6. {ECO:0000255}.; TRANSMEM 270 290 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 12 Extracellular. {ECO:0000255}.; TOPO_DOM 34 50 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 72 93 Extracellular. {ECO:0000255}.; TOPO_DOM 115 135 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 157 190 Extracellular. {ECO:0000255}.; TOPO_DOM 212 238 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 260 269 Extracellular. {ECO:0000255}.; TOPO_DOM 291 310 Cytoplasmic. {ECO:0000255}. FUNCTION: Putative pheromone receptor implicated in the regulation of social and reproductive behavior. {ECO:0000269|PubMed:10219241, ECO:0000269|PubMed:12214233}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Expressed in a subset of sensory neurons located in the apical layer of the vomeronasal organ. {ECO:0000269|PubMed:10219241}. +Q8VIC6 V1R51_MOUSE Vomeronasal type-1 receptor 51 (Pheromone receptor 1) (Vomeronasal type-1 receptor A1) (mV1R1) (Vomeronasal type-1 receptor A8) 319 36,533 Chain (1); Disulfide bond (1); Erroneous initiation (3); Glycosylation (1); Sequence conflict (1); Topological domain (8); Transmembrane (7) TRANSMEM 32 52 Helical; Name=1. {ECO:0000255}.; TRANSMEM 66 86 Helical; Name=2. {ECO:0000255}.; TRANSMEM 110 130 Helical; Name=3. {ECO:0000255}.; TRANSMEM 151 171 Helical; Name=4. {ECO:0000255}.; TRANSMEM 204 224 Helical; Name=5. {ECO:0000255}.; TRANSMEM 255 275 Helical; Name=6. {ECO:0000255}.; TRANSMEM 286 306 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 31 Extracellular. {ECO:0000255}.; TOPO_DOM 53 65 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 87 109 Extracellular. {ECO:0000255}.; TOPO_DOM 131 150 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 172 203 Extracellular. {ECO:0000255}.; TOPO_DOM 225 254 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 276 285 Extracellular. {ECO:0000255}.; TOPO_DOM 307 319 Cytoplasmic. {ECO:0000255}. FUNCTION: Putative pheromone receptor implicated in the regulation of social as well as reproductive behavior. {ECO:0000269|PubMed:12214233}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Expressed in a subset of sensory neurons located in the apical layer of the vomeronasal organ. {ECO:0000269|PubMed:9757043}. +E9Q6I0 V2116_MOUSE Vomeronasal type-2 receptor 116 (Vomeronasal type-2 receptor P5) 856 97,704 Chain (1); Glycosylation (1); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 587 607 Helical. {ECO:0000255}.; TRANSMEM 623 643 Helical. {ECO:0000255}.; TRANSMEM 659 679 Helical. {ECO:0000255}.; TRANSMEM 691 711 Helical. {ECO:0000255}.; TRANSMEM 746 766 Helical. {ECO:0000255}.; TRANSMEM 779 799 Helical. {ECO:0000255}.; TRANSMEM 807 827 Helical. {ECO:0000255}. TOPO_DOM 19 586 Extracellular. {ECO:0000255}.; TOPO_DOM 608 622 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 644 658 Extracellular. {ECO:0000255}.; TOPO_DOM 680 690 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 712 745 Extracellular. {ECO:0000255}.; TOPO_DOM 767 778 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 800 806 Extracellular. {ECO:0000255}.; TOPO_DOM 828 856 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for the Esp1 pheromone. Mediates the response to Esp1 which enhances female sexual receptive behavior (lordosis) upon male mounting, resulting in successful copulation. {ECO:0000269|PubMed:20596023, ECO:0000269|PubMed:23576433, ECO:0000269|Ref.3}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Expressed in the vomeronasal organ. {ECO:0000269|PubMed:20596023}. +Q3TPR7 T184C_MOUSE Transmembrane protein 184C (Transmembrane protein 34) 525 60,043 Alternative sequence (1); Chain (1); Sequence conflict (2); Transmembrane (7) TRANSMEM 17 37 Helical. {ECO:0000255}.; TRANSMEM 48 68 Helical. {ECO:0000255}.; TRANSMEM 83 103 Helical. {ECO:0000255}.; TRANSMEM 121 141 Helical. {ECO:0000255}.; TRANSMEM 212 232 Helical. {ECO:0000255}.; TRANSMEM 254 274 Helical. {ECO:0000255}.; TRANSMEM 287 307 Helical. {ECO:0000255}. FUNCTION: Possible tumor suppressor which may play a role in cell growth. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8R3R5 T185B_MOUSE Transmembrane protein 185B (Erythropoietin-induced EST 3-2) (Protein FAM11B) 350 40,701 Chain (1); Frameshift (1); Transmembrane (7) TRANSMEM 16 36 Helical. {ECO:0000255}.; TRANSMEM 41 61 Helical. {ECO:0000255}.; TRANSMEM 81 101 Helical. {ECO:0000255}.; TRANSMEM 111 131 Helical. {ECO:0000255}.; TRANSMEM 168 188 Helical. {ECO:0000255}.; TRANSMEM 211 231 Helical. {ECO:0000255}.; TRANSMEM 240 260 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q80ZM7 T2AG_MOUSE Transcription initiation factor IIA subunit 2 (General transcription factor IIA subunit 2) (Transcription initiation factor IIA gamma chain) (TFIIA-gamma) 109 12,473 Chain (1); Sequence caution (1) FUNCTION: TFIIA is a component of the transcription machinery of RNA polymerase II and plays an important role in transcriptional activation. TFIIA in a complex with TBP mediates transcriptional activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: TFIIA is a heterodimer of the large unprocessed subunit 1 and a small subunit gamma. It was originally believed to be a heterotrimer of an alpha (p35), a beta (p19) and a gamma subunit (p12). Interacts with NCOA6 general coactivator. TFIIA forms a complex with TBP. Interacts with HSF1 (via transactivation domain). Interacts with HSF1 (via transactivation domain). Interacts with HSF1 (via transactivation domain). {ECO:0000250|UniProtKB:P52656, ECO:0000250|UniProtKB:P52657}. +Q7M720 T2R13_MOUSE Taste receptor type 2 member 13 (T2R13) (Taste receptor type 2 member 121) (T2R121) (mT2R48) 305 35,521 Chain (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 8 28 Helical; Name=1. {ECO:0000255}.; TRANSMEM 44 64 Helical; Name=2. {ECO:0000255}.; TRANSMEM 89 109 Helical; Name=3. {ECO:0000255}.; TRANSMEM 129 149 Helical; Name=4. {ECO:0000255}.; TRANSMEM 183 203 Helical; Name=5. {ECO:0000255}.; TRANSMEM 233 253 Helical; Name=6. {ECO:0000255}.; TRANSMEM 263 283 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 7 Extracellular. {ECO:0000255}.; TOPO_DOM 29 43 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 65 88 Extracellular. {ECO:0000255}.; TOPO_DOM 110 128 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 150 182 Extracellular. {ECO:0000255}.; TOPO_DOM 204 232 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 254 262 Extracellular. {ECO:0000255}.; TOPO_DOM 284 305 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor that may play a role in the perception of bitterness and is gustducin-linked. May play a role in sensing the chemical composition of the gastrointestinal content. The activity of this receptor may stimulate alpha gustducin, mediate PLC-beta-2 activation and lead to the gating of TRPM5 (By similarity). {ECO:0000250|UniProtKB:Q9NYV9}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q06666 T2_MOUSE Octapeptide-repeat protein T2 185 22,806 Chain (1); Region (1); Repeat (15) +Q5QD12 TAA7A_MOUSE Trace amine-associated receptor 7a (TaR-7a) (Trace amine receptor 7a) (mTaar7a) 358 40,368 Chain (1); Disulfide bond (1); Glycosylation (2); Topological domain (8); Transmembrane (7) TRANSMEM 48 68 Helical; Name=1. {ECO:0000255}.; TRANSMEM 84 104 Helical; Name=2. {ECO:0000255}.; TRANSMEM 122 143 Helical; Name=3. {ECO:0000255}.; TRANSMEM 167 187 Helical; Name=4. {ECO:0000255}.; TRANSMEM 213 233 Helical; Name=5. {ECO:0000255}.; TRANSMEM 275 295 Helical; Name=6. {ECO:0000255}.; TRANSMEM 310 333 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 47 Extracellular. {ECO:0000255}.; TOPO_DOM 69 83 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 105 121 Extracellular. {ECO:0000255}.; TOPO_DOM 144 166 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 188 212 Extracellular. {ECO:0000255}.; TOPO_DOM 234 274 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 296 309 Extracellular. {ECO:0000255}.; TOPO_DOM 334 358 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan olfactory receptor specific for trace amines. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Specifically expressed in neurons of the olfactory epithelium. {ECO:0000269|PubMed:16878137}. +Q5SWD9 TSR1_MOUSE Pre-rRNA-processing protein TSR1 homolog 803 92,105 Alternative sequence (3); Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (1); Frameshift (1); Sequence conflict (6) FUNCTION: Required during maturation of the 40S ribosomal subunit in the nucleolus. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. +Q8C8T8 TSR2_MOUSE Pre-rRNA-processing protein TSR2 homolog 191 20,891 Chain (1); Erroneous initiation (1) FUNCTION: May be involved in 20S pre-rRNA processing. {ECO:0000305}. +O54863 TSSK2_MOUSE Testis-specific serine/threonine-protein kinase 2 (TSK-2) (TSK2) (TSSK-2) (Testis-specific kinase 2) (EC 2.7.11.1) (Serine/threonine-protein kinase 22B) 358 41,022 Active site (1); Binding site (1); Chain (1); Domain (1); Nucleotide binding (1); Sequence conflict (6) FUNCTION: Testis-specific serine/threonine-protein kinase required during spermatid development. Phosphorylates 'Ser-281' of TSKS and SPAG16. Involved in the late stages of spermatogenesis, during the reconstruction of the cytoplasm. During spermatogenesis, required for the transformation of a ring-shaped structure around the base of the flagellum originating from the chromatoid body. {ECO:0000269|PubMed:18367677, ECO:0000269|PubMed:18533145, ECO:0000269|PubMed:20053632, ECO:0000269|PubMed:9412477}. PTM: Autophosphorylated. {ECO:0000250|UniProtKB:Q96PF2}.; PTM: Ubiquitinated; HSP90 activity negatively regulates ubiquitination and degradation. {ECO:0000269|PubMed:23599433}. SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Cytoplasmic vesicle, secretory vesicle, acrosome. Note=Present in the cytoplasm of elongating spermatids. In spermatozoa, localizes in the equatorial segment, neck, the midpiece and in a specific sperm head compartment. In spermatids, concentrates in centrioles during flagellogenesis. Localizes in the tail and acrosomal regions of epididymal sperm. SUBUNIT: Interacts with TSSK1B (PubMed:10781952, PubMed:18367677). Interacts with HSP90; this interaction stabilizes TSSK2 (PubMed:23599433). {ECO:0000269|PubMed:10781952, ECO:0000269|PubMed:18367677, ECO:0000269|PubMed:23599433}. TISSUE SPECIFICITY: Testis-specific. Expressed only in the spermatids postmeiotically at the final stages of cytodifferentiation in the seminiferous tubules (at protein level). Not detected in released sperms in the lumen of the seminiferous tubules. Also present in the epididymal sperm (at protein level). {ECO:0000269|PubMed:18533145, ECO:0000269|PubMed:20729278, ECO:0000269|PubMed:9412477, ECO:0000269|PubMed:9651519}. +Q9D411 TSSK4_MOUSE Testis-specific serine/threonine-protein kinase 4 (TSK-4) (TSSK-4) (Testis-specific kinase 4) (EC 2.7.11.1) 328 37,377 Active site (1); Alternative sequence (5); Binding site (1); Chain (1); Domain (1); Modified residue (1); Mutagenesis (2); Nucleotide binding (1); Sequence caution (1); Sequence conflict (3) FUNCTION: Isoform 1: Serine/threonine kinase which is involved in male germ cell development and in mature sperm function (PubMed:17927909, PubMed:23599433, PubMed:23054012, PubMed:25361759, PubMed:26940607). May be involved in the Cre/Creb signaling pathway (PubMed:26940607). Phosphorylates CREB1 on 'Ser-133' in vitro and can stimulate Cre/Creb pathway in cells (By similarity). Phosphorylates CREM on 'Ser-116' in vitro (PubMed:26940607). Phosphorylates ODF2 on 'Ser-95' (PubMed:26961893). {ECO:0000250|UniProtKB:Q6SA08, ECO:0000269|PubMed:17927909, ECO:0000269|PubMed:23054012, ECO:0000269|PubMed:23599433, ECO:0000269|PubMed:25361759, ECO:0000269|PubMed:26940607, ECO:0000269|PubMed:26961893}.; FUNCTION: Isoform 2: Catalytically inactive. {ECO:0000269|PubMed:17927909}.; FUNCTION: Isoform 3: Catalytically inactive. {ECO:0000269|PubMed:17927909}.; FUNCTION: Isoform 4: Catalytically inactive. {ECO:0000269|PubMed:17927909}. PTM: Activated by autophosphorylation on Thr-197. ODF2 potentiates the autophosphorylation activity of TSSK4 at Thr-197. {ECO:0000269|PubMed:23054012, ECO:0000269|PubMed:26940607}.; PTM: Ubiquitinated; HSP90 activity negatively regulates ubiquitination and degradation. {ECO:0000269|PubMed:23599433}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:20729278}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:20729278, ECO:0000269|PubMed:23054012, ECO:0000269|PubMed:25361759}. Note=In spermatozoa, present in the sperm head and in the flagellum. {ECO:0000269|PubMed:20729278}. SUBUNIT: Homodimer (PubMed:17927909, PubMed:23054012). Interacts with HSP90; this interaction stabilizes and activates TSSK4 (PubMed:23599433). Interacts with ODF2 (via C-terminus); this interaction promotes ODF2 phosphorylation on 'Ser-95' (PubMed:25361759, PubMed:26961893). May interact with CREM (PubMed:26940607). Interacts with CREB1; this interaction facilitates CREB1 phosphorylation on 'Ser-133' (By similarity). {ECO:0000250|UniProtKB:Q6SA08, ECO:0000269|PubMed:17927909, ECO:0000269|PubMed:23054012, ECO:0000269|PubMed:23599433, ECO:0000269|PubMed:25361759, ECO:0000269|PubMed:26940607, ECO:0000269|PubMed:26961893}. TISSUE SPECIFICITY: Isoform 1: Expressed in spermatocytes and mature sperm (at protein level) (PubMed:20729278, PubMed:23054012, PubMed:25361759, PubMed:26940607). Highly expressed in the spleen, heart and testis (PubMed:17927909, PubMed:20729278, PubMed:23054012). Isoform 2, isoform 3, and isoform 4: Expressed at highest level in testis and heart and at low levels in the liver, spleen, kidney, brain and thymus (PubMed:17927909). {ECO:0000269|PubMed:17927909, ECO:0000269|PubMed:20729278, ECO:0000269|PubMed:23054012, ECO:0000269|PubMed:25361759, ECO:0000269|PubMed:26940607}. +Q9QXE5 TSSP_MOUSE Thymus-specific serine protease (EC 3.4.-.-) (Serine protease 16) 509 54,523 Active site (3); Chain (1); Glycosylation (3); Signal peptide (1) FUNCTION: Protease that may play a role in T-cell development. SUBCELLULAR LOCATION: Cytoplasmic vesicle. Note=Vesicular, either lysosomal or endosomal. TISSUE SPECIFICITY: Expressed predominantly in cortical thymic epithelial cells, with highest expression around vessels and the thymic capsule. +Q3U269 TSTD2_MOUSE Thiosulfate sulfurtransferase/rhodanese-like domain-containing protein 2 495 55,386 Active site (1); Chain (1); Domain (1); Modified residue (1); Sequence conflict (3) +P70675 TSX_MOUSE Testis-specific protein TSX 144 15,978 Chain (1) FUNCTION: May have an RNA/DNA binding role. TISSUE SPECIFICITY: Testis. +Q8C0S4 TT21A_MOUSE Tetratricopeptide repeat protein 21A (TPR repeat protein 21A) (Tetratricopeptide repeat-containing hedgehog modulator 2) 1314 148,617 Alternative sequence (2); Chain (1); Repeat (19); Sequence conflict (5) +Q0HA38 TT21B_MOUSE Tetratricopeptide repeat protein 21B (TPR repeat protein 21B) (Intraflagellar transport 139 homolog) (Tetratricopeptide repeat-containing hedgehog modulator 1) 1315 150,795 Chain (1); Erroneous initiation (1); Repeat (19); Sequence caution (1) FUNCTION: Component of the IFT complex A (IFT-A), a complex required for retrograde ciliary transport. Negatively modulates the SHH signal transduction. {ECO:0000269|PubMed:18327258}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:18327258}. Note=In polarized epithelial inner medullary collecting ducts cells and in the nodes of mice at 8.0 dpc, colocalizes with alpha-tubulin in cilia. Expressed in a punctate manner throughout the axoneme from the cilia base to the tip. SUBUNIT: Component of the IFT complex A (IFT-A) (By similarity). Interacts with TTC25 (PubMed:25860617). {ECO:0000250, ECO:0000269|PubMed:25860617}. +A6H6E9 TT23L_MOUSE Tetratricopeptide repeat protein 23-like 458 51,532 Chain (1); Coiled coil (2); Erroneous initiation (2) SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q6PF05}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q6PF05}. Midbody {ECO:0000250|UniProtKB:Q6PF05}. Note=Exhibits dynamic subcellular localization during the cell cycle. In prophase cells, detected on split centrosomes. Translocates to the mitotic spindles during metaphase and early anaphase, then to the midbody and cleavage furrow in late anaphase. {ECO:0000250|UniProtKB:Q6PF05}. +A2ACP1 TT39A_MOUSE Tetratricopeptide repeat protein 39A (TPR repeat protein 39A) 578 66,126 Alternative sequence (1); Chain (1); Erroneous gene model prediction (4); Frameshift (1); Repeat (3); Sequence conflict (1) +Q8VE09 TT39C_MOUSE Tetratricopeptide repeat protein 39C (TPR repeat protein 39C) 580 65,445 Chain (1); Repeat (3); Sequence conflict (3) +Q3UVR3 TTBK2_MOUSE Tau-tubulin kinase 2 (EC 2.7.11.1) (Protein bartleby) 1243 136,770 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Compositional bias (2); Domain (1); Erroneous initiation (1); Modified residue (3); Mutagenesis (1); Nucleotide binding (1); Sequence conflict (8) FUNCTION: Serine/threonine kinase that acts as a key regulator of ciliogenesis: controls the initiation of ciliogenesis by binding to the distal end of the basal body and promoting the removal of CCP110, which caps the mother centriole, leading to the recruitment of IFT proteins, which build the ciliary axoneme. Has some substrate preference for proteins that are already phosphorylated on a Tyr residue at the +2 position relative to the phosphorylation site. Able to phosphorylate tau on serines in vitro. {ECO:0000269|PubMed:11257498, ECO:0000269|PubMed:23141541}. SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000269|PubMed:23141541}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:23141541}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:23141541}. Cytoplasm, cytosol {ECO:0000250}. Nucleus {ECO:0000250}. Note=Localizes to the transition zone in primary cilia in response to cell cycle signals that promote ciliogenesis. May also be present in cytosol and, at lower level in the nucleus. SUBUNIT: Interacts with CEP164. {ECO:0000250}. +Q8BW49 TTC12_MOUSE Tetratricopeptide repeat protein 12 (TPR repeat protein 12) 704 78,754 Chain (1); Modified residue (1); Repeat (3) +Q9CSP9 TTC14_MOUSE Tetratricopeptide repeat protein 14 (TPR repeat protein 14) 761 86,792 Alternative sequence (4); Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (1); Frameshift (2); Modified residue (1); Repeat (4); Sequence conflict (12) +Q8C1F5 TTC16_MOUSE Tetratricopeptide repeat protein 16 (TPR repeat protein 16) 767 86,945 Chain (1); Repeat (9) +E9PVB5 TTC17_MOUSE Tetratricopeptide repeat protein 17 (TPR repeat protein 17) 1198 135,521 Alternative sequence (1); Chain (1); Coiled coil (1); Repeat (6); Sequence conflict (2) FUNCTION: Plays a role in primary ciliogenesis by modulating actin polymerization. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Localized with CATIP at F-actin rich zones and at dynamic plasma membrane protrusions. {ECO:0000250}. SUBUNIT: Interacts with CATIP. {ECO:0000250}. +Q8CC21 TTC19_MOUSE Tetratricopeptide repeat protein 19, mitochondrial (TPR repeat protein 19) 365 41,234 Alternative sequence (1); Chain (1); Erroneous gene model prediction (1); Erroneous initiation (1); Frameshift (1); Repeat (4); Sequence conflict (2); Transit peptide (1) FUNCTION: Required for the preservation of the structural and functional integrity of mitochondrial respiratory complex III by allowing the physiological turnover of the Rieske protein UQCRFS1 (PubMed:21278747, PubMed:28673544). Involved in the clearance of UQCRFS1 N-terminal fragments, which are produced upon incorporation into the complex III and whose presence is detrimental for its catalytic activity (PubMed:28673544). {ECO:0000269|PubMed:21278747, ECO:0000269|PubMed:28673544}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:21278747}. SUBUNIT: Binds to the mature mitochondrial complex III dimer, after the incorporation of the Rieske protein UQCRFS1 (PubMed:28673544, PubMed:21278747). Interacts with UQCRC1 and UQCRFS1 (PubMed:21278747). Interacts with ZFYVE26 and CHMP4B (By similarity). {ECO:0000250|UniProtKB:Q6DKK2, ECO:0000269|PubMed:21278747, ECO:0000269|PubMed:28673544}. +Q91Z38 TTC1_MOUSE Tetratricopeptide repeat protein 1 (TPR repeat protein 1) 292 33,263 Chain (1); Modified residue (1); Repeat (3) SUBUNIT: Interacts with the GAP domain of NF1. Interacts (via TPR repeats) with HSP90AA1 and HSPA8. {ECO:0000250|UniProtKB:Q99614}. +Q8C159 TTC22_MOUSE Tetratricopeptide repeat protein 22 (TPR repeat protein 22) 568 63,101 Chain (1); Repeat (7) +Q8CHY7 TTC23_MOUSE Tetratricopeptide repeat protein 23 (TPR repeat protein 23) 488 54,608 Alternative sequence (2); Chain (1); Repeat (5) +Q8BYG0 TTC24_MOUSE Tetratricopeptide repeat protein 24 (TPR repeat protein 24) 334 36,701 Alternative sequence (1); Chain (1); Repeat (4) +Q9D4B2 TTC25_MOUSE Tetratricopeptide repeat protein 25 (TPR repeat protein 25) 624 71,530 Chain (1); Frameshift (1); Repeat (8); Sequence conflict (4) FUNCTION: Required for the docking of the outer dynein arm to cilia, hence plays an essential role in cilia motility. {ECO:0000269|PubMed:27486780}. SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000269|PubMed:25860617}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q96NG3}. SUBUNIT: Interacts with CCDC114 (By similarity). Interacts with components of the IFT complex A, including IFT140, TTC21B/IFT139 and WDR19/IFT144, and the IFT complex B, including IFT46, IFT52 and IFT57 (PubMed:25860617). {ECO:0000250|UniProtKB:Q96NG3, ECO:0000269|PubMed:25860617}. +Q8CD92 TTC27_MOUSE Tetratricopeptide repeat protein 27 (TPR repeat protein 27) 847 96,431 Alternative sequence (1); Chain (1); Erroneous initiation (1); Repeat (6); Sequence conflict (7) +Q80XJ3 TTC28_MOUSE Tetratricopeptide repeat protein 28 (TPR repeat protein 28) 2450 267,459 Chain (1); Erroneous initiation (2); Modified residue (7); Repeat (28); Sequence caution (1); Sequence conflict (1) FUNCTION: During mitosis, may be involved in the condensation of spindle midzone microtubules, leading to the formation of midbody. {ECO:0000250}.; FUNCTION: Essential for the formation and integrity of the midbody. Max play a critical role in the progress of mitosis and cytokinesis during cell cycle (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. Midbody {ECO:0000250}. Note=At interphase, localizes to centrosomes. At prometaphase and metaphase, associated with spindle microtubules and spindle poles. At anaphase, accumulates in the spindle midzone. At telophase, condensed on central spindles. During cytokinesis, condensed on the midbody where it colocalizes with AURKB (By similarity). {ECO:0000250}. SUBUNIT: Interacts with AURKB. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in embryos at all stages examined. In adult tissues, detected in heart and at low levels in kidney and testis. {ECO:0000269|PubMed:23036704}. +Q80VM3 TTC29_MOUSE Tetratricopeptide repeat protein 29 (TPR repeat protein 29) 471 54,282 Alternative sequence (1); Chain (1); Repeat (5) +Q9DAC7 TTC32_MOUSE Tetratricopeptide repeat protein 32 (TPR repeat protein 32) 148 16,796 Chain (1); Repeat (3) +Q9D6K7 TTC33_MOUSE Tetratricopeptide repeat protein 33 (TPR repeat protein 33) 262 29,371 Alternative sequence (2); Chain (1); Modified residue (1); Repeat (3) +Q8C0Q3 TTC34_MOUSE Tetratricopeptide repeat protein 34 (TPR repeat protein 34) 554 60,220 Chain (1); Repeat (8); Sequence conflict (8) +Q8VBW8 TTC36_MOUSE Tetratricopeptide repeat protein 36 (TPR repeat protein 36) 186 20,132 Chain (1); Repeat (3) +A3KMP2 TTC38_MOUSE Tetratricopeptide repeat protein 38 (TPR repeat protein 38) 465 52,224 Alternative sequence (1); Chain (1); Erroneous initiation (2); Repeat (3) +Q692V3 TTC41_MOUSE Tetratricopeptide repeat protein 41 (TPR repeat protein 41) (Grp94-neighboring nucleotidase) 1318 150,823 Alternative sequence (5); Chain (1); Repeat (6); Sequence conflict (4) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15827139}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm.; SUBCELLULAR LOCATION: Isoform 4: Cytoplasm. TISSUE SPECIFICITY: Highly expressed in lung and myeloid leukemia cell line (at protein level). Isoform 4: expressed in heart (at protein level). {ECO:0000269|PubMed:15827139}. +Q8BGB2 TTC7A_MOUSE Tetratricopeptide repeat protein 7A (TPR repeat protein 7A) 858 96,156 Chain (1); Modified residue (7); Repeat (8) FUNCTION: Component of a complex required to localize phosphatidylinositol 4-kinase (PI4K) to the plasma membrane. The complex acts as a regulator of phosphatidylinositol 4-phosphate (PtdIns(4)P) synthesis (By similarity). In the complex, plays a central role in bridging PI4KA to EFR3B and FAM126A, via direct interactions (By similarity). {ECO:0000250|UniProtKB:Q86TV6, ECO:0000250|UniProtKB:Q9ULT0}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9ULT0}. Cell membrane {ECO:0000250|UniProtKB:Q86TV6}. Note=Localizes to the cytosol and is recruited to the plasma membrane following interaction with EFR3 (EFR3A or EFR3B). {ECO:0000250|UniProtKB:Q86TV6}. SUBUNIT: Component of a phosphatidylinositol 4-kinase (PI4K) complex, composed of PI4KA, EFR3 (EFR3A or EFR3B), TTC7 (TTC7A or TTC7B) and FAM126 (FAM126A or FAM126B) (By similarity). Interacts with PI4KA, interaction is direct (By similarity). Interacts with EFR3 (EFR3A or EFR3B), interaction is direct (By similarity). Interacts with FAM126 (FAM126A or FAM126B), interaction is direct (By similarity). Association with the PI4K complex is strongly reduced by TMEM150A (By similarity). {ECO:0000250|UniProtKB:Q86TV6, ECO:0000250|UniProtKB:Q9ULT0}. +Q3V038 TTC9A_MOUSE Tetratricopeptide repeat protein 9A (TPR repeat protein 9A) 219 24,351 Chain (1); Erroneous initiation (2); Modified residue (1); Repeat (3) +Q810A3 TTC9C_MOUSE Tetratricopeptide repeat protein 9C (TPR repeat protein 9C) 171 19,998 Chain (1); Repeat (3); Sequence conflict (1) +A4Q9F3 TTL10_MOUSE Protein polyglycylase TTLL10 (EC 6.3.2.-) (Tubulin--tyrosine ligase-like protein 10) 704 79,250 Alternative sequence (1); Binding site (2); Chain (1); Compositional bias (2); Domain (1); Mutagenesis (1); Nucleotide binding (1); Sequence conflict (4) FUNCTION: Polyglycylase which modifies both tubulin and non-tubulin proteins, generating side chains of glycine on the gamma-carboxyl groups of specific glutamate residues of target proteins. Polyglycylates alpha-tubulin and beta-tubulin, but is not able to initiate glycylation and only has activity toward monoglycylated tubulin. Has the ability to polyglycylate non-tubulin proteins such as NAP1; in this case it can initiate glycylation and does not require preliminary monoglycylation by another glycylase. {ECO:0000269|PubMed:18331838, ECO:0000269|PubMed:19427864, ECO:0000269|PubMed:19524510}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. Cell projection, cilium {ECO:0000305}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000305}. +A4Q9F4 TTL11_MOUSE Tubulin polyglutamylase TTLL11 (EC 6.-.-.-) (Tubulin--tyrosine ligase-like protein 11) 727 82,361 Alternative sequence (2); Binding site (2); Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (1); Erroneous termination (1); Frameshift (1); Nucleotide binding (1); Region (1); Sequence conflict (3) FUNCTION: Polyglutamase which preferentially modifies alpha-tubulin (PubMed:17499049). Involved in the side-chain elongation step of the polyglutamylation reaction rather than in the initiation step. Required for CCSAP localization to both spindle and cilia microtubules (PubMed:17499049). Generates long side-chains (PubMed:20530212). {ECO:0000269|PubMed:17499049, ECO:0000269|PubMed:20530212}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:17499049}. DOMAIN: The flexible c-MTBD (cationic microtubule binding domain) region mediates binding to microtubules. It is positively charged and becomes ordered when bound to microtubules: it interacts with a negatively charged patch on tubulin. The presence of positive charges in the c-MTBD region is essential for proper binding. {ECO:0000250|UniProtKB:Q6ZT98, ECO:0000250|UniProtKB:Q8NHH1}. TISSUE SPECIFICITY: Widely expressed with highest levels in brain, kidney, liver, lung, muscle and testis. {ECO:0000269|PubMed:17499049}. +A4Q9E8 TTLL6_MOUSE Tubulin polyglutamylase TTLL6 (EC 6.-.-.-) (Tubulin--tyrosine ligase-like protein 6) 822 94,507 Alternative sequence (1); Binding site (2); Chain (1); Domain (1); Erroneous gene model prediction (1); Frameshift (1); Nucleotide binding (1); Region (1); Sequence conflict (1) FUNCTION: Polyglutamylase which preferentially modifies alpha-tubulin (PubMed:17499049, PubMed:21074048). Mediates tubulin polyglutamylation in cilia (PubMed:22246503). Involved in the side-chain elongation step of the polyglutamylation reaction rather than in the initiation step (PubMed:17499049, PubMed:21074048). Generates long side-chains (PubMed:20530212). Generates polyglutamylation of CGAS, leading to impair the DNA-binding activity of CGAS (PubMed:26829768). {ECO:0000269|PubMed:17499049, ECO:0000269|PubMed:20530212, ECO:0000269|PubMed:21074048, ECO:0000269|PubMed:22246503}. SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000269|PubMed:17499049}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:17499049}. Note=CEP41 is required for its transport between the basal body and the cilium. {ECO:0000250|UniProtKB:Q8N841}. SUBUNIT: Found in a complex with CEP41. {ECO:0000250|UniProtKB:Q8N841}. DOMAIN: The flexible c-MTBD (cationic microtubule binding domain) region mediates binding to microtubules. It is positively charged and becomes ordered when bound to microtubules: it interacts with a negatively charged patch on tubulin. The presence of positive charges in the c-MTBD region is essential for proper binding. {ECO:0000250|UniProtKB:Q6ZT98, ECO:0000250|UniProtKB:Q8N841}. TISSUE SPECIFICITY: Widely expressed with highest levels in testis. {ECO:0000269|PubMed:17499049}. +Q78S06 SYS1_MOUSE Protein SYS1 homolog 156 17,554 Chain (1); Sequence conflict (1); Transmembrane (4) TRANSMEM 13 33 Helical. {ECO:0000255}.; TRANSMEM 65 85 Helical. {ECO:0000255}.; TRANSMEM 91 111 Helical. {ECO:0000255}.; TRANSMEM 113 133 Helical. {ECO:0000255}. FUNCTION: Involved in protein trafficking. May serve as a receptor for ARFRP1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with ARFRP1. {ECO:0000250}. +P38585 TTL_MOUSE Tubulin--tyrosine ligase (TTL) (EC 6.3.2.25) 377 43,136 Chain (1); Domain (1); Sequence conflict (4) FUNCTION: Catalyzes the post-translational addition of a tyrosine to the C-terminal end of detyrosinated alpha-tubulin. {ECO:0000269|PubMed:27102488}. SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P38584}. +Q9JJL8 SYSM_MOUSE Serine--tRNA ligase, mitochondrial (EC 6.1.1.11) (SerRSmt) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase) 518 58,316 Binding site (3); Chain (1); Modified residue (3); Nucleotide binding (2); Region (1); Sequence conflict (1); Transit peptide (1) Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1. FUNCTION: Catalyzes the attachment of serine to tRNA(Ser). Is also probably able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec). {ECO:0000250|UniProtKB:Q9N0F3}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000305|PubMed:15081407}. SUBUNIT: Homodimer. The tRNA molecule probably binds across the dimer. {ECO:0000250|UniProtKB:Q9N0F3}. DOMAIN: Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding. {ECO:0000250|UniProtKB:Q9N0F3}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15081407}. +P22893 TTP_MOUSE mRNA decay activator protein ZFP36 (Growth factor-inducible nuclear protein NUP475) (TPA-induced sequence 11) (Tristetraprolin) (Zinc finger protein 36) (Zfp-36) 319 33,613 Beta strand (1); Chain (1); Helix (2); Modified residue (14); Mutagenesis (6); Region (9); Repeat (3); Turn (1); Zinc finger (2) FUNCTION: Zinc-finger RNA-binding protein that destabilizes numerous cytoplasmic AU-rich element (ARE)-containing mRNA transcripts by promoting their poly(A) tail removal or deadenylation, and hence provide a mechanism for attenuating protein synthesis (PubMed:10330172, PubMed:10706852, PubMed:10805719, PubMed:15014438, PubMed:15187092, PubMed:15634918, PubMed:17030620, PubMed:19188452, PubMed:20595389, PubMed:21078877, PubMed:22701344, PubMed:27193233). Acts as an 3'-untranslated region (UTR) ARE mRNA-binding adapter protein to communicate signaling events to the mRNA decay machinery (PubMed:21278420). Recruits deadenylase CNOT7 (and probably the CCR4-NOT complex) via association with CNOT1, and hence promotes ARE-mediated mRNA deadenylation (PubMed:21278420). Functions also by recruiting components of the cytoplasmic RNA decay machinery to the bound ARE-containing mRNAs (PubMed:21278420). Self regulates by destabilizing its own mRNA (PubMed:15187092, PubMed:17288565). Binds to 3'-UTR ARE of numerous mRNAs and of its own mRNA (PubMed:11533235, PubMed:15187092, PubMed:16508014, PubMed:17288565, PubMed:17971298, PubMed:20595389, PubMed:21078877, PubMed:21278420, PubMed:22701344, PubMed:27193233). Plays a role in anti-inflammatory responses; suppresses tumor necrosis factor (TNF)-alpha production by stimulating ARE-mediated TNF-alpha mRNA decay and several other inflammatory ARE-containing mRNAs in interferon (IFN)- and/or lipopolysaccharide (LPS)-induced macrophages (PubMed:8630730, PubMed:9703499, PubMed:15014438, PubMed:16514065). Plays also a role in the regulation of dendritic cell maturation at the post-transcriptional level, and hence operates as part of a negative feedback loop to limit the inflammatory response (By similarity). Promotes ARE-mediated mRNA decay of hypoxia-inducible factor HIF1A mRNA during the response of endothelial cells to hypoxia (By similarity). Positively regulates early adipogenesis of preadipocytes by promoting ARE-mediated mRNA decay of immediate early genes (IEGs) (PubMed:22701344). Negatively regulates hematopoietic/erythroid cell differentiation by promoting ARE-mediated mRNA decay of the transcription factor STAT5B mRNA (By similarity). Plays a role in maintaining skeletal muscle satellite cell quiescence by promoting ARE-mediated mRNA decay of the myogenic determination factor MYOD1 mRNA (PubMed:25815583). Associates also with and regulates the expression of non-ARE-containing target mRNAs at the post-transcriptional level, such as MHC class I mRNAs (By similarity). Participates in association with argonaute RISC catalytic components in the ARE-mediated mRNA decay mechanism; assists microRNA (miRNA) targeting ARE-containing mRNAs (By similarity). May also play a role in the regulation of cytoplasmic mRNA decapping; enhances decapping of ARE-containing RNAs, in vitro (By similarity). Involved in the delivery of target ARE-mRNAs to processing bodies (PBs) (By similarity). In addition to its cytosolic mRNA-decay function, affects nuclear pre-mRNA processing (PubMed:22844456). Negatively regulates nuclear poly(A)-binding protein PABPN1-stimulated polyadenylation activity on ARE-containing pre-mRNA during LPS-stimulated macrophages (PubMed:22844456). Also involved in the regulation of stress granule (SG) and P-body (PB) formation and fusion (PubMed:15967811). Plays a role in the regulation of keratinocyte proliferation, differentiation and apoptosis (By similarity). Plays a role as a tumor suppressor by inhibiting cell proliferation in breast cancer cells (By similarity). {ECO:0000250|UniProtKB:P26651, ECO:0000269|PubMed:10330172, ECO:0000269|PubMed:10706852, ECO:0000269|PubMed:10805719, ECO:0000269|PubMed:11533235, ECO:0000269|PubMed:15014438, ECO:0000269|PubMed:15187092, ECO:0000269|PubMed:15634918, ECO:0000269|PubMed:15967811, ECO:0000269|PubMed:16508014, ECO:0000269|PubMed:16514065, ECO:0000269|PubMed:17030620, ECO:0000269|PubMed:17288565, ECO:0000269|PubMed:17971298, ECO:0000269|PubMed:19188452, ECO:0000269|PubMed:20595389, ECO:0000269|PubMed:21078877, ECO:0000269|PubMed:21278420, ECO:0000269|PubMed:22701344, ECO:0000269|PubMed:22844456, ECO:0000269|PubMed:25815583, ECO:0000269|PubMed:27193233, ECO:0000269|PubMed:8630730, ECO:0000269|PubMed:9703499}. PTM: Phosphorylated (PubMed:11533235). Phosphorylation at serine and/or threonine residues occurs in a p38 MAPK- and MAPKAPK2-dependent manner (PubMed:11533235). Phosphorylated by MAPKAPK2 at Ser-52 and Ser-178; phosphorylation increases its stability and cytoplasmic localization, promotes binding to 14-3-3 adapter proteins and inhibits the recruitment of cytoplasmic CCR4-NOT and PAN2-PAN3 deadenylase complexes to the mRNA decay machinery, thereby inhibiting ZFP36-induced ARE-containing mRNA deadenylation and decay processes (PubMed:15014438, PubMed:14688255, PubMed:16508014, PubMed:16508015, PubMed:17170118, PubMed:20595389, PubMed:21078877). Phosphorylation by MAPKAPK2 does not impair ARE-containing RNA-binding (PubMed:20595389, PubMed:21078877). Phosphorylated in a MAPKAPK2- and p38 MAPK-dependent manner upon skeletal muscle satellite cell activation; this phosphorylation inhibits ZFP36-mediated mRNA decay activity, and hence stabilizes MYOD1 mRNA (PubMed:25815583). Phosphorylated by MAPK1 upon mitogen stimulation (PubMed:7768935, PubMed:14688255). Phosphorylated at Ser-58 and Ser-85; these phosphorylations increase in a SH3KBP1-dependent manner (By similarity). Phosphorylated at serine and threonine residues in a pyruvate kinase PKM- and p38 MAPK-dependent manner (By similarity). Phosphorylation at Ser-52 may participate in the PKM-mediated degradation of ZFP36 in a p38 MAPK-dependent manner (By similarity). Dephosphorylated by serine/threonine phosphatase 2A at Ser-178 (PubMed:11533235, PubMed:17170118). {ECO:0000250|UniProtKB:P26651, ECO:0000269|PubMed:11533235, ECO:0000269|PubMed:14688255, ECO:0000269|PubMed:15014438, ECO:0000269|PubMed:16508014, ECO:0000269|PubMed:16508015, ECO:0000269|PubMed:17170118, ECO:0000269|PubMed:20595389, ECO:0000269|PubMed:21078877, ECO:0000269|PubMed:25815583, ECO:0000269|PubMed:7768935}.; PTM: Ubiquitinated; pyruvate kinase (PKM)-dependent ubiquitination leads to proteasomal degradation through a p38 MAPK signaling pathway. {ECO:0000250|UniProtKB:P26651}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11796723, ECO:0000269|PubMed:11886850, ECO:0000269|PubMed:15014438, ECO:0000269|PubMed:16508015, ECO:0000269|PubMed:22844456}. Cytoplasm {ECO:0000269|PubMed:11796723, ECO:0000269|PubMed:11886850, ECO:0000269|PubMed:15014438, ECO:0000269|PubMed:16508015, ECO:0000269|PubMed:17288565, ECO:0000269|PubMed:22844456, ECO:0000269|PubMed:24733888, ECO:0000269|PubMed:9703499}. Cytoplasmic granule {ECO:0000269|PubMed:15014438, ECO:0000269|PubMed:15967811}. Cytoplasm, P-body {ECO:0000269|PubMed:15967811}. Note=Shuttles between nucleus and cytoplasm in a CRM1-dependent manner (PubMed:11796723, PubMed:11886850). Localized predominantly in the cytoplasm in a p38 MAPK- and YWHAB-dependent manner (PubMed:11886850, PubMed:16508015). Colocalizes with SH3KBP1 and MAP3K4 in the cytoplasm (By similarity). Component of cytoplasmic stress granules (SGs) (PubMed:15967811). Localizes to cytoplasmic stress granules upon energy starvation (PubMed:15014438). Localizes in processing bodies (PBs) (By similarity). Excluded from stress granules in a phosphorylation MAPKAPK2-dependent manner (PubMed:15014438). Shuttles in and out of both cytoplasmic P-body and SGs (PubMed:15967811). {ECO:0000250|UniProtKB:P26651, ECO:0000269|PubMed:11796723, ECO:0000269|PubMed:11886850, ECO:0000269|PubMed:15014438, ECO:0000269|PubMed:15967811, ECO:0000269|PubMed:16508015}. SUBUNIT: Associates with cytoplasmic CCR4-NOT and PAN2-PAN3 deadenylase complexes to trigger ARE-containing mRNA deadenylation and decay processes (PubMed:20595389, PubMed:21078877). Part of a mRNA decay activation complex at least composed of poly(A)-specific exoribonucleases CNOT6, EXOSC2 and XRN1 and mRNA-decapping enzymes DCP1A and DCP2 (By similarity). Associates with the RNA exosome complex (By similarity). Interacts (via phosphorylated form) with 14-3-3 proteins; these interactions promote exclusion of ZFP36 from cytoplasmic stress granules in response to arsenite treatment in a MAPKAPK2-dependent manner and does not prevent CCR4-NOT deadenylase complex recruitment or ZFP36-induced ARE-containing mRNA deadenylation and decay processes (PubMed:15014438, PubMed:20595389). Interacts with 14-3-3 proteins; these interactions occur in response to rapamycin in an Akt-dependent manner (By similarity). Interacts with AGO2 and AGO4 (By similarity). Interacts (via C-terminus) with CNOT1; this interaction occurs in a RNA-independent manner and induces mRNA deadenylation (PubMed:21278420). Interacts (via N-terminus) with CNOT6 (By similarity). Interacts with CNOT6L (PubMed:21078877). Interacts (via C-terminus) with CNOT7; this interaction occurs in a RNA-independent manner, induces mRNA deadenylation and is inhibited in a phosphorylation MAPKAPK2-dependent manner (PubMed:20595389, PubMed:21278420). Interacts (via unphosphorylated form) with CNOT8; this interaction occurs in a RNA-independent manner and is inhibited in a phosphorylation MAPKAPK2-dependent manner (PubMed:20595389). Interacts with DCP1A (By similarity). Interacts (via N-terminus) with DCP2 (By similarity). Interacts with EDC3 (By similarity). Interacts (via N-terminus) with EXOSC2 (By similarity). Interacts with heat shock 70 kDa proteins (By similarity). Interacts with KHSRP; this interaction increases upon cytokine-induced treatment (By similarity). Interacts with MAP3K4; this interaction enhances the association with SH3KBP1/CIN85 (By similarity). Interacts with MAPKAPK2; this interaction occurs upon skeletal muscle satellite cell activation (PubMed:25815583). Interacts with NCL (By similarity). Interacts with NUP214; this interaction increases upon lipopolysaccharide (LPS) stimulation (By similarity). Interacts with PABPC1; this interaction occurs in a RNA-dependent manner (PubMed:20595389, PubMed:21078877). Interacts (via hypophosphorylated form) with PABPN1 (via RRM domain and C-terminal arginine-rich region); this interaction occurs in the nucleus in a RNA-independent manner, decreases in presence of single-stranded poly(A) RNA-oligomer and in a p38 MAPK-dependent-manner and inhibits nuclear poly(A) tail synthesis (PubMed:22844456). Interacts with PAN2 (PubMed:21078877). Interacts (via C3H1-type zinc finger domains) with PKM (By similarity). Interacts (via C3H1-type zinc finger domains) with nuclear RNA poly(A) polymerase (PubMed:22844456). Interacts with PPP2CA; this interaction occurs in LPS-stimulated cells and induces ZFP36 dephosphorylation, and hence may promote ARE-containing mRNAs decay (PubMed:17170118). Interacts (via C-terminus) with PRR5L (via C-terminus); this interaction may accelerate ZFP36-mediated mRNA decay during stress (By similarity). Interacts (via C-terminus) with SFN; this interaction occurs in a phosphorylation-dependent manner (PubMed:11886850). Interacts (via extreme C-terminal region) with SH3KBP1/CIN85 (via SH3 domains); this interaction enhances MAP3K4-induced phosphorylation of ZFP36 at Ser-58 and Ser-85 and does not alter neither ZFP36 binding to ARE-containing transcripts nor TNF-alpha mRNA decay (By similarity). Interacts with XRN1 (By similarity). Interacts (via C-terminus and Ser-178 phosphorylated form) with YWHAB; this interaction occurs in a p38/MAPKAPK2-dependent manner, increases cytoplasmic localization of ZFP36 and protects ZFP36 from Ser-178 dephosphorylation by serine/threonine phosphatase 2A, and hence may be crucial for stabilizing ARE-containing mRNAs (PubMed:14688255, PubMed:17170118). Interacts (via phosphorylated form) with YWHAE (PubMed:21078877). Interacts (via C-terminus) with YWHAG; this interaction occurs in a phosphorylation-dependent manner (PubMed:11886850). Interacts with YWHAH; this interaction occurs in a phosphorylation-dependent manner (PubMed:11886850). Interacts with YWHAQ; this interaction occurs in a phosphorylation-dependent manner (PubMed:11886850). Interacts with (via C-terminus) YWHAZ; this interaction occurs in a phosphorylation-dependent manner (PubMed:11886850). Does not interact with SH3KBP1 (PubMed:20221403). Interacts (via the 4EHP-binding motif) with EIF4E2; the interaction is direct (By similarity). Interacts (via P-P-P-P-G repeats) with GIGYF2; the interaction is direct (PubMed:26763119). {ECO:0000250|UniProtKB:P26651, ECO:0000269|PubMed:11886850, ECO:0000269|PubMed:14688255, ECO:0000269|PubMed:15014438, ECO:0000269|PubMed:17170118, ECO:0000269|PubMed:20221403, ECO:0000269|PubMed:20595389, ECO:0000269|PubMed:21078877, ECO:0000269|PubMed:21278420, ECO:0000269|PubMed:22844456, ECO:0000269|PubMed:25815583, ECO:0000269|PubMed:26763119}. DOMAIN: The C3H1-type zinc finger domains are necessary for ARE-binding activity. {ECO:0000250|UniProtKB:P26651}. TISSUE SPECIFICITY: Expressed in skeletal muscle satellite cells (PubMed:25815583). Strongly expressed in differentiated adipocytes compared to preadipocytes (at protein level) (PubMed:22701344). Expressed in embryonic stem cells (ESCs) (PubMed:24733888). Expressed in heart, placenta, kidney, intestine, liver, lung, thymus, fat and spleen (PubMed:2204625, PubMed:1699942). {ECO:0000269|PubMed:1699942, ECO:0000269|PubMed:2204625, ECO:0000269|PubMed:22701344, ECO:0000269|PubMed:24733888, ECO:0000269|PubMed:25815583}. +Q9D3A9 TTYH1_MOUSE Protein tweety homolog 1 (mTTY1) 450 49,032 Alternative sequence (3); Chain (1); Compositional bias (1); Glycosylation (3); Modified residue (1); Sequence caution (1); Sequence conflict (9); Topological domain (6); Transmembrane (5) TRANSMEM 44 64 Helical; Name=1. {ECO:0000255}.; TRANSMEM 89 109 Helical; Name=2. {ECO:0000255}.; TRANSMEM 215 235 Helical; Name=3. {ECO:0000255}.; TRANSMEM 241 261 Helical; Name=4. {ECO:0000255}.; TRANSMEM 391 411 Helical; Name=5. {ECO:0000255}. TOPO_DOM 1 43 Extracellular. {ECO:0000255}.; TOPO_DOM 65 88 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 110 214 Extracellular. {ECO:0000255}.; TOPO_DOM 236 240 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 262 390 Extracellular. {ECO:0000255}.; TOPO_DOM 412 450 Cytoplasmic. {ECO:0000255}. FUNCTION: Probable chloride channel. May be involved in cell adhesion (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Restricted mainly to neural tissues. Strongly expressed in brain and eye. {ECO:0000269|PubMed:17116230}. +Q3TH73 TTYH2_MOUSE Protein tweety homolog 2 (mTTY2) 532 59,008 Alternative sequence (1); Chain (1); Compositional bias (1); Glycosylation (1); Modified residue (2); Sequence conflict (7); Topological domain (6); Transmembrane (5) TRANSMEM 45 65 Helical; Name=1. {ECO:0000255}.; TRANSMEM 88 108 Helical; Name=2. {ECO:0000255}.; TRANSMEM 214 234 Helical; Name=3. {ECO:0000255}.; TRANSMEM 241 261 Helical; Name=4. {ECO:0000255}.; TRANSMEM 386 406 Helical; Name=5. {ECO:0000255}. TOPO_DOM 1 44 Extracellular. {ECO:0000255}.; TOPO_DOM 66 87 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 109 213 Extracellular. {ECO:0000255}.; TOPO_DOM 235 240 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 262 385 Extracellular. {ECO:0000255}.; TOPO_DOM 407 532 Cytoplasmic. {ECO:0000255}. FUNCTION: Probable large-conductance Ca(2+)-activated chloride channel. May play a role in Ca(2+) signal transduction. May be involved in cell proliferation and cell aggregation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q673H1 TUSC1_MOUSE Tumor suppressor candidate gene 1 protein homolog 205 22,712 Chain (1); Coiled coil (1); Compositional bias (1); Modified residue (1) +Q8BTV1 TUSC3_MOUSE Tumor suppressor candidate 3 (Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit TUSC3) (Oligosaccharyl transferase subunit TUSC3) (Magnesium uptake/transporter TUSC3) (Protein N33) 347 39,548 Chain (1); Disulfide bond (1); Domain (1); Glycosylation (1); Signal peptide (1); Topological domain (5); Transmembrane (4) TRANSMEM 197 217 Helical. {ECO:0000255}.; TRANSMEM 222 242 Helical. {ECO:0000255}.; TRANSMEM 277 297 Helical. {ECO:0000255}.; TRANSMEM 313 333 Helical. {ECO:0000255}. TOPO_DOM 42 196 Lumenal. {ECO:0000255}.; TOPO_DOM 218 221 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 243 276 Lumenal. {ECO:0000255}.; TOPO_DOM 298 312 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 334 347 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Acts as accessory component of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. Involved in N-glycosylation of STT3B-dependent substrates. Specifically required for the glycosylation of a subset of acceptor sites that are near cysteine residues; in this function seems to act redundantly with MAGT1. In its oxidized form proposed to form transient mixed disulfides with a glycoprotein substrate to facilitate access of STT3B to the unmodified acceptor site. Has also oxidoreductase-independent functions in the STT3B-containing OST complex possibly involving substrate recognition. {ECO:0000250|UniProtKB:Q13454}.; FUNCTION: Magnesium transporter. {ECO:0000250|UniProtKB:Q13454}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Accessory component of the STT3B-containing form of the oligosaccharyltransferase (OST) complex. OST exists in two different complex forms which contain common core subunits RPN1, RPN2, OST48, OST4, DAD1 and TMEM258, either STT3A or STT3B as catalytic subunits, and form-specific accessory subunits. OST can form stable complexes with the Sec61 complex or with both the Sec61 and TRAP complexes. The association of TUSC3 or MAGT1 with the STT3B-containing complex seems to be mutually exclusvice. {ECO:0000250|UniProtKB:Q13454}. +Q9EP52 TWSG1_MOUSE Twisted gastrulation protein homolog 1 222 24,801 Chain (1); Compositional bias (1); Glycosylation (2); Sequence conflict (5); Signal peptide (1) FUNCTION: May be involved in dorsoventral axis formation. Seems to antagonize BMP signaling by forming ternary complexes with CHRD and BMPs, thereby preventing BMPs from binding to their receptors. In addition to the anti-BMP function, also has pro-BMP activity, partly mediated by cleavage and degradation of CHRD, which releases BMPs from ternary complexes. May be an important modulator of BMP-regulated cartilage development and chondrocyte differentiation. May play a role in thymocyte development. {ECO:0000269|PubMed:11260715, ECO:0000269|PubMed:12119341, ECO:0000269|PubMed:15843411, ECO:0000269|PubMed:16905550}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Interacts with CHRD and/or BMP4. This interaction enhances CHRD/BMP4 complex formation. Interacts with BMP7. {ECO:0000269|PubMed:11260715, ECO:0000269|PubMed:11420619, ECO:0000269|PubMed:15843411}. DOMAIN: The N-terminal domain is sufficient to interact with BMP4. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in lymph node, liver, kidney, and lung. Expression in the kidney was stronger in the medulla than in the cortex, particularly in the cells surrounding the medullary tubules. Expressed in growth plate cartilage of long bones, ribs, and digits and to a lesser extent also in the resting zone of the epiphysis, trabecular bone, and vertebral cartilage. Expression seems to be absent from other skeletal tissues including muscle, skin, and fibroblasts. {ECO:0000269|PubMed:16905550}. +Q9JMI7 TX101_MOUSE Testis-expressed protein 101 (TES101-reactive protein) (TES101RP) 250 26,998 Chain (1); Domain (1); Glycosylation (4); Lipidation (1); Propeptide (1); Signal peptide (1) FUNCTION: Plays a role in fertilization by controlling binding of sperm to zona pellucida and migration of spermatozoa into the oviduct probably through molecule adhesion ADAM3 (PubMed:23633567, PubMed:23969891). May play a role in signal transduction and promote protein tyrosine phosphorylation (By similarity). {ECO:0000250|UniProtKB:Q924B5, ECO:0000269|PubMed:23633567, ECO:0000269|PubMed:23969891}. PTM: N-glycosylated; by high mannose and/or biantennary complex and/or certain types of hybrid oligosaccharides; possesses different oligosaccharides chains according to its subcellular localization in the testis. {ECO:0000269|PubMed:16822331, ECO:0000269|PubMed:18620756}.; PTM: Sheds from membrane raft by ACE and released from the cell surface of epididymal sperm while it passes through the caput epididymis leading to disappearance of TEX101 on spermatozoa; is essential to produce fertile spermatozoa. {ECO:0000269|PubMed:16388701, ECO:0000269|PubMed:23633567, ECO:0000269|PubMed:24501175}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11207211, ECO:0000269|PubMed:16388701, ECO:0000269|PubMed:16678124, ECO:0000269|PubMed:18503752, ECO:0000269|PubMed:18620756, ECO:0000269|PubMed:21724266, ECO:0000269|PubMed:27005865}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:16822331}. Membrane raft {ECO:0000269|PubMed:15917346, ECO:0000269|PubMed:18503752}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:27005865}. Secreted {ECO:0000269|PubMed:18503752, ECO:0000269|PubMed:18620756, ECO:0000269|PubMed:21724266}. Cytoplasmic vesicle {ECO:0000269|PubMed:21724266, ECO:0000269|PubMed:27005865}. Note=Located on plasma membrane of spermatocytes, round and elongated spermatids, and testicular spermatozoa. {ECO:0000269|PubMed:18620756}. SUBUNIT: Interacts with VAMP3 (PubMed:16678124). Interacts with LY6K (PubMed:18503752). Interacts with DPEP3; co-localized on the cell surface of spermatocytes, spermatids, and testicular spermatozoa, co-localized only in cytoplasmic droplets of caput and corpus epididymal sperm (PubMed:21724266). Interacts with ADAM3; co-localized on sperm surface (PubMed:23633567, PubMed:23969891). Interacts with ADAM5 (PubMed:23969891). {ECO:0000269|PubMed:16678124, ECO:0000269|PubMed:18503752, ECO:0000269|PubMed:21724266, ECO:0000269|PubMed:23633567, ECO:0000269|PubMed:23969891}. TISSUE SPECIFICITY: Detected in testis and ovary (PubMed:11207211, PubMed:15689535, PubMed:15917346, PubMed:16388701, PubMed:23969891). Expressed in spermatocytes, spermatids and testicular spermatozoa, but not in spermatogonia or interstitial cells (PubMed:18620756). Expressed abundantly in testicular germ cells (TGCs) but mostly disappeared from epididymal spermatozoa (PubMed:23633567). {ECO:0000269|PubMed:11207211, ECO:0000269|PubMed:15689535, ECO:0000269|PubMed:15917346, ECO:0000269|PubMed:16388701, ECO:0000269|PubMed:18620756, ECO:0000269|PubMed:23633567, ECO:0000269|PubMed:23969891}. +Q8C6N3 SYT15_MOUSE Synaptotagmin-15 (Synaptotagmin XV) (SytXV) 418 47,270 Alternative sequence (2); Chain (1); Domain (2); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 5 27 Helical; Signal-anchor for type III membrane protein. {ECO:0000255}. TOPO_DOM 1 4 Extracellular. {ECO:0000255}.; TOPO_DOM 28 418 Cytoplasmic. {ECO:0000255}. FUNCTION: May be involved in the trafficking and exocytosis of secretory vesicles in non-neuronal tissues. SUBCELLULAR LOCATION: Membrane; Single-pass type III membrane protein. SUBUNIT: Homodimer. {ECO:0000250}. DOMAIN: Neither C2 domains mediates Ca(2+)-dependent or Ca(2+)-independent phospholipid binding. TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in heart, lung, skeletal muscle and testis; not detected in brain, liver and kidney. Isoform 1 is expressed in spleen. {ECO:0000269|PubMed:12788067}. +Q7TN83 SYT16_MOUSE Synaptotagmin-16 (Synaptotagmin 14-like protein) (Synaptotagmin XIV-related protein) 639 71,255 Alternative sequence (5); Chain (1); Domain (2); Frameshift (1); Sequence conflict (1) FUNCTION: May be involved in the trafficking and exocytosis of secretory vesicles in non-neuronal tissues. Is Ca(2+)-independent. {ECO:0000269|PubMed:12801916}. SUBUNIT: Homodimer. Can also form heterodimers. {ECO:0000269|PubMed:12801916}. TISSUE SPECIFICITY: Highly expressed in heart and testis. Moderately expressed in kidney. {ECO:0000269|PubMed:12801916}. +Q9D0R2 SYTC_MOUSE Threonine--tRNA ligase, cytoplasmic (EC 6.1.1.3) (Threonyl-tRNA synthetase) (ThrRS) 722 83,356 Chain (1); Modified residue (4); Mutagenesis (2); Sequence conflict (6) FUNCTION: Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged tRNA(Thr) via its editing domain, at the post-transfer stage. {ECO:0000269|PubMed:29579307}. PTM: ISGylated. {ECO:0000269|PubMed:16139798}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29579307}. SUBUNIT: Homodimer. {ECO:0000250}. +Q99N80 SYTL1_MOUSE Synaptotagmin-like protein 1 (Exophilin-7) 567 62,362 Chain (1); Compositional bias (1); Domain (3); Modified residue (2); Sequence conflict (1) FUNCTION: Binds phosphatidylinositol 3,4,5-trisphosphate (By similarity). May play a role in vesicle trafficking. Acts as a RAB27A effector protein and may play a role in cytotoxic granule exocytosis in lymphocytes. {ECO:0000250, ECO:0000269|PubMed:18266782}. SUBCELLULAR LOCATION: Endomembrane system {ECO:0000269|PubMed:18266782}; Peripheral membrane protein {ECO:0000269|PubMed:18266782}. Cell membrane {ECO:0000269|PubMed:18266782}. SUBUNIT: Monomer. Binds NCF2 and NRXN1 (By similarity). Binds RAB27A that has been activated by GTP-binding via its N-terminus. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in lung. Detected at lower levels in spleen, liver and kidney, and at very low levels in heart, brain and skeletal muscle. Expressed in cytotoxic T-lymphocytes (CTL). {ECO:0000269|PubMed:18266782}. +Q99N48 SYTL3_MOUSE Synaptotagmin-like protein 3 (Exophilin-6) 607 68,568 Alternative sequence (5); Chain (1); Domain (3); Mutagenesis (2); Sequence conflict (1) FUNCTION: May act as Rab effector protein and play a role in vesicle trafficking. Binds phospholipids in the presence of calcium ions. SUBCELLULAR LOCATION: Endomembrane system; Peripheral membrane protein. SUBUNIT: Monomer. Binds NRXN1. Binds RAB27A that has been activated by GTP-binding via its N-terminus. TISSUE SPECIFICITY: Highly expressed in spleen and lung. Detected at lower levels in heart and testis. {ECO:0000269|PubMed:11327731}. +Q9R0Q1 SYTL4_MOUSE Synaptotagmin-like protein 4 (Exophilin-2) (Granuphilin) 673 76,021 Alternative sequence (3); Chain (1); Compositional bias (1); Domain (3); Modified residue (6); Mutagenesis (6); Zinc finger (1) FUNCTION: Modulates exocytosis of dense-core granules and secretion of hormones in the pancreas and the pituitary. Interacts with vesicles containing negatively charged phospholipids in a Ca(2+)-independent manner. {ECO:0000269|PubMed:12590134}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10497219}; Peripheral membrane protein {ECO:0000269|PubMed:10497219}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000269|PubMed:10497219}; Peripheral membrane protein {ECO:0000269|PubMed:10497219}. Note=Detected close to the plasma membrane and on secretory granules. In pancreas, interacts with insulin-containing vesicles. SUBUNIT: Part of a ternary complex containing STX1A and RAB27A. Can bind both dominant negative and dominant active mutants of RAB27A. Binds STXBP1, RAB3A, RAB8A and RAB27B. Interacts with MYO5A. {ECO:0000269|PubMed:10497219, ECO:0000269|PubMed:11773082, ECO:0000269|PubMed:11956164, ECO:0000269|PubMed:12101244, ECO:0000269|PubMed:12590134, ECO:0000269|PubMed:23798443}. TISSUE SPECIFICITY: Detected in the pancreatic islet, in particular in insulin-positive beta cells, and in pituitary. {ECO:0000269|PubMed:10497219}. +P40749 SYT4_MOUSE Synaptotagmin-4 (Synaptotagmin IV) (SytIV) 425 47,659 Chain (1); Domain (2); Metal binding (10); Modified residue (1); Region (1); Sequence conflict (4); Topological domain (2); Transmembrane (1) TRANSMEM 17 37 Helical. {ECO:0000255}. TOPO_DOM 1 16 Vesicular. {ECO:0000255}.; TOPO_DOM 38 425 Cytoplasmic. {ECO:0000255}. FUNCTION: May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. Plays a role in dendrite formation by melanocytes. {ECO:0000250|UniProtKB:P50232, ECO:0000250|UniProtKB:Q9H2B2}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Single-pass membrane protein. TISSUE SPECIFICITY: Expressed in many regions of the nervous system but is undetectable in extra neural tissues (PubMed:8058779). {ECO:0000269|PubMed:8058779}. +Q920N7 SYT12_MOUSE Synaptotagmin-12 (Synaptotagmin XII) (SytXII) 421 46,680 Chain (1); Domain (2); Modified residue (3); Topological domain (2); Transmembrane (1) TRANSMEM 19 39 Helical. {ECO:0000255}. TOPO_DOM 1 18 Vesicular. {ECO:0000255}.; TOPO_DOM 40 421 Cytoplasmic. {ECO:0000255}. FUNCTION: May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. SUBUNIT: Homodimer. Can also form heterodimers (By similarity). {ECO:0000250}. +Q9R0N7 SYT7_MOUSE Synaptotagmin-7 (Synaptotagmin VII) (SytVII) 403 45,472 Alternative sequence (3); Beta strand (9); Chain (1); Domain (2); Helix (2); Metal binding (22); Modified residue (7); Mutagenesis (4); Topological domain (2); Transmembrane (1); Turn (2) TRANSMEM 17 37 Helical. {ECO:0000255}. TOPO_DOM 1 16 Vesicular. {ECO:0000255}.; TOPO_DOM 38 403 Cytoplasmic. {ECO:0000255}. FUNCTION: Ca(2+) sensor involved in Ca(2+)-dependent exocytosis of secretory and synaptic vesicles through Ca(2+) and phospholipid binding to the C2 domain. Ca(2+) induces binding of the C2-domains to phospholipid membranes and to assembled SNARE-complexes; both actions contribute to triggering exocytosis. SYT7 binds Ca(2+) with high affinity and slow kinetics compared to other synaptotagmins (PubMed:26738595). Involved in Ca(2+)-triggered lysosomal exocytosis, a major component of the plasma membrane repair (By similarity). Ca(2+)-regulated delivery of lysosomal membranes to the cell surface is also involved in the phagocytic uptake of particles by macrophages (PubMed:16982801, PubMed:21041449). Ca(2+)-triggered lysosomal exocytosis also plays a role in bone remodeling by regulating secretory pathways in osteoclasts and osteoblasts (PubMed:18539119). Involved in cholesterol transport from lysosome to peroxisome by promoting membrane contacts between lysosomes and peroxisomes: probably acts by promoting vesicle fusion by binding phosphatidylinositol-4,5-bisphosphate on peroxisomal membranes (PubMed:25860611). Acts as a key mediator of synaptic facilitation, a process also named short-term synaptic potentiation: synaptic facilitation takes place at synapses with a low initial release probability and is caused by influx of Ca(2+) into the axon terminal after spike generation, increasing the release probability of neurotransmitters (PubMed:24569478, PubMed:26738595). Probably mediates synaptic facilitation by directly increasing the probability of release (PubMed:26738595). May also contribute to synaptic facilitation by regulating synaptic vesicle replenishment, a process required to ensure that synaptic vesicles are ready for the arrival of the next action potential: SYT7 is required for synaptic vesicle replenishment by acting as a sensor for Ca(2+) and by forming a complex with calmodulin (PubMed:24569478). Also acts as a regulator of Ca(2+)-dependent insulin and glucagon secretion in beta-cells (PubMed:18308938, PubMed:19171650). Triggers exocytosis by promoting fusion pore opening and fusion pore expansion in chromaffin cells (PubMed:20956309). Also regulates the secretion of some non-synaptic secretory granules of specialized cells (By similarity). {ECO:0000250|UniProtKB:Q62747, ECO:0000269|PubMed:16982801, ECO:0000269|PubMed:18308938, ECO:0000269|PubMed:18539119, ECO:0000269|PubMed:19171650, ECO:0000269|PubMed:20956309, ECO:0000269|PubMed:21041449, ECO:0000269|PubMed:24569478, ECO:0000269|PubMed:25860611, ECO:0000269|PubMed:26738595}. PTM: Palmitoylated at its vesicular N-terminus; palmitoylation is required for localization to lysosome and phagocytosis in macrophages. {ECO:0000269|PubMed:21041449}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q62747}; Single-pass membrane protein {ECO:0000255}. Cell junction, synapse, presynaptic cell membrane {ECO:0000269|PubMed:11395007}; Single-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:24569478}; Single-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:21041449, ECO:0000269|PubMed:25860611}; Single-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, phagosome membrane {ECO:0000269|PubMed:16982801}; Single-pass membrane protein {ECO:0000255}. Peroxisome membrane {ECO:0000269|PubMed:25860611}; Single-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:Q62747}; Single-pass membrane protein {ECO:0000255}. Note=Localization to lysosomes is dependent on N-terminal palmitoylation and interaction with CD63. {ECO:0000269|PubMed:21041449}. SUBUNIT: Homodimer (PubMed:10871604). Can also form heterodimers with SYT6, SYT9 and SYT10 (PubMed:10871604). Interacts with calmodulin (CALM1, CALM2 or CALM3) (PubMed:24569478). Interacts with CD63; required for localization to lysosomes (PubMed:21041449). {ECO:0000269|PubMed:10871604, ECO:0000269|PubMed:21041449, ECO:0000269|PubMed:24569478}. DOMAIN: The C2 domains bind Ca(2+) and membranes. Binding to membranes involves Ca(2+)-dependent phospholipid binding. Compared to other members of the family, the C2 domains of SYT7 dock and insert into cellular membranes in response to intracellular Ca(2+) concentrations that are lower than those required for other synaptotagmins. The two C2 domains bind independently to planar membranes, without interdomain cooperativity. Moreover, SYT7 C2 domains insert more deeply into membranes compared to other synaptotagmins. {ECO:0000250|UniProtKB:O43581}. TISSUE SPECIFICITY: Widely expressed. Expressed in insulin-secreting cells (PubMed:18308938). Present in glucagon-secreting cells (at protein level) (PubMed:19171650). {ECO:0000269|PubMed:18308938, ECO:0000269|PubMed:19171650}. +Q9R0N9 SYT9_MOUSE Synaptotagmin-9 (Synaptotagmin IX) (SytIX) (Synaptotagmin V) 491 56,265 Chain (1); Domain (2); Metal binding (12); Modified residue (1); Region (1); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 53 73 Helical. {ECO:0000255}. TOPO_DOM 1 52 Vesicular. {ECO:0000255}.; TOPO_DOM 74 491 Cytoplasmic. {ECO:0000255}. FUNCTION: May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Single-pass membrane protein. SUBUNIT: Homodimer; disulfide-linked via the cysteine motif (PubMed:10531343). Can also form heterodimers with SYT3, SYT6, SYT7 and SYT10 (PubMed:10531343, PubMed:10531344, PubMed:10871604). Interacts with DNAJC5 and SNAP25, but not with HSC70 (PubMed:20847230). The interaction with DNAJC5 is stimulated tenfold in presence of calcium while the interaction with SNAP25 is inhibited (PubMed:20847230). {ECO:0000269|PubMed:10531343, ECO:0000269|PubMed:10531344, ECO:0000269|PubMed:10871604, ECO:0000269|PubMed:20847230}. DOMAIN: The cysteine motif mediates homo- or heterodimer formation via formation of disulfide bonds. {ECO:0000250|UniProtKB:O35681}. +Q8BYR1 TYW4_MOUSE tRNA wybutosine-synthesizing protein 4 (tRNA yW-synthesizing protein 4) (EC 2.1.1.290) (EC 2.3.1.231) (Leucine carboxyl methyltransferase 2) (p21WAF1/CIP1 promoter-interacting protein) (tRNA(Phe) (7-(3-amino-3-(methoxycarbonyl)propyl)wyosine(37)-N)-methoxycarbonyltransferase) (tRNA(Phe) (7-(3-amino-3-carboxypropyl)wyosine(37)-O)-methyltransferase) 686 75,295 Alternative sequence (2); Binding site (4); Chain (1); Erroneous initiation (2); Region (1); Sequence conflict (12) tRNA modification; wybutosine-tRNA(Phe) biosynthesis. FUNCTION: Probable S-adenosyl-L-methionine-dependent methyltransferase that acts as a component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA (By similarity). May methylate the carboxyl group of leucine residues to form alpha-leucine ester residues. {ECO:0000250}. SUBUNIT: Interacts with RNF144B/IBRDC2. {ECO:0000250}. +Q00899 TYY1_MOUSE Transcriptional repressor protein YY1 (Delta transcription factor) (NF-E1) (UCR-motif DNA-binding protein) (Yin and yang 1) (YY-1) 414 44,717 Chain (1); Compositional bias (4); Cross-link (8); Metal binding (16); Modified residue (3); Region (5); Sequence conflict (2); Zinc finger (4) FUNCTION: Multifunctional transcription factor that exhibits positive and negative control on a large number of cellular and viral genes by binding to sites overlapping the transcription start site. Binds to the consensus sequence 5'-CCGCCATNTT-3'; some genes have been shown to contain a longer binding motif allowing enhanced binding; the initial CG dinucleotide can be methylated greatly reducing the binding affinity. The effect on transcription regulation is depending upon the context in which it binds and diverse mechanisms of action include direct activation or repression, indirect activation or repression via cofactor recruitment, or activation or repression by disruption of binding sites or conformational DNA changes. Its activity is regulated by transcription factors and cytoplasmic proteins that have been shown to abrogate or completely inhibit YY1-mediated activation or repression. Binds to the upstream conserved region (UCR) (5'-CGCCATTTT-3') of Moloney murine leukemia virus (MuLV). Acts synergistically with the SMAD1 and SMAD4 in bone morphogenetic protein (BMP)-mediated cardiac-specific gene expression (PubMed:15329343). Binds to SMAD binding elements (SBEs) (5'-GTCT/AGAC-3') within BMP response element (BMPRE) of cardiac activating regions (PubMed:15329343). Proposed to recruit the PRC2/EED-EZH2 complex to target genes that are transcriptional repressed. Involved in DNA repair. In vitro, binds to DNA recombination intermediate structures (Holliday junctions). Involved in spermatogenesis and may play a role in meiotic DNA double-strand break repair. Plays a role in regulating enhancer activation (By similarity). {ECO:0000250|UniProtKB:P25490, ECO:0000269|PubMed:15329343, ECO:0000269|PubMed:18026119, ECO:0000269|PubMed:19786570}.; FUNCTION: Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair; proposed to target the INO80 complex to YY1-responsive elements. {ECO:0000250}. PTM: Transiently poly-ADP-ribosylated by PARP1 upon DNA damage, with the effect of decreasing affinity of YY1 to its cognate DNA binding sites. {ECO:0000250}.; PTM: Ubiquitinated. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21454521}. Nucleus matrix {ECO:0000269|PubMed:19786570}. Cytoplasm {ECO:0000269|PubMed:21454521}. Note=Associated with the nuclear matrix. In testis, localized to heterochromatin of spermatocytes. {ECO:0000269|PubMed:19786570}. SUBUNIT: Interacts with YAF2 through the region encompassing the first and second zinc fingers. Component of the chromatin remodeling INO80 complex; specifically part of a complex module associated with the DBINO domain of INO80. Interacts with EED and EZH2; the interactions are indicative for an association with the PRC2/EED-EZH2 complex (By similarity). Found in a complex with SMAD1 and SMAD4 (PubMed:15329343). Interacts with SFMBT2 (PubMed:18024232). Found in a complex with YY1, SIN3A and HDAC1 (PubMed:21454521). {ECO:0000250, ECO:0000269|PubMed:15329343, ECO:0000269|PubMed:18024232, ECO:0000269|PubMed:21454521}. TISSUE SPECIFICITY: Expressed in ovary and, at lower levels, in testis. {ECO:0000269|PubMed:18024232}. +Q8C4B4 U119B_MOUSE Protein unc-119 homolog B 251 28,303 Alternative sequence (1); Binding site (1); Chain (1); Initiator methionine (1); Modified residue (2); Sequence conflict (1) FUNCTION: Myristoyl-binding protein that acts as a cargo adapter: specifically binds the myristoyl moiety of a subset of N-terminally myristoylated proteins and is required for their localization. Binds myristoylated NPHP3 and plays a key role in localization of NPHP3 to the primary cilium membrane. Does not bind all myristoylated proteins. Probably plays a role in trafficking proteins in photoreceptor cells (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000250}. Note=Enriched at the transition zone and extended into the proximal end of the cilium. {ECO:0000250}. SUBUNIT: Found in a complex with ARL3, RP2 and UNC119B; RP2 induces hydrolysis of GTP ARL3 in the complex, leading to the release of UNC119B. Interacts with NPHP3 (when myristoylated). Interacts with CYS1 (when myristoylated). Interacts with C5orf30; interaction only takes place when UNC119B is not liganded with myristoylated proteins (By similarity). {ECO:0000250}. DOMAIN: Adopts an immunoglobulin-like beta-sandwich fold forming a hydrophobic cavity that capture N-terminally myristoylated target peptides. Phe residues within the hydrophobic beta sandwich are required for myristate binding (By similarity). {ECO:0000250}. +G5E8I7 U17LC_MOUSE Ubiquitin carboxyl-terminal hydrolase 17-like protein C (EC 3.4.19.12) (Deubiquitinating enzyme 2) 545 61,483 Active site (2); Chain (1); Domain (1); Mutagenesis (4); Sequence conflict (1) FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes (PubMed:8995226, PubMed:11443643). Important for preimplantation stage embryonic development (PubMed:22984479). {ECO:0000269|PubMed:11443643, ECO:0000269|PubMed:22984479, ECO:0000269|PubMed:8995226}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6R6M4}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q6R6M4}. TISSUE SPECIFICITY: Expressed in T cells. {ECO:0000269|PubMed:8995226}. +Q3TA38 T120B_MOUSE Transmembrane protein 120B 339 40,407 Alternative sequence (1); Chain (1); Coiled coil (1); Sequence conflict (1); Transmembrane (6) TRANSMEM 102 124 Helical. {ECO:0000255}.; TRANSMEM 132 152 Helical. {ECO:0000255}.; TRANSMEM 159 179 Helical. {ECO:0000255}.; TRANSMEM 187 207 Helical. {ECO:0000255}.; TRANSMEM 270 290 Helical. {ECO:0000255}.; TRANSMEM 302 322 Helical. {ECO:0000255}. FUNCTION: Necessary for efficient adipogenesis (PubMed:26024229). {ECO:0000269|PubMed:26024229}. SUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000269|PubMed:26024229}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Heterooligomer with TMEM120A. {ECO:0000269|PubMed:26024229}. TISSUE SPECIFICITY: Expressed in inguinal and subcutaneous white adipose tissue and in brown adipose tissue. {ECO:0000269|PubMed:26024229}. +Q8VC04 T106A_MOUSE Transmembrane protein 106A 261 29,109 Chain (1); Frameshift (2); Sequence conflict (6); Transmembrane (1) TRANSMEM 93 113 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q9D342 T170A_MOUSE Transmembrane protein 170A 144 15,224 Chain (1); Glycosylation (2); Topological domain (4); Transmembrane (3) TRANSMEM 51 71 Helical. {ECO:0000255}.; TRANSMEM 86 106 Helical. {ECO:0000255}.; TRANSMEM 117 137 Helical. {ECO:0000255}. TOPO_DOM 1 50 Extracellular. {ECO:0000250|UniProtKB:Q8WVE7}.; TOPO_DOM 72 85 Cytoplasmic. {ECO:0000250|UniProtKB:Q8WVE7}.; TOPO_DOM 107 116 Extracellular. {ECO:0000250|UniProtKB:Q8WVE7}.; TOPO_DOM 138 144 Cytoplasmic. {ECO:0000250|UniProtKB:Q8WVE7}. FUNCTION: Acts as a regulator of endoplasmic reticulum (ER) and nuclear envelope (NE) morphogenesis. Affects the ratio between tubular ER and ER sheets by promoting sheet formation at the expense of tubules. Influences NE expansion, nuclear pore complex formation and proper localization of inner nuclear membrane proteins. {ECO:0000250|UniProtKB:Q8WVE7}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8WVE7}; Multi-pass membrane protein {ECO:0000255}. Nucleus envelope {ECO:0000250|UniProtKB:Q8WVE7}. SUBUNIT: Interacts with RTN4. {ECO:0000250|UniProtKB:Q8WVE7}. +Q68FE7 T151B_MOUSE Transmembrane protein 151B 561 61,706 Chain (1); Compositional bias (3); Transmembrane (2) TRANSMEM 59 79 Helical. {ECO:0000255}.; TRANSMEM 106 126 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9EQ52 V1R48_MOUSE Vomeronasal type-1 receptor 48 (Vomeronasal type-1 receptor A3) (Vomeronasal type-1 receptor A6) 302 34,263 Chain (1); Disulfide bond (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 17 37 Helical; Name=1. {ECO:0000255}.; TRANSMEM 50 70 Helical; Name=2. {ECO:0000255}.; TRANSMEM 92 114 Helical; Name=3. {ECO:0000255}.; TRANSMEM 132 152 Helical; Name=4. {ECO:0000255}.; TRANSMEM 194 214 Helical; Name=5. {ECO:0000255}.; TRANSMEM 239 259 Helical; Name=6. {ECO:0000255}.; TRANSMEM 270 290 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 16 Extracellular. {ECO:0000255}.; TOPO_DOM 38 49 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 71 91 Extracellular. {ECO:0000255}.; TOPO_DOM 115 131 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 153 193 Extracellular. {ECO:0000255}.; TOPO_DOM 215 238 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 260 269 Extracellular. {ECO:0000255}.; TOPO_DOM 291 302 Cytoplasmic. {ECO:0000255}. FUNCTION: Putative pheromone receptor implicated in the regulation of social and reproductive behavior. {ECO:0000269|PubMed:12214233}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. +Q9CZ16 T178A_MOUSE Transmembrane protein 178A 297 33,082 Chain (1); Frameshift (2); Glycosylation (1); Sequence conflict (11); Signal peptide (1); Topological domain (4); Transmembrane (3) TRANSMEM 180 200 Helical. {ECO:0000255}.; TRANSMEM 209 229 Helical. {ECO:0000255}.; TRANSMEM 258 278 Helical. {ECO:0000255}. TOPO_DOM 26 179 Extracellular. {ECO:0000255}.; TOPO_DOM 201 208 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 230 257 Extracellular. {ECO:0000255}.; TOPO_DOM 279 297 Cytoplasmic. {ECO:0000255}. FUNCTION: Acts as a negative regulator of osteoclast differentiation in basal and inflammatory conditions by regulating TNFSF11-induced Ca (2+) fluxes, thereby controlling the induction of NFATC1 (PubMed:26644563). {ECO:0000269|PubMed:26644563}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:26644563}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Interacts with STIM1. {ECO:0000269|PubMed:26644563}. TISSUE SPECIFICITY: Highly expressed in the bone and its expression increases during osteoclastogenesis. {ECO:0000269|PubMed:26644563}. +Q8VCA6 T161A_MOUSE Transmembrane protein 161A 480 54,015 Alternative sequence (3); Chain (1); Erroneous initiation (1); Glycosylation (1); Sequence conflict (4); Signal peptide (1); Topological domain (9); Transmembrane (8) TRANSMEM 99 119 Helical. {ECO:0000255}.; TRANSMEM 135 155 Helical. {ECO:0000255}.; TRANSMEM 167 187 Helical. {ECO:0000255}.; TRANSMEM 225 245 Helical. {ECO:0000255}.; TRANSMEM 264 284 Helical. {ECO:0000255}.; TRANSMEM 305 325 Helical. {ECO:0000255}.; TRANSMEM 371 391 Helical. {ECO:0000255}.; TRANSMEM 451 473 Helical. {ECO:0000255}. TOPO_DOM 29 98 Extracellular. {ECO:0000255}.; TOPO_DOM 120 134 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 156 166 Extracellular. {ECO:0000255}.; TOPO_DOM 188 224 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 246 263 Extracellular. {ECO:0000255}.; TOPO_DOM 285 304 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 326 370 Extracellular. {ECO:0000255}.; TOPO_DOM 392 450 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 474 480 Extracellular. {ECO:0000255}. FUNCTION: May play a role in protection against oxidative stress. Overexpression leads to reduced levels of oxidant-induced DNA damage and apoptosis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8BHH9 T179A_MOUSE Transmembrane protein 179 233 26,463 Chain (1); Frameshift (1); Glycosylation (1); Sequence conflict (2); Transmembrane (4) TRANSMEM 6 26 Helical. {ECO:0000255}.; TRANSMEM 75 95 Helical. {ECO:0000255}.; TRANSMEM 104 124 Helical. {ECO:0000255}.; TRANSMEM 170 190 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8BG09 T184B_MOUSE Transmembrane protein 184B 407 45,589 Chain (1); Compositional bias (1); Modified residue (3); Sequence conflict (1); Transmembrane (7) TRANSMEM 40 60 Helical. {ECO:0000255}.; TRANSMEM 84 104 Helical. {ECO:0000255}.; TRANSMEM 121 141 Helical. {ECO:0000255}.; TRANSMEM 178 198 Helical. {ECO:0000255}.; TRANSMEM 214 234 Helical. {ECO:0000255}.; TRANSMEM 249 269 Helical. {ECO:0000255}.; TRANSMEM 290 310 Helical. {ECO:0000255}. FUNCTION: May activate the MAP kinase signaling pathway. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8K4L3 SVIL_MOUSE Supervillin (Archvillin) (p205/p250) 2170 243,162 Alternative sequence (2); Chain (1); Domain (1); Modified residue (26); Region (2); Repeat (5) FUNCTION: Isoform 1: Forms a high-affinity link between the actin cytoskeleton and the membrane. Is among the first costameric proteins to assemble during myogenesis and it contributes to myogenic membrane structure and differentiation. Appears to be involved in myosin II assembly. May modulate myosin II regulation through MLCK during cell spreading, an initial step in cell migration. May play a role in invadopodial function. {ECO:0000250|UniProtKB:O95425}.; FUNCTION: Isoform 2: May be involved in modulation of focal adhesions. Supervillin-mediated down-regulation of focal adhesions involves binding to TRIP6. Plays a role in cytokinesis through KIF14 interaction (By similarity). {ECO:0000250|UniProtKB:O46385}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O95425}; Peripheral membrane protein {ECO:0000250|UniProtKB:O95425}; Cytoplasmic side {ECO:0000250|UniProtKB:O95425}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O95425}. Cell projection, invadopodium {ECO:0000250|UniProtKB:O95425}. Cell projection, podosome {ECO:0000250|UniProtKB:O95425}. Midbody {ECO:0000250|UniProtKB:O46385}. Cleavage furrow {ECO:0000250|UniProtKB:O46385}. Note=Tightly associated with both actin filaments and plasma membranes. {ECO:0000250|UniProtKB:O95425}. SUBUNIT: Associates with F-actin (By similarity). Interacts with NEB (By similarity). Interacts with MYH9 (By similarity). Interacts with MYLK (By similarity). Isoform 2: Interacts with TRIP6 (By similarity). Isoform 2: Interacts with DYNLT1 (By similarity). Isoform 2: Interacts with KIF14; at midbody during cytokinesis (By similarity). {ECO:0000250|UniProtKB:O46385}. DOMAIN: As opposed to other villin-type headpiece domains, supervillin HP (SVHP) doesn't bind F-actin due to the absence of a conformationally flexible region (V-loop). {ECO:0000250}. +Q6PDF3 SVOPL_MOUSE Putative transporter SVOPL (SVOP-like protein) 494 54,461 Alternative sequence (2); Chain (1); Transmembrane (10) TRANSMEM 48 68 Helical. {ECO:0000255}.; TRANSMEM 86 106 Helical. {ECO:0000255}.; TRANSMEM 121 141 Helical. {ECO:0000255}.; TRANSMEM 179 199 Helical. {ECO:0000255}.; TRANSMEM 203 223 Helical. {ECO:0000255}.; TRANSMEM 281 301 Helical. {ECO:0000255}.; TRANSMEM 350 370 Helical. {ECO:0000255}.; TRANSMEM 385 405 Helical. {ECO:0000255}.; TRANSMEM 431 451 Helical. {ECO:0000255}.; TRANSMEM 460 480 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q80YD1 SUV3_MOUSE ATP-dependent RNA helicase SUPV3L1, mitochondrial (EC 3.6.4.13) (Suppressor of var1 3-like protein 1) (SUV3-like protein 1) 779 87,005 Chain (1); Domain (2); Modified residue (2); Nucleotide binding (1); Region (1); Sequence conflict (2); Transit peptide (1) FUNCTION: Major helicase player in mitochondrial RNA metabolism. Component of the mitochondrial degradosome (mtEXO) complex, that degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality in an ATP-dependent manner. ATPase and ATP-dependent multisubstrate helicase, able to unwind double-stranded (ds) DNA and RNA, and RNA/DNA heteroduplexes in the 5'-to-3' direction. Plays a role in the RNA surveillance system in mitochondria; regulates the stability of mature mRNAs, the removal of aberrantly formed mRNAs and the rapid degradation of non coding processing intermediates. Also implicated in recombination and chromatin maintenance pathways. May protect cells from apoptosis. Associates with mitochondrial DNA. {ECO:0000250|UniProtKB:Q8IYB8}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8IYB8}. Mitochondrion matrix {ECO:0000250|UniProtKB:Q8IYB8}. Mitochondrion matrix, mitochondrion nucleoid {ECO:0000250|UniProtKB:Q8IYB8}. SUBUNIT: Homodimer; in free form. Component of the mitochondrial degradosome (mtEXO) complex which is a heteropentamer containing 2 copies of SUPV3L1 and 3 copies of PNPT1. Interacts with LAMTOR5/HBXIP, WRN and BLM. {ECO:0000250|UniProtKB:Q8IYB8}. +Q99LQ4 SVBP_MOUSE Small vasohibin-binding protein (Coiled coil domain-containing protein 23) 66 7,836 Chain (1); Coiled coil (1) FUNCTION: Enhances the tyrosine carboxypeptidase activity of VASH1 and VASH2, thereby promoting the removal of the C-terminal tyrosine residue of alpha-tubulin (PubMed:29146868). Also required to enhance the solubility and secretion of VASH1 and VASH2 (By similarity). {ECO:0000250|UniProtKB:Q8N300, ECO:0000269|PubMed:29146868}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20736312}. Secreted {ECO:0000269|PubMed:20736312}. Note=Detected both intracellularly and extracellularly (PubMed:20736312). Within cells, localizes mainly to the apical part of the cell (PubMed:20736312). {ECO:0000269|PubMed:20736312}. SUBUNIT: Interacts with VASH1 and VASH2. {ECO:0000269|PubMed:29146868}. TISSUE SPECIFICITY: Highly expressed in bone marrow, spleen and testis. {ECO:0000269|PubMed:20736312}. +Q8BGQ7 SYAC_MOUSE Alanine--tRNA ligase, cytoplasmic (EC 6.1.1.7) (Alanyl-tRNA synthetase) (AlaRS) (Protein sticky) (Sti) 968 106,909 Binding site (6); Chain (1); Metal binding (4); Modified residue (4); Mutagenesis (2); Natural variant (1); Nucleotide binding (1); Sequence conflict (2) FUNCTION: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala) (PubMed:16906134, PubMed:20010690, PubMed:25422440, PubMed:27622773). Also edits incorrectly charged tRNA(Ala) via its editing domain (PubMed:16906134, PubMed:20010690, PubMed:25422440, PubMed:29769718). {ECO:0000255|HAMAP-Rule:MF_03133, ECO:0000269|PubMed:16906134, ECO:0000269|PubMed:20010690, ECO:0000269|PubMed:25422440, ECO:0000269|PubMed:27622773, ECO:0000269|PubMed:29769718}. PTM: ISGylated. {ECO:0000255|HAMAP-Rule:MF_03133, ECO:0000269|PubMed:16139798}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03133}. SUBUNIT: Monomer (By similarity). Interacts with ANKRD16; the interaction is direct (PubMed:29769718). {ECO:0000255|HAMAP-Rule:MF_03133, ECO:0000269|PubMed:29769718}. DOMAIN: Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs. {ECO:0000255|HAMAP-Rule:MF_03133}. DISEASE: Note=In sticky (sti); homozygous mice display an unkempt sticky appearance of fur and show cerebellar Purkinje cell loss and ataxia. Defects are caused by impaired ability to edit incorrectly charged tRNA(Ala), resulting in a two-fold increase in Ser-mischarged tRNA(Ala). This results in formation of ubiquitinated protein aggregates in cerebellar Purkinje cells and degeneration of these neurons. {ECO:0000269|PubMed:16906134}. +Q9D176 SUSD3_MOUSE Sushi domain-containing protein 3 269 28,285 Alternative sequence (3); Chain (1); Disulfide bond (2); Domain (1); Frameshift (1); Topological domain (2); Transmembrane (1) TRANSMEM 104 124 Helical. {ECO:0000255}. TOPO_DOM 1 103 Extracellular. {ECO:0000255}.; TOPO_DOM 125 269 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q96L08}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q96L08}. Note=Prominently localized to cell-cell borders. {ECO:0000250|UniProtKB:Q96L08}. +Q8BH32 SUSD4_MOUSE Sushi domain-containing protein 4 490 53,797 Alternative sequence (1); Chain (1); Disulfide bond (8); Domain (4); Glycosylation (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 320 340 Helical. {ECO:0000255}. TOPO_DOM 42 319 Extracellular. {ECO:0000255}.; TOPO_DOM 341 490 Cytoplasmic. {ECO:0000255}. FUNCTION: Acts as complement inhibitor by disrupting the formation of the classical C3 convertase. Isoform 3 inhibits the classical complement pathway, while membrane-bound isoform 1 inhibits deposition of C3b via both the classical and alternative complement pathways. {ECO:0000250|UniProtKB:Q5VX71, ECO:0000269|PubMed:20348246}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. TISSUE SPECIFICITY: High expression in brain and eye, with weaker expression in spinal cord and testis. Detected in white matter of brain and in the outer segments of photoreceptors. {ECO:0000269|PubMed:20348246}. +Q9EPK8 TRPV4_MOUSE Transient receptor potential cation channel subfamily V member 4 (TrpV4) (Osm-9-like TRP channel 4) (OTRPC4) (Transient receptor potential protein 12) (TRP12) (Vanilloid receptor-like channel 2) (Vanilloid receptor-like protein 2) (Vanilloid receptor-related osmotically-activated channel) (VR-OAC) 871 98,027 Binding site (5); Chain (1); Erroneous initiation (1); Frameshift (1); Glycosylation (1); Intramembrane (1); Metal binding (1); Modified residue (4); Motif (1); Mutagenesis (14); Nucleotide binding (1); Region (3); Repeat (3); Sequence conflict (7); Topological domain (8); Transmembrane (6) INTRAMEM 666 685 Pore-forming. {ECO:0000250|UniProtKB:O35433}. TRANSMEM 470 490 Helical. {ECO:0000250|UniProtKB:O35433}.; TRANSMEM 508 534 Helical. {ECO:0000250|UniProtKB:O35433}.; TRANSMEM 548 568 Helical. {ECO:0000250|UniProtKB:O35433}.; TRANSMEM 573 593 Helical. {ECO:0000250|UniProtKB:O35433}.; TRANSMEM 609 636 Helical. {ECO:0000250|UniProtKB:O35433}.; TRANSMEM 694 722 Helical. {ECO:0000250|UniProtKB:O35433}. TOPO_DOM 1 469 Cytoplasmic. {ECO:0000250|UniProtKB:O35433}.; TOPO_DOM 491 507 Extracellular. {ECO:0000250|UniProtKB:O35433}.; TOPO_DOM 535 547 Cytoplasmic. {ECO:0000250|UniProtKB:O35433}.; TOPO_DOM 569 572 Extracellular. {ECO:0000250|UniProtKB:O35433}.; TOPO_DOM 594 608 Cytoplasmic. {ECO:0000250|UniProtKB:O35433}.; TOPO_DOM 637 665 Extracellular. {ECO:0000250|UniProtKB:O35433}.; TOPO_DOM 686 693 Extracellular. {ECO:0000250|UniProtKB:O35433}.; TOPO_DOM 723 871 Cytoplasmic. {ECO:0000250|UniProtKB:O35433}. FUNCTION: Non-selective calcium permeant cation channel involved in osmotic sensitivity and mechanosensitivity (PubMed:11094154). Activation by exposure to hypotonicity within the physiological range exhibits an outward rectification (PubMed:12093812, PubMed:14691263, PubMed:16368742, PubMed:16571723). Also activated by heat, low pH, citrate and phorbol esters (PubMed:14691263). Increase of intracellular Ca(2+) potentiates currents. Channel activity seems to be regulated by a calmodulin-dependent mechanism with a negative feedback mechanism (By similarity). Acts as a regulator of intracellular Ca(2+) in synoviocytes (By similarity). Plays an obligatory role as a molecular component in the nonselective cation channel activation induced by 4-alpha-phorbol 12,13-didecanoate and hypotonic stimulation in synoviocytes and also regulates production of IL-8 (By similarity). Together with PKD2, forms mechano- and thermosensitive channels in cilium (PubMed:18695040). Promotes cell-cell junction formation in skin keratinocytes and plays an important role in the formation and/or maintenance of functional intercellular barriers (PubMed:20413591). Negatively regulates expression of PPARGC1A, UCP1, oxidative metabolism and respiration in adipocytes (PubMed:23021218). Regulates expression of chemokines and cytokines related to proinflammatory pathway in adipocytes (PubMed:23021218). Together with AQP5, controls regulatory volume decrease in salivary epithelial cells (PubMed:16571723). Required for normal development and maintenance of bone and cartilage (By similarity). {ECO:0000250|UniProtKB:Q9HBA0, ECO:0000269|PubMed:11094154, ECO:0000269|PubMed:12093812, ECO:0000269|PubMed:14691263, ECO:0000269|PubMed:16368742, ECO:0000269|PubMed:16571723, ECO:0000269|PubMed:18174177, ECO:0000269|PubMed:18695040, ECO:0000269|PubMed:20413591, ECO:0000269|PubMed:23021218}. PTM: N-glycosylated. {ECO:0000305|PubMed:16368742}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:14691263, ECO:0000269|PubMed:16571723, ECO:0000269|PubMed:16627472, ECO:0000269|PubMed:24509911, ECO:0000305|PubMed:12093812, ECO:0000305|PubMed:16368742}; Multi-pass membrane protein {ECO:0000305}. Cell junction, adherens junction {ECO:0000269|PubMed:20413591}. Cell projection, cilium {ECO:0000269|PubMed:18695040}. Note=Assembly of the putative homotetramer occurs primarily in the endoplasmic reticulum. {ECO:0000250|UniProtKB:Q9HBA0}. SUBUNIT: Homotetramer. Interacts with calmodulin (By similarity). Interacts with CTNNB1 (PubMed:20413591). The TRPV4 and CTNNB1 complex can interact with CDH1 (PubMed:20413591). Part of a complex containing MLC1, AQP4, HEPACAM and ATP1B1 (By similarity). Interacts with MAP7 and Src family Tyr protein kinases LYN, SRC, FYN, HCK, LCK and YES (PubMed:14517216, PubMed:12538589). Interacts with PACSIN1, PACSIN2 and PACSIN3 (via SH3 domain) (PubMed:16627472, PubMed:18174177). Interacts with ITPR3 (By similarity). Interacts with AQP5; the interaction is probably indirect and regulates TRPV4 activation by hypotonicity (PubMed:16571723). Interacts with ANO1 (PubMed:24509911). Interacts (via C-terminus) with PKD2 (via C-terminus) (PubMed:18695040). {ECO:0000250|UniProtKB:Q9HBA0, ECO:0000269|PubMed:12538589, ECO:0000269|PubMed:14517216, ECO:0000269|PubMed:16571723, ECO:0000269|PubMed:16627472, ECO:0000269|PubMed:18174177, ECO:0000269|PubMed:18695040, ECO:0000269|PubMed:20413591, ECO:0000269|PubMed:24509911}. DOMAIN: The ANK repeat region mediates interaction with Ca(2+)-calmodulin and ATP binding. The ANK repeat region mediates interaction with phosphatidylinositol-4,5-bisphosphate and related phosphatidylinositides. {ECO:0000250|UniProtKB:A0A1D5PXA5}. TISSUE SPECIFICITY: Detected in liver, kidney, heart, brain cortex, cerebellum and brainstem (at protein level). Expressed in salivary glands (at protein level) (PubMed:16571723). Expressed in heart, lung, spleen, liver, kidney, brain, skeletal muscle and testis. In the central nervous system, expressed in the lamina terminalis (arched vascular organ and neurons of the subfornical organ), median preoptic area, ventral hippocampal commissure, and ependymal cells of the choroid plexus. In the cochlea, expressed in both inner and outer hair cells, and in marginal cells of the cochlear stria vascularis. Expressed in large neurons of the trigeminal ganglion. In the kidney cortex, strongly expressed by epithelial cells of tubules and much weaker in glomeruli. {ECO:0000269|PubMed:11025659, ECO:0000269|PubMed:11081638, ECO:0000269|PubMed:11094154, ECO:0000269|PubMed:12692122, ECO:0000269|PubMed:16571723, ECO:0000269|PubMed:16627472}. +Q99KK9 SYHM_MOUSE Probable histidine--tRNA ligase, mitochondrial (EC 6.1.1.21) (Histidine--tRNA ligase-like) (Histidyl-tRNA synthetase) (HisRS) 505 56,985 Binding site (4); Chain (1); Modified residue (2); Region (2); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +Q8BMJ2 SYLC_MOUSE Leucine--tRNA ligase, cytoplasmic (EC 6.1.1.4) (Leucyl-tRNA synthetase) (LeuRS) 1178 134,192 Binding site (1); Chain (1); Modified residue (4); Motif (2); Sequence conflict (4) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +Q8BLY2 SYTC2_MOUSE Threonine--tRNA ligase 2, cytoplasmic (EC 6.1.1.3) (Threonyl-tRNA synthetase) (ThrRS) (Threonyl-tRNA synthetase-like protein 2) 790 91,318 Chain (1); Coiled coil (1); Initiator methionine (1); Modified residue (2); Motif (1); Mutagenesis (5); Sequence conflict (1) FUNCTION: Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged tRNA(Thr) via its editing domain, at the post-transfer stage. {ECO:0000269|PubMed:29579307}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29579307}. Nucleus {ECO:0000269|PubMed:29579307}. Note=Primarily cytoplasmic. Also detected at lower levels in the nucleus. {ECO:0000269|PubMed:29579307}. SUBUNIT: May be a component of the multisynthetase complex (MSC), a large multi-subunit complex which contains at least eight different aminoacyl-tRNA synthetases plus three auxillary subunits AIMP1, AIMP2 and EEF1E1. Interacts with the MSC components EPRS, AIMP1, AIMP2 and KARS. {ECO:0000250|UniProtKB:A2RTX5}. TISSUE SPECIFICITY: Ubiquitious (at protein level). Strongly expressed in muscle (at protein level). Moderately expressed in heart and liver (at protein level). Weakly expressed in stomach, kidney, testis, spleen, brain, fat and lung (at protein level). {ECO:0000269|PubMed:29579307}. +Q8BG71 TYW2_MOUSE tRNA wybutosine-synthesizing protein 2 homolog (tRNA-yW-synthesizing protein 2) (EC 2.5.1.114) (tRNA(Phe) (4-demethylwyosine(37)-C(7)) aminocarboxypropyltransferase) 446 50,299 Binding site (3); Chain (1); Frameshift (2); Region (1); Sequence conflict (4) tRNA modification; wybutosine-tRNA(Phe) biosynthesis. FUNCTION: S-adenosyl-L-methionine-dependent transferase that acts as a component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA. Catalyzes the transfer of the alpha-amino-alpha-carboxypropyl (acp) group from S-adenosyl-L-methionine to the C-7 position of 4-demethylwyosine (imG-14) to produce wybutosine-86 (By similarity). {ECO:0000250}. +Q8BSA9 TYW3_MOUSE tRNA wybutosine-synthesizing protein 3 homolog (tRNA-yW-synthesizing protein 3) (EC 2.1.1.282) (tRNA(Phe) 7-((3-amino-3-carboxypropyl)-4-demethylwyosine(37)-N(4))-methyltransferase) 257 28,575 Chain (1); Erroneous initiation (1); Modified residue (1) tRNA modification; wybutosine-tRNA(Phe) biosynthesis. FUNCTION: Probable S-adenosyl-L-methionine-dependent methyltransferase that acts as a component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA (By similarity). {ECO:0000250}. +Q3TTC2 TYY2_MOUSE Transcription factor YY2 (Yin and yang 2) (YY-2) 378 42,031 Chain (1); Region (2); Sequence conflict (1); Zinc finger (4) FUNCTION: Functions as a multifunctional transcription factor that may exhibit positive and negative control on a large number of genes. May antagonize YY1 and function in development and differentiation. {ECO:0000269|PubMed:17478514}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: Weakly expressed by neuronal and glial cells in the cerebral cortex. Expressed by Purkinje cells and in the granular layers of the cerebellum. Expressed in all layers of spermatocytes in testis but not detected in sperm cells. {ECO:0000269|PubMed:16377127}. +Q9DBY1 SYVN1_MOUSE E3 ubiquitin-protein ligase synoviolin (EC 2.3.2.27) (RING-type E3 ubiquitin transferase synoviolin) (Synovial apoptosis inhibitor 1) 612 67,296 Alternative sequence (5); Chain (1); Compositional bias (2); Modified residue (1); Region (2); Sequence conflict (2); Signal peptide (1); Topological domain (6); Transmembrane (5); Zinc finger (1) TRANSMEM 42 62 Helical. {ECO:0000255}.; TRANSMEM 99 119 Helical. {ECO:0000255}.; TRANSMEM 141 161 Helical. {ECO:0000255}.; TRANSMEM 170 190 Helical. {ECO:0000255}.; TRANSMEM 225 245 Helical. {ECO:0000255}. TOPO_DOM 23 41 Lumenal. {ECO:0000255}.; TOPO_DOM 63 98 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 120 140 Lumenal. {ECO:0000255}.; TOPO_DOM 162 169 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 191 224 Lumenal. {ECO:0000255}.; TOPO_DOM 246 612 Cytoplasmic. {ECO:0000255}. Protein modification; protein ubiquitination. FUNCTION: Acts as an E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated UBC7 E2 ligase and transfers it to substrates, promoting their degradation (PubMed:12975321, PubMed:15611074). Component of the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins (PubMed:12975321, PubMed:15611074). Also promotes the degradation of normal but naturally short-lived proteins such as SGK. Protects cells from ER stress-induced apoptosis. Sequesters p53/TP53 in the cytoplasm and promotes its degradation, thereby negatively regulating its biological function in transcription, cell cycle regulation and apoptosis (PubMed:17170702). Required for embryogenesis (PubMed:15611074). Mediates the ubiquitination and subsequent degradation of cytoplasmic NFE2L1 (PubMed:21911472). {ECO:0000269|PubMed:12975321, ECO:0000269|PubMed:15611074, ECO:0000269|PubMed:17170702, ECO:0000269|PubMed:21911472}. PTM: Auto-ubiquitinated. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:17059562}; Multi-pass membrane protein {ECO:0000269|PubMed:17059562}. SUBUNIT: Homodimer (By similarity). Interacts with p53/TP53 and HTT (PubMed:17170702). Interacts with VCP, HERPUD1 and DERL1. Part of a complex containing SYVN1, HERPUD1, SELENOS and DERL1; which probably transfer misfolded proteins from the ER to VCP (By similarity). Part of a complex containing SYVN1, SEL1L and DERL2 (By similarity). Interacts with UBXN6 (By similarity). Interacts (via N-terminal loop) with SEL1L; recruits ERLEC1 and OS9. May form a complex with ERLEC1; HSPA5; OS9 AND SEL1L (PubMed:27064360). Interacts with BAG6 (By similarity). Interacts with NFE2L1 (PubMed:21911472). {ECO:0000250|UniProtKB:Q86TM6, ECO:0000269|PubMed:17170702, ECO:0000269|PubMed:21911472, ECO:0000269|PubMed:27064360}. DOMAIN: The RING-type zinc finger is required for E3 ligase activity. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in bone, spleen, lung and testis. In the brain, present in neurons but not in glial cells. Up-regulated in synovial tissues from mice with collagen-induced arthritis (at protein level). {ECO:0000269|PubMed:12975321, ECO:0000269|PubMed:17059562}. +Q61068 U17PA_MOUSE Ubiquitin carboxyl-terminal hydrolase 17-like protein A (USP17-A) (EC 3.4.19.12) (Deubiquitinating enzyme 1) (Ubiquitin carboxyl-terminal hydrolase DUB-1) (Ubiquitin thioesterase DUB-1) (Ubiquitin-specific-processing protease DUB-1) 526 59,073 Active site (2); Chain (1); Domain (1); Mutagenesis (1) FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes. Has deubiquitinating enzyme activity for DNAH5, suggesting a role in the regulation of DNAH5 degradation by the ubiquitin-proteasome pathway. Has growth-suppressing activity; induces arrest in G1 phase upon controlled expression. {ECO:0000269|PubMed:18980247, ECO:0000269|PubMed:8622927}. PTM: Polyubiquitinated; ubiquitination leads to its subsequent degradation. {ECO:0000269|PubMed:18980247}. TISSUE SPECIFICITY: Expressed in hematopoietic progenitor cell lines Ba/F3 and FDCP1. Not detected in brain, lung, liver, kidney, thymus, spleen and bone marrow. {ECO:0000269|PubMed:8756639}. +D3YU32 T13C1_MOUSE Testis-expressed protein 13C-1 (TEX13 family member C-1) 604 67,298 Chain (1) +Q8C817 T200A_MOUSE Transmembrane protein 200A 491 54,008 Chain (1); Erroneous initiation (1); Glycosylation (1); Modified residue (1); Sequence conflict (1); Topological domain (3); Transmembrane (2) TRANSMEM 62 82 Helical. {ECO:0000255}.; TRANSMEM 127 147 Helical. {ECO:0000255}. TOPO_DOM 1 61 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 83 126 Extracellular. {ECO:0000255}.; TOPO_DOM 148 491 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9EQ51 V1R47_MOUSE Vomeronasal type-1 receptor 47 (Vomeronasal type-1 receptor A4) (Vomeronasal type-1 receptor A7) 310 35,433 Chain (1); Disulfide bond (1); Glycosylation (1); Sequence conflict (1); Topological domain (8); Transmembrane (7) TRANSMEM 17 37 Helical; Name=1. {ECO:0000255}.; TRANSMEM 50 70 Helical; Name=2. {ECO:0000255}.; TRANSMEM 92 114 Helical; Name=3. {ECO:0000255}.; TRANSMEM 132 152 Helical; Name=4. {ECO:0000255}.; TRANSMEM 194 214 Helical; Name=5. {ECO:0000255}.; TRANSMEM 239 259 Helical; Name=6. {ECO:0000255}.; TRANSMEM 270 290 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 16 Extracellular. {ECO:0000255}.; TOPO_DOM 38 49 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 71 91 Extracellular. {ECO:0000255}.; TOPO_DOM 115 131 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 153 193 Extracellular. {ECO:0000255}.; TOPO_DOM 215 238 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 260 269 Extracellular. {ECO:0000255}.; TOPO_DOM 291 310 Cytoplasmic. {ECO:0000255}. FUNCTION: Putative pheromone receptor implicated in the regulation of social and reproductive behavior. {ECO:0000269|PubMed:12214233}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. +Q9EPB8 V1R54_MOUSE Vomeronasal type-1 receptor 54 (Pheromone receptor VN7) (Vomeronasal receptor 7) (Vomeronasal type-1 receptor A9) 315 35,854 Chain (1); Disulfide bond (1); Topological domain (8); Transmembrane (7) TRANSMEM 16 40 Helical; Name=1. {ECO:0000255}.; TRANSMEM 52 71 Helical; Name=2. {ECO:0000255}.; TRANSMEM 91 112 Helical; Name=3. {ECO:0000255}.; TRANSMEM 133 154 Helical; Name=4. {ECO:0000255}.; TRANSMEM 194 212 Helical; Name=5. {ECO:0000255}.; TRANSMEM 240 260 Helical; Name=6. {ECO:0000255}.; TRANSMEM 268 288 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 15 Extracellular. {ECO:0000255}.; TOPO_DOM 41 51 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 72 90 Extracellular. {ECO:0000255}.; TOPO_DOM 113 132 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 155 193 Extracellular. {ECO:0000255}.; TOPO_DOM 213 239 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 261 267 Extracellular. {ECO:0000255}.; TOPO_DOM 289 315 Cytoplasmic. {ECO:0000255}. FUNCTION: Putative pheromone receptor implicated in the regulation of social and reproductive behavior. {ECO:0000269|PubMed:12214233}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. +Q8C2L6 T161B_MOUSE Transmembrane protein 161B 487 55,467 Chain (1); Glycosylation (3); Transmembrane (8) TRANSMEM 107 127 Helical. {ECO:0000255}.; TRANSMEM 136 156 Helical. {ECO:0000255}.; TRANSMEM 169 189 Helical. {ECO:0000255}.; TRANSMEM 228 248 Helical. {ECO:0000255}.; TRANSMEM 265 285 Helical. {ECO:0000255}.; TRANSMEM 305 325 Helical. {ECO:0000255}.; TRANSMEM 367 387 Helical. {ECO:0000255}.; TRANSMEM 459 479 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +P62500 T22D1_MOUSE TSC22 domain family protein 1 (Regulatory protein TSC-22) (TGFB-stimulated clone 22 homolog) (TSC22-related inducible leucine zipper 1b) (Transforming growth factor beta-1-induced transcript 4 protein) 1077 109,811 Alternative sequence (3); Chain (1); Compositional bias (5); Erroneous initiation (3); Modified residue (1); Region (1); Sequence conflict (11) FUNCTION: Transcriptional repressor. Acts on the C-type natriuretic peptide (CNP) promoter. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. SUBUNIT: Homodimer or heterodimer. Can form a heterodimer with TSC22D4 (By similarity). {ECO:0000250}. +Q9Z2S7 T22D3_MOUSE TSC22 domain family protein 3 (Glucocorticoid-induced leucine zipper protein) (TSC22-related-inducible leucine zipper 3) (Tilz3) 137 15,177 Alternative sequence (3); Chain (1); Modified residue (5); Region (2); Sequence conflict (2) FUNCTION: Protects T-cells from IL2 deprivation-induced apoptosis through the inhibition of FOXO3A transcriptional activity that leads to the down-regulation of the pro-apoptotic factor BCL2L11. In macrophages, plays a role in the anti-inflammatory and immunosuppressive effects of glucocorticoids and IL10. In T-cells, inhibits anti-CD3-induced NFKB1 nuclear translocation. In vitro, suppresses AP1 and NFKB1 DNA-binding activities (By similarity). Isoform 1 and isoform 4 inhibit myogenic differentiation and mediate anti-myogenic effects of glucocorticoids by binding and regulating MYOD1 and HDAC1 transcriptional activity resulting in reduced expression of MYOG. {ECO:0000250, ECO:0000269|PubMed:20124407}. SUBCELLULAR LOCATION: Isoform 1: Cytoplasm. Nucleus. Note=Localization depends on differentiation status of myoblasts. In undifferentiated myoblasts, isoform 1 localizes to the cytoplasm, but in differentiating myoblasts, isoform 1 is localized to the nucleus.; SUBCELLULAR LOCATION: Isoform 4: Cytoplasm. Nucleus. Note=Localization depends on differentiation status of myoblasts. In undifferentiated myoblasts, isoform 4 localizes to the cytoplasm, but in differentiating myoblasts, isoform 4 is localized to the nucleus. SUBUNIT: Can form homodimers, however it is likely to function as a monomer. Interacts with AP1 and NFKB1 (By similarity). Isoform 1 and isoform 4 interact with MYOD1. Isoform 1 interacts with HDAC1; this interaction affects HDAC1 activity on MYOG promoter and thus inhibits MYOD1 transcriptional activity. {ECO:0000250, ECO:0000269|PubMed:11397794, ECO:0000269|PubMed:20124407}. DOMAIN: The leucine-zipper is involved in homodimerization. TISSUE SPECIFICITY: Constitutively expressed in lung, intestine, kidney and liver, most probably by resident cells from the macrophage lineage. Expression inversely correlates with T-cell activation, being higher in resting cells and lower in cells activated by TCR/CD3 triggering. Isoform 1 and isoform 4 are expressed in spleen and skeletal muscle (at protein level). Isoform 1 is expressed in thymus, lymph nodes, bone marrow, spleen, lung and skeletal muscle. {ECO:0000269|PubMed:11468175, ECO:0000269|PubMed:12393603, ECO:0000269|PubMed:20124407}. +Q3UFJ6 T184A_MOUSE Transmembrane protein 184A (Sexually dimorphic expressed in male gonads 1) 425 46,818 Chain (1); Erroneous initiation (1); Sequence conflict (2); Transmembrane (7) TRANSMEM 51 71 Helical. {ECO:0000255}.; TRANSMEM 96 116 Helical. {ECO:0000255}.; TRANSMEM 133 153 Helical. {ECO:0000255}.; TRANSMEM 189 209 Helical. {ECO:0000255}.; TRANSMEM 226 246 Helical. {ECO:0000255}.; TRANSMEM 261 281 Helical. {ECO:0000255}.; TRANSMEM 303 323 Helical. {ECO:0000255}. FUNCTION: Acts as a heparin receptor in vascular cells (By similarity). May be involved in vesicle transport in exocrine cells and Sertoli cells (PubMed:18321981, PubMed:19097053). {ECO:0000250|UniProtKB:Q4QQS1, ECO:0000269|PubMed:18321981, ECO:0000269|PubMed:19097053}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q1RMW2}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q1RMW2}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q1RMW2}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000269|PubMed:18321981}; Multi-pass membrane protein {ECO:0000305}. Endosome {ECO:0000269|PubMed:18321981, ECO:0000269|PubMed:19097053}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000269|PubMed:19097053}. Note=Colocalizes with the secretory granule marker VAMP2 in pancreatic acinar cells (PubMed:19097053). {ECO:0000269|PubMed:19097053}. TISSUE SPECIFICITY: Expressed in testis, pancreas, parotid salivary gland and mammary gland (at protein level)(PubMed:17616727, PubMed:19097053). {ECO:0000269|PubMed:17616727, ECO:0000269|PubMed:19097053}. +Q99J38 T30A1_MOUSE Tetratricopeptide repeat protein 30A1 (TPR repeat protein 30A1) 664 76,238 Chain (1); Coiled coil (1); Compositional bias (1); Repeat (8); Sequence conflict (2) FUNCTION: Required for polyglutamylation of axonemal tubulin. Plays a role in anterograde intraflagellar transport (IFT), the process by which cilia precursors are transported from the base of the cilium to the site of their incorporation at the tip. {ECO:0000250}. SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000250}. +P59532 T2R41_MOUSE Taste receptor type 2 member 41 (T2R41) (T2R12) (T2R26) 308 36,177 Chain (1); Glycosylation (2); Topological domain (8); Transmembrane (7) TRANSMEM 8 28 Helical; Name=1. {ECO:0000255}.; TRANSMEM 61 81 Helical; Name=2. {ECO:0000255}.; TRANSMEM 89 109 Helical; Name=3. {ECO:0000255}.; TRANSMEM 129 149 Helical; Name=4. {ECO:0000255}.; TRANSMEM 187 207 Helical; Name=5. {ECO:0000255}.; TRANSMEM 240 260 Helical; Name=6. {ECO:0000255}.; TRANSMEM 265 285 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 7 Extracellular. {ECO:0000255}.; TOPO_DOM 29 60 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 82 88 Extracellular. {ECO:0000255}.; TOPO_DOM 110 128 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 150 186 Extracellular. {ECO:0000255}.; TOPO_DOM 208 239 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 261 264 Extracellular. {ECO:0000255}.; TOPO_DOM 286 308 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor that may play a role in the perception of bitterness and is gustducin-linked. May play a role in sensing the chemical composition of the gastrointestinal content. The activity of this receptor may stimulate alpha gustducin, mediate PLC-beta-2 activation and lead to the gating of TRPM5 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed in subsets of taste receptor cells of the tongue and palate epithelium and exclusively in gustducin-positive cells. +Q9WVA4 TAGL2_MOUSE Transgelin-2 (SM22-beta) 199 22,395 Chain (1); Cross-link (1); Domain (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (8); Repeat (1); Sequence conflict (2) +Q99JX1 TAF11_MOUSE Transcription initiation factor TFIID subunit 11 (TFIID subunit p30-beta) (Transcription initiation factor TFIID 28 kDa subunit) (TAF(II)28) (TAFII-28) (TAFII28) 211 23,333 Chain (1); Modified residue (1) FUNCTION: Core TAFII present in both of the previously described TFIID species which either lack or contain TAFII30 (TFIID alpha and TFIID beta respectively). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: TFIID is composed of TATA binding protein (TBP) and a number of TBP-associated factors (TAFs). {ECO:0000250}. DOMAIN: TBP and TAFII18 bind to distinct domains of TAFII28. {ECO:0000250}. +Q7M732 RTL1_MOUSE Retrotransposon-like protein 1 (Mammalian retrotransposon derived protein 1) (Paternally expressed gene 11 protein) (Retrotransposon-derived protein PEG11) 1744 199,048 Chain (1); Compositional bias (9); Transmembrane (2) TRANSMEM 1473 1493 Helical. {ECO:0000255}.; TRANSMEM 1520 1540 Helical. {ECO:0000255}. FUNCTION: Plays an essential role in capillaries endothelial cells for the maintenance of feto-maternal interface and for development of the placenta. {ECO:0000269|PubMed:18176565}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in placenta and in various tissues in late-fetal stage. {ECO:0000269|PubMed:18176565}. +Q32KG4 RTL9_MOUSE Retrotransposon Gag-like protein 9 (Retrotransposon gag domain-containing protein 1) (Sushi-XF2) 1339 138,467 Alternative sequence (1); Chain (1) +Q6PDC0 RUN3B_MOUSE RUN domain-containing protein 3B 408 45,138 Chain (1); Coiled coil (1); Compositional bias (1); Domain (1); Modified residue (3) SUBUNIT: Interacts with RAP2A. {ECO:0000250}. +Q8R4C2 RUFY2_MOUSE RUN and FYVE domain-containing protein 2 (Leucine zipper FYVE-finger protein) (LZ-FYVE) 606 70,093 Chain (1); Coiled coil (2); Domain (1); Erroneous initiation (1); Sequence conflict (2); Zinc finger (1) SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11506704}. SUBUNIT: Interacts with BMX. {ECO:0000250}. +Q5FW56 T255B_MOUSE Transmembrane protein 255B (Protein FAM70B) 369 39,392 Chain (1); Compositional bias (1); Sequence conflict (1); Transmembrane (2) TRANSMEM 129 149 Helical. {ECO:0000255}.; TRANSMEM 244 264 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +P28705 RXRG_MOUSE Retinoic acid receptor RXR-gamma (Nuclear receptor subfamily 2 group B member 3) (Retinoid X receptor gamma) 463 50,893 Chain (1); DNA binding (1); Domain (1); Region (2); Sequence conflict (1); Zinc finger (2) FUNCTION: Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RAR/RXR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. The high affinity ligand for RXRs is 9-cis retinoic acid (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Homodimer (By similarity) Heterodimer with a RAR molecule. Binds DNA preferentially as a RAR/RXR heterodimer. {ECO:0000250}. DOMAIN: Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain. +A2ADF7 S2534_MOUSE Solute carrier family 25 member 34 318 33,778 Alternative sequence (2); Chain (1); Repeat (3); Transmembrane (6) TRANSMEM 21 41 Helical; Name=1. {ECO:0000255}.; TRANSMEM 59 79 Helical; Name=2. {ECO:0000255}.; TRANSMEM 112 134 Helical; Name=3. {ECO:0000255}.; TRANSMEM 184 205 Helical; Name=4. {ECO:0000255}.; TRANSMEM 220 240 Helical; Name=5. {ECO:0000255}.; TRANSMEM 292 315 Helical; Name=6. {ECO:0000255}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q8BVN7 S2541_MOUSE Solute carrier family 25 member 41 312 34,505 Alternative sequence (1); Chain (1); Repeat (3); Transmembrane (6) TRANSMEM 33 50 Helical; Name=1. {ECO:0000255}.; TRANSMEM 88 107 Helical; Name=2. {ECO:0000255}.; TRANSMEM 131 144 Helical; Name=3. {ECO:0000255}.; TRANSMEM 182 200 Helical; Name=4. {ECO:0000255}.; TRANSMEM 219 243 Helical; Name=5. {ECO:0000255}.; TRANSMEM 279 298 Helical; Name=6. {ECO:0000255}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:O94502}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O94502}. +Q9JI02 S2B20_MOUSE Secretoglobin family 2B member 20 (Allergen dI chain C2C) (Androgen-binding protein delta) (Lacrimal androgen-binding protein delta) 112 12,590 Chain (1); Glycosylation (1); Sequence conflict (2); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Expressed in lacrimal gland, at higher level in males than females. Expressed in the submandibular gland. {ECO:0000269|PubMed:15623751}. +Q7M747 S2B24_MOUSE Secretoglobin family 2B member 24 (Allergen dI chain C2B) (Androgen-binding protein zeta) (Lacrimal androgen-binding protein zeta) 112 12,535 Chain (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Expressed in lacrimal gland, at higher level in males than females. {ECO:0000269|PubMed:15623751}. +Q9Z0E8 S22A5_MOUSE Solute carrier family 22 member 5 (High-affinity sodium-dependent carnitine cotransporter) (Organic cation/carnitine transporter 2) 557 62,780 Chain (1); Glycosylation (3); Modified residue (3); Natural variant (1); Nucleotide binding (1); Topological domain (13); Transmembrane (12) TRANSMEM 21 41 Helical; Name=1. {ECO:0000255}.; TRANSMEM 143 163 Helical; Name=2. {ECO:0000255}.; TRANSMEM 173 193 Helical; Name=3. {ECO:0000255}.; TRANSMEM 198 218 Helical; Name=4. {ECO:0000255}.; TRANSMEM 233 253 Helical; Name=5. {ECO:0000255}.; TRANSMEM 258 278 Helical; Name=6. {ECO:0000255}.; TRANSMEM 342 362 Helical; Name=7. {ECO:0000255}.; TRANSMEM 374 394 Helical; Name=8. {ECO:0000255}.; TRANSMEM 407 427 Helical; Name=9. {ECO:0000255}.; TRANSMEM 431 451 Helical; Name=10. {ECO:0000255}.; TRANSMEM 463 483 Helical; Name=11. {ECO:0000255}.; TRANSMEM 489 509 Helical; Name=12. {ECO:0000255}. TOPO_DOM 1 20 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 42 142 Extracellular. {ECO:0000255}.; TOPO_DOM 164 172 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 194 197 Extracellular. {ECO:0000255}.; TOPO_DOM 219 232 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 254 257 Extracellular. {ECO:0000255}.; TOPO_DOM 279 341 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 363 373 Extracellular. {ECO:0000255}.; TOPO_DOM 395 406 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 428 430 Extracellular. {ECO:0000255}.; TOPO_DOM 452 462 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 484 488 Extracellular. {ECO:0000255}.; TOPO_DOM 510 557 Cytoplasmic. {ECO:0000255}. FUNCTION: Sodium-ion dependent, high affinity carnitine transporter. Involved in the active cellular uptake of carnitine. Transports one sodium ion with one molecule of carnitine. Also transports organic cations such as tetraethylammonium (TEA) without the involvement of sodium. Also relative uptake activity ratio of carnitine to TEA is 11.3. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:15523054}; Multi-pass membrane protein {ECO:0000269|PubMed:15523054}. Note=Colocalizes with PDZK1 on apical membranes of kidney proximal tubules. SUBUNIT: Interacts with PDZK1. {ECO:0000269|PubMed:15523054}. TISSUE SPECIFICITY: Widely expressed. Expressed in kidney, liver and testis. {ECO:0000269|PubMed:11010964}. DISEASE: Note=Defects in Slc22a5 are the cause of the juvenile visceral steatosis (JVS) phenotype. JVS is an autosomal recessive animal model of systemic carnitine deficiency. +P56565 S10A1_MOUSE Protein S100-A1 (S-100 protein alpha chain) (S-100 protein subunit alpha) (S100 calcium-binding protein A1) 94 10,505 Calcium binding (2); Chain (1); Domain (2); Modified residue (1); Sequence conflict (4) FUNCTION: Probably acts as a Ca(2+) signal transducer. In response to an increase in intracellular Ca(2+) levels, binds calcium which triggers a conformational change. This conformational change allows interaction of S1001A with specific target proteins, such as TPR-containing proteins, and the modulation of their activity. {ECO:0000250|UniProtKB:P23297}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P23297}. SUBUNIT: Dimer of either two alpha chains, or two beta chains, or one alpha and one beta chain. Also forms heterodimers with S100P. Interacts with AGER. Interacts with CAPZA1. Interacts with FKBP4. Interacts with RYR1 and RYR2. Interacts with CACYBP in a calcium-dependent manner. Interacts with PPP5C (via TPR repeats); the interaction is calcium-dependent and modulates PPP5C activity. {ECO:0000250|UniProtKB:P23297, ECO:0000250|UniProtKB:P35467}. +Q8R0S9 S22AM_MOUSE Solute carrier family 22 member 22 (Prostaglandin-specific organic anion transporter) 554 62,424 Chain (1); Glycosylation (2); Topological domain (13); Transmembrane (12) TRANSMEM 16 36 Helical; Name=1. {ECO:0000255}.; TRANSMEM 145 165 Helical; Name=2. {ECO:0000255}.; TRANSMEM 173 193 Helical; Name=3. {ECO:0000255}.; TRANSMEM 200 220 Helical; Name=4. {ECO:0000255}.; TRANSMEM 232 252 Helical; Name=5. {ECO:0000255}.; TRANSMEM 259 279 Helical; Name=6. {ECO:0000255}.; TRANSMEM 348 368 Helical; Name=7. {ECO:0000255}.; TRANSMEM 377 397 Helical; Name=8. {ECO:0000255}.; TRANSMEM 406 426 Helical; Name=9. {ECO:0000255}.; TRANSMEM 435 455 Helical; Name=10. {ECO:0000255}.; TRANSMEM 467 487 Helical; Name=11. {ECO:0000255}.; TRANSMEM 492 512 Helical; Name=12. {ECO:0000255}. TOPO_DOM 1 15 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 37 144 Extracellular. {ECO:0000305}.; TOPO_DOM 166 172 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 194 199 Extracellular. {ECO:0000305}.; TOPO_DOM 221 231 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 253 258 Extracellular. {ECO:0000305}.; TOPO_DOM 280 347 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 369 376 Extracellular. {ECO:0000305}.; TOPO_DOM 398 405 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 427 434 Extracellular. {ECO:0000305}.; TOPO_DOM 456 466 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 488 491 Extracellular. {ECO:0000305}.; TOPO_DOM 513 554 Cytoplasmic. {ECO:0000305}. FUNCTION: Sodium-independent organic anion transporter which exhibits high specificity for a subset of prostaglandins including prostaglandin E2 (PGE2), prostaglandin E1 (PGE1), prostaglandin F2-alpha (PGF2-alpha) and prostaglandin D2 (PGD2). {ECO:0000269|PubMed:20448048}. SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000269|PubMed:20448048}; Multi-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Specifically expressed in kidney where it is found in proximal convoluted tubules (at protein level). Colocalizes with the prostaglandin-inactivating enzyme HPGD in kidney (at protein level). Not detected in other tissues tested. {ECO:0000269|PubMed:20448048}. +A2AKQ0 S35D1_MOUSE UDP-glucuronic acid/UDP-N-acetylgalactosamine transporter (UDP-GlcA/UDP-GalNAc transporter) (Solute carrier family 35 member D1) 355 39,272 Alternative sequence (1); Chain (1); Sequence conflict (1); Transmembrane (8) TRANSMEM 39 59 Helical. {ECO:0000255}.; TRANSMEM 69 89 Helical. {ECO:0000255}.; TRANSMEM 157 177 Helical. {ECO:0000255}.; TRANSMEM 185 205 Helical. {ECO:0000255}.; TRANSMEM 217 237 Helical. {ECO:0000255}.; TRANSMEM 254 274 Helical. {ECO:0000255}.; TRANSMEM 281 303 Helical. {ECO:0000255}.; TRANSMEM 315 335 Helical. {ECO:0000255}. FUNCTION: Transports both UDP-glucuronic acid (UDP-GlcA) and UDP-N-acetylgalactosamine (UDP-GalNAc) from the cytoplasm into the endoplasmic reticulum lumen. Plays a role in chondroitin sulfate biosynthesis, which is important for formation of cartilage extracellular matrix and normal skeletal development. {ECO:0000269|PubMed:17952091}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:17952091}; Multi-pass membrane protein {ECO:0000255}. +Q8R2Z3 S26A7_MOUSE Anion exchange transporter (Solute carrier family 26 member 7) 656 71,829 Chain (1); Domain (1); Region (1); Sequence conflict (4); Topological domain (11); Transmembrane (11) TRANSMEM 76 96 Helical. {ECO:0000255}.; TRANSMEM 145 165 Helical. {ECO:0000255}.; TRANSMEM 167 187 Helical. {ECO:0000255}.; TRANSMEM 200 220 Helical. {ECO:0000255}.; TRANSMEM 223 243 Helical. {ECO:0000255}.; TRANSMEM 255 275 Helical. {ECO:0000255}.; TRANSMEM 307 327 Helical. {ECO:0000255}.; TRANSMEM 344 364 Helical. {ECO:0000255}.; TRANSMEM 384 404 Helical. {ECO:0000255}.; TRANSMEM 405 425 Helical. {ECO:0000255}.; TRANSMEM 449 469 Helical. {ECO:0000255}. TOPO_DOM 1 75 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 97 144 Extracellular. {ECO:0000255}.; TOPO_DOM 166 166 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 188 199 Extracellular. {ECO:0000255}.; TOPO_DOM 221 222 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 244 254 Extracellular. {ECO:0000255}.; TOPO_DOM 276 306 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 328 343 Extracellular. {ECO:0000255}.; TOPO_DOM 365 383 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 426 448 Extracellular. {ECO:0000255}.; TOPO_DOM 470 656 Cytoplasmic. {ECO:0000255}. FUNCTION: Acts as a sodium-independent DIDS-sensitive anion exchanger mediating bicarbonate, chloride, sulfate and oxalate transport. May play a role in the maintenance of the electrolyte and acid-base homeostasis in the kidney, by acting as a distal excretory segment-specific anion exchanger, specifically chloride. Plays a major role in gastric acid secretion. {ECO:0000250|UniProtKB:Q8TE54, ECO:0000269|PubMed:12736153, ECO:0000269|PubMed:15591059, ECO:0000269|PubMed:16263805}. SUBCELLULAR LOCATION: Basolateral cell membrane; Multi-pass membrane protein {ECO:0000269|PubMed:12736153, ECO:0000269|PubMed:16263805, ECO:0000269|PubMed:16524946}. Recycling endosome membrane; Multi-pass membrane protein {ECO:0000269|PubMed:12736153, ECO:0000269|PubMed:16263805, ECO:0000269|PubMed:16524946}. Note=Expressed on the basolateral membrane of acid-secreting gastric parietal cells, distal nephron segments and apical domains of proximal tubules and in the glomerulus. Expressed in the cytoplasm in recycling endosomes of kidney outer medullary collecting duct cells and in acid-secreting gastric parietal cells. Targeted to the basolateral membrane in hypertonicity and potassium depletion. {ECO:0000250|UniProtKB:Q8TE54, ECO:0000269|PubMed:12736153, ECO:0000269|PubMed:16263805, ECO:0000269|PubMed:16524946}. TISSUE SPECIFICITY: Abundantly expressed in parietal cells on the glandular portion of the stomach. Lower levels are observed in the kidney, with expression in the proximal tubule and thick ascending limb of the loop of Henle. Also expressed in distal segments of nephron, in extraglomerular mesagial cells and a subpopulation of intercalated cells of outer medullary collecting ducts. {ECO:0000269|PubMed:12736153, ECO:0000269|PubMed:16263805, ECO:0000269|PubMed:16524946}. +P62818 S10A3_MOUSE Protein S100-A3 (Protein S-100E) (S100 calcium-binding protein A3) 101 11,747 Calcium binding (2); Chain (1); Disulfide bond (1); Domain (2); Metal binding (4); Modified residue (1) FUNCTION: Binds both calcium and zinc. May be involved in calcium-dependent cuticle cell differentiation, hair shaft and hair cuticular barrier formation (By similarity). {ECO:0000250}. PTM: More than half of the arginine residues undergo citrullination by PAD1 and PAD2. Arg-51 is specifically citrullinated by PAD3 and promotes tetramerization (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homodimer and homotetramer for the citrullinated form. {ECO:0000250}. TISSUE SPECIFICITY: Skin specific, specifically expressed in cuticle of pelage follicle. {ECO:0000269|PubMed:9804353}. +Q7TML3 S35F2_MOUSE Solute carrier family 35 member F2 375 41,635 Chain (1); Modified residue (6); Sequence conflict (2); Transmembrane (10) TRANSMEM 39 59 Helical. {ECO:0000255}.; TRANSMEM 73 93 Helical. {ECO:0000255}.; TRANSMEM 108 126 Helical. {ECO:0000255}.; TRANSMEM 136 156 Helical. {ECO:0000255}.; TRANSMEM 165 185 Helical. {ECO:0000255}.; TRANSMEM 195 215 Helical. {ECO:0000255}.; TRANSMEM 227 247 Helical. {ECO:0000255}.; TRANSMEM 263 283 Helical. {ECO:0000255}.; TRANSMEM 290 310 Helical. {ECO:0000255}.; TRANSMEM 314 334 Helical. {ECO:0000255}. FUNCTION: Putative solute transporter. {ECO:0000305}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8BZK4 S35F4_MOUSE Solute carrier family 35 member F4 485 53,704 Alternative sequence (4); Chain (1); Domain (1); Sequence conflict (1); Transmembrane (10) TRANSMEM 129 149 Helical. {ECO:0000255}.; TRANSMEM 156 176 Helical. {ECO:0000255}.; TRANSMEM 217 234 Helical. {ECO:0000255}.; TRANSMEM 241 261 Helical. {ECO:0000255}.; TRANSMEM 265 285 Helical. {ECO:0000255}.; TRANSMEM 294 314 Helical. {ECO:0000255}.; TRANSMEM 329 349 Helical. {ECO:0000255}.; TRANSMEM 359 381 Helical. {ECO:0000255}.; TRANSMEM 383 405 Helical. {ECO:0000255}.; TRANSMEM 414 434 Helical. {ECO:0000255}. FUNCTION: Putative solute transporter. {ECO:0000305}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8R314 S35F5_MOUSE Solute carrier family 35 member F5 524 58,613 Chain (1); Compositional bias (1); Domain (1); Modified residue (1); Sequence conflict (1); Transmembrane (10) TRANSMEM 69 89 Helical. {ECO:0000255}.; TRANSMEM 101 121 Helical. {ECO:0000255}.; TRANSMEM 244 264 Helical. {ECO:0000255}.; TRANSMEM 269 289 Helical. {ECO:0000255}.; TRANSMEM 297 317 Helical. {ECO:0000255}.; TRANSMEM 328 348 Helical. {ECO:0000255}.; TRANSMEM 362 382 Helical. {ECO:0000255}.; TRANSMEM 396 416 Helical. {ECO:0000255}.; TRANSMEM 421 441 Helical. {ECO:0000255}.; TRANSMEM 453 473 Helical. {ECO:0000255}. FUNCTION: Putative solute transporter. {ECO:0000305}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8VE96 S35F6_MOUSE Solute carrier family 35 member F6 (ANT2-binding protein) (ANT2BP) (Transport and Golgi organization 9 homolog) 372 40,978 Chain (1); Domain (1); Frameshift (1); Glycosylation (1); Modified residue (1); Sequence conflict (2); Signal peptide (1); Transmembrane (9) TRANSMEM 48 68 Helical. {ECO:0000255}.; TRANSMEM 89 109 Helical. {ECO:0000255}.; TRANSMEM 116 136 Helical. {ECO:0000255}.; TRANSMEM 145 165 Helical. {ECO:0000255}.; TRANSMEM 176 196 Helical. {ECO:0000255}.; TRANSMEM 211 231 Helical. {ECO:0000255}.; TRANSMEM 261 281 Helical. {ECO:0000255}.; TRANSMEM 293 312 Helical. {ECO:0000255}.; TRANSMEM 320 336 Helical. {ECO:0000255}. FUNCTION: Involved in the maintenance of mitochondrial membrane potential in pancreatic ductal adenocarcinoma (PDAC) cells. Promotes pancreatic ductal adenocarcinoma (PDAC) cell growth. May play a role as a nucleotide-sugar transporter (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Lysosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with SLC25A5. {ECO:0000250}. +Q8K4D3 S36A1_MOUSE Proton-coupled amino acid transporter 1 (Proton/amino acid transporter 1) (Solute carrier family 36 member 1) 475 52,466 Chain (1); Disulfide bond (1); Glycosylation (3); Sequence conflict (2); Topological domain (12); Transmembrane (11) TRANSMEM 51 71 Helical. {ECO:0000255}.; TRANSMEM 78 98 Helical. {ECO:0000255}.; TRANSMEM 141 161 Helical. {ECO:0000255}.; TRANSMEM 190 210 Helical. {ECO:0000255}.; TRANSMEM 215 235 Helical. {ECO:0000255}.; TRANSMEM 257 277 Helical. {ECO:0000255}.; TRANSMEM 289 309 Helical. {ECO:0000255}.; TRANSMEM 342 362 Helical. {ECO:0000255}.; TRANSMEM 372 392 Helical. {ECO:0000255}.; TRANSMEM 397 417 Helical. {ECO:0000255}.; TRANSMEM 439 459 Helical. {ECO:0000255}. TOPO_DOM 1 50 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 72 77 Extracellular. {ECO:0000255}.; TOPO_DOM 99 140 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 162 189 Extracellular. {ECO:0000255}.; TOPO_DOM 211 214 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 236 256 Extracellular. {ECO:0000255}.; TOPO_DOM 278 288 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 310 341 Extracellular. {ECO:0000255}.; TOPO_DOM 363 371 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 393 396 Extracellular. {ECO:0000255}.; TOPO_DOM 418 438 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 460 475 Extracellular. {ECO:0000255}. FUNCTION: Neutral amino acid/proton symporter. Has a pH-dependent electrogenic transport activity for small amino acids such as glycine, alanine and proline. Besides small apolar L-amino acids, it also recognizes their D-enantiomers and selected amino acid derivatives such as gamma-aminobutyric acid. {ECO:0000269|PubMed:11959859}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q924A5}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:Q924A5}; Multi-pass membrane protein {ECO:0000255}. Note=In neurons, colocalizes with the exocyst complex in the axonal processes. {ECO:0000250|UniProtKB:Q924A5}. TISSUE SPECIFICITY: Highly expressed in small intestine, colon, kidney and brain. {ECO:0000269|PubMed:11959859}. +Q9ERH8 S28A3_MOUSE Solute carrier family 28 member 3 (Concentrative Na(+)-nucleoside cotransporter 3) (CNT 3) (mCNT3) 703 78,310 Chain (1); Sequence conflict (10); Topological domain (14); Transmembrane (13) TRANSMEM 120 140 Helical. {ECO:0000255}.; TRANSMEM 143 163 Helical. {ECO:0000255}.; TRANSMEM 186 206 Helical. {ECO:0000255}.; TRANSMEM 216 236 Helical. {ECO:0000255}.; TRANSMEM 239 259 Helical. {ECO:0000255}.; TRANSMEM 303 323 Helical. {ECO:0000255}.; TRANSMEM 330 350 Helical. {ECO:0000255}.; TRANSMEM 378 398 Helical. {ECO:0000255}.; TRANSMEM 404 424 Helical. {ECO:0000255}.; TRANSMEM 459 479 Helical. {ECO:0000255}.; TRANSMEM 494 514 Helical. {ECO:0000255}.; TRANSMEM 574 594 Helical. {ECO:0000255}.; TRANSMEM 609 629 Helical. {ECO:0000255}. TOPO_DOM 1 119 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 141 142 Extracellular. {ECO:0000255}.; TOPO_DOM 164 185 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 207 215 Extracellular. {ECO:0000255}.; TOPO_DOM 237 238 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 260 302 Extracellular. {ECO:0000255}.; TOPO_DOM 324 329 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 351 377 Extracellular. {ECO:0000255}.; TOPO_DOM 399 403 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 425 458 Extracellular. {ECO:0000255}.; TOPO_DOM 480 493 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 515 573 Extracellular. {ECO:0000255}.; TOPO_DOM 595 608 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 630 703 Extracellular. {ECO:0000255}. FUNCTION: Sodium-dependent, pyrimidine- and purine-selective. Involved in the homeostasis of endogenous nucleosides. Exhibits the transport characteristics of the nucleoside transport system cib or N3 subtype (N3/cib) (with marked transport of both thymidine and inosine). Employs a 2:1 sodium/nucleoside ratio. Also able to transport gemcitabine, 3'-azido-3'-deoxythymidine (AZT), ribavirin and 3-deazauridine (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q5I012 S38AA_MOUSE Putative sodium-coupled neutral amino acid transporter 10 (Solute carrier family 38 member 10) 1090 117,194 Alternative sequence (6); Chain (1); Erroneous initiation (1); Modified residue (5); Sequence conflict (1); Transmembrane (10) TRANSMEM 9 31 Helical. {ECO:0000255}.; TRANSMEM 36 58 Helical. {ECO:0000255}.; TRANSMEM 84 104 Helical. {ECO:0000255}.; TRANSMEM 123 143 Helical. {ECO:0000255}.; TRANSMEM 153 173 Helical. {ECO:0000255}.; TRANSMEM 229 249 Helical. {ECO:0000255}.; TRANSMEM 272 292 Helical. {ECO:0000255}.; TRANSMEM 323 343 Helical. {ECO:0000255}.; TRANSMEM 345 365 Helical. {ECO:0000255}.; TRANSMEM 378 398 Helical. {ECO:0000255}. FUNCTION: Putative sodium-dependent amino acid/proton antiporter. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8K2P7 S38A1_MOUSE Sodium-coupled neutral amino acid transporter 1 (Amino acid transporter A1) (MNat2) (N-system amino acid transporter 2) (Solute carrier family 38 member 1) (System A amino acid transporter 1) (System N amino acid transporter 1) 485 53,795 Alternative sequence (4); Chain (1); Disulfide bond (1); Glycosylation (2); Modified residue (8); Sequence conflict (4); Topological domain (12); Transmembrane (11) TRANSMEM 75 97 Helical. {ECO:0000255}.; TRANSMEM 113 133 Helical. {ECO:0000255}.; TRANSMEM 149 169 Helical. {ECO:0000255}.; TRANSMEM 189 211 Helical. {ECO:0000255}.; TRANSMEM 217 237 Helical. {ECO:0000255}.; TRANSMEM 274 294 Helical. {ECO:0000255}.; TRANSMEM 311 331 Helical. {ECO:0000255}.; TRANSMEM 349 369 Helical. {ECO:0000255}.; TRANSMEM 392 412 Helical. {ECO:0000255}.; TRANSMEM 415 435 Helical. {ECO:0000255}.; TRANSMEM 451 471 Helical. {ECO:0000255}. TOPO_DOM 1 74 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 98 112 Extracellular. {ECO:0000255}.; TOPO_DOM 134 148 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 170 188 Extracellular. {ECO:0000255}.; TOPO_DOM 212 216 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 238 273 Extracellular. {ECO:0000255}.; TOPO_DOM 295 310 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 332 348 Extracellular. {ECO:0000255}.; TOPO_DOM 370 391 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 413 414 Extracellular. {ECO:0000255}.; TOPO_DOM 436 450 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 472 485 Extracellular. {ECO:0000255}. FUNCTION: Functions as a sodium-dependent amino acid transporter. Mediates the saturable, pH-sensitive and electrogenic cotransport of glutamine and sodium ions with a stoichiometry of 1:1. May also transport small zwitterionic and aliphatic amino acids with a lower affinity. May supply glutamatergic and GABAergic neurons with glutamine which is required for the synthesis of the neurotransmitters glutamate and GABA. {ECO:0000269|PubMed:11325958}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Restricted to the somatodendritic compartment of neurons. Found in the cellular processes of neurons in the developing brain. {ECO:0000250}. TISSUE SPECIFICITY: Specifically expressed in brain and retina (at protein level). Also detected in spleen, small intestine and lung. {ECO:0000269|PubMed:11325958}. +Q3USY0 S38AB_MOUSE Putative sodium-coupled neutral amino acid transporter 11 (Solute carrier family 38 member 11) 453 49,615 Alternative sequence (2); Chain (1); Erroneous gene model prediction (2); Frameshift (1); Glycosylation (2); Transmembrane (11) TRANSMEM 39 59 Helical. {ECO:0000255}.; TRANSMEM 66 86 Helical. {ECO:0000255}.; TRANSMEM 106 126 Helical. {ECO:0000255}.; TRANSMEM 150 170 Helical. {ECO:0000255}.; TRANSMEM 179 199 Helical. {ECO:0000255}.; TRANSMEM 222 242 Helical. {ECO:0000255}.; TRANSMEM 262 282 Helical. {ECO:0000255}.; TRANSMEM 299 319 Helical. {ECO:0000255}.; TRANSMEM 337 357 Helical. {ECO:0000255}.; TRANSMEM 359 379 Helical. {ECO:0000255}.; TRANSMEM 398 418 Helical. {ECO:0000255}. FUNCTION: Putative sodium-dependent amino acid/proton antiporter. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8CFE6 S38A2_MOUSE Sodium-coupled neutral amino acid transporter 2 (Amino acid transporter A2) (Solute carrier family 38 member 2) (System A amino acid transporter 2) (System A transporter 1) (System N amino acid transporter 2) 504 55,503 Chain (1); Disulfide bond (1); Erroneous initiation (1); Glycosylation (2); Modified residue (4); Region (1); Sequence conflict (1); Topological domain (12); Transmembrane (11) TRANSMEM 77 97 Helical. {ECO:0000255}.; TRANSMEM 103 123 Helical. {ECO:0000255}.; TRANSMEM 159 179 Helical. {ECO:0000255}.; TRANSMEM 189 209 Helical. {ECO:0000255}.; TRANSMEM 218 238 Helical. {ECO:0000255}.; TRANSMEM 290 310 Helical. {ECO:0000255}.; TRANSMEM 327 347 Helical. {ECO:0000255}.; TRANSMEM 369 389 Helical. {ECO:0000255}.; TRANSMEM 411 431 Helical. {ECO:0000255}.; TRANSMEM 434 454 Helical. {ECO:0000255}.; TRANSMEM 472 492 Helical. {ECO:0000255}. TOPO_DOM 1 76 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 98 102 Extracellular. {ECO:0000255}.; TOPO_DOM 124 158 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 180 188 Extracellular. {ECO:0000255}.; TOPO_DOM 210 217 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 239 289 Extracellular. {ECO:0000255}.; TOPO_DOM 311 326 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 348 368 Extracellular. {ECO:0000255}.; TOPO_DOM 390 410 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 432 433 Extracellular. {ECO:0000255}.; TOPO_DOM 455 471 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 493 504 Extracellular. {ECO:0000255}. FUNCTION: Functions as a sodium-dependent amino acid transporter. Mediates the saturable, pH-sensitive and electrogenic cotransport of neutral amino acids and sodium ions with a stoichiometry of 1:1. May function in the transport of amino acids at the blood-brain barrier and in the supply of maternal nutrients to the fetus through the placenta. {ECO:0000269|PubMed:16365304}. PTM: Polyubiquitination by NEDD4L regulates the degradation and the activity of SLC38A2. {ECO:0000269|PubMed:17003038}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17003038, ECO:0000269|PubMed:17050538}; Multi-pass membrane protein {ECO:0000269|PubMed:17003038, ECO:0000269|PubMed:17050538}. Note=Insulin promotes recruitment to the plasma membrane from a pool localized in the trans-Golgi network or endosomes. Enriched in the somatodendritic compartment of neurons, it is also detected at the axonal shaft but excluded from the nerve terminal. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in cerebral and cerebellar astrocytes and neurons. {ECO:0000269|PubMed:12971909}. +Q5DTL9 S4A10_MOUSE Sodium-driven chloride bicarbonate exchanger (Solute carrier family 4 member 10) 1118 125,817 Alternative sequence (1); Chain (1); Erroneous initiation (1); Modified residue (5); Sequence conflict (5); Topological domain (13); Transmembrane (12) TRANSMEM 510 530 Helical. {ECO:0000255}.; TRANSMEM 539 559 Helical. {ECO:0000255}.; TRANSMEM 563 583 Helical. {ECO:0000255}.; TRANSMEM 597 617 Helical. {ECO:0000255}.; TRANSMEM 627 647 Helical. {ECO:0000255}.; TRANSMEM 721 741 Helical. {ECO:0000255}.; TRANSMEM 763 783 Helical. {ECO:0000255}.; TRANSMEM 810 830 Helical. {ECO:0000255}.; TRANSMEM 856 876 Helical. {ECO:0000255}.; TRANSMEM 913 933 Helical. {ECO:0000255}.; TRANSMEM 936 956 Helical. {ECO:0000255}.; TRANSMEM 999 1019 Helical. {ECO:0000255}. TOPO_DOM 1 509 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 531 538 Extracellular. {ECO:0000255}.; TOPO_DOM 560 562 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 584 596 Extracellular. {ECO:0000255}.; TOPO_DOM 618 626 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 648 720 Extracellular. {ECO:0000255}.; TOPO_DOM 742 762 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 784 809 Extracellular. {ECO:0000255}.; TOPO_DOM 831 855 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 877 912 Extracellular. {ECO:0000255}.; TOPO_DOM 934 935 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 957 998 Extracellular. {ECO:0000255}.; TOPO_DOM 1020 1118 Cytoplasmic. {ECO:0000255}. FUNCTION: Electrogenic sodium/bicarbonate cotransporter in exchange for intracellular chloride. Plays an important role in regulating intracellular pH. {ECO:0000269|PubMed:10993873}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14592810}; Multi-pass membrane protein {ECO:0000269|PubMed:14592810}. Note=Localizes to the basolateral membrane. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in pancreatic islets and in the brain, in the epithelial cells of the choroid plexus. {ECO:0000269|PubMed:10993873, ECO:0000269|PubMed:14592810}. +O88343 S4A4_MOUSE Electrogenic sodium bicarbonate cotransporter 1 (Sodium bicarbonate cotransporter) (Na(+)/HCO3(-) cotransporter) (Solute carrier family 4 member 4) 1079 121,484 Alternative sequence (4); Chain (1); Compositional bias (1); Disulfide bond (2); Glycosylation (2); Intramembrane (1); Modified residue (20); Region (5); Sequence conflict (16); Topological domain (14); Transmembrane (12) INTRAMEM 961 986 Discontinuously helical. {ECO:0000250|UniProtKB:Q9Y6R1}. TRANSMEM 467 491 Helical; Name=1. {ECO:0000250|UniProtKB:Q9Y6R1}.; TRANSMEM 502 520 Helical; Name=2. {ECO:0000250|UniProtKB:Q9Y6R1}.; TRANSMEM 522 542 Discontinuously helical; Name=3. {ECO:0000250|UniProtKB:Q9Y6R1}.; TRANSMEM 551 571 Helical; Name=4. {ECO:0000250|UniProtKB:Q9Y6R1}.; TRANSMEM 586 609 Helical; Name=5. {ECO:0000250|UniProtKB:Q9Y6R1}.; TRANSMEM 693 710 Helical; Name=6. {ECO:0000250|UniProtKB:Q9Y6R1}.; TRANSMEM 726 745 Helical; Name=7. {ECO:0000250|UniProtKB:Q9Y6R1}.; TRANSMEM 780 807 Helical; Name=8. {ECO:0000250|UniProtKB:Q9Y6R1}.; TRANSMEM 820 836 Helical; Name=9. {ECO:0000250|UniProtKB:Q9Y6R1}.; TRANSMEM 838 855 Discontinuously helical; Name=10. {ECO:0000250|UniProtKB:Q9Y6R1}.; TRANSMEM 878 894 Helical; Name=11. {ECO:0000250|UniProtKB:Q9Y6R1}.; TRANSMEM 902 918 Helical; Name=12. {ECO:0000250|UniProtKB:Q9Y6R1}. TOPO_DOM 1 466 Cytoplasmic. {ECO:0000250|UniProtKB:Q9Y6R1}.; TOPO_DOM 492 501 Extracellular. {ECO:0000250|UniProtKB:Q9Y6R1}.; TOPO_DOM 521 521 Cytoplasmic. {ECO:0000250|UniProtKB:Q9Y6R1}.; TOPO_DOM 543 550 Extracellular. {ECO:0000250|UniProtKB:Q9Y6R1}.; TOPO_DOM 572 585 Cytoplasmic. {ECO:0000250|UniProtKB:Q9Y6R1}.; TOPO_DOM 610 692 Extracellular. {ECO:0000250|UniProtKB:Q9Y6R1}.; TOPO_DOM 711 725 Cytoplasmic. {ECO:0000250|UniProtKB:Q9Y6R1}.; TOPO_DOM 746 779 Extracellular. {ECO:0000250|UniProtKB:Q9Y6R1}.; TOPO_DOM 808 819 Cytoplasmic. {ECO:0000250|UniProtKB:Q9Y6R1}.; TOPO_DOM 837 837 Extracellular. {ECO:0000250|UniProtKB:Q9Y6R1}.; TOPO_DOM 856 877 Cytoplasmic. {ECO:0000250|UniProtKB:Q9Y6R1}.; TOPO_DOM 895 901 Extracellular. {ECO:0000250|UniProtKB:Q9Y6R1}.; TOPO_DOM 919 960 Cytoplasmic. {ECO:0000250|UniProtKB:Q9Y6R1}.; TOPO_DOM 987 1079 Cytoplasmic. {ECO:0000250|UniProtKB:Q9Y6R1}. FUNCTION: Electrogenic sodium/bicarbonate cotransporter with a Na(+):HCO3(-) stoichiometry varying from 1:2 to 1:3. May regulate bicarbonate influx/efflux at the basolateral membrane of cells and regulate intracellular pH. {ECO:0000250|UniProtKB:Q9Y6R1, ECO:0000269|PubMed:19033647}.; FUNCTION: Isoform 2: May have a higher activity than isoform 1. {ECO:0000250|UniProtKB:Q9Y6R1}. PTM: Phosphorylation of Ser-1026 by PKA increases the binding of CA2 and changes the Na(+):HCO3(-) stoichiometry of the transporter from 3:1 to 2:1. Phosphorylated in presence of STK39 and dephosphorylated in presence of PP1 phosphatase; phosphorylation seems to inhibit SLC4A4 activity (PubMed:21317537). {ECO:0000250|UniProtKB:Q9Y6R1, ECO:0000269|PubMed:21317537}.; PTM: N-glycosylated. May not be necessary for the transporter basic functions. {ECO:0000269|PubMed:12604466}. SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000269|PubMed:11171615}; Multi-pass membrane protein {ECO:0000269|PubMed:11171615}. SUBUNIT: Homodimer (By similarity). Interacts with CA2/carbonic anhydrase 2 and CA4/carbonic anhydrase 4 which may regulate transporter activity (PubMed:14567693, PubMed:15218065). Isoform 1 but not isoform 2 interacts with AHCYL1 (via PEST domain when phosphorylated); the interaction increases SLC4A4 isoform 1 activity (PubMed:16769890, PubMed:19033647, PubMed:21317537). Interacts with AHCYL2 (By similarity). {ECO:0000250|UniProtKB:Q9GL77, ECO:0000250|UniProtKB:Q9Y6R1, ECO:0000269|PubMed:14567693, ECO:0000269|PubMed:15218065, ECO:0000269|PubMed:16769890, ECO:0000269|PubMed:19033647, ECO:0000269|PubMed:21317537}. TISSUE SPECIFICITY: Isoform 1 is specifically expressed in pancreatic ducts and acini (PubMed:19033647). Also expressed in parotid acinar cells and in the colonic crypts. {ECO:0000269|PubMed:11171615, ECO:0000269|PubMed:12388213, ECO:0000269|PubMed:12727194, ECO:0000269|PubMed:19033647, ECO:0000269|PubMed:9651366}. +Q80SW1 SAHH2_MOUSE S-adenosylhomocysteine hydrolase-like protein 1 (IP3R-binding protein released with inositol 1,4,5-trisphosphate) (Putative adenosylhomocysteinase 2) (S-adenosyl-L-homocysteine hydrolase 2) (AdoHcyase 2) 530 58,951 Binding site (7); Chain (1); Initiator methionine (1); Modified residue (9); Mutagenesis (5); Nucleotide binding (2); Region (3) FUNCTION: Multifaceted cellular regulator which coordinates several essential cellular functions including regulation of epithelial HCO3(-) and fluid secretion, mRNA processing and DNA replication. Regulates ITPR1 sensitivity to inositol 1,4,5-trisphosphate competing for the common binding site and acting as endogenous 'pseudoligand' whose inhibitory activity can be modulated by its phosphorylation status. In the pancreatic and salivary ducts, at resting state, attenuates inositol 1,4,5-trisphosphate-induced calcium release by interacting with ITPR1 (By similarity). When extracellular stimuli induce ITPR1 phosphorylation or inositol 1,4,5-trisphosphate production, dissociates of ITPR1 to interact with CFTR and SLC26A6 mediating their synergistic activation by calcium and cAMP that stimulates the epithelial secretion of electrolytes and fluid (PubMed:12525476, PubMed:23542070). Also activates basolateral SLC4A4 isoform 1 to coordinate fluid and HCO3(-) secretion (PubMed:19224921). Inhibits the effect of STK39 on SLC4A4 and CFTR by recruiting PP1 phosphatase which activates SLC4A4, SLC26A6 and CFTR through dephosphorylation (PubMed:19033647, PubMed:21317537). Mediates the induction of SLC9A3 surface expression produced by Angiotensin-2. Depending on the cell type, activates SLC9A3 in response to calcium or reverses SLC9A3R2-dependent calcium inhibition. May modulate the polyadenylation state of specific mRNAs, both by controlling the subcellular location of FIP1L1 and by inhibiting PAPOLA activity, in response to a stimulus that alters its phosphorylation state. Acts as a (dATP)-dependent inhibitor of ribonucleotide reductase large subunit RRM1, controlling the endogenous dNTP pool and ensuring normal cell cycle progression (By similarity). In vitro does not exhibit any S-adenosyl-L-homocysteine hydrolase activity (PubMed:12525476). {ECO:0000250|UniProtKB:B5DFN2, ECO:0000250|UniProtKB:O43865, ECO:0000269|PubMed:12525476, ECO:0000269|PubMed:16769890, ECO:0000269|PubMed:19033647, ECO:0000269|PubMed:19224921, ECO:0000269|PubMed:21317537, ECO:0000269|PubMed:23542070}. PTM: Phosphorylated at Ser/Thr residues between Ser-68 and Thr-72 in the PEST region: required for interaction with dATP-bound RRM1 and ITPR1. Phosphorylation at Ser-68 by PRKD1 and CAMK4 is required for further phosphorylations by CSNK1A1. Phosphorylation is induced by oxidative stress. Probably phosphorylated by CAMK2A; phosphorylation at Ser-68 may be required for interaction with SLC9A3. {ECO:0000250|UniProtKB:O43865}. SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:16527252}. Cytoplasm, cytosol {ECO:0000269|PubMed:19220705}. Microsome {ECO:0000269|PubMed:19220705}. Apical cell membrane {ECO:0000250|UniProtKB:B5DFN2}. Note=Associates with membranes when phosphorylated, probably through interaction with ITPR1. {ECO:0000269|PubMed:19220705}. SUBUNIT: Forms multimers (By similarity). Forms heteromultimers with AHCYL2 (via the C-terminal region) (PubMed:19220705). Interacts (when phosphorylated) with ITPR1 (when not phosphorylated); the interaction suppresses inositol 1,4,5-trisphosphate binding to ITPR1 (PubMed:23542070). Interacts with CFTR and SLC26A6; the interactions take place once AHCYL1 is released from ITPR1 and increase CFTR and SLC26A6 activities (PubMed:19033647, PubMed:21317537, PubMed:23542070). Interacts with RRM1; in a phosphorylation- and (dATP)-dependent manner. Interacts (via PEST domain when phosphorylated) with SLC4A4 isoform 1 but not isoform 2; the interaction increases SLC4A4 isoform 1 activity (PubMed:16769890, PubMed:19033647, PubMed:21317537). Interacts (when phosphorylated) with SLC9A3; the interaction is required for SLC9A3 apical location and activity (PubMed:19224921). Interacts (when phosphorylated) with FIP1L1; the interaction is direct and associates AHCYL1 with the CPSF complex and RNA Interacts with PAPOLA (By similarity). {ECO:0000250|UniProtKB:O43865, ECO:0000269|PubMed:12525476, ECO:0000269|PubMed:16527252, ECO:0000269|PubMed:16769890, ECO:0000269|PubMed:19033647, ECO:0000269|PubMed:19220705, ECO:0000269|PubMed:19224921, ECO:0000269|PubMed:21317537, ECO:0000269|PubMed:23542070}. DOMAIN: The PEST region is essential for the interaction with ITPR1, and, when phosphorylated, is also the RRM1-binding region. The PDZ-binding region is required for maximal interaction with ITPR1 and is also responsible for the IP3-insensitive interaction with ITPR1. {ECO:0000250|UniProtKB:O43865, ECO:0000269|PubMed:12525476}. TISSUE SPECIFICITY: Widely expressed (at protein level). Expressed in the lateral and luminal poles of the pancreatic duct (at protein level). {ECO:0000269|PubMed:12525476, ECO:0000269|PubMed:19033647, ECO:0000269|PubMed:19220705}. +Q80XQ2 TBCD5_MOUSE TBC1 domain family member 5 815 91,837 Chain (1); Compositional bias (1); Domain (1); Modified residue (11); Motif (2); Region (2); Sequence conflict (1); Site (2) FUNCTION: May act as a GTPase-activating protein for Rab family protein(s). May act as a GAP for RAB7A. Can displace RAB7A and retromer CSC subcomplex from the endosomal membrane to the cytosol; at least retromer displacement seems to require its catalytic activity. Required for retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN); the function seems to require its catalytic activity. Involved in regulation of autophagy. May act as a molecular switch between endosomal and autophagosomal transport and is involved in reprogramming vesicle trafficking upon autophagy induction. Involved in the trafficking of ATG9A upon activation of autophagy. May regulate the recruitment of ATG9A-AP2-containing vesicles to autophagic membranes (By similarity). {ECO:0000250|UniProtKB:Q92609}. SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250|UniProtKB:Q92609}. Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:Q92609}. Note=During starvation induced autophagy is relocalized from endosomal localization to LC3-positive autophagosomes (By similarity). {ECO:0000250|UniProtKB:Q92609}. SUBUNIT: Interacts with MAP1LC3A, MAP1LC3B, MAP1LC3C, GABARAP, GABARAPL1, GABARAPL2. Interacts with VPS29 and VPS35; indicative for an association with retromer CSC subcomplex. MAP1LC3A and VPS29 compete for binding to TBC1D5. Interacts with AP2M1; indicative for an association with the AP2 complex. Interacts with ULK1 and ATG13 (phosphorylated); indicative for an association with the activated ULK1-ATG13-FIP200 complex. Interacts with ATG9A; the interactions seems to be restricted to the AP2-clathrin-associated fraction of ATG9A. {ECO:0000250|UniProtKB:Q92609}. DOMAIN: The arginine and glutamine fingers are critical for the GTPase-activating mechanism, they pull out Rab's 'switch 2' glutamine and insert in Rab's active site. {ECO:0000250|UniProtKB:Q96BZ9}.; DOMAIN: The LIR (LC3-interacting region) motif mediates the interaction with ATG8 family proteins. LIR 1 is also implicated in interaction with retromer; LIR 2 is only implicated in interaction with ATG8 family proteins. {ECO:0000250|UniProtKB:Q92609}. +Q8BG16 S6A15_MOUSE Sodium-dependent neutral amino acid transporter B(0)AT2 (Sodium- and chloride-dependent neurotransmitter transporter NTT73) (Solute carrier family 6 member 15) (Transporter v7-3) 729 81,792 Chain (1); Glycosylation (4); Modified residue (5); Topological domain (4); Transmembrane (12) TRANSMEM 70 90 Helical; Name=1. {ECO:0000255}.; TRANSMEM 98 117 Helical; Name=2. {ECO:0000255}.; TRANSMEM 142 162 Helical; Name=3. {ECO:0000255}.; TRANSMEM 226 244 Helical; Name=4. {ECO:0000255}.; TRANSMEM 253 270 Helical; Name=5. {ECO:0000255}.; TRANSMEM 306 323 Helical; Name=6. {ECO:0000255}.; TRANSMEM 335 356 Helical; Name=7. {ECO:0000255}.; TRANSMEM 453 472 Helical; Name=8. {ECO:0000255}.; TRANSMEM 496 514 Helical; Name=9. {ECO:0000255}.; TRANSMEM 530 550 Helical; Name=10. {ECO:0000255}.; TRANSMEM 571 592 Helical; Name=11. {ECO:0000255}.; TRANSMEM 620 642 Helical; Name=12. {ECO:0000255}. TOPO_DOM 1 69 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 163 225 Extracellular. {ECO:0000255}.; TOPO_DOM 357 452 Extracellular. {ECO:0000255}.; TOPO_DOM 643 729 Cytoplasmic. {ECO:0000255}. FUNCTION: Functions as a sodium-dependent neutral amino acid transporter. Exhibits preference for methionine and for the branched-chain amino acids, particularly leucine, valine and isoleucine. Mediates the saturable, pH-sensitive and electrogenic cotransport of proline and sodium ions with a stoichiometry of 1:1. May have a role as transporter for neurotransmitter precursors into neurons. In contrast to other members of the neurotransmitter transporter family, does not appear to be chloride-dependent (By similarity). {ECO:0000250, ECO:0000269|PubMed:16185194}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Significant expressed in brain, lung and kidney. regions, the cortex, the cerebellum and the brain stem. {ECO:0000269|PubMed:16185194}. +Q8BM85 TBCK_MOUSE TBC domain-containing protein kinase-like protein 762 86,371 Alternative sequence (2); Chain (1); Domain (2); Erroneous initiation (1) FUNCTION: Involved in the modulation of mTOR signaling and expression of mTOR complex components. Involved in the regulation of cell proliferation and growth. Involved in the control of actin-cytoskeleton organization. {ECO:0000250|UniProtKB:Q8TEA7}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8TEA7}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q8TEA7}. Midbody {ECO:0000250|UniProtKB:Q8TEA7}. Note=Mainly localized in the cytoplasm during interphase. During metaphase, TBCK accumulates at the mitotic spindle. At the end of mitosis, it is detected at the midbody. {ECO:0000250|UniProtKB:Q8TEA7}. DOMAIN: The protein kinase domain is predicted to be catalytically inactive. {ECO:0000255}. +B1AVH7 TBD2A_MOUSE TBC1 domain family member 2A 922 104,260 Alternative sequence (1); Chain (1); Coiled coil (4); Compositional bias (1); Domain (2); Modified residue (1); Region (2); Sequence conflict (7) FUNCTION: Acts as GTPase-activating protein for RAB7A. Signal effector acting as a linker between RAC1 and RAB7A, leading to RAB7A inactivation and subsequent inhibition of cadherin degradation and reduced cell-cell adhesion (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Cell junction {ECO:0000250}. SUBUNIT: Interacts with activated RAC1 and CDH1. +Q9CY86 SAPC1_MOUSE Suppressor APC domain-containing protein 1 (Protein G7d) 146 16,181 Chain (1); Sequence conflict (1) +P36536 SAR1A_MOUSE GTP-binding protein SAR1a 198 22,371 Chain (1); Modified residue (1); Nucleotide binding (3) FUNCTION: Involved in transport from the endoplasmic reticulum to the Golgi apparatus. Required to maintain SEC16A localization at discrete locations on the ER membrane perhaps by preventing its dissociation. SAR1A-GTP-dependent assembly of SEC16A on the ER membrane forms an organized scaffold defining endoplasmic reticulum exit sites (ERES) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250}. Golgi apparatus {ECO:0000250}. SUBUNIT: Interacts with B3GAT1. {ECO:0000250|UniProtKB:Q9NR31}. TISSUE SPECIFICITY: Expressed in most tissues including liver, heart, brain, skeletal muscle and kidney. +Q8BXK4 SAMTR_MOUSE S-adenosylmethionine sensor upstream of mTORC1 (Probable methyltransferase BMT2 homolog) (EC 2.1.1.-) 403 45,952 Binding site (2); Chain (1); Frameshift (1) FUNCTION: S-adenosyl-L-methionine-binding protein that acts as an inhibitor of mTORC1 signaling via interaction with the GATOR1 and KICSTOR complexes. Acts as a sensor of S-adenosyl-L-methionine to signal methionine sufficiency to mTORC1: in presence of methionine, binds S-adenosyl-L-methionine, leading to disrupt interaction with the GATOR1 and KICSTOR complexes and promote mTORC1 signaling. Upon methionine starvation, S-adenosyl-L-methionine levels are reduced, thereby promoting the association with GATOR1 and KICSTOR, leading to inhibit mTORC1 signaling. Probably also acts as a S-adenosyl-L-methionine-dependent methyltransferase. {ECO:0000255|HAMAP-Rule:MF_03044}. SUBUNIT: Interacts with the GATOR1 complex; interaction is disrupted when BMT2/SAMTOR binds S-adenosyl-L-methionine. Interacts with the KICSTOR complex; interaction is disrupted when BMT2/SAMTOR binds S-adenosyl-L-methionine. {ECO:0000255|HAMAP-Rule:MF_03044}. +Q8C4H2 SAMD3_MOUSE Sterile alpha motif domain-containing protein 3 (SAM domain-containing protein 3) 520 60,419 Alternative sequence (2); Chain (1); Domain (1); Erroneous initiation (1) +Q8R197 SAST_MOUSE S-acyl fatty acid synthase thioesterase, medium chain (EC 3.1.2.14) (Oleoyl-ACP hydrolase) (Thioesterase II) (Thioesterase domain-containing protein 1) 265 30,250 Active site (2); Chain (1); Modified residue (1) FUNCTION: Contributes to the release of free fatty acids from fatty acid synthase (FASN). Has broad substrate specificity, giving rise to a range of free fatty acids with chain lengths between 10 and 16 carbon atoms (C10 - C16). {ECO:0000250|UniProtKB:Q9NV23}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P08635}. SUBUNIT: Interacts (via C-terminus) with FASN. {ECO:0000250|UniProtKB:P08635}. +P0DP59 SLUR2_MOUSE Secreted Ly-6/uPAR domain-containing protein 2 (SLURP-2) 97 10,452 Chain (1); Disulfide bond (5); Domain (1); Signal peptide (1) FUNCTION: Binds and may modulate the functional properties of nicotinic and muscarinic acetylcholine receptors. May regulate keratinocytes proliferation, differentiation and apoptosis. In vitro moderately inhibits ACh-evoked currents of alpha-3:beta-2-containing nAChRs, strongly these of alpha-4:beta-2-containing nAChRs, modulates alpha-7-containing nAChRs, and inhibits nicotine-induced signaling probably implicating alpha-3:beta-4-containing nAChRs. Proposed to act on alpha-3:beta-2 and alpha-7 nAChRs in an orthosteric, and on mAChRs, such as CHRM1 and CHRM3, in an allosteric manner. {ECO:0000250|UniProtKB:P0DP57}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P0DP57}. SUBUNIT: Interacts with CHRNA3, CHRNA4, CHRNA5, CHRNA7, CHRNB2 and CHRNB4. Interacts with CHRM1 and CHRM3 probably in an allosteric manner (By similarity). {ECO:0000250|UniProtKB:P0DP57}. TISSUE SPECIFICITY: Widely expressed, including in dendritic cells, macrophages, B- and T-lymphocytes. {ECO:0000269|PubMed:17286989}. +Q920F6 SMC1B_MOUSE Structural maintenance of chromosomes protein 1B (SMC protein 1B) (SMC-1-beta) (SMC-1B) 1248 144,513 Chain (1); Coiled coil (2); Compositional bias (1); Domain (1); Modified residue (3); Nucleotide binding (1) FUNCTION: Meiosis-specific component of cohesin complex. Required for the maintenance of meiotic cohesion, but not, or only to a minor extent, for its establishment. Contributes to axial element (AE) formation and the organization of chromatin loops along the AE. Plays a key role in synapsis, recombination and chromosome movements. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The meiosis-specific cohesin complex probably replaces mitosis specific cohesin complex when it dissociates from chromatin during prophase I. {ECO:0000269|PubMed:11564881, ECO:0000269|PubMed:15146193}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11564881}. Chromosome {ECO:0000269|PubMed:11564881, ECO:0000269|PubMed:24287868}. Chromosome, centromere {ECO:0000269|PubMed:11564881}. Note=Associates with chromatin. In prophase I stage of meiosis, localizes along the AE of synaptonemal complexes. In late-pachytene-diplotene, the bulk of protein dissociates from the chromosome arms probably because of phosphorylation by PLK, except at centromeres, where cohesin complexes remain. Remains chromatin associated at the centromeres up to metaphase II. At anaphase II, dissociates from centromeres, allowing chromosomes segregation. {ECO:0000269|PubMed:11564881}. SUBUNIT: Forms a heterodimer with SMC3. Component of a meiosis-specific cohesin complex, probably composed of the SMC1B and SMC3 heterodimer attached via their SMC hinge domain, RAD21 (or its meiosis-specific related protein REC8), which link them, and STAG3, which interacts with RAD21 or REC8. {ECO:0000269|PubMed:11564881}. DOMAIN: The flexible SMC hinge domain, which separates the large intramolecular coiled coil regions, allows the heterotypic interaction with the corresponding domain of SMC3, forming a V-shaped heterodimer. The two heads of the heterodimer are then connected by different ends of the cleavable RAD21 or REC8 protein, forming a ring structure (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Spermatocytes (at protein level). Testis and ovary specific. Not expressed in somatic cells. {ECO:0000269|PubMed:11564881, ECO:0000269|PubMed:24287868}. +Q8CG48 SMC2_MOUSE Structural maintenance of chromosomes protein 2 (SMC protein 2) (SMC-2) (Chromosome-associated protein E) (FGF-inducible protein 16) (XCAP-E homolog) 1191 134,239 Beta strand (7); Chain (1); Coiled coil (3); Compositional bias (1); Domain (1); Erroneous initiation (1); Helix (11); Modified residue (5); Nucleotide binding (1); Sequence conflict (1); Turn (2) FUNCTION: Central component of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Chromosome {ECO:0000250}. Note=In interphase cells, the majority of the condensin complex is found in the cytoplasm, while a minority of the complex is associated with chromatin. A subpopulation of the complex however remains associated with chromosome foci in interphase cells. During mitosis, most of the condensin complex is associated with the chromatin. At the onset of prophase, the regulatory subunits of the complex are phosphorylated by CDC2, leading to condensin's association with chromosome arms and to chromosome condensation. Dissociation from chromosomes is observed in late telophase (By similarity). {ECO:0000250}. SUBUNIT: Forms a heterodimer with SMC4. Component of the condensin complex, which contains the SMC2 and SMC4 heterodimer, and three non SMC subunits that probably regulate the complex: BRRN1/CAPH, CNAP1/CAPD2 and CAPG (By similarity). {ECO:0000250}. DOMAIN: The SMC hinge domain, which separates the large intramolecular coiled coil regions, allows the heterodimerization with SMC4, forming a V-shaped heterodimer. {ECO:0000250}. +Q9CW03 SMC3_MOUSE Structural maintenance of chromosomes protein 3 (SMC protein 3) (SMC-3) (Basement membrane-associated chondroitin proteoglycan) (Bamacan) (Chondroitin sulfate proteoglycan 6) (Chromosome segregation protein SmcD) (Mad member-interacting protein 1) 1217 141,556 Beta strand (8); Chain (1); Coiled coil (4); Compositional bias (1); Domain (1); Frameshift (1); Helix (13); Modified residue (12); Mutagenesis (1); Nucleotide binding (1); Sequence conflict (2); Turn (2) FUNCTION: Central component of cohesin, a complex required for chromosome cohesion during the cell cycle. The cohesin complex may form a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. Cohesion is coupled to DNA replication and is involved in DNA repair. The cohesin complex plays also an important role in spindle pole assembly during mitosis and in chromosomes movement. {ECO:0000269|PubMed:10375619}. PTM: Phosphorylated at Ser-1083 in a SPO11-dependent manner. {ECO:0000269|PubMed:15378723, ECO:0000269|PubMed:22346761}.; PTM: Acetylation at Lys-105 and Lys-106 by ESCO1 is important for genome stability and S phase sister chromatid cohesion. Regulated by DSCC1, it is required for processive DNA synthesis, coupling sister chromatid cohesion establishment during S phase to DNA replication (By similarity). Deacetylation by HDAC8, regulates release of the cohesin complex from chromatin (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22346761}. Chromosome {ECO:0000269|PubMed:22346761, ECO:0000269|PubMed:24287868}. Chromosome, centromere {ECO:0000269|PubMed:22346761}. Note=Associates with chromatin. Before prophase it is scattered along chromosome arms. During prophase, most of cohesin complexes dissociate from chromatin probably because of phosphorylation by PLK, except at centromeres, where cohesin complexes remain. At anaphase, the RAD21 subunit of the cohesin complex is cleaved, leading to the dissociation of the complex from chromosomes, allowing chromosome separation. The phosphorylated form at Ser-1083 is preferentially associated with unsynapsed chromosomal regions. SUBUNIT: Forms a heterodimer with SMC1A or SMC1B in cohesin complexes (PubMed:11564881). Cohesin complexes are composed of the SMC1 (SMC1A or SMC1B) and SMC3 heterodimer attached via their SMC hinge domain, RAD21 which link them, and one STAG protein (STAG1, STAG2 or STAG3), which interacts with RAD21. Also found in meiosis-specific cohesin complexes. Found in a complex with SMC1A, CDCA5 and RAD21, PDS5A/SCC-112 and PDS5B/APRIN. Interacts with PDS5A and WAPL; regulated by SMC3 acetylation. Interacts with NUMA1, and forms a ternary complex with KIF3B and KIFAP3, suggesting a function in tethering the chromosomes to the spindle pole and a function in chromosome movement. Interacts with SYCP2 and RPGR. Interacts (via SMC hinge domain) with KIAA1328 (via N- and C-terminal domains). Interacts with DDX11. Found in a cohesin complex with SMC1A, STAG1 and RAD21. The SMC1A-SMC3 heterodimer interacts with the NIPBL-MAU2 heterodimer (By similarity). Interacts with MXI1, MXD3 and MXD4 (PubMed:9528857). Interacts with STAG3 (PubMed:11483963). {ECO:0000250|UniProtKB:P97690, ECO:0000250|UniProtKB:Q9UQE7, ECO:0000269|PubMed:11483963, ECO:0000269|PubMed:11564881, ECO:0000269|PubMed:9528857}. DOMAIN: The flexible SMC hinge domain, which separates the large intramolecular coiled coil regions, allows the heterotypic interaction with the corresponding domain of SMC1A or SMC1B, forming a V-shaped heterodimer. The two heads of the heterodimer are then connected by different ends of the cleavable RAD21 protein, forming a ring structure (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Spermatocytes (at protein level). Widely expressed, with higher expression in testis and brain. {ECO:0000269|PubMed:10358101, ECO:0000269|PubMed:24287868}. +Q925E1 SNTG1_MOUSE Gamma-1-syntrophin (G1SYN) (Syntrophin-4) (SYN4) 517 57,982 Alternative sequence (2); Chain (1); Domain (2) FUNCTION: Adapter protein that binds to and probably organizes the subcellular localization of a variety of proteins. May link various receptors to the actin cytoskeleton and the dystrophin glycoprotein complex. May participate in regulating the subcellular location of diacylglycerol kinase-zeta to ensure that diacylglycerol is rapidly inactivated following receptor activation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Nucleus {ECO:0000250}. Note=Mainly cytoplasmic and weakly nuclear. {ECO:0000250}. SUBUNIT: Interacts with the dystrophin protein DMD and related proteins DTNA and DTNB. Interacts with DGKZ (By similarity). {ECO:0000250}. DOMAIN: The PDZ domain binds to the last three or four amino acids of DGKZ. The association with dystrophin or related proteins probably leaves the PDZ domain available to recruit proteins to the membrane (By similarity). {ECO:0000250}. +P62849 RS24_MOUSE 40S ribosomal protein S24 133 15,423 Alternative sequence (2); Chain (1); Cross-link (1); Modified residue (2) FUNCTION: Required for processing of pre-rRNA and maturation of 40S ribosomal subunits. {ECO:0000250}. +B5KM66 SYCE3_MOUSE Synaptonemal complex central element protein 3 (Testis-specific expressed protein 2) (TSEG-2) 88 10,467 Chain (1); Coiled coil (1); Helix (2) FUNCTION: Major component of the transverse central element of synaptonemal complexes (SCS), formed between homologous chromosomes during meiotic prophase. Required for chromosome loading of the central element-specific SCS proteins, and for initiating synapsis between homologous chromosomes. Chromosome loading appears to require SYCP1. Required for fertility. May play a role in apoptosis of spermatogenic cells and pathogenesis of cryptorchidism. {ECO:0000269|PubMed:20407872, ECO:0000269|PubMed:21637789}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21637789}. Chromosome {ECO:0000269|PubMed:21637789}. Note=Colocalizes with SYCE1 in the central elements. {ECO:0000269|PubMed:21637789}. SUBUNIT: Homodimer (PubMed:25394919). Interacts with SYCE1 (PubMed:21637789, PubMed:25394919). Interacts with SYCE2 (PubMed:21637789). {ECO:0000269|PubMed:21637789, ECO:0000269|PubMed:25394919}. TISSUE SPECIFICITY: Expression is restricted to spermatocytes and is absent in spermatogonia, spermatids and spermatogonia (at protein level). Expressed in adult testis and embryonic ovary. Expressed in the convoluted seminiferous tubules in spermatogonia and spermatocytes. {ECO:0000269|PubMed:20407872, ECO:0000269|PubMed:21637789}. +P62274 RS29_MOUSE 40S ribosomal protein S29 56 6,677 Chain (1); Metal binding (4); Modified residue (3) SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P62273}. Cytoplasm {ECO:0000250|UniProtKB:P62273}. Rough endoplasmic reticulum {ECO:0000250|UniProtKB:Q6QAP6}. Note=Detected on cytosolic polysomes (By similarity). Detected in ribosomes that are associated with the rough endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:P62273, ECO:0000250|UniProtKB:Q6QAP6}. SUBUNIT: Component of the 40S small ribosomal subunit. {ECO:0000250|UniProtKB:Q6QAP6}. +Q8VIG3 RSPH1_MOUSE Radial spoke head 1 homolog (Male meiotic metaphase chromosome-associated acidic protein) (Meichroacidin) (Testis-specific gene A2 protein) 301 34,181 Chain (1); Compositional bias (1); Frameshift (1); Repeat (6); Sequence conflict (1) FUNCTION: The specific expression during male germ cell development and its characteristic localization suggest that it may play an important role in male meiosis. It is necessary for proper building of the axonemal central pair and radial spokes (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Chromosome. Cell projection, cilium {ECO:0000250}. Note=Cytoplasmic in late spermatocytes, secondary spermatocytes and round spermatids. Gathered around metaphase chromosomes during meiotic divisions. TISSUE SPECIFICITY: Germ cell specific. Specifically expressed in testis, and to a lower extent in ovary. Not expressed in somatic tissues. +P32921 SYWC_MOUSE Tryptophan--tRNA ligase, cytoplasmic (EC 6.1.1.2) (Tryptophanyl-tRNA synthetase) (TrpRS) [Cleaved into: T1-TrpRS; T2-TrpRS] 481 54,358 Alternative sequence (1); Chain (3); Domain (1); Modified residue (2); Motif (2); Sequence conflict (8) FUNCTION: T1-TrpRS has aminoacylation activity while T2-TrpRS lacks it. T1-TrpRS and T2-TrpRS possess angiostatic activity. T2-TrpRS inhibits fluid shear stress-activated responses of endothelial cells. Regulates ERK, Akt, and eNOS activation pathways that are associated with angiogenesis, cytoskeletal reorganization and shear stress-responsive gene expression (By similarity). {ECO:0000250|UniProtKB:P23381}. PTM: Proteolytic cleavage generates 2 forms; T1-TrpRS and T2-TrpRS. {ECO:0000250|UniProtKB:P23381}. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Homodimer (By similarity). Interacts with oxidized form of GAPDH (By similarity). {ECO:0000250|UniProtKB:P23381}. TISSUE SPECIFICITY: Isoform 2 is widely expressed, isoform 1 is found only in embryonic stem cells. +Q14AI6 RUSD3_MOUSE Mitochondrial mRNA pseudouridine synthase Rpusd3 (EC 5.4.99.-) (RNA pseudouridylate synthase domain-containing protein 3) 344 38,076 Alternative sequence (1); Chain (1); Frameshift (1); Sequence conflict (1); Transit peptide (1) FUNCTION: Catalyzes uridine to pseudouridine isomerization (pseudouridylation) of specific mitochondrial mRNAs (mt-mRNAs), a post-transcriptional modification necessary for their translation. Acts at position 390 in COXI mt-mRNA and at position 697-699 in mitochondrial COXIII mt-mRNA. As a component of a functional protein-RNA module, consisting of RCC1L, NGRN, RPUSD3, RPUSD4, TRUB2, FASTKD2 and 16S mitochondrial ribosomal RNA (16S mt-rRNA), controls 16S mt-rRNA abundance and may play a role in mitochondrial ribosome biogenesis. {ECO:0000250|UniProtKB:Q6P087}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:Q6P087}. Note=Localizes to mitochondrial RNA granules, platforms for post-transcriptional RNA modification and ribosome assembly. {ECO:0000250|UniProtKB:Q6P087}. SUBUNIT: Forms a regulatory protein-RNA complex, consisting of RCC1L, NGRN, RPUSD3, RPUSD4, TRUB2, FASTKD2 and 16S mt-rRNA. {ECO:0000250|UniProtKB:Q6P087}. +Q64336 TBR1_MOUSE T-box brain protein 1 (T-brain-1) (TBR-1) (TES-56) 681 73,940 Chain (1); Compositional bias (1); DNA binding (1); Modified residue (4); Sequence conflict (1) FUNCTION: Probable transcriptional regulator involved in developmental processes. Required for normal brain development. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00201}. SUBUNIT: Part of a complex containing CASK, TBR1 and TSPYL2; may modulate gene expression in response to neuronal synaptic activity. {ECO:0000269|PubMed:15066269}. TISSUE SPECIFICITY: Expressed in specific lamina in the developing and adult brain. +Q80UK7 SAS6_MOUSE Spindle assembly abnormal protein 6 homolog 654 74,054 Alternative sequence (2); Chain (1); Coiled coil (1); Domain (1); Modified residue (3); Sequence conflict (3) FUNCTION: Central scaffolding component of the centrioles ensuring their 9-fold symmetry. Required for centrosome biogenesis and duplication: required both for mother-centriole-dependent centriole duplication and deuterosome-dependent centriole amplification in multiciliated cells (PubMed:24240477). Required for the recruitment of STIL to the procentriole and for STIL-mediated centriole amplification (By similarity). {ECO:0000250|UniProtKB:Q6UVJ0, ECO:0000269|PubMed:24240477}. PTM: Ubiquitinated by the SCF(FBXW5) E3 ubiquitin-protein ligase complex during S phase, leading to its degradation and preventing centriole reduplication. {ECO:0000250|UniProtKB:Q6UVJ0}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q6UVJ0}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:24240477}. Note=Component of the centrosome. Associated only transiently with nascent procentrioles during centriole biogenesis (By similarity). Component of the deuterosome, a structure that promotes de novo centriole amplification in multiciliated cells that can generate more than 100 centrioles (PubMed:24240477). {ECO:0000250|UniProtKB:Q6UVJ0, ECO:0000269|PubMed:24240477}. SUBUNIT: Nine homodimers form a cartwheel structure with an internal diameter of 23 nM and radial spokes connecting to the microtubule triplets. Interacts with FBXW5. Forms a complex with CENPJ and STIL. Interacts with NUP62 and TUBG1 at the centrosome. {ECO:0000250|UniProtKB:Q6UVJ0, ECO:0000250|UniProtKB:Q7ZVT3}. DOMAIN: The 35 nM long coiled-coil domain mediates homodimerization while the globular N-terminus links the dimers at an angle of 40 degrees to form the inner ring. {ECO:0000250|UniProtKB:Q7ZVT3}. +Q810F8 TBX10_MOUSE T-box transcription factor TBX10 (T-box protein 10) (MmTBX7) (T-box protein 13) 385 42,407 Alternative sequence (1); Chain (1); DNA binding (1); Sequence conflict (2) FUNCTION: Probable transcriptional regulator involved in developmental processes. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00201}. DISEASE: Note=Defects in Tbx10 are the cause of a cleft lip and palate (CL/P) phenotype called Dancer (Dc). The defect is caused by a gain of function. {ECO:0000269|PubMed:15118109}. +Q99ME7 TBX19_MOUSE T-box transcription factor TBX19 (T-box protein 19) (T-box factor, pituitary) 446 48,037 Chain (1); DNA binding (1) FUNCTION: Transcriptional regulator involved in developmental processes. Can activate POMC gene expression and repress the alpha glycoprotein subunit and thyroid-stimulating hormone beta promoters. {ECO:0000269|PubMed:11290323}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00201}. +Q61207 SAP_MOUSE Prosaposin (Sulfated glycoprotein 1) (SGP-1) [Cleaved into: Saposin-A; Saposin-B-Val; Saposin-B; Saposin-C; Saposin-D] 557 61,422 Chain (6); Disulfide bond (12); Domain (6); Glycosylation (4); Helix (4); Propeptide (5); Sequence conflict (21); Signal peptide (1) FUNCTION: Prosaposin: Behaves as a myelinotrophic and neurotrophic factor, these effects are mediated by its G-protein-coupled receptors, GPR37 and GPR37L1, undergoing ligand-mediated internalization followed by ERK phosphorylation signaling. {ECO:0000269|PubMed:23690594}.; FUNCTION: Saposin-A and saposin-C stimulate the hydrolysis of glucosylceramide by beta-glucosylceramidase (EC 3.2.1.45) and galactosylceramide by beta-galactosylceramidase (EC 3.2.1.46). Saposin-C apparently acts by combining with the enzyme and acidic lipid to form an activated complex, rather than by solubilizing the substrate. {ECO:0000250|UniProtKB:P07602}.; FUNCTION: Saposin-B stimulates the hydrolysis of galacto-cerebroside sulfate by arylsulfatase A (EC 3.1.6.8), GM1 gangliosides by beta-galactosidase (EC 3.2.1.23) and globotriaosylceramide by alpha-galactosidase A (EC 3.2.1.22). Saposin-B forms a solubilizing complex with the substrates of the sphingolipid hydrolases. {ECO:0000250|UniProtKB:P07602}.; FUNCTION: Saposin-D is a specific sphingomyelin phosphodiesterase activator (EC 3.1.4.12). {ECO:0000250|UniProtKB:P07602}.; FUNCTION: Saposins are specific low-molecular mass non-enzymic proteins, they participate in the lysosomal degradation of sphingolipids, which takes place by the sequential action of specific hydrolases. {ECO:0000250|UniProtKB:P07602}. SUBCELLULAR LOCATION: Prosaposin: Secreted {ECO:0000269|PubMed:23690594}. Note=Secreted as a fully glycosylated 70 kDa protein composed of complex glycans. {ECO:0000269|PubMed:23690594}.; SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:P07602}. SUBUNIT: Saposin-B is a homodimer. Prosaposin exists as a roughly half-half mixture of monomers and disulfide-linked dimers. Monomeric prosaposin interacts (via C-terminus) with sortilin/SORT1, the interaction is required for targeting to lysosomes. {ECO:0000250|UniProtKB:P07602}. +Q99PL7 SCD3_MOUSE Acyl-CoA desaturase 3 (EC 1.14.19.-) (Delta(9)-desaturase 3) (Delta-9 desaturase 3) (Fatty acid desaturase 3) (Palmitoyl-CoA desaturase) (Stearoyl-CoA desaturase 3) 359 41,432 Alternative sequence (1); Binding site (7); Chain (1); Metal binding (9); Modified residue (1); Motif (3); Mutagenesis (1); Sequence conflict (1); Topological domain (5); Transmembrane (4) TRANSMEM 73 93 Helical. {ECO:0000250|UniProtKB:O00767}.; TRANSMEM 98 118 Helical. {ECO:0000250|UniProtKB:O00767}.; TRANSMEM 218 237 Helical. {ECO:0000250|UniProtKB:O00767}.; TRANSMEM 242 263 Helical. {ECO:0000250|UniProtKB:O00767}. TOPO_DOM 1 72 Cytoplasmic. {ECO:0000250|UniProtKB:O00767}.; TOPO_DOM 94 97 Lumenal. {ECO:0000250|UniProtKB:O00767}.; TOPO_DOM 119 217 Cytoplasmic. {ECO:0000250|UniProtKB:O00767}.; TOPO_DOM 238 241 Lumenal. {ECO:0000250|UniProtKB:O00767}.; TOPO_DOM 264 359 Cytoplasmic. {ECO:0000250|UniProtKB:O00767}. FUNCTION: Stearyl-CoA desaturase that utilizes O(2) and electrons from reduced cytochrome b5 to introduce the first double bond into saturated fatty acyl-CoA substrates. Catalyzes the insertion of a cis double bond at the delta-9 position into fatty acyl-CoA substrates including palmitoyl-CoA (PubMed:16443825, PubMed:26098370). Has a strong preference for saturated fatty acids with chain lengths of 14 or 16 carbon atoms (C14:0 and C16:0), and has only very low activity with stearatate (C18:0) (PubMed:16443825, PubMed:26098370). Required for the biosynthesis of membrane phospholipids, cholesterol esters and triglycerides (By similarity). {ECO:0000250|UniProtKB:O00767, ECO:0000269|PubMed:16443825, ECO:0000269|PubMed:26098370}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O00767}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O00767}. Microsome membrane {ECO:0000269|PubMed:16443825}. DOMAIN: The histidine box domains are involved in binding the catalytic metal ions. {ECO:0000250|UniProtKB:O00767}. TISSUE SPECIFICITY: Detected in skin, but at lower levels compared to Scd1. Detected in the middlle part of the sebaceous gland, but not in hair follicle. Not detected in liver and brain. {ECO:0000269|PubMed:11161812}. +Q8VEA7 TCTA_MOUSE T-cell leukemia translocation-altered gene protein homolog 122 13,297 Chain (1); Glycosylation (1); Initiator methionine (1); Modified residue (1); Topological domain (3); Transmembrane (2) TRANSMEM 9 29 Helical. {ECO:0000255}.; TRANSMEM 44 64 Helical. {ECO:0000255}. TOPO_DOM 2 8 Extracellular. {ECO:0000255}.; TOPO_DOM 30 43 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 65 122 Extracellular. {ECO:0000255}. FUNCTION: May be required for cellular fusion during osteoclastogenesis. {ECO:0000250, ECO:0000269|PubMed:19560569}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q6GQS1 SCMC3_MOUSE Calcium-binding mitochondrial carrier protein SCaMC-3 (Small calcium-binding mitochondrial carrier protein 3) (Solute carrier family 25 member 23) 467 52,497 Calcium binding (2); Chain (1); Domain (3); Repeat (3); Topological domain (7); Transmembrane (6) TRANSMEM 188 205 Helical; Name=1. {ECO:0000255}.; TRANSMEM 243 262 Helical; Name=2. {ECO:0000255}.; TRANSMEM 286 299 Helical; Name=3. {ECO:0000255}.; TRANSMEM 336 355 Helical; Name=4. {ECO:0000255}.; TRANSMEM 379 396 Helical; Name=5. {ECO:0000255}.; TRANSMEM 436 455 Helical; Name=6. {ECO:0000255}. TOPO_DOM 1 187 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 206 242 Mitochondrial matrix. {ECO:0000255}.; TOPO_DOM 263 285 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 300 335 Mitochondrial matrix. {ECO:0000255}.; TOPO_DOM 356 378 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 397 435 Mitochondrial matrix. {ECO:0000255}.; TOPO_DOM 456 467 Mitochondrial intermembrane. {ECO:0000255}. FUNCTION: Calcium-dependent mitochondrial solute carrier. Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane. May act as a ATP-Mg/Pi exchanger that mediates the transport of Mg-ATP in exchange for phosphate, catalyzing the net uptake or efflux of adenine nucleotides into or from the mitochondria. Acts as a regulator of mitochondrial calcium uptake via interaction with MCU and MICU1. {ECO:0000250|UniProtKB:Q9BV35}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9BV35}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9BV35}. SUBUNIT: Interacts with MCU. Interacts with MICU1. {ECO:0000250|UniProtKB:Q9BV35}. +Q6DID3 SCAF8_MOUSE Protein SCAF8 (RNA-binding motif protein 16) (SR-related and CTD-associated factor 8) 1268 139,572 Chain (1); Compositional bias (4); Cross-link (1); Domain (2); Erroneous initiation (1); Modified residue (7); Sequence conflict (2) FUNCTION: May play a role in mRNA processing. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9528809}. Nucleus matrix {ECO:0000269|PubMed:9528809}. Note=Detected in granular nuclear foci which correspond to sites of active transcription. SUBUNIT: Interacts with phosphorylated POLR2A (via C-terminus). Identified in a complex with CDC5L and other spliceosomal proteins. May associate with the spliceosome (By similarity). {ECO:0000250}. +Q8K214 SCMH1_MOUSE Polycomb protein SCMH1 (Sex comb on midleg homolog 1) 706 78,669 Alternative sequence (2); Chain (1); Domain (1); Repeat (2) FUNCTION: Associates with Polycomb group (PcG) multiprotein complexes; the complex class is required to maintain the transcriptionally repressive state of some genes. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Associates with a PRC1-like complex (By similarity). Interacts with the SAM domain of PHC1 via its SAM domain in vitro. {ECO:0000250, ECO:0000269|PubMed:10653359}. TISSUE SPECIFICITY: Most abundant in testis. Moderate levels detected in heart, brain, lung, liver, skeletal muscle and kidney and lower levels in spleen. {ECO:0000269|PubMed:10653359}. +Q9R053 SCNBA_MOUSE Sodium channel protein type 11 subunit alpha (NaN) (Sensory neuron sodium channel 2) (Sodium channel protein type XI subunit alpha) (Voltage-gated sodium channel subunit alpha Nav1.9) 1765 201,385 Chain (1); Disulfide bond (2); Glycosylation (11); Intramembrane (4); Repeat (4); Sequence conflict (15); Topological domain (29); Transmembrane (24) INTRAMEM 343 367 Pore-forming. {ECO:0000250|UniProtKB:D0E0C2}.; INTRAMEM 743 763 Pore-forming. {ECO:0000250|UniProtKB:D0E0C2}.; INTRAMEM 1225 1246 Pore-forming. {ECO:0000250|UniProtKB:D0E0C2}.; INTRAMEM 1516 1538 Pore-forming. {ECO:0000250|UniProtKB:D0E0C2}. TRANSMEM 127 148 Helical; Name=S1 of repeat I. {ECO:0000250}.; TRANSMEM 160 179 Helical; Name=S2 of repeat I. {ECO:0000250}.; TRANSMEM 192 211 Helical; Name=S3 of repeat I. {ECO:0000250}.; TRANSMEM 220 239 Helical; Voltage-sensor; Name=S4 of repeat I. {ECO:0000250}.; TRANSMEM 256 269 Helical; Name=S5 of repeat I. {ECO:0000250}.; TRANSMEM 375 400 Helical; Name=S6 of repeat I. {ECO:0000250}.; TRANSMEM 571 594 Helical; Name=S1 of repeat II. {ECO:0000250}.; TRANSMEM 606 629 Helical; Name=S2 of repeat II. {ECO:0000250}.; TRANSMEM 638 659 Helical; Name=S3 of repeat II. {ECO:0000250}.; TRANSMEM 665 684 Helical; Voltage-sensor; Name=S4 of repeat II. {ECO:0000250}.; TRANSMEM 700 722 Helical; Name=S5 of repeat II. {ECO:0000250}.; TRANSMEM 774 799 Helical; Name=S6 of repeat II. {ECO:0000250}.; TRANSMEM 1031 1053 Helical; Name=S1 of repeat III. {ECO:0000250}.; TRANSMEM 1068 1093 Helical; Name=S2 of repeat III. {ECO:0000250}.; TRANSMEM 1100 1117 Helical; Name=S3 of repeat III. {ECO:0000250}.; TRANSMEM 1119 1140 Helical; Voltage-sensor; Name=S4 of repeat III. {ECO:0000250}.; TRANSMEM 1160 1181 Helical; Name=S5 of repeat III. {ECO:0000250}.; TRANSMEM 1263 1289 Helical; Name=S6 of repeat III. {ECO:0000250}.; TRANSMEM 1343 1366 Helical; Name=S1 of repeat IV. {ECO:0000250}.; TRANSMEM 1378 1401 Helical; Name=S2 of repeat IV. {ECO:0000250}.; TRANSMEM 1408 1431 Helical; Name=S3 of repeat IV. {ECO:0000250}.; TRANSMEM 1441 1463 Helical; Voltage-sensor; Name=S4 of repeat IV. {ECO:0000250}.; TRANSMEM 1479 1501 Helical; Name=S5 of repeat IV. {ECO:0000250}.; TRANSMEM 1560 1584 Helical; Name=S6 of repeat IV. {ECO:0000250}. TOPO_DOM 1 126 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 149 159 Extracellular. {ECO:0000305}.; TOPO_DOM 180 191 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 212 219 Extracellular. {ECO:0000305}.; TOPO_DOM 240 255 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 270 342 Extracellular. {ECO:0000305}.; TOPO_DOM 368 374 Extracellular. {ECO:0000305}.; TOPO_DOM 401 570 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 595 605 Extracellular. {ECO:0000305}.; TOPO_DOM 630 637 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 660 664 Extracellular. {ECO:0000305}.; TOPO_DOM 685 699 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 723 742 Extracellular. {ECO:0000305}.; TOPO_DOM 764 773 Extracellular. {ECO:0000305}.; TOPO_DOM 800 1030 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1054 1067 Extracellular. {ECO:0000305}.; TOPO_DOM 1094 1099 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1118 1118 Extracellular. {ECO:0000305}.; TOPO_DOM 1141 1159 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1182 1224 Extracellular. {ECO:0000305}.; TOPO_DOM 1247 1262 Extracellular. {ECO:0000305}.; TOPO_DOM 1290 1342 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1367 1377 Extracellular. {ECO:0000305}.; TOPO_DOM 1402 1407 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1432 1440 Extracellular. {ECO:0000305}.; TOPO_DOM 1464 1478 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1502 1515 Extracellular. {ECO:0000305}.; TOPO_DOM 1539 1559 Extracellular. {ECO:0000305}.; TOPO_DOM 1585 1765 Cytoplasmic. {ECO:0000305}. FUNCTION: This protein mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which sodium ions may pass in accordance with their electrochemical gradient. It is a tetrodotoxin-resistant sodium channel isoform. Also involved, with the contribution of the receptor tyrosine kinase NTRK2, in rapid BDNF-evoked neuronal depolarization (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:D0E0C2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:D0E0C2}. SUBUNIT: The voltage-resistant sodium channel consists of an ion conducting pore forming alpha-subunit regulated by one or more auxiliary subunits SCN1B, SCN2B and SCN3B. DOMAIN: The sequence contains 4 internal repeats, each with 5 hydrophobic segments (S1, S2, S3, S5, S6) and one positively charged segment (S4). Segments S4 are probably the voltage-sensors and are characterized by a series of positively charged amino acids at every third position. {ECO:0000305}. TISSUE SPECIFICITY: Expressed in the dorsal root ganglia (C-fiber neurons), spinal cord, trigeminal ganglia, testis, ovary, uterus and small intestine. {ECO:0000269|PubMed:10623609}. +Q3TMH2 SCRN3_MOUSE Secernin-3 418 47,661 Active site (1); Chain (1); Sequence conflict (1) +O88745 SCRG1_MOUSE Scrapie-responsive protein 1 (Scrapie-responsive gene 1 protein) (ScRG-1) 98 11,173 Chain (1); Glycosylation (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q99M85 SCRT1_MOUSE Transcriptional repressor scratch 1 (Scratch homolog 1 zinc finger protein) (SCRT) (Scratch 1) (mScrt) 348 35,919 Chain (1); Region (1); Zinc finger (5) FUNCTION: Transcriptional repressor that binds E-box motif CAGGTG (By similarity). Appears to function downstream of proneural bHLH proteins in promoting neural differentiation. {ECO:0000250, ECO:0000269|PubMed:11687288}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts (via SNAG domain) with LIMD1 (via LIM domains), WTIP (via LIM domains) and AJUBA (via LIM domains). {ECO:0000269|PubMed:18331720}. DOMAIN: The N-terminal non zinc-finger region mediates the repressor activity. {ECO:0000250}. +Q80YX1 TENA_MOUSE Tenascin (TN) (Hexabrachion) (Tenascin-C) (TN-C) 2110 231,807 Alternative sequence (4); Chain (1); Coiled coil (1); Disulfide bond (42); Domain (30); Glycosylation (20); Modified residue (4); Sequence conflict (5); Signal peptide (1) FUNCTION: Extracellular matrix protein implicated in guidance of migrating neurons as well as axons during development, synaptic plasticity as well as neuronal regeneration. Promotes neurite outgrowth when provided to neurons in culture. May play a role in supporting the growth of epithelial tumors. Ligand for integrins ITGA8:ITGB1, ITGA9:ITGB1, ITGAV:ITGB3 and ITGAV:ITGB6. In tumors, stimulates angiogenesis by elongation, migration and sprouting of endothelial cells (By similarity). {ECO:0000250|UniProtKB:P24821, ECO:0000269|PubMed:16553788}. PTM: N-glycosylated. {ECO:0000269|PubMed:16944957, ECO:0000269|PubMed:1703162}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. SUBUNIT: Homohexamer; disulfide-linked. A homotrimer may be formed in the triple coiled-coil region and may be stabilized by disulfide rings at both ends. Two of such half-hexabrachions may be disulfide linked within the central globule. Interacts with CSPG4 (By similarity). {ECO:0000250|UniProtKB:P24821}. TISSUE SPECIFICITY: Expressed in kidney, aortic valve, corneal limbus, periosteum around the ribs, cerebellum, stomach and intestine (PubMed:14709716). High levels of isoform 2 in lung and brain of newborn mice. High levels of isoform 5 in thymus, moderate levels in brain of newborn and adult mice. Low level of isoform 2 in adult brain. {ECO:0000269|PubMed:14709716, ECO:0000269|PubMed:1717349}. +Q9Z2G6 SE1L1_MOUSE Protein sel-1 homolog 1 (Suppressor of lin-12-like protein 1) (Sel-1L) 790 88,340 Alternative sequence (1); Beta strand (3); Chain (1); Compositional bias (1); Disulfide bond (2); Domain (1); Glycosylation (5); Helix (10); Modified residue (1); Mutagenesis (4); Region (4); Repeat (11); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 735 755 Helical. {ECO:0000255}. TOPO_DOM 22 734 Lumenal. {ECO:0000255}.; TOPO_DOM 756 790 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a role in the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins (PubMed:25066055, PubMed:24453213). Enhances SYVN1 stability (PubMed:24453213). Plays a role in LPL maturation and secretion (PubMed:25066055). Required for normal differentiation of the pancreas epithelium, and for normal exocrine function and survival of pancreatic cells (PubMed:20170518, PubMed:24453213). May play a role in Notch signaling (PubMed:20170518). {ECO:0000269|PubMed:20170518, ECO:0000269|PubMed:24453213, ECO:0000269|PubMed:25066055}. PTM: N-glycosylated. {ECO:0000269|PubMed:25066055}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9UBV2}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9UBV2}. SUBUNIT: Homodimer and homooligomer (PubMed:27064360). Interacts with SYVN1; the interaction is direct (PubMed:25066055, PubMed:27064360). Part of a complex containing SEL1L, SYVN1 and DERL2. May form a complex with ERLEC1, HSPA5, OS9, and SYVN1. Interacts with FOXRED2 and EDEM1 (By similarity). Interacts with LPL and LMF1; may stabilize the complex formed by LPL and LMF1 and thereby promote the export of LPL dimers (PubMed:25066055). {ECO:0000250|UniProtKB:Q9UBV2, ECO:0000269|PubMed:25066055, ECO:0000269|PubMed:27064360}. TISSUE SPECIFICITY: Highly expressed in pancreas, white adipose tissue, liver and spleen (at protein level) (PubMed:25066055, PubMed:24453213). Detected in heart, brain, spleen, lung, liver, kidney and testis (PubMed:9858735). {ECO:0000269|PubMed:24453213, ECO:0000269|PubMed:25066055, ECO:0000269|PubMed:9858735}. +Q80TS8 SE1L3_MOUSE Protein sel-1 homolog 3 (Suppressor of lin-12-like protein 3) (Sel-1L3) 1137 128,680 Alternative sequence (3); Chain (1); Erroneous initiation (2); Glycosylation (3); Modified residue (1); Repeat (8); Sequence conflict (5); Transmembrane (1) TRANSMEM 1067 1087 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q4V9Z5 SE6L2_MOUSE Seizure 6-like protein 2 (Brain-specific receptor-like protein A) (BSRP-A) 910 97,504 Alternative sequence (2); Chain (1); Compositional bias (2); Disulfide bond (13); Domain (8); Glycosylation (5); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 845 865 Helical. {ECO:0000255}. TOPO_DOM 28 844 Extracellular. {ECO:0000255}.; TOPO_DOM 866 910 Cytoplasmic. {ECO:0000255}. FUNCTION: May contribute to specialized endoplasmic reticulum functions in neurons. {ECO:0000269|PubMed:16814779}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:16814779}; Single-pass type I membrane protein {ECO:0000269|PubMed:16814779}. Note=In cerebellar predominantly localized to the endoplasmic reticulum. TISSUE SPECIFICITY: Expressed exclusively in the brain, predominantly in the neurons. Wide expression in the gray matter of the brain with high levels in the olfactory bulb, anterior olfactory nuclei, hippocampal formation and cerebellar cortex. Detected diffusely and weakly in the white matter, such as the corpus callosum and cerebellar medulla. In the cerebellar cortex, intensely expressed in Purkinje cells (PC) and granule cells. Detected also in interneurons in the molecular layer. Up-regulated at two weeks after birth. {ECO:0000269|PubMed:16814779}. +P70368 SEBOX_MOUSE Homeobox protein SEBOX (Homeobox OG-9) (Skin-, embryo-, brain- and oocyte-specific homeobox) 190 20,391 Chain (1); DNA binding (1) FUNCTION: Probable transcription factor involved in the control of specification of mesoderm and endoderm. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. TISSUE SPECIFICITY: Expressed in brain, skin, ovary and liver. Also expressed in maturing oocytes, eggs, zygotes and 2-cell embryos, but not 4-cell embryos. {ECO:0000269|PubMed:10922053, ECO:0000269|PubMed:8855241}. +Q8R238 SDSL_MOUSE Serine dehydratase-like (EC 4.3.1.17) (L-serine deaminase) (L-serine dehydratase/L-threonine deaminase) (L-threonine dehydratase) (TDH) (EC 4.3.1.19) (SDH) 329 34,732 Chain (1); Frameshift (1); Modified residue (2) FUNCTION: Has low serine dehydratase and threonine dehydratase activity. {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Abundantly expressed in liver. {ECO:0000269|PubMed:15757516}. +Q9JLJ1 SELK_MOUSE Selenoprotein K (SelK) 94 10,642 Chain (1); Erroneous termination (1); Non-standard residue (1); Site (1); Transmembrane (1) TRANSMEM 20 42 Helical. {ECO:0000255}. FUNCTION: Required for Ca(2+) flux in immune cells and plays a role in T-cell proliferation and in T-cell and neutrophil migration (PubMed:21220695). Involved in endoplasmic reticulum-associated degradation (ERAD) of soluble glycosylated proteins (By similarity). Required for palmitoylation and cell surface expression of CD36 and involved in macrophage uptake of low-density lipoprotein and in foam cell formation (PubMed:23444136). Together with ZDHHC6, required for palmitoylation of ITPR1 in immune cells, leading to regulate ITPR1 stability and function (PubMed:25368151). Plays a role in protection of cells from ER stress-induced apoptosis (By similarity). Protects cells from oxidative stress when overexpressed in cardiomyocytes (By similarity). {ECO:0000250|UniProtKB:Q9Y6D0, ECO:0000269|PubMed:21220695, ECO:0000269|PubMed:23444136, ECO:0000269|PubMed:25368151}. PTM: Cleaved by CAPN2/m-calpain in resting macrophages but not in activated macrophages. Macrophage activation up-regulates expression of the calpain inhibitor CAST/calpastatin, resulting in inhibition of CAPN2 activity. {ECO:0000269|PubMed:21849499}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21220695}; Single-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q9Y6D0}; Single-pass membrane protein {ECO:0000255}. Note=Probably mainly localized in the ER. {ECO:0000269|PubMed:21220695}. SUBUNIT: Interacts with DERL1, DERL2, DERL3 and SELENOS (PubMed:22016385). The SELENOK-SELENOS complex interacts with VCP (By similarity). Interacts with ZDHHC6 (PubMed:25368151). {ECO:0000250|UniProtKB:Q9Y6D0, ECO:0000269|PubMed:22016385}. TISSUE SPECIFICITY: High expression in spleen and intestine (at protein level). Expressed in a range of immune cells including T and B-cells and also in myeloid cells including macrophages, neutrophils and dendritic cells (at protein level). {ECO:0000269|PubMed:21220695, ECO:0000269|PubMed:21849499}. +D3Z2R5 SELN_MOUSE Selenoprotein N (SelN) 557 62,492 Chain (1); Compositional bias (2); Domain (1); Glycosylation (3); Non-standard residue (1); Signal peptide (1) FUNCTION: Plays an important role in cell protection against oxidative stress and in the regulation of redox-related calcium homeostasis. Regulates the calcium level of the ER by protecting the calcium pump ATP2A2 against the oxidoreductase ERO1A-mediated oxidative damage. Within the ER, ERO1A activity increases the concentration of H(2)O(2), which attacks the luminal thiols in ATP2A2 and thus leads to cysteinyl sulfenic acid formation (-SOH) and SEPN1 reduces the SOH back to free thiol (-SH), thus restoring ATP2A2 activity (PubMed:25452428). Acts as a modulator of ryanodine receptor (RyR) activity: protects RyR from oxidation due to increased oxidative stress, or directly controls the RyR redox state, regulating the RyR-mediated calcium mobilization required for normal muscle development and differentiation (By similarity). Essential for muscle regeneration and satellite cell maintenance in skeletal muscle (PubMed:21131290). {ECO:0000250|UniProtKB:Q9NZV5, ECO:0000269|PubMed:21131290, ECO:0000269|PubMed:25452428}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9NZV5}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9NZV5}. SUBUNIT: Interacts with RYR1, RYR2 and RYR3. {ECO:0000250|UniProtKB:Q9NZV5}. DOMAIN: The N-terminus (first 61 amino acids) contains an endoplasmic reticulum addressing and retention targeting signal. {ECO:0000250|UniProtKB:Q9NZV5}. +Q9Z123 SEM4F_MOUSE Semaphorin-4F (Semaphorin-W) (Sema W) 777 84,490 Chain (1); Disulfide bond (7); Domain (3); Glycosylation (3); Modified residue (2); Natural variant (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 668 688 Helical. {ECO:0000255}. TOPO_DOM 41 667 Extracellular. {ECO:0000255}.; TOPO_DOM 689 777 Cytoplasmic. {ECO:0000255}. FUNCTION: Has growth cone collapse activity against retinal ganglion-cell axons. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. +Q9WUH7 SEM4G_MOUSE Semaphorin-4G 837 92,378 Chain (1); Compositional bias (2); Disulfide bond (7); Domain (3); Glycosylation (6); Modified residue (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 674 694 Helical. {ECO:0000255}. TOPO_DOM 18 673 Extracellular. {ECO:0000255}.; TOPO_DOM 695 837 Cytoplasmic. {ECO:0000255}. FUNCTION: Cell surface receptor for PLXNB2. May play a role in axon guidance. {ECO:0000269|PubMed:21122816}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SUBUNIT: Interacts with PLXNB2. {ECO:0000269|PubMed:21122816}. TISSUE SPECIFICITY: Brain, spinal cord, and several sensory organs as well as specific populations of projection neurons. +Q9Z1S5 SEPT3_MOUSE Neuronal-specific septin-3 350 40,038 Alternative sequence (1); Binding site (3); Chain (1); Domain (1); Frameshift (1); Modified residue (1); Nucleotide binding (2); Region (3); Sequence conflict (1) FUNCTION: Filament-forming cytoskeletal GTPase (By similarity). May play a role in cytokinesis (Potential). {ECO:0000250, ECO:0000305}. PTM: Phosphorylated by PKG on serine residues. Phosphorylated by PKG on Ser-91 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton {ECO:0000250}. Cell junction, synapse {ECO:0000250}. SUBUNIT: Septins polymerize into heterooligomeric protein complexes that form filaments, and can associate with cellular membranes, actin filaments and microtubules. GTPase activity is required for filament formation (By similarity). {ECO:0000250}. +P28661 SEPT4_MOUSE Septin-4 (Brain protein H5) (Peanut-like protein 2) 478 54,936 Alternative sequence (8); Binding site (4); Chain (1); Coiled coil (1); Domain (1); Modified residue (8); Nucleotide binding (2); Region (3); Sequence conflict (1) FUNCTION: Filament-forming cytoskeletal GTPase. Forms a filamentous structure with SEPT12, SEPT6, SEPT2 and probably SEPT4 at the sperm annulus which is required for the structural integrity and motility of the sperm tail during postmeiotic differentiation (By similarity). May play a role in cytokinesis (Potential). May play a role in platelet secretion (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O43236, ECO:0000305}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12581152, ECO:0000269|PubMed:17546647}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:O43236}. Note=Found in the sperm annulus. {ECO:0000250|UniProtKB:O43236}.; SUBCELLULAR LOCATION: Isoform 4: Mitochondrion. Note=In retinoic acid-treated P19 cells, isoform 4 is found first in the mitochondria and at later times, as neuronal differentiation proceeds, in the cytosol. SUBUNIT: Septins polymerize into heterooligomeric protein complexes that form filaments, and can associate with cellular membranes, actin filaments and microtubules. GTPase activity is required for filament formation (By similarity). Interacts with SEPT8 (By similarity). Component of a septin core octomeric complex consisting of SEPT12, SEPT7, SEPT6 and SEPT2 or SEPT4 in the order 12-7-6-2-2-6-7-12 or 12-7-6-4-4-6-7-12 and located in the sperm annulus (By similarity). Isoform 4 interacts with DPYSL5. {ECO:0000250, ECO:0000250|UniProtKB:O43236, ECO:0000269|PubMed:12581152}. TISSUE SPECIFICITY: Expressed in the brain. Abundant in areas of high cell density, particularly in the stria terminalis. Isoform 4 is predominantly expressed in embryonic mouse brain and dorsal root ganglion neurons. {ECO:0000269|PubMed:12581152}. +Q9QUR8 SEM7A_MOUSE Semaphorin-7A (Semaphorin-K1) (Sema K1) (Semaphorin-L) (Sema L) (CD antigen CD108) 664 74,994 Chain (1); Disulfide bond (9); Domain (2); Glycosylation (5); Lipidation (1); Modified residue (1); Motif (1); Propeptide (1); Region (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Plays an important role in integrin-mediated signaling and functions both in regulating cell migration and immune responses. Promotes formation of focal adhesion complexes, activation of the protein kinase PTK2/FAK1 and subsequent phosphorylation of MAPK1 and MAPK3. Promotes production of proinflammatory cytokines by monocytes and macrophages. Plays an important role in modulating inflammation and T-cell-mediated immune responses. Promotes axon growth in the embryonic olfactory bulb. Promotes attachment, spreading and dendrite outgrowth in melanocytes. {ECO:0000269|PubMed:12879062, ECO:0000269|PubMed:16713976, ECO:0000269|PubMed:17377534}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17377534}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:17377534}; Extracellular side {ECO:0000269|PubMed:17377534}. SUBUNIT: Interacts with PLXNC1 (By similarity). Interacts with ITGA1 and ITGB1. {ECO:0000250, ECO:0000269|PubMed:17377534}. TISSUE SPECIFICITY: Highly expressed in activated T-cells (at protein level). Highest expression in brain. Lower in heart, thymus, spleen, testis and ovary. The expression increases in late embryonic and postnatal stages. Detected in T-cells. {ECO:0000269|PubMed:16713976, ECO:0000269|PubMed:17377534}. +Q8K0E7 SERC2_MOUSE Serine incorporator 2 (Tumor differentially expressed protein 2-like) 450 50,478 Chain (1); Transmembrane (11) TRANSMEM 5 27 Helical. {ECO:0000255}.; TRANSMEM 40 57 Helical. {ECO:0000255}.; TRANSMEM 96 118 Helical. {ECO:0000255}.; TRANSMEM 131 150 Helical. {ECO:0000255}.; TRANSMEM 160 182 Helical. {ECO:0000255}.; TRANSMEM 203 225 Helical. {ECO:0000255}.; TRANSMEM 238 257 Helical. {ECO:0000255}.; TRANSMEM 264 286 Helical. {ECO:0000255}.; TRANSMEM 315 337 Helical. {ECO:0000255}.; TRANSMEM 380 402 Helical. {ECO:0000255}.; TRANSMEM 417 439 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q6P4U0 THS7B_MOUSE Thrombospondin type-1 domain-containing protein 7B 1607 179,309 Chain (1); Compositional bias (1); Disulfide bond (21); Domain (18); Glycosylation (14); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1557 1577 Helical. {ECO:0000255}. TOPO_DOM 32 1556 Extracellular. {ECO:0000255}.; TOPO_DOM 1578 1607 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q80UG5 SEPT9_MOUSE Septin-9 (SL3-3 integration site 1 protein) 583 65,575 Alternative sequence (2); Binding site (4); Chain (1); Domain (1); Erroneous initiation (1); Modified residue (12); Nucleotide binding (2); Region (3) FUNCTION: Filament-forming cytoskeletal GTPase (By similarity). May play a role in cytokinesis (Potential). {ECO:0000250, ECO:0000305}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17546647}. Note=In an epithelial cell line, concentrates at cell-cell contact areas. After TGF-beta1 treatment and induction of epithelial to mesenchymal transition, colocalizes with actin stress fibers. SUBUNIT: Septins polymerize into heterooligomeric protein complexes that form filaments, and associate with cellular membranes, actin filaments, and microtubules. GTPase activity is required for filament formation. Interacts with SEPT2, SEPT6, SEPT7, SEPT11 and SEPT14. Interacts with RTKN and ARHGEF18 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in all tissues examined except muscle. Isoforms are differentially expressed in testes, kidney, liver, heart, spleen and brain. {ECO:0000269|PubMed:10666245, ECO:0000269|PubMed:12039034}. DISEASE: Note=Putative proto-oncogene involved in T-cell lymphomagenesis. May play a role in leukemogenesis. +Q8CFT2 SET1B_MOUSE Histone-lysine N-methyltransferase SETD1B (EC 2.1.1.43) (SET domain-containing protein 1B) 1985 215,352 Alternative sequence (1); Chain (1); Compositional bias (3); Domain (3); Modified residue (8); Sequence conflict (2) FUNCTION: Histone methyltransferase that specifically methylates 'Lys-4' of histone H3, when part of the SET1 histone methyltransferase (HMT) complex, but not if the neighboring 'Lys-9' residue is already methylated. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. The non-overlapping localization with SETD1B suggests that SETD1A and SETD1B make non-redundant contributions to the epigenetic control of chromatin structure and gene expression (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}. Chromosome {ECO:0000250}. Note=Localizes to a largely non-overlapping set of euchromatic nuclear speckles with SETD1A, suggesting that SETD1A and SETD1B each bind to a unique set of target genes. {ECO:0000250}. SUBUNIT: Component of the SET1 complex, at least composed of the catalytic subunit (SETD1A or SETD1B), WDR5, WDR82, RBBP5, ASH2L/ASH2, CXXC1/CFP1, HCFC1 and DPY30. Interacts with HCFC1. and ASH2L/ASH2. Interacts (via the RRM domain) with WDR82. Interacts (via the RRM domain) with hyperphosphorylated C-terminal domain (CTD) of RNA polymerase II large subunit (POLR2A) only in the presence of WDR82. Binds specifically to CTD heptad repeats phosphorylated on 'Ser-5' of each heptad. Interacts with RBM15 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:17355966}. +Q5SSN7 SFT2A_MOUSE Vesicle transport protein SFT2A (SFT2 domain-containing protein 1) 159 17,923 Chain (1); Modified residue (1); Topological domain (5); Transmembrane (4) TRANSMEM 37 57 Helical; Name=1. {ECO:0000255}.; TRANSMEM 63 83 Helical; Name=2. {ECO:0000255}.; TRANSMEM 98 118 Helical; Name=3. {ECO:0000255}.; TRANSMEM 123 143 Helical; Name=4. {ECO:0000255}. TOPO_DOM 1 36 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 58 62 Lumenal. {ECO:0000255}.; TOPO_DOM 84 97 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 119 122 Lumenal. {ECO:0000255}.; TOPO_DOM 144 159 Cytoplasmic. {ECO:0000255}. FUNCTION: May be involved in fusion of retrograde transport vesicles derived from an endocytic compartment with the Golgi complex. {ECO:0000250|UniProtKB:P38166}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. +P82347 SGCD_MOUSE Delta-sarcoglycan (Delta-SG) (35 kDa dystrophin-associated glycoprotein) (35DAG) 289 32,133 Chain (1); Disulfide bond (2); Glycosylation (3); Topological domain (2); Transmembrane (1) TRANSMEM 38 56 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 37 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 57 289 Extracellular. {ECO:0000255}. FUNCTION: Component of the sarcoglycan complex, a subcomplex of the dystrophin-glycoprotein complex which forms a link between the F-actin cytoskeleton and the extracellular matrix. PTM: Disulfide bonds are present. SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000269|PubMed:9864373}; Single-pass type II membrane protein {ECO:0000269|PubMed:9864373}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9864373}. SUBUNIT: Interacts with FLNC (By similarity). Cross-link to form 2 major subcomplexes: one consisting of SGCB, SGCD and SGCG and the other consisting of SGCB and SGCD. The association between SGCB and SGCG is particularly strong while SGCA is loosely associated with the other sarcoglycans. Interacts with DAG1. {ECO:0000250, ECO:0000269|PubMed:9864373}. TISSUE SPECIFICITY: Most strongly expressed in skeletal and heart muscle. Also detected in proliferating myoblasts. +Q925N1 SFXN4_MOUSE Sideroflexin-4 313 35,580 Chain (1); Modified residue (1); Sequence conflict (5); Transmembrane (5) TRANSMEM 87 107 Helical. {ECO:0000255}.; TRANSMEM 141 161 Helical. {ECO:0000255}.; TRANSMEM 175 191 Helical. {ECO:0000255}.; TRANSMEM 230 247 Helical. {ECO:0000255}.; TRANSMEM 269 289 Helical. {ECO:0000255}. FUNCTION: Potential iron transporter. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Largely restricted to kidney, brain and heart. {ECO:0000269|PubMed:11274051}. +Q3TUA9 SG196_MOUSE Protein O-mannose kinase (POMK) (EC 2.7.1.183) (Protein kinase-like protein SgK196) (Sugen kinase 196) 349 39,969 Beta strand (9); Chain (1); Domain (1); Glycosylation (3); Helix (13); Sequence conflict (6); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 20 42 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 19 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 43 349 Lumenal. {ECO:0000255}. FUNCTION: Protein O-mannose kinase that specifically mediates phosphorylation at the 6-position of an O-mannose of the trisaccharide (N-acetylgalactosamine (GalNAc)-beta-1,3-N-acetylglucosamine (GlcNAc)-beta-1,4-mannose) to generate phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-1,3-N-acetylglucosamine-beta-1,4-(phosphate-6-)mannose). Phosphorylated O-mannosyl trisaccharide is a carbohydrate structure present in alpha-dystroglycan (DAG1), which is required for binding laminin G-like domain-containing extracellular proteins with high affinity. Only shows kinase activity when the GalNAc-beta-3-GlcNAc-beta-terminus is linked to the 4-position of O-mannose, suggesting that this disaccharide serves as the substrate recognition motif (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. +P43407 SDC2_MOUSE Syndecan-2 (SYND2) (Fibroglycan) (Heparan sulfate proteoglycan core protein) (HSPG) (CD antigen CD362) 202 22,131 Chain (1); Glycosylation (3); Modified residue (2); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 146 170 Helical. {ECO:0000255}. TOPO_DOM 19 145 Extracellular. {ECO:0000255}.; TOPO_DOM 171 202 Cytoplasmic. {ECO:0000255}. FUNCTION: Cell surface proteoglycan that bears heparan sulfate. Regulates dendritic arbor morphogenesis. {ECO:0000269|PubMed:21555464}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Interacts (via cytoplasmic domain) with SARM1 (PubMed:21555464). Forms a complex with SDCBP and PDCD6IP (By similarity). {ECO:0000250|UniProtKB:P34741, ECO:0000269|PubMed:21555464}. TISSUE SPECIFICITY: Preferential expression in cells of mesenchymal origin. +Q64519 SDC3_MOUSE Syndecan-3 (SYND3) 442 46,002 Chain (1); Compositional bias (1); Glycosylation (6); Modified residue (4); Sequence conflict (10); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 388 408 Helical. {ECO:0000255}. TOPO_DOM 45 387 Extracellular. {ECO:0000255}.; TOPO_DOM 409 442 Cytoplasmic. {ECO:0000255}. FUNCTION: Cell surface proteoglycan that may bear heparan sulfate. May have a role in the organization of cell shape by affecting the actin cytoskeleton, possibly by transferring signals from the cell surface in a sugar-dependent mechanism (By similarity). {ECO:0000250}. PTM: O-glycosylated within the Thr/Ser-rich region which could interact with lectin domains on other molecules. {ECO:0000305}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Interacts with TIAM1. {ECO:0000250}. +Q9ESP1 SDF2L_MOUSE Stromal cell-derived factor 2-like protein 1 (SDF2-like protein 1) 221 23,648 Chain (1); Domain (3); Modified residue (1); Motif (1); Signal peptide (1) SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138}. TISSUE SPECIFICITY: Ubiquitously expressed with high expression in the testis, ovary, uterus, and low expression in heart and skeletal muscle. +Q9CQA3 SDHB_MOUSE Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial (EC 1.3.5.1) (Iron-sulfur subunit of complex II) (Ip) 282 31,814 Binding site (1); Chain (1); Domain (2); Metal binding (11); Modified residue (2); Sequence conflict (1); Transit peptide (1) Carbohydrate metabolism; tricarboxylic acid cycle; fumarate from succinate (eukaryal route): step 1/1. FUNCTION: Iron-sulfur protein (IP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Matrix side {ECO:0000250}. SUBUNIT: Component of complex II composed of four subunits: the flavoprotein (FP) SDHA, iron-sulfur protein (IP) SDHB, and a cytochrome b560 composed of SDHC and SDHD. {ECO:0000250}. +O35988 SDC4_MOUSE Syndecan-4 (SYND4) (Ryudocan core protein) 198 21,482 Chain (1); Glycosylation (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 146 170 Helical. {ECO:0000255}. TOPO_DOM 24 145 Extracellular. {ECO:0000255}.; TOPO_DOM 171 198 Cytoplasmic. {ECO:0000255}. FUNCTION: Cell surface proteoglycan that bears heparan sulfate. Regulates exosome biogenesis in concert with SDCBP and PDCD6IP. {ECO:0000250|UniProtKB:P31431}. PTM: Shedding is enhanced by a number of factors such as heparanase, thrombin or EGF. Also by stress and wound healing. PMA-mediated shedding is inhibited by TIMP3. {ECO:0000269|PubMed:10684261}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}. Secreted {ECO:0000269|PubMed:10684261}. Note=Shedding of the ectodomain produces a soluble form. {ECO:0000269|PubMed:10684261}. SUBUNIT: Homodimer. Interacts with CDCP1 and SDCBP (By similarity). Interacts (via its cytoplasmic domain) with GIPC (via its PDZ domain). Interacts (via its cytoplasmic domain) with NUDT16L1. {ECO:0000250|UniProtKB:P31431, ECO:0000269|PubMed:10911369, ECO:0000269|PubMed:11805099}. TISSUE SPECIFICITY: Ubiquitous. Highest levels in liver, kidney and lung. +Q8VBT2 SDHL_MOUSE L-serine dehydratase/L-threonine deaminase (SDH) (EC 4.3.1.17) (L-serine deaminase) (L-threonine dehydratase) (TDH) (EC 4.3.1.19) 327 34,593 Chain (1); Initiator methionine (1); Modified residue (2) Carbohydrate biosynthesis; gluconeogenesis. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +Q8BQU3 SDHF3_MOUSE Succinate dehydrogenase assembly factor 3, mitochondrial (SDH assembly factor 3) (SDHAF3) 125 14,468 Chain (1); Transit peptide (1) FUNCTION: Plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Promotes maturation of the iron-sulfur protein subunit Sdhb of the SDH catalytic dimer, protecting it from the deleterious effects of oxidants. May act together with SDHAF1. {ECO:0000250|UniProtKB:Q04401, ECO:0000250|UniProtKB:Q8SZ16}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:Q04401}. SUBUNIT: Interacts with Sdhb within an Sdha-Sdhb subcomplex. {ECO:0000250|UniProtKB:Q04401}. +Q91WD9 SEGN_MOUSE Secretagogin 276 32,146 Calcium binding (6); Chain (1); Domain (6) SUBCELLULAR LOCATION: Cytoplasm. Secreted {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Predominantly cytoplasmic. A small proportion is associated with secretory granules and membrane fractions (By similarity). {ECO:0000250}. +Q9QZI9 SERC3_MOUSE Serine incorporator 3 (Axotomy-induced glyco/Golgi protein 1) (AIGP-1) (Axotomy-induced glycoprotein 1) (Membrane protein TMS-1) (Tumor differentially expressed protein 1) 472 52,623 Chain (1); Erroneous initiation (1); Glycosylation (1); Modified residue (1); Sequence conflict (10); Topological domain (9); Transmembrane (8) TRANSMEM 97 117 Helical. {ECO:0000255}.; TRANSMEM 133 153 Helical. {ECO:0000255}.; TRANSMEM 159 179 Helical. {ECO:0000255}.; TRANSMEM 207 227 Helical. {ECO:0000255}.; TRANSMEM 239 259 Helical. {ECO:0000255}.; TRANSMEM 330 350 Helical. {ECO:0000255}.; TRANSMEM 406 426 Helical. {ECO:0000255}.; TRANSMEM 446 466 Helical. {ECO:0000255}. TOPO_DOM 1 96 Extracellular. {ECO:0000255}.; TOPO_DOM 118 132 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 154 158 Extracellular. {ECO:0000255}.; TOPO_DOM 180 206 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 228 238 Extracellular. {ECO:0000255}.; TOPO_DOM 260 329 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 351 405 Extracellular. {ECO:0000255}.; TOPO_DOM 427 445 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 467 472 Extracellular. {ECO:0000255}. FUNCTION: Restriction factor required to restrict infectivity of gammaretroviruses: acts by inhibiting early step of viral infection and impairing the ability of the viral particle to translocate its content to the cytoplasm. {ECO:0000250|UniProtKB:Q13530}. PTM: N-glycosylated. {ECO:0000269|PubMed:12486168}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12486168}; Multi-pass membrane protein {ECO:0000269|PubMed:12486168}. Golgi apparatus membrane {ECO:0000269|PubMed:12486168}; Multi-pass membrane protein {ECO:0000269|PubMed:12486168}. Note=Localizes to the cell membrane, where it is efficiently incorporated into budding gammaretrovirus virions and impairs subsequent virion penetration of susceptible target cells (By similarity). {ECO:0000250|UniProtKB:Q86VE9}. TISSUE SPECIFICITY: Highly expressed in the neuronal populations such as Purkinje cells in the cerebellum, brainstem and spinal motor neurons, locus coeruleus and raphe nuclei. Highly expressed also in thymus, kidney liver and testis. {ECO:0000269|PubMed:10637174}. +Q9WU66 SFRP5_MOUSE Secreted frizzled-related protein 5 (sFRP-5) 314 35,382 Chain (1); Disulfide bond (8); Domain (2); Sequence conflict (1); Signal peptide (1) FUNCTION: Soluble frizzled-related proteins (sFRPS) function as modulators of Wnt signaling through direct interaction with Wnts. They have a role in regulating cell growth and differentiation in specific cell types. SFRP5 may be involved in determining the polarity of photoreceptor, and perhaps, other cells in the retina. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. DOMAIN: The FZ domain is involved in binding with Wnt ligands. {ECO:0000250}. +Q8BX51 SGCZ_MOUSE Zeta-sarcoglycan (Zeta-SG) (ZSG1) 311 34,461 Alternative sequence (1); Chain (1); Disulfide bond (1); Glycosylation (2); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 51 71 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 50 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 72 311 Extracellular. {ECO:0000255}. FUNCTION: Component of the sarcoglycan complex, a subcomplex of the dystrophin-glycoprotein complex which forms a link between the F-actin cytoskeleton and the extracellular matrix. May play a role in the maintenance of striated muscle membrane stability. SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the heart, skeletal muscle and arterial vascular smooth muscle. +Q921I6 SH3B4_MOUSE SH3 domain-binding protein 4 962 107,584 Chain (1); Domain (3); Modified residue (6); Sequence conflict (3) FUNCTION: May function in transferrin receptor internalization at the plasma membrane through a cargo-specific control of clathrin-mediated endocytosis. Alternatively, may act as a negative regulator of the amino acid-induced TOR signaling by inhibiting the formation of active Rag GTPase complexes. Preferentially binds inactive Rag GTPase complexes and prevents their interaction with the mTORC1 complex inhibiting its relocalization to lysosomes and its activation. Thereby, may indirectly regulate cell growth, proliferation and autophagy (By similarity). {ECO:0000250}. PTM: Phosphorylated upon EGF stimulation. Phosphorylation prevents interaction with DNM2 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane, clathrin-coated pit {ECO:0000250}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250}. Nucleus {ECO:0000250}. Note=Specifically associated with transferrin receptor-containing clathrin-coated pits and clathrin-coated vesicles. May also localize to the nucleus (By similarity). {ECO:0000250}. SUBUNIT: Homodimer or homooligomer. Interacts with DNM2, EPS15, clathrin, the adapter protein complex 2/AP-2 and TFRC. Interacts with the Rag GTPases RRAGA, RRAGB, RRAGC and RRAGD; the interaction is most probably direct, preferentially occurs with their inactive GDP-bound form and is negatively regulated by amino acids (By similarity). {ECO:0000250}. DOMAIN: The SH3 domain mediates localization to the clathrin-coated pits and vesicles. The SH3 domain mediates interaction with DNM2 and the cytoplasmic part of TFRC with a lower affinity. The SH3 domain also mediates interaction with RRAGB, RRAGC and is required for the negative regulation of mTORC1 (By similarity). {ECO:0000250}. +Q62420 SH3G2_MOUSE Endophilin-A1 (Endophilin-1) (SH3 domain protein 2A) (SH3 domain-containing GRB2-like protein 2) (SH3p4) 352 39,955 Beta strand (1); Chain (1); Coiled coil (1); Domain (2); Helix (7); Modified residue (2); Region (3); Sequence conflict (6); Turn (2) FUNCTION: Implicated in synaptic vesicle endocytosis. May recruit other proteins to membranes with high curvature. Required for BDNF-dependent dendrite outgrowth (PubMed:21849472). Cooperates with SH3GL2 to mediate BDNF-NTRK2 early endocytic trafficking and signaling from early endosomes (PubMed:21849472). {ECO:0000269|PubMed:10490020, ECO:0000269|PubMed:21849472}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O35179}. Membrane {ECO:0000250|UniProtKB:O35179}; Peripheral membrane protein {ECO:0000250|UniProtKB:O35179}. Early endosome {ECO:0000269|PubMed:21849472}. Note=Concentrated in presynaptic nerve terminals in neurons. {ECO:0000250|UniProtKB:O35179}. SUBUNIT: Monomer; in cytoplasm. Homodimer; when associated with membranes (By similarity). Interacts with SYNJ1 (By similarity). Interacts with DNM1 (PubMed:10490020). Interacts with MAP4K3; the interaction appears to regulate MAP4K3-mediated JNK activation (By similarity). Interacts with OPHN1 (PubMed:19481455). Interacts with PDCD6IP (By similarity). Interacts with BIN2 (By similarity). Interacts with ATX2 (PubMed:18602463). Interacts with ADAM9 and ADAM15 cytoplasmic tails (PubMed:10531379). Interacts with TMEM108 (PubMed:21849472). Interacts with ADGRB2 (PubMed:28891236). {ECO:0000250|UniProtKB:O35179, ECO:0000250|UniProtKB:Q99962, ECO:0000269|PubMed:10490020, ECO:0000269|PubMed:10531379, ECO:0000269|PubMed:18602463, ECO:0000269|PubMed:19481455, ECO:0000269|PubMed:21849472, ECO:0000269|PubMed:28891236}. DOMAIN: An N-terminal amphipathic helix, the BAR domain and a second amphipathic helix inserted into helix 1 of the BAR domain (N-BAR domain) induce membrane curvature and bind curved membranes (By similarity). The BAR domain dimer forms a rigid crescent shaped bundle of helices with the pair of second amphipathic helices protruding towards the membrane-binding surface. {ECO:0000250, ECO:0000269|PubMed:16023669}. +O08641 SH3Y1_MOUSE SH3 domain-containing YSC84-like protein 1 340 37,028 Alternative sequence (2); Chain (1); Domain (1); Sequence conflict (1) SUBUNIT: Interacts with SH3D19. {ECO:0000269|PubMed:12615363}. TISSUE SPECIFICITY: Expressed in skin, kidney, stomach, small intestine and colon. Highly expressed in the anagen hair follicle. In hair, it is expressed predominantly in the hair bulb, the hair shaft, inner root sheath, and outer root sheath in the lower half of the follicle. {ECO:0000269|PubMed:10771491}. +O88834 SHD_MOUSE SH2 domain-containing adapter protein D 343 38,481 Alternative sequence (1); Chain (1); Domain (1) FUNCTION: May function as an adapter protein. {ECO:0000269|PubMed:9315092}. PTM: Tyrosine phosphorylated by ABL. {ECO:0000269|PubMed:9315092}. TISSUE SPECIFICITY: Specifically expressed in brain. {ECO:0000269|PubMed:9315092}. +O35324 SH21B_MOUSE SH2 domain-containing protein 1B (EWS/FLI1-activated transcript 2) (EAT-2) 132 15,259 Beta strand (8); Chain (1); Domain (1); Helix (2); Modified residue (1); Mutagenesis (3); Sequence conflict (1) FUNCTION: Cytoplasmic adapter regulating receptors of the signaling lymphocytic activation molecule (SLAM) family such as CD84, SLAMF1, LY9 and CD244. In SLAM signaling seems to cooperate with SH2D1A/SAP. Plays a role in regulation of effector functions of natural killer (NK) cells by controlling signal transduction through CD244/2B4. However, conflicting results are reported which may reflect the use of different strain backgrounds. Proposed to act as an inhibitor of CD244-mediated NK cell function including cytotoxicity and IFN-gamma production, the latter found also by triggering KLRA4 and KLRK1 next to CD244 (PubMed:16127454). Seems to positively regulate CD244- and CD84-dependent NK cell functions implicating CD244-mediated phosphorylation of VAV1. Activation of SLAMF7-mediated NK cell function does not effect receptor tyrosine phosphorylation but distal signaling (PubMed:19151721, PubMed:20962259, PubMed:24687958). In the context of NK cell-mediated cytotoxicity does not enhance conjugate formation with target cells but stimulates polarization of the microtubule-organizing center and cytotoxic granules toward the NK cell synapse (PubMed:24687958). Negatively regulates CD40-induced cytokine production in dendritic cells downstream of SLAM family receptors probably by inducing activation of the PI3K pathway to inhibit p38 MAPK and JNK activation (PubMed:26432891). {ECO:0000250|UniProtKB:O14796, ECO:0000269|PubMed:16127454, ECO:0000269|PubMed:19151721, ECO:0000269|PubMed:20962259, ECO:0000269|PubMed:24687958, ECO:0000269|PubMed:26432891}. PTM: Phosphorylated on tyrosine residues; probably at Tyr-120 and/or Tyr-127. {ECO:0000269|PubMed:16127454}. SUBUNIT: Binds to the phosphorylated receptors CD84, SLAMF1, LY9 and CD244. Does not bind to non-phosphorylated SLAMF1 (By similarity). Interacts with SLAMF7 (via ITSM phosphorylated on 'Tyr-302'). Interacts with Src kinases HCK, LYN, FYN, FGR and LCK (via kinase domains). Interacts (phosphorylated at Tyr-127) with PLCG2. {ECO:0000250|UniProtKB:O14796, ECO:0000269|PubMed:11689425, ECO:0000269|PubMed:16425036, ECO:0000269|PubMed:19151721, ECO:0000269|PubMed:24687958, ECO:0000305|PubMed:21219180}. TISSUE SPECIFICITY: Expressed in spleen, thymus, lung, kidney, heart, colon and small bowel. Expressed in NK cells (all stages of cell maturation), macrophages and dendritic cells. {ECO:0000269|PubMed:16127454, ECO:0000269|PubMed:16425036, ECO:0000269|PubMed:24687958}. +Q9D7V1 SH24A_MOUSE SH2 domain-containing protein 4A 421 48,460 Chain (1); Domain (1); Modified residue (3); Sequence conflict (1) FUNCTION: Inhibits estrogen-induced cell proliferation by competing with PLCG for binding to ESR1, blocking the effect of estrogen on PLCG and repressing estrogen-induced proliferation (By similarity). May play a role in T-cell development and function. {ECO:0000250, ECO:0000269|PubMed:18641339}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17251388}. Note=Located at podocyte foot processes. SUBUNIT: Interacts with ESR1. {ECO:0000250}. TISSUE SPECIFICITY: In the kidney, expressed only in the glomerulus. Expressed in T-cells, B-cells, macrophages and dendritic cells (at protein level). In adult, highest levels are found in muscle and lung with lower levels in kidney. {ECO:0000269|PubMed:17251388, ECO:0000269|PubMed:18641339}. +A6X942 SH24B_MOUSE SH2 domain-containing protein 4B 431 51,120 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (1) +A2A9G7 SHL2A_MOUSE Protein shisa-like-2A 189 20,106 Chain (1); Transmembrane (2) TRANSMEM 48 68 Helical. {ECO:0000255}.; TRANSMEM 70 90 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q91WA6 SHRPN_MOUSE Sharpin (Shank-associated RH domain-interacting protein) (Shank-interacting protein-like 1) (mSIPL1) 380 39,852 Alternative sequence (1); Beta strand (5); Chain (1); Domain (1); Helix (6); Modified residue (2); Region (2); Sequence conflict (1); Zinc finger (1) FUNCTION: Component of the LUBAC complex which conjugates linear polyubiquitin chains in a head-to-tail manner to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation. LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways. Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation. LUBAC is recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex. Together with OTULIN, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis. {ECO:0000269|PubMed:17538631, ECO:0000269|PubMed:21455173, ECO:0000269|PubMed:21455180, ECO:0000269|PubMed:21455181}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9H0F6}. Cell junction, synapse {ECO:0000250|UniProtKB:Q9EQL9}. Note=Enriched at synaptic sites in mature neurons where it colocalizes with SHANK1. {ECO:0000250|UniProtKB:Q9EQL9}. SUBUNIT: Monomer and homodimer (By similarity). Component of the LUBAC complex (linear ubiquitin chain assembly complex) which consists of SHARPIN, RBCK1 and RNF31 (By similarity). LUBAC has a MW of approximately 600 kDa suggesting a heteromultimeric assembly of its subunits (By similarity). Associates with the TNF-R1 signaling complex (TNF-RSC) in a stimulation-dependent manner (By similarity). Interacts with EYA1, EYA2, SHANK1 and SHANK3 (via ANK repeats) (PubMed:20956555). {ECO:0000250|UniProtKB:Q9EQL9, ECO:0000250|UniProtKB:Q9H0F6, ECO:0000269|PubMed:20956555}. DOMAIN: The Ubiquitin-like domain is required for the interaction with RNF31. {ECO:0000250|UniProtKB:Q9H0F6}.; DOMAIN: The RanBP2-type zinc fingers mediate the specific interaction with ubiquitin. Binds preferentially linear polyubiquitin chains and 'Lys-63'-linked polyubiquitin chains over 'Lys-48'-linked polyubiquitin chains. Also binds monoubiquitin (By similarity). {ECO:0000250|UniProtKB:Q9H0F6}. TISSUE SPECIFICITY: Highly expressed in thymus and spleen. Present at high level in splenic B- and T-cells (at protein level). {ECO:0000269|PubMed:21455180}. DISEASE: Note=Defects in Sharpin are the cause of chronic proliferative dermatitis (cpdm). Cpdm is a spontaneous mutation causing a chronic proliferative dermatitis phenotype, which is characterized histologically by severe inflammation, eosinophilic dermatitis and defects in secondary lymphoid organ development. Mice also display lower total and cortical bone mineral content and bone mineral density, trabecular and cortical bone volume, and trabecular number. TNF-alpha-induced NF-kappa-B activation is attenuated due to inability of the LUBAC complex to mediate linear ubiquitination. {ECO:0000269|PubMed:17538631, ECO:0000269|PubMed:19650867, ECO:0000269|PubMed:20811394, ECO:0000269|PubMed:21069580, ECO:0000269|PubMed:21455173, ECO:0000269|PubMed:21455180, ECO:0000269|PubMed:21455181}. +O09039 SH2B3_MOUSE SH2B adapter protein 3 (Lymphocyte adapter protein) (Lymphocyte-specific adapter protein Lnk) (Signal transduction protein Lnk) 548 60,487 Chain (1); Domain (2); Modified residue (4) FUNCTION: Links T-cell receptor activation signal to phospholipase C-gamma-1, GRB2 and phosphatidylinositol 3-kinase. {ECO:0000250}. PTM: Tyrosine phosphorylated. {ECO:0000250}. +Q8VIB3 SIA10_MOUSE Type 2 lactosamine alpha-2,3-sialyltransferase (EC 2.4.99.-) (CMP-NeuAc:beta-galactoside alpha-2,3-sialyltransferase VI) (ST3Gal VI) (ST3GalVI) (Sialyltransferase 10) 329 37,854 Chain (1); Glycosylation (4); Sequence conflict (4); Topological domain (2); Transmembrane (1) TRANSMEM 5 25 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 4 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 26 329 Lumenal. {ECO:0000255}. FUNCTION: Involved in the synthesis of sialyl-paragloboside, a precursor of sialyl-Lewis X determinant. Has a alpha-2,3-sialyltransferase activity toward Gal-beta1,4-GlcNAc structure on glycoproteins and glycolipids. Has a restricted substrate specificity, it utilizes Gal-beta1,4-GlcNAc on glycoproteins, and neolactotetraosylceramide and neolactohexaosylceramide, but not lactotetraosylceramide, lactosylceramide or asialo-GM1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. +Q6PD21 SHB_MOUSE SH2 domain-containing adapter protein B 503 54,708 Alternative sequence (3); Chain (1); Cross-link (1); Domain (1); Erroneous initiation (1); Modified residue (4) FUNCTION: Adapter protein which regulates several signal transduction cascades by linking activated receptors to downstream signaling components. May play a role in angiogenesis by regulating FGFR1, VEGFR2 and PDGFR signaling. May also play a role in T-cell antigen receptor/TCR signaling, interleukin-2 signaling, apoptosis and neuronal cells differentiation by mediating basic-FGF and NGF-induced signaling cascades. May also regulate IRS1 and IRS2 signaling in insulin-producing cells (By similarity). {ECO:0000250}. PTM: Phosphorylated upon PDGFRA, PDGFRB, TCR, IL2 receptor, FGFR1 or VEGFR2 activation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Associates with membrane lipid rafts upon TCR stimulation. {ECO:0000250}. SUBUNIT: Interacts with phosphorylated 'Tyr-720' of the ligand-activated receptor PDGFRA via its SH2 domain. Interacts with the ligand-activated receptors PDGFRB, FGFR1, KDR/VEGFR2, IL2RB and IL2RG. Interacts with EPS8 and V-SRC. Interacts with GRB2 and GRAP. Interacts with CD3Z. Interacts with tyrosine-phosphorylated LAT upon T-cell antigen receptor activation. Interacts with PLCG1. Interacts with ZAP70, LCP2/SLP-76, VAV1 and GRAP2. Interacts with JAK1 and JAK3. Interacts with PTK2/FAK1. Interacts with CRK/CrKII. Interacts with IRS2 (By similarity). Interacts with PTPN11. {ECO:0000250, ECO:0000269|PubMed:12181353}. DOMAIN: The SH2 domain preferentially binds phosphopeptides with the consensus sequence Y-[TVI]-X-L and mediates interaction with PDGFRA, PDGFRB, FGRFR1, IL2RB, IL2RG, CD3Z and CRK/CrKII. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in heart, liver, brain and kidney (at protein level). {ECO:0000269|PubMed:8302579}. +Q91Y74 SIA4C_MOUSE CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 4 (Alpha 2,3-ST 4) (Beta-galactoside alpha-2,3-sialyltransferase 4) (EC 2.4.99.2) (EC 2.4.99.6) (Alpha 2,3-sialyltransferase IV) (Gal-beta-1,4-GalNAc-alpha-2,3-sialyltransferase) (ST3Gal IV) (ST3GalIV) (Sialyltransferase 4C) (SIAT4-C) 333 38,058 Chain (1); Disulfide bond (1); Glycosylation (4); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 9 26 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 8 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 27 333 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Catalyzes the formation of the NeuAc-alpha-2,3-Gal-beta-1,4-GlcNAc-, and NeuAc-alpha-2,3-Gal-beta-1,3-GlcNAc- sequences found in terminal carbohydrate groups of glycoproteins and glycolipids. {ECO:0000269|PubMed:9184827}. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Membrane-bound form in trans cisternae of Golgi. {ECO:0000250}. TISSUE SPECIFICITY: Found in high levels in all tissues tested. {ECO:0000269|PubMed:9184827}. +Q8VDQ8 SIR2_MOUSE NAD-dependent protein deacetylase sirtuin-2 (EC 3.5.1.-) (Regulatory protein SIR2 homolog 2) (SIR2-like protein 2) (mSIR2L2) 389 43,256 Active site (1); Alternative sequence (3); Binding site (1); Chain (1); Domain (1); Initiator methionine (1); Metal binding (4); Modified residue (8); Motif (1); Mutagenesis (1); Nucleotide binding (5); Region (2); Sequence conflict (2) FUNCTION: NAD-dependent protein deacetylase, which deacetylates internal lysines on histone and alpha-tubulin as well as many other proteins such as key transcription factors (PubMed:17521387, PubMed:17681146, PubMed:17574768, PubMed:19037106, PubMed:22014574, PubMed:21791548, PubMed:21841822, PubMed:24334550). Participates in the modulation of multiple and diverse biological processes such as cell cycle control, genomic integrity, microtubule dynamics, cell differentiation, metabolic networks, and autophagy. Plays a major role in the control of cell cycle progression and genomic stability. Functions in the antephase checkpoint preventing precocious mitotic entry in response to microtubule stress agents, and hence allowing proper inheritance of chromosomes. Positively regulates the anaphase promoting complex/cyclosome (APC/C) ubiquitin ligase complex activity by deacetylating CDC20 and FZR1, then allowing progression through mitosis. Associates both with chromatin at transcriptional start sites (TSSs) and enhancers of active genes. Plays a role in cell cycle and chromatin compaction through epigenetic modulation of the regulation of histone H4 'Lys-20' methylation (H4K20me1) during early mitosis. Specifically deacetylates histone H4 at 'Lys-16' (H4K16ac) between the G2/M transition and metaphase enabling H4K20me1 deposition by KMT5A leading to ulterior levels of H4K20me2 and H4K20me3 deposition throughout cell cycle, and mitotic S-phase progression. Deacetylates KMT5A modulating KMT5A chromatin localization during the mitotic stress response. Deacetylates also histone H3 at 'Lys-57' (H3K56ac) during the mitotic G2/M transition. During oocyte meiosis progression, may deacetylate histone H4 at 'Lys-16' (H4K16ac) and alpha-tubulin, regulating spindle assembly and chromosome alignment by influencing microtubule dynamics and kinetochore function. Deacetylates histone H4 at 'Lys-16' (H4K16ac) at the VEGFA promoter and thereby contributes to regulate expression of VEGFA, a key regulator of angiogenesis. Deacetylates alpha-tubulin at 'Lys-40' and hence controls neuronal motility, oligodendroglial cell arbor projection processes and proliferation of non-neuronal cells. Phosphorylation at Ser-368 by a G1/S-specific cyclin E-CDK2 complex inactivates SIRT2-mediated alpha-tubulin deacetylation, negatively regulating cell adhesion, cell migration and neurite outgrowth during neuronal differentiation. Deacetylates PARD3 and participates in the regulation of Schwann cell peripheral myelination formation during early postnatal development and during postinjury remyelination. Involved in several cellular metabolic pathways. Plays a role in the regulation of blood glucose homeostasis by deacetylating and stabilizing phosphoenolpyruvate carboxykinase PCK1 activity in response to low nutrient availability. Acts as a key regulator in the pentose phosphate pathway (PPP) by deacetylating and activating the glucose-6-phosphate G6PD enzyme, and therefore, stimulates the production of cytosolic NADPH to counteract oxidative damage. Maintains energy homeostasis in response to nutrient deprivation as well as energy expenditure by inhibiting adipogenesis and promoting lipolysis. Attenuates adipocyte differentiation by deacetylating and promoting FOXO1 interaction to PPARG and subsequent repression of PPARG-dependent transcriptional activity. Plays a role in the regulation of lysosome-mediated degradation of protein aggregates by autophagy in neuronal cells. Deacetylates FOXO1 in response to oxidative stress or serum deprivation, thereby negatively regulating FOXO1-mediated autophagy (By similarity). Deacetylates a broad range of transcription factors and co-regulators regulating target gene expression. Deacetylates transcriptional factor FOXO3 stimulating the ubiquitin ligase SCF(SKP2)-mediated FOXO3 ubiquitination and degradation (By similarity). Deacetylates HIF1A and therefore promotes HIF1A degradation and inhibition of HIF1A transcriptional activity in tumor cells in response to hypoxia. Deacetylates RELA in the cytoplasm inhibiting NF-kappaB-dependent transcription activation upon TNF-alpha stimulation. Inhibits transcriptional activation by deacetylating p53/TP53 and EP300. Deacetylates also EIF5A. Functions as a negative regulator on oxidative stress-tolerance in response to anoxia-reoxygenation conditions. Plays a role as tumor suppressor (PubMed:22014574, PubMed:23468428). {ECO:0000250|UniProtKB:Q8IXJ6, ECO:0000269|PubMed:17521387, ECO:0000269|PubMed:17574768, ECO:0000269|PubMed:17681146, ECO:0000269|PubMed:19037106, ECO:0000269|PubMed:21791548, ECO:0000269|PubMed:21841822, ECO:0000269|PubMed:21949390, ECO:0000269|PubMed:22014574, ECO:0000269|PubMed:23468428, ECO:0000269|PubMed:24334550}.; FUNCTION: Isoform 1: Deacetylates alpha-tubulin.; FUNCTION: Isoform 2: Deacetylates alpha-tubulin.; FUNCTION: Isoform 4: Deacetylates alpha-tubulin. PTM: Phosphorylated at phosphoserine and phosphothreonine. Phosphorylated at Ser-368 by a mitotic kinase CDK1/cyclin B at the G2/M transition; phosphorylation regulates the delay in cell-cycle progression. Phosphorylated at Ser-368 by a mitotic kinase G1/S-specific cyclin E/Cdk2 complex; phosphorylation inactivates SIRT2-mediated alpha-tubulin deacetylation and thereby negatively regulates cell adhesion, cell migration and neurite outgrowth during neuronal differentiation. Phosphorylated by cyclin A/Cdk2 and p35-Cdk5 complexes and to a lesser extent by the cyclin D3/Cdk4 and cyclin B/Cdk1, in vitro. Dephosphorylated at Ser-368 by CDC14A and CDC14B around early anaphase (By similarity). {ECO:0000250|UniProtKB:Q8IXJ6}.; PTM: Acetylated by EP300; acetylation leads both to the decreased of SIRT2-mediated alpha-tubulin deacetylase activity and SIRT2-mediated down-regulation of TP53 transcriptional activity. {ECO:0000250|UniProtKB:Q8IXJ6}.; PTM: Ubiquitinated. {ECO:0000250|UniProtKB:Q8IXJ6}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24460154}. Cytoplasm {ECO:0000269|PubMed:11056054, ECO:0000269|PubMed:24460154}. Cytoplasm, perinuclear region. Perikaryon. Cytoplasm, cytoskeleton. Cell projection. Cell projection, growth cone. Myelin membrane. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle. Chromosome. Midbody. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250}. Note=Localizes in the cytoplasm during most of the cell cycle except in the G2/M transition and during mitosis, where it is localized in association with chromatin and induces deacetylation of histone at 'Lys-16' (H4K16ac). Colocalizes with CDK1 at centrosome during prophase and splindle fibers during metaphase. Colocalizes with Aurora kinase AURKA in centrioles during early prophase and growing mitotic spindle throughout metaphase. Colocalizes with Aurora kinase AURKB during cytokinesis with the midbody. Detected in perinuclear foci that may be aggresomes containing misfolded, ubiquitinated proteins. Shuttles between the cytoplasm and the nucleus through the CRM1 export pathway. Colocalizes with EP300 in the nucleus. Colocalizes with PARD3 in internodal region of axons. Colocalizes with acetylated alpha-tubulin in cell projection processes during primary oligodendrocyte precursor (OLP) differentiation (By similarity). Deacetylates FOXO3 in the cytoplasm. Colocalizes with Aurora kinase AURKA at centrosome. Colocalizes with microtubules. Colocalizes with PLP1 in internodal regions of myelin sheat, at paranodal axoglial junction and Schmidt-Lanterman incisures. Colocalizes with CDK5R1 in the perikaryon, neurites and growth cone of hippocampal neurons. Colocalizes with alpha-tubulin in neuronal growth cone. Colocalizes with KMT5A at mitotic foci. Localizes in the cytoplasm and nucleus of germinal vesicle (GV) stage oocytes. Colocalizes with alpha-tubulin on the meiotic spindle as the oocytes enter into metaphase, and also during meiotic anaphase and telophase, especially with the midbody. {ECO:0000250}. SUBUNIT: Interacts with CDC20, FOXO3 and FZR1 (PubMed:17521387, PubMed:22014574). Associates with microtubule in primary cortical mature neurons (By similarity). Homotrimer. Interacts (via both phosphorylated, unphosphorylated, active or inactive forms) with HDAC6; the interaction is necessary for the complex to interact with alpha-tubulin, suggesting that these proteins belong to a large complex that deacetylates the cytoskeleton. Interacts with FOXO1; the interaction is disrupted upon serum-starvation or oxidative stress, leading to increased level of acetylated FOXO1 and induction of autophagy (PubMed:17681146, PubMed:19037106). Interacts with RELA; the interaction occurs in the cytoplasm and is increased in a TNF-alpha-dependent manner. Interacts with HOXA10; the interaction is direct. Interacts with YWHAB and YWHAG; the interactions occur in a AKT-dependent manner and increase SIRT2-dependent TP53 deacetylation. Interacts with MAPK1/ERK2 and MAPK3/ERK1; the interactions increase SIRT2 stability and deacetylation activity. Interacts (phosphorylated form) with KMT5A isoform 2; the interaction is direct, stimulates KMT5A-mediated methyltransferase activity on histone at 'Lys-20' (H4K20me1) and is increased in a H(2)O(2)-induced oxidative stress-dependent manner. Interacts with G6PD; the interaction is enhanced by H(2)O(2) treatment. Interacts with a G1/S-specific cyclin E-CDK2 complex. Interacts with AURKA, CDK5R1 (p35 form) and CDK5 and HIF1A. Interacts with the tRNA ligase SARS; recruited to the VEGFA promoter via interaction with SARS (By similarity). Isoform 2 and isoform 4 associate with microtubules in primary cortical mature neurons. Interacts with BEX4; negatively regulates alpha-tubulin deacetylation by SIRT2 (By similarity). {ECO:0000250|UniProtKB:Q8IXJ6, ECO:0000269|PubMed:17521387, ECO:0000269|PubMed:17681146, ECO:0000269|PubMed:18332217, ECO:0000269|PubMed:19037106, ECO:0000269|PubMed:22014574}. TISSUE SPECIFICITY: Isoform 1 is weakly expressed in the cortex at postnatal(P) days P1, P3 and P7, and increases progressively between P17 and older adult cortex. Isoform 1 is also expressed in heart, liver and skeletal muscle, weakly expressed in the striatum and spinal cord. Isoform 2 is not expressed in the cortex at P1, P3 and P7, and increases strongly and progressively between P17 and older adult cortex. Isoform 2 is also expressed in the heart, liver, striatum and spinal cord. Isoform 4 is weakly expressed in older adult cortex and spinal cords. Expressed in the cortex. Expressed in postnatal sciatic nerves during myelination and during remyelination after nerve injury. Expressed in neurons, oligodendrocytes, Schwann cells, Purkinje cells and in astrocytes of white matter. Strongly expressed in preadipocytes compared with differentiated adipocytes. Expressed in cerebellar granule cells. Expressed in the inner ear: in the cochlea, expressed in types I and V fibrocytes in the spiral ligament (SL) and slightly in stria vascularis (SV); in the organ of Corti, expressed in some supporting cells; in the crista ampullaris, expressed in spiral ganglion cells; also expressed in the endolymphatic sac (ES) epithelial cells (at protein level). Expressed in the brain, spinal cord, optic nerve and hippocampus. Strongly expressed in 6-8 week-old ovulated meiosis II oocytes and weakly expressed in 45-58 week-old ovulated meiosis II oocytes. Expressed in the cochlea, vestibule and acoustic nerve of the inner ear. {ECO:0000269|PubMed:16933150, ECO:0000269|PubMed:17634366, ECO:0000269|PubMed:17681146, ECO:0000269|PubMed:18332217, ECO:0000269|PubMed:21791548, ECO:0000269|PubMed:21949390, ECO:0000269|PubMed:24334550, ECO:0000269|PubMed:24460154}. +Q921L3 TMCO1_MOUSE Calcium load-activated calcium channel (CLAC channel) (Transmembrane and coiled-coil domain-containing protein 1) 188 21,175 Chain (1); Coiled coil (1); Compositional bias (1); Intramembrane (1); Modified residue (2); Topological domain (4); Transmembrane (2) INTRAMEM 138 154 Pore-forming. {ECO:0000250|UniProtKB:Q9UM00}. TRANSMEM 10 30 Helical. {ECO:0000255}.; TRANSMEM 91 111 Helical. {ECO:0000255}. TOPO_DOM 1 9 Cytoplasmic. {ECO:0000250|UniProtKB:Q9UM00}.; TOPO_DOM 31 90 Lumenal. {ECO:0000250|UniProtKB:Q9UM00}.; TOPO_DOM 112 137 Cytoplasmic. {ECO:0000250|UniProtKB:Q9UM00}.; TOPO_DOM 155 188 Cytoplasmic. {ECO:0000250|UniProtKB:Q9UM00}. FUNCTION: Calcium-selective channel required to prevent calcium stores from overfilling, thereby playing a key role in calcium homeostasis (PubMed:27212239). In response to endoplasmic reticulum overloading, assembles into a homotetramer, forming a functional calcium-selective channel, regulating the calcium content in endoplasmic reticulum store (PubMed:27212239). {ECO:0000269|PubMed:27212239}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9UM00}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9UM00}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9UM00}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9UM00}. Note=The first transmembrane region is required for localization to the endoplasmic reticulum. {ECO:0000250|UniProtKB:Q9UM00}. SUBUNIT: Homodimer and homotetramer. Homodimer under resting conditions; forms homotetramers following and endoplasmic reticulum calcium overload. {ECO:0000250|UniProtKB:Q9UM00, ECO:0000269|PubMed:27212239}. +P97801 SMN_MOUSE Survival motor neuron protein 288 31,254 Chain (1); Compositional bias (3); Cross-link (2); Domain (1); Modified residue (5); Mutagenesis (5); Region (4) FUNCTION: The SMN complex plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus. Ensures the correct splicing of U12 intron-containing genes that may be important for normal motor and proprioceptive neurons development. Also required for resolving RNA-DNA hybrids created by RNA polymerase II, that form R-loop in transcription terminal regions, an important step in proper transcription termination. May also play a role in the metabolism of small nucleolar ribonucleoprotein (snoRNPs). {ECO:0000250|UniProtKB:Q16637, ECO:0000269|PubMed:23063131}. SUBCELLULAR LOCATION: Nucleus, gem {ECO:0000250|UniProtKB:Q16637}. Nucleus, Cajal body {ECO:0000250|UniProtKB:Q16637}. Cytoplasm {ECO:0000250|UniProtKB:Q16637}. Cytoplasmic granule {ECO:0000250|UniProtKB:Q16637}. Perikaryon {ECO:0000250|UniProtKB:Q16637}. Cell projection {ECO:0000250|UniProtKB:Q16637}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:17353360}. Note=Colocalizes with actin and at the Z-line of skeletal muscle (PubMed:17353360). Under stress conditions colocalizes with RPP20/POP7 in punctuated cytoplasmic granules. Colocalized and redistributed with ZPR1 from the cytoplasm to nuclear gems (Gemini of coiled bodies) and Cajal bodies. Colocalizes with FMR1 in cytoplasmic granules in the soma and neurite cell processes (By similarity). {ECO:0000250|UniProtKB:Q16637}. SUBUNIT: Homodimer (By similarity). Part of the core SMN complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8 and STRAP/UNRIP (By similarity). Part of the SMN-Sm complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8, STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG (By similarity). Component of an import snRNP complex composed of KPNB1, RNUT1, SMN1 and ZNF259 (By similarity). Interacts with DDX20, FBL, NOLA1, RNUT1 and with several spliceosomal snRNP core Sm proteins, including SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE and ILF3 (By similarity). Interacts with OSTF1, LSM10, LSM11 and RPP20/POP7 (By similarity). Interacts (via C-terminal region) with ZPR1 (via C-terminal region) (By similarity). Interacts (via Tudor domain) with COIL (By similarity). Interacts with SETX; recruits SETX to POLR2A (By similarity). Interacts with POLR2A (via the C-terminal domain (CTD)) (By similarity). Interacts with PRMT5 (By similarity). Interacts with XRN2 (By similarity). Interacts (via C-terminus) with FMR1 (via C-terminus); the interaction is direct and occurs in a RNA-independent manner (By similarity). Interacts with SYNCRIP (PubMed:11773003). Interacts (via Tudor domain) with SF3B2 ('Arg-491'-methylated form) (By similarity). Interacts with WRAP53/TCAB1 (By similarity). {ECO:0000250|UniProtKB:Q16637, ECO:0000269|PubMed:11773003}. DOMAIN: The Tudor domain mediates association with dimethylarginines, which are common in snRNP proteins. {ECO:0000250}. +Q8BUN5 SMAD3_MOUSE Mothers against decapentaplegic homolog 3 (MAD homolog 3) (Mad3) (Mothers against DPP homolog 3) (mMad3) (SMAD family member 3) (SMAD 3) (Smad3) 425 48,081 Chain (1); Cross-link (2); Domain (2); Initiator methionine (1); Metal binding (4); Modified residue (12); Region (2); Sequence conflict (3); Site (2) FUNCTION: Receptor-regulated SMAD (R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta (transforming growth factor) and activin type 1 receptor kinases. Binds the TRE element in the promoter region of many genes that are regulated by TGF-beta and, on formation of the SMAD3/SMAD4 complex, activates transcription. Also can form a SMAD3/SMAD4/JUN/FOS complex at the AP-1/SMAD site to regulate TGF-beta-mediated transcription. Has an inhibitory effect on wound healing probably by modulating both growth and migration of primary keratinocytes and by altering the TGF-mediated chemotaxis of monocytes. This effect on wound healing appears to be hormone-sensitive. Regulator of chondrogenesis and osteogenesis and inhibits early healing of bone fractures. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator (By similarity). {ECO:0000250|UniProtKB:P84022, ECO:0000269|PubMed:10559937, ECO:0000269|PubMed:11585338, ECO:0000269|PubMed:14617288, ECO:0000269|PubMed:15356634, ECO:0000269|PubMed:21035443}. PTM: Phosphorylated on serine and threonine residues. Enhanced phosphorylation in the linker region on Thr-179, Ser-204 and Ser-208 on EGF and TGF-beta treatment. Ser-208 is the main site of MAPK-mediated phosphorylation. CDK-mediated phosphorylation occurs in a cell-cycle dependent manner and inhibits both the transcriptional activity and antiproliferative functions of SMAD3. This phosphorylation is inhibited by flavopiridol. Maximum phosphorylation at the G(1)/S junction. Also phosphorylated on serine residues in the C-terminal SXS motif by TGFBR1 and ACVR1. TGFBR1-mediated phosphorylation at these C-terminal sites is required for interaction with SMAD4, nuclear location and transactivational activity, and appears to be a prerequisite for the TGF-beta mediated phosphorylation in the linker region. Dephosphorylated in the C-terminal SXS motif by PPM1A. This dephosphorylation disrupts the interaction with SMAD4, promotes nuclear export and terminates TGF-beta-mediated signaling. Phosphorylation at Ser-418 by CSNK1G2/CK1 promotes ligand-dependent ubiquitination and subsequent proteasome degradation, thus inhibiting SMAD3-mediated TGF-beta responses (By similarity). Phosphorylated by PDPK1 (By similarity). {ECO:0000250|UniProtKB:P84022}.; PTM: Acetylation in the nucleus by EP300 in the MH2 domain regulates positively its transcriptional activity and is enhanced by TGF-beta. {ECO:0000250|UniProtKB:P84022}.; PTM: Ubiquitinated. Monoubiquitinated, leading to prevent DNA-binding. Deubiquitination by USP15 alleviates inhibition and promotes activation of TGF-beta target genes (By similarity). Ubiquitinated by RNF111, leading to its degradation: only SMAD3 proteins that are 'in use' are targeted by RNF111, RNF111 playing a key role in activating SMAD3 and regulating its turnover (PubMed:17341133). Undergoes STUB1-mediated ubiquitination and degradation (By similarity). {ECO:0000250|UniProtKB:P84022, ECO:0000269|PubMed:17341133}.; PTM: Poly-ADP-ribosylated by PARP1 and PARP2. ADP-ribosylation negatively regulates SMAD3 transcriptional responses during the course of TGF-beta signaling. {ECO:0000250|UniProtKB:P84022}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15356634, ECO:0000269|PubMed:22781750}. Nucleus {ECO:0000269|PubMed:15356634, ECO:0000269|PubMed:22781750}. Note=Cytoplasmic and nuclear in the absence of TGF-beta. On TGF-beta stimulation, migrates to the nucleus when complexed with SMAD4. Through the action of the phosphatase PPM1A, released from the SMAD2/SMAD4 complex, and exported out of the nucleus by interaction with RANBP1. Co-localizes with LEMD3 at the nucleus inner membrane. MAPK-mediated phosphorylation appears to have no effect on nuclear import. PDPK1 prevents its nuclear translocation in response to TGF-beta. {ECO:0000250|UniProtKB:P84022}. SUBUNIT: Monomer; in the absence of TGF-beta. Homooligomer; in the presence of TGF-beta. Heterotrimer; forms a heterotrimer in the presence of TGF-beta consisting of two molecules of C-terminally phosphorylated SMAD2 or SMAD3 and one of SMAD4 to form the transcriptionally active SMAD2/SMAD3-SMAD4 complex. Interacts with TGFBR1. Interacts (via MH2 domain) with CITED2 (via C-terminus). Interacts (via the MH2 domain) with ZFYVE9. Interacts with HDAC1, TGIF and TGIF2, RUNX3, CREBBP, SKOR1, SKOR2, SNON, ATF2, SMURF2 and SNW1. Interacts with DACH1; the interaction inhibits the TGF-beta signaling. Part of a complex consisting of AIP1, ACVR2A, ACVR1B and SMAD3. Forms a complex with SMAD2 and TRIM33 upon addition of TGF-beta. Found in a complex with SMAD3, RAN and XPO4. Interacts in the complex directly with XPO4. Interacts (via the MH2 domain) with LEMD3; the interaction represses SMAD3 transcriptional activity through preventing the formation of the heteromeric complex with SMAD4 and translocation to the nucleus. Interacts with RBPMS. Interacts (via MH2 domain) with MECOM. Interacts with WWTR1 (via its coiled-coil domain). Interacts (via the linker region) with EP300 (C-terminal); the interaction promotes SMAD3 acetylation and is enhanced by TGF-beta phosphorylation in the C-terminal of SMAD3. This interaction can be blocked by competitive binding of adenovirus oncoprotein E1A to the same C-terminal site on EP300, which then results in partially inhibited SMAD3/SMAD4 transcriptional activity. Interacts with SKI; the interaction represses SMAD3 transcriptional activity. Component of the multimeric complex SMAD3/SMAD4/JUN/FOS which forms at the AP1 promoter site; required for synergistic transcriptional activity in response to TGF-beta. Interacts (via an N-terminal domain) with JUN (via its basic DNA binding and leucine zipper domains); this interaction is essential for DNA binding and cooperative transcriptional activity in response to TGF-beta. Interacts with PPM1A; the interaction dephosphorylates SMAD3 in the C-terminal SXS motif leading to disruption of the SMAD2/3-SMAD4 complex, nuclear export and termination of TGF-beta signaling. Interacts (dephosphorylated form via the MH1 and MH2 domains) with RANBP3 (via its C-terminal R domain); the interaction results in the export of dephosphorylated SMAD3 out of the nucleus and termination of the TGF-beta signaling. Interacts with AIP1, TGFB1I1, TTRAP, FOXL2, PRDM16, HGS and WWP1. Interacts with NEDD4L; the interaction requires TGF-beta stimulation. Interacts with PML. Interacts with MEN1. Interaction with CSNK1G2. Interacts with PDPK1 (via PH domain). Interacts with DAB2; the interactions are enhanced upon TGF-beta stimulation. Interacts with USP15. Interacts with PPP5C; the interaction decreases SMAD3 phosphorylation and protein levels. Interacts with LDLRAD4 (via the SMAD interaction motif). Interacts with PMEPA1. Interacts with ZC3H3 (PubMed:16115198). Interacts with ZFHX3 (By similarity). Interacts with ZNF451. Identified in a complex that contains at least ZNF451, SMAD2, SMAD3 and SMAD4 (By similarity). Interacts weakly with ZNF8 (PubMed:12370310). Interacts (when phosphorylated) with RNF111; RNF111 acts as an enhancer of the transcriptional responses by mediating ubiquitination and degradation of SMAD3 inhibitors (PubMed:17341133). Interacts with STUB1, HSPA1A, HSPA1B, HSP90AA1 and HSP90AB1 (By similarity). {ECO:0000250|UniProtKB:P84022, ECO:0000269|PubMed:10681527, ECO:0000269|PubMed:11094085, ECO:0000269|PubMed:12370310, ECO:0000269|PubMed:14755691, ECO:0000269|PubMed:15221015, ECO:0000269|PubMed:15356634, ECO:0000269|PubMed:15496141, ECO:0000269|PubMed:16115198, ECO:0000269|PubMed:17341133, ECO:0000269|PubMed:17467076, ECO:0000269|PubMed:18039968, ECO:0000269|PubMed:19106105, ECO:0000269|PubMed:22781750}. DOMAIN: The MH1 domain is required for DNA binding (By similarity). Also binds zinc ions which are necessary for the DNA binding. {ECO:0000250}.; DOMAIN: The MH2 domain is required for both homomeric and heteromeric interactions and for transcriptional regulation. Sufficient for nuclear import (By similarity). {ECO:0000250}.; DOMAIN: The linker region is required for the TGFbeta-mediated transcriptional activity and acts synergistically with the MH2 domain. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in the brain and ovary. Detected in the pyramidal cells of the hippocampus, granule cells of the dentate gyrus, granular cells of the cerebral cortex and the granulosa cells of the ovary. {ECO:0000269|PubMed:10331191}. +Q9QYZ6 SMK2A_MOUSE Sperm motility kinase 2A (EC 2.7.11.1) 504 56,787 Active site (1); Binding site (1); Chain (1); Domain (2); Nucleotide binding (1) FUNCTION: May play a role in sperm motility, especially in the regulation of flagellar function. {ECO:0000269|PubMed:10647005}. TISSUE SPECIFICITY: Testis-specific. Expressed in the testis from 22 days postpartum (22 dpp). {ECO:0000269|PubMed:10647005}. +Q8VE22 RT23_MOUSE 28S ribosomal protein S23, mitochondrial (MRP-S23) (S23mt) 177 20,348 Chain (1); Initiator methionine (1); Modified residue (3) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q2NL27}. SUBUNIT: Component of the mitochondrial ribosome small subunit (28S) which comprises a 12S rRNA and about 30 distinct proteins. {ECO:0000250|UniProtKB:Q2NL27}. +Q8K0T0 RTN1_MOUSE Reticulon-1 (Neuroendocrine-specific protein) 780 83,572 Chain (1); Domain (1); Modified residue (6); Sequence conflict (2); Transmembrane (2) TRANSMEM 607 627 Helical. {ECO:0000255}.; TRANSMEM 709 729 Helical. {ECO:0000255}. FUNCTION: May be involved in neuroendocrine secretion or in membrane trafficking in neuroendocrine cells. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12036513}; Multi-pass membrane protein {ECO:0000269|PubMed:12036513}. SUBUNIT: Interacts with NDRG1. Interacts with TMEM33. {ECO:0000250|UniProtKB:Q16799}. +Q9ER80 RTP4_MOUSE Receptor-transporting protein 4 (28 kDa interferon-responsive protein) 249 28,392 Chain (1); Sequence conflict (4); Topological domain (1); Transmembrane (1) TRANSMEM 228 248 Helical. {ECO:0000255}. TOPO_DOM 1 227 Cytoplasmic. {ECO:0000255}. FUNCTION: Probable chaperone protein which facilitates trafficking and functional cell surface expression of some G-protein coupled receptors (GPCRs). Promotes functional expression of the bitter taste receptor TAS2R16 (By similarity). Also promotes functional expression of the opioid receptor heterodimer OPRD1-OPRM1 (PubMed:18836069). {ECO:0000250|UniProtKB:Q96DX8, ECO:0000269|PubMed:18836069}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type III membrane protein {ECO:0000305}. SUBUNIT: Interacts with TASR16 (By similarity). Interacts with OPRD1 and OPRM1; the interaction promotes cell surface localization of the OPDR1-OPRM1 heterodimer (PubMed:18836069). {ECO:0000250|UniProtKB:Q96DX8, ECO:0000269|PubMed:18836069}. TISSUE SPECIFICITY: Expressed at low levels in olfactory neurons. {ECO:0000269|PubMed:15550249}. +Q9CWX4 RUSD4_MOUSE Mitochondrial RNA pseudouridine synthase Rpusd4 (EC 5.4.99.-) (RNA pseudouridylate synthase domain-containing protein 4) 377 42,407 Active site (1); Chain (1); Transit peptide (1) FUNCTION: Catalyzes uridine to pseudouridine isomerization (pseudouridylation) of different mitochondrial RNA substrates. Acts on position 1397 in 16S mitochondrial ribosomal RNA (16S mt-rRNA). This modification is required for the assembly of 16S mt-rRNA into a functional mitochondrial ribosome. Acts on position 39 in mitochondrial tRNA(Phe). As a component of a functional protein-RNA module, consisting of RCC1L, NGRN, RPUSD3, RPUSD4, TRUB2, FASTKD2 and 16S mt-rRNA, controls 16S mt-rRNA abundance and is required for intra-mitochondrial translation. {ECO:0000250|UniProtKB:Q96CM3}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:Q96CM3}. Note=Localizes to mitochondrial RNA granules, platforms for post-transcriptional RNA modification and ribosome assembly. {ECO:0000250|UniProtKB:Q96CM3}. SUBUNIT: Interacts with 16S mt-rRNA, mt-tRNA(Phe) and mt-tRNA(Met). Forms a regulatory protein-RNA complex, consisting of RCC1L, NGRN, RPUSD3, RPUSD4, TRUB2, FASTKD2 and 16S mt-rRNA. {ECO:0000250|UniProtKB:Q96CM3}. +Q08775 RUNX2_MOUSE Runt-related transcription factor 2 (Acute myeloid leukemia 3 protein) (Core-binding factor subunit alpha-1) (CBF-alpha-1) (Oncogene AML-3) (Osteoblast-specific transcription factor 2) (OSF-2) (Polyomavirus enhancer-binding protein 2 alpha A subunit) (PEA2-alpha A) (PEBP2-alpha A) (SL3-3 enhancer factor 1 alpha A subunit) (SL3/AKV core-binding factor alpha A subunit) 607 66,205 Alternative sequence (10); Chain (1); Compositional bias (3); Cross-link (1); Domain (1); Modified residue (2); Region (4); Sequence conflict (7) FUNCTION: Transcription factor involved in osteoblastic differentiation and skeletal morphogenesis. Essential for the maturation of osteoblasts and both intramembranous and endochondral ossification. CBF binds to the core site, 5'-PYGPYGGT-3', of a number of enhancers and promoters, including murine leukemia virus, polyomavirus enhancer, T-cell receptor enhancers, osteocalcin, osteopontin, bone sialoprotein, alpha 1(I) collagen, LCK, IL-3 and GM-CSF promoters. Inhibits KAT6B-dependent transcriptional activation (By similarity). In osteoblasts, supports transcription activation: synergizes with SPEN/MINT to enhance FGFR2-mediated activation of the osteocalcin FGF-responsive element (OCFRE). {ECO:0000250, ECO:0000269|PubMed:20484411, ECO:0000269|PubMed:9182763}. PTM: Phosphorylated; probably by MAP kinases (MAPK). Phosphorylation by HIPK3 is required for the SPEN/MINT and FGF2 transactivation during osteoblastic differentiation. Phosphorylation at Ser-537 by CDK1 promotes endothelial cell proliferation required for tumor angiogenesis probably by facilitating cell cycle progression (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13950}. SUBUNIT: Heterodimer of an alpha and a beta subunit. The alpha subunit binds DNA as a monomer and through the Runt domain. DNA-binding is increased by heterodimerization. Interacts with XRCC6 (Ku70) and XRCC5 (Ku80). Interacts with CCNB1, KAT6A and KAT6B (By similarity). Interacts with HIVEP3. Interacts with IFI204. Interaction with SATB2; the interaction results in enhanced DNA binding and transactivation by these transcription factors. Binds to HIPK3. Interacts (isoform 3) with DDX5. Interacts with FOXO1 (via a C-terminal region); the interaction inhibits RUNX2 transcriptional activity towards BGLAP. Interacts with FOXP3 (By similarity). Interacts with TMEM119 (PubMed:21239498). Interacts with OLFM2 (By similarity). {ECO:0000250|UniProtKB:Q13950, ECO:0000250|UniProtKB:Q9Z2J9, ECO:0000269|PubMed:15557274, ECO:0000269|PubMed:16728642, ECO:0000269|PubMed:16751105, ECO:0000269|PubMed:17960593, ECO:0000269|PubMed:20484411, ECO:0000269|PubMed:21239498, ECO:0000269|PubMed:21471200}. DOMAIN: A proline/serine/threonine rich region at the C-terminus is necessary for transcriptional activation of target genes and contains the phosphorylation sites. TISSUE SPECIFICITY: Found in thymus and testis, T-cell lines but not in B-cell lines. Isoform 2 is exclusively found in bone, particularly in osteoblasts; isoforms 3 and 4 are expressed in T-cell lines; isoforms 5, 6, 7, 8 and 9 can be found in osteoblasts and osteosarcoma cell lines. +O70622 RTN2_MOUSE Reticulon-2 (Neuroendocrine-specific protein-like 1) (NSP-like protein 1) (Neuroendocrine-specific protein-like I) (NSP-like protein I) (NSPLI) 471 51,347 Alternative sequence (2); Chain (1); Domain (1); Modified residue (3); Transmembrane (2) TRANSMEM 295 315 Helical. {ECO:0000255}.; TRANSMEM 390 410 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Interacts with SPAST. Interacts with TMEM33. {ECO:0000250|UniProtKB:O75298}. TISSUE SPECIFICITY: Expressed predominantly in neural and muscular tissues. {ECO:0000269|PubMed:9530622}. +P0DN91 T254C_MOUSE Transmembrane protein 254c 123 14,239 Alternative sequence (1); Chain (1); Transmembrane (3) TRANSMEM 15 35 Helical. {ECO:0000255}.; TRANSMEM 63 83 Helical. {ECO:0000255}.; TRANSMEM 95 115 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9EQN9 S19A2_MOUSE Thiamine transporter 1 (ThTr-1) (Solute carrier family 19 member 2) 498 55,676 Alternative sequence (1); Chain (1); Glycosylation (1); Modified residue (2); Sequence conflict (1); Topological domain (13); Transmembrane (12) TRANSMEM 29 46 Helical. {ECO:0000255}.; TRANSMEM 72 92 Helical. {ECO:0000255}.; TRANSMEM 106 126 Helical. {ECO:0000255}.; TRANSMEM 129 149 Helical. {ECO:0000255}.; TRANSMEM 165 185 Helical. {ECO:0000255}.; TRANSMEM 187 207 Helical. {ECO:0000255}.; TRANSMEM 296 316 Helical. {ECO:0000255}.; TRANSMEM 335 355 Helical. {ECO:0000255}.; TRANSMEM 361 381 Helical. {ECO:0000255}.; TRANSMEM 387 407 Helical. {ECO:0000255}.; TRANSMEM 424 444 Helical. {ECO:0000255}.; TRANSMEM 457 477 Helical. {ECO:0000255}. TOPO_DOM 1 28 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 47 71 Extracellular. {ECO:0000305}.; TOPO_DOM 93 105 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 127 128 Extracellular. {ECO:0000305}.; TOPO_DOM 150 164 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 186 186 Extracellular. {ECO:0000305}.; TOPO_DOM 208 295 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 317 334 Extracellular. {ECO:0000305}.; TOPO_DOM 356 360 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 382 386 Extracellular. {ECO:0000305}.; TOPO_DOM 408 423 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 445 456 Extracellular. {ECO:0000305}.; TOPO_DOM 478 498 Cytoplasmic. {ECO:0000305}. FUNCTION: High-affinity transporter for the intake of thiamine. {ECO:0000269|PubMed:11481326, ECO:0000269|PubMed:11592824, ECO:0000269|PubMed:12031504, ECO:0000269|PubMed:12393806, ECO:0000269|PubMed:22194418}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11481326, ECO:0000269|PubMed:11592824}; Multi-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Expressed in cochlear hair cells and duodenum (at protein level) (PubMed:11592824). Detected in pancreatic acinar cells (at protein level) (PubMed:22194418). Also expressed strongly in pancreatic islet cells (PubMed:22194418). Isoform 1: Very highly expressed in liver, and also detected at lower levels in heart, testis, kidney, brain and spleen (PubMed:11386850, PubMed:12031504). Isoform 2: Expressed at low levels in liver and spleen (PubMed:12031504). {ECO:0000269|PubMed:11386850, ECO:0000269|PubMed:11592824, ECO:0000269|PubMed:12031504, ECO:0000269|PubMed:22194418}. +Q922G0 S2536_MOUSE Solute carrier family 25 member 36 311 34,170 Chain (1); Repeat (3); Transmembrane (6) TRANSMEM 7 27 Helical; Name=1. {ECO:0000255}.; TRANSMEM 41 57 Helical; Name=2. {ECO:0000255}.; TRANSMEM 111 131 Helical; Name=3. {ECO:0000255}.; TRANSMEM 180 200 Helical; Name=4. {ECO:0000255}.; TRANSMEM 226 246 Helical; Name=5. {ECO:0000255}.; TRANSMEM 291 311 Helical; Name=6. {ECO:0000255}. FUNCTION: Mitochondrial transporter that imports/exports pyrimidine nucleotides into and from mitochondria. Transports preferentially cytosine and uracil (deoxy)nucleoside mono-, di-, and triphosphates by uniport and antiport mechanism. Also transports guanine but not adenine (deoxy)nucleotides. Is inhibited strongly by pyridoxal 5'-phosphate, 4,7-diphenyl-1,10-phenanthroline, tannic acid, and mercurials (mercury dichloride, Mersalyl acid, p-hydroxymercuribenzoate). Participates in mitochondrial genome maintenance, regulation of mitochondrial membrane potential and mitochondrial respiration. {ECO:0000250|UniProtKB:Q96CQ1}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q96CQ1}; Multi-pass membrane protein {ECO:0000255}. +Q9WTW5 S22A3_MOUSE Solute carrier family 22 member 3 (Organic cation transporter 3) 551 61,053 Chain (1); Glycosylation (5); Transmembrane (7) TRANSMEM 21 41 Helical. {ECO:0000255}.; TRANSMEM 177 197 Helical. {ECO:0000255}.; TRANSMEM 236 256 Helical. {ECO:0000255}.; TRANSMEM 264 284 Helical. {ECO:0000255}.; TRANSMEM 376 396 Helical. {ECO:0000255}.; TRANSMEM 464 484 Helical. {ECO:0000255}.; TRANSMEM 493 513 Helical. {ECO:0000255}. FUNCTION: Mediates potential-dependent transport of a variety of organic cations. May play a significant role in the disposition of cationic neurotoxins and neurotransmitters in the brain. {ECO:0000269|PubMed:10966924, ECO:0000305}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Highly expressed in placenta and in kidney cortex, but not in medulla. Low levels found in brain. In the kidney, expressed specifically in the proximal and distal convoluted tubules and within Bowman capsule, but not in the glomerulus. {ECO:0000269|PubMed:10966924, ECO:0000269|PubMed:9933568, ECO:0000305}. +Q9R155 S26A4_MOUSE Pendrin (Sodium-independent chloride/iodide transporter) (Solute carrier family 26 member 4) 780 85,687 Chain (1); Domain (1); Topological domain (13); Transmembrane (12) TRANSMEM 88 108 Helical. {ECO:0000255}.; TRANSMEM 110 130 Helical. {ECO:0000255}.; TRANSMEM 136 156 Helical. {ECO:0000255}.; TRANSMEM 192 212 Helical. {ECO:0000255}.; TRANSMEM 219 239 Helical. {ECO:0000255}.; TRANSMEM 264 284 Helical. {ECO:0000255}.; TRANSMEM 296 316 Helical. {ECO:0000255}.; TRANSMEM 345 365 Helical. {ECO:0000255}.; TRANSMEM 385 405 Helical. {ECO:0000255}.; TRANSMEM 422 442 Helical. {ECO:0000255}.; TRANSMEM 449 469 Helical. {ECO:0000255}.; TRANSMEM 487 507 Helical. {ECO:0000255}. TOPO_DOM 1 87 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 109 109 Extracellular. {ECO:0000255}.; TOPO_DOM 131 135 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 157 191 Extracellular. {ECO:0000255}.; TOPO_DOM 213 218 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 240 263 Extracellular. {ECO:0000255}.; TOPO_DOM 285 295 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 317 344 Extracellular. {ECO:0000255}.; TOPO_DOM 366 384 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 406 421 Extracellular. {ECO:0000255}.; TOPO_DOM 443 448 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 470 486 Extracellular. {ECO:0000255}.; TOPO_DOM 508 780 Cytoplasmic. {ECO:0000255}. FUNCTION: Sodium-independent transporter of chloride and iodide. SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:11459928}; Multi-pass membrane protein {ECO:0000305|PubMed:11459928}. Cell membrane {ECO:0000269|PubMed:11459928}; Multi-pass membrane protein {ECO:0000269|PubMed:11459928}. Note=Localizes to the apical brush border of cells in the cortical collecting ducts of the kidney. TISSUE SPECIFICITY: Throughout the endolymphatic duct and sac, in distinct areas of the utricle and saccule, and in the external sulcus region within the cochlea. {ECO:0000269|PubMed:10449762}. +P97816 S100G_MOUSE Protein S100-G (Calbindin-D9k) (S100 calcium-binding protein G) (Vitamin D-dependent calcium-binding protein, intestinal) (CABP) 79 8,970 Calcium binding (2); Chain (1); Domain (2); Modified residue (2) +Q9D9E0 S22AH_MOUSE Solute carrier family 22 member 17 (24p3 receptor) (24p3R) (Brain-type organic cation transporter) (Lipocalin-2 receptor) 401 43,195 Alternative sequence (1); Chain (1); Sequence conflict (4); Transmembrane (10) TRANSMEM 10 30 Helical. {ECO:0000255}.; TRANSMEM 35 55 Helical. {ECO:0000255}.; TRANSMEM 69 89 Helical. {ECO:0000255}.; TRANSMEM 100 120 Helical. {ECO:0000255}.; TRANSMEM 184 203 Helical. {ECO:0000255}.; TRANSMEM 218 238 Helical. {ECO:0000255}.; TRANSMEM 247 267 Helical. {ECO:0000255}.; TRANSMEM 277 297 Helical. {ECO:0000255}.; TRANSMEM 309 329 Helical. {ECO:0000255}.; TRANSMEM 336 356 Helical. {ECO:0000255}. FUNCTION: Cell surface receptor for LCN2 (24p3) that plays a key role in iron homeostasis and transport. Able to bind iron-bound LCN2 (holo-24p3), followed by internalization of holo-24p3 and release of iron, thereby increasing intracellular iron concentration and leading to inhibition of apoptosis. Also binds iron-free LCN2 (apo-24p3), followed by internalization of apo-24p3 and its association with an intracellular siderophore, leading to iron chelation and iron transfer to the extracellular medium, thereby reducing intracellular iron concentration and resulting in apoptosis. {ECO:0000269|PubMed:16377569}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Vacuole membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Upon LCN2-binding, it is internalized. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:16377569}. +Q78KK3 S22AI_MOUSE Solute carrier family 22 member 18 (Imprinted multi-membrane-spanning polyspecific transporter-related protein 1) (Multi-membrane-spanning polyspecific transporter) (Organic cation transporter-like protein 2) (ORCTL-2) 406 43,013 Chain (1); Erroneous initiation (2); Sequence conflict (15); Transmembrane (10) TRANSMEM 8 28 Helical. {ECO:0000255}.; TRANSMEM 43 63 Helical. {ECO:0000255}.; TRANSMEM 85 105 Helical. {ECO:0000255}.; TRANSMEM 140 160 Helical. {ECO:0000255}.; TRANSMEM 168 188 Helical. {ECO:0000255}.; TRANSMEM 226 246 Helical. {ECO:0000255}.; TRANSMEM 258 278 Helical. {ECO:0000255}.; TRANSMEM 295 315 Helical. {ECO:0000255}.; TRANSMEM 316 336 Helical. {ECO:0000255}.; TRANSMEM 374 394 Helical. {ECO:0000255}. FUNCTION: May act as a transporter of organic cations based on a proton efflux antiport mechanism. May play a role in the transport of chloroquine and quinidine-related compounds in kidney (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Localized at the apical membrane surface of renal proximal tubules. {ECO:0000250}. SUBUNIT: Interacts with RNF167. {ECO:0000250}. TISSUE SPECIFICITY: Expressed at high levels in fetal and adult kidney and liver, and extraembryonic membranes (yolk sac). Expressed at moderate levels in intestine, heart, lung and testis. {ECO:0000269|PubMed:9499412, ECO:0000269|PubMed:9570947, ECO:0000269|PubMed:9802569}. +Q8K3D6 S35E4_MOUSE Solute carrier family 35 member E4 351 37,253 Chain (1); Domain (1); Sequence conflict (2); Transmembrane (9) TRANSMEM 40 60 Helical. {ECO:0000255}.; TRANSMEM 79 99 Helical. {ECO:0000255}.; TRANSMEM 110 130 Helical. {ECO:0000255}.; TRANSMEM 135 155 Helical. {ECO:0000255}.; TRANSMEM 162 182 Helical. {ECO:0000255}.; TRANSMEM 218 238 Helical. {ECO:0000255}.; TRANSMEM 258 278 Helical. {ECO:0000255}.; TRANSMEM 279 299 Helical. {ECO:0000255}.; TRANSMEM 301 321 Helical. {ECO:0000255}. FUNCTION: Putative transporter. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +O88561 S27A3_MOUSE Solute carrier family 27 member 3 (EC 6.2.1.-) (Long-chain fatty acid transport protein 3) (FATP-3) (Fatty acid transport protein 3) (Very long-chain acyl-CoA synthetase homolog 3) (VLCS-3) 667 72,965 Alternative sequence (2); Binding site (5); Chain (1); Erroneous initiation (2); Nucleotide binding (1); Sequence conflict (3); Transmembrane (1) TRANSMEM 3 23 Helical. {ECO:0000255}. FUNCTION: Has acyl-CoA ligase activity for long-chain and very-long-chain fatty acids. Does not exhibit fatty acid transport activity. {ECO:0000269|PubMed:15469937}. SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000269|PubMed:15469937}; Single-pass membrane protein {ECO:0000255}. Note=Mitochondrial in MA-10 Leydig cell line and Neuro-2a neuroblastoma. TISSUE SPECIFICITY: Expressed at high levels in adrenal gland, testis and ovary. Expressed at lower levels in adult brain. Found in adrenal cortical cells, spermatocytes and interstitial cells of the testis, theca cells of the ovary, cerebral cortical neurons, and cerebellar Purkinje cells (at protein level). {ECO:0000269|PubMed:15469937}. +Q8BWH0 S38A7_MOUSE Putative sodium-coupled neutral amino acid transporter 7 (Solute carrier family 38 member 7) 463 49,913 Chain (1); Modified residue (1); Sequence conflict (3); Transmembrane (11) TRANSMEM 56 76 Helical. {ECO:0000255}.; TRANSMEM 82 102 Helical. {ECO:0000255}.; TRANSMEM 130 150 Helical. {ECO:0000255}.; TRANSMEM 179 199 Helical. {ECO:0000255}.; TRANSMEM 206 226 Helical. {ECO:0000255}.; TRANSMEM 240 260 Helical. {ECO:0000255}.; TRANSMEM 283 303 Helical. {ECO:0000255}.; TRANSMEM 320 340 Helical. {ECO:0000255}.; TRANSMEM 372 392 Helical. {ECO:0000255}.; TRANSMEM 396 416 Helical. {ECO:0000255}.; TRANSMEM 429 449 Helical. {ECO:0000255}. FUNCTION: Mediates sodium-dependent transport of amino acids. Substrate preference is ranked l-glutamine > l-histidine > l-serine > l-alanine > l-asparagine > l-aspartic acid > l-glutamic acid > l-methionine > l-leucine > l-glycine. {ECO:0000269|PubMed:21511949}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:21511949}; Multi-pass membrane protein {ECO:0000269|PubMed:21511949}. Note=In neurons, located in soma and axons. TISSUE SPECIFICITY: Highly expressed in the brain, including the hippocampus, especially in the granular layer of dentate gyrus cells and the pyramidal cell layer of the hippocampus, amygdala, thalamus, hypothalamus, in the layer of Purkinje cells in the cerebellum and the layers of cortex. Particularly strong expression in neurons of the ventromedial hypothalamus, basolateral amygdala, ventral tegmental area, and locus coeruleus. Not detected in glial cells, including astrocytes. In addition to brain, also expressed in the spinal cord (at protein level). {ECO:0000269|PubMed:21511949}. +Q91VE0 S27A4_MOUSE Long-chain fatty acid transport protein 4 (FATP-4) (Fatty acid transport protein 4) (EC 6.2.1.-) (Solute carrier family 27 member 4) 643 72,319 Chain (1); Frameshift (1); Nucleotide binding (1); Sequence caution (1); Sequence conflict (2); Transmembrane (2) TRANSMEM 20 42 Helical. {ECO:0000255}.; TRANSMEM 139 156 Helical. {ECO:0000255}. FUNCTION: Involved in translocation of long-chain fatty acids (LFCA) across the plasma membrane. Appears to be the principal fatty acid transporter in small intestinal enterocytes. Plays a role in the formation of the epidermal barrier. Required for fat absorption in early embryogenesis. Has acyl-CoA ligase activity for long-chain and very-long-chain fatty acids (VLCFAs). Indirectly inhibits RPE65 via substrate competition and via production of VLCFA derivatives like lignoceroyl-CoA. Prevents light-induced degeneration of rods and cones. {ECO:0000269|PubMed:10518211, ECO:0000269|PubMed:11404000, ECO:0000269|PubMed:12821645, ECO:0000269|PubMed:15653672, ECO:0000269|PubMed:15699031, ECO:0000269|PubMed:23407971}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Endoplasmic reticulum membrane. TISSUE SPECIFICITY: Most abundantly expressed in small intestine, brain, kidney, liver, skin and heart. In small intestine, expressed at high levels on the apical side of mature enterocytes. Highly expressed by the epithelial cells of the visceral endoderm and localized to the brush-border membrane of extraembryonic endodermal cells (at protein level). Expressed in the retinal pigment epithelium and in the retina (at protein level). Expressed in the retinal pigment epithelium and in the retina. {ECO:0000269|PubMed:10518211, ECO:0000269|PubMed:11404000, ECO:0000269|PubMed:14512415, ECO:0000269|PubMed:23407971, ECO:0000269|PubMed:9671728}. DISEASE: Note=Defects in Slc27a4 are the cause of wrinkle-free (wrfr) phenotype. It is a spontaneous, autosomal recessive mutation resulting in very tight, thick skin and is secondary characterized by severe breathing difficulties. Mice die shortly after birth. This phenotype is similar to human restrictive dermopathy, a very rare human genetic disorder. {ECO:0000269|PubMed:12697906}. +Q91X56 S1PR5_MOUSE Sphingosine 1-phosphate receptor 5 (S1P receptor 5) (S1P5) (Endothelial differentiation G-protein-coupled receptor 8) (Lysophospholipid receptor B4) (Sphingosine 1-phosphate receptor Edg-8) (S1P receptor Edg-8) 400 42,331 Chain (1); Glycosylation (1); Lipidation (1); Modified residue (3); Topological domain (8); Transmembrane (7) TRANSMEM 42 62 Helical; Name=1. {ECO:0000250}.; TRANSMEM 69 89 Helical; Name=2. {ECO:0000250}.; TRANSMEM 112 132 Helical; Name=3. {ECO:0000250}.; TRANSMEM 152 172 Helical; Name=4. {ECO:0000250}.; TRANSMEM 193 213 Helical; Name=5. {ECO:0000250}.; TRANSMEM 254 274 Helical; Name=6. {ECO:0000250}.; TRANSMEM 289 309 Helical; Name=7. {ECO:0000250}. TOPO_DOM 1 41 Extracellular. {ECO:0000250}.; TOPO_DOM 63 68 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 90 111 Extracellular. {ECO:0000250}.; TOPO_DOM 133 151 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 173 192 Extracellular. {ECO:0000250}.; TOPO_DOM 214 253 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 275 288 Extracellular. {ECO:0000250}.; TOPO_DOM 310 400 Cytoplasmic. {ECO:0000250}. FUNCTION: Receptor for the lysosphingolipid sphingosine 1-phosphate (S1P). S1P is a bioactive lysophospholipid that elicits diverse physiological effect on most types of cells and tissues. Is coupled to both the G(i/0)alpha and G(12) subclass of heteromeric G-proteins (By similarity). S1P activation on oligodendroglial cells modulates two distinct functional pathways mediating either process retraction or cell survival. S1P activation on O4-positive pre-oligodendrocytes induces process retraction via a Rho kinase/collapsin response-mediated protein signaling pathway. The S1P-induced survival of mature oligodendrocytes is mediated through a pertussis toxin-sensitive, Akt-dependent pathway. S1P activation on oligodendroglial cells modulates two distinct functional pathways mediating either process retraction or cell survival. These effects depend on the developmental stage of the cell. {ECO:0000250, ECO:0000269|PubMed:15703400}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed in spleen and brain. In the CNS expression is restricted to oligodendrocytes. {ECO:0000269|PubMed:11705398, ECO:0000269|PubMed:15703400}. +Q8BHK3 S36A2_MOUSE Proton-coupled amino acid transporter 2 (Proton/amino acid transporter 2) (Solute carrier family 36 member 2) (Tramdorin-1) 478 52,063 Alternative sequence (2); Chain (1); Sequence conflict (4); Topological domain (12); Transmembrane (11) TRANSMEM 54 74 Helical. {ECO:0000255}.; TRANSMEM 77 97 Helical. {ECO:0000255}.; TRANSMEM 144 164 Helical. {ECO:0000255}.; TRANSMEM 193 213 Helical. {ECO:0000255}.; TRANSMEM 218 238 Helical. {ECO:0000255}.; TRANSMEM 260 280 Helical. {ECO:0000255}.; TRANSMEM 293 313 Helical. {ECO:0000255}.; TRANSMEM 341 361 Helical. {ECO:0000255}.; TRANSMEM 375 395 Helical. {ECO:0000255}.; TRANSMEM 400 420 Helical. {ECO:0000255}.; TRANSMEM 442 462 Helical. {ECO:0000255}. TOPO_DOM 1 53 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 75 76 Extracellular. {ECO:0000255}.; TOPO_DOM 98 143 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 165 192 Extracellular. {ECO:0000255}.; TOPO_DOM 214 217 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 239 259 Extracellular. {ECO:0000255}.; TOPO_DOM 281 292 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 314 340 Extracellular. {ECO:0000255}.; TOPO_DOM 362 374 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 396 399 Extracellular. {ECO:0000255}.; TOPO_DOM 421 441 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 463 478 Extracellular. {ECO:0000255}. FUNCTION: Involved in a pH-dependent electrogenic neuronal transport and sequestration of small amino acids amino acids such as glycine, alanine and proline. Inhibited by sarcosine. {ECO:0000269|PubMed:11959859, ECO:0000269|PubMed:14600155, ECO:0000269|PubMed:15291811}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14600155}; Multi-pass membrane protein {ECO:0000269|PubMed:14600155}. Cytoplasm {ECO:0000269|PubMed:14600155}. TISSUE SPECIFICITY: Expressed in spinal cord, brain, testis, lung, heart, colon, spleen, kidney and muscle. Found in neuronal cell bodies in the anterior horn, in spinal cord brain stem, cerebellum, hippocampus, hypothalamus, rhinencephalon, cerebral cortex, and olfactory bulb in the brain. Also expressed in bone and fat tissues. {ECO:0000269|PubMed:12809675, ECO:0000269|PubMed:14600155, ECO:0000269|PubMed:15058382}. +Q9JIM1 S29A1_MOUSE Equilibrative nucleoside transporter 1 (Equilibrative nitrobenzylmercaptopurine riboside-sensitive nucleoside transporter) (Equilibrative NBMPR-sensitive nucleoside transporter) (Nucleoside transporter, es-type) (Solute carrier family 29 member 1) 460 50,192 Alternative sequence (1); Chain (1); Glycosylation (1); Modified residue (2); Sequence conflict (3); Topological domain (12); Transmembrane (11) TRANSMEM 13 29 Helical. {ECO:0000255}.; TRANSMEM 83 107 Helical. {ECO:0000255}.; TRANSMEM 112 130 Helical. {ECO:0000255}.; TRANSMEM 139 157 Helical. {ECO:0000255}.; TRANSMEM 175 199 Helical. {ECO:0000255}.; TRANSMEM 207 227 Helical. {ECO:0000255}.; TRANSMEM 292 311 Helical. {ECO:0000255}.; TRANSMEM 324 342 Helical. {ECO:0000255}.; TRANSMEM 360 378 Helical. {ECO:0000255}.; TRANSMEM 398 417 Helical. {ECO:0000255}.; TRANSMEM 436 456 Helical. {ECO:0000255}. TOPO_DOM 1 12 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 30 82 Extracellular. {ECO:0000255}.; TOPO_DOM 108 111 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 131 138 Extracellular. {ECO:0000255}.; TOPO_DOM 158 174 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 200 206 Extracellular. {ECO:0000255}.; TOPO_DOM 228 291 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 312 323 Extracellular. {ECO:0000255}.; TOPO_DOM 343 359 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 379 397 Extracellular. {ECO:0000255}.; TOPO_DOM 418 435 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 457 460 Extracellular. {ECO:0000255}. FUNCTION: Mediates both influx and efflux of nucleosides across the membrane (equilibrative transporter). It is sensitive (ES) to low concentrations of the inhibitor nitrobenzylmercaptopurine riboside (NBMPR) and is sodium-independent. It has a higher affinity for adenosine. Resistant to dipyridamole and dilazep inhibition (anticancer chemotherapeutics drugs). SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Apical cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Predominantly localized in the basolateral membrane in polarized MDCK cells. {ECO:0000250}. SUBUNIT: Identified in a complex with STOM. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in heart, spleen, lung, liver and testis. Lower level of expression in brain and kidney. {ECO:0000269|PubMed:11027664}. +Q8BZH0 S39AD_MOUSE Zinc transporter ZIP13 (Solute carrier family 39 member 13) (Zrt- and Irt-like protein 13) (ZIP-13) 361 38,502 Alternative sequence (3); Chain (1); Compositional bias (1); Motif (1); Sequence conflict (3); Topological domain (9); Transmembrane (8) TRANSMEM 7 27 Helical. {ECO:0000255}.; TRANSMEM 69 89 Helical. {ECO:0000255}.; TRANSMEM 109 129 Helical. {ECO:0000255}.; TRANSMEM 151 171 Helical. {ECO:0000255}.; TRANSMEM 233 253 Helical. {ECO:0000255}.; TRANSMEM 276 296 Helical. {ECO:0000255}.; TRANSMEM 307 327 Helical. {ECO:0000255}.; TRANSMEM 340 360 Helical. {ECO:0000255}. TOPO_DOM 1 6 Lumenal. {ECO:0000255}.; TOPO_DOM 28 68 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 90 108 Lumenal. {ECO:0000255}.; TOPO_DOM 130 150 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 172 232 Lumenal. {ECO:0000255}.; TOPO_DOM 254 275 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 297 306 Lumenal. {ECO:0000255}.; TOPO_DOM 328 339 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 361 361 Lumenal. {ECO:0000255}. FUNCTION: Acts as a zinc-influx transporter. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein. SUBUNIT: Homodimer. {ECO:0000250}. +Q9Z1F9 SAE2_MOUSE SUMO-activating enzyme subunit 2 (EC 2.3.2.-) (Anthracycline-associated resistance ARX) (Ubiquitin-like 1-activating enzyme E1B) (Ubiquitin-like modifier-activating enzyme 2) 638 70,569 Active site (1); Binding site (2); Chain (1); Cross-link (15); Metal binding (4); Modified residue (6); Nucleotide binding (4); Sequence conflict (2) Protein modification; protein sumoylation. FUNCTION: The heterodimer acts as an E1 ligase for SUMO1, SUMO2, SUMO3, and probably SUMO4. It mediates ATP-dependent activation of SUMO proteins followed by formation of a thioester bond between a SUMO protein and a conserved active site cysteine residue on UBA2/SAE2 (By similarity). {ECO:0000250}. PTM: Sumoylated with SUMO1 and SUMO2/3 and by UBC9. Sumoylation at Lys-236 inhibits enzymatic activity. Sumoylation at the C-terminal lysine cluster plays an essential role in nuclear trafficking (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Shuttles between the cytoplasm and the nucleus, sumoylation is required either for nuclear translocation or nuclear retention. {ECO:0000250}. SUBUNIT: Heterodimer of SAE1 and UBA2/SAE2. The heterodimer corresponds to the two domains that are encoded on a single polypeptide chain in ubiquitin-activating enzyme E1. Interacts with UBE2I (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Broadly expressed, with highest levels in testis. {ECO:0000269|PubMed:11481243}. +Q8VDB9 S620A_MOUSE Sodium- and chloride-dependent transporter XTRP3A (IMINO-B) (Solute carrier family 6 member 20A) (X transporter protein 3 similar 1) 592 66,178 Chain (1); Glycosylation (1); Sequence conflict (1); Topological domain (13); Transmembrane (12) TRANSMEM 8 28 Helical; Name=1. {ECO:0000255}.; TRANSMEM 43 63 Helical; Name=2. {ECO:0000255}.; TRANSMEM 80 100 Helical; Name=3. {ECO:0000255}.; TRANSMEM 166 186 Helical; Name=4. {ECO:0000255}.; TRANSMEM 195 215 Helical; Name=5. {ECO:0000255}.; TRANSMEM 242 262 Helical; Name=6. {ECO:0000255}.; TRANSMEM 277 297 Helical; Name=7. {ECO:0000255}.; TRANSMEM 390 410 Helical; Name=8. {ECO:0000255}.; TRANSMEM 432 452 Helical; Name=9. {ECO:0000255}.; TRANSMEM 466 486 Helical; Name=10. {ECO:0000255}.; TRANSMEM 505 525 Helical; Name=11. {ECO:0000255}.; TRANSMEM 555 575 Helical; Name=12. {ECO:0000255}. TOPO_DOM 1 7 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 29 42 Extracellular. {ECO:0000255}.; TOPO_DOM 64 79 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 101 165 Extracellular. {ECO:0000255}.; TOPO_DOM 187 194 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 216 241 Extracellular. {ECO:0000255}.; TOPO_DOM 263 276 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 298 389 Extracellular. {ECO:0000255}.; TOPO_DOM 411 431 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 453 465 Extracellular. {ECO:0000255}.; TOPO_DOM 487 504 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 526 554 Extracellular. {ECO:0000255}.; TOPO_DOM 576 592 Cytoplasmic. {ECO:0000255}. FUNCTION: Mediates the calcium-dependent uptake of imino acids such as L-proline, N-methyl-L-proline and pipecolate as well as N-methylated amino acids. {ECO:0000269|PubMed:15689184}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:16174864}; Multi-pass membrane protein {ECO:0000269|PubMed:16174864}. Note=Located in the apical brush border membrane of kidney proximal tubule cells and in the apical membrane of enterocytes lining the intestinal villi. {ECO:0000269|PubMed:16174864}. TISSUE SPECIFICITY: Expressed in brain, kidney, small intestine, thymus, spleen and lung. In the brain, expressed in cerebellum, cortex and brain stem. Not detected in liver, muscle or heart. {ECO:0000269|PubMed:15689184}. +O88575 S620B_MOUSE Sodium- and chloride-dependent transporter XTRP3B (IMINO-K) (Solute carrier family 6 member 20B) 635 70,687 Chain (1); Glycosylation (2); Sequence conflict (4); Topological domain (13); Transmembrane (12) TRANSMEM 57 77 Helical; Name=1. {ECO:0000255}.; TRANSMEM 86 106 Helical; Name=2. {ECO:0000255}.; TRANSMEM 128 148 Helical; Name=3. {ECO:0000255}.; TRANSMEM 209 229 Helical; Name=4. {ECO:0000255}.; TRANSMEM 238 258 Helical; Name=5. {ECO:0000255}.; TRANSMEM 285 305 Helical; Name=6. {ECO:0000255}.; TRANSMEM 320 340 Helical; Name=7. {ECO:0000255}.; TRANSMEM 433 453 Helical; Name=8. {ECO:0000255}.; TRANSMEM 475 495 Helical; Name=9. {ECO:0000255}.; TRANSMEM 509 529 Helical; Name=10. {ECO:0000255}.; TRANSMEM 548 568 Helical; Name=11. {ECO:0000255}.; TRANSMEM 598 618 Helical; Name=12. {ECO:0000255}. TOPO_DOM 1 56 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 78 85 Extracellular. {ECO:0000255}.; TOPO_DOM 107 127 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 149 208 Extracellular. {ECO:0000255}.; TOPO_DOM 230 237 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 259 284 Extracellular. {ECO:0000255}.; TOPO_DOM 306 319 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 341 432 Extracellular. {ECO:0000255}.; TOPO_DOM 454 474 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 496 508 Extracellular. {ECO:0000255}.; TOPO_DOM 530 547 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 569 597 Extracellular. {ECO:0000255}.; TOPO_DOM 619 635 Cytoplasmic. {ECO:0000255}. FUNCTION: Does not show transporter activity with a range of tested amino acids including proline, glutamine, glutamic acid, leucine, alanine, histidine, glycine and arginine. {ECO:0000269|PubMed:15689184}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:16174864}; Multi-pass membrane protein {ECO:0000269|PubMed:16174864}. Note=Located in the apical brush border membrane of kidney proximal tubule cells. SUBUNIT: Interacts with CLTRN. {ECO:0000269|PubMed:17167413}. TISSUE SPECIFICITY: Detected only in kidney and lung. {ECO:0000269|PubMed:15689184, ECO:0000269|PubMed:9932288}. +Q60949 TBCD1_MOUSE TBC1 domain family member 1 1255 142,026 Alternative sequence (1); Chain (1); Domain (2); Erroneous initiation (1); Frameshift (1); Modified residue (27); Sequence conflict (10) FUNCTION: May act as a GTPase-activating protein for Rab family protein(s). May play a role in the cell cycle and differentiation of various tissues. Involved in the trafficking and translocation of GLUT4-containing vesicles and insulin-stimulated glucose uptake into cells. {ECO:0000269|PubMed:19740738}. PTM: Insulin-stimulated phosphorylation by AKT family kinases stimulates SLC2A4/GLUT4 translocation. {ECO:0000269|PubMed:19740738}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:7566974}. TISSUE SPECIFICITY: Expressed in highest levels in hematopoietic cells, testis and kidney. {ECO:0000269|PubMed:7566974}. +Q9JLC8 SACS_MOUSE Sacsin (DnaJ homolog subfamily C member 29) (DNAJC29) 4582 520,685 Alternative sequence (2); Chain (1); Domain (3); Erroneous initiation (1); Modified residue (7); Sequence conflict (6) FUNCTION: Co-chaperone which acts as a regulator of the Hsp70 chaperone machinery and may be involved in the processing of other ataxia-linked proteins. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Predominantly cytoplasmic, a small portion is present in the nucleus and also shows a partial mitochondrial overlap with the mitochondrial marker Hsp60. {ECO:0000250}. DOMAIN: The ubiquitin-like domain mediates interaction with the proteasome. {ECO:0000250}.; DOMAIN: The J domain is functional and is able to stimulate E.coli dnaK ATPase activity. {ECO:0000250}. TISSUE SPECIFICITY: Brain (at protein level). {ECO:0000269|PubMed:19208651}. +P31651 S6A12_MOUSE Sodium- and chloride-dependent betaine transporter (Na(+)/Cl(-) betaine/GABA transporter) (Sodium- and chloride-dependent GABA transporter 2) (GAT-2) (Solute carrier family 6 member 12) 614 69,614 Chain (1); Disulfide bond (1); Glycosylation (2); Topological domain (3); Transmembrane (12) TRANSMEM 45 65 Helical; Name=1. {ECO:0000255}.; TRANSMEM 73 92 Helical; Name=2. {ECO:0000255}.; TRANSMEM 117 137 Helical; Name=3. {ECO:0000255}.; TRANSMEM 211 229 Helical; Name=4. {ECO:0000255}.; TRANSMEM 238 255 Helical; Name=5. {ECO:0000255}.; TRANSMEM 291 308 Helical; Name=6. {ECO:0000255}.; TRANSMEM 320 341 Helical; Name=7. {ECO:0000255}.; TRANSMEM 374 393 Helical; Name=8. {ECO:0000255}.; TRANSMEM 423 441 Helical; Name=9. {ECO:0000255}.; TRANSMEM 458 478 Helical; Name=10. {ECO:0000255}.; TRANSMEM 499 518 Helical; Name=11. {ECO:0000255}.; TRANSMEM 538 556 Helical; Name=12. {ECO:0000255}. TOPO_DOM 1 44 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 138 210 Extracellular. {ECO:0000255}.; TOPO_DOM 557 614 Cytoplasmic. {ECO:0000255}. FUNCTION: Transports betaine and GABA. May have a role in regulation of GABAergic transmission in the brain through the reuptake of GABA into presynaptic terminals, as well as in osmotic regulation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SUBUNIT: Interacts with LIN7C. {ECO:0000250}. TISSUE SPECIFICITY: Brain, liver and kidney. +P31532 SAA4_MOUSE Serum amyloid A-4 protein (Amyloid A-5 protein) 130 15,088 Chain (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Major acute phase reactant. Apolipoprotein of the HDL complex. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Expressed by the liver; secreted in plasma. DISEASE: Note=Reactive, secondary amyloidosis is characterized by the extracellular accumulation in various tissues of the SAA protein. These deposits are highly insoluble and resistant to proteolysis; they disrupt tissue structure and compromise function. +Q9D6X5 S52A3_MOUSE Solute carrier family 52, riboflavin transporter, member 3 (Riboflavin transporter 2) (RFT2) 460 49,559 Alternative sequence (2); Chain (1); Disulfide bond (1); Glycosylation (2); Modified residue (2); Sequence conflict (5); Topological domain (12); Transmembrane (11) TRANSMEM 7 27 Helical. {ECO:0000255}.; TRANSMEM 38 58 Helical. {ECO:0000255}.; TRANSMEM 72 92 Helical. {ECO:0000255}.; TRANSMEM 106 126 Helical. {ECO:0000255}.; TRANSMEM 138 158 Helical. {ECO:0000255}.; TRANSMEM 212 232 Helical. {ECO:0000255}.; TRANSMEM 292 312 Helical. {ECO:0000255}.; TRANSMEM 327 347 Helical. {ECO:0000255}.; TRANSMEM 351 371 Helical. {ECO:0000255}.; TRANSMEM 388 408 Helical. {ECO:0000255}.; TRANSMEM 419 439 Helical. {ECO:0000255}. TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 28 37 Extracellular. {ECO:0000255}.; TOPO_DOM 59 71 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 93 105 Extracellular. {ECO:0000255}.; TOPO_DOM 127 137 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 159 211 Extracellular. {ECO:0000255}.; TOPO_DOM 233 291 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 313 326 Extracellular. {ECO:0000255}.; TOPO_DOM 348 350 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 372 387 Extracellular. {ECO:0000255}.; TOPO_DOM 409 418 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 440 460 Extracellular. {ECO:0000255}. FUNCTION: Transporter for riboflavin, which must be obtained as a nutrient via intestinal absorption. Riboflavin transport is Na(+)-independent at low pH but significantly reduced by Na(+) depletion under neutral pH conditions. {ECO:0000250|UniProtKB:Q9NQ40}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9NQ40}; Multi-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Within the small intestine, it is particulary expressed in the jujenum and the ileum. Almost negligible expression in the stomach, duodenum, and large intestine. {ECO:0000269|PubMed:24264046}. +A6H687 SAC31_MOUSE SAC3 domain-containing protein 1 (SAC3 homology domain-containing protein 1) 427 46,384 Chain (1); Domain (1); Erroneous initiation (1); Modified residue (1); Sequence conflict (2) FUNCTION: Involved in centrosome duplication and mitotic progression. {ECO:0000269|PubMed:15322101}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:15322101}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:15322101}. Note=Localizes on centrosomes in interphase cells and at spindles in mitosis. SUBUNIT: May be part of a SEM1-containing complex. {ECO:0000250}. TISSUE SPECIFICITY: Present in spleen cells (at protein level). {ECO:0000269|PubMed:15322101}. +Q8CIV8 TBCE_MOUSE Tubulin-specific chaperone E (Tubulin-folding cofactor E) 524 59,086 Beta strand (7); Chain (1); Domain (2); Helix (2); Initiator methionine (1); Modified residue (3); Natural variant (2); Repeat (7); Turn (2) FUNCTION: Tubulin-folding protein; involved in the second step of the tubulin folding pathway and in the regulation of tubulin heterodimer dissociation (PubMed:12389029, PubMed:17184771). Required for correct organization of microtubule cytoskeleton and mitotic splindle, and maintenance of the neuronal microtubule network (By similarity). {ECO:0000250|UniProtKB:Q15813, ECO:0000269|PubMed:12389029, ECO:0000269|PubMed:17184771}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. SUBUNIT: Supercomplex made of cofactors A to E. Cofactors A and D function by capturing and stabilizing tubulin in a quasi-native conformation. Cofactor E binds to the cofactor D-tubulin complex; interaction with cofactor C then causes the release of tubulin polypeptides that are committed to the native state. Cofactors B and E can form a heterodimer which binds to alpha-tubulin and enhances their ability to dissociate tubulin heterodimers. Interacts with TBCD (By similarity). {ECO:0000250|UniProtKB:Q15813, ECO:0000269|PubMed:17184771}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:12389029}. +Q99N99 S5A2_MOUSE 3-oxo-5-alpha-steroid 4-dehydrogenase 2 (EC 1.3.1.22) (5 alpha-SR2) (SR type 2) (Steroid 5-alpha-reductase 2) (S5AR 2) 254 28,619 Chain (1); Transmembrane (4) TRANSMEM 8 28 Helical. {ECO:0000255}.; TRANSMEM 72 92 Helical. {ECO:0000255}.; TRANSMEM 146 166 Helical. {ECO:0000255}.; TRANSMEM 206 226 Helical. {ECO:0000255}. FUNCTION: Converts testosterone (T) into 5-alpha-dihydrotestosterone (DHT) and progesterone or corticosterone into their corresponding 5-alpha-3-oxosteroids. It plays a central role in sexual differentiation and androgen physiology. {ECO:0000250|UniProtKB:P31213}. SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9R1K7 TBD_MOUSE Tubulin delta chain (Delta-tubulin) 455 51,023 Chain (1); Nucleotide binding (1) FUNCTION: Acts as a positive regulator of hedgehog signaling and regulates ciliary function (PubMed:29290584). {ECO:0000269|PubMed:29290584}. SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000269|PubMed:29290584}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:10753753}. Cytoplasm {ECO:0000269|PubMed:10753753}. Nucleus {ECO:0000269|PubMed:10753753}. Note=Associated with centrioles (PubMed:10753753). Both cytoplasmic and nuclear (PubMed:10753753). In the elongating spermatid it is associated with the manchette, a specialized microtubule system present during reshaping of the sperm head (PubMed:10753753). {ECO:0000269|PubMed:10753753}. TISSUE SPECIFICITY: Highly expressed in testis. +Q9D6T1 TBE_MOUSE Tubulin epsilon chain (Epsilon-tubulin) 475 52,652 Chain (1); Nucleotide binding (1) SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Associated with pericentriolar material. +Q5U680 SAMC_MOUSE S-adenosylmethionine mitochondrial carrier protein (Mitochondrial S-adenosylmethionine transporter) (Solute carrier family 25 member 26) 274 29,027 Chain (1); Repeat (3); Sequence conflict (1); Transmembrane (6) TRANSMEM 5 25 Helical; Name=1. {ECO:0000255}.; TRANSMEM 49 69 Helical; Name=2. {ECO:0000255}.; TRANSMEM 85 105 Helical; Name=3. {ECO:0000255}.; TRANSMEM 142 162 Helical; Name=4. {ECO:0000255}.; TRANSMEM 182 202 Helical; Name=5. {ECO:0000255}.; TRANSMEM 238 258 Helical; Name=6. {ECO:0000255}. FUNCTION: Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane. Specifically mediates the transport of S-adenosylmethionine (SAM) into the mitochondria (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q9DA37 SAMD8_MOUSE Sphingomyelin synthase-related protein 1 (SMSr) (EC 2.7.8.-) (Ceramide phosphoethanolamine synthase) (CPE synthase) (Sterile alpha motif domain-containing protein 8) (SAM domain-containing protein 8) 478 54,713 Chain (1); Domain (1); Topological domain (1); Transmembrane (6) TRANSMEM 216 236 Helical. {ECO:0000255}.; TRANSMEM 264 284 Helical. {ECO:0000255}.; TRANSMEM 295 315 Helical. {ECO:0000255}.; TRANSMEM 341 361 Helical. {ECO:0000255}.; TRANSMEM 385 405 Helical. {ECO:0000255}.; TRANSMEM 410 430 Helical. {ECO:0000255}. TOPO_DOM 431 478 Cytoplasmic. {ECO:0000255}. FUNCTION: sphingomyelin synthases synthesize sphingolipids through transfer of a phosphatidyl head group on to the primary hydroxyl of ceramide. SAMD8 is an endoplasmic reticulum (ER) transferase that has no sphingomyelin synthase activity but can convert phosphatidylethanolamine (PE) and ceramide to ceramide phosphatidylethanolamine (CPE) albeit with low product yield. Appears to operate as a ceramide sensor to control ceramide homeostasis in the endoplasmic reticulum rather than a converter of ceramides. Seems to be critical for the integrity of the early secretory pathway (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. DOMAIN: The SAM domain is required to retain SMAD8 in the endoplasmic reticulum. membrane protein (By similarity). {ECO:0000250}. +Q66JZ4 TCAIM_MOUSE T-cell activation inhibitor, mitochondrial (Tolerance associated gene-1 protein) (TOAG-1) 499 57,402 Chain (1); Coiled coil (1) FUNCTION: May regulate T-cell apoptosis. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:19684086}. TISSUE SPECIFICITY: Expressed in peripheral blood leukocytes, mainly in T-lymphocytes. {ECO:0000269|PubMed:17456197}. +Q63836 SBP2_MOUSE Selenium-binding protein 2 (56 kDa acetaminophen-binding protein) (AP56) 472 52,610 Chain (1); Modified residue (1); Sequence conflict (1) FUNCTION: Selenium- and acetaminophen-binding protein which may be involved in the sensing of reactive xenobiotics in the cytoplasm. May be involved in intra-Golgi protein transport (By similarity). {ECO:0000250}. PTM: The N-terminus is blocked. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytosol. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=May associate with Golgi membrane. May associate with the membrane of autophagosomes (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Mainly expressed in liver. +Q8BXT9 SC22C_MOUSE Vesicle-trafficking protein SEC22c (SEC22 vesicle trafficking protein-like 3) (SEC22 vesicle-trafficking protein homolog C) 303 33,913 Chain (1); Domain (1); Sequence conflict (3); Topological domain (5); Transmembrane (4) TRANSMEM 184 204 Helical. {ECO:0000255}.; TRANSMEM 224 244 Helical. {ECO:0000255}.; TRANSMEM 249 269 Helical. {ECO:0000255}.; TRANSMEM 271 291 Helical. {ECO:0000255}. TOPO_DOM 1 183 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 205 223 Lumenal. {ECO:0000255}.; TOPO_DOM 245 248 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 270 270 Lumenal. {ECO:0000255}.; TOPO_DOM 292 303 Cytoplasmic. {ECO:0000255}. FUNCTION: May be involved in vesicle transport between the ER and the Golgi complex. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q8K0E3 SC5AB_MOUSE Sodium/myo-inositol cotransporter 2 (Na(+)/myo-inositol cotransporter 2) (Sodium-dependent glucose cotransporter) (Sodium/glucose cotransporter KST1) (Sodium/myo-inositol transporter 2) (SMIT2) (Solute carrier family 5 member 11) 673 73,798 Alternative sequence (1); Chain (1); Frameshift (1); Sequence conflict (3); Topological domain (14); Transmembrane (14) TRANSMEM 28 48 Helical. {ECO:0000255}.; TRANSMEM 66 88 Helical. {ECO:0000255}.; TRANSMEM 103 123 Helical. {ECO:0000255}.; TRANSMEM 149 169 Helical. {ECO:0000255}.; TRANSMEM 181 201 Helical. {ECO:0000255}.; TRANSMEM 209 229 Helical. {ECO:0000255}.; TRANSMEM 273 293 Helical. {ECO:0000255}.; TRANSMEM 309 329 Helical. {ECO:0000255}.; TRANSMEM 376 396 Helical. {ECO:0000255}.; TRANSMEM 419 439 Helical. {ECO:0000255}.; TRANSMEM 447 467 Helical. {ECO:0000255}.; TRANSMEM 480 500 Helical. {ECO:0000255}.; TRANSMEM 522 542 Helical. {ECO:0000255}.; TRANSMEM 653 673 Helical. {ECO:0000255}. TOPO_DOM 1 27 Extracellular. {ECO:0000255}.; TOPO_DOM 49 65 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 89 102 Extracellular. {ECO:0000255}.; TOPO_DOM 124 148 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 170 180 Extracellular. {ECO:0000255}.; TOPO_DOM 202 208 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 230 272 Extracellular. {ECO:0000255}.; TOPO_DOM 294 308 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 330 375 Extracellular. {ECO:0000255}.; TOPO_DOM 397 418 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 440 446 Extracellular. {ECO:0000255}.; TOPO_DOM 468 479 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 501 521 Extracellular. {ECO:0000255}.; TOPO_DOM 543 652 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in the sodium-dependent cotransport of myo-inositol (MI) with a Na(+):MI stoichiometry of 2:1. Exclusively responsible for apical MI transport and absorption in intestine. Also can transport D-chiro-inositol (DCI) but not L-fructose. Exhibits stereospecific cotransport of both D-glucose and D-xylose. May induce apoptosis through the TNF-alpha, PDCD1 pathway. May play a role in the regulation of MI concentration in serum, involving reabsorption in at least the proximal tubule of the kidney (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q28728}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q28728}. +P56844 TCLB4_MOUSE Protein TCL1B4 120 14,123 Chain (1) +O55192 SC6A2_MOUSE Sodium-dependent noradrenaline transporter (Norepinephrine transporter) (NET) (Solute carrier family 6 member 2) 617 69,255 Chain (1); Disulfide bond (1); Glycosylation (2); Metal binding (9); Sequence conflict (1); Topological domain (13); Transmembrane (12) TRANSMEM 63 88 Helical; Name=1. {ECO:0000250|UniProtKB:Q7K4Y6}.; TRANSMEM 93 116 Helical; Name=2. {ECO:0000250|UniProtKB:Q7K4Y6}.; TRANSMEM 136 166 Helical; Name=3. {ECO:0000250|UniProtKB:Q7K4Y6}.; TRANSMEM 234 254 Helical; Name=4. {ECO:0000250|UniProtKB:Q7K4Y6}.; TRANSMEM 258 282 Helical; Name=5. {ECO:0000250|UniProtKB:Q7K4Y6}.; TRANSMEM 307 332 Helical; Name=6. {ECO:0000250|UniProtKB:Q7K4Y6}.; TRANSMEM 339 362 Helical; Name=7. {ECO:0000250|UniProtKB:Q7K4Y6}.; TRANSMEM 403 428 Helical; Name=8. {ECO:0000250|UniProtKB:Q7K4Y6}.; TRANSMEM 444 464 Helical; Name=9. {ECO:0000250|UniProtKB:Q7K4Y6}.; TRANSMEM 466 492 Helical; Name=10. {ECO:0000250|UniProtKB:Q7K4Y6}.; TRANSMEM 523 545 Helical; Name=11. {ECO:0000250|UniProtKB:Q7K4Y6}.; TRANSMEM 549 569 Helical; Name=12. {ECO:0000250|UniProtKB:Q7K4Y6}. TOPO_DOM 1 62 Cytoplasmic. {ECO:0000250|UniProtKB:Q7K4Y6}.; TOPO_DOM 89 92 Extracellular. {ECO:0000250|UniProtKB:Q7K4Y6}.; TOPO_DOM 117 135 Cytoplasmic. {ECO:0000250|UniProtKB:Q7K4Y6}.; TOPO_DOM 167 233 Extracellular. {ECO:0000250|UniProtKB:Q7K4Y6}.; TOPO_DOM 255 257 Cytoplasmic. {ECO:0000250|UniProtKB:Q7K4Y6}.; TOPO_DOM 283 306 Extracellular. {ECO:0000250|UniProtKB:Q7K4Y6}.; TOPO_DOM 333 338 Cytoplasmic. {ECO:0000250|UniProtKB:Q7K4Y6}.; TOPO_DOM 363 402 Extracellular. {ECO:0000250|UniProtKB:Q7K4Y6}.; TOPO_DOM 429 443 Cytoplasmic. {ECO:0000250|UniProtKB:Q7K4Y6}.; TOPO_DOM 465 465 Extracellular. {ECO:0000250|UniProtKB:Q7K4Y6}.; TOPO_DOM 493 522 Cytoplasmic. {ECO:0000250|UniProtKB:Q7K4Y6}.; TOPO_DOM 546 548 Extracellular. {ECO:0000250|UniProtKB:Q7K4Y6}.; TOPO_DOM 570 617 Cytoplasmic. {ECO:0000250|UniProtKB:Q7K4Y6}. FUNCTION: Amine transporter. Terminates the action of noradrenaline by its high affinity sodium-dependent reuptake into presynaptic terminals. {ECO:0000305|PubMed:16269905}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P23975}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q7K4Y6}. SUBUNIT: Interacts with PRKCABP. {ECO:0000250|UniProtKB:P23975}. +Q60857 SC6A4_MOUSE Sodium-dependent serotonin transporter (SERT) (5HT transporter) (5HTT) (Solute carrier family 6 member 4) 630 70,048 Chain (1); Disulfide bond (1); Frameshift (1); Glycosylation (2); Metal binding (9); Modified residue (6); Region (2); Sequence conflict (7); Topological domain (13); Transmembrane (12) TRANSMEM 88 112 Helical; Name=1. {ECO:0000250|UniProtKB:P31645}.; TRANSMEM 116 135 Helical; Name=2. {ECO:0000250|UniProtKB:P31645}.; TRANSMEM 161 186 Helical; Name=3. {ECO:0000250|UniProtKB:P31645}.; TRANSMEM 253 271 Helical; Name=4. {ECO:0000250|UniProtKB:P31645}.; TRANSMEM 278 297 Helical; Name=5. {ECO:0000250|UniProtKB:P31645}.; TRANSMEM 325 347 Helical; Name=6. {ECO:0000250|UniProtKB:P31645}.; TRANSMEM 361 380 Helical; Name=7. {ECO:0000250|UniProtKB:P31645}.; TRANSMEM 422 443 Helical; Name=8. {ECO:0000250|UniProtKB:P31645}.; TRANSMEM 464 483 Helical; Name=9. {ECO:0000250|UniProtKB:P31645}.; TRANSMEM 495 516 Helical; Name=10. {ECO:0000250|UniProtKB:P31645}.; TRANSMEM 539 558 Helical; Name=11. {ECO:0000250|UniProtKB:P31645}.; TRANSMEM 575 595 Helical; Name=12. {ECO:0000250|UniProtKB:P31645}. TOPO_DOM 1 87 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 113 115 Extracellular. {ECO:0000305}.; TOPO_DOM 136 160 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 187 252 Extracellular. {ECO:0000305}.; TOPO_DOM 272 277 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 298 324 Extracellular. {ECO:0000305}.; TOPO_DOM 348 360 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 381 421 Extracellular. {ECO:0000305}.; TOPO_DOM 444 463 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 484 494 Extracellular. {ECO:0000305}.; TOPO_DOM 517 538 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 559 574 Extracellular. {ECO:0000305}.; TOPO_DOM 596 630 Cytoplasmic. {ECO:0000305}. FUNCTION: Serotonin transporter whose primary function in the central nervous system involves the regulation of serotonergic signaling via transport of serotonin molecules from the synaptic cleft back into the pre-synaptic terminal for re-utilization. Plays a key role in mediating regulation of the availability of serotonin to other receptors of serotonergic systems. Terminates the action of serotonin and recycles it in a sodium-dependent manner. {ECO:0000269|PubMed:9037532}. PTM: Glycosylated; modification with sialylated N-glycans is a requirement for transporters to associate with each other and to function as homooligomeric forms. {ECO:0000250}.; PTM: Phosphorylation upon PKC stimulation modifies the SERT distribution and density in the membrane, and diminishes the uptake capacity. Phosphorylation at Thr-276 increases 5-HT uptake and is required for cGMP-mediated SERT regulation. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9037532}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q7K4Y6}. Endomembrane system {ECO:0000250|UniProtKB:P31652}; Multi-pass membrane protein {ECO:0000255}. Endosome membrane {ECO:0000250|UniProtKB:P31652}; Multi-pass membrane protein {ECO:0000255}. Note=Could be part of recycling endosomes. Density of transporter molecules on the plasma membrane is itself regulated by STX1A. Density of transporter molecules on the plasma membrane is also regulated by serotonin (By similarity). {ECO:0000250|UniProtKB:P31645, ECO:0000250|UniProtKB:P31652}. SUBUNIT: Monomer or homooligomer (By similarity). Interacts (via C-terminus) with VIM. Interacts (via C-terminus) with SCAMP2; the interaction is direct and retains transporter molecules intracellularly. Interacts with GTP-bound RAB4 (GTP-bound form); the interaction retains transporter molecules intracellularly. Interacts (via sialylated form) with MYH9. Interacts with filamentous actin and STX1A (By similarity). Interacts with SEC23A, SEC24C and PATJ. Interacts with NOS1; the interaction may diminish the cell surface localization of SERT in the brain and, correspondingly, reduce serotonin reuptake. Interacts with TGFB1I1. {ECO:0000250, ECO:0000269|PubMed:16803896, ECO:0000269|PubMed:17452640}. +Q6GQT6 SCAP_MOUSE Sterol regulatory element-binding protein cleavage-activating protein (SCAP) (SREBP cleavage-activating protein) 1276 139,611 Chain (1); Cross-link (2); Domain (1); Erroneous initiation (1); Glycosylation (3); Modified residue (7); Mutagenesis (3); Region (2); Repeat (7); Sequence conflict (2); Topological domain (9); Transmembrane (8) TRANSMEM 19 39 Helical; Name=1. {ECO:0000255}.; TRANSMEM 280 300 Helical; Name=2. {ECO:0000255}.; TRANSMEM 313 333 Helical; Name=3. {ECO:0000255}.; TRANSMEM 345 365 Helical; Name=4. {ECO:0000255}.; TRANSMEM 402 422 Helical; Name=5. {ECO:0000255}.; TRANSMEM 424 444 Helical; Name=6. {ECO:0000255}.; TRANSMEM 519 539 Helical; Name=7. {ECO:0000255}.; TRANSMEM 708 728 Helical; Name=8. {ECO:0000255}. TOPO_DOM 1 18 Cytoplasmic. {ECO:0000250|UniProtKB:P97260}.; TOPO_DOM 40 279 Lumenal. {ECO:0000250|UniProtKB:P97260}.; TOPO_DOM 301 312 Cytoplasmic. {ECO:0000250|UniProtKB:P97260}.; TOPO_DOM 334 344 Lumenal. {ECO:0000250|UniProtKB:P97260}.; TOPO_DOM 366 401 Cytoplasmic. {ECO:0000250|UniProtKB:P97260}.; TOPO_DOM 423 423 Lumenal. {ECO:0000250|UniProtKB:P97260}.; TOPO_DOM 445 518 Cytoplasmic. {ECO:0000250|UniProtKB:P97260}.; TOPO_DOM 540 707 Lumenal. {ECO:0000250|UniProtKB:P97260}.; TOPO_DOM 729 1276 Cytoplasmic. {ECO:0000250|UniProtKB:P97260}. FUNCTION: Escort protein required for cholesterol as well as lipid homeostasis. Regulates export of the SCAP/SREBF complex from the ER upon low cholesterol. Formation of a ternary complex with INSIG at high sterol concentrations leads to masking of an ER-export signal in SCAP and retention of the complex in the ER. Low sterol concentrations trigger release of INSIG, a conformational change in the SSC domain of SCAP, unmasking of the ER export signal, recruitment into COPII-coated vesicles, transport to the Golgi complex, proteolytic cleavage of SREBF in the Golgi, release of the transcription factor fragment of SREBF from the membrane, its import into the nucleus and up-regulation of LDLR, INSIG1 and the mevalonate pathway. {ECO:0000250|UniProtKB:P97260, ECO:0000269|PubMed:11358865, ECO:0000269|PubMed:9854040}. PTM: Ubiquitinated at Lys-454 and Lys-466. RNF145 triggers ubiquitination of SCAP, likely inhibiting SCAP:SREBPF2 complex transport to the Golgi apparatus and the subsequent processing/maturation of SREBPF2. {ECO:0000269|PubMed:29068315}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P97260}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P97260}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P97260}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P97260}. Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250|UniProtKB:P97260}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P97260}. Note=Moves from the endoplasmic reticulum to the Golgi in the absence of sterols. {ECO:0000250|UniProtKB:P97260}. SUBUNIT: Membrane region forms a homotetramer. Forms a stable complex with SREBF1/SREBP1 or SREBF2/SREBP2 through its C-terminal cytoplasmic domain. Forms a ternary complex with INSIG1 or INSIG2 through its transmembrane domains at high sterol concentrations. Interacts with the SEC23/SEC24 complex in a SAR1-GTP-dependent manner through an ER export signal in its third cytoplasmic loop. Binds cholesterol through its SSC domain. Component of SCAP/SREBP complex composed of SREBF2, SCAP and RNF139; the complex hampers the interaction between SCAP and SEC24B, thereby reducing SREBF2 proteolytic processing. Interacts with RNF139; the interaction inhibits the interaction of SCAP with SEC24B and hampering the ER to Golgi transport of the SCAP/SREBP complex (By similarity). {ECO:0000250}. DOMAIN: Cholesterol bound to SSC domain of SCAP or oxysterol bound to INSIG1/2 leads to masking of an ER export signal on SCAP possibly by moving the signal further away from the ER membrane. {ECO:0000250|UniProtKB:P97260}. +Q6T707 SCD4_MOUSE Acyl-CoA desaturase 4 (EC 1.14.19.1) (Delta(9)-desaturase 4) (Delta-9 desaturase 4) (Fatty acid desaturase 4) (Stearoyl-CoA desaturase 4) 353 41,042 Binding site (7); Chain (1); Metal binding (9); Motif (3); Sequence conflict (4); Topological domain (5); Transmembrane (4) TRANSMEM 67 87 Helical. {ECO:0000250|UniProtKB:O00767}.; TRANSMEM 92 112 Helical. {ECO:0000250|UniProtKB:O00767}.; TRANSMEM 212 231 Helical. {ECO:0000250|UniProtKB:O00767}.; TRANSMEM 236 257 Helical. {ECO:0000250|UniProtKB:O00767}. TOPO_DOM 1 66 Cytoplasmic. {ECO:0000250|UniProtKB:O00767}.; TOPO_DOM 88 91 Lumenal. {ECO:0000250|UniProtKB:O00767}.; TOPO_DOM 113 211 Cytoplasmic. {ECO:0000250|UniProtKB:O00767}.; TOPO_DOM 232 235 Lumenal. {ECO:0000250|UniProtKB:O00767}.; TOPO_DOM 258 353 Cytoplasmic. {ECO:0000250|UniProtKB:O00767, ECO:0000305}. FUNCTION: Stearyl-CoA desaturase that utilizes O(2) and electrons from reduced cytochrome b5 to introduce the first double bond into saturated fatty acyl-CoA substrates. Catalyzes the insertion of a cis double bond at the delta-9 position into fatty acyl-CoA substrates including palmitoyl-CoA and stearoyl-CoA (PubMed:12815040, PubMed:16443825). Required for the biosynthesis of membrane phospholipids, cholesterol esters and triglycerides (By similarity). {ECO:0000250|UniProtKB:O00767, ECO:0000269|PubMed:12815040, ECO:0000269|PubMed:16443825}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O00767}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O00767}. Microsome membrane {ECO:0000269|PubMed:12815040, ECO:0000269|PubMed:16443825}. DOMAIN: The histidine box domains are involved in binding the catalytic metal ions. {ECO:0000250|UniProtKB:O00767}. TISSUE SPECIFICITY: Detected in heart, but not in brain, liver, skin or adipose tissue. {ECO:0000269|PubMed:12815040}. +Q61180 SCNNA_MOUSE Amiloride-sensitive sodium channel subunit alpha (Alpha-NaCH) (Epithelial Na(+) channel subunit alpha) (Alpha-ENaC) (Nonvoltage-gated sodium channel 1 subunit alpha) (SCNEA) 699 78,893 Chain (1); Sequence conflict (2); Topological domain (3); Transmembrane (2) TRANSMEM 111 131 Helical; Name=1. {ECO:0000255}.; TRANSMEM 590 610 Helical; Name=2. {ECO:0000255}. TOPO_DOM 1 110 Cytoplasmic. {ECO:0000250|UniProtKB:P37089}.; TOPO_DOM 132 589 Extracellular. {ECO:0000250|UniProtKB:P37089}.; TOPO_DOM 611 699 Cytoplasmic. {ECO:0000250|UniProtKB:P37089}. FUNCTION: Sodium permeable non-voltage-sensitive ion channel inhibited by the diuretic amiloride. Mediates the electrodiffusion of the luminal sodium (and water, which follows osmotically) through the apical membrane of epithelial cells. Plays an essential role in electrolyte and blood pressure homeostasis, but also in airway surface liquid homeostasis, which is important for proper clearance of mucus. Controls the reabsorption of sodium in kidney, colon, lung and eccrine sweat glands. Also plays a role in taste perception. {ECO:0000269|PubMed:10409305}. PTM: Ubiquitinated; this targets individual subunits for endocytosis and proteasome-mediated degradation. {ECO:0000250|UniProtKB:P37089}.; PTM: ENaC cleavage by furin, and subsequently by prostasin (PRSS8), leads to a stepwise increase in the open probability of the channel as a result of release of the alpha and gamma subunit inhibitory tracts, respectively. Interaction of ENaC subunit SCNN1B with BPIFA1 protects ENaC against proteolytic activation. {ECO:0000250|UniProtKB:P37088}.; PTM: N-glycosylated. {ECO:0000250|UniProtKB:P37089}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:P37089}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P37089}. Cell projection, cilium {ECO:0000250|UniProtKB:P37088}. Cytoplasmic granule {ECO:0000250|UniProtKB:P37088}. Cytoplasm {ECO:0000250|UniProtKB:P37088}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250|UniProtKB:P37089}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:P37089}. Note=In the oviduct and bronchus, located on cilia in multi-ciliated cells. In endometrial non-ciliated epithelial cells, restricted to apical surfaces. In epidermis, located nearly uniformly in the cytoplasm in a granular distribution. In sebaceous glands, observed only in the cytoplasmic space in between the lipid vesicles. In eccrine sweat glands, mainly located at the apical surface of the cells facing the lumen. In skin, in arrector pili muscle cells and in adipocytes, located in the cytoplasm and colocalized with actin fibers. In spermatogonia, spermatocytes and round spermatids, located in the cytoplasm. Prior to spermiation, location shifts from the cytoplasm to the spermatid tail. In spermatozoa, localizes at the acrosome and the central region of the sperm flagellum. {ECO:0000250|UniProtKB:P37088, ECO:0000250|UniProtKB:P37089}. SUBUNIT: Heterotrimer containing an alpha/SCNN1A, a beta/SCNN1B and a gamma/SCNN1G subunit. An additional delta/SCNN1D subunit exists only in some organisms and can replace the alpha/SCNN1A subunit to form an alternative channel with specific properties (Probable). Interacts with NEDD4 (via WW domains) (PubMed:11244092, PubMed:15123669). Interacts with NEDD4L (via WW domains) (PubMed:11244092, PubMed:12424229, PubMed:15123669). Interacts with WWP1 (via WW domains). Interacts with WWP2 (via WW domains). Interacts with the full-length immature form of PCSK9 (pro-PCSK9). {ECO:0000250|UniProtKB:P37088, ECO:0000269|PubMed:11244092, ECO:0000269|PubMed:12424229, ECO:0000269|PubMed:15123669, ECO:0000305, ECO:0000305|PubMed:10409305}. TISSUE SPECIFICITY: Expressed in kidney and lung (at protein level). Also expressed in distal colon and, at low levels, in liver. {ECO:0000269|PubMed:22207244}. +Q8BMD8 SCMC1_MOUSE Calcium-binding mitochondrial carrier protein SCaMC-1 (Small calcium-binding mitochondrial carrier protein 1) (Solute carrier family 25 member 24) 475 52,902 Calcium binding (4); Chain (1); Domain (4); Modified residue (5); Repeat (3); Sequence conflict (4); Topological domain (7); Transmembrane (6) TRANSMEM 198 215 Helical; Name=1. {ECO:0000255}.; TRANSMEM 251 270 Helical; Name=2. {ECO:0000255}.; TRANSMEM 294 307 Helical; Name=3. {ECO:0000255}.; TRANSMEM 344 363 Helical; Name=4. {ECO:0000255}.; TRANSMEM 387 404 Helical; Name=5. {ECO:0000255}.; TRANSMEM 444 463 Helical; Name=6. {ECO:0000255}. TOPO_DOM 1 197 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 216 250 Mitochondrial matrix. {ECO:0000255}.; TOPO_DOM 271 293 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 308 343 Mitochondrial matrix. {ECO:0000255}.; TOPO_DOM 364 386 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 405 443 Mitochondrial matrix. {ECO:0000255}.; TOPO_DOM 464 475 Mitochondrial intermembrane. {ECO:0000255}. FUNCTION: Calcium-dependent mitochondrial solute carrier. Mediates the reversible, electroneutral exchange of Mg-ATP or Mg-ADP against phosphate ions, catalyzing the net uptake or efflux of adenine nucleotides across the mitochondrial inner membrane. Nucleotide transport is inactive when cytosolic calcium levels are low, and is activated by an increase in cytosolic calcium levels. May play a role in protecting cells against oxidative stress-induced cell death, probably by promoting the formation of calcium-phosphate precipitates in the mitochondrial matrix, and thereby buffering calcium levels in the mitochondrial matrix (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. DOMAIN: The N-terminal domain can bind calcium and regulates the ATP carrier activity of the transmembrane domain. The apo form of the N-terminal domain is intrinsically disordered and binds to the transmembrane domain, leading to inhibition of the ATP carrier activity. Calcium binding leads to a major conformation change and abolishes the interaction with the transmembrane domain and the inhibition of the ATP carrier activity (By similarity). {ECO:0000250}. +Q8BHK2 SCN3B_MOUSE Sodium channel subunit beta-3 215 24,789 Chain (1); Disulfide bond (2); Domain (1); Glycosylation (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 160 180 Helical. {ECO:0000255}. TOPO_DOM 25 159 Extracellular. {ECO:0000255}.; TOPO_DOM 181 215 Cytoplasmic. {ECO:0000255}. FUNCTION: Modulates channel gating kinetics. Causes unique persistent sodium currents. Inactivates the sodium channel opening more slowly than the subunit beta-1. Its association with NFASC may target the sodium channels to the nodes of Ranvier of developing axons and retain these channels at the nodes in mature myelinated axons (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: The voltage-sensitive sodium channel consists of an ion conducting pore forming alpha-subunit regulated by one or more beta-1, beta-2, beta-3 and/or beta-4 subunits. Beta-1 and beta-3 are non-covalently associated with alpha, while beta-2 and beta-4 are covalently linked by disulfide bonds (By similarity). {ECO:0000250}. +Q9WTS4 TEN1_MOUSE Teneurin-1 (Ten-1) (Protein Odd Oz/ten-m homolog 1) (Tenascin-M1) (Ten-m1) (Teneurin transmembrane protein 1) [Cleaved into: Ten-1 intracellular domain (IDten-1) (Ten-1 ICD); Teneurin C-terminal-associated peptide (TCPA-1) (Ten-1 extracellular domain) (Ten-1 ECD)] 2731 305,795 Alternative sequence (1); Chain (3); Compositional bias (1); Disulfide bond (22); Domain (9); Glycosylation (14); Modified residue (4); Motif (2); Repeat (28); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 325 345 Helical. {ECO:0000255}. TOPO_DOM 1 324 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 346 2731 Extracellular. {ECO:0000255}. FUNCTION: Involved in neural development, regulating the establishment of proper connectivity within the nervous system. May function as a cellular signal transducer (By similarity). {ECO:0000250}.; FUNCTION: Teneurin C-terminal-associated peptide: Plays a role in the regulation of neuroplasticity in the limbic system. Mediates a rapid reorganization of actin- and tubulin-based cytoskeleton elements with an increase in dendritic arborization and spine density formation of neurons in the hippocampus and amygdala. Induces BDNF transcription inhibition in neurons. Activates the mitogen-activated protein (MAP) kinase 2 (MEK2) and extracellular signal-regulated kinase (ERK) cascade. Acts also as a bioactive neuroprotective peptide on limbic neurons of the brain and regulates stress-induced behavior: attenuates alkalosis-associated necrotic cell death and the effects of corticotropin-releasing factor (CRF) on c-fos/FOS induction and on the reinstatement of cocaine seeking. {ECO:0000269|PubMed:15710242, ECO:0000269|PubMed:17174479, ECO:0000269|PubMed:17644218, ECO:0000269|PubMed:17900539, ECO:0000269|PubMed:18082275, ECO:0000269|PubMed:19428634, ECO:0000269|PubMed:20883474, ECO:0000269|PubMed:21411044, ECO:0000269|PubMed:22209827, ECO:0000269|PubMed:22698694}.; FUNCTION: Ten-1 intracellular domain: Induces gene transcription activation. {ECO:0000250}. PTM: Isoform 2: Once secreted, may also be cleaved to give rise to the TCAP-1 form. {ECO:0000269|PubMed:23026563}.; PTM: Teneurin C-terminal-associated peptide: Derives from the plasma membrane form by proteolytic processing. Further proteolytic cleavage may generate 11.9 and 4.7 kDa bioactive peptides. {ECO:0000269|PubMed:23026563}. SUBCELLULAR LOCATION: Isoform 1: Cell membrane {ECO:0000269|PubMed:23026563}; Single-pass membrane protein {ECO:0000269|PubMed:23026563}. Note=Colocalizes with isoform 2 at the plasma membrane.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Cell membrane. Secreted {ECO:0000305}. Note=Transported to the cell membrane and probably secreted to function as an autocrine or paracrine signaling molecule. The lack of a hydrophobic segment sequence suggests that isoform 2 is released by damaged cells or is secreted by a mechanism differing from that used for other secretory proteins.; SUBCELLULAR LOCATION: Ten-1 intracellular domain: Nucleus {ECO:0000250}. Nucleus speckle {ECO:0000250}. Nucleus matrix {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.; SUBCELLULAR LOCATION: Teneurin C-terminal-associated peptide: Nucleus {ECO:0000305}. Cytoplasm. Cell membrane. Note=Colocalizes with isoform 1 at the plasma membrane. Colocalizes with the dystroglycan complex at the cell membrane in hippocampal cells. Binds hippocampal cell membranes and is incorporated in the cytoplasm by endocytosis in a caveoli-dependent manner. Upon cell internalization is transported arround and in the nucleus. SUBUNIT: Homodimer; disulfide-linked. Heterodimer with either TENM2 or TENM3. May also form heterodimer with TENM4. Ten-1 ICD interacts with SORBS1 (via third SH3 domain). Interacts with MBD1 isoform 2. {ECO:0000269|PubMed:10225957, ECO:0000269|PubMed:15777793}. DOMAIN: EGF-like domains 2 and 5 which have an odd number of cysteines might enable the formation of intermolecular disulfide bonds.; DOMAIN: Cytoplasmic proline-rich regions could serve as docking domains for intracellular SH3-containing proteins. TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in the brain. Isoform 2 is expressed in the granular layer of the dentate gyrus and the pyramidal layer (Py) of the CA1, CA2 and CA3 of the hippocampus (at protein level). Expressed in the cortex, thalamus, CA1, CA2, CA3, dentate gyrus and granular layer of the hippocampus. Weakly expressed in kidney, testis and lung. {ECO:0000269|PubMed:10225957, ECO:0000269|PubMed:12915301, ECO:0000269|PubMed:15710242, ECO:0000269|PubMed:23026563}. +Q5U4D9 THOC6_MOUSE THO complex subunit 6 homolog (WD repeat-containing protein 58) 341 37,315 Chain (1); Modified residue (1); Repeat (7) FUNCTION: Acts as component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and which specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NFX1 pathway.Plays a role in apoptosis negative control involved in brain development (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus speckle {ECO:0000250}. SUBUNIT: Component of the THO complex, which is composed of THOC1, THOC2, THOC3, THOC5, THOC6 and THOC7; together with at least ALYREF/THOC4, DDX39B, SARNP/CIP29 and CHTOP, THO forms the transcription/export (TREX) complex which seems to have a dynamic structure involving ATP-dependent remodeling. {ECO:0000250}. +O54951 SEM6B_MOUSE Semaphorin-6B (Semaphorin VIB) (Sema VIB) (Semaphorin-N) (Sema N) 886 95,467 Chain (1); Compositional bias (1); Disulfide bond (8); Domain (1); Glycosylation (6); Modified residue (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 606 626 Helical. {ECO:0000255}. TOPO_DOM 27 605 Extracellular. {ECO:0000255}.; TOPO_DOM 627 886 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SUBUNIT: Homodimer. Binds specifically the SH3 domain of the protooncogene C-SRC. TISSUE SPECIFICITY: During development it is expressed in subregions of the nervous system and is particularly prominent in muscle. In adulthood, it is expressed ubiquitously. +O88632 SEM3F_MOUSE Semaphorin-3F (Semaphorin IV) (Sema IV) 785 88,549 Alternative sequence (1); Chain (1); Compositional bias (2); Disulfide bond (6); Domain (2); Glycosylation (2); Sequence conflict (6); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000250}. TISSUE SPECIFICITY: Expressed ubiquitously in adulthood. During embryogenesis, expressed in subregions of the central nervous system and various other tissues like skin, kidney, lung and intestine. +Q8R2U0 SEH1_MOUSE Nucleoporin SEH1 (GATOR complex protein SEH1) (Nup107-160 subcomplex subunit SEH1) 360 39,775 Alternative sequence (1); Chain (1); Cross-link (1); Frameshift (1); Modified residue (1); Repeat (6); Sequence conflict (2) FUNCTION: Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex is required for the assembly of a functional NPC. The Nup107-160 subcomplex is also required for normal kinetochore microtubule attachment, mitotic progression and chromosome segregation. This subunit plays a role in recruitment of the Nup107-160 subcomplex to the kinetochore. {ECO:0000250|UniProtKB:Q96EE3}.; FUNCTION: As a component of the GATOR subcomplex GATOR2, functions within the amino acid-sensing branch of the TORC1 signaling pathway. Indirectly activates mTORC1 and the TORC1 signaling pathway through the inhibition of the GATOR1 subcomplex. It is negatively regulated by the upstream amino acid sensors SESN2 and CASTOR1. {ECO:0000250|UniProtKB:Q96EE3}. SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q96EE3}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q96EE3}. Lysosome membrane {ECO:0000250|UniProtKB:Q96EE3}. SUBUNIT: Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex includes NUP160, NUP133, NUP107, NUP98, NUP85, NUP43, NUP37, SEH1 and SEC13. The SEH1 subunit appears to be only weakly associated with the Nup107-160 subcomplex. Within the GATOR complex, component of the GATOR2 subcomplex, made of MIOS, SEC13, SEH1L, WDR24 and WDR59. The GATOR complex strongly interacts with RRAGA/RRAGC and RRAGB/RRAGC heterodimers. The GATOR2 complex interacts with CASTOR2 and CASTOR1; the interaction is negatively regulated by arginine. The GATOR2 complex interacts with SESN1, SESN2 and SESN3; the interaction is negatively regulated by amino acids. {ECO:0000250|UniProtKB:Q96EE3}. +Q62179 SEM4B_MOUSE Semaphorin-4B (Semaphorin-C) (Sema C) 823 91,392 Chain (1); Compositional bias (1); Disulfide bond (6); Domain (3); Erroneous initiation (1); Glycosylation (9); Modified residue (4); Sequence conflict (8); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 704 724 Helical. {ECO:0000255}. TOPO_DOM 31 703 Extracellular. {ECO:0000255}.; TOPO_DOM 725 823 Cytoplasmic. {ECO:0000255}. FUNCTION: Inhibits axonal extension by providing local signals to specify territories inaccessible for growing axons. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Interacts with GIPC PDZ domain. {ECO:0000269|PubMed:10318831}. +O08710 THYG_MOUSE Thyroglobulin (Tg) 2766 304,473 Chain (1); Disulfide bond (30); Domain (11); Glycosylation (20); Modified residue (30); Natural variant (1); Repeat (8); Sequence conflict (23); Signal peptide (1) FUNCTION: Precursor of the iodinated thyroid hormones thyroxine (T4) and triiodothyronine (T3). PTM: Sulfated tyrosines are desulfated during iodination. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Thyroid gland specific. DISEASE: Note=Defects in Tg are the cause of some forms of goiter. Goiter is an enlargement of the thyroid gland. The variant Pro-2283 exhibits a defect in exit from the endoplasmic reticulum. +Q8K4Z5 SF3A1_MOUSE Splicing factor 3A subunit 1 (SF3a120) 791 88,545 Beta strand (6); Chain (1); Compositional bias (6); Cross-link (6); Domain (1); Helix (4); Modified residue (9); Repeat (2); Sequence conflict (3); Site (1); Turn (1) FUNCTION: Subunit of the splicing factor SF3A required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA. May also be involved in the assembly of the 'E' complex (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Identified in the spliceosome C complex (By similarity). Component of splicing factor SF3A which is composed of three subunits; SF3A3/SAP61, SF3A2/SAP62, SF3A1/SAP114. SF3A associates with the splicing factor SF3B and a 12S RNA unit to form the U2 small nuclear ribonucleoproteins complex (U2 snRNP). Interacts with SF3A3 (By similarity). {ECO:0000250}. DOMAIN: SURP motif 2 mediates direct binding to SF3A3. {ECO:0000250}. +Q9Z180 SETBP_MOUSE SET-binding protein (SEB) 1582 173,077 Chain (1); Compositional bias (2); DNA binding (3); Erroneous initiation (1); Modified residue (1); Sequence conflict (5) SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with SET. {ECO:0000250}. +Q91WC0 SETD3_MOUSE Histone-lysine N-methyltransferase setd3 (EC 2.1.1.43) (Endothelial differentiation inhibitory protein D10) (SET domain-containing protein 3) 594 67,176 Alternative sequence (5); Chain (1); Domain (1); Sequence conflict (3) FUNCTION: Histone methyltransferase that methylates 'Lys-4' and 'Lys-36' of histone H3 (H3K4me and H3K36me) (PubMed:21832073). Acts as a transcriptional activator (PubMed:21832073). Plays an important role in the transcriptional regulation of muscle cell differentiation via interaction with MYOD1 (PubMed:21832073). {ECO:0000269|PubMed:21832073}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21832073}. SUBUNIT: Interacts with MYOD1. {ECO:0000269|PubMed:21832073}. TISSUE SPECIFICITY: Prominently expressed in the heart and skeletal muscles and is also detected weakly in the stomach, small intestine, and colon. {ECO:0000269|PubMed:21832073}. +Q9CX34 SGT1_MOUSE Protein SGT1 homolog (Suppressor of G2 allele of SKP1 homolog) 336 38,159 Chain (1); Cross-link (2); Domain (2); Initiator methionine (1); Modified residue (5); Repeat (3); Sequence conflict (2) FUNCTION: May play a role in ubiquitination and subsequent proteasomal degradation of target proteins. PTM: Phosphorylated at Ser-252 and Ser-302, dephosphorylation promotes nuclear translocation, most likely due to disruption of the SUGT1-HSP90 complex. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Translocates the to nucleus upon heat shock, requiring S100A6. {ECO:0000250}. SUBUNIT: Probably associates with SCF (SKP1-CUL1-F-box protein) complex through interaction with SKP1. Interacts with S100A6. Interacts with HSP90 (By similarity). {ECO:0000250}. DOMAIN: The CS domain mediates interaction with HSP90. {ECO:0000250}. +Q8BZT2 SH3R2_MOUSE E3 ubiquitin-protein ligase SH3RF2 (EC 2.3.2.27) (Protein phosphatase 1 regulatory subunit 39) (RING finger protein 158) (RING-type E3 ubiquitin transferase SH3RF2) (SH3 domain-containing RING finger protein 2) 735 80,066 Alternative sequence (1); Beta strand (7); Chain (1); Domain (3); Helix (1); Modified residue (1); Region (2); Sequence conflict (3); Turn (1); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: Has E3 ubiquitin-protein ligase activity. Acts as an anti-apoptotic regulator of the JNK pathway by ubiquitinating and promoting the degradation of SH3RF1, a scaffold protein that is required for pro-apoptotic JNK activation. Facilitates TNF-alpha-mediated recruitment of adapter proteins TRADD and RIPK1 to TNFRSF1A and regulates PAK4 protein stability via inhibition of its ubiquitin-mediated proteasomal degradation. Inhibits PPP1CA phosphatase activity (By similarity). {ECO:0000250|UniProtKB:Q8TEC5}. PTM: Autoubiquitinated. {ECO:0000250|UniProtKB:Q8TEC5}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8TEC5}. SUBUNIT: Interacts with FASLG and PPP1CA. Interacts with PAK4 and TNFRSF1A. Interacts with DLK1, MAP3K10, MAPK8IP1/JIP1, MAPK8IP2/JIP2 and MAPK8IP3/JIP3. Interacts with RAC1 (both active GTP- or inactive GDP-bound forms). {ECO:0000250|UniProtKB:Q498M5, ECO:0000250|UniProtKB:Q8TEC5}. DOMAIN: The RING finger domain is required for ubiquitin ligase activity and autoubiquitination. {ECO:0000250|UniProtKB:Q8TEC5}. +Q8VCZ6 SGSM3_MOUSE Small G protein signaling modulator 3 (RUN and TBC1 domain-containing protein 3) 750 85,490 Beta strand (5); Chain (1); Coiled coil (1); Domain (3); Erroneous initiation (1); Helix (1); Modified residue (1); Sequence conflict (1) FUNCTION: May play a cooperative role in NF2-mediated growth suppression of cells. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96HU1}. SUBUNIT: Interacts with GJA1. Interaction with GJA1 induces its degradation. Interacts via its RUN domain with the C-terminal region of NF2. Interacts with RAB3A, RAB4A, RAB5A, RAB8A, RAB11A, RAP1A, RAP1B, RAP2A, RAP2B and PDCD6I. No interaction with RAB27A (By similarity). {ECO:0000250|UniProtKB:Q96HU1, ECO:0000269|PubMed:15709751}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:17509819}. +Q6P7W2 SHKB1_MOUSE SH3KBP1-binding protein 1 (SETA-binding protein 1) 704 76,103 Alternative sequence (2); Chain (1); Domain (1); Initiator methionine (1); Modified residue (5); Motif (2); Mutagenesis (2); Repeat (5); Sequence conflict (3) FUNCTION: Inhibits CBL-SH3KBP1 complex mediated down-regulation of EGFR signaling by sequestration of SH3KBP1. Binds to SH3KBP1 and prevents its interaction with CBL and inhibits translocation of SH3KBP1 to EGFR containing vesicles upon EGF stimulation (PubMed:21830225). {ECO:0000269|PubMed:21830225}. SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:Q8TBC3}. SUBUNIT: Monomer (By similarity). Interacts with CUL3; interaction is direct and forms a 5:5 heterodecamer (By similarity). Interacts (via PXXXPR motifs) with SH3KBP1 (via SH3 domains) (PubMed:11152963, PubMed:21830225). Directly interacts with cathepsin B/CTSB (By similarity). {ECO:0000250|UniProtKB:Q8TBC3, ECO:0000269|PubMed:11152963, ECO:0000269|PubMed:21830225}. +Q91VW3 SH3L3_MOUSE SH3 domain-binding glutamic acid-rich-like protein 3 93 10,477 Beta strand (4); Chain (1); Domain (1); Helix (4); Initiator methionine (1); Modified residue (1); Turn (1) FUNCTION: Could act as a modulator of glutaredoxin biological activity. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000269|PubMed:15120624}. +Q9JLF7 TLR5_MOUSE Toll-like receptor 5 859 97,627 Chain (1); Disulfide bond (2); Domain (2); Glycosylation (9); Modified residue (1); Natural variant (8); Repeat (20); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 642 662 Helical. {ECO:0000255}. TOPO_DOM 27 641 Extracellular. {ECO:0000255}.; TOPO_DOM 663 859 Cytoplasmic. {ECO:0000255}. FUNCTION: Participates in the innate immune response to microbial agents. Mediates detection of bacterial flagellins. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (By similarity). {ECO:0000250}. PTM: Phosphorylated at Tyr-799 upon flagellin binding; required for signaling. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Homodimer both in the absence and presence of ligand. Binds MYD88 via their respective TIR domains (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in liver. Detected in lung and at very low levels in most other tissues. +Q7TPQ3 SHPRH_MOUSE E3 ubiquitin-protein ligase SHPRH (EC 2.3.2.27) (EC 3.6.4.-) (RING-type E3 ubiquitin transferase SHPRH) (SNF2, histone-linker, PHD and RING finger domain-containing helicase) 1674 191,490 Alternative sequence (5); Chain (1); Domain (4); Modified residue (3); Motif (1); Nucleotide binding (1); Sequence caution (1); Sequence conflict (6); Zinc finger (2) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase involved in DNA repair. Upon genotoxic stress, accepts ubiquitin from the UBE2N-UBE2V2 E2 complex and transfers it to 'Lys-164' of PCNA which had been monoubiquitinated by UBE2A/B-RAD18, promoting the formation of non-canonical poly-ubiquitin chains linked through 'Lys-63'. {ECO:0000250|UniProtKB:Q149N8}. SUBUNIT: Homodimer. Interacts with HLTF, PCNA, UBE2N and RAD18. {ECO:0000250|UniProtKB:Q149N8}. DOMAIN: The RING finger mediates E3 ubiquitin ligase activity. {ECO:0000250}. TISSUE SPECIFICITY: Broadly expressed (at protein level). {ECO:0000269|PubMed:12837266}. +Q9EPW9 TLR6_MOUSE Toll-like receptor 6 (CD antigen CD286) 795 91,116 Beta strand (22); Chain (1); Disulfide bond (4); Domain (2); Erroneous initiation (2); Glycosylation (10); Helix (8); Mutagenesis (1); Repeat (19); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (6) TRANSMEM 585 605 Helical. {ECO:0000255}. TOPO_DOM 28 584 Extracellular. {ECO:0000255}.; TOPO_DOM 606 795 Cytoplasmic. {ECO:0000255}. FUNCTION: Participates in the innate immune response to Gram-positive bacteria and fungi. Specifically recognizes diacylated and, to a lesser extent, triacylated lipopeptides (PubMed:19931471). In response to diacylated lipopeptides, forms the activation cluster TLR2:TLR6:CD14:CD36, this cluster triggers signaling from the cell surface and subsequently is targeted to the Golgi in a lipid-raft dependent pathway. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. Recognizes mycoplasmal macrophage-activating lipopeptide-2kD (MALP-2), soluble tuberculosis factor (STF), phenol-soluble modulin (PSM) and B.burgdorferi outer surface protein A lipoprotein (OspA-L) cooperatively with TLR2. In complex with TLR4, promotes sterile inflammation in monocytes/macrophages in response to oxidized low-density lipoprotein (oxLDL) or amyloid-beta 42. In this context, the initial signal is provided by oxLDL- or amyloid-beta 42-binding to CD36. This event induces the formation of a heterodimer of TLR4 and TLR6, which is rapidly internalized and triggers inflammatory response, leading to the NF-kappa-B-dependent production of CXCL1, CXCL2 and CCL9 cytokines, via MYD88 signaling pathway, and CCL5 cytokine, via TICAM1 signaling pathway, as well as IL1B secretion (PubMed:20037584, PubMed:23812099). {ECO:0000269|PubMed:19931471, ECO:0000269|PubMed:20037584, ECO:0000269|PubMed:23812099}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11095740}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasmic vesicle, phagosome membrane {ECO:0000269|PubMed:11095740}; Single-pass type I membrane protein {ECO:0000255}. Membrane raft {ECO:0000250|UniProtKB:Q9Y2C9}. Golgi apparatus {ECO:0000250|UniProtKB:Q9Y2C9}. Note=Upon complex formation with CD36 and TLR4, internalized through dynamin-dependent endocytosis. Does not reside in lipid rafts before stimulation but accumulates increasingly in the raft upon the presence of the microbial ligand. In response to diacylated lipoproteins, TLR2:TLR6 heterodimers are recruited in lipid rafts, this recruitment determine the intracellular targeting to the Golgi apparatus. {ECO:0000250|UniProtKB:Q9Y2C9}. SUBUNIT: Homodimer (via cytoplasmic TIR domain) (By similarity). Heterodimer with TLR2 via their respective extracellular domains (PubMed:19931471). Binds MYD88 via their respective TIR domains (Probable). Interacts with CD36, following CD36 stimulation by oxLDL or amyloid-beta 42, and forms a heterodimer with TLR4. The trimeric complex is internalized and triggers inflammatory response. LYN kinase activity facilitates TLR4:TLR6 heterodimerization and signal initiation (By similarity). The heterodimer TLR2:TLR6 interacts with CD14 and CD36 in response to triacylated lipopeptides (By similarity). {ECO:0000250|UniProtKB:Q9Y2C9, ECO:0000269|PubMed:19931471, ECO:0000305}. TISSUE SPECIFICITY: Detected in thymus, spleen, ovary and lung. Expressed in macrohpages. {ECO:0000269|PubMed:23812099}. +Q9CQQ0 SMIM8_MOUSE Small integral membrane protein 8 97 11,064 Chain (1); Sequence conflict (1); Transmembrane (1) TRANSMEM 48 67 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q9CU62 SMC1A_MOUSE Structural maintenance of chromosomes protein 1A (SMC protein 1A) (SMC-1-alpha) (SMC-1A) (Chromosome segregation protein SmcB) (Sb1.8) 1233 143,235 Beta strand (10); Chain (1); Coiled coil (4); Compositional bias (1); Domain (1); Helix (14); Modified residue (9); Nucleotide binding (1); Sequence conflict (6); Turn (3) FUNCTION: Involved in chromosome cohesion during cell cycle and in DNA repair. Involved in DNA repair via its interaction with BRCA1 and its related phosphorylation by ATM, and works as a downstream effector in the ATM/NBS1 branch of S-phase checkpoint (By similarity). Central component of cohesin complex. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis. Involved in DNA repair via its interaction with BRCA1 and its related phosphorylation by ATM, or via its phosphorylation by ATR. Works as a downstream effector both in the ATM/NBS1 branch and in the ATR/MSH2 branch of S-phase checkpoint. {ECO:0000250}. PTM: Phosphorylated upon ionizing radiation or DNA methylation. Phosphorylation of Ser-957 and Ser-966 activates it and is required for S-phase checkpoint activation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Chromosome. Chromosome, centromere. Note=Associates with chromatin. The phosphorylated form on Ser-957 and Ser-966 associates with chromatin during G1/S/G2 phases but not during M phase, suggesting that phosphorylation does not regulate cohesin function (By similarity). Before prophase it is scattered along chromosome arms. During prophase, most of cohesin complexes dissociate from chromatin probably because of phosphorylation by PLK, except at centromeres, where cohesin complexes remain. At anaphase, the RAD21 subunit of the cohesin complex is cleaved, leading to the dissociation of the complex from chromosomes, allowing chromosome separation. In germ cells, cohesin complex dissociates from chromatin at prophase I, and may be replaced by a meiosis-specific cohesin complex. {ECO:0000250}. SUBUNIT: Forms a heterodimer with SMC3 in cohesin complexes. Cohesin complexes are composed of the SMC1 (SMC1A or SMC1B) and SMC3 heterodimer attached via their SMC hinge domain, RAD21 which link them, and one STAG protein (STAG1, STAG2 or STAG3), which interacts with RAD21. In germ cell cohesin complexes, SMC1A is mutually exclusive with SMC1B (PubMed:10375619). Interacts with STAG3 (PubMed:11483963). Found in a complex with CDCA5, SMC3 and RAD21, PDS5A/SCC-112 and PDS5B/APRIN. Found in a complex containing POLE and SMC3. Interacts with BRCA1, SYCP2, NDC80, RPGR and BRAT1. Found in a cohesin complex with SMC3, STAG1 and RAD21. The SMC1A-SMC3 heterodimer interacts with the NIPBL-MAU2 heterodimer (By similarity). {ECO:0000250|UniProtKB:O97593, ECO:0000250|UniProtKB:Q14683, ECO:0000250|UniProtKB:Q9Z1M9, ECO:0000269|PubMed:10375619, ECO:0000269|PubMed:11483963}. DOMAIN: The flexible SMC hinge domain, which separates the large intramolecular coiled coil regions, allows the heterotypic interaction with the corresponding domain of SMC3, forming a V-shaped heterodimer. The two heads of the heterodimer are then connected by different ends of the cleavable RAD21 protein, forming a ring structure (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous (at protein level). {ECO:0000269|PubMed:22977523}. +Q9QYZ3 SMK2B_MOUSE Sperm motility kinase 2B (EC 2.7.11.1) 484 54,698 Active site (1); Binding site (1); Chain (1); Domain (2); Nucleotide binding (1) FUNCTION: May play a role in sperm motility, especially in the regulation of flagellar function. {ECO:0000269|PubMed:10647005}. TISSUE SPECIFICITY: Testis-specific. Expressed in the testis from 22 days postpartum (22 dpp). {ECO:0000269|PubMed:10647005}. +Q6P9Z1 SMRD3_MOUSE SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3 (60 kDa BRG-1/Brm-associated factor subunit C) (BRG1-associated factor 60C) (BAF60C) (mBAF60c) 483 54,986 Chain (1); Domain (1); Frameshift (1); Initiator methionine (1); Modified residue (2); Sequence conflict (2) FUNCTION: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner (PubMed:22952240, PubMed:26601204). Stimulates nuclear receptor mediated transcription. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (PubMed:17640523). {ECO:0000250|UniProtKB:Q6STE5, ECO:0000269|PubMed:17640523, ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6STE5}. SUBUNIT: Component of the multiprotein chromatin-remodeling complexes SWI/SNF: SWI/SNF-A (BAF), SWI/SNF-B (PBAF) and related complexes. The canonical complex contains a catalytic subunit (either SMARCA4/BRG1/BAF190A or SMARCA2/BRM/BAF190B) and at least SMARCE1, ACTL6A/BAF53, SMARCC1/BAF155, SMARCC2/BAF170, and SMARCB1/SNF5/BAF47. Other subunits specific to each of the complexes may also be present permitting several possible combinations developmentally and tissue specific (Probable). Component of the BAF complex, which includes at least actin (ACTB), ARID1A/BAF250A, ARID1B/BAF250B, SMARCA2/BRM, SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57, SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C. In muscle cells, the BAF complex also contains DPF3 (By similarity). Component of neural progenitors-specific chromatin remodeling complex (npBAF complex) composed of at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, PHF10/BAF45A, ACTL6A/BAF53A and actin. Component of neuron-specific chromatin remodeling complex (nBAF complex) composed of at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, DPF1/BAF45B, DPF3/BAF45C, ACTL6B/BAF53B and actin (By similarity). May be a component of the SWI/SNF-B (PBAF) chromatin remodeling complex, at least composed of SMARCA4/BRG1, SMARCB1/BAF47/SNF5, ACTL6A/BAF53A or ACTL6B/BAF53B, SMARCE1/BAF57, SMARCD1/BAF60A, SMARCD2/BAF60B, perhaps SMARCD3/BAF60C, SMARCC1/BAF155, SMARCC2/BAF170, PBRM1/BAF180, ARID2/BAF200 and actin (PubMed:22952240, PubMed:26601204). Component of SWI/SNF (GBAF) subcomplex, which includes at least BICRA or BICRAL (mutually exclusive), BRD9, SS18, SMARCA2/BRM, SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, SMARCC1/BAF155, and SMARCD1/BAF60A (PubMed:29374058). Interacts with SMARCA4/BRG1/BAF190A. The precise distribution of the related SMARCD1, SMARCD2 and SMARCD3 proteins among these and other SWI/SNF nucleosome-remodeling complexes is not fully known. May allow recruitment of SWI/SNF containing complexes specifically to promoters where these factors are located. Also interacts with several nuclear receptors including PPARG/NR1C3, RXRA/NR1F1, ESR1, NR5A1, NR5A2/LRH1 and other transcriptional activators including the HLH protein SREBF1/SREBP1 and the homeobox protein PBX1 (By similarity). {ECO:0000250|UniProtKB:Q6STE5, ECO:0000269|PubMed:17640523, ECO:0000269|PubMed:29374058, ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:14701856}. +Q8C0N0 SMKZ_MOUSE Sperm motility kinase Z (EC 2.7.11.1) 497 56,083 Active site (1); Binding site (1); Chain (1); Domain (2); Nucleotide binding (1) FUNCTION: May play a role in sperm motility, especially in the regulation of flagellar function. {ECO:0000250}. +O35979 SMR2D_MOUSE Submaxillary gland androgen-regulated protein 2, isoform delta (Salivary protein MSG2, isoform delta) 143 15,980 Chain (1); Signal peptide (1) FUNCTION: May play a role in protection or detoxification. SUBCELLULAR LOCATION: Secreted. +P97454 SMAD5_MOUSE Mothers against decapentaplegic homolog 5 (MAD homolog 5) (Mothers against DPP homolog 5) (Dwarfin-C) (Dwf-C) (SMAD family member 5) (SMAD 5) (Smad5) (mSmad5) 465 52,172 Beta strand (9); Chain (1); Compositional bias (1); Domain (2); Helix (7); Initiator methionine (1); Metal binding (4); Modified residue (3); Sequence conflict (1) FUNCTION: Transcriptional modulator activated by BMP (bone morphogenetic proteins) type 1 receptor kinase. SMAD5 is a receptor-regulated SMAD (R-SMAD) (By similarity). Required for angiogenesis. {ECO:0000250}. PTM: Phosphorylated on serine by BMP (bone morphogenetic proteins) type 1 receptor kinase.; PTM: Ubiquitin-mediated proteolysis by SMAD-specific E3 ubiquitin ligase SMURF1. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=In the cytoplasm in the absence of ligand. Migration to the nucleus when complexed with SMAD4 (By similarity). {ECO:0000250}. SUBUNIT: May form trimers with the co-SMAD SMAD4. Interacts with PEBP2-alpha subunit and SMURF1. Interacts with SUV39H1 and SUV39H2. Interacts (via MH2 domain) with LEMD3 (By similarity). Interacts with WWP1. Interacts with TMEM119 (PubMed:21239498). Interacts with ZNF8 (PubMed:12370310). Interacts with RANBP3L (By similarity). {ECO:0000250|UniProtKB:Q99717, ECO:0000269|PubMed:12370310, ECO:0000269|PubMed:15221015, ECO:0000269|PubMed:21239498}. +Q9ERB0 SNP29_MOUSE Synaptosomal-associated protein 29 (SNAP-29) (Golgi SNARE of 32 kDa) (Gs32) (Soluble 29 kDa NSF attachment protein) (Vesicle-membrane fusion protein SNAP-29) 260 29,572 Chain (1); Coiled coil (1); Domain (1); Modified residue (8); Sequence conflict (1) FUNCTION: SNAREs, soluble N-ethylmaleimide-sensitive factor-attachment protein receptors, are essential proteins for fusion of cellular membranes. SNAREs localized on opposing membranes assemble to form a trans-SNARE complex, an extended, parallel four alpha-helical bundle that drives membrane fusion. SNAP29 is a SNARE involved in autophagy through the direct control of autophagosome membrane fusion with the lysososome membrane. Plays also a role in ciliogenesis by regulating membrane fusions. {ECO:0000250|UniProtKB:O95721}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O95721}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9Z2P6}; Peripheral membrane protein {ECO:0000305}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:27628032}; Peripheral membrane protein {ECO:0000305}. Cell projection, cilium membrane {ECO:0000250|UniProtKB:O95721}; Peripheral membrane protein {ECO:0000305}. Note=Appears to be mostly membrane-bound, probably via interaction with syntaxins, but a significant portion is cytoplasmic. Localizes to the ciliary pocket from where the cilium protrudes. {ECO:0000250|UniProtKB:O95721}. SUBUNIT: Forms a SNARE complex, composed of VAMP8, SNAP29 and STX17, involved in fusion of autophagosome with lysosome (By similarity). Interacts with multiple syntaxins including STX6 (By similarity). Interacts with EIPR1 (By similarity). {ECO:0000250|UniProtKB:O95721, ECO:0000250|UniProtKB:Q9Z2P6}. +P97496 SMRC1_MOUSE SWI/SNF complex subunit SMARCC1 (BRG1-associated factor 155) (SWI/SNF complex 155 kDa subunit) (SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily C member 1) (SWI3-related protein) (BAF155) 1104 122,890 Alternative sequence (1); Chain (1); Coiled coil (1); Compositional bias (4); Cross-link (7); Domain (2); Frameshift (1); Modified residue (17); Sequence conflict (8) FUNCTION: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. May stimulate the ATPase activity of the catalytic subunit of the complex. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth. {ECO:0000250|UniProtKB:Q92922, ECO:0000269|PubMed:11604513, ECO:0000269|PubMed:17640523, ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Cytoplasm {ECO:0000250|UniProtKB:Q92922}. SUBUNIT: Component of the multiprotein chromatin-remodeling complexes SWI/SNF: SWI/SNF-A (BAF), SWI/SNF-B (PBAF) and related complexes. The canonical complex contains a catalytic subunit (either SMARCA4/BRG1/BAF190A or SMARCA2/BRM/BAF190B) and at least SMARCE1, ACTL6A/BAF53, SMARCC1/BAF155, SMARCC2/BAF170, and SMARCB1/SNF5/BAF47. Other subunits specific to each of the complexes may also be present permitting several possible combinations developmentally and tissue specific (Probable). Component of the BAF complex, which includes at least actin (ACTB), ARID1A/BAF250A, ARID1B/BAF250B, SMARCA2/BRM, SMARCA4/BRG1, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57, SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C. In muscle cells, the BAF complex also contains DPF3 (By similarity). Component of neural progenitors-specific chromatin remodeling complex (npBAF complex) composed of at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, PHF10/BAF45A, ACTL6A/BAF53A and actin. Component of neuron-specific chromatin remodeling complex (nBAF complex) composed of at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, DPF1/BAF45B, DPF3/BAF45C, ACTL6B/BAF53B and actin (PubMed:17640523). Component of the SWI/SNF-B (PBAF) chromatin remodeling complex, at least composed of SMARCA4/BRG1, SMARCB1/BAF47/SNF5, ACTL6A/BAF53A or ACTL6B/BAF53B, SMARCE1/BAF57, SMARCD1/BAF60A, SMARCD2/BAF60B, perhaps SMARCD3/BAF60C, SMARCC1/BAF155, SMARCC2/BAF170, PBRM1/BAF180, ARID2/BAF200 and actin (PubMed:22952240, PubMed:26601204). Component of SWI/SNF (GBAF) subcomplex, which includes at least BICRA or BICRAL (mutually exclusive), BRD9, SS18, SMARCA2/BRM, SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, SMARCC1/BAF155, and SMARCD1/BAF60A (PubMed:29374058). May also interact with the SIN3A histone deacetylase transcription repressor complex in conjunction with SMARCA2 and SMARCA4. The minimal complex composed of SMARCC1 and SMARCA4 seems to be able to associate with cyclin such as CCNE1 or transcription factors such as KLF1 or GATA1. Interacts with NR3C1 and SMARD1. Interacts with TRIP12; leading to disrupt interaction between TRIP12 and SMARCE1 and prevent SMARCE1 ubiquitination (By similarity). Interacts with CEBPB (when not methylated)(PubMed:20111005). Interacts with KDM6B (PubMed:21095589). Interacts with MKKS; the interaction takes place predominantly in the cytoplasm and may modulate SMARCC1 location (By similarity). Interacts with DPF2 (By similarity). {ECO:0000250|UniProtKB:Q92922, ECO:0000269|PubMed:17640523, ECO:0000269|PubMed:20111005, ECO:0000269|PubMed:21095589, ECO:0000269|PubMed:29374058, ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}. TISSUE SPECIFICITY: Highly expressed in adult brain, testis and thymus. +Q9CSN1 SNW1_MOUSE SNW domain-containing protein 1 (Nuclear protein SkiP) (Ski-interacting protein) 536 61,475 Chain (1); Compositional bias (1); Cross-link (17); Initiator methionine (1); Modified residue (10); Region (2) FUNCTION: Involved in pre-mRNA splicing as component of the spliceosome. Is required in the specific splicing of CDKN1A pre-mRNA; the function probably involves the recruitment of U2AF2 to the mRNA. Is proposed to recruit PPIL1 to the spliceosome. May be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. Involved in transcriptional regulation. Modulates TGF-beta-mediated transcription via association with SMAD proteins, MYOD1-mediated transcription via association with PABPN1, RB1-mediated transcriptional repression, and retinoid-X receptor (RXR)- and vitamin D receptor (VDR)-dependent gene transcription in a cell line-specific manner probably involving coactivators NCOA1 and GRIP1. Is involved in NOTCH1-mediated transcriptional activation. Binds to multimerized forms of Notch intracellular domain (NICD) and is proposed to recruit transcriptional coactivators such as MAML1 to form an intermediate preactivation complex which associates with DNA-bound CBF-1/RBPJ to form a transcriptional activation complex by releasing SNW1 and redundant NOTCH1 NICD. {ECO:0000250|UniProtKB:Q13573}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13573}. SUBUNIT: Identified in the spliceosome C complex (By similarity). Associates with U4/U6-U5 tri-small nuclear ribonucleoproteins (U4/U6-U5 tri-snRNPs). Interacts SKI, SMAD2,SMAD3, RBPJ, RB1, PABPN1, MAGEA1, SIRT1, FOXN3, U2AF2, PPIL1, DAXX and ATP1B4. Interacts with VDR and RXRA; preferentially associates with VDR:RXRA heterodimers. Interacts with NCOR2. Interacts with MAML1. Interacts with NOTCH1 NICD; the interaction involves multimerized NOTCH1 NICD. Forms a complex with NOTCH1 NICD and MAML1; the association is dissociated by RBPJ. Associates with positive transcription elongation factor b (P-TEFb). Component of the SNARP complex which consists at least of SNIP1, SNW1, THRAP3, BCLAF1 and PNN (By similarity). {ECO:0000250|UniProtKB:Q13573, ECO:0000269|PubMed:15878163, ECO:0000269|PubMed:17592128}. +Q91YJ2 SNX4_MOUSE Sorting nexin-4 450 51,778 Binding site (4); Chain (1); Domain (1); Modified residue (1) FUNCTION: Involved in the regulation of endocytosis and in several stages of intracellular trafficking. Plays a role in recycling endocytosed transferrin receptor and prevent its degradation. {ECO:0000250|UniProtKB:O95219}. SUBCELLULAR LOCATION: Early endosome {ECO:0000250|UniProtKB:O95219}. Early endosome membrane {ECO:0000250|UniProtKB:O95219}; Peripheral membrane protein {ECO:0000250|UniProtKB:O95219}; Cytoplasmic side {ECO:0000250|UniProtKB:O95219}. SUBUNIT: Interacts with WWC1/KIBRA. Identified in a complex with WWC1/KIBRA and dynein components DYNLL1 and DYNC1I2 (By similarity). Interacts with BIN1 (PubMed:12668730). {ECO:0000250|UniProtKB:O95219, ECO:0000269|PubMed:12668730}. DOMAIN: The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization. {ECO:0000250}. +O70493 SNX12_MOUSE Sorting nexin-12 (SDP8 protein) 165 19,116 Binding site (4); Chain (1); Domain (1); Initiator methionine (1); Modified residue (3); Sequence conflict (2) FUNCTION: May be involved in several stages of intracellular trafficking. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. DOMAIN: The PX domain mediates interaction with membranes enriched in phosphatidylinositol 3-phosphate. {ECO:0000250}. +Q7M713 TR116_MOUSE Taste receptor type 2 member 116 (T2R116) (TRB1) (mT2R56) (TRB4) 305 35,095 Chain (1); Glycosylation (3); Sequence conflict (2); Topological domain (8); Transmembrane (7) TRANSMEM 9 29 Helical; Name=1. {ECO:0000255}.; TRANSMEM 56 76 Helical; Name=2. {ECO:0000255}.; TRANSMEM 102 122 Helical; Name=3. {ECO:0000255}.; TRANSMEM 129 149 Helical; Name=4. {ECO:0000255}.; TRANSMEM 185 205 Helical; Name=5. {ECO:0000255}.; TRANSMEM 237 257 Helical; Name=6. {ECO:0000255}.; TRANSMEM 262 282 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 8 Extracellular. {ECO:0000255}.; TOPO_DOM 30 55 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 77 101 Extracellular. {ECO:0000255}.; TOPO_DOM 123 128 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 150 184 Extracellular. {ECO:0000255}.; TOPO_DOM 206 236 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 258 261 Extracellular. {ECO:0000255}.; TOPO_DOM 283 305 Cytoplasmic. {ECO:0000255}. FUNCTION: Putative taste receptor which may play a role in the perception of bitterness. {ECO:0000305}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q62230 SN_MOUSE Sialoadhesin (Sheep erythrocyte receptor) (SER) (Sialic acid-binding Ig-like lectin 1) (Siglec-1) (CD antigen CD169) 1695 182,979 Alternative sequence (4); Beta strand (11); Binding site (2); Chain (1); Disulfide bond (18); Domain (17); Frameshift (2); Glycosylation (15); Helix (3); Motif (1); Mutagenesis (3); Region (1); Sequence conflict (21); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (2) TRANSMEM 1640 1660 Helical. {ECO:0000255}. TOPO_DOM 20 1639 Extracellular. {ECO:0000255}.; TOPO_DOM 1661 1695 Cytoplasmic. {ECO:0000255}. FUNCTION: Acts as an endocytic receptor mediating clathrin dependent endocytosis. Macrophage-restricted adhesion molecule that mediates sialic-acid dependent binding to lymphocytes, including granulocytes, monocytes, natural killer cells, B-cells and CD8 T-cells (By similarity). Preferentially binds to alpha-2,3-linked sialic acid. Binds to SPN/CD43 on T-cells. May play a role in hematopoiesis. May act as a counter-receptor for CLEC10A in lymph node. {ECO:0000250, ECO:0000269|PubMed:15364954}. SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Isoform 2: Secreted.; SUBCELLULAR LOCATION: Isoform 3: Secreted. SUBUNIT: Interacts with CLEC10A. {ECO:0000269|PubMed:11238599, ECO:0000269|PubMed:12737821, ECO:0000269|PubMed:15364954, ECO:0000269|PubMed:15488769, ECO:0000269|PubMed:9660955}. TISSUE SPECIFICITY: Detected in lymph node in the subcapsular sinus, interfollicular regions, and T and B-cell boundary (at protein level). Expressed by macrophages in various tissues. Highest expression in spleen and lymph node with lower amounts in lung, liver, bone marrow, heart and skin. No expression in thymus, kidney, brain or small intestine. {ECO:0000269|PubMed:15364954}. +Q99J94 SO1A6_MOUSE Solute carrier organic anion transporter family member 1A6 (Kidney-specific organic anion-transporting polypeptide 5) (OATP-5) (Solute carrier family 21 member 13) 670 74,145 Chain (1); Disulfide bond (3); Domain (1); Glycosylation (5); Modified residue (3); Sequence conflict (2); Topological domain (13); Transmembrane (12) TRANSMEM 21 40 Helical; Name=1. {ECO:0000255}.; TRANSMEM 60 80 Helical; Name=2. {ECO:0000255}.; TRANSMEM 87 111 Helical; Name=3. {ECO:0000255}.; TRANSMEM 156 184 Helical; Name=4. {ECO:0000255}.; TRANSMEM 204 224 Helical; Name=5. {ECO:0000255}.; TRANSMEM 243 267 Helical; Name=6. {ECO:0000255}.; TRANSMEM 312 333 Helical; Name=7. {ECO:0000255}.; TRANSMEM 354 377 Helical; Name=8. {ECO:0000255}.; TRANSMEM 382 405 Helical; Name=9. {ECO:0000255}.; TRANSMEM 514 536 Helical; Name=10. {ECO:0000255}.; TRANSMEM 546 571 Helical; Name=11. {ECO:0000255}.; TRANSMEM 606 623 Helical; Name=12. {ECO:0000255}. TOPO_DOM 1 20 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 41 59 Extracellular. {ECO:0000255}.; TOPO_DOM 81 86 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 112 155 Extracellular. {ECO:0000255}.; TOPO_DOM 185 203 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 225 242 Extracellular. {ECO:0000255}.; TOPO_DOM 268 311 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 334 353 Extracellular. {ECO:0000255}.; TOPO_DOM 378 381 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 406 513 Extracellular. {ECO:0000255}.; TOPO_DOM 537 545 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 572 605 Extracellular. {ECO:0000255}.; TOPO_DOM 624 670 Cytoplasmic. {ECO:0000255}. FUNCTION: May mediate the Na(+)-independent transport of organic anions. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Kidney specific. +Q9QX47 SON_MOUSE Protein SON (Negative regulatory element-binding protein) (NRE-binding protein) 2444 265,651 Alternative sequence (4); Chain (1); Cross-link (4); Domain (2); Initiator methionine (1); Modified residue (40); Region (7); Repeat (23); Sequence caution (1); Sequence conflict (9) FUNCTION: RNA-binding protein that acts as a mRNA splicing cofactor by promoting efficient splicing of transcripts that possess weak splice sites. Specifically promotes splicing of many cell-cycle and DNA-repair transcripts that possess weak splice sites, such as TUBG1, KATNB1, TUBGCP2, AURKB, PCNT, AKT1, RAD23A, and FANCG. Probably acts by facilitating the interaction between Serine/arginine-rich proteins such as SRSF2 and the RNA polymerase II. Also binds to DNA; binds to the consensus DNA sequence: 5'-GA[GT]AN[CG][AG]CC-3' (By similarity). Essential for correct RNA splicing of multiple genes critical for brain development, neuronal migration and metabolism, including TUBG1, FLNA, PNKP, WDR62, PSMD3, PCK2, PFKL, IDH2, and ACY1 (By similarity). May also regulate the ghrelin signaling in hypothalamic neuron by acting as a negative regulator of GHSR expression (PubMed:20876580). {ECO:0000250|UniProtKB:P18583, ECO:0000269|PubMed:20876580}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:P18583}. Note=Colocalizes with the pre-mRNA splicing factor SRSF2. {ECO:0000250|UniProtKB:P18583}. SUBUNIT: Interacts with SRSF2. Associates with the spliceosome (By similarity). {ECO:0000250|UniProtKB:P18583}. DOMAIN: Contains 8 types of repeats which are distributed in 3 regions. TISSUE SPECIFICITY: Widely expressed. Highly expressed in brain, heart, spleen, liver, skeletal muscle, kidney and testis. {ECO:0000269|PubMed:20876580}. +Q62245 SOS1_MOUSE Son of sevenless homolog 1 (SOS-1) (mSOS-1) 1319 150,883 Beta strand (11); Chain (1); Compositional bias (1); Domain (4); Helix (2); Modified residue (8); Turn (2) FUNCTION: Promotes the exchange of Ras-bound GDP by GTP. Probably by promoting Ras activation, regulates phosphorylation of MAP kinase MAPK3 in response to EGF (By similarity). Catalytic component of a trimeric complex that participates in transduction of signals from Ras to Rac by promoting the Rac-specific guanine nucleotide exchange factor (GEF) activity (PubMed:10499589, PubMed:11524436). {ECO:0000250|UniProtKB:Q07889, ECO:0000269|PubMed:10499589, ECO:0000269|PubMed:11524436}. PTM: Phosphorylation at Ser-1120 and Ser-1147 by RPS6KA3 create YWHAB and YWHAE binding sites and which contribute to the negative regulation of EGF-induced MAPK1/3 phosphorylation. {ECO:0000250|UniProtKB:Q07889}. SUBUNIT: Interacts (via C-terminus) with GRB2 (via SH3 domain). Forms a complex with phosphorylated MUC1 and GRB2 (via its SH3 domains). Interacts with phosphorylated LAT2. Interacts with NCK1 and NCK2 (By similarity). Part of a complex consisting of ABI1, EPS8 and SOS1 (PubMed:10499589, PubMed:11524436). Interacts (Ser-1120 and Ser-1147 phosphorylated form) with YWHAB and YWHAE (By similarity). {ECO:0000250|UniProtKB:Q07889, ECO:0000269|PubMed:10499589, ECO:0000269|PubMed:11524436}. TISSUE SPECIFICITY: Expressed in most embryonic and adult tissues. +Q8QZR0 TR1L1_MOUSE Translocating chain-associated membrane protein 1-like 1 363 40,983 Chain (1); Domain (1); Sequence conflict (1); Topological domain (9); Transmembrane (8) TRANSMEM 30 50 Helical. {ECO:0000255}.; TRANSMEM 81 101 Helical. {ECO:0000255}.; TRANSMEM 121 141 Helical. {ECO:0000255}.; TRANSMEM 160 179 Helical. {ECO:0000255}.; TRANSMEM 192 214 Helical. {ECO:0000255}.; TRANSMEM 219 241 Helical. {ECO:0000255}.; TRANSMEM 251 271 Helical. {ECO:0000255}.; TRANSMEM 296 316 Helical. {ECO:0000255}. TOPO_DOM 1 29 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 51 80 Lumenal. {ECO:0000255}.; TOPO_DOM 102 120 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 142 159 Lumenal. {ECO:0000255}.; TOPO_DOM 180 191 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 215 218 Lumenal. {ECO:0000255}.; TOPO_DOM 242 250 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 272 295 Lumenal. {ECO:0000255}.; TOPO_DOM 317 363 Cytoplasmic. {ECO:0000255}. FUNCTION: Stimulatory or required for the translocation of secretory proteins across the ER membrane. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q8BGW5 SOSB2_MOUSE SOSS complex subunit B2 (Nucleic acid-binding protein 1) (Oligonucleotide/oligosaccharide-binding fold-containing protein 2A) (Sensor of single-strand DNA complex subunit B2) (Sensor of ssDNA subunit B2) (SOSS-B2) (Single-stranded DNA-binding protein 2) 198 21,749 Alternative sequence (1); Chain (1); DNA binding (1); Sequence conflict (1) FUNCTION: Component of the SOSS complex, a multiprotein complex that functions downstream of the MRN complex to promote DNA repair and G2/M checkpoint. In the SOSS complex, acts as a sensor of single-stranded DNA that binds to single-stranded DNA, in particular to polypyrimidines. The SOSS complex associates with DNA lesions and influences diverse endpoints in the cellular DNA damage response including cell-cycle checkpoint activation, recombinational repair and maintenance of genomic stability. Required for efficient homologous recombination-dependent repair of double-strand breaks (DSBs) and ATM-dependent signaling pathways (By similarity). {ECO:0000250, ECO:0000269|PubMed:16533169}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16533169}. Note=Localizes to nuclear foci following DNA damage. {ECO:0000250}. SUBUNIT: Component of the SOSS complex, composed of SOSS-B (SOSS-B1/NABP2 or SOSS-B2/NABP1), SOSS-A/INTS3 and SOSS-C/INIP. SOSS complexes containing SOSS-B1/NABP2 are more abundant than complexes containing SOSS-B2/NABP1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous with high expression in the thymus. {ECO:0000269|PubMed:16533169}. +O88307 SORL_MOUSE Sortilin-related receptor (Gp250) (Low-density lipoprotein receptor relative with 11 ligand-binding repeats) (LDLR relative with 11 ligand-binding repeats) (LR11) (SorLA-1) (Sorting protein-related receptor containing LDLR class A repeats) (mSorLA) 2215 247,086 Chain (1); Disulfide bond (33); Domain (18); Glycosylation (28); Modified residue (2); Motif (1); Propeptide (1); Repeat (10); Sequence conflict (19); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 2139 2159 Helical. {ECO:0000255}. TOPO_DOM 82 2138 Extracellular. {ECO:0000255}.; TOPO_DOM 2160 2215 Cytoplasmic. {ECO:0000255}. FUNCTION: Likely to be a multifunctional endocytic receptor, that may be implicated in the uptake of lipoproteins and of proteases. Binds LDL, the major cholesterol-carrying lipoprotein of plasma, and transports it into cells by endocytosis. Binds the receptor-associated protein (RAP). Could play a role in cell-cell interaction. May play a role in neural organization, as well as the establishment of embryonic organ systems. Involved in APP trafficking to and from the Golgi apparatus (By similarity). It probably acts as a sorting receptor that protects APP from trafficking to late endosome and from processing into amyloid beta (By similarity). Involved in the regulation of smooth muscle cells migration, probably through PLAUR binding and decreased internalization. {ECO:0000250, ECO:0000269|PubMed:14764453}. PTM: The propeptide removed in the N-terminus may be cleaved by furin or homologous proteases. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Golgi apparatus {ECO:0000250}. Endosome {ECO:0000250}. Secreted {ECO:0000250}. SUBUNIT: Interacts with GGA1 and ROCK2 (By similarity). Interacts with APP. Interacts with PLAUR (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Abundant in brain, where it is mainly expressed in adult cerebellum, hippocampal ca regions, dentate gyrus, and to a much lesser extent in the cerebral cortex. Detectable in kidney, skeletal muscle, lung and spleen, but not in the liver. +Q0P5V2 SOBP_MOUSE Sine oculis-binding protein homolog (Jackson circler protein 1) 864 91,784 Chain (1); Compositional bias (2); Cross-link (1); Modified residue (2); Motif (2); Zinc finger (2) FUNCTION: Implicated in development of the cochlea. {ECO:0000269|Ref.1}. SUBUNIT: Interacts (via SIM domains) with SUMO1 and SUMO2. {ECO:0000250}. +P86448 TR43B_MOUSE Tripartite motif-containing protein 43B 445 52,238 Chain (1); Domain (1); Zinc finger (2) +P06880 SOMA_MOUSE Somatotropin (Growth hormone) 216 24,716 Chain (1); Disulfide bond (2); Metal binding (2); Modified residue (1); Signal peptide (1) FUNCTION: Plays an important role in growth control. Its major role in stimulating body growth is to stimulate the liver and other tissues to secrete IGF-1. It stimulates both the differentiation and proliferation of myoblasts. It also stimulates amino acid uptake and protein synthesis in muscle and other tissues. SUBCELLULAR LOCATION: Secreted. +Q04892 SOX14_MOUSE Transcription factor SOX-14 240 26,515 Chain (1); DNA binding (1) FUNCTION: Acts as a negative regulator of transcription. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}. TISSUE SPECIFICITY: Highly expressed in developing brain and spinal cord. {ECO:0000269|PubMed:10677261}. +Q61473 SOX17_MOUSE Transcription factor SOX-17 419 44,646 Alternative sequence (1); Beta strand (1); Chain (1); Compositional bias (2); DNA binding (1); Domain (1); Helix (3) FUNCTION: Acts as transcription regulator that binds target promoter DNA and bends the DNA. Binds to the sequences 5'-AACAAT-'3 or 5'-AACAAAG-3'. Modulates transcriptional regulation via WNT3A. Inhibits Wnt signaling. Promotes degradation of activated CTNNB1. Plays a key role in the regulation of embryonic development. Required for normal looping of the embryonic heart tube. Required for normal development of the definitive gut endoderm. Probable transcriptional activator in the premeiotic germ cells. Isoform 2 (T-SOX17) shows no DNA-binding activity. {ECO:0000269|PubMed:20802155}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267, ECO:0000269|PubMed:20802155}. SUBUNIT: Interacts with CTNNB1, LEF1 and TCF4. {ECO:0000269|PubMed:19328208, ECO:0000269|PubMed:20802155}. TISSUE SPECIFICITY: Testis. Detected in lung. +Q04886 SOX8_MOUSE Transcription factor SOX-8 464 49,879 Chain (1); DNA binding (1) FUNCTION: May play a role in central nervous system, limb and facial development. May be involved in male sex determination. Binds the consensus motif 5'-[AT][AT]CAA[AT]G-3'. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}. TISSUE SPECIFICITY: Brain, gut, limb, and testes. Slightly in liver, ovaries, spinal cord, lung and heart. +Q8BVK9 SP110_MOUSE Sp110 nuclear body protein (Intracellular pathogen resistance protein 1) 445 50,140 Beta strand (2); Chain (1); Domain (2); Helix (5); Modified residue (4); Motif (1); Sequence caution (1); Sequence conflict (13) FUNCTION: May act as a transcription factor. Plays a role in the innate immunity against intracellular pathogens. Required for resistance to M.tuberculosis and L.monocytogenes. Promotes apoptosis of infected cells. {ECO:0000269|PubMed:15815631}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00185, ECO:0000255|PROSITE-ProRule:PRU00747}. TISSUE SPECIFICITY: Detected in lung and macrophages. {ECO:0000269|PubMed:15815631}. DISEASE: Note=Defects in Sp110 are a cause of severely impaired resistance to infection by M.tuberculosis. {ECO:0000269|PubMed:15815631}. +P53783 SOX1_MOUSE Transcription factor SOX-1 391 39,053 Chain (1); Compositional bias (6); DNA binding (1); Sequence conflict (2) FUNCTION: Transcriptional activator. May function as a switch in neuronal development. Keeps neural cells undifferentiated by counteracting the activity of proneural proteins and suppresses neuronal differentiation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: Mainly in the developing central nervous system. Expressed in developing urogenital ridge. +O89090 SP1_MOUSE Transcription factor Sp1 (Specificity protein 1) 784 80,732 Alternative sequence (1); Chain (1); Compositional bias (2); Cross-link (2); Glycosylation (6); Initiator methionine (1); Modified residue (18); Region (6); Sequence conflict (4); Site (1); Zinc finger (3) FUNCTION: Transcription factor that can activate or repress transcription in response to physiological and pathological stimuli. Binds with high affinity to GC-rich motifs and regulates the expression of a large number of genes involved in a variety of processes such as cell growth, apoptosis, differentiation and immune responses. Highly regulated by post-translational modifications (phosphorylations, sumoylation, proteolytic cleavage, glycosylation and acetylation). Binds also the PDGFR-alpha G-box promoter. May have a role in modulating the cellular response to DNA damage. Implicated in chromatin remodeling. Plays a role in the recruitment of SMARCA4/BRG1 on the c-FOS promoter Plays an essential role in the regulation of FE65 gene expression (By similarity). Positively regulates the transcription of the core clock component ARNTL/BMAL1 (PubMed:24030830). Plays a role in protecting cells against oxidative stress following brain injury by regulating the expression of RNF112 (PubMed:27918959). {ECO:0000250|UniProtKB:P08047, ECO:0000250|UniProtKB:Q01714, ECO:0000269|PubMed:24030830, ECO:0000269|PubMed:27918959}. PTM: Phosphorylated on multiple serine and threonine residues. Phosphorylation is coupled to ubiquitination, sumoylation and proteolytic processing. Phosphorylation on Ser-61 enhances proteolytic cleavage. Phosphorylation on Ser-7 enhances ubiquitination and protein degradation. Hyperphosphorylation on Ser-103 in response to DNA damage has no effect on transcriptional activity. MAPK1/MAPK3-mediated phosphorylation on Thr-455 and Thr-738 enhances VEGF transcription but, represses FGF2-triggered PDGFR-alpha transcription. Also implicated in the repression of RECK by ERBB2. Hyperphosphorylated on Thr-280 and Thr-738 during mitosis by MAPK8 shielding SP1 from degradation by the ubiquitin-dependent pathway. Phosphorylated in the zinc-finger domain by calmodulin-activated PKCzeta. Phosphorylation on Ser-642 by PKCzeta is critical for TSA-activated LHR gene expression through release of its repressor, p107. Phosphorylation on Thr-669, Ser-671 and Thr-682 is stimulated by angiotensin II via the AT1 receptor inducing increased binding to the PDGF-D promoter. This phosphorylation is increased in injured artey wall. Ser-61 and Thr-682 can both be dephosphorylated by PP2A during cell-cycle interphase. Dephosphorylation on Ser-61 leads to increased chromatin association during interphase and increases the transcriptional activity. On insulin stimulation, sequentially glycosylated and phosphorylated on several C-terminal serine and threonine residues (By similarity). {ECO:0000250}.; PTM: Acetylated. Acetylation/deacetylation events affect transcriptional activity. Deacetylation leads to an increase in the expression the 12(s)-lipooxygenase gene though recruitment of p300 to the promoter (By similarity). {ECO:0000250}.; PTM: Ubiquitinated. Ubiquitination occurs on the C-terminal proteolytically-cleaved peptide and is triggered by phosphorylation (By similarity). {ECO:0000250}.; PTM: Sumoylated with SUMO1. Sumoylation modulates proteolytic cleavage of the N-terminal repressor domain. Sumoylation levels are attenuated during tumorigenesis. Phosphorylation mediates SP1 desumoylation (By similarity). {ECO:0000250}.; PTM: Proteolytic cleavage in the N-terminal repressor domain is prevented by sumoylation. The C-terminal cleaved product is susceptible to degradation (By similarity). {ECO:0000250}.; PTM: O-glycosylated; Contains 8 N-acetylglucosamine side chains. Levels are controlled by insulin and the SP1 phosphorylation states. Insulin-mediated O-glycosylation locates SP1 to the nucleus, where it is sequentially deglycosylated and phosphorylated. O-glycosylation affects transcriptional activity through disrupting the interaction with a number of transcription factors including ELF1 and NFYA. Inhibited by peroxisomome proliferator receptor gamma (PPARgamma) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27918959}. Cytoplasm {ECO:0000250}. Note=Nuclear location is governed by glycosylated/phosphorylated states. Insulin promotes nuclear location, while glucagon favors cytoplasmic location (By similarity). {ECO:0000250}. SUBUNIT: Interacts with ATF7IP, ATF7IP2, BAHD1, POGZ, HCFC1, AATF and PHC2. Interacts with SV40 VP2/3 proteins. Interacts with SV40 major capsid protein VP1; this interaction leads to a cooperativity between the 2 proteins in DNA binding. Interacts with HLTF; the interaction may be required for basal transcriptional activity of HLTF. Interacts (deacetylated form) with EP300; the interaction enhances gene expression. Interacts with HDAC1 and JUN. Interacts with ELF1; the interaction is inhibited by glycosylation of SP1. Interaction with NFYA; the interaction is inhibited by glycosylation of SP1. Interacts with SMARCA4/BRG1. Interacts with ATF7IP and TBP. Interacts with MEIS2 isoform 4 and PBX1 isoform PBX1a. Interacts with EGR1 (By similarity). Interacts with RNF112 in an oxidative stress-regulated manner (PubMed:27918959). Interacts with ZBTB7A; ZBTB7A prevents the binding to GC-rich motifs in promoters and represses the transcriptional activity of SP1 (By similarity). {ECO:0000250|UniProtKB:P08047, ECO:0000250|UniProtKB:Q01714, ECO:0000269|PubMed:27918959}.; SUBUNIT: (Microbial infection) Interacts with murine minute virus NS1; this interaction allows high levels of viral P38 promoter transactivation by NS1. {ECO:0000269|PubMed:7799962, ECO:0000269|PubMed:9454706}. +Q3UDK1 TRAD1_MOUSE TRAF-type zinc finger domain-containing protein 1 (Protein FLN29) 580 64,283 Alternative sequence (1); Chain (1); Compositional bias (1); Initiator methionine (1); Modified residue (11); Mutagenesis (1); Sequence conflict (2); Zinc finger (1) FUNCTION: Negative feedback regulator that controls excessive innate immune responses. Regulates both Toll-like receptor 4 (TLR4) and DDX58/RIG1-like helicases (RLH) pathways. May inhibit the LTR pathway by direct interaction with TRAF6 and attenuation of NF-kappa-B activation. May negatively regulate the RLH pathway downstream from MAVS and upstream of NF-kappa-B and IRF3. {ECO:0000269|PubMed:16221674, ECO:0000269|PubMed:18849341}. SUBUNIT: Interacts with MAVS, TICAM1, TRAF1, TRAF2, TRAF3 and TRAF6. {ECO:0000269|PubMed:16221674, ECO:0000269|PubMed:18849341}. TISSUE SPECIFICITY: Expressed in skeletal muscle, brain, liver, kidney, spleen and bone marrow. Expression depends on STAT1. {ECO:0000269|PubMed:16221674}. +Q9D2H6 SP2_MOUSE Transcription factor Sp2 612 64,908 Alternative sequence (1); Chain (1); Erroneous initiation (3); Modified residue (1); Sequence conflict (2); Zinc finger (3) FUNCTION: Binds to GC box promoters elements and selectively activates mRNA synthesis from genes that contain functional recognition sites. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +Q3U0V2 TRADD_MOUSE Tumor necrosis factor receptor type 1-associated DEATH domain protein (TNFR1-associated DEATH domain protein) (TNFRSF1A-associated via death domain) 310 34,577 Chain (1); Domain (1); Motif (2); Mutagenesis (1); Region (1) FUNCTION: Adapter molecule for TNFRSF1A/TNFR1 that specifically associates with the cytoplasmic domain of activated TNFRSF1A/TNFR1 mediating its interaction with FADD. Overexpression of TRADD leads to two major TNF-induced responses, apoptosis and activation of NF-kappa-B (By similarity). The nuclear form acts as a tumor suppressor by preventing ubiquitination and degradation of isoform p19ARF/ARF of CDKN2A by TRIP12: acts by interacting with TRIP12, leading to disrupt interaction between TRIP12 and isoform p19ARF/ARF of CDKN2A. {ECO:0000250, ECO:0000269|PubMed:22561347}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, cytoskeleton. Note=Shuttles between the cytoplasm and the nucleus. SUBUNIT: Stimulation of TNF-alpha receptor TNFRSF1A leads to the formation of two distinct signaling complexes. Plasma membrane-bound complex I is composed of TNFRSF1A, TRADD, RIPK1, TRAF2 and BIRC2/c-IAP1 or BIRC3 which interacts with CHUCK/IKK-alpha, IKBKB/IKK-beta and IKBKG/IKK-gamma promoting cell survival (PubMed:14585990). Subsequently, TRADD, RIPK1 and TRAF2 dissociate from TNFRSF1A and form cytoplasmic complex II with FADD and caspase CASP8 promoting cell apoptosis (By similarity). Within complex I, interacts with TNFRSF1A/TNFR1, TRAF2 and kinase RIPK1 (By similarity). Within complex I, interacts with TRPC4AP; the interaction promotes NF-kappa B activation (PubMed:14585990). UXT1 associates with complex I; the interaction prevents the formation of complex II (By similarity). Within complex I Interacts with scaffold protein DAB2IP (By similarity). Interacts with autophagy receptor SQSTM1 (By similarity). Interacts with E3 ligase TRIP12 (PubMed:22561347). Interacts with kinase HIPK2 (By similarity). Interacts with keratin KRT14 (PubMed:16702408). Interacts with keratin KRT18 (By similarity). Interacts with KRT16 and KRT17 (PubMed:16702408). {ECO:0000250|UniProtKB:Q15628, ECO:0000269|PubMed:14585990, ECO:0000269|PubMed:16702408, ECO:0000269|PubMed:22561347}. DOMAIN: Requires the intact death domain to associate with TNFRSF1A/TNFR1. {ECO:0000250}. +P39429 TRAF2_MOUSE TNF receptor-associated factor 2 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF2) (RING-type E3 ubiquitin transferase TRAF2) 501 56,026 Alternative sequence (1); Chain (1); Coiled coil (1); Cross-link (1); Domain (1); Initiator methionine (1); Modified residue (6); Mutagenesis (4); Region (1); Zinc finger (3) Protein modification; protein ubiquitination. FUNCTION: Regulates activation of NF-kappa-B and JNK and plays a central role in the regulation of cell survival and apoptosis. Required for normal antibody isotype switching from IgM to IgG. Has E3 ubiquitin-protein ligase activity and promotes 'Lys-63'-linked ubiquitination of target proteins, such as BIRC3, RIPK1 and TICAM1. Is an essential constituent of several E3 ubiquitin-protein ligase complexes, where it promotes the ubiquitination of target proteins by bringing them into contact with other E3 ubiquitin ligases. Regulates BIRC2 and BIRC3 protein levels by inhibiting their autoubiquitination and subsequent degradation; this does not depend on the TRAF2 RING-type zinc finger domain. Isoform 2 does not seem to mediate activation of NF-kappa-B but inhibits isoform 1 activity. Plays a role in mediating activation of NF-kappa-B by EIF2AK2/PKR. In complex with BIRC2 or BIRC3, promotes ubiquitination of IKBKE. {ECO:0000269|PubMed:10514016, ECO:0000269|PubMed:15121867, ECO:0000269|PubMed:15175328, ECO:0000269|PubMed:18997792, ECO:0000269|PubMed:18997794, ECO:0000269|PubMed:19409903, ECO:0000269|PubMed:19815541, ECO:0000269|PubMed:9390694}. PTM: Phosphorylated at several serine residues within the first 128 amino acid residues. Phosphorylated at Thr-117 in response to signaling via TNF and TNFRSF1A. Phosphorylation at Thr-117 is required for 'Lys-63'-linked polyubiquitination, but not for 'Lys-48'-linked polyubiquitination. Phosphorylation at Thr-117 is important for interaction with IKKA and IKKB, activation of IKK and subsequent activation of NF-kappa-B. {ECO:0000250|UniProtKB:Q12933}.; PTM: Undergoes both 'Lys-48'-linked and 'Lys-63'-linked polyubiquitination. Polyubiquitinated via 'Lys-63'-linked ubiquitin in response to TNF signaling; this requires prior phosphorylation at Thr-117. 'Lys-63'-linked polyubiquitination promotes TRAF2-mediated activation of NF-kappa-B. Can be polyubiquitinated at several Lys residues via 'Lys-48'-linked ubiquitin chains in response to TNF signaling, leading to proteasomal degradation. Autoubiquitinated, leading to its subsequent proteasomal degradation. Polyubiquitinated by BIRC2 and SIAH2, leading to its subsequent proteasomal degradation. Not ubiquitinated by BIRC3 or SIAH1. Deubiquitinated by CYLD, a protease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. {ECO:0000250|UniProtKB:Q12933}. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Homotrimer (By similarity). Heterotrimer with TRAF1 (PubMed:8069916). Heterotrimer with TRAF3 (via TRAF domain) (By similarity). The domain containing the RING-type and the first TRAF-type zinc finger can also form homodimers (in vitro) (By similarity). Interacts with TNFRSF1B/TNFR2 (PubMed:8069916). Interacts with TNFRSF5/CD40 (PubMed:11909853). Interacts with TNFRSF4, TNFRSF7/CD27, TNFRSF8/CD30, TNFRSF9/CD137, TNFRSF11A/RANK, TNFRSF13B/TACI, TNFRSF14, TNFRSF16/NGFR, TNFRSF17/BCMA, TNFRSF18/AITR, TNFRSF19/TROY, TNFRSF19L/RELT, EDAR and IL15RA (By similarity). Stimulation of TNF-alpha receptor TNFRSF1A leads to the formation of two distinct signaling complexes. Plasma membrane-bound complex I is composed of TNFRSF1A, TRADD, RIPK1, TRAF2 and BIRC2/c-IAP1 or BIRC3 which interacts with CHUCK/IKK-alpha, IKBKB/IKK-beta and IKBKG/IKK-gamma promoting cell survival (PubMed:19150425, PubMed:19815541). Subsequently, TRADD, RIPK1 and TRAF2 dissociate from TNFRSF1A and form cytoplasmic complex II with FADD and caspase CASP8 promoting cell apoptosis (By similarity). Interacts with TRADD (PubMed:8565075). Identified in a complex with TNFRSF1A, RIPK1 and IKBKB/IKK-beta (By similarity). Interacts with RIPK2 (By similarity). Interacts with BIRC2 and BIRC3 N-terminus; a single BIRC2 or BIRC3 molecule interacts with a heterotrimer formed by TRAF1 and TRAF2, or a TRAF2 homotrimer (By similarity). Identified in a complex composed of TRAF2, TRAF3, BIRC2 and BIRC3 (PubMed:18997794). Interacts with BIRC2; the interaction promotes BIRC2 stability (PubMed:19506082). Interaction with BIRC2 and/or BIRC3 is essential for ubiquitination of IKBKE, degradation of NFKBIA and activation of NF-kappa-B (PubMed:19815541). Within complex I, phosphorylated TRAF2 interacts (via 'Lys-63'-linked polyubiquitin chains) with CHUCK/IKK-alpha, IKBKB/IKK-beta, IKBKG/IKK-gamma TAB2, TAB3 and TAK1 in response to TNF-alpha stimulation (PubMed:19150425). Within complex I, interacts with UXT isoform 1 (via TPQE motif); the interaction prevents the recruitment of FADD and CASP8/caspase 8 to complex I (PubMed:21307340). Forms a complex composed of TNFRSF8/CD30 or TNFRSF1B/TNFR2, and TRAF1, TRAF2 and E3 ligase TRAIP (PubMed:9104814). Within the complex, interacts with TRAIP; the interaction inhibits TRAF2-mediated NF-kappa B activation (PubMed:9104814). Component of a complex composed of TANK and TBK1 (By similarity). Interacts with TRPC4AP (PubMed:16876162). Interacts with MAP3K1/MEKK1, MAP3K5/ASK1 and MAP3K11/MLK3 in response to TNF-alpha stimulation; the interaction leads to JNK activation (By similarity). Component of a complex composed of MAP3K14/NIK BIRC3 and TRAF3; the interaction leads to BIRC2/3-mediated ubiquitination of TRAF3 upon CD40 engagement in a TRAF2-dependent manner (PubMed:18997792). Interacts with MAP3K14/NIK in response to TNF-alpha stimulation; the interaction leads to NF-kappa B activation (By similarity). Interacts with PEG3; the interaction may promote TRAF2-mediated NF-kappa B activation (PubMed:9500555). Interacts with HIVEP3; the interaction may inhibit TNF-alpha-TRAF2-mediated NF-kappa B and JNK activation (PubMed:11804591). Interacts with TANK/ITRAF; the interaction prevents interaction between TNFRSF1B/TNFR2 and TRAF2 (By similarity). Interacts with deubiquitinating enzyme CYLD; the interaction results in the deubiquitination and inactivation of TRAF2 (By similarity). Interacts with SIAH2; the interaction leads to TRAF2 ubiquitination and degradation (By similarity). Interacts with E2 conjugating enzyme UBE2N/Ubc13, E3 ligase ITCH and RNF11 in response to TNF-alpha stimulation (By similarity). Interacts with ubiquitin-editing enzyme TNFAIP3/A20 in response to TNF-alpha stimulation; the interaction promotes TRAF2 dissociation from UBE2N/Ubc13, ITCH, RNF11 and TAX1BP1 and prevents prolonged TRAF-2 ubiquitination (PubMed:8692885, PubMed:20185725). Interacts with TAX1BP1 in response to TNF-alpha stimulation; the interaction promotes TRAF2 dissociation from UBE2N/Ubc13 and TNFAIP3/A20, and prevents prolonged TRAF-2 ubiquitination (PubMed:20185725). Interacts (via C-terminus) with EIF2AK2/PKR (via the kinase catalytic domain) (By similarity). Interacts with deubiquitinating enzyme USP48 (By similarity). Interacts with PTPN2; probably involved in TNF-mediated signaling (By similarity). Interacts with Toll-like receptor TLR4/3 adapter TICAM1/TRIF; the interaction may promotes TICAM1 ubiquitination (By similarity). Interacts with kinase/endoribonuclease ERN1/IRE1 and DAB2IP in response to ER stress; the interaction requires DAB2IP (PubMed:18281285). Interacts with ERN1/IRE1 and TAOK3 in response to ER stress; the interaction may promote TRAF2 phosphorylation (By similarity). Interacts (via zinc fingers) with DAB2IP (via C-terminus PER domain) in response to TNF-alpha stimulation (By similarity). Interacts with CASP8AP2/FLASH (PubMed:11340079). Interacts with NFATC2IP; the interaction may repress IL-4 production in T cells (PubMed:11435475). Interacts with kinase CDK9. Interacts with sphingosine kinase 1 SPHK1 (By similarity). Interacts with kinase TNIK (By similarity). Interacts with TRAFD1 (PubMed:18849341). Interacts with DNA phosphodiesterase TDP2 (By similarity). Interacts with MAVS/IPS1. Interacts with CARD14 (By similarity). Interacts with GPS2 (PubMed:22424771). Interacts with XPNPEP3 (By similarity). Interacts with RIPK3 (By similarity). Interacts with RELL2 (By similarity). {ECO:0000250|UniProtKB:Q12933, ECO:0000269|PubMed:11340079, ECO:0000269|PubMed:11435475, ECO:0000269|PubMed:11804591, ECO:0000269|PubMed:11909853, ECO:0000269|PubMed:16876162, ECO:0000269|PubMed:18281285, ECO:0000269|PubMed:18849341, ECO:0000269|PubMed:18997792, ECO:0000269|PubMed:18997794, ECO:0000269|PubMed:19150425, ECO:0000269|PubMed:19506082, ECO:0000269|PubMed:19815541, ECO:0000269|PubMed:20185725, ECO:0000269|PubMed:21307340, ECO:0000269|PubMed:22424771, ECO:0000269|PubMed:8069916, ECO:0000269|PubMed:8565075, ECO:0000269|PubMed:8692885, ECO:0000269|PubMed:9104814, ECO:0000269|PubMed:9500555}. DOMAIN: The coiled coil domain mediates homo- and hetero-oligomerization. {ECO:0000269|PubMed:19815541}.; DOMAIN: The MATH/TRAF domain binds to receptor cytoplasmic domains. {ECO:0000269|PubMed:19815541}.; DOMAIN: The RING-type zinc finger domain is essential for E3 ubiquitin-protein ligase activity. It is not essential for the stabilization of BIRC2, or for the ubiquitination of RIPK1 in response to TNFR1 signaling. {ECO:0000250|UniProtKB:Q12933}. TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in spleen, adipose tissues, skeletal muscles, thymus, testis, heart, lung, brain. Isoform 2 is very weakly expressed in heart, lung and brain. +Q60803 TRAF3_MOUSE TNF receptor-associated factor 3 (EC 2.3.2.27) (CD40 receptor-associated factor 1) (CRAF1) (RING-type E3 ubiquitin transferase TRAF3) (TRAFAMN) 567 64,294 Beta strand (9); Chain (1); Coiled coil (1); Cross-link (2); Domain (1); Helix (6); Mutagenesis (6); Sequence conflict (2); Turn (1); Zinc finger (3) FUNCTION: Regulates pathways leading to the activation of NF-kappa-B and MAP kinases, and plays a central role in the regulation of B-cell survival. Part of signaling pathways leading to the production of cytokines and interferon. Required for normal antibody isotype switching from IgM to IgG. Plays a role T-cell dependent immune responses. Plays a role in the regulation of antiviral responses. Is an essential constituent of several E3 ubiquitin-protein ligase complexes. May have E3 ubiquitin-protein ligase activity and promote 'Lys-63'-linked ubiquitination of target proteins. Inhibits activation of NF-kappa-B in response to LTBR stimulation. Inhibits TRAF2-mediated activation of NF-kappa-B. Down-regulates proteolytic processing of NFKB2, and thereby inhibits non-canonical activation of NF-kappa-B. Promotes ubiquitination and proteasomal degradation of MAP3K14. {ECO:0000269|PubMed:16306936, ECO:0000269|PubMed:16306937, ECO:0000269|PubMed:17015635, ECO:0000269|PubMed:17158868, ECO:0000269|PubMed:18313334, ECO:0000269|PubMed:18997792, ECO:0000269|PubMed:18997794, ECO:0000269|PubMed:19228877, ECO:0000269|PubMed:19898473, ECO:0000269|PubMed:8934568}. PTM: Undergoes 'Lys-48'-linked polyubiquitination, leading to its proteasomal degradation in response to signaling by TNFSF13B, TLR4 or through CD40. 'Lys-48'-linked polyubiquitinated form is deubiquitinated by OTUD7B, preventing TRAF3 proteolysis and over-activation of non-canonical NF-kappa-B. Undergoes 'Lys-63'-linked ubiquitination during early stages of virus infection, and 'Lys-48'-linked ubiquitination during later stages. Undergoes both 'Lys-48'-linked and 'Lys-63'-linked ubiquitination in response to TLR3 and TLR4 signaling. Deubiquitinated by OTUB1, OTUB2 and OTUD5. {ECO:0000269|PubMed:18997792, ECO:0000269|PubMed:19898473, ECO:0000269|PubMed:23334419}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19898473}. Endosome {ECO:0000269|PubMed:19898473}. Note=Undergoes endocytosis together with TLR4 upon LPS signaling. {ECO:0000269|PubMed:19898473}. SUBUNIT: Homotrimer. Heterotrimer with TRAF2 and TRAF5. Interacts with LTBR/TNFRSF3, TNFRSF4, TNFRSF5/CD40, TNFRSF8/CD30, TNFRSF13C TNFRSF17/BCMA, TLR4 and EDAR. Interacts with MAP3K5, MAP3K14, TRAIP/TRIP, TDP2/TTRAP, TANK/ITRAF and TRAF3IP1. Interaction with TNFRSF5/CD40 is modulated by TANK/ITRAF, which competes for the same binding site. Interacts with TICAM1. Interacts with TRAFD1. Interacts with OTUB1, OTUB2 and OTUD5. Interacts with RNF216, MAVS, OPTN and TBK1 (By similarity). Identified in a complex with TRAF2, MAP3K14 and BIRC3. Upon exposure to bacterial lipopolysaccharide (LPS), recruited to a transient complex containing TLR4, TRAF3, TRAF6, IKBKG, MAP3K7, MYD88, TICAM1, BIRC2, BIRC3 and UBE2N. Interacts (via RING-type zinc finger domain) with SRC. Interacts with CARD14 (By similarity). Interacts (via MATH domain) with PTPN22; the interaction promotes TRAF3 polyubiquitination (PubMed:23871208). {ECO:0000250, ECO:0000269|PubMed:23871208}. DOMAIN: The MATH/TRAF domain binds to receptor cytoplasmic domains. {ECO:0000269|PubMed:17158868}.; DOMAIN: The Ring-type zinc finger domain is required for its function in down-regulation of NFKB2 proteolytic processing. {ECO:0000269|PubMed:17158868}. TISSUE SPECIFICITY: Detected in bone marrow macrophages and spleen B-cells (at protein level). In adult, highest in brain. Also found in kidney, heart, thymus, spleen, lung, muscle, testis and ovary. Not found in liver. {ECO:0000269|PubMed:18997792, ECO:0000269|PubMed:19898473, ECO:0000269|PubMed:8660894}. +Q61382 TRAF4_MOUSE TNF receptor-associated factor 4 (Cysteine-rich motif associated to RING and Traf domains protein 1) 470 53,504 Chain (1); Coiled coil (1); Domain (1); Modified residue (1); Sequence conflict (9); Zinc finger (4) FUNCTION: Adapter protein and signal transducer that links members of the tumor necrosis factor receptor (TNFR) family to different signaling pathways. Plays a role in the activation of NF-kappa-B and JNK, and in the regulation of cell survival and apoptosis. Regulates activation of NF-kappa-B in response to signaling through Toll-like receptors. Required for activation of RPS6KB1 in response to TNF signaling. Modulates TRAF6 functions (By similarity). Required for normal skeleton development, and for normal development of the respiratory tract. {ECO:0000250}. PTM: Polyubiquitinated, leading to its proteasomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cell junction, tight junction {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. SUBUNIT: Homotrimer (Probable). Interacts with LTBR/TNFRSF3, NGFR/TNFRSF16, RPS6KB1 and TGFB1I1. Interacts with SMURF1. Interacts (via TRAF domain) with MAP3K4 (via kinase domain). Interacts with NCF1, TICAM1, IRAK1 and TRAF6, and is probably part of a complex containing TRAF4, NCF1, TICAM1, IRAK1 and TRAF6 (By similarity). {ECO:0000250, ECO:0000305}. DOMAIN: The coiled coil domain mediates homo- and hetero-oligomerization. {ECO:0000250}.; DOMAIN: The MATH/TRAF domain binds to receptor cytoplasmic domains. {ECO:0000250}. TISSUE SPECIFICITY: Predominantly expressed in brain. Preferentially expressed by post-mitotic undifferentiated neurons in developing central (CNS) and peripheral (PNS) nervous system, and in nervous tissues of sensory organs. In the embryo, protein expression was shown in brain, thymus, salivary glands and intestine. In the adult, protein expression is restricted to the brain (hippocampus and olfactory bulb). {ECO:0000269|PubMed:9507120}. +P70191 TRAF5_MOUSE TNF receptor-associated factor 5 558 64,145 Beta strand (10); Chain (1); Coiled coil (2); Domain (1); Helix (6); Region (1); Sequence conflict (1); Turn (1); Zinc finger (3) FUNCTION: Adapter protein and signal transducer that links members of the tumor necrosis factor receptor family to different signaling pathways by association with the receptor cytoplasmic domain and kinases. Mediates activation of NF-kappa-B and probably JNK. Seems to be involved in apoptosis. Plays a role in mediating activation of NF-kappa-B by EIF2AK2/PKR. {ECO:0000269|PubMed:15121867}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytosol. SUBUNIT: Homotrimer (Probable). Heterotrimer with TRAF3 (By similarity). Associates with TNFRSF5/CD40 through interaction with TRAF3 (By similarity). Associates with LTBR/TNFRSF3, TNFRSF4, TNFRSF8/CD30, TNFRSF11A/RANK, TNFRSF13B/TACI, TNFRSF14, TNFRSF17, TNFRSF19/TROY, RIPK2, MAP3K14, MAP3K5, and TRAF and TNF receptor associated protein TDP2 (By similarity). Interacts (via C-terminus) with EIF2AK2/PKR (via the kinase catalytic domain) (By similarity). {ECO:0000250, ECO:0000305}. DOMAIN: The MATH/TRAF domain binds to receptor cytoplasmic domains. +Q6P926 SPA24_MOUSE Spermatogenesis-associated protein 24 (TATA-binding protein-like factor-interacting protein) (TLF-interacting protein) (TRF2-interacting protein in testis) (Testis protein T6441 homolog) 205 23,769 Alternative sequence (2); Chain (1); Coiled coil (1); Mutagenesis (1); Region (1) FUNCTION: Binds DNA with high affinity but does not bind to TATA boxes. Synergises with GMNN and TBP in activation of TATA box-containing promoters and with GMNN and TBPL1 in activation of the NF1 TATA-less promoter. May play a role in cytoplasm movement and removal during spermiogenesis. {ECO:0000269|PubMed:18418073, ECO:0000269|PubMed:19515240}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus. Nucleus, nucleoplasm. Note=Associated with chromatin. SUBUNIT: Homodimer. Interacts with CBX3, CBX5, GMNN, GTF2B, TBPL1 and the polycomb proteins PHCF2, RNF2 and SCMH1 but not with CBX1 or PCGF2. {ECO:0000269|PubMed:18418073, ECO:0000269|PubMed:19515240}. TISSUE SPECIFICITY: Testis-specific (at protein level). {ECO:0000269|PubMed:18418073}. +Q8BNN1 SPA2L_MOUSE Spermatogenesis-associated protein 2-like protein (SPATA2-like protein) 426 46,772 Alternative sequence (2); Chain (1); Erroneous initiation (1); Modified residue (2); Sequence conflict (1) +Q8BMJ8 SP8_MOUSE Transcription factor Sp8 486 48,417 Chain (1); Compositional bias (3); Zinc finger (3) FUNCTION: Transcription factor which plays a key role in limb development. Positively regulates FGF8 expression in the apical ectodermal ridge (AER) and contributes to limb outgrowth in embryos. {ECO:0000269|PubMed:15358670}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q6P4P1 SPA3A_MOUSE Serine protease inhibitor A3A (Serpin A3A) 422 47,772 Alternative sequence (2); Chain (1); Glycosylation (3); Region (1); Sequence conflict (1); Signal peptide (1); Site (1) SUBCELLULAR LOCATION: Secreted {ECO:0000250}. DOMAIN: The reactive center loop (RCL) extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site within the RCL, establishing a covalent linkage between the serpin reactive site and the protease. The resulting inactive serpin-protease complex is highly stable (By similarity). Variability within the reactive center loop (RCL) sequences of Serpina3 paralogs may determine target protease specificity. {ECO:0000250}. +P29621 SPA3C_MOUSE Serine protease inhibitor A3C (Serpin A3C) (Kallikrein-binding protein) (KBP) 417 46,766 Chain (1); Glycosylation (5); Region (1); Signal peptide (1); Site (1) SUBCELLULAR LOCATION: Secreted {ECO:0000250}. DOMAIN: The reactive center loop (RCL) extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site within the RCL, establishing a covalent linkage between the serpin reactive site and the protease. The resulting inactive serpin-protease complex is highly stable (By similarity). Variability within the reactive center loop (RCL) sequences of Serpina3 paralogs may determine target protease specificity. {ECO:0000250}. +Q80X76 SPA3F_MOUSE Serine protease inhibitor A3F (Serpin A3F) 445 50,003 Chain (1); Erroneous initiation (1); Glycosylation (4); Region (1); Sequence conflict (5); Site (1) DOMAIN: The reactive center loop (RCL) extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site within the RCL, establishing a covalent linkage between the serpin reactive site and the protease. The resulting inactive serpin-protease complex is highly stable (By similarity). Variability within the reactive center loop (RCL) sequences of Serpina3 paralogs may determine target protease specificity. {ECO:0000250}. +P07759 SPA3K_MOUSE Serine protease inhibitor A3K (Serpin A3K) (Contrapsin) (SPI-2) 418 46,880 Chain (1); Glycosylation (4); Region (1); Sequence conflict (28); Signal peptide (1); Site (1) FUNCTION: Contrapsin inhibits trypsin-like proteases. {ECO:0000269|PubMed:6214866, ECO:0000269|PubMed:6224776}. SUBCELLULAR LOCATION: Secreted. DOMAIN: The reactive center loop (RCL) extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site within the RCL, establishing a covalent linkage between the serpin reactive site and the protease. The resulting inactive serpin-protease complex is highly stable (By similarity). Variability within the reactive center loop (RCL) sequences of Serpina3 paralogs may determine target protease specificity. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in liver and secreted in plasma. {ECO:0000269|PubMed:15638460, ECO:0000269|PubMed:2049065, ECO:0000269|PubMed:6214866, ECO:0000269|PubMed:6224776}. +P70196 TRAF6_MOUSE TNF receptor-associated factor 6 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF6) (RING-type E3 ubiquitin transferase TRAF6) 530 60,070 Alternative sequence (2); Chain (1); Coiled coil (1); Cross-link (4); Domain (1); Region (2); Sequence conflict (4); Zinc finger (3) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin ligase that, together with UBE2N and UBE2V1, mediates the synthesis of 'Lys-63'-linked-polyubiquitin chains conjugated to proteins, such as IKBKG, IRAK1, AKT1 and AKT2. Also mediates ubiquitination of free/unanchored polyubiquitin chain that leads to MAP3K7 activation (By similarity). Leads to the activation of NF-kappa-B and JUN. May be essential for the formation of functional osteoclasts. Seems to also play a role in dendritic cells (DCs) maturation and/or activation. Represses c-Myb-mediated transactivation, in B-lymphocytes. Adapter protein that seems to play a role in signal transduction initiated via TNF receptor, IL-1 receptor and IL-17 receptor. Regulates osteoclast differentiation by mediating the activation of adapter protein complex 1 (AP-1) and NF-kappa-B, in response to RANK-L stimulation. Together with MAP3K8, mediates CD40 signals that activate ERK in B-cells and macrophages, and thus may play a role in the regulation of immunoglobulin production. {ECO:0000250|UniProtKB:Q9Y4K3, ECO:0000269|PubMed:10215628, ECO:0000269|PubMed:10421844, ECO:0000269|PubMed:12881420, ECO:0000269|PubMed:14499111, ECO:0000269|PubMed:15322147, ECO:0000269|PubMed:17092936, ECO:0000269|PubMed:17633018}. PTM: Sumoylated on Lys-124, Lys-142 and Lys-461 with SUMO1. {ECO:0000250|UniProtKB:Q9Y4K3}.; PTM: Polyubiquitinated; after cell stimulation with IL-1-beta or TGF-beta. This ligand-induced cell stimulation leads to dimerization/oligomerization of TRAF6 molecules, followed by auto-ubiquitination which involves UBE2N and UBE2V1 and leads to TRAF6 activation. This 'Lys-63' site-specific poly-ubiquitination appears to be associated with the activation of signaling molecules. Endogenous autoubiquitination occurs only for the cytoplasmic form. Deubiquitinated by USP10 in a TANK-dependent manner, leading to the negative regulation of NF-kappaB signaling upon DNA damage. {ECO:0000250|UniProtKB:Q9Y4K3}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y4K3}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q9Y4K3}. Nucleus {ECO:0000250|UniProtKB:Q9Y4K3}. Lipid droplet {ECO:0000269|PubMed:21435586}. Note=RSAD2/viperin recruits it to the lipid droplet. SUBUNIT: Homotrimer (By similarity). Homooligomer (By similarity). N-terminal region is dimeric while C-terminal region is trimeric; maybe providing a mode of oligomerization. Upon IL1B treatment, forms a complex with PELI1, IRAK1, IRAK4 and MYD88; this complex recruits MAP3K7/TAK1, TAB1 and TAB2 to mediate NF-kappa-B activation. Direct binding of SMAD6 to PELI1 prevents the complex formation and hence negatively regulates IL1R-TLR signaling and eventually NF-kappa-B-mediated gene expression. Binds to TNFRSF5/CD40 and TNFRSF11A/RANK (By similarity). Associates with NGFR, TNFRSF17, IRAK2, IRAK3, PELI2, PELI3, RIPK2, MAP3K1, MAP3K5, MAP3K14, CSK, TRAF, TRAF-interacting protein TRIP and TNF receptor associated protein TDP2. Binds UBE2V1. Interacts with MAVS/IPS1. Interacts with TAX1BP1 (By similarity). Interacts with IL17R. Interacts with SQSTM1 bridging NTRK1 and NGFR. Forms a ternary complex with SQSTM1 and PRKCZ. Interacts with IL1RL1. Interacts with AJUBA (By similarity). Interacts with TRAFD1. Interacts with TICAM2. Interacts with ZFAND5. Interacts with ARRB1 and ARRB2 (By similarity). Interacts with MAP3K7 and TAB1/MAP3K7IP1; during IL-1 signaling. Interacts with UBE2N. Interacts with TGFBR1, HDAC1 and RANGAP1. Interacts with AKT1, AKT2 and AKT3. Interacts (via TRAF domains) with NUMBL (via C-terminal) (By similarity). Interacts (via TRAF domains) with WDR34 (via WD domains). Interacts with RBCK1 (By similarity). Interacts with TRAF3IP2 (By similarity). Interacts with LIMD1 (via LIM domains). Interacts with RSAD2/viperin. Interacts with IFIT3 (via N-terminus) (By similarity). Interacts (via C-terminus) with EIF2AK2/PKR (via the kinase catalytic domain). Interacts with CARD14 (By similarity). Interacts with CD40 and MAP3K8; the interaction is required for ERK activation. Interacts with TICAM1 and this interaction is enhanced in the presence of WDFY1 (By similarity). Interacts with TANK; this interaction increases in response to DNA damage (By similarity). Interacts with USP10; this interaction increases in response to DNA damage (By similarity). Interacts with ZC3H12A; this interaction increases in response to DNA damage and is stimulated by TANK (By similarity). Interacts with WDFY3 (PubMed:27330028). Interacts with TRIM13 (By similarity). Interacts with GPS2 (PubMed:22424771). {ECO:0000250|UniProtKB:Q9Y4K3, ECO:0000269|PubMed:10747026, ECO:0000269|PubMed:10748240, ECO:0000269|PubMed:11244088, ECO:0000269|PubMed:12881420, ECO:0000269|PubMed:16951688, ECO:0000269|PubMed:17092936, ECO:0000269|PubMed:18849341, ECO:0000269|PubMed:21435586, ECO:0000269|PubMed:22424771, ECO:0000269|PubMed:27330028}. DOMAIN: The coiled coil domain mediates homo- and hetero-oligomerization.; DOMAIN: The MATH/TRAF domain binds to receptor cytoplasmic domains. TISSUE SPECIFICITY: Highly expressed in brain, lung, liver, skeletal muscle, and kidney; lower expression in heart, spleen, and testis. +Q9WTS6 TEN3_MOUSE Teneurin-3 (Ten-3) (Protein Odd Oz/ten-m homolog 3) (Tenascin-M3) (Ten-m3) (Teneurin transmembrane protein 3) 2715 303,066 Alternative sequence (5); Chain (1); Disulfide bond (22); Domain (9); Erroneous initiation (1); Glycosylation (17); Repeat (29); Sequence conflict (7); Topological domain (2); Transmembrane (1) TRANSMEM 311 331 Helical. {ECO:0000255}. TOPO_DOM 1 310 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 332 2715 Extracellular. {ECO:0000255}. FUNCTION: Involved in neural development by regulating the establishment of proper connectivity within the nervous system (PubMed:17478416, PubMed:17803360, PubMed:23028443, PubMed:25406022, PubMed:22499796, PubMed:29414938). Acts in both pre- and postsynaptic neurons in the hippocampus to control the assembly of a precise topographic projection: required in both CA1 and subicular neurons for the precise targeting of proximal CA1 axons to distal subiculum, probably by promoting homophilic cell adhesion (PubMed:29414938). Promotes homophilic adhesion in a splicing isoform-dependent manner: most isoforms (isoform-type A and type-B) can mediate homophilic interaction (PubMed:29414938). Promotes axon guidance (PubMed:23028443). Required for proper dendrite morphogenesis and axon targeting in the vertebrate visual system, thereby playing a key role in the development of the visual pathway (PubMed:17803360, PubMed:23028443, PubMed:25406022, PubMed:22499796). Regulates the formation in ipsilateral retinal mapping to both the dorsal lateral geniculate nucleus (dLGN) and the superior colliculus (SC) (PubMed:17803360, PubMed:23028443). May also be involved in the differentiation of the fibroblast-like cells in the superficial layer of mandibular condylar cartilage into chondrocytes (PubMed:20636325). {ECO:0000269|PubMed:17478416, ECO:0000269|PubMed:17803360, ECO:0000269|PubMed:20636325, ECO:0000269|PubMed:22499796, ECO:0000269|PubMed:23028443, ECO:0000269|PubMed:25406022, ECO:0000269|PubMed:29414938}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:29414938, ECO:0000305|PubMed:17478416}; Single-pass membrane protein {ECO:0000269|PubMed:17478416}. Cell projection, axon {ECO:0000269|PubMed:17478416}. SUBUNIT: Homodimer; disulfide-linked; to mediate homophilic cell adhesion (PubMed:29414938, PubMed:12000766). Most isoforms (isoform-type A and type-B) can mediate homophilic interaction (PubMed:29414938). Heterodimer with either TENM1 or TENM2 (PubMed:12000766). May also form heterodimer with TENM4 (PubMed:12000766). Isoform A0B0: Does not form homodimer to mediate homophilic cell adhesion. Isoform A0B0: Heterodimer with ADGRL3 (PubMed:29414938). {ECO:0000269|PubMed:12000766, ECO:0000269|PubMed:29414938}. DOMAIN: EGF-like domains 2 and 5 which have an odd number of cysteines might enable the formation of intermolecular disulfide bonds. {ECO:0000305|PubMed:10225957}.; DOMAIN: Cytoplasmic proline-rich regions could serve as docking domains for intracellular SH3-containing proteins. {ECO:0000305|PubMed:10225957}. TISSUE SPECIFICITY: In brain, expressed in highly specific regions of the postnatal brain: expressed in restricted domains of the developing hippocampal region, including proximal CA1, distal subiculum, and medial entorhinal cortex (at protein level) (PubMed:29414938). Expression matches with topographic connectivity between entorhinal cortex, CA1, and subiculum (at protein level) (PubMed:29414938). Also specifically expressed in subregions of the presubiculum, parasubiculum, medial mammillary nucleus and anteroventral thalamic nucleus that are topographically connected with subiculum or entorhinal cortex (at protein level) (PubMed:29414938). Expressed in neurons of the developing visual pathway (at protein level). Expressed in the dorsal and ventral lateral geniculate nucleus (dLGN and vLGN) and optic tract at birth. Expressed in ipsilateral retinal axons of terminal zones (TZs) in the developing superior colliculus (SC) throughout the first postnatal week. Expressed in the layer V of the visual caudal cortex. Expressed in the femoral and mandibular condylar cartilages. Strongly expressed in fibrous and proliferating chondrocytes. Poorly expressed in mature chondrocytes. Not expressed in hypertrophic chondrocytes (PubMed:12915301, PubMed:17478416, PubMed:17803360, PubMed:20636325, PubMed:23028443). {ECO:0000269|PubMed:12915301, ECO:0000269|PubMed:17478416, ECO:0000269|PubMed:17803360, ECO:0000269|PubMed:20636325, ECO:0000269|PubMed:23028443, ECO:0000269|PubMed:29414938}. +Q921W8 SCT1A_MOUSE Secreted and transmembrane protein 1A 192 21,438 Chain (1); Glycosylation (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 166 186 Helical. {ECO:0000255}. TOPO_DOM 28 165 Extracellular. {ECO:0000255}.; TOPO_DOM 187 192 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Secreted {ECO:0000250}. +Q9JL59 SCT1B_MOUSE Secreted and transmembrane protein 1b (Protein K-12) 212 23,477 Chain (1); Disulfide bond (1); Glycosylation (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 161 181 Helical. {ECO:0000255}. TOPO_DOM 29 160 Extracellular. {ECO:0000255}.; TOPO_DOM 182 212 Cytoplasmic. {ECO:0000255}. FUNCTION: May be involved in thymocyte signaling. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:10652336}; Single-pass type I membrane protein {ECO:0000305|PubMed:10652336}. Secreted {ECO:0000250}. SUBUNIT: Interacts with CD7. {ECO:0000269|PubMed:10652336}. +Q64151 SEM4C_MOUSE Semaphorin-4C (M-Sema F) (Semaphorin-C-like 1) (Sema I) (Semaphorin I) 834 92,557 Chain (1); Compositional bias (2); Disulfide bond (7); Domain (3); Glycosylation (6); Modified residue (1); Motif (1); Mutagenesis (3); Region (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 665 685 Helical. {ECO:0000255}. TOPO_DOM 21 664 Extracellular. {ECO:0000255}.; TOPO_DOM 686 834 Cytoplasmic. {ECO:0000255}. FUNCTION: Cell surface receptor for PLXNB2 that plays an important role in cell-cell signaling. PLXNB2 binding promotes downstream activation of RHOA and phosphorylation of ERBB2 at 'Tyr-1248'. Required for normal brain development, axon guidance and cell migration. Probable signaling receptor which may play a role in myogenic differentiation through activation of the stress-activated MAPK cascade. {ECO:0000269|PubMed:15811348, ECO:0000269|PubMed:17498836, ECO:0000269|PubMed:17554007, ECO:0000269|PubMed:21122816}. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000269|PubMed:11134026}; Single-pass type I membrane protein {ECO:0000269|PubMed:11134026}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:11134026}; Single-pass type I membrane protein {ECO:0000269|PubMed:11134026}. SUBUNIT: Interacts (via the PDZ-binding motif) with GIPC (via the PDZ domain). Interacts with NCDN. Interacts (via the PDZ-binding motif) with DLG4. Interacts with PLXNB2. {ECO:0000269|PubMed:10318831, ECO:0000269|PubMed:11134026, ECO:0000269|PubMed:11162505, ECO:0000269|PubMed:17554007, ECO:0000269|PubMed:21122816}. TISSUE SPECIFICITY: Predominantly expressed in brain (at protein level). {ECO:0000269|PubMed:11134026}. +Q8BMZ5 SEN34_MOUSE tRNA-splicing endonuclease subunit Sen34 (EC 4.6.1.16) (Leukocyte receptor cluster member 5 homolog) (tRNA-intron endonuclease Sen34) 316 34,196 Active site (3); Alternative sequence (1); Chain (1); Sequence conflict (2) FUNCTION: Constitutes one of the two catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3'-cyclic phosphate and 5'-OH termini. There are no conserved sequences at the splice sites, but the intron is invariably located at the same site in the gene, placing the splice sites an invariant distance from the constant structural features of the tRNA body. The tRNA splicing endonuclease is also involved in mRNA processing via its association with pre-mRNA 3'-end processing factors, establishing a link between pre-tRNA splicing and pre-mRNA 3'-end formation, suggesting that the endonuclease subunits function in multiple RNA-processing events (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Note=May be transiently localized in the nucleolus. {ECO:0000250}. SUBUNIT: tRNA splicing endonuclease is a heterotetramer composed of TSEN2, TSEN15, TSEN34/LENG5 and TSEN54. tRNA splicing endonuclease complex also contains proteins of the pre-mRNA 3'-end processing machinery such as CLP1, CPSF1, CPSF4 and CSTF2 (By similarity). {ECO:0000250}. +Q6P7W0 SENP6_MOUSE Sentrin-specific protease 6 (EC 3.4.22.-) (SUMO-1-specific protease 1) (Sentrin/SUMO-specific protease SENP6) 1132 127,013 Active site (3); Alternative sequence (1); Chain (1); Cross-link (1); Erroneous initiation (1); Frameshift (1); Modified residue (8); Region (1); Sequence caution (1); Sequence conflict (6) Protein modification; protein sumoylation. FUNCTION: Protease that deconjugates SUMO1, SUMO2 and SUMO3 from targeted proteins. Processes preferentially poly-SUMO2 and poly-SUMO3 chains, but does not efficiently process SUMO1, SUMO2 and SUMO3 precursors. Deconjugates SUMO1 from RXRA, leading to transcriptional activation. Involved in chromosome alignment and spindle assembly, by regulating the kinetochore CENPH-CENPI-CENPK complex. Desumoylates PML and CENPI, protecting them from degradation by the ubiquitin ligase RNF4, which targets polysumoylated proteins for proteasomal degradation. Desumoylates also RPA1, thus preventing recruitment of RAD51 to the DNA damage foci to initiate DNA repair through homologous recombination. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with RXRA. Forms a complex with KAT5-TIP60 and UBE2I in response to UV irradiation. Interacts with RPA1 to maintain it in hyposumoylated state during S phase preventing DNA repair initiation (By similarity). {ECO:0000250}. +Q8BUH8 SENP7_MOUSE Sentrin-specific protease 7 (EC 3.4.22.-) (SUMO-1-specific protease 2) (Sentrin/SUMO-specific protease SENP7) 1037 116,346 Active site (2); Chain (1); Erroneous initiation (1); Modified residue (5); Region (1) FUNCTION: Protease that deconjugates SUMO2 and SUMO3 from targeted proteins, but not SUMO1. Catalyzes the deconjugation of poly-SUMO2 and poly-SUMO3 chains. Has very low efficiency in processing full-length SUMO proteins to their mature forms. {ECO:0000250|UniProtKB:Q9BQF6}. +Q99K85 SERC_MOUSE Phosphoserine aminotransferase (PSAT) (EC 2.6.1.52) (Endometrial progesterone-induced protein) (EPIP) (Phosphohydroxythreonine aminotransferase) 370 40,473 Binding site (5); Chain (1); Modified residue (9); Region (2) Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 2/3. Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 3/5. FUNCTION: Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine. {ECO:0000250|UniProtKB:P10658}. SUBUNIT: Homodimer. {ECO:0000250}. +Q69ZU6 THS7A_MOUSE Thrombospondin type-1 domain-containing protein 7A [Cleaved into: Thrombospondin type-1 domain-containing protein 7A, soluble form] 1645 183,527 Chain (2); Coiled coil (1); Compositional bias (1); Disulfide bond (31); Domain (19); Glycosylation (13); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1596 1616 Helical. {ECO:0000255}. TOPO_DOM 39 1595 Extracellular. {ECO:0000255}.; TOPO_DOM 1617 1645 Cytoplasmic. {ECO:0000255}. FUNCTION: Thrombospondin type-1 domain-containing protein 7A: Plays a role in actin cytoskeleton rearrangement. {ECO:0000269|PubMed:27214550}.; FUNCTION: Thrombospondin type-1 domain-containing protein 7A, soluble form: The soluble form promotes endothelial cell migration and filopodia formation during sprouting angiogenesis via a FAK-dependent mechanism. {ECO:0000250|UniProtKB:Q9UPZ6}. PTM: Proteolytic cleavage in the extracellular region generates a 210 kDa soluble form. {ECO:0000250|UniProtKB:Q9UPZ6}.; PTM: Extensively N-glycosylated. {ECO:0000250|UniProtKB:Q9UPZ6}. SUBCELLULAR LOCATION: Thrombospondin type-1 domain-containing protein 7A: Cell membrane {ECO:0000269|PubMed:27214550}; Single-pass type I membrane protein {ECO:0000305|PubMed:27214550}. Cell projection {ECO:0000269|PubMed:27214550}. Note=Detected on podocyte foot processes. {ECO:0000269|PubMed:27214550}.; SUBCELLULAR LOCATION: Thrombospondin type-1 domain-containing protein 7A, soluble form: Secreted {ECO:0000250|UniProtKB:Q9UPZ6}. Note=Proteolytic cleavage in the extracellular region generates a 210 kDa soluble form. {ECO:0000250|UniProtKB:Q9UPZ6}. DOMAIN: Sequence analysis combined with the expression of constructs corresponding each to two or three adjacent TSP type-1 domains suggests the presence of 21 TSP type-1 domains; not all of these are detected by standard bioinformatic tools. {ECO:0000250|UniProtKB:Q9UPZ6}. TISSUE SPECIFICITY: Detected on kidney podocytes along the glomerular capillary wall (at protein level). {ECO:0000269|PubMed:27214550}. +Q9JM61 THSD1_MOUSE Thrombospondin type-1 domain-containing protein 1 (Transmembrane molecule with thrombospondin module) 851 94,696 Chain (1); Disulfide bond (3); Domain (1); Frameshift (1); Glycosylation (6); Modified residue (1); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 413 433 Helical. {ECO:0000255}. TOPO_DOM 25 412 Extracellular. {ECO:0000255}.; TOPO_DOM 434 851 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +O88892 SERF1_MOUSE Small EDRK-rich factor 1 (Protein 4F5) (m4F5) 62 7,322 Chain (1) +P84102 SERF2_MOUSE Small EDRK-rich factor 2 (Protein 4F5-related) (4F5rel) 59 6,900 Chain (1) +O88974 SETB1_MOUSE Histone-lysine N-methyltransferase SETDB1 (EC 2.1.1.43) (ERG-associated protein with SET domain) (ESET) (SET domain bifurcated 1) 1307 144,549 Alternative sequence (6); Binding site (3); Chain (1); Coiled coil (1); Cross-link (7); Domain (6); Metal binding (16); Modified residue (9); Mutagenesis (2); Region (2); Sequence conflict (2) FUNCTION: Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. H3 'Lys-9' trimethylation is coordinated with DNA methylation. Probably forms a complex with MBD1 and ATF7IP that represses transcription and couples DNA methylation and histone 'Lys-9' trimethylation. Its activity is dependent on MBD1 and is heritably maintained through DNA replication by being recruited by CAF-1. SETDB1 is targeted to histone H3 by TRIM28/TIF1B, a factor recruited by KRAB zinc-finger proteins. Probably forms a corepressor complex required for activated KRAS-mediated promoter hypermethylation and transcriptional silencing of tumor suppressor genes (TSGs) or other tumor-related genes in colorectal cancer (CRC) cells (By similarity). Also required to maintain a transcriptionally repressive state of genes in undifferentiated embryonic stem cells (ESCs) (By similarity). Associates at promoter regions of tumor suppressor genes (TSGs) leading to their gene silencing. The SETDB1-TRIM28-ZNF274 complex may play a role in recruiting ATRX to the 3'-exons of zinc-finger coding genes with atypical chromatin signatures to establish or maintain/protect H3K9me3 at these transcriptionally active regions (By similarity). {ECO:0000250|UniProtKB:Q15047}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}. Note=Associated with non-pericentromeric regions of chromatin. {ECO:0000250}. SUBUNIT: Part of a complex containing at least CDYL, REST, WIZ, SETB1, EHMT1 and EHMT2. During DNA replication, it is recruited by SETDB1 to form a S phase-specific complex that facilitates methylation of H3 'Lys-9' during replication-coupled chromatin assembly and is at least composed of the CAF-1 subunit CHAF1A, MBD1 and SETDB1. Probably part of a corepressor complex containing ZNF304, TRIM28, SETDB1 and DNMT1. Interacts with TRIM28/TIF1B. Interacts with ATF7IP and ATF7IP2; the interaction with ATF7IP is required to stimulate histone methyltransferase activity and facilitate the conversion of dimethylated to trimethylated H3 'Lys-9'. Interacts with MBD1; interaction is abolished when MBD1 is sumoylated. Interacts with CBX1 and CBX5. Interacts with DNMT3A and DNMT3B. Interacts with SUMO2. Interacts with CHD7, NLK1 and PPARG. Interacts with MPHOSPH8 (By similarity). Interacts with ERG (PubMed:11791185). Interacts with HDAC1, HDAC2, SIN3A, SIN3B (PubMed:12398767). Interacts with ATRX. Forms a complex with ATRX, TRIM28 and ZNF274 (By similarity). {ECO:0000250|UniProtKB:Q15047, ECO:0000269|PubMed:11791185, ECO:0000269|PubMed:12398767}. DOMAIN: The pre-SET, SET and post-SET domains are all required for methyltransferase activity. The 347-amino-acid insertion in the SET domain has no effect on the catalytic activity.; DOMAIN: In the pre-SET domain, Cys residues bind 3 zinc ions that are arranged in a triangular cluster; some of these Cys residues contribute to the binding of two zinc ions within the cluster. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed. Strong expression in liver and testis. {ECO:0000269|PubMed:14522075}. +Q62203 SF3A2_MOUSE Splicing factor 3A subunit 2 (SF3a66) (Spliceosome-associated protein 62) (SAP 62) 475 49,911 Chain (1); Compositional bias (1); Modified residue (3); Zinc finger (1) FUNCTION: Subunit of the splicing factor SF3A required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA. May also be involved in the assembly of the 'E' complex. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00130}. SUBUNIT: Identified in the spliceosome C complex (By similarity). Component of splicing factor SF3A which is composed of three subunits; SF3A3/SAP61, SF3A2/SAP62, SF3A1/SAP114. SF3A associates with the splicing factor SF3B and a 12S RNA unit to form the U2 small nuclear ribonucleoproteins complex (U2 snRNP). Interacts with HTATSF1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Found in all tissues examined. +Q9EQU5 SET_MOUSE Protein SET (Phosphatase 2A inhibitor I2PP2A) (I-2PP2A) (Template-activating factor I) (TAF-I) 289 33,378 Alternative sequence (3); Chain (1); Compositional bias (1); Cross-link (1); Initiator methionine (1); Modified residue (12); Mutagenesis (1); Region (2); Sequence conflict (3) FUNCTION: Multitasking protein, involved in apoptosis, transcription, nucleosome assembly and histone chaperoning. Isoform 2 anti-apoptotic activity is mediated by inhibition of the GZMA-activated DNase, NME1. In the course of cytotoxic T-lymphocyte (CTL)-induced apoptosis, GZMA cleaves SET, disrupting its binding to NME1 and releasing NME1 inhibition. Isoform 1 and isoform 2 are potent inhibitors of protein phosphatase 2A. Isoform 1 and isoform 2 inhibit EP300/CREBBP and PCAF-mediated acetylation of histones (HAT) and nucleosomes, most probably by masking the accessibility of lysines of histones to the acetylases. The predominant target for inhibition is histone H4. HAT inhibition leads to silencing of HAT-dependent transcription and prevents active demethylation of DNA. Both isoforms stimulate DNA replication of the adenovirus genome complexed with viral core proteins; however, isoform 2 specific activity is higher (By similarity). {ECO:0000250}. PTM: Some glutamate residues are glycylated by TTLL8. This modification occurs exclusively on glutamate residues and results in a glycine chain on the gamma-carboxyl group.; PTM: N-terminus of isoform 1 is methylated by METTL11A/NTM1. Mainly trimethylated. {ECO:0000269|PubMed:20668449}.; PTM: Isoform 2: Cleaved after Lys-176 by GZMA. The cleavage inhibits its nucleosome assembly activity and disrupts the inhibition on NME1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Note=In the cytoplasm, found both in the cytosol and associated with the endoplasmic reticulum. The SET complex is associated with the endoplasmic reticulum. Following CTL attack and cleavage by GZMA, moves rapidly to the nucleus, where it is found in the nucleoplasm, avoiding the nucleolus. Similar translocation to the nucleus is also observed for lymphocyte-activated killer cells after the addition of calcium (By similarity). {ECO:0000250}. SUBUNIT: Headphone-shaped homodimer. Isoform 1 and isoform 2 interact directly with each other and with ANP32A within the tripartite INHAT (inhibitor of acetyltransferases) complex. Isoform 1 and isoform 2 interact also with histones. Isoform 2 is a omponent of the SET complex, composed of at least ANP32A, APEX1, HMGB2, NME1, SET and TREX1, but not NME2 or TREX2. Within this complex, directly interacts with ANP32A, NME1, HMGB2 and TREX1; the interaction with ANP32A is enhanced after cleavage. Interacts with APBB1, CHTOP, SETBP1, SGO1. {ECO:0000269|PubMed:22872859}. DOMAIN: A long alpha helix in the N-terminus mediates dimerization, while the earmuff domain is responsible for core histone and dsDNA binding. The C-terminal acidic domain mediates the inhibition of histone acetyltransferases and is required for the DNA replication stimulatory activity (By similarity). {ECO:0000250}. +E9PXB6 SFTA2_MOUSE Surfactant-associated protein 2 (Surfactant-associated protein G) 77 8,502 Chain (1); Glycosylation (1); Signal peptide (1) FUNCTION: Putative surfactant protein. {ECO:0000305}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q6UW10}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniProtKB:Q6UW10}. Golgi apparatus {ECO:0000250|UniProtKB:Q6UW10}. TISSUE SPECIFICITY: Expressed in lung, and specifically in alveolar type II epithelial cells. {ECO:0000269|PubMed:22768197}. +Q923D4 SF3B5_MOUSE Splicing factor 3B subunit 5 (SF3b5) (Pre-mRNA-splicing factor SF3b 10 kDa subunit) 86 10,119 Chain (1); Initiator methionine (1); Modified residue (3); Region (1); Site (2) FUNCTION: Involved in pre-mRNA splicing as a component of the splicing factor SF3B complex, a constituent of the spliceosome. SF3B complex is required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA. {ECO:0000250|UniProtKB:Q9BWJ5}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BWJ5}. SUBUNIT: Component of the spliceosome B complex. Component of splicing factor SF3B complex which is composed of at least eight subunits; SF3B1, SF3B2, SF3B3, SF3B4, SF3B5, SF3B6, PHF5A and DDX42. SF3B associates with the splicing factor SF3A and a 12S RNA unit to form the U2 small nuclear ribonucleoproteins complex (U2 snRNP). Within the SF3B complex interacts directly with SF3B1 (via HEAT domain) and SF3B3. The SF3B complex composed of SF3B1, SF3B2, SF3B3, SF3B4, SF3B5, SF3B6 and PHF5A interacts with U2AF2. Component of the U11/U12 snRNPs that are part of the U12-type spliceosome. {ECO:0000250|UniProtKB:Q9BWJ5}. +Q91X43 SH319_MOUSE SH3 domain-containing protein 19 (Kryn) 789 86,077 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (5); Erroneous initiation (1); Modified residue (2); Sequence caution (2); Sequence conflict (1) FUNCTION: May play a role in regulating A disintegrin and metalloproteases (ADAMs) in the signaling of EGFR-ligand shedding. May be involved in suppression of Ras-induced cellular transformation and Ras-mediated activation of ELK1. Plays a role in the regulation of cell morphology and cytoskeletal organization (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with ADAM12. Isoform 2 (but not isoform 1) interacts with ADAM9, ADAM10, ADAM15 and ADAM17. Interacts with SH3GL1 SH3 domain. Interacts via SH3 3 and SH3 4 or SH3 4 and SH3 5 domains with SOS2. Probably forms a trimeric complex with SH3GL1 and SOS2 (By similarity). Interacts with SH3YL1. {ECO:0000250, ECO:0000269|PubMed:12615363}. TISSUE SPECIFICITY: Expressed in hair follicles. {ECO:0000269|PubMed:12615363}. +Q61120 SHC3_MOUSE SHC-transforming protein 3 (Neuronal Shc) (N-Shc) (SHC-transforming protein C) (Src homology 2 domain-containing-transforming protein C3) (SH2 domain protein C3) 474 52,121 Chain (1); Domain (2); Modified residue (1); Region (1); Sequence conflict (1) FUNCTION: Signaling adapter that couples activated growth factor receptors to signaling pathway in neurons. Involved in the signal transduction pathways of neurotrophin-activated Trk receptors in cortical neurons (By similarity). {ECO:0000250}. PTM: Tyrosine phosphorylated. {ECO:0000250}. SUBUNIT: Interacts with the Trk receptors in a phosphotyrosine-dependent manner. Once activated, binds to GRB2. Interacts with activated EGF receptors (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Predominantly expressed in the adult brain. +Q9Z0V8 TI17A_MOUSE Mitochondrial import inner membrane translocase subunit Tim17-A (Inner membrane preprotein translocase Tim17a) 171 18,112 Chain (1); Disulfide bond (1); Transmembrane (3) TRANSMEM 17 37 Helical. {ECO:0000255}.; TRANSMEM 63 77 Helical. {ECO:0000255}.; TRANSMEM 113 133 Helical. {ECO:0000255}. FUNCTION: Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SUBUNIT: Component of the TIM23 complex at least composed of TIMM23, TIMM17 (TIMM17A or TIMM17B) and TIMM50. The complex interacts with the TIMM44 component of the PAM complex. The complex also interacts with DNAJC15 (By similarity). {ECO:0000250}. +Q8C8M1 SHCAF_MOUSE SIN3-HDAC complex-associated factor (Protein FAM60A) (Tera protein) 221 24,829 Chain (1); Erroneous initiation (1); Sequence conflict (1) FUNCTION: Subunit of the Sin3 deacetylase complex (Sin3/HDAC), this subunit is important for the repression of genes encoding components of the TGF-beta signaling pathway (By similarity). Core component of a SIN3A complex (composed of at least SINHCAF, SIN3A, HDAC1, SAP30, RBBP4, OGT and TET1) present in embryonic stem (ES) cells. Promotes the stability of SIN3A and its presence on chromatin and is essential for maintaining the potential of ES cells to proliferate rapidly, while ensuring a short G1-phase of the cell cycle, thereby preventing premature lineage priming (PubMed:28554894). {ECO:0000250|UniProtKB:Q9NP50, ECO:0000269|PubMed:28554894}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28554894}. SUBUNIT: Component of the Sin3/HDAC corepressor complex at least composed of BRMS1, BRMS1L, ING2, SAP30, SAP30L, HDAC1 (By similarity). Found in a complex composed of at least SINHCAF, SIN3A, HDAC1, SAP30, RBBP4, OGT and TET1. Interacts with SIN3A and OGT (PubMed:28554894). {ECO:0000250|UniProtKB:Q9NP50, ECO:0000269|PubMed:28554894}. TISSUE SPECIFICITY: Embryonic stem cells (at protein level). {ECO:0000269|PubMed:28554894}. +Q62419 SH3G1_MOUSE Endophilin-A2 (Endophilin-2) (SH3 domain protein 2B) (SH3 domain-containing GRB2-like protein 1) (SH3p8) 368 41,518 Chain (1); Coiled coil (1); Domain (2); Modified residue (3); Region (3) FUNCTION: Implicated in endocytosis. May recruit other proteins to membranes with high curvature (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Early endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell projection, podosome {ECO:0000250}. Note=Associated with postsynaptic endosomes in hippocampal neurons. {ECO:0000250}. SUBUNIT: Interacts with ARC, SYNJ1 and DNM1. Interacts with PDCD6IP. Interacts with BIN2 (By similarity). {ECO:0000250}. DOMAIN: An N-terminal amphipathic helix, the BAR domain and a second amphipathic helix inserted into helix 1 of the BAR domain (N-BAR domain) induce membrane curvature and bind curved membranes. {ECO:0000250}. +Q9Z179 SHCBP_MOUSE SHC SH2 domain-binding protein 1 (Protein expressed in activated lymphocytes) (mPAL) (SHC-binding protein) 668 75,917 Chain (1); Compositional bias (1); Initiator methionine (1); Modified residue (5); Repeat (5); Sequence conflict (1) FUNCTION: May play a role in signaling pathways governing cellular proliferation, cell growth and differentiation. May be a component of a novel signaling pathway downstream of Shc. Acts as a positive regulator of FGF signaling in neural progenitor cells. {ECO:0000269|PubMed:10086341, ECO:0000269|PubMed:22508726}. SUBCELLULAR LOCATION: Midbody {ECO:0000250|UniProtKB:Q8NEM2}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q8NEM2}. Note=Displays weak localization to the spindle midzone in some early telophase cells and is concentrated at the midbody in late cytokinesis. {ECO:0000250|UniProtKB:Q8NEM2}. SUBUNIT: Interacts directly with isoform p52shc of SHC1 via its SH2 domain (PubMed:10086341). Interacts with TRIM71; leading to enhanced SHCBP1 protein stability (PubMed:22508726). Interacts with both members of the centralspindlin complex, KIF23 and RACGAP1 (By similarity). {ECO:0000250|UniProtKB:Q8NEM2, ECO:0000269|PubMed:10086341, ECO:0000269|PubMed:22508726}. TISSUE SPECIFICITY: Expressed in spleen, lung and heart with higher expression in testis. No expression in brain, liver and skeletal muscle. Elevated expression in actively cycling cells. {ECO:0000269|PubMed:10086341}. +Q8VD33 SGTB_MOUSE Small glutamine-rich tetratricopeptide repeat-containing protein beta (Beta-SGT) 304 33,429 Chain (1); Compositional bias (1); Modified residue (4); Repeat (4) FUNCTION: Co-chaperone that binds directly to HSC70 and HSP70 and regulates their ATPase activity. {ECO:0000250}. SUBUNIT: Homooligomerize. {ECO:0000250}. +O88890 SH21A_MOUSE SH2 domain-containing protein 1A (Signaling lymphocytic activation molecule-associated protein) (SLAM-associated protein) (T-cell signal transduction molecule SAP) 126 13,904 Alternative sequence (1); Chain (1); Domain (1); Modified residue (1); Mutagenesis (7); Region (1) FUNCTION: Cytoplasmic adapter regulating receptors of the signaling lymphocytic activation molecule (SLAM) family such as SLAMF1, CD244, LY9, CD84, SLAMF6 and SLAMF7. In SLAM signaling seems to cooperate with SH2D1B/EAT-2. Initially it has been proposed that association with SLAMF1 prevents SLAMF1 binding to inhibitory effectors including INPP5D/SHIP1 and PTPN11/SHP-2. However, by simultaneous interactions, recruits FYN which subsequently phosphorylates and activates SLAMF1 (By similarity). Positively regulates CD244/2B4- and CD84-mediated natural killer (NK) cell functions (PubMed:22683124). Can also promote CD48-, SLAMF6 -, LY9-, and SLAMF7-mediated NK cell activation (PubMed:19648922). In the context of NK cell-mediated cytotoxicity enhances conjugate formation with target cells (PubMed:22683124). May also regulate the activity of the neurotrophin receptors NTRK1, NTRK2 and NTRK3. {ECO:0000250|UniProtKB:B2RZ59, ECO:0000250|UniProtKB:O60880, ECO:0000269|PubMed:16223723, ECO:0000269|PubMed:19648922, ECO:0000269|PubMed:20962259, ECO:0000269|PubMed:22683124, ECO:0000305|PubMed:21219180}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. SUBUNIT: Interacts with CD84, CD244, LY9, SLAMF1 and FYN (By similarity). Interacts with NTRK1, NTRK2 and NTRK3. {ECO:0000250|UniProtKB:B2RZ59, ECO:0000250|UniProtKB:O60880, ECO:0000269|PubMed:16223723}. TISSUE SPECIFICITY: T-cells. +D3YZU1 SHAN1_MOUSE SH3 and multiple ankyrin repeat domains protein 1 (Shank1) 2167 226,317 Chain (1); Compositional bias (4); Domain (3); Modified residue (19); Repeat (6); Sequence conflict (1) FUNCTION: Seems to be an adapter protein in the postsynaptic density (PSD) of excitatory synapses that interconnects receptors of the postsynaptic membrane including NMDA-type and metabotropic glutamate receptors, and the actin-based cytoskeleton. Plays a role in the structural and functional organization of the dendritic spine and synaptic junction. Overexpression promotes maturation of dendritic spines and the enlargement of spine heads via its ability to recruit Homer to postsynaptic sites, and enhances presynaptic function (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell junction, synapse {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250}. Note=Colocalizes with alpha-latrotoxin receptor 1. {ECO:0000250}. SUBUNIT: May homomultimerize via its SAM domain. Interacts with the C-terminus of SSTR2 via the PDZ domain. Interacts with SHARPIN, SPTAN1, HOMER1 and DLGAP1/GKAP. Part of a complex with DLG4/PSD-95 and DLGAP1/GKAP. Interacts with BAIAP2. Interacts with IGSF9 (By similarity). Interacts with HOMER1 and HOMER3 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9WV48}. TISSUE SPECIFICITY: In brain, highly expressed in cortex, hyppocampus and cerebellum. {ECO:0000269|PubMed:21423165}. +Q9JI99 SGPP1_MOUSE Sphingosine-1-phosphate phosphatase 1 (SPP) (SPPase1) (mSPP1) (EC 3.1.3.-) (Sphingosine-1-phosphatase 1) 430 47,744 Active site (2); Chain (1); Modified residue (2); Region (3); Site (1); Transmembrane (9) TRANSMEM 121 141 Helical. {ECO:0000255}.; TRANSMEM 152 172 Helical. {ECO:0000255}.; TRANSMEM 193 213 Helical. {ECO:0000255}.; TRANSMEM 216 236 Helical. {ECO:0000255}.; TRANSMEM 246 266 Helical. {ECO:0000255}.; TRANSMEM 279 299 Helical. {ECO:0000255}.; TRANSMEM 311 331 Helical. {ECO:0000255}.; TRANSMEM 348 368 Helical. {ECO:0000255}.; TRANSMEM 409 429 Helical. {ECO:0000255}. FUNCTION: Specifically dephosphorylates sphingosine 1-phosphate (S1P), dihydro-S1P, and phyto-S1P. Does not act on ceramide 1-phoshate, lysophosphatidic acid or phosphatidic acid. Regulates the intracellular levels of the bioactive sphingolipid metabolite S1P that regulates diverse biological processes acting both as an extracellular receptor ligand or as an intracellular second messenger (PubMed:10859351, Ref.2). Involved in efficient ceramide synthesis from exogenous sphingoid bases (PubMed:12235122, PubMed:17895250). Converts S1P to sphingosine, which is readily metabolized to ceramide via ceramide synthase. In concert with sphingosine kinase 2 (SphK2), recycles sphingosine into ceramide though a phosphorylation/dephosphorylation cycle (PubMed:17895250). Regulates intracellular ceramide levels, which in turn regulate apoptosis (PubMed:12235122). Via S1P levels, modulates resting tone, intracellular Ca(2+) and myogenic vasoconstriction in resistance arteries. Also involved in unfolded protein response (UPR) and ER stress-induced autophagy via regulation of intracellular S1P levels (By similarity). {ECO:0000250|UniProtKB:Q9BX95, ECO:0000269|PubMed:10859351, ECO:0000269|PubMed:12235122, ECO:0000269|PubMed:17895250, ECO:0000269|Ref.2}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12235122}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:12235122}; Multi-pass membrane protein {ECO:0000255}. Note=Mainly found in intracellular membrane fractions. {ECO:0000269|PubMed:12235122}. TISSUE SPECIFICITY: Highly expressed in liver and kidney. {ECO:0000269|PubMed:10859351}. +Q80Z38 SHAN2_MOUSE SH3 and multiple ankyrin repeat domains protein 2 (Shank2) (Cortactin-binding protein 1) (CortBP1) 1476 158,969 Alternative sequence (3); Chain (1); Compositional bias (6); Domain (3); Glycosylation (1); Modified residue (9); Motif (1); Sequence conflict (2) FUNCTION: Seems to be an adapter protein in the postsynaptic density (PSD) of excitatory synapses that interconnects receptors of the postsynaptic membrane including NMDA-type and metabotropic glutamate receptors, and the actin-based cytoskeleton. May play a role in the structural and functional organization of the dendritic spine and synaptic junction (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:15207857}. Cell junction, synapse {ECO:0000269|PubMed:15207857}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000269|PubMed:15207857}. Cell projection, dendritic spine {ECO:0000269|PubMed:15207857}. Cell projection, growth cone {ECO:0000250}. Note=Colocalizes with cortactin in growth cones in differentiating hippocampal neurons. Colocalized with PDE4D to the apical membrane of colonic crypt cells (By similarity). Present in the dendritic spines of cerebellar Purkinje cells. {ECO:0000250}. SUBUNIT: Is part of a complex with DLG4/PSD-95 and DLGAP1/GKAP. Interacts with CTTN/cortactin SH3 domain, DLGAP1/GKAP and alpha-latrotoxin receptor 1. Interacts with DNM2, DBNL, GRID2, BAIAP2, SLC9A3, PLCB3 and CFTR. Interacts (via proline-rich region) with PDE4D. Interacts with ABI1 (via SH3 domain). {ECO:0000269|PubMed:15207857, ECO:0000269|PubMed:17244609}. DOMAIN: The PDZ domain is required for interaction with GRID2, PLCB3, SLC9A3 and CFTR. TISSUE SPECIFICITY: Detected in brain (at protein level), where it is highly expressed in Purkinje cells. {ECO:0000269|PubMed:17244609, ECO:0000269|PubMed:21423165, ECO:0000269|PubMed:9742101}. +Q99J19 SI11A_MOUSE Small integral membrane protein 11A (Small integral membrane protein 11) 55 6,345 Chain (1); Coiled coil (1); Transmembrane (1) TRANSMEM 9 29 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in brain, heart, kidney, thymus, liver, stomach, muscle, lung, testis, ovary, skin and eye. +Q3UPR0 SHSA3_MOUSE Protein shisa-3 homolog 238 25,602 Beta strand (4); Chain (1); Compositional bias (1); Helix (2); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 99 119 Helical. {ECO:0000255}. TOPO_DOM 22 98 Lumenal. {ECO:0000305}.; TOPO_DOM 120 238 Cytoplasmic. {ECO:0000305}. FUNCTION: Plays an essential role in the maturation of presomitic mesoderm cells by individual attenuation of both FGF and WNT signaling. {ECO:0000250, ECO:0000269|PubMed:17481602}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q7T0Z7}; Single-pass type I membrane protein {ECO:0000255}. +A2ALV5 SHOC1_MOUSE Protein shortage in chiasmata 1 ortholog (EC 3.6.-.-) 1481 168,065 Chain (1) FUNCTION: ATPase required during meiosis for the formation of crossover recombination intermediates (PubMed:29742103). Binds DNA: preferentially binds to single-stranded DNA and DNA branched structures (By similarity). Does not show nuclease activity in vitro, but shows ATPase activity, which is stimulated by the presence of single-stranded DNA (By similarity). {ECO:0000250|UniProtKB:Q5VXU9, ECO:0000269|PubMed:29742103}. SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:29742103}. Note=Localizes to meiotic chromosomes; associates with mid-stage meiotic recombination intermediates (PubMed:29742103). Localization requires meiotic double-strand breaks (DSBs) recombination intermediates catalyzed by DMC1 (PubMed:29742103). {ECO:0000269|PubMed:29742103}. SUBUNIT: Interacts with TEX11. {ECO:0000250|UniProtKB:Q5VXU9}. TISSUE SPECIFICITY: Mainly expressed in adult testis. {ECO:0000269|PubMed:29742103}. +Q06985 SIA1B_MOUSE E3 ubiquitin-protein ligase SIAH1B (EC 2.3.2.27) (RING-type E3 ubiquitin transferase SIAH1B) (Seven in absentia homolog 1b) (Siah-1b) (Siah1b) 282 31,122 Chain (1); Metal binding (8); Modified residue (1); Region (1); Sequence conflict (1); Zinc finger (2) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates E3 ubiquitin ligase activity either through direct binding to substrates or by functioning as the essential RING domain subunit of larger E3 complexes. Confers constitutive instability to HIPK2 through proteasomal degradation. Probably triggers the ubiquitin-mediated degradation of many substrates. Upon nitric oxid (NO) generation that follows apoptotic stimulation, interacts with S-nitrosylated GAPDH, mediating the translocation of GAPDH to the nucleus. GAPDH acts as a stabilizer of SIAH1, facilitating the degradation of nuclear proteins (By similarity). {ECO:0000250}. PTM: Phosphorylated on Ser-19 by ATM and ATR. This phosphorylation disrupts SIAH1 interaction with HIPK2, and subsequent proteasomal degradation of HIPK2 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Predominantly cytoplasmic. Partially nuclear. {ECO:0000250}. SUBUNIT: Homodimer. Interacts with group 1 glutamate receptors GRM1 and GRM5. Interacts with SNCAIP and HIPK2. Interacts with GAPDH; leading to stabilize SIAH1 (By similarity). Interacts with UBE2E2. Component of some large E3 complex composed of UBE2D1, SIAH1, CACYBP/SIP, SKP1, APC and TBL1X. Interacts with UBE2I. Interacts with alpha-tubulin. Interacts with PEG10, which may inhibit its activity (By similarity). Interacts with DAB1, which may inhibit its activity. Interacts with PEG3 and KLF10 (By similarity). {ECO:0000250}. DOMAIN: The RING-type zinc finger domain is essential for ubiquitin ligase activity.; DOMAIN: The SBD domain (substrate-binding domain) mediates the homodimerization and the interaction with substrate proteins. It is related to the TRAF family. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed at low level in embryos and adults. Due to the high similarity between SIAH1A and SIAH1B, it is difficult to distinguish its own tissue specificity. Overexpressed in endothelial cells of adult lung. {ECO:0000269|PubMed:12842817, ECO:0000269|PubMed:8404535}. +Q9CZN4 SHSA9_MOUSE Protein shisa-9 (Cystine-knot AMPAR modulating protein of 44 kDa) (CKAMP44) 424 46,842 Alternative sequence (4); Chain (1); Erroneous initiation (1); Glycosylation (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 150 170 Helical. {ECO:0000255}. TOPO_DOM 24 149 Extracellular. {ECO:0000255}.; TOPO_DOM 171 424 Cytoplasmic. {ECO:0000255}. FUNCTION: Regulator of short-term neuronal synaptic plasticity in the dentate gyrus. Associates with AMPA receptors (ionotropic glutamate receptors) in synaptic spines and promotes AMPA receptor desensitization at excitatory synapses. {ECO:0000269|PubMed:20185686}. SUBCELLULAR LOCATION: Cell projection, dendritic spine membrane {ECO:0000269|PubMed:20185686}; Single-pass type I membrane protein {ECO:0000269|PubMed:20185686}. Cell junction, synapse {ECO:0000269|PubMed:20185686}. SUBUNIT: Component of some AMPA receptors (ionotropic glutamate receptors) complex, at least composed of some AMPA receptor (GRIA1, GRIA2 and/or GRIA3), CACNG2 and SHISA9, as well as low level of DLG4. {ECO:0000269|PubMed:20185686}. DOMAIN: The extracellular domain contains a pattern of cysteine similar to the snail conotoxin Con-ikot-ikot (AC P0CB20), a toxin known to disrupt AMPA receptors (ionotropic glutamate receptor) desensitization. {ECO:0000269|PubMed:20185686}. TISSUE SPECIFICITY: Brain-specific. Mainly expressed in neurons, including in hippocampus, cerebral cortex, striatum, thalamus, olfactory bulb and cerebellum. Expressed in most brain structures during embryonic and postnatal development. {ECO:0000269|PubMed:20185686}. +Q62226 SHH_MOUSE Sonic hedgehog protein (SHH) (HHG-1) (Shh unprocessed N-terminal signaling and C-terminal autoprocessing domains) (ShhNC) [Cleaved into: Sonic hedgehog protein N-product (ShhN) (Shh N-terminal processed signaling domains) (ShhNp) (Sonic hedgehog protein 19 kDa product)] 437 47,773 Beta strand (9); Chain (2); Compositional bias (1); Glycosylation (1); Helix (7); Lipidation (2); Metal binding (12); Motif (1); Mutagenesis (8); Signal peptide (1); Site (4); Turn (1) FUNCTION: Sonic hedgehog protein: The C-terminal part of the sonic hedgehog protein precursor displays an autoproteolysis and a cholesterol transferase activity (PubMed:8824192, PubMed:7891723). Both activities result in the cleavage of the full-length protein into two parts (ShhN and ShhC) followed by the covalent attachment of a cholesterol moiety to the C-terminal of the newly generated ShhN (PubMed:8824192). Both activities occur in the reticulum endoplasmic (PubMed:21357747). Once cleaved, ShhC is degraded in the endoplasmic reticulum (PubMed:21357747). {ECO:0000269|PubMed:7736596, ECO:0000269|PubMed:7891723, ECO:0000269|PubMed:8824192, ECO:0000305|PubMed:21357747}.; FUNCTION: Sonic hedgehog protein N-product: The dually lipidated sonic hedgehog protein N-product (ShhNp) is a morphogen which is essential for a variety of patterning events during development. Induces ventral cell fate in the neural tube and somites (PubMed:11430830, PubMed:24863049). Involved in the patterning of the anterior-posterior axis of the developing limb bud (PubMed:15315762). Essential for axon guidance (PubMed:12679031). Binds to the patched (PTCH1) receptor, which functions in association with smoothened (SMO), to activate the transcription of target genes (By similarity). In the absence of SHH, PTCH1 represses the constitutive signaling activity of SMO (By similarity). {ECO:0000250|UniProtKB:Q15465, ECO:0000269|PubMed:14687547, ECO:0000269|PubMed:7736596, ECO:0000303|PubMed:24522195}. PTM: Sonic hedgehog protein: The C-terminal domain displays an autoproteolysis activity and a cholesterol transferase activity (PubMed:7891723, PubMed:7736596, PubMed:8824192). Both activities result in the cleavage of the full-length protein and covalent attachment of a cholesterol moiety to the C-terminal of the newly generated N-terminal fragment (ShhN)(PubMed:7891723, PubMed:7736596, PubMed:8824192). Cholesterylation is required for the sonic hedgehog protein N-product targeting to lipid rafts and multimerization (PubMed:24522195, PubMed:8824192). ShhN is the active species in both local and long-range signaling, whereas the C-product (ShhC) is degraded in the reticulum endoplasmic (PubMed:21357747). {ECO:0000269|PubMed:7720571, ECO:0000269|PubMed:7736596, ECO:0000269|PubMed:7891723, ECO:0000269|PubMed:8824192, ECO:0000305|PubMed:21357747, ECO:0000305|PubMed:24522195}.; PTM: Sonic hedgehog protein N-product: N-palmitoylation by HHAT of ShhN is required for sonic hedgehog protein N-product multimerization and full activity (PubMed:11486055, PubMed:15075292). It is a prerequisite for the membrane-proximal positioning and the subsequent shedding of this N-terminal peptide (PubMed:24522195). {ECO:0000269|PubMed:11486055, ECO:0000269|PubMed:15075292, ECO:0000269|PubMed:24522195}.; PTM: Sonic hedgehog protein N-product: The lipidated N- and C-terminal peptides of ShhNp can be cleaved (shedding)(PubMed:24522195). The N-terminal palmitoylated peptide is cleaved at the Cardin-Weintraub (CW) motif site (PubMed:24522195). The cleavage reduced the interactions with heparan sulfate (PubMed:23118222). The cleavage is enhanced by SCUBE2. {ECO:0000269|PubMed:23118222, ECO:0000269|PubMed:24522195}. SUBCELLULAR LOCATION: Sonic hedgehog protein N-product: Cell membrane {ECO:0000269|PubMed:7891723}; Lipid-anchor {ECO:0000269|PubMed:7891723}. Note=The dual-lipidated sonic hedgehog protein N-product (ShhNp) is firmly tethered to the cell membrane where it forms multimers (PubMed:24522195). Further solubilization and release from the cell surface seem to be achieved through different mechanisms, including the interaction with DISP1 and SCUBE2, movement by lipoprotein particles, transport by cellular extensions called cytonemes or by the proteolytic removal of both terminal lipidated peptides. {ECO:0000269|PubMed:24522195, ECO:0000305|PubMed:22677548}. SUBUNIT: Interacts with HHATL/GUP1 which negatively regulates HHAT-mediated palmitoylation of the SHH N-terminus (PubMed:18081866). ShhNp is active as a multimer (PubMed:24522195). Interacts with BOC and CDON (PubMed:18794898). Interacts with HHIP (By similarity). Interacts with DISP1 via its cholesterol anchor (PubMed:22902404, PubMed:22677548). Interacts with SCUBE2 (PubMed:24522195, PubMed:22677548). Interacts with glypican GPC3 (PubMed:18477453). {ECO:0000250|UniProtKB:Q15465, ECO:0000269|PubMed:15075292, ECO:0000269|PubMed:18081866, ECO:0000269|PubMed:18477453, ECO:0000269|PubMed:18794898, ECO:0000269|PubMed:19561611, ECO:0000269|PubMed:20519495, ECO:0000269|PubMed:22677548, ECO:0000269|PubMed:24522195, ECO:0000269|PubMed:7477329}. DOMAIN: Sonic hedgehog protein N-product: Binds calcium and zinc ions; this stabilizes the protein fold and is essential for protein-protein interactions mediated by this domain. {ECO:0000269|PubMed:18794898, ECO:0000269|PubMed:19561611, ECO:0000269|PubMed:20519495}.; DOMAIN: Sonic hedgehog protein N-product: The Cardin-Weintraub (CW) motif is required for heparan sulfate binding of the solubilized ShhNp (PubMed:23118222). The N-terminal palmitoylated peptide is cleaved at the heparan sulfate-binding Cardin-Weintraub (CW) motif site (PubMed:24522195). The cleavage reduced the interactions with heparan sulfate. The cleavage is enhanced by SCUBE2 (PubMed:24522195). {ECO:0000269|PubMed:23118222, ECO:0000269|PubMed:24522195}. TISSUE SPECIFICITY: Expressed in a number of embryonic tissues including the notochord, ventral neural tube, floor plate, lung bud, zone of polarizing activity and posterior distal mesenchyme of limbs. In the adult, expressed in lung and neural retina. +Q11204 SIA4B_MOUSE CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 2 (Alpha 2,3-ST 2) (Beta-galactoside alpha-2,3-sialyltransferase 2) (EC 2.4.99.4) (Gal-NAc6S) (Gal-beta-1,3-GalNAc-alpha-2,3-sialyltransferase) (ST3Gal II) (ST3GalII) (ST3GalA.2) (Sialyltransferase 4B) (SIAT4-B) 350 40,130 Binding site (9); Chain (1); Disulfide bond (3); Glycosylation (1); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 7 27 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 28 350 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Responsible for the synthesis of the sequence NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc- found in terminal carbohydrate groups of certain glycoproteins, oligosaccharides and glycolipids. SIAT4A and SIAT4B sialylate the same acceptor substrates but exhibit different Km values. {ECO:0000269|PubMed:8144500, ECO:0000269|PubMed:9184827}. PTM: The soluble form derives from the membrane form by proteolytic processing. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. Secreted. Note=Membrane-bound form in trans cisternae of Golgi. Secreted into the body fluid. TISSUE SPECIFICITY: Strongly expressed in brain and liver and to a lesser extent in heart and kidney. Scarcely detectable in lung, pancreas, spleen and submaxillary gland. {ECO:0000269|PubMed:8144500}. +Q9ES52 SHIP1_MOUSE Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1 (EC 3.1.3.86) (Inositol polyphosphate-5-phosphatase of 145 kDa) (SIP-145) (SH2 domain-containing inositol 5'-phosphatase 1) (SH2 domain-containing inositol phosphatase 1) (SHIP-1) (p150Ship) 1191 133,542 Alternative sequence (5); Chain (1); Compositional bias (1); Domain (1); Modified residue (8); Motif (5); Mutagenesis (3); Region (1); Sequence conflict (5) FUNCTION: Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways. Acts as a negative regulator of B-cell antigen receptor signaling. Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems. Acts as a negative regulator of myeloid cell proliferation/survival and chemotaxis, mast cell degranulation, immune cells homeostasis, integrin alpha-IIb/beta-3 signaling in platelets and JNK signaling in B-cells. Regulates proliferation of osteoclast precursors, macrophage programming, phagocytosis and activation and is required for endotoxin tolerance. Involved in the control of cell-cell junctions, CD32a signaling in neutrophils and modulation of EGF-induced phospholipase C activity. Key regulator of neutrophil migration, by governing the formation of the leading edge and polarization required for chemotaxis. Modulates FCGR3/CD16-mediated cytotoxicity in NK cells. Mediates the activin/TGF-beta-induced apoptosis through its Smad-dependent expression. May also hydrolyze PtdIns(1,3,4,5)P4, and could thus affect the levels of the higher inositol polyphosphates like InsP6. {ECO:0000269|PubMed:11136821, ECO:0000269|PubMed:11222379, ECO:0000269|PubMed:11359765, ECO:0000269|PubMed:11896575, ECO:0000269|PubMed:12161749, ECO:0000269|PubMed:12370370, ECO:0000269|PubMed:12447389, ECO:0000269|PubMed:12882960, ECO:0000269|PubMed:14993273, ECO:0000269|PubMed:15166241, ECO:0000269|PubMed:17142780, ECO:0000269|PubMed:17173042, ECO:0000269|PubMed:8654924, ECO:0000269|PubMed:8805703, ECO:0000269|PubMed:9244303, ECO:0000269|PubMed:9620849, ECO:0000269|PubMed:9736736, ECO:0000269|PubMed:9763612, ECO:0000269|PubMed:9857188}. PTM: Tyrosine phosphorylated by the members of the SRC family after exposure to a diverse array of extracellular stimuli such as cytokines, growth factors, antibodies, chemokines, integrin ligands and hypertonic and oxidative stress. Phosphorylated upon IgG receptor FCGR2B-binding. {ECO:0000269|PubMed:10068665, ECO:0000269|PubMed:10395202, ECO:0000269|PubMed:10660611, ECO:0000269|PubMed:12370370, ECO:0000269|PubMed:8654924, ECO:0000269|PubMed:8805618, ECO:0000269|PubMed:9099679}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16406061}. Cell membrane {ECO:0000269|PubMed:12393695}; Peripheral membrane protein {ECO:0000305|PubMed:12393695}. Membrane raft {ECO:0000269|PubMed:12393695}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9694708}. Note=Translocates to the plasma membrane when activated, translocation is probably due to different mechanisms depending on the stimulus and cell type (PubMed:12393695). Translocates from the cytoplasm to membrane ruffles in a FCGR3/CD16-dependent manner (PubMed:12393695). Colocalizes with FC-gamma-RIIB receptor (FCGR2B) or FCGR3/CD16 at membrane ruffles (PubMed:12393695). Tyrosine phosphorylation may also participate in membrane localization (PubMed:12393695). {ECO:0000269|PubMed:12393695}.; SUBCELLULAR LOCATION: Isoform 5: Cell membrane {ECO:0000269|PubMed:11567986}; Peripheral membrane protein {ECO:0000305|PubMed:11567986}. Note=Constitutively present at the cell membrane (PubMed:11567986). {ECO:0000269|PubMed:11567986}. SUBUNIT: Interacts with tyrosine phosphorylated form of SHC1 (PubMed:8654924, PubMed:8643691, PubMed:10068665, PubMed:9083021, PubMed:9099679, PubMed:10395202). Interacts with tyrosine phosphorylated form of DOK1 (PubMed:11031258). Interacts with tyrosine phosphorylated form of DOK3 (PubMed:14993273). Interacts with tyrosine phosphorylated form of SLAMF1/CD150 (By similarity). Interacts with PTPN11/SHP-2 in response to IL-3 (PubMed:9110989, PubMed:9393882). Interacts with receptor EPOR (PubMed:10660611). Interacts with receptors MS4A2/FCER1B and FCER1G (By similarity). Interacts with receptors FCGR2B and FCGR3 (PubMed:10395202, PubMed:11016922, PubMed:10779347, PubMed:15456754, PubMed:12393695). Interacts with receptor FCGR2A, leading to regulate gene expression during the phagocytic process (PubMed:12370370). Interacts with GRB2 (PubMed:8643691, PubMed:10068665). Interacts with PLCG1 (PubMed:16000869). Interacts with tyrosine kinases SRC and TEC (PubMed:10794720, PubMed:15492005). Interacts with CRKL (PubMed:11031258). Interacts with c-Met/MET (PubMed:11896575). Interacts with MILR1 (tyrosine-phosphorylated) (PubMed:20526344). Isoform 5 interacts with IL6ST/gp130 (PubMed:17105399). Can weakly interact (via NPXY motif 2) with DAB2 (via PID domain); the interaction is impaired by tyrosine phosphorylation of the NPXY motif (PubMed:11247302). {ECO:0000250|UniProtKB:P97573, ECO:0000250|UniProtKB:Q92835, ECO:0000269|PubMed:10068665, ECO:0000269|PubMed:10395202, ECO:0000269|PubMed:10660611, ECO:0000269|PubMed:10779347, ECO:0000269|PubMed:10794720, ECO:0000269|PubMed:11016922, ECO:0000269|PubMed:11031258, ECO:0000269|PubMed:11247302, ECO:0000269|PubMed:11896575, ECO:0000269|PubMed:12370370, ECO:0000269|PubMed:12393695, ECO:0000269|PubMed:14993273, ECO:0000269|PubMed:15456754, ECO:0000269|PubMed:15492005, ECO:0000269|PubMed:16000869, ECO:0000269|PubMed:17105399, ECO:0000269|PubMed:20526344, ECO:0000269|PubMed:8643691, ECO:0000269|PubMed:8654924, ECO:0000269|PubMed:9083021, ECO:0000269|PubMed:9099679, ECO:0000269|PubMed:9110989, ECO:0000269|PubMed:9393882}. DOMAIN: The SH2 domain interacts with tyrosine phosphorylated forms of proteins such as SHC1 or PTPN11/SHP-2. It competes with that of GRB2 for binding to phosphorylated SHC1 to inhibit the Ras pathway. It is also required for tyrosine phosphorylation. {ECO:0000269|PubMed:9083021}.; DOMAIN: The NPXY sequence motif found in many tyrosine-phosphorylated proteins is required for the specific binding of the PID domain. {ECO:0000269|PubMed:9083021}. TISSUE SPECIFICITY: Specifically expressed in immune and hematopoietic cells. Levels vary considerably within this compartment. Lost during erythropoiesis when erythroid cells become Ter119+. Increases substantially with T-cell maturation and when resting B-cells are activated. Also present in mature granulocytes, monocyte/macrophages, mast cells and platelets. Isoform 5 is the only form expressed in embryonic stem (ES) cells and is coexpressed with other isoforms in hematopoietic stem cells, and disappears with differentiation. {ECO:0000269|PubMed:10068665, ECO:0000269|PubMed:8643691, ECO:0000269|PubMed:8654924, ECO:0000269|PubMed:9531585}. +Q9EQU3 TLR9_MOUSE Toll-like receptor 9 (CD antigen CD289) 1032 116,412 Beta strand (40); Binding site (2); Chain (1); Disulfide bond (8); Domain (1); Glycosylation (18); Helix (22); Mutagenesis (12); Region (4); Repeat (26); Sequence conflict (20); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (13) TRANSMEM 819 839 Helical. {ECO:0000255}. TOPO_DOM 26 818 Extracellular. {ECO:0000255}.; TOPO_DOM 840 1032 Cytoplasmic. {ECO:0000255}. FUNCTION: Key component of innate and adaptive immunity. TLRs (Toll-like receptors) control host immune response against pathogens through recognition of molecular patterns specific to microorganisms. TLR9 is a nucleotide-sensing TLR which is activated by unmethylated cytidine-phosphate-guanosine (CpG) dinucleotides. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (PubMed:18931679, PubMed:21402738, PubMed:14993594, PubMed:17474149, PubMed:25686612, PubMed:18820679). Plays a role in defense against systemic mouse cytomegalovirus infection (PubMed:14993594). Controls lymphocyte response to Helicobacter infection (PubMed:17474149). Upon CpG stimulation, induces B-cell proliferation, activation, survival and antibody production (By similarity). {ECO:0000250|UniProtKB:Q9NR96, ECO:0000269|PubMed:14993594, ECO:0000269|PubMed:17474149, ECO:0000269|PubMed:18820679, ECO:0000269|PubMed:18931679, ECO:0000269|PubMed:21402738, ECO:0000269|PubMed:25686612}. PTM: Activated by proteolytic cleavage of the flexible loop between repeats LRR14 and LRR15 within the ectodomain (PubMed:18931679, PubMed:18820679). Cleavage requires UNC93B1 (PubMed:18820679). Proteolytically processed by first removing the majority of the ectodomain by either asparagine endopeptidase (AEP) or a cathepsin followed by a trimming event that is solely cathepsin mediated and required for optimal receptor signaling (PubMed:21402738). {ECO:0000269|PubMed:18820679, ECO:0000269|PubMed:18931679, ECO:0000269|PubMed:21402738}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18305481}; Single-pass type I membrane protein {ECO:0000269|PubMed:18305481}. Endosome {ECO:0000269|PubMed:18305481}. Lysosome {ECO:0000269|PubMed:18305481, ECO:0000269|PubMed:18820679}. Cytoplasmic vesicle, phagosome {ECO:0000269|PubMed:18305481, ECO:0000269|PubMed:18820679}. Note=Relocalizes from endoplasmic reticulum to endosome and lysosome upon stimulation with agonist (PubMed:18305481). Exit from the ER requires UNC93B1 (PubMed:18820679). Endolysosomal localization is required for proteolytic cleavage and subsequent activation (PubMed:18931679, PubMed:18820679). Intracellular localization of the active receptor may prevent from responding to self nucleic acid (PubMed:18820679). {ECO:0000269|PubMed:18305481, ECO:0000269|PubMed:18820679, ECO:0000269|PubMed:18931679}. SUBUNIT: Monomer and homodimer. Exists as a monomer in the absence of unmethylated cytidine-phosphate-guanosine (CpG) ligand. Proteolytic processing of an insertion loop (Z-loop) is required for homodimerization upon binding to the unmethylated CpG ligand leading to its activation (By similarity). Interacts with MYD88 via their respective TIR domains (PubMed:18820679). Interacts with BTK (By similarity). Interacts (via transmembrane domain) with UNC93B1 (PubMed:17452530, PubMed:18931679). Interacts with CD300LH; the interaction may promote full activation of TLR9-triggered innate responses (PubMed:21940676). Interacts with CNPY3 and HSP90B1; this interaction is required for proper folding in the endoplasmic reticulum (PubMed:18780723, PubMed:20865800). Interacts with SMPDL3B (PubMed:26095358). {ECO:0000250|UniProtKB:Q2EEY0, ECO:0000250|UniProtKB:Q9NR96, ECO:0000269|PubMed:17452530, ECO:0000269|PubMed:18780723, ECO:0000269|PubMed:18820679, ECO:0000269|PubMed:18931679, ECO:0000269|PubMed:20865800, ECO:0000269|PubMed:21940676, ECO:0000269|PubMed:26095358}. TISSUE SPECIFICITY: Expressed in the basolateral region of gastric epithelial cells with high levels detected in antrum and body mucosa (at protein level). Detected in spleen and stomach at higher levels in C57BL/6 mice than BALB/C. {ECO:0000269|PubMed:17474149}. +Q6P549 SHIP2_MOUSE Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2 (EC 3.1.3.86) (AblSH3-binding protein) (Inositol polyphosphate phosphatase-like protein 1) (INPPL-1) (SH2 domain-containing inositol 5'-phosphatase 2) (SH2 domain-containing inositol phosphatase 2) (SHIP-2) 1257 138,973 Chain (1); Compositional bias (1); Domain (2); Erroneous initiation (1); Helix (6); Modified residue (11); Motif (2); Mutagenesis (7); Sequence conflict (4) FUNCTION: Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways. Plays a central role in regulation of PI3K-dependent insulin signaling, although the precise molecular mechanisms and signaling pathways remain unclear. While overexpression reduces both insulin-stimulated MAP kinase and Akt activation, its absence does not affect insulin signaling or GLUT4 trafficking. Confers resistance to dietary obesity. May act by regulating AKT2, but not AKT1, phosphorylation at the plasma membrane. Part of a signaling pathway that regulates actin cytoskeleton remodeling. Required for the maintenance and dynamic remodeling of actin structures as well as in endocytosis, having a major impact on ligand-induced EGFR internalization and degradation. Participates in regulation of cortical and submembraneous actin by hydrolyzing PtdIns(3,4,5)P3 thereby regulating membrane ruffling (By similarity). Regulates cell adhesion and cell spreading (PubMed:29749928). Required for HGF-mediated lamellipodium formation, cell scattering and spreading. Acts as a negative regulator of EPHA2 receptor endocytosis by inhibiting via PI3K-dependent Rac1 activation. Acts as a regulator of neuritogenesis by regulating PtdIns(3,4,5)P3 level and is required to form an initial protrusive pattern, and later, maintain proper neurite outgrowth. Acts as a negative regulator of the FC-gamma-RIIA receptor (FCGR2A). Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems. Involved in EGF signaling pathway. Upon stimulation by EGF, it is recruited by EGFR and dephosphorylates PtdIns(3,4,5)P3. Plays a negative role in regulating the PI3K-PKB pathway, possibly by inhibiting PKB activity. Down-regulates Fc-gamma-R-mediated phagocytosis in macrophages independently of INPP5D/SHIP1. In macrophages, down-regulates NF-kappa-B-dependent gene transcription by regulating macrophage colony-stimulating factor (M-CSF)-induced signaling. May also hydrolyze PtdIns(1,3,4,5)P4, and could thus affect the levels of the higher inositol polyphosphates like InsP6. Involved in endochondral ossification (By similarity). {ECO:0000250|UniProtKB:O15357, ECO:0000269|PubMed:10958682, ECO:0000269|PubMed:11343120, ECO:0000269|PubMed:14744864, ECO:0000269|PubMed:15557176, ECO:0000269|PubMed:15654325, ECO:0000269|PubMed:16179375, ECO:0000269|PubMed:29749928}. PTM: Tyrosine phosphorylated by the members of the SRC family after exposure to a diverse array of extracellular stimuli such as insulin, growth factors such as EGF or PDGF, chemokines, integrin ligands and hypertonic and oxidative stress. May be phosphorylated upon IgG receptor FCGR2B-binding. Phosphorylated at Tyr-987 following cell attachment and spreading. Phosphorylated at Tyr-1161 following EGF signaling pathway stimulation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cytoplasm, cytoskeleton {ECO:0000250}. Membrane; Peripheral membrane protein. Cell projection, filopodium {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Note=Translocates to membrane ruffles when activated, translocation is probably due to different mechanisms depending on the stimulus and cell type. Partly translocated via its SH2 domain which mediates interaction with tyrosine phosphorylated receptors such as the FC-gamma-RIIB receptor (FCGR2B). Tyrosine phosphorylation may also participate in membrane localization. Insulin specifically stimulates its redistribution from the cytosol to the plasma membrane. Recruited to the membrane following M-CSF stimulation. In activated spreading platelets, localizes with actin at filopodia, lamellipodia and the central actin ring. SUBUNIT: Interacts with tyrosine phosphorylated form of SHC1 (By similarity). Interacts with EGFR (By similarity). Upon stimulation by the EGF signaling pathway, it forms a complex with SHC1 and EGFR (By similarity). Interacts with cytoskeletal protein SORBS3/vinexin, promoting its localization to the periphery of cells (By similarity). Forms a complex with filamin (FLNA or FLNB), actin, GPIb (GP1BA or GP1BB) that regulates cortical and submembraneous actin (By similarity). Interacts with c-Met/MET, when c-Met/MET is phosphorylated on 'Tyr-1356' (By similarity). Interacts with p130Cas/BCAR1 (By similarity). Interacts with CENTD3/ARAP3 via its SAM domain (By similarity). Interacts with c-Cbl/CBL and CAP/SORBS1 (By similarity). Interacts with activated EPHA2 receptor (PubMed:29749928). Interacts with receptors FCGR2A (By similarity). Interacts with FCGR2B (PubMed:10789675, PubMed:15456754). Interacts with tyrosine kinase ABL1 (By similarity). Interacts with tyrosine kinase TEC (PubMed:15492005). Interacts with CSF1R (PubMed:15557176). Interacts (via N-terminus) with SH3YL1 (via SH3 domain) (PubMed:21624956). {ECO:0000250|UniProtKB:O15357, ECO:0000269|PubMed:10789675, ECO:0000269|PubMed:15456754, ECO:0000269|PubMed:15492005, ECO:0000269|PubMed:15557176, ECO:0000269|PubMed:21624956, ECO:0000269|PubMed:29749928}. DOMAIN: The SH2 domain interacts with tyrosine phosphorylated forms of proteins such as SHC1 or FCGR2A. It also mediates the interaction with p130Cas/BCAR1 (By similarity). {ECO:0000250}.; DOMAIN: The NPXY sequence motif found in many tyrosine-phosphorylated proteins is required for the specific binding of the PID domain. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10610720}. +Q80W04 TMCC2_MOUSE Transmembrane and coiled-coil domains protein 2 706 77,054 Chain (1); Coiled coil (2); Modified residue (6); Transmembrane (2) TRANSMEM 646 666 Helical. {ECO:0000255}.; TRANSMEM 679 699 Helical. {ECO:0000255}. FUNCTION: May be involved in the regulation of the proteolytic processing of the amyloid precursor protein (APP) possibly also implicating APOE. {ECO:0000250|UniProtKB:O75069}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O75069}; Multi-pass membrane protein {ECO:0000255}. Note=Concentrates in discrete patches along peripheral endoplasmic reticulum tubules. {ECO:0000250|UniProtKB:O75069}. SUBUNIT: May form homodimers and heterodimers with TMCC2 or TMCC3 via the coiled-coil domains. Interacts with ribosomal proteins RPL4 and RPS6. Interacts with APOE and proteolytic processed C-terminal fragment C99 of the amyloid precursor protein (APP C99). {ECO:0000250|UniProtKB:O75069}. +P0C1V4 TMCO2_MOUSE Transmembrane and coiled-coil domain-containing protein 2 183 20,331 Chain (1); Coiled coil (1); Erroneous termination (1); Sequence conflict (1); Transmembrane (1) TRANSMEM 54 74 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q8BH01 TMCO3_MOUSE Transmembrane and coiled-coil domain-containing protein 3 678 75,903 Alternative sequence (3); Chain (1); Coiled coil (1); Compositional bias (1); Glycosylation (3); Sequence conflict (2); Signal peptide (1); Transmembrane (10) TRANSMEM 286 306 Helical. {ECO:0000255}.; TRANSMEM 317 337 Helical. {ECO:0000255}.; TRANSMEM 350 370 Helical. {ECO:0000255}.; TRANSMEM 417 437 Helical. {ECO:0000255}.; TRANSMEM 457 477 Helical. {ECO:0000255}.; TRANSMEM 499 519 Helical. {ECO:0000255}.; TRANSMEM 555 575 Helical. {ECO:0000255}.; TRANSMEM 579 599 Helical. {ECO:0000255}.; TRANSMEM 609 629 Helical. {ECO:0000255}.; TRANSMEM 641 661 Helical. {ECO:0000255}. FUNCTION: Probable Na(+)/H(+) antiporter. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q91WU4 TMCO4_MOUSE Transmembrane and coiled-coil domain-containing protein 4 631 67,945 Alternative sequence (3); Chain (1); Coiled coil (1); Sequence conflict (4); Transmembrane (3) TRANSMEM 200 220 Helical. {ECO:0000255}.; TRANSMEM 228 248 Helical. {ECO:0000255}.; TRANSMEM 343 363 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8BQX5 TMCO6_MOUSE Transmembrane and coiled-coil domain-containing protein 6 494 54,915 Alternative sequence (2); Chain (1); Coiled coil (1); Compositional bias (1); Erroneous translation (1); Frameshift (1); Sequence conflict (2); Transmembrane (2) TRANSMEM 338 358 Helical. {ECO:0000255}.; TRANSMEM 386 406 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9D2R4 TMD11_MOUSE Transmembrane emp24 domain-containing protein 11 (Glycoprotein 25L) (GP25L) (p24 family protein alpha-1) (p24alpha1) 215 24,842 Chain (1); Coiled coil (1); Domain (1); Glycosylation (1); Motif (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 168 185 Helical. {ECO:0000255}. TOPO_DOM 18 167 Lumenal. {ECO:0000255}.; TOPO_DOM 186 215 Cytoplasmic. {ECO:0000255}. FUNCTION: Part of a complex whose function is to bind Ca(2+) to the ER membrane and thereby regulate the retention of ER resident proteins. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. +Q3V009 TMED1_MOUSE Transmembrane emp24 domain-containing protein 1 (Interleukin-1 receptor-like 1 ligand) (Putative T1/ST2 receptor-binding protein) (p24 family protein gamma-1) (p24gamma1) 227 25,263 Alternative sequence (2); Chain (1); Coiled coil (1); Domain (1); Motif (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 195 215 Helical. {ECO:0000255}. TOPO_DOM 25 194 Extracellular. {ECO:0000255}.; TOPO_DOM 216 227 Cytoplasmic. {ECO:0000255}. FUNCTION: Potential role in vesicular protein trafficking, mainly in the early secretory pathway. May act as a cargo receptor at the lumenal side for incorporation of secretory cargo molecules into transport vesicles and may be involved in vesicle coat formation at the cytoplasmic side. {ECO:0000250|UniProtKB:Q13445}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q13445}; Single-pass type I membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q13445}; Single-pass type I membrane protein {ECO:0000255}. Golgi apparatus, cis-Golgi network membrane {ECO:0000250|UniProtKB:Q13445}; Single-pass type I membrane protein {ECO:0000255}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q13445}; Single-pass type I membrane protein {ECO:0000255}. SUBUNIT: Homodimer in endoplasmic reticulum, endoplasmic reticulum-Golgi intermediate compartment and cis-Golgi network. May interact with IL1RL1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:8621446}. +Q9R0Q3 TMED2_MOUSE Transmembrane emp24 domain-containing protein 2 (COPI-coated vesicle membrane protein p24) (Membrane protein p24A) (Sid 394) (p24 family protein beta-1) (p24beta1) 201 22,705 Chain (1); Coiled coil (1); Domain (1); Motif (2); Mutagenesis (1); Region (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 169 189 Helical. {ECO:0000255}. TOPO_DOM 21 168 Lumenal. {ECO:0000255}.; TOPO_DOM 190 201 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in vesicular protein trafficking. Mainly functions in the early secretory pathway but also in post-Golgi membranes. Thought to act as cargo receptor at the lumenal side for incorporation of secretory cargo molecules into transport vesicles and to be involved in vesicle coat formation at the cytoplasmic side. In COPII vesicle-mediated anterograde transport involved in the transport of GPI-anchored proteins and proposed to act together with TMED10 as their cargo receptor; the function specifically implies SEC24C and SEC24D of the COPII vesicle coat and lipid raft-like microdomains of the ER. Recognizes GPI anchors structural remodeled in the ER by PGAP1 and MPPE1. In COPI vesicle-mediated retrograde transport inhibits the GTPase-activating activity of ARFGAP1 towards ARF1 thus preventing immature uncoating and allowing cargo selection to take place. Involved in trafficking of G protein-coupled receptors (GPCRs). Regulates F2RL1, OPRM1 and P2RY4 exocytic trafficking from the Golgi to the plasma membrane thus contributing to receptor resensitization. Facilitates CASR maturation and stabilization in the early secretory pathway and increases CASR plasma membrane targeting. Proposed to be involved in organization of intracellular membranes such as the maintenance of the Golgi apparatus. May also play a role in the biosynthesis of secreted cargo such as eventual processing (By similarity). Required for morphogenesis of embryo and placenta. {ECO:0000250, ECO:0000269|PubMed:20178780}. SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q15363}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250|UniProtKB:Q15363}; Single-pass type I membrane protein {ECO:0000255}. Golgi apparatus, cis-Golgi network membrane {ECO:0000250|UniProtKB:Q15363}; Single-pass type I membrane protein {ECO:0000255}. Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:Q15363}; Single-pass type I membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q15363}; Single-pass type I membrane protein {ECO:0000255}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q15363}; Single-pass type I membrane protein {ECO:0000255}. Note=Cycles between compartments of the early secretatory pathway. {ECO:0000250|UniProtKB:Q15363}. SUBUNIT: Monomer and homodimer in the endoplasmic reticulum, endoplasmic reticulum-Golgi intermediate compartment and Golgi. Probably oligomerizes with other members of the EMP24/GP25L family such as TMED7, TMED9 and TMED10. Interacts (via GOLD domain) with TMED10 (via GOLD domain). Associates with the COPI vesicle coat (coatomer); TMED10:TMED2 heterotetramers are proposed to be involved in coatomer association. Interacts (via C-terminus) with COPG1; the interaction involves dimeric TMED2. Interacts with SEC23A; indicative for an association of TMED2 with the COPII vesicle coat. Interacts with ARF1 and ARFGAP1. Interacts with CD59, SEC24A, SEC24B, SEC24C, SEC24D and ATLA1. Interacts with KDELR1; the interaction is decreased by KDEL ligand. Interacts with F2RL1; the interaction occurs at the Golgi apparatus. Interacts with CASR (immaturely glycosylated form); the interaction occurs in the endoplasmic reticulum-Golgi intermediate compartment or cis-Golgi. Interacts with F2RL1; the interaction occurs at the Golgi apparatus. Interacts with GORASP1 and GORASP2. Found in a complex composed at least of SURF4, TMED2 and TMED10 (By similarity). {ECO:0000250|UniProtKB:Q15363, ECO:0000250|UniProtKB:Q63524}. +Q78IS1 TMED3_MOUSE Transmembrane emp24 domain-containing protein 3 (p24 family protein gamma-4) (p24gamma4) 221 25,465 Chain (1); Domain (1); Frameshift (1); Modified residue (2); Motif (2); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 185 205 Helical. {ECO:0000255}. TOPO_DOM 28 184 Lumenal. {ECO:0000255}.; TOPO_DOM 206 221 Cytoplasmic. {ECO:0000255}. FUNCTION: Potential role in vesicular protein trafficking, mainly in the early secretory pathway. Contributes to the coupled localization of TMED2 and TMED10 in the cis-Golgi network (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q9Y3Q3}; Single-pass type I membrane protein {ECO:0000255}. Golgi apparatus, cis-Golgi network membrane {ECO:0000250|UniProtKB:Q9Y3Q3}; Single-pass type I membrane protein {ECO:0000255}. Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:Q6AY25}; Single-pass type I membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9Y3Q3}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250|UniProtKB:Q9Y3Q3}; Single-pass type I membrane protein {ECO:0000255}. Note=Probably cycles between compartments of the early secretatory pathway. {ECO:0000250|UniProtKB:Q9Y3Q3}. SUBUNIT: Monomer in endoplasmic reticulum, endoplasmic reticulum-Golgi intermediate compartment and cis-Golgi network. Interacts (via C-terminus) with COPG1; the interaction involves dimeric TMED3; however, there are conflicting reports on the interaction. Interacts with GORASP1 and GORASP2 (By similarity). {ECO:0000250}. +Q8R1V4 TMED4_MOUSE Transmembrane emp24 domain-containing protein 4 (Endoplasmic reticulum stress-response protein 25) (ERS25) (p24 family protein alpha-3) (p24alpha3) (p26) 227 26,022 Chain (1); Coiled coil (1); Domain (1); Glycosylation (1); Motif (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 195 212 Helical. {ECO:0000255}. TOPO_DOM 30 194 Lumenal. {ECO:0000255}.; TOPO_DOM 213 227 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in vesicular protein trafficking, mainly in the early secretory pathway. Involved in the maintenance of the Golgi apparatus. Appears to play a role in the biosynthesis of secreted cargo including processing. Involved in endoplasmic reticulum stress response. May play a role in the regulation of heat-shock response and apoptosis (By similarity). {ECO:0000250, ECO:0000269|PubMed:18326488}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18326488}; Single-pass type I membrane protein {ECO:0000269|PubMed:18326488}. +Q9CXE7 TMED5_MOUSE Transmembrane emp24 domain-containing protein 5 (p24 family protein gamma-2) (p24gamma2) 229 26,172 Beta strand (7); Chain (1); Domain (1); Helix (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 197 217 Helical. {ECO:0000255}. TOPO_DOM 28 196 Lumenal. {ECO:0000255}.; TOPO_DOM 218 229 Cytoplasmic. {ECO:0000255}. FUNCTION: Potential role in vesicular protein trafficking, mainly in the early secretory pathway. Required for the maintenance of the Golgi apparatus; involved in protein exchange between Golgi stacks during assembly. Probably not required for COPI-vesicle-mediated retrograde transport (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Golgi apparatus, cis-Golgi network membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Probably cycles between compartments of the early secretatory pathway. {ECO:0000250}. SUBUNIT: Interacts with TMED9 and TMED10. {ECO:0000250}. +Q9CQG0 TMED6_MOUSE Transmembrane emp24 domain-containing protein 6 (p24 family protein gamma-5) (p24gamma5) 239 27,673 Chain (1); Domain (1); Glycosylation (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 201 223 Helical. {ECO:0000255}. TOPO_DOM 22 200 Lumenal. {ECO:0000255}.; TOPO_DOM 224 239 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. +Q3UHI4 TMED8_MOUSE Protein TMED8 326 35,785 Chain (1); Compositional bias (1); Domain (1); Modified residue (1) +Q9D7Y9 SLX4I_MOUSE Protein SLX4IP (SLX4-interacting protein) 413 45,736 Alternative sequence (3); Chain (1); Cross-link (9); Modified residue (1) SUBUNIT: Interacts with SLX4/BTBD12; subunit of different structure-specific endonucleases. {ECO:0000250}. +Q91VZ6 SMAP1_MOUSE Stromal membrane-associated protein 1 440 47,660 Chain (1); Domain (1); Motif (1); Mutagenesis (2); Sequence caution (1); Zinc finger (1) FUNCTION: GTPase activating protein that acts on ARF6. Plays a role in clathrin-dependent endocytosis. May play a role in erythropoiesis. {ECO:0000269|PubMed:15659652, ECO:0000269|PubMed:9644265}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:9644265}; Peripheral membrane protein {ECO:0000305|PubMed:9644265}; Cytoplasmic side {ECO:0000305|PubMed:9644265}. SUBUNIT: Interacts with ARF6. Interacts with clathrin heavy chains via the clathrin box-like motif. {ECO:0000269|PubMed:15659652}. TISSUE SPECIFICITY: Detected in adult brain, lung, heart, liver, ovary and bone marrow. Detected in stromal cells of the red pulp of adult spleen. {ECO:0000269|PubMed:9644265}. +Q7TN29 SMAP2_MOUSE Stromal membrane-associated protein 2 (Stromal membrane-associated protein 1-like) 428 46,578 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (1); Modified residue (5); Mutagenesis (3); Region (2); Sequence conflict (2); Zinc finger (1) FUNCTION: GTPase activating protein that acts on ARF1. Can also activate ARF6 (in vitro). May play a role in clathrin-dependent retrograde transport from early endosomes to the trans-Golgi network. {ECO:0000269|PubMed:16571680}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16571680}. Note=Detected in multiple foci throughout the cytoplasm and in juxtanuclear structures. SUBUNIT: Interacts with ARF1. Interacts with PICALM and clathrin heavy chains. {ECO:0000269|PubMed:16571680}. +O09126 SEM4D_MOUSE Semaphorin-4D (M-Sema G) (Semaphorin-C-like 2) (Semaphorin-J) (Sema J) (CD antigen CD100) 861 95,640 Chain (1); Disulfide bond (8); Domain (3); Glycosylation (8); Modified residue (2); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 734 754 Helical. {ECO:0000255}. TOPO_DOM 24 733 Extracellular. {ECO:0000255}.; TOPO_DOM 755 861 Cytoplasmic. {ECO:0000255}. FUNCTION: Cell surface receptor for PLXN1B and PLXNB2 that plays an important role in cell-cell signaling. Promotes reorganization of the actin cytoskeleton and plays a role in axonal growth cone guidance in the developing central nervous system. Regulates dendrite and axon branching and morphogenesis. Promotes the migration of cerebellar granule cells and of endothelial cells. Plays a role in the immune system; induces B-cells to aggregate and improves their viability (in vitro). Promotes signaling via SRC and PTK2B/PYK2, which then mediates activation of phosphatidylinositol 3-kinase and of the AKT1 signaling cascade. Interaction with PLXNB1 mediates activation of RHOA (By similarity). {ECO:0000250, ECO:0000269|PubMed:17554007}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SUBUNIT: Homodimer. Binds PLXNB1 (By similarity). Interacts with PLXNB2. {ECO:0000250, ECO:0000269|PubMed:17554007}. TISSUE SPECIFICITY: Strongly expressed in lymphoid tissues, especially in the thymus, as well as in the nervous tissues. +P97299 SFRP2_MOUSE Secreted frizzled-related protein 2 (sFRP-2) (Protein SDF5) (Secreted apoptosis-related protein 1) (SARP-1) 295 33,469 Chain (1); Disulfide bond (8); Domain (2); Sequence conflict (2); Signal peptide (1) FUNCTION: Soluble frizzled-related proteins (sFRPS) function as modulators of Wnt signaling through direct interaction with Wnts. They have a role in regulating cell growth and differentiation in specific cell types. SFRP2 may be important for eye retinal development and for myogenesis. SUBCELLULAR LOCATION: Secreted. DOMAIN: The FZ domain is involved in binding with Wnt ligands. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in the eye. Weaker expression in heart and lung. {ECO:0000269|PubMed:9096311}. +Q9D554 SF3A3_MOUSE Splicing factor 3A subunit 3 (SF3a60) (Spliceosome-associated protein 61) (SAP 61) 501 58,842 Chain (1); Compositional bias (1); Modified residue (9); Zinc finger (1) FUNCTION: Subunit of the splicing factor SF3A required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA. May also be involved in the assembly of the 'E' complex (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00130}. SUBUNIT: Identified in the spliceosome C complex. Component of splicing factor SF3A which is composed of three subunits; SF3A3/SAP61, SF3A2/SAP62, SF3A1/SAP114. SF3A associates with the splicing factor SF3B and a 12S RNA unit to form the U2 small nuclear ribonucleoproteins complex (U2 snRNP). Interacts with SF3A1, through its N-terminal region (By similarity). {ECO:0000250}. +Q8BG73 SH3L2_MOUSE SH3 domain-binding glutamic acid-rich-like protein 2 107 12,255 Chain (1); Motif (1) SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +Q8BX32 SLX1_MOUSE Structure-specific endonuclease subunit SLX1 (EC 3.1.-.-) (GIY-YIG domain-containing protein 1) 270 30,656 Alternative sequence (2); Chain (1); Domain (1); Zinc finger (1) FUNCTION: Catalytic subunit of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA. Has a preference for 5'-flap structures, and promotes symmetrical cleavage of static and migrating Holliday junctions (HJs). Resolves HJs by generating two pairs of ligatable, nicked duplex products. {ECO:0000255|HAMAP-Rule:MF_03100}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03100}. SUBUNIT: Forms a heterodimer with SLX4. {ECO:0000255|HAMAP-Rule:MF_03100}. TISSUE SPECIFICITY: Expressed in testis, colon, bone marrow, brain, thymus and to a lesser extent in heart, kidney, skeletal muscle and spleen. {ECO:0000269|PubMed:27010503}. +Q8BJL0 SMAL1_MOUSE SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A-like protein 1 (EC 3.6.4.-) (HepA-related protein) (mharp) (Sucrose nonfermenting protein 2-like 1) 910 100,840 Alternative sequence (6); Beta strand (5); Chain (1); Coiled coil (1); Domain (4); Helix (3); Initiator methionine (1); Modified residue (3); Motif (1); Nucleotide binding (1); Region (1); Sequence conflict (12); Turn (1) FUNCTION: ATP-dependent annealing helicase that binds selectively to fork DNA relative to ssDNA or dsDNA and catalyzes the rewinding of the stably unwound DNA. Rewinds single-stranded DNA bubbles that are stably bound by replication protein A (RPA). Acts throughout the genome to reanneal stably unwound DNA, performing the opposite reaction of many enzymes, such as helicases and polymerases, that unwind DNA. May play an important role in DNA damage response by acting at stalled replication forks (By similarity). {ECO:0000250}. PTM: DNA damage-regulated phosphorylation by kinases that may include ATM, ATR and PRKDC. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Recruited to damaged DNA regions. {ECO:0000250}. SUBUNIT: Interacts with RPA2; the interaction is direct and mediates the recruitment by the RPA complex of SMARCAL1 to sites of DNA damage. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed, with high levels in brain, heart, kidney, liver and testis. {ECO:0000269|PubMed:10857751}. +P0C8K7 SMIM1_MOUSE Small integral membrane protein 1 78 8,764 Chain (1); Modified residue (5); Topological domain (2); Transmembrane (1) TRANSMEM 49 69 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 48 Cytoplasmic. {ECO:0000250|UniProtKB:B2RUZ4}.; TOPO_DOM 70 78 Extracellular. {ECO:0000250|UniProtKB:B2RUZ4}. FUNCTION: Regulator of red blood cell formation. {ECO:0000250|UniProtKB:B3DHH5}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:B2RUZ4}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:B2RUZ4}. SUBUNIT: Homooligomer; disulfide-linked. {ECO:0000250|UniProtKB:B2RUZ4}. +Q8BT42 SMIM5_MOUSE Small integral membrane protein 5 78 8,529 Chain (1); Transmembrane (1) TRANSMEM 32 52 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q8CBY1 SMAG1_MOUSE Protein Smaug homolog 1 (Smaug 1) (mSmaug 1) (Sterile alpha motif domain-containing protein 4A) 711 78,359 Alternative sequence (3); Chain (1); Domain (1); Modified residue (5); Sequence caution (1); Sequence conflict (1) FUNCTION: Acts as a translational repressor of SRE-containing messengers. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16221671}. Cell projection, dendrite {ECO:0000269|PubMed:16221671}. Cell junction, synapse, synaptosome {ECO:0000269|PubMed:16221671}. Note=Colocalizes throughout the cytoplasm in granules with polyadenylated RNAs, PABPC1 and STAU1. Also frequently colocalizes in cytoplasmic stress granule-like foci with ELAVL1, TIA1 and TIAL1. Shuttles between the nucleus and the cytoplasm in a CRM1-dependent manner (By similarity). Enriched in synaptoneurosomes. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain (at protein level). {ECO:0000269|PubMed:16221671}. +Q99KC7 SMAGP_MOUSE Small cell adhesion glycoprotein (Small transmembrane and glycosylated protein) 97 10,696 Chain (1); Glycosylation (6); Topological domain (2); Transmembrane (1) TRANSMEM 37 57 Helical; Signal-anchor for type III membrane protein. {ECO:0000255}. TOPO_DOM 1 36 Extracellular. {ECO:0000255}.; TOPO_DOM 58 97 Cytoplasmic. {ECO:0000255}. FUNCTION: May play a role in epithelial cell-cell contacts. May play a role in tumor invasiveness and metastasis formation (By similarity). {ECO:0000250}. PTM: O-glycosylated. The O-glycan is modified with sialic acid residues (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q0VAQ4}; Single-pass type III membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q0VAQ4}; Single-pass type III membrane protein {ECO:0000255}. Note=Predominantly on lateral parts of the membrane, at cell-cell epithelial junctions. Detected on cytoplasmic membranes in undifferentiated tumors. {ECO:0000250|UniProtKB:Q0VAQ4}. +O35717 SOCS2_MOUSE Suppressor of cytokine signaling 2 (SOCS-2) (Cytokine-inducible SH2 protein 2) (CIS-2) 198 22,434 Chain (1); Domain (2); Modified residue (1) Protein modification; protein ubiquitination. FUNCTION: SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. SOCS2 appears to be a negative regulator in the growth hormone/IGF1 signaling pathway. Probable substrate recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). {ECO:0000250}. SUBUNIT: Associates with the Elongin BC complex. {ECO:0000250}. DOMAIN: The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin ligase complexes. {ECO:0000250}. TISSUE SPECIFICITY: Expressed primarily in the testis, some expression in liver and lung. +Q6NZL0 SOGA3_MOUSE Protein SOGA3 945 103,480 Chain (1); Coiled coil (2); Compositional bias (3); Erroneous initiation (1); Modified residue (2); Sequence conflict (1); Signal peptide (1); Transmembrane (1) TRANSMEM 913 933 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q9D489 SOLH2_MOUSE Spermatogenesis- and oogenesis-specific basic helix-loop-helix-containing protein 2 467 51,325 Chain (1); Domain (1); Sequence conflict (1) FUNCTION: Transcription regulator of both male and female germline differentiation. Suppresses genes involved in spermatogonial stem cells maintenance, and induces genes important for spermatogonial differentiation (PubMed:22056784). Coordinates oocyte differentiation without affecting meiosis I (PubMed:28504655). {ECO:0000269|PubMed:22056784, ECO:0000269|PubMed:28504655}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:16765102, ECO:0000269|PubMed:28504655}. Cytoplasm {ECO:0000269|PubMed:28504655}. Note=Translocates from the cytoplasm into the nucleus and the translocation is dependent on SOHLH1 protein expression. {ECO:0000269|PubMed:28504655}. SUBUNIT: Forms both hetero- and homodimers with SOHLH1. {ECO:0000269|PubMed:22056784}. TISSUE SPECIFICITY: Preferentially expressed in the adult ovary and testis. Expressed in the majority of spermatogonia in adult animals, but not in the most undifferentiated spermatogonial population (PubMed:22056784). {ECO:0000269|PubMed:22056784}. +Q7M710 TR125_MOUSE Taste receptor type 2 member 125 (T2R125) (mT2R59) 311 36,072 Chain (1); Glycosylation (3); Topological domain (8); Transmembrane (7) TRANSMEM 10 32 Helical; Name=1. {ECO:0000255}.; TRANSMEM 48 68 Helical; Name=2. {ECO:0000255}.; TRANSMEM 90 110 Helical; Name=3. {ECO:0000255}.; TRANSMEM 130 150 Helical; Name=4. {ECO:0000255}.; TRANSMEM 187 207 Helical; Name=5. {ECO:0000255}.; TRANSMEM 231 251 Helical; Name=6. {ECO:0000255}.; TRANSMEM 263 283 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 9 Extracellular. {ECO:0000255}.; TOPO_DOM 33 47 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 69 89 Extracellular. {ECO:0000255}.; TOPO_DOM 111 129 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 151 186 Extracellular. {ECO:0000255}.; TOPO_DOM 208 230 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 252 262 Extracellular. {ECO:0000255}.; TOPO_DOM 284 311 Cytoplasmic. {ECO:0000255}. FUNCTION: Putative taste receptor which may play a role in the perception of bitterness. {ECO:0000305}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q7M709 TR129_MOUSE Taste receptor type 2 member 129 (T2R129) (mT2R60) 320 37,178 Chain (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 9 29 Helical; Name=1. {ECO:0000255}.; TRANSMEM 56 76 Helical; Name=2. {ECO:0000255}.; TRANSMEM 89 109 Helical; Name=3. {ECO:0000255}.; TRANSMEM 129 149 Helical; Name=4. {ECO:0000255}.; TRANSMEM 186 206 Helical; Name=5. {ECO:0000255}.; TRANSMEM 234 254 Helical; Name=6. {ECO:0000255}.; TRANSMEM 265 285 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 8 Extracellular. {ECO:0000255}.; TOPO_DOM 30 55 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 77 88 Extracellular. {ECO:0000255}.; TOPO_DOM 110 128 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 150 185 Extracellular. {ECO:0000255}.; TOPO_DOM 207 233 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 255 264 Extracellular. {ECO:0000255}.; TOPO_DOM 286 320 Cytoplasmic. {ECO:0000255}. FUNCTION: Putative taste receptor which may play a role in the perception of bitterness. {ECO:0000305}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9ET35 TR13B_MOUSE Tumor necrosis factor receptor superfamily member 13B (Transmembrane activator and CAML interactor) (CD antigen CD267) 249 26,947 Chain (1); Disulfide bond (6); Repeat (2); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 129 149 Helical; Signal-anchor for type III membrane protein. {ECO:0000255}. TOPO_DOM 1 128 Extracellular. {ECO:0000255}.; TOPO_DOM 150 249 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for TNFSF13/APRIL and TNFSF13B/TALL1/BAFF/BLYS that binds both ligands with similar high affinity. Mediates calcineurin-dependent activation of NF-AT, as well as activation of NF-kappa-B and AP-1. Involved in the stimulation of B- and T-cell function and the regulation of humoral immunity (By similarity). {ECO:0000250, ECO:0000269|PubMed:10880535, ECO:0000269|PubMed:11429548}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type III membrane protein {ECO:0000305}. SUBUNIT: Binds TRAF2, TRAF5 and TRAF6. Binds the NH2-terminal domain of CAMLG with its C-terminus (By similarity). {ECO:0000250}. +Q8BX43 TR19L_MOUSE Tumor necrosis factor receptor superfamily member 19L 436 46,518 Chain (1); Disulfide bond (2); Glycosylation (1); Modified residue (1); Motif (1); Repeat (1); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 170 190 Helical. {ECO:0000255}. TOPO_DOM 32 169 Extracellular. {ECO:0000255}.; TOPO_DOM 191 436 Cytoplasmic. {ECO:0000255}. FUNCTION: May play a role in apoptosis. Induces activation of MAPK14/p38 and MAPK8/JNK MAPK cascades, when overexpressed. {ECO:0000250|UniProtKB:Q969Z4}. PTM: Phosphorylated in vitro by OXSR1. Phosphorylated by STK39. {ECO:0000250|UniProtKB:Q969Z4}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q969Z4}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q969Z4}. Cytoplasm {ECO:0000250|UniProtKB:Q969Z4}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q969Z4}. SUBUNIT: Interacts with RELL1, RELL2, OXSR1, PLSCR1 and STK39. {ECO:0000250|UniProtKB:Q969Z4}. +Q8CGW4 SOX30_MOUSE Transcription factor SOX-30 782 83,938 Chain (1); Compositional bias (3); DNA binding (1) FUNCTION: Transcriptional activator. Binds to the DNA sequence 5'-ACAAT-3' and shows a preference for guanine residues surrounding this core motif (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}. +Q9CXB2 SOAT_MOUSE Solute carrier family 10 member 6 (Sodium-dependent organic anion transporter) 373 40,681 Chain (1); Glycosylation (2); Topological domain (10); Transmembrane (9) TRANSMEM 33 53 Helical. {ECO:0000255}.; TRANSMEM 68 88 Helical. {ECO:0000255}.; TRANSMEM 98 118 Helical. {ECO:0000255}.; TRANSMEM 127 147 Helical. {ECO:0000255}.; TRANSMEM 158 178 Helical. {ECO:0000255}.; TRANSMEM 196 216 Helical. {ECO:0000255}.; TRANSMEM 225 245 Helical. {ECO:0000255}.; TRANSMEM 266 283 Helical. {ECO:0000255}.; TRANSMEM 285 305 Helical. {ECO:0000255}. TOPO_DOM 1 32 Extracellular. {ECO:0000255}.; TOPO_DOM 54 67 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 89 97 Extracellular. {ECO:0000255}.; TOPO_DOM 119 126 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 148 157 Extracellular. {ECO:0000255}.; TOPO_DOM 179 195 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 217 224 Extracellular. {ECO:0000255}.; TOPO_DOM 246 265 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 284 284 Extracellular. {ECO:0000255}.; TOPO_DOM 306 373 Cytoplasmic. {ECO:0000255}. FUNCTION: Transports sulfoconjugated steroid hormones, as well as taurolithocholic acid-3-sulfate and sulfoconjugated pyrenes in a sodium-dependent manner. {ECO:0000250}. PTM: Glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +P53784 SOX3_MOUSE Transcription factor SOX-3 375 37,789 Chain (1); Compositional bias (6); DNA binding (1); Sequence conflict (4) FUNCTION: Transcription factor required during the formation of the hypothalamo-pituitary axis. May function as a switch in neuronal development. Keeps neural cells undifferentiated by counteracting the activity of proneural proteins and suppresses neuronal differentiation. Required also within the pharyngeal epithelia for craniofacial morphogenesis. Controls a genetic switch in male development. Is necessary for initiating male sex determination by directing the development of supporting cell precursors (pre-Sertoli cells) as Sertoli rather than granulosa cells. {ECO:0000269|PubMed:14981518, ECO:0000269|PubMed:17728342, ECO:0000269|PubMed:21183788}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with SOX2 and FGFR1. {ECO:0000269|PubMed:17728342}. TISSUE SPECIFICITY: Mainly in the developing central nervous system. Expressed in developing urogenital ridge. +Q04891 SOX13_MOUSE Transcription factor SOX-13 (SRY (Sex determining region Y)-box 13) (mSox13) 613 68,168 Chain (1); Compositional bias (2); DNA binding (1); Erroneous initiation (2); Modified residue (5); Sequence caution (1); Sequence conflict (3) FUNCTION: Binds to the sequence 5'-AACAAT-3'. {ECO:0000269|PubMed:9421502, ECO:0000269|PubMed:9524265}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267, ECO:0000269|PubMed:9421502}. TISSUE SPECIFICITY: In the embryo, high levels of expression are found in the arterial walls at 13.5 dpc. Low levels are found in the inner ear at 13.5 dpc and in some cells in the thymus at 16.5 dpc. Expressed in the tracheal epithelium below the vocal cord and in the hair follicles at 18 dpc. In adults, expressed in the ovary and kidney. {ECO:0000269|PubMed:9421502, ECO:0000269|PubMed:9524265}. +P86449 TR43C_MOUSE Tripartite motif-containing protein 43C 446 52,533 Chain (1); Domain (1); Zinc finger (2) +Q62252 SP17_MOUSE Sperm surface protein Sp17 (Sperm autoantigenic protein 17) 149 17,296 Chain (1); Domain (1) FUNCTION: Sperm surface zona pellucida binding protein. Helps to bind spermatozoa to the zona pellucida with high affinity. Might function in binding zona pellucida and carbohydrates (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. SUBUNIT: Homodimer. May interact with ROPN1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Testis- and sperm-specific. +O70494 SP3_MOUSE Transcription factor Sp3 783 82,362 Alternative sequence (3); Chain (1); Compositional bias (4); Cross-link (5); Erroneous initiation (2); Modified residue (5); Region (3); Sequence conflict (1); Zinc finger (3) FUNCTION: Transcriptional factor that can act as an activator or repressor depending on isoform and/or post-translational modifications. Binds to GT and GC boxes promoter elements. Competes with SP1 for the GC-box promoters. Weak activator of transcription but can activate a number of genes involved in different processes such as cell-cycle regulation, hormone-induction and house-keeping (By similarity). {ECO:0000250, ECO:0000269|PubMed:15554904}. PTM: Acetylated by histone acetyltransferase p300, deacetylated by HDACs. Acetylation/deacetylation states regulate transcriptional activity. Acetylation appears to activate transcription. Alternate sumoylation and acetylation at Lys-553 also control transcriptional activity (By similarity). {ECO:0000250}.; PTM: Sumoylated on all isoforms. Sumoylated on 2 sites in longer isoforms with Lys-553 being the major site. Sumoylation at this site promotes nuclear localization to the nuclear periphery, nuclear dots and PML nuclear bodies. Sumoylation on Lys-553 represses the transactivation activity, except for the largest isoform which has little effect on transactivation. Alternate sumoylation and acetylation at Lys-553 also control transcriptional activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Nucleus, PML body {ECO:0000250}. Note=Localizes to the nuclear periphery and in nuclear dots when sumoylated. Some localization in PML nuclear bodies (By similarity). {ECO:0000250}. SUBUNIT: Interacts with HLTF; the interaction may be required for basal transcriptional activity of HLTF. Interacts with HDAC1; the interaction deacetylates SP3 and regulates its transcriptional activity. Interacts with HDAC2 (preferably the CK2-phosphorylated form); the interaction deacetylates SP3 and regulates its transcriptional activity. Ceramides can also regulate acetylation/deacetylation events through altering the interaction of HDAC with SP3. Interacts with MEIS2 isoform Meis2D and PBX1 isoform PBX1a (By similarity). {ECO:0000250}. +Q9JHX2 SP5_MOUSE Transcription factor Sp5 398 42,052 Chain (1); Compositional bias (3); Zinc finger (3) FUNCTION: Binds to GC boxes promoters elements. Probable transcriptional activator that has a role in the coordination of changes in transcription required to generate pattern in the developing embryo. SUBCELLULAR LOCATION: Nucleus. +Q8BYY9 SPA3B_MOUSE Serine protease inhibitor A3B (Serpin A3B) 420 47,415 Chain (1); Glycosylation (2); Region (1); Signal peptide (1); Site (1) SUBCELLULAR LOCATION: Secreted {ECO:0000250}. DOMAIN: The reactive center loop (RCL) extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site within the RCL, establishing a covalent linkage between the serpin reactive site and the protease. The resulting inactive serpin-protease complex is highly stable (By similarity). Variability within the reactive center loop (RCL) sequences of Serpina3 paralogs may determine target protease specificity. {ECO:0000250}. +Q64HY3 SP9_MOUSE Transcription factor Sp9 484 48,959 Alternative sequence (1); Chain (1); Compositional bias (5); Modified residue (1); Sequence conflict (1); Zinc finger (3) FUNCTION: Transcription factor which plays a key role in limb development. Positively regulates FGF8 expression in the apical ectodermal ridge (AER) and contributes to limb outgrowth in embryos. {ECO:0000269|PubMed:15358670}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q7TME2 SPAG5_MOUSE Sperm-associated antigen 5 (Mastrin) (Mitotic spindle-associated protein p126) (MAP126) 1165 129,993 Chain (1); Coiled coil (2); Modified residue (8); Region (1); Sequence conflict (9) FUNCTION: Essential component of the mitotic spindle required for normal chromosome segregation and progression into anaphase. Required for chromosome alignment, normal timing of sister chromatid segregation, and maintenance of spindle pole architecture. In complex with SKAP, promotes stable microtubule-kinetochore attachments. May contribute to the regulation of separase activity. May regulate AURKA localization to mitotic spindle, but not to centrosomes and CCNB1 localization to both mitotic spindle and centrosomes. Involved in centriole duplication. Required for CDK5RAP22, CEP152, WDR62 and CEP63 centrosomal localization and promotes the centrosomal localization of CDK2. In non-mitotic cells, upon stress induction, inhibits mammalian target of rapamycin complex 1 (mTORC1) association and recruits the mTORC1 component RPTOR to stress granules (SGs), thereby preventing mTORC1 hyperactivation-induced apoptosis. May enhance GSK3B-mediated phosphorylation of other substrates, such as MAPT/TAU (By similarity). {ECO:0000250|UniProtKB:Q96R06}. PTM: Phosphorylated by AURKA. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96R06}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q96R06}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q96R06}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q96R06}. Midbody {ECO:0000250|UniProtKB:Q96R06}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q96R06}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000250|UniProtKB:Q96R06}. Note=Colocalizes with PCM1 at centriolar satellites throughout the cell cycle (By similarity). In a punctate pattern in interphase cells. During mitosis, detected at spindle poles during prophase, throughout the spindle in metaphase and anaphase, and at midzone microtubules in anaphase and telophase. Efficient targeting to the mitotic spindle may depend upon phosphorylation by GSK3B. Detected on kinetochores of chromosomes that have congressed. The astrin (SPAG5)-kinastrin (SKAP) complex localizes to the microtubule plus ends (By similarity). In non-mitotic non-stressed cells, shows a microtubuli pattern. During oxidative stress, accumulates in stress granules (By similarity). {ECO:0000250|UniProtKB:Q96R06}. SUBUNIT: Homodimer, with a globular head domain and a long stalk. Homooligomer; the globular head domains associate, resulting in aster-like structures. Binds to microtubules in the mitotic spindle. Interacts with DCLRE1B/Apollo. Part of an astrin (SPAG5)-kinastrin (SKAP) complex containing KNSTRN, SPAG5, PLK1, DYNLL1 and SGO2. Interacts with KNSTRN. Interacts with RPTOR; this interaction competes with RPTOR binding to MTOR, resulting in decreased mTORC1 formation. Interacts with G3BP1. The complex formed with G3BP1 AND RPTOR is increased by oxidative stress. Interacts with OSBPL8, PCM1 and CDK5RAP2. Interacts (via C-terminus) with NUMA1 (via C-terminus); this interaction promotes the recruitment of SPAG5 to the microtubules at spindle poles in a dynein-dynactin-dependent manner. {ECO:0000250|UniProtKB:Q96R06}. TISSUE SPECIFICITY: Detected in testis, but not in the other tissues tested. {ECO:0000269|PubMed:12893248}. +Q03734 SPA3M_MOUSE Serine protease inhibitor A3M (Serpin A3M) 418 47,064 Chain (1); Glycosylation (3); Region (1); Sequence conflict (24); Signal peptide (1); Site (1) SUBCELLULAR LOCATION: Secreted {ECO:0000250}. DOMAIN: The reactive center loop (RCL) extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site within the RCL, establishing a covalent linkage between the serpin reactive site and the protease. The resulting inactive serpin-protease complex is highly stable (By similarity). Variability within the reactive center loop (RCL) sequences of Serpina3 paralogs may determine target protease specificity. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in liver and testis. {ECO:0000269|PubMed:15638460}. +Q9JLI7 SPAG6_MOUSE Sperm-associated antigen 6 (Axoneme central apparatus protein) (Protein PF16 homolog) 507 55,269 Chain (1); Repeat (8) FUNCTION: Important for structural integrity of the central apparatus in the sperm tail and for flagellar motility. {ECO:0000269|PubMed:10684790, ECO:0000269|PubMed:12167721}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10684790}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:10684790}. Note=Associated with microtubules. Detected on the sperm flagellum. SUBUNIT: Interacts with SPAG16 AND SPAG17. {ECO:0000269|PubMed:12391165, ECO:0000269|PubMed:15827353}. TISSUE SPECIFICITY: Highly expressed in testis. Not detected in prostate, ovary, spleen, thymus, small intestine, colon and peripheral blood leukocytes. {ECO:0000269|PubMed:10684790, ECO:0000269|PubMed:12391165}. DISEASE: Note=Defects in Spag6 are a cause of hydrocephalus and of male infertility. {ECO:0000269|PubMed:12167721}. +Q3V0Q6 SPAG8_MOUSE Sperm-associated antigen 8 (Sperm membrane protein 1) (SMP-1) (Sperm membrane protein BS-84) 470 50,541 Alternative sequence (2); Chain (1); Sequence conflict (2) FUNCTION: Plays a role in spermatogenesis by enhancing the binding of CREM isoform tau to its coactivator FHL5 and increasing the FHL5-regulated transcriptional activation of CREM isoform tau (PubMed:20488182). Involved in the acrosome reaction and in binding of sperm to the zona pellucida (PubMed:17187156). Plays a role in regulation of the cell cycle by controlling progression through the G2/M phase, possibly by delaying the activation of CDK1 which is required for entry into mitosis (By similarity). May play a role in fertility and microtubule formation through interaction with RANBP9 (By similarity). {ECO:0000250|UniProtKB:Q99932, ECO:0000269|PubMed:17187156, ECO:0000269|PubMed:20488182}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20488182}. Nucleus {ECO:0000269|PubMed:20488182}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:17187156, ECO:0000269|PubMed:20488182}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000250|UniProtKB:Q99932}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q99932}. Note=In mature sperm cells, detected in the acrosomal region of the head and in the middle piece of the tail (PubMed:20488182). Localized to the nucleus and cytoplasm of spermatocytes and round spermatids while, in elongating spermatids, expressed in the cytoplasm but not in the nucleus (PubMed:20488182). During the cell cycle, localized on the microtubule-organizing center (MTOC) during prophase. In metaphase, extends along spindle microtubules. In anaphase, detected on the astral microtubules and mid-zone. In telophase, remains at the mid-zone. After cytokinesis, returns to the MTOC (By similarity). {ECO:0000250|UniProtKB:Q99932, ECO:0000269|PubMed:20488182}. SUBUNIT: Interacts with FHL5 (via second LIM domain) (PubMed:20488182). Interacts with RANBP9 (By similarity). {ECO:0000250|UniProtKB:Q99932, ECO:0000269|PubMed:20488182}. TISSUE SPECIFICITY: Expressed in testis (at protein level). Not detected in brain, heart, kidney, spleen, liver, lung, thymus and colon (at protein level). {ECO:0000269|PubMed:20488182}. +B2RV46 SPA6L_MOUSE Spermatogenesis associated 6-like protein 347 39,981 Chain (1); Modified residue (2) +Q9D7D2 SPA9_MOUSE Serpin A9 418 46,894 Chain (1); Glycosylation (3); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q9D2S4 SPAC7_MOUSE Sperm acrosome-associated protein 7 182 19,943 Chain (1); Glycosylation (1); Signal peptide (1) FUNCTION: Involved in fertilization. Seems not to play a direct role in sperm-egg binding or gamete fusion. {ECO:0000269|PubMed:24307706}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22495889}. Cytoplasmic vesicle, secretory vesicle, acrosome lumen {ECO:0000269|PubMed:22495889, ECO:0000269|PubMed:24307706}. Note=Localized in perinuclear pro-acrosomal granules in round spermatides (PubMed:24307706). Localized between the inner and outer acrosomal membranes (matrix or lumen) in spermatozoa (PubMed:24307706). Secreted during acrosome exocytosis (PubMed:24307706). {ECO:0000269|PubMed:24307706}. TISSUE SPECIFICITY: Testis-specific (PubMed:22495889, PubMed:24307706). Expressed in zygotene and pachytene spermatocytes, round spermatids, elongating spermatids and spermatozoa (at protein level) (PubMed:22495889, PubMed:24307706). Testis-specific (PubMed:22495889). {ECO:0000269|PubMed:22495889, ECO:0000269|PubMed:24307706}. +Q8R1X6 SPART_MOUSE Spartin 671 72,655 Alternative sequence (1); Chain (1); Compositional bias (1); Cross-link (1); Domain (2); Erroneous initiation (2); Modified residue (3); Sequence conflict (4) FUNCTION: May be implicated in endosomal trafficking, or microtubule dynamics, or both. Participates in cytokinesis. {ECO:0000250|UniProtKB:Q8N0X7}. PTM: Ubiquitinated; ubiquitination does not require ITCH and WWP1. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8N0X7}. Midbody {ECO:0000250|UniProtKB:Q8N0X7}. Note=Transiently associated with endosomes. Colocalized with IST1 to the ends of Flemming bodies during cytokinesis. {ECO:0000250|UniProtKB:Q8N0X7}. SUBUNIT: Interacts with ITCH and WWP1. Interacts (via MIT domain) with IST1; leading to the recruitment of SPART to midbodies. {ECO:0000250|UniProtKB:Q8N0X7}. +Q8K1N4 SPAS2_MOUSE Spermatogenesis-associated serine-rich protein 2 (Serine-rich spermatocytes and round spermatid 59 kDa protein) (p59scr) 545 58,956 Alternative sequence (2); Chain (1); Compositional bias (2); Erroneous initiation (1); Modified residue (4) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11944913}. TISSUE SPECIFICITY: Detected in testis, in spermatocytes and round spermatids (at protein level). Highly expressed in testis, and detected at lower levels in brain, heart, thymus, skeletal muscle, ovary, stomach and lung. {ECO:0000269|PubMed:11944913}. +Q9D5R4 SPAT1_MOUSE Spermatogenesis-associated protein 1 444 51,077 Alternative sequence (2); Chain (1); Coiled coil (1) +Q8K004 SPAT2_MOUSE Spermatogenesis-associated protein 2 515 57,812 Alternative sequence (2); Chain (1); Domain (1); Motif (1); Sequence conflict (1) FUNCTION: Bridging factor that mediates the recruitment of CYLD to the LUBAC complex, thereby regulating TNF-alpha-induced necroptosis (By similarity). Acts as a direct binding intermediate that bridges RNF31/HOIP, the catalytic subunit of the LUBAC complex, and the deubiquitinase (CYLD), thereby recruiting CYLD to the TNF-R1 signaling complex (TNF-RSC) (By similarity). Required to activate the 'Met-1'- (linear) and 'Lys-63'-linked deubiquitinase activities of CYLD (PubMed:28701375). Controls the kinase activity of RIPK1 and TNF-alpha-induced necroptosis by promoting 'Met-1'-linked deubiquitination of RIPK1 by CYLD (PubMed:28701375). {ECO:0000250|UniProtKB:Q9UM82, ECO:0000269|PubMed:28701375}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29025062}. Nucleus {ECO:0000250|UniProtKB:Q66HP6}. SUBUNIT: Interacts (via the PIM motif) with RNF31/HOIP (via the PUB domain); the interaction is direct. Interacts (via the PUB domain) with CYLD; the interaction is direct. {ECO:0000250|UniProtKB:Q9UM82}. TISSUE SPECIFICITY: Widely expressed, with highest expression in testis, lung and intestine, and lower expression in brain, heart and spleen (PubMed:28701375). Present at high level in Sertoli cells: expressed from stage I to stage XII of the testis seminiferous epithelium (at protein level) (PubMed:29025062). {ECO:0000269|PubMed:28701375, ECO:0000269|PubMed:29025062}. +Q3U6K5 SPAT6_MOUSE Spermatogenesis-associated protein 6 (Kinesin-related protein) 488 56,101 Alternative sequence (3); Chain (1); Cross-link (1); Erroneous initiation (1); Modified residue (11); Sequence conflict (5); Signal peptide (1) FUNCTION: Required for formation of the sperm connecting piece during spermiogenesis. Sperm connecting piece is essential for linking the developing flagellum to the head during late spermiogenesis (PubMed:12771232, PubMed:25605924). May be involved in myosin-based microfilament transport through interaction with myosin subunits (PubMed:25605924). {ECO:0000269|PubMed:12771232, ECO:0000269|PubMed:25605924}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:25605924}. Note=Specifically localizes to the segmented columns and the capitulum of the sperm connecting piece. {ECO:0000269|PubMed:25605924}. SUBUNIT: Interacts with MYL6. {ECO:0000269|PubMed:25605924}. TISSUE SPECIFICITY: Specifically expressed in developing spermatids and mature spermatozoa (at protein level) (PubMed:25605924). Isoform 1 is weakly expressed in testis, ovary, thymus and placenta. Isoform 2 and isoform 3 are testis-specific. Expression isw higher in spermatids than in spermatocytes and spermatogonia (PubMed:12771232). {ECO:0000269|PubMed:12771232, ECO:0000269|PubMed:25605924}. +Q922B6 TRAF7_MOUSE E3 ubiquitin-protein ligase TRAF7 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase TRAF7) (TNF receptor-associated factor 7) 594 66,487 Chain (1); Modified residue (2); Repeat (7); Zinc finger (2) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin ligase capable of auto-ubiquitination, following phosphorylation by MAP3K3. Potentiates MEKK3-mediated activation of the NF-kappa-B, JUN/AP1 and DDIT3 transcriptional regulators. Induces apoptosis when overexpressed. {ECO:0000250|UniProtKB:Q6Q0C0}. PTM: Phosphorylated by MAP3K3. {ECO:0000250|UniProtKB:Q6Q0C0}.; PTM: Ubiquitinates itself upon phosphorylation. {ECO:0000250|UniProtKB:Q6Q0C0}. SUBCELLULAR LOCATION: Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q6Q0C0}. Note=Colocalizes with MAP3K3 to vesicle-like structures throughout the cytoplasm. {ECO:0000250|UniProtKB:Q6Q0C0}. SUBUNIT: Homodimer. Interacts with MAP3K3 and promotes the kinase activity of this enzyme. {ECO:0000250|UniProtKB:Q6Q0C0}. +Q8CDC0 SPB13_MOUSE Serpin B13 389 44,316 Alternative sequence (1); Chain (1); Sequence conflict (1); Site (1) FUNCTION: May play a role in the proliferation or differentiation of keratinocytes. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +Q3UU67 TRAT1_MOUSE T-cell receptor-associated transmembrane adapter 1 (T-cell receptor-interacting molecule) (TRIM) 187 21,330 Alternative sequence (3); Chain (1); Disulfide bond (1); Erroneous initiation (1); Modified residue (2); Region (1); Topological domain (2); Transmembrane (1) TRANSMEM 8 28 Helical; Signal-anchor for type III membrane protein. {ECO:0000255}. TOPO_DOM 1 7 Extracellular. {ECO:0000255}.; TOPO_DOM 29 187 Cytoplasmic. {ECO:0000255}. FUNCTION: Stabilizes the TCR (T-cell antigen receptor)/CD3 complex at the surface of T-cells. {ECO:0000250}. PTM: Phosphorylated on tyrosines upon TCR activation. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. SUBUNIT: Homodimer; disulfide-linked. Interacts with CD3Z. When phosphorylated, interacts with PIK3R1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Present in T-cells (at protein level). {ECO:0000269|PubMed:11439161}. +O89032 SPD2A_MOUSE SH3 and PX domain-containing protein 2A (Five SH3 domain-containing protein) (SH3 multiple domains protein 1) (Tyrosine kinase substrate with five SH3 domains) 1124 124,201 Alternative sequence (2); Chain (1); Coiled coil (1); Compositional bias (1); Domain (6); Frameshift (2); Modified residue (16); Sequence conflict (1) FUNCTION: Adapter protein involved in invadopodia and podosome formation, extracellular matrix degradation and invasiveness of some cancer cells. Binds matrix metalloproteinases (ADAMs), NADPH oxidases (NOXs) and phosphoinositides. Acts as an organizer protein that allows NOX1- or NOX3-dependent reactive oxygen species (ROS) generation and ROS localization. In association with ADAM12, mediates the neurotoxic effect of amyloid-beta peptide (By similarity). {ECO:0000250, ECO:0000269|PubMed:18417249, ECO:0000269|PubMed:19755709}. PTM: Tyrosine phosphorylated by SRC. Phosphorylation plays a regulatory role in the protein localization. The intramolecular interaction of the PX domain with the third SH3 domain maintains the protein in the cytoplasm and phosphorylation disrupts this interaction, resulting in the redistribution of the protein from cytoplasm to the perimembrane region. Phosphorylated on serine upon DNA damage, probably by ATM or ATR (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Cell projection, podosome {ECO:0000250}. Note=Cytoplasmic in normal cells and localizes to podosomes in Src-transformed cells. {ECO:0000250}. SUBUNIT: Interacts with ADAM12, ADAM15 and ADAM19 (By similarity). Interacts with NOXO1 (By similarity). Interacts (via SH3 domains) with NOXA1; the interaction is direct (By similarity). Interacts (via N-terminus) with CYBA. Interacts with FASLG (By similarity). {ECO:0000250}. DOMAIN: The PX domain is required for podosome localization because of its ability to bind phosphatidylinositol 3-phosphate (PtdIns(3)P) and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) and, to a lesser extent, phosphatidylinositol 4-phosphate (PtdIns(4)P), phosphatidylinositol 5-phosphate (PtdIns(5)P), and phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Binds to the third intramolecular SH3 domain (By similarity). {ECO:0000250}.; DOMAIN: The fifth SH3 domain mediates binding with ADAM12, ADAM15 and ADAM19. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. Not found in the spleen and testis. {ECO:0000269|PubMed:9687503}. +A2AAY5 SPD2B_MOUSE SH3 and PX domain-containing protein 2B (Factor for adipocyte differentiation 49) (Tyrosine kinase substrate with four SH3 domains) 908 101,517 Chain (1); Compositional bias (1); Domain (5); Frameshift (1); Modified residue (7); Mutagenesis (3); Sequence conflict (6) FUNCTION: Adapter protein involved in invadopodia and podosome formation and extracellular matrix degradation. Binds matrix metalloproteinases (ADAMs), NADPH oxidases (NOXs) and phosphoinositides. Acts as an organizer protein that allows NOX1- or NOX3-dependent reactive oxygen species (ROS) generation and ROS localization. Plays a role in mitotic clonal expansion during the immediate early stage of adipocyte differentiation. {ECO:0000269|PubMed:18959745, ECO:0000269|PubMed:19144821, ECO:0000269|PubMed:19755710}. PTM: Phosphorylated in SRC-transformed cells. {ECO:0000269|PubMed:19144821}. SUBCELLULAR LOCATION: Cytoplasm. Cell projection, podosome. Note=Cytoplasmic in normal cells and localizes to podosomes in SRC-transformed cells. SUBUNIT: Interacts with NOXO1 (By similarity). Interacts (via SH3 domains) with NOXA1; the interaction is direct (By similarity). Interacts with ADAM15. Interacts with FASLG (By similarity). {ECO:0000250}. DOMAIN: The PX domain is required for podosome localization because of its ability to bind phosphatidylinositol 3-phosphate (PtdIns(3)P) and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) and, to a lesser extent, phosphatidylinositol 4-phosphate (PtdIns(4)P), phosphatidylinositol 5-phosphate (PtdIns(5)P), and phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Binds to the third intramolecular SH3 domain (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in the stromal-vascular fraction of white adipose tissue with moderate expression in heart, skeletal muscle and the mature adipocyte fraction of white adipose tissue. Also expressed in brain, spleen, kidney and liver. Expressed in white and brown adipose tissues, eye, lung, heart, brain, spleen, stomach, liver and skeletal muscle (at protein level). Not expressed in kidney or bone marrow. {ECO:0000269|PubMed:18959745, ECO:0000269|PubMed:19144821, ECO:0000269|PubMed:19669234}. +Q9JLT2 TREA_MOUSE Trehalase (EC 3.2.1.28) (Alpha,alpha-trehalase) (Alpha,alpha-trehalose glucohydrolase) 576 65,401 Active site (2); Binding site (4); Chain (1); Glycosylation (3); Lipidation (1); Propeptide (1); Region (3); Sequence conflict (2); Signal peptide (1) FUNCTION: Intestinal trehalase is probably involved in the hydrolysis of ingested trehalose. {ECO:0000250|UniProtKB:O43280}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P19813}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P19813}. SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250|UniProtKB:P19813}. +Q8BGQ1 SPE39_MOUSE Spermatogenesis-defective protein 39 homolog (hSPE-39) (VPS33B-interacting protein in apical-basolateral polarity regulator) (VPS33B-interacting protein in polarity and apical restriction) 491 56,625 Alternative sequence (1); Chain (1); Modified residue (6); Sequence conflict (2) FUNCTION: Proposed to be involved in endosomal maturation implicating in part VPS33B. In epithelial cells, the VPS33B:VIPAS39 complex may play a role in the apical RAB11A-dependent recycling pathway and in the maintenance of the apical-basolateral polarity (PubMed:20190753). May play a role in lysosomal trafficking, probably via association with the core HOPS complex in a discrete population of endosomes; the functions seems to be indepenedent of VPS33B (By similarity). May play a role in vesicular trafficking during spermatogenesis (By similarity). May be involved in direct or indirect transcriptional regulation of E-cadherin. {ECO:0000250|UniProtKB:Q23288, ECO:0000250|UniProtKB:Q9H9C1, ECO:0000269|PubMed:20190753}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Early endosome {ECO:0000250|UniProtKB:Q9H9C1}. Recycling endosome {ECO:0000250|UniProtKB:Q9H9C1}. Late endosome {ECO:0000250|UniProtKB:Q9H9C1}. Note=Colocalizes in clusters with VPS33B at cytoplasmic organelles. {ECO:0000250|UniProtKB:Q9H9C1}. SUBUNIT: Interacts with VPS33B. Associates with the homotypic fusion and vacuole protein sorting (HOPS) complex; impaired by VPS33B (By similarity). Interacts with RAB11A (PubMed:20190753). {ECO:0000250|UniProtKB:Q9H9C1, ECO:0000269|PubMed:20190753}. +Q5IBH6 SPE4A_MOUSE Speedy protein E4A (Rapid inducer of G2/M progression in oocytes E4A) (RINGO E4A) (mSpy/Ringo E4A) 268 30,977 Chain (1); Region (1) FUNCTION: Promotes progression through the cell cycle via binding and activation of CDK1. {ECO:0000269|PubMed:15611625}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5MJ70}. SUBUNIT: Interacts with CDK1. Does not interact with CDK2 in vivo. {ECO:0000269|PubMed:15611625}. TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:15611625}. +A2AS89 SPEB_MOUSE Agmatinase, mitochondrial (EC 3.5.3.11) (Agmatine ureohydrolase) (AUH) 358 38,255 Chain (1); Metal binding (3); Modified residue (3); Sequence conflict (1); Transit peptide (1) Amine and polyamine biosynthesis; putrescine biosynthesis via agmatine pathway; putrescine from agmatine: step 1/1. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. TISSUE SPECIFICITY: Detected only in liver. {ECO:0000269|PubMed:11914032}. +Q9D7K2 TEN1L_MOUSE CST complex subunit TEN1 (Protein telomeric pathways with STN1 homolog) (Telomere length regulation protein TEN1 homolog) 161 18,066 Chain (1); DNA binding (1) FUNCTION: Component of the CST complex proposed to act as a specialized replication factor promoting DNA replication under conditions of replication stress or natural replication barriers such as the telomere duplex. The CST complex binds single-stranded DNA with high affinity in a sequence-independent manner, while isolated subunits bind DNA with low affinity by themselves. Initially the CST complex has been proposed to protect telomeres from DNA degradation (PubMed:19854130). However, the CST complex has been shown to be involved in several aspects of telomere replication. The CST complex inhibits telomerase and is involved in telomere length homeostasis; it is proposed to bind to newly telomerase-synthesized 3' overhangs and to terminate telomerase action implicating the association with the ACD:POT1 complex thus interfering with its telomerase stimulation activity. The CST complex is also proposed to be involved in fill-in synthesis of the telomeric C-strand probably implicating recruitment and activation of DNA polymerase alpha. The CST complex facilitates recovery from many forms of exogenous DNA damage; seems to be involved in the re-initiation of DNA replication at repaired forks and/or dormant origins (By similarity). {ECO:0000250|UniProtKB:Q86WV5, ECO:0000269|PubMed:19854130}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19854130}. Chromosome, telomere {ECO:0000269|PubMed:19854130}. SUBUNIT: Component of the CST complex, composed of TEN1, CTC1 and STN1; in the complex interacts directly with STN1. {ECO:0000269|PubMed:19854130}. +Q8BTH6 SCRT2_MOUSE Transcriptional repressor scratch 2 (Scratch homolog 2 zinc finger protein) 311 32,722 Chain (1); Region (1); Zinc finger (5) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q8K2B3 SDHA_MOUSE Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial (EC 1.3.5.1) (Flavoprotein subunit of complex II) (Fp) 664 72,585 Active site (1); Binding site (6); Chain (1); Modified residue (29); Nucleotide binding (3); Sequence conflict (6); Transit peptide (1) Carbohydrate metabolism; tricarboxylic acid cycle; fumarate from succinate (eukaryal route): step 1/1. FUNCTION: Flavoprotein (FP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). Can act as a tumor suppressor. {ECO:0000250|UniProtKB:P31040}. PTM: Acetylation of Lys-498 and Lys-538 is observed in liver mitochondria from fasted mice but not from fed mice. Deacetylated by SIRT3. {ECO:0000269|PubMed:21858060}.; PTM: Phosphorylation at Tyr-215 is important for efficient electron transfer in complex II and the prevention of ROS generation. {ECO:0000250|UniProtKB:P31040}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q0QF01}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q0QF01}; Matrix side {ECO:0000250|UniProtKB:Q0QF01}. SUBUNIT: Component of complex II composed of four subunits: the flavoprotein (FP) SDHA, iron-sulfur protein (IP) SDHB, and a cytochrome b560 composed of SDHC and SDHD (By similarity). Interacts with SDHAF2/SDH5; interaction is required for FAD attachment (By similarity). Interacts with TRAP1 (By similarity). {ECO:0000250|UniProtKB:P31040, ECO:0000250|UniProtKB:Q0QF01}. +Q8C6I2 SDHF2_MOUSE Succinate dehydrogenase assembly factor 2, mitochondrial (SDH assembly factor 2) (SDHAF2) 164 19,431 Alternative sequence (2); Chain (1); Sequence conflict (1); Transit peptide (1) FUNCTION: Plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Required for flavinylation (covalent attachment of FAD) of the flavoprotein subunit SDHA of the SDH catalytic dimer. {ECO:0000255|HAMAP-Rule:MF_03057}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-Rule:MF_03057}. SUBUNIT: Interacts with SDHA within the SDH catalytic dimer. {ECO:0000255|HAMAP-Rule:MF_03057}. +Q8VHE0 SEC63_MOUSE Translocation protein SEC63 homolog 760 87,870 Chain (1); Coiled coil (1); Compositional bias (1); Domain (3); Modified residue (3); Sequence conflict (3); Topological domain (4); Transmembrane (3) TRANSMEM 15 35 Helical. {ECO:0000255}.; TRANSMEM 70 90 Helical. {ECO:0000255}.; TRANSMEM 189 209 Helical. {ECO:0000255}. TOPO_DOM 1 14 Lumenal. {ECO:0000255}.; TOPO_DOM 36 69 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 91 188 Lumenal. {ECO:0000255}.; TOPO_DOM 210 760 Cytoplasmic. {ECO:0000255}. FUNCTION: Mediates cotranslational and post-translational transport of certain precursor polypeptides across endoplasmic reticulum (ER) (PubMed:22375059). Proposed to play an auxiliary role in recognition of precursors with short and apolar signal peptides. May cooperate with SEC62 and HSPA5/BiP to facilitate targeting of small presecretory proteins into the SEC61 channel-forming translocon complex, triggering channel opening for polypeptide translocation to the ER lumen (By similarity). Required for efficient PKD1/Polycystin-1 biogenesis and trafficking to the plasma membrane of the primary cilia (PubMed:21685914). {ECO:0000250|UniProtKB:Q9UGP8, ECO:0000269|PubMed:21685914, ECO:0000269|PubMed:22375059}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SUBUNIT: The ER translocon complex consists of channel-forming core components SEC61A1, SEC61B and SEC61G and different auxiliary components such as SEC62 and SEC63. {ECO:0000250|UniProtKB:P82008}. TISSUE SPECIFICITY: Expressed in kidney (at protein level). {ECO:0000269|PubMed:21685914}. +Q3UQA7 SELH_MOUSE Selenoprotein H (SelH) 116 12,974 Chain (1); Cross-link (1); Modified residue (1); Non-standard residue (1) FUNCTION: May be involved in a redox-related process. {ECO:0000305}. +P60897 SEM1_MOUSE 26S proteasome complex subunit SEM1 (26S proteasome complex subunit DSS1) (Deleted in split hand/split foot protein 1 homolog) (Split hand/foot deleted protein 1 homolog) (Split hand/foot malformation type 1 protein homolog) 70 8,278 Chain (1); Compositional bias (3) FUNCTION: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. Component of the TREX-2 complex (transcription and export complex 2), composed of at least ENY2, GANP, PCID2, SEM1, and either centrin CETN2 or CETN3. The TREX-2 complex functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket). TREX-2 participates in mRNA export and accurate chromatin positioning in the nucleus by tethering genes to the nuclear periphery. Binds and stabilizes BRCA2 and is thus involved in the control of R-loop-associated DNA damage and thus transcription-associated genomic instability. R-loop accumulation increases in SEM1-depleted cells. {ECO:0000250|UniProtKB:P60896}. SUBUNIT: Component of the 19S proteasome regulatory particle complex. The 26S proteasome consists of a 20S core particle (CP) and two 19S regulatory subunits (RP). The regulatory particle is made of a lid composed of 9 subunits including SEM1, a base containing 6 ATPases and few additional components. Belongs to the TREX-2 complex (transcription and export complex 2), composed of at least ENY2, GANP, PCID2, SEM1, and either centrin CETN2 or CETN3. Interacts with the C-terminal of BRCA2. {ECO:0000250|UniProtKB:P60896}. +Q62170 SELPL_MOUSE P-selectin glycoprotein ligand 1 (PSGL-1) (Selectin P ligand) (CD antigen CD162) 397 41,842 Beta strand (1); Chain (1); Disulfide bond (1); Glycosylation (3); Modified residue (3); Mutagenesis (6); Propeptide (1); Region (1); Repeat (10); Sequence conflict (6); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 308 328 Helical. {ECO:0000255}. TOPO_DOM 18 307 Extracellular. {ECO:0000255}.; TOPO_DOM 329 397 Cytoplasmic. {ECO:0000255}. FUNCTION: A SLe(x)-type proteoglycan, which through high affinity, calcium-dependent interactions with E- and P-selectins, mediates rapid rolling of leukocytes over vascular surfaces during the initial steps in inflammation. Critical for the initial leukocyte capture. {ECO:0000269|PubMed:11104809, ECO:0000269|PubMed:12370362, ECO:0000269|PubMed:17442598}. PTM: Displays complex, core-2, sialylated and fucosylated O-linked oligosaccharides, at least some of which appear to contain poly-N-acetyllactosamine with varying degrees of substitution. Mainly disialylated or neutral forms of the core-2 tetrasaccharide, Galbeta1-->4GlcNAcbeta1-->6(Galbeta1-->3)GalNAcOH. The GlcN:GalN ratio is approximately 2:1 and the Man:Fuc ratio 3:5. Contains about 14% fucose with alpha-1,3 linkage present in two forms: One species is a disialylated, monofucosylated glycan, and the other, a monosialylated, trifucosylated glycan with a polylactosamine backbone. The fucosylated forms carry the Lewis antigen and are important for interaction with selectins and for functioning. No sulfated O-glycans. Some N-glycosylation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. SUBUNIT: Homodimer; disulfide-linked. Interacts with P- and E-selectins, through their lectin/EGF domains. Interaction with P-selectin requires sialyl Lewis X glycan modification and tyrosine sulfation, probably on Tyr-54, for high affinity binding (By similarity). Dimerization appears not to be required for P-selectin/SELP binding (By similarity). Interacts with SNX20 (By similarity). Interacts with MSN and SYK; mediates SYK activation downstream of SELPLG (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in blood, bone marrow, brain, adipose tissue, spleen, and thymus. Also expressed in heart, kidney, liver, muscle, ovary, and stomach. {ECO:0000269|PubMed:8639776}. +Q62177 SEM3B_MOUSE Semaphorin-3B (Semaphorin-A) (Sema A) 748 82,700 Chain (1); Compositional bias (2); Disulfide bond (6); Domain (2); Glycosylation (2); Sequence conflict (10); Signal peptide (1) FUNCTION: Inhibits axonal extension by providing local signals to specify territories inaccessible for growing axons. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +Q9DA97 SEP14_MOUSE Septin-14 430 49,811 Binding site (3); Chain (1); Coiled coil (1); Domain (1); Nucleotide binding (2); Region (3); Sequence caution (1); Sequence conflict (1) FUNCTION: Filament-forming cytoskeletal GTPase (By similarity). May play a role in cytokinesis (Potential). {ECO:0000250, ECO:0000305}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Colocalizes with actin stress fibers. {ECO:0000250}. SUBUNIT: Septins polymerize into heterooligomeric protein complexes that form filaments, and can associate with cellular membranes, actin filaments and microtubules. GTPase activity is required for filament formation. Interacts with SEPT9 (By similarity). {ECO:0000250}. +Q62181 SEM3C_MOUSE Semaphorin-3C (Semaphorin-E) (Sema E) 751 85,289 Chain (1); Compositional bias (2); Disulfide bond (6); Domain (2); Glycosylation (7); Sequence conflict (4); Signal peptide (1) FUNCTION: Binds to plexin family members and plays an important role in the regulation of developmental processes. Required for normal cardiovascular development during embryogenesis. Functions as attractant for growing axons, and thereby plays an important role in axon growth and axon guidance. {ECO:0000269|PubMed:11688556, ECO:0000269|PubMed:15239958, ECO:0000269|PubMed:17021275}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Interacts with PLXND1. {ECO:0000269|PubMed:15239958}. +P97321 SEPR_MOUSE Prolyl endopeptidase FAP (EC 3.4.21.26) (Dipeptidyl peptidase FAP) (EC 3.4.14.5) (Fibroblast activation protein alpha) (FAPalpha) (Gelatine degradation protease FAP) (EC 3.4.21.-) (Integral membrane serine protease) (Post-proline cleaving enzyme) (Serine integral membrane protease) (SIMP) (Surface-expressed protease) (Seprase) [Cleaved into: Antiplasmin-cleaving enzyme FAP, soluble form (APCE) (EC 3.4.14.5) (EC 3.4.21.-) (EC 3.4.21.26)] 761 87,945 Active site (3); Alternative sequence (2); Binding site (2); Chain (2); Disulfide bond (4); Glycosylation (6); Mutagenesis (1); Sequence conflict (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 5 25 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 4 Cytoplasmic. {ECO:0000250|UniProtKB:Q12884, ECO:0000255}.; TOPO_DOM 26 761 Extracellular. {ECO:0000250|UniProtKB:Q12884, ECO:0000255}. FUNCTION: Cell surface glycoprotein serine protease that participates in extracellular matrix degradation and involved in many cellular processes including tissue remodeling, fibrosis, wound healing, inflammation and tumor growth. Both plasma membrane and soluble forms exhibit post-proline cleaving endopeptidase activity, with a marked preference for Ala/Ser-Gly-Pro-Ser/Asn/Ala consensus sequences, on substrate such as alpha-2-antiplasmin SERPINF2 and SPRY2. Degrade also gelatin, heat-denatured type I collagen, but not native collagen type I and IV, vibronectin, tenascin, laminin, fibronectin, fibrin or casein. Have also dipeptidyl peptidase activity, exhibiting the ability to hydrolyze the prolyl bond two residues from the N-terminus of synthetic dipeptide substrates provided that the penultimate residue is proline, with a preference for Ala-Pro, Ile-Pro, Gly-Pro, Arg-Pro and Pro-Pro. Natural neuropeptide hormones for dipeptidyl peptidase are the neuropeptide Y (NPY), peptide YY (PYY), substance P (TAC1) and brain natriuretic peptide 32 (NPPB). The plasma membrane form, in association with either DPP4, PLAUR or integrins, is involved in the pericellular proteolysis of the extracellular matrix (ECM), and hence promotes cell adhesion, migration and invasion through the ECM. Plays a role in tissue remodeling during development and wound healing. Participates in the cell invasiveness towards the ECM in malignant melanoma cancers. Enhances tumor growth progression by increasing angiogenesis, collagen fiber degradation and apoptosis and by reducing antitumor response of the immune system. Promotes glioma cell invasion through the brain parenchyma by degrading the proteoglycan brevican. Acts as a tumor suppressor in melanocytic cells through regulation of cell proliferation and survival in a serine protease activity-independent manner. {ECO:0000269|PubMed:10629066, ECO:0000269|PubMed:11330865, ECO:0000269|PubMed:15133496, ECO:0000269|PubMed:21051638, ECO:0000269|PubMed:23710635, ECO:0000269|PubMed:24371721, ECO:0000269|PubMed:9688278}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q12884}.; PTM: The N-terminus may be blocked. {ECO:0000250|UniProtKB:Q12884}. SUBCELLULAR LOCATION: Prolyl endopeptidase FAP: Cell surface {ECO:0000269|PubMed:15133496}. Cell membrane {ECO:0000250|UniProtKB:Q12884}; Single-pass type II membrane protein {ECO:0000255}. Cell projection, lamellipodium membrane {ECO:0000250|UniProtKB:Q12884}; Single-pass type II membrane protein {ECO:0000255}. Cell projection, invadopodium membrane {ECO:0000250|UniProtKB:Q12884}; Single-pass type II membrane protein {ECO:0000255}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q12884}; Single-pass type II membrane protein {ECO:0000255}. Membrane {ECO:0000250|UniProtKB:Q12884}; Single-pass type II membrane protein {ECO:0000255}. Note=Localized on cell surface with lamellipodia and invadopodia membranes and on shed vesicles. Colocalized with DPP4 at invadopodia and lamellipodia membranes of migratory activated endothelial cells in collagenous matrix. Colocalized with DPP4 on endothelial cells of capillary-like microvessels but not large vessels within invasive breast ductal carcinoma. Anchored and enriched preferentially by integrin alpha-3/beta-1 at invadopodia, plasma membrane protrusions that correspond to sites of cell invasion, in a collagen-dependent manner. Localized at plasma and ruffle membranes in a collagen-independent manner. Colocalized with PLAUR preferentially at the cell surface of invadopodia membranes in a cytoskeleton-, integrin- and vitronectin-dependent manner. Concentrated at invadopodia membranes, specialized protrusions of the ventral plasma membrane in a fibrobectin-dependent manner. Colocalizes with extracellular components (ECM), such as collagen fibers and fibronectin. {ECO:0000250|UniProtKB:Q12884}.; SUBCELLULAR LOCATION: Antiplasmin-cleaving enzyme FAP, soluble form: Secreted {ECO:0000269|PubMed:24371721}. Note=Found in blood plasma and serum. {ECO:0000269|PubMed:24371721}. SUBUNIT: Homodimer; homodimerization is required for activity of both plasma membrane and soluble forms. The monomer is inactive. Heterodimer with DPP4. Interacts with PLAUR; the interaction occurs at the cell surface of invadopodia membranes. Interacts with ITGB1. Interacts with ITGA3. Associates with integrin alpha-3/beta-1; the association occurs in a collagen-dependent manner at the cell surface of invadopodia membranes. {ECO:0000250|UniProtKB:Q12884}. TISSUE SPECIFICITY: Expressed strongly in uterus, pancreas, submaxillary gland and skin, less in lymph node, ovary, skeletal muscle, adrenal and bone marrow. Expressed in reactive stromal fibroblast in epithelial cancers. Expressed in melanocytes but not melanomas (at protein level). Detected in fibroblasts, in placenta, uterus, embryos from day 7-19 and in newborn mice (P1). {ECO:0000269|PubMed:15133496, ECO:0000269|PubMed:21051638, ECO:0000269|PubMed:24371721}. +P42209 SEPT1_MOUSE Septin-1 (Differentiation protein 6) (Protein Diff6) (Peanut-like protein 3) 366 42,020 Binding site (4); Chain (1); Domain (1); Frameshift (1); Modified residue (5); Nucleotide binding (2); Region (3); Sequence conflict (1) FUNCTION: Filament-forming cytoskeletal GTPase (By similarity). May play a role in cytokinesis (Potential). {ECO:0000250, ECO:0000305}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Midbody {ECO:0000250}. Note=Remains at the centrosomes and the nearby microtubules throughout mitosis. Localizes to the midbody during cytokinesis (By similarity). {ECO:0000250}. SUBUNIT: Septins polymerize into heterooligomeric protein complexes that form filaments, and can associate with cellular membranes, actin filaments and microtubules. GTPase activity is required for filament formation (By similarity). Interacts with AURKB (By similarity). {ECO:0000250}. +Q61753 SERA_MOUSE D-3-phosphoglycerate dehydrogenase (3-PGDH) (EC 1.1.1.95) (A10) 533 56,586 Active site (3); Binding site (4); Chain (1); Cross-link (2); Initiator methionine (1); Modified residue (5); Nucleotide binding (3); Sequence conflict (6) Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 1/3. FUNCTION: Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L-serine biosynthesis pathway. Does not catalyze the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate and the reversible oxidation of (S)-malate to oxaloacetate. {ECO:0000250|UniProtKB:O08651}. SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:O08651}. +Q8BHJ6 SERC5_MOUSE Serine incorporator 5 (Axotomy-induced glycoprotein 3) (AIGP-3) 461 51,831 Chain (1); Compositional bias (2); Glycosylation (2); Sequence conflict (1); Topological domain (11); Transmembrane (10) TRANSMEM 37 57 Helical. {ECO:0000255}.; TRANSMEM 91 111 Helical. {ECO:0000255}.; TRANSMEM 126 146 Helical. {ECO:0000255}.; TRANSMEM 158 178 Helical. {ECO:0000255}.; TRANSMEM 201 221 Helical. {ECO:0000255}.; TRANSMEM 232 252 Helical. {ECO:0000255}.; TRANSMEM 261 281 Helical. {ECO:0000255}.; TRANSMEM 313 333 Helical. {ECO:0000255}.; TRANSMEM 393 413 Helical. {ECO:0000255}.; TRANSMEM 423 443 Helical. {ECO:0000255}. TOPO_DOM 1 36 Extracellular. {ECO:0000255}.; TOPO_DOM 58 90 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 112 125 Extracellular. {ECO:0000255}.; TOPO_DOM 147 157 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 179 200 Extracellular. {ECO:0000255}.; TOPO_DOM 222 231 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 253 260 Extracellular. {ECO:0000255}.; TOPO_DOM 282 312 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 334 392 Extracellular. {ECO:0000255}.; TOPO_DOM 414 422 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 444 461 Extracellular. {ECO:0000255}. FUNCTION: Restriction factor required to restrict infectivity of gammaretroviruses: acts by inhibiting early step of viral infection and impairing the ability of the viral particle to translocate its content to the cytoplasm (By similarity). Enhances the incorporation of serine into phosphatidylserine and sphingolipids. May play a role in providing serine molecules for the formation of myelin glycosphingolipids in oligodendrocytes (By similarity). {ECO:0000250|UniProtKB:Q63175, ECO:0000250|UniProtKB:Q86VE9}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q86VE9}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to the cell membrane, where it is efficiently incorporated into budding gammaretrovirus virions and impairs subsequent virion penetration of susceptible target cells. {ECO:0000250|UniProtKB:Q86VE9}. +Q8CHH9 SEPT8_MOUSE Septin-8 429 49,812 Alternative sequence (1); Binding site (3); Chain (1); Coiled coil (1); Domain (1); Erroneous initiation (1); Frameshift (1); Initiator methionine (1); Modified residue (2); Nucleotide binding (2); Region (3); Sequence conflict (1) FUNCTION: Filament-forming cytoskeletal GTPase (By similarity). May play a role in platelet secretion (By similarity). Seems to participate in the process of SNARE complex formation in synaptic vesicles (By similarity). {ECO:0000250|UniProtKB:B0BNF1, ECO:0000250|UniProtKB:Q92599}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:B0BNF1}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell junction, synapse {ECO:0000250|UniProtKB:B0BNF1}. Cell projection, axon {ECO:0000250|UniProtKB:B0BNF1}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:B0BNF1}. Note=Expressed in axons of immature neurons, localizes to synapses in mature neurons. Mainly localized in the presynases. {ECO:0000250|UniProtKB:B0BNF1}. SUBUNIT: Septins polymerize into heterooligomeric protein complexes that form filaments, and can associate with cellular membranes, actin filaments and microtubules. GTPase activity is required for filament formation (By similarity). Interacts with SEPT5 (PubMed:12909369). Interacts with CDK14, SEPT4 and SEPT7 (By similarity). InteracSts with VAMP2; the interaction inhibits interaction of VAMP2 with SYP (PubMed:19196426). Interacts with STX1A (By similarity). {ECO:0000250|UniProtKB:B0BNF1, ECO:0000250|UniProtKB:Q92599, ECO:0000269|PubMed:12909369, ECO:0000269|PubMed:19196426}. +P58467 SETD4_MOUSE SET domain-containing protein 4 (EC 2.1.1.-) 439 49,837 Chain (1); Compositional bias (1); Domain (1) +P59708 SF3B6_MOUSE Splicing factor 3B subunit 6 (Pre-mRNA branch site protein p14) (SF3b 14 kDa subunit) 125 14,585 Chain (1); Cross-link (1); Domain (1); Modified residue (2); Region (1) FUNCTION: Involved in pre-mRNA splicing as a component of the splicing factor SF3B complex. SF3B complex is required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Directly contacts the pre-mRNA branch site adenosine for the first catalytic step of splicing. Enters the spliceosome and associates with the pre-mRNA branch site as part of the 17S U2 or, in the case of the minor spliceosome, as part of the 18S U11/U12 snRNP complex, and thus may facilitate the interaction of these snRNP with the branch sites of U2 and U12 respectively. {ECO:0000250|UniProtKB:Q9Y3B4}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y3B4}. SUBUNIT: Component of splicing factor SF3B complex which is composed of at least eight subunits; SF3B1, SF3B2, SF3B3, SF3B4, SF3B5, SF3B6, PHF5A and DDX42. Within the SF3B complex interacts directly with SF3B1. The SF3B complex composed of SF3B1, SF3B2, SF3B3, SF3B4, SF3B5, SF3B6 and PHF5A interacts with U2AF2. Component of the U11/U12 snRNPs that are part of the U12-type spliceosome. {ECO:0000250|UniProtKB:Q9Y3B4}. +Q7TSK2 SEZ6_MOUSE Seizure protein 6 (SEZ-6) (Brain-specific receptor-like protein C) (BSRP-C) 991 107,433 Alternative sequence (4); Chain (1); Compositional bias (2); Disulfide bond (13); Domain (8); Erroneous initiation (1); Glycosylation (4); Sequence conflict (15); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 923 943 Helical. {ECO:0000255}. TOPO_DOM 20 922 Extracellular. {ECO:0000255}.; TOPO_DOM 944 991 Cytoplasmic. {ECO:0000255}. FUNCTION: May play a role in cell-cell recognition and in neuronal membrane signaling. Seems to be important for the achievement of the necessary balance between dendrite elongation and branching during the elaboration of a complex dendritic arbor. Involved in the development of appropriate excitatory synaptic connectivity. {ECO:0000269|PubMed:18031681}. PTM: Glycosylated. {ECO:0000269|PubMed:7488116}. SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I membrane protein. Cell projection, dendrite. Note=Localized on dendrites and in the postsynaptic fraction. Does not appear to be enriched at synapses, at least not in the presynaptic axon terminal.; SUBCELLULAR LOCATION: Isoform 2: Cell membrane; Single-pass type I membrane protein. Cell junction, synapse. Cell projection, dendrite. Note=Localized on dendrites and in the synaptic and postsynaptic fraction.; SUBCELLULAR LOCATION: Isoform 3: Secreted {ECO:0000305}. Cytoplasm. TISSUE SPECIFICITY: Brain-specific. Expressed in extrasynaptic and synaptic subcellular fractions (at protein level). Expression correlates with the most active periods of cortical neurogenesis and neuronal maturation. Expression is restricted to the gray matter with higher levels in the forebrain including the olfactory bulb, anterior olfactory nuclei, olfactory tubercle, striatum, hippocampal CA1 pyramidal cell layer and cerebral cortex. Expression is up-regulated with the convulsant drug, pentylenetetrazole. {ECO:0000269|PubMed:16814779, ECO:0000269|PubMed:7488116, ECO:0000269|PubMed:7723619}. +Q8C4U3 SFRP1_MOUSE Secreted frizzled-related protein 1 (sFRP-1) 314 35,413 Chain (1); Disulfide bond (8); Domain (2); Glycosylation (1); Sequence conflict (2); Signal peptide (1) FUNCTION: Soluble frizzled-related proteins (sFRPS) function as modulators of Wnt signaling through direct interaction with Wnts. They have a role in regulating cell growth and differentiation in specific cell types. SFRP1 decreases intracellular beta-catenin levels (By similarity). Has antiproliferative effects on vascular cells, in vitro and in vivo, and can induce, in vivo, an angiogenic response. In vascular cell cycle, delays the G1 phase and entry into the S phase. In kidney development, inhibits tubule formation and bud growth in metanephroi (By similarity). Inhibits WNT1/WNT4-mediated TCF-dependent transcription (By similarity). {ECO:0000250, ECO:0000269|PubMed:15306229}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Cell membrane or extracellular matrix-associated. Released by heparin-binding (By similarity). {ECO:0000250}. SUBUNIT: Interacts with WNT8, WNT1, WNT2, WNT4 and FRZD6 (By similarity). Interacts with MYOC. {ECO:0000250, ECO:0000269|PubMed:10640709, ECO:0000269|PubMed:19188438}. DOMAIN: The FZ domain is involved in binding with Wnt ligands. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in kidney and embryonic heart. Also highly expressed in the eye, where it is principally localized to the ciliary body and the lens epithelium. Weaker expression in heart, lung and brain. In the brain, is expressed exclusively in the choroid plexus. {ECO:0000269|PubMed:9096311}. +Q9D1Y9 SHL2B_MOUSE Protein shisa-like-2B 158 17,448 Chain (1); Transmembrane (1) TRANSMEM 65 85 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q9QUK6 TLR4_MOUSE Toll-like receptor 4 (CD antigen CD284) 835 95,519 Beta strand (35); Chain (1); Disulfide bond (5); Domain (2); Glycosylation (14); Helix (15); Natural variant (14); Repeat (19); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (13) TRANSMEM 639 659 Helical. {ECO:0000255}. TOPO_DOM 26 638 Extracellular. {ECO:0000255}.; TOPO_DOM 660 835 Cytoplasmic. {ECO:0000255}. FUNCTION: Cooperates with LY96 and CD14 to mediate the innate immune response to bacterial lipopolysaccharide (LPS) (PubMed:9851930, PubMed:9989976, PubMed:20133493). Acts via MYD88, TIRAP and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (PubMed:24380872). Also involved in LPS-independent inflammatory responses triggered by free fatty acids, such as palmitate. In complex with TLR6, promotes sterile inflammation in monocytes/macrophages in response to oxidized low-density lipoprotein (oxLDL) or amyloid-beta 42. In this context, the initial signal is provided by oxLDL- or amyloid-beta 42-binding to CD36. This event induces the formation of a heterodimer of TLR4 and TLR6, which is rapidly internalized and triggers inflammatory response, leading to the NF-kappa-B-dependent production of CXCL1, CXCL2 and CCL9 cytokines, via MYD88 signaling pathway, and CCL5 cytokine, via TICAM1 signaling pathway, as well as IL1B secretion. Binds electronegative LDL (LDL(-)) and mediates the cytokine release induced by LDL(-) (By similarity). {ECO:0000250|UniProtKB:O00206, ECO:0000269|PubMed:10952994, ECO:0000269|PubMed:17478729, ECO:0000269|PubMed:20037584, ECO:0000269|PubMed:20133493, ECO:0000269|PubMed:23812099, ECO:0000269|PubMed:24380872, ECO:0000269|PubMed:9851930, ECO:0000269|PubMed:9989976}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20133493}; Single-pass type I membrane protein {ECO:0000269|PubMed:20133493}. Early endosome {ECO:0000250|UniProtKB:O00206}. Note=Upon complex formation with CD36 and TLR6, internalized through dynamin-dependent endocytosis. Colocalizes with RFTN1 at cell membrane and then together with RFTN1 moves to endosomes, upon lipopolysaccharide stimulation. {ECO:0000250|UniProtKB:O00206}. SUBUNIT: Belongs to the lipopolysaccharide (LPS) receptor, a multi-protein complex containing at least CD14, LY96 and TLR4 (PubMed:24380872). Binding to bacterial LPS leads to homodimerization (PubMed:20133493, PubMed:24380872, PubMed:22532668). Interacts with LY96 via the extracellular domain (PubMed:17803912, PubMed:22532668). Interacts with MYD88 (via the TIR domain). Interacts with TICAM2 and TIRAP (PubMed:24380872). Interacts with NOX4 (By similarity). Interacts with CNPY3 and HSP90B1; this interaction is required for proper folding in the endoplasmic reticulum (PubMed:18780723, PubMed:20865800). Interacts with MAP3K21; this interaction leads to negative regulation of TLR4 signaling (By similarity). Interacts with CD36, following CD36 stimulation by oxLDL or amyloid-beta 42, and forms a heterodimer with TLR6. The trimeric complex is internalized and triggers inflammatory response. LYN kinase activity facilitates TLR4-TLR6 heterodimerization and signal initiation (By similarity). Interacts with TICAM1 in response to LPS in a WDFY1-dependent manner (PubMed:25736436). Interacts with WDFY1 in response to LPS (PubMed:25736436). Interacts with SMPDL3B (PubMed:26095358). Interacts with CEACAM1; upon lipopolysaccharide stimulation, forms a complex including TLR4 and the phosphorylated form of SYK and CEACAM1, which in turn, recruits PTPN6 that dephosphorylates SYK, reducing the production of reactive oxygen species (ROS) and lysosome disruption, which in turn, reduces the activity of the inflammasome (PubMed:22496641). Interacts with RFTN1; the interaction occurs in response to lipopolysaccharide stimulation (By similarity). {ECO:0000250|UniProtKB:O00206, ECO:0000269|PubMed:17803912, ECO:0000269|PubMed:18780723, ECO:0000269|PubMed:20133493, ECO:0000269|PubMed:20865800, ECO:0000269|PubMed:22496641, ECO:0000269|PubMed:22532668, ECO:0000269|PubMed:24380872, ECO:0000269|PubMed:25736436, ECO:0000269|PubMed:26095358}. DOMAIN: The TIR domain mediates interaction with NOX4. {ECO:0000250|UniProtKB:O00206}. TISSUE SPECIFICITY: Highly expressed in heart, spleen, lung and muscle. Lower levels are found in liver and kidney. Expressed in macrophages. {ECO:0000269|PubMed:23812099}. DISEASE: Note=The protein is encoded by the Lps locus, an important susceptibility locus, influencing the propensity to develop a disseminated Gram-negative infection. {ECO:0000269|PubMed:9851930, ECO:0000269|PubMed:9989976}. +Q9JK48 SHLB1_MOUSE Endophilin-B1 (SH3 domain-containing GRB2-like protein B1) 365 40,855 Alternative sequence (2); Beta strand (5); Chain (1); Coiled coil (1); Domain (2); Erroneous initiation (1); Helix (1); Modified residue (2); Region (2); Sequence conflict (1) FUNCTION: May be required for normal outer mitochondrial membrane dynamics. Required for coatomer-mediated retrograde transport in certain cells (PubMed:17086176). May recruit other proteins to membranes with high curvature. May promote membrane fusion (By similarity). Involved in activation of caspase-dependent apoptosis by promoting BAX/BAK1 activation (PubMed:16227588). Isoform 1 acts proapoptotic in fibroblasts (PubMed:24523556). Involved in caspase-independent apoptosis during nutrition starvation and involved in the regulation of autophagy. Activates lipid kinase activity of PIK3C3 during autophagy probably by associating with the PI3K complex II (PI3KC3-C2). Associated with PI3KC3-C2 during autophagy may regulate the trafficking of ATG9A from the Golgi complex to the peripheral cytoplasm for the formation of autophagosomes by inducing Golgi membrane tubulation and fragmentation. Involved in regulation of degradative endocytic trafficking and cytokinesis, probably in the context of PI3KC3-C2 (By similarity). Isoform 2 acts antiapoptotic in neuronal cells; involved in maintenance of mitochondrial morphology and promotes neuronal viability (PubMed:24523556). {ECO:0000250|UniProtKB:Q9Y371, ECO:0000269|PubMed:17086176, ECO:0000269|PubMed:24523556}. PTM: Phosphorylated at Thr-145 by CDK5; this phosphorylation is required for autophagy induction in starved neurons and facilitates homodimerization. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17381077}. Golgi apparatus membrane {ECO:0000269|PubMed:17086176}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q6AYE2}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q9Y371}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9Y371}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:Q9Y371}. Midbody {ECO:0000250|UniProtKB:Q9Y371}. Note=Association with the Golgi apparatus depends on the cell type. Following starvation colocalizes with ATG5 and LC3 autophagy-related protein(s)on autophagosomal membranes. {ECO:0000250|UniProtKB:Q9Y371}. SUBUNIT: Homodimer, and heterodimer with SH3GLB2 (By similarity). Binds BAX; induction of apoptosis augments BAX binding (PubMed:16227588, PubMed:17381077). Binds DNM1, HTT, AMPH, BIN1 and ARFGAP1 (PubMed:12456676, PubMed:17086176). Interacts with UVRAG; UVRAG bridges the interaction to BECN1 indicative for an association with the PI3K complex II (PI3KC3-C2) (By similarity). Isoform 3 interacts with PPP1CC; this interaction leads to the inhibition of phosphatase activity (PubMed:17381077). {ECO:0000250|UniProtKB:Q9Y371, ECO:0000269|PubMed:12456676, ECO:0000269|PubMed:16227588, ECO:0000269|PubMed:17086176, ECO:0000269|PubMed:17381077}. DOMAIN: An N-terminal amphipathic helix, the BAR domain and a second amphipathic helix inserted into helix 1 of the BAR domain (N-BAR domain) induce membrane curvature and bind curved membranes. {ECO:0000250}.; DOMAIN: The SH3 domain is required and sufficient for the interaction with UVRAG. {ECO:0000250|UniProtKB:Q9Y371}. TISSUE SPECIFICITY: Isoform 1 is widely expressed. Isoform 2 is brain-specific. Isoform 3 is predominantly expressed in testis, but it is also detected in liver and, at much lower levels, in skin, stomach and ovary. {ECO:0000269|PubMed:17381077}. +P60041 SMS_MOUSE Somatostatin [Cleaved into: Antrin; Somatostatin-28; Somatostatin-14] 116 12,746 Disulfide bond (1); Peptide (3); Propeptide (1); Signal peptide (1) FUNCTION: Somatostatin inhibits the release of somatotropin. SUBCELLULAR LOCATION: Secreted. +Q8C0V7 SMKW_MOUSE Putative sperm motility kinase W (EC 2.7.11.1) 499 55,407 Active site (1); Binding site (1); Chain (1); Domain (2); Nucleotide binding (1); Sequence conflict (1) FUNCTION: May play a role in sperm motility, especially in the regulation of flagellar function. {ECO:0000250}. +Q9CXL7 SNORC_MOUSE Protein SNORC (Secondary ossification center-associated regulator of chondrocyte maturation protein) 121 12,175 Chain (1); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 93 113 Helical. {ECO:0000255}. TOPO_DOM 25 92 Extracellular. {ECO:0000305}.; TOPO_DOM 114 121 Cytoplasmic. {ECO:0000305}. FUNCTION: Plays a role in the regulation of chondrocyte maturation and postnatal endochondral ossification. May inhibit cell growth stimulation induced by FGF2. {ECO:0000269|PubMed:28323137}. SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:28323137}; Single-pass membrane protein {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:21624478}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:21624478, ECO:0000269|PubMed:28323137}. Note=Appears as reticular-like structures throughout the cytoplasm and adjacent to the plasma membrane (PubMed:21624478). In proliferation and hypertrophic chondrocytes, detected intracellulary and in the pericellular extracellular matrix. In primary spongiosa, detected only in the extracellular matrix (PubMed:28323137). {ECO:0000269|PubMed:21624478, ECO:0000269|PubMed:28323137}. SUBUNIT: Interacts (via the extracellular domain) with FGF2. {ECO:0000269|PubMed:28323137}. TISSUE SPECIFICITY: Expressed only in cartilage, including nasal, knee epiphyseal and rib tissues (PubMed:21624478). In proliferation and hypertrophic chondrocytes, detected intracellulary and in the pericellular extracellular matrix. In primary spongiosa, detected only in the extracellular matrix (PubMed:28323137). {ECO:0000269|PubMed:21624478, ECO:0000269|PubMed:28323137}. +Q9DB90 SMG9_MOUSE Protein SMG9 520 57,621 Alternative sequence (1); Chain (1); Compositional bias (1); Initiator methionine (1); Modified residue (7); Sequence conflict (1) FUNCTION: Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. Is recruited by release factors to stalled ribosomes together with SMG1 and SMG8 (forming the SMG1C protein kinase complex) and, in the SMG1C complex, is required for the efficient association between SMG1 and SMG8 (By similarity). Plays a role in brain, heart, and eye development (PubMed:27018474). {ECO:0000250|UniProtKB:Q9H0W8, ECO:0000269|PubMed:27018474}. PTM: Phosphorylated by SMG1. {ECO:0000250|UniProtKB:Q9H0W8}. SUBUNIT: Component of the SMG1C complex composed of SMG1, SMG8 and SMG9. Self-associates to form homodimers and forms heterodimers with SMG8; these assembly forms may represent SMG1C intermediate forms (By similarity). {ECO:0000250|UniProtKB:Q9H0W8}. +Q9CWT3 SNX10_MOUSE Sorting nexin-10 201 23,542 Binding site (3); Chain (1); Domain (1); Region (1); Sequence conflict (1) FUNCTION: Probable phosphoinositide-binding protein involved in protein sorting and membrane trafficking in endosomes. Plays a role in cilium biogenesis through regulation of the transport and the localization of proteins to the cilium. Required for the localization to the cilium of V-ATPase subunit ATP6V1D and ATP6V0D1, and RAB8A. Involved in osteoclast differentiation and therefore bone resorption. {ECO:0000269|PubMed:22174188}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22174188}. Endosome membrane {ECO:0000269|PubMed:22174188}; Peripheral membrane protein {ECO:0000269|PubMed:22174188}; Cytoplasmic side {ECO:0000269|PubMed:22174188}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Note=May also localize to nucleus and endoplasmic reticulum. SUBUNIT: Interacts with ATP6V1D; may play a role in ciliogenesis. {ECO:0000250}. DOMAIN: The PX domain mediates interaction with membranes enriched in phosphatidylinositol 3-phosphate. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in femur, calvariae and teeth. {ECO:0000269|PubMed:22174188}. +Q9D8U8 SNX5_MOUSE Sorting nexin-5 404 46,797 Beta strand (4); Chain (1); Domain (2); Helix (6); Initiator methionine (1); Modified residue (3); Region (5); Turn (3) FUNCTION: Involved in several stages of intracellular trafficking. Interacts with membranes containing phosphatidylinositol lipids. Acts in part as component of the retromer membrane-deforming SNX-BAR subcomplex. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX-BAR subcomplex functions to deform the donor membrane into a tubular profile called endosome-to-TGN transport carrier (ETC). Does not have in vitro vesicle-to-membrane remodeling activity. Involved in retrograde transport of lysosomal enzyme receptor IGF2R. May function as link between endosomal transport vesicles and dynactin. Plays a role in the internalization of EGFR after EGF stimulation. Involved in EGFR endosomal sorting and degradation; the function involves PIP5K1C and is retromer-independent. Together with PIP5K1C facilitates HGS interaction with ubiquitinated EGFR, which initiates EGFR sorting to intraluminal vesicles (ILVs) of the multivesicular body for subsequent lysosomal degradation. Involved in E-cadherin sorting and degradation; inhibits PIP5K1C-mediated E-cadherin degradation (By similarity). Plays a role in macropinocytosis (PubMed:18854019). {ECO:0000250|UniProtKB:Q9Y5X3, ECO:0000269|PubMed:18854019}. SUBCELLULAR LOCATION: Endosome {ECO:0000250|UniProtKB:Q9Y5X3}. Early endosome {ECO:0000250|UniProtKB:Q9Y5X3}. Early endosome membrane {ECO:0000250|UniProtKB:Q9Y5X3}; Peripheral membrane protein; Cytoplasmic side. Cell membrane {ECO:0000250|UniProtKB:Q9Y5X3}; Peripheral membrane protein; Cytoplasmic side {ECO:0000250|UniProtKB:Q9Y5X3}. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm. Cell projection, phagocytic cup. Cell projection, ruffle. Note=Recruited to the plasma membrane after EGF stimulation, which leads to increased levels of phosphatidylinositol 3,4-bisphosphate (PdtIns(3,4)P2) (By similarity). Detected on macropinosomes (PubMed:18854019). Targeted to membrane ruffles in response to EGFR stimulation (By similarity). {ECO:0000250|UniProtKB:Q9Y5X3, ECO:0000269|PubMed:18854019}. SUBUNIT: Forms heterodimers with BAR domain-containing sorting nexins SNX1 and SNX2; does not homodimerize. The heterodimers are proposed to self-assemble into helical arrays on the membrane to stabilize and expand local membrane curvature underlying endosomal tubule formation. Thought to be a component of the originally described retromer complex (also called SNX-BAR retromer) which is a pentamer containing the heterotrimeric retromer cargo-selective complex (CSC), also descibed as vacuolar protein sorting subcomplex (VPS), and a heterodimeric membrane-deforming subcomplex formed between SNX1 or SNX2 and SNX5 or SNX6 (also called SNX-BAR subcomplex); the respective CSC and SNX-BAR subcomplexes associate with low affinity. Interacts with SNX1, SNX2, VPS26A, VPS29, VPS35, DCTN1, DOCK1, MIB1, PIP5K1C. Interacts with HGS; increased by PIP5K1C kinase activity and by PtdIns(3P) and/or PtdIns(3,4)P2 (By similarity). {ECO:0000250|UniProtKB:Q9Y5X3}. DOMAIN: The PX domain mediates interaction with membranes enriched in phosphatidylinositol 3,4-bisphosphate and/or phosphatidylinositol 4,5-bisphosphate. {ECO:0000250}.; DOMAIN: The BAR domain is able to sense membrane curvature upon dimerization. Membrane remodeling seems to implicate insertion of an amphipatric helix (AH) in the membrane (By similarity). {ECO:0000250|UniProtKB:Q9Y5X3}. TISSUE SPECIFICITY: Detected in macrophages (at protein level). {ECO:0000269|PubMed:18854019}. +Q6IUP1 SOLH1_MOUSE Spermatogenesis- and oogenesis-specific basic helix-loop-helix-containing protein 1 357 38,188 Chain (1); Domain (1) FUNCTION: Transcription regulator of both male and female germline differentiation. Suppresses genes involved in spermatogonial stem cells maintenance, and induces genes important for spermatogonial differentiation (PubMed:22056784). Coordinates oocyte differentiation without affecting meiosis I (PubMed:28504655). {ECO:0000269|PubMed:22056784, ECO:0000269|PubMed:28504655}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16690745, ECO:0000269|PubMed:28504655}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:16690745, ECO:0000269|PubMed:28504655}. SUBUNIT: Forms both hetero- and homodimers with SOHLH2. {ECO:0000269|PubMed:22056784}. TISSUE SPECIFICITY: In males, it is mainly expressed in testis, while in females it is mainly expressed in ovary. In testis, it is exclusively expressed in spermatogonia, with a preference for prespermatogonia and type A spermatogonia. In ovary, it is detected in germ cell cysts, primordial follicles, and primary follicles but is undetectable by the secondary follicle stage (at protein level). Expressed in the majority of spermatogonia in adult animals, but not in the most undifferentiated spermatogonial population (PubMed:22056784). {ECO:0000269|PubMed:16564520, ECO:0000269|PubMed:16690745, ECO:0000269|PubMed:22056784}. +Q8VHQ2 SOCS7_MOUSE Suppressor of cytokine signaling 7 (SOCS-7) 579 62,784 Chain (1); Compositional bias (8); Domain (2); Region (1) Protein modification; protein ubiquitination. FUNCTION: Regulates signaling cascades probably through protein ubiquitination and/or sequestration. Functions in insulin signaling and glucose homeostasis through IRS1 ubiquitination and subsequent proteasomal degradation. Inhibits also prolactin, growth hormone and leptin signaling by preventing STAT3 and STAT5 activation, sequestering them in the cytoplasm and reducing their binding to DNA. May be a substrate recognition component of a SCF-like E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). {ECO:0000250, ECO:0000269|PubMed:15494444, ECO:0000269|PubMed:16127460}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15242778}. Cell membrane {ECO:0000269|PubMed:15242778}; Peripheral membrane protein {ECO:0000269|PubMed:15242778}; Cytoplasmic side {ECO:0000269|PubMed:15242778}. Nucleus {ECO:0000269|PubMed:15242778}. Note=Mostly cytoplasmic, but shuttles between the cytoplasm and the nucleus. Rapidly relocalizes to the nucleus after UV irradiation. Cytoplasmic location depends upon SEPT7 presence (By similarity). {ECO:0000250}. SUBUNIT: Interacts with phosphorylated IRS4 and PIK3R1. Interacts, via the third proline-rich region, with the second SH3 domain of the adapter protein NCK1. Also interacts with GRB2, INSR, IRS1, PLCG1, SORBS3/vinexin and phosphorylated STAT3 and STAT5 (By similarity). Interacts with SEPT6 (By similarity). {ECO:0000250}. DOMAIN: The SOCS box domain is required for IRS1 ubiquitination and subsequent proteasomal degradation. {ECO:0000250}.; DOMAIN: The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin ligase complexes. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed with higher expression in brain and testis where it is expressed by spermatocytes and early spermatids. Also significantly expressed in spleen, skeletal muscle and kidney. {ECO:0000269|PubMed:12052866, ECO:0000269|PubMed:15494444, ECO:0000269|PubMed:16127460}. +P59110 SENP1_MOUSE Sentrin-specific protease 1 (EC 3.4.22.-) (SUMO-1 protease 2) (SuPr-2) (Sentrin/SUMO-specific protease SENP1) 640 72,511 Active site (3); Chain (1); Compositional bias (2); Modified residue (3); Motif (4); Region (2); Sequence conflict (1) FUNCTION: Protease that catalyzes two essential functions in the SUMO pathway (PubMed:15923632, PubMed:29499132). The first is the hydrolysis of an alpha-linked peptide bond at the C-terminal end of the small ubiquitin-like modifier (SUMO) propeptides, SUMO1, SUMO2 and SUMO3 leading to the mature form of the proteins. The second is the deconjugation of SUMO1, SUMO2 and SUMO3 from targeted proteins, by cleaving an epsilon-linked peptide bond between the C-terminal glycine of the mature SUMO and the lysine epsilon-amino group of the target protein. Deconjugates SUMO1 from HIPK2 (By similarity). Deconjugates SUMO1 from HDAC1 and BHLHE40/DEC1, which decreases its transcriptional repression activity (By similarity). Deconjugates SUMO1 from CLOCK, which decreases its transcriptional activation activity (By similarity). Deconjugates SUMO2 from MTA1 (By similarity). Deconjugates SUMO2 from MTA1 (By similarity). Deconjugates SUMO1 from METTL3 (By similarity). Desumoylates CCAR2 which decreases its interaction with SIRT1 (By similarity). Deconjugates SUMO1 from GPS2 (PubMed:29499132). {ECO:0000250|UniProtKB:Q9P0U3, ECO:0000269|PubMed:15923632, ECO:0000269|PubMed:29499132}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9P0U3}. Cytoplasm {ECO:0000250}. Note=Shuttles between cytoplasm and nucleus. {ECO:0000250}. SUBUNIT: Interacts with MTA1. Interacts with CCAR2 (via N-terminus). {ECO:0000250|UniProtKB:Q9P0U3}. +O35464 SEM6A_MOUSE Semaphorin-6A (Semaphorin Q) (Sema Q) (Semaphorin VIA) (Sema VIA) (Semaphorin-6A-1) (SEMA6A-1) 1031 114,433 Alternative sequence (2); Beta strand (40); Chain (1); Compositional bias (1); Disulfide bond (8); Domain (1); Glycosylation (6); Helix (14); Modified residue (2); Mutagenesis (5); Sequence conflict (10); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (8) TRANSMEM 650 670 Helical. {ECO:0000255}. TOPO_DOM 19 649 Extracellular. {ECO:0000255}.; TOPO_DOM 671 1031 Cytoplasmic. {ECO:0000255}. FUNCTION: Cell surface receptor for PLXNA2 that plays an important role in cell-cell signaling. Required for normal granule cell migration in the developing cerebellum. Promotes reorganization of the actin cytoskeleton and plays an important role in axon guidance in the developing central nervous system. Can act as repulsive axon guidance cue. Has repulsive action towards migrating granular neurons. May play a role in channeling sympathetic axons into the sympathetic chains and controlling the temporal sequence of sympathetic target innervation. {ECO:0000269|PubMed:16205717, ECO:0000269|PubMed:19063725, ECO:0000269|PubMed:20877282, ECO:0000269|PubMed:20881961}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20881961}; Single-pass type I membrane protein {ECO:0000269|PubMed:20881961}. SUBUNIT: Active as a homodimer or oligomer. The SEMA6A homodimer interacts with a PLXNA2 homodimer, giving rise to a heterotetramer. Interacts with EVL. {ECO:0000269|PubMed:10993894, ECO:0000269|PubMed:20877282, ECO:0000269|PubMed:20881961}. TISSUE SPECIFICITY: Particularly high levels in spinal cord, cerebellum, metencephalon, superior and inferior colliculus, diencephalon, olfactory bulb and eye. {ECO:0000269|PubMed:16205717}. +Q9WTM3 SEM6C_MOUSE Semaphorin-6C (Semaphorin-Y) (Sema Y) 931 99,538 Chain (1); Compositional bias (2); Disulfide bond (8); Domain (1); Glycosylation (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 606 626 Helical. {ECO:0000255}. TOPO_DOM 26 605 Extracellular. {ECO:0000255}.; TOPO_DOM 627 931 Cytoplasmic. {ECO:0000255}. FUNCTION: May be a stop signal for the dorsal root ganglion neurons in their target areas, and possibly also for other neurons. May also be involved in the maintenance and remodeling of neuronal connections (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. +Q6NXL6 SENP5_MOUSE Sentrin-specific protease 5 (EC 3.4.22.-) (SUMO/Smt3-specific isopeptidase 3) (Smt3ip3) (Sentrin/SUMO-specific protease SENP5) 749 86,100 Active site (3); Chain (1); Region (1); Sequence conflict (3) FUNCTION: Protease that catalyzes two essential functions in the SUMO pathway: processing of full-length SUMO3 to its mature form and deconjugation of SUMO2 and SUMO3 from targeted proteins. Has weak proteolytic activity against full-length SUMO1 or SUMO1 conjugates. Required for cell division. {ECO:0000250|UniProtKB:Q96HI0}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. SUBUNIT: Interacts with CCAR2. {ECO:0000250|UniProtKB:Q96HI0}. +Q4LFA9 SEM3G_MOUSE Semaphorin-3G 780 86,695 Chain (1); Disulfide bond (6); Domain (2); Glycosylation (3); Sequence conflict (1); Signal peptide (1) FUNCTION: Has chemorepulsive activities for sympathetic axons. Ligand of NRP2. {ECO:0000269|PubMed:16098142}. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Highly expressed in lung and kidney. Weakly expressed in brain. +Q8VHL1 SETD7_MOUSE Histone-lysine N-methyltransferase SETD7 (EC 2.1.1.43) (Histone H3-K4 methyltransferase SETD7) (H3-K4-HMTase SETD7) (SET domain-containing protein 7) (SET7/9) 366 40,506 Binding site (4); Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (1); Region (4); Repeat (3); Sequence conflict (2) FUNCTION: Histone methyltransferase that specifically monomethylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Plays a central role in the transcriptional activation of genes such as collagenase or insulin. Recruited by IPF1/PDX-1 to the insulin promoter, leading to activate transcription. Has also methyltransferase activity toward non-histone proteins such as p53/TP53, TAF10, and possibly TAF7 by recognizing and binding the [KR]-[STA]-K in substrate proteins. Monomethylates 'Lys-189' of TAF10, leading to increase the affinity of TAF10 for RNA polymerase II. Monomethylates 'Lys-372' of p53/TP53, stabilizing p53/TP53 and increasing p53/TP53-mediated transcriptional activation. {ECO:0000269|PubMed:12711597}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}. SUBUNIT: Interacts with IPF1/PDX-1. {ECO:0000250}. DOMAIN: The SET domain is necessary but not sufficient for histone methyltransferase activity. {ECO:0000250}. +Q9Z1N6 SFRP4_MOUSE Secreted frizzled-related sequence protein 4 (FRP-4) (sFRP-4) 351 40,342 Chain (1); Disulfide bond (5); Domain (2); Glycosylation (5); Sequence conflict (1); Signal peptide (1) FUNCTION: Soluble frizzled-related proteins (sFRPS) function as modulators of Wnt signaling through direct interaction with Wnts. They have a role in regulating cell growth and differentiation in specific cell types (PubMed:27355534). SFRP4 plays a role in bone morphogenesis (PubMed:27355534). May also act as a regulator of adult uterine morphology and function. May also increase apoptosis during ovulation possibly through modulation of FZ1/FZ4/WNT4 signaling (By similarity). Has phosphaturic effects by specifically inhibiting sodium-dependent phosphate uptake (By similarity). {ECO:0000250|UniProtKB:Q6FHJ7, ECO:0000250|UniProtKB:Q9JLS4, ECO:0000269|PubMed:27355534}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q6FHJ7}. DOMAIN: The FZ domain is involved in binding with Wnt ligands. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the ovary. Localized to granulosa cells of periovulatory follicles and corpora lutea. Weakly expressed in adult tissues including kidney, brain and lung. {ECO:0000269|PubMed:12960062}. +Q8VIJ6 SFPQ_MOUSE Splicing factor, proline- and glutamine-rich (DNA-binding p52/p100 complex, 100 kDa subunit) (Polypyrimidine tract-binding protein-associated-splicing factor) (PSF) (PTB-associated-splicing factor) 699 75,442 Chain (1); Coiled coil (1); Compositional bias (11); Cross-link (3); Domain (2); Modified residue (32); Region (1); Repeat (3); Sequence conflict (2) FUNCTION: DNA- and RNA binding protein, involved in several nuclear processes. Essential pre-mRNA splicing factor required early in spliceosome formation and for splicing catalytic step II, probably as a heteromer with NONO. Binds to pre-mRNA in spliceosome C complex, and specifically binds to intronic polypyrimidine tracts. Involved in regulation of signal-induced alternative splicing. During splicing of PTPRC/CD45, a phosphorylated form is sequestered by THRAP3 from the pre-mRNA in resting T-cells; T-cell activation and subsequent reduced phosphorylation is proposed to lead to release from THRAP3 allowing binding to pre-mRNA splicing regulatotry elements which represses exon inclusion. Interacts with U5 snRNA, probably by binding to a purine-rich sequence located on the 3' side of U5 snRNA stem 1b. May be involved in a pre-mRNA coupled splicing and polyadenylation process as component of a snRNP-free complex with SNRPA/U1A. The SFPQ-NONO heteromer associated with MATR3 may play a role in nuclear retention of defective RNAs. SFPQ may be involved in homologous DNA pairing; in vitro, promotes the invasion of ssDNA between a duplex DNA and produces a D-loop formation. The SFPQ-NONO heteromer may be involved in DNA unwinding by modulating the function of topoisomerase I/TOP1; in vitro, stimulates dissociation of TOP1 from DNA after cleavage and enhances its jumping between separate DNA helices. The SFPQ-NONO heteromer binds DNA. The SFPQ-NONO heteromer may be involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination and may stabilize paired DNA ends; in vitro, the complex strongly stimulates DNA end joining, binds directly to the DNA substrates and cooperates with the Ku70/G22P1-Ku80/XRCC5 (Ku) dimer to establish a functional preligation complex. SFPQ is involved in transcriptional regulation. Functions as transcriptional activator (By similarity). Transcriptional repression is mediated by an interaction of SFPQ with SIN3A and subsequent recruitment of histone deacetylases (HDACs). The SFPQ-NONO-NR5A1 complex binds to the CYP17 promoter and regulates basal and cAMP-dependent transcriptional activity. SFPQ isoform Long binds to the DNA binding domains (DBD) of nuclear hormone receptors, like RXRA and probably THRA, and acts as transcriptional corepressor in absence of hormone ligands. Binds the DNA sequence 5'-CTGAGTC-3' in the insulin-like growth factor response element (IGFRE) and inhibits IGF-I-stimulated transcriptional activity (By similarity). Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex through histone deacetylation (PubMed:21680841, PubMed:22966205). Required for the assembly of nuclear speckles (By similarity). Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway (By similarity). {ECO:0000250|UniProtKB:P23246, ECO:0000269|PubMed:21680841, ECO:0000269|PubMed:22966205}. PTM: Phosphorylated on multiple serine and threonine residues during apoptosis (By similarity). Phosphorylation of C-terminal tyrosines promotes its cytoplasmic localization, impaired its binding to polypyrimidine RNA and led to cell cycle arrest (By similarity). In resting T-cells is phosphorylated at Thr-679 by GSK3B which is proposed to promote association with THRAP and to prevent binding to PTPRC/CD45 pre-mRNA; T-cell activation leads to reduced phosphorylation at Thr-679. {ECO:0000250|UniProtKB:P23246}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:P23246}. Nucleus matrix {ECO:0000269|PubMed:21680841}. Cytoplasm {ECO:0000250|UniProtKB:P23246}. Note=Predominantly in nuclear matrix. {ECO:0000250|UniProtKB:P23246}. SUBUNIT: Heterodimer with NONO. Monomer and component of the SFPQ-NONO complex, which is probably a heterotetramer of two 52 kDa (NONO) and two 100 kDa (SFPQ) subunits. The coiled coil domain mediates interaction with NONO, and can also mediate formation of long, linear homooligomers (in vitro). SFPQ is a component of spliceosome and U5.4/6 snRNP complexes. Interacts with SNRPA/U1A. Component of a snRNP-free complex with SNRPA/U1A. Part of complex consisting of SFPQ, NONO and MATR3. Interacts with polypyrimidine tract-binding protein 1/PTB. Part of a complex consisting of SFPQ, NONO and NR5A1. Interacts with RXRA, probably THRA, and SIN3A. Interacts with TOP1. Part of a complex consisting of SFPQ, NONO and TOP1. Interacts with SNRNP70 in apoptotic cells. Interacts with PSPC1 (PubMed:15140795). Interacts with RNF43 (By similarity). Interacts with PITX3 and NR4A2/NURR1 (PubMed:19144721). Interacts with PTK6. Interacts with THRAP3; the interaction is dependent on SFPQ phosphorylation at 'Thr-687' and inhibits binding of SFPQ to a ESS1 exonic splicing silencer element-containing RNA (By similarity). The large PER complex involved in the histone deacetylation is composed of at least HDAC1, PER2, SFPQ and SIN3A (PubMed:21680841). Interacts with PER1 and PER2 (PubMed:22966205). Part of the HDP-RNP complex composed of at least HEXIM1, PRKDC, XRCC5, XRCC6, paraspeckle proteins (SFPQ, NONO, PSPC1, RBM14, and MATR3) and NEAT1 RNA (By similarity). Interacts with PQBP1. Component of a multiprotein complex with NONO and WASL (By similarity). {ECO:0000250|UniProtKB:P23246, ECO:0000269|PubMed:15140795, ECO:0000269|PubMed:19144721, ECO:0000269|PubMed:21680841, ECO:0000269|PubMed:22966205}. DOMAIN: The coiled coil domain mediates interaction with NONO, and can also mediate formation of long, linear homooligomers (in vitro). The coiled coil domain is required for optimal DNA binding, and optimal transcription activation. {ECO:0000250|UniProtKB:P23246}. +Q91V61 SFXN3_MOUSE Sideroflexin-3 321 35,406 Alternative sequence (1); Chain (1); Modified residue (1); Sequence conflict (1); Transmembrane (4) TRANSMEM 146 164 Helical. {ECO:0000255}.; TRANSMEM 174 194 Helical. {ECO:0000255}.; TRANSMEM 225 245 Helical. {ECO:0000255}.; TRANSMEM 266 286 Helical. {ECO:0000255}. FUNCTION: Potential iron transporter. SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11274051}. +Q925N0 SFXN5_MOUSE Sideroflexin-5 342 37,329 Chain (1); Transmembrane (4) TRANSMEM 105 125 Helical. {ECO:0000255}.; TRANSMEM 165 185 Helical. {ECO:0000255}.; TRANSMEM 256 276 Helical. {ECO:0000255}.; TRANSMEM 289 309 Helical. {ECO:0000255}. FUNCTION: Transports citrate. Potential iron transporter (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Expressed in liver and brain. {ECO:0000269|PubMed:11274051}. +P82348 SGCG_MOUSE Gamma-sarcoglycan (Gamma-SG) (35 kDa dystrophin-associated glycoprotein) (35DAG) 291 32,082 Chain (1); Disulfide bond (2); Glycosylation (1); Topological domain (2); Transmembrane (1) TRANSMEM 38 58 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 37 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 59 291 Extracellular. {ECO:0000255}. FUNCTION: Component of the sarcoglycan complex, a subcomplex of the dystrophin-glycoprotein complex which forms a link between the F-actin cytoskeleton and the extracellular matrix. SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000269|PubMed:9864373}; Single-pass type II membrane protein {ECO:0000269|PubMed:9864373}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9864373}. SUBUNIT: Interacts with the syntrophin SNTA1 and FLNC. Cross-link to form 2 major subcomplexes: one consisting of SGCB, SGCD and SGCG and the other consisting of SGCB and SGCD. The association between SGCB and SGCG is particularly strong while SGCA is loosely associated with the other sarcoglycans. {ECO:0000269|PubMed:7547961, ECO:0000269|PubMed:9864373}. TISSUE SPECIFICITY: Most strongly expressed in skeletal and heart muscle. Also detected in proliferating myoblasts. +Q6UGQ3 SG2B2_MOUSE Secretoglobin family 2B member 2 (Androgen-binding protein epsilon) (Lacrimal androgen-binding protein epsilon) 114 12,857 Chain (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Expressed in lacrimal gland. {ECO:0000269|PubMed:15623751}. +Q920D7 SG3A1_MOUSE Secretoglobin family 3A member 1 (Cytokine HIN-1) (High in normal 1) (Pneumo secretory protein 2) (PnSP-2) (Uteroglobin-related protein 2) 104 10,591 Chain (1); Disulfide bond (1); Signal peptide (1) FUNCTION: Secreted cytokine-like protein. Inhibits cell growth in vitro. {ECO:0000250|UniProtKB:Q96QR1}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q96QR1}. SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250|UniProtKB:Q920H1}. TISSUE SPECIFICITY: Highly expressed in lung, where it localizes to epithelial cells lining the trachea and bronchi (PubMed:12406855, PubMed:12175512). Expression in lung is mainly restricted to bronchi, submucosal glands of the trachea, and tracheal epithelium, with little expression in terminal bronchioles (PubMed:12406855). Expressed in uterus where it localizes to epithelial cells of the uterine glands (PubMed:12175512). Also detected in heart, stomach and small intestine (PubMed:12175512). {ECO:0000269|PubMed:12175512, ECO:0000269|PubMed:12406855}. +P82350 SGCA_MOUSE Alpha-sarcoglycan (Alpha-SG) (50 kDa dystrophin-associated glycoprotein) (50DAG) (Adhalin) 387 43,287 Chain (1); Glycosylation (2); Modified residue (1); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 294 314 Helical. {ECO:0000255}. TOPO_DOM 24 293 Extracellular. {ECO:0000255}.; TOPO_DOM 315 387 Cytoplasmic. {ECO:0000255}. FUNCTION: Component of the sarcoglycan complex, a subcomplex of the dystrophin-glycoprotein complex which forms a link between the F-actin cytoskeleton and the extracellular matrix. SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000269|PubMed:9864373}; Single-pass type I membrane protein {ECO:0000269|PubMed:9864373}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9864373}. SUBUNIT: Cross-link to form 2 major subcomplexes: one consisting of SGCB, SGCD and SGCG and the other consisting of SGCB and SGCD. The association between SGCB and SGCG is particularly strong while SGCA is loosely associated with the other sarcoglycans. Interacts with the syntrophin SNTA1. {ECO:0000269|PubMed:7547961, ECO:0000269|PubMed:9864373}. TISSUE SPECIFICITY: Striated muscle, both skeletal and cardiac. {ECO:0000269|PubMed:9196068}. +P82349 SGCB_MOUSE Beta-sarcoglycan (Beta-SG) (43 kDa dystrophin-associated glycoprotein) (43DAG) 320 34,873 Chain (1); Disulfide bond (2); Glycosylation (3); Topological domain (2); Transmembrane (1) TRANSMEM 68 88 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 67 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 89 320 Extracellular. {ECO:0000255}. FUNCTION: Component of the sarcoglycan complex, a subcomplex of the dystrophin-glycoprotein complex which forms a link between the F-actin cytoskeleton and the extracellular matrix. PTM: Disulfide bonds are present. SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000269|PubMed:9864373}; Single-pass type II membrane protein {ECO:0000269|PubMed:9864373}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9864373}. SUBUNIT: Cross-link to form 2 major subcomplexes: one consisting of SGCB, SGCD and SGCG and the other consisting of SGCB and SGCD. The association between SGCB and SGCG is particularly strong while SGCA is loosely associated with the other sarcoglycans. {ECO:0000269|PubMed:9864373}. TISSUE SPECIFICITY: Most strongly expressed in skeletal and heart muscle. Also detected in proliferating myoblasts. +Q8VD00 SGMR2_MOUSE Sigma intracellular receptor 2 (Sigma-2 receptor) (Sigma2 receptor) (Transmembrane protein 97) 176 20,811 Chain (1); Domain (1); Topological domain (5); Transmembrane (4) TRANSMEM 10 30 Helical; Name=1. {ECO:0000255}.; TRANSMEM 69 89 Helical; Name=2. {ECO:0000255}.; TRANSMEM 100 120 Helical; Name=3. {ECO:0000255}.; TRANSMEM 141 161 Helical; Name=4. {ECO:0000255}. TOPO_DOM 1 9 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 31 68 Extracellular. {ECO:0000255}.; TOPO_DOM 90 99 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 121 140 Extracellular. {ECO:0000255}.; TOPO_DOM 162 176 Cytoplasmic. {ECO:0000255}. FUNCTION: Intracellular orphan receptor that binds numerous drugs and which is highly expressed in various proliferating cells. Corresponds to the sigma-2 receptor, which is thought to play important role in regulating cell survival, morphology and differentiation. May play a role as a regulator of cellular cholesterol homeostasis. May function as sterol isomerase. May alter the activity of some cytochrome P450 proteins. {ECO:0000250|UniProtKB:Q5BJF2}. SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250|UniProtKB:Q5BJF2}; Multi-pass membrane protein {ECO:0000255}. Rough endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q5BJF2}; Multi-pass membrane protein {ECO:0000255}. Note=Localized at cell membrane and in lysosomes in sterol-depleted cells when expression of endogenous TMEM97 is stimulated. {ECO:0000250|UniProtKB:Q5BJF2}. SUBUNIT: Interacts with NPC1. {ECO:0000250|UniProtKB:Q5BJF2}. +Q8BI17 SH2D7_MOUSE SH2 domain-containing protein 7 458 50,552 Alternative sequence (1); Chain (1); Domain (1); Erroneous initiation (1) +Q7TSG5 SH321_MOUSE SH3 domain-containing protein 21 549 60,324 Alternative sequence (1); Chain (1); Coiled coil (1); Compositional bias (1); Domain (1) +Q69ZI1 SH3R1_MOUSE E3 ubiquitin-protein ligase SH3RF1 (EC 2.3.2.27) (Plenty of SH3s) (Protein POSH) (RING-type E3 ubiquitin transferase SH3RF1) (SH3 domain-containing RING finger protein 1) (SH3 multiple domains protein 2) 892 93,447 Alternative sequence (5); Chain (1); Compositional bias (3); Domain (4); Erroneous initiation (1); Modified residue (3); Mutagenesis (2); Region (2); Sequence conflict (10); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: Has E3 ubiquitin-protein ligase activity. In the absence of an external substrate, it can catalyze self-ubiquitination. Stimulates ubiquitination of potassium channel KCNJ1, enhancing its dynamin-dependent and clathrin-independent endocytosis (By similarity). Acts as a scaffold protein that coordinates with MAPK8IP1/JIP1 in organizing different components of the JNK pathway, including RAC1 or RAC2, MAP3K11/MLK3 or MAP3K7/TAK1, MAP2K7/MKK7, MAPK8/JNK1 and/or MAPK9/JNK2 into a functional multiprotein complex to ensure the effective activation of the JNK signaling pathway. Regulates the differentiation of CD4(+) and CD8(+) T-cells and promotes T-helper 1 (Th1) cell differentiation. Regulates the activation of MAPK8/JNK1 and MAPK9/JNK2 in CD4(+) T-cells and the activation of MAPK8/JNK1 in CD8(+) T-cells (PubMed:23963642, PubMed:27084103, PubMed:9482736). Plays a crucial role in the migration of neocortical neurons in the developing brain. Controls proper cortical neuronal migration and the formation of proximal cytoplasmic dilation in the leading process (PCDLP) in migratory neocortical neurons by regulating the proper localization of activated RAC1 and F-actin assembly (PubMed:22959435). {ECO:0000250|UniProtKB:Q7Z6J0, ECO:0000269|PubMed:22959435, ECO:0000269|PubMed:23963642, ECO:0000269|PubMed:27084103, ECO:0000269|PubMed:9482736}. PTM: Phosphorylated at Ser-304 by AKT1 and AKT2. When phosphorylated, it has reduced ability to bind Rac. {ECO:0000250|UniProtKB:Q7Z6J0}.; PTM: Autoubiquitinated. Ubiquitinated by SH3RF2, leading to proteasome-mediated degradation. {ECO:0000250|UniProtKB:Q71F54}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q71F54}. Cell projection, lamellipodium {ECO:0000269|PubMed:14504284, ECO:0000269|PubMed:22959435}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:14504284}. Note=Colocalizes, with AKT2 in lamellipodia. Colocalizes, with HERP1, in trans-Golgi network (By similarity). {ECO:0000250|UniProtKB:Q7Z6J0, ECO:0000269|PubMed:14504284}. SUBUNIT: Interacts with HERP1 (By similarity). Interacts with RAC1; in a GTP-dependent manner (PubMed:22959435, PubMed:9482736). Interacts with MAP3K10/MLK2 and MAP3K11/MLK3. Interacts with MAPK8IP; this interaction leads to the PJAC complex (POSH-JIP or SH3RF1/MAPK8IP1 apoptotic complex) with a 1:1 ratio. Interacts with SIAH1. Probably part of a signaling complex that may contain SH3RF1, MAPK8IP, DLK1, MAP2K4/MKK4, MAP2K7/MKK7, MAPK8/JNK1, MAPK9/JNK2, AKT1 and AKT2 (PubMed:12514131, PubMed:14504284, PubMed:16230351, PubMed:16571722, PubMed:23963642). Found in a complex with RAC2, MAP3K7/TAK1, MAP2K7/MKK7, MAPK8IP1/JIP1, MAPK8/JNK1 and MAPK9/JNK2 (PubMed:27084103). Found in a complex with RAC1, MAP3K11/MLK3, MAP2K7/MKK7, MAPK8IP1/JIP1 and MAPK8/JNK1 (PubMed:23963642). Interacts with SH3RF2 (By similarity). {ECO:0000250|UniProtKB:Q71F54, ECO:0000250|UniProtKB:Q7Z6J0, ECO:0000269|PubMed:12514131, ECO:0000269|PubMed:14504284, ECO:0000269|PubMed:16230351, ECO:0000269|PubMed:16571722, ECO:0000269|PubMed:22959435, ECO:0000269|PubMed:23963642, ECO:0000269|PubMed:27084103, ECO:0000269|PubMed:9482736}. DOMAIN: The RING finger domain is required for ubiquitin ligase activity and autoubiquitination. {ECO:0000250|UniProtKB:Q7Z6J0}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:9482736}. +Q9WUZ7 SH3BG_MOUSE SH3 domain-binding glutamic acid-rich protein (SH3BGR protein) 214 23,102 Chain (1); Compositional bias (1); Motif (1) +Q8BJU0 SGTA_MOUSE Small glutamine-rich tetratricopeptide repeat-containing protein alpha (Alpha-SGT) 315 34,322 Alternative sequence (1); Chain (1); Compositional bias (1); Modified residue (6); Repeat (3); Sequence conflict (1) FUNCTION: Co-chaperone that binds misfolded and hydrophobic patches-containing client proteins in the cytosol. Mediates their targeting to the endoplasmic reticulum but also regulates their sorting to the proteasome when targeting fails. Functions in tail-anchored/type II transmembrane proteins membrane insertion constituting with ASNA1 and the BAG6 complex a targeting module. Functions upstream of the BAG6 complex and ASNA1, binding more rapidly the transmembrane domain of newly synthesized proteins. It is also involved in the regulation of the endoplasmic reticulum-associated misfolded protein catabolic process via its interaction with BAG6: collaborates with the BAG6 complex to maintain hydrophobic substrates in non-ubiquitinated states. Competes with RNF126 for interaction with BAG6, preventing the ubiquitination of client proteins associated with the BAG6 complex. Binds directly to HSC70 and HSP70 and regulates their ATPase activity. {ECO:0000250|UniProtKB:O43765}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O43765}. Nucleus {ECO:0000250|UniProtKB:O43765}. Note=Co-localizes with HSP90AB1 in the cytoplasm. Increased nuclear accumulation seen during cell apoptosis. {ECO:0000250|UniProtKB:O43765}. SUBUNIT: Homodimer (By similarity). Homooligomer (By similarity). Interacts with DNAJC5 and DNAJC5B (PubMed:17034881). Interacts (via TPR repeats) with HSP90AA1. Interacts (via Gln-rich region) with SLC2A1 (By similarity). Interacts with HSP90AB1 (By similarity). Interacts (via TPR repeats) with HSPA8/Hsc70; the interaction is direct (By similarity). Interacts with BAG6 (via ubiquitin-like domain); interaction prevents interaction between BAG6 and RNF126 (By similarity). Forms a multiprotein complex, at least composed of DNAJB12, DNAJB14, HSPA8/Hsc70 and SGTA; interaction with DNAJB14 and HSPA8/Hsc70 is direct (By similarity). {ECO:0000250|UniProtKB:O43765, ECO:0000250|UniProtKB:O70593, ECO:0000269|PubMed:17034881}. +Q80U12 SGSM2_MOUSE Small G protein signaling modulator 2 (RUN and TBC1 domain-containing protein 1) 1005 113,076 Alternative sequence (1); Chain (1); Domain (2); Erroneous initiation (1); Frameshift (2); Modified residue (2) FUNCTION: Possesses GTPase activator activity towards RAB32, RAB33B and RAB38. Regulates the trafficking of melanogenic enzymes TYR, TYRP1 and DCT/TYRP2 to melanosomes in melanocytes by inactivating RAB32 and RAB38. Inhibits RAB32 and RAB38 activation both directly by promoting their GTPase activity and indirectly by disrupting the RAB9A-HPS4 interaction which is required for RAB32/38 activation (PubMed:26620560). {ECO:0000269|PubMed:26620560}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O43147}. Melanosome {ECO:0000269|PubMed:26620560}. Note=Melanosomal localization is mediated by RAB9A. {ECO:0000250|UniProtKB:O43147}. SUBUNIT: Interacts with RAB4A, RAB11A, RAP1A, RAP1B, RAP2A and RAP2B. No interaction with RAB27A. Interacts with RAB9A (By similarity). {ECO:0000250|UniProtKB:O43147}. DOMAIN: The Rab-GAP TBC domain possesses GTPase activator activity. {ECO:0000250|UniProtKB:O43147}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:17509819}. +Q62421 SH3G3_MOUSE Endophilin-A3 (Endophilin-3) (SH3 domain protein 2C) (SH3 domain-containing GRB2-like protein 3) (SH3p13) 347 38,934 Chain (1); Coiled coil (1); Compositional bias (1); Domain (2); Region (3); Sequence conflict (1) FUNCTION: Implicated in endocytosis. May recruit other proteins to membranes with high curvature (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O35180}. Early endosome membrane {ECO:0000250|UniProtKB:O35180}; Peripheral membrane protein {ECO:0000250|UniProtKB:O35180}. Note=Associated with postsynaptic endosomes in hippocampal neurons. Associated with presynaptic endosomes in olfactory neurons. {ECO:0000250|UniProtKB:O35180}. SUBUNIT: Interacts with ARC, DNM1, SGIP1, SYNJ1 and DYDC1. Interacts with FASLG (By similarity). Interacts with ATX2. Interacts with BIN2 (By similarity). {ECO:0000250}. DOMAIN: An N-terminal amphipathic helix, the BAR domain and a second amphipathic helix inserted into helix 1 of the BAR domain (N-BAR domain) induce membrane curvature and bind curved membranes. {ECO:0000250}. +Q9QXK9 SH22A_MOUSE SH2 domain-containing protein 2A (Lck-associated adapter protein) (Lad) (Rlk/Itk-binding protein) (Ribp) 374 40,953 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (1); Modified residue (2); Motif (1); Sequence conflict (2) FUNCTION: Could be a T-cell-specific adapter protein involved in the control of T-cell activation. May play a role in p56-LCK-mediated T-cell signaling. Could be involved in the regulation of responses to T-cell activation stimuli, specifically proliferation and lymphokine production. Interactions with ITK and TXK may provide important biochemical links of these two important kinases with other components in the T-cell activation machinery. {ECO:0000269|PubMed:10587356}. PTM: Phosphorylated on tyrosine residues upon TCR-stimulation. SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Note=Redistributed from cytoplasm to the plasma membrane in a T-cell activation-dependent manner. SUBUNIT: Interacts with KDR (By similarity). Interacts with p56-LCK, TXK and ITK. {ECO:0000250, ECO:0000269|PubMed:10587356}. TISSUE SPECIFICITY: Expression limited to tissues of the immune system and, in particular, activated T-cells and natural killer cells. Expressed in the thymus, lymph node, and to a lesser extent, in the spleen and bone marrow. According to PubMed:10553045, also expressed in the lung. +Q8R550 SH3K1_MOUSE SH3 domain-containing kinase-binding protein 1 (Regulator of ubiquitous kinase) (Ruk) (SH3-containing, expressed in tumorigenic astrocytes) 709 78,170 Alternative sequence (7); Beta strand (9); Chain (1); Coiled coil (1); Domain (3); Helix (2); Modified residue (10); Sequence conflict (3) FUNCTION: Adapter protein involved in regulating diverse signal transduction pathways. Involved in the regulation of endocytosis and lysosomal degradation of ligand-induced receptor tyrosine kinases, including EGFR and MET/hepatocyte growth factor receptor, through an association with CBL and endophilins. The association with CBL, and thus the receptor internalization, may inhibited by an interaction with PDCD6IP and/or SPRY2. Involved in regulation of ligand-dependent endocytosis of the IgE receptor. Attenuates phosphatidylinositol 3-kinase activity by interaction with its regulatory subunit. May be involved in regulation of cell adhesion; promotes the interaction between TTK2B and PDCD6IP. May be involved in the regulation of cellular stress response via the MAPK pathways through its interaction with MAP3K4. Is involved in modulation of tumor necrosis factor mediated apoptosis. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration (By similarity). {ECO:0000250}. PTM: Monoubiquitinated by CBL and CBLB after EGF stimulation; probably on its C-terminus. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96B97}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell junction, synapse, synaptosome {ECO:0000250}. Cell junction, focal adhesion {ECO:0000250}. Note=Localized in endocytic vesicles containing clustered receptors. Colocalizes with ASAP1 in vesicular structures. Colocalized with actin microfilaments and focal adhesions (By similarity). Colocalized with MAGI2 in synaptosomes (By similarity). Translocation to EGFR containing vesicles upon EGF stimulation is inhibited in the presence of SH3KBP1 (PubMed:21830225). Colocalizes with ZFP36 in the cytoplasm (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q96B97, ECO:0000269|PubMed:21830225}. SUBUNIT: Can self-associate and form homotetramers. Interacts with CD2, F-actin capping protein, PIK3R3, GRB2, EGFR, MET, BLNK, MAP3K4, PDCD6IP, SPRY2, ARHGAP17, ARHGAP27, CRK, BCAR1, SOS1, ASAP1, ARAP3, HIP1R, SYNJ2, INPP5D and STAP1 (By similarity). Interacts with CBL (PubMed:21830225). Interacts with CBLB, but does not interact with CBLC. Two molecules of SH3KBP1 seem to bind through their respective SH3 1 domain to one molecule of CBLB. The interaction with CBL or CBLB and EGFR is increased upon EGF stimulation. The interaction with CBL is attenuated by PDCD6IP. Interacts through its proline-rich region with the SH3 domain of endophilins SH3GL1, SH3GL2 and SH3GL3. The SH3KBP1-endophilin complex seems to associate with a complex containing the phosphorylated receptor (EGFR or MET) and phosphorylated CBL. Probably associates with ASAP1 and phosphorylated EGFR. Probably part of a complex consisting of at least SH3KBP1, ASAP1 and ARAP3. Interacts with focal adhesion kinases PTK2/FAK1 AND PTK2B/PYK2, probably as a dimer. Interacts with DAB2 and probably associates with chathrin through its interaction with DAB2. Part of a complex consisting of SH3KBP1, DAB2, and clathrin heavy chain. DAB2 and clathrin dissociate from SH3KBP1 following growth factor treatment, enabling interaction with CBL. Interacts with DDN and probably associates with MAGI2 through its interaction with DDN. Interacts with the SH3 domains of SRC tyrosine-protein kinases SRC, LCK, LYN, FGR, FYN and HCK. Interacts with TRADD, BIRC2, TRAF1, TRAF2 and TNFR1, and the association with a TNFR1-associated complex upon stimulation with TNF-alpha seems to be mediated by SRC. Probably part of a complex consisting of at least SH3KBP1, ASAP1 and ARAP3 (By similarity). Interacts (via SH3 domains) with SHKBP1 (via PXXXPR motifs) (PubMed:11152963, PubMed:21830225). Interacts with ATX2 (PubMed:18602463). Interaction with CBL is abolished in the presence of SHKBP1 (PubMed:21830225). Interacts (via SH3 domains) with ZFP36 (via extreme C-terminal region). Interacts with MAP3K4; this interaction enhances the association with ZFP36 (By similarity). {ECO:0000250|UniProtKB:Q96B97, ECO:0000269|PubMed:11152963, ECO:0000269|PubMed:18602463, ECO:0000269|PubMed:21830225}. +P70390 SHOX2_MOUSE Short stature homeobox protein 2 (Homeobox protein Og12X) (OG-12) (Paired family homeodomain protein Prx3) 331 34,905 Alternative sequence (1); Chain (1); Compositional bias (1); DNA binding (1); Erroneous initiation (2); Motif (1) FUNCTION: May be a growth regulator and have a role in specifying neural systems involved in processing somatosensory information, as well as in face and body structure formation. May also have a role in heart development. SUBCELLULAR LOCATION: Nucleus. TISSUE SPECIFICITY: Highly expressed in striated muscle followed by liver, kidney, testis, brain, heart, lung and spleen. +Q8QZV2 SHSA2_MOUSE Protein shisa-2 homolog (Shisa-like protein 2) (mShisa) (Transmembrane protein 46) 295 31,466 Chain (1); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 111 131 Helical. {ECO:0000255}. TOPO_DOM 34 110 Extracellular. {ECO:0000255}.; TOPO_DOM 132 295 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays an essential role in the maturation of presomitic mesoderm cells by individual attenuation of both FGF and WNT signaling. {ECO:0000269|PubMed:16773659, ECO:0000269|PubMed:17481602}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. +Q3TTP0 SHP1L_MOUSE Testicular spindle-associated protein SHCBP1L (SHC SH2 domain-binding protein 1-like protein) 639 70,948 Chain (1); Coiled coil (1); Modified residue (6); Repeat (4) FUNCTION: Testis-specific spindle-associated factor that plays a role in spermatogenesis (PubMed:24557841). In association with HSPA2, participates in the maintenance of spindle integrity during meiosis in male germ cells (PubMed:24557841). {ECO:0000269|PubMed:24557841}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:24557841}. Note=Colocalizes with alpha tubulin during meiosis (PubMed:24557841). Colocalizes with HSPA2 at spindle during the meiosis process (PubMed:24557841). {ECO:0000269|PubMed:24557841}. SUBUNIT: Interacts with HSPA2; this interaction may promote the recruitment of HSPA2 to the spindle (PubMed:24557841). {ECO:0000269|PubMed:24557841}. TISSUE SPECIFICITY: Expressed in pachytene spermatocytes and elongating spermatids inside the seminiferous tubules (PubMed:24557841). Not detected in ovary (at protein level) (PubMed:24557841). Testis-specific (PubMed:24557841). {ECO:0000269|PubMed:24557841}. +Q9D112 SHLD1_MOUSE Shieldin complex subunit 1 (RINN1-REV7-interacting novel NHEJ regulator 3) 206 22,697 Chain (1) FUNCTION: Component of the shieldin complex, which plays an important role in repair of DNA double-stranded breaks (DSBs). During G1 and S phase of the cell cycle, the complex functions downstream of TP53BP1 to promote non-homologous end joining (NHEJ) and suppress DNA end resection. Mediates various NHEJ-dependent processes including immunoglobulin class-switch recombination, and fusion of unprotected telomeres. {ECO:0000250|UniProtKB:Q8IYI0}. SUBCELLULAR LOCATION: Chromosome {ECO:0000250|UniProtKB:Q8IYI0}. SUBUNIT: Component of the shieldin complex, consisting of SHLD1, SHLD2, SHLD3 and MAD2L2/REV7. Within the complex, SHLD2 forms a scaffold which interacts with a SHLD3-MAD2L2 subcomplex via its N-terminus, and with SHLD1 via its C-terminus. {ECO:0000250|UniProtKB:Q8IYI0}. +Q6P1D7 SLX4_MOUSE Structure-specific endonuclease subunit SLX4 (BTB/POZ domain-containing protein 12) 1565 172,412 Chain (1); Cross-link (10); Domain (1); Modified residue (9); Mutagenesis (4); Region (3) FUNCTION: Regulatory subunit that interacts with and increases the activity of different structure-specific endonucleases. Has several distinct roles in protecting genome stability by resolving diverse forms of deleterious DNA structures originating from replication and recombination intermediates and from DNA damage. Component of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA. Has a preference for 5'-flap structures, and promotes symmetrical cleavage of static and migrating Holliday junctions (HJs). Resolves HJs by generating two pairs of ligatable, nicked duplex products. Interacts with the structure-specific ERCC4-ERCC1 endonuclease and promotes the cleavage of bubble structures. Interacts with the structure-specific MUS81-EME1 endonuclease and promotes the cleavage of 3'-flap and replication fork-like structures. SLX4 is required for recovery from alkylation-induced DNA damage and is involved in the resolution of DNA double-strand breaks (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Localizes to sites of DNA damage. {ECO:0000250}. SUBUNIT: Forms a heterodimer with SLX1A/GIYD1. Interacts with ERCC4; catalytic subunit of the ERCC4-ERCC1 endonuclease. Interacts with MUS81; catalytic subunit of the MUS81-EME1 endonuclease. Interacts with MSH2; component of the MSH2-MSH3 mismatch repair complex. Interacts with TERF2-TERF2IP. Interacts with PLK1 and SLX4IP (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in testis. Expressed in bone marrow, brain, thymus and weakly in heart, kidney and spleen. {ECO:0000269|PubMed:27010503}. +P70340 SMAD1_MOUSE Mothers against decapentaplegic homolog 1 (MAD homolog 1) (Mothers against DPP homolog 1) (Dwarfin-A) (Dwf-A) (Mothers-against-DPP-related 1) (Mad-related protein 1) (mMad1) (SMAD family member 1) (SMAD 1) (Smad1) 465 52,157 Beta strand (7); Chain (1); Compositional bias (1); Domain (2); Helix (7); Metal binding (4); Modified residue (4); Region (1); Sequence conflict (6) FUNCTION: Transcriptional modulator activated by BMP (bone morphogenetic proteins) type 1 receptor kinase. SMAD1 is a receptor-regulated SMAD (R-SMAD) (By similarity). May play a role in the initiation and maintenance of spermatogenesis. SMAD1/OAZ1/PSMB4 complex mediates the degradation of the CREBBP/EP300 repressor SNIP1 (By similarity). May act synergistically with SMAD4 and YY1 in bone morphogenetic protein (BMP)-mediated cardiac-specific gene expression (PubMed:15329343). {ECO:0000250|UniProtKB:Q15797, ECO:0000269|PubMed:15329343}. PTM: Phosphorylation of the C-terminal SVS motif by BMP type 1 receptor kinase activates SMAD1 by promoting dissociation from the receptor and trimerization with SMAD4 (By similarity). Dephosphorylation, probably by PPM1A, induces its export from the nucleus to the cytoplasm (PubMed:25755279). {ECO:0000250|UniProtKB:Q15797, ECO:0000269|PubMed:25755279}.; PTM: Ubiquitinated by SMAD-specific E3 ubiquitin ligase SMURF1, leading to its degradation. Monoubiquitinated, leading to prevent DNA-binding. Deubiquitination by USP15 alleviates inhibition and promotes activation of TGF-beta target genes (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25755279}. Nucleus {ECO:0000269|PubMed:25755279}. Note=In the cytoplasm in the absence of ligand. Migration to the nucleus when complexed with SMAD4. Colocalizes with LEMD3 at the nucleus inner membrane. Exported from the nucleus to the cytoplasm when dephosphorylated (PubMed:25755279). {ECO:0000250|UniProtKB:Q15797, ECO:0000269|PubMed:25755279}. SUBUNIT: Upon C-terminus phosphorylation: forms trimers with another SMAD1 and the co-SMAD SMAD4. Interacts with PEBP2-alpha subunit, CREB-binding protein (CBP), p300, SMURF1, SMURF2, USP15 and HOXC8. Associates with ZNF423 or ZNF521 in response to BMP2 leading to activate transcription of BMP target genes. Interacts with SKOR1. Interacts (via MH2 domain) with LEMD3. Binding to LEMD3 results in at least a partial reduction of receptor-mediated phosphorylation (By similarity). Also interacts with HGS, NANOG and ZCCHC12. Forms a ternary complex with PSMB4 and OAZ1 before PSMB4 is incorporated into the 20S proteasome (By similarity). Found in a complex with SMAD4 and YY1. Interacts (via MH2 domain) with FAM83G (via MH2 domain); in a SMAD4-independent manner. Interacts with ZC3H3 (PubMed:16115198). Interacts with TMEM119 (PubMed:21239498). Interacts (via MH1 and MH2 domains) with ZNF8 (PubMed:12370310). Interacts with RANBP3L; the interaction increases when SMAD1 is not phosphorylated and mediates SMAD1 nuclear export (PubMed:25755279). {ECO:0000250|UniProtKB:Q15797, ECO:0000269|PubMed:11094085, ECO:0000269|PubMed:12370310, ECO:0000269|PubMed:15329343, ECO:0000269|PubMed:16115198, ECO:0000269|PubMed:16801560, ECO:0000269|PubMed:18160706, ECO:0000269|PubMed:20147459, ECO:0000269|PubMed:21239498, ECO:0000269|PubMed:25755279}. DOMAIN: The MH2 domain mediates phosphorylation-dependent trimerization through L3 loop binding of phosphoserines in the adjacent subunit. {ECO:0000250|UniProtKB:Q15797}. TISSUE SPECIFICITY: Ubiquitous. +Q9R0P4 SMAP_MOUSE Small acidic protein (Sid 2057) 181 20,046 Chain (1); Compositional bias (1); Cross-link (3); Modified residue (8) +Q62432 SMAD2_MOUSE Mothers against decapentaplegic homolog 2 (MAD homolog 2) (Mothers against DPP homolog 2) (Mad-related protein 2) (mMad2) (SMAD family member 2) (SMAD 2) (Smad2) 467 52,266 Alternative sequence (1); Chain (1); Domain (2); Initiator methionine (1); Metal binding (4); Modified residue (13); Motif (1); Sequence conflict (2) FUNCTION: Receptor-regulated SMAD (R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta (transforming growth factor) and activin type 1 receptor kinases. Binds the TRE element in the promoter region of many genes that are regulated by TGF-beta and, on formation of the SMAD2/SMAD4 complex, activates transcription. May act as a tumor suppressor in colorectal carcinoma. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator (By similarity). {ECO:0000250|UniProtKB:Q15796, ECO:0000269|PubMed:15356634}. PTM: In response to TGF-beta, phosphorylated on the C-terminal SXS motif by TGF-beta and activin type 1 receptor kinases, phosphorylation declines progressively in a KMT5A-dependent manner. Phosphorylation in this motif is required for interaction with a number of proteins including SMURF2, SNON and SMAD4 in response to TGF-beta. Dephosphorylated in this motif by PPM1A leading to disruption of the SMAD2/3-SMAD4 complex, nuclear export and termination of the TGF-beta signaling. In response to decorin, the naturally occurring inhibitor of TGF-beta signaling, phosphorylated on Ser-240 by CaMK2. Phosphorylated by MAPK3 upon EGF stimulation; which increases transcriptional activity and stability, and is blocked by calmodulin. Phosphorylated by PDPK1. {ECO:0000269|PubMed:12672795, ECO:0000269|PubMed:15356634, ECO:0000269|PubMed:17341133}.; PTM: In response to TGF-beta, ubiquitinated by NEDD4L; which promotes its degradation. Monoubiquitinated, leading to prevent DNA-binding (PubMed:15496141). Deubiquitination by USP15 alleviates inhibition and promotes activation of TGF-beta target genes (By similarity). Ubiquitinated by RNF111, leading to its degradation: only SMAD2 proteins that are 'in use' are targeted by RNF111, RNF111 playing a key role in activating SMAD2 and regulating its turnover (PubMed:17341133). {ECO:0000250|UniProtKB:Q15796, ECO:0000269|PubMed:15496141, ECO:0000269|PubMed:17341133}.; PTM: Acetylated on Lys-19 by coactivators in response to TGF-beta signaling, which increases transcriptional activity. {ECO:0000250|UniProtKB:Q15796}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q15796}. Nucleus {ECO:0000250|UniProtKB:Q15796}. Note=Cytoplasmic and nuclear in the absence of TGF-beta. On TGF-beta stimulation, migrates to the nucleus when complexed with SMAD4. On dephosphorylation by phosphatase PPM1A, released from the SMAD2/SMAD4 complex, and exported out of the nucleus by interaction with RANBP1. {ECO:0000250|UniProtKB:Q15796}. SUBUNIT: Monomer; the absence of TGF-beta. Interacts with ZNF580. Heterodimer; in the presence of TGF-beta. Forms a heterodimer with co-SMAD, SMAD4, in the nucleus to form the transactivation complex SMAD2/SMAD4. Found in a complex with SMAD3 and TRIM33 upon addition of TGF-beta. Interacts with ACVR1B, SMAD3 and TRIM33. Interacts (via the MH2 domain) with ZFYVE9; may form trimers with the SMAD4 co-SMAD. Interacts with FOXH1, homeobox protein TGIF, PEBP2-alpha subunit, CREB-binding protein (CBP), EP300, SKI and SNW1. Interacts with SNON; when phosphorylated at Ser-465/467. Interacts (via PY-motif) with SMURF2. Interacts with SKOR1 and SKOR2. Interacts with PRDM16. Interacts (via MH2 domain) with LEMD3. Interacts with RBPMS. Interacts (dephosphorylated form, via the MH1 and MH2 domains) with RANBP3 (via its C-terminal R domain); the interaction results in the export of dephosphorylated SMAD3 out of the nucleus and termination of the TGF-beta signaling. Interacts with NEDD4L in response to TGF-beta. Interacts with WWP1, AIP1 and HGS. Interacts with PML. Interacts with PDPK1 (via PH domain). Interacts with DAB2; the interactions are enhanced upon TGF-beta stimulation. Interacts with USP15. Interacts with PPP5C. Interacts with LDLRAD4 (via the SMAD interaction motif). Interacts (via MH2 domain) with PMEPA1 (via the SMAD interaction motif). Interacts with ZFHX3 (By similarity). Interacts with ZNF451. Identified in a complex that contains at least ZNF451, SMAD2, SMAD3 and SMAD4 (By similarity). Interacts weakly with ZNF8 (PubMed:12370310). Interacts (when phosphorylated) with RNF111; RNF111 acts as an enhancer of the transcriptional responses by mediating ubiquitination and degradation of SMAD2 inhibitors (PubMed:17341133). {ECO:0000250|UniProtKB:Q15796, ECO:0000269|PubMed:10681527, ECO:0000269|PubMed:11094085, ECO:0000269|PubMed:12370310, ECO:0000269|PubMed:15221015, ECO:0000269|PubMed:15356634, ECO:0000269|PubMed:15496141, ECO:0000269|PubMed:17341133, ECO:0000269|PubMed:22781750}. +P40694 SMBP2_MOUSE DNA-binding protein SMUBP-2 (EC 3.6.4.12) (EC 3.6.4.13) (ATP-dependent helicase IGHMBP2) (Cardiac transcription factor 1) (CATF1) (Immunoglobulin mu-binding protein 2) 993 109,466 Chain (1); Compositional bias (4); Domain (1); Initiator methionine (1); Modified residue (3); Motif (1); Nucleotide binding (1); Region (1); Zinc finger (1) FUNCTION: 5' to 3' helicase that unwinds RNA and DNA duplices in an ATP-dependent reaction. Acts as a transcription regulator. Required for the transcriptional activation of the flounder liver-type antifreeze protein gene. Exhibits strong binding specificity to the enhancer element B of the flounder antifreeze protein gene intron. Binds to the insulin II gene RIPE3B enhancer region (By similarity). May be involved in translation. DNA-binding protein specific to 5'-phosphorylated single-stranded guanine-rich sequence related to the immunoglobulin mu chain switch region. Preferentially binds to the 5'-GGGCT-3' motif. Interacts with tRNA-Tyr. {ECO:0000250, ECO:0000269|PubMed:19158098, ECO:0000269|PubMed:19299493}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cell projection, axon. Note=Colocalizes with the translation initiation factor EIF4G2. SUBUNIT: Homooligomer (By similarity). Interacts with RUVBL1, RUVBL2, GTF3C1 and ABT1 (By similarity). Is part of large cytosolic ribonucleoprotein complexes (Probable). Associates with the ribosomes. {ECO:0000250, ECO:0000269|PubMed:19158098, ECO:0000305}. TISSUE SPECIFICITY: In all tissues examined. +Q99PE5 SMIM3_MOUSE Small integral membrane protein 3 (NGF-induced differentiation clone 67 protein) (Small membrane protein NID67) 60 6,526 Chain (1); Sequence conflict (1); Site (1); Transmembrane (1) TRANSMEM 20 40 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q8R191 SNG3_MOUSE Synaptogyrin-3 229 24,561 Chain (1); Domain (1); Modified residue (1); Sequence conflict (1); Transmembrane (4) TRANSMEM 30 50 Helical. {ECO:0000255}.; TRANSMEM 70 90 Helical. {ECO:0000255}.; TRANSMEM 105 125 Helical. {ECO:0000255}.; TRANSMEM 148 168 Helical. {ECO:0000255}. FUNCTION: May play a role in regulated exocytosis (PubMed:10383386). May indirectly regulate the activity of the plasma membrane dopamine transporter SLC6A3 and thereby regulate dopamine transport back from the synaptic cleft into the presynaptic terminal (PubMed:19357284). {ECO:0000269|PubMed:10383386, ECO:0000269|PubMed:19357284}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:14755516, ECO:0000269|PubMed:19357284}; Multi-pass membrane protein {ECO:0000255}. Cell junction, synapse {ECO:0000269|PubMed:14755516}. Note=Found at the neuromuscular synapses. {ECO:0000269|PubMed:14755516}. SUBUNIT: Interacts (via N-terminus) with SLC6A3 (via N-terminus) (PubMed:19357284). May interact with VMAT2 (PubMed:19357284). {ECO:0000269|PubMed:19357284}. TISSUE SPECIFICITY: Specifically expressed in brain. Found in the brain across the dorsal and ventral corpus striatum as well as in the cortex. {ECO:0000269|PubMed:10383386, ECO:0000269|PubMed:19357284}. +Q6P5C5 SMUG1_MOUSE Single-strand selective monofunctional uracil DNA glycosylase (EC 3.2.2.-) 279 30,654 Binding site (4); Chain (1); Region (1); Sequence conflict (1) FUNCTION: Recognizes base lesions in the genome and initiates base excision DNA repair. Acts as a monofunctional DNA glycosylase specific for uracil (U) residues in DNA with a preference for single-stranded DNA substrates. The activity is greater toward mismatches (U/G) compared to matches (U/A). Excises uracil (U), 5-formyluracil (fU) and uracil derivatives bearing an oxidized group at C5 [5-hydroxyuracil (hoU) and 5-hydroxymethyluracil (hmU)] in ssDNA and dsDNA, but not analogous cytosine derivatives (5-hydroxycytosine and 5-formylcytosine), nor other oxidized bases. The activity is damage-specific and salt-dependent. The substrate preference is the following: ssDNA > dsDNA (G pair) = dsDNA (A pair) at low salt concentration, and dsDNA (G pair) > dsDNA (A pair) > ssDNA at high salt concentration. {ECO:0000250|UniProtKB:Q53HV7}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q53HV7}. +Q8C0X8 SMKX_MOUSE Sperm motility kinase X (EC 2.7.11.1) 640 71,931 Active site (1); Binding site (1); Chain (1); Domain (2); Nucleotide binding (1) FUNCTION: May play a role in sperm motility, especially in the regulation of flagellar function. {ECO:0000250}. +Q9DB05 SNAA_MOUSE Alpha-soluble NSF attachment protein (SNAP-alpha) (N-ethylmaleimide-sensitive factor attachment protein alpha) 295 33,190 Chain (1); Modified residue (4) FUNCTION: Required for vesicular transport between the endoplasmic reticulum and the Golgi apparatus. Together with GNA12 promotes CDH5 localization to plasma membrane. {ECO:0000250|UniProtKB:P54920}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P54920}; Peripheral membrane protein {ECO:0000250|UniProtKB:P54920}. SUBUNIT: Interacts with PRKCABP, and disrupts the interaction between GRIA2 and PRKCABP, leading to the internalization of GRIA2 (By similarity). Found in a complex with VAMP8 (By similarity). Component of a SNARE-like complex that contains at least ZW10, USE1L, RINT1, STX18 and NAPA/SNAP-alpha (By similarity). Interacts with VTI1A (PubMed:9705316). Interacts with STX12 (By similarity). Interacts with GNA12 (via N-terminus); the interaction promotes CDH5 localization to plasma membrane (By similarity). {ECO:0000250|UniProtKB:P54920, ECO:0000250|UniProtKB:P54921, ECO:0000269|PubMed:9705316}. +Q6JHY2 SMGC_MOUSE Submandibular gland protein C 733 74,383 Alternative sequence (4); Chain (1); Compositional bias (1); Erroneous initiation (1); Glycosylation (10); Sequence conflict (5); Signal peptide (1) PTM: N-glycosylated. {ECO:0000269|PubMed:15256252}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Detected in terminal tubule cells of the submandibular gland (at protein level). Expressed in submandibular salivary glands of 3-day-old males but not adults. Expression in adult submandibular glands is restricted to females. Isoform 5 is expressed in both 3-day-old and adult sublingual glands. {ECO:0000269|PubMed:15256252, ECO:0000269|PubMed:15340121}. +O35718 SOCS3_MOUSE Suppressor of cytokine signaling 3 (SOCS-3) (Cytokine-inducible SH2 protein 3) (CIS-3) (Protein EF-10) 225 24,776 Beta strand (9); Chain (1); Domain (2); Helix (5); Mutagenesis (6); Region (2) Protein modification; protein ubiquitination. FUNCTION: SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. SOCS3 is involved in negative regulation of cytokines that signal through the JAK/STAT pathway. Inhibits cytokine signal transduction by binding to tyrosine kinase receptors including gp130, LIF, erythropoietin, insulin, IL12, GCSF and leptin receptors. Binding to JAK2 inhibits its kinase activity. Suppresses fetal liver erythropoiesis. Regulates onset and maintenance of allergic responses mediated by T-helper type 2 cells. Regulates IL-6 signaling in vivo. Probable substrate-recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). Seems to recognize IL6ST. {ECO:0000250, ECO:0000269|PubMed:10490101, ECO:0000269|PubMed:10821852, ECO:0000269|PubMed:12754505, ECO:0000269|PubMed:12847520, ECO:0000269|PubMed:9889194}. PTM: Phosphorylated on tyrosine residues after stimulation by the cytokines, IL-2, EPO or IGF1. {ECO:0000250}. SUBUNIT: Interacts with multiple activated proteins of the tyrosine kinase signaling pathway including IGF1 receptor, insulin receptor and JAK2. Binding to JAK2 is mediated through the KIR and SH2 domains to a phosphorylated tyrosine residue within the JAK2 JH1 domain (By similarity). Binds specific activated tyrosine residues of the leptin, EPO, IL12, GSCF and gp130 receptors (PubMed:10882725). Interaction with CSNK1E stabilizes SOCS3 protein (By similarity). Component of the probable ECS(SOCS3) E3 ubiquitin-protein ligase complex which contains CUL5, RNF7/RBX2, elongin BC complex and SOCS3 (By similarity). Interacts with CUL5, RNF7, ELOB and ELOC (By similarity). Interacts with FGFR3 (By similarity). Interacts with INSR (PubMed:10821852). Interacts with BCL10; this interaction may interfere with BCL10-binding with PELI2 (PubMed:15213237). Interacts with NOD2 (via CARD domain); the interaction promotes NOD2 degradation (PubMed:23019338). {ECO:0000250|UniProtKB:O14543, ECO:0000269|PubMed:10821852, ECO:0000269|PubMed:10882725, ECO:0000269|PubMed:15213237, ECO:0000269|PubMed:16905102, ECO:0000269|PubMed:23019338}. DOMAIN: The ESS and SH2 domains are required for JAK phosphotyrosine binding. Further interaction with the KIR domain is necessary for signal and kinase inhibition.; DOMAIN: The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin ligase complexes. {ECO:0000250}. TISSUE SPECIFICITY: Low expression in lung, spleen and thymus. Expressed in Th2 but not TH1 cells. {ECO:0000269|PubMed:12242343}. +E1U8D0 SOGA1_MOUSE Protein SOGA1 (SOGA family member 1) (Suppressor of glucose by autophagy) (Suppressor of glucose, autophagy-associated protein 1) [Cleaved into: N-terminal form; C-terminal 80 kDa form (80-kDa SOGA fragment)] 1418 159,186 Chain (3); Coiled coil (6); Erroneous initiation (2); Modified residue (2); Site (1) FUNCTION: Regulates autophagy by playing a role in the reduction of glucose production in an adiponectin- and insulin-dependent manner. {ECO:0000269|PubMed:20813965}. PTM: Proteolytically cleaved into a C-terminal SOGA 25 kDa form that is detected in plasma (By similarity). Proteolytically cleaved in primary hepatocytes into a C-terminal SOGA 80 kDa form. {ECO:0000250, ECO:0000269|PubMed:20813965}. SUBCELLULAR LOCATION: C-terminal 80 kDa form: Secreted. Note=Secreted in primary hepatocyte-conditioned media. SUBUNIT: The C-terminal SOGA 25 kDa form occurs as a monomer. {ECO:0000305|PubMed:20813965}. TISSUE SPECIFICITY: Expressed in liver (at protein level). {ECO:0000269|PubMed:20813965}. +Q7M715 TR117_MOUSE Taste receptor type 2 member 117 (T2R117) (mT2R54) 330 38,528 Chain (1); Glycosylation (2); Topological domain (8); Transmembrane (7) TRANSMEM 17 37 Helical; Name=1. {ECO:0000255}.; TRANSMEM 54 74 Helical; Name=2. {ECO:0000255}.; TRANSMEM 96 116 Helical; Name=3. {ECO:0000255}.; TRANSMEM 136 156 Helical; Name=4. {ECO:0000255}.; TRANSMEM 191 211 Helical; Name=5. {ECO:0000255}.; TRANSMEM 240 260 Helical; Name=6. {ECO:0000255}.; TRANSMEM 270 290 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 16 Extracellular. {ECO:0000255}.; TOPO_DOM 38 53 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 75 95 Extracellular. {ECO:0000255}.; TOPO_DOM 117 135 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 157 190 Extracellular. {ECO:0000255}.; TOPO_DOM 212 239 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 261 269 Extracellular. {ECO:0000255}.; TOPO_DOM 291 330 Cytoplasmic. {ECO:0000255}. FUNCTION: Putative taste receptor which may play a role in the perception of bitterness. {ECO:0000305}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q7M721 TR120_MOUSE Taste receptor type 2 member 120 (T2R120) (mT2R47) 295 33,594 Chain (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 6 26 Helical; Name=1. {ECO:0000255}.; TRANSMEM 46 66 Helical; Name=2. {ECO:0000255}.; TRANSMEM 81 101 Helical; Name=3. {ECO:0000255}.; TRANSMEM 128 148 Helical; Name=4. {ECO:0000255}.; TRANSMEM 178 198 Helical; Name=5. {ECO:0000255}.; TRANSMEM 229 249 Helical; Name=6. {ECO:0000255}.; TRANSMEM 256 276 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 5 Extracellular. {ECO:0000255}.; TOPO_DOM 27 45 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 67 80 Extracellular. {ECO:0000255}.; TOPO_DOM 102 127 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 149 177 Extracellular. {ECO:0000255}.; TOPO_DOM 199 228 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 250 255 Extracellular. {ECO:0000255}.; TOPO_DOM 277 295 Cytoplasmic. {ECO:0000255}. FUNCTION: Putative taste receptor which may play a role in the perception of bitterness. {ECO:0000305}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +P59528 TR123_MOUSE Taste receptor type 2 member 123 (T2R123) (STC9-2) (Taste receptor type 2 member 23) (T2R23) (mT2R55) 333 38,032 Chain (1); Glycosylation (4); Sequence conflict (10); Topological domain (8); Transmembrane (7) TRANSMEM 14 34 Helical; Name=1. {ECO:0000255}.; TRANSMEM 61 81 Helical; Name=2. {ECO:0000255}.; TRANSMEM 91 111 Helical; Name=3. {ECO:0000255}.; TRANSMEM 135 155 Helical; Name=4. {ECO:0000255}.; TRANSMEM 206 226 Helical; Name=5. {ECO:0000255}.; TRANSMEM 254 274 Helical; Name=6. {ECO:0000255}.; TRANSMEM 282 302 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 13 Extracellular. {ECO:0000255}.; TOPO_DOM 35 60 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 82 90 Extracellular. {ECO:0000255}.; TOPO_DOM 112 134 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 156 205 Extracellular. {ECO:0000255}.; TOPO_DOM 227 253 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 275 281 Extracellular. {ECO:0000255}.; TOPO_DOM 303 333 Cytoplasmic. {ECO:0000255}. FUNCTION: Gustducin-coupled receptor implicated in the perception of bitter compounds in the oral cavity and the gastrointestinal tract. Signals through PLCB2 and the calcium-regulated cation channel TRPM5 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed in subsets of taste receptor cells of the tongue and palate epithelium and exclusively in gustducin-positive cells. Expressed in the duodenum, antrum and fundus (part of the stomach). {ECO:0000269|PubMed:11854532}. +Q9WV80 SNX1_MOUSE Sorting nexin-1 522 58,952 Binding site (4); Chain (1); Domain (2); Modified residue (9); Region (1); Sequence conflict (5) FUNCTION: Involved in several stages of intracellular trafficking. Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)) or phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Acts in part as component of the retromer membrane-deforming SNX-BAR subcomplex. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX-BAR subcomplex functions to deform the donor membrane into a tubular profile called endosome-to-TGN transport carrier (ETC). Can sense membrane curvature and has in vitro vesicle-to-membrane remodeling activity. Involved in retrograde endosome-to-TGN transport of lysosomal enzyme receptors (IGF2R, M6PR and SORT1). Plays a role in targeting ligand-activated EGFR to the lysosomes for degradation after endocytosis from the cell surface and release from the Golgi. Involvement in retromer-independent endocytic trafficking of P2RY1 and lysosomal degradation of protease-activated receptor-1/F2R. Promotes KALRN- and RHOG-dependent but retromer-independent membrane remodeling such as lamellipodium formation; the function is dependent on GEF activity of KALRN. Required for endocytosis of DRD5 upon agonist stimulation but not for basal receptor trafficking (By similarity). {ECO:0000250|UniProtKB:Q13596}. SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250|UniProtKB:Q13596}; Peripheral membrane protein; Cytoplasmic side. Golgi apparatus, trans-Golgi network membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Early endosome membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q13596}. Note=Enriched on tubular elements of the early endosome membrane. Binds preferentially to highly curved membranes enriched in phosphatidylinositol 3-phosphate (PtdIns(3P)) or phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Colocalized with SORT1 to tubular endosomal membrane structures called endosome-to-TGN transport carriers (ETCs) which are budding from early endosome vacuoles just before maturing into late endosome vacuoles. Colocalized with F-actin at the leading edge of lamellipodia in a KALRN-dependent manner. {ECO:0000250|UniProtKB:Q13596}. SUBUNIT: Predominantly forms heterodimers with BAR domain-containing sorting nexins SNX5, SNX6 and SNX32 (By similarity). Can self-associate to form homodimers (PubMed:11726276). The heterodimers are proposed to self-assemble into helical arrays on the membrane to stabilize and expand local membrane curvature underlying endosomal tubule formation. Thought to be a component of the originally described retromer complex (also called SNX-BAR retromer) which is a pentamer containing the heterotrimeric retromer cargo-selective complex (CSC), also described as vacuolar protein sorting subcomplex (VPS) and a heterodimeric membrane-deforming subcomplex formed between SNX1 or SNX2 and SNX5 or SNX6 (also called SNX-BAR subcomplex); the respective CSC and SNX-BAR subcomplexes associate with low affinity. Interacts with SNX5, SNX6, SNX32, VPS26A, VPS29, VPS35, DRD5, DENND5A, KALRN, RHOG (GDP-bound form). The interaction with SNX2 is reported controversially. Interacts with DNAJC13; prevented by presence of HGS. Interacts with HGS (By similarity). {ECO:0000250|UniProtKB:Q13596, ECO:0000250|UniProtKB:Q99N27}. DOMAIN: The BAR domain is able to sense membrane curvature upon dimerization. Membrane remodeling seems to implicate insertion of a N-terminal amphipatric helix (AH) in the membrane (By similarity). {ECO:0000250|UniProtKB:Q13596}. +Q8K136 SCNM1_MOUSE Sodium channel modifier 1 229 25,823 Alternative sequence (1); Chain (1); Cross-link (1); Modified residue (3); Motif (1); Natural variant (1); Region (1); Zinc finger (1) FUNCTION: Plays a role in alternative splicing of pre-mRNAs, possibly by contributing to the selection of non-consensus donor sites. {ECO:0000269|PubMed:12920299, ECO:0000269|PubMed:17656373}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:17656373}. Nucleus speckle {ECO:0000269|PubMed:17656373}. Note=Colocalizes with LUC7L2 and SNRNP70 in nuclear speckles. {ECO:0000269|PubMed:17656373}. SUBUNIT: Interacts with spliceosomal Sm proteins (By similarity). Interacts with LUC7L2 and SNRNP70, which suggests a role as a spliceosome component. {ECO:0000250|UniProtKB:Q9BWG6, ECO:0000269|PubMed:17656373}. DISEASE: Note=Allele R187X is a disease susceptibility variant, which modifies the severity of the disease jolting mutant (medjo) caused by defects in Scn8a. It reduces the abundance of correctly spliced Scn8a transcripts below the threshold for survival thereby converting a chronic movement disorder into a lethal neurological disease. {ECO:0000269|PubMed:12920299}. +P18828 SDC1_MOUSE Syndecan-1 (SYND1) (CD antigen CD138) 311 32,905 Alternative sequence (1); Chain (1); Glycosylation (6); Modified residue (1); Sequence conflict (1); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 256 276 Helical. {ECO:0000255}. TOPO_DOM 23 255 Extracellular. {ECO:0000255}.; TOPO_DOM 277 311 Cytoplasmic. {ECO:0000255}. FUNCTION: Cell surface proteoglycan that bears both heparan sulfate and chondroitin sulfate and that links the cytoskeleton to the interstitial matrix. Regulates exosome biogenesis in concert with SDCBP and PDCD6IP. {ECO:0000250|UniProtKB:P18827}. PTM: Shedding is enhanced by a number of factors such as heparanase, thrombin or EGF. Also by stress and wound healing. PMA-mediated shedding is inhibited by TIMP3. {ECO:0000269|PubMed:10684261}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}. Secreted {ECO:0000269|PubMed:10684261}. Secreted, exosome {ECO:0000250|UniProtKB:P18827}. Note=Shedding of the ectodomain produces a soluble form. {ECO:0000269|PubMed:10684261}. SUBUNIT: Interacts with CDCP1 (By similarity). Interacts (via C-terminus) with TIAM1 (via PDZ domain) (PubMed:20361982). {ECO:0000250|UniProtKB:P18827, ECO:0000269|PubMed:20361982}. +O08992 SDCB1_MOUSE Syntenin-1 (Scaffold protein Pbp1) (Syndecan-binding protein 1) 299 32,379 Chain (1); Domain (2); Initiator methionine (1); Modified residue (3); Motif (3); Mutagenesis (3); Region (2) FUNCTION: Multifunctional adapter protein involved in diverse array of functions including trafficking of transmembrane proteins, neuro and immunomodulation, exosome biogenesis, and tumorigenesis. Positively regulates TGFB1-mediated SMAD2/3 activation and TGFB1-induced epithelial-to-mesenchymal transition (EMT) and cell migration in various cell types. May increase TGFB1 signaling by enhancing cell-surface expression of TGFR1 by preventing the interaction between TGFR1 and CAV1 and subsequent CAV1-dependent internalization and degradation of TGFR1. In concert with SDC1/4 and PDCD6IP, regulates exosome biogenesis (By similarity). Regulates migration, growth, proliferation, and cell cycle progression in a variety of cancer types (PubMed:26539120). In adherens junctions may function to couple syndecans to cytoskeletal proteins or signaling components. Seems to couple transcription factor SOX4 to the IL-5 receptor (IL5RA). May also play a role in vesicular trafficking. Seems to be required for the targeting of TGFA to the cell surface in the early secretory pathway (By similarity). {ECO:0000250|UniProtKB:O00560, ECO:0000269|PubMed:26539120}. PTM: Phosphorylated on tyrosine residues. {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000250|UniProtKB:O00560}. Cell junction, adherens junction {ECO:0000250|UniProtKB:O00560}. Cell membrane {ECO:0000250|UniProtKB:O00560}; Peripheral membrane protein {ECO:0000250|UniProtKB:O00560}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O00560}; Peripheral membrane protein {ECO:0000250|UniProtKB:O00560}. Nucleus {ECO:0000250|UniProtKB:O00560}. Melanosome {ECO:0000250|UniProtKB:O00560}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:O00560}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O00560}. Secreted, exosome {ECO:0000250|UniProtKB:O00560}. Membrane raft {ECO:0000250|UniProtKB:O00560}. Note=Mainly membrane-associated. Localized to adherens junctions, focal adhesions and endoplasmic reticulum. Colocalized with actin stress fibers. Also found in the nucleus. Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Associated to the plasma membrane in the presence of FZD7 and phosphatidylinositol 4,5-bisphosphate (PIP2) (By similarity). {ECO:0000250|UniProtKB:O00560}. SUBUNIT: Monomer and homodimer. Interacts with SDC1, SDC2, SDC3, SDC4, NRXN2, EPHA7, EPHB1, NF2 isoform 1, TGFA, IL5RA, NFASC, SDCBP2 and PTPRJ (By similarity). Interacts with PDCD6IP (PubMed:22660413). Forms a complex with PDCD6IP and SDC2 (By similarity). Interacts (via C-terminus) with TGFBR1 (By similarity). Binds to FZD7; this interaction is increased by inositol trisphosphate (IP3) (By similarity). Interacts with SMO (PubMed:25644602). {ECO:0000250|UniProtKB:O00560, ECO:0000250|UniProtKB:Q9JI92, ECO:0000269|PubMed:22660413, ECO:0000269|PubMed:25644602}. +P62342 SELT_MOUSE Thioredoxin reductase-like selenoprotein T (SelT) (EC 1.8.1.9) 195 22,292 Chain (1); Cross-link (1); Erroneous initiation (5); Non-standard residue (1); Signal peptide (1); Transmembrane (1) TRANSMEM 85 103 Helical. {ECO:0000255}. FUNCTION: Selenoprotein with thioredoxin reductase-like oxidoreductase activity (By similarity). Protects dopaminergic neurons against oxidative stress ans cell death (PubMed:26866473). Involved in ADCYAP1/PACAP-induced calcium mobilization and neuroendocrine secretion (By similarity). Plays a role in fibroblast anchorage and redox regulation (PubMed:19935881). In gastric smooth muscle, modulates the contraction processes through the regulation of calcium release and MYLK activation (By similarity). In pancreatic islets, involved in the control of glucose homeostasis, contributes to prolonged ADCYAP1/PACAP-induced insulin secretion (PubMed:23913443). {ECO:0000250|UniProtKB:Q1H5H1, ECO:0000269|PubMed:19935881, ECO:0000269|PubMed:23913443, ECO:0000269|PubMed:26866473}. PTM: May contain a selenide-sulfide bond between Cys-46 and Sec-49. This bond is speculated to serve as redox-active pair (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23913443}; Single-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Ubiquitous. Highly expressed in the endocrine pancreas (PubMed:23913443). Expressed at low levels in the adult brain (PubMed:26866473). {ECO:0000269|PubMed:23913443, ECO:0000269|PubMed:26866473}. +Q8C2A2 SEN54_MOUSE tRNA-splicing endonuclease subunit Sen54 (tRNA-intron endonuclease Sen54) 525 59,083 Alternative sequence (1); Chain (1); Modified residue (3); Sequence conflict (1) FUNCTION: Non-catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5' and 3' splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and 5'-OH termini. There are no conserved sequences at the splice sites, but the intron is invariably located at the same site in the gene, placing the splice sites an invariant distance from the constant structural features of the tRNA body. The tRNA splicing endonuclease is also involved in mRNA processing via its association with pre-mRNA 3'-end processing factors, establishing a link between pre-tRNA splicing and pre-mRNA 3'-end formation, suggesting that the endonuclease subunits function in multiple RNA-processing events (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Nucleus, nucleolus {ECO:0000305}. Note=May be transiently localized in the nucleolus. {ECO:0000305}. SUBUNIT: tRNA splicing endonuclease is a heterotetramer composed of TSEN2, TSEN15, TSEN34/LENG5 and TSEN54. tRNA splicing endonuclease complex also contains proteins of the pre-mRNA 3'-end processing machinery such as CLP1, CPSF1, CPSF4 and CSTF2 (By similarity). {ECO:0000250}. +Q8BH34 SEM3D_MOUSE Semaphorin-3D 777 89,549 Chain (1); Compositional bias (1); Disulfide bond (6); Domain (3); Glycosylation (3); Signal peptide (1) FUNCTION: Induces the collapse and paralysis of neuronal growth cones. Could potentially act as repulsive cues toward specific neuronal populations. Binds to neuropilin (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. DOMAIN: Strong binding to neuropilin is mediated by the carboxy third of the protein. +P70275 SEM3E_MOUSE Semaphorin-3E (Semaphorin-H) (Sema H) 775 89,543 Chain (1); Compositional bias (1); Disulfide bond (6); Domain (2); Glycosylation (5); Sequence conflict (1); Signal peptide (1) FUNCTION: Plays an important role in signaling via the cell surface receptor PLXND1. Mediates reorganization of the actin cytoskeleton, leading to the retraction of cell projections. Promotes focal adhesion disassembly and inhibits adhesion of endothelial cells to the extracellular matrix. Regulates angiogenesis, both during embryogenesis and after birth. Can down-regulate sprouting angiogenesis. Required for normal vascular patterning during embryogenesis. Plays an important role in ensuring the specificity of synapse formation. {ECO:0000269|PubMed:15550623, ECO:0000269|PubMed:19421194, ECO:0000269|PubMed:20385769, ECO:0000269|PubMed:22179111}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Interacts with PLXND1. {ECO:0000269|PubMed:15550623, ECO:0000269|PubMed:20385769}. TISSUE SPECIFICITY: Detected in neurons in the thalamus. Detected in embryonic vasculature. Developing lungs, developing skeletal elements and ventral horns of the developing neural tube. Correlates positively with tumor progression. {ECO:0000269|PubMed:15550623, ECO:0000269|PubMed:22179111}. +Q9D2Z4 SENP8_MOUSE Sentrin-specific protease 8 (EC 3.4.22.-) (Deneddylase-1) (NEDD8-specific protease 1) (Sentrin/SUMO-specific protease SENP8) 221 25,057 Active site (3); Chain (1); Erroneous initiation (1); Modified residue (1); Region (1) FUNCTION: Protease that catalyzes two essential functions in the NEDD8 pathway: processing of full-length NEDD8 to its mature form and deconjugation of NEDD8 from targeted proteins such as cullins or p53. {ECO:0000269|PubMed:12759362}. +Q9R1T4 SEPT6_MOUSE Septin-6 434 49,620 Alternative sequence (2); Binding site (3); Chain (1); Coiled coil (1); Domain (1); Erroneous gene model prediction (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (5); Nucleotide binding (2); Region (3); Sequence conflict (8) FUNCTION: Filament-forming cytoskeletal GTPase. Required for normal organization of the actin cytoskeleton. Involved in cytokinesis. Forms a filamentous structure with SEPT12, SEPT6, SEPT2 and probably SEPT4 at the sperm annulus which is required for the structural integrity and motility of the sperm tail during postmeiotic differentiation. {ECO:0000250|UniProtKB:Q14141}. SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton, spindle. Chromosome, centromere, kinetochore {ECO:0000250}. Cleavage furrow {ECO:0000250}. Midbody {ECO:0000250}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q14141}. Note=In metaphase cells, localized within the microtubule spindle. At the metaphase plate, in close apposition to the kinetochores of the congressed chromosomes. In cells undergoing cytokinesis, localized to the midbody, the ingressing cleavage furrow, and the central spindle. Found in the sperm annulus (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q14141}. SUBUNIT: Septins polymerize into heterooligomeric protein complexes that form filaments, and associate with cellular membranes, actin filaments and microtubules. GTPase activity is required for filament formation. Filaments are assembled from asymmetrical heterotrimers, composed of SEPT2, SEPT6 and SEPT7 that associate head-to-head to form a hexameric unit. Within the trimer, directly interacts with SEPT2 and SEPT7. Also interacts with SEPT9 and SEPT12. Interaction with SEPT12 alters filament structure. Component of a septin core octomeric complex consisting of SEPT12, SEPT7, SEPT6 and SEPT2 or SEPT4 in the order 12-7-6-2-2-6-7-12 or 12-7-6-4-4-6-7-12 and located in the sperm annulus. Interacts with SOCS7. Interacts with HNRNPA1 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q14141}. TISSUE SPECIFICITY: Associated with synaptic vesicles in various brain regions, including glomeruli of the olfactory bulb. {ECO:0000269|PubMed:11064363}. +Q5XJV7 SETD5_MOUSE SET domain-containing protein 5 1441 157,426 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (2); Modified residue (7); Sequence conflict (1) FUNCTION: Probable transcriptional regulator that acts via the formation of large multiprotein complexes that modify and/or remodel the chromatin. Acts as a regulator of histone acetylation during gene transcription. {ECO:0000269|PubMed:27864380}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27864380}. SUBUNIT: Interacts with components of the PAF1 complex (PAF1C) such as LEO1, CTR9 and CDC73 (PubMed:27864380). Interacts with NCOR1 (PubMed:27864380). {ECO:0000269|PubMed:27864380}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:27864380}. +Q9CWY3 SETD6_MOUSE N-lysine methyltransferase SETD6 (EC 2.1.1.-) (SET domain-containing protein 6) 473 52,960 Chain (1); Domain (1); Frameshift (1); Modified residue (2); Sequence conflict (1) FUNCTION: Protein-lysine N-methyltransferase. Monomethylates 'Lys-310' of the RELA subunit of NF-kappa-B complex, leading to down-regulate NF-kappa-B transcription factor activity. Monomethylates 'Lys-8' of H2AZ (H2AZK8me1) (By similarity). Required for the maintenance of embryonic stem cell self-renewal (PubMed:23324626). {ECO:0000250|UniProtKB:Q8TBK2, ECO:0000269|PubMed:23324626}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8TBK2}. +Q64213 SF01_MOUSE Splicing factor 1 (CW17) (Mammalian branch point-binding protein) (BBP) (mBBP) (Transcription factor ZFM1) (mZFM) (Zinc finger gene in MEN1 locus) (Zinc finger protein 162) 653 70,403 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (1); Initiator methionine (1); Modified residue (7); Motif (1); Sequence conflict (6); Zinc finger (1) FUNCTION: Necessary for the ATP-dependent first step of spliceosome assembly. Binds to the intron branch point sequence (BPS) 5'-UACUAAC-3' of the pre-mRNA. May act as transcription repressor (By similarity). {ECO:0000250}. PTM: Phosphorylation on Ser-20 interferes with U2AF2 binding and spliceosome assembly. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Binds U2AF2. Interacts with U1 snRNA. Interacts with RBM17. Binds EWSR1, FUS and TAF15 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Detected at intermediate levels in spleen. Lower levels in heart, kidney, brain, liver, testis, bone marrow, adrenal gland, lymph nodes, pancreas and thymus. +Q8C267 SETB2_MOUSE Histone-lysine N-methyltransferase SETDB2 (EC 2.1.1.43) (SET domain bifurcated 2) 713 80,636 Alternative sequence (3); Binding site (1); Chain (1); Domain (3); Metal binding (16); Region (2) FUNCTION: Histone methyltransferase involved in left-right axis specification in early development and mitosis. Specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). H3K9me3 is a specific tag for epigenetic transcriptional repression that recruits HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Contributes to H3K9me3 in both the interspersed repetitive elements and centromere-associated repeats. Plays a role in chromosome condensation and segregation during mitosis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}. DOMAIN: In the pre-SET domain, Cys residues bind 3 zinc ions that are arranged in a triangular cluster; some of these Cys residues contribute to the binding of two zinc ions within the cluster. {ECO:0000250}. +E9Q5F9 SETD2_MOUSE Histone-lysine N-methyltransferase SETD2 (EC 2.1.1.43) (Lysine N-methyltransferase 3A) (Protein-lysine N-methyltransferase SETD2) (EC 2.1.1.-) (SET domain-containing protein 2) 2537 285,663 Alternative sequence (1); Binding site (5); Chain (1); Coiled coil (1); Compositional bias (4); Cross-link (3); Domain (4); Metal binding (12); Modified residue (32); Region (9) FUNCTION: Histone methyltransferase that specifically trimethylates 'Lys-36' of histone H3 (H3K36me3) using dimethylated 'Lys-36' (H3K36me2) as substrate (PubMed:18157086, PubMed:20133625). Represents the main enzyme generating H3K36me3, a specific tag for epigenetic transcriptional activation (PubMed:18157086, PubMed:20133625). Plays a role in chromatin structure modulation during elongation by coordinating recruitment of the FACT complex and by interacting with hyperphosphorylated POLR2A (By similarity). Acts as a key regulator of DNA mismatch repair in G1 and early S phase by generating H3K36me3, a mark required to recruit MSH6 subunit of the MutS alpha complex: early recruitment of the MutS alpha complex to chromatin to be replicated allows a quick identification of mismatch DNA to initiate the mismatch repair reaction (By similarity). Required for DNA double-strand break repair in response to DNA damage: acts by mediating formation of H3K36me3, promoting recruitment of RAD51 and DNA repair via homologous recombination (HR) (By similarity). Acts as a tumor suppressor (By similarity). H3K36me3 also plays an essential role in the maintenance of a heterochromatic state, by recruiting DNA methyltransferase DNMT3A (By similarity). H3K36me3 is also enhanced in intron-containing genes, suggesting that SETD2 recruitment is enhanced by splicing and that splicing is coupled to recruitment of elongating RNA polymerase (By similarity). Required during angiogenesis (PubMed:20133625). Required for endoderm development by promoting embryonic stem cell differentiation toward endoderm: acts by mediating formation of H3K36me3 in distal promoter regions of FGFR3, leading to regulate transcription initiation of FGFR3 (PubMed:25242323). In addition to histones, also mediates methylation of other proteins, such as tubulins and STAT1 (PubMed:27518565). Trimethylates 'Lys-40' of alpha-tubulins such as TUBA1B (alpha-TubK40me3); alpha-TubK40me3 is required for normal mitosis and cytokinesis and may be a specific tag in cytoskeletal remodeling (PubMed:27518565). Involved in interferon-alpha-induced antiviral defense by mediating both monomethylation of STAT1 at 'Lys-525' and catalyzing H3K36me3 on promoters of some interferon-stimulated genes (ISGs) to activate gene transcription (By similarity). {ECO:0000250|UniProtKB:Q9BYW2, ECO:0000269|PubMed:18157086, ECO:0000269|PubMed:20133625, ECO:0000269|PubMed:25242323, ECO:0000269|PubMed:27518565}. PTM: May be automethylated. {ECO:0000250|UniProtKB:Q9BYW2}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18157086}. Chromosome {ECO:0000269|PubMed:18157086}. SUBUNIT: Specifically interacts with hyperphosphorylated C-terminal domain (CTD) of RNA polymerase II large subunit (POLR2A): binds to CTD heptad repeats doubly phosphorylated on 'Ser-2' and 'Ser-5' of each heptad. Interacts with HTT. Interacts with IWS1. Interacts with p53/TP53; leading to regulate p53/TP53 target genes. Component of a complex with HNRNPL. Interacts with TUBA1A; the interaction is independent on alpha-tubulin acetylation on 'Lys-40'. {ECO:0000250|UniProtKB:Q9BYW2}. DOMAIN: The low charge region mediates the transcriptional activation activity. {ECO:0000250|UniProtKB:Q9BYW2}. +Q8VD57 SFT2B_MOUSE Vesicle transport protein SFT2B (SFT2 domain-containing protein 2) 159 17,499 Chain (1); Modified residue (2); Topological domain (5); Transmembrane (4) TRANSMEM 37 57 Helical; Name=1. {ECO:0000255}.; TRANSMEM 64 84 Helical; Name=2. {ECO:0000255}.; TRANSMEM 99 119 Helical; Name=3. {ECO:0000255}.; TRANSMEM 123 143 Helical; Name=4. {ECO:0000255}. TOPO_DOM 1 36 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 58 63 Lumenal. {ECO:0000255}.; TOPO_DOM 85 98 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 120 122 Lumenal. {ECO:0000255}.; TOPO_DOM 144 159 Cytoplasmic. {ECO:0000255}. FUNCTION: May be involved in fusion of retrograde transport vesicles derived from an endocytic compartment with the Golgi complex. {ECO:0000250|UniProtKB:P38166}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. +Q9CSV6 SFT2C_MOUSE Vesicle transport protein SFT2C (SFT2 domain-containing protein 3) 209 21,581 Chain (1); Frameshift (1); Topological domain (5); Transmembrane (4) TRANSMEM 76 96 Helical; Name=1. {ECO:0000255}.; TRANSMEM 102 122 Helical; Name=2. {ECO:0000255}.; TRANSMEM 140 162 Helical; Name=3. {ECO:0000255}.; TRANSMEM 172 194 Helical; Name=4. {ECO:0000255}. TOPO_DOM 1 75 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 97 101 Lumenal. {ECO:0000255}.; TOPO_DOM 123 139 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 163 171 Lumenal. {ECO:0000255}.; TOPO_DOM 195 209 Cytoplasmic. {ECO:0000255}. FUNCTION: May be involved in fusion of retrograde transport vesicles derived from an endocytic compartment with the Golgi complex. {ECO:0000250|UniProtKB:P38166}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. +Q8QZY9 SF3B4_MOUSE Splicing factor 3B subunit 4 424 44,356 Chain (1); Compositional bias (2); Domain (2); Initiator methionine (1); Modified residue (2) FUNCTION: Involved in pre-mRNA splicing as a component of the splicing factor SF3B complex. SF3B complex is required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA. May also be involved in the assembly of the 'E' complex. SF3B4 has been found in complex 'B' and 'C' as well. Belongs also to the minor U12-dependent spliceosome, which is involved in the splicing of rare class of nuclear pre-mRNA intron. {ECO:0000250|UniProtKB:Q15427}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15427}. SUBUNIT: Component of splicing factor SF3B complex which is composed of at least eight subunits; SF3B1, SF3B2, SF3B3, SF3B4, SF3B5, SF3B6, PHF5A and DDX42. SF3B associates with the splicing factor SF3A and a 12S RNA unit to form the U2 small nuclear ribonucleoproteins complex (U2 snRNP). Interacts directly with SF3B2. Found in a complex with PRMT9, SF3B2 and SF3B4. The SF3B complex composed of SF3B1, SF3B2, SF3B3, SF3B4, SF3B5, SF3B6 and PHF5A interacts with U2AF2. Component of the U11/U12 snRNPs that are part of the U12-type spliceosome. {ECO:0000250|UniProtKB:Q15427}. +Q8BSD5 SHE_MOUSE SH2 domain-containing adapter protein E 492 53,353 Chain (1); Compositional bias (1); Domain (1); Modified residue (1); Sequence conflict (1) TISSUE SPECIFICITY: Expressed in heart, brain, lung and skeletal muscle. {ECO:0000269|PubMed:9315092}. +Q8K2Q9 SHOT1_MOUSE Shootin-1 (Shootin1) 631 71,343 Alternative sequence (2); Chain (1); Coiled coil (1); Compositional bias (1); Erroneous initiation (1); Modified residue (13) FUNCTION: Involved in the generation of internal asymmetric signals required for neuronal polarization and neurite outgrowth (PubMed:23864681). Mediates netrin-1-induced F-actin-substrate coupling or 'clutch engagement' within the axon growth cone through activation of CDC42, RAC1 and PAK1-dependent signaling pathway, thereby converting the F-actin retrograde flow into traction forces, concomitantly with filopodium extension and axon outgrowth. Plays a role in cytoskeletal organization by regulating the subcellular localization of phosphoinositide 3-kinase (PI3K) activity at the axonal growth cone. Plays also a role in regenerative neurite outgrowth (By similarity). In the developing cortex, cooperates with KIF20B to promote both the transition from the multipolar to the bipolar stage and the radial migration of cortical neurons from the ventricular zone toward the superficial layer of the neocortex (PubMed:23864681). Involved in the accumulation of phosphatidylinositol 3,4,5-trisphosphate (PIP3) in the growth cone of primary hippocampal neurons (PubMed:23864681). {ECO:0000250|UniProtKB:A0MZ67, ECO:0000269|PubMed:23864681}. PTM: Phosphorylated on Ser-101 and Ser-249 by PAK1 through a CDC42- and RAC1-dependent signaling pathway, which enhances its association with F-actin retrograde flow in filopodia and lamellipodia of axonal growth cones. Phosphorylation on Ser-101 and Ser-249 is increased by netrin-1. {ECO:0000250|UniProtKB:A0MZ67}. SUBCELLULAR LOCATION: Perikaryon {ECO:0000269|PubMed:23864681}. Cell projection, axon {ECO:0000269|PubMed:23864681}. Cell projection, growth cone {ECO:0000269|PubMed:17030985, ECO:0000269|PubMed:23864681}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:23864681}. Cell projection, filopodium {ECO:0000250|UniProtKB:A0MZ67}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:A0MZ67}. Note=Localizes in multiple growth cones at neurite tips before the neuronal symmetry-breaking step. Accumulates in growth cones of a single nascent axon in a neurite length-dependent manner during the neuronal symmetry-breaking step; when absent from the nascent axon's siblings, probably due to competitive transport, prevents the formation of surplus axons. Transported anterogradely from the soma to the axon growth cone in an actin and myosin-dependent manner and passively diffuses back to the cell bodies. Colocalized with L1CAM in close apposition with actin filaments in filopodia and lamellipodia of axonal growth cones in hippocampal neurons. Exhibits retrograde movements in filopodia and lamellopodia of axonal growth cones (By similarity). Colocalized with KIF20B along microtubules to the tip of the growing cone in primary hippocampal neurons (PubMed:23864681). Recruted to the growth cone of developing axon in a KIF20B- and microtubule-dependent manner (PubMed:23864681). {ECO:0000250|UniProtKB:A0MZ67, ECO:0000269|PubMed:23864681}. SUBUNIT: Interacts with L1CAM; this interaction occurs at axonal growth cones. Interacts with actin filament retrograde flow; this interaction is enhanced in a netrin-1- and PAK1-dependent manner and promotes F-actin-substrate coupling and concomitant formation of traction forces at axonal growth cones. Interacts with RUFY3 (By similarity). Interacts with PFN2 (PubMed:19403918). Interacts (via N-terminus) with KIF20B; this interaction is direct and promotes the association of SHTN1 to microtubules in primary neurons (PubMed:23864681). Associates with microtubule (PubMed:23864681). {ECO:0000250|UniProtKB:A0MZ67, ECO:0000269|PubMed:19403918, ECO:0000269|PubMed:23864681}. DOMAIN: The N-terminus region is necessary for interaction with actin retrograde filament flow and accumulation in neuronal growth cones. {ECO:0000250|UniProtKB:A0MZ67}. TISSUE SPECIFICITY: Expressed in hippocampal neurons (PubMed:17030985). {ECO:0000269|PubMed:17030985}. +Q4ACU6 SHAN3_MOUSE SH3 and multiple ankyrin repeat domains protein 3 (Shank3) (Proline-rich synapse-associated protein 2) (ProSAP2) (SPANK-2) 1730 185,397 Alternative sequence (10); Beta strand (10); Chain (1); Coiled coil (1); Compositional bias (3); Domain (3); Helix (2); Modified residue (32); Motif (1); Region (2); Repeat (6); Turn (1) FUNCTION: Major scaffold postsynaptic density protein which interacts with multiple proteins and complexes to orchestrate the dendritic spine and synapse formation, maturation and maintenance. Interconnects receptors of the postsynaptic membrane including NMDA-type and metabotropic glutamate receptors via complexes with GKAP/PSD-95 and HOMER, respectively, and the actin-based cytoskeleton. Plays a role in the structural and functional organization of the dendritic spine and synaptic junction through the interaction with Arp2/3 and WAVE1 complex as well as the promotion of the F-actin clusters. By way of this control of actin dynamics, participates in the regulation of developing neurons growth cone motility and the NMDA receptor-signaling. Also modulates GRIA1 exocytosis and GRM5/MGLUR5 expression and signaling to control the AMPA and metabotropic glutamate receptor-mediated synaptic transmission and plasticity. May be required at an early stage of synapse formation and be inhibited by IGF1 to promote synapse maturation. {ECO:0000269|PubMed:21423165, ECO:0000269|PubMed:21558424, ECO:0000269|PubMed:23739967, ECO:0000269|PubMed:24153177}. SUBCELLULAR LOCATION: Cytoplasm. Cell junction, synapse. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density. Cell projection, dendritic spine {ECO:0000250}. Note=In neuronal cells, extends into the region subjacent to the postsynaptic density (PSD). SUBUNIT: May homomultimerize via its SAM domain. Interacts with BAIAP2, DBNL and SLC17A7/VGLUT1. Interacts with DLGAP1/GKAP, GRM1/MGLUR1, GRM5/MGLUR5 and LZTS3 C-termini via its PDZ domain. Interacts with ABI1, HOMER1, HOMER2, HOMER3 and CTTN/cortactin SH3 domain. Is part of a complex with DLG4/PSD-95 and DLGAP1/GKAP. Interacts (via PDZ domain) with the GRIA1 subunit of the AMPA receptor (via PDZ-binding motif). Interacts with WASF1 and CYFIP2; the interactions mediate the association of SHANK3 with the WAVE1 complex. Interacts with ARPC2; the interaction probably mediates the association of SHANK3 with the Arp2/3 complex. Interacts (via ANK repeats) with SHARPIN and SPTAN1. Interacts (via PDZ domain) with ARHGAP44 (probably via PDZ-binding motif); the interaction takes place in dendritic spines and promotes GRIA1 exocytosis. Interacts with CAMK2A (By similarity). {ECO:0000250|UniProtKB:Q9BYB0, ECO:0000269|PubMed:16606358, ECO:0000269|PubMed:21558424, ECO:0000269|PubMed:23739967, ECO:0000269|PubMed:24153177}. DOMAIN: In isoform 1, the N-terminal region preceding the ANK repeats interacts with the 6 ANK repeats in an intramolecular manner, thereby restricting access to ligands, such as SHARPIN and SPTAN1. {ECO:0000250}. TISSUE SPECIFICITY: In brain, highly expressed in striatum, thalamus, hippocampus and granule cells of the cerebellum. {ECO:0000269|PubMed:21423165, ECO:0000269|PubMed:21558424, ECO:0000269|PubMed:24153177}. +P54751 SIA4A_MOUSE CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1 (Alpha 2,3-ST 1) (Beta-galactoside alpha-2,3-sialyltransferase 1) (EC 2.4.99.4) (Gal-NAc6S) (Gal-beta-1,3-GalNAc-alpha-2,3-sialyltransferase) (ST3Gal I) (ST3GalI) (ST3GalA.1) (ST3O) (Sialyltransferase 4A) (SIAT4-A) 337 39,073 Binding site (9); Chain (1); Disulfide bond (3); Glycosylation (3); Topological domain (2); Transmembrane (1) TRANSMEM 5 25 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 4 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 26 337 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Responsible for the synthesis of the sequence NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc- found on sugar chains O-linked to Thr or Ser and also as a terminal sequence on certain gangliosides. SIAT4A and SIAT4B sialylate the same acceptor substrates but exhibit different Km values. {ECO:0000269|PubMed:8375377, ECO:0000269|PubMed:9184827}. PTM: The soluble form derives from the membrane form by proteolytic processing. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. Secreted. Note=Membrane-bound form in trans cisternae of Golgi. Secreted into the body fluid. TISSUE SPECIFICITY: Highly expressed in submaxillary gland and to a much lesser extent in liver, lung, kidney, heart and brain. {ECO:0000269|PubMed:8375377}. +C4P6S0 SHTAP_MOUSE Sperm head and tail associated protein 806 86,304 Alternative sequence (1); Chain (1); Compositional bias (1); Region (1) FUNCTION: Plays a role during spermatogenesis. {ECO:0000305}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19686095}. Note=Localized to the peri-acrosomal region of the round spermatids as well as the heads and tails of the elongated spermatids and spermatozoa. Redistributed within the head during sperm capacitation. SUBUNIT: Interacts with CRISP2. {ECO:0000269|PubMed:19686095}. TISSUE SPECIFICITY: Isoforms 3 and 4 are expressed in testis (at protein level). {ECO:0000269|PubMed:19686095}. +P58682 TLR8_MOUSE Toll-like receptor 8 (CD antigen CD288) 1032 119,358 Chain (1); Disulfide bond (5); Domain (1); Glycosylation (21); Repeat (26); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 819 839 Helical. {ECO:0000255}. TOPO_DOM 24 818 Extracellular. {ECO:0000255}.; TOPO_DOM 840 1032 Cytoplasmic. {ECO:0000255}. FUNCTION: Key component of innate and adaptive immunity. TLRs (Toll-like receptors) control host immune response against pathogens through recognition of molecular patterns specific to microorganisms. Acts via MYD88 and TRAF6, leading to NF-kappa-B. activation, cytokine secretion and the inflammatory response (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Homodimer. Interacts with MYD88 via their respective TIR domains (By similarity). Interacts with BTK (By similarity). Interacts with UNC93B1. Interacts with SMPDL3B (PubMed:26095358). {ECO:0000250|UniProtKB:Q9NR97, ECO:0000269|PubMed:19451267, ECO:0000269|PubMed:26095358}. +Q9JMD1 SMBT1_MOUSE Scm-like with four MBT domains protein 1 863 97,338 Chain (1); Domain (1); Erroneous termination (1); Modified residue (2); Repeat (4); Sequence caution (1) FUNCTION: Histone-binding protein, which is part of various corepressor complexes. Mediates the recruitment of corepressor complexes to target genes, followed by chromatin compaction and repression of transcription. Plays a role during myogenesis: required for the maintenance of undifferentiated states of myogenic progenitor cells via interaction with MYOD1. Interaction with MYOD1 leads to the recruitment of associated corepressors and silencing of MYOD1 target genes. Part of the SLC complex in germ cells, where it may play a role during spermatogenesis. {ECO:0000269|PubMed:23349461}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with MYOD1 (By similarity). Component of the SLC (SFMBT1-LSD1-CoREST) corepressor complex, which also contains KDM1A/LSD1 and RCOR1/CoREST. Interacts with KDM1A/LSD1 and RCOR1/CoREST (By similarity). Interacts with MYOD1. {ECO:0000250, ECO:0000269|PubMed:23349461, ECO:0000269|PubMed:23592795}. DOMAIN: The MBT repeats mediate binding to histones tails; however, in contrast to other MBT repeats, does not bind specific histone lysine modifications. The MBT repeats lack the conserved Asp and aromatic cage at conserved positions (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in the testis, low expression is detected in brain, kidney, heart and lung. Highly expressed in germ cells, where it associates with the synaptic regions of meiotic chromosomes in pachytene stage spermatocytes. {ECO:0000269|PubMed:10806358, ECO:0000269|PubMed:23592795}. +Q8CD91 SMOC2_MOUSE SPARC-related modular calcium-binding protein 2 (Secreted modular calcium-binding protein 2) (SMOC-2) 447 49,891 Alternative sequence (1); Calcium binding (2); Chain (1); Disulfide bond (9); Domain (5); Glycosylation (2); Sequence conflict (4); Signal peptide (1) FUNCTION: Can stimulate endothelial cell proliferation, migration, as well as angiogenesis (By similarity). Promotes matrix assembly and cell adhesiveness. {ECO:0000250, ECO:0000269|PubMed:18757743}. PTM: N-glycosylated. {ECO:0000269|PubMed:12741954}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000269|PubMed:18757743}. SUBUNIT: Binds various proteins from the extracellular matrix. {ECO:0000269|PubMed:18757743}. TISSUE SPECIFICITY: Strongly expressed in ovary, followed by heart, muscle, spleen, brain, thymus, lung, liver, kidney, spleen, testis, ovary and skeletal muscle. {ECO:0000269|PubMed:12741954}. +Q3V0X1 SMIM9_MOUSE Small integral membrane protein 9 137 15,398 Chain (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 85 105 Helical. {ECO:0000255}. TOPO_DOM 24 84 Extracellular. {ECO:0000255}.; TOPO_DOM 106 137 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +P97471 SMAD4_MOUSE Mothers against decapentaplegic homolog 4 (MAD homolog 4) (Mothers against DPP homolog 4) (Deletion target in pancreatic carcinoma 4 homolog) (SMAD family member 4) (SMAD 4) (Smad4) 551 60,342 Beta strand (6); Chain (1); Compositional bias (1); Cross-link (2); Domain (2); Helix (6); Metal binding (4); Modified residue (3); Region (2); Sequence conflict (2); Site (1); Turn (1) FUNCTION: Common SMAD (co-SMAD) is the coactivator and mediator of signal transduction by TGF-beta (transforming growth factor). Component of the heterotrimeric SMAD2/SMAD3-SMAD4 complex that forms in the nucleus and is required for the TGF-mediated signaling. Promotes binding of the SMAD2/SMAD4/FAST-1 complex to DNA and provides an activation function required for SMAD1 or SMAD2 to stimulate transcription. Component of the multimeric SMAD3/SMAD4/JUN/FOS complex which forms at the AP1 promoter site; required for synergistic transcriptional activity in response to TGF-beta. May act as a tumor suppressor. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator (By similarity). Acts synergistically with SMAD1 and YY1 in bone morphogenetic protein (BMP)-mediated cardiac-specific gene expression (PubMed:15329343). Binds to SMAD binding elements (SBEs) (5'-GTCT/AGAC-3') within BMP response element (BMPRE) of cardiac activating regions (PubMed:15329343). In muscle physiology, plays a central role in the balance between atrophy and hypertrophy. When recruited by MSTN, promotes atrophy response via phosphorylated SMAD2/4. MSTN decrease causes SMAD4 release and subsequent recruitment by the BMP pathway to promote hypertrophy via phosphorylated SMAD1/5/8. {ECO:0000250, ECO:0000269|PubMed:15329343, ECO:0000269|PubMed:24076600}. PTM: Phosphorylated by PDPK1. {ECO:0000250}.; PTM: Monoubiquitinated on Lys-518 by E3 ubiquitin-protein ligase TRIM33. Monoubiquitination hampers its ability to form a stable complex with activated SMAD2/3 resulting in inhibition of TGF-beta/BMP signaling cascade. Deubiquitination by USP9X restores its competence to mediate TGF-beta signaling (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13485}. Nucleus {ECO:0000250|UniProtKB:Q13485}. Note=In the cytoplasm in the absence of ligand. Migration to the nucleus when complexed with R-SMAD. PDPK1 prevents its nuclear translocation. {ECO:0000250|UniProtKB:Q13485}. SUBUNIT: Monomer (By similarity). Heterotrimer; with a C-terminally phosphorylated R-SMAD molecule and to form the transcriptionally active SMAD2/3-SMAD4 complex (By similarity). Found in a ternary complex composed of SMAD4, STK11/LKB1 and STK11IP. Interacts with ATF2, COPS5, DACH1, MSG1, SKI, STK11/LKB1, STK11IP and TRIM33. Associates with ZNF423 or ZNF521 in response to BMP2 leading to activate transcription of BMP target genes. Interacts with USP9X. Interacts with RBPMS. Interacts with WWTR1 (via coiled-coil domain). Interacts with CITED1 and CITED2 (By similarity). Interacts with PDPK1 (via PH domain) (By similarity). Interacts with VPS39; this interaction affects heterodimer formation with SMAD3, but not with SMAD2, and leads to inhibition of SMAD3-dependent transcription activation (By similarity). Interactions with VPS39 and SMAD2 may be mutually exclusive (By similarity). Interacts (via MH2 domain) with ZNF451 (via N-terminal zinc-finger domains) (By similarity). Identified in a complex that contains at least ZNF451, SMAD2, SMAD3 and SMAD4 (By similarity). Found in a complex with SMAD1 and YY1 (PubMed:15329343). Interacts with ZC3H3 (PubMed:16115198). Interacts weakly with ZNF8 (PubMed:12370310). Interacts with NUP93 and IPO7; translocates SMAD4 to the nucleus through the NPC upon BMP7 stimulation resulting in activation of SMAD4 signaling (By similarity). Interacts with CREB3L1, the interaction takes place upon TGFB1 induction and SMAD4 acts as CREB3L1 coactivator to induce the expression of genes involved in the assembly of collagen extracellular matrix (By similarity). Interacts with DLX1 (By similarity). Interacts with ZBTB7A; the interaction is direct and stimulated by TGFB1 (By similarity). Interacts with CREBBP; the recruitment of this transcriptional coactivator is negatively regulated by ZBTB7A (By similarity). Interacts with EP300; the interaction with this transcriptional coactivator is negatively regulated by ZBTB7A (By similarity). Interacts with HDAC1 (By similarity). {ECO:0000250|UniProtKB:O70437, ECO:0000250|UniProtKB:Q13485, ECO:0000269|PubMed:12370310, ECO:0000269|PubMed:15329343, ECO:0000269|PubMed:16115198, ECO:0000269|PubMed:20147459}. DOMAIN: The MH1 domain is required for DNA binding.; DOMAIN: The MH2 domain is required for both homomeric and heteromeric interactions and for transcriptional regulation. Sufficient for nuclear import (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. +P62320 SMD3_MOUSE Small nuclear ribonucleoprotein Sm D3 (Sm-D3) (snRNP core protein D3) 126 13,916 Chain (1); Compositional bias (1); Initiator methionine (1); Modified residue (1); Region (1); Repeat (5) FUNCTION: Plays role in pre-mRNA splicing as core component of the SMN-Sm complex that mediates spliceosomal snRNP assembly and as component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Component of both the pre-catalytic spliceosome B complex and activated spliceosome C complexes. Is also a component of the minor U12 spliceosome (By similarity). As part of the U7 snRNP it is involved in histone pre-mRNA 3'-end processing (PubMed:19470752). {ECO:0000250|UniProtKB:P62318, ECO:0000269|PubMed:19470752}. PTM: Methylated on arginine residues by PRMT5 and PRMT7; probable asymmetric dimethylation which is required for assembly and biogenesis of snRNPs. {ECO:0000250|UniProtKB:P62318}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P62318}. Nucleus {ECO:0000269|PubMed:19470752}. Note=SMN-mediated assembly into core snRNPs occurs in the cytosol before SMN-mediated transport to the nucleus to be included in spliceosomes. {ECO:0000250|UniProtKB:P62318}. SUBUNIT: Core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Most spliceosomal snRNPs contain a common set of Sm proteins, SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. Component of the U1 snRNP. The U1 snRNP is composed of the U1 snRNA and the 7 core Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG, and at least three U1 snRNP-specific proteins SNRNP70/U1-70K, SNRPA/U1-A and SNRPC/U1-C. Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39, plus LSM2, LSM3, LSM4, LSM5, LSM6, LSM7 and LSM8 (By similarity). Component of the U7 snRNP complex, or U7 Sm protein core complex, that is composed of the U7 snRNA and at least LSM10, LSM11, SNRPB, SNRPD3, SNRPE, SNRPF and SNRPG; the complex does not contain SNRPD1 and SNRPD2 (PubMed:19470752). Component of the U11/U12 snRNPs that are part of the U12-type spliceosome. Part of the SMN-Sm complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8, STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG; catalyzes core snRNPs assembly. Forms a 6S pICln-Sm complex composed of CLNS1A/pICln, SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG; ring-like structure where CLNS1A/pICln mimics additional Sm proteins and which is unable to assemble into the core snRNP (By similarity). {ECO:0000250|UniProtKB:P62318, ECO:0000269|PubMed:19470752}. +Q8K190 SMDC1_MOUSE SAYSvFN domain-containing protein 1 188 20,704 Chain (1); Transmembrane (1) TRANSMEM 101 121 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. +Q8K0S9 SNPC1_MOUSE snRNA-activating protein complex subunit 1 (SNAPc subunit 1) (Small nuclear RNA-activating complex polypeptide 1) (snRNA-activating protein complex 43 kDa subunit) (SNAPc 43 kDa subunit) 389 44,576 Chain (1); Compositional bias (1); Modified residue (2); Region (2) FUNCTION: Part of the SNAPc complex required for the transcription of both RNA polymerase II and III small-nuclear RNA genes. Binds to the proximal sequence element (PSE), a non-TATA-box basal promoter element common to these 2 types of genes. Recruits TBP and BRF2 to the U6 snRNA TATA box (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Part of the SNAPc complex composed of 5 subunits: SNAPC1, SNAPC2, SNAPC3, SNAPC4 and SNAPC5. SNAPC1 interacts with SNAPC3, SNAPC4 and TBP (By similarity). {ECO:0000250}. +Q8BTK5 SMYD4_MOUSE SET and MYND domain-containing protein 4 (EC 2.1.1.-) 799 88,538 Alternative sequence (1); Binding site (2); Chain (1); Domain (1); Natural variant (8); Region (2); Sequence conflict (3); Zinc finger (1) +Q91XA5 SNPC2_MOUSE snRNA-activating protein complex subunit 2 (SNAPc subunit 2) (Small nuclear RNA-activating complex polypeptide 2) (snRNA-activating protein complex 45 kDa subunit) (SNAPc 45 kDa subunit) 359 38,370 Chain (1); Sequence conflict (2) FUNCTION: Part of the SNAPc complex required for the transcription of both RNA polymerase II and III small-nuclear RNA genes. Binds to the proximal sequence element (PSE), a non-TATA-box basal promoter element common to these 2 types of genes. Recruits TBP and BRF2 to the U6 snRNA TATA box (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Part of the SNAPc complex composed of 5 subunits: SNAPC1, SNAPC2, SNAPC3, SNAPC4 and SNAPC5. SNAPC2 interacts with TBP and SNAPC4 (By similarity). {ECO:0000250}. +Q9JIW5 SMAD9_MOUSE Mothers against decapentaplegic homolog 9 (MAD homolog 9) (Mothers against DPP homolog 9) (SMAD family member 9) (SMAD 9) (Smad9) (Smad8) 430 48,636 Chain (1); Compositional bias (1); Domain (2); Metal binding (4); Natural variant (1) FUNCTION: Transcriptional modulator activated by BMP (bone morphogenetic proteins) type 1 receptor kinase. SMAD9 is a receptor-regulated SMAD (R-SMAD). Has been shown to be activated by activin type I receptor-like kinases (ALK-2, ALK-3, ALK-6) which stimulate heteromerization between SMAD9 and SMAD4. May play a role in osteoblast differentiation and maturation. PTM: Phosphorylated on serine by BMP (bone morphogenetic proteins) type 1 receptor kinase and activin type I receptor-like kinases (ALK-2, ALK-3 and ALK-6). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Cytoplasmic in the absence of ligand. Migrates to the nucleus when complexed with SMAD4. SUBUNIT: Interaction with the co-SMAD SMAD4. Interacts with PEBP2-alpha subunit (By similarity). Interacts with RANBP3L (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O15198}. +Q3TYX3 SMYD5_MOUSE SET and MYND domain-containing protein 5 (EC 2.1.1.-) (Protein NN8-4AG) (Retinoic acid-induced protein 15) 416 47,095 Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (1); Sequence conflict (1); Zinc finger (1) +Q9QY31 SNAI3_MOUSE Zinc finger protein SNAI3 (Protein snail homolog 3) (Snail-related gene from muscle cells) (Zinc finger protein 293) 287 31,636 Chain (1); Region (1); Sequence conflict (2); Zinc finger (5) FUNCTION: Seems to inhibit myoblast differentiation. Transcriptional repressor of E-box-dependent transactivation of downstream myogenic bHLHs genes. Binds preferentially to the canonical E-box sequences 5'-CAGGTG-3' and 5'-CACCTG-3'. {ECO:0000269|PubMed:10606664}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10606664}. DOMAIN: Binds E-box via C2H2-type zinc finger domain. TISSUE SPECIFICITY: Highly expressed in skeletal muscle and thymus. Lower expression in heart, lung and spleen. {ECO:0000269|PubMed:10606664}. +Q99ME3 SNCAP_MOUSE Synphilin-1 (Alpha-synuclein-interacting protein) 962 105,607 Chain (1); Coiled coil (1); Repeat (6); Sequence conflict (1) PTM: Ubiquitinated; mediated by SIAH1 or RNF19A and leading to its subsequent proteasomal degradation. {ECO:0000250}. SUBUNIT: Associates with SNCA, RNF19A AND PRKN. {ECO:0000250}. +Q78PY7 SND1_MOUSE Staphylococcal nuclease domain-containing protein 1 (EC 3.1.31.1) (100 kDa coactivator) (p100 co-activator) 910 102,088 Chain (1); Cross-link (1); Domain (5); Erroneous initiation (1); Initiator methionine (1); Modified residue (11); Motif (2); Sequence conflict (2) FUNCTION: Endonuclease that mediates miRNA decay of both protein-free and AGO2-loaded miRNAs (By similarity). As part of its function in miRNA decay, regulates mRNAs involved in G1-to-S phase transition (By similarity). Functions as a bridging factor between STAT6 and the basal transcription factor (By similarity). Plays a role in PIM1 regulation of MYB activity (By similarity). Functions as a transcriptional coactivator for STAT5 (PubMed:12819296). {ECO:0000250|UniProtKB:Q7KZF4, ECO:0000269|PubMed:12819296}. PTM: Phosphorylated by PIM1 in vitro. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q7KZF4}. Nucleus {ECO:0000250|UniProtKB:Q7KZF4}. Melanosome {ECO:0000250|UniProtKB:Q7KZF4}. Note=In IL-4 stimulated cells colocalizes with STAT6 in the nucleus. {ECO:0000250|UniProtKB:Q7KZF4}. SUBUNIT: Forms a ternary complex with STAT6 and POLR2A (By similarity). Associates with the RNA-induced silencing complex (RISC) (By similarity). Interacts with the RISC components AGO2, FMR1 and TNRC6A (By similarity). Interacts with GTF2E1 and GTF2E2 (By similarity). Interacts with PIM1 (By similarity). Interacts with STAT5 (PubMed:12819296). {ECO:0000250|UniProtKB:Q7KZF4, ECO:0000269|PubMed:12819296}. +P62301 RS13_MOUSE 40S ribosomal protein S13 151 17,222 Chain (1); Cross-link (1); Modified residue (5) +O54941 SMCE1_MOUSE SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1 (BRG1-associated factor 57) (BAF57) 411 46,638 Chain (1); Coiled coil (1); Compositional bias (1); Cross-link (7); DNA binding (1); Erroneous termination (1); Frameshift (1); Modified residue (3); Sequence caution (1) FUNCTION: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner (PubMed:12110891). Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (PubMed:17640523). Also specifically interacts with the CoREST corepressor resulting in repression of neuronal specific gene promoters in non-neuronal cells (By similarity). Required for the coactivation of estrogen responsive promoters by SWI/SNF complexes and the SRC/p160 family of histone acetyltransferases (HATs)(PubMed:12145209). {ECO:0000250|UniProtKB:Q969G3, ECO:0000269|PubMed:12110891, ECO:0000269|PubMed:12145209, ECO:0000269|PubMed:17640523}. PTM: Ubiquitinated by TRIP12, leading to its degradation by the proteasome. Ubiquitination is prevented upon interaction between TRIP12 and SMARCC1 (By similarity). {ECO:0000250|UniProtKB:Q969G3}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}. SUBUNIT: Component of the multiprotein chromatin-remodeling complexes SWI/SNF: SWI/SNF-A (BAF), SWI/SNF-B (PBAF) and related complexes. The canonical complex contains a catalytic subunit (either SMARCA4/BRG1/BAF190A or SMARCA2/BRM/BAF190B), and at least SMARCE1, ACTL6A/BAF53, SMARCC1/BAF155, SMARCC2/BAF170, and SMARCB1/SNF5/BAF47. Other subunits specific to each of the complexes may also be present permitting several possible combinations developmentally and tissue specific. Component of the BAF complex, which includes at least actin (ACTB), ARID1A/BAF250A, ARID1B/BAF250B, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57, SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C. In muscle cells, the BAF complex also contains DPF3. Component of neural progenitors-specific chromatin remodeling complex (npBAF complex) composed of at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, PHF10/BAF45A, ACTL6A/BAF53A and actin. Component of neuron-specific chromatin remodeling complex (nBAF complex) composed of at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, DPF1/BAF45B, DPF3/BAF45C, ACTL6B/BAF53B and actin. May be a component of the SWI/SNF-B (PBAF) chromatin remodeling complex, at least composed of SMARCA4/BRG1, SMARCB1/BAF47/SNF5, ACTL6A/BAF53A or ACTL6B/BAF53B, SMARCE1/BAF57, SMARCD1/BAF60A, SMARCD2/BAF60B, perhaps SMARCD3/BAF60C, SMARCC1/BAF155, SMARCC2/BAF170, PBRM1/BAF180, ARID2/BAF200 and actin (ACTB)(PubMed:17640523). Interacts with BRDT (By similarity). Also binds to the SRC/p160 family of histone acetyltransferases (HATs) composed of NCOA1, NCOA2, and NCOA3. Interacts with RCOR1/CoREST, NR3C1 and ZMIM2/ZIMP7 (By similarity). {ECO:0000250|UniProtKB:Q56A18, ECO:0000250|UniProtKB:Q969G3, ECO:0000269|PubMed:17640523}. DOMAIN: The HMG domain is essential for CD4 silencing and CD8 activation; mutation of this domain blocks thymus development. {ECO:0000269|PubMed:12110891}. +Q80U23 SNPH_MOUSE Syntaphilin 495 53,753 Alternative sequence (2); Chain (1); Coiled coil (1); Compositional bias (3); Erroneous initiation (5); Modified residue (5); Sequence conflict (4); Transmembrane (1) TRANSMEM 427 446 Helical. {ECO:0000255}. FUNCTION: Inhibits SNARE complex formation by absorbing free syntaxin-1. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Cell junction, synapse, synaptosome. SUBUNIT: Binds to syntaxin-1. {ECO:0000250}. +Q8VIK1 SNR25_MOUSE U11/U12 small nuclear ribonucleoprotein 25 kDa protein (U11/U12 snRNP 25 kDa protein) 123 14,292 Beta strand (6); Chain (1); Domain (1); Helix (3); Sequence conflict (1) SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the U11/U12 snRNPs that are part of the U12-type spliceosome. {ECO:0000250}. +P62270 RS18_MOUSE 40S ribosomal protein S18 (Ke-3) (Ke3) 152 17,719 Chain (1); Cross-link (3); Initiator methionine (1); Modified residue (3); Sequence conflict (1) FUNCTION: Located at the top of the head of the 40S subunit, it contacts several helices of the 18S rRNA. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. +Q925E0 SNTG2_MOUSE Gamma-2-syntrophin (G2SYN) (Syntrophin-5) (SYN5) 539 59,598 Chain (1); Domain (2) FUNCTION: Adapter protein that binds to and probably organizes the subcellular localization of a variety of proteins. May link various receptors to the actin cytoskeleton and the dystrophin glycoprotein complex (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane, sarcolemma; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Note=In skeletal muscle, it localizes at the cytoplasmic side of the sarcolemmal membrane. SUBUNIT: Interacts with the dystrophin protein DMD and related proteins DTNA and DTNB. {ECO:0000250}. DOMAIN: The association with dystrophin or related proteins probably leaves the PDZ domain available to recruit proteins to the membrane. {ECO:0000250}. +P62983 RS27A_MOUSE Ubiquitin-40S ribosomal protein S27a (Ubiquitin carboxyl extension protein 80) [Cleaved into: Ubiquitin; 40S ribosomal protein S27a] 156 17,951 Beta strand (4); Binding site (2); Chain (2); Compositional bias (2); Cross-link (7); Domain (1); Helix (3); Modified residue (5); Site (1); Zinc finger (1) FUNCTION: Ubiquitin: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling. {ECO:0000269|PubMed:19754430}.; FUNCTION: 40S Ribosomal protein S27a: Component of the 40S subunit of the ribosome. {ECO:0000269|PubMed:19754430}. PTM: Ubiquitin: Phosphorylated at Ser-65 by PINK1 during mitophagy. Phosphorylated ubiquitin specifically binds and activates parkin (PRKN), triggering mitophagy. Phosphorylation does not affect E1-mediated E2 charging of ubiquitin but affects discharging of E2 enzymes to form polyubiquitin chains. It also affects deubiquitination by deubiquitinase enzymes such as USP30. {ECO:0000250|UniProtKB:P62979}.; PTM: Ubiquitin: Mono-ADP-ribosylated at the C-terminus by PARP9, a component of the PPAR9-DTX3L complex. ADP-ribosylation requires processing by E1 and E2 enzymes and prevents ubiquitin conjugation to substrates such as histones. {ECO:0000250|UniProtKB:P62979}. SUBCELLULAR LOCATION: Ubiquitin: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Ribosomal protein S27a is part of the 40S ribosomal subunit. {ECO:0000250}. +Q6ZWY3 RS27L_MOUSE 40S ribosomal protein S27-like 84 9,477 Chain (1); Zinc finger (1) +Q8K5A4 RSLAA_MOUSE Ras-like protein family member 10A (Ras-like protein RRP22) (Ras-related protein on chromosome 22 homolog) 203 22,792 Chain (1); Lipidation (1); Modified residue (1); Motif (1); Nucleotide binding (3); Propeptide (1); Region (1) FUNCTION: Potent inhibitor of cellular proliferation. {ECO:0000250}. PTM: Isoprenylation is essential for nucleolar localization, and the proliferation-inhibiting activity of RASL10A. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Nucleus, nucleolus {ECO:0000250}. Note=May cycle in and out of the nucleolus in a GTP-dependent manner. {ECO:0000250}. +Q8BYM7 RSH4A_MOUSE Radial spoke head protein 4 homolog A (Radial spoke head-like protein 3) 716 80,146 Chain (1); Compositional bias (3); Modified residue (1) FUNCTION: Probable component of the axonemal radial spoke head (By similarity). Radial spokes are regularly spaced along cilia, sperm and flagella axonemes. They consist of a thin stalk which is attached to a subfiber of the outer doublet microtubule, and a bulbous head which is attached to the stalk and appears to interact with the projections from the central pair of microtubules. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000305}. Note=Radial spoke. {ECO:0000305}. +Q9D9V4 RSPH9_MOUSE Radial spoke head protein 9 homolog 276 31,331 Chain (1) FUNCTION: Probable component of the axonemal radial spoke head (By similarity). Radial spokes are regularly spaced along cilia, sperm and flagella axonemes. They consist of a thin stalk, which is attached to a subfiber of the outer doublet microtubule, and a bulbous head, which is attached to the stalk and appears to interact with the projections from the central pair of microtubules. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000305}. Note=Radial spoke. {ECO:0000305}. TISSUE SPECIFICITY: Expressed in the embryonic node at E7.5 and in the nasal, lung, tracheal and brain ventricle epithelium at E18.5-E19.5. {ECO:0000269|PubMed:19200523}. +Q9DBU6 RSRC1_MOUSE Serine/Arginine-related protein 53 (SRrp53) (Arginine/serine-rich coiled-coil protein 1) 334 38,637 Chain (1); Coiled coil (1); Compositional bias (1) FUNCTION: Plays a role in pre-mRNA splicing. Involved in both constitutive and alternative pre-mRNA splicing. May have a role in the recognition of the 3' splice site during the second step of splicing (By similarity). {ECO:0000250}. PTM: Phosphorylated. {ECO:0000269|PubMed:15798186}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15798186}. Nucleus speckle {ECO:0000269|PubMed:15798186}. Cytoplasm {ECO:0000269|PubMed:15798186}. Note=Shuttles between the nucleus and cytoplasm. SUBUNIT: Interacts (via Arg/Ser-rich domain) with LUC7L3, RBM39 and RSF1. {ECO:0000250}. +A2RTL5 RSRC2_MOUSE Arginine/serine-rich coiled-coil protein 2 376 43,876 Chain (1); Coiled coil (1); Compositional bias (1); Cross-link (2); Modified residue (2) +Q80X85 RT07_MOUSE 28S ribosomal protein S7, mitochondrial (MRP-S7) (S7mt) 242 28,063 Chain (1); Modified residue (1); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q3T040}. SUBUNIT: Component of the mitochondrial ribosome small subunit (28S) which comprises a 12S rRNA and about 30 distinct proteins. {ECO:0000250|UniProtKB:Q3T040}. +Q14B46 RTKN2_MOUSE Rhotekin-2 (Pleckstrin homology domain-containing family K member 1) (PH domain-containing family K member 1) 604 66,962 Alternative sequence (1); Chain (1); Coiled coil (1); Domain (2); Sequence conflict (12) FUNCTION: May play an important role in lymphopoiesis. {ECO:0000250}. +P25444 RS2_MOUSE 40S ribosomal protein S2 (40S ribosomal protein S4) (Protein LLRep3) 293 31,231 Chain (1); Compositional bias (1); Cross-link (4); Domain (1); Frameshift (1); Initiator methionine (1); Modified residue (7); Sequence conflict (1) PTM: Citrullinated by PADI4 in the Arg/Gly-rich region. {ECO:0000250}.; PTM: Asymmetric arginine dimethylation by PRMT3 occurs at multiple sites in the Arg/Gly-rich region. {ECO:0000250}. +P27048 RSMB_MOUSE Small nuclear ribonucleoprotein-associated protein B (snRNP-B) (snRPB) (Sm protein B) (Sm-B) (SmB) 231 23,656 Chain (1); Modified residue (10); Region (1); Repeat (4) FUNCTION: Plays role in pre-mRNA splicing as core component of the SMN-Sm complex that mediates spliceosomal snRNP assembly and as component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Component of both the pre-catalytic spliceosome B complex and activated spliceosome C complexes. Is also a component of the minor U12 spliceosome (By similarity). As part of the U7 snRNP it is involved in histone pre-mRNA 3'-end processing (PubMed:19470752). {ECO:0000250|UniProtKB:P14678, ECO:0000269|PubMed:19470752}. PTM: Methylated. Arg-108 and Arg-112 are dimethylated, probably to asymmetric dimethylarginine. {ECO:0000250|UniProtKB:P14678}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P14678}. Nucleus {ECO:0000269|PubMed:19470752}. Note=SMN-mediated assembly into core snRNPs occurs in the cytosol before SMN-mediated transport to the nucleus to be included in spliceosomes. {ECO:0000250|UniProtKB:P14678}. SUBUNIT: Core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Most spliceosomal snRNPs contain a common set of Sm proteins, SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. Component of the U1 snRNP. The U1 snRNP is composed of the U1 snRNA and the 7 core Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG, and at least three U1 snRNP-specific proteins SNRNP70/U1-70K, SNRPA/U1-A and SNRPC/U1-C. Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39, plus LSM2, LSM3, LSM4, LSM5, LSM6, LSM7 and LSM8 (By similarity). Component of the U7 snRNP complex, or U7 Sm protein core complex, that is composed of the U7 snRNA and at least LSM10, LSM11, SNRPB, SNRPD3, SNRPE, SNRPF and SNRPG; the complex does not contain SNRPD1 and SNRPD2 (PubMed:19470752). Component of the U11/U12 snRNPs that are part of the U12-type spliceosome. Part of the SMN-Sm complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8, STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG; catalyzes core snRNPs assembly. Forms a 6S pICln-Sm complex composed of CLNS1A/pICln, SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG; ring-like structure where CLNS1A/pICln mimics additional Sm proteins and which is unable to assemble into the core snRNP (By similarity). Identified in a histone pre-mRNA complex, at least composed of ERI1, LSM11, SLBP, SNRPB, SYNCRIP and YBX1 (PubMed:19470752). Interacts with TDRD3 and SNUPN (By similarity). {ECO:0000250|UniProtKB:P14678, ECO:0000269|PubMed:19470752}. +P63163 RSMN_MOUSE Small nuclear ribonucleoprotein-associated protein N (snRNP-N) (Sm protein D) (Sm-D) (Sm protein N) (Sm-N) (SmN) (Tissue-specific-splicing protein) 240 24,614 Chain (1); Modified residue (8); Region (1); Repeat (5) FUNCTION: May be involved in tissue-specific alternative RNA processing events. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with TDRD3. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain and embryonic stem (ES) cells. {ECO:0000269|PubMed:10318933}. +Q8BVR6 RSPRY_MOUSE RING finger and SPRY domain-containing protein 1 576 64,322 Alternative sequence (3); Chain (1); Domain (1); Frameshift (1); Glycosylation (1); Modified residue (1); Sequence conflict (4); Signal peptide (1); Zinc finger (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Expressed in embryonic bone during primary endochondral ossification. Strong localization is observed in the perichondrium and periostium (at protein level). Also expressed in embryonic and postnatal brain and craniofacial tissues. Expressed in skeletal muscles (PubMed:26497270). {ECO:0000269|PubMed:26365341, ECO:0000269|PubMed:26497270}. +Q99N87 RT05_MOUSE 28S ribosomal protein S5, mitochondrial (MRP-S5) (S5mt) 432 48,207 Chain (1); Domain (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P82675}. SUBUNIT: Component of the mitochondrial ribosome small subunit (28S) which comprises a 12S rRNA and about 30 distinct proteins. {ECO:0000250|UniProtKB:P82675}. +P58064 RT06_MOUSE 28S ribosomal protein S6, mitochondrial (MRP-S6) (S6mt) 125 14,309 Chain (1); Erroneous initiation (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P82932}. SUBUNIT: Component of the mitochondrial ribosome small subunit (28S) which comprises a 12S rRNA and about 30 distinct proteins. {ECO:0000250|UniProtKB:P82932}. +Q8BK72 RT27_MOUSE 28S ribosomal protein S27, mitochondrial (MRP-S27) (S27mt) (Mitochondrial ribosomal protein S27) 415 47,779 Chain (1); Coiled coil (1); Repeat (2); Sequence conflict (1); Transit peptide (1) FUNCTION: RNA-binding component of the mitochondrial small ribosomal subunit (mt-SSU) that plays a role in mitochondrial protein synthesis. Stimulates mitochondrial mRNA translation of subunit components of the mitochondrial electron transport chain. Binds to the mitochondrial 12S rRNA (12S mt-rRNA) and tRNA(Glu). Overexpressed in hepatocellular carcinoma tissues compared with adjacent non-tumoral liver tissues. {ECO:0000250|UniProtKB:Q92552}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q92552}. Mitochondrion {ECO:0000250|UniProtKB:Q92552}. SUBUNIT: Component of the mitochondrial ribosome small subunit (28S) which comprises a 12S rRNA and about 30 distinct proteins. Interacts with NOA1. Interacts with MIEF1 upstream open reading frame protein. {ECO:0000250|UniProtKB:Q92552}. +Q9CQF8 RT63_MOUSE Ribosomal protein 63, mitochondrial (Mitochondrial ribosomal protein 63) (Mitochondrial ribosomal protein L57) (mMRP63) 102 11,952 Chain (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. +Q9CYK1 SYWM_MOUSE Tryptophan--tRNA ligase, mitochondrial (EC 6.1.1.2) ((Mt)TrpRS) (Tryptophanyl-tRNA synthetase) (TrpRS) 360 40,153 Binding site (3); Chain (1); Nucleotide binding (3); Sequence conflict (1); Transit peptide (1) FUNCTION: Mitochondrial aminoacyl-tRNA synthetase that activate and transfer the amino acids to their corresponding tRNAs during the translation of mitochondrial genes and protein synthesis. {ECO:0000250|UniProtKB:Q9UGM6}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:Q9UGM6}. +Q9CQR2 RS21_MOUSE 40S ribosomal protein S21 83 9,141 Chain (1); Modified residue (2) SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P63220}. Cytoplasm {ECO:0000250|UniProtKB:P63220}. Rough endoplasmic reticulum {ECO:0000250|UniProtKB:P63221}. Note=Detected on cytosolic polysomes (By similarity). Detected in ribosomes that are associated with the rough endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:P63220, ECO:0000250|UniProtKB:P63221}. SUBUNIT: Component of the 40S small ribosomal subunit. {ECO:0000250|UniProtKB:P63220}. +P62267 RS23_MOUSE 40S ribosomal protein S23 143 15,808 Chain (1); Cross-link (1); Modified residue (3) FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. Plays an important role in translational accuracy. {ECO:0000250|UniProtKB:P62266}. PTM: Hydroxylation at Pro-62 affects translation termination efficiency. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P62266}. Cytoplasm {ECO:0000250|UniProtKB:P62266}. Rough endoplasmic reticulum {ECO:0000250|UniProtKB:Q6SA96}. Note=Detected on cytosolic polysomes (By similarity). Detected in ribosomes that are associated with the rough endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:P62266, ECO:0000250|UniProtKB:Q6SA96}. SUBUNIT: Component of the 40S small ribosomal subunit. {ECO:0000250|UniProtKB:P62266}. +Q8CBB9 RSAD2_MOUSE Radical S-adenosyl methionine domain-containing protein 2 (Viperin) (Virus inhibitory protein, endoplasmic reticulum-associated, interferon-inducible) 362 41,524 Beta strand (10); Chain (1); Erroneous termination (1); Helix (12); Metal binding (3); Sequence conflict (43); Turn (4) FUNCTION: Interferon-inducible iron-sulfur (4FE-4S) cluster-binding antiviral protein which plays a major role in the cell antiviral state induced by type I and type II interferon. Can inhibit a wide range of viruses, including west Nile virus (WNV), dengue virus, sindbis virus, influenza A virus, sendai virus and vesicular stomatitis virus (VSV). Displays antiviral activity against influenza A virus by inhibiting the budding of the virus from the plasma membrane by disturbing the lipid rafts. This is accomplished, at least in part, through binding and inhibition of the enzyme farnesyl diphosphate synthase (FPPS), which is essential for the biosynthesis of isoprenoid-derived lipids. Promotes TLR7 and TLR9-dependent production of IFN-beta production in plasmacytoid dendritic cells (pDCs) by facilitating Lys-63'-linked ubiquitination of IRAK1. Plays a role in CD4+ T-cells activation and differentiation. Facilitates T-cell receptor (TCR)-mediated GATA3 activation and optimal T-helper 2 (Th2) cytokine production by modulating NFKB1 and JUNB activities. Can inhibit secretion of soluble proteins. {ECO:0000269|PubMed:17686841, ECO:0000269|PubMed:19047684, ECO:0000269|PubMed:21435586, ECO:0000269|PubMed:21880757}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Lipid droplet. SUBUNIT: Homodimer. Interacts with FPPS (By similarity). Interacts (via C-terminus) with VAPA/VAP33 (via C-terminus) and inhibits its interaction with hepatitis virus C (HCV) protein NS5A. Interacts with HADHB (By similarity). Interacts with IRAK1 and TRAF6. {ECO:0000250, ECO:0000269|PubMed:21435586}. DOMAIN: The N-terminal region (1-43) is necessary for its localization to the endoplasmic reticulum membrane and lipid droplet. TISSUE SPECIFICITY: Expressed at higher levels in atherosclerotic arteries than in normal arteries. {ECO:0000269|PubMed:15890971}. +Q80T69 RSBN1_MOUSE Lysine-specific demethylase 9 (KDM9) (EC 1.14.11.-) (Round spermatid basic protein 1) (Rosbin) 795 89,251 Binding site (2); Chain (1); Compositional bias (4); Cross-link (4); Erroneous initiation (4); Metal binding (3); Modified residue (1); Motif (1); Sequence conflict (1) FUNCTION: Histone demethylase that specifically demethylates dimethylated 'Lys-20' of histone H4 (H4K20me2), thereby modulating chromosome architecture. {ECO:0000269|PubMed:28867287}. PTM: Phosphorylated by PKA. {ECO:0000305|PubMed:14724137}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14724137}. TISSUE SPECIFICITY: Testis. Expressed exclusively in haploid round spermatids. {ECO:0000269|PubMed:14724137}. +Q8C0C7 SYFA_MOUSE Phenylalanine--tRNA ligase alpha subunit (EC 6.1.1.20) (Phenylalanyl-tRNA synthetase alpha subunit) (PheRS) 508 57,599 Binding site (2); Chain (1); Initiator methionine (1); Modified residue (4); Region (1); Sequence conflict (5) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q505J8}. SUBUNIT: Heterotetramer; dimer of two heterodimers formed by FARSA and FARSB. {ECO:0000250|UniProtKB:Q9Y285}. +Q8CDR2 RSH6A_MOUSE Radial spoke head protein 6 homolog A (Radial spoke head-like protein 1) 708 80,202 Chain (1); Compositional bias (2); Sequence conflict (2) TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:11237735}. +O89026 ROBO1_MOUSE Roundabout homolog 1 1612 176,407 Chain (1); Disulfide bond (5); Domain (8); Glycosylation (5); Modified residue (8); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 859 879 Helical. {ECO:0000255}. TOPO_DOM 20 858 Extracellular. {ECO:0000255}.; TOPO_DOM 880 1612 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for SLIT1 and SLIT2 that mediates cellular responses to molecular guidance cues in cellular migration, including axonal navigation at the ventral midline of the neural tube and projection of axons to different regions during neuronal development (PubMed:10433822, PubMed:24560577). Interaction with the intracellular domain of FLRT3 mediates axon attraction towards cells expressing NTN1 (PubMed:24560577). In axon growth cones, the silencing of the attractive effect of NTN1 by SLIT2 may require the formation of a ROBO1-DCC complex (By similarity). Plays a role in the regulation of cell migration via its interaction with MYO9B; inhibits MYO9B-mediated stimulation of RHOA GTPase activity, and thereby leads to increased levels of active, GTP-bound RHOA (By similarity). May be required for lung development (PubMed:11734623). {ECO:0000250|UniProtKB:Q9Y6N7, ECO:0000269|PubMed:10433822, ECO:0000269|PubMed:11734623, ECO:0000269|PubMed:15091338, ECO:0000269|PubMed:24560577}. PTM: Ubiquitinated. May be deubiquitinated by USP33. {ECO:0000269|PubMed:19684588}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24560577}; Single-pass type I membrane protein {ECO:0000305}. Cell projection, axon {ECO:0000269|PubMed:24560577}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:O55005}; Single-pass membrane protein {ECO:0000250|UniProtKB:O55005}. Note=Detected at growth cones in thalamus neurons (PubMed:24560577). PRRG4 prevents cell surface location and both colocalize in the Endoplasmic reticulum/Golgi adjacent to the cell nucleus (By similarity). {ECO:0000250|UniProtKB:O55005, ECO:0000269|PubMed:24560577}. SUBUNIT: Homodimer. Dimerization is mediated by the extracellular domain and is independent of SLIT liganding (By similarity). Interacts with SLIT1 (PubMed:10433822) Interacts with SLIT2 (By similarity). Interacts with FLRT3 (PubMed:24560577). Interacts with MYO9B (via Rho-GAP domain) (By similarity). {ECO:0000250|UniProtKB:Q9Y6N7, ECO:0000269|PubMed:10433822, ECO:0000269|PubMed:19684588, ECO:0000269|PubMed:19706539, ECO:0000269|PubMed:24560577}. TISSUE SPECIFICITY: Detected in embryonic thalamus neurons (at protein level) (PubMed:24560577). Expressed in embryonal spinal chord. Expressed in embryonal lung, and in adult lung bronchial epithelial cells of large proximal airways. {ECO:0000269|PubMed:12123796, ECO:0000269|PubMed:15091338, ECO:0000269|PubMed:24560577}. +O88569 ROA2_MOUSE Heterogeneous nuclear ribonucleoproteins A2/B1 (hnRNP A2/B1) 353 37,403 Alternative sequence (2); Chain (1); Compositional bias (1); Cross-link (9); Domain (2); Modified residue (36); Motif (1); Region (2); Sequence conflict (3) FUNCTION: Heterogeneous nuclear ribonucleoprotein (hnRNP) that associates with nascent pre-mRNAs, packaging them into hnRNP particles. The hnRNP particle arrangement on nascent hnRNA is non-random and sequence-dependent and serves to condense and stabilize the transcripts and minimize tangling and knotting. Packaging plays a role in various processes such as transcription, pre-mRNA processing, RNA nuclear export, subcellular location, mRNA translation and stability of mature mRNAs. Forms hnRNP particles with at least 20 other different hnRNP and heterogeneous nuclear RNA in the nucleus. Involved in transport of specific mRNAs to the cytoplasm in oligodendrocytes and neurons: acts by specifically recognizing and binding the A2RE (21 nucleotide hnRNP A2 response element) or the A2RE11 (derivative 11 nucleotide oligonucleotide) sequence motifs present on some mRNAs, and promotes their transport to the cytoplasm (By similarity). Specifically binds single-stranded telomeric DNA sequences, protecting telomeric DNA repeat against endonuclease digestion (By similarity). Also binds other RNA molecules, such as primary miRNA (pri-miRNAs): acts as a nuclear 'reader' of the N6-methyladenosine (m6A) mark by specifically recognizing and binding a subset of nuclear m6A-containing pri-miRNAs. Binding to m6A-containing pri-miRNAs promotes pri-miRNA processing by enhancing binding of DGCR8 to pri-miRNA transcripts. Involved in miRNA sorting into exosomes following sumoylation, possibly by binding (m6A)-containing pre-miRNAs. Acts as a regulator of efficiency of mRNA splicing, possibly by binding to m6A-containing pre-mRNAs (By similarity). {ECO:0000250|UniProtKB:A7VJC2, ECO:0000250|UniProtKB:P22626}. PTM: Sumoylated in exosomes, promoting miRNAs-binding. {ECO:0000250|UniProtKB:P22626}.; PTM: Asymmetric dimethylation at Arg-266 constitutes the major methylation site (By similarity). According to a report, methylation affects subcellular location and promotes nuclear localization (By similarity). According to another report, methylation at Arg-266 does not influence nucleocytoplasmic shuttling (By similarity). {ECO:0000250|UniProtKB:A7VJC2, ECO:0000250|UniProtKB:P22626}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P22626}. Cytoplasmic granule {ECO:0000250|UniProtKB:P22626}. Secreted, exosome {ECO:0000250|UniProtKB:P22626}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Component of ribonucleosomes. Not found in the nucleolus. Found in exosomes follwong sumoylation. {ECO:0000250|UniProtKB:P22626}. SUBUNIT: Identified in the spliceosome C complex. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with IGF2BP1. Interacts with C9orf72. Interacts with DGCR8. Interacts with TARDBP. Interacts with CKAP5. {ECO:0000250|UniProtKB:P22626}. DOMAIN: The low complexity (LC) region is intrinsically disordered. When incubated at high concentration, it is able to polymerize into labile, amyloid-like fibers and form cross-beta polymerization structures, probably driving the formation of hydrogels. In contrast to irreversible, pathogenic amyloids, the fibers polymerized from LC regions disassemble upon dilution. A number of evidences suggest that formation of cross-beta structures by LC regions mediate the formation of RNA granules, liquid-like droplets, and hydrogels. {ECO:0000250|UniProtKB:P22626}. +Q8BG05 ROA3_MOUSE Heterogeneous nuclear ribonucleoprotein A3 (hnRNP A3) 379 39,652 Alternative sequence (1); Chain (1); Compositional bias (1); Cross-link (6); Domain (2); Modified residue (31) FUNCTION: Plays a role in cytoplasmic trafficking of RNA. Binds to the cis-acting response element, A2RE. May be involved in pre-mRNA splicing (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Component of ribonucleosomes. {ECO:0000250}. SUBUNIT: Identified in the spliceosome C complex. {ECO:0000250}. +Q9EQ00 ROP1L_MOUSE Ropporin-1-like protein (AKAP-associated sperm protein) 218 24,516 Chain (1); Domain (1); Frameshift (1) FUNCTION: Important for male fertility. With ROPN1, involved in fibrous sheath integrity and sperm motility, plays a role in PKA-dependent signaling processes required for spermatozoa capacitation. {ECO:0000269|PubMed:23303679}. PTM: Sumoylated, sumoylation decreases upon spermatozoa capacitation conditions. {ECO:0000269|PubMed:27398160}. SUBCELLULAR LOCATION: Cell projection, cilium, flagellum {ECO:0000269|PubMed:23303679}. Cell projection, cilium {ECO:0000250|UniProtKB:Q96C74}. SUBUNIT: May interact with AKAP3 (By similarity). Interacts with FSCB; the interaction increases upon spermatozoa capacitation conditions (PubMed:27398160). {ECO:0000250|UniProtKB:Q96C74, ECO:0000269|PubMed:27398160}. TISSUE SPECIFICITY: Testis-specific. Expression is restricted to germ cells. {ECO:0000269|PubMed:11278869, ECO:0000269|PubMed:12021058, ECO:0000269|PubMed:23303679}. +Q923G2 RPAB3_MOUSE DNA-directed RNA polymerases I, II, and III subunit RPABC3 (RNA polymerases I, II, and III subunit ABC3) (DNA-directed RNA polymerase II subunit H) (RPB17) (RPB8 homolog) 150 17,143 Chain (1); Initiator methionine (1); Modified residue (1); Region (1) FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. SUBUNIT: Component of the RNA polymerase I (Pol I), RNA polymerase II (Pol II) and RNA polymerase III (Pol III) complexes consisting of at least 13, 12 and 17 subunits, respectively. Directly interacts with POLR2A (By similarity). {ECO:0000250}. +Q8K202 RPA49_MOUSE DNA-directed RNA polymerase I subunit RPA49 (RNA polymerase I subunit A49) (DNA-directed RNA polymerase I subunit E) (RNA polymerase I-associated factor 1) (RNA polymerase I-associated factor 53) 482 54,034 Alternative sequence (3); Chain (1); Modified residue (1); Sequence conflict (3) FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I which synthesizes ribosomal RNA precursors. Appears to be involved in the formation of the initiation complex at the promoter by mediating the interaction between Pol I and UBTF/UBF. {ECO:0000269|PubMed:8641287, ECO:0000269|PubMed:9254723}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:8641287, ECO:0000269|PubMed:9254723}. SUBUNIT: Component of the RNA polymerase I (Pol I) complex consisting of at least 13 subunits (PubMed:9254723). Interacts with PAF49/CD3EAP (PubMed:15226435). Also binds UBTF/UBF (PubMed:8641287). Interacts with PWP1 (By similarity). {ECO:0000250|UniProtKB:Q9GZS1, ECO:0000269|PubMed:15226435, ECO:0000269|PubMed:8641287, ECO:0000269|PubMed:9254723}. +Q921X6 RPC6_MOUSE DNA-directed RNA polymerase III subunit RPC6 (RNA polymerase III subunit C6) (DNA-directed RNA polymerase III subunit F) 316 35,652 Beta strand (3); Chain (1); Cross-link (2); Helix (3); Initiator methionine (1); Modified residue (1) FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. May direct RNA Pol III binding to the TFIIIB-DNA complex. Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts induce type I interferon and NF- Kappa-B through the RIG-I pathway (By similarity). Preferentially binds double-stranded DNA (dsDNA) (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9H1D9}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the RNA polymerase III (Pol III) complex consisting of 17 subunits. RPC3/POLR3C, RPC6/POLR3F and RPC7/POLR3G form a Pol III subcomplex (By similarity). Directly interacts with POLR3C (By similarity). Interacts with TBP and TFIIIB90 and GTF3C4 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9H1D9}. +Q9EPQ2 RPGR1_MOUSE X-linked retinitis pigmentosa GTPase regulator-interacting protein 1 (RPGR-interacting protein 1) 1331 151,996 Alternative sequence (8); Chain (1); Coiled coil (3); Domain (1); Region (1); Sequence conflict (9) FUNCTION: May function as scaffolding protein. Required for normal location of RPGR at the connecting cilium of photoreceptor cells. Required for normal disk morphogenesis and disk organization in the outer segment of photoreceptor cells and for survival of photoreceptor cells. {ECO:0000269|PubMed:12651948}. SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000269|PubMed:11104772, ECO:0000269|PubMed:12651948}. Note=Situated between the axonemal microtubules and the plasma membrane. SUBUNIT: Interacts with NPHP4. Interacts with NEK4 (By similarity). Forms homodimers and elongated homopolymers. Interacts with RPGR. Interacts with SPATA7 (PubMed:25398945). Interacts with CEP290/NPHP6; mediating the association between RPGR and CEP290/NPHP6 (By similarity). {ECO:0000250|UniProtKB:Q96KN7, ECO:0000269|PubMed:11104772, ECO:0000269|PubMed:12651948, ECO:0000269|PubMed:25398945}. DOMAIN: The C2 domain does not bind calcium ions, and does not bind phosphoinositides. {ECO:0000250|UniProtKB:Q96KN7}. TISSUE SPECIFICITY: Colocalizes with RGPR in the photoreceptor connecting cilium, a thin bridge linking the cell body and the light-sensing outer segment (at protein level). {ECO:0000269|PubMed:11104772, ECO:0000269|PubMed:12140192, ECO:0000269|PubMed:12651948}. +Q91ZQ5 RPE65_MOUSE Retinoid isomerohydrolase (EC 3.1.1.64) (All-trans-retinyl-palmitate hydrolase) (Meso-zeaxanthin isomerase) (EC 5.3.3.-) (Retinal pigment epithelium-specific 65 kDa protein) (Retinol isomerase) 533 61,085 Chain (1); Initiator methionine (1); Lipidation (4); Metal binding (4); Modified residue (5); Natural variant (1) FUNCTION: Critical isomerohydrolase in the retinoid cycle involved in regeneration of 11-cis-retinal, the chromophore of rod and cone opsins. Catalyzes the cleavage and isomerization of all-trans-retinyl fatty acid esters to 11-cis-retinol which is further oxidized by 11-cis retinol dehydrogenase to 11-cis-retinal for use as visual chromophore (PubMed:15765048, PubMed:9843205, PubMed:23407971, PubMed:28500718). Essential for the production of 11-cis retinal for both rod and cone photoreceptors (PubMed:17251447). Also capable of catalyzing the isomerization of lutein to meso-zeaxanthin an eye-specific carotenoid. The soluble form binds vitamin A (all-trans-retinol), making it available for LRAT processing to all-trans-retinyl ester. The membrane form, palmitoylated by LRAT, binds all-trans-retinyl esters, making them available for IMH (isomerohydrolase) processing to all-cis-retinol. The soluble form is regenerated by transferring its palmitoyl groups onto 11-cis-retinol, a reaction catalyzed by LRAT (By similarity). {ECO:0000250|UniProtKB:Q16518, ECO:0000250|UniProtKB:Q28175, ECO:0000269|PubMed:15765048, ECO:0000269|PubMed:17251447, ECO:0000269|PubMed:23407971, ECO:0000269|PubMed:28500718, ECO:0000269|PubMed:9843205}. PTM: Palmitoylation by LRAT regulates ligand binding specificity; the palmitoylated form (membrane form) specifically binds all-trans-retinyl-palmitate, while the soluble unpalmitoylated form binds all-trans-retinol (vitamin A). {ECO:0000250|UniProtKB:Q28175}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A9C3R9}. Cell membrane {ECO:0000250|UniProtKB:Q28175}; Lipid-anchor {ECO:0000250|UniProtKB:Q28175}. Microsome membrane {ECO:0000250|UniProtKB:Q28175}. Note=Attached to the membrane by a lipid anchor when palmitoylated (membrane form), soluble when unpalmitoylated. Undergoes light-dependent intracellular transport to become more concentrated in the central region of the retina pigment epithelium cells (By similarity). {ECO:0000250|UniProtKB:Q16518, ECO:0000250|UniProtKB:Q28175}. SUBUNIT: Interacts with MYO7A; this mediates light-dependent intracellular transport of RPE65. {ECO:0000250|UniProtKB:Q16518}. TISSUE SPECIFICITY: Retinal pigment epithelium specific. {ECO:0000269|PubMed:15765048, ECO:0000269|PubMed:23407971}. DISEASE: Note=Defects in Rpe65 are the cause of light damage susceptibility (LDS) of the retina. {ECO:0000305|PubMed:11150319}. +Q91YQ5 RPN1_MOUSE Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1 (Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 67 kDa subunit) (Ribophorin I) (RPN-I) (Ribophorin-1) 608 68,528 Chain (1); Cross-link (1); Glycosylation (1); Modified residue (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 441 458 Helical. {ECO:0000255}. TOPO_DOM 26 440 Lumenal. {ECO:0000255}.; TOPO_DOM 459 608 Cytoplasmic. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. {ECO:0000250|UniProtKB:E2RQ08}. SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:E2RQ08, ECO:0000250|UniProtKB:Q9GMB0}. Endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000305}. Melanosome {ECO:0000250|UniProtKB:P04843}. SUBUNIT: Component of the oligosaccharyltransferase (OST) complex. OST exists in two different complex forms which contain common core subunits RPN1, RPN2, OST48, OST4, DAD1 and TMEM258, either STT3A or STT3B as catalytic subunits, and form-specific accessory subunits. STT3A complex assembly occurs through the formation of 3 subcomplexes. Subcomplex 1 contains RPN1 and TMEM258, subcomplex 2 contains the STT3A-specific subunits STT3A, DC2/OSTC, and KCP2 as well as the core subunit OST4, and subcomplex 3 contains RPN2, DAD1, and OST48. The STT3A complex can form stable complexes with the Sec61 complex or with both the Sec61 and TRAP complexes. {ECO:0000250|UniProtKB:E2RQ08}. +Q9ERE3 SGK3_MOUSE Serine/threonine-protein kinase Sgk3 (EC 2.7.11.1) (Cytokine-independent survival kinase) (Serum/glucocorticoid-regulated kinase 3) (Serum/glucocorticoid-regulated kinase-like) 496 57,145 Active site (1); Beta strand (3); Binding site (1); Chain (1); Domain (3); Helix (6); Modified residue (4); Motif (1); Mutagenesis (2); Nucleotide binding (1); Sequence conflict (2); Turn (1) FUNCTION: Serine/threonine-protein kinase which is involved in the regulation of a wide variety of ion channels, membrane transporters, cell growth, proliferation, survival and migration. Up-regulates Na(+) channels: SCNN1A/ENAC and SCN5A, K(+) channels: KCNA3/KV1.3, KCNE1, KCNQ1 and KCNH2/HERG, epithelial Ca(2+) channels: TRPV5 and TRPV6, chloride channel: BSND, creatine transporter: SLC6A8, Na(+)/dicarboxylate cotransporter: SLC13A2/NADC1, Na(+)-dependent phosphate cotransporter: SLC34A2/NAPI-2B, amino acid transporters: SLC1A5/ASCT2 and SLC6A19, glutamate transporters: SLC1A3/EAAT1, SLC1A6/EAAT4 and SLC1A7/EAAT5, glutamate receptors: GRIA1/GLUR1 and GRIK2/GLUR6, Na(+)/H(+) exchanger: SLC9A3/NHE3, and the Na(+)/K(+) ATPase. Plays a role in the regulation of renal tubular phosphate transport and bone density. Phosphorylates NEDD4L and GSK3B. Positively regulates ER transcription activity through phosphorylation of FLII. Negatively regulates the function of ITCH/AIP4 via its phosphorylation and thereby prevents CXCR4 from being efficiently sorted to lysosomes. {ECO:0000269|PubMed:15774535, ECO:0000269|PubMed:15774536, ECO:0000269|PubMed:21113728, ECO:0000269|PubMed:21451460, ECO:0000269|PubMed:21865597}. PTM: Activated by phosphorylation on Ser-486 by an unknown kinase (may be mTORC2 but not confirmed), transforming it into a substrate for PDPK1 which then phosphorylates it on Thr-320. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasmic vesicle {ECO:0000269|PubMed:21865597}. Early endosome {ECO:0000269|PubMed:21865597}. Recycling endosome {ECO:0000250}. Note=Endosomal localization is a prerequisite for complete kinase activity. It is essential for its colocalization with the kinase responsible for phosphorylating Ser-486 thus allowing PDPK1 phosphorylation of Thr-320 resulting in complete activation of SGK3. Colocalizes with SLC9A3/NHE3 in the recycling endosomes (By similarity). Localized in vesicle-like structures and in the early endosome. {ECO:0000250}. SUBUNIT: Interacts with GSK3B and FLII. Interacts with PDPK1 in a phosphorylation-dependent manner. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed, predominantly in the heart, spleen and 7-day embryo. +Q8BKF1 RPOM_MOUSE DNA-directed RNA polymerase, mitochondrial (MtRPOL) (EC 2.7.7.6) 1207 136,705 Active site (3); Chain (1); Region (1); Repeat (2); Sequence conflict (1); Transit peptide (1) FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of mitochondrial DNA into RNA using the four ribonucleoside triphosphates as substrates. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:23283301}. SUBUNIT: Upon metabolic stress, forms a complex composed of FOXO3, SIRT3 and mitochondrial RNA polymerase POLRMT; the complex is recruited to mtDNA in a SIRT3-dependent manner (PubMed:23283301). Also forms a complex composed of FOXO3, SIRT3, TFAM and POLRMT (By similarity). Interacts with TFB1M and TFB2M, leading to the stimulation of transcription (By similarity). Interacts with TEFM (By similarity). {ECO:0000250|UniProtKB:O00411, ECO:0000269|PubMed:23283301}. +P16043 SLIB_MOUSE Somatoliberin (Growth hormone-releasing factor) (GRF) (Growth hormone-releasing hormone) (GHRH) 103 12,064 Peptide (1); Propeptide (2); Signal peptide (1) FUNCTION: GRF is released by the hypothalamus and acts on the adenohypophyse to stimulate the secretion of growth hormone. SUBCELLULAR LOCATION: Secreted. +Q810C1 SLIK1_MOUSE SLIT and NTRK-like protein 1 696 77,817 Chain (1); Domain (4); Modified residue (1); Repeat (12); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 623 643 Helical. {ECO:0000255}. TOPO_DOM 18 622 Extracellular. {ECO:0000255}.; TOPO_DOM 644 696 Cytoplasmic. {ECO:0000255}. FUNCTION: It is involved in synaptogenesis and promotes excitatory synapse differentiation (By similarity). Enhances neuronal dendrite outgrowth (PubMed:14550773). {ECO:0000250|UniProtKB:Q96PX8, ECO:0000269|PubMed:14550773}. PTM: Undergoes proteolytic cleavage that results in shedding of the ectodomain and cleavage of the C-terminal cytoplasmic tail. Glycosylated. Phosphorylation at Ser-695 is necessary for proper function in promoting neurite outgrowth. {ECO:0000250|UniProtKB:Q96PX8}. SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q96PX8}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q96PX8}. Secreted {ECO:0000250|UniProtKB:Q96PX8}. Cell junction, synapse {ECO:0000269|PubMed:27273464}. SUBUNIT: Can form homodimers; homodimerization requires repeat LRR 2 (By similarity). Interacts with YWHAB, YWHAE, YWHAG, YWHAH, SFN, YWHAQ and YWHAZ (By similarity). {ECO:0000250|UniProtKB:Q96PX8}. TISSUE SPECIFICITY: In the adult, significant expression is detected only in the brain. Broadly expressed in embryonic brain with highest expression in subventricular zone, subplate, cortical plate, pyramidal cell layer of hippocampus, thalamus and hypothalamus where levels are highest in ventromedial hypothalamus and medial part of periaqueductal gray matter. Also expressed in mantle layer of spinal cord and in lateral and medial motor columns. {ECO:0000269|PubMed:14550773}. +Q810C0 SLIK2_MOUSE SLIT and NTRK-like protein 2 846 95,436 Beta strand (14); Chain (1); Disulfide bond (4); Domain (3); Glycosylation (3); Helix (6); Modified residue (1); Mutagenesis (5); Region (1); Repeat (12); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (3) TRANSMEM 623 643 Helical. {ECO:0000255}. TOPO_DOM 22 622 Extracellular. {ECO:0000255}.; TOPO_DOM 644 846 Cytoplasmic. {ECO:0000255}. FUNCTION: It is involved in synaptogenesis (PubMed:25989451). Promotes excitatory synapse differentiation (By similarity). Suppresses neurite outgrowth (PubMed:14550773). {ECO:0000250|UniProtKB:Q9H156, ECO:0000269|PubMed:14550773, ECO:0000269|PubMed:25989451}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Cell membrane {ECO:0000250|UniProtKB:Q9H156}. SUBUNIT: Interacts with PTPRD; this interaction is PTPRD splicing-dependent and may induces pre-synaptic differentiation. {ECO:0000269|PubMed:25989451}. TISSUE SPECIFICITY: In the adult, significant expression is detected only in the brain. Broadly expressed in embryonic brain with highest expression in ventricular layer, subventricular zone, cortical plate, pyramidal layer of hippocampus, subicular neuroepithelium, thalamus, hypothalumus and spinal cord. {ECO:0000269|PubMed:14550773}. +Q810B9 SLIK3_MOUSE SLIT and NTRK-like protein 3 980 109,406 Chain (1); Domain (3); Glycosylation (2); Repeat (12); Sequence conflict (6); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 656 676 Helical. {ECO:0000255}. TOPO_DOM 30 655 Extracellular. {ECO:0000255}.; TOPO_DOM 677 980 Cytoplasmic. {ECO:0000255}. FUNCTION: Suppresses neurite outgrowth. {ECO:0000269|PubMed:14550773}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Broadly expressed in embryonic brain with highest expression in cortical plate, pyramidal cell layer of the hippocampus, thalamus and hypothalamus. {ECO:0000269|PubMed:14550773}. +P62264 RS14_MOUSE 40S ribosomal protein S14 151 16,273 Chain (1); Cross-link (3); Modified residue (3) +Q8BHJ9 SLU7_MOUSE Pre-mRNA-splicing factor SLU7 585 68,080 Chain (1); Cross-link (2); Erroneous gene model prediction (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (4); Motif (1); Sequence conflict (2); Zinc finger (1) FUNCTION: Participates in the second catalytic step of pre-mRNA splicing, when the free hydroxyl group of exon I attacks the 3'-splice site to generate spliced mRNA and the excised lariat intron. Required for holding exon 1 properly in the spliceosome and for correct AG identification when more than one possible AG exists in 3'-splicing site region. May be involved in the activation of proximal AG. Probably also involved in alternative splicing regulation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Predominantly nuclear. Shuttling between the nucleus and the cytoplasm is regulated by the CCHC-type zinc finger. Translocates from the nucleus to the cytoplasm after heat shock cell treatment. Accumulates in cytoplasmic vesicle-like organelles after heat shock treatment, which may represent stress granules (By similarity). {ECO:0000250}. SUBUNIT: Component of late spliceosomal complexes. Associates with the spliceosome prior to recognition of the 3'-splice site for step II, probably during catalysis of step I (By similarity). {ECO:0000250}. DOMAIN: The CCHC-type zinc finger is required to retain the protein within the nucleus and prevent its shuttle back to the cytoplasm via the CRM1 pathway. {ECO:0000250}. +Q8BYM8 SYCM_MOUSE Probable cysteine--tRNA ligase, mitochondrial (EC 6.1.1.16) (Cysteinyl-tRNA synthetase) (CysRS) 551 61,272 Binding site (1); Chain (1); Erroneous initiation (1); Metal binding (4); Motif (2); Sequence conflict (2); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. +Q8CH25 SLTM_MOUSE SAFB-like transcription modulator (Modulator of estrogen-induced transcription) (SAF-like transcription modulator) 1031 116,919 Alternative sequence (1); Chain (1); Coiled coil (2); Compositional bias (2); Cross-link (4); Domain (2); Erroneous initiation (3); Initiator methionine (1); Modified residue (24); Sequence conflict (2) FUNCTION: When overexpressed, acts as a general inhibitor of transcription that eventually leads to apoptosis. {ECO:0000269|PubMed:17630952}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17630952}. Note=Detected in punctate structures. +Q91ZW3 SMCA5_MOUSE SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5 (EC 3.6.4.-) (Sucrose nonfermenting protein 2 homolog) (mSnf2h) 1051 121,627 Chain (1); Compositional bias (1); Cross-link (7); Domain (4); Erroneous initiation (1); Initiator methionine (1); Modified residue (9); Motif (1); Nucleotide binding (1); Sequence conflict (7) FUNCTION: Helicase that possesses intrinsic ATP-dependent nucleosome-remodeling activity. Complexes containing SMARCA5 are capable of forming ordered nucleosome arrays on chromatin; this may require intact histone H4 tails. Also required for replication of pericentric heterochromatin in S-phase specifically in conjunction with BAZ1A. Probably plays a role in repression of polI dependent transcription of the rDNA locus, through the recruitment of the SIN3/HDAC1 corepressor complex to the rDNA promoter. Essential component of the WICH complex, a chromatin remodeling complex that mobilizes nucleosomes and reconfigures irregular chromatin to a regular nucleosomal array structure. The WICH complex regulates the transcription of various genes, has a role in RNA polymerase I and RNA polymerase III transcription, mediates the histone H2AX phosphorylation at 'Tyr-142', and is involved in the maintenance of chromatin structures during DNA replication processes. Essential component of the NoRC (nucleolar remodeling complex) complex, a complex that mediates silencing of a fraction of rDNA by recruiting histone-modifying enzymes and DNA methyltransferases, leading to heterochromatin formation and transcriptional silencing. {ECO:0000269|PubMed:11532953, ECO:0000269|PubMed:11980720, ECO:0000269|PubMed:12198165, ECO:0000269|PubMed:12368916, ECO:0000269|PubMed:14617767, ECO:0000269|PubMed:19092802}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00624, ECO:0000269|PubMed:11532953}. SUBUNIT: Catalytic subunit of the four known chromatin-remodeling complexes: CHRAC, RSF, ACF/WCRF, and WICH. Each complex contains subunits which may regulate the specificity or catalytic activity of SMARCA5. ACF/WCRF contains BAZ1A; CHRAC contains BAZ1A, CHRAC1, and POLE3; RSF contains HBXAP; WICH contains BAZ1B/WSTF. SMARCA5 is the catalytic subunit of the NoRC chromatin-remodeling complex, which also contains BAZ2A/TIP5. The BAZ2A/TIP5 subunit of NoRC also interacts with DNMT1, DNMT3B and HDAC1, which allows NoRC to actively suppress rDNA transcription by a combination of nucleosome remodeling, histone deacetylation, and DNA methylation. Catalytic subunit of SMARCA5/cohesin/NuRD complexes. Component of the B-WICH complex, at least composed of SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21. Interacts with MYO1C. Interacts with BEND3 (By similarity). {ECO:0000250|UniProtKB:O60264, ECO:0000269|PubMed:11532953, ECO:0000269|PubMed:11980720, ECO:0000269|PubMed:12198165, ECO:0000269|PubMed:12368916, ECO:0000269|PubMed:16514417, ECO:0000269|PubMed:19092802}. TISSUE SPECIFICITY: Ubiquitously expressed. +Q62189 SNRPA_MOUSE U1 small nuclear ribonucleoprotein A (U1 snRNP A) (U1-A) (U1A) 287 31,835 Chain (1); Compositional bias (1); Domain (2); Modified residue (2) FUNCTION: Component of the spliceosomal U1 snRNP, which is essential for recognition of the pre-mRNA 5' splice-site and the subsequent assembly of the spliceosome. U1 snRNP is the first snRNP to interact with pre-mRNA. This interaction is required for the subsequent binding of U2 snRNP and the U4/U6/U5 tri-snRNP. SNRPA binds stem loop II of U1 snRNA. In a snRNP-free form (SF-A) may be involved in coupled pre-mRNA splicing and polyadenylation process. May bind preferentially to the 5'-UGCAC-3' motif on RNAs (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: U1 snRNP is composed of the 7 core Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP, and at least three U1 snRNP-specific proteins SNRNP70/U1-70K, SNRPA/U1-A and SNRPC/U1-C. Interacts with SFPQ; component of a snRNP-free complex with SFPQ (By similarity). {ECO:0000250}. +Q8C9X1 SNTAN_MOUSE Sentan (Protein S100-A1-like) (S100 calcium-binding protein A1-like) 147 16,415 Chain (1) FUNCTION: May be a component of the linker structure that bridges the ciliary membrane and peripheral singlet microtubules. {ECO:0000269|PubMed:18829862}. SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000269|PubMed:18829862}. Note=Expressed exclusively at the cilium tip where it localizes between the cell membrane and peripheral A-subfibers. TISSUE SPECIFICITY: Expressed exclusively in ciliated epithelial cells. Detected in ciliated epithelium of trachea and oviduct (at protein level). {ECO:0000269|PubMed:18829862}. +Q99L88 SNTB1_MOUSE Beta-1-syntrophin (59 kDa dystrophin-associated protein A1 basic component 1) (DAPA1B) (Syntrophin-2) 537 58,081 Alternative sequence (2); Chain (1); Compositional bias (2); Domain (4); Initiator methionine (1); Modified residue (10); Region (1) FUNCTION: Adapter protein that binds to and probably organizes the subcellular localization of a variety of membrane proteins. May link various receptors to the actin cytoskeleton and the dystrophin glycoprotein complex. PTM: Phosphorylated by CaM-kinase II. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000269|PubMed:9214383}; Peripheral membrane protein {ECO:0000269|PubMed:9214383}; Cytoplasmic side {ECO:0000269|PubMed:9214383}. Cell junction {ECO:0000269|PubMed:9214383}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9214383}. Note=In skeletal muscle, it localizes at the cytoplasmic side of the sarcolemmal membrane and at neuromuscular junctions. SUBUNIT: Monomer and homodimer (Probable). Interacts with the viral HTLV-1 TAX protein and other members of the syntrophin family: SNTA1 and SNTB2 (By similarity). Interacts with the dystrophin protein DMD and related proteins DTNA and UTRN and with the sodium channel proteins SCN4A and SCN5A. {ECO:0000250, ECO:0000269|PubMed:9214383, ECO:0000269|PubMed:9412493, ECO:0000305}. DOMAIN: The PH 1 domain mediates the oligomerization in a calcium dependent manner. {ECO:0000250}.; DOMAIN: The PDZ domain binds to the last three or four amino acids of ion channels and receptor proteins. The association with dystrophin or related proteins probably leaves the PDZ domain available to recruit proteins to the membrane (By similarity). {ECO:0000250}.; DOMAIN: The SU domain binds calmodulin in a calcium-dependent manner. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. Expressed at high levels in the liver. +Q8BHS8 SYBU_MOUSE Syntabulin (Golgi-localized syntaphilin-related protein) (m-Golsyn) (Syntaxin-1-binding protein) 665 73,024 Alternative sequence (6); Chain (1); Coiled coil (1); Compositional bias (1); Erroneous initiation (1); Modified residue (4); Region (2); Sequence conflict (3); Transmembrane (1) TRANSMEM 609 629 Helical. {ECO:0000255}. FUNCTION: Part of a kinesin motor-adapter complex that is critical for the anterograde axonal transport of active zone components and contributes to activity-dependent presynaptic assembly during neuronal development. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=Colocalizes with syntaxin vesicles along microtubules in neuronal processes. {ECO:0000250}. SUBUNIT: Interacts with STX1A and KIF5B. {ECO:0000250}. +Q5SUV1 RSAD1_MOUSE Radical S-adenosyl methionine domain-containing protein 1, mitochondrial (EC 1.3.99.-) (Oxygen-independent coproporphyrinogen-III oxidase-like protein RSAD1) 442 48,665 Binding site (7); Chain (1); Metal binding (3); Region (1); Transit peptide (1) FUNCTION: May be involved in porphyrin cofactor biosynthesis. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}. +Q8VDX6 RXLT1_MOUSE Ribitol-5-phosphate xylosyltransferase 1 (EC 2.4.2.-) (Transmembrane protein 5) (UDP-D-xylose:ribitol-5-phosphate beta1,4-xylosyltransferase) 444 51,386 Chain (1); Topological domain (2); Transmembrane (1) TRANSMEM 10 30 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 9 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 31 444 Extracellular. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: UDP-xylosyltransferase involved in the biosynthesis of the phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-3-N-acetylglucosamine-beta-4-(phosphate-6-)mannose), a carbohydrate structure present in alpha-dystroglycan (DAG1), which is required for binding laminin G-like domain-containing extracellular proteins with high affinity (By similarity). Acts as a UDP-D-xylose:ribitol-5-phosphate beta1,4-xylosyltransferase, which catalyzes the transfer of UDP-D-xylose to ribitol 5-phosphate (Rbo5P) to form the Xylbeta1-4Rbo5P linkage on O-mannosyl glycan (By similarity). {ECO:0000250|UniProtKB:Q9Y2B1}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9Y2B1}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9Y2B1}. SUBUNIT: Forms a complex composed of FKTN/fukutin, FKRP and RXYLT1/TMEM5. {ECO:0000250|UniProtKB:Q9Y2B1}. +P27005 S10A8_MOUSE Protein S100-A8 (Calgranulin-A) (Chemotactic cytokine CP-10) (Leukocyte L1 complex light chain) (Migration inhibitory factor-related protein 8) (MRP-8) (p8) (Pro-inflammatory S100 cytokine) (S100 calcium-binding protein A8) 89 10,295 Calcium binding (2); Chain (1); Domain (2); Initiator methionine (1); Metal binding (3); Modified residue (1); Sequence conflict (1) FUNCTION: S100A8 is a calcium- and zinc-binding protein which plays a prominent role in the regulation of inflammatory processes and immune response. It can induce neutrophil chemotaxis and adhesion. Predominantly found as calprotectin (S100A8/A9) which has a wide plethora of intra- and extracellular functions. The intracellular functions include: facilitating leukocyte arachidonic acid trafficking and metabolism, modulation of the tubulin-dependent cytoskeleton during migration of phagocytes and activation of the neutrophilic NADPH-oxidase. Activates NADPH-oxidase by facilitating the enzyme complex assembly at the cell membrane, transferring arachidonic acid, an essential cofactor, to the enzyme complex and S100A8 contributes to the enzyme assembly by directly binding to NCF2/P67PHOX. The extracellular functions involve proinflammatory, antimicrobial, oxidant-scavenging and apoptosis-inducing activities. Its proinflammatory activity includes recruitment of leukocytes, promotion of cytokine and chemokine production, and regulation of leukocyte adhesion and migration. Acts as an alarmin or a danger associated molecular pattern (DAMP) molecule and stimulates innate immune cells via binding to pattern recognition receptors such as Toll-like receptor 4 (TLR4) and receptor for advanced glycation endproducts (AGER). Binding to TLR4 and AGER activates the MAP-kinase and NF-kappa-B signaling pathways resulting in the amplification of the proinflammatory cascade. Has antimicrobial activity towards bacteria and fungi and exerts its antimicrobial activity probably via chelation of Zn(2+) which is essential for microbial growth. Can induce cell death via autophagy and apoptosis and this occurs through the cross-talk of mitochondria and lysosomes via reactive oxygen species (ROS) and the process involves BNIP3. Can regulate neutrophil number and apoptosis by an anti-apoptotic effect; regulates cell survival via ITGAM/ITGB and TLR4 and a signaling mechanism involving MEK-ERK. Its role as an oxidant scavenger has a protective role in preventing exaggerated tissue damage by scavenging oxidants. The iNOS-S100A8/A9 transnitrosylase complex is proposed to direct selective inflammatory stimulus-dependent S-nitrosylation of multiple targets such as GAPDH, ANXA5, EZR, MSN and VIM by recognizing a [IL]-x-C-x-x-[DE] motif; S100A8 seems to contribute to S-nitrosylation site selectivity (By similarity). {ECO:0000250|UniProtKB:P05109, ECO:0000269|PubMed:17767165, ECO:0000269|PubMed:18403730}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17767165}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Predominantly localized in the cytoplasm. Upon elevation of the intracellular calcium level, translocated from the cytoplasm to the cytoskeleton and the cell membrane. Upon neutrophil activation or endothelial adhesion of monocytes, is secreted via a microtubule-mediated, alternative pathway. SUBUNIT: Homodimer. Preferentially exists as a heterodimer or heterotetramer with S100A9 known as calprotectin (S100A8/A9). Calprotectin (S100A8/9) interacts with CEACAM3 and tubulin filaments in a calcium-dependent manner. Heterotetrameric calprotectin (S100A8/A9) interacts with ANXA6 and associates with tubulin filaments in activated monocytes. S100A8 and calprotectin (S100A8/9) interact with NCF2/P67PHOX, RAC1 and RAC2. Calprotectin (S100A8/9) interacts with CYBA and CYBB (By similarity). S100A8 interacts with AGER, ATP2A2 and with the heterodimeric complex formed by TLR4 and LY96. Calprotectin (S100A8/9) interacts with NOS2 to form the iNOS-S100A8/A9 transnitrosylase complex (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P05109, ECO:0000269|PubMed:17767165, ECO:0000269|PubMed:18403730}. +Q924N4 S12A6_MOUSE Solute carrier family 12 member 6 (Electroneutral potassium-chloride cotransporter 3) (K-Cl cotransporter 3) 1150 127,527 Alternative sequence (2); Chain (1); Compositional bias (1); Glycosylation (1); Modified residue (4); Sequence conflict (2); Topological domain (7); Transmembrane (12) TRANSMEM 186 206 Helical. {ECO:0000255}.; TRANSMEM 208 228 Helical. {ECO:0000255}.; TRANSMEM 236 256 Helical. {ECO:0000255}.; TRANSMEM 277 297 Helical. {ECO:0000255}.; TRANSMEM 320 340 Helical. {ECO:0000255}.; TRANSMEM 343 363 Helical. {ECO:0000255}.; TRANSMEM 481 501 Helical. {ECO:0000255}.; TRANSMEM 518 538 Helical. {ECO:0000255}.; TRANSMEM 559 579 Helical. {ECO:0000255}.; TRANSMEM 632 652 Helical. {ECO:0000255}.; TRANSMEM 690 710 Helical. {ECO:0000255}.; TRANSMEM 789 809 Helical. {ECO:0000255}. TOPO_DOM 1 185 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 229 235 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 298 319 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 364 480 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 539 558 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 653 689 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 810 1150 Cytoplasmic. {ECO:0000255}. FUNCTION: Mediates electroneutral potassium-chloride cotransport. May be activated by cell swelling. May contribute to cell volume homeostasis in single cells. {ECO:0000269|PubMed:10347194}. PTM: N-glycosylated. {ECO:0000269|PubMed:11246162}. SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000269|PubMed:16048901}; Multi-pass membrane protein {ECO:0000269|PubMed:16048901}. SUBUNIT: Homomultimer and heteromultimer with other K-Cl cotransporters. {ECO:0000250}. TISSUE SPECIFICITY: Isoform 1 is highly expressed throughout the brain and detected at lower levels in kidney. Highly expressed in highly myelinated white matter of the brain, but not in gray matter. Detected in the corpus callosum, in packed cell layers of the hippocampus and in Purkinje neurons within the cerebellum. Highly expressed in white matter in the spinal cord, but not in dorsal root ganglia or sciatic nerve. Colocalizes with the oligodendrocyte marker CNP. Isoform 2 is highly expressed in kidney, but not detected in brain. {ECO:0000269|PubMed:16048901}. DISEASE: Note=Defects in Slc12a6 are a cause of locomotor abnormalities beginning at 2 weeks of age. Slc12a6 deficient mice show hypomyelination, decompaction of myelin, demyelination, axonal swelling and fiber degeneration. {ECO:0000269|PubMed:12368912}. +P62305 RUXE_MOUSE Small nuclear ribonucleoprotein E (snRNP-E) (Sm protein E) (Sm-E) (SmE) 92 10,804 Chain (1) FUNCTION: Plays role in pre-mRNA splicing as core component of the SMN-Sm complex that mediates spliceosomal snRNP assembly and as component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Component of both the pre-catalytic spliceosome B complex and activated spliceosome C complexes. Is also a component of the minor U12 spliceosome. As part of the U7 snRNP it is involved in histone 3'-end processing. May indirectly play a role in hair development. {ECO:0000250|UniProtKB:P62304}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P62304}. Nucleus {ECO:0000250|UniProtKB:P62304}. Note=SMN-mediated assembly into core snRNPs occurs in the cytosol before SMN-mediated transport to the nucleus to be included in spliceosomes. {ECO:0000250|UniProtKB:P62304}. SUBUNIT: Core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Most spliceosomal snRNPs contain a common set of Sm proteins, SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. Component of the U1 snRNP. The U1 snRNP is composed of the U1 snRNA and the 7 core Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG, and at least three U1 snRNP-specific proteins SNRNP70/U1-70K, SNRPA/U1-A and SNRPC/U1-C. Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39, plus LSM2, LSM3, LSM4, LSM5, LSM6, LSM7 and LSM8. Component of the U7 snRNP complex, or U7 Sm protein core complex, that is composed of the U7 snRNA and at least LSM10, LSM11, SNRPB, SNRPD3, SNRPE, SNRPF and SNRPG; the complex does not contain SNRPD1 and SNRPD2. Component of the U11/U12 snRNPs that are part of the U12-type spliceosome. Part of the SMN-Sm complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8, STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG; catalyzes core snRNPs assembly. Forms a 6S pICln-Sm complex composed of CLNS1A/pICln, SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG; ring-like structure where CLNS1A/pICln mimics additional Sm proteins and which is unable to assemble into the core snRNP. {ECO:0000250|UniProtKB:P62304}. +Q9WVL3 S12A7_MOUSE Solute carrier family 12 member 7 (Electroneutral potassium-chloride cotransporter 4) (K-Cl cotransporter 4) 1083 119,481 Alternative sequence (1); Chain (1); Erroneous initiation (1); Frameshift (1); Glycosylation (4); Modified residue (7); Sequence conflict (3); Topological domain (7); Transmembrane (12) TRANSMEM 119 139 Helical. {ECO:0000255}.; TRANSMEM 141 161 Helical. {ECO:0000255}.; TRANSMEM 201 221 Helical. {ECO:0000255}.; TRANSMEM 253 273 Helical. {ECO:0000255}.; TRANSMEM 276 296 Helical. {ECO:0000255}.; TRANSMEM 416 436 Helical. {ECO:0000255}.; TRANSMEM 457 477 Helical. {ECO:0000255}.; TRANSMEM 494 514 Helical. {ECO:0000255}.; TRANSMEM 554 574 Helical. {ECO:0000255}.; TRANSMEM 578 598 Helical. {ECO:0000255}.; TRANSMEM 625 645 Helical. {ECO:0000255}.; TRANSMEM 845 865 Helical. {ECO:0000255}. TOPO_DOM 1 118 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 162 200 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 274 275 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 437 456 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 515 553 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 599 624 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 866 1083 Cytoplasmic. {ECO:0000255}. FUNCTION: Mediates electroneutral potassium-chloride cotransport when activated by cell swelling (By similarity). May mediate K(+) uptake into Deiters' cells in the cochlea and contribute to K(+) recycling in the inner ear. Important for the survival of cochlear outer and inner hair cells and the maintenance of the organ of Corti. May be required for basolateral Cl(-) extrusion in the kidney and contribute to renal acidification. {ECO:0000250, ECO:0000269|PubMed:11976689}. PTM: Glycosylation at Asn-331 and Asn-344 is required for proper trafficking to the cell surface, and augments protein stability. {ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:19656770, ECO:0000269|PubMed:23376777}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23376777}; Multi-pass membrane protein {ECO:0000269|PubMed:23376777}. SUBUNIT: Homomultimer and heteromultimer with other K-Cl cotransporters. {ECO:0000305|PubMed:11551954}. TISSUE SPECIFICITY: Detected in proximal tubules in the kidney, in particular in basolateral membranes of intercalated cells in the cortical collecting duct. DISEASE: Note=Defects in Slc12a7 are a cause of deafness due to the progressive degeneration of outer and inner hair cells in the cochlea and of neurons in the cochlear ganglion, leading to the loss of the organ of Corti. {ECO:0000269|PubMed:11976689}. +Q9JHI4 S13A1_MOUSE Solute carrier family 13 member 1 (NaSi-1) (Renal sodium/sulfate cotransporter) (Na(+)/sulfate cotransporter) 594 66,084 Alternative sequence (2); Chain (1); Frameshift (1); Glycosylation (2); Sequence conflict (3); Transmembrane (13) TRANSMEM 13 33 Helical. {ECO:0000255}.; TRANSMEM 40 60 Helical. {ECO:0000255}.; TRANSMEM 77 97 Helical. {ECO:0000255}.; TRANSMEM 113 133 Helical. {ECO:0000255}.; TRANSMEM 134 154 Helical. {ECO:0000255}.; TRANSMEM 239 259 Helical. {ECO:0000255}.; TRANSMEM 283 303 Helical. {ECO:0000255}.; TRANSMEM 347 367 Helical. {ECO:0000255}.; TRANSMEM 380 400 Helical. {ECO:0000255}.; TRANSMEM 461 481 Helical. {ECO:0000255}.; TRANSMEM 487 507 Helical. {ECO:0000255}.; TRANSMEM 511 531 Helical. {ECO:0000255}.; TRANSMEM 552 572 Helical. {ECO:0000255}. FUNCTION: Sodium/sulfate cotransporter that mediates sulfate reabsorption in the kidney. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Highly expressed in kidney and ileum, detected at lower levels in duodenum/jejunum and colon, and at very low levels in cecum, testis, adrenal and adipose tissues. Expression of isoform 2 is very low. +Q8R0Y8 S2542_MOUSE Mitochondrial coenzyme A transporter SLC25A42 (Solute carrier family 25 member 42) 318 35,241 Chain (1); Repeat (3); Transmembrane (6) TRANSMEM 33 53 Helical; Name=1. {ECO:0000255}.; TRANSMEM 89 109 Helical; Name=2. {ECO:0000255}.; TRANSMEM 135 155 Helical; Name=3. {ECO:0000255}.; TRANSMEM 186 206 Helical; Name=4. {ECO:0000255}.; TRANSMEM 230 250 Helical; Name=5. {ECO:0000255}.; TRANSMEM 293 313 Helical; Name=6. {ECO:0000255}. FUNCTION: Mitochondrial carrier mediating the transport of coenzyme A (CoA) in mitochondria in exchange for intramitochondrial (deoxy)adenine nucleotides and adenosine 3',5'-diphosphate. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. +A8Y5H7 S14L1_MOUSE SEC14-like protein 1 715 81,216 Alternative sequence (2); Chain (1); Domain (3); Modified residue (2); Region (1); Sequence conflict (1) FUNCTION: May play a role in innate immunity by inhibiting the antiviral RIG-I signaling pathway. In this pathway, functions as a negative regulator of DDX58/RIG-I, the cytoplasmic sensor of viral nucleic acids. Prevents the interaction of DDX58 with MAVS/IPS1, an important step in signal propagation. May also regulate the SLC18A3 and SLC5A7 cholinergic transporters. {ECO:0000250|UniProtKB:Q92503}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q92503}. Golgi apparatus {ECO:0000250|UniProtKB:Q92503}. SUBUNIT: Interacts with DDX58 (via tandem CARD domain); the interaction is direct. Interacts (via GOLD domain) with SLC18A3; the interaction is direct. Interacts with SLC5A7 (via GOLD domain); the interaction is direct. {ECO:0000250|UniProtKB:Q92503}. +Q99NH7 S26A5_MOUSE Prestin (Solute carrier family 26 member 5) 744 81,337 Chain (1); Domain (1); Glycosylation (2); Sequence conflict (1); Topological domain (13); Transmembrane (12) TRANSMEM 80 100 Helical; Name=1. {ECO:0000255}.; TRANSMEM 103 123 Helical; Name=2. {ECO:0000255}.; TRANSMEM 132 152 Helical; Name=3. {ECO:0000255}.; TRANSMEM 185 205 Helical; Name=4. {ECO:0000255}.; TRANSMEM 212 232 Helical; Name=5. {ECO:0000255}.; TRANSMEM 254 274 Helical; Name=6. {ECO:0000255}.; TRANSMEM 287 307 Helical; Name=7. {ECO:0000255}.; TRANSMEM 335 355 Helical; Name=8. {ECO:0000255}.; TRANSMEM 375 395 Helical; Name=9. {ECO:0000255}.; TRANSMEM 412 432 Helical; Name=10. {ECO:0000255}.; TRANSMEM 442 462 Helical; Name=11. {ECO:0000255}.; TRANSMEM 480 500 Helical; Name=12. {ECO:0000255}. TOPO_DOM 1 79 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 101 102 Extracellular. {ECO:0000255}.; TOPO_DOM 124 131 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 153 184 Extracellular. {ECO:0000255}.; TOPO_DOM 206 211 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 233 253 Extracellular. {ECO:0000255}.; TOPO_DOM 275 286 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 308 334 Extracellular. {ECO:0000255}.; TOPO_DOM 356 374 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 396 411 Extracellular. {ECO:0000255}.; TOPO_DOM 433 441 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 463 479 Extracellular. {ECO:0000255}.; TOPO_DOM 501 744 Cytoplasmic. {ECO:0000255}. FUNCTION: Motor protein that converts auditory stimuli to length changes in outer hair cells and mediates sound amplification in the mammalian hearing organ. Prestin is a bidirectional voltage-to-force converter, it can operate at microsecond rates. It uses cytoplasmic anions as extrinsic voltage sensors, probably chloride and bicarbonate. After binding to a site with millimolar affinity, these anions are translocated across the membrane in response to changes in the transmembrane voltage. They move towards the extracellular surface following hyperpolarization, and towards the cytoplasmic side in response to depolarization. As a consequence, this translocation triggers conformational changes in the protein that ultimately alter its surface area in the plane of the plasma membrane. The area decreases when the anion is near the cytoplasmic face of the membrane (short state), and increases when the ion has crossed the membrane to the outer surface (long state). So, it acts as an incomplete transporter. It swings anions across the membrane, but does not allow these anions to dissociate and escape to the extracellular space. Salicylate, an inhibitor of outer hair cell motility, acts as competitive antagonist at the prestin anion-binding site (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Lateral wall of outer hair cells. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the outer hair cells (OHC) of the organ of Corti of the inner ear. Also weak expression in brain and testis. Very weakly expressed in heart, spleen, muscle and lactating mammary glands. {ECO:0000269|PubMed:12584604}. +Q9CQS4 S2546_MOUSE Solute carrier family 25 member 46 418 46,224 Chain (1); Modified residue (3); Repeat (2); Sequence conflict (3); Transmembrane (6) TRANSMEM 103 123 Helical; Name=1. {ECO:0000255}.; TRANSMEM 167 187 Helical; Name=2. {ECO:0000255}.; TRANSMEM 202 222 Helical; Name=3. {ECO:0000255}.; TRANSMEM 258 278 Helical; Name=4. {ECO:0000255}.; TRANSMEM 314 334 Helical; Name=5. {ECO:0000255}.; TRANSMEM 382 402 Helical; Name=6. {ECO:0000255}. FUNCTION: May play a role in mitochondrial dynamics by controlling mitochondrial membrane fission. {ECO:0000250|UniProtKB:Q96AG3}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q96AG3}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Interacts with IMMT. {ECO:0000250|UniProtKB:Q96AG3}. +Q8VC69 S22A6_MOUSE Solute carrier family 22 member 6 (Kidney-specific transport protein) (Novel kidney transcript) (mNKT) (Organic anion transporter 1) (Renal organic anion transporter 1) (mROAT1) 545 60,013 Chain (1); Glycosylation (6); Mutagenesis (5); Sequence conflict (1); Topological domain (13); Transmembrane (12) TRANSMEM 10 30 Helical. {ECO:0000255}.; TRANSMEM 130 150 Helical. {ECO:0000255}.; TRANSMEM 158 177 Helical. {ECO:0000255}.; TRANSMEM 181 201 Helical. {ECO:0000255}.; TRANSMEM 219 239 Helical. {ECO:0000255}.; TRANSMEM 243 263 Helical. {ECO:0000255}.; TRANSMEM 332 352 Helical. {ECO:0000255}.; TRANSMEM 363 383 Helical. {ECO:0000255}.; TRANSMEM 390 410 Helical. {ECO:0000255}.; TRANSMEM 420 440 Helical. {ECO:0000255}.; TRANSMEM 451 471 Helical. {ECO:0000255}.; TRANSMEM 479 499 Helical. {ECO:0000255}. TOPO_DOM 1 9 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 31 129 Extracellular. {ECO:0000255}.; TOPO_DOM 151 157 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 178 180 Extracellular. {ECO:0000255}.; TOPO_DOM 202 218 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 240 242 Extracellular. {ECO:0000255}.; TOPO_DOM 264 331 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 353 362 Extracellular. {ECO:0000255}.; TOPO_DOM 384 389 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 411 419 Extracellular. {ECO:0000255}.; TOPO_DOM 441 450 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 472 478 Extracellular. {ECO:0000255}.; TOPO_DOM 500 545 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in the renal elimination of endogenous and exogenous organic anions. Functions as organic anion exchanger when the uptake of one molecule of organic anion is coupled with an efflux of one molecule of endogenous dicarboxylic acid (glutarate, ketoglutarate, etc). Mediates the sodium-independent uptake of 2,3-dimercapto-1-propanesulfonic acid (DMPS), cidofovir, adefovir, 9-(2-phosphonylmethoxyethyl) guanine (PMEG), 9-(2-phosphonylmethoxyethyl) diaminopurine (PMEDAP), ochratoxin (OTA), acyclovir (ACV), 3'-azido-3-'deoxythymidine (AZT), cimetidine (CMD), 2,4-dichloro-phenoxyacetate (2,4-D), hippurate (HA), indoleacetate (IA), indoxyl sulfate (IS) and 3-carboxy-4-methyl-5-propyl-2-furanpropionate (CMPF) and edaravone sulfate (By similarity). Mediates the sodium-independent uptake of p-aminohippurate (PAH). PAH uptake is inhibited by benzothiazolylcysteine (BTC), S-chlorotrifluoroethylcysteine (CTFC), cysteine S-conjugates S-dichlorovinylcysteine (DCVC), furosemide, steviol, phorbol 12-myristate 13-acetate (PMA), calcium ionophore A23187, benzylpenicillin, bumetamide, losartan, probenecid, phenol red, urate, glutarate and alpha-ketoglutarate (By similarity). PAH uptake is inhibited by p-chloromercuribenzenesulphonate (PCMBS), diethyl pyrocarbonate (DEPC), indomethacin, sulindac, diclofenac, carprofen, okadaic acid and PKC activators. {ECO:0000250, ECO:0000269|PubMed:10744714, ECO:0000269|PubMed:14979872, ECO:0000269|PubMed:9880528}. PTM: Glycosylated. Glycosylation is necessary for proper targeting of the transporter to the plasma membrane. {ECO:0000269|PubMed:14749323}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9045672}; Multi-pass membrane protein {ECO:0000269|PubMed:9045672}. Note=Localized to the plasma membrane. DOMAIN: Multiple cysteine residues are necessary for proper targeting to the plasma membrane. TISSUE SPECIFICITY: Expressed in kidney; in the basolateral membrane and at much lower levels in brain. {ECO:0000269|PubMed:9045672, ECO:0000269|PubMed:9880528}. +Q8BW66 S2548_MOUSE Solute carrier family 25 member 48 306 33,387 Chain (1); Repeat (3); Sequence conflict (1); Transmembrane (6) TRANSMEM 9 29 Helical; Name=1. {ECO:0000255}.; TRANSMEM 61 81 Helical; Name=2. {ECO:0000255}.; TRANSMEM 107 127 Helical; Name=3. {ECO:0000255}.; TRANSMEM 184 204 Helical; Name=4. {ECO:0000255}.; TRANSMEM 212 232 Helical; Name=5. {ECO:0000255}.; TRANSMEM 272 290 Helical; Name=6. {ECO:0000255}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q8BGK5 S35F1_MOUSE Solute carrier family 35 member F1 408 45,304 Chain (1); Compositional bias (1); Sequence caution (1); Sequence conflict (3); Transmembrane (10) TRANSMEM 60 80 Helical. {ECO:0000255}.; TRANSMEM 94 114 Helical. {ECO:0000255}.; TRANSMEM 129 147 Helical. {ECO:0000255}.; TRANSMEM 159 179 Helical. {ECO:0000255}.; TRANSMEM 186 206 Helical. {ECO:0000255}.; TRANSMEM 221 241 Helical. {ECO:0000255}.; TRANSMEM 247 267 Helical. {ECO:0000255}.; TRANSMEM 284 304 Helical. {ECO:0000255}.; TRANSMEM 311 331 Helical. {ECO:0000255}.; TRANSMEM 335 355 Helical. {ECO:0000255}. FUNCTION: Putative solute transporter. {ECO:0000305}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q3V050 S47A2_MOUSE Multidrug and toxin extrusion protein 2 (MATE-2) (mMATE-2) (H(+)/organic cation antiporter kidney-specific) (Solute carrier family 47 member 2) 573 61,789 Chain (1); Erroneous gene model prediction (1); Topological domain (14); Transmembrane (13) TRANSMEM 47 67 Helical. {ECO:0000255}.; TRANSMEM 82 102 Helical. {ECO:0000255}.; TRANSMEM 123 143 Helical. {ECO:0000255}.; TRANSMEM 162 182 Helical. {ECO:0000255}.; TRANSMEM 197 217 Helical. {ECO:0000255}.; TRANSMEM 226 246 Helical. {ECO:0000255}.; TRANSMEM 267 286 Helical. {ECO:0000255}.; TRANSMEM 305 325 Helical. {ECO:0000255}.; TRANSMEM 346 366 Helical. {ECO:0000255}.; TRANSMEM 380 400 Helical. {ECO:0000255}.; TRANSMEM 416 436 Helical. {ECO:0000255}.; TRANSMEM 444 464 Helical. {ECO:0000255}.; TRANSMEM 546 566 Helical. {ECO:0000255}. TOPO_DOM 1 46 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 68 81 Extracellular. {ECO:0000255}.; TOPO_DOM 103 122 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 144 161 Extracellular. {ECO:0000255}.; TOPO_DOM 183 196 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 218 225 Extracellular. {ECO:0000255}.; TOPO_DOM 247 266 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 287 304 Extracellular. {ECO:0000255}.; TOPO_DOM 326 345 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 367 379 Extracellular. {ECO:0000255}.; TOPO_DOM 401 415 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 437 443 Extracellular. {ECO:0000255}.; TOPO_DOM 465 545 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 567 573 Extracellular. {ECO:0000255}. FUNCTION: Solute transporter for tetraethylammonium (TEA), cimetidine, choline, procainamide, cimetidine, quinidine, guanidine, N-methylnicotinamide (NMN). Responsible for the secretion of cationic drugs across the brush border membranes. {ECO:0000269|PubMed:17715386}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=Localized to the plasma membrane and to the intracellular organelles. {ECO:0000269|PubMed:17715386}. TISSUE SPECIFICITY: Expressed in testis; especially in testicular Leydig cells. {ECO:0000269|PubMed:17715386}. +Q8BXR1 S7A14_MOUSE Probable cationic amino acid transporter (Solute carrier family 7 member 14) 771 83,984 Chain (1); Erroneous initiation (1); Glycosylation (2); Modified residue (6); Transmembrane (14) TRANSMEM 58 78 Helical. {ECO:0000255}.; TRANSMEM 83 103 Helical. {ECO:0000255}.; TRANSMEM 119 141 Helical. {ECO:0000255}.; TRANSMEM 187 207 Helical. {ECO:0000255}.; TRANSMEM 216 236 Helical. {ECO:0000255}.; TRANSMEM 251 271 Helical. {ECO:0000255}.; TRANSMEM 291 311 Helical. {ECO:0000255}.; TRANSMEM 336 356 Helical. {ECO:0000255}.; TRANSMEM 384 404 Helical. {ECO:0000255}.; TRANSMEM 407 427 Helical. {ECO:0000255}.; TRANSMEM 565 585 Helical. {ECO:0000255}.; TRANSMEM 596 616 Helical. {ECO:0000255}.; TRANSMEM 628 648 Helical. {ECO:0000255}.; TRANSMEM 655 675 Helical. {ECO:0000255}. FUNCTION: May be involved in arginine transport. {ECO:0000250}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Exhibits a punctated pattern in the cytoplasm, which partially ovelaps with lysosomes. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in retina, brain and spinal cord. In the retina, expressed in the inner nuclear layer and photoreceptor layer (at protein level). {ECO:0000269|PubMed:24670872}. +Q75N73 S39AE_MOUSE Zinc transporter ZIP14 (Factor for adipocyte differentiation 123) (FAD-123) (Solute carrier family 39 member 14) (Zrt- and Irt-like protein 14) (ZIP-14) 489 53,962 Alternative sequence (1); Chain (1); Glycosylation (4); Motif (2); Mutagenesis (1); Sequence conflict (4); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 156 176 Helical. {ECO:0000255}.; TRANSMEM 185 205 Helical. {ECO:0000255}.; TRANSMEM 222 242 Helical. {ECO:0000255}.; TRANSMEM 350 370 Helical. {ECO:0000255}.; TRANSMEM 395 415 Helical. {ECO:0000255}.; TRANSMEM 422 442 Helical. {ECO:0000255}.; TRANSMEM 458 478 Helical. {ECO:0000255}. TOPO_DOM 29 155 Extracellular. {ECO:0000255}.; TOPO_DOM 177 184 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 206 221 Extracellular. {ECO:0000255}.; TOPO_DOM 243 349 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 371 394 Extracellular. {ECO:0000255}.; TOPO_DOM 416 421 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 443 457 Extracellular. {ECO:0000255}.; TOPO_DOM 479 489 Cytoplasmic. {ECO:0000255}. FUNCTION: Broad-scope metal ion transporter with a preference for zinc uptake. Also mediates cellular uptake of nontransferrin-bound iron. {ECO:0000269|PubMed:15794747, ECO:0000269|PubMed:15863613, ECO:0000269|PubMed:16950869, ECO:0000269|PubMed:17065364, ECO:0000269|PubMed:21653899}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15794747, ECO:0000269|PubMed:15863613, ECO:0000269|PubMed:16950869}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:Q15043}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q15043}. Note=Localized to the plasma membrane and also found colocalized with F-actin concentrated on lamellipodiae. {ECO:0000250|UniProtKB:Q15043, ECO:0000269|PubMed:15794747, ECO:0000269|PubMed:15863613, ECO:0000269|PubMed:16950869}. SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:Q15043}. TISSUE SPECIFICITY: Highly and transiently expressed during the early stage of adipocyte differentiation. Strongly expressed in liver, preadipocyte, duodenum and jejunum, moderately in brain, heart, skeletal muscle, spleen, pancreas, kidney and white adipose cells. Expression is almost undetectable in lung, testis and brown adipose cells. {ECO:0000269|PubMed:15794747, ECO:0000269|PubMed:15863613, ECO:0000269|PubMed:16950869, ECO:0000269|PubMed:17065364}. +P05367 SAA2_MOUSE Serum amyloid A-2 protein [Cleaved into: Amyloid protein A (Amyloid fibril protein AA)] 122 13,622 Chain (2); Natural variant (1); Signal peptide (1) FUNCTION: Major acute phase reactant. Apolipoprotein of the HDL complex. PTM: This protein is the precursor of amyloid protein A, which is formed by the removal of residues from the C-terminal end. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Expressed by the liver; secreted in plasma. DISEASE: Note=Reactive, secondary amyloidosis is characterized by the extracellular accumulation in various tissues of the SAA protein. These deposits are highly insoluble and resistant to proteolysis; they disrupt tissue structure and compromise function. +P04918 SAA3_MOUSE Serum amyloid A-3 protein 122 13,774 Chain (1); Helix (5); Sequence conflict (1); Signal peptide (1) FUNCTION: Major acute phase reactant. Apolipoprotein of the HDL complex. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. TISSUE SPECIFICITY: Found in various tissues. +Q9R1T2 SAE1_MOUSE SUMO-activating enzyme subunit 1 (Ubiquitin-like 1-activating enzyme E1A) [Cleaved into: SUMO-activating enzyme subunit 1, N-terminally processed] 350 38,620 Alternative sequence (1); Chain (2); Initiator methionine (1); Modified residue (4) Protein modification; protein sumoylation. FUNCTION: The heterodimer acts as an E1 ligase for SUMO1, SUMO2, SUMO3, and probably SUMO4. It mediates ATP-dependent activation of SUMO proteins followed by formation of a thioester bond between a SUMO protein and a conserved active site cysteine residue on UBA2/SAE2 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Heterodimer of SAE1 and UBA2/SAE2. The heterodimer corresponds to the two domains that are encoded on a single polypeptide chain in ubiquitin-activating enzyme E1. Interacts with UBE2I (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Broadly expressed, with highest levels in testis. {ECO:0000269|PubMed:11481243}. +Q9ER74 SALL1_MOUSE Sal-like protein 1 (Zinc finger protein Spalt-3) (Sal-3) (mSal-3) 1322 140,230 Chain (1); Compositional bias (3); Cross-link (10); Modified residue (4); Sequence conflict (3); Zinc finger (9) FUNCTION: Transcriptional repressor involved in organogenesis. Essential for ureteric bud invasion in kidney development. Homozygous deletion of SALL1 results in an incomplete ureteric bud outgrowth, a failure of tubule formation in the mesenchyme and an apoptosis of the mesenchyme. {ECO:0000269|PubMed:11836251}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with HDAC1, HDAC2, RBBP4, RBPP7, MTA1 and MTA2. Interacts with CCNQ (By similarity). Probably associates with NuRD histone deacetylase complex (HDAC). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the metanephric mesenchyme surrounding ureteric bud. +Q9QX96 SALL2_MOUSE Sal-like protein 2 (Spalt-like protein 2) (Zinc finger protein Spalt-2) (Sal-2) (mSal-2) 1004 104,944 Chain (1); Compositional bias (5); Cross-link (1); Modified residue (4); Sequence conflict (5); Zinc finger (7) FUNCTION: Probable transcription factor that plays a role in eye development before, during, and after optic fissure closure. {ECO:0000269|PubMed:24412933}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: Expressed throughout embryonic development. In adult predominantly in brain. +D3YXK1 SAMD1_MOUSE Atherin (Sterile alpha motif domain-containing protein 1) (SAM domain-containing protein 1) 519 54,533 Chain (1); Compositional bias (5); Domain (1); Modified residue (3) FUNCTION: May play a role in atherogenesis by immobilizing LDL in the atherial wall. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Secreted {ECO:0000250}. +Q8C1C1 SAPL1_MOUSE Proactivator polypeptide-like 1 [Cleaved into: Saposin A-like; Saposin B-Val-like; Saposin B-like; Saposin C-like; Saposin D-like] 522 57,061 Chain (5); Disulfide bond (12); Domain (6); Erroneous initiation (1); Frameshift (2); Glycosylation (2); Propeptide (5); Sequence conflict (3); Signal peptide (1) FUNCTION: May activate the lysosomal degradation of sphingolipids. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q60611 SATB1_MOUSE DNA-binding protein SATB1 (Special AT-rich sequence-binding protein 1) 764 85,880 Beta strand (5); Binding site (2); Chain (1); Compositional bias (2); Cross-link (2); DNA binding (3); Helix (10); Modified residue (3); Motif (3); Region (3); Sequence conflict (2); Site (1); Turn (2) FUNCTION: Required for the switching of fetal globin species, and beta- and gamma-globin genes regulation during erythroid differentiation. Plays a role in chromatin organization and nuclear architecture during apoptosis (By similarity). Crucial silencing factor contributing to the initiation of X inactivation mediated by Xist RNA that occurs during embryogenesis and in lymphoma. Binds to DNA at special AT-rich sequences, the consensus SATB1-binding sequence (CSBS), at nuclear matrix- or scaffold-associated regions. Thought to recognize the sugar-phosphate structure of double-stranded DNA. Transcriptional repressor controlling nuclear and viral gene expression in a phosphorylated and acetylated status-dependent manner, by binding to matrix attachment regions (MARs) of DNA and inducing a local chromatin-loop remodeling. Acts as a docking site for several chromatin remodeling enzymes and also by recruiting corepressors (HDACs) or coactivators (HATs) directly to promoters and enhancers. Modulates genes that are essential in the maturation of the immune T-cell CD8SP from thymocytes. {ECO:0000250, ECO:0000269|PubMed:10716941, ECO:0000269|PubMed:11463840, ECO:0000269|PubMed:12692553, ECO:0000269|PubMed:15814699, ECO:0000269|PubMed:17057718, ECO:0000269|PubMed:18722016, ECO:0000269|PubMed:19103759, ECO:0000269|PubMed:19386260, ECO:0000269|PubMed:9271405}. PTM: Sumoylated. Sumoylation promotes cleavage by caspases. {ECO:0000250}.; PTM: Phosphorylated by PKC. Acetylated by PCAF. Phosphorylated form interacts with HDAC1, but unphosphorylated form interacts with PCAF. DNA binding properties are activated by phosphorylation and inactivated by acetylation. In opposition, gene expression is down-regulated by phosphorylation but up-regulated by acetylation (By similarity). {ECO:0000250}.; PTM: Cleaved at Asp-254 by caspase-3 and caspase-6 during T-cell apoptosis in thymus and during B-cell stimulation. The cleaved forms cannot dimerize and lose transcription regulation function because of impaired DNA and chromatin association. {ECO:0000269|PubMed:11463840}. SUBCELLULAR LOCATION: Nucleus. Nucleus, PML body. Note=Organized into a cage-like network anchoring loops of heterochromatin and tethering specialized DNA sequences. When sumoylated, localized in promyelocytic leukemia nuclear bodies (PML NBs) (By similarity). {ECO:0000250}. SUBUNIT: Interacts with PCAF. Interacts with sumoylated PML and HDAC1 Tat via the PDZ-like dimerization domain. Interacts also with DYNLT3 and POLR2J2. Binds to EP300 (By similarity). Homodimer. Part of the nuclear protein complex gamma-globin promoter and enhancer binding factor (gamma-PE) composed at least of SATB1 and HOXB2. Interaction with CtBP1 when not acetylated stabalizes attachment to DNA and promotes transcription repression. Interacts with CUX1 (via DNA-binding domains); the interaction inhibits the attachment of both proteins to DNA. {ECO:0000250, ECO:0000269|PubMed:10373541, ECO:0000269|PubMed:19103759}. TISSUE SPECIFICITY: Mainly expressed in thymus, spleen, and lymph nodes with a lower level observed in the brain. {ECO:0000269|PubMed:15814699}. +Q8BI29 SARG_MOUSE Specifically androgen-regulated gene protein 606 65,092 Alternative sequence (1); Chain (1); Modified residue (6); Sequence conflict (12) FUNCTION: Putative androgen-specific receptor. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +Q6QR59 TCAF3_MOUSE TRPM8 channel-associated factor 3 (Experimental autoimmune prostatitis antigen 2) 914 102,243 Chain (1); Domain (1) FUNCTION: May play a role in the regulation of the cation channel TRPM8 activity. {ECO:0000250|UniProtKB:A6NFQ2, ECO:0000250|UniProtKB:Q9Y4C2}. TISSUE SPECIFICITY: Prostate-specific. Present in both dorso-lateral and anterior prostate. {ECO:0000269|PubMed:16223778, ECO:0000269|PubMed:17003280}. +Q8BQB6 SAXO2_MOUSE Stabilizer of axonemal microtubules 2 394 45,533 Chain (1); Sequence conflict (1) +Q80UF7 TCAM1_MOUSE TIR domain-containing adapter molecule 1 (TICAM-1) (Toll-interleukin-1 receptor domain-containing adapter protein inducing interferon beta) (TIR domain-containing adapter protein inducing IFN-beta) 732 79,230 Chain (1); Compositional bias (2); Domain (1); Erroneous initiation (1); Frameshift (1); Motif (3); Region (2); Sequence caution (1); Sequence conflict (5) FUNCTION: Involved in innate immunity against invading pathogens. Adapter used by TLR3 and TLR4 (through TICAM2) to mediate NF-kappa-B and interferon-regulatory factor (IRF) activation, and to induce apoptosis. Ligand binding to these receptors results in TRIF recruitment through its TIR domain. Distinct protein-interaction motifs allow recruitment of the effector proteins TBK1, TRAF6 and RIPK1, which in turn, lead to the activation of transcription factors IRF3 and IRF7, NF-kappa-B and FADD respectively. Component of a multi-helicase-TICAM1 complex that acts as a cytoplasmic sensor of viral double-stranded RNA (dsRNA) and plays a role in the activation of a cascade of antiviral responses including the induction of proinflammatory cytokines (PubMed:21703541). {ECO:0000269|PubMed:12855817, ECO:0000269|PubMed:16002681, ECO:0000269|PubMed:21703541}. PTM: Phosphorylated by TBK1. {ECO:0000250}.; PTM: Polyubiquitinated by TRIM38 with 'Lys-48'-linked chains, leading to proteasomal degradation. {ECO:0000250|UniProtKB:Q8IUC6}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:21703541}. Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:Q8IUC6}. Mitochondrion {ECO:0000269|PubMed:21703541}. Note=Colocalizes with UBQLN1 in the autophagosome. Colocalizes in the cytosol with DDX1, DDX21 and DHX36 (PubMed:21703541). Colocalizes in the mitochondria with DDX1 and poly(I:C) RNA ligand (PubMed:21703541). The multi-helicase-TICAM1 complex may translocate to the mitochondria upon poly(I:C) RNA ligand stimulation (PubMed:21703541). {ECO:0000250|UniProtKB:Q8IUC6, ECO:0000269|PubMed:21703541}. SUBUNIT: Homodimer (By similarity). Found in a multi-helicase-TICAM1 complex at least composed of DHX36, DDX1, DDX21 and TICAM1; this complex exists in resting cells with or without poly(I:C) RNA ligand stimulation (PubMed:21703541). Interacts (via TIR domain) with DDX21 (via C-terminus) (PubMed:21703541). Interacts (via TIR domain) with DHX36 (via C-terminus) (PubMed:21703541). Interacts with AZI2, IRF3 and IRF7 (By similarity). Interacts with TICAM2 in TLR4 recruitment (By similarity). Interaction with PIAS4 inhibits the TICAM1-induced NF-kappa-B, IRF and IFNB1 activation (By similarity). Interacts with IKBKB and IKBKE (By similarity). Interaction with SARM1 blocks TICAM1-dependent transcription factor activation (By similarity). Interacts with TRAF3. Interacts with TRAFD1. Interacts with UBQLN1 (via UBA domain). Interacts with TBK1, TRAF6 and RIPK1 and these interactions are enhanced in the presence of WDFY1 (By similarity). Interacts (via the TIR domain) with TLR3 in response to poly(I:C) and this interaction is enhanced in the presence of WDFY1 (PubMed:25736436). Interacts with TLR4 in response to poly(I:C) in a WDFY1-dependent manner (PubMed:25736436). Interacts with WDFY1 in response to poly(I:C) (PubMed:25736436). Interacts with TRIM56 (By similarity). {ECO:0000250|UniProtKB:Q8IUC6, ECO:0000269|PubMed:16306936, ECO:0000269|PubMed:18849341, ECO:0000269|PubMed:21703541, ECO:0000269|PubMed:25736436}. DOMAIN: The N-terminal region is essential for activation of the IFNB promoter activity. {ECO:0000250}.; DOMAIN: The N-terminal domain (TRIF-NTD) is globular and consists of two alpha-helical subdomains connected by a 14-residue linker. It shares structural similarity with IFIT family members N-terminal regions. {ECO:0000250|UniProtKB:Q8IUC6}. +P17563 SBP1_MOUSE Methanethiol oxidase (MTO) (EC 1.8.3.4) (56 kDa selenium-binding protein) (SBP56) (SP56) (Selenium-binding protein 1) 472 52,514 Chain (1); Initiator methionine (1); Modified residue (3); Sequence conflict (3) Organosulfur degradation. FUNCTION: Catalyzes the oxidation of methanethiol, an organosulfur compound known to be produced in substantial amounts by gut bacteria (PubMed:29255262). Selenium-binding protein which may be involved in the sensing of reactive xenobiotics in the cytoplasm. May be involved in intra-Golgi protein transport (By similarity). {ECO:0000250|UniProtKB:Q8VIF7, ECO:0000269|PubMed:29255262}. PTM: The N-terminus is blocked. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13228}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q13228}. Membrane {ECO:0000250|UniProtKB:Q8VIF7}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8VIF7}. Note=May associate with Golgi membrane (By similarity). May associate with the membrane of autophagosomes (By similarity). {ECO:0000250|UniProtKB:Q8VIF7}. SUBUNIT: Interacts with USP33. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in liver, kidney and, to a lesser extent, lung. +Q9D3P1 TCHL1_MOUSE Trichohyalin-like protein 1 638 70,707 Chain (1); Domain (1); Sequence conflict (2) +Q9R0P6 SC11A_MOUSE Signal peptidase complex catalytic subunit SEC11A (EC 3.4.21.89) (Endopeptidase SP18) (Microsomal signal peptidase 18 kDa subunit) (SPase 18 kDa subunit) (SEC11 homolog A) (SEC11-like protein 1) (SPC18) (Sid 2895) 179 20,626 Active site (1); Chain (1); Topological domain (2); Transmembrane (1) TRANSMEM 17 36 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 16 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 37 179 Lumenal. {ECO:0000255}. FUNCTION: Component of the microsomal signal peptidase complex which removes signal peptides from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum. {ECO:0000250}. SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. SUBUNIT: Component of the microsomal signal peptidase complex which consists of five members: SEC11A, SEC11C, SPCS1, SPCS2 and SPCS3. {ECO:0000250}. +P56280 TCL1A_MOUSE T-cell leukemia/lymphoma protein 1A (Oncogene TCL-1) (Oncogene TCL1) (Protein p14 TCL1) 116 14,112 Beta strand (11); Chain (1); Turn (1) FUNCTION: Enhances the phosphorylation and activation of AKT1 and AKT2. Enhances cell proliferation, stabilizes mitochondrial membrane potential and promotes cell survival (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10716693}. Nucleus {ECO:0000269|PubMed:10716693}. Microsome {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Note=Microsomal fraction. {ECO:0000250}. SUBUNIT: Homodimer. Interacts with AKT1, AKT2 and AKT3 (via PH domain). Interacts with PNPT1; the interaction has no effect on PNPT1 exonuclease activity (By similarity). {ECO:0000250}. +Q49B93 SC5AC_MOUSE Sodium-coupled monocarboxylate transporter 2 (Electroneutral sodium monocarboxylate cotransporter) (Low-affinity sodium-lactate cotransporter) (Solute carrier family 5 member 12) 619 67,951 Alternative sequence (1); Chain (1); Glycosylation (2); Topological domain (14); Transmembrane (13) TRANSMEM 10 30 Helical. {ECO:0000255}.; TRANSMEM 48 68 Helical. {ECO:0000255}.; TRANSMEM 81 101 Helical. {ECO:0000255}.; TRANSMEM 129 149 Helical. {ECO:0000255}.; TRANSMEM 158 178 Helical. {ECO:0000255}.; TRANSMEM 181 201 Helical. {ECO:0000255}.; TRANSMEM 236 256 Helical. {ECO:0000255}.; TRANSMEM 276 296 Helical. {ECO:0000255}.; TRANSMEM 322 342 Helical. {ECO:0000255}.; TRANSMEM 386 406 Helical. {ECO:0000255}.; TRANSMEM 412 432 Helical. {ECO:0000255}.; TRANSMEM 438 458 Helical. {ECO:0000255}.; TRANSMEM 505 525 Helical. {ECO:0000255}. TOPO_DOM 1 9 Extracellular. {ECO:0000255}.; TOPO_DOM 31 47 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 69 80 Extracellular. {ECO:0000255}.; TOPO_DOM 102 128 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 150 157 Extracellular. {ECO:0000255}.; TOPO_DOM 179 180 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 202 235 Extracellular. {ECO:0000255}.; TOPO_DOM 257 275 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 297 321 Extracellular. {ECO:0000255}.; TOPO_DOM 343 385 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 407 411 Extracellular. {ECO:0000255}.; TOPO_DOM 433 437 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 459 504 Extracellular. {ECO:0000255}.; TOPO_DOM 526 619 Cytoplasmic. {ECO:0000255}. FUNCTION: Acts as an electroneutral and low-affinity sodium (Na(+))-dependent sodium-coupled solute transporter. Catalyzes the transport across the plasma membrane of many monocarboxylates such as lactate, pyruvate, nicotinate, propionate, butyrate and beta-D-hydroxybutyrate. May be responsible for the first step of reabsorption of monocarboxylates from the lumen of the proximal tubule of the kidney and the small intestine. May play also a role in monocarboxylates transport in the retina. Mediates electroneutral uptake of lactate, with a stoichiometry of 2 Na(+) for each lactate. {ECO:0000269|PubMed:16104846, ECO:0000269|PubMed:16873376}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:16873376, ECO:0000269|PubMed:17692818}; Multi-pass membrane protein {ECO:0000269|PubMed:16873376, ECO:0000269|PubMed:17692818}. Note=Detected at the brush border membrane of the kidney. Colocalizes with vimentin in Mueller cells. TISSUE SPECIFICITY: Expressed in the cortical region of the kidney corresponding to the proximal tubule. Expressed in Mueller cells of the inner retina (at protein level). Isoform 1 is expressed in the retina, kidney, small intestine and skeletal muscle. Isoform 2 is not detected in the kidney, small intestine and skeletal muscle. In the kidney, expressed predominantly in tubular epithelial cells of the cortical region and in the convoluted portions of the proximal tubule (pars convoluta). In the small intestine, its expression is highest in the proximal part and gradually decreased towards the distal end. Expressed in the neural retina. Not detected in the caecum and colon. {ECO:0000269|PubMed:16104846, ECO:0000269|PubMed:16873376, ECO:0000269|PubMed:17591909, ECO:0000269|PubMed:17692818}. +Q9JKV5 SCAM4_MOUSE Secretory carrier-associated membrane protein 4 (SC4) (Secretory carrier membrane protein 4) 230 25,342 Chain (1); Modified residue (1); Topological domain (2); Transmembrane (4) TRANSMEM 40 60 Helical. {ECO:0000255}.; TRANSMEM 61 81 Helical. {ECO:0000255}.; TRANSMEM 106 126 Helical. {ECO:0000255}.; TRANSMEM 149 169 Helical. {ECO:0000255}. TOPO_DOM 1 39 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 170 230 Cytoplasmic. {ECO:0000255}. FUNCTION: Probably involved in membrane protein trafficking. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. +Q9EQG3 SCEL_MOUSE Sciellin 652 72,972 Chain (1); Domain (1); Modified residue (3); Region (1); Repeat (15) FUNCTION: May function in the assembly or regulation of proteins in the cornified envelope. The LIM domain may be involved in homotypic or heterotypic associations and may function to localize sciellin to the cornified envelope (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Membrane. Note=May become cross-linked to membrane proteins by transglutaminase. TISSUE SPECIFICITY: Expressed in the upper layers of stratified epithelia, including, ependyma and choroid plexus of the brain ventricles. +Q8BYF6 SC5A8_MOUSE Sodium-coupled monocarboxylate transporter 1 (Electrogenic sodium monocarboxylate cotransporter) (Solute carrier family 5 member 8) 611 66,766 Chain (1); Erroneous initiation (1); Glycosylation (1); Sequence conflict (1); Topological domain (14); Transmembrane (13) TRANSMEM 10 30 Helical. {ECO:0000255}.; TRANSMEM 52 72 Helical. {ECO:0000255}.; TRANSMEM 87 107 Helical. {ECO:0000255}.; TRANSMEM 133 153 Helical. {ECO:0000255}.; TRANSMEM 162 182 Helical. {ECO:0000255}.; TRANSMEM 185 205 Helical. {ECO:0000255}.; TRANSMEM 240 260 Helical. {ECO:0000255}.; TRANSMEM 280 300 Helical. {ECO:0000255}.; TRANSMEM 337 359 Helical. {ECO:0000255}.; TRANSMEM 390 410 Helical. {ECO:0000255}.; TRANSMEM 416 436 Helical. {ECO:0000255}.; TRANSMEM 440 460 Helical. {ECO:0000255}.; TRANSMEM 519 539 Helical. {ECO:0000255}. TOPO_DOM 1 9 Extracellular. {ECO:0000255}.; TOPO_DOM 31 51 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 73 86 Extracellular. {ECO:0000255}.; TOPO_DOM 108 132 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 154 161 Extracellular. {ECO:0000255}.; TOPO_DOM 183 184 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 206 239 Extracellular. {ECO:0000255}.; TOPO_DOM 261 279 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 301 336 Extracellular. {ECO:0000255}.; TOPO_DOM 360 389 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 411 415 Extracellular. {ECO:0000255}.; TOPO_DOM 437 439 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 461 518 Extracellular. {ECO:0000255}.; TOPO_DOM 540 611 Cytoplasmic. {ECO:0000255}. FUNCTION: Acts as an electrogenic sodium (Na(+)) and chloride (Cl-)-dependent sodium-coupled solute transporter, including transport of monocarboxylates (short-chain fatty acids including L-lactate, D-lactate, pyruvate, acetate, propionate, valerate and butyrate), lactate, mocarboxylate drugs (nicotinate, benzoate, salicylate and 5-aminosalicylate) and ketone bodies (beta-D-hydroxybutyrate, acetoacetate and alpha-ketoisocaproate), with a Na(+):substrate stoichiometry of between 4:1 and 2:1. Catalyzes passive carrier mediated diffusion of iodide. Mediates iodide transport from the thyrocyte into the colloid lumen through the apical membrane. May be responsible for the absorption of D-lactate and monocarboxylate drugs from the intestinal tract. May play a critical role in the entry of L-lactate and ketone bodies into neurons by a process driven by an electrochemical Na(+) gradient and hence contribute to the maintenance of the energy status and function of neurons. {ECO:0000269|PubMed:15322102, ECO:0000269|PubMed:15651982, ECO:0000269|PubMed:15867356, ECO:0000269|PubMed:16805814}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:17099289, ECO:0000269|PubMed:17245649}; Multi-pass membrane protein {ECO:0000269|PubMed:17099289, ECO:0000269|PubMed:17245649}. Apical cell membrane; Multi-pass membrane protein {ECO:0000269|PubMed:17099289, ECO:0000269|PubMed:17245649}. Note=Restricted to the apical cell membrane of enterocytes. {ECO:0000269|PubMed:17099289, ECO:0000269|PubMed:17245649}. TISSUE SPECIFICITY: Expressed in brain, colon, kidney and in the ileum and jejunum of small intestine. In the kidney, expression occurred in the proximal tubule and the loop of Henle, being restricted to tubular epithelial cells in both the cortex and the medulla. In the colon, predominantly expressed in the distal half of the large bowel and in the most terminal ileum. Localized selectively in the luminal surface of crypts in the large intestine and to the brush border in the middle parts of crypts in the cecum. In the brain, expression was seen throughout, exclusively in neurons, including the cortex, hippocampus, cerebellum and pituitary gland (at protein level). Expression is reduced in oligodendrogliomas. {ECO:0000269|PubMed:15322102, ECO:0000269|PubMed:15867356, ECO:0000269|PubMed:16805814, ECO:0000269|PubMed:17099289, ECO:0000269|PubMed:17245649}. +A2ASZ8 SCMC2_MOUSE Calcium-binding mitochondrial carrier protein SCaMC-2 (Small calcium-binding mitochondrial carrier protein 2) (Solute carrier family 25 member 25) 469 52,621 Alternative sequence (3); Calcium binding (1); Chain (1); Domain (3); Erroneous gene model prediction (2); Erroneous initiation (3); Repeat (3); Topological domain (7); Transmembrane (6) TRANSMEM 190 207 Helical; Name=1. {ECO:0000255}.; TRANSMEM 245 264 Helical; Name=2. {ECO:0000255}.; TRANSMEM 288 301 Helical; Name=3. {ECO:0000255}.; TRANSMEM 338 357 Helical; Name=4. {ECO:0000255}.; TRANSMEM 381 398 Helical; Name=5. {ECO:0000255}.; TRANSMEM 438 457 Helical; Name=6. {ECO:0000255}. TOPO_DOM 1 189 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 208 244 Mitochondrial matrix. {ECO:0000255}.; TOPO_DOM 265 287 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 302 337 Mitochondrial matrix. {ECO:0000255}.; TOPO_DOM 358 380 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 399 437 Mitochondrial matrix. {ECO:0000255}.; TOPO_DOM 458 469 Mitochondrial intermembrane. {ECO:0000255}. FUNCTION: Calcium-dependent mitochondrial solute carrier. Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane. May act as a ATP-Mg/Pi exchanger that mediates the transport of Mg-ATP in exchange for phosphate, catalyzing the net uptake or efflux of adenine nucleotides into or from the mitochondria (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q9DAH1 SCP2D_MOUSE SCP2 sterol-binding domain-containing protein 1 156 17,371 Chain (1); Domain (1); Erroneous initiation (1); Sequence conflict (1) +Q9WU39 SCNNG_MOUSE Amiloride-sensitive sodium channel subunit gamma (Epithelial Na(+) channel subunit gamma) (Gamma-ENaC) (Gamma-NaCH) (Nonvoltage-gated sodium channel 1 subunit gamma) (SCNEG) 655 74,635 Chain (1); Glycosylation (3); Topological domain (3); Transmembrane (2) TRANSMEM 56 76 Helical; Name=1. {ECO:0000255}.; TRANSMEM 548 568 Helical; Name=2. {ECO:0000255}. TOPO_DOM 1 55 Cytoplasmic. {ECO:0000250|UniProtKB:P37089}.; TOPO_DOM 77 547 Extracellular. {ECO:0000250|UniProtKB:P37089}.; TOPO_DOM 569 655 Cytoplasmic. {ECO:0000250|UniProtKB:P37089}. FUNCTION: Sodium permeable non-voltage-sensitive ion channel inhibited by the diuretic amiloride. Mediates the electrodiffusion of the luminal sodium (and water, which follows osmotically) through the apical membrane of epithelial cells. Plays an essential role in electrolyte and blood pressure homeostasis, but also in airway surface liquid homeostasis, which is important for proper clearance of mucus. Controls the reabsorption of sodium in kidney, colon, lung and sweat glands. Also plays a role in taste perception. {ECO:0000250|UniProtKB:P51170, ECO:0000269|PubMed:10409305}. PTM: ENaC cleavage by furin, and subsequently by prostasin (PRSS8), leads to a stepwise increase in the open probability of the channel as a result of release of the alpha and gamma subunit inhibitory tracts, respectively. Interaction of ENaC subunit SCNN1B with BPIFA1 protects ENaC against proteolytic activation. {ECO:0000250|UniProtKB:P51170}.; PTM: Phosphorylated on serine and threonine residues. Aldosterone and insulin increase the basal level of phosphorylation. {ECO:0000250|UniProtKB:P37091}.; PTM: Ubiquitinated; this targets individual subunits for endocytosis and proteasome-mediated degradation. {ECO:0000250|UniProtKB:P37091}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000303|PubMed:10409305}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P37089}. Note=Apical membrane of epithelial cells. {ECO:0000303|PubMed:10409305}. SUBUNIT: Heterotrimer containing an alpha/SCNN1A, a beta/SCNN1B and a gamma/SCNN1G subunit. An additional delta/SCNN1D subunit exists only in some organisms and can replace the alpha/SCNN1A subunit to form an alternative channel with specific properties (Probable). Interacts with NEDD4; via the WW domains (PubMed:11244092, PubMed:15123669). Interacts with NEDD4L; via the WW domains (PubMed:12424229, PubMed:11244092, PubMed:15123669). Interacts with WWP1; via the WW domains (By similarity). Interacts with WWP2; via the WW domains. Interacts with the full-length immature form of PCSK9 (pro-PCSK9) (By similarity). {ECO:0000250|UniProtKB:P51170, ECO:0000269|PubMed:11244092, ECO:0000269|PubMed:12424229, ECO:0000269|PubMed:15123669, ECO:0000305|PubMed:10409305}. TISSUE SPECIFICITY: Lung and kidney. {ECO:0000269|PubMed:10409305}. +Q6QIY3 SCNAA_MOUSE Sodium channel protein type 10 subunit alpha (Peripheral nerve sodium channel 3) (PN3) (Sensory neuron sodium channel) (Sodium channel protein type X subunit alpha) (Voltage-gated sodium channel subunit alpha Nav1.8) 1958 220,552 Alternative sequence (2); Chain (1); Disulfide bond (2); Domain (1); Glycosylation (9); Intramembrane (4); Modified residue (7); Mutagenesis (2); Repeat (4); Topological domain (29); Transmembrane (24) INTRAMEM 341 365 Pore-forming. {ECO:0000250|UniProtKB:D0E0C2}.; INTRAMEM 834 854 Pore-forming. {ECO:0000250|UniProtKB:D0E0C2}.; INTRAMEM 1355 1376 Pore-forming. {ECO:0000250|UniProtKB:D0E0C2}.; INTRAMEM 1648 1670 Pore-forming. {ECO:0000250|UniProtKB:D0E0C2}. TRANSMEM 126 149 Helical; Name=S1 of repeat I. {ECO:0000255}.; TRANSMEM 155 174 Helical; Name=S2 of repeat I. {ECO:0000255}.; TRANSMEM 188 206 Helical; Name=S3 of repeat I. {ECO:0000255}.; TRANSMEM 213 232 Helical; Voltage-sensor; Name=S4 of repeat I. {ECO:0000255}.; TRANSMEM 249 272 Helical; Name=S5 of repeat I. {ECO:0000255}.; TRANSMEM 373 398 Helical; Name=S6 of repeat I. {ECO:0000255}.; TRANSMEM 659 683 Helical; Name=S1 of repeat II. {ECO:0000255}.; TRANSMEM 695 718 Helical; Name=S2 of repeat II. {ECO:0000255}.; TRANSMEM 727 746 Helical; Name=S3 of repeat II. {ECO:0000255}.; TRANSMEM 753 772 Helical; Voltage-sensor; Name=S4 of repeat II. {ECO:0000255}.; TRANSMEM 789 809 Helical; Name=S5 of repeat II. {ECO:0000255}.; TRANSMEM 864 889 Helical; Name=S6 of repeat II. {ECO:0000255}.; TRANSMEM 1149 1172 Helical; Name=S1 of repeat III. {ECO:0000255}.; TRANSMEM 1186 1211 Helical; Name=S2 of repeat III. {ECO:0000255}.; TRANSMEM 1218 1239 Helical; Name=S3 of repeat III. {ECO:0000255}.; TRANSMEM 1244 1265 Helical; Voltage-sensor; Name=S4 of repeat III. {ECO:0000255}.; TRANSMEM 1285 1312 Helical; Name=S5 of repeat III. {ECO:0000255}.; TRANSMEM 1393 1419 Helical; Name=S6 of repeat III. {ECO:0000255}.; TRANSMEM 1473 1496 Helical; Name=S1 of repeat IV. {ECO:0000255}.; TRANSMEM 1508 1531 Helical; Name=S2 of repeat IV. {ECO:0000255}.; TRANSMEM 1538 1561 Helical; Name=S3 of repeat IV. {ECO:0000255}.; TRANSMEM 1574 1595 Helical; Voltage-sensor; Name=S4 of repeat IV. {ECO:0000255}.; TRANSMEM 1611 1633 Helical; Name=S5 of repeat IV. {ECO:0000255}.; TRANSMEM 1699 1723 Helical; Name=S6 of repeat IV. {ECO:0000255}. TOPO_DOM 1 125 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 150 154 Extracellular. {ECO:0000305}.; TOPO_DOM 175 187 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 207 212 Extracellular. {ECO:0000305}.; TOPO_DOM 233 248 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 273 340 Extracellular. {ECO:0000305}.; TOPO_DOM 366 372 Extracellular. {ECO:0000305}.; TOPO_DOM 399 658 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 684 694 Extracellular. {ECO:0000305}.; TOPO_DOM 719 726 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 747 752 Extracellular. {ECO:0000305}.; TOPO_DOM 773 788 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 810 833 Extracellular. {ECO:0000305}.; TOPO_DOM 855 863 Extracellular. {ECO:0000305}.; TOPO_DOM 890 1148 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1173 1185 Extracellular. {ECO:0000305}.; TOPO_DOM 1212 1217 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1240 1243 Extracellular. {ECO:0000305}.; TOPO_DOM 1266 1284 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1313 1354 Extracellular. {ECO:0000305}.; TOPO_DOM 1377 1392 Extracellular. {ECO:0000305}.; TOPO_DOM 1420 1472 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1497 1507 Extracellular. {ECO:0000305}.; TOPO_DOM 1532 1537 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1562 1573 Extracellular. {ECO:0000305}.; TOPO_DOM 1596 1610 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1634 1647 Extracellular. {ECO:0000305}.; TOPO_DOM 1671 1698 Extracellular. {ECO:0000305}.; TOPO_DOM 1724 1958 Cytoplasmic. {ECO:0000305}. FUNCTION: Tetrodotoxin-resistant channel that mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which sodium ions may pass in accordance with their electrochemical gradient. Plays a role in neuropathic pain mechanisms. {ECO:0000269|PubMed:24159039}. PTM: Ubiquitinated by NEDD4L; which promotes its endocytosis. {ECO:0000305}.; PTM: Phosphorylation at Ser-1452 by PKC in a highly conserved cytoplasmic loop slows inactivation of the sodium channel and reduces peak sodium currents. {ECO:0000250}.; PTM: Lacks the cysteine which covalently binds the conotoxin GVIIJ. This cysteine (position 815) is speculated in other sodium channel subunits alpha to be implied in covalent binding with the sodium channel subunit beta-2 or beta-4. {ECO:0000250|UniProtKB:P15389}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:D0E0C2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:D0E0C2}. Note=It can be translocated to the cell membrane through association with S100A10. {ECO:0000250}. SUBUNIT: The channel consists of an ion conducting pore forming alpha-subunit regulated by one or more associated auxiliary subunits SCN1B, SCN2B and SCN3B; electrophysiological properties may vary depending on the type of the associated beta subunits. Found in a number of complexes with PRX, DYNLT1 and PDZD2. Interacts with proteins such as FSTL1, PRX, DYNLT1, PDZD2, S100A10 and many others (By similarity). Interacts with NEDD4 and NEDD4L. {ECO:0000250, ECO:0000269|PubMed:15123669}. DOMAIN: The sequence contains 4 internal repeats, each with 5 hydrophobic segments (S1, S2, S3, S5, S6) and one positively charged segment (S4). Segments S4 are probably the voltage-sensors and are characterized by a series of positively charged amino acids at every third position. {ECO:0000305}. TISSUE SPECIFICITY: Expressed in dorsal root ganglion and trigeminal ganglion. +Q9JJS0 SCUB2_MOUSE Signal peptide, CUB and EGF-like domain-containing protein 2 (Protein CEGP1) (Scube/You) 997 109,924 Chain (1); Disulfide bond (19); Domain (10); Glycosylation (1); Mutagenesis (1); Region (1); Signal peptide (1) FUNCTION: Lipid-binding protein required for SHH long-range signaling by binding to the dually lipid-modified SHH (ShhNp) and by promoting ShhNp mobilization, solubilization and release from the cell membrane (PubMed:22902404, PubMed:22677548). Acts by enhancing the proteolytic processing (shedding) of the lipid-modified N- and C- terminal of ShhNp at the cell surface (PubMed:24522195). Synergizes with DISP1 to cause a increase in SHH secretion (PubMed:22902404). Probable cell surface coreceptor for VEGFR2 involved in VEGFR2-mediated angiogenesis (PubMed:27834687). {ECO:0000269|PubMed:22677548, ECO:0000269|PubMed:22902404, ECO:0000269|PubMed:24522195, ECO:0000269|PubMed:27834687}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9NQ36}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9NQ36}. Cell surface {ECO:0000250|UniProtKB:Q9NQ36}. Note=Secreted and tethered at the cell surface. {ECO:0000250|UniProtKB:Q9NQ36}. SUBUNIT: Interacts with SHH via the cholesterol anchor of the dually lipid-modified SHH (ShhNp) (PubMed:22902404). Interacts with PTCH1 (PubMed:22902404). Forms homooligomers and heterooligomers with SCUBE1 and SCUBE3 (By similarity). Interacts with VEGFR2 (PubMed:27834687). {ECO:0000250|UniProtKB:Q8IX30, ECO:0000269|PubMed:22902404, ECO:0000269|PubMed:27834687}. DOMAIN: The CUB domain is important for the interaction with the cholesterol-anchor of SHH. The CUB domain regulates protease recruitment and activation during SHH shedding. {ECO:0000269|PubMed:24522195}. TISSUE SPECIFICITY: Expressed in adult heart, lung and testis. {ECO:0000269|PubMed:11287194}. +Q8CG47 SMC4_MOUSE Structural maintenance of chromosomes protein 4 (SMC protein 4) (SMC-4) (Chromosome-associated polypeptide C) (XCAP-C homolog) 1286 146,895 Beta strand (7); Chain (1); Coiled coil (3); Compositional bias (2); Domain (1); Helix (12); Modified residue (7); Nucleotide binding (1); Sequence conflict (1) FUNCTION: Central component of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Chromosome {ECO:0000250}. Note=In interphase cells, the majority of the condensin complex is found in the cytoplasm, while a minority of the complex is associated with chromatin. A subpopulation of the complex however remains associated with chromosome foci in interphase cells. During mitosis, most of the condensin complex is associated with the chromatin. At the onset of prophase, the regulatory subunits of the complex are phosphorylated by CDC2, leading to condensin's association with chromosome arms and to chromosome condensation. Dissociation from chromosomes is observed in late telophase (By similarity). {ECO:0000250}. SUBUNIT: Forms a heterodimer with SMC2. Component of the condensin complex, which contains the SMC2 and SMC4 heterodimer, and three non SMC subunits that probably regulate the complex: BRRN1/CAPH, CNAP1/CAPD2 and CAPG (By similarity). {ECO:0000250}. DOMAIN: The SMC hinge domain, which separates the large intramolecular coiled coil regions, allows the heterodimerization with SMC2, forming a V-shaped heterodimer. {ECO:0000250}. +Q8CG46 SMC5_MOUSE Structural maintenance of chromosomes protein 5 (SMC protein 5) (SMC-5) (mSMC5) (Protein expressed in male leptotene and zygotene spermatocytes 453) (MLZ-453) 1101 128,813 Alternative sequence (2); Chain (1); Coiled coil (4); Compositional bias (1); Erroneous initiation (1); Modified residue (2); Nucleotide binding (1); Region (1); Sequence conflict (3) FUNCTION: Core component of the SMC5-SMC6 complex, a complex involved in repair of DNA double-strand breaks by homologous recombination. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The complex is required for telomere maintenance via recombination and mediates sumoylation of shelterin complex (telosome) components. Required for sister chromatid cohesion during prometaphase and mitotic progression; the function seems to be independent of SMC6 (By similarity). {ECO:0000250}. PTM: Sumoylated. {ECO:0000250}.; PTM: Ubiquitinated. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11408570, ECO:0000269|PubMed:20339383}. Chromosome {ECO:0000269|PubMed:11408570}. Nucleus, PML body {ECO:0000250|UniProtKB:Q8IY18}. Chromosome, telomere {ECO:0000250|UniProtKB:Q8IY18}. Note=Colocalizes with SMC6 on the X-Y chromosome pair within the sex vesicle during late pachytene/diplotene (PubMed:11408570). Associates with chromatin. Localizes to PML nuclear bodies in ALT cell lines. Accumulates with RAD18 and the SLF1-SLF2 complex at replication-coupled DNA interstrand repair and DNA double-strand breaks (DSBs) sites on chromatin in a ubiquitin-dependent manner. {ECO:0000250|UniProtKB:Q8IY18, ECO:0000269|PubMed:11408570}. SUBUNIT: Forms a heterodimer with SMC6. Component of the SMC5-SMC6 complex which consists at least of SMC5, SMC6, NSMCE2, NSMCE1, NSMCE4A or EID3 and NSMCE3. Interacts with NSMCE2. Interacts with SLF2; this interaction induces an association of the SLF1-SLF2 complex with the SMC5-SMC6 complex. Interacts with RAD18; this interaction is increased in a SLF1 or SLF2-dependent manner. {ECO:0000250|UniProtKB:Q8IY18}. DOMAIN: The flexible hinge domain, which separates the large intramolecular coiled coil regions, allows the heterotypic interaction with the corresponding domain of SMC6, forming a V-shaped heterodimer. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in testis but not ovary. {ECO:0000269|PubMed:20339383}. +P60867 RS20_MOUSE 40S ribosomal protein S20 119 13,373 Chain (1); Cross-link (2); Initiator methionine (1); Modified residue (6) PTM: Monoubiquitinated by ZNF598 when a ribosome has stalled during translation of poly(A) sequences, leading to preclude synthesis of a long poly-lysine tail and initiate the ribosome quality control (RQC) pathway to degrade the potentially detrimental aberrant nascent polypeptide. {ECO:0000250|UniProtKB:P60866}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Component of the 40S small ribosomal subunit. {ECO:0000250}. +P62852 RS25_MOUSE 40S ribosomal protein S25 125 13,742 Chain (1); Modified residue (7) +Q5D525 SYC1L_MOUSE Synaptonemal complex central element protein 1-like (Meiosis-related protein) 247 28,461 Alternative sequence (2); Chain (1); Coiled coil (1); Erroneous initiation (1); Sequence conflict (6) FUNCTION: May be involved in meiosis. Isoform 1 may be involved in meiosis during spermatogenesis while isoform 2 is probably related to a later stage of meiosis, in the development stage of secondary spermatocytes and spermatids. {ECO:0000269|PubMed:16328886}. TISSUE SPECIFICITY: Isoform 1 is abundantly expressed in testis and weakly in ovary, it is not found in other tissues. Isoform 2 is expressed in testis and poorly in brain, heart, lung and other examined tissues. {ECO:0000269|PubMed:16328886}. +A0A0M3U1B0 SYC2L_MOUSE Synaptonemal complex protein 2-like (SCP-2-like) 842 96,055 Chain (1) FUNCTION: Oocyte-specific protein that localizes to centromeres at the dictyate stage and regulates the survival of primordial oocytes. {ECO:0000269|PubMed:26362258}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26362258}. Chromosome, centromere {ECO:0000269|PubMed:26362258}. Note=Localized to the synaptonemal complex lateral elements in late diplotene oocytes, while it is absent on the synaptonemal complex of leptotene, zygotene, pachytene and early diplotene oocytes (PubMed:26362258). Localizes to centromeres in dictyate oocytes (PubMed:26362258). Detected in nuclear granules and sizable aggregates (By similarity). {ECO:0000250|UniProtKB:Q5T4T6, ECO:0000269|PubMed:26362258}. TISSUE SPECIFICITY: Specifically expressed in oocytes. {ECO:0000269|PubMed:26362258}. +Q9ER72 SYCC_MOUSE Cysteine--tRNA ligase, cytoplasmic (EC 6.1.1.16) (Cysteinyl-tRNA synthetase) (CysRS) 831 94,860 Alternative sequence (1); Binding site (1); Chain (1); Initiator methionine (1); Metal binding (4); Modified residue (5); Motif (2); Sequence conflict (6) SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Monomer. {ECO:0000250}. +Q505B8 SYCE2_MOUSE Synaptonemal complex central element protein 2 171 19,558 Alternative sequence (1); Chain (1); Coiled coil (2); Sequence conflict (1) FUNCTION: Major component of the transverse central element of synaptonemal complexes (SCS), formed between homologous chromosomes during meiotic prophase. Requires SYCP1 in order to be incorporated into the central element. May have a role in the synaptonemal complex assembly, stabilization and recombination. {ECO:0000269|PubMed:15944401}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15944401}. Chromosome {ECO:0000269|PubMed:15944401}. Note=Associates with chromatin. In prophase I stage of meiosis, localizes in the transverse central elements of the central region between lateral elements of the synaptonemal complexes. Found only where the chromosome cores are synapsed. Colocalizes with SYCE1 in the central elements. SUBUNIT: Homodimer. Found in a complex with SYCP1 and SYCE1. Interacts with SYCP1, SYCE1 and SYCE3. {ECO:0000269|PubMed:15944401, ECO:0000269|PubMed:21637789}. TISSUE SPECIFICITY: Meiotic cells (at protein level). Expressed in the ovary and testis. {ECO:0000269|PubMed:15944401}. +Q9CQE3 RT17_MOUSE 28S ribosomal protein S17, mitochondrial (MRP-S17) (S17mt) 120 13,382 Chain (1); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P82916}. SUBUNIT: Component of the mitochondrial ribosome small subunit (28S) which comprises a 12S rRNA and about 30 distinct proteins. {ECO:0000250|UniProtKB:P82916}. +Q99N84 RT18B_MOUSE 28S ribosomal protein S18b, mitochondrial (MRP-S18-b) (Mrps18-b) (S18mt-b) (28S ribosomal protein S18-2, mitochondrial) (MRP-S18-2) 254 28,703 Alternative sequence (1); Chain (1); Frameshift (1); Modified residue (1); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9Y676}. SUBUNIT: Component of the mitochondrial ribosome small subunit (28S) which comprises a 12S rRNA and about 30 distinct proteins. {ECO:0000250|UniProtKB:Q9Y676}. +Q9CR88 RT14_MOUSE 28S ribosomal protein S14, mitochondrial (MRP-S14) (S14mt) 128 14,920 Chain (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:O60783}. SUBUNIT: Component of the mitochondrial ribosome small subunit (28S) which comprises a 12S rRNA and about 30 distinct proteins (By similarity). Interacts with LIAT1. {ECO:0000250|UniProtKB:O60783, ECO:0000269|PubMed:25369936}. +Q9D2R8 RT33_MOUSE 28S ribosomal protein S33, mitochondrial (MRP-S33) (S33mt) (Ganglioside-induced differentiation-associated-protein 3) 106 12,459 Chain (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (1); Sequence conflict (2) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9Y291}. SUBUNIT: Component of the mitochondrial ribosome small subunit (28S) which comprises a 12S rRNA and about 30 distinct proteins. {ECO:0000250|UniProtKB:P82926}. +Q80ZS3 RT26_MOUSE 28S ribosomal protein S26, mitochondrial (MRP-S26) (S26mt) 200 23,444 Chain (1); Modified residue (1); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q3SZ86}. SUBUNIT: Component of the mitochondrial ribosome small subunit (28S) which comprises a 12S rRNA and about 30 distinct proteins. {ECO:0000250|UniProtKB:Q3SZ86}. +Q0VGM9 RTEL1_MOUSE Regulator of telomere elongation helicase 1 (EC 3.6.4.12) 1203 133,767 Alternative sequence (6); Chain (1); Domain (1); Erroneous gene model prediction (1); Erroneous initiation (1); Metal binding (4); Motif (4); Mutagenesis (5); Nucleotide binding (1); Sequence conflict (16) FUNCTION: ATP-dependent DNA helicase implicated in telomere-length regulation, DNA repair and the maintenance of genomic stability. Acts as an anti-recombinase to counteract toxic recombination and limit crossover during meiosis. Regulates meiotic recombination and crossover homeostasis by physically dissociating strand invasion events and thereby promotes noncrossover repair by meiotic synthesis dependent strand annealing (SDSA) as well as disassembly of D loop recombination intermediates. Also disassembles T loops and prevents telomere fragility by counteracting telomeric G4-DNA structures, which together ensure the dynamics and stability of the telomere. {ECO:0000255|HAMAP-Rule:MF_03065, ECO:0000269|PubMed:15210109, ECO:0000269|PubMed:22579284, ECO:0000269|PubMed:22593209, ECO:0000269|PubMed:24115439}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03065, ECO:0000269|PubMed:15210109, ECO:0000269|PubMed:24115439}. Note=Colocalizes with PCNA within the replication foci in S-phase cells. SUBUNIT: Interacts with TERF1. Interacts (via PIP-box) with PCNA; the interaction is direct and essential for suppressing telomere fragility. Interacts with MMS19; the interaction mediates the association of RTEL1 with the cytosolic iron-sulfur protein assembly (CIA) complex. {ECO:0000255|HAMAP-Rule:MF_03065, ECO:0000269|PubMed:24115439}. DOMAIN: The PIP-box (PCNA interacting peptide) motif mediates the interaction with PCNA and localization to replication foci. {ECO:0000255|HAMAP-Rule:MF_03065, ECO:0000269|PubMed:24115439}. TISSUE SPECIFICITY: Widely expressed. Expressed in spleen, thymus, Peyer patches, kidney, and intestine. Not expressed in brain, heart, lung, skeletal muscles, skin and white fat. In the adult gonad, it is highly expressed in the testis, mainly in the spermatogonia and meiotic spermatocytes. {ECO:0000269|PubMed:15210109}. +Q8VCZ8 RUSD1_MOUSE RNA pseudouridylate synthase domain-containing protein 1 (Ribosomal large subunit pseudouridine synthase C-like protein) 306 34,231 Active site (1); Chain (1); Compositional bias (1); Modified residue (1) +Q3U0X8 TACT_MOUSE T-cell surface protein tactile (Cell surface antigen CD96) (T cell-activated increased late expression protein) (CD antigen CD96) 602 67,133 Chain (1); Compositional bias (1); Disulfide bond (3); Domain (3); Glycosylation (16); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 537 557 Helical. {ECO:0000255}. TOPO_DOM 22 536 Extracellular. {ECO:0000255}.; TOPO_DOM 558 602 Cytoplasmic. {ECO:0000255}. FUNCTION: May be involved in adhesive interactions of activated T and NK cells during the late phase of the immune response. Promotes NK cell-target adhesion by interacting with PVR present on target cells. May function at a time after T and NK cells have penetrated the endothelium using integrins and selectins, when they are actively engaging diseased cells and moving within areas of inflammation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Homodimer; disulfide-linked. Interacts with PVR (By similarity). {ECO:0000250}. +Q3TAA7 S11IP_MOUSE Serine/threonine-protein kinase 11-interacting protein (LKB1-interacting protein 1) 1072 118,005 Chain (1); Compositional bias (1); Modified residue (6); Repeat (8); Sequence conflict (2) FUNCTION: May regulate STK11/LKB1 function by controlling its subcellular localization. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Some cells show granular or punctuate expression. Colocalizes with STK11/LKB1 and SMAD4 in granular or punctuate structures (By similarity). {ECO:0000250}. SUBUNIT: Found in a ternary complex composed of STK11/LKB1, STK11IP and SMAD4 (By similarity). Interacts with SMAD4 (By similarity). Interacts with STK11/LKB1. {ECO:0000250, ECO:0000269|PubMed:11741830}. +Q91ZZ5 RXFP2_MOUSE Relaxin receptor 2 (G-protein coupled receptor 106) (G-protein coupled receptor affecting testicular descent) (Leucine-rich repeat-containing G-protein coupled receptor 8) (Relaxin family peptide receptor 2) 737 82,934 Chain (1); Disulfide bond (4); Domain (1); Glycosylation (6); Repeat (10); Sequence conflict (1); Topological domain (8); Transmembrane (7) TRANSMEM 400 420 Helical; Name=1. {ECO:0000255}.; TRANSMEM 439 459 Helical; Name=2. {ECO:0000255}.; TRANSMEM 479 501 Helical; Name=3. {ECO:0000255}.; TRANSMEM 521 541 Helical; Name=4. {ECO:0000255}.; TRANSMEM 576 596 Helical; Name=5. {ECO:0000255}.; TRANSMEM 623 643 Helical; Name=6. {ECO:0000255}.; TRANSMEM 654 674 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 399 Extracellular. {ECO:0000255}.; TOPO_DOM 421 438 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 460 478 Extracellular. {ECO:0000255}.; TOPO_DOM 502 520 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 542 575 Extracellular. {ECO:0000255}.; TOPO_DOM 597 622 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 644 653 Extracellular. {ECO:0000255}.; TOPO_DOM 675 737 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for relaxin. The activity of this receptor is mediated by G proteins leading to stimulation of adenylate cyclase and an increase of cAMP. May also be a receptor for Leydig insulin-like peptide (INSL3) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed in embryonic and adult gonads of males and females, as well in male gubernarculum. Expressed also in brain. Not detected in kidney, spleen and heart. DISEASE: Note=Defects in Rxfp2 seems to be a cause of impaired testicular descent (known as cryptorchidism). {ECO:0000305|PubMed:11353515}. +Q8VCK7 SYCN_MOUSE Syncollin 134 14,595 Chain (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Functions in exocytosis in pancreatic acinar cells regulating the fusion of zymogen granules with each other. May have a pore-forming activity on membranes and regulate exocytosis in other exocrine tissues. {ECO:0000269|PubMed:11839820, ECO:0000269|PubMed:15040787, ECO:0000269|PubMed:15462671}. PTM: Contains intrachain disulfide bonds. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Lumenal side {ECO:0000250}. Note=Localizes to zymogen granules. Associated with lipid rafts in a cholesterol-dependent manner. {ECO:0000250}. SUBUNIT: Monomer and homooligomer; most probably hexameric. Interacts with GP2 (By similarity). {ECO:0000250}. +P62858 RS28_MOUSE 40S ribosomal protein S28 69 7,841 Chain (1); Modified residue (2) SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P62857}. Cytoplasm {ECO:0000250|UniProtKB:P62857}. Rough endoplasmic reticulum {ECO:0000250|UniProtKB:Q6QAT1}. Note=Detected on cytosolic polysomes (By similarity). Detected in ribosomes that are associated with the rough endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:P62857, ECO:0000250|UniProtKB:Q6QAT1}. SUBUNIT: Component of the 40S small ribosomal subunit. {ECO:0000250|UniProtKB:Q6QAT1}. +Q922B2 SYDC_MOUSE Aspartate--tRNA ligase, cytoplasmic (EC 6.1.1.12) (Aspartyl-tRNA synthetase) (AspRS) 501 57,147 Binding site (5); Chain (1); Modified residue (4); Nucleotide binding (3); Region (1); Sequence conflict (1) FUNCTION: Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA. {ECO:0000250|UniProtKB:P15178}. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Homodimer (By similarity). Part of a multisubunit complex that groups tRNA ligases for Arg (RARS), Asp (DARS), Gln (QARS), Ile (IARS), Leu (LARS), Lys (KARS), Met (MARS) the bifunctional ligase for Glu and Pro (EPRS) and the auxiliary subunits AIMP1/p43, AIMP2/p38 and EEF1E1/p18 (PubMed:12060739). {ECO:0000250|UniProtKB:P14868, ECO:0000269|PubMed:12060739}. +Q9DBZ9 SYDE1_MOUSE Rho GTPase-activating protein SYDE1 (Synapse defective protein 1 homolog 1) (Protein syd-1 homolog 1) 737 80,496 Chain (1); Compositional bias (1); Domain (1); Modified residue (7) FUNCTION: GTPase activator for the Rho-type GTPases. As a GCM1 downstream effector, it is involved in placental development and positively regulates trophoblast cells migration. It regulates cytoskeletal remodeling by controlling the activity of Rho GTPases including RHOA, CDC42 and RAC1. {ECO:0000250|UniProtKB:Q6ZW31}. +Q8BIP0 SYDM_MOUSE Aspartate--tRNA ligase, mitochondrial (EC 6.1.1.12) (Aspartyl-tRNA synthetase) (AspRS) 653 74,102 Binding site (3); Chain (1); Modified residue (2); Nucleotide binding (2); Region (1); Sequence conflict (3); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:Q6PI48}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q6PI48}. +Q3UC65 RSRP1_MOUSE Arginine/serine-rich protein 1 298 34,539 Alternative sequence (3); Chain (1); Compositional bias (1); Modified residue (3); Sequence conflict (1) +Q924T2 RT02_MOUSE 28S ribosomal protein S2, mitochondrial (MRP-S2) (S2mt) 291 32,313 Chain (1) FUNCTION: Required for mitoribosome formation and stability, and mitochondrial translation. {ECO:0000250|UniProtKB:Q9Y399}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9Y399}. SUBUNIT: Component of the mitochondrial ribosome small subunit (28S) which comprises a 12S rRNA and about 30 distinct proteins. {ECO:0000250|UniProtKB:Q9Y399}. +Q9DC71 RT15_MOUSE 28S ribosomal protein S15, mitochondrial (MRP-S15) (S15mt) 258 29,464 Chain (1); Sequence conflict (6); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P82913}. SUBUNIT: Component of the mitochondrial ribosome small subunit (28S) which comprises a 12S rRNA and about 30 distinct proteins. {ECO:0000250|UniProtKB:P82913}. +Q8BJZ4 RT35_MOUSE 28S ribosomal protein S35, mitochondrial (MRP-S35) (S35mt) 320 35,975 Chain (1); Erroneous initiation (1); Sequence conflict (8); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q2YDF6}. SUBUNIT: Component of the mitochondrial ribosome small subunit (28S) which comprises a 12S rRNA and about 30 distinct proteins. {ECO:0000250|UniProtKB:Q2YDF6}. +O35680 RT12_MOUSE 28S ribosomal protein S12, mitochondrial (MRP-S12) (S12mt) (MT-RPS12) 139 15,437 Chain (1); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:O15235}. SUBUNIT: Component of the mitochondrial ribosome small subunit (28S) which comprises a 12S rRNA and about 30 distinct proteins. {ECO:0000250|UniProtKB:O15235}. +Q9CQV5 RT24_MOUSE 28S ribosomal protein S24, mitochondrial (MRP-S24) (S24mt) 167 18,901 Chain (1); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q2M2T7}. SUBUNIT: Component of the mitochondrial ribosome small subunit (28S) which comprises a 12S rRNA and about 30 distinct proteins. {ECO:0000250|UniProtKB:Q2M2T7}. +Q0VDN7 RUND1_MOUSE RUN domain-containing protein 1 615 67,865 Chain (1); Coiled coil (2); Domain (1); Modified residue (2); Sequence conflict (5) FUNCTION: May play a role as p53/TP53 inhibitor and thus may have oncogenic activity. {ECO:0000250}. +Q5QGU6 RTP3_MOUSE Receptor-transporting protein 3 (Transmembrane protein 7) 474 52,220 Chain (1); Sequence conflict (13); Topological domain (1); Transmembrane (1) TRANSMEM 454 474 Helical. {ECO:0000255}. TOPO_DOM 1 453 Cytoplasmic. {ECO:0000255}. FUNCTION: Promotes functional cell surface expression of the bitter taste receptors TAS2R16 and TAS2R43. {ECO:0000250|UniProtKB:Q9BQQ7}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type III membrane protein {ECO:0000305}. SUBUNIT: Interacts with TAS2R16. {ECO:0000250|UniProtKB:Q9BQQ7}. TISSUE SPECIFICITY: Expressed predominantly in the liver. Not detected in the olfactory epithelium. {ECO:0000269|PubMed:12461651, ECO:0000269|PubMed:15550249}. +Q62376 RU17_MOUSE U1 small nuclear ribonucleoprotein 70 kDa (U1 snRNP 70 kDa) (U1-70K) (snRNP70) 448 51,992 Alternative sequence (2); Chain (1); Compositional bias (4); Cross-link (1); Domain (1); Initiator methionine (1); Modified residue (8); Region (1); Sequence conflict (2) FUNCTION: Component of the spliceosomal U1 snRNP, which is essential for recognition of the pre-mRNA 5' splice-site and the subsequent assembly of the spliceosome. SNRNP70 binds to the loop I region of U1-snRNA. {ECO:0000250|UniProtKB:P08621}.; FUNCTION: Isoform 2: Truncated isoforms that lack the RRM domain cannot bind U1-snRNA. {ECO:0000250|UniProtKB:P08621}. PTM: Extensively phosphorylated on serine residues in the C-terminal region. {ECO:0000250|UniProtKB:P08621}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:17656373}. Nucleus, nucleoplasm {ECO:0000269|PubMed:17656373}. Note=Colocalizes with SCNM1 and LUC7L2 in nuclear speckles. {ECO:0000269|PubMed:17656373}. SUBUNIT: Component of the U1 snRNP. The U1 snRNP is composed of the U1 snRNA and the 7 core Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP, and at least three U1 snRNP-specific proteins SNRNP70/U1-70K, SNRPA/U1-A and SNRPC/U1-C (By similarity). Interacts with SCNM1 (PubMed:17656373). Found in a pre-mRNA splicing complex with SFRS4, SFRS5, SNRNP70, SNRPA1, SRRM1 and SRRM2. Found in a pre-mRNA exonic splicing enhancer (ESE) complex with SNRNP70, SNRPA1, SRRM1 and TRA2B/SFRS10. Interacts with dephosphorylated SFRS13A and SFPQ. Interacts with NUDT21/CPSF5, CPSF6, SCAF11, and ZRANB2. Interacts with GEMIN5 (By similarity). Interacts with FUS (By similarity). {ECO:0000250|UniProtKB:P08621, ECO:0000269|PubMed:17656373}. DOMAIN: The RRM domain mediates interaction with U1 RNA. {ECO:0000250|UniProtKB:P08621}. +P60122 RUVB1_MOUSE RuvB-like 1 (EC 3.6.4.12) (49 kDa TATA box-binding protein-interacting protein) (49 kDa TBP-interacting protein) (DNA helicase p50) (Pontin 52) (TIP49a) 456 50,214 Chain (1); Cross-link (4); Modified residue (1); Nucleotide binding (1) FUNCTION: Possesses single-stranded DNA-stimulated ATPase and ATP-dependent DNA helicase (3' to 5') activity; hexamerization is thought to be critical for ATP hydrolysis and adjacent subunits in the ring-like structure contribute to the ATPase activity. {ECO:0000250}.; FUNCTION: Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. The NuA4 complex ATPase and helicase activities seem to be, at least in part, contributed by the association of RUVBL1 and RUVBL2 with EP400. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AFZ from the nucleosome (By similarity). {ECO:0000250}.; FUNCTION: Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. {ECO:0000250}.; FUNCTION: Plays an essential role in oncogenic transformation by MYC and also modulates transcriptional activation by the LEF1/TCF1-CTNNB1 complex. Essential for cell proliferation (By similarity). {ECO:0000250}.; FUNCTION: May be able to bind plasminogen at cell surface and enhance plasminogen activation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Forms homohexameric rings. Can form a dodecamer with RUVBL2 made of two stacked hexameric rings; however, even though RUVBL1 and RUVBL2 are present in equimolar ratio, the oligomeric status of each hexamer is not known. Oligomerization may regulate binding to nucleic acids and conversely, binding to nucleic acids may affect the dodecameric assembly. Interacts with the transcriptional activation domain of MYC. Component of the RNA polymerase II holoenzyme complex. May also act to bridge the LEF1/TCF1-CTNNB1 complex and TBP. Component of the NuA4 histone acetyltransferase complex which contains the catalytic subunit KAT5/TIP60 and the subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6. The NuA4 complex interacts with MYC and the adenovirus E1A protein. RUVBL1 interacts with EP400. Component of a NuA4-related complex which contains EP400, TRRAP/PAF400, SRCAP, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, actin, ACTL6A/BAF53A, VPS72 and YEATS4/GAS41. Component of the BAF53 complex, at least composed of ACTL6A/BAF53A, RUVBL1/TIP49, SMARCA2/BRM, and TRRAP/PAF400. Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Associates with alpha and gamma tubulins, particularly during metaphase and early anaphase. Interacts with NPAT. Component of the chromatin-remodeling INO80 complex; specifically part of a complex module associated with the helicase ATP-binding and the helicase C-terminal domain of INO80. Interacts with IGHMBP2. Interacts with OFD1. Interacts with HINT1. Component of a complex with USP49 and PSMC5. Component of a SWR1-like complex. Component of the R2TP complex composed at least of PIHD1, RUVBL1, RUVBL2 and RPAP3. Interacts with PIH1D1. Interacts with ITFG1. Interacts with WAC; WAC positively regulates MTOR activity by promoting the assembly of the TTT complex composed of TELO2, TTI1 and TTI2 and the RUVBL complex composed of RUVBL1 and RUVBL2 into the TTT-RUVBL complex which leads to the dimerization of the mTORC1 complex and its subsequent activation. {ECO:0000250|UniProtKB:Q9Y265}. +P55012 S12A2_MOUSE Solute carrier family 12 member 2 (Basolateral Na-K-Cl symporter) (Bumetanide-sensitive sodium-(potassium)-chloride cotransporter 1) 1205 131,034 Chain (1); Compositional bias (1); Glycosylation (2); Modified residue (11); Sequence conflict (2); Topological domain (13); Transmembrane (12) TRANSMEM 279 299 Helical. {ECO:0000255}.; TRANSMEM 303 323 Helical. {ECO:0000255}.; TRANSMEM 360 380 Helical. {ECO:0000255}.; TRANSMEM 404 424 Helical. {ECO:0000255}.; TRANSMEM 429 449 Helical. {ECO:0000255}.; TRANSMEM 480 500 Helical. {ECO:0000255}.; TRANSMEM 514 534 Helical. {ECO:0000255}.; TRANSMEM 585 605 Helical. {ECO:0000255}.; TRANSMEM 645 667 Helical. {ECO:0000255}.; TRANSMEM 674 691 Helical. {ECO:0000255}.; TRANSMEM 710 730 Helical. {ECO:0000255}.; TRANSMEM 893 913 Helical. {ECO:0000255}. TOPO_DOM 1 278 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 300 302 Extracellular. {ECO:0000255}.; TOPO_DOM 324 359 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 381 403 Extracellular. {ECO:0000255}.; TOPO_DOM 425 428 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 450 479 Extracellular. {ECO:0000255}.; TOPO_DOM 501 513 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 535 584 Extracellular. {ECO:0000255}.; TOPO_DOM 606 644 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 668 673 Extracellular. {ECO:0000255}.; TOPO_DOM 692 709 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 731 892 Extracellular. {ECO:0000255}.; TOPO_DOM 914 1205 Cytoplasmic. {ECO:0000255}. FUNCTION: Electrically silent transporter system. Mediates sodium and chloride reabsorption. Plays a vital role in the regulation of ionic balance and cell volume. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. +P59158 S12A3_MOUSE Solute carrier family 12 member 3 (Na-Cl symporter) (Thiazide-sensitive sodium-chloride cotransporter) 1002 110,694 Chain (1); Glycosylation (4); Modified residue (9); Mutagenesis (3); Topological domain (7); Transmembrane (12) TRANSMEM 134 154 Helical. {ECO:0000255}.; TRANSMEM 165 185 Helical. {ECO:0000255}.; TRANSMEM 217 237 Helical. {ECO:0000255}.; TRANSMEM 260 280 Helical. {ECO:0000255}.; TRANSMEM 285 305 Helical. {ECO:0000255}.; TRANSMEM 338 358 Helical. {ECO:0000255}.; TRANSMEM 376 396 Helical. {ECO:0000255}.; TRANSMEM 451 471 Helical. {ECO:0000255}.; TRANSMEM 510 530 Helical. {ECO:0000255}.; TRANSMEM 576 596 Helical. {ECO:0000255}.; TRANSMEM 659 679 Helical. {ECO:0000255}.; TRANSMEM 811 831 Helical. {ECO:0000255}. TOPO_DOM 1 133 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 186 216 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 281 284 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 359 375 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 472 509 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 597 658 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 832 1002 Cytoplasmic. {ECO:0000255}. FUNCTION: Electroneutral sodium and chloride ion cotransporter. In kidney distal convoluted tubules, key mediator of sodium and chloride reabsorption (By similarity). Receptor for the proinflammatory cytokine IL18. Contributes to IL18-induced cytokine production, including IFNG, IL6, IL18 and CCL2. May act either independently of IL18R1, or in a complex with IL18R1 (PubMed:26099046). {ECO:0000250|UniProtKB:P55017, ECO:0000269|PubMed:26099046}. PTM: Ubiquitinated; ubiquitination is essential for regulation of endocytosis. {ECO:0000269|PubMed:20392800}.; PTM: Phosphorylated in response to IL18. {ECO:0000269|PubMed:26099046}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26099046}; Multi-pass membrane protein. SUBUNIT: Interacts with KLHL3 (By similarity). Interacts with IL18R1 in peritoneal macrophages; this interaction is increased by IL18 treatment (PubMed:26099046). {ECO:0000250|UniProtKB:P55017, ECO:0000269|PubMed:26099046}. TISSUE SPECIFICITY: Expressed predominantly in kidney, including in distal tubules (at protein level). Detected at low levels in heart, lung and liver. Not detected in normal aorta, but abundantly expressed in fatty streaks and advanced atherosclerotic lesions. In atherosclerotic lesions, expressed in macrophages, smooth muscle cells and endothelial cells (at protein level). {ECO:0000269|PubMed:26099046}. +Q91V14 S12A5_MOUSE Solute carrier family 12 member 5 (Electroneutral potassium-chloride cotransporter 2) (K-Cl cotransporter 2) (mKCC2) (Neuronal K-Cl cotransporter) 1138 126,271 Alternative sequence (1); Chain (1); Erroneous initiation (1); Glycosylation (2); Modified residue (4); Mutagenesis (2); Sequence conflict (2); Topological domain (7); Transmembrane (12) TRANSMEM 134 154 Helical. {ECO:0000255}.; TRANSMEM 156 176 Helical. {ECO:0000255}.; TRANSMEM 195 215 Helical. {ECO:0000255}.; TRANSMEM 217 237 Helical. {ECO:0000255}.; TRANSMEM 255 275 Helical. {ECO:0000255}.; TRANSMEM 278 298 Helical. {ECO:0000255}.; TRANSMEM 419 439 Helical. {ECO:0000255}.; TRANSMEM 459 479 Helical. {ECO:0000255}.; TRANSMEM 497 517 Helical. {ECO:0000255}.; TRANSMEM 570 590 Helical. {ECO:0000255}.; TRANSMEM 631 651 Helical. {ECO:0000255}.; TRANSMEM 848 868 Helical. {ECO:0000255}. TOPO_DOM 1 133 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 177 194 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 238 254 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 299 418 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 480 496 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 591 630 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 869 1138 Cytoplasmic. {ECO:0000255}. FUNCTION: Mediates electroneutral potassium-chloride cotransport in mature neurons and is required for neuronal Cl(-) homeostasis. As major extruder of intracellular chloride, it establishes the low neuronal Cl(-) levels required for chloride influx after binding of GABA-A and glycine to their receptors, with subsequent hyperpolarization and neuronal inhibition. Involved in the regulation of dendritic spine formation and maturation. {ECO:0000250|UniProtKB:Q63633}. SUBCELLULAR LOCATION: Cell projection, dendrite {ECO:0000269|PubMed:11395011}. Cell membrane {ECO:0000269|PubMed:11395011}; Multi-pass membrane protein {ECO:0000269|PubMed:11395011}. Note=Detected on dendrites, but not on axons of spinal cord neurons and at GPHN-positive inhibitory synapses. SUBUNIT: Homomultimer and heteromultimer with other K-Cl cotransporters (By similarity). Interacts with AP2A1. {ECO:0000250, ECO:0000269|PubMed:18625303}. TISSUE SPECIFICITY: Isoform 2 expressed in brainstem and spinal cord, isoform 1 expressed in brainstem, spinal cord and olfactory bulb of E17 embryos. Isoforms 1 and 2 expressed in all parts of the brain and spinal cord in postnatal day 14 mice. {ECO:0000269|PubMed:17715129}. +E9Q401 RYR2_MOUSE Ryanodine receptor 2 (RYR-2) (RyR2) (Cardiac muscle ryanodine receptor) (Cardiac muscle ryanodine receptor-calcium release channel) (Type 2 ryanodine receptor) 4966 564,819 Beta strand (54); Chain (1); Domain (8); Helix (30); Intramembrane (1); Modified residue (10); Mutagenesis (11); Region (2); Repeat (4); Sequence conflict (9); Topological domain (2); Transmembrane (7); Turn (13) INTRAMEM 4819 4828 Pore-forming. {ECO:0000305}. TRANSMEM 4232 4252 Helical. {ECO:0000255}.; TRANSMEM 4278 4298 Helical. {ECO:0000255}.; TRANSMEM 4502 4522 Helical. {ECO:0000255}.; TRANSMEM 4579 4599 Helical. {ECO:0000255}.; TRANSMEM 4729 4749 Helical. {ECO:0000255}.; TRANSMEM 4768 4788 Helical. {ECO:0000255}.; TRANSMEM 4849 4869 Helical. {ECO:0000255}. TOPO_DOM 1 4231 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 4870 4966 Cytoplasmic. {ECO:0000255}. FUNCTION: Calcium channel that mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytoplasm and thereby plays a key role in triggering cardiac muscle contraction. Aberrant channel activation can lead to cardiac arrhythmia. In cardiac myocytes, calcium release is triggered by increased Ca(2+) levels due to activation of the L-type calcium channel CACNA1C. The calcium channel activity is modulated by formation of heterotetramers with RYR3. Required for cellular calcium ion homeostasis. Required for embryonic heart development. {ECO:0000269|PubMed:10473538, ECO:0000269|PubMed:20431056, ECO:0000269|PubMed:21098440, ECO:0000269|PubMed:9628868}. PTM: Channel activity is modulated by phosphorylation. Phosphorylation at Ser-2807 and Ser-2813 increases the open probability of the calcium channel. Phosphorylation is increased in failing heart, leading to calcium leaks and increased cytoplasmic Ca(2+) levels. {ECO:0000269|PubMed:17693412, ECO:0000269|PubMed:20431056, ECO:0000269|PubMed:21098440}.; PTM: Phosphorylation at Ser-2030 by PKA enhances the response to lumenal calcium. {ECO:0000269|PubMed:17693412}. SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane {ECO:0000305|PubMed:10473538}; Multi-pass membrane protein {ECO:0000305|PubMed:10473538}. Membrane {ECO:0000305|PubMed:10473538}; Multi-pass membrane protein {ECO:0000305|PubMed:10473538}. Sarcoplasmic reticulum {ECO:0000250|UniProtKB:P30957}. Note=The number of predicted transmembrane domains varies between orthologs, but both N-terminus and C-terminus seem to be cytoplasmic. {ECO:0000250}. SUBUNIT: Homotetramer. Can also form heterotetramers with RYR1 and RYR3. Interacts with CALM and S100A1; these interactions regulate channel activity. Identified in a complex composed of RYR2, FKBP1B, PKA catalytic subunit, PRKAR2A, AKAP6, and the protein phosphatases PP2A and PP1. Interacts directly with FKBP1B, PKA, PP1 and PP2A (By similarity). Interacts with FKBP1A and FKBP1B; these interactions may stabilize the channel in its closed state and prevent Ca(2+) leaks. Interacts with SELENON (By similarity). Identified in a complex, composed of FSD2, CMYA5 and RYR2 (PubMed:28740084). {ECO:0000250|UniProtKB:P30957, ECO:0000250|UniProtKB:Q92736, ECO:0000269|PubMed:10473538, ECO:0000269|PubMed:20431056, ECO:0000269|PubMed:21098440, ECO:0000269|PubMed:28740084}. DOMAIN: The calcium release channel activity resides in the C-terminal region while the remaining part of the protein resides in the cytoplasm. {ECO:0000305}. TISSUE SPECIFICITY: Highly expressed in heart, lung, cerebellum and brain. Detected at lower levels in adrenal gland, stomach, thymus, esophagus and ovary. {ECO:0000269|PubMed:7621815, ECO:0000269|PubMed:7876312}. +O35602 RX_MOUSE Retinal homeobox protein Rx (Retina and anterior neural fold homeobox protein) 342 36,335 Chain (1); Compositional bias (1); DNA binding (1); Motif (3); Sequence conflict (4) FUNCTION: Plays a critical role in eye formation by regulating the initial specification of retinal cells and/or their subsequent proliferation. Binds to the photoreceptor conserved element-I (PCE-1/Ret 1) in the photoreceptor cell-specific arrestin promoter (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. TISSUE SPECIFICITY: Expressed in the photoreceptor and inner nuclear layers. +P97352 S10AD_MOUSE Protein S100-A13 (S100 calcium-binding protein A13) 98 11,158 Beta strand (2); Calcium binding (2); Chain (1); Domain (1); Helix (7); Modified residue (1); Turn (1) FUNCTION: Plays a role in the export of proteins that lack a signal peptide and are secreted by an alternative pathway. Binds two calcium ions per subunit. Binds one copper ion. Binding of one copper ion does not interfere with calcium binding. Required for the copper-dependent stress-induced export of IL1A and FGF1. The calcium-free protein binds to lipid vesicles containing phosphatidylserine, but not to vesicles containing phosphatidylcholine. {ECO:0000269|PubMed:11432880, ECO:0000269|PubMed:12746488, ECO:0000269|PubMed:17991455}. SUBCELLULAR LOCATION: Cytoplasm. Secreted. Note=Secretion is mediated by exposure to stress and requires copper ions. SUBUNIT: Homodimer. Part of a copper-dependent multiprotein complex containing S100A13, FGF1 and SYT1. Interacts with FGF1 and SYT1. {ECO:0000269|PubMed:11432880, ECO:0000269|PubMed:17991455, ECO:0000269|Ref.9}. +Q5SWT3 S2535_MOUSE Solute carrier family 25 member 35 300 32,631 Chain (1); Erroneous gene model prediction (1); Erroneous initiation (1); Repeat (3); Transmembrane (6) TRANSMEM 38 58 Helical; Name=1. {ECO:0000255}.; TRANSMEM 59 79 Helical; Name=2. {ECO:0000255}.; TRANSMEM 91 119 Helical; Name=3. {ECO:0000255}.; TRANSMEM 169 190 Helical; Name=4. {ECO:0000255}.; TRANSMEM 205 225 Helical; Name=5. {ECO:0000255}.; TRANSMEM 277 300 Helical; Name=6. {ECO:0000255}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q9WVC8 S26A3_MOUSE Chloride anion exchanger (Down-regulated in adenoma) (Protein DRA) (Solute carrier family 26 member 3) 757 83,590 Chain (1); Domain (1); Glycosylation (2); Helix (2); Topological domain (12); Transmembrane (11) TRANSMEM 72 92 Helical. {ECO:0000255}.; TRANSMEM 94 114 Helical. {ECO:0000255}.; TRANSMEM 125 145 Helical. {ECO:0000255}.; TRANSMEM 177 197 Helical. {ECO:0000255}.; TRANSMEM 202 222 Helical. {ECO:0000255}.; TRANSMEM 251 271 Helical. {ECO:0000255}.; TRANSMEM 279 299 Helical. {ECO:0000255}.; TRANSMEM 336 356 Helical. {ECO:0000255}.; TRANSMEM 368 388 Helical. {ECO:0000255}.; TRANSMEM 405 425 Helical. {ECO:0000255}.; TRANSMEM 463 483 Helical. {ECO:0000255}. TOPO_DOM 1 71 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 93 93 Extracellular. {ECO:0000305}.; TOPO_DOM 115 124 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 146 176 Extracellular. {ECO:0000305}.; TOPO_DOM 198 201 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 223 250 Extracellular. {ECO:0000305}.; TOPO_DOM 272 278 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 300 335 Extracellular. {ECO:0000305}.; TOPO_DOM 357 367 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 389 404 Extracellular. {ECO:0000305}.; TOPO_DOM 426 462 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 484 757 Extracellular. {ECO:0000305}. FUNCTION: Chloride/bicarbonate exchanger. Mediates the efficient absorption of chloride ions in the colon, participating in fluid homeostasis. Plays a role in the chloride and bicarbonate homeostasis during sperm epididymal maturation and capacitation. {ECO:0000269|PubMed:10428871, ECO:0000269|PubMed:21976599}. PTM: N-glycosylation is required for efficient cell surface expression, and protection from proteolytic degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Membrane {ECO:0000269|PubMed:21976599}; Multi-pass membrane protein {ECO:0000269|PubMed:21976599}. Note=Localized in sperm membranes. Midpiece of sperm tail. Colocalizes with CFTR at the midpiece of sperm tail. SUBUNIT: Interacts with PDZK1 (By similarity). Interacts with CFTR, SLC26A6 and SLC9A3R1. {ECO:0000250, ECO:0000269|PubMed:21976599}. TISSUE SPECIFICITY: Expressed in spermatogenic cells. {ECO:0000269|PubMed:21976599}. +Q922Q5 S35B3_MOUSE Adenosine 3'-phospho 5'-phosphosulfate transporter 2 (PAPS transporter 2) (Solute carrier family 35 member B3) 369 40,889 Chain (1); Glycosylation (2); Transmembrane (10) TRANSMEM 46 66 Helical. {ECO:0000255}.; TRANSMEM 79 99 Helical. {ECO:0000255}.; TRANSMEM 115 135 Helical. {ECO:0000255}.; TRANSMEM 138 158 Helical. {ECO:0000255}.; TRANSMEM 168 188 Helical. {ECO:0000255}.; TRANSMEM 191 211 Helical. {ECO:0000255}.; TRANSMEM 235 255 Helical. {ECO:0000255}.; TRANSMEM 266 285 Helical. {ECO:0000255}.; TRANSMEM 292 314 Helical. {ECO:0000255}.; TRANSMEM 317 337 Helical. {ECO:0000255}. FUNCTION: Mediates the transport of adenosine 3'-phospho 5'-phosphosulfate (PAPS), from cytosol into Golgi. PAPS is a universal sulfuryl donor for sulfation events that take place in the Golgi. Compensates for the insufficient expression of SLC35B2/PAPST1 during the synthesis of sulfated glycoconjugates in the colon (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q762D5 S35D2_MOUSE UDP-N-acetylglucosamine/UDP-glucose/GDP-mannose transporter (Solute carrier family 35 member D2) (UDP-galactose transporter-related protein 8) (UGTrel8) 326 35,896 Alternative sequence (2); Chain (1); Sequence conflict (1); Topological domain (9); Transmembrane (8) TRANSMEM 16 36 Helical. {ECO:0000255}.; TRANSMEM 42 62 Helical. {ECO:0000255}.; TRANSMEM 131 151 Helical. {ECO:0000255}.; TRANSMEM 156 176 Helical. {ECO:0000255}.; TRANSMEM 190 210 Helical. {ECO:0000255}.; TRANSMEM 226 246 Helical. {ECO:0000255}.; TRANSMEM 254 276 Helical. {ECO:0000255}.; TRANSMEM 281 303 Helical. {ECO:0000255}. TOPO_DOM 1 15 Extracellular. {ECO:0000255}.; TOPO_DOM 37 41 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 63 130 Extracellular. {ECO:0000255}.; TOPO_DOM 152 155 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 177 189 Extracellular. {ECO:0000255}.; TOPO_DOM 211 225 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 247 253 Extracellular. {ECO:0000255}.; TOPO_DOM 277 280 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 304 326 Extracellular. {ECO:0000255}. FUNCTION: Antiporter transporting nucleotide sugars such as UDP-N-acetylglucosamine (UDP-GlcNAc), UDP-glucose (UDP-Glc) and GDP-mannose (GDP-Man) pooled in the cytosol into the lumen of the Golgi in exchange for the corresponding nucleosides monophosphates (UMP for UDP-sugars and GMP for GDP-sugars). May take part in heparan sulfate synthesis by supplying UDP-Glc-NAc, the donor substrate, and thus be involved in growth factor signaling (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q8BGF8 S35D3_MOUSE Solute carrier family 35 member D3 (Fringe connection-like protein 1) 422 44,917 Chain (1); Frameshift (1); Sequence conflict (1); Transmembrane (10) TRANSMEM 9 29 Helical. {ECO:0000255}.; TRANSMEM 38 58 Helical. {ECO:0000255}.; TRANSMEM 64 84 Helical. {ECO:0000255}.; TRANSMEM 103 123 Helical. {ECO:0000255}.; TRANSMEM 131 151 Helical. {ECO:0000255}.; TRANSMEM 155 175 Helical. {ECO:0000255}.; TRANSMEM 187 207 Helical. {ECO:0000255}.; TRANSMEM 224 244 Helical. {ECO:0000255}.; TRANSMEM 257 277 Helical. {ECO:0000255}.; TRANSMEM 280 300 Helical. {ECO:0000255}. FUNCTION: May play a role in hemostasis as a regulator of the biosynthesis of platelet-dense granules. {ECO:0000269|PubMed:17062724}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in brain. {ECO:0000269|PubMed:17062724}. +Q61420 S35A1_MOUSE CMP-sialic acid transporter (CMP-SA-Tr) (CMP-Sia-Tr) (Solute carrier family 35 member A1) 336 36,453 Chain (1); Sequence conflict (4); Topological domain (11); Transmembrane (10) TRANSMEM 10 30 Helical. {ECO:0000255}.; TRANSMEM 46 64 Helical. {ECO:0000255}.; TRANSMEM 88 108 Helical. {ECO:0000255}.; TRANSMEM 114 135 Helical. {ECO:0000255}.; TRANSMEM 142 160 Helical. {ECO:0000255}.; TRANSMEM 176 196 Helical. {ECO:0000255}.; TRANSMEM 213 228 Helical. {ECO:0000255}.; TRANSMEM 244 262 Helical. {ECO:0000255}.; TRANSMEM 273 291 Helical. {ECO:0000255}.; TRANSMEM 297 315 Helical. {ECO:0000255}. TOPO_DOM 1 9 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 31 45 Lumenal. {ECO:0000255}.; TOPO_DOM 65 87 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 109 113 Lumenal. {ECO:0000255}.; TOPO_DOM 136 141 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 161 175 Lumenal. {ECO:0000255}.; TOPO_DOM 197 212 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 229 243 Lumenal. {ECO:0000255}.; TOPO_DOM 263 272 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 292 296 Lumenal. {ECO:0000255}.; TOPO_DOM 316 336 Cytoplasmic. {ECO:0000255}. FUNCTION: Transport CMP-sialic acid from the cytosol into Golgi vesicles where glycosyltransferases function. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:10085119}; Multi-pass membrane protein {ECO:0000269|PubMed:10085119}. TISSUE SPECIFICITY: Found in all the tissues examined including skeletal muscle, brain, heart, liver, kidney and spleen. +Q9Z2J0 S23A1_MOUSE Solute carrier family 23 member 1 (Na(+)/L-ascorbic acid transporter 1) (Sodium-dependent vitamin C transporter 1) (Yolk sac permease-like molecule 3) 605 65,554 Chain (1); Glycosylation (2); Intramembrane (1); Modified residue (3); Sequence conflict (4); Topological domain (14); Transmembrane (12) INTRAMEM 237 250 Helical. {ECO:0000255}. TRANSMEM 60 80 Helical. {ECO:0000255}.; TRANSMEM 89 109 Helical. {ECO:0000255}.; TRANSMEM 111 131 Helical. {ECO:0000255}.; TRANSMEM 167 187 Helical. {ECO:0000255}.; TRANSMEM 215 232 Helical. {ECO:0000255}.; TRANSMEM 258 278 Helical. {ECO:0000255}.; TRANSMEM 320 340 Helical. {ECO:0000255}.; TRANSMEM 366 386 Helical. {ECO:0000255}.; TRANSMEM 410 430 Helical. {ECO:0000255}.; TRANSMEM 434 454 Helical. {ECO:0000255}.; TRANSMEM 465 485 Helical. {ECO:0000255}.; TRANSMEM 498 518 Helical. {ECO:0000255}. TOPO_DOM 1 59 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 81 88 Extracellular. {ECO:0000255}.; TOPO_DOM 110 110 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 132 166 Extracellular. {ECO:0000255}.; TOPO_DOM 188 214 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 233 236 Extracellular. {ECO:0000255}.; TOPO_DOM 251 257 Extracellular. {ECO:0000255}.; TOPO_DOM 279 319 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 341 365 Extracellular. {ECO:0000255}.; TOPO_DOM 387 409 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 431 433 Extracellular. {ECO:0000255}.; TOPO_DOM 455 464 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 486 497 Extracellular. {ECO:0000255}.; TOPO_DOM 519 605 Cytoplasmic. {ECO:0000255}. FUNCTION: Sodium/ascorbate cotransporter. Mediates electrogenic uptake of vitamin C, with a stoichiometry of 2 Na(+) for each ascorbate (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein. +Q8CFZ5 S22AC_MOUSE Solute carrier family 22 member 12 (Renal-specific transporter) (RST) (Urate anion exchanger 1) 553 60,194 Chain (1); Glycosylation (1); Modified residue (2); Sequence conflict (1); Transmembrane (12) TRANSMEM 10 30 Helical. {ECO:0000255}.; TRANSMEM 146 166 Helical. {ECO:0000255}.; TRANSMEM 182 202 Helical. {ECO:0000255}.; TRANSMEM 204 224 Helical. {ECO:0000255}.; TRANSMEM 232 252 Helical. {ECO:0000255}.; TRANSMEM 260 280 Helical. {ECO:0000255}.; TRANSMEM 351 371 Helical. {ECO:0000255}.; TRANSMEM 378 398 Helical. {ECO:0000255}.; TRANSMEM 412 432 Helical. {ECO:0000255}.; TRANSMEM 435 455 Helical. {ECO:0000255}.; TRANSMEM 466 486 Helical. {ECO:0000255}.; TRANSMEM 495 515 Helical. {ECO:0000255}. FUNCTION: Required for efficient urate re-absorption in the kidney. Regulates blood urate levels. Mediates saturable urate uptake by facilitating the exchange of urate against organic anions or chloride ions. {ECO:0000269|PubMed:14747372}. PTM: N-glycosylated. {ECO:0000269|PubMed:14747372}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14747372}; Multi-pass membrane protein {ECO:0000269|PubMed:14747372}. Note=Detected in the luminal membrane of the epithelium of renal proximal tubules. SUBUNIT: Interacts with PDZK1. {ECO:0000250}. TISSUE SPECIFICITY: Detected in kidney (at protein level). Detected in kidney cortex, in proximal tubules. {ECO:0000269|PubMed:14747372, ECO:0000269|PubMed:9409754}. +Q8C8Y5 SAMD7_MOUSE Sterile alpha motif domain-containing protein 7 (SAM domain-containing protein 7) 445 49,259 Alternative sequence (2); Chain (1); Domain (1); Erroneous translation (1) FUNCTION: Involved in the regulation of gene expression in the retina. It functions as a negative regulator of CRX-controlled genes. {ECO:0000269|PubMed:23565263}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23565263}. Cytoplasm {ECO:0000269|PubMed:23565263}. TISSUE SPECIFICITY: Expressed in the retina and the pineal gland. In the retina, it is predominantly expressed in the outer nuclear layer. {ECO:0000269|PubMed:23565263}. +Q3U2P1 SC24A_MOUSE Protein transport protein Sec24A (SEC24-related protein A) 1090 118,782 Alternative sequence (2); Chain (1); Compositional bias (1); Frameshift (1); Metal binding (4); Region (1); Repeat (1); Sequence conflict (3) FUNCTION: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules for their transport to the Golgi complex. Plays a central role in cargo selection within the COPII complex and together with SEC24B may have a different specificity compared to SEC24C and SEC24D. May package preferentially cargos with cytoplasmic DxE or LxxLE motifs and may also recognize conformational epitopes. {ECO:0000250|UniProtKB:O95486}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250|UniProtKB:O95486}; Peripheral membrane protein {ECO:0000250|UniProtKB:O95486}; Cytoplasmic side {ECO:0000250|UniProtKB:O95486}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O95486}; Peripheral membrane protein {ECO:0000250|UniProtKB:O95486}; Cytoplasmic side {ECO:0000250|UniProtKB:O95486}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:O95486}. SUBUNIT: COPII is composed of at least five proteins: the Sec23/24 complex, the Sec13/31 complex and Sar1. Interacts with TMED2. Interacts (as part of the Sec23/24 complex) with SEC22B; recruits SEC22B into COPII-coated vesicles for its transport from the endoplasmic reticulum to the Golgi. {ECO:0000250|UniProtKB:O95486}. +O35316 SC6A6_MOUSE Sodium- and chloride-dependent taurine transporter (Solute carrier family 6 member 6) 621 69,856 Chain (1); Glycosylation (3); Modified residue (1); Sequence conflict (1); Topological domain (3); Transmembrane (12) TRANSMEM 50 70 Helical; Name=1. {ECO:0000255}.; TRANSMEM 77 97 Helical; Name=2. {ECO:0000255}.; TRANSMEM 123 143 Helical; Name=3. {ECO:0000255}.; TRANSMEM 216 236 Helical; Name=4. {ECO:0000255}.; TRANSMEM 245 265 Helical; Name=5. {ECO:0000255}.; TRANSMEM 290 310 Helical; Name=6. {ECO:0000255}.; TRANSMEM 332 352 Helical; Name=7. {ECO:0000255}.; TRANSMEM 380 400 Helical; Name=8. {ECO:0000255}.; TRANSMEM 430 450 Helical; Name=9. {ECO:0000255}.; TRANSMEM 465 485 Helical; Name=10. {ECO:0000255}.; TRANSMEM 508 528 Helical; Name=11. {ECO:0000255}.; TRANSMEM 545 565 Helical; Name=12. {ECO:0000255}. TOPO_DOM 1 49 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 144 215 Extracellular. {ECO:0000255}.; TOPO_DOM 566 621 Cytoplasmic. {ECO:0000255}. FUNCTION: Sodium-dependent taurine and beta-alanine transporter. Chloride ions are necessary for optimal uptake. {ECO:0000269|PubMed:1465453, ECO:0000269|PubMed:22896705}. PTM: Down-regulated upon Ser-322 phosphorylation. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1465453}; Multi-pass membrane protein {ECO:0000269|PubMed:1465453}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:1465453, ECO:0000269|PubMed:22896705}. +Q9CQS8 SC61B_MOUSE Protein transport protein Sec61 subunit beta 96 9,958 Chain (1); Initiator methionine (1); Lipidation (1); Modified residue (6); Topological domain (1); Transmembrane (1) TRANSMEM 71 91 Helical. {ECO:0000255}. TOPO_DOM 2 70 Cytoplasmic. {ECO:0000255}. FUNCTION: Component of SEC61 channel-forming translocon complex that mediates transport of signal peptide-containing precursor polypeptides across endoplasmic reticulum (ER) (By similarity). Required for PKD1/Polycystin-1 biogenesis (PubMed:28375157). {ECO:0000250|UniProtKB:P60467, ECO:0000269|PubMed:28375157}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. SUBUNIT: The ER translocon complex consists of channel-forming core components SEC61A1, SEC61B and SEC61G and different auxiliary components such as SEC62 and SEC63. {ECO:0000250|UniProtKB:P60467}. +Q9ERN0 SCAM2_MOUSE Secretory carrier-associated membrane protein 2 (Secretory carrier membrane protein 2) 329 36,465 Chain (1); Modified residue (2); Region (1); Topological domain (5); Transmembrane (4) TRANSMEM 154 174 Helical. {ECO:0000255}.; TRANSMEM 182 202 Helical. {ECO:0000255}.; TRANSMEM 219 239 Helical. {ECO:0000255}.; TRANSMEM 263 283 Helical. {ECO:0000255}. TOPO_DOM 1 153 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 175 181 Lumenal. {ECO:0000255}.; TOPO_DOM 203 218 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 240 262 Lumenal. {ECO:0000255}.; TOPO_DOM 284 329 Cytoplasmic. {ECO:0000255}. FUNCTION: Functions in post-Golgi recycling pathways. Acts as a recycling carrier to the cell surface (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Recycling endosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with SLC6A4 and SLC9A7. {ECO:0000250}. +Q8K299 SCAR5_MOUSE Scavenger receptor class A member 5 491 53,667 Alternative sequence (3); Chain (1); Coiled coil (1); Disulfide bond (3); Domain (2); Glycosylation (7); Sequence conflict (5); Topological domain (2); Transmembrane (1) TRANSMEM 61 81 Helical; Signal-anchor for type II membrane protein. {ECO:0000255|HAMAP-Rule:MF_03070}. TOPO_DOM 1 60 Cytoplasmic. {ECO:0000255|HAMAP-Rule:MF_03070}.; TOPO_DOM 82 491 Extracellular. {ECO:0000255|HAMAP-Rule:MF_03070}. FUNCTION: Ferritin receptor that mediates non-transferrin-dependent delivery of iron. Mediates cellular uptake of ferritin-bound iron by stimulating ferritin endocytosis from the cell surface with consequent iron delivery within the cell. Delivery of iron to cells by ferritin is required for the development of specific cell types, suggesting the existence of cell type-specific mechanisms of iron traffic in organogenesis, which alternatively utilize transferrin or non-transferrin iron delivery pathways. Ferritin mediates iron uptake in capsule cells of the developing kidney. Binds preferrentially ferritin light chain (FTL) compared to heavy chain (FTH1). {ECO:0000255|HAMAP-Rule:MF_03070, ECO:0000269|PubMed:19154717}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_03070, ECO:0000269|PubMed:19154717}; Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_03070, ECO:0000269|PubMed:19154717}. SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_03070, ECO:0000269|PubMed:16407294}. TISSUE SPECIFICITY: Expressed in the testis, trachea, lung, bladder and small intestine; especially in epithelial cells associated with mucosal surfaces. {ECO:0000269|PubMed:16407294}. +Q9JJV9 SCN5A_MOUSE Sodium channel protein type 5 subunit alpha (Sodium channel protein cardiac muscle subunit alpha) (Sodium channel protein type V subunit alpha) (Voltage-gated sodium channel subunit alpha Nav1.5) (mH1) 2019 227,576 Alternative sequence (1); Chain (1); Disulfide bond (2); Domain (1); Glycosylation (13); Intramembrane (4); Modified residue (16); Region (2); Repeat (4); Sequence conflict (8); Topological domain (29); Transmembrane (24) INTRAMEM 358 382 Pore-forming. {ECO:0000250|UniProtKB:D0E0C2}.; INTRAMEM 886 906 Pore-forming. {ECO:0000250|UniProtKB:D0E0C2}.; INTRAMEM 1408 1429 Pore-forming. {ECO:0000250|UniProtKB:D0E0C2}.; INTRAMEM 1699 1721 Pore-forming. {ECO:0000250|UniProtKB:D0E0C2}. TRANSMEM 132 150 Helical; Name=S1 of repeat I. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 158 178 Helical; Name=S2 of repeat I. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 193 210 Helical; Name=S3 of repeat I. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 217 233 Helical; Name=S4 of repeat I. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 253 272 Helical; Name=S5 of repeat I. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 390 410 Helical; Name=S6 of repeat I. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 718 736 Helical; Name=S1 of repeat II. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 748 767 Helical; Name=S2 of repeat II. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 782 801 Helical; Name=S3 of repeat II. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 804 821 Helical; Name=S4 of repeat II. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 838 856 Helical; Name=S5 of repeat II. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 920 940 Helical; Name=S6 of repeat II. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1209 1226 Helical; Name=S1 of repeat III. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1240 1258 Helical; Name=S2 of repeat III. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1273 1291 Helical; Name=S3 of repeat III. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1300 1318 Helical; Name=S4 of repeat III. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1336 1355 Helical; Name=S5 of repeat III. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1447 1468 Helical; Name=S6 of repeat III. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1532 1549 Helical; Name=S1 of repeat IV. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1561 1579 Helical; Name=S2 of repeat IV. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1592 1609 Helical; Name=S3 of repeat IV. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1623 1639 Helical; Name=S4 of repeat IV. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1659 1676 Helical; Name=S5 of repeat IV. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1751 1773 Helical; Name=S6 of repeat IV. {ECO:0000250|UniProtKB:D0E0C2}. TOPO_DOM 1 131 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 151 157 Extracellular. {ECO:0000305}.; TOPO_DOM 179 192 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 211 216 Extracellular. {ECO:0000305}.; TOPO_DOM 234 252 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 273 357 Extracellular. {ECO:0000305}.; TOPO_DOM 383 389 Extracellular. {ECO:0000305}.; TOPO_DOM 411 717 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 737 747 Extracellular. {ECO:0000305}.; TOPO_DOM 768 781 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 802 803 Extracellular. {ECO:0000305}.; TOPO_DOM 822 837 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 857 885 Extracellular. {ECO:0000305}.; TOPO_DOM 907 919 Extracellular. {ECO:0000305}.; TOPO_DOM 941 1208 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1227 1239 Extracellular. {ECO:0000305}.; TOPO_DOM 1259 1272 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1292 1299 Extracellular. {ECO:0000305}.; TOPO_DOM 1319 1335 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1356 1407 Extracellular. {ECO:0000305}.; TOPO_DOM 1430 1446 Extracellular. {ECO:0000305}.; TOPO_DOM 1469 1531 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1550 1560 Extracellular. {ECO:0000305}.; TOPO_DOM 1580 1591 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1610 1622 Extracellular. {ECO:0000305}.; TOPO_DOM 1640 1658 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1677 1698 Extracellular. {ECO:0000305}.; TOPO_DOM 1722 1750 Extracellular. {ECO:0000305}.; TOPO_DOM 1774 2019 Cytoplasmic. {ECO:0000305}. FUNCTION: This protein mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient (PubMed:11834499, PubMed:23420830). It is a tetrodotoxin-resistant Na(+) channel isoform. This channel is responsible for the initial upstroke of the action potential. Channel inactivation is regulated by intracellular calcium levels (By similarity). {ECO:0000250|UniProtKB:Q14524, ECO:0000269|PubMed:11834499, ECO:0000269|PubMed:23420830}. PTM: Phosphorylation at Ser-1505 by PKC in a highly conserved cytoplasmic loop slows inactivation of the sodium channel and reduces peak sodium currents (By similarity). Regulated through phosphorylation by CaMK2D (PubMed:17124532). {ECO:0000250|UniProtKB:Q14524, ECO:0000269|PubMed:17124532}.; PTM: Ubiquitinated by NEDD4L; which promotes its endocytosis. Does not seem to be ubiquitinated by NEDD4 or WWP2. {ECO:0000250|UniProtKB:Q14524}.; PTM: Lacks the cysteine which covalently binds the conotoxin GVIIJ. This cysteine (position 868) is speculated in other sodium channel subunits alpha to be implied in covalent binding with the sodium channel subunit beta-2 or beta-4. {ECO:0000250|UniProtKB:P15389}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11834499, ECO:0000269|PubMed:23420830}; Multi-pass membrane protein {ECO:0000250|UniProtKB:D0E0C2}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q14524}. Cell membrane, sarcolemma, T-tubule {ECO:0000250|UniProtKB:P15389}. Note=RANGRF promotes trafficking to the cell membrane. {ECO:0000269|PubMed:23420830}. SUBUNIT: Interacts with the PDZ domain of the syntrophin SNTA1, SNTB1 and SNTB2 (PubMed:9412493). Interacts with NEDD4, NEDD4L, WWP2 and GPD1L (By similarity). Interacts with CALM (By similarity). Interacts with FGF13; the interaction is direct and may regulate SNC5A density at membranes and function (PubMed:21817159). Interacts with FGF12 and FGF14 (By similarity). Interacts with ANK3 (By similarity). {ECO:0000250|UniProtKB:Q14524, ECO:0000269|PubMed:21817159, ECO:0000269|PubMed:9412493}. DOMAIN: The sequence contains 4 internal repeats, each with 5 hydrophobic segments (S1, S2, S3, S5, S6) and one positively charged segment (S4). Segments S4 are probably the voltage-sensors and are characterized by a series of positively charged amino acids at every third position. {ECO:0000305}.; DOMAIN: The IQ domain mediates association with calmodulin. {ECO:0000250|UniProtKB:Q14524}. TISSUE SPECIFICITY: Expressed in the myocardium. {ECO:0000269|PubMed:11834499}. +Q9WU38 SCNNB_MOUSE Amiloride-sensitive sodium channel subunit beta (Beta-NaCH) (Epithelial Na(+) channel subunit beta) (Beta-ENaC) (Nonvoltage-gated sodium channel 1 subunit beta) (SCNEB) 638 72,197 Chain (1); Glycosylation (3); Modified residue (2); Sequence conflict (2); Topological domain (3); Transmembrane (2) TRANSMEM 51 71 Helical; Name=1. {ECO:0000255}.; TRANSMEM 531 551 Helical; Name=2. {ECO:0000255}. TOPO_DOM 1 50 Cytoplasmic. {ECO:0000250|UniProtKB:P37089}.; TOPO_DOM 72 530 Extracellular. {ECO:0000250|UniProtKB:P37089}.; TOPO_DOM 552 638 Cytoplasmic. {ECO:0000250|UniProtKB:P37089}. FUNCTION: Sodium permeable non-voltage-sensitive ion channel inhibited by the diuretic amiloride. Mediates the electrodiffusion of the luminal sodium (and water, which follows osmotically) through the apical membrane of epithelial cells. Plays an essential role in electrolyte and blood pressure homeostasis, but also in airway surface liquid homeostasis, which is important for proper clearance of mucus. Controls the reabsorption of sodium in kidney, colon, lung and sweat glands. Also plays a role in taste perception. {ECO:0000269|PubMed:10409305}. PTM: N-glycosylated. N-glycosylation is required for interaction with BPIFA1. {ECO:0000250|UniProtKB:P51168}.; PTM: Phosphorylated on serine and threonine residues. Aldosterone and insulin increase the basal level of phosphorylation. {ECO:0000250|UniProtKB:P37090}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:P37090}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P37089}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P37090}. Note=Apical membrane of epithelial cells. {ECO:0000250|UniProtKB:P37090}. SUBUNIT: Heterotrimer containing an alpha/SCNN1A, a beta/SCNN1B and a gamma/SCNN1G subunit. An additional delta/SCNN1D subunit exists only in some organisms and can replace the alpha/SCNN1A subunit to form an alternative channel with specific properties (By similarity). Interacts with NEDD4 (via WW domains) (PubMed:11244092, PubMed:15123669). Interacts with NEDD4L (via WW domains) (PubMed:11244092, PubMed:12424229, PubMed:15123669). Interacts with WWP1 (via WW domains). Interacts with WWP2 (via WW domains). Interacts with the full-length immature form of PCSK9 (pro-PCSK9) (By similarity). Interacts (N-glycosylated) with BPIFA1; the interaction is direct and inhibits the proteolytic processing of SCNN1A and SCNN1G and the activation of ENaC (By similarity). {ECO:0000250|UniProtKB:P51168, ECO:0000269|PubMed:11244092, ECO:0000269|PubMed:12424229, ECO:0000269|PubMed:15123669, ECO:0000305|PubMed:10409305}. TISSUE SPECIFICITY: Lung and kidney. {ECO:0000269|PubMed:10409305}. +Q01730 RSU1_MOUSE Ras suppressor protein 1 (RSP-1) (Rsu-1) 277 31,550 Chain (1); Initiator methionine (1); Modified residue (1); Repeat (7) FUNCTION: Potentially plays a role in the Ras signal transduction pathway. Capable of suppressing v-Ras transformation in vitro. +Q9D7N3 RT09_MOUSE 28S ribosomal protein S9, mitochondrial (MRP-S9) (S9mt) 390 44,929 Chain (1); Sequence conflict (2); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P82933}. SUBUNIT: Component of the mitochondrial ribosome small subunit (28S) which comprises a 12S rRNA and about 30 distinct proteins. {ECO:0000250|UniProtKB:P82933}. +Q9JIK9 RT34_MOUSE 28S ribosomal protein S34, mitochondrial (MRP-S34) (S34mt) (T-complex expressed gene 2 protein) 218 25,827 Chain (1); Mutagenesis (1); Sequence conflict (1) FUNCTION: Required for mitochondrial translation, plays a role in maintaining the stability of the small ribosomal subunit and the 12S rRNA that are required for mitoribosome formation. {ECO:0000269|PubMed:25816300}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25816300}. SUBUNIT: Component of the mitochondrial ribosome small subunit (28S) which comprises a 12S rRNA and about 30 distinct proteins. TISSUE SPECIFICITY: Widely expressed (at protein liver). {ECO:0000269|PubMed:25816300}. +P58059 RT21_MOUSE 28S ribosomal protein S21, mitochondrial (MRP-S21) (S21mt) 87 10,561 Chain (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P82920}. SUBUNIT: Component of the mitochondrial ribosome small subunit (28S) which comprises a 12S rRNA and about 30 distinct proteins. {ECO:0000250|UniProtKB:P82920}. +Q9CXW2 RT22_MOUSE 28S ribosomal protein S22, mitochondrial (MRP-S22) (S22mt) 359 41,192 Chain (1); Erroneous initiation (1); Modified residue (2) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P82649}. SUBUNIT: Component of the mitochondrial ribosome small subunit (28S) which comprises a 12S rRNA and about 30 distinct proteins. {ECO:0000250|UniProtKB:P82649}. +Q99PI8 RTN4R_MOUSE Reticulon-4 receptor (Nogo receptor) (NgR) (Nogo-66 receptor) (Nogo66 receptor-1) (NgR1) 473 50,987 Beta strand (15); Chain (1); Disulfide bond (5); Domain (2); Glycosylation (3); Helix (9); Lipidation (1); Propeptide (1); Repeat (8); Signal peptide (1); Turn (7) FUNCTION: Receptor for RTN4, OMG and MAG (PubMed:11201742, PubMed:12089450, PubMed:15504325, PubMed:18411262, PubMed:22923615). Functions as receptor for the sialylated gangliosides GT1b and GM1 (PubMed:18411262). Besides, functions as receptor for chondroitin sulfate proteoglycans (PubMed:22406547). Can also bind heparin (PubMed:22406547). Intracellular signaling cascades are triggered via the coreceptor NGFR (By similarity). Signaling mediates activation of Rho and downstream reorganization of the actin cytoskeleton (PubMed:22325200). Mediates axonal growth inhibition (By similarity). Mediates axonal growth inhibition and plays a role in regulating axon regeneration and neuronal plasticity in the adult central nervous system (PubMed:11201742, PubMed:12089450, PubMed:15504325, PubMed:22923615). Plays a role in postnatal brain development (PubMed:27339102). Required for normal axon migration across the brain midline and normal formation of the corpus callosum (PubMed:27339102). Protects motoneurons against apoptosis; protection against apoptosis is probably mediated via interaction with MAG (PubMed:26335717). Acts in conjunction with RTN4 and LINGO1 in regulating neuronal precursor cell motility during cortical development (PubMed:20093372). Like other family members, plays a role in restricting the number dendritic spines and the number of synapses that are formed during brain development (PubMed:22325200). {ECO:0000250|UniProtKB:Q9BZR6, ECO:0000269|PubMed:11201742, ECO:0000269|PubMed:12089450, ECO:0000269|PubMed:15504325, ECO:0000269|PubMed:20093372, ECO:0000269|PubMed:22325200, ECO:0000269|PubMed:22406547, ECO:0000269|PubMed:22923615, ECO:0000269|PubMed:26335717, ECO:0000269|PubMed:27339102}. PTM: N-glycosylated (PubMed:29095159). O-glycosylated. Contains terminal sialic acid groups on its glycan chains (By similarity). {ECO:0000250|UniProtKB:Q99M75, ECO:0000269|PubMed:29095159}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11201742, ECO:0000269|PubMed:22325200}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:11201742}. Membrane raft {ECO:0000250|UniProtKB:Q9BZR6}. Cell projection, dendrite {ECO:0000269|PubMed:22325200}. Cell projection, axon {ECO:0000269|PubMed:22325200}. Perikaryon {ECO:0000250|UniProtKB:Q99M75}. Note=Detected along dendrites and axons, close to synapses, but clearly excluded from synapses. {ECO:0000269|PubMed:22325200}. SUBUNIT: Homodimer (PubMed:29095159). Interacts with MAG (PubMed:12089450). Interacts with RTN4 (PubMed:15504325). Interacts with NGFR(PubMed:22923615). Interacts with LINGO1(PubMed:22923615). Interacts with KIAA0319L (By similarity). Interacts with OLFM1; this inhibits interaction with LINGO1 and NGFR (PubMed:22923615). Interacts with OMG (By similarity). {ECO:0000250|UniProtKB:Q99M75, ECO:0000250|UniProtKB:Q9BZR6, ECO:0000269|PubMed:12089450, ECO:0000269|PubMed:15504325, ECO:0000269|PubMed:22923615, ECO:0000269|PubMed:29095159}. TISSUE SPECIFICITY: Detected in embryonic hippocampus neurons (PubMed:22325200). Detected in brain (at protein level) (PubMed:15504325, PubMed:22406547). Detected in neurons in the neocortex, in hippocampus, dorsal thalamus, cerebellum granule cell layer and the mitral cell layer in the olfactory bulb (PubMed:15647357). Detected in brain, dorsal root ganglion and heart. {ECO:0000269|PubMed:11201742, ECO:0000269|PubMed:15504325, ECO:0000269|PubMed:15647357, ECO:0000269|PubMed:22325200, ECO:0000269|PubMed:22406547, ECO:0000269|PubMed:22923615}. +P57784 RU2A_MOUSE U2 small nuclear ribonucleoprotein A' (U2 snRNP A') 255 28,357 Chain (1); Cross-link (2); Domain (1); Modified residue (5); Repeat (4); Sequence conflict (2) FUNCTION: Involved in pre-mRNA splicing as component of the spliceosome. Associated with sn-RNP U2, where it contributes to the binding of stem loop IV of U2 snRNA. {ECO:0000250|UniProtKB:P09661}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P09661}. SUBUNIT: Identified in the spliceosome B complex. Identified in the spliceosome C complex. Found in a pre-mRNA splicing complex with SFRS4, SFRS5, SNRNP70, SNRPA1, SRRM1 and SRRM2. Found in a pre-mRNA exonic splicing enhancer (ESE) complex with SNRNP70, SNRPA1, SRRM1 and TRA2B. Contributes to the binding of stem loop IV of U2 snRNA with SNRPB2. {ECO:0000250|UniProtKB:P09661}. +Q5DTT4 RTL5_MOUSE Retrotransposon Gag-like protein 5 (Retrotransposon gag domain-containing protein 4) 599 68,721 Chain (1); Compositional bias (2); Erroneous initiation (1) +Q505G4 RTL6_MOUSE Retrotransposon Gag-like protein 6 (Mammalian retrotransposon-derived protein 6) (Protein LDOC1L) (Protein Sushi-15E3) 243 26,660 Chain (1); Coiled coil (1); Frameshift (1) TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15716091}. +Q8BG26 RUSC1_MOUSE RUN and SH3 domain-containing protein 1 893 95,195 Alternative sequence (2); Chain (1); Domain (2); Erroneous initiation (2); Erroneous termination (1); Region (2); Sequence conflict (1) FUNCTION: Putative signaling adapter which may play a role in neuronal differentiation. May be involved in regulation of NGF-dependent neurite outgrowth. Proposed to play a role in neuronal vesicular trafficking, specifically involving pre-synaptic membrane proteins. Seems to be involved in signaling pathways that are regulated by the prolonged activation of MAPK. Can regulate the polyubiquitination of IKBKG and thus may be involved in regulation of the NF-kappa-B pathway. {ECO:0000269|PubMed:22404429}. PTM: Phosphorylated on serine residues following nuclear translocation. {ECO:0000250}.; PTM: Polyubiquitinated; polyubiquitination involves TRAF6. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22404429}. Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:22404429}. Cytoplasmic vesicle {ECO:0000305|PubMed:22404429}. Early endosome {ECO:0000305|PubMed:22404429}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000269|PubMed:22404429}. Golgi apparatus {ECO:0000305|PubMed:22404429}. Note=Translocated to the nuclear envelope upon stimulation with NGF (By similarity). Associated with membranes and microtubules. {ECO:0000250}. SUBUNIT: Interacts with IKBKG and TRAF6 (By similarity). Interacts with F-actin, acetylated actin, TUBB3, STX1A, KIF5B and KLC1. {ECO:0000250, ECO:0000269|PubMed:22404429}. DOMAIN: The RUN domain is necessary for NGF induced nuclear redistribution. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain, brain stem and spinal chord (at protein level). +Q149F1 RUSD2_MOUSE RNA pseudouridylate synthase domain-containing protein 2 553 61,535 Active site (1); Chain (1); Modified residue (1); Sequence conflict (4) +P28700 RXRA_MOUSE Retinoic acid receptor RXR-alpha (Nuclear receptor subfamily 2 group B member 1) (Retinoid X receptor alpha) 467 51,217 Beta strand (2); Chain (1); Cross-link (2); DNA binding (1); Domain (1); Helix (14); Modified residue (8); Mutagenesis (12); Region (2); Turn (2); Zinc finger (2) FUNCTION: Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RAR/RXR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. The high affinity ligand for RXRs is 9-cis retinoic acid. RXRA serves as a common heterodimeric partner for a number of nuclear receptors. In the absence of ligand, the RXR-RAR heterodimers associate with a multiprotein complex containing transcription corepressors that induce histone acetylation, chromatin condensation and transcriptional suppression. On ligand binding, the corepressors dissociate from the receptors and associate with the coactivators leading to transcriptional activation. The RXRA/PPARA heterodimer is required for PPARA transcriptional activity on fatty acid oxidation genes such as ACOX1 and the P450 system genes. {ECO:0000269|PubMed:10383391, ECO:0000269|PubMed:12032153, ECO:0000269|PubMed:1310259}. PTM: Phosphorylated on serine and threonine residues mainly in the N-terminal modulating domain. Phosphorylated on Ser-28, in vitro, by PKA. This phosphorylation is required for repression of cAMP-mediated transcriptional activity of RARA (By similarity). Constiutively phosphorylated on Ser-22 in the presence or absence of ligand. Under stress conditions, hyperphosphorylated by activated JNK on Ser-61, Ser-75, Thr-87 and Ser-265. {ECO:0000250, ECO:0000269|PubMed:10383391, ECO:0000269|PubMed:12032153}.; PTM: Sumoylation negatively regulates transcriptional activity. Desumoylated specifically by SENP6 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Homodimer (By similarity). Heterodimer with RARA; required for ligand-dependent retinoic acid receptor transcriptional activity. Heterodimer with PPARA (via the leucine-like zipper in the LBD); the interaction is required for PPARA transcriptional activity. Also heterodimerizes with PPARG (By similarity). Interacts with coactivator NCOA3, PELP1, SENP6, SFPQ, DNTTIP2 and RNF8. Interacts with PRMT2. Interacts with BHLHE40/DEC1, BHLHE41/DEC2, NCOR1 and NCOR2. Interacts in a ligand-dependent fashion with MED1 (By similarity). Interacts with coactivator NCOA6, and FAM120B. Interacts with ASXL1. Interacts in a ligand-dependent fashion with NCOA1. Interacts with VDR (By similarity). {ECO:0000250, ECO:0000269|PubMed:10788465, ECO:0000269|PubMed:10882070, ECO:0000269|PubMed:15528208, ECO:0000269|PubMed:16606617, ECO:0000269|PubMed:17595322, ECO:0000269|PubMed:7838715}. DOMAIN: Composed of three domains: a modulating N-terminal or AF1 domain, a DNA-binding domain and a C-terminal ligand-binding or AF2 domain. +Q9CPR1 RWDD4_MOUSE RWD domain-containing protein 4 188 21,138 Chain (1); Domain (1) +P08207 S10AA_MOUSE Protein S100-A10 (Calpactin I light chain) (Calpactin-1 light chain) (Cellular ligand of annexin II) (S100 calcium-binding protein A10) (p10 protein) (p11) 97 11,186 Chain (1); Modified residue (4); Region (1) FUNCTION: Because S100A10 induces the dimerization of ANXA2/p36, it may function as a regulator of protein phosphorylation in that the ANXA2 monomer is the preferred target (in vitro) of tyrosine-specific kinase. SUBUNIT: Heterotetramer containing 2 light chains of S100A10/p11 and 2 heavy chains of ANXA2/p36. Interacts with SCN10A (By similarity). {ECO:0000250}. +Q8VI23 S12A8_MOUSE Solute carrier family 12 member 8 (Cation-chloride cotransporter 9) 705 77,020 Alternative sequence (4); Chain (1); Sequence conflict (2); Transmembrane (13) TRANSMEM 38 58 Helical. {ECO:0000255}.; TRANSMEM 69 89 Helical. {ECO:0000255}.; TRANSMEM 92 112 Helical. {ECO:0000255}.; TRANSMEM 121 141 Helical. {ECO:0000255}.; TRANSMEM 159 179 Helical. {ECO:0000255}.; TRANSMEM 181 201 Helical. {ECO:0000255}.; TRANSMEM 232 252 Helical. {ECO:0000255}.; TRANSMEM 268 288 Helical. {ECO:0000255}.; TRANSMEM 306 326 Helical. {ECO:0000255}.; TRANSMEM 368 388 Helical. {ECO:0000255}.; TRANSMEM 390 410 Helical. {ECO:0000255}.; TRANSMEM 587 607 Helical. {ECO:0000255}.; TRANSMEM 612 632 Helical. {ECO:0000255}. FUNCTION: Cation/chloride cotransporter that may play a role in the control of keratinocyte proliferation. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +A2AGL3 RYR3_MOUSE Ryanodine receptor 3 (RYR-3) (RyR3) (Brain ryanodine receptor-calcium release channel) (Brain-type ryanodine receptor) (Type 3 ryanodine receptor) 4863 551,328 Alternative sequence (1); Chain (1); Domain (8); Intramembrane (1); Region (3); Repeat (4); Sequence conflict (7); Site (1); Topological domain (2); Transmembrane (7) INTRAMEM 4716 4725 Pore-forming. {ECO:0000250}. TRANSMEM 4180 4200 Helical. {ECO:0000255}.; TRANSMEM 4403 4423 Helical. {ECO:0000255}.; TRANSMEM 4478 4498 Helical. {ECO:0000255}.; TRANSMEM 4603 4623 Helical. {ECO:0000255}.; TRANSMEM 4626 4646 Helical. {ECO:0000255}.; TRANSMEM 4665 4685 Helical. {ECO:0000255}.; TRANSMEM 4746 4766 Helical. {ECO:0000255}. TOPO_DOM 1 4179 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 4767 4863 Cytoplasmic. {ECO:0000255}. FUNCTION: Calcium channel that mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytoplasm in muscle and thereby plays a role in triggering muscle contraction. May regulate Ca(2+) release by other calcium channels. Calcium channel that mediates Ca(2+)-induced Ca(2+) release from the endoplasmic reticulum in non-muscle cells. Plays a role in cellular calcium signaling. Contributes to cellular calcium ion homeostasis. Isoform 2 lacks a predicted transmembrane segment and does not form functional calcium channels by itself; however, it can form tetramers with isoforms that contain the full complement of transmembrane segments and modulate their activity. {ECO:0000269|PubMed:11500519, ECO:0000269|PubMed:11717163, ECO:0000269|PubMed:17596299, ECO:0000269|PubMed:7621815, ECO:0000269|PubMed:8702664, ECO:0000269|PubMed:9582272}. SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane {ECO:0000305|PubMed:9582272}; Multi-pass membrane protein {ECO:0000305|PubMed:9582272}. Membrane {ECO:0000269|PubMed:9582272}; Multi-pass membrane protein {ECO:0000269|PubMed:9582272}. Microsome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Sarcoplasmic reticulum {ECO:0000250|UniProtKB:Q9TS33}. Note=The number of predicted transmembrane domains varies between orthologs, but both N-terminus and C-terminus seem to be cytoplasmic. {ECO:0000250}. SUBUNIT: Homotetramer. Isoform 2 can form tetramers with isoform 1. Heterotetramer with RYR2. Interacts with FKBP1A. Interacts with CALM. Interacts with SELENON (By similarity). {ECO:0000250|UniProtKB:Q9TS33}. DOMAIN: The calcium release channel activity resides in the C-terminal region while the remaining part of the protein resides in the cytoplasm. {ECO:0000305}. TISSUE SPECIFICITY: Detected in hippocampus, cerebellum, striatum, frontal brain cortex and parietal brain cortex. Detected in skeletal muscle, diaphragm muscle and myometrium (at protein level). Detected in egg cells. Detected in heart, diaphragm, stomach, spleen, ovary, testis germ cells, brain and cerebellum. Detected in cerebral artery smooth muscle cells. {ECO:0000269|PubMed:11717163, ECO:0000269|PubMed:17596299, ECO:0000269|PubMed:7621815, ECO:0000269|PubMed:7635066, ECO:0000269|PubMed:7876312, ECO:0000269|PubMed:9582272}. +Q7TPE5 S7A6O_MOUSE Probable RNA polymerase II nuclear localization protein SLC7A6OS (Solute carrier family 7 member 6 opposite strand transcript homolog) 306 35,041 Chain (1); Modified residue (2) FUNCTION: Directs RNA polymerase II nuclear import. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. +Q9D8F3 S52A2_MOUSE Solute carrier family 52, riboflavin transporter, member 2 (Porcine endogenous retrovirus A receptor 2 homolog) (PERV-A receptor 2 homolog) (Protein GPR172B) (Riboflavin transporter 1) (mRFT1) 450 46,864 Alternative sequence (2); Chain (1); Compositional bias (1); Glycosylation (1); Transmembrane (11) TRANSMEM 14 34 Helical. {ECO:0000255}.; TRANSMEM 47 67 Helical. {ECO:0000255}.; TRANSMEM 86 106 Helical. {ECO:0000255}.; TRANSMEM 112 132 Helical. {ECO:0000255}.; TRANSMEM 147 167 Helical. {ECO:0000255}.; TRANSMEM 201 221 Helical. {ECO:0000255}.; TRANSMEM 282 302 Helical. {ECO:0000255}.; TRANSMEM 317 337 Helical. {ECO:0000255}.; TRANSMEM 344 364 Helical. {ECO:0000255}.; TRANSMEM 369 389 Helical. {ECO:0000255}.; TRANSMEM 409 429 Helical. {ECO:0000255}. FUNCTION: Riboflavin transporter. Riboflavin transport is Na(+)-independent but moderately pH-sensitive. Activity is strongly inhibited by riboflavin analogs, such as lumiflavin. Weakly inhibited by flavin adenine dinucleotide (FAD). In case of infection by retroviruses, acts as a cell receptor to retroviral envelopes similar to the porcine endogenous retrovirus (PERV-A) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q8BYA0 TBCD_MOUSE Tubulin-specific chaperone D (Beta-tubulin cofactor D) (Tubulin-folding cofactor D) 1196 133,321 Chain (1); Repeat (4) FUNCTION: Tubulin-folding protein implicated in the first step of the tubulin folding pathway and required for tubulin complex assembly. Involved in the regulation of microtubule polymerization or depolymerization, it modulates microtubule dynamics by capturing GTP-bound beta-tubulin (TUBB). Its ability to interact with beta tubulin is regulated via its interaction with ARL2. Acts as a GTPase-activating protein (GAP) for ARL2. Induces microtubule disruption in absence of ARL2. Increases degradation of beta tubulin, when overexpressed in polarized cells. Promotes epithelial cell detachment, a process antagonized by ARL2. Induces tight adherens and tight junctions disassembly at the lateral cell membrane. Required for correct assembly and maintenance of the mitotic spindle, and proper progression of mitosis. Involved in neuron morphogenesis. {ECO:0000250|UniProtKB:Q28205, ECO:0000250|UniProtKB:Q9BTW9}. SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000250|UniProtKB:Q28205}. Lateral cell membrane {ECO:0000250|UniProtKB:Q28205}. Cytoplasm {ECO:0000250|UniProtKB:Q28205}. Cell junction, adherens junction {ECO:0000250|UniProtKB:Q28205}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9BTW9}. Note=Localized in cell-cell contacts. {ECO:0000250|UniProtKB:Q28205}. SUBUNIT: Found in a complex with at least ARL2, PPP2CB, PPP2R1A, PPP2R2A, PPP2R5E and TBCD. Interacts with PPP2CB (By similarity). Part of a supercomplex made of cofactors A to E. Cofactors A and D function by capturing and stabilizing tubulin in a quasi-native conformation. Cofactor E binds to the cofactor D-tubulin complex; interaction with cofactor C then causes the release of tubulin polypeptides that are committed to the native state. Interacts with ARL2; interaction is enhanced with the GDP-bound form of ARL2. Does not interact with ARL3, ARL4A and ARL4D. Interacts with beta tubulin. Interacts with TBCE (By similarity). {ECO:0000250|UniProtKB:Q28205, ECO:0000250|UniProtKB:Q9BTW9}. +Q8CDA1 SAC2_MOUSE Phosphatidylinositide phosphatase SAC2 (EC 3.1.3.25) (Inositol polyphosphate 5-phosphatase F) (Sac domain-containing inositol phosphatase 2) (Sac domain-containing phosphoinositide 4-phosphatase 2) (hSAC2) 1132 127,608 Alternative sequence (5); Chain (1); Domain (2); Frameshift (1); Modified residue (8); Mutagenesis (2); Sequence conflict (1) FUNCTION: Inositol 4-phosphatase which mainly acts on phosphatidylinositol 4-phosphate. May be functionally linked to OCRL, which converts phosphatidylinositol 4,5-bisphosphate to phosphatidylinositol, for a sequential dephosphorylation of phosphatidylinositol 4,5-bisphosphate at the 5 and 4 position of inositol, thus playing an important role in the endocytic recycling (PubMed:25869668, PubMed:25869669). Regulator of TF:TFRC and integrins recycling pathway, is also involved in cell migration mechanisms (By similarity). Modulates AKT/GSK3B pathway by decreasing AKT and GSK3B phosphorylation (PubMed:17322895). Negatively regulates STAT3 signaling pathway through inhibition of STAT3 phosphorylation and translocation to the nucleus (By similarity). Functionally important modulator of cardiac myocyte size and of the cardiac response to stress (PubMed:19875726). May play a role as negative regulator of axon regeneration after central nervous system injuries (PubMed:26203138). {ECO:0000250|UniProtKB:Q9Y2H2, ECO:0000269|PubMed:17322895, ECO:0000269|PubMed:19875726, ECO:0000269|PubMed:25869668, ECO:0000269|PubMed:25869669, ECO:0000269|PubMed:26203138}. SUBCELLULAR LOCATION: Membrane, clathrin-coated pit {ECO:0000269|PubMed:25869668}. Early endosome {ECO:0000269|PubMed:25869668}. Recycling endosome {ECO:0000250|UniProtKB:Q9Y2H2}. Note=Also found on macropinosomes. {ECO:0000269|PubMed:25869668}. SUBUNIT: Homodimer (By similarity). Interacts with OCRL and RAB5. Interacts with INPP5B and INPP4A (PubMed:25869668). Interacts with STAT3; the interaction is independent of STAT3 'TYR-705' phosphorylation status (By similarity). {ECO:0000250|UniProtKB:Q9Y2H2, ECO:0000269|PubMed:25869668}. TISSUE SPECIFICITY: Highly expressed in brain and hypothalamus, expressed in lung and pancreas, and detected at low levels in liver and heart (at protein level). {ECO:0000269|PubMed:25869669, ECO:0000269|PubMed:26203138}. +O88576 S6A18_MOUSE Sodium-dependent neutral amino acid transporter B(0)AT3 (Sodium- and chloride-dependent transporter XTRP2) (Solute carrier family 6 member 18) (System B(0) neutral amino acid transporter AT3) 615 69,229 Alternative sequence (6); Chain (1); Glycosylation (1); Mutagenesis (22); Topological domain (13); Transmembrane (12) TRANSMEM 27 47 Helical; Name=1. {ECO:0000255}.; TRANSMEM 53 73 Helical; Name=2. {ECO:0000255}.; TRANSMEM 106 126 Helical; Name=3. {ECO:0000255}.; TRANSMEM 178 198 Helical; Name=4. {ECO:0000255}.; TRANSMEM 207 227 Helical; Name=5. {ECO:0000255}.; TRANSMEM 256 276 Helical; Name=6. {ECO:0000255}.; TRANSMEM 289 309 Helical; Name=7. {ECO:0000255}.; TRANSMEM 398 418 Helical; Name=8. {ECO:0000255}.; TRANSMEM 442 462 Helical; Name=9. {ECO:0000255}.; TRANSMEM 473 493 Helical; Name=10. {ECO:0000255}.; TRANSMEM 521 541 Helical; Name=11. {ECO:0000255}.; TRANSMEM 571 591 Helical; Name=12. {ECO:0000255}. TOPO_DOM 1 26 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 48 52 Extracellular. {ECO:0000255}.; TOPO_DOM 74 105 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 127 177 Extracellular. {ECO:0000255}.; TOPO_DOM 199 206 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 228 255 Extracellular. {ECO:0000255}.; TOPO_DOM 277 288 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 310 397 Extracellular. {ECO:0000255}.; TOPO_DOM 419 441 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 463 472 Extracellular. {ECO:0000255}.; TOPO_DOM 494 520 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 542 570 Extracellular. {ECO:0000255}.; TOPO_DOM 592 615 Cytoplasmic. {ECO:0000255}. FUNCTION: Functions as a sodium and chloride-dependent neutral amino acid transporter in kidneys (PubMed:26240152, PubMed:19478081). Required CLTRN for cell surface expression and for its amino acid transporter activity (PubMed:26240152). {ECO:0000269|PubMed:19478081, ECO:0000269|PubMed:26240152}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:19478081}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:26240152}; Multi-pass membrane protein {ECO:0000255}. Note=In kidneys localizes to the apical membrane in distal segments of the proximal tubule. {ECO:0000269|PubMed:19478081}. SUBUNIT: Interacts with CLTRN; this interaction regulates the trafficking of SLC6A18 to the cell membrane and its activity. {ECO:0000269|PubMed:19478081, ECO:0000269|PubMed:26240152}. TISSUE SPECIFICITY: Expressed predominantly in kidney. {ECO:0000269|PubMed:9932288}. +Q68FF9 S5A1_MOUSE 3-oxo-5-alpha-steroid 4-dehydrogenase 1 (EC 1.3.1.22) (SR type 1) (Steroid 5-alpha-reductase 1) (S5AR 1) 255 29,344 Chain (1); Sequence conflict (3); Transmembrane (5) TRANSMEM 6 26 Helical. {ECO:0000255}.; TRANSMEM 82 102 Helical. {ECO:0000255}.; TRANSMEM 107 127 Helical. {ECO:0000255}.; TRANSMEM 142 162 Helical. {ECO:0000255}.; TRANSMEM 205 225 Helical. {ECO:0000255}. FUNCTION: Converts testosterone into 5-alpha-dihydrotestosterone and progesterone or corticosterone into their corresponding 5-alpha-3-oxosteroids. It plays a central role in sexual differentiation and androgen physiology (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9D9X8 SACA3_MOUSE Sperm acrosome membrane-associated protein 3 (Lysozyme-like protein 3) (Sperm lysozyme-like protein 1) (mSLLP1) [Cleaved into: Sperm acrosome membrane-associated protein 3, membrane form; Sperm acrosome membrane-associated protein 3, processed form] 221 25,020 Alternative sequence (1); Beta strand (4); Chain (2); Disulfide bond (4); Helix (8); Sequence conflict (3); Site (1); Topological domain (2); Transmembrane (1); Turn (4) TRANSMEM 70 90 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 69 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 91 221 Extracellular. {ECO:0000255}. FUNCTION: Sperm surface membrane protein that may be involved in sperm-egg plasma membrane adhesion and fusion during fertilization. It could be a potential receptor for the egg oligosaccharide residue N-acetylglucosamine, which is present in the extracellular matrix over the egg plasma membrane. The processed form has no detectable bacteriolytic activity in vitro (By similarity). {ECO:0000250, ECO:0000269|PubMed:15982649}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome membrane {ECO:0000305|PubMed:15982649}; Single-pass type II membrane protein {ECO:0000305|PubMed:15982649}. Note=Anterior acrosome in non-capacitated spermatozoa and retained in the equatorial segment and in the luminal face of both the inner and outer acrosomal membranes following capacitation and the acrosome reaction.; SUBCELLULAR LOCATION: Isoform 2: Secreted {ECO:0000305}. SUBUNIT: Interacts with ASTL. {ECO:0000269|PubMed:22206759}. TISSUE SPECIFICITY: The processed form is expressed in sperm (at protein level). Expressed strongly in testis and epididymis and weakly in pancreas. {ECO:0000269|PubMed:15982649, ECO:0000269|PubMed:16014814}. +P12246 SAMP_MOUSE Serum amyloid P-component (SAP) 224 26,247 Chain (1); Disulfide bond (1); Domain (1); Glycosylation (1); Metal binding (8); Sequence conflict (3); Signal peptide (1) SUBCELLULAR LOCATION: Secreted. SUBUNIT: Homopentamer. Pentraxin (or pentaxin) have a discoid arrangement of 5 non-covalently bound subunits. DISEASE: Note=SAP is a precursor of amyloid component P which is found in basement membrane and associated with amyloid deposits. +Q9D5N8 SATL1_MOUSE Spermidine/spermine N(1)-acetyltransferase-like protein 1 (EC 2.3.1.-) 744 83,276 Binding site (2); Chain (1); Domain (1); Erroneous initiation (1); Region (4); Sequence conflict (4) +P57725 SAMN1_MOUSE SAM domain-containing protein SAMSN-1 (SAM domain, SH3 domain and nuclear localization signals protein 1) (SH3 protein expressed in lymphocytes 2) (SH3-lymphocyte protein 2) (SLy2) 372 41,601 Chain (1); Domain (2); Helix (6); Modified residue (8); Motif (1); Mutagenesis (1); Sequence conflict (7); Turn (2) FUNCTION: Negative regulator of B-cell activation. Down-regulates cell proliferation (in vitro). Promotes RAC1-dependent membrane ruffle formation and reorganization of the actin cytoskeleton. Regulates cell spreading and cell polarization. Stimulates HDAC1 activity. Regulates LYN activity by modulating its tyrosine phosphorylation. {ECO:0000269|PubMed:15381729, ECO:0000269|PubMed:19923443, ECO:0000269|PubMed:20478393, ECO:0000269|PubMed:21296879}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cell projection, ruffle. Note=Shuttles between cytoplasm and nucleus. Colocalizes with the actin cytoskeleton and actin-rich membrane ruffles. SUBUNIT: Interacts with FASLG (By similarity). Interacts with phosphotyrosine containing proteins. Interacts (via SH3 domain) with CTTN. Interacts (phosphorylated at Ser-23) with YWHAB, YWHAE, YWHAG, YWHAH, YWHAZ and SFN. Interacts directly with SAP30 and HDAC1. Identified in a complex with SAP30 and HDAC1. {ECO:0000250, ECO:0000269|PubMed:15381729, ECO:0000269|PubMed:20478393, ECO:0000269|PubMed:21296879}. TISSUE SPECIFICITY: Detected in spleen and lymph node (at protein level). {ECO:0000269|PubMed:15381729}. +A3KGA4 TCAL7_MOUSE Transcription elongation factor A protein-like 7 (TCEA-like protein 7) (Transcription elongation factor S-II protein-like 7) 98 11,697 Chain (1); Coiled coil (1); Compositional bias (1) FUNCTION: Plays a role in the negative regulation of NF-kappa-B signaling at the basal level by modulating transcriptional activity of NF-kappa-B on its target gene promoters. Associates with cyclin D1 promoter containing Myc E-box sequence and transcriptionally represses cyclin D1 expression. Regulates telomerase reverse transcriptase expression and telomerase activity in both ALT (alternative lengthening of telomeres)and telomerase-positive cell lines (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +P56840 TCLB1_MOUSE Protein TCL1B1 116 13,432 Chain (1) +P56845 TCLB5_MOUSE Protein TCL1B5 121 13,668 Chain (1) +Q61327 SC6A3_MOUSE Sodium-dependent dopamine transporter (DA transporter) (DAT) (Solute carrier family 6 member 3) 619 68,805 Chain (1); Disulfide bond (2); Glycosylation (4); Metal binding (9); Mutagenesis (4); Region (1); Site (1); Topological domain (3); Transmembrane (12) TRANSMEM 69 89 Helical; Name=1. {ECO:0000255}.; TRANSMEM 96 116 Helical; Name=2. {ECO:0000255}.; TRANSMEM 140 160 Helical; Name=3. {ECO:0000255}.; TRANSMEM 237 255 Helical; Name=4. {ECO:0000255}.; TRANSMEM 264 281 Helical; Name=5. {ECO:0000255}.; TRANSMEM 317 334 Helical; Name=6. {ECO:0000255}.; TRANSMEM 346 367 Helical; Name=7. {ECO:0000255}.; TRANSMEM 400 419 Helical; Name=8. {ECO:0000255}.; TRANSMEM 446 464 Helical; Name=9. {ECO:0000255}.; TRANSMEM 480 500 Helical; Name=10. {ECO:0000255}.; TRANSMEM 521 540 Helical; Name=11. {ECO:0000255}.; TRANSMEM 559 577 Helical; Name=12. {ECO:0000255}. TOPO_DOM 1 68 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 161 236 Extracellular. {ECO:0000255}.; TOPO_DOM 578 619 Cytoplasmic. {ECO:0000255}. FUNCTION: Amine transporter. Terminates the action of dopamine by its high affinity sodium-dependent reuptake into presynaptic terminals. {ECO:0000269|PubMed:10375632, ECO:0000269|PubMed:12606774, ECO:0000305}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10375632, ECO:0000269|PubMed:12606774}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q7K4Y6}. SUBUNIT: Homooligomer; disulfide-linked (By similarity). Interacts with PRKCABP and TGFB1I1. Interacts (via N-terminus) with SYNGR3 (via N-terminus). Interacts with SLC18A2. Interacts with TOR1A (ATP-bound); TOR1A regulates SLC6A3 subcellular location. {ECO:0000250|UniProtKB:Q01959, ECO:0000269|PubMed:12177201, ECO:0000269|PubMed:19357284}. TISSUE SPECIFICITY: Found in the substantia nigra and ventral tegmental dopamine neurons, in fibers of the medial forebrain bundle ascending into the striatum, and within dense fiber networks and varicosities in the dorsal and ventral striatum. Lower expression in the cortex. Absent from the corpus callosum. {ECO:0000269|PubMed:19357284}. +Q91XT4 SC16B_MOUSE Protein transport protein Sec16B (Leucine zipper transcription regulator 2) (Regucalcin gene promoter region-related protein p117) (RGPR-p117) (SEC16 homolog B) 1051 115,513 Chain (1); Compositional bias (3); Erroneous initiation (1); Modified residue (11); Region (1); Sequence conflict (12) FUNCTION: Plays a role in the organization of the endoplasmic reticulum exit sites (ERES), also known as transitional endoplasmic reticulum (tER). Required for secretory cargo traffic from the endoplasmic reticulum to the Golgi apparatus. Involved in peroxisome biogenesis. Regulates the transport of peroxisomal biogenesis factors PEX3 and PEX16 from the ER to peroxisomes. {ECO:0000250|UniProtKB:Q96JE7}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q96JE7}; Peripheral membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Localizes to endoplasmic reticulum exit sites (ERES), also known as transitional endoplasmic reticulum (tER). {ECO:0000250|UniProtKB:Q96JE7}. SUBUNIT: SEC16A and SEC16B are each present in multiple copies in a heteromeric complex. Interacts with TFG. Interacts with SEC13. {ECO:0000250|UniProtKB:Q96JE7}. TISSUE SPECIFICITY: Liver. {ECO:0000269|PubMed:12244571}. +Q1EHW4 SAP25_MOUSE Histone deacetylase complex subunit SAP25 (25 kDa Sin3-associated polypeptide) (Sin3 corepressor complex subunit SAP25) (mSin3A-binding protein) 186 19,845 Beta strand (4); Chain (1); Frameshift (1); Helix (1); Turn (2) FUNCTION: Involved in the transcriptional repression mediated by the mSIN3A but not the N-CoR corepressor complex. {ECO:0000269|PubMed:16449650}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16449650}. Cytoplasm {ECO:0000269|PubMed:16449650}. Note=Shuttles between the nucleus and the cytoplasm. SUBUNIT: May be a component of the mSIN3A corepressor complex. Interacts with SIN3A and HDAC2. {ECO:0000269|PubMed:16449650, ECO:0000269|PubMed:18089292}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:16449650}. +Q8K352 SASH3_MOUSE SAM and SH3 domain-containing protein 3 (SH3 protein expressed in lymphocytes) 380 41,609 Chain (1); Domain (2); Modified residue (12); Sequence conflict (1) FUNCTION: May function as a signaling adapter protein in lymphocytes. {ECO:0000269|PubMed:11470164}. TISSUE SPECIFICITY: Preferentially expressed in lymphoid tissues. Expressed in bone marrow, thymus, spleen, lymph nodes and Peyer patches of gut. In the spleen and lymph nodes, expressed in both T- and B-cells. In the thymus, in the medulla and cortex. {ECO:0000269|PubMed:11470164}. +D3YUG0 SAM13_MOUSE Sterile alpha motif domain-containing protein 13 (SAM domain-containing protein 13) 102 11,336 Chain (1); Domain (1) +Q6P8J2 SAT2_MOUSE Diamine acetyltransferase 2 (EC 2.3.1.57) (Polyamine N-acetyltransferase 2) (Spermidine/spermine N(1)-acetyltransferase 2) 170 19,305 Binding site (3); Chain (1); Domain (1); Modified residue (1); Region (4) Amine and polyamine degradation; putrescine degradation; N-acetylputrescine from putrescine: step 1/1. FUNCTION: Enzyme which catalyzes the acetylation of polyamines. Substrate specificity: norspermidine > spermidine = spermine >> N(1)acetylspermine = putrescine (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Intracellular organelles. {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +Q9ES03 TBX20_MOUSE T-box transcription factor TBX20 (T-box protein 20) 445 49,096 Alternative sequence (1); Chain (1); Compositional bias (3); DNA binding (1); Sequence conflict (2) FUNCTION: Acts as a transcriptional activator and repressor required for cardiac development and may have key roles in the maintenance of functional and structural phenotypes in adult heart. {ECO:0000269|PubMed:22328084}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00201}. TISSUE SPECIFICITY: Prominently expressed in the extraembryonic mesoderm, developing heart, eye analage and motor neurons of hindbrain and spinal cord. Expressed in extraembryonic tissues such as the amnion and allantois. {ECO:0000269|PubMed:11118890}. +Q9JKD8 TBX21_MOUSE T-box transcription factor TBX21 (T-box protein 21) (T-cell-specific T-box transcription factor T-bet) (Transcription factor TBLYM) 530 57,852 Beta strand (15); Chain (1); Cross-link (1); DNA binding (1); Helix (5); Modified residue (11); Mutagenesis (17); Sequence conflict (1); Site (1) FUNCTION: Lineage-defining transcription factor which initiates Th1 lineage development from naive Th precursor cells both by activating Th1 genetic programs and by repressing the opposing Th2 and Th17 genetic programs. Activates transcription of a set of genes important for Th1 cell function, including those encoding IFN-gamma and the chemokine receptor CXCR3. Activates IFNG and CXCR3 genes in part by recruiting chromatin remodeling complexes including KDM6B, a SMARCA4-containing SWI/SNF-complex, and an H3K4me2-methyltransferase complex to their promoters and all of these complexes serve to establish a more permissive chromatin state conducive with transcriptional activation (PubMed:10761931, PubMed:17923685, PubMed:21095589). Can activate Th1 genes also via recruitment of Mediator complex and P-TEFb (composed of CDK9 and CCNT1/cyclin-T1) in the form of the super elongation complex (SEC) to super-enhancers and associated genes in activated Th1 cells (PubMed:27292648). Inhibits the Th17 cell lineage commitment by blocking RUNX1-mediated transactivation of Th17 cell-specific transcriptinal regulator RORC (PubMed:21151104). Inhibits the Th2 cell lineage commitment by suppressing the production of Th2 cytokines, such as IL-4, IL-5, and IL- 13, via repression of transcriptional regulators GATA3 and NFATC2 (PubMed:15662016, PubMed:21690296, PubMed:23616576). Protects Th1 cells from amplifying aberrant type-I IFN response in an IFN-gamma abundant microenvironment by acting as a repressor of type-I IFN transcription factors and type-I IFN- stimulated genes (PubMed:28623086). Acts as a regulator of antiviral B-cell responses; controls chronic viral infection by promoting the antiviral antibody IgG2a isotype switching and via regulation of a broad antiviral gene expression program (PubMed:27430722). {ECO:0000269|PubMed:10761931, ECO:0000269|PubMed:15662016, ECO:0000269|PubMed:17923685, ECO:0000269|PubMed:21095589, ECO:0000269|PubMed:21151104, ECO:0000269|PubMed:21690296, ECO:0000269|PubMed:23616576, ECO:0000269|PubMed:27292648, ECO:0000269|PubMed:27430722, ECO:0000269|PubMed:28607488, ECO:0000269|PubMed:28623086}. PTM: Phosphorylations at Ser-52, Tyr-76, Ser-224 and Ser-508 are regulated by mTORC1 (PubMed:28424242). Phosphorylation at Tyr-525 is essential for its interaction GATA3 (PubMed:15662016). Phosphorylation at Tyr-219, Tyr-265 and Tyr-304 enhances its transcriptional activator activity (PubMed:21690296). Phosphorylation at Thr-302 is required for its interaction with NFATC2 (PubMed:23616576). {ECO:0000269|PubMed:15662016, ECO:0000269|PubMed:21690296, ECO:0000269|PubMed:23616576, ECO:0000269|PubMed:28424242}.; PTM: Ubiquitinated at Lys-313, leading to its degradation by the proteasome. Ubiquitination is essential for controlling protein stability, binding to the T-box-binding element of the IFN-gamma promoter, and for interaction with NFATC2 through induction of phosphorylation at Thr-302 (PubMed:23616576). Deubiquitinated by USP10 leading to its stabilization (By similarity). {ECO:0000250|UniProtKB:Q9UL17, ECO:0000269|PubMed:23616576}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10761931, ECO:0000269|PubMed:15662016, ECO:0000269|PubMed:21690296, ECO:0000269|PubMed:23616576}. SUBUNIT: Interacts with RUNX1 and RUNX3 (PubMed:21151104). Interacts with ITK (PubMed:15662016). The phosphorylated form (at Tyr-525) interacts with GATA3 (PubMed:15662016, PubMed:21690296, PubMed:23616576). Interacts with ABL1 (PubMed:21690296). Interacts with RELA (PubMed:23616576). The phosphorylated form (at Thr-302) interacts with NFATC2 (PubMed:23616576). Interacts with KDM6B (PubMed:21095589). Interacts with SMARCA4 in a KDM6B-dependent manner (PubMed:21095589). Interacts with CCTN1 and CDK9 (PubMed:27292648). Interacts with USP10 (By similarity). {ECO:0000250|UniProtKB:Q9UL17, ECO:0000269|PubMed:15662016, ECO:0000269|PubMed:21095589, ECO:0000269|PubMed:21151104, ECO:0000269|PubMed:21690296, ECO:0000269|PubMed:23616576, ECO:0000269|PubMed:27292648}. TISSUE SPECIFICITY: T-cell specific (PubMed:10761931, PubMed:11087660). Expressed in regulatory T (TReg) cells (PubMed:28607488). {ECO:0000269|PubMed:10761931, ECO:0000269|PubMed:11087660, ECO:0000269|PubMed:28607488}. +O08547 SC22B_MOUSE Vesicle-trafficking protein SEC22b (ER-Golgi SNARE of 24 kDa) (ERS-24) (ERS24) (SEC22 vesicle-trafficking protein homolog B) (SEC22 vesicle-trafficking protein-like 1) (mSec22b) 215 24,741 Beta strand (7); Chain (1); Domain (2); Helix (6); Modified residue (7); Sequence conflict (1); Topological domain (1); Transmembrane (1); Turn (5) TRANSMEM 195 215 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 1 194 Cytoplasmic. {ECO:0000255}. FUNCTION: SNARE involved in targeting and fusion of ER-derived transport vesicles with the Golgi complex as well as Golgi-derived retrograde transport vesicles with the ER. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q4KM74}; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:Q4KM74}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q4KM74}. Golgi apparatus, cis-Golgi network membrane {ECO:0000250|UniProtKB:Q4KM74}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q4KM74}. Melanosome {ECO:0000250|UniProtKB:O75396}. Note=Concentrated most in the intermediate compartment/cis-Golgi network and the cis-Golgi cisternae 1 and 2. Greatly reduced in concentration at the trans end of the Golgi apparatus. {ECO:0000250|UniProtKB:Q4KM74}. SUBUNIT: Interacts with STX17. Component of two distinct SNARE complexes consisting of STX5, GOSR2/BOS1, BET1 and SEC22B or STX18, USE1L, BNIP1/SEC20L and SEC22B. YKT6 can probably replace SEC22B as subunit of either complex (By similarity). Interacts with the COPII Sec23/24 complex composed of SEC23A and SEC24A; recruits SEC22B into COPII-coated vesicles to allow its transport from the endoplasmic reticulum to the Golgi (By similarity). {ECO:0000250|UniProtKB:O75396, ECO:0000250|UniProtKB:Q4KM74}. +Q761V0 SC6A5_MOUSE Sodium- and chloride-dependent glycine transporter 2 (GlyT-2) (GlyT2) (Solute carrier family 6 member 5) 799 87,861 Alternative sequence (1); Chain (1); Disulfide bond (1); Glycosylation (5); Metal binding (8); Modified residue (3); Sequence conflict (2); Topological domain (3); Transmembrane (12) TRANSMEM 202 222 Helical; Name=1. {ECO:0000255}.; TRANSMEM 229 249 Helical; Name=2. {ECO:0000255}.; TRANSMEM 273 293 Helical; Name=3. {ECO:0000255}.; TRANSMEM 397 417 Helical; Name=4. {ECO:0000255}.; TRANSMEM 433 453 Helical; Name=5. {ECO:0000255}.; TRANSMEM 472 492 Helical; Name=6. {ECO:0000255}.; TRANSMEM 510 530 Helical; Name=7. {ECO:0000255}.; TRANSMEM 565 585 Helical; Name=8. {ECO:0000255}.; TRANSMEM 611 631 Helical; Name=9. {ECO:0000255}.; TRANSMEM 640 660 Helical; Name=10. {ECO:0000255}.; TRANSMEM 677 697 Helical; Name=11. {ECO:0000255}.; TRANSMEM 717 737 Helical; Name=12. {ECO:0000255}. TOPO_DOM 1 201 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 294 396 Extracellular. {ECO:0000255}.; TOPO_DOM 738 799 Cytoplasmic. {ECO:0000255}. FUNCTION: Terminates the action of glycine by its high affinity sodium-dependent reuptake into presynaptic terminals. May be responsible for the termination of neurotransmission at strychnine-sensitive glycinergic synapses (By similarity). {ECO:0000250|UniProtKB:P58295}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P58295}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q7K4Y6}. TISSUE SPECIFICITY: Isoform a and isoform b are expressed at high levels in brain stem and spinal cord. Isoform a is also expressed in the cerebellum. {ECO:0000269|PubMed:15081419}. +Q3TZ89 SC31B_MOUSE Protein transport protein Sec31B (SEC31-like protein 2) (SEC31-related protein B) 1158 125,633 Alternative sequence (1); Chain (1); Compositional bias (1); Repeat (8); Sequence conflict (6) FUNCTION: As a component of the coat protein complex II (COPII), may function in vesicle budding and cargo export from the endoplasmic reticulum. {ECO:0000250|UniProtKB:Q9NQW1}. PTM: Monoubiquitinated by the BCR(KLHL12) E3 ubiquitin ligase complex, leading to regulate the size of COPII coats. {ECO:0000250|UniProtKB:Q9NQW1}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NQW1}. Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250|UniProtKB:Q9NQW1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9NQW1}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9NQW1}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9NQW1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9NQW1}. SUBUNIT: COPII is composed of at least 5 proteins: the SEC23/24 complex, the SEC13/31 complex and SAR1. SEC13 and SEC31 make a 2:2 tetramer that forms the edge element of the COPII outer coat. The tetramer self-assembles in multiple copies to form the complete polyhedral cage. Interacts (via WD 8) with SEC13 (By similarity). Interacts with SEC31A (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9NQW1}. +Q9JLI6 SCLY_MOUSE Selenocysteine lyase (mSCL) (EC 4.4.1.16) 432 47,174 Active site (1); Alternative sequence (1); Chain (1); Modified residue (3); Sequence conflict (3) FUNCTION: Catalyzes the decomposition of L-selenocysteine to L-alanine and elemental selenium. {ECO:0000269|PubMed:10692412}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10692412}. SUBUNIT: Homodimer. {ECO:0000269|PubMed:10692412}. TISSUE SPECIFICITY: Widely expressed. Present in liver, kidney, testis (at protein level). {ECO:0000269|PubMed:10692412}. +A2APX8 SCN1A_MOUSE Sodium channel protein type 1 subunit alpha (Sodium channel protein brain I subunit alpha) (Sodium channel protein type I subunit alpha) (Voltage-gated sodium channel subunit alpha Nav1.1) 2009 228,800 Alternative sequence (2); Chain (1); Disulfide bond (4); Domain (1); Glycosylation (4); Intramembrane (4); Modified residue (8); Mutagenesis (1); Region (2); Repeat (4); Topological domain (29); Transmembrane (24) INTRAMEM 368 392 Pore-forming. {ECO:0000250|UniProtKB:D0E0C2}.; INTRAMEM 937 957 Pore-forming. {ECO:0000250|UniProtKB:D0E0C2}.; INTRAMEM 1419 1440 Pore-forming. {ECO:0000250|UniProtKB:D0E0C2}.; INTRAMEM 1710 1732 Pore-forming. {ECO:0000250|UniProtKB:D0E0C2}. TRANSMEM 129 147 Helical; Name=S1 of repeat I. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 155 175 Helical; Name=S2 of repeat I. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 190 207 Helical; Name=S3 of repeat I. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 214 230 Helical; Name=S4 of repeat I. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 250 269 Helical; Name=S5 of repeat I. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 400 420 Helical; Name=S6 of repeat I. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 769 787 Helical; Name=S1 of repeat II. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 799 818 Helical; Name=S2 of repeat II. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 833 852 Helical; Name=S3 of repeat II. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 855 872 Helical; Name=S4 of repeat II. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 889 907 Helical; Name=S5 of repeat II. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 971 991 Helical; Name=S6 of repeat II. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1220 1237 Helical; Name=S1 of repeat III. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1251 1269 Helical; Name=S2 of repeat III. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1284 1302 Helical; Name=S3 of repeat III. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1311 1329 Helical; Name=S4 of repeat III. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1347 1366 Helical; Name=S5 of repeat III. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1458 1479 Helical; Name=S6 of repeat III. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1543 1560 Helical; Name=S1 of repeat IV. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1572 1590 Helical; Name=S2 of repeat IV. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1603 1620 Helical; Name=S3 of repeat IV. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1634 1650 Helical; Name=S4 of repeat IV. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1670 1687 Helical; Name=S5 of repeat IV. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1763 1785 Helical; Name=S6 of repeat IV. {ECO:0000250|UniProtKB:D0E0C2}. TOPO_DOM 1 128 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 148 154 Extracellular. {ECO:0000305}.; TOPO_DOM 176 189 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 208 213 Extracellular. {ECO:0000305}.; TOPO_DOM 231 249 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 270 367 Extracellular. {ECO:0000305}.; TOPO_DOM 393 399 Extracellular. {ECO:0000305}.; TOPO_DOM 421 768 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 788 798 Extracellular. {ECO:0000305}.; TOPO_DOM 819 832 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 853 854 Extracellular. {ECO:0000305}.; TOPO_DOM 873 888 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 908 936 Extracellular. {ECO:0000305}.; TOPO_DOM 958 970 Extracellular. {ECO:0000305}.; TOPO_DOM 992 1219 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1238 1250 Extracellular. {ECO:0000305}.; TOPO_DOM 1270 1283 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1303 1310 Extracellular. {ECO:0000305}.; TOPO_DOM 1330 1346 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1367 1418 Extracellular. {ECO:0000305}.; TOPO_DOM 1441 1457 Extracellular. {ECO:0000305}.; TOPO_DOM 1480 1542 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1561 1571 Extracellular. {ECO:0000305}.; TOPO_DOM 1591 1602 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1621 1633 Extracellular. {ECO:0000305}.; TOPO_DOM 1651 1669 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1688 1709 Extracellular. {ECO:0000305}.; TOPO_DOM 1733 1762 Extracellular. {ECO:0000305}.; TOPO_DOM 1786 2009 Cytoplasmic. {ECO:0000305}. FUNCTION: Mediates the voltage-dependent sodium ion permeability of excitable membranes (PubMed:16921370, PubMed:17928448, PubMed:27281198). Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient. Plays a key role in brain, probably by regulating the moment when neurotransmitters are released in neurons (PubMed:16921370, PubMed:22914087). Involved in sensory perception of mechanical pain: activation in somatosensory neurons induces pain without neurogenic inflammation and produces hypersensitivity to mechanical, but not thermal stimuli (PubMed:27281198). {ECO:0000269|PubMed:16921370, ECO:0000269|PubMed:17928448, ECO:0000269|PubMed:22914087, ECO:0000269|PubMed:27281198}. PTM: Phosphorylation at Ser-1516 by PKC in a highly conserved cytoplasmic loop slows inactivation of the sodium channel and reduces peak sodium currents. {ECO:0000250|UniProtKB:P04775}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P35498}; Multi-pass membrane protein {ECO:0000250|UniProtKB:D0E0C2}. SUBUNIT: The voltage-sensitive sodium channel consists of an ion conducting pore forming alpha-subunit regulated by one or more beta-1 (SCN1B), beta-2 (SCN2B), beta-3 (SCN3B) and/or beta-4 (SCN4B). Beta-1 (SCN1B) and beta-3 (SCN3B) are non-covalently associated with alpha, while beta-2 (SCN2B) and beta-4 (SCN4B) are covalently linked by disulfide bonds. Interacts with FGF13. Interacts with the conotoxin GVIIJ. {ECO:0000250|UniProtKB:P04774, ECO:0000250|UniProtKB:P35498}. DOMAIN: The S3b-S4 and S1-S2 loops of repeat IV are targeted by H.maculata toxins Hm1a and Hm1b, leading to inhibit fast inactivation of Nav1.1/SCN1A. Selectivity for H.maculata toxins Hm1a and Hm1b depends on S1-S2 loops of repeat IV (PubMed:27281198). {ECO:0000269|PubMed:27281198}.; DOMAIN: The sequence contains 4 internal repeats, each with 5 hydrophobic segments (S1, S2, S3, S5, S6) and one positively charged segment (S4). Segments S4 are probably the voltage-sensors and are characterized by a series of positively charged amino acids at every third position. {ECO:0000305}. TISSUE SPECIFICITY: Present in cerebellar Purkinje neurons (at protein level) (PubMed:17928448). Expressed by myelinated, non-C-fiber neurons in sensory ganglia (PubMed:27281198). {ECO:0000269|PubMed:17928448, ECO:0000269|PubMed:27281198}. +A2ASI5 SCN3A_MOUSE Sodium channel protein type 3 subunit alpha (Sodium channel protein brain III subunit alpha) (Sodium channel protein type III subunit alpha) (Voltage-gated sodium channel subtype III) (Voltage-gated sodium channel subunit alpha Nav1.3) 1947 220,880 Alternative sequence (2); Chain (1); Disulfide bond (4); Domain (1); Glycosylation (8); Intramembrane (4); Modified residue (4); Natural variant (1); Repeat (4); Topological domain (29); Transmembrane (24) INTRAMEM 369 393 Pore-forming. {ECO:0000250|UniProtKB:D0E0C2}.; INTRAMEM 880 900 Pore-forming. {ECO:0000250|UniProtKB:D0E0C2}.; INTRAMEM 1356 1377 Pore-forming. {ECO:0000250|UniProtKB:D0E0C2}.; INTRAMEM 1647 1669 Pore-forming. {ECO:0000250|UniProtKB:D0E0C2}. TRANSMEM 129 147 Helical; Name=S1 of repeat I. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 155 175 Helical; Name=S2 of repeat I. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 190 207 Helical; Name=S3 of repeat I. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 214 230 Helical; Name=S4 of repeat I. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 250 269 Helical; Name=S5 of repeat I. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 401 421 Helical; Name=S6 of repeat I. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 712 730 Helical; Name=S1 of repeat II. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 742 761 Helical; Name=S2 of repeat II. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 776 795 Helical; Name=S3 of repeat II. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 798 815 Helical; Name=S4 of repeat II. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 832 850 Helical; Name=S5 of repeat II. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 914 934 Helical; Name=S6 of repeat II. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1159 1177 Helical; Name=S1 of repeat III. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1191 1209 Helical; Name=S2 of repeat III. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1224 1242 Helical; Name=S3 of repeat III. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1251 1269 Helical; Name=S4 of repeat III. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1287 1306 Helical; Name=S5 of repeat III. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1395 1416 Helical; Name=S6 of repeat III. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1480 1497 Helical; Name=S1 of repeat IV. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1509 1527 Helical; Name=S2 of repeat IV. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1540 1557 Helical; Name=S3 of repeat IV. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1571 1587 Helical; Name=S4 of repeat IV. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1607 1624 Helical; Name=S5 of repeat IV. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1700 1722 Helical; Name=S6 of repeat IV. {ECO:0000250|UniProtKB:D0E0C2}. TOPO_DOM 1 128 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 148 154 Extracellular. {ECO:0000305}.; TOPO_DOM 176 189 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 208 213 Extracellular. {ECO:0000305}.; TOPO_DOM 231 249 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 270 368 Extracellular. {ECO:0000305}.; TOPO_DOM 394 400 Extracellular. {ECO:0000305}.; TOPO_DOM 422 711 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 731 741 Extracellular. {ECO:0000305}.; TOPO_DOM 762 775 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 796 797 Extracellular. {ECO:0000305}.; TOPO_DOM 816 831 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 851 879 Extracellular. {ECO:0000305}.; TOPO_DOM 901 913 Extracellular. {ECO:0000305}.; TOPO_DOM 935 1158 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1178 1190 Extracellular. {ECO:0000305}.; TOPO_DOM 1210 1223 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1243 1250 Extracellular. {ECO:0000305}.; TOPO_DOM 1270 1286 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1307 1355 Extracellular. {ECO:0000305}.; TOPO_DOM 1378 1394 Extracellular. {ECO:0000305}.; TOPO_DOM 1417 1479 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1498 1508 Extracellular. {ECO:0000305}.; TOPO_DOM 1528 1539 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1558 1570 Extracellular. {ECO:0000305}.; TOPO_DOM 1588 1606 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1625 1646 Extracellular. {ECO:0000305}.; TOPO_DOM 1670 1699 Extracellular. {ECO:0000305}.; TOPO_DOM 1723 1947 Cytoplasmic. {ECO:0000305}. FUNCTION: Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient (PubMed:29142310). May contribute to the regulation of serotonin/5-hydroxytryptamine release by enterochromaffin cells (PubMed:29142310). In pancreatic endocrine cells, required for both glucagon and glucose-induced insulin secretion (PubMed:25172946). {ECO:0000269|PubMed:25172946, ECO:0000269|PubMed:29142310}. PTM: May be ubiquitinated by NEDD4L; which would promote its endocytosis. {ECO:0000250|UniProtKB:Q9NY46}.; PTM: Phosphorylation at Ser-1453 in a highly conserved cytoplasmic loop slows inactivation of the channel and reduces peak sodium currents. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9NY46}; Multi-pass membrane protein {ECO:0000250|UniProtKB:D0E0C2}. Basal cell membrane {ECO:0000269|PubMed:29142310}. Note=In enterochromaffin cells, localized highly asymmetrically, almost exclusively at the basal side. {ECO:0000269|PubMed:29142310}. SUBUNIT: Heterooligomer of a large alpha subunit and 2-3 smaller beta subunits. Heterooligomer with SCN2B or SCN4B; disulfide-linked. Interacts with NEDD4L. {ECO:0000250|UniProtKB:Q9NY46}. DOMAIN: The sequence contains 4 internal repeats, each with 5 hydrophobic segments (S1, S2, S3, S5, S6) and one positively charged segment (S4). Segments S4 are probably the voltage-sensors and are characterized by a series of positively charged amino acids at every third position. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in enterochromaffin cells in both colon and small bowel (at protein level) (PubMed:29142310). Expressed in pancreatic alpha and beta cells (PubMed:25172946). {ECO:0000269|PubMed:25172946, ECO:0000269|PubMed:29142310}. +Q5SUC9 SCO1_MOUSE Protein SCO1 homolog, mitochondrial 284 31,617 Chain (1); Disulfide bond (1); Metal binding (3); Mutagenesis (1); Region (1); Topological domain (2); Transit peptide (1); Transmembrane (1) TRANSMEM 81 98 Helical. {ECO:0000255}. TOPO_DOM ? 80 Mitochondrial matrix. {ECO:0000250|UniProtKB:O75880}.; TOPO_DOM 99 284 Mitochondrial intermembrane. {ECO:0000250|UniProtKB:O75880}. FUNCTION: Copper metallochaperone essential for the maturation of cytochrome c oxidase subunit II (MT-CO2/COX2). Not required for the synthesis of MT-CO2/COX2 but plays a crucial role in stabilizing MT-CO2/COX2 during its subsequent maturation. Involved in transporting copper to the Cu(A) site on MT-CO2/COX2 (By similarity). Plays an important role in the regulation of copper homeostasis by controlling the abundance and cell membrane localization of copper transporter CTR1 (PubMed:25683716, PubMed:28973536). {ECO:0000250|UniProtKB:O75880, ECO:0000269|PubMed:25683716, ECO:0000269|PubMed:28973536}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:O75880}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:O75880}; Single-pass membrane protein {ECO:0000255}. SUBUNIT: Homodimer. Interacts with COA6. Found in a complex with TMEM177, COX20, COA6, MT-CO2/COX2, COX18 and SCO2. Interacts with TMEM177 in a COX20-dependent manner. Interacts with COX20 in a MT-CO2/COX2- and COX18-dependent manner. Interacts with COX16. {ECO:0000250|UniProtKB:O75880}. +Q8R127 SCPDL_MOUSE Saccharopine dehydrogenase-like oxidoreductase (EC 1.-.-.-) 429 47,129 Chain (1); Initiator methionine (1); Modified residue (4) +O35114 SCRB2_MOUSE Lysosome membrane protein 2 (85 kDa lysosomal membrane sialoglycoprotein) (LGP85) (Lysosome membrane protein II) (LIMP II) (Scavenger receptor class B member 2) 478 54,044 Chain (1); Disulfide bond (2); Glycosylation (11); Mutagenesis (22); Region (1); Topological domain (3); Transmembrane (2) TRANSMEM 5 27 Helical. {ECO:0000255}.; TRANSMEM 434 459 Helical. {ECO:0000255}. TOPO_DOM 1 4 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 28 433 Lumenal. {ECO:0000255}.; TOPO_DOM 460 478 Cytoplasmic. {ECO:0000255}. FUNCTION: Acts as a lysosomal receptor for glucosylceramidase (GBA) targeting. {ECO:0000269|PubMed:18022370, ECO:0000269|PubMed:24162852}. PTM: Acylated by palmitic acid group(s). {ECO:0000250}.; PTM: Heavily glycosylated. {ECO:0000269|PubMed:19349973}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:24162852, ECO:0000269|PubMed:9399579}; Multi-pass membrane protein {ECO:0000269|PubMed:24162852, ECO:0000269|PubMed:9399579}. SUBUNIT: Interacts with GBA. {ECO:0000269|PubMed:18022370, ECO:0000269|PubMed:24162852}. TISSUE SPECIFICITY: Detected in the extracts of brain, heart, lung, liver and kidney. +Q9CZC8 SCRN1_MOUSE Secernin-1 414 46,326 Chain (1); Erroneous initiation (1); Sequence conflict (2) FUNCTION: Regulates exocytosis in mast cells. Increases both the extent of secretion and the sensitivity of mast cells to stimulation with calcium (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +Q8VCA8 SCRN2_MOUSE Secernin-2 425 46,601 Active site (1); Chain (1) +Q6P1D5 SE6L1_MOUSE Seizure 6-like protein (Acupuncture-induced protein 1-L) (Brain-specific receptor-like protein B) (BSRP-B) 963 104,827 Alternative sequence (1); Chain (1); Disulfide bond (13); Domain (8); Glycosylation (11); Sequence conflict (6); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 898 918 Helical. {ECO:0000255}. TOPO_DOM 32 897 Extracellular. {ECO:0000255}.; TOPO_DOM 919 963 Cytoplasmic. {ECO:0000255}. FUNCTION: Candidate tumor suppressor gene. May contribute to specialized endoplasmic reticulum functions in neurons. {ECO:0000250, ECO:0000269|PubMed:16814779}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:16814779}; Single-pass type I membrane protein {ECO:0000305|PubMed:16814779}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:16814779}; Single-pass type I membrane protein {ECO:0000269|PubMed:16814779}. Note=In cerebellar predominantly localized to the endoplasmic reticulum. TISSUE SPECIFICITY: Expressed exclusively in the brain, predomimantly in neurons. Wide expression in the gray matter of the brain with high levels in the olfactory bulb, anterior olfactory nuclei, hippocampal formation and cerebellar cortex. Detected diffusely and weakly in the white matter, such as the corpus callosum and cerebellar medulla. In the cerebellar cortex, intensely expressed in Purkinje cells and granule cells. Detected also in interneurons in the molecular layer. {ECO:0000269|PubMed:16814779}. +Q3UH53 SDK1_MOUSE Protein sidekick-1 2193 240,306 Alternative sequence (2); Beta strand (47); Chain (1); Compositional bias (1); Disulfide bond (5); Domain (19); Erroneous initiation (2); Glycosylation (17); Helix (8); Motif (1); Mutagenesis (1); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (2) TRANSMEM 1992 2012 Helical. {ECO:0000255}. TOPO_DOM ? 1991 Extracellular. {ECO:0000255}.; TOPO_DOM 2013 2193 Cytoplasmic. {ECO:0000255}. FUNCTION: Adhesion molecule that promotes lamina-specific synaptic connections in the retina. Expressed in specific subsets of interneurons and retinal ganglion cells (RGCs) and promotes synaptic connectivity via homophilic interactions. {ECO:0000250|UniProtKB:Q8AV58}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8AV58}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q8AV58}. Cell junction, synapse {ECO:0000269|PubMed:20219992}. SUBUNIT: Homodimer; mediates homophilic interactions to promote cell adhesion (PubMed:15703275). Interacts (via PDZ-binding motif) with MAGI1, MAGI2, DLG2, DLG3 and DLG4 (PubMed:20219992). Isoform 2: Does not mediate homophilic interactions (PubMed:15703275). {ECO:0000269|PubMed:15703275, ECO:0000269|PubMed:20219992}. DOMAIN: the PDZ-binding motif mediates interaction with PDZ domain-containing proteins MAGI1, MAGI2, DLG2, DLG3 and DLG4 and is required for is required for synaptic localization in photoreceptors. {ECO:0000250|UniProtKB:Q6V4S5}.; DOMAIN: Ig-like C2-type domains 1 and 2 mediate homophilic interactions. {ECO:0000269|PubMed:15703275}. TISSUE SPECIFICITY: Expressed by non-overlapping subsets of retinal neurons. Sdk1 and Sdk2 are expressed in non-overlapping subsets of interneurons and retinal ganglion cells (RGCs) that form synapses in distinct inner plexiform layer (IPL) sublaminae (at protein level). {ECO:0000269|PubMed:26287463}. +Q8BU14 SEC62_MOUSE Translocation protein SEC62 (Translocation protein 1) (TP-1) 398 45,581 Chain (1); Modified residue (6); Sequence conflict (1); Topological domain (3); Transmembrane (2) TRANSMEM 197 217 Helical. {ECO:0000255}.; TRANSMEM 235 255 Helical. {ECO:0000255}. TOPO_DOM 1 196 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 218 234 Lumenal. {ECO:0000255}.; TOPO_DOM 256 398 Cytoplasmic. {ECO:0000255}. FUNCTION: Mediates post-translational transport of precursor polypeptides across endoplasmic reticulum (ER). Proposed to act as a targeting receptor for small presecretory proteins containing short and apolar signal peptides. Targets and properly positions newly synthesized presecretory proteins into the SEC61 channel-forming translocon complex, triggering channel opening for polypeptide translocation to the ER lumen. {ECO:0000250|UniProtKB:Q99442}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: The ER translocon complex that consists of channel-forming core components SEC61A1, SEC61B and SEC61G and different auxiliary components such as SEC62 and SEC63. Interacts with SEC61B. {ECO:0000250|UniProtKB:P82009, ECO:0000250|UniProtKB:Q99442}. +Q9DBC0 SELO_MOUSE Selenoprotein O (SelO) 667 74,221 Chain (1); Erroneous termination (2); Modified residue (2); Non-standard residue (1); Sequence conflict (1) FUNCTION: May be a redox-active mitochondrial selenoprotein which interacts with a redox target protein. {ECO:0000250|UniProtKB:Q9BVL4}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9BVL4}. +Q62217 SEM5A_MOUSE Semaphorin-5A (Semaphorin-F) (Sema F) 1077 120,826 Chain (1); Disulfide bond (18); Domain (8); Glycosylation (10); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 972 992 Helical. {ECO:0000255}. TOPO_DOM 22 971 Extracellular. {ECO:0000255}.; TOPO_DOM 993 1077 Cytoplasmic. {ECO:0000255}. FUNCTION: Bifunctional axonal guidance cue regulated by sulfated proteoglycans; attractive effects result from interactions with heparan sulfate proteoglycans (HSPGs), while the inhibitory effects depend on interactions with chondroitin sulfate proteoglycans (CSPGs). Ligand for receptor PLXNB3. In glioma cells, SEMA5A stimulation of PLXNB3 results in the disassembly of F-actin stress fibers, disruption of focal adhesions and cellular collapse as well as inhibition of cell migration and invasion through ARHGDIA-mediated inactivation of RAC1 (By similarity). May promote angiogenesis by increasing endothelial cell proliferation and migration and inhibiting apoptosis. {ECO:0000250, ECO:0000269|PubMed:19850054}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Binds PLXNB3. {ECO:0000250}. TISSUE SPECIFICITY: In adult, detected in liver, brain, kidney, heart, lung and spleen. +O08665 SEM3A_MOUSE Semaphorin-3A (Semaphorin III) (Sema III) (Semaphorin-D) (Sema D) 772 88,813 Beta strand (40); Chain (1); Compositional bias (1); Disulfide bond (6); Domain (2); Glycosylation (3); Helix (9); Sequence conflict (14); Signal peptide (1); Turn (7) FUNCTION: Plays a role in growth cones guidance. May function to pattern sensory projections by selectively repelling axons that normally terminate dorsally. Involved in the development of the olfactory system and in neuronal control of puberty (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Interacts with PXND1. {ECO:0000269|PubMed:15239958}. DOMAIN: Strong binding to neuropilin is mediated by the carboxy third of the protein. +P70274 SEPP1_MOUSE Selenoprotein P (SeP) (Plasma selenoprotein P) 380 42,706 Chain (1); Glycosylation (5); Modified residue (1); Non-standard residue (10); Sequence conflict (8); Signal peptide (1) FUNCTION: Might be responsible for some of the extracellular antioxidant defense properties of selenium or might be involved in the transport of selenium (By similarity). May supply selenium to tissues such as brain and testis. {ECO:0000250}. PTM: Phosphorylation sites are present in the extracellular medium. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18174160}. Note=Passes from plasma into the glomerular filtrate where it is removed by endocytosis mediated by LRP2 in the proximal tubule epithelium. {ECO:0000269|PubMed:18174160}. DOMAIN: The C-terminus is not required for endocytic uptake in the proximal tubule epithelium. {ECO:0000269|PubMed:18174160}. TISSUE SPECIFICITY: In the kidney, expressed in the cortex with no expression observed in the medulla (at protein level) (PubMed:18174160). Expressed by the liver and secreted in plasma (PubMed:9687017). {ECO:0000269|PubMed:18174160, ECO:0000269|PubMed:9687017}. +Q76KF0 SEM6D_MOUSE Semaphorin-6D 1073 119,815 Alternative sequence (4); Chain (1); Disulfide bond (8); Domain (2); Erroneous initiation (1); Glycosylation (5); Modified residue (7); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 663 683 Helical. {ECO:0000255}. TOPO_DOM 21 662 Extracellular. {ECO:0000255}.; TOPO_DOM 684 1073 Cytoplasmic. {ECO:0000255}. FUNCTION: Shows growth cone collapsing activity on dorsal root ganglion (DRG) neurons in vitro. May be a stop signal for the DRG neurons in their target areas, and possibly also for other neurons. May also be involved in the maintenance and remodeling of neuronal connections (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain and lung. {ECO:0000269|PubMed:14715272}. +Q99LS3 SERB_MOUSE Phosphoserine phosphatase (PSP) (PSPase) (EC 3.1.3.3) (O-phosphoserine phosphohydrolase) 225 25,096 Active site (2); Binding site (3); Chain (1); Metal binding (3); Modified residue (1); Region (1) Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 3/3. FUNCTION: Catalyzes the last step in the biosynthesis of serine from carbohydrates. The reaction mechanism proceeds via the formation of a phosphoryl-enzyme intermediates (By similarity). {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +Q9QZI8 SERC1_MOUSE Serine incorporator 1 (Axotomy-induced glyco/Golgi protein 2) (Membrane protein TMS-2) (Tumor differentially expressed protein 1-like) (Tumor differentially expressed protein 2) 453 50,509 Chain (1); Initiator methionine (1); Lipidation (1); Modified residue (4); Topological domain (11); Transmembrane (10) TRANSMEM 40 60 Helical. {ECO:0000255}.; TRANSMEM 89 109 Helical. {ECO:0000255}.; TRANSMEM 124 144 Helical. {ECO:0000255}.; TRANSMEM 152 172 Helical. {ECO:0000255}.; TRANSMEM 198 218 Helical. {ECO:0000255}.; TRANSMEM 232 252 Helical. {ECO:0000255}.; TRANSMEM 260 280 Helical. {ECO:0000255}.; TRANSMEM 310 330 Helical. {ECO:0000255}.; TRANSMEM 388 408 Helical. {ECO:0000255}.; TRANSMEM 427 447 Helical. {ECO:0000255}. TOPO_DOM 2 39 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 61 88 Lumenal. {ECO:0000255}.; TOPO_DOM 110 123 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 145 151 Lumenal. {ECO:0000255}.; TOPO_DOM 173 197 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 219 231 Lumenal. {ECO:0000255}.; TOPO_DOM 253 259 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 281 309 Lumenal. {ECO:0000255}.; TOPO_DOM 331 387 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 409 426 Lumenal. {ECO:0000255}.; TOPO_DOM 448 453 Cytoplasmic. {ECO:0000255}. FUNCTION: Enhances the incorporation of serine into phosphatidylserine and sphingolipids. {ECO:0000250|UniProtKB:Q7TNK0}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q7TNK0}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q7TNK0}. SUBUNIT: Interacts with SPTLC1. {ECO:0000250|UniProtKB:Q7TNK0}. TISSUE SPECIFICITY: Highly expressed in the neuronal populations such as Purkinje cells in the cerebellum, brainstem and spinal motor neurons, locus coeruleus and raphe nuclei. +P19221 THRB_MOUSE Prothrombin (EC 3.4.21.5) (Coagulation factor II) [Cleaved into: Activation peptide fragment 1; Activation peptide fragment 2; Thrombin light chain; Thrombin heavy chain] 618 70,269 Active site (3); Beta strand (14); Chain (3); Disulfide bond (12); Domain (4); Glycosylation (4); Helix (13); Modified residue (10); Mutagenesis (1); Peptide (2); Propeptide (1); Region (1); Signal peptide (1); Site (3); Turn (6) FUNCTION: Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing (By similarity). {ECO:0000250}. PTM: The gamma-carboxyglutamyl residues, which bind calcium ions, result from the carboxylation of glutamyl residues by a microsomal enzyme, the vitamin K-dependent carboxylase. The modified residues are necessary for the calcium-dependent interaction with a negatively charged phospholipid surface, which is essential for the conversion of prothrombin to thrombin. {ECO:0000269|PubMed:2222810}. SUBUNIT: Heterodimer (named alpha-thrombin) of a light and a heavy chain; disulfide-linked. Forms a heterodimer with SERPINA5 (By similarity). {ECO:0000250}. +Q62264 THRSP_MOUSE Thyroid hormone-inducible hepatic protein (Spot 14 protein) (S14) (SPOT14) 150 17,093 Beta strand (1); Chain (1); Helix (5); Modified residue (1) FUNCTION: Plays a role in the regulation of lipogenesis, especially in lactating mammary gland. Important for the biosynthesis of triglycerides with medium-length fatty acid chains. May modulate lipogenesis by interacting with MID1IP1 and preventing its interaction with ACACA. May function as transcriptional coactivator. May modulate the transcription factor activity of THRB (By similarity). {ECO:0000250, ECO:0000269|PubMed:15890771, ECO:0000269|PubMed:20952656}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20952656}. Cytoplasm {ECO:0000269|PubMed:20952656}. SUBUNIT: Homodimer. Heterodimer with MID1IP1. Interacts with THRB and PLAGL1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Mainly expressed in tissues that synthesize triglycerides. {ECO:0000269|PubMed:15890771}. +Q9ES97 RTN3_MOUSE Reticulon-3 964 103,879 Alternative sequence (4); Chain (1); Domain (1); Initiator methionine (1); Intramembrane (3); Modified residue (14); Region (2); Sequence conflict (6); Topological domain (4) INTRAMEM 796 819 Helical. {ECO:0000255}.; INTRAMEM 877 899 Helical. {ECO:0000255}.; INTRAMEM 904 926 Helical. {ECO:0000255}. TOPO_DOM 2 795 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 820 876 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 900 903 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 927 964 Cytoplasmic. {ECO:0000255}. FUNCTION: May be involved in membrane trafficking in the early secretory pathway. Inhibits BACE1 activity and amyloid precursor protein processing. May induce caspase-8 cascade and apoptosis. May favor BCL2 translocation to the mitochondria upon endoplasmic reticulum stress (By similarity). Induces the formation of endoplasmic reticulum tubules (PubMed:24262037). {ECO:0000250|UniProtKB:O95197, ECO:0000269|PubMed:24262037}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15350194}; Multi-pass membrane protein {ECO:0000269|PubMed:15350194}. Golgi apparatus membrane {ECO:0000250|UniProtKB:O95197}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Homodimer. Interacts with RTN4. Isoform 3 interacts with BACE1, BACE2, BCL2 and FADD (By similarity). Interacts with ATL1 and ATL2 (PubMed:19665976). Isoform 3 interacts with TMEM33 (PubMed:25612671). Interacts with ZFYVE27 and with KIF5A in a ZFYVE27-dependent manner (By similarity). {ECO:0000250|UniProtKB:O95197, ECO:0000269|PubMed:19665976, ECO:0000269|PubMed:25612671}. TISSUE SPECIFICITY: Isoform 1, isoform 3, isoform 4 and isoform 5 are expressed in spinal cord. Isoform 1 is present in brain, where it is expressed in the neurons of cerebral cortex, hippocampus, hypothalamus and cerebellum (at protein level). {ECO:0000269|PubMed:15350194, ECO:0000269|PubMed:15946766}. +Q9D9S3 RWD2A_MOUSE RWD domain-containing protein 2A 292 33,916 Chain (1); Domain (1) +P63084 S10A5_MOUSE Protein S100-A5 (Protein S-100D) (S100 calcium-binding protein A5) 93 10,812 Calcium binding (2); Chain (1); Domain (2) FUNCTION: Binds calcium, zinc and copper. One subunit can simultaneously bind 2 calcium ions or 2 copper ions plus 1 zinc ion. Calcium and copper ions compete for the same binding sites (By similarity). {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +P14069 S10A6_MOUSE Protein S100-A6 (5B10) (Calcyclin) (Prolactin receptor-associated protein) (S100 calcium-binding protein A6) 89 10,051 Beta strand (2); Calcium binding (2); Chain (1); Domain (2); Helix (5); Modified residue (4); Sequence conflict (1) FUNCTION: May function as calcium sensor and modulator, contributing to cellular calcium signaling. May function by interacting with other proteins, such as TPR-containing proteins, and indirectly play a role in many physiological processes such as the reorganization of the actin cytoskeleton and in cell motility. Binds 2 calcium ions. Calcium binding is cooperative (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. SUBUNIT: Homodimer; head to tail assembly of 2 subunits. Interacts with CACYBP in a calcium-dependent manner. Interacts with ANXA2 and ANXA11 (via N-terminus). Interacts with SUGT1. Interacts with TP53; has higher affinity for TP53 that is phosphorylated on its N-terminal domain, and lower affinity for TP53 that is phosphorylated on its C-terminal domain. Interacts with tropomyosin. Interacts with FKBP4. Interacts with PPP5C (via TPR repeats); the interaction is calcium-dependent and modulates PPP5C activity (By similarity). {ECO:0000250}. +Q91Y63 S13A3_MOUSE Solute carrier family 13 member 3 (Na(+)/dicarboxylate cotransporter 3) (NaDC-3) (mNaDC3) (Sodium-dependent high-affinity dicarboxylate transporter 2) 600 66,143 Chain (1); Glycosylation (2); Intramembrane (1); Topological domain (13); Transmembrane (11) INTRAMEM 423 443 Helical. {ECO:0000255}. TRANSMEM 17 37 Helical. {ECO:0000255}.; TRANSMEM 56 76 Helical. {ECO:0000255}.; TRANSMEM 83 103 Helical. {ECO:0000255}.; TRANSMEM 138 158 Helical. {ECO:0000255}.; TRANSMEM 230 250 Helical. {ECO:0000255}.; TRANSMEM 279 299 Helical. {ECO:0000255}.; TRANSMEM 337 357 Helical. {ECO:0000255}.; TRANSMEM 373 393 Helical. {ECO:0000255}.; TRANSMEM 462 482 Helical. {ECO:0000255}.; TRANSMEM 506 526 Helical. {ECO:0000255}.; TRANSMEM 547 567 Helical. {ECO:0000255}. TOPO_DOM 1 16 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 38 55 Extracellular. {ECO:0000255}.; TOPO_DOM 77 82 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 104 137 Extracellular. {ECO:0000255}.; TOPO_DOM 159 229 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 251 278 Extracellular. {ECO:0000255}.; TOPO_DOM 300 336 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 358 372 Extracellular. {ECO:0000255}.; TOPO_DOM 394 422 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 444 461 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 483 505 Extracellular. {ECO:0000255}.; TOPO_DOM 527 546 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 568 600 Extracellular. {ECO:0000255}. FUNCTION: High-affinity sodium-dicarboxylate cotransporter that accepts a range of substrates with 4-5 carbon atoms. The stoichiometry is probably 3 Na(+) for 1 divalent succinate. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Highly expressed in kidney, and at much lower levels in brain. +Q8BGF9 S2544_MOUSE Solute carrier family 25 member 44 314 35,339 Chain (1); Repeat (3); Transmembrane (6) TRANSMEM 20 42 Helical; Name=1. {ECO:0000255}.; TRANSMEM 71 90 Helical; Name=2. {ECO:0000255}.; TRANSMEM 113 133 Helical; Name=3. {ECO:0000255}.; TRANSMEM 185 201 Helical; Name=4. {ECO:0000255}.; TRANSMEM 222 239 Helical; Name=5. {ECO:0000255}.; TRANSMEM 278 296 Helical; Name=6. {ECO:0000255}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q80ZD3 S2611_MOUSE Sodium-independent sulfate anion transporter (Solute carrier family 26 member 11) 593 64,109 Alternative sequence (2); Chain (1); Domain (1); Erroneous initiation (1); Sequence conflict (5); Topological domain (12); Transmembrane (11) TRANSMEM 35 55 Helical. {ECO:0000255}.; TRANSMEM 57 77 Helical. {ECO:0000255}.; TRANSMEM 83 100 Helical. {ECO:0000255}.; TRANSMEM 107 127 Helical. {ECO:0000255}.; TRANSMEM 177 197 Helical. {ECO:0000255}.; TRANSMEM 234 254 Helical. {ECO:0000255}.; TRANSMEM 288 308 Helical. {ECO:0000255}.; TRANSMEM 325 345 Helical. {ECO:0000255}.; TRANSMEM 362 382 Helical. {ECO:0000255}.; TRANSMEM 384 404 Helical. {ECO:0000255}.; TRANSMEM 418 438 Helical. {ECO:0000255}. TOPO_DOM 1 34 Extracellular. {ECO:0000255}.; TOPO_DOM 56 56 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 78 82 Extracellular. {ECO:0000255}.; TOPO_DOM 101 106 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 128 176 Extracellular. {ECO:0000255}.; TOPO_DOM 198 233 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 255 287 Extracellular. {ECO:0000255}.; TOPO_DOM 309 324 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 346 361 Extracellular. {ECO:0000255}.; TOPO_DOM 383 383 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 405 417 Extracellular. {ECO:0000255}.; TOPO_DOM 439 593 Cytoplasmic. {ECO:0000255}. FUNCTION: Exhibits sodium-independent sulfate anion transporter activity that may cooperate with SLC26A2 to mediate DIDS-sensitive sulfate uptake into high endothelial venules endothelial cells (HEVEC). {ECO:0000250|UniProtKB:Q86WA9}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q86WA9}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q86WA9}. Lysosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q86WA9}. +Q9EPR4 S23A2_MOUSE Solute carrier family 23 member 2 (Na(+)/L-ascorbic acid transporter 2) (Sodium-dependent vitamin C transporter 2) (SVCT-2) (mSVCT2) (Yolk sac permease-like molecule 2) 648 70,049 Alternative sequence (2); Chain (1); Erroneous gene model prediction (1); Erroneous initiation (2); Glycosylation (2); Intramembrane (1); Modified residue (6); Topological domain (14); Transmembrane (12) INTRAMEM 287 300 Helical. {ECO:0000255}. TRANSMEM 111 131 Helical. {ECO:0000255}.; TRANSMEM 140 160 Helical. {ECO:0000255}.; TRANSMEM 162 182 Helical. {ECO:0000255}.; TRANSMEM 217 237 Helical. {ECO:0000255}.; TRANSMEM 265 282 Helical. {ECO:0000255}.; TRANSMEM 308 328 Helical. {ECO:0000255}.; TRANSMEM 370 390 Helical. {ECO:0000255}.; TRANSMEM 416 436 Helical. {ECO:0000255}.; TRANSMEM 460 480 Helical. {ECO:0000255}.; TRANSMEM 484 504 Helical. {ECO:0000255}.; TRANSMEM 515 535 Helical. {ECO:0000255}.; TRANSMEM 546 566 Helical. {ECO:0000255}. TOPO_DOM 9 110 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 132 139 Extracellular. {ECO:0000255}.; TOPO_DOM 161 161 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 183 216 Extracellular. {ECO:0000255}.; TOPO_DOM 238 264 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 283 286 Extracellular. {ECO:0000255}.; TOPO_DOM 301 307 Extracellular. {ECO:0000255}.; TOPO_DOM 329 369 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 391 415 Extracellular. {ECO:0000255}.; TOPO_DOM 437 459 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 481 483 Extracellular. {ECO:0000255}.; TOPO_DOM 505 514 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 536 545 Extracellular. {ECO:0000255}.; TOPO_DOM 567 648 Cytoplasmic. {ECO:0000255}. FUNCTION: Sodium/ascorbate cotransporter. Mediates electrogenic uptake of vitamin C, with a stoichiometry of 2 Na(+) for each ascorbate (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed in metabolically active and specialized tissues, including high expression in brain and adrenals. Detected in a wide range of tissues. Expression in kidney is almost undetectable. {ECO:0000269|PubMed:17689499}. DISEASE: Note=Elevated expression levels in the adrenals of diabetic mice. {ECO:0000269|PubMed:17689499}. +P58735 S26A1_MOUSE Sulfate anion transporter 1 (SAT-1) (Solute carrier family 26 member 1) 704 75,788 Chain (1); Domain (1); Glycosylation (3); Modified residue (3); Mutagenesis (3); Transmembrane (9) TRANSMEM 68 90 Helical. {ECO:0000255}.; TRANSMEM 94 116 Helical. {ECO:0000255}.; TRANSMEM 185 207 Helical. {ECO:0000255}.; TRANSMEM 260 282 Helical. {ECO:0000255}.; TRANSMEM 295 314 Helical. {ECO:0000255}.; TRANSMEM 347 369 Helical. {ECO:0000255}.; TRANSMEM 382 404 Helical. {ECO:0000255}.; TRANSMEM 417 439 Helical. {ECO:0000255}.; TRANSMEM 477 499 Helical. {ECO:0000255}. FUNCTION: Mediates sulfate transport with high affinity (PubMed:12217875, PubMed:27210743). Mediates oxalate transport (PubMed:12217875). Mediates bicarbonate transport (PubMed:27210743). Does not accept succinate as cosubstrate (By similarity). {ECO:0000250|UniProtKB:P45380, ECO:0000269|PubMed:12217875, ECO:0000269|PubMed:27210743}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27210743}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:P45380}. +Q1LZI2 S35F3_MOUSE Putative thiamine transporter SLC35F3 (Solute carrier family 35 member F3) 421 46,924 Chain (1); Sequence conflict (2); Transmembrane (10) TRANSMEM 66 86 Helical. {ECO:0000255}.; TRANSMEM 98 118 Helical. {ECO:0000255}.; TRANSMEM 149 169 Helical. {ECO:0000255}.; TRANSMEM 179 199 Helical. {ECO:0000255}.; TRANSMEM 208 228 Helical. {ECO:0000255}.; TRANSMEM 232 252 Helical. {ECO:0000255}.; TRANSMEM 266 286 Helical. {ECO:0000255}.; TRANSMEM 305 325 Helical. {ECO:0000255}.; TRANSMEM 326 346 Helical. {ECO:0000255}.; TRANSMEM 352 372 Helical. {ECO:0000255}. FUNCTION: May be a thiamine transporter. {ECO:0000250|UniProtKB:Q8IY50}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q3U1J0 S38A5_MOUSE Sodium-coupled neutral amino acid transporter 5 (Solute carrier family 38 member 5) (System N transporter 2) 479 52,617 Alternative sequence (1); Chain (1); Disulfide bond (1); Erroneous initiation (1); Glycosylation (1); Sequence conflict (2); Topological domain (12); Transmembrane (11) TRANSMEM 62 84 Helical. {ECO:0000255}.; TRANSMEM 98 118 Helical. {ECO:0000255}.; TRANSMEM 136 156 Helical. {ECO:0000255}.; TRANSMEM 177 197 Helical. {ECO:0000255}.; TRANSMEM 203 223 Helical. {ECO:0000255}.; TRANSMEM 265 285 Helical. {ECO:0000255}.; TRANSMEM 303 323 Helical. {ECO:0000255}.; TRANSMEM 342 362 Helical. {ECO:0000255}.; TRANSMEM 384 404 Helical. {ECO:0000255}.; TRANSMEM 407 427 Helical. {ECO:0000255}.; TRANSMEM 447 467 Helical. {ECO:0000255}. TOPO_DOM 1 61 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 85 97 Extracellular. {ECO:0000255}.; TOPO_DOM 119 135 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 157 176 Extracellular. {ECO:0000255}.; TOPO_DOM 198 202 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 224 264 Extracellular. {ECO:0000255}.; TOPO_DOM 286 302 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 324 341 Extracellular. {ECO:0000255}.; TOPO_DOM 363 383 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 405 406 Extracellular. {ECO:0000255}.; TOPO_DOM 428 446 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 468 479 Extracellular. {ECO:0000255}. FUNCTION: Functions as a sodium-dependent amino acid transporter which countertransport protons. Mediates the saturable, pH-sensitive, and electrogenic cotransport of several neutral amino acids including glycine, asparagine, alanine, serine, glutamine and histidine with sodium (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q9D8K8 S2539_MOUSE Solute carrier family 25 member 39 359 39,221 Chain (1); Repeat (3); Transmembrane (6) TRANSMEM 15 35 Helical; Name=1. {ECO:0000255}.; TRANSMEM 122 142 Helical; Name=2. {ECO:0000255}.; TRANSMEM 165 185 Helical; Name=3. {ECO:0000255}.; TRANSMEM 215 235 Helical; Name=4. {ECO:0000255}.; TRANSMEM 256 276 Helical; Name=5. {ECO:0000255}.; TRANSMEM 318 338 Helical; Name=6. {ECO:0000255}. FUNCTION: Required for normal heme biosynthesis. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Abundant expression in bone marrow, spleen, testis and kidney. {ECO:0000269|PubMed:19656490}. +Q921R7 S35A5_MOUSE Probable UDP-sugar transporter protein SLC35A5 (Solute carrier family 35 member A5) 437 50,115 Chain (1); Glycosylation (1); Modified residue (3); Sequence conflict (1); Transmembrane (10) TRANSMEM 22 42 Helical. {ECO:0000255}.; TRANSMEM 66 86 Helical. {ECO:0000255}.; TRANSMEM 107 129 Helical. {ECO:0000255}.; TRANSMEM 133 155 Helical. {ECO:0000255}.; TRANSMEM 159 179 Helical. {ECO:0000255}.; TRANSMEM 242 262 Helical. {ECO:0000255}.; TRANSMEM 277 297 Helical. {ECO:0000255}.; TRANSMEM 317 337 Helical. {ECO:0000255}.; TRANSMEM 344 364 Helical. {ECO:0000255}.; TRANSMEM 368 388 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9CTN5 S6OS1_MOUSE Protein SIX6OS1 (Six6 opposite strand transcript 1 homolog) 574 66,867 Alternative sequence (2); Chain (1); Compositional bias (1); Modified residue (2) FUNCTION: Meiotic protein that localizes to the central element of the synaptonemal complex and is required for chromosome synapsis during meiotic recombination (PubMed:27796301). Required for the appropriate processing of intermediate recombination nodules before crossover formation (PubMed:27796301). {ECO:0000269|PubMed:27796301}. SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:27796301}. Note=Component of the central element of the synaptonemal complex (PubMed:27796301). In spermatocytes, detected from zygonema to pachynema and localizes along synapsed lateral elements (PubMed:27796301). Loading to the central element of the synaptonemal complex is dependent on the assembly of the tripartite synaptonemal complex structure that occurs upon synapsis between homologous chromosomes (PubMed:27796301). {ECO:0000269|PubMed:27796301}. SUBUNIT: Interacts with SYCE1 (PubMed:27796301). {ECO:0000269|PubMed:27796301}. TISSUE SPECIFICITY: Most abundantly expressed in testis (PubMed:27796301). Also expressed in retina and skeletal muscle (PubMed:15703187). {ECO:0000269|PubMed:15703187, ECO:0000269|PubMed:27796301}. +Q7TPM5 SACA9_MOUSE Sperm acrosome-associated protein 9 (Acrosome and sperm tail protein) (MAST) 168 19,482 Alternative sequence (2); Chain (1); Compositional bias (1); Sequence conflict (1); Site (2) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24256100}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:24256100}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:27914912}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:27914912}. Nucleus {ECO:0000250|UniProtKB:Q4V8P4}. Note=In caudal sperms localizes onto sperm head. Is also present on midpiece and principle piece of sperm tails. Acrosome and sperm tail localization is regulated by Y-chromosome. {ECO:0000269|PubMed:24256100}. SUBUNIT: Interacts with CABP1 AND CALR (PubMed:24256100). Interacts with INCA1 (By similarity). {ECO:0000250|UniProtKB:Q4V8P4, ECO:0000269|PubMed:24256100}. TISSUE SPECIFICITY: Expressed in sperm (at protein level) (Ref.4). Expressed from almost all the cell types of testis, with abundant expression in round and elongated spermatids (at protein level) (PubMed:24256100). Predominantly expressed in tissues containing motile cilia (PubMed:27914912). {ECO:0000269|PubMed:24256100, ECO:0000269|PubMed:27914912, ECO:0000269|Ref.4}. +Q80YR5 SAFB2_MOUSE Scaffold attachment factor B2 (SAF-B2) 991 111,838 Chain (1); Compositional bias (4); Cross-link (20); Domain (2); Erroneous initiation (1); Initiator methionine (1); Modified residue (8); Motif (1); Sequence conflict (1) FUNCTION: Binds to scaffold/matrix attachment region (S/MAR) DNA. Can function as an estrogen receptor corepressor and can also inhibit cell proliferation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Interacts with SAFB/SAFB1 and SCAM1. Interacts with SRPK1 and inhibits its activity. {ECO:0000250}. +P05366 SAA1_MOUSE Serum amyloid A-1 protein 122 13,770 Chain (1); Region (1); Signal peptide (1) FUNCTION: Major acute phase protein. {ECO:0000269|PubMed:9518179}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9518179}. SUBUNIT: Homohexamer; dimer of trimers. Can form amyloid fibrils after partial proteolysis; the native, undenatured protein does not form amyloid fibrils (in vitro). Apolipoprotein of the HDL complex. Binds to heparin (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Detected in blood plasma (at protein level). Detected in liver. {ECO:0000269|PubMed:3857624, ECO:0000269|PubMed:9518179}. +Q68FL4 SAHH3_MOUSE Putative adenosylhomocysteinase 3 (AdoHcyase 3) (EC 3.3.1.1) (Long-IRBIT) (S-adenosyl-L-homocysteine hydrolase 3) (S-adenosylhomocysteine hydrolase-like protein 2) 613 66,899 Alternative sequence (1); Binding site (9); Chain (1); Initiator methionine (1); Modified residue (6); Nucleotide binding (3); Region (1); Sequence conflict (1) Amino-acid biosynthesis; L-homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1. FUNCTION: May regulate the electrogenic sodium/bicarbonate cotransporter SLC4A4 activity and Mg(2+)-sensitivity. On the contrary of its homolog AHCYL1, does not regulate ITPR1 sensitivity to inositol 1,4,5-trisphosphate. {ECO:0000250|UniProtKB:A6QLP2, ECO:0000250|UniProtKB:Q96HN2}. PTM: Phosphorylated during neuronal differentiation at the LISN domain. {ECO:0000269|PubMed:19220705}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A6QLP2, ECO:0000269|PubMed:19220705}. Microsome {ECO:0000269|PubMed:19220705}. Note=Associates with membranes when phosphorylated, probably through interaction with ITPR1. {ECO:0000269|PubMed:19220705}. SUBUNIT: Homotetramer. Forms heteromultimers with AHCYL1 (via the C-terminal region). Interacts with ITPR1; with lower affinity than AHCYL1 and maybe via ITPR1. Interacts with SLC4A4. {ECO:0000250|UniProtKB:A6QLP2, ECO:0000250|UniProtKB:Q96HN2}. TISSUE SPECIFICITY: Highly expressed in cerebrum, cerebellum and kidney. Also expressed in thymus, spleen, testis, ovary and, at lower, levels in lung and liver (at protein level). In cerebellum, expressed in interneurons. {ECO:0000269|PubMed:19220705}. +Q9JMA9 S6A14_MOUSE Sodium- and chloride-dependent neutral and basic amino acid transporter B(0+) (Amino acid transporter ATB0+) (Colonic system B0+ amino acid transporter CATB0+) (Solute carrier family 6 member 14) 638 71,456 Chain (1); Glycosylation (7); Sequence conflict (7); Topological domain (3); Transmembrane (12) TRANSMEM 45 65 Helical; Name=1. {ECO:0000255}.; TRANSMEM 72 92 Helical; Name=2. {ECO:0000255}.; TRANSMEM 110 130 Helical; Name=3. {ECO:0000255}.; TRANSMEM 231 251 Helical; Name=4. {ECO:0000255}.; TRANSMEM 257 277 Helical; Name=5. {ECO:0000255}.; TRANSMEM 311 331 Helical; Name=6. {ECO:0000255}.; TRANSMEM 344 364 Helical; Name=7. {ECO:0000255}.; TRANSMEM 395 415 Helical; Name=8. {ECO:0000255}.; TRANSMEM 453 473 Helical; Name=9. {ECO:0000255}.; TRANSMEM 476 496 Helical; Name=10. {ECO:0000255}.; TRANSMEM 524 544 Helical; Name=11. {ECO:0000255}.; TRANSMEM 559 579 Helical; Name=12. {ECO:0000255}. TOPO_DOM 1 44 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 131 230 Extracellular. {ECO:0000255}.; TOPO_DOM 580 638 Cytoplasmic. {ECO:0000255}. FUNCTION: Mediates the uptake of a broad range of neutral and cationic amino acids (with the exception of proline) in a Na(+)/Cl(-)-dependent manner. {ECO:0000269|PubMed:11306607, ECO:0000269|PubMed:11447016}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed in the distal region of the intestinal tract: cecum and colon. {ECO:0000269|PubMed:11306607, ECO:0000269|PubMed:11447016}. +Q8C5W3 TBCEL_MOUSE Tubulin-specific chaperone cofactor E-like protein (Leucine-rich repeat-containing protein 35) 424 48,032 Alternative sequence (1); Chain (1); Coiled coil (1); Domain (2); Modified residue (2); Repeat (7); Sequence conflict (1) FUNCTION: Acts as a regulator of tubulin stability. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. +Q9DA48 SACA1_MOUSE Sperm acrosome membrane-associated protein 1 305 33,343 Chain (1); Compositional bias (1); Glycosylation (1); Modified residue (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 232 252 Helical. {ECO:0000255}. TOPO_DOM 29 231 Extracellular. {ECO:0000255}.; TOPO_DOM 253 305 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a role in acrosome expansion and establishment of normal sperm morphology during spermatogenesis. Important for male fertility. {ECO:0000269|PubMed:22949614}. PTM: N-glycosylated. {ECO:0000269|PubMed:22949614}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome inner membrane {ECO:0000269|PubMed:22949614}; Single-pass type I membrane protein {ECO:0000305}. Note=Primarily found in the equatorial segment of the acrosome (PubMed:22949614). The tyrosine phosphorylated protein localizes to a smaller region within the equatorial segment (By similarity). Also expressed weakly in the principal segment (By similarity). {ECO:0000250|UniProtKB:D5K8A9, ECO:0000250|UniProtKB:Q9HBV2}. TISSUE SPECIFICITY: Testis specific (at protein level). {ECO:0000269|PubMed:22949614}. +Q3U0J8 TBD2B_MOUSE TBC1 domain family member 2B 965 109,950 Chain (1); Coiled coil (1); Domain (2); Erroneous initiation (1); Modified residue (4); Sequence conflict (2) FUNCTION: May act as a GTPase-activating protein. {ECO:0000250}. +O55128 SAP18_MOUSE Histone deacetylase complex subunit SAP18 (18 kDa Sin3-associated polypeptide) (Sin3-associated polypeptide p18) 153 17,595 Beta strand (5); Chain (1); Cross-link (1); Helix (8); Initiator methionine (1); Modified residue (1); Mutagenesis (1); Region (1); Turn (1) FUNCTION: Component of the SIN3-repressing complex. Enhances the ability of SIN3-HDAC1-mediated transcriptional repression. When tethered to the promoter, it can direct the formation of a repressive complex to core histone proteins. Auxiliary component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Component of the ASAP and PSAP complexes which bind RNA in a sequence-independent manner and are proposed to be recruited to the EJC prior to or during the splicing process and to regulate specific excision of introns in specific transcription subsets. The ASAP complex can inhibit mRNA processing during in vitro splicing reactions. The ASAP complex promotes apoptosis and is disassembled after induction of apoptosis. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits the formation of proapoptotic isoforms such as Bcl-X(S); the activity is different from the established EJC assembly and function (By similarity). {ECO:0000250, ECO:0000269|PubMed:22388736}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O00422}. Cytoplasm {ECO:0000250|UniProtKB:O00422}. Nucleus speckle {ECO:0000250|UniProtKB:O00422}. Note=Shuttles between the nucleus and the cytoplasm (By similarity). Colocalizes with ACIN1 and SRSF2 in nuclear speckles (By similarity). {ECO:0000250|UniProtKB:O00422}. SUBUNIT: Found in a mRNA splicing-dependent exon junction complex (EJC). Component of the heterotrimeric ASAP (apoptosis- and splicing-associated protein) and PSAP complexes consisting of RNPS1, SAP18 and either ACIN1 or PNN, respectively; the ASAP and PSAP complexes probably are formed mutually exclusive. For the ASAP complex, the association of SAP18 seems to require a preformed RNPS1:ACIN1 complex. Forms a complex with SIN3A and HDAC1. Interacts with SUFU. {ECO:0000269|PubMed:22388736}. TISSUE SPECIFICITY: Expressed in all tissues tested; highest levels in the brain, kidney and muscle; lowest levels in lung spleen, liver, intestine and testis, and moderate levels in salivary gland and heart. {ECO:0000269|PubMed:9511770}. +Q60648 SAP3_MOUSE Ganglioside GM2 activator (Cerebroside sulfate activator protein) (GM2-AP) (Sphingolipid activator protein 3) (SAP-3) 193 20,824 Beta strand (9); Chain (1); Disulfide bond (4); Glycosylation (1); Helix (2); Mutagenesis (1); Sequence conflict (1); Signal peptide (1); Turn (1) FUNCTION: Binds gangliosides and stimulates ganglioside GM2 degradation. It stimulates only the breakdown of ganglioside GM2 and glycolipid GA2 by beta-hexosaminidase A. It extracts single GM2 molecules from membranes and presents them in soluble form to beta-hexosaminidase A for cleavage of N-acetyl-D-galactosamine and conversion to GM3. The large binding pocket can accommodate several single chain phospholipids and fatty acids, GM2A also exhibits some calcium-independent phospholipase activity. {ECO:0000269|PubMed:16216074}. SUBCELLULAR LOCATION: Lysosome. TISSUE SPECIFICITY: Widely expressed. Most abundant in kidney and testis. +Q0VE29 SAM12_MOUSE Sterile alpha motif domain-containing protein 12 (SAM domain-containing protein 12) 161 18,245 Chain (1); Domain (1) +Q60710 SAMH1_MOUSE Deoxynucleoside triphosphate triphosphohydrolase SAMHD1 (dNTPase) (EC 3.1.5.-) (Interferon-gamma-inducible protein Mg11) (SAM domain and HD domain-containing protein 1) (mSAMHD1) 658 75,893 Active site (1); Alternative sequence (1); Beta strand (10); Binding site (15); Chain (1); Cross-link (1); Domain (2); Erroneous initiation (6); Frameshift (1); Helix (34); Metal binding (4); Modified residue (7); Mutagenesis (5); Nucleotide binding (2); Region (2); Sequence conflict (2); Turn (6) FUNCTION: Isoform 1: Protein that acts both as a host restriction factor involved in defense response to virus and as a regulator of DNA end resection at stalled replication forks (By similarity). Has deoxynucleoside triphosphate (dNTPase) activity, which is required to restrict infection by viruses: dNTPase activity reduces cellular dNTP levels to levels too low for retroviral reverse transcription to occur, blocking early-stage virus replication in dendritic and other myeloid cells (PubMed:23972988, PubMed:23872947, PubMed:26667483, PubMed:29379009). Likewise, suppresses LINE-1 retrotransposon activity (PubMed:26667483). In addition to virus restriction, dNTPase activity acts as a regulator of DNA precursor pools by regulating dNTP pools (By similarity). Phosphorylation at Thr-634 acts as a switch to control dNTPase-dependent and -independent functions: it inhibits dNTPase activity and ability to restrict infection by viruses, while it promotes DNA end resection at stalled replication forks (By similarity). Functions during S phase at stalled DNA replication forks to promote the resection of gapped or reversed forks: acts by stimulating the exonuclease activity of MRE11, activating the ATR-CHK1 pathway and allowing the forks to restart replication (By similarity). Its ability to promote degradation of nascent DNA at stalled replication forks is required to prevent induction of type I interferons, thereby preventing chronic inflammation (By similarity). Ability to promote DNA end resection at stalled replication forks is independent of dNTPase activity (By similarity). Enhances immunoglobulin hypermutation in B-lymphocytes by promoting transversion mutation (PubMed:29669924). {ECO:0000250|UniProtKB:Q9Y3Z3, ECO:0000269|PubMed:23872947, ECO:0000269|PubMed:23972988, ECO:0000269|PubMed:26667483, ECO:0000269|PubMed:29379009, ECO:0000269|PubMed:29669924}. PTM: Isoform 1: Phosphorylation at Thr-634 by CDK1 acts as a switch to control deoxynucleoside triphosphate (dNTPase)-dependent and -independent functions (PubMed:26667483) (By similarity). Phosphorylation at Thr-634 takes place in cycling cells: it reduces the stability of the homotetramer, impairing the dNTPase activity and subsequent ability to restrict infection by viruses (Probable). It also inhibits ability to suppress LINE-1 retrotransposon activity (PubMed:26667483). In contrast, phosphorylation at Thr-634 promotes DNA end resection at stalled replication forks in response to DNA damage (By similarity). {ECO:0000250|UniProtKB:Q9Y3Z3, ECO:0000269|PubMed:26667483, ECO:0000305|PubMed:26667483}.; PTM: Isoform 2: Not phosphorylated by CDK1 at the C-terminus. {ECO:0000305}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y3Z3}. Chromosome {ECO:0000250|UniProtKB:Q9Y3Z3}. Note=Localizes to sites of DNA double-strand breaks in response to DNA damage. {ECO:0000250|UniProtKB:Q9Y3Z3}. SUBUNIT: Homodimer; in absence of GTP and dNTP (By similarity). Homotetramer; in GTP- and dNTP-bound form (PubMed:29379009). Interacts with MRE11; leading to stimulate the exonuclease activity of MRE11 (By similarity). Interacts with RBBP8/CtIP (By similarity). {ECO:0000250|UniProtKB:Q9Y3Z3, ECO:0000269|PubMed:29379009}. DOMAIN: In mouse, the SAM domain is required for deoxynucleoside triphosphate (dNTPase) activity and ability to restrict infection by viruses. It acts by capping allosteric sites. {ECO:0000269|PubMed:29379009}. +Q921P9 TCAL1_MOUSE Transcription elongation factor A protein-like 1 (TCEA-like protein 1) (Transcription elongation factor S-II protein-like 1) 165 19,312 Chain (1) FUNCTION: May be involved in transcriptional regulation. Modulates various viral and cellular promoters in a promoter context-dependent manner. Does not bind DNA directly (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +Q8QZX0 SBK1_MOUSE Serine/threonine-protein kinase SBK1 (EC 2.7.11.1) (SH3-binding kinase 1) 417 45,696 Active site (1); Binding site (1); Chain (1); Compositional bias (1); Domain (1); Nucleotide binding (1) FUNCTION: May be involved in signal-transduction pathways related to the control of brain development. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +P0C5K1 SBK2_MOUSE Serine/threonine-protein kinase SBK2 (EC 2.7.11.1) (SH3-binding domain kinase family member 2) (Sugen kinase 69) (SgK069) 362 39,699 Active site (1); Binding site (1); Chain (1); Domain (1); Nucleotide binding (1) +Q8VDT1 SC5A9_MOUSE Sodium/glucose cotransporter 4 (Na(+)/glucose cotransporter 4) (mSGLT4) (Solute carrier family 5 member 9) 685 75,065 Chain (1); Glycosylation (1); Sequence conflict (4); Topological domain (14); Transmembrane (14) TRANSMEM 33 53 Helical. {ECO:0000255}.; TRANSMEM 72 94 Helical. {ECO:0000255}.; TRANSMEM 111 131 Helical. {ECO:0000255}.; TRANSMEM 154 174 Helical. {ECO:0000255}.; TRANSMEM 187 207 Helical. {ECO:0000255}.; TRANSMEM 214 234 Helical. {ECO:0000255}.; TRANSMEM 272 292 Helical. {ECO:0000255}.; TRANSMEM 314 334 Helical. {ECO:0000255}.; TRANSMEM 380 402 Helical. {ECO:0000255}.; TRANSMEM 424 444 Helical. {ECO:0000255}.; TRANSMEM 456 476 Helical. {ECO:0000255}.; TRANSMEM 484 504 Helical. {ECO:0000255}.; TRANSMEM 527 547 Helical. {ECO:0000255}.; TRANSMEM 665 685 Helical. {ECO:0000255}. TOPO_DOM 1 32 Extracellular. {ECO:0000255}.; TOPO_DOM 54 71 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 95 110 Extracellular. {ECO:0000255}.; TOPO_DOM 132 153 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 175 186 Extracellular. {ECO:0000255}.; TOPO_DOM 208 213 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 235 271 Extracellular. {ECO:0000255}.; TOPO_DOM 293 313 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 335 379 Extracellular. {ECO:0000255}.; TOPO_DOM 403 423 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 445 455 Extracellular. {ECO:0000255}.; TOPO_DOM 477 483 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 505 526 Extracellular. {ECO:0000255}.; TOPO_DOM 548 664 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in sodium-dependent transport of D-mannose, D-glucose and D-fructose. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +P56842 TCLB3_MOUSE Protein TCL1B3 122 14,170 Chain (1) +O88822 SC5D_MOUSE Lathosterol oxidase (EC 1.14.19.20) (C-5 sterol desaturase) (Delta(7)-sterol 5-desaturase) (Delta(7)-sterol C5(6)-desaturase) (Lathosterol 5-desaturase) (Sterol-C5-desaturase) 299 35,062 Chain (1); Domain (1); Modified residue (1); Motif (3); Sequence conflict (2); Transmembrane (4) TRANSMEM 32 52 Helical. {ECO:0000255}.; TRANSMEM 79 99 Helical. {ECO:0000255}.; TRANSMEM 117 137 Helical. {ECO:0000255}.; TRANSMEM 186 206 Helical. {ECO:0000255}. FUNCTION: Catalyzes a dehydrogenation to introduce C5-6 double bond into lathosterol. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. DOMAIN: The histidine box domains may contain the active site and/or be involved in metal ion binding. +Q5U4D8 SC5A6_MOUSE Sodium-dependent multivitamin transporter (Na(+)-dependent multivitamin transporter) (Solute carrier family 5 member 6) 634 68,511 Chain (1); Glycosylation (2); Sequence conflict (1); Transmembrane (13) TRANSMEM 23 43 Helical. {ECO:0000255}.; TRANSMEM 65 85 Helical. {ECO:0000255}.; TRANSMEM 100 120 Helical. {ECO:0000255}.; TRANSMEM 142 162 Helical. {ECO:0000255}.; TRANSMEM 175 195 Helical. {ECO:0000255}.; TRANSMEM 207 227 Helical. {ECO:0000255}.; TRANSMEM 255 275 Helical. {ECO:0000255}.; TRANSMEM 295 315 Helical. {ECO:0000255}.; TRANSMEM 350 370 Helical. {ECO:0000255}.; TRANSMEM 403 423 Helical. {ECO:0000255}.; TRANSMEM 427 447 Helical. {ECO:0000255}.; TRANSMEM 455 475 Helical. {ECO:0000255}.; TRANSMEM 526 546 Helical. {ECO:0000255}. FUNCTION: Transports pantothenate, biotin and lipoate in the presence of sodium. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. +Q8BH47 SC22A_MOUSE Vesicle-trafficking protein SEC22a (SEC22 vesicle-trafficking protein homolog A) (SEC22 vesicle-trafficking protein-like 2) 307 35,025 Chain (1); Domain (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (3); Topological domain (5); Transmembrane (4) TRANSMEM 188 208 Helical. {ECO:0000255}.; TRANSMEM 227 247 Helical. {ECO:0000255}.; TRANSMEM 254 271 Helical. {ECO:0000255}.; TRANSMEM 275 295 Helical. {ECO:0000255}. TOPO_DOM 2 187 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 209 226 Lumenal. {ECO:0000255}.; TOPO_DOM 248 253 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 272 274 Lumenal. {ECO:0000255}.; TOPO_DOM 296 307 Cytoplasmic. {ECO:0000255}. FUNCTION: May be involved in vesicle transport between the ER and the Golgi complex. {ECO:0000250|UniProtKB:Q642F4}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q8BRF7 SCFD1_MOUSE Sec1 family domain-containing protein 1 (Syntaxin-binding protein 1-like 2) 639 72,323 Alternative sequence (4); Chain (1); Erroneous initiation (1); Modified residue (3); Sequence conflict (1) FUNCTION: Plays a role in SNARE-pin assembly and Golgi-to-ER retrograde transport via its interaction with COG4. Involved in vesicular transport between the endoplasmic reticulum and the Golgi (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Golgi apparatus, Golgi stack membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. SUBUNIT: Interacts with STX17. Interacts with STX5A. Interacts with the COG complex via COG4 (By similarity). {ECO:0000250}. +P47867 SCG3_MOUSE Secretogranin-3 (Secretogranin III) (SgIII) 471 53,326 Alternative sequence (1); Chain (1); Modified residue (2); Signal peptide (1) SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:12388744}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Secreted {ECO:0000269|PubMed:12388744}. Note=Associated with the secretory granule membrane through direct binding to cholesterol-enriched lipid rafts in intragranular conditions. In neuroblastoma cells, colocalizes with PMCH, NPY, POMC and orexin/HCRT in secretory granules. SUBUNIT: Interacts with CHGA; this interaction is optimal in conditions mimicking the lumenal milieu of the trans-Golgi network, i.e. pH 5.5 and 10 mM Ca(+2). {ECO:0000269|PubMed:12388744}. TISSUE SPECIFICITY: Expressed in various brain areas, with highest levels in the arcuate nucleus and the lateral hypothalamic area, as well as the paraventricular nucleus and the ventromedial hypothalamus (at protein level). {ECO:0000269|PubMed:17200173}. +Q3UU41 SCIMP_MOUSE SLP adapter and CSK-interacting membrane protein 150 17,140 Chain (1); Compositional bias (1); Erroneous initiation (2); Lipidation (2); Modified residue (3); Transmembrane (1) TRANSMEM 8 28 Helical. {ECO:0000255}. FUNCTION: Lipid tetraspanin-associated transmembrane adapter/mediator involved in major histocompatibility complex class II (MHC-II) signaling transduction. Required in generating the calcium response and enhancing ERK activity upon MHC-II stimulation (By similarity). {ECO:0000250}. PTM: Phosphorylated by tyrosine-protein kinases LYN and SRC (By similarity). Phosphorylation occurs on tyrosine residues upon MHC-II stimulation. {ECO:0000250, ECO:0000269|PubMed:21930792}.; PTM: Palmitoylated. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Note=Together with MHC-II, associates with lipid-enriched microdomains called tetraspanin-enriched microdomains (TEMs). Rapidly translocates into immunological synapse (IS) at cell-cell contacts between antigen-presenting cells (APCs) and T-cells (By similarity). Colocalized with tetraspanins CD37, CD53, and CD81 at the uropod. Present at regions of cell-cell contacts but also at the leading edge of migrating cells. {ECO:0000250}. SUBUNIT: Interacts with CD37, CD53 and CD81. Interacts (via prolin-rich region) with LYN (via SH3 domain). Interacts with CSK (via SH2 domain) (By similarity). Interacts with BLNK and GRB2. {ECO:0000250, ECO:0000269|PubMed:21930792}. TISSUE SPECIFICITY: Expressed in peripheral blood leukocytes (PBLs) (at protein level). Strongly expressed in the spleen and lymph nodes and weakly in other tissues of the immune system, including bone marrow, peripheral blood leukocytes (PBLs) and thymus. Not detected in the majority of nonimmune tissues, with the exception of lung. Expressed in antigen-presenting cells. {ECO:0000269|PubMed:21930792}. +P16014 SCG1_MOUSE Secretogranin-1 (Chromogranin-B) (CgB) (Secretogranin I) (SgI) [Cleaved into: CCB peptide; PE-11] 677 77,969 Chain (1); Disulfide bond (1); Glycosylation (1); Modified residue (24); Peptide (2); Sequence conflict (1); Signal peptide (1) FUNCTION: Secretogranin-1 is a neuroendocrine secretory granule protein, which may be the precursor for other biologically active peptides. SUBCELLULAR LOCATION: Secreted. Note=Neuroendocrine and endocrine secretory granules. +Q7M729 SCN4B_MOUSE Sodium channel subunit beta-4 228 25,192 Beta strand (12); Chain (1); Disulfide bond (2); Domain (1); Glycosylation (4); Helix (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 162 182 Helical. {ECO:0000255}. TOPO_DOM 31 161 Extracellular. {ECO:0000255}.; TOPO_DOM 183 228 Cytoplasmic. {ECO:0000255}. FUNCTION: Modulates channel gating kinetics. Causes negative shifts in the voltage dependence of activation of certain alpha sodium channels, but does not affect the voltage dependence of inactivation. Modulates the susceptibility of the sodium channel to inhibition by toxic peptides from spider, scorpion, wasp and sea anemone venom (By similarity). {ECO:0000250}. PTM: Contains an interchain disulfide bond with SCN2A. {ECO:0000250}.; PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Component of the voltage-sensitive sodium channel complex that consists of an ion-conducting pore-forming alpha subunit and one or more regulatory beta subunits. Heterooligomer with SCN2A; disulfide-linked (By similarity). {ECO:0000250}. +Q80VG1 SCML4_MOUSE Sex comb on midleg-like protein 4 408 44,445 Alternative sequence (1); Chain (1); Domain (1); Modified residue (2); Sequence conflict (1) FUNCTION: Putative Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q8VCL2 SCO2_MOUSE Protein SCO2 homolog, mitochondrial 255 28,944 Chain (1); Disulfide bond (1); Domain (1); Metal binding (3); Topological domain (2); Transit peptide (1); Transmembrane (1) TRANSMEM 50 67 Helical. {ECO:0000255}. TOPO_DOM 42 49 Mitochondrial matrix. {ECO:0000250|UniProtKB:O43819}.; TOPO_DOM 68 255 Mitochondrial intermembrane. {ECO:0000250|UniProtKB:O43819}. FUNCTION: Copper metallochaperone essential for the synthesis and maturation of cytochrome c oxidase subunit II (MT-CO2/COX2). Involved in transporting copper to the Cu(A) site on MT-CO2/COX2. Also acts as a thiol-disulfide oxidoreductase to regulate the redox state of the cysteines in SCO1 during maturation of MT-CO2/COX2. {ECO:0000250|UniProtKB:O43819}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:O43819}; Single-pass membrane protein {ECO:0000255}. SUBUNIT: Homodimer. Interacts with COA6. Found in a complex with TMEM177, COX20, COA6, MT-CO2/COX2, COX18 and SCO1. Interacts with TMEM177 in a COX20-dependent manner. Interacts with COX20 in a MT-CO2/COX2- and COX18-dependent manner. Interacts with COX16. {ECO:0000250|UniProtKB:O43819}. TISSUE SPECIFICITY: Expressed in retina, retinal pigment epithelium, and sclera. {ECO:0000269|PubMed:23643385}. +Q78YZ6 SCOC_MOUSE Short coiled-coil protein 125 14,155 Alternative sequence (2); Chain (1); Coiled coil (1); Sequence conflict (2) FUNCTION: Positive regulator of amino acid starvation-induced autophagy. {ECO:0000250|UniProtKB:Q9UIL1}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9UIL1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9UIL1}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9UIL1}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q9UIL1}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9UIL1}. SUBUNIT: Homodimer. Interacts with ARL1, ARL2 and ARL3. Directly interacts with FEZ1 and UVRAG. The interaction with UVRAG is reduced by amino acid starvation, but the complex is stabilized in the presence of FEZ1. Interacts with NRBF2. {ECO:0000250|UniProtKB:Q9UIL1}. +Q62205 SCN9A_MOUSE Sodium channel protein type 9 subunit alpha (Peripheral sodium channel 1) (PN1) (Sodium channel protein type IX subunit alpha) (Voltage-gated sodium channel subunit alpha Nav1.7) 1984 225,813 Chain (1); Coiled coil (2); Disulfide bond (4); Domain (1); Intramembrane (4); Modified residue (1); Repeat (4); Topological domain (29); Transmembrane (24) INTRAMEM 347 371 Pore-forming. {ECO:0000250|UniProtKB:D0E0C2}.; INTRAMEM 912 932 Pore-forming. {ECO:0000250|UniProtKB:D0E0C2}.; INTRAMEM 1391 1412 Pore-forming. {ECO:0000250|UniProtKB:D0E0C2}.; INTRAMEM 1682 1704 Pore-forming. {ECO:0000250|UniProtKB:D0E0C2}. TRANSMEM 127 145 Helical; Name=S1 of repeat I. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 153 173 Helical; Name=S2 of repeat I. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 188 205 Helical; Name=S3 of repeat I. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 212 228 Helical; Name=S4 of repeat I. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 248 267 Helical; Name=S5 of repeat I. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 379 399 Helical; Name=S6 of repeat I. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 744 762 Helical; Name=S1 of repeat II. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 774 793 Helical; Name=S2 of repeat II. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 808 827 Helical; Name=S3 of repeat II. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 830 847 Helical; Name=S4 of repeat II. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 864 882 Helical; Name=S5 of repeat II. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 946 966 Helical; Name=S6 of repeat II. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1192 1209 Helical; Name=S1 of repeat III. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1223 1241 Helical; Name=S2 of repeat III. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1256 1274 Helical; Name=S3 of repeat III. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1283 1301 Helical; Name=S4 of repeat III. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1319 1338 Helical; Name=S5 of repeat III. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1430 1451 Helical; Name=S6 of repeat III. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1515 1532 Helical; Name=S1 of repeat IV. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1544 1562 Helical; Name=S2 of repeat IV. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1575 1592 Helical; Name=S3 of repeat IV. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1606 1622 Helical; Name=S4 of repeat IV. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1642 1659 Helical; Name=S5 of repeat IV. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1735 1757 Helical; Name=S6 of repeat IV. {ECO:0000250|UniProtKB:D0E0C2}. TOPO_DOM 1 126 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 146 152 Extracellular. {ECO:0000305}.; TOPO_DOM 174 187 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 206 211 Extracellular. {ECO:0000305}.; TOPO_DOM 229 247 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 268 346 Extracellular. {ECO:0000305}.; TOPO_DOM 372 378 Extracellular. {ECO:0000305}.; TOPO_DOM 400 743 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 763 773 Extracellular. {ECO:0000305}.; TOPO_DOM 794 807 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 828 829 Extracellular. {ECO:0000305}.; TOPO_DOM 848 863 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 883 911 Extracellular. {ECO:0000305}.; TOPO_DOM 933 945 Extracellular. {ECO:0000305}.; TOPO_DOM 967 1191 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1210 1222 Extracellular. {ECO:0000305}.; TOPO_DOM 1242 1255 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1275 1282 Extracellular. {ECO:0000305}.; TOPO_DOM 1302 1318 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1339 1390 Extracellular. {ECO:0000305}.; TOPO_DOM 1413 1429 Extracellular. {ECO:0000305}.; TOPO_DOM 1452 1514 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1533 1543 Extracellular. {ECO:0000305}.; TOPO_DOM 1563 1574 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1593 1605 Extracellular. {ECO:0000305}.; TOPO_DOM 1623 1641 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1660 1681 Extracellular. {ECO:0000305}.; TOPO_DOM 1705 1734 Extracellular. {ECO:0000305}.; TOPO_DOM 1758 1984 Cytoplasmic. {ECO:0000305}. FUNCTION: Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient (PubMed:15123669). It is a tetrodotoxin-sensitive Na(+) channel isoform. Plays a role in pain mechanisms, especially in the development of inflammatory pain (PubMed:15314237). {ECO:0000250|UniProtKB:Q15858, ECO:0000269|PubMed:15123669, ECO:0000269|PubMed:15314237}. PTM: Ubiquitinated by NEDD4L; which may promote its endocytosis. Does not seem to be ubiquitinated by NEDD4. {ECO:0000269|PubMed:15123669}.; PTM: Phosphorylation at Ser-1488 by PKC in a highly conserved cytoplasmic loop increases peak sodium currents. {ECO:0000250|UniProtKB:Q15858}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15123669}; Multi-pass membrane protein {ECO:0000250|UniProtKB:D0E0C2}. Cell projection {ECO:0000250|UniProtKB:O08562}. Note=In neurite terminals. {ECO:0000250|UniProtKB:O08562}. SUBUNIT: The sodium channel complex consists of a large, channel-forming alpha subunit and 2-3 smaller, ancillary beta subunits (By similarity). Interacts with NEDD4 and NEDD4L. Interacts with the conotoxin GVIIJ (By similarity). {ECO:0000250|UniProtKB:O08562, ECO:0000250|UniProtKB:Q15858, ECO:0000269|PubMed:15123669}. DOMAIN: The sequence contains 4 internal repeats, each with 5 hydrophobic segments (S1, S2, S3, S5, S6) and one positively charged segment (S4). Segments S4 are probably the voltage-sensors and are characterized by a series of positively charged amino acids at every third position. {ECO:0000305}. +Q9JJN4 SCO2A_MOUSE Succinyl-CoA:3-ketoacid coenzyme A transferase 2A, mitochondrial (EC 2.8.3.5) (3-oxoacid CoA-transferase 2A) (Testis-specific succinyl-CoA:3-oxoacid CoA-transferase 1) (SCOT-t1) 520 56,473 Active site (1); Chain (1); Transit peptide (1) Ketone metabolism; succinyl-CoA degradation; acetoacetyl-CoA from succinyl-CoA: step 1/1. FUNCTION: Key enzyme for ketone body catabolism. Transfers the CoA moiety from succinate to acetoacetate. Formation of the enzyme-CoA intermediate proceeds via an unstable anhydride species formed between the carboxylate groups of the enzyme and substrate (By similarity). Probably play and important roles in the energy metabolism of spermatozoa. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +Q9ER60 SCN4A_MOUSE Sodium channel protein type 4 subunit alpha (Sodium channel protein skeletal muscle subunit alpha) (Sodium channel protein type IV subunit alpha) (Voltage-gated sodium channel subunit alpha Nav1.4) 1841 208,798 Chain (1); Disulfide bond (4); Domain (1); Glycosylation (10); Intramembrane (4); Modified residue (1); Repeat (4); Sequence conflict (2); Topological domain (29); Transmembrane (24) INTRAMEM 386 410 Pore-forming. {ECO:0000250|UniProtKB:D0E0C2}.; INTRAMEM 741 761 Pore-forming. {ECO:0000250|UniProtKB:D0E0C2}.; INTRAMEM 1225 1246 Pore-forming. {ECO:0000250|UniProtKB:D0E0C2}.; INTRAMEM 1516 1538 Pore-forming. {ECO:0000250|UniProtKB:D0E0C2}. TRANSMEM 132 150 Helical; Name=S1 of repeat I. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 158 178 Helical; Name=S2 of repeat I. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 193 210 Helical; Name=S3 of repeat I. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 217 233 Helical; Name=S4 of repeat I. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 253 272 Helical; Name=S5 of repeat I. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 418 438 Helical; Name=S6 of repeat I. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 573 591 Helical; Name=S1 of repeat II. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 603 622 Helical; Name=S2 of repeat II. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 637 656 Helical; Name=S3 of repeat II. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 659 676 Helical; Name=S4 of repeat II. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 693 711 Helical; Name=S5 of repeat II. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 775 795 Helical; Name=S6 of repeat II. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1027 1044 Helical; Name=S1 of repeat III. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1058 1076 Helical; Name=S2 of repeat III. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1091 1109 Helical; Name=S3 of repeat III. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1118 1136 Helical; Name=S4 of repeat III. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1154 1173 Helical; Name=S5 of repeat III. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1264 1285 Helical; Name=S6 of repeat III. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1349 1366 Helical; Name=S1 of repeat IV. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1378 1396 Helical; Name=S2 of repeat IV. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1409 1426 Helical; Name=S3 of repeat IV. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1440 1456 Helical; Name=S4 of repeat IV. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1476 1493 Helical; Name=S5 of repeat IV. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1569 1591 Helical; Name=S6 of repeat IV. {ECO:0000250|UniProtKB:D0E0C2}. TOPO_DOM 1 131 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 151 157 Extracellular. {ECO:0000305}.; TOPO_DOM 179 192 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 211 216 Extracellular. {ECO:0000305}.; TOPO_DOM 234 252 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 273 385 Extracellular. {ECO:0000305}.; TOPO_DOM 411 417 Extracellular. {ECO:0000305}.; TOPO_DOM 439 572 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 592 602 Extracellular. {ECO:0000305}.; TOPO_DOM 623 636 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 657 658 Extracellular. {ECO:0000305}.; TOPO_DOM 677 692 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 712 740 Extracellular. {ECO:0000305}.; TOPO_DOM 762 774 Extracellular. {ECO:0000305}.; TOPO_DOM 796 1026 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1045 1057 Extracellular. {ECO:0000305}.; TOPO_DOM 1077 1090 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1110 1117 Extracellular. {ECO:0000305}.; TOPO_DOM 1137 1153 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1174 1224 Extracellular. {ECO:0000305}.; TOPO_DOM 1247 1263 Extracellular. {ECO:0000305}.; TOPO_DOM 1286 1348 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1367 1377 Extracellular. {ECO:0000305}.; TOPO_DOM 1397 1408 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1427 1439 Extracellular. {ECO:0000305}.; TOPO_DOM 1457 1475 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1494 1515 Extracellular. {ECO:0000305}.; TOPO_DOM 1539 1568 Extracellular. {ECO:0000305}.; TOPO_DOM 1592 1841 Cytoplasmic. {ECO:0000305}. FUNCTION: This protein mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient. This sodium channel may be present in both denervated and innervated skeletal muscle. PTM: Phosphorylation at Ser-1322 by PKC in a highly conserved cytoplasmic loop slows inactivation of the sodium channel and reduces peak sodium currents. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P35499}; Multi-pass membrane protein {ECO:0000250|UniProtKB:D0E0C2}. SUBUNIT: Muscle sodium channels contain an alpha subunit and a smaller beta subunit. Heterooligomer with SCN2B or SCN4B; disulfide-linked. Interacts with the PDZ domain of the syntrophin SNTA1, SNTB1 and SNTB2. Interacts with the conotoxin GVIIJ. {ECO:0000250|UniProtKB:P04775, ECO:0000250|UniProtKB:P15390, ECO:0000250|UniProtKB:Q9JJV9}. DOMAIN: The sequence contains 4 internal repeats, each with 5 hydrophobic segments (S1, S2, S3, S5, S6) and one positively charged segment (S4). Segments S4 are probably the voltage-sensors and are characterized by a series of positively charged amino acids at every third position. {ECO:0000305}. TISSUE SPECIFICITY: Expressed in the myocardium. {ECO:0000269|PubMed:11834499}. +Q64124 SCX_MOUSE Basic helix-loop-helix transcription factor scleraxis 207 22,239 Chain (1); Compositional bias (1); Domain (1) FUNCTION: Plays an early essential role in mesoderm formation, as well as a later role in formation of somite-derived chondrogenic lineages. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}. SUBUNIT: Efficient DNA binding requires dimerization with another bHLH protein. Dimerizes and binds the E-box consensus sequence with E12. TISSUE SPECIFICITY: Expressed in mesenchymal precursors of cartilage and in connective tissue. Highly expressed in tendons in the limb, tongue and diaphragm and in cartilage of the bronchi. +Q5FWI2 SCTR_MOUSE Secretin receptor (SCT-R) 447 50,932 Chain (1); Glycosylation (5); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 143 166 Helical; Name=1. {ECO:0000255}.; TRANSMEM 174 193 Helical; Name=2. {ECO:0000255}.; TRANSMEM 216 239 Helical; Name=3. {ECO:0000255}.; TRANSMEM 254 275 Helical; Name=4. {ECO:0000255}.; TRANSMEM 294 316 Helical; Name=5. {ECO:0000255}.; TRANSMEM 343 361 Helical; Name=6. {ECO:0000255}.; TRANSMEM 369 391 Helical; Name=7. {ECO:0000255}. TOPO_DOM 29 142 Extracellular. {ECO:0000255}.; TOPO_DOM 167 173 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 194 215 Extracellular. {ECO:0000255}.; TOPO_DOM 240 253 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 276 293 Extracellular. {ECO:0000255}.; TOPO_DOM 317 342 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 362 368 Extracellular. {ECO:0000255}.; TOPO_DOM 392 447 Cytoplasmic. {ECO:0000255}. FUNCTION: This is a receptor for secretin. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q6NZL8 SCUB1_MOUSE Signal peptide, CUB and EGF-like domain-containing protein 1 1018 111,606 Alternative sequence (3); Chain (1); Disulfide bond (18); Domain (10); Glycosylation (7); Sequence conflict (6); Signal peptide (1) FUNCTION: Could function as an adhesive molecule and its matrix bound and soluble fragments may play a critical role in vascular biology. {ECO:0000250}. PTM: N-glycosylated. {ECO:0000250}.; PTM: Could be proteolytically cleaved to release a smaller active fragment. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8IWY4}. Cell membrane {ECO:0000250|UniProtKB:Q8IWY4}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8IWY4}. SUBUNIT: Forms homooligomers and heterooligomers with SCUBE2 and SCUBE3. {ECO:0000250}. +Q8CFE4 SCYL2_MOUSE SCY1-like protein 2 (Coated vesicle-associated kinase of 104 kDa) 930 103,317 Alternative sequence (3); Chain (1); Domain (1); Modified residue (3); Repeat (1) FUNCTION: Component of AP2-containing clathrin coated structures at the plasma membrane or of endocytic coated vesicles. May be a serine/threonine-protein kinase. May regulate clathrin-dependent trafficking between the TGN and/or the endosomal system (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250}. Endosome membrane {ECO:0000250}. Note=Plasma membrane-associated in clathrin-coated vesicles. Colocalizes to the trans-Golgi network (TGN) and to endosomal membranes with clathrin, transferrin and plasma membrane adapter AP1 and AP3 complexes (By similarity). {ECO:0000250}. SUBUNIT: Interacts with clathrin and AP2B1; the interaction mediates the association with the AP-2 complex. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:16914521}. +O88574 SAP30_MOUSE Histone deacetylase complex subunit SAP30 (30 kDa Sin3-associated polypeptide) (Sin3 corepressor complex subunit SAP30) (Sin3-associated polypeptide p30) 220 23,231 Beta strand (2); Chain (1); Compositional bias (1); Cross-link (3); Helix (3); Modified residue (4); Region (2); Zinc finger (1) FUNCTION: Involved in the functional recruitment of the Sin3-histone deacetylase complex (HDAC) to a specific subset of N-CoR corepressor complexes. Capable of transcription repression by N-CoR. Active in deacetylating core histone octamers (when in a complex) but inactive in deacetylating nucleosomal histones. {ECO:0000250|UniProtKB:O75446, ECO:0000269|PubMed:9702189}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with HCFC1 (By similarity). A component of the histone deacetylase complex that includes at least SIN3A, HDAC1 and HDAC2. Interacts with SIN3A, SIN3B, HDAC1, HDAC2, RBBP4 and NCOR1 (PubMed:9702189). Interacts directly with SAMSN1 (PubMed:20478393). Found in a complex composed of at least SINHCAF, SIN3A, HDAC1, SAP30, RBBP4, OGT and TET1 (PubMed:28554894). {ECO:0000250|UniProtKB:O75446, ECO:0000269|PubMed:20478393, ECO:0000269|PubMed:28554894, ECO:0000269|PubMed:9702189}. +Q9JI13 SAS10_MOUSE Something about silencing protein 10 (Charged amino acid-rich leucine zipper 1) (Crl-1) (Disrupter of silencing SAS10) (UTP3 homolog) 469 53,399 Alternative sequence (2); Chain (1); Compositional bias (1); Cross-link (1); Modified residue (5); Sequence conflict (2) FUNCTION: Essential for gene silencing: has a role in the structure of silenced chromatin. Plays a role in the developing brain. {ECO:0000250|UniProtKB:Q12136, ECO:0000269|PubMed:11404095}. PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11404095}. TISSUE SPECIFICITY: Detected mainly in subsets of neuronal cells of the brain. In the 17.5 dpc embryo, mainly expressed in the olfactory bulb and cerebral cortex. Postnatally, additionally expressed in the cerebellar cortex, most strongly in the hippocampus. {ECO:0000269|PubMed:11404095}. +Q7TST3 SAM10_MOUSE Sterile alpha motif domain-containing protein 10 (SAM domain-containing protein 10) 202 22,761 Chain (1); Domain (1) +Q921K8 TCAF2_MOUSE TRPM8 channel-associated factor 2 (TRP channel-associated factor 2) 919 101,598 Chain (1); Domain (1); Erroneous initiation (1); Sequence conflict (6) FUNCTION: Negatively regulates the plasma membrane cation channel TRPM8 activity. Involved in the recruitment of TRPM8 to the cell surface. Promotes prostate cancer cell migration stimulation in a TRPM8-dependent manner. {ECO:0000250|UniProtKB:A6NFQ2}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:A6NFQ2}. Note=Colocalizes with TRPM8 on the plasma membrane. {ECO:0000250|UniProtKB:A6NFQ2}. SUBUNIT: Interacts with TRPM8 (via N-terminus and C-terminus domains); the interaction inhibits TRPM8 channel activity. Interacts with TRPV6. {ECO:0000250|UniProtKB:A6NFQ2}. +Q6A098 SBP2L_MOUSE Selenocysteine insertion sequence-binding protein 2-like (SECIS-binding protein 2-like) 1086 119,641 Chain (1); Erroneous initiation (1); Modified residue (1) FUNCTION: Binds SECIS (Sec insertion sequence) elements present on selenocysteine (Sec) protein mRNAs, but does not promote Sec incorporation into selenoproteins. {ECO:0000250}. +Q8K2B0 SC65_MOUSE Endoplasmic reticulum protein SC65 (Leprecan-like protein 4) (Prolyl 3-hydroxylase family member 4) (Synaptonemal complex protein SC65) 443 51,132 Chain (1); Compositional bias (1); Glycosylation (1); Signal peptide (1) FUNCTION: Part of a complex composed of PLOD1, P3H3 and P3H4 that catalyzes hydroxylation of lysine residues in collagen alpha chains and is required for normal assembly and cross-linking of collagen fibrils (PubMed:27119146). Required for normal bone density and normal skin stability via its role in hydroxylation of lysine residues in collagen alpha chains and in collagen fibril assembly (PubMed:23959653, PubMed:27119146, PubMed:28115524). {ECO:0000269|PubMed:23959653, ECO:0000269|PubMed:27119146, ECO:0000269|PubMed:28115524}. SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:Q92791}. SUBUNIT: Interacts with PLOD1, P3H3 and PPIB. Identified in a complex with PLOD1 and P3H3. {ECO:0000269|PubMed:27119146}. TISSUE SPECIFICITY: Detected in calvaria, cartilage, kidney, ribs, and at lower levels in tail (PubMed:23959653, PubMed:27119146). Detected in proliferating and prehypertrophic chondrocytes in the growth plate of long bones and in mineralizing chondro-osseus bone collar and cortical bone (PubMed:23959653). Detected on osteoblasts in long bones (PubMed:23959653, PubMed:27119146). Detected in skin fibroblasts (at protein level) (PubMed:27119146). Detected in fetal ribs, and in tibia and metatarsus from neonates (PubMed:23959653). {ECO:0000269|PubMed:23959653, ECO:0000269|PubMed:27119146}. +Q01405 SC23A_MOUSE Protein transport protein Sec23A (SEC23-related protein A) 765 86,162 Chain (1); Frameshift (1); Initiator methionine (1); Metal binding (4); Modified residue (2); Repeat (1); Sequence conflict (15) FUNCTION: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules for their transport to the Golgi complex (By similarity). Required for the translocation of insulin-induced glucose transporter SLC2A4/GLUT4 to the cell membrane (PubMed:27354378). {ECO:0000250|UniProtKB:Q15436, ECO:0000269|PubMed:27354378}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250|UniProtKB:Q15436}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q15436}; Cytoplasmic side {ECO:0000250|UniProtKB:Q15436}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q15436}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q15436}; Cytoplasmic side {ECO:0000250|UniProtKB:Q15436}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q15436}. Note=Enriched at endoplasmic reticulum exit sites (ERES), also known as transitional endoplasmic reticulum (tER). {ECO:0000250|UniProtKB:Q15436}. SUBUNIT: COPII is composed of at least five proteins: the Sec23/24 complex, the Sec13/31 complex and Sar1 (By similarity). Interacts with SEC23IP (PubMed:10400679). Interacts with HTR4 (PubMed:15466885). Interacts with SEC16A (PubMed:17428803). Interacts with SLC6A4 (PubMed:17452640). Interacts (as part of the Sec23/24 complex) with SEC22B; recruits SEC22B into COPII-coated vesicles and allows the transport of this cargo from the endoplasmic reticulum to the Golgi. Interacts (via Gelsolin-like repeat) with MIA2 and MIA3; specifically involved in the transport of large cargos like the collagen COL7A1 (By similarity). Interacts with DDHD1 (PubMed:17428803). {ECO:0000250|UniProtKB:P15303, ECO:0000250|UniProtKB:Q15436, ECO:0000269|PubMed:10400679, ECO:0000269|PubMed:15466885, ECO:0000269|PubMed:17428803, ECO:0000269|PubMed:17452640}. DOMAIN: The Gelsolin-like repeat mediates interaction with proteins containing PPP motifs that include MIA2, MIA3 but also SEC31A. These interactions are probably competitive. {ECO:0000250|UniProtKB:Q15436}. TISSUE SPECIFICITY: High levels in brain and fibroblasts. {ECO:0000269|PubMed:8417978}. +E9QAT4 SC16A_MOUSE Protein transport protein Sec16A (SEC16 homolog A) (p250) 2357 254,202 Alternative sequence (1); Chain (1); Modified residue (28); Region (5); Sequence conflict (1) FUNCTION: Acts as a molecular scaffold that plays a key role in the organization of the endoplasmic reticulum exit sites (ERES), also known as transitional endoplasmic reticulum (tER). SAR1A-GTP-dependent assembly of SEC16A on the ER membrane forms an organized scaffold defining an ERES. Required for secretory cargo traffic from the endoplasmic reticulum to the Golgi apparatus (PubMed:17428803). Mediates the recruitment of MIA3/TANGO to ERES. Regulates both conventional (ER/Golgi-dependent) and GORASP2-mediated unconventional (ER/Golgi-independent) trafficking of CFTR to cell membrane (By similarity). Acts as a RAB10 effector in the regulation of insulin-induced SLC2A4/GLUT4 glucose transporter-enriched vesicles delivery to the plasma membrane in adipocytes (PubMed:27354378). {ECO:0000250|UniProtKB:O15027, ECO:0000269|PubMed:17428803, ECO:0000269|PubMed:27354378}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O15027}; Peripheral membrane protein. Golgi apparatus membrane {ECO:0000250|UniProtKB:O15027}; Peripheral membrane protein {ECO:0000250|UniProtKB:O15027}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:27354378}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:O15027}. Microsome membrane {ECO:0000250|UniProtKB:O15027}. Note=SAR1A activity is required to maintain SEC16A localization at discrete locations on the ER membrane perhaps by preventing its dissociation (By similarity). Localizes to endoplasmic reticulum exit sites (ERES), also known as transitional endoplasmic reticulum (tER). MIA3 and LRRK2 are required for its proper localization to ERES (PubMed:25201882). Recruited to microsomal membrane in SAR1-dependent manner (By similarity). {ECO:0000250|UniProtKB:O15027, ECO:0000269|PubMed:25201882}. SUBUNIT: SEC16A and SEC16B are each present in multiple copies in a heteromeric complex (By similarity). Interacts with SEC23A (PubMed:17428803). Interacts with RNF183, RNF152, MIA3 and SEC13 (By similarity). Interacts with GORASP2 in response to ER stress (By similarity). Interacts with LRRK2 (via ROC domain) (PubMed:25201882). Interacts with RAB10 (PubMed:27354378). {ECO:0000250|UniProtKB:O15027, ECO:0000269|PubMed:17428803, ECO:0000269|PubMed:25201882, ECO:0000269|PubMed:27354378}. +Q9JKD3 SCAM5_MOUSE Secretory carrier-associated membrane protein 5 (Secretory carrier membrane protein 5) 235 26,068 Chain (1); Topological domain (5); Transmembrane (4) TRANSMEM 40 60 Helical. {ECO:0000255}.; TRANSMEM 68 88 Helical. {ECO:0000255}.; TRANSMEM 103 125 Helical. {ECO:0000255}.; TRANSMEM 149 169 Helical. {ECO:0000255}. TOPO_DOM 1 39 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 61 67 Extracellular. {ECO:0000255}.; TOPO_DOM 89 102 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 126 148 Extracellular. {ECO:0000255}.; TOPO_DOM 170 235 Cytoplasmic. {ECO:0000255}. FUNCTION: Required for the calcium-dependent exocytosis of signal sequence-containing cytokines such as CCL5. Probably acts in cooperation with the SNARE machinery (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11050114}; Multi-pass membrane protein {ECO:0000269|PubMed:11050114}. Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Recycling endosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:11050114}; Multi-pass membrane protein {ECO:0000269|PubMed:11050114}. Note=Mainly localizes in Golgi apparatus membrane. Upon calcium-triggered exocytosis, it translocates to the cell membrane. Highly enriched in synaptic vesicles (By similarity). {ECO:0000250}. SUBUNIT: Interacts (via C-terminal part) with SYT1 and SYT2; interaction with synaptotagmins making a link with the SNARE molecules. Interacts with SLC9A7 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Brain-specific. {ECO:0000269|PubMed:11050114}. +Q8VBW1 SC6A8_MOUSE Sodium- and chloride-dependent creatine transporter 1 (CT1) (Creatine transporter 1) (Solute carrier family 6 member 8) 640 70,999 Alternative sequence (2); Chain (1); Glycosylation (3); Modified residue (3); Topological domain (13); Transmembrane (12) TRANSMEM 61 81 Helical. {ECO:0000255}.; TRANSMEM 88 108 Helical. {ECO:0000255}.; TRANSMEM 139 159 Helical. {ECO:0000255}.; TRANSMEM 231 251 Helical. {ECO:0000255}.; TRANSMEM 270 290 Helical. {ECO:0000255}.; TRANSMEM 305 325 Helical. {ECO:0000255}.; TRANSMEM 342 362 Helical. {ECO:0000255}.; TRANSMEM 395 415 Helical. {ECO:0000255}.; TRANSMEM 445 470 Helical. {ECO:0000255}.; TRANSMEM 485 505 Helical. {ECO:0000255}.; TRANSMEM 526 546 Helical. {ECO:0000255}.; TRANSMEM 566 586 Helical. {ECO:0000255}. TOPO_DOM 1 60 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 82 87 Extracellular. {ECO:0000255}.; TOPO_DOM 109 138 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 160 230 Extracellular. {ECO:0000255}.; TOPO_DOM 252 269 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 291 304 Extracellular. {ECO:0000255}.; TOPO_DOM 326 341 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 363 394 Extracellular. {ECO:0000255}.; TOPO_DOM 416 444 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 471 484 Extracellular. {ECO:0000255}.; TOPO_DOM 506 525 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 547 565 Extracellular. {ECO:0000255}.; TOPO_DOM 587 640 Cytoplasmic. {ECO:0000255}. FUNCTION: Required for the uptake of creatine. Plays an important role in supplying creatine to the brain via the blood-brain barrier. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +P97952 SCN1B_MOUSE Sodium channel subunit beta-1 218 24,650 Chain (1); Disulfide bond (1); Domain (1); Glycosylation (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 161 182 Helical. {ECO:0000255}. TOPO_DOM 19 160 Extracellular. {ECO:0000255}.; TOPO_DOM 183 218 Cytoplasmic. {ECO:0000255}. FUNCTION: Crucial in the assembly, expression, and functional modulation of the heterotrimeric complex of the sodium channel. The subunit beta-1 can modulate multiple alpha subunit isoforms from brain, skeletal muscle, and heart. Its association with NFASC may target the sodium channels to the nodes of Ranvier of developing axons and retain these channels at the nodes in mature myelinated axons (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q07699}; Single-pass type I membrane protein {ECO:0000255}. SUBUNIT: The voltage-sensitive sodium channel consists of an ion conducting pore forming alpha-subunit regulated by one or more beta-1, beta-2, beta-3 and/or beta-4 subunits. Beta-1 and beta-3 are non-covalently associated with alpha, while beta-2 and beta-4 are covalently linked by disulfide bonds. Beta-1 or beta-3 subunits associate with NFASC. Associates with SCN10A. Interacts with SCN1A. Interacts with SCN8A (By similarity). {ECO:0000250|UniProtKB:Q00954, ECO:0000250|UniProtKB:Q07699}. +Q56A07 SCN2B_MOUSE Sodium channel subunit beta-2 215 24,228 Chain (1); Disulfide bond (2); Domain (1); Glycosylation (3); Modified residue (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 160 180 Helical. {ECO:0000255}. TOPO_DOM 30 159 Extracellular. {ECO:0000255}.; TOPO_DOM 181 215 Cytoplasmic. {ECO:0000255}. FUNCTION: Crucial in the assembly, expression, and functional modulation of the heterotrimeric complex of the sodium channel. The subunit beta-2 causes an increase in the plasma membrane surface area and in its folding into microvilli. Interacts with TNR may play a crucial role in clustering and regulation of activity of sodium channels at nodes of Ranvier (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: The voltage-sensitive sodium channel consists of an ion conducting pore forming alpha-subunit regulated by one or more beta-1, beta-2, beta-3 and/or beta-4 subunits. Beta-1 and beta-3 are non-covalently associated with alpha, while beta-2 and beta-4 are covalently linked by disulfide bonds (By similarity). {ECO:0000250}. +Q9ESL0 SCO2B_MOUSE Succinyl-CoA:3-ketoacid coenzyme A transferase 2B, mitochondrial (EC 2.8.3.5) (3-oxoacid CoA-transferase 2B) (Testis-specific succinyl-CoA:3-oxoacid CoA-transferase 2) (SCOT-t2) 520 56,592 Active site (1); Chain (1); Sequence conflict (1); Transit peptide (1) Ketone metabolism; succinyl-CoA degradation; acetoacetyl-CoA from succinyl-CoA: step 1/1. FUNCTION: Key enzyme for ketone body catabolism. Transfers the CoA moiety from succinate to acetoacetate. Formation of the enzyme-CoA intermediate proceeds via an unstable anhydride species formed between the carboxylate groups of the enzyme and substrate (By similarity). Probably play and important roles in the energy metabolism of spermatozoa. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Testis specific. Expressed in late spermatids. Accumulates during spermiogenesis. Also detected in the midpiece of spermatozoa. {ECO:0000269|PubMed:11090426}. +Q9WTS5 TEN2_MOUSE Teneurin-2 (Ten-2) (Protein Odd Oz/ten-m homolog 2) (Tenascin-M2) (Ten-m2) (Teneurin transmembrane protein 2) [Cleaved into: Ten-2, soluble form; Ten-2 intracellular domain (Ten-2 ICD)] 2764 306,468 Chain (3); Compositional bias (2); Disulfide bond (22); Domain (9); Glycosylation (15); Modified residue (4); Repeat (28); Sequence conflict (33); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 380 400 Helical. {ECO:0000255}. TOPO_DOM 1 379 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 401 2764 Extracellular. {ECO:0000255}. FUNCTION: Involved in neural development, regulating the establishment of proper connectivity within the nervous system. Acts as a ligand of the ADGRL1 receptor. Promotes the formation of filopodia and enlarged growth cone in neuronal cells. Mediates axon guidance and homophilic and heterophilic cell-cell adhesion. May function as a cellular signal transducer (By similarity). {ECO:0000250}.; FUNCTION: Ten-2 intracellular domain: Induces gene transcription inhibition. {ECO:0000250}. PTM: Ten-2, soluble form: Derives from the membrane form by proteolytic processing. {ECO:0000250}.; PTM: Ten-2 intracellular domain: Derives from the plasma membrane form by proteolytic cleavage and translocates to the nucleus. Homophilic binding of the C-terminal extracellular domain stimulates its proteolytic cleavage and release in the cytoplasmic. Is subjected to rapid degradation by the proteasome pathway (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Golgi apparatus {ECO:0000250}. Cell junction, synapse {ECO:0000250}. Cell projection, dendritic spine {ECO:0000250}. Cell projection, filopodium {ECO:0000250}. Cell projection, growth cone {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cell junction, synapse, synaptosome {ECO:0000250}. Note=Colocalizes with ADGRL1 across intercellular junctions. {ECO:0000250}.; SUBCELLULAR LOCATION: Ten-2 intracellular domain: Nucleus, PML body {ECO:0000250}. SUBUNIT: Homodimer; disulfide-linked. Heterodimer with either TENM1 or TENM3. May also form heterodimer with TENM4. DOMAIN: EGF-like domains 2 and 5 which have an odd number of cysteines might enable the formation of intermolecular disulfide bonds.; DOMAIN: Cytoplasmic proline-rich regions could serve as docking domains for intracellular SH3-containing proteins. TISSUE SPECIFICITY: Expressed in the cortex, CA1, CA2, CA3, dentate gyrus and granular layer of the hippocampus. Expressed in the Purkinje cells and molecular layer of the cerebellum. {ECO:0000269|PubMed:12915301}. +Q8K1J5 SDE2_MOUSE Replication stress response regulator SDE2 448 48,580 Chain (1); Coiled coil (1); Domain (1); Modified residue (5); Motif (1); Propeptide (1); Site (1) FUNCTION: Involved in both DNA replication and cell cycle control. Unprocessed SDE2 interacts with PCNA via its PIP-box. The interaction with PCNA prevents monoubiquitination of the latter thereby inhibiting translesion DNA synthesis. The binding of SDE2 to PCNA also leads to processing of SDE2 by an unidentified deubiquitinating enzyme, cleaving off the N-terminal ubiquitin-like domain. The resulting mature SDE2 is degraded by the DCX(DTL) complex in a cell cycle- and DNA damage dependent manner. Binding of SDE2 to PCNA is necessary to counteract damage due to ultraviolet light induced replication stress. The complete degradation of SDE2 is necessary to allow S-phase progression. {ECO:0000250|UniProtKB:Q6IQ49}. PTM: The protein is cleaved at Gly-77 by a deubiquitinating enzyme to form the active SDE2. {ECO:0000250|UniProtKB:Q6IQ49}.; PTM: Both SDE2-UBL and the mature SDE2 are polyubiquitinated. {ECO:0000250|UniProtKB:Q6IQ49}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6IQ49}. DOMAIN: The PIP-box (PCNA interacting peptide) motif mediates both the interaction with PCNA and cleavage of the SDE2 precursor by a deubiquitinating enzyme. {ECO:0000250|UniProtKB:Q6IQ49}.; DOMAIN: The SAP domain is necessary for specific binding to DNA. {ECO:0000250|UniProtKB:Q6IQ49}.; DOMAIN: The propeptide displays a ubiquitin-like fold. {ECO:0000250|UniProtKB:Q6IQ49}. +Q99JZ0 SDCB2_MOUSE Syntenin-2 (Syndecan-binding protein 2) 292 31,565 Chain (1); Domain (2) FUNCTION: Binds phosphatidylinositol 4,5-bisphosphate (PIP2). May play a role in the organization of nuclear PIP2, cell division and cell survival. {ECO:0000250|UniProtKB:Q9H190}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H190}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9H190}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9H190}. Cell membrane {ECO:0000250|UniProtKB:Q9H190}. Nucleus speckle {ECO:0000250|UniProtKB:Q9H190}. Note=Associates with intracellular membranes and enriched in the apical region of the cell and in intracellular compartments. Colocalizes with TM4SF1 in the apical region of the cell. Predominantly targeted to nuclear PIP2 pools. Shuttles between several subcellular compartments. PIP2 plays an important role in the distribution of SDCBP2. {ECO:0000250|UniProtKB:Q9H190}. SUBUNIT: Monomer and homodimer. Interacts with SDCBP. Interacts with TM4SF1. {ECO:0000250|UniProtKB:Q9H190}. DOMAIN: The two PDZ domains mediate the interaction with phosphatidylinositol 4,5-bisphosphate (PIP2) and target SDCBP2 to the plasma membranes and nucleoli, PIP2-rich regions. {ECO:0000250|UniProtKB:Q9H190}. +Q3V172 SE1L2_MOUSE Protein sel-1 homolog 2 (Suppressor of lin-12-like protein 2) (Sel-1L2) 688 77,989 Chain (1); Glycosylation (2); Repeat (11); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 663 683 Helical. {ECO:0000255}. TOPO_DOM 19 662 Extracellular. {ECO:0000255}.; TOPO_DOM 684 688 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. +Q80UZ2 SDA1_MOUSE Protein SDA1 homolog (SDA1 domain-containing protein 1) 687 79,559 Alternative sequence (3); Chain (1); Coiled coil (1); Modified residue (7); Sequence conflict (6) FUNCTION: Required for 60S pre-ribosomal subunits export to the cytoplasm. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. +Q9CY52 THG1_MOUSE Probable tRNA(His) guanylyltransferase (EC 2.7.7.79) (tRNA-histidine guanylyltransferase) 298 34,971 Chain (1); Metal binding (5); Nucleotide binding (2); Sequence conflict (1) FUNCTION: Adds a GMP to the 5'-end of tRNA(His) after transcription and RNase P cleavage. This step is essential for proper recognition of the tRNA and for the fidelity of protein synthesis. {ECO:0000250|UniProtKB:Q9NWX6}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homotetramer. {ECO:0000250}. +Q9BCZ4 SELS_MOUSE Selenoprotein S (SelS) (Minor histocompatibility antigen H47) 190 21,509 Chain (1); Erroneous termination (3); Natural variant (1); Non-standard residue (1); Region (1); Sequence conflict (1); Transmembrane (1) TRANSMEM 28 48 Helical. {ECO:0000255}. FUNCTION: Involved in the degradation process of misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Probably acts by serving as a linker between DERL1, which mediates the retrotranslocation of misfolded proteins into the cytosol, and the ATPase complex VCP, which mediates the translocation and ubiquitination (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with DERL1 and (via VIM motif) with VCP, suggesting that it forms a membrane complex with DERL1 that serves as a receptor for VCP. Also interacts with DERL2, DERL3 and SELENOK. The SELENOK-SELENOS complex interacts with VCP (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9BQE4}. +Q9ERR7 SEP15_MOUSE Selenoprotein F (15 kDa selenoprotein) 162 17,806 Chain (1); Non-standard residue (1); Sequence conflict (4); Signal peptide (1) FUNCTION: May be involved in redox reactions associated with the formation of disulfide bonds. May contribute to the quality control of protein folding in the endoplasmic reticulum (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250}. Note=The association with UGGT1/UGCGL1 is essential for its retention in the endoplasmic reticulum. {ECO:0000250}. SUBUNIT: Forms a tight complex with UGGT1/UGCGL1. +Q91YJ3 THYN1_MOUSE Thymocyte nuclear protein 1 (Thymocyte protein Thy28) (mThy28) 226 26,178 Chain (1); Motif (1) FUNCTION: Specifically binds 5-hydroxymethylcytosine (5hmC), suggesting that it acts as a specific reader of 5hmC. {ECO:0000269|PubMed:23434322}. PTM: Phosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14580360, ECO:0000269|PubMed:14601557}. TISSUE SPECIFICITY: Expressed in the medulla containing mature thymocytes, but not the cortex having immature thymocytes (at protein level). Abundant expression seen in testis, liver, brain and kidney with lower levels of the expression in thymus, spleen, heart and stomach. {ECO:0000269|PubMed:12384300, ECO:0000269|PubMed:14580360, ECO:0000269|PubMed:14601557}. +Q8BMC3 SHC2_MOUSE SHC-transforming protein 2 (Protein Sck) (Protein Sli) (SHC-transforming protein B) (Src homology 2 domain-containing-transforming protein C2) (SH2 domain protein C2) 573 61,771 Chain (1); Domain (2); Modified residue (3); Region (1); Sequence conflict (1) FUNCTION: Signaling adapter that couples activated growth factor receptors to signaling pathway in neurons. Involved in the signal transduction pathways of neurotrophin-activated Trk receptors in cortical neurons. PTM: Phosphorylated on tyrosine by the Trk receptors. {ECO:0000269|PubMed:12006576}. SUBUNIT: Interacts with the Trk receptors in a phosphotyrosine-dependent manner and MEGF12. Once activated, binds to GRB2 (By similarity). {ECO:0000250}. DOMAIN: The PID domain mediates binding to the TrkA receptor. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain. Expressed at high level in the hypothalamus and at low level in the caudate nucleus. +Q91ZM2 SH2B1_MOUSE SH2B adapter protein 1 (Pro-rich, PH and SH2 domain-containing signaling mediator) (PSM) (SH2 domain-containing protein 1B) (SH2-B PH domain-containing signaling mediator 1) 756 79,625 Alternative sequence (6); Beta strand (7); Chain (1); Domain (2); Helix (4); Modified residue (7); Region (5); Sequence conflict (3); Turn (1) FUNCTION: Adapter protein for several members of the tyrosine kinase receptor family. Involved in multiple signaling pathways mediated by Janus kinase (JAK) and receptor tyrosine kinases, including the receptors of insulin (INS), insulin-like growth factor I (IGF1), nerve growth factor (NGF), brain-derived neurotrophic factor (BDNF), glial cell line-derived neurotrophic factor (GDNF), platelet-derived growth factor (PDGF) and fibroblast growth factors (FGFs). In growth hormone (GH) signaling, autophosphorylated ('Tyr-813') JAK2 recruits SH2B1, which in turn is phosphorylated by JAK2 on tyrosine residues. These phosphotyrosines form potential binding sites for other signaling proteins. GH also promotes serine/threonine phosphorylation of SH2B1 and these phosphorylated residues may serve to recruit other proteins to the GHR-JAK2-SH2B1 complexes, such as RAC1. In leptin (LEP) signaling, binds to and potentiates the activation of JAK2 by globally enhancing downstream pathways. In response to leptin, binds simultaneously to both, JAK2 and IRS1 or IRS2, thus mediating formation of a complex of JAK2, SH2B1 and IRS1 or IRS2. Mediates tyrosine phosphorylation of IRS1 and IRS2, resulting in activation of the PI 3-kinase pathway. Acts as positive regulator of NGF-mediated activation of the Akt/Forkhead pathway; prolongs NGF-induced phosphorylation of AKT1 on 'Ser-473' and AKT1 enzymatic activity. Enhances the kinase activity of the cytokine receptor-associated tyrosine kinase JAK2 and of other receptor tyrosine kinases, such as FGFR3 and NTRK1. For JAK2, the mechanism seems to involve dimerization of both, SH2B1 and JAK2. Enhances RET phosphorylation and kinase activity (By similarity). Isoforms seem to be differentially involved in IGF-I and PDGF-induced mitogenesis, according the order: isoform 3 > isoform 4 > isoform 1 > isoform 2. {ECO:0000250, ECO:0000269|PubMed:11502739, ECO:0000269|PubMed:15316008, ECO:0000269|PubMed:16098827, ECO:0000269|PubMed:9343427}. PTM: Phosphorylated on tyrosine residues in response to IGF-I and PDGF stimulation. {ECO:0000269|PubMed:11502739}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000305}. Nucleus {ECO:0000250}. Note=Shuttles between the nucleus and the cytoplasm. {ECO:0000250}. SUBUNIT: Self-associates. Homopentamer (By similarity). Forms a heteromultimeric complex with SH2B2 (By similarity). Interacts with SH2B2. Isoform 1 interacts via its SH2 domain with JAK2. Isoform 2 interacts via its SH2 domain and its N-terminus with JAK2; the SH2 domain is required for the major interaction with JAK2 phosphorylated on tyrosine residues; the N-terminus provides a low-affinity binding to JAK2 independent of JAK2 phosphorylation. Isoform 3 interacts via its SH2 domain with JAK2. Isoform 1 interacts via its SH2 domain with INSR; the interaction requires receptor activation. Isoform 3 interacts via its SH2 domain with INSR; the interaction requires receptor activation and requires INSR phosphorylation at 'Tyr-1175'. Isoform 1 interacts with IGF1R; the interaction requires receptor activation. Isoform 2 interacts via its SH2 domain with FGFR3; the interaction requires FGFR3 'Tyr-719' and 'Tyr-755'. Isoform 2 interacts with RET; the interaction requires RET kinase activity and RET 'Tyr-982'. Isoform 2 interacts with RAC1. Isoform 2 interacts with PDGFRA and/or PDGFRB; the interaction requires receptor activation. Interacts with ISR1 and ISR2. Isoform 3 is probably part of a complex consisting of INSR, ISR1 and SH2B1. Probably part of a ternary complex consisting of SH2B1, JAK2 and ISR1 or ISR2. May interact with FCER1G (By similarity). Interacts (via SH2 domain) with NTRK1 (phosphorylated) (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed with highest levels in liver, brain and heart. Isoform 3 is widely expressed. {ECO:0000269|PubMed:10594240, ECO:0000269|PubMed:9498552}. +O88520 SHOC2_MOUSE Leucine-rich repeat protein SHOC-2 (Protein soc-2 homolog) (Protein sur-8 homolog) 582 64,893 Chain (1); Repeat (20); Sequence conflict (1) FUNCTION: Regulatory subunit of protein phosphatase 1 (PP1c) that acts as a M-Ras/MRAS effector and participates in MAPK pathway activation. Upon M-Ras/MRAS activation, targets PP1c to specifically dephosphorylate the 'Ser-259' inhibitory site of RAF1 kinase and stimulate RAF1 activity at specialized signaling complexes (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Translocates from cytoplasm to nucleus upon growth factor stimulation. {ECO:0000250}. SUBUNIT: Interacts with M-Ras/MRAS, and RAF1. Forms a multiprotein complex with Ras (M-Ras/MRAS), Raf (RAF1) and protein phosphatase 1 (PPP1CA, PPP1CB and PPP1CC). Interacts with ERBIN; disrupts the interaction with RAF1 and Ras, leading to prevent activation of the Ras signaling pathway. Specifically binds K-Ras/KRAS, M-Ras/MRAS and N-Ras/NRAS but not H-Ras/HRAS (By similarity). {ECO:0000250}. +Q9JID9 SH2B2_MOUSE SH2B adapter protein 2 (Adapter protein with pleckstrin homology and Src homology 2 domains) (SH2 and PH domain-containing adapter protein APS) 621 66,557 Beta strand (8); Chain (1); Domain (2); Helix (1); Modified residue (5); Sequence conflict (2); Turn (1) FUNCTION: Adapter protein for several members of the tyrosine kinase receptor family. Involved in multiple signaling pathways. May be involved in coupling from immunoreceptor to Ras signaling. Acts as a negative regulator of cytokine signaling in collaboration with CBL. Binds to EPOR and suppresses EPO-induced STAT5 activation, possibly through a masking effect on STAT5 docking sites in EPOR. Suppresses PDGF-induced mitogenesis. May induce cytoskeletal reorganization via interaction with VAV3 (By similarity). {ECO:0000250}. PTM: Tyrosine phosphorylated by JAK2, KIT and other kinases activated by B-cell receptor in response to stimulation with cytokines, IL3, IL5, PDGF, IGF1, IGF2, CSF2/GM-CSF and cross-linking of the B-cell receptor complex. {ECO:0000269|PubMed:10872802}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Cytoplasmic before PDGF stimulation. After PDGF stimulation, localized at the cell membrane and peripheral region (By similarity). {ECO:0000250}. SUBUNIT: Homodimer. Interacts with KIT/c-KIT, SHC1, EPOR, PDGFR, VAV1 and VAV3. Interacts (via N-terminal region) with SHC1. Interacts (via the phosphorylated C-terminus) with GRB2. Interacts (via its SH2 domain) with EPOR, INSR and KIT. Interacts with GRB2 after B-cell antigen receptor stimulation. Interacts (via PH domain) with VAV3. Interacts with NTRK1, NTRK2 and NTRK3 (phosphorylated); after stimulation of the receptor by its extracellular ligand and subsequent autophosphorylation of the receptor. Binds INSR, GRB2, ASB6 and CAP. Insulin stimulation leads to dissociation of CAP. Binds CBS only when SH2B2/APS has become phosphorylated. INSR binding does not depend on the phosphorylation of SH2B2/APS (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Strongly expressed in brain; also expressed in spleen, kidney and skeletal muscle, and at low levels in small intestine and bone marrow. Strongly expressed in B-cell lines, but not T-cell lines. Also expressed in myeloid and fibroblast cell lines. {ECO:0000269|PubMed:10872802}. +Q6A4L0 S22AD_MOUSE Solute carrier family 22 member 13 (Organic cation transporter-like 3) (ORCTL-3) 551 60,724 Chain (1); Glycosylation (4); Natural variant (3); Sequence conflict (1); Topological domain (13); Transmembrane (12) TRANSMEM 23 43 Helical. {ECO:0000255}.; TRANSMEM 143 163 Helical. {ECO:0000255}.; TRANSMEM 168 188 Helical. {ECO:0000255}.; TRANSMEM 196 216 Helical. {ECO:0000255}.; TRANSMEM 225 245 Helical. {ECO:0000255}.; TRANSMEM 252 272 Helical. {ECO:0000255}.; TRANSMEM 333 353 Helical. {ECO:0000255}.; TRANSMEM 355 375 Helical. {ECO:0000255}.; TRANSMEM 405 425 Helical. {ECO:0000255}.; TRANSMEM 428 448 Helical. {ECO:0000255}.; TRANSMEM 453 473 Helical. {ECO:0000255}.; TRANSMEM 479 499 Helical. {ECO:0000255}. TOPO_DOM 1 22 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 44 142 Extracellular. {ECO:0000255}.; TOPO_DOM 164 167 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 189 195 Extracellular. {ECO:0000255}.; TOPO_DOM 217 224 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 246 251 Extracellular. {ECO:0000255}.; TOPO_DOM 273 332 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 354 354 Extracellular. {ECO:0000255}.; TOPO_DOM 376 404 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 426 427 Extracellular. {ECO:0000255}.; TOPO_DOM 449 452 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 474 478 Extracellular. {ECO:0000255}.; TOPO_DOM 500 551 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q99PL8 S19A3_MOUSE Thiamine transporter 2 (ThTr-2) (ThTr2) (Solute carrier family 19 member 3) 488 55,073 Chain (1); Glycosylation (2); Sequence conflict (5); Topological domain (13); Transmembrane (12) TRANSMEM 9 29 Helical. {ECO:0000255}.; TRANSMEM 55 75 Helical. {ECO:0000255}.; TRANSMEM 83 103 Helical. {ECO:0000255}.; TRANSMEM 112 132 Helical. {ECO:0000255}.; TRANSMEM 146 166 Helical. {ECO:0000255}.; TRANSMEM 173 193 Helical. {ECO:0000255}.; TRANSMEM 277 297 Helical. {ECO:0000255}.; TRANSMEM 311 331 Helical. {ECO:0000255}.; TRANSMEM 336 356 Helical. {ECO:0000255}.; TRANSMEM 370 390 Helical. {ECO:0000255}.; TRANSMEM 400 420 Helical. {ECO:0000255}.; TRANSMEM 429 449 Helical. {ECO:0000255}. TOPO_DOM 1 8 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 30 54 Extracellular. {ECO:0000255}.; TOPO_DOM 76 82 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 104 111 Extracellular. {ECO:0000255}.; TOPO_DOM 133 145 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 167 172 Extracellular. {ECO:0000255}.; TOPO_DOM 194 276 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 298 310 Extracellular. {ECO:0000255}.; TOPO_DOM 332 335 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 357 369 Extracellular. {ECO:0000255}.; TOPO_DOM 391 399 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 421 428 Extracellular. {ECO:0000255}.; TOPO_DOM 450 488 Cytoplasmic. {ECO:0000255}. FUNCTION: Mediates high affinity thiamine uptake, probably via a proton anti-port mechanism. Has no folate transport activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: High expression in kidney, brain, lung and small intestine. +O08966 S22A1_MOUSE Solute carrier family 22 member 1 (Organic cation transporter 1) (mOCT1) 556 61,521 Chain (1); Glycosylation (1); Modified residue (2); Sequence conflict (3); Site (1); Topological domain (13); Transmembrane (12) TRANSMEM 22 42 Helical. {ECO:0000255}.; TRANSMEM 151 171 Helical. {ECO:0000255}.; TRANSMEM 178 198 Helical. {ECO:0000255}.; TRANSMEM 212 231 Helical. {ECO:0000255}.; TRANSMEM 239 259 Helical. {ECO:0000255}.; TRANSMEM 264 284 Helical. {ECO:0000255}.; TRANSMEM 349 369 Helical. {ECO:0000255}.; TRANSMEM 378 398 Helical. {ECO:0000255}.; TRANSMEM 404 424 Helical. {ECO:0000255}.; TRANSMEM 430 452 Helical. {ECO:0000255}.; TRANSMEM 466 486 Helical. {ECO:0000255}.; TRANSMEM 494 514 Helical. {ECO:0000255}. TOPO_DOM 1 21 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 43 150 Extracellular. {ECO:0000255}.; TOPO_DOM 172 177 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 199 211 Extracellular. {ECO:0000255}.; TOPO_DOM 232 238 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 260 263 Extracellular. {ECO:0000255}.; TOPO_DOM 285 348 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 370 377 Extracellular. {ECO:0000255}.; TOPO_DOM 399 403 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 425 429 Extracellular. {ECO:0000255}.; TOPO_DOM 453 465 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 487 493 Extracellular. {ECO:0000255}.; TOPO_DOM 515 556 Cytoplasmic. {ECO:0000255}. FUNCTION: Translocates a broad array of organic cations with various structures and molecular weights including the model compounds 1-methyl-4-phenylpyridinium (MPP), tetraethylammonium (TEA), N-1-methylnicotinamide (NMN), 4-(4-(dimethylamino)styryl)-N-methylpyridinium (ASP), the endogenous compounds choline, guanidine, histamine, epinephrine, adrenaline, noradrenaline and dopamine, and the drugs quinine, and metformin. The transport of organic cations is inhibited by a broad array of compounds like tetramethylammonium (TMA), cocaine, lidocaine, NMDA receptor antagonists, atropine, prazosin, cimetidine, TEA and NMN, guanidine, cimetidine, choline, procainamide, quinine, tetrabutylammonium, and tetrapentylammonium. Translocates organic cations in an electrogenic and pH-independent manner. Translocates organic cations across the plasma membrane in both directions. Transports the polyamines spermine and spermidine. Transports pramipexole across the basolateral membrane of the proximal tubular epithelial cells. The choline transport is activated by MMTS. Regulated by various intracellular signaling pathways including inhibition by protein kinase A activation, and endogenously activation by the calmodulin complex, the calmodulin-dependent kinase II and LCK tyrosine kinase. {ECO:0000269|PubMed:10216142, ECO:0000269|PubMed:12176030}. PTM: Phosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Basolateral cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Highly expressed in liver, kidney and intestine. Weakly expressed in adrenals and in lacting mammary glands. {ECO:0000269|PubMed:16381671, ECO:0000269|PubMed:8854860}. +Q504N2 S22AF_MOUSE Solute carrier family 22 member 15 544 60,286 Alternative sequence (2); Chain (1); Compositional bias (1); Glycosylation (5); Sequence conflict (3); Transmembrane (12) TRANSMEM 22 42 Helical. {ECO:0000255}.; TRANSMEM 111 131 Helical. {ECO:0000255}.; TRANSMEM 141 161 Helical. {ECO:0000255}.; TRANSMEM 170 190 Helical. {ECO:0000255}.; TRANSMEM 201 221 Helical. {ECO:0000255}.; TRANSMEM 226 246 Helical. {ECO:0000255}.; TRANSMEM 303 323 Helical. {ECO:0000255}.; TRANSMEM 338 358 Helical. {ECO:0000255}.; TRANSMEM 368 388 Helical. {ECO:0000255}.; TRANSMEM 401 420 Helical. {ECO:0000255}.; TRANSMEM 433 453 Helical. {ECO:0000255}.; TRANSMEM 462 482 Helical. {ECO:0000255}. FUNCTION: Probably transports organic cations. Appears not to be the agmatine transporter. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q67BT3 S13A5_MOUSE Solute carrier family 13 member 5 (Na(+)/citrate cotransporter) (NaCT) (Sodium-coupled citrate transporter) (Sodium-dependent citrate transporter) 572 63,823 Chain (1); Glycosylation (2); Transmembrane (12) TRANSMEM 13 33 Helical. {ECO:0000255}.; TRANSMEM 53 73 Helical. {ECO:0000255}.; TRANSMEM 80 100 Helical. {ECO:0000255}.; TRANSMEM 124 144 Helical. {ECO:0000255}.; TRANSMEM 218 238 Helical. {ECO:0000255}.; TRANSMEM 255 275 Helical. {ECO:0000255}.; TRANSMEM 315 335 Helical. {ECO:0000255}.; TRANSMEM 357 377 Helical. {ECO:0000255}.; TRANSMEM 410 430 Helical. {ECO:0000255}.; TRANSMEM 443 463 Helical. {ECO:0000255}.; TRANSMEM 491 511 Helical. {ECO:0000255}.; TRANSMEM 532 552 Helical. {ECO:0000255}. FUNCTION: High-affinity sodium/citrate cotransporter that mediates citrate entry into cells. The transport process is electrogenic; it is the trivalent form of citrate rather than the divalent form that is recognized as a substrate. May facilitate the utilization of circulating citrate for the generation of metabolic energy and for the synthesis of fatty acids and cholesterol (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Cell membrane {ECO:0000250|UniProtKB:Q86YT5}. +Q8R139 S29A4_MOUSE Equilibrative nucleoside transporter 4 (Solute carrier family 29 member 4) 528 58,099 Chain (1); Compositional bias (1); Glycosylation (1); Topological domain (11); Transmembrane (10) TRANSMEM 69 89 Helical. {ECO:0000255}.; TRANSMEM 102 122 Helical. {ECO:0000255}.; TRANSMEM 140 160 Helical. {ECO:0000255}.; TRANSMEM 167 187 Helical. {ECO:0000255}.; TRANSMEM 232 252 Helical. {ECO:0000255}.; TRANSMEM 347 367 Helical. {ECO:0000255}.; TRANSMEM 377 397 Helical. {ECO:0000255}.; TRANSMEM 412 432 Helical. {ECO:0000255}.; TRANSMEM 446 466 Helical. {ECO:0000255}.; TRANSMEM 482 504 Helical. {ECO:0000255}. TOPO_DOM 1 68 Extracellular. {ECO:0000255}.; TOPO_DOM 90 101 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 123 139 Extracellular. {ECO:0000255}.; TOPO_DOM 161 166 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 188 231 Extracellular. {ECO:0000255}.; TOPO_DOM 253 346 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 368 376 Extracellular. {ECO:0000255}.; TOPO_DOM 398 411 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 433 445 Extracellular. {ECO:0000255}.; TOPO_DOM 467 481 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 505 528 Extracellular. {ECO:0000255}. FUNCTION: Functions as a polyspecific organic cation transporter, efficiently transporting many organic cations such as monoamine neurotransmitters 1-methyl-4-phenylpyridinium and biogenic amines including serotonin, dopamine, norepinephrine and epinephrine. May play a role in regulating central nervous system homeostasis of monoamine neurotransmitters. May be involved in luminal transport of organic cations in the kidney and seems to use luminal proton gradient to drive organic cation reabsorptprev reabsorption. Does not seem to transport nucleoside and nucleoside analogs such as uridine, cytidine, thymidine, adenosine, inosine, guanosine, and azidothymidine. In (PubMed:16873718) adenosine is efficiently transported but in a fashion highly sensitive to extracellular pH, with maximal activity in the pH range 5.5 to 6.5. Glu-206 is essential for the cation selectivity and may function as the charge sensor for cationic substrates. Transport is chloride and sodium-independent but appears to be sensitive to changes in membrane potential. Weakly inhibited by the classical inhibitors of equilibrative nucleoside transport, dipyridamole, dilazep, and nitrobenzylthioinosine. May play a role in the regulation of extracellular adenosine concentrations in cardiac tissues, in particular during ischemia (By similarity). {ECO:0000250, ECO:0000269|PubMed:16873718}. PTM: N-glycosylated. {ECO:0000269|PubMed:16873718}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Apical cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Located to the plasma membranes of ventricular myocytes and vascular endothelial cells. Targeted to the apical membranes of differentiated kidney epithelial cells (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in heart. {ECO:0000269|PubMed:16873718}. +Q9D5K4 S1PBP_MOUSE S100P-binding protein 396 44,473 Alternative sequence (7); Chain (1); Sequence conflict (3) SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96BU1}. Note=Colocalizes with S100P in the nucleus. {ECO:0000250|UniProtKB:Q96BU1}. SUBUNIT: Interacts with S100P. {ECO:0000250|UniProtKB:Q96BU1}. +Q02614 S30BP_MOUSE SAP30-binding protein (Transcriptional regulator protein HCNGP) 308 33,832 Chain (1); Compositional bias (1); Cross-link (4); Modified residue (5); Sequence conflict (2) FUNCTION: Induces cell death. May act as a transcriptional corepressor of a gene related to cell survival (By similarity). May be involved in the regulation of beta-2-microglobulin genes. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:1459361}. SUBUNIT: Interacts with SAP30. {ECO:0000250}. +O08530 S1PR1_MOUSE Sphingosine 1-phosphate receptor 1 (S1P receptor 1) (S1P1) (Endothelial differentiation G-protein coupled receptor 1) (Lysophospholipid receptor B1) (Sphingosine 1-phosphate receptor Edg-1) (S1P receptor Edg-1) (CD antigen CD363) 382 42,639 Chain (1); Disulfide bond (2); Glycosylation (1); Initiator methionine (1); Lipidation (1); Modified residue (5); Region (2); Sequence conflict (4); Topological domain (8); Transmembrane (7) TRANSMEM 47 68 Helical; Name=1. {ECO:0000250}.; TRANSMEM 83 104 Helical; Name=2. {ECO:0000250}.; TRANSMEM 117 138 Helical; Name=3. {ECO:0000250}.; TRANSMEM 161 182 Helical; Name=4. {ECO:0000250}.; TRANSMEM 197 224 Helical; Name=5. {ECO:0000250}.; TRANSMEM 258 278 Helical; Name=6. {ECO:0000250}.; TRANSMEM 290 310 Helical; Name=7. {ECO:0000250}. TOPO_DOM 2 46 Extracellular. {ECO:0000250}.; TOPO_DOM 69 82 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 105 116 Extracellular. {ECO:0000250}.; TOPO_DOM 139 160 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 183 196 Extracellular. {ECO:0000250}.; TOPO_DOM 225 257 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 279 289 Extracellular. {ECO:0000250}.; TOPO_DOM 311 382 Cytoplasmic. {ECO:0000250}. FUNCTION: G-protein coupled receptor for the bioactive lysosphingolipid sphingosine 1-phosphate (S1P) that seems to be coupled to the G(i) subclass of heteromeric G proteins. Signaling leads to the activation of RAC1, SRC, PTK2/FAK1 and MAP kinases. Plays an important role in cell migration, probably via its role in the reorganization of the actin cytoskeleton and the formation of lamellipodia in response to stimuli that increase the activity of the sphingosine kinase SPHK1. Required for normal chemotaxis toward sphingosine 1-phosphate. Required for normal embryonic heart development and normal cardiac morphogenesis. Plays an important role in the regulation of sprouting angiogenesis and vascular maturation. Inhibits sprouting angiogenesis to prevent excessive sprouting during blood vessel development. Required for normal egress of mature T-cells from the thymus into the blood stream and into peripheral lymphoid organs. Plays a role in the migration of osteoclast precursor cells, the regulation of bone mineralization and bone homeostasis. Plays a role in responses to oxidized 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphocholine by pulmonary endothelial cells and in the protection against ventilator-induced lung injury. {ECO:0000269|PubMed:11032855, ECO:0000269|PubMed:11230698, ECO:0000269|PubMed:11726541, ECO:0000269|PubMed:12869509, ECO:0000269|PubMed:14732704, ECO:0000269|PubMed:14737169, ECO:0000269|PubMed:19204730, ECO:0000269|PubMed:19286607, ECO:0000269|PubMed:21668976, ECO:0000269|PubMed:22951644}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Endosome {ECO:0000250}. Membrane, caveola {ECO:0000250}. Note=Recruited to caveolin-enriched plasma membrane microdomains in response to oxidized 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphocholine. Ligand binding leads to receptor internalization (By similarity). {ECO:0000250}. SUBUNIT: Interacts with GNAI1 and GNAI3. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in a wide variety of tissues with highest levels in brain, heart and spleen. Lower levels found in kidney, liver, lung, muscle, placenta, thymus, and uterus. Very low levels in intestine, stomach and testis. According to PubMed:9931453, expressed modestly in apparent endothelial cells surrounding some blood vessels (e.g. aortic trunk). {ECO:0000269|PubMed:11032855, ECO:0000269|PubMed:9931453}. +Q80UJ1 S22AK_MOUSE Solute carrier family 22 member 20 (Organic anion transporter 6) 556 60,944 Chain (1); Glycosylation (4); Topological domain (13); Transmembrane (12) TRANSMEM 16 36 Helical. {ECO:0000255}.; TRANSMEM 138 158 Helical. {ECO:0000255}.; TRANSMEM 167 187 Helical. {ECO:0000255}.; TRANSMEM 195 215 Helical. {ECO:0000255}.; TRANSMEM 226 246 Helical. {ECO:0000255}.; TRANSMEM 251 271 Helical. {ECO:0000255}.; TRANSMEM 340 360 Helical. {ECO:0000255}.; TRANSMEM 367 387 Helical. {ECO:0000255}.; TRANSMEM 398 418 Helical. {ECO:0000255}.; TRANSMEM 426 446 Helical. {ECO:0000255}.; TRANSMEM 458 478 Helical. {ECO:0000255}.; TRANSMEM 486 506 Helical. {ECO:0000255}. TOPO_DOM 1 15 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 37 137 Extracellular. {ECO:0000255}.; TOPO_DOM 159 166 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 188 194 Extracellular. {ECO:0000255}.; TOPO_DOM 216 225 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 247 250 Extracellular. {ECO:0000255}.; TOPO_DOM 272 339 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 361 366 Extracellular. {ECO:0000255}.; TOPO_DOM 388 397 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 419 425 Extracellular. {ECO:0000255}.; TOPO_DOM 447 457 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 479 485 Extracellular. {ECO:0000255}.; TOPO_DOM 507 556 Cytoplasmic. {ECO:0000255}. FUNCTION: Organic anion transporter that mediates the uptake of estrone sulfate. Inhibited by probenecid, propionate, 2-methylbutyrate, 3-methylbutyrate, benzoate, heptanoate and 2-ethylhaxanoate. May act as an odorant transporter. {ECO:0000269|PubMed:16478971, ECO:0000269|PubMed:17094945}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Highly expressed in olfactory mucosa. Weakly expressed in testis. Not detected in heart, spleen, lung, kidney or brain. {ECO:0000269|PubMed:15369770, ECO:0000269|PubMed:17094945}. +Q8VCX2 S35C2_MOUSE Solute carrier family 35 member C2 (Ovarian cancer-overexpressed gene 1 protein) 364 40,302 Chain (1); Glycosylation (1); Modified residue (2); Transmembrane (9) TRANSMEM 14 34 Helical. {ECO:0000255}.; TRANSMEM 42 62 Helical. {ECO:0000255}.; TRANSMEM 104 124 Helical. {ECO:0000255}.; TRANSMEM 136 156 Helical. {ECO:0000255}.; TRANSMEM 166 186 Helical. {ECO:0000255}.; TRANSMEM 202 222 Helical. {ECO:0000255}.; TRANSMEM 238 258 Helical. {ECO:0000255}.; TRANSMEM 272 292 Helical. {ECO:0000255}.; TRANSMEM 295 315 Helical. {ECO:0000255}. FUNCTION: May play an important role in the cellular response to tissue hypoxia. May be either a GDP-fucose transporter that competes with SLC35C1 for GDP-fucose, or a factor that otherwise enhances the fucosylation of Notch and is required for optimal Notch signaling in mammalian cells (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Golgi apparatus, cis-Golgi network membrane {ECO:0000250}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250}. +Q3UHH2 S22AN_MOUSE Solute carrier family 22 member 23 689 74,325 Alternative sequence (2); Chain (1); Glycosylation (2); Sequence conflict (2); Transmembrane (10) TRANSMEM 229 249 Helical. {ECO:0000255}.; TRANSMEM 253 273 Helical. {ECO:0000255}.; TRANSMEM 283 303 Helical. {ECO:0000255}.; TRANSMEM 310 330 Helical. {ECO:0000255}.; TRANSMEM 339 359 Helical. {ECO:0000255}.; TRANSMEM 466 486 Helical. {ECO:0000255}.; TRANSMEM 489 509 Helical. {ECO:0000255}.; TRANSMEM 541 561 Helical. {ECO:0000255}.; TRANSMEM 572 592 Helical. {ECO:0000255}.; TRANSMEM 601 621 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q5HZI9 S2551_MOUSE Solute carrier family 25 member 51 (Mitochondrial carrier triple repeat protein 1) 298 33,689 Chain (1); Erroneous initiation (6); Repeat (3); Sequence conflict (1); Transmembrane (6) TRANSMEM 36 56 Helical; Name=1. {ECO:0000255}.; TRANSMEM 85 105 Helical; Name=2. {ECO:0000255}.; TRANSMEM 119 139 Helical; Name=3. {ECO:0000255}.; TRANSMEM 180 200 Helical; Name=4. {ECO:0000255}.; TRANSMEM 216 236 Helical; Name=5. {ECO:0000255}.; TRANSMEM 269 290 Helical; Name=6. {ECO:0000255}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q6PGC7 S35E3_MOUSE Solute carrier family 35 member E3 313 34,892 Chain (1); Transmembrane (9) TRANSMEM 17 37 Helical. {ECO:0000255}.; TRANSMEM 40 60 Helical. {ECO:0000255}.; TRANSMEM 71 91 Helical. {ECO:0000255}.; TRANSMEM 126 146 Helical. {ECO:0000255}.; TRANSMEM 154 174 Helical. {ECO:0000255}.; TRANSMEM 187 206 Helical. {ECO:0000255}.; TRANSMEM 225 245 Helical. {ECO:0000255}.; TRANSMEM 252 272 Helical. {ECO:0000255}.; TRANSMEM 275 295 Helical. {ECO:0000255}. FUNCTION: Putative transporter. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q60850 S23A3_MOUSE Solute carrier family 23 member 3 (Na(+)/L-ascorbic acid transporter 3) (Sodium-dependent vitamin C transporter 3) (Yolk sac permease-like molecule 1) (YSPL-1) 611 64,878 Alternative sequence (3); Chain (1); Frameshift (1); Sequence conflict (6); Topological domain (13); Transmembrane (12) TRANSMEM 53 73 Helical. {ECO:0000255}.; TRANSMEM 89 109 Helical. {ECO:0000255}.; TRANSMEM 169 189 Helical. {ECO:0000255}.; TRANSMEM 192 212 Helical. {ECO:0000255}.; TRANSMEM 216 236 Helical. {ECO:0000255}.; TRANSMEM 270 290 Helical. {ECO:0000255}.; TRANSMEM 320 340 Helical. {ECO:0000255}.; TRANSMEM 359 379 Helical. {ECO:0000255}.; TRANSMEM 398 417 Helical. {ECO:0000255}.; TRANSMEM 427 449 Helical. {ECO:0000255}.; TRANSMEM 456 475 Helical. {ECO:0000255}.; TRANSMEM 490 510 Helical. {ECO:0000255}. TOPO_DOM 1 52 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 74 88 Extracellular. {ECO:0000255}.; TOPO_DOM 110 168 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 190 191 Extracellular. {ECO:0000255}.; TOPO_DOM 213 215 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 237 269 Extracellular. {ECO:0000255}.; TOPO_DOM 291 319 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 341 358 Extracellular. {ECO:0000255}.; TOPO_DOM 380 397 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 418 426 Extracellular. {ECO:0000255}.; TOPO_DOM 450 455 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 476 489 Extracellular. {ECO:0000255}.; TOPO_DOM 511 611 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: Isoform 4: Cytoplasm. +Q6NZC7 S23IP_MOUSE SEC23-interacting protein 998 110,780 Chain (1); Compositional bias (1); Domain (2); Modified residue (4); Region (1); Sequence caution (1) FUNCTION: Plays a role in the organization of endoplasmic reticulum exit sites. Specifically binds to phosphatidylinositol 3-phosphate (PI(3)P), phosphatidylinositol 4-phosphate (PI(4)P) and phosphatidylinositol 5-phosphate (PI(5)P). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endoplasmic reticulum {ECO:0000305}. SUBUNIT: Interacts with SEC23A. {ECO:0000250}. +G3UVW3 S38A6_MOUSE Probable sodium-coupled neutral amino acid transporter 6 (Na(+)-coupled neutral amino acid transporter 6) (Solute carrier family 38 member 6) 457 50,253 Chain (1); Disulfide bond (1); Modified residue (3); Sequence conflict (2); Transmembrane (11) TRANSMEM 48 68 Helical. {ECO:0000255}.; TRANSMEM 70 90 Helical. {ECO:0000255}.; TRANSMEM 112 132 Helical. {ECO:0000255}.; TRANSMEM 171 191 Helical. {ECO:0000255}.; TRANSMEM 192 212 Helical. {ECO:0000255}.; TRANSMEM 251 271 Helical. {ECO:0000255}.; TRANSMEM 289 309 Helical. {ECO:0000255}.; TRANSMEM 328 348 Helical. {ECO:0000255}.; TRANSMEM 372 392 Helical. {ECO:0000255}.; TRANSMEM 395 415 Helical. {ECO:0000255}.; TRANSMEM 432 452 Helical. {ECO:0000255}. FUNCTION: Probable sodium-dependent amino acid/proton antiporter, could be a neuronal transporter for glutamate. {ECO:0000305|PubMed:24752331}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24752331}; Multi-pass membrane protein {ECO:0000255}. Note=Colocalizes with synaptotagmins and SNAP25. {ECO:0000269|PubMed:24752331}. TISSUE SPECIFICITY: Expressed exclusively in neurons and not in astrocytes and glia cells. Highly expressed in the synapse. Highly expressed in glutamatergic neurons. Primarily expressed in excitatory neurons, with some minor expression in inhibitory neurons. {ECO:0000269|PubMed:24752331}. +Q62273 S26A2_MOUSE Sulfate transporter (Diastrophic dysplasia protein homolog) (ST-OB) (Solute carrier family 26 member 2) 739 81,604 Chain (1); Domain (1); Glycosylation (2); Modified residue (1); Sequence conflict (1); Transmembrane (8) TRANSMEM 112 132 Helical. {ECO:0000255}.; TRANSMEM 137 157 Helical. {ECO:0000255}.; TRANSMEM 227 247 Helical. {ECO:0000255}.; TRANSMEM 255 275 Helical. {ECO:0000255}.; TRANSMEM 378 398 Helical. {ECO:0000255}.; TRANSMEM 420 440 Helical. {ECO:0000255}.; TRANSMEM 455 475 Helical. {ECO:0000255}.; TRANSMEM 524 544 Helical. {ECO:0000255}. FUNCTION: Sulfate transporter. May play a role in endochondral bone formation. {ECO:0000250|UniProtKB:P50443}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P50443}; Multi-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Distributed mainly in the thymus, testis and osteoblastic cells. +Q9Z0U9 S1PR3_MOUSE Sphingosine 1-phosphate receptor 3 (S1P receptor 3) (S1P3) (Endothelial differentiation G-protein coupled receptor 3) (Lysophospholipid receptor B3) (Sphingosine 1-phosphate receptor Edg-3) (S1P receptor Edg-3) 378 42,270 Chain (1); Glycosylation (1); Modified residue (1); Sequence conflict (1); Topological domain (8); Transmembrane (7) TRANSMEM 45 65 Helical; Name=1. {ECO:0000250}.; TRANSMEM 75 95 Helical; Name=2. {ECO:0000250}.; TRANSMEM 116 136 Helical; Name=3. {ECO:0000250}.; TRANSMEM 155 175 Helical; Name=4. {ECO:0000250}.; TRANSMEM 197 217 Helical; Name=5. {ECO:0000250}.; TRANSMEM 245 265 Helical; Name=6. {ECO:0000250}.; TRANSMEM 282 302 Helical; Name=7. {ECO:0000250}. TOPO_DOM 1 44 Extracellular. {ECO:0000250}.; TOPO_DOM 66 74 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 96 115 Extracellular. {ECO:0000250}.; TOPO_DOM 137 154 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 176 196 Extracellular. {ECO:0000250}.; TOPO_DOM 218 244 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 266 281 Extracellular. {ECO:0000250}.; TOPO_DOM 303 378 Cytoplasmic. {ECO:0000250}. FUNCTION: Receptor for the lysosphingolipid sphingosine 1-phosphate (S1P). S1P is a bioactive lysophospholipid that elicits diverse physiological effect on most types of cells and tissues. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Most abundant in heart, lung, kidney and spleen; low but detectable in brain, thymus, muscle and testis; and nearly undetectable in liver, stomach, and intestine. Expressed in embryonic lung from embryonic day 14-18. Also abundantly detected in embryonic nasal cartilage, sphenoid bone, vena cava, Meckel's cartilage/incisor teeth, genital tubercle and bladder. {ECO:0000269|PubMed:9931453}. +Q8BY79 S35G1_MOUSE Solute carrier family 35 member G1 (Transmembrane protein 20) 368 40,217 Chain (1); Domain (2); Transmembrane (10) TRANSMEM 72 92 Helical. {ECO:0000255}.; TRANSMEM 100 120 Helical. {ECO:0000255}.; TRANSMEM 134 154 Helical. {ECO:0000255}.; TRANSMEM 161 181 Helical. {ECO:0000255}.; TRANSMEM 190 210 Helical. {ECO:0000255}.; TRANSMEM 225 245 Helical. {ECO:0000255}.; TRANSMEM 256 276 Helical. {ECO:0000255}.; TRANSMEM 289 309 Helical. {ECO:0000255}.; TRANSMEM 316 336 Helical. {ECO:0000255}.; TRANSMEM 340 360 Helical. {ECO:0000255}. FUNCTION: May play a role in intracellular calcium sensing and homeostasis. May act as a negative regulator of plasma membrane calcium-transporting ATPases preventing calcium efflux from the cell (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Translocates from the endoplasmic reticulum to the cell membrane in response to a depletion of intracellular calcium and is detected at punctae corresponding to junctions between the endoplasmic reticulum and the cell membrane. {ECO:0000250}. SUBUNIT: Interacts with STIM1; stimulated by depletion of intracellular calcium. Interacts with ORAI1. Interacts with the plasma membrane calcium-transporting ATPases ATP2B1 and ATP2B4. Interacts with ATP1A1, ATP2A2, KPNB1 and XPO1 (By similarity). {ECO:0000250}. +Q31125 S39A7_MOUSE Zinc transporter SLC39A7 (Histidine-rich membrane protein Ke4) (Solute carrier family 39 member 7) (Zrt-, Irt-like protein 7) (ZIP7) 476 50,657 Chain (1); Compositional bias (2); Frameshift (1); Modified residue (1); Sequence conflict (3); Transmembrane (6) TRANSMEM 7 27 Helical. {ECO:0000255}.; TRANSMEM 146 166 Helical. {ECO:0000255}.; TRANSMEM 177 197 Helical. {ECO:0000255}.; TRANSMEM 222 242 Helical. {ECO:0000255}.; TRANSMEM 393 413 Helical. {ECO:0000255}.; TRANSMEM 417 437 Helical. {ECO:0000255}. FUNCTION: Zinc transporter, that transports Zn(2+) from the endoplasmic reticulum/Golgi apparatus to the cytosol. {ECO:0000269|PubMed:15705588}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Golgi apparatus, cis-Golgi network membrane {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15705588, ECO:0000269|PubMed:2294398}. +P31649 S6A13_MOUSE Sodium- and chloride-dependent GABA transporter 2 (GAT-2) (Sodium- and chloride-dependent GABA transporter 3) (GAT-3) (Solute carrier family 6 member 13) 602 68,285 Chain (1); Disulfide bond (1); Glycosylation (4); Modified residue (2); Topological domain (3); Transmembrane (12) TRANSMEM 41 61 Helical; Name=1. {ECO:0000255}.; TRANSMEM 68 88 Helical; Name=2. {ECO:0000255}.; TRANSMEM 121 141 Helical; Name=3. {ECO:0000255}.; TRANSMEM 207 227 Helical; Name=4. {ECO:0000255}.; TRANSMEM 233 253 Helical; Name=5. {ECO:0000255}.; TRANSMEM 282 302 Helical; Name=6. {ECO:0000255}.; TRANSMEM 319 339 Helical; Name=7. {ECO:0000255}.; TRANSMEM 366 386 Helical; Name=8. {ECO:0000255}.; TRANSMEM 418 438 Helical; Name=9. {ECO:0000255}.; TRANSMEM 453 473 Helical; Name=10. {ECO:0000255}.; TRANSMEM 490 510 Helical; Name=11. {ECO:0000255}.; TRANSMEM 528 548 Helical; Name=12. {ECO:0000255}. TOPO_DOM 1 40 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 142 206 Extracellular. {ECO:0000255}.; TOPO_DOM 549 602 Cytoplasmic. {ECO:0000255}. FUNCTION: Sodium-dependent GABA and taurine transporter. In presynaptic terminals, regulates GABA signaling termination through GABA uptake. In the liver, may be the major contributor for GABA uptake. Also involved in beta-alanine transport. {ECO:0000269|PubMed:22896705}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22896705}; Multi-pass membrane protein {ECO:0000269|PubMed:22896705}. Note=In the kidney, detected at the basolateral membranes of parts of proximal tubules. TISSUE SPECIFICITY: Expressed at high levels in liver, followed by kidney and leptomeninges, and very low levels in the cerebellum (at protein level).In the brain, detected in some blood vessels (at protein level). In the kidney, expressed in the cortex, including parts of the proximal tubules, but not in the medulla (at protein level). In the liver, highest expression in periportal hepatocytes, with highest density at the vascular side (at protein level). Also detected at low levels in other organs, including skeletal muscle. {ECO:0000269|PubMed:22896705}. +Q8JZR6 S4A8_MOUSE Electroneutral sodium bicarbonate exchanger 1 (Electroneutral Na+-driven Cl-HCO3 exchanger) (Solute carrier family 4 member 8) (k-NBC3) 1089 122,421 Alternative sequence (1); Chain (1); Compositional bias (1); Disulfide bond (2); Erroneous initiation (1); Sequence conflict (7); Topological domain (12); Transmembrane (11) TRANSMEM 477 497 Helical. {ECO:0000255}.; TRANSMEM 506 526 Helical. {ECO:0000255}.; TRANSMEM 564 584 Helical. {ECO:0000255}.; TRANSMEM 594 614 Helical. {ECO:0000255}.; TRANSMEM 686 706 Helical. {ECO:0000255}.; TRANSMEM 730 750 Helical. {ECO:0000255}.; TRANSMEM 777 797 Helical. {ECO:0000255}.; TRANSMEM 823 843 Helical. {ECO:0000255}.; TRANSMEM 880 900 Helical. {ECO:0000255}.; TRANSMEM 903 923 Helical. {ECO:0000255}.; TRANSMEM 961 981 Helical. {ECO:0000255}. TOPO_DOM 1 476 Extracellular. {ECO:0000255}.; TOPO_DOM 498 505 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 527 563 Extracellular. {ECO:0000255}.; TOPO_DOM 585 593 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 615 685 Extracellular. {ECO:0000255}.; TOPO_DOM 707 729 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 751 776 Extracellular. {ECO:0000255}.; TOPO_DOM 798 822 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 844 879 Extracellular. {ECO:0000255}.; TOPO_DOM 901 902 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 924 960 Extracellular. {ECO:0000255}.; TOPO_DOM 982 1089 Cytoplasmic. {ECO:0000255}. FUNCTION: Mediates electroneutral sodium- and carbonate-dependent chloride-HCO3(-) exchange with a Na(+):HCO3(-) stoichiometry of 2:1. Plays a major role in pH regulation in neurons. May be involved in cell pH regulation by transporting HCO3(-) from blood to cell. Enhanced expression in severe acid stress could be important for cell survival by mediating the influx of HCO3(-) into the cells. Also mediates lithium-dependent HCO3(-) cotransport. May be regulated by osmolarity. {ECO:0000269|PubMed:11260402}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11260402}; Multi-pass membrane protein {ECO:0000269|PubMed:11260402}. TISSUE SPECIFICITY: Highly expressed in brain with lower levels in lung, kidney and heart. In the kidney, there is high expression in the inner medulla, localized to the inner medullary collecting duct. In the brain, there seems to be three transcripts each having a different expression pattern. The smaller 3kb transcript has highest expression levels in the thalamus and the largest 9.5kb transcript has highest levels in the substantia nigra. The middle transcript of 4.4kb, which is also the main transcript in kidney, is highly expressed in thalamus. Hence, the highest levels are observed in the thalamus, amygdala and caudate nucleus and very low expression was seen in the corpus callosum. {ECO:0000269|PubMed:11260402}. +P59808 SASH1_MOUSE SAM and SH3 domain-containing protein 1 1230 135,591 Chain (1); Compositional bias (1); Domain (3); Modified residue (5) FUNCTION: May have a role in a signaling pathway. Could act as a tumor suppressor. +Q99LB7 SARDH_MOUSE Sarcosine dehydrogenase, mitochondrial (SarDH) (EC 1.5.8.3) 919 101,682 Chain (1); Modified residue (17); Transit peptide (1) Amine and polyamine degradation; sarcosine degradation; formaldehyde and glycine from sarcosine: step 1/1. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. +Q8BX22 SALL4_MOUSE Sal-like protein 4 (Zinc finger protein SALL4) 1067 113,110 Alternative sequence (2); Chain (1); Compositional bias (1); Cross-link (19); Modified residue (5); Sequence conflict (8); Zinc finger (7) FUNCTION: Transcription factor with a key role in the maintenance and self-renewal of embryonic and hematopoietic stem cells. {ECO:0000250}. PTM: Sumoylation with both SUMO1 and SUMO2 regulates the stability, subcellular localization, transcriptional activity, and may reduce interaction with POU5F1/OCT4. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Interacts with POU5F1/OCT4 (By similarity). Interacts with NANOG. Interacts with BEND3. {ECO:0000250, ECO:0000250|UniProtKB:Q9UJQ4, ECO:0000269|PubMed:16840789}. +Q8K070 SAM14_MOUSE Sterile alpha motif domain-containing protein 14 (SAM domain-containing protein 14) 417 45,102 Chain (1); Coiled coil (1); Compositional bias (1); Domain (1); Frameshift (2); Modified residue (6); Sequence conflict (2) +F6XZJ7 SAM15_MOUSE Sterile alpha motif domain-containing protein 15 (SAM domain-containing protein 15) 620 70,457 Chain (1); Domain (1) +Q8R3Q0 SARAF_MOUSE Store-operated calcium entry-associated regulatory factor (SARAF) (SOCE-associated regulatory factor) (Transmembrane protein 66) 334 35,856 Chain (1); Erroneous initiation (7); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 169 189 Helical. {ECO:0000255}. TOPO_DOM 32 168 Lumenal. {ECO:0000255}.; TOPO_DOM 190 334 Cytoplasmic. {ECO:0000255}. FUNCTION: Negative regulator of store-operated Ca(2+) entry (SOCE) involved in protecting cells from Ca(2+) overfilling. In response to cytosolic Ca(2+) elevation after endoplasmic reticulum Ca(2+) refilling, promotes a slow inactivation of STIM (STIM1 or STIM2)-dependent SOCE activity: possibly act by facilitating the deoligomerization of STIM to efficiently turn off ORAI when the endoplasmic reticulum lumen is filled with the appropriate Ca(2+) levels, and thus preventing the overload of the cell with excessive Ca(2+) ions (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Translocates to the endoplasmic reticulum-plasma membrane (ER-PM) region in a STIM1-dependent manner following cytosolic Ca(2+) elevation. {ECO:0000250}. SUBUNIT: Interacts with STIM1. {ECO:0000250}. DOMAIN: The cytoplasmic C-terminal region mediates interaction with STIM1, while the N-terminal lumenal region mediates regulation of SOCE activity. {ECO:0000250}. +Q8BGH2 SAM50_MOUSE Sorting and assembly machinery component 50 homolog 469 51,864 Chain (1); Domain (1); Modified residue (1); Sequence conflict (3) FUNCTION: Plays a crucial role in the maintenance of the structure of mitochondrial cristae and the proper assembly of the mitochondrial respiratory chain complexes. Required for the assembly of TOMM40 into the TOM complex. {ECO:0000250|UniProtKB:Q9Y512}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q9Y512}; Multi-pass membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250|UniProtKB:Q6AXV4}. Mitochondrion {ECO:0000250|UniProtKB:Q9Y512}. SUBUNIT: Associates with the mitochondrial contact site and cristae organizing system (MICOS) complex, composed of at least MINOS1/MIC10, CHCHD3/MIC19, CHCHD6/MIC25, APOOL/MIC27, IMMT/MIC60, APOO/MIC23/MIC26 and QIL1/MIC13. This complex was also known under the names MINOS or MitOS complex. The MICOS complex associates with mitochondrial outer membrane proteins SAMM50, MTX1 and MTX2 (together described as components of the mitochondrial outer membrane sorting assembly machinery (SAM) complex) and DNAJC11, mitochondrial inner membrane protein TMEM11 and with HSPA9. The MICOS and SAM complexes together with DNAJC11 are part of a large protein complex spanning both membranes termed the mitochondrial intermembrane space bridging (MIB) complex. Interacts with IMMT/MIC60 (By similarity). Interacts with CHCHD3/MIC19. {ECO:0000250|UniProtKB:Q9Y512, ECO:0000269|PubMed:21081504}. DOMAIN: Its C-terminal part seems to contain many membrane-spanning sided beta-sheets, that have the potential to adopt a transmembrane beta-barrel type structure. {ECO:0000250}. +O35874 SATT_MOUSE Neutral amino acid transporter A (Alanine/serine/cysteine/threonine transporter 1) (ASCT-1) (SATT) (Solute carrier family 1 member 4) 532 56,062 Chain (1); Glycosylation (2); Modified residue (4); Topological domain (2); Transmembrane (9) TRANSMEM 42 62 Helical. {ECO:0000255}.; TRANSMEM 88 108 Helical. {ECO:0000255}.; TRANSMEM 119 139 Helical. {ECO:0000255}.; TRANSMEM 217 237 Helical. {ECO:0000255}.; TRANSMEM 257 277 Helical. {ECO:0000255}.; TRANSMEM 298 318 Helical. {ECO:0000255}.; TRANSMEM 328 348 Helical. {ECO:0000255}.; TRANSMEM 373 393 Helical. {ECO:0000255}.; TRANSMEM 418 438 Helical. {ECO:0000255}. TOPO_DOM 1 41 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 140 216 Extracellular. {ECO:0000255}. FUNCTION: Transporter for alanine, serine, cysteine, and threonine. Exhibits sodium dependence (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Melanosome {ECO:0000250}. +Q6PDS3 SARM1_MOUSE Sterile alpha and TIR motif-containing protein 1 (Tir-1 homolog) (MyD88-5) 724 79,606 Alternative sequence (4); Chain (1); Domain (3); Erroneous gene model prediction (1); Erroneous initiation (1); Modified residue (2); Sequence conflict (1); Transit peptide (1) FUNCTION: Negative regulator of MYD88- and TRIF-dependent toll-like receptor signaling pathway which plays a pivotal role in activating axonal degeneration following injury. Promotes Wallerian degeneration an injury-induced axonal death pathway which involves degeneration of an axon distal to the injury site. Can activate neuronal death in response to stress. Regulates dendritic arborization through the MAPK4-JNK pathway. Involved in innate immune response. Inhibits both TICAM1/TRIF- and MYD88-dependent activation of JUN/AP-1, TRIF-dependent activation of NF-kappa-B and IRF3, and the phosphorylation of MAPK14/p38. Can restrict West Nile virus (WNV) pathogenesis. {ECO:0000269|PubMed:17724133, ECO:0000269|PubMed:19587044, ECO:0000269|PubMed:21555464, ECO:0000269|PubMed:22678360}. SUBCELLULAR LOCATION: Cytoplasm. Cell projection, axon. Cell projection, dendrite. Cell junction, synapse. Mitochondrion. Note=Associated with microtubules. SUBUNIT: Interacts with TICAM1/TRIF and thereby interferes with TICAM1/TRIF function (By similarity). Interacts with SDC2 (via cytoplasmic domain) and MAPK10/JNK3. {ECO:0000250, ECO:0000269|PubMed:17724133, ECO:0000269|PubMed:21555464}. TISSUE SPECIFICITY: Widely expressed in the brain and neurons (at protein level). {ECO:0000269|PubMed:21555464}. +Q9D1J3 SARNP_MOUSE SAP domain-containing ribonucleoprotein (Nuclear protein Hcc-1) 210 23,533 Chain (1); Domain (1); Initiator methionine (1); Modified residue (4) FUNCTION: Binds both single-stranded and double-stranded DNA with higher affinity for the single-stranded form. Specifically binds to scaffold/matrix attachment region DNA. Also binds single-stranded RNA. Enhances RNA unwinding activity of DDX39A. May participate in important transcriptional or translational control of cell growth, metabolism and carcinogenesis. Component of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NFX1 pathway (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus speckle {ECO:0000250}. SUBUNIT: Interacts with DDX39A. Interacts with FUS. Component of the transcription/export (TREX) complex at least composed of ALYREF/THOC4, DDX39B, SARNP/CIP29, CHTOP and the THO subcomplex; TREX seems to have dynamic structure involving ATP-dependent remodeling; in the complex interacts directly with DDX39B in a ATP-dependent manner which bridges it to ALYREF/THOC4 (By similarity). {ECO:0000250}. +Q8R0A5 TCAL3_MOUSE Transcription elongation factor A protein-like 3 (TCEA-like protein 3) (Transcription elongation factor S-II protein-like 3) 200 22,468 Chain (1); Compositional bias (1); Modified residue (1); Sequence conflict (2) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q8VEB2 SAV1_MOUSE Protein salvador homolog 1 (45 kDa WW domain protein) (mWW45) 386 44,845 Beta strand (7); Chain (1); Coiled coil (1); Domain (3); Modified residue (3); Sequence conflict (1); Turn (4) FUNCTION: Regulator of STK3/MST2 and STK4/MST1 in the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS1/2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. SAV1 is required for STK3/MST2 and STK4/MST1 activation and promotes cell-cycle exit and terminal differentiation in developing epithelial tissues. Plays a role in centrosome disjunction by regulating the localization of NEK2 to centrosomes, and its ability to phosphorylate CROCC and CEP250. In conjunction with STK3/MST2, activates the transcriptional activity of ESR1 through the modulation of its phosphorylation (By similarity). {ECO:0000250, ECO:0000269|PubMed:18369314, ECO:0000269|PubMed:20080689}. PTM: Phosphorylated by STK3/MST2 and STK4/MST1. Phosphorylation is not required for SAV1 stability and may increase the number of protein binding sites on the scaffold molecule (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. SUBUNIT: Homodimer. Stabilized through interaction with STK3/MST2 or STK4/MST1. Interacts (via SARAH domain) with isoform 1 of NEK2. Interacts with ESR1 only in the presence of STK3/MST2. Interacts with WTIP and AJUBA. {ECO:0000250|UniProtKB:Q9H4B6}. TISSUE SPECIFICITY: Ubiquitously expressed in adult tissues with the highest level found in testis. +Q8CCT4 TCAL5_MOUSE Transcription elongation factor A protein-like 5 (TCEA-like protein 5) (Transcription elongation factor S-II protein-like 5) 200 22,038 Chain (1); Compositional bias (1); Sequence conflict (1) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +P01849 TCA_MOUSE T-cell receptor alpha chain C region 138 15,495 Beta strand (8); Chain (1); Erroneous initiation (1); Glycosylation (3); Helix (1); Natural variant (2); Non-terminal residue (1); Region (1); Topological domain (1); Transmembrane (1); Turn (1) TRANSMEM 113 133 Helical. {ECO:0000255}. TOPO_DOM 134 138 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +P01851 TCB2_MOUSE T-cell receptor beta-2 chain C region 173 19,297 Beta strand (11); Chain (1); Glycosylation (2); Helix (3); Natural variant (2); Non-terminal residue (1); Region (1); Topological domain (1); Transmembrane (1) TRANSMEM 147 168 Helical. {ECO:0000255}. TOPO_DOM 169 173 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q5SWY8 SC5AA_MOUSE Sodium/glucose cotransporter 5 (Na(+)/glucose cotransporter 5) (Solute carrier family 5 member 10) 596 64,706 Chain (1); Glycosylation (2); Modified residue (4); Topological domain (14); Transmembrane (14) TRANSMEM 16 36 Helical. {ECO:0000255}.; TRANSMEM 73 93 Helical. {ECO:0000255}.; TRANSMEM 100 120 Helical. {ECO:0000255}.; TRANSMEM 150 170 Helical. {ECO:0000255}.; TRANSMEM 174 194 Helical. {ECO:0000255}.; TRANSMEM 201 221 Helical. {ECO:0000255}.; TRANSMEM 265 285 Helical. {ECO:0000255}.; TRANSMEM 301 321 Helical. {ECO:0000255}.; TRANSMEM 356 376 Helical. {ECO:0000255}.; TRANSMEM 410 430 Helical. {ECO:0000255}.; TRANSMEM 444 464 Helical. {ECO:0000255}.; TRANSMEM 472 492 Helical. {ECO:0000255}.; TRANSMEM 514 534 Helical. {ECO:0000255}.; TRANSMEM 576 596 Helical. {ECO:0000255}. TOPO_DOM 1 15 Extracellular. {ECO:0000255}.; TOPO_DOM 37 72 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 94 99 Extracellular. {ECO:0000255}.; TOPO_DOM 121 149 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 171 173 Extracellular. {ECO:0000255}.; TOPO_DOM 195 200 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 222 264 Extracellular. {ECO:0000255}.; TOPO_DOM 286 300 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 322 355 Extracellular. {ECO:0000255}.; TOPO_DOM 377 409 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 431 443 Extracellular. {ECO:0000255}.; TOPO_DOM 465 471 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 493 513 Extracellular. {ECO:0000255}.; TOPO_DOM 535 575 Cytoplasmic. {ECO:0000255}. FUNCTION: High capacity transporter for mannose and fructose and, to a lesser extent, glucose, AMG, and galactose. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein. +P60060 SC61G_MOUSE Protein transport protein Sec61 subunit gamma 68 7,741 Chain (1); Modified residue (2); Topological domain (2); Transmembrane (1) TRANSMEM 33 61 Helical. {ECO:0000255}. TOPO_DOM 1 32 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 62 68 Extracellular. {ECO:0000255}. FUNCTION: Component of SEC61 channel-forming translocon complex that mediates transport of signal peptide-containing precursor polypeptides across endoplasmic reticulum (ER). {ECO:0000250|UniProtKB:P60058}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. SUBUNIT: The ER translocon complex consists of channel-forming core components SEC61A1, SEC61B and SEC61G and different auxiliary components such as SEC62 and SEC63. {ECO:0000250|UniProtKB:P60058}. +Q3TVW5 TCHP_MOUSE Trichoplein keratin filament-binding protein (Protein TCHP) (Mitochondrial protein with oncostatic activity) (Mitostatin) 497 60,642 Alternative sequence (1); Chain (1); Coiled coil (3); Compositional bias (1); Erroneous initiation (1); Region (2); Sequence conflict (2) FUNCTION: Tumor suppressor which has the ability to inhibit cell growth and be pro-apoptotic during cell stress. May act as a 'capping' or 'branching' protein for keratin filaments in the cell periphery. May regulate K8/K18 filament and desmosome organization mainly at the apical or peripheral regions of simple epithelial cells (By similarity). Is a negative regulator of ciliogenesis (By similarity). {ECO:0000250|UniProtKB:Q9BT92}. PTM: Ubiquitinated. Ubiquitination by the BCR(KCTD17) E3 ubiquitin ligase complex results in proteasomal degradation, and induces ciliogenesis. {ECO:0000250|UniProtKB:Q9BT92}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Mitochondrion {ECO:0000250}. SUBUNIT: Interacts specifically with keratin proteins including, KRT5, KRT6A, KRT8, KRT14, KRT16 and KRT18. Interacts with KCTD17 (By similarity). {ECO:0000250|UniProtKB:Q9BT92}. TISSUE SPECIFICITY: Expressed in all tissues examined, including brain, liver, small intestine, large intestine, lung and heart. Found concentrated in tubular structures within hepatocytes, and in the apical cortical region and desmosomes of the apical junctional domain in enterocytes of the small intestine. In the hair follicle, localized at the outer root sheath. Also expressed in blood vessels (at protein level). {ECO:0000269|PubMed:15731013}. +Q8C3K6 SC5A1_MOUSE Sodium/glucose cotransporter 1 (Na(+)/glucose cotransporter 1) (High affinity sodium-glucose cotransporter) (Solute carrier family 5 member 1) 665 73,449 Binding site (1); Chain (1); Disulfide bond (1); Glycosylation (1); Intramembrane (1); Modified residue (2); Site (3); Topological domain (14); Transmembrane (13) INTRAMEM 527 563 Helical. {ECO:0000255}. TRANSMEM 29 49 Helical. {ECO:0000255}.; TRANSMEM 65 85 Helical. {ECO:0000255}.; TRANSMEM 106 126 Helical. {ECO:0000255}.; TRANSMEM 143 163 Helical. {ECO:0000255}.; TRANSMEM 179 201 Helical. {ECO:0000255}.; TRANSMEM 209 229 Helical. {ECO:0000255}.; TRANSMEM 278 298 Helical. {ECO:0000255}.; TRANSMEM 314 334 Helical. {ECO:0000255}.; TRANSMEM 381 401 Helical. {ECO:0000255}.; TRANSMEM 424 444 Helical. {ECO:0000255}.; TRANSMEM 456 476 Helical. {ECO:0000255}.; TRANSMEM 485 505 Helical. {ECO:0000255}.; TRANSMEM 645 665 Helical. {ECO:0000255}. TOPO_DOM 1 28 Extracellular. {ECO:0000255}.; TOPO_DOM 50 64 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 86 105 Extracellular. {ECO:0000255}.; TOPO_DOM 127 142 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 164 178 Extracellular. {ECO:0000255}.; TOPO_DOM 202 208 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 230 277 Extracellular. {ECO:0000255}.; TOPO_DOM 299 313 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 335 380 Extracellular. {ECO:0000255}.; TOPO_DOM 402 423 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 445 455 Extracellular. {ECO:0000255}.; TOPO_DOM 477 484 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 506 526 Extracellular. {ECO:0000255}.; TOPO_DOM 564 644 Extracellular. {ECO:0000255}. FUNCTION: Actively transports glucose into cells by Na(+) cotransport with a Na(+) to glucose coupling ratio of 2:1. Efficient substrate transport in mammalian kidney is provided by the concerted action of a low affinity high capacity and a high affinity low capacity Na(+)/glucose cotransporter arranged in series along kidney proximal tubules. PTM: N-glycosylation is not necessary for the cotransporter function. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. +P31648 SC6A1_MOUSE Sodium- and chloride-dependent GABA transporter 1 (GAT-1) (Solute carrier family 6 member 1) 599 67,001 Chain (1); Disulfide bond (1); Glycosylation (3); Metal binding (9); Modified residue (2); Motif (1); Sequence conflict (4); Topological domain (3); Transmembrane (12) TRANSMEM 53 73 Helical; Name=1. {ECO:0000255}.; TRANSMEM 81 100 Helical; Name=2. {ECO:0000255}.; TRANSMEM 124 144 Helical; Name=3. {ECO:0000255}.; TRANSMEM 212 230 Helical; Name=4. {ECO:0000255}.; TRANSMEM 239 256 Helical; Name=5. {ECO:0000255}.; TRANSMEM 292 309 Helical; Name=6. {ECO:0000255}.; TRANSMEM 321 342 Helical; Name=7. {ECO:0000255}.; TRANSMEM 375 394 Helical; Name=8. {ECO:0000255}.; TRANSMEM 422 440 Helical; Name=9. {ECO:0000255}.; TRANSMEM 457 477 Helical; Name=10. {ECO:0000255}.; TRANSMEM 498 517 Helical; Name=11. {ECO:0000255}.; TRANSMEM 536 554 Helical; Name=12. {ECO:0000255}. TOPO_DOM 1 52 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 145 211 Extracellular. {ECO:0000255}.; TOPO_DOM 555 599 Cytoplasmic. {ECO:0000255}. FUNCTION: Terminates the action of GABA by its high affinity sodium-dependent reuptake into presynaptic terminals. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Localized at the plasma membrane and in a subset of intracellular vesicles (By similarity). Localized at the presynaptic terminals of interneurons. {ECO:0000250, ECO:0000269|PubMed:15234345}. SUBUNIT: Interacts with MPP5. {ECO:0000269|PubMed:15234345}. DOMAIN: The PDZ domain-binding motif is involved in the interaction with MPP5. {ECO:0000250}. TISSUE SPECIFICITY: Brain. Expressed in the dentate gyrus of hippocampus, striatum and cerebellum (at protein level). {ECO:0000269|PubMed:15234345}. +Q923I7 SC5A2_MOUSE Sodium/glucose cotransporter 2 (Na(+)/glucose cotransporter 2) (Low affinity sodium-glucose cotransporter) (Solute carrier family 5 member 2) 670 73,008 Chain (1); Glycosylation (1); Topological domain (11); Transmembrane (11) TRANSMEM 24 42 Helical. {ECO:0000255}.; TRANSMEM 60 80 Helical. {ECO:0000255}.; TRANSMEM 101 121 Helical. {ECO:0000255}.; TRANSMEM 167 187 Helical. {ECO:0000255}.; TRANSMEM 204 224 Helical. {ECO:0000255}.; TRANSMEM 269 289 Helical. {ECO:0000255}.; TRANSMEM 313 332 Helical. {ECO:0000255}.; TRANSMEM 422 441 Helical. {ECO:0000255}.; TRANSMEM 454 474 Helical. {ECO:0000255}.; TRANSMEM 525 545 Helical. {ECO:0000255}.; TRANSMEM 649 669 Helical. {ECO:0000255}. TOPO_DOM 1 23 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 43 59 Extracellular. {ECO:0000255}.; TOPO_DOM 81 100 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 122 166 Extracellular. {ECO:0000255}.; TOPO_DOM 188 203 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 225 268 Extracellular. {ECO:0000255}.; TOPO_DOM 290 312 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 333 421 Extracellular. {ECO:0000255}.; TOPO_DOM 442 453 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 475 524 Extracellular. {ECO:0000255}.; TOPO_DOM 546 648 Cytoplasmic. {ECO:0000255}. FUNCTION: Efficient substrate transport in mammalian kidney is provided by the concerted action of a low affinity high capacity and a high affinity low capacity Na(+)/glucose cotransporter arranged in series along kidney proximal tubules. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. +Q9D8V7 SC11C_MOUSE Signal peptidase complex catalytic subunit SEC11C (EC 3.4.21.89) (Microsomal signal peptidase 21 kDa subunit) (SPase 21 kDa subunit) (SEC11 homolog C) (SEC11-like protein 3) (SPC21) 192 21,660 Active site (1); Chain (1); Topological domain (2); Transmembrane (1) TRANSMEM 29 48 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 28 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 49 192 Lumenal. {ECO:0000255}. FUNCTION: Component of the microsomal signal peptidase complex which removes signal peptides from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum. {ECO:0000250}. SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. SUBUNIT: Component of the microsomal signal peptidase complex which consists of five members: SEC11A, SEC11C, SPCS1, SPCS2 and SPCS3. {ECO:0000250}. +P56841 TCLB2_MOUSE Protein TCL1B2 117 13,672 Chain (1) +Q9JKZ2 SC5A3_MOUSE Sodium/myo-inositol cotransporter (Na(+)/myo-inositol cotransporter) (Sodium/myo-inositol transporter 1) (SMIT1) (Solute carrier family 5 member 3) 718 79,583 Chain (1); Glycosylation (1); Modified residue (2); Sequence conflict (1); Site (2); Topological domain (13); Transmembrane (12) TRANSMEM 10 29 Helical. {ECO:0000255}.; TRANSMEM 39 57 Helical. {ECO:0000255}.; TRANSMEM 87 110 Helical. {ECO:0000255}.; TRANSMEM 124 144 Helical. {ECO:0000255}.; TRANSMEM 158 183 Helical. {ECO:0000255}.; TRANSMEM 187 205 Helical. {ECO:0000255}.; TRANSMEM 304 324 Helical. {ECO:0000255}.; TRANSMEM 354 376 Helical. {ECO:0000255}.; TRANSMEM 407 430 Helical. {ECO:0000255}.; TRANSMEM 444 462 Helical. {ECO:0000255}.; TRANSMEM 511 532 Helical. {ECO:0000255}.; TRANSMEM 696 716 Helical. {ECO:0000255}. TOPO_DOM 1 9 Extracellular. {ECO:0000255}.; TOPO_DOM 30 38 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 58 86 Extracellular. {ECO:0000255}.; TOPO_DOM 111 123 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 145 157 Extracellular. {ECO:0000255}.; TOPO_DOM 184 186 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 206 303 Extracellular. {ECO:0000255}.; TOPO_DOM 325 353 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 377 406 Extracellular. {ECO:0000255}.; TOPO_DOM 431 443 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 463 510 Extracellular. {ECO:0000255}.; TOPO_DOM 533 695 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 717 718 Extracellular. {ECO:0000255}. FUNCTION: Prevents intracellular accumulation of high concentrations of myo-inositol (an osmolyte) that result in impairment of cellular function. {ECO:0000269|PubMed:12719585}.; FUNCTION: Functions as a retroviral receptor for M813 murine leukemia virus (MuLV) entry. {ECO:0000269|PubMed:12719585}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. +Q8BGY9 SC5A7_MOUSE High affinity choline transporter 1 (Hemicholinium-3-sensitive choline transporter) (CHT) (Solute carrier family 5 member 7) 580 63,365 Chain (1); Glycosylation (1); Region (1); Sequence conflict (6); Topological domain (14); Transmembrane (13) TRANSMEM 7 27 Helical. {ECO:0000255}.; TRANSMEM 49 69 Helical. {ECO:0000255}.; TRANSMEM 82 102 Helical. {ECO:0000255}.; TRANSMEM 126 146 Helical. {ECO:0000255}.; TRANSMEM 165 185 Helical. {ECO:0000255}.; TRANSMEM 192 212 Helical. {ECO:0000255}.; TRANSMEM 238 258 Helical. {ECO:0000255}.; TRANSMEM 275 295 Helical. {ECO:0000255}.; TRANSMEM 318 338 Helical. {ECO:0000255}.; TRANSMEM 377 397 Helical. {ECO:0000255}.; TRANSMEM 407 427 Helical. {ECO:0000255}.; TRANSMEM 436 456 Helical. {ECO:0000255}.; TRANSMEM 482 502 Helical. {ECO:0000255}. TOPO_DOM 1 6 Extracellular. {ECO:0000255}.; TOPO_DOM 28 48 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 70 81 Extracellular. {ECO:0000255}.; TOPO_DOM 103 125 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 147 164 Extracellular. {ECO:0000255}.; TOPO_DOM 186 191 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 213 237 Extracellular. {ECO:0000255}.; TOPO_DOM 259 274 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 296 317 Extracellular. {ECO:0000255}.; TOPO_DOM 339 376 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 398 406 Extracellular. {ECO:0000255}.; TOPO_DOM 428 435 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 457 481 Extracellular. {ECO:0000255}.; TOPO_DOM 503 580 Cytoplasmic. {ECO:0000255}. FUNCTION: Transmembrane transporter that imports choline from the extracellular space to the neuron with high affinity. Choline uptake is the rate-limiting step in acetylcholine synthesis. Sodium ion- and chloride ion-dependent. {ECO:0000269|PubMed:15173594}. PTM: Phosphorylated by PKC and dephosphorylated by PP1/PP2A. {ECO:0000269|PubMed:15064333}. SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9GZV3}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9GZV3}. Cell membrane {ECO:0000250|UniProtKB:Q9GZV3}. Cell junction, synapse {ECO:0000250|UniProtKB:Q9GZV3}. Note=Localized at the neuromuscular junction. {ECO:0000250|UniProtKB:Q9GZV3}. SUBUNIT: Homooligomerizes at cell surface. Interacts with SEC14L1; may regulate SLC5A7. {ECO:0000250|UniProtKB:Q9GZV3}. TISSUE SPECIFICITY: Found in spinal cord, brain-stem, mid-brain and striatum. Specific for cholinergic neurons. +Q8K021 SCAM1_MOUSE Secretory carrier-associated membrane protein 1 (Secretory carrier membrane protein 1) 338 38,029 Chain (1); Initiator methionine (1); Modified residue (3); Topological domain (5); Transmembrane (4) TRANSMEM 156 176 Helical. {ECO:0000255}.; TRANSMEM 182 202 Helical. {ECO:0000255}.; TRANSMEM 219 239 Helical. {ECO:0000255}.; TRANSMEM 262 282 Helical. {ECO:0000255}. TOPO_DOM 2 155 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 177 181 Lumenal. {ECO:0000255}.; TOPO_DOM 203 218 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 240 261 Lumenal. {ECO:0000255}.; TOPO_DOM 283 338 Cytoplasmic. {ECO:0000255}. FUNCTION: Functions in post-Golgi recycling pathways. Acts as a recycling carrier to the cell surface (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Recycling endosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with SYNRG, ITSN1 and SLC9A7. {ECO:0000250}. +Q3UPL0 SC31A_MOUSE Protein transport protein Sec31A (SEC31-like protein 1) (SEC31-related protein A) 1230 133,569 Alternative sequence (2); Chain (1); Compositional bias (1); Cross-link (2); Modified residue (6); Motif (1); Region (2); Repeat (8); Sequence conflict (1) FUNCTION: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER) (By similarity). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules (By similarity). {ECO:0000250|UniProtKB:O94979, ECO:0000250|UniProtKB:Q9Z2Q1}. PTM: Monoubiquitinated by the BCR(KLHL12) E3 ubiquitin ligase complex, leading to regulate the size of COPII coats. {ECO:0000250|UniProtKB:O94979}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250|UniProtKB:O94979}; Peripheral membrane protein {ECO:0000250|UniProtKB:O94979}; Cytoplasmic side {ECO:0000250|UniProtKB:O94979}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Associates with membranes in a GTP-dependent manner (By similarity). Localizes to endoplasmic reticulum exit sites (ERES), also known as transitional endoplasmic reticulum (tER) (PubMed:25201882). {ECO:0000250|UniProtKB:Q9Z2Q1, ECO:0000269|PubMed:25201882}. SUBUNIT: COPII is composed of at least 5 proteins: the SEC23/24 complex, the SEC13/31 complex and SAR1. SEC13 and SEC31 make a 2:2 tetramer that forms the edge element of the COPII outer coat. The tetramer self-assembles in multiple copies to form the complete polyhedral cage. Interacts (via WD 8) with SEC13 (By similarity). Interacts with PDCD6; interaction takes place in response to cytosolic calcium increase and leads to bridge together the BCR(KLHL12) complex and SEC31A, leading to monoubiquitination. Interacts with KLHL12 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O94979}. DOMAIN: The ALG-2-binding site motif-2 (ABS-2) contains a PXPGF sequence that binds hydrophobic pocket 3 of PDCD6. {ECO:0000250|UniProtKB:O94979}. +P28571 SC6A9_MOUSE Sodium- and chloride-dependent glycine transporter 1 (GlyT-1) (GlyT1) (Solute carrier family 6 member 9) 692 76,544 Alternative sequence (2); Chain (1); Modified residue (3); Sequence conflict (5); Topological domain (3); Transmembrane (12) TRANSMEM 95 115 Helical; Name=1. {ECO:0000255}.; TRANSMEM 122 142 Helical; Name=2. {ECO:0000255}.; TRANSMEM 174 194 Helical; Name=3. {ECO:0000255}.; TRANSMEM 272 292 Helical; Name=4. {ECO:0000255}.; TRANSMEM 301 321 Helical; Name=5. {ECO:0000255}.; TRANSMEM 346 366 Helical; Name=6. {ECO:0000255}.; TRANSMEM 393 413 Helical; Name=7. {ECO:0000255}.; TRANSMEM 436 456 Helical; Name=8. {ECO:0000255}.; TRANSMEM 492 512 Helical; Name=9. {ECO:0000255}.; TRANSMEM 516 536 Helical; Name=10. {ECO:0000255}.; TRANSMEM 556 576 Helical; Name=11. {ECO:0000255}.; TRANSMEM 596 616 Helical; Name=12. {ECO:0000255}. TOPO_DOM 1 94 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 195 271 Extracellular. {ECO:0000255}.; TOPO_DOM 617 692 Cytoplasmic. {ECO:0000255}. FUNCTION: Terminates the action of glycine by its high affinity sodium-dependent reuptake into presynaptic terminals. May play a role in regulation of glycine levels in NMDA receptor-mediated neurotransmission. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed in the brain (at protein level) (PubMed:27773429). At E11, expressed in the ventral part of the ventricular zone. At E15, also expressed in adjacent mantle tissue and the meninges. Strongly expressed in E12 and E15 liver. {ECO:0000269|PubMed:27773429, ECO:0000269|PubMed:7891186, ECO:0000269|PubMed:8226790}. +P20826 SCF_MOUSE Kit ligand (Hematopoietic growth factor KL) (Mast cell growth factor) (MGF) (Steel factor) (Stem cell factor) (SCF) (c-Kit ligand) [Cleaved into: Soluble KIT ligand (sKITLG)] 273 30,645 Alternative sequence (1); Beta strand (2); Chain (2); Disulfide bond (2); Glycosylation (4); Helix (6); Natural variant (3); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (2) TRANSMEM 215 237 Helical. {ECO:0000255}. TOPO_DOM 26 214 Extracellular. {ECO:0000255}.; TOPO_DOM 238 273 Cytoplasmic. {ECO:0000255}. FUNCTION: Ligand for the receptor-type protein-tyrosine kinase KIT. Plays an essential role in the regulation of cell survival and proliferation, hematopoiesis, stem cell maintenance, gametogenesis, mast cell development, migration and function, and in melanogenesis. KITLG/SCF binding can activate several signaling pathways. Promotes phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, and subsequent activation of the kinase AKT1. KITLG/SCF and KIT also transmit signals via GRB2 and activation of RAS, RAF1 and the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. KITLG/SCF and KIT promote activation of STAT family members STAT1, STAT3 and STAT5. KITLG/SCF and KIT promote activation of PLCG1, leading to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. KITLG/SCF acts synergistically with other cytokines, probably interleukins. PTM: A soluble form is produced by proteolytic processing of isoform 1 in the extracellular domain. SUBCELLULAR LOCATION: Isoform 1: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm {ECO:0000250|UniProtKB:P21583}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000250|UniProtKB:P21583}; Single-pass type I membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P21583}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:P21583}. Cell projection, filopodium {ECO:0000250|UniProtKB:P21583}.; SUBCELLULAR LOCATION: Soluble KIT ligand: Secreted {ECO:0000250}. SUBUNIT: Homodimer, non-covalently linked (Probable). Heterotetramer with KIT, binding two KIT molecules; thereby mediates KIT dimerization and subsequent activation by autophosphorylation. {ECO:0000269|PubMed:17255936, ECO:0000305}. TISSUE SPECIFICITY: Expressed in the cochlea. {ECO:0000269|PubMed:26522471}. +P0DPB4 SCHI1_MOUSE Schwannomin-interacting protein 1 (SCHIP-1) 484 53,306 Alternative sequence (4); Chain (1); Coiled coil (1); Compositional bias (2); Erroneous initiation (1); Frameshift (1); Sequence caution (2); Sequence conflict (2) SUBUNIT: Homooligomer (via coiled coil domain) (By similarity). Interacts with NF2; the interaction is direct (By similarity). Interacts with ANK3 (By similarity). {ECO:0000250|UniProtKB:P0DPB3}. +Q9D0K2 SCOT1_MOUSE Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial (EC 2.8.3.5) (3-oxoacid CoA-transferase 1) (Somatic-type succinyl-CoA:3-oxoacid CoA-transferase) (SCOT-s) 520 55,989 Active site (1); Chain (1); Modified residue (5); Sequence conflict (1); Transit peptide (1) Ketone metabolism; succinyl-CoA degradation; acetoacetyl-CoA from succinyl-CoA: step 1/1. FUNCTION: Key enzyme for ketone body catabolism. Transfers the CoA moiety from succinate to acetoacetate. Formation of the enzyme-CoA intermediate proceeds via an unstable anhydride species formed between the carboxylate groups of the enzyme and substrate (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +Q66PY1 SCUB3_MOUSE Signal peptide, CUB and EGF-like domain-containing protein 3 993 108,984 Alternative sequence (2); Chain (1); Disulfide bond (28); Domain (10); Glycosylation (5); Signal peptide (1) FUNCTION: Binds to TGFBR2 and activates TGFB signaling. {ECO:0000250}. PTM: N-glycosylated. {ECO:0000269|PubMed:15234972}.; PTM: Proteolytic cleavage produces a CUB-containing C-terminal fragment that retains the ability to bind to TGFBR2. This reaction is catalyzed in vitro by MMP2 and, to a lesser extent, by MMP9 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. Cell surface {ECO:0000250|UniProtKB:Q8IX30}. SUBUNIT: Forms homooligomers and heterooligomers with SCUBE1. Interacts with TGFBR2 through the CUB domain; this interaction does not affect TGFB1-binding to TGFBR2. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in femur and humerus with little or no expression in non-bone tissues. {ECO:0000269|PubMed:15234972}. +Q61009 SCRB1_MOUSE Scavenger receptor class B member 1 (SRB1) (SR-BI) 509 56,754 Alternative sequence (1); Beta strand (1); Chain (1); Disulfide bond (1); Glycosylation (11); Helix (4); Lipidation (1); Sequence conflict (2); Topological domain (3); Transmembrane (2); Turn (1) TRANSMEM 12 32 Helical. {ECO:0000255}.; TRANSMEM 441 461 Helical. {ECO:0000255}. TOPO_DOM 1 11 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 33 440 Extracellular. {ECO:0000255}.; TOPO_DOM 462 509 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for different ligands such as phospholipids, cholesterol ester, lipoproteins, phosphatidylserine and apoptotic cells (By similarity). Both isoform 1 and isoform 2 act as receptors for HDL, mediating selective uptake of cholesteryl ether and HDL-dependent cholesterol efflux (PubMed:9254074, PubMed:9614139). Also facilitates the flux of free and esterified cholesterol between the cell surface and apoB-containing lipoproteins and modified lipoproteins, although less efficiently than HDL. May be involved in the phagocytosis of apoptotic cells, via its phosphatidylserine binding activity (By similarity). {ECO:0000250|UniProtKB:Q8WTV0, ECO:0000269|PubMed:9254074, ECO:0000269|PubMed:9614139}. PTM: N-glycosylated. {ECO:0000250}.; PTM: The six cysteines of the extracellular domain are all involved in intramolecular disulfide bonds. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9254074, ECO:0000269|PubMed:9614139}; Multi-pass membrane protein {ECO:0000250}. Membrane, caveola {ECO:0000269|PubMed:9614139}; Multi-pass membrane protein {ECO:0000250}. Note=Predominantly localized to cholesterol and sphingomyelin-enriched domains within the plasma membrane, called caveolae. {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 1: Cell membrane {ECO:0000269|PubMed:9614139}. Membrane, caveola {ECO:0000269|PubMed:9614139}.; SUBCELLULAR LOCATION: Isoform 2: Cell membrane {ECO:0000269|PubMed:9614139}. Membrane, caveola {ECO:0000269|PubMed:9614139}. SUBUNIT: The C-terminal region binds to PDZK1. {ECO:0000250}. TISSUE SPECIFICITY: Expressed primarily in liver, ovary and adrenal gland, and, at lower levels in other non-placental steroidogenic tissues, including adipose tissue, mammary gland and testis (at protein level) (PubMed:8560269, PubMed:9254074, PubMed:9614139). Isoform 2 is expressed at lower levels than isoform 1 in liver, testis and adrenal gland (PubMed:9614139). At the mRNA, but not at the protein level, isoform 2 is the predominant isoform in testis (80%) (PubMed:9254074). {ECO:0000269|PubMed:8560269, ECO:0000269|PubMed:9254074, ECO:0000269|PubMed:9614139}. +Q80U72 SCRIB_MOUSE Protein scribble homolog (Scribble) (Protein LAP4) 1612 174,059 Alternative sequence (3); Chain (1); Coiled coil (3); Compositional bias (4); Domain (4); Erroneous initiation (1); Modified residue (38); Region (2); Repeat (16); Sequence conflict (5) FUNCTION: Scaffold protein involved in different aspects of polarized cells differentiation regulating epithelial and neuronal morphogenesis. Most probably functions in the establishment of apico-basal cell polarity. May function in cell proliferation regulating progression from G1 to S phase and as a positive regulator of apoptosis for instance during acinar morphogenesis of the mammary epithelium. May also function in cell migration and adhesion and hence regulate cell invasion through MAPK signaling. May play a role in exocytosis and in the targeting synaptic vesicles to synapses. Functions as an activator of Rac GTPase activity. {ECO:0000269|PubMed:12499390, ECO:0000269|PubMed:18716323, ECO:0000269|PubMed:19041750, ECO:0000269|PubMed:19458197}. PTM: Ubiquitinated; targeted for UBE3A-dependent multiubiquitination and degraded. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q14160}; Peripheral membrane protein {ECO:0000250}. Cell junction, adherens junction {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Note=Targeting to cell-cell junctions which is CDH1-dependent is required for the pro-apoptotic activity. Localizes to neuronal post- and pre-synaptic regions (By similarity). {ECO:0000250}. SUBUNIT: Interacts with UBE3A. Interacts with PAK1 and PAK2. Interacts (via PDZ domains) with LPP and TRIP6; the interaction is direct. Interacts (via PDZ domains) with TJP2. Interacts (via PDZ domains) with TSHR; regulates TSHR trafficking and function (By similarity). Interacts (via PDZ domains) with VANGL2. Interacts with ARHGEF7 and GIT1; interacts directly with ARHGEF7. Interacts (via PDZ domains) with APC; may mediate APC targeting to adherens junctions of epithelial cells. Interacts with CTNNB1 and MAPK12. Interacts (via PDZ domains 1 and 3) with MCC (By similarity). Interacts with DLG5 (By similarity). Interacts with STK4/MST1 and LATS1 in the presence of DLG5 (By similarity). {ECO:0000250|UniProtKB:Q14160, ECO:0000269|PubMed:15182672, ECO:0000269|PubMed:15878399, ECO:0000269|PubMed:16611247, ECO:0000269|PubMed:16687519, ECO:0000269|PubMed:18716323, ECO:0000269|PubMed:19458197}. TISSUE SPECIFICITY: Found in a wide range of tissues including liver, brain, kidney and spleen. {ECO:0000269|PubMed:15806148}. +Q6V4S5 SDK2_MOUSE Protein sidekick-2 2176 239,902 Alternative sequence (3); Beta strand (37); Chain (1); Disulfide bond (5); Domain (19); Glycosylation (6); Helix (5); Motif (1); Mutagenesis (1); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (3) TRANSMEM 1937 1957 Helical. {ECO:0000255}. TOPO_DOM 25 1936 Extracellular. {ECO:0000255}.; TOPO_DOM 1958 2176 Cytoplasmic. {ECO:0000255}. FUNCTION: Adhesion molecule that promotes lamina-specific synaptic connections in the retina and is specifically required for the formation of neuronal circuits that detect motion (PubMed:26287463). Acts by promoting formation of synapses between two specific retinal cell types: the retinal ganglion cells W3B-RGCs and the excitatory amacrine cells VG3-ACs. Formation of synapses between these two cells plays a key role in detection of motion (PubMed:26287463). Promotes synaptic connectivity via homophilic interactions (PubMed:26287463). {ECO:0000269|PubMed:26287463}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8AV57}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q8AV57}. Cell junction, synapse {ECO:0000269|PubMed:20219992, ECO:0000305|PubMed:26287463}. SUBUNIT: Homodimer; mediates homophilic interactions to promote cell adhesion (PubMed:15703275, PubMed:26287463). Interacts (via PDZ-binding motif) with MAGI1, MAGI2, DLG2, DLG3 and DLG4 (PubMed:20219992). {ECO:0000269|PubMed:15703275, ECO:0000269|PubMed:20219992, ECO:0000269|PubMed:26287463}. DOMAIN: the PDZ-binding motif mediates interaction with PDZ domain-containing proteins MAGI1, MAGI2, DLG2, DLG3 and DLG4 and is required for is required for synaptic localization in photoreceptors. {ECO:0000269|PubMed:20219992}. TISSUE SPECIFICITY: Expressed in retinal ganglion cells (RGCs) that form synapses in distinct inner plexiform layer (IPL) sublaminae. Specifically expressed in specific subsets of retinal ganglion cells (RGCs), named W3B-RGCs, that specifically respond when the timing of the movement of a small object differs from that of the background, but not when they coincide (at protein level). Also present in excitatory amacrine cell type called VG3-ACs, that provide strong and selective input W3B-RGCs (at protein level) (PubMed:26287463). Expressed at low levels in the glomeruli (PubMed:15213259). {ECO:0000269|PubMed:15213259, ECO:0000269|PubMed:26287463}. +P63300 SELW_MOUSE Selenoprotein W (SelW) 88 9,687 Beta strand (4); Chain (1); Cross-link (1); Helix (2); Modified residue (1); Mutagenesis (4); Non-standard residue (1); Turn (1) FUNCTION: Plays a role as a glutathione (GSH)-dependent antioxidant. May be involved in a redox-related process. May play a role in the myopathies of selenium deficiency. {ECO:0000269|PubMed:12062442, ECO:0000269|PubMed:16876868, ECO:0000269|PubMed:17503775}. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Interacts with DPYSL2, PRDX1, YWHAB, YWHAG, HSP70 and HSP90. {ECO:0000269|PubMed:17503775, ECO:0000269|PubMed:17928294}. TISSUE SPECIFICITY: In the embryo, expressed in the developing nervous system and in mesoderm-derived tissues such as heart and limbs. In the adult, predominantly expressed in brain, skeletal muscle and heart. {ECO:0000269|PubMed:16876868, ECO:0000269|PubMed:17503775}. +Q7TMY4 THOC7_MOUSE THO complex subunit 7 homolog (Ngg1-interacting factor 3-like protein 1-binding protein 1) 204 23,715 Alternative sequence (1); Chain (1); Coiled coil (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (3); Region (2); Sequence conflict (1) FUNCTION: Required for efficient export of polyadenylated RNA. Acts as component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and which specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NFX1 pathway. {ECO:0000250|UniProtKB:Q6I9Y2}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6I9Y2}. Nucleus {ECO:0000250|UniProtKB:Q6I9Y2}. Nucleus speckle {ECO:0000250|UniProtKB:Q6I9Y2}. Note=Interaction with THOC5 is required for nuclear localization. {ECO:0000250|UniProtKB:Q6I9Y2}. SUBUNIT: Component of the THO complex, which is composed of THOC1, THOC2, THOC3, THOC5, THOC6 and THOC7; together with at least ALYREF/THOC4, DDX39B, SARNP/CIP29 and CHTOP, THO forms the transcription/export (TREX) complex which seems to have a dynamic structure involving ATP-dependent remodeling (By similarity). Interacts with NIF3L1 (PubMed:12951069). Interacts with THOC5 (By similarity). {ECO:0000250|UniProtKB:Q6I9Y2, ECO:0000269|PubMed:12951069}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:12951069}. +Q9JHW4 SELB_MOUSE Selenocysteine-specific elongation factor (Elongation factor sec) (Eukaryotic elongation factor, selenocysteine-tRNA-specific) (mSelB) 583 63,539 Chain (1); Domain (1); Modified residue (3); Motif (1); Nucleotide binding (3); Region (5); Sequence conflict (2) FUNCTION: Translation factor necessary for the incorporation of selenocysteine into proteins. It probably replaces EF-Tu for the insertion of selenocysteine directed by the UGA codon. SelB binds GTP and GDP. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}. +Q6P7W5 SEN2_MOUSE tRNA-splicing endonuclease subunit Sen2 (EC 4.6.1.16) (tRNA-intron endonuclease Sen2) 460 52,214 Active site (3); Chain (1); Modified residue (3) FUNCTION: Constitutes one of the two catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3'-cyclic phosphate and 5'-OH termini. There are no conserved sequences at the splice sites, but the intron is invariably located at the same site in the gene, placing the splice sites an invariant distance from the constant structural features of the tRNA body. Probably carries the active site for 5'-splice site cleavage. The tRNA splicing endonuclease is also involved in mRNA processing via its association with pre-mRNA 3'-end processing factors, establishing a link between pre-tRNA splicing and pre-mRNA 3'-end formation, suggesting that the endonuclease subunits function in multiple RNA-processing events (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Note=May be transiently localized in the nucleolus. {ECO:0000250}. SUBUNIT: tRNA splicing endonuclease is a heterotetramer composed of TSEN2, TSEN15, TSEN34/LENG5 and TSEN54. tRNA splicing endonuclease complex also contains proteins of the pre-mRNA 3'-end processing machinery such as CLP1, CPSF1, CPSF4 and CSTF2 (By similarity). {ECO:0000250}. +Q8C1A5 THOP1_MOUSE Thimet oligopeptidase (EC 3.4.24.15) 687 78,026 Active site (1); Chain (1); Metal binding (3); Modified residue (5); Sequence conflict (5) FUNCTION: Involved in the metabolism of neuropeptides under 20 amino acid residues long. Involved in cytoplasmic peptide degradation. Able to degrade the amyloid-beta precursor protein and generate amyloidogenic fragments (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. +O08576 RUN3A_MOUSE RUN domain-containing protein 3A (Rap2-interacting protein 8) (RPIP-8) 446 50,018 Alternative sequence (4); Chain (1); Coiled coil (1); Domain (1); Modified residue (4); Region (1) FUNCTION: May act as an effector of RAP2A in neuronal cells. {ECO:0000269|PubMed:9523700}. SUBUNIT: Interacts with the GTP-bound form of RAP2A. {ECO:0000269|PubMed:9523700}. TISSUE SPECIFICITY: Brain. {ECO:0000269|PubMed:9523700}. +Q3TD16 RUBCL_MOUSE Protein RUBCNL-like 648 72,279 Chain (1); Erroneous initiation (1) FUNCTION: May act as a tumor suppressor. {ECO:0000250|UniProtKB:Q9H714}. +Q9D394 RUFY3_MOUSE Protein RUFY3 (Rap2-interacting protein x) (RIPx) (Single axon-regulated protein 1) (Singar1) 469 53,007 Alternative sequence (3); Beta strand (1); Chain (1); Coiled coil (1); Domain (1); Helix (12); Modified residue (11); Sequence conflict (3); Turn (1) FUNCTION: Plays a role in the generation of neuronal polarity formation and axon growth (PubMed:24720729). Implicated in the formation of a single axon by developing neurons (PubMed:24720729). May inhibit the formation of additional axons by inhibition of PI3K in minor neuronal processes (By similarity). Plays a role in the formation of F-actin-enriched protrusive structures at the cell periphery (By similarity). Plays a role in cytoskeletal organization by regulating the subcellular localization of FSCN1 and DBN1 at axonal growth cones (PubMed:24720729). Promotes gastric cancer cell migration and invasion in a PAK1-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q5FVJ0, ECO:0000250|UniProtKB:Q7L099, ECO:0000269|PubMed:24720729}. PTM: Phosphorylated by PAK1. Isoform 1 is partially phosphorylated. {ECO:0000250|UniProtKB:Q5FVJ0, ECO:0000250|UniProtKB:Q7L099}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q7L099}. Endomembrane system {ECO:0000250|UniProtKB:Q7L099}. Cell projection, invadopodium {ECO:0000250|UniProtKB:Q7L099}. Perikaryon {ECO:0000269|PubMed:24720729}. Cell projection {ECO:0000269|PubMed:24720729}. Cell projection, growth cone {ECO:0000269|PubMed:24720729}. Cell projection, filopodium {ECO:0000269|PubMed:24720729}. Cell projection, lamellipodium {ECO:0000269|PubMed:24720729}. Note=Accumulates in axon growth cones in a F-actin-dependent manner (PubMed:24720729). Colocalized with FSCN1 and F-actin at filipodia and lamellipodia of axonal growth cones (PubMed:24720729). Colocalized with DBN1 and F-actin at transitional domain of the axonal growth cone (PubMed:24720729). Colocalizes with PAK1, F-actin, myosins and integrins in invadopodia at the cell periphery (By similarity). Colocalized with Ras-related Rab-5 proteins in cytoplasmic vesicles (By similarity). {ECO:0000250|UniProtKB:Q5FVJ0, ECO:0000250|UniProtKB:Q7L099, ECO:0000269|PubMed:24720729}. SUBUNIT: Interacts (via N-terminus) with FSCN1; this interaction induces neuron axon development (PubMed:24720729). Interacts with DBN1 (PubMed:24720729). Interacts with PAK1 (By similarity). Interacts (via C-terminus) with Ras-related Rab-5 proteins (By similarity). Interacts (via C-terminus) with Ras-related Rap-2 proteins (By similarity). Interacts with PIK3CA and PIK3R1 (By similarity). {ECO:0000250|UniProtKB:Q5FVJ0, ECO:0000250|UniProtKB:Q7L099, ECO:0000269|PubMed:24720729}. TISSUE SPECIFICITY: Expressed in brain (at protein level) (PubMed:24720729). {ECO:0000269|PubMed:24720729}. +Q80U62 RUBIC_MOUSE Run domain Beclin-1-interacting and cysteine-rich domain-containing protein (Rubicon) 956 106,860 Alternative sequence (3); Chain (1); Compositional bias (3); Domain (1); Erroneous initiation (2); Modified residue (8); Region (7); Sequence conflict (16) FUNCTION: Inhibits PIK3C3 activity; under basal conditions negatively regulates PI3K complex II (PI3KC3-C2) function in autophagy. Negatively regulates endosome maturation and degradative endocytic trafficking and impairs autophagosome maturation process (PubMed:19270693). Can sequester UVRAG from association with a class C Vps complex (possibly the HOPS complex) and negatively regulates Rab7 activation (By similarity). {ECO:0000250|UniProtKB:Q92622, ECO:0000269|PubMed:19270693}.; FUNCTION: Involved in regulation of pathogen-specific host defense of activated macrophages. Following bacterial infection promotes NADH oxidase activity by association with CYBA thereby affecting TLR2 signaling and probably other TLR-NOX pathways. Stabilizes the CYBA:CYBB NADPH oxidase heterodimer, increases its association with TLR2 and its phagosome trafficking to induce antimicrobial burst of ROS and production of inflammatory cytokines. Following fungal or viral infection (implicating CLEC7A (dectin-1)-mediated myeloid cell activation or DDX58/RIG-I-dependent sensing of RNA viruses) negatively regulates pro-inflammatory cytokine production by association with CARD9 and sequestering it from signaling complexes (By similarity). {ECO:0000250|UniProtKB:Q92622}. SUBCELLULAR LOCATION: Late endosome {ECO:0000269|PubMed:19270693}. Lysosome {ECO:0000269|PubMed:19270693}. Early endosome {ECO:0000269|PubMed:19270693}. Note=Predominantly located in late endosomes/lysosomes, only partially detected in early endosome and not at all in the Golgi apparatus. SUBUNIT: Associates with PI3K (PI3KC3/PI3K-III/class III phosphatidylinositol 3-kinase) complex II (PI3KC3-C2) in which the core composed of the catalytic subunit PIK3C3, the regulatory subunit PIK3R4 and BECN1 is associated with UVRAG; in the complex interacts directly with PI3KC3 and UVRAG (PubMed:19270693). Interacts with Rab7 (RAB7A or RAB7B) (GTP-bound form); Rab7 and UVRAG compete for RUBCN binding; can interact simultaneously with Rab7 and the PI3K complex. Interacts with CYBA and CYBB; indicative for the association with the CYBA:CYBB NADPH oxidase heterodimer. Interacts with NOX4 and probably associates with the CYBA:NOX4 complex. Interacts with YWHAB and CARD9 in a competetive and stimulation-dependent manner; RUBCN exchanges interaction from YWHAB to CARD9 upon stimulation with beta-1,3-glucan (By similarity). {ECO:0000250|UniProtKB:Q92622, ECO:0000269|PubMed:19270693}. +P0DN89 T254A_MOUSE Transmembrane protein 254 123 14,239 Alternative sequence (1); Chain (1); Transmembrane (3) TRANSMEM 15 35 Helical. {ECO:0000255}.; TRANSMEM 63 83 Helical. {ECO:0000255}.; TRANSMEM 95 115 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q99M03 RWD2B_MOUSE RWD domain-containing protein 2B 290 32,892 Chain (1); Domain (1); Sequence conflict (2) +Q9CQK7 RWDD1_MOUSE RWD domain-containing protein 1 (DRG family-regulatory protein 2) (IH1) 243 27,785 Chain (1); Domain (1); Initiator methionine (1); Modified residue (2); Region (1) FUNCTION: Protects DRG2 from proteolytic degradation. {ECO:0000269|PubMed:15676025}. SUBUNIT: Interacts with androgen receptor (By similarity). Interacts with DRG2. {ECO:0000250, ECO:0000269|PubMed:15676025}. +Q99MR3 S12A9_MOUSE Solute carrier family 12 member 9 (Cation-chloride cotransporter-interacting protein 1) (Potassium-chloride transporter 9) 914 96,330 Chain (1); Compositional bias (2); Glycosylation (2); Modified residue (1); Sequence conflict (3); Topological domain (13); Transmembrane (12) TRANSMEM 37 57 Helical. {ECO:0000255}.; TRANSMEM 73 93 Helical. {ECO:0000255}.; TRANSMEM 120 140 Helical. {ECO:0000255}.; TRANSMEM 168 188 Helical. {ECO:0000255}.; TRANSMEM 194 214 Helical. {ECO:0000255}.; TRANSMEM 263 283 Helical. {ECO:0000255}.; TRANSMEM 298 318 Helical. {ECO:0000255}.; TRANSMEM 339 359 Helical. {ECO:0000255}.; TRANSMEM 377 399 Helical. {ECO:0000255}.; TRANSMEM 417 437 Helical. {ECO:0000255}.; TRANSMEM 467 487 Helical. {ECO:0000255}.; TRANSMEM 741 761 Helical. {ECO:0000255}. TOPO_DOM 1 36 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 58 72 Extracellular. {ECO:0000255}.; TOPO_DOM 94 119 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 141 167 Extracellular. {ECO:0000255}.; TOPO_DOM 189 193 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 215 262 Extracellular. {ECO:0000255}.; TOPO_DOM 284 297 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 319 338 Extracellular. {ECO:0000255}.; TOPO_DOM 360 376 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 400 416 Extracellular. {ECO:0000255}.; TOPO_DOM 438 466 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 488 740 Extracellular. {ECO:0000255}.; TOPO_DOM 762 914 Cytoplasmic. {ECO:0000255}. FUNCTION: May be an inhibitor of SLC12A1. Seems to correspond to a subunit of a multimeric transport system and thus, additional subunits may be required for its function (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with SLC12A1. {ECO:0000250}. +O70577 S22A2_MOUSE Solute carrier family 22 member 2 (Organic cation transporter 2) 553 61,831 Alternative sequence (2); Chain (1); Glycosylation (1); Site (1); Topological domain (13); Transmembrane (12) TRANSMEM 22 42 Helical. {ECO:0000255}.; TRANSMEM 151 171 Helical. {ECO:0000255}.; TRANSMEM 178 198 Helical. {ECO:0000255}.; TRANSMEM 211 231 Helical. {ECO:0000255}.; TRANSMEM 239 259 Helical. {ECO:0000255}.; TRANSMEM 264 284 Helical. {ECO:0000255}.; TRANSMEM 349 369 Helical. {ECO:0000255}.; TRANSMEM 376 396 Helical. {ECO:0000255}.; TRANSMEM 405 425 Helical. {ECO:0000255}.; TRANSMEM 433 453 Helical. {ECO:0000255}.; TRANSMEM 465 485 Helical. {ECO:0000255}.; TRANSMEM 495 515 Helical. {ECO:0000255}. TOPO_DOM 1 21 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 43 150 Extracellular. {ECO:0000255}.; TOPO_DOM 172 177 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 199 210 Extracellular. {ECO:0000255}.; TOPO_DOM 232 238 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 260 263 Extracellular. {ECO:0000255}.; TOPO_DOM 285 348 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 370 375 Extracellular. {ECO:0000255}.; TOPO_DOM 397 404 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 426 432 Extracellular. {ECO:0000255}.; TOPO_DOM 454 464 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 486 494 Extracellular. {ECO:0000255}.; TOPO_DOM 516 553 Cytoplasmic. {ECO:0000255}. FUNCTION: Mediates tubular uptake of organic compounds from circulation. Mediates the influx of agmatine, dopamine, noradrenaline (norepinephrine), serotonin, choline, famotidine, ranitidine, histamin, creatinine, amantadine, memantine, acriflavine, 4-[4-(dimethylamino)-styryl]-N-methylpyridinium ASP, amiloride, metformin, N-1-methylnicotinamide (NMN), tetraethylammonium (TEA), 1-methyl-4-phenylpyridinium (MPP), cimetidine, cisplatin and oxaliplatin. Cisplatin may develop a nephrotoxic action. Transport of creatinine is inhibited by fluoroquinolones such as DX-619 and LVFX. This transporter is a major determinant of the anticancer activity of oxaliplatin and may contribute to antitumor specificity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in kidney and ureter. To a lower extent, also expressed in brain and embryo. {ECO:0000269|PubMed:10051314}. +Q9CQC9 SAR1B_MOUSE GTP-binding protein SAR1b 198 22,382 Chain (1); Metal binding (2); Modified residue (1); Nucleotide binding (3) FUNCTION: Involved in transport from the endoplasmic reticulum to the Golgi apparatus. Activated by the guanine nucleotide exchange factor PREB. Involved in the selection of the protein cargo and the assembly of the COPII coat complex. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11422940}; Peripheral membrane protein {ECO:0000269|PubMed:11422940}. Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:11422940}; Peripheral membrane protein {ECO:0000269|PubMed:11422940}. Note=Associated with the endoplasmic reticulum and Golgi stacks, in particular in the juxta-nuclear Golgi region. SUBUNIT: Homodimer. Part of the COPII coat complex. Binds to the cytoplasmic tails of target proteins in the endoplasmic reticulum (By similarity). Binds PREB. {ECO:0000250}. +Q62255 SALL3_MOUSE Sal-like protein 3 (MSal) (Spalt-like protein 3) 1320 138,760 Alternative sequence (1); Chain (1); Compositional bias (4); Erroneous initiation (1); Modified residue (3); Sequence conflict (7); Zinc finger (9) FUNCTION: Probable transcription factor. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: In adult brain, testis and kidney. In lower levels also in adult ovaries and embryonic stem cells. In embryo in developing neuroectoderm of brain, inner ear and spinal chord. Also weakly and transiently expressed in embryonic branchial arches, notochord, limb buds and heart. +Q8VI24 SATB2_MOUSE DNA-binding protein SATB2 (Special AT-rich sequence-binding protein 2) 733 82,559 Alternative sequence (1); Chain (1); Cross-link (8); DNA binding (3); Erroneous initiation (1); Modified residue (5) FUNCTION: Binds to DNA, at nuclear matrix- or scaffold-associated regions. Thought to recognize the sugar-phosphate structure of double-stranded DNA. Transcription factor controlling nuclear gene expression, by binding to matrix attachment regions (MARs) of DNA and inducing a local chromatin-loop remodeling. Acts as a docking site for several chromatin remodeling enzymes and also by recruiting corepressors (HDACs) or coactivators (HATs) directly to promoters and enhancers. Required for the initiation of the upper-layer neurons (UL1) specific genetic program and for the inactivation of deep-layer neurons (DL) and UL2 specific genes, probably by modulating Bcl11b expression. Repressor of Ctip2 and regulatory determinant of corticocortical connections in the developing cerebral cortex. May play an important role in palate formation. Acts as a molecular node in a transcriptional network regulating skeletal development and osteoblast differentiation. {ECO:0000269|PubMed:16751105, ECO:0000269|PubMed:18255030, ECO:0000269|PubMed:18255031}. PTM: Sumoylated by PIAS1. Sumoylation promotes nuclear localization, but represses transcription factor activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-ProRule:PRU00374}. SUBUNIT: Interacts with PIAS1 (By similarity). Interacts with ATF4 and RUNX2; resulting in enhanced DNA binding and transactivation by these transcription factors. {ECO:0000250, ECO:0000269|PubMed:16751105}. TISSUE SPECIFICITY: Expressed in cortical neurons that extend axons across the corpus callosum. Also expressed in branchial arches and in cells of the osteoblast lineage, but not in chondrocytes and osteoclasts. {ECO:0000269|PubMed:16751105, ECO:0000269|PubMed:18255030}. +Q9D662 SC23B_MOUSE Protein transport protein Sec23B (SEC23-related protein B) 767 86,437 Chain (1); Initiator methionine (1); Metal binding (4); Modified residue (2); Repeat (1); Sequence conflict (4) FUNCTION: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules for their transport to the Golgi complex. {ECO:0000250|UniProtKB:Q15436}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250|UniProtKB:Q15436}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q15436}; Cytoplasmic side {ECO:0000250|UniProtKB:Q15436}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q15437}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q15436}; Cytoplasmic side {ECO:0000250|UniProtKB:Q15436}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q15436}. SUBUNIT: COPII is composed of at least five proteins: the Sec23/24 complex, the Sec13/31 complex and Sar1 (By similarity). Interacts with SAR1A (By similarity). {ECO:0000250|UniProtKB:Q15436, ECO:0000250|UniProtKB:Q15437}. +O88968 TCO2_MOUSE Transcobalamin-2 (TC-2) (Transcobalamin II) (TC II) (TCII) 430 47,586 Binding site (3); Chain (1); Disulfide bond (3); Metal binding (1); Natural variant (1); Region (3); Sequence conflict (2); Signal peptide (1) FUNCTION: Primary vitamin B12-binding and transport protein. Delivers cobalamin to cells. {ECO:0000250|UniProtKB:P20062}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P20062}. SUBUNIT: Interacts with CD320 (via LDL-receptor class A domains). {ECO:0000250|UniProtKB:P20062}. +Q6PGE7 SC6A7_MOUSE Sodium-dependent proline transporter (Solute carrier family 6 member 7) 637 71,066 Chain (1); Glycosylation (1); Modified residue (8); Sequence conflict (2); Topological domain (3); Transmembrane (12) TRANSMEM 46 66 Helical; Name=1. {ECO:0000255}.; TRANSMEM 74 93 Helical; Name=2. {ECO:0000255}.; TRANSMEM 117 137 Helical; Name=3. {ECO:0000255}.; TRANSMEM 215 233 Helical; Name=4. {ECO:0000255}.; TRANSMEM 242 259 Helical; Name=5. {ECO:0000255}.; TRANSMEM 295 312 Helical; Name=6. {ECO:0000255}.; TRANSMEM 324 345 Helical; Name=7. {ECO:0000255}.; TRANSMEM 378 397 Helical; Name=8. {ECO:0000255}.; TRANSMEM 425 443 Helical; Name=9. {ECO:0000255}.; TRANSMEM 459 479 Helical; Name=10. {ECO:0000255}.; TRANSMEM 500 519 Helical; Name=11. {ECO:0000255}.; TRANSMEM 538 556 Helical; Name=12. {ECO:0000255}. TOPO_DOM 1 45 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 138 214 Extracellular. {ECO:0000255}.; TOPO_DOM 557 637 Cytoplasmic. {ECO:0000255}. FUNCTION: Terminates the action of proline by its high affinity sodium-dependent reuptake into presynaptic terminals. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q8BTY8 SCFD2_MOUSE Sec1 family domain-containing protein 2 (Neuronal Sec1) (Syntaxin-binding protein 1-like 1) 684 74,751 Alternative sequence (4); Chain (1); Compositional bias (1); Erroneous initiation (2); Sequence conflict (4) FUNCTION: May be involved in protein transport. {ECO:0000250}. +O35609 SCAM3_MOUSE Secretory carrier-associated membrane protein 3 (Secretory carrier membrane protein 3) 349 38,458 Chain (1); Cross-link (1); Modified residue (8); Sequence conflict (6); Topological domain (2); Transmembrane (4) TRANSMEM 169 189 Helical. {ECO:0000255}.; TRANSMEM 200 220 Helical. {ECO:0000255}.; TRANSMEM 236 256 Helical. {ECO:0000255}.; TRANSMEM 277 297 Helical. {ECO:0000255}. TOPO_DOM 1 168 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 298 349 Cytoplasmic. {ECO:0000255}. FUNCTION: Functions in post-Golgi recycling pathways. Acts as a recycling carrier to the cell surface. PTM: Monoubiquitinated. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SUBUNIT: Interacts with NEDD4 and NEDD4L and TSG101 (By similarity). Interacts with RNF126. {ECO:0000250|UniProtKB:O14828, ECO:0000269|PubMed:23418353}. +Q9WTU3 SCN8A_MOUSE Sodium channel protein type 8 subunit alpha (Sodium channel protein type VIII subunit alpha) (Voltage-gated sodium channel subunit alpha Nav1.6) 1978 225,141 Alternative sequence (5); Chain (1); Disulfide bond (4); Domain (1); Glycosylation (8); Helix (1); Intramembrane (4); Modified residue (3); Natural variant (2); Nucleotide binding (1); Repeat (4); Sequence conflict (6); Topological domain (29); Transmembrane (24) INTRAMEM 356 380 Pore-forming. {ECO:0000250|UniProtKB:D0E0C2}.; INTRAMEM 920 940 Pore-forming. {ECO:0000250|UniProtKB:D0E0C2}.; INTRAMEM 1398 1419 Pore-forming. {ECO:0000250|UniProtKB:D0E0C2}.; INTRAMEM 1689 1711 Pore-forming. {ECO:0000250|UniProtKB:D0E0C2}. TRANSMEM 133 151 Helical; Name=S1 of repeat I. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 159 179 Helical; Name=S2 of repeat I. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 194 211 Helical; Name=S3 of repeat I. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 218 234 Helical; Name=S4 of repeat I. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 254 273 Helical; Name=S5 of repeat I. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 388 408 Helical; Name=S6 of repeat I. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 752 770 Helical; Name=S1 of repeat II. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 782 801 Helical; Name=S2 of repeat II. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 816 835 Helical; Name=S3 of repeat II. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 838 855 Helical; Name=S4 of repeat II. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 872 890 Helical; Name=S5 of repeat II. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 954 974 Helical; Name=S6 of repeat II. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1198 1215 Helical; Name=S1 of repeat III. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1229 1247 Helical; Name=S2 of repeat III. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1262 1280 Helical; Name=S3 of repeat III. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1289 1307 Helical; Name=S4 of repeat III. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1325 1344 Helical; Name=S5 of repeat III. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1437 1458 Helical; Name=S6 of repeat III. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1522 1539 Helical; Name=S1 of repeat IV. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1551 1569 Helical; Name=S2 of repeat IV. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1582 1599 Helical; Name=S3 of repeat IV. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1613 1629 Helical; Name=S4 of repeat IV. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1649 1666 Helical; Name=S5 of repeat IV. {ECO:0000250|UniProtKB:D0E0C2}.; TRANSMEM 1741 1763 Helical; Name=S6 of repeat IV. {ECO:0000250|UniProtKB:D0E0C2}. TOPO_DOM 1 132 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 152 158 Extracellular. {ECO:0000305}.; TOPO_DOM 180 193 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 212 217 Extracellular. {ECO:0000305}.; TOPO_DOM 235 253 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 274 355 Extracellular. {ECO:0000305}.; TOPO_DOM 381 387 Extracellular. {ECO:0000305}.; TOPO_DOM 409 751 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 771 781 Extracellular. {ECO:0000305}.; TOPO_DOM 802 815 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 836 837 Extracellular. {ECO:0000305}.; TOPO_DOM 856 871 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 891 919 Extracellular. {ECO:0000305}.; TOPO_DOM 941 953 Extracellular. {ECO:0000305}.; TOPO_DOM 975 1197 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1216 1228 Extracellular. {ECO:0000305}.; TOPO_DOM 1248 1261 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1281 1288 Extracellular. {ECO:0000305}.; TOPO_DOM 1308 1324 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1345 1397 Extracellular. {ECO:0000305}.; TOPO_DOM 1420 1436 Extracellular. {ECO:0000305}.; TOPO_DOM 1459 1521 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1540 1550 Extracellular. {ECO:0000305}.; TOPO_DOM 1570 1581 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1600 1612 Extracellular. {ECO:0000305}.; TOPO_DOM 1630 1648 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1667 1688 Extracellular. {ECO:0000305}.; TOPO_DOM 1712 1740 Extracellular. {ECO:0000305}.; TOPO_DOM 1764 1978 Cytoplasmic. {ECO:0000305}. FUNCTION: Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient. In macrophages, isoform 5 may participate in the control of podosome and invadopodia formation. {ECO:0000269|PubMed:19136557}. PTM: May be ubiquitinated by NEDD4L; which would promote its endocytosis. {ECO:0000250}.; PTM: Phosphorylation at Ser-1495 by PKC in a highly conserved cytoplasmic loop slows inactivation of the sodium channel and reduces peak sodium currents. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19136557}; Multi-pass membrane protein {ECO:0000269|PubMed:19136557}. SUBUNIT: The voltage-sensitive sodium channel consists of an ion conducting pore forming alpha-subunit regulated by one or more beta-1 (SCN1B), beta-2 (SCN2B), beta-3 (SCN3B) and/or beta-4 (SCN4B). Beta-1 (SCN1B) and beta-3 (SCN3B) are non-covalently associated with alpha, while beta-2 (SCN2B) and beta-4 (SCN4B) are covalently linked by disulfide bonds. Interacts with FGF13 (By similarity). Interacts with NEDD4 and NEDD4L (PubMed:15123669). Interacts with FGF14, GBG3, GBB2 and SCN1B (By similarity). Interacts with the conotoxin GVIIJ. {ECO:0000250|UniProtKB:O88420, ECO:0000250|UniProtKB:Q9UQD0, ECO:0000269|PubMed:15123669}. DOMAIN: The sequence contains 4 internal repeats, each with 5 hydrophobic segments (S1, S2, S3, S5, S6) and one positively charged segment (S4). Segments S4 are probably the voltage-sensors and are characterized by a series of positively charged amino acids at every third position. {ECO:0000305}. TISSUE SPECIFICITY: Expressed in brain, cerebellum and spinal cord. Isoform 5 may be expressed in non-neuronal tissues, such as peritoneal macrophages. {ECO:0000269|PubMed:19136557, ECO:0000269|PubMed:7670495}. DISEASE: Note=Defects in Scn8a are the cause of motor endplate disease (med). Med is a recessive neuromuscular disorder that is characterized by lack of signal transmission at the neuromuscular junction, excess preterminal arborization and degeneration of cerebellar Purkinje cells. It produces early onset progressive paralysis of hind limbs, severe muscle atrophy and juvenile lethality.; DISEASE: Note=Defects in Scn8a are the cause of the jolting mutant (medjo), a mild form of motor endplate disease which is characterized by the absence of spontaneous, regular, simple discharges from Purkinje cells. After 3 weeks of age, jolting mice are unsteady and have wide-based gait and a rhythmical tremor of head and neck induced by attempted movement. {ECO:0000269|PubMed:7670495, ECO:0000269|PubMed:8815882}.; DISEASE: Note=Defects in Scn8a are a cause of degenerating muscle (dmu). Dmu is an autosomal recessive neuromuscular disorder that is characterized by skeletal and cardiac muscle degeneration. It produces early onset progressive loss of mobility of the hind limbs and subsequent lethality in the first month of life. {ECO:0000269|PubMed:11532991, ECO:0000305|PubMed:8663325}. +Q9DCT5 SDF2_MOUSE Stromal cell-derived factor 2 (SDF-2) 211 23,159 Chain (1); Domain (3); Erroneous initiation (1); Sequence conflict (3); Signal peptide (1) SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Ubiquitously expressed with highest expression in liver and kidney. +Q80UF4 SDCG8_MOUSE Serologically defined colon cancer antigen 8 homolog (Centrosomal colon cancer autoantigen protein) (mCCCAP) 717 82,979 Chain (1); Coiled coil (4); Compositional bias (2); Modified residue (2); Region (1) FUNCTION: Plays a role in the establishment of cell polarity and epithelial lumen formation. May play a role in ciliogenesis. {ECO:0000269|PubMed:20835237}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:12559564, ECO:0000269|PubMed:20835237}. Cell junction {ECO:0000250}. Note=Located at the distal ends of both centrioles and colocalizes to centrosomes throughout the cell cycle. Pariculary prominent at the distal basal body and the transition zone of photoreceptors. SUBUNIT: Homodimer. Interacts with OFD1; the interaction is direct (By similarity). Interacts with FAM161A (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in liver, kidney, spleen, brain, heart and muscle. Expressed in photoreceptor cells of the retina. {ECO:0000269|PubMed:12559564, ECO:0000269|PubMed:20835237}. +Q8BTE0 SDHF4_MOUSE Succinate dehydrogenase assembly factor 4, mitochondrial (SDH assembly factor 4) (SDHAF4) 104 11,889 Chain (1); Sequence conflict (1); Transit peptide (1) FUNCTION: Plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol (PubMed:24954416). Binds to the flavoprotein subunit Sdha in its FAD-bound form, blocking the generation of excess reactive oxigen species (ROS) and facilitating its assembly with the iron-sulfur protein subunit Sdhb into the SDH catalytic dimer (By similarity). {ECO:0000250|UniProtKB:P38345, ECO:0000269|PubMed:24954416}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:P38345}. SUBUNIT: Interacts with Sdha in its FAD-bound form. {ECO:0000250|UniProtKB:P38345}. +Q8R3W5 SEN15_MOUSE tRNA-splicing endonuclease subunit Sen15 (tRNA-intron endonuclease Sen15) 168 18,530 Chain (1); Modified residue (2); Sequence conflict (1) FUNCTION: Non-catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5' and 3' splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and 5'-OH termini. There are no conserved sequences at the splice sites, but the intron is invariably located at the same site in the gene, placing the splice sites an invariant distance from the constant structural features of the tRNA body. The tRNA splicing endonuclease is also involved in mRNA processing via its association with pre-mRNA 3'-end processing factors, establishing a link between pre-tRNA splicing and pre-mRNA 3'-end formation, suggesting that the endonuclease subunits function in multiple RNA-processing events (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Nucleus, nucleolus {ECO:0000305}. Note=May be transiently localized in the nucleolus. {ECO:0000305}. SUBUNIT: Homodimer. tRNA splicing endonuclease is a heterotetramer composed of TSEN2, TSEN15, TSEN34/LENG5 and TSEN54. tRNA splicing endonuclease complex also contains proteins of the pre-mRNA 3' end processing machinery such as CLP1, CPSF1, CPSF4 and CSTF2 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q8WW01}. +Q8C650 SEP10_MOUSE Septin-10 452 52,422 Alternative sequence (1); Binding site (3); Chain (1); Domain (1); Modified residue (1); Nucleotide binding (2); Region (3); Sequence conflict (1) FUNCTION: Filament-forming cytoskeletal GTPase (By similarity). May play a role in cytokinesis (Potential). {ECO:0000250, ECO:0000305}. SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton {ECO:0000250}. SUBUNIT: Septins polymerize into heterooligomeric protein complexes that form filaments, and can associate with cellular membranes, actin filaments and microtubules. GTPase activity is required for filament formation (By similarity). {ECO:0000250}. +Q60519 SEM5B_MOUSE Semaphorin-5B (Semaphorin-G) (Sema G) 1093 120,327 Alternative sequence (3); Chain (1); Disulfide bond (18); Domain (8); Glycosylation (13); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 979 999 Helical. {ECO:0000255}. TOPO_DOM 20 978 Extracellular. {ECO:0000255}.; TOPO_DOM 1000 1093 Cytoplasmic. {ECO:0000255}. FUNCTION: May act as positive axonal guidance cues. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. TISSUE SPECIFICITY: In adult, only detected in brain. +Q9EP97 SENP3_MOUSE Sentrin-specific protease 3 (EC 3.4.22.-) (SUMO-1-specific protease 3) (Sentrin/SUMO-specific protease SENP3) (Smt3-specific isopeptidase 1) (Smt3ip1) 568 64,403 Active site (3); Chain (1); Compositional bias (2); Modified residue (9); Motif (2); Region (1); Sequence conflict (2) FUNCTION: Protease that releases SUMO2 and SUMO3 monomers from sumoylated substrates, but has only weak activity against SUMO1 conjugates. Deconjugates SUMO2 from MEF2D, which increases its transcriptional activation capability. Deconjugates SUMO2 and SUMO3 from CDCA8. Redox sensor that, when redistributed into nucleoplasm, can act as an effector to enhance HIF1A transcriptional activity by desumoylating EP300. Required for rRNA processing through deconjugation of SUMO2 and SUMO3 from nucleophosmin. Plays a role in the regulation of sumoylation status of ZNF148. Functions as a component of the Five Friends of Methylated CHTOP (5FMC) complex; the 5FMC complex is recruited to ZNF148 by methylated CHTOP, leading to desumoylation of ZNF148 and subsequent transactivation of ZNF148 target genes. {ECO:0000269|PubMed:11029585, ECO:0000269|PubMed:22872859}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11029585}. Nucleus, nucleoplasm {ECO:0000269|PubMed:22872859}. Cytoplasm {ECO:0000269|PubMed:22872859}. Note=Redistributes between the nucleolus and the nucleoplasm in response to mild oxidative stress (By similarity). Mainly found in the nucleoplasm, with low levels detected in the cytoplasmic and chromatin fractions (PubMed:22872859). {ECO:0000250|UniProtKB:Q9H4L4, ECO:0000269|PubMed:22872859}. SUBUNIT: Binds to SUMO1 and SUMO3. Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Interacts with EP300, NPM1 and CDCA8 (By similarity). Component of the 5FMC complex, at least composed of PELP1, LAS1L, TEX10, WDR18 and SENP3; the complex interacts with methylated CHTOP and ZNF148. Interacts with NOL9. Interacts with CCAR2 (By similarity). {ECO:0000250|UniProtKB:Q9H4L4, ECO:0000269|PubMed:22872859}. +Q9Z2Q6 SEPT5_MOUSE Septin-5 (Cell division control-related protein 1) (CDCrel-1) (Peanut-like protein 1) 369 42,748 Binding site (4); Chain (1); Coiled coil (1); Domain (1); Modified residue (5); Nucleotide binding (2); Region (3) FUNCTION: Filament-forming cytoskeletal GTPase (By similarity). Involved in cytokinesis (Potential). May play a role in platelet secretion. {ECO:0000250, ECO:0000269|PubMed:11880646, ECO:0000305}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. SUBUNIT: Septins polymerize into heterooligomeric protein complexes that form filaments, and can associate with cellular membranes, actin filaments and microtubules. GTPase activity is required for filament formation (By similarity). Interacts with SEPT2 and SEPT5. Interaction with SEPT4 not detected. In platelets, associated with a complex containing STX4 (By similarity). Interacts with PRKN. This interaction leads to SEPT5 ubiquitination and degradation. {ECO:0000250, ECO:0000269|PubMed:11078524, ECO:0000269|PubMed:11739749}. +Q3UTY6 THSD4_MOUSE Thrombospondin type-1 domain-containing protein 4 (A disintegrin and metalloproteinase with thrombospondin motifs-like protein 6) (ADAMTS-like protein 6) (ADAMTSL-6) (ADAMTS-like protein 4) (ADAMTSL-4) 1018 113,243 Alternative sequence (2); Chain (1); Domain (7); Sequence conflict (2); Signal peptide (1) FUNCTION: Promotes FBN1 matrix assembly. Attenuates TGFB signaling, possibly by accelerating the sequestration of large latent complexes of TGFB or active TGFB by FBN1 microfibril assembly, thereby negatively regulating the expression of TGFB regulatory targets, such as POSTN. {ECO:0000269|PubMed:18757743, ECO:0000269|PubMed:19940141, ECO:0000269|PubMed:21880733}. SUBCELLULAR LOCATION: Isoform 1: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:18757743, ECO:0000269|PubMed:19940141}. Note=Mostly deposited into pericellular fibrillar matrices (PubMed:19940141). Colocalizes with FBN1 (PubMed:19940141). {ECO:0000269|PubMed:19940141}.; SUBCELLULAR LOCATION: Isoform 2: Secreted {ECO:0000269|PubMed:19940141}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:18757743, ECO:0000269|PubMed:19940141}. Note=Mostly secreted in the extracellular milieu (PubMed:19940141). In the pericellular fibrillar matrix, colocalizes with FBN1 (PubMed:19940141) (PubMed:21880733). {ECO:0000269|PubMed:19940141, ECO:0000269|PubMed:21880733}. SUBUNIT: Isoform 2 interacts with FBN1. Isoform 2 may interact with TGFB1. {ECO:0000269|PubMed:19940141, ECO:0000269|PubMed:21880733}. TISSUE SPECIFICITY: Both isoforms are expressed in the embryo from 7 dpc through 17. Isoform 1 is widely expressed in adult tissues. Isoform 2 is detected in brain, spinal cord, eye, kidney, stomach and uterus. Mainly observed in fibrillar extracellular matrices in elastic tissues (at protein level). {ECO:0000269|PubMed:19940141}. +Q9EPB5 SERHL_MOUSE Serine hydrolase-like protein (SHL) (EC 3.1.-.-) 311 35,311 Active site (1); Chain (1); Domain (1); Modified residue (1); Sequence conflict (1) FUNCTION: Probable serine hydrolase. May be related to cell muscle hypertrophy. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Peroxisome. Note=Concentrated in perinuclear vesicles. May be located in peroxisomes. TISSUE SPECIFICITY: Ubiquitous. High protein expression in skeletal and cardiac muscle. +Q99J99 THTM_MOUSE 3-mercaptopyruvate sulfurtransferase (MST) (EC 2.8.1.2) 297 33,097 Active site (1); Beta strand (9); Binding site (1); Chain (1); Disulfide bond (1); Domain (2); Helix (15); Initiator methionine (1); Modified residue (6); Mutagenesis (3); Region (1); Sequence conflict (4) FUNCTION: Transfer of a sulfur ion to cyanide or to other thiol compounds. Also has weak rhodanese activity. Detoxifies cyanide and is required for thiosulfate biosynthesis. Acts as an antioxidant. In combination with cysteine aminotransferase (CAT), contributes to the catabolism of cysteine and is an important producer of hydrogen sulfide in the brain, retina and vascular endothelial cells. Hydrogen sulfide H(2)S is an important synaptic modulator, signaling molecule, smooth muscle contractor and neuroprotectant. Its production by the 3MST/CAT pathway is regulated by calcium ions. {ECO:0000269|PubMed:18855522, ECO:0000269|PubMed:21937432, ECO:0000269|PubMed:22808324, ECO:0000269|PubMed:28079151}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P97532}. Mitochondrion {ECO:0000269|PubMed:18855522}. Cell junction, synapse, synaptosome {ECO:0000269|PubMed:18855522}. SUBUNIT: Monomer (active form). Homodimer; disulfide-linked (inactive form). {ECO:0000250|UniProtKB:P97532}. DOMAIN: Contains two rhodanese domains with different primary structures but with near identical secondary structure conformations suggesting a common evolutionary origin. Only the C-terminal rhodanese domain contains the catalytic cysteine residue (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the brain and retina. In the retina, localized to the inner and outer plexiform layer, the inner and outer nuclear layer and the outer segments of photoreceptors. In the brain, localized to neurons of mitral cell layers, glomerular, and external plexiform layers in the olfactory bulb. Also found in Purkinje cell stomata and proximal dendrites. In the spinal cord, localized to large neurons. In the cerebral cortex, localized to pyramidial neurons in layers II/III and V, and in layers I-VI of neocortical areas. In the hippocampus, found in CA1 and CA3 pyramidal cells. {ECO:0000269|PubMed:18855522, ECO:0000269|PubMed:21937432, ECO:0000269|PubMed:22808324}. +Q8JZL3 THTPA_MOUSE Thiamine-triphosphatase (ThTPase) (EC 3.6.1.28) 224 24,264 Beta strand (9); Binding site (7); Chain (1); Domain (1); Helix (9); Initiator methionine (1); Metal binding (5); Modified residue (1); Turn (2) FUNCTION: Hydrolase highly specific for thiamine triphosphate (ThTP). {ECO:0000269|PubMed:18276586}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000269|PubMed:18276586}. +P52196 THTR_MOUSE Thiosulfate sulfurtransferase (EC 2.8.1.1) (Rhodanese) 297 33,466 Active site (1); Binding site (2); Chain (1); Domain (2); Glycosylation (1); Modified residue (15); Region (1) FUNCTION: Together with MRPL18, acts as a mitochondrial import factor for the cytosolic 5S rRNA. Only the nascent unfolded cytoplasmic form is able to bind to the 5S rRNA (By similarity). Formation of iron-sulfur complexes and cyanide detoxification. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion matrix. SUBUNIT: Monomer. DOMAIN: Contains two rhodanese domains with different primary structures but with near identical secondary structure conformations suggesting a common evolutionary origin. Only the C-terminal rhodanese domain contains the catalytic cysteine residue (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in numerous tissues. +Q99J36 THUM1_MOUSE THUMP domain-containing protein 1 350 38,885 Chain (1); Domain (1); Initiator methionine (1); Modified residue (6) FUNCTION: Functions as a tRNA-binding adapter to mediate NAT10-dependent tRNA acetylation. {ECO:0000250|UniProtKB:Q9NXG2}. SUBUNIT: Interacts with NAT10. {ECO:0000250|UniProtKB:Q9NXG2}. +Q9CZB3 THUM2_MOUSE THUMP domain-containing protein 2 528 57,669 Chain (1); Domain (1) +P97770 THUM3_MOUSE THUMP domain-containing protein 3 (GtROSA26asSor) 505 56,431 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (1); Sequence conflict (5) TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:9108056}. +A2AKX3 SETX_MOUSE Probable helicase senataxin (EC 3.6.4.-) (Amyotrophic lateral sclerosis 4 protein homolog) (SEN1 homolog) 2646 297,589 Alternative sequence (1); Chain (1); Cross-link (5); Frameshift (1); Modified residue (12); Motif (1); Nucleotide binding (1); Region (1); Sequence caution (1); Sequence conflict (2) FUNCTION: Probable RNA/DNA helicase involved in diverse aspects of RNA metabolism and genomic integrity. Plays a role in transcription regulation by its ability to modulate RNA Polymerase II (Pol II) binding to chromatin and through its interaction with proteins involved in transcription. Contributes to the mRNA splicing efficiency and splice site selection. Required for the resolution of R-loop RNA-DNA hybrid formation at G-rich pause sites located downstream of the poly(A) site, allowing XRN2 recruitment and XRN2-mediated degradation of the downstream cleaved RNA and hence efficient RNA polymerase II (RNAp II) transcription termination (By similarity). Required for the 3' transcriptional termination of PER1 and CRY2, thus playing an important role in the circadian rhythm regulation (PubMed:22767893). Involved in DNA double-strand breaks damage response generated by oxidative stress. In association with RRP45, targets the RNA exosome complex to sites of transcription-induced DNA damage (By similarity). Plays a role in the development and maturation of germ cells: essential for male meiosis, acting at the interface of transcription and meiotic recombination, and in the process of gene silencing during meiotic sex chromosome inactivation (MSCI) (PubMed:23593030). Plays a role in neurite outgrowth in hippocampal cells through FGF8-activated signaling pathways. Inhibits retinoic acid-induced apoptosis. May be involved in telomeric stability through the regulation of telomere repeat-containing RNA (TERRA) transcription (By similarity). {ECO:0000250|UniProtKB:Q7Z333, ECO:0000269|PubMed:22767893, ECO:0000269|PubMed:23593030}. PTM: Ubiquitinated. {ECO:0000250|UniProtKB:Q7Z333}.; PTM: Sumoylated preferentially with SUMO2 or SUMO3. {ECO:0000250|UniProtKB:Q7Z333}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q7Z333}. Nucleus, nucleoplasm {ECO:0000269|PubMed:16644229}. Nucleus, nucleolus {ECO:0000269|PubMed:16644229}. Cytoplasm {ECO:0000269|PubMed:16644229}. Chromosome {ECO:0000269|PubMed:23593030}. Chromosome, telomere {ECO:0000250|UniProtKB:Q7Z333}. Cell projection, axon {ECO:0000250|UniProtKB:Q7Z333}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q7Z333}. Note=Most abundant in the nucleus (By similarity). Detected in granules (By similarity). Colocalized in cycling cells with FBL in the nucleolus. Localizes with telomeric DNA in a transcription-dependent manner. Under replication stress, colocalizes with a variety of DNA damage signaling and repair response proteins at distinct nuclear foci in mitotic S/G2- and G1-phase cells in a transcription- and RNA/DNA hybrid-dependent manner. Localizes at limited number of nuclear foci. Colocalizes with EXOSC9 in nuclear foci upon induction of transcription-related DNA damage at the S phase (By similarity). At pachytene stage, colocalizes predominantly to the heterochromatic XY-body of sex chromosomes with DNA damage response proteins in a BRCA1-dependent manner (PubMed:23593030). May be detected in the nucleolus only in cycling cells (PubMed:16644229). {ECO:0000250|UniProtKB:Q7Z333, ECO:0000269|PubMed:16644229, ECO:0000269|PubMed:23593030}. SUBUNIT: Homodimer (By similarity). Interacts with PER2; the interaction inhibits termination of circadian target genes (PubMed:22767893). Interacts with CHD4, POLR2A, PRKDC and TRIM28. Does not interact with C14orf178. Interacts with UBE2I. Interacts (via N-terminus domain) with EXOSC9 (via C-terminus region); the interaction enhances SETX sumoylation. Interacts with NCL (via N-terminus domain). Interacts with PABPN1, PABPC1 and SF3B1. Interacts with SMN1/SMN2 and POLR2A; SMN1/SMN2 recruits SETX to POLR2A (By similarity). {ECO:0000250|UniProtKB:Q7Z333, ECO:0000269|PubMed:22767893}. DOMAIN: The N-terminus domain is necessary for S/G2 nuclear foci localization. {ECO:0000250|UniProtKB:Q7Z333}. TISSUE SPECIFICITY: Expressed in cerebellum, hippocampus, olfactory bulb, Bergmann glial fibers, stellate cells and Purkinje cells. Expressed in the epithelial cells of the lens but not in mature lens fiber cells. Expressed in the retina (highly expressed in inner and outer segments of photoreceptors and outer plexiform layer cells but weakly expressed in the inner plexiform and ganglion cell layers). Expressed in the kidney. {ECO:0000269|PubMed:16644229}. +Q3UZY0 SFI1_MOUSE Protein SFI1 homolog 1216 144,033 Alternative sequence (8); Chain (1); Erroneous initiation (1); Region (3); Repeat (5); Sequence conflict (6) FUNCTION: Plays a role in the dynamic structure of centrosome-associated contractile fibers via its interaction with CETN2. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250}. Note=Localized close to the centriole. {ECO:0000250}. SUBUNIT: Interacts with CETN2 (via C-terminus). {ECO:0000250}. DOMAIN: CETN2-binding regions contains a conserved Trp residue in their C-terminal ends, which seems critical for interaction with CETN2. +Q3USH5 SFSWA_MOUSE Splicing factor, suppressor of white-apricot homolog (Splicing factor, arginine/serine-rich 8) (Suppressor of white apricot protein homolog) 945 104,190 Chain (1); Coiled coil (1); Compositional bias (4); Modified residue (9); Repeat (2) FUNCTION: Plays a role as an alternative splicing regulator. Regulates its own expression at the level of RNA processing. Also regulates the splicing of fibronectin and CD45 genes. May act, at least in part, by interaction with other R/S-containing splicing factors. Represses the splicing of MAPT/Tau exon 10 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q5U4C3 SFR19_MOUSE Splicing factor, arginine/serine-rich 19 (SR-related and CTD-associated factor 1) 1256 133,842 Alternative sequence (2); Chain (1); Compositional bias (8); Cross-link (1); Modified residue (27); Region (1) FUNCTION: May function in pre-mRNA splicing. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with POLR2A. {ECO:0000250}. +Q99JR1 SFXN1_MOUSE Sideroflexin-1 322 35,649 Chain (1); Frameshift (1); Initiator methionine (1); Modified residue (1); Transmembrane (5) TRANSMEM 103 120 Helical. {ECO:0000255}.; TRANSMEM 147 167 Helical. {ECO:0000255}.; TRANSMEM 175 195 Helical. {ECO:0000255}.; TRANSMEM 229 249 Helical. {ECO:0000255}.; TRANSMEM 267 287 Helical. {ECO:0000255}. FUNCTION: Might be involved in the transport of a component required for iron utilization into or out of the mitochondria. SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Widely expressed, with highest expression in kidney and liver. {ECO:0000269|PubMed:11274051}. DISEASE: Note=Defects in Sfxn1 are the cause of a transitory hypochromic, microcytic anemia characterized by a large number of siderocytes containing non-heme iron granules. The anemia begins at 12 dpc, is most intense at 15 dpc and is still severe at birth, but disappears by 2 weeks of age. Mutant adults are no longer anemic, but they have an impaired response to hemopoietic stress. Most homozygotes also have flexed tails and a belly spot. {ECO:0000269|PubMed:11274051}. +O70258 SGCE_MOUSE Epsilon-sarcoglycan (Epsilon-SG) 437 49,736 Alternative sequence (1); Chain (1); Compositional bias (1); Erroneous initiation (3); Glycosylation (1); Mutagenesis (2); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 318 338 Helical. {ECO:0000255}. TOPO_DOM 1 317 Extracellular. {ECO:0000255}.; TOPO_DOM 339 437 Cytoplasmic. {ECO:0000255}. FUNCTION: Component of the sarcoglycan complex, a subcomplex of the dystrophin-glycoprotein complex which forms a link between the F-actin cytoskeleton and the extracellular matrix. PTM: N-glycosylated. {ECO:0000269|PubMed:17200151}.; PTM: Ubiquitinated, leading to its degradation by the proteasome. {ECO:0000269|PubMed:17200151}. SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000269|PubMed:17200151}; Single-pass membrane protein {ECO:0000269|PubMed:17200151}. Golgi apparatus {ECO:0000269|PubMed:17200151}. Cell projection, dendrite {ECO:0000269|PubMed:17200151}. Cytoplasm, cytoskeleton {ECO:0000250}. TISSUE SPECIFICITY: Identified in all tissues tested. Expression highest in lung and placenta, moderate in brain, heart and skeletal muscle, low in kidney and liver. Also detected in embryo. +Q7M742 SG1C1_MOUSE Secretoglobin family 1C member 1 (Secretoglobin RYD5) 95 10,571 Chain (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +Q920H1 SG3A2_MOUSE Secretoglobin family 3A member 2 (Pneumo secretory protein 1) (PnSP-1) (Uteroglobin-related protein 1) 91 9,819 Alternative sequence (2); Chain (1); Disulfide bond (1); Mutagenesis (1); Signal peptide (1) FUNCTION: Secreted cytokine-like protein (By similarity). Binds to the scavenger receptor MARCO (By similarity). Can also bind to pathogens including the Gram-positive bacterium L.monocytogenes, the Gram-negative bacterium P.aeruginosa, and yeast (By similarity). Strongly inhibits phospholipase A2 (PLA2G1B) activity (PubMed:24213919). Seems to have anti-inflammatory effects in respiratory epithelium (PubMed:16456148, PubMed:25242865). Also has anti-fibrotic activity in lung (PubMed:24213919, PubMed:26559674). May play a role in fetal lung development and maturation (PubMed:18535256). Promotes branching morphogenesis during early stages of lung development (PubMed:18535256). In the pituitary, may inhibit production of follicle-stimulating hormone (FSH) and luteinizing hormone (LH) (PubMed:24514953). {ECO:0000250|UniProtKB:Q96PL1, ECO:0000269|PubMed:16456148, ECO:0000269|PubMed:18535256, ECO:0000269|PubMed:24213919, ECO:0000269|PubMed:24514953, ECO:0000269|PubMed:25242865, ECO:0000269|PubMed:26559674}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11682631}. SUBUNIT: Homodimer; disulfide-linked (PubMed:11682631, PubMed:24213919). Monomer (PubMed:11682631, PubMed:24213919). Interacts with APOA1 (By similarity). {ECO:0000250|UniProtKB:Q96PL1, ECO:0000269|PubMed:11682631, ECO:0000269|PubMed:24213919}. TISSUE SPECIFICITY: Highly expressed in lung where it localizes to epithelial cells of the trachea, bronchus and bronchioles (at protein level) (PubMed:11682631, PubMed:12406855, PubMed:12175512, PubMed:25242865). Expressed in club/Clara cells of the bronchioles (PubMed:12406855). Also detected in the anterior and posterior lobes of the pituitary gland where it may localize to gonadotropic cells (at protein level) (PubMed:24514953). Not detected in other tissues tested (PubMed:11682631, PubMed:12175512). {ECO:0000269|PubMed:11682631, ECO:0000269|PubMed:12175512, ECO:0000269|PubMed:12406855, ECO:0000269|PubMed:24514953, ECO:0000269|PubMed:25242865}. +Q7TSY8 SGO2_MOUSE Shugoshin 2 (Shugoshin-2) (Shugoshin-like 2) 1164 130,277 Chain (1); Coiled coil (1); Modified residue (1); Sequence caution (1); Sequence conflict (1) FUNCTION: Cooperates with PPP2CA to protect centromeric cohesin from separase-mediated cleavage in oocytes specifically during meiosis I. Has a crucial role in protecting REC8 at centromeres from cleavage by separase. During meiosis, protects centromeric cohesion complexes until metaphase II/anaphase II transition, preventing premature release of meiosis-specific REC8 cohesin complexes from anaphase I centromeres. Is thus essential for an accurate gametogenesis. May act by targeting PPP2CA to centromeres, thus leading to cohesin dephosphorylation. Essential for recruiting KIF2C to the inner centromere and for correcting defective kinetochore attachments. Involved in centromeric enrichment of AUKRB in prometaphase. {ECO:0000250|UniProtKB:Q562F6, ECO:0000269|PubMed:18084284, ECO:0000269|PubMed:18765791}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q562F6}. Chromosome, centromere {ECO:0000269|PubMed:17205076, ECO:0000269|PubMed:18084284}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:17205076}. Note=Centromeric localization requires the presence of BUB1 and AUKRB (By similarity). During meiosis I, accumulates at centromeres during diplotene, and colocalizes differentially with the cohesin subunits RAD21 and REC8 at metaphase I centromeres (PubMed:17205076) (PubMed:18084284). SGO2 and RAD21 change their relative distributions during telophase I when sister-kinetochore association is lost (PubMed:17205076). During meiosis II, it shows a striking tension-dependent redistribution within centromeres throughout chromosome congression during prometaphase II, as it does during mitosis (PubMed:17205076). {ECO:0000250|UniProtKB:Q562F6, ECO:0000269|PubMed:17205076, ECO:0000269|PubMed:18084284}. SUBUNIT: Interacts with PPP2CA. Part of an astrin (SPAG5)-kinastrin (SKAP) complex containing KNSTRN, SPAG5, PLK1, DYNLL1 and SGO2. Interacts with CDCA8 (By similarity). {ECO:0000250|UniProtKB:Q562F6}. TISSUE SPECIFICITY: Ubiquitously expressed in proliferating cells. Highly expressed in the testis and oocytes. {ECO:0000269|PubMed:18084284}. +Q9Z0V7 TI17B_MOUSE Mitochondrial import inner membrane translocase subunit Tim17-B 172 18,352 Chain (1); Disulfide bond (1); Transmembrane (3) TRANSMEM 17 37 Helical. {ECO:0000255}.; TRANSMEM 61 77 Helical. {ECO:0000255}.; TRANSMEM 113 133 Helical. {ECO:0000255}. FUNCTION: Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SUBUNIT: Component of the TIM23 complex at least composed of TIMM23, TIMM17 (TIMM17A or TIMM17B) and TIMM50. The complex interacts with the TIMM44 component of the PAM complex. The complex also interacts with DNAJC15 (By similarity). {ECO:0000250}. +Q8C120 SH3R3_MOUSE E3 ubiquitin-protein ligase SH3RF3 (EC 2.3.2.27) (Plenty of SH3s 2) (SH3 domain-containing RING finger protein 3) (SH3 multiple domains protein 4) 878 93,130 Alternative sequence (8); Chain (1); Domain (4); Modified residue (2); Region (1); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: Has E3 ubiquitin-protein ligase activity. {ECO:0000250|UniProtKB:Q8TEJ3}. PTM: Autoubiquitinated. {ECO:0000250|UniProtKB:Q8TEJ3}. SUBUNIT: Interacts (via SH3 domain 3) with PAK2. Interacts with RAC1 (GTP-bound form). {ECO:0000250|UniProtKB:Q8TEJ3}. DOMAIN: The RING finger domain is required for ubiquitin ligase activity and autoubiquitination. {ECO:0000250|UniProtKB:Q8TEJ3}. +Q8BPQ7 SGSM1_MOUSE Small G protein signaling modulator 1 (RUN and TBC1 domain-containing protein 2) 1093 123,196 Alternative sequence (2); Beta strand (10); Chain (1); Domain (2); Helix (6); Mutagenesis (7); Region (2); Sequence conflict (2); Turn (3) FUNCTION: Interacts with numerous Rab family members, functioning as Rab effector for some, and as GTPase activator for others. Promotes GTP hydrolysis by RAB34 and RAB36. Probably functions as GTPase effector with RAB9A and RAB9B; does not stimulate GTP hydrolysis with RAB9A and RAB9B. {ECO:0000250|UniProtKB:Q2NKQ1}. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:17509819}. Cytoplasm {ECO:0000269|PubMed:25220469}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:25220469}; Peripheral membrane protein {ECO:0000269|PubMed:25220469}. Note=Recruited to cytoplasmic vesicle membranes via its interaction with Rab family members, such as RAB9A. {ECO:0000269|PubMed:25220469}. SUBUNIT: Interacts with RAB9A (GTP-bound form) and RAB9B (PubMed:25220469). Interacts with RAB3A, RAB4A, RAB5A, RAB8A, RAB11A, RAP1A, RAP1B, RAP2A and RAP2B. No interaction with RAB27A (By similarity). {ECO:0000250|UniProtKB:Q2NKQ1, ECO:0000269|PubMed:25220469}. TISSUE SPECIFICITY: Expressed only in brain. {ECO:0000269|PubMed:17509819}. +Q45HK4 SH21C_MOUSE SH2 domain-containing protein 1B2 (EAT-2-related transducer) (ERT) (EAT-2B) 132 15,044 Chain (1); Domain (1); Natural variant (1) FUNCTION: Cytoplasmic adapter regulating receptors of the signaling lymphocytic activation molecule (SLAM) family. In SLAM signaling may cooperate with Sh2d1a/SAP. Plays a role in regulation of effector functions of natural killer (NK) cells by controlling signal transduction through Cd244/2b4. However, conflicting results are reported which may reflect the use of different strain backgrounds. Proposed to act as an inhibitor of Cd244-mediated NK cell function including cytotoxicity and IFN-gamma production, the latter found also by triggering Klra4 and Klrk1 next to Cd244 (PubMed:16127454). Seems to positively regulate Cd244- and Cd84-dependent NK cell functions implicating Cd244-mediated phosphorylation of Vav1 (PubMed:20962259). {ECO:0000269|PubMed:16127454, ECO:0000269|PubMed:20962259}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. SUBUNIT: Interacts with SLAMF1 (phosphorylated). Interacts with CD244. Interacts with Src kinases HCK, LYN, FYN, FGR and LCK (via kinase domains). {ECO:0000269|PubMed:16127454, ECO:0000269|PubMed:16425036}. TISSUE SPECIFICITY: Expressed in spleen. Expressed in macrophages, CD8(+) T-Cells and NK cells (PubMed:16425036). Conflictingly found only in NK cells (PubMed:16127454). {ECO:0000269|PubMed:16127454, ECO:0000269|PubMed:16425036}. +Q810K3 SGPP2_MOUSE Sphingosine-1-phosphate phosphatase 2 (SPPase2) (Spp2) (EC 3.1.3.-) (Sphingosine-1-phosphatase 2) 354 40,248 Active site (2); Chain (1); Region (3); Site (1); Transmembrane (9) TRANSMEM 43 63 Helical. {ECO:0000255}.; TRANSMEM 76 96 Helical. {ECO:0000255}.; TRANSMEM 115 135 Helical. {ECO:0000255}.; TRANSMEM 140 160 Helical. {ECO:0000255}.; TRANSMEM 173 193 Helical. {ECO:0000255}.; TRANSMEM 202 222 Helical. {ECO:0000255}.; TRANSMEM 235 255 Helical. {ECO:0000255}.; TRANSMEM 273 293 Helical. {ECO:0000255}.; TRANSMEM 334 354 Helical. {ECO:0000255}. FUNCTION: Has specific phosphohydrolase activity towards sphingoid base 1-phosphates. Has high phosphohydrolase activity against dihydrosphingosine-1-phosphate and sphingosine-1-phosphate (S1P) in vitro. May play a role in attenuating intracellular sphingosine 1-phosphate (S1P) signaling. May play a role in pro-inflammatory signaling (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q9JJU8 SH3L1_MOUSE SH3 domain-binding glutamic acid-rich-like protein 114 12,811 Chain (1); Motif (1) +Q8C0T5 SI1L1_MOUSE Signal-induced proliferation-associated 1-like protein 1 (SIPA1-like protein 1) 1782 197,031 Alternative sequence (2); Chain (1); Coiled coil (1); Compositional bias (3); Domain (2); Modified residue (42); Sequence conflict (2) FUNCTION: Stimulates the GTPase activity of RAP2A. Promotes reorganization of the actin cytoskeleton and recruits DLG4 to F-actin. Contributes to the regulation of dendritic spine morphogenesis (By similarity). {ECO:0000250}. PTM: Ubiquitinated and degraded by the SCF(BTRC) following phosphorylation by PLK2. {ECO:0000250}.; PTM: Phosphorylated at Ser-1328 by CDK5, creating a docking site for the POLO box domains of PLK2. Subsequently, PLK2 binds and phosphorylates SIPA1L1, leading to ubiquitination and degradation by the proteasome (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250}. Cell junction, synapse, synaptosome {ECO:0000250}. Note=Associated with the actin cytoskeleton. Detected at synapses and dendritic spines of cultured hippocampal neurons (By similarity). {ECO:0000250}. SUBUNIT: Interacts with DLG4, PDLIM5, PDLIM7 and LZTS3. Interacts with the actin cytoskeleton (By similarity). Interacts (via PDZ domain) with EPHA4 (via PDZ motif); controls neuronal morphology through regulation of the RAP1 (RAP1A or RAP1B) and RAP2 (RAP2A, RAP2B or RAP2C) GTPases. {ECO:0000250, ECO:0000269|PubMed:18094260}. +G3X9J0 SI1L3_MOUSE Signal-induced proliferation-associated 1-like protein 3 (SIPA1-like protein 3) (SPA-1-like protein 3) 1776 195,063 Chain (1); Coiled coil (1); Domain (2); Modified residue (13) FUNCTION: Plays a critical role in epithelial cell morphogenesis, polarity, adhesion and cytoskeletal organization in the lens (PubMed:26231217). {ECO:0000269|PubMed:26231217}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:O60292}. Note=Detected in tricellular junctions. Colocalizes with apical F-actin. {ECO:0000250|UniProtKB:O60292}. +P61092 SIA1A_MOUSE E3 ubiquitin-protein ligase SIAH1A (EC 2.3.2.27) (RING-type E3 ubiquitin transferase SIAH1A) (Seven in absentia homolog 1a) (Siah-1a) (Siah1a) (mSiah-1a) 282 31,137 Beta strand (9); Chain (1); Helix (8); Metal binding (8); Modified residue (1); Mutagenesis (4); Region (1); Turn (2); Zinc finger (2) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates E3 ubiquitin ligase activity either through direct binding to substrates or by functioning as the essential RING domain subunit of larger E3 complexes. Triggers the ubiquitin-mediated degradation of many substrates, including proteins involved in transcription regulation (ELL2, MYB, POU2AF1, PML and RBBP8), a cell surface receptor (DCC), the cell-surface receptor-type tyrosine kinase FLT3, the cytoplasmic signal transduction molecules (KLF10/TIEG1 and NUMB), an antiapoptotic protein (BAG1), a microtubule motor protein (KIF22), a protein involved in synaptic vesicle function in neurons (SYP), a structural protein (CTNNB1) and SNCAIP. Confers constitutive instability to HIPK2 through proteasomal degradation. It is thereby involved in many cellular processes such as apoptosis, tumor suppression, cell cycle, axon guidance, transcription, spermatogenesis and TNF-alpha signaling. Has some overlapping function with SIAH2. Required for completion of meiosis I in males. Induces apoptosis in cooperation with PEG3. Upon nitric oxid (NO) generation that follows apoptotic stimulation, interacts with S-nitrosylated GAPDH, mediating the translocation of GAPDH to the nucleus. GAPDH acts as a stabilizer of SIAH1, facilitating the degradation of nuclear proteins. {ECO:0000269|PubMed:10681424, ECO:0000269|PubMed:11884614, ECO:0000269|PubMed:16615911}. PTM: Phosphorylated on Ser-19 by ATM and ATR. This phosphorylation disrupts SIAH1 interaction with HIPK2, and subsequent proteasomal degradation of HIPK2 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Predominantly cytoplasmic. Partially nuclear. SUBUNIT: Homodimer. Interacts with group 1 glutamate receptors GRM1 and GRM5. Interacts with SNCAIP and HIPK2. Interacts with GAPDH; leading to stabilize SIAH1 (By similarity). Interacts with UBE2E2. Component of some large E3 complex composed of UBE2D1, SIAH1, CACYBP/SIP, SKP1, APC and TBL1X. Interacts with UBE2I. Interacts with alpha-tubulin. Interacts with PEG10, which may inhibit its activity (By similarity). Interacts with DAB1, which may inhibit its activity. Interacts with PEG3 and KLF10. {ECO:0000250, ECO:0000269|PubMed:10681424, ECO:0000269|PubMed:11742346, ECO:0000269|PubMed:12646221, ECO:0000269|PubMed:16615911}. DOMAIN: The RING-type zinc finger domain is essential for ubiquitin ligase activity.; DOMAIN: The SBD domain (substrate-binding domain) mediates the homodimerization and the interaction with substrate proteins. It is related to the TRAF family. {ECO:0000269|PubMed:11742346}. TISSUE SPECIFICITY: Widely expressed at low level in embryos and adults. Expressed at higher level in testis. Due to the high similarity between SIAH1A and SIAH1B, it is difficult to distinguish its own tissue specificity. {ECO:0000269|PubMed:8404535}. +P97797 SHPS1_MOUSE Tyrosine-protein phosphatase non-receptor type substrate 1 (SHP substrate 1) (SHPS-1) (Brain Ig-like molecule with tyrosine-based activation motifs) (Bit) (CD172 antigen-like family member A) (Inhibitory receptor SHPS-1) (MyD-1 antigen) (Signal-regulatory protein alpha-1) (Sirp-alpha-1) (mSIRP-alpha1) (p84) (CD antigen CD172a) 513 56,425 Alternative sequence (2); Beta strand (12); Chain (1); Disulfide bond (3); Domain (3); Glycosylation (14); Helix (1); Modified residue (4); Motif (5); Natural variant (15); Sequence conflict (16); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 374 394 Helical. {ECO:0000255}. TOPO_DOM 32 373 Extracellular. {ECO:0000255}.; TOPO_DOM 395 511 Cytoplasmic. {ECO:0000255}. FUNCTION: Immunoglobulin-like cell surface receptor for CD47. Acts as docking protein and induces translocation of PTPN6, PTPN11 and other binding partners from the cytosol to the plasma membrane. Supports adhesion of cerebellar neurons, neurite outgrowth and glial cell attachment. May play a key role in intracellular signaling during synaptogenesis and in synaptic function. Involved in the negative regulation of receptor tyrosine kinase-coupled cellular responses induced by cell adhesion, growth factors or insulin. Mediates negative regulation of phagocytosis, mast cell activation and dendritic cell activation. CD47 binding prevents maturation of immature dendritic cells and inhibits cytokine production by mature dendritic cells (By similarity). {ECO:0000250, ECO:0000269|PubMed:2303162}. PTM: N-glycosylated. {ECO:0000269|PubMed:10585853, ECO:0000269|PubMed:16944957, ECO:0000269|PubMed:9348339, ECO:0000269|PubMed:9507023, ECO:0000269|PubMed:9712903}.; PTM: Phosphorylated on tyrosine residues. {ECO:0000269|PubMed:9507023, ECO:0000269|PubMed:9712903}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Binds PTPN11 when tyrosine-phosphorylated, except in macrophages, where it primarily binds PTPN6. Binds GRB2 vitro. Binds FGR. Binds JAK2 irrespective of its phosphorylation status and forms a stable complex. Binds SCAP1 and/or SCAP2. The resulting complex recruits FYB1. Binds PTK2B (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in cerebral cortex, brain, spinal cord, cerebellum and spleen, and at much lower levels in kidney, thymus, heart, lung and liver. Within the cerebellum, highly expressed throughout the molecular layer, and in synaptic glomeruli in the granule cell layer. Detected in neurons of the hippocampus and dentate gyrus, and in olfactory bulb. Not detected in Purkinje cells. Highly expressed in the plexiform layers, optic fiber layer and the outer segments of the photoreceptor layer in the retina. Highly expressed in macrophages. Isoform 3 is detected at very low levels in all tissues tested. {ECO:0000269|PubMed:2303162, ECO:0000269|PubMed:9348339, ECO:0000269|PubMed:9712903, ECO:0000269|PubMed:9872987}. +P58681 TLR7_MOUSE Toll-like receptor 7 1050 121,837 Chain (1); Domain (1); Glycosylation (12); Repeat (28); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 838 858 Helical. {ECO:0000255}. TOPO_DOM 27 837 Extracellular. {ECO:0000255}.; TOPO_DOM 859 1050 Cytoplasmic. {ECO:0000255}. FUNCTION: Key component of innate and adaptive immunity. TLRs (Toll-like receptors) control host immune response against pathogens through recognition of molecular patterns specific to microorganisms. TLR7 is a nucleotide-sensing TLR which is activated by single-stranded RNA. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. {ECO:0000269|PubMed:14976261}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18305481}; Single-pass type I membrane protein {ECO:0000269|PubMed:18305481}. Endosome {ECO:0000269|PubMed:18305481}. Lysosome {ECO:0000269|PubMed:18305481}. Cytoplasmic vesicle, phagosome {ECO:0000269|PubMed:18305481}. Note=Relocalizes from endoplasmic reticulum to endosome and lysosome upon stimulation with agonist. SUBUNIT: Interacts with MYD88 via their respective TIR domains (By similarity). Interacts with UNC93B1. Interacts with SMPDL3B (PubMed:26095358). {ECO:0000250|UniProtKB:Q9NYK1, ECO:0000269|PubMed:17452530, ECO:0000269|PubMed:26095358}. +Q5SX79 SHRM1_MOUSE Protein Shroom1 823 89,951 Alternative sequence (1); Chain (1); Domain (2); Modified residue (9) FUNCTION: May be involved in the assembly of microtubule arrays during cell elongation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. SUBUNIT: Interacts with F-actin. {ECO:0000250}. DOMAIN: The ASD1 domain mediates F-actin binding. {ECO:0000250}. +A2ALU4 SHRM2_MOUSE Protein Shroom2 (Protein Apxl) 1481 164,703 Alternative sequence (1); Chain (1); Domain (3); Erroneous initiation (2); Frameshift (1); Modified residue (11); Sequence conflict (6) FUNCTION: May be involved in endothelial cell morphology changes during cell spreading. In the retinal pigment epithelium, may regulate the biogenesis of melanosomes and promote their association with the apical cell surface by inducing gamma-tubulin redistribution. {ECO:0000269|PubMed:16684770, ECO:0000269|PubMed:16987870}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:16684770}. Cell junction, tight junction {ECO:0000269|PubMed:16684770}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16684770}. Note=Associates with cortical F-actin. SUBUNIT: Interacts with F-actin. {ECO:0000269|PubMed:16684770}. DOMAIN: The ASD1 domain mediates F-actin binding. TISSUE SPECIFICITY: Present in kidney tubules and in the vasculature of many tissues (at protein level). {ECO:0000269|PubMed:16684770}. +Q9QXN0 SHRM3_MOUSE Protein Shroom3 1986 214,888 Alternative sequence (2); Chain (1); Coiled coil (1); Compositional bias (2); Domain (3); Frameshift (2); Modified residue (14); Sequence conflict (24) FUNCTION: Controls cell shape changes in the neuroepithelium during neural tube closure. Induces apical constriction in epithelial cells by promoting the apical accumulation of F-actin and myosin II, and probably by bundling stress fibers. Induces apicobasal cell elongation by redistributing gamma-tubulin and directing the assembly of robust apicobasal microtubule arrays. {ECO:0000269|PubMed:10589677, ECO:0000269|PubMed:14680628, ECO:0000269|PubMed:16249236, ECO:0000269|PubMed:16684770}. SUBCELLULAR LOCATION: Cell junction, adherens junction {ECO:0000269|PubMed:10589677}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10589677}. Note=Colocalizes with F-actin in stress fibers and adherens junctions. SUBUNIT: Interacts with F-actin. {ECO:0000269|PubMed:10589677}. DOMAIN: The ASD1 domain mediates F-actin binding.; DOMAIN: The ASD2 domain is required for apical constriction induction. +Q9ERE8 TLRN1_MOUSE Talin rod domain-containing protein 1 (Mesoderm development candidate 1) 362 37,786 Chain (1); Initiator methionine (1); Modified residue (1) FUNCTION: Actin-binding protein which may have an oncogenic function and regulates cell proliferation, migration and invasion in cancer cells. {ECO:0000250|UniProtKB:Q9H1K6}. SUBUNIT: May homodimerize. Interacts with F-actin. {ECO:0000269|PubMed:20610383}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11247670}. +O55144 TLX3_MOUSE T-cell leukemia homeobox protein 3 (Homeobox TLX-3) (Homeobox protein Hox-11L2) (Respiratory neuron homeobox protein) 291 31,837 Chain (1); DNA binding (1); Sequence conflict (1) SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q9CQG9 TM100_MOUSE Transmembrane protein 100 134 14,504 Chain (1); Modified residue (2); Mutagenesis (1); Transmembrane (2) TRANSMEM 56 76 Helical. {ECO:0000255}.; TRANSMEM 84 104 Helical. {ECO:0000255}. FUNCTION: Plays a role during embryonic arterial endothelium differentiation and vascular morphogenesis through the ACVRL1 receptor-dependent signaling pathway upon stimulation by bone morphogenetic proteins, such as GDF2/BMP9 and BMP10 (PubMed:22783020). Involved in the regulation of nociception, acting as a modulator of the interaction between TRPA1 and TRPV1, two molecular sensors and mediators of pain signals in dorsal root ganglia (DRG) neurons (PubMed:25640077). Mechanistically, it weakens their interaction, thereby releasing the inhibition of TRPA1 by TRPV1 and increasing the single-channel open probability of the TRPA1-TRPV1 complex (PubMed:25640077). {ECO:0000269|PubMed:22783020, ECO:0000269|PubMed:25640077}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23485812, ECO:0000269|PubMed:25640077}; Multi-pass membrane protein {ECO:0000269|PubMed:23485812, ECO:0000269|PubMed:25640077}. Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Perikaryon {ECO:0000269|PubMed:23485812}. Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Note=Colocalized with HSPA5 in the endoplasmic reticulum (ER). Enriched in ER microsome. Colocalized with BMP4 in neural cell bodies and neural fibers of the enteric nervous system (By similarity). {ECO:0000250}. SUBUNIT: Interacts (via C-terminus) with TRPA1 and TRPV1 (PubMed:25640077). {ECO:0000269|PubMed:25640077}. TISSUE SPECIFICITY: Expressed in dorsal root ganglia. Expressed in neurons as well as nerve fiber bundles connecting ganglia and fibers innervating muscle layer of the gastric body, jejunum, and proximal colon. Expressed in arterial endothelial cells and neurons of the central nervous system and peripheral nervous system (at protein level). Expressed strongly in lung, weakly in brain, heart and muscle. Expressed in enteric neurons and vascular tissue in the muscularis propria of the gastrointestinal tract. {ECO:0000269|PubMed:22783020, ECO:0000269|PubMed:23485812, ECO:0000269|PubMed:25640077}. +Q91VP7 TM101_MOUSE Transmembrane protein 101 257 28,783 Chain (1); Sequence conflict (1); Transmembrane (8) TRANSMEM 24 40 Helical. {ECO:0000255}.; TRANSMEM 52 72 Helical. {ECO:0000255}.; TRANSMEM 77 97 Helical. {ECO:0000255}.; TRANSMEM 110 130 Helical. {ECO:0000255}.; TRANSMEM 139 159 Helical. {ECO:0000255}.; TRANSMEM 182 202 Helical. {ECO:0000255}.; TRANSMEM 206 226 Helical. {ECO:0000255}.; TRANSMEM 233 253 Helical. {ECO:0000255}. FUNCTION: May activate NF-kappa-B signaling pathways. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q3UPR7 TM102_MOUSE Transmembrane protein 102 509 54,923 Chain (1); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 313 329 Helical. {ECO:0000255}. TOPO_DOM 1 312 Extracellular. {ECO:0000255}.; TOPO_DOM 330 509 Cytoplasmic. {ECO:0000255}. FUNCTION: Selectively involved in CSF2 deprivation-induced apoptosis via a mitochondria-dependent pathway. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=Also located in intracellular compartments. {ECO:0000250}. SUBUNIT: Interacts with CSF2RB; this interaction occurs preferentially in the absence of CSF2. {ECO:0000250}. +Q8R0I4 TM2D2_MOUSE TM2 domain-containing protein 2 213 22,853 Chain (1); Glycosylation (1); Sequence conflict (2); Signal peptide (1); Transmembrane (2) TRANSMEM 144 164 Helical. {ECO:0000255}.; TRANSMEM 182 202 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8BJ83 TM2D3_MOUSE TM2 domain-containing protein 3 261 28,880 Alternative sequence (1); Chain (1); Glycosylation (1); Signal peptide (1); Transmembrane (2) TRANSMEM 194 214 Helical. {ECO:0000255}.; TRANSMEM 230 250 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9D328 TM35A_MOUSE Transmembrane protein 35A (Peroxisomal membrane protein 52) (PMP52) 167 18,505 Chain (1); Region (1); Sequence conflict (1); Transmembrane (4) TRANSMEM 6 26 Helical. {ECO:0000255}.; TRANSMEM 62 82 Helical. {ECO:0000255}.; TRANSMEM 89 109 Helical. {ECO:0000255}.; TRANSMEM 115 132 Helical. {ECO:0000255}. FUNCTION: A soluble peptide released by shedding may interact with NGFR and modulate neurite outgrowth. {ECO:0000250}. SUBCELLULAR LOCATION: Peroxisome membrane; Multi-pass membrane protein. Cytoplasmic vesicle {ECO:0000250}. Note=Shedding may lead to a soluble peptide. {ECO:0000250}. SUBUNIT: May interact with NGFR. {ECO:0000250}. +Q9DAV9 TM38B_MOUSE Trimeric intracellular cation channel type B (TRIC-B) (TRICB) (Mitsugumin-33B) (Transmembrane protein 38B) 292 32,640 Binding site (2); Chain (1); Erroneous gene model prediction (1); Sequence conflict (4); Topological domain (8); Transmembrane (7) TRANSMEM 17 34 Helical;Name=1. {ECO:0000255}.; TRANSMEM 48 69 Helical;Name=2. {ECO:0000255}.; TRANSMEM 83 100 Helical;Name=3. {ECO:0000255}.; TRANSMEM 104 122 Helical;Name=4. {ECO:0000255}.; TRANSMEM 141 158 Helical;Name=5. {ECO:0000255}.; TRANSMEM 179 195 Helical;Name=6. {ECO:0000255}.; TRANSMEM 207 225 Helical;Name=7. {ECO:0000255}. TOPO_DOM 1 16 Lumenal. {ECO:0000305}.; TOPO_DOM 35 47 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 70 82 Lumenal. {ECO:0000305}.; TOPO_DOM 101 103 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 123 140 Lumenal. {ECO:0000305}.; TOPO_DOM 159 178 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 196 206 Lumenal. {ECO:0000305}.; TOPO_DOM 226 292 Cytoplasmic. {ECO:0000305}. FUNCTION: Monovalent cation channel required for maintenance of rapid intracellular calcium release. May act as a potassium counter-ion channel that functions in synchronization with calcium release from intracellular stores. {ECO:0000269|PubMed:17611541}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:17611541}; Multi-pass membrane protein {ECO:0000269|PubMed:17611541}. SUBUNIT: Homotrimer; trimerization probably requires binding to phosphatidylinositol 4,5-bisphosphate (PIP2). {ECO:0000250|UniProtKB:A5A6S6, ECO:0000250|UniProtKB:Q9NA73}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:17611541}. +Q9CYC3 TM39A_MOUSE Transmembrane protein 39A 486 55,720 Alternative sequence (1); Chain (1); Glycosylation (1); Sequence conflict (1); Transmembrane (8) TRANSMEM 72 92 Helical. {ECO:0000255}.; TRANSMEM 110 130 Helical. {ECO:0000255}.; TRANSMEM 155 175 Helical. {ECO:0000255}.; TRANSMEM 182 202 Helical. {ECO:0000255}.; TRANSMEM 285 305 Helical. {ECO:0000255}.; TRANSMEM 317 337 Helical. {ECO:0000255}.; TRANSMEM 418 438 Helical. {ECO:0000255}.; TRANSMEM 444 464 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q810L4 TM39B_MOUSE Transmembrane protein 39B 492 56,377 Chain (1); Compositional bias (1); Glycosylation (1); Transmembrane (8) TRANSMEM 77 97 Helical. {ECO:0000255}.; TRANSMEM 115 135 Helical. {ECO:0000255}.; TRANSMEM 153 175 Helical. {ECO:0000255}.; TRANSMEM 185 205 Helical. {ECO:0000255}.; TRANSMEM 288 308 Helical. {ECO:0000255}.; TRANSMEM 322 342 Helical. {ECO:0000255}.; TRANSMEM 421 441 Helical. {ECO:0000255}.; TRANSMEM 447 467 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q91WV7 SLC31_MOUSE Neutral and basic amino acid transport protein rBAT (Solute carrier family 3 member 1) (b(0,+)-type amino acid transport protein) (NBAT) 685 78,118 Chain (1); Glycosylation (6); Modified residue (1); Topological domain (2); Transmembrane (1) TRANSMEM 89 109 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 88 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 110 685 Extracellular. {ECO:0000255}. FUNCTION: Involved in the high-affinity sodium-independent transport of cystine and neutral and dibasic amino acids (system B(0,+)-like activity). May function as an activator of SLC7A9 and be involved in the high-affinity reabsorption of cystine in the kidney proximal tubule. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12167606}; Single-pass type II membrane protein {ECO:0000269|PubMed:12167606}. SUBUNIT: Disulfide-linked heterodimer with the amino acid transporter SLC7A9. {ECO:0000269|PubMed:12167606}. TISSUE SPECIFICITY: Expressed in the brush border membrane in the kidney (at protein level). {ECO:0000269|PubMed:12167606}. +Q6S5I3 S115A_MOUSE Protein S100-A15A (Protein S100-A7A) (S100 calcium-binding protein A15A) (S100 calcium-binding protein A7A) 108 12,870 Calcium binding (1); Chain (1); Domain (1) +P50114 S100B_MOUSE Protein S100-B (S-100 protein beta chain) (S-100 protein subunit beta) (S100 calcium-binding protein B) 92 10,728 Calcium binding (2); Chain (1); Domain (2); Initiator methionine (1); Modified residue (1) FUNCTION: Weakly binds calcium but binds zinc very tightly-distinct binding sites with different affinities exist for both ions on each monomer. Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites. Binds to and initiates the activation of STK38 by releasing autoinhibitory intramolecular interactions within the kinase. Interaction with AGER after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling. Could assist ATAD3A cytoplasmic processing, preventing aggregation and favoring mitochondrial localization. May mediate calcium-dependent regulation on many physiological processes by interacting with other proteins, such as TPR-containing proteins, and modulating their activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Dimer of either two alpha chains, or two beta chains, or one alpha and one beta chain. The S100B dimer binds two molecules of STK38. Interacts with CACYBP in a calcium-dependent manner. Interacts with ATAD3A; this interaction probably occurs in the cytosol prior to ATAD3A mitochondrial targeting. Interacts with S100A6. The S100B dimer interacts with two molecules of CAPZA1. Interacts with AGER. Interacts with PPP5C (via TPR repeats); the interaction is calcium-dependent and modulates PPP5C activity (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Although predominant among the water-soluble brain proteins, S100 is also found in a variety of other tissues. +A2A3V2 S2543_MOUSE Solute carrier family 25 member 43 341 38,064 Chain (1); Repeat (3); Transmembrane (6) TRANSMEM 16 36 Helical; Name=1. {ECO:0000255}.; TRANSMEM 68 88 Helical; Name=2. {ECO:0000255}.; TRANSMEM 110 130 Helical; Name=3. {ECO:0000255}.; TRANSMEM 166 186 Helical; Name=4. {ECO:0000255}.; TRANSMEM 205 225 Helical; Name=5. {ECO:0000255}.; TRANSMEM 262 282 Helical; Name=6. {ECO:0000255}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q8CIA5 S35B4_MOUSE UDP-xylose and UDP-N-acetylglucosamine transporter (Solute carrier family 35 member B4) 331 37,517 Alternative sequence (1); Chain (1); Sequence conflict (1); Transmembrane (11) TRANSMEM 4 24 Helical. {ECO:0000255}.; TRANSMEM 30 50 Helical. {ECO:0000255}.; TRANSMEM 59 79 Helical. {ECO:0000255}.; TRANSMEM 92 112 Helical. {ECO:0000255}.; TRANSMEM 124 144 Helical. {ECO:0000255}.; TRANSMEM 153 173 Helical. {ECO:0000255}.; TRANSMEM 201 221 Helical. {ECO:0000255}.; TRANSMEM 229 249 Helical. {ECO:0000255}.; TRANSMEM 251 267 Helical. {ECO:0000255}.; TRANSMEM 268 288 Helical. {ECO:0000255}.; TRANSMEM 294 314 Helical. {ECO:0000255}. FUNCTION: Sugar transporter that specifically mediates the transport of UDP-xylose (UDP-Xyl) and UDP-N-acetylglucosamine (UDP-GlcNAc) from cytosol into Golgi. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q8VCA0 S22AJ_MOUSE Solute carrier family 22 member 19 (Organic anion transporter 5) 551 60,864 Chain (1); Glycosylation (4); Sequence conflict (1); Topological domain (12); Transmembrane (11) TRANSMEM 6 26 Helical. {ECO:0000255}.; TRANSMEM 146 166 Helical. {ECO:0000255}.; TRANSMEM 189 209 Helical. {ECO:0000255}.; TRANSMEM 235 255 Helical. {ECO:0000255}.; TRANSMEM 260 280 Helical. {ECO:0000255}.; TRANSMEM 350 370 Helical. {ECO:0000255}.; TRANSMEM 378 398 Helical. {ECO:0000255}.; TRANSMEM 407 427 Helical. {ECO:0000255}.; TRANSMEM 435 455 Helical. {ECO:0000255}.; TRANSMEM 469 489 Helical. {ECO:0000255}.; TRANSMEM 496 516 Helical. {ECO:0000255}. TOPO_DOM 1 5 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 27 145 Extracellular. {ECO:0000305}.; TOPO_DOM 167 188 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 210 234 Extracellular. {ECO:0000305}.; TOPO_DOM 256 259 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 281 349 Extracellular. {ECO:0000305}.; TOPO_DOM 371 377 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 399 406 Extracellular. {ECO:0000305}.; TOPO_DOM 428 434 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 456 468 Extracellular. {ECO:0000305}.; TOPO_DOM 490 495 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 517 551 Extracellular. {ECO:0000305}. FUNCTION: Sodium-independent organic anion transporter which shows high specificity for estrone sulfate, dehydroepiandrosterone sulfate, and the mycotoxin ochratoxin A (OTA) (PubMed:15068970, PubMed:16150593). Transport of OTA is strongly inhibited by estrone sulfate and probenecid, and to a lesser extent by 2,4-dichlorophenoxyacetic acid (2,4-D) and salicylate (PubMed:15068970). Transport of estrone sulfate is inhibited by various steroid sulfate conjugates including dehydroepiandrosterone sulfate, alpha-naphthyl sulfate, beta-estradiol sulfate, 4-methylumbelliferyl sulfate and p-nitrophenyl sulfate (but not minoxidil sulfate) (PubMed:16150593). {ECO:0000269|PubMed:15068970, ECO:0000269|PubMed:16150593}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:15068970, ECO:0000269|PubMed:16150593}; Multi-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Specifically expressed in kidney, where it localizes to proximal tubules of the outer medulla (at protein level) (PubMed:15068970, PubMed:16150593). Not detected in other tissues tested (PubMed:15068970). {ECO:0000269|PubMed:15068970, ECO:0000269|PubMed:16150593}. +Q91WU2 S22A7_MOUSE Solute carrier family 22 member 7 (Organic anion transporter 2) (mOAT2) 540 59,614 Alternative sequence (2); Chain (1); Sequence conflict (7); Transmembrane (12) TRANSMEM 21 41 Helical. {ECO:0000255}.; TRANSMEM 144 164 Helical. {ECO:0000255}.; TRANSMEM 172 192 Helical. {ECO:0000255}.; TRANSMEM 202 222 Helical. {ECO:0000255}.; TRANSMEM 232 252 Helical. {ECO:0000255}.; TRANSMEM 257 277 Helical. {ECO:0000255}.; TRANSMEM 344 364 Helical. {ECO:0000255}.; TRANSMEM 378 398 Helical. {ECO:0000255}.; TRANSMEM 402 422 Helical. {ECO:0000255}.; TRANSMEM 429 449 Helical. {ECO:0000255}.; TRANSMEM 462 484 Helical. {ECO:0000255}.; TRANSMEM 488 510 Helical. {ECO:0000255}. FUNCTION: Mediates sodium-independent multispecific organic anion transport. High affinity transport of glutarate and prostaglandin E2 in a sodium-independent manner. Mediates also the uptake of alpha-ketoglutarate, p-aminohippuric acid, methotrexate, ochratoxin A, valproate, allopurinol and bumetanide. {ECO:0000269|PubMed:16256982}. SUBCELLULAR LOCATION: Basolateral cell membrane; Multi-pass membrane protein. Note=Apical side of the renal tubule. {ECO:0000250}. TISSUE SPECIFICITY: Abundant expression in male and female kidney and also in female liver. {ECO:0000269|PubMed:12065749}. +Q76M72 S22AR_MOUSE Solute carrier family 22 member 27 (Organic anion transporter 9) 551 62,045 Alternative sequence (1); Chain (1); Glycosylation (5); Topological domain (13); Transmembrane (12) TRANSMEM 16 36 Helical. {ECO:0000255}.; TRANSMEM 146 166 Helical. {ECO:0000255}.; TRANSMEM 174 194 Helical. {ECO:0000255}.; TRANSMEM 204 224 Helical. {ECO:0000255}.; TRANSMEM 235 255 Helical. {ECO:0000255}.; TRANSMEM 259 279 Helical. {ECO:0000255}.; TRANSMEM 349 369 Helical. {ECO:0000255}.; TRANSMEM 377 397 Helical. {ECO:0000255}.; TRANSMEM 406 426 Helical. {ECO:0000255}.; TRANSMEM 433 453 Helical. {ECO:0000255}.; TRANSMEM 468 488 Helical. {ECO:0000255}.; TRANSMEM 495 515 Helical. {ECO:0000255}. TOPO_DOM 1 15 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 37 145 Extracellular. {ECO:0000305}.; TOPO_DOM 167 173 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 195 203 Extracellular. {ECO:0000305}.; TOPO_DOM 225 234 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 256 258 Extracellular. {ECO:0000305}.; TOPO_DOM 280 348 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 370 376 Extracellular. {ECO:0000305}.; TOPO_DOM 398 405 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 427 432 Extracellular. {ECO:0000305}.; TOPO_DOM 454 467 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 489 494 Extracellular. {ECO:0000305}.; TOPO_DOM 516 551 Cytoplasmic. {ECO:0000305}. FUNCTION: Isoform 1: Does not appear to have transporter activity. {ECO:0000269|PubMed:20332632}.; FUNCTION: Isoform 2: Sodium-independent organic anion transporter which exhibits high specificity for L-carnitine. Can also transport salicylic acid and the drug cimetidine. {ECO:0000269|PubMed:20332632}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20332632}; Multi-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Expressed in proximal kidney tubules, and in liver hepatocytes (at protein level). {ECO:0000269|PubMed:20332632}. +Q8R0C3 S26A8_MOUSE Testis anion transporter 1 (Anion exchange transporter) (Solute carrier family 26 member 8) 999 112,978 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (1); Glycosylation (1); Region (1); Topological domain (14); Transmembrane (13) TRANSMEM 94 114 Helical. {ECO:0000255}.; TRANSMEM 118 138 Helical. {ECO:0000255}.; TRANSMEM 140 160 Helical. {ECO:0000255}.; TRANSMEM 201 221 Helical. {ECO:0000255}.; TRANSMEM 231 251 Helical. {ECO:0000255}.; TRANSMEM 269 289 Helical. {ECO:0000255}.; TRANSMEM 306 326 Helical. {ECO:0000255}.; TRANSMEM 355 375 Helical. {ECO:0000255}.; TRANSMEM 391 411 Helical. {ECO:0000255}.; TRANSMEM 428 448 Helical. {ECO:0000255}.; TRANSMEM 454 474 Helical. {ECO:0000255}.; TRANSMEM 495 515 Helical. {ECO:0000255}.; TRANSMEM 545 565 Helical. {ECO:0000255}. TOPO_DOM 1 93 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 115 117 Extracellular. {ECO:0000255}.; TOPO_DOM 139 139 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 161 200 Extracellular. {ECO:0000255}.; TOPO_DOM 222 230 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 252 268 Extracellular. {ECO:0000255}.; TOPO_DOM 290 305 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 327 354 Extracellular. {ECO:0000255}.; TOPO_DOM 376 390 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 412 427 Extracellular. {ECO:0000255}.; TOPO_DOM 449 453 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 475 494 Extracellular. {ECO:0000255}.; TOPO_DOM 516 544 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 566 999 Extracellular. {ECO:0000255}. FUNCTION: Acts as a DIDS-sensitive anion exchanger mediating chloride, sulfate and oxalate transport. May fulfill critical anion exchange functions in male germ line during meiosis and hence may play a role in spermatogenesis. May be involved in a new regulatory pathway linking sulfate transport to RhoGTPase signaling in male germ cells. A critical component of the sperm annulus that is essential for correct sperm tail differentiation and motility and hence male fertility. May form a molecular complex involved in the regulation of chloride and bicarbonate ions fluxes during sperm capacitation (By similarity). {ECO:0000250, ECO:0000269|PubMed:17517695}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q96RN1}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:17517695}; Multi-pass membrane protein {ECO:0000269|PubMed:17517695}. Note=Located at the annulus ring structure within the sperm cell. {ECO:0000269|PubMed:17517695}. SUBUNIT: Interacts with RACGAP1. Interacts with CFTR. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in testis and epididymis. Located at the end of the midpiece of the flagella, known as the annulus, in spermatozoa. {ECO:0000269|PubMed:17517695}. +Q8BU91 S26A9_MOUSE Solute carrier family 26 member 9 (Anion transporter/exchanger protein 9) 790 86,852 Chain (1); Compositional bias (1); Domain (1); Sequence conflict (4); Transmembrane (13) TRANSMEM 43 63 Helical. {ECO:0000255}.; TRANSMEM 71 91 Helical. {ECO:0000255}.; TRANSMEM 92 112 Helical. {ECO:0000255}.; TRANSMEM 115 135 Helical. {ECO:0000255}.; TRANSMEM 179 199 Helical. {ECO:0000255}.; TRANSMEM 200 220 Helical. {ECO:0000255}.; TRANSMEM 222 242 Helical. {ECO:0000255}.; TRANSMEM 249 269 Helical. {ECO:0000255}.; TRANSMEM 280 300 Helical. {ECO:0000255}.; TRANSMEM 332 352 Helical. {ECO:0000255}.; TRANSMEM 377 397 Helical. {ECO:0000255}.; TRANSMEM 406 426 Helical. {ECO:0000255}.; TRANSMEM 474 494 Helical. {ECO:0000255}. FUNCTION: DIDS- and thiosulfate- sensitive anion exchanger mediating chloride, sulfate and oxalate transport. Mediates chloride/bicarbonate exchange or chloride-independent bicarbonate extrusion thus assuring bicarbonate secretion. Inhibited by ammonium and thiosulfate. {ECO:0000269|PubMed:15800055, ECO:0000269|PubMed:17120765}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in stomach and trachea. Abundantly expressed in the apical domain of the surface epithelial cells and the deep cells in the gastric gland. Also expressed in heart, brain, lung and liver. {ECO:0000269|PubMed:15800055}. +Q9DCP2 S38A3_MOUSE Sodium-coupled neutral amino acid transporter 3 (N-system amino acid transporter 1) (Na(+)-coupled neutral amino acid transporter 3) (Solute carrier family 38 member 3) (mNAT) (System N amino acid transporter 1) 505 55,592 Chain (1); Disulfide bond (1); Glycosylation (4); Sequence conflict (3); Transmembrane (11) TRANSMEM 82 102 Helical. {ECO:0000255}.; TRANSMEM 105 125 Helical. {ECO:0000255}.; TRANSMEM 143 163 Helical. {ECO:0000255}.; TRANSMEM 186 206 Helical. {ECO:0000255}.; TRANSMEM 212 232 Helical. {ECO:0000255}.; TRANSMEM 288 308 Helical. {ECO:0000255}.; TRANSMEM 325 345 Helical. {ECO:0000255}.; TRANSMEM 367 387 Helical. {ECO:0000255}.; TRANSMEM 409 429 Helical. {ECO:0000255}.; TRANSMEM 432 452 Helical. {ECO:0000255}.; TRANSMEM 472 492 Helical. {ECO:0000255}. FUNCTION: Sodium-dependent amino acid/proton antiporter. Mediates electrogenic cotransport of glutamine and sodium ions in exchange for protons. Also recognizes histidine, asparagine and alanine. May mediate amino acid transport in either direction under physiological conditions. May play a role in nitrogen metabolism and synaptic transmission. {ECO:0000250|UniProtKB:Q9JHZ9, ECO:0000269|PubMed:10716701}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10716701}; Multi-pass membrane protein {ECO:0000269|PubMed:10716701}. TISSUE SPECIFICITY: Expressed predominantly in liver, moderately expressed in kidney and brain, and barely detectable in heart and muscle. Within liver, expressed in hepatocytes. Not detected in testis. {ECO:0000269|PubMed:10716701}. +Q3TZX3 S2533_MOUSE Solute carrier family 25 member 33 320 35,064 Chain (1); Frameshift (1); Repeat (3); Sequence conflict (6); Transmembrane (6) TRANSMEM 12 32 Helical; Name=1. {ECO:0000255}.; TRANSMEM 49 65 Helical; Name=2. {ECO:0000255}.; TRANSMEM 121 141 Helical; Name=3. {ECO:0000255}.; TRANSMEM 190 210 Helical; Name=4. {ECO:0000255}.; TRANSMEM 233 253 Helical; Name=5. {ECO:0000255}.; TRANSMEM 298 318 Helical; Name=6. {ECO:0000255}. FUNCTION: Mitochondrial transporter that imports/exports pyrimidine nucleotides into and from mitochondria. Transports preferentially uracil, thymine, and cytosine (deoxy)nucleoside di- and triphosphates by an antiport mechanism. Also transports guanine but not adenine (deoxy)nucleotides. Is inhibited strongly by pyridoxal 5'-phosphate, 4,7-diphenyl-1,10-phenanthroline, tannic acid, and mercurials (mercury dichloride, mersalyl acid, p-hydroxymercuribenzoate). Participates in mitochondrial genome maintenance, regulation of mitochondrial membrane potential and mitochondrial respiration (By similarity). Upon INS or IGF1 stimulation regulates cell growth and proliferation by controlling mitochondrial DNA replication and transcription, the ratio of mitochondria-to nuclear-encoded components of the electron transport chain resulting in control of mitochondrial ROS production (PubMed:17596519). Participates in dendritic cell endocytosis and may associate with mitochondrial oxidative phosphorylation (By similarity). {ECO:0000250|UniProtKB:Q9BSK2, ECO:0000269|PubMed:17596519}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305|PubMed:17596519}; Multi-pass membrane protein {ECO:0000255}. +P52592 S1PR2_MOUSE Sphingosine 1-phosphate receptor 2 (S1P receptor 2) (S1P2) (Endothelial differentiation G-protein coupled receptor 5) (Lysophospholipid receptor B2) (Sphingosine 1-phosphate receptor Edg-5) (S1P receptor Edg-5) 352 38,829 Chain (1); Glycosylation (1); Lipidation (1); Sequence conflict (5); Topological domain (8); Transmembrane (7) TRANSMEM 35 59 Helical; Name=1. {ECO:0000250}.; TRANSMEM 67 95 Helical; Name=2. {ECO:0000250}.; TRANSMEM 110 128 Helical; Name=3. {ECO:0000250}.; TRANSMEM 148 173 Helical; Name=4. {ECO:0000250}.; TRANSMEM 190 210 Helical; Name=5. {ECO:0000250}.; TRANSMEM 234 255 Helical; Name=6. {ECO:0000250}.; TRANSMEM 272 292 Helical; Name=7. {ECO:0000250}. TOPO_DOM 1 34 Extracellular. {ECO:0000250}.; TOPO_DOM 60 66 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 96 109 Extracellular. {ECO:0000250}.; TOPO_DOM 129 147 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 174 189 Extracellular. {ECO:0000250}.; TOPO_DOM 211 233 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 256 271 Extracellular. {ECO:0000250}.; TOPO_DOM 293 352 Cytoplasmic. {ECO:0000250}. FUNCTION: Receptor for the lysosphingolipid sphingosine 1-phosphate (S1P) (By similarity). S1P is a bioactive lysophospholipid that elicits diverse physiological effects on most types of cells and tissues (By similarity). Receptor for the chemokine-like protein FAM19A5 (By similarity). Mediates the inhibitory effect of FAM19A5 on vascular smooth muscle cell proliferation and migration (By similarity). {ECO:0000250|UniProtKB:P47752}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Most abundant in heart and lung; low, but clearly observed in kidney, liver and thymus; much lower but detectable in brain, testis, stomach and intestine. Not significantly detected in any of the sections of embryonic day (E) 14-18, except in embryonic brain. {ECO:0000269|PubMed:9931453}. +Q5HZH7 S38A8_MOUSE Putative sodium-coupled neutral amino acid transporter 8 (Solute carrier family 38 member 8) 432 46,898 Chain (1); Transmembrane (11) TRANSMEM 29 49 Helical. {ECO:0000255}.; TRANSMEM 59 79 Helical. {ECO:0000255}.; TRANSMEM 103 123 Helical. {ECO:0000255}.; TRANSMEM 144 164 Helical. {ECO:0000255}.; TRANSMEM 175 195 Helical. {ECO:0000255}.; TRANSMEM 215 237 Helical. {ECO:0000255}.; TRANSMEM 253 273 Helical. {ECO:0000255}.; TRANSMEM 292 312 Helical. {ECO:0000255}.; TRANSMEM 345 365 Helical. {ECO:0000255}.; TRANSMEM 368 388 Helical. {ECO:0000255}.; TRANSMEM 409 429 Helical. {ECO:0000255}. FUNCTION: Putative sodium-dependent amino acid/proton antiporter. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in the eye. {ECO:0000269|PubMed:24045842}. +Q8BGD6 S38A9_MOUSE Sodium-coupled neutral amino acid transporter 9 (Solute carrier family 38 member 9) 560 63,392 Chain (1); Disulfide bond (1); Erroneous initiation (1); Glycosylation (4); Modified residue (1); Region (1); Sequence conflict (1); Topological domain (11); Transmembrane (11) TRANSMEM 119 139 Helical; Name=1. {ECO:0000250|UniProtKB:Q08BA4}.; TRANSMEM 146 166 Helical; Name=2. {ECO:0000250|UniProtKB:Q08BA4}.; TRANSMEM 198 224 Helical; Name=3. {ECO:0000250|UniProtKB:Q08BA4}.; TRANSMEM 283 299 Helical; Name=4. {ECO:0000250|UniProtKB:Q08BA4}.; TRANSMEM 309 333 Helical; Name=5. {ECO:0000250|UniProtKB:Q08BA4}.; TRANSMEM 356 376 Helical; Name=6. {ECO:0000250|UniProtKB:Q08BA4}.; TRANSMEM 394 414 Helical; Name=7. {ECO:0000250|UniProtKB:Q08BA4}.; TRANSMEM 437 457 Helical; Name=8. {ECO:0000250|UniProtKB:Q08BA4}.; TRANSMEM 479 499 Helical; Name=9. {ECO:0000250|UniProtKB:Q08BA4}.; TRANSMEM 507 527 Helical; Name=10. {ECO:0000250|UniProtKB:Q08BA4}.; TRANSMEM 540 560 Helical; Name=11. {ECO:0000250|UniProtKB:Q08BA4}. TOPO_DOM 1 118 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 140 145 Lumenal. {ECO:0000305}.; TOPO_DOM 167 197 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 225 282 Lumenal. {ECO:0000305}.; TOPO_DOM 300 308 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 334 355 Lumenal. {ECO:0000305}.; TOPO_DOM 377 393 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 415 436 Lumenal. {ECO:0000305}.; TOPO_DOM 458 478 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 500 506 Lumenal. {ECO:0000305}.; TOPO_DOM 528 539 Cytoplasmic. {ECO:0000305}. FUNCTION: Lysosomal amino acid transporter involved in the activation of mTORC1 in response to amino acid levels. Probably acts as an amino acid sensor of the Rag GTPases and Ragulator complexes, 2 complexes involved in amino acid sensing and activation of mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids. Following activation by amino acids, the Ragulator and Rag GTPases function as a scaffold recruiting mTORC1 to lysosomes where it is in turn activated. SLC38A9 mediates transport of amino acids with low capacity and specificity with a slight preference for polar amino acids. Acts as an arginine sensor. Following activation by arginine binding, mediates transport of leucine, tyrosine and phenylalanine with high efficiency, and is required for the efficient utilization of these amino acids after lysosomal protein degradation. {ECO:0000250|UniProtKB:Q8NBW4}. PTM: Glycosylated. {ECO:0000250|UniProtKB:Q8NBW4}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q8NBW4}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q08BA4}. Late endosome membrane {ECO:0000250|UniProtKB:Q8NBW4}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q08BA4}. SUBUNIT: Associated component of the Ragulator complex (composed of LAMTOR1, LAMTOR2, LAMTOR3, LAMTOR4 and LAMTOR5). Associated component of the Rag GTPases heterodimers (composed of RRAGA, RRAGB, RRAGC and RRAGD). {ECO:0000250|UniProtKB:Q8NBW4}. DOMAIN: The cytosolic N-terminus part of the protein mediates interaction with the Ragulator complex and the Rag GTPases heterodimers. {ECO:0000250|UniProtKB:Q8NBW4}. +Q80UP8 S20A2_MOUSE Sodium-dependent phosphate transporter 2 (Phosphate transporter 2) (PiT-2) (Solute carrier family 20 member 2) (Type III sodium-dependent phosphate transporter) 656 70,866 Chain (1); Glycosylation (1); Modified residue (6); Sequence conflict (10); Topological domain (13); Transmembrane (11) TRANSMEM 6 26 Helical. {ECO:0000255}.; TRANSMEM 47 67 Helical. {ECO:0000255}.; TRANSMEM 110 130 Helical. {ECO:0000255}.; TRANSMEM 143 163 Helical. {ECO:0000255}.; TRANSMEM 191 211 Helical. {ECO:0000255}.; TRANSMEM 214 234 Helical. {ECO:0000255}.; TRANSMEM 484 504 Helical. {ECO:0000255}.; TRANSMEM 532 552 Helical. {ECO:0000255}.; TRANSMEM 573 587 Helical. {ECO:0000255}.; TRANSMEM 595 610 Helical. {ECO:0000255}.; TRANSMEM 623 643 Helical. {ECO:0000255}. TOPO_DOM 1 5 Extracellular. {ECO:0000255}.; TOPO_DOM 27 46 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 68 86 Extracellular. {ECO:0000255}.; TOPO_DOM 108 109 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 131 142 Extracellular. {ECO:0000255}.; TOPO_DOM 164 190 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 212 213 Extracellular. {ECO:0000255}.; TOPO_DOM 235 483 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 505 531 Extracellular. {ECO:0000255}.; TOPO_DOM 553 572 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 588 594 Extracellular. {ECO:0000255}.; TOPO_DOM 611 622 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 644 655 Extracellular. {ECO:0000255}. FUNCTION: Sodium-phosphate symporter which seems to play a fundamental housekeeping role in phosphate transport by absorbing phosphate from interstitial fluid for normal cellular functions such as cellular metabolism, signal transduction, and nucleic acid and lipid synthesis. In vitro, sodium-dependent phosphate uptake is not siginificantly affected by acidic and alkaline conditions, however sodium-independent phosphate uptake occurs at acidic conditions. May play a role in extracellular matrix, cartilage and vascular calcification. Functions as a retroviral receptor (By similarity). {ECO:0000250, ECO:0000269|PubMed:11003594}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed including intestine, kidney, heart, liver, brain, testis and skin. Expressed throughout the vertcal crypt-axial axis of intestinal epithelium. {ECO:0000269|PubMed:11003594}. +Q8CH36 S36A4_MOUSE Proton-coupled amino acid transporter 4 (Proton/amino acid transporter 4) (Solute carrier family 36 member 4) 500 55,448 Chain (1); Glycosylation (1); Modified residue (1); Sequence conflict (4); Transmembrane (9) TRANSMEM 84 104 Helical. {ECO:0000255}.; TRANSMEM 151 171 Helical. {ECO:0000255}.; TRANSMEM 203 223 Helical. {ECO:0000255}.; TRANSMEM 228 248 Helical. {ECO:0000255}.; TRANSMEM 270 290 Helical. {ECO:0000255}.; TRANSMEM 306 326 Helical. {ECO:0000255}.; TRANSMEM 354 374 Helical. {ECO:0000255}.; TRANSMEM 411 431 Helical. {ECO:0000255}.; TRANSMEM 444 464 Helical. {ECO:0000255}. FUNCTION: Functions as a sodium-independent electroneutral transporter for tryptophan, proline and alanine. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8BWY7 S39AB_MOUSE Zinc transporter ZIP11 (Solute carrier family 39 member 11) (Zrt- and Irt-like protein 11) (ZIP-11) 342 35,466 Alternative sequence (2); Chain (1); Erroneous initiation (1); Sequence caution (1); Sequence conflict (2); Transmembrane (7) TRANSMEM 12 32 Helical. {ECO:0000255}.; TRANSMEM 44 64 Helical. {ECO:0000255}.; TRANSMEM 72 92 Helical. {ECO:0000255}.; TRANSMEM 194 214 Helical. {ECO:0000255}.; TRANSMEM 263 285 Helical. {ECO:0000255}.; TRANSMEM 290 307 Helical. {ECO:0000255}.; TRANSMEM 322 342 Helical. {ECO:0000255}. FUNCTION: Functions as a cellular zinc transporter. {ECO:0000269|PubMed:23643525}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24089422}; Multi-pass membrane protein {ECO:0000305}. Nucleus {ECO:0000269|PubMed:24089422}. Cytoplasm {ECO:0000269|PubMed:24089422}. Golgi apparatus {ECO:0000269|PubMed:21702047}. TISSUE SPECIFICITY: Highly expressed in the testes and portions of the digestive system including the stomach, ileum and cecum. In contrast, expressed at very low levels in liver, duodenum, jejunum, and colon. {ECO:0000269|PubMed:23643525, ECO:0000269|PubMed:24089422}. +Q9ET37 S5A4A_MOUSE Solute carrier family 5 member 4A 656 71,838 Chain (1); Glycosylation (1); Mutagenesis (1); Topological domain (11); Transmembrane (11) TRANSMEM 29 47 Helical. {ECO:0000255}.; TRANSMEM 65 85 Helical. {ECO:0000255}.; TRANSMEM 106 126 Helical. {ECO:0000255}.; TRANSMEM 172 191 Helical. {ECO:0000255}.; TRANSMEM 209 229 Helical. {ECO:0000255}.; TRANSMEM 271 291 Helical. {ECO:0000255}.; TRANSMEM 315 334 Helical. {ECO:0000255}.; TRANSMEM 424 443 Helical. {ECO:0000255}.; TRANSMEM 456 476 Helical. {ECO:0000255}.; TRANSMEM 527 547 Helical. {ECO:0000255}.; TRANSMEM 635 655 Helical. {ECO:0000255}. TOPO_DOM 1 28 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 48 64 Extracellular. {ECO:0000255}.; TOPO_DOM 86 105 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 127 171 Extracellular. {ECO:0000255}.; TOPO_DOM 192 208 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 230 270 Extracellular. {ECO:0000255}.; TOPO_DOM 292 314 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 335 423 Extracellular. {ECO:0000255}.; TOPO_DOM 444 455 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 477 526 Extracellular. {ECO:0000255}.; TOPO_DOM 548 634 Cytoplasmic. {ECO:0000255}. FUNCTION: Has sugar-induced sodium-independent electrogenic activity. Generation of glucose-induced inward currents is pH-dependent, with activity in acidic conditions (pH 5) but not neutral conditions. Does not have sugar transport activity. {ECO:0000269|PubMed:22301059}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:22301059}; Multi-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Expressed in small intestine. {ECO:0000269|PubMed:22301059}. +Q9QZ03 S39A1_MOUSE Zinc transporter ZIP1 (Solute carrier family 39 member 1) (Zinc-iron-regulated transporter-like) (Zrt- and Irt-like protein 1) (ZIP-1) (mZIP1) 324 34,293 Chain (1); Frameshift (1); Region (1); Sequence conflict (13); Topological domain (8); Transmembrane (8) TRANSMEM 31 51 Helical. {ECO:0000255}.; TRANSMEM 69 89 Helical. {ECO:0000255}.; TRANSMEM 105 125 Helical. {ECO:0000255}.; TRANSMEM 180 200 Helical. {ECO:0000255}.; TRANSMEM 207 227 Helical. {ECO:0000255}.; TRANSMEM 238 258 Helical. {ECO:0000255}.; TRANSMEM 273 293 Helical. {ECO:0000255}.; TRANSMEM 304 324 Helical. {ECO:0000255}. TOPO_DOM 1 30 Extracellular. {ECO:0000255}.; TOPO_DOM 52 68 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 90 104 Extracellular. {ECO:0000255}.; TOPO_DOM 126 179 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 201 206 Extracellular. {ECO:0000255}.; TOPO_DOM 228 237 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 259 272 Extracellular. {ECO:0000255}.; TOPO_DOM 294 303 Cytoplasmic. {ECO:0000255}. FUNCTION: Mediates zinc uptake. May function as a major endogenous zinc uptake transporter in many cells of the body (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. Highest levels seen in kidney, salivary gland and placenta. {ECO:0000269|PubMed:10610721}. +Q80ZQ0 SACA4_MOUSE Sperm acrosome membrane-associated protein 4 127 13,380 Chain (1); Compositional bias (1); Disulfide bond (5); Domain (1); Lipidation (1); Propeptide (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Sperm surface membrane protein that may be involved in sperm-egg plasma membrane adhesion and fusion during fertilization. {ECO:0000250|UniProtKB:Q8TDM5}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8TDM5}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q8TDM5}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250|UniProtKB:Q8TDM5}. Note=Expressed in acrosomal matrix and outer and inner acrosomal membranes. {ECO:0000250|UniProtKB:Q8TDM5}. +Q99K24 S39A3_MOUSE Zinc transporter ZIP3 (Solute carrier family 39 member 3) (Zrt- and Irt-like protein 3) (ZIP-3) 317 34,002 Chain (1); Modified residue (2); Topological domain (9); Transmembrane (8) TRANSMEM 4 24 Helical. {ECO:0000255}.; TRANSMEM 43 63 Helical. {ECO:0000255}.; TRANSMEM 86 106 Helical. {ECO:0000255}.; TRANSMEM 173 193 Helical. {ECO:0000255}.; TRANSMEM 200 220 Helical. {ECO:0000255}.; TRANSMEM 233 253 Helical. {ECO:0000255}.; TRANSMEM 266 286 Helical. {ECO:0000255}.; TRANSMEM 295 315 Helical. {ECO:0000255}. TOPO_DOM 1 3 Extracellular. {ECO:0000255}.; TOPO_DOM 25 42 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 64 85 Extracellular. {ECO:0000255}.; TOPO_DOM 107 172 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 194 199 Extracellular. {ECO:0000255}.; TOPO_DOM 221 232 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 254 265 Extracellular. {ECO:0000255}.; TOPO_DOM 287 294 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 316 317 Extracellular. {ECO:0000255}. FUNCTION: Acts as a zinc-influx transporter. {ECO:0000305}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +P61620 S61A1_MOUSE Protein transport protein Sec61 subunit alpha isoform 1 (Sec61 alpha-1) 476 52,265 Chain (1); Mutagenesis (2); Topological domain (11); Transmembrane (10) TRANSMEM 34 53 Helical. {ECO:0000255}.; TRANSMEM 77 96 Helical. {ECO:0000255}.; TRANSMEM 118 138 Helical. {ECO:0000255}.; TRANSMEM 145 165 Helical. {ECO:0000255}.; TRANSMEM 173 193 Helical. {ECO:0000255}.; TRANSMEM 241 261 Helical. {ECO:0000255}.; TRANSMEM 289 309 Helical. {ECO:0000255}.; TRANSMEM 355 375 Helical. {ECO:0000255}.; TRANSMEM 421 441 Helical. {ECO:0000255}.; TRANSMEM 446 462 Helical. {ECO:0000255}. TOPO_DOM 1 33 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 54 76 Lumenal. {ECO:0000255}.; TOPO_DOM 97 117 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 139 144 Lumenal. {ECO:0000255}.; TOPO_DOM 166 172 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 194 240 Lumenal. {ECO:0000255}.; TOPO_DOM 262 288 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 310 354 Lumenal. {ECO:0000255}.; TOPO_DOM 376 420 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 442 445 Lumenal. {ECO:0000255}.; TOPO_DOM 463 476 Cytoplasmic. {ECO:0000255}. FUNCTION: Component of SEC61 channel-forming translocon complex that mediates transport of signal peptide-containing precursor polypeptides across endoplasmic reticulum (ER). Forms a ribosome receptor and a gated pore in the ER membrane, both functions required for cotranslational translocation of nascent polypeptides. May cooperate with auxiliary protein SEC62, SEC63 and HSPA5/BiP to enable post-translational transport of small presecretory proteins. Controls the passive efflux of calcium ions from the ER lumen to the cytosol through SEC61 channel, contributing to the maintenance of cellular calcium homeostasis (By similarity). Plays a critical role in nephrogenesis, specifically at pronephros stage (PubMed:27392076). {ECO:0000250|UniProtKB:P61619, ECO:0000269|PubMed:27392076}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P61619}; Multi-pass membrane protein {ECO:0000305}. Note=Localizes exclusively in granular structures in the endoplasmic reticulum (ER). {ECO:0000250|UniProtKB:P61619}. SUBUNIT: The ER translocon complex consists of channel-forming core components SEC61A1, SEC61B and SEC61G and different auxiliary components such as SEC62 and SEC63. {ECO:0000250|UniProtKB:P38377}. +Q91WN3 S7A13_MOUSE Solute carrier family 7 member 13 (Sodium-independent aspartate/glutamate transporter 1) (X-amino acid transporter 2) 478 53,233 Chain (1); Topological domain (13); Transmembrane (12) TRANSMEM 15 35 Helical; Name=1. {ECO:0000255}.; TRANSMEM 48 68 Helical; Name=2. {ECO:0000255}.; TRANSMEM 90 110 Helical; Name=3. {ECO:0000255}.; TRANSMEM 130 150 Helical; Name=4. {ECO:0000255}.; TRANSMEM 164 184 Helical; Name=5. {ECO:0000255}.; TRANSMEM 209 229 Helical; Name=6. {ECO:0000255}.; TRANSMEM 243 263 Helical; Name=7. {ECO:0000255}.; TRANSMEM 289 309 Helical; Name=8. {ECO:0000255}.; TRANSMEM 339 359 Helical; Name=9. {ECO:0000255}.; TRANSMEM 361 381 Helical; Name=10. {ECO:0000255}.; TRANSMEM 396 416 Helical; Name=11. {ECO:0000255}.; TRANSMEM 424 444 Helical; Name=12. {ECO:0000255}. TOPO_DOM 1 14 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 36 47 Extracellular. {ECO:0000255}.; TOPO_DOM 69 89 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 111 129 Extracellular. {ECO:0000255}.; TOPO_DOM 151 163 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 185 208 Extracellular. {ECO:0000255}.; TOPO_DOM 230 242 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 264 288 Extracellular. {ECO:0000255}.; TOPO_DOM 310 338 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 360 360 Extracellular. {ECO:0000255}.; TOPO_DOM 382 395 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 417 423 Extracellular. {ECO:0000255}.; TOPO_DOM 445 478 Cytoplasmic. {ECO:0000255}. FUNCTION: Mediates the transport L-aspartate and L-glutamate in a sodium-independent manner. {ECO:0000269|PubMed:11907033}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in the kidney. {ECO:0000269|PubMed:11907033, ECO:0000269|PubMed:11943479}. +A2AJN7 S4A11_MOUSE Sodium bicarbonate transporter-like protein 11 (Bicarbonate transporter-related protein 1) (Sodium borate cotransporter 1) (NaBC1) (Solute carrier family 4 member 11) 862 96,751 Chain (1); Glycosylation (2); Sequence conflict (2); Transmembrane (10) TRANSMEM 345 365 Helical. {ECO:0000255}.; TRANSMEM 385 405 Helical. {ECO:0000255}.; TRANSMEM 428 448 Helical. {ECO:0000255}.; TRANSMEM 462 482 Helical. {ECO:0000255}.; TRANSMEM 543 563 Helical. {ECO:0000255}.; TRANSMEM 634 654 Helical. {ECO:0000255}.; TRANSMEM 671 691 Helical. {ECO:0000255}.; TRANSMEM 727 747 Helical. {ECO:0000255}.; TRANSMEM 749 769 Helical. {ECO:0000255}.; TRANSMEM 817 837 Helical. {ECO:0000255}. FUNCTION: Transporter which plays an important role in sodium-mediated fluid transport in different organs. Prevents severe morphological changes of the cornea caused by increased sodium chloride concentrations in the stroma. In the inner ear, is involved in transport of potassium through the fibrocyte layer to the stria vascularis and is essential for the generation of the endocochlear potential but not for regulation of potassium concentrations in the endolymph. In the kidney, is essential for urinary concentration, mediates a sodium flux into the thin descending limb of Henle loop to allow countercurrent multiplication by osmotic equilibration. Involved in borate homeostasis. In the absence of borate, it functions as a Na(+) and OH(-)(H(+)) channel. In the presence of borate functions as an electrogenic Na(+) coupled borate cotransporter. {ECO:0000269|PubMed:20185830}. PTM: Glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane. Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the endothelial cells of the cornea. In the inner ear, is located in fibrocytes underlying the stria vascularis. In the kidney, is expressed in the thin descending limb of Henle loop. {ECO:0000269|PubMed:20185830}. +P31650 S6A11_MOUSE Sodium- and chloride-dependent GABA transporter 3 (GAT-3) (Sodium- and chloride-dependent GABA transporter 4) (GAT-4) (Solute carrier family 6 member 11) 627 69,961 Chain (1); Glycosylation (3); Modified residue (1); Topological domain (3); Transmembrane (12) TRANSMEM 54 74 Helical; Name=1. {ECO:0000255}.; TRANSMEM 82 101 Helical; Name=2. {ECO:0000255}.; TRANSMEM 126 146 Helical; Name=3. {ECO:0000255}.; TRANSMEM 221 239 Helical; Name=4. {ECO:0000255}.; TRANSMEM 248 265 Helical; Name=5. {ECO:0000255}.; TRANSMEM 301 318 Helical; Name=6. {ECO:0000255}.; TRANSMEM 330 351 Helical; Name=7. {ECO:0000255}.; TRANSMEM 384 403 Helical; Name=8. {ECO:0000255}.; TRANSMEM 433 451 Helical; Name=9. {ECO:0000255}.; TRANSMEM 468 488 Helical; Name=10. {ECO:0000255}.; TRANSMEM 509 528 Helical; Name=11. {ECO:0000255}.; TRANSMEM 548 566 Helical; Name=12. {ECO:0000255}. TOPO_DOM 1 53 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 147 220 Extracellular. {ECO:0000255}.; TOPO_DOM 567 627 Cytoplasmic. {ECO:0000255}. FUNCTION: Terminates the action of GABA by its high affinity sodium-dependent reuptake into presynaptic terminals. Can also transport beta-alanine and taurine. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Brain. +Q8BYJ6 TBCD4_MOUSE TBC1 domain family member 4 (Akt substrate of 160 kDa) (AS160) 1307 147,451 Alternative sequence (8); Chain (1); Domain (3); Modified residue (23); Sequence conflict (8) FUNCTION: May act as a GTPase-activating protein for RAB2A, RAB8A, RAB10 and RAB14. Promotes insulin-induced glucose transporter SLC2A4/GLUT4 translocation at the plasma membrane, thus increasing glucose uptake (By similarity). {ECO:0000250}. PTM: Phosphorylated by AKT1; insulin-induced. Also phosphorylated by AMPK in response to insulin. Insulin-stimulated phosphorylation is required for SLC2A4/GLUT4 translocation. Has no effect on SLC2A4/GLUT4 internalization. {ECO:0000269|PubMed:11994271, ECO:0000269|PubMed:12637568, ECO:0000269|PubMed:16804075, ECO:0000269|PubMed:16804077}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11994271}. Note=Cytoplasmic perinuclear. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed, including in pancreatic beta cells. {ECO:0000269|PubMed:11994271, ECO:0000269|PubMed:18276765}. +Q8BTY2 S4A7_MOUSE Sodium bicarbonate cotransporter 3 (Solute carrier family 4 member 7) 1034 116,514 Alternative sequence (3); Chain (1); Disulfide bond (2); Glycosylation (5); Modified residue (15); Motif (1); Region (1); Sequence conflict (2); Topological domain (10); Transmembrane (9) TRANSMEM 477 497 Helical. {ECO:0000255}.; TRANSMEM 506 526 Helical. {ECO:0000255}.; TRANSMEM 564 584 Helical. {ECO:0000255}.; TRANSMEM 594 614 Helical. {ECO:0000255}.; TRANSMEM 686 706 Helical. {ECO:0000255}.; TRANSMEM 730 750 Helical. {ECO:0000255}.; TRANSMEM 777 797 Helical. {ECO:0000255}.; TRANSMEM 813 833 Helical. {ECO:0000255}.; TRANSMEM 877 897 Helical. {ECO:0000255}. TOPO_DOM 1 476 Extracellular. {ECO:0000255}.; TOPO_DOM 498 505 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 527 563 Extracellular. {ECO:0000255}.; TOPO_DOM 585 593 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 615 685 Extracellular. {ECO:0000255}.; TOPO_DOM 707 729 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 751 776 Extracellular. {ECO:0000255}.; TOPO_DOM 798 812 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 834 876 Extracellular. {ECO:0000255}.; TOPO_DOM 898 1034 Cytoplasmic. {ECO:0000255}. FUNCTION: Electroneutral sodium- and bicarbonate-dependent cotransporter with a Na(+):HCO3(-) 1:1 stoichiometry. Regulates intracellular pH and may play a role in bicarbonate salvage in secretory epithelia. May also have an associated sodium channel activity. {ECO:0000269|PubMed:12808454}. SUBCELLULAR LOCATION: Basolateral cell membrane; Multi-pass membrane protein. Apical cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell projection, stereocilium {ECO:0000250}. Note=Also described at the apical cell membrane. Localizes to the stereocilia of cochlear outer hair cells and to the lateral membrane of cochlear inner hair cells (By similarity). {ECO:0000250}. SUBUNIT: Forms a complex with ATP6V1B1 and SLC9A3R1/EBP50. Interacts in a pH dependent-manner with CA2/carbonic anhydrase 2 (By similarity). Interacts with CFTR through SLC9A3R1/EBP50. Interacts with USH1C. {ECO:0000250, ECO:0000269|PubMed:12403779, ECO:0000269|PubMed:16301216}. DOMAIN: The PDZ-binding motif mediates interaction with the CFTR, SLC9A3R1/EBP50 complex and probably with USH1C. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the spiral ligament throughout the cochlea and in photoreceptors of the outer plexiform layer of the retina (at protein level). {ECO:0000269|PubMed:12808454, ECO:0000269|PubMed:16301216}. +Q9Z1A9 TBCD8_MOUSE TBC1 domain family member 8 (BUB2-like protein 1) (Vascular Rab-GAP/TBC-containing protein) 1134 130,057 Chain (1); Domain (3); Erroneous initiation (2); Sequence conflict (3); Site (2) FUNCTION: May act as a GTPase-activating protein for Rab family protein(s). DOMAIN: The arginine and glutamine fingers are critical for the GTPase-activating mechanism, they pull out Rab's 'switch 2' glutamine and insert in Rab's active site. {ECO:0000250}. +Q3UYK3 TBCD9_MOUSE TBC1 domain family member 9 1264 143,024 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (4); Sequence conflict (4); Site (2) FUNCTION: May act as a GTPase-activating protein for Rab family protein(s). DOMAIN: The arginine and glutamine fingers are critical for the GTPase-activating mechanism, they pull out Rab's 'switch 2' glutamine and insert in Rab's active site. {ECO:0000250}. +Q8BJI1 S6A17_MOUSE Sodium-dependent neutral amino acid transporter SLC6A17 (Sodium-dependent neurotransmitter transporter NTT4) (Solute carrier family 6 member 17) 727 81,071 Chain (1); Glycosylation (2); Modified residue (5); Sequence conflict (1); Topological domain (13); Transmembrane (12) TRANSMEM 69 89 Helical; Name=1. {ECO:0000255}.; TRANSMEM 97 116 Helical; Name=2. {ECO:0000255}.; TRANSMEM 141 161 Helical; Name=3. {ECO:0000255}.; TRANSMEM 225 243 Helical; Name=4. {ECO:0000255}.; TRANSMEM 252 269 Helical; Name=5. {ECO:0000255}.; TRANSMEM 305 322 Helical; Name=6. {ECO:0000255}.; TRANSMEM 334 355 Helical; Name=7. {ECO:0000255}.; TRANSMEM 452 471 Helical; Name=8. {ECO:0000255}.; TRANSMEM 495 513 Helical; Name=9. {ECO:0000255}.; TRANSMEM 529 549 Helical; Name=10. {ECO:0000255}.; TRANSMEM 570 591 Helical; Name=11. {ECO:0000255}.; TRANSMEM 619 641 Helical; Name=12. {ECO:0000255}. TOPO_DOM 1 68 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 90 96 Extracellular. {ECO:0000255}.; TOPO_DOM 117 140 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 162 224 Extracellular. {ECO:0000255}.; TOPO_DOM 244 251 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 270 304 Extracellular. {ECO:0000255}.; TOPO_DOM 323 333 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 356 451 Extracellular. {ECO:0000255}.; TOPO_DOM 472 494 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 514 528 Extracellular. {ECO:0000255}.; TOPO_DOM 550 569 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 592 618 Extracellular. {ECO:0000255}.; TOPO_DOM 642 727 Cytoplasmic. {ECO:0000255}. FUNCTION: Functions as a sodium-dependent vesicular transporter selective for proline, glycine, leucine and alanine. In contrast to other members of this neurotransmitter transporter family, does not appear to be chloride-dependent (By similarity). {ECO:0000250|UniProtKB:P31662}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:P31662}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P31662}. Note=Localizes at synaptic junctions - at both pre- and post-synaptic sites - particularly in excitatory glutamatergic terminals. {ECO:0000269|PubMed:25704603}. TISSUE SPECIFICITY: Expressed in the brain. The strongest expression levels in embryonic, postnatal, and adult stages are found in both cortical and hippocampal tissues. {ECO:0000269|PubMed:25704603}. +Q9D818 SAPC2_MOUSE Suppressor APC domain-containing protein 2 (Protein Ang) 391 42,780 Alternative sequence (2); Chain (1); Coiled coil (2); Erroneous initiation (1); Modified residue (2); Sequence conflict (1) FUNCTION: Plays a role in planar mitotic spindle orientation in retinal progenitor cells (RPCs) and promotes the production of symmetric terminal divisions (PubMed:26766442). Negatively regulates the mitotic apical cortex localization of GPSM2 (By similarity). Involved also in positive regulation of cell proliferation and tumor cell growth (By similarity). {ECO:0000250|UniProtKB:Q86UD0, ECO:0000269|PubMed:26766442}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q86UD0}. Nucleus {ECO:0000250|UniProtKB:Q86UD0}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q86UD0}. Apical cell membrane {ECO:0000269|PubMed:26766442}. Cell junction, tight junction {ECO:0000250|UniProtKB:Q86UD0}. Note=Localized at the apical membrane during the M phase (PubMed:26766442). In horizontally retinal progenitor dividing cells, localized at the pole cortical region from prophase to telophase cells (PubMed:26766442). In vertically retinal progenitor dividing cells, not detected at the pole cortical region at any stage of mitosis (PubMed:26766442). {ECO:0000269|PubMed:26766442}. SUBUNIT: Interacts with a spindle orientation complex at least composed of GNAI1, GPSM2 and NUMA1. Interacts with GPSM2 (via TPR motifs); this interaction is required to prevent GPSM2 anchoring at the mitotic apical cortex and is inhibited in presence of NUMA1 in a dose dependent manner. Interacts with PARD3. {ECO:0000250|UniProtKB:Q86UD0}. TISSUE SPECIFICITY: Expressed in the retina (PubMed:26766442). Expressed in retinal progenitor cells and newly differentiated neurons but not in mature retinal cells (at protein level) (PubMed:26766442). {ECO:0000269|PubMed:26766442}. +Q9CQD6 SARCO_MOUSE Sarcolipin 31 3,808 Peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 8 26 Helical. {ECO:0000250}. TOPO_DOM 1 7 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 27 31 Lumenal. {ECO:0000250}. FUNCTION: Reversibly inhibits the activity of ATP2A1 in sarcoplasmic reticulum by decreasing the apparent affinity of the ATPase for Ca(2+). Modulates calcium re-uptake during muscle relaxation and plays an important role in calcium homeostasis in muscle (PubMed:21697544, PubMed:26816378). Required for muscle-based, non-shivering thermogenesis (PubMed:22961106). {ECO:0000269|PubMed:21697544, ECO:0000269|PubMed:22961106, ECO:0000269|PubMed:26816378}. SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:26816378}; Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P42532}; Single-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with calcium ATPase ATP2A1/SERCA1. {ECO:0000250|UniProtKB:P42532}. TISSUE SPECIFICITY: Highly expressed in heart atrium, red gastrocnemius muscle and soleus. Detected at lower levels in the extensor digitorum longus muscle (at protein level). {ECO:0000269|PubMed:21697544}. +Q3UB74 TBRG1_MOUSE Transforming growth factor beta regulator 1 (Nuclear interactor of ARF and Mdm2) 406 44,881 Chain (1); Domain (2); Erroneous initiation (4); Initiator methionine (1); Modified residue (2); Sequence conflict (8) FUNCTION: Acts as a growth inhibitor. Can activate p53/TP53, causes G1 arrest and collaborates with CDKN2A to restrict proliferation, but does not require either protein to inhibit DNA synthesis. Redistributes CDKN2A into the nucleoplasm. Involved in maintaining chromosomal stability. {ECO:0000269|PubMed:17110379}. PTM: Ubiquitinated; mediated by MDM2 and leading to its subsequent proteasomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17110379}. SUBUNIT: Interacts with CDKN2A and MDM2. {ECO:0000269|PubMed:17110379}. +Q9EPZ6 TBX18_MOUSE T-box transcription factor TBX18 (T-box protein 18) 613 65,464 Chain (1); DNA binding (1); Motif (2) FUNCTION: Acts as transcriptional repressor involved in developmental processes of a variety of tissues and organs, including the heart, the coronary vessels, the ureter, and the vertebral column. Required for embryonic development of the sino atrial node (SAN) head area. {ECO:0000269|PubMed:15155583, ECO:0000269|PubMed:16511601, ECO:0000269|PubMed:17584735, ECO:0000269|PubMed:19096026, ECO:0000269|PubMed:24016759}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00201, ECO:0000269|PubMed:17584735}. SUBUNIT: Homodimer. Can form a heterodimer with TBX15. Interacts with GATA4 AND NKX2-5. Interacts (via engrailed homology 1 repressor motif) with TLE3; this interaction represses TBX18 transcriptional activity. Interacts with PAX3. Interacts with SIX1 (By similarity). {ECO:0000250|UniProtKB:O95935, ECO:0000269|PubMed:17584735, ECO:0000269|PubMed:18644785}. +P48026 SAT1_MOUSE Diamine acetyltransferase 1 (EC 2.3.1.57) (Polyamine N-acetyltransferase 1) (Putrescine acetyltransferase) (Spermidine/spermine N(1)-acetyltransferase 1) (SSAT) (SSAT-1) 171 20,012 Beta strand (7); Binding site (2); Chain (1); Domain (1); Helix (10); Mutagenesis (2); Region (6); Turn (2) Amine and polyamine degradation; putrescine degradation; N-acetylputrescine from putrescine: step 1/1. FUNCTION: Enzyme which catalyzes the acetylation of polyamines. Substrate specificity: norspermidine = spermidine >> spermine > N(1)-acetylspermine > putrescine. This highly regulated enzyme allows a fine attenuation of the intracellular concentration of polyamines. Also involved in the regulation of polyamine transport out of cells. Acts on 1,3-diaminopropane, 1,5-diaminopentane, putrescine, spermidine (forming N(1)- and N(8)-acetylspermidine), spermine, N(1)-acetylspermidine and N(8)-acetylspermidine (By similarity). {ECO:0000250|UniProtKB:P21673, ECO:0000305|PubMed:18690703}. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Homodimer. {ECO:0000269|PubMed:18690703}. +Q8K402 TBX22_MOUSE T-box transcription factor TBX22 (T-box protein 22) 517 58,498 Chain (1); DNA binding (1) FUNCTION: Probable transcriptional regulator involved in developmental processes. This is major determinant crucial to palatogenesis. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00201}. +P0C5K0 SBK3_MOUSE Uncharacterized serine/threonine-protein kinase SBK3 (EC 2.7.11.1) (SH3-binding domain kinase family member 3) (Sugen kinase 110) 361 39,117 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Compositional bias (2); Domain (1); Nucleotide binding (1) +Q9CZY2 TCAL8_MOUSE Transcription elongation factor A protein-like 8 (TCEA-like protein 8) (Transcription elongation factor S-II protein-like 8) 117 13,472 Chain (1); Coiled coil (1); Sequence conflict (1) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q9DD24 TCAL9_MOUSE Transcription elongation factor A protein-like 9 (TCEA-like protein 9) (Schlafen 8-interacting protein) (Transcription elongation factor S-II protein-like 9) (WW domain-binding protein 5) (WBP-5) 104 12,664 Chain (1); Compositional bias (1); Erroneous translation (1) FUNCTION: May be involved in transcriptional regulation. {ECO:0000305}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q689Z5 SBNO1_MOUSE Protein strawberry notch homolog 1 (mSno1) 1390 153,738 Alternative sequence (1); Chain (1); Coiled coil (1); Compositional bias (1); Modified residue (15); Sequence caution (1); Sequence conflict (5) TISSUE SPECIFICITY: Highly expressed in brain and testis. Expressed in the hippocampus, olfactory bulb, and cerebellum. Low expression detected in lung, heart, liver, skin, colon and kidney. {ECO:0000269|PubMed:17045962}. +Q7TNB8 SBNO2_MOUSE Protein strawberry notch homolog 2 1349 149,294 Alternative sequence (5); Chain (1); Compositional bias (5); Sequence conflict (2) FUNCTION: Acts as a transcriptional coregulator, that can have both coactivator and corepressor functions (PubMed:18025162, PubMed:23980096). Inhibits the DCSTAMP-repressive activity of TAL1, hence enhancing the access of the transcription factor MITF to the DC-STAMP promoter in osteoclast (PubMed:23980096). Plays a role in bone homeostasis; required as a positive regulator in TNFSF11//RANKL-mediated osteoclast fusion via a DCSTAMP-dependent pathway (PubMed:23980096). May also be required in the regulation of osteoblast differentiation (PubMed:23980096). Involved in the transcriptional corepression of NF-kappaB in macrophages. Plays a role as a regulator in the proinflammatory cascade (By similarity). {ECO:0000250|UniProtKB:Q9Y2G9, ECO:0000269|PubMed:23980096}. SUBUNIT: Interacts with TAL1; this interaction inhibits TAL1 occupancy of the DCSTAMP promoter, leading to the activation of the DCSTAMP promoter by the transcription factor MITF (PubMed:23980096). {ECO:0000269|PubMed:23980096}. TISSUE SPECIFICITY: Expressed in the spleen and bone marrow, and to a lesser extent in the kidney, liver, brain, skin, heart and muscle (PubMed:23980096). Expressed predominantly in osteoclasts, and to a lesser extent in T-cells, B-cells and osteoblasts (PubMed:23980096). Expressed in macrophages (PubMed:18025162). {ECO:0000269|PubMed:18025162, ECO:0000269|PubMed:23980096}. +Q8BJQ4 TCAM2_MOUSE TIR domain-containing adapter molecule 2 (TICAM-2) (TRIF-related adapter molecule) (Toll/interleukin-1 receptor domain-containing protein) 232 26,362 Chain (1); Domain (1); Initiator methionine (1); Lipidation (1); Mutagenesis (4); Sequence conflict (1) FUNCTION: Functions as sorting adapter in LPS-TLR4 signaling to regulate the MYD88-independent pathway during the innate immune response to LPS. Physically bridges TLR4 and TICAM1 and functionally transmits LPS-TRL4 signal to TICAM1; signaling is proposed to occur in early endosomes after endocytosis of TLR4. May also be involved in IL1-triggered NF-kappa-B activation, functioning upstream of IRAK1, IRAK2, TRAF6, and IKBKB; however, reports are controversial. Involved in IL-18 signaling and is proposed to function as a sorting adaptor for MYD88 in IL-18 signaling during adaptive immune response. {ECO:0000269|PubMed:14556004, ECO:0000269|PubMed:18297073, ECO:0000269|PubMed:22685567}. PTM: Myristoylated. Required for membrane association which is critical for its ability to initiate efficient signaling (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:18297073}. Early endosome {ECO:0000269|PubMed:18297073}. Late endosome {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Note=Localized to the plasma membrane as a result of myristoylation. {ECO:0000250}. SUBUNIT: Homodimer. Interacts with TLR4, TICAM1, IRF3 and IRF7 in response to LPS. Interacts with IL1R1, IL1RAP, IRAK2, IRAK3 and TRAF6. Interacts with kinase-inactive mutants of IRAK1 and IRAK4. Interacts with MYD88; the interaction decreases after IL-18 stimulation in a time-dependent manner. Interacts with IL18R1 and IL18RAP (By similarity). {ECO:0000250}. DOMAIN: The TIR domain mediates the interaction with TRAF6 and MYD88. {ECO:0000250}. +P01852 TCB1_MOUSE T-cell receptor beta-1 chain C region 173 19,346 Beta strand (11); Chain (1); Disulfide bond (1); Glycosylation (2); Helix (3); Natural variant (1); Non-terminal residue (1); Region (1); Topological domain (1); Transmembrane (1) TRANSMEM 146 167 Helical. {ECO:0000255}. TOPO_DOM 168 173 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q9JLI8 SART3_MOUSE Squamous cell carcinoma antigen recognized by T-cells 3 (SART-3) (mSART-3) (Tumor-rejection antigen SART3) 962 109,619 Alternative sequence (2); Chain (1); Coiled coil (1); Domain (2); Erroneous initiation (1); Initiator methionine (1); Modified residue (7); Region (4); Repeat (9); Sequence conflict (2) FUNCTION: U6 snRNP-binding protein that functions as a recycling factor of the splicing machinery. Promotes the initial reassembly of U4 and U6 snRNPs following their ejection from the spliceosome during its maturation. Also binds U6atac snRNPs and may function as a recycling factor for U4atac/U6atac spliceosomal snRNP, an initial step in the assembly of U12-type spliceosomal complex. The U12-type spliceosomal complex plays a role in the splicing of introns with non-canonical splice sites. May also function as a substrate-targeting factor for deubiquitinases like USP4 and USP15. Recruits USP4 to ubiquitinated PRPF3 within the U4/U5/U6 tri-snRNP complex, promoting PRPF3 deubiquitination and thereby regulating the spliceosome U4/U5/U6 tri-snRNP spliceosomal complex disassembly. May also recruit the deubiquitinase USP15 to histone H2B and mediate histone deubiquitination, thereby regulating gene expression and/or DNA repair (By similarity). May play a role in hematopoiesis probably through transcription regulation of specific genes including MYC (PubMed:21447833). {ECO:0000250|UniProtKB:Q15020, ECO:0000269|PubMed:21447833}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:12578909}. Nucleus, Cajal body {ECO:0000269|PubMed:12578909}. Nucleus speckle {ECO:0000250|UniProtKB:Q15020}. Cytoplasm {ECO:0000250|UniProtKB:Q15020}. SUBUNIT: Component of the 7SK snRNP complex at least composed of P-TEFb (composed of CDK9 and CCNT1/cyclin-T1), HEXIM1, HEXIM2, BCDIN3, SART3 proteins and 7SK and U6 snRNAs. Interacts with AGO1 and AGO2. Interacts with PRPF3 and USP4; the interaction with PRPF3 is direct and recruits USP4 to its substrate PRPF3. Interacts with USP15; the interaction is direct. {ECO:0000250|UniProtKB:Q15020}. TISSUE SPECIFICITY: Ubiquitously expressed, with low level of expression in liver, heart and skeletal (PubMed:10761712). Also detected in hematopoietic cells (at protein level) (PubMed:21447833). {ECO:0000269|PubMed:10761712, ECO:0000269|PubMed:21447833}. +Q9D915 TCIM_MOUSE Transcriptional and immune response regulator 106 12,215 Chain (1) FUNCTION: Seems to be involved in the regulation of cell growth an differentiation, may play different and opposite roles depending on the tissue or cell type. May enhance the WNT-CTNNB1 pathway by relieving antagonistic activity of CBY1. Enhances the proliferation of follicular dendritic cells. Plays a role in the mitogen-activated MAPK2/3 signaling pathway, positively regulates G1-to-S-phase transition of the cell cycle. In endothelial cells, enhances key inflammatory mediators and inflammatory response through the modulation of NF-kappaB transcriptional regulatory activity. Involved in the regulation of heat shock response, seems to play a positive feedback with HSF1 to modulate heat-shock downstream gene expression (By similarity). Plays a role in the regulation of hematopoiesis even if the mechanisms are unknown (PubMed:24937306). In cancers such as thyroid or lung cancer, it has been described as promoter of cell proliferation, G1-to-S-phase transition and inhibitor of apoptosis. However, it negatively regulates self-renewal of liver cancer cells via suppresion of NOTCH2 signaling (By similarity). {ECO:0000250|UniProtKB:Q9NR00, ECO:0000269|PubMed:24937306}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24937306}. Nucleus {ECO:0000269|PubMed:24937306}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9NR00}. Nucleus speckle {ECO:0000250|UniProtKB:Q9NR00}. Note=Localizes in nucleus speckles in presence of CBY1. Translocates to the nucleus upon cellular stress such as H(2)O(2). {ECO:0000250|UniProtKB:Q9NR00}. SUBUNIT: Monomer. Interacts with NOTCH2 (via ANK repeats), the interaction inhibits the nuclear translocation of NOTCH2 N2ICD. Interacts (C-terminus) with CBY1 (C-terminus), TCIM competes with CTNNB1 for the interaction with CBY1. {ECO:0000250|UniProtKB:Q9NR00}. TISSUE SPECIFICITY: Expressed in liver, expression levels decrease in regenerating liver (PubMed:25985737). In bone marrow, expressed in large progenitor-like cells, cells with ring-shaped nuclei and, at lower, levels in hematopietic stem cell-like cells with round nuclei (at protein level) (PubMed:24937306). {ECO:0000269|PubMed:24937306, ECO:0000269|PubMed:25985737}. +Q99PN0 SC5A5_MOUSE Sodium/iodide cotransporter (Na(+)/I(-) cotransporter) (Sodium-iodide symporter) (Na(+)/I(-) symporter) (Solute carrier family 5 member 5) 618 65,568 Chain (1); Glycosylation (2); Modified residue (1); Topological domain (14); Transmembrane (13) TRANSMEM 17 37 Helical. {ECO:0000255}.; TRANSMEM 54 74 Helical. {ECO:0000255}.; TRANSMEM 89 109 Helical. {ECO:0000255}.; TRANSMEM 137 157 Helical. {ECO:0000255}.; TRANSMEM 164 184 Helical. {ECO:0000255}.; TRANSMEM 187 207 Helical. {ECO:0000255}.; TRANSMEM 242 262 Helical. {ECO:0000255}.; TRANSMEM 287 307 Helical. {ECO:0000255}.; TRANSMEM 327 347 Helical. {ECO:0000255}.; TRANSMEM 392 412 Helical. {ECO:0000255}.; TRANSMEM 417 437 Helical. {ECO:0000255}.; TRANSMEM 445 465 Helical. {ECO:0000255}.; TRANSMEM 521 541 Helical. {ECO:0000255}. TOPO_DOM 1 16 Extracellular. {ECO:0000255}.; TOPO_DOM 38 53 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 75 88 Extracellular. {ECO:0000255}.; TOPO_DOM 110 136 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 158 163 Extracellular. {ECO:0000255}.; TOPO_DOM 185 186 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 208 241 Extracellular. {ECO:0000255}.; TOPO_DOM 263 286 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 308 326 Extracellular. {ECO:0000255}.; TOPO_DOM 348 391 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 413 416 Extracellular. {ECO:0000255}.; TOPO_DOM 438 444 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 466 520 Extracellular. {ECO:0000255}.; TOPO_DOM 542 618 Cytoplasmic. {ECO:0000255}. FUNCTION: Mediates iodide uptake in the thyroid gland. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. +Q8C8N2 SCAI_MOUSE Protein SCAI (Suppressor of cancer cell invasion protein) 606 70,275 Alternative sequence (2); Chain (1); Erroneous initiation (1); Modified residue (1); Region (2); Sequence conflict (1); Transmembrane (1) TRANSMEM 472 492 Helical. {ECO:0000255}. FUNCTION: Tumor suppressor which functions to suppress MRTFA-induced SRF transcriptional activity. May function in the RHOA-DIAPH1 signal transduction pathway and regulate cell migration through transcriptional regulation of ITGB1. {ECO:0000269|PubMed:19350017}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Nucleus {ECO:0000269|PubMed:19350017}. Cytoplasm {ECO:0000269|PubMed:19350017}. Note=Nuclear localization is required for inhibition of MRTFA. SUBUNIT: Interacts with DIAPH1. Forms a nuclear ternary complex with MRTFA and SRF. {ECO:0000269|PubMed:19350017}. TISSUE SPECIFICITY: Expressed in most tissues tested with higher expression levels in brain, spleen and thymus. {ECO:0000269|PubMed:19350017}. +Q9D2X5 SCC4_MOUSE MAU2 chromatid cohesion factor homolog (MAU-2) (Cohesin loading complex subunit SCC4 homolog) 619 69,579 Alternative sequence (1); Chain (1); Erroneous initiation (1); Region (1); Repeat (4); Sequence conflict (2) FUNCTION: Plays an important role in the loading of the cohesin complex on to DNA. Forms a heterodim. eric complex (also known as cohesin loading complex) with NIPBL/SCC2 which mediates the loading of the cohesin complex onto chromatin Plays a role in sister chromatid cohesion and normal progression through prometaphase. {ECO:0000250|UniProtKB:Q9Y6X3}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9Y6X3}. Chromosome {ECO:0000269|PubMed:24287868}. Nucleus {ECO:0000250|UniProtKB:Q9Y6X3}. Note=Binds to chromatin from the end of mitosis until prophase. {ECO:0000250|UniProtKB:Q9Y6X3}. SUBUNIT: Heterodimerizes with MAU2/SCC2 to form the cohesin loading complex. The NIPBL-MAU2 heterodimer interacts with the SMC1A-SMC3 heterodimer and with the cohesin complex composed of SMC1A, SMC3, RAD21 and STAG1. {ECO:0000250|UniProtKB:Q9Y6X3}. TISSUE SPECIFICITY: Spermatocytes and oocytes (at protein level). {ECO:0000269|PubMed:24287868}. +Q8C850 SCAR3_MOUSE Scavenger receptor class A member 3 606 65,471 Chain (1); Domain (2); Glycosylation (10); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 57 77 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 56 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 78 606 Extracellular. {ECO:0000255}. FUNCTION: Seems to protect cells by scavenging oxidative molecules or harmful products of oxidation. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Endoplasmic reticulum and/or Golgi. {ECO:0000250}. +G5E861 SCLT1_MOUSE Sodium channel and clathrin linker 1 (Sodium channel-associated protein 1) 688 80,492 Alternative sequence (2); Chain (1); Coiled coil (2); Initiator methionine (1); Modified residue (2) FUNCTION: Adapter protein that links SCN10A to clathrin. Regulates SCN10A channel activity, possibly by promoting channel internalization (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250}. Note=Localizes to the distal appendage region of the centriole, which anchors the mother centriole to the plasma membrane. {ECO:0000250}. SUBUNIT: Interacts with SCN10A and clathrin. Identified in a complex containing SCN10A, clathrin and SCLT1 (By similarity). {ECO:0000250}. +Q03517 SCG2_MOUSE Secretogranin-2 (Chromogranin-C) (Secretogranin II) (SgII) [Cleaved into: Secretoneurin (SN); Manserin] 617 70,644 Chain (1); Modified residue (7); Peptide (2); Sequence conflict (1); Signal peptide (1) FUNCTION: Secretogranin-2 is a neuroendocrine secretory granule protein, which may be the precursor for other biologically active peptides. SUBCELLULAR LOCATION: Secreted. Note=Neuroendocrine and endocrine secretory granules. +P09838 TDT_MOUSE DNA nucleotidylexotransferase (EC 2.7.7.31) (EC 3.1.11.-) (Terminal addition enzyme) (Terminal deoxynucleotidyltransferase) (TDT) (Terminal transferase) 510 58,266 Alternative sequence (1); Beta strand (10); Chain (1); Domain (1); Helix (21); Metal binding (3); Modified residue (1); Motif (1); Mutagenesis (10); Region (5); Sequence conflict (7); Turn (1) FUNCTION: Isoform TDT-S: Transferase that catalyzes the nontemplated addition of nucleoside triphosphate to coding ends during V(D)J recombination (N addition). Involved in the generation of diversity in the antigen-binding region of immunoglobulin heavy and light chains and T-cell receptors during B-and T-cell development. Does not act on double-stranded DNA with blunt ends. {ECO:0000269|PubMed:11136823, ECO:0000269|PubMed:11938351, ECO:0000269|PubMed:23856622, ECO:0000269|PubMed:7556063, ECO:0000269|PubMed:8464703}.; FUNCTION: Isoform TDT-L: 3'-to-5' DNA exonuclease. Involved in the generation of diversity in the antigen-binding region of immunoglobulin heavy and light chains and T-cell receptors during B-and T-cell development. Acts on single-stranded and double-stranded DNA with 3' or 5' extensions, but not on double-stranded DNA with blunt ends. Attenuates not only isoform TDT-S-catalyzed N addition, but also P (palindromic) addition in coding joins (PubMed:11938351). Lacks terminal transferase activity (PubMed:11136823, PubMed:7556063). {ECO:0000269|PubMed:11136823, ECO:0000269|PubMed:11938351, ECO:0000269|PubMed:7556063}. SUBCELLULAR LOCATION: Isoform TDT-S: Nucleus {ECO:0000269|PubMed:7556063}.; SUBCELLULAR LOCATION: Isoform TDT-L: Nucleus {ECO:0000269|PubMed:11136823}. Cytoplasm {ECO:0000269|PubMed:7556063}. Note=The subcellular location is controversial. Detected in the nucleus (PubMed:11136823). Found mainly in the cytoplasm (PubMed:7556063). {ECO:0000269|PubMed:11136823, ECO:0000269|PubMed:7556063}. SUBUNIT: Interacts with PRP19 and DNTTIP1. Forms a ternary complex with DNTTIP2 and core histone. Released from this complex by PCNA. Interacts with TRERF1. {ECO:0000250|UniProtKB:P04053}. TISSUE SPECIFICITY: Isoform TDT-L: Expressed in the thymus, and, at lower levels, in the bone marrow (PubMed:8464703, PubMed:11136823, PubMed:7556063). Detected in both cycling and noncycling pro-B and pre-B cells (at protein level) (PubMed:11938351). Isoform TDT-S: Expressed in both cycling and noncycling pro-B, but not pre-B, cells (at protein level) (PubMed:11938351). Not detected in mature peripheral or germinal center B cells (PubMed:11938351). {ECO:0000269|PubMed:11136823, ECO:0000269|PubMed:11938351, ECO:0000269|PubMed:7556063, ECO:0000269|PubMed:8464703}. +Q3UHK6 TEN4_MOUSE Teneurin-4 (Ten-4) (Downstream of CHOP4) (Protein Odd Oz/ten-m homolog 4) (Tenascin-M4) (Ten-m4) (Teneurin transmembrane protein 4) 2771 308,425 Alternative sequence (5); Chain (1); Compositional bias (1); Disulfide bond (22); Domain (9); Glycosylation (12); Modified residue (2); Repeat (28); Sequence conflict (31); Topological domain (2); Transmembrane (1) TRANSMEM 346 366 Helical. {ECO:0000255}. TOPO_DOM 1 345 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 367 2771 Extracellular. {ECO:0000255}. FUNCTION: Involved in neural development, regulating the establishment of proper connectivity within the nervous system. Plays a role in the establishment of the anterior-posterior axis during gastrulation. Regulates the differentiation and cellular process formation of oligodendrocytes and myelination of small-diameter axons in the central nervous system (CNS). Promotes activation of focal adhesion kinase. May function as a cellular signal transducer. {ECO:0000269|PubMed:15489520, ECO:0000269|PubMed:22915103}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6N022}; Single-pass membrane protein {ECO:0000255}. Cell projection {ECO:0000269|PubMed:22915103}. Nucleus {ECO:0000269|PubMed:22915103}. Cytoplasm {ECO:0000269|PubMed:22915103}. SUBUNIT: Homodimer; disulfide-linked. May also form heterodimer with either TENM1 or TENM2 or TENM3. DOMAIN: EGF-like domains 2 and 5 which have an odd number of cysteines might enable the formation of intermolecular disulfide bonds.; DOMAIN: Cytoplasmic proline-rich regions could serve as docking domains for intracellular SH3-containing proteins. TISSUE SPECIFICITY: Expressed in brain and spinal cord (at protein level). Expressed in neurons and oligodendrocytes of the spinal cord. Expressed weakly in kidney, lung and spleen. Expressed in the cortex, CA1, CA2 and CA3 of the hippocampus. Expressed in the white matter, Purkinje cells and molecular layer of the cerebellum. {ECO:0000269|PubMed:12915301, ECO:0000269|PubMed:15489520, ECO:0000269|PubMed:22915103}. +Q9EQC5 SCYL1_MOUSE N-terminal kinase-like protein (105 kDa kinase-like protein) (Mitosis-associated kinase-like protein NTKL) (SCY1-like protein 1) 806 89,160 Chain (1); Coiled coil (1); Domain (1); Modified residue (1); Mutagenesis (1); Region (1); Repeat (3); Sequence conflict (6) FUNCTION: Regulates COPI-mediated retrograde protein traffic at the interface between the Golgi apparatus and the endoplasmic reticulum. Involved in the maintenance of the Golgi apparatus morphology. Has no detectable kinase activity in vitro. {ECO:0000250|UniProtKB:Q96KG9}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:11118629, ECO:0000269|PubMed:12783284}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250}. Golgi apparatus, cis-Golgi network {ECO:0000250}. Note=Localized to the Endoplasmic reticulum-Golgi intermediate and cis-Golgi in an ARF1-independent manner. {ECO:0000250}. SUBUNIT: Homooligomer (By similarity). Interacts with GORAB. Interacts with COPA, COPB1 and COPB2. Interacts with AP2B1 (By similarity). {ECO:0000250}. DOMAIN: The protein kinase domain is predicted to be catalytically inactive. TISSUE SPECIFICITY: Expressed in diaphragm, quadriceps, thymus, liver, lung, spleen, kidney, heart and brain. Prominently expressed in neurons, and enriched at central nervous system synapses and neuromuscular junctions. {ECO:0000269|PubMed:11118629, ECO:0000269|PubMed:17571074}. DISEASE: Note=Defects in Scyl1 are the cause of the muscle deficient phenotype (mdf). Mice exhibit progressive neuromuscular atrophy, hindlimb paralysis, gait ataxia, abnormal hindlimb posture and tremor. Pathology of mdf comprises cerebellar atrophy, Purkinje cell loss and optic nerve atrophy. {ECO:0000269|PubMed:17571074}. +P40224 SDF1_MOUSE Stromal cell-derived factor 1 (SDF-1) (12-O-tetradecanoylphorbol 13-acetate repressed protein 1) (TPAR1) (C-X-C motif chemokine 12) (Pre-B cell growth-stimulating factor) (PBSF) (Thymic lymphoma cell-stimulating factor) (TLSF) 93 10,561 Alternative sequence (1); Binding site (3); Chain (1); Disulfide bond (2); Motif (1); Region (5); Signal peptide (1); Site (4) FUNCTION: Chemoattractant active on T-lymphocytes and monocytes but not neutrophils. Activates the C-X-C chemokine receptor CXCR4 to induce a rapid and transient rise in the level of intracellular calcium ions and chemotaxis. Also binds to atypical chemokine receptor ACKR3, which activates the beta-arrestin pathway and acts as a scavenger receptor for SDF-1. Binds to the allosteric site (site 2) of integrins and activates integrins ITGAV:ITGB3, ITGA4:ITGB1 and ITGA5:ITGB1 in a CXCR4-independent manner (By similarity). Acts as a positive regulator of monocyte migration and a negative regulator of monocyte adhesion via the LYN kinase. Stimulates migration of monocytes and T-lymphocytes through its receptors, CXCR4 and ACKR3, and decreases monocyte adherence to surfaces coated with ICAM-1, a ligand for beta-2 integrins. SDF1A/CXCR4 signaling axis inhibits beta-2 integrin LFA-1 mediated adhesion of monocytes to ICAM-1 through LYN kinase. Plays a protective role after myocardial infarction. Induces down-regulation and internalization of ACKR3 expressed in various cells (By similarity). Has several critical functions during embryonic development; required for B-cell lymphopoiesis, myelopoiesis in bone marrow and heart ventricular septum formation. Stimulates the proliferation of bone marrow-derived B-cell progenitors in the presence of IL7 as well as growth of stromal cell-dependent pre-B-cells (PubMed:8134392). {ECO:0000250|UniProtKB:P48061, ECO:0000269|PubMed:8134392, ECO:0000269|PubMed:8757135}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Monomer or homodimer; in equilibrium. Dimer formation is induced by non acidic pH and the presence of multivalent anions, and by binding to CXCR4 or heparin. Monomeric form is required for full chemotactic activity and resistance to ischemia/reperfusion injury, whereas the dimeric form acts as a partial agonist of CXCR4, stimulating Ca2+ mobilization but with no chemotactic activity and instead acts as a selective antagonist that blocks chemotaxis induced by the monomeric form. Interacts with the N-terminus of ACKR3. Interacts with integrin subunit ITGB3 (via the allosteric site (site 2)). {ECO:0000250|UniProtKB:P48061}. TISSUE SPECIFICITY: Highest expression levels detected in kidney, liver, spleen and muscle. Isoform Alpha is expressed ubiquitously but at varying levels, while isoform Beta displays tissue-specific expression, with expression detected in kidney, liver, heart, spleen and muscle but not in lung, colon, brain, skin and stomach. {ECO:0000269|PubMed:7982471}. +Q8BR65 SDS3_MOUSE Sin3 histone deacetylase corepressor complex component SDS3 (Suppressor of defective silencing 3 protein homolog) 328 38,107 Chain (1); Coiled coil (1); Cross-link (3); Helix (2); Initiator methionine (1); Modified residue (9); Region (2); Sequence conflict (3) FUNCTION: Regulatory protein which represses transcription and augments histone deacetylase activity of HDAC1. May have a potential role in tumor suppressor pathways through regulation of apoptosis. May function in the assembly and/or enzymatic activity of the mSin3A corepressor complex or in mediating interactions between the complex and other regulatory complexes (By similarity). {ECO:0000250|UniProtKB:Q9H7L9, ECO:0000269|PubMed:11909966}. PTM: Polyubiquitinated. 'Lys-63'-polyubiquitinated SUDS3 positively regulates histone deacetylation. Regulated through deubiquitination by USP17L2/USP17 that cleaves 'Lys-63'-linked ubiquitin chains (By similarity). {ECO:0000250|UniProtKB:Q9H7L9}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H7L9}. SUBUNIT: Interacts with HCFC1 (By similarity). Homodimer. Component of the SIN3 histone deacetylase (HDAC) corepressor complex. Interacts with SIN3A. Interaction with SIN3B enhances the interaction between SIN3B and HDAC1 to form a complex. Component of a mSin3A corepressor complex that contains SIN3A, SAP130, SUDS3/SAP45, ARID4B/SAP180, HDAC1 and HDAC2. Interacts with USP17L2; the interaction is direct (By similarity). Interacts with FOXK2 (By similarity). {ECO:0000250|UniProtKB:Q9H7L9}. DOMAIN: The C-terminus is involved in transcriptional repression by HDAC-independent mechanisms. {ECO:0000250|UniProtKB:Q9H7L9}. TISSUE SPECIFICITY: Expressed in all newborn tissues tested, including brain, kidney and liver. {ECO:0000269|PubMed:11909966}. +Q3TKT4 SMCA4_MOUSE Transcription activator BRG1 (EC 3.6.4.-) (ATP-dependent helicase SMARCA4) (BRG1-associated factor 190A) (BAF190A) (Protein brahma homolog 1) (SNF2-beta) (SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4) 1613 181,427 Alternative sequence (1); Chain (1); Compositional bias (4); Cross-link (1); Domain (5); Modified residue (17); Motif (1); Nucleotide binding (1); Region (4); Sequence conflict (1); Site (1) FUNCTION: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. Component of the CREST-BRG1 complex, a multiprotein complex that regulates promoter activation by orchestrating the calcium-dependent release of a repressor complex and the recruitment of an activator complex. In resting neurons, transcription of the c-FOS promoter is inhibited by SMARCA4-dependent recruitment of a phospho-RB1-HDAC repressor complex. Upon calcium influx, RB1 is dephosphorylated by calcineurin, which leads to release of the repressor complex. At the same time, there is increased recruitment of CREBBP to the promoter by a CREST-dependent mechanism, which leads to transcriptional activation. The CREST-BRG1 complex also binds to the NR2B promoter, and activity-dependent induction of NR2B expression involves the release of HDAC1 and recruitment of CREBBP (By similarity). Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development, a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role in regulating the activity of genes essential for dendrite growth. SMARCA4/BAF190A may promote neural stem cell self-renewal/proliferation by enhancing Notch-dependent proliferative signals, while concurrently making the neural stem cell insensitive to SHH-dependent differentiating cues. Acts as a corepressor of ZEB1 to regulate E-cadherin transcription and is required for induction of epithelial-mesenchymal transition (EMT) by ZEB1 (By similarity). Binds via DLX1 to enhancers located in the intergenic region between DLX5 and DLX6 and this binding is stabilized by the long non-coding RNA (lncRNA) Evf2 (PubMed:26138476). Binds to RNA in a promiscuous manner (PubMed:26138476). Binding to RNAs including lncRNA Evf2 leads to inhibition of SMARCA4 ATPase and chromatin remodeling activities (PubMed:26138476). {ECO:0000250|UniProtKB:P51532, ECO:0000269|PubMed:17640523, ECO:0000269|PubMed:26138476}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00549, ECO:0000269|PubMed:26138476}. Note=Colocalizes with long non-coding RNA Evf2 in nuclear RNA clouds. {ECO:0000269|PubMed:26138476}. SUBUNIT: Component of the multiprotein chromatin-remodeling complexes SWI/SNF: SWI/SNF-A (BAF), SWI/SNF-B (PBAF) and related complexes. The canonical complex contains a catalytic subunit (either SMARCA4/BRG1/BAF190A or SMARCA2/BRM/BAF190B) and at least SMARCE1, ACTL6A/BAF53, SMARCC1/BAF155, SMARCC2/BAF170, and SMARCB1/SNF5/BAF47. Other subunits specific to each of the complexes may also be present permitting several possible developmental- and tissue-specific combinations (Probable). Component of the BAF complex, which includes at least actin (ACTB), ARID1A/BAF250A, ARID1B/BAF250B, SMARCA2/BRM, SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57, SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C. In muscle cells, the BAF complex also contains DPF3. Component of neural progenitors-specific chromatin remodeling complex (npBAF complex) composed of at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, PHF10/BAF45A, ACTL6A/BAF53A and actin. Component of neuron-specific chromatin remodeling complex (nBAF complex) composed of at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, DPF1/BAF45B, DPF3/BAF45C, ACTL6B/BAF53B and actin (PubMed:17640523). Component of the SWI/SNF-B (PBAF) chromatin remodeling complex, at least composed of SMARCA4/BRG1, SMARCB1/BAF47/SNF5, ACTL6A/BAF53A or ACTL6B/BAF53B, SMARCE1/BAF57, SMARCD1/BAF60A, SMARCD2/BAF60B, perhaps SMARCD3/BAF60C, SMARCC1/BAF155, SMARCC2/BAF170, PBRM1/BAF180, ARID2/BAF200 and actin. Component of SWI/SNF (GBAF) subcomplex, which includes at least BICRA or BICRAL (mutually exclusive), BRD9, SS18, SMARCA2/BRM, SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, SMARCC1/BAF155, and SMARCD1/BAF60A (PubMed:29374058). Component of the BAF53 complex, at least composed of BAF53A, RUVBL1, SMARCA4/BRG1/BAF190A, and TRRAP, which preferentially acetylates histone H4 (and H2A) within nucleosomes (By similarity). Component of the CREST-BRG1 complex, at least composed of SMARCA4/BRG1/BAF190A, SS18L1/CREST, HDAC1, RB1 and SP1 (By similarity). Interacts with PHF10/BAF45A (PubMed:17640523). Interacts with MYOG (PubMed:16424906). Interacts directly with IKFZ1; the interaction associates IKFZ1 with the BAF complex. Interacts with ZEB1 (via N-terminus). Interacts with NR3C1, PGR, SMARD1, TOPBP1 and ZMIM2/ZIMP7. Interacts with (via the bromodomain) with TERT; the interaction regulates Wnt-mediated signaling (By similarity). Interacts with KDM6A and KDM6B (PubMed:21095589). Interacts with TBX21 in a KDM6B-dependent manner (PubMed:21095589). Interacts with HNRNPU; this interaction occurs in embryonic stem cells and stimulates global Pol II-mediated transcription (PubMed:22162999). Interacts with ACTL6A (By similarity). Interacts with DLX1 (PubMed:26138476). Interacts with DPF2 (By similarity). {ECO:0000250|UniProtKB:P51532, ECO:0000269|PubMed:16424906, ECO:0000269|PubMed:17640523, ECO:0000269|PubMed:21095589, ECO:0000269|PubMed:22162999, ECO:0000269|PubMed:26138476, ECO:0000269|PubMed:29374058, ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}. +Q8CEZ1 SMCO1_MOUSE Single-pass membrane and coiled-coil domain-containing protein 1 (Single-pass membrane protein with coiled-coil domains 1) 214 24,517 Alternative sequence (1); Chain (1); Coiled coil (1); Erroneous initiation (1); Transmembrane (1) TRANSMEM 59 81 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q9DA21 SMCO2_MOUSE Single-pass membrane and coiled-coil domain-containing protein 2 347 39,357 Chain (1); Coiled coil (1); Modified residue (1); Transmembrane (1) TRANSMEM 288 308 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q8BQM7 SMCO3_MOUSE Single-pass membrane and coiled-coil domain-containing protein 3 225 24,787 Chain (1); Coiled coil (2); Frameshift (1); Sequence conflict (1); Transmembrane (1) TRANSMEM 155 175 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q3UMB5 SMCR8_MOUSE Guanine nucleotide exchange protein SMCR8 (Smith-Magenis syndrome chromosomal region candidate gene 8 protein homolog) 935 104,957 Alternative sequence (1); Chain (1); Domain (3); Modified residue (8); Sequence conflict (4) FUNCTION: Component of the C9orf72-SMCR8 complex, a complex that has guanine nucleotide exchange factor (GEF) activity and regulates autophagy (PubMed:27617292). In the complex, C9orf72 and SMCR8 probably constitute the catalytic subunits that promote the exchange of GDP to GTP, converting inactive GDP-bound RAB8A and RAB39B into their active GTP-bound form, thereby promoting autophagosome maturation (By similarity). The C9orf72-SMCR8 complex also acts as a negative regulator of autophagy initiation by interacting with the ATG1/ULK1 kinase complex and inhibiting its protein kinase activity (PubMed:27617292). Acts as a regulator of mTORC1 signaling by promoting phosphorylation of mTORC1 substrates (By similarity). In addition to its activity in the cytoplasm within the C9orf72-SMCR8 complex, SMCR8 also localizes in the nucleus, where it associates with chromatin and negatively regulates expression of suppresses ULK1 and WIPI2 genes (By similarity). {ECO:0000250|UniProtKB:Q8TEV9, ECO:0000269|PubMed:27617292}. PTM: Phosphorylation by TBK1 is required to promote autophagosome maturation. Phosphorylated by ULK1. {ECO:0000250|UniProtKB:Q8TEV9}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27617292}. Nucleus {ECO:0000250|UniProtKB:Q8TEV9}. Note=Localizes mainly in the cytoplasm. {ECO:0000250|UniProtKB:Q8TEV9}. SUBUNIT: Interacts with C9orf72; the interaction is direct (PubMed:27875531). Component of the C9orf72-SMCR8 complex, at least composed of C9orf72, SMCR8 and WDR41 (Probable). The C9orf72-SMCR8 complex associates with the ATG1/ULK1 kinase complex (By similarity). {ECO:0000250|UniProtKB:Q8TEV9, ECO:0000269|PubMed:27875531}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11997338}. +Q6PE01 SNR40_MOUSE U5 small nuclear ribonucleoprotein 40 kDa protein (U5 snRNP 40 kDa protein) (WD repeat-containing protein 57) 358 39,276 Chain (1); Cross-link (2); Frameshift (1); Modified residue (1); Repeat (7); Sequence conflict (2) FUNCTION: Component of the U5 small nuclear ribonucleoprotein (snRNP) complex. The U5 snRNP is part of the spliceosome, a multiprotein complex that catalyzes the removal of introns from pre-messenger RNAs (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Identified in the spliceosome C complex. Associated with the spliceosome complex. Part of the U5 snRNP complex. Interacts with PRPF8. Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, WDR57, SNRNP40, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39 (By similarity). {ECO:0000250}. +Q9D361 SNR48_MOUSE U11/U12 small nuclear ribonucleoprotein 48 kDa protein (U11/U12 snRNP 48 kDa protein) 337 39,453 Alternative sequence (3); Chain (1); Cross-link (2); Sequence caution (1); Sequence conflict (9); Zinc finger (1) FUNCTION: Likely involved in U12-type 5' splice site recognition. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the U11/U12 snRNPs that are part of the U12-type spliceosome. Not found in the major spliceosome (By similarity). {ECO:0000250}. DOMAIN: The CHHC region interacts with the 5' splice site of the U12-type Intron. {ECO:0000250}. +Q8VDU5 SNRK_MOUSE SNF-related serine/threonine-protein kinase (EC 2.7.11.1) (SNF1-related kinase) 748 81,913 Active site (1); Binding site (1); Chain (1); Domain (2); Modified residue (9); Nucleotide binding (1); Sequence conflict (3) FUNCTION: May play a role in hematopoietic cell proliferation or differentiation. Potential mediator of neuronal apoptosis (By similarity). {ECO:0000250|UniProtKB:Q63553, ECO:0000250|UniProtKB:Q9NRH2}. PTM: Autophosphorylated. Phosphorylation on Thr-173 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed in all tissues examined. {ECO:0000269|PubMed:12234663}. +Q9Z315 SNUT1_MOUSE U4/U6.U5 tri-snRNP-associated protein 1 (Hypoxia-associated factor) (Squamous cell carcinoma antigen recognized by T-cells 1) (SART-1) (mSART-1) 806 90,885 Chain (1); Coiled coil (2); Cross-link (23); Modified residue (15); Sequence conflict (4) FUNCTION: Plays a role in mRNA splicing as a component of the U4/U6-U5 tri-snRNP, one of the building blocks of the spliceosome. May also bind to DNA. Appears to play a role in hypoxia-induced regulation of EPO gene expression. {ECO:0000269|PubMed:10887110}. PTM: Sumoylated with SUMO2. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Identified in the spliceosome C complex. Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed. Shows a high expression in fetal liver and a low expression in adult liver. {ECO:0000269|PubMed:10887110}. +P62855 RS26_MOUSE 40S ribosomal protein S26 115 13,015 Chain (1); Modified residue (1); Sequence conflict (1) SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P62854}. Cytoplasm {ECO:0000250|UniProtKB:P62854}. Rough endoplasmic reticulum {ECO:0000250|UniProtKB:P49171}. Note=Detected on cytosolic polysomes (By similarity). Detected in ribosomes that are associated with the rough endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:P49171, ECO:0000250|UniProtKB:P62854}. SUBUNIT: Component of the 40S small ribosomal subunit. {ECO:0000250|UniProtKB:P49171}. +Q9D495 SYCE1_MOUSE Synaptonemal complex central element protein 1 329 38,205 Chain (1); Coiled coil (2); Compositional bias (1) FUNCTION: Major component of the transverse central element of synaptonemal complexes (SCS), formed between homologous chromosomes during meiotic prophase. Requires SYCP1 in order to be incorporated into the central element. May have a role in the synaptonemal complex assembly, stabilization and recombination. {ECO:0000269|PubMed:15944401}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15944401}. Chromosome {ECO:0000269|PubMed:15944401}. Note=Associates with chromatin. In prophase I stage of meiosis, localizes in the transverse central elements of the central region between lateral elements of the synaptonemal complexes. Found only where the chromosome cores are synapsed. Colocalizes with SYCE2 in the central elements. {ECO:0000269|PubMed:15944401}. SUBUNIT: Homodimer (PubMed:15944401). Found in a complex with SYCP1 and SYCE2 (PubMed:15944401). Interacts with SYCP1, SYCE2 and SYCE3 (PubMed:15944401, PubMed:21637789). Interacts with SIX6OS1 (PubMed:27796301). {ECO:0000269|PubMed:15944401, ECO:0000269|PubMed:21637789, ECO:0000269|PubMed:27796301}. TISSUE SPECIFICITY: Meiotic cells (at protein level). Expressed in the ovary and testis. {ECO:0000269|PubMed:15944401}. +Q6ZWU9 RS27_MOUSE 40S ribosomal protein S27 84 9,461 Chain (1); Modified residue (1); Zinc finger (1) FUNCTION: Component of the small ribosomal subunit (By similarity). Required for proper rRNA processing and maturation of 18S rRNAs (By similarity). {ECO:0000250|UniProtKB:P42677}. SUBUNIT: Component of the small ribosomal subunit. {ECO:0000250|UniProtKB:P42677}. +Q8BJ73 RSPO4_MOUSE R-spondin-4 (Cysteine-rich and single thrombospondin domain-containing protein 4) (Cristin-4) (mCristin-4) (Roof plate-specific spondin-4) 228 25,866 Alternative sequence (2); Chain (1); Disulfide bond (11); Domain (1); Frameshift (1); Glycosylation (1); Repeat (1); Signal peptide (1) FUNCTION: Activator of the canonical Wnt signaling pathway by acting as a ligand for LGR4-6 receptors. Upon binding to LGR4-6 (LGR4, LGR5 or LGR6), LGR4-6 associate with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increase expression of target genes. Also regulates the canonical Wnt/beta-catenin-dependent pathway and non-canonical Wnt signaling by acting as an inhibitor of ZNRF3, an important regulator of the Wnt signaling pathway. {ECO:0000269|PubMed:21693646}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Binds heparin (By similarity). Interacts with LGR4, LGR5 and LGR6. {ECO:0000250, ECO:0000269|PubMed:21693646}. DOMAIN: The FU repeat is required for activation and stabilization of beta-catenin. {ECO:0000250}. +Q9D0G0 RT30_MOUSE 28S ribosomal protein S30, mitochondrial (MRP-S30) (S30mt) 442 49,939 Chain (1); Sequence conflict (3) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. SUBUNIT: Component of the mitochondrial ribosome small subunit (28S) which comprises a 12S rRNA and about 30 distinct proteins. +Q99N85 RT18A_MOUSE 28S ribosomal protein S18a, mitochondrial (MRP-S18-a) (Mrps18a) (S18mt-a) (28S ribosomal protein S18-3, mitochondrial) (MRP-S18-3) 196 22,321 Chain (1); Erroneous initiation (1); Sequence conflict (1); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P82919}. SUBUNIT: Component of the mitochondrial ribosome small subunit (28S) which comprises a 12S rRNA and about 30 distinct proteins. {ECO:0000250|UniProtKB:P82919}. +Q80ZK0 RT10_MOUSE 28S ribosomal protein S10, mitochondrial (MRP-S10) (S10mt) 160 18,698 Chain (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P82664}. SUBUNIT: Component of the mitochondrial ribosome small subunit (28S) which comprises a 12S rRNA and about 30 distinct proteins. {ECO:0000250|UniProtKB:P82664}. +Q99LF4 RTCB_MOUSE tRNA-splicing ligase RtcB homolog (EC 6.5.1.3) (Focal adhesion-associated protein) (FAAP) 505 55,249 Active site (1); Binding site (3); Chain (1); Cross-link (1); Metal binding (6); Modified residue (1); Nucleotide binding (3); Sequence conflict (5) FUNCTION: Catalytic subunit of the tRNA-splicing ligase complex that acts by directly joining spliced tRNA halves to mature-sized tRNAs by incorporating the precursor-derived splice junction phosphate into the mature tRNA as a canonical 3',5'-phosphodiester. May act as an RNA ligase with broad substrate specificity, and may function toward other RNAs (By similarity). Essential during post-implantation development of embryos. {ECO:0000250, ECO:0000269|PubMed:20510672}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03144, ECO:0000269|PubMed:18508721}. Note=Enters into the nucleus in case of active transcription while it accumulates in cytosol when transcription level is low. {ECO:0000250}. SUBUNIT: Catalytic component of the tRNA-splicing ligase complex. {ECO:0000255|HAMAP-Rule:MF_03144}. TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in the epididymis with predominant enrichment in the initial segment. During sexual maturation, it is expressed in the caput epididymides. {ECO:0000269|PubMed:21046479}. +Q8C8C1 RTP1_MOUSE Receptor-transporting protein 1 263 30,732 Chain (1); Topological domain (2); Transmembrane (1) TRANSMEM 239 259 Helical. {ECO:0000255}. TOPO_DOM 1 238 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 260 263 Extracellular. {ECO:0000255}. FUNCTION: Specifically promotes functional cell surface expression of olfactory receptors, but not of other GPCRs. {ECO:0000269|PubMed:15550249}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15550249}; Single-pass type III membrane protein {ECO:0000269|PubMed:15550249}. Note=Effective cell surface expression depends upon interaction with olfactory receptors. SUBUNIT: Interacts with olfactory receptors. {ECO:0000269|PubMed:15550249}. TISSUE SPECIFICITY: Predominantly expressed in olfactory and vomeronasal organs, in mature olfactory sensory neurons. {ECO:0000269|PubMed:15550249}. +Q03347 RUNX1_MOUSE Runt-related transcription factor 1 (Acute myeloid leukemia 1 protein) (Core-binding factor subunit alpha-2) (CBF-alpha-2) (Oncogene AML-1) (Polyomavirus enhancer-binding protein 2 alpha B subunit) (PEA2-alpha B) (PEBP2-alpha B) (SL3-3 enhancer factor 1 alpha B subunit) (SL3/AKV core-binding factor alpha B subunit) 451 48,610 Alternative sequence (7); Beta strand (13); Binding site (4); Chain (1); Compositional bias (1); Domain (1); Helix (3); Modified residue (13); Mutagenesis (13); Region (6); Sequence conflict (1); Turn (1) FUNCTION: Forms the heterodimeric complex core-binding factor (CBF) with CBFB. RUNX members modulate the transcription of their target genes through recognizing the core consensus binding sequence 5'-TGTGGT-3', or very rarely, 5'-TGCGGT-3', within their regulatory regions via their runt domain, while CBFB is a non-DNA-binding regulatory subunit that allosterically enhances the sequence-specific DNA-binding capacity of RUNX. The heterodimers bind to the core site of a number of enhancers and promoters, including murine leukemia virus, polyomavirus enhancer, T-cell receptor enhancers, LCK, IL3 and GM-CSF promoters (Probable). Essential for the development of normal hematopoiesis. Acts synergistically with ELF4 to transactivate the IL-3 promoter and with ELF2 to transactivate the BLK promoter. Inhibits KAT6B-dependent transcriptional activation (By similarity). Involved in lineage commitment of immature T cell precursors. CBF complexes repress ZBTB7B transcription factor during cytotoxic (CD8+) T cell development. They bind to RUNX-binding sequence within the ZBTB7B locus acting as transcriptional silencer and allowing for cytotoxic T cell differentiation (PubMed:18258917). CBF complexes binding to the transcriptional silencer is essential for recruitment of nuclear protein complexes that catalyze epigenetic modifications to establish epigenetic ZBTB7B silencing (PubMed:23481257). Controls the anergy and suppressive function of regulatory T-cells (Treg) by associating with FOXP3. Activates the expression of IL2 and IFNG and down-regulates the expression of TNFRSF18, IL2RA and CTLA4, in conventional T-cells (PubMed:17377532). Positively regulates the expression of RORC in T-helper 17 cells (PubMed:21151104). {ECO:0000250|UniProtKB:Q01196, ECO:0000269|PubMed:17377532, ECO:0000269|PubMed:18258917, ECO:0000269|PubMed:21151104, ECO:0000269|PubMed:23481257, ECO:0000305}.; FUNCTION: Isoform 4 shows higher binding activities for target genes and binds TCR-beta-E2 and RAG-1 target site with threefold higher affinity than other isoforms. It is less effective in the context of neutrophil terminal differentiation. {ECO:0000269|PubMed:11203699}. PTM: Phosphorylated in its C-terminus upon IL-6 treatment. Phosphorylation enhances interaction with KAT6A (By similarity). {ECO:0000250}.; PTM: Methylated. {ECO:0000250}.; PTM: Phosphorylated in Ser-249 Thr-273 and Ser-276 by HIPK2 when associated with CBFB and DNA. This phosphorylation promotes subsequent EP300 phosphorylation. {ECO:0000269|PubMed:16917507}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17377532}. SUBUNIT: Heterodimer with CBFB. RUNX1 binds DNA as a monomer and through the Runt domain. DNA-binding is increased by heterodimerization. Interacts with TLE1 and ALYREF/THOC4. Interacts with HIPK2, ELF1, ELF2 and SPI1. Interacts via its Runt domain with the ELF4 N-terminal region. Interaction with ELF2 isoform 2 (NERF-1a) may act to repress RUNX1-mediated transactivation. Interacts with KAT6A and KAT6B. Interacts with SUV39H1, leading to abrogation of transactivating and DNA-binding properties of RUNX1 (By similarity). Interacts with YAP1. Interaction with CDK6 prevents myeloid differentiation, reducing its transcription transactivation activity (By similarity). Found in a complex with PRMT5, RUNX1 and CBFB. Interacts with FOXP3. Interacts with TBX21 (PubMed:21151104). Interacts with DPF2 (By similarity). {ECO:0000250|UniProtKB:Q01196, ECO:0000269|PubMed:11257229, ECO:0000269|PubMed:11375505, ECO:0000269|PubMed:16917507, ECO:0000269|PubMed:17377532, ECO:0000269|PubMed:21151104, ECO:0000269|PubMed:22193545}. DOMAIN: A proline/serine/threonine rich region at the C-terminus is necessary for transcriptional activation of target genes. TISSUE SPECIFICITY: Isoform 4 is expressed at high levels in thymus, spleen and T-cell lines and at lower levels in myeloid cell lines and nonhematopoietic cells. Isoform 5 is expressed ubiquitously in lumbar vertebrae, brain, kidney, heart, muscle, ovary and osteoblast-like cell line MC3T3-E1. DISEASE: Note=Mice with an Runx1 lacking the DNA-binding region are found to die between embryonic days 11.5 to 12.5 due to hemorrhaging in the central nervous system. This hemorrhaging is preceded by necrosis and hematopoiesis is blocked (PubMed:8622955). {ECO:0000269|PubMed:8622955}. +P48776 T23O_MOUSE Tryptophan 2,3-dioxygenase (TDO) (EC 1.13.11.11) (Tryptamin 2,3-dioxygenase) (Tryptophan oxygenase) (TO) (TRPO) (Tryptophan pyrrolase) (Tryptophanase) 406 47,756 Binding site (2); Chain (1); Metal binding (1); Modified residue (1); Region (1); Sequence conflict (4) Amino-acid degradation; L-tryptophan degradation via kynurenine pathway; L-kynurenine from L-tryptophan: step 1/2. FUNCTION: Heme-dependent dioxygenase that catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring and converts L-tryptophan to N-formyl-L-kynurenine. Catalyzes the oxidative cleavage of the indole moiety. {ECO:0000255|HAMAP-Rule:MF_03020}. SUBUNIT: Homotetramer. Dimer of dimers. {ECO:0000255|HAMAP-Rule:MF_03020}. +P0DN90 T254B_MOUSE Transmembrane protein 254b 123 14,239 Alternative sequence (1); Chain (1); Transmembrane (3) TRANSMEM 15 35 Helical. {ECO:0000255}.; TRANSMEM 63 83 Helical. {ECO:0000255}.; TRANSMEM 95 115 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q01887 RYK_MOUSE Tyrosine-protein kinase RYK (EC 2.7.10.1) (Kinase VIK) (Met-related kinase) (NYK-R) 594 66,285 Active site (1); Binding site (1); Chain (1); Domain (2); Erroneous initiation (1); Frameshift (1); Glycosylation (5); Modified residue (1); Nucleotide binding (1); Sequence conflict (11); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 212 239 Helical. {ECO:0000255}. TOPO_DOM 35 211 Extracellular. {ECO:0000255}.; TOPO_DOM 240 594 Cytoplasmic. {ECO:0000255}. FUNCTION: May be a coreceptor along with FZD8 of Wnt proteins, such as WNT1, WNT3, WNT3A and WNT5A. Involved in neuron differentiation, axon guidance, corpus callosum establishment and neurite outgrowth. In response to WNT3 stimulation, receptor C-terminal cleavage occurs in its transmembrane region and allows the C-terminal intracellular product to translocate from the cytoplasm to the nucleus where it plays a crucial role in neuronal development. {ECO:0000269|PubMed:15454084, ECO:0000269|PubMed:16116452, ECO:0000269|PubMed:16723543, ECO:0000269|PubMed:19000841}. PTM: Proteolytically cleaved, in part by presenilin, in response to WNT3 stimulation. {ECO:0000269|PubMed:19000841}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:19000841}; Single-pass type I membrane protein {ECO:0000269|PubMed:19000841}. Nucleus {ECO:0000269|PubMed:19000841}. Cytoplasm {ECO:0000269|PubMed:19000841}. Note=In cells that have undergone neuronal differentiation, the C-terminal cleaved part is translocated from the cytoplasm to the nucleus. SUBUNIT: Interacts with DVL1 (via PDZ domain). {ECO:0000269|PubMed:15454084}. DOMAIN: The extracellular WIF domain is responsible for Wnt binding. {ECO:0000269|PubMed:15454084}. TISSUE SPECIFICITY: Is detected in all the tissues. Highest levels are seen in the ovary, lung and placenta. +E9PZQ0 RYR1_MOUSE Ryanodine receptor 1 (RYR-1) (RyR1) (Skeletal muscle calcium release channel) (Skeletal muscle ryanodine receptor) (Skeletal muscle-type ryanodine receptor) (Type 1 ryanodine receptor) 5035 565,039 Binding site (1); Chain (1); Compositional bias (3); Domain (9); Intramembrane (1); Metal binding (3); Modified residue (8); Motif (1); Mutagenesis (2); Nucleotide binding (3); Region (3); Repeat (6); Sequence conflict (6); Topological domain (8); Transmembrane (6) INTRAMEM 4878 4897 Pore-forming. {ECO:0000250|UniProtKB:P11716}. TRANSMEM 4557 4577 Helical; Name=1. {ECO:0000250|UniProtKB:P11716}.; TRANSMEM 4639 4659 Helical; Name=2. {ECO:0000250|UniProtKB:P11716}.; TRANSMEM 4778 4800 Helical; Name=3. {ECO:0000250|UniProtKB:P11716}.; TRANSMEM 4802 4818 Helical; Name=4. {ECO:0000250|UniProtKB:P11716}.; TRANSMEM 4834 4854 Helical; Name=5. {ECO:0000250|UniProtKB:P11716}.; TRANSMEM 4918 4938 Helical; Name=6. {ECO:0000250|UniProtKB:P11716}. TOPO_DOM 1 4556 Cytoplasmic. {ECO:0000250|UniProtKB:P11716}.; TOPO_DOM 4578 4638 Lumenal. {ECO:0000250|UniProtKB:P11716}.; TOPO_DOM 4660 4777 Cytoplasmic. {ECO:0000250|UniProtKB:P11716}.; TOPO_DOM 4801 4801 Lumenal. {ECO:0000250|UniProtKB:P11716}.; TOPO_DOM 4819 4833 Cytoplasmic. {ECO:0000250|UniProtKB:P11716}.; TOPO_DOM 4855 4877 Lumenal. {ECO:0000250|UniProtKB:P11716}.; TOPO_DOM 4898 4917 Lumenal. {ECO:0000250|UniProtKB:P11716}.; TOPO_DOM 4939 5035 Cytoplasmic. {ECO:0000250|UniProtKB:P11716}. FUNCTION: Calcium channel that mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytoplasm and thereby plays a key role in triggering muscle contraction following depolarization of T-tubules (PubMed:18003898, PubMed:7515481, PubMed:7621815, PubMed:21156754). Repeated very high-level exercise increases the open probability of the channel and leads to Ca(2+) leaking into the cytoplasm (PubMed:18268335). Can also mediate the release of Ca(2+) from intracellular stores in neurons, and may thereby promote prolonged Ca(2+) signaling in the brain (PubMed:22036948). Required for normal embryonic development of muscle fibers and skeletal muscle (PubMed:7515481). Required for normal heart morphogenesis, skin development and ossification during embryogenesis (PubMed:18003898, PubMed:7515481). {ECO:0000269|PubMed:18003898, ECO:0000269|PubMed:18268335, ECO:0000269|PubMed:21156754, ECO:0000269|PubMed:22036948, ECO:0000269|PubMed:7515481, ECO:0000269|PubMed:7621815}. PTM: Channel activity is modulated by phosphorylation. Phosphorylation at Ser-2844 may increase channel activity. Repeated very high-level exercise increases phosphorylation at Ser-2844. {ECO:0000269|PubMed:18268335, ECO:0000269|PubMed:21156754}.; PTM: Activated by reversible S-nitrosylation (PubMed:22036948). Repeated very high-level exercise increases S-nitrosylation. {ECO:0000250, ECO:0000269|PubMed:18268335, ECO:0000269|PubMed:22036948}. SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:18003898, ECO:0000269|PubMed:7621815}; Multi-pass membrane protein {ECO:0000269|PubMed:18003898}. Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Sarcoplasmic reticulum {ECO:0000250|UniProtKB:P11716}. Note=The number of predicted transmembrane domains varies between orthologs, but the 3D-structures show the presence of six transmembrane regions. Both N-terminus and C-terminus are cytoplasmic. {ECO:0000250|UniProtKB:P11716}. SUBUNIT: Homotetramer (PubMed:18003898). Can also form heterotetramers with RYR2 (By similarity). Identified in a complex composed of RYR1, PDE4D, PKA, FKBP1A and protein phosphatase 1 (PP1) (PubMed:18268335). Repeated very high-level exercise decreases interaction with PDE4D and protein phosphatase 1 (PP1) (PubMed:18268335). Interacts with CALM; CALM with bound calcium inhibits the RYR1 channel activity (By similarity). Interacts with S100A1 (By similarity). Interacts with FKBP1A; this stabilizes the closed conformation of the channel. Interacts with CACNA1S; interaction with CACNA1S is important for activation of the RYR1 channel. Interacts with CACNB1. Interacts with TRDN and ASPH; these interactions stimulate RYR1 channel activity. Interacts with SELENON (By similarity). {ECO:0000250|UniProtKB:P11716, ECO:0000250|UniProtKB:P21817, ECO:0000269|PubMed:18003898, ECO:0000269|PubMed:18268335}. DOMAIN: The calcium release channel activity resides in the C-terminal region while the remaining part of the protein constitutes the 'foot' structure spanning the junctional gap between the sarcoplasmic reticulum (SR) and the T-tubule (PubMed:7621815, PubMed:7724570). Pore opening is mediated via the cytoplasmic calcium-binding domains that mediate a small rotation of the channel-forming transmembrane regions that then leads to channel opening (By similarity). {ECO:0000250|UniProtKB:P11716, ECO:0000269|PubMed:7621815, ECO:0000269|PubMed:7724570}. TISSUE SPECIFICITY: Detected in muscle and myotubes (at protein level) (PubMed:18003898). Ubiquitous. Detected in diaphragm, skeletal muscle, esophagus, spleen, submaxillary gland, adrenal gland, cerebellum, brain and in testis germ cells. {ECO:0000269|PubMed:18003898, ECO:0000269|PubMed:21156754, ECO:0000269|PubMed:22036948, ECO:0000269|PubMed:7621815, ECO:0000269|PubMed:7876312}. +P62309 RUXG_MOUSE Small nuclear ribonucleoprotein G (snRNP-G) (Sm protein G) (Sm-G) (SmG) 76 8,496 Chain (1) FUNCTION: Plays role in pre-mRNA splicing as core component of the SMN-Sm complex that mediates spliceosomal snRNP assembly and as component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Component of both the pre-catalytic spliceosome B complex and activated spliceosome C complexes. Is also a component of the minor U12 spliceosome. As part of the U7 snRNP it is involved in histone 3'-end processing. {ECO:0000250|UniProtKB:P62308}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P62308}. Nucleus {ECO:0000250|UniProtKB:P62308}. Note=SMN-mediated assembly into core snRNPs occurs in the cytosol before SMN-mediated transport to the nucleus to be included in spliceosomes. {ECO:0000250|UniProtKB:P62308}. SUBUNIT: Core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Most spliceosomal snRNPs contain a common set of Sm proteins, SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. Component of the U1 snRNP. The U1 snRNP is composed of the U1 snRNA and the 7 core Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG, and at least three U1 snRNP-specific proteins SNRNP70/U1-70K, SNRPA/U1-A and SNRPC/U1-C. Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39, plus LSM2, LSM3, LSM4, LSM5, LSM6, LSM7 and LSM8. Component of the U7 snRNP complex, or U7 Sm protein core complex, that is composed of the U7 snRNA and at least LSM10, LSM11, SNRPB, SNRPD3, SNRPE, SNRPF and SNRPG; the complex does not contain SNRPD1 and SNRPD2. Component of the U11/U12 snRNPs that are part of the U12-type spliceosome. Part of the SMN-Sm complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8, STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG; catalyzes core snRNPs assembly. Forms a 6S pICln-Sm complex composed of CLNS1A/pICln, SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG; ring-like structure where CLNS1A/pICln mimics additional Sm proteins and which is unable to assemble into the core snRNP. {ECO:0000250|UniProtKB:P62308}. +Q9JIS8 S12A4_MOUSE Solute carrier family 12 member 4 (Electroneutral potassium-chloride cotransporter 1) (Erythroid K-Cl cotransporter 1) (mKCC1) 1085 120,624 Chain (1); Compositional bias (2); Glycosylation (4); Modified residue (6); Topological domain (7); Transmembrane (12) TRANSMEM 119 139 Helical. {ECO:0000255}.; TRANSMEM 149 169 Helical. {ECO:0000255}.; TRANSMEM 215 235 Helical. {ECO:0000255}.; TRANSMEM 253 273 Helical. {ECO:0000255}.; TRANSMEM 276 296 Helical. {ECO:0000255}.; TRANSMEM 356 376 Helical. {ECO:0000255}.; TRANSMEM 416 436 Helical. {ECO:0000255}.; TRANSMEM 453 473 Helical. {ECO:0000255}.; TRANSMEM 494 514 Helical. {ECO:0000255}.; TRANSMEM 567 587 Helical. {ECO:0000255}.; TRANSMEM 628 648 Helical. {ECO:0000255}.; TRANSMEM 845 865 Helical. {ECO:0000255}. TOPO_DOM 1 118 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 170 214 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 274 275 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 377 415 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 474 493 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 588 627 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 866 1085 Cytoplasmic. {ECO:0000255}. FUNCTION: Mediates electroneutral potassium-chloride cotransport when activated by cell swelling. May contribute to cell volume homeostasis in single cells. May be involved in the regulation of basolateral Cl(-) exit in NaCl absorbing epithelia. PTM: N-glycosylated. {ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:19656770}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SUBUNIT: Homomultimer and heteromultimer with other K-Cl cotransporters. {ECO:0000269|PubMed:11551954}. TISSUE SPECIFICITY: Detected in embryo, adult heart, erythrocytes, brain, kidney, stomach, ovary, testis and liver. +Q9D708 S10AG_MOUSE Protein S100-A16 (Protein S100F) (S100 calcium binding protein A16) 124 14,324 Calcium binding (1); Chain (1); Domain (2); Sequence conflict (1) FUNCTION: Calcium-binding protein. Binds one calcium ion per monomer (PubMed:17030513). Can promote differentiation of adipocytes (in vitro). Overexpression in 3T3-L1 preadipocytes increases their proliferation, enhances adipogenesis and reduces insulin-stimulated glucose uptake (PubMed:21266506, PubMed:23526364). {ECO:0000269|PubMed:17030513, ECO:0000269|PubMed:21266506, ECO:0000269|PubMed:23526364}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:17030513, ECO:0000269|PubMed:21266506}. Cytoplasm {ECO:0000269|PubMed:17030513, ECO:0000269|PubMed:21266506}. Note=Primarily nucleolar. A high intracellular calcium level induces nucleolar exit and nucleocytoplasmic transport, whereas a low intracellular calcium level leads to nuclear translocation and accumulation within specific region of nucleoli (PubMed:17030513). SUBUNIT: Homodimer (PubMed:17030513). Interacts with TP53 (PubMed:21266506). {ECO:0000269|PubMed:17030513, ECO:0000269|PubMed:21266506}. DOMAIN: S100A16 proteins, but not other S100 proteins, have only one functional Ca(2+) binding site per monomer (PubMed:14684152, PubMed:17030513). Upon Ca(2+) binding, undergoes conformational changes leading to the exposure of hydrophobic patches which could be implicated in the Ca(2+)-dependent nuclear export. Binds Zn(2+) (PubMed:17030513). Ca(2+) and Zn(2+) do not bind to the same site (PubMed:17030513). Does not bind Cu(2+) (PubMed:17030513). {ECO:0000269|PubMed:17030513, ECO:0000303|PubMed:14684152}. TISSUE SPECIFICITY: Ubiquitous (PubMed:17030513). Widely distributed throughout the adult brain and predominantly expressed within specific astrocyte populations (PubMed:17030513). Expressed at high level in adipose tissues of obese animals (PubMed:21266506). {ECO:0000269|PubMed:17030513, ECO:0000269|PubMed:21266506}. +Q99P65 S29A3_MOUSE Equilibrative nucleoside transporter 3 (mENT3) (Solute carrier family 29 member 3) 475 51,719 Chain (1); Glycosylation (1); Modified residue (1); Topological domain (12); Transmembrane (11) TRANSMEM 52 72 Helical. {ECO:0000255}.; TRANSMEM 106 126 Helical. {ECO:0000255}.; TRANSMEM 135 155 Helical. {ECO:0000255}.; TRANSMEM 163 183 Helical. {ECO:0000255}.; TRANSMEM 200 220 Helical. {ECO:0000255}.; TRANSMEM 231 251 Helical. {ECO:0000255}.; TRANSMEM 306 326 Helical. {ECO:0000255}.; TRANSMEM 341 361 Helical. {ECO:0000255}.; TRANSMEM 378 398 Helical. {ECO:0000255}.; TRANSMEM 416 436 Helical. {ECO:0000255}.; TRANSMEM 451 471 Helical. {ECO:0000255}. TOPO_DOM 1 51 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 73 105 Extracellular. {ECO:0000255}.; TOPO_DOM 127 134 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 156 162 Extracellular. {ECO:0000255}.; TOPO_DOM 184 199 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 221 230 Extracellular. {ECO:0000255}.; TOPO_DOM 252 305 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 327 340 Extracellular. {ECO:0000255}.; TOPO_DOM 362 377 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 399 415 Extracellular. {ECO:0000255}.; TOPO_DOM 437 450 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 472 475 Extracellular. {ECO:0000255}. FUNCTION: Mediates both influx and efflux of nucleosides across the membrane (equilibrative transporter). Mediates transport of adenine, adenosine and uridine (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Late endosome membrane. Lysosome membrane. Note=Intracellular localization shows a partial overlap with late endosomes/lysosomes. Not detected at the cell surface (By similarity). {ECO:0000250}. +P97858 S35B1_MOUSE Solute carrier family 35 member B1 (UDP-galactose translocator 2) (UDP-galactose transporter-related protein 1) (UGTrel1) 322 35,883 Alternative sequence (1); Chain (1); Motif (1); Transmembrane (8) TRANSMEM 12 32 Helical. {ECO:0000255}.; TRANSMEM 51 71 Helical. {ECO:0000255}.; TRANSMEM 85 105 Helical. {ECO:0000255}.; TRANSMEM 136 156 Helical. {ECO:0000255}.; TRANSMEM 168 188 Helical. {ECO:0000255}.; TRANSMEM 210 230 Helical. {ECO:0000255}.; TRANSMEM 243 263 Helical. {ECO:0000255}.; TRANSMEM 285 305 Helical. {ECO:0000255}. FUNCTION: Probable sugar transporter. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. DOMAIN: The di-lysine motif confers endoplasmic reticulum localization for type I membrane proteins. {ECO:0000250}. +Q91ZN5 S35B2_MOUSE Adenosine 3'-phospho 5'-phosphosulfate transporter 1 (PAPS transporter 1) (Solute carrier family 35 member B2) 431 47,370 Alternative sequence (1); Chain (1); Frameshift (1); Sequence conflict (1); Transmembrane (9) TRANSMEM 5 25 Helical. {ECO:0000255}.; TRANSMEM 39 59 Helical. {ECO:0000255}.; TRANSMEM 109 129 Helical. {ECO:0000255}.; TRANSMEM 153 173 Helical. {ECO:0000255}.; TRANSMEM 238 258 Helical. {ECO:0000255}.; TRANSMEM 265 285 Helical. {ECO:0000255}.; TRANSMEM 299 319 Helical. {ECO:0000255}.; TRANSMEM 353 373 Helical. {ECO:0000255}.; TRANSMEM 387 407 Helical. {ECO:0000255}. FUNCTION: Mediates the transport of adenosine 3'-phospho 5'-phosphosulfate (PAPS), from cytosol into Golgi. PAPS is a universal sulfuryl donor for sulfation events that take place in the Golgi (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q8CFJ7 S2545_MOUSE Solute carrier family 25 member 45 288 31,690 Alternative sequence (2); Chain (1); Erroneous initiation (1); Frameshift (1); Repeat (3); Transmembrane (6) TRANSMEM 6 26 Helical; Name=1. {ECO:0000255}.; TRANSMEM 58 78 Helical; Name=2. {ECO:0000255}.; TRANSMEM 102 122 Helical; Name=3. {ECO:0000255}.; TRANSMEM 166 186 Helical; Name=4. {ECO:0000255}.; TRANSMEM 202 222 Helical; Name=5. {ECO:0000255}.; TRANSMEM 266 286 Helical; Name=6. {ECO:0000255}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed, with highest levels in testis, liver and kidney and low levels in brain, including cortex, cerebellum, hippocampus and hypothalamus, and heart. {ECO:0000269|PubMed:19287344}. +Q8CIW6 S26A6_MOUSE Solute carrier family 26 member 6 (Anion exchange transporter) (Chloride-formate exchanger) (Pendrin-L1) (Pendrin-like protein 1) (Putative anion transporter-1) (Pat-1) 758 82,834 Alternative sequence (2); Chain (1); Domain (1); Erroneous gene model prediction (3); Modified residue (2); Mutagenesis (1); Sequence conflict (4); Topological domain (9); Transmembrane (8) TRANSMEM 118 138 Helical. {ECO:0000255}.; TRANSMEM 188 208 Helical. {ECO:0000255}.; TRANSMEM 264 284 Helical. {ECO:0000255}.; TRANSMEM 293 313 Helical. {ECO:0000255}.; TRANSMEM 341 361 Helical. {ECO:0000255}.; TRANSMEM 381 401 Helical. {ECO:0000255}.; TRANSMEM 418 438 Helical. {ECO:0000255}.; TRANSMEM 486 506 Helical. {ECO:0000255}. TOPO_DOM 1 117 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 139 187 Extracellular. {ECO:0000255}.; TOPO_DOM 209 263 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 285 292 Extracellular. {ECO:0000255}.; TOPO_DOM 314 340 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 362 380 Extracellular. {ECO:0000255}.; TOPO_DOM 402 417 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 439 485 Extracellular. {ECO:0000255}.; TOPO_DOM 507 758 Cytoplasmic. {ECO:0000255}. FUNCTION: Apical membrane anion-exchanger with wide epithelial distribution that plays a role as a component of the pH buffering system for maintaining acid-base homeostasis. Acts as a versatile DIDS-sensitive inorganic and organic anion transporter that mediates the uptake of monovalent anions like chloride, bicarbonate, formate and hydroxyl ion and divalent anions like sulfate and oxalate. Function in multiple exchange modes involving pairs of these anions, which include chloride-bicarbonate, chloride-oxalate, oxalate-formate, oxalate-sulfate and chloride-formate exchange. Apical membrane chloride-bicarbonate exchanger that mediates luminal chloride absorption and bicarbonate secretion by the small intestinal brush border membrane and contributes to intracellular pH regulation in the duodenal upper villous epithelium during proton-coupled peptide absorption, possibly by providing a bicarbonate import pathway. Its association with carbonic anhydrase CA2 forms a bicarbonate transport metabolon; hence maximizes the local concentration of bicarbonate at the transporter site. Mediates also intestinal chloride absorption and oxalate secretion, thereby preventing hyperoxaluria and calcium oxalate urolithiasis. Transepithelial oxalate secretion, chloride-formate, chloride-oxalate and chloride-bicarbonate transport activities in the duodenum are inhibited by PKC activation in a calcium-independent manner. The apical membrane chloride-bicarbonate exchanger provides also a major route for fluid and bicarbonate secretion into the proximal tubules of the kidney as well as into the proximal part of the interlobular pancreatic ductal tree, where it mediates electrogenic chloride-bicarbonate exchange with a chloride-bicarbonate stoichiometry of 1:2, and hence will dilute and alkalinize protein-rich acinar secretion. Mediates also the transcellular sulfate absorption and oxalate secretion across the apical membrane in the duodenum and the formate ion efflux at the apical brush border of cells in the proximal tubules of kidney. Plays a role in sperm capacitation by increasing intracellular pH. {ECO:0000269|PubMed:11459928, ECO:0000269|PubMed:11842009, ECO:0000269|PubMed:12119287, ECO:0000269|PubMed:12217875, ECO:0000269|PubMed:15203903, ECO:0000269|PubMed:16141316, ECO:0000269|PubMed:16532010, ECO:0000269|PubMed:16606687, ECO:0000269|PubMed:17053783, ECO:0000269|PubMed:17170027, ECO:0000269|PubMed:18046080, ECO:0000269|PubMed:18496516, ECO:0000269|PubMed:20150244, ECO:0000269|PubMed:20969732, ECO:0000269|PubMed:21976599, ECO:0000269|PubMed:22021714, ECO:0000269|PubMed:22895259}. PTM: Phosphorylated on serine residues by PKC; the phosphorylation disrupts interaction with carbonic anhydrase CA2 and reduces bicarbonate transport activity in a phorbol myristate acetate (PMA)-induced manner. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. Apical cell membrane; Multi-pass membrane protein. Cytoplasmic vesicle membrane; Multi-pass membrane protein. Microsome. Note=Colocalized with CA2 at the surface of the cell membrane in order to form a bicarbonate transport metabolon; colocalization is reduced in phorbol myristate acetate (PMA)-induced cells (By similarity). Localized in sperm membranes. Colocalizes with CFTR at the midpiece of sperm tail. Localizes to the apical membrane brush border of epithelial cells in the proximal tubules of kidney, of enterocytes of the small intestine and of gastric parietal cells in the stomach. May be translocated from the cytosolic surface of the cell membrane to the intracellular space by PKC in phorbol myristate acetate (PMA)-induced cells. {ECO:0000250}. SUBUNIT: Interacts (via C-terminal cytoplasmic domain) with CA2; the interaction stimulates chloride-bicarbonate exchange activity. Interacts with SLC9A3R1 (via the PDZ domains). Interacts with SLC9A3R2 (via the PDZ domains) (By similarity). Interacts (via C-terminal domain) with PDZK1 (via C-terminal PDZ domain); the interaction induces chloride and oxalate exchange transport. Interacts with CFTR, SLC26A3 and SLC9A3R1. Interacts with AHCYL1; the interaction increases SLC26A6 activity (PubMed:23542070). {ECO:0000250|UniProtKB:Q9BXS9, ECO:0000269|PubMed:16141316, ECO:0000269|PubMed:21976599, ECO:0000269|PubMed:23542070}. TISSUE SPECIFICITY: Expressed in kidney (at protein level). Highly expressed in stomach, kidney, heart and small intestine, low in the lung, liver, testis, brain, skeletal muscle and colon. Expressed in spermatogenic cells. Isoform 1 is expressed in intestine, kidney, testis, brain, muscle, heart, and stomach. {ECO:0000269|PubMed:11459928, ECO:0000269|PubMed:11842009, ECO:0000269|PubMed:12217875, ECO:0000269|PubMed:17170027, ECO:0000269|PubMed:21976599}. +Q91XD8 S2538_MOUSE Mitochondrial glycine transporter (Solute carrier family 25 member 38) 326 35,390 Chain (1); Repeat (3); Transmembrane (6) TRANSMEM 51 76 Helical; Name=1. {ECO:0000255|HAMAP-Rule:MF_03064}.; TRANSMEM 109 135 Helical; Name=2. {ECO:0000255|HAMAP-Rule:MF_03064}.; TRANSMEM 147 172 Helical; Name=3. {ECO:0000255|HAMAP-Rule:MF_03064}.; TRANSMEM 200 223 Helical; Name=4. {ECO:0000255|HAMAP-Rule:MF_03064}.; TRANSMEM 241 267 Helical; Name=5. {ECO:0000255|HAMAP-Rule:MF_03064}.; TRANSMEM 296 314 Helical; Name=6. {ECO:0000255|HAMAP-Rule:MF_03064}. FUNCTION: Mitochondrial glycine transporter that imports glycine into the mitochondrial matrix. Plays an important role in providing glycine for the first enzymatic step in heme biosynthesis, the condensation of glycine with succinyl-CoA to produce 5-aminolevulinate (ALA) in the mitochondrial matrix. Required during erythropoiesis. {ECO:0000255|HAMAP-Rule:MF_03064}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03064}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03064}. +Q5EBI0 S2610_MOUSE Solute carrier family 26 member 10 492 52,857 Chain (1); Transmembrane (10) TRANSMEM 101 121 Helical. {ECO:0000255}.; TRANSMEM 124 144 Helical. {ECO:0000255}.; TRANSMEM 149 165 Helical. {ECO:0000255}.; TRANSMEM 190 210 Helical. {ECO:0000255}.; TRANSMEM 226 246 Helical. {ECO:0000255}.; TRANSMEM 267 287 Helical. {ECO:0000255}.; TRANSMEM 300 320 Helical. {ECO:0000255}.; TRANSMEM 353 373 Helical. {ECO:0000255}.; TRANSMEM 398 418 Helical. {ECO:0000255}.; TRANSMEM 426 446 Helical. {ECO:0000255}. FUNCTION: Chloride/bicarbonate exchanger. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8R1T4 S35A3_MOUSE UDP-N-acetylglucosamine transporter (Golgi UDP-GlcNAc transporter) (Solute carrier family 35 member A3) 326 35,976 Chain (1); Sequence conflict (1); Transmembrane (8) TRANSMEM 4 24 Helical. {ECO:0000255}.; TRANSMEM 38 58 Helical. {ECO:0000255}.; TRANSMEM 136 156 Helical. {ECO:0000255}.; TRANSMEM 174 194 Helical. {ECO:0000255}.; TRANSMEM 212 232 Helical. {ECO:0000255}.; TRANSMEM 243 263 Helical. {ECO:0000255}.; TRANSMEM 269 289 Helical. {ECO:0000255}.; TRANSMEM 293 313 Helical. {ECO:0000255}. FUNCTION: Uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) transporter in the Golgi apparatus. May supply UDP-GlcNAc as substrate for Golgi-resident glycosyltransferases that generate branching of diantennary oligosaccharides (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with SLC35A2. {ECO:0000250}. +Q69Z37 SAM9L_MOUSE Sterile alpha motif domain-containing protein 9-like (SAM domain-containing protein 9-like) 1561 180,203 Chain (1); Domain (1); Erroneous initiation (1) FUNCTION: May be involved in endosome fusion. Mediates down-regulation of growth factor signaling via internalization of growth factor receptors. {ECO:0000269|PubMed:24029230}. SUBCELLULAR LOCATION: Early endosome {ECO:0000269|PubMed:24029230}. SUBUNIT: Interacts with EEA1. {ECO:0000250|UniProtKB:Q8IVG5}. +Q3V1H9 SAMD5_MOUSE Sterile alpha motif domain-containing protein 5 (SAM domain-containing protein 5) 173 19,221 Chain (1); Compositional bias (1); Domain (1); Frameshift (1); Helix (6); Mutagenesis (3); Sequence conflict (2) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28388653}. SUBUNIT: Interacts promiscuously (via SAM domain) with EPHA5, EPHA6, EPHA7, EPHA8, EPHB1, EPHB2, EPHB3 and EPHB4 (via SAM domain) (in vitro). {ECO:0000269|PubMed:29749928}. TISSUE SPECIFICITY: Detected in kidney glomeruli, and in peribiliary gland (PBG) cells at the hepatic hilum (at protein level). Detected in liver, kidney and small intestine. {ECO:0000269|PubMed:28388653}. +O70306 TBX15_MOUSE T-box transcription factor TBX15 (T-box protein 15) (MmTBx8) (T-box transcription factor TBX14) (T-box protein 14) 602 65,802 Chain (1); DNA binding (1); Modified residue (1); Sequence conflict (2) FUNCTION: Probable transcriptional regulator involved in the development of the skeleton of the limb, vertebral column and head. Acts by controlling the number of mesenchymal precursor cells and chondrocytes. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00201}. SUBUNIT: Can form a heterodimer with TBX18. {ECO:0000269|PubMed:17584735}. +Q1RNF8 SAM11_MOUSE Sterile alpha motif domain-containing protein 11 (SAM domain-containing protein 11) (Major retinal SAM domain-containing protein) (Mr-s) 542 57,784 Chain (1); Domain (1); Modified residue (2); Sequence conflict (1) FUNCTION: May play a role in photoreceptor development. {ECO:0000269|PubMed:16539743}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16539743}. SUBUNIT: Homodimer. TISSUE SPECIFICITY: Predominantly expressed in retinal photoreceptors and pineal gland. {ECO:0000269|PubMed:16539743}. +P70323 TBX1_MOUSE T-box transcription factor TBX1 (T-box protein 1) (Testis-specific T-box protein) 479 51,668 Alternative sequence (1); Chain (1); Compositional bias (3); DNA binding (1); Sequence conflict (9) FUNCTION: Probable transcriptional regulator involved in developmental processes. Is required for normal development of the pharyngeal arch arteries. {ECO:0000269|PubMed:11412027}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00201}. SUBUNIT: Interacts with DSCR6. {ECO:0000269|PubMed:21177346}. TISSUE SPECIFICITY: Expressed in skeletal muscle, lung and testis. {ECO:0000269|PubMed:11412027}. +P70122 SBDS_MOUSE Ribosome maturation protein SBDS (Protein 22A3) (Shwachman-Bodian-Diamond syndrome protein homolog) 250 28,781 Chain (1); Initiator methionine (1); Modified residue (2) FUNCTION: Required for the assembly of mature ribosomes and ribosome biogenesis. Together with EFL1, triggers the GTP-dependent release of EIF6 from 60S pre-ribosomes in the cytoplasm, thereby activating ribosomes for translation competence by allowing 80S ribosome assembly and facilitating EIF6 recycling to the nucleus, where it is required for 60S rRNA processing and nuclear export. Required for normal levels of protein synthesis. May play a role in cellular stress resistance. May play a role in cellular response to DNA damage. May play a role in cell proliferation (By similarity). {ECO:0000250, ECO:0000269|PubMed:19602484, ECO:0000269|PubMed:21536732}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus {ECO:0000250}. Nucleus, nucleoplasm. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Detected in the cytoplasm, but not in the nucleus (PubMed:21536732). Primarily detected in the cytoplasm, and at low levels in nucleus (PubMed:19602484). Detected in the nucleolus during G1 and G2 phase of the cell cycle, and diffusely distributed in the nucleus during S phase. Detected at the mitotic spindle. Colocalizes with the microtubule organizing center during interphase (By similarity). {ECO:0000250, ECO:0000269|PubMed:19602484, ECO:0000269|PubMed:21536732}. SUBUNIT: Associates with the 60S ribosomal subunit. Interacts with NPM1, RPA1 and PRKDC. May interact with NIP7. Found in a complex consisting of the 60S ribosomal subunit, SBDS and EFL1. {ECO:0000250|UniProtKB:Q9Y3A5}. TISSUE SPECIFICITY: Detected in adult liver, brain, heart, spleen, pancreas, kidney, lung and testis (at protein level). Detected in heart, brain, lung, liver, kidney and testis. {ECO:0000269|PubMed:16914746}. +Q9Z132 RSPO1_MOUSE R-spondin-1 (Cysteine-rich and single thrombospondin domain-containing protein 3) (Cristin-3) (mCristin-3) (Roof plate-specific spondin-1) 265 29,332 Chain (1); Disulfide bond (11); Domain (1); Glycosylation (1); Repeat (2); Sequence conflict (2); Signal peptide (1) FUNCTION: Activator of the canonical Wnt signaling pathway by acting as a ligand for LGR4-6 receptors. Upon binding to LGR4-6 (LGR4, LGR5 or LGR6), LGR4-6 associate with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increase expression of target genes (PubMed:21693646). Also regulates the canonical Wnt/beta-catenin-dependent pathway and non-canonical Wnt signaling by acting as an inhibitor of ZNRF3, an important regulator of the Wnt signaling pathway. Acts as a ligand for frizzled FZD8 and LRP6. May negatively regulate the TGF-beta pathway. Has a essential roles in ovary determination (By similarity). Regulates Wnt signaling by antagonizing DKK1/KREM1-mediated internalization of LRP6 through an interaction with KREM1 (By similarity). {ECO:0000250|UniProtKB:Q2MKA7, ECO:0000269|PubMed:21693646}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16543246}. Nucleus {ECO:0000269|PubMed:14732490}. Note=Seems to mainly localize to nucleoli. {ECO:0000269|PubMed:14732490}. SUBUNIT: Interacts with ZNRF3; promoting indirect interaction between ZNRF3 and LGR4 and membrane clearance of ZNRF3. Identified in a complex composed of RNF43, LGR5 and RSPO1 (By similarity). Interacts with the extracellular domain of FZD8 and LRP6. It however does not form a ternary complex with FZD8 and LRP6. Interacts with WNT1. Binds heparin. Interacts with LGR4, LGR5 and LGR6 (PubMed:16543246, PubMed:21693646). Interacts (via FU repeats) with KREM1 (By similarity). {ECO:0000250|UniProtKB:Q2MKA7, ECO:0000269|PubMed:16543246, ECO:0000269|PubMed:21693646}. DOMAIN: The FU repeats are required for activation and stabilization of beta-catenin. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the dorsal part of the neural tube on 10 and 12 dpc, especially in the boundary region between roof plate and neuroepithelium. This expression is enhanced in the rostral part. Also expressed in other tissues such as truncal region neighboring forelimbs and mesenchymal tissues around the nasal cavity. {ECO:0000269|PubMed:14732490}. +P14206 RSSA_MOUSE 40S ribosomal protein SA (37 kDa laminin receptor precursor) (37LRP) (37 kDa oncofetal antigen) (37/67 kDa laminin receptor) (LRP/LR) (67 kDa laminin receptor) (67LR) (Laminin receptor 1) (LamR) (Laminin-binding protein precursor p40) (LBP/p40) (OFA/iLRP) 295 32,838 Chain (1); Cross-link (1); Initiator methionine (1); Modified residue (5); Region (4); Repeat (5); Sequence conflict (5); Site (2) FUNCTION: Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. Also functions as a cell surface receptor for laminin. Plays a role in cell adhesion to the basement membrane and in the consequent activation of signaling transduction pathways. May play a role in cell fate determination and tissue morphogenesis. Also acts as a receptor for several other ligands, including the pathogenic prion protein, viruses, and bacteria. Acts as a PPP1R16B-dependent substrate of PPP1CA (By similarity). Enables malignant tumor cells to penetrate laminin tissue and vessel barriers. Activates precursor thymic anti-OFA/iLRP specific cytotoxic T-cell. May induce CD8 T-suppressor cells secreting IL-10. {ECO:0000255|HAMAP-Rule:MF_03016, ECO:0000269|PubMed:10697612, ECO:0000269|PubMed:1374897, ECO:0000269|PubMed:16453457, ECO:0000269|PubMed:6301485, ECO:0000269|PubMed:6302102}. PTM: Acylated. Acylation may be a prerequisite for conversion of the monomeric 37 kDa laminin receptor precursor (37LRP) to the mature dimeric 67 kDa laminin receptor (67LR), and may provide a mechanism for membrane association. {ECO:0000255|HAMAP-Rule:MF_03016}.; PTM: Cleaved by stromelysin-3 (ST3) at the cell surface. Cleavage by stromelysin-3 may be a mechanism to alter cell-extracellular matrix interactions. {ECO:0000255|HAMAP-Rule:MF_03016}. SUBCELLULAR LOCATION: Cell membrane. Cytoplasm. Nucleus. Note=67LR is found at the surface of the plasma membrane, with its C-terminal laminin-binding domain accessible to extracellular ligands. 37LRP is found at the cell surface, in the cytoplasm and in the nucleus. Colocalizes with PPP1R16B in the cell membrane (By similarity). 37LRP shuttles to the nucleus upon midkine (MDK) binding. {ECO:0000255|HAMAP-Rule:MF_03016}. SUBUNIT: Monomer (37LRP) and homodimer (67LR) (By similarity). Component of the small ribosomal subunit. Mature ribosomes consist of a small (40S) and a large (60S) subunit. The 40S subunit contains about 33 different proteins and 1 molecule of RNA (18S). The 60S subunit contains about 49 different proteins and 3 molecules of RNA (28S, 5.8S and 5S). Interacts with RPS21 (By similarity). Interacts with several laminins including at least LAMB1. Interacts with MDK. Interacts with PRNP. The mature dimeric form interacts with PPP1R16B (via its fourth ankyrin repeat). Interacts with PPP1CA only in the presence of PPP1R16B (By similarity). {ECO:0000255|HAMAP-Rule:MF_03016}. +Q9D125 RT25_MOUSE 28S ribosomal protein S25, mitochondrial (MRP-S25) (S25mt) 171 19,920 Chain (1); Sequence conflict (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P82669}. SUBUNIT: Component of the mitochondrial ribosome small subunit (28S) which comprises a 12S rRNA and about 30 distinct proteins. {ECO:0000250|UniProtKB:P82669}. +Q8R2L5 RT18C_MOUSE 28S ribosomal protein S18c, mitochondrial (MRP-S18-c) (Mrps18-c) (S18mt-c) (28S ribosomal protein S18-1, mitochondrial) (MRP-S18-1) 143 16,275 Chain (1); Sequence conflict (1); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P82917}. SUBUNIT: Component of the mitochondrial ribosome small subunit (28S) which comprises a 12S rRNA and about 30 distinct proteins. {ECO:0000250|UniProtKB:P82917}. +Q9CPX7 RT16_MOUSE 28S ribosomal protein S16, mitochondrial (MRP-S16) (S16mt) 135 15,192 Chain (1); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9Y3D3}. SUBUNIT: Component of the mitochondrial ribosome small subunit (28S) which comprises a 12S rRNA and about 30 distinct proteins. {ECO:0000250|UniProtKB:Q9Y3D3}. +Q9CQX8 RT36_MOUSE 28S ribosomal protein S36, mitochondrial (MRP-S36) (S36mt) 102 11,101 Chain (1); Initiator methionine (1); Modified residue (5) SUBCELLULAR LOCATION: Mitochondrion. SUBUNIT: Component of the mitochondrial ribosome small subunit (28S) which comprises a 12S rRNA and about 30 distinct proteins. +Q9D7H3 RTCA_MOUSE RNA 3'-terminal phosphate cyclase (RNA cyclase) (RNA-3'-phosphate cyclase) (EC 6.5.1.4) (RNA terminal phosphate cyclase domain-containing protein 1) 366 39,254 Active site (1); Binding site (1); Chain (1); Nucleotide binding (1); Sequence conflict (1) FUNCTION: Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. +Q924D0 RT4I1_MOUSE Reticulon-4-interacting protein 1, mitochondrial (NOGO-interacting mitochondrial protein) 396 43,371 Chain (1); Sequence conflict (5); Transit peptide (1) FUNCTION: Plays a role in the regulation of retinal ganglion cell (RGC) neurite outgrowth, and hence in the development of the inner retina and optic nerve (PubMed:26593267). Appears to be a potent inhibitor of regeneration following spinal cord injury (PubMed:12067236). {ECO:0000269|PubMed:12067236, ECO:0000269|PubMed:26593267}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:12067236}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q8WWV3}. Note=Colocalizes with the endoplasmic reticulum HSPA5 at spots corresponding to contacts with mitochondria. {ECO:0000250|UniProtKB:Q8WWV3}. SUBUNIT: Interacts with RTN4, UQCRC1 and UQCRC2. {ECO:0000269|PubMed:12067236}. TISSUE SPECIFICITY: Widely expressed in mitochondria-enriched tissues. Found in heart, kidney, liver, brain and spinal cord. {ECO:0000269|PubMed:12067236}. +Q6P1Y1 RTL3_MOUSE Retrotransposon Gag-like protein 3 (Zinc finger CCHC domain-containing protein 5) 553 61,382 Chain (1); Coiled coil (1); Zinc finger (1) FUNCTION: May function as a transcriptional regulator (Probable). Plays a role in postnatal myogenesis, may be involved in the regulation of satellite cells self-renewal (PubMed:27446912). {ECO:0000269|PubMed:27446912, ECO:0000305|PubMed:27446912}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:27446912}. TISSUE SPECIFICITY: Expressed in embryonic myogenic progenitor cells, not expressed in adult and aged satellite cells. {ECO:0000269|PubMed:27446912}. +Q9CQI7 RU2B_MOUSE U2 small nuclear ribonucleoprotein B'' (U2 snRNP B'') 225 25,323 Chain (1); Cross-link (1); Domain (2); Modified residue (2); Sequence conflict (1) FUNCTION: Involved in pre-mRNA splicing as component of the spliceosome. Associated with sn-RNP U2, where it contributes to the binding of stem loop IV of U2 snRNA. {ECO:0000250|UniProtKB:P08579}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P08579}. SUBUNIT: Identified in the spliceosome B complex. Identified in the spliceosome C complex. Present in a spliceosome complex assembled in vitro, and composed of SNRPB2, HPRP8BP and CRNKL1. Contributes to the binding of stem loop IV of U2 snRNA with SNRPP1. {ECO:0000250|UniProtKB:P08579}. +Q80ZI2 RTP2_MOUSE Receptor-transporting protein 2 223 25,900 Chain (1); Topological domain (2); Transmembrane (1) TRANSMEM 194 216 Helical. {ECO:0000255}. TOPO_DOM 1 193 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 217 223 Extracellular. {ECO:0000255}. FUNCTION: Specifically promotes functional cell surface expression of olfactory receptors, but not of other GPCRs. {ECO:0000269|PubMed:15550249}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15550249}; Single-pass type III membrane protein {ECO:0000269|PubMed:15550249}. Note=Effective cell surface expression depends upon interaction with olfactory receptors. SUBUNIT: Interacts with olfactory receptors. {ECO:0000269|PubMed:15550249}. TISSUE SPECIFICITY: Predominantly expressed in olfactory and vomeronasal organs, in mature olfactory sensory neurons. {ECO:0000269|PubMed:15550249}. +A2AQ19 RTF1_MOUSE RNA polymerase-associated protein RTF1 homolog 715 80,797 Chain (1); Coiled coil (1); Compositional bias (4); Domain (1); Erroneous initiation (2); Modified residue (5) FUNCTION: Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and is involved in transcriptional elongation, acting both indepentently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1. PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B ubiquitination is proposed to be coupled to transcription. PAF1C is involved in mRNA 3' end formation probably through association with cleavage and poly(A) factors. Binds single-stranded DNA (By similarity). Required for maximal induction of heat-shock genes. Required for the trimethylation of histone H3 'Lys-4' (H3K4me3) on genes involved in stem cell pluripotency; this function is synergistic with CXXC1 indicative for an involvement of a SET1 complex. {ECO:0000250, ECO:0000269|PubMed:19345177}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}. SUBUNIT: Component of the PAF1 complex, which consists of CDC73, PAF1, LEO1, CTR9, RTF1 and WDR61. The PAF1 complex interacts with PHF5A (PubMed:27749823). {ECO:0000250|UniProtKB:Q92541, ECO:0000269|PubMed:27749823}. DOMAIN: The Plus3 domain mediates single-stranded DNA-binding. {ECO:0000250}. +Q99K95 RTF2_MOUSE Protein RTF2 homolog (Replication termination factor 2 domain-containing protein 1) 307 33,935 Chain (1); Modified residue (1) +Q9WTM5 RUVB2_MOUSE RuvB-like 2 (EC 3.6.4.12) (p47 protein) 463 51,113 Chain (1); Cross-link (3); Initiator methionine (1); Modified residue (2); Nucleotide binding (1) FUNCTION: Possesses single-stranded DNA-stimulated ATPase and ATP-dependent DNA helicase (5' to 3') activity; hexamerization is thought to be critical for ATP hydrolysis and adjacent subunits in the ring-like structure contribute to the ATPase activity. {ECO:0000250}.; FUNCTION: Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. The NuA4 complex ATPase and helicase activities seem to be, at least in part, contributed by the association of RUVBL1 and RUVBL2 with EP400. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AFZ from the nucleosome (By similarity). {ECO:0000250}.; FUNCTION: Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. {ECO:0000250}.; FUNCTION: Plays an essential role in oncogenic transformation by MYC and also modulates transcriptional activation by the LEF1/TCF1-CTNNB1 complex. May also inhibit the transcriptional activity of ATF2 (By similarity). {ECO:0000250}.; FUNCTION: Involved in the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway where it negatively regulates expression of ER stress response genes. {ECO:0000250|UniProtKB:Q9Y230}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Forms homohexameric rings (Probable). Can form a dodecamer with RUVBL1 made of two stacked hexameric rings; however, even though RUVBL1 and RUVBL2 are present in equimolar ratio, the oligomeric status of each hexamer is not known. Oligomerization may regulate binding to nucleic acids and conversely, binding to nucleic acids may affect the dodecameric assembly. Interacts with the transcriptional activation domain of MYC. Interacts With ATF2. Component of the RNA polymerase II holoenzyme complex. May also act to bridge the LEF1/TCF1-CTNNB1 complex and TBP. Component of the NuA4 histone acetyltransferase complex which contains the catalytic subunit KAT5/TIP60 and the subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6. The NuA4 complex interacts with MYC and the adenovirus E1A protein. RUVBL2 interacts with EP400. Component of a NuA4-related complex which contains EP400, TRRAP/PAF400, SRCAP, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, actin, ACTL6A/BAF53A, VPS72 and YEATS4/GAS41. Interacts with NPAT. Component of the chromatin-remodeling INO80 complex; specifically part of a complex module associated with the helicase ATP-binding and the helicase C-terminal domain of INO80. Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Interacts with IGHMBP2. Interacts with TELO2. Interacts with HINT1. Component of a SWR1-like complex. Component of the R2TP complex composed at least of PIHD1, RUVBL1, RUVBL2 and RPAP3. Interacts with ITFG1. Interacts with ZMYND10. Interacts with WAC; WAC positively regulates MTOR activity by promoting the assembly of the TTT complex composed of TELO2, TTI1 and TTI2 and the RUVBL complex composed of RUVBL1 and RUVBL2 into the TTT-RUVBL complex which leads to the dimerization of the mTORC1 complex and its subsequent activation. {ECO:0000250|UniProtKB:Q9Y230, ECO:0000305}. +P07091 S10A4_MOUSE Protein S100-A4 (Metastasin) (Metastatic cell protein) (PEL98) (Placental calcium-binding protein) (Protein 18A2) (Protein Mts1) (S100 calcium-binding protein A4) 101 11,721 Calcium binding (2); Chain (1); Domain (2); Initiator methionine (1); Modified residue (2); Sequence conflict (1) SUBUNIT: Homodimer. Interacts with PPFIBP1 in a calcium-dependent mode (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Specifically expressed in different metastatic cells. +P28704 RXRB_MOUSE Retinoic acid receptor RXR-beta (MHC class I regulatory element-binding protein H-2RIIBP) (Nuclear receptor subfamily 2 group B member 2) (Retinoid X receptor beta) 520 55,866 Alternative sequence (1); Chain (1); DNA binding (1); Domain (1); Modified residue (1); Region (2); Sequence conflict (3); Zinc finger (2) FUNCTION: Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RAR/RXR heterodimers bind to the retinoic acid response elements (RARE). {ECO:0000269|PubMed:1310259, ECO:0000269|PubMed:1312497}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Homodimer (in vitro). Heterodimer with other retinoic acid receptor family members. Binds DNA preferentially as a RAR/RXR heterodimer. Interacts with NR1H3 (By similarity). Interacts with AKAP13 (PubMed:20139090). {ECO:0000250|UniProtKB:P28702, ECO:0000269|PubMed:20139090}. DOMAIN: Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain. {ECO:0000305|PubMed:1312497}. TISSUE SPECIFICITY: In all tissues tested, including brain, thymus, spleen and liver. {ECO:0000269|PubMed:1312497, ECO:0000269|PubMed:8194750}. +P31725 S10A9_MOUSE Protein S100-A9 (Calgranulin-B) (Leukocyte L1 complex heavy chain) (Migration inhibitory factor-related protein 14) (MRP-14) (p14) (S100 calcium-binding protein A9) 113 13,049 Calcium binding (2); Chain (1); Domain (2); Initiator methionine (1); Mass spectrometry (1); Metal binding (4); Modified residue (2) FUNCTION: S100A9 is a calcium- and zinc-binding protein which plays a prominent role in the regulation of inflammatory processes and immune response. It can induce neutrophil chemotaxis, adhesion, can increase the bactericidal activity of neutrophils by promoting phagocytosis via activation of SYK, PI3K/AKT, and ERK1/2 and can induce degranulation of neutrophils by a MAPK-dependent mechanism. Predominantly found as calprotectin (S100A8/A9) which has a wide plethora of intra- and extracellular functions. The intracellular functions include: facilitating leukocyte arachidonic acid trafficking and metabolism, modulation of the tubulin-dependent cytoskeleton during migration of phagocytes and activation of the neutrophilic NADPH-oxidase. Activates NADPH-oxidase by facilitating the enzyme complex assembly at the cell membrane, transferring arachidonic acid, an essential cofactor, to the enzyme complex and S100A8 contributes to the enzyme assembly by directly binding to NCF2/P67PHOX. The extracellular functions involve proinflammatory, antimicrobial, oxidant-scavenging and apoptosis-inducing activities. Its proinflammatory activity includes recruitment of leukocytes, promotion of cytokine and chemokine production, and regulation of leukocyte adhesion and migration. Acts as an alarmin or a danger associated molecular pattern (DAMP) molecule and stimulates innate immune cells via binding to pattern recognition receptors such as Toll-like receptor 4 (TLR4) and receptor for advanced glycation endproducts (AGER). Binding to TLR4 and AGER activates the MAP-kinase and NF-kappa-B signaling pathways resulting in the amplification of the proinflammatory cascade. Has antimicrobial activity towards bacteria and fungi and exerts its antimicrobial activity probably via chelation of Zn(2+) which is essential for microbial growth. Can induce cell death via autophagy and apoptosis and this occurs through the cross-talk of mitochondria and lysosomes via reactive oxygen species (ROS) and the process involves BNIP3. Can regulate neutrophil number and apoptosis by an anti-apoptotic effect; regulates cell survival via ITGAM/ITGB and TLR4 and a signaling mechanism involving MEK-ERK. Its role as an oxidant scavenger has a protective role in preventing exaggerated tissue damage by scavenging oxidants. The iNOS-S100A8/A9 transnitrosylase complex is proposed to direct selective inflammatory stimulus-dependent S-nitrosylation of multiple targets such as GAPDH, NXA5, EZR, MSN and VIM by recognizing a [IL]-x-C-x-x-[DE] motif (By similarity). {ECO:0000250|UniProtKB:P06702, ECO:0000269|PubMed:15331440, ECO:0000269|PubMed:17767165, ECO:0000269|PubMed:18403730, ECO:0000269|PubMed:19402754, ECO:0000269|PubMed:21382888, ECO:0000269|PubMed:22804476}. PTM: Phosphorylated. Phosphorylation inhibits activation of tubulin polymerization (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Cytoplasm. Cytoplasm, cytoskeleton. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Predominantly localized in the cytoplasm. Upon elevation of the intracellular calcium level, translocated from the cytoplasm to the cytoskeleton and the cell membrane. Upon neutrophil activation or endothelial adhesion of monocytes, is secreted via a microtubule-mediated, alternative pathway. SUBUNIT: Homodimer. Preferentially exists as a heterodimer or heterotetramer with S100A8 known as calprotectin (S100A8/A9). S100A9 interacts with beta-APP40 (amyloid-beta protein 40) peptide of APP (By similarity). S100A9 interacts with AGER and the heterodimeric complex formed by TLR4 and LY96 in the presence of calcium and/or zinc ions. S100A9 binds quinoline-3-carboxamides in the presence of calcium and/or zinc ions. S100A9 interacts with ATP2A2. Calprotectin (S100A8/9) interacts with NCF2/P67PHOX, RAC1, RAC2, CYBA and CYBB (By similarity). Heterotetrameric calprotectin (S100A8/A9) interacts with ANXA6 and associates with tubulin filaments in activated monocytes (By similarity). Calprotectin (S100A8/9) interacts with CEACAM3 and tubulin filaments in a calcium-dependent manner. Calprotectin (S100A8/9) interacts with NOS2 to form the iNOS-S100A8/A9 transnitrosylase complex (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P06702, ECO:0000269|PubMed:15331440, ECO:0000269|PubMed:17767165, ECO:0000269|PubMed:18403730, ECO:0000269|PubMed:19402754}. +Q6R6I7 RXFP1_MOUSE Relaxin receptor 1 (Leucine-rich repeat-containing G-protein coupled receptor 7) (Relaxin family peptide receptor 1) 758 86,957 Chain (1); Disulfide bond (4); Domain (1); Glycosylation (6); Metal binding (6); Repeat (10); Topological domain (8); Transmembrane (7) TRANSMEM 410 430 Helical; Name=1. {ECO:0000255}.; TRANSMEM 444 464 Helical; Name=2. {ECO:0000255}.; TRANSMEM 487 507 Helical; Name=3. {ECO:0000255}.; TRANSMEM 528 548 Helical; Name=4. {ECO:0000255}.; TRANSMEM 578 598 Helical; Name=5. {ECO:0000255}.; TRANSMEM 630 650 Helical; Name=6. {ECO:0000255}.; TRANSMEM 652 672 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 409 Extracellular. {ECO:0000255}.; TOPO_DOM 431 443 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 465 486 Extracellular. {ECO:0000255}.; TOPO_DOM 508 527 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 549 577 Extracellular. {ECO:0000255}.; TOPO_DOM 599 629 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 651 651 Extracellular. {ECO:0000255}.; TOPO_DOM 673 758 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for relaxins. The activity of this receptor is mediated by G proteins leading to stimulation of adenylate cyclase and an increase of cAMP. Binding of the ligand may also activate a tyrosine kinase pathway that inhibits the activity of a phosphodiesterase that degrades cAMP. {ECO:0000269|PubMed:15566402}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBUNIT: Interacts with C1QTNF8. {ECO:0000250|UniProtKB:Q9HBX9}. +P50543 S10AB_MOUSE Protein S100-A11 (Calgizzarin) (Endothelial monocyte-activating polypeptide) (EMAP) (Protein S100-C) (S100 calcium-binding protein A11) 98 11,083 Calcium binding (2); Chain (1); Disulfide bond (1); Domain (2); Modified residue (2) FUNCTION: Facilitates the differentiation and the cornification of keratinocytes. {ECO:0000250}. PTM: Phosphorylation at Thr-5 significantly suppresses homodimerization and promotes association with NCL/nucleolin which induces nuclear translocation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}. SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}. +O88909 S22A8_MOUSE Solute carrier family 22 member 8 (Organic anion transporter 3) (mOat3) (Reduced in osteosclerosis transporter) 537 59,246 Chain (1); Glycosylation (1); Modified residue (1); Sequence conflict (2); Topological domain (12); Transmembrane (11) TRANSMEM 12 32 Helical. {ECO:0000255}.; TRANSMEM 124 144 Helical. {ECO:0000255}.; TRANSMEM 151 171 Helical. {ECO:0000255}.; TRANSMEM 177 197 Helical. {ECO:0000255}.; TRANSMEM 213 233 Helical. {ECO:0000255}.; TRANSMEM 237 257 Helical. {ECO:0000255}.; TRANSMEM 328 348 Helical. {ECO:0000255}.; TRANSMEM 355 375 Helical. {ECO:0000255}.; TRANSMEM 384 404 Helical. {ECO:0000255}.; TRANSMEM 412 432 Helical. {ECO:0000255}.; TRANSMEM 472 492 Helical. {ECO:0000255}. TOPO_DOM 1 11 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 33 123 Extracellular. {ECO:0000255}.; TOPO_DOM 145 150 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 172 176 Extracellular. {ECO:0000255}.; TOPO_DOM 198 212 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 234 236 Extracellular. {ECO:0000255}.; TOPO_DOM 258 327 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 349 354 Extracellular. {ECO:0000255}.; TOPO_DOM 376 383 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 405 411 Extracellular. {ECO:0000255}.; TOPO_DOM 433 471 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 493 537 Extracellular. {ECO:0000255}. FUNCTION: Plays an important role in the excretion/detoxification of endogenous and exogenous organic anions, especially from the brain and kidney. Mediates the uptake of p-amino-hippurate (PAH) and estron sulfate (ES). Also mediates uptake of several organic compounds such as prostaglandin E(2), prostaglandin F(2-alpha), allopurinol, 6-mercaptopurine (6-MP), 5-fluorouracil (5-FU), and L-carnitine. {ECO:0000269|PubMed:12011098, ECO:0000269|PubMed:15075193, ECO:0000269|PubMed:15100168}. SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=Localizes on the brush border membrane of the choroid epithelial cells. Localizes to the basolateral membrane of the proximal tubular cells. Localizes on the abluminal and possibly, luminal membrane of the brain capillary endothelial cells (BCEC) (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in kidney. Expressed in developing bone. Weakly expressed in brain and eye. {ECO:0000269|PubMed:10087192, ECO:0000269|PubMed:15100168}. +Q8C811 S35E2_MOUSE Solute carrier family 35 member E2A 405 44,279 Chain (1); Transmembrane (10) TRANSMEM 76 96 Helical. {ECO:0000255}.; TRANSMEM 106 126 Helical. {ECO:0000255}.; TRANSMEM 142 162 Helical. {ECO:0000255}.; TRANSMEM 167 187 Helical. {ECO:0000255}.; TRANSMEM 195 215 Helical. {ECO:0000255}.; TRANSMEM 219 241 Helical. {ECO:0000255}.; TRANSMEM 264 284 Helical. {ECO:0000255}.; TRANSMEM 296 316 Helical. {ECO:0000255}.; TRANSMEM 326 346 Helical. {ECO:0000255}.; TRANSMEM 347 367 Helical. {ECO:0000255}. FUNCTION: Putative transporter. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q60714 S27A1_MOUSE Long-chain fatty acid transport protein 1 (FATP-1) (Fatty acid transport protein 1) (EC 6.2.1.-) (Fatty acid transport protein) (Solute carrier family 27 member 1) 646 71,276 Chain (1); Mutagenesis (3); Nucleotide binding (1); Region (1); Topological domain (2); Transmembrane (1) TRANSMEM 14 34 Helical. {ECO:0000255}. TOPO_DOM 1 13 Extracellular. {ECO:0000305|PubMed:11470793}.; TOPO_DOM 35 646 Cytoplasmic. {ECO:0000305|PubMed:11470793}. FUNCTION: Mediates the ATP-dependent import of long-chain fatty acids (LCFA) into the cell by mediating their translocation at the plasma membrane (PubMed:7954810, PubMed:9786857, PubMed:9671728, PubMed:10471110, PubMed:12235169, PubMed:11970897, PubMed:15699031, PubMed:28178239). Has also an acyl-CoA ligase activity for long-chain and very-long-chain fatty acids (PubMed:10593920, PubMed:12235169, PubMed:12937175). May act directly as a bona fide transporter, or alternatively, in a cytoplasmic or membrane-associated multimeric protein complex to trap and draw fatty acids towards accumulation (PubMed:14991074, PubMed:15897321). Plays a pivotal role in regulating available LCFA substrates from exogenous sources in tissues undergoing high levels of beta-oxidation or triglyceride synthesis (PubMed:12235169). May be involved in regulation of cholesterol metabolism (PubMed:12235169). {ECO:0000269|PubMed:10471110, ECO:0000269|PubMed:10593920, ECO:0000269|PubMed:11970897, ECO:0000269|PubMed:12235169, ECO:0000269|PubMed:12937175, ECO:0000269|PubMed:14991074, ECO:0000269|PubMed:15699031, ECO:0000269|PubMed:15897321, ECO:0000269|PubMed:28178239, ECO:0000269|PubMed:7954810, ECO:0000269|PubMed:9671728, ECO:0000269|PubMed:9786857}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10471110, ECO:0000269|PubMed:10593920, ECO:0000269|PubMed:11470793, ECO:0000269|PubMed:11970897, ECO:0000269|PubMed:28178239, ECO:0000269|PubMed:7954810, ECO:0000269|PubMed:9786857}; Single-pass membrane protein {ECO:0000269|PubMed:11470793, ECO:0000269|PubMed:7954810}. Endomembrane system {ECO:0000269|PubMed:10593920, ECO:0000269|PubMed:15897321}; Single-pass membrane protein {ECO:0000269|PubMed:11470793, ECO:0000269|PubMed:7954810}. Cytoplasm {ECO:0000269|PubMed:10593920, ECO:0000269|PubMed:15897321}. Note=Plasma membrane and intracellular membranes, at least in adipocytes (PubMed:10593920, PubMed:11970897, PubMed:28178239). In adipocytes, but not myocytes, insulin via the mTORC1 signaling pathway induces a rapid translocation of SLC27A1 from intracellular compartments to the plasma membrane, paralleled by increased LCFA uptake (PubMed:11970897, PubMed:28178239). Insulin-dependent translocation from the cytoplasm to the cell membrane is regulated by EPRS (PubMed:11970897, PubMed:28178239). Predominantly cytoplasmic in myocytes (PubMed:15897321). {ECO:0000269|PubMed:10593920, ECO:0000269|PubMed:11970897, ECO:0000269|PubMed:15897321, ECO:0000269|PubMed:28178239}. SUBUNIT: Self-associates. May function as a homodimer (PubMed:12533547). Interacts with EPRS; mediates the translocation of SLC27A1 from the cytoplasm to the plasma membrane thereby increasing the uptake of long-chain fatty acids (PubMed:28178239). {ECO:0000269|PubMed:12533547, ECO:0000269|PubMed:28178239}. TISSUE SPECIFICITY: Highest expression in skeletal muscle, heart and fat. Lower levels in brain, kidney, lung, liver and testis. No expression in spleen or intestine. {ECO:0000269|PubMed:7954810, ECO:0000269|PubMed:9671728}. +Q9D321 S35A4_MOUSE Probable UDP-sugar transporter protein SLC35A4 (Solute carrier family 35 member A4) 324 34,695 Chain (1); Sequence conflict (4); Transmembrane (9) TRANSMEM 19 39 Helical. {ECO:0000255}.; TRANSMEM 53 73 Helical. {ECO:0000255}.; TRANSMEM 86 106 Helical. {ECO:0000255}.; TRANSMEM 143 163 Helical. {ECO:0000255}.; TRANSMEM 181 201 Helical. {ECO:0000255}.; TRANSMEM 215 235 Helical. {ECO:0000255}.; TRANSMEM 249 271 Helical. {ECO:0000255}.; TRANSMEM 280 300 Helical. {ECO:0000255}.; TRANSMEM 302 322 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q91ZR7}; Multi-pass membrane protein {ECO:0000255}. +Q9D856 S39A5_MOUSE Zinc transporter ZIP5 (Solute carrier family 39 member 5) (Zrt- and Irt-like protein 5) (ZIP-5) 535 56,275 Chain (1); Compositional bias (1); Glycosylation (2); Modified residue (1); Sequence conflict (2); Signal peptide (1); Topological domain (7); Transmembrane (6) TRANSMEM 211 231 Helical. {ECO:0000255}.; TRANSMEM 243 263 Helical. {ECO:0000255}.; TRANSMEM 286 306 Helical. {ECO:0000255}.; TRANSMEM 440 460 Helical. {ECO:0000255}.; TRANSMEM 466 486 Helical. {ECO:0000255}.; TRANSMEM 504 524 Helical. {ECO:0000255}. TOPO_DOM 20 210 Extracellular. {ECO:0000269|PubMed:15322118}.; TOPO_DOM 232 242 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 264 285 Extracellular. {ECO:0000255}.; TOPO_DOM 307 439 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 461 465 Extracellular. {ECO:0000255}.; TOPO_DOM 487 503 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 525 535 Extracellular. {ECO:0000269|PubMed:15322118}. FUNCTION: May play a role in polarized cells by carrying out serosal-to-mucosal zinc transport. Plays a role in eye development. Could regulate the BMP/TGF-beta (bone morphogenetic protein/transforming growth factor-beta) signaling pathway and modulates extracellular matrix (ECM) proteins of the sclera (PubMed:24891338). Seems to play a central role in controlling organismal zinc status. {ECO:0000250|UniProtKB:Q6ZMH5, ECO:0000269|PubMed:15322118}. PTM: Glycosylated. {ECO:0000269|PubMed:15322118}. SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000269|PubMed:15322118}; Multi-pass membrane protein {ECO:0000269|PubMed:15322118}. TISSUE SPECIFICITY: Expressed in all stages of eye development and primarily in the sclera and several layers of the retina, including the inner segment, outer plexiform layer and ganglion cell layer. {ECO:0000269|PubMed:24891338}. +Q8C145 S39A6_MOUSE Zinc transporter ZIP6 (Endoplasmic reticulum membrane-linked protein) (Ermelin) (Solute carrier family 39 member 6) (Zrt- and Irt-like protein 6) (ZIP-6) 765 86,380 Chain (1); Coiled coil (1); Compositional bias (4); Erroneous initiation (1); Frameshift (1); Glycosylation (5); Modified residue (2); Sequence conflict (2); Signal peptide (1); Topological domain (7); Transmembrane (6) TRANSMEM 336 356 Helical; Name=1. {ECO:0000255}.; TRANSMEM 366 386 Helical; Name=2. {ECO:0000255}.; TRANSMEM 434 454 Helical; Name=3. {ECO:0000255}.; TRANSMEM 668 688 Helical; Name=4. {ECO:0000255}.; TRANSMEM 697 717 Helical; Name=5. {ECO:0000255}.; TRANSMEM 735 755 Helical; Name=6. {ECO:0000255}. TOPO_DOM 21 335 Extracellular. {ECO:0000255}.; TOPO_DOM 357 365 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 387 433 Extracellular. {ECO:0000255}.; TOPO_DOM 455 667 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 689 696 Extracellular. {ECO:0000255}.; TOPO_DOM 718 734 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 756 765 Extracellular. {ECO:0000255}. FUNCTION: May act as a zinc-influx transporter. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Found in the endoplasmic reticulum when overexpressed. {ECO:0000269|PubMed:11891044}. TISSUE SPECIFICITY: Highly expressed in the brain and testis. In the brain strongly expressed in the CA1 and CA3 regions, Purkinje cells in cerebellum and dentate gyrus in hippocampus. In testis found in spermatids or mature sperms in the central areas of seminiferous tubules. {ECO:0000269|PubMed:11891044}. +D3YVE8 S35G2_MOUSE Solute carrier family 35 member G2 (Transmembrane protein 22) 412 46,395 Chain (1); Domain (2); Modified residue (1); Transmembrane (10) TRANSMEM 105 125 Helical. {ECO:0000255}.; TRANSMEM 131 151 Helical. {ECO:0000255}.; TRANSMEM 169 189 Helical. {ECO:0000255}.; TRANSMEM 194 214 Helical. {ECO:0000255}.; TRANSMEM 218 238 Helical. {ECO:0000255}.; TRANSMEM 255 275 Helical. {ECO:0000255}.; TRANSMEM 286 306 Helical. {ECO:0000255}.; TRANSMEM 319 339 Helical. {ECO:0000255}.; TRANSMEM 346 366 Helical. {ECO:0000255}.; TRANSMEM 368 388 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +O88627 S28A2_MOUSE Sodium/nucleoside cotransporter 2 (Concentrative nucleoside transporter 2) (CNT 2) (Na(+)/nucleoside cotransporter 2) (Sodium-coupled nucleoside transporter 2) (Sodium/purine nucleoside cotransporter) (SPNT) (Solute carrier family 28 member 2) 660 72,916 Chain (1); Modified residue (1); Sequence conflict (7); Transmembrane (14) TRANSMEM 82 102 Helical. {ECO:0000255}.; TRANSMEM 106 125 Helical. {ECO:0000255}.; TRANSMEM 150 168 Helical. {ECO:0000255}.; TRANSMEM 174 194 Helical. {ECO:0000255}.; TRANSMEM 202 222 Helical. {ECO:0000255}.; TRANSMEM 235 255 Helical. {ECO:0000255}.; TRANSMEM 262 282 Helical. {ECO:0000255}.; TRANSMEM 297 316 Helical. {ECO:0000255}.; TRANSMEM 338 357 Helical. {ECO:0000255}.; TRANSMEM 364 383 Helical. {ECO:0000255}.; TRANSMEM 425 445 Helical. {ECO:0000255}.; TRANSMEM 456 476 Helical. {ECO:0000255}.; TRANSMEM 531 551 Helical. {ECO:0000255}.; TRANSMEM 569 589 Helical. {ECO:0000255}. FUNCTION: Sodium-dependent and purine-selective. Exhibits the transport characteristics of the nucleoside transport system cif or N1 subtype (N1/cif) (selective for purine nucleosides and uridine) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. +E9Q8Q8 SACA6_MOUSE Sperm acrosome membrane-associated protein 6 339 38,503 Alternative sequence (5); Chain (1); Compositional bias (1); Disulfide bond (1); Domain (1); Glycosylation (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 311 331 Helical. {ECO:0000255, ECO:0000305}. TOPO_DOM 42 310 Extracellular. {ECO:0000305}.; TOPO_DOM 332 339 Cytoplasmic. {ECO:0000305}. FUNCTION: Sperm protein potentially involved sperm-egg fusion. {ECO:0000269|PubMed:24275887}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Highly expressed in testis. Predominantly expressed in testicular germ cells during spermiogenesis. Most abundant in round spermatids and detected at lower levels in elongating spermatids. {ECO:0000269|PubMed:24275887}. +Q8CE47 S49A3_MOUSE Solute carrier family 49 member A3 (Major facilitator superfamily domain-containing protein 7A) 516 54,646 Chain (1); Sequence conflict (1); Transmembrane (12) TRANSMEM 34 54 Helical. {ECO:0000255}.; TRANSMEM 74 94 Helical. {ECO:0000255}.; TRANSMEM 104 124 Helical. {ECO:0000255}.; TRANSMEM 139 159 Helical. {ECO:0000255}.; TRANSMEM 170 190 Helical. {ECO:0000255}.; TRANSMEM 199 219 Helical. {ECO:0000255}.; TRANSMEM 253 273 Helical. {ECO:0000255}.; TRANSMEM 289 309 Helical. {ECO:0000255}.; TRANSMEM 321 341 Helical. {ECO:0000255}.; TRANSMEM 344 364 Helical. {ECO:0000255}.; TRANSMEM 382 402 Helical. {ECO:0000255}.; TRANSMEM 425 445 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9JLR1 S61A2_MOUSE Protein transport protein Sec61 subunit alpha isoform 2 (Sec61 alpha-2) 476 52,248 Chain (1); Topological domain (11); Transmembrane (10) TRANSMEM 34 53 Helical. {ECO:0000255}.; TRANSMEM 77 96 Helical. {ECO:0000255}.; TRANSMEM 118 138 Helical. {ECO:0000255}.; TRANSMEM 145 165 Helical. {ECO:0000255}.; TRANSMEM 173 193 Helical. {ECO:0000255}.; TRANSMEM 241 261 Helical. {ECO:0000255}.; TRANSMEM 289 309 Helical. {ECO:0000255}.; TRANSMEM 355 375 Helical. {ECO:0000255}.; TRANSMEM 421 441 Helical. {ECO:0000255}.; TRANSMEM 446 462 Helical. {ECO:0000255}. TOPO_DOM 1 33 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 54 76 Lumenal. {ECO:0000255}.; TOPO_DOM 97 117 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 139 144 Lumenal. {ECO:0000255}.; TOPO_DOM 166 172 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 194 240 Lumenal. {ECO:0000255}.; TOPO_DOM 262 288 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 310 354 Lumenal. {ECO:0000255}.; TOPO_DOM 376 420 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 442 445 Lumenal. {ECO:0000255}.; TOPO_DOM 463 476 Cytoplasmic. {ECO:0000255}. FUNCTION: Appears to play a crucial role in the insertion of secretory and membrane polypeptides into the ER. It is required for assembly of membrane and secretory proteins. Found to be tightly associated with membrane-bound ribosomes, either directly or through adaptor proteins (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Heterotrimeric complex composed of SEC61-alpha, SEC61-beta and SEC61-gamma. {ECO:0000250}. +Q9D0K0 TBCD7_MOUSE TBC1 domain family member 7 293 33,826 Alternative sequence (1); Chain (1); Domain (1) FUNCTION: Component of the TSC-TBC complex, that contains TBC1D7 in addition to the TSC1-TSC2 complex and consists of the functional complex possessing GTPase-activating protein (GAP) activity toward RHEB in response to alterations in specific cellular growth conditions. The small GTPase RHEB is a direct activator of the protein kinase activity of mTORC1 and the TSC-TBC complex acts as a negative regulator of mTORC1 signaling cascade by acting as a GAP for RHEB. Participates in the proper sensing of growth factors and glucose, but not amino acids, by mTORC1. It is unclear whether TBC1D7 acts as a GTPase-activating protein and additional studies are required to answer this question. {ECO:0000269|PubMed:22795129}. SUBCELLULAR LOCATION: Cytoplasmic vesicle {ECO:0000250}. Note=Localizes in the cytoplasmic vesicles of the endomembrane in association with TSC1-TSC2 complex. {ECO:0000250}. SUBUNIT: Component of the TSC-TBC complex (also named Rhebulator complex), composed of the TSC1-TSC2 heterodimer and TBC1D7. Interacts with TSC1 (via C-terminal half of the coiled-coil domain). {ECO:0000269|PubMed:22795129}. +Q9D2C2 SAAL1_MOUSE Protein SAAL1 (Synoviocyte proliferation-associated in collagen-induced arthritis protein 1) (SPACIA1) 474 52,769 Alternative sequence (1); Chain (1); Modified residue (3) FUNCTION: Plays a role in promoting the proliferation of synovial fibroblasts in response to proinflammatory stimuli. {ECO:0000250|UniProtKB:Q96ER3}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96ER3}. TISSUE SPECIFICITY: Expressed in the synovial tissue of knee joints. {ECO:0000269|PubMed:22127701}. +Q9EP69 SAC1_MOUSE Phosphatidylinositide phosphatase SAC1 (EC 3.1.3.-) (Suppressor of actin mutations 1-like protein) 587 66,944 Chain (1); Domain (1); Erroneous initiation (1); Modified residue (1); Transmembrane (3) TRANSMEM 56 76 Helical. {ECO:0000255}.; TRANSMEM 521 541 Helical. {ECO:0000255}.; TRANSMEM 549 569 Helical. {ECO:0000255}. FUNCTION: Phosphoinositide phosphatase that hydrolyzes phosphatidylinositol 3-phosphate (PtdIns(3)P) and phosphatidylinositol 4-phosphate (PtdIns(4)P) (By similarity). Has low activity towards PtdIns(3,5)P2 (By similarity). {ECO:0000250|UniProtKB:Q9ES21, ECO:0000250|UniProtKB:Q9NTJ5}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9ES21}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9ES21}. TISSUE SPECIFICITY: Detected in brain, lung, liver and kidney, and at lower levels in spleen and skeletal muscle. {ECO:0000269|PubMed:11352561}. +D3YXK2 SAFB1_MOUSE Scaffold attachment factor B1 (SAF-B1) 937 105,104 Chain (1); Coiled coil (1); Compositional bias (4); Cross-link (13); Domain (2); Initiator methionine (1); Modified residue (21); Motif (1); Region (2) FUNCTION: Binds to scaffold/matrix attachment region (S/MAR) DNA and forms a molecular assembly point to allow the formation of a 'transcriptosomal' complex (consisting of SR proteins and RNA polymerase II) coupling transcription and RNA processing. Can function as an estrogen receptor corepressor and can also bind to the HSP27 promoter and decrease its transcription. Can inhibit cell proliferation. When associated with RBMX, binds to and stimulates transcription from the SREBF1 promoter. {ECO:0000269|PubMed:19403048}. PTM: Sumoylated by PIAS1 with SUMO1 and SUMO2/3, desumoylated by SENP1. Sumoylation is required for transcriptional repressor activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Monomer. Can form homodimers. Interacts with KHDRBS3, POLR2A, SAFB2 or SFRS1, SFRS9 and TRA2B/SFRS10 (By similarity). Interacts with RBMX. Interacts with SRPK1 and inhibits its activity (By similarity). Interacts with FUS (By similarity). {ECO:0000250}. +Q9D687 S6A19_MOUSE Sodium-dependent neutral amino acid transporter B(0)AT1 (Solute carrier family 6 member 19) (System B(0) neutral amino acid transporter AT1) 634 71,367 Chain (1); Glycosylation (6); Modified residue (2); Topological domain (13); Transmembrane (12) TRANSMEM 42 62 Helical; Name=1. {ECO:0000255}.; TRANSMEM 68 88 Helical; Name=2. {ECO:0000255}.; TRANSMEM 120 140 Helical; Name=3. {ECO:0000255}.; TRANSMEM 193 213 Helical; Name=4. {ECO:0000255}.; TRANSMEM 222 242 Helical; Name=5. {ECO:0000255}.; TRANSMEM 269 289 Helical; Name=6. {ECO:0000255}.; TRANSMEM 305 325 Helical; Name=7. {ECO:0000255}.; TRANSMEM 414 434 Helical; Name=8. {ECO:0000255}.; TRANSMEM 457 477 Helical; Name=9. {ECO:0000255}.; TRANSMEM 488 508 Helical; Name=10. {ECO:0000255}.; TRANSMEM 532 552 Helical; Name=11. {ECO:0000255}.; TRANSMEM 582 602 Helical; Name=12. {ECO:0000255}. TOPO_DOM 1 41 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 63 67 Extracellular. {ECO:0000255}.; TOPO_DOM 89 119 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 141 192 Extracellular. {ECO:0000255}.; TOPO_DOM 214 221 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 243 268 Extracellular. {ECO:0000255}.; TOPO_DOM 290 304 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 326 413 Extracellular. {ECO:0000255}.; TOPO_DOM 435 456 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 478 487 Extracellular. {ECO:0000255}.; TOPO_DOM 509 531 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 553 581 Extracellular. {ECO:0000255}.; TOPO_DOM 603 634 Cytoplasmic. {ECO:0000255}. FUNCTION: Transporter that mediates resorption of neutral amino acids across the apical membrane of renal and intestinal epithelial cells (PubMed:17167413, PubMed:26240152, PubMed:19185582, PubMed:15044460). Required CLTRN in kidney or ACE2 in intestine for cell surface expression and amino acid transporter activity (PubMed:19185582, PubMed:17167413). This uptake is sodium-dependent and chloride-independent (PubMed:15044460, PubMed:18424768, PubMed:19185582, PubMed:21636576, PubMed:26240152). {ECO:0000269|PubMed:15044460, ECO:0000269|PubMed:17167413, ECO:0000269|PubMed:18424768, ECO:0000269|PubMed:19185582, ECO:0000269|PubMed:21636576, ECO:0000269|PubMed:26240152}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18424768}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes in small intestine brush border membranes (at protein level). {ECO:0000269|PubMed:19185582}. SUBUNIT: Interacts in a tissue-specific manner with ACE2 in small intestine and with CLTRN in the kidney. Interacts with CLTRN; this interaction is required for trafficking of SLC6A19 to the plasma membrane and for its catalytic activation in kidneys (PubMed:17167413). Interacts with ACE2; this interaction is required for trafficking of SLC6A19 to the plasma membrane and for its catalytic activation in intestine (PubMed:19185582). {ECO:0000269|PubMed:17167413, ECO:0000269|PubMed:19185582}. TISSUE SPECIFICITY: Predominantly expressed in kidney and small intestine (PubMed:15044460, PubMed:19185582). Expression not observed in other organs, such as lung, skeletal muscle, brain, liver and pancreas. In kidney, expression is localized in the renal cortex but not in the medulla. Substantial amounts of expression in the proximal tubules. The distal nephron segments and the glomeruli are consistently negative. In the small intestine, expression is exclusively localized in villus enterocytes. High resolution of the hybridization-positive villi reveals a gradient of expression with the highest levels in apical cells. Not detected in crypt cells or in any other cell types of the small intestine. {ECO:0000269|PubMed:15044460, ECO:0000269|PubMed:19185582}. +P46097 SYT2_MOUSE Synaptotagmin-2 (Inositol polyphosphate-binding protein) (IP4-binding protein) (IP4BP) (Synaptotagmin II) (SytII) 422 47,263 Chain (1); Domain (2); Glycosylation (1); Helix (1); Metal binding (14); Modified residue (3); Mutagenesis (9); Region (1); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 61 87 Helical. {ECO:0000255}. TOPO_DOM 1 60 Vesicular. {ECO:0000255}.; TOPO_DOM 88 422 Cytoplasmic. {ECO:0000255}. FUNCTION: Exhibits calcium-dependent phospholipid and inositol polyphosphate binding properties (PubMed:7961887). May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse (PubMed:7961887). Plays a role in dendrite formation by melanocytes (By similarity). {ECO:0000250|UniProtKB:Q8N9I0, ECO:0000269|PubMed:7961887}.; FUNCTION: (Microbial infection) Receptor for C.botulinum neurotoxin type B (BoNT/B, botB); interaction is improved in the presence of gangliosides (PubMed:14504267). The toxin binds via the vesicular domain (residues 47-60) (PubMed:14504267, PubMed:17167418, PubMed:23807078). {ECO:0000269|PubMed:14504267, ECO:0000269|PubMed:17167418, ECO:0000269|PubMed:23807078}.; FUNCTION: (Microbial infection) Receptor for C.botulinum neurotoxin type G (BoNT/G, botG); gangliosides are not required for (or only very slightly improve) binding to a membrane-anchored receptor fragment (PubMed:20219474). The toxin binds via the vesicular domain (residues 47-55) (PubMed:20219474). {ECO:0000269|PubMed:20219474}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Single-pass membrane protein. Cytoplasmic vesicle, secretory vesicle, chromaffin granule membrane; Single-pass membrane protein. Cytoplasm. Note=Synaptic vesicles and chromaffin granules. SUBUNIT: Homotetramer (Probable). Interacts with SCAMP5 (By similarity). Interacts with STON2 (By similarity). Interacts with PRRT2 (PubMed:27052163). {ECO:0000250|UniProtKB:Q8N9I0, ECO:0000269|PubMed:27052163, ECO:0000305}.; SUBUNIT: (Microbial infection) Interacts with C.botulinum neurotoxin type B (BoNT/B, botB). {ECO:0000269|PubMed:14504267, ECO:0000269|PubMed:17167418, ECO:0000269|PubMed:23807078}.; SUBUNIT: (Microbial infection) Interacts with C.botulinum neurotoxin type G (BoNT/G, botG). {ECO:0000269|PubMed:20219474}. DOMAIN: The first C2 domain mediates Ca(2+)-dependent phospholipid binding (PubMed:7961887).; DOMAIN: The second C2 domain mediates interaction with Stonin 2. The second C2 domain mediates phospholipid and inositol polyphosphate binding in a calcium-independent manner (PubMed:7961887). {ECO:0000269|PubMed:7961887}.; DOMAIN: (Microbial infection) Binding to BoNT/B induces formation of an alpha-helix in the membrane-proximal extracytoplasmic domain (PubMed:17167418, PubMed:23807078). {ECO:0000305|PubMed:17167418, ECO:0000305|PubMed:23807078}. +Q80T23 SYTL5_MOUSE Synaptotagmin-like protein 5 753 84,089 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (3); Modified residue (1); Zinc finger (1) FUNCTION: May act as Rab effector protein and play a role in vesicle trafficking. Binds phospholipids (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. SUBUNIT: Binds RAB27A that has been activated by GTP-binding. +Q9R0N4 SYT10_MOUSE Synaptotagmin-10 (Synaptotagmin X) (SytX) 523 59,019 Chain (1); Domain (2); Metal binding (12); Modified residue (1); Mutagenesis (6); Region (1); Topological domain (2); Transmembrane (1) TRANSMEM 56 76 Helical. {ECO:0000255}. TOPO_DOM 1 55 Vesicular. {ECO:0000255}.; TOPO_DOM 77 523 Cytoplasmic. {ECO:0000255}. FUNCTION: Ca(2+) sensor specifically required for the Ca(2+)-dependent exocytosis of secretory vesicles containing IGF1 in neurons of the olfactory bulb (PubMed:21496647). Exocytosis of IGF1 is required for sensory perception of smell (PubMed:21496647). Not involved in Ca(2+)-dependent synaptic vesicle exocytosis (PubMed:21496647). Acts through Ca(2+) and phospholipid binding to the C2 domain: Ca(2+) induces binding of the C2-domains to phospholipid membranes and to assembled SNARE-complexes; both actions contribute to triggering exocytosis (By similarity). {ECO:0000250|UniProtKB:O08625, ECO:0000269|PubMed:21496647}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000269|PubMed:21496647, ECO:0000269|PubMed:23345244}; Single-pass membrane protein {ECO:0000255}. Note=Localizes to neuronal vesicles containing IGF1 that are not enriched at synapses (PubMed:21496647, PubMed:23345244). Does not colocalize with synaptic vesicles or with the Golgi apparatus (PubMed:21496647, PubMed:23345244). {ECO:0000269|PubMed:21496647, ECO:0000269|PubMed:23345244}. SUBUNIT: Homodimer; disulfide-linked via the cysteine motif (PubMed:10531343). Can also form heterodimers with SYT3, SYT6, SYT7 and SYT9 (PubMed:10531343, PubMed:10531344, PubMed:10871604). {ECO:0000269|PubMed:10531343, ECO:0000269|PubMed:10531344, ECO:0000269|PubMed:10871604}. DOMAIN: The cysteine motif mediates homo- or heterodimer formation via formation of disulfide bonds. {ECO:0000250|UniProtKB:O35681}.; DOMAIN: The first C2 domain mediates Ca(2+)-dependent phospholipid binding. {ECO:0000250|UniProtKB:O08625}. TISSUE SPECIFICITY: Highly expressed in the olfactory bulb. {ECO:0000305|PubMed:21496647}. +Q3U2A8 SYVM_MOUSE Valine--tRNA ligase, mitochondrial (EC 6.1.1.9) (Valyl-tRNA synthetase) (ValRS) 1060 118,461 Binding site (1); Chain (1); Erroneous initiation (2); Modified residue (1); Motif (2); Sequence caution (1); Sequence conflict (29); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}. +Q9Z0F7 SYUG_MOUSE Gamma-synuclein (Persyn) 123 13,160 Chain (1); Modified residue (3); Region (1); Repeat (4) FUNCTION: Plays a role in neurofilament network integrity. May be involved in modulating axonal architecture during development and in the adult. In vitro, increases the susceptibility of neurofilament-H to calcium-dependent proteases. May also function in modulating the keratin network in skin. Activates the MAPK and Elk-1 signal transduction pathway (By similarity). {ECO:0000250}. PTM: Phosphorylated. Phosphorylation by GRK5 appears to occur on residues distinct from the residue phosphorylated by other kinases (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Associated with centrosomes in several interphase cells. In mitotic cells, localized to the poles of the spindle (By similarity). {ECO:0000250}. SUBUNIT: May be a centrosome-associated protein. Interacts with MYOC; affects its secretion and its aggregation. {ECO:0000269|PubMed:16392033}. TISSUE SPECIFICITY: Highly expressed in brain, particularly in the substantia nigra. Also expressed in the corpus callosum, heart, skeletal muscle, ovary, testis, colon and spleen. Weak expression in pancreas, kidney and lung. Expressed predominantly in the cell bodies and axons of primary sensory neurons, sympathetic neurons and motoneurons. +Q8BYL4 SYYM_MOUSE Tyrosine--tRNA ligase, mitochondrial (EC 6.1.1.1) (Tyrosyl-tRNA synthetase) (TyrRS) 472 52,597 Binding site (9); Chain (1); Modified residue (2); Motif (2); Transit peptide (1) FUNCTION: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr). {ECO:0000250|UniProtKB:Q9Y2Z4}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:Q9Y2Z4}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9Y2Z4}. +Q80VP8 T106C_MOUSE Transmembrane protein 106C 260 28,952 Chain (1); Glycosylation (1); Initiator methionine (1); Lipidation (1); Transmembrane (2) TRANSMEM 85 105 Helical. {ECO:0000255}.; TRANSMEM 196 216 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Membrane {ECO:0000250|UniProtKB:Q9BVX2}; Lipid-anchor {ECO:0000250|UniProtKB:Q9BVX2}. +Q8CEF9 T132C_MOUSE Transmembrane protein 132C 1099 121,378 Chain (1); Erroneous initiation (2); Glycosylation (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 916 936 Helical. {ECO:0000255}. TOPO_DOM 32 915 Extracellular. {ECO:0000255}.; TOPO_DOM 937 1099 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +A2A9C3 SZT2_MOUSE KICSTOR complex protein SZT2 (Seizure threshold 2 protein) (Transcript increased in glutamate resistance) (TIGR) 3431 377,627 Alternative sequence (1); Chain (1); Compositional bias (1); Frameshift (2); Modified residue (4); Region (1); Sequence caution (1); Sequence conflict (6) FUNCTION: As part of the KICSTOR complex functions in the amino acid-sensing branch of the TORC1 signaling pathway. Recruits, in an amino acid-independent manner, the GATOR1 complex to the lysosomal membranes and allows its interaction with GATOR2 and the RAG GTPases. Functions upstream of the RAG GTPases and is required to negatively regulate mTORC1 signaling in absence of amino acids (By similarity). In absence of the KICSTOR complex mTORC1 is constitutively localized to the lysosome and activated. The KICSTOR complex is also probably involved in the regulation of mTORC1 by glucose (PubMed:28199306, PubMed:28199315). May play a role in the cellular response to oxidative stress (PubMed:20045724). {ECO:0000250|UniProtKB:Q5T011, ECO:0000269|PubMed:20045724, ECO:0000269|PubMed:28199306, ECO:0000269|PubMed:28199315}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q5T011}. Peroxisome {ECO:0000269|PubMed:20045724}. Note=Localization to lysosomes is amino acid-independent. {ECO:0000250|UniProtKB:Q5T011}. SUBUNIT: Part of the KICSTOR complex composed of KPTN, ITFG2, C12orf66 and SZT2. SZT2 probably serves as a link between the other three proteins in the KICSTOR complex and may mediate the direct interaction with the GATOR complex via GATOR1. The KICSTOR complex interacts directly with the GATOR1 complex and most probably indirectly with the GATOR2 complexe in an amino acid-independent manner. {ECO:0000250|UniProtKB:Q5T011}. TISSUE SPECIFICITY: Mostly expressed in brain, spinal cord and lung. {ECO:0000269|PubMed:19624305, ECO:0000269|PubMed:20045724}. +Q91WN2 T150A_MOUSE Transmembrane protein 150A (Transmembrane protein 150) 271 29,066 Chain (1); Glycosylation (2); Topological domain (7); Transmembrane (6) TRANSMEM 3 23 Helical. {ECO:0000255}.; TRANSMEM 76 96 Helical. {ECO:0000255}.; TRANSMEM 109 129 Helical. {ECO:0000255}.; TRANSMEM 141 161 Helical. {ECO:0000255}.; TRANSMEM 179 199 Helical. {ECO:0000255}.; TRANSMEM 212 232 Helical. {ECO:0000255}. TOPO_DOM 1 2 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 24 75 Extracellular. {ECO:0000305}.; TOPO_DOM 97 108 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 130 140 Extracellular. {ECO:0000305}.; TOPO_DOM 162 178 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 200 211 Extracellular. {ECO:0000305}.; TOPO_DOM 233 271 Cytoplasmic. {ECO:0000250|UniProtKB:Q86TG1}. FUNCTION: Regulates localization of phosphatidylinositol 4-kinase (PI4K) to the plasma membrane, possibly by reducing the association of TTC7 (TTC7A or TTC7B) with the PI4K complex. Acts as a regulator of phosphatidylinositol 4-phosphate (PtdIns(4)P) synthesis (By similarity). May also play a role in fasting-induced catabolism (By similarity). {ECO:0000250|UniProtKB:Q86TG1, ECO:0000250|UniProtKB:Q9QZE9}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q86TG1}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q86TG1}. Note=Localizes mainly at the plasma membrane; only a minor fraction localizes on intracellular structures. {ECO:0000250|UniProtKB:Q86TG1}. SUBUNIT: Interacts (via C-terminal cytoplasmic tail) with PI4KA. {ECO:0000250|UniProtKB:Q86TG1}. +Q8C8S3 T150C_MOUSE Transmembrane protein 150C (Tentonin 3) 249 27,759 Alternative sequence (1); Chain (1); Erroneous initiation (1); Mutagenesis (5); Topological domain (7); Transmembrane (6) TRANSMEM 10 30 Helical. {ECO:0000255}.; TRANSMEM 65 85 Helical. {ECO:0000255}.; TRANSMEM 98 118 Helical. {ECO:0000255}.; TRANSMEM 131 151 Helical. {ECO:0000255}.; TRANSMEM 169 189 Helical. {ECO:0000255}.; TRANSMEM 193 213 Helical. {ECO:0000255}. TOPO_DOM 1 9 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 31 64 Extracellular. {ECO:0000305}.; TOPO_DOM 86 97 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 119 130 Extracellular. {ECO:0000305}.; TOPO_DOM 152 168 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 190 192 Extracellular. {ECO:0000305}.; TOPO_DOM 214 249 Cytoplasmic. {ECO:0000250|UniProtKB:Q86TG1}. FUNCTION: Component of a mechanosensitive cation channel. Confers mechanically activated (MA) currents with slow inactivation kinetics. May contribute to proprioception (PubMed:27321926). {ECO:0000269|PubMed:27321926}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27321926}; Multi-pass membrane protein {ECO:0000250|UniProtKB:B9EJG8}. Lysosome membrane {ECO:0000250|UniProtKB:B9EJG8}; Multi-pass membrane protein {ECO:0000250|UniProtKB:B9EJG8}. Note=Localizes at the plasma membrane. A portion co-localizes with LAMP1 lysosomal marker. {ECO:0000250|UniProtKB:B9EJG8}. TISSUE SPECIFICITY: High expression in the epididymis, pancreas, dorsal-root ganglion, eye, brain, and spinal cord. Expressed in muscle spindle afferents (at protein level)(PubMed:27321926). {ECO:0000269|PubMed:27321926}. +B9EJI9 T229A_MOUSE Transmembrane protein 229A 371 41,526 Chain (1); Transmembrane (6) TRANSMEM 51 71 Helical. {ECO:0000255}.; TRANSMEM 117 137 Helical. {ECO:0000255}.; TRANSMEM 235 255 Helical. {ECO:0000255}.; TRANSMEM 269 289 Helical. {ECO:0000255}.; TRANSMEM 301 321 Helical. {ECO:0000255}.; TRANSMEM 334 354 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8BFQ2 T229B_MOUSE Transmembrane protein 229B 167 19,561 Chain (1); Frameshift (1); Sequence conflict (2); Topological domain (5); Transmembrane (4) TRANSMEM 15 35 Helical. {ECO:0000255}.; TRANSMEM 41 61 Helical. {ECO:0000255}.; TRANSMEM 74 94 Helical. {ECO:0000255}.; TRANSMEM 110 130 Helical. {ECO:0000255}. TOPO_DOM 1 14 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 36 40 Extracellular. {ECO:0000255}.; TOPO_DOM 62 73 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 95 109 Extracellular. {ECO:0000255}.; TOPO_DOM 131 167 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8C0G2 T3JAM_MOUSE TRAF3-interacting JNK-activating modulator (TRAF3-interacting protein 3) 513 58,564 Chain (1); Coiled coil (1); Compositional bias (2); Frameshift (1); Sequence caution (1); Sequence conflict (3); Topological domain (2); Transmembrane (1) TRANSMEM 486 506 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 1 485 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 507 513 Extracellular. {ECO:0000255}. FUNCTION: May function as an adapter molecule that regulates TRAF3-mediated JNK activation. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}. SUBUNIT: Binds to the isoleucine zipper of TRAF3 via its coiled-coil domain. TISSUE SPECIFICITY: Expressed in bone marrow, spleen and thymus. Not detected in heart, kidney and liver. {ECO:0000269|PubMed:14572659}. +Q9QXE4 T53I1_MOUSE Tumor protein p53-inducible nuclear protein 1 (Stress-induced protein) (Thymus-expressed acidic protein) (TEAP) (p53-dependent damage-inducible nuclear protein 1) (p53DINP1) 239 26,935 Alternative sequence (1); Chain (1); Compositional bias (1); Motif (1) FUNCTION: Antiproliferative and proapoptotic protein involved in cell stress response which acts as a dual regulator of transcription and autophagy. Acts as a positive regulator of autophagy. In response to cellular stress or activation of autophagy, relocates to autophagosomes where it interacts with autophagosome-associated proteins GABARAP, GABARAPL1/L2, MAP1LC3A/B/C and regulates autophagy. Acts as an antioxidant and plays a major role in p53/TP53-driven oxidative stress response. Possesses both a p53/TP53-independent intracellular reactive oxygen species (ROS) regulatory function and a p53/TP53-dependent transcription regulatory function. Positively regulates p53/TP53 and p73/TP73 and stimulates their capacity to induce apoptosis and regulate cell cycle. In response to double-strand DNA breaks, promotes p53/TP53 phosphorylation on 'Ser-46' and subsequent apoptosis. Acts as a tumor suppressor by inducing cell death by an autophagy and caspase-dependent mechanism. Can reduce cell migration by regulating the expression of SPARC. {ECO:0000269|PubMed:11557757, ECO:0000269|PubMed:16044147, ECO:0000269|PubMed:19118006, ECO:0000269|PubMed:21339733}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Nucleus {ECO:0000269|PubMed:11557757}. Nucleus, PML body {ECO:0000250}. Cytoplasmic vesicle, autophagosome {ECO:0000250}. Note=Shuttles between the nucleus and the cytoplasm, depending on cellular stress conditions, and re-localizes to autophagosomes on autophagy activation. {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. SUBUNIT: Interacts with p53/TP53 and HIPK2. Interacts with PRKCG, GABARAP, GABARAPL1, GABARAPL2, MAP1LC3A, MAP1LC3B and MAP1LC3C. {ECO:0000250}. DOMAIN: The LC3 interacting region (LIR) motif mediates interaction with GABARAP, GABARAPL1, GABARAPL2, MAP1LC3A, MAP1LC3B and MAP1LC3C. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed with highest levels in the thymus. {ECO:0000269|PubMed:10630289, ECO:0000269|PubMed:11557757}. +Q5QD16 TAAR3_MOUSE Trace amine-associated receptor 3 (TaR-3) (Trace amine receptor 3) (mTaar3) 343 38,745 Chain (1); Disulfide bond (1); Glycosylation (2); Topological domain (8); Transmembrane (7) TRANSMEM 36 56 Helical; Name=1. {ECO:0000255}.; TRANSMEM 69 89 Helical; Name=2. {ECO:0000255}.; TRANSMEM 151 168 Helical; Name=3. {ECO:0000255}.; TRANSMEM 173 193 Helical; Name=4. {ECO:0000255}.; TRANSMEM 199 223 Helical; Name=5. {ECO:0000255}.; TRANSMEM 258 278 Helical; Name=6. {ECO:0000255}.; TRANSMEM 288 308 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 35 Extracellular. {ECO:0000255}.; TOPO_DOM 57 68 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 90 150 Extracellular. {ECO:0000255}.; TOPO_DOM 169 172 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 194 198 Extracellular. {ECO:0000255}.; TOPO_DOM 224 257 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 279 287 Extracellular. {ECO:0000255}.; TOPO_DOM 309 343 Cytoplasmic. {ECO:0000255}. FUNCTION: Olfactory receptor activated by several primary trace amines, including isoamylamine. Activated by isoamylamine and cyclohexylamine, but not to the corresponding alcohols, isoamylalcohol and cyclohexanol. This receptor is probably mediated by the G(s)-class of G-proteins which activate adenylate cyclase. {ECO:0000269|PubMed:16878137}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Specifically expressed in neurons of the olfactory epithelium. {ECO:0000269|PubMed:16878137}. +Q5QD15 TAAR4_MOUSE Trace amine-associated receptor 4 (TaR-4) (Trace amine receptor 4) (mTaar4) (2-phenylethylamine receptor) 347 38,904 Chain (1); Disulfide bond (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 38 58 Helical; Name=1. {ECO:0000255}.; TRANSMEM 70 90 Helical; Name=2. {ECO:0000255}.; TRANSMEM 111 129 Helical; Name=3. {ECO:0000255}.; TRANSMEM 150 170 Helical; Name=4. {ECO:0000255}.; TRANSMEM 198 218 Helical; Name=5. {ECO:0000255}.; TRANSMEM 261 281 Helical; Name=6. {ECO:0000255}.; TRANSMEM 297 317 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 37 Extracellular. {ECO:0000255}.; TOPO_DOM 59 69 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 91 110 Extracellular. {ECO:0000255}.; TOPO_DOM 130 149 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 171 197 Extracellular. {ECO:0000255}.; TOPO_DOM 219 260 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 282 296 Extracellular. {ECO:0000255}.; TOPO_DOM 318 347 Cytoplasmic. {ECO:0000255}. FUNCTION: Olfactory receptor specific for 2-phenylethylamine, a trace amine present at high concentration in the urine of carnivore species, playing a key role in fear and avoidance responses. 2-phenylethylamine acts as a kairomone in the chemical detection of carnivore odor and triggers fear in mice. This receptor is probably mediated by the G(s)-class of G-proteins which activate adenylate cyclase. {ECO:0000269|PubMed:16878137, ECO:0000269|PubMed:21690383, ECO:0000269|PubMed:23624375}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Specifically expressed in neurons of the olfactory epithelium, to discrete glomeruli predominantly localized to a confined bulb region. Present in the dorsal area of the main olfactory epithelium. {ECO:0000269|PubMed:16878137, ECO:0000269|PubMed:22837392}. +Q5QD14 TAAR5_MOUSE Trace amine-associated receptor 5 (TaR-5) (Trace amine receptor 5) (mTaar5) (Trimethylamine receptor) 337 38,220 Chain (1); Disulfide bond (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 39 59 Helical; Name=1. {ECO:0000255}.; TRANSMEM 71 91 Helical; Name=2. {ECO:0000255}.; TRANSMEM 110 130 Helical; Name=3. {ECO:0000255}.; TRANSMEM 155 175 Helical; Name=4. {ECO:0000255}.; TRANSMEM 205 225 Helical; Name=5. {ECO:0000255}.; TRANSMEM 254 274 Helical; Name=6. {ECO:0000255}.; TRANSMEM 285 307 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 38 Extracellular. {ECO:0000255}.; TOPO_DOM 60 70 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 92 109 Extracellular. {ECO:0000255}.; TOPO_DOM 131 154 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 176 204 Extracellular. {ECO:0000255}.; TOPO_DOM 226 253 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 275 284 Extracellular. {ECO:0000255}.; TOPO_DOM 308 337 Cytoplasmic. {ECO:0000255}. FUNCTION: Olfactory receptor specific for trimethylamine, a trace amine enriched in the urine of male mice, playing a role in social behavior. Trimethylamine is present at high concentration in the urine of male mice after puberty and acts as an attractant. This receptor is probably mediated by the G(s)-class of G-proteins which activate adenylate cyclase. {ECO:0000269|PubMed:16878137, ECO:0000269|PubMed:23177478}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Specifically expressed in neurons of the olfactory epithelium, to discrete glomeruli predominantly localized to a confined bulb region. Present in the dorsal area of the main olfactory epithelium. {ECO:0000269|PubMed:16878137, ECO:0000269|PubMed:22837392}. +Q5QD13 TAAR6_MOUSE Trace amine-associated receptor 6 (TaR-6) (Trace amine receptor 6) (mTaar6) 345 38,279 Chain (1); Disulfide bond (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 33 53 Helical; Name=1. {ECO:0000255}.; TRANSMEM 69 89 Helical; Name=2. {ECO:0000255}.; TRANSMEM 108 128 Helical; Name=3. {ECO:0000255}.; TRANSMEM 148 168 Helical; Name=4. {ECO:0000255}.; TRANSMEM 203 223 Helical; Name=5. {ECO:0000255}.; TRANSMEM 260 276 Helical; Name=6. {ECO:0000255}.; TRANSMEM 283 302 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 32 Extracellular. {ECO:0000255}.; TOPO_DOM 54 68 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 90 107 Extracellular. {ECO:0000255}.; TOPO_DOM 129 147 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 169 202 Extracellular. {ECO:0000255}.; TOPO_DOM 224 259 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 277 282 Extracellular. {ECO:0000255}.; TOPO_DOM 303 345 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan olfactory receptor specific for trace amines. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Specifically expressed in neurons of the olfactory epithelium, to discrete glomeruli predominantly localized to a confined bulb region. Present in a ventral area of the main olfactory epithelium. {ECO:0000269|PubMed:16878137, ECO:0000269|PubMed:22837392}. +Q8C1W1 VASH1_MOUSE Tubulinyl-Tyr carboxypeptidase 1 (EC 3.4.17.17) (Tyrosine carboxypeptidase 1) (TTCP 1) (Vasohibin-1) 375 41,875 Active site (3); Chain (1); Frameshift (1); Mutagenesis (1); Region (1); Sequence conflict (2); Site (2) FUNCTION: Tyrosine carboxypeptidase that removes the C-terminal tyrosine residue of alpha-tubulin, thereby regulating microtubule dynamics and function (PubMed:29146868). Acts as an angiogenesis inhibitor: inhibits migration, proliferation and network formation by endothelial cells as well as angiogenesis (PubMed:19204325). This inhibitory effect is selective to endothelial cells as it does not affect the migration of smooth muscle cells or fibroblasts (By similarity). {ECO:0000250|UniProtKB:Q7L8A9, ECO:0000269|PubMed:19204325, ECO:0000269|PubMed:29146868}. PTM: Ubiquitinated in vitro. {ECO:0000250|UniProtKB:Q7L8A9}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q7L8A9}. Secreted {ECO:0000250|UniProtKB:Q7L8A9}. Note=Mainly localizes in the cytoplasm. Some fraction is secreted via a non-canonical secretion system; interaction with SVBP promotes secretion. {ECO:0000250|UniProtKB:Q7L8A9}. SUBUNIT: Interacts with SVBP; interaction enhances VASH1 tyrosine carboxypeptidase activity. {ECO:0000269|PubMed:29146868}. TISSUE SPECIFICITY: Expressed at low level in proliferating endothelial cells at the sprouting front but highly expressed in nonproliferating endothelial cells in the termination zone. {ECO:0000269|PubMed:19204325}. +Q9D0D5 T2EA_MOUSE General transcription factor IIE subunit 1 (General transcription factor IIE 56 kDa subunit) (Transcription initiation factor IIE subunit alpha) (TFIIE-alpha) 440 49,593 Chain (1); Compositional bias (1); Domain (1); Initiator methionine (1); Modified residue (3); Zinc finger (1) FUNCTION: Recruits TFIIH to the initiation complex and stimulates the RNA polymerase II C-terminal domain kinase and DNA-dependent ATPase activities of TFIIH. Both TFIIH and TFIIE are required for promoter clearance by RNA polymerase. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P29083}. SUBUNIT: Tetramer of two alpha and two beta chains. Interacts with TAF6/TAFII80. Interacts with ATF7IP. Interacts with SND1. {ECO:0000250|UniProtKB:P29083}. +Q8CF89 TAB1_MOUSE TGF-beta-activated kinase 1 and MAP3K7-binding protein 1 (Mitogen-activated protein kinase kinase kinase 7-interacting protein 1) (TGF-beta-activated kinase 1-binding protein 1) (TAK1-binding protein 1) 502 54,616 Chain (1); Compositional bias (1); Domain (1); Modified residue (3); Sequence conflict (3); Site (1) FUNCTION: May be an important signaling intermediate between TGFB receptors and MAP3K7/TAK1. May play an important role in mammalian embryogenesis. PTM: Monoubiquitinated. {ECO:0000250}. SUBUNIT: Interacts with XIAP and BIRC7. Interacts with TRAF6 and MAP3K7; during IL-1 signaling. Identified in the TRIKA2 complex composed of MAP3K7, TAB1 and TAB2 (By similarity). {ECO:0000250}. +Q99K90 TAB2_MOUSE TGF-beta-activated kinase 1 and MAP3K7-binding protein 2 (Mitogen-activated protein kinase kinase kinase 7-interacting protein 2) (TAK1-binding protein 2) (TAB-2) (TGF-beta-activated kinase 1-binding protein 2) 693 76,442 Chain (1); Coiled coil (1); Domain (1); Frameshift (1); Modified residue (6); Mutagenesis (6); Region (1); Sequence conflict (3); Turn (2); Zinc finger (1) FUNCTION: Adapter linking MAP3K7/TAK1 and TRAF6. Promotes MAP3K7 activation in the IL1 signaling pathway. The binding of 'Lys-63'-linked polyubiquitin chains to TAB2 promotes autophosphorylation of MAP3K7 at 'Thr-187' (By similarity). Regulates the IL1-mediated translocation of NCOR1 out of the nucleus. Involved in heart development (By similarity). {ECO:0000250, ECO:0000269|PubMed:12150997, ECO:0000269|PubMed:19927120}. PTM: Ubiquitinated; following IL1 stimulation or TRAF6 overexpression. Ubiquitination involves RBCK1 leading to7 proteasomal degradation (By similarity). {ECO:0000250}.; PTM: Phosphorylated. {ECO:0000305|PubMed:12150997}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12150997}. Cytoplasm, cytosol {ECO:0000269|PubMed:12150997}. Note=Cytoplasmic when activated. Following IL1 stimulation, localized in the to cytosol. SUBUNIT: Interacts with MAP3K7 and TRAF6. Identified in the TRIKA2 complex composed of MAP3K7, TAB1 and TAB2. Binds 'Lys-63'-linked polyubiquitin chains. Interacts with NCOR1 and HDAC3 to form a ternary complex. Interacts (via C-terminal) with NUMBL (via PTB domain). Interacts (via the C-terminus) with WDR34 (via WD domains). Interacts with RBCK1 (By similarity). Interacts with TRIM5 (By similarity). {ECO:0000250}. DOMAIN: The RanBP2-type zinc finger (NZF) mediates binding to two consecutive 'Lys-63'-linked ubiquitins. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12150997}. +Q8R0A0 T2FB_MOUSE General transcription factor IIF subunit 2 (EC 3.6.4.12) (ATP-dependent helicase GTF2F2) (Transcription initiation factor IIF subunit beta) (TFIIF-beta) 249 28,381 Chain (1); Initiator methionine (1); Modified residue (6); Nucleotide binding (1) FUNCTION: TFIIF is a general transcription initiation factor that binds to RNA polymerase II and helps to recruit it to the initiation complex in collaboration with TFIIB. It promotes transcription elongation. This subunit shows ATP-dependent DNA-helicase activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Heterodimer of an alpha and a beta subunit. Interacts with HTATSF1 and URI1 (By similarity). Interacts with GPBP1. Interacts with GTF2B (via N-terminus); this interaction is inhibited in presence of GTF2F1 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P13984, ECO:0000269|PubMed:14612417}. +Q91XT6 TAC2N_MOUSE Tandem C2 domains nuclear protein (Membrane targeting tandem C2 domain-containing protein 1) (Tandem C2 protein in nucleus) (Tac2-N) 489 54,988 Chain (1); Domain (1); Modified residue (8); Motif (1); Mutagenesis (1); Sequence conflict (1) SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11526914}. +Q62282 TAL2_MOUSE T-cell acute lymphocytic leukemia protein 2 homolog (TAL-2) 108 12,315 Chain (1); Domain (1) +Q9JJG0 TACC2_MOUSE Transforming acidic coiled-coil-containing protein 2 1149 124,130 Alternative sequence (7); Chain (1); Coiled coil (2); Compositional bias (2); Domain (1); Modified residue (21); Sequence conflict (2) FUNCTION: Plays a role in the microtubule-dependent coupling of the nucleus and the centrosome. Involved in the processes that regulate centrosome-mediated interkinetic nuclear migration (INM) of neural progenitors. May play a role in organizing centrosomal microtubules (By similarity). {ECO:0000250, ECO:0000269|PubMed:15226440, ECO:0000269|PubMed:17920017}. PTM: Phosphorylated; which is required for localization in centrosome. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O95359}. Nucleus {ECO:0000250|UniProtKB:O95359}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:O95359}. SUBUNIT: Interacts with microtubules. Interacts with YEATS4, GCN5L2 and PCAF (By similarity). Interacts with CCDC100/CEP120. {ECO:0000250, ECO:0000269|PubMed:17920017}. TISSUE SPECIFICITY: Expressed in brain, kidney, lung, thymus and ovary. Not detectable in normal tissues at protein level. {ECO:0000269|PubMed:15226440}. +Q8C092 TAF5_MOUSE Transcription initiation factor TFIID subunit 5 (Transcription initiation factor TFIID 100 kDa subunit) (TAF(II)100) (TAFII-100) (TAFII100) 801 87,045 Chain (1); Domain (1); Repeat (6); Sequence conflict (9) FUNCTION: TAFs are components of the transcription factor IID (TFIID) complex, PCAF histone acetylase complex and TBP-free TAFII complex (TFTC). TAFs components-TIIFD are essential for mediating regulation of RNA polymerase transcription. TAF5/TAFII100 interacts strongly with the histone H4-related TAF6/TAFII80 and the histone H3-related TAF9/TAFII31, as well as a stable complex comprised of both TAF5/TAFII80 and TAF6/TAFII31. Apparently weaker interactions of TAF5/TAFII100 with TBP, TAF1/TAFII250, TAF11/TAFII28, and TAF12/TAFII20, but not TAF7/TAFII55, also have been observed (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Homodimer. TFIID and PCAF are composed of TATA binding protein (TBP) and a number of TBP-associated factors (TAFs). TBP is not part of TFTC. Component of the TFTC-HAT complex, at least composed of TAF5L, TAF6L, TADA3L, SUPT3H/SPT3, TAF2/TAFII150, TAF4/TAFII135, TAF5/TAFII100, GCN5L2/GCN5, TAF10 and TRRAP (By similarity). {ECO:0000250}. DOMAIN: Distinct domains of TAF5/TAFII100 are required for functional interaction with transcription factor TFIIFB (RAP30) and incorporation into the TFIID complex. {ECO:0000250}. +Q8R1G1 TASP1_MOUSE Threonine aspartase 1 (Taspase-1) (EC 3.4.25.-) [Cleaved into: Threonine aspartase subunit alpha; Threonine aspartase subunit beta] 420 44,360 Active site (1); Alternative sequence (2); Chain (2); Erroneous initiation (1) FUNCTION: Protease involved in KMT2A/MLL1 processing and, consequently, in the correct expression of the early HOXA gene cluster. {ECO:0000250}. SUBUNIT: Intramolecular proteolysis generates 2 subunits, alpha and beta, which reassemble through a non-covalent association to form the fully active enzyme. {ECO:0000250|UniProtKB:Q9H6P5}. +Q8BYC6 TAOK3_MOUSE Serine/threonine-protein kinase TAO3 (EC 2.7.11.1) (Thousand and one amino acid protein 3) 898 105,336 Active site (1); Binding site (1); Chain (1); Coiled coil (3); Compositional bias (1); Domain (1); Modified residue (8); Nucleotide binding (1) FUNCTION: Serine/threonine-protein kinase that acts as a regulator of the p38/MAPK14 stress-activated MAPK cascade and of the MAPK8/JNK cascade. Acts as an activator of the p38/MAPK14 stress-activated MAPK cascade. In response to DNA damage, involved in the G2/M transition DNA damage checkpoint by activating the p38/MAPK14 stress-activated MAPK cascade, probably by mediating phosphorylation of upstream MAP2K3 and MAP2K6 kinases. Inhibits basal activity of MAPK8/JNK cascade and diminishes its activation in response epidermal growth factor (EGF) (By similarity). {ECO:0000250}. PTM: Autophosphorylated. Phosphorylation at Ser-324 by ATM following DNA damage is required for activation of the p38/MAPK14 stress-activated MAPK cascade. Phosphorylated by LRRK2 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Self-associates. Interacts with ERN1 and TRAF2. Interaction with TRAF2 is facilitated under ER stress conditions, such as treatment with tunicamycin, and may promote TRAF2 phosphorylation (By similarity). {ECO:0000250}. +Q8R2N0 TAP26_MOUSE Thyroid transcription factor 1-associated protein 26 (TTF-1-associated protein 26) (Coiled-coil domain-containing protein 59) 240 28,034 Alternative sequence (2); Chain (1); Sequence conflict (2) FUNCTION: Component of the transcription complexes of the pulmonary surfactant-associated protein-B (SFTPB) and -C (SFTPC). Enhances homeobox protein Nkx-2.1-activated SFTPB and SFTPC promoter activities (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with NKX2-1. {ECO:0000250}. +P36371 TAP2_MOUSE Antigen peptide transporter 2 (APT2) (ATP-binding cassette sub-family B member 3) (Histocompatibility antigen modifier 2) 702 77,445 Chain (1); Domain (2); Nucleotide binding (1); Region (2); Topological domain (10); Transmembrane (9) TRANSMEM 7 27 Helical; Name=1. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 57 77 Helical; Name=2. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 99 119 Helical; Name=3. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 148 168 Helical; Name=4. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 187 207 Helical; Name=5. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 266 286 Helical; Name=6. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 293 313 Helical; Name=7. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 374 394 Helical; Name=8. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 408 428 Helical; Name=9. {ECO:0000255|PROSITE-ProRule:PRU00441}. TOPO_DOM 1 6 Lumenal. {ECO:0000255}.; TOPO_DOM 28 56 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 78 98 Lumenal. {ECO:0000255}.; TOPO_DOM 120 147 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 169 186 Lumenal. {ECO:0000255}.; TOPO_DOM 208 265 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 287 292 Lumenal. {ECO:0000255}.; TOPO_DOM 314 373 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 395 407 Lumenal. {ECO:0000255}.; TOPO_DOM 429 702 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum for association with MHC class I molecules. Also acts as a molecular scaffold for the final stage of MHC class I folding, namely the binding of peptide. Nascent MHC class I molecules associate with TAP via tapasin (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. Note=The transmembrane segments seem to form a pore in the membrane. SUBUNIT: Heterodimer of TAP1 and TAP2. DOMAIN: The peptide-binding site is shared between the cytoplasmic loops of TAP1 and TAP2. {ECO:0000250}. +P05213 TBA1B_MOUSE Tubulin alpha-1B chain (Alpha-tubulin 2) (Alpha-tubulin isotype M-alpha-2) (Tubulin alpha-2 chain) [Cleaved into: Detyrosinated tubulin alpha-1B chain] 451 50,152 Chain (2); Cross-link (2); Modified residue (9); Nucleotide binding (1); Sequence conflict (8); Site (1) FUNCTION: Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. PTM: Some glutamate residues at the C-terminus are polyglycylated, resulting in polyglycine chains on the gamma-carboxyl group. Glycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Both modifications can coexist on the same protein on adjacent residues, and lowering polyglycylation levels increases polyglutamylation, and reciprocally. The precise function of polyglycylation is still unclear. {ECO:0000269|PubMed:19524510}.; PTM: Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (PubMed:1967194, PubMed:15890843). Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity by SPAST increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold (By similarity). {ECO:0000250|UniProtKB:Q71U36, ECO:0000269|PubMed:15890843, ECO:0000269|PubMed:1967194}.; PTM: Acetylation of alpha chains at Lys-40 is located inside the microtubule lumen. This modification has been correlated with increased microtubule stability, intracellular transport and ciliary assembly. {ECO:0000269|PubMed:16954346, ECO:0000269|PubMed:19564401}.; PTM: Methylation of alpha chains at Lys-40 is found in mitotic microtubules and is required for normal mitosis and cytokinesis contributing to genomic stability. {ECO:0000250|UniProtKB:P68363}.; PTM: Nitration of Tyr-451 is irreversible and interferes with normal dynein intracellular distribution. {ECO:0000250|UniProtKB:Q71U36}.; PTM: Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (VASH1 or VASH2) and tubulin tyrosine ligase (TTL), respectively. {ECO:0000269|PubMed:16954346, ECO:0000269|PubMed:19564401, ECO:0000269|PubMed:26446751, ECO:0000269|PubMed:27102488, ECO:0000269|PubMed:29146868}.; PTM: Tubulin alpha-1B chain: Tyrosination promotes microtubule interaction with CAP-Gly domain-containing proteins such as CLIP1, CLIP2 and DCTN1 (PubMed:16954346, PubMed:19564401). Tyrosination regulates the initiation of dynein-dynactin motility via interaction with DCTN1, which brings the dynein-dynactin complex into contact with microtubules. In neurons, tyrosinated tubulins mediate the initiation of retrograde vesicle transport (By similarity). {ECO:0000250|UniProtKB:Q71U36, ECO:0000269|PubMed:16954346, ECO:0000269|PubMed:19564401}.; PTM: Detyrosinated tubulin alpha-1B chain: Detyrosination is involved in metaphase plate congression by guiding chromosomes during mitosis: detyrosination promotes interaction with CENPE, promoting pole-proximal transport of chromosomes toward the equator (By similarity). Detyrosination increases microtubules-dependent mechanotransduction in dystrophic cardiac and skeletal muscle (PubMed:26446751). In cardiomyocytes, detyrosinated microtubules are required to resist to contractile compression during contraction: detyrosination promotes association with desmin (DES) at force-generating sarcomeres, leading to buckled microtubules and mechanical resistance to contraction (PubMed:27102488). {ECO:0000250|UniProtKB:P68363, ECO:0000269|PubMed:26446751, ECO:0000269|PubMed:27102488}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SUBUNIT: Dimer of alpha and beta chains. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells. TISSUE SPECIFICITY: Ubiquitously expressed with highest levels in spleen, thymus and immature brain. +O35681 SYT3_MOUSE Synaptotagmin-3 (Synaptotagmin III) (SytIII) 587 63,254 Chain (1); Domain (2); Metal binding (12); Modified residue (1); Mutagenesis (3); Region (1); Sequence conflict (4); Topological domain (2); Transmembrane (1) TRANSMEM 55 75 Helical. {ECO:0000255}. TOPO_DOM 1 54 Vesicular. {ECO:0000255}.; TOPO_DOM 76 587 Cytoplasmic. {ECO:0000255}. FUNCTION: Ca(2+) sensor involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain. Ca(2+) induces binding of the C2-domains to phospholipid membranes and to assembled SNARE-complexes; both actions contribute to triggering exocytosis. Plays a role in dendrite formation by melanocytes. {ECO:0000250|UniProtKB:P40748, ECO:0000250|UniProtKB:Q9BQG1}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P40748}; Single-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000255}. SUBUNIT: Homodimer; disulfide-linked via the cysteine motif (PubMed:10531343). Can also form heterodimers with SYT6, SYT9 and SYT10 (PubMed:10531343, PubMed:10531344). {ECO:0000269|PubMed:10531343, ECO:0000269|PubMed:10531344}. DOMAIN: The cysteine motif mediates homo- or heterodimer formation via formation of disulfide bonds. {ECO:0000269|PubMed:10531343}.; DOMAIN: The first C2 domain mediates Ca(2+)-dependent phospholipid binding. {ECO:0000250|UniProtKB:P40748}. +Q3UQ84 SYTM_MOUSE Threonine--tRNA ligase, mitochondrial (EC 6.1.1.3) (Threonyl-tRNA synthetase) (ThrRS) (Threonyl-tRNA synthetase-like 1) 723 81,700 Chain (1); Modified residue (1); Sequence conflict (1); Transit peptide (1) FUNCTION: Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged tRNA(Thr) via its editing domain. {ECO:0000250|UniProtKB:Q9BW92}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9BW92}. +Q9R0N3 SYT11_MOUSE Synaptotagmin-11 (Synaptotagmin XI) (SytXI) 430 48,333 Chain (1); Domain (2); Metal binding (10); Modified residue (1); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 16 36 Helical. {ECO:0000255}. TOPO_DOM 1 15 Vesicular. {ECO:0000255}.; TOPO_DOM 37 430 Cytoplasmic. {ECO:0000255}. FUNCTION: May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. {ECO:0000250}. PTM: Ubiquitinated and targeted to the proteasome complex for degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. SUBUNIT: Homodimer. Can also form heterodimers. Interacts with PRKN (By similarity). {ECO:0000250}. +Q9R0N5 SYT5_MOUSE Synaptotagmin-5 (Synaptotagmin IX) (Synaptotagmin V) (SytV) 386 43,130 Chain (1); Domain (2); Metal binding (18); Topological domain (2); Transmembrane (1) TRANSMEM 25 45 Helical. {ECO:0000255}. TOPO_DOM 1 24 Vesicular. {ECO:0000255}.; TOPO_DOM 46 386 Cytoplasmic. {ECO:0000255}. FUNCTION: May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. Regulates the Ca(2+)-dependent secretion of norepinephrine in PC12 cells. Required for export from the endocytic recycling compartment to the cell surface. {ECO:0000269|PubMed:11751925}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:11751925}; Single-pass membrane protein {ECO:0000269|PubMed:11751925}. Recycling endosome membrane {ECO:0000269|PubMed:11751925}; Single-pass membrane protein {ECO:0000269|PubMed:11751925}. Note=In mast cells, localizes to the endocytic recycling compartment. SUBUNIT: Homodimer (By similarity). Interacts with both alpha- and beta-tubulin (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P47861}. +Q9R0N8 SYT6_MOUSE Synaptotagmin-6 (Synaptotagmin VI) (SytVI) 511 57,204 Alternative sequence (1); Chain (1); Domain (2); Metal binding (12); Modified residue (1); Region (2); Sequence conflict (3); Topological domain (2); Transmembrane (1) TRANSMEM 60 80 Helical. {ECO:0000255}. TOPO_DOM 1 59 Vesicular. {ECO:0000255}.; TOPO_DOM 81 511 Cytoplasmic. {ECO:0000255}. FUNCTION: May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis (By similarity). May mediate Ca(2+)-regulation of exocytosis in acrosomal reaction in sperm (PubMed:15774481). {ECO:0000250, ECO:0000269|PubMed:15774481}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:10531344}; Single-pass membrane protein {ECO:0000269|PubMed:10531344}.; SUBCELLULAR LOCATION: Isoform 1: Membrane; Single-pass membrane protein. Note=Localized predominantly to endoplasmic reticulum (ER) and/or Golgi-like perinuclear compartment (PubMed:10531344). {ECO:0000269|PubMed:10531344}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm, cytosol {ECO:0000269|PubMed:10531344}. Cell membrane {ECO:0000269|PubMed:10531344}; Peripheral membrane protein {ECO:0000269|PubMed:10531344}. SUBUNIT: Isoform 1: Homodimer; disulfide-linked via the cysteine motif (PubMed:10531343, PubMed:10531344). Isoform 1: Can also form heterodimers with SYT3, SYT7, SYT9 and SYT10 (PubMed:10531343, PubMed:10531344, PubMed:10871604). Isoform 1: Interacts with STX1A, STX1B and STX2; the interaction is Ca(2+)-dependent (PubMed:15774481). Isoform 2: Is not able to form homodimer and heterodimers (PubMed:10531344). {ECO:0000269|PubMed:10531343, ECO:0000269|PubMed:10531344, ECO:0000269|PubMed:10871604, ECO:0000269|PubMed:15774481}. DOMAIN: The cysteine motif mediates homo- or heterodimer formation via formation of disulfide bonds. {ECO:0000250|UniProtKB:O35681}. TISSUE SPECIFICITY: Isoform 1 is expressed in the olfactory bulb. Isoform 2 is expressed in the brain (at protein level). {ECO:0000269|PubMed:10531344}. +Q91ZZ3 SYUB_MOUSE Beta-synuclein 133 14,052 Chain (1); Modified residue (2); Region (1); Repeat (4) FUNCTION: May be involved in neuronal plasticity. {ECO:0000250}. PTM: Phosphorylated. Phosphorylation by G-protein coupled receptor kinases (GRK) is more efficient than phosphorylation by CK1, CK2 and CaM-kinase II (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in the brain. {ECO:0000269|PubMed:11474193}. +Q922P8 T132A_MOUSE Transmembrane protein 132A (HSPA5-binding protein 1) 1018 110,239 Chain (1); Erroneous initiation (1); Erroneous termination (1); Glycosylation (1); Region (2); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 847 867 Helical. {ECO:0000255}. TOPO_DOM 33 846 Extracellular. {ECO:0000255}.; TOPO_DOM 868 1018 Cytoplasmic. {ECO:0000255}. FUNCTION: May play a role in embryonic and postnatal development of the brain. Increased resistance to cell death induced by serum starvation in cultured cells. Regulates cAMP-induced GFAP gene expression via STAT3 phosphorylation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Interacts with HSPA5/GRP78. {ECO:0000250}. +Q91XD3 T4S4_MOUSE Transmembrane 4 L6 family member 4 202 21,296 Chain (1); Glycosylation (1); Topological domain (5); Transmembrane (4) TRANSMEM 10 30 Helical. {ECO:0000255}.; TRANSMEM 49 69 Helical. {ECO:0000255}.; TRANSMEM 94 114 Helical. {ECO:0000255}.; TRANSMEM 159 179 Helical. {ECO:0000255}. TOPO_DOM 1 9 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 31 48 Extracellular. {ECO:0000255}.; TOPO_DOM 70 93 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 115 158 Extracellular. {ECO:0000255}.; TOPO_DOM 180 202 Cytoplasmic. {ECO:0000255}. FUNCTION: Regulates the adhesive and proliferative status of intestinal epithelial cells. Can mediate density-dependent cell proliferation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q8VE65 TAF12_MOUSE Transcription initiation factor TFIID subunit 12 (Transcription initiation factor TFIID 20 kDa subunits) (TAFII-20) (TAFII20) 161 17,875 Chain (1); Cross-link (1); Domain (1); Modified residue (3); Sequence conflict (3) FUNCTION: TAFs are components of the transcription factor IID (TFIID) complex, PCAF histone acetylase complex and TBP-free TAFII complex (TFTC). TAFs components-TIIFD are essential for mediating regulation of RNA polymerase transcription (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: TFIID and PCAF are composed of TATA binding protein (TBP) and a number of TBP-associated factors (TAFs). TBP is not part of TFTC. Interacts directly with TBP; additional interactions between TAFII20 and TAFII28 or TAFII30 were detected. Component of the PCAF complex, at least composed of TADA2L/ADA2, TADA3L/ADA3, TAF5L, SUPT3H, TAF6L, TAF9, TAF10, TAF12 and TRRAP. Component of the STAGA transcription coactivator-HAT complex, at least composed of SUPT3H, GCN5L2, TAF5L, TAF6L, SUPT7L, TADA3L, TAD1L, TAF10, TAF12, TRRAP and TAF9. Interacts with ATF7 (via its transactivation domain); the interaction promotes the transactivation of ATF7 and is prevented by sumoylation of ATF7 (By similarity). {ECO:0000250}. +G5E8Z2 TAF4B_MOUSE Transcription initiation factor TFIID subunit 4B (Transcription initiation factor TFIID 105 kDa subunit) (TAF(II)105) (TAFII-105) (TAFII105) 850 89,528 Chain (1); Domain (2); Modified residue (1); Motif (1); Region (2); Sequence conflict (2) FUNCTION: Cell type-specific subunit of the general transcription factor TFIID that may function as a gene-selective coactivator in certain cells. TFIID is a multimeric protein complex that plays a central role in mediating promoter responses to various activators asond repressors. TAF4B is a transcriptional coactivator of the p65/RELA NF-kappa-B subunit. Involved in the activation of a subset of antiapoptotic genes including TNFAIP3. Through interaction with OCBA/POU2AF1, acts as a coactivator of B-cell-specific transcription. Plays a role in spermiogenesis and oogenesis. {ECO:0000250|UniProtKB:Q92750, ECO:0000269|PubMed:11557891, ECO:0000269|PubMed:15774719}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92750}. Cytoplasm {ECO:0000250|UniProtKB:Q92750}. Note=Export into the cytoplasm is mediated by a CRM1-independent nuclear export pathway and not by phosphorylation. {ECO:0000250|UniProtKB:Q92750}. SUBUNIT: TFIID is composed of TATA binding protein (TBP) and a number of TBP-associated factors (TAFs). Heterodimerizes with TAF12/TFII20 via the C-terminal H2A-like histone-fold domain. This heterodimer forms a histone-like octamer with the TAF6/TAFII70-TAF9/TAFII31 heterodimer. Interacts with P65/RELA homodimers and P65/RELA-REL heterodimers. Interaction with POU2AF1, via its C-terminal activation domain, is required for octamer-dependent transcription. {ECO:0000250|UniProtKB:Q92750}. TISSUE SPECIFICITY: Highly expressed in the testes and ovary, whereas lower levels are detected in most other tissues. {ECO:0000269|PubMed:11557891}. +P97358 TAF1B_MOUSE TATA box-binding protein-associated factor RNA polymerase I subunit B (RNA polymerase I-specific TBP-associated factor 68 kDa) (TAFI68) (TATA box-binding protein-associated factor 1B) (TBP-associated factor 1B) (Transcription initiation factor SL1/TIF-IB subunit B) 586 67,954 Alternative sequence (2); Chain (1); Metal binding (4); Modified residue (2); Region (4); Sequence conflict (8); Zinc finger (1) FUNCTION: Component of RNA polymerase I core factor complex that acts as a GTF2B/TFIIB-like factor and plays a key role in multiple steps during transcription initiation such as pre-initiation complex (PIC) assembly and postpolymerase recruitment events in polymerase I (Pol I) transcription. Binds rDNA promoters and plays a role in Pol I recruitment as a component of the SL1/TIF-IB complex and, possibly, directly through its interaction with RRN3. {ECO:0000269|PubMed:9050847}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. SUBUNIT: Component of the transcription factor SL1/TIF-IB complex, composed of TBP and at least TAF1A, TAF1B, TAF1C and TAF1D. In the complex interacts directly with TBP, TAF1A and TAF1C. Interaction of the SL1/TIF-IB subunits with TBP excludes interaction of TBP with the transcription factor IID (TFIID) subunits. Interacts with TBP and RRN3. Interacts with FLNA (via N-terminus). {ECO:0000269|PubMed:12015311, ECO:0000269|PubMed:21228480, ECO:0000269|PubMed:9050847}. DOMAIN: Although it shares weak sequence similarity with GTF2B/TFIIB, displays a similar subdomain organization as GTF2B/TFIIB, with a N-terminal zinc finger, a connecting region (composed of B-reader and B-linker regions), followed by 2 cyclin folds. The RRN7-type zinc finger plays an essential postrecruitment role in Pol I transcription at a step preceding synthesis of the first 40 nucleotides (By similarity). {ECO:0000250}. +P58871 TB182_MOUSE 182 kDa tankyrase-1-binding protein 1720 181,825 Chain (1); Compositional bias (2); Erroneous gene model prediction (1); Modified residue (66); Motif (2); Region (2); Sequence conflict (2) PTM: ADP-ribosylated by TNKS1. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Chromosome {ECO:0000250}. Note=Colocalizes with chromosomes during mitosis, and in the cytoplasm with cortical actin. {ECO:0000250}. SUBUNIT: Binds to the ANK repeat domain of TNKS1 and TNKS2. {ECO:0000250}. +Q8BYH7 TBC17_MOUSE TBC1 domain family member 17 645 72,860 Chain (1); Compositional bias (1); Domain (1); Modified residue (4); Region (1); Sequence conflict (2); Site (2) FUNCTION: Probable GTPase-activating protein for Rab8; its transient association with Rab8 is mediated by OPTN. Inhibits Rab8-mediated endocytic trafficking, such as of transferrin receptor (TfR) and reduces Rab8 recruitnment to tubules emanating from the endocytic recycling compartment (ERC). Involved in regulation of autophagy. Mediates inhibition of autophagy caused by the OPTN variant GLC1E LYS-50; the function requires its catalytic activity, however, the involved Rab is not known (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome {ECO:0000250}. SUBUNIT: Interacts with OPTN. DOMAIN: The arginine and glutamine fingers are critical for the GTPase-activating mechanism, they pull out Rab's 'switch 2' glutamine and insert in Rab's active site. {ECO:0000250}. +P48428 TBCA_MOUSE Tubulin-specific chaperone A (TCP1-chaperonin cofactor A) (Tubulin-folding cofactor A) (CFA) 108 12,758 Chain (1); Initiator methionine (1); Modified residue (1) FUNCTION: Tubulin-folding protein; involved in the early step of the tubulin folding pathway. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SUBUNIT: Supercomplex made of cofactors A to E. Cofactors A and D function by capturing and stabilizing tubulin in a quasi-native conformation. Cofactor E binds to the cofactor D-tubulin complex; interaction with cofactor C then causes the release of tubulin polypeptides that are committed to the native state. TISSUE SPECIFICITY: Widely expressed, but is most abundant in the testis. +Q9D5I4 TC1D1_MOUSE Tctex1 domain-containing protein 1 173 19,680 Chain (1) SUBUNIT: Interacts with ZMYND10. {ECO:0000250|UniProtKB:Q8N7M0}. +P01853 TCC1_MOUSE T-cell receptor gamma chain C region C10.5 167 19,101 Chain (1); Non-terminal residue (1); Region (1); Topological domain (1); Transmembrane (1) TRANSMEM 135 155 Helical. {ECO:0000255}. TOPO_DOM 156 167 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q8CGF7 TCRG1_MOUSE Transcription elongation regulator 1 (Formin-binding protein 28) (FBP 28) (TATA box-binding protein-associated factor 2S) (Transcription factor CA150) (p144) 1100 123,788 Alternative sequence (3); Beta strand (7); Chain (1); Coiled coil (3); Compositional bias (6); Cross-link (3); Domain (9); Erroneous initiation (1); Modified residue (8); Motif (1); Natural variant (1); Sequence conflict (3); Turn (3) FUNCTION: Transcription factor that binds RNA polymerase II and inhibits the elongation of transcripts from target promoters. Regulates transcription elongation in a TATA box-dependent manner (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Binds RNA polymerase II, HD and SF1 (By similarity). Binds formin. Interacts (via the second WW domain) with TREX1 (via proline-rich region). {ECO:0000250, ECO:0000269|PubMed:15485897, ECO:0000269|PubMed:17355961, ECO:0000269|PubMed:8605874}. DOMAIN: The FF domains preferentially binds peptides with the consensus sequence [DE](2-5)-[FWY]-[DE](2-5) and mediate interaction with HTATSF1 and probably bind the phosphorylated C-terminus of the largest subunit of RNA polymerase II. {ECO:0000269|PubMed:15485897}.; DOMAIN: The WW domains bind Pro-rich domains. {ECO:0000269|PubMed:15485897}. +Q8K1H1 TDRD7_MOUSE Tudor domain-containing protein 7 (PCTAIRE2-binding protein) (Tudor repeat associator with PCTAIRE-2) (Trap) 1086 122,174 Beta strand (8); Chain (1); Compositional bias (1); Domain (5); Erroneous gene model prediction (2); Helix (14); Modified residue (1); Region (2); Turn (5) FUNCTION: Component of specific cytoplasmic RNA granules involved in post-transcriptional regulation of specific genes: probably acts by binding to specific mRNAs and regulating their translation. Required for lens transparency during lens development, by regulating translation of genes such as CRYBB3 and HSPB1 in the developing lens. Also required during spermatogenesis. {ECO:0000269|PubMed:21436445}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11527406, ECO:0000269|PubMed:17141210, ECO:0000269|PubMed:21436445}. Note=Localizes to cytoplasmic RNA granules. Present in chromatoid body (CB) of spermatids (mammalian counterpart of germplasm, pole plasm or polar granules in Drosophila germ cells), also named processing bodies (P-bodies) in somatic cells. Detected in the multilobular cytoplasmic CBs (also called intermitochondrial cementin) in pachytene spermatocytes and as a single perinuclear CB in haploid round spermatids. SUBUNIT: Found in a mRNP complex, at least composed of TDRD1, TDRD6, TDRD7 and DDX4. Found in a complex containing CABLES1, CDK16 and CDK17. Interacts with CABLES1, CDK17 and PIWIL1. {ECO:0000269|PubMed:11527406, ECO:0000269|PubMed:17141210, ECO:0000269|PubMed:19584108}. TISSUE SPECIFICITY: Mainly expressed in testis. Expressed in spermatogonia, spermatocytes and round spermatids (at protein level). Also expressed in the developing lens. {ECO:0000269|PubMed:17141210, ECO:0000269|PubMed:21436445}. +P51865 TDGF1_MOUSE Teratocarcinoma-derived growth factor (Cripto growth factor) (Epidermal growth factor-like Cripto protein) 171 18,754 Beta strand (2); Chain (1); Disulfide bond (6); Domain (1); Glycosylation (1); Lipidation (1); Mutagenesis (1); Propeptide (1); Signal peptide (1) FUNCTION: GPI-anchored cell membrane protein involved in Nodal signaling. Cell-associated Tdgf1 acts as a Nodal coreceptor in cis. Shedding of Tdgf1 by Tmem8a modulates Nodal signaling by allowing soluble Tdgf1 to act as a Nodal coreceptor on other cells. Could play a role in the determination of the epiblastic cells that subsequently give rise to the mesoderm. {ECO:0000250|UniProtKB:P13385}. PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, it is processed by GPI processing phospholipase A2 (Tmem8a), removing an acyl-chain at the sn-2 position of GPI and releasing Tdgf1 as a lysophosphatidylinositol-bearing form, which is further cleaved by phospholipase D (Gpld1) into a soluble form. {ECO:0000250|UniProtKB:P13385}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10640699}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:10640699}. Secreted {ECO:0000250|UniProtKB:P13385}. Note=Released from the cell membrane by GPI cleavage. {ECO:0000250|UniProtKB:P13385}. SUBUNIT: Interacts with the activin type-1 receptor ACVR1B. {ECO:0000250}. TISSUE SPECIFICITY: Expressed at low level in specific organs of the adult animal such as spleen, heart, lung and brain. During gastrulation, expressed in the forming mesoderm. In later stages of the developing heart, expression is restricted to the truncus arteriosus. +Q80VL1 TDRKH_MOUSE Tudor and KH domain-containing protein (Tudor domain-containing protein 2) 560 62,134 Beta strand (5); Chain (1); Cross-link (14); Domain (3); Helix (3); Modified residue (1); Turn (1) FUNCTION: Participates in the primary piRNA biogenesis pathway and is required during spermatogenesis to repress transposable elements and prevent their mobilization, which is essential for the germline integrity. The piRNA metabolic process mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and govern the methylation and subsequent repression of transposons. Required for the final steps of primary piRNA biogenesis by participating in the processing of 31-37 nt intermediates into mature piRNAs. May act in pi-bodies and piP-bodies by transferring piRNA precursors or intermediates to or between these granules. {ECO:0000269|PubMed:23714778}. PTM: Ubiquitinated by PRKN during mitophagy, leading to its degradation and enhancement of mitophagy. Deubiquitinated by USP30. {ECO:0000250|UniProtKB:Q9Y2W6}. SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion. Note=Probable component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis. Colocalizes with pi- and piP-bodies, a subset of the nuage which contains secondary piRNAs. Associated with mitochondria in the germline. SUBUNIT: Interacts with (symmetrically methylated) PIWIL1, PIWIL2 and PIWIL4. {ECO:0000269|PubMed:19584108, ECO:0000269|PubMed:19918066, ECO:0000269|PubMed:23714778}. TISSUE SPECIFICITY: Highly expressed in testis, present at lower level in brain. Weakly or not expressed in other tissues (at protein level). {ECO:0000269|PubMed:19918066}. +Q6YCH2 TDPZ4_MOUSE TD and POZ domain-containing protein 4 370 42,196 Chain (1); Domain (2); Sequence conflict (18) +Q9JLC6 TEF_MOUSE Thyrotroph embryonic factor 301 33,145 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (1); Modified residue (1); Region (2); Sequence conflict (5) FUNCTION: Transcription factor that binds to and transactivates the TSHB promoter. Binds to a minimal DNA-binding sequence 5'-[TC][AG][AG]TTA[TC][AG]-3' (By similarity). Also activates the telokin promoter in smooth muscle-specific and calcium-dependent manner. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Binds DNA as a homodimer or a heterodimer. Can form a heterodimer with DBP (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Isoform Alpha and isoform Beta are expressed at high levels in lung, bladder, kidney, gut and brain. +O55042 SYUA_MOUSE Alpha-synuclein (Non-A beta component of AD amyloid) (Non-A4 component of amyloid precursor) (NACP) 140 14,485 Alternative sequence (2); Chain (1); Metal binding (2); Modified residue (3); Region (1); Repeat (4); Sequence conflict (1) FUNCTION: May be involved in the regulation of dopamine release and transport. PTM: Phosphorylated, predominantly on serine residues. Phosphorylated on Tyr-125 upon osmotic stress (By similarity). {ECO:0000250}.; PTM: Ubiquitinated. The predominant conjugate is the diubiquitinated form (By similarity). {ECO:0000250}.; PTM: Acetylation at Met-1 seems to be important for proper folding and native oligomeric structure. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P37840}. Membrane {ECO:0000250|UniProtKB:P37840}. Nucleus {ECO:0000250|UniProtKB:P37840}. Cell junction, synapse {ECO:0000250|UniProtKB:P37840}. Secreted {ECO:0000250|UniProtKB:P37840}. SUBUNIT: Interacts with UCHL1. {ECO:0000250}. +Q8K1H7 T11L2_MOUSE T-complex protein 11-like protein 2 517 57,889 Chain (1); Compositional bias (1); Erroneous initiation (1); Modified residue (1) +Q8R218 T150B_MOUSE Modulator of macroautophagy TMEM150B (Transmembrane protein 150B) 238 26,578 Alternative sequence (2); Chain (1); Glycosylation (1); Topological domain (7); Transmembrane (6) TRANSMEM 9 29 Helical. {ECO:0000255}.; TRANSMEM 52 72 Helical. {ECO:0000255}.; TRANSMEM 87 107 Helical. {ECO:0000255}.; TRANSMEM 117 137 Helical. {ECO:0000255}.; TRANSMEM 157 177 Helical. {ECO:0000255}.; TRANSMEM 187 207 Helical. {ECO:0000255}. TOPO_DOM 1 8 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 30 51 Extracellular. {ECO:0000305}.; TOPO_DOM 73 86 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 108 116 Extracellular. {ECO:0000305}.; TOPO_DOM 138 156 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 178 186 Extracellular. {ECO:0000305}.; TOPO_DOM 208 238 Cytoplasmic. {ECO:0000250|UniProtKB:Q86TG1}. FUNCTION: Modulator of macroautophagy that causes accumulation of autophagosomes under basal conditions and enhances autophagic flux (By similarity). Represses cell death and promotes long-term clonogenic survival of cells grown in the absence of glucose in a macroautophagy-independent manner (By similarity). May have some role in extracellular matrix engulfment or growth factor receptor recycling, both of which can modulate cell survival (By similarity). {ECO:0000250|UniProtKB:A6NC51}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:A6NC51}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A6NC51}. Endosome membrane {ECO:0000250|UniProtKB:A6NC51}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:A6NC51}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes mainly at the plasma membrane where it concentrates at actin-rich focal adhesions (By similarity). {ECO:0000250|UniProtKB:A6NC51}. +Q7TQA6 T2R38_MOUSE Taste receptor type 2 member 38 (T2R38) (T2R138) (mT2R31) 331 36,966 Chain (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 18 38 Helical; Name=1. {ECO:0000255}.; TRANSMEM 56 76 Helical; Name=2. {ECO:0000255}.; TRANSMEM 95 115 Helical; Name=3. {ECO:0000255}.; TRANSMEM 143 163 Helical; Name=4. {ECO:0000255}.; TRANSMEM 190 210 Helical; Name=5. {ECO:0000255}.; TRANSMEM 244 264 Helical; Name=6. {ECO:0000255}.; TRANSMEM 277 297 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 17 Extracellular. {ECO:0000255}.; TOPO_DOM 39 55 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 77 94 Extracellular. {ECO:0000255}.; TOPO_DOM 116 142 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 164 189 Extracellular. {ECO:0000255}.; TOPO_DOM 211 243 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 265 276 Extracellular. {ECO:0000255}.; TOPO_DOM 298 331 Cytoplasmic. {ECO:0000255}. FUNCTION: Putative taste receptor which may play a role in the perception of bitterness. {ECO:0000303|PubMed:12734386}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Low levels in tongue, stomach and duodenum. {ECO:0000269|PubMed:15886333}. +Q7TQA5 T2R39_MOUSE Taste receptor type 2 member 39 (T2R39) (mT2R34) 319 36,308 Chain (1); Glycosylation (4); Topological domain (8); Transmembrane (7) TRANSMEM 17 37 Helical; Name=1. {ECO:0000255}.; TRANSMEM 66 86 Helical; Name=2. {ECO:0000255}.; TRANSMEM 98 118 Helical; Name=3. {ECO:0000255}.; TRANSMEM 138 158 Helical; Name=4. {ECO:0000255}.; TRANSMEM 195 215 Helical; Name=5. {ECO:0000255}.; TRANSMEM 248 268 Helical; Name=6. {ECO:0000255}.; TRANSMEM 274 294 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 16 Extracellular. {ECO:0000255}.; TOPO_DOM 38 65 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 87 97 Extracellular. {ECO:0000255}.; TOPO_DOM 119 137 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 159 194 Extracellular. {ECO:0000255}.; TOPO_DOM 216 247 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 269 273 Extracellular. {ECO:0000255}.; TOPO_DOM 295 319 Cytoplasmic. {ECO:0000255}. FUNCTION: Putative taste receptor which may play a role in the perception of bitterness. {ECO:0000303|PubMed:12734386}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. +A2AKQ8 T30A2_MOUSE Tetratricopeptide repeat protein 30A2 (TPR repeat protein 30A2) 664 76,120 Chain (1); Coiled coil (1); Compositional bias (1); Repeat (8) FUNCTION: Required for polyglutamylation of axonemal tubulin. Plays a role in anterograde intraflagellar transport (IFT), the process by which cilia precursors are transported from the base of the cilium to the site of their incorporation at the tip. {ECO:0000250}. SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000250}. +Q9D4V4 TAF1D_MOUSE TATA box-binding protein-associated factor RNA polymerase I subunit D (TATA box-binding protein-associated factor 1D) (TBP-associated factor 1D) (Transcription initiation factor SL1/TIF-IB subunit D) 322 36,977 Alternative sequence (2); Chain (1); Modified residue (3); Sequence conflict (4) FUNCTION: Component of the transcription factor SL1/TIF-IB complex, which is involved in the assembly of the PIC (preinitiation complex) during RNA polymerase I-dependent transcription. The rate of PIC formation probably is primarily dependent on the rate of association of SL1/TIF-IB with the rDNA promoter. SL1/TIF-IB is involved in stabilization of nucleolar transcription factor 1/UBTF on rDNA. Formation of SL1/TIF-IB excludes the association of TBP with TFIID subunits (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the transcription factor SL1/TIF-IB complex, composed of TBP and at least TAF1A, TAF1B, TAF1C and TAF1D. Interacts with UBTF (By similarity). {ECO:0000250}. +Q8BGV3 TACD2_MOUSE Tumor-associated calcium signal transducer 2 (Cell surface glycoprotein Trop-2) 317 35,574 Chain (1); Disulfide bond (3); Domain (1); Glycosylation (4); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 271 291 Helical. {ECO:0000255}. TOPO_DOM 25 270 Extracellular. {ECO:0000255}.; TOPO_DOM 292 317 Cytoplasmic. {ECO:0000255}. FUNCTION: May function as a growth factor receptor. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Expressed in kidney, lung, ovary and testis. High levels of expression in immortalized keratinocytes. {ECO:0000269|PubMed:9462726}. +Q9EQH4 TAF8_MOUSE Transcription initiation factor TFIID subunit 8 (Protein taube nuss) (TBP-associated factor 8) 308 33,988 Alternative sequence (6); Chain (1); Domain (1); Initiator methionine (1); Modified residue (3); Motif (1); Sequence conflict (3) FUNCTION: Transcription factor TFIID is one of the general factors required for accurate and regulated initiation by RNA polymerase II. Mediates both basal and activator-dependent transcription. Plays a role in the differentiation of preadipocyte fibroblasts to adipocytes, however does not seem to play a role in differentiation of myoblasts. Required for the integration of TAF10 in the TAF complex (By similarity). May be important for survival of cells of the inner cell mass which constitute the pluripotent cell population of the early embryo. {ECO:0000250, ECO:0000269|PubMed:11076765, ECO:0000269|PubMed:14580349}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11076765}. Cytoplasm {ECO:0000269|PubMed:11076765}. Note=Localized in the cytoplasm and transported from the cytoplasm to the nucleus in some cells, possibly depending on the functional or developmental state of the cell. SUBUNIT: TFIID is composed of TATA binding protein (TBP) and a number of TBP-associated factors (TAFs). Interacts with TBP, TAF1, TAF6, TAF10, TAF11 and TAF13. Component also of a small TAF complex (SMAT) containing TAF8, TAF10 and SUPT7L. Forms a heterodimer with TAF10. Interaction with TAF10 is mediated mainly via its histone fold domain while interaction with SUPT7L is via its C-terminal region (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Low level of expression throughout the brain with slightly higher expression in the hippocampus. +P70347 TANK_MOUSE TRAF family member-associated NF-kappa-B activator (TRAF-interacting protein) (I-TRAF) 448 50,939 Alternative sequence (5); Chain (1); Coiled coil (1); Modified residue (6); Region (4); Sequence conflict (1); Zinc finger (1) FUNCTION: Adapter protein involved in I-kappa-B-kinase (IKK) regulation which constitutively binds TBK1 and IKBKE playing a role in antiviral innate immunity. Acts as a regulator of TRAF function by maintaining them in a latent state. Blocks TRAF2 binding to LMP1 and inhibits LMP1-mediated NF-kappa-B activation. Negatively regulates NF-kappaB signaling and cell survival upon DNA damage. Plays a role as an adapter to assemble ZC3H12A, USP10 in a deubiquitination complex which plays a negative feedback response to attenuate NF-kappaB activation through the deubiquitination of IKBKG or TRAF6 in response to interleukin-1-beta (IL1B) stimulation or upon DNA damage. Promotes UBP10-induced deubiquitination of TRAF6 in response to DNA damage. May control negatively TRAF2-mediated NF-kappa-B activation signaled by CD40, TNFR1 and TNFR2. Essential for the efficient induction of IRF-dependent transcription following infection with Sendai virus. {ECO:0000250|UniProtKB:Q92844}. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Homodimer. Found in a deubiquitination complex with TANK, USP10 and ZC3H12A; this complex inhibits genotoxic stress- or interleukin-1-beta-mediated NF-kappaB activation by promoting IKBKG or TRAF6 deubiquitination. Interacts with IKBKG; this interaction increases in response to DNA damage. Interacts with TRAF6; this interaction increases in response to DNA damage and recruits USP10 to the ubiquitinated TRAF6. Interacts with USP10; this interaction increases in response to DNA damage. Interacts with TBK1 and IKBKE. Interacts also with TRAF1, TRAF2, and TRAF3 by binding to their TRAF-C domains; the interaction with TRAF2 is disrupted by the phosphorylation of TANK by IKBKE. Interacts more strongly with TRAF1 and TRAF2 than TRAF3. Part of a ternary complex consisting of TANK, IKBKB and IKBKG (By similarity). Interacts with IKBKG; the interaction is enhanced by IKBKE and TBK1 (PubMed:12133833). {ECO:0000250|UniProtKB:Q92844, ECO:0000269|PubMed:12133833}. TISSUE SPECIFICITY: Heart, brain, spleen, lung, liver, skeletal muscle, kidney and testis. +P21958 TAP1_MOUSE Antigen peptide transporter 1 (APT1) (ATP-binding cassette sub-family B member 2) (Histocompatibility antigen modifier 1) (Peptide transporter TAP1) 724 78,864 Chain (1); Domain (2); Nucleotide binding (1); Region (2); Sequence conflict (11); Topological domain (11); Transmembrane (10) TRANSMEM 12 32 Helical; Name=1. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 37 59 Helical; Name=2. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 69 89 Helical; Name=3. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 110 130 Helical; Name=4. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 163 183 Helical; Name=5. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 204 224 Helical; Name=6. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 275 295 Helical; Name=7. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 305 325 Helical; Name=8. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 395 415 Helical; Name=9. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 420 440 Helical; Name=10. {ECO:0000255|PROSITE-ProRule:PRU00441}. TOPO_DOM 1 11 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 33 36 Lumenal. {ECO:0000255}.; TOPO_DOM 60 68 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 90 109 Lumenal. {ECO:0000255}.; TOPO_DOM 131 162 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 184 203 Lumenal. {ECO:0000255}.; TOPO_DOM 225 274 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 296 304 Lumenal. {ECO:0000255}.; TOPO_DOM 326 394 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 416 419 Lumenal. {ECO:0000255}.; TOPO_DOM 441 724 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum for association with MHC class I molecules. Also acts as a molecular scaffold for the final stage of MHC class I folding, namely the binding of peptide. Nascent MHC class I molecules associate with TAP via tapasin (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. Note=The transmembrane segments seem to form a pore in the membrane. SUBUNIT: Heterodimer of TAP1 and TAP2. Interacts with PSMB5 and PSMB8 (By similarity). {ECO:0000250}. DOMAIN: The peptide-binding site is shared between the cytoplasmic loops of TAP1 and TAP2. {ECO:0000250}. +Q4VBD2 TAPT1_MOUSE Transmembrane anterior posterior transformation protein 1 564 63,894 Chain (1); Compositional bias (1); Initiator methionine (1); Modified residue (3); Transmembrane (6) TRANSMEM 108 128 Helical. {ECO:0000255}.; TRANSMEM 154 176 Helical. {ECO:0000255}.; TRANSMEM 233 253 Helical. {ECO:0000255}.; TRANSMEM 332 352 Helical. {ECO:0000255}.; TRANSMEM 400 420 Helical. {ECO:0000255}.; TRANSMEM 429 449 Helical. {ECO:0000255}. FUNCTION: Plays a role in primary cilia formation (By similarity). May act as a downstream effector of HOXC8 possibly by transducing or transmitting extracellular information required for axial skeletal patterning during development (By similarity). May be involved in cartilage and bone development (By similarity). May play a role in the differentiation of cranial neural crest cells (By similarity). {ECO:0000250|UniProtKB:A2BIE7, ECO:0000250|UniProtKB:Q6NXT6, ECO:0000269|PubMed:17151244}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q6NXT6}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q6NXT6}. Membrane {ECO:0000250|UniProtKB:Q6NXT6}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q6NXT6}. TISSUE SPECIFICITY: Ubiquitous. Expressed throughout embryo. {ECO:0000269|PubMed:17151244}. +P58802 TB10A_MOUSE TBC1 domain family member 10A (EBP50-PDX interactor of 64 kDa) (EPI64 protein) 500 56,202 Chain (1); Domain (1); Modified residue (5); Region (1); Site (2) FUNCTION: Acts as GTPase-activating protein for RAB27A. {ECO:0000250}. SUBCELLULAR LOCATION: Cell projection, microvillus {ECO:0000250}. Note=Localizes to the microvilli-rich region of the syncytiotrophoblast. {ECO:0000250}. SUBUNIT: Binds to the first PDZ domain of SLC9A3R1 and SLC9A3R2. {ECO:0000250}. DOMAIN: The arginine and glutamine fingers are critical for the GTPase-activating mechanism, they pull out Rab's 'switch 2' glutamine and insert in Rab's active site. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in most tissues, except for skeletal muscle. {ECO:0000269|PubMed:11285285}. +Q3UX10 TBAL3_MOUSE Tubulin alpha chain-like 3 446 49,988 Chain (1); Nucleotide binding (1); Sequence conflict (1) FUNCTION: Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain (By similarity). {ECO:0000250}. PTM: Some glutamate residues at the C-terminus are polyglycylated, resulting in polyglycine chains on the gamma-carboxyl group. Glycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Both modifications can coexist on the same protein on adjacent residues, and lowering polyglycylation levels increases polyglutamylation, and reciprocally. The precise function of polyglycylation is still unclear. {ECO:0000250|UniProtKB:P68369}.; PTM: Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (By similarity). Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity by SPAST increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold (By similarity). {ECO:0000250|UniProtKB:P68369, ECO:0000250|UniProtKB:Q71U36}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. SUBUNIT: Dimer of alpha and beta chains. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells. +A3KGB4 TBC8B_MOUSE TBC1 domain family member 8B 1114 127,893 Chain (1); Domain (4); Site (2) FUNCTION: May act as a GTPase-activating protein for Rab family protein(s). DOMAIN: The arginine and glutamine fingers are critical for the GTPase-activating mechanism, they pull out Rab's 'switch 2' glutamine and insert in Rab's active site. {ECO:0000250}. +Q9D9D3 TBC21_MOUSE TBC1 domain family member 21 (Male germ cell Rab GTPase-activating protein) 336 39,261 Chain (1); Domain (1); Sequence conflict (1) FUNCTION: May act as a GTPase-activating protein for Rab family protein(s). May be involved in acrosome formation and cytoskeletal reorganization during spermiogenesis, possibly by regulating RAB3A activity. {ECO:0000305|PubMed:21128978}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:21128978}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:21128978}. Note=Located at the edge of the acrosomal region, neck and annulus during spermiogenesis. Colocalizes with RAB3A at the acrosome-acroplaxome and neck regions of spermatids. Colocalizes with ACTB at the neck region in elongated spermatids. {ECO:0000269|PubMed:21128978}. SUBUNIT: Interacts with ACTB. {ECO:0000269|PubMed:21128978}. TISSUE SPECIFICITY: Expressed in testis, specifically in elongating and elongated spermatids (at protein level). {ECO:0000269|PubMed:21128978}. +Q8K0F1 TBC23_MOUSE TBC1 domain family member 23 684 76,426 Alternative sequence (2); Chain (1); Domain (2); Modified residue (6); Mutagenesis (1); Region (3) FUNCTION: Putative Rab GTPase-activating protein which plays a role in vesicular trafficking. Involved in endosome-to-Golgi trafficking. Acts as a bridging protein by binding simultaneously to golgins, including GOLGA1 and GOLGA4, located at the trans-Golgi, and to the WASH complex, located on endosome-derived vesicles (PubMed:29084197). Together with WDR11 complex facilitates the golgin-mediated capture of vesicles generated using AP-1 (By similarity). Plays a role in brain development, including in cortical neuron positioning. May also be important for neurite outgrowth, possibly through its involvement in membrane trafficking and cargo delivery, 2 processes which are essential for axonal and dendritic growth (PubMed:28823707). May act as a general inhibitor of innate immunity signaling, strongly inhibiting multiple TLR and dectin/CLEC7A-signaling pathways. Does not alter initial activation events, but instead affects maintenance of inflammatory gene expression several hours after bacterial lipopolysaccharide (LPS) challenge (PubMed:22312129). {ECO:0000250|UniProtKB:Q9NUY8, ECO:0000269|PubMed:22312129, ECO:0000269|PubMed:28823707, ECO:0000269|PubMed:29084197}. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:29084197}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q9NUY8}. Note=Localization to the trans-Golgi (TGN) is regulated by ARL1 and ARL5B/ARL8. ARL1 increases Golgi localization, while ARL5B decreases it. Recruitment to the trans-Golgi network requires the presence of GOLGA1 and GOLGA4, but not that of FAM91A1 (By similarity). Recruited on AP-1-derived vesicles by WDR11 complex (By similarity). {ECO:0000250|UniProtKB:Q9NUY8}. SUBUNIT: Directly interacts with GOLGA1 and GOLGA4 (PubMed:29084197). Interacts with FAM91A1, C17ORF75 and WDR11; the interaction recruits TBC1D23 to AP-1-derived vesicles (PubMed:29084197). Directly interacts with WASHC1 and WASHC2/FAM21 (PubMed:29084197). Interacts with FKBP15 (PubMed:29084197). {ECO:0000269|PubMed:29084197}. +Q9QYC7 VKGC_MOUSE Vitamin K-dependent gamma-carboxylase (EC 4.1.1.90) (Gamma-glutamyl carboxylase) (Peptidyl-glutamate 4-carboxylase) (Vitamin K gamma glutamyl carboxylase) 757 87,195 Chain (1); Disulfide bond (1); Initiator methionine (1); Modified residue (1); Sequence conflict (1); Topological domain (6); Transmembrane (5) TRANSMEM 61 81 Helical. {ECO:0000255}.; TRANSMEM 114 134 Helical. {ECO:0000255}.; TRANSMEM 137 157 Helical. {ECO:0000255}.; TRANSMEM 293 313 Helical. {ECO:0000255}.; TRANSMEM 362 382 Helical. {ECO:0000255}. TOPO_DOM 2 60 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 82 113 Lumenal. {ECO:0000255}.; TOPO_DOM 135 136 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 158 292 Lumenal. {ECO:0000255}.; TOPO_DOM 314 361 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 383 757 Lumenal. {ECO:0000255}. FUNCTION: Mediates the vitamin K-dependent carboxylation of glutamate residues to calcium-binding gamma-carboxyglutamate (Gla) residues with the concomitant conversion of the reduced hydroquinone form of vitamin K to vitamin K epoxide. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Monomer. May interact with CALU. {ECO:0000250}. +Q640P7 TBCC1_MOUSE TBCC domain-containing protein 1 552 62,848 Alternative sequence (2); Chain (1); Domain (1); Frameshift (1); Sequence conflict (1) FUNCTION: Plays a role in the regulation of centrosome and Golgi apparatus positioning, with consequences on cell shape and cell migration. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. Note=Localizes at the spindle midzone, midbody and basal bodies of primary and motile cilia. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain and testis (at protein level). {ECO:0000269|PubMed:20168327}. +P83887 TBG1_MOUSE Tubulin gamma-1 chain (Gamma-1-tubulin) (Gamma-tubulin complex component 1) (GCP-1) 451 51,101 Chain (1); Modified residue (1); Mutagenesis (2); Nucleotide binding (1) FUNCTION: Tubulin is the major constituent of microtubules. The gamma chain is found at microtubule organizing centers (MTOC) such as the spindle poles or the centrosome. Pericentriolar matrix component that regulates alpha/beta chain minus-end nucleation, centrosome duplication and spindle formation (By similarity). {ECO:0000250}. PTM: Phosphorylation at Ser-131 by BRSK1 regulates centrosome duplication, possibly by mediating relocation of gamma-tubulin and its associated proteins from the cytoplasm to the centrosome. {ECO:0000269|PubMed:19648910}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:19648910}. Note=Mainly localizes to the centrosome, but a fraction is found outside of the centrosome in the cytoplasm. SUBUNIT: Interacts with TUBGCP2 and TUBGCP3 (By similarity). Interacts with B9D2 (PubMed:18287022). Interacts with CDK5RAP2; the interaction is leading to centrosomal localization of TUBG1 and CDK5RAP2 (By similarity). Interacts with PIFO (PubMed:20643351). Interacts with SAS6 and NUP62 at the centrosome (By similarity). {ECO:0000250|UniProtKB:P23258, ECO:0000269|PubMed:18287022, ECO:0000269|PubMed:20643351}. +Q7TMM9 TBB2A_MOUSE Tubulin beta-2A chain 445 49,907 Chain (1); Cross-link (2); Modified residue (8); Nucleotide binding (1) FUNCTION: Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain (By similarity). {ECO:0000250}. PTM: Some glutamate residues at the C-terminus are polyglycylated, resulting in polyglycine chains on the gamma-carboxyl group. Glycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Both modifications can coexist on the same protein on adjacent residues, and lowering polyglycylation levels increases polyglutamylation, and reciprocally. The precise function of polyglycylation is still unclear. {ECO:0000269|PubMed:19524510}.; PTM: Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (PubMed:15890843). Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity by SPAST increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold (By similarity). {ECO:0000250|UniProtKB:Q71U36, ECO:0000269|PubMed:15890843}.; PTM: Phosphorylated on Ser-172 by CDK1 during the cell cycle, from metaphase to telophase, but not in interphase. This phosphorylation inhibits tubulin incorporation into microtubules. {ECO:0000250|UniProtKB:Q13885}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. SUBUNIT: Part of a complex composed at least of ASCL2, EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; this complex may have a histone H3-specific methyltransferase activity (By similarity). Dimer of alpha and beta chains. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells. Interacts with ZNRF1. {ECO:0000250, ECO:0000269|PubMed:19737534}. +Q9CWF2 TBB2B_MOUSE Tubulin beta-2B chain 445 49,953 Chain (1); Cross-link (2); Modified residue (9); Nucleotide binding (1); Sequence conflict (2) FUNCTION: Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. Plays a critical role in proper axon guidance in both central and peripheral axon tracts. Implicated in neuronal migration. {ECO:0000250, ECO:0000250|UniProtKB:Q9BVA1}. PTM: Some glutamate residues at the C-terminus are polyglycylated, resulting in polyglycine chains on the gamma-carboxyl group. Glycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Both modifications can coexist on the same protein on adjacent residues, and lowering polyglycylation levels increases polyglutamylation, and reciprocally. The precise function of polyglycylation is still unclear. {ECO:0000269|PubMed:19524510}.; PTM: Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (PubMed:15890843). Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity by SPAST increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold (By similarity). {ECO:0000250|UniProtKB:Q71U36, ECO:0000269|PubMed:15890843}.; PTM: Phosphorylated on Ser-172 by CDK1 during the cell cycle, from metaphase to telophase, but not in interphase. This phosphorylation inhibits tubulin incorporation into microtubules. {ECO:0000250|UniProtKB:Q9BVA1}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9BVA1}. SUBUNIT: Dimer of alpha and beta chains. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells. {ECO:0000250|UniProtKB:Q9BVA1}. TISSUE SPECIFICITY: Strong expression is detected in the developing cortex and peripheral nervous system, as well as in the adult cerebellum, hippocampus and olfactory bulb. {ECO:0000269|PubMed:19465910}. +Q60707 TBX2_MOUSE T-box transcription factor TBX2 (T-box protein 2) 711 75,081 Chain (1); Compositional bias (2); DNA binding (1); Frameshift (1); Modified residue (5); Region (1); Sequence conflict (6) FUNCTION: Involved in the transcriptional regulation of genes required for mesoderm differentiation. Probably plays a role in limb pattern formation. Acts as a negative regulator of PML function in cellular senescence. May be required for cardiac atrioventricular canal formation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00201}. SUBUNIT: Interacts with PML. {ECO:0000250}. DOMAIN: The repression domain 1 (RD1) is necessary for its interaction with PML. {ECO:0000250}. TISSUE SPECIFICITY: In adults, highest levels in lung. Also found in heart, kidney, and ovary. +Q9CQ66 TC1D2_MOUSE Tctex1 domain-containing protein 2 144 16,499 Chain (1) FUNCTION: Required for proper retrograde ciliary transport. {ECO:0000250|UniProtKB:Q8WW35}. SUBUNIT: Interacts with WDR60. {ECO:0000250|UniProtKB:Q8WW35}. +P11985 TC1D3_MOUSE Tctex1 domain-containing protein 3 (LC2) (T-complex testis-specific protein 2) (T-complex testis-specific protein 3) (T-complex-associated testis-expressed protein 3) (Tcte-3) (T-complex-associated testis-expressed protein 4) (TCTEX-4) (TCTEX-2) 191 22,379 Alternative sequence (1); Chain (1); Natural variant (11); Sequence conflict (3) FUNCTION: May be an accessory component of axonemal dynein and cytoplasmic dynein 1. Candidate for involvement in male sterility. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305|PubMed:7601308}. Cytoplasmic granule {ECO:0000269|PubMed:7601308}. Membrane {ECO:0000269|PubMed:7601308}; Peripheral membrane protein {ECO:0000269|PubMed:7601308}. Note=Found on the surface of sperm tail. Stored in cytoplasmic granules during spermatogenesis. SUBUNIT: Interacts with CSNK2B. {ECO:0000269|PubMed:12849985}. TISSUE SPECIFICITY: Expressed in testis (at protein level). Expressed at the pachyten stage of the first meiotic division and in later haploid spermatogenic stages. {ECO:0000269|PubMed:11278908, ECO:0000269|PubMed:12849985, ECO:0000269|PubMed:1718647, ECO:0000269|PubMed:3653077, ECO:0000269|PubMed:7601308}. DISEASE: Note=Could be involved in transmission ratio distortion (trd) in mouse t-haplotype which causes male sterility. +Q8BNE1 TCAF1_MOUSE TRPM8 channel-associated factor 1 (TRP channel-associated factor 1) 924 102,735 Alternative sequence (3); Chain (1); Domain (1); Erroneous initiation (1); Sequence conflict (3) FUNCTION: Positively regulates the plasma membrane cation channel TRPM8 activity. Involved in the recruitment of TRPM8 to the cell surface. Promotes prostate cancer cell migration inhibition in a TRPM8-dependent manner. {ECO:0000250|UniProtKB:Q9Y4C2}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9Y4C2}. Note=Colocalizes with TRPM8 on the plasma membrane. {ECO:0000250|UniProtKB:Q9Y4C2}. SUBUNIT: Interacts with TRPM8 (via N-terminus and C-terminus domains); the interaction inhibits TRPM8 channel activity. Interacts with TRPV6. {ECO:0000250|UniProtKB:Q9Y4C2}. DOMAIN: The C-terminal region is necessary for the channel activity stimulation. {ECO:0000250|UniProtKB:Q9Y4C2}. +P70326 TBX5_MOUSE T-box transcription factor TBX5 (T-box protein 5) 518 57,832 Beta strand (11); Chain (1); DNA binding (1); Helix (5); Modified residue (1); Sequence conflict (2) FUNCTION: DNA-binding protein that regulates the transcription of several genes and is involved in heart development and limb pattern formation. Binds to the core DNA motif of NPPA promoter. {ECO:0000250|UniProtKB:Q99593}. PTM: Acetylation at Lys-339 by KAT2A and KAT2B promotes nuclear retention. {ECO:0000250|UniProtKB:Q99593}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q99593, ECO:0000255|PROSITE-ProRule:PRU00201}. Cytoplasm {ECO:0000250|UniProtKB:Q99593}. Note=Shuttles between the cytoplasm and the nucleus. Acetylation at Lys-339 promotes nuclear retention. {ECO:0000250|UniProtKB:Q99593}. SUBUNIT: Monomer. Homodimer (via the T-box); binds DNA as homodimer. Interacts (via the T-box) with NKX2-5 (via the homeobox); this complex binds DNA. Interacts with GATA4. Interacts with KAT2A and KAT2B. {ECO:0000250|UniProtKB:Q99593}. DOMAIN: The T-Box domain binds to double-stranded DNA. {ECO:0000250|UniProtKB:Q99593}. +P80318 TCPG_MOUSE T-complex protein 1 subunit gamma (TCP-1-gamma) (CCT-gamma) (Matricin) (mTRiC-P5) 545 60,630 Beta strand (9); Chain (1); Cross-link (4); Disulfide bond (1); Erroneous initiation (1); Helix (5); Modified residue (10); Sequence conflict (9) FUNCTION: Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin. {ECO:0000250|UniProtKB:P49368}. PTM: The N-terminus is blocked. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. SUBUNIT: Component of the chaperonin-containing T-complex (TRiC), a heterooligomeric complex of about 850 to 900 kDa that forms two stacked rings, 12 to 16 nm in diameter. Interacts with PACRG (By similarity). Interacts with DNAAF4 (PubMed:23872636). {ECO:0000250|UniProtKB:P49368, ECO:0000269|PubMed:23872636}. +Q61390 TCPW_MOUSE T-complex protein 1 subunit zeta-2 (TCP-1-zeta-2) (CCT-zeta-2) (Cctz-2) 531 58,185 Chain (1); Sequence conflict (1) FUNCTION: Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. {ECO:0000250|UniProtKB:Q92526}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q92526}. SUBUNIT: Component of the chaperonin-containing T-complex (TRiC), a heterooligomeric complex of about 850 to 900 kDa that forms two stacked rings, 12 to 16 nm in diameter. {ECO:0000250|UniProtKB:Q92526}. TISSUE SPECIFICITY: Testis specific. +P80315 TCPD_MOUSE T-complex protein 1 subunit delta (TCP-1-delta) (A45) (CCT-delta) 539 58,066 Chain (1); Modified residue (10); Sequence conflict (3) FUNCTION: Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin. {ECO:0000250|UniProtKB:P50991}. PTM: The N-terminus is blocked. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23807208}. Melanosome {ECO:0000250|UniProtKB:P50991}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:23807208}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:23807208}. SUBUNIT: Component of the chaperonin-containing T-complex (TRiC), a heterooligomeric complex of about 850 to 900 kDa that forms two stacked rings, 12 to 16 nm in diameter. Interacts with PACRG (By similarity). Interacts with DNAAF4 (PubMed:23872636). {ECO:0000250|UniProtKB:P50991, ECO:0000269|PubMed:23872636}. +Q91VL8 TE2IP_MOUSE Telomeric repeat-binding factor 2-interacting protein 1 (TERF2-interacting telomeric protein 1) (TRF2-interacting telomeric protein 1) (Repressor/activator protein 1 homolog) (RAP1 homolog) 393 43,353 Chain (1); Compositional bias (1); Cross-link (6); Domain (2); Erroneous initiation (1); Initiator methionine (1); Modified residue (7); Motif (1); Sequence conflict (2) FUNCTION: Acts both as a regulator of telomere function and as a transcription regulator. Involved in the regulation of telomere length and protection as a component of the shelterin complex (telosome). In contrast to other components of the shelterin complex, it is dispensible for telomere capping and does not participate in the protection of telomeres against non-homologous end-joining (NHEJ)-mediated repair. Instead, it is required to negatively regulate telomere recombination and is essential for repressing homology-directed repair (HDR), which can affect telomere length. Does not bind DNA directly: recruited to telomeric double-stranded 5'-TTAGGG-3' repeats via its interaction with TERF2. Independently of its function in telomeres, also acts as a transcription regulator: recruited to extratelomeric 5'-TTAGGG-3' sites via its association with TERF2 or other factors, and regulates gene expression. When cytoplasmic, associates with the I-kappa-B-kinase (IKK) complex and acts as a regulator of the NF-kappa-B signaling by promoting IKK-mediated phosphorylation of RELA/p65, leading to activate expression of NF-kappa-B target genes. {ECO:0000269|PubMed:20339076, ECO:0000269|PubMed:20622869, ECO:0000269|PubMed:20622870}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20622870}. Cytoplasm {ECO:0000269|PubMed:20622870}. Chromosome {ECO:0000269|PubMed:20622869}. Chromosome, telomere {ECO:0000269|PubMed:20622869}. Note=Associates with chromosomes, both at telomeres and in extratelomeric sites (PubMed:20622869). Also exists as a cytoplasmic form, where it associates with the IKK complex (PubMed:20622870). {ECO:0000269|PubMed:20622869, ECO:0000269|PubMed:20622870}. SUBUNIT: Homodimer. Component of the shelterin complex (telosome) composed of TERF1, TERF2, TINF2, TERF2IP ACD and POT1. Binds to TERF2 (but not TERF1) with its C-terminus. Interacts with SLX4/BTBD12 (By similarity). Interacts with TERF2; the interaction is direct. Does not interact with TERF1. Associates with the I-kappa-B-kinase (IKK) core complex, composed of CHUK, IKBKB and IKBKG. {ECO:0000250, ECO:0000269|PubMed:20339076, ECO:0000269|PubMed:20622870}. +Q717B2 TDPZ2_MOUSE TD and POZ domain-containing protein 2 364 41,537 Chain (1); Domain (2); Sequence conflict (15) +Q3U132 TESP1_MOUSE Protein TESPA1 (Thymocyte-expressed positive selection-associated protein 1) 458 51,768 Alternative sequence (3); Chain (1); Erroneous initiation (2); Modified residue (1) FUNCTION: May play a role in the regulation of inositol 1,4,5-trisphosphate receptor-mediated Ca(2+) release and mitochondrial Ca(2+) uptake via the mitochondria-associated endoplasmic reticulum membrane (MAM) compartment (By similarity). Required for the development and maturation of T-cells, its function being essential for the late stages of thymocyte development. Plays a role in T-cell antigen receptor (TCR)-mediated activation of the ERK and NFAT signaling pathways, possibly by serving as a scaffolding protein that promotes the assembly of the LAT signalosome in thymocytes. {ECO:0000250, ECO:0000269|PubMed:22561606}. PTM: May be phosphorylated in response to store-operated Ca(+2) entry. {ECO:0000269|PubMed:23541577}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A2RU30}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:23650607}. Note=May localize to mitochondria-associated endoplasmic reticulum membrane (MAM). {ECO:0000250|UniProtKB:A2RU30}. SUBUNIT: Interacts with PLCG1 and GRB2; the association is increased with prolonged stimulation of the TCR and may facilitate the assembly of the LAT signalosome (By similarity). Interacts with ITPR1 and ITPR3. Interacts with HSPA9 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in lymphoid tissues, with highest expression levels detected in thymus and lower levels in spleen and lymph nodes (at protein level). Detected in CD4(+) and CD8(+) T-cells, B-cells and mast cells. Not detected in monocytes/macrophages. {ECO:0000269|PubMed:22561606, ECO:0000269|PubMed:23650607}. +Q9DA60 TEX44_MOUSE Testis-expressed protein 44 530 56,574 Chain (1); Erroneous initiation (1); Modified residue (1); Sequence conflict (5) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q53QW1}. +Q8CFK2 TF3B_MOUSE Transcription factor IIIB 90 kDa subunit (TFIIIB90) (mTFIIIB90) (B-related factor 1) (BRF-1) 676 73,799 Chain (1); Metal binding (3); Modified residue (3); Repeat (2); Zinc finger (1) FUNCTION: General activator of RNA polymerase which utilizes different TFIIIB complexes at structurally distinct promoters. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: TFIIIB comprises at least the TATA-binding protein (TBP) and the B-related factor 1 (BRF1/TFIIIB90). Interacts with BDP1 (By similarity). {ECO:0000250}. +Q62296 TEAD4_MOUSE Transcriptional enhancer factor TEF-3 (ETF-related factor 2) (ETFR-2) (TEA domain family member 4) (TEAD-4) (TEF-1-related factor 1) (TEF-1-related factor FR-19) (RTEF-1) 427 48,028 Alternative sequence (1); Beta strand (15); Chain (1); DNA binding (1); Erroneous initiation (1); Helix (6); Motif (1); Sequence caution (1); Sequence conflict (1); Turn (4) FUNCTION: Transcription factor which plays a key role in the Hippo signaling pathway, a pathway involved in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein MST1/MST2, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Acts by mediating gene expression of YAP1 and WWTR1/TAZ, thereby regulating cell proliferation, migration and epithelial mesenchymal transition (EMT) induction. Binds specifically and non-cooperatively to the Sph and GT-IIC 'enhansons' (5'-GTGGAATGT-3') and activates transcription. Binds to the M-CAT motif (By similarity). Might play a role in the embryonic development of skeletal muscle. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with WWTR1/TAZ (By similarity). Interacts with YAP1. {ECO:0000250, ECO:0000269|PubMed:20123908}. TISSUE SPECIFICITY: Preferentially expressed in lung and in skeletal muscle. +Q9CR81 TEX12_MOUSE Testis-expressed protein 12 123 13,958 Chain (1) TISSUE SPECIFICITY: Testis specific. Expressed only in male germ cells. +Q8K0H5 TAF10_MOUSE Transcription initiation factor TFIID subunit 10 (Transcription initiation factor TFIID 30 kDa subunit) (TAF(II)30) (TAFII-30) (TAFII30) (mTAFII30) 218 21,841 Chain (1); Initiator methionine (1); Modified residue (5); Motif (1); Sequence conflict (2) FUNCTION: TAFs are components of the transcription factor IID (TFIID) complex, PCAF histone acetylase complex and TBP-free TAFII complex (TFTC). TIIFD is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. May regulate cyclin E expression. {ECO:0000269|PubMed:10469660}. PTM: Monomethylated at Lys-189 by SETD7, leading to increased affinity for RNA polymerase II. {ECO:0000250|UniProtKB:Q12962}.; PTM: Lysine deamination at Lys-189 to form allysine is mediated by LOXL2. Allysine formation by LOXL2 results in release of TAF10 from promoters, leading to inhibition of TFIID-dependent transcription. {ECO:0000250|UniProtKB:Q12962}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q12962}. SUBUNIT: TFIID and PCAF are composed of TATA binding protein (TBP) and a number of TBP-associated factors (TAFs). TBP is not part of TFTC. Component of the PCAF complex, at least composed of TADA2L/ADA2, TADA3L/ADA3, SUPT3H, TAF5L, TAF6L, TAF9, TAF10, TAF12 and TRRAP. Component of the TFTC-HAT complex, at least composed of TAF5L, TAF6L, TADA3L, SUPT3H, TAF2, TAF4, TAF5, GCN5L2/GCN5, TAF10 and TRRAP. Component of the STAGA transcription coactivator-HAT complex, at least composed of SUPT3H, GCN5L2, TAF5L, TAF6L, SUPT7L, TADA3L, TAD1L, TAF10, TAF12, TRRAP and TAF9. The STAGA core complex is associated with a subcomplex required for histone deubiquitination composed of ATXN7L3, ENY2 and USP22 (By similarity). Interacts with TAF3 (PubMed:11438666). Interacts with LOXL2 (By similarity). {ECO:0000250|UniProtKB:Q12962, ECO:0000269|PubMed:11438666}. DOMAIN: The [KR]-[STA]-K motif is specifically recognized by the SETD7 methyltransferase. {ECO:0000250|UniProtKB:Q12962}. +Q93092 TALDO_MOUSE Transaldolase (EC 2.2.1.2) 337 37,387 Active site (1); Beta strand (8); Chain (1); Helix (19); Modified residue (7); Turn (3) Carbohydrate degradation; pentose phosphate pathway; D-glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage): step 2/3. FUNCTION: Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. SUBUNIT: Homodimer. {ECO:0000250}. +Q6Y685 TACC1_MOUSE Transforming acidic coiled-coil-containing protein 1 774 83,952 Alternative sequence (2); Chain (1); Coiled coil (1); Domain (2); Initiator methionine (1); Modified residue (11); Motif (1); Region (4) FUNCTION: Likely involved in the processes that promote cell division prior to the formation of differentiated tissues. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O75410}. Nucleus {ECO:0000250|UniProtKB:O75410}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:O75410}. Midbody {ECO:0000250|UniProtKB:O75410}. Note=Nucleus during interphase. Weakly concentrated at centrosomes during mitosis and colocalizes with AURKC at the midbody during cytokinesis. {ECO:0000250|UniProtKB:O75410}. SUBUNIT: Interacts with CH-TOG and YEATS4. Interacts with the AURKA and AURKB and AURKC. Interacts with LSM7, TDRD7 and SNRPG. Interacts with GCN5L2 and PCAF (By similarity). {ECO:0000250}. +Q8C176 TAF2_MOUSE Transcription initiation factor TFIID subunit 2 (TBP-associated factor 150 kDa) (Transcription initiation factor TFIID 150 kDa subunit) (TAF(II)150) (TAFII-150) (TAFII150) 1104 126,997 Chain (1); Compositional bias (3); Modified residue (5) FUNCTION: Transcription factor TFIID is one of the general factors required for accurate and regulated initiation by RNA polymerase II. TFIID is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. It requires core promoter-specific cofactors for productive transcription stimulation. TAF2 stabilizes TFIID binding to core promoter (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of transcription factor TFIID which is composed of TBP and a number of TBP-associated factors. Interacts with TAF2C1. Component of the TFTC-HAT complex (By similarity). {ECO:0000250}. +P61216 TAF13_MOUSE Transcription initiation factor TFIID subunit 13 (Transcription initiation factor TFIID 18 kDa subunit) (TAF(II)18) (TAFII-18) (TAFII18) 124 14,287 Chain (1); Domain (1) FUNCTION: Component of the DNA-binding general RNA polymerase II transcription factor IID complex (TFIID). TFIID plays a critical role in the regulation of gene transcription in eukaryotic cells (By similarity). {ECO:0000250|UniProtKB:Q15543}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15543}. SUBUNIT: TFIID is composed of TATA binding protein (TBP) and a number of TBP-associated factors (TAFs). Interacts with TBP, and more strongly with TAF10 and TAF11 (By similarity). {ECO:0000250|UniProtKB:Q15543}. DOMAIN: The binding of TAF10 and TAF11 requires distinct domains of TAF13. {ECO:0000250|UniProtKB:Q15543}. +Q5HZG4 TAF3_MOUSE Transcription initiation factor TFIID subunit 3 (140 kDa TATA box-binding protein-associated factor) (TBP-associated factor 3) (Transcription initiation factor TFIID 140 kDa subunit) (TAF(II)140) (TAF140) (TAFII-140) (TAFII140) 932 105,115 Alternative sequence (2); Beta strand (6); Chain (1); Compositional bias (5); Cross-link (2); Erroneous initiation (1); Helix (2); Modified residue (12); Sequence conflict (2); Turn (2); Zinc finger (1) FUNCTION: Transcription factor TFIID is one of the general factors required for accurate and regulated initiation by RNA polymerase II. TFIID is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. Required in complex with TBPL2 for the differentiation of myoblasts into myocytes. The complex replaces TFIID at specific promoters at an early stage in the differentiation process. {ECO:0000269|PubMed:17704303}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17704303}. SUBUNIT: Belongs to the TFIID complex which is composed of TATA binding protein (TBP) and a number of TBP-associated factors (TAFs). Interacts with TAF10 via histone fold. Interacts with TAF13, TBP, SAP130 and GCN5L2 (By similarity). Interacts with TBPL2. {ECO:0000250, ECO:0000269|PubMed:11438666, ECO:0000269|PubMed:17704303, ECO:0000269|PubMed:18682226}. DOMAIN: The PHD-type zinc finger mediates binding to histone H3 methyllysine at position 4 (H3K4me3). +Q5F2E8 TAOK1_MOUSE Serine/threonine-protein kinase TAO1 (EC 2.7.11.1) (Thousand and one amino acid protein 1) 1001 116,050 Active site (1); Binding site (1); Chain (1); Coiled coil (2); Compositional bias (1); Domain (1); Erroneous initiation (2); Modified residue (5); Nucleotide binding (1) FUNCTION: Serine/threonine-protein kinase involved in various processes such as p38/MAPK14 stress-activated MAPK cascade, DNA damage response and regulation of cytoskeleton stability. Phosphorylates MAP2K3, MAP2K6 and MARK2. Acts as an activator of the p38/MAPK14 stress-activated MAPK cascade by mediating phosphorylation and subsequent activation of the upstream MAP2K3 and MAP2K6 kinases. Involved in G-protein coupled receptor signaling to p38/MAPK14. In response to DNA damage, involved in the G2/M transition DNA damage checkpoint by activating the p38/MAPK14 stress-activated MAPK cascade, probably by mediating phosphorylation of MAP2K3 and MAP2K6. Acts as a regulator of cytoskeleton stability by phosphorylating 'Thr-208' of MARK2, leading to activate MARK2 kinase activity and subsequent phosphorylation and detachment of MAPT/TAU from microtubules. Also acts as a regulator of apoptosis: regulates apoptotic morphological changes, including cell contraction, membrane blebbing and apoptotic bodies formation via activation of the MAPK8/JNK cascade (By similarity). {ECO:0000250}. PTM: Proteolytically processed by caspase-3 (CASP3).; PTM: Autophosphorylated (By similarity). Phosphorylated by ATM in response to DNA damage. Phosphorylated by LRRK2. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Self-associates. Interacts with MAP2K3. Interacts with SPRED1 and TESK1. Interacts with MAP3K7 (By similarity). {ECO:0000250}. +Q9JJZ2 TBA8_MOUSE Tubulin alpha-8 chain (Alpha-tubulin 8) 449 50,052 Chain (1); Nucleotide binding (1); Sequence conflict (1) FUNCTION: Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. PTM: Some glutamate residues at the C-terminus are polyglycylated, resulting in polyglycine chains on the gamma-carboxyl group. Glycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Both modifications can coexist on the same protein on adjacent residues, and lowering polyglycylation levels increases polyglutamylation, and reciprocally. The precise function of polyglycylation is still unclear. {ECO:0000269|PubMed:19524510}.; PTM: Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (PubMed:15890843). Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity by SPAST increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold (By similarity). {ECO:0000250|UniProtKB:Q71U36, ECO:0000269|PubMed:15890843}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SUBUNIT: Dimer of alpha and beta chains. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells. TISSUE SPECIFICITY: Expressed at highest levels in the testis, followed by skeletal and heart muscle. Expressed at low levels in the developing brain. {ECO:0000269|PubMed:20466094}. +P68369 TBA1A_MOUSE Tubulin alpha-1A chain (Alpha-tubulin 1) (Alpha-tubulin isotype M-alpha-1) (Tubulin alpha-1 chain) [Cleaved into: Detyrosinated tubulin alpha-1A chain] 451 50,136 Chain (2); Modified residue (5); Nucleotide binding (1); Sequence conflict (5); Site (1) FUNCTION: Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. PTM: Some glutamate residues at the C-terminus are polyglycylated, resulting in polyglycine chains on the gamma-carboxyl group. Glycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Both modifications can coexist on the same protein on adjacent residues, and lowering polyglycylation levels increases polyglutamylation, and reciprocally. The precise function of polyglycylation is still unclear. {ECO:0000269|PubMed:19524510}.; PTM: Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (PubMed:1967194, PubMed:15890843). Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity by SPAST increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold (By similarity). {ECO:0000250|UniProtKB:Q71U36, ECO:0000269|PubMed:15890843, ECO:0000269|PubMed:1967194}.; PTM: Acetylation of alpha chains at Lys-40 is located inside the microtubule lumen. This modification has been correlated with increased microtubule stability, intracellular transport and ciliary assembly. {ECO:0000250|UniProtKB:Q71U36}.; PTM: Methylation of alpha chains at Lys-40 is found in mitotic microtubules and is required for normal mitosis and cytokinesis contributing to genomic stability. {ECO:0000250|UniProtKB:P68363}.; PTM: Nitration of Tyr-451 is irreversible and interferes with normal dynein intracellular distribution. {ECO:0000250|UniProtKB:Q71U36}.; PTM: Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (VASH1 or VASH2) and tubulin tyrosine ligase (TTL), respectively. {ECO:0000269|PubMed:16954346, ECO:0000269|PubMed:19564401, ECO:0000269|PubMed:26446751, ECO:0000269|PubMed:27102488, ECO:0000269|PubMed:29146868}.; PTM: Tubulin alpha-1A chain: Tyrosination promotes microtubule interaction with CAP-Gly domain-containing proteins such as CLIP1, CLIP2 and DCTN1 (PubMed:16954346, PubMed:19564401). Tyrosination regulates the initiation of dynein-dynactin motility via interaction with DCTN1, which brings the dynein-dynactin complex into contact with microtubules. In neurons, tyrosinated tubulins mediate the initiation of retrograde vesicle transport (By similarity). {ECO:0000250|UniProtKB:Q71U36, ECO:0000269|PubMed:16954346, ECO:0000269|PubMed:19564401}.; PTM: Detyrosinated tubulin alpha-1A chain: Detyrosination is involved in metaphase plate congression by guiding chromosomes during mitosis: detyrosination promotes interaction with CENPE, promoting pole-proximal transport of chromosomes toward the equator (By similarity). Detyrosination increases microtubules-dependent mechanotransduction in dystrophic cardiac and skeletal muscle (PubMed:26446751). In cardiomyocytes, detyrosinated microtubules are required to resist to contractile compression during contraction: detyrosination promotes association with desmin (DES) at force-generating sarcomeres, leading to buckled microtubules and mechanical resistance to contraction (PubMed:27102488). {ECO:0000250|UniProtKB:Q71U36, ECO:0000269|PubMed:26446751, ECO:0000269|PubMed:27102488}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SUBUNIT: Dimer of alpha and beta chains. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells. TISSUE SPECIFICITY: Ubiquitously expressed, although primarily in lung and brain. {ECO:0000269|PubMed:3785200}. +Q9D1E6 TBCB_MOUSE Tubulin-folding cofactor B (Cytoskeleton-associated protein 1) (Cytoskeleton-associated protein CKAPI) (Tubulin-specific chaperone B) 244 27,386 Beta strand (16); Chain (1); Domain (1); Helix (4); Modified residue (6); Sequence conflict (1); Turn (2) FUNCTION: Binds to alpha-tubulin folding intermediates after their interaction with cytosolic chaperonin in the pathway leading from newly synthesized tubulin to properly folded heterodimer (By similarity). Involved in regulation of tubulin heterodimer dissociation (PubMed:17184771). May function as a negative regulator of axonal growth (PubMed:17217416). {ECO:0000250|UniProtKB:Q99426, ECO:0000269|PubMed:17184771, ECO:0000269|PubMed:17217416}. PTM: Phosphorylation by PAK1 is required for normal function. {ECO:0000250|UniProtKB:Q99426}.; PTM: Ubiquitinated in the presence of GAN which targets it for degradation by the proteasome. {ECO:0000250|UniProtKB:Q99426}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17217416}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17217416}. Note=Colocalizes with microtubules. In differentiated neurons, located in the cytoplasm. In differentiating neurons, accumulates at the growth cone. {ECO:0000269|PubMed:17217416}. SUBUNIT: Supercomplex made of cofactors A to E. Cofactors A and D function by capturing and stabilizing tubulin in a quasi-native conformation. Cofactor E binds to the cofactor D-tubulin complex; interaction with cofactor C then causes the release of tubulin polypeptides that are committed to the native state (By similarity). Cofactors B and E can form a heterodimer which binds to alpha-tubulin and enhances their ability to dissociate tubulin heterodimers (PubMed:17184771). Interacts with GAN. Interacts with DCTN1 (By similarity). {ECO:0000250|UniProtKB:Q99426, ECO:0000269|PubMed:17184771}. TISSUE SPECIFICITY: Widely expressed with highest levels in brain. Broadly distributed throughout the neonate brain but restricted mainly to ependymary cells in the adult brain where it is concentrated in the cilia. {ECO:0000269|PubMed:17217416}. +P29037 TBP_MOUSE TATA-box-binding protein (TATA sequence-binding protein) (TATA-binding factor) (TATA-box factor) (Transcription initiation factor TFIID TBP subunit) 316 34,709 Chain (1); Compositional bias (1); Natural variant (1); Repeat (2); Sequence conflict (2) FUNCTION: General transcription factor that functions at the core of the DNA-binding multiprotein factor TFIID. Binding of TFIID to the TATA box is the initial transcriptional step of the pre-initiation complex (PIC), playing a role in the activation of eukaryotic genes transcribed by RNA polymerase II. Component of a BRF2-containing transcription factor complex that regulates transcription mediated by RNA polymerase III. Component of the transcription factor SL1/TIF-IB complex, which is involved in the assembly of the PIC (pre-initiation complex) during RNA polymerase I-dependent transcription. The rate of PIC formation probably is primarily dependent on the rate of association of SL1 with the rDNA promoter. SL1 is involved in stabilization of nucleolar transcription factor 1/UBTF on rDNA. {ECO:0000250|UniProtKB:P20226}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P20226}. SUBUNIT: Binds DNA as monomer. Belongs to the TFIID complex together with the TBP-associated factors (TAFs). Part of a TFIID-containing RNA polymerase II pre-initiation complex that is composed of TBP and at least GTF2A1, GTF2A2, GTF2E1, GTF2E2, GTF2F1, GTF2H2, GTF2H3, GTF2H4, GTF2H5, GTF2B, TCEA1, ERCC2, ERCC3, TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13 (By similarity). Component of the transcription factor SL1/TIF-IB complex, composed of TBP and at least TAF1A, TAF1B, TAF1C and TAF1D. Association of TBP to form either TFIID or SL1/TIF-IB appears to be mutually exclusive. Interacts with TAF1A, TAF1B and TAF1C (PubMed:9050847). Interacts with TFIIB, NCOA6, DRAP1, DR1 and ELF3. Interacts with SPIB, SNAPC1, SNAPC2 and SNAPC4 (By similarity). Interacts with UTF1 (PubMed:9524124). Interacts with BRF2; this interaction promotes recruitment of BRF2 to TATA box-containing promoters. Interacts with UBTF (By similarity). Interacts with GPBP1 (PubMed:14612417). Interacts with CITED2 (PubMed:10593900). Interacts with ATF7IP (Probable). Interacts with LLPH (PubMed:26961175). Interacts with HSF1 (via transactivation domain) (By similarity). Interacts with GTF2B (via C-terminus); this interaction with promoter-bound TBP guides RNA polymerase II into the pre-initiation complex (PIC) (By similarity). {ECO:0000250|UniProtKB:P20226, ECO:0000269|PubMed:10593900, ECO:0000269|PubMed:14612417, ECO:0000269|PubMed:26961175, ECO:0000269|PubMed:9050847, ECO:0000269|PubMed:9524124, ECO:0000305}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:16412700}. +P70324 TBX3_MOUSE T-box transcription factor TBX3 (T-box protein 3) 741 79,160 Alternative sequence (1); Chain (1); DNA binding (2); Modified residue (8); Sequence conflict (5) FUNCTION: Transcriptional repressor involved in developmental processes. Probably plays a role in limb pattern formation. Acts as a negative regulator of PML function in cellular senescence (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00201}. SUBUNIT: Interacts with PML. {ECO:0000250}. TISSUE SPECIFICITY: In adults, highest levels in lung. Also found in brain, heart, kidney, liver and ovary. +P70325 TBX4_MOUSE T-box transcription factor TBX4 (T-box protein 4) 552 61,101 Chain (1); DNA binding (1); Modified residue (1); Sequence conflict (4) FUNCTION: Involved in the transcriptional regulation of genes required for mesoderm differentiation. Probably plays a role in limb pattern formation. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00201}. +P10711 TCEA1_MOUSE Transcription elongation factor A protein 1 (Transcription elongation factor S-II protein 1) (Transcription elongation factor TFIIS.o) 301 33,880 Alternative sequence (1); Chain (1); Cross-link (1); Domain (2); Modified residue (5); Sequence caution (1); Zinc finger (1) FUNCTION: Necessary for efficient RNA polymerase II transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by S-II allows the resumption of elongation from the new 3'-terminus. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Associates with UBR5 and forms a transcription regulatory complex made of CDK9, RNAP II, UBR5 and TFIIS/TCEA1 that can stimulates target gene transcription by recruiting their promoters (By similarity). Interacts with EAF2. {ECO:0000250, ECO:0000269|PubMed:12761297}. +O08784 TCOF_MOUSE Treacle protein (Treacher Collins syndrome protein homolog) 1320 135,001 Chain (1); Compositional bias (9); Cross-link (8); Domain (1); Modified residue (48); Region (1); Repeat (10); Sequence conflict (2) FUNCTION: Nucleolar protein that acts as a regulator of RNA polymerase I by connecting RNA polymerase I with enzymes responsible for ribosomal processing and modification. Required for neural crest specification: following monoubiquitination by the BCR(KBTBD8) complex, associates with NOLC1 and acts as a platform to connect RNA polymerase I with enzymes responsible for ribosomal processing and modification, leading to remodel the translational program of differentiating cells in favor of neural crest specification. {ECO:0000250|UniProtKB:Q13428}. PTM: Ubiquitinated. Monoubiquitination by the BCR(KBTBD8) complex promotes the formation of a NOLC1-TCOF1 complex that acts as a platform to connect RNA polymerase I with enzymes responsible for ribosomal processing and modification, leading to remodel the translational program of differentiating cells in favor of neural crest specification. {ECO:0000250|UniProtKB:Q13428}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q13428}. SUBUNIT: Heterodimer; heterodimerizes with NOLC1 following monoubiquitination. Part of a large pre-ribosomal ribonucleoprotein (RNP) complex, that consists of at least 62 ribosomal proteins, 45 nonribosomal proteins and both pre-rRNA and mature rRNA species. Within this complex directly interacts with NOP56 in an RNA-independent manner. {ECO:0000250|UniProtKB:Q13428}. TISSUE SPECIFICITY: Ubiquitous in adult and embryonic tissues. {ECO:0000269|PubMed:9299440}. +P42932 TCPQ_MOUSE T-complex protein 1 subunit theta (TCP-1-theta) (CCT-theta) 548 59,555 Chain (1); Cross-link (6); Initiator methionine (1); Modified residue (11) FUNCTION: Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin. {ECO:0000250|UniProtKB:P50990}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P50990}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P50990}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:23807208}. SUBUNIT: Component of the chaperonin-containing T-complex (TRiC), a heterooligomeric complex of about 850 to 900 kDa that forms two stacked rings, 12 to 16 nm in diameter. Interacts with PACRG (By similarity). Interacts with DNAAF4 (PubMed:23872636). {ECO:0000250|UniProtKB:P50990, ECO:0000269|PubMed:23872636}. +Q01755 TCP11_MOUSE T-complex protein 11 (Testis-specific protein PBS13) 566 61,970 Chain (1); Compositional bias (1); Modified residue (1); Transmembrane (1) TRANSMEM 393 412 Helical. {ECO:0000255}. FUNCTION: Plays a role in the process of sperm capacitation and acrosome reactions (PubMed:9322250, PubMed:9820206). Probable receptor for the putative fertilization-promoting peptide (FPP) at the sperm membrane that may modulate the activity of the adenylyl cyclase cAMP pathway (PubMed:9322250, PubMed:9820206). {ECO:0000269|PubMed:9322250, ECO:0000269|PubMed:9820206}. PTM: Constitutively phosphorylated on serine, threonine and tyrosine residues within the head and tail regions of noncapacitated spermatozoa (PubMed:27105888). Phosphorylation on tyrosine residues increases upon sperm capacitation within the acrosomal region in a protein kinase A (PKA)-dependent signaling pathway (PubMed:27105888). {ECO:0000269|PubMed:27105888}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:27105888, ECO:0000269|PubMed:9322250}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:27105888, ECO:0000269|PubMed:9322250}. Note=Localizes on the acrosomal cap region of acrosome-intact, but not acrosome-reacted sperm (PubMed:9322250). Colocalizes with MROH2B and PRKACA on the acrosome and tail regions in round spermatids and spermatozoa regardless of the capacitation status of the sperm (PubMed:27105888). {ECO:0000269|PubMed:27105888, ECO:0000269|PubMed:9322250}. SUBUNIT: Found in a complex at least composed of MROH2B isoform 2, PRKACA isoform 2 and TCP11 (PubMed:27105888). Interacts with MROH2B isoform 2 (PubMed:27105888). Interacts with PRKACA isoform 2 (PubMed:27105888). Interacts with ODF1 (via leucine zipper motif) (By similarity). {ECO:0000250|UniProtKB:Q8WWU5, ECO:0000269|PubMed:27105888}. TISSUE SPECIFICITY: Testis-specific (PubMed:1893875). Expressed in mature epididymal spermatozoa (at protein level) (PubMed:9322250). {ECO:0000269|PubMed:1893875, ECO:0000269|PubMed:9322250}. +P80314 TCPB_MOUSE T-complex protein 1 subunit beta (TCP-1-beta) (CCT-beta) 535 57,477 Chain (1); Cross-link (1); Initiator methionine (1); Modified residue (6); Sequence conflict (2) FUNCTION: Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin. {ECO:0000250|UniProtKB:P78371}. PTM: The N-terminus is blocked. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P78371}. SUBUNIT: Component of the chaperonin-containing T-complex (TRiC), a heterooligomeric complex of about 850 to 900 kDa that forms two stacked rings, 12 to 16 nm in diameter. Interacts with PACRG. Interacts with FLCN. {ECO:0000250|UniProtKB:P78371}. +P20293 TBXT_MOUSE T-box transcription factor T (Brachyury protein) (Protein T) 436 47,440 Chain (1); DNA binding (1) FUNCTION: Involved in the transcriptional regulation of genes required for mesoderm formation and differentiation (PubMed:7588606). Binds to a palindromic site (called T site) and activates gene transcription when bound to such a site (PubMed:8344258, PubMed:7588606). {ECO:0000269|PubMed:7588606, ECO:0000269|PubMed:8344258}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:7588606}. SUBUNIT: Monomer. Binds DNA as a monomer. {ECO:0000269|PubMed:8344258}. DISEASE: Note=Embryo lacking the T gene fail to form the notochord, the entire posterior region and the allantois, and die at about 10 days of gestation. +Q8R3L2 TCF25_MOUSE Transcription factor 25 (TCF-25) (Nuclear localized protein 1) 676 76,685 Alternative sequence (6); Chain (1); Erroneous initiation (2); Frameshift (1); Modified residue (1); Sequence conflict (18) FUNCTION: May play a role in cell death control. Acts as a transcriptional repressor. Has been shown to repress transcription of SRF in vitro and so may play a role in heart development (By similarity). {ECO:0000250, ECO:0000269|PubMed:18068114}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12107429, ECO:0000269|PubMed:18068114}. Note=Some staining in the cytosol; cytosolic localization is reduced in staurosporine-induced cell death. SUBUNIT: Interacts with XIAP. {ECO:0000269|PubMed:18068114}. DOMAIN: The C-terminal region mediates transcriptional repression. {ECO:0000250}. TISSUE SPECIFICITY: Broadly expressed in the embryo during the early stages of organogenesis with highest levels in dorsal root ganglia and little or no expression in liver and skin. {ECO:0000269|PubMed:12107429}. +Q91W18 TDRD3_MOUSE Tudor domain-containing protein 3 743 82,253 Alternative sequence (2); Beta strand (5); Chain (1); Cross-link (1); Domain (2); Erroneous initiation (4); Helix (1); Modified residue (2); Region (1); Sequence conflict (12); Turn (2) FUNCTION: Scaffolding protein that specifically recognizes and binds dimethylarginine-containing proteins. In nucleus, acts as a coactivator: recognizes and binds asymmetric dimethylation on the core histone tails associated with transcriptional activation (H3R17me2a and H4R3me2a) and recruits proteins at these arginine-methylated loci. In cytoplasm, may play a role in the assembly and/or disassembly of mRNA stress granules and in the regulation of translation of target mRNAs by binding Arg/Gly-rich motifs (GAR) in dimethylarginine-containing proteins (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Predominantly cytoplasmic. Associated with actively translating polyribosomes and with mRNA stress granules (By similarity). {ECO:0000250}. SUBUNIT: Component of mRNA stress granules. Interacts with FMR1, FXR1, FXR2, EWSR1, FUS, SERBP1, EEF1A1 and DDX3X or DDX3Y, and with the small nuclear ribonucleoprotein-associated proteins SNRPB and SNRPN. Interacts with 'Lys-48'-linked tetra-ubiquitin, but not with monoubiquitin or 'Lys-63'-linked ubiquitin chains. May interact with the exon junction complex (EJC) composed at least of CASC3, EIF4A3, MAGOH and RBM8A. Interacts with POLR2A (via the C-terminal domain (CTD)). {ECO:0000250|UniProtKB:Q9H7E2}. DOMAIN: The Tudor domain specifically recognizes and binds asymmetric dimethylation of histone H3 'Arg-17' (H3R17me2a) and histones H4 'Arg-3', 2 tags for epigenetic transcriptional activation. {ECO:0000250}. +Q5VCS6 TDRD5_MOUSE Tudor domain-containing protein 5 1040 116,016 Alternative sequence (1); Chain (1); Domain (4); Modified residue (2); Sequence conflict (4) FUNCTION: Required during spermiogenesis to participate in the repression transposable elements and prevent their mobilization, which is essential for the germline integrity. Probably acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and govern the methylation and subsequent repression of transposons. Required for chromatoid body (CB) assembly. {ECO:0000269|PubMed:21383078}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21383078}. Note=Localizes to chromatoid body (CB) and pi-body (also called intermitochondrial cementin), 2 cytoplasmic ribonucleoprotein granules involved in RNA processing for spermatogenesis. TISSUE SPECIFICITY: Gonad-specific. Mainly expressed in testis. Present at low level in ovary (at protein level). {ECO:0000269|PubMed:15465492, ECO:0000269|PubMed:21383078}. +P61407 TDRD6_MOUSE Tudor domain-containing protein 6 2134 237,914 Chain (1); Domain (6); Modified residue (7) FUNCTION: Involved in spermiogenesis, chromatoid body formation and for proper precursor and mature miRNA expression. {ECO:0000269|PubMed:19345099}. PTM: Undergoes proteolytic cleavage near the C-terminal by an unknown protease during the transition from meiosis I to meiosis II in primary spermatocytes. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17141210, ECO:0000269|PubMed:19345099}. Note=Present in chromatoid body (CB) of spermatids (mammalian counterpart of germplasm, pole plasm or polar granules in Drosophila germ cells), also named processing bodies (P-bodies) in somatic cells. Detected in the multilobular cytoplasmic CBs (also called intermitochondrial cementin) in pachytene spermatocytes and as a single perinuclear CB in haploid round spermatids. Colocalizes in CB with DDX4, PIWIL1, PIWIL2, TDRD1 and TDRD7. SUBUNIT: Found in a mRNP complex, at least composed of TDRD1, TDRD6, TDRD7 and DDX4. Found in a complex, at least composed of PIWIL1, PIWIL2 and TDRD6. Interacts with DDX4 and PIWIL1. Interacts with Tex19.1 and, probably, Tex19.2 (PubMed:28254886). {ECO:0000269|PubMed:17141210, ECO:0000269|PubMed:19345099, ECO:0000269|PubMed:19584108, ECO:0000269|PubMed:19926723, ECO:0000269|PubMed:28254886}. TISSUE SPECIFICITY: Testis specific. Expressed in primary spermatocytes at post natal (PN) day 17.5. Expressed in midpachytene stage of primary spermatocytes at PN16 and in round spermatids at PN22 (at protein level). {ECO:0000269|PubMed:17141210, ECO:0000269|PubMed:19345099, ECO:0000269|PubMed:19926723}. +Q922G7 TEKT2_MOUSE Tektin-2 (Tektin-t) (Testicular tektin) 430 50,311 Chain (1); Coiled coil (2); Sequence conflict (1) FUNCTION: Structural component of ciliary and flagellar microtubules. Plays a key role in the assembly or attachment of the inner dynein arm to microtubules in sperm flagella and tracheal cilia. Forms filamentous polymers in the walls of ciliary and flagellar microtubules. {ECO:0000269|PubMed:15340058}. PTM: Tyrosine phosphorylated. {ECO:0000250|UniProtKB:Q1W6C3}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:15340058}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:10456331}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000269|PubMed:24394471}. Note=Colocalized with CCDC172 at the perinuclear region (PubMed:24394471). {ECO:0000269|PubMed:24394471}. SUBUNIT: May interact with CCDC172. {ECO:0000269|PubMed:24394471}. TISSUE SPECIFICITY: Testis specific. {ECO:0000269|PubMed:10456331}. +Q810U2 TDM1A_MOUSE Transmembrane epididymal protein 1A (Transmembrane epididymal protein 1-1) 305 34,794 Chain (1); Glycosylation (1); Sequence conflict (2); Transmembrane (6) TRANSMEM 4 24 Helical. {ECO:0000255}.; TRANSMEM 54 74 Helical. {ECO:0000255}.; TRANSMEM 124 144 Helical. {ECO:0000255}.; TRANSMEM 159 179 Helical. {ECO:0000255}.; TRANSMEM 187 207 Helical. {ECO:0000255}.; TRANSMEM 223 243 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +G5E8A8 TEKT5_MOUSE Tektin-5 557 62,734 Alternative sequence (1); Chain (1); Coiled coil (1); Region (1); Repeat (6) FUNCTION: May be a structural component of the sperm flagellum. {ECO:0000305|PubMed:20378928}. SUBCELLULAR LOCATION: Cell projection, cilium, flagellum {ECO:0000269|PubMed:20378928}. Note=Appears to be associated with flagellar accessory structures and not the axoneme. {ECO:0000269|PubMed:20378928}. TISSUE SPECIFICITY: Strongly expressed in germ cells of the testis (at protein level). Also detected in brain. {ECO:0000269|PubMed:20378928}. +Q717B4 TDPZ3_MOUSE TD and POZ domain-containing protein 3 365 41,521 Chain (1); Domain (2); Sequence conflict (6) +P30051 TEAD1_MOUSE Transcriptional enhancer factor TEF-1 (NTEF-1) (Protein GT-IIC) (TEA domain family member 1) (TEAD-1) (Transcription factor 13) (TCF-13) 426 47,948 Chain (1); Compositional bias (1); DNA binding (1); Modified residue (2); Region (1); Sequence caution (3); Sequence conflict (2) FUNCTION: Transcription factor which plays a key role in the Hippo signaling pathway, a pathway involved in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein MST1/MST2, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Acts by mediating gene expression of YAP1 and WWTR1/TAZ, thereby regulating cell proliferation, migration and epithelial mesenchymal transition (EMT) induction. Binds specifically and cooperatively to the SPH and GT-IIC 'enhansons' (5'-GTGGAATGT-3') and activates transcription in vivo in a cell-specific manner. The activation function appears to be mediated by a limiting cell-specific transcriptional intermediary factor (TIF). Involved in cardiac development. Binds to the M-CAT motif (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with YAP1 and WWTR1/TAZ. {ECO:0000250}. TISSUE SPECIFICITY: In developing skeletal muscle and myocardium, in mitotic neuroblasts both in the brain and spinal cord. At later stages of embryogenesis expressed in several developing structures such as the olfactory system, the intestine, and the kidney. +Q9D5W8 TEX47_MOUSE Testis-expressed protein 47 253 29,423 Chain (1) +Q9D845 TEX9_MOUSE Testis-expressed protein 9 (Testis-specifically expressed protein 1) (Tsec-1) 387 44,066 Alternative sequence (3); Chain (1); Coiled coil (1) TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:9388464}. +O08523 TECTA_MOUSE Alpha-tectorin 2155 239,433 Alternative sequence (1); Chain (1); Disulfide bond (8); Domain (10); Glycosylation (31); Lipidation (1); Propeptide (1); Sequence conflict (5); Signal peptide (1) FUNCTION: One of the major non-collagenous components of the tectorial membrane (By similarity). The tectorial membrane is an extracellular matrix of the inner ear that covers the neuroepithelium of the cochlea and contacts the stereocilia bundles of specialized sensory hair cells. Sound induces movement of these hair cells relative to the tectorial membrane, deflects the stereocilia and leads to fluctuations in hair-cell membrane potential, transducing sound into electrical signals. {ECO:0000250}. PTM: 3 products of tectorin seem to exist: HMM, MMM and LMM. They may be generated by active processing or the result of proteolysis occurring between intrachain disulfide bonds.; PTM: The presence of a hydrophobic C-terminus preceded by a potential cleavage site strongly suggests that tectorins are synthesized as glycosylphosphatidylinositol-linked, membrane-bound precursors. Tectorins are targeted to the apical surface of the inner ear epithelia by the lipid and proteolytically released into the extracellular compartment. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:9079715}; Lipid-anchor, GPI-anchor {ECO:0000305|PubMed:9079715}; Extracellular side {ECO:0000305|PubMed:9079715}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:9079715}. Note=Found in the non-collagenous matrix of the tectorial membrane. SUBUNIT: May form homomeric filament after self-association or heteromeric filament after association with beta-tectorin. Interacts with CEACAM16 (By similarity). {ECO:0000250}. DOMAIN: Zona pellucida domain may enable to form filaments. TISSUE SPECIFICITY: Cochlea-specific. {ECO:0000269|PubMed:9079715}. +Q3TL26 TFB2M_MOUSE Dimethyladenosine transferase 2, mitochondrial (EC 2.1.1.-) (Mitochondrial 12S rRNA dimethylase 2) (Mitochondrial transcription factor B2) (mTFB2M) (mtTFB2) (S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase 2) 396 45,864 Binding site (3); Chain (1); Sequence conflict (9); Transit peptide (1) FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase which specifically dimethylates mitochondrial 12S rRNA at the conserved stem loop. Also required for basal transcription of mitochondrial DNA, probably via its interaction with POLRMT and TFAM. Stimulates transcription independently of the methyltransferase activity. {ECO:0000269|PubMed:15526033}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. SUBUNIT: Interacts with mitochondrial RNA polymerase POLRMT. Interacts with TFAM (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:12532263}. +Q921Z5 TFIP8_MOUSE Tumor necrosis factor alpha-induced protein 8 (TNF alpha-induced protein 8) 198 22,960 Alternative sequence (2); Chain (1); Coiled coil (1); Helix (9); Sequence conflict (5); Turn (2) FUNCTION: Acts as a negative mediator of apoptosis. Suppresses the TNF-mediated apoptosis by inhibiting caspase-8 activity but not the processing of procaspase-8, subsequently resulting in inhibition of BID cleavage and caspase-3 activation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +Q08639 TFDP1_MOUSE Transcription factor Dp-1 (DRTF1-polypeptide 1) (E2F dimerization partner 1) 410 45,231 Chain (1); Compositional bias (2); DNA binding (1); Modified residue (2); Motif (1); Region (5) FUNCTION: Can stimulate E2F-dependent transcription. Binds DNA cooperatively with E2F family members through the E2 recognition site, 5'-TTTC[CG]CGC-3', found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. The E2F1:DP complex appears to mediate both cell proliferation and apoptosis. Blocks adipocyte differentiation by repressing CEBPA binding to its target gene promoters (PubMed:20176812). {ECO:0000250|UniProtKB:Q14186, ECO:0000269|PubMed:20176812}. PTM: Ubiquitinated by the BCR(KBTBD5) complex, leading to its subsequent degradation. {ECO:0000269|PubMed:25940086}.; PTM: Phosphorylation by E2F1-bound cyclin A-CDK2, in the S phase, inhibits E2F-mediated DNA binding and transactivation. {ECO:0000250|UniProtKB:Q14186}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25940086}. Cytoplasm {ECO:0000269|PubMed:25940086}. Note=Shuttles between the cytoplasm and nucleus and translocates into the nuclear compartment upon heterodimerization with E2F1. {ECO:0000305|PubMed:25940086}. SUBUNIT: Component of the E2F:DP transcription factor complex. Forms heterodimers with E2F family members. The complex can interact with hypophosphorylated retinoblastoma protein RB1 and related proteins (RBL1 and RBL2) that inhibit the E2F transactivation domain. This repression involves recruitment of histone deacetylase (HDAC). During the cell cycle, from mid-to-late G1 phase, RB family members become phosphorylated, detach from the DRTF1/E2F complex to render E2F transcriptionally active. Part of the E2F6.com-1 complex in G0 phase is composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1, RING1, RNF2, MBLR, L3MBTL2 YAF2. Component of the DREAM complex (also named LINC complex) at least composed of E2F4, E2F5, LIN9, LIN37, LIN52, LIN54, MYBL1, MYBL2, RBL1, RBL2, RBBP4, TFDP1 and TFDP2. The complex exists in quiescent cells where it represses cell cycle-dependent genes. It dissociates in S phase when LIN9, LIN37, LIN52 and LIN54 form a subcomplex that binds to MYBL2. The complex TFDP1:E2F1 interacts with CEBPA; the interaction prevents CEBPA binding to target gene promoters and represses its transcriptional activity (By similarity). {ECO:0000250|UniProtKB:Q14186}. +Q04207 TF65_MOUSE Transcription factor p65 (Nuclear factor NF-kappa-B p65 subunit) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 3) 549 60,212 Alternative sequence (1); Beta strand (27); Chain (1); Cross-link (3); Domain (1); Helix (11); Modified residue (19); Motif (2); Mutagenesis (4); Region (3); Sequence conflict (2); Turn (3) FUNCTION: NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The heterodimeric RELA-NFKB1 complex appears to be most abundant one. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. The NF-kappa-B heterodimeric RELA-NFKB1 and RELA-REL complexes, for instance, function as transcriptional activators. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. The inhibitory effect of I-kappa-B on NF-kappa-B through retention in the cytoplasm is exerted primarily through the interaction with RELA. RELA shows a weak DNA-binding site which could contribute directly to DNA binding in the NF-kappa-B complex. Beside its activity as a direct transcriptional activator, it is also able to modulate promoters accessibility to transcription factors and thereby indirectly regulate gene expression (PubMed:29813070). Associates with chromatin at the NF-kappa-B promoter region via association with DDX1. Essential for cytokine gene expression in T-cells (By similarity). The NF-kappa-B homodimeric RELA-RELA complex appears to be involved in invasin-mediated activation of IL-8 expression (By similarity). {ECO:0000250|UniProtKB:Q04206, ECO:0000269|PubMed:21131967, ECO:0000269|PubMed:22244329, ECO:0000269|PubMed:29813070}. PTM: Ubiquitinated, leading to its proteasomal degradation. Degradation is required for termination of NF-kappa-B response (By similarity). {ECO:0000250}.; PTM: Monomethylated at Lys-310 by SETD6. Monomethylation at Lys-310 is recognized by the ANK repeats of EHMT1 and promotes the formation of repressed chromatin at target genes, leading to down-regulation of NF-kappa-B transcription factor activity. Phosphorylation at Ser-311 disrupts the interaction with EHMT1 without preventing monomethylation at Lys-310 and relieves the repression of target genes. {ECO:0000269|PubMed:12881425, ECO:0000269|PubMed:21131967}.; PTM: Phosphorylation on Ser-534 stimulates acetylation on Lys-310 and interaction with CBP; the phosphorylated and acetylated forms show enhanced transcriptional activity (By similarity). Phosphorylation at Ser-311 disrupts the interaction with EHMT1 and promotes transcription factor activity. Phosphorylation at Ser-276 by RPS6KA4 and RPS6KA5 promotes its transactivation and transcriptional activities. {ECO:0000250, ECO:0000269|PubMed:12881425, ECO:0000269|PubMed:21131967}.; PTM: Reversibly acetylated; the acetylation seems to be mediated by CBP, the deacetylation by HDAC3 and SIRT2. Acetylation at Lys-122 enhances DNA binding and impairs association with NFKBIA. Acetylation at Lys-310 is required for full transcriptional activity in the absence of effects on DNA binding and NFKBIA association. Acetylation at Lys-310 promotes interaction with BRD4. Acetylation can also lower DNA-binding and results in nuclear export. Interaction with BRMS1 promotes deacetylation of Lys-310. Lys-310 is deacetylated by SIRT2 (By similarity). {ECO:0000250}.; PTM: S-nitrosylation of Cys-38 inactivates the enzyme activity. {ECO:0000269|PubMed:22244329}.; PTM: Sulfhydration at Cys-38 mediates the anti-apoptotic activity by promoting the interaction with RPS3 and activating the transcription factor activity.; PTM: Sumoylation by PIAS3 negatively regulates DNA-bound activated NF-kappa-B. {ECO:0000250}.; PTM: Proteolytically cleaved within a conserved N-terminus region required for base-specific contact with DNA in a CPEN1-mediated manner, and hence inhibits NF-kappa-B transcriptional activity. {ECO:0000250|UniProtKB:Q04206}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21131967}. Cytoplasm {ECO:0000269|PubMed:21131967}. Note=Nuclear, but also found in the cytoplasm in an inactive form complexed to an inhibitor (I-kappa-B) (PubMed:21131967). Colocalized with DDX1 in the nucleus upon TNF-alpha induction (By similarity). Colocalizes with GFI1 in the nucleus after lipopolysaccharide (LPS) stimulation. {ECO:0000250|UniProtKB:Q04206, ECO:0000269|PubMed:21131967}. SUBUNIT: Component of the NF-kappa-B p65-p50 complex. Component of the NF-kappa-B p65-c-Rel complex. Homodimer; component of the NF-kappa-B p65-p65 complex. Component of the NF-kappa-B p65-p52 complex. May interact with ETHE1. Binds AES and TLE1. Interacts with TP53BP2. Binds to and is phosphorylated by the activated form of either RPS6KA4 or RPS6KA5. Interacts with ING4 and this interaction may be indirect. Interacts with CARM1, USP48 and UNC5CL. Interacts with IRAK1BP1. Interacts with NFKBIA. Interacts with GSK3B. Interacts with NFKBIB. Interacts with NFKBIE. Interacts with NFKBIZ. Part of a 70-90 kDa complex at least consisting of CHUK, IKBKB, NFKBIA, RELA, ELP1 and MAP3K14. Interacts with HDAC3; HDAC3 mediates the deacetylation of RELA. Interacts with HDAC1; the interaction requires non-phosphorylated RELA. Interacts with CBP; the interaction requires phosphorylated RELA. Interacts (phosphorylated at 'Thr-254') with PIN1; the interaction inhibits p65 binding to NFKBIA. Interacts with SOCS1. Interacts with MTDH and PHF11. Interacts with NFKBID. Interacts with ARRB2. Interacts with NFKBIA (when phosphorylated), the interaction is direct; phosphorylated NFKBIA is associated with a SCF(BTRC)-like complex lacking CUL1. Interacts with RNF25. Interacts (via C-terminus) with DDX1 (By similarity). Interacts with UFL1 and COMMD1 (By similarity). Interacts with BRMS1; this promotes deacetylation of 'Lys-310'. Interacts (when acetylated at Lys-310) with BRD4; leading to activation of the NF-kappa-B pathway (By similarity). Interacts with EHMT1 (via ANK repeats). Interacts with NOTCH2. Directly interacts with MEN1; this interaction represses NFKB-mediated transactivation (By similarity). Interacts with AKIP1, which promotes the phosphorylation and nuclear retention of RELA (By similarity). Interacts (via the RHD) with GFI1; the interaction, after bacterial lipopolysaccharide (LPS) stimulation, inhibits the transcriptional activity by interfering with the DNA-binding activity to target gene promoter DNA. Interacts with MEFV (By similarity). Interacts with CLOCK. Interacts with FOXP3 (By similarity). Interacts (via N-terminus) with CPEN1; this interaction induces proteolytic cleavage of p65/RELA subunit and inhibition of NF-kappa-B transcriptional activity (By similarity). Interacts with CDK5RAP3; stimulates the interaction of RELA with HDAC1, HDAC2 and HDAC3 thereby inhibiting NF-kappa-B transcriptional activity (By similarity). Interacts with DHX9; this interaction is direct and activates NF-kappa-B-mediated transcription (By similarity). Interacts with TBX21 (PubMed:23616576). Interacts with LRRC25 (By similarity). Interacts with KAT2A (PubMed:25024434). Interacts (via transcriptional activation domain 3) with ZBTB7A; involved in the control by RELA of the accessibility of target gene promoters (PubMed:29813070). {ECO:0000250|UniProtKB:Q04206, ECO:0000269|PubMed:11931770, ECO:0000269|PubMed:15051764, ECO:0000269|PubMed:15485901, ECO:0000269|PubMed:15616592, ECO:0000269|PubMed:18710934, ECO:0000269|PubMed:21131967, ECO:0000269|PubMed:22895791, ECO:0000269|PubMed:23616576, ECO:0000269|PubMed:25024434, ECO:0000269|PubMed:29813070, ECO:0000269|PubMed:8816457, ECO:0000269|PubMed:9990853}. DOMAIN: The transcriptional activation domain 3/TA3 does not participate to the direct transcriptional activity of RELA but is involved in the control by RELA of the accessibility of target gene promoters. Mediates interaction with ZBTB7A. {ECO:0000269|PubMed:29813070}.; DOMAIN: The transcriptional activation domain 1/TA1 and the transcriptional activation domain 2/TA2 have direct transcriptional activation properties (PubMed:29813070). The 9aaTAD motif found within the transcriptional activation domain 2 is a conserved motif present in a large number of transcription factors that is required for their transcriptional transactivation activity (By similarity). {ECO:0000250|UniProtKB:Q04206, ECO:0000269|PubMed:29813070}. +Q62351 TFR1_MOUSE Transferrin receptor protein 1 (TR) (TfR) (TfR1) (Trfr) (CD antigen CD71) 763 85,731 Chain (1); Disulfide bond (2); Domain (1); Glycosylation (5); Lipidation (1); Modified residue (5); Motif (3); Mutagenesis (1); Region (2); Sequence conflict (3); Topological domain (2); Transmembrane (1) TRANSMEM 68 88 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 67 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 89 763 Extracellular. {ECO:0000255}. FUNCTION: Cellular uptake of iron occurs via receptor-mediated endocytosis of ligand-occupied transferrin receptor into specialized endosomes. Endosomal acidification leads to iron release. The apotransferrin-receptor complex is then recycled to the cell surface with a return to neutral pH and the concomitant loss of affinity of apotransferrin for its receptor. Transferrin receptor is necessary for development of erythrocytes and the nervous system (By similarity). Upon stimulation, positively regulates T and B cell proliferation through iron uptake (PubMed:26642240). {ECO:0000250, ECO:0000269|PubMed:10192390, ECO:0000269|PubMed:26642240}. PTM: N- and O-glycosylated, phosphorylated and palmitoylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P02786}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P02786}. Melanosome {ECO:0000250|UniProtKB:P02786}. SUBUNIT: Homodimer; disulfide-linked. Binds one transferrin molecule per subunit. Interacts with SH3BP4 (By similarity). Interacts with STEAP3; facilitates TFRC endocytosis in erythroid precursor cells (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P02786}. +Q64092 TFE3_MOUSE Transcription factor E3 572 61,536 Alternative sequence (2); Chain (1); Cross-link (1); Domain (1); Modified residue (7); Region (2); Sequence conflict (6) FUNCTION: Transcription factor that specifically recognizes and binds E-box sequences (5'-CANNTG-3'). Efficient DNA-binding requires dimerization with itself or with another MiT/TFE family member such as TFEB or MITF. In association with TFEB, activates the expression of CD40L in T-cells, thereby playing a role in T-cell-dependent antibody responses in activated CD4(+) T-cells and thymus-dependent humoral immunity. Specifically recognizes the MUE3 box, a subset of E-boxes, present in the immunoglobulin enhancer. It also binds very well to a USF/MLTF site. {ECO:0000269|PubMed:16936731}. PTM: Sumoylated; does not affect dimerization with MITF. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Homodimer and heterodimer; with TFEB or MITF. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:16936731}. +Q9WTW4 TFEC_MOUSE Transcription factor EC (TFE-C) (mTFEC) 317 35,144 Chain (1); Domain (1); Region (2); Sequence conflict (1) FUNCTION: Transcriptional regulator that acts as a repressor or an activator. Acts as a transcriptional transactivator on the proximal promoter region of the tartrate-resistant acid phosphatase (TRAP) E-box containing promoter. Collaborates with MITF in target gene activation. Acts as a transcriptional repressor on minimal promoter containing element F (that includes an E-box sequence) (By similarity). Binds to element F in an E-box sequence-specific manner (By similarity). Acts as a transcriptional repressor on minimal promoter containing mu E3 enhancer sequence (By similarity). Binds to mu E3 DNA sequence of the immunoglobulin heavy-chain gene enhancer (By similarity). Binds DNA in a homo- or heterodimeric form. {ECO:0000250, ECO:0000269|PubMed:11818452}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}. SUBUNIT: Homodimer. Forms heterodimers with MITF. Interacts with MITF. Forms heterodimers with TFE3 (By similarity). {ECO:0000250}. DOMAIN: Contains an activation domain in the C-terminal region. TISSUE SPECIFICITY: Expressed in osteoclast-like cells (at protein level). Expressed in cells of the mononuclear phagocyte lineage. Expressed in macrophages and in osteoclast-like cells. {ECO:0000269|PubMed:9973413}. +Q8C152 TET5B_MOUSE Terminal nucleotidyltransferase 5B (EC 2.7.7.-) 427 46,998 Chain (1); Erroneous initiation (1); Sequence conflict (2) FUNCTION: Probable nucleotidyltransferase that may act as a non-canonical poly(A) RNA polymerase. {ECO:0000250|UniProtKB:Q96A09}. +P04202 TGFB1_MOUSE Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)] 390 44,310 Chain (2); Disulfide bond (8); Glycosylation (3); Motif (1); Region (3); Signal peptide (1); Site (1) FUNCTION: Transforming growth factor beta-1 proprotein: Precursor of the Latency-associated peptide (LAP) and Transforming growth factor beta-1 (TGF-beta-1) chains, which constitute the regulatory and active subunit of TGF-beta-1, respectively. {ECO:0000250|UniProtKB:P01137}.; FUNCTION: Latency-associated peptide: Required to maintain the Transforming growth factor beta-1 (TGF-beta-1) chain in a latent state during storage in extracellular matrix (PubMed:29909984). Associates non-covalently with TGF-beta-1 and regulates its activation via interaction with 'milieu molecules', such as LTBP1, LRRC32/GARP and LRRC33/NRROS, that control activation of TGF-beta-1 (PubMed:29909984). Interaction with LRRC33/NRROS regulates activation of TGF-beta-1 in macrophages and microglia (PubMed:29909984). Interaction with LRRC32/GARP controls activation of TGF-beta-1 on the surface of activated regulatory T-cells (Tregs) (By similarity). Interaction with integrins (ITGAV:ITGB6 or ITGAV:ITGB8) results in distortion of the Latency-associated peptide chain and subsequent release of the active TGF-beta-1 (PubMed:10025398). {ECO:0000250|UniProtKB:P01137, ECO:0000269|PubMed:10025398, ECO:0000269|PubMed:29909984}.; FUNCTION: Transforming growth factor beta-1: Multifunctional protein that regulates the growth and differentiation of various cell types and is involved in various processes, such as normal development, immune function, microglia function and responses to neurodegeneration (PubMed:22781750, PubMed:29909984). Activation into mature form follows different steps: following cleavage of the proprotein in the Golgi apparatus, Latency-associated peptide (LAP) and Transforming growth factor beta-1 (TGF-beta-1) chains remain non-covalently linked rendering TGF-beta-1 inactive during storage in extracellular matrix (By similarity). At the same time, LAP chain interacts with 'milieu molecules', such as LTBP1, LRRC32/GARP and LRRC33/NRROS that control activation of TGF-beta-1 and maintain it in a latent state during storage in extracellular milieus (PubMed:29909984). TGF-beta-1 is released from LAP by integrins (ITGAV:ITGB6 or ITGAV:ITGB8): integrin-binding to LAP stabilizes an alternative conformation of the LAP bowtie tail and results in distortion of the LAP chain and subsequent release of the active TGF-beta-1 (PubMed:10025398) (By similarity). Once activated following release of LAP, TGF-beta-1 acts by binding to TGF-beta receptors (TGFBR1 and TGFBR2), which transduce signal (By similarity). While expressed by many cells types, TGF-beta-1 only has a very localized range of action within cell environment thanks to fine regulation of its activation by Latency-associated peptide chain (LAP) and 'milieu molecules' (PubMed:29909984). Plays an important role in bone remodeling: acts as a potent stimulator of osteoblastic bone formation, causing chemotaxis, proliferation and differentiation in committed osteoblasts (PubMed:22781750). Can promote either T-helper 17 cells (Th17) or regulatory T-cells (Treg) lineage differentiation in a concentration-dependent manner (PubMed:18368049). At high concentrations, leads to FOXP3-mediated suppression of RORC and down-regulation of IL-17 expression, favoring Treg cell development (PubMed:18368049). At low concentrations in concert with IL-6 and IL-21, leads to expression of the IL-17 and IL-23 receptors, favoring differentiation to Th17 cells (PubMed:18368049). Stimulates sustained production of collagen through the activation of CREB3L1 by regulated intramembrane proteolysis (RIP) (By similarity). Mediates SMAD2/3 activation by inducing its phosphorylation and subsequent translocation to the nucleus. Can induce epithelial-to-mesenchymal transition (EMT) and cell migration in various cell types (By similarity). {ECO:0000250|UniProtKB:P01137, ECO:0000269|PubMed:10025398, ECO:0000269|PubMed:18368049, ECO:0000269|PubMed:22781750, ECO:0000269|PubMed:29909984}. PTM: Transforming growth factor beta-1 proprotein: The precursor proprotein is cleaved in the Golgi apparatus by FURIN to form Transforming growth factor beta-1 (TGF-beta-1) and Latency-associated peptide (LAP) chains, which remain non-covalently linked, rendering TGF-beta-1 inactive. {ECO:0000250|UniProtKB:P01137}.; PTM: Latency-associated peptide: N-glycosylated. Deglycosylation leads to activation of Transforming growth factor beta-1 (TGF-beta-1); mechanisms triggering deglycosylation-driven activation of TGF-beta-1 are however unclear. {ECO:0000250|UniProtKB:P01137}. SUBCELLULAR LOCATION: Latency-associated peptide: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P01137}.; SUBCELLULAR LOCATION: Transforming growth factor beta-1: Secreted {ECO:0000250|UniProtKB:P01137}. SUBUNIT: Homodimer; disulfide-linked (By similarity). Interacts with the serine proteases, HTRA1 and HTRA3: the interaction with either inhibits TGFB1-mediated signaling. The HTRA protease activity is required for this inhibition (PubMed:14973287, PubMed:15206957). May interact with THSD4; this interaction may lead to sequestration by FBN1 microfibril assembly and attenuation of TGFB signaling (PubMed:21880733). Interacts with CD109, DPT and ASPN. Latency-associated peptide: Homodimer; disulfide-linked (By similarity). Latency-associated peptide: Interacts with Transforming growth factor beta-1 (TGF-beta-1) chain; interaction is non-covalent and maintains (TGF-beta-1) in a latent state; each Latency-associated peptide (LAP) monomer interacts with TGF-beta-1 in the other monomer (By similarity). Latency-associated peptide: Interacts with LTBP1; leading to regulate activation of TGF-beta-1 (By similarity). Latency-associated peptide: Interacts with LRRC32/GARP; leading to regulate activation of TGF-beta-1 on the surface of activated regulatory T-cells (Tregs) (By similarity). Latency-associated peptide: Interacts with LRRC33/NRROS; leading to regulate activation of TGF-beta-1 in macrophages and microglia (PubMed:29909984). Latency-associated peptide: Interacts (via cell attachment site) with integrins ITGAV and ITGB6 (ITGAV:ITGB6), leading to release of the active TGF-beta-1 (PubMed:10025398). Latency-associated peptide: Interacts with NREP; the interaction results in a decrease in TGFB1 autoinduction (PubMed:14985127). Latency-associated peptide: Interacts with HSP90AB1; inhibits latent TGFB1 activation. Transforming growth factor beta-1: Homodimer; disulfide-linked. Transforming growth factor beta-1: Interacts with TGF-beta receptors (TGFBR1 and TGFBR2), leading to signal transduction (By similarity). {ECO:0000250|UniProtKB:P01137, ECO:0000269|PubMed:10025398, ECO:0000269|PubMed:14973287, ECO:0000269|PubMed:14985127, ECO:0000269|PubMed:15206957, ECO:0000269|PubMed:21880733, ECO:0000269|PubMed:29909984}. DOMAIN: Latency-associated peptide: The 'straitjacket' and 'arm' domains encircle the Transforming growth factor beta-1 (TGF-beta-1) monomers and are fastened together by strong bonding between Lys-56 and Tyr-103/Tyr-104. {ECO:0000250|UniProtKB:P07200}.; DOMAIN: Latency-associated peptide: The cell attachment site motif mediates binding to integrins (ITGAV:ITGB6 or ITGAV:ITGB8). The motif locates to a long loop in the arm domain called the bowtie tail. Integrin-binding stabilizes an alternative conformation of the bowtie tail. Activation by integrin requires force application by the actin cytoskeleton, which is resisted by the 'milieu molecules' (such as LTBP1, LRRC32/GARP and/or LRRC33/NRROS), resulting in distortion of the prodomain and release of the active TGF-beta-1. {ECO:0000250|UniProtKB:P01137}. +Q8R5L3 VPS39_MOUSE Vam6/Vps39-like protein 886 101,693 Alternative sequence (1); Chain (1); Domain (1); Repeat (1) FUNCTION: May play a role in clustering and fusion of late endosomes and lysosomes (By similarity). Regulator of TGF-beta/activin signaling, inhibiting SMAD3- and activating SMAD2-dependent transcription. Acts by interfering with SMAD3/SMAD4 complex formation, this would lead to inhibition of SMAD3-dependent transcription and relieve SMAD3 inhibition of SMAD2-dependent promoters, thus increasing SMAD2-dependent transcription (By similarity). {ECO:0000250|UniProtKB:Q96JC1}.; FUNCTION: Plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport and autophagic pathways. Believed to act in part as a component of the putative HOPS endosomal tethering complex which is proposed to be involved in the Rab5-to-Rab7 endosome conversion probably implicating MON1A/B, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion. The HOPS complex is proposed to be recruited to Rab7 on the late endosomal membrane and to regulate late endocytic, phagocytic and autophagic traffic towards lysosomes. Involved in homotypic vesicle fusions between late endosomes and in heterotypic fusions between late endosomes and lysosomes. Required for fusion of endosomes and autophagosomes with lysosomes (By similarity). {ECO:0000250|UniProtKB:Q96JC1}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96JC1}. Lysosome membrane {ECO:0000250|UniProtKB:Q96JC1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q96JC1}. Late endosome membrane {ECO:0000250|UniProtKB:Q96JC1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q96JC1}. Late endosome {ECO:0000250|UniProtKB:Q96JC1}. Lysosome {ECO:0000250|UniProtKB:Q96JC1}. Note=Colocalizes with TGFBR1 and TGFBR2 in cytoplasmic vesicular structures and most prominently in cortical vesicles. {ECO:0000250|UniProtKB:Q96JC1}. SUBUNIT: Homooligomer (By similarity). Interacts with TGFBR2 and, less efficiently, with TGFBR1; interaction with TGFBR2 is independent of the receptor kinase activity and of the presence of TGF-beta. Also interacts with ACVR2B, but not with BMPR2. Interacts with SMAD4, preferentially following TGF-beta treatment (By similarity). Component of the putative homotypic fusion and vacuole protein sorting (HOPS) complex; the core of which composed of the class C Vps proteins VPS11, VPS16, VPS18 and VPS33A, is associated with VPS39 and VPS41. Interacts with PLEKHM2; involved in VPS39 recruitment to ARL8B-containing lysosomes (By similarity). Associates with adaptor protein complex 3 (AP-3) and clathrin:AP-3 complexes (PubMed:21411634). {ECO:0000250|UniProtKB:Q96JC1, ECO:0000269|PubMed:21411634}. +P27090 TGFB2_MOUSE Transforming growth factor beta-2 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-2 (TGF-beta-2)] 414 47,589 Beta strand (10); Chain (2); Disulfide bond (5); Glycosylation (3); Helix (2); Sequence conflict (1); Signal peptide (1) FUNCTION: Transforming growth factor beta-2 proprotein: Precursor of the Latency-associated peptide (LAP) and Transforming growth factor beta-2 (TGF-beta-2) chains, which constitute the regulatory and active subunit of TGF-beta-2, respectively. {ECO:0000250|UniProtKB:P01137, ECO:0000250|UniProtKB:P04202}.; FUNCTION: Latency-associated peptide: Required to maintain the Transforming growth factor beta-2 (TGF-beta-2) chain in a latent state during storage in extracellular matrix. Associates non-covalently with TGF-beta-2 and regulates its activation via interaction with 'milieu molecules', such as LTBP1 and LRRC32/GARP, that control activation of TGF-beta-2. {ECO:0000250|UniProtKB:P01137, ECO:0000250|UniProtKB:P04202}.; FUNCTION: Transforming growth factor beta-2: Multifunctional protein that regulates various processes such as angiogenesis and heart development (By similarity). Activation into mature form follows different steps: following cleavage of the proprotein in the Golgi apparatus, Latency-associated peptide (LAP) and Transforming growth factor beta-2 (TGF-beta-2) chains remain non-covalently linked rendering TGF-beta-2 inactive during storage in extracellular matrix (By similarity). At the same time, LAP chain interacts with 'milieu molecules', such as LTBP1 and LRRC32/GARP, that control activation of TGF-beta-2 and maintain it in a latent state during storage in extracellular milieus (By similarity). Once activated following release of LAP, TGF-beta-2 acts by binding to TGF-beta receptors (TGFBR1 and TGFBR2), which transduce signal (By similarity). {ECO:0000250|UniProtKB:P01137, ECO:0000250|UniProtKB:P04202, ECO:0000250|UniProtKB:P61812}. PTM: Transforming growth factor beta-2 proprotein: The precursor proprotein is cleaved in the Golgi apparatus to form Transforming growth factor beta-2 (TGF-beta-2) and Latency-associated peptide (LAP) chains, which remain non-covalently linked, rendering TGF-beta-2 inactive. {ECO:0000250|UniProtKB:P01137}. SUBCELLULAR LOCATION: Latency-associated peptide: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P01137}.; SUBCELLULAR LOCATION: Transforming growth factor beta-2: Secreted {ECO:0000250|UniProtKB:P01137}. SUBUNIT: Interacts with the serine proteases, HTRA1 and HTRA3 (PubMed:15206957, PubMed:14973287). Interacts with ASPN (By similarity). Interacts with MFAP5 (PubMed:23963447). Latency-associated peptide: Interacts with Transforming growth factor beta-2 (TGF-beta-2) chain; interaction is non-covalent and maintains (TGF-beta-2) in a latent state (By similarity). Latency-associated peptide: Interacts with LRRC32/GARP; leading to regulate activation of TGF-beta-2 (By similarity). Latency-associated peptide: Interacts with NREP; the interaction results in a decrease in TGFB2 autoinduction (PubMed:14985127). Transforming growth factor beta-2: Homodimer; disulfide-linked (By similarity). Transforming growth factor beta-2: Interacts with TGF-beta receptors (TGFBR1 and TGFBR2), leading to signal transduction (By similarity). {ECO:0000250|UniProtKB:P01137, ECO:0000250|UniProtKB:P61812, ECO:0000269|PubMed:14973287, ECO:0000269|PubMed:14985127, ECO:0000269|PubMed:15206957, ECO:0000269|PubMed:23963447}. +P97390 VPS45_MOUSE Vacuolar protein sorting-associated protein 45 (mVps45) 570 65,053 Chain (1); Modified residue (2); Sequence conflict (1) FUNCTION: May play a role in vesicle-mediated protein trafficking from the Golgi stack through the trans-Golgi network. SUBCELLULAR LOCATION: Golgi apparatus membrane; Peripheral membrane protein. Endosome membrane; Peripheral membrane protein. Note=Associated with Golgi/endosomal vesicles and the trans-Golgi network. SUBUNIT: Interacts with ZFYVE20 (By similarity). Interacts with STX6. {ECO:0000250, ECO:0000269|PubMed:9045632}. +Q6PDZ2 TAF1C_MOUSE TATA box-binding protein-associated factor RNA polymerase I subunit C (RNA polymerase I-specific TBP-associated factor 95 kDa) (TAFI95) (TATA box-binding protein-associated factor 1C) (TBP-associated factor 1C) (Transcription initiation factor SL1/TIF-IB subunit C) 836 92,023 Chain (1); Modified residue (1); Sequence conflict (2) FUNCTION: Component of the transcription factor SL1/TIF-IB complex, which is involved in the assembly of the PIC (preinitiation complex) during RNA polymerase I-dependent transcription. The rate of PIC formation probably is primarily dependent on the rate of association of SL1/TIF-IB with the rDNA promoter. SL1/TIF-IB is involved in stabilization of nucleolar transcription factor 1/UBTF on rDNA. Formation of SL1/TIF-IB excludes the association of TBP with TFIID subunits. Recruits RNA polymerase I to the rRNA gene promoter via interaction with RRN3 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9451438}. SUBUNIT: Component of the transcription factor SL1/TIF-IB complex, composed of TBP and at least TAF1A, TAF1B, TAF1C and TAF1D. In the complex interacts directly with TBP, TAF1A and TAF1B. Interaction of the SL1/TIF-IB subunits with TBP excludes interaction of TBP with the transcription factor IID (TFIID) subunits. Interacts with MYC and RRN3. Interacts with p53/TP53; the interaction prevents the association of SL1/TIF-IB with UBTF and represses RNA polymerase I transcription (By similarity). {ECO:0000250}. +P50518 VATE1_MOUSE V-type proton ATPase subunit E 1 (V-ATPase subunit E 1) (V-ATPase 31 kDa subunit) (p31) (Vacuolar proton pump subunit E 1) 226 26,157 Chain (1); Initiator methionine (1); Modified residue (2); Sequence conflict (10) FUNCTION: Subunit of the peripheral V1 complex of vacuolar ATPase essential for assembly or catalytic function. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'' and d). Interacts with ALDOC. Interacts with RAB11B (By similarity). Interacts with RABL2/RABL2A; binds preferentially to GTP-bound RABL2. {ECO:0000250, ECO:0000269|PubMed:23055941}. TISSUE SPECIFICITY: Expressed within the midpiece of sperm tail (at protein level). Ubiquitous. {ECO:0000269|PubMed:11872743, ECO:0000269|PubMed:23055941}. +Q6A039 TBC12_MOUSE TBC1 domain family member 12 696 76,810 Chain (1); Coiled coil (1); Domain (1); Erroneous initiation (1); Modified residue (5) FUNCTION: May act as a GTPase-activating protein for Rab family protein(s). +Q8R3D1 TBC13_MOUSE TBC1 domain family member 13 400 46,453 Chain (1); Domain (1) FUNCTION: Acts as a GTPase-activating protein for RAB35. Together with RAB35 may be involved in regulation of insulin-induced glucose transporter SLC2A4/GLUT4 translocation to the plasma membrane in adipocytes. {ECO:0000269|PubMed:22762500}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:22762500}. Cytoplasm {ECO:0000269|PubMed:22762500}. SUBUNIT: Interacts with RAB1A and RAB10; in a GTP-dependent manner. {ECO:0000269|PubMed:22762500}. TISSUE SPECIFICITY: Expressed in adipocytes. {ECO:0000269|PubMed:22762500}. +Q9D6F9 TBB4A_MOUSE Tubulin beta-4A chain (Tubulin beta-4 chain) 444 49,586 Chain (1); Modified residue (2); Nucleotide binding (1); Sequence conflict (8) FUNCTION: Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. PTM: Some glutamate residues at the C-terminus are polyglycylated, resulting in polyglycine chains on the gamma-carboxyl group. Glycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Both modifications can coexist on the same protein on adjacent residues, and lowering polyglycylation levels increases polyglutamylation, and reciprocally. The precise function of polyglycylation is still unclear. {ECO:0000269|PubMed:19524510}.; PTM: Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (PubMed:15890843). Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity by SPAST increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold (By similarity). {ECO:0000250|UniProtKB:Q71U36, ECO:0000269|PubMed:15890843}.; PTM: Phosphorylated on Ser-172 by CDK1 during the cell cycle, from metaphase to telophase, but not in interphase. This phosphorylation inhibits tubulin incorporation into microtubules. {ECO:0000250|UniProtKB:P04350}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SUBUNIT: Dimer of alpha and beta chains. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells. DOMAIN: The highly acidic C-terminal region may bind cations such as calcium. +Q8VHI5 VITRN_MOUSE Vitrin (Akhirin) 650 70,699 Alternative sequence (1); Chain (1); Disulfide bond (2); Domain (3); Glycosylation (1); Sequence conflict (22); Signal peptide (1) FUNCTION: Promotes matrix assembly and cell adhesiveness (PubMed:18757743). Plays a role in spinal cord formation by regulating the proliferation and differentiation of neural stem cells (PubMed:25331329). {ECO:0000269|PubMed:18757743, ECO:0000269|PubMed:25331329}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:18757743}. SUBUNIT: Binds dermatan sulfate and chondroitin sulfate. {ECO:0000269|PubMed:18757743}. +Q922F4 TBB6_MOUSE Tubulin beta-6 chain 447 50,090 Chain (1); Modified residue (2); Nucleotide binding (1) FUNCTION: Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. {ECO:0000250|UniProtKB:P02557}. PTM: Some glutamate residues at the C-terminus are polyglycylated, resulting in polyglycine chains on the gamma-carboxyl group. Glycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Both modifications can coexist on the same protein on adjacent residues, and lowering polyglycylation levels increases polyglutamylation, and reciprocally. The precise function of polyglycylation is still unclear. {ECO:0000269|PubMed:19524510}.; PTM: Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (PubMed:15890843). Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity by SPAST increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold (By similarity). {ECO:0000250|UniProtKB:Q71U36, ECO:0000269|PubMed:15890843}.; PTM: Phosphorylated on Ser-172 by CDK1 during the cell cycle, from metaphase to telophase, but not in interphase. This phosphorylation inhibits tubulin incorporation into microtubules. {ECO:0000250|UniProtKB:Q9BUF5}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. SUBUNIT: Dimer of alpha and beta chains. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells. DOMAIN: The highly acidic C-terminal region may bind cations such as calcium. +Q69ZT9 TBC30_MOUSE TBC1 domain family member 30 766 84,893 Chain (1); Coiled coil (1); Domain (1); Erroneous initiation (1); Frameshift (1); Modified residue (1); Sequence conflict (2) FUNCTION: GTPase-activating protein (GAP) with broad specificity. Acts as a GAP for RAB3A. Also exhibits significant GAP activity toward RAB22A, RAB27A, and RAB35 in vitro (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. +Q8BHJ5 TBL1R_MOUSE F-box-like/WD repeat-containing protein TBL1XR1 (Nuclear receptor corepressor/HDAC3 complex subunit TBLR1) (TBL1-related protein 1) (Transducin beta-like 1X-related protein 1) 514 55,661 Beta strand (32); Chain (1); Compositional bias (1); Cross-link (1); Domain (2); Helix (1); Initiator methionine (1); Modified residue (2); Mutagenesis (10); Repeat (8); Sequence conflict (3); Turn (3) FUNCTION: F-box-like protein involved in the recruitment of the ubiquitin/19S proteasome complex to nuclear receptor-regulated transcription units. Plays an essential role in transcription activation mediated by nuclear receptors. Probably acts as integral component of the N-Cor corepressor complex that mediates the recruitment of the 19S proteasome complex, leading to the subsequent proteasomal degradation of N-Cor complex, thereby allowing cofactor exchange, and transcription activation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the N-Cor repressor complex, at least composed of NCOR1, NCOR2, HDAC3, TBL1X, TBL1XR1, CORO2A and GPS2. Probable component of some E3 ubiquitin ligase complex. Interacts with histones H2B and H4 (By similarity). Interacts with MECP2; bridges interaction between MECP2 and NCOR1 (PubMed:28348241). {ECO:0000250|UniProtKB:Q9BZK7, ECO:0000269|PubMed:28348241}. DOMAIN: The F-box-like domain is related to the F-box domain, and apparently displays the same function as component of ubiquitin E3 ligase complexes. {ECO:0000250}. +Q9R099 TBL2_MOUSE Transducin beta-like protein 2 442 49,584 Chain (1); Cross-link (1); Modified residue (1); Repeat (7); Sequence conflict (2) +Q8C4J7 TBL3_MOUSE Transducin beta-like protein 3 801 88,266 Chain (1); Cross-link (1); Initiator methionine (1); Modified residue (2); Repeat (13); Sequence conflict (5) SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. +Q9WUN2 TBK1_MOUSE Serine/threonine-protein kinase TBK1 (EC 2.7.11.1) (T2K) (TANK-binding kinase 1) 729 83,425 Active site (1); Beta strand (23); Binding site (1); Chain (1); Coiled coil (2); Cross-link (3); Domain (2); Helix (22); Modified residue (2); Nucleotide binding (1); Region (1); Sequence conflict (3); Turn (3) FUNCTION: Serine/threonine kinase that plays an essential role in regulating inflammatory responses to foreign agents (PubMed:10581243, PubMed:15210742, PubMed:15661922, PubMed:23396211). Following activation of toll-like receptors by viral or bacterial components, associates with TRAF3 and TANK and phosphorylates interferon regulatory factors (IRFs) IRF3 and IRF7 as well as DDX3X (By similarity). This activity allows subsequent homodimerization and nuclear translocation of the IRFs leading to transcriptional activation of pro-inflammatory and antiviral genes including IFNA and IFNB. In order to establish such an antiviral state, TBK1 form several different complexes whose composition depends on the type of cell and cellular stimuli. Thus, several scaffolding molecules including FADD, TRADD, MAVS, AZI2, TANK or TBKBP1/SINTBAD can be recruited to the TBK1-containing-complexes. Under particular conditions, functions as a NF-kappa-B effector by phosphorylating NF-kappa-B inhibitor alpha/NFKBIA, IKBKB or RELA to translocate NF-Kappa-B to the nucleus. Restricts bacterial proliferation by phosphorylating the autophagy receptor OPTN/Optineurin on 'Ser-177', thus enhancing LC3 binding affinity and antibacterial autophagy (By similarity). Phosphorylates SMCR8 component of the C9orf72-SMCR8 complex, promoting autophagosome maturation (By similarity). Phosphorylates and activates AKT1. Seems to play a role in energy balance regulation by sustaining a state of chronic, low-grade inflammation in obesity, wich leads to a negative impact on insulin sensitivity. {ECO:0000250|UniProtKB:Q9UHD2, ECO:0000269|PubMed:10581243, ECO:0000269|PubMed:15210742, ECO:0000269|PubMed:15661922, ECO:0000269|PubMed:23396211}. PTM: Autophosphorylation at Ser-172 activates the kinase, and is an essential step for virus-triggered signaling. Phosphorylated by IKBKB/IKKB at Ser-172. Phosphorylation requires homodimerization and ubiquitination at Lys-30 and Lys-401. Dephosphorylated at Ser-172 by PPM1B and this negatively regulates its role in mediating antiviral response. {ECO:0000250|UniProtKB:Q9UHD2}.; PTM: 'Lys-63'-linked polyubiquitination by MIB1 after RNA virus infection, or by NRDP1 after LPS stimulation at Lys-30 and Lys-401, participates in kinase activation. 'Lys-48'-linked polyubiquitination at Lys-670 by DTX4 leads to proteasomal degradation. 'Lys-48'-linked polyubiquitination by TRAIP also leads to proteasomal degradation. 'Lys-63'-linked polyubiquitination by RNF128 at Lys-30 and Lys-401 leads to the activation of antiviral responses. {ECO:0000250|UniProtKB:Q9UHD2}. SUBCELLULAR LOCATION: Cytoplasm. Note=Upon mitogen stimulation or triggering of the immune system, TBK1 is recruited to the exocyst by EXOC2. {ECO:0000250}. SUBUNIT: Homodimer. Interacts with DDX3X, TIRAP and TRAF2. Part of a ternary complex consisting of TANK, TRAF2 and TBK1. Interacts with AZI2, TANK and TBKBP1; these interactions are mutually exclusive and mediate TBK1 activation. Interacts with GSK3B; this interaction promotes TBK1 self-association and autophosphorylation. Interacts with SIKE1; SIKE1 is associated with TBK1 under physiological condition and dissociated from TBK1 upon viral infection or TLR3 stimulation. Interacts with IRF3 and DDX58/RIG-I. Interacts with CYLD. Interacts with OPTN and TRAF3. Interacts with SRC. Interacts with the exocyst complex subunit SEC5/EXOC2; this interaction is sufficient to trigger TBK1 activity. Interacts with TMEM173/MITA. Interacts with IFIT3 (via N-terminus). Interacts with MAVS only in the presence of IFIT3. Interacts with TICAM1 and this interaction is enhanced in the presence of WDFY1 (By similarity). Interacts with TRIM23 (By similarity). {ECO:0000250|UniProtKB:Q9UHD2, ECO:0000269|PubMed:23746807}. DOMAIN: Comprises A N-terminal kinase domain, a ubiquitin-like domain and a C-terminal coiled-coil region mediating homodimerization. {ECO:0000269|PubMed:23746807}. +A2A9T0 TBKB1_MOUSE TANK-binding kinase 1-binding protein 1 (TBK1-binding protein 1) (Similar to NAP1 TBK1 adapter) 611 67,001 Alternative sequence (2); Chain (1); Coiled coil (2); Compositional bias (3); Modified residue (9); Region (2) FUNCTION: Adapter protein which constitutively binds TBK1 and IKBKE playing a role in antiviral innate immunity. Essential for the efficient induction of IRF-dependent transcription following infection with Sendai virus. {ECO:0000269|PubMed:17568778}. SUBUNIT: Homodimer. May form a heterodimer with NAP1. Interacts with TKB1 and IKBKE. {ECO:0000269|PubMed:17568778}. +P11983 TCPA_MOUSE T-complex protein 1 subunit alpha (TCP-1-alpha) (CCT-alpha) (Tailless complex polypeptide 1A) (TCP-1-A) (Tailless complex polypeptide 1B) (TCP-1-B) 556 60,449 Alternative sequence (2); Chain (1); Frameshift (2); Modified residue (8); Sequence conflict (32) FUNCTION: Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin. {ECO:0000250|UniProtKB:P17987}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P17987}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P17987}. SUBUNIT: Component of the chaperonin-containing T-complex (TRiC), a heterooligomeric complex of about 850 to 900 kDa that forms two stacked rings, 12 to 16 nm in diameter. Interacts with PACRG. Interacts with GBA (By similarity). {ECO:0000250|UniProtKB:P17987}. +P23881 TCEA3_MOUSE Transcription elongation factor A protein 3 (Transcription elongation factor S-II protein 3) (Transcription elongation factor TFIIS.h) 347 38,850 Chain (1); Domain (2); Erroneous translation (1); Helix (5); Modified residue (2); Sequence caution (1); Sequence conflict (3); Zinc finger (1) FUNCTION: Necessary for efficient RNA polymerase II transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by S-II allows the resumption of elongation from the new 3'-terminus. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: Liver, kidney and heart. +Q80VP0 TCPR1_MOUSE Tectonin beta-propeller repeat-containing protein 1 1166 130,266 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (2); Modified residue (6); Repeat (9); Sequence conflict (3) FUNCTION: Tethering factor involved in autophagy. Involved in autophagosome maturation by promoting the autophagosome fusion with lysosomes: acts by associating with both the ATG5-ATG12 conjugate and phosphatidylinositol-3-phosphate (PtdIns(3)P) present at the surface of autophagosomes. Also involved in selective autophagy against bacterial pathogens, by being required for phagophore/preautophagosomal structure biogenesis and maturation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane {ECO:0000250}. Lysosome membrane {ECO:0000250}. Note=Localizes to Lysosome membranes, and binds PtdIns(3)P at the surface of autophagosome. Localizes to autolysosomes, a vesicle formed by the fusion between autophagosomes and lysosomes (By similarity). {ECO:0000250}. SUBUNIT: Interacts with ATG5; the interaction is direct. Interacts with WIPI2. Interacts with the ATG5-ATG12 conjugate, the interaction is however mutually exclusive with ATG16, since it does not interact with ATG12-ATG5-ATG16 complex. DOMAIN: The PH domain mediates the binding to phosphatidylinositol-3-phosphate (PtdIns(3)P). {ECO:0000250}. +Q60756 TCF15_MOUSE Transcription factor 15 (TCF-15) (Meso1) (Paraxis) (Protein bHLH-EC2) 195 20,721 Chain (1); Compositional bias (1); Domain (1); Modified residue (1); Sequence conflict (1) FUNCTION: May function as an early transcriptional regulator, involved in the patterning of the mesoderm and in lineage determination of cell types derived from the mesoderm. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}. SUBUNIT: Efficient DNA binding requires dimerization with another bHLH protein. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in heart and skeletal muscle. +Q99KJ5 TCF19_MOUSE Transcription factor 19-like protein (TCF-19) (SC1 protein homolog) 263 28,068 Chain (1); Domain (1); Modified residue (1); Sequence conflict (3) SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +P63028 TCTP_MOUSE Translationally-controlled tumor protein (TCTP) (21 kDa polypeptide) (p21) (p23) 172 19,462 Chain (1); Domain (1); Modified residue (3); Sequence conflict (5) FUNCTION: Involved in calcium binding and microtubule stabilization. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Seems to self-interact. Interacts with STEAP3 (By similarity). {ECO:0000250}. +Q8K3F7 TDH_MOUSE L-threonine 3-dehydrogenase, mitochondrial (EC 1.1.1.103) 373 41,462 Active site (1); Beta strand (14); Binding site (3); Chain (1); Helix (16); Mutagenesis (5); Nucleotide binding (3); Sequence conflict (5); Transit peptide (1); Turn (1) Amino-acid degradation; L-threonine degradation via oxydo-reductase pathway; glycine from L-threonine: step 1/2. FUNCTION: Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2-amino-3-ketobutyrate, mediating L-threonine catabolism. {ECO:0000269|PubMed:26492815}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q8MIR0}. SUBUNIT: Homodimer. {ECO:0000305|PubMed:26492815}. +Q6X6Z7 TEKT3_MOUSE Tektin-3 490 56,673 Chain (1); Coiled coil (1); Glycosylation (7) FUNCTION: May be a structural component of the sperm flagellum. Required for normal sperm mobility. {ECO:0000269|PubMed:18951373}. PTM: N- and O-glycosylated. {ECO:0000250|UniProtKB:A6H782}.; PTM: May be proteolytically processed during the epididymal transit of spermatozoa. {ECO:0000250|UniProtKB:A6H782}. SUBCELLULAR LOCATION: Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:A6H782, ECO:0000250|UniProtKB:Q4V8G8}. Cytoplasmic vesicle, secretory vesicle, acrosome outer membrane {ECO:0000250|UniProtKB:A6H782, ECO:0000250|UniProtKB:Q4V8G8}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q4V8G8}. Note=In the sperm flagellum, localizes to the periaxonemal region where it associates with the mitochondrial sheath and outer dense fibers (By similarity). Not detected in the central axonemal region of the flagellum (By similarity). Associates with the acrosome membrane in the equatorial segment of the sperm head (By similarity). Also detected just below the plasma membrane in the post-acrosomal region where it might localize to the postacrosomal dense lamina (By similarity). However, other studies report little or no expression in the postacrosomal region (By similarity). Translocates from the postacrosomal region to the equatorial segment after sperm activation (By similarity). Retained in the postacromal region, but not the equatorial segment, following the acrosome reaction (By similarity). Some studies report strong expression in the anterior cap region (By similarity). However, other studies report little or no expression in the acrosomal cap (By similarity). {ECO:0000250|UniProtKB:A6H782, ECO:0000250|UniProtKB:Q4V8G8}. TISSUE SPECIFICITY: Expressed preferentially in testis. Expressed predominantly in late pachytene spermatocytes and early round spermatids. {ECO:0000269|PubMed:14735490}. +Q149S1 TEKT4_MOUSE Tektin-4 (Testicular microtubules-related protein 4) 447 52,045 Chain (1); Coiled coil (2); Sequence conflict (3) FUNCTION: May be a structural component of the sperm flagellum. Contributes to normal sperm motility. {ECO:0000269|PubMed:17244819}. SUBCELLULAR LOCATION: Cell projection, cilium, flagellum {ECO:0000269|PubMed:16596631, ECO:0000269|PubMed:17244819}. Note=Found in the abaxial (convex) surface of outer dense fibers in sperm flagella. {ECO:0000269|PubMed:16596631}. TISSUE SPECIFICITY: Detected in testis, where it is weakly expressed in round spermatids, and strongly expressed in the flagellum of step 16 elongated spermatids (at protein level) (PubMed:17244819). In the sperm flagellum, localizes to the principal piece and midpiece (at protein level) (PubMed:17244819, PubMed:16596631). Specifically expressed in testis; not detected in other tissues tested (PubMed:17244819). {ECO:0000269|PubMed:16596631, ECO:0000269|PubMed:17244819}. +Q6YCH1 TDPZ5_MOUSE TD and POZ domain-containing protein 5 340 38,827 Chain (1); Domain (2) +O35536 TFPI2_MOUSE Tissue factor pathway inhibitor 2 (TFPI-2) 230 26,137 Chain (1); Disulfide bond (9); Domain (3); Glycosylation (2); Signal peptide (1); Site (3) FUNCTION: May play a role in the regulation of plasmin-mediated matrix remodeling. Inhibits trypsin, plasmin, factor VIIa/tissue factor and weakly factor Xa. Has no effect on thrombin (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Finds in a complex with ABCB1, TFPI2 and PPP2R3C; leading to the dephosphorylation of ABCB1. {ECO:0000250|UniProtKB:P48307}. DOMAIN: This inhibitor contains three inhibitory domains. TISSUE SPECIFICITY: Highly expressed in placenta. Also expressed in liver and kidney. +Q3U1J1 TFPT_MOUSE TCF3 fusion partner homolog (Protein FB1) (Protein amida) 259 28,954 Alternative sequence (1); Chain (1); Cross-link (1); Modified residue (6) FUNCTION: Appears to promote apoptosis in a p53/TP53-independent manner. {ECO:0000250}.; FUNCTION: Putative regulatory component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with NOL3; translocates NOL3 into the nucleus and negatively regulated TFPT-induced cell death. Component of the chromatin remodeling INO80 complex; specifically part of a complex module associated with the N-terminus of INO80 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9JMG6}. +Q9R210 TFEB_MOUSE Transcription factor EB 475 52,614 Chain (1); Compositional bias (3); Domain (1); Erroneous initiation (1); Modified residue (11); Region (2) FUNCTION: Transcription factor that specifically recognizes and binds E-box sequences (5'-CANNTG-3'). Efficient DNA-binding requires dimerization with itself or with another MiT/TFE family member such as TFE3 or MITF. In association with TFE3, activates the expression of CD40L in T-cells, thereby playing a role in T-cell-dependent antibody responses in activated CD4(+) T-cells and thymus-dependent humoral immunity. Specifically recognizes and binds the CLEAR-box sequence (5'-GTCACGTGAC-3') present in the regulatory region of many lysosomal genes, leading to activate their expression. It thereby plays a central role in expression of lysosomal genes. Acts as a positive regulator of autophagy by promoting expression of genes involved in autophagy. Specifically recognizes the gamma-E3 box, a subset of E-boxes, present in the heavy-chain immunoglobulin enhancer. Plays a role in the signal transduction processes required for normal vascularization of the placenta. {ECO:0000269|PubMed:16936731, ECO:0000269|PubMed:9806910}. PTM: Sumoylated; does not affect dimerization with MITF. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P19484}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}. Note=Mainly present in the cytoplasm. Under aberrant lysosomal storage conditions, it translocates from the cytoplasm to the nucleus. In macrophages, translocates into the nucleus upon live S.enterica infection. {ECO:0000250|UniProtKB:P19484}. SUBUNIT: Homodimer and heterodimer; with TFE3 or MITF. {ECO:0000250}. DOMAIN: The leucin zipper region is essential for homo- or heterodimerization and high-affinity DNA binding. DNA binding is mediated by the basic region (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:16936731}. +Q62293 TGTP1_MOUSE T-cell-specific guanine nucleotide triphosphate-binding protein 1 (EC 3.6.5.-) (Interferon-gamma-inducible GTPase Ifggb5) 415 47,121 Chain (1); Domain (1); Nucleotide binding (3); Sequence conflict (2) FUNCTION: Involved in innate cell-autonomous resistance to intracellular pathogens, such as Toxoplasma gondii. During avirulent type II T. gondii infection, recruited to the parasitophorous vacuole (PV) membrane, leading to PV vesiculation and rupture, and subsequent digestion of the parasite within the cytosol (PubMed:19265156, PubMed:24563254). Not recruited to virulent type I T. gondii PV membrane (PubMed:19265156). May confer an antiviral state for vesicular stomatitis virus (PubMed:9725230). {ECO:0000269|PubMed:19265156, ECO:0000269|PubMed:24563254, ECO:0000269|PubMed:9725230}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19285957}. Endoplasmic reticulum {ECO:0000269|PubMed:19285957}. Golgi apparatus {ECO:0000269|PubMed:19285957}. Note=In astrocytes stimulated with IFNG or TNF, diffuse cytoplasmic localization decreases and the protein partially relocalizes to the endoplasmic reticulum and Golgi apparatus (PubMed:19285957). Due to sequence similarity with Tgtp2, it is impossible to assign unambiguously experimental data published in the literature to Tgtp1 or Tgtp2 gene (Probable). {ECO:0000269|PubMed:19285957, ECO:0000305|PubMed:22892676}. TISSUE SPECIFICITY: Expressed in thymus and lymph nodes, predominantly T-cells. Not expressed by immature CD4(+) CD8(+) thymocytes (at protein level) (PubMed:7836757). Expressed in IFNG-stimulated macrophages (PubMed:7884320). Expressed at low levels in unstimulated astrocytes (PubMed:19285957). Due to sequence similarity with Tgtp2, it is impossible to assign unambiguously experimental data published in the literature to Tgtp1 or Tgtp2 gene. {ECO:0000269|PubMed:19285957, ECO:0000269|PubMed:7836757, ECO:0000269|PubMed:7884320}. +Q8BI84 TGO1_MOUSE Transport and Golgi organization protein 1 homolog (TANGO1) (Melanoma inhibitory activity protein 3) 1930 213,675 Alternative sequence (4); Chain (1); Coiled coil (3); Compositional bias (4); Domain (1); Glycosylation (2); Intramembrane (1); Modified residue (11); Region (3); Signal peptide (1); Topological domain (3); Transmembrane (1) INTRAMEM 1172 1192 {ECO:0000255}. TRANSMEM 1203 1223 Helical. {ECO:0000255}. TOPO_DOM 25 1171 Lumenal. {ECO:0000255}.; TOPO_DOM 1193 1202 Lumenal. {ECO:0000255}.; TOPO_DOM 1224 1930 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a role in the transport of cargos that are too large to fit into COPII-coated vesicles and require specific mechanisms to be incorporated into membrane-bound carriers and exported from the endoplasmic reticulum. This protein is required for collagen VII (COL7A1) secretion by loading COL7A1 into transport carriers. It may participate in cargo loading of COL7A1 at endoplasmic reticulum exit sites by binding to COPII coat subunits Sec23/24 and guiding SH3-bound COL7A1 into a growing carrier. Does not play a role in global protein secretion and is apparently specific to COL7A1 cargo loading. However, it may participate in secretion of other proteins in cells that do not secrete COL7A1. It is also specifically required for the secretion of lipoproteins by participating in their export from the endoplasmic reticulum. Required for correct assembly of COPII coat components at endoplasmic reticulum exit sites (ERES) and for the localization of SEC16A and membrane-bound ER-resident complexes consisting of MIA2 and PREB/SEC12 to ERES. {ECO:0000250|UniProtKB:Q5JRA6}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q5JRA6}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q5JRA6}. Note=Localizes at endoplasmic reticulum exit sites (ERES), also known as transitional endoplasmic reticulum (tER). SEC16A is required for its proper localization to ERES. After loading of COL7A1 into transport carriers, it is not incorporated into COPII carriers and remains in the endoplasmic reticulum membrane. {ECO:0000250|UniProtKB:Q5JRA6}. SUBUNIT: Interacts with MIA2. Interacts (via SH3 domain) with COL7A1. Interacts with the COPII coat subunits SEC23A, SEC23B and maybe SEC24C. May interact with APOB and MIA2. Interacts with SEC16A. {ECO:0000250|UniProtKB:Q5JRA6}. DOMAIN: The proline-rich domain (PRD) contains repeated PPP motifs. A single PPP motif is necessary and sufficient to mediate interaction with the COPII coat subunits SEC23A and SEC23B. {ECO:0000250|UniProtKB:Q5JRA6}.; DOMAIN: Although 2 transmembrane domains are predicted, it only contains one transmembrane domain. The other predicted transmembrane region is probably a hairpin-type region embedded into the membrane, which does not cross the membrane. It is unclear which of the 2 predicted transmembrane regions is the transmembrane or the hairpin-type region. {ECO:0000250|UniProtKB:Q5JRA6}. +Q9CQ80 VPS25_MOUSE Vacuolar protein-sorting-associated protein 25 (ESCRT-II complex subunit VPS25) 176 20,748 Alternative sequence (1); Chain (1) FUNCTION: Component of the ESCRT-II complex (endosomal sorting complex required for transport II), which is required for multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs. The MVB pathway mediates delivery of transmembrane proteins into the lumen of the lysosome for degradation. The ESCRT-II complex is probably involved in the recruitment of the ESCRT-III complex. The ESCRT-II complex may also play a role in transcription regulation, possibly via its interaction with ELL (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Endosome membrane {ECO:0000250}. Nucleus {ECO:0000250}. Note=Distributes diffusely throughout the cytoplasm and nucleoplasm, but exhibits a punctate distribution on coexpression with CHMP6. {ECO:0000250}. SUBUNIT: Component of a complex at least composed of ELL, SNF8/EAP30, VPS25/EAP20 and VPS36/EAP45 (By similarity). Component of the endosomal sorting complex required for transport II (ESCRT-II), composed of SNF8, VPS36 and 2 copies of VPS25. Interacts with CFTR; the interaction requires misfolded CFTR. Interacts (via C-terminal half) with the ESCRT-III subunit CHMP6 (via N-terminal half) (By similarity). {ECO:0000250}. +Q3U3D7 T131L_MOUSE Transmembrane protein 131-like 1597 175,772 Alternative sequence (3); Chain (1); Compositional bias (2); Erroneous initiation (2); Glycosylation (4); Region (1); Sequence caution (1); Sequence conflict (10); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 870 890 Helical. {ECO:0000255}. TOPO_DOM 41 869 Extracellular. {ECO:0000255}.; TOPO_DOM 891 1597 Cytoplasmic. {ECO:0000255}. FUNCTION: In its membrane-associated form, antagonizes canonical Wnt signaling by triggering lysosome-dependent degradation of Wnt-activated LRP6. Regulates thymocyte proliferation. {ECO:0000250|UniProtKB:A2VDJ0}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:A2VDJ0}; Single-pass type I membrane protein {ECO:0000305}. Endoplasmic reticulum {ECO:0000250|UniProtKB:A2VDJ0}. Cytoplasm {ECO:0000250|UniProtKB:A2VDJ0}. Note=During intrathymic development, resides in punctate cytoplasmic structures in DN1 and DN2 cells. In DN3 cells, found in large crescent-shaped membrane structures, which preferentially localize in cell-to-cell contact zones. {ECO:0000250|UniProtKB:A2VDJ0}. +Q8BTG3 T11L1_MOUSE T-complex protein 11-like protein 1 509 56,332 Chain (1); Modified residue (1) +Q8C1E7 T120A_MOUSE Transmembrane protein 120A (Transmembrane protein induced by tumor necrosis factor alpha) 343 40,751 Chain (1); Glycosylation (1); Topological domain (6); Transmembrane (5) TRANSMEM 136 156 Helical. {ECO:0000255}.; TRANSMEM 163 183 Helical. {ECO:0000255}.; TRANSMEM 191 211 Helical. {ECO:0000255}.; TRANSMEM 274 294 Helical. {ECO:0000255}.; TRANSMEM 306 326 Helical. {ECO:0000255}. TOPO_DOM 1 135 Extracellular. {ECO:0000255}.; TOPO_DOM 157 162 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 184 190 Extracellular. {ECO:0000255}.; TOPO_DOM 212 273 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 295 305 Extracellular. {ECO:0000255}.; TOPO_DOM 327 343 Cytoplasmic. {ECO:0000255}. FUNCTION: Necessary for efficient adipogenesis (PubMed:26024229). {ECO:0000269|PubMed:26024229}. SUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000269|PubMed:20091084}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Homooligomer and heterooligomer with TMEM120B. {ECO:0000269|PubMed:26024229}. TISSUE SPECIFICITY: Highly expressed in white adipose tissue (at protein level). Highly expressed in brown adipose tissue and expressed at low levels in liver. {ECO:0000269|PubMed:26024229}. +Q80X71 T106B_MOUSE Transmembrane protein 106B 275 31,172 Chain (1); Glycosylation (5); Initiator methionine (1); Lipidation (1); Modified residue (1); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 98 118 Helical. {ECO:0000255}. TOPO_DOM 2 97 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 119 275 Lumenal. {ECO:0000255}. FUNCTION: Involved in dendrite morphogenesis and maintenance by regulating lysosomal trafficking via its interaction with MAP6. May act by inhibiting retrograde transport of lysosomes along dendrites. Required for dendrite branching (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250}; Single-pass type II membrane protein. Lysosome membrane {ECO:0000250}; Single-pass type II membrane protein. Membrane {ECO:0000250|UniProtKB:Q9NUM4}; Lipid-anchor {ECO:0000250|UniProtKB:Q9NUM4}. SUBUNIT: Interacts with MAP6. {ECO:0000250}. +Q9D1R1 T126B_MOUSE Complex I assembly factor TMEM126B, mitochondrial (Transmembrane protein 126B) 230 25,444 Chain (1); Transmembrane (4) TRANSMEM 70 92 Helical. {ECO:0000255}.; TRANSMEM 107 126 Helical. {ECO:0000255}.; TRANSMEM 139 161 Helical. {ECO:0000255}.; TRANSMEM 196 218 Helical. {ECO:0000255}. FUNCTION: Chaperone protein involved in the assembly of the mitochondrial NADH:ubiquinone oxidoreductase complex (complex I). Participates in constructing the membrane arm of complex I (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Part of the mitochondrial complex I assembly (MCIA) complex. The complex comprises at least TMEM126B, NDUFAF1, ECSIT, and ACAD9. Associates with the intermediate 370 kDa subcomplex of incompletely assembled complex I (By similarity). {ECO:0000250}. +Q9DCS1 T176A_MOUSE Transmembrane protein 176A (Gene signature 188) (Kidney-expressed gene 2 protein) 244 26,596 Chain (1); Frameshift (1); Modified residue (1); Sequence conflict (1); Transmembrane (4) TRANSMEM 60 80 Helical. {ECO:0000255}.; TRANSMEM 92 112 Helical. {ECO:0000255}.; TRANSMEM 122 142 Helical. {ECO:0000255}.; TRANSMEM 204 224 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Specifically expressed in lung, kidney and spleen. {ECO:0000269|PubMed:11967007}. +Q9EP79 V1R52_MOUSE Vomeronasal type-1 receptor 52 (Pheromone receptor VN3) (Vomeronasal receptor 3) (Vomeronasal type-1 receptor A7) 309 35,050 Chain (1); Disulfide bond (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 20 40 Helical; Name=1. {ECO:0000255}.; TRANSMEM 50 70 Helical; Name=2. {ECO:0000255}.; TRANSMEM 94 114 Helical; Name=3. {ECO:0000255}.; TRANSMEM 135 155 Helical; Name=4. {ECO:0000255}.; TRANSMEM 188 208 Helical; Name=5. {ECO:0000255}.; TRANSMEM 239 259 Helical; Name=6. {ECO:0000255}.; TRANSMEM 269 289 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 19 Extracellular. {ECO:0000255}.; TOPO_DOM 41 49 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 71 93 Extracellular. {ECO:0000255}.; TOPO_DOM 115 134 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 156 187 Extracellular. {ECO:0000255}.; TOPO_DOM 209 238 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 260 268 Extracellular. {ECO:0000255}.; TOPO_DOM 290 309 Cytoplasmic. {ECO:0000255}. FUNCTION: Putative pheromone receptor implicated in the regulation of social and reproductive behavior. {ECO:0000269|PubMed:12214233}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. +Q9EP93 V1R53_MOUSE Vomeronasal type-1 receptor 53 (Pheromone receptor VN5) (Vomeronasal receptor 5) (Vomeronasal type-1 receptor B3) 310 35,399 Chain (1); Disulfide bond (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 21 41 Helical; Name=1. {ECO:0000255}.; TRANSMEM 51 71 Helical; Name=2. {ECO:0000255}.; TRANSMEM 94 114 Helical; Name=3. {ECO:0000255}.; TRANSMEM 135 155 Helical; Name=4. {ECO:0000255}.; TRANSMEM 184 204 Helical; Name=5. {ECO:0000255}.; TRANSMEM 239 259 Helical; Name=6. {ECO:0000255}.; TRANSMEM 269 289 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 20 Extracellular. {ECO:0000255}.; TOPO_DOM 42 50 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 72 93 Extracellular. {ECO:0000255}.; TOPO_DOM 115 134 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 156 183 Extracellular. {ECO:0000255}.; TOPO_DOM 205 238 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 260 268 Extracellular. {ECO:0000255}.; TOPO_DOM 290 310 Cytoplasmic. {ECO:0000255}. FUNCTION: Putative pheromone receptor implicated in the regulation of social and reproductive behavior. {ECO:0000269|PubMed:12214233}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. +Q9CQY8 T4S20_MOUSE Transmembrane 4 L6 family member 20 226 24,760 Chain (1); Sequence conflict (2); Site (1); Topological domain (5); Transmembrane (4) TRANSMEM 15 35 Helical. {ECO:0000255}.; TRANSMEM 50 70 Helical. {ECO:0000255}.; TRANSMEM 84 104 Helical. {ECO:0000255}.; TRANSMEM 192 212 Helical. {ECO:0000255}. TOPO_DOM 1 14 Lumenal. {ECO:0000305}.; TOPO_DOM 36 49 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 71 83 Lumenal. {ECO:0000305}.; TOPO_DOM 105 191 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 213 226 Lumenal. {ECO:0000305}. FUNCTION: Polytopic transmembrane protein. Inhibits regulated intramembrane proteolysis (RIP) of CREB3L1, inhibiting its activation and the induction of collagen synthesis. In response to ceramide, which alters TM4SF20 membrane topology, stimulates RIP activation of CREB3L1. Ceramide reverses the direction through which transmembrane helices are translocated into the endoplasmic reticulum membrane during translation of TM4SF20, this mechanism is called 'regulated alternative translocation' (RAT) and regulates the function of the transmembrane protein. {ECO:0000250|UniProtKB:Q53R12}. PTM: Glycosylated at Asn-132, Asn-148 and Asn-163 in presence of ceramide which inverts the orientation of TM4SF20 in membranes exposing these residues to the endoplasmic reticulum lumen. {ECO:0000250|UniProtKB:Q53R12}.; PTM: Cleaved by signal peptidase at Ser-14 but the peptide does not act as a signal peptide. Cleavage is inhibited by ceramide which inverts the orientation of TM4SF20 in membranes exposing the N-terminus to the cytosol and not to the endoplasmic reticulum lumen. {ECO:0000250|UniProtKB:Q53R12}. SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q53R12}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q53R12}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q53R12}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q53R12}. Note=Ceramide alters the direction through which transmembrane helices are translocated into the endoplasmic reticulum membrane during translation of TM4SF20. {ECO:0000250|UniProtKB:Q53R12}. DOMAIN: The first transmembrane helix plays a critical role for the insertion orientation in the endoplasmic reticulum membrane. {ECO:0000250|UniProtKB:Q53R12}. +Q7TQB8 T2R40_MOUSE Taste receptor type 2 member 40 (T2R40) (mT2R33) 319 36,559 Chain (1); Glycosylation (2); Topological domain (8); Transmembrane (7) TRANSMEM 18 38 Helical; Name=1. {ECO:0000255}.; TRANSMEM 67 87 Helical; Name=2. {ECO:0000255}.; TRANSMEM 98 118 Helical; Name=3. {ECO:0000255}.; TRANSMEM 137 157 Helical; Name=4. {ECO:0000255}.; TRANSMEM 190 210 Helical; Name=5. {ECO:0000255}.; TRANSMEM 252 272 Helical; Name=6. {ECO:0000255}.; TRANSMEM 282 302 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 17 Extracellular. {ECO:0000255}.; TOPO_DOM 39 66 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 88 97 Extracellular. {ECO:0000255}.; TOPO_DOM 119 136 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 158 189 Extracellular. {ECO:0000255}.; TOPO_DOM 211 251 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 273 281 Extracellular. {ECO:0000255}.; TOPO_DOM 303 319 Cytoplasmic. {ECO:0000255}. FUNCTION: Gustducin-coupled receptor implicated in the perception of bitter compounds in the oral cavity and the gastrointestinal tract. Signals through PLCB2 and the calcium-regulated cation channel TRPM5 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. +P59529 T2R16_MOUSE Taste receptor type 2 member 16 (T2R16) (Candidate taste receptor mt2r40) (T2R18) 299 34,761 Chain (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 6 26 Helical; Name=1. {ECO:0000255}.; TRANSMEM 48 68 Helical; Name=2. {ECO:0000255}.; TRANSMEM 83 103 Helical; Name=3. {ECO:0000255}.; TRANSMEM 126 146 Helical; Name=4. {ECO:0000255}.; TRANSMEM 184 204 Helical; Name=5. {ECO:0000255}.; TRANSMEM 234 254 Helical; Name=6. {ECO:0000255}.; TRANSMEM 259 279 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 5 Extracellular. {ECO:0000255}.; TOPO_DOM 27 47 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 69 82 Extracellular. {ECO:0000255}.; TOPO_DOM 104 125 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 147 183 Extracellular. {ECO:0000255}.; TOPO_DOM 205 233 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 255 258 Extracellular. {ECO:0000255}.; TOPO_DOM 280 299 Cytoplasmic. {ECO:0000255}. FUNCTION: Gustducin-coupled receptor implicated in the perception of bitter compounds in the oral cavity and the gastrointestinal tract. Signals through PLCB2 and the calcium-regulated cation channel TRPM5 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9NYV7}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Interacts with RTP3 and RTP4. {ECO:0000250|UniProtKB:Q9NYV7}. +Q5QD11 TAA7B_MOUSE Trace amine-associated receptor 7b (TaR-7b) (Trace amine receptor 7b) (mTaar7b) 358 40,231 Chain (1); Disulfide bond (1); Glycosylation (3); Topological domain (8); Transmembrane (7) TRANSMEM 48 68 Helical; Name=1. {ECO:0000255}.; TRANSMEM 84 104 Helical; Name=2. {ECO:0000255}.; TRANSMEM 122 143 Helical; Name=3. {ECO:0000255}.; TRANSMEM 167 187 Helical; Name=4. {ECO:0000255}.; TRANSMEM 213 233 Helical; Name=5. {ECO:0000255}.; TRANSMEM 275 295 Helical; Name=6. {ECO:0000255}.; TRANSMEM 310 333 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 47 Extracellular. {ECO:0000255}.; TOPO_DOM 69 83 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 105 121 Extracellular. {ECO:0000255}.; TOPO_DOM 144 166 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 188 212 Extracellular. {ECO:0000255}.; TOPO_DOM 234 274 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 296 309 Extracellular. {ECO:0000255}.; TOPO_DOM 334 358 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan olfactory receptor specific for trace amines. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Specifically expressed in neurons of the olfactory epithelium. {ECO:0000269|PubMed:16878137}. +Q8CFU8 T53I2_MOUSE Tumor protein p53-inducible nuclear protein 2 (Diabetes and obesity-regulated protein) 221 24,288 Alternative sequence (1); Chain (1); Modified residue (1); Motif (1); Sequence conflict (3) FUNCTION: Dual regulator of transcription and autophagy. Positively regulates autophagy and is required for autophagosome formation and processing. May act as a scaffold protein that recruits MAP1LC3A, GABARAP and GABARAPL2 and brings them to the autophagosome membrane by interacting with VMP1 where, in cooperation with the BECN1-PI3-kinase class III complex, they trigger autophagosome development. Acts as a transcriptional activator of THRA. {ECO:0000269|PubMed:18030323}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Nucleus {ECO:0000250}. Nucleus, PML body {ECO:0000250}. Cytoplasmic vesicle, autophagosome {ECO:0000250}. Note=Shuttles between the nucleus and the cytoplasm, depending on cellular stress conditions, and re-localizes to autophagosomes on autophagy activation. {ECO:0000250}. SUBUNIT: Interacts with VMP1, GABARAP, GABARAPL1, GABARAPL2, MAP1LC3A, MAP1LC3B, MAP1LC3C and THRA. {ECO:0000250}. DOMAIN: The LC3 interacting region (LIR) motif mediates interaction with GABARAP, GABARAPL1, GABARAPL2, MAP1LC3A, MAP1LC3B and MAP1LC3C. {ECO:0000250}. +Q5QD05 TAA8C_MOUSE Trace amine-associated receptor 8c (TaR-8c) (Trace amine receptor 8c) (mTaar8c) 344 37,890 Chain (1); Disulfide bond (1); Glycosylation (2); Topological domain (8); Transmembrane (7) TRANSMEM 32 52 Helical; Name=1. {ECO:0000255}.; TRANSMEM 68 88 Helical; Name=2. {ECO:0000255}.; TRANSMEM 112 132 Helical; Name=3. {ECO:0000255}.; TRANSMEM 147 167 Helical; Name=4. {ECO:0000255}.; TRANSMEM 196 216 Helical; Name=5. {ECO:0000255}.; TRANSMEM 261 281 Helical; Name=6. {ECO:0000255}.; TRANSMEM 283 303 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 31 Extracellular. {ECO:0000255}.; TOPO_DOM 53 67 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 89 111 Extracellular. {ECO:0000255}.; TOPO_DOM 133 146 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 168 195 Extracellular. {ECO:0000255}.; TOPO_DOM 217 260 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 282 282 Extracellular. {ECO:0000255}.; TOPO_DOM 304 344 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan olfactory receptor specific for trace amines. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Specifically expressed in neurons of the olfactory epithelium. {ECO:0000269|PubMed:16878137}. +Q8R2K4 TAF6L_MOUSE TAF6-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 6L (PCAF-associated factor 65-alpha) (PAF65-alpha) 616 67,236 Alternative sequence (1); Chain (1); Modified residue (5) FUNCTION: Functions as a component of the PCAF complex. The PCAF complex is capable of efficiently acetylating histones in a nucleosomal context. The PCAF complex could be considered as the human version of the yeast SAGA complex (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: The PCAF complex is composed of a number of TBP-associated factors (TAFS), such as TAF5, TAF5L, TAF6, TAF6L, TAF9, TAF10 and TAF12, PCAF, and also PCAF-associated factors (PAFs), such as TADA2L/ADA2, TADA3L/ADA3 and SPT3 (By similarity). Component of the STAGA transcription coactivator-HAT complex, at least composed of SUPT3H, GCN5L2, TAF5L, TAF6L, SUPT7L, TADA3L, TAD1L, TAF10, TAF12, TRRAP and TAF9. {ECO:0000250}. +P22091 TAL1_MOUSE T-cell acute lymphocytic leukemia protein 1 homolog (TAL-1) (Stem cell protein) 329 34,279 Chain (1); Compositional bias (1); Domain (1); Modified residue (3); Mutagenesis (1) FUNCTION: Implicated in the genesis of hemopoietic malignancies. It may play an important role in hemopoietic differentiation. Serves as a positive regulator of erythroid differentiation. {ECO:0000269|PubMed:9391090}. PTM: Phosphorylated on serine residues. Phosphorylation of Ser-122 by MAPK is strongly stimulated by hypoxia. {ECO:0000269|PubMed:11904294}.; PTM: Ubiquitinated; subsequent to hypoxia-dependent phosphorylation of Ser-122, ubiquitination targets the protein for rapid degradation via the ubiquitin system. This process may be characteristic for microvascular endothelial cells, since it could not be observed in large vessel endothelial cells. {ECO:0000269|PubMed:11904294}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:9391090}. SUBUNIT: Efficient DNA binding requires dimerization with another bHLH protein. Forms heterodimers with TCF3. Binds to the LIM domain containing protein LMO2 and to DRG1. Can assemble in a complex with LDB1 and LMO2. Component of a TAL-1 complex composed at least of CBFA2T3, LDB1, TAL1 and TCF3 (PubMed:9391090). Interacts with SBNO2; this interaction inhibits TAL1 occupancy of the DCSTAMP promoter, leading to the activation of the DCSTAMP promoter by the transcription factor MITF (PubMed:23980096). {ECO:0000269|PubMed:23980096, ECO:0000269|PubMed:9391090}. DOMAIN: The helix-loop-helix domain is necessary and sufficient for the interaction with DRG1. TISSUE SPECIFICITY: Erythroid and myeloid cells. +Q9R1Q8 TAGL3_MOUSE Transgelin-3 (Neuronal protein NP25) 199 22,471 Chain (1); Domain (1); Modified residue (1); Repeat (1) +B2RWW0 TAGAP_MOUSE T-cell activation Rho GTPase-activating protein (T-cell activation GTPase-activating protein) 714 78,920 Chain (1); Domain (1); Modified residue (1); Sequence conflict (4) FUNCTION: May function as a GTPase-activating protein. May play a role in transmission ratio distortion (TRD) in mouse, in which heterozygous males for t-locus transmit their t-carrying chromosome to 95% or more of their offspring. {ECO:0000269|PubMed:16116428}. TISSUE SPECIFICITY: Highly expressed in testis. {ECO:0000269|PubMed:16116428}. +P68373 TBA1C_MOUSE Tubulin alpha-1C chain (Alpha-tubulin 6) (Alpha-tubulin isotype M-alpha-6) (Tubulin alpha-6 chain) [Cleaved into: Detyrosinated tubulin alpha-1C chain] 449 49,909 Chain (2); Modified residue (5); Nucleotide binding (1); Sequence conflict (1); Site (1) FUNCTION: Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. PTM: Some glutamate residues at the C-terminus are polyglycylated, resulting in polyglycine chains on the gamma-carboxyl group. Glycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Both modifications can coexist on the same protein on adjacent residues, and lowering polyglycylation levels increases polyglutamylation, and reciprocally. The precise function of polyglycylation is still unclear. {ECO:0000269|PubMed:19524510}.; PTM: Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (PubMed:15890843). Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity by SPAST increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold (By similarity). {ECO:0000250|UniProtKB:Q71U36, ECO:0000269|PubMed:15890843}.; PTM: Acetylation of alpha chains at Lys-40 is located inside the microtubule lumen. This modification has been correlated with increased microtubule stability, intracellular transport and ciliary assembly. {ECO:0000250|UniProtKB:Q71U36}.; PTM: Methylation of alpha chains at Lys-40 is found in mitotic microtubules and is required for normal mitosis and cytokinesis contributing to genomic stability. {ECO:0000250|UniProtKB:P68363}.; PTM: Nitration of Tyr-449 is irreversible and interferes with normal dynein intracellular distribution. {ECO:0000250|UniProtKB:Q71U36}.; PTM: Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (VASH1 or VASH2) and tubulin tyrosine ligase (TTL), respectively. {ECO:0000269|PubMed:16954346, ECO:0000269|PubMed:19564401, ECO:0000269|PubMed:26446751, ECO:0000269|PubMed:27102488, ECO:0000269|PubMed:29146868}.; PTM: Tubulin alpha-1C chain: Tyrosination promotes microtubule interaction with CAP-Gly domain-containing proteins such as CLIP1, CLIP2 and DCTN1 (PubMed:16954346, PubMed:19564401). Tyrosination regulates the initiation of dynein-dynactin motility via interaction with DCTN1, which brings the dynein-dynactin complex into contact with microtubules. In neurons, tyrosinated tubulins mediate the initiation of retrograde vesicle transport (By similarity). {ECO:0000250|UniProtKB:Q71U36, ECO:0000269|PubMed:16954346, ECO:0000269|PubMed:19564401}.; PTM: Detyrosinated tubulin alpha-1C chain: Detyrosination is involved in metaphase plate congression by guiding chromosomes during mitosis: detyrosination promotes interaction with CENPE, promoting pole-proximal transport of chromosomes toward the equator (By similarity). Detyrosination increases microtubules-dependent mechanotransduction in dystrophic cardiac and skeletal muscle (PubMed:26446751). In cardiomyocytes, detyrosinated microtubules are required to resist to contractile compression during contraction: detyrosination promotes association with desmin (DES) at force-generating sarcomeres, leading to buckled microtubules and mechanical resistance to contraction (PubMed:27102488). {ECO:0000250|UniProtKB:Q9BQE3, ECO:0000269|PubMed:26446751, ECO:0000269|PubMed:27102488}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SUBUNIT: Dimer of alpha and beta chains. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells. TISSUE SPECIFICITY: Minor alpha-tubulin expressed in all tissues. {ECO:0000269|PubMed:3785200}. +Q5SVR0 TBC9B_MOUSE TBC1 domain family member 9B 1263 141,779 Alternative sequence (1); Chain (1); Domain (4); Erroneous initiation (2); Modified residue (6); Sequence conflict (5); Site (2); Transmembrane (1) TRANSMEM 669 689 Helical. {ECO:0000255}. FUNCTION: May act as a GTPase-activating protein for Rab family protein(s). SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. DOMAIN: The arginine and glutamine fingers are critical for the GTPase-activating mechanism, they pull out Rab's 'switch 2' glutamine and insert in Rab's active site. {ECO:0000250}. +Q3UUG6 TBC24_MOUSE TBC1 domain family member 24 561 63,236 Alternative sequence (1); Binding site (4); Chain (1); Domain (2); Erroneous initiation (1); Frameshift (1); Modified residue (2); Region (1); Sequence conflict (6) FUNCTION: May act as a GTPase-activating protein for Rab family protein(s) (PubMed:20727515). Involved in neuronal projections development, probably through a negative modulation of ARF6 function (PubMed:20727515). {ECO:0000269|PubMed:20727515}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9ULP9}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9ULP9}. Cytoplasm {ECO:0000250|UniProtKB:Q9ULP9}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q9VIH7}. Note=Mainly cytoplasmatic with partial expression at the plasma membrane (By similarity). Associates with certain types of membrane phosphoinositides, preferentially those phosphorylated at the D5 position of the inositol ring such as phosphatidylinositol 4,5-bisphosphate (PIP2) and phosphatidylinositol 3,4,5-trisphosphate (PIP3) (By similarity). {ECO:0000250|UniProtKB:Q9ULP9, ECO:0000250|UniProtKB:Q9VIH7}. SUBUNIT: Interacts with ARF6. {ECO:0000250|UniProtKB:Q9ULP9}. DOMAIN: The Rab-GAP TBC domain is essential for phosphatidylinositol binding. {ECO:0000250|UniProtKB:Q9VIH7}. TISSUE SPECIFICITY: Expressed in brain, particularly at the level of the cortex and the hippocampus. Expressed in the inner ear in spiral ganglion cells, a collection of neurons critical for hearing and balance. {ECO:0000269|PubMed:20727515, ECO:0000269|PubMed:24387994}. +A1A5B6 TBC25_MOUSE TBC1 domain family member 25 742 82,575 Chain (1); Compositional bias (4); Domain (1); Erroneous initiation (1); Modified residue (3); Sequence conflict (2) FUNCTION: Acts as a GTPase-activating protein specific for RAB33B. Involved in the regulation of autophagosome maturation, the process in which autophagosomes fuse with endosomes and lysosomes. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasmic vesicle, autophagosome {ECO:0000250}. Note=It is dispersed in the cytoplasm under nutrient-rich conditions. {ECO:0000250}. SUBUNIT: Interacts (via N-terminus) with MAP1LC3B, GABARAP and GABARAPL2. {ECO:0000269|PubMed:21383079}. +Q8VCN9 TBCC_MOUSE Tubulin-specific chaperone C (Tubulin-folding cofactor C) (CFC) 341 38,125 Chain (1); Domain (1); Modified residue (2); Sequence conflict (1) FUNCTION: Tubulin-folding protein; involved in the final step of the tubulin folding pathway. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Detected predominantly in the photoreceptor connecting cilium. {ECO:0000250}. SUBUNIT: Supercomplex made of cofactors A to E. Cofactors A and D function by capturing and stabilizing tubulin in a quasi-native conformation. Cofactor E binds to the cofactor D-tubulin complex; interaction with cofactor C then causes the release of tubulin polypeptides that are committed to the native state (By similarity). {ECO:0000250}. +Q9QXE7 TBL1X_MOUSE F-box-like/WD repeat-containing protein TBL1X (Transducin beta-like protein 1X) 527 56,802 Chain (1); Compositional bias (2); Cross-link (1); Domain (2); Erroneous gene model prediction (1); Initiator methionine (1); Modified residue (2); Mutagenesis (6); Repeat (8); Sequence conflict (2) FUNCTION: F-box-like protein involved in the recruitment of the ubiquitin/19S proteasome complex to nuclear receptor-regulated transcription units. Plays an essential role in transcription activation mediated by nuclear receptors. Probably acts as integral component of corepressor complexes that mediates the recruitment of the 19S proteasome complex, leading to the subsequent proteasomal degradation of transcription repressor complexes, thereby allowing cofactor exchange (By similarity). {ECO:0000250|UniProtKB:O60907}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Colocalized with MECP2 to the heterochromatin foci. {ECO:0000269|PubMed:28348241}. SUBUNIT: Homotetramer; dimer of dimers (By similarity). Component of the N-Cor repressor complex, at least composed of NCOR1, NCOR2, HDAC3, TBL1X, TBL1R, CORO2A and GPS2. Component of a E3 ubiquitin ligase complex containing UBE2D1, SIAH1, CACYBP/SIP, SKP1, APC and TBL1X. Interacts with GPS2 (when sumoylated); leading to protect GPS2 against degradation by the proteasome (PubMed:26070566). Probably part of other corepressor complexes, that do not contain NCOR1 and NCOR2. Interacts with histones H2B, H3a and H4 (By similarity). Interacts with MECP2; recuits TBL1X to the heterochromatin foci (PubMed:28348241). {ECO:0000250|UniProtKB:O60907, ECO:0000269|PubMed:26070566, ECO:0000269|PubMed:28348241}. DOMAIN: The F-box-like domain is related to the F-box domain, and apparently displays the same function as component of ubiquitin E3 ligase complexes. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the cochlea. {ECO:0000269|PubMed:10330347}. +Q8VCK3 TBG2_MOUSE Tubulin gamma-2 chain (Gamma-2-tubulin) 451 51,122 Chain (1); Modified residue (1); Mutagenesis (2); Nucleotide binding (1) FUNCTION: Tubulin is the major constituent of microtubules. The gamma chain is found at microtubule organizing centers (MTOC) such as the spindle poles or the centrosome. Pericentriolar matrix component that regulates alpha/beta chain minus-end nucleation, centrosome duplication and spindle formation (By similarity). {ECO:0000250}. PTM: Phosphorylation at Ser-131 by BRSK1 regulates centrosome duplication, possibly by mediating relocation of gamma-tubulin and its associated proteins from the cytoplasm to the centrosome. {ECO:0000269|PubMed:19648910}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:19648910}. Note=Mainly localizes to the centrosome, but a fraction is found outside of the centrosome in the cytoplasm. +Q8CDY7 TC1D4_MOUSE Tctex1 domain-containing protein 4 219 23,451 Chain (1); Modified residue (1); Sequence conflict (2) SUBUNIT: Interacts with ENG/endoglin, TGFBR2 and TGFBR3. {ECO:0000250}. +Q6SJ95 TBPL2_MOUSE TATA box-binding protein-like protein 2 (TBP-like protein 2) (TATA box-binding protein-related factor 3) (TBP-related factor 3) 350 38,967 Chain (1); Sequence conflict (3) FUNCTION: Transcription factor required in complex with TAF3 for the differentiation of myoblasts into myocytes. The complex replaces TFIID at specific promoters at an early stage in the differentiation process. {ECO:0000269|PubMed:17704303}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6SJ96, ECO:0000269|PubMed:17704303}. Nucleus {ECO:0000250|UniProtKB:Q6SJ96, ECO:0000269|PubMed:17704303}. Note=Present in the cytoplasm during cytokinesis. {ECO:0000250|UniProtKB:Q6SJ96}. SUBUNIT: Interacts with TAF3. {ECO:0000269|PubMed:17704303}. TISSUE SPECIFICITY: Expressed in myotubes and myofibers (at protein level). Expressed in a wide variety of tissues with highest levels in heart, lung, liver, uterus and placenta and especially the gonads. Expression is higher in the ovary than the testis, and within the ovary expression is localized to the oocytes. {ECO:0000269|PubMed:14634207, ECO:0000269|PubMed:15062100, ECO:0000269|PubMed:16412700, ECO:0000269|PubMed:17704303}. +Q8VC51 TCAB1_MOUSE Telomerase Cajal body protein 1 (WD repeat-containing protein 79) (WD40 repeat-containing protein antisense to TP53 gene homolog) 532 58,151 Chain (1); Modified residue (5); Repeat (6) FUNCTION: RNA chaperone that plays a key role in telomere maintenance and RNA localization to Cajal bodies (PubMed:29804836). Specifically recognizes and binds the Cajal body box (CAB box) present in both small Cajal body RNAs (scaRNAs) and telomerase RNA template component (TERC) (PubMed:29804836). Essential component of the telomerase holoenzyme complex, a ribonucleoprotein complex essential for the replication of chromosome termini that elongates telomeres in most eukaryotes (By similarity). In the telomerase holoenzyme complex, required to stimulate the catalytic activity of the complex (PubMed:29804836). Acts by specifically binding the CAB box of the TERC RNA and controlling the folding of the CR4/CR5 region of the TERC RNA, a critical step for telomerase activity (By similarity). In addition, also controls telomerase holoenzyme complex localization to Cajal body (By similarity). During S phase, required for delivery of TERC to telomeres during S phase and for telomerase activity (By similarity). In addition to its role in telomere maintenance, also required for Cajal body formation, probably by mediating localization of scaRNAs to Cajal bodies (By similarity). Also plays a role in DNA repair: phosphorylated by ATM in response to DNA damage and relocalizes to sites of DNA double-strand breaks to promote the repair of DNA double-strand breaks (By similarity). Acts by recruiting the ubiquitin ligase RNF8 to DNA breaks and promote both homologous recombination (HR) and non-homologous end joining (NHEJ) (By similarity). {ECO:0000250|UniProtKB:Q9BUR4, ECO:0000269|PubMed:29804836}. PTM: Phosphorylated at Ser-61 by ATM in response to DNA damage, promoting its interaction with histone H2AX/H2AFX and localization to sites of DNA double-strand breaks. {ECO:0000250|UniProtKB:Q9BUR4}. SUBCELLULAR LOCATION: Nucleus, Cajal body {ECO:0000250|UniProtKB:Q9BUR4}. Chromosome, telomere {ECO:0000250|UniProtKB:Q9BUR4}. Chromosome {ECO:0000250|UniProtKB:Q9BUR4}. Note=Released from telomerase RNA template component (TERC) in mitotic cells coincident with delocalization from Cajal bodies. In response to DNA damage, localizes to sites of DNA double-strand breaks following phosphorylation by ATM. {ECO:0000250|UniProtKB:Q9BUR4}. SUBUNIT: Component of the telomerase holoenzyme complex composed of one molecule of TERT, one molecule of WRAP53/TCAB1, two molecules of H/ACA ribonucleoprotein complex subunits DKC1, NOP10, NHP2 and GAR1, and a telomerase RNA template component (TERC). The telomerase holoenzyme complex is associated with TEP1, SMG6/EST1A and POT1. Interacts with the chaperonin-containing T-complex (TRiC) complex; which mediates the folding of WRAP53/TCAB1. Interacts with COIL. Interacts with SMN1. Interacts with RNF8. Interacts with histone H2AX/H2AFX. {ECO:0000250|UniProtKB:Q9BUR4}. +Q9QVN7 TCEA2_MOUSE Transcription elongation factor A protein 2 (Protein S-II-T1) (Testis-specific S-II) (Transcription elongation factor S-II protein 2) (Transcription elongation factor TFIIS.l) 299 33,663 Chain (1); Cross-link (1); Domain (2); Modified residue (2); Zinc finger (1) FUNCTION: Necessary for efficient RNA polymerase II transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by S-II allows the resumption of elongation from the new 3'-terminus. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with the basal transcription factor GTF2B. Interacts with REXO1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Testis and ovary specific. Specific to testicular germ cells. +P70327 TBX6_MOUSE T-box transcription factor TBX6 (T-box protein 6) 436 47,006 Alternative sequence (1); Chain (1); DNA binding (1); Frameshift (1); Sequence conflict (4) FUNCTION: T-box transcription factor that plays an essential role in the determination of the fate of axial stem cells: neural vs mesodermal. Acts in part by down-regulating, a specific enhancer (N1) of SOX2, to inhibit neural development. Seems to play also an essential role in left/right axis determination and acts through effects on Notch signaling around the node as well as through an effect on the morphology and motility of the nodal cilia. {ECO:0000269|PubMed:15545628, ECO:0000269|PubMed:18575602, ECO:0000269|PubMed:21331042, ECO:0000269|PubMed:9490412}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00201}. +Q9EPQ8 TCF20_MOUSE Transcription factor 20 (TCF-20) (Nuclear factor SPBP) (Stromelysin-1 PDGF-responsive element-binding protein) (SPRE-binding protein) 1987 215,683 Alternative sequence (1); Chain (1); Compositional bias (7); Cross-link (32); DNA binding (1); Frameshift (1); Modified residue (22); Motif (3); Mutagenesis (7); Region (1); Sequence conflict (11); Zinc finger (2) FUNCTION: Transcriptional activator that binds to the regulatory region of MMP3 and thereby controls stromelysin expression. It stimulates the activity of various transcriptional activators such as JUN, SP1, PAX6 and ETS1, suggesting a function as a coactivator. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Homodimer (Probable). Interacts with RNF4 and JUN. Binds to the regulatory region of MMP3. {ECO:0000269|PubMed:10849425, ECO:0000269|PubMed:8663478, ECO:0000305}. DOMAIN: The atypical PHD domain functions as a negative modulator of cofactor binding. TISSUE SPECIFICITY: Expressed in brain, lung, liver, kidney and testes. {ECO:0000269|PubMed:10849425}. +P80313 TCPH_MOUSE T-complex protein 1 subunit eta (TCP-1-eta) (CCT-eta) 544 59,652 Chain (1); Cross-link (1); Modified residue (5) FUNCTION: Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. The TRiC complex plays a role in the folding of actin and tubulin. {ECO:0000250|UniProtKB:Q99832}. PTM: The N-terminus is blocked. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:7953530}. SUBUNIT: Component of the chaperonin-containing T-complex (TRiC), a heterooligomeric complex of about 850 to 900 kDa that forms two stacked rings, 12 to 16 nm in diameter. Interacts with PACRG. {ECO:0000250|UniProtKB:Q99832}. +P80317 TCPZ_MOUSE T-complex protein 1 subunit zeta (TCP-1-zeta) (CCT-zeta-1) 531 58,004 Chain (1); Cross-link (1); Initiator methionine (1); Modified residue (8) FUNCTION: Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. The TRiC complex plays a role in the folding of actin and tubulin. {ECO:0000250|UniProtKB:P40227}. PTM: The N-terminus is blocked. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P40227}. SUBUNIT: Component of the chaperonin-containing T-complex (TRiC), a heterooligomeric complex of about 850 to 900 kDa that forms two stacked rings, 12 to 16 nm in diameter. Interacts with PACRG. {ECO:0000250|UniProtKB:P40227}. TISSUE SPECIFICITY: Expressed in all tissues examined. +P11031 TCP4_MOUSE Activated RNA polymerase II transcriptional coactivator p15 (Positive cofactor 4) (PC4) (SUB1 homolog) (Single-stranded DNA-binding protein p9) (p14) 127 14,427 Chain (1); Compositional bias (3); Cross-link (2); Modified residue (16); Region (2); Sequence conflict (1); Site (1) FUNCTION: General coactivator that functions cooperatively with TAFs and mediates functional interactions between upstream activators and the general transcriptional machinery. May be involved in stabilizing the multiprotein transcription complex. Binds single-stranded DNA. Also binds, in vitro, non-specifically to double-stranded DNA (ds DNA). PTM: Activity is controlled by protein kinases that target the regulatory region. Phosphorylation inactivates both ds DNA-binding and cofactor function, but does not affect binding to ssDNA (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Homodimer. Interacts with CSTF2 (By similarity). {ECO:0000250}. +Q99MV1 TDRD1_MOUSE Tudor domain-containing protein 1 1172 129,696 Beta strand (14); Chain (1); Domain (4); Erroneous initiation (4); Helix (5); Mutagenesis (5); Sequence conflict (3); Turn (2); Zinc finger (1) FUNCTION: Plays a central role during spermatogenesis by participating in the repression transposable elements and preventing their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons. Required for the localization of Piwi proteins to the meiotic nuage. Involved in the piRNA metabolic process by ensuring the entry of correct transcripts into the normal piRNA pool and limiting the entry of cellular transcripts into the piRNA pathway. May act by allowing the recruitment of piRNA biogenesis or loading factors that ensure the correct entry of transcripts and piRNAs into Piwi proteins. {ECO:0000269|PubMed:17038506, ECO:0000269|PubMed:19465913, ECO:0000269|PubMed:19584108}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14550528, ECO:0000269|PubMed:17038506, ECO:0000269|PubMed:17141210, ECO:0000269|PubMed:19345100, ECO:0000269|PubMed:19465913, ECO:0000269|PubMed:19584108, ECO:0000269|PubMed:20439430}. Note=Component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis (PubMed:20439430). DDX4 is required for meiotic nuage localization. Also present in chromatoid body. {ECO:0000269|PubMed:20439430}. SUBUNIT: Found in a mRNP complex, at least composed of TDRD1, TDRD6, TDRD7 and DDX4. Interacts with MAEL. Interacts with PIWIL1, PIWIL2 and PIWIL4 (when methylated on arginine residues). Interacts with TDRD12. {ECO:0000269|PubMed:16787967, ECO:0000269|PubMed:17141210, ECO:0000269|PubMed:19345100, ECO:0000269|PubMed:19465913, ECO:0000269|PubMed:19584108, ECO:0000269|PubMed:22996915, ECO:0000269|PubMed:24067652}. DOMAIN: Tudor domains 2 and 3 have higher affinity for arginine-methylated peptides, tudor domain 1 is a poor binder due to an impaired aromatic cage. TISSUE SPECIFICITY: Testis and ovary specific. Present in germ-line cells and is most abundant in fetal prospermatogonia and postnatal primary spermatocytes (at protein level). {ECO:0000269|PubMed:14550528}. +Q8R2M2 TDIF2_MOUSE Deoxynucleotidyltransferase terminal-interacting protein 2 758 84,277 Chain (1); Coiled coil (1); Cross-link (12); Modified residue (15); Region (1); Sequence conflict (1) FUNCTION: Regulates the transcriptional activity of DNTT and ESR1. May function as a chromatin remodeling protein (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Forms a ternary complex with DNTT and core histone; interaction with PCNA releases DNTT and H2A/H2B histones from this ternary complex. Interacts with ESR1, ESR2, PPARG and RXRA (By similarity). {ECO:0000250}. +P0DMR6 TDP1L_MOUSE TD and POZ domain-containing protein 1-like 365 41,674 Chain (1); Domain (2) +Q9DC40 TELO2_MOUSE Telomere length regulation protein TEL2 homolog 840 93,313 Alternative sequence (3); Chain (1); Erroneous termination (1); Helix (1); Modified residue (9); Mutagenesis (3); Sequence conflict (19); Site (3) FUNCTION: Regulator of the DNA damage response (DDR). Part of the TTT complex that is required to stabilize protein levels of the phosphatidylinositol 3-kinase-related protein kinase (PIKK) family proteins. The TTT complex is involved in the cellular resistance to DNA damage stresses, like ionizing radiation (IR), ultraviolet (UV) and mitomycin C (MMC). Together with the TTT complex and HSP90 may participate in the proper folding of newly synthesized PIKKs. Promotes assembly, stabilizes and maintains the activity of mTORC1 and mTORC2 complexes, which regulate cell growth and survival in response to nutrient and hormonal signals. May be involved in telomere length regulation (By similarity). {ECO:0000250}. PTM: Hydroxylation by PHD3 is required for a proper interaction with ATR, and activation of the ATR/CHK1/p53 pathway following DNA damage. {ECO:0000250}.; PTM: Phosphorylated at Ser-486 by CK2 following growth factor deprivation, leading to its subsequent ubiquitination by the SCF(FBXO9) complex. Phosphorylation by CK2 only takes place when TELO2 is bound to mTORC1, not mTORC2; leading to selective ubiquitination of mTORC1-associated protein (By similarity). {ECO:0000250}.; PTM: Ubiquitinated by the SCF(FBXO9) complex following phosphorylation by CK2 in response to growth factor deprivation, leading to its degradation by the proteasome. Only mTORC1-associated protein is ubiquitinated and degraded, leading to selective inactivation of mTORC1 to restrain cell growth and protein translation, while mTORC2 is activated due to the relief of feedback inhibition by mTORC1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}. Nucleus {ECO:0000250}. Chromosome, telomere {ECO:0000305}. SUBUNIT: Component of the TTT complex composed of TELO2, TTI1 and TTI2. Interacts with ATM, ATR, MTOR, PRKDC, RUVBL2, TTI1, TTI2, SMG1 and TRRAP. Component of the mTORC1 and mTORC2 complexes. Interacts (phosphorylated form) with PIH1D1 (PubMed:24794838). Interaction with PIH1D1 mediates interaction of TELO2 with the R2TP complex composed of RUVBL1, RUVBL2, PIH1D1, and RPAP3 (By similarity). {ECO:0000250|UniProtKB:Q9Y4R8, ECO:0000269|PubMed:24794838}. +Q9JHJ7 TEST_MOUSE Testisin (EC 3.4.21.-) (Serine protease 21) (Tryptase 4) 324 36,175 Active site (3); Chain (1); Disulfide bond (5); Domain (1); Erroneous termination (1); Glycosylation (4); Lipidation (1); Propeptide (2); Sequence conflict (1); Signal peptide (1) FUNCTION: Could regulate proteolytic events associated with testicular germ cell maturation. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}. TISSUE SPECIFICITY: Testis. +P70210 TEAD3_MOUSE Transcriptional enhancer factor TEF-5 (DTEF-1) (ETF-related factor 1) (ETFR-1) (TEA domain family member 3) (TEAD-3) 439 48,938 Chain (1); Compositional bias (2); DNA binding (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (2); Natural variant (1); Region (1); Sequence caution (3) FUNCTION: Transcription factor which plays a key role in the Hippo signaling pathway, a pathway involved in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein MST1/MST2, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Acts by mediating gene expression of YAP1 and WWTR1/TAZ, thereby regulating cell proliferation, migration and epithelial mesenchymal transition (EMT) induction (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with YAP1 and WWTR1/TAZ. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in embryos as well as in many adult tissues. +Q8JZM0 TFB1M_MOUSE Dimethyladenosine transferase 1, mitochondrial (EC 2.1.1.-) (Mitochondrial 12S rRNA dimethylase 1) (Mitochondrial transcription factor B1) (mtTFB1) (S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase 1) 345 38,962 Beta strand (9); Binding site (6); Chain (1); Helix (20); Region (1); Transit peptide (1); Turn (5) FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase which specifically dimethylates mitochondrial 12S rRNA at the conserved stem loop. Also required for basal transcription of mitochondrial DNA, probably via its interaction with POLRMT and TFAM. Stimulates transcription independently of the methyltransferase activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. SUBUNIT: Interacts with mitochondrial RNA polymerase POLRMT. Interacts with TFAM (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:12532263}. +Q8R2T8 TF3C5_MOUSE General transcription factor 3C polypeptide 5 (TF3C-epsilon) (Transcription factor IIIC 63 kDa subunit) (TFIIIC 63 kDa subunit) (TFIIIC63) (Transcription factor IIIC subunit epsilon) 520 60,502 Alternative sequence (1); Chain (1); Compositional bias (3); Initiator methionine (1); Modified residue (1); Sequence conflict (1) FUNCTION: Involved in RNA polymerase III-mediated transcription. Integral, tightly associated component of the DNA-binding TFIIIC2 subcomplex that directly binds tRNA and virus-associated RNA promoters (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Part of the TFIIIC subcomplex TFIIIC2, consisting of six subunits, GTF3C1, GTF3C2, GTF3C3, GTF3C4, GTF3C5 and GTF3C6. Interacts with BRF1, GTF3C6 and TBP (By similarity). {ECO:0000250}. +P24604 TEC_MOUSE Tyrosine-protein kinase Tec (EC 2.7.10.2) 630 73,426 Active site (1); Alternative sequence (5); Beta strand (7); Binding site (1); Chain (1); Domain (4); Metal binding (4); Modified residue (3); Mutagenesis (1); Nucleotide binding (1); Sequence conflict (27); Turn (1); Zinc finger (1) FUNCTION: Non-receptor tyrosine kinase that contributes to signaling from many receptors and participates as a signal transducer in multiple downstream pathways, including regulation of the actin cytoskeleton. Plays a redundant role to ITK in regulation of the adaptive immune response. Regulates the development, function and differentiation of conventional T-cells and nonconventional NKT-cells. Required for TCR-dependent IL2 gene induction. Phosphorylates DOK1, one CD28-specific substrate, and contributes to CD28-signaling. Mediates signals that negatively regulate IL2RA expression induced by TCR cross-linking. Plays a redundant role to BTK in BCR-signaling for B-cell development and activation, especially by phosphorylating STAP1, a BCR-signaling protein. Required in mast cells for efficient cytokine production. Involved in both growth and differentiation mechanisms of myeloid cells through activation by the granulocyte colony-stimulating factor CSF3, a critical cytokine to promoting the growth, differentiation, and functional activation of myeloid cells. Participates in platelet signaling downstream of integrin activation. Cooperates with JAK2 through reciprocal phosphorylation to mediate cytokine-driven activation of FOS transcription. GRB10, a negative modifier of the FOS activation pathway, is another substrate of TEC. TEC is involved in G protein-coupled receptor- and integrin-mediated signalings in blood platelets. Plays a role in hepatocyte proliferation and liver regeneration and is involved in HGF-induced ERK signaling pathway. TEC regulates also FGF2 unconventional secretion (endoplasmic reticulum (ER)/Golgi-independent mechanism) under various physiological conditions through phosphorylation of FGF2 'Tyr-82'. May also be involved in the regulation of osteoclast differentiation. {ECO:0000269|PubMed:10382746, ECO:0000269|PubMed:15214045, ECO:0000269|PubMed:19688741, ECO:0000269|PubMed:21094130, ECO:0000269|PubMed:9473212, ECO:0000269|PubMed:9872994}. PTM: Following B-cell or T-cell receptors engagement, translocates to the plasma membrane where it gets phosphorylated at Tyr-518. Undergoes also tyrosine phosphorylation during platelet activation. {ECO:0000269|PubMed:8621063, ECO:0000269|PubMed:8877094, ECO:0000269|PubMed:9473212}. SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral membrane protein. Cytoplasm, cytoskeleton. Note=Following B-cell or T-cell receptors activation by antigen, translocates to the plasma membrane through its PH domain. Thrombin and integrin engagement induces translocation of TEC to the cytoskeleton during platelet activation. In cardiac myocytes, assumes a diffuse intracellular localization under basal conditions but is recruited to striated structures upon various stimuli, including ATP (By similarity). {ECO:0000250}. SUBUNIT: Interacts with INPP5D/SHIP1 and INPPL1/SHIP2. Interacts with CD28, FASLG, FGF2, GRB10 and KIT (By similarity). Interacts with VAV1 and JAK2. Interacts with LYN. {ECO:0000250, ECO:0000269|PubMed:8877094, ECO:0000269|PubMed:9872994}. DOMAIN: The PH domain mediates the binding to inositol polyphosphate and phosphoinositides, leading to its targeting to the plasma membrane. It is extended in the BTK kinase family by a region designated the TH (Tec homology) domain, which consists of about 80 residues preceding the SH3 domain. {ECO:0000269|PubMed:15214045}.; DOMAIN: The SH3 domain is essential for its targeting to activated CD28 costimulatory molecule. {ECO:0000250}. TISSUE SPECIFICITY: Preferentially expressed in liver. Expression is also seen in the hematopoietic cells such as bone marrow, thymus and spleen. Lower expression is seen in the heart, kidney and ovary. +Q8K2X8 TF2H5_MOUSE General transcription factor IIH subunit 5 (General transcription factor IIH polypeptide 5) (TFB5 ortholog) (TFIIH basal transcription factor complex TTD-A subunit) 71 8,037 Chain (1); Modified residue (1); Sequence conflict (1) FUNCTION: Component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module CAK controls the initiation of transcription. Necessary for the stability of the TFIIH complex and for the presence of normal levels of TFIIH in the cell. {ECO:0000250|UniProtKB:Q6ZYL4}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the 7-subunit TFIIH core complex composed of XPB/ERCC3, XPD/ERCC2, GTF2H1, GTF2H2, GTF2H3, GTF2H4 and GTF2H5, which is active in NER. The core complex associates with the 3-subunit CDK-activating kinase (CAK) module composed of CCNH/cyclin H, CDK7 and MNAT1 to form the 10-subunit holoenzyme (holo-TFIIH) active in transcription. {ECO:0000250|UniProtKB:Q6ZYL4}. +P62082 RS7_MOUSE 40S ribosomal protein S7 194 22,127 Chain (1); Compositional bias (1); Cross-link (2); Modified residue (2) FUNCTION: Required for rRNA maturation. {ECO:0000250|UniProtKB:P62081}. PTM: Phosphorylated by NEK6. {ECO:0000250|UniProtKB:P62081}.; PTM: Ubiquitinated. Deubiquitinated by DESI2, leading to its stabilization. {ECO:0000250|UniProtKB:P62081}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P62081}. Note=Colocalizes with NEK6 in the centrosome. {ECO:0000250|UniProtKB:P62081}. SUBUNIT: Binds IPO9 with high affinity. Interacts with NEK6. Interacts with DESI2. {ECO:0000250|UniProtKB:P62081}. +Q9D3W1 RSP14_MOUSE Radial spoke head 14 homolog (Rhabdoid tumor deletion region protein 1) 341 37,809 Chain (1); Repeat (8) +Q2TJ95 RSPO3_MOUSE R-spondin-3 (Cabriolet) (Cysteine-rich and single thrombospondin domain-containing protein 1) (Cristin-1) (Nucleopondin) (Roof plate-specific spondin-3) 277 31,454 Chain (1); Disulfide bond (11); Domain (1); Frameshift (1); Glycosylation (1); Repeat (2); Sequence conflict (4); Signal peptide (1) FUNCTION: Activator of the canonical Wnt signaling pathway by acting as a ligand for LGR4-6 receptors, which acts as a key regulator of angiogenesis (PubMed:16543246, PubMed:21693646, PubMed:26766444). Upon binding to LGR4-6 (LGR4, LGR5 or LGR6), LGR4-6 associate with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increase expression of target genes. Also regulates the canonical Wnt/beta-catenin-dependent pathway and non-canonical Wnt signaling by acting as an inhibitor of ZNRF3, an important regulator of the Wnt signaling pathway. Acts as a ligand for frizzled FZD8 and LRP6. May negatively regulate the TGF-beta pathway (PubMed:16543246, PubMed:21693646). Acts as a key regulator of angiogenesis by controlling vascular stability and pruning: acts by activating the non-canonical Wnt signaling pathway in endothelial cells (PubMed:26766444, PubMed:16543246, PubMed:21693646). Can also amplify Wnt signaling pathway independently of LGR4-6 receptors, possibly by acting as a direct antagonistic ligand to RNF43 and ZNRF3 (By similarity). {ECO:0000250|UniProtKB:Q9BXY4, ECO:0000269|PubMed:16543246, ECO:0000269|PubMed:21693646, ECO:0000269|PubMed:26766444}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16543246}. SUBUNIT: Interacts with the extracellular domain of FZD8 and LRP6 (PubMed:16543246). It however does not form a ternary complex with FZD8 and LRP6 (PubMed:16543246). Interacts with WNT1 (PubMed:16543246). Binds heparin. Interacts with LGR4, LGR5 and LGR6 (PubMed:21693646). {ECO:0000269|PubMed:16543246, ECO:0000269|PubMed:21693646}. DOMAIN: The FU repeats are required for activation and stabilization of beta-catenin. {ECO:0000269|PubMed:16543246}. TISSUE SPECIFICITY: Highly expressed in endothelial cells (PubMed:26766444). {ECO:0000269|PubMed:26766444}. +Q61733 RT31_MOUSE 28S ribosomal protein S31, mitochondrial (MRP-S31) (S31mt) (Imogen 38) 384 43,881 Chain (1); Sequence conflict (3); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P82925}. SUBUNIT: Component of the mitochondrial ribosome small subunit (28S) which comprises a 12S rRNA and about 30 distinct proteins. {ECO:0000250|UniProtKB:P82925}. +Q3URY0 RTL4_MOUSE Retrotransposon Gag-like protein 4 (Mammalian retrotransposon-derived protein 4) (Sushi-XF2b protein) (Sushi-ichi-related retrotransposon homolog 11) (Zinc finger CCHC domain-containing protein 16) 304 34,266 Chain (1); Frameshift (1); Sequence conflict (1); Zinc finger (1) FUNCTION: Involved in cognitive function in the brain, possibly via the noradrenergic system. {ECO:0000269|PubMed:26402067}. TISSUE SPECIFICITY: In adults, expressed in brain, eye, kidney, ovary and testis (PubMed:26402067, PubMed:15716091). Weakly expressed in thymus, heart and muscle (PubMed:15716091). {ECO:0000269|PubMed:15716091, ECO:0000269|PubMed:26402067}. +Q80U22 RUSC2_MOUSE Iporin (Interacting protein of Rab1) (RUN and SH3 domain-containing protein 2) 1514 161,139 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (2); Erroneous initiation (1); Modified residue (6) SUBCELLULAR LOCATION: Cytoplasm, cytosol. Note=Cytosolic punctate distribution. Also observed in the perinuclear region (By similarity). {ECO:0000250}. SUBUNIT: Interacts with active RAB1A and RAB1B, and with GOLGA2. {ECO:0000250}. DOMAIN: The RUN domain is required for the interaction with RAB1A and RAB1B. {ECO:0000250}. +Q8BHW5 T255A_MOUSE Transmembrane protein 255A (Protein FAM70A) 351 38,633 Alternative sequence (2); Chain (1); Compositional bias (1); Sequence conflict (2); Transmembrane (4) TRANSMEM 30 50 Helical. {ECO:0000255}.; TRANSMEM 57 77 Helical. {ECO:0000255}.; TRANSMEM 89 109 Helical. {ECO:0000255}.; TRANSMEM 226 246 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8K0Z7 TACO1_MOUSE Translational activator of cytochrome c oxidase 1 (Coiled-coil domain-containing protein 44) (Translational activator of mitochondrially-encoded cytochrome c oxidase 1) 294 32,314 Beta strand (7); Chain (1); Coiled coil (1); Helix (8); Modified residue (1); Sequence conflict (1); Turn (1) FUNCTION: Acts as a translational activator of mitochondrially-encoded cytochrome c oxidase 1. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. +Q8CHV6 TAD2A_MOUSE Transcriptional adapter 2-alpha (Transcriptional adapter 2-like) (ADA2-like protein) 443 51,339 Beta strand (3); Chain (1); Compositional bias (1); Cross-link (2); DNA binding (1); Domain (2); Erroneous initiation (2); Helix (4); Modified residue (1); Mutagenesis (3); Sequence conflict (1); Turn (1) FUNCTION: Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4 (By similarity). Required for the function of some acidic activation domains, which activate transcription from a distant site (By similarity). Binds double-stranded DNA (PubMed:16299514). Binds dinucleosomes, probably at the linker region between neighboring nucleosomes (PubMed:16299514). Plays a role in chromatin remodeling (By similarity). May promote TP53/p53 'Lys-321' acetylation, leading to reduced TP53 stability and transcriptional activity (By similarity). May also promote XRCC6 acetylation thus facilitating cell apoptosis in response to DNA damage (By similarity). {ECO:0000250|UniProtKB:O75478, ECO:0000269|PubMed:16299514}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00624, ECO:0000269|PubMed:16299514}. Chromosome {ECO:0000269|PubMed:16299514}. SUBUNIT: Interacts with GCN5. Interacts with NR3C1. Associated with the P/CAF protein in the PCAF complex. Component of the PCAF complex, at least composed of TADA2L/ADA2, TADA3L/ADA3, TAF5L/PAF65-beta, TAF6L/PAF65-alpha, TAF10/TAFII30, TAF12/TAFII20, TAF9/TAFII31 and TRRAP. Component of the ADA2A-containing complex (ATAC), composed of KAT14, KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1. Interacts with CCDC134. {ECO:0000250|UniProtKB:O75478}. +P62307 RUXF_MOUSE Small nuclear ribonucleoprotein F (snRNP-F) (Sm protein F) (Sm-F) (SmF) 86 9,725 Chain (1); Initiator methionine (1); Modified residue (1) FUNCTION: Plays role in pre-mRNA splicing as core component of the SMN-Sm complex that mediates spliceosomal snRNP assembly and as component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Component of both the pre-catalytic spliceosome B complex and activated spliceosome C complexes. Is also a component of the minor U12 spliceosome. As part of the U7 snRNP it is involved in histone 3'-end processing. {ECO:0000250|UniProtKB:P62306}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P62306}. Nucleus {ECO:0000250|UniProtKB:P62306}. Note=SMN-mediated assembly into core snRNPs occurs in the cytosol before SMN-mediated transport to the nucleus to be included in spliceosomes. {ECO:0000250|UniProtKB:P62306}. SUBUNIT: Core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Most spliceosomal snRNPs contain a common set of Sm proteins, SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. Component of the U1 snRNP. The U1 snRNP is composed of the U1 snRNA and the 7 core Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG, and at least three U1 snRNP-specific proteins SNRNP70/U1-70K, SNRPA/U1-A and SNRPC/U1-C. Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39, plus LSM2, LSM3, LSM4, LSM5, LSM6, LSM7 and LSM8. Component of the U7 snRNP complex, or U7 Sm protein core complex, that is composed of the U7 snRNA and at least LSM10, LSM11, SNRPB, SNRPD3, SNRPE, SNRPF and SNRPG; the complex does not contain SNRPD1 and SNRPD2. Component of the U11/U12 snRNPs that are part of the U12-type spliceosome. Part of the SMN-Sm complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8, STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG; catalyzes core snRNPs assembly. Forms a 6S pICln-Sm complex composed of CLNS1A/pICln, SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG; ring-like structure where CLNS1A/pICln mimics additional Sm proteins and which is unable to assemble into the core snRNP. {ECO:0000250|UniProtKB:P62306}. +P55014 S12A1_MOUSE Solute carrier family 12 member 1 (BSC1) (Bumetanide-sensitive sodium-(potassium)-chloride cotransporter 2) (Kidney-specific Na-K-Cl symporter) 1095 120,355 Alternative sequence (4); Chain (1); Glycosylation (2); Modified residue (7); Sequence conflict (15); Topological domain (7); Transmembrane (12) TRANSMEM 174 194 Helical. {ECO:0000255}.; TRANSMEM 198 218 Helical. {ECO:0000255}.; TRANSMEM 256 276 Helical. {ECO:0000255}.; TRANSMEM 299 319 Helical. {ECO:0000255}.; TRANSMEM 324 344 Helical. {ECO:0000255}.; TRANSMEM 376 396 Helical. {ECO:0000255}.; TRANSMEM 414 434 Helical. {ECO:0000255}.; TRANSMEM 481 501 Helical. {ECO:0000255}.; TRANSMEM 547 567 Helical. {ECO:0000255}.; TRANSMEM 568 588 Helical. {ECO:0000255}.; TRANSMEM 606 626 Helical. {ECO:0000255}.; TRANSMEM 789 809 Helical. {ECO:0000255}. TOPO_DOM 1 173 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 219 255 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 320 323 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 397 413 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 502 546 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 589 605 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 810 1095 Cytoplasmic. {ECO:0000255}. FUNCTION: Electrically silent transporter system. Mediates sodium and chloride reabsorption. Plays a vital role in the regulation of ionic balance and cell volume. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Predominant in kidney. Isoform F is most highly expressed in the inner stripe of outer medulla, isoform A is most highly expressed in the outer stripe of the outer medulla, and isoform B is most highly expressed in the cortical thick ascending limb. +Q8VIL2 RWDD3_MOUSE RWD domain-containing protein 3 (RWD domain-containing sumoylation enhancer) (RSUME) 267 29,890 Chain (1); Domain (1); Region (2); Sequence conflict (1) FUNCTION: Enhancer of SUMO conjugation. Via its interaction with UBE2I/UBC9, increases SUMO conjugation to proteins by promoting the binding of E1 and E2 enzymes, thioester linkage between SUMO and UBE2I/UBC9 and transfer of SUMO to specific target proteins which include HIF1A, PIAS, NFKBIA, NR3C1 and TOP1. Positively regulates the NF-kappa-B signaling pathway by enhancing the sumoylation of NF-kappa-B inhibitor alpha (NFKBIA), promoting its stabilization which consequently leads to an increased inhibition of NF-kappa-B transcriptional activity. Negatively regulates the hypoxia-inducible factor-1 alpha (HIF1A) signaling pathway by increasing the sumoylation of HIF1A, promoting its stabilization, transcriptional activity and the expression of its target gene VEGFA during hypoxia. Has no effect on ubiquitination. {ECO:0000269|PubMed:22009797}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y3V2}. Cytoplasm {ECO:0000250|UniProtKB:Q9Y3V2}. Note=Colocalizes with UBC9/UBE2I in nuclear spots. {ECO:0000250}. SUBUNIT: Interacts with UBE2I/UBC9, NFKBIA, HIF1A and NCOA2. {ECO:0000250|UniProtKB:Q9Y3V2}. DOMAIN: The RWD domain is required for the sumoylation enhancement activity. {ECO:0000250}. +Q9D2Q8 S10AE_MOUSE Protein S100-A14 (S100 calcium-binding protein A14) (S114) 104 11,599 Chain (1); Domain (1); Sequence conflict (1) FUNCTION: Modulates P53/TP53 protein levels, and thereby plays a role in the regulation of cell survival and apoptosis. Depending on the context, it can promote cell proliferation or apoptosis. Plays a role in the regulation of cell migration by modulating the levels of MMP2, a matrix protease that is under transcriptional control of P53/TP53. Does not bind calcium (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homodimer. Interacts with AGER (By similarity). {ECO:0000250}. +Q8BGP6 S2540_MOUSE Solute carrier family 25 member 40 337 37,964 Alternative sequence (1); Chain (1); Repeat (3); Sequence conflict (3); Transmembrane (6) TRANSMEM 20 40 Helical; Name=1. {ECO:0000255}.; TRANSMEM 104 124 Helical; Name=2. {ECO:0000255}.; TRANSMEM 146 166 Helical; Name=3. {ECO:0000255}.; TRANSMEM 200 221 Helical; Name=4. {ECO:0000255}.; TRANSMEM 240 260 Helical; Name=5. {ECO:0000255}.; TRANSMEM 299 319 Helical; Name=6. {ECO:0000255}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q497L8 S22AG_MOUSE Solute carrier family 22 member 16 (Carnitine transporter 2) (CT2) 649 73,933 Alternative sequence (1); Chain (1); Glycosylation (3); Transmembrane (12) TRANSMEM 19 39 Helical. {ECO:0000255}.; TRANSMEM 156 176 Helical. {ECO:0000255}.; TRANSMEM 190 210 Helical. {ECO:0000255}.; TRANSMEM 214 234 Helical. {ECO:0000255}.; TRANSMEM 244 264 Helical. {ECO:0000255}.; TRANSMEM 268 288 Helical. {ECO:0000255}.; TRANSMEM 356 376 Helical. {ECO:0000255}.; TRANSMEM 389 409 Helical. {ECO:0000255}.; TRANSMEM 417 437 Helical. {ECO:0000255}.; TRANSMEM 445 465 Helical. {ECO:0000255}.; TRANSMEM 475 495 Helical. {ECO:0000255}.; TRANSMEM 501 521 Helical. {ECO:0000255}. FUNCTION: High affinity carnitine transporter; the uptake is partially sodium-ion dependent. Thought to mediate the L-carnitine secretion mechanism from testis epididymal epithelium into the lumen which is involved in the maturation of spermatozoa. Also transports organic cations such as tetraethylammonium (TEA) and doxorubicin. The uptake of TEA is inhibited by various organic cations. The uptake of doxorubicin is sodium-independent (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cell membrane {ECO:0000250}. +Q9Z306 S22A4_MOUSE Solute carrier family 22 member 4 (Organic cation/carnitine transporter 1) 553 62,290 Chain (1); Glycosylation (3); Nucleotide binding (1); Topological domain (13); Transmembrane (12) TRANSMEM 21 41 Helical; Name=1. {ECO:0000255}.; TRANSMEM 143 163 Helical; Name=2. {ECO:0000255}.; TRANSMEM 172 192 Helical; Name=3. {ECO:0000255}.; TRANSMEM 198 218 Helical; Name=4. {ECO:0000255}.; TRANSMEM 233 253 Helical; Name=5. {ECO:0000255}.; TRANSMEM 258 278 Helical; Name=6. {ECO:0000255}.; TRANSMEM 340 360 Helical; Name=7. {ECO:0000255}.; TRANSMEM 374 394 Helical; Name=8. {ECO:0000255}.; TRANSMEM 401 421 Helical; Name=9. {ECO:0000255}.; TRANSMEM 429 449 Helical; Name=10. {ECO:0000255}.; TRANSMEM 463 483 Helical; Name=11. {ECO:0000255}.; TRANSMEM 489 509 Helical; Name=12. {ECO:0000255}. TOPO_DOM 1 20 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 42 142 Extracellular. {ECO:0000255}.; TOPO_DOM 164 171 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 193 197 Extracellular. {ECO:0000255}.; TOPO_DOM 219 232 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 254 257 Extracellular. {ECO:0000255}.; TOPO_DOM 279 339 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 361 373 Extracellular. {ECO:0000255}.; TOPO_DOM 395 400 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 422 428 Extracellular. {ECO:0000255}.; TOPO_DOM 450 462 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 484 488 Extracellular. {ECO:0000255}.; TOPO_DOM 510 553 Cytoplasmic. {ECO:0000255}. FUNCTION: Sodium-ion dependent, low affinity carnitine transporter. Probably transports one sodium ion with one molecule of carnitine. Also transports organic cations such as tetraethylammonium (TEA) without the involvement of sodium. Relative uptake activity ratio of carnitine to TEA is 1.78. {ECO:0000269|PubMed:11010964}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11010964}; Multi-pass membrane protein {ECO:0000269|PubMed:11010964}. SUBUNIT: Interacts with PDZK1. {ECO:0000269|PubMed:14531806}. TISSUE SPECIFICITY: Expressed in kidney, liver and testis. Weakly expressed in other tissues. {ECO:0000269|PubMed:11010964}. +P59530 TA2R7_MOUSE Taste receptor type 2 member 7 (T2R7) (STC7-4) (T2R30) (T2R6) (mT2R42) 312 35,510 Chain (1); Glycosylation (2); Sequence conflict (13); Topological domain (8); Transmembrane (7) TRANSMEM 10 30 Helical; Name=1. {ECO:0000255}.; TRANSMEM 50 70 Helical; Name=2. {ECO:0000255}.; TRANSMEM 102 122 Helical; Name=3. {ECO:0000255}.; TRANSMEM 129 149 Helical; Name=4. {ECO:0000255}.; TRANSMEM 188 208 Helical; Name=5. {ECO:0000255}.; TRANSMEM 236 256 Helical; Name=6. {ECO:0000255}.; TRANSMEM 267 287 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 9 Extracellular. {ECO:0000255}.; TOPO_DOM 31 49 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 71 101 Extracellular. {ECO:0000255}.; TOPO_DOM 123 128 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 150 187 Extracellular. {ECO:0000255}.; TOPO_DOM 209 235 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 257 266 Extracellular. {ECO:0000255}.; TOPO_DOM 288 312 Cytoplasmic. {ECO:0000255}. FUNCTION: Gustducin-coupled receptor implicated in the perception of bitter compounds in the oral cavity and the gastrointestinal tract. Signals through PLCB2 and the calcium-regulated cation channel TRPM5. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed in subsets of taste receptor cells of the tongue and palate epithelium and exclusively in gustducin-positive cells. Expressed in 15% taste bud cells in circumvallate and foliate papillae but only in 2% in fungiform papillae. Expressed in gastric and duodenal tissues. +Q5QD06 TAA8B_MOUSE Trace amine-associated receptor 8b (TaR-8b) (Trace amine receptor 8b) (mTaar8b) 344 38,006 Chain (1); Disulfide bond (1); Glycosylation (2); Topological domain (8); Transmembrane (7) TRANSMEM 32 52 Helical; Name=1. {ECO:0000255}.; TRANSMEM 68 88 Helical; Name=2. {ECO:0000255}.; TRANSMEM 112 132 Helical; Name=3. {ECO:0000255}.; TRANSMEM 147 167 Helical; Name=4. {ECO:0000255}.; TRANSMEM 196 216 Helical; Name=5. {ECO:0000255}.; TRANSMEM 261 281 Helical; Name=6. {ECO:0000255}.; TRANSMEM 283 303 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 31 Extracellular. {ECO:0000255}.; TOPO_DOM 53 67 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 89 111 Extracellular. {ECO:0000255}.; TOPO_DOM 133 146 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 168 195 Extracellular. {ECO:0000255}.; TOPO_DOM 217 260 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 282 282 Extracellular. {ECO:0000255}.; TOPO_DOM 304 344 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan olfactory receptor specific for trace amines. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Specifically expressed in neurons of the olfactory epithelium. {ECO:0000269|PubMed:16878137}. +Q7TQA7 TA2R3_MOUSE Taste receptor type 2 member 3 (T2R3) (T2R137) (T2R37) (mT2r41) 316 36,289 Chain (1); Erroneous gene model prediction (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 8 28 Helical; Name=1. {ECO:0000255}.; TRANSMEM 51 71 Helical; Name=2. {ECO:0000255}.; TRANSMEM 87 107 Helical; Name=3. {ECO:0000255}.; TRANSMEM 129 149 Helical; Name=4. {ECO:0000255}.; TRANSMEM 187 207 Helical; Name=5. {ECO:0000255}.; TRANSMEM 235 255 Helical; Name=6. {ECO:0000255}.; TRANSMEM 267 287 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 7 Extracellular. {ECO:0000255}.; TOPO_DOM 29 50 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 72 86 Extracellular. {ECO:0000255}.; TOPO_DOM 108 128 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 150 186 Extracellular. {ECO:0000255}.; TOPO_DOM 208 234 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 256 266 Extracellular. {ECO:0000255}.; TOPO_DOM 288 316 Cytoplasmic. {ECO:0000255}. FUNCTION: Gustducin-coupled receptor implicated in the perception of bitter compounds in the oral cavity and the gastrointestinal tract. Signals through PLCB2 and the calcium-regulated cation channel TRPM5 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. +Q5QD17 TAAR2_MOUSE Trace amine-associated receptor 2 (TaR-2) (Trace amine receptor 2) (mTaar2) (G-protein coupled receptor 58) 339 38,517 Chain (1); Disulfide bond (1); Glycosylation (2); Topological domain (8); Transmembrane (7) TRANSMEM 37 57 Helical; Name=1. {ECO:0000255}.; TRANSMEM 68 88 Helical; Name=2. {ECO:0000255}.; TRANSMEM 107 127 Helical; Name=3. {ECO:0000255}.; TRANSMEM 151 171 Helical; Name=4. {ECO:0000255}.; TRANSMEM 196 216 Helical; Name=5. {ECO:0000255}.; TRANSMEM 252 272 Helical; Name=6. {ECO:0000255}.; TRANSMEM 288 310 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 36 Extracellular. {ECO:0000255}.; TOPO_DOM 58 67 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 89 106 Extracellular. {ECO:0000255}.; TOPO_DOM 128 150 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 172 195 Extracellular. {ECO:0000255}.; TOPO_DOM 217 251 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 273 287 Extracellular. {ECO:0000255}.; TOPO_DOM 311 339 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan olfactory receptor specific for trace amines. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Specifically expressed in neurons of the olfactory epithelium. {ECO:0000269|PubMed:16878137}. +Q9JKT3 TA2R4_MOUSE Taste receptor type 2 member 4 (T2R4) (Taste receptor type 2 member 8) (T2R8) 297 34,202 Chain (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 12 32 Helical; Name=1. {ECO:0000255}.; TRANSMEM 47 67 Helical; Name=2. {ECO:0000255}.; TRANSMEM 81 101 Helical; Name=3. {ECO:0000255}.; TRANSMEM 129 149 Helical; Name=4. {ECO:0000255}.; TRANSMEM 172 192 Helical; Name=5. {ECO:0000255}.; TRANSMEM 230 250 Helical; Name=6. {ECO:0000255}.; TRANSMEM 261 281 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 11 Extracellular. {ECO:0000255}.; TOPO_DOM 33 46 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 68 80 Extracellular. {ECO:0000255}.; TOPO_DOM 102 128 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 150 171 Extracellular. {ECO:0000255}.; TOPO_DOM 193 229 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 251 260 Extracellular. {ECO:0000255}.; TOPO_DOM 282 297 Cytoplasmic. {ECO:0000255}. FUNCTION: Gustducin-coupled receptor for denatonium and N(6)-propyl-2-thiouracil implicated in the perception of bitter compounds in the oral cavity and the gastrointestinal tract. Signals through PLCB2 and the calcium-regulated cation channel TRPM5. In airway epithelial cells, binding of denatonium increases the intracellular calcium ion concentration and stimulates ciliary beat frequency (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Cell projection, cilium membrane. Note=In airway epithelial cells, localizes to motile cilia. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in subsets of taste receptor cells of the tongue and palate epithelium and exclusively in gustducin-positive cells. Expressed in 15% taste bud cells in circumvallate and foliate papillae but only in 2% in fungiform papillae. +Q9CZT5 VASN_MOUSE Vasorin (Protein slit-like 2) 673 72,261 Chain (1); Disulfide bond (3); Domain (4); Glycosylation (6); Repeat (10); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 577 597 Helical. {ECO:0000255}. TOPO_DOM 25 576 Extracellular. {ECO:0000255}.; TOPO_DOM 598 673 Cytoplasmic. {ECO:0000255}. FUNCTION: May act as an inhibitor of TGF-beta signaling. {ECO:0000250}. PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Interacts with TGFB1, TGFB2 and TGFB3. {ECO:0000250}. +P70460 VASP_MOUSE Vasodilator-stimulated phosphoprotein (VASP) 375 39,667 Chain (1); Coiled coil (1); Compositional bias (2); Domain (1); Erroneous gene model prediction (1); Initiator methionine (1); Modified residue (12); Motif (1); Mutagenesis (4); Natural variant (1); Region (5); Repeat (2); Sequence conflict (3) FUNCTION: Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance, lamellipodial and filopodial dynamics, platelet activation and cell migration. VASP promotes actin filament elongation. It protects the barbed end of growing actin filaments against capping and increases the rate of actin polymerization in the presence of capping protein. VASP stimulates actin filament elongation by promoting the transfer of profilin-bound actin monomers onto the barbed end of growing actin filaments. Plays a role in actin-based mobility of Listeria monocytogenes in host cells. Regulates actin dynamics in platelets and plays an important role in regulating platelet aggregation (By similarity). {ECO:0000250, ECO:0000269|PubMed:10660044}. PTM: Major substrate for cAMP-dependent (PKA) and cGMP-dependent protein kinase (PKG) in platelets. The preferred site for PKA is Ser-153, the preferred site for PKG, Ser-235. In ADP-activated platelets, phosphorylation by PKA or PKG/PRKG1 on Ser-153 leads to fibrinogen receptor inhibition. Phosphorylation on Thr-274 requires prior phosphorylation on Ser-153 and Ser-235. In response to phorbol ester (PMA) stimulation, phosphorylated by PKC/PRKCA. In response to thrombin, phosphorylated by both PKC and ROCK1. Phosphorylation at Thr-274 by AMPK does not require prior phosphorylation at Ser-153 or Ser-235. Phosphorylation at Ser-153 by PKA is required for localization to the tight junctions in epithelial cells. Phosphorylation modulates F-actin binding, actin filament elongation and platelet activation. Phosphorylation at Ser-318 by AMPK also alters actin filament binding. Carbon monoxide (CO) promotes phosphorylation at Ser-153, while nitric oxide (NO) promotes phosphorylation at Ser-153, but also at Ser-235. {ECO:0000269|PubMed:10085070, ECO:0000269|PubMed:10882740, ECO:0000269|PubMed:12372613, ECO:0000269|PubMed:21945940}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10660044}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10660044}. Cell junction, focal adhesion {ECO:0000269|PubMed:10660044}. Cell junction, tight junction {ECO:0000250}. Cell projection, lamellipodium membrane {ECO:0000269|PubMed:10660044}. Cell projection, filopodium membrane {ECO:0000269|PubMed:10660044}. Note=Targeted to stress fibers and focal adhesions through interaction with a number of proteins including MRL family members. Localizes to the plasma membrane in protruding lamellipodia and filopodial tips. Stimulation by thrombin or PMA, also translocates VASP to focal adhesions. Localized along the sides of actin filaments throughout the peripheral cytoplasm under basal conditions (By similarity). In pre-apoptotic cells, colocalizes with MEFV in large specks (pyroptosomes) (By similarity). {ECO:0000250}. SUBUNIT: Homotetramer (By similarity). Interacts with PFN1, PFN2, LPP, ACTN1 and ACTG1. Interacts, via the EVH1 domain, with the Pro-rich regions of ZYX. This interaction is important for targeting to focal adhesions and the formation of actin-rich structures at the apical surface of cells. Interacts, via the EVH1 domain, with the Pro-rich domain of Listeria monocytogenes actA. Interacts with APBB1IP. Interacts, via the Pro-rich domain, with the C-terminal SH3 domain of DNMBP. Interacts weakly with MEFV (By similarity). {ECO:0000250}. DOMAIN: The EVH2 domain is comprised of 3 regions. Block A is a thymosin-like domain required for G-actin binding. The KLKR motif within this block is essential for the G-actin binding and for actin polymerization. Block B is required for F-actin binding and subcellular location, and Block C for tetramerization.; DOMAIN: The WH1 domain mediates interaction with XIRP1. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in thymus and spleen. Lower levels in lung, ovary, placenta and fat. {ECO:0000269|PubMed:10069337}. +Q8R0L9 TADA3_MOUSE Transcriptional adapter 3 (ADA3 homolog) (mADA3) (Transcriptional adapter 3-like) (ADA3-like protein) 432 48,900 Alternative sequence (2); Chain (1); Coiled coil (2); Cross-link (2); Modified residue (3); Sequence conflict (3) FUNCTION: Functions as a component of the PCAF complex. The PCAF complex is capable of efficiently acetylating histones in a nucleosomal context. The PCAF complex could be considered as the human version of the yeast SAGA complex. Also known as a coactivator for p53/TP53-dependent transcriptional activation (By similarity). Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: The PCAF complex is composed of a number of TBP-associated factors (TAFS), such as TAF5, TAF5L, TAF6, TAF6L, TAF9, TAF10 and TAF12, PCAF, and also PCAF-associated factors (PAFs), such as TADA2L/ADA2, TADA3L/ADA3 and SPT3. Interacts directly with TADA2L and PCAF and also with the high-risk HPV oncoprotein E6. Component of the STAGA transcription coactivator-HAT complex, at least composed of SUPT3H, GCN5L2, TAF5L, TAF6L, SUPT7L, TADA3L, TAD1L, TAF10, TAF12, TRRAP and TAF9. Component of the TFTC-HAT complex (By similarity). Component of the ADA2A-containing complex (ATAC), composed of KAT14, KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1 (By similarity). {ECO:0000250}. +Q9R1C0 TAF7_MOUSE Transcription initiation factor TFIID subunit 7 (RNA polymerase II TBP-associated factor subunit F) (Transcription initiation factor TFIID 55 kDa subunit) (TAF(II)55) (TAFII-55) (TAFII55) 341 39,126 Chain (1); Coiled coil (1); Modified residue (5); Motif (1) FUNCTION: Functions as a component of the DNA-binding general transcription factor complex TFIID, a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. Present in both of the previously described TFIID species which either lack or contain TAFII30 (TFIID alpha and TFIID beta respectively). {ECO:0000269|PubMed:10438527}. PTM: Phosphorylated by CIITA. Phosphorylation at Ser-256 by TAF1 in early G1 phase disrupts binding to TAF1 (By similarity). {ECO:0000250|UniProtKB:Q15545}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10438527}. SUBUNIT: TFIID is composed of TATA binding protein (TBP) and a number of TBP-associated factors (TAFs) (PubMed:10438527). Part of a TFIID-containing RNA polymerase II pre-initiation complex that is composed of TBP and at least GTF2A1, GTF2A2, GTF2E1, GTF2E2, GTF2F1, GTF2H2, GTF2H3, GTF2H4, GTF2H5, GTF2B, TCEA1, ERCC2, ERCC3, TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13. Interacts with TAF1; the interaction is direct (By similarity). Interacts with TAFII250, TAFII100, TAFII28, TAFII20, and TAFII18, but not with TAFII30 or TBP (PubMed:10438527). Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Binds to CIITA and TAF1 and inhibits their acetyltransferase activity, thereby repressing activated transcription and behaving as a repressor at these promoters (By similarity). {ECO:0000250|UniProtKB:Q15545, ECO:0000269|PubMed:10438527}. DOMAIN: The [KR]-[STA]-K motif is specifically recognized by the SETD7 methyltransferase. {ECO:0000250}. +Q921F2 TADBP_MOUSE TAR DNA-binding protein 43 (TDP-43) 414 44,548 Beta strand (5); Chain (1); Compositional bias (1); Cross-link (6); Domain (2); Helix (2); Modified residue (3); Region (1); Sequence conflict (3); Turn (1) FUNCTION: DNA and RNA-binding protein which regulates transcription and splicing. Involved in the regulation of CFTR splicing. It promotes CFTR exon 9 skipping by binding to the UG repeated motifs in the polymorphic region near the 3'-splice site of this exon. The resulting aberrant splicing is associated with pathological features typical of cystic fibrosis. May also be involved in microRNA biogenesis, apoptosis and cell division. Can repress HIV-1 transcription by binding to the HIV-1 long terminal repeat. Stabilizes the low molecular weight neurofilament (NFL) mRNA through a direct interaction with the 3' UTR. {ECO:0000250|UniProtKB:Q13148}. PTM: Hyperphosphorylated. {ECO:0000250}.; PTM: Ubiquitinated. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13148}. SUBUNIT: Homodimer. Interacts with BRDT (PubMed:22570411). Binds specifically to pyrimidine-rich motifs of TAR DNA and to single stranded TG repeated sequences. Binds to RNA, specifically to UG repeated sequences with a minimum of six contiguous repeats. Interacts with ATNX2; the interaction is RNA-dependent. Interacts with MATR3. Interacts with UBQLN2. Interacts with HNRNPA2B1 (By similarity). Interacts with ZNF106 (PubMed:28072389). {ECO:0000250|UniProtKB:Q13148, ECO:0000269|PubMed:22570411, ECO:0000269|PubMed:28072389}. DOMAIN: The RRM domains can bind to both DNA and RNA. +Q99KW3 TARA_MOUSE TRIO and F-actin-binding protein (Protein Tara) (Trio-associated repeat on actin) 2014 223,368 Alternative sequence (5); Chain (1); Coiled coil (1); Domain (1); Erroneous initiation (1); Modified residue (5); Sequence conflict (8) FUNCTION: May regulate actin cytoskeletal organization, cell spreading and cell contraction by directly binding and stabilizing filamentous F-actin. The localized formation of TARA and TRIO complexes coordinates the amount of F-actin present in stress fibers. May also serve as a linker protein to recruit proteins required for F-actin formation and turnover. PTM: Ubiquitinated by HECTD3, leading to its degradation by the proteasome. {ECO:0000250}.; PTM: Isoform 1: Phosphorylation at Thr-445 by PLK1 ensures mitotic progression and is essential for accurate chromosome segregation. {ECO:0000250|UniProtKB:Q9H2D6}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Localized to F-actin in a periodic pattern. {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 1: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Midbody {ECO:0000250}. Note=Centrosomal localization occurs upon phosphorylation by PLK1 at Thr-445 and lasts from prophase to anaphase. At telophase, relocalizes to midbody (By similarity). {ECO:0000250}. SUBUNIT: Binds to TRIO and F-actin. May also interact with myosin II (By similarity). Interacts with HECTD3 (By similarity). {ECO:0000250}. DOMAIN: Contains at least 2 actin-binding sites per coiled-coil dimer. {ECO:0000250}. +B6A8R8 TARM1_MOUSE T-cell-interacting, activating receptor on myeloid cells protein 1 (OSCAR-like transcript-2 protein) (OLT-2) 288 31,392 Chain (1); Disulfide bond (2); Domain (2); Glycosylation (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 259 279 Helical. {ECO:0000255}. TOPO_DOM 17 258 Extracellular. {ECO:0000255}.; TOPO_DOM 280 288 Cytoplasmic. {ECO:0000255}. FUNCTION: May act as receptor. Negatively regulates TCR-mediated CD4(+) T cell proliferation and activation, possibly by binding an unknown ligand on the T cell surface. Enhances Toll-like receptor-mediated production of pro-inflammatory cytokines by macrophages and neutrophils. {ECO:0000269|PubMed:26311901}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:B6A8C7}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26311901}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Interacts with Fc receptor gamma chain FCER1G. {ECO:0000250|UniProtKB:B6A8C7}. TISSUE SPECIFICITY: Expressed in lung, uterus, lymph nodes, spleen, thymus and bone marrow. Expressed in bone marrow CD11b(+)Gr-1(+) granulocyte precursors and mature neutrophils. {ECO:0000269|PubMed:26311901}. +Q69ZR9 TASOR_MOUSE Protein TASOR (Transgene activation suppressor protein) 1610 181,396 Alternative sequence (4); Chain (1); Cross-link (4); Initiator methionine (1); Modified residue (12); Mutagenesis (1) FUNCTION: Component of the HUSH complex, a multiprotein complex that mediates epigenetic repression. The HUSH complex is recruited to genomic loci rich in H3K9me3 and is probably required to maintain transcriptional silencing by promoting recruitment of SETDB1, a histone methyltransferase that mediates further deposition of H3K9me3. {ECO:0000250|UniProtKB:Q9UK61}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24781204}. Chromosome {ECO:0000250|UniProtKB:Q9UK61}. Note=Localizes to chromatin. {ECO:0000250|UniProtKB:Q9UK61}. SUBUNIT: Component of the HUSH complex; at least composed of FAM208A/TASOR, PPHLN1 and MPHOSPH8. {ECO:0000250|UniProtKB:Q9UK61}. TISSUE SPECIFICITY: Present in skin, brain and testis (at protein level). {ECO:0000269|PubMed:24781204}. +Q6P8M1 TATD1_MOUSE Putative deoxyribonuclease TATDN1 (EC 3.1.21.-) 295 33,365 Alternative sequence (2); Chain (1); Metal binding (5); Modified residue (2) FUNCTION: Putative deoxyribonuclease. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q3U1C6 TATD3_MOUSE Putative deoxyribonuclease TATDN3 (EC 3.1.21.-) 294 32,436 Alternative sequence (3); Chain (1); Erroneous initiation (1); Metal binding (7); Sequence conflict (1) FUNCTION: Putative deoxyribonuclease. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q8C9V1 TB10C_MOUSE Carabin (TBC1 domain family member 10C) 444 49,930 Alternative sequence (4); Chain (1); Domain (1); Erroneous initiation (1); Region (1); Site (2) FUNCTION: Inhibits the Ras signaling pathway through its intrinsic Ras GTPase-activating protein (GAP) activity. Acts as a negative feedback inhibitor of the calcineurin signaling pathway that also mediates crosstalk between calcineurin and Ras (By similarity). {ECO:0000250}. SUBUNIT: Interacts with both calcineurin and HRAS. {ECO:0000250}. DOMAIN: The arginine and glutamine fingers are critical for the GTPase-activating mechanism, they pull out Rab's 'switch 2' glutamine and insert in Rab's active site. {ECO:0000250}. +P10637 TAU_MOUSE Microtubule-associated protein tau (Neurofibrillary tangle protein) (Paired helical filament-tau) (PHF-tau) 733 76,243 Alternative sequence (6); Chain (1); Cross-link (16); Disulfide bond (1); Glycosylation (1); Helix (1); Initiator methionine (1); Modified residue (68); Repeat (4); Sequence conflict (6) FUNCTION: Promotes microtubule assembly and stability, and might be involved in the establishment and maintenance of neuronal polarity. The C-terminus binds axonal microtubules while the N-terminus binds neural plasma membrane components, suggesting that tau functions as a linker protein between both. Axonal polarity is predetermined by tau localization (in the neuronal cell) in the domain of the cell body defined by the centrosome. The short isoforms allow plasticity of the cytoskeleton whereas the longer isoforms may preferentially play a role in its stabilization. PTM: Polyubiquitinated. Requires functional TRAF6 and may provoke SQSTM1-dependent degradation by the proteasome (By similarity). {ECO:0000250}.; PTM: Phosphorylation at various serine and threonine residues in S-P or T-P motifs by proline-directed protein kinases (PDPK1, CDK1, CDK5, GSK3, MAPK) (a few sites per protein in interphase, more in mitosis), and at serine residues in K-X-G-S motifs by MAP/microtubule affinity-regulating kinase (MARK1, MARK2, MARK3, MARK4), causing detachment from microtubules, and their disassembly (By similarity). Phosphorylated by PHK. Dephosphorylation at several serine and threonine residues by the serine/threonine phosphatase PPP5C. Phosphorylation at Ser-554 by BRSK1 and BRSK2 in neurons affects ability to bind microtubules and plays a role in neuron polarization. Phosphorylation at Ser-188 by SGK1 mediates microtubule depolymerization and neurite formation in hippocampal neurons (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P10636}. SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Cell projection, axon. Cytoplasm {ECO:0000250|UniProtKB:P10636}. Cell projection, dendrite {ECO:0000250|UniProtKB:P10636}. Note=Mostly found in the axons of neurons, in the cytosol and in association with plasma membrane components. SUBUNIT: Interacts with MARK1, MARK2, MARK3 AND MARK4 (By similarity). Interacts with SQSTM1 when polyubiquitinated (By similarity). Interacts with PSMC2 through SQSTM1. Interacts with FKBP4. Binds to CSNK1D (By similarity). Interacts with SGK1 (By similarity). Interacts with EPM2A; the interaction dephosphorylates MAPT at Ser-369 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P10636}. DOMAIN: The tau/MAP repeat binds to tubulin. Type I isoforms contain 3 repeats while type II isoforms contain 4 repeats. TISSUE SPECIFICITY: Expressed in neurons and at a lower level in the liver and kidney. Isoform PNS-tau is expressed in the peripheral nervous system while the others are expressed in the central nervous system. DISEASE: Note=May be involved in the pathogenesis of cytoplasmic inclusions (as Mallory bodies) in livers of mice chronically intoxicated with Griseofulvin or DDC (3,5-diethoxycarbonyl-2,4-dihydrocollidine), a model for human alcoholic hepatitis. Alteration of Tau (abnormal phosphorylation and cross-linking) could contribute to Mallory bodies formation and disturbance of microtubule function in alcoholic liver disease. +Q7TSD4 TBATA_MOUSE Protein TBATA (Protein SPATIAL) (Stromal protein associated with thymii and lymph node) (Thymus, brain and testes-associated protein) 393 43,842 Alternative sequence (8); Chain (1); Erroneous initiation (2); Frameshift (1) FUNCTION: Isoform 1 and isoform 2 may play a role in spermatid differentiation. Isoform 1 and isoform 2 regulate thymus function by modulating stromal cell proliferation via interference with the NEDD8 pathway. {ECO:0000269|PubMed:17196196, ECO:0000269|PubMed:20937703}. SUBCELLULAR LOCATION: Isoform 1: Cytoplasm, cytosol {ECO:0000269|PubMed:17196196}. Note=Located throughout the cytosol of early round spermatids. By the end stages of round spermatid development, concentrated at the side of the cell near the nascent flagellum and in the manchette. In mature sperm, located in the principle piece of the tail. {ECO:0000269|PubMed:17196196}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm, cytosol {ECO:0000269|PubMed:17196196}. Note=Located throughout the cytosol of early round spermatids. By the end stages of round spermatid development, concentrated at the side of the cell near the nascent flagellum and in the manchette. In mature sperm, located in the principle piece of the tail. {ECO:0000269|PubMed:17196196}.; SUBCELLULAR LOCATION: Isoform 6: Nucleus {ECO:0000269|PubMed:11196687}.; SUBCELLULAR LOCATION: Isoform 7: Nucleus {ECO:0000269|PubMed:11196687}. SUBUNIT: Interacts with KIF17. Interacts with UBA3. {ECO:0000269|PubMed:17196196, ECO:0000269|PubMed:17961552, ECO:0000269|PubMed:20937703}. TISSUE SPECIFICITY: Expressed in the subcapsular region of the thymus and lymph node (at protein level). Highly expressed in thymic cortical stromal cells and testis. Lower levels found in brain cortex, hippocampus, kidney, cerebellum, skeletal muscle, epididymis and ovary. No expression detected in other lymphoid organs including bone marrow and spleen. Isoform 1 and isoform 2 are expressed predominantly in testis. Isoform 3, isoform 4 and isoform 5 are expressed predominantly in thymus although isoform 3 is also expressed in testis. In the CNS, highly expressed in restricted areas, the cerebellum and hippocampus. {ECO:0000269|PubMed:12711538}. +Q6NXY1 TBC31_MOUSE TBC1 domain family member 31 (Protein 4-B-3) (WD repeat-containing protein 67) 996 115,838 Alternative sequence (3); Chain (1); Coiled coil (2); Domain (1); Repeat (7); Sequence caution (3); Sequence conflict (4) +Q8CGA2 TBC14_MOUSE TBC1 domain family member 14 694 78,315 Chain (1); Domain (1); Erroneous initiation (3); Modified residue (2); Sequence conflict (3) FUNCTION: Negative regulator of starvation-induced autophagosome formation. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network {ECO:0000250}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Note=After amino acid starvation, Golgi apparatus-associated protein levels increase compared with fed conditions. May be cycling between the Golgi apparatus and an endosomal pool, redistributing to the Golgi apparatus upon starvation (By similarity). {ECO:0000250}. SUBUNIT: Interacts with ULK1. May interact with RAB11A and RAB11B, but does not exhibit any GTPase-activating activity toward these proteins (By similarity). {ECO:0000250}. +P68372 TBB4B_MOUSE Tubulin beta-4B chain (Tubulin beta-2C chain) 445 49,831 Chain (1); Modified residue (4); Nucleotide binding (1); Sequence conflict (2) FUNCTION: Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. PTM: Some glutamate residues at the C-terminus are polyglycylated, resulting in polyglycine chains on the gamma-carboxyl group. Glycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Both modifications can coexist on the same protein on adjacent residues, and lowering polyglycylation levels increases polyglutamylation, and reciprocally. The precise function of polyglycylation is still unclear. {ECO:0000269|PubMed:19524510}.; PTM: Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (PubMed:15890843). Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity by SPAST increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold (By similarity). {ECO:0000250|UniProtKB:Q71U36, ECO:0000269|PubMed:15890843}.; PTM: Phosphorylated on Ser-172 by CDK1 during the cell cycle, from metaphase to telophase, but not in interphase. This phosphorylation inhibits tubulin incorporation into microtubules. {ECO:0000250|UniProtKB:P68371}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SUBUNIT: Dimer of alpha and beta chains. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells. DOMAIN: The highly acidic C-terminal region may bind cations such as calcium. TISSUE SPECIFICITY: Widely expressed. Expressed in the retina and the cochlea. {ECO:0000269|PubMed:29198720}. +Q9CWU0 TDR12_MOUSE Putative ATP-dependent RNA helicase TDRD12 (EC 3.6.4.13) (ES cell-associated transcript 8 protein) (Tudor domain-containing protein 12) 1215 137,627 Alternative sequence (2); Chain (1); Domain (4); Motif (1); Nucleotide binding (1); Sequence conflict (1) FUNCTION: Probable ATP-binding RNA helicase required during spermatogenesis to repress transposable elements and preventing their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons (PubMed:24067652). Involved in the secondary piRNAs metabolic process (PubMed:24067652). Acts via the PET complex, a multiprotein complex required during the secondary piRNAs metabolic process for the PIWIL2 slicing-triggered loading of PIWIL4 piRNAs (PubMed:26669262). {ECO:0000269|PubMed:24067652, ECO:0000269|PubMed:26669262}. SUBUNIT: Component of a mRNP complex containing PIWIL2, TDRD1 and piRNAs (PubMed:24067652). Component of the PET complex, at least composed of EXD1, PIWIL2, TDRD12 and piRNAs (PubMed:26669262). {ECO:0000269|PubMed:24067652, ECO:0000269|PubMed:26669262}. TISSUE SPECIFICITY: Restricted to the gonads. {ECO:0000269|PubMed:12787504, ECO:0000269|PubMed:24067652}. +Q3B807 TCRGL_MOUSE Transcription elongation regulator 1-like protein 590 66,376 Alternative sequence (3); Chain (1); Compositional bias (1); Domain (4); Erroneous initiation (3); Frameshift (1); Sequence caution (1); Sequence conflict (3) +Q14BI7 TDRD9_MOUSE ATP-dependent RNA helicase TDRD9 (EC 3.6.4.13) (Tudor domain-containing protein 9) 1383 155,980 Alternative sequence (3); Chain (1); Domain (3); Motif (1); Mutagenesis (1); Nucleotide binding (1) FUNCTION: ATP-binding RNA helicase which plays a central role during spermatogenesis by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity (PubMed:20059948, PubMed:28633017). Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons (PubMed:20059948, PubMed:28633017). Acts downstream of piRNA biogenesis: exclusively required for transposon silencing in the nucleus, suggesting that it acts as a nuclear effector in the nucleus together with PIWIL4 (PubMed:28633017). {ECO:0000269|PubMed:20059948, ECO:0000269|PubMed:28633017}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20011505, ECO:0000269|PubMed:20059948, ECO:0000269|PubMed:28633017}. Nucleus {ECO:0000269|PubMed:20059948, ECO:0000269|PubMed:28633017}. Note=Component of the nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis. Specifically localizes to piP-bodies, a subset of the nuage which contains secondary piRNAs. PIWIL2 is required for its localization to piP-bodies. {ECO:0000269|PubMed:20059948}. SUBUNIT: Interacts with piRNA-associated proteins PIWIL1 and PIWIL4. {ECO:0000269|PubMed:19584108, ECO:0000269|PubMed:20059948}. TISSUE SPECIFICITY: Predominantly expressed in reproductive organs. Detected in mitotic spermatogonia, meiotic spermatocytes (predominantly at the pachytene stage), haploid spermatids in the testis, and in growing oocytes in the ovary (at protein level). {ECO:0000269|PubMed:20059948}. +Q9QYM9 TEFF2_MOUSE Tomoregulin-2 (TR-2) (Transmembrane protein with EGF-like and two follistatin-like domains) 374 41,415 Alternative sequence (1); Chain (1); Compositional bias (1); Disulfide bond (9); Domain (3); Frameshift (1); Glycosylation (2); Region (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 321 341 Helical. {ECO:0000255}. TOPO_DOM 41 320 Extracellular. {ECO:0000255}.; TOPO_DOM 342 374 Cytoplasmic. {ECO:0000255}. FUNCTION: May be a survival factor for hippocampal and mesencephalic neurons. The shedded form may up-regulate cell proliferation (By similarity). {ECO:0000250}. PTM: N-glycosylated. Contains chondroitin sulfate glycosaminoglycans (By similarity). {ECO:0000250}.; PTM: A soluble form (TMEFF2-ECD) is produced by proteolytic shedding. This shedding can be induced by phorbol ester or proinflammatory cytokines such as TNFalpha, and is mediated by a metalloproteinase ADAM (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Widely expressed in the brain. In the olfactory bulb expressed in mitral cell, granule, and glomerular layers. In the hippocampus expressed in hippocampal cornu ammonis, pyramidal layer, dentate gyrus, and substantia nigra pars compacta. {ECO:0000269|PubMed:10903839}. +Q5SSK3 TEFM_MOUSE Transcription elongation factor, mitochondrial 364 41,874 Chain (1); Transit peptide (1) FUNCTION: Transcription elongation factor which increases mitochondrial RNA polymerase processivity. Regulates transcription of the mitochondrial genome, including genes important for the oxidative phosphorylation machinery (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. Mitochondrion matrix, mitochondrion nucleoid {ECO:0000250}. SUBUNIT: Interacts with POLRMT. {ECO:0000250}. +P0DMR5 TDPZ1_MOUSE TD and POZ domain-containing protein 1 (MAPP family protein 2) 365 41,584 Chain (1); Domain (2); Erroneous initiation (1); Sequence conflict (11) +Q80Z71 TENN_MOUSE Tenascin-N (TN-N) (Tenascin-W) (TN-W) 1560 173,090 Alternative sequence (1); Chain (1); Disulfide bond (9); Domain (16); Glycosylation (1); Sequence conflict (6); Signal peptide (1) FUNCTION: Extracellular matrix protein that seems to be a ligand for ITGA8:ITGB1, ITGAV:ITGB1 and ITGA4:ITGB1 (By similarity) (PubMed:14709716). Involved in neurite outgrowth and cell migration in hippocampal explants (PubMed:12812753). During endochondral bone formation, inhibits proliferation and differentiation of proteoblasts mediated by canonical WNT signaling (PubMed:17395156). In tumors, stimulates angiogenesis by elongation, migration and sprouting of endothelial cells (By similarity). Expressed in most mammary tumors, may facilitate tumorigenesis by supporting the migratory behavior of breast cancer cells (PubMed:15592496). {ECO:0000250|UniProtKB:Q9UQP3, ECO:0000269|PubMed:12812753, ECO:0000269|PubMed:14709716, ECO:0000269|PubMed:15592496, ECO:0000269|PubMed:17395156}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:15592496}. SUBUNIT: Homohexamer. {ECO:0000269|PubMed:14709716}. TISSUE SPECIFICITY: Highest expression in kidney followed by spleen and brain. In brain, highest expression is found in hippocampus, cerebellum and olfactory bulb. Expressed in aortic valve, corneal limbus (PubMed:14709716). Expressed in ribs periosteum. During a fracture repair process, expression increases in cells of newly formed perichondrium/peristeum surrounding the cartalaginous callus (PubMed:14709716, PubMed:17395156). {ECO:0000269|PubMed:12812753, ECO:0000269|PubMed:14709716, ECO:0000269|PubMed:17395156}. +Q9DAJ2 TEKT1_MOUSE Tektin-1 418 48,641 Chain (1); Coiled coil (4) FUNCTION: Structural component of ciliary and flagellar microtubules. Forms filamentous polymers in the walls of ciliary and flagellar microtubules (By similarity). {ECO:0000250}. +Q8R2Q6 TECT3_MOUSE Tectonic-3 595 64,824 Alternative sequence (4); Chain (1); Compositional bias (1); Glycosylation (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 576 594 Helical. {ECO:0000255}. TOPO_DOM 23 575 Extracellular. {ECO:0000255}.; TOPO_DOM 595 595 Cytoplasmic. {ECO:0000255}. FUNCTION: Part of the tectonic-like complex which is required for tissue-specific ciliogenesis and may regulate ciliary membrane composition. May be involved in apoptosis regulation (By similarity). Necessary for signal transduction through the sonic hedgehog (Shh) signaling pathway. {ECO:0000250, ECO:0000269|PubMed:21725307}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Part of the tectonic-like complex (also named B9 complex). {ECO:0000269|PubMed:21725307}. +Q3URK3 TET1_MOUSE Methylcytosine dioxygenase TET1 (EC 1.14.11.n2) (CXXC-type zinc finger protein 6) (Ten-eleven translocation 1 gene protein homolog) 2007 219,261 Binding site (4); Chain (1); Erroneous initiation (1); Metal binding (15); Modified residue (1); Mutagenesis (2); Region (4); Sequence caution (1); Zinc finger (1) FUNCTION: Dioxygenase that catalyzes the conversion of the modified genomic base 5-methylcytosine (5mC) into 5-hydroxymethylcytosine (5hmC) and plays a key role in active DNA demethylation. Also mediates subsequent conversion of 5hmC into 5-formylcytosine (5fC), and conversion of 5fC to 5-carboxylcytosine (5caC). Conversion of 5mC into 5hmC, 5fC and 5caC probably constitutes the first step in cytosine demethylation. Methylation at the C5 position of cytosine bases is an epigenetic modification of the mammalian genome which plays an important role in transcriptional regulation. In addition to its role in DNA demethylation, plays a more general role in chromatin regulation. Preferentially binds to CpG-rich sequences at promoters of both transcriptionally active and Polycomb-repressed genes. Involved in the recruitment of the O-GlcNAc transferase OGT to CpG-rich transcription start sites of active genes, thereby promoting histone H2B GlcNAcylation by OGT. Also involved in transcription repression of a subset of genes through recruitment of transcriptional repressors to promoters. Involved in the balance between pluripotency and lineage commitment of cells it plays a role in embryonic stem cells maintenance and inner cell mass cell specification. Plays an essential role in the tumorigenicity of glioblastoma cells. TET1-mediated production of 5hmC acts as a recruitment signal for the CHTOP-methylosome complex to selective sites on the chromosome, where it methylates H4R3 and activates the transcription of genes involved in glioblastomagenesis (PubMed:25284789). {ECO:0000269|PubMed:20639862, ECO:0000269|PubMed:21451524, ECO:0000269|PubMed:21490601, ECO:0000269|PubMed:21496894, ECO:0000269|PubMed:21514197, ECO:0000269|PubMed:21778364, ECO:0000269|PubMed:23352454, ECO:0000269|PubMed:25284789}. PTM: Glycosylated. Interaction with OGT leads to GlcNAcylation. {ECO:0000269|PubMed:23352454}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20639862}. SUBUNIT: Interacts with SIN3A; recruits the transcriptional co-repressor SIN3A to gene promoters (PubMed:21490601). Interacts with HCFC1 and OGT (PubMed:23352454). Found in a complex composed of at least SINHCAF, SIN3A, HDAC1, SAP30, RBBP4, OGT and TET1 (PubMed:28554894). {ECO:0000269|PubMed:21490601, ECO:0000269|PubMed:23352454, ECO:0000269|PubMed:28554894}. TISSUE SPECIFICITY: Present in embryonic stem cells (ES cells). {ECO:0000269|PubMed:20639862}. +O54819 TFPI1_MOUSE Tissue factor pathway inhibitor (TFPI) (Extrinsic pathway inhibitor) (EPI) (Lipoprotein-associated coagulation inhibitor) (LACI) 306 34,987 Alternative sequence (2); Chain (1); Disulfide bond (9); Domain (3); Glycosylation (4); Sequence conflict (1); Signal peptide (1); Site (3) FUNCTION: Inhibits factor X (X(a)) directly and, in a Xa-dependent way, inhibits VIIa/tissue factor activity, presumably by forming a quaternary Xa/LACI/VIIa/TF complex. It possesses an antithrombotic action and also the ability to associate with lipoproteins in plasma (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. DOMAIN: This inhibitor contains three inhibitory domains. The first domain interacts with VIIa and TF, the second one with Xa (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Isoform alpha is expressed in heart and spleen; isoform beta in heart and lung. +Q99LM9 TADA1_MOUSE Transcriptional adapter 1 (Transcriptional adapter 1-like protein) 335 37,409 Chain (1) FUNCTION: Probably involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the STAGA transcription coactivator-HAT complex, at least composed of SUPT3H, GCN5L2, TAF5L, TAF6L, SUPT7L, TADA3L, TAD1L, TAF10, TAF12, TRRAP and TAF9. {ECO:0000250}. +P97357 TAF1A_MOUSE TATA box-binding protein-associated factor RNA polymerase I subunit A (RNA polymerase I-specific TBP-associated factor 48 kDa) (TAFI48) (TATA box-binding protein-associated factor 1A) (TBP-associated factor 1A) (Transcription initiation factor SL1/TIF-IB subunit A) 453 52,718 Chain (1) FUNCTION: Component of the transcription factor SL1/TIF-IB complex, which is involved in the assembly of the PIC (pre-initiation complex) during RNA polymerase I-dependent transcription. The rate of PIC formation probably is primarily dependent on the rate of association of SL1/TIF-IB with the rDNA promoter. SL1/TIF-IB is involved in stabilization of nucleolar transcription factor 1/UBTF on rDNA. Formation of SL1/TIF-IB excludes the association of TBP with TFIID subunits (By similarity). {ECO:0000250, ECO:0000269|PubMed:9050847}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the transcription factor SL1/TIF-IB complex, composed of TBP and at least TAF1A, TAF1B, TAF1C and TAF1D. In the complex interacts directly with TBP, TAF1A and TAF1B. Interaction of the SL1/TIF-IB subunits with TBP excludes interaction of TBP with the transcription factor IID (TFIID) subunits. Interacts with UBFT (By similarity). Interacts with CEBPA (isoform 1 and isoform 4) (By similarity). {ECO:0000250|UniProtKB:Q15573}. +P05214 TBA3_MOUSE Tubulin alpha-3 chain (Alpha-tubulin 3/7) (Alpha-tubulin isotype M-alpha-3/7) (Tubulin alpha-3/alpha-7 chain) [Cleaved into: Detyrosinated tubulin alpha-3 chain] 450 49,960 Chain (2); Modified residue (6); Nucleotide binding (1); Site (1) FUNCTION: Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. PTM: Some glutamate residues at the C-terminus are polyglycylated, resulting in polyglycine chains on the gamma-carboxyl group. Glycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Both modifications can coexist on the same protein on adjacent residues, and lowering polyglycylation levels increases polyglutamylation, and reciprocally. The precise function of polyglycylation is still unclear. {ECO:0000269|PubMed:19524510}.; PTM: Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (PubMed:15890843). Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity by SPAST increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold (By similarity). {ECO:0000250|UniProtKB:Q71U36, ECO:0000269|PubMed:15890843}.; PTM: Acetylation of alpha chains at Lys-40 is located inside the microtubule lumen. This modification has been correlated with increased microtubule stability, intracellular transport and ciliary assembly. {ECO:0000250|UniProtKB:Q71U36}.; PTM: Methylation of alpha chains at Lys-40 is found in mitotic microtubules and is required for normal mitosis and cytokinesis contributing to genomic stability. {ECO:0000250|UniProtKB:P68363}.; PTM: Nitration of Tyr-450 is irreversible and interferes with normal dynein intracellular distribution. {ECO:0000250|UniProtKB:Q71U36}.; PTM: Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (VASH1 or VASH2) and tubulin tyrosine ligase (TTL), respectively. {ECO:0000269|PubMed:16954346, ECO:0000269|PubMed:19564401, ECO:0000269|PubMed:26446751, ECO:0000269|PubMed:27102488, ECO:0000269|PubMed:29146868}.; PTM: Tubulin alpha-3 chain: Tyrosination promotes microtubule interaction with CAP-Gly domain-containing proteins such as CLIP1, CLIP2 and DCTN1 (PubMed:16954346, PubMed:19564401). Tyrosination regulates the initiation of dynein-dynactin motility via interaction with DCTN1, which brings the dynein-dynactin complex into contact with microtubules. In neurons, tyrosinated tubulins mediate the initiation of retrograde vesicle transport (By similarity). {ECO:0000250|UniProtKB:Q71U36, ECO:0000269|PubMed:16954346, ECO:0000269|PubMed:19564401}.; PTM: Detyrosinated tubulin alpha-3 chain: Detyrosination is involved in metaphase plate congression by guiding chromosomes during mitosis: detyrosination promotes interaction with CENPE, promoting pole-proximal transport of chromosomes toward the equator (By similarity). Detyrosination increases microtubules-dependent mechanotransduction in dystrophic cardiac and skeletal muscle (PubMed:26446751). In cardiomyocytes, detyrosinated microtubules are required to resist to contractile compression during contraction: detyrosination promotes association with desmin (DES) at force-generating sarcomeres, leading to buckled microtubules and mechanical resistance to contraction (PubMed:27102488). {ECO:0000250|UniProtKB:Q6PEY2, ECO:0000269|PubMed:26446751, ECO:0000269|PubMed:27102488}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SUBUNIT: Dimer of alpha and beta chains. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells. TISSUE SPECIFICITY: Alpha-3 and alpha-7 are identical but coded by two different genes, they are testis-specific. {ECO:0000269|PubMed:3785200}. +Q9D9I4 TBC20_MOUSE TBC1 domain family member 20 402 45,825 Chain (1); Domain (1); Natural variant (1); Sequence conflict (1); Site (2); Transmembrane (2) TRANSMEM 237 257 Helical. {ECO:0000255}.; TRANSMEM 366 386 Helical. {ECO:0000255}. FUNCTION: GTPase-activating protein specific for Rab1 and Rab2 small GTPase families for which it can accelerate the intrinsic GTP hydrolysis rate by more than five orders of magnitude. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. DOMAIN: The arginine and glutamine fingers are critical for the GTPase-activating mechanism, they pull out Rab's 'switch 2' glutamine and insert in Rab's active site. {ECO:0000250}. DISEASE: Note=Defects in Tbc1d20 are the cause of spontaneous autosomal recessive blind sterile (bs) phenotype. Bs animals exhibit embryonic non-progressive nuclear cataracts and spermatid abnormalities associated with male infertility. +P62340 TBPL1_MOUSE TATA box-binding protein-like protein 1 (TBP-like protein 1) (21 kDa TBP-like protein) (TATA box-binding protein-related factor 2) (TBP-related factor 2) (TBP-like factor) (TBP-related protein) 186 20,887 Chain (1) FUNCTION: Part of a specialized transcription system that mediates the transcription of most ribosomal proteins through the 5'-TCT-3' motif which is a core promoter element at these genes (By similarity). Seems to also mediate the transcription of NF1. Does not bind the TATA box. {ECO:0000250, ECO:0000269|PubMed:15767669, ECO:0000269|PubMed:9889269}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Binds TFIIA and TFIIB. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:16412700, ECO:0000269|PubMed:9889269}. +P03985 TCC2_MOUSE T-cell receptor gamma chain C region C7.5 172 19,797 Chain (1); Non-terminal residue (1); Region (1); Topological domain (1); Transmembrane (1) TRANSMEM 141 160 Helical. {ECO:0000255}. TOPO_DOM 161 172 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +P06334 TCC3_MOUSE T-cell receptor gamma chain C region DFL12 169 19,426 Beta strand (6); Chain (1); Helix (2); Non-terminal residue (1); Region (1); Topological domain (1); Transmembrane (1); Turn (1) TRANSMEM 137 157 Helical. {ECO:0000255}. TOPO_DOM 158 169 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +P06335 TCC4_MOUSE T-cell receptor gamma chain C region 5/10-13 190 22,065 Chain (1); Non-terminal residue (1); Region (1); Topological domain (1); Transmembrane (1) TRANSMEM 158 178 Helical. {ECO:0000255}. TOPO_DOM 179 190 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +O35437 TCF21_MOUSE Transcription factor 21 (TCF-21) (Capsulin) (Epicardin) (Podocyte-expressed 1) (Pod-1) 179 19,681 Chain (1); Domain (1) FUNCTION: Involved in epithelial-mesenchymal interactions in kidney and lung morphogenesis that include epithelial differentiation and branching morphogenesis. May be involved in the organogenesis of the spleen and heart and in cardiac and coronary artery development. May function in the development and sex differentiation of gonad via transcriptional regulation of AD4BP/SF-1. {ECO:0000269|PubMed:10944221}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}. SUBUNIT: Efficient DNA binding requires dimerization with another bHLH protein. Forms a heterodimer with TCF3 and binds the E box (5'-CANNTG-3'). TISSUE SPECIFICITY: Expressed at high levels in lung, kidney, gut, heart, ovary and podocytes (visceral glomerular epithelial cells). Also found in spleen, large intestine, uterus, bladder and testis. +Q9JLR5 TCF23_MOUSE Transcription factor 23 (TCF-23) (Basic helix-loop-helix transcription factor OUT) (Ovary, uterus and testis protein) 209 22,895 Chain (1); Domain (1) FUNCTION: Inhibits E-box-mediated binding and transactivation of bHLH factors. Inhibitory effect is similar to that of ID proteins. Inhibits the formation of TCF3 and MYOD1 homodimers and heterodimers. Lacks DNA binding activity. May be involved in the regulation or modulation of smooth muscle contraction of the uterus during pregnancy and particularly around the time of delivery. Seems to play a role in the inhibition of myogenesis. {ECO:0000269|PubMed:10652346}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:10652346}. SUBUNIT: Forms inactive heterodimeric complex with TCF3. {ECO:0000269|PubMed:10652346}. DOMAIN: Both the bHLH region and the C-terminal portion are essential for inhibitory function. TISSUE SPECIFICITY: Highly expressed in the uterus (predominantly in myometrium), ovary, and testis. Expression in the uterus is higher in the diestrus phase than in the estrus phase and reaches a maximum at 7.5 dpc. Expression declines towards the time of delivery and returns to the non-pregnant level 4 days after delivery. Low expression seen in lung, heart, intestine, and spleen. {ECO:0000269|PubMed:10652346}. +Q00417 TCF7_MOUSE Transcription factor 7 (TCF-7) (T-cell-specific transcription factor 1) (T-cell factor 1) (TCF-1) 419 45,465 Alternative sequence (1); Chain (1); Compositional bias (1); DNA binding (1); Motif (1); Region (1) FUNCTION: Transcriptional activator involved in T-cell lymphocyte differentiation. Necessary for the survival of CD4(+) CD8(+) immature thymocytes. Isoforms lacking the N-terminal CTNNB1 binding domain cannot fulfill this role. Binds to the T-lymphocyte-specific enhancer element (5'-WWCAAAG-3') found in the promoter of the CD3E gene. May also act as feedback transcriptional repressor of CTNNB1 and TCF7L2 target genes. TLE1, TLE2, TLE3 and TLE4 repress transactivation mediated by TCF7 and CTNNB1 (By similarity). {ECO:0000250, ECO:0000269|PubMed:11477404}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Binds the armadillo repeat of CTNNB1 and forms a stable complex. Binds AES, TLE1, TLE2, TLE3 and TLE4. Interacts with MLLT11. {ECO:0000250|UniProtKB:P36402}. TISSUE SPECIFICITY: T-cell specific. DISEASE: Note=Defects in Tcf7 may allow the formation of epithelial tumors. {ECO:0000269|PubMed:10489374}. +P56581 TDG_MOUSE G/T mismatch-specific thymine DNA glycosylase (EC 3.2.2.29) (C-JUN leucine zipper interactive protein JZA-3) (Thymine-DNA glycosylase) 421 46,879 Alternative sequence (1); Chain (1); Cross-link (4); Mutagenesis (1); Sequence conflict (17) FUNCTION: DNA glycosylase that plays a key role in active DNA demethylation: specifically recognizes and binds 5-formylcytosine (5fC) and 5-carboxylcytosine (5caC) in the context of CpG sites and mediates their excision through base-excision repair (BER) to install an unmethylated cytosine (PubMed:21817016). Cannot remove 5-hydroxymethylcytosine (5hmC). According to an alternative model, involved in DNA demethylation by mediating DNA glycolase activity toward 5-hydroxymethyluracil (5hmU) produced by deamination of 5hmC (PubMed:21722948). Also involved in DNA repair by acting as a thymine-DNA glycosylase that mediates correction of G/T mispairs to G/C pairs: in the DNA of higher eukaryotes, hydrolytic deamination of 5-methylcytosine to thymine leads to the formation of G/T mismatches. Its role in the repair of canonical base damage is however minor compared to its role in DNA demethylation. It is capable of hydrolyzing the carbon-nitrogen bond between the sugar-phosphate backbone of the DNA and a mispaired thymine. In addition to the G/T, it can remove thymine also from C/T and T/T mispairs in the order G/T >> C/T > T/T. It has no detectable activity on apyrimidinic sites and does not catalyze the removal of thymine from A/T pairs or from single-stranded DNA. It can also remove uracil and 5-bromouracil from mispairs with guanine. {ECO:0000269|PubMed:21278727, ECO:0000269|PubMed:21722948, ECO:0000269|PubMed:21817016}. PTM: Sumoylation on Lys-341 by either SUMO1 or SUMO2 induces dissociation of the product DNA. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Homodimer. Interacts with AICDA and GADD45A (By similarity). {ECO:0000250}. +Q6PFE7 TEFF1_MOUSE Tomoregulin-1 (TR-1) (M7365) (Transmembrane protein with EGF-like and one follistatin-like domain) 372 40,114 Alternative sequence (2); Chain (1); Compositional bias (1); Disulfide bond (9); Domain (3); Erroneous initiation (1); Glycosylation (1); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 323 343 Helical. {ECO:0000255}. TOPO_DOM 36 322 Extracellular. {ECO:0000255}.; TOPO_DOM 344 372 Cytoplasmic. {ECO:0000255}. FUNCTION: May inhibit NODAL and BMP signaling during neural patterning. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: May interact with ST14. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain, neurointermediate lobe, pars distalis, pancreas, ovary and testis. {ECO:0000269|PubMed:11025219, ECO:0000269|PubMed:11165370}. +Q8C5P7 TDRP_MOUSE Testis development-related protein 182 20,186 Alternative sequence (1); Chain (1); Modified residue (1) FUNCTION: Contributes to normal sperm motility, but not essential for male fertility. {ECO:0000269|PubMed:27069551}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27069551}. Cytoplasm {ECO:0000269|PubMed:27069551}. Note=Mainly nuclear. Also detected in cytoplasm near the midpiece of the flagellum. {ECO:0000269|PubMed:27069551}. SUBUNIT: Interacts with PRM2. {ECO:0000269|PubMed:27069551}. TISSUE SPECIFICITY: Strongly expressed in testis. Also detected at lower levels in epididymis, bone marrow and kidney. {ECO:0000269|PubMed:27069551}. +Q9R0Q7 TEBP_MOUSE Prostaglandin E synthase 3 (EC 5.3.99.3) (Cytosolic prostaglandin E2 synthase) (cPGES) (Hsp90 co-chaperone) (Progesterone receptor complex p23) (Sid 3177) (Telomerase-binding protein p23) 160 18,721 Chain (1); Compositional bias (1); Cross-link (2); Domain (1); Modified residue (8); Motif (1); Sequence conflict (3) Lipid metabolism; prostaglandin biosynthesis. FUNCTION: Cytosolic prostaglandin synthase that catalyzes the oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2). Molecular chaperone that localizes to genomic response elements in a hormone-dependent manner and disrupts receptor-mediated transcriptional activation, by promoting disassembly of transcriptional regulatory complexes. Facilitates HIF alpha proteins hydroxylation via interaction with EGLN1/PHD2, leading to recruit EGLN1/PHD2 to the HSP90 pathway. {ECO:0000250|UniProtKB:Q15185}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q3ZBF7}. SUBUNIT: Probably forms a complex composed of chaperones HSP90 and HSP70, co-chaperones STIP1/HOP, CDC37, PPP5C, PTGES3/p23, TSC1 and client protein TSC2. Binds to the progesterone receptor. Interacts with TERT; the interaction, together with HSP90AA1, is required for correct assembly and stabilization of the telomerase holoenzyme complex. Interacts (via PXLE motif) with EGLN1/PHD2, recruiting EGLN1/PHD2 to the HSP90 pathway to facilitate HIF alpha proteins hydroxylation. Interacts with HSP90AA1, FLCN, FNIP1 and FNIP2. {ECO:0000250|UniProtKB:Q15185}. TISSUE SPECIFICITY: Expressed in testis, kidney, bladder and ovary. {ECO:0000269|PubMed:14563409}. +Q8BFZ1 TECRL_MOUSE Trans-2,3-enoyl-CoA reductase-like (EC 1.3.1.-) (Steroid 5-alpha-reductase 2-like 2 protein) 361 41,893 Chain (1); Modified residue (2); Sequence conflict (1); Transmembrane (4) TRANSMEM 139 159 Helical. {ECO:0000255}.; TRANSMEM 181 201 Helical. {ECO:0000255}.; TRANSMEM 215 235 Helical. {ECO:0000255}.; TRANSMEM 309 329 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q5HYJ1}. TISSUE SPECIFICITY: Expression is highest in the heart with very low to almost undetectable levels in brain, skeletal muscle, stomach, pancreas, liver, kidney, small intestine, and uterus. {ECO:0000269|PubMed:27861123}. +Q9D9I1 TEX43_MOUSE Testis-expressed protein 43 141 16,282 Chain (1) +Q3URQ0 TEX10_MOUSE Testis-expressed protein 10 928 105,209 Chain (1); Modified residue (1); Repeat (1) FUNCTION: Functions as a component of the Five Friends of Methylated CHTOP (5FMC) complex; the 5FMC complex is recruited to ZNF148 by methylated CHTOP, leading to desumoylation of ZNF148 and subsequent transactivation of ZNF148 target genes (PubMed:22872859). Component of the PELP1 complex involved in the nucleolar steps of 28S rRNA maturation and the subsequent nucleoplasmic transit of the pre-60S ribosomal subunit (By similarity). {ECO:0000250|UniProtKB:Q9NXF1, ECO:0000269|PubMed:22872859}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9NXF1}. Nucleus, nucleoplasm {ECO:0000269|PubMed:22872859}. Cytoplasm {ECO:0000269|PubMed:22872859}. Note=Mainly found in the nucleoplasm, with low levels detected in the cytoplasmic and chromatin fractions. {ECO:0000269|PubMed:22872859}. SUBUNIT: Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, KAT8/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10 (By similarity). Component of the 5FMC complex, at least composed of PELP1, LAS1L, TEX10, WDR18 and SENP3; the complex interacts with methylated CHTOP and ZNF148 (PubMed:22872859). Component of the PELP1 complex, composed of at least PELP1, TEX10 and WDR18. The complex interacts with pre-60S ribosome particles (By similarity). {ECO:0000250|UniProtKB:Q9NXF1, ECO:0000269|PubMed:22872859}. +Q3TTI8 TEX52_MOUSE Testis-expressed protein 52 308 35,370 Alternative sequence (2); Chain (1); Sequence conflict (1) TISSUE SPECIFICITY: Expressed in Testis. {ECO:0000305}. +Q64163 TFDP2_MOUSE Transcription factor Dp-2 (Dp-3) (E2F dimerization partner 2) 446 49,098 Alternative sequence (3); Chain (1); Compositional bias (1); DNA binding (1); Initiator methionine (1); Modified residue (4); Motif (2); Region (4) FUNCTION: Can stimulate E2F-dependent transcription. Binds DNA cooperatively with E2F family members through the E2 recognition site, 5'-TTTC[CG]CGC-3', found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. The TFDP2:E2F complex functions in the control of cell-cycle progression from G1 to S phase. The E2F1:DP complex appears to mediate both cell proliferation and apoptosis. Blocks adipocyte differentiation by repressing CEBPA binding to its target gene promoters. {ECO:0000250|UniProtKB:Q14188}. PTM: Phosphorylation by E2F1-bound cyclin A-CDK2, in the S phase, inhibits E2F-mediated DNA binding and transactivation. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Component of the DRTF1/E2F transcription factor complex. Forms heterodimers with E2F family members. The complex can interact with hypophosphorylated retinoblastoma protein RB1 and related proteins (RBL1 and RBL2) that inhibit the E2F transactivation domain. During the cell cycle, RB becomes phosphorylated in mid-to-late G1 phase, detaches from the DRTF1/E2F complex rendering E2F transcriptionally active. Interacts with GMCL (By similarity). Component of the DREAM complex (also named LINC complex) at least composed of E2F4, E2F5, LIN9, LIN37, LIN52, LIN54, MYBL1, MYBL2, RBL1, RBL2, RBBP4, TFDP1 and TFDP2. The complex exists in quiescent cells where it represses cell cycle-dependent genes. It dissociates in S phase when LIN9, LIN37, LIN52 and LIN54 form a subcomplex that binds to MYBL2. The complex TFDP2:E2F1 interacts with CEBPA; the interaction prevents CEBPA binding to target gene promoters and represses its transcriptional activity (By similarity). {ECO:0000250|UniProtKB:Q14188, ECO:0000269|PubMed:9878064}. TISSUE SPECIFICITY: Expressed in all tissues examined. Highest levels in spleen and heart. +Q9CY16 RT28_MOUSE 28S ribosomal protein S28, mitochondrial (MRP-S28) (S28mt) 186 20,520 Chain (1); Modified residue (2); Sequence conflict (1); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P82928}. SUBUNIT: Component of the mitochondrial ribosome small subunit (28S) which comprises a 12S rRNA and about 30 distinct proteins. {ECO:0000250|UniProtKB:P82928}. +Q3TYX8 RUFY4_MOUSE RUN and FYVE domain-containing protein 4 563 64,036 Alternative sequence (1); Chain (1); Domain (1); Sequence conflict (5); Zinc finger (1) FUNCTION: Positively regulates macroautophagy in primary dendritic cells. Increases autophagic flux, probably by stimulating both autophagosome formation and facilitating tethering with lysosomes. Binds to phosphatidylinositol 3-phosphate (PtdIns3P) through its FYVE-type zinc finger. {ECO:0000250|UniProtKB:Q6ZNE9}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:Q6ZNE9}. SUBUNIT: Interacts (via RUN domain) with RAB7A. {ECO:0000250|UniProtKB:Q6ZNE9}. DOMAIN: The RUN domain and the FYVE-type zinc finger are essential for its function in the positive regulation of macroautophagy. {ECO:0000250|UniProtKB:Q6ZNE9}. +Q9ER88 RT29_MOUSE 28S ribosomal protein S29, mitochondrial (MRP-S29) (S29mt) (Death-associated protein 3) (DAP-3) 391 44,699 Alternative sequence (1); Chain (1); Erroneous initiation (4); Modified residue (2); Sequence conflict (3); Transit peptide (1) FUNCTION: Involved in mediating interferon-gamma-induced cell death. {ECO:0000250|UniProtKB:P51398}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P51398}. SUBUNIT: Component of the mitochondrial ribosome small subunit (28S) which comprises a 12S rRNA and about 30 distinct proteins. Interacts with DELE1. Interacts with NOA1. {ECO:0000250|UniProtKB:P51398}. +Q8R4Y8 RTTN_MOUSE Rotatin 2226 248,489 Alternative sequence (8); Chain (1); Erroneous initiation (1); Modified residue (2); Sequence conflict (2) FUNCTION: Involved in the genetic cascade that governs left-right specification. Required for correct asymmetric expression of NODAL, LEFTY and PITX2 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250}. Note=Colocalizes with the basal bodies at the primary cilium. {ECO:0000250}. +Q64131 RUNX3_MOUSE Runt-related transcription factor 3 (Acute myeloid leukemia 2 protein) (Core-binding factor subunit alpha-3) (CBF-alpha-3) (Oncogene AML-2) (Polyomavirus enhancer-binding protein 2 alpha C subunit) (PEA2-alpha C) (PEBP2-alpha C) (SL3-3 enhancer factor 1 alpha C subunit) (SL3/AKV core-binding factor alpha C subunit) 409 43,518 Alternative sequence (1); Chain (1); Compositional bias (1); Cross-link (1); Domain (1); Modified residue (1); Mutagenesis (1); Sequence conflict (2) FUNCTION: Forms the heterodimeric complex core-binding factor (CBF) with CBFB. RUNX members modulate the transcription of their target genes through recognizing the core consensus binding sequence 5'-TGTGGT-3', or very rarely, 5'-TGCGGT-3', within their regulatory regions via their runt domain, while CBFB is a non-DNA-binding regulatory subunit that allosterically enhances the sequence-specific DNA-binding capacity of RUNX. The heterodimers bind to the core site of a number of enhancers and promoters, including murine leukemia virus, polyomavirus enhancer, T-cell receptor enhancers, LCK, IL3 and GM-CSF promoters (Probable). May be involved in the control of cellular proliferation and/or differentiation. In association with ZFHX3, upregulates CDKN1A promoter activity following TGF-beta stimulation (By similarity). CBF complexes repress ZBTB7B transcription factor during cytotoxic (CD8+) T cell development. They bind to RUNX-binding sequence within the ZBTB7B locus acting as transcriptional silencer and allowing for cytotoxic T cell differentiation (PubMed:18258917). CBF complexes binding to the transcriptional silencer is essential for recruitment of nuclear protein complexes that catalyze epigenetic modifications to establish epigenetic ZBTB7B silencing (PubMed:23481257). {ECO:0000250|UniProtKB:Q13761, ECO:0000269|PubMed:18258917, ECO:0000269|PubMed:23481257, ECO:0000305}. PTM: Phosphorylated on tyrosine residues by SRC. Phosphorylated by LCK and FYN (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13761}. Cytoplasm {ECO:0000250|UniProtKB:Q13761}. Note=The tyrosine phosphorylated form localizes to the cytoplasm. Translocates from the cytoplasm to the nucleus following TGF-beta stimulation. {ECO:0000250|UniProtKB:Q13761}. SUBUNIT: Heterodimer with CBFB. RUNX3 binds DNA as a monomer and through the Runt domain. DNA-binding is increased by heterodimerization (Probable). Interacts with TLE1 and SUV39H1. The tyrosine phosphorylated form (via runt domain) interacts with SRC (via protein kinase domain). Interacts with FYN and LCK. Interacts with FOXP3. Interacts with ZFHX3. Interacts with TBX21 (PubMed:21151104). {ECO:0000250|UniProtKB:Q13761, ECO:0000269|PubMed:21151104, ECO:0000305|PubMed:18258917}. DOMAIN: A proline/serine/threonine rich region at the C-terminus is necessary for transcriptional activation of target genes. +Q91W34 RUS1_MOUSE RUS1 family protein C16orf58 homolog 466 50,469 Alternative sequence (2); Chain (1); Initiator methionine (1); Modified residue (1); Sequence conflict (8); Transmembrane (1) TRANSMEM 245 265 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q8CCI5 RYBP_MOUSE RING1 and YY1-binding protein (Death effector domain-associated factor) (DED-associated factor) 228 24,777 Chain (1); Compositional bias (3); Cross-link (1); Erroneous initiation (1); Modified residue (5); Mutagenesis (1); Region (1); Sequence conflict (1); Zinc finger (1) FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1-like complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility (PubMed:22325148, PubMed:28596365). Component of a PRC1-like complex that mediates monoubiquitination of histone H2A 'Lys-119' on the X chromosome and is required for normal silencing of one copy of the X chromosome in XX females (PubMed:28596365). May stimulate ubiquitination of histone H2A 'Lys-119' by recruiting the complex to target sites (PubMed:22325148, PubMed:28596365). Inhibits ubiquitination and subsequent degradation of TP53, and thereby plays a role in regulating transcription of TP53 target genes (By similarity). May also regulate the ubiquitin-mediated proteasomal degradation of other proteins like FANK1 to regulate apoptosis (PubMed:17874297). May be implicated in the regulation of the transcription as a repressor of the transcriptional activity of E4TF1 (By similarity). May bind to DNA (PubMed:19170609). May play a role in the repression of tumor growth and metastasis in breast cancer by down-regulating SRRM3 (PubMed:27748911). {ECO:0000250|UniProtKB:Q8N488, ECO:0000269|PubMed:17874297, ECO:0000269|PubMed:19170609, ECO:0000269|PubMed:22325148, ECO:0000269|PubMed:27748911, ECO:0000269|PubMed:28596365}. PTM: Monoubiquitinated. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17070805}. Cytoplasm {ECO:0000250|UniProtKB:Q8N488}. Nucleus, nucleoplasm {ECO:0000269|PubMed:17070805}. Note=Primarily found in the nucleus. Detected in a punctate pattern likely to represent Polycomb group (PcG) bodies. {ECO:0000269|PubMed:17070805}. SUBUNIT: Monomer. Component of repressive BCOR complex containing Polycomb group subcomplex at least composed of BCOR, PCGF1, RING1 and RNF2/RING2 (By similarity). Component of PCR1-like complexes (PubMed:22325148, PubMed:28596365). Interacts with PCGF1. Part of a PCR1-like complex that contains AUTS2, PCGF5, RNF2, CSNK2B AND RYBP. Interacts with RNF2; the interaction is direct (By similarity). Interacts with CBX2, YAF2, RING1 and RNF2 (PubMed:10369680, PubMed:19170609, PubMed:22226355). Interacts with ubiquitin and ubiquitinated proteins (PubMed:17070805). Interacts with ubiquitinated histone H2A (PubMed:17070805). Interacts with apoptin, DEDD, FADD, CASP8, CASP10, YY1 and GABPB1. Together with GABPB1 and YY1, it forms a ternary complex, probably being the bridge factor between these two transcription factors. Interacts with MDM2, and thereby inhibits ubiquitination of TP53. Identified in a ternary complex containing MDM2, TP53 and RYBP. Interacts with FANK1; may prevent the ubiquitin-mediated proteasomal degradation of FANK1 (By similarity). Interacts with IFT57 (PubMed:17874297). {ECO:0000250|UniProtKB:Q8N488, ECO:0000269|PubMed:10369680, ECO:0000269|PubMed:17070805, ECO:0000269|PubMed:17874297, ECO:0000269|PubMed:19170609, ECO:0000269|PubMed:22226355, ECO:0000269|PubMed:22325148, ECO:0000269|PubMed:28596365}. DOMAIN: Intrinsically unstructured in the absence of binding partners. Folds upon binding to DNA or RNF2. {ECO:0000269|PubMed:19170609}. TISSUE SPECIFICITY: Expressed in embryonic stem cells. {ECO:0000269|PubMed:22226355}. +Q8CAK3 RYDEN_MOUSE Repressor of yield of DENV protein homolog (RyDEN) 290 33,015 Alternative sequence (1); Chain (1); Compositional bias (1); Motif (2); Region (1) FUNCTION: May exhibit antiviral activity. {ECO:0000250|UniProtKB:Q9NUL5}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NUL5}. Nucleus {ECO:0000250|UniProtKB:Q9NUL5}. Note=Predominantly found in the cytoplasm. {ECO:0000250|UniProtKB:Q9NUL5}. SUBUNIT: Interacts with PABPC1. Found in a complex with PABPC1 and LARP1. {ECO:0000250|UniProtKB:Q9NUL5}. +Q9ES88 S13A2_MOUSE Solute carrier family 13 member 2 (Na(+)/dicarboxylate cotransporter 1) (NaDC-1) (Renal sodium/dicarboxylate cotransporter) 586 64,111 Chain (1); Transmembrane (12) TRANSMEM 13 33 Helical. {ECO:0000255}.; TRANSMEM 53 73 Helical. {ECO:0000255}.; TRANSMEM 86 106 Helical. {ECO:0000255}.; TRANSMEM 215 235 Helical. {ECO:0000255}.; TRANSMEM 264 284 Helical. {ECO:0000255}.; TRANSMEM 319 339 Helical. {ECO:0000255}.; TRANSMEM 366 386 Helical. {ECO:0000255}.; TRANSMEM 407 427 Helical. {ECO:0000255}.; TRANSMEM 445 465 Helical. {ECO:0000255}.; TRANSMEM 478 498 Helical. {ECO:0000255}.; TRANSMEM 506 526 Helical. {ECO:0000255}.; TRANSMEM 535 555 Helical. {ECO:0000255}. FUNCTION: Cotransport of sodium ions and dicarboxylates such as succinate and citrate. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Highly expressed in kidney and small intestine. Not detectable in brain, heart, stomach and skeletal muscle. +Q9WTN6 S22AL_MOUSE Solute carrier family 22 member 21 (Organic cation/carnitine transporter 3) (Solute carrier family 22 member 9) 564 63,321 Chain (1); Glycosylation (3); Nucleotide binding (1); Topological domain (13); Transmembrane (12) TRANSMEM 21 41 Helical; Name=1. {ECO:0000255}.; TRANSMEM 143 163 Helical; Name=2. {ECO:0000255}.; TRANSMEM 173 193 Helical; Name=3. {ECO:0000255}.; TRANSMEM 198 218 Helical; Name=4. {ECO:0000255}.; TRANSMEM 233 253 Helical; Name=5. {ECO:0000255}.; TRANSMEM 258 278 Helical; Name=6. {ECO:0000255}.; TRANSMEM 345 365 Helical; Name=7. {ECO:0000255}.; TRANSMEM 377 397 Helical; Name=8. {ECO:0000255}.; TRANSMEM 410 430 Helical; Name=9. {ECO:0000255}.; TRANSMEM 434 454 Helical; Name=10. {ECO:0000255}.; TRANSMEM 466 486 Helical; Name=11. {ECO:0000255}.; TRANSMEM 492 512 Helical; Name=12. {ECO:0000255}. TOPO_DOM 1 20 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 42 142 Extracellular. {ECO:0000255}.; TOPO_DOM 164 172 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 194 197 Extracellular. {ECO:0000255}.; TOPO_DOM 219 232 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 254 257 Extracellular. {ECO:0000255}.; TOPO_DOM 279 344 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 366 376 Extracellular. {ECO:0000255}.; TOPO_DOM 398 409 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 431 433 Extracellular. {ECO:0000255}.; TOPO_DOM 455 465 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 487 491 Extracellular. {ECO:0000255}.; TOPO_DOM 513 564 Cytoplasmic. {ECO:0000255}. FUNCTION: Sodium-ion independent, medium affinity carnitine transporter. Also transports organic cations such as tetraethylammonium (TEA) without the involvement of sodium. Relative uptake activity ratio of carnitine to TEA is 746. {ECO:0000269|PubMed:11010964}. SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000269|PubMed:11010964, ECO:0000269|PubMed:12535646, ECO:0000269|PubMed:16288981}; Multi-pass membrane protein {ECO:0000269|PubMed:11010964, ECO:0000269|PubMed:12535646, ECO:0000269|PubMed:16288981}. TISSUE SPECIFICITY: Predominantly expressed in testis. {ECO:0000269|PubMed:11010964}. +Q6IS41 S2547_MOUSE Solute carrier family 25 member 47 (Hepatocellular carcinoma down-regulated mitochondrial carrier homolog) 310 33,646 Chain (1); Erroneous initiation (1); Repeat (3); Sequence conflict (1); Transmembrane (6) TRANSMEM 3 23 Helical; Name=1. {ECO:0000255}.; TRANSMEM 55 75 Helical; Name=2. {ECO:0000255}.; TRANSMEM 98 114 Helical; Name=3. {ECO:0000255}.; TRANSMEM 194 210 Helical; Name=4. {ECO:0000255}.; TRANSMEM 219 239 Helical; Name=5. {ECO:0000255}.; TRANSMEM 280 298 Helical; Name=6. {ECO:0000255}. FUNCTION: Uncoupling protein which may catalyze the physiological 'proton leak' in liver. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q8CD26 S35E1_MOUSE Solute carrier family 35 member E1 409 44,325 Chain (1); Erroneous initiation (1); Modified residue (1); Transmembrane (9) TRANSMEM 50 70 Helical. {ECO:0000255}.; TRANSMEM 111 131 Helical. {ECO:0000255}.; TRANSMEM 133 153 Helical. {ECO:0000255}.; TRANSMEM 165 184 Helical. {ECO:0000255}.; TRANSMEM 188 207 Helical. {ECO:0000255}.; TRANSMEM 222 242 Helical. {ECO:0000255}.; TRANSMEM 252 274 Helical. {ECO:0000255}.; TRANSMEM 282 303 Helical. {ECO:0000255}.; TRANSMEM 312 332 Helical. {ECO:0000255}. FUNCTION: Putative transporter. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9R0M8 S35A2_MOUSE UDP-galactose translocator (Solute carrier family 35 member A2) (UDP-galactose transporter) (UDP-Gal-Tr) (UGT) (mUGT1) 390 40,766 Chain (1); Transmembrane (10) TRANSMEM 3 23 Helical. {ECO:0000255}.; TRANSMEM 37 57 Helical. {ECO:0000255}.; TRANSMEM 65 85 Helical. {ECO:0000255}.; TRANSMEM 97 117 Helical. {ECO:0000255}.; TRANSMEM 140 160 Helical. {ECO:0000255}.; TRANSMEM 169 189 Helical. {ECO:0000255}.; TRANSMEM 200 220 Helical. {ECO:0000255}.; TRANSMEM 238 258 Helical. {ECO:0000255}.; TRANSMEM 269 289 Helical. {ECO:0000255}.; TRANSMEM 315 335 Helical. {ECO:0000255}. FUNCTION: Transports nucleotide sugars from the cytosol into Golgi vesicles where glycosyltransferases function. SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane protein. SUBUNIT: Interacts with SLC35A3. {ECO:0000250}. +Q8R1S9 S38A4_MOUSE Sodium-coupled neutral amino acid transporter 4 (Amino acid transporter A3) (Na(+)-coupled neutral amino acid transporter 4) (Solute carrier family 38 member 4) (System A amino acid transporter 3) 547 60,464 Chain (1); Disulfide bond (1); Erroneous initiation (1); Glycosylation (3); Modified residue (1); Mutagenesis (5); Sequence conflict (5); Topological domain (11); Transmembrane (10) TRANSMEM 105 125 Helical. {ECO:0000255}.; TRANSMEM 152 172 Helical. {ECO:0000255}.; TRANSMEM 196 216 Helical. {ECO:0000255}.; TRANSMEM 221 241 Helical. {ECO:0000255}.; TRANSMEM 333 353 Helical. {ECO:0000255}.; TRANSMEM 370 390 Helical. {ECO:0000255}.; TRANSMEM 412 432 Helical. {ECO:0000255}.; TRANSMEM 454 474 Helical. {ECO:0000255}.; TRANSMEM 477 497 Helical. {ECO:0000255}.; TRANSMEM 515 535 Helical. {ECO:0000255}. TOPO_DOM 1 104 Extracellular. {ECO:0000255}.; TOPO_DOM 126 151 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 173 195 Extracellular. {ECO:0000255}.; TOPO_DOM 217 220 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 242 332 Extracellular. {ECO:0000255}.; TOPO_DOM 354 369 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 391 411 Extracellular. {ECO:0000255}.; TOPO_DOM 433 453 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 475 476 Extracellular. {ECO:0000255}.; TOPO_DOM 498 514 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 536 547 Extracellular. {ECO:0000255}. FUNCTION: Sodium-dependent amino acid transporter. Mediates electrogenic symport of neutral amino acids and sodium ions. Has a broad specificity, with a preference for Ala, followed by Ser, His, Gly, Cys, Asn, Thr, Pro, Gln and Met. May mediate sodium-independent transport of cationic amino acids, such as Arg and Lys. Amino acid uptake is pH-dependent, with lower transport activities at pH 6.5, intermediate at pH 7.0 and highest between pH 7.5 and 8.5. {ECO:0000269|PubMed:12537539}. PTM: The disulfide bond plays an important role in substrate transport, but has no effect on trafficking to the cell surface. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12537539}; Multi-pass membrane protein {ECO:0000269|PubMed:12537539}. TISSUE SPECIFICITY: Detected in liver, in hepatocytes surrounding the central vein. Not detected in heart, kidney, brain, lung, small intestine, spleen and thymus. {ECO:0000269|PubMed:12537539}. +O35488 S27A2_MOUSE Very long-chain acyl-CoA synthetase (VLACS) (VLCS) (EC 6.2.1.-) (Fatty acid transport protein 2) (FATP-2) (Fatty-acid-coenzyme A ligase, very long-chain 1) (Long-chain-fatty-acid--CoA ligase) (EC 6.2.1.3) (Solute carrier family 27 member 2) (THCA-CoA ligase) (Very long-chain-fatty-acid-CoA ligase) 620 70,423 Chain (1); Frameshift (1); Modified residue (2); Nucleotide binding (1); Sequence conflict (8); Topological domain (4); Transmembrane (3) TRANSMEM 5 27 Helical. {ECO:0000255}.; TRANSMEM 107 127 Helical. {ECO:0000255}.; TRANSMEM 268 288 Helical. {ECO:0000255}. TOPO_DOM 1 4 Lumenal. {ECO:0000250}.; TOPO_DOM 28 106 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 128 267 Lumenal. {ECO:0000255}.; TOPO_DOM 289 620 Cytoplasmic. {ECO:0000250}. FUNCTION: Acyl-CoA synthetase probably involved in bile acid metabolism. Proposed to activate C27 precursors of bile acids to their CoA thioesters derivatives before side chain cleavage via peroxisomal beta-oxidation occurs. In vitro, activates 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanate (THCA), the C27 precursor of cholic acid deriving from the de novo synthesis from cholesterol. Does not utilize C24 bile acids as substrates. In vitro, also activates long- and branched-chain fatty acids and may have additional roles in fatty acid metabolism (By similarity). May be involved in translocation of long-chain fatty acids (LFCA) across membranes. {ECO:0000250, ECO:0000269|PubMed:15699031}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Peroxisome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Peripheral membrane associated with the lumenal side of peroxisomes. {ECO:0000250}. TISSUE SPECIFICITY: Strong expression in liver and kidney, low expression in brain and testis, no expression in skeletal muscle and spleen. Shows uniform distribution in liver acinus. {ECO:0000269|PubMed:11980911}. +Q78IQ7 S39A4_MOUSE Zinc transporter ZIP4 (Activated in W/Wv mouse stomach 2) (mAWMS2) (Solute carrier family 39 member 4) (Zrt- and Irt-like protein 4) (ZIP-4) 660 71,063 Alternative sequence (2); Chain (1); Compositional bias (1); Glycosylation (4); Sequence conflict (1); Signal peptide (1); Topological domain (7); Transmembrane (6) TRANSMEM 338 358 Helical; Name=1. {ECO:0000255}.; TRANSMEM 377 397 Helical; Name=2. {ECO:0000255}.; TRANSMEM 421 441 Helical; Name=3. {ECO:0000255}.; TRANSMEM 572 592 Helical; Name=4. {ECO:0000255}.; TRANSMEM 600 620 Helical; Name=5. {ECO:0000255}.; TRANSMEM 631 651 Helical; Name=6. {ECO:0000255}. TOPO_DOM 23 337 Extracellular. {ECO:0000255}.; TOPO_DOM 359 376 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 398 420 Extracellular. {ECO:0000255}.; TOPO_DOM 442 571 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 593 599 Extracellular. {ECO:0000255}.; TOPO_DOM 621 630 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 652 660 Extracellular. {ECO:0000255}. FUNCTION: Plays an important role in cellular zinc homeostasis as a zinc transporter. Regulated in response to zinc availability. {ECO:0000269|PubMed:12801924}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14612438}; Multi-pass membrane protein {ECO:0000269|PubMed:14612438}. Recycling endosome membrane {ECO:0000269|PubMed:14612438}; Multi-pass membrane protein {ECO:0000269|PubMed:14612438}. Note=Colocalized with TFRC in the recycling endosomes. Cycles between endosomal compartments and the plasma membrane in response to zinc availability. TISSUE SPECIFICITY: Highly expressed in the small intestine and embryonic visceral yolk sac. Weakly expressed in the stomach and liver. Found to the apical surface of enterocytes and visceral endoderm cells during zinc deficiency. {ECO:0000269|PubMed:12801924}. +Q9Z0L1 S1PR4_MOUSE Sphingosine 1-phosphate receptor 4 (S1P receptor 4) (S1P4) (Endothelial differentiation G-protein coupled receptor 6) (Lysophospholipid receptor C1) (Sphingosine 1-phosphate receptor Edg-6) (S1P receptor Edg-6) 386 42,263 Chain (1); Glycosylation (2); Lipidation (1); Sequence conflict (1); Topological domain (8); Transmembrane (7) TRANSMEM 57 77 Helical; Name=1. {ECO:0000250}.; TRANSMEM 88 108 Helical; Name=2. {ECO:0000250}.; TRANSMEM 121 141 Helical; Name=3. {ECO:0000250}.; TRANSMEM 164 184 Helical; Name=4. {ECO:0000250}.; TRANSMEM 209 229 Helical; Name=5. {ECO:0000250}.; TRANSMEM 255 275 Helical; Name=6. {ECO:0000250}.; TRANSMEM 291 311 Helical; Name=7. {ECO:0000250}. TOPO_DOM 1 56 Extracellular. {ECO:0000250}.; TOPO_DOM 78 87 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 109 120 Extracellular. {ECO:0000250}.; TOPO_DOM 142 163 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 185 208 Extracellular. {ECO:0000250}.; TOPO_DOM 230 254 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 276 290 Extracellular. {ECO:0000250}.; TOPO_DOM 312 386 Cytoplasmic. {ECO:0000250}. FUNCTION: Receptor for the lysosphingolipid sphingosine 1-phosphate (S1P). S1P is a bioactive lysophospholipid that elicits diverse physiological effect on most types of cells and tissues. May be involved in cell migration processes that are specific for lymphocytes (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Specifically expressed in fetal and adult lymphoid and hematopoietic tissue. Expressed in lung, spleen, thymus and lymph node but absent in other non-lymphatic tissue. Coexpressed with GNA15 at the same relative levels in all tissues examined, with the highest levels in adult spleen and lung. {ECO:0000269|PubMed:12401211}. +Q4LDG0 S27A5_MOUSE Bile acyl-CoA synthetase (BACS) (EC 6.2.1.7) (Bile acid-CoA ligase) (BA-CoA ligase) (BAL) (Cholate--CoA ligase) (Fatty acid transport protein 5) (FATP-5) (Solute carrier family 27 member 5) (Very long-chain acyl-CoA synthetase-related protein) (VLACS-related) (VLACSR) 689 76,203 Chain (1); Nucleotide binding (1); Sequence conflict (4); Topological domain (2); Transmembrane (2) TRANSMEM 30 50 Helical. {ECO:0000255}.; TRANSMEM 55 75 Helical. {ECO:0000255}. TOPO_DOM 1 29 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 76 689 Cytoplasmic. {ECO:0000250}. FUNCTION: Acyl-CoA synthetase involved in bile acid metabolism. Proposed to catalyze the first step in the conjugation of C24 bile acids (choloneates) to glycine and taurine before excretion into bile canaliculi by activating them to their CoA thioesters. Seems to activate secondary bile acids entering the liver from the enterohepatic circulation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: In liver expressed in a periportal distribution. {ECO:0000269|PubMed:11980911}. +Q5F297 S35G3_MOUSE Solute carrier family 35 member G3 (Acyl-malonyl-condensing enzyme 1) 340 35,573 Chain (1); Domain (2); Erroneous gene model prediction (2); Frameshift (2); Transmembrane (9) TRANSMEM 39 59 Helical. {ECO:0000255}.; TRANSMEM 69 89 Helical. {ECO:0000255}.; TRANSMEM 107 127 Helical. {ECO:0000255}.; TRANSMEM 160 180 Helical. {ECO:0000255}.; TRANSMEM 189 209 Helical. {ECO:0000255}.; TRANSMEM 223 243 Helical. {ECO:0000255}.; TRANSMEM 257 277 Helical. {ECO:0000255}.; TRANSMEM 283 303 Helical. {ECO:0000255}.; TRANSMEM 307 327 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q61609 S20A1_MOUSE Sodium-dependent phosphate transporter 1 (Gibbon ape leukemia virus receptor 1) (GLVR-1) (Leukemia virus receptor 1 homolog) (Phosphate transporter 1) (PiT-1) (Solute carrier family 20 member 1) 681 74,153 Chain (1); Modified residue (2); Mutagenesis (3); Region (1); Sequence caution (1); Sequence conflict (8); Transmembrane (10) TRANSMEM 25 45 Helical. {ECO:0000255}.; TRANSMEM 66 86 Helical. {ECO:0000255}.; TRANSMEM 106 126 Helical. {ECO:0000255}.; TRANSMEM 162 182 Helical. {ECO:0000255}.; TRANSMEM 201 221 Helical. {ECO:0000255}.; TRANSMEM 234 254 Helical. {ECO:0000255}.; TRANSMEM 514 534 Helical. {ECO:0000255}.; TRANSMEM 561 581 Helical. {ECO:0000255}.; TRANSMEM 602 622 Helical. {ECO:0000255}.; TRANSMEM 652 672 Helical. {ECO:0000255}. FUNCTION: Sodium-phosphate symporter which plays a fundamental housekeeping role in phosphate transport, such as absorbing phosphate from interstitial fluid for normal cellular functions such as cellular metabolism, signal transduction, and nucleic acid and lipid synthesis. May play a role in extracellular matrix and cartilage calcification as well as in vascular calcification. {ECO:0000269|PubMed:1531369, ECO:0000269|PubMed:9755124, ECO:0000269|PubMed:9916777}.; FUNCTION: (Microbial infection) May function as a retroviral receptor but do not confer infection susceptibility to Gibbon Ape Leukemia Virus (GaLV), Simian sarcoma-associated virus (SSAV) and Feline leukemia virus subgroup B (FeLV-B). {ECO:0000269|PubMed:12097582, ECO:0000269|PubMed:1309898}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. DOMAIN: Region A does not confer susceptibility to infection by Gibbon Ape Leukemia Virus (GaLV) and Feline leukemia virus subgroup B (FeLV-B). Substitution of Human SLC20A1 region A by region A of murine SLC20A1 prevents viral infection. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:9916777}. +Q91W10 S39A8_MOUSE Zinc transporter ZIP8 (Solute carrier family 39 member 8) (Zrt- and Irt-like protein 8) (ZIP-8) 462 50,082 Alternative sequence (2); Chain (1); Compositional bias (1); Motif (1); Sequence conflict (8); Topological domain (9); Transmembrane (8) TRANSMEM 7 23 Helical. {ECO:0000255}.; TRANSMEM 133 153 Helical. {ECO:0000255}.; TRANSMEM 161 181 Helical. {ECO:0000255}.; TRANSMEM 192 212 Helical. {ECO:0000255}.; TRANSMEM 305 325 Helical. {ECO:0000255}.; TRANSMEM 368 388 Helical. {ECO:0000255}.; TRANSMEM 391 411 Helical. {ECO:0000255}.; TRANSMEM 432 452 Helical. {ECO:0000255}. TOPO_DOM 1 6 Extracellular. {ECO:0000255}.; TOPO_DOM 24 132 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 154 160 Extracellular. {ECO:0000255}.; TOPO_DOM 182 191 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 213 304 Extracellular. {ECO:0000255}.; TOPO_DOM 326 367 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 389 390 Extracellular. {ECO:0000255}.; TOPO_DOM 412 431 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 453 462 Extracellular. {ECO:0000255}. FUNCTION: Acts as a manganese and zinc influx transporter. Plays a role in manganese reabsorption in the proximal tubule of the kidney and in manganese uptake into the brain. {ECO:0000250|UniProtKB:Q9C0K1}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8BFU1 S39A9_MOUSE Zinc transporter ZIP9 (Solute carrier family 39 member 9) (Zrt- and Irt-like protein 9) (ZIP-9) 308 32,368 Chain (1); Glycosylation (2); Transmembrane (8) TRANSMEM 4 24 Helical. {ECO:0000255}.; TRANSMEM 35 55 Helical. {ECO:0000255}.; TRANSMEM 107 127 Helical. {ECO:0000255}.; TRANSMEM 147 167 Helical. {ECO:0000255}.; TRANSMEM 177 197 Helical. {ECO:0000255}.; TRANSMEM 211 231 Helical. {ECO:0000255}.; TRANSMEM 245 265 Helical. {ECO:0000255}.; TRANSMEM 287 307 Helical. {ECO:0000255}. FUNCTION: May act as a zinc-influx transporter. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q811P0 S36A3_MOUSE Proton-coupled amino acid transporter 3 (Proton/amino acid transporter 3) (Solute carrier family 36 member 3) (Tramdorin-2) 477 53,068 Chain (1); Compositional bias (1); Sequence conflict (1); Topological domain (12); Transmembrane (11) TRANSMEM 55 75 Helical. {ECO:0000255}.; TRANSMEM 78 98 Helical. {ECO:0000255}.; TRANSMEM 145 165 Helical. {ECO:0000255}.; TRANSMEM 203 223 Helical. {ECO:0000255}.; TRANSMEM 226 246 Helical. {ECO:0000255}.; TRANSMEM 260 280 Helical. {ECO:0000255}.; TRANSMEM 292 312 Helical. {ECO:0000255}.; TRANSMEM 345 365 Helical. {ECO:0000255}.; TRANSMEM 375 395 Helical. {ECO:0000255}.; TRANSMEM 400 420 Helical. {ECO:0000255}.; TRANSMEM 433 453 Helical. {ECO:0000255}. TOPO_DOM 1 54 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 76 77 Extracellular. {ECO:0000255}.; TOPO_DOM 99 144 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 166 202 Extracellular. {ECO:0000255}.; TOPO_DOM 224 225 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 247 259 Extracellular. {ECO:0000255}.; TOPO_DOM 281 291 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 313 344 Extracellular. {ECO:0000255}.; TOPO_DOM 366 374 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 396 399 Extracellular. {ECO:0000255}.; TOPO_DOM 421 432 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 454 477 Extracellular. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Specifically expressed in testis. {ECO:0000269|PubMed:12809675, ECO:0000269|PubMed:15058382}. +Q6P5F6 S39AA_MOUSE Zinc transporter ZIP10 (Solute carrier family 39 member 10) (Zrt- and Irt-like protein 10) (ZIP-10) 833 94,394 Chain (1); Compositional bias (4); Erroneous initiation (2); Glycosylation (4); Modified residue (3); Sequence conflict (3); Signal peptide (1); Transmembrane (7) TRANSMEM 413 433 Helical. {ECO:0000255}.; TRANSMEM 440 460 Helical. {ECO:0000255}.; TRANSMEM 497 517 Helical. {ECO:0000255}.; TRANSMEM 689 709 Helical. {ECO:0000255}.; TRANSMEM 734 754 Helical. {ECO:0000255}.; TRANSMEM 761 781 Helical. {ECO:0000255}.; TRANSMEM 803 823 Helical. {ECO:0000255}. FUNCTION: May act as a zinc-influx transporter. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q61672 S29A2_MOUSE Equilibrative nucleoside transporter 2 (36 kDa hydrophobic nucleolar protein) (36 kDa nucleolar protein HNP36) (Delayed-early response protein 12) (Equilibrative nitrobenzylmercaptopurine riboside-insensitive nucleoside transporter) (Equilibrative NBMPR-insensitive nucleoside transporter) (Nucleoside transporter, ei-type) (Solute carrier family 29 member 2) 456 50,255 Chain (1); Erroneous initiation (1); Glycosylation (1); Modified residue (1); Transmembrane (11) TRANSMEM 13 33 Helical. {ECO:0000255}.; TRANSMEM 69 89 Helical. {ECO:0000255}.; TRANSMEM 98 118 Helical. {ECO:0000255}.; TRANSMEM 123 143 Helical. {ECO:0000255}.; TRANSMEM 161 181 Helical. {ECO:0000255}.; TRANSMEM 192 212 Helical. {ECO:0000255}.; TRANSMEM 288 308 Helical. {ECO:0000255}.; TRANSMEM 323 343 Helical. {ECO:0000255}.; TRANSMEM 360 380 Helical. {ECO:0000255}.; TRANSMEM 396 416 Helical. {ECO:0000255}.; TRANSMEM 432 452 Helical. {ECO:0000255}. FUNCTION: Mediates equilibrative transport of purine and pyrimidine nucleosides, and the purine base hypoxanthine. SUBCELLULAR LOCATION: Nucleus membrane; Multi-pass membrane protein. Basolateral cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q5FWH7 S39AC_MOUSE Zinc transporter ZIP12 (Solute carrier family 39 member 12) (Zrt- and Irt-like protein 12) (ZIP-12) 689 76,215 Alternative sequence (1); Chain (1); Compositional bias (2); Erroneous initiation (1); Glycosylation (2); Motif (1); Topological domain (9); Transmembrane (8) TRANSMEM 202 222 Helical. {ECO:0000255}.; TRANSMEM 370 390 Helical. {ECO:0000255}.; TRANSMEM 398 418 Helical. {ECO:0000255}.; TRANSMEM 448 468 Helical. {ECO:0000255}.; TRANSMEM 537 557 Helical. {ECO:0000255}.; TRANSMEM 601 621 Helical. {ECO:0000255}.; TRANSMEM 630 650 Helical. {ECO:0000255}.; TRANSMEM 663 683 Helical. {ECO:0000255}. TOPO_DOM 1 201 Extracellular. {ECO:0000255}.; TOPO_DOM 223 369 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 391 397 Extracellular. {ECO:0000255}.; TOPO_DOM 419 447 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 469 536 Extracellular. {ECO:0000255}.; TOPO_DOM 558 600 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 622 629 Extracellular. {ECO:0000255}.; TOPO_DOM 651 662 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 684 689 Extracellular. {ECO:0000255}. FUNCTION: Acts as a zinc-influx transporter. {ECO:0000305}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9WV96 T10B_MOUSE Mitochondrial import inner membrane translocase subunit Tim10 B (Mitochondrial import inner membrane translocase subunit Tim9 B) (TIMM10B) (Tim10b) 100 11,314 Chain (1); Disulfide bond (2); Motif (1); Sequence conflict (1) FUNCTION: Component of the TIM22 complex, a complex that mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. The TIM22 complex forms a twin-pore translocase that uses the membrane potential as the external driving force. In the TIM22 complex, it may act as a docking point for the soluble 70 kDa complex that guides the target proteins in transit through the aqueous mitochondrial intermembrane space. {ECO:0000250|UniProtKB:Q9Y5J6}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9Y5J6}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9Y5J6}. SUBUNIT: Component of the TIM22 complex, which core is composed of TIMM22, associated with TIMM10 (TIMM10A and/or TIMM10B), TIMM9, AGK and TIMM29. {ECO:0000250|UniProtKB:Q9Y5J6}. DOMAIN: The twin CX3C motif contains 4 conserved Cys residues that form 2 disulfide bonds in the mitochondrial intermembrane space. However, during the transit of TIMM10B from cytoplasm into mitochondrion, the Cys residues probably coordinate zinc, thereby preventing folding and allowing its transfer across mitochondrial outer membrane. {ECO:0000250|UniProtKB:P87108}. +Q9JJ11 TACC3_MOUSE Transforming acidic coiled-coil-containing protein 3 (ARNT-interacting protein) 631 70,627 Alternative sequence (2); Chain (1); Coiled coil (1); Helix (1); Initiator methionine (1); Modified residue (4); Region (2); Sequence conflict (2) FUNCTION: Plays a role in the microtubule-dependent coupling of the nucleus and the centrosome. Involved in the processes that regulate centrosome-mediated interkinetic nuclear migration (INM) of neural progenitors (PubMed:17920017). Acts as component of the TACC3/ch-TOG/clathrin complex proposed to contribute to stabilization of kinetochore fibers of the mitotic spindle by acting as inter-microtubule bridge. The TACC3/ch-TOG/clathrin complex is required for the maintenance of kinetochore fiber tension (By similarity). May be involved in the control of cell growth and differentiation. May have a role in embryonic development. {ECO:0000250|UniProtKB:Q9Y6A5, ECO:0000269|PubMed:17920017}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17920017}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9Y6A5}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q9PTG8}. Note=In complex with CKAP5 localized to microtubule plus-ends in mitosis and interphase. In complex with CKAP5 and clathrin localized to inter-microtubule bridges in mitotic spindles. {ECO:0000250|UniProtKB:Q9Y6A5}. SUBUNIT: Interacts with GCN5L2 and PCAF (By similarity). The coiled coil C-terminal region interacts with AH receptor nuclear translocator protein (ARNT) and ARNT2 (PubMed:11025203). Interacts with CCDC100/CEP120 (PubMed:17920017). Interacts with CKAP5 independently of clathrin. Interacts with CKAP5 and clathrin forming the TACC3/ch-TOG/clathrin complex located at spindle inter-microtubules bridges; TACC3 (phosphorylated at Ser-347 by AURKA) and CLTC are proposed to form a composite microtubule interaction surface (By similarity). {ECO:0000250|UniProtKB:Q9Y6A5, ECO:0000269|PubMed:11025203, ECO:0000269|PubMed:17920017}. TISSUE SPECIFICITY: Embryonically expressed. +E9PV87 TALD3_MOUSE Protein TALPID3 1520 166,721 Chain (1); Coiled coil (1); Erroneous initiation (1); Modified residue (6); Region (1); Sequence conflict (2) FUNCTION: Required for ciliogenesis and sonic hedgehog/SHH signaling (PubMed:21750036). Required for the centrosomal recruitment of RAB8A and for the targeting of centriole satellite proteins to centrosomes such as of PCM1. May play a role in early ciliogenesis in the disappearance of centriolar satellites that preceeds ciliary vesicle formation (By similarity). Involved in regulation of cell intracellular organization (PubMed:26386247). Involved in regulation of cell polarity (By similarity). Required for asymmetrical localization of CEP120 to daughter centrioles (PubMed:25251415). {ECO:0000250|UniProtKB:Q1G7G9, ECO:0000269|PubMed:21750036, ECO:0000269|PubMed:25251415, ECO:0000269|PubMed:26386247}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9BVV6}. Photoreceptor inner segment {ECO:0000269|PubMed:26386247}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:26386247}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:26386247}. Note=In photoreceptor cells localized to the joint between the inner and outer segments, specifically localized at the mother centriole (basal body) and the adjacent centriole as well as between the two centrioles but not in the connecting cilium (PubMed:26386247). {ECO:0000269|PubMed:26386247}. SUBUNIT: Interacts with CEP120 (PubMed:25251415). Interacts with CCP110, CEP290, CEP97, KIF24 (By similarity). {ECO:0000250|UniProtKB:Q9BVV6, ECO:0000269|PubMed:25251415}. TISSUE SPECIFICITY: Expressed in photoreceptor cells (at protein level). {ECO:0000269|PubMed:26386247}. +Q91WQ5 TAF5L_MOUSE TAF5-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 5L (PCAF-associated factor 65 beta) (PAF65-beta) 589 65,911 Chain (1); Repeat (6) FUNCTION: Functions as a component of the PCAF complex. The PCAF complex is capable of efficiently acetylating histones in a nucleosomal context. The PCAF complex could be considered as the human version of the yeast SAGA complex (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: The PCAF complex is composed of a number of TBP-associated factors (TAFS), such as TAF5, TAF5L, TAF6, TAF6L, TAF9, TAF10 and TAF12, PCAF, and also PCAF-associated factors (PAFs), such as TADA2L/ADA2, TADA3L/ADA3 and SPT3. Component of the STAGA transcription coactivator-HAT complex, at least composed of SUPT3H, GCN5L2, TAF5L, TAF6L, SUPT7L, TADA3L, TAD1L, TAF10, TAF12, TRRAP and TAF9 (By similarity). {ECO:0000250}. +Q8VI33 TAF9_MOUSE Transcription initiation factor TFIID subunit 9 (RNA polymerase II TBP-associated factor subunit G) (Transcription initiation factor TFIID 31 kDa subunit) (TAFII-31) (TAFII31) (Transcription initiation factor TFIID 32 kDa subunit) (TAFII-32) (TAFII32) 264 28,979 Chain (1); Compositional bias (1); Erroneous initiation (1); Modified residue (11); Sequence conflict (1) FUNCTION: Essential for cell viability. TAF9 and TAF9B are involved in transcriptional activation as well as repression of distinct but overlapping sets of genes. May have a role in gene regulation associated with apoptosis. TAFs are components of the transcription factor IID (TFIID) complex, the TBP-free TAFII complex (TFTC), the PCAF histone acetylase complex and the STAGA transcription coactivator-HAT complex. TFIID or TFTC are essential for the regulation of RNA polymerase II-mediated transcription (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of TFIID, the TATA-binding protein-free TAF complex (TFTC), the PCAF complex and the STAGA transcription coactivator-HAT complex. The PCAF complex consists at least of TADA2L/ADA2, SUPT3H/SPT3, TADA3L/ADA3, TAF5L/PAF65-beta, TAF6L/PAF65-alpha, TAF10/TAFII30, TAF12/TAFII20, TAF9/TAFII31 and TRRAP. The STAGA transcription coactivator-HAT complex consists at least of SUPT3H, GCN5L2, SUPT7L, TAF5L, TAF6L, TADA3L, TAD1L, TAF10, TAF12, TRRAP and TAF9. Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Binds N-terminal domain of p53/TP53 which is essential for transcription. Binds TFIIB and the Herpes simplex virus activator VP16. Forms a heterodimer with TAF6/TAFII80 in a complex with the TAF4B/TAFII105-TAF12/TAFII20 heterodimer. Also interacts with TAF5. Binds directly DNA. Increased DNA binding when complexed with TAF6/TAFII80 (By similarity). {ECO:0000250}. +Q3UKC1 TAXB1_MOUSE Tax1-binding protein 1 homolog 814 93,630 Chain (1); Coiled coil (1); Modified residue (6); Region (1); Sequence conflict (6); Zinc finger (2) FUNCTION: Inhibits TNF-induced apoptosis by mediating the TNFAIP3 anti-apoptotic activity. Degraded by caspase-3-like family proteins upon TNF-induced apoptosis. May also play a role in the pro-inflammatory cytokine IL-1 signaling cascade (By similarity). {ECO:0000250}. PTM: Phosphorylated in the C-terminal region by CHUK/IKKA leading to NF-kappa-B signaling down-regulation. {ECO:0000250}. SUBUNIT: Homooligomer. Interacts with TRAF6 in a IL-1-dependent manner. Interacts with STARD13 (By similarity). Interacts with TNFAIP3. {ECO:0000250, ECO:0000269|PubMed:10435631}. DOMAIN: The C-terminal UBZ-type zinc fingers function as ubiquitin-binding domains. {ECO:0000250|UniProtKB:Q86VP1}. +Q9CXF4 TBC15_MOUSE TBC1 domain family member 15 (GTPase-activating protein RAB7) (GAP for RAB7) (Rab7-GAP) 671 76,527 Chain (1); Domain (1); Initiator methionine (1); Modified residue (9) FUNCTION: Acts as a GTPase activating protein for RAB7A. Does not act on RAB4, RAB5 or RAB6. {ECO:0000269|PubMed:16055087, ECO:0000269|PubMed:20363736}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16055087}. TISSUE SPECIFICITY: Ubiquitous, with highest expression in heart, liver and testis and lower expression in brain, spleen, lung, kidney and skeletal muscle. {ECO:0000269|PubMed:16055087}. +Q80UB0 TEST2_MOUSE Testin-2 [Cleaved into: Testin-1] 333 38,090 Active site (2); Chain (2); Disulfide bond (3); Glycosylation (1); Sequence conflict (1); Signal peptide (1); Site (1) SUBCELLULAR LOCATION: Secreted {ECO:0000250}. TISSUE SPECIFICITY: Expressed in testis and ovary. Low level in spleen, epididymis, kidney, and uterus. Expressed in primary cultures of Sertoli cells. {ECO:0000269|PubMed:12606342}. +P80316 TCPE_MOUSE T-complex protein 1 subunit epsilon (TCP-1-epsilon) (CCT-epsilon) 541 59,624 Chain (1); Cross-link (7); Erroneous initiation (1); Initiator methionine (1); Modified residue (4); Sequence conflict (6) FUNCTION: Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin. {ECO:0000250|UniProtKB:P48643}. PTM: The N-terminus is blocked. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P48643}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P48643}. SUBUNIT: Component of the chaperonin-containing T-complex (TRiC), a heterooligomeric complex of about 850 to 900 kDa that forms two stacked rings, 12 to 16 nm in diameter. Interacts with PACRG (By similarity). Interacts with DNAAF4 (PubMed:23872636). {ECO:0000250|UniProtKB:P48643, ECO:0000269|PubMed:23872636}. +Q8BL74 TF3C2_MOUSE General transcription factor 3C polypeptide 2 (TF3C-beta) (Transcription factor IIIC 110 kDa subunit) (TFIIIC 110 kDa subunit) (TFIIIC110) (Transcription factor IIIC subunit beta) 907 100,275 Chain (1); Compositional bias (1); Erroneous initiation (1); Modified residue (10); Repeat (4); Sequence caution (1); Sequence conflict (7) FUNCTION: Required for RNA polymerase III-mediated transcription. Component of TFIIIC that initiates transcription complex assembly on tRNA and is required for transcription of 5S rRNA and other stable nuclear and cytoplasmic RNAs. May play a direct role in stabilizing interactions of TFIIIC2 with TFIIIC1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Part of the TFIIIC subcomplex TFIIIC2, consisting of six subunits, GTF3C1, GTF3C2, GTF3C3, GTF3C4, GTF3C5 and GTF3C6. {ECO:0000250}. +P47226 TES_MOUSE Testin (TES1/TES2) 423 47,983 Alternative sequence (1); Chain (1); Domain (4) FUNCTION: Scaffold protein that may play a role in cell adhesion, cell spreading and in the reorganization of the actin cytoskeleton. Plays a role in the regulation of cell proliferation. May act as a tumor suppressor (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21278383}. Cell junction, focal adhesion {ECO:0000250}. Note=Detected along actin stress fibers (By similarity). Detected at the subacrosomal layer in round spermatids. {ECO:0000250}. SUBUNIT: Interacts via LIM domain 1 with ZYX. Interacts (via LIM domain 3) with ENAH and VASP. Interacts with ALKBH4, talin, actin, alpha-actinin, GRIP1 and PXN. Interacts (via LIM domain 2) with ACTL7A (via N-terminus). Heterodimer with ACTL7A; the heterodimer interacts with ENAH to form a heterotrimer (By similarity). {ECO:0000250}. DOMAIN: The N-terminal and the C-terminal halves of the protein can associate with each other, thereby hindering interactions with ZYX. {ECO:0000250}. TISSUE SPECIFICITY: Detected at the acrosome of round spermatids (at protein level). Isoform TES1 transcript is highly expressed in adult testis and detected at low levels in other tissues. Isoform TES2 transcript is highly expressed in testis, kidney and spleen; intermediate in thymus, submaxillary gland and lung; detected at low levels in other tissues. {ECO:0000269|PubMed:21278383}. +Q9D9U4 TEX22_MOUSE Testis-expressed protein 22 (Testis-expressed protein of 22 kDa) 189 21,502 Chain (1); Sequence conflict (1) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12359214}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:12359214}. Note=Localizes in the acrosomal region of early elongating spermatids. During late stages of elongating spermatids, no longer detected in the acrosomal region, while it mainly localizes in the cytoplasm. Incorporated into the midpiece of spermatids and is also present in the mitochondrial sheath of mature spermatozoa. TISSUE SPECIFICITY: Mainly expressed in spermatocytes and spermatids in testis. {ECO:0000269|PubMed:12359214}. +Q9D8P7 TF3C6_MOUSE General transcription factor 3C polypeptide 6 (Transcription factor IIIC 35 kDa subunit) (TFIIIC 35 kDa subunit) (TFIIIC35) (Transcription factor IIIC subunit 6) 227 25,548 Chain (1) FUNCTION: Involved in RNA polymerase III-mediated transcription. Integral, tightly associated component of the DNA-binding TFIIIC2 subcomplex that directly binds tRNA and virus-associated RNA promoters (By similarity). {ECO:0000250|UniProtKB:Q969F1}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q969F1}. SUBUNIT: Part of the TFIIIC subcomplex TFIIIC2, consisting of six subunits, GTF3C1, GTF3C2, GTF3C3, GTF3C4, GTF3C5 and GTF3C6. Interacts with GTF3C4 and GTF3C5 (By similarity). {ECO:0000250|UniProtKB:Q969F1}. +Q9D1C8 VPS28_MOUSE Vacuolar protein sorting-associated protein 28 homolog (Caspase-activated DNase inhibitor that interacts with ASK1) (CIIA) (ESCRT-I complex subunit VPS28) 221 25,452 Chain (1); Domain (2); Modified residue (1) FUNCTION: Component of the ESCRT-I complex, a regulator of vesicular trafficking process. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Late endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. SUBUNIT: Component of the ESCRT-I complex (endosomal sorting complex required for transport I) which consists of TSG101, VPS28, a VPS37 protein (VPS37A to -D) and MVB12A or MVB12B in a 1:1:1:1 stoichiometry. Interacts with TSG101, VPS37B, VPS37C, MVB12A and MVB12B. Component of an ESCRT-I complex (endosomal sorting complex required for transport I) which consists of TSG101, VPS28, VPS37A and UBAP1 in a 1:1:1:1 stoichiometry. Interacts WITH VPS36; the interaction mediates the association with the ESCRT-II complex. Interacts with SNF8 and VPS25. Interacts with CEP55 (By similarity). {ECO:0000250}. +Q9QZ88 VPS29_MOUSE Vacuolar protein sorting-associated protein 29 (Vesicle protein sorting 29) 182 20,496 Alternative sequence (1); Beta strand (13); Chain (1); Helix (3); Metal binding (8); Modified residue (1); Mutagenesis (4); Turn (2) FUNCTION: Acts as component of the retromer cargo-selective complex (CSC). The CSC is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway. The recruitment of the CSC to the endosomal membrane involves RAB7A and SNX3. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX3-retromer mediates the retrograde endosome-to-TGN transport of WLS distinct from the SNX-BAR retromer pathway. The SNX27-retromer is believed to be involved in endosome-to-plasma membrane trafficking and recycling of a broad spectrum of cargo proteins. The CSC seems to act as recruitment hub for other proteins, such as the WASH complex and TBC1D5. Required to regulate transcytosis of the polymeric immunoglobulin receptor (pIgR-pIgA) (By similarity). Has no activity towards p-nitrophenylphosphate, p-nitrophenylphosphorylcholine or phosphatidylinositlphosphates or a phosphorylated peptide derived from retromer cargo (in vitro) (PubMed:21629666, PubMed:15965486). {ECO:0000250|UniProtKB:Q9UBQ0, ECO:0000269|PubMed:15965486, ECO:0000269|PubMed:21629666}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Endosome membrane {ECO:0000269|PubMed:15965486}; Peripheral membrane protein {ECO:0000269|PubMed:15965486}. SUBUNIT: Component of the heterotrimeric retromer cargo-selective complex (CSC), also described as vacuolar protein sorting subcomplex (VPS) formed by VPS26 (VPS26A or VPS26B), VPS29 and VPS35 (PubMed:21040701, PubMed:20875039, PubMed:21920005). The CSC has a highly elongated structure with VPS26 and VPS29 binding independently at opposite distal ends of VPS35 as central platform (By similarity). The CSC is believed to associate with variable sorting nexins to form functionally distinct retromer complex variants. The originally described retromer complex (also called SNX-BAR retromer) is a pentamer containing the CSC and a heterodimeric membrane-deforming subcomplex formed between SNX1 or SNX2 and SNX5 or SNX6 (also called SNX-BAR subcomplex); the respective CSC and SNX-BAR subcomplexes associate with low affinity. The CSC associates with SNX3 to form a SNX3-retromer complex. The CSC associates with SNX27, the WASH complex and the SNX-BAR subcomplex to form the SNX27-retromer complex (By similarity). Interacts with VPS26A, VPS26B, VPS35, ANKRD27 (PubMed:20875039, PubMed:21920005, PubMed:24856514). Interacts with SNX1, SNX2, SNX27, WASHC5 (By similarity). {ECO:0000250|UniProtKB:Q9UBQ0, ECO:0000269|PubMed:15965486, ECO:0000269|PubMed:20875039, ECO:0000269|PubMed:21040701, ECO:0000269|PubMed:21920005, ECO:0000269|PubMed:24856514}. +P46467 VPS4B_MOUSE Vacuolar protein sorting-associated protein 4B (EC 3.6.4.6) (Suppressor of K(+) transport growth defect 1) (Protein SKD1) 444 49,419 Beta strand (12); Chain (1); Coiled coil (1); Domain (1); Helix (17); Modified residue (3); Mutagenesis (3); Nucleotide binding (1); Sequence conflict (2); Turn (7) FUNCTION: Involved in late steps of the endosomal multivesicular bodies (MVB) pathway. Recognizes membrane-associated ESCRT-III assemblies and catalyzes their disassembly, possibly in combination with membrane fission. Redistributes the ESCRT-III components to the cytoplasm for further rounds of MVB sorting. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. In conjunction with the ESCRT machinery also appears to function in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis. VPS4A/B are required for the exosomal release of SDCBP, CD63 and syndecan (By similarity). {ECO:0000250|UniProtKB:O75351, ECO:0000269|PubMed:10393249, ECO:0000269|PubMed:10679028}. SUBCELLULAR LOCATION: Prevacuolar compartment membrane; Peripheral membrane protein. Late endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Membrane-associated in the prevacuolar endosomal compartment. SUBUNIT: Proposed to be monomeric or homodimeric in nucleotide-free form and to oligomerize upon binding to ATP to form two stacked hexameric or heptameric rings with a central pore through which ESCRT-III substrates are translocated in an ATP-dependent manner. In vitro, associates on the inside of a helical tubular structure formed by a CHMP2A-CHMP3 polymer. Interacts with CHMP1A, CHMP1B, CHMP4B and CHMP6. Interacts with CHMP2A (PubMed:15173323). Interacts with VPS4A; the interaction suggests a heteromeric assembly with VPS4A (PubMed:12594041). Interacts with VTA1 (By similarity). {ECO:0000250|UniProtKB:O75351, ECO:0000269|PubMed:12594041, ECO:0000269|PubMed:15173323}. DOMAIN: The MIT domain serves as an adapter for ESCRT-III proteins. It forms an asymmetric three-helix bundle that binds amphipathic MIM (MIT interacting motif) helices along the groove between MIT helices 2 and 3 present in a subset of ESCRT-III proteins thus establishing the canonical MIM-MIT interaction. In an extended conformation along the groove between helices 1 and 3, also binds to a type-2 MIT interacting motif (MIM2). {ECO:0000250|UniProtKB:O75351}. TISSUE SPECIFICITY: High level expression seen in the kidney. It is also expressed in the heart, brain, spleen, lung, liver, skeletal muscle, and testis. {ECO:0000269|PubMed:12594041, ECO:0000269|PubMed:8082782}. +Q9DA15 THEGL_MOUSE Testicular haploid expressed gene protein-like 459 51,801 Chain (1); Compositional bias (1); Repeat (8) +Q9JMB1 THEG_MOUSE Testicular haploid expressed gene protein 375 42,796 Alternative sequence (1); Chain (1); Modified residue (1); Repeat (7); Sequence conflict (2) FUNCTION: May be involved (but not essential) in spermatogenesis. {ECO:0000269|PubMed:12748127}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11173852, ECO:0000269|PubMed:12748127}. Note=Localized predominantly in the nucleus of haploid round spermatid. SUBUNIT: Interacts with CCT5. {ECO:0000269|PubMed:10747865}. TISSUE SPECIFICITY: Testis specific (at protein level). Specifically expressed in spermatids; Sertoli cells maintain the level of expression in spermatids. If isolated spermatids are cultivated for 16 hours alone, the expression of THEG is down-regulated. May require signals from Sertoli cells to initiate changes in its gene expression through spermatogenesis. {ECO:0000269|PubMed:10330110, ECO:0000269|PubMed:10747865, ECO:0000269|PubMed:11173852, ECO:0000269|PubMed:12748127}. +Q8CHW1 THAP1_MOUSE THAP domain-containing protein 1 210 24,611 Chain (1); Coiled coil (1); Motif (1); Zinc finger (1) FUNCTION: DNA-binding transcription regulator that regulates endothelial cell proliferation and G1/S cell-cycle progression. Specifically binds the 5'-[AT]NTNN[GT]GGCA[AGT]-3' core DNA sequence and acts by modulating expression of pRB-E2F cell-cycle target genes, including RRM1. Component of a THAP1/THAP3-HCFC1-OGT complex that is required for the regulation of the transcriptional activity of RRM1. May also have pro-apoptopic activity by potentiating both serum-withdrawal and TNF-induced apoptosis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}. Nucleus, PML body {ECO:0000250}. SUBUNIT: Interacts with PAWR. Component of a THAP1/THAP3-HCFC1-OGT complex that contains, either THAP1 or THAP3, HCFC1 and OGT. Interacts with OGT. Interacts (via the HBM) with HCFC1 (via the Kelch-repeat domain); the interaction recruits HCFC1 to the RRM1 promoter (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highest levels in heart, liver and kidney. Lower levels in brain and lung. {ECO:0000269|PubMed:20200153}. +P70701 WN10A_MOUSE Protein Wnt-10a 417 46,454 Chain (1); Disulfide bond (11); Glycosylation (2); Lipidation (1); Modified residue (1); Signal peptide (1) FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors (Probable). Functions in the canonical Wnt/beta-catenin signaling pathway. Plays a role in normal ectoderm development. Required for normal tooth development. Required for normal postnatal development and maintenance of tongue papillae and sweat ducts. Required for normal proliferation of basal cells in tongue filiform papillae, plantar epithelium and sweat ducts. Required for normal expression of keratins in tongue papillae. Required for normal expression of KRT9 in foot plant epithelium. Required for normal hair follicle function. {ECO:0000269|PubMed:28589954, ECO:0000305}. PTM: Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition. {ECO:0000250|UniProtKB:P27467, ECO:0000250|UniProtKB:P56704}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q9GZT5}. Secreted {ECO:0000250|UniProtKB:Q9GZT5}. SUBUNIT: Forms a soluble 1:1 complex with AFM; this prevents oligomerization and is required for prolonged biological activity. The complex with AFM may represent the physiological form in body fluids. {ECO:0000250|UniProtKB:Q9GZT5}. TISSUE SPECIFICITY: Detected in foot plant epidermis, footpad epidermis, haired skin epidermis. Detected in adult epithelia, including filiform and fungiform papillae and sweat ducts. Detected in sweat gland myoepithelial cells, but not in sweat gland mesenchyme. {ECO:0000269|PubMed:28589954}. +Q6IEE6 T132E_MOUSE Transmembrane protein 132E 982 106,990 Chain (1); Glycosylation (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 803 823 Helical. {ECO:0000255}. TOPO_DOM 26 802 Extracellular. {ECO:0000255}.; TOPO_DOM 824 982 Cytoplasmic. {ECO:0000255}. FUNCTION: Required for normal inner ear hair cell function and hearing. {ECO:0000250|UniProtKB:Q6IEE7}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Widely expressed, with highest levels in the cochlea. In the cochlea, detected in spiral ganglion, the organ of Corti and stria vascularis. In the organ of Corti, prominently expressed in the outer and inner hair cells, especially at the apical and basal region of the outer hair cell body (at protein level). {ECO:0000269|PubMed:25331638}. +Q64302 T4S1_MOUSE Transmembrane 4 L6 family member 1 (Membrane component chromosome 3 surface marker 1 homolog) (Tumor-associated antigen L6) 202 22,243 Chain (1); Glycosylation (2); Topological domain (5); Transmembrane (4) TRANSMEM 10 30 Helical. {ECO:0000305}.; TRANSMEM 50 70 Helical. {ECO:0000305}.; TRANSMEM 94 114 Helical. {ECO:0000305}.; TRANSMEM 162 182 Helical. {ECO:0000305}. TOPO_DOM 1 9 Cytoplasmic. {ECO:0000305|PubMed:7510285}.; TOPO_DOM 31 49 Extracellular. {ECO:0000305|PubMed:7510285}.; TOPO_DOM 71 93 Cytoplasmic. {ECO:0000305|PubMed:7510285}.; TOPO_DOM 115 161 Extracellular. {ECO:0000305|PubMed:7510285}.; TOPO_DOM 183 202 Cytoplasmic. {ECO:0000305|PubMed:7510285}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Note=Colocalizes with SDCBP2 in the apical region of the cell. {ECO:0000250|UniProtKB:P30408}. SUBUNIT: Present in high molecular weight complexes in tumor cells. Interacts with SDCBP2 (By similarity). {ECO:0000250|UniProtKB:P30408}. TISSUE SPECIFICITY: Highly expressed in skin and lung. Moderately expressed in lymph nodes and kidneys. Also present in thymic stroma and fibroblasts. {ECO:0000269|PubMed:7510285}. +Q5QD09 TAA7E_MOUSE Trace amine-associated receptor 7e (TaR-7e) (Trace amine receptor 7e) (mTaar7e) 358 40,163 Chain (1); Disulfide bond (1); Glycosylation (2); Topological domain (8); Transmembrane (7) TRANSMEM 48 68 Helical; Name=1. {ECO:0000255}.; TRANSMEM 84 104 Helical; Name=2. {ECO:0000255}.; TRANSMEM 122 143 Helical; Name=3. {ECO:0000255}.; TRANSMEM 167 187 Helical; Name=4. {ECO:0000255}.; TRANSMEM 213 233 Helical; Name=5. {ECO:0000255}.; TRANSMEM 275 295 Helical; Name=6. {ECO:0000255}.; TRANSMEM 310 333 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 47 Extracellular. {ECO:0000255}.; TOPO_DOM 69 83 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 105 121 Extracellular. {ECO:0000255}.; TOPO_DOM 144 166 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 188 212 Extracellular. {ECO:0000255}.; TOPO_DOM 234 274 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 296 309 Extracellular. {ECO:0000255}.; TOPO_DOM 334 358 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan olfactory receptor specific for trace amines. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Specifically expressed in neurons of the olfactory epithelium. {ECO:0000269|PubMed:16878137}. +Q5QD08 TAA7F_MOUSE Trace amine-associated receptor 7f (TaR-7f) (Trace amine receptor 7f) (mTaar7f) 358 40,165 Chain (1); Disulfide bond (1); Glycosylation (2); Topological domain (8); Transmembrane (7) TRANSMEM 48 68 Helical; Name=1. {ECO:0000255}.; TRANSMEM 84 104 Helical; Name=2. {ECO:0000255}.; TRANSMEM 122 143 Helical; Name=3. {ECO:0000255}.; TRANSMEM 167 187 Helical; Name=4. {ECO:0000255}.; TRANSMEM 213 233 Helical; Name=5. {ECO:0000255}.; TRANSMEM 275 295 Helical; Name=6. {ECO:0000255}.; TRANSMEM 310 333 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 47 Extracellular. {ECO:0000255}.; TOPO_DOM 69 83 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 105 121 Extracellular. {ECO:0000255}.; TOPO_DOM 144 166 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 188 212 Extracellular. {ECO:0000255}.; TOPO_DOM 234 274 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 296 309 Extracellular. {ECO:0000255}.; TOPO_DOM 334 358 Cytoplasmic. {ECO:0000255}. FUNCTION: Olfactory receptor activated by trace amine N-methylpiperidine. This receptor is probably mediated by the G(s)-class of G-proteins which activate adenylate cyclase. {ECO:0000269|PubMed:16878137}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Specifically expressed in neurons of the olfactory epithelium. {ECO:0000269|PubMed:16878137}. +Q5QD07 TAA8A_MOUSE Trace amine-associated receptor 8a (TaR-8a) (Trace amine receptor 8a) (mTaar8a) 344 37,848 Chain (1); Disulfide bond (1); Glycosylation (2); Topological domain (8); Transmembrane (7) TRANSMEM 32 52 Helical; Name=1. {ECO:0000255}.; TRANSMEM 68 88 Helical; Name=2. {ECO:0000255}.; TRANSMEM 112 132 Helical; Name=3. {ECO:0000255}.; TRANSMEM 147 167 Helical; Name=4. {ECO:0000255}.; TRANSMEM 196 216 Helical; Name=5. {ECO:0000255}.; TRANSMEM 261 281 Helical; Name=6. {ECO:0000255}.; TRANSMEM 283 303 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 31 Extracellular. {ECO:0000255}.; TOPO_DOM 53 67 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 89 111 Extracellular. {ECO:0000255}.; TOPO_DOM 133 146 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 168 195 Extracellular. {ECO:0000255}.; TOPO_DOM 217 260 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 282 282 Extracellular. {ECO:0000255}.; TOPO_DOM 304 344 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan olfactory receptor specific for trace amines. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Specifically expressed in neurons of the olfactory epithelium. {ECO:0000269|PubMed:16878137}. +Q62311 TAF6_MOUSE Transcription initiation factor TFIID subunit 6 (Transcription initiation factor TFIID 70 kDa subunit) (TAF(II)70) (TAFII-70) (TAFII70) (Transcription initiation factor TFIID 80 kDa subunit) (TAF(II)80) (TAFII-80) (TAFII80) (p80) 678 72,673 Chain (1); Cross-link (1); Modified residue (10) FUNCTION: TAFs are components of the transcription factor IID (TFIID) complex, PCAF histone acetylase complex and TBP-free TAFII complex (TFTC). TIIFD is multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: TFIID and PCAF are composed of TATA binding protein (TBP) and a number of TBP-associated factors (TAFs). TBP is not part of TFTC. Interacts directly with TBP, TAF1/TAFII250, TAF9/TAFII31 AND TAF12/TAFII20. The TAF6/TAFII70-TAF9/TAFII31 heterodimer forms an octamer complex with the TAF4B/TFII105-TAF12/TFIID20 heterodimer. Also interacts with the GTFs, TFIIEalpha/GTF2E1 and TFIIFalpha/GTF2F1. Component of the TFTC-HAT complex. Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Interacts with TP53/p53. {ECO:0000250|UniProtKB:P49848}. +P37804 TAGL_MOUSE Transgelin (Actin-associated protein p27) (Smooth muscle protein 22-alpha) (SM22-alpha) 201 22,576 Beta strand (2); Chain (1); Domain (1); Helix (6); Initiator methionine (1); Modified residue (5); Repeat (1); Sequence conflict (1); Turn (2) FUNCTION: Actin cross-linking/gelling protein. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. +Q80UV9 TAF1_MOUSE Transcription initiation factor TFIID subunit 1 (EC 2.3.1.48) (EC 2.7.11.1) (Cell cycle gene 1 protein) (TBP-associated factor 250 kDa) (p250) (Transcription initiation factor TFIID 250 kDa subunit) (TAF(II)250) (TAFII-250) (TAFII250) 1891 214,419 Alternative sequence (2); Chain (1); Compositional bias (3); Cross-link (2); DNA binding (1); Domain (4); Erroneous initiation (1); Modified residue (8); Motif (1); Region (2); Sequence conflict (12) FUNCTION: Largest component and core scaffold of the TFIID basal transcription factor complex (PubMed:10438527). Contains novel N- and C-terminal Ser/Thr kinase domains which can autophosphorylate or transphosphorylate other transcription factors. Phosphorylates TP53 on 'Thr-55' which leads to MDM2-mediated degradation of TP53. Phosphorylates GTF2A1 and GTF2F1 on Ser residues. Possesses DNA-binding activity. Essential for progression of the G1 phase of the cell cycle. Exhibits histone acetyltransferase activity towards histones H3 and H4. {ECO:0000250|UniProtKB:P21675, ECO:0000250|UniProtKB:Q60544, ECO:0000269|PubMed:10438527}. PTM: Phosphorylated by casein kinase II in vitro. {ECO:0000250|UniProtKB:P21675}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P21675}. SUBUNIT: TAF1 is the largest component of transcription factor TFIID that is composed of TBP and a variety of TBP-associated factors (PubMed:10438527). TAF1, when part of the TFIID complex, interacts with C-terminus of TP53. Part of a TFIID-containing RNA polymerase II pre-initiation complex that is composed of TBP and at least GTF2A1, GTF2A2, GTF2E1, GTF2E2, GTF2F1, GTF2H2, GTF2H3, GTF2H4, GTF2H5, GTF2B, TCEA1, ERCC2, ERCC3, TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13. Interacts with TAF7; the interaction is direct. Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, KAT8/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. RB1 interacts with the N-terminal domain of TAF1. Interacts with ASF1A and ASF1B. Interacts (via bromo domains) with acetylated lysine residues on the N-terminus of histone H1.4, H2A, H2B, H3 and H4 (in vitro) (By similarity). {ECO:0000250|UniProtKB:P21675}. DOMAIN: The Bromo domain mediates interaction with histones that have acetylated lysine residues at specific positions. The second domain also recognizes and binds histones that are butyrylated and crotonylated. {ECO:0000250|UniProtKB:P21675}. +Q8C838 TARG1_MOUSE Trafficking regulator of GLUT4 1 (Dispanin subfamily B member 1) (DSPB1) (Tumor suppressor candidate 5 homolog) 173 18,719 Chain (1); Modified residue (6); Topological domain (3); Transmembrane (2) TRANSMEM 103 123 Helical. {ECO:0000255}.; TRANSMEM 151 171 Helical. {ECO:0000255}. TOPO_DOM 1 102 Extracellular. {ECO:0000255}.; TOPO_DOM 124 150 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 172 173 Extracellular. {ECO:0000255}. FUNCTION: Regulates insulin-mediated adipose tissue glucose uptake and transport by modulation of SLC2A4 recycling. Not required for SLC2A4 membrane fusion upon an initial stimulus, but rather is necessary for proper protein recycling during prolonged insulin stimulation. {ECO:0000269|PubMed:26240143, ECO:0000269|PubMed:26629404}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26240143, ECO:0000269|PubMed:26629404}; Multi-pass membrane protein {ECO:0000305}. Endomembrane system {ECO:0000269|PubMed:26240143, ECO:0000269|PubMed:26629404}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:26240143}. Note=Shifts from low-density microsome vesicles to the cell membrane upon insulin stimulation. {ECO:0000269|PubMed:26240143, ECO:0000269|PubMed:26629404}. SUBUNIT: Interacts with SLC2A4; the interaction is required for proper SLC2A4 reacycling after insulin stimulation. {ECO:0000269|PubMed:26629404}. TISSUE SPECIFICITY: Expressed specifically in white and brown adipose tissues. {ECO:0000269|PubMed:26240143, ECO:0000269|PubMed:26629404}. +A2A690 TANC2_MOUSE Protein TANC2 (Tetratricopeptide repeat, ankyrin repeat and coiled-coil domain-containing protein 2) 1994 220,263 Alternative sequence (1); Chain (1); Glycosylation (1); Modified residue (14); Repeat (14) +Q8R5A6 TB22A_MOUSE TBC1 domain family member 22A 516 59,362 Alternative sequence (1); Chain (1); Domain (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (3); Sequence conflict (2) FUNCTION: May act as a GTPase-activating protein for Rab family protein(s). {ECO:0000250}. SUBUNIT: Homodimer. Interacts with ACBD3 and ARFGEF1. Interacts with YWHAB, YWHAE, YWHAG, YWHAH, YWHAQ and YWHAZ. {ECO:0000250|UniProtKB:Q8WUA7}. +Q9ERD7 TBB3_MOUSE Tubulin beta-3 chain 450 50,419 Chain (1); Modified residue (3); Mutagenesis (1); Nucleotide binding (1); Sequence conflict (1) FUNCTION: Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. TUBB3 plays a critical role in proper axon guidance and mantainance. {ECO:0000269|PubMed:20074521}. PTM: Some glutamate residues at the C-terminus are polyglycylated, resulting in polyglycine chains on the gamma-carboxyl group. Glycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Both modifications can coexist on the same protein on adjacent residues, and lowering polyglycylation levels increases polyglutamylation, and reciprocally. The precise function of polyglycylation is still unclear. {ECO:0000269|PubMed:19524510}.; PTM: Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (PubMed:15890843). Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity by SPAST increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold (By similarity). {ECO:0000250|UniProtKB:Q71U36, ECO:0000269|PubMed:15890843}.; PTM: Phosphorylated on Ser-172 by CDK1 during the cell cycle, from metaphase to telophase, but not in interphase. This phosphorylation inhibits tubulin incorporation into microtubules. {ECO:0000269|PubMed:16371510}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SUBUNIT: Dimer of alpha and beta chains. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells. DOMAIN: The highly acidic C-terminal region may bind cations such as calcium. +Q99LB0 TDIF1_MOUSE Deoxynucleotidyltransferase terminal-interacting protein 1 (Terminal deoxynucleotidyltransferase-interacting factor 1) (TdIF1) (TdT-interacting factor 1) 328 36,852 Chain (1); DNA binding (2); Modified residue (1); Motif (1); Region (2) FUNCTION: Increases DNTT terminal deoxynucleotidyltransferase activity (in vitro). Also acts as a transcriptional regulator, binding to the consensus sequence 5'-GNTGCATG-3' following an AT-tract. Associates with RAB20 promoter and positively regulates its transcription. Binds DNA and nucleosomes; may recruit HDAC1 complexes to nucleosomes or naked DNA. {ECO:0000250|UniProtKB:Q9H147}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H147}. SUBUNIT: Monomer and homodimer (By similarity). A minor proportion may form homotrimers (By similarity). Interacts with ZNF541 (PubMed:18849567). Interacts with the terminal deoxynucleotidyltransferase DNTT (By similarity). Interacts with TRERF1 (By similarity). Identified in a histone deacetylase complex that contains DNTTIP1, HDAC1 and ELMSAN1; this complex assembles into a tetramer that contains four copies of each protein chain (By similarity). Component of a histone deacetylase complex containing DNTTIP1, ZNF541, HDAC1 and HDAC2 (By similarity). {ECO:0000250|UniProtKB:Q9H147, ECO:0000269|PubMed:18849567}. DOMAIN: The N-terminal domain mediates dimerization. {ECO:0000250|UniProtKB:Q9H147}.; DOMAIN: The C-terminal domain mediates interaction with DNA and nucleosomes. It contains a HTH motif that mediates recognition of the consensus sequence. {ECO:0000250|UniProtKB:Q9H147}. +Q9DAG4 TEX37_MOUSE Testis-expressed sequence 37 protein (Testis-specific conserved protein of 21 kDa) 180 21,041 Alternative sequence (1); Chain (1) SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17091336}. Cytoplasm {ECO:0000250|UniProtKB:Q96LM6}. Note=Present in the germ cell lineage at all stages. {ECO:0000250|UniProtKB:Q96LM6}. TISSUE SPECIFICITY: Only detected after the mouse is 35 days old. Expression increases gradually from day 35 to 6 months, and remains stable after 54 days. Exclusively expressed in the epididymis and testis. Not expressed in other tissues. {ECO:0000269|PubMed:17091336}. +P48301 TEAD2_MOUSE Transcriptional enhancer factor TEF-4 (ETEF-1) (Embryonic TEA domain-containing factor) (ETF) (TEA domain family member 2) (TEAD-2) 445 49,041 Chain (1); Compositional bias (1); DNA binding (1); Region (1); Sequence conflict (1) FUNCTION: Transcription factor which plays a key role in the Hippo signaling pathway, a pathway involved in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein MST1/MST2, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Acts by mediating gene expression of YAP1 and WWTR1/TAZ, thereby regulating cell proliferation, migration and epithelial mesenchymal transition (EMT) induction (By similarity). Binds to the SPH and GT-IIC 'enhansons' (5'-GTGGAATGT-3'). May be involved in the gene regulation of neural development. Binds to the M-CAT motif. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with YAP1 and WWTR1/TAZ. {ECO:0000250}. TISSUE SPECIFICITY: Highest expression in brain. High levels also found in lung, testis and ovarian follicle cells. Lower levels in heart and spleen. +A2A8T7 TEX38_MOUSE Testis-expressed protein 38 (ATPAF1 antisense RNA 1) (ATPAF1 antisense gene protein 1) 201 22,716 Chain (1); Sequence conflict (1); Transmembrane (1) TRANSMEM 3 23 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q8BZ64 TECT1_MOUSE Tectonic-1 593 63,447 Alternative sequence (2); Chain (1); Compositional bias (1); Frameshift (1); Glycosylation (3); Modified residue (1); Signal peptide (1) FUNCTION: Component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. Regulator of Hedgehog (Hh), required for both activation and inhibition of the Hh pathway in the patterning of the neural tube. During neural tube development, it is required for formation of the most ventral cell types and for full Hh pathway activation. Functions in Hh signal transduction to fully activate the pathway in the presence of high Hh levels and to repress the pathway in the absence of Hh signals. Modulates Hh signal transduction downstream of SMO and RAB23. {ECO:0000269|PubMed:16357211, ECO:0000269|PubMed:21725307, ECO:0000269|PubMed:22179047}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body. Secreted. Note=Localizes at the transition zone, a region between the basal body and the ciliary axoneme. Despite the presence of a signal sequence, the full-length protein might not be secreted (PubMed:16357211). {ECO:0000269|PubMed:16357211}. SUBUNIT: Part of the tectonic-like complex (also named B9 complex). {ECO:0000269|PubMed:21725307, ECO:0000269|PubMed:22179047}. +O08524 TECTB_MOUSE Beta-tectorin 329 36,986 Chain (1); Disulfide bond (1); Domain (1); Glycosylation (4); Lipidation (1); Propeptide (1); Signal peptide (1) FUNCTION: One of the major non-collagenous components of the tectorial membrane (By similarity). The tectorial membrane is an extracellular matrix of the inner ear that covers the neuroepithelium of the cochlea and contacts the stereocilia bundles of specialized sensory hair cells. Sound induces movement of these hair cells relative to the tectorial membrane, deflects the stereocilia and leads to fluctuations in hair-cell membrane potential, transducing sound into electrical signals. {ECO:0000250}. PTM: The presence of a hydrophobic C-terminus preceded by a potential cleavage site strongly suggests that tectorins are synthesized as glycosylphosphatidylinositol-linked, membrane-bound precursors. Tectorins are targeted to the apical surface of the inner ear epithelia by the lipid and proteolytically released into the extracellular compartment. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}; Extracellular side {ECO:0000305}. Secreted, extracellular space, extracellular matrix. Note=Found in the non-collagenous matrix of the tectorial membrane. {ECO:0000250}. SUBUNIT: May form homomeric filament after self-association or heteromeric filament after association with alpha-tectorin. DOMAIN: Zona pellucida domain may enable to form filaments. +O70146 TESK1_MOUSE Dual specificity testis-specific protein kinase 1 (EC 2.7.12.1) (Testicular protein kinase 1) 627 68,052 Active site (1); Binding site (1); Chain (1); Domain (1); Modified residue (2); Nucleotide binding (1); Sequence conflict (2) FUNCTION: Dual specificity protein kinase activity catalyzing autophosphorylation and phosphorylation of exogenous substrates on both serine/threonine and tyrosine residues. Probably plays a central role at and after the meiotic phase of spermatogenesis (By similarity). {ECO:0000250}. SUBUNIT: Interacts with SPRY4. Interacts with TAOK2; leading to inhibit TAOK2 activity. Interacts with SPRED1; leading to inhibit activity (By similarity). {ECO:0000250}. DOMAIN: The extracatalytic C-terminal part is highly rich in proline residues. TISSUE SPECIFICITY: Predominantly expressed in testis. {ECO:0000269|PubMed:9469938}. +Q9ERA6 TFP11_MOUSE Tuftelin-interacting protein 11 (Septin and tuftelin-interacting protein 1) (STIP-1) (Tuftelin-interacting protein 39) 838 96,305 Chain (1); Compositional bias (1); Domain (1); Modified residue (6); Motif (1); Mutagenesis (4); Region (2); Sequence conflict (1) FUNCTION: Involved in pre-mRNA splicing, specifically in spliceosome disassembly during late-stage splicing events. Intron turnover seems to proceed through reactions in two lariat-intron associated complexes termed Intron Large (IL) and Intron Small (IS). In cooperation with DHX15 seems to mediate the transition of the U2, U5 and U6 snRNP-containing IL complex to the snRNP-free IS complex leading to efficient debranching and turnover of excised introns. May play a role in the differentiation of ameloblasts and odontoblasts or in the forming of the enamel extracellular matrix. {ECO:0000269|PubMed:15868102, ECO:0000269|PubMed:19857462}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=In the nucleus localizes to unique speckle domains in close proximity to nuclear speckles and not identical to paraspeckles. SUBUNIT: Identified in the spliceosome C complex. Found in the Intron Large (IL) complex, a post-mRNA release spliceosomal complex containing the excised intron, U2, U5 and U6 snRNPs, and splicing factors. Interacts with TUFT1. Interacts with DHX15; indicative for a recruitment of DHX15 to the IL complex. Interacts with GCFC2. {ECO:0000269|PubMed:10806191, ECO:0000269|PubMed:19165350}. TISSUE SPECIFICITY: Widely expressed. In tooth it is expressed in ameloblasts and odontoblasts. +Q3UR70 TGFA1_MOUSE Transforming growth factor-beta receptor-associated protein 1 (TGF-beta receptor-associated protein 1) (TRAP-1) (TRAP1) 860 97,303 Alternative sequence (2); Chain (1); Domain (1); Repeat (1) FUNCTION: Plays a role in the TGF-beta/activin signaling pathway. It associates with inactive heteromeric TGF-beta and activin receptor complexes, mainly through the type II receptor, and is released upon activation of signaling. May recruit SMAD4 to the vicinity of the receptor complex and facilitate its interaction with receptor-regulated Smads, such as SMAD2 (By similarity). {ECO:0000250}.; FUNCTION: Plays a role in vesicle-mediated protein trafficking of the endocytic membrane transport pathway. Believed to act as a component of the putative CORVET endosomal tethering complexes which is proposed to be involved in the Rab5-to-Rab7 endosome conversion probably implicating MON1A/B, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion. The CORVET complex is proposed to function as a Rab5 effector to mediate early endosome fusion probably in specific endosome subpopulations. Functions predominantly in APPL1-containing endosomes and in degradative but not recycling trafficking of endocytosed cargo (By similarity). {ECO:0000250|UniProtKB:Q8WUH2}. SUBCELLULAR LOCATION: Cytoplasm. Early endosome {ECO:0000250|UniProtKB:Q8WUH2}. Note=Colocalizes with TGF-beta receptors in the absence of signaling. {ECO:0000250|UniProtKB:Q8WUH2}. SUBUNIT: Interacts with TGFBR2 and ACVR2B; in the absence of ligand stimulation. Interacts with TGFBR1, ACVRL1, BMPR1A and ACVR1B; in the absence of ligand stimulation and to a less extent. Interacts with SMAD4; the interaction seems to be mutually exclusive with the interaction of SMAD4 and phosphorylated SMAD2. May interact with ALOX5 (By similarity). Interacts with RAB5C. Interacts with VPS8, VPS11 and VPS16. Component of the putative class C core vacuole/endosome tethering (CORVET) complex; the core of which composed of the class C Vps proteins VPS11, VPS16, VPS18 and VPS33A, is associated with VPS8 and TGFBRAP1 (PubMed:25266290). {ECO:0000250|UniProtKB:Q8WUH2, ECO:0000269|PubMed:25266290, ECO:0000305|PubMed:25266290}. +Q8C0V1 TERB1_MOUSE Telomere repeats-binding bouquet formation protein 1 (Coiled-coil domain-containing protein 79) 768 86,835 Alternative sequence (8); Beta strand (1); Chain (1); Coiled coil (1); Domain (1); Helix (3); Modified residue (1); Mutagenesis (2); Region (1); Repeat (2); Sequence conflict (1) FUNCTION: Meiosis-specific telomere-associated protein involved in meiotic telomere attachment to the nucleus inner membrane, a crucial step for homologous pairing and synapsis (PubMed:24885367, PubMed:24413433, PubMed:26548954). Component of the MAJIN-TERB1-TERB2 complex, which promotes telomere cap exchange by mediating attachment of telomeric DNA to the inner nuclear membrane and replacement of the protective cap of telomeric chromosomes: in early meiosis, the MAJIN-TERB1-TERB2 complex associates with telomeric DNA and the shelterin/telosome complex. During prophase, the complex matures and promotes release of the shelterin/telosome complex from telomeric DNA (PubMed:26548954). In the MAJIN-TERB1-TERB2 complex, TERB1 probably mediates association with the shelterin/telosome complex via interaction with TERF1, promoting priming telomeric DNA attachment' (PubMed:26548954). Promotes telomere association with the nuclear envelope and deposition of the SUN-KASH/LINC complex (PubMed:24885367, PubMed:24413433). Also recruits cohesin to telomeres to develop structural rigidity (PubMed:24413433). {ECO:0000269|PubMed:24413433, ECO:0000269|PubMed:26548954, ECO:0000305|PubMed:24885367}. PTM: Phosphorylated by CDK (PubMed:24413433, PubMed:26548954). Phosphorylation by CDK takes place in late prophase when the cap exchange is prominent (PubMed:26548954). is important for the stabilization of telomere attachment but dispenable for the cap exchange (PubMed:26548954). {ECO:0000269|PubMed:24413433, ECO:0000269|PubMed:26548954}. SUBCELLULAR LOCATION: Chromosome, telomere {ECO:0000269|PubMed:24413433, ECO:0000269|PubMed:24885367}. Nucleus inner membrane {ECO:0000269|PubMed:26548954}. Note=Localizes to telomeres during meiotic prophase (PubMed:24413433). In leptotene spermatocytes, localizes to telomeres that localize to the nucleus inner membrane (PubMed:26548954). {ECO:0000269|PubMed:24413433, ECO:0000269|PubMed:26548954}. SUBUNIT: Component of the MAJIN-TERB1-TERB2 complex, composed of MAJIN, TERB1 and TERB2 (PubMed:26548954). Interacts with TERF1, STAG3 and SUN1 (PubMed:24413433). Interacts (via Myb-like domain) with the cohesin complex; probably mediated via interaction with STAG3 (PubMed:24413433). {ECO:0000269|PubMed:24413433, ECO:0000269|PubMed:26548954}. TISSUE SPECIFICITY: Expressed in testis and fetal oocytes. {ECO:0000269|PubMed:24413433}. +P20352 TF_MOUSE Tissue factor (TF) (Coagulation factor III) (CD antigen CD142) 294 32,935 Chain (1); Disulfide bond (2); Glycosylation (4); Lipidation (1); Motif (1); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 252 274 Helical. {ECO:0000255}. TOPO_DOM 29 251 Extracellular. {ECO:0000255}.; TOPO_DOM 275 294 Cytoplasmic. {ECO:0000255}. FUNCTION: Initiates blood coagulation by forming a complex with circulating factor VII or VIIa. The [TF:VIIa] complex activates factors IX or X by specific limited protolysis. TF plays a role in normal hemostasis by initiating the cell-surface assembly and propagation of the coagulation protease cascade. SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P13726}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P13726}. SUBUNIT: Interacts with HSPE; the interaction, inhibited by heparin, promotes the generation of activated factor X and activates coagulation in the presence of activated factor VII. {ECO:0000250}. +P0C7L0 WIPF3_MOUSE WAS/WASL-interacting protein family member 3 (Corticosteroids and regional expression protein 16 homolog) 485 49,453 Alternative sequence (1); Chain (1); Compositional bias (3); Domain (1); Frameshift (1); Modified residue (4); Motif (5); Sequence conflict (1) FUNCTION: May be a regulator of cytoskeletal organization (Potential). May have a role in spermatogenesis. {ECO:0000269|PubMed:17573773, ECO:0000305}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17573773}. Note=In hippocampal neurons colocalizes with WASL in the cell body, axons and the growth cone (By similarity). Localizes to the actin filaments at the Sertoli cell-spermatid junctions. {ECO:0000250}. SUBUNIT: Interacts with WASL, and monomeric and filamentous actin. {ECO:0000250}. DOMAIN: The WH2 domain is found in a number of putative actin-binding proteins. {ECO:0000250}.; DOMAIN: The profilin-binding motif has been implicated in the interaction with profilin and SH3 domains. {ECO:0000250}.; DOMAIN: The KLKR motif is essential for G-actin binding and for actin polymerization. {ECO:0000250}. TISSUE SPECIFICITY: Isoform 1 is expressed in brain and testis and isoform 2 is expressed only in brain (at protein level). {ECO:0000269|PubMed:17573773}. +Q8QZT1 THIL_MOUSE Acetyl-CoA acetyltransferase, mitochondrial (EC 2.3.1.9) (Acetoacetyl-CoA thiolase) 424 44,816 Active site (3); Binding site (3); Chain (1); Metal binding (5); Modified residue (27); Region (1); Transit peptide (1) FUNCTION: Plays a major role in ketone body metabolism. {ECO:0000250}. PTM: Succinylation at Lys-265, adjacent to a coenzyme A binding site. Desuccinylated by SIRT5. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. SUBUNIT: Homotetramer. {ECO:0000250}. +Q5SSZ5 TENS3_MOUSE Tensin-3 (Tensin-like SH2 domain-containing protein 1) 1440 155,589 Alternative sequence (1); Chain (1); Domain (3); Modified residue (20); Sequence conflict (4) FUNCTION: May play a role in actin remodeling. Involved in the dissociation of the integrin-tensin-actin complex. EGF activates TNS4 and down-regulates TNS3 which results in capping the tail of ITGB1. Seems to be involved in mammary cell migration (By similarity). May be involved in cell migration and bone development. {ECO:0000250, ECO:0000269|PubMed:15733665}. SUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000250}. SUBUNIT: EGF promotes the interaction with EGFR. Interacts with PTK2/FAK1 and BCAR1. Tyrosine phosphorylation is critical for these interactions (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain, heart, lung, liver, spleen, kidney, stomach, small intestine, skeletal muscle, skin, thymus, testis, uterus, placenta, aorta and trachea. {ECO:0000269|PubMed:15733665}. +Q7M6U3 TEX14_MOUSE Inactive serine/threonine-protein kinase TEX14 (Testis-expressed sequence 14) (Testis-expressed sequence 14 protein) 1450 162,541 Alternative sequence (1); Binding site (1); Chain (1); Domain (1); Erroneous initiation (1); Modified residue (11); Motif (2); Mutagenesis (6); Nucleotide binding (1); Repeat (3); Sequence conflict (1) FUNCTION: Required both for the formation of intercellular bridges during meiosis and for kinetochore-microtubule attachment during mitosis. Intercellular bridges are evolutionarily conserved structures that connect differentiating germ cells and are required for spermatogenesis and male fertility. Acts by promoting the conversion of midbodies into intercellular bridges via its interaction with CEP55: interaction with CEP55 inhibits the interaction between CEP55 and PDCD6IP/ALIX and TSG101, blocking cell abscission and leading to transform midbodies into intercellular bridges. Also plays a role during mitosis: recruited to kinetochores by PLK1 during early mitosis and regulates the maturation of the outer kinetochores and microtubule attachment. Has no protein kinase activity in vitro. {ECO:0000269|PubMed:16549803, ECO:0000269|PubMed:19020301, ECO:0000269|PubMed:20176808, ECO:0000269|PubMed:22405274}. PTM: Phosphorylated on Thr residues by CDK1 during early phases of mitosis, promoting the interaction with PLK1 and recruitment to kinetochores. Phosphorylated on Ser-431 by PLK1 during late prometaphase promotes the rapid depletion from kinetochores and its subsequent degradation by the APC/C complex. {ECO:0000269|PubMed:22405274}. SUBCELLULAR LOCATION: Cytoplasm. Midbody. Chromosome, centromere, kinetochore. Note=Detected in the intercellular bridges that connect male germ cell daughter cells after cell division. SUBUNIT: Interacts with KIF23 and RBM44. Interacts with CEP55; inhibiting interaction between CEP55 and PDCD6IP/ALIX and TSG101. {ECO:0000269|PubMed:17383626, ECO:0000269|PubMed:20176808, ECO:0000269|PubMed:21364893}. DOMAIN: The protein kinase domain is predicted to be catalytically inactive.; DOMAIN: The GPPX3Y motif mediates interaction with CEP55. {ECO:0000269|PubMed:20176808}. TISSUE SPECIFICITY: Detected in testis and spermatogonia. Not detectable in the other tissues tested. {ECO:0000269|PubMed:11279525, ECO:0000269|PubMed:12711554, ECO:0000269|PubMed:16549803}. +P97499 TEP1_MOUSE Telomerase protein component 1 (Telomerase-associated protein 1) (Telomerase protein 1) (p240) (p80 telomerase homolog) 2629 291,460 Chain (1); Domain (2); Nucleotide binding (1); Repeat (25) FUNCTION: Component of the telomerase ribonucleoprotein complex that is essential for the replication of chromosome termini (By similarity). Also component of the ribonucleoprotein vaults particle, a multi-subunit structure involved in nucleo-cytoplasmic transport (PubMed:11149928). Responsible for the localizing and stabilizing vault RNA (vRNA) association in the vault ribonucleoprotein particle (PubMed:11149928). {ECO:0000250|UniProtKB:Q99973, ECO:0000269|PubMed:11149928}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome, telomere. SUBUNIT: Associated component of the telomerase holoenzyme complex (By similarity). Component of the vault ribonucleoprotein particle, at least composed of MVP, PARP4 and one or more vault RNAs (vRNAs) (PubMed:11149928, PubMed:9020079). Binds to VAULTRC1, VAULTRC2 and VAULTRC4/hvg4 vRNAs (PubMed:11149928, PubMed:9020079). {ECO:0000250|UniProtKB:Q99973, ECO:0000269|PubMed:11149928, ECO:0000269|PubMed:9020079}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9020079, ECO:0000269|PubMed:9118230}. +Q3TUU5 TEX30_MOUSE Testis-expressed protein 30 225 25,263 Chain (1); Erroneous initiation (2); Sequence conflict (1) +Q14BK3 TEX35_MOUSE Testis-expressed protein 35 (Testis-specific conserved protein of 24 kDa) 207 24,056 Alternative sequence (1); Chain (1); Coiled coil (1); Sequence conflict (4) SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17077512}. TISSUE SPECIFICITY: Testis-specific. Expressed during spermatogenesis. {ECO:0000269|PubMed:17077512}. +Q8R4I4 TF2AY_MOUSE TFIIA-alpha and beta-like factor (General transcription factor II A, 1-like factor) 468 51,525 Chain (1); Sequence conflict (1) FUNCTION: May function as a testis specific transcription factor. Binds DNA in conjunction with GTF2A2 and TBP (the TATA-binding protein) and together with GTF2A2, allows mRNA transcription. SUBCELLULAR LOCATION: Nucleus. TISSUE SPECIFICITY: Testis specific. Expressed in pachytene spermatocytes and haploid spermatids. {ECO:0000269|PubMed:11159353, ECO:0000269|PubMed:11889132}. +Q8VDR7 TGDS_MOUSE dTDP-D-glucose 4,6-dehydratase (EC 4.2.1.46) 355 40,570 Active site (3); Binding site (1); Chain (1); Sequence conflict (1) +Q924A0 TF7L2_MOUSE Transcription factor 7-like 2 (HMG box transcription factor 4) (T-cell-specific transcription factor 4) (T-cell factor 4) (TCF-4) (mTCF-4) 459 51,217 Alternative sequence (10); Chain (1); Compositional bias (1); Cross-link (2); DNA binding (1); Modified residue (2); Motif (1); Region (2); Sequence conflict (6) FUNCTION: Participates in the Wnt signaling pathway and modulates MYC expression by binding to its promoter in a sequence-specific manner. Acts as repressor in the absence of CTNNB1, and as activator in its presence. Activates transcription from promoters with several copies of the Tcf motif CCTTTGATC in the presence of CTNNB1. TLE1, TLE2, TLE3 and TLE4 repress transactivation mediated by TCF7L2/TCF4 and CTNNB1. Expression of dominant-negative mutants results in cell-cycle arrest in G1 (By similarity). Necessary for the maintenance of the epithelial stem-cell compartment of the small intestine. {ECO:0000250, ECO:0000269|PubMed:21856776, ECO:0000269|PubMed:9697701}. PTM: Phosphorylated at Thr-178 and/or Thr-189 by NLK. Phosphorylation by NLK at these sites inhibits DNA-binding by TCF7L2/TCF4, thereby preventing transcriptional activation of target genes of the canonical Wnt/beta-catenin signaling pathway (By similarity). {ECO:0000250}.; PTM: Polysumoylated. Sumoylation is enhanced by PIAS family members and desumoylation is enhanced by SENP2. Sumoylation/desumoylation regulates TCF7L2/TCF4 transcription activity in the Wnt/beta-catenin signaling pathway without altering interaction with CTNNB1 nor binding to DNA (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, PML body. Note=Diffuse pattern. Colocalizes with SUMO1 and PIAS4 in a subset of PML (promyelocytic leukemia) nuclear bodies (By similarity). {ECO:0000250}. SUBUNIT: Interacts with TGFB1I1 (PubMed:16291758). Interacts with SPIN1 (By similarity). Interacts with CTNNB1 (via the armadillo repeat); forms stable transcription complex (PubMed:19816403). Interacts with EP300. Interacts with NLK. Interacts with CCDC85B (probably through the HMG box); prevents interaction with CTNNB1 (By similarity). Interacts with TNIK (PubMed:19816403). Interacts with MAD2L2; prevents TCF7L2/TCF4 binding to promZIPK/DAPK3oters, negatively modulating its transcriptional activity. Interacts with ZIPK/DAPK3. Interacts with XIAP/BIRC4 and TLE3. Interacts with DDIT3/CHOP. The CTNNB1 and TCF7L2/TCF4 complex interacts with PML (isoform PML-4). Identified in a complex with CTNNB1 and FERMT2. Interacts with C11orf84/SPINDOC in a SPIN1-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q9NQB0, ECO:0000269|PubMed:16291758, ECO:0000269|PubMed:19816403}. TISSUE SPECIFICITY: Detected in adult brain and liver, and at lower levels in intestine, with a clear increase from the distal colon to the duodenum. Detected at low levels in heart, lung, kidney, pituitary and testis. DISEASE: Note=Constitutive activation and subsequent transactivation of target genes may lead to the maintenance of stem-cell characteristics (cycling and longevity) in cells that should normally undergo terminal differentiation and constitute the primary transforming event in colorectal cancer (CRC). +Q8BZH1 TGM4_MOUSE Protein-glutamine gamma-glutamyltransferase 4 (EC 2.3.2.13) (Experimental autoimmune prostatitis antigen 1) (Transglutaminase-4) (TGase-4) 670 75,591 Active site (3); Chain (1); Glycosylation (5); Metal binding (4); Sequence conflict (7) FUNCTION: Associated with the mammalian reproductive process. Plays an important role in the formation of the seminal coagulum through the cross-linking of specific proteins present in the seminal plasma. Transglutaminase is also required to stabilize the copulatory plug. {ECO:0000269|PubMed:19027372}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19027372}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q99041}. TISSUE SPECIFICITY: Expressed in the coagulating gland and in the dorsal part of the prostate. Not expressed in the brain, heart, kidney, liver, lung, muscle, pancreas, spleen, stomach, testis and thymus. {ECO:0000269|PubMed:16223778, ECO:0000269|PubMed:19027372}. +Q9D7I9 TGM5_MOUSE Protein-glutamine gamma-glutamyltransferase 5 (EC 2.3.2.13) (Transglutaminase-5) (TGase-5) 724 81,014 Active site (3); Chain (1); Initiator methionine (1); Metal binding (4); Modified residue (1) FUNCTION: Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. Contributes to the formation of the cornified cell envelope of keratinocytes (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Associated with intermediate filaments. {ECO:0000250}. +O88393 TGBR3_MOUSE Transforming growth factor beta receptor type 3 (TGF-beta receptor type 3) (TGFR-3) (Betaglycan) (Transforming growth factor beta receptor III) (TGF-beta receptor type III) 850 93,829 Beta strand (10); Chain (1); Disulfide bond (3); Domain (1); Glycosylation (7); Mutagenesis (2); Region (1); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (2) TRANSMEM 786 808 Helical. {ECO:0000255}. TOPO_DOM 23 785 Extracellular. {ECO:0000255}.; TOPO_DOM 809 850 Cytoplasmic. {ECO:0000255}. FUNCTION: Binds to TGF-beta. Could be involved in capturing and retaining TGF-beta for presentation to the signaling receptors (By similarity). {ECO:0000250}. PTM: Extensively modified by glycosaminoglycan (GAG), either chondroitin sulfate or heparan sulfate depending upon the tissue of origin. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Secreted {ECO:0000250}. Secreted, extracellular space, extracellular matrix {ECO:0000250}. Note=Exists both as a membrane-bound form and as soluble form in serum and in the extracellular matrix. {ECO:0000250}. SUBUNIT: Interacts with TCTEX1D4. {ECO:0000250}. +P70284 TGIF1_MOUSE Homeobox protein TGIF1 (5'-TG-3'-interacting factor 1) 272 29,573 Alternative sequence (1); Chain (1); Compositional bias (1); DNA binding (1); Motif (1); Sequence conflict (1) FUNCTION: Binds to a retinoid X receptor (RXR) responsive element from the cellular retinol-binding protein II promoter (CRBPII-RXRE). Inhibits the 9-cis-retinoic acid-dependent RXR alpha transcription activation of the retinoic acid responsive element. May participate in the transmission of nuclear signals during development and in the adult, as illustrated by the down-modulation of the RXR alpha activities (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with CTBP, SMAD2, SMAD3 and HDAC1. {ECO:0000250}. +Q921H8 THIKA_MOUSE 3-ketoacyl-CoA thiolase A, peroxisomal (EC 2.3.1.16) (Acetyl-CoA acyltransferase A) (Beta-ketothiolase A) (Peroxisomal 3-oxoacyl-CoA thiolase A) 424 43,953 Active site (3); Chain (1); Modified residue (2); Transit peptide (1) Lipid metabolism; fatty acid metabolism. SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Mainly expressed in liver and intestine. {ECO:0000269|PubMed:15043762}. +Q91YX0 THMS2_MOUSE Protein THEMIS2 (Induced by contact to basement membrane 1 protein) (Protein ICB-1) (Thymocyte-expressed molecule involved in selection protein 2) 663 74,378 Chain (1); Compositional bias (1); Erroneous initiation (1); Modified residue (2); Mutagenesis (3); Region (2) FUNCTION: May constitute a control point in macrophage inflammatory response, promoting LPS-induced TLR4-mediated TNF production. {ECO:0000269|PubMed:20644716}. PTM: Phosphorylation at Tyr-660 is induced by LPS. {ECO:0000269|PubMed:20644716}. SUBUNIT: When phosphorylated, interacts with LYN. Interacts with VAV1 and GRB2. {ECO:0000269|PubMed:20644716}. TISSUE SPECIFICITY: Restricted to B-cells, macrophages and dendritic cells. Down-regulated in splenocytes of mice developing arthritis in a collagen-induced model, not in those of mice failing to develop the disease. Transiently down-regulated in splenocytes of mice infected with influenza virus. {ECO:0000269|PubMed:19597499}. +Q9CU24 THMS3_MOUSE Protein THEMIS3 (Thymocyte-expressed molecule involved in selection protein 3) 569 64,720 Chain (1); Region (2) TISSUE SPECIFICITY: Specifically expressed in the intestine. {ECO:0000269|PubMed:19597499}. +Q3UH66 WNK2_MOUSE Serine/threonine-protein kinase WNK2 (EC 2.7.11.1) (Protein kinase lysine-deficient 2) (Protein kinase with no lysine 2) 2149 227,527 Active site (1); Alternative sequence (9); Binding site (2); Chain (1); Domain (1); Erroneous initiation (3); Modified residue (16); Nucleotide binding (1); Sequence conflict (1) FUNCTION: Serine/threonine kinase which plays an important role in the regulation of electrolyte homeostasis, cell signaling, survival, and proliferation. Acts as an activator and inhibitor of sodium-coupled chloride cotransporters and potassium-coupled chloride cotransporters respectively. Activates SLC12A2, SCNN1A, SCNN1B, SCNN1D and SGK1 and inhibits SLC12A5. Negatively regulates the EGF-induced activation of the ERK/MAPK-pathway and the downstream cell cycle progression. Affects MAPK3/MAPK1 activity by modulating the activity of MAP2K1 and this modulation depends on phosphorylation of MAP2K1 by PAK1. WNK2 acts by interfering with the activity of PAK1 by controlling the balance of the activity of upstream regulators of PAK1 activity, RHOA and RAC1, which display reciprocal activity. {ECO:0000269|PubMed:21733846}. PTM: Autophosphorylated. {ECO:0000250|UniProtKB:Q9Y3S1}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y3S1}. Cell membrane {ECO:0000250|UniProtKB:Q9Y3S1}. SUBUNIT: Forms a complex with the phosphorylated form of STK39 in the brain. {ECO:0000269|PubMed:21733846}. TISSUE SPECIFICITY: Brain and heart. {ECO:0000269|PubMed:21733846}. +B1AZI6 THOC2_MOUSE THO complex subunit 2 (Tho2) 1594 182,773 Chain (1); Coiled coil (2); Modified residue (8); Motif (1) FUNCTION: Required for efficient export of polyadenylated RNA and spliced mRNA. Acts as component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and which specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NFX1 pathway. Plays a role for proper neuronal development. {ECO:0000250|UniProtKB:Q8NI27}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Nucleus speckle {ECO:0000250}. SUBUNIT: Component of the THO complex, which is composed of THOC1, THOC2, THOC3, THOC5, THOC6 and THOC7; together with at least ALYREF/THOC4, DDX39B, SARNP/CIP29 and CHTOP, THO forms the transcription/export (TREX) complex which seems to have a dynamic structure involving ATP-dependent remodeling. Interacts with THOC1, POLDIP3 and ZC3H11A (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the hippocampus and the cortical neurons. {ECO:0000269|PubMed:26166480}. +Q80XP9 WNK3_MOUSE Serine/threonine-protein kinase WNK3 (EC 2.7.11.1) (Protein kinase lysine-deficient 3) (Protein kinase with no lysine 3) 1757 193,991 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Domain (1); Modified residue (7); Nucleotide binding (1) FUNCTION: Serine/threonine kinase which plays an important role in the regulation of electrolyte homeostasis, cell signaling, survival and proliferation. Acts as an activator and inhibitor of sodium-coupled chloride cotransporters and potassium-coupled chloride cotransporters respectively. Activates SLC12A1, SLC12A2, SLC12A3, SCNN1A, SCNN1B, SCNN1D and SGK1. Inhibits SLC12A4, SLC12A5, SLC12A6 and SLC12A7. Phosphorylates WNK4. Increases Ca(2+) influx mediated by TRPV5 and TRPV6 by enhancing their membrane expression level via a kinase-dependent pathway. Inhibits KCNJ1 by decreasing its expression at the cell membrane in a non-catalytic manner. {ECO:0000269|PubMed:19470686}. PTM: Ubiquitinated by the BCR(KLHL2) complex, leading to its degradation. {ECO:0000250|UniProtKB:Q9BYP7}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BYP7}. SUBUNIT: Interacts with WNK1 and WNK4. {ECO:0000250|UniProtKB:Q9BYP7}. TISSUE SPECIFICITY: Expressed in pancreatic duct (PubMed:21317537). {ECO:0000269|PubMed:21317537}. +Q8VE80 THOC3_MOUSE THO complex subunit 3 (Tho3) 351 38,738 Chain (1); Initiator methionine (1); Modified residue (1); Repeat (6); Sequence conflict (3) FUNCTION: Required for efficient export of polyadenylated RNA and spliced mRNA. Acts as component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and which specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NFX1 pathway (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Nucleus speckle {ECO:0000305}. SUBUNIT: Component of the THO complex, which is composed of THOC1, THOC2, THOC3, THOC5, THOC6 and THOC7; together with at least ALYREF/THOC4, DDX39B, SARNP/CIP29 and CHTOP, THO forms the transcription/export (TREX) complex which seems to have a dynamic structure involving ATP-dependent remodeling. {ECO:0000250}. +Q80UE6 WNK4_MOUSE Serine/threonine-protein kinase WNK4 (EC 2.7.11.1) (Protein kinase lysine-deficient 4) (Protein kinase with no lysine 4) 1222 132,410 Active site (1); Binding site (2); Chain (1); Cross-link (14); Domain (1); Erroneous initiation (3); Modified residue (5); Mutagenesis (5); Nucleotide binding (1); Sequence conflict (2) FUNCTION: Serine/threonine kinase which plays an important role in the regulation of electrolyte homeostasis, cell signaling, survival and proliferation. Acts as an activator and inhibitor of sodium-coupled chloride cotransporters and potassium-coupled chloride cotransporters respectively. Activates SCNN1A, SCNN1B, SCNN1D, SGK1, TRPV5 and TRPV6. Regulates the activity of the thiazide-sensitive Na-Cl cotransporter, SLC12A3, by phosphorylation which appears to prevent membrane trafficking of SLC12A3. Also inhibits the renal K(+) channel, KCNJ1, via a kinase-independent mechanism by which it induces clearance of the protein from the cell surface by clathrin-dependent endocytosis. WNK4 appears to act as a molecular switch that can vary the balance between NaCl reabsorption and K(+) secretion to maintain integrated homeostasis. Phosphorylates NEDD4L. Acts as a scaffold to inhibit SLC4A4 as well as CFTR activities and surface expression, recruits STK39 which mediates the inhibition (PubMed:21317537). {ECO:0000269|PubMed:12671053, ECO:0000269|PubMed:14608358, ECO:0000269|PubMed:17975670, ECO:0000269|PubMed:21317537}. PTM: Phosphorylated by WNK1 and WNK3. {ECO:0000269|PubMed:17975670}.; PTM: Ubiquitinated by the BCR(KLHL3) complex, leading to its degradation and increased expression of KCNJ1 at the cell surface. Ubiquitinated by the BCR(KLHL2) complex (By similarity). {ECO:0000250|UniProtKB:Q96J92}. SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000269|PubMed:11498583}. Note=Present exclusively in intercellular junctions in the distal convoluted tubule and in both the cytoplasm and intercellular junctions in the cortical collecting duct. WNK4 is part of the tight junction complex. {ECO:0000269|PubMed:11498583}. SUBUNIT: Interacts with the C-terminal region of KCNJ1 (PubMed:14608358). Interacts with WNK1 and WNK3 (PubMed:17975670). Interacts with KLHL3 (By similarity). {ECO:0000250|UniProtKB:Q96J92, ECO:0000269|PubMed:14608358, ECO:0000269|PubMed:17975670}. TISSUE SPECIFICITY: Locates to the distal convoluted tubule, the medullary collecting duct and the cortical collecting duct of the kidney (PubMed:11498583). Expressed in pancreatic duct (PubMed:21317537). {ECO:0000269|PubMed:11498583, ECO:0000269|PubMed:21317537}. +P48615 WNT11_MOUSE Protein Wnt-11 354 39,135 Chain (1); Disulfide bond (11); Glycosylation (5); Lipidation (1); Signal peptide (1) FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors. Probable developmental protein. May be a signaling molecule which affects the development of discrete regions of tissues. Is likely to signal over only few cell diameters. PTM: Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition. {ECO:0000250|UniProtKB:P27467, ECO:0000250|UniProtKB:P56704}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. +Q9QYS1 WNT16_MOUSE Protein Wnt-16 364 40,727 Chain (1); Disulfide bond (11); Glycosylation (3); Lipidation (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors. Probable developmental protein. May be a signaling molecule which affects the development of discrete regions of tissues. Is likely to signal over only few cell diameters (By similarity). {ECO:0000250}. PTM: Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition. {ECO:0000250|UniProtKB:P27467, ECO:0000250|UniProtKB:P56704}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. +P04426 WNT1_MOUSE Proto-oncogene Wnt-1 (Proto-oncogene Int-1) 370 41,086 Chain (1); Disulfide bond (11); Glycosylation (4); Lipidation (1); Signal peptide (1) FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors. Acts in the canonical Wnt signaling pathway by promoting beta-catenin-dependent transcriptional activation (By similarity). In some developmental processes, is also a ligand for the coreceptor RYK, thus triggering Wnt signaling (PubMed:15454084, PubMed:16116452). Plays an essential role in the development of the embryonic brain and central nervous system (CNS) (PubMed:2202907, PubMed:16116452). Has a role in osteoblast function, bone development and bone homeostasis (By similarity). {ECO:0000250|UniProtKB:P04628, ECO:0000269|PubMed:15454084, ECO:0000269|PubMed:16116452, ECO:0000269|PubMed:2202907}. PTM: Palmitoleoylation is required for efficient binding to frizzled receptors. Palmitoleoylation is necessary for proper trafficking to cell surface (By similarity). Depalmitoleoylated by NOTUM, leading to inhibit Wnt signaling pathway (By similarity). {ECO:0000250|UniProtKB:P56704, ECO:0000250|UniProtKB:Q91029}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P04628}. Secreted {ECO:0000250|UniProtKB:P04628}. SUBUNIT: Forms a soluble 1:1 complex with AFM; this prevents oligomerization and is required for prolonged biological activity. The complex with AFM may represent the physiological form in body fluids (By similarity). Interacts with PORCN (PubMed:10866835). Interacts with RSPO1, RSPO2 and RSPO3 (PubMed:16543246). Interacts with WLS (PubMed:19841259). {ECO:0000250|UniProtKB:P04628, ECO:0000269|PubMed:10866835, ECO:0000269|PubMed:16543246, ECO:0000269|PubMed:19841259}. TISSUE SPECIFICITY: Testis and mid-gestational embryos. In the testis, detected only in postmeiotic germ cells undergoing differentiation from round spermatids into mature spermatozoa. In the embryos, expression is restricted to the developing CNS in regions of the neural tube other than the telencephalon. Expressed in osteoblast; expression levels increase with advancing osteoblast differentiation. Expressed in the brain, femur, spleen, and hematopoietic bone marrow. {ECO:0000269|PubMed:23499309, ECO:0000269|PubMed:23656646, ECO:0000269|PubMed:3594566}. +O70283 WNT2B_MOUSE Protein Wnt-2b (Protein Wnt-13) 389 43,753 Chain (1); Disulfide bond (11); Glycosylation (2); Lipidation (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors (Probable). Functions in the canonical Wnt/beta-catenin signaling pathway (PubMed:19686689). Plays a redundant role in embryonic lung development (PubMed:19686689). {ECO:0000269|PubMed:19686689, ECO:0000305}. PTM: Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition. {ECO:0000250|UniProtKB:P27467, ECO:0000250|UniProtKB:P56704}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q93097}. Secreted {ECO:0000250|UniProtKB:Q93097}. SUBUNIT: Forms a soluble 1:1 complex with AFM; this prevents oligomerization and is required for prolonged biological activity. The complex with AFM may represent the physiological form in body fluids (By similarity). Interacts with FZD4 and FZD5 (By similarity). {ECO:0000250|UniProtKB:Q93097, ECO:0000250|UniProtKB:Q98SN7}. +P68368 TBA4A_MOUSE Tubulin alpha-4A chain (Alpha-tubulin 4) (Alpha-tubulin isotype M-alpha-4) (Tubulin alpha-4 chain) 448 49,924 Chain (1); Erroneous initiation (1); Modified residue (5); Nucleotide binding (1); Sequence conflict (1) FUNCTION: Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. PTM: Some glutamate residues at the C-terminus are polyglycylated, resulting in polyglycine chains on the gamma-carboxyl group. Glycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Both modifications can coexist on the same protein on adjacent residues, and lowering polyglycylation levels increases polyglutamylation, and reciprocally. The precise function of polyglycylation is still unclear. {ECO:0000269|PubMed:19524510}.; PTM: Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (PubMed:15890843). Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity by SPAST increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold (By similarity). {ECO:0000250|UniProtKB:Q71U36, ECO:0000269|PubMed:15890843}.; PTM: Acetylation of alpha chains at Lys-40 is located inside the microtubule lumen. This modification has been correlated with increased microtubule stability, intracellular transport and ciliary assembly. {ECO:0000250|UniProtKB:Q71U36}.; PTM: Methylation of alpha chains at Lys-40 is found in mitotic microtubules and is required for normal mitosis and cytokinesis contributing to genomic stability. {ECO:0000250|UniProtKB:P68363}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SUBUNIT: Dimer of alpha and beta chains. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells. Interacts with CFAP157 (PubMed:27965440). {ECO:0000269|PubMed:27965440}. +Q9CY27 TECR_MOUSE Very-long-chain enoyl-CoA reductase (EC 1.3.1.93) (Synaptic glycoprotein SC2) (Trans-2,3-enoyl-CoA reductase) (TER) 308 36,090 Chain (1); Glycosylation (2); Modified residue (3); Transmembrane (3) TRANSMEM 87 107 Helical. {ECO:0000255}.; TRANSMEM 194 214 Helical. {ECO:0000255}.; TRANSMEM 255 275 Helical. {ECO:0000255}. Lipid metabolism; fatty acid biosynthesis. FUNCTION: Catalyzes the last of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme reduces the trans-2,3-enoyl-CoA fatty acid intermediate to an acyl-CoA that can be further elongated by entering a new cycle of elongation. Thereby, it participates in the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. {ECO:0000250|UniProtKB:Q9NZ01}. PTM: Glycosylated. {ECO:0000250|UniProtKB:Q64232}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9NZ01}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9NZ01}. SUBUNIT: Interacts with ELOVL1 and LASS2. {ECO:0000250|UniProtKB:Q9NZ01}. +O70548 TELT_MOUSE Telethonin (Titin cap protein) 167 19,078 Chain (1); Modified residue (1) FUNCTION: Muscle assembly regulating factor. Mediates the antiparallel assembly of titin (TTN) molecules at the sarcomeric Z-disk (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere. SUBUNIT: Interacts with MYOZ1, MYOZ2 and MYOZ3. Interacts with CSRP3. Interacts directly with the N-terminal Ig-like domains of 2 titin (TTN) molecules. Interacts with ANKRD2; the interaction is direct (By similarity). {ECO:0000250}. +Q9DBA9 TF2H1_MOUSE General transcription factor IIH subunit 1 (Basic transcription factor 2 62 kDa subunit) (BTF2 p62) (General transcription factor IIH polypeptide 1) (TFIIH basal transcription factor complex p62 subunit) 547 61,851 Chain (1); Domain (2); Modified residue (3); Sequence conflict (4) FUNCTION: Component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module CAK controls the initiation of transcription. {ECO:0000250|UniProtKB:P32780}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Component of the 7-subunit TFIIH core complex composed of XPB/ERCC3, XPD/ERCC2, GTF2H1, GTF2H2, GTF2H3, GTF2H4 and GTF2H5, which is active in NER. The core complex associates with the 3-subunit CDK-activating kinase (CAK) module composed of CCNH/cyclin H, CDK7 and MNAT1 to form the 10-subunit holoenzyme (holo-TFIIH) active in transcription. Interacts with PUF60. {ECO:0000250|UniProtKB:P32780}. +Q62395 TFF3_MOUSE Trefoil factor 3 (Intestinal trefoil factor) (mITF) 81 8,808 Chain (1); Disulfide bond (4); Domain (1); Signal peptide (1) FUNCTION: Involved in the maintenance and repair of the intestinal mucosa. Promotes the mobility of epithelial cells in healing processes (motogen). {ECO:0000269|PubMed:8824194}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q07654}. Cytoplasm {ECO:0000250|UniProtKB:Q07654}. SUBUNIT: Monomer. Homodimer; disulfide-linked. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in goblet cells of the intestines and colon (at protein level). Expressed abundantly in goblet cells of intestine and colon, and at low levels in stomach. No expression in brain, lung, spleen, kidney, uterus, pancreas, liver, heart or thymus. {ECO:0000269|PubMed:7575467, ECO:0000269|PubMed:7741746}. +Q5DP50 TEX24_MOUSE Protein Tex24 (Testis-expressed protein 24) (Testis-specific factor 1) 351 38,993 Chain (1) FUNCTION: Nuclear factor which might have a role in spermatogenesis. {ECO:0000305|PubMed:16343427}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16343427}. TISSUE SPECIFICITY: Specific to testis, where it is expressed in spermatogonia. {ECO:0000269|PubMed:16343427}. +P62915 TF2B_MOUSE Transcription initiation factor IIB (EC 2.3.1.48) (General transcription factor TFIIB) (RNA polymerase II alpha initiation factor) 316 34,819 Chain (1); Metal binding (4); Modified residue (4); Region (4); Repeat (2); Zinc finger (1) FUNCTION: General transcription factor that plays a role in transcription initiation by RNA polymerase II (Pol II). Involved in the pre-initiation complex (PIC) formation and Pol II recruitment at promoter DNA. Together with the TATA box-bound TBP forms the core initiation complex and provides a bridge between TBP and the Pol II-TFIIF complex. Released from the PIC early following the onset of transcription during the initiation and elongation transition and reassociates with TBP during the next transcription cycle. Associates with chromatin to core promoter-specific regions. Binds to two distinct DNA core promoter consensus sequence elements in a TBP-independent manner; these IIB-recognition elements (BREs) are localized immediately upstream (BREu), 5'-[GC][GC][GA]CGCC-3', and downstream (BREd), 5'-[GA]T[TGA][TG][GT][TG][TG]-3', of the TATA box element. Modulates transcription start site selection. Exhibits also autoacetyltransferase activity that contributes to the activated transcription. {ECO:0000250|UniProtKB:Q00403}. PTM: Acetylated. Autoacetylated; autoacetylation at Lys-238 stimulates transcription activation. {ECO:0000250|UniProtKB:Q00403}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q00403}. Chromosome {ECO:0000250|UniProtKB:Q00403}. Note=Non-acetylated form colocalizes with DNA in the G0/1, S and G2 phases of the cell cycle, but not during mitosis. Acetylated form colocalizes at transcriptionally silent mitotic chromatids during mitosis at metaphase, anaphase, and telophase phases of the cell cycle. {ECO:0000250|UniProtKB:Q00403}. SUBUNIT: Found in a ternary complex with TATA box-bound TBP. Part of a TFIID-containing RNA polymerase II pre-initiation complex (PIC) that is composed of TBP and at least GTF2A1, GTF2A2, GTF2E1, GTF2E2, GTF2F1, GTF2H2, GTF2H3, GTF2H4, GTF2H5, GTF2B, TCEA1, ERCC2, ERCC3, TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13. Associates with TFIID-TFIIA (DA complex) to form TFIID-TFIIA-TFIIB (DAB complex), which is then recognized by RNA polymerase II (Pol II). Found in a RNA polymerase II initiation complex. Interacts (via C-terminus) with TBP; this interaction with TATA box-bound TBP guides Pol II into the PIC. Interacts (via N-terminus) with Pol II. Interacts (via C-terminus) with SSU72; this interaction is inhibited by SYMPK. Interacts with NR2F1; this interaction is direct. Interacts with PGR. Interacts with ESR1. Interacts with GTF2F1 (via C-terminus and preferentially via acetylated form); this interaction prevents binding of GTF2B to GTF2F2. Interacts with GTF2F2 (via N-terminus); this interaction is inhibited in presence of GTF2F1. Interacts with the transcription elongation factor TCEA2. Interacts with HSF1 (via transactivation domain) (By similarity). Interacts with GPBP1 (PubMed:14612417). {ECO:0000250|UniProtKB:Q00403, ECO:0000269|PubMed:14612417}. DOMAIN: The TFIIB-type zinc-binding domain is necessary for the interaction and recruitment of RNA polymerase II to the core promoter, the formation of a fully competent pre-initiation complex (PIC) assembly and basal transcription initiation. The C-terminus is necessary and sufficient for interaction with the TATA box-bound TBP complex and for the formation of PIC. {ECO:0000250|UniProtKB:Q00403}. +Q9JKX3 TFR2_MOUSE Transferrin receptor protein 2 (TfR2) 798 88,402 Alternative sequence (3); Chain (1); Disulfide bond (2); Glycosylation (3); Motif (1); Sequence conflict (8); Topological domain (2); Transmembrane (1) TRANSMEM 82 102 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 81 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 103 798 Extracellular. {ECO:0000255}. FUNCTION: Mediates cellular uptake of transferrin-bound iron in a non-iron dependent manner. May be involved in iron metabolism, hepatocyte function and erythrocyte differentiation. SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein.; SUBCELLULAR LOCATION: Isoform 3: Cytoplasm. TISSUE SPECIFICITY: Predominantly expressed in liver. Also expressed in kidney, spleen, brain, lung, heart and muscle with very low expression in kidney, muscle and heart. +Q9D494 TERB2_MOUSE Telomere repeats-binding bouquet formation protein 2 218 25,030 Chain (1) FUNCTION: Meiosis-specific telomere-associated protein involved in meiotic telomere attachment to the nucleus inner membrane, a crucial step for homologous pairing and synapsis. Component of the MAJIN-TERB1-TERB2 complex, which promotes telomere cap exchange by mediating attachment of telomeric DNA to the inner nuclear membrane and replacement of the protective cap of telomeric chromosomes: in early meiosis, the MAJIN-TERB1-TERB2 complex associates with telomeric DNA and the shelterin/telosome complex. During prophase, the complex matures and promotes release of the shelterin/telosome complex from telomeric DNA. {ECO:0000269|PubMed:26548954}. SUBCELLULAR LOCATION: Chromosome, telomere {ECO:0000269|PubMed:26548954}. Nucleus inner membrane {ECO:0000269|PubMed:26548954}. Note=Localizes to telomeres throughout meiotic prophase I and disapears in metaphase I. In leptotene spermatocytes, localizes to telomeres that localize to the nucleus inner membrane. {ECO:0000269|PubMed:26548954}. SUBUNIT: Component of the MAJIN-TERB1-TERB2 complex, composed of MAJIN, TERB1 and TERB2. {ECO:0000269|PubMed:26548954}. TISSUE SPECIFICITY: Specifically expressed in germline tissues. {ECO:0000269|PubMed:26548954}. +P21981 TGM2_MOUSE Protein-glutamine gamma-glutamyltransferase 2 (EC 2.3.2.13) (Tissue transglutaminase) (Transglutaminase C) (TG(C)) (TGC) (TGase C) (Transglutaminase-2) (TGase-2) 686 77,061 Active site (3); Chain (1); Initiator methionine (1); Metal binding (4); Modified residue (2); Sequence conflict (18) FUNCTION: Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. SUBUNIT: Monomer. +Q03404 TFF2_MOUSE Trefoil factor 2 (Spasmolytic polypeptide) (SP) 129 14,172 Chain (1); Disulfide bond (7); Domain (2); Signal peptide (1) FUNCTION: Inhibits gastrointestinal motility and gastric acid secretion. Could function as a structural component of gastric mucus, possibly by stabilizing glycoproteins in the mucus gel through interactions with carbohydrate side chains (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Stomach and pancreas. +P43025 TETN_MOUSE Tetranectin (TN) (C-type lectin domain family 3 member B) (Plasminogen kringle 4-binding protein) 202 22,257 Chain (1); Disulfide bond (3); Domain (1); Sequence conflict (4); Signal peptide (1) FUNCTION: Tetranectin binds to plasminogen and to isolated kringle 4. May be involved in the packaging of molecules destined for exocytosis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Homotrimer. {ECO:0000250}. TISSUE SPECIFICITY: Highest expression in lung and skeletal muscle. +P17125 TGFB3_MOUSE Transforming growth factor beta-3 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-3 (TGF-beta-3)] 410 46,885 Chain (2); Disulfide bond (5); Glycosylation (3); Modified residue (1); Motif (1); Signal peptide (1) FUNCTION: Transforming growth factor beta-3 proprotein: Precursor of the Latency-associated peptide (LAP) and Transforming growth factor beta-3 (TGF-beta-3) chains, which constitute the regulatory and active subunit of TGF-beta-3, respectively. {ECO:0000250|UniProtKB:P01137, ECO:0000250|UniProtKB:P04202}.; FUNCTION: Latency-associated peptide: Required to maintain the Transforming growth factor beta-3 (TGF-beta-3) chain in a latent state during storage in extracellular matrix (By similarity). Associates non-covalently with TGF-beta-3 and regulates its activation via interaction with 'milieu molecules', such as LTBP1 and LRRC32/GARP, that control activation of TGF-beta-3 (PubMed:28912269). Interaction with integrins results in distortion of the Latency-associated peptide chain and subsequent release of the active TGF-beta-3 (By similarity). {ECO:0000250|UniProtKB:P01137, ECO:0000250|UniProtKB:P04202, ECO:0000269|PubMed:28912269}.; FUNCTION: Transforming growth factor beta-3: Multifunctional protein that regulates embryogenesis and cell differentiation and is required in various processes such as secondary palate development (PubMed:7493021, PubMed:7493022, PubMed:10433915, PubMed:28912269). Activation into mature form follows different steps: following cleavage of the proprotein in the Golgi apparatus, Latency-associated peptide (LAP) and Transforming growth factor beta-3 (TGF-beta-3) chains remain non-covalently linked rendering TGF-beta-3 inactive during storage in extracellular matrix (By similarity). At the same time, LAP chain interacts with 'milieu molecules', such as LTBP1 and LRRC32/GARP that control activation of TGF-beta-3 and maintain it in a latent state during storage in extracellular milieus (PubMed:28912269). TGF-beta-3 is released from LAP by integrins: integrin-binding results in distortion of the LAP chain and subsequent release of the active TGF-beta-3 (By similarity). Once activated following release of LAP, TGF-beta-3 acts by binding to TGF-beta receptors (TGFBR1 and TGFBR2), which transduce signal (By similarity). {ECO:0000250|UniProtKB:P01137, ECO:0000250|UniProtKB:P04202, ECO:0000269|PubMed:10433915, ECO:0000269|PubMed:28912269, ECO:0000269|PubMed:7493021, ECO:0000269|PubMed:7493022}. PTM: Transforming growth factor beta-3 proprotein: The precursor proprotein is cleaved in the Golgi apparatus to form Transforming growth factor beta-3 (TGF-beta-3) and Latency-associated peptide (LAP) chains, which remain non-covalently linked, rendering TGF-beta-3 inactive. {ECO:0000250|UniProtKB:P01137}.; PTM: Methylated at Gln-291 by N6AMT1. {ECO:0000250|UniProtKB:P10600}. SUBCELLULAR LOCATION: Latency-associated peptide: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P01137}.; SUBCELLULAR LOCATION: Transforming growth factor beta-3: Secreted {ECO:0000250|UniProtKB:P01137}. SUBUNIT: Interacts with ASPN (By similarity). Latency-associated peptide: Homodimer; disulfide-linked (By similarity). Latency-associated peptide: Interacts with Transforming growth factor beta-3 (TGF-beta-3) chain; interaction is non-covalent and maintains (TGF-beta-3) in a latent state (By similarity). Latency-associated peptide: Interacts with LRRC32/GARP; leading to regulate activation of TGF-beta-3 and promote epithelial fusion during palate development (PubMed:28912269). Latency-associated peptide: Interacts (via cell attachment site) with integrins, leading to release of the active TGF-beta-3 (By similarity). Transforming growth factor beta-3: Homodimer; disulfide-linked (By similarity). Transforming growth factor beta-3: Interacts with TGF-beta receptors (TGFBR1 and TGFBR2), leading to signal transduction (By similarity). {ECO:0000250|UniProtKB:P01137, ECO:0000250|UniProtKB:P04202, ECO:0000250|UniProtKB:P10600, ECO:0000269|PubMed:28912269}. +Q62219 TGFI1_MOUSE Transforming growth factor beta-1-induced transcript 1 protein (Androgen receptor-associated protein of 55 kDa) (Hydrogen peroxide-inducible clone 5 protein) (Hic-5) (TGF beta-stimulated clone 5) (TSC-5) 461 50,101 Alternative sequence (12); Chain (1); Domain (4); Erroneous initiation (2); Erroneous translation (2); Frameshift (1); Modified residue (12); Motif (4); Mutagenesis (9); Region (3) FUNCTION: Functions as a molecular adapter coordinating multiple protein-protein interactions at the focal adhesion complex and in the nucleus. Links various intracellular signaling modules to plasma membrane receptors and regulates the Wnt and TGFB signaling pathways. May also regulate SLC6A3 and SLC6A4 targeting to the plasma membrane hence regulating their activity. In the nucleus, functions as a nuclear receptor coactivator regulating glucocorticoid, androgen, mineralocorticoid and progesterone receptor transcriptional activity. May play a role in the processes of cell growth, proliferation, migration, differentiation and senescence. May have a zinc-dependent DNA-binding activity. {ECO:0000269|PubMed:10649439, ECO:0000269|PubMed:10848625, ECO:0000269|PubMed:11463817, ECO:0000269|PubMed:11546764, ECO:0000269|PubMed:11937715, ECO:0000269|PubMed:12153727, ECO:0000269|PubMed:14755691, ECO:0000269|PubMed:15687259, ECO:0000269|PubMed:15713747, ECO:0000269|PubMed:16183059, ECO:0000269|PubMed:16291758, ECO:0000269|PubMed:16737959, ECO:0000269|PubMed:17166536, ECO:0000269|PubMed:17233630, ECO:0000269|PubMed:17299801, ECO:0000269|PubMed:7929412, ECO:0000269|PubMed:9722648}. PTM: Phosphorylated by gonadotropin-releasing hormone-activated SRC. {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, focal adhesion. Nucleus matrix. Cytoplasm, cytoskeleton. Note=Associated with the actin cytoskeleton, colocalizes with stress fibers. SUBUNIT: Homooligomer. Interacts with CRIP2, HSPB1, ILK, LIMS1, LIMS2, NCK2, NUDT16L1, PAK, PPARG, PTPN12, TCF3, TCF7L2 and VCL. Forms a complex with GIT1 and ARHGEF7. Interacts with AR/androgen receptor in a ligand-dependent manner. Interacts with CSK, LYN, MAPK15, NR3C1, PPARG, PTK2/FAK1, PTK2B/PYK2, SLC6A3, SLC6A4, SMAD3, SRC and talin. Interacts (via LIM zinc-binding domain 2) with CBLC (via RING-type zinc finger); the interaction is direct and enhances CBLC E3 ubiquitin-protein ligase activity. {ECO:0000269|PubMed:10092676, ECO:0000269|PubMed:10330411, ECO:0000269|PubMed:10649439, ECO:0000269|PubMed:10848625, ECO:0000269|PubMed:11134073, ECO:0000269|PubMed:11546764, ECO:0000269|PubMed:11779876, ECO:0000269|PubMed:11805099, ECO:0000269|PubMed:12153727, ECO:0000269|PubMed:12177201, ECO:0000269|PubMed:14755691, ECO:0000269|PubMed:15687259, ECO:0000269|PubMed:15713747, ECO:0000269|PubMed:16291758, ECO:0000269|PubMed:16624805, ECO:0000269|PubMed:16737959, ECO:0000269|PubMed:17233630, ECO:0000269|PubMed:9422762, ECO:0000269|PubMed:9756887, ECO:0000269|PubMed:9858471}. DOMAIN: The LIM zinc-binding domains mediate glucocorticoid receptor coactivation and interaction with AR, CRIP2, ILK, LIMS1, NR3C1, PPARG, TCF3, TCF7L2, SLC6A3 and SMAD3. The LIM zinc-binding 2 and LIM zinc-binding 3 domains mediate targeting to focal adhesions and actin stress fibers. The LIM zinc-binding 3 and LIM zinc-binding 4 domains mediate interaction with TRAF4 and MAPK15. The LIM zinc-binding 4 domain mediates interaction with HSPB1, homooligomerization and targeting to the nuclear matrix. The LIM zinc-binding 3 domain mediates interaction with PTPN12.; DOMAIN: The LD (leucine and aspartate-rich) motif 3 mediates interaction with GIT1 and functions as a nuclear export signal. TISSUE SPECIFICITY: Ubiquitously expressed. Higher expression is detected in lung and spleen. Expression decreases during pregnancy in mammary glands. Expressed in all brain areas, with higher levels in cerebellum, prefrontal cortex and hypothalamus. Expressed in smooth muscle, myoepithelial cells and platelets (at protein level). Preferentially expressed in mesenchymal versus epithelial cells (at protein level). {ECO:0000269|PubMed:12177201, ECO:0000269|PubMed:15713747, ECO:0000269|PubMed:16219310, ECO:0000269|PubMed:16219691, ECO:0000269|PubMed:17233630, ECO:0000269|PubMed:7929412}. +Q8CI71 VPS50_MOUSE Syndetin (Bcl2-like protein blm) (Coiled-coil domain-containing protein 132) (EARP/GARPII complex subunit VPS50) 964 111,174 Alternative sequence (4); Chain (1); Coiled coil (2); Cross-link (2); Erroneous initiation (2); Modified residue (6); Sequence conflict (5) FUNCTION: Acts as component of the EARP complex that is involved in endocytic recycling. The EARP complex associates with Rab4-positive endosomes and promotes recycling of internalized transferrin receptor (TFRC) to the plasma membrane. Within the EARP complex, required to tether the complex to recycling endosomes. Not involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN). {ECO:0000250|UniProtKB:Q96JG6}. SUBCELLULAR LOCATION: Recycling endosome {ECO:0000250|UniProtKB:Q96JG6}. SUBUNIT: Component of the endosome-associated retrograde protein (EARP) complex, composed of VPS51, VPS52, VPS53 and VPS50/Syndetin. The EARP complex interacts with EIPR1. {ECO:0000250|UniProtKB:F1LSG8, ECO:0000250|UniProtKB:Q96JG6}. +Q3UVL4 VPS51_MOUSE Vacuolar protein sorting-associated protein 51 homolog (Protein fat-free homolog) 782 86,187 Alternative sequence (4); Chain (1); Coiled coil (2); Frameshift (1); Initiator methionine (1); Modified residue (4); Sequence conflict (4) FUNCTION: Acts as component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN). The GARP complex is required for the maintenance of protein retrieval from endosomes to the TGN, acid hydrolase sorting, lysosome function, endosomal cholesterol traffic and autophagy. VPS51 participates in retrograde transport of acid hydrolase receptors, likely by promoting tethering and SNARE-dependent fusion of endosome-derived carriers to the TGN. Acts as component of the EARP complex that is involved in endocytic recycling. The EARP complex associates with Rab4-positive endosomes and promotes recycling of internalized transferrin receptor (TFRC) to the plasma membrane. {ECO:0000250|UniProtKB:Q9UID3}. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q9UID3}. Recycling endosome {ECO:0000250|UniProtKB:Q9UID3}. Note=Localizes to the trans-Golgi network as part of the GARP complex, while it localizes to recycling endosomes as part of the EARP complex. {ECO:0000250|UniProtKB:Q9UID3}. SUBUNIT: Component of the Golgi-associated retrograde protein (GARP) complex, also called VFT (VPS fifty-three) complex, composed of VPS51, VPS52, VPS53 and VPS54. Component of the endosome-associated retrograde protein (EARP) complex, composed of VPS51, VPS52, VPS53 and VPS50/Syndetin. EIPR1 interacts with both EARP and GARP complexes and mediates the recruitment of the GARP complex to the trans-Golgi network. Interacts with STX6. {ECO:0000250|UniProtKB:Q9UID3}. +Q8VCZ3 THAP7_MOUSE THAP domain-containing protein 7 309 34,593 Chain (1); Modified residue (2); Motif (1); Zinc finger (1) FUNCTION: Chromatin-associated, histone tail-binding protein that represses transcription via recruitment of HDAC3 and nuclear hormone receptor corepressors. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}. SUBUNIT: Interacts with HDAC3 and nuclear hormone receptor corepressors. {ECO:0000250}. +Q9JJD0 THA11_MOUSE THAP domain-containing protein 11 (Ronin) 305 33,276 Chain (1); Coiled coil (1); Compositional bias (3); Erroneous initiation (1); Motif (1); Zinc finger (1) FUNCTION: Transcriptional repressor that plays a central role for embryogenesis and the pluripotency of embryonic stem (ES) cells. Sequence-specific DNA-binding factor that represses gene expression in pluripotent ES cells by directly binding to key genetic loci and recruiting epigenetic modifiers. {ECO:0000269|PubMed:18585351}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18585351}. Cytoplasm {ECO:0000269|PubMed:18585351}. Note=May be regulated by shuttling of the protein between the cytoplasm and nucleus. SUBUNIT: Interacts (via coiled coil domain) with HCFC1. {ECO:0000269|PubMed:18585351}. TISSUE SPECIFICITY: Mainly restricted to pluripotent cells of the developing embryo, to oocytes, and to certain regions of the adult brain. {ECO:0000269|PubMed:18585351}. +P63058 THA_MOUSE Thyroid hormone receptor alpha (Nuclear receptor subfamily 1 group A member 1) (c-erbA-1) (c-erbA-alpha) 492 55,023 Alternative sequence (3); Binding site (2); Chain (1); DNA binding (1); Domain (1); Erroneous gene model prediction (1); Region (1); Sequence conflict (1); Zinc finger (2) FUNCTION: Nuclear hormone receptor that can act as a repressor or activator of transcription. High affinity receptor for thyroid hormones, including triiodothyronine and thyroxine. Isoform Alpha-deltaE6 does not bind DNA, inhibits the activity of isoform Alpha-1, and stimulates myoblast differentiation. {ECO:0000269|PubMed:16322094}. SUBCELLULAR LOCATION: Nucleus.; SUBCELLULAR LOCATION: Isoform Alpha-deltaE6: Cytoplasm. Note=Sequesters isoform Alpha-1 into this compartment. SUBUNIT: Binds DNA as a dimer; homodimer and heterodimer with RXRB. Interacts with NCOA3 and NCOA6 coactivators, leading to a strong increase of transcription of target genes. Probably interacts with SFPQ. Interacts with AKAP13. Interacts with C1D. Interacts with TP53INP2. Interacts with PER2. {ECO:0000269|PubMed:10681503, ECO:0000269|PubMed:20159955, ECO:0000269|PubMed:9405624}. DOMAIN: Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain. Isoform Alpha-deltaE6 lacks the hinge region that connects the modulating domain and the DNA binding domain. TISSUE SPECIFICITY: Ubiquitous (Isoform Alpha-deltaE6). {ECO:0000269|PubMed:16322094}. +Q3UUI3 THEM4_MOUSE Acyl-coenzyme A thioesterase THEM4 (Acyl-CoA thioesterase THEM4) (EC 3.1.2.2) (Carboxyl-terminal modulator protein) (Thioesterase superfamily member 4) 230 26,031 Active site (1); Binding site (1); Chain (1); Modified residue (8); Region (1); Sequence caution (3); Sequence conflict (2); Transit peptide (1) FUNCTION: Has acyl-CoA thioesterase activity towards medium and long-chain (C14 to C18) fatty acyl-CoA substrates, and probably plays an role in mitochondrial fatty acid metabolism. Plays a role in the apoptotic process, possibly via its regulation of AKT1 activity (By similarity). {ECO:0000250|UniProtKB:Q5T1C6, ECO:0000269|PubMed:19421406}. PTM: Phosphorylated. {ECO:0000250|UniProtKB:Q5T1C6}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q5T1C6}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q5T1C6}. Cytoplasm {ECO:0000250|UniProtKB:Q5T1C6}. Mitochondrion {ECO:0000269|PubMed:19421406}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q5T1C6}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q5T1C6}. Mitochondrion intermembrane space {ECO:0000250|UniProtKB:Q5T1C6}. Note=Released from the mitochondria into the cytosol in response to apoptotic stimuli. {ECO:0000250|UniProtKB:Q5T1C6}. SUBUNIT: Homodimer and homotetramer (By similarity). Interacts with AKT1 in the cytosol. Interacts with V-AKT from AKT8 murine leukemia virus. {ECO:0000250|UniProtKB:Q5T1C6, ECO:0000269|PubMed:11598301}. +O88286 WIZ_MOUSE Protein Wiz (Widely-interspaced zinc finger-containing protein) 1684 184,291 Alternative sequence (6); Chain (1); Compositional bias (5); Cross-link (28); Modified residue (20); Mutagenesis (2); Region (2); Sequence conflict (10); Zinc finger (10) FUNCTION: May link EHMT1 and EHMT2 histone methyltransferases to the CTBP corepressor machinery. May be involved in EHMT1-EHMT2 heterodimer formation and stabilization. {ECO:0000269|PubMed:16702210}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16702210}. SUBUNIT: Part of a complex containing at least CDYL, REST, WIZ, SETB1, EHMT1 and EHMT2 (By similarity). Interacts with EHMT1, EHMT2, CTBP1 and CTBP2. {ECO:0000250, ECO:0000269|PubMed:16702210}. DOMAIN: The C2H2-type zinc finger 10 mediates interaction with EHMT1 and EHMT2. TISSUE SPECIFICITY: According to PubMed:9795207, isoform L and isoform S are brain-specific. According to PubMed:16702210, isoform S is ubiquitously expressed. {ECO:0000269|PubMed:16702210, ECO:0000269|PubMed:9795207}. +Q6DID7 WLS_MOUSE Protein wntless homolog (Integral membrane protein GPR177) (Protein evenness interrupted homolog) (EVI) 541 62,188 Alternative sequence (1); Chain (1); Erroneous initiation (5); Region (1); Sequence conflict (2); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 233 253 Helical; Name=1. {ECO:0000255}.; TRANSMEM 269 289 Helical; Name=2. {ECO:0000255}.; TRANSMEM 304 324 Helical; Name=3. {ECO:0000255}.; TRANSMEM 332 352 Helical; Name=4. {ECO:0000255}.; TRANSMEM 381 401 Helical; Name=5. {ECO:0000255}.; TRANSMEM 432 452 Helical; Name=6. {ECO:0000255}.; TRANSMEM 472 492 Helical; Name=7. {ECO:0000255}. TOPO_DOM 43 232 Lumenal. {ECO:0000255}.; TOPO_DOM 254 268 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 290 303 Lumenal. {ECO:0000255}.; TOPO_DOM 325 331 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 353 380 Lumenal. {ECO:0000255}.; TOPO_DOM 402 431 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 453 471 Lumenal. {ECO:0000255}.; TOPO_DOM 493 541 Cytoplasmic. {ECO:0000255}. FUNCTION: Regulates Wnt proteins sorting and secretion in a feedback regulatory mechanism. This reciprocal interaction plays a key role in the regulation of expression, subcellular location, binding and organelle-specific association of Wnt proteins. Plays also an important role in establishment of the anterior-posterior body axis formation during development. {ECO:0000269|PubMed:19841259}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:19841259}; Multi-pass membrane protein {ECO:0000269|PubMed:19841259}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:19841259}; Multi-pass membrane protein {ECO:0000269|PubMed:19841259}. Cell membrane {ECO:0000250|UniProtKB:Q5T9L3}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q5T9L3}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q5T9L3}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:Q5T9L3}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Interacts with WNT3A (By similarity). Interacts with WNT1, WNT3 and WNT5. {ECO:0000250, ECO:0000269|PubMed:19841259}. TISSUE SPECIFICITY: Expressed in kidney, lung, skin, intestine, brain, spinal cord, skeleton, eyes, excretion glands, tooth and palatal shelves. {ECO:0000269|PubMed:19841259}. +P48614 WN10B_MOUSE Protein Wnt-10b (Protein Wnt-12) 389 43,119 Alternative sequence (1); Chain (1); Disulfide bond (11); Glycosylation (2); Lipidation (1); Modified residue (1); Signal peptide (1) FUNCTION: Member of the Wnt ligand gene family that encodes for secreted proteins, which activate the Wnt signaling cascade. Specifically activates canonical Wnt/beta-catenin signaling and thus triggers beta-catenin/LEF/TCF-mediated transcriptional programs. Involved in signaling networks controlling stemness, pluripotency and cell fate decisions. Acts in the immune system, mammary gland, adipose tissue, bone and skin. {ECO:0000305|PubMed:21447090}. PTM: Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition. {ECO:0000250|UniProtKB:P27467, ECO:0000250|UniProtKB:P56704}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:O00744}. Secreted {ECO:0000250|UniProtKB:O00744}. SUBUNIT: Forms a soluble 1:1 complex with AFM; this prevents oligomerization and is required for prolonged biological activity. The complex with AFM may represent the physiological form in body fluids. {ECO:0000250|UniProtKB:O00744}. TISSUE SPECIFICITY: Expressed in embryos and in the mammary gland of non-pregnant mice. +P83741 WNK1_MOUSE Serine/threonine-protein kinase WNK1 (EC 2.7.11.1) (Protein kinase lysine-deficient 1) (Protein kinase with no lysine 1) 2377 250,934 Active site (1); Alternative sequence (9); Binding site (2); Chain (1); Domain (1); Erroneous gene model prediction (1); Erroneous initiation (1); Modified residue (17); Mutagenesis (1); Nucleotide binding (1); Region (1); Sequence caution (2); Sequence conflict (2) FUNCTION: Serine/threonine kinase which plays an important role in the regulation of electrolyte homeostasis, cell signaling, survival, and proliferation. Acts as an activator and inhibitor of sodium-coupled chloride cotransporters and potassium-coupled chloride cotransporters respectively. Activates SCNN1A, SCNN1B, SCNN1D and SGK1. Controls sodium and chloride ion transport by inhibiting the activity of WNK4, by either phosphorylating the kinase or via an interaction between WNK4 and the autoinhibitory domain of WNK1. WNK4 regulates the activity of the thiazide-sensitive Na-Cl cotransporter, SLC12A3, by phosphorylation. WNK1 may also play a role in actin cytoskeletal reorganization. Phosphorylates NEDD4L. Acts as a scaffold to inhibit SLC4A4, SLC26A6 as well as CFTR activities and surface expression, recruits STK39 which mediates the inhibition (PubMed:21317537, PubMed:23542070). {ECO:0000269|PubMed:12671053, ECO:0000269|PubMed:21317537, ECO:0000269|PubMed:23542070}.; FUNCTION: Isoform 7: Dominant-negative regulator of the longer isoform 1. Does not have kinase activity, does not directly inhibit WNK4 and has no direct effect on sodium and chloride ion transport. Downregulates sodium-chloride cotransporter activity indirectly by inhibiting isoform 1, it associates with isoform 1 and attenuates its kinase activity. In kidney, may play an important role regulating sodium and potassium balance. {ECO:0000250|UniProtKB:Q9JIH7}. PTM: Autophosphorylation at Ser-382 is inhibited by intracellular calcium. {ECO:0000250|UniProtKB:Q9JIH7}.; PTM: Ubiquitinated in vitro by the BCR(KLHL3) complex and in vivo by a BCR(KLHL2) complex, leading to proteasomal degradation. {ECO:0000250|UniProtKB:Q9H4A3}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11498583}. SUBUNIT: Interacts with SYT2. Interacts with KLHL3, WNK3 and WNK4 (By similarity). Isoform 7: Interacts with isoform 1 (By similarity). {ECO:0000250|UniProtKB:Q9H4A3, ECO:0000250|UniProtKB:Q9JIH7}. TISSUE SPECIFICITY: Widely expressed in both adult and embryonic tissue, with highest levels observed in the testis and lower levels in heart, lung, kidney, placenta, brain and skeletal muscle. Expressed in pancreatic duct (PubMed:21317537). Two isoforms are expressed in heart, a single shorter isoform in the kidney. Locates to the distal convoluted tubule, the medullary collecting duct and the cortical collecting duct of the kidney. HSN2-containing isoform 2 and isoform 3 are restricted to the nervous system, expressed preferentially in sensory neurons than in motor neurons and in general more abundant in axons than in cell bodies (at protein level). In the DRG, predominantly expressed in the satellite cells that envelop sensory neurons, but low expression also observed in the cell bodies of neurons (at protein level). In the sciatic nerve, expressed in the Schwann cells that surround axons and in a mosaic distribution of axons (at protein level). In the spinal cord, expressed in superficial layers (LI and LII), as well as in the fibers of the Lissauer tract (at protein level). Also detected in the axon fibers of dorsolateral funiculus and lateral funiculus (at protein level). {ECO:0000269|PubMed:11498583, ECO:0000269|PubMed:14514722, ECO:0000269|PubMed:18521183, ECO:0000269|PubMed:21317537}. +O35144 TERF2_MOUSE Telomeric repeat-binding factor 2 (TTAGGG repeat-binding factor 2) (Telomeric DNA-binding protein) 541 60,263 Alternative sequence (1); Chain (1); Compositional bias (1); Cross-link (6); DNA binding (1); Domain (1); Erroneous initiation (2); Modified residue (6); Motif (1); Mutagenesis (2); Region (1); Sequence conflict (4) FUNCTION: Binds the telomeric double-stranded 5'-TTAGGG-3' repeat and plays a central role in telomere maintenance and protection against end-to-end fusion of chromosomes. In addition to its telomeric DNA-binding role, required to recruit a number of factors and enzymes required for telomere protection, including the shelterin complex, TERF2IP/RAP1 and DCLRE1B/Apollo. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded 5'-TTAGGG-3' repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways. Together with DCLRE1B/Apollo, plays a key role in telomeric loop (T loop) formation by generating 3' single-stranded overhang at the leading end telomeres: T loops have been proposed to protect chromosome ends from degradation and repair. Required both to recruit DCLRE1B/Apollo to telomeres and activate the exonuclease activity of DCLRE1B/Apollo. Preferentially binds to positive supercoiled DNA. Together with DCLRE1B/Apollo, required to control the amount of DNA topoisomerase (TOP1, TOP2A and TOP2B) needed for telomere replication during fork passage and prevent aberrant telomere topology. Recruits TERF2IP/RAP1 to telomeres, thereby participating in to repressing homology-directed repair (HDR), which can affect telomere length. {ECO:0000269|PubMed:20339076, ECO:0000269|PubMed:20619712, ECO:0000269|PubMed:20622870}. PTM: Phosphorylated upon DNA damage, most probably by ATM. Phosphorylated TERF2 is not bound to telomeric DNA, and rapidly localizes to damage sites (By similarity). {ECO:0000250}.; PTM: Methylated by PRMT1 at multiple arginines within the N-terminal Arg-rich region. Methylation may control association with telomeres (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:20339076}. Chromosome, telomere {ECO:0000269|PubMed:20339076}. Note=Colocalizes with telomeric DNA in interphase cells and is located at chromosome ends during metaphase. SUBUNIT: Homodimer. Component of the shelterin complex (telosome) composed of TERF1, TERF2, TINF2, TERF2IP/RAP1, ACD and POT1. Interacts with TERF2IP. Interacts with NBN. Interacts with SLX4/BTBD12. Interacts with DCLRE1B/Apollo; the interaction is direct (By similarity). Interacts with TERF2IP/RAP1; the interaction is direct. {ECO:0000250, ECO:0000269|PubMed:20339076, ECO:0000269|PubMed:20619712, ECO:0000269|PubMed:20622870}. DOMAIN: The TRFH dimerization region mediates the interaction with DCLRE1B/Apollo but not TINF2. {ECO:0000250}.; DOMAIN: The HTH domain is an independent structural unit and mediates binding to telomeric DNA. {ECO:0000250}. +Q8VD76 TF2H3_MOUSE General transcription factor IIH subunit 3 (Basic transcription factor 2 34 kDa subunit) (BTF2 p34) (General transcription factor IIH polypeptide 3) (TFIIH basal transcription factor complex p34 subunit) 309 34,244 Chain (1); Zinc finger (1) FUNCTION: Component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module CAK controls the initiation of transcription. {ECO:0000250|UniProtKB:Q13889}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13889}. SUBUNIT: Part of a TFIID-containing RNA polymerase II pre-initiation complex that is composed of TBP and at least GTF2A1, GTF2A2, GTF2E1, GTF2E2, GTF2F1, GTF2H2, GTF2H3, GTF2H4, GTF2H5, GTF2B, TCEA1, ERCC2, ERCC3, TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13. Component of the 7-subunit TFIIH core complex composed of XPB/ERCC3, XPD/ERCC2, GTF2H1, GTF2H2, GTF2H3, GTF2H4 and GTF2H5, which is active in NER. The core complex associates with the 3-subunit CDK-activating kinase (CAK) module composed of CCNH/cyclin H, CDK7 and MNAT1 to form the 10-subunit holoenzyme (holo-TFIIH) active in transcription (By similarity). Interacts with RARA; the interaction requires prior phosphorylation of RARA on 'Ser-369' which then enhances interaction of RARA with CDK7 (PubMed:9230306). {ECO:0000250|UniProtKB:Q13889, ECO:0000269|PubMed:9230306}. +Q8R307 VPS18_MOUSE Vacuolar protein sorting-associated protein 18 homolog 973 110,219 Chain (1); Coiled coil (2); Initiator methionine (1); Modified residue (7); Repeat (1); Sequence conflict (2); Zinc finger (1) FUNCTION: Plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport and autophagic pathways. Believed to act as a core component of the putative HOPS and CORVET endosomal tethering complexes which are proposed to be involved in the Rab5-to-Rab7 endosome conversion probably implicating MON1A/B, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion. The HOPS complex is proposed to be recruited to Rab7 on the late endosomal membrane and to regulate late endocytic, phagocytic and autophagic traffic towards lysosomes. The CORVET complex is proposed to function as a Rab5 effector to mediate early endosome fusion probably in specific endosome subpopulations (By similarity). Required for fusion of endosomes and autophagosomes with lysosomes (PubMed:14517315, PubMed:22854957). Involved in dendrite development of Pukinje cells (PubMed:22699122). {ECO:0000250|UniProtKB:Q9P253, ECO:0000269|PubMed:14517315, ECO:0000269|PubMed:22699122, ECO:0000269|PubMed:22854957}. SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250|UniProtKB:Q9P253}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9P253}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9P253}. Lysosome membrane {ECO:0000250|UniProtKB:Q9P253}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9P253}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9P253}. Early endosome {ECO:0000250|UniProtKB:Q9P253}. Cytoplasmic vesicle, autophagosome {ECO:0000305}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000305}. Note=Cytoplasmic, peripheral membrane protein associated with early endosomes and late endosomes/lysosomes. SUBUNIT: Core component of at least two putative endosomal tethering complexes, the homotypic fusion and vacuole protein sorting (HOPS) complex and the class C core vacuole/endosome tethering (CORVET) complex. Their common core is composed of the class C Vps proteins VPS11, VPS16, VPS18 and VPS33A, which in HOPS further associates with VPS39 and VPS41 and in CORVET with VPS8 and TGFBRAP1. Interacts with RAB5C (PubMed:25266290). Interacts with HOOK1 (PubMed:14668490). Interacts with STX7, MON1B (By similarity). Associates with adaptor protein complex 3 (AP-3) and clathrin:AP-3 complexes (PubMed:21411634). Interacts with SYNPO2 (By similarity). {ECO:0000250|UniProtKB:Q9P253, ECO:0000269|PubMed:14668490, ECO:0000269|PubMed:21411634, ECO:0000269|PubMed:25266290}. +Q9Z1J1 TF7L1_MOUSE Transcription factor 7-like 1 (HMG box transcription factor 3) (TCF-3) (mTCF-3) 584 62,298 Chain (1); Compositional bias (2); DNA binding (1); Motif (1); Mutagenesis (2); Region (1); Sequence conflict (6) FUNCTION: Participates in the Wnt signaling pathway. Binds to DNA and acts as a repressor in the absence of CTNNB1, and as an activator in its presence. Necessary for the terminal differentiation of epidermal cells, the formation of keratohyalin granules and the development of the barrier function of the epidermis. {ECO:0000269|PubMed:11445543}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Binds the armadillo repeat of CTNNB1 and forms a stable complex. DOMAIN: The putative Groucho interaction domain between the N-terminal CTNNB1 binding domain and the HMG-box is necessary for repression of the transactivation mediated by TCF7L1 and CTNNB1. TISSUE SPECIFICITY: Detected in the basal layer of epidermis and in outer root sheath and bulge of hair follicles. {ECO:0000269|PubMed:10498690}. +P15806 TFE2_MOUSE Transcription factor E2-alpha (Immunoglobulin enhancer-binding factor E12/E47) (Transcription factor 3) (TCF-3) (Transcription factor A1) 651 67,701 Alternative sequence (1); Chain (1); Cross-link (2); Domain (1); Helix (2); Modified residue (9); Natural variant (1); Region (1); Sequence conflict (5) FUNCTION: Transcriptional regulator. Involved in the initiation of neuronal differentiation. Heterodimers between TCF3 and tissue-specific basic helix-loop-helix (bHLH) proteins play major roles in determining tissue-specific cell fate during embryogenesis, like muscle or early B-cell differentiation. Dimers bind DNA on E-box motifs: 5'-CANNTG-3'. Binds to the kappa-E2 site in the kappa immunoglobulin gene enhancer. Binds to IEB1 and IEB2, which are short DNA sequences in the insulin gene transcription control region. {ECO:0000269|PubMed:18214987}. PTM: Phosphorylated following NGF stimulation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Forms a heterodimer with TWIST2. Forms a heterodimer with NEUROD1; the heterodimer is inhibited in presence of ID2, but not NR0B2, to E-box element. Isoform E12 interacts with RALGAPA1 and FIGLA. Interacts with EP300. Efficient DNA binding requires dimerization with another bHLH protein (By similarity). Homodimer. Heterodimer. Forms a heterodimer with MYOG; heterodimerization enhances MYOG DNA-binding and transcriptional activities. Interacts with PTF1A, TGFB1I1 and UBE2I. Component of a nuclear TAL-1 complex composed at least of CBFA2T3, LDB1, TAL1 and TCF3. Interacts with NEUROD2. Interacts with BHLHA9. Forms a heterodimer with ATOH8; repress transcription of TCF3 and TCF3/NEUROG3 dimer-induced transactivation of E box-dependent promoters. {ECO:0000250|UniProtKB:P15923, ECO:0000269|PubMed:11318877, ECO:0000269|PubMed:12196028, ECO:0000269|PubMed:12200424, ECO:0000269|PubMed:16291758, ECO:0000269|PubMed:16407974, ECO:0000269|PubMed:18069799, ECO:0000269|PubMed:18214987, ECO:0000269|PubMed:23938248, ECO:0000269|PubMed:7589808, ECO:0000269|PubMed:9409784}. +Q6A070 TGRM1_MOUSE TOG array regulator of axonemal microtubules protein 1 (Crescerin-1) (Protein FAM179B) 1776 194,910 Alternative sequence (1); Chain (1); Compositional bias (1); Helix (19); Mutagenesis (3); Region (4); Repeat (13); Turn (1) FUNCTION: Required for normal structure and function of primary cilia. Plays a role in the organization of axoneme microtubule bundles in primary cilia (By similarity). Interacts with microtubules and promotes microtubule polymerization via its HEAT repeat domains, especially those in TOG region 2 and 4 (PubMed:26378256). {ECO:0000250|UniProtKB:Q17423, ECO:0000269|PubMed:26378256}. SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000269|PubMed:26378256}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:26378256}. Note=Detected along the length of primary cilia and at the basal body. Colocalization with the cytoplasmic microtubule cytoskeleton upon heterologous expression is most likely an artifact. {ECO:0000269|PubMed:26378256}. DOMAIN: The TOG regions are composed of HEAT-type repeats that assemble into a solenoid structure. They mediate interaction with microtubules. {ECO:0000269|PubMed:26378256}. +Q8CAY6 THIC_MOUSE Acetyl-CoA acetyltransferase, cytosolic (EC 2.3.1.9) (Cytosolic acetoacetyl-CoA thiolase) 397 41,298 Active site (3); Chain (1); Erroneous initiation (1); Modified residue (4); Sequence conflict (9) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homotetramer. {ECO:0000250}. +Q9WUA1 WIF1_MOUSE Wnt inhibitory factor 1 (WIF-1) 379 41,590 Chain (1); Disulfide bond (15); Domain (6); Glycosylation (2); Signal peptide (1) FUNCTION: Binds to WNT proteins and inhibits their activities. May be involved in mesoderm segmentation. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Interacts with MYOC. {ECO:0000250}. TISSUE SPECIFICITY: Expression highest in heart and lung. Lower in brain and eye. +Q9Z0G4 WISP2_MOUSE WNT1-inducible-signaling pathway protein 2 (WISP-2) (CCN family member 5) (Connective tissue growth factor-like protein) (CTGF-L) 251 27,095 Chain (1); Domain (3); Glycosylation (1); Sequence conflict (3); Signal peptide (1) FUNCTION: May play an important role in modulating bone turnover. Promotes the adhesion of osteoblast cells and inhibits the binding of fibrinogen to integrin receptors. In addition, inhibits osteocalcin production (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +O88978 TILB_MOUSE Protein tilB homolog (Leucine-rich repeat-containing protein 6) (Leucine-rich testis-specific protein) (Testis-specific leucine-rich repeat protein) 473 55,049 Chain (1); Coiled coil (1); Compositional bias (1); Domain (2); Repeat (4); Sequence conflict (4) FUNCTION: May play a role in dynein arm assembly, hence essential for proper axoneme building for cilia motility. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10775177}. Cell projection, cilium {ECO:0000250}. SUBUNIT: Interacts (via CS domain) with ZMYND10 (via C-terminus). {ECO:0000250|UniProtKB:Q86X45}. TISSUE SPECIFICITY: Testis-specific (at protein level). Expressed in testis. Abundant expression in late prophase of meiosis I with a dramatic decrease after the first meiotic division. {ECO:0000269|PubMed:10775177}. +Q8BUY5 TIDC1_MOUSE Complex I assembly factor TIMMDC1, mitochondrial (Translocase of inner mitochondrial membrane domain-containing protein 1) (TIMM domain containing-protein 1) 285 31,791 Chain (1); Modified residue (1); Sequence conflict (4); Transmembrane (4) TRANSMEM 80 100 Helical. {ECO:0000255}.; TRANSMEM 137 159 Helical. {ECO:0000255}.; TRANSMEM 165 185 Helical. {ECO:0000255}.; TRANSMEM 188 208 Helical. {ECO:0000255}. FUNCTION: Chaperone protein involved in the assembly of the mitochondrial NADH:ubiquinone oxidoreductase complex (complex I). Participates in constructing the membrane arm of complex I (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Associates with the intermediate 315 kDa subcomplex of incompletely assembled complex I. {ECO:0000250}. +Q99N14 TKN4_MOUSE Tachykinin-4 (Preprotachykinin-C) (PPT-C) [Cleaved into: Hemokinin (HK1) (Hemokinin-1) (Hemokinin-I) (HK-I)] 128 13,937 Modified residue (1); Peptide (1); Propeptide (2); Signal peptide (1) FUNCTION: Tachykinins are active peptides which excite neurons, evoke behavioral responses, are potent vasodilators and secretagogues, and contract (directly or indirectly) many smooth muscles. Hemokinin induces plasma extravasation, mast cell degranulation, muscle contraction, salivary secretion and scratching behavior. Increases sperm motility. Induces potent analgesic effects and may play a role in pain modulation. Promotes survival of bone marrow B lineage cells and of cultured LPS-stimulated pre-B cells and may act as an autocrine factor required for B-cell survival and proliferation. Lowers systemic arterial pressure following intravenous injection. Induces interferon-gamma production and may play a role in the inflammatory response. Shows potent affinity and specificity for the NK-1 receptor. {ECO:0000269|PubMed:11062498, ECO:0000269|PubMed:11725292, ECO:0000269|PubMed:11786503, ECO:0000269|PubMed:12044836, ECO:0000269|PubMed:12842130, ECO:0000269|PubMed:15153465, ECO:0000269|PubMed:16102736, ECO:0000269|PubMed:17628523}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Expressed in hematopoietic cells with highest levels in pre- and pro-B cells but not in later developmental stages. Also detected in uterus, skeletal muscle, brain, spleen, stomach, skin and lactating mammary gland and in cells of myeloid lineage including dendritic and microglial cells and macrophages. In uterus, highest expression is observed in non-pregnant diestrus mice and in day 5 pregnant mice. Compared with mice in diestrus, decreases 2.6-fold in uteri from non-pregnant mice in estrus and 10.2-fold in day 17 pregnant mice. Detected at sites of chronic inflammation such as granulomas. {ECO:0000269|PubMed:11062498, ECO:0000269|PubMed:12383518, ECO:0000269|PubMed:12716968, ECO:0000269|PubMed:12842130, ECO:0000269|PubMed:15153465, ECO:0000269|PubMed:15342200, ECO:0000269|PubMed:15647454}. +Q02858 TIE2_MOUSE Angiopoietin-1 receptor (EC 2.7.10.1) (Endothelial tyrosine kinase) (HYK) (STK1) (Tunica interna endothelial cell kinase) (Tyrosine kinase with Ig and EGF homology domains-2) (Tyrosine-protein kinase receptor TEK) (Tyrosine-protein kinase receptor TIE-2) (mTIE2) (p140 TEK) (CD antigen CD202b) 1122 125,701 Active site (1); Binding site (1); Chain (1); Disulfide bond (14); Domain (9); Glycosylation (9); Modified residue (4); Mutagenesis (3); Nucleotide binding (1); Sequence conflict (10); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 747 767 Helical. {ECO:0000255}. TOPO_DOM 23 746 Extracellular. {ECO:0000255}.; TOPO_DOM 768 1122 Cytoplasmic. {ECO:0000255}. FUNCTION: Tyrosine-protein kinase that acts as cell-surface receptor for ANGPT1, ANGPT2 and ANGPT4 and regulates angiogenesis, endothelial cell survival, proliferation, migration, adhesion and cell spreading, reorganization of the actin cytoskeleton, but also maintenance of vascular quiescence. Has anti-inflammatory effects by preventing the leakage of proinflammatory plasma proteins and leukocytes from blood vessels. Required for normal angiogenesis and heart development during embryogenesis. Required for post-natal hematopoiesis. After birth, activates or inhibits angiogenesis, depending on the context. Inhibits angiogenesis and promotes vascular stability in quiescent vessels, where endothelial cells have tight contacts. In quiescent vessels, ANGPT1 oligomers recruit TEK to cell-cell contacts, forming complexes with TEK molecules from adjoining cells, and this leads to preferential activation of phosphatidylinositol 3-kinase and the AKT1 signaling cascades. In migrating endothelial cells that lack cell-cell adhesions, ANGT1 recruits TEK to contacts with the extracellular matrix, leading to the formation of focal adhesion complexes, activation of PTK2/FAK and of the downstream kinases MAPK1/ERK2 and MAPK3/ERK1, and ultimately to the stimulation of sprouting angiogenesis. ANGPT1 signaling triggers receptor dimerization and autophosphorylation at specific tyrosine residues that then serve as binding sites for scaffold proteins and effectors. Signaling is modulated by ANGPT2 that has lower affinity for TEK, can promote TEK autophosphorylation in the absence of ANGPT1, but inhibits ANGPT1-mediated signaling by competing for the same binding site. Signaling is also modulated by formation of heterodimers with TIE1, and by proteolytic processing that gives rise to a soluble TEK extracellular domain. The soluble extracellular domain modulates signaling by functioning as decoy receptor for angiopoietins. TEK phosphorylates DOK2, GRB7, GRB14, PIK3R1, SHC1 and TIE1. {ECO:0000269|PubMed:10521483, ECO:0000269|PubMed:12665569, ECO:0000269|PubMed:15284220, ECO:0000269|PubMed:20973951, ECO:0000269|PubMed:7596437, ECO:0000269|PubMed:7958865, ECO:0000269|PubMed:9632797}. PTM: Proteolytic processing leads to the shedding of the extracellular domain (soluble TIE-2 alias sTIE-2). {ECO:0000250}.; PTM: Autophosphorylated on tyrosine residues in response to ligand binding. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Autophosphorylation occurs in a sequential manner, where Tyr-990 in the kinase activation loop is phosphorylated first, followed by autophosphorylation at Tyr-1106 and at additional tyrosine residues. ANGPT1-induced phosphorylation is impaired during hypoxia, due to increased expression of ANGPT2 (By similarity). Phosphorylation is important for interaction with GRB14, PIK3R1 and PTPN11. Phosphorylation at Tyr-1100 is important for interaction with GRB2 and GRB7. Phosphorylation at Tyr-1106 is important for interaction with DOK2 and for coupling to downstream signal transduction pathways in endothelial cells. Dephosphorylated by PTPRB. {ECO:0000250, ECO:0000269|PubMed:10557082, ECO:0000269|PubMed:12665569}.; PTM: Ubiquitinated. The phosphorylated receptor is ubiquitinated and internalized, leading to its degradation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Cell junction {ECO:0000250}. Cell junction, focal adhesion {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Secreted {ECO:0000250}. Note=Recruited to cell-cell contacts in quiescent endothelial cells. Colocalizes with the actin cytoskeleton and at actin stress fibers during cell spreading. Recruited to the lower surface of migrating cells, especially the rear end of the cell. Proteolytic processing gives rise to a soluble extracellular domain that is secreted (By similarity). {ECO:0000250}. SUBUNIT: Homodimer. Heterodimer with TIE1. Interacts with ANGPT1, ANGPT2 and ANGPT4. At cell-cell contacts in quiescent cells, forms a signaling complex composed of ANGPT1 plus TEK molecules from two adjoining cells. In the absence of endothelial cell-cell contacts, interaction with ANGPT1 mediates contacts with the extracellular matrix. Interacts (tyrosine phosphorylated) with TNIP2. Interacts (tyrosine phosphorylated) with SHC1 (via SH2 domain) (By similarity). Interacts with PTPRB; this promotes endothelial cell-cell adhesion. Interacts with DOK2, GRB2, GRB7, GRB14, PIK3R1 and PTPN11/SHP2. Colocalizes with DOK2 at contacts with the extracellular matrix in migrating cells. {ECO:0000250, ECO:0000269|PubMed:10521483, ECO:0000269|PubMed:12427764, ECO:0000269|PubMed:12665569, ECO:0000269|PubMed:15284220, ECO:0000269|PubMed:19451274, ECO:0000269|PubMed:20973951, ECO:0000269|PubMed:9632797}. DOMAIN: The soluble extracellular domain is functionally active in angiopoietin binding and can modulate the activity of the membrane-bound form by competing for angiopoietins. {ECO:0000250}. TISSUE SPECIFICITY: Specifically expressed in developing vascular endothelial cells. Abundantly expressed in lung and heart, moderately in brain, liver and kidney, and weakly in thymus, spleen and testis. {ECO:0000269|PubMed:8395828}. +Q64127 TIF1A_MOUSE Transcription intermediary factor 1-alpha (TIF1-alpha) (EC 2.3.2.27) (E3 ubiquitin-protein ligase Trim24) (RING-type E3 ubiquitin transferase TIF1-alpha) (Tripartite motif-containing protein 24) 1051 116,657 Alternative sequence (1); Chain (1); Coiled coil (1); Compositional bias (4); Cross-link (20); Domain (1); Modified residue (14); Motif (1); Mutagenesis (2); Region (2); Site (2); Zinc finger (4) Protein modification; protein ubiquitination. FUNCTION: Transcriptional coactivator that interacts with numerous nuclear receptors and coactivators and modulates the transcription of target genes. Interacts with chromatin depending on histone H3 modifications, having the highest affinity for histone H3 that is both unmodified at 'Lys-4' (H3K4me0) and acetylated at 'Lys-23' (H3K23ac) (By similarity). Has E3 protein-ubiquitin ligase activity. Promotes ubiquitination and proteasomal degradation of p53/TP53. Plays a role in the regulation of cell proliferation and apoptosis via its effects on p53/TP53 levels. Up-regulates ligand-dependent transcription activation by AR, GCR/NR3C1, thyroid hormone receptor (TR) and ESR1. Modulates transcription activation by retinoic acid (RA) receptors, such as RARA. Plays a role in regulating retinoic acid-dependent proliferation of hepatocytes. Required for normal transition from proliferating neonatal hepatocytes to quiescent adult hepatocytes. {ECO:0000250, ECO:0000269|PubMed:10610177, ECO:0000269|PubMed:16322096, ECO:0000269|PubMed:16880268, ECO:0000269|PubMed:18026104, ECO:0000269|PubMed:19556538, ECO:0000269|PubMed:19909775, ECO:0000269|PubMed:7744009}. PTM: Sumoylated. {ECO:0000269|PubMed:11313457}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Detected in the cytoplasm of the zygote. Translocates into the pronucleus at the time of genome activation. Colocalizes with sites of active transcription. SUBUNIT: Interacts (via bromo domain) with histone H3 (via N-terminus), provided that it is not methylated at 'Lys-4' (H3K4me0). Does not interact with histone H3 that is methylated at 'Lys-4' (H3K4me1, H3K4me2 or H3K4me3). Interacts (via bromo domain) with histone H3 (via N-terminus) that is acetylated at 'Lys-23' (H3K23ac). Has the highest affinity for histone H3 that is both unmodified at 'Lys-4' (H3K4me0) and acetylated at 'Lys-23' (H3K23ac). Has very low affinity for histone H3 that is methylated at 'Lys-9' (H3K9me), or acetylated at both 'Lys-9' (H3K9ac) and 'Lys-14' (H3K14ac), or acetylated at 'Lys-27' (H3K27ac) (in vitro). Interacts with TRIM16. Interacts with NR3C2/MCR (By similarity). Interacts with the ligand-binding domain of estrogen receptors (in vitro). Interaction with DNA-bound estrogen receptors requires the presence of estradiol (By similarity). Interacts with AR, CARM1, KAT5/TIP60, NCOA2/GRIP1, BRD7, CBX1, CBX3 and CBX5. Part of a coactivator complex containing TRIM24, NCOA2/GRIP1 and CARM1. Interacts with p53/TP53 and PML. {ECO:0000250, ECO:0000269|PubMed:10610177, ECO:0000269|PubMed:11313457, ECO:0000269|PubMed:16322096, ECO:0000269|PubMed:19556538, ECO:0000269|PubMed:19909775, ECO:0000269|PubMed:7744009, ECO:0000269|PubMed:8978696}. TISSUE SPECIFICITY: Detected in embryonic and adult liver. Detected in zygote and throughout embryogenesis (at protein level). Detected in all adult tissues, with the highest expression level in testis. {ECO:0000269|PubMed:17412818, ECO:0000269|PubMed:18026104}. DISEASE: Note=A chromosomal aberration involving TRIM24 produces a TRIM24-BRAF (T18) oncogene originally isolated from a furfural-induced hepatoma. +Q5F285 TM256_MOUSE Transmembrane protein 256 113 11,656 Chain (1); Modified residue (1); Signal peptide (1); Topological domain (2); Transmembrane (2) TRANSMEM 64 84 Helical. {ECO:0000255}.; TRANSMEM 93 113 Helical. {ECO:0000255}. TOPO_DOM 30 63 Extracellular. {ECO:0000255}.; TOPO_DOM 85 92 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +A9JSM3 TM238_MOUSE Transmembrane protein 238 176 18,226 Chain (1); Compositional bias (1); Modified residue (1); Topological domain (3); Transmembrane (2) TRANSMEM 37 57 Helical. {ECO:0000255}.; TRANSMEM 70 90 Helical. {ECO:0000255}. TOPO_DOM 1 36 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 58 69 Extracellular. {ECO:0000255}.; TOPO_DOM 91 176 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9DA47 TM239_MOUSE Transmembrane protein 239 151 17,201 Chain (1); Compositional bias (2); Transmembrane (3) TRANSMEM 61 81 Helical. {ECO:0000255}.; TRANSMEM 85 105 Helical. {ECO:0000255}.; TRANSMEM 116 138 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8K071 TM221_MOUSE Transmembrane protein 221 230 23,954 Chain (1); Transmembrane (4) TRANSMEM 12 32 Helical. {ECO:0000255}.; TRANSMEM 73 93 Helical. {ECO:0000255}.; TRANSMEM 125 145 Helical. {ECO:0000255}.; TRANSMEM 147 167 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +P61166 TM258_MOUSE Transmembrane protein 258 (Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit TMEM258) (Oligosaccharyl transferase subunit TMEM258) 79 9,079 Chain (1); Modified residue (1); Transmembrane (2) TRANSMEM 17 37 Helical. {ECO:0000255}.; TRANSMEM 55 75 Helical. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. Involved in ER homeostasis in the colonic epithelium. {ECO:0000269|PubMed:27974209}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P61165}. SUBUNIT: Component of the oligosaccharyltransferase (OST) complex. OST exists in two different complex forms which contain common core subunits RPN1, RPN2, OST48, OST4, DAD1 and TMEM258, either STT3A or STT3B as catalytic subunits, and form-specific accessory subunits (Probable). STT3A complex assembly occurs through the formation of 3 subcomplexes. Subcomplex 1 contains RPN1 and TMEM258, subcomplex 2 contains the STT3A-specific subunits STT3A, DC2/OSTC, and KCP2 as well as the core subunit OST4, and subcomplex 3 contains RPN2, DAD1, and OST48. The STT3A complex can form stable complexes with the Sec61 complex or with both the Sec61 and TRAP complexes (By similarity). {ECO:0000250|UniProtKB:E2RKN8, ECO:0000305|PubMed:27974209}. +Q9CXT7 TM192_MOUSE Transmembrane protein 192 266 30,336 Alternative sequence (1); Chain (1); Modified residue (4); Sequence conflict (1); Topological domain (5); Transmembrane (4) TRANSMEM 47 67 Helical. {ECO:0000255}.; TRANSMEM 90 110 Helical. {ECO:0000255}.; TRANSMEM 138 158 Helical. {ECO:0000255}.; TRANSMEM 172 192 Helical. {ECO:0000255}. TOPO_DOM 1 46 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 68 89 Lumenal. {ECO:0000255}.; TOPO_DOM 111 137 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 159 171 Lumenal. {ECO:0000255}.; TOPO_DOM 193 266 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q8IY95}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8IY95}. Late endosome {ECO:0000250|UniProtKB:Q8IY95}. SUBUNIT: Homodimer. {ECO:0000250}. +B1AZA5 TM245_MOUSE Transmembrane protein 245 876 97,357 Chain (1); Glycosylation (4); Initiator methionine (1); Modified residue (10); Transmembrane (15) TRANSMEM 56 76 Helical. {ECO:0000255}.; TRANSMEM 115 135 Helical. {ECO:0000255}.; TRANSMEM 144 164 Helical. {ECO:0000255}.; TRANSMEM 181 201 Helical. {ECO:0000255}.; TRANSMEM 215 235 Helical. {ECO:0000255}.; TRANSMEM 237 257 Helical. {ECO:0000255}.; TRANSMEM 351 371 Helical. {ECO:0000255}.; TRANSMEM 377 397 Helical. {ECO:0000255}.; TRANSMEM 457 477 Helical. {ECO:0000255}.; TRANSMEM 623 643 Helical. {ECO:0000255}.; TRANSMEM 647 667 Helical. {ECO:0000255}.; TRANSMEM 728 748 Helical. {ECO:0000255}.; TRANSMEM 749 769 Helical. {ECO:0000255}.; TRANSMEM 773 793 Helical. {ECO:0000255}.; TRANSMEM 812 832 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9D075 TM10B_MOUSE tRNA methyltransferase 10 homolog B (EC 2.1.1.221) (RNA (guanine-9-)-methyltransferase domain-containing protein 3) (tRNA (guanine(9)-N(1))-methyltransferase TRMT10B) 318 36,377 Chain (1); Coiled coil (1); Domain (1); Erroneous gene model prediction (2); Sequence conflict (1) FUNCTION: S-adenosyl-L-methionine-dependent guanine N(1)-methyltransferase that catalyzes the formation of N(1)-methylguanine at position 9 (m1G9) in tRNAs. Probably not able to catalyze formation of N(1)-methyladenine at position 9 (m1A9) in tRNAs. {ECO:0000250|UniProtKB:Q6PF06}. +Q8R0J4 TM134_MOUSE Transmembrane protein 134 195 21,637 Alternative sequence (2); Chain (1); Modified residue (1); Sequence conflict (1); Topological domain (3); Transmembrane (2) TRANSMEM 123 143 Helical. {ECO:0000255}.; TRANSMEM 155 175 Helical. {ECO:0000255}. TOPO_DOM 1 122 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 144 154 Extracellular. {ECO:0000255}.; TOPO_DOM 176 195 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9H6X4}. +Q8BH18 TM117_MOUSE Transmembrane protein 117 514 60,356 Chain (1); Erroneous initiation (1); Glycosylation (2); Modified residue (1); Topological domain (9); Transmembrane (8) TRANSMEM 16 36 Helical. {ECO:0000255}.; TRANSMEM 66 86 Helical. {ECO:0000255}.; TRANSMEM 111 131 Helical. {ECO:0000255}.; TRANSMEM 155 175 Helical. {ECO:0000255}.; TRANSMEM 199 219 Helical. {ECO:0000255}.; TRANSMEM 240 260 Helical. {ECO:0000255}.; TRANSMEM 296 316 Helical. {ECO:0000255}.; TRANSMEM 395 415 Helical. {ECO:0000255}. TOPO_DOM 1 15 Cytoplasmic. {ECO:0000250|UniProtKB:Q9H0C3}.; TOPO_DOM 37 65 Extracellular. {ECO:0000250|UniProtKB:Q9H0C3}.; TOPO_DOM 87 110 Cytoplasmic. {ECO:0000250|UniProtKB:Q9H0C3}.; TOPO_DOM 132 154 Extracellular. {ECO:0000250|UniProtKB:Q9H0C3}.; TOPO_DOM 176 198 Cytoplasmic. {ECO:0000250|UniProtKB:Q9H0C3}.; TOPO_DOM 220 239 Extracellular. {ECO:0000250|UniProtKB:Q9H0C3}.; TOPO_DOM 261 295 Cytoplasmic. {ECO:0000250|UniProtKB:Q9H0C3}.; TOPO_DOM 317 394 Extracellular. {ECO:0000250|UniProtKB:Q9H0C3}.; TOPO_DOM 416 514 Cytoplasmic. {ECO:0000250|UniProtKB:Q9H0C3}. FUNCTION: Involved in endoplasmic reticulum (ER) stress-induced cell death pathway. {ECO:0000250|UniProtKB:Q9H0C3}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9H0C3}; Multi-pass membrane protein {ECO:0000255}. +Q8R235 TM203_MOUSE Transmembrane protein 203 136 15,776 Chain (1); Sequence conflict (1); Transmembrane (4) TRANSMEM 14 34 Helical. {ECO:0000255}.; TRANSMEM 50 72 Helical. {ECO:0000255}.; TRANSMEM 81 101 Helical. {ECO:0000255}.; TRANSMEM 112 132 Helical. {ECO:0000255}. FUNCTION: Involved in the regulation of cellular calcium homeotasis (PubMed:25996873). Required for spermatogenesis (PubMed:25996873). {ECO:0000269|PubMed:25996873}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q969S6}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Interacts with ATP2A2, ITPR3 and STIM1. {ECO:0000250|UniProtKB:Q969S6}. +Q1JRP2 TM11C_MOUSE Transmembrane protease serine 11C (EC 3.4.21.-) (Neurobin) [Cleaved into: Transmembrane protease serine 11C non-catalytic chain; Transmembrane protease serine 11C catalytic chain] 431 48,073 Active site (3); Chain (2); Disulfide bond (3); Domain (2); Glycosylation (3); Mutagenesis (4); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 34 54 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 33 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 55 431 Extracellular. {ECO:0000305}. FUNCTION: Serine protease which has a preference for Arg or Lys in position P1 and uncharged residues in positions P2 and P3. Shows specificity towards FGF2 in vitro. {ECO:0000269|PubMed:18215125}. PTM: Proteolytically cleaved via an autocatalytic mechanism. {ECO:0000269|PubMed:18215125}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18215125}; Single-pass type II membrane protein {ECO:0000305}. Cell projection, dendrite {ECO:0000269|PubMed:18215125}. Perikaryon {ECO:0000269|PubMed:18215125}. TISSUE SPECIFICITY: Expressed specifically in Purkinje neurons of the cerebellum (at protein level). Also detected in spinal cord. {ECO:0000269|PubMed:18215125}. +Q8K003 TMA7_MOUSE Translation machinery-associated protein 7 (Coiled-coil domain-containing protein 72) 64 7,066 Chain (1); Coiled coil (1); Modified residue (1) +Q8VCZ2 TM45B_MOUSE Transmembrane protein 45B 278 32,388 Chain (1); Modified residue (2); Sequence conflict (1); Transmembrane (7) TRANSMEM 7 27 Helical. {ECO:0000255}.; TRANSMEM 49 69 Helical. {ECO:0000255}.; TRANSMEM 95 115 Helical. {ECO:0000255}.; TRANSMEM 117 137 Helical. {ECO:0000255}.; TRANSMEM 149 169 Helical. {ECO:0000255}.; TRANSMEM 183 203 Helical. {ECO:0000255}.; TRANSMEM 215 235 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9CQC4 TM216_MOUSE Transmembrane protein 216 (Thymus atrophy-related protein) 141 16,160 Alternative sequence (1); Chain (1); Transmembrane (4) TRANSMEM 15 35 Helical. {ECO:0000255}.; TRANSMEM 49 69 Helical. {ECO:0000255}.; TRANSMEM 82 102 Helical. {ECO:0000255}.; TRANSMEM 115 135 Helical. {ECO:0000255}. FUNCTION: Part of the tectonic-like complex which is required for tissue-specific ciliogenesis and may regulate ciliary membrane composition. {ECO:0000269|PubMed:21725307}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:21725307}. Note=Localizes at the transition zone, a region between the basal body and the ciliary axoneme. SUBUNIT: Part of the tectonic-like complex (also named B9 complex) (PubMed:21725307). Interacts with TMEM107 (By similarity). {ECO:0000250|UniProtKB:Q9P0N5, ECO:0000269|PubMed:21725307}. +Q9D9D5 TMC5A_MOUSE Transmembrane and coiled-coil domain-containing protein 5A 303 35,854 Alternative sequence (1); Chain (1); Coiled coil (1); Erroneous gene model prediction (2); Transmembrane (1) TRANSMEM 242 264 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q80X59 TMC5B_MOUSE Transmembrane and coiled-coil domain-containing protein 5B 307 36,059 Chain (1); Coiled coil (1); Sequence conflict (1); Transmembrane (1) TRANSMEM 246 268 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q8BH24 TM9S4_MOUSE Transmembrane 9 superfamily member 4 643 74,693 Chain (1); Modified residue (1); Sequence conflict (4); Signal peptide (1); Topological domain (10); Transmembrane (9) TRANSMEM 283 303 Helical. {ECO:0000255}.; TRANSMEM 348 368 Helical. {ECO:0000255}.; TRANSMEM 378 398 Helical. {ECO:0000255}.; TRANSMEM 418 438 Helical. {ECO:0000255}.; TRANSMEM 451 471 Helical. {ECO:0000255}.; TRANSMEM 503 523 Helical. {ECO:0000255}.; TRANSMEM 537 557 Helical. {ECO:0000255}.; TRANSMEM 572 592 Helical. {ECO:0000255}.; TRANSMEM 600 620 Helical. {ECO:0000255}. TOPO_DOM 24 282 Extracellular. {ECO:0000255}.; TOPO_DOM 304 347 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 369 377 Extracellular. {ECO:0000255}.; TOPO_DOM 399 417 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 439 450 Extracellular. {ECO:0000255}.; TOPO_DOM 472 502 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 524 536 Extracellular. {ECO:0000255}.; TOPO_DOM 558 571 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 593 599 Extracellular. {ECO:0000255}.; TOPO_DOM 621 643 Cytoplasmic. {ECO:0000255}. FUNCTION: Associates with proteins harboring glycine-rich transmembrane domains and ensures their efficient localization to the cell surface. {ECO:0000250|UniProtKB:Q92544}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus {ECO:0000250|UniProtKB:Q92544}. Early endosome {ECO:0000250|UniProtKB:Q92544}. +Q7TN60 TMC6_MOUSE Transmembrane channel-like protein 6 810 90,546 Alternative sequence (5); Chain (1); Glycosylation (2); Modified residue (4); Sequence conflict (3); Topological domain (11); Transmembrane (10) TRANSMEM 206 226 Helical. {ECO:0000255}.; TRANSMEM 254 274 Helical. {ECO:0000255}.; TRANSMEM 339 359 Helical. {ECO:0000255}.; TRANSMEM 430 450 Helical. {ECO:0000255}.; TRANSMEM 469 489 Helical. {ECO:0000255}.; TRANSMEM 505 525 Helical. {ECO:0000255}.; TRANSMEM 553 573 Helical. {ECO:0000255}.; TRANSMEM 604 624 Helical. {ECO:0000255}.; TRANSMEM 650 670 Helical. {ECO:0000255}.; TRANSMEM 722 742 Helical. {ECO:0000255}. TOPO_DOM 1 205 Lumenal. {ECO:0000255}.; TOPO_DOM 227 253 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 275 338 Lumenal. {ECO:0000255}.; TOPO_DOM 360 429 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 451 468 Lumenal. {ECO:0000255}.; TOPO_DOM 490 504 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 526 552 Lumenal. {ECO:0000255}.; TOPO_DOM 574 603 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 625 649 Lumenal. {ECO:0000255}.; TOPO_DOM 671 721 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 743 810 Lumenal. {ECO:0000255}. FUNCTION: Probable ion channel. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12812529, ECO:0000269|PubMed:12906855}. +Q8C428 TMC7_MOUSE Transmembrane channel-like protein 7 726 83,337 Alternative sequence (1); Chain (1); Glycosylation (3); Modified residue (1); Sequence conflict (2); Topological domain (10); Transmembrane (9) TRANSMEM 167 187 Helical. {ECO:0000255}.; TRANSMEM 218 238 Helical. {ECO:0000255}.; TRANSMEM 262 282 Helical. {ECO:0000255}.; TRANSMEM 361 381 Helical. {ECO:0000255}.; TRANSMEM 403 423 Helical. {ECO:0000255}.; TRANSMEM 493 513 Helical. {ECO:0000255}.; TRANSMEM 554 574 Helical. {ECO:0000255}.; TRANSMEM 599 619 Helical. {ECO:0000255}.; TRANSMEM 664 684 Helical. {ECO:0000255}. TOPO_DOM 1 166 Extracellular. {ECO:0000255}.; TOPO_DOM 188 217 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 239 261 Extracellular. {ECO:0000255}.; TOPO_DOM 283 360 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 382 402 Extracellular. {ECO:0000255}.; TOPO_DOM 424 492 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 514 553 Extracellular. {ECO:0000255}.; TOPO_DOM 575 598 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 620 663 Extracellular. {ECO:0000255}.; TOPO_DOM 685 726 Cytoplasmic. {ECO:0000255}. FUNCTION: Probable ion channel. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:12812529}. +Q7TN58 TMC8_MOUSE Transmembrane channel-like protein 8 (Epidermodysplasia verruciformis protein 2 homolog) 722 82,329 Alternative sequence (1); Chain (1); Glycosylation (3); Modified residue (6); Sequence conflict (2); Topological domain (9); Transmembrane (8) TRANSMEM 119 139 Helical. {ECO:0000255}.; TRANSMEM 205 225 Helical. {ECO:0000255}.; TRANSMEM 308 328 Helical. {ECO:0000255}.; TRANSMEM 376 396 Helical. {ECO:0000255}.; TRANSMEM 431 451 Helical. {ECO:0000255}.; TRANSMEM 493 513 Helical. {ECO:0000255}.; TRANSMEM 537 557 Helical. {ECO:0000255}.; TRANSMEM 599 619 Helical. {ECO:0000255}. TOPO_DOM 1 118 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 140 204 Lumenal. {ECO:0000255}.; TOPO_DOM 226 307 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 329 375 Lumenal. {ECO:0000255}.; TOPO_DOM 397 430 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 452 492 Lumenal. {ECO:0000255}.; TOPO_DOM 514 536 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 558 598 Lumenal. {ECO:0000255}.; TOPO_DOM 620 722 Cytoplasmic. {ECO:0000255}. FUNCTION: Probable ion channel. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Expressed in thymus, lung, prostate, placenta, testis and spleen. {ECO:0000269|PubMed:12812529, ECO:0000269|PubMed:12906855}. +Q91W52 TMM19_MOUSE Transmembrane protein 19 336 36,296 Alternative sequence (1); Chain (1); Sequence conflict (1); Transmembrane (6) TRANSMEM 15 35 Helical. {ECO:0000255}.; TRANSMEM 49 69 Helical. {ECO:0000255}.; TRANSMEM 78 98 Helical. {ECO:0000255}.; TRANSMEM 218 238 Helical. {ECO:0000255}.; TRANSMEM 257 277 Helical. {ECO:0000255}.; TRANSMEM 313 333 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q7TSH8 TMM94_MOUSE Transmembrane protein 94 1360 151,796 Chain (1); Erroneous initiation (1); Glycosylation (6); Modified residue (9); Transmembrane (10) TRANSMEM 65 85 Helical. {ECO:0000255}.; TRANSMEM 94 114 Helical. {ECO:0000255}.; TRANSMEM 274 294 Helical. {ECO:0000255}.; TRANSMEM 321 341 Helical. {ECO:0000255}.; TRANSMEM 1097 1117 Helical. {ECO:0000255}.; TRANSMEM 1125 1145 Helical. {ECO:0000255}.; TRANSMEM 1173 1193 Helical. {ECO:0000255}.; TRANSMEM 1233 1253 Helical. {ECO:0000255}.; TRANSMEM 1270 1290 Helical. {ECO:0000255}.; TRANSMEM 1311 1331 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q80VW5 WHRN_MOUSE Whirlin 918 98,012 Alternative sequence (13); Chain (1); Compositional bias (2); Domain (3); Helix (7); Modified residue (1); Sequence conflict (1) FUNCTION: Involved in hearing and vision as member of the USH2 complex (PubMed:20502675). Necessary for elongation and maintenance of inner and outer hair cell stereocilia in the organ of Corti in the inner ear (PubMed:15590699). Involved in the maintenance of the hair bundle ankle region, which connects stereocilia in cochlear hair cells of the inner ear (PubMed:20502675, PubMed:24334608). In retina photoreceptors, required for the maintenance of periciliary membrane complex that seems to play a role in regulating intracellular protein transport (PubMed:20502675). {ECO:0000269|PubMed:15590699, ECO:0000269|PubMed:20502675, ECO:0000269|PubMed:24334608}. SUBCELLULAR LOCATION: Cytoplasm. Cell projection, stereocilium {ECO:0000269|PubMed:15590698, ECO:0000269|PubMed:15590699, ECO:0000269|PubMed:15654330, ECO:0000269|PubMed:17567809, ECO:0000269|PubMed:20502675, ECO:0000269|PubMed:24334608}. Cell projection, growth cone {ECO:0000269|PubMed:17584769}. Photoreceptor inner segment {ECO:0000269|PubMed:20502675, ECO:0000269|PubMed:24334608}. Cell junction, synapse {ECO:0000250|UniProtKB:Q810W9}. Note=Detected at the level of stereocilia in inner and outer hair cells of the cochlea and vestibule. Localizes to both tip and ankle-link stereocilia regions. Colocalizes with the growing ends of actin filaments (PubMed:15590699, PubMed:15590698, PubMed:15654330, PubMed:24334608). Colocalizes with MPP1 in the retina, at the outer limiting membrane (OLM), outer plexifirm layer (OPL), basal bodies and at the connecting cilium (CC) (PubMed:17584769). In photoreceptors, localizes at a plasma membrane microdomain in the apical inner segment that surrounds the connecting cilia called periciliary membrane complex (PubMed:20502675, PubMed:24334608). {ECO:0000269|PubMed:15590698, ECO:0000269|PubMed:15590699, ECO:0000269|PubMed:15654330, ECO:0000269|PubMed:17584769, ECO:0000269|PubMed:20502675, ECO:0000269|PubMed:24334608}. SUBUNIT: Forms homooligomers (PubMed:15590698, PubMed:25406310). Interacts (via C-terminal PDZ domain) with MYO15A; this interaction is necessary for localization of WHRN to stereocilia tips (PubMed:15654330, PubMed:15590698). Interacts (via C-terminal PDZ domain) with MPP1/p55 (PubMed:16829577, PubMed:17584769). Interacts with LRRC4C/NGL1 (PubMed:15590698). Interacts with MYO7A (PubMed:15590698). Interacts with RPGR (PubMed:22323458). Interacts with EPS8 (PubMed:21236676). Interacts with CASK. Interacts with CIB2 (By similarity). Component of USH2 complex, composed of ADGRV1, PDZD7, USH2A and WHRN (PubMed:20502675, PubMed:25406310). Interacts (via PDZ domains) with PDZD7; the interaction is direct (PubMed:25406310). Interacts (via N-terminal PDZ domain) with USH2A (via cytoplasmic region) (PubMed:16301217, PubMed:20502675, PubMed:23055499). Interacts with ADGRV1/MASS1 (via cytoplasmic region) (PubMed:20502675, PubMed:23055499). {ECO:0000250|UniProtKB:Q810W9, ECO:0000250|UniProtKB:Q9P202, ECO:0000269|PubMed:15590698, ECO:0000269|PubMed:15654330, ECO:0000269|PubMed:16301217, ECO:0000269|PubMed:16829577, ECO:0000269|PubMed:17584769, ECO:0000269|PubMed:20502675, ECO:0000269|PubMed:21236676, ECO:0000269|PubMed:22323458, ECO:0000269|PubMed:23055499, ECO:0000269|PubMed:25406310}. TISSUE SPECIFICITY: Expressed in the retina. Colocalizes with RPGR in the photoreceptor connecting cilium, a thin bridge linking the cell body and the light-sensing outer segment (at protein level). Detected in the inner ear throughout development from embryonic day 12 to 20 days after birth. Displays a dynamic pattern of expression after birth, demonstrating an ordered appearance and fade-out across stereocilia rows. Isoforms 5, 6, 7 and 8 are not detected in the retina (PubMed:20502675). {ECO:0000269|PubMed:12833159, ECO:0000269|PubMed:15590699, ECO:0000269|PubMed:17567809, ECO:0000269|PubMed:20502675, ECO:0000269|PubMed:22323458}. DISEASE: Note=Defects in Whrn are the cause of the phenotype whirler (wi). Mutants are characterized by deafness due to malformation of the cochlear inner and outer hair cells and by circling behavior. Stereocilia are shorter and wider than in wild-type animals and there is a decrease in the number of actin filaments in inner and outer hair cells. The number of outer hair cell stereocilia is reduced with increased spacing between them. {ECO:0000269|PubMed:12124769, ECO:0000269|PubMed:12833159, ECO:0000269|PubMed:17326148}. +Q8VCH0 THIKB_MOUSE 3-ketoacyl-CoA thiolase B, peroxisomal (EC 2.3.1.16) (Acetyl-CoA acyltransferase B) (Beta-ketothiolase B) (Peroxisomal 3-oxoacyl-CoA thiolase B) 424 43,995 Active site (3); Chain (1); Modified residue (2); Transit peptide (1) Lipid metabolism; fatty acid metabolism. SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Mainly expressed in liver; weaker levels in kidney, intestine and white adipose tissue. {ECO:0000269|PubMed:15043762}. +Q8K1I7 WIPF1_MOUSE WAS/WASL-interacting protein family member 1 (Wiskott-Aldrich syndrome protein-interacting protein) (WASP-interacting protein) 493 50,080 Chain (1); Compositional bias (3); Domain (1); Modified residue (7); Region (1); Repeat (3) FUNCTION: Plays a role in the reorganization of the actin cytoskeleton. Contributes with NCK1 and GRB2 in the recruitment and activation of WASL. May participate in regulating the subcellular localization of WASL, resulting in the disassembly of stress fibers in favor of filopodia formation (By similarity). Plays a role in the formation of cell ruffles. {ECO:0000250, ECO:0000269|PubMed:12147689, ECO:0000269|PubMed:19910490}. SUBCELLULAR LOCATION: Cytoplasmic vesicle {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell projection, ruffle {ECO:0000269|PubMed:12147689, ECO:0000269|PubMed:19910490}. Note=Vesicle surfaces and along actin tails. Colocalizes with actin stress fibers. When coexpressed with WASL, no longer associated with actin filaments but accumulated in perinuclear and cortical areas like WASL (By similarity). {ECO:0000250}. SUBUNIT: Binds to WAS within the N-terminal region, at a site distinct from the CDC42-binding site. Binds profilin and actin (By similarity). Binds to WASL. Interacts with DBNL. Interacts with DBNL. Interacts with FNBP1L (via the SH3 domain) (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O43516, ECO:0000269|PubMed:12147689, ECO:0000269|PubMed:19910490}. +Q8R3E3 WIPI1_MOUSE WD repeat domain phosphoinositide-interacting protein 1 (WIPI-1) (WD40 repeat protein interacting with phosphoinositides of 49 kDa) (WIPI 49 kDa) 446 48,758 Alternative sequence (3); Chain (1); Erroneous initiation (2); Motif (1); Repeat (3) FUNCTION: Component of the autophagy machinery that controls the major intracellular degradation process by which cytoplasmic materials are packaged into autophagosomes and delivered to lysosomes for degradation. Plays an important role in starvation- and calcium-mediated autophagy, as well as in mitophagy (By similarity) (PubMed:22275429). Functions downstream of the ULK1 and PI3-kinases that produce phosphatidylinositol 3-phosphate (PtdIns3P) on membranes of the endoplasmic reticulum once activated. Binds phosphatidylinositol 3-phosphate (PtdIns3P), and maybe other phosphoinositides including PtdIns3,5P2 and PtdIns5P, and is recruited to phagophore assembly sites at the endoplasmic reticulum membranes. There, it assists WIPI2 in the recruitment of ATG12-ATG5-ATG16L1, a complex that directly controls the elongation of the nascent autophagosomal membrane. Involved in xenophagy of Staphylococcus aureus. Invading S.aureus cells become entrapped in autophagosome-like WIPI1 positive vesicles targeted for lysosomal degradation. Plays also a distinct role in controlling the transcription of melanogenic enzymes and melanosome maturation, a process that is distinct from starvation-induced autophagy. May also regulate the trafficking of proteins involved in the mannose-6-phosphate receptor (MPR) recycling pathway (By similarity). {ECO:0000250|UniProtKB:Q5MNZ9, ECO:0000269|PubMed:22275429}. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q5MNZ9}. Endosome {ECO:0000250|UniProtKB:Q5MNZ9}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:Q5MNZ9}. Preautophagosomal structure membrane {ECO:0000269|PubMed:21896713}; Peripheral membrane protein {ECO:0000269|PubMed:21896713}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q5MNZ9}. Note=Trans elements of the Golgi and peripheral endosomes. Dynamically cycles through these compartments and is susceptible to conditions that modulate membrane flux. Enriched in clathrin-coated vesicles. Upon starvation-induced autophagy, accumulates at subcellular structures in the cytoplasm: enlarged vesicular and lasso-like structures, and large cup-shaped structures predominantly around the nucleus. Recruitment to autophagic membranes is controlled by MTMR14. Labile microtubules specifically recruit markers of autophagosome formation like WIPI1, whereas mature autophagosomes may bind to stable microtubules. {ECO:0000250|UniProtKB:Q5MNZ9}. SUBUNIT: Interacts with androgen receptor (AR) and the estrogen receptors ESR1 and ESR2. Interacts with WIPI2. Interacts with WDR45. Interacts with ATG16L1. May interact with NUDC. {ECO:0000250|UniProtKB:Q5MNZ9}. DOMAIN: The N-terminus might form a beta-propeller domain involved in specific binding to phosphatidylinositol 3,5-bisphosphate (PIP2), leading to the association of the protein to the membrane. Association to the membrane can also occur through binding to phosphatidylinositol 3-monophosphate (PI3P). +P97493 THIOM_MOUSE Thioredoxin, mitochondrial (MTRX) (Mt-Trx) (Thioredoxin-2) 166 18,255 Active site (2); Chain (1); Disulfide bond (1); Domain (1); Modified residue (2); Site (3); Transit peptide (1) FUNCTION: Important for the control of mitochondrial reactive oxygen species homeostasis, apoptosis regulation and cell viability. Possesses a dithiol-reducing activity. {ECO:0000250|UniProtKB:Q99757, ECO:0000269|PubMed:12529397}. SUBCELLULAR LOCATION: Mitochondrion. +Q8K0P3 TLDC1_MOUSE TLD domain-containing protein 1 (TBC/LysM-associated domain-containing protein 1) 455 50,845 Alternative sequence (2); Chain (1); Domain (1); Erroneous initiation (1); Frameshift (1); Initiator methionine (1); Lipidation (1) SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q6P9B6}. Cytoplasm {ECO:0000250|UniProtKB:Q6P9B6}. +Q9R1X4 TIM_MOUSE Protein timeless homolog (mTim) 1197 137,503 Alternative sequence (4); Chain (1); Compositional bias (2); Modified residue (5); Region (3); Sequence caution (2); Sequence conflict (10) FUNCTION: Plays an important role in the control of DNA replication, maintenance of replication fork stability, maintenance of genome stability throughout normal DNA replication, DNA repair and in the regulation of the circadian clock (PubMed:9856465, PubMed:23418588, PubMed:10428031, PubMed:12875843). Required to stabilize replication forks during DNA replication by forming a complex with TIPIN: this complex regulates DNA replication processes under both normal and stress conditions, stabilizes replication forks and influences both CHEK1 phosphorylation and the intra-S phase checkpoint in response to genotoxic stress (PubMed:12875843). TIMELESS promotes TIPIN nuclear localization (PubMed:12875843). Involved in cell survival after DNA damage or replication stress by promoting DNA repair (PubMed:12875843). In response to double-strand breaks (DSBs), accumulates at DNA damage sites and promotes homologous recombination repair via its interaction with PARP1 (By similarity). May be specifically required for the ATR-CHEK1 pathway in the replication checkpoint induced by hydroxyurea or ultraviolet light (PubMed:23418588). Involved in the determination of period length and in the DNA damage-dependent phase advancing of the circadian clock (PubMed:23418588, PubMed:10428031). Negatively regulates CLOCK|NPAS2-ARTNL/BMAL1|ARTNL2/BMAL2-induced transactivation of PER1 possibly via translocation of PER1 into the nucleus (PubMed:9856465). May also play an important role in epithelial cell morphogenesis and formation of branching tubules (PubMed:10963667). {ECO:0000250|UniProtKB:Q9UNS1, ECO:0000269|PubMed:10428031, ECO:0000269|PubMed:10963667, ECO:0000269|PubMed:12875843, ECO:0000269|PubMed:23418588, ECO:0000269|PubMed:9856465}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10231394, ECO:0000269|PubMed:10428031, ECO:0000269|PubMed:23418588, ECO:0000269|PubMed:24489120}. Chromosome {ECO:0000250|UniProtKB:Q9UNS1}. Note=In response to double-strand breaks (DSBs), accumulates at DNA damage sites via its interaction with PARP1. {ECO:0000250|UniProtKB:Q9UNS1}. SUBUNIT: Homodimer or homomultimer (PubMed:12875843, PubMed:23418588). Component of the circadian core oscillator, which includes the CRY proteins, CLOCK or NPAS2, ARTNL/BMAL1 or ARTNL2/BMAL2, CSKN1D and/or CSNK1E, TIMELESS, and the PER proteins (PubMed:9856465). Interacts directly with PER2; the interaction with PER2 is via its second PAS domain (PubMed:14564007). Interacts directly with PER1 and PER3 (PubMed:9856465, PubMed:10231394, PubMed:14564007). Interacts with CRY1 (PubMed:10428031, PubMed:23418588, PubMed:24489120). Interacts with CRY2 (PubMed:10428031). Interacts with CHEK1, ATR and ATRIP (By similarity). Interacts with CLSPN (By similarity). Interacts with TIPIN (PubMed:12875843). Interacts with DDX11; this interaction increases recruitment of both proteins onto chromatin in response to replication stress induction by hydroxyurea (By similarity). Interacts with PARP1; interaction is direct and independent of poly-ADP-ribose (By similarity). {ECO:0000250|UniProtKB:Q9UNS1, ECO:0000269|PubMed:10231394, ECO:0000269|PubMed:10428031, ECO:0000269|PubMed:12875843, ECO:0000269|PubMed:14564007, ECO:0000269|PubMed:23418588, ECO:0000269|PubMed:24489120, ECO:0000269|PubMed:9856465}. TISSUE SPECIFICITY: Predominantly and robustly expressed in proliferative organs (spleen, thymus, intestine and testis) compared to those more differentiated such as kidney and liver (at protein level). Expressed in all tissues examined including brain, heart, lung, liver, skeletal muscle, kidney, placenta, pancreas, spleen, thymus and testis. Strongly expressed in the suprachiasmatic nucleus (SCN) and pars tuberalis, moderately in the cingulate cortex, pyrimidal cell layer of the piriform cortex, periventricular part of the caudate putamen, and granular layer of the cerebellum, and weakly in the cerebral cortex, gyrus dentatus, hippocampus and thalamic nuclei. In embryonic kidney, expression is highest in regions of active ureteric bud cell branching. {ECO:0000269|PubMed:10231394, ECO:0000269|PubMed:10428031, ECO:0000269|PubMed:10963667, ECO:0000269|PubMed:23418588, ECO:0000269|PubMed:9856465, ECO:0000269|PubMed:9856466, ECO:0000269|PubMed:9891984}. +Q9CPV0 TM107_MOUSE Transmembrane protein 107 140 15,593 Alternative sequence (1); Chain (1); Glycosylation (1); Natural variant (1); Sequence conflict (1); Transmembrane (4) TRANSMEM 7 27 Helical. {ECO:0000255}.; TRANSMEM 53 73 Helical. {ECO:0000255}.; TRANSMEM 83 103 Helical. {ECO:0000255}.; TRANSMEM 113 133 Helical. {ECO:0000255}. FUNCTION: Plays a role in cilia formation and embryonic patterning. Requires for normal Sonic hedgehog (Shh) signaling in the neural tube and acts in combination with GLI2 and GLI3 to pattern ventral and intermediate neuronal cell types. During ciliogenesis regulates the ciliary transition zone localization of some MKS complex proteins (PubMed:26595381, PubMed:26518474). {ECO:0000269|PubMed:22698544, ECO:0000269|PubMed:26518474, ECO:0000269|PubMed:26595381}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cell projection, cilium. Note=Localizes at the transition zone, a region between the basal body and the ciliary axoneme. {ECO:0000269|PubMed:26518474}. SUBUNIT: Part of the tectonic-like complex (also named B9 complex). Interacts with TMEM237, TMEM231, MKS1 and TMEM216. {ECO:0000250|UniProtKB:Q6UX40}. DISEASE: Note=Defect in TMEM107 is the cause of the schlei phenotype. Schlei mice display Shh-related defects including, preaxial polydactyly, exencephaly, and disrupted ventral neural tube patterning. Mice shown decreased numbers of cilia in several developing tissues and organs. However, nodal cilia appear normal in schlei mutants and subsequently, no left-right defects are observed. {ECO:0000269|PubMed:22698544}. +Q9D123 TM219_MOUSE Insulin-like growth factor-binding protein 3 receptor (IGFBP-3R) (Transmembrane protein 219) 240 25,573 Alternative sequence (3); Chain (1); Compositional bias (1); Glycosylation (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 205 225 Helical. {ECO:0000255}. TOPO_DOM 39 204 Extracellular. {ECO:0000255}.; TOPO_DOM 226 240 Cytoplasmic. {ECO:0000255}. FUNCTION: Cell death receptor specific for IGFBP3, may mediate caspase-8-dependent apoptosis upon ligand binding. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane protein. SUBUNIT: Interacts with IGFBP3. Interacts with CASP8 (By similarity). {ECO:0000250}. +Q8VEH0 TM144_MOUSE Transmembrane protein 144 348 37,771 Chain (1); Sequence conflict (1); Transmembrane (10) TRANSMEM 8 28 Helical. {ECO:0000255}.; TRANSMEM 39 59 Helical. {ECO:0000255}.; TRANSMEM 64 86 Helical. {ECO:0000255}.; TRANSMEM 93 115 Helical. {ECO:0000255}.; TRANSMEM 125 145 Helical. {ECO:0000255}.; TRANSMEM 193 213 Helical. {ECO:0000255}.; TRANSMEM 235 255 Helical. {ECO:0000255}.; TRANSMEM 267 287 Helical. {ECO:0000255}.; TRANSMEM 296 316 Helical. {ECO:0000255}.; TRANSMEM 326 346 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +B2RWJ3 TM240_MOUSE Transmembrane protein 240 173 20,005 Chain (1); Modified residue (1); Transmembrane (2) TRANSMEM 5 25 Helical; Name=1. {ECO:0000255}.; TRANSMEM 90 110 Helical; Name=2. {ECO:0000255}. SUBCELLULAR LOCATION: Cell junction, synapse {ECO:0000269|PubMed:22645316}. Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +P56983 TM14A_MOUSE Transmembrane protein 14A 99 10,594 Chain (1); Transmembrane (3) TRANSMEM 1 21 Helical. {ECO:0000255}.; TRANSMEM 24 44 Helical. {ECO:0000255}.; TRANSMEM 79 99 Helical. {ECO:0000255}. FUNCTION: Inhibits apoptosis via negative regulation of the mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway. {ECO:0000250|UniProtKB:Q9Y6G1}. SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250|UniProtKB:Q9Y6G1}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9Y6G1}. +P86045 TM207_MOUSE Transmembrane protein 207 143 15,808 Chain (1); Sequence caution (1); Signal peptide (1); Transmembrane (1) TRANSMEM 52 72 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Interacts with WWOX. {ECO:0000250}. +Q8CIB6 TM230_MOUSE Transmembrane protein 230 120 13,188 Chain (1); Modified residue (2); Sequence conflict (1); Transmembrane (2) TRANSMEM 46 66 Helical. {ECO:0000255}.; TRANSMEM 79 99 Helical. {ECO:0000255}. FUNCTION: Involved in trafficking and recycling of synaptic vesicles. {ECO:0000250|UniProtKB:Q96A57}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000269|PubMed:27270108}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q96A57}. Early endosome {ECO:0000250|UniProtKB:Q96A57}. Recycling endosome {ECO:0000250|UniProtKB:Q96A57}. Late endosome {ECO:0000250|UniProtKB:Q96A57}. Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:Q96A57}. TISSUE SPECIFICITY: Widely expressed, including dopaminergic neurons in the substantia nigra. {ECO:0000269|PubMed:27270108}. +Q8BZB3 TM266_MOUSE Transmembrane protein 266 538 58,897 Alternative sequence (4); Chain (1); Coiled coil (1); Glycosylation (1); Transmembrane (3) TRANSMEM 103 123 Helical. {ECO:0000255}.; TRANSMEM 131 151 Helical. {ECO:0000255}.; TRANSMEM 170 190 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q9CXY1 TM175_MOUSE Endosomal/lysosomal potassium channel TMEM175 (Transmembrane protein 175) (mTMEM175) 499 55,578 Chain (1); Modified residue (1); Motif (2); Region (4); Sequence conflict (4); Site (6); Topological domain (13); Transmembrane (12) TRANSMEM 33 53 Helical; Name=TM1-1. {ECO:0000255}.; TRANSMEM 70 90 Helical; Name=TM2-1. {ECO:0000255}.; TRANSMEM 108 128 Helical; Name=TM3-1. {ECO:0000255}.; TRANSMEM 135 155 Helical; Name=TM4-1. {ECO:0000255}.; TRANSMEM 182 202 Helical; Name=TM5-1. {ECO:0000255}.; TRANSMEM 208 227 Helical; Name=TM6-1. {ECO:0000255}.; TRANSMEM 258 278 Helical; Name=TM1-2. {ECO:0000255}.; TRANSMEM 307 327 Helical; Name=TM2-2. {ECO:0000255}.; TRANSMEM 337 357 Helical; Name=TM3-2. {ECO:0000255}.; TRANSMEM 375 395 Helical; Name=TM4-2. {ECO:0000255}.; TRANSMEM 414 434 Helical; Name=TM5-2. {ECO:0000255}.; TRANSMEM 450 470 Helical; Name=TM6-2. {ECO:0000255}. TOPO_DOM 1 32 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 54 69 Lumenal. {ECO:0000305}.; TOPO_DOM 91 107 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 129 134 Lumenal. {ECO:0000305}.; TOPO_DOM 156 181 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 203 207 Lumenal. {ECO:0000305}.; TOPO_DOM 228 257 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 279 306 Lumenal. {ECO:0000305}.; TOPO_DOM 328 336 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 358 374 Lumenal. {ECO:0000305}.; TOPO_DOM 396 413 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 435 449 Lumenal. {ECO:0000305}.; TOPO_DOM 471 499 Cytoplasmic. {ECO:0000305}. FUNCTION: Organelle-specific potassium channel specifically responsible for potassium conductance in endosomes and lysosomes. Forms a potassium-permeable leak-like channel, which regulates lumenal pH stability and is required for autophagosome-lysosome fusion. Constitutes the major lysosomal potassium channel. {ECO:0000269|PubMed:26317472}. SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250|UniProtKB:Q9BSA9}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:Q9BSA9}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9BSA9}. DOMAIN: Composed of two modules of six transmembranes, forming a homodimer with a tetrameric architecture (By similarity). The six transmembrane regions of each module are tightly packed within each subunit without undergoing domain swapping (By similarity). Transmembranes TM1-TM3 of each module are positioned on the inner circle of the channel tetramer and participate in inter-subunit interactions that are central to the assembly of the ion conduction pore (By similarity). The RxxxFSD motifs within transmembranes TM1 coordinate a network of specific inter- and intra-subunit interactions with other conserved residues on TM2 and TM3 and play a key role in the tetrameric assembly of the channel (By similarity). Transmembranes TM4-TM6 are positioned on the periphery of the channel and do not contribute contacts with neighboring subunits (By similarity). Transmembranes TM1 and TM2 are linked by an extended strand-like tail and two short helices (H1 and H2) which protrude outwards from the main body of the transmembrane domain and enclose the external open entrance of the ion conduction pore in the channel tetramer (By similarity). Transmembranes TM1 form the pore-lining inner helix at the center of the channel, creating an hourglass-shaped ion permeation pathway in the channel tetramer (By similarity). Three hydrophobic residues on the C-terminal half of the TM1 helices form a bottleneck along the ion conduction pathway and serve as the selectivity filter of the channel (By similarity). Ile-43 (and Ile-268) are probably responsible for channel selectivity (By similarity). {ECO:0000250|UniProtKB:K9UJK2, ECO:0000250|UniProtKB:Q9BSA9}. +Q3UFY8 TM10C_MOUSE tRNA methyltransferase 10 homolog C (Mitochondrial ribonuclease P protein 1) (Mitochondrial RNase P protein 1) (RNA (guanine-9-)-methyltransferase domain-containing protein 1) (mRNA methyladenosine-N(1)-methyltransferase) (EC 2.1.1.-) (tRNA (adenine(9)-N(1))-methyltransferase) (EC 2.1.1.218) (tRNA (guanine(9)-N(1))-methyltransferase) (EC 2.1.1.221) 414 48,386 Chain (1); Coiled coil (1); Domain (1); Modified residue (1); Sequence conflict (9); Transit peptide (1) FUNCTION: Mitochondrial tRNA N(1)-methyltransferase involved in mitochondrial tRNA maturation. Component of mitochondrial ribonuclease P, a complex composed of TRMT10C/MRPP1, HSD17B10/MRPP2 and MRPP3, which cleaves tRNA molecules in their 5'-ends. Together with HSD17B10/MRPP2, forms a subcomplex of the mitochondrial ribonuclease P, named MRPP1-MRPP2 subcomplex, which displays functions that are independent of the ribonuclease P activity. The MRPP1-MRPP2 subcomplex catalyzes the formation of N(1)-methylguanine and N(1)-methyladenine at position 9 (m1G9 and m1A9, respectively) in tRNAs; TRMT10C/MRPP1 acting as the catalytic N(1)-methyltransferase subunit. The MRPP1-MRPP2 subcomplex also acts as a tRNA maturation platform: following 5'-end cleavage by the mitochondrial ribonuclease P complex, the MRPP1-MRPP2 subcomplex enhances the efficiency of 3'-processing catalyzed by ELAC2, retains the tRNA product after ELAC2 processing and presents the nascent tRNA to the mitochondrial CCA tRNA nucleotidyltransferase TRNT1 enzyme. In addition to tRNA N(1)-methyltransferase activity, TRMT10C/MRPP1 also acts as a mRNA N(1)-methyltransferase by mediating methylation of adenosine residues at the N(1) position of MT-ND5 mRNA. {ECO:0000250|UniProtKB:Q7L0Y3}. SUBCELLULAR LOCATION: Mitochondrion matrix, mitochondrion nucleoid {ECO:0000250|UniProtKB:Q7L0Y3}. SUBUNIT: Component of mitochondrial ribonuclease P, a complex composed of TRMT10C/MRPP1, HSD17B10/MRPP2 and MRPP31. Interacts with HSD17B10/MRPP2; forming the MRPP1-MRPP2 subcomplex of the mitochondrial ribonuclease P complex. Interacts with GRSF1. {ECO:0000250|UniProtKB:Q7L0Y3}. +Q923U0 TM1L1_MOUSE TOM1-like protein 1 (Src-activating and signaling molecule protein) (Target of Myb-like protein 1) 474 52,695 Alternative sequence (2); Chain (1); Domain (2); Modified residue (4); Motif (2); Mutagenesis (3); Region (2); Sequence conflict (1) FUNCTION: Probable adapter protein involved in signaling pathways. Interacts with the SH2 and SH3 domains of various signaling proteins when it is phosphorylated. May promote FYN activation, possibly by disrupting intramolecular SH3-dependent interactions. {ECO:0000269|PubMed:11711534}. PTM: Phosphorylated on tyrosines by LYN (By similarity). Phosphorylated on tyrosines by FYN. {ECO:0000250, ECO:0000269|PubMed:11711534}. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack. Endosome membrane {ECO:0000305}. Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=A small proportion is membrane-associated. {ECO:0000250}. SUBUNIT: Interacts with LYN (By similarity). Interacts with the SH2 and SH3 domains of FYN when phosphorylated. Also interacts with GRB2 and PIK3R1 when phosphorylated. {ECO:0000250}. TISSUE SPECIFICITY: Strongly expressed in brain and kidney, expressed at intermediate levels skin and heart, and weakly expressed in thymus. Not expressed in liver and spleen. +Q5SRX1 TM1L2_MOUSE TOM1-like protein 2 (Target of Myb-like protein 2) 507 55,663 Alternative sequence (7); Chain (1); Domain (2); Modified residue (2); Motif (1); Sequence conflict (4) FUNCTION: Probable role in protein transport. May regulate growth factor-induced mitogenic signaling (By similarity). {ECO:0000250}. SUBUNIT: Interacts with clathrin, SRC and TOLLIP. {ECO:0000250}. DOMAIN: The GAT domain mediates interaction with TOLLIP. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed. Splicing pattern displays tissue specific variation. {ECO:0000269|PubMed:11997338}. +A2A8U2 TM201_MOUSE Transmembrane protein 201 (Spindle-associated membrane protein 1) 664 72,500 Alternative sequence (4); Chain (1); Compositional bias (1); Modified residue (9); Sequence conflict (1); Topological domain (6); Transmembrane (5) TRANSMEM 215 235 Helical. {ECO:0000255}.; TRANSMEM 298 318 Helical. {ECO:0000255}.; TRANSMEM 323 343 Helical. {ECO:0000255}.; TRANSMEM 357 374 Helical. {ECO:0000255}.; TRANSMEM 643 663 Helical. {ECO:0000255}. TOPO_DOM 1 214 Nuclear. {ECO:0000250|UniProtKB:Q5SNT2}.; TOPO_DOM 236 297 Perinuclear space. {ECO:0000305}.; TOPO_DOM 319 322 Nuclear. {ECO:0000305}.; TOPO_DOM 344 356 Perinuclear space. {ECO:0000305}.; TOPO_DOM 375 642 Nuclear. {ECO:0000250|UniProtKB:Q5SNT2, ECO:0000305}.; TOPO_DOM 664 664 Perinuclear space. {ECO:0000305}. FUNCTION: Involved in nuclear movement during fibroblast polarization and migration (PubMed:22349700). May recruit Ran GTPase to the nuclear periphery (By similarity). {ECO:0000250|UniProtKB:Q5SNT2, ECO:0000269|PubMed:22349700}.; FUNCTION: Isoform 2: May define a distinct membrane domain in the vicinity of the mitotic spindle. Involved in the organization of the nuclear envelope implicating EMD, SUN1 and A-type lamina. {ECO:0000250|UniProtKB:Q5SNT2}.; FUNCTION: Isoform 3: Proposed to be involved in actin-dependent nuclear movement; via SUN2 associates with transmembrane actin-associated nuclear (TAN) lines which are bound to F-actin cables and couple the nucleus to retrograde actin flow. {ECO:0000305|PubMed:22349700}. SUBCELLULAR LOCATION: Isoform 2: Nucleus inner membrane {ECO:0000250|UniProtKB:Q5SNT2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5SNT2}. Note=The C-terminal of isoform 2 is located on the nucleoplasmic side. During interphase, isoform 2 is distributed in the inner nuclear membrane and during mitosis, it is found in the ER but it also localizes to the polar regions of the mitotic spindle (By similarity). {ECO:0000250|UniProtKB:Q5SNT2}. SUBUNIT: Isoform 2 interacts with EMD (By similarity). Isoform 3 interacts with SUN2 and LMNA (PubMed:22349700). May bind to Ran GTPase; has a greater affinity for Ran-GTP over Ran-GDP (By similarity). {ECO:0000250|UniProtKB:Q5SNT2, ECO:0000269|PubMed:22349700}. +Q80W35 TM202_MOUSE Transmembrane protein 202 275 31,551 Chain (1); Transmembrane (4) TRANSMEM 60 80 Helical. {ECO:0000255}.; TRANSMEM 116 136 Helical. {ECO:0000255}.; TRANSMEM 151 171 Helical. {ECO:0000255}.; TRANSMEM 193 213 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q3TYE7 TM136_MOUSE Transmembrane protein 136 245 27,705 Chain (1); Domain (1); Transmembrane (6) TRANSMEM 1 21 Helical. {ECO:0000255}.; TRANSMEM 38 58 Helical. {ECO:0000255}.; TRANSMEM 75 95 Helical. {ECO:0000255}.; TRANSMEM 99 119 Helical. {ECO:0000255}.; TRANSMEM 162 182 Helical. {ECO:0000255}.; TRANSMEM 191 211 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9CZR3 TM40L_MOUSE Mitochondrial import receptor subunit TOM40B (Protein TOMM40-like) 308 34,005 Chain (1); Region (1) FUNCTION: Potential channel-forming protein implicated in import of protein precursors into mitochondria. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Forms part of the preprotein translocase of the outer mitochondrial membrane (TOM complex) containing TOMM22, TOMM40, TOMM40L and TOMM70. Interacts with mitochondrial targeting sequences (By similarity). {ECO:0000250}. +Q9CRG1 TM7S3_MOUSE Transmembrane 7 superfamily member 3 (NARP1) 565 63,251 Chain (1); Compositional bias (1); Glycosylation (4); Sequence conflict (11); Signal peptide (1); Transmembrane (7) TRANSMEM 287 307 Helical. {ECO:0000255}.; TRANSMEM 315 335 Helical. {ECO:0000255}.; TRANSMEM 341 361 Helical. {ECO:0000255}.; TRANSMEM 364 384 Helical. {ECO:0000255}.; TRANSMEM 402 422 Helical. {ECO:0000255}.; TRANSMEM 427 447 Helical. {ECO:0000255}.; TRANSMEM 478 498 Helical. {ECO:0000255}. FUNCTION: Involved in the inhibition of cytokine-induced death of pancreatic beta cells (PubMed:21853325). Involved in the promotion of insulin secretion from pancreatic beta cells (By similarity). Is a downstream transcriptional target of p53/TP53, and acts as a pro-survival homeostatic factor that attenuates the development of cellular stress. Maintains protein homeostasis and promotes cell survival through attenuation of endoplasmic reticulum (ER) stress and the subsequent induction of unfolded protein response (UPR) (PubMed:27740623). {ECO:0000250|UniProtKB:Q9NS93, ECO:0000269|PubMed:21853325, ECO:0000269|PubMed:27740623}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9NS93}; Multi-pass membrane protein {ECO:0000255}. +Q8K1A5 TM41B_MOUSE Transmembrane protein 41B 291 32,429 Alternative sequence (2); Chain (1); Modified residue (2); Region (1); Sequence conflict (13); Transmembrane (6) TRANSMEM 52 72 Helical. {ECO:0000255}.; TRANSMEM 109 129 Helical. {ECO:0000255}.; TRANSMEM 147 169 Helical. {ECO:0000255}.; TRANSMEM 197 217 Helical. {ECO:0000255}.; TRANSMEM 225 245 Helical. {ECO:0000255}.; TRANSMEM 262 282 Helical. {ECO:0000255}. FUNCTION: Required for normal motor neuron development. Required for autophagosome formation. {ECO:0000250|UniProtKB:A1A5V7, ECO:0000250|UniProtKB:Q5BJD5}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q5BJD5}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Interacts with VMP1. {ECO:0000250|UniProtKB:Q5BJD5}. DOMAIN: The VTT domain was previously called the SNARE-assoc domain. As there is no evidence that this domain associates with SNARE proteins, it was renamed as VMP1, TMEM41, and TVP38 (VTT) domain. {ECO:0000250|UniProtKB:Q5BJD5}. TISSUE SPECIFICITY: Expressed in brain, spinal cord, kidney and first lumbar dorsal root ganglia during postnatal development. Expressed in motor neurons and proprioceptive neurons. {ECO:0000269|PubMed:23063131}. +Q8BKU8 TM87B_MOUSE Transmembrane protein 87B 555 62,898 Alternative sequence (2); Chain (1); Frameshift (1); Glycosylation (4); Modified residue (3); Sequence conflict (8); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 217 237 Helical; Name=1. {ECO:0000255}.; TRANSMEM 249 269 Helical; Name=2. {ECO:0000255}.; TRANSMEM 301 321 Helical; Name=3. {ECO:0000255}.; TRANSMEM 324 344 Helical; Name=4. {ECO:0000255}.; TRANSMEM 352 372 Helical; Name=5. {ECO:0000255}.; TRANSMEM 395 415 Helical; Name=6. {ECO:0000255}.; TRANSMEM 430 450 Helical; Name=7. {ECO:0000255}. TOPO_DOM 43 216 Lumenal. {ECO:0000305}.; TOPO_DOM 238 248 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 270 300 Lumenal. {ECO:0000305}.; TOPO_DOM 322 323 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 345 351 Lumenal. {ECO:0000305}.; TOPO_DOM 373 394 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 416 429 Lumenal. {ECO:0000305}.; TOPO_DOM 451 555 Cytoplasmic. {ECO:0000305}. FUNCTION: May be involved in retrograde transport from endosomes to the trans-Golgi network (TGN). {ECO:0000250|UniProtKB:Q96K49}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q96K49}; Multi-pass membrane protein {ECO:0000255}. +Q9CXL1 TM50A_MOUSE Transmembrane protein 50A (Small membrane protein 1) 157 17,495 Chain (1); Initiator methionine (1); Modified residue (2); Transmembrane (4) TRANSMEM 26 46 Helical. {ECO:0000255}.; TRANSMEM 58 78 Helical. {ECO:0000255}.; TRANSMEM 95 115 Helical. {ECO:0000255}.; TRANSMEM 126 146 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +P58021 TM9S2_MOUSE Transmembrane 9 superfamily member 2 662 75,330 Chain (1); Signal peptide (1); Topological domain (10); Transmembrane (9) TRANSMEM 300 320 Helical. {ECO:0000255}.; TRANSMEM 374 394 Helical. {ECO:0000255}.; TRANSMEM 398 418 Helical. {ECO:0000255}.; TRANSMEM 437 457 Helical. {ECO:0000255}.; TRANSMEM 466 486 Helical. {ECO:0000255}.; TRANSMEM 522 542 Helical. {ECO:0000255}.; TRANSMEM 554 574 Helical. {ECO:0000255}.; TRANSMEM 591 611 Helical. {ECO:0000255}.; TRANSMEM 631 651 Helical. {ECO:0000255}. TOPO_DOM 29 299 Lumenal. {ECO:0000255}.; TOPO_DOM 321 373 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 395 397 Lumenal. {ECO:0000255}.; TOPO_DOM 419 436 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 458 465 Lumenal. {ECO:0000255}.; TOPO_DOM 487 521 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 543 553 Lumenal. {ECO:0000255}.; TOPO_DOM 575 590 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 612 630 Lumenal. {ECO:0000255}.; TOPO_DOM 652 662 Cytoplasmic. {ECO:0000255}. FUNCTION: In the intracellular compartments, may function as a channel or small molecule transporter. {ECO:0000250}. SUBCELLULAR LOCATION: Endosome membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q0VBF2 TM52B_MOUSE Transmembrane protein 52B 186 20,312 Chain (1); Signal peptide (1); Transmembrane (1) TRANSMEM 44 64 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q8C581 TMM91_MOUSE Transmembrane protein 91 (Dispanin subfamily C member 3) (DSPC3) (Synapse differentiation-induced protein 3) 172 18,085 Chain (1); Topological domain (3); Transmembrane (2) TRANSMEM 98 118 Helical. {ECO:0000255}.; TRANSMEM 140 160 Helical. {ECO:0000255}. TOPO_DOM 1 97 Extracellular. {ECO:0000255}.; TOPO_DOM 119 139 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 161 172 Extracellular. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q3V0Q7 TMPSC_MOUSE Transmembrane protease serine 12 (EC 3.4.21.-) 336 36,916 Active site (3); Chain (1); Disulfide bond (4); Domain (1); Glycosylation (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 313 333 Helical. {ECO:0000255}. TOPO_DOM 19 312 Extracellular. {ECO:0000255}.; TOPO_DOM 334 336 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q9QZ47 TNNT3_MOUSE Troponin T, fast skeletal muscle (TnTf) (Fast skeletal muscle troponin T) (fTnT) 272 32,241 Alternative sequence (7); Chain (1); Initiator methionine (1); Modified residue (8); Natural variant (1); Sequence conflict (1) FUNCTION: Troponin T is the tropomyosin-binding subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity. {ECO:0000250}. TISSUE SPECIFICITY: Expressed predominantly in skeletal muscle. {ECO:0000269|PubMed:9249073}. +Q8C3K5 TMM72_MOUSE Transmembrane protein 72 275 30,372 Chain (1); Sequence conflict (7); Transmembrane (4) TRANSMEM 16 36 Helical. {ECO:0000255}.; TRANSMEM 41 61 Helical. {ECO:0000255}.; TRANSMEM 85 105 Helical. {ECO:0000255}.; TRANSMEM 108 128 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q920Q4 VPS16_MOUSE Vacuolar protein sorting-associated protein 16 homolog (mVPS16) 839 94,928 Alternative sequence (1); Chain (1); Modified residue (1); Mutagenesis (1); Region (1); Sequence conflict (8) FUNCTION: Plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport and autophagic pathways. Believed to act as a core component of the putative HOPS and CORVET endosomal tethering complexes which are proposed to be involved in the Rab5-to-Rab7 endosome conversion probably implicating MON1A/B, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion. The HOPS complex is proposed to be recruited to Rab7 on the late endosomal membrane and to regulate late endocytic, phagocytic and autophagic traffic towards lysosomes. The CORVET complex is proposed to function as a Rab5 effector to mediate early endosome fusion probably in specific endosome subpopulations. Required for recruitment of VPS33A to the HOPS complex. Required for fusion of endosomes and autophagosomes with lysosomes; the function is dependent on its association with VPS33A but not VPS33B. The function in autophagosome-lysosome fusion implicates STX17 but not UVRAG. {ECO:0000250|UniProtKB:Q9H269}. SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250|UniProtKB:Q9H269}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9H269}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9H269}. Lysosome membrane {ECO:0000250|UniProtKB:Q9H269}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9H269}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9H269}. Early endosome {ECO:0000250|UniProtKB:Q9H269, ECO:0000269|PubMed:21411634}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:21411634}. Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:Q9H269}. Note=Colocalizes with AP-3, clathrin, Rab5 and Rab7b (PubMed:21411634). Cytoplasmic, peripheral membrane protein associated with early endosomes and late endosomes/lysosomes. {ECO:0000250|UniProtKB:Q9H269, ECO:0000269|PubMed:21411634}. SUBUNIT: Core component of at least two putative endosomal tethering complexes, the homotypic fusion and vacuole protein sorting (HOPS) complex and the class C core vacuole/endosome tethering (CORVET) complex. Their common core is composed of the class C Vps proteins VPS11, VPS16, VPS18 and VPS33A, which in HOPS further associates with VPS39 and VPS41 and in CORVET with VPS8 and TGFBRAP1 (PubMed:25266290). Interacts with RAB5C (PubMed:25266290). Interacts with STX17, MON1B (By similarity). Associates with adaptor protein complex 3 (AP-3) and clathrin:AP-3 complexes (PubMed:21411634). {ECO:0000250|UniProtKB:Q9H269, ECO:0000269|PubMed:21411634, ECO:0000269|PubMed:25266290, ECO:0000305|PubMed:25266290}. +Q0VB26 TEX26_MOUSE Testis-expressed protein 26 296 34,527 Chain (1) +Q9DA77 TEX29_MOUSE Testis-expressed protein 29 186 20,894 Chain (1); Compositional bias (1); Topological domain (2); Transmembrane (1) TRANSMEM 57 77 Helical. {ECO:0000255}. TOPO_DOM 1 56 Extracellular. {ECO:0000255}.; TOPO_DOM 78 151 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q9D9J2 TEX33_MOUSE Testis-expressed protein 33 266 30,228 Chain (1) +Q3UK37 TEDC1_MOUSE Tubulin epsilon and delta complex protein 1 (Uncharacterized protein C14orf80 homolog) 420 46,797 Chain (1); Coiled coil (2); Compositional bias (1); Sequence conflict (8) FUNCTION: May play a role in counteracting perturbation of actin filaments, such as after treatment with the actin depolymerizing microbial metabolite Chivosazole F. {ECO:0000250|UniProtKB:Q86SX3}. +Q6GQV0 TEDC2_MOUSE Tubulin epsilon and delta complex protein 2 436 47,848 Alternative sequence (1); Chain (1); Modified residue (1) +Q3UNW5 TF2L1_MOUSE Transcription factor CP2-like protein 1 (CP2-related transcriptional repressor 1) (CRTR-1) 479 54,737 Chain (1); Region (3); Sequence conflict (10) FUNCTION: Transcription factor that facilitates establishment and maintenance of pluripotency in embryonic stem cells (ESCs) (PubMed:23942233, PubMed:26321140). With Klf2, acts as the major effector of self-renewal that mediates induction of pluripotency downstream of LIF/Stat3 and Wnt/beta-catenin signaling (PubMed:23942238, PubMed:23942233, PubMed:26321140). Required for normal duct development in the salivary gland and kidney (PubMed:17079272). Coordinates the development of the kidney collecting ducts intercalated (IC) and principal (PC) cells, which regulate acid-base and salt-water homeostasis, respectively (PubMed:28577314). Regulates the expression of IC genes including subunits B1 and D2 of the V-ATPase complex, Oxgr1, Ca12, Slc4a1, Aqp6 and IC-specific transcription factor Foxi1 (PubMed:28577314). Regulates also the expression of Jag1 and subsequent notch signaling in the collecting duct (PubMed:28577314). Jag1 initiates notch signaling in PCs but inhibits notch signaling in ICs (PubMed:28577314). Acts as a transcriptional suppressor that may suppress UBP1-mediated transcriptional activation (PubMed:11073954). Modulates the placental expression of CYP11A1 (By similarity). {ECO:0000250|UniProtKB:Q9NZI6, ECO:0000269|PubMed:11073954, ECO:0000269|PubMed:17079272, ECO:0000269|PubMed:23942233, ECO:0000269|PubMed:23942238, ECO:0000269|PubMed:26321140, ECO:0000269|PubMed:28577314}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28577314}. SUBUNIT: Forms homohexamers via its SAM-like domain (By similarity). Interacts with Mta1; which is indispensable for Tfcp2l1-mediated self-renewal-promoting effect and endoderm-inhibiting action (PubMed:28982712). {ECO:0000250|UniProtKB:Q9NZI6, ECO:0000269|PubMed:28982712}. DOMAIN: The CP2-like domain is required for direct DNA-binding (By similarity). The CP2-like domain is essential to maintain the undifferentiated state of embryonic stem cells (PubMed:28982712). {ECO:0000250|UniProtKB:Q9NZI6, ECO:0000269|PubMed:28982712}.; DOMAIN: The SAM-like domain is required for homohexamerization (By similarity). {ECO:0000250|UniProtKB:Q9NZI6}. TISSUE SPECIFICITY: Highly expressed in placenta, testis, small intestine, kidney and stomach (PubMed:11073954, PubMed:17079272). Low levels of expression in lung, mesenteric lymph nodes, muscle, ovary, and thymus (PubMed:11073954). No expression was detected in brain, heart, liver, and spleen (PubMed:11073954). Expressed in eccrine glands in the palm (PubMed:11073954). Expression is prominent in both kidney collecting ducts intercalated (IC) and principal (PC) cells (PubMed:28577314). Also expressed in the thick limb of Henle and connecting segments of the nephron (PubMed:28577314). {ECO:0000269|PubMed:11073954, ECO:0000269|PubMed:17079272, ECO:0000269|PubMed:28577314}. +P0CAX8 TGAP1_MOUSE T-cell activation GTPase-activating protein 1 505 55,747 Chain (1); Sequence conflict (3) +Q08189 TGM3_MOUSE Protein-glutamine gamma-glutamyltransferase E (EC 2.3.2.13) (Transglutaminase E) (TG(E)) (TGE) (TGase E) (Transglutaminase-3) (TGase-3) [Cleaved into: Protein-glutamine gamma-glutamyltransferase E 50 kDa catalytic chain; Protein-glutamine gamma-glutamyltransferase E 27 kDa non-catalytic chain] 693 77,309 Active site (3); Chain (2); Frameshift (1); Metal binding (14); Modified residue (2); Sequence conflict (8); Site (1) FUNCTION: Catalyzes the calcium-dependent formation of isopeptide cross-links between glutamine and lysine residues in various proteins, as well as the conjugation of polyamines to proteins. Involved in the formation of the cornified envelope (CE), a specialized component consisting of covalent cross-links of proteins beneath the plasma membrane of terminally differentiated keratinocytes. Catalyzes small proline-rich proteins (SPRR1 and SPRR2) and LOR cross-linking to form small interchain oligomers, which are further cross-linked by TGM1 onto the growing CE scaffold (By similarity). In hair follicles, involved in cross-linking structural proteins to hardening the inner root sheath. {ECO:0000250}. PTM: Activated by proteolytic processing. In vitro activation is commonly achieved by cleavage with dispase, a neutral bacterial protease. Physiological activation may be catalyzed by CTSL and, to a lesser extent, by CTSS (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q08188}. SUBUNIT: Consists of two polypeptide chains, which are synthesized as a precursor form of a single polypeptide. TISSUE SPECIFICITY: Expressed in skin and stomach and, at lower levels, in testis, kidney and spleen (at protein level). On the basis of its catalytic activity, detected in the epidermis, around the granular and spinous layers but not in the outermost cornified layers. In hair follicles, mainly located in the medulla and the hair cortex. {ECO:0000269|PubMed:11331204, ECO:0000269|PubMed:20716179}. +P40630 TFAM_MOUSE Transcription factor A, mitochondrial (mtTFA) (Testis-specific high mobility group protein) (TS-HMG) 243 27,988 Alternative sequence (2); Chain (1); DNA binding (2); Erroneous initiation (1); Frameshift (1); Modified residue (7); Sequence conflict (1); Site (2); Transit peptide (1) FUNCTION: Isoform Mitochondrial binds to the mitochondrial light strand promoter and functions in mitochondrial transcription regulation. Required for accurate and efficient promoter recognition by the mitochondrial RNA polymerase. Promotes transcription initiation from the HSP1 and the light strand promoter by binding immediately upstream of transcriptional start sites. Is able to unwind DNA. Bends the mitochondrial light strand promoter DNA into a U-turn shape via its HMG boxes. Required for maintenance of normal levels of mitochondrial DNA. May play a role in organizing and compacting mitochondrial DNA. Isoform Nuclear may also function as a transcriptional activator or may have a structural role in the compaction of nuclear DNA during spermatogenesis. {ECO:0000269|PubMed:17581862, ECO:0000269|PubMed:8673128, ECO:0000269|PubMed:9500544}. PTM: Phosphorylation by PKA within the HMG box 1 impairs DNA binding and promotes degradation by the AAA+ Lon protease. {ECO:0000250}. SUBCELLULAR LOCATION: Isoform Mitochondrial: Mitochondrion {ECO:0000250|UniProtKB:Q00059}. Mitochondrion matrix, mitochondrion nucleoid {ECO:0000250|UniProtKB:Q00059}.; SUBCELLULAR LOCATION: Isoform Nuclear: Nucleus. SUBUNIT: Monomer; binds DNA as a monomer. Upon metabolic stress, forms a complex composed of FOXO3, SIRT3, TFAM and POLRMT. Interacts with TFB1M and TFB2M. Interacts with CLPX; this enhances DNA-binding. {ECO:0000250|UniProtKB:Q00059}. DOMAIN: Binds DNA via its HMG boxes. When bound to the mitochondrial light strand promoter, bends DNA into a U-turn shape, each HMG box bending the DNA by 90 degrees (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: The mitochondrial isoform is widely expressed while the nuclear isoform is testis-specific. +Q4JK59 TET2_MOUSE Methylcytosine dioxygenase TET2 (EC 1.14.11.n2) (Protein Ayu17-449) 1912 212,130 Alternative sequence (2); Binding site (4); Chain (1); Compositional bias (4); Erroneous initiation (6); Frameshift (2); Metal binding (14); Modified residue (5); Mutagenesis (7); Region (3); Sequence conflict (14) FUNCTION: Dioxygenase that catalyzes the conversion of the modified genomic base 5-methylcytosine (5mC) into 5-hydroxymethylcytosine (5hmC) and plays a key role in active DNA demethylation. Has a preference for 5-hydroxymethylcytosine in CpG motifs. Also mediates subsequent conversion of 5hmC into 5-formylcytosine (5fC), and conversion of 5fC to 5-carboxylcytosine (5caC). Conversion of 5mC into 5hmC, 5fC and 5caC probably constitutes the first step in cytosine demethylation. Methylation at the C5 position of cytosine bases is an epigenetic modification of the mammalian genome which plays an important role in transcriptional regulation. In addition to its role in DNA demethylation, also involved in the recruitment of the O-GlcNAc transferase OGT to CpG-rich transcription start sites of active genes, thereby promoting histone H2B GlcNAcylation by OGT. {ECO:0000269|PubMed:20639862, ECO:0000269|PubMed:21057493, ECO:0000269|PubMed:21778364, ECO:0000269|PubMed:21817016, ECO:0000269|PubMed:23352454, ECO:0000269|PubMed:23353889}. PTM: May be glycosylated. It is unclear whether interaction with OGT leads to GlcNAcylation. According to a report, it is GlcNAcylated by OGT (PubMed:23352454). In contrast, another group reports no GlcNAcylation by OGT in human ortholog. {ECO:0000269|PubMed:23352454}. SUBUNIT: Interacts with HCFC1 (By similarity). Interacts with OGT. {ECO:0000250, ECO:0000269|PubMed:23352454}. TISSUE SPECIFICITY: Highly expressed in the brain, kidney, heart, lung, muscle and stomach. Present in embryonic stem cells (ES cells). {ECO:0000269|PubMed:16722336, ECO:0000269|PubMed:20639862}. +Q923W1 TGS1_MOUSE Trimethylguanosine synthase (EC 2.1.1.-) (Nuclear receptor coactivator 6-interacting protein) (PRIP-interacting protein with methyltransferase motif) (PIMT) (PIPMT) 853 96,790 Binding site (1); Chain (1); Compositional bias (1); Modified residue (10); Sequence conflict (2) FUNCTION: Catalyzes the 2 serial methylation steps for the conversion of the 7-monomethylguanosine (m(7)G) caps of snRNAs and snoRNAs to a 2,2,7-trimethylguanosine (m(2,2,7)G) cap structure. The enzyme is specific for guanine, and N7 methylation must precede N2 methylation. Hypermethylation of the m7G cap of U snRNAs leads to their concentration in nuclear foci, their colocalization with coilin and the formation of canonical Cajal bodies (CBs). Plays a role in transcriptional regulation (By similarity). {ECO:0000250, ECO:0000269|PubMed:11517327}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96RS0}. Nucleus, Cajal body {ECO:0000269|PubMed:11517327}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q96RS0}. SUBUNIT: May form homooligomers. Interacts with CREBBP/CBP, EED/WAIT1, EP300/P300, NCOA6/PRIP, PPARBP/PBP and SMN (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:11517327}. +Q9JMA2 TGT_MOUSE Queuine tRNA-ribosyltransferase catalytic subunit 1 (EC 2.4.2.29) (Guanine insertion enzyme) (tRNA-guanine transglycosylase) 403 44,093 Active site (2); Binding site (3); Chain (1); Erroneous initiation (1); Frameshift (1); Initiator methionine (1); Metal binding (4); Modified residue (2); Region (3) FUNCTION: Catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine) (PubMed:19414587). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming queuine, allowing a nucleophilic attack on the C1' of the ribose to form the product (By similarity). {ECO:0000255|HAMAP-Rule:MF_03218, ECO:0000269|PubMed:19414587}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03218, ECO:0000269|PubMed:19414587}. Mitochondrion outer membrane {ECO:0000255|HAMAP-Rule:MF_03218, ECO:0000269|PubMed:19414587}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03218, ECO:0000305|PubMed:19414587}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03218, ECO:0000269|PubMed:19414587}. Nucleus {ECO:0000269|PubMed:19414587}. Note=Weakly associates with mitochondria, possibly via QTRT2. {ECO:0000255|HAMAP-Rule:MF_03218, ECO:0000269|PubMed:19414587}. SUBUNIT: Heterodimer of a catalytic subunit QTRT1 and an accessory subunit QTRT2. {ECO:0000255|HAMAP-Rule:MF_03218, ECO:0000269|PubMed:19414587}. TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver, ling, skeletal muscle, spleen and testis. {ECO:0000269|PubMed:19414587}. +Q91XD6 VPS36_MOUSE Vacuolar protein-sorting-associated protein 36 (ESCRT-II complex subunit VPS36) 386 43,736 Beta strand (7); Chain (1); Coiled coil (1); Domain (2); Helix (2); Turn (1) FUNCTION: Component of the ESCRT-II complex (endosomal sorting complex required for transport II), which is required for multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs. The MVB pathway mediates delivery of transmembrane proteins into the lumen of the lysosome for degradation. The ESCRT-II complex is probably involved in the recruitment of the ESCRT-III complex. Its ability to bind ubiquitin probably plays a role in endosomal sorting of ubiquitinated cargo proteins by ESCRT complexes. The ESCRT-II complex may also play a role in transcription regulation, possibly via its interaction with ELL. Binds phosphoinosides such as PtdIns(3,4,5)P3. {ECO:0000250|UniProtKB:Q86VN1, ECO:0000269|PubMed:15755741}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Endosome {ECO:0000250}. Late endosome {ECO:0000269|PubMed:15755741}. Membrane {ECO:0000250}. Nucleus {ECO:0000250}. Note=Colocalizes with ubiquitinated proteins on late endosomes. Recruited to the endosome membrane to participate in vesicle formation. {ECO:0000269|PubMed:15755741}. SUBUNIT: Component of a complex at least composed of ELL, SNF8/EAP30, VPS25/EAP20 and VPS36/EAP45 (By similarity). Component of the endosomal sorting complex required for transport II (ESCRT-II), composed of SNF8, VPS36 and two copies of VPS25 (By similarity). Interacts with VPS25, SNF8, TSG101 and CHMP6 (By similarity). Interacts (via GLUE domain) with ubiquitin (PubMed:15755741). Interacts with RILPL1 (via the C-terminal domain); which recruits ESCRT-II to the endosome membranes (By similarity). Interacts with ECPAS (By similarity). {ECO:0000250|UniProtKB:P0C0A2, ECO:0000250|UniProtKB:Q86VN1, ECO:0000269|PubMed:15755741}. DOMAIN: The GLUE domain (GRAM-like ubiquitin-binding in EAP45) mediates binding to ubiquitin and phosphoinosides. {ECO:0000269|PubMed:15755741}. +Q8VEJ9 VPS4A_MOUSE Vacuolar protein sorting-associated protein 4A (EC 3.6.4.6) 437 48,907 Chain (1); Coiled coil (1); Domain (1); Modified residue (3); Mutagenesis (1); Nucleotide binding (1) FUNCTION: Involved in late steps of the endosomal multivesicular bodies (MVB) pathway. Recognizes membrane-associated ESCRT-III assemblies and catalyzes their disassembly, possibly in combination with membrane fission. Redistributes the ESCRT-III components to the cytoplasm for further rounds of MVB sorting. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. In conjunction with the ESCRT machinery also appears to function in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis. Involved in cytokinesis: retained at the midbody by ZFYVE19/ANCHR and CHMP4C until abscission checkpoint signaling is terminated at late cytokinesis. It is then released following dephosphorylation of CHMP4C, leading to abscission. VPS4A/B are required for the exosomal release of SDCBP, CD63 and syndecan (By similarity). {ECO:0000250|UniProtKB:Q9UN37}. SUBCELLULAR LOCATION: Prevacuolar compartment membrane {ECO:0000269|PubMed:12594041}; Peripheral membrane protein {ECO:0000269|PubMed:12594041}. Late endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Midbody {ECO:0000250}. Note=Membrane-associated in the prevacuolar endosomal compartment. Localizes to the midbody of dividing cells. Localizes to the midbody of dividing cells, interaction with ZFYVE19/ANCHR mediates retention at midbody. Localized in two distinct rings on either side of the Flemming body (By similarity). {ECO:0000250}. SUBUNIT: Proposed to be monomeric or homodimeric in nucleotide-free form and to oligomerize upon binding to ATP to form two stacked hexameric or heptameric rings with a central pore through which ESCRT-III substrates are translocated in an ATP-dependent manner. Interacts with CHMP1A, CHMP1B, CHMP2A, CHMP2B, CHMP3, CHMP4A, CHMP4B, CHMP4C and CHMP6. Interacts with VPS4B; the interaction suggests a heteromeric assembly with VPS4B. Interacts with SPAST. Interacts with IST1. Interacts with ZFYVE19/ANCHR; leading to retain it at midbody (By similarity). {ECO:0000250}. DOMAIN: The MIT domain serves as an adapter for ESCRT-III proteins. It forms an asymmetric three-helix bundle that binds amphipathic MIM (MIT interacting motif) helices along the groove between MIT helices 2 and 3 present in a subset of ESCRT-III proteins thus establishing the canonical MIM-MIT interaction. In an extended conformation along the groove between helices 1 and 3, also binds to a type-2 MIT interacting motif (MIM2) (By similarity). {ECO:0000250|UniProtKB:O75351}. TISSUE SPECIFICITY: Highly expressed in testis and moderately in heart and brain. Not detected in spleen, lung, liver, skeletal muscle or kidney. {ECO:0000269|PubMed:12594041}. +Q8BJ25 THAP3_MOUSE THAP domain-containing protein 3 218 24,627 Chain (1); Modified residue (1); Motif (1); Sequence conflict (1); Zinc finger (1) FUNCTION: Component of a THAP1/THAP3-HCFC1-OGT complex that is required for the regulation of the transcriptional activity of RRM1. {ECO:0000250}. SUBUNIT: Component of a THAP1/THAP3-HCFC1-OGT complex that contains at least, either THAP1 or THAP3, HCFC1 and OGT. Interacts directly with OGT and HCFC1 (via its HBM) (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highest levels in heart, liver and kidney. Lower levels in brain and lung. {ECO:0000269|PubMed:20200153}. +P36423 THAS_MOUSE Thromboxane-A synthase (TS) (TXA synthase) (TXS) (EC 5.3.99.5) (Cytochrome P450 5A1) 533 60,391 Chain (1); Metal binding (1); Sequence conflict (1); Topological domain (5); Transmembrane (4) TRANSMEM 11 31 Helical. {ECO:0000255}.; TRANSMEM 76 96 Helical. {ECO:0000255}.; TRANSMEM 224 244 Helical. {ECO:0000255}.; TRANSMEM 336 356 Helical. {ECO:0000255}. TOPO_DOM 1 10 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 32 75 Lumenal. {ECO:0000255}.; TOPO_DOM 97 223 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 245 335 Lumenal. {ECO:0000255}.; TOPO_DOM 357 533 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. +A8C756 THADA_MOUSE Thyroid adenoma-associated protein homolog 1938 217,289 Alternative sequence (5); Chain (1); Coiled coil (1); Compositional bias (3); Erroneous termination (1); Frameshift (1); Modified residue (3); Sequence caution (1); Sequence conflict (4) +P61939 THBG_MOUSE Thyroxine-binding globulin (Serpin A7) (T4-binding globulin) 418 47,052 Binding site (2); Chain (1); Glycosylation (6); Signal peptide (1) FUNCTION: Major thyroid hormone transport protein in serum. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +Q80ZW2 THEM6_MOUSE Protein THEM6 207 23,803 Chain (1); Glycosylation (1); Modified residue (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q4FZG7 TI8AB_MOUSE Putative mitochondrial import inner membrane translocase subunit Tim8 A-B 97 11,283 Chain (1); Disulfide bond (2); Motif (1) FUNCTION: Putative mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Intermembrane side {ECO:0000250}. SUBUNIT: Heterohexamer; possibly composed of 3 copies of TIMM8AB and 3 copies of TIMM13. {ECO:0000250}. DOMAIN: The twin CX3C motif contains 4 conserved Cys residues that form 2 disulfide bonds in the mitochondrial intermembrane space. However, during the transit of Timm8ab from cytoplasm into mitochondrion, the Cys residues probably coordinate zinc, thereby preventing folding and allowing its transfer across mitochondrial outer membrane (By similarity). {ECO:0000250}. +Q60610 TIAM1_MOUSE T-lymphoma invasion and metastasis-inducing protein 1 (TIAM-1) 1591 177,533 Beta strand (8); Chain (1); Compositional bias (2); Domain (5); Helix (21); Initiator methionine (1); Lipidation (1); Modified residue (7); Mutagenesis (3); Turn (4) FUNCTION: Modulates the activity of RHO-like proteins and connects extracellular signals to cytoskeletal activities. Acts as a GDP-dissociation stimulator protein that stimulates the GDP-GTP exchange activity of RHO-like GTPases and activates them. Activates RAC1, CDC42, and to a lesser extent RHOA. Required for normal cell adhesion and cell migration (By similarity). Affects invasiveness of T-lymphoma cells. {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction {ECO:0000269|PubMed:17339315}. Cell membrane {ECO:0000269|PubMed:17339315}; Peripheral membrane protein {ECO:0000269|PubMed:17339315}; Cytoplasmic side {ECO:0000269|PubMed:17339315}. Note=Presence of KRIT1, CDH5 and RAP1B is required for its localization to the cell junction (By similarity). Detected at the boundary between cells with actin-rich protrusions. {ECO:0000250}. SUBUNIT: Component of the Par polarity complex, composed of at least phosphorylated PRKCZ, PARD3 and TIAM1 (By similarity). Interacts with BAIAP2. Interacts (via PDZ domain) with CNTNAP4, SDC1 and SDC3 (via C-terminus) (By similarity). Interacts with CD44, PARD3 and MAPK8IP2. Interacts with EPHA8; regulates clathrin-mediated endocytosis of EPHA8. Interacts with NTRK2; mediates the activation of RAC1 by BDNF. {ECO:0000250, ECO:0000269|PubMed:11130063, ECO:0000269|PubMed:16801538, ECO:0000269|PubMed:19893486, ECO:0000269|PubMed:20496116}. DOMAIN: The first PH domain mediates interaction with membranes enriched in phosphoinositides. {ECO:0000269|PubMed:17339315}. TISSUE SPECIFICITY: Highly expressed in brain and testis and at low or moderate levels in almost all other normal tissues. Found in virtually all analyzed tumor cell lines including B- and T-lymphomas, neuroblastomas, melanomas and carcinomas. +Q9WTQ8 TIM23_MOUSE Mitochondrial import inner membrane translocase subunit Tim23 209 21,978 Chain (1); Transmembrane (3) TRANSMEM 73 93 Helical. {ECO:0000255}.; TRANSMEM 125 145 Helical. {ECO:0000255}.; TRANSMEM 181 197 Helical. {ECO:0000255}. FUNCTION: Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:O14925}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Component of the TIM23 complex at least composed of TIMM23, TIMM17 (TIMM17A or TIMM17B) and TIMM50; within this complex, directly interacts with TIMM50. The complex interacts with the TIMM44 component of the PAM complex and with DNAJC15. {ECO:0000250}. +Q62288 TICN1_MOUSE Testican-1 (Protein SPOCK) 442 49,551 Chain (1); Disulfide bond (8); Domain (2); Glycosylation (2); Sequence conflict (3); Signal peptide (1) FUNCTION: May play a role in cell-cell and cell-matrix interactions. May contribute to various neuronal mechanisms in the central nervous system. PTM: Contains chondroitin sulfate and heparan sulfate O-linked oligosaccharides. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. TISSUE SPECIFICITY: Predominantly expressed in the postsynaptic area of pyramidal neurons. +P70371 TERF1_MOUSE Telomeric repeat-binding factor 1 (TTAGGG repeat-binding factor 1) 421 48,224 Chain (1); Compositional bias (1); Cross-link (1); DNA binding (1); Domain (1); Initiator methionine (1); Modified residue (2); Motif (1); Region (2); Sequence conflict (1) FUNCTION: Binds the telomeric double-stranded 5'-TTAGGG-3' repeat and negatively regulates telomere length. Involved in the regulation of the mitotic spindle. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded 5'-TTAGGG-3' repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways. {ECO:0000269|PubMed:24413433}. PTM: Phosphorylated preferentially on Ser-219 in an ATM-dependent manner in response to ionizing DNA damage. {ECO:0000250}.; PTM: ADP-ribosylation by TNKS1 or TNKS2 diminishes its ability to bind to telomeric DNA. {ECO:0000250}.; PTM: Ubiquitinated by RLIM/RNF12, leading to its degradation by the proteasome. Ubiquitinated by a SCF (SKP1-CUL1-F-box protein) ubiquitin-protein ligase complex, leading to its degradation by the proteasome (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625}. Chromosome, telomere {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Colocalizes with telomeric DNA in interphase and prophase cells. Telomeric localization decreases in metaphase, anaphase and telophase. Associates with the mitotic spindle (By similarity). {ECO:0000250}. SUBUNIT: Homodimer; can contain both isoforms. Found in a complex with POT1; TINF2 and TNKS1. Interacts with ATM, TINF2, TNKS1, TNKS2, PINX1, NEK2 and MAPRE1. Component of the shelterin complex (telosome) composed of TERF1, TERF2, TINF2, TERF2IP ACD and POT1. Interacts with RLIM (via N-terminus). Interacts with FBXO4. Interaction with TINF2 protects against interaction with FBXO4 and subsequent polyubiquitination and proteasomal degradation (By similarity). Interacts with GNL3L; this interaction promotes homodimerization. Interacts with TIN2. Interactions with GNL3L and TIN2 are mutually exclusive. Interacts with RTEL1 (By similarity). Interacts with CCDC79/TERB1. {ECO:0000250, ECO:0000269|PubMed:19487455, ECO:0000269|PubMed:24413433}. DOMAIN: The acidic N-terminal domain binds to the ankyrin repeats of TNKS1 and TNKS2. The C-terminal domain binds microtubules (By similarity). {ECO:0000250}.; DOMAIN: The TRFH dimerization region mediates the interaction with TINF2. {ECO:0000250}.; DOMAIN: The HTH domain is an independent structural unit and mediates binding to telomeric DNA. {ECO:0000250}. +Q2MV57 TECT2_MOUSE Tectonic-2 700 77,111 Alternative sequence (1); Chain (1); Compositional bias (1); Glycosylation (5); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 666 682 Helical. {ECO:0000255}. TOPO_DOM 26 665 Extracellular. {ECO:0000255}.; TOPO_DOM 683 700 Cytoplasmic. {ECO:0000255}. FUNCTION: Component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. Required for hedgehog signaling transduction. {ECO:0000269|PubMed:21565611, ECO:0000269|PubMed:21725307, ECO:0000269|PubMed:22179047}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:21725307}. Note=Localizes at the transition zone, a region between the basal body and the ciliary axoneme. SUBUNIT: Part of the tectonic-like complex (also named B9 complex). {ECO:0000269|PubMed:21725307, ECO:0000269|PubMed:22179047}. TISSUE SPECIFICITY: Significant expression is observed in brain, kidney and eye. {ECO:0000269|PubMed:21462283}. +Q8R2M0 TEAN2_MOUSE Transcription elongation factor A N-terminal and central domain-containing protein 2 207 24,200 Chain (1); Domain (2); Frameshift (1); Modified residue (1); Sequence conflict (1) SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00649, ECO:0000255|PROSITE-ProRule:PRU00651}. +Q14AT2 TEX11_MOUSE Testis-expressed protein 11 (Protein ZIP4 homolog) (ZIP4H) 947 109,624 Alternative sequence (2); Chain (1); Sequence conflict (1) FUNCTION: Regulator of crossing-over during meiosis. Involved in initiation and/or maintenance of chromosome synapsis and formation of crossovers. {ECO:0000269|PubMed:18316482, ECO:0000269|PubMed:18369460}. SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:18316482, ECO:0000269|PubMed:18369460}. Note=Forms arrays of discrete foci along synaptonemal complexes in spermatocytes and fetal oocytes. SUBUNIT: Interacts with SYCP2 (PubMed:18316482). Interacts with PBXIP1; may prevent interaction between PBXIP1 and ESR2 (PubMed:22383461). Interacts with SHOC1 (By similarity). {ECO:0000250|UniProtKB:Q8IYF3, ECO:0000269|PubMed:18316482, ECO:0000269|PubMed:22383461}. TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:11279525, ECO:0000269|PubMed:18316482, ECO:0000269|PubMed:18369460}. +Q8K284 TF3C1_MOUSE General transcription factor 3C polypeptide 1 (TF3C-alpha) (TFIIIC box B-binding subunit) (Transcription factor IIIC 220 kDa subunit) (TFIIIC 220 kDa subunit) (TFIIIC220) (Transcription factor IIIC subunit alpha) 2101 237,476 Alternative sequence (4); Chain (1); Compositional bias (3); Cross-link (3); Erroneous initiation (1); Modified residue (5); Sequence conflict (1) FUNCTION: Required for RNA polymerase III-mediated transcription. Component of TFIIIC that initiates transcription complex assembly on tRNA and is required for transcription of 5S rRNA and other stable nuclear and cytoplasmic RNAs. Binds to the box B promoter element (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Part of the TFIIIC subcomplex TFIIIC2, consisting of six subunits, GTF3C1, GTF3C2, GTF3C3, GTF3C4, GTF3C5 and GTF3C6. Interacts with IGHMBP2. {ECO:0000250}. +Q8VCT9 TESK2_MOUSE Dual specificity testis-specific protein kinase 2 (EC 2.7.12.1) (Testicular protein kinase 2) 570 63,470 Active site (1); Binding site (1); Chain (1); Domain (1); Modified residue (4); Nucleotide binding (1) FUNCTION: Dual specificity protein kinase activity catalyzing autophosphorylation and phosphorylation of exogenous substrates on both serine/threonine and tyrosine residues. Phosphorylates cofilin at 'Ser-3'. May play an important role in spermatogenesis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +P48030 TGFA_MOUSE Protransforming growth factor alpha [Cleaved into: Transforming growth factor alpha (TGF-alpha) (EGF-like TGF) (ETGF) (TGF type 1)] 159 17,018 Chain (2); Disulfide bond (3); Domain (1); Glycosylation (1); Lipidation (2); Propeptide (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 98 123 Helical. {ECO:0000255}. TOPO_DOM 24 97 Extracellular. {ECO:0000255}.; TOPO_DOM 124 159 Cytoplasmic. {ECO:0000255}. FUNCTION: TGF alpha is a mitogenic polypeptide that is able to bind to the EGF receptor/EGFR and to act synergistically with TGF beta to promote anchorage-independent cell proliferation in soft agar. SUBCELLULAR LOCATION: Transforming growth factor alpha: Secreted, extracellular space.; SUBCELLULAR LOCATION: Protransforming growth factor alpha: Cell membrane; Single-pass type I membrane protein. SUBUNIT: Interacts with the PDZ domains of SDCBP and SNTA1. The interaction with SDCBP, is required for the targeting to the cell surface. In the endoplasmic reticulum, in its immature form (i.e. with a prosegment and lacking full N-glycosylation), interacts with CNIH. In the Golgi apparatus, may form a complex with CNIH and GORASP2. Interacts (via cytoplasmic C-terminal domain) with NKD2 (By similarity). Interacts with MAGI3. {ECO:0000250, ECO:0000269|PubMed:15652357}. +Q62314 TGON2_MOUSE Trans-Golgi network integral membrane protein 2 (TGN38B) 363 38,821 Chain (1); Glycosylation (1); Modified residue (3); Motif (1); Region (1); Repeat (7); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 309 329 Helical. {ECO:0000255}. TOPO_DOM 18 308 Extracellular. {ECO:0000255}.; TOPO_DOM 330 363 Cytoplasmic. {ECO:0000255}. FUNCTION: May be involved in regulating membrane traffic to and from trans-Golgi network. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Primarily in trans-Golgi network. Cycles between the trans-Golgi network and the cell surface returning via endosomes (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. +Q8C0Y1 TGIF2_MOUSE Homeobox protein TGIF2 (5'-TG-3'-interacting factor 2) (TGF-beta-induced transcription factor 2) (TGFB-induced factor 2) 237 25,933 Chain (1); DNA binding (1); Modified residue (2); Region (1) FUNCTION: Transcriptional repressor, which probably repress transcription by binding directly the 5'-CTGTCAA-3' DNA sequence or by interacting with TGF-beta activated SMAD proteins. Probably represses transcription via the recruitment of histone deacetylase proteins (By similarity). {ECO:0000250}. PTM: The C-terminal part is phosphorylated in response to EGF signaling by the Ras/MAPK pathway. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. Note=Excluded from nucleoli. {ECO:0000250}. SUBUNIT: Interacts with the transcriptional modulator SMAD3 and the histone deacetylase HDAC1. {ECO:0000250}. +Q08423 TFF1_MOUSE Trefoil factor 1 (Protein pS2) 87 9,670 Chain (1); Compositional bias (1); Disulfide bond (3); Domain (1); Modified residue (1); Signal peptide (1) FUNCTION: Stabilizer of the mucous gel overlying the gastrointestinal mucosa that provides a physical barrier against various noxious agents. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Strong expression found in normal gastric mucosa. Not detected in the small or large intestine nor in normal mammary gland. +Q6PEV3 WIPF2_MOUSE WAS/WASL-interacting protein family member 2 (WASP-interacting protein-related protein) (WIP-related protein) 440 46,297 Chain (1); Compositional bias (9); Domain (1); Modified residue (1); Region (1) FUNCTION: Plays an active role in the formation of cell surface protrusions downstream of activated PDGFB receptors. Plays an important role in actin-microspike formation through cooperation with WASL. May cooperate with WASP and WASL to induce mobilization and reorganization of the actin filament system (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Note=Localized to stress fibers and bundles of actin filaments. {ECO:0000250}. SUBUNIT: Interacts with WASL and WASP, and this interaction results in cytoplasmic relocation of these two proteins along actin filaments. Interacts with NCK2 resulting in the localization to sites of focal adhesions (By similarity). {ECO:0000250}. +Q8R3N6 THOC1_MOUSE THO complex subunit 1 (Tho1) (Nuclear matrix protein p84) 657 75,436 Chain (1); Cross-link (5); Domain (1); Modified residue (8); Motif (1) FUNCTION: Required for efficient export of polyadenylated RNA. Acts as component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and which specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NFX1 pathway. Regulates transcriptional elongation of a subset of genes. Involved in genome stability by preventing co-transcriptional R-loop formation (By similarity). {ECO:0000250}.; FUNCTION: Participates in an apoptotic pathway which is characterized by activation of caspase-6, increases in the expression of BAK1 and BCL2L1 and activation of NF-kappa-B. This pathway does not require p53/TP53, nor does the presence of p53/TP53 affect the efficiency of cell killing. Activates a G2/M cell cycle checkpoint prior to the onset of apoptosis. Apoptosis is inhibited by association with RB1 (By similarity). Essential for early embryonic development. Required for normal gene expression during postnatal testis development. {ECO:0000250, ECO:0000269|PubMed:16705185, ECO:0000269|PubMed:19307311}. PTM: Expression is altered specifically during apoptosis and is accompanied by the appearance of novel forms with smaller apparent molecular mass. {ECO:0000250}.; PTM: Polyubiquitinated, leading to proteasomal degradation; probably involves NEDD4. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000269|PubMed:16705185}. Nucleus matrix {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Can shuttle between the nucleus and cytoplasm. Nuclear localization is required for induction of apoptotic cell death. Translocates to the cytoplasm during the early phase of apoptosis execution (By similarity). {ECO:0000250}. SUBUNIT: Component of the THO complex, which is composed of THOC1, THOC2, THOC3, THOC5, THOC6 and THOC7; together with at least ALYREF/THOC4, DDX39B, SARNP/CIP29 and CHTOP, THO forms the transcription/export (TREX) complex which seems to have a dynamic structure involving ATP-dependent remodeling. Binds to the hypophosphorylated form of RB1. Interacts with THOC2, DDX39B and RNA polymerase II (By similarity). Interacts with THOC5 (PubMed:16909111). Interacts with LUZP4 (By similarity). {ECO:0000250|UniProtKB:Q96FV9, ECO:0000269|PubMed:16909111}. DOMAIN: An intact death domain is needed for apoptosis. {ECO:0000250}. +Q80W22 THNS2_MOUSE Threonine synthase-like 2 (TSH2) (mTSH2) (EC 4.2.3.-) 483 54,188 Chain (1); Modified residue (1); Sequence conflict (2) FUNCTION: Acts as a catabolic phospho-lyase on both gamma- and beta-phosphorylated substrates. Degrades O-phospho-threonine (PThr) to alpha-ketobutyrate, ammonia and phosphate. Also degrades O-phospho-homoserine (PHS), but this is not its physiological substrate. {ECO:0000269|PubMed:17034760}. +O08583 THOC4_MOUSE THO complex subunit 4 (Tho4) (Ally of AML-1 and LEF-1) (Aly/REF export factor) (REF1-I) (RNA and export factor-binding protein 1) (Transcriptional coactivator Aly/REF) 255 26,940 Alternative sequence (1); Beta strand (4); Chain (1); Compositional bias (1); Domain (1); Helix (2); Initiator methionine (1); Modified residue (20); Region (1) FUNCTION: Export adapter involved in nuclear export of spliced and unspliced mRNA. Binds mRNA which is thought to be transferred to the NXF1-NXT1 heterodimer for export (TAP/NFX1 pathway). Component of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm. TREX recruitment occurs via an interaction between ALYREF/THOC4 and the cap-binding protein NCBP1. Required for TREX complex assembly and for linking DDX39B to the cap-binding complex (CBC). In conjunction with THOC5 functions in NXF1-NXT1 mediated nuclear export of HSP70 mRNA; both proteins enhance the RNA binding activity of NXF1 and are required for NXF1 localization to the nuclear rim. Involved in the nuclear export of intronless mRNA; proposed to be recruited to intronless mRNA by ATP-bound DDX39B. Involved in transcription elongation and genome stability.; FUNCTION: Acts as chaperone and promotes the dimerization of transcription factors containing basic leucine zipper (bZIP) domains and thereby promotes transcriptional activation. PTM: Arg-50 and Arg-203 are dimethylated, probably to asymmetric dimethylarginine. Arginine methylation reduces RNA binding (By similarity). {ECO:0000250}.; PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9119228}. Nucleus speckle {ECO:0000250|UniProtKB:Q86V81}. Cytoplasm {ECO:0000269|PubMed:9119228}. Note=Colocalizes with the core EJC, ALYREF/THOC4, NXF1 and DDX39B in the nucleus and nuclear speckles. Localizes to regions surrounding nuclear speckles known as perispeckles in which TREX complex assembly seems to occur. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. {ECO:0000250|UniProtKB:Q86V81}. SUBUNIT: Homomultimer (By similarity). Is part of several complexes involved in mRNA processing and export (By similarity). Component of the transcription/export (TREX) complex at least composed of ALYREF/THOC4, DDX39B, SARNP/CIP29, CHTOP and the THO subcomplex; TREX seems to have a dynamic structure involving ATP-dependent remodeling; in the complex interacts (via C-terminus) directly with DDX39B and interacts directly with THOC1 and THOC2 (By similarity). Found in mRNA splicing-dependent exon junction complexes (EJC) (By similarity). Identified in the spliceosome C complex (By similarity). Found in a mRNP complex with UPF3A and UPF3B (By similarity). Interacts with RBM8A, NCBP1, THOC5, LEF1, RUNX1, EIF4A3, RNPS1, SRRM1, IWS1 and EXOSC1 (By similarity). Interacts with RBM15B. Interacts with NXF1; the interaction is direct (PubMed:10786854). {ECO:0000250|UniProtKB:Q86V81, ECO:0000269|PubMed:10786854}. TISSUE SPECIFICITY: Highly expressed in heart, brain, spleen, lung, liver, skeletal muscle, kidney and testis. {ECO:0000269|PubMed:9119228}. +Q8BKT7 THOC5_MOUSE THO complex subunit 5 homolog (Fms-interacting protein) (FMIP) 683 78,686 Chain (1); Cross-link (1); Initiator methionine (1); Modified residue (8); Motif (1); Mutagenesis (3); Region (2); Sequence conflict (2) FUNCTION: Acts as component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and which specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NFX1 pathway. THOC5 in conjunction with ALYREF/THOC4 functions in NXF1-NXT1 mediated nuclear export of HSP70 mRNA; both proteins enhance the RNA binding activity of NXF1 and are required for NXF1 localization to the nuclear rim. Involved in transcription elongation and genome stability. Involved in alternative polyadenylation site choice by recruiting CPSF6 to 5' region of target genes; probably mediates association of the TREX and CFIm complexes.; FUNCTION: Regulates the expression of myeloid transcription factors CEBPA, CEBPB and GAB2 by enhancing the levels of phosphatidylinositol 3,4,5-trisphosphate. May be involved in the differentiation of granulocytes and adipocytes. Essential for hematopoietic primitive cell survival and plays an integral role in monocytic development. PTM: Phosphorylated on tyrosine upon binding to activated CSF1R; which causes a dissociation of the two proteins. Phosphorylation on Ser-5 and/or Ser-6 is required for nuclear export. Phosphorylated on Thr-328 in insulin-stimulated adipocytes. {ECO:0000269|PubMed:10597251, ECO:0000269|PubMed:15221008, ECO:0000269|PubMed:15451025, ECO:0000269|PubMed:19015024}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15221008}. Cytoplasm {ECO:0000269|PubMed:15221008}. Note=Shuttles between nucleus and cytoplasm. {ECO:0000250|UniProtKB:Q13769}. SUBUNIT: Interacts with phosphorylated CSF1R (PubMed:10597251). Component of the THO complex, which is composed of THOC1, THOC2, THOC3, THOC5, THOC6 and THOC7; together with at least ALYREF/THOC4, DDX39B, SARNP/CIP29 and CHTOP, THO forms the transcription/export (TREX) complex which seems to have a dynamic structure involving ATP-dependent remodeling. Interacts with ALYREF/THOC4, and THOC7. Interacts (via N-terminus) with the NTF2 domain of NXF1 (By similarity). Forms a complex with CEBPB (PubMed:19015024). Interacts with CPSF6; indicative for an association with the cleavage factor Im (CFIm) complex (By similarity). Interacts with THOC1 (PubMed:16909111). Interacts with LUZP4 (By similarity). Interacts with NCBP3 (By similarity). {ECO:0000250|UniProtKB:Q13769, ECO:0000269|PubMed:10597251, ECO:0000269|PubMed:16909111}. TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in testis, liver and heart. {ECO:0000269|PubMed:10597251, ECO:0000269|PubMed:15451025}. +O70372 TERT_MOUSE Telomerase reverse transcriptase (EC 2.7.7.49) (Telomerase catalytic subunit) 1122 127,978 Chain (1); Domain (1); Metal binding (3); Modified residue (2); Motif (1); Region (11); Sequence conflict (1); Site (2) FUNCTION: Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. Active in progenitor and cancer cells. Inactive, or very low activity, in normal somatic cells. Catalytic component of the teleromerase holoenzyme complex whose main activity is the elongation of telomeres by acting as a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme. Catalyzes the RNA-dependent extension of 3'-chromosomal termini with the 6-nucleotide telomeric repeat unit, 5'-TTAGGG-3'. The catalytic cycle involves primer binding, primer extension and release of product once the template boundary has been reached or nascent product translocation followed by further extension. More active on substrates containing 2 or 3 telomeric repeats. Telomerase activity is regulated by a number of factors including telomerase complex-associated proteins, chaperones and polypeptide modifiers. Modulates Wnt signaling. Plays important roles in aging and antiapoptosis (By similarity). {ECO:0000250, ECO:0000269|PubMed:17130244, ECO:0000269|PubMed:19571879, ECO:0000269|PubMed:9582020}. PTM: Phosphorylation at Tyr-697 under oxidative stress leads to translocation of TERT to the cytoplasm and reduces its antiapoptotic activity. Dephosphorylated by SHP2/PTPN11 leading to nuclear retention. Phosphorylation by the AKT pathway promotes nuclear location. Phosphorylation at the G2/M phase at Ser-447 by DYRK2 promotes ubiquitination by the EDVP complex and degradation (By similarity). {ECO:0000250}.; PTM: Ubiquitinated by the EDVP complex, a E3 ligase complex following phosphorylation at Ser-447 by DYRK2. Ubiquitinated leads to proteasomal degradation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:O14746}. Nucleus, nucleoplasm {ECO:0000250}. Nucleus. Chromosome, telomere. Cytoplasm {ECO:0000250}. Nucleus, PML body {ECO:0000250}. Note=Shuttling between nuclear and cytoplasm depends on cell cycle, phosphorylation states, transformation and DNA damage. Diffuse localization in the nucleoplasm. Enriched in nucleoli of certain cell types. Translocated to the cytoplasm via nuclear pores in a CRM1/RAN-dependent manner involving oxidative stress-mediated phosphorylation at Tyr-697. Dephosphorylation at this site by SHP2 retains TERT in the nucleus. Translocated to the nucleus by phosphorylation by AKT (By similarity). {ECO:0000250}. SUBUNIT: Catalytic component of the telomerase holoenzyme complex composed of one molecule of TERT, one molecule of WRAP53/TCAB1, two molecules of H/ACA ribonucleoprotein complex subunits DKC1, NOP10, NHP2 and GAR1, and a telomerase RNA template component (TERC). The telomerase holoenzyme complex is associated with TEP1, SMG6/EST1A and POT1. The molecular chaperone HSP90/P23 complex is required for correct assembly and stabilization of the active telomerase. Interacts directly with HSP90A and PTGES3. Interacts with HSPA1A; the interaction occurs in the absence of TERC and dissociates once the complex has formed. Interacts with RAN; the interaction promotes nuclear export of TERT. Interacts with XPO1. Interacts with PTPN11; the interaction retains TERT in the nucleus. Interacts with NCL (via RRM1 and C-terminal RRM4/Arg/Gly-rich domains); the interaction is important for nucleolar localization of TERT (By similarity). Interacts with SMARCA4 (via the bromodomain); the interaction regulates Wnt-mediated signaling (PubMed:19571879). Interacts with MCRS1 (isoform MCRS2); the interaction inhibits in vitro telomerase activity (By similarity). Interacts with PIF1; the interaction has no effect on the elongation activity of TERT (PubMed:17130244). Interacts with PML; the interaction recruits TERT to PML bodies and inhibits telomerase activity (By similarity). Interacts with GNL3L (PubMed:19487455). Interacts with isoform 1 and isoform 2 of NVL (By similarity). Interacts with DHX36 (By similarity). {ECO:0000250|UniProtKB:O14746, ECO:0000269|PubMed:17130244, ECO:0000269|PubMed:19487455, ECO:0000269|PubMed:19571879}. DOMAIN: The primer grip sequence in the RT domain is required for telomerase activity and for stable association with short telomeric primers. {ECO:0000250}.; DOMAIN: The RNA-interacting domain 1 (RD1)/N-terminal extension (NTE) is required for interaction with the pseudoknot-template domain of each of TERC dimers. It contains anchor sites that bind primer nucleotides upstream of the RNA-DNA hybrid and is thus an essential determinant of repeat addition processivity (By similarity). {ECO:0000250}.; DOMAIN: The RNA-interacting domain 2 (RD2) is essential for both interaction with the CR4-CR5 domain of TERC and for DNA synthesis. {ECO:0000250}. TISSUE SPECIFICITY: High activity in intestine, liver and testis, moderate in lung, very low in muscle, heart and brain. {ECO:0000269|PubMed:13679242, ECO:0000269|PubMed:9582020, ECO:0000269|PubMed:9724727}. +Q8BZ33 TENS4_MOUSE Tensin-4 696 74,622 Chain (1); Compositional bias (1); Domain (2); Modified residue (1); Sequence conflict (4); Signal peptide (1) FUNCTION: May be involved in cell migration, cartilage development and in linking signal transduction pathways to the cytoskeleton May promote apoptosis, via its cleavage by caspase-3. Cytoplasm, cytoskeleton. {ECO:0000250}. PTM: Proteolytically cleaved by caspase-3 during apoptosis. {ECO:0000250}.; PTM: Tyrosine phosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. SUBUNIT: Binds to actin filaments and interacts with phosphotyrosine-containing proteins. {ECO:0000250}. +Q9JIB4 TF2H2_MOUSE General transcription factor IIH subunit 2 (Basic transcription factor 2 44 kDa subunit) (BTF2 p44) (General transcription factor IIH polypeptide 2) (TFIIH basal transcription factor complex p44 subunit) 396 44,687 Chain (1); Compositional bias (1); Domain (1); Modified residue (1); Zinc finger (1) FUNCTION: Component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module CAK controls the initiation of transcription. The N-terminus of GTF2H2 interacts with and regulates XPD whereas an intact C-terminus is required for a successful escape of RNAP II form the promoter. {ECO:0000250|UniProtKB:Q13888}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13888}. SUBUNIT: Component of the TFIID-containing RNA polymerase II pre-initiation complex that is composed of TBP and at least GTF2A1, GTF2A2, GTF2E1, GTF2E2, GTF2F1, GTF2H2, GTF2H3, GTF2H4, GTF2H5, GTF2B, TCEA1, ERCC2 and ERCC3. Component of the 7-subunit TFIIH core complex composed of XPB/ERCC3, XPD/ERCC2, GTF2H1, GTF2H2, GTF2H3, GTF2H4 and GTF2H5, which is active in NER. The core complex associates with the 3-subunit CDK-activating kinase (CAK) module composed of CCNH/cyclin H, CDK7 and MNAT1 to form the 10-subunit holoenzyme (holo-TFIIH) active in transcription. Interacts with XPB, XPD, GTF2H1 and GTF2H3. {ECO:0000250|UniProtKB:Q13888}. +Q8BMQ2 TF3C4_MOUSE General transcription factor 3C polypeptide 4 (EC 2.3.1.48) (TF3C-delta) (Transcription factor IIIC 90 kDa subunit) (TFIIIC 90 kDa subunit) (TFIIIC90) (Transcription factor IIIC subunit delta) 817 91,613 Alternative sequence (2); Chain (1); Cross-link (2); Modified residue (4); Sequence conflict (2) FUNCTION: Essential for RNA polymerase III to make a number of small nuclear and cytoplasmic RNAs, including 5S RNA, tRNA, and adenovirus-associated (VA) RNA of both cellular and viral origin. Has histone acetyltransferase activity (HAT) with unique specificity for free and nucleosomal H3. May cooperate with GTF3C5 in facilitating the recruitment of TFIIIB and RNA polymerase through direct interactions with BRF1, POLR3C and POLR3F. May be localized close to the A box (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Part of the TFIIIC subcomplex TFIIIC2, consisting of six subunits, GTF3C1, GTF3C2, GTF3C3, GTF3C4, GTF3C5 and GTF3C6. Interacts with BRF1, GTF3C1, GTF3C2, GTF3C5, GTF3C6, POLR3C and POLR3F (By similarity). {ECO:0000250}. +Q9D305 THAP2_MOUSE THAP domain-containing protein 2 217 24,993 Chain (1); Motif (1); Zinc finger (1) +Q6P3Z3 THAP4_MOUSE THAP domain-containing protein 4 569 62,571 Alternative sequence (2); Chain (1); Metal binding (1); Modified residue (2); Motif (1); Sequence conflict (4); Zinc finger (1) SUBUNIT: Homodimer. {ECO:0000250}. +P37242 THB_MOUSE Thyroid hormone receptor beta (Nuclear receptor subfamily 1 group A member 2) (c-erbA-2) (c-erbA-beta) 461 52,630 Alternative sequence (1); Binding site (4); Chain (1); DNA binding (1); Domain (1); Region (2); Sequence conflict (1); Zinc finger (2) FUNCTION: Nuclear hormone receptor that can act as a repressor or activator of transcription. High affinity receptor for thyroid hormones, including triiodothyronine and thyroxine. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Binds DNA as a dimer; homodimer and heterodimer with RXRB. Interacts with the coactivators NCOA1/SRC1, NCOA2/GRIP1, NCOA7 and MED1/TRAP220 in a ligand-inducible manner. Interacts with the corepressor NCOR1 in absence of ligand (By similarity). Interacts with C1D. Interacts with NR2F6; the interaction impairs the binding of the THRB homodimer and THRB:RXRB heterodimer to T3 response elements. Interacts with PRMT2 and THRSP (By similarity). {ECO:0000250}. DOMAIN: Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain. +Q91WA1 TIPIN_MOUSE TIMELESS-interacting protein 278 31,498 Chain (1); Modified residue (3); Region (1); Sequence conflict (2) FUNCTION: Plays an important role in the control of DNA replication and the maintenance of replication fork stability. Important for cell survival after DNA damage or replication stress. May be specifically required for the ATR-CHEK1 pathway in the replication checkpoint induced by hydroxyurea or ultraviolet light. Forms a complex with TIMELESS and this complex regulates DNA replication processes under both normal and stress conditions, stabilizes replication forks and influences both CHEK1 phosphorylation and the intra-S phase checkpoint in response to genotoxic stress. {ECO:0000269|PubMed:17141802}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12875843}. Nucleus {ECO:0000269|PubMed:12875843}. SUBUNIT: Interacts with MCM6 and MCM7 (By similarity). Interacts with TIMELESS, which impairs TIMELESS self-association. Interacts with RPA2 and PRDX2. {ECO:0000250, ECO:0000269|PubMed:12875843, ECO:0000269|PubMed:17141802}. TISSUE SPECIFICITY: Expressed in brain. {ECO:0000269|PubMed:12875843}. +P25785 TIMP2_MOUSE Metalloproteinase inhibitor 2 (Tissue inhibitor of metalloproteinases 2) (TIMP-2) 220 24,328 Chain (1); Disulfide bond (6); Domain (1); Metal binding (1); Region (2); Sequence conflict (3); Signal peptide (1); Site (3) FUNCTION: Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. PTM: The activity of TIMP2 is dependent on the presence of disulfide bonds. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Interacts (via the C-terminal) with MMP2 (via the C-terminal PEX domain); the interaction inhibits the MMP2 activity. {ECO:0000250}. TISSUE SPECIFICITY: Detected in testis, retina, hippocampus and cerebral cortex. {ECO:0000269|PubMed:16985004}. +A2ACG1 TLDC2_MOUSE TLD domain-containing protein 2 (TBC/LysM-associated domain-containing protein 2) 198 21,987 Chain (1); Compositional bias (1); Domain (1) +Q9WVM6 TLL2_MOUSE Tolloid-like protein 2 (EC 3.4.24.-) 1012 113,252 Active site (1); Chain (1); Disulfide bond (19); Domain (8); Glycosylation (5); Metal binding (3); Modified residue (2); Propeptide (1); Signal peptide (1) FUNCTION: Protease which specifically processes pro-lysyl oxidase. Required for the embryonic development. Predominant protease, which in the development, influences dorsal-ventral patterning and skeletogenesis. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +A2ASS6 TITIN_MOUSE Titin (EC 2.7.11.1) (Connectin) 35213 3,906,488 Active site (1); Alternative sequence (4); Binding site (1); Chain (1); Coiled coil (2); Compositional bias (11); Disulfide bond (45); Domain (277); Modified residue (63); Nucleotide binding (1); Region (2); Repeat (144) FUNCTION: Key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The size and extensibility of the cross-links are the main determinants of sarcomere extensibility properties of muscle. In non-muscle cells, seems to play a role in chromosome condensation and chromosome segregation during mitosis. Might link the lamina network to chromatin or nuclear actin, or both during interphase. {ECO:0000250|UniProtKB:Q8WZ42, ECO:0000269|PubMed:16702235, ECO:0000269|PubMed:17261657}. PTM: Autophosphorylated. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000250|UniProtKB:Q8WZ42}. SUBUNIT: Interacts with MYOM1, MYOM2, tropomyosin and myosin. Interacts with actin, primarily via the PEVK domains and with MYPN. Interacts with FHL2, NEB, CRYAB, LMNA/lamin-A and LMNB/lamin-B. Interacts with TCAP/telethonin and/or ANK1 isoform Mu17/ank1.5, via the first two N-terminal immunoglobulin domains. Interacts with TRIM63, TRIM55, ANKRD1, ANKRD2, ANKRD23, and CAPN3 through several Ig domains. Interacts with NBR1 through the protein kinase domain (By similarity). Interacts with CMYA5 (By similarity). {ECO:0000250}. DOMAIN: ZIS1 and ZIS5 regions contain multiple SPXR consensus sites for ERK- and CDK-like protein kinases as well as multiple SP motifs. ZIS1 could adopt a closed conformation which would block the TCAP-binding site (By similarity). {ECO:0000250|UniProtKB:Q8WZ42}.; DOMAIN: The PEVK region may serve as an entropic spring of a chain of structural folds and may also be an interaction site to other myofilament proteins to form interfilament connectivity in the sarcomere. {ECO:0000250|UniProtKB:Q8WZ42}. +Q9DCD5 TJAP1_MOUSE Tight junction-associated protein 1 (Protein incorporated later into tight junctions) (Tight junction protein 4) 539 59,420 Chain (1); Coiled coil (1); Modified residue (7); Sequence conflict (1) SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:11602598}. Cell junction, tight junction {ECO:0000269|PubMed:11602598}. Note=Recruited to tight junctions (TJ) during late stages of maturation of the TJ complexes. Excluded from adherens junctions and desmosomes. SUBUNIT: Interacts with DLG1. {ECO:0000250}. +B2RVY9 TM182_MOUSE Transmembrane protein 182 229 25,845 Chain (1); Glycosylation (4); Signal peptide (1); Topological domain (4); Transmembrane (3) TRANSMEM 115 135 Helical. {ECO:0000255}.; TRANSMEM 154 174 Helical. {ECO:0000255}.; TRANSMEM 201 221 Helical. {ECO:0000255}. TOPO_DOM 27 114 Extracellular. {ECO:0000255}.; TOPO_DOM 136 153 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 175 200 Extracellular. {ECO:0000255}.; TOPO_DOM 222 229 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Highly expressed in white adipose tissues (WAT), with 10-fold to 20-fold higher levels than in brown adipose tissue (BAT). Also expressed in skeletal muscle, heart and lung. Lower relative levels of expression in kidney, spleen, testis, brain and liver. {ECO:0000269|PubMed:18803820}. +Q9JJB9 TM183_MOUSE Transmembrane protein 183 375 42,945 Chain (1); Sequence conflict (1); Transmembrane (1) TRANSMEM 299 319 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q99LQ7 TM189_MOUSE Transmembrane protein 189 271 31,134 Chain (1); Transmembrane (3) TRANSMEM 48 68 Helical. {ECO:0000255}.; TRANSMEM 75 95 Helical. {ECO:0000255}.; TRANSMEM 166 186 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:A5PLL7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A5PLL7}. +Q91VX9 TM168_MOUSE Transmembrane protein 168 697 79,674 Chain (1); Glycosylation (4); Sequence conflict (2); Transmembrane (10) TRANSMEM 36 56 Helical. {ECO:0000255}.; TRANSMEM 63 83 Helical. {ECO:0000255}.; TRANSMEM 89 109 Helical. {ECO:0000255}.; TRANSMEM 172 192 Helical. {ECO:0000255}.; TRANSMEM 199 219 Helical. {ECO:0000255}.; TRANSMEM 223 243 Helical. {ECO:0000255}.; TRANSMEM 265 285 Helical. {ECO:0000255}.; TRANSMEM 293 313 Helical. {ECO:0000255}.; TRANSMEM 352 372 Helical. {ECO:0000255}.; TRANSMEM 380 400 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8VCR3 TM242_MOUSE Transmembrane protein 242 140 14,916 Alternative sequence (3); Chain (1); Frameshift (1); Modified residue (1); Sequence conflict (4); Transmembrane (2) TRANSMEM 29 49 Helical. {ECO:0000255}.; TRANSMEM 81 101 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9D9S2 TM225_MOUSE Transmembrane protein 225 230 26,483 Chain (1); Motif (1); Mutagenesis (1); Topological domain (5); Transmembrane (4) TRANSMEM 9 29 Helical. {ECO:0000255}.; TRANSMEM 72 92 Helical. {ECO:0000255}.; TRANSMEM 100 120 Helical. {ECO:0000255}.; TRANSMEM 140 160 Helical. {ECO:0000255}. TOPO_DOM 1 8 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 30 71 Extracellular. {ECO:0000305}.; TOPO_DOM 93 99 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 121 139 Extracellular. {ECO:0000305}.; TOPO_DOM 161 230 Cytoplasmic. {ECO:0000305}. FUNCTION: Probably inhibits protein phosphatase 1 (PP1) in sperm via binding to catalytic subunit PPP1CC. {ECO:0000269|PubMed:25605614}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome membrane {ECO:0000269|PubMed:25605614}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Interacts (via RVxF motif) with PPP1CC. {ECO:0000269|PubMed:25605614}. TISSUE SPECIFICITY: Expressed in testis, epididymis and spermatozoa (at protein level). Not expressed in brain, heart, lung, liver, spleen, kidney and skeletal muscle. {ECO:0000269|PubMed:25605614}. +Q9DAM7 TM263_MOUSE Transmembrane protein 263 115 11,549 Chain (1); Transmembrane (2) TRANSMEM 39 59 Helical. {ECO:0000255}.; TRANSMEM 77 97 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9CZB9 TM128_MOUSE Transmembrane protein 128 163 19,069 Chain (1); Sequence conflict (4); Transmembrane (4) TRANSMEM 47 67 Helical. {ECO:0000255}.; TRANSMEM 79 99 Helical. {ECO:0000255}.; TRANSMEM 117 137 Helical. {ECO:0000255}.; TRANSMEM 142 162 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9CQN6 TM14C_MOUSE Transmembrane protein 14C 114 11,642 Chain (1); Transmembrane (4) TRANSMEM 8 28 Helical. {ECO:0000255}.; TRANSMEM 33 53 Helical. {ECO:0000255}.; TRANSMEM 63 83 Helical. {ECO:0000255}.; TRANSMEM 89 109 Helical. {ECO:0000255}. FUNCTION: Required for normal heme biosynthesis. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q8BRG8 TM209_MOUSE Transmembrane protein 209 561 62,982 Alternative sequence (3); Chain (1); Compositional bias (1); Frameshift (1); Glycosylation (2); Modified residue (5); Sequence conflict (3); Transmembrane (2) TRANSMEM 28 48 Helical. {ECO:0000255}.; TRANSMEM 60 80 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8C4Q9 TM154_MOUSE Transmembrane protein 154 181 19,879 Alternative sequence (2); Chain (1); Modified residue (2); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 75 95 Helical. {ECO:0000255}. TOPO_DOM 23 74 Extracellular. {ECO:0000255}.; TOPO_DOM 96 181 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q8BYI9 TENR_MOUSE Tenascin-R (TN-R) (Janusin) (Neural recognition molecule J1-160/180) (Restrictin) 1358 149,589 Alternative sequence (1); Chain (1); Coiled coil (1); Compositional bias (1); Disulfide bond (2); Domain (15); Glycosylation (13); Modified residue (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Neural extracellular matrix (ECM) protein involved in interactions with different cells and matrix components. Theses interactions can influence cellular behavior by either evoking a stable adhesion and differentiation, or repulsion and inhibition of neurite growth. Binding to cell surface gangliosides inhibits RGD-dependent integrin-mediated cell adhesion and results in an inhibition of PTK2/FAK1 (FAK) phosphorylation and cell detachment. Binding to membrane surface sulfatides results in a oligodendrocyte adhesion and differentiation. Interaction with CNTN1 induces a repulsion of neurons and an inhibition of neurite outgrowth. Interacts with SCN2B may play a crucial role in clustering and regulation of activity of sodium channels at nodes of Ranvier. TNR-linked chondroitin sulfate glycosaminoglycans are involved in the interaction with FN1 and mediates inhibition of cell adhesion and neurite outgrowth. The highly regulated addition of sulfated carbohydrate structure may modulate the adhesive properties of TNR over the course of development and during synapse maintenance (By similarity). {ECO:0000250, ECO:0000269|PubMed:10383637, ECO:0000269|PubMed:10773191, ECO:0000269|PubMed:7678967, ECO:0000269|PubMed:9169525}. PTM: Contains N-linked oligosaccharides with a sulfated carbohydrate structures (By similarity). Contains N-linked oligosaccharides, O-linked sialylated structures and O-linked chondroitin sulfate glycosaminoglycans. {ECO:0000250, ECO:0000269|PubMed:10406848, ECO:0000269|PubMed:10773191}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SUBUNIT: Interacts with BCAN and ACAN in a calcium-dependent manner. Interacts with SCN2B, PTPRZ1, and CSPG3 (By similarity). Forms oligomers. Isoforms 1 and 2 form respectively trimeric (tribrachion) and dimeric kink-armed rodlike structures, which are linked by disulfide bridges. Interacts with CNTN1, TNC and FN1. {ECO:0000250, ECO:0000269|PubMed:10773191, ECO:0000269|PubMed:7678967}. DOMAIN: The EGF-like domains mediate interaction with CNTN1. The fibronectin type-III domains 3-5 mediate interaction with BCAN. The fibronectin type-III domains 1-2 and 7-9 mediate interaction with SCN2B (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Brain-specific. {ECO:0000269|PubMed:2477380}. +Q6IMH0 TEPP_MOUSE Testis, prostate and placenta-expressed protein 216 24,949 Alternative sequence (1); Chain (1); Sequence conflict (1) +O70422 TF2H4_MOUSE General transcription factor IIH subunit 4 (Basic transcription factor 2 52 kDa subunit) (BTF2 p52) (General transcription factor IIH polypeptide 4) (TFIIH basal transcription factor complex p52 subunit) 463 52,224 Chain (1) FUNCTION: Component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module CAK controls the initiation of transcription. {ECO:0000250|UniProtKB:Q92759}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Component of the 7-subunit TFIIH core complex composed of XPB/ERCC3, XPD/ERCC2, GTF2H1, GTF2H2, GTF2H3, GTF2H4 and GTF2H5, which is active in NER. The core complex associates with the 3-subunit CDK-activating kinase (CAK) module composed of CCNH/cyclin H, CDK7 and MNAT1 to form the 10-subunit holoenzyme (holo-TFIIH) active in transcription. {ECO:0000250|UniProtKB:Q92759}. +Q01853 TERA_MOUSE Transitional endoplasmic reticulum ATPase (TER ATPase) (EC 3.6.4.6) (15S Mg(2+)-ATPase p97 subunit) (Valosin-containing protein) (VCP) 806 89,322 Beta strand (28); Binding site (2); Chain (1); Cross-link (2); Helix (38); Initiator methionine (1); Modified residue (18); Motif (1); Mutagenesis (1); Nucleotide binding (2); Region (1); Sequence conflict (7); Turn (5) FUNCTION: Necessary for the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis. Involved in the formation of the transitional endoplasmic reticulum (tER). The transfer of membranes from the endoplasmic reticulum to the Golgi apparatus occurs via 50-70 nm transition vesicles which derive from part-rough, part-smooth transitional elements of the endoplasmic reticulum (tER). Vesicle budding from the tER is an ATP-dependent process. The ternary complex containing UFD1, VCP and NPLOC4 binds ubiquitinated proteins and is necessary for the export of misfolded proteins from the ER to the cytoplasm, where they are degraded by the proteasome. The NPLOC4-UFD1-VCP complex regulates spindle disassembly at the end of mitosis and is necessary for the formation of a closed nuclear envelope. Regulates E3 ubiquitin-protein ligase activity of RNF19A. Component of the VCP/p97-AMFR/gp78 complex that participates in the final step of the sterol-mediated ubiquitination and endoplasmic reticulum-associated degradation (ERAD) of HMGCR. Involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for proteasomal degradation. Plays a role in the regulation of stress granules (SGs) clearance process upon arsenite-induced response (By similarity). Also involved in DNA damage response: recruited to double-strand breaks (DSBs) sites in a RNF8- and RNF168-dependent manner and promotes the recruitment of TP53BP1 at DNA damage sites. Recruited to stalled replication forks by SPRTN: may act by mediating extraction of DNA polymerase eta (POLH) to prevent excessive translesion DNA synthesis and limit the incidence of mutations induced by DNA damage. Required for cytoplasmic retrotranslocation of stressed/damaged mitochondrial outer-membrane proteins and their subsequent proteasomal degradation. Essential for the maturation of ubiquitin-containing autophagosomes and the clearance of ubiquitinated protein by autophagy. Acts as a negative regulator of type I interferon production by interacting with DDX58/RIG-I: interaction takes place when DDX58/RIG-I is ubiquitinated via 'Lys-63'-linked ubiquitin on its CARD domains, leading to recruit RNF125 and promote ubiquitination and degradation of DDX58/RIG-I. May play a role in the ubiquitin-dependent sorting of membrane proteins to lysosomes where they undergo degradation. May more particularly play a role in caveolins sorting in cells. By controlling the steady-state expression of the IGF1R receptor, indirectly regulates the insulin-like growth factor receptor signaling pathway. {ECO:0000250|UniProtKB:P46462, ECO:0000250|UniProtKB:P55072}. PTM: Phosphorylated by tyrosine kinases in response to T-cell antigen receptor activation. Phosphorylated in mitotic cells. {ECO:0000250|UniProtKB:P46462}.; PTM: ISGylated. {ECO:0000269|PubMed:16139798}.; PTM: Methylation at Lys-315 catalyzed by VCPKMT is increased in the presence of ASPSCR1. Lys-315 methylation may decrease ATPase activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P55072}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P55072}. Nucleus {ECO:0000250|UniProtKB:P55072}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:P55072}. Note=Recruited to the cytoplasmic surface of the endoplasmic reticulum via interaction with AMFR/gp78. Following DNA double-strand breaks, recruited to the sites of damage. Recruited to stalled replication forks via interaction with SPRTN. Recruited to damaged lysosomes decorated with K48-linked ubiquitin chains. Colocalizes with TIA1, ZFAND1 and G3BP1 in cytoplasmic stress granules (SGs) in response to arsenite-induced stress treatment (By similarity). {ECO:0000250|UniProtKB:P55072}. SUBUNIT: Homohexamer. Forms a ring-shaped particle of 12.5 nm diameter, that displays 6-fold radial symmetry. Part of a ternary complex containing STX5A, NSFL1C and VCP. NSFL1C forms a homotrimer that binds to one end of a VCP homohexamer. The complex binds to membranes enriched in phosphatidylethanolamine-containing lipids and promotes Golgi membrane fusion. Binds to a heterodimer of NPLOC4 and UFD1, binding to this heterodimer inhibits Golgi-membrane fusion. Interaction with VCIP135 leads to dissociation of the complex via ATP hydrolysis by VCP. Part of a ternary complex containing NPLOC4, UFD1 and VCP. Interacts with NSFL1C-like protein p37; the complex has membrane fusion activity and is required for Golgi and endoplasmic reticulum biogenesis. Interacts with RNF103. Interacts with TRIM13 and TRIM21. Component of a VCP/p97-AMFR/gp78 complex that participates in the final step of the endoplasmic reticulum-associated degradation (ERAD) of HMGCR. Interacts directly with AMFR/gp78 (via its VIM). Interacts with RHBDD1 (via C-terminal domain). Interacts with SPRTN; leading to recruitment to stalled replication forks. Interacts with SELENOS and SYVN1, as well as with DERL1, DERL2 and DERL3; which probably transfer misfolded proteins from the ER to VCP. Interacts with SVIP. Component of a complex required to couple retrotranslocation, ubiquitination and deglycosylation composed of NGLY1, SAKS1, AMFR, VCP and RAD23B. Directly interacts with UBXN4 and RNF19A. Interacts with CASR. Interacts with UBE4B and YOD1. Interacts with clathrin. Interacts with RNF103. Interacts with TRIM13 and TRIM21. Component of a VCP/p97-AMFR/gp78 complex that participates in the final step of the endoplasmic reticulum-associated degradation (ERAD) of HMGCR. Interacts directly with AMFR/gp78 (via its VIM). Interacts with WASHC5. Interacts with UBOX5. Interacts (via N- terminus) with UBXN7, UBXN8, and probably several other UBX domain-containing proteins (via UBX domains); the interactions are mutually exclusive with VIM-dependent interactions such as those with AMFR and SELENOS. Forms a complex with UBQLN1 and UBXN4 (By similarity). Interacts (via the PIM motif) with RNF31 (via the PUB domain) (By similarity). Interacts with DDX58/RIG-I and RNF125; interaction takes place when DDX58/RIG-I is ubiquitinated via'Lys-63'-linked ubiquitin on its CARD domains, leading to recruit RNF125 and promote ubiquitination and degradation of DDX58/RIG-I (By similarity). Interacts with BAG6 (By similarity). Interacts with UBXN10 (By similarity). Interacts with UBXN6; the interaction with UBXN6 is direct and competitive with UFD1 (By similarity). Forms a ternary complex with CAV1 and UBXN6. Interacts with PLAA, UBXN6 and YOD1; may form a complex involved in macroautophagy (By similarity). Interacts with ANKZF1 (By similarity). Interacts with ubiquitin-binding protein FAF1 (By similarity). Interacts with ZFAND2B (via VIM motif); the interaction is direct (PubMed:24160817, PubMed:26337389). Interacts with ZFAND1 (via its ubiquitin-like region); this interaction occurs in an arsenite-dependent manner (By similarity). {ECO:0000250|UniProtKB:P46462, ECO:0000250|UniProtKB:P55072, ECO:0000269|PubMed:15189447, ECO:0000269|PubMed:15456787, ECO:0000269|PubMed:16249333, ECO:0000269|PubMed:16709668, ECO:0000269|PubMed:17141156, ECO:0000269|PubMed:24160817, ECO:0000269|PubMed:26337389}. DOMAIN: The N-terminal domain shows evolutionary conservation with that of PEX1, and is able to bind phospholipids with a preference for phosphatidylinositol mono- and bisphosphates.; DOMAIN: The PIM (PUB-interaction motif) motif mediates interaction with the PUB domain of RNF31. {ECO:0000250|UniProtKB:P55072}. +Q64729 TGFR1_MOUSE TGF-beta receptor type-1 (TGFR-1) (EC 2.7.11.30) (ESK2) (Transforming growth factor-beta receptor type I) (TGF-beta receptor type I) (TbetaR-I) 503 56,179 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Cross-link (1); Disulfide bond (5); Domain (2); Glycosylation (1); Modified residue (6); Motif (1); Nucleotide binding (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 127 147 Helical. {ECO:0000255}. TOPO_DOM 30 126 Extracellular. {ECO:0000255}.; TOPO_DOM 148 503 Cytoplasmic. {ECO:0000255}. FUNCTION: Transmembrane serine/threonine kinase forming with the TGF-beta type II serine/threonine kinase receptor, TGFBR2, the non-promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3. Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to the cytoplasm and is thus regulating a plethora of physiological and pathological processes including cell cycle arrest in epithelial and hematopoietic cells, control of mesenchymal cell proliferation and differentiation, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. The formation of the receptor complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound to the cytokine dimer results in the phosphorylation and the activation of TGFBR1 by the constitutively active TGFBR2. Activated TGFBR1 phosphorylates SMAD2 which dissociates from the receptor and interacts with SMAD4. The SMAD2-SMAD4 complex is subsequently translocated to the nucleus where it modulates the transcription of the TGF-beta-regulated genes. This constitutes the canonical SMAD-dependent TGF-beta signaling cascade. Also involved in non-canonical, SMAD-independent TGF-beta signaling pathways. For instance, TGFBR1 induces TRAF6 autoubiquitination which in turn results in MAP3K7 ubiquitination and activation to trigger apoptosis. Also regulates epithelial to mesenchymal transition through a SMAD-independent signaling pathway through PARD6A phosphorylation and activation (By similarity). {ECO:0000250|UniProtKB:P36897}. PTM: Phosphorylated at basal levels in the absence of ligand. Activated upon phosphorylation by TGFBR2, mainly in the GS domain. Phosphorylation in the GS domain abrogates FKBP1A-binding (By similarity). {ECO:0000250|UniProtKB:P36897}.; PTM: N-Glycosylated. {ECO:0000250|UniProtKB:P36897}.; PTM: Ubiquitinated; undergoes ubiquitination catalyzed by several E3 ubiquitin ligases including SMURF1, SMURF2 and NEDD4L2. Results in the proteasomal and/or lysosomal degradation of the receptor thereby negatively regulating its activity. Deubiquitinated by USP15, leading to stabilization of the protein and enhanced TGF-beta signal. Its ubiquitination and proteasome-mediated degradation is negatively regulated by SDCBP (By similarity). {ECO:0000250|UniProtKB:P36897}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P36897}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P36897}. Cell junction, tight junction {ECO:0000250|UniProtKB:P36897}. Membrane raft {ECO:0000250|UniProtKB:P36897}. Cell surface {ECO:0000250|UniProtKB:P36897}. SUBUNIT: Homodimer; in the endoplasmic reticulum but also at the cell membrane. Heterohexamer; TGFB1, TGFB2 and TGFB3 homodimeric ligands assemble a functional receptor composed of two TGFBR1 and TGFBR2 heterodimers to form a ligand-receptor heterohexamer. The respective affinity of TGBRB1 and TGFBR2 for the ligands may modulate the kinetics of assembly of the receptor and may explain the different biological activities of TGFB1, TGFB2 and TGFB3. Interacts with CD109; inhibits TGF-beta receptor activation in keratinocytes. Interacts with RBPMS. Interacts (unphosphorylated) with FKBP1A; prevents TGFBR1 phosphorylation by TGFBR2 and stabilizes it in the inactive conformation. Interacts with SMAD2, SMAD3 and ZFYVE9; ZFYVE9 recruits SMAD2 and SMAD3 to the TGF-beta receptor. Interacts with TRAF6 and MAP3K7; induces MAP3K7 activation by TRAF6. Interacts with PARD6A; involved in TGF-beta induced epithelial to mesenchymal transition. Interacts with SMAD7, NEDD4L, SMURF1 and SMURF2; SMAD7 recruits NEDD4L, SMURF1 and SMURF2 to the TGF-beta receptor (By similarity). Interacts with USP15 and VPS39. Interacts with SDCBP (via C-terminus). Interacts with CAV1 and this interaction is impaired in the presence of SDCBP (By similarity). {ECO:0000250|UniProtKB:P36897}. +Q62312 TGFR2_MOUSE TGF-beta receptor type-2 (TGFR-2) (EC 2.7.11.30) (TGF-beta type II receptor) (Transforming growth factor-beta receptor type II) (TGF-beta receptor type II) (TbetaR-II) 592 67,122 Active site (1); Alternative sequence (2); Binding site (1); Chain (1); Disulfide bond (6); Domain (1); Glycosylation (3); Modified residue (3); Nucleotide binding (1); Sequence conflict (7); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 185 214 Helical. {ECO:0000255}. TOPO_DOM 24 184 Extracellular. {ECO:0000255}.; TOPO_DOM 215 592 Cytoplasmic. {ECO:0000255}. FUNCTION: Transmembrane serine/threonine kinase forming with the TGF-beta type I serine/threonine kinase receptor, TGFBR1, the non-promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3. Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to the cytoplasm and is thus regulating a plethora of physiological and pathological processes including cell cycle arrest in epithelial and hematopoietic cells, control of mesenchymal cell proliferation and differentiation, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. The formation of the receptor complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound to the cytokine dimer results in the phosphorylation and the activation of TGFRB1 by the constitutively active TGFBR2. Activated TGFBR1 phosphorylates SMAD2 which dissociates from the receptor and interacts with SMAD4. The SMAD2-SMAD4 complex is subsequently translocated to the nucleus where it modulates the transcription of the TGF-beta-regulated genes. This constitutes the canonical SMAD-dependent TGF-beta signaling cascade. Also involved in non-canonical, SMAD-independent TGF-beta signaling pathways (By similarity). {ECO:0000250|UniProtKB:P37173}. PTM: Phosphorylated on a Ser/Thr residue in the cytoplasmic domain. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P37173}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P37173}. Membrane raft {ECO:0000250|UniProtKB:P37173}. SUBUNIT: Homodimer. Heterohexamer; TGFB1, TGFB2 and TGFB3 homodimeric ligands assemble a functional receptor composed of two TGFBR1 and TGFBR2 heterodimers to form a ligand-receptor heterohexamer. The respective affinity of TGFRB1 and TGFRB2 for the ligands may modulate the kinetics of assembly of the receptor and may explain the different biological activities of TGFB1, TGFB2 and TGFB3. Interacts with DAXX. Interacts with TCTEX1D4. Interacts with ZFYVE9; ZFYVE9 recruits SMAD2 and SMAD3 to the TGF-beta receptor (By similarity). Interacts with and is activated by SCUBE3; this interaction does not affect TGFB1-binding to TGFBR2 (By similarity). Interacts with VPS39; this interaction is independent of the receptor kinase activity and of the presence of TGF-beta (By similarity). {ECO:0000250|UniProtKB:P37173}. TISSUE SPECIFICITY: Widely expressed in adult. Expressed primarily in mesenchyme and epidermis of the midgestational fetus. +Q62313 TGON1_MOUSE Trans-Golgi network integral membrane protein 1 (TGN38A) 353 37,848 Chain (1); Glycosylation (2); Motif (1); Region (1); Repeat (6); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 299 319 Helical. {ECO:0000255}. TOPO_DOM 18 298 Extracellular. {ECO:0000255}.; TOPO_DOM 320 353 Cytoplasmic. {ECO:0000255}. FUNCTION: May be involved in regulating membrane traffic to and from trans-Golgi network. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Primarily in trans-Golgi network. Cycles between the trans-Golgi network and the cell surface returning via endosomes (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. +Q80W47 WIPI2_MOUSE WD repeat domain phosphoinositide-interacting protein 2 (WIPI-2) 445 48,477 Chain (1); Modified residue (1); Motif (1); Repeat (3) FUNCTION: Component of the autophagy machinery that controls the major intracellular degradation process by which cytoplasmic materials are packaged into autophagosomes and delivered to lysosomes for degradation. Involved in an early step of the formation of preautophagosomal structures. Binds and is activated by phosphatidylinositol 3-phosphate (PtdIns3P) forming on membranes of the endoplasmic reticulum upon activation of the upstream ULK1 and PI3 kinases. Once activated, WIPI2 recruits at phagophore assembly sites the ATG12-ATG5-ATG16L1 complex that directly controls the elongation of the nascent autophagosomal membrane. {ECO:0000269|PubMed:23051912, ECO:0000269|PubMed:23291478, ECO:0000269|PubMed:24954904}. SUBCELLULAR LOCATION: Preautophagosomal structure membrane {ECO:0000269|PubMed:23051912, ECO:0000269|PubMed:23291478, ECO:0000269|PubMed:24954904}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9Y4P8}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9Y4P8}. Note=Localizes to omegasomes membranes which are endoplasmic reticulum connected structures at the origin of preautophagosomal structures. Enriched at preautophagosomal structure membranes in response to PtdIns3P. {ECO:0000250|UniProtKB:Q9Y4P8}. SUBUNIT: Interacts with TECPR1 (By similarity). Interacts with ATG16L1 (PubMed:24954904). Interacts with ATG5 (By similarity). Interacts with WIPI1 (By similarity). Interacts with WDR45 (By similarity). May interact with NUDC (By similarity). {ECO:0000250|UniProtKB:Q9Y4P8, ECO:0000269|PubMed:24954904}. DOMAIN: The FRRG motif is required for recruitment to PtdIns3P. {ECO:0000303|PubMed:24954904}. +D3Z5L9 WISP3_MOUSE WNT1-inducible-signaling pathway protein 3 (WISP-3) (CCN family member 6) 354 39,379 Chain (1); Disulfide bond (7); Domain (3); Glycosylation (1); Signal peptide (1) FUNCTION: Appears to be required for normal postnatal skeletal growth and cartilage homeostasis. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +P70318 TIAR_MOUSE Nucleolysin TIAR (TIA-1-related protein) 392 43,389 Chain (1); Domain (3); Modified residue (2) FUNCTION: RNA-binding protein. Possesses nucleolytic activity against cytotoxic lymphocyte target cells. May be involved in apoptosis (By similarity). {ECO:0000250}. PTM: Phosphorylated by MAPK14 following DNA damage, releasing TIAR from GADD45A mRNA. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19861488}. Nucleus {ECO:0000269|PubMed:19861488}. Cytoplasmic granule {ECO:0000269|PubMed:19861488}. Note=The cytoplasmic granules are stress granules which are a dense aggregation in the cytosol composed of proteins and RNAs that appear when the cell is under stress. Colocalizes with NANOS3 in the stress granules. TISSUE SPECIFICITY: Expressed both in primordial germ cells (PGCs) and in neighboring somatic cells. {ECO:0000269|PubMed:19861488}. +Q0VBL1 TIGD2_MOUSE Tigger transposable element-derived protein 2 525 59,651 Chain (1); DNA binding (2); Domain (3) SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00320, ECO:0000255|PROSITE-ProRule:PRU00583}. +O35857 TIM44_MOUSE Mitochondrial import inner membrane translocase subunit TIM44 452 51,091 Chain (1); Modified residue (4); Nucleotide binding (1); Sequence conflict (1); Transit peptide (1) FUNCTION: Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. Recruits mitochondrial HSP70 to drive protein translocation into the matrix using ATP as an energy source. {ECO:0000250|UniProtKB:Q01852}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:9419343}; Peripheral membrane protein {ECO:0000269|PubMed:9419343}; Matrix side {ECO:0000269|PubMed:9419343}. SUBUNIT: Probable component of the PAM complex at least composed of a mitochondrial HSP70 protein, GRPEL1 or GRPEL2, TIMM44, TIMM16/PAM16 and TIMM14/DNAJC19. The complex interacts with the TIMM23 component of the TIM23 complex (By similarity). {ECO:0000250}. +Q8VC30 TKFC_MOUSE Triokinase/FMN cyclase (Bifunctional ATP-dependent dihydroxyacetone kinase/FAD-AMP lyase (cyclizing)) [Includes: ATP-dependent dihydroxyacetone kinase (DHA kinase) (EC 2.7.1.28) (EC 2.7.1.29) (Glycerone kinase) (Triokinase) (Triose kinase); FAD-AMP lyase (cyclizing) (EC 4.6.1.15) (FAD-AMP lyase (cyclic FMN forming)) (FMN cyclase)] 578 59,691 Active site (1); Binding site (3); Chain (1); Domain (2); Modified residue (2); Nucleotide binding (4); Region (1) FUNCTION: Catalyzes both the phosphorylation of dihydroxyacetone and of glyceraldehyde, and the splitting of ribonucleoside diphosphate-X compounds among which FAD is the best substrate. Represses IFIH1-mediated cellular antiviral response. {ECO:0000250|UniProtKB:F1RKQ4, ECO:0000250|UniProtKB:Q3LXA3, ECO:0000250|UniProtKB:Q4KLZ6}. SUBUNIT: Homodimer (By similarity). Interacts with IFIH1 (via the CARD domains), the interaction is inhibited by viral infection (By similarity). {ECO:0000250|UniProtKB:F1RKQ4, ECO:0000250|UniProtKB:Q3LXA3}. DOMAIN: DhaK and DhaL domains have differential roles, individually DhaK is inactive and DhaL displays cyclase but not kinase activity. {ECO:0000250|UniProtKB:Q3LXA3}. +Q8CCM6 TIM21_MOUSE Mitochondrial import inner membrane translocase subunit Tim21 (TIM21-like protein, mitochondrial) 249 28,304 Alternative sequence (3); Chain (1); Sequence conflict (1); Transit peptide (1); Transmembrane (1) TRANSMEM 107 127 Helical. {ECO:0000255}. FUNCTION: Participates in the translocation of transit peptide-containing proteins across the mitochondrial inner membrane. Also required for assembly of mitochondrial respiratory chain complex I and complex IV as component of the MITRAC (mitochondrial translation regulation assembly intermediate of cytochrome c oxidase complex) complex. Probably shuttles between the presequence translocase and respiratory-chain assembly intermediates in a process that promotes incorporation of early nuclear-encoded subunits into these complexes. {ECO:0000250|UniProtKB:Q9BVV7}. SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. SUBUNIT: Component of the TIM23 complex. Component of the MITRAC (mitochondrial translation regulation assembly intermediate of cytochrome c oxidase complex) complex, the core components of this complex being COA3/MITRAC12 and COX14. Interacts with COA3 AND MT-CO1/COX1. {ECO:0000250|UniProtKB:Q9BVV7}. +P41539 TKN1_MOUSE Protachykinin-1 (PPT) [Cleaved into: Substance P; Neurokinin A (NKA) (Neuromedin L) (Substance K); Neuropeptide K (NPK); Neuropeptide gamma; C-terminal-flanking peptide] 130 15,045 Alternative sequence (1); Modified residue (2); Peptide (6); Propeptide (1); Signal peptide (1); Site (1) FUNCTION: Tachykinins are active peptides which excite neurons, evoke behavioral responses, are potent vasodilators and secretagogues, and contract (directly or indirectly) many smooth muscles. PTM: The substance P form is cleaved at Pro-59 by the prolyl endopeptidase FAP (seprase) activity (in vitro). {ECO:0000250|UniProtKB:P20366}. SUBCELLULAR LOCATION: Secreted. +Q9JHB3 TIMP4_MOUSE Metalloproteinase inhibitor 4 (Tissue inhibitor of metalloproteinases 4) (TIMP-4) 224 25,774 Chain (1); Disulfide bond (6); Domain (1); Metal binding (1); Region (2); Sequence conflict (3); Signal peptide (1); Site (1) FUNCTION: Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Expressed in brain, heart, ovary and skeletal muscle. +Q99JT6 TLCD1_MOUSE Calfacilitin (TLC domain-containing protein 1) 247 28,787 Alternative sequence (4); Chain (1); Domain (1); Intramembrane (1); Sequence conflict (1); Signal peptide (1); Topological domain (6); Transmembrane (4) INTRAMEM 124 144 Helical. {ECO:0000255}. TRANSMEM 47 67 Helical. {ECO:0000255}.; TRANSMEM 84 104 Helical. {ECO:0000255}.; TRANSMEM 174 194 Helical. {ECO:0000255}.; TRANSMEM 202 222 Helical. {ECO:0000255}. TOPO_DOM 28 46 Extracellular. {ECO:0000255}.; TOPO_DOM 68 83 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 105 123 Extracellular. {ECO:0000255}.; TOPO_DOM 145 173 Extracellular. {ECO:0000255}.; TOPO_DOM 195 201 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 223 247 Extracellular. {ECO:0000255}. FUNCTION: Calcium channel facilitator that increases calcium flux by generating a larger window current and slowing inactivation of the L-type CACNA1C/CaV1.2 channel. Regulation of intracellular calcium by Calfacilitin is required for neural plate formation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with CACNA1C. {ECO:0000250}. +Q99MX0 TKTL1_MOUSE Transketolase-like protein 1 (EC 2.2.1.1) (Transketolase 2) (TK 2) 595 65,245 Active site (1); Binding site (5); Chain (1); Metal binding (3); Nucleotide binding (1); Sequence conflict (2) FUNCTION: Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P51854}. Nucleus {ECO:0000250|UniProtKB:P51854}. Note=Predominantly cytoplasmic and to a lesser extent also nuclear. {ECO:0000250|UniProtKB:P51854}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P23254}. +Q08122 TLE3_MOUSE Transducin-like enhancer protein 3 (ESG) (Grg-3) 772 83,447 Alternative sequence (3); Chain (1); Modified residue (19); Motif (1); Region (4); Repeat (7); Sequence conflict (2) FUNCTION: Transcriptional corepressor that binds to a number of transcription factors. Inhibits the transcriptional activation mediated by CTNNB1 and TCF family members in Wnt signaling. The effects of full-length TLE family members may be modulated by association with dominant-negative AES (By similarity). May play an important role during spermatogenesis. {ECO:0000250}. PTM: Ubiquitinated by XIAP/BIRC4. This ubiquitination does not affect its stability, nuclear localization, or capacity to tetramerize but inhibits its interaction with TCF7L2/TCF4 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Homotetramer and heterooligomer with other family members. Binds FOXA2 (By similarity). Interacts with XIAP/BIRC4 (By similarity). Binds LEF1, TCF7, TCF7L1 and TCF7L2/TCF4. Interacts with TBX18 (via engrailed homology 1 repressor motif), leading to decreased of TBX18 transcriptional activity. {ECO:0000250, ECO:0000269|PubMed:11266540, ECO:0000269|PubMed:17584735}. DOMAIN: WD repeat Groucho/TLE family members are characterized by 5 regions, a glutamine-rich Q domain, a glycine/proline-rich GP domain, a central CcN domain, containing a nuclear localization signal, and a serine/proline-rich SP domain. The most highly conserved are the N-terminal Q domain and the C-terminal WD-repeat domain. {ECO:0000305|PubMed:18254933}. TISSUE SPECIFICITY: Expressed only in testis. +Q5NCI0 URGCP_MOUSE Up-regulator of cell proliferation (HBV X protein up-regulated gene 4 protein homolog) (HBxAg up-regulated gene 4 protein homolog) 926 104,683 Alternative sequence (1); Chain (1); Domain (1); Frameshift (1); Modified residue (1); Sequence caution (1); Sequence conflict (4) FUNCTION: May be involved in cell cycle progression through the regulation of cyclin D1 expression. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8TCY9}. Nucleus {ECO:0000250|UniProtKB:Q8TCY9}. Note=In epithelial cells localized predominantly in the cytoplasm and occasionally in nuclei. {ECO:0000250}. +P25688 URIC_MOUSE Uricase (EC 1.7.3.3) (Urate oxidase) 303 35,039 Active site (3); Binding site (2); Chain (1); Initiator methionine (1); Modified residue (21); Motif (1); Region (2) Purine metabolism; urate degradation; (S)-allantoin from urate: step 1/3. FUNCTION: Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin. PTM: Acetylation of Lys-118, Lys-164 and Lys-290 is observed in liver mitochondria from fasted mice but not from fed mice. May be deacetylated by Sirt5; however it is unclear whether Sirt5 mediates deacetylation or desuccinylation of Uox; additional evidence is required to validate these results (PubMed:23085393). {ECO:0000269|PubMed:23085393, ECO:0000269|Ref.3}. SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:23085393}. Mitochondrion {ECO:0000269|PubMed:23085393}. +Q91X17 UROM_MOUSE Uromodulin (Tamm-Horsfall urinary glycoprotein) (THP) [Cleaved into: Uromodulin, secreted form] 642 70,845 Chain (2); Disulfide bond (17); Domain (4); Glycosylation (10); Lipidation (1); Propeptide (1); Region (3); Sequence conflict (14); Signal peptide (1); Site (1) FUNCTION: Uromodulin: Functions in biogenesis and organization of the apical membrane of epithelial cells of the thick ascending limb of Henle's loop (TALH), where it promotes formation of complex filamentous gel-like structure that may play a role in the water barrier permeability. May serve as a receptor for binding and endocytosis of cytokines (IL-1, IL-2) and TNF. Facilitates neutrophil migration across renal epithelia. {ECO:0000250|UniProtKB:P07911}.; FUNCTION: Uromodulin, secreted form: In the urine, may contribute to colloid osmotic pressure, retards passage of positively charged electrolytes, prevents urinary tract infection and inhibits formation of liquid containing supersaturated salts and subsequent formation of salt crystals. {ECO:0000269|PubMed:14871399, ECO:0000269|PubMed:15327412}. PTM: N-glycosylated. {ECO:0000269|PubMed:12021773, ECO:0000269|PubMed:26673890}.; PTM: Proteolytically cleaved at a conserved C-terminal proteolytic cleavage site to generate the secreted form found in urine (PubMed:18375198). This cleavage is catalyzed by HPN (PubMed:26673890). {ECO:0000269|PubMed:18375198, ECO:0000269|PubMed:26673890}. SUBCELLULAR LOCATION: Uromodulin, secreted form: Secreted {ECO:0000269|PubMed:26673890}. Note=Detected in urine. {ECO:0000269|PubMed:26673890}.; SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:26673890}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P07911}. Basolateral cell membrane {ECO:0000250|UniProtKB:P07911}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P07911}. Cell projection, cilium membrane {ECO:0000250|UniProtKB:P07911}. Note=Only a small fraction sorts to the basolateral pole of tubular epithelial cells compared to apical localization. Secreted into urine after cleavage. Colocalizes with NPHP1 and KIF3A. {ECO:0000250|UniProtKB:P07911}. SUBUNIT: Uromodulin, secreted form: homodimer that then polymerizes into long filaments. {ECO:0000269|PubMed:26673890}. DOMAIN: The ZP domain mediates polymerization, leading to the formation of long filaments. {ECO:0000269|PubMed:12021773, ECO:0000269|PubMed:26673890}. TISSUE SPECIFICITY: Detected in urine (secreted form). Detected in kidney thick ascending limb epithelial cells (at protein level). {ECO:0000269|PubMed:26673890}. +Q80XC3 US6NL_MOUSE USP6 N-terminal-like protein 819 93,574 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (1); Frameshift (1); Modified residue (14); Sequence conflict (2) FUNCTION: Acts as a GTPase-activating protein for RAB5A and RAB43. Involved in receptor trafficking. In complex with EPS8 inhibits internalization of EGFR. Involved in retrograde transport from the endocytic pathway to the Golgi apparatus. Involved in the transport of Shiga toxin from early and recycling endosomes to the trans-Golgi network. Required for structural integrity of the Golgi complex (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. SUBUNIT: Interacts with EPS8. {ECO:0000250}. +Q8VHL0 UT1_MOUSE Urea transporter 1 (Solute carrier family 14 member 1) (Urea transporter B) (UT-B) (Urea transporter, erythrocyte) 384 42,126 Alternative sequence (1); Chain (1); Glycosylation (1); Intramembrane (4); Modified residue (1); Sequence conflict (2); Site (1); Transmembrane (8) INTRAMEM 47 64 Helical. {ECO:0000250}.; INTRAMEM 68 83 Helical. {ECO:0000250}.; INTRAMEM 215 229 Helical. {ECO:0000250}.; INTRAMEM 234 245 Helical. {ECO:0000250}. TRANSMEM 86 105 Helical. {ECO:0000250}.; TRANSMEM 110 132 Helical. {ECO:0000250}.; TRANSMEM 139 163 Helical. {ECO:0000250}.; TRANSMEM 168 188 Helical. {ECO:0000250}.; TRANSMEM 250 269 Helical. {ECO:0000250}.; TRANSMEM 279 299 Helical. {ECO:0000250}.; TRANSMEM 304 325 Helical. {ECO:0000250}.; TRANSMEM 328 348 Helical. {ECO:0000250}. FUNCTION: Urea channel that facilitates transmembrane urea transport down a concentration gradient. A constriction of the transmembrane channel functions as selectivity filter through which urea is expected to pass in dehydrated form. The rate of urea conduction is increased by hypotonic stress. Plays an important role in the kidney medulla collecting ducts, where it allows rapid equilibration between the lumen of the collecting ducts and the interstitium, and thereby prevents water loss driven by the high concentration of urea in the urine. Facilitates urea transport across erythrocyte membranes. May also play a role in transmembrane water transport, possibly by indirect means. {ECO:0000269|PubMed:11792714, ECO:0000269|PubMed:12133842}. PTM: N-glycosylated in red blood cells, as well as in most non-erythroid tissues, except in the gastrocnemius muscle and in the gastrointestinal tract, including liver, colon and stomach. {ECO:0000269|PubMed:15563580}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Basolateral cell membrane; Multi-pass membrane protein. Note=Restricted to the basolateral membrane in various portions of the urothelium. SUBUNIT: Homotrimer; each subunit contains a pore through which urea permeates. Identified in a complex with STOM (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain, kidney, heart, liver, lung, skeletal muscle, spleen, testis, ureter and urinary bladder (at protein level). Along the gastrointestinal tract, detected in colon, jejunum and stomach (at protein level). In the kidney, expressed in some microvessels of the inner and outer medulla, but not all (at protein level). Not detected in the cortex (at protein level). Detected in the urothelium all along the urinary tract, including the papilla surface, the ureter, the bladder and the urethra (at protein level). In the brain, expressed at the border of the corpus callosum and striatum in astrocytic cellular processes surrounding blood microvessels (at protein level). Detected in erythrocytes (at protein level). {ECO:0000269|PubMed:11792714, ECO:0000269|PubMed:12133842, ECO:0000269|PubMed:15563580}. +Q5XG71 UTP20_MOUSE Small subunit processome component 20 homolog (Down-regulated in metastasis protein) 2788 317,744 Chain (1); Coiled coil (1); Compositional bias (2); Erroneous initiation (1); Frameshift (1); Modified residue (2); Repeat (2); Sequence caution (1); Sequence conflict (4) FUNCTION: Involved in 18S pre-rRNA processing. Associates with U3 snoRNA (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Note=Colocalizes with NCL in the nucleolus. {ECO:0000250}. SUBUNIT: Interacts with FBL and PPP1R26. {ECO:0000250}. +Q9Z1Z0 USO1_MOUSE General vesicular transport factor p115 (Protein USO1 homolog) (Transcytosis-associated protein) (TAP) (Vesicle-docking protein) 959 106,983 Alternative sequence (4); Chain (1); Coiled coil (1); Compositional bias (1); Modified residue (3); Region (1); Repeat (12); Sequence conflict (3) FUNCTION: General vesicular transport factor required for intercisternal transport in the Golgi stack; it is required for transcytotic fusion and/or subsequent binding of the vesicles to the target membrane. May well act as a vesicular anchor by interacting with the target membrane and holding the vesicular and target membranes in proximity. {ECO:0000250|UniProtKB:P41542}. PTM: Phosphorylated in a cell cycle-specific manner; phosphorylated in interphase but not in mitotic cells. Dephosphorylated protein associates with the Golgi membrane; phosphorylation promostes dissociation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Recycles between the cytosol and the Golgi apparatus during interphase. {ECO:0000250}. SUBUNIT: Homodimer. Dimerizes by parallel association of the tails, resulting in an elongated structure with two globular head domains side by side, and a long rod-like tail structure. Interacts with MIF (By similarity). {ECO:0000250}. DOMAIN: Composed of a globular head, an elongated tail (coiled-coil) and a highly acidic C-terminal domain. +Q9EQ46 V1R40_MOUSE Vomeronasal type-1 receptor 40 (Vomeronasal type-1 receptor A11) (Vomeronasal type-1 receptor B7) 310 35,207 Chain (1); Disulfide bond (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 21 41 Helical; Name=1. {ECO:0000255}.; TRANSMEM 51 71 Helical; Name=2. {ECO:0000255}.; TRANSMEM 94 114 Helical; Name=3. {ECO:0000255}.; TRANSMEM 135 155 Helical; Name=4. {ECO:0000255}.; TRANSMEM 191 211 Helical; Name=5. {ECO:0000255}.; TRANSMEM 239 259 Helical; Name=6. {ECO:0000255}.; TRANSMEM 269 289 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 20 Extracellular. {ECO:0000255}.; TOPO_DOM 42 50 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 72 93 Extracellular. {ECO:0000255}.; TOPO_DOM 115 134 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 156 190 Extracellular. {ECO:0000255}.; TOPO_DOM 212 238 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 260 268 Extracellular. {ECO:0000255}.; TOPO_DOM 290 310 Cytoplasmic. {ECO:0000255}. FUNCTION: Putative pheromone receptor implicated in the regulation of social and reproductive behavior. {ECO:0000269|PubMed:12214233}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. +Q8VBS7 V1R42_MOUSE Vomeronasal type-1 receptor 42 (Vomeronasal type-1 receptor A1) (Vomeronasal type-1 receptor A10) (Vomeronasal type-1 receptor A3) (Vomeronasal type-1 receptor A6) 329 37,352 Chain (1); Disulfide bond (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 33 53 Helical; Name=1. {ECO:0000255}.; TRANSMEM 66 86 Helical; Name=2. {ECO:0000255}.; TRANSMEM 110 130 Helical; Name=3. {ECO:0000255}.; TRANSMEM 151 171 Helical; Name=4. {ECO:0000255}.; TRANSMEM 210 230 Helical; Name=5. {ECO:0000255}.; TRANSMEM 255 275 Helical; Name=6. {ECO:0000255}.; TRANSMEM 286 306 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 32 Extracellular. {ECO:0000255}.; TOPO_DOM 54 65 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 87 109 Extracellular. {ECO:0000255}.; TOPO_DOM 131 150 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 172 209 Extracellular. {ECO:0000255}.; TOPO_DOM 231 254 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 276 285 Extracellular. {ECO:0000255}.; TOPO_DOM 307 329 Cytoplasmic. {ECO:0000255}. FUNCTION: Putative pheromone receptor implicated in the regulation of social and reproductive behavior. {ECO:0000269|PubMed:12214233}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. +Q8VIC7 V1R45_MOUSE Vomeronasal type-1 receptor 45 (Pheromone receptor 2) (Vomeronasal type-1 receptor A2) (mV1R2) (Vomeronasal type-1 receptor A9) 318 36,348 Chain (1); Disulfide bond (1); Erroneous initiation (1); Glycosylation (1); Sequence conflict (1); Topological domain (8); Transmembrane (7) TRANSMEM 33 53 Helical; Name=1. {ECO:0000255}.; TRANSMEM 66 86 Helical; Name=2. {ECO:0000255}.; TRANSMEM 110 130 Helical; Name=3. {ECO:0000255}.; TRANSMEM 151 171 Helical; Name=4. {ECO:0000255}.; TRANSMEM 207 227 Helical; Name=5. {ECO:0000255}.; TRANSMEM 255 275 Helical; Name=6. {ECO:0000255}.; TRANSMEM 286 306 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 32 Extracellular. {ECO:0000255}.; TOPO_DOM 54 65 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 87 109 Extracellular. {ECO:0000255}.; TOPO_DOM 131 150 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 172 206 Extracellular. {ECO:0000255}.; TOPO_DOM 228 254 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 276 285 Extracellular. {ECO:0000255}.; TOPO_DOM 307 318 Cytoplasmic. {ECO:0000255}. FUNCTION: Putative pheromone receptor implicated in the regulation of social and reproductive behavior. {ECO:0000269|PubMed:12214233}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Expressed in a subset of sensory neurons located in the apical layer of the vomeronasal organ. {ECO:0000269|PubMed:9757043}. +Q9EQ45 V1R46_MOUSE Vomeronasal type-1 receptor 46 (Vomeronasal type-1 receptor A13) (Vomeronasal type-1 receptor B8) 309 35,006 Chain (1); Disulfide bond (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 21 41 Helical; Name=1. {ECO:0000255}.; TRANSMEM 51 71 Helical; Name=2. {ECO:0000255}.; TRANSMEM 86 106 Helical; Name=3. {ECO:0000255}.; TRANSMEM 135 155 Helical; Name=4. {ECO:0000255}.; TRANSMEM 193 213 Helical; Name=5. {ECO:0000255}.; TRANSMEM 238 258 Helical; Name=6. {ECO:0000255}.; TRANSMEM 268 288 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 20 Extracellular. {ECO:0000255}.; TOPO_DOM 42 50 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 72 85 Extracellular. {ECO:0000255}.; TOPO_DOM 107 134 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 156 192 Extracellular. {ECO:0000255}.; TOPO_DOM 214 237 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 259 267 Extracellular. {ECO:0000255}.; TOPO_DOM 289 309 Cytoplasmic. {ECO:0000255}. FUNCTION: Putative pheromone receptor implicated in the regulation of social and reproductive behavior. {ECO:0000269|PubMed:12214233}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. +P51863 VA0D1_MOUSE V-type proton ATPase subunit d 1 (V-ATPase subunit d 1) (P39) (Physophilin) (V-ATPase 40 kDa accessory protein) (V-ATPase AC39 subunit) (Vacuolar proton pump subunit d 1) 351 40,301 Chain (1); Modified residue (2); Sequence conflict (1) FUNCTION: Subunit of the integral membrane V0 complex of vacuolar ATPase. Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells, thus providing most of the energy required for transport processes in the vacuolar system. May play a role in coupling of proton transport and ATP hydrolysis. May play a role in cilium biogenesis through regulation of the transport and the localization of proteins to the cilium (By similarity). In aerobic conditions, involved in intracellular iron homeostasis, thus triggering the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent proteasomal degradation (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P61421, ECO:0000269|PubMed:12963731}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Localizes to centrosome and the base of the cilium. {ECO:0000250}. SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'' and d). TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12527205, ECO:0000269|PubMed:12963731}. +Q80SY3 VA0D2_MOUSE V-type proton ATPase subunit d 2 (V-ATPase subunit d 2) (Osteoclast-specific vacuolar ATP synthase) (Vacuolar proton pump subunit d 2) 350 40,494 Chain (1); Sequence conflict (4) FUNCTION: Subunit of the integral membrane V0 complex of vacuolar ATPase. Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells, thus providing most of the energy required for transport processes in the vacuolar system (By similarity). May play a role in coupling of proton transport and ATP hydrolysis. Regulator of osteoclast fusion and bone formation. {ECO:0000250, ECO:0000269|PubMed:12963731, ECO:0000269|PubMed:17128270}. SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'' and d). TISSUE SPECIFICITY: Predominantly expressed in the kidney. Also expressed in the lung, testis, skeletal muscle and heart. Upr-egulated during osteoclast differentiation and is most abundant in mature osteoclasts. {ECO:0000269|PubMed:12527205, ECO:0000269|PubMed:12963731, ECO:0000269|PubMed:17128270}. +Q9QY76 VAPB_MOUSE Vesicle-associated membrane protein-associated protein B (VAMP-B) (VAMP-associated protein B) (VAP-B) (VAMP-associated protein 33b) 243 26,946 Chain (1); Coiled coil (1); Cross-link (1); Domain (1); Initiator methionine (1); Modified residue (5); Topological domain (1); Transmembrane (1) TRANSMEM 219 239 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 2 218 Cytoplasmic. {ECO:0000255}. FUNCTION: Participates in the endoplasmic reticulum unfolded protein response (UPR) by inducing ERN1/IRE1 activity. Involved in cellular calcium homeostasis regulation. {ECO:0000250|UniProtKB:O95292}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O95292}; Single-pass type IV membrane protein {ECO:0000255}. SUBUNIT: Homodimer, and heterodimer with VAPA. Interacts with RMDN3, VAMP1 and VAMP2 (By similarity). Interacts (via MSP domain) with ZFYVE27 (PubMed:24251978). Interacts with KIF5A in a ZFYVE27-dependent manner (By similarity). Interacts with STARD3 (via FFAT motif) (By similarity). Interacts with STARD3NL (via FFAT motif) (By similarity). {ECO:0000250|UniProtKB:O95292, ECO:0000269|PubMed:24251978}. +Q9Z2P8 VAMP5_MOUSE Vesicle-associated membrane protein 5 (VAMP-5) (Myobrevin) 102 11,416 Chain (1); Domain (1); Modified residue (3); Topological domain (2); Transmembrane (1) TRANSMEM 73 93 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 1 72 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 94 102 Vesicular. {ECO:0000255}. FUNCTION: May participate in trafficking events that are associated with myogenesis, such as myoblast fusion and/or GLUT4 trafficking. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}. Endomembrane system {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}. Golgi apparatus, trans-Golgi network membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}. Note=Associated with the plasma membrane as well as intracellular perinuclear and peripheral vesicular structures of myotubes. Associated with the trans-Golgi, but not with the cis-Golgi apparatus. TISSUE SPECIFICITY: Preferentially expressed in the skeletal muscle and heart, detected at lower levels in several other tissues but not in the brain. +P70280 VAMP7_MOUSE Vesicle-associated membrane protein 7 (VAMP-7) (Synaptobrevin-like protein 1) 220 24,967 Beta strand (6); Chain (1); Compositional bias (1); Domain (2); Helix (5); Initiator methionine (1); Modified residue (3); Topological domain (2); Transmembrane (1); Turn (2) TRANSMEM 189 209 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 2 188 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 210 220 Vesicular. {ECO:0000255}. FUNCTION: Involved in the targeting and/or fusion of transport vesicles to their target membrane during transport of proteins from the early endosome to the lysosome. Required for heterotypic fusion of late endosomes with lysosomes and homotypic lysosomal fusion. Required for calcium regulated lysosomal exocytosis. Involved in the export of chylomicrons from the endoplasmic reticulum to the cis Golgi. Required for exocytosis of mediators during eosinophil and neutrophil degranulation, and target cell killing by natural killer cells. Required for focal exocytosis of late endocytic vesicles during phagosome formation. {ECO:0000269|PubMed:15470500}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane; Single-pass type IV membrane protein. Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Late endosome membrane; Single-pass type IV membrane protein. Lysosome membrane; Single-pass type IV membrane protein. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Cytoplasmic vesicle, phagosome membrane; Single-pass type IV membrane protein. Cell junction, synapse, synaptosome. Note=In immature neurons expression is localized in vesicular structures in axons and dendrites while in mature neurons it is localized to the somatodendritic region. Colocalizes with LAMP1 in kidney cells. Localization to the endoplasmic reticulum membrane was observed in the intestine but not in liver or kidney (By similarity). {ECO:0000250}. SUBUNIT: Component of the SNARE complex composed of STX4, SNAP23 and VAMP7 that binds SYT7 during lysosomal exocytosis. Component of the SNARE complex composed of STX7, STX8, VAMP7 and VTI1B that is required for heterotypic fusion of late endosomes with lysosomes (By similarity). May interact with STX17. {ECO:0000250}. +O70404 VAMP8_MOUSE Vesicle-associated membrane protein 8 (VAMP-8) (Endobrevin) (Edb) 101 11,451 Chain (1); Domain (1); Helix (1); Modified residue (7); Mutagenesis (2); Sequence conflict (2); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 76 96 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 1 75 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 97 101 Vesicular. {ECO:0000255}. FUNCTION: SNAREs, soluble N-ethylmaleimide-sensitive factor-attachment protein receptors, are essential proteins for fusion of cellular membranes. SNAREs localized on opposing membranes assemble to form a trans-SNARE complex, an extended, parallel four alpha-helical bundle that drives membrane fusion. VAMP8 is a SNARE involved in autophagy through the direct control of autophagosome membrane fusion with the lysososome membrane via its interaction with the STX17-SNAP29 binary t-SNARE complex (By similarity). Also required for dense-granule secretion in platelets (By similarity). Plays also a role in regulated enzyme secretion in pancreatic acinar cells (PubMed:15363411). Involved in the abscission of the midbody during cell division, which leads to completely separate daughter cells (By similarity). Involved in the homotypic fusion of early and late endosomes (By similarity). {ECO:0000250|UniProtKB:Q9BV40, ECO:0000269|PubMed:15363411, ECO:0000269|PubMed:22118466}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:27628032}; Single-pass type IV membrane protein {ECO:0000305}. Late endosome membrane {ECO:0000250|UniProtKB:Q9WUF4}; Single-pass type IV membrane protein {ECO:0000305}. Early endosome membrane {ECO:0000250|UniProtKB:Q9WUF4}; Single-pass type IV membrane protein {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:22118466}; Single-pass type IV membrane protein {ECO:0000305}. Note=Perinuclear vesicular structures of the early and late endosomes, coated pits, and trans-Golgi (By similarity). Sub-tight junctional domain in retinal pigment epithelium cells (By similarity). Midbody region during cytokinesis (By similarity). Lumenal oriented, apical membranes of nephric tubular cell (By similarity). Cycles through the apical but not through the basolateral plasma membrane (By similarity). Apical region of acinar cells; in zymogen granule membranes (PubMed:9614193). {ECO:0000250|UniProtKB:Q9WUF4, ECO:0000269|PubMed:9614193}. SUBUNIT: Forms a SNARE complex composed of VAMP8, SNAP29 and STX17 involved in fusion of autophagosome with lysosome (By similarity). Found in a number of SNARE complexes with NAPA, SNAP23, SNAP25, STX1A, STX4, STX7, STX8 and VTI1B (PubMed:15363411). Interacts with CALM (PubMed:22118466). SNARE complex formation and binding by CALM are mutually exclusive processes for VAMP8 (PubMed:22118466). {ECO:0000250|UniProtKB:Q9BV40, ECO:0000269|PubMed:15363411, ECO:0000269|PubMed:22118466}. TISSUE SPECIFICITY: Expressed abundantly in the kidney, less in the liver, brain, kidney, heart, lung, pancreas and placenta. {ECO:0000269|PubMed:15363411, ECO:0000269|PubMed:9553086}. +Q8VHK8 TM11D_MOUSE Transmembrane protease serine 11D (EC 3.4.21.-) (Adrenal secretory serine protease) (AsP) (Airway trypsin-like protease) (AT) [Cleaved into: Transmembrane protease serine 11D non-catalytic chain; Transmembrane protease serine 11D catalytic chain] 417 46,254 Active site (3); Alternative sequence (2); Beta strand (4); Chain (2); Disulfide bond (4); Domain (2); Helix (4); Sequence conflict (1); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 18 38 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 17 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 39 417 Extracellular. {ECO:0000255}. FUNCTION: May play some biological role in the host defense system on the mucous membrane independently of or in cooperation with other substances in airway mucous or bronchial secretions. Preferentially cleaves the C-terminal side of arginine residues at the P1 position of certain peptides (By similarity). Plays a role in the proteolytic processing of ACE2. Isoform 2 may play a key role in regulating adrenal proliferation by specifically cleaving N-POMC. {ECO:0000250, ECO:0000269|PubMed:24227843}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: Transmembrane protease serine 11D catalytic chain: Secreted {ECO:0000250}. Note=Activated by cleavage and secreted. {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in the esophagus, tongue, and trachea, low expression was seen in heart, lung, and adrenal gland. Isoform 2 is also highly expressed in the adrenal gland. {ECO:0000269|PubMed:14691009}. +Q8C996 TM163_MOUSE Transmembrane protein 163 (Synaptic vesicle membrane protein of 31 kDa) 288 31,193 Chain (1); Modified residue (5); Sequence conflict (2); Topological domain (7); Transmembrane (6) TRANSMEM 88 108 Helical. {ECO:0000255}.; TRANSMEM 116 136 Helical. {ECO:0000255}.; TRANSMEM 150 170 Helical. {ECO:0000255}.; TRANSMEM 187 207 Helical. {ECO:0000255}.; TRANSMEM 217 237 Helical. {ECO:0000255}.; TRANSMEM 255 275 Helical. {ECO:0000255}. TOPO_DOM 1 87 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 109 115 Extracellular. {ECO:0000255}.; TOPO_DOM 137 149 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 171 186 Extracellular. {ECO:0000255}.; TOPO_DOM 208 216 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 238 254 Extracellular. {ECO:0000255}.; TOPO_DOM 276 288 Cytoplasmic. {ECO:0000255}. FUNCTION: May bind zinc and other divalent cations and recruit them to vesicular organelles. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:17623043}; Multi-pass membrane protein {ECO:0000269|PubMed:17623043}. Early endosome membrane {ECO:0000250}. Note=Glutamatergic synaptic vesicles. TISSUE SPECIFICITY: Specifically expressed in brain. Mainly expressed in the glutaminergic neuron subpopulations. {ECO:0000269|PubMed:17623043}. +A2AJB2 TM141_MOUSE Transmembrane protein 141 108 11,893 Chain (1); Frameshift (1); Transmembrane (2) TRANSMEM 30 52 Helical. {ECO:0000255}.; TRANSMEM 59 78 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q3V0J1 TM237_MOUSE Transmembrane protein 237 (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 4 protein homolog) 427 47,343 Alternative sequence (3); Chain (1); Modified residue (2); Transmembrane (4) TRANSMEM 252 272 Helical. {ECO:0000255}.; TRANSMEM 290 310 Helical. {ECO:0000255}.; TRANSMEM 325 345 Helical. {ECO:0000255}.; TRANSMEM 375 395 Helical. {ECO:0000255}. FUNCTION: Component of the transition zone in primary cilia. Required for ciliogenesis. {ECO:0000269|PubMed:22152675}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cell projection, cilium {ECO:0000269|PubMed:22152675}. Note=Localizes at the proximal region of primary cilia were observed, consistent with localization to the transition zone. SUBUNIT: Part of the tectonic-like complex (also named B9 complex). Interacts with TMEM107. {ECO:0000250|UniProtKB:Q96Q45}. +Q9CQE2 TM223_MOUSE Transmembrane protein 223 199 21,857 Chain (1); Transmembrane (2) TRANSMEM 44 64 Helical. {ECO:0000255}.; TRANSMEM 95 115 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8CHQ6 TM125_MOUSE Transmembrane protein 125 216 22,055 Chain (1); Erroneous initiation (1); Frameshift (1); Sequence conflict (5); Transmembrane (4) TRANSMEM 32 52 Helical. {ECO:0000255}.; TRANSMEM 65 85 Helical. {ECO:0000255}.; TRANSMEM 111 131 Helical. {ECO:0000255}.; TRANSMEM 144 164 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8C1Z8 TM10A_MOUSE tRNA methyltransferase 10 homolog A (EC 2.1.1.221) (RNA (guanine-9-)-methyltransferase domain-containing protein 2) (tRNA (guanine(9)-N(1))-methyltransferase TRMT10A) 328 37,966 Chain (1); Coiled coil (1); Domain (1); Erroneous initiation (3); Modified residue (1); Sequence caution (1); Sequence conflict (12) FUNCTION: S-adenosyl-L-methionine-dependent guanine N(1)-methyltransferase that catalyzes the formation of N(1)-methylguanine at position 9 (m1G9) in tRNAs. Probably not able to catalyze formation of N(1)-methyladenine at position 9 (m1A9) in tRNAs. {ECO:0000250|UniProtKB:Q8TBZ6}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8TBZ6}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q8TBZ6}. SUBUNIT: Interacts with tRNA. {ECO:0000250|UniProtKB:Q8TBZ6}. +Q8BGP5 TM127_MOUSE Transmembrane protein 127 238 25,835 Chain (1); Modified residue (2); Transmembrane (3) TRANSMEM 96 116 Helical. {ECO:0000255}.; TRANSMEM 130 150 Helical. {ECO:0000255}.; TRANSMEM 169 189 Helical. {ECO:0000255}. FUNCTION: Controls cell proliferation acting as a negative regulator of TOR signaling pathway mediated by mTORC1. May act as a tumor suppressor. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Association of TMEM127 with the cell membrane is enhanced by inhibition of endocytosis. In the cytoplasm, it colocalizes with markers of early endosomal structures, Golgi apparatus and lysosomes. {ECO:0000250}. +Q9DCX7 TM174_MOUSE Transmembrane protein 174 243 26,449 Chain (1); Sequence conflict (1); Transmembrane (2) TRANSMEM 40 60 Helical. {ECO:0000255}.; TRANSMEM 73 93 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q8K304 TM129_MOUSE E3 ubiquitin-protein ligase TM129 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase TM129) 362 40,628 Alternative sequence (1); Chain (1); Sequence conflict (2); Topological domain (4); Transmembrane (3); Zinc finger (1) TRANSMEM 7 27 Helical. {ECO:0000255}.; TRANSMEM 57 77 Helical. {ECO:0000255}.; TRANSMEM 95 115 Helical. {ECO:0000255}. TOPO_DOM 1 6 Lumenal. {ECO:0000255}.; TOPO_DOM 28 56 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 78 94 Lumenal. {ECO:0000255}.; TOPO_DOM 116 362 Cytoplasmic. {ECO:0000255}. Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase involved in ER-associated protein degradation, preferentially associates with the E2 enzyme UBE2J2. Exploited by viral US11 proteins to mediate HLA class I proteins degradation. {ECO:0000250|UniProtKB:A0AVI4}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:A0AVI4}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A0AVI4}. SUBUNIT: Integral component of ER-resident dislocation complexes. {ECO:0000250|UniProtKB:A0AVI4}. DOMAIN: The RING-type zinc finger domain is responsible for E3 ubiquitin ligase activity. {ECO:0000250|UniProtKB:A0AVI4}. +Q6NXM3 TM130_MOUSE Transmembrane protein 130 419 46,628 Chain (1); Domain (1); Erroneous initiation (1); Glycosylation (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 337 357 Helical. {ECO:0000255}. TOPO_DOM 26 336 Extracellular. {ECO:0000255}.; TOPO_DOM 358 419 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. +Q3U145 TMM64_MOUSE Transmembrane protein 64 381 39,815 Chain (1); Frameshift (1); Region (1); Sequence conflict (5); Transmembrane (6) TRANSMEM 52 72 Helical. {ECO:0000255}.; TRANSMEM 85 105 Helical. {ECO:0000255}.; TRANSMEM 121 141 Helical. {ECO:0000255}.; TRANSMEM 161 181 Helical. {ECO:0000255}.; TRANSMEM 189 209 Helical. {ECO:0000255}.; TRANSMEM 310 330 Helical. {ECO:0000255}. FUNCTION: Positively regulates TNFSF11-induced osteoclast differentiation. Acts as a regulator of TNFSF11-mediated Ca(2+) signaling pathways via its interaction with SERCA2 which is critical for the TNFSF11-induced CREB1 activation and mitochondrial ROS generation necessary for proper osteoclast generation. Association between TMEM64 and SERCA2 in the ER leads to cytosolic Ca (2+) spiking for activation of NFATC1 and production of mitochondrial ROS, thereby triggering Ca (2+) signaling cascades that promote osteoclast differentiation and activation (PubMed:23395171). Negatively regulates osteoblast differentiation and positively regulates adipocyte differentiation via modulation of the canonical Wnt signaling pathway. Mediates the switch in lineage commitment to osteogenesis rather than to adipogenesis in mesenchymal stem cells by negatively regulating the expression, activity and nuclear localization of CTNNB1 (PubMed:25979161). {ECO:0000269|PubMed:23395171, ECO:0000269|PubMed:25979161}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum {ECO:0000269|PubMed:23395171}. SUBUNIT: Interacts with ATP2A2 (PubMed:23395171). {ECO:0000269|PubMed:23395171}. DOMAIN: The VTT domain was previously called the SNARE-assoc domain. As there is no evidence that this domain associates with SNARE proteins, it was renamed as VMP1, TMEM41, and TVP38 (VTT) domain. {ECO:0000250|UniProtKB:P36164}. TISSUE SPECIFICITY: Liver, testis, kidney and muscle. {ECO:0000269|PubMed:23395171}. +Q9ESN3 TMM8A_MOUSE Post-GPI attachment to proteins factor 6 (EC 3.1.1.4) (GPI processing phospholipase A2) (GPI-PLA2) (M83 protein) (Transmembrane protein 8) (Transmembrane protein 8A) 769 85,329 Alternative sequence (1); Chain (1); Disulfide bond (3); Domain (1); Glycosylation (2); Sequence conflict (2); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 544 564 Helical. {ECO:0000255}.; TRANSMEM 568 588 Helical. {ECO:0000255}.; TRANSMEM 604 624 Helical. {ECO:0000255}.; TRANSMEM 628 648 Helical. {ECO:0000255}.; TRANSMEM 652 672 Helical. {ECO:0000255}.; TRANSMEM 689 709 Helical. {ECO:0000255}.; TRANSMEM 716 736 Helical. {ECO:0000255}. TOPO_DOM 34 543 Extracellular. {ECO:0000255}.; TOPO_DOM 565 567 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 589 603 Extracellular. {ECO:0000255}.; TOPO_DOM 625 627 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 649 651 Extracellular. {ECO:0000255}.; TOPO_DOM 673 688 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 710 715 Extracellular. {ECO:0000255}.; TOPO_DOM 737 769 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in the lipid remodeling steps of GPI-anchor maturation. Lipid remodeling steps consist in the generation of 2 saturated fatty chains at the sn-2 position of GPI-anchor proteins (GPI-AP). Has phospholipase A2 activity that removes an acyl-chain at the sn-2 position of GPI-anchors during the remodeling of GPI. Required for the shedding of the GPI-AP TDGF1, but not CFC1, at the cell surface. Shedding of TDGF1 modulates Nodal signaling by allowing soluble TDGF1 to act as a Nodal coreceptor on other cells. Also indirectly involved in the translocation of RAC1 from the cytosol to the plasma membrane by maintaining the steady state amount of CAV1-enriched plasma membrane subdomains, stabilizing RAC1 at the plasma membrane. {ECO:0000250|UniProtKB:Q9HCN3}. PTM: Glycosylated. {ECO:0000250|UniProtKB:Q9HCN3}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9HCN3}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:Q9HCN3}; Multi-pass membrane protein {ECO:0000255}. +Q921T2 TOIP1_MOUSE Torsin-1A-interacting protein 1 (Lamina-associated polypeptide 1B) (LAP1B) 595 66,781 Alternative sequence (2); Chain (1); Coiled coil (1); Compositional bias (1); Cross-link (1); Erroneous initiation (1); Glycosylation (1); Modified residue (12); Region (1); Sequence conflict (3); Topological domain (2); Transmembrane (1) TRANSMEM 352 372 Helical. {ECO:0000255}. TOPO_DOM 1 351 Nuclear. {ECO:0000255}.; TOPO_DOM 373 595 Perinuclear space. {ECO:0000255}. FUNCTION: Required for nuclear membrane integrity. Induces TOR1A and TOR1B ATPase activity and is required for their location on the nuclear membrane. Binds to A- and B-type lamins. Possible role in membrane attachment and assembly of the nuclear lamina. {ECO:0000269|PubMed:20457914}. SUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with ATP1B4. Interacts with TOR1A (ATP-bound). Interacts with TOR1B, TOR2A and TOR3A. Interacts with VIM. {ECO:0000269|PubMed:20457914}. TISSUE SPECIFICITY: Expressed in the spinal cord and liver (at protein level). {ECO:0000269|PubMed:16364897}. +Q5GIG6 TNI3K_MOUSE Serine/threonine-protein kinase TNNI3K (EC 2.7.11.1) (Cardiac ankyrin repeat kinase) (TNNI3-interacting kinase) 834 92,575 Active site (1); Alternative sequence (2); Binding site (1); Chain (1); Coiled coil (1); Compositional bias (1); Domain (1); Initiator methionine (1); Lipidation (1); Nucleotide binding (1); Repeat (10); Sequence conflict (2) FUNCTION: May play a role in cardiac physiology. {ECO:0000250|UniProtKB:Q59H18}. PTM: Autophosphorylated. {ECO:0000250|UniProtKB:Q59H18}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Expressed at lower levels in the cytoplasm. {ECO:0000250}. SUBUNIT: Interacts with TNNI3, ACTC, ACTA1, MYBPC3, AIP, BABP3 and HADHB. {ECO:0000250}. +Q3UHC0 TNR6C_MOUSE Trinucleotide repeat-containing gene 6C protein 1690 175,775 Chain (1); Coiled coil (1); Compositional bias (4); Domain (2); Erroneous initiation (1); Modified residue (5); Region (6); Sequence conflict (1) FUNCTION: Plays a role in RNA-mediated gene silencing by micro-RNAs (miRNAs). Required for miRNA-dependent translational repression of complementary mRNAs by argonaute family proteins As scaffoldng protein associates with argonaute proteins bound to partially complementary mRNAs and simultaneously can recruit CCR4-NOT and PAN deadenylase complexes (By similarity). {ECO:0000250}. SUBUNIT: Interacts with one or more of the argonaute family proteins AGO1, AGO2, AGO3 and AGO4. Interacts with CNOT1; the interaction mediates the association with the CCR4-NOT complex. Interacts with PAN3; the interaction mediates the association with the PAN complex (By similarity). {ECO:0000250}. DOMAIN: The silencing domain, also known as C-terminal effector domain (CED), can act in autonomous repression, including both translational inhibition and mRNA degradation. {ECO:0000250}. +O88746 TOM1_MOUSE Target of Myb protein 1 492 54,325 Alternative sequence (2); Chain (1); Cross-link (1); Domain (2); Modified residue (10) FUNCTION: May be involved in intracellular trafficking. Probable association with membranes. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. SUBUNIT: Interacts with ZFYVE16; interaction is required to target it to endosomes. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. In adult brain, it is highly expressed at the mesencephalic level, in the hippocampal formation and medial lemniscus. In cerebellum, it is highly expressed in Purkinje cells and granular layers. +Q9QZ06 TOLIP_MOUSE Toll-interacting protein 274 30,345 Chain (1); Compositional bias (1); Domain (2); Initiator methionine (1); Modified residue (2); Motif (2) FUNCTION: Component of the signaling pathway of IL-1 and Toll-like receptors. Inhibits cell activation by microbial products. Recruits IRAK1 to the IL-1 receptor complex. Inhibits IRAK1 phosphorylation and kinase activity. Connects the ubiquitin pathway to autophagy by functioning as a ubiquitin-ATG8 family adapter and thus mediating autophagic clearance of ubiquitin conjugates. The TOLLIP-dependent selective autophagy pathway plays an important role in clearance of cytotoxic polyQ proteins aggregates (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. SUBUNIT: Oligomerizes. Binds to TLR2 and the TLR4-MD2 complex via its C-terminus. Exists as complex with IRAK1 in unstimulated cells. Upon IL-1 signaling, Tollip binds to the activated IL-1 receptor complex containing IL-1RI, IL-1RacP and the adapter protein MyD88, where it interacts with the TIR domain of IL-1RacP. MyD88 then triggers IRAK1 autophosphorylation, which in turn leads to the dissociation of IRAK1 from Tollip and IL-1RAcP. Interacts with TOM1L2 (By similarity). Interacts with ATG8 family proteins (via the AIM motifs), and ubiquitin (via the CUE domain) (By similarity). {ECO:0000250}. DOMAIN: Both ATG8-interaction motifs (AIM1 and AIM2) are required for the association with ATG8 family proteins. {ECO:0000250}. TISSUE SPECIFICITY: Detected in heart, brain, spleen, lung, liver, skeletal muscle, kidney, thymus, pancreas and testis. +Q9CQN3 TOM6_MOUSE Mitochondrial import receptor subunit TOM6 homolog (Overexpressed breast tumor protein homolog) (Translocase of outer membrane 6 kDa subunit homolog) 74 7,865 Chain (1); Initiator methionine (1); Modified residue (1) SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250}. SUBUNIT: Forms part of the preprotein translocase complex of the outer mitochondrial membrane (TOM complex) which consists of at least 7 different proteins (TOMM5, TOMM6, TOMM7, TOMM20, TOMM22, TOMM40 and TOMM70). {ECO:0000250}. +P11214 TPA_MOUSE Tissue-type plasminogen activator (t-PA) (t-plasminogen activator) (tPA) (EC 3.4.21.68) [Cleaved into: Tissue-type plasminogen activator chain A; Tissue-type plasminogen activator chain B] 559 63,097 Active site (3); Chain (3); Disulfide bond (17); Domain (5); Glycosylation (2); Propeptide (2); Region (1); Sequence conflict (2); Signal peptide (1); Site (3) FUNCTION: Converts the abundant, but inactive, zymogen plasminogen to plasmin by hydrolyzing a single Arg-Val bond in plasminogen. By controlling plasmin-mediated proteolysis, it plays an important role in tissue remodeling and degradation, in cell migration and many other physiopathological events. PTM: The single chain, almost fully active enzyme, can be further processed into a two-chain fully active form by a cleavage after Arg-308 catalyzed by plasmin, tissue kallikrein or factor Xa. SUBCELLULAR LOCATION: Secreted, extracellular space. SUBUNIT: Heterodimer of chain A and chain B held by a disulfide bond. Binds to fibrin with high affinity. This interaction leads to an increase in the catalytic efficiency of the enzyme due to an increase in affinity for plasminogen. Similarly, binding to heparin increases the activation of plasminogen. Binds to annexin A2, cytokeratin-8, fibronectin and laminin. Binds to mannose receptor and the low-density lipoprotein receptor-related protein (LRP1); these proteins are involved in TPA clearance. Binds LRP1B; binding is followed by internalization and degradation. Forms heterodimer with SERPINA5 (By similarity). {ECO:0000250}. DOMAIN: Both FN1 and one of the kringle domains are required for binding to fibrin. {ECO:0000250}.; DOMAIN: Both FN1 and EGF-like domains are important for binding to LRP1. {ECO:0000250}.; DOMAIN: The FN1 domain mediates binding to annexin A2. {ECO:0000250}.; DOMAIN: The second kringle domain is implicated in binding to cytokeratin-8 and to the endothelial cell surface binding site. {ECO:0000250}. +O70274 TP4A2_MOUSE Protein tyrosine phosphatase type IVA 2 (EC 3.1.3.48) (Protein-tyrosine phosphatase 4a2) (Protein-tyrosine phosphatase of regenerating liver 2) (PRL-2) 167 19,127 Active site (2); Beta strand (6); Binding site (1); Chain (1); Disulfide bond (1); Domain (1); Helix (6); Lipidation (1); Modified residue (1); Mutagenesis (1); Propeptide (1); Region (1); Turn (1) FUNCTION: Protein tyrosine phosphatase which stimulates progression from G1 into S phase during mitosis. Inhibits geranylgeranyl transferase type II activity by blocking the association between RABGGTA and RABGGTB (By similarity). {ECO:0000250}. PTM: Farnesylated. Farnesylation is required for membrane targeting and for interaction with RABGGTB (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10747914}. Early endosome {ECO:0000269|PubMed:10747914}. Cytoplasm {ECO:0000269|PubMed:10747914}. SUBUNIT: In contrast to PTP4A1 and PTP4A3, does not interact with tubulin. Interacts with RABGGTB (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in skeletal muscle, and at lower levels in liver, lung, heart, kidney, brain, testis and spleen. {ECO:0000269|PubMed:9514946}. +Q66JT5 TPGS2_MOUSE Tubulin polyglutamylase complex subunit 2 (PGs2) 296 33,184 Chain (1); Erroneous initiation (1); Sequence conflict (2) SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. SUBUNIT: Part of the neuronal tubulin polyglutamylase complex which contains TPGS1, TPGS2, TTLL1, LRRC49 and NICN1. +Q8BWC0 TPC2_MOUSE Two pore calcium channel protein 2 (Voltage-dependent calcium channel protein TPC2) 731 83,595 Alternative sequence (3); Chain (1); Frameshift (1); Glycosylation (2); Intramembrane (2); Mutagenesis (4); Sequence conflict (3); Topological domain (15); Transmembrane (12) INTRAMEM 239 263 Helical; Pore-forming. {ECO:0000255}.; INTRAMEM 619 641 Helical; Pore-forming. {ECO:0000255}. TRANSMEM 69 89 Helical; Name=S1 of repeat I. {ECO:0000255}.; TRANSMEM 112 132 Helical; Name=S2 of repeat I. {ECO:0000255}.; TRANSMEM 140 160 Helical; Name=S3 of repeat I. {ECO:0000255}.; TRANSMEM 168 188 Helical; Name=S4 of repeat I. {ECO:0000255}.; TRANSMEM 204 224 Helical; Name=S5 of repeat I. {ECO:0000255}.; TRANSMEM 271 291 Helical; Name=S6 of repeat I. {ECO:0000255}.; TRANSMEM 418 438 Helical; Name=S1 of repeat II. {ECO:0000255}.; TRANSMEM 450 470 Helical; Name=S2 of repeat II. {ECO:0000255}.; TRANSMEM 487 507 Helical; Name=S3 of repeat II. {ECO:0000255}.; TRANSMEM 525 542 Helical; Name=S4 of repeat II. {ECO:0000255}.; TRANSMEM 565 585 Helical; Name=S5 of repeat II. {ECO:0000255}.; TRANSMEM 657 677 Helical; Name=S6 of repeat II. {ECO:0000255}. TOPO_DOM 1 68 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 90 111 Extracellular. {ECO:0000255}.; TOPO_DOM 133 139 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 161 167 Extracellular. {ECO:0000255}.; TOPO_DOM 189 203 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 225 238 Extracellular. {ECO:0000255}.; TOPO_DOM 264 270 Extracellular. {ECO:0000255}.; TOPO_DOM 292 417 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 439 449 Extracellular. {ECO:0000255}.; TOPO_DOM 471 486 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 508 524 Extracellular. {ECO:0000255}.; TOPO_DOM 543 564 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 586 618 Extracellular. {ECO:0000255}.; TOPO_DOM 642 656 Extracellular. {ECO:0000255}.; TOPO_DOM 678 731 Cytoplasmic. {ECO:0000255}. FUNCTION: Nicotinic acid adenine dinucleotide phosphate (NAADP) receptor that may function as one of the major voltage-gated Ca(2+) channels (VDCC) across the lysosomal membrane. Involved in smooth muscle contraction. {ECO:0000269|PubMed:19387438, ECO:0000269|PubMed:20495006, ECO:0000269|PubMed:20547763}. PTM: N-glycosylated. {ECO:0000269|PubMed:19557428}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:19557428, ECO:0000269|PubMed:20495006}; Multi-pass membrane protein {ECO:0000269|PubMed:19557428, ECO:0000269|PubMed:20495006}. Note=Only the acidic lysosomal fraction is sensitive to NAADP. SUBUNIT: Homodimer (PubMed:19557428). Interacts with LRRK2. Interacts with HAX1 (By similarity). {ECO:0000250|UniProtKB:Q8NHX9, ECO:0000305|PubMed:19557428}. DOMAIN: Each of the two internal repeats contains five hydrophobic transmembrane segments (S1, S2, S3, S5, S6) and one positively charged transmembrane segment (S4). S4 segments probably represent the voltage-sensor and are characterized by a series of positively charged amino acids at every third position (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:19557428}. +Q9D658 TP4A3_MOUSE Protein tyrosine phosphatase type IVA 3 (EC 3.1.3.48) (Protein-tyrosine phosphatase 4a3) (Protein-tyrosine phosphatase of regenerating liver 3) (PRL-3) 173 19,652 Active site (2); Binding site (1); Chain (1); Disulfide bond (1); Domain (1); Lipidation (1); Modified residue (1); Mutagenesis (2); Propeptide (1); Sequence conflict (2) FUNCTION: Protein tyrosine phosphatase which stimulates progression from G1 into S phase during mitosis. Enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. May be involved in the progression of cardiac hypertrophy by inhibiting intracellular calcium mobilization in response to angiotensin II. {ECO:0000269|PubMed:15161639}. PTM: Farnesylated. Farnesylation is required for membrane targeting. Unfarnesylated forms are shifted into the nucleus. SUBCELLULAR LOCATION: Cell membrane. Early endosome. SUBUNIT: Interacts with tubulin. {ECO:0000250}. TISSUE SPECIFICITY: Present in the small intestine, where it is located in the differentiated epithelial cells of the villus but not in the proliferating crypt cells (at protein level). Expressed in heart and skeletal muscle, and at lower levels in lung, spleen and testis. {ECO:0000269|PubMed:15161639, ECO:0000269|PubMed:9514946}. +P40226 TPO_MOUSE Thrombopoietin (C-mpl ligand) (ML) (Megakaryocyte colony-stimulating factor) (Megakaryocyte growth and development factor) (MGDF) (Myeloproliferative leukemia virus oncogene ligand) 356 37,836 Alternative sequence (1); Chain (1); Disulfide bond (2); Glycosylation (7); Signal peptide (1) FUNCTION: Lineage-specific cytokine affecting the proliferation and maturation of megakaryocytes from their committed progenitor cells. It acts at a late stage of megakaryocyte development. It may be the major physiological regulator of circulating platelets. SUBCELLULAR LOCATION: Secreted. DOMAIN: Two-domain structure with an erythropoietin-like N-terminal and a Ser/Pro/Thr-rich C-terminal. TISSUE SPECIFICITY: Found mainly in the liver, kidney and skeletal muscle. +Q7TQD2 TPPP_MOUSE Tubulin polymerization-promoting protein (TPPP) 218 23,575 Chain (1); Glycosylation (1); Modified residue (8); Region (1) FUNCTION: May play a role in the polymerization of tubulin into microtubules, microtubule bundling and the stabilization of existing microtubules, thus maintaining the integrity of the microtubule network. May play a role in mitotic spindle assembly and nuclear envelope breakdown. {ECO:0000269|PubMed:18028908}. PTM: Poor substrate for GSK3. Phosphorylated by LIMK1 on serine residues. Phosphorylation may alter the tubulin polymerization activity. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18028908}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:18028908}. Nucleus {ECO:0000269|PubMed:18028908}. SUBUNIT: Homodimer. Binds tubulin; binding is inhibited by GTP. Interacts with GSK3. Interacts with MAPK1. Interacts with LIMK1 (via the PDZ domain); the interaction is direct. Interacts with GAPDH; the interaction is direct. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed with higher expression in brain (at protein level). {ECO:0000269|PubMed:18028908}. +Q9CQU0 TXD12_MOUSE Thioredoxin domain-containing protein 12 (EC 1.8.4.2) (Endoplasmic reticulum resident protein 19) (ER protein 19) (ERp19) (Thioredoxin-like protein p19) 170 19,049 Chain (1); Disulfide bond (1); Glycosylation (1); Motif (1); Signal peptide (1) FUNCTION: Possesses significant protein thiol-disulfide oxidase activity. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138, ECO:0000269|PubMed:12930873}. +Q6P902 TXND2_MOUSE Thioredoxin domain-containing protein 2 (Spermatid-specific thioredoxin-1) (Sptrx-1) (Thioredoxin-4) 515 57,767 Chain (1); Disulfide bond (1); Domain (1); Erroneous initiation (1); Modified residue (3); Region (1); Repeat (21) FUNCTION: Probably plays a regulatory role in sperm development. May participate in regulation of fibrous sheath (FS) assembly by supporting the formation of disulfide bonds during sperm tail morphogenesis. May also be required to rectify incorrect disulfide pairing and generate suitable pairs between the FS constituents. Can reduce disulfide bonds in vitro in the presence of NADP and thioredoxin reductase. SUBCELLULAR LOCATION: Cytoplasm. TISSUE SPECIFICITY: Testis-specific. Strongly expressed in the testicular seminiferous tubules, mostly in the round spermatids. {ECO:0000269|PubMed:12149401, ECO:0000269|PubMed:12390887}. +P26369 U2AF2_MOUSE Splicing factor U2AF 65 kDa subunit (U2 auxiliary factor 65 kDa subunit) (U2 snRNP auxiliary factor large subunit) 475 53,517 Beta strand (6); Chain (1); Compositional bias (1); Cross-link (2); Domain (3); Erroneous initiation (1); Helix (4); Initiator methionine (1); Modified residue (7); Region (2); Turn (1) FUNCTION: Plays a role in pre-mRNA splicing and 3'-end processing. By recruiting PRPF19 and the PRP19C/Prp19 complex/NTC/Nineteen complex to the RNA polymerase II C-terminal domain (CTD), and thereby pre-mRNA, may couple transcription to splicing. Required for the export of mRNA out of the nucleus, even if the mRNA is encoded by an intron-less gene. Positively regulates pre-mRNA 3'-end processing by recruiting the CFIm complex to cleavage and polyadenylation signals. {ECO:0000250|UniProtKB:P26368}. PTM: Lysyl-hydroxylation at Lys-15 and Lys-276 affects the mRNA splicing activity of the protein, leading to regulate some, but not all, alternative splicing events. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with U2AF1L4 (PubMed:16819553). Heterodimer with U2AF1. Binds unphosphorylated SF1. Interacts with SCAF11 and SNW1. Interacts with ZRSR2/U2AF1-RS2. Interacts with RBM17. Interacts with PRPF19; the interaction is direct. Interacts with POLR2A (via the C-terminal domain); Interacts with PRPF19; the interaction is direct. Interacts with POLR2A (via the C-terminal domain); recruits PRPF19 and the Prp19 complex to the pre-mRNA. Interacts with KHDC4 (Isoform 2). Interacts with ZRSR2. Interacts with the SF3B complex composed of SF3B1, SF3B2, SF3B3, SF3B4, SF3B5, SF3B6 and PHF5A (By similarity). Interacts (via N-terminus) with CPSF7 (via C-terminus); this interaction stimulates pre-mRNA 3'-end processing by promoting the recruitment of the CFIm complex to cleavage and polyadenylation signals (By similarity). {ECO:0000250|UniProtKB:P26368, ECO:0000269|PubMed:16819553}. +Q9DBA6 TYSD1_MOUSE Peroxisomal leader peptide-processing protease (EC 3.4.21.-) (Trypsin domain-containing protein 1) [Cleaved into: Peroxisomal leader peptide-processing protease, 10 kDa form; Peroxisomal leader peptide-processing protease, 49 kDa form] 568 59,066 Active site (3); Chain (3); Region (1); Site (1) FUNCTION: Peroxisomal protease that mediates both the removal of the leader peptide from proteins containing a PTS2 target sequence and processes several PTS1-containing proteins. Catalyzes the processing of PTS1-proteins involved in the peroxisomal beta-oxidation of fatty acids (By similarity). {ECO:0000250, ECO:0000269|PubMed:17255948}. PTM: Self-cleavage gives rise to an N-terminal 10-kDa fragment and C-terminal 49-kDa fragment upon import into the peroxisomes. The full-lengh TYSND1 is the active the proteolytic processing of PTS1- and PTS2-proteins and in self-cleavage, and intermolecular self-cleavage of TYSND1 down-regulates its protease activity. {ECO:0000269|PubMed:17255948}. SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:17255948}. SUBUNIT: Homodimer. Forms a heterodimer with the C-terminal cleavage product (49 kDa form). Forms a heterodimer with the N-terminal cleavage product (10 kDa form). Interacts with PEX5. Interacts with LONP2. {ECO:0000250}. +P31254 UBA1Y_MOUSE Ubiquitin-like modifier-activating enzyme 1 Y (EC 6.2.1.45) (Ubiquitin-activating enzyme E1) (Ubiquitin-activating enzyme E1 Y) 1058 118,038 Active site (1); Binding site (4); Chain (1); Nucleotide binding (1); Sequence conflict (5) Protein modification; protein ubiquitination. FUNCTION: Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP (By similarity). The Y chromosome form could be involved in the survival and proliferation of differentiating spermatogonia. {ECO:0000250|UniProtKB:P22314, ECO:0000305}. SUBUNIT: Monomer. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in testis in A spermatogonia and spermatids but not (or at very low levels) in pachytene spermatocytes. Also expressed in Y-bearing ovaries and at very low levels in adrenal gland. {ECO:0000269|PubMed:8948595}. +Q9JJZ4 UB2J1_MOUSE Ubiquitin-conjugating enzyme E2 J1 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme J1) (Non-canonical ubiquitin-conjugating enzyme 1) (NCUBE-1) 318 34,990 Active site (1); Chain (1); Modified residue (3); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 283 303 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 1 282 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 304 318 Lumenal. {ECO:0000255}. Protein modification; protein ubiquitination. FUNCTION: Catalyzes the covalent attachment of ubiquitin to other proteins. Functions in the selective degradation of misfolded membrane proteins from the endoplasmic reticulum (ERAD). {ECO:0000255|PROSITE-ProRule:PRU00388}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9Y385}; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:Q9Y385}. +Q91VX2 UBAP2_MOUSE Ubiquitin-associated protein 2 (UBAP-2) (Protein lingerer homolog 1) (mLig-1) 1132 117,966 Chain (1); Compositional bias (1); Domain (1); Modified residue (4); Sequence conflict (1) +Q6P073 UB2J2_MOUSE Ubiquitin-conjugating enzyme E2 J2 (EC 2.3.2.23) (Non-canonical ubiquitin-conjugating enzyme 2) (NCUBE-2) 259 28,954 Active site (1); Chain (1); Mutagenesis (1); Sequence conflict (14); Topological domain (2); Transmembrane (1) TRANSMEM 227 247 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 1 226 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 248 259 Lumenal. {ECO:0000255}. Protein modification; protein ubiquitination. FUNCTION: Catalyzes the covalent attachment of ubiquitin to other proteins. Seems to function in the selective degradation of misfolded membrane proteins from the endoplasmic reticulum (ERAD). {ECO:0000269|PubMed:12082160}.; FUNCTION: In case of infection by the murid herpesvirus 4, its association with the viral E3 ligase K3 mediates ubiquitination of host surface class I (MHC-I) H-2D(b)/H2-D1 and H-2K(b)/H2-K1 molecules before they exit the endoplasmic reticulum, leading to their degradation by the ERAD system, thus blocking the immune detection of virus-infected cells. The complex formed with the murid herpesvirus 4 protein K3 mediates ubiquitination of lysine, as well as serine and threonine residues present in the cytoplasmic tail of surface class I molecules and promotes ubiquitination of hydroxylated serine or threonine residues via ester bonds instead of the classical isopeptide linkage. {ECO:0000269|PubMed:11278356, ECO:0000269|PubMed:19951915}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11278356, ECO:0000269|PubMed:12082160}; Single-pass type IV membrane protein {ECO:0000269|PubMed:11278356, ECO:0000269|PubMed:12082160}. SUBUNIT: Interacts with murid herpesvirus 4 protein K3 (mK3). {ECO:0000269|PubMed:19951915}. +Q3TW96 UAP1L_MOUSE UDP-N-acetylhexosamine pyrophosphorylase-like protein 1 (EC 2.7.7.-) 507 56,614 Alternative sequence (1); Binding site (7); Chain (1); Erroneous initiation (1); Motif (2); Region (1); Sequence caution (1) +P70691 UD12_MOUSE UDP-glucuronosyltransferase 1-2 (UDPGT 1-2) (UGT1*2) (UGT1-02) (UGT1.2) (EC 2.4.1.17) (Bilirubin-specific UDPGT) (UDP-glucuronosyltransferase 1A2) (UGT1A2) 533 60,285 Chain (1); Glycosylation (3); Sequence conflict (1); Signal peptide (1); Transmembrane (1) TRANSMEM 491 511 Helical. {ECO:0000255}. FUNCTION: UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. SUBCELLULAR LOCATION: Microsome {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Expressed in kidney. {ECO:0000269|PubMed:14672974}. +P81615 UCN1_MOUSE Urocortin 122 13,558 Modified residue (1); Peptide (1); Propeptide (1); Signal peptide (1) FUNCTION: Acts in vitro to stimulate the secretion of adrenocorticotropic hormone (ACTH) (By similarity). Binds with high affinity to CRF receptor types 1, 2-alpha, and 2-beta (By similarity). Plays a role in the establishment of normal hearing thresholds (PubMed:12091910). Reduces food intake and regulates ghrelin levels in gastric body and plasma (By similarity). {ECO:0000250|UniProtKB:P55089, ECO:0000250|UniProtKB:P55090, ECO:0000269|PubMed:12091910}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Interacts with CRHR1 and CRHR2 (via their N-terminal extracellular domain). {ECO:0000250}. TISSUE SPECIFICITY: In the organ of Corti, detected in the inner hair cell region (at protein level) (PubMed:12091910). Expressed in skin (at protein level) (PubMed:10690896). {ECO:0000269|PubMed:10690896, ECO:0000269|PubMed:12091910}. +Q6ZQM8 UD17C_MOUSE UDP-glucuronosyltransferase 1-7C (UDPGT 1-7C) (UGT1*7C) (UGT1-07C) (UGT1.7C) (EC 2.4.1.17) (UDP-glucuronosyltransferase 1A7C) (UGT1A10) 531 59,758 Chain (1); Compositional bias (1); Glycosylation (2); Signal peptide (1); Transmembrane (1) TRANSMEM 489 509 Helical. {ECO:0000255}. FUNCTION: UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. This isoform has specificity for phenols. SUBCELLULAR LOCATION: Microsome. Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Widely expressed with highest levels detected in colon and kidney. {ECO:0000269|PubMed:14672974}. +Q62452 UD19_MOUSE UDP-glucuronosyltransferase 1-9 (UDPGT 1-9) (UGT1*9) (UGT1-09) (UGT1.9) (EC 2.4.1.17) (UDP-glucuronosyltransferase 1-7) (UDPGT) (UDP-glucuronosyltransferase 1A9) (UGT1A12) (UGTP4) 528 60,008 Chain (1); Erroneous initiation (1); Glycosylation (3); Modified residue (1); Sequence conflict (7); Signal peptide (1); Transmembrane (1) TRANSMEM 486 506 Helical. {ECO:0000255}. FUNCTION: UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. SUBCELLULAR LOCATION: Microsome. Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Highly expressed in liver and at lower levels in stomach and kidney. {ECO:0000269|PubMed:14672974}. +Q9CR09 UFC1_MOUSE Ubiquitin-fold modifier-conjugating enzyme 1 (Ufm1-conjugating enzyme 1) 167 19,481 Active site (1); Chain (1) FUNCTION: E2-like enzyme which forms an intermediate with UFM1 via a thioester linkage. {ECO:0000250|UniProtKB:Q9Y3C8}. SUBUNIT: Interacts with UBA5 (via C-terminus). Interacts with UFL1. Interacts with KIRREL3. {ECO:0000250|UniProtKB:Q9Y3C8}. +P70362 UFD1_MOUSE Ubiquitin recognition factor in ER-associated degradation protein 1 (Ubiquitin fusion degradation protein 1 homolog) (UB fusion protein 1) 307 34,481 Chain (1); Modified residue (6); Sequence conflict (3) Protein degradation; proteasomal ubiquitin-dependent pathway. FUNCTION: Essential component of the ubiquitin-dependent proteolytic pathway which degrades ubiquitin fusion proteins. The ternary complex containing UFD1, VCP and NPLOC4 binds ubiquitinated proteins and is necessary for the export of misfolded proteins from the ER to the cytoplasm, where they are degraded by the proteasome. The NPLOC4-UFD1-VCP complex regulates spindle disassembly at the end of mitosis and is necessary for the formation of a closed nuclear envelope. It may be involved in the development of some ectoderm-derived structures (By similarity). Acts as a negative regulator of type I interferon production via the complex formed with VCP and NPLOC4, which binds to DDX58/RIG-I and recruits RNF125 to promote ubiquitination and degradation of DDX58/RIG-I (By similarity). {ECO:0000250|UniProtKB:Q92890, ECO:0000250|UniProtKB:Q9ES53}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9ES53}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9ES53}. SUBUNIT: Heterodimer with NPLOC4, this heterodimer binds VCP and inhibits Golgi membrane fusion. Interacts with USP13 (By similarity). Interacts with ZFAND2B; probably through VCP (PubMed:24160817). {ECO:0000250|UniProtKB:Q92890, ECO:0000269|PubMed:24160817}. +Q9CZP0 UFSP1_MOUSE Ufm1-specific protease 1 (UfSP1) (EC 3.4.22.-) 217 23,421 Active site (3); Beta strand (8); Chain (1); Helix (6); Mutagenesis (6); Turn (6) FUNCTION: Thiol protease which recognizes and hydrolyzes the peptide bond at the C-terminal Gly of UFM1, a ubiquitin-like modifier protein bound to a number of target proteins. Does not hydrolyze SUMO1 or ISG15 ubiquitin-like proteins. {ECO:0000269|PubMed:17182609}. TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in brain, heart, kidney and skeletal muscle. {ECO:0000269|PubMed:17182609}. +Q99K23 UFSP2_MOUSE Ufm1-specific protease 2 (UfSP2) (EC 3.4.22.-) 461 52,515 Active site (3); Beta strand (15); Chain (1); Erroneous termination (1); Helix (14); Mutagenesis (5); Turn (3) FUNCTION: Thiol protease which recognizes and hydrolyzes the peptide bond at the C-terminal Gly of UFM1, a ubiquitin-like modifier protein bound to a number of target proteins. Does not hydrolyze SUMO1 or ISG15 ubiquitin-like proteins (PubMed:17182609, PubMed:21228277). Through TRIP4 deufmylation may regulate intracellular nuclear receptors transactivation and thereby regulate cell proliferation and differentiation (By similarity). {ECO:0000250|UniProtKB:Q9NUQ7, ECO:0000269|PubMed:17182609, ECO:0000269|PubMed:21228277}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21228277}. Endoplasmic reticulum {ECO:0000269|PubMed:21228277}. Nucleus {ECO:0000269|PubMed:21228277}. SUBUNIT: Interacts with DDRGK1 (PubMed:21228277). Interacts with TRIP4; deufmylates TRIP4 (By similarity). {ECO:0000250|UniProtKB:Q9NUQ7, ECO:0000269|PubMed:21228277}. TISSUE SPECIFICITY: Expressed at high level in brain, kidney, stomach, skeletal muscle and testis. {ECO:0000269|PubMed:17182609}. +Q00993 UFO_MOUSE Tyrosine-protein kinase receptor UFO (EC 2.7.10.1) (Adhesion-related kinase) 888 98,191 Active site (1); Binding site (1); Chain (1); Disulfide bond (2); Domain (5); Glycosylation (6); Modified residue (4); Nucleotide binding (1); Region (1); Sequence conflict (5); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 446 466 Helical. {ECO:0000255}. TOPO_DOM 19 445 Extracellular. {ECO:0000255}.; TOPO_DOM 467 888 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding growth factor GAS6 and which is thus regulating many physiological processes including cell survival, cell proliferation, migration and differentiation. Ligand binding at the cell surface induces dimerization and autophosphorylation of AXL. Following activation by ligand, ALX binds and induces tyrosine phosphorylation of PI3-kinase subunits PIK3R1, PIK3R2 and PIK3R3; but also GRB2, PLCG1, LCK and PTPN11. Other downstream substrate candidates for AXL are CBL, NCK2, SOCS1 and TNS2. Recruitment of GRB2 and phosphatidylinositol 3 kinase regulatory subunits by AXL leads to the downstream activation of the AKT kinase. GAS6/AXL signaling plays a role in various processes such as endothelial cell survival during acidification by preventing apoptosis, optimal cytokine signaling during human natural killer cell development, hepatic regeneration, gonadotropin-releasing hormone neuron survival and migration, platelet activation, or regulation of thrombotic responses. Plays also an important role in inhibition of Toll-like receptors (TLRs)-mediated innate immune response. {ECO:0000269|PubMed:18083102, ECO:0000269|PubMed:20363878}. PTM: Monoubiquitinated upon GAS6-binding. A very small proportion of the receptor could be subjected to polyubiquitination in a very transient fashion (By similarity). {ECO:0000250}.; PTM: Phosphorylated at tyrosine residues by autocatalysis, which activates kinase activity. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Heterodimer and heterotetramer with ligand GAS6 (By similarity). Interacts with CBL, GRB2, LCK, NCK2, PIK3R1, PIK3R2, PIK3R3, PLCG1, SOCS1 and TNS2. Part of a complex including AXL, TNK2 and GRB2, in which GRB2 promotes AXL recruitment by TNK2 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: In distinct substructures of a broad spectrum of developing tissues (in the late embryogenesis). In cells forming organ capsules as well as in connective tissue structures (in adult). +Q6P5E4 UGGG1_MOUSE UDP-glucose:glycoprotein glucosyltransferase 1 (UGT1) (EC 2.4.1.-) (UDP--Glc:glycoprotein glucosyltransferase) (UDP-glucose ceramide glucosyltransferase-like 1) 1551 176,434 Chain (1); Glycosylation (3); Modified residue (1); Motif (1); Region (1); Sequence conflict (8); Signal peptide (1) Protein modification; protein glycosylation. FUNCTION: Recognizes glycoproteins with minor folding defects. Reglucosylates single N-glycans near the misfolded part of the protein, thus providing quality control for protein folding in the endoplasmic reticulum. Reglucosylated proteins are recognized by calreticulin for recycling to the endoplasmic reticulum and refolding or degradation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:Q9NYU2, ECO:0000255|PROSITE-ProRule:PRU10138}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000255|PROSITE-ProRule:PRU10138}. SUBUNIT: Monomer as well as in a tight complex with SELENOF. Interacts with METTL23 (By similarity). {ECO:0000250}. DOMAIN: The N-terminal non-catalytic domain is assumed to mediate recognition of proteins with partial folding defects. {ECO:0000250}. +P35456 UPAR_MOUSE Urokinase plasminogen activator surface receptor (U-PAR) (uPAR) (CD antigen CD87) 327 35,428 Alternative sequence (2); Beta strand (20); Chain (1); Disulfide bond (14); Domain (3); Glycosylation (7); Helix (2); Lipidation (1); Propeptide (1); Signal peptide (1); Turn (2) FUNCTION: Acts as a receptor for urokinase plasminogen activator. Plays a role in localizing and promoting plasmin formation. Mediates the proteolysis-independent signal transduction activation effects of U-PA. SUBCELLULAR LOCATION: Isoform 1: Cell membrane {ECO:0000250|UniProtKB:P49616}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P49616}.; SUBCELLULAR LOCATION: Isoform 2: Secreted {ECO:0000250|UniProtKB:P49616}. SUBUNIT: Monomer (Probable). Interacts (via the UPAR/Ly6 domains) with SRPX2. Interacts with MRC2 (By similarity). Interacts with SORL1 (By similarity). {ECO:0000250, ECO:0000305}. TISSUE SPECIFICITY: Expressed in angiogenic endothelial cells (at protein level). {ECO:0000269|PubMed:19667118}. +Q9Z2C6 UPK1B_MOUSE Uroplakin-1b (UP1b) (Uroplakin Ib) (UPIb) 260 29,762 Chain (1); Sequence conflict (3); Topological domain (5); Transmembrane (4) TRANSMEM 16 36 Helical. {ECO:0000255}.; TRANSMEM 60 80 Helical. {ECO:0000255}.; TRANSMEM 87 107 Helical. {ECO:0000255}.; TRANSMEM 230 250 Helical. {ECO:0000255}. TOPO_DOM 1 15 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 37 59 Extracellular. {ECO:0000255}.; TOPO_DOM 81 86 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 108 229 Extracellular. {ECO:0000255}.; TOPO_DOM 251 260 Cytoplasmic. {ECO:0000255}. FUNCTION: Component of the asymmetric unit membrane (AUM); a highly specialized biomembrane elaborated by terminally differentiated urothelial cells. May play an important role in normal bladder epithelial physiology, possibly in regulating membrane permeability of superficial umbrella cells or in stabilizing the apical membrane through AUM/cytoskeletal interactions (By similarity). {ECO:0000250}. PTM: N-glycosylated with high-mannose oligosaccharides. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SUBUNIT: Heterodimer with uroplakin-3A (UPK3A) or uroplakin-3B (UPK3B). {ECO:0000250}. TISSUE SPECIFICITY: Bladder epithelium. +Q9D701 UPK3L_MOUSE Uroplakin-3b-like protein 1 249 27,250 Chain (1); Erroneous initiation (2); Glycosylation (3); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 195 215 Helical. {ECO:0000255}. TOPO_DOM 27 194 Extracellular. {ECO:0000255}.; TOPO_DOM 216 249 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +O89023 TPP1_MOUSE Tripeptidyl-peptidase 1 (TPP-1) (EC 3.4.14.9) (Lysosomal pepstatin-insensitive protease) (LPIC) (Tripeptidyl aminopeptidase) (Tripeptidyl-peptidase I) (TPP-I) 562 61,342 Active site (3); Chain (1); Disulfide bond (3); Domain (1); Erroneous initiation (1); Glycosylation (5); Metal binding (5); Propeptide (1); Sequence conflict (2); Signal peptide (1) FUNCTION: Lysosomal serine protease with tripeptidyl-peptidase I activity. May act as a non-specific lysosomal peptidase which generates tripeptides from the breakdown products produced by lysosomal proteinases. Requires substrates with an unsubstituted N-terminus. {ECO:0000250|UniProtKB:Q9EQV6}. PTM: Activated by autocatalytic proteolytical processing upon acidification. N-glycosylation is required for processing and activity (By similarity). {ECO:0000250|UniProtKB:O14773}. SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:19941651}. Melanosome {ECO:0000250|UniProtKB:O14773}. SUBUNIT: Monomer (By similarity). Interacts with CLN5 (PubMed:19941651). {ECO:0000250|UniProtKB:O14773, ECO:0000269|PubMed:19941651}. +Q9ES56 TPPC4_MOUSE Trafficking protein particle complex subunit 4 (Synbindin) (TRS23 homolog) 219 24,385 Chain (1) FUNCTION: May play a role in vesicular transport from endoplasmic reticulum to Golgi. May play a role in dendrite postsynaptic membrane trafficking. SUBCELLULAR LOCATION: Membrane. Cell junction, synapse, postsynaptic cell membrane. Golgi apparatus. Endoplasmic reticulum {ECO:0000305}. Note=Associated with postsynaptic membranes and in intracellular cisterns and vesicles (Golgi). SUBUNIT: Component of the multisubunit TRAPP (transport protein particle) complex, which includes at least TRAPPC2, TRAPPC2L, TRAPPC3, TRAPPC3L, TRAPPC4, TRAPPC5, TRAPPC8, TRAPPC9, TRAPPC10, TRAPPC11 and TRAPPC12 (By similarity). Interacts with SDC2. {ECO:0000250, ECO:0000269|PubMed:11018053}. TISSUE SPECIFICITY: Widely expressed. +P21107 TPM3_MOUSE Tropomyosin alpha-3 chain (Gamma-tropomyosin) (Tropomyosin-3) 285 32,994 Alternative sequence (3); Chain (1); Coiled coil (1); Initiator methionine (2); Modified residue (14); Sequence conflict (3) FUNCTION: Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments. {ECO:0000250|UniProtKB:P09493}. SUBCELLULAR LOCATION: Isoform 2: Cytoplasm, cytoskeleton. SUBUNIT: Homodimer. Heterodimer of an alpha (TPM1, TPM3 or TPM4) and a beta (TPM2) chain. Interacts with TMOD1. {ECO:0000250|UniProtKB:P04692, ECO:0000250|UniProtKB:P06753}. DOMAIN: The molecule is in a coiled coil structure that is formed by 2 polypeptide chains. The sequence exhibits a prominent seven-residues periodicity. +Q6IRU2 TPM4_MOUSE Tropomyosin alpha-4 chain (Tropomyosin-4) 248 28,468 Chain (1); Coiled coil (1); Initiator methionine (1); Modified residue (5) FUNCTION: Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments. Binds calcium. {ECO:0000250|UniProtKB:P09495, ECO:0000250|UniProtKB:P67936}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P09495}. Note=Associates with F-actin stress fibers. {ECO:0000250|UniProtKB:P09495}. SUBUNIT: Homodimer. Heterodimer of an alpha (TPM1, TPM3 or TPM4) and a beta (TPM2) chain. {ECO:0000250|UniProtKB:P09495}. DOMAIN: The molecule is in a coiled coil structure that is formed by 2 polypeptide chains. The sequence exhibits a prominent seven-residues periodicity. +P83877 TXN4A_MOUSE Thioredoxin-like protein 4A (DIM1 protein homolog) (Spliceosomal U5 snRNP-specific 15 kDa protein) (Thioredoxin-like U5 snRNP protein U5-15kD) 142 16,786 Chain (1); Disulfide bond (1); Modified residue (1) FUNCTION: Plays role in pre-mRNA splicing as component of the U5 snRNP and U4/U6-U5 tri-snRNP complexes that are involved in spliceosome assembly, and as component of the precatalytic spliceosome (spliceosome B complex). {ECO:0000250|UniProtKB:P83876}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P83876}. SUBUNIT: Component of the precatalytic spliceosome (spliceosome B complex). Component of the U5 snRNP complex. Component of the U4/U6-U5 tri-snRNP complex. The U4/U6-U5 tri-snRNP complex is a building block of the precatalytic spliceosome (spliceosome B complex). The U4/U6-U5 tri-snRNP complex is composed of the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39, plus LSM2, LSM3, LSM4, LSM5, LSM6, LSM7 and LSM8. Directly interacts with CD2BP2. Interacts with HNRPF, HNRPH2, NEDD9 and PQBP1. Interacts with ERBB4. {ECO:0000250|UniProtKB:P83876}. +Q715T0 TXND3_MOUSE Thioredoxin domain-containing protein 3 (NME/NM23 family member 8) (Spermatid-specific thioredoxin-2) (Sptrx-2) 586 66,857 Alternative sequence (2); Chain (1); Disulfide bond (1); Domain (1); Region (3); Sequence conflict (2) FUNCTION: Probably required during the final stages of sperm tail maturation in the testis and/or epididymis, where extensive disulfide bonding of fibrous sheath (FS) proteins occurs. May be involved in the reduction of disulfide bonds within the sperm FS components. In vitro, it has neither NDP kinase nor reducing activity on disulfide bonds (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12909633}. SUBUNIT: Monomer. {ECO:0000250}. DOMAIN: Contains 3 inactive NDK domains that each lack the active His residue, suggesting that they have no NDP kinase activity. TISSUE SPECIFICITY: Testis-specific. Expressed mainly in round spermatids. {ECO:0000269|PubMed:12909633}. +Q6ZWY8 TYB10_MOUSE Thymosin beta-10 44 5,026 Chain (1); Initiator methionine (1); Modified residue (9) FUNCTION: Plays an important role in the organization of the cytoskeleton. Binds to and sequesters actin monomers (G actin) and therefore inhibits actin polymerization (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. +P29812 TYRP2_MOUSE L-dopachrome tautomerase (DCT) (DT) (EC 5.3.3.12) (DOPAchrome conversion factor) (DOPAchrome isomerase) (DOPAchrome oxidoreductase) (L-dopachrome Delta-isomerase) (SLATY locus protein) (Tyrosinase-related protein 2) (TRP-2) (TRP2) 517 58,510 Chain (1); Glycosylation (7); Metal binding (6); Natural variant (3); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 473 491 Helical. {ECO:0000255}. TOPO_DOM 24 472 Lumenal, melanosome. {ECO:0000255}.; TOPO_DOM 492 517 Cytoplasmic. {ECO:0000255}. Pigment biosynthesis; melanin biosynthesis. FUNCTION: Catalyzes the conversion of L-dopachrome into 5,6-dihydroxyindole-2-carboxylic acid (DHICA) (PubMed:1537333). Involved in regulating eumelanin and phaeomelanin levels. {ECO:0000269|PubMed:1537333}. PTM: Glycosylated. {ECO:0000269|PubMed:1537333}. SUBCELLULAR LOCATION: Melanosome membrane {ECO:0000250|UniProtKB:P40126}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P40126}. Melanosome {ECO:0000269|PubMed:26620560}. Note=Proper trafficking to melanosome is regulated by SGSM2, ANKRD27, RAB9A, RAB32 and RAB38. {ECO:0000269|PubMed:26620560}. SUBUNIT: Tyrosinase, TYRP1 and DCT/TYRP2 may form a multienzyme complex. TISSUE SPECIFICITY: Melanocytes and retinal pigmented epithelium. DISEASE: Note=The slaty mutation in Tyrp2 leads to a decrease of DT activity and a consequent change in the pigmentation of the mice to a dark gray/brown eumelanin. The slaty-2j mutation has a similar phenotype, the slaty-lt (light) mutation has a more severe effect and is semidominant; its phenotype may be a result of the failure of the enzyme to be correctly targeted to its normal location on the inner face of the melanosomal membrane. {ECO:0000269|PubMed:8530099}. +Q9D883 U2AF1_MOUSE Splicing factor U2AF 35 kDa subunit (U2 auxiliary factor 35 kDa subunit) (U2 snRNP auxiliary factor small subunit) 239 27,815 Chain (1); Compositional bias (1); Domain (1); Initiator methionine (1); Modified residue (5); Sequence conflict (1); Zinc finger (2) FUNCTION: Plays a critical role in both constitutive and enhancer-dependent splicing by mediating protein-protein interactions and protein-RNA interactions required for accurate 3'-splice site selection. Recruits U2 snRNP to the branch point. Directly mediates interactions between U2AF2 and proteins bound to the enhancers and thus may function as a bridge between U2AF2 and the enhancer complex to recruit it to the adjacent intron (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18758164}. Nucleus speckle {ECO:0000269|PubMed:18758164}. SUBUNIT: Identified in the spliceosome C complex. Heterodimer with U2AF2. Interacts with ZRANB2 (By similarity). Interacts (via RS domain) with PHF5A (via N-terminus). {ECO:0000250, ECO:0000269|PubMed:18758164}. DOMAIN: The C-terminal SR-rich domain is required for interactions with SR proteins and the splicing regulators TRA and TRA2, and the N-terminal domain is required for formation of the U2AF1/U2AF2 heterodimer. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in primary spermatocytes and elongating spermatids (at protein level). {ECO:0000269|PubMed:18758164}. +Q8BH48 UBAP1_MOUSE Ubiquitin-associated protein 1 (UBAP-1) 502 55,028 Alternative sequence (1); Chain (1); Domain (3); Frameshift (2); Modified residue (3) FUNCTION: Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Binds to ubiquitinated cargo proteins and is required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies (MVBs). Plays a role in the proteasomal degradation of ubiquitinated cell-surface proteins, such as EGFR and BST2 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Endosome {ECO:0000250}. Note=Predominantly cytosolic. Recruited to endosomes as part of the ESCRT-I complex (By similarity). {ECO:0000250}. SUBUNIT: Component of an ESCRT-I complex (endosomal sorting complex required for transport I) which consists of TSG101, VPS28, VPS37A and UBAP1 in a 1:1:1:1 stoichiometry. Can be a component of ESCRT-I complexes containing VPS37B, VPS37C and VPS37D (in vitro), but may have a preference for the ESCRT-I complex containing VPS37A. Interacts with PTPN23. Interacts (via UBA domains) with ubiquitinated proteins (By similarity). {ECO:0000250}. DOMAIN: The UMA domain mediates association with the ESCRT-I complex. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. Highly expressed in heart, liver, brain, kidney, spleen, skeletal muscle, stomach, testis and lung. {ECO:0000269|PubMed:11599797}. +Q91YN5 UAP1_MOUSE UDP-N-acetylhexosamine pyrophosphorylase [Includes: UDP-N-acetylgalactosamine pyrophosphorylase (EC 2.7.7.83); UDP-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23)] 522 58,609 Alternative sequence (2); Beta strand (24); Binding site (7); Chain (1); Helix (23); Motif (2); Natural variant (1); Region (1); Turn (7) Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1. FUNCTION: Converts UTP and GlcNAc-1-P into UDP-GlcNAc, and UTP and GalNAc-1-P into UDP-GalNAc. Isoform AGX1 has 2 to 3 times higher activity towards GalNAc-1-P, while isoform AGX2 has 8 times more activity towards GlcNAc-1-P (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Monomer and homodimer. Isoform AGX1 is a homodimer. Isoform AGX2 is a monomer (By similarity). {ECO:0000250}. +Q9QZU9 UB2L6_MOUSE Ubiquitin/ISG15-conjugating enzyme E2 L6 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme L6) (UbcM8) (Ubiquitin carrier protein L6) (Ubiquitin-protein ligase L6) 153 17,841 Active site (1); Chain (1); Erroneous initiation (1); Sequence conflict (2) Protein modification; protein ubiquitination. FUNCTION: Catalyzes the covalent attachment of ubiquitin or ISG15 to other proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Promotes ubiquitination and subsequent proteasomal degradation of FLT3. {ECO:0000250|UniProtKB:O14933}. PTM: ISGylated. {ECO:0000250|UniProtKB:O14933}. SUBUNIT: Interacts with RNF19A, RNF19B and RNF144B. Interacts with FLT3 (tyrosine phosphorylated). {ECO:0000250|UniProtKB:O14933}. +P61082 UBC12_MOUSE NEDD8-conjugating enzyme Ubc12 (EC 2.3.2.-) (NEDD8 carrier protein) (Ubiquitin-conjugating enzyme E2 M) 183 20,900 Active site (1); Chain (1); Modified residue (5); Region (1) Protein modification; protein neddylation. FUNCTION: Accepts the ubiquitin-like protein NEDD8 from the UBA3-NAE1 E1 complex and catalyzes its covalent attachment to other proteins. The specific interaction with the E3 ubiquitin ligase RBX1, but not RBX2, suggests that the RBX1-UBE2M complex neddylates specific target proteins, such as CUL1, CUL2, CUL3 and CUL4. Involved in cell proliferation (By similarity). {ECO:0000250}. PTM: The acetylation of Met-1 increases affinity for DCUN1D1 by about 2 orders of magnitude and is crucial for NEDD8 transfer to cullins. {ECO:0000250}. SUBUNIT: Interacts with UBA3 and RBX1. Interacts (acetylated at N-terminal methionine) with DCUN1D1 (via DCUN1 domain). {ECO:0000250|UniProtKB:P61081}. DOMAIN: Both the N-terminal docking peptide and the catalytic core domain must bind the UBA3-NAE1 complex simultaneously for optimal transfer of NEDD8. {ECO:0000250}. +Q9D2M8 UB2V2_MOUSE Ubiquitin-conjugating enzyme E2 variant 2 (Ubc-like protein MMS2) 145 16,367 Alternative sequence (1); Chain (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (1); Sequence conflict (6) FUNCTION: Has no ubiquitin ligase activity on its own. The UBE2V2/UBE2N heterodimer catalyzes the synthesis of non-canonical poly-ubiquitin chains that are linked through 'Lys-63'. This type of poly-ubiquitination does not lead to protein degradation by the proteasome. Mediates transcriptional activation of target genes. Plays a role in the control of progress through the cell cycle and differentiation. Plays a role in the error-free DNA repair pathway and contributes to the survival of cells after DNA damage. {ECO:0000269|PubMed:11406273}. SUBUNIT: Heterodimer with UBE2N. Binds CHFR (By similarity). {ECO:0000250}. +P61087 UBE2K_MOUSE Ubiquitin-conjugating enzyme E2 K (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme K) (Huntingtin-interacting protein 2) (HIP-2) (Ubiquitin carrier protein) (Ubiquitin-conjugating enzyme E2-25 kDa) (Ubiquitin-conjugating enzyme E2(25K)) (Ubiquitin-conjugating enzyme E2-25K) (Ubiquitin-protein ligase) 200 22,407 Active site (1); Chain (1); Cross-link (2); Domain (1); Initiator methionine (1); Modified residue (3); Sequence conflict (1) Protein modification; protein ubiquitination. FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro, in the presence or in the absence of BRCA1-BARD1 E3 ubiquitin-protein ligase complex, catalyzes the synthesis of 'Lys-48'-linked polyubiquitin chains. Does not transfer ubiquitin directly to but elongates monoubiquitinated substrate protein. Mediates the selective degradation of short-lived and abnormal proteins, such as the endoplasmic reticulum-associated degradation (ERAD) of misfolded lumenal proteins. Ubiquitinates huntingtin. May mediate foam cell formation by the suppression of apoptosis of lipid-bearing macrophages through ubiquitination and subsequence degradation of p53/TP53. Proposed to be involved in ubiquitination and proteolytic processing of NF-kappa-B; in vitro supports ubiquitination of NFKB1. Involved in stabilization of CASP12 during ER stress-mediated amyloid-beta neurotoxicity probably by inhibiting proteasome activity; in vitro ubiquitinates CASP12. {ECO:0000269|PubMed:18710920}. PTM: Sumoylation at Lys-14 impairs catalytic activity. {ECO:0000250|UniProtKB:P61085}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P61085}. SUBUNIT: Interacts with RNF138/NARF. Interacts with BRCA1. {ECO:0000250|UniProtKB:P61086}. TISSUE SPECIFICITY: Expressed in the brain, with highest levels found in the mitral cells of the olfactory bulb, the pyramidal cell layer of the hippocampus and the Purkinje cells of the cerebellar cortex. {ECO:0000269|PubMed:10585161}. +Q283N4 URAD_MOUSE 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase (OHCU decarboxylase) (EC 4.1.1.97) (Parahox neighbor) (Ureidoimidazoline (2-oxo-4-hydroxy-4-carboxy-5-) decarboxylase) 178 20,017 Active site (1); Binding site (1); Chain (1); Region (2) Purine metabolism; urate degradation; (S)-allantoin from urate: step 3/3. FUNCTION: Catalyzes the stereoselective decarboxylation of 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU) to (S)-allantoin. {ECO:0000250, ECO:0000269|PubMed:16462750}. SUBCELLULAR LOCATION: Peroxisome {ECO:0000305}. +Q8K2T4 UQCC3_MOUSE Ubiquinol-cytochrome-c reductase complex assembly factor 3 89 9,584 Chain (1); Region (1); Topological domain (2); Transmembrane (1) TRANSMEM 8 28 Helical. {ECO:0000255}. TOPO_DOM 1 7 Mitochondrial matrix. {ECO:0000250|UniProtKB:Q6UW78}.; TOPO_DOM 29 89 Mitochondrial intermembrane. {ECO:0000250|UniProtKB:Q6UW78}. FUNCTION: Required for the assembly of the ubiquinol-cytochrome c reductase complex (mitochondrial respiratory chain complex III or cytochrome b-c1 complex), mediating cytochrome b recruitment and probably stabilization within the complex. Thereby, plays an important role in ATP production by mitochondria. Cardiolipin-binding protein, it may also control the cardiolipin composition of mitochondria membranes and their morphology. {ECO:0000250|UniProtKB:Q6UW78}. PTM: Probably cleaved by OMA1 under mitochondrial stress conditions. {ECO:0000250|UniProtKB:Q6UW78}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q6UW78}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q6UW78}. SUBUNIT: Associates with the ubiquinol-cytochrome c reductase complex (mitochondrial respiratory chain complex III or cytochrome b-c1 complex). {ECO:0000250|UniProtKB:Q6UW78}. +Q9CQ56 USE1_MOUSE Vesicle transport protein USE1 (Protein D12) (USE1-like protein) 270 30,594 Alternative sequence (2); Chain (1); Coiled coil (1); Sequence conflict (3); Topological domain (2); Transmembrane (1) TRANSMEM 243 263 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 1 242 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 264 270 Lumenal. {ECO:0000255}. FUNCTION: SNARE that may be involved in targeting and fusion of Golgi-derived retrograde transport vesicles with the ER. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. SUBUNIT: Component of a SNARE complex consisting of STX18, USE1L, BNIP1/SEC20L and SEC22B. Interacts directly with STX18 (By similarity). {ECO:0000250}. +P70398 USP9X_MOUSE Probable ubiquitin carboxyl-terminal hydrolase FAF-X (EC 3.4.19.12) (Deubiquitinating enzyme FAF-X) (Fat facets homolog) (Fat facets protein-related, X-linked) (Ubiquitin carboxyl-terminal hydrolase FAM) (Ubiquitin thioesterase FAF-X) (Ubiquitin-specific protease 9, X chromosome) (Ubiquitin-specific-processing protease FAF-X) 2559 290,711 Active site (2); Chain (1); Domain (1); Modified residue (8); Sequence conflict (13) FUNCTION: Deubiquitinase involved both in the processing of ubiquitin precursors and of ubiquitinated proteins. May therefore play an important regulatory role at the level of protein turnover by preventing degradation of proteins through the removal of conjugated ubiquitin. Specifically hydrolyzes 'Lys-48'-, 'Lys-29'- and 'Lys-33'-linked polyubiquitins chains. Essential component of TGF-beta/BMP signaling cascade. Specifically deubiquitinates monoubiquitinated SMAD4, opposing the activity of E3 ubiquitin-protein ligase TRIM33. Deubiquitinates alkylation repair enzyme ALKBH3. OTUD4 recruits USP7 and USP9X to stabilize ALKBH3, thereby promoting the repair of alkylated DNA lesions. Regulates chromosome alignment and segregation in mitosis by regulating the localization of BIRC5/survivin to mitotic centromeres (By similarity). Involved in axonal growth and neuronal cell migration (By similarity) (PubMed:24607389). Regulates cellular clock function by enhancing the protein stability and transcriptional activity of the core circadian protein ARNTL/BMAL1 via its deubiquitinating activity (PubMed:29626158). {ECO:0000250|UniProtKB:Q93008, ECO:0000269|PubMed:24607389, ECO:0000269|PubMed:29626158}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q93008}. Cell projection, growth cone {ECO:0000269|PubMed:24607389}. SUBUNIT: Interacts with SMAD4, MARK4, NUAK1 and BIRC5/survivin. Interacts with DCX. Interacts with OTUD4 and USP7; the interaction is direct (By similarity). Interacts with ARNTL/BMAL1 (PubMed:29626158). {ECO:0000250|UniProtKB:Q93008, ECO:0000269|PubMed:29626158}. TISSUE SPECIFICITY: Ubiquitously expressed in adult tissues. +Q9ES64 USH1C_MOUSE Harmonin (PDZ domain-containing protein) (Usher syndrome type-1C protein homolog) 910 102,285 Alternative sequence (5); Beta strand (6); Chain (1); Coiled coil (2); Domain (3); Helix (3); Modified residue (1); Region (2); Sequence conflict (2) FUNCTION: Anchoring/scaffolding protein that is a part of the functional network formed by USH1C, USH1G, CDH23 and MYO7A that mediates mechanotransduction in cochlear hair cells. Required for normal development and maintenance of cochlear hair cell bundles (PubMed:19447093). As part of the intermicrovillar adhesion complex/IMAC plays a role in brush border differentiation, controlling microvilli organization and length. Probably plays a central regulatory role in the assembly of the complex, recruiting CDHR2, CDHR5 and MYO7B to the microvilli tips (PubMed:24725409, PubMed:26812018). {ECO:0000269|PubMed:19447093, ECO:0000269|PubMed:24725409, ECO:0000269|PubMed:26812018}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9Y6N9}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19447093}. Cell projection, microvillus {ECO:0000269|PubMed:24725409}. Note=Colocalizes with F-actin (PubMed:19447093). Detected at the tip of cochlear hair cell stereocilia (PubMed:19447093). Enriched in microvilli of the intestinal brush border (PubMed:24725409). {ECO:0000269|PubMed:19447093, ECO:0000269|PubMed:24725409}. SUBUNIT: Part of the IMAC/intermicrovillar adhesion complex/intermicrovillar tip-link complex composed of ANKS4B, MYO7B, USH1C, CDHR2 and CDHR5 (By similarity). Part of a complex composed of USH1C, USH1G and MYO7A (By similarity). Interacts with F-actin (PubMed:19447093). Interacts with USH2A (PubMed:16301217). Interacts with SLC4A7 (PubMed:16301216). Interacts (via PDZ1 domain) with the C-terminus of USHBP1 (By similarity). Interacts (via N-terminus and PDZ 2 domain) with CDH23 (PubMed:19447093). Interacts with USH1G (By similarity). Interacts with MYO7B (PubMed:26812017). Interacts with CDHR2 and CDHR5; may mediate their interaction with MYO7B at the microvilli tip (By similarity) (PubMed:26812017). Interacts (via PDZ 1 domain) with ANKS4B (PubMed:12588794, PubMed:15461667). {ECO:0000250|UniProtKB:Q9Y6N9, ECO:0000269|PubMed:12588794, ECO:0000269|PubMed:15461667, ECO:0000269|PubMed:16301216, ECO:0000269|PubMed:16301217, ECO:0000269|PubMed:19447093, ECO:0000269|PubMed:26812017}. DOMAIN: The PDZ 1 domain mediates interaction with ANKS4B, USHBP1, USH1G, SLC4A7. {ECO:0000250|UniProtKB:Q9Y6N9, ECO:0000269|PubMed:15461667}.; DOMAIN: The N-terminal region constitutes an independently folded domain that has structural similarity with the CCM2 C-terminus, despite very low sequence similarity. {ECO:0000250|UniProtKB:Q9Y6N9}. TISSUE SPECIFICITY: Detected in stereocilia of cochlear hair cells (at protein level). Isoform 1 is expressed in the eye, cochlea, vestibule, heart, kidney, small intestine and testis; it is barely visible in skeletal muscle, liver, and lung and is absent from the brain. Isoforms 2 and 3 are expressed in the cochlea and vestibule. {ECO:0000269|PubMed:10973247, ECO:0000269|PubMed:19447093, ECO:0000269|PubMed:24725409}. +Q8K245 UVRAG_MOUSE UV radiation resistance associated protein 698 77,525 Chain (1); Coiled coil (1); Domain (1); Helix (1); Modified residue (9); Region (3); Sequence conflict (3) FUNCTION: Versatile protein that is involved in regulation of different cellular pathways implicated in membrane trafficking. Involved in regulation of the COPI-dependent retrograde transport from Golgi and the endoplasmic reticulum by associating with the NRZ complex; the function is dependent on its binding to phosphatidylinositol 3-phosphate (PtdIns(3)P). During autophagy acts as regulatory subunit of the alternative PI3K complex II (PI3KC3-C2) that mediates formation of phosphatidylinositol 3-phosphate and is believed to be involved in maturation of autophagosomes and endocytosis. Activates lipid kinase activity of PIK3C3. Involved in the regulation of degradative endocytic trafficking and cytokinesis, and in regulation of ATG9A transport from the Golgi to the autophagosome; the functions seems to implicate its association with PI3KC3-C2. Involved in maturation of autophagosomes and degradative endocytic trafficking independently of BECN1 but depending on its association with a class C Vps complex (possibly the HOPS complex); the association is also proposed to promote autophagosome recruitment and activation of Rab7 and endosome-endosome fusion events. Enhances class C Vps complex (possibly HOPS complex) association with a SNARE complex and promotes fusogenic SNARE complex formation during late endocytic membrane fusion. In case of negative-strand RNA virus infection is required for efficient virus entry, promotes endocytic transport of virions and is implicated in a VAMP8-specific fusogenic SNARE complex assembly (By similarity). {ECO:0000250|UniProtKB:Q9P2Y5, ECO:0000305}.; FUNCTION: Involved in maintaining chromosomal stability. Promotes DNA double-strand break (DSB) repair by association with DNA-dependent protein kinase complex DNA-PK and activating it in non-homologous end joining (NHEJ). Required for centrosome stability and proper chromosome segregation (By similarity). {ECO:0000250|UniProtKB:Q9P2Y5}. PTM: Phosphorylated at Ser-497 by MTOR under basal conditions; increases the interaction with RUBCN implicated in inhibitory effect of RUBCN on PI3KC3 and decreases interaction with RAB7A, and VPS16 and VPS39 (indicative for a class C Vps complex, possibly the HOPS complex) (By similarity). {ECO:0000250|UniProtKB:Q9P2Y5}. SUBCELLULAR LOCATION: Late endosome {ECO:0000250|UniProtKB:Q9P2Y5}. Lysosome {ECO:0000250|UniProtKB:Q9P2Y5}. Early endosome {ECO:0000250|UniProtKB:Q9P2Y5}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9P2Y5}. Midbody {ECO:0000250|UniProtKB:Q9P2Y5}. Chromosome, centromere {ECO:0000250|UniProtKB:Q9P2Y5}. Note=Colocalizes with RAB9-positive compartments involved in retrograde transport from late endosomes to trans-Golgi network. Colocalization with early endosomes is only partial (By similarity). {ECO:0000250|UniProtKB:Q9P2Y5}. SUBUNIT: Component of the PI3K (PI3KC3/PI3K-III/class III phosphatidylinositol 3-kinase) complex II (PI3KC3-C2) in which the core composed of the catalytic subunit PIK3C3, the regulatory subunit PIK3R4 and BECN1 is associated with UVRAG; in the complex interacts directly with BECN1. PI3KC3-C2 can associate with further regulatory subunits such as RUBCN and probably SH3GLB1/Bif-1. Interacts with SH3GLB1; UVRAG bridges the interaction to BECN1 indicative for an association with the PI3K complex PI3KC3-C2. Interacts with RINT1. Associates with the NRZ complex under basal conditions and dissociates from it under autophagy conditions to associate with the PI3K complex; these complex associations seem to be mutually exclusive. Interacts with VPS16; VPS11; VPS18; VPS33 (VPS33A or VPS33B) and VPS39; indicative for an association with a class C Vps tethering complex (possibly the HOPS complex). Interacts with RAB7A; RAB7A competes with UVRAG for RUBCN binding. Interacts with STX7, VTI1B, STX8. Interacts with PRKDC, XRCC6 and XRCC5; indicative for an association with the DNA-dependent protein kinase complex DNA-PK. Interacts with CEP63. Directly interacts with FEZ1 and SCOC; the interaction with SCOC is reduced by amino acid starvation, but the complex is stabilized in the presence of FEZ1. Interacts with BECN1P1/BECN2 (By similarity). Interacts with SLAMF1 (PubMed:22493499). {ECO:0000250|UniProtKB:Q9P2Y5, ECO:0000269|PubMed:22493499}. +Q9JKB3 YBOX3_MOUSE Y-box-binding protein 3 (Cold shock domain-containing protein A) (DNA-binding protein A) (Y-box protein 3) 361 38,814 Alternative sequence (1); Chain (1); Compositional bias (2); Domain (1); Initiator methionine (1); Modified residue (14); Sequence conflict (3) FUNCTION: Binds to the GM-CSF promoter. Seems to act as a repressor (By similarity). Binds also to full-length mRNA and to short RNA sequences containing the consensus site 5'-UCCAUCA-3'. May have a role in translation repression. {ECO:0000250, ECO:0000269|PubMed:12117816}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10772793}. Nucleus {ECO:0000250}. SUBUNIT: Found in a mRNP complex with YBX2 (PubMed:10772793). Interacts with RRP1B (By similarity). {ECO:0000250|UniProtKB:P16989, ECO:0000269|PubMed:10772793}. TISSUE SPECIFICITY: Expressed in oocytes, spermatocytes and spermatids (at protein level). Expressed in skeletal muscle, kidney, brain, spleen, liver, heart and spermatids. Isoform 2 is preferentially expressed in somatic tissues (PubMed:10956549). {ECO:0000269|PubMed:10772793, ECO:0000269|PubMed:10956549, ECO:0000269|PubMed:12117816}. +P62838 UB2D2_MOUSE Ubiquitin-conjugating enzyme E2 D2 (EC 2.3.2.23) ((E3-independent) E2 ubiquitin-conjugating enzyme D2) (EC 2.3.2.24) (E2 ubiquitin-conjugating enzyme D2) (Ubiquitin carrier protein D2) (Ubiquitin-conjugating enzyme E2(17)KB 2) (Ubiquitin-conjugating enzyme E2-17 kDa 2) (Ubiquitin-protein ligase D2) 147 16,735 Active site (1); Chain (1) Protein modification; protein ubiquitination. FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Mediates ubiquitination of PEX5 and autoubiquitination of STUB1 and TRAF6. Involved in the signal-induced conjugation and subsequent degradation of NFKBIA, FBXW2-mediated GCM1 ubiquitination and degradation, MDM2-dependent degradation of p53/TP53 and the activation of MAVS in the mitochondria by DDX58/RIG-I in response to viral infection. Essential for viral activation of IRF3. {ECO:0000250|UniProtKB:P62837}. SUBUNIT: Interacts with SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex. Interacts with CNOT4 (via RING domain). Interacts with E3 ubiquitin-protein ligases CBLC, PJA1 and PJA2. Interacts with PDZRN3. Interacts with PPP1R11 (PubMed:27805901). {ECO:0000250|UniProtKB:P62837, ECO:0000269|PubMed:12036302, ECO:0000269|PubMed:17576800, ECO:0000269|PubMed:27805901}. +Q8CGB3 UACA_MOUSE Uveal autoantigen with coiled-coil domains and ankyrin repeats (Nuclear membrane-binding protein) (Nucling) 1411 160,813 Alternative sequence (2); Chain (1); Coiled coil (3); Erroneous initiation (2); Modified residue (2); Repeat (6); Sequence conflict (4) FUNCTION: Regulates APAF1 expression and plays an important role in the regulation of stress-induced apoptosis. Promotes apoptosis by regulating three pathways, apoptosome up-regulation, LGALS3/galectin-3 down-regulation and NF-kappa-B inactivation. Regulates the redistribution of APAF1 into the nucleus after proapoptotic stress. Down-regulates the expression of LGALS3 by inhibiting NFKB1. {ECO:0000269|PubMed:14961764, ECO:0000269|PubMed:15271982}.; FUNCTION: Modulates isoactin dynamics to regulate the morphological alterations required for cell growth and motility. Interaction with ARF6 may modulate cell shape and motility after injury (By similarity). May be involved in multiple neurite formation (PubMed:23624502). {ECO:0000250|UniProtKB:Q8HYY4, ECO:0000269|PubMed:23624502}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12761289}. Cytoplasm {ECO:0000269|PubMed:12761289}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12761289}. Note=Expressed diffusely in cytoplasm. SUBUNIT: Component of the apoptosome complex, composed of APAF1, pro-caspase-9 and UACA. In the complex, it probably interacts directly with APAF1. Interacts with LGALS3, ARF6 and ACTB. Interacts with RAB39A. {ECO:0000269|PubMed:14961764, ECO:0000269|PubMed:15271982, ECO:0000269|PubMed:23624502}. TISSUE SPECIFICITY: Highly expressed in heart, liver, kidney and testis. Weakly expressed in lung and skeletal muscle. Not expressed in brain and spleen. {ECO:0000269|PubMed:12761289}. +Q6ZWZ2 UB2R2_MOUSE Ubiquitin-conjugating enzyme E2 R2 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme R2) (Ubiquitin carrier protein R2) (Ubiquitin-conjugating enzyme E2-CDC34B) (Ubiquitin-protein ligase R2) 238 27,166 Active site (1); Chain (1); Compositional bias (1); Modified residue (1); Sequence conflict (6) Protein modification; protein ubiquitination. FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes monoubiquitination and 'Lys-48'-linked polyubiquitination. May be involved in degradation of katenin. {ECO:0000250|UniProtKB:Q712K3}. SUBUNIT: When phosphorylated, interacts with beta-TrCP (BTRC). {ECO:0000250|UniProtKB:Q712K3}. +P52483 UB2E3_MOUSE Ubiquitin-conjugating enzyme E2 E3 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme E3) (UbcM2) (Ubiquitin carrier protein E3) (Ubiquitin-conjugating enzyme E2-23 kDa) (Ubiquitin-protein ligase E3) 207 22,913 Active site (1); Chain (1); Initiator methionine (1); Modified residue (2); Mutagenesis (1); Sequence conflict (1) Protein modification; protein ubiquitination. FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'- and 'Lys-48'-, as well as 'Lys-63'-linked polyubiquitination (By similarity). Participates in the regulation of transepithelial sodium transport in renal cells. May be involved in cell growth arrest. {ECO:0000250|UniProtKB:Q969T4, ECO:0000269|PubMed:14993279}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Shuttles between the nucleus and cytoplasm in a IPO11-dependent manner. SUBUNIT: Interacts with NEDD4L. The ubiquitin-loaded form interacts specifically with importin-11 (IPO11), leading to its import into the nucleus. {ECO:0000269|PubMed:11032817, ECO:0000269|PubMed:14993279, ECO:0000269|PubMed:15545318}. +Q3UWQ3 UB2FB_MOUSE NEDD8-conjugating enzyme UBE2F-B (EC 2.3.2.-) (NEDD8 carrier protein UBE2F-B) (NEDD8 protein ligase UBE2F-B) (RING-type E3 NEDD8 transferase UBE2F-B) (Ubiquitin-conjugating enzyme E2 F-B) 185 21,352 Active site (1); Chain (1) Protein modification; protein neddylation. FUNCTION: Accepts the ubiquitin-like protein NEDD8 from the UBA3-NAE1 E1 complex and catalyzes its covalent attachment to other proteins. The specific interaction with the E3 ubiquitin ligase RBX2, but not RBX1, suggests that the RBX2-UBE2F complex neddylates specific target proteins, such as CUL5. {ECO:0000250}. PTM: The acetylation of Met-1 increases affinity for DCUN1D3 by about 2 orders of magnitude and is crucial for NEDD8 transfer to cullins. {ECO:0000250}. SUBUNIT: Interacts with UBA3 and RBX2. {ECO:0000250}. +Q8VDW4 UBE2W_MOUSE Ubiquitin-conjugating enzyme E2 W (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme W) (N-terminal E2 ubiquitin-conjugating enzyme) (EC 2.3.2.25) (N-terminus-conjugating E2) (Ubiquitin carrier protein W) (Ubiquitin-protein ligase W) 151 17,345 Active site (1); Chain (1); Cross-link (1); Erroneous initiation (1); Mutagenesis (1); Sequence conflict (3) Protein modification; protein ubiquitination. FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Specifically monoubiquitinates the N-terminus of various substrates, including ATXN3, MAPT/TAU, POLR2H/RPB8 and STUB1/CHIP, by recognizing backbone atoms of disordered N-termini (PubMed:21855799, PubMed:21229326). Involved in degradation of misfolded chaperone substrates by mediating monoubiquitination of STUB1/CHIP, leading to recruitment of ATXN3 to monoubiquitinated STUB1/CHIP, and restriction of the length of ubiquitin chain attached to STUB1/CHIP substrates by ATXN3 (PubMed:21855799). After UV irradiation, but not after mitomycin-C (MMC) treatment, acts as a specific E2 ubiquitin-conjugating enzyme for the Fanconi anemia complex by associating with E3 ubiquitin-protein ligase FANCL and catalyzing monoubiquitination of FANCD2, a key step in the DNA damage pathway (PubMed:21229326). In vitro catalyzes 'Lys-11'-linked polyubiquitination. UBE2W-catalyzed ubiquitination occurs also in the presence of inactive RING/U-box type E3s, i.e. lacking the active site cysteine residues to form thioester bonds with ubiquitin, or even in the absence of E3, albeit at a slower rate (By similarity). {ECO:0000250|UniProtKB:Q96B02, ECO:0000269|PubMed:21229326, ECO:0000269|PubMed:21855799}. PTM: Autoubiquitinated at Met-1. {ECO:0000250|UniProtKB:Q96B02}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21229326}. Note=In the nucleus, colocalizes with FANCL. SUBUNIT: Homodimer (By similarity). Interacts with FANCL. Interacts with STUB1/CHIP. {ECO:0000250|UniProtKB:Q96B02, ECO:0000269|PubMed:21229326, ECO:0000269|PubMed:21855799}. +B2RUP2 UN13D_MOUSE Protein unc-13 homolog D (Munc13-4) 1085 123,119 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (4); Modified residue (1); Region (1); Sequence conflict (2) FUNCTION: Plays a role in cytotoxic granule exocytosis in lymphocytes. Required for both granule maturation and granule docking and priming at the immunologic synapse. Regulates assembly of recycling and late endosomal structures, leading to the formation of an endosomal exocytic compartment that fuses with perforin-containing granules at the immunologic synapse and licences them for exocytosis (By similarity). Regulates Ca(2+)-dependent secretory lysosome exocytosis in mast cells. {ECO:0000250, ECO:0000269|PubMed:18354201}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Late endosome {ECO:0000250}. Recycling endosome {ECO:0000250}. Lysosome {ECO:0000269|PubMed:18354201}. Note=Colocalizes with cytotoxic granules at the plasma membrane. Localizes to endosomal exocytic vesicles. {ECO:0000250}. SUBUNIT: Interacts with RAB27A and DOC2A. Both RAB27A and DOC2A can simultaneously bind UNC13D. {ECO:0000269|PubMed:18354201}. DOMAIN: The MHD1 and MHD2 domains mediate localization on recycling endosomes and lysosome. {ECO:0000250}. TISSUE SPECIFICITY: Mast cells. {ECO:0000269|PubMed:18354201}. +Q8CGY6 UN45B_MOUSE Protein unc-45 homolog B (Unc-45B) 931 103,638 Alternative sequence (1); Chain (1); Repeat (6); Sequence conflict (2) FUNCTION: Acts as a co-chaperone for HSP90 and is required for proper folding of the myosin motor domain. Plays a role in sarcomere formation during muscle cell development (PubMed:12356907, PubMed:18326487, PubMed:18478096). Is necessary for normal early lens development (By similarity). {ECO:0000250|UniProtKB:Q6DGE9, ECO:0000269|PubMed:12356907, ECO:0000269|PubMed:18326487, ECO:0000269|PubMed:18478096}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:18478096}. SUBUNIT: Interacts with HSP90 in an ATP-independent manner (PubMed:18326487, PubMed:18478096). Interacts with UBE4B; the interaction may target UNC45B for proteasomal degradation (By similarity). {ECO:0000250|UniProtKB:Q8IWX7, ECO:0000269|PubMed:18326487, ECO:0000269|PubMed:18478096}. TISSUE SPECIFICITY: Highly expressed in adult skeletal muscle and heart. Detected at intermediate levels in lung. Highly expressed in embryonic heart. {ECO:0000269|PubMed:12356907}. +Q6R653 UN5CL_MOUSE UNC5C-like protein (Protein unc-5 homolog C-like) (ZU5 and death domain-containing protein) 518 57,956 Active site (2); Alternative sequence (6); Chain (1); Domain (2); Frameshift (1); Region (2); Sequence conflict (4); Topological domain (2); Transmembrane (1) TRANSMEM 11 31 Helical; Signal-anchor for type III membrane protein. {ECO:0000255}. TOPO_DOM 1 10 Extracellular. {ECO:0000255}.; TOPO_DOM 32 518 Cytoplasmic. {ECO:0000255}. FUNCTION: Inhibits NF-kappa-B-dependent transcription by impairing NF-kappa-B binding to its targets. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type III membrane protein {ECO:0000305}. Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with p65/RELA and NFKB1. {ECO:0000250}. +Q8VCW4 UN93B_MOUSE Protein unc-93 homolog B1 (Unc-93B1) 598 66,981 Alternative sequence (1); Chain (1); Erroneous initiation (1); Glycosylation (3); Modified residue (2); Mutagenesis (3); Sequence conflict (8); Transmembrane (12) TRANSMEM 64 84 Helical. {ECO:0000255}.; TRANSMEM 110 130 Helical. {ECO:0000255}.; TRANSMEM 132 152 Helical. {ECO:0000255}.; TRANSMEM 160 180 Helical. {ECO:0000255}.; TRANSMEM 223 243 Helical. {ECO:0000255}.; TRANSMEM 285 305 Helical. {ECO:0000255}.; TRANSMEM 343 363 Helical. {ECO:0000255}.; TRANSMEM 378 398 Helical. {ECO:0000255}.; TRANSMEM 403 423 Helical. {ECO:0000255}.; TRANSMEM 428 448 Helical. {ECO:0000255}.; TRANSMEM 469 489 Helical. {ECO:0000255}.; TRANSMEM 495 515 Helical. {ECO:0000255}. FUNCTION: Plays an important role in innate and adaptive immunity by regulating nucleotide-sensing Toll-like receptor (TLR) signaling. Required for the transport of a subset of TLRs (including TLR3, TLR7 and TLR9) from the endoplasmic reticulum to endolysosomes where they can engage pathogen nucleotides and activate signaling cascades. May play a role in autoreactive B-cells removal. {ECO:0000269|PubMed:16415873, ECO:0000269|PubMed:17452530, ECO:0000269|PubMed:18305481}. PTM: N-glycosylated. {ECO:0000269|PubMed:17452530}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. Endosome. Lysosome. Cytoplasmic vesicle, phagosome. Note=Colocalizes with LAMP5 in large endosomal intracellular vesicles (By similarity). Relocalizes from endoplasmic reticulum to endosome and lysosome upon cell-stimulation with CpG dinucleotides. {ECO:0000250}. SUBUNIT: Interacts with TLR3, TLR7, TLR8, TLR9 and TLR13 (probably via transmembrane domain). {ECO:0000269|PubMed:17452530, ECO:0000269|PubMed:19451267}. +Q4KUS2 UN13A_MOUSE Protein unc-13 homolog A (Munc13-1) 1712 193,782 Chain (1); Coiled coil (1); Compositional bias (1); Domain (5); Metal binding (6); Modified residue (4); Mutagenesis (1); Sequence conflict (2); Zinc finger (1) FUNCTION: Plays a role in vesicle maturation during exocytosis as a target of the diacylglycerol second messenger pathway. Involved in neurotransmitter release by acting in synaptic vesicle priming prior to vesicle fusion and participates in the activity-dependent refilling of readily releasable vesicle pool (RRP). Essential for synaptic vesicle maturation in most excitatory/glutamatergic but not inhibitory/GABA-mediated synapses. Also involved in secretory granule priming in insulin secretion. Plays a role in dendrite formation by melanocytes (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9UPW8, ECO:0000269|PubMed:10440375, ECO:0000269|PubMed:12070347, ECO:0000269|PubMed:15988013, ECO:0000269|PubMed:16644700, ECO:0000269|PubMed:16697276, ECO:0000269|PubMed:17267576, ECO:0000269|PubMed:17639022}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q62768}. Cell membrane {ECO:0000250|UniProtKB:Q62768}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q62768}. Cell junction, synapse, presynaptic cell membrane {ECO:0000250|UniProtKB:Q62768}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q62768}. Note=Localized to the active zone of presynaptic density. Translocated to the plasma membrane in response to phorbol ester binding (By similarity). {ECO:0000250|UniProtKB:Q62768}. SUBUNIT: Interacts with the N-termini of STX1A and/or STX1B1 and DOC2A. Interacts with BSN. Interacts with RIMS1 which recruits UNC13A to the active zone. Forms homodimers via its first C2 domain. Also interacts via this domain with the zinc finger domain of RIMS2. Part of a complex consisting of ERC2, RIMS1 and UNC13A. Also part of a complex consisting of UNC13A, RIMS2 and RAB3A (By similarity). Interacts with FBXO45 (via SRY domain); leading to the degradation of UNC13A by the proteasome. {ECO:0000250, ECO:0000269|PubMed:19996097}. DOMAIN: The C2 domains are not involved in calcium-dependent phospholipid binding. {ECO:0000250|UniProtKB:Q62768}.; DOMAIN: The C-terminal region containing both MHD domains and the third C2 domain is required for synaptic vesicle priming activity. {ECO:0000250|UniProtKB:Q62768}. +Q8K1S3 UNC5B_MOUSE Netrin receptor UNC5B (Protein unc-5 homolog 2) (Protein unc-5 homolog B) 945 103,739 Alternative sequence (1); Chain (1); Disulfide bond (9); Domain (6); Erroneous initiation (1); Glycosylation (2); Helix (8); Lipidation (1); Modified residue (1); Region (2); Sequence conflict (4); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 378 398 Helical. {ECO:0000255}. TOPO_DOM 27 377 Extracellular. {ECO:0000255}.; TOPO_DOM 399 945 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for netrin required for axon guidance. Mediates axon repulsion of neuronal growth cones in the developing nervous system upon ligand binding. Axon repulsion in growth cones may be caused by its association with DCC that may trigger signaling for repulsion (By similarity). Functions as netrin receptor that negatively regulates vascular branching during angiogenesis (PubMed:15510105). Mediates retraction of tip cell filopodia on endothelial growth cones in response to netrin (PubMed:15510105). It also acts as a dependence receptor required for apoptosis induction when not associated with netrin ligand. Mediates apoptosis by activating DAPK1. In the absence of NTN1, activates DAPK1 by reducing its autoinhibitory phosphorylation at Ser-308 thereby increasing its catalytic activity (By similarity). {ECO:0000250|UniProtKB:O08722, ECO:0000269|PubMed:15510105}. PTM: Phosphorylated on cytoplasmic tyrosine residues. {ECO:0000250}.; PTM: Palmitoylation is required for pro-apoptotic activity, but not for location at lipid rafts. {ECO:0000250|UniProtKB:O08722}.; PTM: Proteolytically cleaved by caspases during apoptosis. The cleavage does not take place when the receptor is associated with netrin ligand. Its cleavage by caspases is required to induce apoptosis. {ECO:0000250|UniProtKB:O08722}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19492039, ECO:0000269|PubMed:21673655, ECO:0000269|PubMed:25374360}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:O08722}. Membrane raft {ECO:0000250|UniProtKB:O08722}. Note=Associated with lipid rafts. {ECO:0000250|UniProtKB:O08722}. SUBUNIT: Interacts with the cytoplasmic part of DCC (By similarity). Interacts with GNAI2 via its cytoplasmic part. Interacts (via death domain) with DAPK1 (via death domain) (By similarity). Interacts (via extracellular domain) with FLRT2 and FLRT3 (via extracellular domain), but has higher affinity for FLRT3 (PubMed:19492039, PubMed:21673655, PubMed:22405201, PubMed:25374360). Identified in a complex with FLRT3 and ADGRL3; does not interact with ADGRL3 by itself (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O08722, ECO:0000250|UniProtKB:Q8IZJ1, ECO:0000269|PubMed:19492039, ECO:0000269|PubMed:21673655, ECO:0000269|PubMed:22405201, ECO:0000269|PubMed:25374360}. TISSUE SPECIFICITY: Highly expressed in brain. Expressed in lung during late development. Expressed during early blood vessel formation, in the semicircular canal and in a dorsal to ventral gradient in the retina. {ECO:0000269|PubMed:12351186, ECO:0000269|PubMed:12799072, ECO:0000269|PubMed:15510105}. +O08747 UNC5C_MOUSE Netrin receptor UNC5C (Protein unc-5 homolog 3) (Protein unc-5 homolog C) (Rostral cerebellar malformation protein) 931 103,063 Alternative sequence (1); Chain (1); Disulfide bond (9); Domain (6); Glycosylation (2); Modified residue (2); Mutagenesis (1); Region (1); Sequence conflict (3); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 381 401 Helical. {ECO:0000255}. TOPO_DOM 41 380 Extracellular. {ECO:0000255}.; TOPO_DOM 402 931 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for netrin required for axon guidance. Mediates axon repulsion of neuronal growth cones in the developing nervous system upon ligand binding. Axon repulsion in growth cones may be caused by its association with DCC that may trigger signaling for repulsion. Also involved in corticospinal tract axon guidances independently of DCC (PubMed:9126743, PubMed:9389662, PubMed:12451134). It also acts as a dependence receptor required for apoptosis induction when not associated with netrin ligand (By similarity). {ECO:0000250|UniProtKB:Q761X5, ECO:0000269|PubMed:12451134, ECO:0000269|PubMed:9126743, ECO:0000269|PubMed:9389662}. PTM: Phosphorylated on different cytoplasmic tyrosine residues. Phosphorylation of Tyr-568 leads to an interaction with PTPN11 phosphatase, suggesting that its activity is regulated by phosphorylation/dephosphorylation. Tyrosine phosphorylation is netrin-dependent. {ECO:0000269|PubMed:11533026}.; PTM: Proteolytically cleaved by caspases during apoptosis. The cleavage does not take place when the receptor is associated with netrin ligand. Its cleavage by caspases is required to induce apoptosis. {ECO:0000250|UniProtKB:Q761X5}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22405201}; Single-pass type I membrane protein {ECO:0000305}. Cell junction, synapse, synaptosome {ECO:0000250|UniProtKB:Q761X5}. SUBUNIT: Interacts with the cytoplasmic part of DCC (PubMed:10399920, PubMed:11533026). Interacts (tyrosine phosphorylated form) with PTPN11 (PubMed:11533026). Interacts (via extracellular domain) with FLRT3 (via extracellular domain) (PubMed:22405201). {ECO:0000269|PubMed:10399920, ECO:0000269|PubMed:11533026, ECO:0000269|PubMed:22405201}. TISSUE SPECIFICITY: Mainly expressed in regions of differentiating neurons. Highly expressed in brain and lung. Weakly expressed in testis, ovary, spleen, thymus and bladder. Expressed at very low level in kidney, intestine and salivary gland. {ECO:0000269|PubMed:9126743, ECO:0000269|PubMed:9389662}. DISEASE: Note=Defects in Unc5c are the cause of rostral cerebellar malformation (Rcm). Rcm is characterized by cerebellar and midbrain defects, apparently as a result of abnormal neuronal migration. {ECO:0000269|PubMed:9126743}. +Q8BLN6 UNC80_MOUSE Protein unc-80 homolog (mUNC-80) 3261 363,504 Alternative sequence (2); Chain (1); Compositional bias (1); Erroneous gene model prediction (4); Frameshift (1); Modified residue (3); Mutagenesis (1); Sequence conflict (1); Transmembrane (4) TRANSMEM 2271 2291 Helical. {ECO:0000255}.; TRANSMEM 2401 2421 Helical. {ECO:0000255}.; TRANSMEM 2788 2808 Helical. {ECO:0000255}.; TRANSMEM 2834 2854 Helical. {ECO:0000255}. FUNCTION: Component of the NALCN sodium channel complex, required for channel regulation. This complex is a cation channel activated by neuropeptides substance P, neurotensin, and extracellular calcium that regulates neuronal excitability by controlling the sizes of NALCN-dependent sodium-leak current. UNC80 is essential for NALCN sensitivity to extracellular calcium. {ECO:0000269|PubMed:19092807, ECO:0000269|PubMed:21040849}. PTM: Phosphorylated on tyrosine residues. {ECO:0000269|PubMed:19092807}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Found in a complex with NALCN, UNC79 and UNC80; UNC80 bridges NALCN to UNC79 (PubMed:21040849). Interacts with NALCN (PubMed:19092807,PubMed:21040849). Interacts with UNC79 (PubMed:21040849,PubMed:19092807). {ECO:0000269|PubMed:19092807, ECO:0000269|PubMed:21040849}. TISSUE SPECIFICITY: Expressed almost exclusively in the brain (PubMed:26708753). Expressed in hippocampus and ventral tegmental area neurons (PubMed:19092807). {ECO:0000269|PubMed:19092807, ECO:0000269|PubMed:26708753}. +Q9D132 UPK1A_MOUSE Uroplakin-1a (UP1a) (Uroplakin Ia) (UPIa) (UPKa) 257 28,854 Chain (1); Glycosylation (1); Topological domain (5); Transmembrane (4) TRANSMEM 14 34 Helical. {ECO:0000255}.; TRANSMEM 59 85 Helical. {ECO:0000255}.; TRANSMEM 91 111 Helical. {ECO:0000255}.; TRANSMEM 230 251 Helical. {ECO:0000255}. TOPO_DOM 1 13 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 35 58 Extracellular. {ECO:0000255}.; TOPO_DOM 86 90 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 112 229 Extracellular. {ECO:0000255}.; TOPO_DOM 252 257 Cytoplasmic. {ECO:0000255}. FUNCTION: Component of the asymmetric unit membrane (AUM); a highly specialized biomembrane elaborated by terminally differentiated urothelial cells. May play an important role in normal bladder epithelial physiology, possibly in regulating membrane permeability of superficial umbrella cells or in stabilizing the apical membrane through AUM/cytoskeletal interactions (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SUBUNIT: Homodimer; disulfide-linked. Interacts with uroplakin-2 (UPK2) (By similarity). Binds to uropathogenic E.coli fimH. {ECO:0000250, ECO:0000269|PubMed:11739641}. +P38575 UPK2_MOUSE Uroplakin-2 (UP2) (Uroplakin II) (UPII) 184 19,572 Chain (1); Glycosylation (3); Propeptide (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 156 180 Helical. {ECO:0000255}. TOPO_DOM 85 155 Lumenal. {ECO:0000255}.; TOPO_DOM 181 184 Cytoplasmic. {ECO:0000255}. FUNCTION: Component of the asymmetric unit membrane (AUM); a highly specialized biomembrane elaborated by terminally differentiated urothelial cells. May play an important role in regulating the assembly of the AUM. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Heterodimer formation with UPK1A is a prerequisite to exit out of the endoplasmic reticulum (ER). {ECO:0000250}. SUBUNIT: Interacts with uroplakin-1a (UPK1A). {ECO:0000250}. +Q8VIH9 UR2R_MOUSE Urotensin-2 receptor (UR-2-R) (G-protein coupled receptor 14) (Urotensin II receptor) (UR-II-R) 385 42,523 Chain (1); Disulfide bond (1); Glycosylation (2); Topological domain (8); Transmembrane (7) TRANSMEM 54 76 Helical; Name=1. {ECO:0000255}.; TRANSMEM 87 112 Helical; Name=2. {ECO:0000255}.; TRANSMEM 124 145 Helical; Name=3. {ECO:0000255}.; TRANSMEM 167 185 Helical; Name=4. {ECO:0000255}.; TRANSMEM 209 231 Helical; Name=5. {ECO:0000255}.; TRANSMEM 258 283 Helical; Name=6. {ECO:0000255}.; TRANSMEM 299 320 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 53 Extracellular. {ECO:0000255}.; TOPO_DOM 77 86 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 113 123 Extracellular. {ECO:0000255}.; TOPO_DOM 146 166 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 186 208 Extracellular. {ECO:0000255}.; TOPO_DOM 232 257 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 284 298 Extracellular. {ECO:0000255}.; TOPO_DOM 321 385 Cytoplasmic. {ECO:0000255}. FUNCTION: High affinity receptor for urotensin-2 and urotensin-2B. The activity of this receptor is mediated by a G-protein that activate a phosphatidylinositol-calcium second messenger system (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +P46938 YAP1_MOUSE Transcriptional coactivator YAP1 (Yes-associated protein 1) (Protein yorkie homolog) (Yes-associated protein YAP65 homolog) 488 52,383 Alternative sequence (1); Beta strand (1); Chain (1); Coiled coil (2); Compositional bias (1); Domain (2); Helix (3); Modified residue (22); Region (1) FUNCTION: Transcriptional regulator which can act both as a coactivator and a corepressor and is the critical downstream regulatory target in the Hippo signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Plays a key role in tissue tension and 3D tissue shape by regulating cortical actomyosin network formation. Acts via ARHGAP18, a Rho GTPase activating protein that suppresses F-actin polymerization. Plays a key role to control cell proliferation in response to cell contact. Phosphorylation of YAP1 by LATS1/2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. The presence of TEAD transcription factors are required for it to stimulate gene expression, cell growth, anchorage-independent growth, and epithelial mesenchymal transition (EMT) induction. {ECO:0000250|UniProtKB:P46937}. PTM: Phosphorylated by LATS1 and LATS2; leading to cytoplasmic translocation and inactivation. Phosphorylated by ABL1; leading to YAP1 stabilization, enhanced interaction with TP73 and recruitment onto proapoptotic genes; in response to DNA damage. Phosphorylation at Ser-385 and Ser-388 by CK1 is triggered by previous phosphorylation at Ser-382 by LATS proteins and leads to YAP1 ubiquitination by SCF(beta-TRCP) E3 ubiquitin ligase and subsequent degradation (By similarity). Phosphorylated at Thr-104, Ser-123, Ser-352 and Thr-397 by MAPK8/JNK1 and MAPK9/JNK2, which is required for the regulation of apoptosis by YAP1 (By similarity). {ECO:0000250|UniProtKB:P46937}.; PTM: Ubiquitinated by SCF(beta-TRCP) E3 ubiquitin ligase. {ECO:0000250|UniProtKB:P46937}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P46937}. Nucleus {ECO:0000269|PubMed:28087714}. Note=Both phosphorylation and cell density can regulate its subcellular localization. Phosphorylation sequesters it in the cytoplasm by inhibiting its translocation into the nucleus. At low density, predominantly nuclear and is translocated to the cytoplasm at high density. PTPN14 induces translocation from the nucleus to the cytoplasm. {ECO:0000250|UniProtKB:P46937}. SUBUNIT: Binds to the SH3 domain of the YES kinase (By similarity). Binds to WBP1 and WBP2 (PubMed:7644498). Binds, in vitro, through the WW1 domain, to neural isoforms of ENAH that contain the PPSY motif (PubMed:9407065). The phosphorylated form interacts with YWHAB (By similarity). Interacts (via WW domains) with LATS1 (via PPxY motif 2) (By similarity). Interacts with LATS2 (By similarity). Interacts (via WW domain 1) with isoform JM-A of ERBB4 (via PPxY motif 2) (By similarity). Interacts with TEAD1, TEAD2 and TEAD3 (By similarity). Interacts with TP73 and HCK (By similarity). Interacts with RUNX1 (By similarity). Interacts with TEAD4 (PubMed:20123908). Interacts (via WW domains) with PTPN14 (via PPxY motif 2); this interaction leads to the cytoplasmic sequestration of YAP1 and inhibits its transcriptional co-activator activity (By similarity). {ECO:0000250|UniProtKB:P46937, ECO:0000269|PubMed:20123908, ECO:0000269|PubMed:7644498, ECO:0000269|PubMed:9407065}. DOMAIN: The first coiled-coil region mediates most of the interaction with TEAD transcription factors. {ECO:0000250|UniProtKB:P46937}. TISSUE SPECIFICITY: Isoforms lacking the transactivation domain seen in striatal neurons (at protein level). Ubiquitous. Isoform 2 is expressed at higher levels in the neural tissues. In the embryo, it is expressed in brain, eye, and the maxillary and frontonasal components of the primary palate. {ECO:0000269|PubMed:12807903, ECO:0000269|PubMed:16461361, ECO:0000269|PubMed:24462371}. +Q8R4T9 UT2_MOUSE Urea transporter 2 (Solute carrier family 14 member 2) (Urea transporter, kidney) 930 102,047 Alternative sequence (4); Chain (1); Glycosylation (1); Modified residue (1); Sequence conflict (7); Transmembrane (16) TRANSMEM 145 165 Helical. {ECO:0000255}.; TRANSMEM 185 205 Helical. {ECO:0000255}.; TRANSMEM 213 233 Helical. {ECO:0000255}.; TRANSMEM 242 262 Helical. {ECO:0000255}.; TRANSMEM 280 300 Helical. {ECO:0000255}.; TRANSMEM 311 331 Helical. {ECO:0000255}.; TRANSMEM 350 372 Helical. {ECO:0000255}.; TRANSMEM 401 421 Helical. {ECO:0000255}.; TRANSMEM 610 630 Helical. {ECO:0000255}.; TRANSMEM 648 668 Helical. {ECO:0000255}.; TRANSMEM 676 696 Helical. {ECO:0000255}.; TRANSMEM 705 725 Helical. {ECO:0000255}.; TRANSMEM 774 794 Helical. {ECO:0000255}.; TRANSMEM 813 833 Helical. {ECO:0000255}.; TRANSMEM 842 862 Helical. {ECO:0000255}.; TRANSMEM 864 884 Helical. {ECO:0000255}. FUNCTION: Specialized low-affinity vasopressin-regulated urea transporter. Mediates rapid transepithelial urea transport across the inner medullary collecting duct and plays a major role in the urinary concentrating mechanism. Vasopressin regulates urea transport by increasing isoform A1 accumulation in the plasma membrane and/or phosphorylation of isoform A1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Isoform A1 interacts with SNAPIN which may be important for recruitment to the plasma membrane. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in kidney medulla. Also detected at the protein level in testes, heart, brain and liver. In the kidney, present in thin descending limbs of the loop of Henle and in the middle and terminal inner medullary collecting ducts. Isoform A5 is expressed in the peritubular myoid cells forming the outermost layer of the seminiferous tubules within the testes and is not detected in kidney. Isoform A5 mRNA levels are coordinated with the stage of testes development and increase 15 days postpartum, commensurate with the start of seminiferous tubule fluid movement. {ECO:0000269|PubMed:12217874}. +Q5SSI6 UTP18_MOUSE U3 small nucleolar RNA-associated protein 18 homolog (WD repeat-containing protein 50) 552 61,218 Chain (1); Cross-link (4); Modified residue (8); Repeat (6) FUNCTION: Involved in nucleolar processing of pre-18S ribosomal RNA. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. +Q78IK2 USMG5_MOUSE Up-regulated during skeletal muscle growth protein 5 (ATP synthase membrane subunit DAPIT) (Diabetes-associated protein in insulin-sensitive tissues) 58 6,382 Chain (1); Modified residue (2); Sequence conflict (4); Transmembrane (1) TRANSMEM 23 45 Helical. {ECO:0000255}. FUNCTION: Plays a critical role in maintaining the ATP synthase population in mitochondria. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. SUBUNIT: Component of an ATP synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MD and MP68. {ECO:0000250}. +Q6J1H4 UTF1_MOUSE Undifferentiated embryonic cell transcription factor 1 339 36,408 Alternative sequence (1); Chain (1); Erroneous initiation (1); Modified residue (4); Region (1) FUNCTION: Acts as a transcriptional coactivator of ATF2. {ECO:0000269|PubMed:9524124}. PTM: Phosphorylated. {ECO:0000269|PubMed:9524124}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Binds to the N-terminal region of ATF2. Associates with the TFIID complex through interaction with TBP. {ECO:0000269|PubMed:9524124}. DOMAIN: The leucine-zipper domain is required for coactivation activity. When this domain is deleted, the protein is able to stimulate transcription from a number of gene promoters. {ECO:0000269|PubMed:10329418}. TISSUE SPECIFICITY: Expressed mainly in pluripotent cells with expression rapidly down-regulated upon cell differentiation. {ECO:0000269|PubMed:9524124}. +Q9CZJ1 UTP11_MOUSE Probable U3 small nucleolar RNA-associated protein 11 (U3 snoRNA-associated protein 11) (UTP11-like protein) 253 30,551 Chain (1); Cross-link (11); Modified residue (2) FUNCTION: Involved in nucleolar processing of pre-18S ribosomal RNA. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. SUBUNIT: Component of the ribosomal small subunit (SSU) processome. {ECO:0000250}. +P07607 TYSY_MOUSE Thymidylate synthase (TS) (TSase) (EC 2.1.1.45) 307 34,958 Active site (1); Beta strand (12); Binding site (4); Chain (1); Cross-link (2); Helix (12); Modified residue (1); Nucleotide binding (3); Turn (4) Pyrimidine metabolism; dTTP biosynthesis. FUNCTION: Contributes to the de novo mitochondrial thymidylate biosynthesis pathway. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Mitochondrion {ECO:0000250}. Mitochondrion matrix {ECO:0000250}. Mitochondrion inner membrane {ECO:0000250}. SUBUNIT: Homodimer. +Q8R1K1 UBAC2_MOUSE Ubiquitin-associated domain-containing protein 2 (UBA domain-containing protein 2) (Phosphoglycerate dehydrogenase-like protein 1) 345 39,057 Chain (1); Domain (1); Glycosylation (1); Signal peptide (1); Topological domain (4); Transmembrane (3) TRANSMEM 92 112 Helical. {ECO:0000255}.; TRANSMEM 126 146 Helical. {ECO:0000255}.; TRANSMEM 164 184 Helical. {ECO:0000255}. TOPO_DOM 40 91 Extracellular. {ECO:0000255}.; TOPO_DOM 113 125 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 147 163 Extracellular. {ECO:0000255}.; TOPO_DOM 185 345 Cytoplasmic. {ECO:0000255}. FUNCTION: Restricts trafficking of FAF2 from the endoplasmic reticulum to lipid droplets. {ECO:0000250|UniProtKB:Q8NBM4}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8NBM4}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Interacts with FAF2. {ECO:0000250|UniProtKB:Q8NBM4}. +Q3UJD6 UBP19_MOUSE Ubiquitin carboxyl-terminal hydrolase 19 (EC 3.4.19.12) (Deubiquitinating enzyme 19) (Ubiquitin thioesterase 19) (Ubiquitin-specific-processing protease 19) 1360 150,549 Active site (2); Alternative sequence (2); Chain (1); Compositional bias (1); Domain (3); Erroneous initiation (1); Modified residue (1); Sequence conflict (5); Topological domain (2); Transmembrane (1); Zinc finger (1) TRANSMEM 1334 1354 Helical. {ECO:0000255}. TOPO_DOM 1 1333 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1355 1360 Lumenal. {ECO:0000255}. FUNCTION: Deubiquitinating enzyme that regulates the degradation of various proteins. Deubiquitinates and prevents proteasomal degradation of RNF123 which in turn stimulates CDKN1B ubiquitin-dependent degradation thereby playing a role in cell proliferation. Involved in decreased protein synthesis in atrophying skeletal muscle. Modulates transcription of major myofibrillar proteins. Also involved in turnover of endoplasmic-reticulum-associated degradation (ERAD) substrates (By similarity). Regulates the stability of BIRC2/c-IAP1 and BIRC3/c-IAP2 by preventing thier ubiquitination. Required for cells to mount an appropriate response to hypoxia and rescues HIF1A from degradation in a non-catalytic manner. Exhibits a preference towards 'Lys-63'-linked ubiquitin chains (By similarity). Plays an important role in 17 beta-estradiol (E2)-inhibited myogenesis. Decreases the levels of ubiquitinated proteins during skeletal muscle formation and acts to repress myogenesis. {ECO:0000250, ECO:0000269|PubMed:21971047}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with and stabilizes RNF123 (By similarity). Interacts with BIRC2/c-IAP1, BIRC3/c-IAP2 and XIAP/BIRC4. Interacts with HIF1A (via N-terminus) (By similarity). {ECO:0000250}. +Q5BKP2 UBP13_MOUSE Ubiquitin carboxyl-terminal hydrolase 13 (EC 3.4.19.12) (Deubiquitinating enzyme 13) (Ubiquitin thioesterase 13) (Ubiquitin-specific-processing protease 13) 858 96,723 Active site (2); Chain (1); Cross-link (2); Domain (3); Modified residue (1); Zinc finger (1) FUNCTION: Deubiquitinase that mediates deubiquitination of target proteins such as BECN1, MITF, SKP2 and USP10 and is involved in various processes such as autophagy and endoplasmic reticulum-associated degradation (ERAD). Component of a regulatory loop that controls autophagy and p53/TP53 levels: mediates deubiquitination of BECN1, a key regulator of autophagy, leading to stabilize the PIK3C3/VPS34-containing complexes. Also deubiquitinates USP10, an essential regulator of p53/TP53 stability. In turn, PIK3C3/VPS34-containing complexes regulate USP13 stability, suggesting the existence of a regulatory system by which PIK3C3/VPS34-containing complexes regulate p53/TP53 protein levels via USP10 and USP13. Recruited by nuclear UFD1 and mediates deubiquitination of SKP2, thereby regulating endoplasmic reticulum-associated degradation (ERAD). Also regulates ERAD through the deubiquitination of UBL4A a component of the BAG6/BAT3 complex. Mediates stabilization of SIAH2 independently of deubiquitinase activity: binds ubiquitinated SIAH2 and acts by impairing SIAH2 autoubiquitination. Has a weak deubiquitinase activity in vitro and preferentially cleaves 'Lys-63'-linked polyubiquitin chains. In contrast to USP5, it is not able to mediate unanchored polyubiquitin disassembly. Able to cleave ISG15 in vitro; however, additional experiments are required to confirm such data. {ECO:0000250|UniProtKB:Q92995}. SUBUNIT: Interacts with UFD1. Interacts (via UBA domains) with SIAH2 (when ubiquitinated). Interacts with BAG6; the interaction is direct and may mediate UBL4A deubiquitination. Interacts (via UBA 2 domain) with AMFR; the interaction is direct. Interacts with UBL4A; may be indirect via BAG6. {ECO:0000250|UniProtKB:Q92995}. DOMAIN: The UBP-type zinc finger has lost its ability to bind ubiquitin and USP13 is not activated by unanchored ubiquitin. {ECO:0000250}.; DOMAIN: The UBA domains mediate binding to ubiquitin. {ECO:0000250}. +Q99LG0 UBP16_MOUSE Ubiquitin carboxyl-terminal hydrolase 16 (EC 3.4.19.12) (Deubiquitinating enzyme 16) (Ubiquitin thioesterase 16) (Ubiquitin-specific-processing protease 16) 825 93,434 Active site (2); Chain (1); Cross-link (1); Domain (1); Metal binding (12); Modified residue (4); Sequence conflict (2); Zinc finger (1) FUNCTION: Specifically deubiquitinates 'Lys-120' of histone H2A (H2AK119Ub), a specific tag for epigenetic transcriptional repression, thereby acting as a coactivator. Deubiquitination of histone H2A is a prerequisite for subsequent phosphorylation at 'Ser-11' of histone H3 (H3S10ph), and is required for chromosome segregation when cells enter into mitosis. In resting B- and T-lymphocytes, phosphorylation by AURKB leads to enhance its activity, thereby maintaining transcription in resting lymphocytes (PubMed:24034696). Regulates Hox gene expression via histone H2A deubiquitination. Prefers nucleosomal substrates. Does not deubiquitinate histone H2B. {ECO:0000269|PubMed:24034696}. PTM: Phosphorylated at the onset of mitosis and dephosphorylated during the metaphase/anaphase transition. Phosphorylation by AURKB enhances the deubiquitinase activity. {ECO:0000255|HAMAP-Rule:MF_03062, ECO:0000269|PubMed:24034696}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03062}. SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_03062}. DOMAIN: The UBP-type zinc finger binds 3 zinc ions that form a pair of cross-braced ring fingers encapsulated within a third zinc finger in the primary structure. It recognizes the C-terminal tail of free ubiquitin. {ECO:0000255|HAMAP-Rule:MF_03062}. +P57080 UBP25_MOUSE Ubiquitin carboxyl-terminal hydrolase 25 (EC 3.4.19.12) (Deubiquitinating enzyme 25) (Ubiquitin thioesterase 25) (Ubiquitin-specific-processing protease 25) (mUSP25) 1055 121,420 Active site (2); Chain (1); Cross-link (2); Domain (4); Helix (4); Modified residue (2); Motif (1); Region (1); Sequence conflict (4) FUNCTION: Deubiquitinating enzyme that hydrolyzes ubiquitin moieties conjugated to substrates and thus, functions to process newly synthesized Ubiquitin, to recycle ubiquitin molecules or to edit polyubiquitin chains and prevents proteasomal degradation of substrates. Hydrolyzes both 'Lys-48'- and 'Lys-63'-linked tetraubiquitin chains (By similarity). {ECO:0000250}.; FUNCTION: The muscle-specific isoform (USP25m) may have a role in the regulation of muscular differentiation and function. PTM: Acetylated. {ECO:0000250}.; PTM: Sumoylation impairs binding to and hydrolysis of ubiquitin chains. Sumoylated preferentially with SUMO2 or SUMO3. Desumoylated by SENP1. Regulated by ubiquitination on the same residue (By similarity). {ECO:0000250}.; PTM: Preferentially monoubiquitinated but can also be polyubiquitinated. Autodeubiquitinated. Ubiquitination activates the enzymatic activity either by preventing sumoylation or by allowing novel interactions (By similarity). {ECO:0000250}.; PTM: Phosphorylation in the C-terminal by SYK regulates USP25 cellular levels. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16501887}. Nucleus {ECO:0000269|PubMed:16501887}. Note=The longer muscle-specific isoform (USP25m) Some transient punctuate nuclear location in myotubes during myocyte development. SUBUNIT: Homodimer or oligomer (By similarity). Interacts with ACTA1 (via its C-terminus); the interaction occurs for all isoforms but is strongest for isoform USP25m in muscle differentiating cells. Interacts (isoform USP25m only) with MYBPC1; the interaction prevents proteasomal degradation of MYBPC1. Interacts (isoform USP25m only) with FLNC (via filament repeats 17-18, 20-21 and 24). Interacts with GAPDH. Interacts with SUMO3; the interaction sumoylates efficiently USP25. Interacts with SUMO2; the interaction sumoylates efficiently USP25. Interacts with SUMO1; the interaction only weakly sumoylates USP25. Interacts with SYK; phosphorylates USP25 and regulates USP25 intracellular levels (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in testis especially in primary and secondary spematocytes and in immature spermatids. Also found in brain, skeletal muscle, liver and heart. {ECO:0000269|PubMed:10644437}. +Q9WTV6 UBP18_MOUSE Ubl carboxyl-terminal hydrolase 18 (EC 3.4.19.-) (43 kDa ISG15-specific protease) (ISG15-specific-processing protease) (Ubl thioesterase 18) 368 42,472 Active site (2); Beta strand (17); Chain (1); Domain (1); Helix (11); Sequence conflict (2); Turn (2) FUNCTION: Involved in the regulation of inflammatory response to interferon type 1. Can efficiently cleave only ISG15 fusions including native ISG15 conjugates linked via isopeptide bonds. Necessary to maintain a critical cellular balance of ISG15-conjugated proteins in both healthy and stressed organisms. {ECO:0000250|UniProtKB:Q9UMW8}. +Q6ZQ93 UBP34_MOUSE Ubiquitin carboxyl-terminal hydrolase 34 (EC 3.4.19.12) (Deubiquitinating enzyme 34) (Ubiquitin thioesterase 34) (Ubiquitin-specific-processing protease 34) 3582 408,214 Active site (2); Alternative sequence (4); Chain (1); Domain (1); Erroneous initiation (1); Modified residue (12); Sequence caution (1); Sequence conflict (1) FUNCTION: Ubiquitin hydrolase that can remove conjugated ubiquitin from AXIN1 and AXIN2, thereby acting as a regulator of Wnt signaling pathway. Acts as an activator of the Wnt signaling pathway downstream of the beta-catenin destruction complex by deubiquitinating and stabilizing AXIN1 and AXIN2, leading to promote nuclear accumulation of AXIN1 and AXIN2 and positively regulate beta-catenin (CTNBB1)-mediated transcription. Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins. {ECO:0000250|UniProtKB:Q70CQ2}. SUBUNIT: Interacts with AXIN1 and AXIN2. {ECO:0000250|UniProtKB:Q70CQ2}. +Q8C2S0 UBP44_MOUSE Ubiquitin carboxyl-terminal hydrolase 44 (EC 3.4.19.12) (Deubiquitinating enzyme 44) (Ubiquitin thioesterase 44) (Ubiquitin-specific-processing protease 44) 711 80,479 Active site (2); Chain (1); Domain (1); Sequence caution (2); Zinc finger (1) FUNCTION: Deubiquitinase that plays a key regulatory role in the spindle assembly checkpoint or mitotic checkpoint by preventing premature anaphase onset. Acts by specifically mediating deubiquitination of CDC20, a negative regulator of the anaphase promoting complex/cyclosome (APC/C). Deubiquitination of CDC20 leads to stabilize the MAD2L1-CDC20-APC/C ternary complex (also named mitotic checkpoint complex), thereby preventing premature activation of the APC/C. Promotes association of MAD2L1 with CDC20 and reinforces the spindle assembly checkpoint. Acts as a negative regulator of histone H2B (H2BK120ub1) ubiquitination. {ECO:0000269|PubMed:21853124}. PTM: Dephosphorylated by CTDP1. {ECO:0000250}.; PTM: Ubiquitinated; undergoes both 'Lys-48'- and 'Lys-63'-linked polyubiquitination and is degraded by the proteasome. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21853124}. Note=Peaks in interphase, with relatively low levels maintained throughout mitosis. TISSUE SPECIFICITY: Widely expressed. Highly expressed in lung, pancreas, skin, liver, stomach and intestine. {ECO:0000269|PubMed:20402667}. +B1AQJ2 UBP36_MOUSE Ubiquitin carboxyl-terminal hydrolase 36 (EC 3.4.19.12) (Deubiquitinating enzyme 36) (Ubiquitin thioesterase 36) (Ubiquitin-specific-processing protease 36) 1098 119,913 Active site (2); Chain (1); Domain (1); Erroneous initiation (1); Modified residue (7); Sequence conflict (3) FUNCTION: Deubiquitinase essential for the regulation of nucleolar structure and function. Required for cell and organism viability. Plays an important role in ribosomal RNA processing and protein synthesis, which is mediated, at least in part, through deubiquitination of DHX33, NPM1 and FBL, regulating their protein stability (PubMed:29273634). Function as a transcriptional repressor by deubiquiting histone H2B at the promoters of genes critical for cellular differentiation, such as CDKN1A, thereby preventing histone H3 'Lys-4' trimethylation (H3K4). Specifically deubiquitinates MYC in the nucleolus, leading to prevent MYC degradation by the proteasome: acts by specifically interacting with isoform 3 of FBXW7 (FBW7gamma) in the nucleolus and counteracting ubiquitination of MYC by the SCF(FBW7) complex. In contrast, it does not interact with isoform 1 of FBXW7 (FBW7alpha) in the nucleoplasm. Interacts to and regulates the actions of E3 ubiquitin-protein ligase NEDD4L over substrates such as NTRK1, KCNQ2 and KCNQ3, affecting their expression an functions. Deubiquitinates SOD2, regulates SOD2 protein stability. Deubiquitinase activity is required to control selective autophagy activation by ubiquitinated proteins (By similarity). {ECO:0000250|UniProtKB:Q9P275, ECO:0000269|PubMed:29273634}. PTM: Polyubiquitinated by NEDD4L, no effect on USP36 protein levels. Both proteins interact with and regulate each other's ubiquitination levels. {ECO:0000250|UniProtKB:Q9P275}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9P275}. Cytoplasm {ECO:0000250|UniProtKB:Q9P275}. SUBUNIT: Interacts with isoform 3 of FBXW7; the interaction inhibits MYC degradation induced by SCF(FBW7) complex. Interacts with NTRK1; USP36 does not deubiquitinate NTRK1. Interacts with NEDD4L (via domains WW1, 3 and 4); the interaction inhibits ubiquitination of, at least, NTRK1, KCNQ2 and KCNQ3 by NEDD4L. {ECO:0000250|UniProtKB:Q9P275}. +A2AN08 UBR4_MOUSE E3 ubiquitin-protein ligase UBR4 (EC 2.3.2.27) (N-recognin-4) (RING-type E3 ubiquitin transferase UBR4) (Zinc finger UBR1-type protein 1) (p600) 5180 572,290 Alternative sequence (6); Chain (1); Compositional bias (4); Erroneous initiation (1); Modified residue (20); Sequence conflict (1); Transmembrane (2); Zinc finger (1) TRANSMEM 329 349 Helical. {ECO:0000255}.; TRANSMEM 408 428 Helical. {ECO:0000255}. Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. Together with clathrin, forms meshwork structures involved in membrane morphogenesis and cytoskeletal organization. Regulates integrin-mediated signaling. May play a role in activation of FAK in response to cell-matrix interactions. Mediates ubiquitination of ACLY, leading to its subsequent degradation. {ECO:0000269|PubMed:16055722}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Nucleus {ECO:0000250}. Note=Concentrates at the leading edge of membrane structures involved in actin motility. {ECO:0000250}. SUBUNIT: Interacts with RB1 and calmodulin. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed in adult and embryonic stages with highest levels in testis and brain. {ECO:0000269|PubMed:16055722}. +Q8R317 UBQL1_MOUSE Ubiquilin-1 (Protein linking IAP with cytoskeleton 1) (PLIC-1) 582 61,976 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (6); Erroneous initiation (2); Initiator methionine (1); Modified residue (1); Region (1); Sequence caution (1); Sequence conflict (1) FUNCTION: Plays an important role in the regulation of different protein degradation mechanisms and pathways including ubiquitin-proteasome system (UPS), autophagy and endoplasmic reticulum-associated protein degradation (ERAD) pathway. Mediates the proteasomal targeting of misfolded or accumulated proteins for degradation by binding (via UBA domain) to their polyubiquitin chains and by interacting (via ubiquitin-like domain) with the subunits of the proteasome. Plays a role in the ERAD pathway via its interaction with ER-localized proteins UBXN4, VCP and HERPUD1 and may form a link between the polyubiquitinated ERAD substrates and the proteasome. Plays a role in unfolded protein response (UPR) by attenuating the induction of UPR-inducible genes, DDTI3/CHOP, HSPA5 and PDIA2 during ER stress. Involved in the regulation of macroautophagy and autophagosome formation; required for maturation of autophagy-related protein LC3 from the cytosolic form LC3-I to the membrane-bound form LC3-II and may assist in the maturation of autophagosomes to autolysosomes by mediating autophagosome-lysosome fusion. Negatively regulates the TICAM1/TRIF-dependent toll-like receptor signaling pathway by decreasing the abundance of TICAM1 via the autophagic pathway. Plays a key role in the regulation of the levels of PSEN1 by targeting its accumulation to aggresomes which may then be removed from cells by autophagocytosis. Promotes the ubiquitination and lysosomal degradation of ORAI1, consequently downregulating the ORAI1-mediated Ca2+ mobilization. Suppresses the maturation and proteasomal degradation of amyloid beta A4 protein (A4) by stimulating the lysine 63 (K63)-linked polyubiquitination. Delays the maturation of A4 by sequestering it in the Golgi apparatus and preventing its transport to the cell surface for subsequent processing (By similarity). Links CD47 to the cytoskeleton (PubMed:10549293). {ECO:0000250|UniProtKB:Q9JJP9, ECO:0000250|UniProtKB:Q9UMX0, ECO:0000269|PubMed:10549293}. PTM: Degraded during both macroautophagy and during chaperone-mediated autophagy (CMA). {ECO:0000250|UniProtKB:Q9UMX0}.; PTM: Phosphorylated. {ECO:0000250|UniProtKB:Q9UMX0}.; PTM: Ubiquitinated. {ECO:0000250|UniProtKB:Q9UMX0}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UMX0}. Cytoplasm {ECO:0000269|PubMed:10549293}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9UMX0}. Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:20529957}. Cell membrane {ECO:0000250|UniProtKB:Q9UMX0}. Note=Detected in neuronal processes and at synapses. Recruited to the ER during ER-associated protein degradation (ERAD). Colocalizes with PSEN1 in the cell membrane and in cytoplasmic juxtanuclear structures called aggresomes. Colocalizes with ORAI1 and TICAM1 in the autophagosome. Colocalizes with EPS15 and HGS in ubiquitin-rich cytoplasmic aggregates that are not endocytic compartments and with EPS15 also in aggresomes. {ECO:0000250|UniProtKB:Q9JJP9, ECO:0000250|UniProtKB:Q9UMX0}. SUBUNIT: Monomer and homodimer. Heterodimer with UBQLN2 (By similarity). Binds CD47 (PubMed:10549293). Binds NBL1, GABRA1, GABRA2, GABRA3, GABRA6, GABRB1, GABRB2 and GABRB3. Binds UBE3A, BTRC, P4HB and MTOR. Interacts with the proteasome 19S subunit. Interacts (via ubiquitin-like domain) with TREX1; the interaction is direct and may control TREX1 subcellular location. Forms a complex with UBXN4 and VCP. Interacts (via UBA domain) with UBQLN4 (via ubiquitin-like domain). Found in a complex with UBQLN2 and MAP1LC3A/B/C. The monomeric form interacts with PSEN1 and PSEN2. Interacts with ORAI1. Interacts (via UBA domain) with TICAM1. Interacts with EPS15. Interacts (via UBA domain) with UBA52 and (via ubiquitin-like domain) with PSMD3 and PSMD4. Interacts with HERPUD1. Interacts with MAP1LC3A/B/C in the presence of UBQLN4. Interacts (via ubiquitin-like domain) with EPS15 (via UIM domains) and both the ubiquitinated and non-ubiquitinated forms can interact with EPS15. Interacts (via ubiquitin-like domain) with EPS15L1, HGS (via UIM domain) and STAM2 (via UIM domain) (By similarity). {ECO:0000250|UniProtKB:Q9JJP9, ECO:0000250|UniProtKB:Q9UMX0, ECO:0000269|PubMed:10549293}. DOMAIN: The UBA domain mediates binding to PSEN1 and PSEN2. It also binds ubiquitin with micromolar affinity, independently of polyubiquitin linkage type. Essential for its association with microtubule-associated protein 1 light chain 3 (MAP1LC3). {ECO:0000250|UniProtKB:Q9UMX0}.; DOMAIN: The ubiquitin-like domain mediates its association with the subunits of the proteasome. {ECO:0000250|UniProtKB:Q9UMX0}.; DOMAIN: Dimerization is dependent upon the central region of the protein containing the STI1 domains and is independent of its ubiquitin-like and UBA domains. {ECO:0000250|UniProtKB:Q9UMX0}. TISSUE SPECIFICITY: Highly expressed in heart, brain, liver, smooth muscle and kidney. {ECO:0000269|PubMed:10549293}. +Q3V3E1 UBS3A_MOUSE Ubiquitin-associated and SH3 domain-containing protein A (Suppressor of T-cell receptor signaling 2) (STS-2) (T-cell ubiquitin ligand 1) (TULA-1) 624 70,145 Beta strand (7); Chain (1); Domain (2); Helix (15); Region (1); Sequence conflict (5); Turn (2) FUNCTION: Interferes with CBL-mediated down-regulation and degradation of receptor-type tyrosine kinases. Promotes accumulation of activated target receptors, such as T-cell receptors, EGFR and PDGFRB, on the cell surface. May inhibit dynamin-dependent endocytic pathways by functionally sequestering dynamin via its SH3 domain (By similarity). Exhibits negligigle protein tyrosine phosphatase activity at neutral pH. May act as a dominant-negative regulator of UBASH3B-dependent dephosphorylation. {ECO:0000250, ECO:0000269|PubMed:19196006}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Homodimer or homooligomer. Interacts with CBL. Part of a complex containing CBL and activated EGFR. Interacts with ubiquitin and with mono-ubiquitinated proteins. Interacts with dynamin (By similarity). {ECO:0000250}. +Q99PL6 UBXN6_MOUSE UBX domain-containing protein 6 (UBX domain-containing protein 1) 442 49,796 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (2); Frameshift (3); Modified residue (1); Region (2); Sequence conflict (2) FUNCTION: May negatively regulate the ATPase activity of VCP, an ATP-driven segregase that associates with different cofactors to control a wide variety of cellular processes. As a cofactor of VCP, it may play a role in the transport of CAV1 to lysosomes for degradation. It may also play a role in endoplasmic reticulum-associated degradation (ERAD) of misfolded proteins. Together with VCP and other cofactors, it may play a role in macroautophagy, regulating for instance the clearance of damaged lysosomes. {ECO:0000250|UniProtKB:Q9BZV1}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BZV1}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9BZV1}. Membrane {ECO:0000250|UniProtKB:Q9BZV1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9BZV1}. Nucleus {ECO:0000250|UniProtKB:Q9BZV1}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9BZV1}. Early endosome membrane {ECO:0000250|UniProtKB:Q9BZV1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9BZV1}. Late endosome membrane {ECO:0000250|UniProtKB:Q9BZV1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9BZV1}. Lysosome membrane {ECO:0000250|UniProtKB:Q9BZV1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9BZV1}. Note=Localizes at the centrosome both in interphase and during mitosis. May be recruited to endosomal and lysosomal membranes as part of a ternary complex with CAV1 and VCP. Recruited to damaged lysosomes decorated with K48-linked ubiquitin chains. {ECO:0000250|UniProtKB:Q9BZV1}. SUBUNIT: Interacts with VCP through the PUB domain (via C-terminus) and VIM motif (via N-terminus); the interaction is direct. Forms a ternary complex with CAV1 and VCP. Interacts with SYVN1. Interacts with HERPUD1. Interacts with VCPKMT. May interact with DERL1. Interacts with PLAA, VCP and YOD1; may form a complex involved in macroautophagy. Interacts with LMAN1. {ECO:0000250|UniProtKB:Q9BZV1}. DOMAIN: The UBX domain lacks key residues critical for VCP binding. {ECO:0000250|UniProtKB:Q9BZV1}. TISSUE SPECIFICITY: Widely expressed (at protein level). Highest expression in brain (at protein level). {ECO:0000269|PubMed:18656546}. +Q9QZM0 UBQL2_MOUSE Ubiquilin-2 (Chap1) (DSK2 homolog) (Protein linking IAP with cytoskeleton 2) (PLIC-2) (Ubiquitin-like product Chap1/Dsk2) 638 67,351 Chain (1); Compositional bias (3); Domain (6); Initiator methionine (1); Modified residue (2); Region (1); Repeat (11); Sequence conflict (2) FUNCTION: Plays an important role in the regulation of different protein degradation mechanisms and pathways including ubiquitin-proteasome system (UPS), autophagy and the endoplasmic reticulum-associated protein degradation (ERAD) pathway. Mediates the proteasomal targeting of misfolded or accumulated proteins for degradation by binding (via UBA domain) to their polyubiquitin chains and by interacting (via ubiquitin-like domain) with the subunits of the proteasome. Plays a role in the ERAD pathway via its interaction with ER-localized proteins FAF2/UBXD8 and HERPUD1 and may form a link between the polyubiquitinated ERAD substrates and the proteasome. Involved in the regulation of macroautophagy and autophagosome formation; required for maturation of autophagy-related protein LC3 from the cytosolic form LC3-I to the membrane-bound form LC3-II and may assist in the maturation of autophagosomes to autolysosomes by mediating autophagosome-lysosome fusion. Negatively regulates the endocytosis of GPCR receptors: AVPR2 and ADRB2, by specifically reducing the rate at which receptor-arrestin complexes concentrate in clathrin-coated pits (CCPs) (By similarity). Links CD47 to vimentin-containing intermediate filaments of the cytoskeleton (PubMed:10549293). {ECO:0000250|UniProtKB:Q9UHD9, ECO:0000269|PubMed:10549293}. PTM: Degraded during macroautophagy. {ECO:0000250|UniProtKB:Q9UHD9}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10549293}. Nucleus {ECO:0000269|PubMed:10549293}. Membrane {ECO:0000269|PubMed:10549293}. Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:Q9UHD9}. Note=Colocalizes with a subset of proteasomes, namely those that are cytoskeleton associated or free in the cytosol. Associated with fibers in mitotic cells. {ECO:0000250|UniProtKB:Q9UHD9}. SUBUNIT: Homodimer. Forms heterodimer with UBQLN1. Binds UBE3A and BTRC. Interacts with the 19S proteasome subunit. Interacts with C9orf72 (By similarity). Binds CD47 (PubMed:10549293). Interacts with HNRNPA1 and HNRNPU. Found in a complex with UBQLN1 and MAP1LC3A/B/C. Interacts with EPS15, EPN1 and EPN2. Interacts with HERPUD1. Interacts with RAD23A. Interacts with TARDBP. Interacts (via C-terminus) with FAF2 (via N-terminus). Interacts with UBQLN4 (By similarity). {ECO:0000250|UniProtKB:Q9UHD9, ECO:0000269|PubMed:10549293}. DOMAIN: The ubiquitin-like domain is essential for its inhibitory effect on GPCR endocytosis. Mediates its association with the subunits of the proteasome. {ECO:0000250|UniProtKB:Q9UHD9}.; DOMAIN: The UBA domain is essential for its association with microtubule-associated protein 1 light chain 3 (MAP1LC3). Mediates its association with ubiquitinated substrates. {ECO:0000250|UniProtKB:Q9UHD9}.; DOMAIN: Dimerization is dependent upon the central region of the protein containing the STI1 domains and is independent of its ubiquitin-like and UBA domains. {ECO:0000250|UniProtKB:Q9UHD9}. TISSUE SPECIFICITY: Highly expressed in smooth muscle. Expression in other tissues is very low. {ECO:0000269|PubMed:10549293}. +Q6PGH0 UBTD2_MOUSE Ubiquitin domain-containing protein 2 234 26,144 Chain (1); Domain (1); Sequence conflict (2) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +P58321 UCHL4_MOUSE Ubiquitin carboxyl-terminal hydrolase isozyme L4 (UCH-L4) (EC 3.4.19.12) (Ubiquitin thioesterase L4) 233 26,450 Active site (2); Chain (1); Modified residue (1); Region (2); Site (1) FUNCTION: Ubiquitin-protein hydrolase is involved both in the processing of ubiquitin precursors and of ubiquitinated proteins. This enzyme is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. TISSUE SPECIFICITY: Expressed in various tissues at low level. +Q63886 UD11_MOUSE UDP-glucuronosyltransferase 1-1 (UDPGT 1-1) (UGT1*1) (UGT1-01) (UGT1.1) (EC 2.4.1.17) (UDP-glucuronosyltransferase 1A1) (UGTBR1) 535 60,047 Chain (1); Glycosylation (3); Sequence conflict (3); Signal peptide (1); Transmembrane (1) TRANSMEM 493 509 Helical. {ECO:0000255}. FUNCTION: UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. SUBCELLULAR LOCATION: Microsome. Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. SUBUNIT: Part of a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX. TISSUE SPECIFICITY: Highly expressed in liver and at lower levels in colon, kidney, stomach and intestine. {ECO:0000269|PubMed:14672974}. +Q14BU0 UCMA_MOUSE Unique cartilage matrix-associated protein (Upper zone of growth plate and cartilage matrix associated protein) [Cleaved into: Unique cartilage matrix-associated protein C-terminal fragment (Ucma-C) (Gla-rich protein) (GRP)] 138 16,579 Alternative sequence (2); Chain (2); Coiled coil (1); Propeptide (1); Signal peptide (1) FUNCTION: May be involved in the negative control of osteogenic differentiation of osteochondrogenic precursor cells in peripheral zones of fetal cartilage and at the cartilage-bone interface. {ECO:0000269|PubMed:18156182}. PTM: Proteolytically cleaved by a furin-like convertase to generate a persistent C-terminal fragment found in almost the entire cartilage matrix, and affecting osteoblast differentiation.; PTM: Sulfated on one or two tyrosine residues within the tryptic peptide 121-135. {ECO:0000269|PubMed:18156182}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:18156182, ECO:0000269|PubMed:19819238}.; SUBCELLULAR LOCATION: Isoform 1: Secreted. Golgi apparatus.; SUBCELLULAR LOCATION: Isoform 3: Secreted. Golgi apparatus.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm, cytoskeleton {ECO:0000305}. Note=Colocalizes with aggresomes, which are aggregates of misfolded proteins, at the centrosome.; SUBCELLULAR LOCATION: Isoform 4: Cytoplasm, cytoskeleton {ECO:0000305}. Note=Colocalizes with aggresomes, which are aggregates of misfolded proteins, at the centrosome. TISSUE SPECIFICITY: Predominantly expressed in resting chondrocytes. {ECO:0000269|PubMed:18156182}. +Q64435 UD16_MOUSE UDP-glucuronosyltransferase 1-6 (UDPGT 1-6) (UGT1*6) (UGT1-06) (UGT1.6) (EC 2.4.1.17) (Phenol UDP-glucuronosyltransferase) (UDP-glucuronosyltransferase 1A6) (UGT1A6) (UGP1A1) (UGT1A7) 531 60,439 Chain (1); Glycosylation (2); Sequence conflict (10); Signal peptide (1); Transmembrane (1) TRANSMEM 489 505 Helical. {ECO:0000255}. FUNCTION: UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. Conjugates small planar phenolic molecules such as 4-nitrophenol, 1-naphthol, and 4-methylumbelliferone. The bulky phenol 4-hydroxybiphenyl, androgens and estrogens are not substrates. 2-hydroxybiphenyl is an excellent substrate. SUBCELLULAR LOCATION: Microsome. Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in liver, kidney and at very low levels in colon. {ECO:0000269|PubMed:14672974}. +P12242 UCP1_MOUSE Mitochondrial brown fat uncoupling protein 1 (UCP 1) (Solute carrier family 25 member 7) (Thermogenin) 307 33,248 Chain (1); Modified residue (1); Mutagenesis (7); Repeat (3); Topological domain (7); Transmembrane (6) TRANSMEM 11 32 Helical; Name=1. {ECO:0000255}.; TRANSMEM 74 96 Helical; Name=2. {ECO:0000255}.; TRANSMEM 117 133 Helical; Name=3. {ECO:0000255}.; TRANSMEM 179 195 Helical; Name=4. {ECO:0000255}.; TRANSMEM 213 232 Helical; Name=5. {ECO:0000255}.; TRANSMEM 267 289 Helical; Name=6. {ECO:0000255}. TOPO_DOM 1 10 Mitochondrial intermembrane. {ECO:0000250|UniProtKB:P04633}.; TOPO_DOM 33 73 Mitochondrial matrix. {ECO:0000250|UniProtKB:P04633}.; TOPO_DOM 97 116 Mitochondrial intermembrane. {ECO:0000250|UniProtKB:P04633}.; TOPO_DOM 134 178 Mitochondrial matrix. {ECO:0000250|UniProtKB:P04633}.; TOPO_DOM 196 212 Mitochondrial intermembrane. {ECO:0000250|UniProtKB:P04633}.; TOPO_DOM 233 266 Mitochondrial matrix. {ECO:0000250|UniProtKB:P04633}.; TOPO_DOM 290 307 Mitochondrial intermembrane. {ECO:0000250|UniProtKB:P04633}. FUNCTION: Mitochondrial protein responsible for thermogenic respiration, a specialized capacity of brown adipose tissue and beige fat that participates to non-shivering adaptive thermogenesis to temperature and diet variations and more generally to the regulation of energy balance (PubMed:9139827, PubMed:19187776, PubMed:23063128, PubMed:27027295). Functions as a long-chain fatty acid/LCFA and proton symporter, simultaneously transporting one LCFA and one proton through the inner mitochondrial membrane. However, LCFAs remaining associated with the transporter via their hydrophobic tails, it results in an apparent transport of protons activated by LCFAs. Thereby, dissipates the mitochondrial proton gradient and converts the energy of substrate oxydation into heat instead of ATP (PubMed:23063128). Regulates the production of reactive oxygen species/ROS by mitochondria (PubMed:20416274, PubMed:20466728). {ECO:0000269|PubMed:19187776, ECO:0000269|PubMed:20416274, ECO:0000269|PubMed:20466728, ECO:0000269|PubMed:23063128, ECO:0000269|PubMed:27027295, ECO:0000269|PubMed:9139827}. PTM: Sulfenylation at Cys-254 is increased upon cold exposure. It increases the sensitivity of UCP1 thermogenic function to the activation by noradrenaline probably through structural effects. {ECO:0000269|PubMed:27027295}.; PTM: May undergo ubiquitin-mediated proteasomal degradation. {ECO:0000250|UniProtKB:P04633}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:23063128}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P04633}. SUBUNIT: Most probably functions as a monomer. Binds one purine nucleotide per monomer. However, has also been suggested to function as a homodimer or a homotetramer. Tightly associates with cardiolipin in the mitochondrion inner membrane; may stabilize and regulate its activity. {ECO:0000250|UniProtKB:P25874, ECO:0000250|UniProtKB:W5PSH7}. TISSUE SPECIFICITY: Expressed in brown adipose tissue. {ECO:0000269|PubMed:8264627}. +P38639 UF01_MOUSE Unknown protein from 2D-PAGE of fibroblasts (P19) (Fragment) 5 717 Chain (1); Non-terminal residue (1) +P38642 UF04_MOUSE Unknown protein from 2D-PAGE of fibroblasts (P46) (Fragment) 7 766 Chain (1); Non-terminal residue (1) +P38643 UF05_MOUSE Unknown protein from 2D-PAGE of fibroblasts (P48) (Fragment) 11 1,330 Chain (1); Non-terminal residue (1) +P38644 UF06_MOUSE Unknown protein from 2D-PAGE of fibroblasts (P50) (Fragment) 8 817 Chain (1); Non-terminal residue (1) +Q91ZJ5 UGPA_MOUSE UTP--glucose-1-phosphate uridylyltransferase (EC 2.7.7.9) (UDP-glucose pyrophosphorylase) (UDPGP) (UGPase) 508 56,979 Active site (1); Alternative sequence (1); Binding site (6); Chain (1); Metal binding (2); Modified residue (6); Region (5) FUNCTION: Plays a central role as a glucosyl donor in cellular metabolic pathways. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homooctamer. {ECO:0000250}. +P97931 UNG_MOUSE Uracil-DNA glycosylase (UDG) (EC 3.2.2.27) 306 33,926 Active site (1); Alternative sequence (1); Chain (1); Modified residue (5); Sequence conflict (2) FUNCTION: Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. PTM: Isoform 1 is processed by cleavage of a transit peptide. SUBCELLULAR LOCATION: Isoform 1: Mitochondrion.; SUBCELLULAR LOCATION: Isoform 2: Nucleus. SUBUNIT: Monomer. Interacts with FAM72A. {ECO:0000255|HAMAP-Rule:MF_03166}. +P52624 UPP1_MOUSE Uridine phosphorylase 1 (UPase 1) (UrdPase 1) (EC 2.4.2.3) 311 34,086 Binding site (3); Chain (1); Region (1); Sequence conflict (1) Pyrimidine metabolism; UMP biosynthesis via salvage pathway; uracil from uridine (phosphorylase route): step 1/1. FUNCTION: Catalyzes the reversible phosphorylytic cleavage of uridine and deoxyuridine to uracil and ribose- or deoxyribose-1-phosphate (PubMed:7744869). The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis. {ECO:0000269|PubMed:7744869, ECO:0000305}. PTM: The N-terminus is blocked. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q16831}. +B2RX14 TUT4_MOUSE Terminal uridylyltransferase 4 (TUTase 4) (EC 2.7.7.52) (Zinc finger CCHC domain-containing protein 11) 1644 184,650 Binding site (3); Chain (1); Compositional bias (1); Domain (2); Erroneous gene model prediction (2); Metal binding (2); Modified residue (4); Mutagenesis (4); Region (4); Sequence conflict (4); Zinc finger (4) FUNCTION: Uridylyltransferase that mediates the terminal uridylation of mRNAs with short (less than 25 nucleotides) poly(A) tails, hence facilitating global mRNA decay (PubMed:28792939). Essential for both oocyte maturation and fertility. Through 3' terminal uridylation of mRNA, sculpts, with TUT7, the maternal transcriptome by eliminating transcripts during oocyte growth (PubMed:28792939). Involved in microRNA (miRNA)-induced gene silencing through uridylation of deadenylated miRNA targets. Also functions as an integral regulator of microRNA biogenesiS using 3 different uridylation mechanisms (By similarity). Acts as a suppressor of miRNA biogenesis by mediating the terminal uridylation of some miRNA precursors, including that of let-7 (pre-let-7), miR107, miR-143 and miR-200c. Uridylated miRNAs are not processed by Dicer and undergo degradation. Degradation of pre-let-7 contributes to the maintenance of embryonic stem (ES) cell pluripotency (By similarity). Also catalyzes the 3' uridylation of miR-26A, a miRNA that targets IL6 transcript. This abrogates the silencing of IL6 transcript, hence promoting cytokine expression (PubMed:19703396). In the absence of LIN28A, TUT7 and TUT4 monouridylate group II pre-miRNAs, which includes most of pre-let7 members, that shapes an optimal 3' end overhang for efficient processing (PubMed:28671666). Add oligo-U tails to truncated pre-miRNAS with a 5' overhang which may promote rapid degradation of non-functional pre-miRNA species (By similarity). May also suppress Toll-like receptor-induced NF-kappa-B activation via binding to T2BP (By similarity). Does not play a role in replication-dependent histone mRNA degradation (By similarity). Due to functional redundancy between TUT4 and TUT7, the identification of the specific role of each of these proteins is difficult (PubMed:28671666, PubMed:28792939, PubMed:22898984). TUT4 and TUT7 restrict retrotransposition of long interspersed element-1 (LINE-1) in cooperation with MOV10 counteracting the RNA chaperonne activity of L1RE1. TUT7 uridylates LINE-1 mRNAs in the cytoplasm which inhibits initiation of reverse transcription once in the nucleus, whereas uridylation by TUT4 destabilizes mRNAs in cytoplasmic ribonucleoprotein granules (By similarity). {ECO:0000250|UniProtKB:Q5TAX3, ECO:0000269|PubMed:19703396, ECO:0000269|PubMed:22898984, ECO:0000269|PubMed:28671666, ECO:0000269|PubMed:28792939}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5TAX3}. Cytoplasm {ECO:0000269|PubMed:19703396}. Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000250|UniProtKB:Q5TAX3}. Note=Mainly cytoplasmic (PubMed:19703396). Translocates into the cytoplasm following treatment of the cell with LPS. Co-enriched in cytoplasmic foci with MOV10. {ECO:0000250|UniProtKB:Q5TAX3, ECO:0000269|PubMed:19703396}. SUBUNIT: Interacts with LIN28A in the presence of pre-let-7 RNA (PubMed:28671666). Interacts with T2BP. Interacts with MOV10; the interaction is RNA-dependent. {ECO:0000250|UniProtKB:Q5TAX3}. DOMAIN: Utilizes two multidomain functional modules during the switch from monouridylation to oligouridylation. The catalytic module (containing the 3 CCHC-type Zinc finger domains) is essential for both activites while the Lin28-interacting module (LIM) at the N-termail part is indispensable for oligouridylation. {ECO:0000269|PubMed:28671666}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:19701194}. +P01734 TVB1_MOUSE T-cell receptor beta chain V region 3H.25 135 15,123 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (3); Signal peptide (1) +Q6P6J9 TXD15_MOUSE Thioredoxin domain-containing protein 15 344 38,146 Chain (1); Domain (1); Erroneous initiation (1); Glycosylation (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 306 326 Helical. {ECO:0000255}. TOPO_DOM 21 305 Extracellular. {ECO:0000255}.; TOPO_DOM 327 344 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q8BJ37 TYDP1_MOUSE Tyrosyl-DNA phosphodiesterase 1 (Tyr-DNA phosphodiesterase 1) (EC 3.1.4.-) (Protein expressed in male leptotene and zygotene spermatocytes 501) (MLZ-501) 609 68,689 Active site (2); Binding site (2); Chain (1); Erroneous initiation (1); Modified residue (5); Region (1); Sequence conflict (4); Site (1) FUNCTION: DNA repair enzyme that can remove a variety of covalent adducts from DNA through hydrolysis of a 3'-phosphodiester bond, giving rise to DNA with a free 3' phosphate. Catalyzes the hydrolysis of dead-end complexes between DNA and the topoisomerase I active site tyrosine residue. Hydrolyzes 3'-phosphoglycolates on protruding 3' ends on DNA double-strand breaks due to DNA damage by radiation and free radicals. Acts on blunt-ended double-strand DNA breaks and on single-stranded DNA. Has low 3'exonuclease activity and can remove a single nucleoside from the 3'end of DNA and RNA molecules with 3'hydroxyl groups. Has no exonuclease activity towards DNA or RNA with a 3'phosphate (By similarity). {ECO:0000250|UniProtKB:Q9NUW8, ECO:0000269|PubMed:17914460, ECO:0000269|PubMed:17948061}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20339383}. Cytoplasm {ECO:0000269|PubMed:17948061}. SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9NUW8}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:17948061, ECO:0000269|PubMed:20339383}. +Q8BJM7 TYW1_MOUSE S-adenosyl-L-methionine-dependent tRNA 4-demethylwyosine synthase (EC 4.1.3.44) (Radical S-adenosyl methionine and flavodoxin domain-containing protein 1) (tRNA wybutosine-synthesizing protein 1 homolog) (tRNA-yW-synthesizing protein) 721 81,599 Alternative sequence (2); Chain (1); Domain (1); Metal binding (3); Nucleotide binding (2); Sequence caution (1) tRNA modification; wybutosine-tRNA(Phe) biosynthesis. FUNCTION: Probable component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA. Catalyzes the condensation of N-methylguanine with 2 carbon atoms from pyruvate to form the tricyclic 4-demethylwyosine, an intermediate in wybutosine biosynthesis (By similarity). {ECO:0000250}. +P0CG49 UBB_MOUSE Polyubiquitin-B [Cleaved into: Ubiquitin] 305 34,369 Binding site (2); Chain (4); Cross-link (8); Domain (4); Modified residue (3); Propeptide (1); Sequence conflict (6); Site (1) FUNCTION: Ubiquitin: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling. {ECO:0000269|PubMed:19754430}. PTM: Ubiquitin: Phosphorylated at Ser-65 by PINK1 during mitophagy. Phosphorylated ubiquitin specifically binds and activates parkin (PRKN), triggering mitophagy. Phosphorylation does not affect E1-mediated E2 charging of ubiquitin but affects discharging of E2 enzymes to form polyubiquitin chains. It also affects deubiquitination by deubiquitinase enzymes such as USP30. {ECO:0000250|UniProtKB:P0CG47}.; PTM: Ubiquitin: Mono-ADP-ribosylated at the C-terminus by PARP9, a component of the PPAR9-DTX3L complex. ADP-ribosylation requires processing by E1 and E2 enzymes and prevents ubiquitin conjugation to substrates such as histones. {ECO:0000250|UniProtKB:P0CG47}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. +Q6P3B2 UBAD1_MOUSE UBA-like domain-containing protein 1 176 18,910 Chain (1); Compositional bias (1) +Q91W82 UB2E2_MOUSE Ubiquitin-conjugating enzyme E2 E2 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme E2) (Ubiquitin carrier protein E2) (Ubiquitin-protein ligase E2) 201 22,241 Active site (1); Chain (1); Initiator methionine (1); Modified residue (5) Protein modification; protein ubiquitination. FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'- and 'Lys-48'-, as well as 'Lys-63'-linked polyubiquitination. Catalyzes the ISGylation of influenza A virus NS1 protein. {ECO:0000250|UniProtKB:Q96LR5}. PTM: Autoubiquitinated. {ECO:0000250|UniProtKB:Q96LR5}. +Q8BL06 UBP54_MOUSE Inactive ubiquitin carboxyl-terminal hydrolase 54 (Inactive ubiquitin-specific peptidase 54) 1588 176,664 Alternative sequence (3); Chain (1); Coiled coil (1); Compositional bias (1); Domain (1); Erroneous initiation (3); Modified residue (5); Sequence conflict (6) FUNCTION: Has no peptidase activity. {ECO:0000250}. +Q5U430 UBR3_MOUSE E3 ubiquitin-protein ligase UBR3 (EC 2.3.2.27) (N-recognin-3) (RING-type E3 ubiquitin transferase UBR3) (Ubiquitin-protein ligase E3-alpha-3) (Ubiquitin-protein ligase E3-alpha-III) (Zinc finger protein 650) 1889 212,757 Alternative sequence (3); Chain (1); Coiled coil (1); Compositional bias (2); Modified residue (3); Sequence conflict (1); Transmembrane (3); Zinc finger (2) TRANSMEM 761 781 Helical. {ECO:0000255}.; TRANSMEM 919 939 Helical. {ECO:0000255}.; TRANSMEM 1807 1827 Helical. {ECO:0000255}. Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase which is a component of the N-end rule pathway (PubMed:17462990). Does not bind to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation (PubMed:17462990). May play a role in Shh signaling by mediating the ubiquitination of Kif7 (PubMed:27195754). May be important for MYH9 function in certain tissues, possibly by regulating the ubiquitination of MYH9 and consequently affecting its interaction with MYO7A (PubMed:27331610). {ECO:0000250|UniProtKB:Q6ZT12, ECO:0000269|PubMed:17462990, ECO:0000269|PubMed:27195754, ECO:0000269|PubMed:27331610}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Interacts with UBE2A and UBE2B. {ECO:0000269|PubMed:17462990}. TISSUE SPECIFICITY: Expressed in numerous cells of the smell, touch, vision, hearing and taste senses. Expressed in cells of the olfactory pathway, including the olfactory cell layer of the main olfactory epithelium (MOE), a mitral neuron cell layer of the olfactory bulb (OB), and a pyramidal cell layer of the piriform cortex of the olfactory cortex (OC). Expressed in the vomeronasal sensory epithelium of the vomeronasal organ (VNO) and the mitral cells of the accessory olfactory bulb. Expressed in tactile tissues, including the dorsal root ganglion, trigeminal ganglion and follicle-sinus complexes. Expressed in cells between hair follicle and sinus and also in the region of the rete ridge collar. Expressed in taste buds of the fungiform, circumvallate, and foliate papillae. Expressed in the spiral ganglion, the organ of Corti of the cochlea in the inner ear, in the sensory epithelium of macula and vestibular ganglion of the balancing system (at protein level). Expressed in the liver and skeletal muscle. {ECO:0000269|PubMed:17462990}. +Q80TP3 UBR5_MOUSE E3 ubiquitin-protein ligase UBR5 (EC 2.3.2.26) (E3 ubiquitin-protein ligase, HECT domain-containing 1) (HECT-type E3 ubiquitin transferase UBR5) (Hyperplastic discs protein homolog) 2792 308,352 Active site (1); Chain (1); Compositional bias (12); Domain (2); Initiator methionine (1); Modified residue (34); Sequence conflict (1); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Ubiquitinates acetylated PCK1. Also acts as a regulator of DNA damage response by acting as a suppressor of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of 'Lys-63'-linked histone H2A and H2AX at DNA damage sites, thereby acting as a guard against excessive spreading of ubiquitinated chromatin at damaged chromosomes (By similarity). Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. Involved in maturation and/or transcriptional regulation of mRNA by activating CDK9 by polyubiquitination. May play a role in control of cell cycle progression. May have tumor suppressor function. Plays an essential role in extraembryonic development. Regulates DNA topoisomerase II binding protein (TopBP1) for the DNA damage response. {ECO:0000250, ECO:0000269|PubMed:15282321, ECO:0000269|PubMed:16055722}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Binds TOPBP1. Associates with CDK9 and TFIIS/TCEA1 and forms a transcription regulatory complex made of CDK9, RNAP II, UBR5 and TFIIS/TCEA1 that can stimulate target gene transcription by recruiting their promoters. Associates with the E3 ligase complex containing DYRK2, EDD/UBR5, DDB1 and DCAF1 proteins (EDVP complex). Interacts directly with DYRK2. Interacts with PIH1D1. {ECO:0000250|UniProtKB:O95071}. +Q8VCH8 UBXN4_MOUSE UBX domain-containing protein 4 (Erasin) (UBX domain-containing protein 2) 506 56,472 Beta strand (6); Chain (1); Domain (1); Helix (2); Intramembrane (1); Modified residue (1); Region (1); Sequence conflict (2); Topological domain (2); Turn (1) INTRAMEM 412 432 {ECO:0000255}. TOPO_DOM 1 411 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 433 506 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in endoplasmic reticulum-associated protein degradation (ERAD). Acts as a platform to recruit both UBQLN1 and VCP to the ER during ERAD. {ECO:0000250|UniProtKB:Q92575}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q92575}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q92575}. Nucleus envelope {ECO:0000250|UniProtKB:Q92575}. Note=Both the N- and the C-terminus face the cytosol. Also found in the nucleus envelope contiguous to the ER. {ECO:0000250|UniProtKB:Q92575}. SUBUNIT: Directly interacts with VCP. Interacts with UBQLN1. Forms a complex with VCP and UBQLN1. {ECO:0000250|UniProtKB:Q92575}. DOMAIN: The UBX domain is required for interaction with VCP. {ECO:0000250|UniProtKB:Q92575}.; DOMAIN: The intramembrane domain also contains the signal for ER targeting. {ECO:0000250|UniProtKB:Q92575}. TISSUE SPECIFICITY: Expressed in many tissues, including brain, heart, kidney, liver, muscle and spleen (at protein level). {ECO:0000269|PubMed:16968747}. +Q9QZ49 UBXN8_MOUSE UBX domain-containing protein 8 (Reproduction 8 protein) (Rep-8 protein) (UBX domain-containing protein 6) 277 31,555 Beta strand (5); Chain (1); Domain (1); Helix (2); Topological domain (3); Transmembrane (2); Turn (1) TRANSMEM 2 22 Helical. {ECO:0000255}.; TRANSMEM 34 54 Helical. {ECO:0000255}. TOPO_DOM 1 1 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 23 33 Lumenal. {ECO:0000255}.; TOPO_DOM 55 277 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins, possibly by tethering VCP to the endoplasmic reticulum membrane. May play a role in reproduction (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with SYVN1 and VCP. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in gonads. In testis, expressed in post-meiotic round spermatids, while in ovaries it is expressed in granulosa cells. {ECO:0000269|PubMed:21949850}. +Q14DL0 UBQLN_MOUSE Ubiquilin-like protein 610 67,566 Chain (1); Domain (2); Helix (4); Sequence conflict (23) +Q9D572 UBX11_MOUSE UBX domain-containing protein 11 (Socius) (UBX domain-containing protein 5) 484 54,875 Alternative sequence (2); Chain (1); Coiled coil (1); Domain (2); Frameshift (2); Modified residue (2); Sequence conflict (1) FUNCTION: May be involved in the reorganization of actin cytoskeleton mediated by RND1, RND2 AND RND3. Promotes RHOA activation mediated by GNA12 and GNA13 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. SUBUNIT: Interacts with GNA12, GNA13, RND1, RND2 AND RND3. {ECO:0000250}. +Q99KJ0 UBX2A_MOUSE UBX domain-containing protein 2A (UBX domain-containing protein 4) 258 29,197 Chain (1); Domain (2) +Q9CR68 UCRI_MOUSE Cytochrome b-c1 complex subunit Rieske, mitochondrial (EC 1.10.2.2) (Complex III subunit 5) (Cytochrome b-c1 complex subunit 5) (Rieske iron-sulfur protein) (RISP) (Rieske protein UQCRFS1) (Ubiquinol-cytochrome c reductase iron-sulfur subunit) [Cleaved into: Cytochrome b-c1 complex subunit 9 (Su9) (Subunit 9) (8 kDa subunit 9) (Complex III subunit IX) (Cytochrome b-c1 complex subunit 11) (Ubiquinol-cytochrome c reductase 8 kDa protein)] 274 29,368 Chain (2); Disulfide bond (1); Domain (1); Metal binding (4); Transit peptide (1); Transmembrane (1) TRANSMEM 103 140 Helical. {ECO:0000250}. FUNCTION: Cytochrome b-c1 complex subunit Rieske, mitochondrial: Component of the mitochondrial ubiquinol-cytochrome c reductase complex dimer (complex III dimer), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis (PubMed:28673544). Incorporation of UQCRFS1 is the penultimate step in complex III assembly (By similarity). {ECO:0000250|UniProtKB:P47985, ECO:0000269|PubMed:28673544}.; FUNCTION: Cytochrome b-c1 complex subunit 9: Possible component of the mitochondrial ubiquinol-cytochrome c reductase complex dimer (complex III dimer), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis (PubMed:28673544). UQCRFS1 undergoes proteolytic processing once it is incorporated in the complex III dimer, including this fragment, called subunit 9, which corresponds to the transit peptide (PubMed:28673544). The proteolytic processing is necessary for the correct insertion of UQCRFS1 in the complex III dimer, but the persistence of UQCRFS1-derived fragments may prevent newly imported UQCRFS1 to be processed and assembled into complex III and is detrimental for the complex III structure and function (PubMed:28673544). It is therefore unsure whether the UQCRFS1 fragments, including this fragment, are structural subunits (PubMed:28673544). {ECO:0000269|PubMed:28673544}. PTM: Proteolytic processing is necessary for the correct insertion of UQCRFS1 in the complex III dimer (PubMed:28673544). Several fragments are generated during UQCRFS1 insertion, most probably due to the endogenous matrix-processing peptidase (MPP) activity (PubMed:28673544). The action of the protease is also necessary for the clearance of the UQCRFS1 fragments (PubMed:28673544). {ECO:0000269|PubMed:28673544}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q5ZLR5}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q5ZLR5}. SUBUNIT: Binds to the mitochondrial respiratory complex III dimer. The monomeric module of the mitochondrial respiratory complex III contains 11 subunits: 3 respiratory subunits involved in its catalytic activity (cytochrome b, cytochrome c1 and Rieske protein UQCRFS1), 2 core proteins (UQCRC1/QCR1 and UQCRC2/QCR2) and 6 low-molecular weight proteins (UQCRH/QCR6, UQCRB/QCR7, UQCRQ/QCR8, UQCR10/QCR9, UQCR11/QCR10 and subunit 9, the cleavage product of Rieske protein UQCRFS1) (By similarity). Incorporation of the Rieske protein UQCRFS1 is the penultimate step in complex III assembly (By similarity). Interacts with TTC19, which is involved in the clearance of UQCRFS1 fragments (PubMed:28673544). {ECO:0000250|UniProtKB:P13272, ECO:0000250|UniProtKB:P47985, ECO:0000269|PubMed:28673544}. +P52623 UCK1_MOUSE Uridine-cytidine kinase 1 (UCK 1) (EC 2.7.1.48) (Cytidine monophosphokinase 1) (Uridine monophosphokinase 1) 277 31,068 Binding site (7); Chain (1); Modified residue (1); Nucleotide binding (1) Pyrimidine metabolism; CTP biosynthesis via salvage pathway; CTP from cytidine: step 1/3. Pyrimidine metabolism; UMP biosynthesis via salvage pathway; UMP from uridine: step 1/1. FUNCTION: Phosphorylates uridine and cytidine to uridine monophosphate and cytidine monophosphate. Does not phosphorylate deoxyribonucleosides or purine ribonucleosides. Can use ATP or GTP as a phosphate donor. Can also phosphorylate cytidine and uridine nucleoside analogs such as 6-azauridine, 5-fluorouridine, 4-thiouridine, 5-bromouridine, N(4)-acetylcytidine, N(4)-benzoylcytidine, 5-fluorocytidine, 2-thiocytidine, 5-methylcytidine, and N(4)-anisoylcytidine (By similarity). {ECO:0000250}. +Q6PDD0 UD2A2_MOUSE UDP-glucuronosyltransferase 2A2 (UDPGT 2A2) (EC 2.4.1.17) 528 59,967 Chain (1); Glycosylation (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 495 515 Helical. {ECO:0000255}. TOPO_DOM 22 494 Extracellular. {ECO:0000255}.; TOPO_DOM 516 528 Cytoplasmic. {ECO:0000255}. FUNCTION: UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q8BWQ1 UD2A3_MOUSE UDP-glucuronosyltransferase 2A3 (UDPGT 2A3) (EC 2.4.1.17) 534 61,119 Chain (1); Glycosylation (2); Modified residue (1); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 494 514 Helical. {ECO:0000255}. TOPO_DOM 19 493 Extracellular. {ECO:0000255}.; TOPO_DOM 515 534 Cytoplasmic. {ECO:0000255}. FUNCTION: UDP-glucuronosyltransferases catalyze phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase water solubility and enhance excretion. They are of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Highly expressed in liver, with lower levels in duodenum and jejunum. {ECO:0000269|PubMed:17050650}. +P70406 UCP2_MOUSE Mitochondrial uncoupling protein 2 (UCP 2) (Solute carrier family 25 member 8) (UCPH) 309 33,374 Beta strand (2); Chain (1); Helix (16); Region (1); Repeat (3); Sequence conflict (1); Topological domain (7); Transmembrane (6); Turn (2) TRANSMEM 11 32 Helical; Name=1. {ECO:0000255}.; TRANSMEM 78 100 Helical; Name=2. {ECO:0000255}.; TRANSMEM 120 136 Helical; Name=3. {ECO:0000255}.; TRANSMEM 181 197 Helical; Name=4. {ECO:0000255}.; TRANSMEM 215 234 Helical; Name=5. {ECO:0000255}.; TRANSMEM 269 291 Helical; Name=6. {ECO:0000255}. TOPO_DOM 1 10 Mitochondrial matrix. {ECO:0000255}.; TOPO_DOM 33 77 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 101 119 Mitochondrial matrix. {ECO:0000255}.; TOPO_DOM 137 180 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 198 214 Mitochondrial matrix. {ECO:0000255}.; TOPO_DOM 235 268 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 292 309 Mitochondrial matrix. {ECO:0000255}. FUNCTION: UCP are mitochondrial transporter proteins that create proton leaks across the inner mitochondrial membrane, thus uncoupling oxidative phosphorylation from ATP synthesis. As a result, energy is dissipated in the form of heat (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:21785437}; Multi-pass membrane protein {ECO:0000269|PubMed:21785437}. SUBUNIT: Acts as a dimer forming a proton channel. {ECO:0000250}. TISSUE SPECIFICITY: Highest in white adipose tissue, also detected in brown adipose tissue, heart and kidney. 4-6 times higher levels are detected in ob/ob and db/db mice. +Q8JZZ0 UD3A2_MOUSE UDP-glucuronosyltransferase 3A2 (UDPGT 3A2) (EC 2.4.1.17) 523 59,673 Chain (1); Glycosylation (1); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 488 508 Helical. {ECO:0000255}. TOPO_DOM 23 487 Extracellular. {ECO:0000255}.; TOPO_DOM 509 523 Cytoplasmic. {ECO:0000255}. FUNCTION: UDP-glucuronosyltransferases catalyze phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase water solubility and enhance excretion. They are of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Highly expressed in kidney, while it is expressed at low levels in liver. Not detected in other tissues examined. {ECO:0000269|PubMed:17050650}. +P38640 UF02_MOUSE Unknown protein from 2D-PAGE of fibroblasts (P32) (Fragment) 9 1,103 Chain (1); Non-terminal residue (1) +P38641 UF03_MOUSE Unknown protein from 2D-PAGE of fibroblasts (P36) (Fragment) 7 842 Chain (1); Non-terminal residue (1) +P61961 UFM1_MOUSE Ubiquitin-fold modifier 1 85 9,118 Beta strand (5); Chain (1); Cross-link (2); Helix (2); Propeptide (1) FUNCTION: Ubiquitin-like modifier which can be covalently attached via an isopeptide bond to substrate proteins as a monomer or a lysine-linked polymer (PubMed:21494687). The so-called ufmylation, requires the UFM1-activating E1 enzyme UBA5, the UFM1-conjugating E2 enzyme UFC1, and the UFM1-ligase E3 enzyme UFL1. This post-translational modification on lysine residues of proteins may play a crucial role in a number of cellular processes. TRIP4 ufmylation may for instance play a role in nuclear receptors-mediated transcription (By similarity). Other substrates may include DDRGK1 with which it may play a role in the cellular response to endoplasmic reticulum stress (PubMed:21494687). {ECO:0000250|UniProtKB:P61960, ECO:0000269|PubMed:21494687}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21494687}. Cytoplasm {ECO:0000269|PubMed:21494687}. SUBUNIT: Interacts with UBA5. {ECO:0000250|UniProtKB:P61960}. TISSUE SPECIFICITY: Widely expressed with higher expression in secretory tissues (at protein level). {ECO:0000269|PubMed:21494687}. +A2RSJ4 UH1BL_MOUSE UHRF1-binding protein 1-like (Syntaxin-6 Habc-interacting protein of 164 kDa) 1457 161,940 Chain (1); Coiled coil (1); Erroneous initiation (1); Modified residue (5); Sequence conflict (9) SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:A0JNW5}. Early endosome {ECO:0000250|UniProtKB:A0JNW5}. Note=Primarily cytosolic. Recruited to early endosomes following STX6 overexpression. Overexpression of both STX6 and UHRF1BP1L results in aberrant tubulation of endosomal membranes. {ECO:0000250|UniProtKB:A0JNW5}. SUBUNIT: Homodimer (via N-terminus). Associates with the Golgi-associated retrograde protein (GARP) complex. Interacts with GARP complex component VPS52. Interacts (via C-terminal coiled-coil domain) with STX6. {ECO:0000250|UniProtKB:A0JNW5}. +P97343 UHMK1_MOUSE Serine/threonine-protein kinase Kist (EC 2.7.11.1) (Kinase interacting with stathmin) (PAM COOH-terminal interactor protein 2) (P-CIP2) (U2AF homology motif kinase 1) 419 46,489 Active site (1); Binding site (1); Chain (1); Domain (2); Nucleotide binding (1); Sequence conflict (3) FUNCTION: Upon serum stimulation, phosphorylates CDKN1B/p27Kip1, thus controlling CDKN1B subcellular location and cell cycle progression in G1 phase. May be involved in trafficking and/or processing of RNA (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12093740}. Note=Mostly nuclear. SUBUNIT: Interacts with PAM and CDKN1B/p27Kip1 (By similarity). Interacts with stathmin. {ECO:0000250, ECO:0000269|PubMed:12093740, ECO:0000269|PubMed:7724523}. +Q8VDF2 UHRF1_MOUSE E3 ubiquitin-protein ligase UHRF1 (EC 2.3.2.27) (Nuclear protein 95) (Nuclear zinc finger protein Np95) (RING-type E3 ubiquitin transferase UHRF1) (Ubiquitin-like PHD and RING finger domain-containing protein 1) (mUhrf1) (Ubiquitin-like-containing PHD and RING finger domains protein 1) 782 88,304 Alternative sequence (1); Beta strand (10); Binding site (4); Chain (1); Cross-link (3); Domain (2); Helix (5); Modified residue (14); Mutagenesis (2); Region (9); Sequence conflict (15); Site (3); Turn (4); Zinc finger (2) Protein modification; protein ubiquitination. FUNCTION: Multidomain protein that acts as a key epigenetic regulator by bridging DNA methylation and chromatin modification. Specifically recognizes and binds hemimethylated DNA at replication forks via its YDG domain and recruits DNMT1 methyltransferase to ensure faithful propagation of the DNA methylation patterns through DNA replication. In addition to its role in maintenance of DNA methylation, also plays a key role in chromatin modification: through its tudor-like regions and PHD-type zinc fingers, specifically recognizes and binds histone H3 trimethylated at 'Lys-9' (H3K9me3) and unmethylated at 'Arg-2' (H3R2me0), respectively, and recruits chromatin proteins. Enriched in pericentric heterochromatin where it recruits different chromatin modifiers required for this chromatin replication. Also localizes to euchromatic regions where it negatively regulates transcription possibly by impacting DNA methylation and histone modifications. Has E3 ubiquitin-protein ligase activity by mediating the ubiquitination of target proteins such as histone H3 and PML. It is still unclear how E3 ubiquitin-protein ligase activity is related to its role in chromatin in vivo. May be involved in DNA repair. {ECO:0000269|PubMed:12058012, ECO:0000269|PubMed:12084726, ECO:0000269|PubMed:14993289, ECO:0000269|PubMed:15361834, ECO:0000269|PubMed:17673620, ECO:0000269|PubMed:17994007, ECO:0000269|PubMed:21268065, ECO:0000269|PubMed:21489993}. PTM: Phosphorylation at Ser-303 of the linker region decreases the binding to H3K9me3. Phosphorylation at Ser-639 by CDK1 during M phase impairs interaction with USP7, preventing deubiquitination and leading to degradation by the proteasome (By similarity). {ECO:0000250}.; PTM: Ubiquitinated; which leads to proteasomal degradation. Autoubiquitinated; interaction with USP7 leads to deubiquitination and prevents degradation. Ubiquitination and degradation takes place during M phase, when phosphorylation at Ser-639 prevents intereaction with USP7 and subsequent deubiquitination. Polyubiquitination may be stimulated by DNA damage. {ECO:0000269|PubMed:21268065}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00358, ECO:0000269|PubMed:10984098, ECO:0000269|PubMed:11161719, ECO:0000269|PubMed:14993289, ECO:0000269|PubMed:17994007, ECO:0000269|PubMed:21489993, ECO:0000269|PubMed:8634372}. Note=Localizes to replication foci. Enriched in pericentric heterochromatin. Also localizes to euchromatic regions. SUBUNIT: Interacts with DNMT1; the interaction is direct. Interacts with USP7; leading to its deubiquitination. Interacts with HDAC1, but not with HDAC2. Interacts with UHRF1BP1. Interacts with PML. Interacts with EHMT2. Binds hemimethylated CpG containing oligonucleotides. Interacts with histones H3, H1 and H2B. Interacts with DNMT3A and DNMT3B (PubMed:14993289, PubMed:15361834, PubMed:17994007, PubMed:18772888, PubMed:18772891, PubMed:19056828, PubMed:19798101, PubMed:21268065). Interacts with PRAMEL7 (PubMed:28604677). {ECO:0000269|PubMed:14993289, ECO:0000269|PubMed:15361834, ECO:0000269|PubMed:17994007, ECO:0000269|PubMed:18772888, ECO:0000269|PubMed:18772891, ECO:0000269|PubMed:19056828, ECO:0000269|PubMed:19798101, ECO:0000269|PubMed:21268065, ECO:0000269|PubMed:28604677}. DOMAIN: The tudor-like regions specifically recognize and bind histone H3 unmethylated at 'Arg-2' (H3R2me0), while the PHD-type zinc finger specifically recognizes and binds histone H3 trimethylated at 'Lys-9' (H3K9me3). The tudor-like regions simultaneously recognizes H3K9me3 through a conserved aromatic cage in the first tudor-like subdomain and unmodified H3K4 (H3K4me0) within a groove between the tandem subdomains (PubMed:21489993). The linker region plays a role in the formation of a histone H3-binding hole between the reader modules formed by the tudor-like regions and the PHD-type zinc finger by making extended contacts with the tandem tudor-like regions. {ECO:0000269|PubMed:21489993}.; DOMAIN: The YDG domain (also named SRA domain) specifically recognizes and binds hemimethylated DNA at replication forks (DNA that is only methylated on the mother strand of replicating DNA) (PubMed:17994007). The YDG domain contains a binding pocket that accommodates the 5-methylcytosine that is flipped out of the duplex DNA. 2 specialized loops reach through the resulting gap in the DNA from both the major and the minor grooves to read the other 3 bases of the CpG duplex. The major groove loop confers both specificity for the CpG dinucleotide and discrimination against methylation of deoxycytidine of the complementary strand (PubMed:18772888). The YDG domain also recognizes and binds 5-hydroxymethylcytosine (5hmC). {ECO:0000269|PubMed:17994007, ECO:0000269|PubMed:18772888}.; DOMAIN: The RING finger is required for ubiquitin ligase activity. TISSUE SPECIFICITY: Expressed in thymus, testis, spleen and lung. Within testis, expressed in almost all cells except elongated spermatids. {ECO:0000269|PubMed:10984098, ECO:0000269|PubMed:9880673}. +P99032 ULAL_MOUSE Unknown protein from spot 2D-0014M9 of 2D-PAGE of liver tissue (Fragment) 12 1,327 Chain (1); Non-terminal residue (1) +O70405 ULK1_MOUSE Serine/threonine-protein kinase ULK1 (EC 2.7.11.1) (Serine/threonine-protein kinase Unc51.1) (Unc-51-like kinase 1) 1051 112,463 Active site (1); Binding site (1); Chain (1); Compositional bias (1); Domain (1); Modified residue (16); Mutagenesis (11); Nucleotide binding (1); Region (2); Sequence conflict (1) FUNCTION: Serine/threonine-protein kinase involved in autophagy in response to starvation. Acts upstream of phosphatidylinositol 3-kinase PIK3C3 to regulate the formation of autophagophores, the precursors of autophagosomes. Part of regulatory feedback loops in autophagy: acts both as a downstream effector and negative regulator of mammalian target of rapamycin complex 1 (mTORC1) via interaction with RPTOR. Activated via phosphorylation by AMPK and also acts as a regulator of AMPK by mediating phosphorylation of AMPK subunits PRKAA1, PRKAB2 and PRKAG1, leading to negatively regulate AMPK activity. May phosphorylate ATG13/KIAA0652 and RPTOR; however such data need additional evidences. Plays a role early in neuronal differentiation and is required for granule cell axon formation. May also phosphorylate SESN2 and SQSTM1 to regulate autophagy (PubMed:25040165). {ECO:0000269|PubMed:10624947, ECO:0000269|PubMed:19258318, ECO:0000269|PubMed:21205641, ECO:0000269|PubMed:21258367, ECO:0000269|PubMed:21460634, ECO:0000269|PubMed:25040165}. PTM: Autophosphorylated. Phosphorylated under nutrient-rich conditions; dephosphorylated during starvation or following treatment with rapamycin. In response to nutrient limitation, phosphorylated and activated by AMPK, leading to activate autophagy. Under nutrient sufficiency, phosphorylated by MTOR/mTOR, disrupting the interaction with AMPK and preventing activation of ULK1. {ECO:0000269|PubMed:19258318, ECO:0000269|PubMed:21205641, ECO:0000269|PubMed:21258367}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:19258318}. Preautophagosomal structure {ECO:0000269|PubMed:19258318}. Note=Under starvation conditions, is localized to puncate structures primarily representing the isolation membrane that sequesters a portion of the cytoplasm resulting in the formation of an autophagosome. SUBUNIT: Interacts with GABARAP and GABARAPL2 (By similarity). Interacts (via C-terminus) with ATG13 (PubMed:19258318). Part of a complex consisting of ATG13, ATG101, ULK1 and RB1CC1 (PubMed:19258318). Associates with the mammalian target of rapamycin complex 1 (mTORC1) through an interaction with RPTOR; the association depends on nutrient conditions and is reduced during starvation (By similarity). Interacts with FEZ1; SCOC interferes with FEZ1-binding (By similarity). Interacts with TBC1D14 (By similarity). Interacts (phosphorylated form) with TRIM5 (By similarity). When phosphorylated at Ser-317, interacts with MEFV and BECN1 simultaneously. Interacts with TRIM21 and IRF3, in the presence of TRIM21 (By similarity). Interacts with SESN2 (PubMed:25040165). Interacts with SQSTM1 (PubMed:25040165). Interacts with C9orf72 (By similarity). Interacts with WDR45 (By similarity). {ECO:0000250|UniProtKB:O75385, ECO:0000269|PubMed:19258318, ECO:0000269|PubMed:25040165}. +Q3U3Q1 ULK3_MOUSE Serine/threonine-protein kinase ULK3 (EC 2.7.11.1) (Unc-51-like kinase 3) 472 53,572 Active site (1); Alternative sequence (3); Binding site (1); Chain (1); Compositional bias (1); Domain (3); Erroneous initiation (1); Modified residue (4); Nucleotide binding (1); Sequence conflict (1) FUNCTION: Serine/threonine protein kinase that acts as a regulator of Sonic hedgehog (SHH) signaling and autophagy. Acts as a negative regulator of SHH signaling in the absence of SHH ligand: interacts with SUFU, thereby inactivating the protein kinase activity and preventing phosphorylation of GLI proteins (GLI1, GLI2 and/or GLI3). Positively regulates SHH signaling in the presence of SHH: dissociates from SUFU, autophosphorylates and mediates phosphorylation of GLI2, activating it and promoting its nuclear translocation. Phosphorylates in vitro GLI2, as well as GLI1 and GLI3, although less efficiently. Also acts as a regulator of autophagy: following cellular senescence, able to induce autophagy (By similarity). {ECO:0000250}. PTM: Autophosphorylated. Autophosphorylation is blocked by interaction with SUFU (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Localizes to pre-autophagosomal structure during cellular senescence. {ECO:0000250}. SUBUNIT: Interacts (via protein kinase domain) with SUFU. {ECO:0000250}. +Q3V129 ULK4_MOUSE Serine/threonine-protein kinase ULK4 (EC 2.7.11.1) (Unc-51-like kinase 4) 1303 145,342 Active site (1); Alternative sequence (9); Chain (1); Compositional bias (1); Domain (1); Repeat (7) FUNCTION: May be involved in the remodeling of cytoskeletal components, such as alpha-tubulin, and in this way regulates neurite branching and elongation, as well as cell motility. {ECO:0000250|UniProtKB:Q96C45}. TISSUE SPECIFICITY: Expressed in embryonic and adult brain. In the brain, widely expressed, with highest levels in layers II/III and V of the cortex, piriform cortex, CA1-3 of hippocampus, dentate gyrus, ependymal cells lining the ventricles and choroid plexus, and in the thalamic reticular nucleus (at protein level). {ECO:0000269|PubMed:24284070}. +Q9CQ85 TIM22_MOUSE Mitochondrial import inner membrane translocase subunit Tim22 194 20,114 Chain (1); Disulfide bond (2); Erroneous gene model prediction (1); Sequence conflict (1); Transmembrane (3) TRANSMEM 74 94 Helical. {ECO:0000255}.; TRANSMEM 123 143 Helical. {ECO:0000255}.; TRANSMEM 170 190 Helical. {ECO:0000255}. FUNCTION: Essential core component of the TIM22 complex, a complex that mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. In the TIM22 complex, it constitutes the voltage-activated and signal-gated channel. Forms a twin-pore translocase that uses the membrane potential as external driving force in 2 voltage-dependent steps (By similarity). {ECO:0000250|UniProtKB:Q12328}. PTM: Disulfide bonds promote efficient assembly of the TIM22 complex. {ECO:0000250|UniProtKB:Q9Y584}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9Y584}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Component of the TIM22 complex, whose core is composed of TIMM22, associated with peripheral protein FXC1/TIMM10B and the 70 kDa heterohexamer. In most cases, the 70 kDa complex is composed of TIMM9 and TIMM10 (TIMM10A or TIMM10B). A small fraction of the 70 kDa complex is composed of TIMM8 (TIMM8A/DDP1 or TIMM8B/DDP2) and TIMM13. The TIM22 complex also contains AGK and TIMM29. Interacts directly with TIMM9, TIMM10A and FXC1/TIMM10B. Interacts (when oxidized) with TIMM29; interaction is direct. {ECO:0000250|UniProtKB:Q9Y584}. +Q8R183 TIMD2_MOUSE T-cell immunoglobulin and mucin domain-containing protein 2 (TIMD-2) (T-cell immunoglobulin mucin receptor 2) (TIM-2) (T-cell membrane protein 2) 305 33,504 Beta strand (8); Chain (1); Compositional bias (1); Disulfide bond (3); Domain (1); Glycosylation (2); Helix (4); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 232 252 Helical. {ECO:0000255}. TOPO_DOM 22 231 Extracellular. {ECO:0000255}.; TOPO_DOM 253 305 Cytoplasmic. {ECO:0000255}. FUNCTION: Probable receptor for SEMA4A involved in the regulation of T-cell function. The interaction with SEMA4A enhances T-cell activation. {ECO:0000269|PubMed:12374982}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17363299}; Single-pass type I membrane protein {ECO:0000269|PubMed:17363299}. SUBUNIT: Homodimer. {ECO:0000269|PubMed:17363299}. +Q9D710 TMX2_MOUSE Thioredoxin-related transmembrane protein 2 (Thioredoxin domain-containing protein 14) 295 33,943 Chain (1); Domain (1); Modified residue (2); Motif (1); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 103 125 Helical. {ECO:0000255}. TOPO_DOM 49 102 Extracellular. {ECO:0000255}.; TOPO_DOM 126 295 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. DOMAIN: The thioredoxin domain lacks the 2 redox-active cysteines, suggesting that it lacks thioredoxin activity. {ECO:0000250}.; DOMAIN: The di-lysine motif confers endoplasmic reticulum localization for type I membrane proteins. {ECO:0000250}. +Q9D0N8 TMM88_MOUSE Transmembrane protein 88 159 17,358 Chain (1); Sequence conflict (1); Transmembrane (2) TRANSMEM 43 63 Helical. {ECO:0000255}.; TRANSMEM 88 108 Helical. {ECO:0000255}. FUNCTION: Inhibits the Wnt/beta-catenin signaling pathway. Crucial for heart development and acts downstream of GATA factors in the pre-cardiac mesoderm to specify lineage commitment of cardiomyocyte development (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein. SUBUNIT: Interacts (via C-terminus) with DVL1. {ECO:0000250}. +Q3UHK8 TNR6A_MOUSE Trinucleotide repeat-containing gene 6A protein 1896 203,150 Chain (1); Compositional bias (7); Domain (1); Modified residue (9); Region (10); Sequence conflict (1) FUNCTION: Plays a role in RNA-mediated gene silencing by both micro-RNAs (miRNAs) and short interfering RNAs (siRNAs) (PubMed:22187428). Required for miRNA-dependent repression of translation and for siRNA-dependent endonucleolytic cleavage of complementary mRNAs by argonaute family proteins (PubMed:22187428). As a scaffolding protein, associates with argonaute proteins bound to partially complementary mRNAs, and can simultaneously recruit CCR4-NOT and PAN deadenylase complexes (By similarity). {ECO:0000250|UniProtKB:Q8NDV7, ECO:0000269|PubMed:22187428}. SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000250|UniProtKB:Q8NDV7}. Note=Mammalian P-bodies are also known as GW bodies (GWBs). {ECO:0000250|UniProtKB:Q8NDV7}. SUBUNIT: Interacts with AGO2. Interacts with AGO1, AGO3 and AGO4. Interacts with CNOT1; the interaction is direct and mediates the association with the CCR4-NOT complex. Interacts with ZC3H12A. Interacts with SND1. {ECO:0000250|UniProtKB:Q8NDV7}. +Q9D2E2 TOE1_MOUSE Target of EGR1 protein 1 511 56,871 Alternative sequence (2); Chain (1); Initiator methionine (1); Modified residue (4); Motif (1); Sequence conflict (7); Zinc finger (1) FUNCTION: Inhibits cell growth rate and cell cycle. Induces CDKN1A expression as well as TGF-beta expression. Mediates the inhibitory growth effect of EGR1. Involved in the maturation of snRNAs and snRNA 3'-tail processing. {ECO:0000250|UniProtKB:Q96GM8}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q96GM8}. Nucleus speckle {ECO:0000250|UniProtKB:Q96GM8}. Note=Localizes to nuclear speckles. {ECO:0000250|UniProtKB:Q96GM8}. SUBUNIT: Interacts with U1, U2, U4, U5 and U6 snRNAs. {ECO:0000250|UniProtKB:Q96GM8}. +Q9JLL3 TNR19_MOUSE Tumor necrosis factor receptor superfamily member 19 (TRADE) (Toxicity and JNK inducer) 416 45,265 Alternative sequence (6); Chain (1); Disulfide bond (8); Glycosylation (1); Repeat (3); Sequence conflict (5); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 171 191 Helical. {ECO:0000255}. TOPO_DOM 30 170 Extracellular. {ECO:0000255}.; TOPO_DOM 192 416 Cytoplasmic. {ECO:0000255}. FUNCTION: Can mediate activation of c-Jun and NF-kappa-B. May promote caspase-independent cell death (By similarity). Isoform 2 and isoform 3 may act as decoy receptors. {ECO:0000250}. SUBCELLULAR LOCATION: Isoform 1: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: Isoform 3: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: Isoform 4: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: Isoform 2: Secreted {ECO:0000305}. SUBUNIT: Associates with TRAF1, TRAF2, TRAF3 and TRAF5. Interacts with LINGO1. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in adult brain, and in embryos from day 11-17, but not earlier. Detected in embryonic brain and epithelium, and at lower levels in adult heart, lung and liver. In neonatal mice, mainly in hair follicles and neuron-like cells in the cerebellum, but not in the skin epidermis. Isoform 3 was found in embryonic day 17.5 skin but not in brain and liver. +Q9ER38 TOR3A_MOUSE Torsin-3A (ATP-dependent interferon-responsive protein) (Torsin family 3 member A) 385 43,814 Chain (1); Glycosylation (1); Natural variant (1); Nucleotide binding (1); Sequence conflict (14); Signal peptide (1) PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Endoplasmic reticulum lumen {ECO:0000250}. SUBUNIT: Interacts with TOR1AIP1. {ECO:0000269|PubMed:16364897}. +Q9Z321 TOP3B_MOUSE DNA topoisomerase 3-beta-1 (EC 5.99.1.2) (DNA topoisomerase III beta-1) 862 96,949 Active site (1); Chain (1); Domain (1) FUNCTION: Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand than undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone (By similarity). Possesses negatively supercoiled DNA relaxing activity. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in testis. +O55060 TPMT_MOUSE Thiopurine S-methyltransferase (EC 2.1.1.67) (Thiopurine methyltransferase) 240 27,586 Beta strand (11); Binding site (4); Chain (1); Helix (10); Modified residue (2); Natural variant (1); Region (2); Turn (5) FUNCTION: Catalyzes the S-methylation of thiopurine drugs such as 6-mercaptopurine (also called mercaptopurine, 6-MP or its brand name Purinethol) using S-adenosyl-L-methionine as the methyl donor (PubMed:18484748). TPMT activity modulates the cytotoxic effects of thiopurine prodrugs. A natural substrate for this enzyme has yet to be identified. {ECO:0000269|PubMed:18484748, ECO:0000305}. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Monomer. {ECO:0000269|PubMed:18484748}. +Q9DBS2 TPRGL_MOUSE Tumor protein p63-regulated gene 1-like protein (Mossy fiber terminal-associated vertebrate-specific presynaptic protein) (Protein FAM79A) 266 29,814 Chain (1); Domain (1); Modified residue (3); Region (2) FUNCTION: Presynaptic protein involved in the synaptic transmission tuning. Regulates synaptic release probability by decreasing the calcium sensitivity of release. {ECO:0000250|UniProtKB:A8WCF8}. PTM: Phosphorylated. Phosphorylation promotes association with synaptic vesicle membranes. {ECO:0000250|UniProtKB:A8WCF8}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:A8WCF8}; Peripheral membrane protein {ECO:0000250|UniProtKB:A8WCF8}. Note=Localized to the active zone presynaptic nerve terminals. {ECO:0000250|UniProtKB:A8WCF8}. SUBUNIT: Forms homomultimers (By similarity). Multimerization appears to be important for presynaptic targeting (By similarity). Interacts with BSN (PubMed:17869247). {ECO:0000250|UniProtKB:A8WCF8, ECO:0000269|PubMed:17869247}. +Q7M723 TR104_MOUSE Taste receptor type 2 member 104 (T2R104) (mT2R45) 302 34,855 Chain (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 8 28 Helical; Name=1. {ECO:0000255}.; TRANSMEM 44 64 Helical; Name=2. {ECO:0000255}.; TRANSMEM 88 108 Helical; Name=3. {ECO:0000255}.; TRANSMEM 129 149 Helical; Name=4. {ECO:0000255}.; TRANSMEM 183 203 Helical; Name=5. {ECO:0000255}.; TRANSMEM 230 250 Helical; Name=6. {ECO:0000255}.; TRANSMEM 260 280 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 7 Extracellular. {ECO:0000255}.; TOPO_DOM 29 43 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 65 87 Extracellular. {ECO:0000255}.; TOPO_DOM 109 128 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 150 182 Extracellular. {ECO:0000255}.; TOPO_DOM 204 229 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 251 259 Extracellular. {ECO:0000255}.; TOPO_DOM 281 302 Cytoplasmic. {ECO:0000255}. FUNCTION: Putative taste receptor which may play a role in the perception of bitterness. {ECO:0000305}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q58Y74 TRCG1_MOUSE Taste receptor cell protein 1 (Taste receptor protein 1) 825 88,916 Alternative sequence (3); Chain (1); Compositional bias (2); Sequence conflict (2); Signal peptide (1) TISSUE SPECIFICITY: Expression is restricted to circumvallate papillae. {ECO:0000269|PubMed:15780750}. +Q9QZM4 TR10B_MOUSE Tumor necrosis factor receptor superfamily member 10B (Death receptor 5) (MK) (CD antigen CD262) 381 42,165 Chain (1); Disulfide bond (7); Domain (1); Repeat (3); Sequence conflict (10); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 181 201 Helical. {ECO:0000255}. TOPO_DOM 53 180 Extracellular. {ECO:0000255}.; TOPO_DOM 202 381 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for the cytotoxic ligand TNFSF10/TRAIL. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. Promotes the activation of NF-kappa-B. Essential for ER stress-induced apoptosis. {ECO:0000250|UniProtKB:O14763}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Monomer. Can interact with TRADD and RIPK1. Three TNFRSF10B molecules interact with the TNFSF10 homotrimer. {ECO:0000250|UniProtKB:O14763}. TISSUE SPECIFICITY: Highly expressed in heart, lung and kidney. +E9Q9K5 TRDN_MOUSE Triadin 693 77,844 Alternative sequence (7); Chain (1); Compositional bias (1); Disulfide bond (2); Glycosylation (2); Modified residue (1); Sequence conflict (3); Topological domain (2); Transmembrane (1) TRANSMEM 48 68 Helical. {ECO:0000255}. TOPO_DOM 1 47 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 69 693 Lumenal. {ECO:0000255}. FUNCTION: Contributes to the regulation of lumenal Ca2+ release via the sarcoplasmic reticulum calcium release channels RYR1 and RYR2, a key step in triggering skeletal and heart muscle contraction. Required for normal organization of the triad junction, where T-tubules and the sarcoplasmic reticulum terminal cisternae are in close contact. Required for normal skeletal muscle strength (PubMed:19843516). Plays a role in excitation-contraction coupling in the heart and in regulating the rate of heart beats. {ECO:0000269|PubMed:19383796, ECO:0000269|PubMed:19843516, ECO:0000269|PubMed:22768324}. PTM: Phosphorylated by CaMK2. {ECO:0000250|UniProtKB:Q28820}.; PTM: N-glycosylated. {ECO:0000269|PubMed:19383796}. SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:11707337}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q28820}. SUBUNIT: Homooligomer of variable subunit number; disulfide-linked. Interacts with CASQ1 and RYR1 in skeletal muscle. Interacts with CASQ2. {ECO:0000250|UniProtKB:Q13061, ECO:0000250|UniProtKB:Q28820}. TISSUE SPECIFICITY: Detected in heart (at protein level). Detected in heart. {ECO:0000269|PubMed:11707337, ECO:0000269|PubMed:19383796, ECO:0000269|PubMed:19843516}. +Q9R0M5 TPK1_MOUSE Thiamin pyrophosphokinase 1 (mTPK1) (EC 2.7.6.2) (Thiamine pyrophosphokinase 1) 243 27,068 Alternative sequence (3); Beta strand (18); Chain (1); Helix (8); Sequence conflict (1); Turn (1) Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine diphosphate from thiamine: step 1/1. FUNCTION: Catalyzes the phosphorylation of thiamine to thiamine pyrophosphate. Can also catalyze the phosphorylation of pyrithiamine to pyrithiamine pyrophosphate. {ECO:0000269|PubMed:10567383, ECO:0000269|PubMed:16365036}. SUBUNIT: Homodimer. {ECO:0000269|PubMed:10567383, ECO:0000269|PubMed:11419946, ECO:0000269|PubMed:16365036}. TISSUE SPECIFICITY: Detected in kidney and liver, and at lower levels in heart, brain and testis. {ECO:0000269|PubMed:10567383}. +Q61069 USF1_MOUSE Upstream stimulatory factor 1 (Major late transcription factor 1) 310 33,570 Chain (1); Cross-link (1); Domain (1); Region (1) FUNCTION: Transcription factor that binds to a symmetrical DNA sequence (E-boxes) (5'-CACGTG-3') that is found in a variety of viral and cellular promoters. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Efficient DNA binding requires dimerization with another bHLH protein. Binds DNA as a homodimer or a heterodimer (USF1/USF2). +Q8BUB6 UST_MOUSE Uronyl 2-sulfotransferase (EC 2.8.2.-) 407 47,730 Chain (1); Frameshift (1); Glycosylation (5); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 50 70 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 49 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 71 407 Lumenal. {ECO:0000255}. FUNCTION: Sulfotransferase that catalyzes the transfer of sulfate to the position 2 of uronyl residues. Has mainly activity toward iduronyl residues in dermatan sulfate, and weaker activity toward glucuronyl residues of chondroitin sulfate. Has no activity toward desulfated N-resulfated heparin (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. +Q8C7V3 UTP15_MOUSE U3 small nucleolar RNA-associated protein 15 homolog (Src-associated protein SAW) 528 59,375 Chain (1); Cross-link (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (1); Repeat (7); Sequence conflict (1) FUNCTION: Ribosome biogenesis factor. Involved in nucleolar processing of pre-18S ribosomal RNA. Required for optimal pre-ribosomal RNA transcription by RNA polymerase I. {ECO:0000250|UniProtKB:Q8TED0}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q8TED0}. Note=Found predominantly at the fibrillar center. {ECO:0000250|UniProtKB:Q8TED0}. SUBUNIT: Interacts directly with UTP4 and WDR43 (). May be a component of the proposed t-UTP subcomplex of the ribosomal small subunit (SSU) processome containing at least UTP4, WDR43, HEATR1, UTP15, WDR75. {ECO:0000250|UniProtKB:Q8TED0}. +Q9Z2C8 YBOX2_MOUSE Y-box-binding protein 2 (FRGY2 homolog) (Germ cell-specific Y-box-binding protein) 360 38,271 Alternative sequence (2); Chain (1); Compositional bias (2); Domain (1); Modified residue (3); Mutagenesis (2); Region (2); Sequence conflict (3) FUNCTION: Major constituent of messenger ribonucleoprotein particles (mRNPs). Involved in the regulation of the stability and/or translation of germ cell mRNAs. Binds to Y-box consensus promoter element. Binds to full-length mRNA with high affinity in a sequence-independent manner. Binds to short RNA sequences containing the consensus site 5'-UCCAUCA-3' with low affinity and limited sequence specificity. Its binding with maternal mRNAs is necessary for its cytoplasmic retention. May mark specific mRNAs (those transcribed from Y-box promoters) in the nucleus for cytoplasmic storage, thereby linking transcription and mRNA storage/translational delay. {ECO:0000269|PubMed:10076007, ECO:0000269|PubMed:12297523, ECO:0000269|PubMed:12648488, ECO:0000269|PubMed:15031116, ECO:0000269|PubMed:15665108}. PTM: Phosphorylated during oocyte maturation and dephosphorylated following egg activation. Phosphorylated in vitro by a kinase activity associated with testicular mRNPs. Dephosphorylation leads to a decrease in its affinity to bind RNA in vitro. {ECO:0000269|PubMed:10076007, ECO:0000269|PubMed:11566752}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11566752}. Nucleus {ECO:0000269|PubMed:11566752}. SUBUNIT: Found in a mRNP complex with PABPC1 and YBX3. {ECO:0000269|PubMed:10076007, ECO:0000269|PubMed:10772793}. TISSUE SPECIFICITY: Expressed in meiotic and postmeiotic male germ cells and oocytes; poorly expressed in two cell stage embryos (at protein level). Not detected in preimplantation embryos. {ECO:0000269|PubMed:11566752, ECO:0000269|PubMed:9780336}. +Q91XL3 UXS1_MOUSE UDP-glucuronic acid decarboxylase 1 (EC 4.1.1.35) (UDP-glucuronate decarboxylase 1) (UGD) (UXS-1) 420 47,553 Active site (1); Binding site (3); Chain (1); Glycosylation (1); Modified residue (2); Nucleotide binding (5); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 20 40 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 19 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 41 420 Lumenal. {ECO:0000255}. Nucleotide-sugar biosynthesis; UDP-alpha-D-xylose biosynthesis; UDP-alpha-D-xylose from UDP-alpha-D-glucuronate: step 1/1. FUNCTION: Catalyzes the NAD-dependent decarboxylation of UDP-glucuronic acid to UDP-xylose. Necessary for the biosynthesis of the core tetrasaccharide in glycosaminoglycan biosynthesis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. SUBUNIT: Interacts with AKT1. {ECO:0000250}. +Q9WTZ0 UXT_MOUSE Protein UXT (Ubiquitously expressed transcript protein) 157 18,187 Chain (1); Sequence conflict (1) FUNCTION: Involved in gene transcription regulation. Acts in concert with the corepressor URI1 to regulate androgen receptor AR-mediated transcription. Together with URI1, associates with chromatin to the NKX3-1 promoter region. Negatively regulates the transcriptional activity of the estrogen receptor ESR1 by inducing its translocation into the cytoplasm. May act as nuclear chaperone that facilitates the formation of the NF-kappa-B enhanceosome and thus positively regulates NF-kappa-B transcription activity. Potential component of mitochondrial-associated LRPPRC, a multidomain organizer that potentially integrates mitochondria and the microtubular cytoskeleton with chromosome remodeling. Increasing concentrations of UXT contributes to progressive aggregation of mitochondria and cell death potentially through its association with LRPPRC. Suppresses cell transformation and it might mediate this function by interaction and inhibition of the biological activity of cell proliferation and survival stimulatory factors like MECOM. {ECO:0000250|UniProtKB:Q9UBK9}.; FUNCTION: Isoform 1: Plays a role in protecting cells against TNF-alpha-induced apoptosis by preventing the recruitment of FADD and caspase 8 to the apoptotic complex I, composed of TRADD, TRAF2 and RIPK1/RIP. {ECO:0000269|PubMed:21307340}. SUBCELLULAR LOCATION: Isoform 1: Cytoplasm {ECO:0000250|UniProtKB:Q9UBK9}.; SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UBK9}. Nucleus {ECO:0000250|UniProtKB:Q9UBK9}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9UBK9}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q9UBK9}. Note=Predominantly localizes to the nucleus. Localizes to spindle pole during mitosis. {ECO:0000250|UniProtKB:Q9UBK9}. SUBUNIT: Homohexamer (By similarity). Interacts with LRPPRC (By similarity). Isoform 2 interacts with androgen receptor AR (via N-terminus) (By similarity). Interacts with estrogen receptor ESR1; the interaction relocalizes ESR1 to the cytoplasm (By similarity). In the nucleus, interacts specifically with RELA (via RHD domain) and forms a dynamic complex with NF-kappa-B and is recruited to the NF-kappa-B enhanceosome upon stimulation (By similarity). Interacts with MECOM (By similarity). Interacts with URI1 (By similarity). Isoform 1 is part of complex I composed of TNF-alpha receptor, TRADD, TRAF2 and RIPK1 (By similarity). Within the complex, interacts (via TPQE motif) with TRAF2; the interaction prevents the recruitment of FADD and CASP8/caspase 8 to complex I (PubMed:21307340). {ECO:0000250|UniProtKB:Q9UBK9, ECO:0000269|PubMed:21307340}. +Q8R2E6 V1A11_MOUSE Vomeronasal type-1 receptor A11 318 36,003 Chain (1); Disulfide bond (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 33 53 Helical; Name=1. {ECO:0000255}.; TRANSMEM 66 86 Helical; Name=2. {ECO:0000255}.; TRANSMEM 102 118 Helical; Name=3. {ECO:0000255}.; TRANSMEM 148 168 Helical; Name=4. {ECO:0000255}.; TRANSMEM 207 227 Helical; Name=5. {ECO:0000255}.; TRANSMEM 255 275 Helical; Name=6. {ECO:0000255}.; TRANSMEM 286 306 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 32 Extracellular. {ECO:0000255}.; TOPO_DOM 54 65 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 87 101 Extracellular. {ECO:0000255}.; TOPO_DOM 119 147 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 169 206 Extracellular. {ECO:0000255}.; TOPO_DOM 228 254 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 276 285 Extracellular. {ECO:0000255}.; TOPO_DOM 307 318 Cytoplasmic. {ECO:0000255}. FUNCTION: Putative pheromone receptor implicated in the regulation of social and reproductive behavior. {ECO:0000269|PubMed:12214233}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. +Q62463 V1AR_MOUSE Vasopressin V1a receptor (V1aR) (AVPR V1a) (Antidiuretic hormone receptor 1a) (Vascular/hepatic-type arginine vasopressin receptor) 423 47,182 Chain (1); Disulfide bond (1); Glycosylation (2); Lipidation (2); Modified residue (1); Natural variant (2); Topological domain (8); Transmembrane (7) TRANSMEM 53 76 Helical; Name=1. {ECO:0000255}.; TRANSMEM 89 110 Helical; Name=2. {ECO:0000255}.; TRANSMEM 126 147 Helical; Name=3. {ECO:0000255}.; TRANSMEM 169 190 Helical; Name=4. {ECO:0000255}.; TRANSMEM 221 241 Helical; Name=5. {ECO:0000255}.; TRANSMEM 299 318 Helical; Name=6. {ECO:0000255}.; TRANSMEM 337 356 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 52 Extracellular. {ECO:0000255}.; TOPO_DOM 77 88 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 111 125 Extracellular. {ECO:0000255}.; TOPO_DOM 148 168 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 191 220 Extracellular. {ECO:0000255}.; TOPO_DOM 242 298 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 319 336 Extracellular. {ECO:0000255}.; TOPO_DOM 357 423 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for arginine vasopressin. The activity of this receptor is mediated by G proteins which activate a phosphatidyl-inositol-calcium second messenger system. Involved in social memory formation. {ECO:0000269|PubMed:14647484}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q9WU02 V1BR_MOUSE Vasopressin V1b receptor (V1bR) (AVPR V1b) (AVPR V3) (Antidiuretic hormone receptor 1b) (Vasopressin V3 receptor) 421 46,539 Chain (1); Disulfide bond (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 36 59 Helical; Name=1. {ECO:0000255}.; TRANSMEM 72 93 Helical; Name=2. {ECO:0000255}.; TRANSMEM 109 130 Helical; Name=3. {ECO:0000255}.; TRANSMEM 152 173 Helical; Name=4. {ECO:0000255}.; TRANSMEM 203 223 Helical; Name=5. {ECO:0000255}.; TRANSMEM 281 300 Helical; Name=6. {ECO:0000255}.; TRANSMEM 319 338 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 35 Extracellular. {ECO:0000255}.; TOPO_DOM 60 71 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 94 108 Extracellular. {ECO:0000255}.; TOPO_DOM 131 151 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 174 202 Extracellular. {ECO:0000255}.; TOPO_DOM 224 280 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 301 318 Extracellular. {ECO:0000255}.; TOPO_DOM 339 421 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for arginine vasopressin. The activity of this receptor is mediated by G proteins which activate a phosphatidyl-inositol-calcium second messenger system. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q9EQ44 V1R41_MOUSE Vomeronasal type-1 receptor 41 (Vomeronasal type-1 receptor A12) (Vomeronasal type-1 receptor B9) 310 35,228 Chain (1); Disulfide bond (1); Erroneous initiation (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 21 41 Helical; Name=1. {ECO:0000255}.; TRANSMEM 50 70 Helical; Name=2. {ECO:0000255}.; TRANSMEM 94 114 Helical; Name=3. {ECO:0000255}.; TRANSMEM 135 155 Helical; Name=4. {ECO:0000255}.; TRANSMEM 191 211 Helical; Name=5. {ECO:0000255}.; TRANSMEM 239 259 Helical; Name=6. {ECO:0000255}.; TRANSMEM 270 290 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 20 Extracellular. {ECO:0000255}.; TOPO_DOM 42 49 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 71 93 Extracellular. {ECO:0000255}.; TOPO_DOM 115 134 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 156 190 Extracellular. {ECO:0000255}.; TOPO_DOM 212 238 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 260 269 Extracellular. {ECO:0000255}.; TOPO_DOM 291 310 Cytoplasmic. {ECO:0000255}. FUNCTION: Putative pheromone receptor implicated in the regulation of social and reproductive behavior. {ECO:0000269|PubMed:12214233}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. +Q8VIC9 V1R43_MOUSE Vomeronasal type-1 receptor 43 (Vomeronasal type-1 receptor A2) (Vomeronasal type-1 receptor A5) 329 37,649 Chain (1); Disulfide bond (1); Glycosylation (2); Topological domain (8); Transmembrane (7) TRANSMEM 33 53 Helical; Name=1. {ECO:0000255}.; TRANSMEM 66 86 Helical; Name=2. {ECO:0000255}.; TRANSMEM 110 130 Helical; Name=3. {ECO:0000255}.; TRANSMEM 148 168 Helical; Name=4. {ECO:0000255}.; TRANSMEM 210 230 Helical; Name=5. {ECO:0000255}.; TRANSMEM 256 276 Helical; Name=6. {ECO:0000255}.; TRANSMEM 286 306 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 32 Extracellular. {ECO:0000255}.; TOPO_DOM 54 65 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 87 109 Extracellular. {ECO:0000255}.; TOPO_DOM 131 147 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 169 209 Extracellular. {ECO:0000255}.; TOPO_DOM 231 255 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 277 285 Extracellular. {ECO:0000255}.; TOPO_DOM 307 329 Cytoplasmic. {ECO:0000255}. FUNCTION: Putative pheromone receptor implicated in the regulation of social and reproductive behavior. {ECO:0000269|PubMed:12214233}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. +Q9EQ47 V1R44_MOUSE Vomeronasal type-1 receptor 44 (Vomeronasal type-1 receptor A10) (Vomeronasal type-1 receptor B11) (Vomeronasal type-1 receptor B4) 310 35,388 Chain (1); Disulfide bond (1); Frameshift (1); Glycosylation (1); Sequence conflict (5); Topological domain (8); Transmembrane (7) TRANSMEM 21 41 Helical; Name=1. {ECO:0000255}.; TRANSMEM 51 71 Helical; Name=2. {ECO:0000255}.; TRANSMEM 94 114 Helical; Name=3. {ECO:0000255}.; TRANSMEM 132 152 Helical; Name=4. {ECO:0000255}.; TRANSMEM 191 211 Helical; Name=5. {ECO:0000255}.; TRANSMEM 239 259 Helical; Name=6. {ECO:0000255}.; TRANSMEM 269 289 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 20 Extracellular. {ECO:0000255}.; TOPO_DOM 42 50 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 72 93 Extracellular. {ECO:0000255}.; TOPO_DOM 115 131 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 153 190 Extracellular. {ECO:0000255}.; TOPO_DOM 212 238 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 260 268 Extracellular. {ECO:0000255}.; TOPO_DOM 290 310 Cytoplasmic. {ECO:0000255}. FUNCTION: Putative pheromone receptor implicated in the regulation of social and reproductive behavior. {ECO:0000269|PubMed:12214233}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. +O70410 V2R1_MOUSE Vomeronasal type-2 receptor 1 (Putative pheromone receptor V2R1) (V2Rx) 912 102,349 Chain (1); Glycosylation (4); Sequence conflict (2); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 624 644 Helical. {ECO:0000255}.; TRANSMEM 658 678 Helical. {ECO:0000255}.; TRANSMEM 692 712 Helical. {ECO:0000255}.; TRANSMEM 733 753 Helical. {ECO:0000255}.; TRANSMEM 779 799 Helical. {ECO:0000255}.; TRANSMEM 813 833 Helical. {ECO:0000255}.; TRANSMEM 841 861 Helical. {ECO:0000255}. TOPO_DOM 22 623 Extracellular. {ECO:0000255}.; TOPO_DOM 645 657 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 679 691 Extracellular. {ECO:0000255}.; TOPO_DOM 713 732 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 754 778 Extracellular. {ECO:0000255}.; TOPO_DOM 800 812 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 834 840 Extracellular. {ECO:0000255}.; TOPO_DOM 862 912 Cytoplasmic. {ECO:0000255}. FUNCTION: Putative pheromone receptor. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed at the sensory surface of the vomeronasal organ. {ECO:0000269|PubMed:11157070}. +Q6TAC4 V2R26_MOUSE Vomeronasal type-2 receptor 26 (Putative pheromone receptor V2R1b) (Vomeronasal type-2 receptor 1b) 855 96,200 Chain (1); Glycosylation (2); Sequence conflict (10); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 596 616 Helical. {ECO:0000255}.; TRANSMEM 631 651 Helical. {ECO:0000255}.; TRANSMEM 663 683 Helical. {ECO:0000255}.; TRANSMEM 707 727 Helical. {ECO:0000255}.; TRANSMEM 754 774 Helical. {ECO:0000255}.; TRANSMEM 787 807 Helical. {ECO:0000255}.; TRANSMEM 815 835 Helical. {ECO:0000255}. TOPO_DOM 23 595 Extracellular. {ECO:0000255}.; TOPO_DOM 617 630 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 652 662 Extracellular. {ECO:0000255}.; TOPO_DOM 684 706 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 728 753 Extracellular. {ECO:0000255}.; TOPO_DOM 775 786 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 808 814 Extracellular. {ECO:0000255}.; TOPO_DOM 836 855 Cytoplasmic. {ECO:0000255}. FUNCTION: Putative pheromone receptor. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in the basal epithelium of the vomeronasal organ. Located to vomeronasal sensory neurons that project their axons to six to ten glomeruli that reside in globally conserved areas within the caudal accessory olfactory bulb (AOB). {ECO:0000269|PubMed:12354396}. +O88721 V2R_MOUSE Vasopressin V2 receptor (V2R) (AVPR V2) (Antidiuretic hormone receptor) (Renal-type arginine vasopressin receptor) 371 40,645 Chain (1); Glycosylation (2); Lipidation (2); Topological domain (8); Transmembrane (7) TRANSMEM 39 63 Helical; Name=1. {ECO:0000255}.; TRANSMEM 78 98 Helical; Name=2. {ECO:0000255}.; TRANSMEM 114 135 Helical; Name=3. {ECO:0000255}.; TRANSMEM 160 180 Helical; Name=4. {ECO:0000255}.; TRANSMEM 201 220 Helical; Name=5. {ECO:0000255}.; TRANSMEM 272 293 Helical; Name=6. {ECO:0000255}.; TRANSMEM 309 328 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 38 Extracellular. {ECO:0000255}.; TOPO_DOM 64 77 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 99 113 Extracellular. {ECO:0000255}.; TOPO_DOM 136 159 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 181 200 Extracellular. {ECO:0000255}.; TOPO_DOM 221 271 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 294 308 Extracellular. {ECO:0000255}.; TOPO_DOM 329 371 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for arginine vasopressin. The activity of this receptor is mediated by G proteins which activate adenylate cyclase. Involved in renal water reabsorption (By similarity). {ECO:0000250|UniProtKB:P30518}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P30518}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P30518}. SUBUNIT: Interacts with ARRDC4. Identified in a complex containing at least ARRDC4, V2R and HGS. {ECO:0000250|UniProtKB:P30518}. +P63024 VAMP3_MOUSE Vesicle-associated membrane protein 3 (VAMP-3) (Cellubrevin) (CEB) (Synaptobrevin-3) 103 11,480 Chain (1); Domain (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 82 102 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 1 81 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 103 103 Vesicular. {ECO:0000255}. FUNCTION: SNARE involved in vesicular transport from the late endosomes to the trans-Golgi network. {ECO:0000250}. PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type X (BoNT/X) which hydrolyzes the 53-Arg-|-Ala-54 bond and probably inhibits neurotransmitter release (PubMed:28770820). It remains unknown whether BoNT/X is ever produced, or what organisms it targets. {ECO:0000269|PubMed:28770820}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}. Cell junction, synapse, synaptosome {ECO:0000250}. SUBUNIT: Interacts with BVES (via the C-terminus cytoplasmic tail). Interacts with BCAP31; involved in VAMP3 export from the endoplasmic reticulum. Interacts with BAIAP3; this interaction is increased in the presence of calcium (By similarity). {ECO:0000250|UniProtKB:Q15836, ECO:0000269|PubMed:20057356, ECO:0000269|PubMed:9396746}. +O70480 VAMP4_MOUSE Vesicle-associated membrane protein 4 (VAMP-4) 141 16,353 Beta strand (1); Chain (1); Domain (1); Helix (2); Modified residue (2); Sequence conflict (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 119 139 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 1 118 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 140 141 Vesicular. {ECO:0000255}. FUNCTION: Involved in the pathway that functions to remove an inhibitor (probably synaptotagmin-4) of calcium-triggered exocytosis during the maturation of secretory granules. May be a marker for this sorting pathway that is critical for remodeling the secretory response of granule (By similarity). {ECO:0000250}. PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type X (BoNT/X) which hydrolyzes the 87-Arg-|-Ser-88 bond and probably inhibits neurotransmitter release (PubMed:28770820). It remains unknown whether BoNT/X is ever produced, or what organisms it targets. {ECO:0000269|PubMed:28770820}. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}. Note=Associated with trans Golgi network (TGN) and newly formed immature secretory granules (ISG). Not found on the mature secretory organelles (By similarity). {ECO:0000250}. SUBUNIT: Identified in a complex containing STX6, STX12, VAMP4 and VTI1A (PubMed:17159904). Interacts with BAIAP3; this interaction is increased in the presence of calcium (By similarity). {ECO:0000250|UniProtKB:O75379, ECO:0000269|PubMed:17159904}. +Q62442 VAMP1_MOUSE Vesicle-associated membrane protein 1 (VAMP-1) (Synaptobrevin-1) 118 12,890 Alternative sequence (1); Chain (1); Domain (1); Modified residue (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 97 116 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 1 96 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 117 118 Vesicular. {ECO:0000255}. FUNCTION: Involved in the targeting and/or fusion of transport vesicles to their target membrane. PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type X (BoNT/X) which hydrolyzes the 68-Arg-|-Ala-69 bond and probably inhibits neurotransmitter release (PubMed:28770820). It remains unknown whether BoNT/X is ever produced, or what organisms it targets. {ECO:0000269|PubMed:28770820}. SUBCELLULAR LOCATION: Isoform 1: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Cell junction, synapse, synaptosome {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasmic vesicle membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Cell junction, synapse, synaptosome {ECO:0000250}. SUBUNIT: Interacts with VAPA and VAPB. {ECO:0000250}. +P29533 VCAM1_MOUSE Vascular cell adhesion protein 1 (V-CAM 1) (VCAM-1) (CD antigen CD106) 739 81,317 Alternative sequence (2); Chain (1); Disulfide bond (6); Domain (7); Glycosylation (5); Lipidation (1); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 699 720 Helical. {ECO:0000255}. TOPO_DOM 25 698 Extracellular. {ECO:0000255}.; TOPO_DOM 721 739 Cytoplasmic. {ECO:0000255}. FUNCTION: Important in cell-cell recognition. Appears to function in leukocyte-endothelial cell adhesion. Interacts with integrin alpha-4/beta-1 (ITGA4/ITGB1) on leukocytes, and mediates both adhesion and signal transduction. The VCAM1/ITGA4/ITGB1 interaction may play a pathophysiologic role both in immune responses and in leukocyte emigration to sites of inflammation. SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Isoform 2: Cell membrane; Lipid-anchor, GPI-anchor. SUBUNIT: (Microbial infection) Interacts with ECMV-D capsid proteins and acts as a receptor for this virus. {ECO:0000269|PubMed:7514674}. TISSUE SPECIFICITY: Expressed on inflamed vascular endothelium, as well as on macrophage-like and dendritic cell types in both normal and inflamed tissue. Expressed in the bone marrow. {ECO:0000269|PubMed:1713592}. +B7ZWI3 TMM92_MOUSE Transmembrane protein 92 162 18,079 Alternative sequence (1); Chain (1); Compositional bias (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 64 84 Helical. {ECO:0000255}. TOPO_DOM 23 63 Extracellular. {ECO:0000255}.; TOPO_DOM 85 162 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q8BRH0 TMTC3_MOUSE Protein O-mannosyl-transferase TMTC3 (EC 2.4.1.109) (Transmembrane and TPR repeat-containing protein 3) 920 104,198 Alternative sequence (2); Chain (1); Glycosylation (1); Modified residue (1); Repeat (10); Sequence conflict (1); Transmembrane (9) TRANSMEM 15 35 Helical. {ECO:0000255}.; TRANSMEM 95 115 Helical. {ECO:0000255}.; TRANSMEM 141 163 Helical. {ECO:0000255}.; TRANSMEM 172 192 Helical. {ECO:0000255}.; TRANSMEM 199 219 Helical. {ECO:0000255}.; TRANSMEM 237 257 Helical. {ECO:0000255}.; TRANSMEM 326 346 Helical. {ECO:0000255}.; TRANSMEM 359 379 Helical. {ECO:0000255}.; TRANSMEM 382 402 Helical. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Transfers mannosyl residues to the hydroxyl group of serine or threonine residues. The 4 members of the TMTC family are O-mannosyl-transferases dedicated primarily to the cadherin superfamily, each member seems to have a distinct role in decorating the cadherin domains with O-linked mannose glycans at specific regions. Also acts as O-mannosyl-transferase on other proteins such as PDIA3. Involved in the positive regulation of proteasomal protein degradation in the endoplasmic reticulum (ER), and the control of ER stress response. {ECO:0000250|UniProtKB:Q6ZXV5}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q6ZXV5}. +Q8BGN6 TMG4_MOUSE Transmembrane gamma-carboxyglutamic acid protein 4 (Proline-rich gamma-carboxyglutamic acid protein 4) (Proline-rich Gla protein 4) 226 25,401 Chain (1); Compositional bias (1); Disulfide bond (1); Domain (1); Modified residue (9); Propeptide (1); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 114 134 Helical. {ECO:0000255}. TOPO_DOM 50 113 Extracellular. {ECO:0000255}.; TOPO_DOM 135 226 Cytoplasmic. {ECO:0000255}. FUNCTION: May control axon guidance across the CNS (By similarity). Prevents the delivery of ROBO1 at the cell surface and downregulates its expression (By similarity). {ECO:0000250|UniProtKB:Q9BZD6}. PTM: Gla residues are produced after subsequent post-translational modifications of glutamate by a vitamin K-dependent gamma-carboxylase. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q9BZD6}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9BZD6}. +Q3V209 TMUB2_MOUSE Transmembrane and ubiquitin-like domain-containing protein 2 319 33,808 Alternative sequence (1); Beta strand (6); Chain (1); Domain (1); Erroneous initiation (1); Frameshift (1); Helix (1); Sequence conflict (3); Transmembrane (3); Turn (3) TRANSMEM 36 56 Helical. {ECO:0000255}.; TRANSMEM 264 284 Helical. {ECO:0000255}.; TRANSMEM 298 318 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q921N7 TMM70_MOUSE Transmembrane protein 70, mitochondrial 253 28,275 Chain (1); Frameshift (1); Sequence conflict (7); Transit peptide (1); Transmembrane (2) TRANSMEM 100 120 Helical. {ECO:0000255}.; TRANSMEM 136 156 Helical. {ECO:0000255}. FUNCTION: Involved in biogenesis of mitochondrial ATP synthase. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q149F5 TMM71_MOUSE Transmembrane protein 71 287 31,871 Chain (1); Sequence conflict (2); Transmembrane (2) TRANSMEM 218 238 Helical. {ECO:0000255}.; TRANSMEM 244 264 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +P0DJF3 TMM95_MOUSE Transmembrane protein 95 176 20,158 Chain (1); Glycosylation (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 147 167 Helical. {ECO:0000255}. TOPO_DOM 17 146 Extracellular. {ECO:0000255}.; TOPO_DOM 168 176 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q9D3H0 TMM80_MOUSE Transmembrane protein 80 123 13,473 Alternative sequence (1); Chain (1); Transmembrane (4) TRANSMEM 2 22 Helical. {ECO:0000255}.; TRANSMEM 35 55 Helical. {ECO:0000255}.; TRANSMEM 68 88 Helical. {ECO:0000255}.; TRANSMEM 102 122 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cell projection, cilium {ECO:0000269|PubMed:26982032}. Note=Localizes at the transition zone, a region between the basal body and the ciliary axoneme. {ECO:0000269|PubMed:26982032}. +P50284 TNR3_MOUSE Tumor necrosis factor receptor superfamily member 3 (Lymphotoxin-beta receptor) 415 44,956 Chain (1); Disulfide bond (10); Glycosylation (2); Modified residue (1); Repeat (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 224 244 Helical. {ECO:0000255}. TOPO_DOM 31 223 Extracellular. {ECO:0000255}.; TOPO_DOM 245 415 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for the heterotrimeric lymphotoxin containing LTA and LTB, and for TNFS14/LIGHT. Promotes apoptosis via TRAF3 and TRAF5. May play a role in the development of lymphoid organs (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Self-associates (By similarity). Associates with TRAF5. Associates with TRAF3 and TRAF4 (By similarity). {ECO:0000250}. +B9EKI3 TMF1_MOUSE TATA element modulatory factor (TMF) (Androgen receptor coactivator 160 kDa protein) (Androgen receptor-associated protein of 160 kDa) 1091 121,803 Chain (1); Coiled coil (3); Compositional bias (2); Frameshift (1); Modified residue (17); Region (1); Sequence conflict (6) FUNCTION: Potential coactivator of the androgen receptor. May play critical roles in two RAB6-dependent retrograde transport processes: one from endosomes to the Golgi and the other from the Golgi to the ER (By similarity). Mediates STAT3 degradation. {ECO:0000250, ECO:0000269|PubMed:15467733}. PTM: Phosphorylated by FER. {ECO:0000269|PubMed:9742951}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}. Note=Concentrated at the budding structures localized at the tips of cisternae. {ECO:0000250}. SUBUNIT: Component of the SNF/SWI transcription factor complexes (By similarity). Interacts with RAB6A. Interacts with TCEB1 (By similarity). Interacts with STAT3 and FER. Interacts with TRNP1; may regulate TRNP1 proteasomal degradation. {ECO:0000250, ECO:0000269|PubMed:15467733, ECO:0000269|PubMed:16792503}. DOMAIN: The Elongin BC complex binding domain is also known as BC-box with the consensus [APST]-L-x(3)-C-x(3)-[AILV]. +O35305 TNR11_MOUSE Tumor necrosis factor receptor superfamily member 11A (Osteoclast differentiation factor receptor) (ODFR) (Receptor activator of NF-KB) (CD antigen CD265) 625 66,621 Beta strand (19); Chain (1); Disulfide bond (10); Glycosylation (2); Helix (2); Metal binding (5); Modified residue (1); Repeat (4); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (2) TRANSMEM 215 234 Helical. {ECO:0000255}. TOPO_DOM 31 214 Extracellular. {ECO:0000255}.; TOPO_DOM 235 625 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for TNFSF11/RANKL/TRANCE/OPGL; essential for RANKL-mediated osteoclastogenesis. Involved in the regulation of interactions between T-cells and dendritic cells. {ECO:0000269|PubMed:20483727, ECO:0000269|PubMed:9878548}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Binds to the clefts between the subunits of the TNFSF11 ligand trimer to form a heterohexamer. Interacts with TRAF1, TRAF2, TRAF3, TRAF5 and TRAF6 (By similarity). Interacts (via cytoplasmic domain) with GAB2 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous expression with high levels in trabecular bone, thymus, small intestine, lung, brain and kidney. Weakly expressed in spleen and bone marrow. +Q8C3S2 TNG6_MOUSE Transport and Golgi organization protein 6 homolog (Transmembrane and coiled-coil domain-containing protein 7) 1079 118,732 Alternative sequence (3); Chain (1); Modified residue (1); Repeat (2); Sequence conflict (4); Transmembrane (1) TRANSMEM 473 493 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q8BYU6 TOIP2_MOUSE Torsin-1A-interacting protein 2 502 54,496 Chain (1); Glycosylation (1); Modified residue (5); Region (1); Sequence conflict (3); Topological domain (2); Transmembrane (1) TRANSMEM 247 267 Helical. {ECO:0000255}. TOPO_DOM 1 246 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 268 502 Lumenal. {ECO:0000255}. FUNCTION: Required for endoplasmic reticulum integrity. Regulates the distribution of TOR1A between the endoplasmic reticulum and the nuclear envelope as well as induces TOR1A, TOR1B and TOR3A ATPase activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Nucleus envelope {ECO:0000250}. SUBUNIT: Interacts with TOR1A and TOR1B (ATP-bound). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the spinal cord and liver (at protein level). {ECO:0000269|PubMed:16364897}. +Q9JKK7 TMOD2_MOUSE Tropomodulin-2 (Neuronal tropomodulin) (N-Tmod) 351 39,511 Alternative sequence (3); Chain (1); Modified residue (1); Sequence conflict (4) FUNCTION: Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. SUBUNIT: Binds to the N-terminus of tropomyosin and to actin. TISSUE SPECIFICITY: Neuronal-tissue specific. +O88472 TNR17_MOUSE Tumor necrosis factor receptor superfamily member 17 (B-cell maturation protein) (CD antigen CD269) 185 20,442 Alternative sequence (1); Chain (1); Disulfide bond (3); Repeat (1); Topological domain (2); Transmembrane (1) TRANSMEM 50 70 Helical; Signal-anchor for type III membrane protein. {ECO:0000255}. TOPO_DOM 1 49 Extracellular. {ECO:0000255}.; TOPO_DOM 71 185 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for TNFSF13B/BLyS/BAFF and TNFSF13/APRIL. Promotes B-cell survival and plays a role in the regulation of humoral immunity. Activates NF-kappa-B and JNK (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type III membrane protein {ECO:0000305}. SUBUNIT: Associates with TRAF1, TRAF2, TRAF3, TRAF5 and TRAF6. {ECO:0000250}. TISSUE SPECIFICITY: Detected in spleen, thymus, bone marrow and heart, and at lower levels in kidney and lung. +P13412 TNNI2_MOUSE Troponin I, fast skeletal muscle (Troponin I, fast-twitch isoform) 182 21,358 Calcium binding (1); Chain (1); Initiator methionine (1); Modified residue (3); Region (2) FUNCTION: Troponin I is the inhibitory subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity. SUBUNIT: Binds to actin and tropomyosin. +Q99JG7 TNIP2_MOUSE TNFAIP3-interacting protein 2 (A20-binding inhibitor of NF-kappa-B activation 2) (ABIN-2) 430 49,094 Chain (1); Coiled coil (3); Modified residue (1); Region (1); Sequence conflict (1); Zinc finger (1) FUNCTION: Inhibits NF-kappa-B activation by blocking the interaction of RIPK1 with its downstream effector NEMO/IKBKG. Forms a ternary complex with NFKB1 and MAP3K8 but appears to function upstream of MAP3K8 in the TLR4 signaling pathway that regulates MAP3K8 activation. Involved in activation of the MEK/ERK signaling pathway during innate immune response; this function seems to be stimulus- and cell type specific. Required for stability of MAP3K8. Involved in regulation of apoptosis in endothelial cells; promotes TEK agonist-stimulated endothelial survival. May act as transcriptional coactivator when translocated to the nucleus. Enhances CHUK-mediated NF-kappa-B activation involving NF-kappa-B p50-p65 and p50-c-Rel complexes. {ECO:0000269|PubMed:11390377, ECO:0000269|PubMed:16633345}. PTM: In vitro phosphorylated by CHUK. {ECO:0000250}.; PTM: Ubiquitinated; undergoes 'Lys-48'-linked polyubiquitination probably leading to constitutive proteasomal degradation which can be impaired by IKK-A/CHUK or IKBKB probably involving deubiquitination. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8NFZ5}. SUBUNIT: Interacts with STK11/LKB1, TNFAIP3, IKBKG, NFKB1, MAP3K8, TEK, RIPK1, CHUK, IKBKB and SMARCD1. Interacts with polyubiquitin (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed in all tissues examined. {ECO:0000269|PubMed:11390377}. +Q99ML2 TNK1_MOUSE Non-receptor tyrosine-protein kinase TNK1 (EC 2.7.10.2) (Kinase of embryonic stem cells) 666 73,099 Active site (1); Alternative sequence (2); Binding site (1); Chain (1); Compositional bias (1); Domain (2); Modified residue (6); Mutagenesis (1); Nucleotide binding (1); Sequence conflict (5) FUNCTION: May function in signaling pathways utilized broadly during fetal development and more selectively in adult tissues and in cells of the lymphohematopoietic system. Could specifically be involved in phospholipid signal transduction (By similarity). Involved in negative regulation of cell growth. Has tumor suppressor properties. Plays a negative regulatory role in the Ras-MAPK pathway. {ECO:0000250, ECO:0000269|PubMed:12789265, ECO:0000269|PubMed:18974114}. PTM: Autophosphorylated on tyrosine residues. {ECO:0000269|PubMed:12789265}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:12789265}. SUBUNIT: Interacts with the SH3 domain of PLCG1 via its Pro-rich domain. {ECO:0000250|UniProtKB:Q13470}. TISSUE SPECIFICITY: Expressed in whole embryo and all adult tissues examined including liver, kidney, heart, brain, skeletal muscle and intestine. Also detected in various myeloid- and lymphoid-derived cell lines. {ECO:0000269|PubMed:12789265}. +Q60846 TNR8_MOUSE Tumor necrosis factor receptor superfamily member 8 (CD30L receptor) (Lymphocyte activation antigen CD30) (CD antigen CD30) 498 53,216 Chain (1); Disulfide bond (8); Glycosylation (3); Modified residue (2); Repeat (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 259 279 Helical. {ECO:0000255}. TOPO_DOM 19 258 Extracellular. {ECO:0000255}.; TOPO_DOM 280 498 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for TNFSF8/CD30L. May play a role in the regulation of cellular growth and transformation of activated lymphoblasts. Regulates gene expression through activation of NF-kappa-B (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Interacts with TRAF1, TRAF2, TRAF3 and TRAF5. {ECO:0000250}. TISSUE SPECIFICITY: Detected in thymus and in activated splenocytes. +P20334 TNR9_MOUSE Tumor necrosis factor receptor superfamily member 9 (4-1BB ligand receptor) (T-cell antigen 4-1BB) (CD antigen CD137) 256 27,598 Beta strand (15); Chain (1); Disulfide bond (10); Glycosylation (2); Helix (1); Repeat (4); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 188 208 Helical. {ECO:0000255}. TOPO_DOM 24 187 Extracellular. {ECO:0000255}.; TOPO_DOM 209 256 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for TNFSF9/4-1BBL. Possibly active during T cell activation. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Principally a homodimer, but also found as a monomer. Associates with p56-LCK. Interacts with TRAF1, TRAF2 and TRAF3 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed on the surface of activated T-cells. +Q8BX35 TNR27_MOUSE Tumor necrosis factor receptor superfamily member 27 (X-linked ectodysplasin-A2 receptor) (EDA-A2 receptor) 297 33,066 Chain (1); Disulfide bond (8); Glycosylation (2); Repeat (3); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 139 159 Helical; Signal-anchor for type III membrane protein. {ECO:0000255}. TOPO_DOM 1 138 Extracellular. {ECO:0000255}.; TOPO_DOM 160 297 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for EDA isoform A2, but not for EDA isoform A1. Mediates the activation of the NF-kappa-B and JNK pathways. Activation seems to be mediated by binding to TRAF3 and TRAF6 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. SUBUNIT: Associates with TRAF1, TRAF3 and TRAF6. {ECO:0000250}. +Q9CZW5 TOM70_MOUSE Mitochondrial import receptor subunit TOM70 (Mitochondrial precursor proteins import receptor) (Translocase of outer membrane 70 kDa subunit) (Translocase of outer mitochondrial membrane protein 70) 611 67,590 Chain (1); Cross-link (1); Initiator methionine (1); Modified residue (8); Repeat (10); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 42 62 Helical. {ECO:0000255}. TOPO_DOM 2 41 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 63 611 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor that accelerates the import of all mitochondrial precursor proteins. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. SUBUNIT: Forms part of the preprotein translocase complex of the outer mitochondrial membrane (TOM complex) which consists of at least 7 different proteins (TOMM5, TOMM6, TOMM7, TOMM20, TOMM22, TOMM40 and TOMM70). Interacts with CAPN8. {ECO:0000269|PubMed:16476741}. TISSUE SPECIFICITY: Expressed in the base region of the oxyntic and pyloric mucosae. {ECO:0000269|PubMed:16476741}. +Q01320 TOP2A_MOUSE DNA topoisomerase 2-alpha (EC 5.99.1.3) (DNA topoisomerase II, alpha isozyme) 1528 172,790 Active site (1); Binding site (2); Chain (1); Cross-link (41); Domain (1); Metal binding (4); Modified residue (25); Nucleotide binding (3); Region (2); Sequence conflict (7); Site (10) FUNCTION: Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks. Essential during mitosis and meiosis for proper segregation of daughter chromosomes. May play a role in regulating the period length of ARNTL/BMAL1 transcriptional oscillation (PubMed:24321095). {ECO:0000269|PubMed:1331984, ECO:0000269|PubMed:24321095}. PTM: Phosphorylation has no effect on catalytic activity. However, phosphorylation at Ser-1105 by CSNK1D/CK1 promotes DNA cleavable complex formation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Homodimer. Interacts with COPS5. Interacts with RECQL5; this stimulates DNA decatenation. Interacts with SETMAR; stimulates the topoisomerase activity. Interacts with DHX9; this interaction occurs in a E2 enzyme UBE2I- and RNA-dependent manner, negatively regulates DHX9-mediated double-stranded DNA and RNA duplex helicase activity and stimulates TOP2A-mediated supercoiled DNA relaxation activity. Interacts with HNRNPU (via C-terminus); this interaction protects the topoisomerase TOP2A from degradation and positively regulates the relaxation of supercoiled DNA in a RNA-dependent manner. {ECO:0000250|UniProtKB:P11388, ECO:0000250|UniProtKB:P41516}. +P0C7W3 TOR2X_MOUSE Prosalusin (Torsin family 2 member A) (Torsin-2A) [Cleaved into: Salusin-beta] 231 25,377 Chain (1); Glycosylation (1); Nucleotide binding (1); Peptide (1); Propeptide (1); Region (1); Signal peptide (1) FUNCTION: Salusin may be a endocrine and/or paracrine factor able to increase intracellular calcium concentrations and induce cell mitogenesis. Salusin may also be a potent hypotensive peptide (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +Q8K288 TP8L1_MOUSE Tumor necrosis factor alpha-induced protein 8-like protein 1 (TIPE1) (TNF alpha-induced protein 8-like protein 1) (TNFAIP8-like protein 1) (Oxidative stress regulated gene-beta) (Oxy-beta) 186 20,818 Chain (1); Sequence conflict (5) FUNCTION: Acts as a negative regulator of mTOR activity. {ECO:0000269|PubMed:24444419}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21600655}. SUBUNIT: Interacts with FBXW5; TNFAIP8L1 competes with TSC2 to bind FBXW5 increasing TSC2 stability by preventing its ubiquitination. {ECO:0000269|PubMed:24444419}. TISSUE SPECIFICITY: Detected in wide variety tissues, such as neurons in brain, hepatocytes, germ cells of female and male reproductive organs, muscular tissues and variety types of cells of the epithelial origin (at protein level). {ECO:0000269|PubMed:21600655}. +Q9D8Y7 TP8L2_MOUSE Tumor necrosis factor alpha-induced protein 8-like protein 2 (TIPE2) (TNF alpha-induced protein 8-like protein 2) (TNFAIP8-like protein 2) 184 20,615 Chain (1) FUNCTION: Acts as a negative regulator of innate and adaptive immunity by maintaining immune homeostasis. Negative regulator of Toll-like receptor and T-cell receptor function. Prevents hyperresponsiveness of the immune system and maintains immune homeostasis. Inhibits JUN/AP1 and NF-kappa-B activation. Promotes Fas-induced apoptosis. {ECO:0000269|PubMed:18455983}. SUBUNIT: May interact with CASP8; however, such result is unclear. DOMAIN: The central region was initially thought to constitute a DED (death effector) domain. However, 3D-structure data reveal a previously uncharacterized fold that is different from the predicted fold of a DED (death effector) domain. It consists of a large, hydrophobic central cavity that is poised for cofactor binding (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in thymus, spleen, lymph node and small intestine, but not in liver, heart, muscle, testis, spinal cord or brain. Up-regulated in the spinal cord of mice with experimental autoimmune encephalomyelitis. Constitutively expressed by macrophages, B and T-lymphocytes at various developmental stages. {ECO:0000269|PubMed:18455983}. +O54818 TPD53_MOUSE Tumor protein D53 (mD53) (Tumor protein D52-like 1) 204 22,515 Chain (1); Coiled coil (1); Modified residue (8) SUBUNIT: Forms a homodimer or heterodimer with other members of the family. {ECO:0000250}. +Q9CYZ2 TPD54_MOUSE Tumor protein D54 (Tumor protein D52-like 2) 220 24,043 Chain (1); Coiled coil (1); Modified residue (13) SUBUNIT: Forms a homodimer or heterodimer with other members of the family. Interacts with MAL2 (By similarity). {ECO:0000250}. +Q99MS8 TPGS1_MOUSE Tubulin polyglutamylase complex subunit 1 (PGs1) (p32) 303 32,626 Chain (1); Modified residue (2) FUNCTION: May act in the targeting of the tubulin polyglutamylase complex. Required for the development of the spermatid flagellum. {ECO:0000269|PubMed:12242242, ECO:0000269|PubMed:12972506, ECO:0000269|PubMed:15890843}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:12972506}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:12972506}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:12972506}. Cytoplasm, cytoskeleton, flagellum basal body {ECO:0000269|PubMed:12972506}. Cell projection, axon {ECO:0000269|PubMed:12972506}. Cell projection, dendrite {ECO:0000269|PubMed:12972506}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:12972506}. Note=Associated with microtubules from neurites, centrosomes, basal bodies and axonemes. SUBUNIT: Part of the neuronal tubulin polyglutamylase complex which contains TPGS1, TPGS2, TTLL1, LRRC49 and NICN1. TISSUE SPECIFICITY: Broadly expressed at low levels. Highly expressed in brain. Present in brain neurons (at protein level). {ECO:0000269|PubMed:12242242, ECO:0000269|PubMed:12972506}. +Q9JLV2 TP4AP_MOUSE Short transient receptor potential channel 4-associated protein (Trp4-associated protein) (Trpc4-associated protein) (Protein TAP1) (Rabex-5/Rin2-interacting protein) (TNF-receptor ubiquitous scaffolding/signaling protein) (Protein TRUSS) 797 90,727 Alternative sequence (1); Chain (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (1); Region (1); Sequence conflict (6) Protein modification; protein ubiquitination. FUNCTION: Substrate-specific adapter of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex required for cell cycle control. The DCX(TRUSS) complex specifically mediates the polyubiquitination and subsequent degradation of MYC (By similarity). Also participates in the activation of NFKB1 in response to ligation of TNFRSF1A, possibly by linking TNFRSF1A to the IKK signalosome. Involved in JNK activation via its interaction with TRAF2. Also involved in elevation of endoplasmic reticulum Ca(2+) storage reduction in response to CHRM1. {ECO:0000250, ECO:0000269|PubMed:16876162, ECO:0000269|PubMed:20458742}. SUBUNIT: Component of the DCX(TRUSS) E3 ubiquitin ligase complex, at least composed of CUL4A, DDB1, TRPC4AP/TRUSS and RBX1. Interacts directly with DDB1 (By similarity). Interacts with MYC (By similarity). Constitutively associated with TNFRSF1A. Directly interacts with TRADD, TRAF2, CHUK, IKBKB and IKBKG. Interacts with TRPC1, TRPC4 and TRPC5. {ECO:0000250|UniProtKB:Q8TEL6, ECO:0000269|PubMed:14585990, ECO:0000269|PubMed:16876162, ECO:0000269|PubMed:20458742}. TISSUE SPECIFICITY: Widely expressed, with high levels in heart, liver and testis. +P58771 TPM1_MOUSE Tropomyosin alpha-1 chain (Alpha-tropomyosin) (Tropomyosin-1) 284 32,681 Alternative sequence (1); Chain (1); Coiled coil (1); Modified residue (9) FUNCTION: Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments. {ECO:0000250|UniProtKB:P09493}. PTM: Phosphorylated at Ser-283 by DAPK1 in response to oxidative stress and this phosphorylation enhances stress fiber formation in endothelial cells. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P04692}. Note=Associates with F-actin stress fibers. {ECO:0000250|UniProtKB:P04692}. SUBUNIT: Homodimer. Heterodimer of an alpha (TPM1, TPM3 or TPM4) and a beta (TPM2) chain. Interacts with HRG (via the HRR domain); the interaction contributes to the antiangiogenic properties of the histidine/proline-rich region (HRR) of HRG. Interacts (via N-terminus) with LMOD2 (via N-terminus) and TMOD1 (via N-terminus). {ECO:0000250|UniProtKB:P04268, ECO:0000250|UniProtKB:P04692, ECO:0000250|UniProtKB:P09493}. DOMAIN: The molecule is in a coiled coil structure that is formed by 2 polypeptide chains. The sequence exhibits a prominent seven-residues periodicity. +Q7M707 TR109_MOUSE Taste receptor type 2 member 109 (T2R109) (mT2R62) 316 36,750 Chain (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 15 35 Helical; Name=1. {ECO:0000255}.; TRANSMEM 63 83 Helical; Name=2. {ECO:0000255}.; TRANSMEM 95 115 Helical; Name=3. {ECO:0000255}.; TRANSMEM 136 156 Helical; Name=4. {ECO:0000255}.; TRANSMEM 192 212 Helical; Name=5. {ECO:0000255}.; TRANSMEM 242 262 Helical; Name=6. {ECO:0000255}.; TRANSMEM 271 291 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 14 Extracellular. {ECO:0000255}.; TOPO_DOM 36 62 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 84 94 Extracellular. {ECO:0000255}.; TOPO_DOM 116 135 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 157 191 Extracellular. {ECO:0000255}.; TOPO_DOM 213 241 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 263 270 Extracellular. {ECO:0000255}.; TOPO_DOM 292 316 Cytoplasmic. {ECO:0000255}. FUNCTION: Putative taste receptor which may play a role in the perception of bitterness. {ECO:0000305}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +P46686 TULP2_MOUSE Tubby-related protein 2 (Protein P4-6) (Tubby-like protein 2) 562 62,724 Alternative sequence (4); Chain (1); Erroneous initiation (3); Modified residue (5); Sequence conflict (7) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19695251}. Secreted {ECO:0000269|PubMed:19695251}. Note=Does not have a cleavable signal peptide and is secreted by a non-conventional pathway. TISSUE SPECIFICITY: Expressed in retina and testis. +Q9JIL5 TULP4_MOUSE Tubby-related protein 4 (Tubby superfamily protein) (Tubby-like protein 4) 1547 169,638 Chain (1); Domain (1); Modified residue (5); Region (1); Repeat (3); Sequence conflict (1) Protein modification; protein ubiquitination. FUNCTION: May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. DOMAIN: The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin ligase complexes. {ECO:0000250}. +P19473 TUR8_MOUSE Tumor rejection antigen P815A 224 25,758 Chain (1); Compositional bias (2); Motif (1) SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: P185A and B result from the expression by tumor P815 of a gene that is silent or expressed at a very low level in most if not all normal cells of adult mice. Expressed in testis and mastocytoma. +Q9CXJ1 SYEM_MOUSE Probable glutamate--tRNA ligase, mitochondrial (EC 6.1.1.17) (Glutamyl-tRNA synthetase) (GluRS) 523 58,326 Binding site (4); Chain (1); Modified residue (2); Motif (2); Nucleotide binding (1); Region (2); Sequence conflict (2); Transit peptide (1) FUNCTION: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. +Q9Z2R6 U119A_MOUSE Protein unc-119 homolog A (Retinal protein 4) (mRG4) 240 27,010 Binding site (1); Chain (1); Modified residue (3) FUNCTION: Involved in synaptic functions in photoreceptor cells, the signal transduction in immune cells as a Src family kinase activator, endosome recycling, the uptake of bacteria and endocytosis, protein trafficking in sensory neurons and as lipid-binding chaperone with specificity for a diverse subset of myristoylated proteins. Specifically binds the myristoyl moiety of a subset of N-terminally myristoylated proteins and is required for their localization. Binds myristoylated GNAT1 and is required for G-protein localization and trafficking in sensory neurons (PubMed:21642972). Probably plays a role in trafficking proteins in photoreceptor cells (PubMed:17174953). Plays important roles in mediating Src family kinase signals for the completion of cytokinesis via RAB11A. {ECO:0000250|UniProtKB:Q13432, ECO:0000269|PubMed:17174953, ECO:0000269|PubMed:19781630, ECO:0000269|PubMed:21642972}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q13432}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q13432}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q13432}. Note=ocalizes to the centrosome in interphase cells and begins to translocate from the spindle pole to the spindle midzone after the onset of mitosis; it then localizes to the intercellular bridge in telophase cells and to the midbody in cytokinetic cells. {ECO:0000250|UniProtKB:Q13432}. SUBUNIT: May interact with GTP-bound ARL1. Interacts with ARL2 and ARL3 (GTP-bound forms); this promotes the release of myristoylated cargo proteins (By similarity). Found in a complex with ARL3, RP2 and UNC119; RP2 induces hydrolysis of GTP ARL3 in the complex, leading to the release of UNC119. Interacts with NPHP3 (when myristoylated). Interacts with CYS1 (when myristoylated). Interacts with C5orf30; interaction only takes place when UNC119 is not liganded with myristoylated proteins (By similarity). Interacts with CABP4; in the absence of calcium. Interacts with DNM1; leading to a decrease of DNM1 GTPase activity. Interacts with LCK; this interaction plays a crucial role in activation of LCK (By similarity). Interacts with FYN (By similarity). Interacts with RAB11A; in a cell cycle-dependent manner (By similarity). Interacts with LYN (via SH2 and SH3 domains); leading to LYN activation (By similarity). Found in a complex with ABL1, ABL2, CRK and UNC119; leading to the inhibition of CRK phosphorylation by ABL kinases. Interacts with CD44 (By similarity). {ECO:0000250}. DOMAIN: Adopts an immunoglobulin-like beta-sandwich fold forming a hydrophobic cavity that captures N-terminally myristoylated target peptides. Phe residues within the hydrophobic beta sandwich are required for myristate binding (By similarity). {ECO:0000250|UniProtKB:Q13432}. TISSUE SPECIFICITY: Localized in photoreceptor synapses in the outer plexiform layer of the retina. {ECO:0000269|PubMed:18296658}. +Q91WQ3 SYYC_MOUSE Tyrosine--tRNA ligase, cytoplasmic (EC 6.1.1.1) (Tyrosyl-tRNA synthetase) (TyrRS) [Cleaved into: Tyrosine--tRNA ligase, cytoplasmic, N-terminally processed] 528 59,105 Binding site (5); Chain (2); Domain (1); Initiator methionine (1); Modified residue (9); Motif (2); Sequence conflict (6) FUNCTION: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +Q76HP3 T132D_MOUSE Transmembrane protein 132D (Mature oligodendrocytes transmembrane protein) (Mature OL transmembrane protein) 1097 121,416 Chain (1); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 914 934 Helical. {ECO:0000255}. TOPO_DOM 31 913 Extracellular. {ECO:0000255}.; TOPO_DOM 935 1097 Cytoplasmic. {ECO:0000255}. FUNCTION: May serve as a cell-surface marker for oligodendrocyte differentiation. {ECO:0000269|PubMed:12966072}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in mature oligodendrocytes in the white and gray matter of the brain. {ECO:0000269|PubMed:12966072}. +Q6NXN1 SZRD1_MOUSE SUZ domain-containing protein 1 152 16,998 Alternative sequence (1); Chain (1); Domain (1); Modified residue (6); Sequence conflict (1) +Q9D8Y1 T126A_MOUSE Transmembrane protein 126A 196 21,539 Chain (1); Topological domain (5); Transmembrane (4) TRANSMEM 35 55 Helical. {ECO:0000255}.; TRANSMEM 58 78 Helical. {ECO:0000255}.; TRANSMEM 107 127 Helical. {ECO:0000255}.; TRANSMEM 160 176 Helical. {ECO:0000255}. TOPO_DOM 1 34 Mitochondrial matrix. {ECO:0000255}.; TOPO_DOM 56 57 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 79 106 Mitochondrial matrix. {ECO:0000255}.; TOPO_DOM 128 159 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 177 196 Mitochondrial matrix. {ECO:0000255}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: In the retina, significant levels of expression are detected in the ganglion cell layer, the optic nerve head, the outer plexiform layer, and in the outer ellipsoide length of photoreceptor inner segments. {ECO:0000269|PubMed:19327736}. +Q9JJB1 T191C_MOUSE Transmembrane protein 191C 302 33,974 Alternative sequence (1); Chain (1); Coiled coil (1); Transmembrane (1) TRANSMEM 242 262 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. +P86050 T170B_MOUSE Transmembrane protein 170B 132 14,416 Chain (1); Glycosylation (1); Topological domain (4); Transmembrane (3) TRANSMEM 38 58 Helical. {ECO:0000255}.; TRANSMEM 69 89 Helical. {ECO:0000255}.; TRANSMEM 105 125 Helical. {ECO:0000255}. TOPO_DOM 1 37 Extracellular. {ECO:0000255}.; TOPO_DOM 59 68 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 90 104 Extracellular. {ECO:0000255}.; TOPO_DOM 126 132 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q5T4T1}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Interacts with CTNNB1. {ECO:0000250|UniProtKB:Q5T4T1}. +Q6GQT5 T151A_MOUSE Transmembrane protein 151A 468 51,312 Chain (1); Transmembrane (2) TRANSMEM 45 65 Helical. {ECO:0000255}.; TRANSMEM 98 118 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9R1Q6 T176B_MOUSE Transmembrane protein 176B (Protein LR8) 263 28,367 Chain (1); Modified residue (3); Sequence conflict (2); Transmembrane (4) TRANSMEM 61 81 Helical. {ECO:0000255}.; TRANSMEM 89 109 Helical. {ECO:0000255}.; TRANSMEM 121 141 Helical. {ECO:0000255}.; TRANSMEM 197 217 Helical. {ECO:0000255}. FUNCTION: May play a role in the process of maturation of dendritic cells (By similarity). Required for the development of cerebellar granule cells. {ECO:0000250, ECO:0000269|PubMed:16814752}. SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed with higher expression in lung, liver, kidney and colon. Expressed in cerebellar granule cells. {ECO:0000269|PubMed:16814752}. +Q9EP51 V1R50_MOUSE Vomeronasal type-1 receptor 50 (Pheromone receptor VN2) (Vomeronasal receptor 2) (Vomeronasal type-1 receptor A5) (Vomeronasal type-1 receptor B1) 310 35,195 Chain (1); Disulfide bond (1); Glycosylation (1); Sequence conflict (1); Topological domain (8); Transmembrane (7) TRANSMEM 17 37 Helical; Name=1. {ECO:0000255}.; TRANSMEM 51 71 Helical; Name=2. {ECO:0000255}.; TRANSMEM 94 114 Helical; Name=3. {ECO:0000255}.; TRANSMEM 135 155 Helical; Name=4. {ECO:0000255}.; TRANSMEM 194 214 Helical; Name=5. {ECO:0000255}.; TRANSMEM 238 258 Helical; Name=6. {ECO:0000255}.; TRANSMEM 270 290 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 16 Extracellular. {ECO:0000255}.; TOPO_DOM 38 50 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 72 93 Extracellular. {ECO:0000255}.; TOPO_DOM 115 134 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 156 193 Extracellular. {ECO:0000255}.; TOPO_DOM 215 237 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 259 269 Extracellular. {ECO:0000255}.; TOPO_DOM 291 310 Cytoplasmic. {ECO:0000255}. FUNCTION: Putative pheromone receptor implicated in the regulation of social and reproductive behavior. {ECO:0000269|PubMed:12214233}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Expressed in a subset of sensory neurons located in the apical layer of the vomeronasal organ. {ECO:0000269|PubMed:12214233}. +Q9CY24 T179B_MOUSE Transmembrane protein 179B 219 23,528 Chain (1); Modified residue (1); Sequence conflict (1); Transmembrane (4) TRANSMEM 9 29 Helical. {ECO:0000255}.; TRANSMEM 65 85 Helical. {ECO:0000255}.; TRANSMEM 98 118 Helical. {ECO:0000255}.; TRANSMEM 162 182 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9EQN3 T22D4_MOUSE TSC22 domain family protein 4 (TSC22-related-inducible leucine zipper protein 2) (Thg-1pit) 387 39,979 Chain (1); Frameshift (1); Modified residue (12); Region (1); Sequence conflict (2) FUNCTION: Transcriptional repressor. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Forms a homodimer or heterodimer. Can form a heterodimer with TSC22D1 (By similarity). {ECO:0000250}. +A2AF53 T185A_MOUSE Transmembrane protein 185A (Erythropoietin-induced EST 3) (Protein FAM11A) 350 40,620 Chain (1); Region (1); Transmembrane (7) TRANSMEM 16 36 Helical. {ECO:0000255}.; TRANSMEM 41 61 Helical. {ECO:0000255}.; TRANSMEM 81 101 Helical. {ECO:0000255}.; TRANSMEM 111 131 Helical. {ECO:0000255}.; TRANSMEM 177 197 Helical. {ECO:0000255}.; TRANSMEM 211 231 Helical. {ECO:0000255}.; TRANSMEM 240 260 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Cell projection, dendrite {ECO:0000269|PubMed:15525354}. Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Interacts with MAP1B. {ECO:0000250}. TISSUE SPECIFICITY: Broadly expressed in brain where it is specifically expressed by neurons (at protein level). Also detected in some cells of arterioles, intestine, lung and testis (at protein level). {ECO:0000269|PubMed:15525354}. +Q9CQD8 VA0E1_MOUSE V-type proton ATPase subunit e 1 (V-ATPase subunit e 1) (Vacuolar proton pump subunit e 1) 81 9,340 Chain (1); Transmembrane (2) TRANSMEM 8 28 Helical. {ECO:0000255}.; TRANSMEM 36 56 Helical. {ECO:0000255}. FUNCTION: Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Composed of at least 10 subunits. +Q91XE7 VA0E2_MOUSE V-type proton ATPase subunit e 2 (V-ATPase subunit e 2) (Vacuolar proton pump subunit e 2) 81 9,198 Chain (1); Transmembrane (2) TRANSMEM 8 28 Helical. {ECO:0000255}.; TRANSMEM 36 56 Helical. {ECO:0000255}. FUNCTION: Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Composed of at least 10 subunits. +Q9CXA2 T3HPD_MOUSE Trans-L-3-hydroxyproline dehydratase (EC 4.2.1.77) (Trans-3-hydroxy-L-proline dehydratase) 354 37,804 Active site (1); Binding site (1); Chain (1); Region (2); Sequence conflict (4) FUNCTION: Catalyzes the dehydration of trans-3-hydroxy-L-proline to delta-1-pyrroline-2-carboxylate (Pyr2C). {ECO:0000269|PubMed:22528483}. SUBUNIT: Homodimer. {ECO:0000250}. +P30987 TA2R_MOUSE Thromboxane A2 receptor (TXA2-R) (Prostanoid TP receptor) 341 37,098 Chain (1); Disulfide bond (1); Glycosylation (2); Modified residue (1); Topological domain (8); Transmembrane (7) TRANSMEM 30 52 Helical; Name=1. {ECO:0000255}.; TRANSMEM 66 86 Helical; Name=2. {ECO:0000255}.; TRANSMEM 106 127 Helical; Name=3. {ECO:0000255}.; TRANSMEM 148 170 Helical; Name=4. {ECO:0000255}.; TRANSMEM 192 217 Helical; Name=5. {ECO:0000255}.; TRANSMEM 245 268 Helical; Name=6. {ECO:0000255}.; TRANSMEM 288 309 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 29 Extracellular. {ECO:0000255}.; TOPO_DOM 53 65 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 87 105 Extracellular. {ECO:0000255}.; TOPO_DOM 128 147 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 171 191 Extracellular. {ECO:0000255}.; TOPO_DOM 218 244 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 269 287 Extracellular. {ECO:0000255}.; TOPO_DOM 310 341 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for thromboxane A2 (TXA2), a potent stimulator of platelet aggregation. The activity of this receptor is mediated by a G-protein that activates a phosphatidylinositol-calcium second messenger system. In the kidney, the binding of TXA2 to glomerular TP receptors causes intense vasoconstriction. Activates phospholipase C and adenylyl cyclase. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBUNIT: Interacts with RPGRIP1L. Interacts with RACK1; the interaction regulates TBXA2R cell surface expression (By similarity). {ECO:0000250}. +Q80WQ2 VAC14_MOUSE Protein VAC14 homolog 782 88,048 Chain (1); Modified residue (5); Natural variant (1); Region (1); Repeat (6); Sequence conflict (3) FUNCTION: The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Acts as a positive activator of PIKfyve kinase activity. Also required to maintain normal levels of phosphatidylinositol 3-phosphate (PtdIns(3)P) and phosphatidylinositol 5-phosphate (PtdIns(5)P). Plays a role in the biogenesis of endosome carrier vesicles (ECV) / multivesicular bodies (MVB) transport intermediates from early endosomes. {ECO:0000269|PubMed:17956977, ECO:0000269|PubMed:19037259}. SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:19037259}. Microsome membrane {ECO:0000250}. Note=Mainly associated with membranes of the late endocytic pathway. SUBUNIT: Forms homooligomers (By similarity). Component of the PI(3,5)P2 regulatory complex/PAS complex, at least composed of PIKFYVE, FIG4 and VAC14. VAC14 nucleates the assembly of the complex and serves as a scaffold. Interacts with NOS1 (By similarity). {ECO:0000250}. DOMAIN: The C-terminal domain (residues 523-782) mediates homomeric interactions and is necessary for the formation and maintenance of the PI(3,5)P2 regulatory complex. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:17956977}. DISEASE: Note=Defects in Vac14 are the cause of the infantile gliosis phenotype (ingls). Mice exhibit reduced body size and diluted pigmentation that can be recognized as early as postnatal day 3 (P3). By P14, the mice exhibit a tremor and impaired motor function. Maximal survival of the mice is for 3 weeks. Small areas with the appearance of spongiform degeneration are visible in several brain regions, including the thalamus, brain stem and cerebellar nucleus. {ECO:0000269|PubMed:19037259}. +Q5QD10 TAA7D_MOUSE Trace amine-associated receptor 7d (TaR-7d) (Trace amine receptor 7d) (mTaar7d) 358 40,305 Chain (1); Disulfide bond (1); Glycosylation (2); Topological domain (8); Transmembrane (7) TRANSMEM 48 68 Helical; Name=1. {ECO:0000255}.; TRANSMEM 84 104 Helical; Name=2. {ECO:0000255}.; TRANSMEM 122 143 Helical; Name=3. {ECO:0000255}.; TRANSMEM 167 187 Helical; Name=4. {ECO:0000255}.; TRANSMEM 213 233 Helical; Name=5. {ECO:0000255}.; TRANSMEM 275 295 Helical; Name=6. {ECO:0000255}.; TRANSMEM 310 333 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 47 Extracellular. {ECO:0000255}.; TOPO_DOM 69 83 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 105 121 Extracellular. {ECO:0000255}.; TOPO_DOM 144 166 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 188 212 Extracellular. {ECO:0000255}.; TOPO_DOM 234 274 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 296 309 Extracellular. {ECO:0000255}.; TOPO_DOM 334 358 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan olfactory receptor specific for trace amines. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Specifically expressed in neurons of the olfactory epithelium. {ECO:0000269|PubMed:16878137}. +Q923Y8 TAAR1_MOUSE Trace amine-associated receptor 1 (TaR-1) (Trace amine receptor 1) 332 37,621 Chain (1); Disulfide bond (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 25 45 Helical; Name=1. {ECO:0000255}.; TRANSMEM 59 79 Helical; Name=2. {ECO:0000255}.; TRANSMEM 98 118 Helical; Name=3. {ECO:0000255}.; TRANSMEM 139 159 Helical; Name=4. {ECO:0000255}.; TRANSMEM 188 208 Helical; Name=5. {ECO:0000255}.; TRANSMEM 250 270 Helical; Name=6. {ECO:0000255}.; TRANSMEM 288 308 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 24 Extracellular. {ECO:0000255}.; TOPO_DOM 46 58 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 80 97 Extracellular. {ECO:0000255}.; TOPO_DOM 119 138 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 160 187 Extracellular. {ECO:0000255}.; TOPO_DOM 209 249 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 271 287 Extracellular. {ECO:0000255}.; TOPO_DOM 309 332 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for trace amines, including beta-phenylethylamine (b-PEA), p-tyramine (p-TYR), octopamine and tryptamine, with highest affinity for b-PEA and p-TYR. Unresponsive to classical biogenic amines, such as epinephrine and histamine and only partially activated by dopamine and serotonin. Trace amines are biogenic amines present in very low levels in mammalian tissues. Although some trace amines have clearly defined roles as neurotransmitters in invertebrates, the extent to which they function as true neurotransmitters in vertebrates has remained speculative. Trace amines are likely to be involved in a variety of physiological functions that have yet to be fully understood. The signal transduced by this receptor is mediated by the G(s)-class of G-proteins which activate adenylate cyclase. {ECO:0000269|PubMed:15718104}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Widely distributed throughout the brain. Strongly expressed in the mitral cell layer of the olfactory bulb, piriform cortex, the arcuate, motor, and mesencephalic trigeminal nuclei, lateral reticular and hypoglossal nuclei, cerebellar Purkinje cells, and ventral horn of the spinal cord. Moderately expressed in the frontal, entorhinal, and agranular cortices, the ventral pallidum, thalamus, hippocampus, several hypothalamic nuclei, ambiguus, dorsal raphe, and gigantocellular reticular nuclei. Weakly expressed in the septum, basal ganglia, amygdala, myelencephalon, and spinal cord dorsal horn. Particularly interesting is the moderate expression in several monoaminergic cell groups, namely the dorsal raphe, the locus coeruleus, and the ventral tegmental area. +Q9R1Q9 VAS1_MOUSE V-type proton ATPase subunit S1 (V-ATPase subunit S1) (Protein C7-1) (V-ATPase Ac45 subunit) (V-ATPase S1 accessory protein) (Vacuolar proton pump subunit S1) 463 51,008 Chain (1); Glycosylation (8); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 413 433 Helical. {ECO:0000255}. TOPO_DOM 33 412 Vacuolar. {ECO:0000255}.; TOPO_DOM 434 463 Cytoplasmic. {ECO:0000255}. FUNCTION: Accessory subunit of the proton-transporting vacuolar (V)-ATPase protein pump, which is required for luminal acidification of secretory vesicles. Guides the V-type ATPase into specialized subcellular compartments, such as neuroendocrine regulated secretory vesicles or the ruffled border of the osteoclast, thereby regulating its activity. Involved in membrane trafficking and Ca(2+)-dependent membrane fusion. May play a role in the assembly of the V-type ATPase complex. In aerobic conditions, involved in intracellular iron homeostasis, thus triggering the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent proteasomal degradation (By similarity). {ECO:0000250|UniProtKB:Q15904}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q15904}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q15904}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q15904}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q15904}. Note=Not detected in trans-Golgi network. {ECO:0000250|UniProtKB:Q15904}. SUBUNIT: Component of the multisubunit proton-transporting vacuolar (V)-ATPase protein pump. {ECO:0000250|UniProtKB:Q15904}. TISSUE SPECIFICITY: Expressed in brain cortex (at protein level). {ECO:0000269|PubMed:27231034}. +Q8C5G2 VASH2_MOUSE Tubulinyl-Tyr carboxypeptidase 2 (EC 3.4.17.17) (Vasohibin-2) (Vasohibin-like protein) 355 40,499 Active site (3); Chain (1); Erroneous initiation (1); Modified residue (1); Mutagenesis (1); Sequence conflict (1) FUNCTION: Tyrosine carboxypeptidase that removes the C-terminal tyrosine residue of alpha-tubulin, thereby regulating microtubule dynamics and function (PubMed:29146868). Acts as an activator of angiogenesis: expressed in infiltrating mononuclear cells in the sprouting front to promote angiogenesis (PubMed:19204325). {ECO:0000269|PubMed:19204325, ECO:0000269|PubMed:29146868}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q86V25}. Secreted {ECO:0000250|UniProtKB:Q86V25}. Note=Mainly localizes in the cytoplasm. Some fraction is secreted via a non-canonical secretion system; interaction with SVBP promotes secretion. {ECO:0000250|UniProtKB:Q86V25}. SUBUNIT: Interacts with SVBP; interaction enhances VASH1 tyrosine carboxypeptidase activity. {ECO:0000269|PubMed:29146868}. TISSUE SPECIFICITY: Preferentially expressed in bone marrow-derived mononuclear cells at the sprouting front. {ECO:0000269|PubMed:29146868}. +Q5QD04 TAAR9_MOUSE Trace amine-associated receptor 9 (TaR-9) (Trace amine receptor 9) (mTaar9) 348 38,901 Chain (1); Disulfide bond (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 34 54 Helical; Name=1. {ECO:0000255}.; TRANSMEM 69 89 Helical; Name=2. {ECO:0000255}.; TRANSMEM 108 128 Helical; Name=3. {ECO:0000255}.; TRANSMEM 148 168 Helical; Name=4. {ECO:0000255}.; TRANSMEM 198 218 Helical; Name=5. {ECO:0000255}.; TRANSMEM 260 280 Helical; Name=6. {ECO:0000255}.; TRANSMEM 295 315 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 33 Extracellular. {ECO:0000255}.; TOPO_DOM 55 68 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 90 107 Extracellular. {ECO:0000255}.; TOPO_DOM 129 147 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 169 197 Extracellular. {ECO:0000255}.; TOPO_DOM 219 259 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 281 294 Extracellular. {ECO:0000255}.; TOPO_DOM 316 348 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan olfactory receptor specific for trace amines. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Specifically expressed in neurons of the olfactory epithelium. {ECO:0000269|PubMed:16878137}. +Q9D902 T2EB_MOUSE General transcription factor IIE subunit 2 (Transcription initiation factor IIE subunit beta) (TFIIE-beta) 292 33,047 Chain (1); Compositional bias (3); DNA binding (1); Modified residue (3); Sequence conflict (2) FUNCTION: Recruits TFIIH to the initiation complex and stimulates the RNA polymerase II C-terminal domain kinase and DNA-dependent ATPase activities of TFIIH. Both TFIIH and TFIIE are required for promoter clearance by RNA polymerase (By similarity). {ECO:0000250|UniProtKB:P29084}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00682}. SUBUNIT: Tetramer of two alpha and two beta chains. Interacts with FACT subunit SUPT16H. Interacts with ATF7IP. Interacts with SND1. {ECO:0000250|UniProtKB:P29084}. +Q80TB8 VAT1L_MOUSE Synaptic vesicle membrane protein VAT-1 homolog-like (EC 1.-.-.-) 417 45,817 Chain (1); Erroneous initiation (1); Modified residue (4) +Q3THK3 T2FA_MOUSE General transcription factor IIF subunit 1 (Transcription initiation factor IIF subunit alpha) (TFIIF-alpha) 508 57,241 Chain (1); Compositional bias (1); Initiator methionine (1); Modified residue (19); Sequence conflict (4) FUNCTION: TFIIF is a general transcription initiation factor that binds to RNA polymerase II and helps to recruit it to the initiation complex in collaboration with TFIIB. It promotes transcription elongation (By similarity). {ECO:0000250}. PTM: Phosphorylated on Ser and other residues by TAF1 and casein kinase II-like kinases. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Heterodimer of an alpha and a beta subunit. Interacts with GTF2F2, CTDP1, TAF6/TAFII80 and URI1 (By similarity). Interacts with GTF2B (via C-terminus and preferentially via acetylated form); this interaction prevents binding of GTF2B to GTF2F2 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P35269}. +Q571K4 TAB3_MOUSE TGF-beta-activated kinase 1 and MAP3K7-binding protein 3 (Mitogen-activated protein kinase kinase kinase 7-interacting protein 3) (TAK1-binding protein 3) (TAB-3) (TGF-beta-activated kinase 1-binding protein 3) 716 79,029 Chain (1); Coiled coil (1); Compositional bias (3); Domain (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (9); Turn (2); Zinc finger (1) FUNCTION: Adapter linking MAP3K7/TAK1 and TRAF6 or TRAF2. Mediator of MAP3K7 activation, respectively in the IL-1 and TNF signaling pathways. Plays a role in activation of NF-kappa-B and AP1 transcription factor (By similarity). {ECO:0000250}. PTM: Phosphorylated at Ser-510 by MAPKAPK2 and MAPKAPK3 following IL1 treatment.; PTM: Ubiquitinated; following IL1 stimulation or TRAF6 overexpression. {ECO:0000250}. SUBUNIT: Interacts with TAB1, TAB2, MAP3K7, TRAF2 and TRAF6. The minimal TAB3-containing complex (TAB1-MAP3K7-TAB3) appears not to contain TAB2. However, it seems sensible to consider that TAB2 may also join this complex and may act in a cooperative manner with TAB3. Interacts with WDR34 (via the WD domains). Binds 'Lys-63'-linked polyubiquitin chains. Interacts with RBCK1 (By similarity). Interacts with TRIM5 (By similarity). {ECO:0000250}. DOMAIN: The RanBP2-type zinc finger (NZF) mediates binding to two consecutive 'Lys-63'-linked ubiquitins. +Q9D3R9 TAF7L_MOUSE Transcription initiation factor TFIID subunit 7-like (TATA box binding protein-associated factor RNA polymerase II subunit Q) (TATA box-binding protein-associated factor 50 kDa) (Transcription initiation factor TFIID 50 kDa subunit) 471 52,905 Alternative sequence (1); Chain (1); Coiled coil (1); Modified residue (1); Sequence conflict (1) FUNCTION: Probably functions as a spermatogensis-specific component of the DNA-binding general transcription factor complex TFIID, a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. May play a role in spermatogenesis. {ECO:0000269|PubMed:12665565}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Cytoplasmic in spermatogonia and early spermatocytes (preleptotene, leptotene, and zygotene); translocates into the nuclei of pachytene spermatocytes and round spermatids. SUBUNIT: TFIID is composed of TATA binding protein (TBP) and a number of TBP-associated factors (TAFs). TAF7L may replace TAF7 in a spermatogenesis-specific form of TFIID. Interacts with TBP; the interaction occurs in a sub-population of cells (pachytene and haploid round spermatids) and is developmentally regulated through differential intracellular localization of the two proteins. Interacts with TAF1. {ECO:0000269|PubMed:12665565}. TISSUE SPECIFICITY: Testis-specific (at protein level). Expressed during spermatogenesis from spermatogonia stage up to the stage of round spermatids. {ECO:0000269|PubMed:11279525, ECO:0000269|PubMed:17242199}. +Q6NZA9 TAF9B_MOUSE Transcription initiation factor TFIID subunit 9B (Transcription initiation factor TFIID subunit 9-like) (Transcription-associated factor TAFII31L) 249 27,172 Chain (1); Compositional bias (1); Erroneous initiation (2); Modified residue (4); Sequence conflict (2) FUNCTION: Essential for cell viability. TAF9 and TAF9B are involved in transcriptional activation as well as repression of distinct but overlapping sets of genes. May have a role in gene regulation associated with apoptosis. TAFs are components of the transcription factor IID (TFIID) complex, the TBP-free TAFII complex (TFTC), the PCAF histone acetylase complex and the STAGA transcription coactivator-HAT complex. TFIID or TFTC are essential for the regulation of RNA polymerase II-mediated transcription (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Binds TAF5 and TAF6. Component of TFIID and the TATA-binding protein-free TAF complex (TFTC). TFIID is composed of TATA binding protein (TBP) and a number of TBP-associated factors (TAFs). Binds N-terminal domain of p53/TP53 which is essential for transcription (By similarity). {ECO:0000250}. +Q9D593 VATE2_MOUSE V-type proton ATPase subunit E 2 (V-ATPase subunit E 2) (Vacuolar proton pump subunit E 2) 226 26,307 Chain (1); Sequence conflict (1) FUNCTION: Subunit of the peripheral V1 complex of vacuolar ATPase essential for assembly or catalytic function. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. This isoform is essential for energy coupling involved in acidification of acrosome. {ECO:0000269|PubMed:11872743}. SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'' and d). TISSUE SPECIFICITY: Testis specific. {ECO:0000269|PubMed:11872743}. +Q3TUH1 TAM41_MOUSE Phosphatidate cytidylyltransferase, mitochondrial (EC 2.7.7.41) (CDP-diacylglycerol synthase) (CDP-DAG synthase) (Mitochondrial translocator assembly and maintenance protein 41 homolog) (TAM41) 337 37,828 Alternative sequence (2); Chain (1); Frameshift (1); Transit peptide (1) Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3. FUNCTION: Catalyzes the formation of CDP-diacylglycerol (CDP-DAG) from phosphatidic acid (PA) in the mitochondrial inner membrane. Required for the biosynthesis of the dimeric phospholipid cardiolipin, which stabilizes supercomplexes of the mitochondrial respiratory chain in the mitochondrial inner membrane (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Matrix side {ECO:0000250}. +Q0VGY8 TANC1_MOUSE Protein TANC1 (Tetratricopeptide repeat, ankyrin repeat and coiled-coil domain-containing protein 1) 1856 200,805 Alternative sequence (3); Chain (1); Compositional bias (2); Erroneous gene model prediction (2); Modified residue (12); Repeat (14); Sequence conflict (3) FUNCTION: May be a scaffold component in the postsynaptic density. {ECO:0000250}. PTM: Phosphorylated; by MINK1 and TNIK upon stimulation by RAP2A. {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250}. SUBUNIT: Interacts probably directly with DLG1, DLG4, HOMER1. Interacts with DLGAP1, INA, CAMK2A, GRIN2B and GRIA1. Interacts with TNIK and MINK1 (By similarity). {ECO:0000250}. +Q6ZQ29 TAOK2_MOUSE Serine/threonine-protein kinase TAO2 (EC 2.7.11.1) (Thousand and one amino acid protein 2) 1240 139,297 Active site (1); Alternative sequence (2); Binding site (1); Chain (1); Coiled coil (4); Compositional bias (3); Domain (1); Erroneous initiation (1); Modified residue (9); Nucleotide binding (1); Sequence caution (1); Transmembrane (5) TRANSMEM 972 992 Helical. {ECO:0000255}.; TRANSMEM 994 1014 Helical. {ECO:0000255}.; TRANSMEM 1019 1039 Helical. {ECO:0000255}.; TRANSMEM 1045 1065 Helical. {ECO:0000255}.; TRANSMEM 1175 1195 Helical. {ECO:0000255}. FUNCTION: Serine/threonine-protein kinase involved in different processes such as membrane blebbing and apoptotic bodies formation DNA damage response and MAPK14/p38 MAPK stress-activated MAPK cascade. Phosphorylates itself, MBP, activated MAPK8, MAP2K3, MAP2K6 and tubulins. Activates the MAPK14/p38 MAPK signaling pathway through the specific activation and phosphorylation of the upstream MAP2K3 and MAP2K6 kinases. In response to DNA damage, involved in the G2/M transition DNA damage checkpoint by activating the p38/MAPK14 stress-activated MAPK cascade, probably by mediating phosphorylation of upstream MAP2K3 and MAP2K6 kinases. May affect microtubule organization and stability. May play a role in the osmotic stress-MAPK8 pathway. Prevents MAP3K7-mediated activation of CHUK, and thus NF-kappa-B activation. Isoform 2, but not isoform 1, is required for PCDH8 endocytosis. Following homophilic interactions between PCDH8 extracellular domains, isoform 2 phosphorylates and activates MAPK14/p38 MAPK which in turn phosphorylates isoform 2. This process leads to PCDH8 endocytosis and CDH2 cointernalization. Both isoforms are involved in MAPK14/p38 MAPK activation (By similarity). {ECO:0000250}. PTM: Autophosphorylated. Phosphorylated by ATM (By similarity). {ECO:0000250}.; PTM: Isoform 2: Phosphorylated on Ser-1037 by MAPK14. This phosphorylation is required PCDH8 for endocytosis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Found to be perinuclear and localized to vesicular compartment. {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 2: Cell projection, dendrite {ECO:0000250}. Note=In dendrites, colocalizes with PCDH8. {ECO:0000250}. SUBUNIT: Interacts with MAP2K3 and MAP2K6 (By similarity). Self-associates. Interacts with tubulins. Interacts with MAP3K7 and interfers with MAP3K7-binding to CHUK and thus prevents NF-kappa-B activation (By similarity). Isoform 2 interacts with PCDH8; this complex may also include CDH2 (By similarity). {ECO:0000250}. +Q8BHL3 TB10B_MOUSE TBC1 domain family member 10B (Protein wz3-85) 798 87,275 Chain (1); Coiled coil (1); Domain (1); Erroneous initiation (5); Modified residue (9); Sequence conflict (5) FUNCTION: Acts as GTPase-activating protein for RAB3A, RAB22A, RAB27A, AND RAB35. Does not act on RAB2A and RAB6A (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +P99024 TBB5_MOUSE Tubulin beta-5 chain 444 49,671 Chain (1); Cross-link (2); Modified residue (9); Mutagenesis (2); Nucleotide binding (1); Sequence conflict (7) FUNCTION: Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. PTM: Some glutamate residues at the C-terminus are polyglycylated, resulting in polyglycine chains on the gamma-carboxyl group. Glycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Both modifications can coexist on the same protein on adjacent residues, and lowering polyglycylation levels increases polyglutamylation, and reciprocally. The precise function of polyglycylation is still unclear. {ECO:0000269|PubMed:19524510}.; PTM: Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (PubMed:15890843). Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity by SPAST increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold (By similarity). {ECO:0000250|UniProtKB:Q71U36, ECO:0000269|PubMed:15890843}.; PTM: Phosphorylated on Ser-172 by CDK1 during the cell cycle, from metaphase to telophase, but not in interphase. This phosphorylation inhibits tubulin incorporation into microtubules. {ECO:0000269|PubMed:16371510}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:26637975}. SUBUNIT: Heterodimer of alpha and beta chains (By similarity). A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells. Interacts with PIFO (PubMed:20643351). Interacts with DIAPH1 (By similarity). Interacts with MX1 (By similarity). May interact with RNABP10 (PubMed:18347012). Interacts with CFAP157 (PubMed:27965440). {ECO:0000250|UniProtKB:P07437, ECO:0000250|UniProtKB:P69893, ECO:0000269|PubMed:18347012, ECO:0000269|PubMed:20643351, ECO:0000269|PubMed:27965440}. TISSUE SPECIFICITY: Ubiquitously expressed with highest levels in spleen, thymus and immature brain. Expressed in embryonic brain, including throughout the developing cortex and in the subventricular zone. Also found in radial glial cells, intermediate progenitors, migrating neurons and postmitotic neurons (PubMed:23246003). Expressed in skin and developing hair follicle (PubMed:26637975). {ECO:0000269|PubMed:23246003, ECO:0000269|PubMed:26637975}. +A2AQ07 TBB1_MOUSE Tubulin beta-1 chain 451 50,441 Chain (1); Modified residue (3); Nucleotide binding (1) FUNCTION: Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain (By similarity). {ECO:0000250}. PTM: Some glutamate residues at the C-terminus are polyglycylated, resulting in polyglycine chains on the gamma-carboxyl group. Glycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Both modifications can coexist on the same protein on adjacent residues, and lowering polyglycylation levels increases polyglutamylation, and reciprocally. The precise function of polyglycylation is still unclear. {ECO:0000269|PubMed:19524510}.; PTM: Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (PubMed:15890843). Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity by SPAST increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold (By similarity). {ECO:0000250|UniProtKB:Q71U36, ECO:0000269|PubMed:15890843}.; PTM: Phosphorylated on Ser-172 by CDK1 during the cell cycle, from metaphase to telophase, but not in interphase. This phosphorylation inhibits tubulin incorporation into microtubules. {ECO:0000250|UniProtKB:Q9H4B7}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. SUBUNIT: Dimer of alpha and beta chains. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells. Interacts with RANBP10. {ECO:0000269|PubMed:18347012}. +P22599 A1AT2_MOUSE Alpha-1-antitrypsin 1-2 (AAT) (Alpha-1 protease inhibitor 2) (Alpha-1-antiproteinase) (Serine protease inhibitor 1-2) (Serine protease inhibitor A1b) (Serpin A1b) 413 45,975 Chain (1); Glycosylation (3); Region (1); Sequence conflict (29); Signal peptide (1); Site (1) FUNCTION: Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. {ECO:0000269|PubMed:11961105, ECO:0000269|PubMed:8619829}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11961105, ECO:0000269|PubMed:8619829}. DOMAIN: The reactive center loop (RCL) extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site within the RCL, establishing a covalent linkage between the carboxyl group of the serpin reactive site and the serine hydroxyl of the protease. The resulting inactive serpin-protease complex is highly stable (By similarity). Variability within the reactive center loop (RCL) sequences of Serpina1-related genes may determine target protease specificity. {ECO:0000250}. +Q6PAM0 AAKB2_MOUSE 5'-AMP-activated protein kinase subunit beta-2 (AMPK subunit beta-2) 271 30,209 Chain (1); Modified residue (10) FUNCTION: Non-catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Beta non-catalytic subunit acts as a scaffold on which the AMPK complex assembles, via its C-terminus that bridges alpha (PRKAA1 or PRKAA2) and gamma subunits (PRKAG1, PRKAG2 or PRKAG3) (By similarity). {ECO:0000250}. PTM: Phosphorylated when associated with the catalytic subunit (PRKAA1 or PRKAA2). Phosphorylated by ULK1 and ULK2; leading to negatively regulate AMPK activity and suggesting the existence of a regulatory feedback loop between ULK1, ULK2 and AMPK. {ECO:0000269|PubMed:21460634}. SUBUNIT: AMPK is a heterotrimer of an alpha catalytic subunit (PRKAA1 or PRKAA2), a beta (PRKAB1 or PRKAB2) and a gamma non-catalytic subunits (PRKAG1, PRKAG2 or PRKAG3). {ECO:0000250}. +Q5SSE9 ABCAD_MOUSE ATP-binding cassette sub-family A member 13 5034 568,897 Alternative sequence (4); Chain (1); Domain (2); Erroneous initiation (1); Nucleotide binding (2); Sequence conflict (18); Transmembrane (14) TRANSMEM 23 43 Helical. {ECO:0000255}.; TRANSMEM 3536 3556 Helical. {ECO:0000255}.; TRANSMEM 3590 3610 Helical. {ECO:0000255}.; TRANSMEM 3616 3636 Helical. {ECO:0000255}.; TRANSMEM 3647 3667 Helical. {ECO:0000255}.; TRANSMEM 3677 3697 Helical. {ECO:0000255}.; TRANSMEM 3720 3740 Helical. {ECO:0000255}.; TRANSMEM 4206 4226 Helical. {ECO:0000255}.; TRANSMEM 4432 4452 Helical. {ECO:0000255}.; TRANSMEM 4478 4498 Helical. {ECO:0000255}.; TRANSMEM 4510 4530 Helical. {ECO:0000255}.; TRANSMEM 4540 4560 Helical. {ECO:0000255}.; TRANSMEM 4581 4601 Helical. {ECO:0000255}.; TRANSMEM 4625 4645 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Ubiquitously expressed. May be primarily expressed in kidney. {ECO:0000269|PubMed:12697998, ECO:0000269|PubMed:12706902}. +Q9QXM0 ABHD2_MOUSE Monoacylglycerol lipase ABHD2 (EC 3.1.1.23) (2-arachidonoylglycerol hydrolase) (Abhydrolase domain-containing protein 2) (Lung alpha/beta hydrolase 2) (MmLABH2) 425 48,378 Active site (3); Chain (1); Domain (1); Glycosylation (2); Sequence conflict (3); Topological domain (2); Transmembrane (1) TRANSMEM 10 30 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 9 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 31 425 Extracellular. {ECO:0000305}. FUNCTION: Progesterone-dependent acylglycerol lipase that catalyzes hydrolysis of endocannabinoid arachidonoylglycerol (AG) from cell membrane. Acts as a progesterone receptor: progesterone-binding activates the acylglycerol lipase activity, mediating degradation of 1-arachidonoylglycerol (1AG) and 2-arachidonoylglycerol (2AG) to glycerol and arachidonic acid (AA) (By similarity). Involved in acrosomal reaction (PubMed:26989199). May also play a role in smooth muscle cells migration (PubMed:15721306). {ECO:0000250|UniProtKB:P08910, ECO:0000269|PubMed:15721306, ECO:0000305|PubMed:26989199}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P08910}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P08910}. Cytoplasmic vesicle, secretory vesicle, acrosome membrane {ECO:0000269|PubMed:26989199}. Note=Absent from the sperm flagellum. {ECO:0000269|PubMed:26989199}. TISSUE SPECIFICITY: Widely expressed with higher expression in testis. Expressed by vascular smooth muscle cells, non vascular smooth muscle cells and heart. {ECO:0000269|PubMed:11922611, ECO:0000269|PubMed:15721306}. +Q80YU0 ABHGB_MOUSE Protein ABHD16B (EC 3.-.-.-) (Alpha/beta hydrolase domain-containing protein 16B) (Abhydrolase domain-containing protein 16B) 474 53,297 Active site (3); Chain (1); Compositional bias (2); Domain (1) +Q497M3 ABEC4_MOUSE Putative C->U-editing enzyme APOBEC-4 (EC 3.5.4.-) (Apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 4) 374 42,721 Active site (1); Chain (1); Domain (1); Metal binding (3); Sequence caution (1) FUNCTION: Putative C to U editing enzyme whose physiological substrate is not yet known. {ECO:0000250}. TISSUE SPECIFICITY: Predominantly expressed in testis. {ECO:0000269|PubMed:16082223}. +P61222 ABCE1_MOUSE ATP-binding cassette sub-family E member 1 (RNase L inhibitor) (Ribonuclease 4 inhibitor) (RNS4I) 599 67,314 Chain (1); Domain (4); Modified residue (2); Nucleotide binding (2); Sequence conflict (2) FUNCTION: Antagonizes the binding of 2-5A (5'-phosphorylated 2',5'-linked oligoadenylates) by RNase L through direct interaction with RNase L and therefore inhibits its endoribonuclease activity. May play a central role in the regulation of mRNA turnover. Antagonizes the anti-viral effect of the interferon-regulated 2-5A/RNase L pathway (By similarity). {ECO:0000250, ECO:0000269|PubMed:10866653}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Mitochondrion {ECO:0000250}. Note=Localized to clusters of virus formation at the plasma membrane. {ECO:0000250}. SUBUNIT: Probably heterodimerizes with RNASEL; this interaction inhibits the RNASEL. {ECO:0000250}. +Q80UX8 ABHDD_MOUSE Protein ABHD13 (EC 3.-.-.-) (Alpha/beta hydrolase domain-containing protein 13) (Abhydrolase domain-containing protein 13) 337 38,525 Active site (3); Chain (1); Erroneous initiation (1); Glycosylation (1); Transmembrane (1) TRANSMEM 37 57 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. +Q6P542 ABCF1_MOUSE ATP-binding cassette sub-family F member 1 837 94,945 Chain (1); Compositional bias (1); Domain (2); Modified residue (8); Nucleotide binding (2) FUNCTION: Required for efficient Cap- and IRES-mediated mRNA translation initiation. Not involved in the ribosome biogenesis (By similarity). {ECO:0000250}. PTM: Phosphorylated at phosphoserine and phosphothreonine. Phosphorylation on Ser-107 and Ser-138 by CK2; inhibits association of EIF2 with ribosomes (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8NE71}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q8NE71}. Nucleus envelope {ECO:0000250|UniProtKB:Q8NE71}. SUBUNIT: Interacts (via N-terminus) with EIF2S1; the interaction is independent of its phosphorylated status. Associates (via both ABC transporter domains) with the ribosomes (By similarity). {ECO:0000250}. +Q8BPZ8 ABRX1_MOUSE BRCA1-A complex subunit Abraxas 1 (Coiled-coil domain-containing protein 98) (Protein FAM175A) 407 46,039 Alternative sequence (2); Chain (1); Coiled coil (1); Compositional bias (1); Domain (1); Erroneous initiation (2); Frameshift (1); Modified residue (5); Motif (1); Sequence conflict (3) FUNCTION: Involved in DNA damage response and double-strand break (DSB) repair. Component of the BRCA1-A complex, acting as a central scaffold protein that assembles the various components of the complex and mediates the recruitment of BRCA1. The BRCA1-A complex specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesion sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at DSBs. This complex also possesses deubiquitinase activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. {ECO:0000250|UniProtKB:Q6UWZ7}. PTM: Phosphorylation of Ser-404 of the pSXXF motif by ATM or ATR constitutes a specific recognition motif for the BRCT domain of BRCA1. {ECO:0000250|UniProtKB:Q6UWZ7}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6UWZ7}. Note=Localizes at sites of DNA damage at double-strand breaks (DSBs). {ECO:0000250|UniProtKB:Q6UWZ7}. SUBUNIT: Component of the ARISC complex, at least composed of UIMC1/RAP80, ABRAXAS1, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1. Component of the BRCA1-A complex, at least composed of the BRCA1, BARD1, UIMC1/RAP80, ABRAXAS1, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1. In the complex, interacts directly with UIMC1/RAP80, BRCC3/BRCC36 and BABAM2. Homodimer. Interacts directly (when phosphorylated at Ser-404) with BRCA1. The phosphorylated homodimer can interact directly with two BRCA1 chains, giving rise to a heterotetramer. Binds polyubiquitin. {ECO:0000250|UniProtKB:Q6UWZ7}. +Q3TCJ1 ABRX2_MOUSE BRISC complex subunit Abraxas 2 (Abraxas brother protein 1) (Protein FAM175B) 415 46,943 Chain (1); Coiled coil (1); Domain (1); Modified residue (5); Region (2) FUNCTION: Component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked polyubiquitin, leaving the last ubiquitin chain attached to its substrates. May act as a central scaffold protein that assembles the various components of the BRISC complex and retains them in the cytoplasm (By similarity). Plays a role in regulating the onset of apoptosis via its role in modulating 'Lys-63'-linked ubiquitination of target proteins (PubMed:21195082). Required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating NUMA1. Plays a role in interferon signaling via its role in the deubiquitination of the interferon receptor IFNAR1; deubiquitination increases IFNAR1 activities by enhancing its stability and cell surface expression (PubMed:24075985, PubMed:26344097). Down-regulates the response to bacterial lipopolysaccharide (LPS) via its role in IFNAR1 deubiquitination (PubMed:24075985). Required for normal induction of p53/TP53 in response to DNA damage. Independent of the BRISC complex, promotes interaction between USP7 and p53/TP53, and thereby promotes deubiquitination of p53/TP53, preventing its degradation and resulting in increased p53/TP53-mediated transcription regulation and p53/TP53-dependent apoptosis in response to DNA damage (By similarity). {ECO:0000250|UniProtKB:Q15018, ECO:0000269|PubMed:24075985, ECO:0000269|PubMed:26344097, ECO:0000305|PubMed:21195082}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q15018}. Nucleus {ECO:0000250|UniProtKB:Q15018}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q15018}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q15018}. Note=A minor proportion is detected in the nucleus. Translocates into the nucleus in response to DNA damage. Directly binds to microtubules and is detected at the minus end of K-fibers. Co-localizes with NUMA1 at mitotic spindle poles. {ECO:0000250|UniProtKB:Q15018}. SUBUNIT: Component of the BRISC complex, at least composed of ABRAXAS2, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1. Interacts with BRCC3/BRCC36; the interaction is direct. Interacts with BABAM1. Does not interact with BRCA1. Interacts with SHMT1 and SHMT2; the interaction is direct. Identified in a complex with SHMT2 and the other subunits of the BRISC complex. The BRISC complex binds monoubiquitin and both 'Lys-48'- and 'Lys-63'-linked polyubiquitin. Identified in complexes with IFNAR1, IFNAR2 and SHMT2. Interacts with THAP5 (By similarity). Interacts with ATF4 (PubMed:22974638). Identified in a complex with p53/TP53 and USP7; interacts directly with both proteins. Interacts with NUMA1. Interacts with microtubule minus ends. Binds polyubiquitin (By similarity). {ECO:0000250|UniProtKB:Q15018, ECO:0000269|PubMed:22974638}. TISSUE SPECIFICITY: Detected in heart (at protein level). {ECO:0000269|PubMed:21195082}. +Q9QYL7 ABT1_MOUSE Activator of basal transcription 1 269 30,659 Chain (1); Coiled coil (2); Compositional bias (3); Domain (1); Sequence conflict (2) FUNCTION: Could be a novel TATA-binding protein (TBP) which can function as a basal transcription activator. Can act as a regulator of basal transcription for class II genes. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10648625}. Nucleus, nucleolus {ECO:0000269|PubMed:10648625}. SUBUNIT: Interacts with ESF1/ABTAP. Interacts with IGHMBP2. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:10648625}. +Q91X60 ACHA2_MOUSE Neuronal acetylcholine receptor subunit alpha-2 512 58,735 Chain (1); Compositional bias (1); Disulfide bond (2); Glycosylation (3); Signal peptide (1); Topological domain (2); Transmembrane (4) TRANSMEM 242 266 Helical. {ECO:0000255}.; TRANSMEM 274 292 Helical. {ECO:0000255}.; TRANSMEM 308 329 Helical. {ECO:0000255}.; TRANSMEM 486 504 Helical. {ECO:0000255}. TOPO_DOM 28 241 Extracellular. {ECO:0000255}.; TOPO_DOM 330 485 Cytoplasmic. {ECO:0000255}. FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Neuronal AChR seems to be composed of two different types of subunits: alpha and non-alpha (beta). Alpha-2 subunit can be combined to beta-2 or beta-4 to give rise to functional receptors. The alpha-2:beta-2 nAChR complex is proposed to be a heteropentamer with two subtypes: LS (low agonist sensitivity) with a (alpha-2)3:(beta-2)2 and HS (high agonist sensitivity) with a (alpha-2)2:(beta-2)3 stoichiometry; the subtypes differ in their subunit binding interfaces which are involved in ligand binding (By similarity). {ECO:0000250|UniProtKB:Q15822}. +P13011 ACOD2_MOUSE Acyl-CoA desaturase 2 (EC 1.14.19.1) (Delta(9)-desaturase 2) (Delta-9 desaturase 2) (Fatty acid desaturase 2) (Stearoyl-CoA desaturase 2) 358 40,916 Binding site (7); Chain (1); Metal binding (9); Motif (3); Sequence conflict (2); Topological domain (5); Transmembrane (4) TRANSMEM 72 92 Helical. {ECO:0000250|UniProtKB:O00767}.; TRANSMEM 97 117 Helical. {ECO:0000250|UniProtKB:O00767}.; TRANSMEM 217 236 Helical. {ECO:0000250|UniProtKB:O00767}.; TRANSMEM 241 262 Helical. {ECO:0000250|UniProtKB:O00767}. TOPO_DOM 1 71 Cytoplasmic. {ECO:0000250|UniProtKB:P13516}.; TOPO_DOM 93 96 Lumenal. {ECO:0000250|UniProtKB:P13516}.; TOPO_DOM 118 216 Cytoplasmic. {ECO:0000250|UniProtKB:P13516}.; TOPO_DOM 237 240 Lumenal. {ECO:0000250|UniProtKB:P13516}.; TOPO_DOM 263 358 Cytoplasmic. {ECO:0000250|UniProtKB:P13516}. FUNCTION: Stearyl-CoA desaturase that utilizes O(2) and electrons from reduced cytochrome b5 to introduce the first double bond into saturated fatty acyl-CoA substrates (PubMed:16443825). Catalyzes the insertion of a cis double bond at the delta-9 position into fatty acyl-CoA substrates including palmitoyl-CoA and stearoyl-CoA (PubMed:16443825). Gives rise to a mixture of 16:1 and 18:1 unsaturated fatty acids (PubMed:16443825). Contributes to the biosynthesis of membrane phospholipids, cholesterol esters and triglycerides, especially during embryonic development and in neonates (PubMed:16118274). Important for normal permeability barrier function of the skin in neonates (PubMed:16118274). {ECO:0000269|PubMed:16118274, ECO:0000269|PubMed:16443825}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305|PubMed:16443825}; Multi-pass membrane protein {ECO:0000305|PubMed:16443825}. Microsome membrane {ECO:0000269|PubMed:16443825}. DOMAIN: The histidine box domains are involved in binding the catalytic metal ions. {ECO:0000250|UniProtKB:O00767}. TISSUE SPECIFICITY: Detected in brain and skin (PubMed:10545940, PubMed:11161812, PubMed:16118274). Highly expressed in brain, and detected at low levels in heart, stomach, lung and testis (PubMed:11161812, PubMed:12815040). Detected both in dermis and epidermis (PubMed:16118274). {ECO:0000269|PubMed:10545940, ECO:0000269|PubMed:12815040, ECO:0000269|PubMed:16118274}. +P83855 ACLP_MOUSE Putative sperm adenylate cyclase (EC 4.6.1.1) (Fragment) 21 2,502 Chain (1); Non-terminal residue (1) +Q99KI0 ACON_MOUSE Aconitate hydratase, mitochondrial (Aconitase) (EC 4.2.1.3) (Citrate hydro-lyase) 780 85,464 Binding site (4); Chain (1); Metal binding (3); Modified residue (32); Region (2); Sequence conflict (3); Transit peptide (1) Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 2/2. FUNCTION: Catalyzes the isomerization of citrate to isocitrate via cis-aconitate. {ECO:0000250|UniProtKB:P16276}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P16276}. SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P16276}. +O55137 ACOT1_MOUSE Acyl-coenzyme A thioesterase 1 (Acyl-CoA thioesterase 1) (EC 3.1.2.2) (CTE-I) (Inducible cytosolic acyl-coenzyme A thioester hydrolase) (Long chain acyl-CoA thioester hydrolase) (Long chain acyl-CoA hydrolase) 419 46,136 Active site (3); Chain (1); Modified residue (1); Mutagenesis (4) FUNCTION: Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. True acyl-CoA thioesterase being highly specific for saturated C12-C20 acyl-CoAs, with only a very low activity with decanoyl-CoA as substrate. Most active on myristoyl- and palmitoyl-CoA. Introduction of one or two double bonds decreases the activity to about half. No detectable activity with bile acid CoAs such as choloyl-CoA and chenodeoxycholoyl-CoA. {ECO:0000269|PubMed:10567408}. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Monomer. TISSUE SPECIFICITY: Expressed in heart, kidney, brown adipose tissue, white adipose tissue, adrenal gland and muscle. {ECO:0000269|PubMed:10567408, ECO:0000269|PubMed:11330065}. +Q6Q2Z6 ACOT5_MOUSE Acyl-coenzyme A thioesterase 5 (Acyl-CoA thioesterase 5) (EC 3.1.2.2) (Peroxisomal acyl-coenzyme A thioester hydrolase Ic) (Peroxisomal acyl-CoA thioesterase Ic) 421 46,573 Active site (3); Chain (1); Motif (1); Sequence conflict (1) FUNCTION: Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Seems to be involved in intraperoxisomal regulation of acyl-CoA levels, but not CoASH levels. Mainly active on medium-chain acyl-CoAs. May have a function in termination of beta-oxidation of fatty acids. {ECO:0000269|PubMed:15007068}. SUBCELLULAR LOCATION: Peroxisome. TISSUE SPECIFICITY: Highly expressed in spleen, brain, testis and proximal and distal intestine; expressed at low level in the liver. {ECO:0000269|PubMed:15007068}. +Q06649 3BP2_MOUSE SH3 domain-binding protein 2 (3BP-2) 559 62,208 Chain (1); Compositional bias (2); Domain (2); Modified residue (6); Motif (1) FUNCTION: Binds differentially to the SH3 domains of certain proteins of signal transduction pathways. Binds to phosphatidylinositols; linking the hemopoietic tyrosine kinase fes to the cytoplasmic membrane in a phosphorylation dependent mechanism (By similarity). {ECO:0000250}. PTM: Phosphorylated. Phosphorylation at Tyr-446 may stimulate the activity of the LYN kinase. {ECO:0000269|PubMed:12709437}. +Q6KAU8 A16L2_MOUSE Autophagy-related protein 16-2 (APG16-like 2) 623 69,241 Alternative sequence (2); Chain (1); Coiled coil (1); Erroneous initiation (1); Repeat (7); Sequence caution (1) FUNCTION: May play a role in autophagy. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Localizes also to discrete punctae along the ciliary axoneme. {ECO:0000269|PubMed:24089209}. +P97288 5HT4R_MOUSE 5-hydroxytryptamine receptor 4 (5-HT-4) (5-HT4) (Serotonin receptor 4) 388 43,962 Alternative sequence (3); Chain (1); Disulfide bond (1); Glycosylation (1); Lipidation (1); Sequence conflict (1); Topological domain (8); Transmembrane (7) TRANSMEM 20 40 Helical; Name=1. {ECO:0000250}.; TRANSMEM 59 79 Helical; Name=2. {ECO:0000250}.; TRANSMEM 94 116 Helical; Name=3. {ECO:0000250}.; TRANSMEM 138 158 Helical; Name=4. {ECO:0000250}.; TRANSMEM 193 213 Helical; Name=5. {ECO:0000250}.; TRANSMEM 261 281 Helical; Name=6. {ECO:0000250}.; TRANSMEM 295 315 Helical; Name=7. {ECO:0000250}. TOPO_DOM 1 19 Extracellular. {ECO:0000250}.; TOPO_DOM 41 58 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 80 93 Extracellular. {ECO:0000250}.; TOPO_DOM 117 137 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 159 192 Extracellular. {ECO:0000250}.; TOPO_DOM 214 260 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 282 294 Extracellular. {ECO:0000250}.; TOPO_DOM 316 388 Cytoplasmic. {ECO:0000250}. FUNCTION: This is one of the several different receptors for 5-hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. The activity of this receptor is mediated by G proteins that stimulate adenylate cyclase (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Endosome. Note=Interaction with SNX27 mediates recruitment to early endosomes, while interaction with SLC9A3R1 and EZR might target the protein to specialized subcellular regions, such as microvilli. SUBUNIT: Isoform 5-HT4(A) interacts with MAGI2, MPP3, SLC9A3R1 and SNX27 isoforms 1 and 2. Isoform 5-HT4(E) interacts with PATJ, NOS1 and SEC23A. Isoform 5-HT4(A) forms a complex including SLC9A3R1 and EZR. Interacts (via C-terminus 330-346 AA) with GRK5; this interaction is promoted by 5-HT (serotonin) (By similarity). {ECO:0000250}. +P51912 AAAT_MOUSE Neutral amino acid transporter B(0) (ATB(0)) (ASC-like Na(+)-dependent neutral amino acid transporter ASCT2) (Insulin-activated amino acid transporter) (Sodium-dependent neutral amino acid transporter type 2) (Solute carrier family 1 member 5) 553 58,483 Chain (1); Glycosylation (2); Intramembrane (2); Metal binding (5); Modified residue (6); Sequence conflict (3); Topological domain (11); Transmembrane (8) INTRAMEM 346 376 Discontinuously helical. {ECO:0000250|UniProtKB:P43003}.; INTRAMEM 426 459 Discontinuously helical. {ECO:0000250|UniProtKB:P43003}. TRANSMEM 51 80 Helical; Name=1. {ECO:0000250|UniProtKB:P43003}.; TRANSMEM 94 115 Helical; Name=2. {ECO:0000250|UniProtKB:P43003}.; TRANSMEM 130 152 Helical; Name=3. {ECO:0000250|UniProtKB:P43003}.; TRANSMEM 237 260 Helical; Name=4. {ECO:0000250|UniProtKB:P43003}.; TRANSMEM 270 297 Helical; Name=5. {ECO:0000250|UniProtKB:P43003}.; TRANSMEM 319 340 Helical; Name=6. {ECO:0000250|UniProtKB:P43003}.; TRANSMEM 386 412 Helical; Name=7. {ECO:0000250|UniProtKB:P43003}.; TRANSMEM 473 494 Helical; Name=8. {ECO:0000250|UniProtKB:P43003}. TOPO_DOM 1 50 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 81 93 Extracellular. {ECO:0000305}.; TOPO_DOM 116 129 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 153 236 Extracellular. {ECO:0000305}.; TOPO_DOM 261 269 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 298 318 Extracellular. {ECO:0000305}.; TOPO_DOM 341 345 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 377 385 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 413 425 Extracellular. {ECO:0000305}.; TOPO_DOM 460 472 Extracellular. {ECO:0000305}.; TOPO_DOM 495 553 Cytoplasmic. {ECO:0000305}. FUNCTION: Sodium-dependent amino acids transporter that has a broad substrate specificity, with a preference for zwitterionic amino acids. It accepts as substrates all neutral amino acids, including glutamine, asparagine, and branched-chain and aromatic amino acids, and excludes methylated, anionic, and cationic amino acids. {ECO:0000269|PubMed:7702599, ECO:0000269|PubMed:8662767}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7702599, ECO:0000269|PubMed:8662767}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q15758}. Melanosome {ECO:0000250|UniProtKB:Q15758}. SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:Q15758}. TISSUE SPECIFICITY: Highly expressed in adipose tissue, lower levels seen in lung. Not expressed in brain, kidney, liver or heart and only traces are detected in spleen, thymus and skeletal muscle. +E9PX95 ABCAH_MOUSE ATP-binding cassette sub-family A member 17 1733 196,020 Chain (1); Compositional bias (1); Domain (2); Glycosylation (1); Nucleotide binding (2); Sequence conflict (12); Transmembrane (14) TRANSMEM 22 42 Helical. {ECO:0000255}.; TRANSMEM 262 282 Helical. {ECO:0000255}.; TRANSMEM 306 326 Helical. {ECO:0000255}.; TRANSMEM 342 362 Helical. {ECO:0000255}.; TRANSMEM 372 392 Helical. {ECO:0000255}.; TRANSMEM 403 423 Helical. {ECO:0000255}.; TRANSMEM 444 464 Helical. {ECO:0000255}.; TRANSMEM 906 926 Helical. {ECO:0000255}.; TRANSMEM 1082 1102 Helical. {ECO:0000255}.; TRANSMEM 1128 1148 Helical. {ECO:0000255}.; TRANSMEM 1160 1180 Helical. {ECO:0000255}.; TRANSMEM 1192 1212 Helical. {ECO:0000255}.; TRANSMEM 1230 1250 Helical. {ECO:0000255}.; TRANSMEM 1287 1307 Helical. {ECO:0000255}. FUNCTION: Promotes cholesterol efflux from sperm which renders sperm capable of fertilization (PubMed:22237709). Has also been shown to decrease levels of intracellular esterified neutral lipids including cholesteryl esters, fatty acid esters and triacylglycerols (PubMed:15810880). {ECO:0000269|PubMed:15810880, ECO:0000269|PubMed:22237709}. PTM: N-glycosylated. {ECO:0000269|PubMed:15810880}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15810880}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:22237709}. TISSUE SPECIFICITY: In the testis, detected predominantly in elongated spermatids at the late stage of germ cell development and in sperm, with no expression detected in immature germ cells such as spermatogonia and spermatocytes or in somatic cells such as Sertoli cells (at protein level) (PubMed:15810880). Expressed in the head and tail midpiece of elongated spermatids and sperm (at protein level) (PubMed:22237709). Expressed exclusively in the testis (PubMed:15810880, PubMed:22237709). {ECO:0000269|PubMed:15810880, ECO:0000269|PubMed:22237709}. +Q99LJ2 ABTB1_MOUSE Ankyrin repeat and BTB/POZ domain-containing protein 1 478 54,058 Chain (1); Coiled coil (1); Domain (2); Repeat (2); Sequence conflict (2) FUNCTION: May act as a mediator of the PTEN growth-suppressive signaling pathway. May play a role in developmental processes (By similarity). {ECO:0000250|UniProtKB:Q969K4}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q969K4}. +Q99PE8 ABCG5_MOUSE ATP-binding cassette sub-family G member 5 (Sterolin-1) 652 73,244 Chain (1); Domain (2); Glycosylation (3); Lipidation (1); Mutagenesis (10); Natural variant (1); Nucleotide binding (1); Topological domain (7); Transmembrane (6) TRANSMEM 385 405 Helical; Name=1. {ECO:0000250|UniProtKB:Q9H222}.; TRANSMEM 423 443 Helical; Name=2. {ECO:0000250|UniProtKB:Q9H222}.; TRANSMEM 469 490 Helical; Name=3. {ECO:0000250|UniProtKB:Q9H222}.; TRANSMEM 502 522 Helical; Name=4. {ECO:0000250|UniProtKB:Q9H222}.; TRANSMEM 530 550 Helical; Name=5. {ECO:0000250|UniProtKB:Q9H222}.; TRANSMEM 625 645 Helical; Name=6. {ECO:0000250|UniProtKB:Q9H222}. TOPO_DOM 1 384 Cytoplasmic. {ECO:0000250|UniProtKB:Q9H222}.; TOPO_DOM 406 422 Extracellular. {ECO:0000250|UniProtKB:Q9H222}.; TOPO_DOM 444 468 Cytoplasmic. {ECO:0000250|UniProtKB:Q9H222}.; TOPO_DOM 491 501 Extracellular. {ECO:0000250|UniProtKB:Q9H222}.; TOPO_DOM 523 529 Cytoplasmic. {ECO:0000250|UniProtKB:Q9H222}.; TOPO_DOM 551 624 Extracellular. {ECO:0000250|UniProtKB:Q9H222}.; TOPO_DOM 646 652 Cytoplasmic. {ECO:0000250|UniProtKB:Q9H222}. FUNCTION: ABCG5 and ABCG8 form an obligate heterodimer that mediates Mg(2+)- and ATP-dependent sterol transport across the cell membrane (PubMed:16352607, PubMed:16867993, PubMed:18402465). Plays an essential role in the selective transport of dietary plant sterols and cholesterol in and out of the enterocytes and in the selective sterol excretion by the liver into bile (PubMed:12444248, PubMed:14504269, PubMed:14657202, PubMed:19846887, PubMed:25378657). Required for normal sterol homeostasis (PubMed:12444248, PubMed:14657202). The heterodimer with ABCG8 has ATPase activity (PubMed:16352607, PubMed:16867993). {ECO:0000269|PubMed:12444248, ECO:0000269|PubMed:14504269, ECO:0000269|PubMed:14657202, ECO:0000269|PubMed:16352607, ECO:0000269|PubMed:16867993, ECO:0000269|PubMed:18402465, ECO:0000269|PubMed:19846887, ECO:0000269|PubMed:25378657}. PTM: N-glycosylated (PubMed:12208867, PubMed:12444248, PubMed:16867993, PubMed:15040800, PubMed:15054092, PubMed:18402465, PubMed:25378657). N-glycosylation is important for efficient export out of the endoplasmic reticulum (PubMed:15054092). {ECO:0000269|PubMed:12208867, ECO:0000269|PubMed:12444248, ECO:0000269|PubMed:15040800, ECO:0000269|PubMed:15054092, ECO:0000269|PubMed:16867993, ECO:0000269|PubMed:18402465, ECO:0000269|PubMed:25378657}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12208867, ECO:0000269|PubMed:18402465, ECO:0000305|PubMed:16352607}; Multi-pass membrane protein {ECO:0000305}. Apical cell membrane {ECO:0000269|PubMed:12208867, ECO:0000269|PubMed:14504269, ECO:0000269|PubMed:15040800, ECO:0000269|PubMed:16867993, ECO:0000269|PubMed:18402465}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Heterodimer with ABCG8. {ECO:0000269|PubMed:12208867, ECO:0000269|PubMed:14504269, ECO:0000269|PubMed:15054092, ECO:0000269|PubMed:16352607, ECO:0000269|PubMed:16867993, ECO:0000269|PubMed:18402465}. DOMAIN: The Walker motif (consensus sequence G-X-X-G-X-G-K-[ST]-T) is expected to bind ATP. Within this motif, the conserved Lys is essential for transport activity mediated by the heterodimer with ABCG8. {ECO:0000269|PubMed:16352607}. TISSUE SPECIFICITY: Detected in liver and jejunum (PubMed:12444248, PubMed:15040800, PubMed:18402465, PubMed:25378657). Detected on enterocyte villi (at protein level) (PubMed:15040800). Expressed in jejunum, ileum and, at lower level, in the liver (PubMed:11138003, PubMed:11907139, PubMed:11099417, PubMed:12444248, PubMed:25378657). {ECO:0000269|PubMed:11099417, ECO:0000269|PubMed:11138003, ECO:0000269|PubMed:11907139, ECO:0000269|PubMed:12444248, ECO:0000269|PubMed:15040800, ECO:0000269|PubMed:18402465, ECO:0000269|PubMed:25378657}. DISEASE: Note=A spontaneous mutation gives raise to thrombocytopenia and cardiomyopathy (trac), with recessive inheritance and fully penetrant phenotype. Mice are small, infertile, and have shortened lifespan. {ECO:0000269|PubMed:19846887}. +Q99JW1 AB17A_MOUSE Alpha/beta hydrolase domain-containing protein 17A (Abhydrolase domain-containing protein 17A) (EC 3.1.2.22) 310 33,950 Active site (3); Alternative sequence (1); Chain (1); Erroneous initiation (1); Modified residue (1) FUNCTION: Hydrolyzes fatty acids from S-acylated cysteine residues in proteins. Has depalmitoylating activity towards NRAS. Has depalmitoylating activity towards DLG4/PSD95. May have depalmitoylating activity towars MAP6. {ECO:0000250|UniProtKB:Q5XIJ5, ECO:0000250|UniProtKB:Q96GS6}. PTM: Palmitoylated on cysteine residues located in a cysteine cluster at the N-terminus which promotes membrane localization. Palmitoylation is required for post-synaptic localization and for depalmitoylating activity towards DLG4/PSD95. {ECO:0000250|UniProtKB:Q7M759}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q96GS6}; Lipid-anchor {ECO:0000250|UniProtKB:Q96GS6}; Cytoplasmic side {ECO:0000250|UniProtKB:Q96GS6}. Endosome membrane {ECO:0000250|UniProtKB:Q96GS6}; Lipid-anchor {ECO:0000250|UniProtKB:Q96GS6}; Cytoplasmic side {ECO:0000250|UniProtKB:Q96GS6}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:Q5XIJ5}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250|UniProtKB:Q5XIJ5}. +Q8JZN5 ACAD9_MOUSE Acyl-CoA dehydrogenase family member 9, mitochondrial (ACAD-9) (EC 1.3.99.-) 625 68,722 Active site (1); Chain (1); Modified residue (6); Sequence conflict (8); Transit peptide (1) FUNCTION: Required for mitochondrial complex I assembly (By similarity). Has a dehydrogenase activity on palmitoyl-CoA (C16:0) and stearoyl-CoA (C18:0). It is three times more active on palmitoyl-CoA then on stearoyl-CoA. However, it does not play a primary role in long-chain fatty acid oxidation (By similarity). Has little activity on octanoyl-CoA (C8:0), butyryl-CoA (C4:0) or isovaleryl-CoA (5:0) (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9H845}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9H845}. SUBUNIT: Part of the mitochondrial complex I assembly (MCIA) complex. The complex comprises at least TMEM126B, NDUFAF1, ECSIT, and ACAD9 (By similarity). Interacts with NDUFAF1 and ECSIT (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9H845}. +Q07417 ACADS_MOUSE Short-chain specific acyl-CoA dehydrogenase, mitochondrial (SCAD) (EC 1.3.8.1) (Butyryl-CoA dehydrogenase) 412 44,890 Active site (1); Binding site (5); Chain (1); Modified residue (12); Nucleotide binding (4); Region (1); Sequence conflict (3); Transit peptide (1) Lipid metabolism; mitochondrial fatty acid beta-oxidation. FUNCTION: Introduces a double bond at position 2 in saturated acyl-CoA's of short chain length, i.e. less than 6 carbon atoms. {ECO:0000250|UniProtKB:P15651}. SUBCELLULAR LOCATION: Mitochondrion matrix. SUBUNIT: Homotetramer. +Q5EE38 ACD_MOUSE Adrenocortical dysplasia protein 416 44,713 Alternative sequence (9); Chain (1); Compositional bias (1); Cross-link (1); Modified residue (3); Motif (1); Region (1); Sequence conflict (2) FUNCTION: Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded TTAGGG repeats added by telomerase and protects chromosome ends. Without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways. Promotes binding of POT1 to single-stranded telomeric DNA. Modulates the inhibitory effects of POT1 on telomere elongation. The ACD-POT1 heterodimer enhances telomere elongation by recruiting telomerase to telomeres and increasing its processivity (By similarity). May play a role in organogenesis (PubMed:15537664). {ECO:0000250|UniProtKB:Q96AP0, ECO:0000269|PubMed:15537664}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96AP0}. Chromosome, telomere {ECO:0000250|UniProtKB:Q96AP0}. SUBUNIT: Component of the shelterin complex (telosome) composed of TERF1, TERF2, TINF2, TERF2IP ACD and POT1. Forms heterodimers with POT1. Identified in a complex with POT1 and single-stranded telomeric DNA. Interacts with STN1 and TINF2. {ECO:0000250|UniProtKB:Q96AP0, ECO:0000269|PubMed:19648609}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15537664}. DISEASE: Note=Defects in Acd are the cause of adrenocortical dysplasia (ACD). ACD is a spontaneous autosomal recessive mouse mutant resulting from spontaneous splicing mutation of acd. ACD mice are characterized by developmental defects in organs derived from the urogenital ridge, reduced survival, poor growth, skin hyperpigmentation and adrenal insufficiency. Forty percent of the mutants died within 24 hours. Analysis of E14.5 to E17.5 embryos revealed reduced formation of caudal structure as well as limb defects. +Q8R493 ACHB4_MOUSE Neuronal acetylcholine receptor subunit beta-4 495 55,809 Chain (1); Disulfide bond (1); Glycosylation (4); Signal peptide (1); Site (3); Topological domain (5); Transmembrane (4) TRANSMEM 236 256 Helical. {ECO:0000255}.; TRANSMEM 265 285 Helical. {ECO:0000255}.; TRANSMEM 298 318 Helical. {ECO:0000255}.; TRANSMEM 464 484 Helical. {ECO:0000255}. TOPO_DOM 21 235 Extracellular. {ECO:0000255}.; TOPO_DOM 257 264 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 286 297 Extracellular. {ECO:0000255}.; TOPO_DOM 319 463 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 485 495 Extracellular. {ECO:0000255}. FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Neuronal AChR is composed of two different types of subunits: alpha and beta. Beta-4 subunit can be combined to alpha-2, alpha-3 or alpha-4 to give rise to functional receptors. Interacts with RIC3; which is required for proper folding and assembly. Interacts with LYPD6. The pentamer alpha3-beta-4 interacts with the conotoxin BuIA. The heteropentamer composed of alpha-3 and beta-4 subunits interacts with the alpha-conotoxin ImI (By similarity). {ECO:0000250|UniProtKB:P12392, ECO:0000250|UniProtKB:P30926}. TISSUE SPECIFICITY: Predominantly expressed by immature T-cells in the thymus. {ECO:0000269|PubMed:12225896}. +Q99LH9 3BP5L_MOUSE SH3 domain-binding protein 5-like (SH3BP-5-like) 392 43,374 Chain (1); Coiled coil (2); Compositional bias (1); Modified residue (8); Sequence conflict (3) FUNCTION: Functions as guanine nucleotide exchange factor (GEF) for RAB11A. {ECO:0000250|UniProtKB:Q7L8J4}. +Q9JHJ5 5HT3B_MOUSE 5-hydroxytryptamine receptor 3B (5-HT3-B) (5-HT3B) (Serotonin receptor 3B) 437 50,321 Chain (1); Disulfide bond (1); Glycosylation (4); Region (1); Signal peptide (1); Topological domain (5); Transmembrane (4) TRANSMEM 239 259 Helical; Name=1. {ECO:0000255}.; TRANSMEM 265 282 Helical; Name=2. {ECO:0000255}.; TRANSMEM 293 313 Helical; Name=3. {ECO:0000255}.; TRANSMEM 411 431 Helical; Name=4. {ECO:0000255}. TOPO_DOM 22 238 Extracellular. {ECO:0000255}.; TOPO_DOM 260 264 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 283 292 Extracellular. {ECO:0000255}.; TOPO_DOM 314 410 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 432 437 Extracellular. {ECO:0000255}. FUNCTION: This is one of the several different receptors for 5-hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. This receptor is a ligand-gated ion channel, which when activated causes fast, depolarizing responses. It is a cation-specific, but otherwise relatively nonselective, ion channel. {ECO:0000269|PubMed:12867984}. PTM: N-glycosylation is required for membrane localization. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Note=Presumably retained within the endoplasmic reticulum unless complexed with HTR3A. {ECO:0000250}. SUBUNIT: Forms a pentaheteromeric complex with HTR3A. Not functional as a homomeric complex (By similarity). {ECO:0000250}. +Q61503 5NTD_MOUSE 5'-nucleotidase (5'-NT) (EC 3.1.3.5) (Ecto-5'-nucleotidase) (CD antigen CD73) 576 63,864 Binding site (5); Chain (1); Disulfide bond (4); Glycosylation (4); Lipidation (1); Metal binding (7); Propeptide (1); Region (1); Signal peptide (1); Site (2) FUNCTION: Hydrolyzes extracellular nucleotides into membrane permeable nucleosides. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +Q9DCD0 6PGD_MOUSE 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44) 483 53,247 Active site (2); Binding site (7); Chain (1); Modified residue (4); Nucleotide binding (4); Region (2) Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 3/3. FUNCTION: Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +Q8R2R3 AAGAB_MOUSE Alpha- and gamma-adaptin-binding protein p34 316 34,511 Chain (1); Modified residue (2); Sequence conflict (1) FUNCTION: May be involved in endocytic recycling of growth factor receptors such as EGFR. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. SUBUNIT: Associated with AP-1 and AP-2 complexes. {ECO:0000250}. +Q9WVM8 AADAT_MOUSE Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial (KAT/AadAT) (2-aminoadipate aminotransferase) (2-aminoadipate transaminase) (EC 2.6.1.39) (Alpha-aminoadipate aminotransferase) (AadAT) (Kynurenine aminotransferase II) (Kynurenine--oxoglutarate aminotransferase II) (Kynurenine--oxoglutarate transaminase 2) (EC 2.6.1.7) (Kynurenine--oxoglutarate transaminase II) 425 47,598 Binding site (4); Chain (1); Modified residue (13); Transit peptide (1) Amino-acid degradation; L-lysine degradation via saccharopine pathway; glutaryl-CoA from L-lysine: step 4/6. FUNCTION: Transaminase with broad substrate specificity. Has transaminase activity towards aminoadipate, kynurenine, methionine and glutamate. Shows activity also towards tryptophan, aspartate and hydroxykynurenine. Accepts a variety of oxo-acids as amino-group acceptors, with a preference for 2-oxoglutarate, 2-oxocaproic acid, phenylpyruvate and alpha-oxo-gamma-methiol butyric acid. Can also use glyoxylate as amino-group acceptor (in vitro) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}. SUBUNIT: Homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Expressed mainly in kidney and to a lesser amount in liver and brain. {ECO:0000269|PubMed:10441733}. +Q99LR1 ABD12_MOUSE Monoacylglycerol lipase ABHD12 (EC 3.1.1.23) (2-arachidonoylglycerol hydrolase) (Abhydrolase domain-containing protein 12) 398 45,270 Active site (3); Alternative sequence (1); Chain (1); Compositional bias (2); Erroneous initiation (1); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 75 95 Helical. {ECO:0000269|PubMed:18096503}. TOPO_DOM 1 74 Cytoplasmic. {ECO:0000269|PubMed:18096503}.; TOPO_DOM 96 398 Extracellular. {ECO:0000269|PubMed:18096503}. FUNCTION: Lysophosphatidylserine (LPS) lipase that plays a key role in the central nervous system. Represents a major LPS lipase in the brain (PubMed:23297193). May also have a 2-arachidonoylglycerol (2-AG) hydrolase activity and act as a regulator of endocannabinoid signaling pathways (PubMed:18096503). {ECO:0000269|PubMed:18096503, ECO:0000269|PubMed:23297193}. PTM: Glycosylated. {ECO:0000269|PubMed:18096503}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:18096503}; Single-pass membrane protein {ECO:0000269|PubMed:18096503}. Mitochondrion {ECO:0000269|PubMed:20657592}. +Q4KML4 ABRAL_MOUSE Costars family protein ABRACL (ABRA C-terminal-like protein) 81 9,030 Chain (1); Erroneous initiation (1); Modified residue (1) +P41234 ABCA2_MOUSE ATP-binding cassette sub-family A member 2 (ATP-binding cassette transporter 2) (ATP-binding cassette 2) 2434 270,509 Chain (1); Domain (2); Glycosylation (25); Modified residue (5); Nucleotide binding (2); Transmembrane (13) TRANSMEM 22 42 Helical. {ECO:0000255}.; TRANSMEM 54 74 Helical. {ECO:0000255}.; TRANSMEM 698 718 Helical. {ECO:0000255}.; TRANSMEM 749 769 Helical. {ECO:0000255}.; TRANSMEM 781 801 Helical. {ECO:0000255}.; TRANSMEM 812 832 Helical. {ECO:0000255}.; TRANSMEM 893 913 Helical. {ECO:0000255}.; TRANSMEM 1461 1481 Helical. {ECO:0000255}.; TRANSMEM 1793 1813 Helical. {ECO:0000255}.; TRANSMEM 1842 1862 Helical. {ECO:0000255}.; TRANSMEM 1873 1893 Helical. {ECO:0000255}.; TRANSMEM 1906 1926 Helical. {ECO:0000255}.; TRANSMEM 1992 2012 Helical. {ECO:0000255}. FUNCTION: Probable transporter, its natural substrate has not been found yet. May have a role in macrophage lipid metabolism and neural development. PTM: Methylated at Gln-271 by N6AMT1. {ECO:0000250|UniProtKB:Q9BZC7}. SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250|UniProtKB:Q9BZC7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9BZC7}. Lysosome membrane {ECO:0000250|UniProtKB:Q9BZC7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9BZC7}. Note=Forms discrete, punctate intracellular vesicles. {ECO:0000250|UniProtKB:Q9BZC7}. TISSUE SPECIFICITY: Widely expressed in adult tissues. Highest levels are found in brain and pregnant uterus. +P04760 ACHG_MOUSE Acetylcholine receptor subunit gamma 519 58,745 Alternative sequence (1); Chain (1); Disulfide bond (1); Glycosylation (2); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (4) TRANSMEM 241 265 Helical. {ECO:0000255}.; TRANSMEM 274 292 Helical. {ECO:0000255}.; TRANSMEM 308 329 Helical. {ECO:0000255}.; TRANSMEM 477 497 Helical. {ECO:0000255}. TOPO_DOM 23 240 Extracellular. {ECO:0000255}.; TOPO_DOM 330 476 Cytoplasmic. {ECO:0000255}. FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. SUBUNIT: Pentamer of two alpha chains, and one each of the beta, delta, and gamma (in immature muscle) or epsilon (in mature muscle) chains. TISSUE SPECIFICITY: At least in myotubes of skeletal muscle. +A2AKE7 ACL10_MOUSE Actin-like protein 10 346 37,759 Chain (1) +P26149 3BHS2_MOUSE 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2 (3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type II) (3-beta-HSD II) [Includes: 3-beta-hydroxy-Delta(5)-steroid dehydrogenase (EC 1.1.1.145) (3-beta-hydroxy-5-ene steroid dehydrogenase) (Progesterone reductase); Steroid Delta-isomerase (EC 5.3.3.1) (Delta-5-3-ketosteroid isomerase)] 373 41,923 Active site (1); Binding site (1); Chain (1); Sequence conflict (4); Transmembrane (1) TRANSMEM 288 308 Helical. {ECO:0000255}. Lipid metabolism; steroid biosynthesis. FUNCTION: 3-beta-HSD is a bifunctional enzyme, that catalyzes the oxidative conversion of Delta(5)-ene-3-beta-hydroxy steroid, and the oxidative conversion of ketosteroids. The 3-beta-HSD enzymatic system plays a crucial role in the biosynthesis of all classes of hormonal steroids. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. Mitochondrion membrane; Single-pass membrane protein. TISSUE SPECIFICITY: Liver and kidney. +P12023 A4_MOUSE Amyloid-beta A4 protein (ABPP) (APP) (Alzheimer disease amyloid A4 protein homolog) (Amyloid precursor protein) (Amyloid-beta precursor protein) (Amyloidogenic glycoprotein) (AG) [Cleaved into: N-APP; Soluble APP-alpha (S-APP-alpha); Soluble APP-beta (S-APP-beta); C99 (APP-C99) (Beta-secretase C-terminal fragment) (Beta-CTF); Amyloid-beta protein 42 (Abeta42) (Beta-APP42); Amyloid-beta protein 40 (Abeta40) (Beta-APP40); C83 (Alpha-secretase C-terminal fragment) (Alpha-CTF); P3(42); P3(40); C80; Gamma-secretase C-terminal fragment 59 (APP-C59) (Amyloid intracellular domain 59) (AID(59)) (Gamma-CTF(59)); Gamma-secretase C-terminal fragment 57 (APP-C57) (Amyloid intracellular domain 57) (AID(57)) (Gamma-CTF(57)); Gamma-secretase C-terminal fragment 50 (Amyloid intracellular domain 50) (AID(50)) (Gamma-CTF(50)); C31] 770 86,722 Alternative sequence (3); Chain (13); Compositional bias (2); Cross-link (1); Disulfide bond (9); Domain (3); Glycosylation (2); Helix (6); Metal binding (5); Modified residue (8); Motif (2); Mutagenesis (14); Peptide (2); Region (9); Sequence conflict (2); Signal peptide (1); Site (11); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 700 723 Helical. {ECO:0000255}. TOPO_DOM 18 699 Extracellular. {ECO:0000255}.; TOPO_DOM 724 770 Cytoplasmic. {ECO:0000255}. FUNCTION: Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Interaction between APP molecules on neighboring cells promotes synaptogenesis. Involved in cell mobility and transcription regulation through protein-protein interactions. Can promote transcription activation through binding to APBB1-KAT5 and inhibit Notch signaling through interaction with Numb. Couples to apoptosis-inducing pathways such as those mediated by G(O) and JIP. Inhibits G(o) alpha ATPase activity (By similarity). Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1. May be involved in copper homeostasis/oxidative stress through copper ion reduction. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV (By similarity). The splice isoforms that contain the BPTI domain possess protease inhibitor activity. Induces a AGER-dependent pathway that involves activation of p38 MAPK, resulting in internalization of amyloid-beta peptide and leading to mitochondrial dysfunction in cultured cortical neurons (By similarity). Provides Cu(2+) ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1. {ECO:0000250, ECO:0000269|PubMed:15677459}.; FUNCTION: Amyloid-beta peptides are lipophilic metal chelators with metal-reducing activity. Binds transient metals such as copper, zinc and iron. Rat and mouse amyloid-beta peptides bind only weakly transient metals and have little reducing activity due to substitutions of transient metal chelating residues. Amyloid-beta protein 42 may activate mononuclear phagocytes in the brain and elicit inflammatory responses. Promotes both tau aggregation and TPK II-mediated phosphorylation. Also binds GPC1 in lipid rafts (By similarity). {ECO:0000250}.; FUNCTION: The gamma-CTF peptides as well as the caspase-cleaved peptides, including C31, are potent enhancers of neuronal apoptosis. {ECO:0000269|PubMed:15677459}.; FUNCTION: N-APP binds TNFRSF21 triggering caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6). {ECO:0000250}. PTM: Proteolytically processed under normal cellular conditions. Cleavage either by alpha-secretase, beta-secretase or theta-secretase leads to generation and extracellular release of soluble APP peptides, S-APP-alpha and S-APP-beta, and the retention of corresponding membrane-anchored C-terminal fragments, C80, C83 and C99. Subsequent processing of C80 and C83 by gamma-secretase yields P3 peptides. This is the major secretory pathway and is non-amyloidogenic. Alternatively, presenilin/nicastrin-mediated gamma-secretase processing of C99 releases the amyloid-beta proteins, amyloid-beta protein 40 and amyloid-beta protein 42, major components of amyloid plaques, and the cytotoxic C-terminal fragments, gamma-CTF(50), gamma-CTF(57) and gamma-CTF(59). {ECO:0000269|PubMed:23931995}.; PTM: Proteolytically cleaved by caspases during neuronal apoptosis. Cleavage at Asp-739 by either caspase-3, -8 or -9 results in the production of the neurotoxic C31 peptide and the increased production of amyloid-beta peptides (By similarity). {ECO:0000250}.; PTM: N- and O-glycosylated. {ECO:0000250}.; PTM: Phosphorylation in the C-terminal on tyrosine, threonine and serine residues is neuron-specific. Phosphorylation can affect APP processing, neuronal differentiation and interaction with other proteins. The Thr-743 phosphorylated form causes a conformational change which reduces binding of Fe65 family members (By similarity). Phosphorylation on Tyr-757 is required for SHC binding (By similarity). {ECO:0000250}.; PTM: Extracellular binding and reduction of copper, results in a corresponding oxidation of Cys-144 and Cys-158, and the formation of a disulfide bond. {ECO:0000250}.; PTM: Trophic-factor deprivation triggers the cleavage of surface APP by beta-secretase to release sAPP-beta which is further cleaved to release an N-terminal fragment of APP (N-APP). {ECO:0000250}.; PTM: Amyloid-beta peptides are degraded by IDE. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26260791}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P05067}. Membrane {ECO:0000250|UniProtKB:P05067}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P05067}. Perikaryon {ECO:0000250|UniProtKB:P08592}. Cell projection, growth cone {ECO:0000250|UniProtKB:P08592}. Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:P05067}. Early endosome {ECO:0000269|PubMed:25592972, ECO:0000269|PubMed:26260791}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:P05067}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:23931995}. Note=Cell surface protein that rapidly becomes internalized via clathrin-coated pits. Only a minor proportion is present at the cell membrane; most of the protein is present in intracellular vesicles. During maturation, the immature APP (N-glycosylated in the endoplasmic reticulum) moves to the Golgi complex where complete maturation occurs (O-glycosylated and sulfated). After alpha-secretase cleavage, soluble APP is released into the extracellular space and the C-terminal is internalized to endosomes and lysosomes. Some APP accumulates in secretory transport vesicles leaving the late Golgi compartment and returns to the cell surface. APP sorts to the basolateral surface in epithelial cells. During neuronal differentiation, the Thr-743 phosphorylated form is located mainly in growth cones, moderately in neurites and sparingly in the cell body. Casein kinase phosphorylation can occur either at the cell surface or within a post-Golgi compartment (By similarity). Associates with GPC1 in perinuclear compartments (PubMed:15677459). Colocalizes with SORL1 in a vesicular pattern in cytoplasm and perinuclear regions (By similarity). Upon neuronal activation, routed into BACE1-positive recycling endosomes via a clathrin -dependent mechanism (PubMed:23931995). {ECO:0000250|UniProtKB:P05067, ECO:0000269|PubMed:15677459, ECO:0000269|PubMed:23931995}.; SUBCELLULAR LOCATION: Soluble APP-beta: Secreted {ECO:0000305}.; SUBCELLULAR LOCATION: Amyloid-beta protein 42: Cell surface. Note=Associates with FPR2 at the cell surface and the complex is then rapidly internalized. {ECO:0000250|UniProtKB:P05067}.; SUBCELLULAR LOCATION: Gamma-secretase C-terminal fragment 59: Nucleus {ECO:0000250|UniProtKB:P05067}. Cytoplasm {ECO:0000250|UniProtKB:P05067}. Note=located to both the cytoplasm and nuclei of neurons. It can be translocated to the nucleus through association with APBB1 (Fe65). {ECO:0000250|UniProtKB:P05067}. SUBUNIT: Binds, via its C-terminus, to the PID domain of several cytoplasmic proteins, including APBB family members, the APBA family, MAPK8IP1, SHC1, NUMB and DAB1. Binding to DAB1 inhibits its serine phosphorylation. Interacts (via NPXY motif) with DAB2 (via PID domain); the interaction is impaired by tyrosine phosphorylation of the NPXY motif. Also interacts with GPCR-like protein BPP, APPBP1, IB1, KNS2 (via its TPR domains), APPBP2 (via BaSS) and DDB1 (By similarity). In vitro, it binds MAPT via the MT-binding domains (By similarity). Associates with microtubules in the presence of ATP and in a kinesin-dependent manner (By similarity). Interacts, through a C-terminal domain, with GNAO1 (By similarity). Amyloid-beta protein 42 binds CHRNA7 in hippocampal neurons (By similarity). Amyloid-beta associates with HADH2 (By similarity). Interacts with ANKS1B, TNFRSF21 and AGER (By similarity). Interacts with CPEB1. Interacts with ITM2B. Interacts with ITM2C. Interacts with IDE. Can form homodimers; dimerization is enhanced in the presence of Cu(2+) ions. Can form homodimers; this is promoted by heparin binding (By similarity). Amyloid-beta protein 40 interacts with S100A9 (By similarity). CTF-alpha product of APP interacts with GSAP (By similarity). Interacts with SORL1. Interacts with PLD3 (By similarity). Interacts with VDAC1 (PubMed:25168729). Interacts with NSG1; could regulate APP processing (PubMed:21084623). Amyloid-beta protein 42 interacts with FPR2 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P05067, ECO:0000269|PubMed:21084623, ECO:0000269|PubMed:25168729}. DOMAIN: The GFLD subdomain binds Cu(2+) ions; this promotes homodimerization. {ECO:0000250|UniProtKB:P05067}.; DOMAIN: The basolateral sorting signal (BaSS) is required for sorting of membrane proteins to the basolateral surface of epithelial cells.; DOMAIN: The NPXY sequence motif found in many tyrosine-phosphorylated proteins is required for the specific binding of the PID domain. However, additional amino acids either N- or C-terminal to the NPXY motif are often required for complete interaction. The PID domain-containing proteins which bind APP require the YENPTY motif for full interaction. These interactions are independent of phosphorylation on the terminal tyrosine residue. The YENPXY site is also involved in clathrin-mediated endocytosis. {ECO:0000250|UniProtKB:P05067}. TISSUE SPECIFICITY: Expressed in the brain with expression in cortex, cerebellum, hippocampus, olfactory bulb, neurons, astrocytes and microglia (at protein level) (PubMed:26260791). Isoform APP770 is expressed in kidney. Isoform APP751 is widely expressed. Isoform APP695 is expressed in brain, kidney and liver. Isoform APP695, isoform APP714 and isoform APP751 are expressed in several different brain regions including hippocampus, substania nigra pars compacta and cerebellum. In the cerebellum, these isoforms are abundantly expressed in Purkinje cells. {ECO:0000269|PubMed:26260791, ECO:0000269|PubMed:8510506}. +A3KFX0 5NT1A_MOUSE Cytosolic 5'-nucleotidase 1A (cN1A) (EC 3.1.3.5) (Cytosolic 5'-nucleotidase IA) (cN-IA) 365 40,678 Active site (1); Chain (1) FUNCTION: Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides and has a broad substrate specificity. Helps to regulate adenosine levels in heart during ischemia and hypoxia (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +Q91YE9 5NT1B_MOUSE Cytosolic 5'-nucleotidase 1B (cN1B) (EC 3.1.3.5) (Autoimmune infertility-related protein) (Cytosolic 5'-nucleotidase IB) (cN-IB) 573 65,002 Active site (1); Alternative sequence (2); Chain (1); Erroneous initiation (1); Sequence conflict (6) FUNCTION: Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides. Helps to regulate adenosine levels. {ECO:0000269|PubMed:11690631}. SUBCELLULAR LOCATION: Cytoplasm. TISSUE SPECIFICITY: Highly expressed in testis and brain. Detected at lower levels in skeletal muscle, heart and kidney. {ECO:0000269|PubMed:11690631}. +Q91ZH7 ABHD3_MOUSE Phospholipase ABHD3 (EC 3.1.1.32) (EC 3.1.1.4) (Abhydrolase domain-containing protein 3) (Lung alpha/beta hydrolase 3) (MmLABH3) 411 46,232 Active site (3); Alternative sequence (1); Chain (1); Domain (1); Sequence conflict (2); Transmembrane (1) TRANSMEM 25 45 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. FUNCTION: Phospholipase that may play a role in phospholipids remodeling. May selectively cleave myristate (C14)-containing phosphatidylcholines through its predominant phospholipase 1 activity, cleaving preferentially acyl groups in sn1 position. In parallel, may have a minor phospholipase 2 activity acting on acyl groups in position sn2. In addition to (C14)-containing phosphatidylcholines, may also act on other medium-chain-containing and oxidatively truncated phospholipids. {ECO:0000269|PubMed:21926997}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Widely expressed with higher expression in liver. {ECO:0000269|PubMed:11922611}. +Q61285 ABCD2_MOUSE ATP-binding cassette sub-family D member 2 (Adrenoleukodystrophy-related protein) 741 83,483 Chain (1); Domain (2); Glycosylation (2); Modified residue (1); Nucleotide binding (1); Region (1); Sequence conflict (3); Transmembrane (4) TRANSMEM 107 127 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 144 164 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 251 271 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 351 371 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}. FUNCTION: Probable transporter. {ECO:0000250}. SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. SUBUNIT: Can form heterodimers with ABCD1/ALD and ABCD3/PMP70. Dimerization is necessary to form an active transporter. Interacts with PEX19 (By similarity). {ECO:0000250}. +E9Q4Z2 ACACB_MOUSE Acetyl-CoA carboxylase 2 (EC 6.4.1.2) (ACC-beta) [Includes: Biotin carboxylase (EC 6.3.4.14)] 2448 275,750 Active site (1); Binding site (3); Chain (1); Domain (5); Metal binding (4); Modified residue (20); Mutagenesis (1); Nucleotide binding (1); Region (1); Sequence conflict (6); Transit peptide (1) Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. FUNCTION: Catalyzes the ATP-dependent carboxylation of acetyl-CoA to malonyl-CoA (By similarity). Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase (By similarity). Involved in inhibition of fatty acid and glucose oxidation and enhancement of fat storage (PubMed:11283375, PubMed:12920182, PubMed:15677334, PubMed:18487439, PubMed:22362781). May play a role in regulation of mitochondrial fatty acid oxidation through malonyl-CoA-dependent inhibition of carnitine palmitoyltransferase 1 (PubMed:10677481). {ECO:0000250|UniProtKB:O00763, ECO:0000269|PubMed:11283375, ECO:0000269|PubMed:12920182, ECO:0000269|PubMed:15677334, ECO:0000269|PubMed:18487439, ECO:0000269|PubMed:22362781, ECO:0000303|PubMed:10677481}. PTM: Phosphorylated by AMPK, leading to inactivation of the enzyme. Required for the maintenance of skeletal muscle lipid and glucose homeostasis. {ECO:0000269|PubMed:24913514}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:10677481}. Nucleus {ECO:0000250|UniProtKB:O00763}. Endomembrane system {ECO:0000250|UniProtKB:O00763}. Note=May associate with membranes. {ECO:0000250|UniProtKB:O00763}. SUBUNIT: Monomer, homodimer, and homotetramer. Can form filamentous polymers. Interacts with MID1IP1; interaction with MID1IP1 promotes oligomerization and increases its activity. {ECO:0000250|UniProtKB:O00763}. +Q9D7B6 ACAD8_MOUSE Isobutyryl-CoA dehydrogenase, mitochondrial (EC 1.3.99.-) (Acyl-CoA dehydrogenase family member 8) (ACAD-8) 413 45,020 Active site (1); Binding site (5); Chain (1); Erroneous initiation (1); Modified residue (5); Nucleotide binding (6); Region (1); Sequence conflict (7); Transit peptide (1) Amino-acid degradation; L-valine degradation. FUNCTION: Has very high activity toward isobutyryl-CoA. Is an isobutyryl-CoA dehydrogenase that functions in valine catabolism (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. SUBUNIT: Homotetramer, formed by a dimer of dimers. Subunit of the large multiprotein complex ARC/DRIP (By similarity). {ECO:0000250}. +P49582 ACHA7_MOUSE Neuronal acetylcholine receptor subunit alpha-7 502 56,632 Chain (1); Disulfide bond (2); Glycosylation (3); Signal peptide (1); Topological domain (2); Transmembrane (4) TRANSMEM 231 255 Helical. {ECO:0000255}.; TRANSMEM 262 280 Helical. {ECO:0000255}.; TRANSMEM 296 317 Helical. {ECO:0000255}.; TRANSMEM 470 490 Helical. {ECO:0000255}. TOPO_DOM 23 230 Extracellular. {ECO:0000255}.; TOPO_DOM 318 469 Cytoplasmic. {ECO:0000255}. FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. The channel is blocked by alpha-bungarotoxin. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. SUBUNIT: Homopentamer. Interacts with RIC3; which is required for proper folding and assembly. Interacts with LYPD6. Interacts with the alpha-conotoxin RgIA (By similarity). Interacts with alpha-conotoxins ImI and ImII (By similarity). {ECO:0000250|UniProtKB:P36544, ECO:0000250|UniProtKB:P54131, ECO:0000250|UniProtKB:Q05941}. +P21836 ACES_MOUSE Acetylcholinesterase (AChE) (EC 3.1.1.7) 614 68,169 Active site (3); Beta strand (24); Chain (1); Disulfide bond (4); Glycosylation (3); Helix (28); Signal peptide (1); Turn (7) FUNCTION: Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. SUBCELLULAR LOCATION: Cell junction, synapse. Secreted. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform H: Cell membrane; Lipid-anchor, GPI-anchor; Extracellular side. SUBUNIT: Isoform H generates GPI-anchored dimers; disulfide linked. Isoform T generates multiple structures, ranging from monomers and dimers to collagen-tailed and hydrophobic-tailed forms, in which catalytic tetramers are associated with anchoring proteins that attach them to the basal lamina or to cell membranes. In the collagen-tailed forms, isoform T subunits are associated with a specific collagen, COLQ, which triggers the formation of isoform T tetramers, from monomers and dimers (By similarity). Interacts with PRIMA1. The interaction with PRIMA1 is required to anchor it to the basal lamina of cells and organize into tetramers. {ECO:0000250, ECO:0000269|PubMed:11804574, ECO:0000269|PubMed:12505979}. TISSUE SPECIFICITY: Predominates in most expressing tissues except erythrocytes where a glycophospholipid-attached form of ACHE predominates. +P68033 ACTC_MOUSE Actin, alpha cardiac muscle 1 (Alpha-cardiac actin) [Cleaved into: Actin, alpha cardiac muscle 1, intermediate form] 377 42,019 Chain (2); Initiator methionine (1); Modified residue (5) FUNCTION: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. PTM: Oxidation of Met-46 and Met-49 by MICALs (MICAL1, MICAL2 or MICAL3) to form methionine sulfoxide promotes actin filament depolymerization. MICAL1 and MICAL2 produce the (R)-S-oxide form. The (R)-S-oxide form is reverted by MSRB1 and MSRB2, which promotes actin repolymerization. {ECO:0000269|PubMed:23911929}.; PTM: Monomethylation at Lys-86 (K86me1) regulates actin-myosin interaction and actomyosin-dependent processes. Demethylation by ALKBH4 is required for maintaining actomyosin dynamics supporting normal cleavage furrow ingression during cytokinesis and cell migration. {ECO:0000250|UniProtKB:P68032}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SUBUNIT: Polymerization of globular actin (G-actin) leads to a structural filament (F-actin) in the form of a two-stranded helix. Each actin can bind to 4 others. +Q9DC29 ABCB6_MOUSE ATP-binding cassette sub-family B member 6, mitochondrial 842 93,770 Binding site (1); Chain (1); Domain (2); Frameshift (1); Mutagenesis (3); Nucleotide binding (1); Transmembrane (11) TRANSMEM 27 47 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 73 93 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 107 127 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 148 168 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 186 206 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 264 284 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 292 312 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 376 396 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 409 431 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 500 520 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 530 550 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}. FUNCTION: Binds heme and porphyrins and functions in their ATP-dependent uptake into the mitochondria. Plays a crucial role in heme synthesis. {ECO:0000269|PubMed:17006453}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9NP58}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane {ECO:0000269|PubMed:17006453}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9NP58}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9NP58}; Multi-pass membrane protein {ECO:0000255}. Endosome membrane {ECO:0000269|PubMed:23519333}; Multi-pass membrane protein {ECO:0000255}. Note=localized to the endosome-like compartment and dendrite tips. {ECO:0000269|PubMed:23519333}. SUBUNIT: Homodimer. {ECO:0000250}. +Q9DBL9 ABHD5_MOUSE 1-acylglycerol-3-phosphate O-acyltransferase ABHD5 (EC 2.3.1.51) (Abhydrolase domain-containing protein 5) (Lipid droplet-binding protein CGI-58) (Protein CGI-58) 351 39,155 Alternative sequence (1); Beta strand (1); Chain (1); Domain (1); Helix (1); Modified residue (1); Motif (1) FUNCTION: Lysophosphatidic acid acyltransferase which functions in phosphatidic acid biosynthesis (PubMed:16679289). May regulate the cellular storage of triacylglycerol through activation of the phospholipase PNPLA2 (PubMed:16679289). Involved in keratinocyte differentiation (PubMed:16679289). Regulates lipid droplet fusion (PubMed:26083785). {ECO:0000269|PubMed:16679289, ECO:0000269|PubMed:26083785}. SUBCELLULAR LOCATION: Cytoplasm. Lipid droplet. Note=Colocalized with PLIN and ADRP on the surface of lipid droplets. The localization is dependent upon the metabolic status of the adipocytes and the activity of PKA. SUBUNIT: Interacts with ADRP (By similarity). Interacts with PLIN. Interacts with and PNPLA2. Interacts with PLIN5; promotes interaction with PNPLA2. {ECO:0000250, ECO:0000269|PubMed:15292255, ECO:0000269|PubMed:16679289, ECO:0000269|PubMed:19064991, ECO:0000269|PubMed:21148142}. DOMAIN: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in the adipose tissue and testes. Weakly expressed in the liver, muscle, kidney, and heart. Expressed by upper epidermal layers and dermal fibroblasts in skin, hepatocytes and hypothalamus in brain (at protein level). {ECO:0000269|PubMed:15292255, ECO:0000269|PubMed:16679289, ECO:0000269|PubMed:18832586}. +P55096 ABCD3_MOUSE ATP-binding cassette sub-family D member 3 (68 kDa peroxisomal membrane protein) (PMP68) (70 kDa peroxisomal membrane protein) (PMP70) 659 75,475 Chain (1); Domain (2); Glycosylation (3); Modified residue (6); Nucleotide binding (1); Region (2); Sequence conflict (5); Transmembrane (4) TRANSMEM 84 104 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 126 146 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 224 244 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 313 333 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}. FUNCTION: Probable transporter involved in the transport of branched-chain fatty acids and C27 bile acids into the peroxisome; the latter function is a crucial step in bile acid biosynthesis. The nucleotide-binding fold acts as an ATP-binding subunit with ATPase activity. {ECO:0000250|UniProtKB:P28288}. SUBCELLULAR LOCATION: Peroxisome membrane; Multi-pass membrane protein. SUBUNIT: Homodimer or heterodimer (Potential). Interacts with PEX19 (By similarity). {ECO:0000250, ECO:0000305}. +P00520 ABL1_MOUSE Tyrosine-protein kinase ABL1 (EC 2.7.10.2) (Abelson murine leukemia viral oncogene homolog 1) (Abelson tyrosine-protein kinase 1) (Proto-oncogene c-Abl) (p150) 1123 122,673 Active site (1); Alternative sequence (3); Beta strand (28); Binding site (1); Chain (1); Compositional bias (4); Domain (3); Helix (22); Initiator methionine (1); Lipidation (1); Modified residue (32); Motif (5); Mutagenesis (15); Nucleotide binding (2); Region (3); Sequence conflict (4); Turn (1) FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in many key processes linked to cell growth and survival such as cytoskeleton remodeling in response to extracellular stimuli, cell motility and adhesion, receptor endocytosis, autophagy, DNA damage response and apoptosis. Coordinates actin remodeling through tyrosine phosphorylation of proteins controlling cytoskeleton dynamics like WASF3 (involved in branch formation); ANXA1 (involved in membrane anchoring); DBN1, DBNL, CTTN, RAPH1 and ENAH (involved in signaling); or MAPT and PXN (microtubule-binding proteins). Phosphorylation of WASF3 is critical for the stimulation of lamellipodia formation and cell migration. Involved in the regulation of cell adhesion and motility through phosphorylation of key regulators of these processes such as BCAR1, CRK, CRKL, DOK1, EFS or NEDD9. Phosphorylates multiple receptor tyrosine kinases and more particularly promotes endocytosis of EGFR, facilitates the formation of neuromuscular synapses through MUSK, inhibits PDGFRB-mediated chemotaxis and modulates the endocytosis of activated B-cell receptor complexes. Other substrates which are involved in endocytosis regulation are the caveolin (CAV1) and RIN1. Moreover, ABL1 regulates the CBL family of ubiquitin ligases that drive receptor down-regulation and actin remodeling. Phosphorylation of CBL leads to increased EGFR stability. Involved in late-stage autophagy by regulating positively the trafficking and function of lysosomal components. ABL1 targets to mitochondria in response to oxidative stress and thereby mediates mitochondrial dysfunction and cell death. In response to oxidative stress, phosphorylates serine/threonine kinase PRKD2 at 'Tyr-717' (By similarity). ABL1 is also translocated in the nucleus where it has DNA-binding activity and is involved in DNA-damage response and apoptosis. Many substrates are known mediators of DNA repair: DDB1, DDB2, ERCC3, ERCC6, RAD9A, RAD51, RAD52 or WRN. Activates the proapoptotic pathway when the DNA damage is too severe to be repaired. Phosphorylates TP73, a primary regulator for this type of damage-induced apoptosis. Phosphorylates the caspase CASP9 on 'Tyr-191' and regulates its processing in the apoptotic response to DNA damage. Phosphorylates PSMA7 that leads to an inhibition of proteasomal activity and cell cycle transition blocks. Regulates T-cell differentiation in a TBX21-dependent manner (PubMed:21690296). Phosphorylates TBX21 on tyrosine residues leading to an enhancement of its transcriptional activator activity (PubMed:21690296). {ECO:0000250|UniProtKB:P00519, ECO:0000269|PubMed:11279004, ECO:0000269|PubMed:11279131, ECO:0000269|PubMed:11350980, ECO:0000269|PubMed:12107171, ECO:0000269|PubMed:12748290, ECO:0000269|PubMed:14993293, ECO:0000269|PubMed:19878872, ECO:0000269|PubMed:19903482, ECO:0000269|PubMed:21690296, ECO:0000269|PubMed:7780740, ECO:0000269|PubMed:8194526, ECO:0000269|PubMed:9109492}. PTM: Acetylated at Lys-710 by EP300 which promotes the cytoplasmic translocation. {ECO:0000250}.; PTM: Phosphorylation at Tyr-70 by members of the SRC family of kinases disrupts SH3 domain-based autoinhibitory interactions and intermolecular associations, such as that with ABI1, and also enhances kinase activity (By similarity). Phosphorylation at Tyr-226 and Tyr-393 correlate with increased activity (By similarity). DNA damage-induced activation of ABL1 requires the function of ATM and Ser-446 phosphorylation. Phosphorylation at Thr-547 and Ser-569 has been attributed to a CDC2-associated kinase and is coupled to cell division. Phosphorylation at Ser-618 and Ser-619 by PAK2 increases binding to CRK and reduces binding to ABI1 (By similarity). Phosphorylation on Thr-734 is required for binding 14-3-3 proteins for cytoplasmic translocation (By similarity). Phosphorylated by PDGFRB and PRKDC. {ECO:0000250, ECO:0000269|PubMed:10988075, ECO:0000269|PubMed:12748290, ECO:0000269|PubMed:14993293, ECO:0000269|PubMed:1566087, ECO:0000269|PubMed:19903482, ECO:0000269|PubMed:2183353, ECO:0000269|PubMed:9109492}.; PTM: Polyubiquitinated. Polyubiquitination of ABL1 leads to degradation (By similarity). {ECO:0000250}.; PTM: Isoform IV is myristoylated on Gly-2. {ECO:0000269|PubMed:12654251}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Nucleus. Mitochondrion. Note=The myristoylated c-ABL protein is reported to be nuclear. Sequestered into the cytoplasm through interaction with 14-3-3 proteins (By similarity). Localizes to mitochondria in response to oxidative stress. {ECO:0000250}. SUBUNIT: Interacts with INPPL1/SHIP2. Interacts with SORBS1 following insulin stimulation. Found in a trimolecular complex containing CDK5 and CABLES1. Interacts with CABLES1 and PSTPIP1. Interacts with ZDHHC16. Interacts with the 14-3-3 proteins, YWHAB, YWHAE, YWHAG, YWHAH, SFN AND YWHAZ; the interaction with 14-3-3 proteins requires phosphorylation on Thr-734 and sequesters ABL1 into the cytoplasm. Interacts (via SH3 domain) with CASP9; the interaction is direct and increases in the response of cells to genotoxic stress and ABL1/c-Abl activation (By similarity). Interacts with ABI1, ABI2, BCR, CRK, FYN, LYN, PSMA7 RAD9A, RAD51, RAD52, TP73 and WASF3. A complex made of ABL1, CTTN and MYLK regulates cortical actin-based cytoskeletal rearrangement critical to sphingosine 1-phosphate (S1P)-mediated endothelial cell (EC) barrier enhancement. Interacts with STX17; probably phosphorylates STX17 (By similarity). Interacts with ITGB1, HCK and FGR. Found in a complex with ABL1, ABL2, CRK and UNC119; leading to the inhibition of CRK phosphorylation by ABL kinases (By similarity). Interacts with TBX21 (PubMed:21690296). {ECO:0000250|UniProtKB:P00519, ECO:0000269|PubMed:10896159, ECO:0000269|PubMed:11163214, ECO:0000269|PubMed:11279004, ECO:0000269|PubMed:12021275, ECO:0000269|PubMed:12748290, ECO:0000269|PubMed:19903482, ECO:0000269|PubMed:21690296}. TISSUE SPECIFICITY: Widely expressed. +O08707 ACKR2_MOUSE Atypical chemokine receptor 2 (C-C chemokine receptor D6) (Chemokine-binding protein 2) (Chemokine-binding protein D6) 378 43,207 Chain (1); Disulfide bond (1); Glycosylation (1); Region (1); Sequence conflict (1); Topological domain (8); Transmembrane (7) TRANSMEM 50 70 Helical; Name=1. {ECO:0000255}.; TRANSMEM 92 112 Helical; Name=2. {ECO:0000255}.; TRANSMEM 118 139 Helical; Name=3. {ECO:0000255}.; TRANSMEM 162 182 Helical; Name=4. {ECO:0000255}.; TRANSMEM 217 237 Helical; Name=5. {ECO:0000255}.; TRANSMEM 250 270 Helical; Name=6. {ECO:0000255}.; TRANSMEM 293 313 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 49 Extracellular. {ECO:0000255}.; TOPO_DOM 71 91 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 113 117 Extracellular. {ECO:0000255}.; TOPO_DOM 140 161 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 183 216 Extracellular. {ECO:0000255}.; TOPO_DOM 238 249 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 271 292 Extracellular. {ECO:0000255}.; TOPO_DOM 314 378 Cytoplasmic. {ECO:0000255}. FUNCTION: Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing receptor) or chemokine-scavenging receptor or chemokine decoy receptor. Acts as a receptor for chemokines including CCL2, CCL3, CCL3L1, CCL4, CCL5, CCL7, CCL8, CCL11, CCL13, CCL17, CCL22, CCL23, CCL24, SCYA2/MCP-1, SCY3/MIP-1-alpha, SCYA5/RANTES and SCYA7/MCP-3. Upon active ligand stimulation, activates a beta-arrestin 1 (ARRB1)-dependent, G protein-independent signaling pathway that results in the phosphorylation of the actin-binding protein cofilin (CFL1) through a RAC1-PAK1-LIMK1 signaling pathway. Activation of this pathway results in up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. By scavenging chemokines in tissues, on the surfaces of lymphatic vessels, and in placenta, plays an essential role in the resolution (termination) of the inflammatory response and in the regulation of adaptive immune responses. Plays a major role in the immune silencing of macrophages during the resolution of inflammation. Acts as a regulator of inflammatory leukocyte interactions with lymphatic endothelial cells (LECs) and is required for immature/mature dendritic cells discrimination by LECs. {ECO:0000269|PubMed:22651933}. PTM: Phosphorylated on serine residues in the C-terminal cytoplasmic tail. {ECO:0000250}. SUBCELLULAR LOCATION: Early endosome {ECO:0000250}. Recycling endosome {ECO:0000250}. Cell membrane; Multi-pass membrane protein. Note=Predominantly localizes to endocytic vesicles, and upon stimulation by the ligand is internalized via clathrin-coated pits. Once internalized, the ligand dissociates from the receptor, and is targeted to degradation while the receptor is recycled back to the cell membrane (By similarity). {ECO:0000250}. DOMAIN: The C-terminal cytoplasmic tail controls its phosphorylation, stability, intracellular trafficking itinerary, and chemokine scavenging properties. {ECO:0000250}. TISSUE SPECIFICITY: Expressed on apoptotic neutrophils (at protein level). {ECO:0000269|PubMed:22651933}. +Q9R0W9 ACHA6_MOUSE Neuronal acetylcholine receptor subunit alpha-6 494 56,856 Chain (1); Disulfide bond (2); Glycosylation (2); Modified residue (1); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (4) TRANSMEM 241 265 Helical. {ECO:0000255}.; TRANSMEM 272 290 Helical. {ECO:0000255}.; TRANSMEM 306 327 Helical. {ECO:0000255}.; TRANSMEM 466 485 Helical. {ECO:0000255}. TOPO_DOM 31 240 Extracellular. {ECO:0000255}.; TOPO_DOM 328 465 Cytoplasmic. {ECO:0000255}. FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Neuronal AChR seems to be composed of two different types of subunits: alpha and non-alpha (beta). Interacts with LYPD6. {ECO:0000250|UniProtKB:Q15825}. +Q9JI91 ACTN2_MOUSE Alpha-actinin-2 (Alpha-actinin skeletal muscle isoform 2) (F-actin cross-linking protein) 894 103,834 Calcium binding (2); Chain (1); Domain (4); Modified residue (1); Region (1); Repeat (4); Sequence conflict (6) FUNCTION: F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein (By similarity). {ECO:0000250}. PTM: Ubiquitinated by FBXL22, leading to proteasomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:19932097}. Note=Colocalizes with MYOZ1 and FLNC at the Z-lines of skeletal muscle. SUBUNIT: Homodimer; antiparallel. Also forms heterodimers with ACTN3. Interacts with ADAM12, MYOZ1, MYOZ2 and MYOZ3. Interacts via its C-terminal region with the LDB3 PDZ domain. Interacts with XIRP2. Interacts with DST (via N-terminus). Interacts with PARVB. Interacts with SYNPO2 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P35609}. +Q8K348 ACV1C_MOUSE Activin receptor type-1C (EC 2.7.11.30) (Activin receptor type IC) (ACTR-IC) (Activin receptor-like kinase 7) (ALK-7) 493 54,700 Active site (1); Binding site (1); Chain (1); Domain (2); Frameshift (1); Nucleotide binding (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 114 134 Helical. {ECO:0000255}. TOPO_DOM 27 113 Extracellular. {ECO:0000255}.; TOPO_DOM 135 493 Cytoplasmic. {ECO:0000255}. FUNCTION: Serine/threonine protein kinase which forms a receptor complex on ligand binding. The receptor complex consisting of 2 type II and 2 type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators, SMAD2 and SMAD3. Receptor for activin AB, activin B and NODAL. Plays a role in cell differentiation, growth arrest and apoptosis. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Binds the type 2 receptor protein ACVR2A. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in interdigital regions in developing limb buds. {ECO:0000269|PubMed:15485907}. +Q8CG27 ACTL9_MOUSE Actin-like protein 9 415 45,771 Chain (1); Sequence conflict (1) SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. +Q6PAT0 ADAT3_MOUSE Probable inactive tRNA-specific adenosine deaminase-like protein 3 (tRNA-specific adenosine-34 deaminase subunit ADAT3) 349 37,517 Chain (1); Domain (1); Metal binding (3); Modified residue (1); Sequence conflict (1) +Q60718 ADAM2_MOUSE Disintegrin and metalloproteinase domain-containing protein 2 (ADAM 2) (Fertilin subunit beta) (PH-30) (PH30) (PH30-beta) 735 82,375 Chain (1); Compositional bias (1); Disulfide bond (7); Domain (3); Glycosylation (8); Modified residue (1); Propeptide (1); Sequence conflict (12); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 687 707 Helical. {ECO:0000255}. TOPO_DOM 19 686 Extracellular. {ECO:0000255}.; TOPO_DOM 708 735 Cytoplasmic. {ECO:0000255}. FUNCTION: Sperm surface membrane protein that may be involved in sperm-egg plasma membrane adhesion and fusion during fertilization. Could have a direct role in sperm-zona binding or migration of sperm from the uterus into the oviduct. Interactions with egg membrane could be mediated via binding between its disintegrin-like domain to one or more integrins receptors on the egg. This is a non catalytic metalloprotease-like protein (By similarity). {ECO:0000250}. PTM: The signal and the metalloprotease domain are cleaved during the epididymal maturation of the spermatozoa. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Heterodimer with ADAM1/fertilin subunit alpha. DOMAIN: A tripeptide motif (QDE) within disintegrin-like domain could be involved in the binding to egg integrin receptor and thus could mediate sperm/egg binding. {ECO:0000250}. TISSUE SPECIFICITY: Expressed specifically in testis. +Q8VCR7 ABHEB_MOUSE Protein ABHD14B (EC 3.-.-.-) (Alpha/beta hydrolase domain-containing protein 14B) (Abhydrolase domain-containing protein 14B) (CCG1-interacting factor B) 210 22,451 Active site (3); Chain (1); Modified residue (1) FUNCTION: Has hydrolase activity towards p-nitrophenyl butyrate (in vitro). May activate transcription (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: May interact with TAF1. {ECO:0000250}. +Q8K268 ABCF3_MOUSE ATP-binding cassette sub-family F member 3 709 79,865 Chain (1); Domain (2); Frameshift (1); Initiator methionine (1); Modified residue (6); Nucleotide binding (2); Sequence conflict (1) FUNCTION: Displays an antiviral effect against flaviviruses such as west Nile virus (WNV) in the presence of OAS1B. {ECO:0000269|PubMed:22623793}. +Q8VHQ9 ACO11_MOUSE Acyl-coenzyme A thioesterase 11 (Acyl-CoA thioesterase 11) (EC 3.1.2.-) (Acyl-CoA thioester hydrolase 11) (Adipose-associated thioesterase) (Brown fat-inducible thioesterase) (BFIT) 594 67,355 Binding site (1); Chain (1); Domain (3); Modified residue (2); Region (3) FUNCTION: Has acyl-CoA thioesterase activity towards medium (C12) and long-chain (C18) fatty acyl-CoA substrates. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +Q9ERZ4 ACM2_MOUSE Muscarinic acetylcholine receptor M2 466 51,499 Chain (1); Disulfide bond (2); Glycosylation (3); Modified residue (4); Motif (2); Region (3); Sequence conflict (1); Topological domain (8); Transmembrane (7) TRANSMEM 23 45 Helical; Name=1. {ECO:0000250}.; TRANSMEM 60 80 Helical; Name=2. {ECO:0000250}.; TRANSMEM 98 119 Helical; Name=3. {ECO:0000250}.; TRANSMEM 140 162 Helical; Name=4. {ECO:0000250}.; TRANSMEM 185 209 Helical; Name=5. {ECO:0000250}.; TRANSMEM 388 410 Helical; Name=6. {ECO:0000250}.; TRANSMEM 419 442 Helical; Name=7. {ECO:0000250}. TOPO_DOM 1 22 Extracellular. {ECO:0000250}.; TOPO_DOM 46 59 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 81 97 Extracellular. {ECO:0000250}.; TOPO_DOM 120 139 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 163 184 Extracellular. {ECO:0000250}.; TOPO_DOM 210 387 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 411 418 Extracellular. {ECO:0000250}.; TOPO_DOM 443 466 Cytoplasmic. {ECO:0000250}. FUNCTION: The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is adenylate cyclase inhibition. Signaling promotes phospholipase C activity, leading to the release of inositol trisphosphate (IP3); this then triggers calcium ion release into the cytosol (By similarity). {ECO:0000250}. PTM: Phosphorylated in response to agonist treatment. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Phosphorylation in response to agonist binding promotes receptor internalization. {ECO:0000250}. SUBUNIT: Interacts with ARRB1 and ARRB2. Interacts with RACK1; the interaction regulates CHRM2 internalization (By similarity). {ECO:0000250}. +P60710 ACTB_MOUSE Actin, cytoplasmic 1 (Beta-actin) [Cleaved into: Actin, cytoplasmic 1, N-terminally processed] 375 41,737 Chain (2); Initiator methionine (1); Modified residue (6); Sequence conflict (7) FUNCTION: Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm of cells (By similarity). Actin exists in both monomeric (G-actin) and polymeric (F-actin) forms, both forms playing key functions, such as cell motility and contraction (By similarity). In addition to their role in the cytoplasmic cytoskeleton, G- and F-actin also localize in the nucleus, and regulate gene transcription and motility and repair of damaged DNA (PubMed:23558171, PubMed:25759381). {ECO:0000250|UniProtKB:P60709, ECO:0000269|PubMed:23558171, ECO:0000269|PubMed:25759381}. PTM: ISGylated. {ECO:0000269|PubMed:16139798}.; PTM: Oxidation of Met-44 and Met-47 by MICALs (MICAL1, MICAL2 or MICAL3) to form methionine sulfoxide promotes actin filament depolymerization (PubMed:23911929). MICAL1 and MICAL2 produce the (R)-S-oxide form. The (R)-S-oxide form is reverted by MSRB1 and MSRB2, which promote actin repolymerization (PubMed:23911929). {ECO:0000269|PubMed:23911929}.; PTM: Monomethylation at Lys-84 (K84me1) regulates actin-myosin interaction and actomyosin-dependent processes. Demethylation by ALKBH4 is required for maintaining actomyosin dynamics supporting normal cleavage furrow ingression during cytokinesis and cell migration. {ECO:0000250|UniProtKB:P60709}.; PTM: Actin, cytoplasmic 1, N-terminally processed: N-terminal acetylation by NAA80 affects actin filament depolymerization and elongation, including elongation driven by formins. In contrast, filament nucleation by the Arp2/3 complex is not affected. {ECO:0000250|UniProtKB:P60709}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Nucleus {ECO:0000269|PubMed:23558171, ECO:0000269|PubMed:25759381}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. {ECO:0000250|UniProtKB:P60709}. SUBUNIT: Polymerization of globular actin (G-actin) leads to a structural filament (F-actin) in the form of a two-stranded helix (PubMed:25759381). Each actin can bind to 4 others (By similarity). Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs (By similarity). Component of the BAF complex, which includes at least actin (ACTB), ARID1A, ARID1B/BAF250, SMARCA2, SMARCA4/BRG1, MARCB1/BAF47, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57, SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more of SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C (By similarity). In muscle cells, the BAF complex also contains DPF3 (By similarity). Found in a complex with XPO6, Ran, ACTB and PFN1 (By similarity). Component of a complex composed at least of ACTB, AP2M1, AP2A1, AP2A2, MEGF10 and VIM (By similarity). Interacts with XPO6 and EMD (By similarity). Interacts with ERBB2 (By similarity). Interacts with GCSAM (By similarity). Interacts with CPNE1 (via VWFA domain) and CPNE4 (via VWFA domain) (PubMed:12522145). Interacts with TBC1D21 (PubMed:21128978). Interacts with DHX9 (via C-terminus); this interaction is direct and mediates the attachment to nuclear ribonucleoprotein complexes (By similarity). Interacts with FAM107A (PubMed:21969592). {ECO:0000250|UniProtKB:P60709, ECO:0000269|PubMed:12522145, ECO:0000269|PubMed:21128978, ECO:0000269|PubMed:21969592, ECO:0000269|PubMed:25759381}. +P68134 ACTS_MOUSE Actin, alpha skeletal muscle (Alpha-actin-1) [Cleaved into: Actin, alpha skeletal muscle, intermediate form] 377 42,051 Beta strand (14); Chain (2); Helix (22); Initiator methionine (1); Modified residue (6); Turn (2) FUNCTION: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. PTM: Oxidation of Met-46 and Met-49 by MICALs (MICAL1, MICAL2 or MICAL3) to form methionine sulfoxide promotes actin filament depolymerization. MICAL1 and MICAL2 produce the (R)-S-oxide form. The (R)-S-oxide form is reverted by MSRB1 and MSRB2, which promotes actin repolymerization. {ECO:0000269|PubMed:23911929}.; PTM: Monomethylation at Lys-86 (K84me1) regulates actin-myosin interaction and actomyosin-dependent processes. Demethylation by ALKBH4 is required for maintaining actomyosin dynamics supporting normal cleavage furrow ingression during cytokinesis and cell migration. {ECO:0000250|UniProtKB:P68133}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SUBUNIT: Polymerization of globular actin (G-actin) leads to a structural filament (F-actin) in the form of a two-stranded helix. Each actin can bind to 4 others. Interacts with TTID. Interacts (via its C-terminus) with USP25; the interaction occurs for all USP25 isoforms but is strongest for isoform USP25m in muscle differentiating cells (By similarity). Identified in a complex composed of ACTA1, COBL, GSN AND TMSB4X (By similarity). {ECO:0000250}. +Q80WC9 ACSF4_MOUSE Beta-alanine-activating enzyme (EC 6.2.1.-) (Acyl-CoA synthetase family member 4) (Protein LYS2 homolog) 1100 121,569 Alternative sequence (2); Binding site (3); Chain (1); Domain (1); Modified residue (2); Mutagenesis (1); Nucleotide binding (1) FUNCTION: Covalently binds beta-alanine in an ATP-dependent manner to form a thioester bond with its phosphopantetheine group and transfers it to an as yet unknown acceptor via an amide bond. May be required for a post-translational protein modification or for post-transcriptional modification of an RNA. {ECO:0000269|PubMed:24467666, ECO:0000303|PubMed:24467666}. +P24815 3BHS1_MOUSE 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1 (3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type I) (3-beta-HSD I) (3-beta-hydroxy-5-ene steroid dehydrogenase) (3-beta-hydroxy-Delta(5)-steroid dehydrogenase) (EC 1.1.1.145) (3-beta-hydroxysteroid 3-dehydrogenase) (EC 1.1.1.270) (Delta-5-3-ketosteroid isomerase) (Dihydrotestosterone oxidoreductase) (EC 1.1.1.210) (Steroid Delta-isomerase) (EC 5.3.3.1) 373 42,062 Active site (1); Binding site (2); Chain (1); Nucleotide binding (1); Sequence conflict (2); Transmembrane (1) TRANSMEM 288 308 Helical. {ECO:0000255}. Steroid hormone biosynthesis. Steroid metabolism. FUNCTION: A bifunctional enzyme responsible for the oxidation and isomerization of 3beta-hydroxy-Delta(5)-steroid precursors to 3-oxo-Delta(4)-steroids, an essential step in steroid hormone biosynthesis. Specifically catalyzes the conversion of pregnenolone to progesterone, 17alpha-hydroxypregnenolone to 17alpha-hydroxyprogesterone, dehydroepiandrosterone (DHEA) to 4-androstenedione, and androstenediol to testosterone. Additionally, catalyzes the interconversion between 3beta-hydroxy and 3-oxo-5alpha-androstane steroids controlling the bioavalability of the active forms. Specifically converts dihydrotestosterone to its inactive form 5alpha-androstanediol, that does not bind androgen receptor/AR. Also converts androstanedione, a precursor of testosterone and estrone, to epiandrosterone. Expected to use NAD(+) as preferred electron donor for the 3-beta-hydroxy-steroid dehydrogenase activity and NADPH for the 3-ketosteroid reductase activity. {ECO:0000250|UniProtKB:P14060, ECO:0000250|UniProtKB:P22071}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. Mitochondrion membrane; Single-pass membrane protein. TISSUE SPECIFICITY: Steroidogenic tissues (includes testes, ovaries and adrenal glands). +Q60876 4EBP1_MOUSE Eukaryotic translation initiation factor 4E-binding protein 1 (4E-BP1) (eIF4E-binding protein 1) (Phosphorylated heat- and acid-stable protein regulated by insulin 1) (PHAS-I) 117 12,325 Chain (1); Cross-link (1); Initiator methionine (1); Modified residue (14); Motif (2); Mutagenesis (1); Sequence conflict (1) FUNCTION: Repressor of translation initiation that regulates EIF4E activity by preventing its assembly into the eIF4F complex: hypophosphorylated form competes with EIF4G1/EIF4G3 and strongly binds to EIF4E, leading to repress translation. In contrast, hyperphosphorylated form dissociates from EIF4E, allowing interaction between EIF4G1/EIF4G3 and EIF4E, leading to initiation of translation (By similarity). Mediates the regulation of protein translation by hormones, growth factors and other stimuli that signal through the MAP kinase and mTORC1 pathways (PubMed:7629182). {ECO:0000250|UniProtKB:Q13541, ECO:0000269|PubMed:7629182}. PTM: Phosphorylated on serine and threonine residues in response to insulin, EGF and PDGF. Phosphorylation at Thr-36, Thr-45, Ser-64 and Thr-69, corresponding to the hyperphosphorylated form, is regulated by mTORC1 and abolishes binding to EIF4E. {ECO:0000269|PubMed:7629182}.; PTM: Ubiquitinated: when eIF4E levels are low, hypophosphorylated form is ubiquitinated by the BCR(KLHL25) complex, leading to its degradation and serving as a homeostatic mechanism to maintain translation and prevent eIF4E inhibition when eIF4E levels are low. Not ubiquitinated when hyperphosphorylated (at Thr-36, Thr-45, Ser-64 and Thr-69) or associated with eIF4E. {ECO:0000250|UniProtKB:Q13541}. SUBUNIT: Hypophosphorylated EIF4EBP1 competes with EIF4G1/EIF4G3 to interact with EIF4E; insulin stimulated MAP-kinase (MAPK1 and MAPK3) or mTORC1 phosphorylation of EIF4EBP1 causes dissociation of the complex allowing EIF4G1/EIF4G3 to bind and consequent initiation of translation (PubMed:7629182). Interacts (via TOS motif) with RPTOR; promoting phosphorylation by mTORC1 (PubMed:24139800). {ECO:0000269|PubMed:24139800, ECO:0000269|PubMed:7629182}. DOMAIN: The TOS motif mediates interaction with RPTOR, leading to promote phosphorylation by mTORC1 complex. {ECO:0000269|PubMed:24139800}. TISSUE SPECIFICITY: Highest expression in fat cells. {ECO:0000269|PubMed:7629182}. +P70445 4EBP2_MOUSE Eukaryotic translation initiation factor 4E-binding protein 2 (4E-BP2) (eIF4E-binding protein 2) (Phosphorylated heat- and acid-stable protein regulated by insulin 2) (PHAS-II) 120 12,898 Chain (1); Modified residue (7); Motif (2); Mutagenesis (6) FUNCTION: Repressor of translation initiation involved in synaptic plasticity, learning and memory formation (PubMed:16237163, PubMed:17029989). Regulates EIF4E activity by preventing its assembly into the eIF4F complex: hypophosphorylated form of EIF4EBP2 competes with EIF4G1/EIF4G3 and strongly binds to EIF4E, leading to repress translation. In contrast, hyperphosphorylated form dissociates from EIF4E, allowing interaction between EIF4G1/EIF4G3 and EIF4E, leading to initiation of translation (PubMed:17029989, PubMed:20347422, PubMed:23172145). EIF4EBP2 is enriched in brain and acts as a regulator of synapse activity and neuronal stem cell renewal via its ability to repress translation initiation (PubMed:20347422, PubMed:24139800, PubMed:23172145). Mediates the regulation of protein translation by hormones, growth factors and other stimuli that signal through the MAP kinase and mTORC1 pathways (PubMed:8939971). {ECO:0000250|UniProtKB:Q13542, ECO:0000269|PubMed:16237163, ECO:0000269|PubMed:17029989, ECO:0000269|PubMed:20347422, ECO:0000269|PubMed:23172145, ECO:0000269|PubMed:24139800, ECO:0000269|PubMed:8939971}. PTM: Phosphorylation at Thr-37, Thr-46, Ser-65, Thr-70 and Ser-83 is mediated by MTOR and corresponds to the hyperphosphorylated form: it abolishes binding to EIF4E by inducing folding of intrinsically disordered regions. First phosphorylated at Thr-37 and Thr-46 by MTOR, inducing folding of region encompassing residues from Pro-18 to Arg-62 of into a four-stranded beta-domain that sequesters the helical YXXXXLPhi motif into a partly buried beta-strand, blocking accessibility to EIF4E. Protein phosphorylated at Thr-37 and Thr-46 is however unstable and subsequent phosphorylation at Ser-65, Thr-70 and Ser-83 is required to stabilize the fold, decreasing affinity for EIF4E by a factor of 4000. Phosphorylated in response to insulin, EGF and PDGF. {ECO:0000250|UniProtKB:Q13542, ECO:0000269|PubMed:24139800}.; PTM: Deamidated at Asn-99 and Asn-102 to aspartate (Asp) in brain. Deamidation promotes interaction with RPTOR, subsequent phosphorylation by mTORC1 and increased translation, leading to impair kinetics of excitatory synaptic transmission. Deamidation takes place during postnatal development, when the PI3K-Akt-mTOR signaling is reduced, suggesting it acts as a compensatory mechanism to promote translation despite attenuated PI3K-Akt-mTOR signaling in neuron development (PubMed:20347422). Deamidation converts Asn residues into a mixture of Asp and isoaspartate; interactions with PCMT1 is required to prevent isoaspartate accumulation and convert isoaspartate to Asp (PubMed:20424163). {ECO:0000269|PubMed:20347422, ECO:0000269|PubMed:20424163}. SUBUNIT: Hypophosphorylated EIF4EBP2 interacts with EIF4E; phosphorylation of EIF4EBP2 by mTORC1 causes dissociation of the complex allowing EIF4G1/EIF4G3 to bind and consequent initiation of translation. Interacts (via TOS motif) with RPTOR; promoting phosphorylation by mTORC1 (PubMed:20347422, PubMed:23184952). Interacts with PCMT1; required to prevent isoaspartate accumulation and convert isoaspartate to Asp (PubMed:20424163). {ECO:0000250|UniProtKB:Q13542, ECO:0000269|PubMed:20347422, ECO:0000269|PubMed:20424163, ECO:0000269|PubMed:23184952}. DOMAIN: The TOS motif mediates interaction with RPTOR, leading to promote phosphorylation by mTORC1 complex. {ECO:0000269|PubMed:20347422}.; DOMAIN: Intrinsically disordered protein that undergoes folding upon phosphorylation. Hypophosphorylated form interacts strongly with EIF4E using (1) the YXXXXLPhi motif, that undergoes a disorder-to-helix transition upon binding and (2) the secondary EIF4E binding sites (residues 78-82). Phosphorylation at Thr-37 and Thr-46 induces folding of region encompassing residues from Pro-18 to Arg-62 of into a four-stranded beta-domain that sequesters the helical YXXXXLPhi motif into a buried beta-strand, blocking accessibility to EIF4E. Protein phosphorylated at Thr-37 and Thr-46 is however unstable and subsequent phosphorylation at Ser-65, Thr-70 and Ser-83 is required to stabilize the fold, decreasing affinity for EIF4E by a factor of 4000. {ECO:0000250|UniProtKB:Q13542}. TISSUE SPECIFICITY: Enriched in brain. {ECO:0000269|PubMed:16237163}. +Q9D020 5NT3A_MOUSE Cytosolic 5'-nucleotidase 3A (EC 3.1.3.5) (7-methylguanosine phosphate-specific 5'-nucleotidase) (7-methylguanosine nucleotidase) (EC 3.1.3.91) (Cytosolic 5'-nucleotidase 3) (Cytosolic 5'-nucleotidase III) (cN-III) (Lupin) (Pyrimidine 5'-nucleotidase 1) (P5'N-1) (P5N-1) (PN-I) 331 37,252 Active site (2); Alternative sequence (1); Beta strand (11); Binding site (4); Chain (1); Helix (15); Metal binding (3); Modified residue (1); Region (1); Sequence conflict (2); Turn (3) FUNCTION: Nucleotidase which shows specific activity towards cytidine monophosphate (CMP) and 7-methylguanosine monophosphate (m(7)GMP). CMP seems to be the preferred substrate. {ECO:0000250|UniProtKB:Q9H0P0}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. SUBUNIT: Monomer. TISSUE SPECIFICITY: Isoform 2 is highly expressed in the brain, heart, spleen, kidney and blood. Isoform 2 is expressed (at protein level) in the spleen, skeletal muscle and gastrointestinal epithelia. +Q9CQ60 6PGL_MOUSE 6-phosphogluconolactonase (6PGL) (EC 3.1.1.31) 257 27,254 Chain (1); Initiator methionine (1); Modified residue (3) Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3. FUNCTION: Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +Q00896 A1AT3_MOUSE Alpha-1-antitrypsin 1-3 (Alpha-1 protease inhibitor 3) (Alpha-1 protease inhibitor 6) (Alpha-1-antitrypsin 1-6) (Serine protease inhibitor 1-3) (Serine protease inhibitor 1-6) (Serine protease inhibitor A1c) (Serpin A1c) 412 45,823 Chain (1); Glycosylation (3); Region (1); Sequence conflict (8); Signal peptide (1); Site (1) FUNCTION: Inhibitor of serine proteases. Can inhibit trypsin and chymotrypsin; relatively ineffective against elastase. {ECO:0000269|PubMed:11961105, ECO:0000269|PubMed:8619829}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11961105, ECO:0000269|PubMed:8619829}. DOMAIN: The reactive center loop (RCL) extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site within the RCL, establishing a covalent linkage between the carboxyl group of the serpin reactive site and the serine hydroxyl of the protease. The resulting inactive serpin-protease complex is highly stable (By similarity). Variability within the reactive center loop (RCL) sequences of Serpina1-related genes may determine target protease specificity. {ECO:0000250}. +Q99PG0 AAAD_MOUSE Arylacetamide deacetylase (EC 3.1.1.3) 398 45,250 Active site (3); Chain (1); Disulfide bond (1); Glycosylation (1); Motif (1); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 6 26 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 5 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 27 398 Lumenal. {ECO:0000255}. FUNCTION: Displays cellular triglyceride lipase activity in liver, increases the levels of intracellular fatty acids derived from the hydrolysis of newly formed triglyceride stores and plays a role in very low-density lipoprotein assembly (By similarity). Displays serine esterase activity in liver. Deacetylates a variety of arylacetamide substrates, including xenobiotic compounds and procarcinogens, converting them to the primary arylamide compounds and increasing their toxicity. {ECO:0000250, ECO:0000269|PubMed:19654421, ECO:0000269|PubMed:22207054}. PTM: N-glycosylated. {ECO:0000269|PubMed:19654421}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19654421}; Single-pass type II membrane protein {ECO:0000269|PubMed:19654421}. Microsome membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Highest levels in liver with lower levels in jejunum and kidney. {ECO:0000269|PubMed:19654421, ECO:0000269|PubMed:22207054}. +P30966 5HT5A_MOUSE 5-hydroxytryptamine receptor 5A (5-HT-5) (5-HT-5A) (5-HT5A) (Serotonin receptor 5A) 357 40,736 Chain (1); Disulfide bond (1); Glycosylation (2); Sequence conflict (2); Topological domain (8); Transmembrane (7) TRANSMEM 41 63 Helical; Name=1. {ECO:0000250}.; TRANSMEM 79 99 Helical; Name=2. {ECO:0000250}.; TRANSMEM 116 137 Helical; Name=3. {ECO:0000250}.; TRANSMEM 159 181 Helical; Name=4. {ECO:0000250}.; TRANSMEM 199 219 Helical; Name=5. {ECO:0000250}.; TRANSMEM 283 303 Helical; Name=6. {ECO:0000250}.; TRANSMEM 321 341 Helical; Name=7. {ECO:0000250}. TOPO_DOM 1 40 Extracellular. {ECO:0000250}.; TOPO_DOM 64 78 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 100 115 Extracellular. {ECO:0000250}.; TOPO_DOM 138 158 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 182 198 Extracellular. {ECO:0000250}.; TOPO_DOM 220 282 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 304 320 Extracellular. {ECO:0000250}.; TOPO_DOM 342 357 Cytoplasmic. {ECO:0000250}. FUNCTION: This is one of the several different receptors for 5-hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. The activity of this receptor is mediated by G proteins. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed predominantly in the central nervous system; in the cerebral cortex, hippocampus, habenula, olfactory bulb and granular layer of the cerebellum. +Q7TQI7 ABTB2_MOUSE Ankyrin repeat and BTB/POZ domain-containing protein 2 1024 113,503 Chain (1); Domain (1); Repeat (4) FUNCTION: May be involved in the initiation of hepatocyte growth. {ECO:0000250}. +Q9CXJ4 ABCB8_MOUSE ATP-binding cassette sub-family B member 8, mitochondrial 717 78,000 Chain (1); Domain (2); Nucleotide binding (1); Sequence conflict (3); Transit peptide (1); Transmembrane (5) TRANSMEM 65 85 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 127 147 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 178 198 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 278 298 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 365 385 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. SUBUNIT: Monomer. {ECO:0000305}. +Q8K2H4 ACAP1_MOUSE Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1 (Centaurin-beta-1) (Cnt-b1) 740 81,704 Chain (1); Domain (3); Modified residue (1); Mutagenesis (1); Region (3); Repeat (3); Sequence conflict (2); Zinc finger (1) FUNCTION: GTPase-activating protein (GAP) for ADP ribosylation factor 6 (ARF6) required for clathrin-dependent export of proteins from recycling endosomes to trans-Golgi network and cell surface. Required for regulated export of ITGB1 from recycling endosomes to the cell surface and ITGB1-dependent cell migration (By similarity). {ECO:0000250, ECO:0000269|PubMed:17664335}. SUBCELLULAR LOCATION: Recycling endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. SUBUNIT: Banana-shaped homodimer laterally assembling into tetramers, the tetramers further pack helically onto the membrane. Interacts with GTP-bound ARF6. Interacts with third cytoplasmic loop of SLC2A4/GLUT4. Interacts with CLTC. Interacts with GULP1. Forms a complex with GDP-bound ARF6 and GULP1. Interacts with ITGB1; required for ITGB1 recycling. {ECO:0000250|UniProtKB:Q15027, ECO:0000269|PubMed:17664335}. DOMAIN: PH domain binds phospholipids including phosphatidic acid, phosphatidylinositol 3-phosphate, phosphatidylinositol 3,5-bisphosphate (PIP2) and phosphatidylinositol 3,4,5-trisphosphate (PIP3). May mediate ACAP1-binding to PIP2 or PIP3 containing membranes. Only one PH domain of one ACAP1 dimer inserts into the membrane, while the other PH domain acts primaryly to interact with adjacent ACAP1 dimers (By similarity). {ECO:0000250|UniProtKB:Q15027}.; DOMAIN: The BAR domain mediates homodimerization, it can neither bind membrane nor impart curvature, but instead requires the neighboring PH domain to achieve these functions (By similarity). {ECO:0000250|UniProtKB:Q15027}. +Q9ERK7 ACHB2_MOUSE Neuronal acetylcholine receptor subunit beta-2 501 57,113 Chain (1); Disulfide bond (1); Glycosylation (2); Sequence conflict (1); Signal peptide (1); Site (3); Topological domain (4); Transmembrane (4) TRANSMEM 239 259 Helical. {ECO:0000255}.; TRANSMEM 268 288 Helical. {ECO:0000255}.; TRANSMEM 301 321 Helical. {ECO:0000255}.; TRANSMEM 460 480 Helical. {ECO:0000255}. TOPO_DOM 26 238 Extracellular. {ECO:0000255}.; TOPO_DOM 260 267 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 289 300 Extracellular. {ECO:0000255}.; TOPO_DOM 322 459 Cytoplasmic. {ECO:0000255}. FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane permeable to sodiun ions. {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. SUBUNIT: Neuronal AChR is composed of two different types of subunits: alpha and beta. Beta-2 subunit can be combined to alpha-2, alpha-3 or alpha-4 to give rise to functional receptors, complexes with beta-2 may be heteropentamers. Alpha-2/4:beta-2 nAChR complexes are proposed to exist in two subtypes: LS (low agonist sensitivity) with a (alpha-2/4)3:(beta-2)2 and HS (high agonist sensitivity) with a (alpha-2/4)2:(beta-2)3 stoichiometry; the subtypes differ in their subunit binding interfaces which are involved in ligand binding. Interacts with RIC3; which is required for proper folding and assembly. Interacts with LYPD6. The heteropentamer alpha3-beta-2 interacts with alpha-cconotoxins BuIA, MII, ImI, ImII, PnIA and GID (By similarity). The heteropentamer alpha-4-beta-2 interacts with the alpha-conotoxins PnIA, GID and MII (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P12390, ECO:0000250|UniProtKB:P17787}. +P23979 5HT3A_MOUSE 5-hydroxytryptamine receptor 3A (5-HT3-A) (5-HT3A) (5-hydroxytryptamine receptor 3) (5-HT-3) (5-HT3R) (Serotonin receptor 3A) (Serotonin-gated ion channel receptor) 487 56,056 Alternative sequence (1); Beta strand (14); Chain (1); Disulfide bond (1); Glycosylation (3); Helix (9); Region (1); Sequence conflict (10); Signal peptide (1); Topological domain (5); Transmembrane (4); Turn (3) TRANSMEM 246 272 Helical; Name=1. {ECO:0000255}.; TRANSMEM 278 296 Helical; Name=2. {ECO:0000255}.; TRANSMEM 306 324 Helical; Name=3. {ECO:0000255}.; TRANSMEM 465 484 Helical; Name=4. {ECO:0000255}. TOPO_DOM 24 245 Extracellular. {ECO:0000255}.; TOPO_DOM 273 277 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 297 305 Extracellular. {ECO:0000255}.; TOPO_DOM 325 464 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 485 487 Extracellular. {ECO:0000255}. FUNCTION: This is one of the several different receptors for 5-hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. This receptor is a ligand-gated ion channel, which when activated causes fast, depolarizing responses in neurons. It is a cation-specific, but otherwise relatively nonselective, ion channel. {ECO:0000269|PubMed:12867984}. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. SUBUNIT: Forms pentahomomeric complex as well as pentaheteromeric complex with HTR3B; homomeric complex is functional but exhibits low conductance with modified voltage dependence, and decreased agonist and antagonist affinity. Interacts with RIC3 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Brain, spinal cord, and heart. +Q67BJ4 A4GAT_MOUSE Lactosylceramide 4-alpha-galactosyltransferase (EC 2.4.1.228) (Alpha-1,4-N-acetylglucosaminyltransferase) (Alpha-1,4-galactosyltransferase) (Alpha4Gal-T1) (Globotriaosylceramide synthase) (Gb3 synthase) (UDP-galactose:beta-D-galactosyl-beta1-R 4-alpha-D-galactosyltransferase) 359 41,366 Chain (1); Glycosylation (2); Motif (1); Topological domain (2); Transmembrane (1) TRANSMEM 31 51 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 30 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 52 359 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Necessary for the biosynthesis of the Pk antigen of blood histogroup P. Catalyzes the transfer of galactose to lactosylceramide and galactosylceramide. Necessary for the synthesis of the receptor for bacterial verotoxins (By similarity). {ECO:0000250|UniProtKB:Q9NPC4}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. DOMAIN: The conserved DXD motif is involved in enzyme activity. {ECO:0000250}. +Q64343 ABCG1_MOUSE ATP-binding cassette sub-family G member 1 (ATP-binding cassette transporter 8) (White protein homolog) 666 74,033 Chain (1); Domain (2); Lipidation (4); Nucleotide binding (1); Topological domain (7); Transmembrane (6) TRANSMEM 415 433 Helical. {ECO:0000255}.; TRANSMEM 445 465 Helical. {ECO:0000255}.; TRANSMEM 495 513 Helical. {ECO:0000255}.; TRANSMEM 522 543 Helical. {ECO:0000255}.; TRANSMEM 556 574 Helical. {ECO:0000255}.; TRANSMEM 638 657 Helical. {ECO:0000255}. TOPO_DOM 1 414 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 434 444 Extracellular. {ECO:0000255}.; TOPO_DOM 466 494 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 514 521 Extracellular. {ECO:0000255}.; TOPO_DOM 544 555 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 575 637 Extracellular. {ECO:0000255}.; TOPO_DOM 658 666 Cytoplasmic. {ECO:0000255}. FUNCTION: Transporter involved in macrophage lipid homeostasis. Is an active component of the macrophage lipid export complex. Could also be involved in intracellular lipid transport processes. The role in cellular lipid homeostasis may not be limited to macrophages. {ECO:0000269|PubMed:14668945}. PTM: Palmitoylation at Cys-315 seems important for trafficking from the endoplasmic reticulum. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed mainly in brain, thymus, lung, adrenals, spleen and placenta. Little or no expression in liver, kidney, heart, muscle or testes. +Q8K441 ABCA6_MOUSE ATP-binding cassette sub-family A member 6 1624 183,283 Alternative sequence (2); Chain (1); Domain (2); Glycosylation (3); Nucleotide binding (2); Sequence conflict (2); Transmembrane (15) TRANSMEM 31 51 Helical. {ECO:0000255}.; TRANSMEM 222 242 Helical. {ECO:0000255}.; TRANSMEM 267 287 Helical. {ECO:0000255}.; TRANSMEM 297 317 Helical. {ECO:0000255}.; TRANSMEM 326 346 Helical. {ECO:0000255}.; TRANSMEM 356 376 Helical. {ECO:0000255}.; TRANSMEM 395 415 Helical. {ECO:0000255}.; TRANSMEM 854 874 Helical. {ECO:0000255}.; TRANSMEM 971 991 Helical. {ECO:0000255}.; TRANSMEM 1005 1025 Helical. {ECO:0000255}.; TRANSMEM 1058 1078 Helical. {ECO:0000255}.; TRANSMEM 1094 1114 Helical. {ECO:0000255}.; TRANSMEM 1130 1150 Helical. {ECO:0000255}.; TRANSMEM 1154 1174 Helical. {ECO:0000255}.; TRANSMEM 1194 1214 Helical. {ECO:0000255}. FUNCTION: Probable transporter which may play a role in macrophage lipid homeostasis. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Widely expressed with higher expression in heart, lung, brain, spleen and testis. {ECO:0000269|PubMed:12532264}. +P51908 ABEC1_MOUSE C->U-editing enzyme APOBEC-1 (EC 3.5.4.36) (Apolipoprotein B mRNA-editing enzyme 1) (mRNA(cytosine(6666)) deaminase 1) 229 27,522 Active site (1); Chain (1); Compositional bias (1); Domain (1); Metal binding (3); Sequence conflict (1) FUNCTION: Catalytic component of the apolipoprotein B mRNA editing enzyme complex which is responsible for the postranscriptional editing of a CAA codon for Gln to a UAA codon for stop in the APOB mRNA. May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation. {ECO:0000269|PubMed:21496894}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P41238}. SUBUNIT: Homodimer. Part of the apolipoprotein B mRNA editing complex with APC. Interacts with HNRPAB and SYNCRIP. {ECO:0000250|UniProtKB:P41238}. TISSUE SPECIFICITY: Expressed in the spleen. Expressed at lower level in the kidney, testis, lung, brain and liver. {ECO:0000269|PubMed:12859895}. +Q99J72 ABEC3_MOUSE DNA dC->dU-editing enzyme APOBEC-3 (EC 3.5.4.38) (Apolipoprotein B mRNA-editing complex 3) (Arp3) (CEM-15) (CEM15) 440 52,213 Active site (1); Alternative sequence (3); Chain (1); Domain (2); Erroneous initiation (3); Metal binding (6); Mutagenesis (4); Natural variant (36); Sequence conflict (7) FUNCTION: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single-or double-stranded RNA. Exhibits antiviral activity against HIV-1, simian immunodeficiency viruses (SIVs), mouse mammary tumor virus (MMTV) and friend murine leukemia virus (FrMLV) and may inhibit the mobility of LTR retrotransposons. {ECO:0000269|PubMed:16378963, ECO:0000269|PubMed:16527742, ECO:0000269|PubMed:17259974, ECO:0000269|PubMed:18786991}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16527742}. SUBUNIT: Homodimer. Interacts with mouse mammary tumor virus (MMTV) nucleocapsid protein p14. {ECO:0000269|PubMed:17020885, ECO:0000269|PubMed:17259974}. DOMAIN: The CMP/dCMP deaminase domain 1 confers deoxycytidine deaminase activity, whereas the CMP/dCMP deaminase domain 2 mediates RNA-dependent oligomerization and virion incorporation. {ECO:0000269|PubMed:17020885}. TISSUE SPECIFICITY: Expressed in spleen, node and lung. {ECO:0000269|PubMed:12859895}. +Q8VD66 ABHD4_MOUSE Protein ABHD4 (EC 3.-.-.-) (Alpha/beta hydrolase domain-containing protein 4) (Abhydrolase domain-containing protein 4) (Alpha/beta-hydrolase 4) (Lyso-N-acylphosphatidylethanolamine lipase) 342 38,861 Chain (1); Domain (1) FUNCTION: Lysophospholipase selective for N-acyl phosphatidylethanolamine (NAPE). Contributes to the biosynthesis of N-acyl ethanolamines, including the endocannabinoid anandamide by hydrolyzing the sn-1 and sn-2 acyl chains from N-acyl phosphatidylethanolamine (NAPE) generating glycerophospho-N-acyl ethanolamine (GP-NAE), an intermediate for N-acyl ethanolamine biosynthesis. Hydrolyzes substrates bearing saturated, monounsaturated, polyunsaturated N-acyl chains. Shows no significant activity towards other lysophospholipids, including lysophosphatidylcholine, lysophosphatidylethanolamine and lysophosphatidylserine. {ECO:0000269|PubMed:16818490}. TISSUE SPECIFICITY: Highest levels in the CNS and in testis, intermediate levels in liver and kidney. Hardly detectable in heart. {ECO:0000269|PubMed:16818490}. +Q7M759 AB17B_MOUSE Alpha/beta hydrolase domain-containing protein 17B (Abhydrolase domain-containing protein 17B) (EC 3.1.2.22) 288 32,201 Active site (3); Chain (1); Modified residue (1); Mutagenesis (5) FUNCTION: Hydrolyzes fatty acids from S-acylated cysteine residues in proteins (PubMed:27307232). Has depalmitoylating activity towards DLG4/PSD95 (PubMed:27307232). Has depalmitoylating activity towards GAP43 (PubMed:27307232). Has depalmitoylating activity towards MAP6 (PubMed:28521134). Has depalmitoylating activity towards NRAS (By similarity). {ECO:0000250|UniProtKB:Q5VST6, ECO:0000269|PubMed:27307232, ECO:0000305|PubMed:28521134}. PTM: Palmitoylated on cysteine residues located in a cysteine cluster at the N-terminus which promotes membrane localization. Palmitoylation is required for post-synaptic localization and for depalmitoylating activity towards DLG4/PSD95. {ECO:0000269|PubMed:27307232}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27307232}; Lipid-anchor {ECO:0000269|PubMed:27307232}; Cytoplasmic side {ECO:0000269|PubMed:27307232}. Recycling endosome membrane {ECO:0000269|PubMed:27307232}; Lipid-anchor {ECO:0000269|PubMed:27307232}; Cytoplasmic side {ECO:0000269|PubMed:27307232}. Cell projection, dendritic spine {ECO:0000269|PubMed:27307232}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000269|PubMed:27307232}. TISSUE SPECIFICITY: Expressed in brain. {ECO:0000269|PubMed:27307232}. +Q8K442 ABC8A_MOUSE ATP-binding cassette sub-family A member 8-A 1620 184,180 Chain (1); Domain (2); Frameshift (1); Glycosylation (3); Nucleotide binding (2); Sequence conflict (3); Transmembrane (15) TRANSMEM 30 50 Helical. {ECO:0000255}.; TRANSMEM 224 244 Helical. {ECO:0000255}.; TRANSMEM 263 283 Helical. {ECO:0000255}.; TRANSMEM 294 314 Helical. {ECO:0000255}.; TRANSMEM 328 348 Helical. {ECO:0000255}.; TRANSMEM 357 377 Helical. {ECO:0000255}.; TRANSMEM 397 417 Helical. {ECO:0000255}.; TRANSMEM 861 881 Helical. {ECO:0000255}.; TRANSMEM 979 999 Helical. {ECO:0000255}.; TRANSMEM 1019 1039 Helical. {ECO:0000255}.; TRANSMEM 1068 1088 Helical. {ECO:0000255}.; TRANSMEM 1105 1125 Helical. {ECO:0000255}.; TRANSMEM 1133 1153 Helical. {ECO:0000255}.; TRANSMEM 1159 1179 Helical. {ECO:0000255}.; TRANSMEM 1196 1216 Helical. {ECO:0000255}. FUNCTION: ATP-dependent lipophilic drug transporter. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Expressed in lung, heart, liver, skeletal muscle and testis. {ECO:0000269|PubMed:12532264, ECO:0000269|PubMed:16445568}. +P05202 AATM_MOUSE Aspartate aminotransferase, mitochondrial (mAspAT) (EC 2.6.1.1) (EC 2.6.1.7) (Fatty acid-binding protein) (FABP-1) (Glutamate oxaloacetate transaminase 2) (Kynurenine aminotransferase 4) (Kynurenine aminotransferase IV) (Kynurenine--oxoglutarate transaminase 4) (Kynurenine--oxoglutarate transaminase IV) (Plasma membrane-associated fatty acid-binding protein) (FABPpm) (Transaminase A) 430 47,411 Beta strand (10); Binding site (4); Chain (1); Helix (18); Modified residue (39); Sequence conflict (5); Transit peptide (1); Turn (6) FUNCTION: Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Plays a key role in amino acid metabolism. Important for metabolite exchange between mitochondria and cytosol. Facilitates cellular uptake of long-chain free fatty acids. {ECO:0000269|PubMed:20977429, ECO:0000269|PubMed:7878064}. PTM: Acetylation of Lys-296, Lys-345 and Lys-363 is observed in liver mitochondria from fasted mice but not from fed mice. SUBCELLULAR LOCATION: Mitochondrion matrix. Cell membrane. SUBUNIT: Homodimer. {ECO:0000269|PubMed:19826765, ECO:0000269|PubMed:20977429}. TISSUE SPECIFICITY: Detected in brain (at protein level). {ECO:0000269|PubMed:17442055}. +P09690 ACHB_MOUSE Acetylcholine receptor subunit beta 501 56,931 Chain (1); Disulfide bond (1); Glycosylation (1); Modified residue (1); Signal peptide (1); Topological domain (2); Transmembrane (4) TRANSMEM 245 269 Helical. {ECO:0000255}.; TRANSMEM 277 295 Helical. {ECO:0000255}.; TRANSMEM 311 332 Helical. {ECO:0000255}.; TRANSMEM 470 488 Helical. {ECO:0000255}. TOPO_DOM 24 244 Extracellular. {ECO:0000255}.; TOPO_DOM 333 469 Cytoplasmic. {ECO:0000255}. FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. SUBUNIT: Pentamer of two alpha chains, and one each of the beta, delta, and gamma (in immature muscle) or epsilon (in mature muscle) chains. The muscle heteropentamer composed of alpha-1, beta-1, delta, epsilon subunits interacts with the alpha-conotoxin ImII. {ECO:0000250|UniProtKB:P11230}. +Q6PD03 2A5A_MOUSE Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform (PP2A B subunit isoform B'-alpha) (PP2A B subunit isoform B56-alpha) (PP2A B subunit isoform PR61-alpha) (PR61alpha) (PP2A B subunit isoform R5-alpha) 486 56,347 Chain (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (4) FUNCTION: The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Chromosome, centromere {ECO:0000250}. Note=From mitotic prophase to metaphase, localizes at the inner centromere between a pair of sister kinetochores. Decreased expression at the onset of anaphase (By similarity). {ECO:0000250}. SUBUNIT: PP2A consists of a common heterodimeric core enzyme, composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant regulatory subunit (PR65 or subunit A), that associates with a variety of regulatory subunits. Proteins that associate with the core dimer include three families of regulatory subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa variable regulatory subunit, viral proteins, and cell signaling molecules. Interacts with SGO1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed with highest levels in thymus and ovary. {ECO:0000269|PubMed:15095873}. +P62259 1433E_MOUSE 14-3-3 protein epsilon (14-3-3E) 255 29,174 Chain (1); Cross-link (1); Modified residue (10); Site (2) FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Positively regulates phosphorylated protein HSF1 nuclear export to the cytoplasm. {ECO:0000250|UniProtKB:P62258, ECO:0000250|UniProtKB:P62261}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P62258}. Cytoplasm {ECO:0000250|UniProtKB:P62258}. Melanosome {ECO:0000250|UniProtKB:P62258}. SUBUNIT: Homodimer (By similarity). Heterodimerizes with YWHAZ (By similarity). Interacts with PKA-phosphorylated AANAT (By similarity). Interacts with ABL1 (phosphorylated form); the interaction retains it in the cytoplasm (By similarity). Interacts with ARHGEF28 (PubMed:11533041). Interacts with BEX3 (PubMed:11278287). Weakly interacts with CDKN1B (By similarity). Interacts with the 'Thr-369' phosphorylated form of DAPK2 (PubMed:26047703). Interacts with DENND1A (By similarity). Interacts with GAB2 (By similarity). Interacts with phosphorylated GRB10 (PubMed:15722337). Interacts with KSR1 (PubMed:10409742). Interacts with NDEL1 (PubMed:12796778). Interacts with PI4KB, TBC1D22A and TBC1D22B (By similarity). Interacts with the phosphorylated (by AKT1) form of SRPK2 (By similarity). Interacts with TIAM2 (PubMed:17320046). Interacts with the 'Ser-1134' and 'Ser-1161' phosphorylated form of SOS1 (By similarity). Interacts with ZFP36 (via phosphorylated form) (PubMed:21078877). Interacts with SLITRK1 (By similarity). Interacts with HSF1 (via phosphorylated form); this interaction promotes HSF1 sequestration in the cytoplasm in a ERK-dependent manner (By similarity). Interacts with RIPOR2 (By similarity). Interacts with KLHL22; required for the nuclear localization of KLHL22 upon amino acid starvation (By similarity). {ECO:0000250|UniProtKB:P62258, ECO:0000250|UniProtKB:P62260, ECO:0000269|PubMed:10409742, ECO:0000269|PubMed:11278287, ECO:0000269|PubMed:11533041, ECO:0000269|PubMed:12796778, ECO:0000269|PubMed:15722337, ECO:0000269|PubMed:17320046, ECO:0000269|PubMed:21078877, ECO:0000269|PubMed:26047703}. +Q80VV3 4EBP3_MOUSE Eukaryotic translation initiation factor 4E-binding protein 3 (4E-BP3) (eIF4E-binding protein 3) 101 11,019 Chain (1); Motif (2) FUNCTION: Repressor of translation initiation that regulates EIF4E activity by preventing its assembly into the eIF4F complex: hypophosphorylated form competes with EIF4G1/EIF4G3 and strongly binds to EIF4E, leading to repress translation. In contrast, hyperphosphorylated form dissociates from EIF4E, allowing interaction between EIF4G1/EIF4G3 and EIF4E, leading to initiation of translation. {ECO:0000250|UniProtKB:Q13541}. PTM: Phosphorylated. {ECO:0000250|UniProtKB:O60516}. SUBUNIT: EIF4EBP3 interacts with EIF4E. {ECO:0000250|UniProtKB:O60516}. +Q3V1L4 5NTC_MOUSE Cytosolic purine 5'-nucleotidase (EC 3.1.3.5) (Cytosolic 5'-nucleotidase II) 560 64,809 Active site (2); Binding site (5); Chain (1); Compositional bias (1); Metal binding (3); Modified residue (4); Region (1); Sequence conflict (4) FUNCTION: May have a critical role in the maintenance of a constant composition of intracellular purine/pyrimidine nucleotides in cooperation with other nucleotidases. Preferentially hydrolyzes inosine 5'-monophosphate (IMP) and other purine nucleotides (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homotetramer. {ECO:0000250}. +Q61618 AA3R_MOUSE Adenosine receptor A3 (A3AR) 319 36,449 Chain (1); Disulfide bond (1); Glycosylation (3); Lipidation (1); Sequence conflict (3); Topological domain (8); Transmembrane (7) TRANSMEM 16 38 Helical; Name=1. {ECO:0000250}.; TRANSMEM 50 73 Helical; Name=2. {ECO:0000250}.; TRANSMEM 86 107 Helical; Name=3. {ECO:0000250}.; TRANSMEM 128 149 Helical; Name=4. {ECO:0000250}.; TRANSMEM 179 199 Helical; Name=5. {ECO:0000250}.; TRANSMEM 233 256 Helical; Name=6. {ECO:0000250}.; TRANSMEM 263 285 Helical; Name=7. {ECO:0000250}. TOPO_DOM 1 15 Extracellular. {ECO:0000250}.; TOPO_DOM 39 49 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 74 85 Extracellular. {ECO:0000250}.; TOPO_DOM 108 127 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 150 178 Extracellular. {ECO:0000250}.; TOPO_DOM 200 232 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 257 262 Extracellular. {ECO:0000250}.; TOPO_DOM 286 319 Cytoplasmic. {ECO:0000250}. FUNCTION: Receptor for adenosine. The activity of this receptor is mediated by G proteins which inhibits adenylyl cyclase. {ECO:0000250|UniProtKB:P0DMS8}. PTM: Phosphorylation on Thr-317 and Thr-318 may be crucial for rapid desensitization. Phosphorylation on Thr-317 may be necessary for phosphorylation on Thr-318 to occur. {ECO:0000250|UniProtKB:P28647}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q28309}; Multi-pass membrane protein {ECO:0000255}. +Q8BGM7 AAKG3_MOUSE 5'-AMP-activated protein kinase subunit gamma-3 (AMPK gamma3) (AMPK subunit gamma-3) 489 53,849 Alternative sequence (1); Binding site (9); Chain (1); Domain (4); Motif (1); Nucleotide binding (6); Sequence conflict (1) FUNCTION: AMP/ATP-binding subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (PRKAA1 or PRKAA2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits. ADP also stimulates phosphorylation, without stimulating already phosphorylated catalytic subunit. ATP promotes dephosphorylation of catalytic subunit, rendering the AMPK enzyme inactive (By similarity). {ECO:0000250}. PTM: Phosphorylated by ULK1; leading to negatively regulate AMPK activity and suggesting the existence of a regulatory feedback loop between ULK1 and AMPK. {ECO:0000269|PubMed:21460634}. SUBUNIT: AMPK is a heterotrimer of an alpha catalytic subunit (PRKAA1 or PRKAA2), a beta (PRKAB1 or PRKAB2) and a gamma non-catalytic subunits (PRKAG1, PRKAG2 or PRKAG3). Interacts with FNIP1 and FNIP2 (By similarity). {ECO:0000250}. DOMAIN: The AMPK pseudosubstrate motif resembles the sequence around sites phosphorylated on target proteins of AMPK, except the presence of a non-phosphorylatable residue in place of Ser. In the absence of AMP this pseudosubstrate sequence may bind to the active site groove on the alpha subunit (PRKAA1 or PRKAA2), preventing phosphorylation by the upstream activating kinase STK11/LKB1 (By similarity). {ECO:0000250}.; DOMAIN: The 4 CBS domains mediate binding to nucleotides. Of the 4 potential nucleotide-binding sites, 3 are occupied, designated as sites 1, 3, and 4 based on the CBS modules that provide the acidic residue for coordination with the 2'- and 3'-hydroxyl groups of the ribose of AMP. Of these, site 4 appears to be a structural site that retains a tightly held AMP molecule (AMP 3). The 2 remaining sites, 1 and 3, can bind either AMP, ADP or ATP. Site 1 (AMP, ADP or ATP 1) is the high-affinity binding site and likely accommodates AMP or ADP. Site 3 (AMP, ADP or ATP 2) is the weakest nucleotide-binding site on the gamma subunit, yet it is exquisitely sensitive to changes in nucleotide levels and this allows AMPK to respond rapidly to changes in cellular energy status. Site 3 is likely to be responsible for protection of a conserved threonine in the activation loop of the alpha catalytic subunit through conformational changes induced by binding of AMP or ADP. {ECO:0000250|UniProtKB:P80385}. +Q8R0P4 AAMDC_MOUSE Mth938 domain-containing protein (LI2) 122 13,244 Alternative sequence (1); Chain (1); Region (1) FUNCTION: May play a role in preadipocyte differentiation and adipogenesis. {ECO:0000269|PubMed:22279136}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21622130}. Note=Diffuse distribution with some highly concentrated spots around the nucleus. TISSUE SPECIFICITY: Widely expressed, with high expression in the adipose tissue and skeletal muscle (at protein level). {ECO:0000269|PubMed:21622130}. +Q8K448 ABCA5_MOUSE ATP-binding cassette sub-family A member 5 1642 185,895 Chain (1); Domain (2); Erroneous initiation (1); Glycosylation (5); Nucleotide binding (2); Sequence conflict (14); Transmembrane (15) TRANSMEM 32 52 Helical. {ECO:0000255}.; TRANSMEM 220 240 Helical. {ECO:0000255}.; TRANSMEM 264 284 Helical. {ECO:0000255}.; TRANSMEM 297 317 Helical. {ECO:0000255}.; TRANSMEM 328 348 Helical. {ECO:0000255}.; TRANSMEM 355 375 Helical. {ECO:0000255}.; TRANSMEM 396 416 Helical. {ECO:0000255}.; TRANSMEM 864 884 Helical. {ECO:0000255}.; TRANSMEM 967 987 Helical. {ECO:0000255}.; TRANSMEM 1021 1041 Helical. {ECO:0000255}.; TRANSMEM 1071 1091 Helical. {ECO:0000255}.; TRANSMEM 1102 1122 Helical. {ECO:0000255}.; TRANSMEM 1138 1158 Helical. {ECO:0000255}.; TRANSMEM 1164 1184 Helical. {ECO:0000255}.; TRANSMEM 1207 1227 Helical. {ECO:0000255}. FUNCTION: May play a role in the processing of autolysosomes. {ECO:0000269|PubMed:15870284}. PTM: N-glycosylated. {ECO:0000269|PubMed:15870284}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Lysosome membrane {ECO:0000269|PubMed:15870284}; Multi-pass membrane protein {ECO:0000269|PubMed:15870284}. Late endosome membrane {ECO:0000269|PubMed:15870284}; Multi-pass membrane protein {ECO:0000269|PubMed:15870284}. TISSUE SPECIFICITY: Expressed in cardiomyocytes, oligodendrocytes and astrocytes in brain, alveolar type 2 cells in lung and follicular cells in the thyroid gland (at protein level). Detected in brain, testis, lung, heart, liver, kidney, skeletal muscle and placenta. {ECO:0000269|PubMed:12532264, ECO:0000269|PubMed:15870284}. +Q8K449 ABCA9_MOUSE ATP-binding cassette sub-family A member 9 1623 183,114 Chain (1); Domain (2); Glycosylation (1); Nucleotide binding (2); Sequence conflict (1); Transmembrane (14) TRANSMEM 31 51 Helical. {ECO:0000255}.; TRANSMEM 225 245 Helical. {ECO:0000255}.; TRANSMEM 265 285 Helical. {ECO:0000255}.; TRANSMEM 295 315 Helical. {ECO:0000255}.; TRANSMEM 329 349 Helical. {ECO:0000255}.; TRANSMEM 354 374 Helical. {ECO:0000255}.; TRANSMEM 398 418 Helical. {ECO:0000255}.; TRANSMEM 863 883 Helical. {ECO:0000255}.; TRANSMEM 1025 1045 Helical. {ECO:0000255}.; TRANSMEM 1071 1091 Helical. {ECO:0000255}.; TRANSMEM 1107 1127 Helical. {ECO:0000255}.; TRANSMEM 1135 1155 Helical. {ECO:0000255}.; TRANSMEM 1163 1183 Helical. {ECO:0000255}.; TRANSMEM 1199 1219 Helical. {ECO:0000255}. FUNCTION: May play a role in monocyte differentiation and lipid homeostasis. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Highly expressed in heart and to lower extent in kidney, brain and spleen. {ECO:0000269|PubMed:12532264}. +Q99J27 ACATN_MOUSE Acetyl-coenzyme A transporter 1 (AT-1) (Acetyl-CoA transporter 1) (Solute carrier family 33 member 1) 550 61,075 Chain (1); Glycosylation (1); Modified residue (1); Sequence conflict (8); Topological domain (12); Transmembrane (11) TRANSMEM 75 95 Helical. {ECO:0000255}.; TRANSMEM 114 134 Helical. {ECO:0000255}.; TRANSMEM 142 162 Helical. {ECO:0000255}.; TRANSMEM 176 196 Helical. {ECO:0000255}.; TRANSMEM 218 238 Helical. {ECO:0000255}.; TRANSMEM 257 277 Helical. {ECO:0000255}.; TRANSMEM 301 321 Helical. {ECO:0000255}.; TRANSMEM 345 365 Helical. {ECO:0000255}.; TRANSMEM 376 396 Helical. {ECO:0000255}.; TRANSMEM 406 426 Helical. {ECO:0000255}.; TRANSMEM 510 530 Helical. {ECO:0000255}. TOPO_DOM 1 74 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 96 113 Extracellular. {ECO:0000255}.; TOPO_DOM 135 141 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 163 175 Extracellular. {ECO:0000255}.; TOPO_DOM 197 217 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 239 256 Extracellular. {ECO:0000255}.; TOPO_DOM 278 300 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 322 344 Extracellular. {ECO:0000255}.; TOPO_DOM 366 375 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 397 405 Extracellular. {ECO:0000255}.; TOPO_DOM 427 509 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 531 550 Extracellular. {ECO:0000255}. FUNCTION: Probable acetyl-CoA transporter necessary for O-acetylation of gangliosides (PubMed:10570973). Negatively regulates BMP signaling (By similarity). {ECO:0000250|UniProtKB:O00400, ECO:0000269|PubMed:10570973}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in all adult tissues examined including brain, heart, kidney, liver and spleen, with maximum expression in liver and kidney. {ECO:0000269|PubMed:10570973}. +Q5SSL4 ABR_MOUSE Active breakpoint cluster region-related protein 859 97,667 Alternative sequence (4); Chain (1); Domain (4); Erroneous gene model prediction (2); Modified residue (1); Sequence conflict (2) FUNCTION: GTPase-activating protein for RAC and CDC42. Promotes the exchange of RAC or CDC42-bound GDP by GTP, thereby activating them (By similarity). {ECO:0000250}. +D0G895 ACE3_MOUSE Angiotensin-converting enzyme-like protein Ace3 737 85,874 Chain (1); Glycosylation (1); Signal peptide (1); Topological domain (3); Transmembrane (2) TRANSMEM 640 660 Helical. {ECO:0000255}.; TRANSMEM 701 721 Helical. {ECO:0000255}. TOPO_DOM 24 639 Extracellular. {ECO:0000305}.; TOPO_DOM 661 700 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 722 737 Extracellular. {ECO:0000305}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome membrane {ECO:0000269|PubMed:20421979}; Multi-pass membrane protein {ECO:0000255}. Note=Disappears from acrosome reacted sperm. Co-localizes with IZUMO1 at acrosomal cap area. {ECO:0000269|PubMed:20421979}. SUBUNIT: Interacts with IZUMO1. {ECO:0000269|PubMed:20421979}. TISSUE SPECIFICITY: Expressed in sperm and testis (at protein level) (PubMed:20421979). Expressed in heart and testis (PubMed:17597519). Not detected in kidney, lung, liver, brain, ovary, spleen and thymus (PubMed:17597519, PubMed:20421979). {ECO:0000269|PubMed:17597519, ECO:0000269|PubMed:20421979}. +Q9CQV8 1433B_MOUSE 14-3-3 protein beta/alpha (Protein kinase C inhibitor protein 1) (KCIP-1) [Cleaved into: 14-3-3 protein beta/alpha, N-terminally processed] 246 28,086 Alternative sequence (1); Chain (2); Cross-link (1); Helix (11); Initiator methionine (1); Modified residue (13); Sequence conflict (4); Site (2); Turn (1) FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negative regulator of osteogenesis. Blocks the nuclear translocation of the phosphorylated form (by AKT1) of SRPK2 and antagonizes its stimulatory effect on cyclin D1 expression resulting in blockage of neuronal apoptosis elicited by SRPK2. Negative regulator of signaling cascades that mediate activation of MAP kinases via AKAP13. {ECO:0000250|UniProtKB:P31946}. PTM: Isoform alpha differs from isoform beta in being phosphorylated (By similarity). Phosphorylated on Ser-60 by protein kinase C delta type catalytic subunit in a sphingosine-dependent fashion. {ECO:0000250, ECO:0000269|PubMed:9705322}.; PTM: Isoform Short contains a N-acetylmethionine at position 1. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P31946}. Melanosome {ECO:0000250|UniProtKB:P31946}. SUBUNIT: Homodimer (By similarity). Interacts with SAMSN1 and PRKCE (PubMed:18604201, PubMed:20478393). Interacts with AKAP13. Interacts with SSH1 and TORC2/CRTC2. Interacts with ABL1; the interaction results in cytoplasmic location of ABL1 and inhibition of cABL-mediated apoptosis. Interacts with ROR2 (dimer); the interaction results in phosphorylation of YWHAB on tyrosine residues. Interacts with GAB2. Interacts with YAP1 (phosphorylated form). Interacts with the phosphorylated (by AKT1) form of SRPK2. Interacts with PKA-phosphorylated AANAT. Interacts with MYO1C. Interacts with SIRT2 (By similarity). Interacts with the 'Thr-369' phosphorylated form of DAPK2 (PubMed:26047703). Interacts with PI4KB, TBC1D22A and TBC1D22B. Interacts with the 'Ser-1134' and 'Ser-1161' phosphorylated form of SOS1 (By similarity). Interacts (via phosphorylated form) with YWHAB; this interaction occurs in a protein kinase AKT1-dependent manner (By similarity). Interacts with SLITRK1 (By similarity). Interacts with SYNPO2 (phosphorylated form); YWHAB competes with ACTN2 for interaction with SYNPO2 (PubMed:15883195). Interacts with RIPOR2 (via phosphorylated form); this interaction occurs in a chemokine-dependent manner and does not compete for binding of RIPOR2 with RHOA nor blocks inhibition of RIPOR2-mediated RHOA activity (By similarity). {ECO:0000250|UniProtKB:P31946, ECO:0000269|PubMed:15883195, ECO:0000269|PubMed:18604201, ECO:0000269|PubMed:20478393, ECO:0000269|PubMed:26047703}. +Q61151 2A5E_MOUSE Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit epsilon isoform (PP2A B subunit isoform B'-epsilon) (PP2A B subunit isoform B56-epsilon) (PP2A B subunit isoform PR61-epsilon) (PP2A B subunit isoform R5-epsilon) 467 54,713 Chain (1); Erroneous initiation (1); Frameshift (1); Initiator methionine (1); Modified residue (5); Sequence conflict (4) FUNCTION: The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment. Interacts with cyclin G in vitro. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: PP2A consists of a common heterodimeric core enzyme, composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant regulatory subunit (PR65 or subunit A), that associates with a variety of regulatory subunits. Proteins that associate with the core dimer include three families of regulatory subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa variable regulatory subunit, viral proteins, and cell signaling molecules. Interacts with SGO1. Found in a complex with at least ARL2, PPP2CB; PPP2R1A, PPP2R2A, PPP2R5E and TBCD (By similarity). {ECO:0000250}. +Q3UX83 1A1L2_MOUSE Probable inactive 1-aminocyclopropane-1-carboxylate synthase-like protein 2 (ACC synthase-like protein 2) 580 66,129 Alternative sequence (1); Chain (1); Modified residue (1) +O35469 3BHS6_MOUSE 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 6 (EC 1.1.1.-) (3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type VI) (3-beta-HSD VI) [Includes: 3-beta-hydroxy-Delta(5)-steroid dehydrogenase (EC 1.1.1.145) (3-beta-hydroxy-5-ene steroid dehydrogenase) (Progesterone reductase); Steroid Delta-isomerase (EC 5.3.3.1) (Delta-5-3-ketosteroid isomerase)] 373 41,977 Active site (1); Binding site (1); Chain (1); Sequence conflict (3); Transmembrane (1) TRANSMEM 288 308 Helical. {ECO:0000255}. Lipid metabolism; steroid biosynthesis. FUNCTION: 3-beta-HSD is a bifunctional enzyme, that catalyzes the oxidative conversion of Delta(5)-ene-3-beta-hydroxy steroid, and the oxidative conversion of ketosteroids. The 3-beta-HSD enzymatic system plays a crucial role in the biosynthesis of all classes of hormonal steroids. May be involved in local production of progesterone. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. Mitochondrion membrane; Single-pass membrane protein. TISSUE SPECIFICITY: Expressed in skin and testis. +Q3UKZ7 A14EL_MOUSE ARL14 effector protein-like 152 17,541 Chain (1); Compositional bias (1) +P10852 4F2_MOUSE 4F2 cell-surface antigen heavy chain (4F2hc) (Solute carrier family 3 member 2) (CD antigen CD98) 526 58,337 Alternative sequence (1); Chain (1); Cross-link (2); Disulfide bond (1); Erroneous initiation (1); Glycosylation (8); Modified residue (6); Mutagenesis (1); Topological domain (2); Transmembrane (1) TRANSMEM 76 99 Helical; Signal-anchor for type II membrane protein. TOPO_DOM 1 75 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 100 526 Extracellular. {ECO:0000255}. FUNCTION: Required for the function of light chain amino-acid transporters. Involved in sodium-independent, high-affinity transport of large neutral amino acids such as phenylalanine, tyrosine, leucine, arginine and tryptophan. Involved in guiding and targeting of LAT1 and LAT2 to the plasma membrane. When associated with SLC7A6 or SLC7A7 acts as an arginine/glutamine exchanger, following an antiport mechanism for amino acid transport, influencing arginine release in exchange for extracellular amino acids. Plays a role in nitric oxide synthesis in human umbilical vein endothelial cells (HUVECs) via transport of L-arginine. Required for normal and neoplastic cell growth. When associated with SLC7A5/LAT1, is also involved in the transport of L-DOPA across the blood-brain barrier, and that of thyroid hormones triiodothyronine (T3) and thyroxine (T4) across the cell membrane in tissues such as placenta. Involved in the uptake of methylmercury (MeHg) when administered as the L-cysteine or D,L-homocysteine complexes, and hence plays a role in metal ion homeostasis and toxicity. When associated with SLC7A5 or SLC7A8, involved in the cellular activity of small molecular weight nitrosothiols, via the stereoselective transport of L-nitrosocysteine (L-CNSO) across the transmembrane. Together with ICAM1, regulates the transport activity LAT2 in polarized intestinal cells, by generating and delivering intracellular signals. When associated with SLC7A5, plays an important role in transporting L-leucine from the circulating blood to the retina across the inner blood-retinal barrier. When associated with LAPTM4B, recruits SLC3A2 and SLC7A5 to lysosomes to promote leucine uptake into these organelles and is required for mTORC1 activation (By similarity). {ECO:0000250|UniProtKB:P08195, ECO:0000269|PubMed:10391915, ECO:0000269|PubMed:11011012, ECO:0000269|PubMed:9915839}. PTM: Phosphorylation on Ser-300 or Ser-302 and on Ser-420 by ecto-protein kinases favors heterotypic cell-cell interactions. {ECO:0000250}. SUBCELLULAR LOCATION: Apical cell membrane; Single-pass type II membrane protein. Melanosome {ECO:0000250}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV (By similarity). Localized to the plasma membrane when associated with SLC7A5 or SLC7A8 (By similarity). Localized to the placental apical membrane (By similarity). Located selectively at cell-cell adhesion sites. Colocalized with SLC7A8/LAT2 at the basolateral membrane of kidney proximal tubules and small intestine epithelia. Expressed in both luminal and abluminal membranes of brain capillary endothelial cells (By similarity). {ECO:0000250}. SUBUNIT: Disulfide-linked heterodimer of a glycosylated heavy chain and a non-glycosylated light chain (SLC7A5, SLC7A6, SLCA7A7, SLC7A8, SLC7A10 or SLCA7A11). Colocalizes with cadherins (By similarity). Interacts with FAM57A/CT120 and ICAM1 (By similarity). Constitutively and specifically associates with beta-1 integrins (alpha-2/beta-1, alpha-3/beta-1, alpha-5/beta-1 and alpha-6/beta-1), but minimally with alpha-4/beta-1 (By similarity). Interacts with LAPTM4B; recruits SLC3A2 and SLC7A5 to lysosomes to promote leucine uptake into these organelles and is required for mTORC1 activation (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P08195}. TISSUE SPECIFICITY: Observed in all adult tissues tested with strongest expression in kidney, small intestine, spleen, thymus and liver. Moderate expression in brain, stomach, heart, testis, lung, skin, pancreas and skeletal muscle. Expressed on the surface of epithelial cells of most embryonic tissues including epidermis, choroid plexus in the brain, retina, as well as intestinal, renal, and thymic epithelium. In brain expressed on capillary endothelia in cerebral cortex. {ECO:0000269|PubMed:10574970, ECO:0000269|PubMed:2928113, ECO:0000269|PubMed:9915839}. +Q61247 A2AP_MOUSE Alpha-2-antiplasmin (Alpha-2-AP) (Alpha-2-plasmin inhibitor) (Alpha-2-PI) (Serpin F2) 491 54,972 Beta strand (13); Chain (1); Disulfide bond (1); Glycosylation (4); Helix (11); Modified residue (1); Propeptide (1); Signal peptide (1); Site (3); Turn (4) FUNCTION: Serine protease inhibitor. The major targets of this inhibitor are plasmin and trypsin, but it also inactivates matriptase-3/TMPRSS7 and chymotrypsin (By similarity). {ECO:0000250}. PTM: Proteolytically cleaved at Pro-35 by both the prolyl endopeptidase FAP form and antiplasmin-cleaving enzyme FAP soluble form to generate mature alpha-2-antiplasmin. {ECO:0000250|UniProtKB:P08697}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Forms protease inhibiting heterodimer with TMPRSS7. {ECO:0000250}. TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma. +Q9D2R0 AACS_MOUSE Acetoacetyl-CoA synthetase (EC 6.2.1.16) 672 75,200 Chain (1); Sequence conflict (5) FUNCTION: Activates acetoacetate to acetoacetyl-CoA. May be involved in utilizing ketone body for the fatty acid-synthesis during adipose tissue development (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. +Q6GQT1 A2MG_MOUSE Alpha-2-macroglobulin-P (Alpha-2-macroglobulin) 1474 164,353 Chain (1); Cross-link (1); Disulfide bond (13); Glycosylation (9); Region (1); Sequence conflict (4); Signal peptide (1) FUNCTION: Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase (By similarity). {ECO:0000250|UniProtKB:P01023}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Homotetramer; disulfide-linked. {ECO:0000250|UniProtKB:P01023}. TISSUE SPECIFICITY: Expressed in uterus, mesometrial lymphoid aggregate and mammary tissue during pregnancy. Expressed in ovary, testis and kidney. Low level expression in heart. Not expressed in liver. {ECO:0000269|PubMed:15355875}. +P35363 5HT2A_MOUSE 5-hydroxytryptamine receptor 2A (5-HT-2) (5-HT-2A) (Serotonin receptor 2A) 471 52,842 Chain (1); Disulfide bond (2); Glycosylation (5); Modified residue (1); Motif (3); Region (2); Site (1); Topological domain (8); Transmembrane (7) TRANSMEM 76 99 Helical; Name=1. {ECO:0000250}.; TRANSMEM 111 132 Helical; Name=2. {ECO:0000250}.; TRANSMEM 149 171 Helical; Name=3. {ECO:0000250}.; TRANSMEM 192 215 Helical; Name=4. {ECO:0000250}.; TRANSMEM 234 254 Helical; Name=5. {ECO:0000250}.; TRANSMEM 325 346 Helical; Name=6. {ECO:0000250}.; TRANSMEM 363 384 Helical; Name=7. {ECO:0000250}. TOPO_DOM 1 75 Extracellular. {ECO:0000250}.; TOPO_DOM 100 110 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 133 148 Extracellular. {ECO:0000250}.; TOPO_DOM 172 191 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 216 233 Extracellular. {ECO:0000250}.; TOPO_DOM 255 324 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 347 362 Extracellular. {ECO:0000250}.; TOPO_DOM 385 471 Cytoplasmic. {ECO:0000250}. FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various drugs and psychoactive substances, including mescaline, psilocybin, 1-(2,5-dimethoxy-4-iodophenyl)-2-aminopropane (DOI) and lysergic acid diethylamide (LSD). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Beta-arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways. Signaling activates phospholipase C and a phosphatidylinositol-calcium second messenger system that modulates the activity of phosphatidylinositol 3-kinase and promotes the release of Ca(2+) ions from intracellular stores. Affects neural activity, perception, cognition and mood. Plays a role in the regulation of behavior, including responses to anxiogenic situations and psychoactive substances. Plays a role in intestinal smooth muscle contraction, and may play a role in arterial vasoconstriction. {ECO:0000269|PubMed:11960784, ECO:0000269|PubMed:16873667, ECO:0000269|PubMed:17270739, ECO:0000269|PubMed:18297054, ECO:0000269|PubMed:21645528, ECO:0000269|PubMed:23129762, ECO:0000269|PubMed:23346101}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21645528}; Multi-pass membrane protein {ECO:0000305}. Cell projection, dendrite {ECO:0000269|PubMed:11960784}. Cell projection, axon {ECO:0000250|UniProtKB:P14842}. Cytoplasmic vesicle {ECO:0000269|PubMed:11960784}. Membrane, caveola {ECO:0000250|UniProtKB:P14842}. Note=Localizes to the postsynaptic thickening of axo-dendritic synapses. SUBUNIT: Interacts with MPDZ and PATJ. May interact with MPP3, PRDX6, DLG4, DLG1, CASK, APBA1 and MAGI2 (By similarity). Interacts with GRM2 and DRD2; this may affect signaling. {ECO:0000250|UniProtKB:P28223, ECO:0000269|PubMed:18297054, ECO:0000269|PubMed:21645528}. DOMAIN: The PDZ domain-binding motif is involved in the interaction with PATJ, CASK, APBA1, DLG1 and DLG4. {ECO:0000250|UniProtKB:P28223}. TISSUE SPECIFICITY: Detected in neurons in brain cortex. Detected in adult intestine, especially in mucosal epithelium, longitudinal and circular layers of muscularis externa and myenteric plexuses. Highly expressed in Paneth cells, and detected at lower levels in enterocytes (at protein level). Detected in neurons in the brain cortex. {ECO:0000269|PubMed:11960784, ECO:0000269|PubMed:18297054, ECO:0000269|PubMed:23129762}. +Q3THG9 AASD1_MOUSE Alanyl-tRNA editing protein Aarsd1 (Alanyl-tRNA deacylase alaX) (AlaX) (AlaXp-II) (Alanyl-tRNA synthetase domain-containing protein 1) 412 44,971 Chain (1); Metal binding (4); Modified residue (1); Sequence conflict (3) FUNCTION: Functions in trans to edit the amino acid moiety from incorrectly charged Ser-tRNA(Ala). {ECO:0000269|PubMed:18172502}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +Q8R420 ABCA3_MOUSE ATP-binding cassette sub-family A member 3 1704 191,971 Chain (1); Domain (2); Nucleotide binding (2); Sequence conflict (9); Transmembrane (14) TRANSMEM 22 42 Helical. {ECO:0000255}.; TRANSMEM 261 283 Helical. {ECO:0000255}.; TRANSMEM 307 327 Helical. {ECO:0000255}.; TRANSMEM 344 364 Helical. {ECO:0000255}.; TRANSMEM 373 393 Helical. {ECO:0000255}.; TRANSMEM 405 425 Helical. {ECO:0000255}.; TRANSMEM 447 467 Helical. {ECO:0000255}.; TRANSMEM 925 945 Helical. {ECO:0000255}.; TRANSMEM 1100 1120 Helical. {ECO:0000255}.; TRANSMEM 1144 1164 Helical. {ECO:0000255}.; TRANSMEM 1183 1203 Helical. {ECO:0000255}.; TRANSMEM 1213 1233 Helical. {ECO:0000255}.; TRANSMEM 1245 1265 Helical. {ECO:0000255}.; TRANSMEM 1310 1330 Helical. {ECO:0000255}. FUNCTION: Plays an important role in the formation of pulmonary surfactant, probably by transporting lipids such as cholesterol. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. DOMAIN: Multifunctional polypeptide with two homologous halves, each containing a hydrophobic membrane-anchoring domain and an ATP binding cassette (ABC) domain. {ECO:0000250}. +Q99LE6 ABCF2_MOUSE ATP-binding cassette sub-family F member 2 628 71,782 Chain (1); Domain (2); Modified residue (3); Nucleotide binding (2); Sequence conflict (2) +Q99PU5 ACBG1_MOUSE Long-chain-fatty-acid--CoA ligase ACSBG1 (EC 6.2.1.3) (Acyl-CoA synthetase bubblegum family member 1) (mBG1) (Gonadotropin-regulated long chain acyl CoA synthetase) (GR-LACS) (Lipidosin) 721 80,426 Binding site (3); Chain (1); Erroneous initiation (1); Modified residue (5); Mutagenesis (2); Nucleotide binding (2); Sequence conflict (1) FUNCTION: Mediates activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Able to activate long-chain fatty acids. Can activate diverse saturated, monosaturated and polyunsaturated fatty acids (By similarity). {ECO:0000250, ECO:0000269|PubMed:11112418, ECO:0000269|PubMed:12975357, ECO:0000269|PubMed:14516277}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasmic vesicle. Microsome. Endoplasmic reticulum. TISSUE SPECIFICITY: Mainly expressed in brain. Also expressed in adrenal gland and testis. In brain, it is present in cerebral cortical and cerebellar neurons and in steroidogenic cells of the adrenal gland, testis and ovary (at protein level). {ECO:0000269|PubMed:11112418, ECO:0000269|PubMed:12975357, ECO:0000269|PubMed:14516277, ECO:0000269|PubMed:16469493}. +Q4JIM5 ABL2_MOUSE Tyrosine-protein kinase ABL2 (EC 2.7.10.2) (Abelson murine leukemia viral oncogene homolog 2) (Abelson tyrosine-protein kinase 2) (Abelson-related gene protein) (Tyrosine-protein kinase ARG) 1182 128,196 Active site (1); Beta strand (8); Binding site (1); Chain (1); Compositional bias (3); Domain (3); Helix (15); Initiator methionine (1); Lipidation (1); Modified residue (32); Motif (2); Mutagenesis (5); Nucleotide binding (2); Region (3); Turn (1) FUNCTION: Non-receptor tyrosine-protein kinase that plays an ABL1-overlapping role in key processes linked to cell growth and survival such as cytoskeleton remodeling in response to extracellular stimuli, cell motility and adhesion, receptor endocytosis, autophagy, DNA damage response and apoptosis. Coordinates actin remodeling through tyrosine phosphorylation of proteins controlling cytoskeleton dynamics like MYH10 (involved in movement); CTTN (involved in signaling); or TUBA1 and TUBB (microtubule subunits). Binds directly F-actin and regulates actin cytoskeletal structure through its F-actin-bundling activity. Involved in the regulation of cell adhesion and motility through phosphorylation of key regulators of these processes such as CRK, CRKL or DOK1. Required for adhesion-dependent phosphorylation of ARHGAP35 which promotes its association with RASA1, resulting in recruitment of ARHGAP35 to the cell periphery where it inhibits RHO. Phosphorylates multiple receptor tyrosine kinases like PDGFRB and other substrates which are involved in endocytosis regulation such as RIN1. In brain, may regulate neurotransmission by phosphorylating proteins at the synapse. Finally, functions as its own regulator through autocatalytic activity as well as through phosphorylation of its inhibitor, ABI1. {ECO:0000269|PubMed:11279004, ECO:0000269|PubMed:11752434, ECO:0000269|PubMed:12748290, ECO:0000269|PubMed:14993293, ECO:0000269|PubMed:16971514, ECO:0000269|PubMed:17892306, ECO:0000269|PubMed:9883720}. PTM: Phosphorylated at Tyr-261 by ABL1 in response to oxidative stress (By similarity). Phosphorylated by PDGFRB. {ECO:0000250, ECO:0000269|PubMed:12748290, ECO:0000269|PubMed:14993293}.; PTM: Polyubiquitinated. Polyubiquitination of ABL2 leads to degradation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11752434}. SUBUNIT: Interacts with PSMA7. Interacts with CTTN (By similarity). Found in a complex with ABL1, ABL2, CRK and UNC119; leading to the inhibition of CRK phosphorylation by ABL kinases (By similarity). {ECO:0000250}. DOMAIN: Contains two distinct classes of F-actin-binding domains. Although both can each bind F-actin, the 2 are required to bundle actin filaments. {ECO:0000269|PubMed:11752434, ECO:0000269|PubMed:20841568}. TISSUE SPECIFICITY: Most abundant in adult mouse brain, especially in synapse-rich regions. {ECO:0000269|PubMed:9883720}. +Q8CBW3 ABI1_MOUSE Abl interactor 1 (Abelson interactor 1) (Abi-1) (Ablphilin-1) (Eps8 SH3 domain-binding protein) (Eps8-binding protein) (Spectrin SH3 domain-binding protein 1) (e3B1) 481 52,288 Alternative sequence (4); Chain (1); Compositional bias (1); Domain (2); Initiator methionine (1); Modified residue (16); Region (1); Sequence conflict (1) FUNCTION: May act in negative regulation of cell growth and transformation by interacting with nonreceptor tyrosine kinases ABL1 and/or ABL2. In vitro, at least isoform 2 and isoform 4 suppress the transforming activity of Abelson murine leukemia virus (v-Abl) after overexpression in fibroblasts. May play a role in regulation EGF-induced Erk pathway activation. Involved in cytoskeletal reorganization and EGFR signaling. Together with EPS8 participates in transduction of signals from Ras to Rac. In vitro, a trimeric complex of ABI1, EPS8 and SOS1 exhibits Rac specific guanine nucleotide exchange factor (GEF) activity and ABI1 seems to act as an adapter in the complex. Regulates ABL1/c-Abl-mediated phosphorylation of ENAH. Recruits WASF1 to lamellipodia and there seems to regulate WASF1 protein level. In brain, seems to regulate the dendritic outgrowth and branching as well as to determine the shape and number of synaptic contacts of developing neurons. {ECO:0000269|PubMed:10499589, ECO:0000269|PubMed:11526477, ECO:0000269|PubMed:12672821, ECO:0000269|PubMed:15143189, ECO:0000269|PubMed:15558031, ECO:0000269|PubMed:7590237}. PTM: Phosphorylated on tyrosine residues after serum stimulation or induction by v-Abl. Seems to be phosphorylated at Tyr-53 by ABL1, required for nuclear but not for synaptic localization (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Cell projection, filopodium {ECO:0000250}. Cell projection, growth cone {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Localized to protruding lamellipodia and filopodia tips. Also localized to neuronal growth cones and synaptosomes. May shuttle from the postsynaptic densities to the nucleus (By similarity). {ECO:0000250}. SUBUNIT: Interacts with ENAH, Abelson murine leukemia virus V-ABL, ABL1, STX1A, SNAP25, VAMP2, and through its N-terminus with WASF1. Part of a complex consisting of ABI1, STX1A and SNAP25. Part of a complex consisting of ABI1, EPS8 and SOS1. Interacts with EPS8, SOS1, SOS2, GRB2, SPTA1, and the first SH3 domain of NCK1 (By similarity). Component of the WAVE2 complex composed of ABI1, CYFIP1/SRA1, NCKAP1/NAP1 (NCKAP1l/HEM1 in hematopoietic cells) and WASF2/WAVE2. Interacts (via SH3 domain) with SHANK2 and SHANK3, but not SHANK1; the interaction is direct. Interacts with the heterodimer MYC:MAX; the interaction may enhance MYC:MAX transcriptional activity. Interacts with FNBP1L (via the SH3 domain), WASF2, and CDC42, but only in the presence of FNBP1L (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q8IZP0, ECO:0000269|PubMed:10499589, ECO:0000269|PubMed:12672821, ECO:0000269|PubMed:15143189, ECO:0000269|PubMed:15558031, ECO:0000269|PubMed:7590237}. DOMAIN: The t-SNARE coiled-coil homology domain is necessary and sufficient for interaction with STX1A. TISSUE SPECIFICITY: Widely expressed with highest levels in bone marrow, spleen, brain, testes, and embryonic brain. In adult brain prominently expressed in the neocortex, hippocampus and dentate gyrus. {ECO:0000269|PubMed:10995551, ECO:0000269|PubMed:7590237}. +Q8R2Y0 ABHD6_MOUSE Monoacylglycerol lipase ABHD6 (EC 3.1.1.23) (2-arachidonoylglycerol hydrolase) (Abhydrolase domain-containing protein 6) 336 38,205 Active site (3); Alternative sequence (1); Chain (1); Erroneous initiation (2); Mutagenesis (1); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 9 29 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 8 Extracellular. {ECO:0000255}.; TOPO_DOM 30 336 Cytoplasmic. {ECO:0000255}. FUNCTION: Lipase that preferentially hydrolysis medium-chain saturated monoacylglycerols including 2-arachidonoylglycerol. Through 2-arachidonoylglycerol degradation may regulate endocannabinoid signaling pathways (PubMed:18096503, PubMed:20657592). May also have a lysophosphatidyl lipase activity with a preference for lysophosphatidylglycerol among other lysophospholipids (PubMed:24095738). {ECO:0000250|UniProtKB:Q9BV23, ECO:0000269|PubMed:18096503, ECO:0000269|PubMed:20657592, ECO:0000269|PubMed:24095738}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:18096503}; Single-pass type II membrane protein {ECO:0000255}. Mitochondrion {ECO:0000269|PubMed:20657592}. TISSUE SPECIFICITY: Widely expressed with higher expression in small intestine, liver and brown adipose tissue (PubMed:24095738). In brain, expressed postsynaptically in cortical neurons but not detected in microglia (at protein level) (PubMed:20657592). {ECO:0000269|PubMed:20657592, ECO:0000269|PubMed:24095738}. +Q9JJ59 ABCB9_MOUSE ATP-binding cassette sub-family B member 9 (ATP-binding cassette transporter 9) (ABC transporter 9 protein) (mABCB9) (TAP-like protein) (TAPL) 762 83,963 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (2); Erroneous initiation (1); Nucleotide binding (1); Sequence conflict (5); Transmembrane (8) TRANSMEM 7 27 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 47 67 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 84 104 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 116 136 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 181 201 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 221 241 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 315 335 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 412 432 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}. FUNCTION: ATP-dependent low-affinity peptide transporter which translocates a broad spectrum of peptides from the cytosol to the lysosomal lumen. Displays a broad peptide length specificity from 6-mer up to at least 59-mer peptides with an optimum of 23-mers. Favors positively charged, aromatic or hydrophobic residues in the N- and C-terminal positions whereas negatively charged residues as well as asparagine and methionine are not favored (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. Note=May be located in membrane rafts. {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. DOMAIN: The N-terminal region comprising the first four transmembrane domains is required for lysosomal localization but not for homodimerization or peptide transport. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in testis, particularly in the Sertoli cells of the seminiferous tubules, and at moderate levels in brain and spinal cord. {ECO:0000269|PubMed:10748049}. +Q8R0I0 ACE2_MOUSE Angiotensin-converting enzyme 2 (EC 3.4.17.23) (ACE-related carboxypeptidase) [Cleaved into: Processed angiotensin-converting enzyme 2] 805 92,368 Active site (2); Alternative sequence (1); Binding site (8); Chain (2); Disulfide bond (3); Frameshift (1); Glycosylation (5); Metal binding (3); Region (2); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 741 761 Helical. {ECO:0000255}. TOPO_DOM 18 740 Extracellular. {ECO:0000255}.; TOPO_DOM 762 805 Cytoplasmic. {ECO:0000255}. FUNCTION: Carboxypeptidase which converts angiotensin I to angiotensin 1-9, a peptide of unknown function, and angiotensin II to angiotensin 1-7, a vasodilator. Also able to hydrolyze apelin-13 and dynorphin-13 with high efficiency. May be an important regulator of heart function. May have a protective role in acute lung injury. Plays an important role in amino acid transport by acting as binding partner of amino acid transporter SLC6A19, regulating its trafficking on the cell surface and its activity (PubMed:19185582). {ECO:0000269|PubMed:12075344, ECO:0000269|PubMed:12967627, ECO:0000269|PubMed:16001071, ECO:0000269|PubMed:19185582}. PTM: Proteolytic cleavage by ADAM17 generates a secreted form. Also cleaved by serine proteases: TMPRSS2, TMPRSS11D and HPN/TMPRSS1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Processed angiotensin-converting enzyme 2: Secreted {ECO:0000250}.; SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23535237}; Single-pass type I membrane protein {ECO:0000269|PubMed:23535237}. Cytoplasm {ECO:0000269|PubMed:23535237}. Note=Detected in both cell membrane and cytoplasm in neurons. SUBUNIT: Interacts with ITGB1 and the catalytically active form of TMPRSS2 (By similarity). Interacts with SLC6A19 (PubMed:19185582). {ECO:0000250, ECO:0000269|PubMed:19185582}.; SUBUNIT: (Microbial infection) Weakly interacts with SARS-CoV S protein. {ECO:0000269|PubMed:15452268}. TISSUE SPECIFICITY: Expressed in heart, kidney and forebrain (at protein level). Ubiquitously expressed, with highest levels in ileum, kidney and lung. In lung, expressed on vascular endothelial and airway epithelial cells. {ECO:0000269|PubMed:12487024, ECO:0000269|PubMed:15949646, ECO:0000269|PubMed:16001071}. +Q8R4X1 ACER1_MOUSE Alkaline ceramidase 1 (AlkCDase 1) (Alkaline CDase 1) (maCER1) (EC 3.5.1.23) (Acylsphingosine deacylase 3) (N-acylsphingosine amidohydrolase 3) 273 32,082 Chain (1); Topological domain (7); Transmembrane (7) TRANSMEM 37 57 Helical. {ECO:0000255}.; TRANSMEM 73 93 Helical. {ECO:0000255}.; TRANSMEM 94 114 Helical. {ECO:0000255}.; TRANSMEM 127 147 Helical. {ECO:0000255}.; TRANSMEM 150 167 Helical. {ECO:0000255}.; TRANSMEM 178 198 Helical. {ECO:0000255}.; TRANSMEM 216 236 Helical. {ECO:0000255}. TOPO_DOM 1 36 Lumenal. {ECO:0000255}.; TOPO_DOM 58 72 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 115 126 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 148 149 Lumenal. {ECO:0000255}.; TOPO_DOM 168 177 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 199 215 Lumenal. {ECO:0000255}.; TOPO_DOM 237 273 Cytoplasmic. {ECO:0000255}. FUNCTION: Hydrolyzes the sphingolipid ceramide into sphingosine and free fatty acid at an optimal pH of 8.0. Has a highly restricted substrate specificity for the natural stereoisomer of ceramide with D-erythro-sphingosine but not D-ribo-phytosphingosine or D-erythro-dihydrosphingosine as a backbone. May have a role in regulating the levels of bioactive lipids ceramide and sphingosine 1-phosphate, as well as complex sphingolipids. {ECO:0000269|PubMed:12783875}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12783875}; Multi-pass membrane protein {ECO:0000269|PubMed:12783875}. TISSUE SPECIFICITY: Highly expressed in skin. Weakly or not expressed in other tissues. {ECO:0000269|PubMed:12783875}. +Q9D099 ACER3_MOUSE Alkaline ceramidase 3 (AlkCDase 3) (Alkaline CDase 3) (EC 3.5.1.-) (EC 3.5.1.23) (Alkaline phytoceramidase) (aPHC) 267 31,565 Chain (1); Sequence conflict (2); Transmembrane (7) TRANSMEM 30 52 Helical. {ECO:0000255}.; TRANSMEM 65 84 Helical. {ECO:0000255}.; TRANSMEM 94 111 Helical. {ECO:0000255}.; TRANSMEM 118 137 Helical. {ECO:0000255}.; TRANSMEM 147 169 Helical. {ECO:0000255}.; TRANSMEM 174 196 Helical. {ECO:0000255}.; TRANSMEM 216 238 Helical. {ECO:0000255}. Sphingolipid metabolism. FUNCTION: Catalyzes the hydrolysis of unsaturated long-chain C18:1-, C20:1- and C20:4-ceramides, dihydroceramides and phytoceramides (PubMed:26474409). Controls the generation of sphingosine in erythrocytes, and thereby sphingosine-1-phosphate in plasma (By similarity). Through the regulation of ceramides and sphingosine-1-phosphate homeostasis in the brain may play a role in neurons survival and function (PubMed:26474409). By regulating the levels of proinflammatory ceramides in immune cells and tissues, may modulate the inflammatory response (PubMed:26938296). {ECO:0000250|UniProtKB:Q9NUN7, ECO:0000269|PubMed:26474409, ECO:0000269|PubMed:26938296}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9NUN7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9NUN7}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9NUN7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9NUN7}. TISSUE SPECIFICITY: Up-regulated with age in cerebeLlum and cerebrum. {ECO:0000269|PubMed:26474409}. +Q8BGG9 ACNT2_MOUSE Acyl-coenzyme A amino acid N-acyltransferase 2 (EC 2.3.1.-) 420 46,595 Active site (3); Alternative sequence (1); Chain (1); Erroneous initiation (2); Motif (1); Sequence conflict (1) FUNCTION: Acyltransferase which efficiently conjugates very long-chain and long-chain fatty acids to taurine. Shows no conjugation activity in the presence of glycine (By similarity). {ECO:0000250|UniProtKB:A2AKK5}. SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:A2AKK5}. +Q91V92 ACLY_MOUSE ATP-citrate synthase (EC 2.3.3.8) (ATP-citrate (pro-S-)-lyase) (Citrate cleavage enzyme) 1091 119,728 Active site (1); Binding site (5); Chain (1); Cross-link (3); Domain (1); Metal binding (3); Modified residue (18); Nucleotide binding (4); Region (1) FUNCTION: ATP-citrate synthase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. Has a central role in de novo lipid synthesis. In nervous tissue it may be involved in the biosynthesis of acetylcholine (By similarity). {ECO:0000250}. PTM: ISGylated. {ECO:0000269|PubMed:16139798}.; PTM: Acetylated at Lys-530, Lys-536 and Lys-544 by KAT2B/PCAF. Acetylation is promoted by glucose and stabilizes the protein, probably by preventing ubiquitination at the same sites. Acetylation promotes de novo lipid synthesis. Deacetylated by SIRT2 (By similarity). {ECO:0000250}.; PTM: Ubiquitinated at Lys-530, Lys-536 and Lys-544 by UBR4, leading to its degradation. Ubiquitination is probably inhibited by acetylation at same site (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homotetramer. {ECO:0000250}. +F8VQ03 ADAM3_MOUSE A disintegrin and metallopeptidase domain 3 (Cyritestin) 822 91,444 Chain (1); Disulfide bond (7); Domain (3); Signal peptide (1); Transmembrane (1) TRANSMEM 689 709 Helical. {ECO:0000255}. FUNCTION: Involved in fertilization by controlling sperm migration into oviduct. {ECO:0000269|PubMed:19339711}. PTM: Initially synthesized as a 110-kDa precursor in round spermatids, and the precursor is then processed into a 42-kDa mature protein during the sperm transport into and/or once in the epididymis. {ECO:0000269|PubMed:15514464, ECO:0000269|PubMed:24501175}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15514464}; Single-pass membrane protein {ECO:0000255}. Note=Localized in round and elongating spermatids. Localized on the anterior part of the sperm head, and is removed during the acrosome reaction. {ECO:0000269|PubMed:15514464}. SUBUNIT: Interacts with LY6K (PubMed:24501175). Interacts with TEX101 (PubMed:23633567). {ECO:0000269|PubMed:23633567, ECO:0000269|PubMed:24501175}. +Q8R400 ADIG_MOUSE Adipogenin (Small adipocyte factor 1) (SMAF-1) 80 9,362 Chain (1); Modified residue (1); Transmembrane (1) TRANSMEM 16 36 Helical. {ECO:0000255}. FUNCTION: Plays a role in stimulating adipocyte differentiation and development. {ECO:0000269|PubMed:16132694}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. Nucleus {ECO:0000269|PubMed:15567149, ECO:0000269|PubMed:16132694}. TISSUE SPECIFICITY: Selectively expressed in adipose tissue where it is particularly enriched in brown adipose tissue. In adipose tissue, expressed exclusively in adipocytes and not in the stromal-vascular cell population. Expressed at much lower levels in heart, stomach and muscle and barely detected in kidney and lung. {ECO:0000269|PubMed:15567149, ECO:0000269|PubMed:16132694}. +Q99K67 AASS_MOUSE Alpha-aminoadipic semialdehyde synthase, mitochondrial (LKR/SDH) [Includes: Lysine ketoglutarate reductase (LKR) (LOR) (EC 1.5.1.8); Saccharopine dehydrogenase (SDH) (EC 1.5.1.9)] 926 102,975 Binding site (3); Chain (1); Modified residue (27); Nucleotide binding (2); Region (4); Sequence conflict (2); Transit peptide (1) Amino-acid degradation; L-lysine degradation via saccharopine pathway; glutaryl-CoA from L-lysine: step 1/6. Amino-acid degradation; L-lysine degradation via saccharopine pathway; glutaryl-CoA from L-lysine: step 2/6. FUNCTION: Bifunctional enzyme that catalyzes the first two steps in lysine degradation. The N-terminal and the C-terminal contain lysine-oxoglutarate reductase and saccharopine dehydrogenase activity, respectively. SUBCELLULAR LOCATION: Mitochondrion. SUBUNIT: Homodimer. TISSUE SPECIFICITY: Both enzymes are highly expressed in kidney and liver, very low expression is seen in heart, brain, spleen, lung, skeletal muscle and testis. SDH was detected only in cortical regions of the kidney. +Q8R0P8 ABHD8_MOUSE Protein ABHD8 (EC 3.-.-.-) (Alpha/beta hydrolase domain-containing protein 8) (Abhydrolase domain-containing protein 8) 439 48,229 Active site (3); Chain (1); Domain (1); Sequence conflict (2) +Q9D061 ACBD6_MOUSE Acyl-CoA-binding domain-containing protein 6 282 30,887 Alternative sequence (4); Binding site (2); Chain (1); Domain (1); Modified residue (2); Region (1); Repeat (2); Sequence conflict (2) FUNCTION: Binds long-chain acyl-coenzyme A molecules with a strong preference for unsaturated C18:1-CoA, lower affinity for unsaturated C20:4-CoA, and very weak affinity for saturated C16:0-CoA. Does not bind fatty acids (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. +P09470 ACE_MOUSE Angiotensin-converting enzyme (ACE) (EC 3.2.1.-) (EC 3.4.15.1) (Dipeptidyl carboxypeptidase I) (Kininase II) (CD antigen CD143) [Cleaved into: Angiotensin-converting enzyme, soluble form] 1312 150,918 Active site (2); Alternative sequence (2); Binding site (7); Chain (2); Disulfide bond (4); Glycosylation (13); Metal binding (6); Modified residue (1); Mutagenesis (3); Propeptide (1); Region (2); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1265 1281 Helical. {ECO:0000255}. TOPO_DOM 35 1264 Extracellular. {ECO:0000255}.; TOPO_DOM 1282 1312 Cytoplasmic. {ECO:0000255}. FUNCTION: Converts angiotensin I to angiotensin II by release of the terminal His-Leu, this results in an increase of the vasoconstrictor activity of angiotensin. Also able to inactivate bradykinin, a potent vasodilator. Has also a glycosidase activity which releases GPI-anchored proteins from the membrane by cleaving the mannose linkage in the GPI moiety. This GPIase activity seems to be crucial for the egg-binding ability of the sperm. {ECO:0000269|PubMed:15665832, ECO:0000269|PubMed:7753170, ECO:0000269|PubMed:8642790}. PTM: Phosphorylated by CK2 on Ser-1305; which allows membrane retention. {ECO:0000250}. SUBCELLULAR LOCATION: Angiotensin-converting enzyme, soluble form: Secreted {ECO:0000250}.; SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23535237}; Single-pass type I membrane protein {ECO:0000269|PubMed:23535237}. Cytoplasm {ECO:0000269|PubMed:23535237}. Note=Detected in both cell membrane and cytoplasm in neurons. TISSUE SPECIFICITY: Testis-specific isoform is expressed in spermatocytes, adult testis. +Q8BMN3 ACHB3_MOUSE Neuronal acetylcholine receptor subunit beta-3 464 53,112 Alternative sequence (1); Chain (1); Disulfide bond (1); Glycosylation (2); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (4) TRANSMEM 239 263 Helical. {ECO:0000255}.; TRANSMEM 271 288 Helical. {ECO:0000255}.; TRANSMEM 305 326 Helical. {ECO:0000255}.; TRANSMEM 435 453 Helical. {ECO:0000255}. TOPO_DOM 31 238 Extracellular. {ECO:0000255}.; TOPO_DOM 327 434 Cytoplasmic. {ECO:0000255}. FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. SUBUNIT: Neuronal AChR seems to be composed of two different types of subunits: alpha and beta. {ECO:0000250}. +P28271 ACOC_MOUSE Cytoplasmic aconitate hydratase (Aconitase) (EC 4.2.1.3) (Citrate hydro-lyase) (Iron regulatory protein 1) (IRP1) (Iron-responsive element-binding protein 1) (IRE-BP 1) 889 98,126 Binding site (4); Chain (1); Metal binding (3); Region (2); Sequence conflict (4) FUNCTION: Iron sensor. Binds a 4Fe-4S cluster and functions as aconitase when cellular iron levels are high. Functions as mRNA binding protein that regulates uptake, sequestration and utilization of iron when cellular iron levels are low. Binds to iron-responsive elements (IRES) in target mRNA species when iron levels are low. Binding of a 4Fe-4S cluster precludes RNA binding. {ECO:0000250|UniProtKB:P21399}.; FUNCTION: Catalyzes the isomerization of citrate to isocitrate via cis-aconitate. {ECO:0000250, ECO:0000250|UniProtKB:P21399}. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Interacts (when associated with the 4Fe-4S) with FBXL5. Interacts with frataxin(81-210). {ECO:0000250|UniProtKB:P21399}. +P32211 ACM4_MOUSE Muscarinic acetylcholine receptor M4 (Mm4 mAChR) 479 52,973 Chain (1); Disulfide bond (1); Glycosylation (2); Modified residue (3); Sequence conflict (2); Topological domain (8); Transmembrane (7) TRANSMEM 31 53 Helical; Name=1. {ECO:0000250}.; TRANSMEM 68 88 Helical; Name=2. {ECO:0000250}.; TRANSMEM 106 127 Helical; Name=3. {ECO:0000250}.; TRANSMEM 148 170 Helical; Name=4. {ECO:0000250}.; TRANSMEM 193 215 Helical; Name=5. {ECO:0000250}.; TRANSMEM 402 422 Helical; Name=6. {ECO:0000250}.; TRANSMEM 437 456 Helical; Name=7. {ECO:0000250}. TOPO_DOM 1 30 Extracellular. {ECO:0000250}.; TOPO_DOM 54 67 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 89 105 Extracellular. {ECO:0000250}.; TOPO_DOM 128 147 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 171 192 Extracellular. {ECO:0000250}.; TOPO_DOM 216 401 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 423 436 Extracellular. {ECO:0000250}.; TOPO_DOM 457 479 Cytoplasmic. {ECO:0000250}. FUNCTION: The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is inhibition of adenylate cyclase. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein. +Q9R0H0 ACOX1_MOUSE Peroxisomal acyl-coenzyme A oxidase 1 (AOX) (EC 1.3.3.6) (Palmitoyl-CoA oxidase) 661 74,649 Active site (1); Alternative sequence (1); Binding site (2); Chain (1); Erroneous initiation (1); Modified residue (25); Motif (1); Sequence conflict (5) Lipid metabolism; peroxisomal fatty acid beta-oxidation. FUNCTION: Catalyzes the desaturation of acyl-CoAs to 2-trans-enoyl-CoAs. Isoform 1 shows highest activity against medium-chain fatty acyl-CoAs and activity decreases with increasing chain length. Isoform 2 is active against a much broader range of substrates and shows activity towards very long-chain acyl-CoAs (By similarity). {ECO:0000250|UniProtKB:P07872}. SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:P07872}. SUBUNIT: Homodimer (By similarity). Interacts with LONP2 (By similarity). {ECO:0000250|UniProtKB:P07872, ECO:0000250|UniProtKB:Q15067}. TISSUE SPECIFICITY: Highest levels of isoform 1 are found in liver and kidney while highest levels of isoform 2 are found in white adipose tissue. Isoform 1 is expressed at higher levels than isoform 2 in liver and kidney while isoform 2 is expressed at higher levels in brain, heart, lung, muscle, white adipose tissue and testis. {ECO:0000269|PubMed:20195242}. +Q9CQR4 ACO13_MOUSE Acyl-coenzyme A thioesterase 13 (Acyl-CoA thioesterase 13) (EC 3.1.2.-) (Thioesterase superfamily member 2) 140 15,183 Beta strand (7); Binding site (1); Chain (1); Helix (3); Modified residue (6); Turn (3) FUNCTION: Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Has acyl-CoA thioesterase activity towards medium (C12) and long-chain (C18) fatty acyl-CoA substrates. Can also hydrolyze 3-hydroxyphenylacetyl-CoA (in vitro). May play a role in controlling adaptive thermogenesis. {ECO:0000269|PubMed:19405909, ECO:0000269|PubMed:24072708}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:17045243, ECO:0000269|PubMed:17704541, ECO:0000269|PubMed:19405909}. Mitochondrion {ECO:0000269|PubMed:19405909}. Nucleus {ECO:0000269|PubMed:17045243, ECO:0000269|PubMed:17704541}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:17045243}. Note=During interphase, found both in the nucleus and in the cytoplasm. At mitosis, localizes to the spindle. Colocalizes with tubulin. {ECO:0000269|PubMed:17045243}. SUBUNIT: Homotetramer. Interacts with PCTP. {ECO:0000269|PubMed:17704541, ECO:0000269|PubMed:19405909}. TISSUE SPECIFICITY: Highly expressed in the kidney and moderately in the heart, liver, brain, small and large intestine. Also expressed in brown adipose tissue. {ECO:0000269|PubMed:17045243, ECO:0000269|PubMed:17704541, ECO:0000269|PubMed:19405909, ECO:0000269|PubMed:22345407}. +P63260 ACTG_MOUSE Actin, cytoplasmic 2 (Gamma-actin) [Cleaved into: Actin, cytoplasmic 2, N-terminally processed] 375 41,793 Chain (2); Initiator methionine (1); Modified residue (6) FUNCTION: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. {ECO:0000250|UniProtKB:P63261}. PTM: Oxidation of Met-44 and Met-47 by MICALs (MICAL1, MICAL2 or MICAL3) to form methionine sulfoxide promotes actin filament depolymerization. MICAL1 and MICAL2 produce the (R)-S-oxide form (PubMed:23911929). The (R)-S-oxide form is reverted by MSRB1 and MSRB2, which promote actin repolymerization (PubMed:23911929). {ECO:0000269|PubMed:23911929}.; PTM: Monomethylation at Lys-84 (K84me1) regulates actin-myosin interaction and actomyosin-dependent processes. Demethylation by ALKBH4 is required for maintaining actomyosin dynamics supporting normal cleavage furrow ingression during cytokinesis and cell migration. {ECO:0000250|UniProtKB:P63261}.; PTM: Actin, cytoplasmic 2, N-terminally processed: N-terminal acetylation by NAA80 affects actin filament depolymerization and elongation, including elongation driven by formins. In contrast, filament nucleation by the Arp2/3 complex is not affected. {ECO:0000250|UniProtKB:P63261}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P63261}. SUBUNIT: Polymerization of globular actin (G-actin) leads to a structural filament (F-actin) in the form of a two-stranded helix. Each actin can bind to 4 others. Interacts with TWF1, CAPZB, cofilin and profilin. {ECO:0000250|UniProtKB:P63261}. +Q9CZW4 ACSL3_MOUSE Long-chain-fatty-acid--CoA ligase 3 (EC 6.2.1.3) (Long-chain acyl-CoA synthetase 3) (LACS 3) 720 80,492 Chain (1); Modified residue (1); Sequence conflict (1); Topological domain (1); Transmembrane (1) TRANSMEM 21 41 Helical; Signal-anchor for type III membrane protein. {ECO:0000255}. TOPO_DOM 42 720 Cytoplasmic. {ECO:0000255}. FUNCTION: Acyl-CoA synthetases (ACSL) activates long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. ACSL3 has mainly an anabolic role in energy metabolism (By similarity). Required for the incorporation of fatty acids into phosphatidylcholine, the major phospholipid located on the surface of VLDL (very low density lipoproteins) (By similarity). Mediates hepatic lipogenesis (By similarity). Preferentially uses myristate, laurate, arachidonate and eicosapentaenoate as substrates (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Peroxisome membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Microsome membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. +Q9QXG4 ACSA_MOUSE Acetyl-coenzyme A synthetase, cytoplasmic (EC 6.2.1.1) (Acetate--CoA ligase) (Acetyl-CoA synthetase) (ACS) (AceCS) (Acyl-CoA synthetase short-chain family member 2) (Acyl-activating enzyme) 701 78,862 Binding site (5); Chain (1); Modified residue (5); Nucleotide binding (2); Region (1); Sequence conflict (2) FUNCTION: Activates acetate so that it can be used for lipid synthesis or for energy generation. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +Q80W40 ACSM4_MOUSE Acyl-coenzyme A synthetase ACSM4, mitochondrial (EC 6.2.1.2) (Olfactory specific medium-chain acyl CoA synthetase) (O-MACS) 580 65,427 Binding site (3); Chain (1); Nucleotide binding (2); Transit peptide (1) FUNCTION: Has medium-chain fatty acid:CoA ligase activity with broad substrate specificity (in vitro). Acts on acids from C(4) to C(11) and on the corresponding 3-hydroxy- and 2,3- or 3,4-unsaturated acids (in vitro) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. +Q8C0I1 ADAS_MOUSE Alkyldihydroxyacetonephosphate synthase, peroxisomal (Alkyl-DHAP synthase) (EC 2.5.1.26) (Alkylglycerone-phosphate synthase) 645 71,684 Active site (1); Binding site (1); Chain (1); Domain (1); Modified residue (5); Nucleotide binding (4); Region (1); Site (1); Transit peptide (1) Glycerolipid metabolism; ether lipid biosynthesis. FUNCTION: Catalyzes the exchange of an acyl for a long-chain alkyl group and the formation of the ether bond in the biosynthesis of ether phospholipids. {ECO:0000250}. SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +Q80XL6 ACD11_MOUSE Acyl-CoA dehydrogenase family member 11 (ACAD-11) (EC 1.3.99.-) 779 87,366 Binding site (7); Chain (1); Modified residue (8); Nucleotide binding (6); Region (1); Sequence conflict (4) FUNCTION: Acyl-CoA dehydrogenase, that exhibits maximal activity towards saturated C22-CoA. {ECO:0000250}. SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:17768142}. Mitochondrion {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +Q9R0X4 ACOT9_MOUSE Acyl-coenzyme A thioesterase 9, mitochondrial (Acyl-CoA thioesterase 9) (EC 3.1.2.-) (Acyl coenzyme A thioester hydrolase 2) (MTE-2) (Acyl-CoA thioester hydrolase 9) (Mitochondrial 48 kDa acyl-CoA thioester hydrolase 1) (Mt-ACT48.1) (Protein U8) (p48) 439 50,560 Chain (1); Domain (2); Modified residue (1); Sequence conflict (1); Transit peptide (1) FUNCTION: Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Active on long chain acyl-CoAs. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305|PubMed:10383425}. SUBUNIT: Interacts with NYAP1, NYAP2 and MYO16. {ECO:0000269|PubMed:21946561}. +Q32MW3 ACO10_MOUSE Acyl-coenzyme A thioesterase 10, mitochondrial (Acyl-CoA thioesterase 10) (EC 3.1.2.-) (Mitochondrial 48 kDa acyl-CoA thioester hydrolase 2) (Mt-ACT48.2) 439 50,552 Chain (1); Domain (2); Sequence conflict (6); Transit peptide (1) FUNCTION: Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Active on long chain acyl-CoAs. {ECO:0000305}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:10383425, ECO:0000305}. +Q2MKA5 ACHA5_MOUSE Neuronal acetylcholine receptor subunit alpha-5 467 53,448 Alternative sequence (1); Chain (1); Disulfide bond (2); Glycosylation (3); Signal peptide (1); Topological domain (2); Transmembrane (4) TRANSMEM 255 275 Helical. {ECO:0000255}.; TRANSMEM 284 304 Helical. {ECO:0000255}.; TRANSMEM 317 337 Helical. {ECO:0000255}.; TRANSMEM 430 450 Helical. {ECO:0000255}. TOPO_DOM 338 429 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 451 467 Extracellular. {ECO:0000255}. FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Neuronal AChR seems to be composed of two different types of subunits: alpha and non-alpha (beta). Interacts with LYPD6. {ECO:0000250|UniProtKB:P30532}. +Q9QXD1 ACOX2_MOUSE Peroxisomal acyl-coenzyme A oxidase 2 (EC 1.17.99.3) (3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA 24-hydroxylase) (3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA oxidase) (Trihydroxycoprostanoyl-CoA oxidase) (THCA-CoA oxidase) (THCCox) 681 76,863 Chain (1); Modified residue (8); Motif (1); Sequence conflict (1) FUNCTION: Oxidizes the CoA esters of the bile acid intermediates di- and tri-hydroxycoprostanic acids. {ECO:0000250|UniProtKB:P97562}. PTM: Acetylation of Lys-667 is observed in liver mitochondria from fasted mice but not from fed mice. SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:Q99424}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P07872}. +Q9EPL9 ACOX3_MOUSE Peroxisomal acyl-coenzyme A oxidase 3 (EC 1.3.3.6) (Branched-chain acyl-CoA oxidase) (BRCACox) (Pristanoyl-CoA oxidase) 700 78,404 Chain (1); Modified residue (3); Motif (1); Sequence conflict (9) Lipid metabolism; peroxisomal fatty acid beta-oxidation. FUNCTION: Oxidizes the CoA-esters of 2-methyl-branched fatty acids. {ECO:0000250}. SUBCELLULAR LOCATION: Peroxisome {ECO:0000305}. +Q8VCW8 ACSF2_MOUSE Acyl-CoA synthetase family member 2, mitochondrial (EC 6.2.1.-) 615 67,951 Binding site (3); Chain (1); Modified residue (13); Nucleotide binding (1); Sequence conflict (3); Transit peptide (1) FUNCTION: Acyl-CoA synthases catalyze the initial reaction in fatty acid metabolism, by forming a thioester with CoA. Has some preference toward medium-chain substrates. Plays a role in adipocyte differentiation. {ECO:0000269|PubMed:17762044}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}. +Q61824 ADA12_MOUSE Disintegrin and metalloproteinase domain-containing protein 12 (ADAM 12) (EC 3.4.24.-) (Meltrin-alpha) 903 98,504 Active site (1); Chain (1); Compositional bias (1); Disulfide bond (7); Domain (3); Glycosylation (7); Metal binding (4); Modified residue (1); Motif (6); Propeptide (1); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 707 727 Helical. {ECO:0000255}. TOPO_DOM 206 706 Extracellular. {ECO:0000255}.; TOPO_DOM 728 903 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in skeletal muscle regeneration, specifically at the onset of cell fusion. Also involved in macrophage-derived giant cells (MGC) and osteoclast formation from mononuclear precursors. PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Interacts with alpha-actinin-2 and with syndecans. Interacts with SH3PXD2A. Interacts with FST3. Interacts with RACK1; the interaction is required for PKC-dependent translocation of ADAM12 to the cell membrane (By similarity). {ECO:0000250}. DOMAIN: The first 30 amino acids of the cytoplasmic domain contain a major binding site to alpha-actinin-2. This interaction is necessary to promote muscle cell fusion.; DOMAIN: The cysteine-rich domain supports cell adhesion through syndecans and triggers signaling events that lead to beta-1 integrin-dependent cell spreading. In carcinoma cells the binding of this domain to syndecans does not allow the integrin-mediated cell spreading (By similarity). {ECO:0000250}.; DOMAIN: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme. TISSUE SPECIFICITY: Expressed during early developing mesenchymal cells that give rise to skeletal muscle, bones and visceral organs. Not expressed in adult normal muscle but expressed in regenerating muscle. {ECO:0000269|PubMed:9622634}. +Q80V03 ADCK5_MOUSE Uncharacterized aarF domain-containing protein kinase 5 (EC 2.7.11.-) 582 66,654 Alternative sequence (1); Chain (1); Domain (1); Sequence caution (1); Sequence conflict (2); Transmembrane (1) TRANSMEM 50 69 Helical. {ECO:0000255}. FUNCTION: The function of this protein is not yet clear. It is not known if it has protein kinase activity and what type of substrate it would phosphorylate (Ser, Thr or Tyr). SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +P51569 AGAL_MOUSE Alpha-galactosidase A (EC 3.2.1.22) (Alpha-D-galactosidase A) (Alpha-D-galactoside galactohydrolase) (Melibiase) 419 47,643 Active site (2); Chain (1); Disulfide bond (5); Glycosylation (3); Modified residue (1); Region (1); Signal peptide (1) SUBCELLULAR LOCATION: Lysosome. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P06280}. +Q9DBL1 ACDSB_MOUSE Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial (SBCAD) (EC 1.3.8.5) (2-methyl branched chain acyl-CoA dehydrogenase) (2-MEBCAD) (2-methylbutyryl-coenzyme A dehydrogenase) (2-methylbutyryl-CoA dehydrogenase) 432 47,874 Active site (1); Binding site (5); Chain (1); Modified residue (7); Nucleotide binding (4); Region (2); Transit peptide (1) Lipid metabolism; mitochondrial fatty acid beta-oxidation. FUNCTION: Has greatest activity toward short branched chain acyl-CoA derivative such as (s)-2-methylbutyryl-CoA, isobutyryl-CoA, and 2-methylhexanoyl-CoA as well as toward short straight chain acyl-CoAs such as butyryl-CoA and hexanoyl-CoA. Can use valproyl-CoA as substrate and may play a role in controlling the metabolic flux of valproic acid in the development of toxicity of this agent (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000305}. SUBUNIT: Homotetramer. {ECO:0000250}. +Q8R4G9 ACHA3_MOUSE Neuronal acetylcholine receptor subunit alpha-3 499 57,110 Chain (1); Disulfide bond (2); Erroneous initiation (1); Glycosylation (2); Modified residue (2); Signal peptide (1); Topological domain (2); Transmembrane (4) TRANSMEM 235 259 Helical. {ECO:0000255}.; TRANSMEM 267 285 Helical. {ECO:0000255}.; TRANSMEM 301 322 Helical. {ECO:0000255}.; TRANSMEM 472 491 Helical. {ECO:0000255}. TOPO_DOM 26 234 Extracellular. {ECO:0000255}.; TOPO_DOM 323 471 Cytoplasmic. {ECO:0000255}. FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Neuronal AChR is composed of two different types of subunits: alpha and beta. Alpha-3 subunit can be combined to beta-2 or beta-4 to give rise to functional receptors. Interacts with RIC3; which is required for proper folding and assembly. Interacts with LYPD6. The heteropentamer alpha-3-beta-2 interacts with alpha-conotoxins ImI, ImII, PnIA, GID and MII. The heteropentamer alpha-3-beta-4 interacts with the alpha-conotoxin ImI. {ECO:0000250|UniProtKB:P04757, ECO:0000250|UniProtKB:P32297}. +Q9QUI6 ACKR1_MOUSE Atypical chemokine receptor 1 (Duffy antigen/chemokine receptor) (CD antigen CD234) 334 36,694 Chain (1); Disulfide bond (2); Glycosylation (4); Natural variant (11); Topological domain (8); Transmembrane (7) TRANSMEM 62 82 Helical; Name=1. {ECO:0000255}.; TRANSMEM 94 114 Helical; Name=2. {ECO:0000255}.; TRANSMEM 128 151 Helical; Name=3. {ECO:0000255}.; TRANSMEM 165 185 Helical; Name=4. {ECO:0000255}.; TRANSMEM 206 226 Helical; Name=5. {ECO:0000255}.; TRANSMEM 243 263 Helical; Name=6. {ECO:0000255}.; TRANSMEM 286 306 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 61 Extracellular. {ECO:0000255}.; TOPO_DOM 83 93 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 115 127 Extracellular. {ECO:0000255}.; TOPO_DOM 152 164 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 186 205 Extracellular. {ECO:0000255}.; TOPO_DOM 227 242 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 264 285 Extracellular. {ECO:0000255}.; TOPO_DOM 307 334 Cytoplasmic. {ECO:0000255}. FUNCTION: Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing receptor) or chemokine-scavenging receptor or chemokine decoy receptor. Has a promiscuous chemokine-binding profile, interacting with inflammatory chemokines of both the CXC and the CC subfamilies but not with homeostatic chemokines. Acts as a receptor for chemokines including CCL2, CCL5, CCL7, CCL11, CCL13, CCL14, CCL17, CXCL5, CXCL6, IL8/CXCL8, CXCL11, GRO, RANTES, MCP-1 and TARC. May regulate chemokine bioavailability and, consequently, leukocyte recruitment through two distinct mechanisms: when expressed in endothelial cells, it sustains the abluminal to luminal transcytosis of tissue-derived chemokines and their subsequent presentation to circulating leukocytes; when expressed in erythrocytes, serves as blood reservoir of cognate chemokines but also as a chemokine sink, buffering potential surges in plasma chemokine levels (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Early endosome {ECO:0000250}. Recycling endosome {ECO:0000250}. Membrane; Multi-pass membrane protein. Note=Predominantly localizes to endocytic vesicles, and upon stimulation by the ligand is internalized via caveolae. Once internalized, the ligand dissociates from the receptor, and is targeted to degradation while the receptor is recycled back to the cell membrane (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in liver and brain. +Q9JIX8 ACINU_MOUSE Apoptotic chromatin condensation inducer in the nucleus (Acinus) 1338 150,719 Alternative sequence (4); Chain (1); Compositional bias (4); Cross-link (9); Domain (1); Frameshift (1); Modified residue (39); Region (1); Sequence conflict (14); Site (1) FUNCTION: Auxiliary component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Component of the ASAP complexes which bind RNA in a sequence-independent manner and are proposed to be recruited to the EJC prior to or during the splicing process and to regulate specific excision of introns in specific transcription subsets; ACIN1 confers RNA-binding to the complex. The ASAP complex can inhibit RNA processing during in vitro splicing reactions. The ASAP complex promotes apoptosis and is disassembled after induction of apoptosis. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms such as Bcl-X(S); the activity is different from the established EJC assembly and function. Induces apoptotic chromatin condensation after activation by CASP3. Regulates cyclin A1, but not cyclin A2, expression in leukemia cells (By similarity). {ECO:0000250}. PTM: Undergoes proteolytic cleavage; the processed form is active, contrary to the uncleaved form. {ECO:0000250}.; PTM: Phosphorylation on Ser-1179 by SRPK2 up-regulates its stimulatory effect on cyclin A1. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus speckle {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Note=Phosphorylation on Ser-1179 by SRPK2 redistributes it from the nuclear speckles to the nucleoplasm. {ECO:0000250}. SUBUNIT: Found in a mRNA splicing-dependent exon junction complex (EJC). Component of the heterotrimeric ASAP (apoptosis- and splicing-associated protein) complexes consisting of RNPS1, SAP18 and different isoforms of ACIN1; the association of SAP18 seems to require a preformed RNPS1:ACIN1 complex. Interacts with API5. Interacts with SRPK2 in a phosphorylation-dependent manner (By similarity). {ECO:0000250}. +Q9DBS4 ACOXL_MOUSE Acyl-coenzyme A oxidase-like protein (Acyl-CoA oxidase-like protein) (EC 1.3.3.-) 632 70,706 Alternative sequence (1); Chain (1); Nucleotide binding (1) +Q9QYR9 ACOT2_MOUSE Acyl-coenzyme A thioesterase 2, mitochondrial (Acyl-CoA thioesterase 2) (EC 3.1.2.2) (Acyl coenzyme A thioester hydrolase) (MTE-I) (Very-long-chain acyl-CoA thioesterase) 453 49,657 Active site (3); Chain (1); Modified residue (2); Sequence conflict (2); Transit peptide (1) FUNCTION: Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Most active on substrates with chain lengths ranging from C14-C20. The enzyme is involved in enhancing the hepatic fatty acid oxidation in meitochondria. {ECO:0000269|PubMed:25114170}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:25114170}. SUBUNIT: Monomer. {ECO:0000269|PubMed:25114170}. TISSUE SPECIFICITY: Highly expressed in brown and white adipose tissue, muscle, heart, kidney, lung, adrenal gland and spleen; weakly expressed in intestine, testis and brain. {ECO:0000269|PubMed:10567408, ECO:0000269|PubMed:11330065}. +Q9QYR7 ACOT3_MOUSE Acyl-coenzyme A thioesterase 3 (Acyl-CoA thioesterase 3) (EC 3.1.2.2) (PTE-Ia) (Peroxisomal acyl-coenzyme A thioester hydrolase 2a) (Peroxisomal long-chain acyl-CoA thioesterase 2) 432 47,490 Active site (3); Alternative sequence (1); Chain (1); Motif (1) FUNCTION: Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Mainly active on long-chain acyl-CoAs. May have a function in termination of beta-oxidation of fatty acids. SUBCELLULAR LOCATION: Peroxisome. TISSUE SPECIFICITY: Widely expressed. Highly expressed in the kidney, expressed at low level in the liver. Isoform 2 is expressed in the kidney, but not in the liver. Isoform 1 is expressed in more liver-specific. {ECO:0000269|PubMed:10567408}. +P23578 ACRO_MOUSE Acrosin (EC 3.4.21.10) [Cleaved into: Acrosin light chain; Acrosin heavy chain] 436 48,929 Active site (3); Chain (3); Disulfide bond (6); Domain (1); Erroneous initiation (3); Glycosylation (2); Propeptide (1); Sequence conflict (39); Signal peptide (1) FUNCTION: Acrosin is the major protease of mammalian spermatozoa. It is a serine protease of trypsin-like cleavage specificity, it is synthesized in a zymogen form, proacrosin and stored in the acrosome. SUBUNIT: Heavy chain (catalytic) and a light chain linked by two disulfide bonds. Forms a heterodimer with SERPINA5 (By similarity). {ECO:0000250}. +Q9QY84 ACL7A_MOUSE Actin-like protein 7A (Actin-like-7-alpha) (Testis-specific actin-2) (T-actin-2) 440 49,451 Chain (1); Region (1); Sequence conflict (5) SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:21278383}. Golgi apparatus {ECO:0000269|PubMed:21278383}. Cytoplasm {ECO:0000269|PubMed:12672658}. Nucleus {ECO:0000269|PubMed:12672658, ECO:0000269|PubMed:21278383}. Note=Detected at the Golgi apparatus during acrosome biogenesis (PubMed:21278383). Detected at the subacrosomal layer in round spermatids (PubMed:21278383). Detected in sperm head and tail (PubMed:21278383). SUBUNIT: Interacts (via N-terminus) with TES (via LIM domain 2). Heterodimer with TES; the heterodimer interacts with ENAH to form a heterotrimer (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Detected in testis. Detected at the acrosome of round spermatids (at protein level). Detected in adult and embryonic testis. Detected in developing male germ cells. {ECO:0000269|PubMed:12672658, ECO:0000269|PubMed:12704725, ECO:0000269|PubMed:21278383}. +P56375 ACYP2_MOUSE Acylphosphatase-2 (EC 3.6.1.7) (Acylphosphatase, muscle type isozyme) (Acylphosphate phosphohydrolase 2) 106 11,878 Active site (2); Chain (1); Domain (1); Erroneous initiation (1); Modified residue (1); Sequence conflict (3) +A2A7Z8 ADCL3_MOUSE Arylacetamide deacetylase-like 3 (EC 3.1.1.-) 408 46,340 Active site (3); Chain (1); Glycosylation (1); Motif (1); Transmembrane (3) TRANSMEM 2 22 Helical. {ECO:0000255}.; TRANSMEM 46 66 Helical. {ECO:0000255}.; TRANSMEM 109 129 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +P97297 ADML_MOUSE ADM [Cleaved into: Adrenomedullin (AM); Proadrenomedullin N-20 terminal peptide (ProAM N-terminal 20 peptide) (PAMP) (ProAM-N20)] 184 20,750 Disulfide bond (1); Modified residue (2); Peptide (2); Propeptide (2); Sequence conflict (1); Signal peptide (1) FUNCTION: AM and PAMP are potent hypotensive and vasodilatator agents. SUBCELLULAR LOCATION: Secreted. +P97783 AF1Q_MOUSE Protein AF1q 90 10,029 Chain (1); Modified residue (1); Motif (1) FUNCTION: Cofactor for the transcription factor TCF7. Involved in regulation of lymphoid development by driving multipotent hematopoietic progenitor cells towards a T-cell fate. {ECO:0000250|UniProtKB:Q13015}. PTM: Ubiquitinated, leading to degradation. {ECO:0000250|UniProtKB:Q13015}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13015}. Cytoplasm {ECO:0000250|UniProtKB:Q13015}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q13015}. Note=Continuous nuclear export is followed by degradation. {ECO:0000250|UniProtKB:Q13015}. SUBUNIT: Interacts with HSPA8 and LAMP2 isoform A; the interaction may target MLLT11 for degradation via chaperone-mediated autophagy. Interacts with TCF7. {ECO:0000250|UniProtKB:Q13015}. TISSUE SPECIFICITY: Detected in embryonic brain cortex. {ECO:0000269|PubMed:15530661}. +Q9JI39 ABCBA_MOUSE ATP-binding cassette sub-family B member 10, mitochondrial (ABC-mitochondrial erythroid protein) (ABC-me protein) (ATP-binding cassette transporter 10) (ABC transporter 10 protein) 715 77,188 Chain (1); Domain (2); Modified residue (1); Nucleotide binding (1); Topological domain (6); Transit peptide (1); Transmembrane (5) TRANSMEM 138 158 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 181 201 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 267 287 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 361 381 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 396 416 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}. TOPO_DOM 83 137 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 159 180 Mitochondrial matrix. {ECO:0000255}.; TOPO_DOM 202 266 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 288 360 Mitochondrial matrix. {ECO:0000255}.; TOPO_DOM 382 395 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 417 715 Mitochondrial matrix. {ECO:0000255}. FUNCTION: May mediate critical mitochondrial transport functions related to heme biosynthesis. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SUBUNIT: Homodimer or homooligomer. {ECO:0000269|PubMed:15215243}. TISSUE SPECIFICITY: Expressed at particularly high levels in fetal liver, and erythroid tissues of embryos and adults. Found also in adult bone marrow, liver and kidney, and at lower levels in heart, brain and spleen. +P13516 ACOD1_MOUSE Acyl-CoA desaturase 1 (EC 1.14.19.1) (Delta(9)-desaturase 1) (Delta-9 desaturase 1) (Fatty acid desaturase 1) (Stearoyl-CoA desaturase 1) 355 41,046 Beta strand (5); Binding site (7); Chain (1); Helix (22); Metal binding (9); Motif (3); Natural variant (1); Sequence conflict (2); Topological domain (5); Transmembrane (4); Turn (4) TRANSMEM 69 89 Helical. {ECO:0000269|PubMed:26098370}.; TRANSMEM 94 114 Helical. {ECO:0000269|PubMed:26098370}.; TRANSMEM 214 233 Helical. {ECO:0000269|PubMed:26098370}.; TRANSMEM 238 259 Helical. {ECO:0000269|PubMed:26098370}. TOPO_DOM 1 68 Cytoplasmic. {ECO:0000305|PubMed:16275639}.; TOPO_DOM 90 93 Lumenal. {ECO:0000305|PubMed:26098370}.; TOPO_DOM 115 213 Cytoplasmic. {ECO:0000305|PubMed:26098370}.; TOPO_DOM 234 237 Lumenal. {ECO:0000305|PubMed:26098370}.; TOPO_DOM 260 355 Cytoplasmic. {ECO:0000305|PubMed:16275639}. FUNCTION: Stearyl-CoA desaturase that utilizes O(2) and electrons from reduced cytochrome b5 to introduce the first double bond into saturated fatty acyl-CoA substrates. Catalyzes the insertion of a cis double bond at the Delta-9 position into fatty acyl-CoA substrates including palmitoyl-CoA and stearoyl-CoA (PubMed:11500518, PubMed:11533264, PubMed:16275639, PubMed:16443825, PubMed:26098370). Gives rise to a mixture of 16:1 and 18:1 unsaturated fatty acids (PubMed:11500518, PubMed:11533264, PubMed:16443825, PubMed:26098370). Plays an important role in lipid biosynthesis (PubMed:17127673, PubMed:10899171, PubMed:11500518, PubMed:11441127, PubMed:11533264, PubMed:12177411, PubMed:26098370). Plays an important role in regulating the expression of genes that are involved in lipogenesis and in regulating mitochondrial fatty acid oxidation (PubMed:12177411, PubMed:17127673, PubMed:24356954, PubMed:24295027). Plays an important role in body energy homeostasis (PubMed:17127673, PubMed:15210843, PubMed:24295027, PubMed:24356954). Contributes to the biosynthesis of membrane phospholipids, cholesterol esters and triglycerides (PubMed:10899171, PubMed:11500518, PubMed:11441127, PubMed:11533264, PubMed:12177411, PubMed:15210843, PubMed:26098370). Required for normal development of sebaceous glands (PubMed:17738154, PubMed:11533264). Required for the biosynthesis of normal levels of Delta-9 unsaturated fatty acids and 1-alkyl-2,3-diacylglycerol in the Harderian gland (PubMed:11500518). Required for normal production of meibum, an oily material that prevents drying of the cornea (PubMed:11533264). {ECO:0000269|PubMed:10899171, ECO:0000269|PubMed:11441127, ECO:0000269|PubMed:11500518, ECO:0000269|PubMed:11533264, ECO:0000269|PubMed:12177411, ECO:0000269|PubMed:15210843, ECO:0000269|PubMed:16275639, ECO:0000269|PubMed:16443825, ECO:0000269|PubMed:17127673, ECO:0000269|PubMed:26098370, ECO:0000305|PubMed:24295027, ECO:0000305|PubMed:24356954}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16275639, ECO:0000305|PubMed:16443825}; Multi-pass membrane protein {ECO:0000269|PubMed:16275639}. Microsome membrane {ECO:0000269|PubMed:10899171, ECO:0000269|PubMed:11500518, ECO:0000269|PubMed:11533264, ECO:0000269|PubMed:16443825}. DOMAIN: The histidine box domains are involved in binding the catalytic metal ions. {ECO:0000269|PubMed:26098370}. TISSUE SPECIFICITY: Detected in liver (at protein level) (PubMed:10899171, PubMed:11533264). Detected in skin and liver (PubMed:10545940, PubMed:11161812, PubMed:11441127, PubMed:11533264). Detected in sebaceous gland, but not in hair follicle (PubMed:10545940). Detected in white and brown adipose tissue, eyelid, Harderian gland, and at lower levels in Meibomian gland, eyeball and adrenal gland (PubMed:11500518, PubMed:11533264). Highly expressed in liver, and detected at low levels in brain, heart, lung, stomach, skeletal muscle and kidney (PubMed:11161812, PubMed:12815040). {ECO:0000269|PubMed:10545940, ECO:0000269|PubMed:10899171, ECO:0000269|PubMed:11441127, ECO:0000269|PubMed:11500518, ECO:0000269|PubMed:11533264, ECO:0000269|PubMed:12815040}. DISEASE: Note=Defects is Scd1 are the cause of asebia (ab) (PubMed:17738154, PubMed:10545940, PubMed:10854228, PubMed:10899171, PubMed:15278437). The trait is due to spontaneous autosomal recessive mutations that give rise to deletions or point mutations in Scd1. The ab trait has complete penetrance (PubMed:17738154). Ab mice are characterized by reduced body weight, extreme sebaceous gland hypoplasia leading to nearly complete absence of sebaceous glands, and thickened, scaly skin with hyperkeratosis and alopecia (PubMed:17738154, PubMed:10854228, PubMed:15278437). The hair follicles are abnormally long and extend at a sharp angle into the subcutis, probably due to abnormal persistence of inner root sheath. Frequently the hair shaft ruptures through the base of the hair follicle, giving rise to inflammation that results in scarring alopecia (PubMed:10854228, PubMed:15278437). Besides, ab mice display increased transepithelial water loss (PubMed:10854228). Ab mice present a narrow eye fissure and their eyes are nearly closed (PubMed:10854228, PubMed:15278437). Older mice develop blindness (PubMed:17738154). Scd1 activity is almost absent in liver, and is not compensated by expression of another family member (PubMed:10899171). Liver levels of total cholesterol esters are decreased by 87%, while plasma cholesterol levels are increased by 35% (PubMed:10899171). Likewise, skin sterol esters and diol diesters are strongly reduced (PubMed:10854228). Liver triglyceride levels are decreased by 62%, while plasma triglyceride levels are decreased by 67% (PubMed:10899171). The fatty acid composition of liver triglycerides is altered, with a decrease of about 85% in palmitoleate (C16:1) and oleate (C18:1) levels (PubMed:10899171). These defects cannot be compensated by a diet enriched in unsaturated fatty acids (PubMed:10899171, PubMed:11441127). {ECO:0000269|PubMed:10545940, ECO:0000269|PubMed:10854228, ECO:0000269|PubMed:10899171, ECO:0000269|PubMed:11441127, ECO:0000269|PubMed:11533264, ECO:0000269|PubMed:15278437, ECO:0000269|PubMed:17738154}. +O70174 ACHA4_MOUSE Neuronal acetylcholine receptor subunit alpha-4 629 70,305 Chain (1); Disulfide bond (2); Glycosylation (3); Lipidation (1); Modified residue (3); Natural variant (1); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (4) TRANSMEM 250 270 Helical. {ECO:0000255}.; TRANSMEM 279 299 Helical. {ECO:0000255}.; TRANSMEM 312 332 Helical. {ECO:0000255}.; TRANSMEM 604 624 Helical. {ECO:0000255}. TOPO_DOM 32 249 Extracellular. {ECO:0000255}.; TOPO_DOM 333 603 Cytoplasmic. {ECO:0000255}. FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane permeable to sodium ions. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. SUBUNIT: Neuronal AChR is composed of two different types of subunits: alpha and beta. Alpha-4 subunit can be combined to beta-2 or beta-4 to give rise to functional receptors, complexes with beta-2 may be heteropentamers. Interacts with RIC3; which is required for proper folding and assembly. Interacts with LYPD6. The heteropentamer alpha-4-beta-2 interacts with alpha-conotoxins PnIA, GID and MII (By similarity). {ECO:0000250|UniProtKB:P09483, ECO:0000250|UniProtKB:P43681}. +Q9DBK0 ACO12_MOUSE Acyl-coenzyme A thioesterase 12 (Acyl-CoA thioesterase 12) (EC 3.1.2.1) (Acyl-CoA thioester hydrolase 12) (Cytoplasmic acetyl-CoA hydrolase 1) (CACH-1) (mCACH-1) 556 61,762 Binding site (1); Chain (1); Domain (3); Modified residue (4); Region (3) Carbohydrate metabolism; pyruvate metabolism. FUNCTION: Hydrolyzes acetyl-CoA to acetate and CoA. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homodimer or homotetramer. {ECO:0000250}. +Q924I3 ACKR4_MOUSE Atypical chemokine receptor 4 (C-C chemokine receptor type 11) (C-C CKR-11) (CC-CKR-11) (CCR-11) (CC chemokine receptor-like 1) (CCRL1) (CCX CKR) 350 39,531 Chain (1); Glycosylation (2); Sequence conflict (3); Topological domain (8); Transmembrane (7) TRANSMEM 42 62 Helical; Name=1. {ECO:0000255}.; TRANSMEM 78 99 Helical; Name=2. {ECO:0000255}.; TRANSMEM 115 135 Helical; Name=3. {ECO:0000255}.; TRANSMEM 155 175 Helical; Name=4. {ECO:0000255}.; TRANSMEM 200 220 Helical; Name=5. {ECO:0000255}.; TRANSMEM 241 261 Helical; Name=6. {ECO:0000255}.; TRANSMEM 290 310 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 41 Extracellular. {ECO:0000255}.; TOPO_DOM 63 77 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 100 114 Extracellular. {ECO:0000255}.; TOPO_DOM 136 154 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 176 199 Extracellular. {ECO:0000255}.; TOPO_DOM 221 240 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 262 289 Extracellular. {ECO:0000255}.; TOPO_DOM 311 350 Cytoplasmic. {ECO:0000255}. FUNCTION: Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing receptor) or chemokine-scavenging receptor or chemokine decoy receptor. Acts as a receptor for chemokines CCL2, CCL8, CCL13, CCL19, CCL21 and CCL25. Chemokine-binding does not activate G-protein-mediated signal transduction but instead induces beta-arrestin recruitment, leading to ligand internalization. Plays an important role in controlling the migration of immune and cancer cells that express chemokine receptors CCR7 and CCR9, by reducing the availability of CCL19, CCL21, and CCL25 through internalization. Negatively regulates CXCR3-induced chemotaxis. Regulates T-cell development in the thymus and inhibits spontaneous autoimmunity. {ECO:0000269|PubMed:11981810, ECO:0000269|PubMed:23152546}. PTM: The Ser/Thr residues in the C-terminal cytoplasmic tail may be phosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Early endosome {ECO:0000250}. Recycling endosome {ECO:0000250}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Predominantly localizes to endocytic vesicles, and upon stimulation by the ligand is internalized via caveolae. Once internalized, the ligand dissociates from the receptor, and is targeted to degradation while the receptor is recycled back to the cell membrane (By similarity). {ECO:0000250}. SUBUNIT: Forms heteromers with CXCR3. Interacts with ARRB1 and ARRB2 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in lung, heart, spleen, skeletal muscle, testis, astrocytes and microglia. Expressed by cortical thymic epithelial cells. {ECO:0000269|PubMed:11063828, ECO:0000269|PubMed:11981810, ECO:0000269|PubMed:23152546}. +Q9Z2N8 ACL6A_MOUSE Actin-like protein 6A (53 kDa BRG1-associated factor A) (Actin-related protein Baf53a) (BRG1-associated factor 53A) (BAF53A) 429 47,448 Chain (1); Cross-link (1); Initiator methionine (1); Modified residue (3); Sequence conflict (3) FUNCTION: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. Required for maximal ATPase activity of SMARCA4/BRG1/BAF190A and for association of the SMARCA4/BRG1/BAF190A containing remodeling complex BAF with chromatin/nuclear matrix. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and is required for the proliferation of neural progenitors. During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (PubMed:17640523). Component of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Putative core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair (By similarity). {ECO:0000250|UniProtKB:O96019, ECO:0000269|PubMed:17640523, ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O96019}. SUBUNIT: Component of numerous complexes with chromatin remodeling and histone acetyltransferase activity. Component of the NuA4 histone acetyltransferase complex which contains the catalytic subunit KAT5/TIP60 and the subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6. The NuA4 complex interacts with MYC and the adenovirus E1A protein. Component of a NuA4-related complex which contains EP400, TRRAP/PAF400, SRCAP, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, actin, ACTL6A/BAF53A, VPS72 and YEATS4/GAS41. Component of the multiprotein chromatin-remodeling complexes SWI/SNF: SWI/SNF-A (BAF), SWI/SNF-B (PBAF) and related complexes. The canonical complex contains a catalytic subunit (either SMARCA4/BRG1/BAF190A or SMARCA2/BRM/BAF190B) and at least SMARCE1, ACTL6A/BAF53, SMARCC1/BAF155, SMARCC2/BAF170, and SMARCB1/SNF5/BAF47. Other subunits specific to each of the complexes may also be present permitting several possible combinations developmentally and tissue specific. Component of the BAF complex, which includes at least actin (ACTB), ARID1A/BAF250A, ARID1B/BAF250B, SMARCA2/BRM, SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57, SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C. In muscle cells, the BAF complex also contains DPF3 (Probable). Component of the BAF53 complex, at least composed of ACTL6A/BAF53A, RUVBL1/TIP49, SMARCA2/BRM/BAF190B and TRRAP/PAF400, and which may also include a HAT activity related to, but distinct from, that of KAT5. Component of neural progenitors-specific chromatin remodeling complex (npBAF complex) composed of at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, PHF10/BAF45A, ACTL6A/BAF53A and actin. Component of SWI/SNF (GBAF) subcomplex, which includes at least BICRA or BICRAL (mutually exclusive), BRD9, SS18, SMARCA2/BRM, SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, SMARCC1/BAF155, and SMARCD1/BAF60A (PubMed:29374058). May be a component of the SWI/SNF-B (PBAF) chromatin remodeling complex, at least composed of SMARCA4/BRG1, SMARCB1/BAF47/SNF5, ACTL6A/BAF53A or ACTL6B/BAF53B, SMARCE1/BAF57, SMARCD1/BAF60A, SMARCD2/BAF60B, perhaps SMARCD3/BAF60C, SMARCC1/BAF155, SMARCC2/BAF170, PBRM1/BAF180, ARID2/BAF200 and actin (By similarity). Interacts with SMARCA4/BRG1/BAF190A (By similarity). Interacts with PHF10/BAF45A (PubMed:17640523). Component of the chromatin remodeling INO80 complex; specifically part of a complex module associated with the DBINO domain of INO80 (By similarity). Interacts with DPF2 (By similarity). {ECO:0000250|UniProtKB:O96019, ECO:0000269|PubMed:17640523, ECO:0000269|PubMed:29374058, ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}. TISSUE SPECIFICITY: Widely expressed. Expressed selectively in neural stem and progenitor cells (at protein level). {ECO:0000269|PubMed:17640523}. +P63268 ACTH_MOUSE Actin, gamma-enteric smooth muscle (Alpha-actin-3) (Gamma-2-actin) (Smooth muscle gamma-actin) [Cleaved into: Actin, gamma-enteric smooth muscle, intermediate form] 376 41,877 Chain (2); Initiator methionine (1); Modified residue (3) FUNCTION: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. PTM: Oxidation of Met-45 and Met-48 by MICALs (MICAL1, MICAL2 or MICAL3) to form methionine sulfoxide promotes actin filament depolymerization. MICAL1 and MICAL2 produce the (R)-S-oxide form. The (R)-S-oxide form is reverted by MSRB1 and MSRB2, which promotes actin repolymerization. {ECO:0000269|PubMed:23911929}.; PTM: Monomethylation at Lys-85 (K85me1) regulates actin-myosin interaction and actomyosin-dependent processes. Demethylation by ALKBH4 is required for maintaining actomyosin dynamics supporting normal cleavage furrow ingression during cytokinesis and cell migration. {ECO:0000250|UniProtKB:P68134}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SUBUNIT: Polymerization of globular actin (G-actin) leads to a structural filament (F-actin) in the form of a two-stranded helix. Each actin can bind to 4 others. TISSUE SPECIFICITY: Expressed in tissues containing smooth muscle particularly the intestines and bladder. {ECO:0000269|PubMed:24337657}. +Q3TTE0 ADAM5_MOUSE Disintegrin and metalloproteinase domain-containing protein 5 (Transmembrane metalloproteinase-like, disintegrin-like, and cysteine-rich protein II) (tMDC II) 751 84,534 Alternative sequence (5); Chain (1); Compositional bias (1); Disulfide bond (7); Domain (3); Propeptide (1); Sequence conflict (8); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 692 712 Helical. {ECO:0000255}. TOPO_DOM 17 691 Extracellular. {ECO:0000255}.; TOPO_DOM 713 751 Cytoplasmic. {ECO:0000255}. FUNCTION: This is a non catalytic metalloprotease-like protein. May play a role in sperm-egg fusion (By similarity). {ECO:0000250}. PTM: Subject to proteolytic processing during epididymal transit of spermatozoa. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Interacts with TEX101. {ECO:0000269|PubMed:23969891}. TISSUE SPECIFICITY: Detected in brain, kidney, liver, lung, spleen and ovary. Highly expressed in testis. {ECO:0000269|PubMed:7750654}. +Q80TL1 ADCY2_MOUSE Adenylate cyclase type 2 (EC 4.6.1.1) (ATP pyrophosphate-lyase 2) (Adenylate cyclase type II) (Adenylyl cyclase 2) 1090 123,270 Binding site (3); Chain (1); Erroneous initiation (1); Glycosylation (3); Metal binding (5); Modified residue (2); Nucleotide binding (4); Region (2); Topological domain (3); Transmembrane (12) TRANSMEM 45 65 Helical. {ECO:0000255}.; TRANSMEM 75 95 Helical. {ECO:0000255}.; TRANSMEM 107 127 Helical. {ECO:0000255}.; TRANSMEM 132 152 Helical. {ECO:0000255}.; TRANSMEM 157 177 Helical. {ECO:0000255}.; TRANSMEM 186 206 Helical. {ECO:0000255}.; TRANSMEM 601 621 Helical. {ECO:0000255}.; TRANSMEM 626 646 Helical. {ECO:0000255}.; TRANSMEM 679 699 Helical. {ECO:0000255}.; TRANSMEM 734 754 Helical. {ECO:0000255}.; TRANSMEM 763 783 Helical. {ECO:0000255}.; TRANSMEM 800 820 Helical. {ECO:0000255}. TOPO_DOM 1 44 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 207 600 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 821 1090 Cytoplasmic. {ECO:0000255}. FUNCTION: Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling. Down-stream signaling cascades mediate changes in gene expression patterns and lead to increased IL6 production. Functions in signaling cascades downstream of the muscarinic acetylcholine receptors. {ECO:0000250|UniProtKB:P26769}. PTM: Phosphorylated by RAF1. {ECO:0000250|UniProtKB:Q08462}. SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P26769}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P26769}. Cell membrane {ECO:0000250|UniProtKB:P26769}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P26769}. Cytoplasm {ECO:0000250|UniProtKB:Q08462}. SUBUNIT: Interacts with RAF1 (By similarity). Interacts with GNAS. Interacts with the G protein beta and gamma subunit complex (By similarity). {ECO:0000250|UniProtKB:P26769, ECO:0000250|UniProtKB:Q08462}. DOMAIN: The protein contains two modules with six transmembrane helices each; both are required for catalytic activity. Isolated N-terminal or C-terminal guanylate cyclase domains have no catalytic activity, but when they are brought together, enzyme activity is restored. The active site is at the interface of the two domains. Both contribute substrate-binding residues, but the catalytic metal ions are bound exclusively via the N-terminal guanylate cyclase domain. {ECO:0000250|UniProtKB:P26769}. +P03958 ADA_MOUSE Adenosine deaminase (EC 3.5.4.4) (Adenosine aminohydrolase) 352 39,992 Active site (1); Beta strand (11); Binding site (4); Chain (1); Helix (22); Initiator methionine (1); Metal binding (4); Modified residue (3); Mutagenesis (10); Sequence conflict (1); Site (3); Turn (1) FUNCTION: Catalyzes the hydrolytic deamination of adenosine and 2-deoxyadenosine (PubMed:9272950). Plays an important role in purine metabolism and in adenosine homeostasis (PubMed:9272950, PubMed:10720488). Modulates signaling by extracellular adenosine, and so contributes indirectly to cellular signaling events (PubMed:11435465). Acts as a positive regulator of T-cell coactivation, by binding DPP4. Its interaction with DPP4 regulates lymphocyte-epithelial cell adhesion (By similarity). Enhances dendritic cell immunogenicity by affecting dendritic cell costimulatory molecule expression and cytokines and chemokines secretion (By similarity). Enhances CD4+ T-cell differentiation and proliferation (By similarity). Acts as a positive modulator of adenosine receptors ADORA1 and ADORA2A, by enhancing their ligand affinity via conformational change (By similarity). Stimulates plasminogen activation (By similarity). Plays a role in male fertility (By similarity). Plays a protective role in early postimplantation embryonic development (PubMed:9272950). {ECO:0000250|UniProtKB:P00813, ECO:0000250|UniProtKB:P56658, ECO:0000269|PubMed:10720488, ECO:0000269|PubMed:11435465, ECO:0000269|PubMed:9272950}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Extracellular side {ECO:0000250}. Cell junction {ECO:0000250|UniProtKB:P00813}. Cytoplasmic vesicle lumen {ECO:0000269|PubMed:8783262}. Cytoplasm {ECO:0000250}. Lysosome {ECO:0000250|UniProtKB:P00813}. Note=Colocalized with DPP4 at the cell surface. {ECO:0000250|UniProtKB:P00813}. SUBUNIT: Interacts with DPP4 (via extracellular domain). Interacts with PLG (via Kringle 4 domain); the interaction stimulates PLG activation when in complex with DPP4. {ECO:0000250|UniProtKB:P00813}. TISSUE SPECIFICITY: Detected in brain neurons in the median emninence (at protein level) (PubMed:8783262). Expressed in secondary deciduum (at protein level) (PubMed:9272950). Found in all tissues, occurs in large amounts in T-lymphocytes and, at the time of weaning, in gastrointestinal tissues. {ECO:0000269|PubMed:8783262, ECO:0000269|PubMed:9272950}. +Q61072 ADAM9_MOUSE Disintegrin and metalloproteinase domain-containing protein 9 (ADAM 9) (EC 3.4.24.-) (Meltrin-gamma) (Metalloprotease/disintegrin/cysteine-rich protein 9) (Myeloma cell metalloproteinase) 845 92,079 Active site (1); Chain (1); Compositional bias (1); Disulfide bond (7); Domain (3); Erroneous initiation (1); Glycosylation (6); Metal binding (3); Mutagenesis (5); Sequence conflict (3); Signal peptide (1); Site (2); Topological domain (2); Transmembrane (1) TRANSMEM 698 718 Helical. {ECO:0000255}. TOPO_DOM 30 697 Extracellular. {ECO:0000255}.; TOPO_DOM 719 845 Cytoplasmic. {ECO:0000255}. FUNCTION: Cleaves and releases a number of molecules with important roles in tumorigenesis and angiogenesis, such as TEK, KDR, EPHB4, CD40, VCAM1 and CDH5 (PubMed:19273593). May mediate cell-cell, cell-matrix interactions and regulate the motility of cells via interactions with integrins (PubMed:10825303). {ECO:0000269|PubMed:10825303, ECO:0000269|PubMed:19273593}. PTM: Proteolytically cleaved in the trans-Golgi network before it reaches the plasma membrane to generate a mature protein. The removal of the pro-domain occurs via cleavage at two different sites. Processed most likely by a pro-protein convertase such as furin, at the boundary between the pro-domain and the catalytic domain. An additional upstream cleavage pro-protein convertase site (Arg-56/Glu-57) has an important role in the activation of ADAM9. {ECO:0000269|PubMed:25795784, ECO:0000269|PubMed:9920899}.; PTM: Phosphorylation is induced in vitro by phorbol-12-myristate-13-acetate (PMA) (PubMed:9920899). {ECO:0000269|PubMed:9920899}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25795784, ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Interacts with SH3GL2 and SNX9 through its cytoplasmic tail (PubMed:10531379). Interacts with ITGA6 (PubMed:10825303). {ECO:0000269|PubMed:10531379, ECO:0000269|PubMed:10825303}. +Q9D0L4 ADCK1_MOUSE Uncharacterized aarF domain-containing protein kinase 1 (EC 2.7.11.-) 525 59,736 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Domain (1); Nucleotide binding (1); Signal peptide (1) FUNCTION: The function of this protein is not yet clear. It is not known if it has protein kinase activity and what type of substrate it would phosphorylate (Ser, Thr or Tyr). SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q01341 ADCY6_MOUSE Adenylate cyclase type 6 (EC 4.6.1.1) (ATP pyrophosphate-lyase 6) (Adenylate cyclase type VI) (Adenylyl cyclase 6) (AC6) (Ca(2+)-inhibitable adenylyl cyclase) 1165 130,319 Binding site (3); Chain (1); Glycosylation (3); Metal binding (5); Modified residue (5); Nucleotide binding (4); Sequence conflict (6); Topological domain (4); Transmembrane (12) TRANSMEM 150 166 Helical. {ECO:0000255}.; TRANSMEM 179 195 Helical. {ECO:0000255}.; TRANSMEM 212 228 Helical. {ECO:0000255}.; TRANSMEM 237 253 Helical. {ECO:0000255}.; TRANSMEM 257 273 Helical. {ECO:0000255}.; TRANSMEM 287 303 Helical. {ECO:0000255}.; TRANSMEM 671 688 Helical. {ECO:0000255}.; TRANSMEM 699 715 Helical. {ECO:0000255}.; TRANSMEM 740 756 Helical. {ECO:0000255}.; TRANSMEM 817 833 Helical. {ECO:0000255}.; TRANSMEM 836 852 Helical. {ECO:0000255}.; TRANSMEM 894 910 Helical. {ECO:0000255}. TOPO_DOM 1 149 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 304 670 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 757 816 Extracellular. {ECO:0000255}.; TOPO_DOM 911 1165 Cytoplasmic. {ECO:0000255}. FUNCTION: Catalyzes the formation of the signaling molecule cAMP downstream of G protein-coupled receptors (PubMed:18071070, PubMed:24363043). Functions in signaling cascades downstream of beta-adrenergic receptors in the heart and in vascular smooth muscle cells (PubMed:18071070). Functions in signaling cascades downstream of the vasopressin receptor in the kidney and has a role in renal water reabsorption (PubMed:20466003, PubMed:20864687). Functions in signaling cascades downstream of PTH1R and plays a role in regulating renal phosphate excretion (PubMed:24854272). Functions in signaling cascades downstream of the VIP and SCT receptors in pancreas and contributes to the regulation of pancreatic amylase and fluid secretion (PubMed:23753526). Signaling mediates cAMP-dependent activation of protein kinase PKA and promotes increased phosphorylation of various proteins, including AKT (PubMed:18071070, PubMed:23753526). Plays a role in regulating cardiac sarcoplasmic reticulum Ca(2+) uptake and storage, and is required for normal heart ventricular contractibility (PubMed:18071070). May contribute to normal heart function (PubMed:18071070, PubMed:20359598). Mediates vasodilatation after activation of beta-adrenergic receptors by isoproterenol (By similarity). Contributes to bone cell responses to mechanical stimuli (PubMed:20371630, PubMed:24277577). {ECO:0000250|UniProtKB:O43306, ECO:0000269|PubMed:1379717, ECO:0000269|PubMed:18071070, ECO:0000269|PubMed:20359598, ECO:0000269|PubMed:20371630, ECO:0000269|PubMed:20466003, ECO:0000269|PubMed:20864687, ECO:0000269|PubMed:23753526, ECO:0000269|PubMed:24277577, ECO:0000269|PubMed:24363043, ECO:0000269|PubMed:24854272}. PTM: Phosphorylation by RAF1 increases enzyme activity. Phosphorylation by PKA on Ser-659 inhibits the GNAS-mediated increase in catalytic activity. Phosphorylation by PKC on Ser-553, Ser-659 and Thr-916 inhibits catalytic activity. {ECO:0000250|UniProtKB:Q03343}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1379717, ECO:0000269|PubMed:20466003, ECO:0000269|PubMed:21670265}; Multi-pass membrane protein {ECO:0000269|PubMed:21670265}. Cell projection, cilium {ECO:0000269|PubMed:20371630, ECO:0000269|PubMed:20466003, ECO:0000269|PubMed:21670265}. Cell projection, stereocilium {ECO:0000269|PubMed:17567809}. SUBUNIT: Part of a complex containing AKAP5, ADCY5, PDE4C and PKD2 (PubMed:21670265). Interacts with RAF1. Interacts (via cytoplasmic N-terminus) with GNAS, GNB1 and GNG2 (By similarity). {ECO:0000250|UniProtKB:O43306, ECO:0000269|PubMed:21670265}. DOMAIN: The protein contains two modules with six transmembrane helices each; both are required for catalytic activity. Isolated N-terminal or C-terminal guanylate cyclase domains have no catalytic activity, but when they are brought together, enzyme activity is restored. The active site is at the interface of the two domains. Both contribute substrate-binding residues, but the catalytic metal ions are bound exclusively via the N-terminal guanylate cyclase domain. {ECO:0000250|UniProtKB:P26769}. TISSUE SPECIFICITY: Detected in kidney tubules (PubMed:20466003). Detected in primary bone cells with osteocyte morphology (PubMed:24277577). Detected in heart (at protein level) (PubMed:18071070). Highly expressed in heart (PubMed:1379717, PubMed:18071070). Detected in kidney, pancreas acini and ducts (PubMed:23753526). Expressed in cochlear outer and inner hair cells (PubMed:17567809). Weakly detectable in brain, intestine, lung and spleen (PubMed:1379717). {ECO:0000269|PubMed:1379717, ECO:0000269|PubMed:17567809, ECO:0000269|PubMed:18071070, ECO:0000269|PubMed:20466003, ECO:0000269|PubMed:23753526, ECO:0000269|PubMed:24277577}. +O35674 ADA19_MOUSE Disintegrin and metalloproteinase domain-containing protein 19 (ADAM 19) (EC 3.4.24.-) (Meltrin-beta) 920 100,860 Active site (1); Chain (1); Compositional bias (3); Disulfide bond (7); Domain (3); Glycosylation (4); Metal binding (4); Motif (2); Propeptide (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 704 724 Helical. {ECO:0000255}. TOPO_DOM 27 703 Extracellular. {ECO:0000255}.; TOPO_DOM 725 920 Cytoplasmic. {ECO:0000255}. FUNCTION: Participates in the proteolytic processing of beta-type neuregulin isoforms which are involved in neurogenesis and synaptogenesis, suggesting a regulatory role in glial cell. Also cleaves alpha-2 macroglobulin. May be involved in osteoblast differentiation and/or osteoblast activity in bone (By similarity). {ECO:0000250, ECO:0000269|PubMed:11116142}. PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Interacts with SH3PXD2A. {ECO:0000250}. DOMAIN: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme. TISSUE SPECIFICITY: Widely expressed, with the highest expression in bone, heart and lung, followed by brain and spleen and relatively low expression in liver, skeletal muscle, kidney and testis. In bone, primarily expressed in cell of the osteoblast lineage and not detected in mature osteoclasts. +P97490 ADCY8_MOUSE Adenylate cyclase type 8 (EC 4.6.1.1) (ATP pyrophosphate-lyase 8) (Adenylate cyclase type VIII) (Adenylyl cyclase 8) (Ca(2+)/calmodulin-activated adenylyl cyclase) 1249 140,095 Binding site (3); Chain (1); Glycosylation (3); Metal binding (5); Modified residue (3); Motif (2); Nucleotide binding (4); Region (4); Sequence conflict (3); Site (5); Topological domain (3); Transmembrane (12) TRANSMEM 181 201 Helical. {ECO:0000255}.; TRANSMEM 210 230 Helical. {ECO:0000255}.; TRANSMEM 245 265 Helical. {ECO:0000255}.; TRANSMEM 272 292 Helical. {ECO:0000255}.; TRANSMEM 294 314 Helical. {ECO:0000255}.; TRANSMEM 319 339 Helical. {ECO:0000255}.; TRANSMEM 714 734 Helical. {ECO:0000255}.; TRANSMEM 736 756 Helical. {ECO:0000255}.; TRANSMEM 785 805 Helical. {ECO:0000255}.; TRANSMEM 829 849 Helical. {ECO:0000255}.; TRANSMEM 859 879 Helical. {ECO:0000255}.; TRANSMEM 892 912 Helical. {ECO:0000255}. TOPO_DOM 1 180 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 340 713 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 913 1249 Cytoplasmic. {ECO:0000255}. FUNCTION: Catalyzes the formation of cAMP in response to calcium entry leadings to cAMP signaling activation that affect processes suche as synaptic plasticity and insulin secretion (PubMed:10864938, PubMed:25403481, PubMed:10482244, PubMed:14585998, PubMed:18448650). Plays a role in many brain functions, such as learning, memory, drug addiction, and anxiety modulation through regulation of synaptic plasticity by modulating long-term memory and long-term potentiation (LTP) through CREB transcription factor activity modulation (PubMed:10482244, PubMed:14585998, PubMed:18448650, PubMed:10864938, PubMed:12441059, PubMed:20638449, PubMed:27234425, PubMed:18222416). Plays a central role in insulin secretion by controlling glucose homeostasis through glucagon-like peptide 1 and glucose signaling pathway and maintains insulin secretion through calcium-dependent PKA activation leading to vesicle pool replenishment (PubMed:25403481). Also, allows PTGER3 to induce potentiation of PTGER4-mediated PLA2 secretion by switching from a negative to a positive regulation, during the IL1B induced-dedifferentiation of smooth muscle cells (By similarity). {ECO:0000250|UniProtKB:P40146, ECO:0000269|PubMed:10482244, ECO:0000269|PubMed:10864938, ECO:0000269|PubMed:12441059, ECO:0000269|PubMed:14585998, ECO:0000269|PubMed:18222416, ECO:0000269|PubMed:18448650, ECO:0000269|PubMed:20638449, ECO:0000269|PubMed:25403481, ECO:0000269|PubMed:27234425}. PTM: Phosphorylated by PKA; mediates inhibition of adenylate cyclase activity at membrane raft; does not influence either CALM1 or PPP2CA interaction with ADCY8. {ECO:0000250|UniProtKB:P40146}.; PTM: N-glycosylated; N-glycosylation is responsible for raft-targeting; is not necessary for CCE-stimulated adenylate cyclase activity. {ECO:0000250|UniProtKB:P40146}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14585998}; Multi-pass membrane protein. Basolateral cell membrane {ECO:0000269|PubMed:14585998}. Apical cell membrane {ECO:0000269|PubMed:14585998}. Cell junction, synapse {ECO:0000269|PubMed:14585998}. Cell projection, dendrite {ECO:0000269|PubMed:14585998, ECO:0000269|PubMed:17335981}. Cell projection, axon {ECO:0000269|PubMed:14585998, ECO:0000269|PubMed:17335981}. Cell junction, synapse, presynaptic cell membrane {ECO:0000269|PubMed:17335981, ECO:0000269|PubMed:18448650}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000269|PubMed:17335981}. Membrane raft {ECO:0000250|UniProtKB:P40146}. Membrane, coated pit {ECO:0000250|UniProtKB:P40146}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250|UniProtKB:P40146}. Membrane, caveola {ECO:0000250|UniProtKB:P40146}. Note=Localized to dendritic arbors (PubMed:17335981). Monomeric N-glycosylated species localizes in membrane raft. In contrast, monomeric unglycosylated forms are enriched in clathrin-coated pits and vesicles. Dimers are also localized outside of membrane rafts. Membrane raft localization and integrity is indispensable for CCE-stimulated adenylate cyclase activity (By similarity). {ECO:0000250|UniProtKB:P40146, ECO:0000269|PubMed:17335981}. SUBUNIT: Homodimer; via transmembrane domain (PubMed:19158400). Monomer (PubMed:19158400). Heterodimer. Oligemer; via transmembrane domain. Interacts with PRKAR2A and AKAP5; inhibits adenylate cyclase activity through PKA phosphorylation. Interacts with PPP2CA and PPP2R1A; does not mediate the inhibitory effects of PKA on adenylate cyclase activity; interaction is dependent of catalytically active PPP2CA; antagonizes interaction with calmodulin. Interacts with AKAP5 (palmitoylated form); promotes the phosphorylation of ADCY8 after store-operated calcium entry (SOCE) stimulation at membrane raft. Interacts with ORAI1; interaction is calcium store depletion independent; interaction occurs in membrane raft; interaction increases markedly after store depletion; positively regulates SOCE-induced adenylate cyclase activity; contributes to the targeting of ADCY8 to discrete regions of the plasma membrane that are shielded from other calcium events. Interacts with STIM1. Interacts with actin; interaction is calcium independent; interaction is affected by calcium-calmodulin; interaction controls the distribution and regulation of ADCY8. Interacts with calmodulin; at rest, interacts via N-terminal domain; upon a calcium rise, calmodulin becomes calcium-saturated and subsequently binds to the C-terminal domain forming an autoinhibitory complex; fully calcium-saturated calmodulin leaves the N-terminal domain, binding solely to the C-terminal domain leading to dissociation of autoinhibitory complex and resulting in activation of adenylate cyclase; antagonizes interaction with PPP2CA; interaction is calcium dependent. Interacts with PPP2R5D (By similarity). {ECO:0000250|UniProtKB:P40146, ECO:0000269|PubMed:19158400}. DOMAIN: The protein contains two modules with six transmembrane helices each; both are required for catalytic activity. Isolated N-terminal or C-terminal guanylate cyclase domains have no catalytic activity, but when they are brought together, enzyme activity is restored. The active site is at the interface of the two domains. Both contribute substrate-binding residues, but the catalytic metal ions are bound exclusively via the N-terminal guanylate cyclase domain. The two transmembrane clusters are necessary and suficient for the plasma membrane targeting and oligomers assembly. The N-terminal and C-terminal domains interact at rest as part of a larger autoinhibitory complex, with calmodulin pre-associated at the N-terminal domain; the binding is specifically inhibited by fully calcium-saturated calmodulin, resulting in activation of AC8. {ECO:0000250|UniProtKB:P40146}. TISSUE SPECIFICITY: Abundantly expressed within the olfactory bulb, thalamus, habenula, CA1 region of the hippocampus, and hypothalamus (PubMed:10864938). Strongly expressed in pyramidal cells of CA1 and weakly in CA3 and the dentate gyrus. Strongly and homogeneously expressed in all cell layers of the anterior cingulate cortex (ACC). Widely expressed in the insular cortex. Weakly expressed in the spinal dorsal horn (PubMed:12441059). Abundantly present in the CA1/CA2 region in the hippocampus neonatal and intensifies by adulthood. Weakly expressed in the cerebellum at postnatal day 7 and decreased further by postnatal day 14 (PubMed:17335981). {ECO:0000269|PubMed:10864938, ECO:0000269|PubMed:12441059, ECO:0000269|PubMed:17335981}. +P45952 ACADM_MOUSE Medium-chain specific acyl-CoA dehydrogenase, mitochondrial (MCAD) (EC 1.3.8.7) 421 46,481 Active site (1); Binding site (3); Chain (1); Modified residue (18); Nucleotide binding (6); Region (1); Sequence conflict (2); Transit peptide (1) Lipid metabolism; mitochondrial fatty acid beta-oxidation. FUNCTION: Acyl-CoA dehydrogenase specific for acyl chain lengths of 4 to 16 that catalyzes the initial step of fatty acid beta-oxidation. Utilizes the electron transfer flavoprotein (ETF) as an electron acceptor to transfer electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase). {ECO:0000250|UniProtKB:P11310}. PTM: Acetylation at Lys-307 and Lys-311 in proximity of the cofactor-binding sites reduces catalytic activity. These sites are deacetylated by SIRT3 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. SUBUNIT: Homotetramer. {ECO:0000250}. +O54967 ACK1_MOUSE Activated CDC42 kinase 1 (ACK-1) (EC 2.7.10.2) (EC 2.7.11.1) (Non-receptor protein tyrosine kinase Ack) (Tyrosine kinase non-receptor protein 2) 1055 116,975 Active site (1); Alternative sequence (2); Binding site (1); Chain (1); Compositional bias (1); Domain (4); Modified residue (10); Mutagenesis (4); Nucleotide binding (1); Region (4); Sequence caution (1); Sequence conflict (7) FUNCTION: Non-receptor tyrosine-protein and serine/threonine-protein kinase that is implicated in cell spreading and migration, cell survival, cell growth and proliferation. Transduces extracellular signals to cytosolic and nuclear effectors. Phosphorylates AKT1, AR, MCF2, WASL and WWOX. Implicated in trafficking and clathrin-mediated endocytosis through binding to epidermal growth factor receptor (EGFR) and clathrin. Binds to both poly- and mono-ubiquitin and regulates ligand-induced degradation of EGFR, thereby contributing to the accumulation of EGFR at the limiting membrane of early endosomes. Downstream effector of CDC42 which mediates CDC42-dependent cell migration via phosphorylation of BCAR1. May be involved both in adult synaptic function and plasticity and in brain development. Activates AKT1 by phosphorylating it on 'Tyr-176'. Phosphorylates AR on 'Tyr-267' and 'Tyr-363' thereby promoting its recruitment to androgen-responsive enhancers (AREs). Phosphorylates WWOX on 'Tyr-287'. Phosphorylates MCF2, thereby enhancing its activity as a guanine nucleotide exchange factor (GEF) toward Rho family proteins. Contributes to the control of AXL receptor levels. Confers metastatic properties on cancer cells and promotes tumor growth by negatively regulating tumor suppressor such as WWOX and positively regulating pro-survival factors such as AKT1 and AR. {ECO:0000269|PubMed:17182860, ECO:0000269|PubMed:20333297}. PTM: Autophosphorylation regulates kinase activity. Phosphorylation on Tyr-533 is required for interaction with SRC and is observed during association with clathrin-coated pits (By similarity). {ECO:0000250}.; PTM: Polyubiquitinated by NEDD4 and NEDD4L. Degradation can be induced by EGF and is lysosome-dependent. {ECO:0000269|PubMed:20086093}. SUBCELLULAR LOCATION: Cell membrane. Nucleus. Endosome. Cell junction, adherens junction. Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250}. Membrane, clathrin-coated pit {ECO:0000250}. Note=The Tyr-284 phosphorylated form is found both in the membrane and nucleus. Co-localizes with EGFR on endosomes. Nuclear translocation is CDC42-dependent. SUBUNIT: Homodimer. Interacts with CSPG4 (activated). Interacts with MERTK (activated); stimulates autophosphorylation. May interact (phosphorylated) with HSP90AB1; maintains kinase activity. Interacts with NPHP1. Interacts with SNX9 (via SH3 domain). Interacts with SRC (via SH2 and SH3 domain). Part of a collagen stimulated complex involved in cell migration composed of CDC42, CRK, TNK2 and BCAR1/p130cas. Interacts with BCAR1/p130cas via SH3 domains. Forms complexes with GRB2 and numerous receptor tyrosine kinases (RTK) including LTK, AXL or PDGFRL, in which GRB2 promotes RTK recruitment by TNK2 (By similarity). Interacts with CDC42. Interacts with EGFR, and this interaction is dependent on EGF stimulation and kinase activity of EGFR. Interacts (via kinase domain) with AKT1. Interacts with NEDD4 (via WW3 domain). NEDD4L and EGF promote association with NEDD4. {ECO:0000250, ECO:0000269|PubMed:16052498, ECO:0000269|PubMed:17182860, ECO:0000269|PubMed:20086093, ECO:0000269|PubMed:20333297}. DOMAIN: The EBD (EGFR-binding domain) domain is necessary for interaction with EGFR.; DOMAIN: The SAM-like domain is necessary for NEDD4-mediated ubiquitination. Promotes membrane localization and dimerization to allow for autophosphorylation.; DOMAIN: The UBA domain binds both poly- and mono-ubiquitin. TISSUE SPECIFICITY: Ubiquitously present in all tissues tested. Highly expressed in the adult central nervous system (CNS); hippocampus, neocortex, and cerebellum, both at dendritic spines and presynaptic axon terminals. Levels are strongly increased during enhanced neural activity. {ECO:0000269|PubMed:16052498, ECO:0000269|PubMed:16750431, ECO:0000269|PubMed:16777958}. +P58137 ACOT8_MOUSE Acyl-coenzyme A thioesterase 8 (Acyl-CoA thioesterase 8) (EC 3.1.2.27) (Choloyl-coenzyme A thioesterase) (Peroxisomal acyl-CoA thioesterase 2) (PTE-2) (Peroxisomal acyl-coenzyme A thioester hydrolase 1) (PTE-1) (Peroxisomal long-chain acyl-CoA thioesterase 1) 320 35,827 Active site (3); Chain (1); Motif (1); Sequence conflict (1) FUNCTION: Acyl-coenzyme A (acyl-CoA) thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH (PubMed:11673457). Competes with bile acid CoA:amino acid N-acyltransferase (BAAT) for bile acid-CoA substrate (such as chenodeoxycholoyl-CoA) (PubMed:11673457). Shows a preference for medium-length fatty acyl-CoAs (C2 to C20) (PubMed:11673457). Catalyzes the hydrolysis of CoA esters of bile acids, such as choloyl-CoA and chenodeoxycholoyl-CoA (PubMed:11673457). May be involved in the metabolic regulation of peroxisome proliferation (By similarity). {ECO:0000250|UniProtKB:O14734, ECO:0000269|PubMed:11673457}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O14734}. Peroxisome matrix {ECO:0000269|PubMed:11673457}. Note=Predominantly localized in the peroxisome (PubMed:11673457). {ECO:0000269|PubMed:11673457}. SUBUNIT: homodimer. {ECO:0000269|PubMed:11673457}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11673457}. +Q8R5C5 ACTY_MOUSE Beta-centractin (Actin-related protein 1B) (ARP1B) 376 42,281 Chain (1); Modified residue (2) FUNCTION: Component of a multi-subunit complex involved in microtubule based vesicle motility. It is associated with the centrosome (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. +Q3V140 ACRBP_MOUSE Acrosin-binding protein (Proacrosin-binding protein sp32) 540 61,141 Alternative sequence (2); Chain (1); Sequence conflict (4); Signal peptide (1) FUNCTION: May be involved in packaging and condensation of the acrosin zymogen in the acrosomal matrix via its association with proacrosin. {ECO:0000250}. PTM: The N-terminus is blocked. {ECO:0000250}.; PTM: Phosphorylated on Tyr residues in capacitated sperm. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q29016}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:22357636}. SUBUNIT: Binds proacrosin. {ECO:0000250|UniProtKB:Q29016}. TISSUE SPECIFICITY: Expressed by testicular and epididymal spermatozoa (at protein level). {ECO:0000269|PubMed:22357636}. +Q61271 ACV1B_MOUSE Activin receptor type-1B (EC 2.7.11.30) (Activin receptor type IB) (ACTR-IB) (Activin receptor-like kinase 4) (ALK-4) (Serine/threonine-protein kinase receptor R2) (SKR2) 505 56,700 Active site (1); Binding site (1); Chain (1); Domain (2); Glycosylation (1); Modified residue (1); Nucleotide binding (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 127 149 Helical. {ECO:0000255}. TOPO_DOM 24 126 Extracellular. {ECO:0000255}.; TOPO_DOM 150 505 Cytoplasmic. {ECO:0000255}. FUNCTION: Transmembrane serine/threonine kinase activin type-1 receptor forming an activin receptor complex with activin receptor type-2 (ACVR2A or ACVR2B). Transduces the activin signal from the cell surface to the cytoplasm and is thus regulating a many physiological and pathological processes including neuronal differentiation and neuronal survival, hair follicle development and cycling, FSH production by the pituitary gland, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. Activin is also thought to have a paracrine or autocrine role in follicular development in the ovary. Within the receptor complex, type-2 receptors (ACVR2A and/or ACVR2B) act as a primary activin receptors whereas the type-1 receptors like ACVR1B act as downstream transducers of activin signals. Activin binds to type-2 receptor at the plasma membrane and activates its serine-threonine kinase. The activated receptor type-2 then phosphorylates and activates the type-1 receptor such as ACVR1B. Once activated, the type-1 receptor binds and phosphorylates the SMAD proteins SMAD2 and SMAD3, on serine residues of the C-terminal tail. Soon after their association with the activin receptor and subsequent phosphorylation, SMAD2 and SMAD3 are released into the cytoplasm where they interact with the common partner SMAD4. This SMAD complex translocates into the nucleus where it mediates activin-induced transcription. Inhibitory SMAD7, which is recruited to ACVR1B through FKBP1A, can prevent the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. Activin signal transduction is also antagonized by the binding to the receptor of inhibin-B via the IGSF1 inhibin coreceptor. ACVR1B also phosphorylates TDP2. {ECO:0000269|PubMed:16885157, ECO:0000269|PubMed:18039968}. PTM: Autophosphorylated. Phosphorylated by activin receptor type-2 (ACVR2A or ACVR2B) in response to activin-binding at serine and threonine residues in the GS domain. Phosphorylation of ACVR1B by activin receptor type-2 regulates association with SMAD7 (By similarity). {ECO:0000250}.; PTM: Ubiquitinated. Level of ubiquitination is regulated by the SMAD7-SMURF1 complex (By similarity). {ECO:0000250}.; PTM: Ubiquitinated. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Forms an activin receptor complex with activin receptor type-2 (ACVR2A or ACVR2B). Interacts with TDP2 (By similarity). Interacts with AIP1, FKBP1A, IGSF1, TDGF1, SMAD2, SMAD3 and SMAD7 (By similarity). {ECO:0000250}. DOMAIN: The GS domain is a 30-amino-acid sequence adjacent to the N-terminal boundary of the kinase domain and highly conserved in all other known type-1 receptors but not in type-2 receptors. The GS domain is the site of activation through phosphorylation by the II receptors (By similarity). {ECO:0000250}. +Q91XE4 ACY3_MOUSE N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming) (EC 3.5.1.114) (Acylase III) (Aminoacylase III) (AAIII) (Aminoacylase-3) (ACY-3) (Aspartoacylase-2) (Hepatitis C virus core-binding protein 1) (HCBP1) 318 35,286 Beta strand (17); Binding site (3); Chain (1); Helix (10); Metal binding (3); Modified residue (1); Mutagenesis (2); Region (3); Sequence conflict (3); Turn (2) FUNCTION: Plays an important role in deacetylating mercapturic acids in kidney proximal tubules. Also acts on N-acetyl-aromatic amino acids. {ECO:0000269|PubMed:14656720, ECO:0000269|PubMed:17012540}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:14656720}; Peripheral membrane protein {ECO:0000269|PubMed:14656720}. Cytoplasm {ECO:0000269|PubMed:14656720}. Note=Predominantly localized in the apical membrane of cells in the S1 segment. In the proximal straight tubules (S2 and S3 segments) is expressed diffusely throughout the cytoplasm. SUBUNIT: Exists as a mixture of homodimers and homotetramer, both catalytically active. {ECO:0000269|PubMed:14656720, ECO:0000269|PubMed:17434493, ECO:0000269|PubMed:20921362}. TISSUE SPECIFICITY: Expressed predominantly in kidney and to a lesser extent in liver. Weakly expressed in heart, small intestine, brain, lung, testis, and stomach. {ECO:0000269|PubMed:14656720}. +Q91VA0 ACSM1_MOUSE Acyl-coenzyme A synthetase ACSM1, mitochondrial (EC 6.2.1.2) (Acyl-CoA synthetase medium-chain family member 1) (Butyrate--CoA ligase 1) (Butyryl-coenzyme A synthetase 1) (Lipoate-activating enzyme) (Middle-chain acyl-CoA synthetase 1) 573 64,760 Alternative sequence (1); Binding site (3); Chain (1); Modified residue (18); Nucleotide binding (1); Sequence conflict (2); Transit peptide (1) FUNCTION: Functions as GTP-dependent lipoate-activating enzyme that generates the substrate for lipoyltransferase (By similarity). Has medium-chain fatty acid:CoA ligase activity with broad substrate specificity (in vitro). Acts on acids from C(4) to C(11) and on the corresponding 3-hydroxy- and 2,3- or 3,4-unsaturated acids (in vitro). {ECO:0000250, ECO:0000269|PubMed:11470804}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:11470804}. SUBUNIT: Monomer. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in liver and kidney. {ECO:0000269|PubMed:11470804}. +O88839 ADA15_MOUSE Disintegrin and metalloproteinase domain-containing protein 15 (ADAM 15) (EC 3.4.24.-) (AD56) (Metalloprotease RGD disintegrin protein) (Metalloproteinase-like, disintegrin-like, and cysteine-rich protein 15) (MDC-15) (Metargidin) 864 92,664 Active site (1); Alternative sequence (3); Chain (1); Compositional bias (2); Disulfide bond (7); Domain (3); Glycosylation (5); Metal binding (4); Modified residue (2); Motif (3); Mutagenesis (6); Propeptide (1); Sequence conflict (15); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 697 717 Helical. {ECO:0000255}. TOPO_DOM 208 696 Extracellular. {ECO:0000255}.; TOPO_DOM 718 864 Cytoplasmic. {ECO:0000255}. FUNCTION: Active metalloproteinase with gelatinolytic and collagenolytic activity. Plays a role in the wound healing process. Mediates both heterotypic intraepithelial cell/T-cell interactions and homotypic T-cell aggregation. Inhibits beta-1 integrin-mediated cell adhesion and migration of airway smooth muscle cells. Suppresses cell motility on or towards fibronectin possibly by driving alpha-v/beta-1 integrin (ITAGV-ITGB1) cell surface expression via ERK1/2 inactivation. Cleaves E-cadherin in response to growth factor deprivation. Plays a role in glomerular cell migration (By similarity). Plays a role in pathological neovascularization. May play a role in cartilage remodeling. May be proteolytically processed, during sperm epididymal maturation and the acrosome reaction. May play a role in sperm-egg binding through its disintegrin domain. Interactions with egg membrane could be mediated via binding between the disintegrin-like domain to one or more integrin receptors on the egg. {ECO:0000250, ECO:0000269|PubMed:11882657, ECO:0000269|PubMed:12897135, ECO:0000269|PubMed:15818704, ECO:0000269|PubMed:18390692}. PTM: The precursor is cleaved by a furin endopeptidase. An additional membrane proximal site of cleavage affects a small percentage of the proteins and results in disulfide-linked fragments. The prodomain is apparently cleaved in several positions that are N-terminal of the furin cleavage site. {ECO:0000269|PubMed:9748307}.; PTM: May be partially sialylated.; PTM: Phosphorylation increases association with PTKs. {ECO:0000250}. SUBCELLULAR LOCATION: Endomembrane system {ECO:0000269|PubMed:18390692}; Single-pass type I membrane protein {ECO:0000269|PubMed:18390692}. Cell junction, adherens junction {ECO:0000250}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:18390692}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:18390692}. Note=The majority of the protein is localized in a perinuclear compartment which may correspond to the trans-Golgi network or the late endosome. The pro-protein is the major detectable form on the cell surface, whereas the majority of the protein in the cell is processed. SUBUNIT: Interacts specifically with Src family protein-tyrosine kinases (PTKs) (By similarity). Interacts with ITAGV-ITGB3 (vitronectin receptor). Interacts with SH3GL2 and SNX9; this interaction occurs preferentially with ADAM15 precursor, rather than the processed form, suggesting it occurs in a secretory pathway compartment prior to the medial Golgi. Interacts with ITAG9-ITGB1. Interacts with SH3PXD2A (By similarity). Interacts with ITAGV-ITGB1. Interacts with GRB2, HCK, ITSN1, ITSN2, LYN, MAPK1, MAPK3, NCF1, NCK1, nephrocystin, PTK6, SNX33, LCK and SRC (By similarity). {ECO:0000250}. DOMAIN: The cytoplasmic domain is required for SH3GL2- and SNX9-binding.; DOMAIN: Disintegrin domain binds to integrin alphaV-beta3. {ECO:0000250}.; DOMAIN: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme. TISSUE SPECIFICITY: Expressed moderately in pericytes of retina. Expressed in testis and in spermatozoa from the caput, corpus, and cauda epididymis, as well as in non-capacitated and acrosome-reacted sperm (at protein level). Highly expressed in heart, brain, lung, and kidney. Expressed at lower levels in spleen, liver, testis and muscle. {ECO:0000269|PubMed:18381816, ECO:0000269|PubMed:18390692}. +Q91WF3 ADCY4_MOUSE Adenylate cyclase type 4 (EC 4.6.1.1) (ATP pyrophosphate-lyase 4) (Adenylate cyclase type IV) (Adenylyl cyclase 4) 1077 120,380 Binding site (3); Chain (1); Glycosylation (2); Metal binding (5); Modified residue (2); Nucleotide binding (4); Topological domain (4); Transmembrane (12) TRANSMEM 29 50 Helical. {ECO:0000255}.; TRANSMEM 61 80 Helical. {ECO:0000255}.; TRANSMEM 94 117 Helical. {ECO:0000255}.; TRANSMEM 120 138 Helical. {ECO:0000255}.; TRANSMEM 141 162 Helical. {ECO:0000255}.; TRANSMEM 170 190 Helical. {ECO:0000255}.; TRANSMEM 583 604 Helical. {ECO:0000255}.; TRANSMEM 608 630 Helical. {ECO:0000255}.; TRANSMEM 661 684 Helical. {ECO:0000255}.; TRANSMEM 718 738 Helical. {ECO:0000255}.; TRANSMEM 746 766 Helical. {ECO:0000255}.; TRANSMEM 793 809 Helical. {ECO:0000255}. TOPO_DOM 1 28 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 191 582 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 685 717 Extracellular. {ECO:0000255}.; TOPO_DOM 810 1077 Cytoplasmic. {ECO:0000255}. FUNCTION: Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling. {ECO:0000250|UniProtKB:P26770}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P26770}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P26770}. Cytoplasm {ECO:0000250|UniProtKB:Q8NFM4}. DOMAIN: The protein contains two modules with six transmembrane helices each; both are required for catalytic activity. Isolated N-terminal or C-terminal modules have no catalytic activity, but when they are brought together, enzyme activity is restored. The active site is at the interface of the two modules. {ECO:0000250|UniProtKB:P30803}. +Q9JHI2 ADAT1_MOUSE tRNA-specific adenosine deaminase 1 (mADAT1) (EC 3.5.4.34) (tRNA-specific adenosine-37 deaminase) 499 55,355 Active site (1); Alternative sequence (2); Binding site (6); Chain (1); Domain (1); Metal binding (3); Modified residue (1); Sequence conflict (1) FUNCTION: Specifically deaminates adenosine-37 to inosine in tRNA-Ala. {ECO:0000269|PubMed:10675613}. +Q6P6J0 ADAT2_MOUSE tRNA-specific adenosine deaminase 2 (EC 3.5.4.33) (Deaminase domain-containing protein 1) (tRNA-specific adenosine-34 deaminase subunit ADAT2) 191 21,308 Active site (1); Chain (1); Domain (1); Metal binding (3); Sequence conflict (4) FUNCTION: Probably participates in deamination of adenosine-34 to inosine in many tRNAs. {ECO:0000250}. +A2AM29 AF9_MOUSE Protein AF-9 (Myeloid/lymphoid or mixed-lineage leukemia translocated to chromosome 3 protein homolog) 569 63,375 Chain (1); Compositional bias (3); Cross-link (1); Domain (1); Modified residue (5); Motif (1); Sequence conflict (6) FUNCTION: Chromatin reader component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. Specifically recognizes and binds acylated histone H3, with a marked preference for histone H3 that is crotonylated. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. Recognizes and binds histone H3 crotonylated at 'Lys-9' (H3K9cr), and with slightly lower affinity histone H3 crotonylated at 'Lys-18' (H3K18cr). Also recognizes and binds histone H3 acetylated at 'Lys-9' (H3K9ac), but with lower affinity than crotonylated histone H3. In the SEC complex, MLLT3 is required to recruit the complex to crotonylated histones. {ECO:0000250|UniProtKB:P42568}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00376, ECO:0000269|PubMed:11439343}. Chromosome {ECO:0000250|UniProtKB:P42568}. Note=Colocalizes with acylated histone H3. H3 Colocalizes with histone H3 crotonylated at 'Lys-18' (H3K18cr). {ECO:0000250|UniProtKB:P42568}. SUBUNIT: Component of the super elongation complex (SEC), at least composed of EAF1, EAF2, CDK9, MLLT3/AF9, AFF (AFF1 or AFF4), the P-TEFb complex and ELL (ELL, ELL2 or ELL3) (By similarity). Interacts with BCOR (By similarity). Interacts with CBX8 (PubMed:11439343). Interacts with ALKBH4 (By similarity). {ECO:0000250|UniProtKB:P42568, ECO:0000269|PubMed:11439343}. DOMAIN: The YEATS domain specifically recognizes and binds acylated histones, with a marked preference histones that are crotonylated. Also binds histone H3 acetylated at 'Lys-9' (H3K9ac), but with lower affinity. {ECO:0000250|UniProtKB:P42568}. TISSUE SPECIFICITY: Ubiquitously expressed. Strong expression in the spleen. {ECO:0000269|PubMed:11439343}. +Q920H4 ACM5_MOUSE Muscarinic acetylcholine receptor M5 532 60,253 Chain (1); Disulfide bond (1); Glycosylation (1); Modified residue (2); Sequence conflict (4); Topological domain (8); Transmembrane (7) TRANSMEM 30 53 Helical; Name=1. {ECO:0000250}.; TRANSMEM 67 87 Helical; Name=2. {ECO:0000250}.; TRANSMEM 105 126 Helical; Name=3. {ECO:0000250}.; TRANSMEM 147 169 Helical; Name=4. {ECO:0000250}.; TRANSMEM 192 214 Helical; Name=5. {ECO:0000250}.; TRANSMEM 444 464 Helical; Name=6. {ECO:0000250}.; TRANSMEM 479 498 Helical; Name=7. {ECO:0000250}. TOPO_DOM 1 29 Extracellular. {ECO:0000250}.; TOPO_DOM 54 66 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 88 104 Extracellular. {ECO:0000250}.; TOPO_DOM 127 146 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 170 191 Extracellular. {ECO:0000250}.; TOPO_DOM 215 443 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 465 478 Extracellular. {ECO:0000250}.; TOPO_DOM 499 532 Cytoplasmic. {ECO:0000250}. FUNCTION: The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is Pi turnover (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein. +Q8R519 ACMSD_MOUSE 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase (EC 4.1.1.45) (Picolinate carboxylase) 336 38,027 Binding site (1); Chain (1); Metal binding (4) Secondary metabolite metabolism; quinolate metabolism. FUNCTION: Converts alpha-amino-beta-carboxymuconate-epsilon-semialdehyde (ACMS) to alpha-aminomuconate semialdehyde (AMS). ACMS can be converted non-enzymatically to quinolate (QA), a key precursor of NAD, and a potent endogenous excitotoxin of neuronal cells which is implicated in the pathogenesis of various neurodegenerative disorders. In the presence of ACMSD, ACMS is converted to AMS, a benign catabolite. ACMSD ultimately controls the metabolic fate of tryptophan catabolism along the kynurenine pathway. SUBUNIT: Monomer. {ECO:0000250}. TISSUE SPECIFICITY: Highest expression in kidney with lower levels in liver and brain. {ECO:0000269|PubMed:12140278}. +P12657 ACM1_MOUSE Muscarinic acetylcholine receptor M1 460 51,379 Chain (1); Disulfide bond (1); Glycosylation (2); Modified residue (5); Sequence conflict (4); Topological domain (8); Transmembrane (7) TRANSMEM 25 47 Helical; Name=1. {ECO:0000250}.; TRANSMEM 62 82 Helical; Name=2. {ECO:0000250}.; TRANSMEM 100 121 Helical; Name=3. {ECO:0000250}.; TRANSMEM 142 164 Helical; Name=4. {ECO:0000250}.; TRANSMEM 187 209 Helical; Name=5. {ECO:0000250}.; TRANSMEM 367 387 Helical; Name=6. {ECO:0000250}.; TRANSMEM 402 421 Helical; Name=7. {ECO:0000250}. TOPO_DOM 1 24 Extracellular. {ECO:0000255}.; TOPO_DOM 48 61 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 83 99 Extracellular. {ECO:0000255}.; TOPO_DOM 122 141 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 165 186 Extracellular. {ECO:0000255}.; TOPO_DOM 210 366 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 388 401 Extracellular. {ECO:0000255}.; TOPO_DOM 422 460 Cytoplasmic. {ECO:0000255}. FUNCTION: The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is Pi turnover. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein. SUBUNIT: Interacts with GPRASP2. {ECO:0000250}. +Q8BWN8 ACOT4_MOUSE Acyl-coenzyme A thioesterase 4 (Acyl-CoA thioesterase 4) (EC 3.1.2.2) (PTE-2b) (Peroxisomal acyl coenzyme A thioester hydrolase Ib) (Peroxisomal long-chain acyl-CoA thioesterase Ib) (PTE-Ib) 421 46,481 Active site (3); Chain (1); Modified residue (1); Motif (1); Sequence conflict (3) FUNCTION: Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. {ECO:0000250}. SUBCELLULAR LOCATION: Peroxisome {ECO:0000305}. TISSUE SPECIFICITY: Expressed in liver, kidney, intestine, adrenal gland and white and brown tissues. Not detected in other tissues. {ECO:0000269|PubMed:10567408}. +Q3URE1 ACSF3_MOUSE Acyl-CoA synthetase family member 3, mitochondrial (EC 6.2.1.-) 583 65,077 Alternative sequence (2); Binding site (3); Chain (1); Erroneous initiation (1); Nucleotide binding (1); Transit peptide (1) FUNCTION: Catalyzes the initial reaction in intramitochondrial fatty acid synthesis, by activating malonate and methylmalonate, but not acetate, into their respective CoA thioester. May have some preference toward very-long-chain substrates (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. +Q9JLN6 ADA28_MOUSE Disintegrin and metalloproteinase domain-containing protein 28 (ADAM 28) (EC 3.4.24.-) (Thymic epithelial cell-ADAM) (TECADAM) 793 88,671 Active site (1); Alternative sequence (3); Chain (1); Compositional bias (2); Disulfide bond (7); Domain (3); Glycosylation (7); Metal binding (4); Motif (1); Mutagenesis (1); Propeptide (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 669 689 Helical. {ECO:0000255}. TOPO_DOM 196 668 Extracellular. {ECO:0000255}.; TOPO_DOM 690 793 Cytoplasmic. {ECO:0000255}. FUNCTION: May play a role in organogenesis and organ-specific functions such as thymic T-cell development. PTM: Pro-domain removal and maturation may be, at least in part, autocatalytic. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. DOMAIN: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme. TISSUE SPECIFICITY: Strong expression in thymic epithelial cells and developmentally related tissues including the trachea, thyroid, lung and stomach, but not in lymphocytes. Expressed at high levels also in epididymis. In contrast with human is not expressed in immature or mature lymphocyte populations of thymocytes, lymph node, spleen, and bone marrow. {ECO:0000269|PubMed:11867223}. +P56376 ACYP1_MOUSE Acylphosphatase-1 (EC 3.6.1.7) (Acylphosphatase, organ-common type isozyme) (Acylphosphate phosphohydrolase 1) 99 11,241 Active site (2); Chain (1); Domain (1); Initiator methionine (1); Modified residue (1) FUNCTION: Its physiological role is not yet clear. +Q9QYY9 ADH4_MOUSE Alcohol dehydrogenase 4 (EC 1.1.1.1) (ADH2) (Alcohol dehydrogenase class II) (Alcohol dehydrogenase II) 377 40,211 Beta strand (20); Binding site (4); Chain (1); Helix (19); Metal binding (7); Mutagenesis (3); Nucleotide binding (3); Sequence conflict (2); Turn (3) FUNCTION: Involved in the reduction of benzoquinones. {ECO:0000269|PubMed:10514444}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Dimer. {ECO:0000269|PubMed:10970744}. TISSUE SPECIFICITY: Liver specific. {ECO:0000269|PubMed:10514444}. +Q64437 ADH7_MOUSE Alcohol dehydrogenase class 4 mu/sigma chain (EC 1.1.1.1) (ADH-C2) (Alcohol dehydrogenase 7) (Alcohol dehydrogenase class IV mu/sigma chain) (Gastric alcohol dehydrogenase) (Retinol dehydrogenase) 374 39,904 Binding site (3); Chain (1); Metal binding (7); Nucleotide binding (2); Sequence conflict (4) FUNCTION: Could function in retinol oxidation for the synthesis of retinoic acid, a hormone important for cellular differentiation. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Homodimer. TISSUE SPECIFICITY: High expression in the stomach mucosa. Lower expression in eye, thymus, skin and ovary. Very low expression in small intestine, liver and uterus. +Q9Z103 ADNP_MOUSE Activity-dependent neuroprotector homeobox protein (Activity-dependent neuroprotective protein) 1108 124,308 Chain (1); Compositional bias (1); Cross-link (35); DNA binding (1); Modified residue (18); Region (1); Zinc finger (9) FUNCTION: Potential transcription factor. May mediate some of the neuroprotective peptide VIP-associated effects involving normal growth and cancer proliferation. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. TISSUE SPECIFICITY: Expressed in the brain, with a higher expression in cerebellum and hippocampus. Weakly expressed in lung, kidney and intestine, and expressed at intermediate level in testis. +P28474 ADHX_MOUSE Alcohol dehydrogenase class-3 (EC 1.1.1.1) (Alcohol dehydrogenase 2) (Alcohol dehydrogenase 5) (Alcohol dehydrogenase B2) (ADH-B2) (Alcohol dehydrogenase class-III) (Glutathione-dependent formaldehyde dehydrogenase) (FALDH) (FDH) (GSH-FDH) (EC 1.1.1.-) (S-(hydroxymethyl)glutathione dehydrogenase) (EC 1.1.1.284) 374 39,548 Chain (1); Initiator methionine (1); Metal binding (7); Modified residue (6); Sequence conflict (6); Site (1) FUNCTION: Class-III ADH is remarkably ineffective in oxidizing ethanol, but it readily catalyzes the oxidation of long-chain primary alcohols and the oxidation of S-(hydroxymethyl) glutathione. {ECO:0000250|UniProtKB:P11766}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P11766}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:7738026}. +Q99KS6 ADPRM_MOUSE Manganese-dependent ADP-ribose/CDP-alcohol diphosphatase (EC 3.6.1.13) (EC 3.6.1.16) (EC 3.6.1.53) (ADPRibase-Mn) (CDP-choline phosphohydrolase) 340 38,948 Alternative sequence (2); Chain (1); Metal binding (8); Modified residue (1); Sequence conflict (1) FUNCTION: Hydrolyzes ADP-ribose, IDP-ribose, CDP-glycerol, CDP-choline and CDP-ethanolamine, but not other non-reducing ADP-sugars or CDP-glucose. May be involved in immune cell signaling as suggested by the second-messenger role of ADP-ribose, which activates TRPM2 as a mediator of oxidative/nitrosative stress (By similarity). {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. +P51830 ADCY9_MOUSE Adenylate cyclase type 9 (EC 4.6.1.1) (ATP pyrophosphate-lyase 9) (Adenylate cyclase type IX) (Adenylyl cyclase 9) (AC9) (Adenylyl cyclase type 10) (ACTP10) 1353 150,954 Binding site (3); Chain (1); Glycosylation (3); Metal binding (5); Modified residue (10); Nucleotide binding (4); Sequence conflict (3); Topological domain (13); Transmembrane (12) TRANSMEM 118 138 Helical. {ECO:0000255}.; TRANSMEM 142 162 Helical. {ECO:0000255}.; TRANSMEM 172 192 Helical. {ECO:0000255}.; TRANSMEM 216 235 Helical. {ECO:0000255}.; TRANSMEM 242 259 Helical. {ECO:0000255}.; TRANSMEM 281 301 Helical. {ECO:0000255}.; TRANSMEM 787 807 Helical. {ECO:0000255}.; TRANSMEM 819 839 Helical. {ECO:0000255}.; TRANSMEM 868 888 Helical. {ECO:0000255}.; TRANSMEM 892 912 Helical. {ECO:0000255}.; TRANSMEM 921 941 Helical. {ECO:0000255}.; TRANSMEM 976 996 Helical. {ECO:0000255}. TOPO_DOM 1 117 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 139 141 Extracellular. {ECO:0000255}.; TOPO_DOM 163 171 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 193 215 Extracellular. {ECO:0000255}.; TOPO_DOM 236 241 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 260 280 Extracellular. {ECO:0000255}.; TOPO_DOM 302 786 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 808 818 Extracellular. {ECO:0000255}.; TOPO_DOM 840 867 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 889 891 Extracellular. {ECO:0000255}.; TOPO_DOM 913 920 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 942 975 Extracellular. {ECO:0000255}.; TOPO_DOM 997 1353 Cytoplasmic. {ECO:0000255}. FUNCTION: Adenylyl cyclase that catalyzes the formation of the signaling molecule cAMP in response to activation of G protein-coupled receptors. Contributes to signaling cascades activated by CRH (corticotropin-releasing factor), corticosteroids and by beta-adrenergic receptors. {ECO:0000250|UniProtKB:O60503, ECO:0000269|PubMed:8662814}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8662814}; Multi-pass membrane protein {ECO:0000305}. DOMAIN: The protein contains two modules with six transmembrane helices each; both are required for catalytic activity. Isolated N-terminal or C-terminal guanylate cyclase domains have no catalytic activity, but when they are brought together, enzyme activity is restored. The active site is at the interface of the two domains. Both contribute substrate-binding residues, but the catalytic metal ions are bound exclusively via the N-terminal guanylate cyclase domain. {ECO:0000250|UniProtKB:P26769}. TISSUE SPECIFICITY: Detected in brain, spleen, lung, liver and testis (at protein level). Detected in brain, especially in hippocampus, cerebellum and neocortex. Found in decreasing order in skeletal muscle, heart, adrenal gland, ovary and brain; and to a lesser extent, in kidney, liver, testis, lung, thymus and spleen. {ECO:0000269|PubMed:8662814}. +O54826 AF10_MOUSE Protein AF-10 1068 113,029 Chain (1); Compositional bias (2); Cross-link (1); Modified residue (7); Region (2); Sequence conflict (7); Zinc finger (3) FUNCTION: Probably involved in transcriptional regulation. Binds to cruciform DNA (By similarity). In cells, binding to unmodified histone H3 regulates DOT1L functions including histone H3 'Lys-79' dimethylation (H3K79me2) and gene activation (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P55197}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Self-associates. Interacts with FSTL3; the interaction enhances MLLT10 in vitro transcriptional activity and self-association. Interacts with YEATS4. Interacts with SS18. Interacts with DOT1L (By similarity). Interacts with histone H3; interaction is necessary for MLLT10 binding to nucleosomes; interaction is inhibited by histone H3 'Lys-27' methylations (H3K27me1, H3K27me2 and H3K27me3) amd acetylation; interaction stabilizes association of MLLT10 at chromatin; interaction is essential for histone H3 'Lys-79' dimethylation (H3K79me2) (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P55197}. +Q920A7 AFG31_MOUSE AFG3-like protein 1 (EC 3.4.24.-) 789 87,047 Active site (1); Alternative sequence (2); Chain (1); Erroneous initiation (1); Frameshift (1); Metal binding (3); Mutagenesis (1); Nucleotide binding (1); Transit peptide (1); Transmembrane (2) TRANSMEM 139 158 Helical. {ECO:0000255}.; TRANSMEM 246 264 Helical. {ECO:0000255}. FUNCTION: Putative ATP-dependent protease. Required for the maturation of paraplegin (SPG7) after its cleavage by mitochondrial-processing peptidase (MPP), converting it into a proteolytically active mature form. {ECO:0000269|PubMed:19656850}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:19656850}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Homooligomer (PubMed:17101804). Forms heterooligomers with SPG7 and AFG3L2 (PubMed:17101804, PubMed:19656850). Interacts with SPG7 and AFG3L2 (PubMed:19656850). {ECO:0000269|PubMed:17101804, ECO:0000269|PubMed:19656850}. +Q8CGM1 AGRB2_MOUSE Adhesion G protein-coupled receptor B2 (Brain-specific angiogenesis inhibitor 2) 1561 169,863 Alternative sequence (2); Chain (1); Compositional bias (6); Disulfide bond (16); Domain (5); Glycosylation (8); Modified residue (1); Sequence conflict (10); Signal peptide (1); Site (1); Topological domain (8); Transmembrane (7) TRANSMEM 931 951 Helical; Name=1. {ECO:0000255}.; TRANSMEM 960 980 Helical; Name=2. {ECO:0000255}.; TRANSMEM 989 1009 Helical; Name=3. {ECO:0000255}.; TRANSMEM 1031 1051 Helical; Name=4. {ECO:0000255}.; TRANSMEM 1073 1093 Helical; Name=5. {ECO:0000255}.; TRANSMEM 1116 1136 Helical; Name=6. {ECO:0000255}.; TRANSMEM 1148 1168 Helical; Name=7. {ECO:0000255}. TOPO_DOM 21 930 Extracellular. {ECO:0000305}.; TOPO_DOM 952 959 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 981 988 Extracellular. {ECO:0000305}.; TOPO_DOM 1010 1030 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1052 1072 Extracellular. {ECO:0000305}.; TOPO_DOM 1094 1115 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1137 1147 Extracellular. {ECO:0000305}.; TOPO_DOM 1169 1561 Cytoplasmic. {ECO:0000305}. FUNCTION: Orphan G-protein coupled receptor involved in cell adhesion and probably in cell-cell interactions. Activates NFAT-signaling pathway, a transcription factor, via the G-protein GNAZ. Involved in angiogenesis inhibition (PubMed:12218411). {ECO:0000250|UniProtKB:O60241, ECO:0000269|PubMed:12218411}. PTM: Glycosylated. {ECO:0000250|UniProtKB:O60241}.; PTM: Proteolytic processes at the GPS domain; this cleavage modulates receptor activity. Additionally, furin is involved in the cleavage at another site, in the middle of the extracellular domain, generating a soluble fragment. {ECO:0000250|UniProtKB:O60241}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O60241}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Heterodimer of 2 chains generated by proteolytic processing; the large extracellular N-terminal fragment and the membrane-bound C-terminal fragment predominantly remain associated and non-covalently linked. Interacts with GABPB2 (PubMed:16412436). Interacts (via carboxy-terminus) with TAX1BP3. Interacts with GNAZ (By similarity). Interacts with SH3GL2 (PubMed:28891236). {ECO:0000250|UniProtKB:O60241, ECO:0000269|PubMed:16412436, ECO:0000269|PubMed:28891236}. TISSUE SPECIFICITY: Specifically expressed in the brain. The peak level in the brain is observed 10 days after birth. {ECO:0000269|PubMed:12218411}. +O54931 AKAP2_MOUSE A-kinase anchor protein 2 (AKAP-2) (AKAP expressed in kidney and lung) (AKAP-KL) (Protein kinase A-anchoring protein 2) (PRKA2) 893 98,579 Alternative sequence (4); Chain (1); Coiled coil (2); Compositional bias (1); Cross-link (2); Frameshift (2); Modified residue (12); Mutagenesis (2); Region (1); Sequence conflict (9) FUNCTION: Binds to regulatory subunit (RII) of protein kinase A. May be involved in establishing polarity in signaling systems or in integrating PKA-RII isoforms with downstream effectors to capture, amplify and focus diffuse, trans-cellular signals carried by cAMP. DOMAIN: The RII-alpha binding site, predicted to form an amphipathic helix, could participate in protein-protein interactions with a complementary surface on the R-subunit dimer. TISSUE SPECIFICITY: Highly expressed in lung and weakly in thymus and cerebellum. Little or no expression in liver, heart and cerebral cortex. All isoforms are expressed in lung, but KL2A and KL2B isoforms are the principal isoforms in cerebellum. +P02716 ACHD_MOUSE Acetylcholine receptor subunit delta 520 59,143 Chain (1); Disulfide bond (1); Glycosylation (3); Modified residue (1); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (4) TRANSMEM 249 273 Helical.; TRANSMEM 281 299 Helical.; TRANSMEM 315 336 Helical.; TRANSMEM 475 493 Helical. TOPO_DOM 25 248 Extracellular.; TOPO_DOM 337 474 Cytoplasmic. FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. SUBUNIT: Pentamer of two alpha chains, and one each of the beta, delta, and gamma (in immature muscle) or epsilon (in mature muscle) chains. The muscle heteropentamer composed of alpha-1, beta-1, delta, epsilon subunits interacts with the alpha-conotoxin ImII (By similarity). {ECO:0000250|UniProtKB:Q07001}. +Q32Q92 ACOT6_MOUSE Acyl-coenzyme A thioesterase 6 (Acyl-CoA thioesterase 6) (EC 3.1.2.-) 419 46,769 Active site (3); Alternative sequence (2); Chain (1); Erroneous initiation (1); Frameshift (1); Motif (1); Sequence caution (1) FUNCTION: Acyl-CoA thioesterase that catalyzes the hydrolysis of phytanoyl-CoA and pristanoyl-CoA to free fatty acids and coenzyme A (CoASH). {ECO:0000269|PubMed:17613526}. SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:17613526}. TISSUE SPECIFICITY: Highly expressed in white adipose tissue. Detected at lower levels in kidney, liver, brown adipose tissue and brain. {ECO:0000269|PubMed:17613526}. +Q99NB1 ACS2L_MOUSE Acetyl-coenzyme A synthetase 2-like, mitochondrial (EC 6.2.1.1) (Acetate--CoA ligase 2) (Acetyl-CoA synthetase 2) (AceCS2) (Acyl-CoA synthetase short-chain family member 1) 682 74,623 Binding site (5); Chain (1); Erroneous initiation (1); Modified residue (2); Nucleotide binding (2); Region (1); Sequence conflict (1); Transit peptide (1) FUNCTION: Important for maintaining normal body temperature during fasting and for energy homeostasis. Essential for energy expenditure under ketogenic conditions. Converts acetate to acetyl-CoA so that it can be used for oxidation through the tricarboxylic cycle to produce ATP and CO(2). {ECO:0000269|PubMed:11150295, ECO:0000269|PubMed:16790548, ECO:0000269|PubMed:19187775}. PTM: Reversibly acetylated at Lys-635. The acetyl-CoA synthase activity is inhibited by acetylation and activated by deacetylation. {ECO:0000269|PubMed:16790548}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:11150295}. SUBUNIT: Interacts with SIRT3. {ECO:0000269|PubMed:16790548}. TISSUE SPECIFICITY: Highly expressed in heart, testis, kidney, skeletal muscle, lung and spleen. Detected at low levels in brain. +Q91WC3 ACSL6_MOUSE Long-chain-fatty-acid--CoA ligase 6 (EC 6.2.1.3) (Long-chain acyl-CoA synthetase 6) (LACS 6) 697 78,017 Alternative sequence (1); Chain (1); Sequence conflict (2); Topological domain (1); Transmembrane (1) TRANSMEM 25 45 Helical; Signal-anchor for type III membrane protein. {ECO:0000255}. TOPO_DOM 46 697 Cytoplasmic. {ECO:0000255}. FUNCTION: Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Plays an important role in fatty acid metabolism in brain and the acyl-CoAs produced may be utilized exclusively for the synthesis of the brain lipid (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Peroxisome membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Microsome membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. +Q8K0L3 ACSM2_MOUSE Acyl-coenzyme A synthetase ACSM2, mitochondrial (EC 6.2.1.2) (Acyl-CoA synthetase medium-chain family member 2) (Butyrate--CoA ligase 2) (Butyryl-coenzyme A synthetase 2) (Middle-chain acyl-CoA synthetase 2) 575 64,269 Alternative sequence (2); Binding site (8); Chain (1); Nucleotide binding (2); Region (2); Sequence conflict (1); Transit peptide (1) FUNCTION: Has medium-chain fatty acid:CoA ligase activity with broad substrate specificity (in vitro). Acts on acids from C(4) to C(11) and on the corresponding 3-hydroxy- and 2,3- or 3,4-unsaturated acids (in vitro) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. +Q14DH7 ACSS3_MOUSE Acyl-CoA synthetase short-chain family member 3, mitochondrial (EC 6.2.1.1) 682 74,518 Alternative sequence (2); Binding site (4); Chain (1); Modified residue (2); Nucleotide binding (2); Region (1); Sequence conflict (1); Transit peptide (1) FUNCTION: Activates acetate so that it can be used for lipid synthesis or for energy generation. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}. +Q8R2V5 ADAP2_MOUSE Arf-GAP with dual PH domain-containing protein 2 (Centaurin-alpha-2) (Cnt-a2) 381 43,989 Chain (1); Domain (3); Zinc finger (1) FUNCTION: GTPase-activating protein for the ADP ribosylation factor family (Potential). Binds phosphatidylinositol 3,4,5-trisphosphate (PtdInsP3) and inositol 1,3,4,5-tetrakisphosphate (InsP4). Possesses a stoichiometry of two binding sites for InsP4 with identical affinity (By similarity). {ECO:0000250, ECO:0000305}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Constitutively associated with the plasma membrane. Excluded from the nucleus (By similarity). {ECO:0000250}. +P00329 ADH1_MOUSE Alcohol dehydrogenase 1 (EC 1.1.1.1) (ADH-A2) (Alcohol dehydrogenase A subunit) 375 39,771 Binding site (3); Chain (1); Initiator methionine (1); Metal binding (7); Modified residue (3); Nucleotide binding (2) SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Dimer of identical or non-identical chains of three types (A, B, C), which are coded by 3 separate genes at different loci. TISSUE SPECIFICITY: Expressed at high levels in the liver, small intestine and eye, at moderate levels in kidney, ovary and uterus, and at low levels in the spinal cord, thymus, heart, stomach mucosa, skin and testis. {ECO:0000269|PubMed:7738026}. +Q5SUE7 ADAD1_MOUSE Adenosine deaminase domain-containing protein 1 (Testis nuclear RNA-binding protein) 619 67,840 Alternative sequence (3); Chain (1); Domain (2); Erroneous gene model prediction (3); Sequence conflict (2) FUNCTION: Plays a role in spermatogenesis. Binds to RNA but not to DNA. {ECO:0000269|PubMed:15649457}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:7543294}. TISSUE SPECIFICITY: Testis-specific. Detected in round spermatid cells from stage II-XI (at protein level). Expressed in germ cells from mid-pachytene spermatocytes to mid-round spermatids. {ECO:0000269|PubMed:7543294}. +Q8CHC8 ADNP2_MOUSE Activity-dependent neuroprotector homeobox protein 2 (ADNP homeobox protein 2) (Zinc finger protein 508) 1165 126,768 Chain (1); Cross-link (3); DNA binding (1); Erroneous initiation (3); Zinc finger (9) FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +P25962 ADRB3_MOUSE Beta-3 adrenergic receptor (Beta-3 adrenoreceptor) (Beta-3 adrenoceptor) 400 43,006 Alternative sequence (1); Binding site (2); Chain (1); Disulfide bond (2); Glycosylation (2); Lipidation (1); Region (3); Topological domain (8); Transmembrane (7) TRANSMEM 37 60 Helical; Name=1. {ECO:0000250}.; TRANSMEM 70 88 Helical; Name=2. {ECO:0000250}.; TRANSMEM 109 130 Helical; Name=3. {ECO:0000250}.; TRANSMEM 153 175 Helical; Name=4. {ECO:0000250}.; TRANSMEM 201 222 Helical; Name=5. {ECO:0000250}.; TRANSMEM 290 311 Helical; Name=6. {ECO:0000250}.; TRANSMEM 324 344 Helical; Name=7. {ECO:0000250}. TOPO_DOM 1 36 Extracellular. {ECO:0000250}.; TOPO_DOM 61 69 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 89 108 Extracellular. {ECO:0000250}.; TOPO_DOM 131 152 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 176 200 Extracellular. {ECO:0000250}.; TOPO_DOM 223 289 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 312 323 Extracellular. {ECO:0000250}.; TOPO_DOM 345 400 Cytoplasmic. {ECO:0000250}. FUNCTION: Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. Beta-3 is involved in the regulation of lipolysis and thermogenesis. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBUNIT: Interacts with ARRDC3. {ECO:0000250|UniProtKB:P13945}. TISSUE SPECIFICITY: White and brown adipose tissues, and digestive tract. Isoform B highest in brain. +Q8JZQ2 AFG32_MOUSE AFG3-like protein 2 (EC 3.4.24.-) 802 89,519 Active site (1); Chain (1); Metal binding (3); Modified residue (1); Mutagenesis (1); Natural variant (1); Nucleotide binding (1); Propeptide (1); Transit peptide (1); Transmembrane (2) TRANSMEM 142 162 Helical. {ECO:0000255}.; TRANSMEM 250 270 Helical. {ECO:0000255}. FUNCTION: ATP-dependent protease which is essential for axonal and neuron development (PubMed:18337413, PubMed:27642048). In neurons, mediates degradation of SMDT1/EMRE before its assembly with the uniporter complex, limiting the availability of SMDT1/EMRE for MCU assembly and promoting efficient assembly of gatekeeper subunits with MCU (By similarity). Required for the maturation of paraplegin (SPG7) after its cleavage by mitochondrial-processing peptidase (MPP), converting it into a proteolytically active mature form. {ECO:0000250|UniProtKB:Q9Y4W6, ECO:0000269|PubMed:18337413, ECO:0000269|PubMed:27642048}. PTM: Upon import into the mitochondrion, the N-terminal transit peptide is cleaved to generate an intermediate form which undergoes autocatalytic proteolytic processing to generate the proteolytically active mature form. {ECO:0000269|PubMed:19656850}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:19656850}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Homooligomer (PubMed:17101804). Forms heterooligomers with SPG7 and AFG3L1 (PubMed:17101804, PubMed:19656850). Interacts with SPG7; the interaction is required for the efficient assembly of mitochondrial complex I (PubMed:22563492, PubMed:19656850). Interacts with AFG3L1 (PubMed:19656850). Interacts with MAIP1 (PubMed:27642048). {ECO:0000250|UniProtKB:Q9Y4W6, ECO:0000269|PubMed:17101804, ECO:0000269|PubMed:19656850, ECO:0000269|PubMed:22563492, ECO:0000269|PubMed:27642048}. TISSUE SPECIFICITY: Highly expressed in the cerebellar Purkinje cells. {ECO:0000269|PubMed:20208537}. DISEASE: Note=Defects in Afg3l2 are the cause of the paralyze (par) phenotype, a spontaneous mutant strain. Par mice have a normal appearance and fertility but are significantly smaller than their littermates at 1 week of age and display a rapidly progressive loss of motor function in all limbs by 12-14 days. As the disease progresses, they lose the ability to support their own weight or turn themselves over when placed on their back and exhibit a typical posture with over extension of all limbs and uncoordinated movements. They rarely survive beyond 16 days of age, when they are completely paralyzed. {ECO:0000269|PubMed:18337413}. +Q8R534 ADM1B_MOUSE Disintegrin and metalloproteinase domain-containing protein 1b (ADAM 1b) (EC 3.4.24.-) (Fertilin subunit alpha-b) 806 89,369 Active site (1); Chain (1); Compositional bias (1); Disulfide bond (7); Domain (3); Glycosylation (6); Metal binding (3); Propeptide (1); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 705 725 Helical. {ECO:0000255}. TOPO_DOM ? 704 Extracellular. {ECO:0000255}.; TOPO_DOM 726 806 Cytoplasmic. {ECO:0000255}. FUNCTION: May play a role in spermatogenesis and sperm maturation. {ECO:0000303|PubMed:12095680}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Heterodimer with ADAM2/fertilin subunit beta. TISSUE SPECIFICITY: Testis. {ECO:0000269|PubMed:12095680}. +P41216 ACSL1_MOUSE Long-chain-fatty-acid--CoA ligase 1 (EC 6.2.1.3) (Long-chain acyl-CoA synthetase 1) (LACS 1) 699 77,951 Chain (1); Glycosylation (1); Modified residue (9); Sequence conflict (1); Topological domain (1); Transmembrane (1) TRANSMEM 25 45 Helical; Signal-anchor for type III membrane protein. {ECO:0000255}. TOPO_DOM 46 699 Cytoplasmic. {ECO:0000255}. FUNCTION: Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses oleate, arachidonate, eicosapentaenoate and docosahexaenoate as substrates (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Peroxisome membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Microsome membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. +Q9QYB8 ADDB_MOUSE Beta-adducin (Add97) (Erythrocyte adducin subunit beta) 725 80,642 Alternative sequence (3); Chain (1); Modified residue (28); Region (2); Sequence conflict (8) FUNCTION: Membrane-cytoskeleton-associated protein that promotes the assembly of the spectrin-actin network. Binds to the erythrocyte membrane receptor SLC2A1/GLUT1 and may therefore provide a link between the spectrin cytoskeleton to the plasma membrane. Binds to calmodulin. Calmodulin binds preferentially to the beta subunit (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. SUBUNIT: Found in a complex with ADD2, DMTN and SLC2A1. Interacts with SLC2A1 (By similarity). Heterodimer of an alpha and a beta subunit. {ECO:0000250}. DOMAIN: Each subunit is comprised of three regions: a NH2-terminal protease-resistant globular head region, a short connecting subdomain, and a protease-sensitive tail region. +Q99JW2 ACY1_MOUSE Aminoacylase-1 (ACY-1) (EC 3.5.1.14) (N-acyl-L-amino-acid amidohydrolase) 408 45,781 Active site (2); Chain (1); Metal binding (6); Sequence conflict (8) FUNCTION: Involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homodimer (By similarity). Interacts with SPHK1. {ECO:0000250, ECO:0000269|PubMed:15196915}. +Q640N1 AEBP1_MOUSE Adipocyte enhancer-binding protein 1 (AE-binding protein 1) (Aortic carboxypeptidase-like protein) 1128 128,365 Alternative sequence (1); Chain (1); Compositional bias (3); Domain (1); Frameshift (1); Glycosylation (1); Mutagenesis (2); Region (5); Sequence conflict (24); Signal peptide (1) FUNCTION: Isoform 1: As a positive regulator of collagen fibrillogenesis, it is probably involved in the organization and remodeling of the extracellualr matrix. {ECO:0000250|UniProtKB:Q8IUX7}.; FUNCTION: Isoform 2: May positively regulate MAP-kinase activity in adipocytes, leading to enhanced adipocyte proliferation and reduced adipocyte differentiation. May also positively regulate NF-kappa-B activity in macrophages by promoting the phosphorylation and subsequent degradation of I-kappa-B-alpha (NFKBIA), leading to enhanced macrophage inflammatory responsiveness. Can act as a transcriptional repressor. {ECO:0000269|PubMed:10406805, ECO:0000269|PubMed:11152475, ECO:0000269|PubMed:11438679, ECO:0000269|PubMed:14729459, ECO:0000269|PubMed:16307171, ECO:0000269|PubMed:16461908, ECO:0000269|PubMed:16538615, ECO:0000269|PubMed:17202411, ECO:0000269|PubMed:7477299}. PTM: Phosphorylated by MAPK1 in vitro. {ECO:0000269|PubMed:15654748}. SUBCELLULAR LOCATION: Isoform 1: Secreted {ECO:0000269|PubMed:11438679, ECO:0000269|PubMed:15927179}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm {ECO:0000269|PubMed:17202411, ECO:0000269|PubMed:9624159}. Nucleus {ECO:0000269|PubMed:17202411}. SUBUNIT: Isoform 1: Interacts with different types of collagen, including collagens I, III, and V (By similarity). Isoform 2: Interacts with GNG5, NFKBIA, MAPK1, MAPK3 and PTEN. Interaction with MAPK1 may stimulate DNA-binding. May interact with calmodulin. Binds to DNA in vitro. {ECO:0000250|UniProtKB:Q8IUX7, ECO:0000269|PubMed:10406805, ECO:0000269|PubMed:11152475, ECO:0000269|PubMed:16538615, ECO:0000269|PubMed:17202411, ECO:0000269|PubMed:17299101}. DOMAIN: Isoform 1: The F5/8 type C domain binds to different types of collagen, including collagens I, III, and V. {ECO:0000250|UniProtKB:Q8IUX7}. TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in adipose tissue, brain, heart, kidney, liver, lung, skeletal muscle, small intestine, spleen and testis. Isoform 2 is expressed in macrophages. Expressed in aorta, preadipocytes, adipocyte tissue, brain, heart, liver, lung, skeletal muscle, skin and spleen (at protein level). {ECO:0000269|PubMed:11438679, ECO:0000269|PubMed:11738825, ECO:0000269|PubMed:9624159}. +P46660 AINX_MOUSE Alpha-internexin (Alpha-Inx) (66 kDa neurofilament protein) (NF-66) (Neurofilament-66) 501 55,383 Chain (1); Compositional bias (1); Domain (1); Modified residue (5); Region (7); Sequence conflict (21) FUNCTION: Class-IV neuronal intermediate filament that is able to self-assemble. It is involved in the morphogenesis of neurons. It may form an independent structural network without the involvement of other neurofilaments or it may cooperate with NF-L to form the filamentous backbone to which NF-M and NF-H attach to form the cross-bridges (By similarity). {ECO:0000250}. PTM: O-glycosylated. {ECO:0000269|PubMed:16452088}. +Q8BXF8 ACTT3_MOUSE Actin-related protein T3 (ARP-T3) (Actin-related protein M1) 369 40,443 Chain (1); Erroneous initiation (1); Sequence conflict (2) SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:18692047}. Nucleus {ECO:0000269|PubMed:18692047}. Note=The localization changes from the peripheral region to inside the nucleus during differentiation from round to elongated spermatid. SUBUNIT: Interacts with PFN3. {ECO:0000269|PubMed:18692047}. TISSUE SPECIFICITY: Testis specific (at protein level). Expressed specifically in haploid germ cells. +Q3UNX5 ACSM3_MOUSE Acyl-coenzyme A synthetase ACSM3, mitochondrial (EC 6.2.1.2) (Acyl-CoA synthetase medium-chain family member 3) (Butyrate--CoA ligase 3) (Butyryl-coenzyme A synthetase 3) (Middle-chain acyl-CoA synthetase 3) (Protein SA homolog) 580 65,623 Alternative sequence (1); Binding site (3); Chain (1); Erroneous initiation (4); Frameshift (1); Modified residue (3); Nucleotide binding (2); Sequence conflict (1); Transit peptide (1) FUNCTION: Has medium-chain fatty acid:CoA ligase activity with broad substrate specificity (in vitro). Acts on acids from C(4) to C(11) and on the corresponding 3-hydroxy- and 2,3- or 3,4-unsaturated acids (in vitro). {ECO:0000269|PubMed:11470804}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:11470804, ECO:0000269|PubMed:15525578}. TISSUE SPECIFICITY: Detected in kidney (at protein level). Detected in kidney proximal tubules and in liver. Detected at low levels in testis, stomach, heart and lung. {ECO:0000269|PubMed:11470804, ECO:0000269|PubMed:15525578, ECO:0000269|PubMed:9449642, ECO:0000269|PubMed:9507200}. +Q9QYB5 ADDG_MOUSE Gamma-adducin (Adducin-like protein 70) 706 78,777 Alternative sequence (1); Chain (1); Cross-link (1); Initiator methionine (1); Modified residue (17); Region (1); Sequence conflict (3) FUNCTION: Membrane-cytoskeleton-associated protein that promotes the assembly of the spectrin-actin network. Plays a role in actin filament capping. Binds to calmodulin. {ECO:0000250|UniProtKB:Q9UEY8}. PTM: Sumoylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell membrane; Peripheral membrane protein; Cytoplasmic side. SUBUNIT: Heterodimer of an alpha and a gamma subunit. DOMAIN: Comprised of three regions: a N-terminal protease-resistant globular head region, a short connecting subdomain, and a protease-sensitive tail region. +P97718 ADA1A_MOUSE Alpha-1A adrenergic receptor (Alpha-1A adrenoreceptor) (Alpha-1A adrenoceptor) (Alpha-1C adrenergic receptor) 466 51,744 Chain (1); Disulfide bond (1); Erroneous initiation (1); Glycosylation (3); Lipidation (1); Modified residue (1); Motif (1); Sequence conflict (2); Topological domain (8); Transmembrane (7) TRANSMEM 28 51 Helical; Name=1. {ECO:0000250}.; TRANSMEM 65 88 Helical; Name=2. {ECO:0000250}.; TRANSMEM 100 122 Helical; Name=3. {ECO:0000250}.; TRANSMEM 144 167 Helical; Name=4. {ECO:0000250}.; TRANSMEM 182 205 Helical; Name=5. {ECO:0000250}.; TRANSMEM 274 297 Helical; Name=6. {ECO:0000250}.; TRANSMEM 306 329 Helical; Name=7. {ECO:0000250}. TOPO_DOM 1 27 Extracellular. {ECO:0000250}.; TOPO_DOM 52 64 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 89 99 Extracellular. {ECO:0000250}.; TOPO_DOM 123 143 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 168 181 Extracellular. {ECO:0000250}.; TOPO_DOM 206 273 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 298 305 Extracellular. {ECO:0000250}.; TOPO_DOM 330 466 Cytoplasmic. {ECO:0000250}. FUNCTION: This alpha-adrenergic receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. Its effect is mediated by G(q) and G(11) proteins. Nuclear ADRA1A-ADRA1B heterooligomers regulate phenylephrine (PE)-stimulated ERK signaling in cardiac myocytes (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:22120526}; Multi-pass membrane protein {ECO:0000269|PubMed:22120526}. Cell membrane {ECO:0000250|UniProtKB:P35348}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:P35348}. Membrane, caveola {ECO:0000250|UniProtKB:P35348}. Note=Location at the nuclear membrane facilitates heterooligomerization and regulates ERK-mediated signaling in cardiac myocytes. Colocalizes with GNAQ, PLCB1 as well as LAP2 at the nuclear membrane of cardiac myocytes (By similarity). {ECO:0000250}. SUBUNIT: Homo- and heterooligomer. Heterooligomerizes with ADRA1B homooligomers in cardiac myocytes. Interacts with CAVIN4. {ECO:0000250|UniProtKB:P35348}. +Q9R1V6 ADA22_MOUSE Disintegrin and metalloproteinase domain-containing protein 22 (ADAM 22) 904 99,715 Alternative sequence (16); Chain (1); Compositional bias (1); Disulfide bond (20); Domain (3); Glycosylation (4); Modified residue (8); Mutagenesis (1); Propeptide (1); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 735 755 Helical. {ECO:0000255}. TOPO_DOM 24 734 Extracellular. {ECO:0000255}.; TOPO_DOM 756 857 Cytoplasmic. {ECO:0000255}. FUNCTION: Probable ligand for integrin in the brain. This is a non catalytic metalloprotease-like protein. Involved in regulation of cell adhesion and spreading and in inhibition of cell proliferation (By similarity). Neuronal receptor for LGI1. {ECO:0000250|UniProtKB:Q9P0K1, ECO:0000269|PubMed:16990550}. PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20089912}; Single-pass type I membrane protein {ECO:0000305}. Cell projection, axon {ECO:0000269|PubMed:20089912}. SUBUNIT: Interacts with LGI1 (PubMed:18974846, PubMed:20089912). Can bind to LGI4(PubMed:18974846). Interacts with KCNA2, DLG2 and DLG4 (PubMed:20089912). {ECO:0000269|PubMed:16990550, ECO:0000269|PubMed:18974846, ECO:0000269|PubMed:20089912}. TISSUE SPECIFICITY: Detected in juxtaparanodal zones in the central nervous system and at nerve terminal plexuses of basket cells in the cerebellum (at protein level) (PubMed:20089912). Expressed at high levels in the brain. Strongly expressed in cerebellar granule cells and hippocampus. In spinal cord, expression is restricted to gray matter. {ECO:0000269|PubMed:15876356, ECO:0000269|PubMed:20089912}. +O89020 AFAM_MOUSE Afamin (Alpha-albumin) (Alpha-Alb) 608 69,379 Alternative sequence (3); Chain (1); Disulfide bond (16); Domain (3); Glycosylation (5); Region (1); Sequence caution (1); Sequence conflict (10); Signal peptide (1) FUNCTION: Functions as carrier for hydrophobic molecules in body fluids. Essential for the solubility and activity of lipidated Wnt family members, including WNT1, WNT2B, WNT3, WNT3A, WNT5A, WNT7A, WNT7B, WNT8, WNT9A, WNT9B, WNT10A and WNT10B. Binds vitamin E. May transport vitamin E in body fluids under conditions where the lipoprotein system is not sufficient. May be involved in the transport of vitamin E across the blood-brain barrier. {ECO:0000250|UniProtKB:P43652}. PTM: N-glycosylated; more than 90% of the glycans are sialylated. {ECO:0000250|UniProtKB:P43652}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P43652}. SUBUNIT: Forms a 1:1 complex with Wnt family members; interacts with WNT1, WNT2B, WNT3, WNT5A, WNT7A, WNT7B, WNT8, WNT9A, WNT9B, WNT10A and WNT10B (By similarity). Interacts with WNT3A (PubMed:26902720). {ECO:0000250|UniProtKB:P43652, ECO:0000269|PubMed:26902720}. DOMAIN: The second albumin domain forms a deep binding pocket that contains palmitoleic acid (in vitro). Palmitoleic acid is most likely not the physiological ligand. Instead, this pocket may accomodate the covalently bound lipid moiety of Wnt family members. {ECO:0000250|UniProtKB:P43652}. TISSUE SPECIFICITY: Detected in brain, especially on brain capillaries (at protein level). Expressed in isolated brain capillaries. {ECO:0000269|PubMed:19046407}. +P51881 ADT2_MOUSE ADP/ATP translocase 2 (ADP,ATP carrier protein 2) (Adenine nucleotide translocator 2) (ANT 2) (Solute carrier family 25 member 5) [Cleaved into: ADP/ATP translocase 2, N-terminally processed] 298 32,931 Binding site (4); Chain (2); Initiator methionine (1); Modified residue (22); Motif (1); Region (1); Repeat (3); Transmembrane (6) TRANSMEM 8 37 Helical; Name=1. {ECO:0000250|UniProtKB:P02722}.; TRANSMEM 75 99 Helical; Name=2. {ECO:0000250|UniProtKB:P02722}.; TRANSMEM 110 130 Helical; Name=3. {ECO:0000250|UniProtKB:P02722}.; TRANSMEM 179 199 Helical; Name=4. {ECO:0000250|UniProtKB:P02722}.; TRANSMEM 211 231 Helical; Name=5. {ECO:0000250|UniProtKB:P02722}.; TRANSMEM 274 291 Helical; Name=6. {ECO:0000250|UniProtKB:P02722}. FUNCTION: Catalyzes the exchange of cytoplasmic ADP with mitochondrial ATP across the mitochondrial inner membrane. As part of the mitotic spindle-associated MMXD complex it may play a role in chromosome segregation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SUBUNIT: Homodimer. Component of the MMXD complex, which includes CIAO1, ERCC2, CIAO2B, MMS19 and SLC25A5 (By similarity). {ECO:0000250}. DOMAIN: The transmembrane helices are not perpendicular to the plane of the membrane, but cross the membrane at an angle. Odd-numbered transmembrane helices exhibit a sharp kink, due to the presence of a conserved proline residue. {ECO:0000250|UniProtKB:P02722}. +Q9CYR6 AGM1_MOUSE Phosphoacetylglucosamine mutase (PAGM) (EC 5.4.2.3) (Acetylglucosamine phosphomutase) (N-acetylglucosamine-phosphate mutase) (Phosphoglucomutase-3) (PGM 3) 542 59,453 Active site (1); Beta strand (5); Binding site (1); Chain (1); Helix (2); Metal binding (4); Modified residue (3); Region (2) Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I): step 2/2. FUNCTION: Catalyzes the conversion of GlcNAc-6-P into GlcNAc-1-P during the synthesis of uridine diphosphate/UDP-GlcNAc, a sugar nucleotide critical to multiple glycosylation pathways including protein N- and O-glycosylation. {ECO:0000250|UniProtKB:O95394}. +Q923X1 AGRL4_MOUSE Adhesion G protein-coupled receptor L4 (EGF, latrophilin seven transmembrane domain-containing protein 1) 739 82,246 Chain (1); Disulfide bond (9); Domain (4); Glycosylation (8); Sequence conflict (2); Signal peptide (1); Site (1); Topological domain (8); Transmembrane (7) TRANSMEM 482 502 Helical; Name=1. {ECO:0000255}.; TRANSMEM 514 534 Helical; Name=2. {ECO:0000255}.; TRANSMEM 549 569 Helical; Name=3. {ECO:0000255}.; TRANSMEM 582 602 Helical; Name=4. {ECO:0000255}.; TRANSMEM 623 643 Helical; Name=5. {ECO:0000255}.; TRANSMEM 668 688 Helical; Name=6. {ECO:0000255}.; TRANSMEM 696 716 Helical; Name=7. {ECO:0000255}. TOPO_DOM 20 481 Extracellular. {ECO:0000305}.; TOPO_DOM 503 513 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 535 548 Extracellular. {ECO:0000305}.; TOPO_DOM 570 581 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 603 622 Extracellular. {ECO:0000305}.; TOPO_DOM 644 667 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 689 695 Extracellular. {ECO:0000305}.; TOPO_DOM 717 739 Cytoplasmic. {ECO:0000305}. FUNCTION: Endothelial orphan receptor that acts as a key regulator of angiogenesis. {ECO:0000250|UniProtKB:Q9HBW9, ECO:0000269|PubMed:23871637}. PTM: Glycosylated. {ECO:0000250|UniProtKB:Q9HBW9}.; PTM: Proteolytically cleaved into 2 subunits, an extracellular alpha subunit and a seven-transmembrane subunit. {ECO:0000250|UniProtKB:Q9ESC1}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23871637}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Heterodimer of 2 chains generated by proteolytic processing; the large extracellular N-terminal fragment and the membrane-bound C-terminal fragment predominantly remain associated and non-covalently linked. {ECO:0000250|UniProtKB:Q9ESC1}. DOMAIN: The transmembrane domain is not required for cleavage, but it is required for dimer formation. {ECO:0000250|UniProtKB:Q9ESC1}. +Q64362 AKTIP_MOUSE AKT-interacting protein (FT1) (Fused toes protein) 292 32,942 Chain (1); Modified residue (1) FUNCTION: Component of the FTS/Hook/FHIP complex (FHF complex). The FHF complex may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting complex (the HOPS complex). Regulates apoptosis by enhancing phosphorylation and activation of AKT1. Increases release of TNFSF6 via the AKT1/GSK3B/NFATC1 signaling cascade (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. SUBUNIT: Component of the FTS/Hook/FHIP complex (FHF complex), composed of AKTIP/FTS, FAM160A2, and one or more members of the Hook family of proteins HOOK1, HOOK2, and HOOK3. May interact directly with HOOK1, HOOK2 and HOOK3. The FHF complex associates with the homotypic vesicular sorting complex (the HOPS complex). Also interacts with AKT1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. Highest expression in kidney, testis and brain and lowest in spleen and liver. {ECO:0000269|PubMed:9383278}. DISEASE: Note=Defects in Aktip are a cause of embryonic death in homozygous animals. Death occurs at about 10 days of development. Symptoms include loss of left-right asymmetry, malformation of the developing brain and of the spinal cord, syndactyly and polydactyly. Heterozygous animals are characterized by polydactyly and thymic hyperplasia. {ECO:0000269|PubMed:7956835}. +A2A3V1 AK17B_MOUSE A-kinase anchor protein 17B (AKAP-17B) (Protein Talia) (Protein kinase A-anchoring protein 17B) (PRKA17B) (Splicing factor, arginine/serine-rich 17B) 959 111,066 Chain (1); Coiled coil (1); Compositional bias (3); Domain (1); Erroneous gene model prediction (1); Frameshift (1); Modified residue (2); Sequence conflict (1) FUNCTION: Splice factor regulating alternative splice site selection for certain mRNA precursors. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}. SUBUNIT: Monomer. Component of the spliceosome (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:17302988}. +Q9JLJ2 AL9A1_MOUSE 4-trimethylaminobutyraldehyde dehydrogenase (TMABADH) (EC 1.2.1.47) (Aldehyde dehydrogenase family 9 member A1) (EC 1.2.1.3) 494 53,515 Active site (2); Chain (1); Initiator methionine (1); Modified residue (8); Nucleotide binding (1) Amine and polyamine biosynthesis; carnitine biosynthesis. FUNCTION: Converts gamma-trimethylaminobutyraldehyde into gamma-butyrobetaine. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homotetramer. {ECO:0000250}. +Q3TZM9 ALG11_MOUSE GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase (EC 2.4.1.131) (Asparagine-linked glycosylation protein 11 homolog) (Glycolipid 2-alpha-mannosyltransferase) 492 55,270 Alternative sequence (2); Chain (1); Transmembrane (2) TRANSMEM 22 42 Helical. {ECO:0000255}.; TRANSMEM 234 254 Helical. {ECO:0000255}. FUNCTION: Mannosyltransferase involved in the last steps of the synthesis of Man5GlcNAc(2)-PP-dolichol core oligosaccharide on the cytoplasmic face of the endoplasmic reticulum. Catalyzes the addition of the 4th and 5th mannose residues to the dolichol-linked oligosaccharide chain (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +E9Q4F7 ANR11_MOUSE Ankyrin repeat domain-containing protein 11 2643 296,186 Chain (1); Compositional bias (4); Modified residue (17); Mutagenesis (1); Region (1); Repeat (4); Sequence conflict (1) FUNCTION: Chromatin regulator which modulates histone acetylation and gene expression in neural precursor cells (PubMed:25556659). May recruit histone deacetylases (HDACs) to the p160 coactivators/nuclear receptor complex to inhibit ligand-dependent transactivation (By similarity). Has a role in proliferation and development of cortical neural precursors (PubMed:25556659). May also regulate bone homeostasis (PubMed:17986521). {ECO:0000250|UniProtKB:Q6UB99, ECO:0000269|PubMed:17986521, ECO:0000269|PubMed:25556659}. PTM: Subject to proteasomal degradation which is probably essential to regulate its activity. {ECO:0000269|PubMed:25413698}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25413698}. Note=Localizes to chromatin during prometaphase (By similarity). {ECO:0000250|UniProtKB:Q6UB99}. SUBUNIT: Interacts with the PAS region of the p160 coactivators. {ECO:0000250|UniProtKB:Q6UB99}. +Q99PE2 ANRA2_MOUSE Ankyrin repeat family A protein 2 (RFXANK-like protein 2) 312 34,063 Chain (1); Repeat (5) FUNCTION: May regulate the interaction between the 3M complex and the histone deacetylases HDAC4 and HDAC5 (By similarity). May also regulate LRP2/megalin (PubMed:11095640). {ECO:0000250|UniProtKB:Q9H9E1, ECO:0000269|PubMed:11095640}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11095640}. Membrane {ECO:0000269|PubMed:11095640}; Peripheral membrane protein {ECO:0000269|PubMed:11095640}. SUBUNIT: Interacts (via ANK repeats) with CCDC8 (via PxLPxI/L motif); mediates the interaction with the 3M complex which is composed of CCDC8, CUL7 and OBSL1. Interacts (via ANK repeats) with HDAC4 (via PxLPxI/L motif). Interacts (via ANK repeats) with HDAC5 (via PxLPxI/L motif) (By similarity). Interacts (via ANK repeats) with LRP2/megalin (via PxLPxI/L motif) (PubMed:11095640). Interacts (via ANK repeats) with RFX7 (via PxLPxI/L motif) (By similarity). Interacts with AHRR (PubMed:17949687). Interacts with NEK6 (By similarity). {ECO:0000250|UniProtKB:Q9H9E1, ECO:0000269|PubMed:11095640, ECO:0000269|PubMed:17949687}. DOMAIN: The ankyrin repeats, mainly ANK 2, ANK 3 and ANK 4, mediate interaction with a wide array of PxLPxI/L motif-containing proteins including HDAC4 and LRP2. The PxLPxI/L motif of interactors can contain a Ser or a Thr residue in position 2, which phosphorylation prevents the interaction with ANKRA2. {ECO:0000250|UniProtKB:Q9H9E1}. +Q80V94 AP4E1_MOUSE AP-4 complex subunit epsilon-1 (AP-4 adaptor complex subunit epsilon) (Adaptor-related protein complex 4 subunit epsilon-1) (Epsilon subunit of AP-4) (Epsilon-adaptin) 1122 124,845 Chain (1); Frameshift (1); Modified residue (2); Region (1); Sequence conflict (4) FUNCTION: Component of the adaptor protein complex 4 (AP-4). Adaptor protein complexes are vesicle coat components involved both in vesicle formation and cargo selection. They control the vesicular transport of proteins in different trafficking pathways. AP-4 forms a non clathrin-associated coat on vesicles departing the trans-Golgi network (TGN) and may be involved in the targeting of proteins from the trans-Golgi network (TGN) to the endosomal-lysosomal system. It is also involved in protein sorting to the basolateral membrane in epithelial cells and the proper asymmetric localization of somatodendritic proteins in neurons. AP-4 is involved in the recognition and binding of tyrosine-based sorting signals found in the cytoplasmic part of cargos, but may also recognize other types of sorting signal. {ECO:0000250|UniProtKB:Q9UPM8}. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q9UPM8}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9UPM8}. SUBUNIT: Adaptor protein complex 4 (AP-4) is a heterotetramer composed of two large adaptins (epsilon-type subunit AP4E1 and beta-type subunit AP4B1), a medium adaptin (mu-type subunit AP4M1) and a small adaptin (sigma-type AP4S1). Interacts with TEPSIN (By similarity). Interacts with GRIA2; probably indirect it mediates the somatodendritic localization of GRIA2 in neurons (PubMed:18341993). {ECO:0000250|UniProtKB:Q9UPM8, ECO:0000269|PubMed:18341993}. +Q8R034 APC13_MOUSE Anaphase-promoting complex subunit 13 (APC13) (Cyclosome subunit 13) 74 8,346 Chain (1) Protein modification; protein ubiquitination. FUNCTION: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: The mammalian APC/C is composed at least of 14 distinct subunits ANAPC1, ANAPC2, CDC27/APC3, ANAPC4, ANAPC5, CDC16/APC6, ANAPC7, CDC23/APC8, ANAPC10, ANAPC11, CDC26/APC12, ANAPC13, ANAPC15 and ANAPC16 that assemble into a complex of at least 19 chains with a combined molecular mass of around 1.2 MDa; APC/C interacts with FZR1 and FBXO5. {ECO:0000250|UniProtKB:Q9BS18}. +P00688 AMYP_MOUSE Pancreatic alpha-amylase (PA) (EC 3.2.1.1) (1,4-alpha-D-glucan glucanohydrolase) 508 57,318 Active site (2); Binding site (3); Chain (1); Disulfide bond (5); Metal binding (4); Modified residue (1); Natural variant (12); Sequence conflict (6); Signal peptide (1); Site (1) SUBCELLULAR LOCATION: Secreted, extracellular space. SUBUNIT: Monomer. {ECO:0000250}. +O35608 ANGP2_MOUSE Angiopoietin-2 (ANG-2) 496 56,576 Chain (1); Coiled coil (1); Disulfide bond (3); Domain (1); Glycosylation (6); Metal binding (4); Sequence conflict (2); Signal peptide (1) FUNCTION: Binds to TEK/TIE2, competing for the ANGPT1 binding site, and modulating ANGPT1 signaling. Can induce tyrosine phosphorylation of TEK/TIE2 in the absence of ANGPT1. In the absence of angiogenic inducers, such as VEGF, ANGPT2-mediated loosening of cell-matrix contacts may induce endothelial cell apoptosis with consequent vascular regression. In concert with VEGF, it may facilitate endothelial cell migration and proliferation, thus serving as a permissive angiogenic signal (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Interacts with TEK/TIE2, competing for the same binding site as ANGPT1. {ECO:0000250}. DOMAIN: The Fibrinogen C-terminal domain mediates interaction with the TEK/TIE2 receptor. {ECO:0000250}. TISSUE SPECIFICITY: Expressed only at sites of vascular remodeling. +P16406 AMPE_MOUSE Glutamyl aminopeptidase (EAP) (EC 3.4.11.7) (Aminopeptidase A) (AP-A) (BP-1/6C3 antigen) (CD antigen CD249) 945 107,956 Active site (1); Binding site (2); Chain (1); Glycosylation (9); Metal binding (3); Region (1); Site (2); Topological domain (2); Transmembrane (1) TRANSMEM 19 39 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 18 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 40 945 Extracellular. {ECO:0000255}. FUNCTION: Regulates central hypertension through its calcium-modulated preference to cleave N-terminal acidic residues from peptides such as angiotensin II. {ECO:0000250|UniProtKB:Q07075}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q07075}; Single-pass type II membrane protein. SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250|UniProtKB:Q07075}. TISSUE SPECIFICITY: Early B-lineage cells and certain stromal cell of hemopoietic tissues. Also expressed by capillary endothelial cells, placenta, and epithelial cells of the intestine and proximal renal tubules. {ECO:0000269|PubMed:1689065}. +Q8BZ25 ANKK1_MOUSE Ankyrin repeat and protein kinase domain-containing protein 1 (EC 2.7.11.1) 745 82,480 Active site (1); Binding site (1); Chain (1); Domain (1); Nucleotide binding (1); Repeat (11) +G3X982 AOXC_MOUSE Aldehyde oxidase 3 (EC 1.2.3.1) (Aldehyde oxidase homolog 1) (Azaheterocycle hydroxylase 3) (EC 1.17.3.-) 1335 146,902 Active site (1); Beta strand (44); Binding site (8); Chain (1); Domain (2); Helix (50); Metal binding (8); Modified residue (1); Mutagenesis (4); Nucleotide binding (1); Sequence conflict (2); Turn (14) FUNCTION: Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide and phthalazine, as well as aldehydes, such as benzaldehyde, retinal and pyridoxal. Plays a key role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. Is probably involved in the regulation of reactive oxygen species homeostasis. May be a prominent source of superoxide generation via the one-electron reduction of molecular oxygen. Also may catalyze nitric oxide (NO) production via the reduction of nitrite to NO with NADH or aldehyde as electron donor. {ECO:0000269|PubMed:11562361, ECO:0000269|PubMed:18981221, ECO:0000269|PubMed:21705476, ECO:0000269|PubMed:23019336}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11562361, ECO:0000269|PubMed:15383531}. SUBUNIT: Homodimer. {ECO:0000269|PubMed:23019336}. TISSUE SPECIFICITY: Highly expressed in liver (at protein level). In liver, the expression is greater in males than females. {ECO:0000269|PubMed:11562361, ECO:0000269|PubMed:15383531, ECO:0000269|PubMed:18981221}. +A2ARS0 ANR63_MOUSE Ankyrin repeat domain-containing protein 63 390 41,068 Chain (1); Modified residue (2); Repeat (5) +Q3U3W5 ANM9_MOUSE Protein arginine N-methyltransferase 9 (Protein arginine N-methyltransferase 10) (EC 2.1.1.320) 846 94,220 Alternative sequence (2); Chain (1); Domain (2); Frameshift (1); Repeat (3); Sequence conflict (4) FUNCTION: Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA). Specifically mediates the symmetrical dimethylation of SF3B2. Involved in the regulation of alternative splicing of pre-mRNA. {ECO:0000250|UniProtKB:Q6P2P2}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6P2P2}. SUBUNIT: Found in a complex with PRMT9, SF3B2 and SF3B4. Interacts with SF3B2. {ECO:0000250|UniProtKB:Q6P2P2}. +Q00623 APOA1_MOUSE Apolipoprotein A-I (Apo-AI) (ApoA-I) (Apolipoprotein A1) [Cleaved into: Proapolipoprotein A-I (ProapoA-I); Truncated apolipoprotein A-I] 264 30,616 Beta strand (1); Chain (3); Helix (7); Mass spectrometry (5); Modified residue (4); Natural variant (1); Region (1); Repeat (10); Sequence conflict (8); Signal peptide (1); Turn (2) FUNCTION: Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility. PTM: Glycosylated. {ECO:0000250}.; PTM: Palmitoylated. {ECO:0000250}.; PTM: May be acylated.; PTM: Phosphorylation sites are present in the extracellular medium. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Interacts with APOA1BP and CLU. Component of a sperm activating protein complex (SPAP), consisting of APOA1, an immunoglobulin heavy chain, an immunoglobulin light chain and albumin. Interacts with NDRG1. Interacts with SCGB3A2. {ECO:0000250|UniProtKB:P02647}. TISSUE SPECIFICITY: Major protein of plasma HDL, also found in chylomicrons. +P34928 APOC1_MOUSE Apolipoprotein C-I (Apo-CI) (ApoC-I) (Apolipoprotein C1) [Cleaved into: Truncated apolipoprotein C-I] 88 9,696 Chain (2); Mass spectrometry (2); Signal peptide (1) FUNCTION: Inhibitor of lipoprotein binding to the low density lipoprotein (LDL) receptor, LDL receptor-related protein, and very low density lipoprotein (VLDL) receptor. Associates with high density lipoproteins (HDL) and the triacylglycerol-rich lipoproteins in the plasma and makes up about 10% of the protein of the VLDL and 2% of that of HDL. Appears to interfere directly with fatty acid uptake and is also the major plasma inhibitor of cholesteryl ester transfer protein (CETP). Modulates the interaction of APOE with beta-migrating VLDL and inhibits binding of beta-VLDL to the LDL receptor-related protein (By similarity). Binds free fatty acids and reduces their intracellular esterification. {ECO:0000250|UniProtKB:P02654, ECO:0000250|UniProtKB:P33047, ECO:0000269|PubMed:17339654}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02654}. TISSUE SPECIFICITY: Adult and fetal liver. {ECO:0000269|PubMed:8276416}. +Q03157 APLP1_MOUSE Amyloid-like protein 1 (APLP) (APLP-1) [Cleaved into: C30] 653 72,751 Chain (1); Compositional bias (3); Disulfide bond (6); Domain (2); Glycosylation (2); Motif (2); Mutagenesis (1); Peptide (1); Region (9); Sequence conflict (1); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 584 606 Helical. {ECO:0000255}. TOPO_DOM 38 583 Extracellular. {ECO:0000255}.; TOPO_DOM 607 653 Cytoplasmic. {ECO:0000255}. FUNCTION: May play a role in postsynaptic function. The C-terminal gamma-secretase processed fragment, ALID1, activates transcription activation through APBB1 (Fe65) binding. Couples to JIP signal transduction through C-terminal binding. May interact with cellular G-protein signaling pathways. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I.; FUNCTION: The gamma-CTF peptide, C30, is a potent enhancer of neuronal apoptosis. {ECO:0000250}. PTM: Proteolytically cleaved by caspases during neuronal apoptosis. Cleaved, in vitro, at Asp-623 by caspase-3 (By similarity). {ECO:0000250}.; PTM: N- and O-glycosylated. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: C30: Cytoplasm. Note=C-terminally processed in the Golgi complex. SUBUNIT: Monomer and homodimer. Heparin binding promotes homodimerization. Binds, via its C-terminus, to the PID domain of several cytoplasmic proteins, including APBB and APBA family members, MAPK8IP1 and Dab1 (By similarity). Binding to Dab1 inhibits its serine phosphorylation. Interacts with CPEB1. Interacts (via NPXY motif) with DAB2 (via PID domain); the interaction is impaired by tyrosine phosphorylation of the NPXY motif. Interacts (via NPXY motif) with DAB1. {ECO:0000250, ECO:0000269|PubMed:10460257, ECO:0000269|PubMed:11247302, ECO:0000269|PubMed:11517249, ECO:0000269|PubMed:12228233, ECO:0000269|PubMed:12826668, ECO:0000269|PubMed:16314516}. DOMAIN: The NPXY sequence motif found in many tyrosine-phosphorylated proteins is required for the specific binding of the PID domain. However, additional amino acids either N- or C-terminal to the NPXY motif are often required for complete interaction. The NPXY site is also involved in clathrin-mediated endocytosis. +Q91V80 APOF_MOUSE Apolipoprotein F (Apo-F) (Leukemia virus-inactivating factor) (LVIF) 315 34,359 Chain (1); Erroneous initiation (7); Propeptide (1); Signal peptide (1) FUNCTION: Minor apolipoprotein that associates with LDL. Inhibits cholesteryl ester transfer protein (CETP) activity and appears to be an important regulator of cholesterol transport. Also associates to a lesser degree with VLDL, Apo-AI and Apo-AII. {ECO:0000250|UniProtKB:Q13790}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q13790}. TISSUE SPECIFICITY: Liver. {ECO:0000269|PubMed:11836406}. +Q810N6 ANR45_MOUSE Ankyrin repeat domain-containing protein 45 248 27,734 Chain (1); Repeat (2) +Q8BVF7 APH1A_MOUSE Gamma-secretase subunit APH-1A (APH-1a) (Aph-1alpha) 265 28,986 Alternative sequence (2); Chain (1); Topological domain (8); Transmembrane (7) TRANSMEM 3 23 Helical; Name=1. {ECO:0000250|UniProtKB:Q96BI3}.; TRANSMEM 32 52 Helical; Name=2. {ECO:0000250|UniProtKB:Q96BI3}.; TRANSMEM 69 89 Helical; Name=3. {ECO:0000250|UniProtKB:Q96BI3}.; TRANSMEM 119 139 Helical; Name=4. {ECO:0000250|UniProtKB:Q96BI3}.; TRANSMEM 159 179 Helical; Name=5. {ECO:0000250|UniProtKB:Q96BI3}.; TRANSMEM 187 207 Helical; Name=6. {ECO:0000250|UniProtKB:Q96BI3}.; TRANSMEM 214 234 Helical; Name=7. {ECO:0000250|UniProtKB:Q96BI3}. TOPO_DOM 1 2 Lumenal. {ECO:0000250|UniProtKB:Q96BI3}.; TOPO_DOM 24 31 Cytoplasmic. {ECO:0000250|UniProtKB:Q96BI3}.; TOPO_DOM 53 68 Lumenal. {ECO:0000250|UniProtKB:Q96BI3}.; TOPO_DOM 90 118 Cytoplasmic. {ECO:0000250|UniProtKB:Q96BI3}.; TOPO_DOM 140 158 Lumenal. {ECO:0000250|UniProtKB:Q96BI3}.; TOPO_DOM 180 186 Cytoplasmic. {ECO:0000250|UniProtKB:Q96BI3}.; TOPO_DOM 208 213 Lumenal. {ECO:0000250|UniProtKB:Q96BI3}.; TOPO_DOM 235 265 Cytoplasmic. {ECO:0000250|UniProtKB:Q96BI3}. FUNCTION: Non-catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (amyloid-beta precursor protein) (PubMed:15634781, PubMed:19369254). Required for normal gamma-secretase assembly (PubMed:15634781, PubMed:19369254). The gamma-secretase complex plays a role in Notch and Wnt signaling cascades and regulation of downstream processes via its role in processing key regulatory proteins, and by regulating cytosolic CTNNB1 levels (Probable). {ECO:0000269|PubMed:15634781, ECO:0000269|PubMed:19369254, ECO:0000305}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q96BI3}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q96BI3}. Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:Q96BI3}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q96BI3}. Note=Predominantly located in the endoplasmic reticulum and in the cis-Golgi. {ECO:0000250|UniProtKB:Q96BI3}. SUBUNIT: The functional gamma-secretase complex is composed of at least four polypeptides: a presenilin homodimer (PSEN1 or PSEN2), nicastrin (NCSTN), APH1 (APH1A or APH1B) and PEN2. {ECO:0000269|PubMed:15634781, ECO:0000269|PubMed:19369254}. +Q8BSL7 ARF2_MOUSE ADP-ribosylation factor 2 181 20,746 Beta strand (6); Chain (1); Helix (8); Initiator methionine (1); Lipidation (1); Nucleotide binding (3); Sequence conflict (2); Turn (1) FUNCTION: GTP-binding protein that functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. Involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus. SUBCELLULAR LOCATION: Golgi apparatus. +O08739 AMPD3_MOUSE AMP deaminase 3 (EC 3.5.4.6) (AMP deaminase H-type) (AMP deaminase isoform E) (Heart-type AMPD) 766 88,652 Active site (1); Binding site (2); Chain (1); Metal binding (4); Modified residue (2); Region (2); Sequence conflict (2) Purine metabolism; IMP biosynthesis via salvage pathway; IMP from AMP: step 1/1. FUNCTION: AMP deaminase plays a critical role in energy metabolism. SUBUNIT: Homotetramer. {ECO:0000250}. TISSUE SPECIFICITY: Found in heart, lung brain, spleen, kidney and to a lesser extent in liver. +A2AS55 ANR16_MOUSE Ankyrin repeat domain-containing protein 16 361 39,776 Alternative sequence (2); Chain (1); Mutagenesis (3); Repeat (9); Site (3) FUNCTION: Required to prevent the misactivation of serine (Ser) with tRNA(Ala) by promoting the hydrolysis of Ser-mischarged tRNA(Ala), thereby playing a role in translational fidelity (PubMed:29769718). Binds directly to the catalytic domain of AARS/AlaRS and captures Ser that is misactivated by AARS/AlaRS, preventing the charging of Ser adenylates to tRNA(Ala) and precluding Ser misincorporation in nascent peptides (PubMed:29769718). {ECO:0000269|PubMed:29769718}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29769718}. Nucleus {ECO:0000269|PubMed:29769718}. SUBUNIT: Interacts with AARS; the interaction is direct. {ECO:0000269|PubMed:29769718}. DOMAIN: Side chains of Lys-102, Lys-135 and Lys-165 capture Ser that is misactivated by AARS/AlaRS. {ECO:0000269|PubMed:29769718}. TISSUE SPECIFICITY: Widely expressed in brain (at protein level). {ECO:0000269|PubMed:29769718}. +P97384 ANX11_MOUSE Annexin A11 (Annexin XI) (Annexin-11) (Calcyclin-associated annexin 50) (CAP-50) 503 54,079 Chain (1); Modified residue (3); Repeat (4); Sequence conflict (2) FUNCTION: Required for midbody formation and completion of the terminal phase of cytokinesis (By similarity). Binds specifically to calcyclin in a calcium-dependent manner. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Melanosome {ECO:0000250}. Nucleus envelope {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Found throughout the nucleoplasm at interphase and during mitosis concentrates around the mitotic apparatus. Elevation of intracellular calcium causes relocalization from the nucleoplasm to the nuclear envelope, with little effect on the cytoplasmic pool. Localization to the nuclear envelope is cell-cycle dependent. {ECO:0000250}. SUBUNIT: Interacts with S100A6. Interacts with PDCD6 in a calcium-dependent manner. Interacts with KIF23 during cytokinesis. {ECO:0000250}. DOMAIN: A pair of annexin repeats may form one binding site for calcium and phospholipid. +Q6P1H6 ANKL2_MOUSE Ankyrin repeat and LEM domain-containing protein 2 (LEM domain-containing protein 4) 964 106,198 Alternative sequence (4); Chain (1); Domain (1); Modified residue (8); Repeat (1); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 8 28 Helical; Signal-anchor for type III membrane protein. {ECO:0000255}. TOPO_DOM 1 7 Extracellular. {ECO:0000255}.; TOPO_DOM 29 964 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in mitotic nuclear envelope reassembly by promoting dephosphorylation of BAF/BANF1 during mitotic exit. Coordinates the control of BAF/BANF1 dephosphorylation by inhibiting VRK1 kinase and promoting dephosphorylation of BAF/BANF1 by protein phosphatase 2A (PP2A), thereby facilitating nuclear envelope assembly. It is unclear whether it acts as a real PP2A regulatory subunit or whether it is involved in recruitment of the PP2A complex (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. SUBUNIT: Interacts with BAF/BANF1. Interacts with protein phosphatase 2A (PP2A) components PPP2C (PPP2CA or PPP2CB) and PPP2R1A (By similarity). {ECO:0000250}. +P11859 ANGT_MOUSE Angiotensinogen (Serpin A8) [Cleaved into: Angiotensin-1 (Angiotensin 1-10) (Angiotensin I) (Ang I); Angiotensin-2 (Angiotensin 1-8) (Angiotensin II) (Ang II); Angiotensin-3 (Angiotensin 2-8) (Angiotensin III) (Ang III) (Des-Asp[1]-angiotensin II); Angiotensin-4 (Angiotensin 3-8) (Angiotensin IV) (Ang IV); Angiotensin 1-9; Angiotensin 1-7; Angiotensin 1-5; Angiotensin 1-4] 477 51,990 Beta strand (15); Chain (1); Disulfide bond (1); Glycosylation (3); Helix (12); Peptide (8); Signal peptide (1); Turn (4) FUNCTION: Essential component of the renin-angiotensin system (RAS), a potent regulator of blood pressure, body fluid and electrolyte homeostasis.; FUNCTION: Angiotensin-2: acts directly on vascular smooth muscle as a potent vasoconstrictor, affects cardiac contractility and heart rate through its action on the sympathetic nervous system, and alters renal sodium and water absorption through its ability to stimulate the zona glomerulosa cells of the adrenal cortex to synthesize and secrete aldosterone. {ECO:0000250}.; FUNCTION: Angiotensin-3: stimulates aldosterone release. {ECO:0000250}.; FUNCTION: Angiotensin 1-7: is a ligand for the G-protein coupled receptor MAS1. Has vasodilator and antidiuretic effects. Has an antithrombotic effect that involves MAS1-mediated release of nitric oxide from platelets. PTM: In response to low blood pressure, the enzyme renin/REN cleaves angiotensinogen to produce angiotensin-1. Angiotensin-1 is a substrate of ACE (angiotensin converting enzyme) that removes a dipeptide to yield the physiologically active peptide angiotensin-2. Angiotensin-1 and angiotensin-2 can be further processed to generate angiotensin-3, angiotensin-4 (By similarity). Angiotensin 1-9 is cleaved from angiotensin-1 by ACE2 (By similarity) and can be further processed by ACE to produce angiotensin 1-7, angiotensin 1-5 and angiotensin 1-4. Angiotensin 1-7 has also been proposed to be cleaved from angiotensin-2 by ACE2 or from angiotensin-1 by MME (neprilysin) (By similarity). {ECO:0000250}.; PTM: The disulfide bond is labile. Angiotensinogen is present in the circulation in a near 40:60 ratio with the oxidized disulfide-bonded form, which preferentially interacts with receptor-bound renin. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma. +Q640P2 ANGL1_MOUSE Angiopoietin-related protein 1 (Angiopoietin-like protein 1) 490 56,323 Alternative sequence (2); Chain (1); Coiled coil (1); Disulfide bond (2); Domain (1); Frameshift (1); Glycosylation (2); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +Q6DFX2 ANTR2_MOUSE Anthrax toxin receptor 2 487 53,184 Chain (1); Compositional bias (2); Disulfide bond (1); Domain (1); Glycosylation (1); Metal binding (3); Modified residue (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 319 339 Helical. {ECO:0000255}. TOPO_DOM 32 318 Extracellular. {ECO:0000255}.; TOPO_DOM 340 487 Cytoplasmic. {ECO:0000255}. FUNCTION: Necessary for cellular interactions with laminin and the extracellular matrix. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Binds laminin, and possibly also collagen type IV. Binds to the protective antigen (PA) of Bacillus anthracis in a divalent cation-dependent manner. Binding of PA leads to heptamerization of the receptor-PA complex (By similarity). {ECO:0000250}. DOMAIN: Binding to PA seems to be effected through the VWA domain. {ECO:0000250}. +Q8BH79 ANO10_MOUSE Anoctamin-10 (Transmembrane protein 16K) 659 76,188 Alternative sequence (4); Chain (1); Erroneous initiation (1); Frameshift (1); Sequence caution (1); Topological domain (9); Transmembrane (8) TRANSMEM 208 228 Helical. {ECO:0000255}.; TRANSMEM 241 261 Helical. {ECO:0000255}.; TRANSMEM 317 337 Helical. {ECO:0000255}.; TRANSMEM 353 373 Helical. {ECO:0000255}.; TRANSMEM 401 421 Helical. {ECO:0000255}.; TRANSMEM 501 521 Helical. {ECO:0000255}.; TRANSMEM 554 574 Helical. {ECO:0000255}.; TRANSMEM 591 611 Helical. {ECO:0000255}. TOPO_DOM 1 207 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 229 240 Extracellular. {ECO:0000255}.; TOPO_DOM 262 316 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 338 352 Extracellular. {ECO:0000255}.; TOPO_DOM 374 400 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 422 500 Extracellular. {ECO:0000255}.; TOPO_DOM 522 553 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 575 590 Extracellular. {ECO:0000255}.; TOPO_DOM 612 659 Cytoplasmic. {ECO:0000255}. FUNCTION: Does not exhibit calcium-activated chloride channel (CaCC) activity. Can inhibit the activity of ANO1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Shows predominantly an intracellular localization with a weak expression in the cell membrane. {ECO:0000250}. TISSUE SPECIFICITY: Predominant expression seen in epithelial tissues. {ECO:0000269|PubMed:20056604}. +O54774 AP3D1_MOUSE AP-3 complex subunit delta-1 (AP-3 complex subunit delta) (Adaptor-related protein complex 3 subunit delta-1) (Delta-adaptin) (mBLVR1) 1199 135,081 Chain (1); Coiled coil (4); Compositional bias (2); Initiator methionine (1); Modified residue (11); Repeat (9) FUNCTION: Part of the AP-3 complex, an adaptor-related complex which is not clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to lysosomes (By similarity). Involved in process of CD8+ T-cell and NK cell degranulation (By similarity). In concert with the BLOC-1 complex, AP-3 is required to target cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals (PubMed:21998198). {ECO:0000250|UniProtKB:O14617, ECO:0000269|PubMed:21998198}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. SUBUNIT: Adaptor protein complex 3 (AP-3) is a heterotetramer composed of two large adaptins (delta-type subunit AP3D1 and beta-type subunit AP3B1 or AP3B2), a medium adaptin (mu-type subunit AP3M1 or AP3M2) and a small adaptin (sigma-type subunit APS1 or AP3S2) (By similarity). AP-3 associates with the BLOC-1 complex. Interacts with SLC30A2. {ECO:0000250|UniProtKB:O14617, ECO:0000250|UniProtKB:Q865S1}. +Q14AT5 ANO7_MOUSE Anoctamin-7 (New gene expressed in prostate homolog) (Transmembrane protein 16G) 859 97,128 Alternative sequence (2); Chain (1); Glycosylation (2); Topological domain (9); Transmembrane (8) TRANSMEM 298 318 Helical. {ECO:0000255}.; TRANSMEM 363 383 Helical. {ECO:0000255}.; TRANSMEM 442 462 Helical. {ECO:0000255}.; TRANSMEM 493 513 Helical. {ECO:0000255}.; TRANSMEM 531 551 Helical. {ECO:0000255}.; TRANSMEM 652 672 Helical. {ECO:0000255}.; TRANSMEM 701 721 Helical. {ECO:0000255}.; TRANSMEM 781 801 Helical. {ECO:0000255}. TOPO_DOM 1 297 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 319 362 Extracellular. {ECO:0000255}.; TOPO_DOM 384 441 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 463 492 Extracellular. {ECO:0000255}.; TOPO_DOM 514 530 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 552 651 Extracellular. {ECO:0000255}.; TOPO_DOM 673 700 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 722 780 Extracellular. {ECO:0000255}.; TOPO_DOM 802 859 Cytoplasmic. {ECO:0000255}. FUNCTION: Has calcium-dependent phospholipid scramblase activity; scrambles phosphatidylserine, phosphatidylcholine and galactosylceramide. Does not exhibit calcium-activated chloride channel (CaCC) activity. May play a role in cell-cell interactions. {ECO:0000269|PubMed:23532839}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6IWH7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q6IWH7}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q6IWH7}. Note=Concentrates at sites of cell-cell contact. Shows an intracellular localization. {ECO:0000250|UniProtKB:Q6IWH7}. TISSUE SPECIFICITY: Highly expressed in the stomach. Expressed at low levels in small intestine and large intestine. {ECO:0000269|PubMed:20056604, ECO:0000269|PubMed:23532839}. +Q922H1 ANM3_MOUSE Protein arginine N-methyltransferase 3 (EC 2.1.1.-) (Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 3) 532 59,902 Active site (2); Alternative sequence (1); Beta strand (3); Binding site (5); Chain (1); Domain (1); Helix (7); Initiator methionine (1); Modified residue (4); Zinc finger (1) FUNCTION: Methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in some proteins. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Monomer or homodimer (By similarity). Interacts with EPB41L3; this inhibits methylation of target proteins. Interacts with the 40S ribosomal protein RPS2 (By similarity). {ECO:0000250}. DOMAIN: The zinc-finger is responsible for substrate specificity. {ECO:0000250}. +Q8VBT6 APOBR_MOUSE Apolipoprotein B receptor (Apolipoprotein B-100 receptor) (Apolipoprotein B48 receptor) (apoB-48R) 942 102,705 Chain (1); Compositional bias (1); Modified residue (3) FUNCTION: Macrophage receptor that binds to the apolipoprotein B48 (APOB) of dietary triglyceride (TG)-rich lipoproteins (TRL) or to a like domain of APOB in hypertriglyceridemic very low density lipoprotein (HTG-VLDL). Binds and internalizes TRL when out of the context of the macrophage. May provide essential lipids to reticuloendothelial cells. Could also be involved in foam cell formation with elevated TRL and remnant lipoprotein (RLP). Mediates the rapid high-affinity uptake of chylomicrons (CM), HTG-VLDL, and trypsinized (tryp) VLDL devoid of APOE in vitro in macrophages. {ECO:0000269|PubMed:12177162}. PTM: There are 2 forms in macrophages, the membrane-binding proteins 200 kDa (MBP 200) and 235 kDa (MBP 235), that can be reduced into a single active ligand-binding species with intermediate mobility (MBP 200R). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Binds monocyte-macrophage membrane. Thought to be anchored in the membrane through an interaction with an integral membrane protein (By similarity). {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in spleen, lung and skeletal muscle, and weakly in brain, heart, kidney, and testis. {ECO:0000269|PubMed:12177162}. +Q9Z1K7 APCL_MOUSE Adenomatous polyposis coli protein 2 2274 243,139 Chain (1); Coiled coil (2); Compositional bias (2); Modified residue (3); Region (4); Repeat (11) FUNCTION: Stabilizes microtubules and may regulate actin fiber dynamics through the activation of Rho family GTPases. May also function in Wnt signaling by promoting the rapid degradation of CTNNB1. {ECO:0000250|UniProtKB:O95996}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O95996}. Golgi apparatus {ECO:0000250|UniProtKB:O95996}. Cytoplasm {ECO:0000250|UniProtKB:O95996}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O95996}. Note=Associated with actin filaments. Associated with microtubule network. {ECO:0000250|UniProtKB:O95996}. SUBUNIT: Interacts with APC, CTNNB1, TP53BP2 and possibly with AXIN2 (By similarity). Interacts with MAPRE3, PSRC1 and probably MAPRE1. {ECO:0000250, ECO:0000269|PubMed:17310996}. TISSUE SPECIFICITY: Expressed in brain and other neural tissues. {ECO:0000269|PubMed:15018807}. +Q8BSZ2 AP3S2_MOUSE AP-3 complex subunit sigma-2 (AP-3 complex subunit sigma-3B) (Adaptor-related protein complex 3 subunit sigma-2) (Sigma-3B-adaptin) (Sigma3B-adaptin) (Sigma-adaptin 3b) 193 22,017 Chain (1); Sequence conflict (1) FUNCTION: Part of the AP-3 complex, an adaptor-related complex which is not clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to lysosomes. In concert with the BLOC-1 complex, AP-3 is required to target cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. {ECO:0000269|PubMed:21998198}. SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex. {ECO:0000250}. SUBUNIT: Adaptor protein complex 3 (AP-3) is a heterotetramer composed of two large adaptins (delta-type subunit AP3D1 and beta-type subunit AP3B1 or AP3B2), a medium adaptin (mu-type subunit AP3M1 or AP3M2) and a small adaptin (sigma-type subunit APS1 or AP3S2) (By similarity). AP-3 associates with the BLOC-1 complex. Interacts with AGAP1. {ECO:0000250, ECO:0000269|PubMed:12967569}. TISSUE SPECIFICITY: Present in all adult tissues examined. +Q68G58 APEX2_MOUSE DNA-(apurinic or apyrimidinic site) lyase 2 (EC 3.1.-.-) (EC 4.2.99.18) (APEX nuclease 2) (Apurinic-apyrimidinic endonuclease 2) (AP endonuclease 2) 516 57,340 Active site (2); Alternative sequence (7); Chain (1); Metal binding (5); Region (1); Sequence conflict (4); Site (3) FUNCTION: Function as a weak apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents. Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends. Displays also double-stranded DNA 3'-5' exonuclease, 3'-phosphodiesterase activities. Shows robust 3'-5' exonuclease activity on 3'-recessed heteroduplex DNA and is able to remove mismatched nucleotides preferentially. Shows fairly strong 3'-phosphodiesterase activity involved in the removal of 3'-damaged termini formed in DNA by oxidative agents. In the nucleus functions in the PCNA-dependent BER pathway. Required for somatic hypermutation (SHM) and DNA cleavage step of class switch recombination (CSR) of immunoglobulin genes. Required for proper cell cycle progression during proliferation of peripheral lymphocytes. {ECO:0000269|PubMed:12573260, ECO:0000269|PubMed:15319281, ECO:0000269|PubMed:18025127, ECO:0000269|PubMed:19556307}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Mitochondrion {ECO:0000305}. Note=Together with PCNA, is redistributed in discrete nuclear foci in presence of oxidative DNA damaging agents. SUBUNIT: Interacts with PCNA. This interaction is increased by misincorporation of uracil in nuclear DNA (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in lymphocytes, thymocytes and splenocytes (at protein level). Highly expressed in the thymus and weakly expressed in the bone marrow, spleen, eye, kidney, lung, brain and uterus. {ECO:0000269|PubMed:12573260, ECO:0000269|PubMed:15319281}. +Q8C4A0 AQP6_MOUSE Aquaporin-6 (AQP-6) 293 30,709 Chain (1); Glycosylation (1); Motif (2); Topological domain (7); Transmembrane (6) TRANSMEM 28 45 Helical. {ECO:0000255}.; TRANSMEM 52 70 Helical. {ECO:0000255}.; TRANSMEM 97 118 Helical. {ECO:0000255}.; TRANSMEM 139 159 Helical. {ECO:0000255}.; TRANSMEM 166 185 Helical. {ECO:0000255}.; TRANSMEM 212 233 Helical. {ECO:0000255}. TOPO_DOM 1 27 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 46 51 Extracellular. {ECO:0000255}.; TOPO_DOM 71 96 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 119 138 Extracellular. {ECO:0000255}.; TOPO_DOM 160 165 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 186 211 Extracellular. {ECO:0000255}.; TOPO_DOM 234 293 Cytoplasmic. {ECO:0000255}. FUNCTION: Forms a water-specific channel that participates in distinct physiological functions such as glomerular filtration, tubular endocytosis and acid-base metabolism. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. DOMAIN: Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA). +Q8BHH1 AQP11_MOUSE Aquaporin-11 (AQP-11) 271 30,481 Chain (1); Erroneous initiation (1); Motif (2); Transmembrane (6) TRANSMEM 15 35 Helical; Name=1. {ECO:0000255}.; TRANSMEM 42 62 Helical; Name=2. {ECO:0000255}.; TRANSMEM 75 95 Helical; Name=3. {ECO:0000255}.; TRANSMEM 164 184 Helical; Name=4. {ECO:0000255}.; TRANSMEM 195 215 Helical; Name=5. {ECO:0000255}.; TRANSMEM 235 255 Helical; Name=6. {ECO:0000255}. FUNCTION: Aquaporins facilitate the transport of water and small neutral solutes across cell membranes. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. DOMAIN: Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA). +Q3UYH7 ARBK2_MOUSE Beta-adrenergic receptor kinase 2 (Beta-ARK-2) (EC 2.7.11.15) 688 79,657 Active site (1); Binding site (1); Chain (1); Domain (4); Nucleotide binding (1); Region (1); Sequence conflict (1) FUNCTION: Specifically phosphorylates the agonist-occupied form of the beta-adrenergic and closely related receptors. PTM: Ubiquitinated. {ECO:0000250}. +Q6ZPS6 AKIB1_MOUSE Ankyrin repeat and IBR domain-containing protein 1 (EC 2.3.2.31) 1085 121,876 Active site (1); Chain (1); Coiled coil (1); Domain (1); Erroneous termination (1); Initiator methionine (1); Lipidation (1); Metal binding (20); Modified residue (3); Region (1); Repeat (2); Zinc finger (3) FUNCTION: Might act as an E3 ubiquitin-protein ligase, or as part of E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes and then transfers it to substrates. {ECO:0000250}. DOMAIN: Members of the RBR family are atypical E3 ligases. They interact with the E2 conjugating enzyme UBE2L3 and function like HECT-type E3 enzymes: they bind E2s via the first RING domain, but require an obligate trans-thiolation step during the ubiquitin transfer, requiring a conserved cysteine residue in the second RING domain. {ECO:0000250|UniProtKB:O60260}. +Q9JJR5 AKIP1_MOUSE A-kinase-interacting protein 1 (Breast cancer-associated gene 3 protein) (PKA-interacting protein) (Proline-rich protein BCA3) 212 23,979 Chain (1) FUNCTION: Enhances NF-kappa-B transcriptional activity by regulating the nuclear localization of the NF-kappa-B subunit RELA and promoting the phosphorylation of RELA by PRKACA. Regulates the effect of the cAMP-dependent protein kinase signaling pathway on the NF-kappa-B activation cascade (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Locates to punctate spots. {ECO:0000250}. SUBUNIT: Interacts with PRKACA and RELA. {ECO:0000250}. +B1AXD8 AKIR2_MOUSE Akirin-2 201 22,113 Chain (1); Compositional bias (1); Frameshift (1); Modified residue (3); Motif (1); Sequence conflict (2) FUNCTION: Forms a complex with YWHAB that acts to repress transcription of DUSP1 (By similarity). Required for embryonic development and the innate immune response. Downstream effector of the Toll-like receptor (TLR), TNF and IL-1 beta signaling pathways leading to the production of IL-6. {ECO:0000250, ECO:0000269|PubMed:18066067}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q53H80}. SUBUNIT: Interacts with YWHAB. {ECO:0000250|UniProtKB:Q25C79}. +Q9CZS1 AL1B1_MOUSE Aldehyde dehydrogenase X, mitochondrial (EC 1.2.1.3) (Aldehyde dehydrogenase family 1 member B1) 519 57,553 Active site (2); Chain (1); Modified residue (15); Nucleotide binding (1); Sequence conflict (2); Site (1); Transit peptide (1) Alcohol metabolism; ethanol degradation; acetate from ethanol: step 2/2. FUNCTION: ALDHs play a major role in the detoxification of alcohol-derived acetaldehyde. They are involved in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. SUBUNIT: Homotetramer. {ECO:0000250}. +Q8K023 AKC1H_MOUSE Aldo-keto reductase family 1 member C18 (EC 1.1.-.-) (20-alpha-hydroxysteroid dehydrogenase) (20-alpha-HSD) (EC 1.1.1.149) 323 37,177 Active site (1); Alternative sequence (1); Binding site (3); Chain (1); Nucleotide binding (4); Site (2) FUNCTION: Catalyzes the conversion of progesterone into 20-alpha-dihydroprogesterone (20 alpha-OHP). SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. +Q8QZR5 ALAT1_MOUSE Alanine aminotransferase 1 (ALT1) (EC 2.6.1.2) (Glutamate pyruvate transaminase 1) (GPT 1) (Glutamic--alanine transaminase 1) (Glutamic--pyruvic transaminase 1) 496 55,143 Chain (1); Initiator methionine (1); Modified residue (3) Amino-acid degradation; L-alanine degradation via transaminase pathway; pyruvate from L-alanine: step 1/1. FUNCTION: Catalyzes the reversible transamination between alanine and 2-oxoglutarate to form pyruvate and glutamate. Participates in cellular nitrogen metabolism and also in liver gluconeogenesis starting with precursors transported from skeletal muscles (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Mainly expressed in liver, intestine, colon and white adipose tissue. {ECO:0000269|PubMed:15122758}. +A2ASQ1 AGRIN_MOUSE Agrin [Cleaved into: Agrin N-terminal 110 kDa subunit; Agrin C-terminal 110 kDa subunit; Agrin C-terminal 90 kDa fragment (C90); Agrin C-terminal 22 kDa fragment (C22)] 1950 207,539 Alternative sequence (3); Beta strand (13); Calcium binding (2); Chain (5); Compositional bias (4); Disulfide bond (48); Domain (19); Erroneous gene model prediction (1); Glycosylation (5); Helix (4); Modified residue (2); Natural variant (1); Sequence conflict (1); Site (7); Topological domain (2); Transmembrane (1) TRANSMEM 27 47 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 26 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 48 1950 Extracellular. {ECO:0000255}. FUNCTION: Isoform 1: heparan sulfate basal lamina glycoprotein that plays a central role in the formation and the maintenance of the neuromuscular junction (NMJ) and directs key events in postsynaptic differentiation. This neuron-specific (z+) isoform is a component of the AGRN-LRP4 receptor complex that induces the phosphorylation and activation of MUSK. The activation of MUSK in myotubes induces the formation of NMJ by regulating different processes including the transcription of specific genes and the clustering of AChR in the postsynaptic membrane. Calcium ions are required for maximal AChR clustering. AGRN function in neurons is highly regulated by alternative splicing, glycan binding and proteolytic processing. Modulates calcium ion homeostasis in neurons, specifically by inducing an increase in cytoplasmic calcium ions. Functions differentially in the central nervous system (CNS) by inhibiting the alpha(3)-subtype of Na+/K+-ATPase and evoking depolarization at CNS synapses. This transmembrane agrin (TM-agrin) isoform, the predominate form in neurons of the brain, induces dendritic filopodia and synapse formation in mature hippocampal neurons in large part due to the attached glycosaminoglycan chains and the action of Rho-family GTPases.; FUNCTION: Isoform 2 and isoform 3: these isoforms lacking the 'z' insert (z0) are muscle-specific, have no AChR clustering ability and may be involved in nervous system endothelial cell differentiation.; FUNCTION: Agrin N-terminal 110 kDa subunit: involved in regulation of neurite outgrowth probably due to the presence of the glycosaminoglcan (GAG) side chains of heparan and chondroitin sulfate attached to the Ser/Thr- and Gly/Ser-rich regions. Also involved in modulation of growth factor signaling (By similarity). {ECO:0000250, ECO:0000269|PubMed:10402191, ECO:0000269|PubMed:11018052, ECO:0000269|PubMed:12796478, ECO:0000269|PubMed:17611272, ECO:0000269|PubMed:19303856, ECO:0000269|PubMed:21885656, ECO:0000269|PubMed:8653787}.; FUNCTION: Agrin C-terminal 22 kDa fragment: this released fragment is important for agrin signaling and to exert a maximal dendritic filopodia-inducing effect. All 'z' splice variants (z+) of this fragment also show an increase in the number of filopodia. PTM: Contains heparan and chondroitin sulfate chains and alpha-dystroglycan as well as N-linked and O-linked oligosaccharides. Heparin and heparin sulfate binding in the G3 domain is independent of calcium ions. Binds heparin with a stoichiometry of 2:1. Binds sialic acid with a stoichiometry of 1:1 and binding requires calcium ions (By similarity). Glycosaminoglycans (GAGs), present in the N-terminal 110 kDa fragment, are required for induction of filopodia in hippocampal neurons. The first cluster (Gly/Ser-rich) for GAG attachment contains heparan sulfate (HS) chains and the second cluster (Ser/Thr-rich), contains chondroitin sulfate (CS) chains. {ECO:0000250}.; PTM: At synaptic junctions, cleaved at two conserved sites, alpha and beta, by neurotrypsin. Cleavage at the alpha-site produces the agrin N-terminal 110-kDa subunit and the agrin C-terminal 110-kDa subunit. Further cleavage of agrin C-terminal 110-kDa subunit at the beta site produces the C-terminal fragments, agrin C-terminal 90 kDa fragment and agrin C-terminal 22 kDa fragment. Excessive cleavage at the beta-site releases large amounts of the agrin C-terminal 22 kDa fragment leading to destabilization at the neuromuscular junction (NMJ). Cleavage is developmentally regulated. In developing brain, neurotrypsin-mediated cleavage occurs mainly during late fetal days and in the first postnatal week. {ECO:0000269|PubMed:18230682, ECO:0000269|PubMed:19303856, ECO:0000269|PubMed:21885656}. SUBCELLULAR LOCATION: Cell junction, synapse {ECO:0000269|PubMed:10402191, ECO:0000269|PubMed:12796478, ECO:0000269|PubMed:17611272, ECO:0000269|PubMed:18230682, ECO:0000269|PubMed:8653787}. Cell membrane {ECO:0000269|PubMed:11018052, ECO:0000269|PubMed:11161480}; Single-pass type II membrane protein {ECO:0000269|PubMed:11018052, ECO:0000269|PubMed:11161480}. SUBUNIT: Monomer (By similarity). Interacts (N-terminal subunit) with TGF-beta family members, BMP2 AND BMP4; the interactions inhibit the activity of these growth factors. Interacts with TGFB1; the interaction enhances the activity of TGFB1. Interacts with DAG1; the interaction is influenced by cell surface glycosaminoglycans and by alternative splicing of AGRN (By similarity). Component of the AGRN-LRP4 complex that consists of a tetramer of two AGRN-LRP4 heterodimers. Interacts (via the laminin G-like 3 domain) directly with LRP4; the interaction is required for activation of MUSK and clustering of AChR and requires the 'z8' insert present in the z(+8) isoforms. {ECO:0000250, ECO:0000269|PubMed:8653787}. DOMAIN: Both laminin G-like 2 (G2) and laminin G-like 3 (G3) domains are required for alpha-dystroglycan binding. G3 domain is required for C-terminal heparin, heparan sulfate and sialic acid binding (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in central nervous system (CNS) synapses such as in the cerebral cortex and hippocampus. Localizes to basal lamina of hippocampal blood vessels. Both (z+) and (z-) isoforms found in kidney, heart and cerebral vasculature. {ECO:0000269|PubMed:10402191, ECO:0000269|PubMed:11018052, ECO:0000269|PubMed:17611272, ECO:0000269|PubMed:18230682}. +E9Q394 AKP13_MOUSE A-kinase anchor protein 13 (AKAP-13) (AKAP-Lbc) 2776 303,976 Alternative sequence (2); Chain (1); Coiled coil (2); Compositional bias (4); Domain (2); Modified residue (25); Region (3); Zinc finger (1) FUNCTION: Scaffold protein that plays an important role in assembling signaling complexes downstream of several types of G protein-coupled receptors. Activates RHOA in response to signaling via G protein-coupled receptors via its function as Rho guanine nucleotide exchange factor. May also activate other Rho family members (PubMed:23658642). Part of a kinase signaling complex that links ADRA1A and ADRA1B adrenergic receptor signaling to the activation of downstream p38 MAP kinases, such as MAPK11 and MAPK14. Part of a signaling complex that links ADRA1B signaling to the activation of RHOA and IKBKB/IKKB, leading to increased NF-kappa-B transcriptional activity. Part of a RHOA-dependent signaling cascade that mediates responses to lysophosphatidic acid (LPA), a signaling molecule that activates G-protein coupled receptors and potentiates transcriptional activation of the glucocorticoid receptor NR3C1 (By similarity). Part of a signaling cascade that stimulates MEF2C-dependent gene expression in response to lysophosphatidic acid (LPA) (By similarity). Part of a signaling pathway that activates MAPK11 and/or MAPK14 and leads to increased transcription activation of the estrogen receptors ESR1 and ESR2. Part of a signaling cascade that links cAMP and EGFR signaling to BRAF signaling and to PKA-mediated phosphorylation of KSR1, leading to the activation of downstream MAP kinases, such as MAPK1 or MAPK3 (By similarity). Functions as scaffold protein that anchors cAMP-dependent protein kinase (PKA) and PRKD1. This promotes activation of PRKD1, leading to increased phosphorylation of HDAC5 and ultimately cardiomyocyte hypertrophy (PubMed:24161911). Has no guanine nucleotide exchange activity on CDC42, Ras or Rac (By similarity). Required for normal embryonic heart development, and in particular for normal sarcomere formation in the developing cardiomyocytes (PubMed:20139090). Plays a role in cardiomyocyte growth and cardiac hypertrophy in response to activation of the beta-adrenergic receptor by phenylephrine or isoproterenol (PubMed:23658642, PubMed:24161911). Required for normal adaptive cardiac hypertrophy in response to pressure overload (PubMed:17537920, PubMed:24161911). Plays a role in osteogenesis (PubMed:25892096). {ECO:0000250|UniProtKB:Q12802, ECO:0000269|PubMed:17537920, ECO:0000269|PubMed:20139090, ECO:0000269|PubMed:23658642, ECO:0000269|PubMed:24161911, ECO:0000269|PubMed:25892096}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q12802}. Cytoplasm {ECO:0000250|UniProtKB:Q12802}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q12802}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:20139090}. Nucleus {ECO:0000250|UniProtKB:Q12802}. Membrane {ECO:0000250|UniProtKB:Q12802}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q12802}. Note=Colocalizes with actin and myosin filaments in developing cardiomyocytes (PubMed:20139090). Colocalizes with the actin cytoskeleton at the cell cortex (By similarity). {ECO:0000250|UniProtKB:Q12802, ECO:0000269|PubMed:20139090}. SUBUNIT: Interacts with the cAMP-dependent protein kinase (PKA) holoenzyme and with the regulatory subunit PRKAR2A (PubMed:21102438, PubMed:24161911, PubMed:23658642). Interacts with RHOA. Interacts also with RHOB and RHOC. Identified in a ternary complex with RHOA and PRKAR2A. Identified in a complex with NR3C1 and RHOA (By similarity). Interacts with BRAF and KSR1. Identified in a complex with BRAF and KSR1 (PubMed:21102438). Component of a signaling complex containing at least AKAP13, PKN1, MAPK14, ZAK and MAP2K3. Within this complex, AKAP13 interacts directly with PKN1, which in turn recruits MAPK14, MAP2K3 and ZAK. Interacts (phosphorylated form) with YWHAB and YWHAZ. Interaction with YWHAB inhibits activation of RHOA, interferes with PKN1 binding and activation of MAP kinases. Interacts with GNA12 (By similarity). Interacts with IKBKB (PubMed:23090968). Interacts with ESR1, THRA, PPARA and NME2 (By similarity). Interacts (via the C-terminal domain after the PH domain) with MEF2C and RXRB (PubMed:20139090). Interacts (via the C-terminal domain after the PH domain) with PRKD1 (PubMed:23658642, PubMed:24161911). {ECO:0000250|UniProtKB:Q12802, ECO:0000269|PubMed:20139090, ECO:0000269|PubMed:21102438, ECO:0000269|PubMed:23090968, ECO:0000269|PubMed:23658642, ECO:0000269|PubMed:24161911}. DOMAIN: The DH domain is sufficient for interaction with RHOA, and for guanine nucleotide exchange (GEF) activity with RHOA. Forms that lack C-terminal regulatory domains have transforming activity and function as oncogenes. {ECO:0000250|UniProtKB:Q12802}.; DOMAIN: The PH domain does not play a role in lipid-binding. Instead, it inhibits the guanine nucleotide exchange (GEF) activity of the isolated DH domain (in vitro). {ECO:0000250|UniProtKB:Q12802}.; DOMAIN: The C-terminal domain after the PH domain is involved in protein-protein interactions that are required for normal, compensatory cardiac hypertrophy in response to pressure overload. {ECO:0000269|PubMed:24161911}. TISSUE SPECIFICITY: Detected in embryonic heart, limb bud, first branchial arch and forebrain (at protein level) (PubMed:20139090). Detected in heart (PubMed:20139090). Detected in perichondrium, but not in the bone growth plate (PubMed:25892096). {ECO:0000269|PubMed:20139090, ECO:0000269|PubMed:25892096}. +Q14DN9 AKD1B_MOUSE Ankyrin repeat and death domain-containing protein 1B 521 58,456 Alternative sequence (2); Chain (1); Domain (1); Repeat (10); Sequence caution (1); Sequence conflict (1) +P47739 AL3A1_MOUSE Aldehyde dehydrogenase, dimeric NADP-preferring (EC 1.2.1.5) (Aldehyde dehydrogenase 4) (Aldehyde dehydrogenase family 3 member A1) (Dioxin-inducible aldehyde dehydrogenase 3) 453 50,481 Active site (2); Chain (1); Initiator methionine (1); Modified residue (3); Natural variant (3); Nucleotide binding (1); Sequence conflict (2) FUNCTION: ALDHs play a major role in the detoxification of alcohol-derived acetaldehyde (Probable). They are involved in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation (Probable). Oxidizes medium and long chain aldehydes into non-toxic fatty acids (PubMed:25286108). Preferentially oxidizes aromatic aldehyde substrates (PubMed:11784860). Comprises about 50 percent of corneal epithelial soluble proteins (PubMed:11784860). May play a role in preventing corneal damage caused by ultraviolet light (PubMed:10376761). {ECO:0000250|UniProtKB:P30838, ECO:0000269|PubMed:10376761, ECO:0000269|PubMed:11784860, ECO:0000269|PubMed:25286108, ECO:0000305}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25286108}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P30838}. TISSUE SPECIFICITY: Constitutively expressed in cornea, stomach, skin, bladder and lungs. Lowest expression levels in lungs and bladder. {ECO:0000269|PubMed:10376761}. +Q8BIX3 AL14E_MOUSE ARL14 effector protein (ARF7 effector protein) 276 31,011 Alternative sequence (2); Chain (1); Compositional bias (1); Cross-link (1); Modified residue (2); Sequence conflict (2) FUNCTION: Through its interaction with ARL14 and MYO1E, may connect MHC class II-containing cytoplasmic vesicles to the actin network and hence controls the movement of these vesicles along the actin cytoskeleton in dendritic cells. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with ARL14 and MYO1E. {ECO:0000250}. +Q8VCT3 AMPB_MOUSE Aminopeptidase B (AP-B) (EC 3.4.11.6) (Arginine aminopeptidase) (Arginyl aminopeptidase) (Cytosol aminopeptidase IV) 650 72,416 Active site (1); Chain (1); Metal binding (3); Modified residue (1); Region (1); Sequence conflict (2); Site (1) FUNCTION: Exopeptidase which selectively removes arginine and/or lysine residues from the N-terminus of several peptide substrates including Arg(0)-Leu-enkephalin, Arg(0)-Met-enkephalin and Arg(-1)-Lys(0)-somatostatin-14. Can hydrolyze leukotriene A4 (LTA-4) into leukotriene B4 (LTB-4) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Monomer. {ECO:0000250}. +Q9CPY7 AMPL_MOUSE Cytosol aminopeptidase (EC 3.4.11.1) (Leucine aminopeptidase 3) (LAP-3) (Leucyl aminopeptidase) (Proline aminopeptidase) (EC 3.4.11.5) (Prolyl aminopeptidase) 519 56,141 Active site (2); Alternative sequence (1); Chain (1); Erroneous initiation (5); Metal binding (7); Modified residue (14); Sequence conflict (3) FUNCTION: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homohexamer. {ECO:0000250}. +A2RT91 ANKAR_MOUSE Ankyrin and armadillo repeat-containing protein 1465 165,290 Chain (1); Repeat (11); Sequence conflict (1); Transmembrane (1) TRANSMEM 313 329 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q99LW0 ANR10_MOUSE Ankyrin repeat domain-containing protein 10 415 43,975 Chain (1); Repeat (4); Sequence conflict (1) +Q9JHZ2 ANKH_MOUSE Progressive ankylosis protein (Fn54 protein) 492 54,298 Chain (1); Natural variant (1); Topological domain (9); Transmembrane (8) TRANSMEM 86 106 Helical. {ECO:0000255}.; TRANSMEM 132 152 Helical. {ECO:0000255}.; TRANSMEM 159 179 Helical. {ECO:0000255}.; TRANSMEM 190 210 Helical. {ECO:0000255}.; TRANSMEM 327 347 Helical. {ECO:0000255}.; TRANSMEM 351 371 Helical. {ECO:0000255}.; TRANSMEM 404 426 Helical. {ECO:0000255}.; TRANSMEM 430 452 Helical. {ECO:0000255}. TOPO_DOM 1 85 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 107 131 Extracellular. {ECO:0000255}.; TOPO_DOM 153 158 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 180 189 Extracellular. {ECO:0000255}.; TOPO_DOM 211 326 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 348 350 Extracellular. {ECO:0000255}.; TOPO_DOM 372 403 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 427 429 Extracellular. {ECO:0000255}.; TOPO_DOM 453 492 Cytoplasmic. {ECO:0000255}. FUNCTION: Regulates intra- and extracellular levels of inorganic pyrophosphate (PPi), probably functioning as PPi transporter. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in heart, brain, liver, spleen, lung, muscle, and kidney of adult animals. Strongly expressed in the developing articular cartilage of joints in the shoulder, elbow, wrist, and digits of the embryo. DISEASE: Note=Defects in Ankh are the cause of a generalized, progressive form of arthritis. In ank mice hydroxyapatite crystals develop in articular surfaces and synovial fluid leading to joint space narrowing, cartilage erosion, and formation of bony outgrowths or osteophytes that cause fusion and joint immobility and destruction. +P48036 ANXA5_MOUSE Annexin A5 (Anchorin CII) (Annexin V) (Annexin-5) (Calphobindin I) (CBP-I) (Endonexin II) (Lipocortin V) (Placental anticoagulant protein 4) (PP4) (Placental anticoagulant protein I) (PAP-I) (Thromboplastin inhibitor) (Vascular anticoagulant-alpha) (VAC-alpha) 319 35,752 Chain (1); Cross-link (2); Initiator methionine (1); Modified residue (8); Motif (1); Repeat (4); Sequence conflict (4) FUNCTION: This protein is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade. PTM: S-nitrosylation is induced by interferon-gamma and oxidatively-modified low-densitity lipoprotein (LDL(ox)) possibly implicating the iNOS-S100A8/9 transnitrosylase complex. {ECO:0000250|UniProtKB:P08758}. SUBUNIT: Monomer. Binds ATRX and EIF5B (By similarity). {ECO:0000250}. DOMAIN: A pair of annexin repeats may form one binding site for calcium and phospholipid.; DOMAIN: The [IL]-x-C-x-x-[DE] motif is a proposed target motif for cysteine S-nitrosylation mediated by the iNOS-S100A8/A9 transnitrosylase complex. {ECO:0000250|UniProtKB:P08758}. +O35298 AOAH_MOUSE Acyloxyacyl hydrolase (EC 3.1.1.77) [Cleaved into: Acyloxyacyl hydrolase small subunit; Acyloxyacyl hydrolase large subunit] 574 65,155 Active site (1); Beta strand (10); Binding site (1); Chain (2); Disulfide bond (9); Domain (1); Glycosylation (4); Helix (29); Metal binding (18); Mutagenesis (1); Propeptide (1); Region (2); Signal peptide (1); Turn (13) FUNCTION: Removes the secondary (acyloxyacyl-linked) fatty acyl chains from the lipid A region of bacterial lipopolysaccharides (LPS) (PubMed:12810692, PubMed:15155618, PubMed:17322564, PubMed:19860560). By breaking down LPS, terminates the host response to bacterial infection and prevents prolonged and damaging inflammatory responses (PubMed:17322564, PubMed:19860560, PubMed:28622363). In peritoneal macrophages, seems to be important for recovery from a state of immune tolerance following infection by Gram-negative bacteria (PubMed:18779055). {ECO:0000269|PubMed:12810692, ECO:0000269|PubMed:15155618, ECO:0000269|PubMed:17322564, ECO:0000269|PubMed:18779055, ECO:0000269|PubMed:19860560, ECO:0000269|PubMed:28622363}. PTM: Cleaved into a large and a small subunit. {ECO:0000250|UniProtKB:P28039}.; PTM: The small subunit is N-glycosylated. {ECO:0000250|UniProtKB:P28039}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15155618}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:P28039}. Note=Detected in urine. {ECO:0000269|PubMed:15155618}. SUBUNIT: Heterodimer of the large and small subunits; disulfide-linked. {ECO:0000305|PubMed:15155618, ECO:0000305|PubMed:29343645}. TISSUE SPECIFICITY: Detected in peritoneal macrophages (at protein level) (PubMed:17322564, PubMed:28622363). Strongly expressed in kidney cortex, where it may be produced by proximal tubule cells (PubMed:15155618). In liver, expressed at high levels in Kupffer cells (PubMed:17322564). Expressed by dendritic cells (PubMed:12810692). Detected at low levels in alveolar macrophages (PubMed:28622363). {ECO:0000269|PubMed:12810692, ECO:0000269|PubMed:15155618, ECO:0000269|PubMed:17322564, ECO:0000269|PubMed:28622363}. +P32261 ANT3_MOUSE Antithrombin-III (ATIII) (Serpin C1) 465 52,004 Binding site (3); Chain (1); Disulfide bond (3); Glycosylation (4); Modified residue (2); Signal peptide (1); Site (1) FUNCTION: Most important serine protease inhibitor in plasma that regulates the blood coagulation cascade. AT-III inhibits thrombin, matriptase-3/TMPRSS7, as well as factors IXa, Xa and XIa. Its inhibitory activity is greatly enhanced in the presence of heparin (By similarity). {ECO:0000250}. PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000250|UniProtKB:P01008}. SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250}. SUBUNIT: Forms protease inhibiting heterodimer with TMPRSS7. {ECO:0000250}. TISSUE SPECIFICITY: Plasma. +Q9JME5 AP3B2_MOUSE AP-3 complex subunit beta-2 (Adaptor protein complex AP-3 subunit beta-2) (Adaptor-related protein complex 3 subunit beta-2) (Beta-3B-adaptin) (Clathrin assembly protein complex 3 beta-2 large chain) 1082 119,193 Chain (1); Compositional bias (1); Modified residue (2); Sequence conflict (1) FUNCTION: Subunit of non-clathrin- and clathrin-associated adaptor protein complex 3 (AP-3) that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. AP-3 appears to be involved in the sorting of a subset of transmembrane proteins targeted to lysosomes and lysosome-related organelles. In concert with the BLOC-1 complex, AP-3 is required to target cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. {ECO:0000269|PubMed:21998198}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Golgi apparatus {ECO:0000250}. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex. {ECO:0000250}. SUBUNIT: Adaptor protein complex 3 (AP-3) is a heterotetramer composed of two large adaptins (delta-type subunit AP3D1 and beta-type subunit AP3B1 or AP3B2), a medium adaptin (mu-type subunit AP3M1 or AP3M2) and a small adaptin (sigma-type subunit APS1 or AP3S2) (By similarity). AP-3 associates with the BLOC-1 complex. {ECO:0000250}. +Q9D3J5 ANR22_MOUSE Ankyrin repeat domain-containing protein 22 191 21,910 Chain (1); Repeat (4); Sequence conflict (2) +P98084 APBA2_MOUSE Amyloid-beta A4 precursor protein-binding family A member 2 (Adapter protein X11beta) (Neuron-specific X11L protein) (Neuronal Munc18-1-interacting protein 2) (Mint-2) 750 82,758 Chain (1); Domain (3); Modified residue (2); Region (1); Sequence conflict (5) FUNCTION: Putative function in synaptic vesicle exocytosis by binding to STXBP1, an essential component of the synaptic vesicle exocytotic machinery. May modulate processing of the amyloid-beta precursor protein (APP) and hence formation of APP-beta. SUBUNIT: Part of a multimeric complex containing STXBP1 and syntaxin-1. Binds to the cytoplasmic domain of amyloid-beta protein, and to the nuclear factor NF-kappa-B/p65 via its PDZ domain. Interacts with the N-terminal domain of APBA2BP (By similarity). {ECO:0000250}. DOMAIN: Composed of an N-terminal domain that binds STXBP1, a middle phosphotyrosine-binding domain (PID/PTB) that mediates binding with the cytoplasmic domain of the amyloid-beta precursor protein, and two C-terminal PDZ domains thought to attach proteins to the plasma membrane. TISSUE SPECIFICITY: Specifically expressed in neurons, predominantly of the cerebellum, hippocampus, and spinal cord. Lesser extent in neurons of the cerebral cortex and anterior thalmic nuclei. +Q64133 AOFA_MOUSE Amine oxidase [flavin-containing] A (EC 1.4.3.4) (Monoamine oxidase type A) (MAO-A) 526 59,602 Chain (1); Modified residue (3); Region (1); Sequence conflict (1); Site (2); Topological domain (2); Transmembrane (1) TRANSMEM 498 518 Helical; Anchor for type IV membrane protein. {ECO:0000250}. TOPO_DOM 1 497 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 519 526 Mitochondrial intermembrane. {ECO:0000250}. FUNCTION: Catalyzes the oxidative deamination of biogenic and xenobiotic amines and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. MAOA preferentially oxidizes biogenic amines such as 5-hydroxytryptamine (5-HT), norepinephrine and epinephrine (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass type IV membrane protein; Cytoplasmic side. SUBUNIT: Monomer, homo- or heterodimer (containing two subunits of similar size). Each subunit contains a covalently bound flavin. Enzymatically active as monomer (By similarity). {ECO:0000250}. +P24549 AL1A1_MOUSE Retinal dehydrogenase 1 (RALDH 1) (RalDH1) (EC 1.2.1.-) (EC 1.2.1.36) (ALDH-E1) (ALHDII) (Aldehyde dehydrogenase family 1 member A1) (Aldehyde dehydrogenase, cytosolic) 501 54,468 Active site (2); Chain (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (12); Nucleotide binding (7); Sequence conflict (7); Site (1) Cofactor metabolism; retinol metabolism. FUNCTION: Can convert/oxidize retinaldehyde to retinoic acid. Binds free retinal and cellular retinol-binding protein-bound retinal (By similarity). May have a broader specificity and oxidize other aldehydes in vivo (By similarity). {ECO:0000250|UniProtKB:P00352, ECO:0000250|UniProtKB:P51647}. PTM: The N-terminus is blocked most probably by acetylation. {ECO:0000250|UniProtKB:P15437}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P48644}. SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P51977}. TISSUE SPECIFICITY: Expressed in the liver, lung, and testis. Apparently not expressed at detectable levels in kidney, stomach, ovary, heart, and brain. +Q6P8H8 ALG8_MOUSE Probable dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase (EC 2.4.1.265) (Asparagine-linked glycosylation protein 8 homolog) (Dol-P-Glc:Glc(1)Man(9)GlcNAc(2)-PP-dolichyl alpha-1,3-glucosyltransferase) (Dolichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichyl glucosyltransferase) 526 59,535 Chain (1); Sequence conflict (1); Transmembrane (11) TRANSMEM 9 29 Helical. {ECO:0000255}.; TRANSMEM 108 128 Helical. {ECO:0000255}.; TRANSMEM 143 163 Helical. {ECO:0000255}.; TRANSMEM 188 208 Helical. {ECO:0000255}.; TRANSMEM 238 258 Helical. {ECO:0000255}.; TRANSMEM 334 354 Helical. {ECO:0000255}.; TRANSMEM 361 380 Helical. {ECO:0000255}.; TRANSMEM 400 422 Helical. {ECO:0000255}.; TRANSMEM 427 449 Helical. {ECO:0000255}.; TRANSMEM 461 481 Helical. {ECO:0000255}.; TRANSMEM 487 507 Helical. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Adds the second glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Glc(1)Man(9)GlcNAc(2)-PP-Dol before it is transferred to the nascent peptide (By similarity). Required for PKD1/Polycystin-1 maturation and localization to the plasma membrane of the primary cilia (PubMed:28375157). {ECO:0000250|UniProtKB:P40351, ECO:0000269|PubMed:28375157}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q9D4H4 AMOL1_MOUSE Angiomotin-like protein 1 (junction-enriched and -associated protein) (JEAP) 968 107,950 Alternative sequence (1); Chain (1); Coiled coil (4); Modified residue (9); Motif (1); Sequence conflict (1) FUNCTION: Inhibits the Wnt/beta-catenin signaling pathway, probably by recruiting CTNNB1 to recycling endosomes and hence preventing its translocation to the nucleus. {ECO:0000250}. PTM: Polyubiquitinated by NEDD4, leading to proteasomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000269|PubMed:11733531}. TISSUE SPECIFICITY: Expressed in exocrine glands, including pancreas, submandibular gland, lacrimal gland, parotid gland and sublingual gland (at protein level). {ECO:0000269|PubMed:11733531}. +Q2KHK3 AMPQ_MOUSE Aminopeptidase Q (AP-Q) (APQ) (EC 3.4.11.-) (Laeverin) 559 63,338 Active site (1); Binding site (1); Chain (1); Glycosylation (5); Metal binding (3); Region (1); Sequence conflict (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 14 34 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 13 Cytoplasmic. {ECO:0000250|UniProtKB:Q6Q4G3}.; TOPO_DOM 35 559 Lumenal. {ECO:0000250|UniProtKB:Q6Q4G3}. FUNCTION: Metalloprotease which may be important for placentation by regulating biological activity of key peptides at the embryo-maternal interface. On synthetic substrates it shows a marked preference for Leu-4-methylcoumaryl-7-amide (Leu-MCA) over Met-MCA, Arg-LCA and Lys-LCA. Cleaves the N-terminal amino acid of several peptides such as angiotensin-3, kisspeptin-10 and endokinin C. {ECO:0000250|UniProtKB:Q6Q4G3}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q6Q4G3}. SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q6Q4G3}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q6Q4G3}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q6Q4G3}. +Q9DBT5 AMPD2_MOUSE AMP deaminase 2 (EC 3.5.4.6) (AMP deaminase isoform L) 798 92,024 Active site (1); Binding site (2); Chain (1); Erroneous initiation (1); Metal binding (4); Modified residue (10); Region (2) Purine metabolism; IMP biosynthesis via salvage pathway; IMP from AMP: step 1/1. FUNCTION: AMP deaminase plays a critical role in energy metabolism. Catalyzes the deamination of AMP to IMP and plays an important role in the purine nucleotide cycle (By similarity). {ECO:0000250}. SUBUNIT: Homotetramer. {ECO:0000250}. +Q3UUE9 ANKUB_MOUSE Protein ANKUB1 (Ankyrin repeat and ubiquitin domain-containing 1) 192 22,006 Chain (1) +Q8BLB8 AN34C_MOUSE Ankyrin repeat domain-containing protein 34C 534 58,171 Chain (1); Modified residue (2); Repeat (4) +P56380 AP4A_MOUSE Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical] (EC 3.6.1.17) (Diadenosine 5',5'''-P1,P4-tetraphosphate asymmetrical hydrolase) (Ap4A hydrolase) (Ap4Aase) (Diadenosine tetraphosphatase) (Nucleoside diphosphate-linked moiety X motif 2) (Nudix motif 2) 147 16,989 Chain (1); Domain (1); Initiator methionine (1); Modified residue (1); Motif (1); Sequence conflict (1) FUNCTION: Asymmetrically hydrolyzes Ap4A to yield AMP and ATP. Plays a major role in maintaining homeostasis (By similarity). {ECO:0000250}. +Q69ZU8 ANKR6_MOUSE Ankyrin repeat domain-containing protein 6 (Diversin) 712 77,982 Alternative sequence (1); Chain (1); Coiled coil (2); Compositional bias (1); Repeat (8) FUNCTION: Recruits CKI-epsilon to the beta-catenin degradation complex that consists of AXN1 or AXN2 and GSK3-beta and allows efficient phosphorylation of beta-catenin, thereby inhibiting beta-catenin/Tcf signals. {ECO:0000269|PubMed:12183362}. SUBUNIT: Interacts with AXN1, AXN2 and CSNK1E/CKI-epsilon. {ECO:0000269|PubMed:12183362}. +P61967 AP1S1_MOUSE AP-1 complex subunit sigma-1A (Adaptor protein complex AP-1 subunit sigma-1A) (Adaptor-related protein complex 1 subunit sigma-1A) (Clathrin assembly protein complex 1 sigma-1A small chain) (Clathrin coat assembly protein AP19) (Golgi adaptor HA1/AP1 adaptin sigma-1A subunit) (HA1 19 kDa subunit) (Sigma 1a subunit of AP-1 clathrin) (Sigma-adaptin 1A) (Sigma1A-adaptin) 158 18,733 Chain (1); Modified residue (1) FUNCTION: Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Membrane, clathrin-coated pit. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex. SUBUNIT: Adaptor protein complex 1 (AP-1) is a heterotetramer composed of two large adaptins (gamma-type subunit AP1G1 and beta-type subunit AP1B1), a medium adaptin (mu-type subunit AP1M1 or AP1M2) and a small adaptin (sigma-type subunit AP1S1 or AP1S2 or AP1S3). TISSUE SPECIFICITY: Detected in brain and embryonic stem cells. +Q922X9 ANM7_MOUSE Protein arginine N-methyltransferase 7 (EC 2.1.1.321) (Histone-arginine N-methyltransferase PRMT7) ([Myelin basic protein]-arginine N-methyltransferase PRMT7) 692 78,301 Active site (2); Beta strand (35); Chain (1); Domain (2); Erroneous initiation (1); Helix (26); Modified residue (1); Sequence conflict (2); Turn (4) FUNCTION: Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Specifically mediates the symmetric dimethylation of histone H4 'Arg-3' to form H4R3me2s. Plays a role in gene imprinting by being recruited by CTCFL at the H19 imprinted control region (ICR) and methylating histone H4 to form H4R3me2s, possibly leading to recruit DNA methyltransferases at these sites. May also play a role in embryonic stem cell (ESC) pluripotency. Also able to mediate the arginine methylation of histone H2A and myelin basic protein (MBP) in vitro; the relevance of such results is however unclear in vivo (By similarity). {ECO:0000250, ECO:0000269|PubMed:17048991}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Homodimer and heterodimer. Interacts with PRMT5 and SNRPD3 (By similarity). Interacts with CTCFL. {ECO:0000250, ECO:0000269|PubMed:17048991}. +Q6P9J9 ANO6_MOUSE Anoctamin-6 (Small-conductance calcium-activated nonselective cation channel) (SCAN channel) (Transmembrane protein 16F) 911 106,255 Alternative sequence (2); Chain (1); Glycosylation (6); Mutagenesis (3); Topological domain (9); Transmembrane (8) TRANSMEM 296 316 Helical. {ECO:0000255}.; TRANSMEM 377 397 Helical. {ECO:0000255}.; TRANSMEM 456 476 Helical. {ECO:0000255}.; TRANSMEM 515 535 Helical. {ECO:0000255}.; TRANSMEM 553 573 Helical. {ECO:0000255}.; TRANSMEM 671 691 Helical. {ECO:0000255}.; TRANSMEM 727 747 Helical. {ECO:0000255}.; TRANSMEM 826 846 Helical. {ECO:0000255}. TOPO_DOM 1 295 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 317 376 Extracellular. {ECO:0000255}.; TOPO_DOM 398 455 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 477 514 Extracellular. {ECO:0000255}.; TOPO_DOM 536 552 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 574 670 Extracellular. {ECO:0000255}.; TOPO_DOM 692 726 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 748 825 Extracellular. {ECO:0000255}.; TOPO_DOM 847 911 Cytoplasmic. {ECO:0000255}. FUNCTION: Small-conductance calcium-activated nonselective cation (SCAN) channel which acts as a regulator of phospholipid scrambling in platelets, osteoblasts and fetal thymocytes. Phospholipid scrambling results in surface exposure of phosphatidylserine which in platelets is essential to trigger the clotting system whereas in osteoblasts is essential for the deposition of hydroxyapatite during bone mineralization. Has calcium-dependent phospholipid scramblase activity; scrambles phosphatidylserine, phosphatidylcholine and galactosylceramide. Can generate outwardly rectifying chloride channel currents in airway epithelial cells and Jurkat T lymphocytes. {ECO:0000269|PubMed:21107324, ECO:0000269|PubMed:21908539, ECO:0000269|PubMed:22936354, ECO:0000269|PubMed:23021219, ECO:0000269|PubMed:23532839}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q4KMQ2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q4KMQ2}. Note=Shows an intracellular localization. {ECO:0000250|UniProtKB:Q4KMQ2}. TISSUE SPECIFICITY: Predominant expression seen in epithelial tissues. Also found in skeletal system where it is primarily expressed in osteoblasts. {ECO:0000269|PubMed:20056604, ECO:0000269|PubMed:22936354}. +Q9DCR2 AP3S1_MOUSE AP-3 complex subunit sigma-1 (AP-3 complex subunit sigma-3A) (Adaptor-related protein complex 3 subunit sigma-1) (Sigma-3A-adaptin) (Sigma3A-adaptin) (Sigma-adaptin 3a) 193 21,732 Chain (1); Modified residue (1); Sequence conflict (1) FUNCTION: Part of the AP-3 complex, an adaptor-related complex which is not clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to lysosomes. In concert with the BLOC-1 complex, AP-3 is required to target cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. {ECO:0000269|PubMed:21998198}. SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex. {ECO:0000250}. SUBUNIT: Adaptor protein complex 3 (AP-3) is a heterotetramer composed of two large adaptins (delta-type subunit AP3D1 and beta-type subunit AP3B1 or AP3B2), a medium adaptin (mu-type subunit AP3M1 or AP3M2) and a small adaptin (sigma-type subunit APS1 or AP3S2) (By similarity). AP-3 associates with the BLOC-1 complex. Interacts with AGAP1. {ECO:0000250, ECO:0000269|PubMed:12967569}. +P51910 APOD_MOUSE Apolipoprotein D (Apo-D) (ApoD) 189 21,530 Chain (1); Disulfide bond (2); Glycosylation (2); Modified residue (1); Natural variant (1); Signal peptide (1) FUNCTION: APOD occurs in the macromolecular complex with lecithin-transport and binding of bilin. Appears to be able to transport a variety of ligands in a number of different contexts. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Highest levels of expression in brain, testis, virgin mammary gland and salivary gland. Moderate levels in skeletal muscle, lactating mammary gland and thymus. Low levels in lung and lymph node. No expression in kidney, pancreas, liver or spleen. +Q3V096 ANR42_MOUSE Ankyrin repeat domain-containing protein 42 527 58,533 Alternative sequence (4); Chain (1); Coiled coil (1); Repeat (10); Sequence conflict (5) +Q8BVM7 AL2SB_MOUSE Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 12 protein homolog 383 44,916 Alternative sequence (2); Chain (1); Coiled coil (2); Modified residue (1) SUBCELLULAR LOCATION: Isoform 1: Cytoplasm {ECO:0000269|PubMed:21402173}. Cytoplasmic granule {ECO:0000269|PubMed:21402173}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:21402173}. Note=Expressed in the principal piece of the sperm tail, nearest the sperm head. {ECO:0000269|PubMed:21402173}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm {ECO:0000269|PubMed:21402173}. Cytoplasmic granule {ECO:0000269|PubMed:21402173}. TISSUE SPECIFICITY: Isoform 1 is specific to germ cells of the testis and localizes to the principal piece of the sperm flagellum. Isoform 2 seems to be expressed mainly in somatic cells of the testis, and is not detected in mature spermatozoa (at protein level). Isoform 2 may also be expressed weakly in brain. {ECO:0000269|PubMed:21402173}. +E9Q3E1 AL3B2_MOUSE Aldehyde dehydrogenase family 3 member B2 (EC 1.2.1.3) (Aldehyde dehydrogenase 8) 479 52,983 Active site (2); Chain (1); Lipidation (1); Modified residue (1); Mutagenesis (3); Propeptide (1) Alcohol metabolism; ethanol degradation; acetate from ethanol: step 2/2. FUNCTION: Oxidizes medium and long chain aldehydes into non-toxic fatty acids. {ECO:0000269|PubMed:25286108}. PTM: Geranylgeranylation is important for localization to lipid droplets and enzyme activity. {ECO:0000269|PubMed:25286108}. SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:25286108}. TISSUE SPECIFICITY: Expressed in testis, white adipose tissue, lung, small intestine, kidney, spleen and liver. {ECO:0000269|PubMed:25286108}. +Q62148 AL1A2_MOUSE Retinal dehydrogenase 2 (RALDH 2) (RalDH2) (EC 1.2.1.36) (Aldehyde dehydrogenase family 1 member A2) (Retinaldehyde-specific dehydrogenase type 2) (RALDH(II)) 518 56,626 Active site (2); Chain (1); Erroneous initiation (2); Modified residue (2); Nucleotide binding (1); Site (1) Cofactor metabolism; retinol metabolism. FUNCTION: Recognizes as substrates free retinal and cellular retinol-binding protein-bound retinal. Does metabolize octanal and decanal but does not metabolize citral, benzaldehyde, acetaldehyde and propanal efficiently (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Homotetramer. {ECO:0000250}. +P45376 ALDR_MOUSE Aldose reductase (AR) (EC 1.1.1.21) (Aldehyde reductase) 316 35,732 Active site (1); Binding site (1); Chain (1); Initiator methionine (1); Modified residue (5); Nucleotide binding (2); Sequence conflict (4); Site (1) FUNCTION: Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Monomer. TISSUE SPECIFICITY: Abundant in the testis, skeletal muscle and kidney. +J3QPP8 ALKL1_MOUSE ALK and LTK ligand 1 (Augmentor beta) (Protein FAM150A) 127 14,246 Chain (1); Signal peptide (1) FUNCTION: Ligand for receptor tyrosine kinase LTK and perhaps receptor tyrosine kinase ALK; activation of ALK is reported conflictingly. {ECO:0000250|UniProtKB:Q6UXT8}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q7TS75 AMER1_MOUSE APC membrane recruitment protein 1 (Amer1) (Protein FAM123B) 1132 124,164 Chain (1); Compositional bias (4); Erroneous termination (1); Frameshift (1); Modified residue (1); Sequence caution (1) FUNCTION: Regulator of the canonical Wnt signaling pathway. Acts by specifically binding phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), translocating to the cell membrane and interacting with key regulators of the canonical Wnt signaling pathway, such as components of the beta-catenin destruction complex. Acts both as a positive and negative regulator of the Wnt signaling pathway, depending on the context: acts as a positive regulator by promoting LRP6 phosphorylation. Also acts as a negative regulator by acting as a scaffold protein for the beta-catenin destruction complex and promoting stabilization of Axin at the cell membrane. Promotes CTNNB1 ubiquitination and degradation. Involved in kidney development (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus {ECO:0000250}. Note=Shuttles between nucleus and cytoplasm. Detected in nuclear paraspeckles that are found close to splicing speckles. Translocates to the cell membrane following binding to PtdIns(4,5)P2 (By similarity). {ECO:0000250}. SUBUNIT: Interacts with CTNNB1, AXIN1, LRP6, KEAP1, APC and BTRC. Interacts with SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes containing BTRC and/or FBXW11. Identified in the beta-catenin destruction complex containing CTNNB1, APC, AXIN1 and AXIN2. Interacts with WT1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in kidney. {ECO:0000269|PubMed:17204608}. +Q9D3J8 AMTN_MOUSE Amelotin 213 22,119 Chain (1); Compositional bias (1); Signal peptide (1) FUNCTION: Is a promoter of calcium phosphate mineralization, playing a critical role in the formation of the compact, mineralized, aprismatic enamel surface layer during the maturation stage of amelogenesis. {ECO:0000269|PubMed:16304441, ECO:0000269|PubMed:25407797}. PTM: Phosphorylated by FAM20C in vitro. {ECO:0000250|UniProtKB:Q6UX39}.; PTM: O-glycosylated. {ECO:0000250|UniProtKB:Q3HS82}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16304441}. TISSUE SPECIFICITY: Specifically expressed in maturation-stage ameloblasts. {ECO:0000269|PubMed:16304441, ECO:0000269|PubMed:16787391}. +P19091 ANDR_MOUSE Androgen receptor (Dihydrotestosterone receptor) (Nuclear receptor subfamily 3 group C member 4) 899 98,194 Beta strand (4); Binding site (3); Chain (1); Compositional bias (5); Cross-link (4); DNA binding (1); Domain (1); Helix (11); Modified residue (15); Region (6); Site (2); Turn (1); Zinc finger (2) FUNCTION: Steroid hormone receptors are ligand-activated transcription factors that regulate eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Transcription factor activity is modulated by bound coactivator and corepressor proteins like ZBTB7A that recruits NCOR1 and NCOR2 to the androgen response elements/ARE on target genes, negatively regulating androgen receptor signaling and androgen-induced cell proliferation. Transcription activation is also down-regulated by NR0B2. Activated, but not phosphorylated, by HIPK3 and ZIPK/DAPK3. {ECO:0000250|UniProtKB:P10275, ECO:0000250|UniProtKB:P15207}. PTM: Phosphorylated in prostate cancer cells in response to several growth factors including EGF. Phosphorylation is induced by c-Src kinase (CSK). Tyr-514 is one of the major phosphorylation sites and an increase in phosphorylation and Src kinase activity is associated with prostate cancer progression (By similarity). Phosphorylation by TNK2 enhances the DNA-binding and transcriptional activity. Phosphorylation at Ser-61 by CDK9 regulates AR promoter selectivity and cell growth. Phosphorylation by PAK6 leads to AR-mediated transcription inhibition (By similarity). {ECO:0000250|UniProtKB:P10275}.; PTM: Sumoylated on Lys-381 (major) and Lys-500 (By similarity). Ubiquitinated. Deubiquitinated by USP26 (By similarity). 'Lys-6' and 'Lys-27'-linked polyubiquitination by RNF6 modulates AR transcriptional activity and specificity (By similarity). {ECO:0000250|UniProtKB:P10275}.; PTM: Palmitoylated by ZDHHC7 and ZDHHC21. Palmitoylation is required for plasma membrane targeting and for rapid intracellular signaling via ERK and AKT kinases and cAMP generation (By similarity). {ECO:0000250|UniProtKB:P10275}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P10275}. Cytoplasm {ECO:0000250|UniProtKB:P10275}. Note=Detected at the promoter of target genes. Predominantly cytoplasmic in unligated form but translocates to the nucleus upon ligand-binding. Can also translocate to the nucleus in unligated form in the presence of RACK1. {ECO:0000250|UniProtKB:P10275}. SUBUNIT: Binds DNA as a homodimer. Part of a ternary complex containing AR, EFCAB6/DJBP and PARK7. Interacts with HIPK3 and NR0B2 in the presence of androgen. The ligand binding domain interacts with KAT7/HBO1 in the presence of dihydrotestosterone. Interacts with EFCAB6/DJBP, PELP1, PQBP1, RANBP9, SPDEF, SRA1, TGFB1I1, ZNF318 and RREB1. The AR N-terminal poly-Gln region binds Ran resulting in enhancement of AR-mediated transactivation. Ran-binding decreases as the poly-Gln length increases. Interacts with ZMIZ1/ZIMP10 and ZMIZ2/ZMIP7 which both enhance its transactivation activity. Interacts with RBAK. Interacts via the ligand-binding domain with LXXLL and FXXLF motifs from NCOA1, NCOA2, NCOA3, NCOA4 and MAGEA11. Interacts with HIP1 (via coiled coil domain). Interacts with SLC30A9 and RAD54L2/ARIP4. Interacts with MACROD1. Interacts (via ligand-binding domain) with TRIM68. Interacts with TNK2. Interacts with USP26. Interacts with RNF6. Interacts (regulated by RNF6 probably through polyubiquitination) with RNF14; regulates AR transcriptional activity. Interacts with PRMT2 and TRIM24. Interacts with RACK1. Interacts with RANBP10; this interaction enhances hormone-induced AR transcriptional activity. Interacts with PRPF6 in a hormone-independent way; this interaction enhances hormone-induced AR transcriptional activity. Interacts with STK4/MST1. Interacts with ZIPK/DAPK3. Interacts with LPXN. Interacts with MAK. Part of a complex containing AR, MAK and NCOA3. Interacts with CRY1. Interacts with CCAR1 and GATA2 (By similarity). Interacts with BUD31 (By similarity). Interacts with ARID4A (PubMed:23487765). Interacts with ARID4B (PubMed:23487765). Interacts (via NR LBD domain) with ZBTB7A; the interaction is direct and androgen-dependent (By similarity). Interacts with NCOR1 (By similarity). Interacts with NCOR2 (By similarity). {ECO:0000250|UniProtKB:P10275, ECO:0000250|UniProtKB:P15207, ECO:0000269|PubMed:12058073, ECO:0000269|PubMed:15199138, ECO:0000269|PubMed:15882980, ECO:0000269|PubMed:15988012, ECO:0000269|PubMed:16446156, ECO:0000269|PubMed:17911242, ECO:0000269|PubMed:22170608, ECO:0000269|PubMed:23487765}. DOMAIN: Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain. In the presence of bound steroid the ligand-binding domain interacts with the N-terminal modulating domain, and thereby activates AR transcription factor activity. Agonist binding is required for dimerization and binding to target DNA. The transcription factor activity of the complex formed by ligand-activated AR and DNA is modulated by interactions with coactivator and corepressor proteins. Interaction with RANBP9 is mediated by both the N-terminal domain and the DNA-binding domain. Interaction with EFCAB6/DJBP is mediated by the DNA-binding domain (By similarity). {ECO:0000250}. +P70180 ANPRC_MOUSE Atrial natriuretic peptide receptor 3 (Atrial natriuretic peptide clearance receptor) (Atrial natriuretic peptide receptor type C) (ANP-C) (ANPR-C) (NPR-C) (EF-2) 536 59,808 Binding site (3); Chain (1); Disulfide bond (3); Glycosylation (3); Natural variant (2); Propeptide (1); Sequence conflict (8); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 479 499 Helical. {ECO:0000255}. TOPO_DOM 41 478 Extracellular. {ECO:0000255}.; TOPO_DOM 500 536 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for the natriuretic peptide hormones, binding with similar affinities atrial natriuretic peptide NPPA/ANP, brain natriuretic peptide NPPB/BNP, and C-type natriuretic peptide NPPC/CNP (PubMed:10377427, PubMed:17951249). May function as a clearance receptor for NPPA, NPPB and NPPC, regulating their local concentrations and effects (PubMed:10377427, PubMed:17951249). May regulate diuresis, blood pressure and skeletal development (PubMed:10377427). Does not have guanylate cyclase activity (PubMed:10377427). {ECO:0000269|PubMed:10377427, ECO:0000269|PubMed:17951249}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Homodimer; disulfide-linked (By similarity). Interacts with OSTN (PubMed:17951249). {ECO:0000250|UniProtKB:P17342, ECO:0000269|PubMed:17951249}. DISEASE: Note=Defects in Npr3 are the cause of a number of skeletal-overgrowth phenotypes, Longjohn (Lgj), Longjohn-2J (Lgj-2J) and Strigosus (Stri). These are all recessive conditions characterized by an elongated body, thoracic kyphosis, arachnodactyly, and sacral and/or tail kinks, but no significant changes in craniofacial structures (PubMed:10468599). {ECO:0000269|PubMed:10468599}. +Q9R045 ANGL2_MOUSE Angiopoietin-related protein 2 (Angiopoietin-like protein 2) 493 57,105 Chain (1); Coiled coil (2); Disulfide bond (2); Domain (1); Glycosylation (2); Sequence conflict (1); Signal peptide (1) FUNCTION: Induces sprouting in endothelial cells through an autocrine and paracrine action. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed in heart, tongue, lung and skeletal muscle. Also found in lower levels in kidney, epididymis and testis. +Q9WV76 AP4B1_MOUSE AP-4 complex subunit beta-1 (AP-4 adaptor complex subunit beta) (Adaptor-related protein complex 4 subunit beta-1) (Beta subunit of AP-4) (Beta4-adaptin) 738 82,976 Chain (1); Region (2); Sequence conflict (25) FUNCTION: Component of the adaptor protein complex 4 (AP-4). Adaptor protein complexes are vesicle coat components involved both in vesicle formation and cargo selection. They control the vesicular transport of proteins in different trafficking pathways. AP-4 forms a non clathrin-associated coat on vesicles departing the trans-Golgi network (TGN) and may be involved in the targeting of proteins from the trans-Golgi network (TGN) to the endosomal-lysosomal system (By similarity). It is also involved in protein sorting to the basolateral membrane in epithelial cells and the proper asymmetric localization of somatodendritic proteins in neurons (PubMed:18341993). AP-4 is involved in the recognition and binding of tyrosine-based sorting signals found in the cytoplasmic part of cargos, but may also recognize other types of sorting signal (By similarity). {ECO:0000250|UniProtKB:Q9Y6B7, ECO:0000269|PubMed:18341993}. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q9Y6B7}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9Y6B7}. SUBUNIT: Adaptor protein complex 4 (AP-4) is a heterotetramer composed of two large adaptins (epsilon-type subunit AP4E1 and beta-type subunit AP4B1), a medium adaptin (mu-type subunit AP4M1) and a small adaptin (sigma-type AP4S1). Interacts with TEPSIN; this interaction requires the presence of a functional AP-4 complex (By similarity). Interacts with GRIA2; probably indirect it mediates the somatodendritic localization of GRIA2 in neurons (PubMed:18341993). {ECO:0000250|UniProtKB:Q9Y6B7, ECO:0000269|PubMed:18341993}. +Q9JIF0 ANM1_MOUSE Protein arginine N-methyltransferase 1 (EC 2.1.1.319) (Histone-arginine N-methyltransferase PRMT1) 371 42,436 Active site (2); Alternative sequence (2); Binding site (5); Chain (1); Cross-link (1); Domain (1); Modified residue (5); Mutagenesis (9) FUNCTION: Arginine methyltransferase that methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues present in proteins such as ESR1, histone H2, H3 and H4, ILF3, HNRNPA1, HNRNPD, NFATC2IP, SUPT5H, TAF15, EWS, HABP4 and SERBP1 (PubMed:15327772, PubMed:19858291). Constitutes the main enzyme that mediates monomethylation and asymmetric dimethylation of histone H4 'Arg-4' (H4R3me1 and H4R3me2a, respectively), a specific tag for epigenetic transcriptional activation (By similarity). Methylates H4R3 in genes involved in glioblastomagenesis in a CHTOP- and/or TET1-dependent manner (By similarity). May be involved in the regulation of TAF15 transcriptional activity, act as an activator of estrogen receptor (ER)-mediated transactivation, play a key role in neurite outgrowth and act as a negative regulator of megakaryocytic differentiation, by modulating p38 MAPK pathway (By similarity). Methylates RBM15, promoting ubiquitination and degradation of RBM15 (By similarity). Methylates CHTOP and this methylation is critical for its 5-hydroxymethylcytosine (5hmC)-binding activity (PubMed:19858291). {ECO:0000250|UniProtKB:Q99873, ECO:0000269|PubMed:15327772, ECO:0000269|PubMed:19858291}. PTM: Polyubiquitinated at Lys-145 by the SCF(FBXL17) complex, leading to its subsequent degradation (PubMed:28883095). Ubiquitination is regulated by acetylation at Lys-228 and Lys-233 (PubMed:28883095). {ECO:0000269|PubMed:28883095}.; PTM: Acetylation at Lys-228 and Lys-233 regulates ubiquitination by the SCF(FBXL17) complex. Acetylated at Lys-233 by p300/EP300. Deacetylated at Lys-228 and Lys-233 by SIRT1. {ECO:0000269|PubMed:28883095}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19858291}. Nucleus, nucleoplasm {ECO:0000269|PubMed:22872859}. Cytoplasm, cytosol {ECO:0000269|PubMed:19858291}. Cytoplasm {ECO:0000269|PubMed:19858291}. Note=Mostly found in the cytoplasm (PubMed:19858291). Colocalizes with CHTOP within the nucleus (PubMed:19858291). Low levels detected also in the chromatin fraction (PubMed:22872859). {ECO:0000269|PubMed:19858291, ECO:0000269|PubMed:22872859}. SUBUNIT: Homodimer and heterodimer with PRMT8. Homooctamer; individual homodimers associates to form a homooctamer. Individual homodimers can associate to form a homohexamer. Interacts with BTG1, BTG2 and IFNAR1. Interacts with ILF3 and SUPT5H. Interacts with and methylates FOXO1, leading to the nuclear retention of FOXO1 and the stimulation of FOXO1 transcriptional activity. Methylation of FOXO1 is increased upon oxidative stress (By similarity). Interacts with NFATC2IP. Interacts with and methylates CHTOP, thereby enabling the interaction of CHTOP with the 5FMC complex. Interacts with and probably methylates ATXN2L (By similarity). Component of the methylosome, a 20S complex containing at least CLNS1A/pICln, PRMT5/SKB1, WDR77/MEP50, PRMT1 and ERH (By similarity). Interacts with DHX9 (via RGG region) (By similarity). Interacts (via N-terminus) with HABP4 (By similarity). {ECO:0000250|UniProtKB:Q99873, ECO:0000269|PubMed:15327772, ECO:0000269|PubMed:19858291, ECO:0000269|PubMed:22872859}. +Q61313 AP2B_MOUSE Transcription factor AP-2-beta (AP2-beta) (Activating enhancer-binding protein 2-beta) 459 50,373 Chain (1); Compositional bias (1); Cross-link (1); Erroneous initiation (1); Modified residue (1); Region (1) FUNCTION: Sequence-specific DNA-binding protein that interacts with inducible viral and cellular enhancer elements to regulate transcription of selected genes. AP-2 factors bind to the consensus sequence 5'-GCCNNNGGC-3' and activate genes involved in a large spectrum of important biological functions including proper eye, face, body wall, limb and neural tube development. They also suppress a number of genes including MCAM/MUC18, C/EBP alpha and MYC. AP-2-beta appears to be required for normal face and limb development and for proper terminal differentiation and function of renal tubular epithelia. {ECO:0000250|UniProtKB:Q92481}. PTM: Sumoylated on Lys-21; which inhibits transcriptional activity. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Binds DNA as a dimer. Can form homodimers or heterodimers with other AP-2 family members. Interacts with CITED4. Interacts with UBE2I. Interacts with KCTD1; this interaction represses transcription activation. Interacts with CITED2 (via C-terminus); the interaction stimulates TFAP2B-transcriptional activity (By similarity). {ECO:0000250|UniProtKB:Q92481}. +Q80VM7 ANR24_MOUSE Ankyrin repeat domain-containing protein 24 985 106,238 Chain (1); Coiled coil (1); Compositional bias (1); Repeat (5); Sequence conflict (1) +O88888 APBA3_MOUSE Amyloid-beta A4 precursor protein-binding family A member 3 (Adapter protein X11gamma) (Neuron-specific X11L2 protein) (Neuronal Munc18-1-interacting protein 3) (Mint-3) 571 60,718 Chain (1); Domain (3); Modified residue (3); Sequence conflict (2) FUNCTION: May modulate processing of the amyloid-beta precursor protein (APP) and hence formation of APP-beta. May enhance the activity of HIF1A in macrophages by inhibiting the activity of HIF1AN (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}. SUBUNIT: Binds to the cytoplasmic domain of amyloid protein (APP). Interacts with HIF1AN (via N-terminus) (By similarity). Interacts with NECAB3; seems to mediate the interaction between NECAB3 and HIF1AN (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O96018}. DOMAIN: Composed of an N-terminal domain, a middle phosphotyrosine-binding domain (PID/PTB) that mediates binding with the cytoplasmic domain of the amyloid-beta precursor protein, and two C-terminal PDZ domains thought to attach proteins to the plasma membrane. TISSUE SPECIFICITY: Ubiquitous. +Q9R144 ANM2_MOUSE Protein arginine N-methyltransferase 2 (EC 2.1.1.319) (Histone-arginine N-methyltransferase PRMT2) 448 50,476 Active site (2); Binding site (5); Chain (1); Domain (2); Modified residue (2); Region (3) FUNCTION: Arginine methyltransferase that methylates the guanidino nitrogens of arginyl residues in proteins such as STAT3, FBL, histone H4. May inhibit NF-kappa-B transcription, and promote apoptosis. Represses E2F1 transcriptional activity (in a RB1-dependent manner). Has a negative regulation effect on G1 to S transition of mitotic cell cycle. Involved in growth regulation. Acts as a coactivator (with NCOA2) of the androgen receptor (AR)-mediated transactivation. Acts as a coactivator (with estrogen) of estrogen receptor (ER)-mediated transactivation. Enhances PGR, PPARG, RARA-mediated transactivation. {ECO:0000269|PubMed:16616919, ECO:0000269|PubMed:16648481, ECO:0000269|PubMed:20708585, ECO:0000269|PubMed:20798359}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Translocates from the cytoplasm to the nucleus, after hormone exposure. {ECO:0000250}. SUBUNIT: Self-associates (By similarity). Interacts with HNRNPUL1. Interacts with NFKBIA (By similarity). Interacts with NCOA6 coactivator. Interacts (via SH3 domain) with PRMT8. Interacts with AR. Interacts with ESR1, ESR2, PGR, PPARG, RARA, RXRA and THRB (By similarity). Interacts with RB1 and E2F1. {ECO:0000250, ECO:0000269|PubMed:16616919}. TISSUE SPECIFICITY: Expressed in liver, pancreas, lung, brain, skeletal muscle, heart, muscle and fat. {ECO:0000269|PubMed:16616919}. +Q505D1 ANR28_MOUSE Serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit A (PP6-ARS-A) (Serine/threonine-protein phosphatase 6 regulatory subunit ARS-A) (Ankyrin repeat domain-containing protein 28) (Phosphatase interactor targeting protein hnRNP K) (PITK) 1053 112,898 Chain (1); Compositional bias (1); Modified residue (2); Repeat (27) FUNCTION: Putative regulatory subunit of protein phosphatase 6 (PP6) that may be involved in the recognition of phosphoprotein substrates. Involved in the PP6-mediated dephosphorylation of NFKBIE opposing its degradation in response to TNF-alpha. Selectively inhibits the phosphatase activity of PPP1C. Targets PPP1C to modulate HNRPK phosphorylation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm. Note=Seems to be excluded from nucleoli. {ECO:0000250}. SUBUNIT: Protein phosphatase 6 (PP6) holoenzyme is proposed to be a heterotrimeric complex formed by the catalytic subunit, a SAPS domain-containing subunit (PP6R) and an ankyrin repeat-domain containing regulatory subunit (ARS). Interacts with PPP1C and HNRPK. Interacts with PPP6C, PPP6R1 and PPP6R3 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed (at protein level). {ECO:0000269|PubMed:16564677}. +O35936 ALOX8_MOUSE Arachidonate 8S-lipoxygenase (8-LOX) (8S-LOX) (EC 1.13.11.-) (15-lipoxygenase 2) (15-LOX-2) (Arachidonate 15-lipoxygenase B) (15-LOX-B) 677 76,230 Chain (1); Domain (2); Metal binding (12); Mutagenesis (4); Natural variant (6) Lipid metabolism; hydroperoxy eicosatetraenoic acid biosynthesis. FUNCTION: Non-heme iron-containing dioxygenase that catalyzes the stereo-specific peroxidation of free and esterified polyunsaturated fatty acids generating a spectrum of bioactive lipid mediators. Catalyzes the peroxidation of arachidonate and linoleate into (8S)-HPETE and (9S)-HPODE respectively. From arachidonate mainly produces (8S)-HPETE and in addition, minor products derived from (8S)-HPETE itself that may include leukotriene A4 and 8,15-diHPETE. With arachidonate as substrate, has no detectable 15S-lipoxygenase activity and only displays a 8S-lipoxygenase activity. However, it may have a 15S-lipoxygenase activity with (8S)-HPETE to produce (8S,15S)-diHPETE. May also catalyze (15S)-HPETE peroxidation to produce 8,15-diHPETE. May play a role in keratinocyte differentiation through activation of the peroxisome proliferator activated receptor signaling pathway. {ECO:0000269|PubMed:10625675, ECO:0000269|PubMed:10965849, ECO:0000269|PubMed:16143298, ECO:0000269|PubMed:9305900}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Predominantly cytosolic; becomes enriched at membranes upon calcium binding. {ECO:0000250}. DOMAIN: The PLAT domain can bind calcium ions; this promotes association with membranes. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in epidermis and brain. No expression found in heart, spleen, liver, skeletal muscle, kidney or testis. {ECO:0000269|PubMed:9305900, ECO:0000269|PubMed:9518531}. +O35137 ALX4_MOUSE Homeobox protein aristaless-like 4 (ALX-4) 399 42,763 Chain (1); DNA binding (1); Modified residue (1); Motif (1); Natural variant (1) FUNCTION: Transcription factor involved in skull and limb development. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Binds DNA. TISSUE SPECIFICITY: Expressed in osteoblasts. Not expressed in brain, heart, intestine, kidney, liver, muscle, spleen and testis. DISEASE: Note=Defects in Alx4 are the cause of Strong luxoid (lst) phenotype. At heterozygosity lst is characterized by preaxial abnormalities of the hindfeet and, very rarely, of the forefeet. Homozygotes show preaxial polydactyly of all four limbs, reductions and duplications of the radius, absence of the tibia, craniofacial defects, reduction of the pubis, and dorsal alopecia. {ECO:0000269|PubMed:9636085}. +Q99JB7 AMNLS_MOUSE Protein amnionless 458 48,696 Chain (1); Domain (1); Glycosylation (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 363 383 Helical. {ECO:0000255}. TOPO_DOM 20 362 Extracellular. {ECO:0000255}.; TOPO_DOM 384 458 Cytoplasmic. {ECO:0000255}. FUNCTION: Necessary for efficient absorption of vitamin B12 (By similarity). Required for normal CUBN-mediated protein transport in the kidney (PubMed:15342463). May direct the production of trunk mesoderm during development by modulating a bone morphogenetic protein (BMP) signaling pathway in the underlying visceral endoderm. {ECO:0000250|UniProtKB:Q9BXJ7, ECO:0000269|PubMed:11279523, ECO:0000269|PubMed:15342463, ECO:0000269|PubMed:9851841}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:15342463}; Single-pass type I membrane protein {ECO:0000305}. Cell membrane {ECO:0000250|UniProtKB:Q9BXJ7}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9BXJ7}. Endosome {ECO:0000250|UniProtKB:Q9BXJ7}. Membrane, coated pit {ECO:0000250|UniProtKB:Q9BXJ7}. SUBUNIT: Interacts with CUBN/cubilin. {ECO:0000269|PubMed:15342463}. TISSUE SPECIFICITY: Expressed in polarized epithelial cells which are specialized in resorption or transport, specifically kidney proximal tubules and intestinal epithelium. {ECO:0000269|PubMed:15342463}. +Q9DAZ9 ANCHR_MOUSE Abscission/NoCut checkpoint regulator (ANCHR) (Zinc finger FYVE domain-containing protein 19) 389 43,272 Beta strand (10); Chain (1); Coiled coil (1); Compositional bias (2); Cross-link (1); Helix (2); Modified residue (3); Motif (2); Natural variant (6); Turn (7); Zinc finger (1) FUNCTION: Key regulator of abscission step in cytokinesis: part of the cytokinesis checkpoint, a process required to delay abscission to prevent both premature resolution of intercellular chromosome bridges and accumulation of DNA damage. Together with CHMP4C, required to retain abscission-competent VPS4 (VPS4A and/or VPS4B) at the midbody ring until abscission checkpoint signaling is terminated at late cytokinesis. Deactivation of AURKB results in dephosphorylation of CHMP4C followed by its dissociation from ZFYVE19/ANCHR and VPS4 and subsequent abscission (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q96K21}. Cleavage furrow {ECO:0000250|UniProtKB:Q96K21}. Midbody, Midbody ring {ECO:0000250|UniProtKB:Q96K21}. Note=Localizes mainly on centrosomes in interphase and early mitosis. Localizes at the cleavage furrow and midbody ring in late mitosis and cytokinesis. {ECO:0000250|UniProtKB:Q96K21}. SUBUNIT: Interacts (via MIM1-B) with VPS4A; interaction takes place at the midbody ring following cytokinesis checkpoint activation. {ECO:0000250}. DOMAIN: The FYVE-type zinc finger mediates binding to phosphatidylinositol-3-phosphate (PtdIns(3)P). {ECO:0000250}.; DOMAIN: The MIM1-B motif mediates interaction with VPS4A. {ECO:0000250}. +O35381 AN32A_MOUSE Acidic leucine-rich nuclear phosphoprotein 32 family member A (Acidic nuclear phosphoprotein pp32) (Leucine-rich acidic nuclear protein) (LANP) (Potent heat-stable protein phosphatase 2A inhibitor I1PP2A) 247 28,538 Beta strand (7); Chain (1); Compositional bias (1); Domain (1); Helix (7); Modified residue (3); Region (2); Repeat (4); Sequence conflict (1); Turn (1) FUNCTION: Implicated in a number of cellular processes, including proliferation, differentiation, caspase-dependent and caspase-independent apoptosis, suppression of transformation (tumor suppressor), inhibition of protein phosphatase 2A, regulation of mRNA trafficking and stability in association with ELAVL1, and inhibition of acetyltransferases as part of the INHAT (inhibitor of histone acetyltransferases) complex. Plays a role in E4F1-mediated transcriptional repression. {ECO:0000269|PubMed:17557114}. PTM: Phosphorylated on serine residues. {ECO:0000250}.; PTM: Some glutamate residues are glycylated by TTLL8. This modification occurs exclusively on glutamate residues and results in a glycine chain on the gamma-carboxyl group. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12807913}. Cytoplasm {ECO:0000269|PubMed:12807913}. Endoplasmic reticulum {ECO:0000250}. Note=Shuttles between nucleus and cytoplasm. Translocates to the cytoplasm during the process of neuritogenesis. SUBUNIT: Component of the SET complex, composed of at least ANP32A, APEX1, HMGB2, NME1, SET and TREX1. Directly interacts with SET. Interacts with ATXN1/SCA1. Interacts with MAP1B. Interacts with ELAVL1. Part of the INHAT (inhibitor of histone acetyltransferases) complex. Interacts with E4F1. {ECO:0000269|PubMed:12807913, ECO:0000269|PubMed:17557114, ECO:0000269|PubMed:9353121}. TISSUE SPECIFICITY: Predominantly expressed in the cerebellum. Expressed also in cortex, lung, skeletal muscle, gastrointestinal tract, spleen, liver and heart. {ECO:0000269|PubMed:15895553}. +Q8R0Z6 ANGL6_MOUSE Angiopoietin-related protein 6 (Angiopoietin-like protein 6) (Angiopoietin-related growth factor) 457 51,095 Chain (1); Coiled coil (2); Disulfide bond (2); Domain (1); Glycosylation (1); Signal peptide (1) FUNCTION: May play a role in the wound healing process. May promote epidermal proliferation, remodeling and regeneration. May promote the chemotactic activity of endothelial cells and induce neovascularization. May counteract high-fat diet-induced obesity and related insulin resistance through increased energy expenditure. {ECO:0000269|PubMed:12871997, ECO:0000269|PubMed:14764539, ECO:0000269|PubMed:15778720}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Highly expressed in the liver, specifically in hepatocytes, and weakly in the heart. Expressed in hematopoietic cells, platelets and mast cells, and detected at wounded skin. {ECO:0000269|PubMed:12871997}. +Q8R1Q3 ANGL7_MOUSE Angiopoietin-related protein 7 (Angiopoietin-like protein 7) 337 39,014 Chain (1); Coiled coil (1); Disulfide bond (2); Domain (1); Glycosylation (4); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +P61110 ANRE_MOUSE Kidney androgen-regulated protein (ARP) (KAP) 121 13,263 Chain (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Kidney, submaxillary gland, urine. +Q07076 ANXA7_MOUSE Annexin A7 (Annexin VII) (Annexin-7) (Synexin) 463 49,925 Chain (1); Modified residue (1); Region (2); Repeat (7); Sequence conflict (1) FUNCTION: Calcium/phospholipid-binding protein which promotes membrane fusion and is involved in exocytosis. SUBUNIT: Interacts with PDCD6. {ECO:0000250}. DOMAIN: A pair of annexin repeats may form one binding site for calcium and phospholipid. +Q8BVM2 ANTRL_MOUSE Anthrax toxin receptor-like 641 70,443 Chain (1); Compositional bias (1); Domain (1); Metal binding (3); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 364 384 Helical. {ECO:0000255}. TOPO_DOM 28 363 Extracellular. {ECO:0000255}.; TOPO_DOM 385 641 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +P22892 AP1G1_MOUSE AP-1 complex subunit gamma-1 (Adaptor protein complex AP-1 subunit gamma-1) (Adaptor-related protein complex 1 subunit gamma-1) (Clathrin assembly protein complex 1 gamma-1 large chain) (Gamma-adaptin) (Gamma1-adaptin) (Golgi adaptor HA1/AP1 adaptin subunit gamma-1) 822 91,350 Beta strand (12); Chain (1); Domain (1); Helix (41); Initiator methionine (1); Mutagenesis (3); Turn (4) FUNCTION: Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasmic vesicle, clathrin-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex. SUBUNIT: Adaptor protein complex 1 (AP-1) is a heterotetramer composed of two large adaptins (gamma-type subunit AP1G1 and beta-type subunit AP1B1), a medium adaptin (mu-type subunit AP1M1 or AP1M2) and a small adaptin (sigma-type subunit AP1S1 or AP1S2 or AP1S3) (By similarity). Binds RABEP1 (By similarity). Binds EPS15 and SYNRG. Interacts (via GAE domain) with AP1AR (via coiled-coil domain) (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. +O88512 AP1G2_MOUSE AP-1 complex subunit gamma-like 2 (Gamma2-adaptin) (G2ad) 791 87,863 Chain (1); Domain (1); Sequence conflict (1) FUNCTION: May function in protein sorting in late endosomes or multivesucular bodies (MVBs). Involved in MVB-assisted maturation of hepatitis B virus (HBV). {ECO:0000250|UniProtKB:O75843}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:O75843}; Peripheral membrane protein {ECO:0000250|UniProtKB:O75843}; Cytoplasmic side {ECO:0000250|UniProtKB:O75843}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:O75843}; Peripheral membrane protein {ECO:0000250|UniProtKB:O75843}. Endosome membrane {ECO:0000250|UniProtKB:O75843}; Peripheral membrane protein {ECO:0000250|UniProtKB:O75843}. Note=Mainly localized to perinuclear vesicular structures. Colocalizes with HBV major surface antigen L and HBV core protein C in CD63-containing compartments. Colocalizes with HBV major surface antigen L to cis-Golgi-like structures. {ECO:0000250|UniProtKB:O75843}. SUBUNIT: Probably interacts with AP1S1/Sigma1A-adaptin AP1S2/Sigma1B-adaptin. Probably does not interact with APB1. Interacts with HBV major surface antigen L. Interacts with HBV core protein C in a ubiquitin-dependent manner. Binds ubiquitin. {ECO:0000250|UniProtKB:O75843}. TISSUE SPECIFICITY: Widely expressed. +Q9D742 AP5S1_MOUSE AP-5 complex subunit sigma-1 (Adaptor-related protein complex 5 sigma subunit) (Sigma5) 170 18,806 Chain (1) FUNCTION: As part of AP-5, a probable fifth adaptor protein complex it may be involved in endosomal transport. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol. Late endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Lysosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. SUBUNIT: Probably part of the adaptor protein complex 5 (AP-5) a tetramer composed of AP5B1, AP5M1, AP5S1 and AP5Z1. Interacts with ZFYVE26 and SPG11 (By similarity). {ECO:0000250}. +Q9D7N9 APMAP_MOUSE Adipocyte plasma membrane-associated protein (Protein DD16) 415 46,434 Chain (1); Glycosylation (1); Initiator methionine (1); Modified residue (2); Topological domain (2); Transmembrane (1) TRANSMEM 40 60 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 2 39 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 61 415 Extracellular. {ECO:0000255}. FUNCTION: Exhibits strong arylesterase activity with beta-naphthyl acetate and phenyl acetate (By similarity). May play a role in adipocyte differentiation. {ECO:0000250}. PTM: Glycosylated in vitro. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Strongly expressed in adipose tissue. Highly expressed in liver, heart, and kidney. Expressed at intermediate level in brain and lung. Weakly expressed in spleen, skeletal muscle and testis. +P28352 APEX1_MOUSE DNA-(apurinic or apyrimidinic site) lyase (EC 3.1.-.-) (EC 4.2.99.18) (APEX nuclease) (APEN) (Apurinic-apyrimidinic endonuclease 1) (AP endonuclease 1) (REF-1) (Redox factor-1) [Cleaved into: DNA-(apurinic or apyrimidinic site) lyase, mitochondrial] 317 35,490 Active site (2); Chain (2); Disulfide bond (1); Initiator methionine (1); Metal binding (5); Modified residue (13); Motif (2); Mutagenesis (3); Region (3); Site (5) FUNCTION: Multifunctional protein that plays a central role in the cellular response to oxidative stress. The two major activities of APEX1 are DNA repair and redox regulation of transcriptional factors. Functions as a apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents. Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends. Does also incise at AP sites in the DNA strand of DNA/RNA hybrids, single-stranded DNA regions of R-loop structures, and single-stranded RNA molecules. Has a 3'-5' exoribonuclease activity on mismatched deoxyribonucleotides at the 3' termini of nicked or gapped DNA molecules during short-patch BER. Possesses a DNA 3' phosphodiesterase activity capable of removing lesions (such as phosphoglycolate) blocking the 3' side of DNA strand breaks. May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation. Acts as a loading factor for POLB onto non-incised AP sites in DNA and stimulates the 5'-terminal deoxyribose 5'-phosphate (dRp) excision activity of POLB. Plays a role in the protection from granzymes-mediated cellular repair leading to cell death. Also involved in the DNA cleavage step of class switch recombination (CSR). On the other hand, APEX1 also exerts reversible nuclear redox activity to regulate DNA binding affinity and transcriptional activity of transcriptional factors by controlling the redox status of their DNA-binding domain, such as the FOS/JUN AP-1 complex after exposure to IR. Involved in calcium-dependent down-regulation of parathyroid hormone (PTH) expression by binding to negative calcium response elements (nCaREs). Together with HNRNPL or the dimer XRCC5/XRCC6, associates with nCaRE, acting as an activator of transcriptional repression. Stimulates the YBX1-mediated MDR1 promoter activity, when acetylated at Lys-6 and Lys-7, leading to drug resistance. Acts also as an endoribonuclease involved in the control of single-stranded RNA metabolism. Plays a role in regulating MYC mRNA turnover by preferentially cleaving in between UA and CA dinucleotides of the MYC coding region determinant (CRD). In association with NMD1, plays a role in the rRNA quality control process during cell cycle progression. Associates, together with YBX1, on the MDR1 promoter. Together with NPM1, associates with rRNA. Binds DNA and RNA. {ECO:0000269|PubMed:18025127, ECO:0000269|PubMed:19556307}. PTM: Phosphorylated. Phosphorylation by kinase PKC or casein kinase CK2 results in enhanced redox activity that stimulates binding of the FOS/JUN AP-1 complex to its cognate binding site. AP-endodeoxyribonuclease activity is not affected by CK2-mediated phosphorylation (By similarity). Phosphorylation of Thr-232 by CDK5 in response to MPP(+)/MPTP (1-methyl-4-phenylpyridinium) reduces AP-endodeoxyribonuclease activity resulting in accumulation of DNA damage and contributing to neuronal death. {ECO:0000250, ECO:0000269|PubMed:20473298}.; PTM: Acetylated on Lys-6 and Lys-7. Acetylation is increased by the transcriptional coactivator EP300 acetyltransferase, genotoxic agents like H(2)O(2) and methyl methanesulfonate (MMS). Acetylation increases its binding affinity to the negative calcium response element (nCaRE) DNA promoter. The acetylated form induces a stronger binding of YBX1 to the Y-box sequence in the MDR1 promoter than the unacetylated form. Deacetylated on lysines. Lys-6 and Lys-7 are deacetylated by SIRT1 (By similarity). {ECO:0000250}.; PTM: Cleaved at Lys-30 by granzyme A to create the mitochondrial form; leading in reduction of binding to DNA, AP endodeoxyribonuclease activity, redox activation of transcription factors and to enhanced cell death. Cleaved by granzyme K; leading to intracellular ROS accumulation and enhanced cell death after oxidative stress (By similarity). {ECO:0000250}.; PTM: Cys-64 and Cys-92 are nitrosylated in response to nitric oxide (NO) and lead to the exposure of the nuclear export signal (NES). {ECO:0000250}.; PTM: Ubiquitinated by MDM2; leading to translocation to the cytoplasm and proteasomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Nucleus, nucleolus {ECO:0000250}. Nucleus speckle {ECO:0000255|PROSITE-ProRule:PRU00764}. Endoplasmic reticulum {ECO:0000250}. Cytoplasm. Note=Colocalized with SIRT1 in the nucleus. Colocalized with YBX1 in nuclear speckles after genotoxic stress. Together with OGG1 is recruited to nuclear speckles in UVA-irradiated cells. Colocalized with nucleolin and NPM1 in the nucleolus. Its nucleolar localization is cell cycle dependent and requires active rRNA transcription. Colocalized with calreticulin in the endoplasmic reticulum. Translocation from the nucleus to the cytoplasm is stimulated in presence of nitric oxide (NO) and function in a CRM1-dependent manner, possibly as a consequence of demasking a nuclear export signal (amino acid position 63-79). S-nitrosylation at Cys-92 and Cys-309 regulates its nuclear-cytosolic shuttling. Ubiquitinated form is localized predominantly in the cytoplasm. Detected in the cytoplasm of B-cells stimulated to switch (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: DNA-(apurinic or apyrimidinic site) lyase, mitochondrial: Mitochondrion. Note=Translocation from the cytoplasm to the mitochondria is mediated by ROS signaling and cleavage mediated by granzyme A. Tom20-dependent translocated mitochondrial APEX1 level is significantly increased after genotoxic stress (By similarity). The cleaved APEX2 is only detected in mitochondria. {ECO:0000250}. SUBUNIT: Monomer. Homodimer; disulfide-linked. Component of the SET complex, composed of at least APEX1, SET, ANP32A, HMGB2, NME1 and TREX1. Associates with the dimer XRCC5/XRCC6 in a DNA-dependent manner. Interacts with SIRT1; the interaction is increased in the context of genotoxic stress. Interacts with HDAC1, HDAC2 and HDAC3; the interactions are not dependent on the APEX1 acetylation status. Interacts with XRCC1; the interaction is induced by SIRT1 and increased with the APEX1 acetylated form. Interacts with NPM1 (via N-terminal domain); the interaction is RNA-dependent and decreases in hydrogen peroxide-damaged cells. Interacts (via N-terminus) with YBX1 (via C-terminus); the interaction is increased in presence of APEX1 acetylated at Lys-6 and Lys-7. Interacts with HNRNPL; the interaction is DNA-dependent. Interacts (via N-terminus) with KPNA1 and KPNA2. Interacts with TXN; the interaction stimulates the FOS/JUN AP-1 complex DNA-binding activity in a redox-dependent manner. Interacts with GZMA, KRT8, MDM2, POLB, PRDX6, PRPF19, RPLP0, TOMM20 and WDR77. Binds to CDK5. {ECO:0000269|PubMed:20473298}. DOMAIN: The N-terminus contains the redox activity while the C-terminus exerts the DNA AP-endodeoxyribonuclease activity; both function are independent in their actions. An unconventional mitochondrial targeting sequence (MTS) is harbored within the C-terminus, that appears to be masked by the N-terminal sequence containing the nuclear localization signal (NLS), that probably blocks the interaction between the MTS and Tom proteins (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in both resting and stimulated B cells stimulated to switch (at protein level). +B2RUJ5 APBA1_MOUSE Amyloid-beta A4 precursor protein-binding family A member 1 (Adapter protein X11alpha) (Neuron-specific X11 protein) (Neuronal Munc18-1-interacting protein 1) (Mint-1) 842 92,909 Alternative sequence (3); Chain (1); Compositional bias (3); Domain (3); Modified residue (15); Region (1); Sequence conflict (1) FUNCTION: Putative function in synaptic vesicle exocytosis by binding to Munc18-1, an essential component of the synaptic vesicle exocytotic machinery. May modulate processing of the amyloid-beta precursor protein (APP) and hence formation of AAP-beta (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 3: Golgi apparatus. SUBUNIT: Part of a multimeric complex containing Munc18-1 and syntaxin-1. Also part of the brain-specific heterotrimeric complex LIN-10/X11-alpha, LIN-2/CASK, and LIN7. Binds to the cytoplasmic domain of amyloid protein (APP) (By similarity). Interacts (via PDZ 1 and 2 domains) with FSPB (By similarity). Isoform 3 interacts (via its truncated PID domain) with active, GTP-bound RAB6A. Also interacts with GTP-bound RAB6B (By similarity). {ECO:0000250}. DOMAIN: Composed of an N-terminal domain that binds Munc18-1 and LIN-2/CASK, a middle phosphotyrosine-binding domain (PID/PTB) that mediates binding with the cytoplasmic domain of the amyloid-beta precursor protein, and two C-terminal PDZ domains thought to attach proteins to the plasma membrane. {ECO:0000250}.; DOMAIN: The autoinhibitory helix linker occludes the APP binding site. {ECO:0000250}.; DOMAIN: The PID domain, truncated by 11 amino acids, as observed in isoform 3, but not full-length, mediates the interaction with RAB6A. {ECO:0000250}. TISSUE SPECIFICITY: Isoform 3 is expressed in brain. {ECO:0000269|PubMed:23737971}. +P97449 AMPN_MOUSE Aminopeptidase N (AP-N) (mAPN) (EC 3.4.11.2) (Alanyl aminopeptidase) (Aminopeptidase M) (AP-M) (Membrane protein p161) (Microsomal aminopeptidase) (CD antigen CD13) 966 109,651 Active site (1); Chain (1); Disulfide bond (2); Glycosylation (13); Metal binding (3); Modified residue (4); Region (3); Sequence conflict (20); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 9 32 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 8 Cytoplasmic. {ECO:0000250|UniProtKB:P15144}.; TOPO_DOM 33 966 Extracellular. {ECO:0000250|UniProtKB:P15144}. FUNCTION: Broad specificity aminopeptidase which plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. Also involved in the processing of various peptides including peptide hormones, such as angiotensin III and IV, neuropeptides, and chemokines (By similarity). May also be involved the cleavage of peptides bound to major histocompatibility complex class II molecules of antigen presenting cells (PubMed:8691132). May have a role in angiogenesis and promote cholesterol crystallization (By similarity). {ECO:0000250|UniProtKB:P15144, ECO:0000269|PubMed:8691132}. PTM: N- and O-glycosylated. {ECO:0000269|PubMed:8805662}.; PTM: Sulfated. {ECO:0000250|UniProtKB:P15145}.; PTM: May undergo proteolysis and give rise to a soluble form. {ECO:0000250|UniProtKB:P15144}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8805662}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P15144}. Note=Also found as a soluble form. {ECO:0000250|UniProtKB:P15144}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P15144}. TISSUE SPECIFICITY: Highly expressed in intestinal tract and kidney, present in liver, lymph node, spleen, and brain. Found as well in monocytes, macrophages, dendritic cells, veiled cells and B-cells but not on T-cells and thymocytes. {ECO:0000269|PubMed:8103749, ECO:0000269|PubMed:8805662}. +Q8BZQ7 ANC2_MOUSE Anaphase-promoting complex subunit 2 (APC2) (Cyclosome subunit 2) 837 95,307 Chain (1); Modified residue (6); Sequence conflict (1) Protein modification; protein ubiquitination. FUNCTION: Together with the RING-H2 protein ANAPC11, constitutes the catalytic component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. The CDC20-APC/C complex positively regulates the formation of synaptic vesicle clustering at active zone to the presynaptic membrane in postmitotic neurons. CDC20-APC/C-induced degradation of NEUROD2 drives presynaptic differentiation. {ECO:0000250|UniProtKB:Q9UJX6, ECO:0000269|PubMed:19900895}. SUBUNIT: The mammalian APC/C is composed at least of 14 distinct subunits ANAPC1, ANAPC2, CDC27/APC3, ANAPC4, ANAPC5, CDC16/APC6, ANAPC7, CDC23/APC8, ANAPC10, ANAPC11, CDC26/APC12, ANAPC13, ANAPC15 and ANAPC16 that assemble into a complex of at least 19 chains with a combined molecular mass of around 1.2 MDa; APC/C interacts with FZR1 and FBXO5 (By similarity). In the context of the APC/C complex, directly interacts with UBE2C and UBE2S (By similarity). Interacts (via cullin domain) with ANAPC11 and with UBCH10 (By similarity). Interacts with NEUROD2 (PubMed:19900895). {ECO:0000250|UniProtKB:Q9UJX6, ECO:0000269|PubMed:19900895}. +Q80ZD9 AMGO2_MOUSE Amphoterin-induced protein 2 (AMIGO-2) (Alivin-1) 519 57,562 Chain (1); Disulfide bond (5); Domain (3); Glycosylation (9); Repeat (6); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 398 418 Helical. {ECO:0000255}. TOPO_DOM 39 397 Extracellular. {ECO:0000255}.; TOPO_DOM 419 519 Cytoplasmic. {ECO:0000255}. FUNCTION: Required for depolarization-dependent survival of cultured cerebellar granule neurons. May mediate homophilic as well as heterophilic cell-cell interaction with AMIGO1 or AMIGO3. May contribute to signal transduction through its intracellular domain (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Nucleus {ECO:0000250}. Note=Associated with nucleus as well as plasma membrane. Restricted to somata of cerebellar as well as hippocampal neurons (By similarity). {ECO:0000250}. SUBUNIT: Binds itself as well as AMIGO1 and AMIGO3. {ECO:0000250}. TISSUE SPECIFICITY: Highest level in cerebellum, retina, liver, and lung. Lower levels in cerebrum, kidney, small intestine, spleen and testis. {ECO:0000269|PubMed:12629050}. +Q9D2J7 ANKE1_MOUSE Ankyrin repeat and EF-hand domain-containing protein 1 (Ankyrin repeat domain-containing protein 5) 775 86,904 Chain (1); Repeat (8) +Q64438 ANG2_MOUSE Angiogenin-2 (Angiogenin-related protein) 145 16,593 Active site (2); Beta strand (8); Binding site (1); Chain (1); Disulfide bond (3); Helix (4); Metal binding (3); Motif (1); Region (1); Sequence conflict (1); Signal peptide (1); Site (1); Turn (2) FUNCTION: Has ribonuclease activity (in vitro). Seems to lack angiogenic activity. {ECO:0000269|PubMed:8633065}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle lumen {ECO:0000250|UniProtKB:Q3TMQ6}. Secreted {ECO:0000250|UniProtKB:P10152}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P03950}. Note=Rapidly endocytosed by target cells and translocated to the nucleus where it accumulates in the nucleolus and binds to DNA (By similarity). {ECO:0000250|UniProtKB:P03950}. SUBUNIT: Homodimer. {ECO:0000269|PubMed:23170778}. TISSUE SPECIFICITY: Expressed (at protein level) in macrophages. {ECO:0000269|PubMed:16045902}. +P97802 ANG3_MOUSE Angiogenin-3 (EC 3.1.27.-) (Angiogenin-related protein 2) (EF-5) 145 16,696 Active site (2); Beta strand (8); Binding site (1); Chain (1); Disulfide bond (3); Helix (4); Metal binding (2); Modified residue (1); Motif (1); Region (1); Signal peptide (1); Site (1); Turn (3) FUNCTION: May promote vascularization of normal and malignant tissues (By similarity). Has low ribonuclease activity (in vitro). {ECO:0000250, ECO:0000269|PubMed:11437607}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle lumen {ECO:0000250|UniProtKB:Q3TMQ6}. Secreted {ECO:0000250|UniProtKB:P10152}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P03950}. Note=Rapidly endocytosed by target cells and translocated to the nucleus where it accumulates in the nucleolus and binds to DNA (By similarity). {ECO:0000250|UniProtKB:P03950}. +Q6VVW5 ANPRB_MOUSE Atrial natriuretic peptide receptor 2 (EC 4.6.1.2) (Atrial natriuretic peptide receptor type B) (ANP-B) (ANPR-B) (NPR-B) (Guanylate cyclase B) (GC-B) 1047 117,060 Alternative sequence (3); Chain (1); Disulfide bond (3); Domain (2); Glycosylation (7); Modified residue (7); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 459 478 Helical. {ECO:0000255}. TOPO_DOM 17 458 Extracellular. {ECO:0000255}.; TOPO_DOM 479 1047 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for the C-type natriuretic peptide NPPC/CNP hormone. Has guanylate cyclase activity upon binding of its ligand. May play a role in the regulation of skeletal growth. {ECO:0000269|PubMed:15572448}. PTM: Phosphorylated. Phosphorylation of the protein kinase-like domain is required for full activation by CNP. {ECO:0000250|UniProtKB:P16067}.; PTM: Glycosylated. {ECO:0000250|UniProtKB:P20594}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P20594}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P20594}. TISSUE SPECIFICITY: Widely expressed. Expressed in the columnar proliferating and prehypertrophic chondrocyte layers of the tibia. {ECO:0000269|PubMed:15572448}. +Q9Z1T1 AP3B1_MOUSE AP-3 complex subunit beta-1 (Adaptor protein complex AP-3 subunit beta-1) (Adaptor-related protein complex 3 subunit beta-1) (Beta-3A-adaptin) (Clathrin assembly protein complex 3 beta-1 large chain) 1105 122,740 Chain (1); Compositional bias (1); Modified residue (4); Sequence conflict (9) FUNCTION: Subunit of non-clathrin- and clathrin-associated adaptor protein complex 3 (AP-3) that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. AP-3 appears to be involved in the sorting of a subset of transmembrane proteins targeted to lysosomes and lysosome-related organelles. In concert with the BLOC-1 complex, AP-3 is required to target cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. {ECO:0000269|PubMed:21998198}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Golgi apparatus {ECO:0000250}. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex. {ECO:0000250}. SUBUNIT: Adaptor protein complex 3 (AP-3) is a heterotetramer composed of two large adaptins (delta-type subunit AP3D1 and beta-type subunit AP3B1 or AP3B2), a medium adaptin (mu-type subunit AP3M1 or AP3M2) and a small adaptin (sigma-type subunit APS1 or AP3S2). AP-3 associates with the BLOC-1 complex. TISSUE SPECIFICITY: Ubiquitously expressed. DISEASE: Note=Defects in Ap3b1 are the cause of the autosomal recessive phenotype 'pearl' (pe). Pearl mice exhibit hypopigmentation, lysosomal secretion abnormalities, and platelet-dense granules with reduced levels of adenine nucleotides and serotonin. The changes in platelets lead to prolonged bleeding. Additionally, pearl mice exhibit reduced sensitivity in the dark-adapted state (PubMed:9931340). {ECO:0000269|PubMed:9931340}. +Q8BIZ1 ANS1B_MOUSE Ankyrin repeat and sterile alpha motif domain-containing protein 1B (Amyloid-beta protein intracellular domain-associated protein 1) (AIDA-1) (E2A-PBX1-associated protein) (EB-1) 1259 139,047 Alternative sequence (7); Chain (1); Domain (3); Modified residue (14); Motif (1); Repeat (7); Sequence conflict (5) FUNCTION: Isoform 2 may participate in the regulation of nucleoplasmic coilin protein interactions in neuronal and transformed cells. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 2: Nucleus {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 4: Cell junction, synapse, postsynaptic cell membrane, postsynaptic density. Cell projection, dendritic spine. Nucleus. SUBUNIT: Interacts with EPHA8. Isoform 2 interacts with COIL (By similarity). {ECO:0000250}. +Q8CFW1 ANO2_MOUSE Anoctamin-2 (Transmembrane protein 16B) 1002 114,134 Chain (1); Erroneous initiation (1); Glycosylation (4); Motif (1); Mutagenesis (1); Sequence caution (1); Topological domain (9); Transmembrane (8) TRANSMEM 365 385 Helical. {ECO:0000255}.; TRANSMEM 434 454 Helical. {ECO:0000255}.; TRANSMEM 537 557 Helical. {ECO:0000255}.; TRANSMEM 581 601 Helical. {ECO:0000255}.; TRANSMEM 622 642 Helical. {ECO:0000255}.; TRANSMEM 747 767 Helical. {ECO:0000255}.; TRANSMEM 800 820 Helical. {ECO:0000255}.; TRANSMEM 906 926 Helical. {ECO:0000255}. TOPO_DOM 1 364 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 386 433 Extracellular. {ECO:0000255}.; TOPO_DOM 455 536 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 558 580 Extracellular. {ECO:0000255}.; TOPO_DOM 602 621 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 643 746 Extracellular. {ECO:0000255}.; TOPO_DOM 768 799 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 821 905 Extracellular. {ECO:0000255}.; TOPO_DOM 927 1002 Cytoplasmic. {ECO:0000255}. FUNCTION: Calcium-activated chloride channel (CaCC) which may play a role in olfactory signal transduction. Odorant molecules bind to odor-sensing receptors (OSRs), leading to an increase in calcium entry that activates CaCC current which amplifies the depolarization of the OSR cells, ANO2 seems to be the underlying chloride channel involved in this process. May mediate light perception amplification in retina. {ECO:0000269|PubMed:19474308, ECO:0000269|PubMed:19475416, ECO:0000269|PubMed:19561302, ECO:0000269|PubMed:21890523, ECO:0000269|PubMed:22075693}. PTM: Glycosylated. {ECO:0000269|PubMed:19474308}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19474308, ECO:0000269|PubMed:19561302}; Multi-pass membrane protein {ECO:0000269|PubMed:19474308, ECO:0000269|PubMed:19561302}. SUBUNIT: Component of a presynaptic protein complex recruited to specialized plasma membrane domains of photoreceptors. Interacts with DLG4 by its C-terminal region. {ECO:0000269|PubMed:19474308}. TISSUE SPECIFICITY: Expressed in retina, especially in the photoreceptor synaptic terminals, and in olfactory epithelium, particularly in sensory neurons (OSNs) and cilia (at protein level). Also observed in retinal pigment epithelium (RPE), olfactory bulb, brain, and cortex. {ECO:0000269|PubMed:19474308, ECO:0000269|PubMed:19561302, ECO:0000269|PubMed:20056604}. +Q9CPV2 APC16_MOUSE Anaphase-promoting complex subunit 16 (APC16) (Cyclosome subunit 16) 110 11,667 Chain (1); Compositional bias (1); Initiator methionine (1); Modified residue (1) Protein modification; protein ubiquitination. FUNCTION: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. {ECO:0000269|PubMed:20360068}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20360068}. Nucleus {ECO:0000269|PubMed:20360068}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q96DE5}. SUBUNIT: The mammalian APC/C is composed at least of 14 distinct subunits ANAPC1, ANAPC2, CDC27/APC3, ANAPC4, ANAPC5, CDC16/APC6, ANAPC7, CDC23/APC8, ANAPC10, ANAPC11, CDC26/APC12, ANAPC13, ANAPC15 and ANAPC16 that assemble into a complex of at least 19 chains with a combined molecular mass of around 1.2 MDa; APC/C interacts with FZR1 and FBXO5. ANAPC16 associates with the rest of the complex independently of ANAPC2 and ANAPC11. {ECO:0000250|UniProtKB:Q96DE5}. +P06728 APOA4_MOUSE Apolipoprotein A-IV (Apo-AIV) (ApoA-IV) (Apolipoprotein A4) 395 45,029 Chain (1); Compositional bias (1); Natural variant (1); Region (1); Repeat (13); Sequence conflict (9); Signal peptide (1) FUNCTION: May have a role in chylomicrons and VLDL secretion and catabolism. Required for efficient activation of lipoprotein lipase by ApoC-II; potent activator of LCAT. Apoa-IV is a major component of HDL and chylomicrons. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P06727}. DOMAIN: Nine of the thirteen 22-amino acid tandem repeats (each 22-mer is actually a tandem array of two, A and B, related 11-mers) occurring in this sequence are predicted to be highly alpha-helical, and many of these helices are amphipathic. They may therefore serve as lipid-binding domains with lecithin:cholesterol acyltransferase (LCAT) activating abilities. TISSUE SPECIFICITY: Secreted in plasma. +Q8R5G7 ARAP3_MOUSE Arf-GAP with Rho-GAP domain, ANK repeat and PH domain-containing protein 3 (Centaurin-delta-3) (Cnt-d3) (Dual specificity Rho- and Arf-GTPase-activating protein 1) 1538 169,741 Alternative sequence (3); Chain (1); Compositional bias (1); Domain (9); Erroneous initiation (2); Modified residue (5); Mutagenesis (3); Sequence conflict (7) FUNCTION: Phosphatidylinositol 3,4,5-trisphosphate-dependent GTPase-activating protein that modulates actin cytoskeleton remodeling by regulating ARF and RHO family members. Is activated by phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) binding. Can be activated by phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4,5)P2) binding, albeit with lower efficiency. Acts preferentially on ARF5 and on RHOA. {ECO:0000269|PubMed:15546919}. PTM: Tyrosine phosphorylated at a low basal level. PDGF treatment stimulates phosphorylation. Tyrosine phosphorylation is increased in cells that are in the process of becoming attached to a substrate and that start spreading and flattening. {ECO:0000269|PubMed:15546919}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15546919}. Cell membrane {ECO:0000269|PubMed:15546919}; Peripheral membrane protein {ECO:0000269|PubMed:15546919}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15546919}. Cell projection, lamellipodium {ECO:0000269|PubMed:15546919}. Cell projection, ruffle {ECO:0000269|PubMed:15546919}. Note=Cytoplasmic, and associated with F-actin-rich membrane ruffles and lamellipodia. SUBUNIT: Interacts (via SAM domain) with INPPL1/SHIP2. {ECO:0000250}. +P55088 AQP4_MOUSE Aquaporin-4 (AQP-4) (Mercurial-insensitive water channel) (MIWC) (WCH4) 323 34,436 Alternative sequence (2); Chain (1); Glycosylation (2); Modified residue (6); Motif (2); Natural variant (1); Sequence conflict (9); Topological domain (7); Transmembrane (6) TRANSMEM 37 58 Helical. {ECO:0000255}.; TRANSMEM 65 85 Helical. {ECO:0000255}.; TRANSMEM 116 136 Helical. {ECO:0000255}.; TRANSMEM 156 176 Helical. {ECO:0000255}.; TRANSMEM 185 205 Helical. {ECO:0000255}.; TRANSMEM 232 252 Helical. {ECO:0000255}. TOPO_DOM 1 36 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 59 64 Extracellular. {ECO:0000255}.; TOPO_DOM 86 115 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 137 155 Extracellular. {ECO:0000255}.; TOPO_DOM 177 184 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 206 231 Extracellular. {ECO:0000255}.; TOPO_DOM 253 323 Cytoplasmic. {ECO:0000255}. FUNCTION: Forms a water-specific channel. Osmoreceptor which regulates body water balance and mediates water flow within the central nervous system. PTM: Phosphorylation by PKC at Ser-180 reduces conductance by 50%. Phosphorylation by PKG at Ser-111 in response to glutamats increases conductance by 40% (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SUBUNIT: Homotetramer. Part of a complex containing MLC1, TRPV4, HEPACAM and ATP1B1. {ECO:0000250}. DOMAIN: Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA). +Q8K371 AMOL2_MOUSE Angiomotin-like protein 2 772 85,278 Chain (1); Coiled coil (1); Erroneous initiation (1); Frameshift (1); Modified residue (3); Motif (1); Sequence conflict (11) FUNCTION: Regulates the translocation of phosphorylated SRC to peripheral cell-matrix adhesion sites. Required for proper architecture of actin filaments. Inhibits the Wnt/beta-catenin signaling pathway, probably by recruiting CTNNB1 to recycling endosomes and hence preventing its translocation to the nucleus. Participates in angiogenesis. May play a role in the polarity, proliferation and migration of endothelial cells. Selectively promotes FGF-induced MAPK activation through SRC (By similarity). {ECO:0000250}. PTM: Phosphorylation at Tyr-107 is necessary for efficient binding to SRC and synergistically functioning with SRC to activate the downstream MAPK pathway. {ECO:0000250}. SUBCELLULAR LOCATION: Recycling endosome {ECO:0000250}. SUBUNIT: Interacts with SRC. {ECO:0000250}. +Q80ZD8 AMGO1_MOUSE Amphoterin-induced protein 1 (AMIGO-1) (Alivin-2) 492 55,343 Alternative sequence (2); Beta strand (17); Chain (1); Disulfide bond (5); Domain (3); Erroneous initiation (1); Frameshift (1); Glycosylation (5); Helix (7); Modified residue (2); Mutagenesis (1); Repeat (6); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (3) TRANSMEM 372 392 Helical. {ECO:0000255}. TOPO_DOM 28 371 Extracellular. {ECO:0000255}.; TOPO_DOM 393 492 Cytoplasmic. {ECO:0000255}. FUNCTION: Promotes growth and fasciculation of neurites from cultured hippocampal neurons. May be involved in fasciculation as well as myelination of developing neural axons. May have a role in regeneration as well as neural plasticity in the adult nervous system. May mediate homophilic as well as heterophilic cell-cell interaction and contribute to signal transduction through its intracellular domain (By similarity). Assembled with KCNB1 modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1 (PubMed:22056818). {ECO:0000250|UniProtKB:Q80ZD7, ECO:0000269|PubMed:22056818}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21983541, ECO:0000269|PubMed:22056818}; Single-pass type I membrane protein {ECO:0000269|PubMed:21983541}. Perikaryon {ECO:0000269|PubMed:22056818}. Cell projection, dendrite {ECO:0000269|PubMed:22056818}. Note=Colocalizes with KCNB1 at high-density somatodendritic clusters on the surface of hippocampal and cortical neurons (PubMed:22056818). Associated with axons of neuronal cells (By similarity). {ECO:0000250|UniProtKB:Q80ZD7, ECO:0000269|PubMed:22056818}. SUBUNIT: Homodimer, and heterodimer with AMIGO2 and AMIGO3 (PubMed:21983541). Interacts with KCNB1 (PubMed:22056818). {ECO:0000269|PubMed:21983541, ECO:0000269|PubMed:22056818}. DOMAIN: The LRR repeat region mediates homodimerization. TISSUE SPECIFICITY: Expressed in hippocampal and cortical neurons (at protein level) (PubMed:22056818). High levels in cerebellum, cerebrum, and retina. Low levels in liver, kidney, small intestine, spleen, lung and heart. {ECO:0000269|PubMed:12629050, ECO:0000269|PubMed:22056818}. +P55302 AMRP_MOUSE Alpha-2-macroglobulin receptor-associated protein (Alpha-2-MRAP) (Heparin-binding protein 44) (HBP-44) (Low density lipoprotein receptor-related protein-associated protein 1) (RAP) 360 42,215 Chain (1); Coiled coil (1); Glycosylation (1); Modified residue (2); Motif (1); Region (1); Signal peptide (1) FUNCTION: Molecular chaperone for LDL receptor-related proteins that may regulate their ligand binding activity along the secretory pathway. {ECO:0000250|UniProtKB:P30533}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:P30533}. SUBCELLULAR LOCATION: Rough endoplasmic reticulum lumen {ECO:0000250|UniProtKB:P30533}. Endoplasmic reticulum-Golgi intermediate compartment lumen {ECO:0000250|UniProtKB:P30533}. Golgi apparatus, cis-Golgi network {ECO:0000250|UniProtKB:P30533}. Golgi apparatus lumen {ECO:0000250|UniProtKB:P30533}. Endosome lumen {ECO:0000250|UniProtKB:P30533}. Cell surface {ECO:0000250|UniProtKB:P30533}. Note=May be associated with receptors at the cell surface. {ECO:0000250|UniProtKB:P30533}. SUBUNIT: Interacts with the LRP1/alpha-2-macroglobulin receptor heavy and light chains; the interaction is transient and coincides with a reduction of ligand binding by the receptor. Interacts with LRP2/glycoprotein 330. Interacts with LRP1B; binding is followed by internalization and degradation. Interacts with LDLR. {ECO:0000250|UniProtKB:P30533}. TISSUE SPECIFICITY: Highly expressed in PYS-2 parietal endoderm cells and in the kidney. The RNA level increased about 10-fold during differentiation of F9 embryonal carcinoma cells to parietal endoderm cells. {ECO:0000269|PubMed:2229028}. +Q80UU1 ANKZ1_MOUSE Ankyrin repeat and zinc finger domain-containing protein 1 748 82,976 Alternative sequence (2); Chain (1); Coiled coil (1); Frameshift (1); Modified residue (5); Region (1); Repeat (2); Sequence conflict (3); Zinc finger (1) FUNCTION: Plays a role in the cellular response to hydrogen peroxide and in the maintenance of mitochondrial integrity under conditions of cellular stress (By similarity). Involved in the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway (By similarity). {ECO:0000250|UniProtKB:Q9H8Y5}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H8Y5}. Note=Translocates to the mitochondria upon exposure to hydrogen peroxide. {ECO:0000250|UniProtKB:Q9H8Y5}. SUBUNIT: Interacts (via VIM motif) with VCP. {ECO:0000250|UniProtKB:Q9H8Y5}. +Q8BTI7 ANR52_MOUSE Serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit C (PP6-ARS-C) (Serine/threonine-protein phosphatase 6 regulatory subunit ARS-C) 1076 115,032 Chain (1); Modified residue (2); Repeat (28) FUNCTION: Putative regulatory subunit of protein phosphatase 6 (PP6) that may be involved in the recognition of phosphoprotein substrates. {ECO:0000250}. SUBUNIT: Protein phosphatase 6 (PP6) holoenzyme is proposed to be a heterotrimeric complex formed by the catalytic subunit, a SAPS domain-containing subunit (PP6R) and an ankyrin repeat-domain containing regulatory subunit (ARS). Interacts with PPP6R1 (By similarity). {ECO:0000250}. +P21570 ANGI_MOUSE Angiogenin (EC 3.1.27.-) (Angiogenin-1) (Ribonuclease 5) (RNase 5) 145 16,228 Active site (2); Beta strand (8); Chain (1); Disulfide bond (3); Helix (5); Modified residue (1); Motif (1); Region (1); Signal peptide (1); Turn (3) FUNCTION: Binds to actin on the surface of endothelial cells; once bound, angiogenin is endocytosed and translocated to the nucleus. Stimulates ribosomal RNA synthesis including that containing the initiation site sequences of 45S rRNA. Cleaves tRNA within anticodon loops to produce tRNA-derived stress-induced fragments (tiRNAs) which inhibit protein synthesis and triggers the assembly of stress granules (SGs). Angiogenin induces vascularization of normal and malignant tissues. Angiogenic activity is regulated by interaction with RNH1 in vivo (By similarity). {ECO:0000250, ECO:0000269|PubMed:19114040}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle lumen {ECO:0000250|UniProtKB:Q3TMQ6}. Secreted {ECO:0000250|UniProtKB:P10152}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P03950}. Note=Rapidly endocytosed by target cells and translocated to the nucleus where it accumulates in the nucleolus and binds to DNA (By similarity). {ECO:0000250|UniProtKB:P03950}. SUBUNIT: Homodimer. Interacts with and forms a tight 1:1 complex with RNH1. Dimerization of two such complexes may occur (By similarity). {ECO:0000250|UniProtKB:P03950}. +Q9WVP1 AP1M2_MOUSE AP-1 complex subunit mu-2 (AP-mu chain family member mu1B) (Adaptor protein complex AP-1 subunit mu-2) (Adaptor-related protein complex 1 subunit mu-2) (Clathrin assembly protein complex 1 mu-2 medium chain 2) (Golgi adaptor HA1/AP1 adaptin mu-2 subunit) (Mu-adaptin 2) (Mu1B-adaptin) 423 48,137 Alternative sequence (1); Chain (1); Domain (1); Sequence conflict (2) FUNCTION: Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the trans-Golgi network (TGN) and endosomes. The AP complexes mediate the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. PTM: Phosphorylation of membrane-bound AP1M1/AP1M2 increases its affinity for sorting signals. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasmic vesicle, clathrin-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex. SUBUNIT: Adaptor protein complex 1 (AP-1) is a heterotetramer composed of two large adaptins (gamma-type subunit AP1G1 and beta-type subunit AP1B1), a medium adaptin (mu-type subunit AP1M1 or AP1M2) and a small adaptin (sigma-type subunit AP1S1 or AP1S2 or AP1S3). {ECO:0000269|PubMed:11964383}. +Q9DBR4 APBB2_MOUSE Amyloid-beta A4 precursor protein-binding family B member 2 760 83,201 Alternative sequence (2); Beta strand (9); Chain (1); Domain (3); Helix (2); Modified residue (5); Turn (2) FUNCTION: May modulate the internalization of amyloid-beta precursor protein. {ECO:0000250}. SUBUNIT: Binds to the intracellular domain of the amyloid-beta precursor protein. {ECO:0000250}. +Q8BJ63 AP5M1_MOUSE AP-5 complex subunit mu-1 (Adaptor-related protein complex 5 subunit mu-1) (Mu5) (Mu-2-related death-inducing protein) (MuD) 490 54,337 Alternative sequence (4); Chain (1); Domain (1); Sequence conflict (13) FUNCTION: As part of AP-5, a probable fifth adaptor protein complex it may be involved in endosomal transport. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol. Late endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Lysosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=May cycle on and off membranes. {ECO:0000250}. SUBUNIT: Probably part of the adaptor protein complex 5 (AP-5) a tetramer composed of AP5B1, AP5M1, AP5S1 and AP5Z1. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed, including in small intestine and testis. In small intestine, highly expressed in cytoplasm of villi epithelial cells and internal glands. In testis, selectively expressed in maturing sperm cells (at protein level). {ECO:0000269|PubMed:18395520}. +Q8BW75 AOFB_MOUSE Amine oxidase [flavin-containing] B (EC 1.4.3.4) (Monoamine oxidase type B) (MAO-B) 520 58,558 Chain (1); Compositional bias (1); Initiator methionine (1); Modified residue (4); Sequence conflict (2); Site (3); Topological domain (2); Transmembrane (1) TRANSMEM 490 516 Helical; Anchor for type IV membrane protein. {ECO:0000250}. TOPO_DOM 2 489 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 517 520 Mitochondrial intermembrane. {ECO:0000250}. FUNCTION: Catalyzes the oxidative deamination of biogenic and xenobiotic amines and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. MAOB preferentially degrades benzylamine and phenylethylamine (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. SUBUNIT: Monomer, homo- or heterodimer (containing two subunits of similar size). Each subunit contains a covalently bound flavin. Enzymatically active as monomer (By similarity). {ECO:0000250}. +Q61268 APOC4_MOUSE Apolipoprotein C-IV (Apo-CIV) (ApoC-IV) (Apolipoprotein C2-linked) (ACL) (Apolipoprotein C4) 124 14,288 Chain (1); Glycosylation (1); Signal peptide (1) FUNCTION: May participate in lipoprotein metabolism. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma. +P62743 AP2S1_MOUSE AP-2 complex subunit sigma (Adaptor protein complex AP-2 subunit sigma) (Adaptor-related protein complex 2 subunit sigma) (Clathrin assembly protein 2 sigma small chain) (Clathrin coat assembly protein AP17) (Clathrin coat-associated protein AP17) (Plasma membrane adaptor AP-2 17 kDa protein) (Sigma-adaptin 3b) (Sigma2-adaptin) 142 17,018 Beta strand (7); Chain (1); Helix (5); Modified residue (1); Mutagenesis (10) FUNCTION: Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via Transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. The AP-2 alpha and AP-2 sigma subunits are thought to contribute to the recognition of the [ED]-X-X-X-L-[LI] motif. May also play a role in extracellular calcium homeostasis (By similarity). {ECO:0000250, ECO:0000269|PubMed:14745134, ECO:0000269|PubMed:15473838}. SUBCELLULAR LOCATION: Cell membrane. Membrane, coated pit; Peripheral membrane protein; Cytoplasmic side. Note=AP-2 appears to be excluded from internalizing CCVs and to disengage from sites of endocytosis seconds before internalization of the nascent CCV. {ECO:0000250}. SUBUNIT: Adaptor protein complex 2 (AP-2) is a heterotetramer composed of two large adaptins (alpha-type subunit AP2A1 or AP2A2 and beta-type subunit AP2B1), a medium adaptin (mu-type subunit AP2M1) and a small adaptin (sigma-type subunit AP2S1). {ECO:0000269|PubMed:12086608, ECO:0000269|PubMed:19140243}. +Q3U128 APCD1_MOUSE Protein APCDD1 (Adenomatosis polyposis coli down-regulated 1 protein homolog) 514 58,638 Chain (1); Erroneous termination (1); Glycosylation (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 493 513 Helical. {ECO:0000255}. TOPO_DOM 27 492 Extracellular. {ECO:0000255}.; TOPO_DOM 514 514 Cytoplasmic. {ECO:0000255}. FUNCTION: Negative regulator of the Wnt signaling pathway. Inhibits Wnt signaling in a cell-autonomous manner and functions upstream of beta-catenin. May act via its interaction with Wnt and LRP proteins (By similarity). {ECO:0000250}. PTM: N-Glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Homodimer. Interacts with LRP5 and WNT3A (By similarity). {ECO:0000250}. +Q05020 APOC2_MOUSE Apolipoprotein C-II (Apo-CII) (ApoC-II) (Apolipoprotein C2) 97 10,741 Chain (1); Region (2); Sequence conflict (1); Signal peptide (1) FUNCTION: Component of chylomicrons, very low-density lipoproteins (VLDL), low-density lipoproteins (LDL), and high-density lipoproteins (HDL) in plasma. Plays an important role in lipoprotein metabolism as an activator of lipoprotein lipase. {ECO:0000250|UniProtKB:P02655}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02655}. TISSUE SPECIFICITY: Adult and fetal liver, intestine and peritoneal macrophages. {ECO:0000269|PubMed:7691714}. +Q6PGD0 ARAID_MOUSE All-trans retinoic acid-induced differentiation factor (Apoptosis-related protein 3) (APR-3) 223 23,858 Alternative sequence (1); Chain (1); Disulfide bond (3); Domain (1); Erroneous translation (1); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 194 214 Helical. {ECO:0000255}. TOPO_DOM 26 193 Extracellular. {ECO:0000255}.; TOPO_DOM 215 223 Cytoplasmic. {ECO:0000255}. FUNCTION: Promotes osteoblast cell differentiation and terminal mineralization. Plays a role in inducing the cell cycle arrest via inhibiting CCND1 expression in all-trans-retinoic acid (ATRA) signal pathway (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000250|UniProtKB:Q6UW56}. Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q6UW56}. Note=Colocalizes with NELL1 on the nuclear envelope and the perinuclear region. {ECO:0000250|UniProtKB:Q6UW56}. SUBUNIT: Interacts with NELL1; the interaction promotes osteoblastic differentiation and mineralization. {ECO:0000250}. +Q07456 AMBP_MOUSE Protein AMBP [Cleaved into: Alpha-1-microglobulin; Inter-alpha-trypsin inhibitor light chain (ITI-LC) (Bikunin) (HI-30); Trypstatin] 349 39,029 Binding site (4); Chain (3); Disulfide bond (7); Domain (2); Glycosylation (3); Sequence conflict (2); Signal peptide (1); Site (2) FUNCTION: Inter-alpha-trypsin inhibitor inhibits trypsin, plasmin, and lysosomal granulocytic elastase. Inhibits calcium oxalate crystallization (By similarity). {ECO:0000250}.; FUNCTION: Trypstatin is a trypsin inhibitor. {ECO:0000250}. PTM: The precursor is proteolytically processed into separately functioning proteins.; PTM: 3-hydroxykynurenine, an oxidized tryptophan metabolite that is common in biological fluids, reacts with Cys-52, Lys-110, Lys-136, and Lys-148 to form heterogeneous polycyclic chromophores including hydroxanthommatin. The reaction by alpha-1-microglobulin is autocatalytic. The chromophore can react with accessible cysteines forming non-reducible thioether cross-links with other molecules of alpha-1-microglobulin or with other proteins such as Ig alpha-1 chain C region (By similarity). {ECO:0000250}.; PTM: Heavy chains are interlinked with bikunin via a chondroitin 4-sulfate bridge to the their C-terminal aspartate. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: I-alpha-I plasma protease inhibitors are assembled from one or two heavy chains (H1, H2 or H3) and one light chain, bikunin. Inter-alpha-inhibitor (I-alpha-I) is composed of H1, H2 and bikunin, inter-alpha-like inhibitor (I-alpha-LI) of H2 and bikunin, and pre-alpha-inhibitor (P-alpha-I) of H3 and bikunin. Alpha-1-microglobulin occurs as a monomer and also in complexes with IgA and albumin. Alpha-1-microglobulin interacts with FN1. Trypstatin is a monomer and also occurs as a complex with tryptase in mast cells (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma. Alpha-1-microglobulin occurs in many physiological fluids including plasma, urine, and cerebrospinal fluid. Inter-alpha-trypsin inhibitor is present in plasma and urine. +Q8CCJ4 AMER2_MOUSE APC membrane recruitment protein 2 (Amer2) (Protein FAM123A) 672 69,933 Alternative sequence (1); Chain (1); Compositional bias (1); Erroneous initiation (5); Modified residue (7) FUNCTION: Negative regulator of the canonical Wnt signaling pathway involved in neuroectodermal patterning. Acts by specifically binding phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), translocating to the cell membrane and interacting with key regulators of the canonical Wnt signaling pathway, such as components of the beta-catenin destruction complex (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Translocates to the cell membrane following binding to PtdIns(4,5)P2. {ECO:0000250}. SUBUNIT: Interacts with APC. {ECO:0000250}. +A2AH22 AMRA1_MOUSE Activating molecule in BECN1-regulated autophagy protein 1 1300 142,879 Alternative sequence (6); Chain (1); Compositional bias (3); Modified residue (7); Repeat (3); Sequence conflict (2) FUNCTION: Regulates autophagy and development of the nervous system. Involved in autophagy in controlling protein turnover during neuronal development, and in regulating normal cell survival and proliferation. {ECO:0000269|PubMed:17589504}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome {ECO:0000305|PubMed:17589504, ECO:0000305|PubMed:24089209}. Note=Localizes also to discrete punctae along the ciliary axoneme. SUBUNIT: Interacts with BECN1 (PubMed:17589504). Probably forms a complex with BECN1 and PIK3C3 (PubMed:17589504). Interacts with BECN2 (By similarity). {ECO:0000250|UniProtKB:Q9C0C7, ECO:0000269|PubMed:17589504}. +Q64G17 AN32C_MOUSE Putative acidic leucine-rich nuclear phosphoprotein 32 family member C 123 14,066 Chain (1); Repeat (4) +Q5F259 AN13B_MOUSE Ankyrin repeat domain-containing protein 13B 626 70,374 Alternative sequence (1); Chain (1); Compositional bias (2); Domain (3); Modified residue (1); Repeat (2) FUNCTION: Ubiquitin-binding protein that specifically recognizes and binds 'Lys-63'-linked ubiquitin. Does not bind 'Lys-48'-linked ubiquitin. Positively regulates the internalization of ligand-activated EGFR by binding to the Ub moiety of ubiquitinated EGFR at the cell membrane (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane. Late endosome. Early endosome. Note=Interaction with EGFR may enhance association with the cell membrane. {ECO:0000250}. SUBUNIT: Interacts with EGFR (ubiquitinated); the interaction is direct and may regulate EGFR internalization. {ECO:0000250}. +Q8VCU0 ANGE1_MOUSE Protein angel homolog 1 667 75,254 Chain (1); Modified residue (2); Sequence conflict (2) +Q91WK7 ANR54_MOUSE Ankyrin repeat domain-containing protein 54 (Lyn-interacting ankyrin repeat protein) 299 32,486 Chain (1); Frameshift (1); Initiator methionine (1); Modified residue (2); Motif (2); Mutagenesis (4); Region (1); Repeat (4); Sequence conflict (1) FUNCTION: Plays an important role in regulating intracellular signaling events associated with erythroid terminal differentiation. {ECO:0000269|PubMed:19064729}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19064729}. Cytoplasm {ECO:0000269|PubMed:19064729}. Midbody {ECO:0000269|PubMed:19064729}. Note=Shuttles between nucleus and cytoplasm during the cell cycle. EPO stimulation induces nuclear accumulation. SUBUNIT: Interacts (via ankyrin repeat region) with LYN (via SH3-domain) in an activation-independent status of LYN. Forms a multiprotein complex with LYN and HCLS1. Interacts with TSN2, VAV1, DBNL AND LASP1. {ECO:0000269|PubMed:19064729}. TISSUE SPECIFICITY: Expressed in a variety of hemopoietic cell lines and tissue with high levels in testis. Highly expressed in ciliated cells. {ECO:0000269|PubMed:17971504, ECO:0000269|PubMed:19064729}. +P14824 ANXA6_MOUSE Annexin A6 (67 kDa calelectrin) (Annexin VI) (Annexin-6) (Calphobindin-II) (CPB-II) (Chromobindin-20) (Lipocortin VI) (Protein III) (p68) (p70) 673 75,885 Chain (1); Initiator methionine (1); Modified residue (15); Repeat (8); Sequence conflict (3) FUNCTION: May associate with CD21. May regulate the release of Ca(2+) from intracellular stores. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Melanosome {ECO:0000250}. DOMAIN: A pair of annexin repeats may form one binding site for calcium and phospholipid. +Q812C9 AOC2_MOUSE Retina-specific copper amine oxidase (RAO) (EC 1.4.3.21) (Amine oxidase [copper-containing]) 757 83,583 Active site (2); Chain (1); Disulfide bond (3); Glycosylation (5); Metal binding (12); Modified residue (1); Region (3); Sequence conflict (2); Signal peptide (1) FUNCTION: Has a monoamine oxidase activity with substrate specificity for 2-phenylethylamine and tryptamine. May play a role in adipogenesis. May be a critical modulator of signal transmission in retina (By similarity). {ECO:0000250}. PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue. {ECO:0000250|UniProtKB:P12807}. SUBUNIT: Homodimer; disulfide-linked (By similarity). Forms a heterodimer with AOC3 (By similarity). {ECO:0000250|UniProtKB:O75106, ECO:0000250|UniProtKB:P19801}. TISSUE SPECIFICITY: Significantly much highly expressed in retina. +P59672 ANS1A_MOUSE Ankyrin repeat and SAM domain-containing protein 1A (Odin) 1150 125,242 Alternative sequence (3); Chain (1); Compositional bias (1); Domain (3); Erroneous initiation (1); Helix (6); Initiator methionine (1); Modified residue (14); Repeat (6); Turn (1) FUNCTION: Regulator of different signaling pathways. Regulates EPHA8 receptor tyrosine kinase signaling to control cell migration and neurite retraction. {ECO:0000269|PubMed:17875921}. PTM: Phosphorylated on tyrosine residues in response to EGF and PDGF. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell projection {ECO:0000269|PubMed:17875921}. Note=Cytoplasmic before and after growth factor treatment. {ECO:0000250}. SUBUNIT: Interacts (via SAM domain) with EPHA2 (via SAM domain) (By similarity). Interacts with EPHA8; EPHA8 kinase activity-independent but stimulated by EPHA8 ubiquitination (PubMed:17875921). Interacts (via SAM domain) with EPHA6 (via SAM domain) (PubMed:29749928). {ECO:0000250|UniProtKB:Q92625, ECO:0000269|PubMed:17875921, ECO:0000269|PubMed:29749928}. +Q3U3N6 AP4AT_MOUSE AP-4 complex accessory subunit Tepsin (ENTH domain-containing protein 2) 573 60,761 Chain (1); Compositional bias (1); Domain (1); Frameshift (1); Modified residue (1); Region (2); Sequence conflict (6) FUNCTION: Associates with the adapter-like complex 4 (AP-4) and may therefore play a role in vesicular trafficking of proteins at the trans-Golgi network. {ECO:0000250|UniProtKB:Q96N21}. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q96N21}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q96N21}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q96N21}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q96N21}. Note=Extensively colocalizes with AP-4 which mediates the recruitment of TEPSIN to the trans-Golgi network. {ECO:0000250|UniProtKB:Q96N21}. SUBUNIT: Interacts with AP4B1 and AP4E1; the interaction is direct and mediates the association of TEPSIN with the adapter-like complex 4 (AP-4), a heterotetramer composed of AP4B1, AP4E1, AP4M1 and AP4S1. {ECO:0000250|UniProtKB:Q96N21}. +Q9D504 ANKR7_MOUSE Ankyrin repeat domain-containing protein 7 279 31,202 Chain (1); Repeat (5); Sequence conflict (4) +Q8BH83 ANKR9_MOUSE Ankyrin repeat domain-containing protein 9 326 35,513 Chain (1); Compositional bias (1); Repeat (3) +Q61312 AP2C_MOUSE Transcription factor AP-2 gamma (AP2-gamma) (AP-2.2) (Activating enhancer-binding protein 2 gamma) 449 49,137 Chain (1); Compositional bias (1); Cross-link (1); Modified residue (2); Motif (1); Region (1); Sequence conflict (1) FUNCTION: Sequence-specific DNA-binding protein that interacts with inducible viral and cellular enhancer elements to regulate transcription of selected genes. AP-2 factors bind to the consensus sequence 5'-GCCNNNGGC-3' and activate genes involved in a large spectrum of important biological functions including proper eye, face, body wall, limb and neural tube development. They also suppress a number of genes including MCAM/MUC18, C/EBP alpha and MYC. PTM: Sumoylated on Lys-10; which inhibits transcriptional activity. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Binds DNA as a dimer. Can form homodimers or heterodimers with other AP-2 family members. Interacts with WWOX. Interacts with UBE2I (By similarity). Interacts with CITED4. Interacts with KCTD1; this interaction represses transcription activation. Interacts with CITED2 (via C-terminus); the interaction stimulates TFAP2B-transcriptional activity. Interacts with MTA1 (By similarity). {ECO:0000250}. DOMAIN: The PPxY motif mediates interaction with WWOX. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in lung, ovary and testis. Expressed in most squamous epithelia. Also, detected in several exocrine glands including the prostate, the preputial and salivary glands, serous glands of the tongue and ocular harderian glands. +Q3UMR0 ANR27_MOUSE Ankyrin repeat domain-containing protein 27 (VPS9 domain-containing protein) (VPS9-ankyrin-repeat protein) 1048 116,809 Alternative sequence (2); Chain (1); Domain (1); Frameshift (1); Modified residue (3); Mutagenesis (6); Region (6); Repeat (11); Sequence conflict (6) FUNCTION: May be a guanine exchange factor (GEF) for Rab21, Rab32 and Rab38 and regulate endosome dynamics (By similarity). May regulate the participation of VAMP7 in membrane fusion events; in vitro inhibits VAMP7-mediated SNARE complex formation by trapping VAMP7 in a closed, fusogenically inactive conformation (By similarity). Involved in peripheral melanosomal distribution of TYRP1 in melanocytes; the function, which probably is implicating vesicle-trafficking, includes cooperation with Rab32, Rab38 and VAMP7 (PubMed:19403694, PubMed:21187289). Involved in the regulation of neurite growth; the function seems to require its GEF activity, probably towards Rab21, and VAMP7 but not Rab32/38 (PubMed:19745841, PubMed:22171327). Proposed to be involved in Golgi sorting of VAMP7 and transport of VAMP7 vesicles to the cell surface; the function seems to implicate kinesin heavy chain isoform 5 proteins, GOLGA4, RAB21 and MACF1. Required for the colocalization of VAMP7 and Rab21, probably on TGN sites (By similarity). Involved in GLUT1 endosome-to-plasma membrane trafficking; the function is dependent of association with VPS29 (By similarity). Regulates the proper trafficking of melanogenic enzymes TYR, TYRP1 and DCT/TYRP2 to melanosomes in melanocytes (PubMed:26620560). {ECO:0000250|UniProtKB:Q96NW4, ECO:0000269|PubMed:19403694, ECO:0000269|PubMed:21187289, ECO:0000269|PubMed:26620560}. SUBCELLULAR LOCATION: Early endosome {ECO:0000250|UniProtKB:Q96NW4}. Late endosome {ECO:0000250|UniProtKB:Q96NW4}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q96NW4}. Lysosome {ECO:0000250|UniProtKB:Q96NW4}. Cell membrane {ECO:0000250|UniProtKB:Q96NW4}. Melanosome {ECO:0000269|PubMed:19403694}. Cytoplasmic vesicle {ECO:0000269|PubMed:19403694}. Note=Colocalizes with VAMP7 in transport vesicles in the shaft of hippocampal neurons. {ECO:0000269|PubMed:19745841}. SUBUNIT: Interacts with RAB21 (GDP-bound form), VPS29, KIF5A, KIF5C, GOLGA4 (By similarity). Interacts with RAB32 (GTP-bound form), RAB38 (GTP-bound form), VAMP7 (PubMed:19403694, PubMed:21187289). Interacts with low affinity with RAB5 (By similarity). ANKRD27:RAB32 heterodimers can homodimerize to form tetramers (By similarity). Can interact with RAB38 or RAB32, VPS29 and VAMP7 simultaneously (By similarity). A decreased interaction with RAB32 seen in the presence of SGSM2 (By similarity). {ECO:0000250|UniProtKB:Q96NW4, ECO:0000269|PubMed:16525121, ECO:0000269|PubMed:19403694, ECO:0000269|PubMed:21187289}. +Q3U829 AP5Z1_MOUSE AP-5 complex subunit zeta-1 (Adaptor-related protein complex 5 zeta subunit) (Zeta5) 807 89,407 Chain (1); Compositional bias (1); Erroneous initiation (1); Sequence conflict (4) FUNCTION: As part of AP-5, a probable fifth adaptor protein complex it may be involved in endosomal transport. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Probably part of the adaptor protein complex 5 (AP-5) a tetramer composed of AP5B1, AP5M1, AP5S1 and AP5Z1. Interacts with ZFYVE26 and SPG11 (By similarity). {ECO:0000250}. +P60007 APC15_MOUSE Anaphase-promoting complex subunit 15 (APC15) 132 15,378 Alternative sequence (1); Chain (1); Compositional bias (1) FUNCTION: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. In the complex, plays a role in the release of the mitotic checkpoint complex (MCC) from the APC/C: not required for APC/C activity itself, but promotes the turnover of CDC20 and MCC on the APC/C, thereby participating in the responsiveness of the spindle assembly checkpoint. Also required for degradation of CDC20 (By similarity). {ECO:0000250}. SUBUNIT: The mammalian APC/C is composed at least of 14 distinct subunits ANAPC1, ANAPC2, CDC27/APC3, ANAPC4, ANAPC5, CDC16/APC6, ANAPC7, CDC23/APC8, ANAPC10, ANAPC11, CDC26/APC12, ANAPC13, ANAPC15 and ANAPC16 that assemble into a complex of at least 19 chains with a combined molecular mass of around 1.2 MDa; APC/C interacts with FZR1 and FBXO5. {ECO:0000250|UniProtKB:P60006}. +Q06335 APLP2_MOUSE Amyloid-like protein 2 (APLP-2) (CDEI box-binding protein) (CDEBP) 707 80,467 Alternative sequence (1); Chain (1); Compositional bias (3); Disulfide bond (6); Domain (2); Glycosylation (1); Metal binding (3); Modified residue (2); Motif (1); Region (3); Sequence conflict (6); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 637 660 Helical. {ECO:0000255}. TOPO_DOM 32 636 Extracellular. {ECO:0000255}.; TOPO_DOM 661 707 Cytoplasmic. {ECO:0000255}. FUNCTION: May play a role in the regulation of hemostasis. The soluble form may have inhibitory properties towards coagulation factors. May interact with cellular G-protein signaling pathways. May bind to the DNA 5'-GTCACATG-3'(CDEI box). Inhibits trypsin, chymotrypsin, plasmin, factor XIA and plasma and glandular kallikrein (By similarity). Modulates the Cu/Zn nitric oxide-catalyzed autodegradation of GPC1 heparan sulfate side chains in fibroblasts. {ECO:0000250, ECO:0000269|PubMed:15677459}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Nucleus {ECO:0000305}. SUBUNIT: Interacts with CPEB1. Interacts (via NPXY motif) with DAB2 (via PID domain); the interaction is impaired by tyrosine phosphorylation of the NPXY motif. {ECO:0000269|PubMed:11247302, ECO:0000269|PubMed:16314516}. +Q7TPR4 ACTN1_MOUSE Alpha-actinin-1 (Alpha-actinin cytoskeletal isoform) (F-actin cross-linking protein) (Non-muscle alpha-actinin-1) 892 103,068 Calcium binding (2); Chain (1); Domain (4); Modified residue (9); Mutagenesis (2); Region (2); Repeat (4) FUNCTION: F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:23100251}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:11114196}. Cell membrane {ECO:0000250|UniProtKB:Q9Z1P2}. Cell junction {ECO:0000250|UniProtKB:Q9Z1P2}. Cell projection, ruffle {ECO:0000269|PubMed:17298598}. Note=Colocalizes with MYOZ2 and PPP3CA at the Z-line of heart and skeletal muscle (PubMed:11114196). Colocalizes with PSD in membrane ruffles and central reticular structures (PubMed:17298598). {ECO:0000269|PubMed:11114196, ECO:0000269|PubMed:17298598}. SUBUNIT: Homodimer; antiparallel. Interacts with MYOZ2, TTID and LPP. Interacts with DDN (By similarity). Interacts with PSD (PubMed:17298598). Interacts with MICALL2 (PubMed:23100251). Interacts with DNM2 and CTTN. Interacts with PDLIM1. Interacts with PDLIM2. Interacts with PDLIM4 (via PDZ domain) (By similarity). {ECO:0000250|UniProtKB:P12814, ECO:0000250|UniProtKB:Q9Z1P2, ECO:0000269|PubMed:17298598, ECO:0000269|PubMed:23100251}. +P57780 ACTN4_MOUSE Alpha-actinin-4 (Non-muscle alpha-actinin 4) 912 104,977 Calcium binding (2); Chain (1); Domain (4); Modified residue (10); Motif (1); Region (6); Repeat (4) FUNCTION: F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein. Probably involved in vesicular trafficking via its association with the CART complex. The CART complex is necessary for efficient transferrin receptor recycling but not for EGFR degradation (By similarity). Involved in tight junction assembly in epithelial cells probably through interaction with MICALL2. Links MICALL2 to the actin cytoskeleton and recruits it to the tight junctions (PubMed:18332111). May also function as a transcriptional coactivator, stimulating transcription mediated by the nuclear hormone receptors PPARG and RARA (By similarity). {ECO:0000250|UniProtKB:O43707, ECO:0000269|PubMed:18332111}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O43707}. Cytoplasm {ECO:0000250|UniProtKB:O43707}. Cell junction {ECO:0000269|PubMed:18332111}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:O43707}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. {ECO:0000250|UniProtKB:O43707}. SUBUNIT: Homodimer; antiparallel (By similarity). Interacts with BAIAP1 and PDLIM2 (By similarity). Identified in a complex with CASK, IQGAP1, MAGI2, NPHS1, SPTAN1 and SPTBN1 (By similarity). Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Component of the CART complex, at least composed of ACTN4, HGS/HRS, MYO5B and TRIM3. Binds TRIM3 at the N-terminus. Interacts with MICALL2 (preferentially in opened conformation); stimulated by RAB13 activation. Interacts with PPARG and RARA (By similarity). Binds to VCL; this interaction triggers VCL conformational changes (By similarity). {ECO:0000250|UniProtKB:O43707, ECO:0000250|UniProtKB:Q9QXQ0, ECO:0000269|PubMed:18332111}. DOMAIN: Contains one Leu-Xaa-Xaa-Leu-Leu (LXXLL) motif that mediates interaction with nuclear receptors. {ECO:0000250|UniProtKB:O43707}. +P34971 ADRB1_MOUSE Beta-1 adrenergic receptor (Beta-1 adrenoreceptor) (Beta-1 adrenoceptor) 466 50,494 Binding site (2); Chain (1); Disulfide bond (2); Glycosylation (1); Lipidation (1); Modified residue (4); Motif (1); Region (3); Sequence conflict (1); Topological domain (8); Transmembrane (7) TRANSMEM 56 84 Helical; Name=1. {ECO:0000250}.; TRANSMEM 94 120 Helical; Name=2. {ECO:0000250}.; TRANSMEM 133 154 Helical; Name=3. {ECO:0000250}.; TRANSMEM 173 196 Helical; Name=4. {ECO:0000250}.; TRANSMEM 223 248 Helical; Name=5. {ECO:0000250}.; TRANSMEM 309 338 Helical; Name=6. {ECO:0000250}.; TRANSMEM 344 366 Helical; Name=7. {ECO:0000250}. TOPO_DOM 1 55 Extracellular. {ECO:0000250}.; TOPO_DOM 85 93 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 121 132 Extracellular. {ECO:0000250}.; TOPO_DOM 155 172 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 197 222 Extracellular. {ECO:0000250}.; TOPO_DOM 249 308 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 339 343 Extracellular. {ECO:0000250}.; TOPO_DOM 367 466 Cytoplasmic. {ECO:0000250}. FUNCTION: Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. This receptor binds epinephrine and norepinephrine with approximately equal affinity. Mediates Ras activation through G(s)-alpha- and cAMP-mediated signaling (By similarity). {ECO:0000250}. PTM: Homologous desensitization of the receptor is mediated by its phosphorylation by beta-adrenergic receptor kinase. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Early endosome {ECO:0000250}. Note=Colocalizes with RAPGEF2 at the plasma membrane. Found in the Golgi upon GOPC overexpression (By similarity). {ECO:0000250}. SUBUNIT: Interacts (via C-terminus PDZ motif) with RAPGEF2; the interaction is direct. Interacts with GOPC, MAGI3 and DLG4 (By similarity). {ECO:0000250}. DOMAIN: The PDZ domain-binding motif mediates competitive interactions with GOPC, MAGI3 and DLG4 and plays a role in subcellular location of the receptor. {ECO:0000250}. +Q60813 ADM1A_MOUSE Disintegrin and metalloproteinase domain-containing protein 1a (ADAM 1a) (EC 3.4.24.-) (Fertilin subunit alpha-a) 791 87,490 Active site (1); Chain (1); Compositional bias (1); Disulfide bond (7); Domain (3); Glycosylation (5); Metal binding (3); Propeptide (1); Sequence conflict (5); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 741 761 Helical. {ECO:0000255}. TOPO_DOM ? 740 Extracellular. {ECO:0000255}.; TOPO_DOM 762 791 Cytoplasmic. {ECO:0000255}. FUNCTION: May be involved in sperm-egg fusion. {ECO:0000269|PubMed:8146185}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Heterodimer with ADAM2/fertilin subunit beta. TISSUE SPECIFICITY: Testis. {ECO:0000269|PubMed:12095680}. +Q91ZE5 AGRE4_MOUSE Adhesion G protein-coupled receptor E4 (EGF-like module receptor 4) (EGF-like module-containing mucin-like hormone receptor-like 4) (F4/80-like-receptor) (Seven-span membrane protein FIRE) 689 77,045 Chain (1); Disulfide bond (6); Domain (3); Erroneous initiation (1); Glycosylation (8); Sequence conflict (1); Signal peptide (1); Site (1); Topological domain (8); Transmembrane (7) TRANSMEM 351 371 Helical; Name=1. {ECO:0000255}.; TRANSMEM 380 400 Helical; Name=2. {ECO:0000255}.; TRANSMEM 408 428 Helical; Name=3. {ECO:0000255}.; TRANSMEM 456 476 Helical; Name=4. {ECO:0000255}.; TRANSMEM 500 520 Helical; Name=5. {ECO:0000255}.; TRANSMEM 545 565 Helical; Name=6. {ECO:0000255}.; TRANSMEM 571 591 Helical; Name=7. {ECO:0000255}. TOPO_DOM 38 350 Extracellular. {ECO:0000255}.; TOPO_DOM 372 379 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 401 407 Extracellular. {ECO:0000255}.; TOPO_DOM 429 455 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 477 499 Extracellular. {ECO:0000255}.; TOPO_DOM 521 544 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 566 570 Extracellular. {ECO:0000255}.; TOPO_DOM 592 689 Cytoplasmic. {ECO:0000255}. FUNCTION: May mediate the cellular interaction between myeloid cells and B-cells. {ECO:0000269|PubMed:12023293}. PTM: Proteolytically cleaved into 2 subunits, an extracellular alpha subunit and a seven-transmembrane subunit. {ECO:0000269|PubMed:12023293}.; PTM: Glycosylated. {ECO:0000269|PubMed:12023293}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12023293}; Multi-pass membrane protein. SUBUNIT: Forms a heterodimer, consisting of a large extracellular region (alpha subunit) non-covalently linked to a seven-transmembrane moiety (beta subunit). {ECO:0000269|PubMed:12023293}. DOMAIN: The second EGF domain mediates the interaction with the putative ligand. {ECO:0000269|PubMed:12023293}. TISSUE SPECIFICITY: Predominantly expressed in myeloid cells. Predominantly expressed on resident macrophages. {ECO:0000269|PubMed:11564768, ECO:0000269|PubMed:12023293}. +Q8C138 ADTRP_MOUSE Androgen-dependent TFPI-regulating protein 230 27,003 Chain (1); Erroneous gene model prediction (1); Erroneous initiation (1); Transmembrane (6) TRANSMEM 8 28 Helical. {ECO:0000255}.; TRANSMEM 46 66 Helical. {ECO:0000255}.; TRANSMEM 86 106 Helical. {ECO:0000255}.; TRANSMEM 121 141 Helical. {ECO:0000255}.; TRANSMEM 155 175 Helical. {ECO:0000255}.; TRANSMEM 191 211 Helical. {ECO:0000255}. FUNCTION: Regulates the expression and the cell-associated anticoagulant activity of the inhibitor TFPI in endothelial cells (in vitro). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Colocalized with TFPI and CAV1 in lipid rafts. {ECO:0000250}. +P31230 AIMP1_MOUSE Aminoacyl tRNA synthase complex-interacting multifunctional protein 1 (Multisynthase complex auxiliary component p43) [Cleaved into: Endothelial monocyte-activating polypeptide 2 (EMAP-2) (Endothelial monocyte-activating polypeptide II) (EMAP-II) (Small inducible cytokine subfamily E member 1)] 310 33,997 Chain (2); Domain (1); Initiator methionine (1); Modified residue (3); Region (4) FUNCTION: Non-catalytic component of the multisynthase complex (PubMed:12060739). Stimulates the catalytic activity of cytoplasmic arginyl-tRNA synthase (By similarity). Binds tRNA. Possesses inflammatory cytokine activity (PubMed:1400342, PubMed:7545917). Negatively regulates TGF-beta signaling through stabilization of SMURF2 by binding to SMURF2 and inhibiting its SMAD7-mediated degradation (PubMed:18448069). Involved in glucose homeostasis through induction of glucagon secretion at low glucose levels (PubMed:17001013). Promotes dermal fibroblast proliferation and wound repair (PubMed:15681823). Regulates KDELR1-mediated retention of HSP90B1/gp96 in the endoplasmic reticulum (PubMed:17525271). Plays a role in angiogenesis by inducing endothelial cell migration at low concentrations and endothelian cell apoptosis at high concentrations (By similarity). Induces maturation of dendritic cells and monocyte cell adhesion (PubMed:18292511). Modulates endothelial cell responses by degrading HIF-1A through interaction with PSMA7 (By similarity). {ECO:0000250|UniProtKB:Q12904, ECO:0000269|PubMed:12060739, ECO:0000269|PubMed:1400342, ECO:0000269|PubMed:15681823, ECO:0000269|PubMed:17001013, ECO:0000269|PubMed:17525271, ECO:0000269|PubMed:18292511, ECO:0000269|PubMed:18448069, ECO:0000269|PubMed:7545917}. PTM: Cleaved by caspase-7 in response to apoptosis to produce EMAP-II. {ECO:0000269|PubMed:11306575}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q12904}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q12904}. Secreted {ECO:0000269|PubMed:17001013, ECO:0000269|PubMed:9770485}. Endoplasmic reticulum {ECO:0000269|PubMed:17525271}. Golgi apparatus {ECO:0000269|PubMed:17525271}. Note=Enriched in secretory vesicles of pancreatic alpha cells and secreted from the pancreas in response to low glucose levels (PubMed:17001013). Secreted in response to hypoxia (By similarity). Also secreted in response to both apoptotic and necrotic cell death. {ECO:0000250|UniProtKB:Q12904, ECO:0000269|PubMed:17001013}. SUBUNIT: Homodimer. Part of the multisynthetase complex (MSC), a multisubunit complex that groups tRNA ligases for Arg (RARS), Asp (DARS), Gln (QARS), Ile (IARS), Leu (LARS), Lys (KARS), Met (MARS) the bifunctional ligase for Glu and Pro (EPRS) and the auxiliary subunits AIMP1/p43, AIMP2/p38 and EEF1E1/p18 (PubMed:12060739). Interacts (via N-terminus) with RARS (via N-terminus). Part of a complex composed of RARS, QARS and AIMP1. Interacts (via C-terminus) with SMURF2 (PubMed:18448069). Interacts (via N-terminus) with HSP90B1/gp96 (via C-terminus) (PubMed:17525271). Interacts with PSMA7 (By similarity). Interacts with TARSL2. {ECO:0000250|UniProtKB:Q12904, ECO:0000269|PubMed:12060739, ECO:0000269|PubMed:17525271, ECO:0000269|PubMed:18448069}. TISSUE SPECIFICITY: Highly expressed in salivary glands and pancreatic alpha cells in the adult (at protein level) (PubMed:17001013). In the embryo, expressed primarily at sites of tissue remodeling such as ganglia, developing bones and teeth (PubMed:9770485). {ECO:0000269|PubMed:17001013, ECO:0000269|PubMed:9770485}. +Q9DBR0 AKAP8_MOUSE A-kinase anchor protein 8 (AKAP-8) (A-kinase anchor protein 95 kDa) (AKAP 95) 687 76,294 Chain (1); Cross-link (1); Modified residue (11); Motif (1); Region (7); Sequence conflict (6); Zinc finger (2) FUNCTION: Anchoring protein that mediates the subcellular compartmentation of cAMP-dependent protein kinase (PKA type II). Acts as an anchor for a PKA-signaling complex onto mitotic chromosomes, which is required for maintenance of chromosomes in a condensed form throughout mitosis. Recruits condensin complex subunit NCAPD2 to chromosomes required for chromatin condensation; the function appears to be independent from PKA-anchoring (By similarity). Specifically involved in recruitment of CAPD2 to, and condensation of maternal but not paternal chromosomes (PubMed:12082153). May help to deliver cyclin D/E to CDK4 to facilitate cell cycle progression (PubMed:14641107). Required for cell cycle G2/M transition and histone deacetylation during mitosis. In mitotic cells recruits HDAC3 to the vicinity of chromatin leading to deacetylation and subsequent phosphorylation at 'Ser-10' of histone H3; in this function may act redundantly with AKAP8L. Involved in nuclear retention of RPS6KA1 upon ERK activation thus inducing cell proliferation. May be involved in regulation of DNA replication by acting as scaffold for MCM2. Enhances HMT activity of the KMT2 family MLL4/WBP7 complex and is involved in transcriptional regulation. In a teratocarcinoma cell line is involved in retinoic acid-mediated induction of developmental genes implicating H3 'Lys-4' methylation. May be involved in recruitment of active CASP3 to the nucleus in apoptotic cells. May act as a carrier protein of GJA1 for its transport to the nucleus. Seems to involved in modulation of rDNA transcription. Preferentially binds GC-rich DNA in vitro and associates to GC-rich ribosomal RNA promoters (By similarity). Involved in modulation of Toll-like receptor signaling. Required for the cAMP-dependent suppression of TNF-alpha in early stages of LPS-induced macrophage activation; the function probably implicates targeting of PKA to NFKB1 (PubMed:19531803). {ECO:0000250|UniProtKB:O43823, ECO:0000250|UniProtKB:Q63014}. PTM: Phosphorylated on tyrosine residues probably by SRC subfamily protein kinases; multiple phosphorylation is leading to dissociation from nuclear structures implicated in chromatin structural changes. {ECO:0000250|UniProtKB:O43823}. SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000269|PubMed:16751186}. Nucleus, nucleolus {ECO:0000250|UniProtKB:O43823}. Cytoplasm {ECO:0000269|PubMed:19531803}. Note=Associated with the nuclear matrix. Redistributed and detached from condensed chromatin during mitosis (By similarity). Localizes specifically to the vicinity of the meiotic spindle in metaphase II oocytes. {ECO:0000250|UniProtKB:O43823, ECO:0000269|PubMed:12082153}. SUBUNIT: Binds to the PKA RII-alpha regulatory subunit PRKAR2A (By similarity). Interacts (via C-terminus) with FIGN (PubMed:16751186). Interacts with NCAPD2, CCND3, CCNE1, MCM2, RPS6KA1, DDX5, PDE4A (By similarity). Interacts with MYCBP; MYCBP is translocated to the nucleus and the interaction prevents the association of the PKA catalytic subunit leading to suppression of PKA activity (PubMed:12414807). Interacts with CCND1, CASP3 (PubMed:14641107, PubMed:16227597). Interacts with NFKB1; detetcted in the cytoplasm (PubMed:19531803). Interacts with DPY30; mediating AKAP8 association with at least the MLL4/WBP7 HMT complex. Interacts with HDAC3; increased during mitosis. Interacts with GJA1; in the nucleus and in the nuclear membrane; the nuclear association increases with progress of cell cycle G1, S and G2 phase and decreases in M phase (By similarity). {ECO:0000250|UniProtKB:O43823, ECO:0000250|UniProtKB:Q5VK71, ECO:0000250|UniProtKB:Q63014, ECO:0000269|PubMed:12414807, ECO:0000269|PubMed:14641107, ECO:0000269|PubMed:16227597, ECO:0000269|PubMed:16751186, ECO:0000269|PubMed:19531803}. +Q8VCX1 AK1D1_MOUSE 3-oxo-5-beta-steroid 4-dehydrogenase (EC 1.3.1.3) (Aldo-keto reductase family 1 member D1) (Delta(4)-3-ketosteroid 5-beta-reductase) (Delta(4)-3-oxosteroid 5-beta-reductase) 325 37,290 Active site (1); Binding site (8); Chain (1); Modified residue (1); Nucleotide binding (4) FUNCTION: Efficiently catalyzes the reduction of progesterone, androstenedione, 17-alpha-hydroxyprogesterone and testosterone to 5-beta-reduced metabolites. The bile acid intermediates 7-alpha,12-alpha-dihydroxy-4-cholesten-3-one and 7-alpha-hydroxy-4-cholesten-3-one can also act as substrates. {ECO:0000250|UniProtKB:P51857}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +Q921Q3 ALG1_MOUSE Chitobiosyldiphosphodolichol beta-mannosyltransferase (EC 2.4.1.142) (Asparagine-linked glycosylation protein 1 homolog) (Beta-1,4-mannosyltransferase) (GDP-Man:GlcNAc2-PP-dolichol mannosyltransferase) (GDP-mannose-dolichol diphosphochitobiose mannosyltransferase) 482 54,417 Alternative sequence (1); Chain (1); Frameshift (1); Modified residue (1); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 3 23 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 2 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 24 482 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. Involved in assembling the dolichol-pyrophosphate-GlcNAc(2)-Man(5) intermediate on the cytoplasmic surface of the ER (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. +Q9R0L7 AKP8L_MOUSE A-kinase anchor protein 8-like (AKAP8-like protein) (Neighbor of A-kinase-anchoring protein 95) (Neighbor of AKAP95) 642 71,454 Chain (1); Compositional bias (3); Modified residue (10); Motif (3); Region (1); Zinc finger (2) FUNCTION: Could play a role in constitutive transport element (CTE)-mediated gene expression by association with DHX9. Increases CTE-dependent nuclear unspliced mRNA export. Proposed to target PRKACA to the nucleus but does not seem to be implicated in the binding of regulatory subunit II of PKA. May be involved in nuclear envelope breakdown and chromatin condensation. May be involved in anchoring nuclear membranes to chromatin in interphase and in releasing membranes from chromating at mitosis. May regulate the initiation phase of DNA replication when associated with TMPO isoform Beta. Required for cell cycle G2/M transition and histone deacetylation during mitosis. In mitotic cells recruits HDAC3 to the vicinity of chromatin leading to deacetylation and subsequent phosphorylation at 'Ser-10' of histone H3; in this function seems to act redundantly with AKAP8. May be involved in regulation of pre-mRNA splicing (By similarity). {ECO:0000250|UniProtKB:Q9ULX6}. PTM: Phosphorylated on serine or threonine residues possibly by PKA. {ECO:0000250|UniProtKB:Q9ULX6}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9ULX6}. Nucleus matrix {ECO:0000250|UniProtKB:Q9ULX6}. Nucleus speckle {ECO:0000250|UniProtKB:Q9ULX6}. Nucleus, PML body {ECO:0000250|UniProtKB:Q9ULX6}. Cytoplasm {ECO:0000250|UniProtKB:Q9ULX6}. Note=Colocalizes with PRPF40A in the nuclear matrix. Nuclear at steady state but shuttles between the nucleus and cytoplasm. The shuttling property has been questioned. Colocalizes with EBNA-LP in PML bodies. {ECO:0000250|UniProtKB:Q9ULX6}. SUBUNIT: Interacts (via N-terminus) with DHX9 (via RGG region). Interacts with TMPO isoform Beta, PRPF40A, RNF43, lamin-B. Interacts with HDAC3; increased during mitosis (By similarity). {ECO:0000250|UniProtKB:Q9ULX6}. +P47740 AL3A2_MOUSE Fatty aldehyde dehydrogenase (EC 1.2.1.3) (Aldehyde dehydrogenase 3) (Aldehyde dehydrogenase family 3 member A2) 484 53,971 Active site (2); Chain (1); Modified residue (1); Motif (1); Nucleotide binding (1); Sequence conflict (3); Topological domain (1); Transmembrane (1) TRANSMEM 464 484 Helical. {ECO:0000255}. TOPO_DOM 1 463 Cytoplasmic. FUNCTION: Catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Active on a variety of saturated and unsaturated aliphatic aldehydes between 6 and 24 carbons in length (PubMed:25286108). Responsible for conversion of the sphingosine 1-phosphate (S1P) degradation product hexadecenal to hexadecenoic acid (PubMed:25286108). {ECO:0000269|PubMed:25286108}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:25286108}. Microsome membrane {ECO:0000250|UniProtKB:P51648}; Single-pass membrane protein {ECO:0000250|UniProtKB:P51648}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P51648}; Single-pass membrane protein {ECO:0000250|UniProtKB:P51648}; Cytoplasmic side {ECO:0000250|UniProtKB:P30839}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P51648}. +Q3TAE8 ALG6_MOUSE Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase (EC 2.4.1.267) (Asparagine-linked glycosylation protein 6 homolog) (Dol-P-Glc:Man(9)GlcNAc(2)-PP-Dol alpha-1,3-glucosyltransferase) (Dolichyl-P-Glc:Man9GlcNAc2-PP-dolichyl glucosyltransferase) 507 57,874 Chain (1); Sequence conflict (1); Transmembrane (11) TRANSMEM 4 24 Helical. {ECO:0000255}.; TRANSMEM 115 135 Helical. {ECO:0000255}.; TRANSMEM 144 164 Helical. {ECO:0000255}.; TRANSMEM 173 193 Helical. {ECO:0000255}.; TRANSMEM 227 247 Helical. {ECO:0000255}.; TRANSMEM 298 318 Helical. {ECO:0000255}.; TRANSMEM 324 344 Helical. {ECO:0000255}.; TRANSMEM 362 382 Helical. {ECO:0000255}.; TRANSMEM 388 408 Helical. {ECO:0000255}.; TRANSMEM 438 458 Helical. {ECO:0000255}.; TRANSMEM 473 493 Helical. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Adds the first glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Man(9)GlcNAc(2)-PP-Dol (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q7TN79 AKA7G_MOUSE A-kinase anchor protein 7 isoform gamma (AKAP-7 isoform gamma) (A-kinase anchor protein 18) (AKAP-18) (Protein kinase A-anchoring protein 7 isoform gamma) (PRKA7 isoform gamma) 314 35,482 Binding site (2); Chain (1); Mutagenesis (4); Nucleotide binding (2); Region (3); Sequence conflict (2) FUNCTION: Probably targets cAMP-dependent protein kinase (PKA) to the cellular membrane or cytoskeletal structures. The membrane-associated form reduces epithelial sodium channel (ENaC) activity, whereas the free cytoplasmic form may negatively regulate ENaC channel feedback inhibition by intracellular sodium (By similarity). {ECO:0000250|UniProtKB:Q9P0M2, ECO:0000305}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12804576}. Cytoplasm {ECO:0000269|PubMed:12804576}. Note=In oocytes, localizes to the nucleus, to germinal vesicles and throughout the cytoplasm. {ECO:0000269|PubMed:12804576}. SUBUNIT: Binds cAMP-dependent protein kinase (PKA). Interacts with PRKCA; only the cytoplasmic form is capable of interacting with PRKCA (By similarity). {ECO:0000250|UniProtKB:Q9P0M2, ECO:0000269|PubMed:12804576}. TISSUE SPECIFICITY: Expressed in oocytes. {ECO:0000269|PubMed:12804576}. +P61164 ACTZ_MOUSE Alpha-centractin (Centractin) (ARP1) (Actin-RPV) (Centrosome-associated actin homolog) 376 42,614 Chain (1); Modified residue (1) FUNCTION: Component of a multi-subunit complex involved in microtubule based vesicle motility. It is associated with the centrosome. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P85515}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P85515}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:P61163}. SUBUNIT: Interacts with BCCIP. {ECO:0000250|UniProtKB:P61163}. +Q01338 ADA2A_MOUSE Alpha-2A adrenergic receptor (Alpha-2A adrenoreceptor) (Alpha-2A adrenoceptor) (Alpha-2AAR) 450 48,865 Chain (1); Disulfide bond (1); Glycosylation (2); Lipidation (1); Modified residue (2); Site (3); Topological domain (8); Transmembrane (7) TRANSMEM 34 59 Helical; Name=1. {ECO:0000250}.; TRANSMEM 71 96 Helical; Name=2. {ECO:0000250}.; TRANSMEM 107 129 Helical; Name=3. {ECO:0000250}.; TRANSMEM 150 173 Helical; Name=4. {ECO:0000250}.; TRANSMEM 193 217 Helical; Name=5. {ECO:0000250}.; TRANSMEM 375 399 Helical; Name=6. {ECO:0000250}.; TRANSMEM 410 430 Helical; Name=7. {ECO:0000250}. TOPO_DOM 1 33 Extracellular. {ECO:0000250}.; TOPO_DOM 60 70 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 97 106 Extracellular. {ECO:0000250}.; TOPO_DOM 130 149 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 174 192 Extracellular. {ECO:0000250}.; TOPO_DOM 218 374 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 400 409 Extracellular. {ECO:0000250}.; TOPO_DOM 431 450 Cytoplasmic. {ECO:0000250}. FUNCTION: Alpha-2 adrenergic receptors mediate the catecholamine-induced inhibition of adenylate cyclase through the action of G proteins. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q8BGA8 ACSM5_MOUSE Acyl-coenzyme A synthetase ACSM5, mitochondrial (EC 6.2.1.2) 578 64,328 Alternative sequence (2); Binding site (3); Chain (1); Compositional bias (1); Modified residue (6); Nucleotide binding (2); Sequence conflict (6); Transit peptide (1) FUNCTION: Has medium-chain fatty acid:CoA ligase activity with broad substrate specificity (in vitro). Acts on acids from C(4) to C(11) and on the corresponding 3-hydroxy- and 2,3- or 3,4-unsaturated acids (in vitro) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. +Q8VHH7 ADCY3_MOUSE Adenylate cyclase type 3 (EC 4.6.1.1) (ATP pyrophosphate-lyase 3) (Adenylate cyclase type III) (AC-III) (Adenylate cyclase, olfactive type) (Adenylyl cyclase 3) (AC3) 1145 129,085 Binding site (3); Chain (1); Cross-link (1); Glycosylation (1); Metal binding (5); Modified residue (3); Mutagenesis (1); Nucleotide binding (4); Sequence conflict (2); Topological domain (3); Transmembrane (12) TRANSMEM 80 100 Helical. {ECO:0000255}.; TRANSMEM 105 125 Helical. {ECO:0000255}.; TRANSMEM 139 159 Helical. {ECO:0000255}.; TRANSMEM 173 193 Helical. {ECO:0000255}.; TRANSMEM 226 246 Helical. {ECO:0000255}.; TRANSMEM 381 401 Helical. {ECO:0000255}.; TRANSMEM 632 652 Helical. {ECO:0000255}.; TRANSMEM 663 683 Helical. {ECO:0000255}.; TRANSMEM 707 727 Helical. {ECO:0000255}.; TRANSMEM 753 773 Helical. {ECO:0000255}.; TRANSMEM 774 794 Helical. {ECO:0000255}.; TRANSMEM 834 854 Helical. {ECO:0000255}. TOPO_DOM 1 79 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 402 631 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 855 1145 Cytoplasmic. {ECO:0000255}. FUNCTION: Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling (PubMed:9768837, PubMed:11055432, PubMed:25329148). Participates in signaling cascades triggered by odorant receptors via its function in cAMP biosynthesis (PubMed:9768837, PubMed:11055432). Required for the perception of odorants (PubMed:11055432). Required for normal sperm motility and normal male fertility (PubMed:15705663). Plays a role in regulating insulin levels and body fat accumulation in response to a high fat diet (PubMed:25329148). {ECO:0000269|PubMed:11055432, ECO:0000269|PubMed:15705663, ECO:0000269|PubMed:9768837}. PTM: N-glycosylated. {ECO:0000269|PubMed:9768837}.; PTM: Rapidly phosphorylated after stimulation by odorants or forskolin. Phosphorylation by CaMK2 at Ser-1077 down-regulates enzyme activity. {ECO:0000269|PubMed:9768837}.; PTM: Sumoylated (PubMed:25908845). Sumoylation is required for targeting of olfactory cilia. {ECO:0000250|UniProtKB:P21932, ECO:0000269|PubMed:25908845}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:11055432}; Multi-pass membrane protein {ECO:0000305}. Cell projection, cilium {ECO:0000269|PubMed:11055432, ECO:0000269|PubMed:9768837}. Golgi apparatus {ECO:0000250|UniProtKB:P21932}. Cytoplasm {ECO:0000250|UniProtKB:O60266}. DOMAIN: The protein contains two modules with six transmembrane helices each; both are required for catalytic activity. Isolated N-terminal or C-terminal modules have no catalytic activity, but when they are brought together, enzyme activity is restored. The active site is at the interface of the two modules. {ECO:0000250|UniProtKB:P30803}. TISSUE SPECIFICITY: Detected in the acrosomal region of epididymal spermatozoa, the acrosomal region of round spermatids and in elongating spermatids (PubMed:15705663). Detected in cilia in the olfactory epithelium (at protein level) (PubMed:9768837, PubMed:11055432, PubMed:25908845). Detected in olfactory epithelium neurons (PubMed:11055432). Detected in brain, testis, late pachytene spermatocytes, round spermatids and elongating spermatids (PubMed:15705663). {ECO:0000269|PubMed:11055432, ECO:0000269|PubMed:15705663}. +Q8R3P0 ACY2_MOUSE Aspartoacylase (EC 3.5.1.15) (Aminoacylase-2) (ACY-2) 312 35,345 Active site (1); Binding site (3); Chain (1); Metal binding (3); Region (2); Sequence conflict (6) FUNCTION: Catalyzes the deacetylation of N-acetylaspartic acid (NAA) to produce acetate and L-aspartate. NAA occurs in high concentration in brain and its hydrolysis NAA plays a significant part in the maintenance of intact white matter (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +G3UZ78 ADGB_MOUSE Androglobin (Calpain-7-like protein) 1657 188,556 Alternative sequence (4); Chain (1); Coiled coil (1); Compositional bias (1); Domain (2) TISSUE SPECIFICITY: Strongly expressed in testis and lung. Weakly expressed in heart, brain, spleen, kidney and tongue. {ECO:0000269|PubMed:22115833}. +P84309 ADCY5_MOUSE Adenylate cyclase type 5 (EC 4.6.1.1) (ATP pyrophosphate-lyase 5) (Adenylate cyclase type V) (Adenylyl cyclase 5) 1262 139,122 Alternative sequence (1); Binding site (3); Chain (1); Coiled coil (1); Compositional bias (2); Domain (2); Glycosylation (5); Metal binding (5); Modified residue (6); Nucleotide binding (4); Sequence conflict (3); Topological domain (4); Transmembrane (12) TRANSMEM 197 217 Helical. {ECO:0000255}.; TRANSMEM 243 263 Helical. {ECO:0000255}.; TRANSMEM 269 289 Helical. {ECO:0000255}.; TRANSMEM 300 320 Helical. {ECO:0000255}.; TRANSMEM 326 346 Helical. {ECO:0000255}.; TRANSMEM 375 395 Helical. {ECO:0000255}.; TRANSMEM 764 784 Helical. {ECO:0000255}.; TRANSMEM 790 810 Helical. {ECO:0000255}.; TRANSMEM 837 857 Helical. {ECO:0000255}.; TRANSMEM 911 931 Helical. {ECO:0000255}.; TRANSMEM 936 956 Helical. {ECO:0000255}.; TRANSMEM 985 1005 Helical. {ECO:0000255}. TOPO_DOM 1 196 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 396 763 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 858 910 Extracellular. {ECO:0000255}.; TOPO_DOM 1006 1262 Cytoplasmic. {ECO:0000255}. FUNCTION: Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling. Mediates signaling downstream of ADRB1. Regulates the increase of free cytosolic Ca(2+) in response to increased blood glucose levels and contributes to the regulation of Ca(2+)-dependent insulin secretion. {ECO:0000250|UniProtKB:O95622}. PTM: Phosphorylated by RAF1. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P30803}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P30803}. Cell projection, cilium {ECO:0000269|PubMed:21670265}. SUBUNIT: Interacts with GNAS, GNB1 and GNG2 (By similarity). Part of a complex containing AKAP5, ADCY6, PDE4C and PKD2 (PubMed:21670265). Interacts with RAF1 (By similarity). {ECO:0000250|UniProtKB:O95622, ECO:0000269|PubMed:21670265}. DOMAIN: The protein contains two modules with six transmembrane helices each; both are required for catalytic activity. Isolated N-terminal or C-terminal guanylate cyclase domains have no catalytic activity, but when they are brought together, enzyme activity is restored. The active site is at the interface of the two domains. Both contribute substrate-binding residues, but the catalytic metal ions are bound exclusively via the N-terminal guanylate cyclase domain. {ECO:0000250|UniProtKB:P30803}. +Q5DTU0 AF1L2_MOUSE Actin filament-associated protein 1-like 2 (AFAP1-like protein 2) 825 92,175 Alternative sequence (1); Chain (1); Coiled coil (1); Domain (2); Erroneous initiation (2); Frameshift (1); Modified residue (5); Sequence conflict (1) FUNCTION: May play a role in a signaling cascade by enhancing the kinase activity of SRC. Contributes to SRC-regulated transcription activation (By similarity). {ECO:0000250}. PTM: Tyrosine phosphorylated (by SRC). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with SRC. Interacts with LCK when tyrosine phosphorylated (By similarity). {ECO:0000250}. +Q3V3Z3 AGRG5_MOUSE Adhesion G-protein coupled receptor G5 (G-protein coupled receptor 114) (G-protein coupled receptor PGR27) 524 58,675 Alternative sequence (1); Chain (1); Domain (1); Glycosylation (8); Mutagenesis (4); Sequence conflict (1); Signal peptide (1); Site (1); Topological domain (8); Transmembrane (7) TRANSMEM 247 267 Helical; Name=1. {ECO:0000255}.; TRANSMEM 285 305 Helical; Name=2. {ECO:0000255}.; TRANSMEM 320 340 Helical; Name=3. {ECO:0000255}.; TRANSMEM 352 372 Helical; Name=4. {ECO:0000255}.; TRANSMEM 414 434 Helical; Name=5. {ECO:0000255}.; TRANSMEM 454 476 Helical; Name=6. {ECO:0000255}.; TRANSMEM 481 500 Helical; Name=7. {ECO:0000255}. TOPO_DOM 24 246 Extracellular. {ECO:0000305}.; TOPO_DOM 268 284 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 306 319 Extracellular. {ECO:0000305}.; TOPO_DOM 341 351 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 373 413 Extracellular. {ECO:0000305}.; TOPO_DOM 435 453 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 477 480 Extracellular. {ECO:0000305}.; TOPO_DOM 501 524 Cytoplasmic. {ECO:0000305}. FUNCTION: Adhesion G protein-coupled receptor (GPCR). Transduces intracellular signals through coupling to guanine nucleotide-binding protein G(s) subunit alpha and activation of adenylate cyclase pathway (PubMed:22575658). Isoform 1, but not isoform 2, is constitutively active, as evidenced by elevated basal cAMP levels, and responds to mechanical activation (shaking) (PubMed:26499266). {ECO:0000269|PubMed:22575658, ECO:0000269|PubMed:26499266, ECO:0000305|PubMed:25713288}. PTM: Autoproteolysis between residues Leu-222 and Thr-223 occurs in the lumen of the endoplasmic reticulum during receptor biosynthesis. The N-terminal fragment (NTF) subsequently reassociates with the C-terminal fragment (CTF) either in a homogeneric heterodimerization, or with another family member through heterogeneric heterodimerization. Autocatalytic cleavage is thought to be critical for the maturation, stability, trafficking, and function. {ECO:0000305|PubMed:25713288}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26499266}; Multi-pass membrane protein {ECO:0000305|PubMed:25713288}. TISSUE SPECIFICITY: Expressed at least in kidney, heart, brain and spleen. In the kidney, both isoform 1 and isoform 2 are expressed at similar levels. Isoform 1 is predominant in spleen, while isoform 2 is the major form in heart and brain. {ECO:0000269|PubMed:26499266}. +Q91ZV8 AGRA2_MOUSE Adhesion G protein-coupled receptor A2 (G-protein coupled receptor 124) (Tumor endothelial marker 5) 1336 143,170 Chain (1); Compositional bias (2); Disulfide bond (1); Domain (3); Erroneous initiation (3); Glycosylation (7); Modified residue (1); Motif (2); Mutagenesis (2); Repeat (4); Signal peptide (1); Site (2); Topological domain (8); Transmembrane (7) TRANSMEM 770 790 Helical; Name=1. {ECO:0000255}.; TRANSMEM 806 826 Helical; Name=2. {ECO:0000255}.; TRANSMEM 831 851 Helical; Name=3. {ECO:0000255}.; TRANSMEM 885 905 Helical; Name=4. {ECO:0000255}.; TRANSMEM 923 943 Helical; Name=5. {ECO:0000255}.; TRANSMEM 1017 1037 Helical; Name=6. {ECO:0000255}.; TRANSMEM 1045 1065 Helical; Name=7. {ECO:0000255}. TOPO_DOM 34 769 Extracellular. {ECO:0000250|UniProtKB:Q96PE1}.; TOPO_DOM 791 805 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 827 830 Extracellular. {ECO:0000255}.; TOPO_DOM 852 884 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 906 922 Extracellular. {ECO:0000255}.; TOPO_DOM 944 1016 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1038 1044 Extracellular. {ECO:0000255}.; TOPO_DOM 1066 1336 Cytoplasmic. {ECO:0000250|UniProtKB:Q96PE1}. FUNCTION: Endothelial receptor which functions together with RECK to enable brain endothelial cells to selectively respond to Wnt7 signals (WNT7A or WNT7B) (PubMed:25373781, PubMed:25558062, PubMed:28803732). Plays a key role in Wnt7-specific responses, such as endothelial cell sprouting and migration in the forebrain and neural tube, and establishment of the blood-brain barrier (PubMed:21071672, PubMed:21282641, PubMed:21421844, PubMed:25373781, PubMed:28288111). Acts as a Wnt7-specific coactivator of canonical Wnt signaling: required to deliver RECK-bound Wnt7 to frizzled by assembling a higher-order RECK-ADGRA2-Fzd-LRP5-LRP6 complex (By similarity). ADGRA2-tethering function does not rely on its G-protein coupled receptor (GPCR) structure but instead on its combined capacity to interact with RECK extracellularly and recruit the Dishevelled scaffolding protein intracellularly (By similarity). Binds to the glycosaminoglycans heparin, heparin sulfate, chondroitin sulfate and dermatan sulfate (By similarity). {ECO:0000250|UniProtKB:Q96PE1, ECO:0000269|PubMed:21071672, ECO:0000269|PubMed:21282641, ECO:0000269|PubMed:21421844, ECO:0000269|PubMed:25373781, ECO:0000269|PubMed:25558062, ECO:0000269|PubMed:28288111, ECO:0000269|PubMed:28803732}. PTM: Glycosylated. {ECO:0000250|UniProtKB:Q96PE1}.; PTM: Proteolytically cleaved into two subunits, an extracellular subunit and a seven-transmembrane subunit. Cleaved by thrombin (F2) and MMP1. Also cleaved by MMP9, with lower efficiency. Presence of the protein disulfide-isomerase P4HB at the cell surface is additionally required for shedding of the extracellular subunit, suggesting that the subunits are linked by disulfide bonds. Shedding is enhanced by the growth factor FGF2 and may promote cell survival during angiogenesis. {ECO:0000250|UniProtKB:Q96PE1}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25558062, ECO:0000269|PubMed:28803732}; Multi-pass membrane protein {ECO:0000255}. Cell projection, filopodium {ECO:0000250|UniProtKB:Q96PE1}. Note=Enriched at lateral cell borders and also at sites of cell-ECM (extracellular matrix) contact. {ECO:0000250|UniProtKB:Q96PE1}. SUBUNIT: Interacts with RECK; the interaction is direct (PubMed:28803732). Interacts (via PDZ-binding motif) with DLG1 (via PDZ domains) (PubMed:25558062). The cleaved extracellular subunit interacts with the integrin heterodimer ITGAV:ITGB3 (By similarity). {ECO:0000250|UniProtKB:Q96PE1, ECO:0000269|PubMed:25558062, ECO:0000269|PubMed:28803732}. DOMAIN: The leucine-rich repeats (LRRs) are important for potentiation of Wnt7 signaling. {ECO:0000269|PubMed:25558062}.; DOMAIN: The RGD motif is involved in integrin ITGAV:ITGB3 binding. {ECO:0000250|UniProtKB:Q96PE1}. TISSUE SPECIFICITY: Abundantly expressed in the vasculature of the developing embryo (PubMed:11559528, PubMed:21071672, PubMed:21282641). Expression in normal adult tissues is specifically vascular with endothelial expression in CNS, including brain and retina and more widespread pericyte expression in the brain and organs, including the kidney, pancreas and corpus luteum (PubMed:21071672). {ECO:0000269|PubMed:11559528, ECO:0000269|PubMed:21071672, ECO:0000269|PubMed:21282641}. +Q8BM96 AGRG7_MOUSE Adhesion G-protein coupled receptor G7 (G-protein coupled receptor 128) 785 87,684 Chain (1); Domain (1); Glycosylation (12); Sequence conflict (1); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 436 456 Helical; Name=1. {ECO:0000255}.; TRANSMEM 466 486 Helical; Name=2. {ECO:0000255}.; TRANSMEM 524 544 Helical; Name=3. {ECO:0000255}.; TRANSMEM 562 582 Helical; Name=4. {ECO:0000255}.; TRANSMEM 624 644 Helical; Name=5. {ECO:0000255}.; TRANSMEM 669 689 Helical; Name=6. {ECO:0000255}.; TRANSMEM 695 715 Helical; Name=7. {ECO:0000255}. TOPO_DOM 27 435 Extracellular. {ECO:0000305}.; TOPO_DOM 457 465 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 487 523 Extracellular. {ECO:0000305}.; TOPO_DOM 545 561 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 583 623 Extracellular. {ECO:0000305}.; TOPO_DOM 645 668 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 690 694 Extracellular. {ECO:0000305}.; TOPO_DOM 716 785 Cytoplasmic. {ECO:0000305}. FUNCTION: Orphan receptor. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Selectively expressed in the intestinal tissues. {ECO:0000269|PubMed:24574718}. +O55074 AKA7A_MOUSE A-kinase anchor protein 7 isoform alpha (AKAP-7 isoform alpha) (A-kinase anchor protein 18) (AKAP-18) (A-kinase anchor protein 9 kDa) (AKAP 9) (Protein kinase A-anchoring protein 7 isoform alpha) (PRKA7 isoform alpha) 81 9,169 Chain (1); Initiator methionine (1); Lipidation (3); Region (2); Sequence conflict (3) FUNCTION: Targets the cAMP-dependent protein kinase (PKA) to the plasma membrane, and permits functional coupling to the L-type calcium channel. The membrane-associated form reduces epithelial sodium channel (ENaC) activity, whereas the free cytoplasmic form may negatively regulate ENaC channel feedback inhibition by intracellular sodium (By similarity). {ECO:0000250, ECO:0000269|PubMed:9620705}. SUBCELLULAR LOCATION: Lateral cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000269|PubMed:9545239}. SUBUNIT: Binds cAMP-dependent protein kinase (PKA). Interacts with PRKCA; only the cytoplasmic form is capable of interacting with PRKCA (By similarity). {ECO:0000250}. +P04756 ACHA_MOUSE Acetylcholine receptor subunit alpha 457 51,939 Beta strand (13); Chain (1); Disulfide bond (2); Glycosylation (1); Helix (3); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (4); Turn (3) TRANSMEM 231 255 Helical.; TRANSMEM 263 281 Helical.; TRANSMEM 297 316 Helical.; TRANSMEM 429 447 Helical. TOPO_DOM 21 230 Extracellular.; TOPO_DOM 317 428 Cytoplasmic. FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. SUBUNIT: Pentamer of two alpha chains, and one each of the beta, delta, and gamma (in immature muscle) or epsilon (in mature muscle) chains (PubMed:17643119). The muscle heteropentamer composed of alpha-1, beta-1, delta, epsilon subunits interacts with the alpha-conotoxin ImII (By similarity). {ECO:0000250|UniProtKB:P02708, ECO:0000269|PubMed:17643119}. +P62737 ACTA_MOUSE Actin, aortic smooth muscle (Alpha-actin-2) [Cleaved into: Actin, aortic smooth muscle, intermediate form] 377 42,009 Chain (2); Initiator methionine (1); Modified residue (6) FUNCTION: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. PTM: Oxidation of Met-46 and Met-49 by MICALs (MICAL1, MICAL2 or MICAL3) to form methionine sulfoxide promotes actin filament depolymerization. MICAL1 and MICAL2 produce the (R)-S-oxide form. The (R)-S-oxide form is reverted by MSRB1 and MSRB2, which promotes actin repolymerization. {ECO:0000269|PubMed:23911929}.; PTM: Monomethylation at Lys-86 (K84me1) regulates actin-myosin interaction and actomyosin-dependent processes. Demethylation by ALKBH4 is required for maintaining actomyosin dynamics supporting normal cleavage furrow ingression during cytokinesis and cell migration (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SUBUNIT: Polymerization of globular actin (G-actin) leads to a structural filament (F-actin) in the form of a two-stranded helix. Each actin can bind to 4 others. +O88990 ACTN3_MOUSE Alpha-actinin-3 (Alpha-actinin skeletal muscle isoform 3) (F-actin cross-linking protein) 900 103,043 Calcium binding (2); Chain (1); Domain (4); Modified residue (1); Region (1); Repeat (4) FUNCTION: F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein (By similarity). {ECO:0000250}. SUBUNIT: Homodimer; antiparallel. Also forms heterodimers with ACTN2. Interacts with MYOZ1 (By similarity). {ECO:0000250}. +Q9R1V4 ADA11_MOUSE Disintegrin and metalloproteinase domain-containing protein 11 (ADAM 11) (Metalloproteinase-like, disintegrin-like, and cysteine-rich protein) (MDC) 773 84,134 Chain (1); Compositional bias (1); Disulfide bond (7); Domain (3); Glycosylation (4); Propeptide (1); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 739 759 Helical. {ECO:0000255}. TOPO_DOM 230 738 Extracellular. {ECO:0000255}.; TOPO_DOM 760 773 Cytoplasmic. {ECO:0000255}. FUNCTION: Probable ligand for integrin in the brain. This is a non catalytic metalloprotease-like protein. PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Can bind to LGI1 and LGI4. DOMAIN: A conserved motif [AVN[ED]CD] within the disintegrin-like domain could be involved in the binding to the integrin receptor. TISSUE SPECIFICITY: Highly expressed in the brain. Weakly detected in the heart, liver and testis. +Q8K410 ADA32_MOUSE Disintegrin and metalloproteinase domain-containing protein 32 (ADAM 32) 754 83,985 Alternative sequence (1); Chain (1); Compositional bias (1); Disulfide bond (7); Domain (3); Erroneous initiation (2); Glycosylation (5); Modified residue (1); Propeptide (1); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 690 710 Helical. {ECO:0000255}. TOPO_DOM 177 689 Extracellular. {ECO:0000255}.; TOPO_DOM 711 754 Cytoplasmic. {ECO:0000255}. FUNCTION: May play a role in sperm development and fertilization This is a non-catalytic metalloprotease-like protein. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Highly expressed in the testis and weakly expressed in the epididymis, brain and heart. {ECO:0000269|PubMed:12568724}. +Q9R0X2 ADEC1_MOUSE ADAM DEC1 (EC 3.4.24.-) (A disintegrin and metalloproteinase domain-like protein decysin-1) (ADAM-like protein decysin-1) 467 52,956 Active site (1); Chain (1); Disulfide bond (2); Domain (2); Glycosylation (2); Metal binding (3); Propeptide (1); Signal peptide (1) FUNCTION: May play an important role in the control of the immune response and during pregnancy. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Expressed highly in uterus during pregnancy. +Q9R157 ADA18_MOUSE Disintegrin and metalloproteinase domain-containing protein 18 (ADAM 18) (Disintegrin and metalloproteinase domain-containing protein 27) (ADAM 27) (Transmembrane metalloproteinase-like, disintegrin-like, and cysteine-rich protein III) (tMDC III) 719 79,210 Chain (1); Compositional bias (1); Disulfide bond (7); Domain (3); Glycosylation (12); Propeptide (1); Sequence conflict (6); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 684 704 Helical. {ECO:0000255}. TOPO_DOM 173 683 Extracellular. {ECO:0000255}.; TOPO_DOM 705 719 Cytoplasmic. {ECO:0000255}. FUNCTION: Sperm surface membrane protein that may be involved in spermatogenesis and fertilization. This is a non catalytic metalloprotease-like protein. PTM: The prodomain and the metalloprotease-like domain are cleaved during the epididymal maturation of the spermatozoa. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. DOMAIN: A tripeptide motif (ECD) within disintegrin-like domain could be involved in the binding to egg integrin receptor and thus could mediate sperm/egg binding. TISSUE SPECIFICITY: Expressed specifically in testis. +P51829 ADCY7_MOUSE Adenylate cyclase type 7 (EC 4.6.1.1) (ATP pyrophosphate-lyase 7) (Adenylate cyclase type VII) (Adenylyl cyclase 7) 1099 122,708 Binding site (3); Chain (1); Glycosylation (1); Metal binding (5); Nucleotide binding (4); Region (3); Sequence conflict (3); Topological domain (3); Transmembrane (12) TRANSMEM 34 54 Helical. {ECO:0000255}.; TRANSMEM 63 83 Helical. {ECO:0000255}.; TRANSMEM 95 117 Helical. {ECO:0000255}.; TRANSMEM 122 142 Helical. {ECO:0000255}.; TRANSMEM 147 167 Helical. {ECO:0000255}.; TRANSMEM 178 198 Helical. {ECO:0000255}.; TRANSMEM 596 616 Helical. {ECO:0000255}.; TRANSMEM 621 641 Helical. {ECO:0000255}.; TRANSMEM 670 689 Helical. {ECO:0000255}.; TRANSMEM 719 738 Helical. {ECO:0000255}.; TRANSMEM 747 766 Helical. {ECO:0000255}.; TRANSMEM 813 833 Helical. {ECO:0000255}. TOPO_DOM 1 33 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 199 595 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 834 1099 Cytoplasmic. {ECO:0000255}. FUNCTION: Catalyzes the formation of cAMP in response to activation of G protein-coupled receptors (Probable). Functions in signaling cascades activated namely by thrombin and sphingosine 1-phosphate and mediates regulation of cAMP synthesis through synergistic action of the stimulatory G alpha protein with GNA13 (PubMed:18541530). Also, during inflammation, mediates zymosan-induced increase intracellular cAMP, leading to protein kinase A pathway activation in order to modulate innate immune responses through heterotrimeric G proteins G(12/13) (PubMed:23178822). Functions in signaling cascades activated namely by dopamine and C5 alpha chain and mediates regulation of cAMP synthesis through synergistic action of the stimulatory G protein with G beta:gamma complex (By similarity). Functions, through cAMP response regulation, to keep inflammation under control during bacterial infection by sensing the presence of serum factors, such as the bioactive lysophospholipid (LPA) that regulate LPS-induced TNF-alpha production. However, it is also required for the optimal functions of B and T cells during adaptive immune responses by regulating cAMP synthesis in both B and T cells (PubMed:20505140). {ECO:0000250|UniProtKB:P51828, ECO:0000269|PubMed:18541530, ECO:0000269|PubMed:20505140, ECO:0000269|PubMed:23178822, ECO:0000305|PubMed:18541530, ECO:0000305|PubMed:23178822, ECO:0000305|PubMed:23229509}. PTM: Phosphorylated by PRKCD. {ECO:0000250|UniProtKB:P51828}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. DOMAIN: The protein contains two modules with six transmembrane helices each; both are required for catalytic activity. Isolated N-terminal or C-terminal guanylate cyclase domains have no catalytic activity, but when they are brought together, enzyme activity is restored. The active site is at the interface of the two domains. Both contribute substrate-binding residues, but the catalytic metal ions are bound exclusively via the N-terminal guanylate cyclase domain. {ECO:0000250|UniProtKB:P26769}. TISSUE SPECIFICITY: Most abundant in heart, spleen and lung. {ECO:0000269|PubMed:7961850}. +Q60994 ADIPO_MOUSE Adiponectin (30 kDa adipocyte complement-related protein) (Adipocyte complement-related 30 kDa protein) (ACRP30) (Adipocyte, C1q and collagen domain-containing protein) (Adipocyte-specific protein AdipoQ) 247 26,809 Beta strand (10); Chain (1); Disulfide bond (1); Domain (2); Glycosylation (6); Modified residue (9); Mutagenesis (5); Sequence conflict (7); Signal peptide (1); Site (4); Turn (1) FUNCTION: Important adipokine involved in the control of fat metabolism and insulin sensitivity, with direct anti-diabetic, anti-atherogenic and anti-inflammatory activities. Stimulates AMPK phosphorylation and activation in the liver and the skeletal muscle, enhancing glucose utilization and fatty-acid combustion. Antagonizes TNF-alpha by negatively regulating its expression in various tissues such as liver and macrophages, and also by counteracting its effects. Inhibits endothelial NF-kappa-B signaling through a cAMP-dependent pathway. May play a role in cell growth, angiogenesis and tissue remodeling by binding and sequestering various growth factors with distinct binding affinities, depending on the type of complex, LMW, MMW or HMW. {ECO:0000269|PubMed:11479627, ECO:0000269|PubMed:11479628, ECO:0000269|PubMed:12840063, ECO:0000269|PubMed:15734737, ECO:0000269|PubMed:15760892}. PTM: HMW complexes are more extensively glycosylated than smaller oligomers. Hydroxylation and glycosylation of the lysine residues within the collagen-like domain of adiponectin seem to be critically involved in regulating the formation and/or secretion of HMW complexes and consequently contribute to the insulin-sensitizing activity of adiponectin in hepatocytes. {ECO:0000269|PubMed:11912203, ECO:0000269|PubMed:23209641}.; PTM: O-glycosylated. Not N-glycosylated (By similarity) O-linked glycans on hydroxylysine residues consist of Glc-Gal disaccharides bound to the oxygen atom of post-translationally added hydroxyl groups (By similarity). O-linked glycosylation in the N-terminal is disialylated with the structure Neu5Acalpha2->8Neu5Acalpha2->3Gal. Sialylated by alpha 2,8-sialyltransferase III. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23209641}. SUBUNIT: Homomultimer (PubMed:23209641). Forms trimers, hexamers and 12- to 18-mers. The trimers (low molecular weight complexes / LMW) are assembled via non-covalent interactions of the collagen-like domains in a triple helix and hydrophobic interactions within the globular C1q domain. Several trimers can associate to form disulfide-linked hexamers (middle molecular weight complexes / MMW) and larger complexes (higher molecular weight / HMW) (PubMed:23209641). The HMW-complex assembly is also modulated by the degree of lysine hydroxylation and glycosylation (PubMed:23209641). LMW, MMW and HMW complexes bind to HBEGF, MMW and HMW complexes bind to PDGFB, and HMW complex binds to FGF2. Interacts with CTRP9 via the C1q domain (heterotrimeric complex) (PubMed:18787108). {ECO:0000269|PubMed:15734737, ECO:0000269|PubMed:15760892, ECO:0000269|PubMed:16621799, ECO:0000269|PubMed:18787108, ECO:0000269|PubMed:19855092, ECO:0000269|PubMed:23209641}. TISSUE SPECIFICITY: Synthesized exclusively by adipocytes and secreted into plasma. +Q3V132 ADT4_MOUSE ADP/ATP translocase 4 (ADP,ATP carrier protein 4) (Adenine nucleotide translocator 4) (ANT 4) (Solute carrier family 25 member 31) (Sperm flagellar energy carrier protein) 320 35,258 Binding site (3); Chain (1); Motif (1); Region (1); Repeat (3); Sequence conflict (2); Transmembrane (6) TRANSMEM 21 50 Helical; Name=1. {ECO:0000250|UniProtKB:P02722}.; TRANSMEM 88 112 Helical; Name=2. {ECO:0000250|UniProtKB:P02722}.; TRANSMEM 123 143 Helical; Name=3. {ECO:0000250|UniProtKB:P02722}.; TRANSMEM 192 212 Helical; Name=4. {ECO:0000250|UniProtKB:P02722}.; TRANSMEM 224 244 Helical; Name=5. {ECO:0000250|UniProtKB:P02722}.; TRANSMEM 285 302 Helical; Name=6. {ECO:0000250|UniProtKB:P02722}. FUNCTION: Catalyzes the exchange of cytoplasmic ADP with mitochondrial ATP across the mitochondrial inner membrane. May serve to mediate energy generating and energy consuming processes in the distal flagellum, possibly as a nucleotide shuttle between flagellar glycolysis, protein phosphorylation and mechanisms of motility. {ECO:0000269|PubMed:17137571}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell projection, cilium, flagellum {ECO:0000250}. Note=In sperm flagellum this protein is located in the fibrous sheath, a non-mitochondrial region. {ECO:0000250}. DOMAIN: The transmembrane helices are not perpendicular to the plane of the membrane, but cross the membrane at an angle. Odd-numbered transmembrane helices exhibit a sharp kink, due to the presence of a conserved proline residue. {ECO:0000250|UniProtKB:P02722}. +Q9DCJ7 AKIP_MOUSE Aurora kinase A-interacting protein (AURKA-interacting protein) (28S ribosomal protein S38, mitochondrial) (MRP-S38) 200 23,300 Chain (1); Sequence conflict (1) FUNCTION: May act as a negative regulator of Aurora-A kinase, by down-regulation through proteasome-dependent degradation. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Nucleus. SUBUNIT: Component of the mitochondrial ribosome small subunit (28S) which comprises a 12S rRNA and about 30 distinct proteins (By similarity). Interacts with Aurora-A. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed and especially highly expressed in heart, skeletal muscle and testis. +P30355 AL5AP_MOUSE Arachidonate 5-lipoxygenase-activating protein (FLAP) (MK-886-binding protein) 161 18,136 Chain (1); Intramembrane (1); Region (2); Sequence conflict (1); Topological domain (5); Transmembrane (4) INTRAMEM 108 115 {ECO:0000250}. TRANSMEM 9 30 Helical. {ECO:0000250}.; TRANSMEM 53 77 Helical. {ECO:0000250}.; TRANSMEM 81 102 Helical. {ECO:0000250}.; TRANSMEM 116 128 Helical. {ECO:0000250}. TOPO_DOM 1 8 Lumenal. {ECO:0000250}.; TOPO_DOM 31 52 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 78 80 Lumenal. {ECO:0000250}.; TOPO_DOM 103 107 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 129 161 Lumenal. {ECO:0000250}. FUNCTION: Required for leukotriene biosynthesis by ALOX5 (5-lipoxygenase). Anchors ALOX5 to the membrane. Binds arachidonic acid, and could play an essential role in the transfer of arachidonic acid to ALOX5. Binds to MK-886, a compound that blocks the biosynthesis of leukotrienes (By similarity). {ECO:0000250, ECO:0000269|PubMed:19075240}. SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:19075240}; Multi-pass membrane protein {ECO:0000269|PubMed:19075240}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Homotrimer. Interacts with LTC4S and ALOX5. {ECO:0000269|PubMed:19075240}. DOMAIN: The C-terminal part after residue 140 is mostly disordered. {ECO:0000250}. +Q99MR0 ACL6B_MOUSE Actin-like protein 6B (53 kDa BRG1-associated factor B) (Actin-related protein Baf53b) (ArpN-alpha) (ArpNa) (BRG1-associated factor 53B) (BAF53B) 426 46,891 Chain (1); Region (1) FUNCTION: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. Belongs to the neuron-specific chromatin remodeling complex (nBAF complex), as such plays a role in remodeling mononucleosomes in an ATP-dependent fashion, and is required for postmitotic neural development and dendritic outgrowth. During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth. ACTL6B/BAF53B is not essential for assembly of the nBAF complex but is required for targeting the complex and CREST to the promoter of genes essential for dendritic growth. {ECO:0000269|PubMed:12368262, ECO:0000269|PubMed:17640523, ECO:0000269|PubMed:17920018}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12437990}. SUBUNIT: Component of the multiprotein chromatin-remodeling complexes SWI/SNF: SWI/SNF-A (BAF), SWI/SNF-B (PBAF) and related complexes. The canonical complex contains a catalytic subunit (either SMARCA4/BRG1/BAF190A or SMARCA2/BRM/BAF190B) and at least SMARCE1, ACTL6A/BAF53, SMARCC1/BAF155, SMARCC2/BAF170, and SMARCB1/SNF5/BAF47. Other subunits specific to each of the complexes may also be present permitting several possible combinations developmentally and tissue specific (PubMed:22952240, PubMed:26601204).Component of the BAF complex, which includes at least actin (ACTB), ARID1A/BAF250A, ARID1B/BAF250B, SMARCA2/BRM, SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57, SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C (By similarity). Component of neuron-specific chromatin remodeling complex (nBAF complex) composed of at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A or SMARCD2/BAF60B or SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, DPF1/BAF45B, DPF3/BAF45C, ACTL6B/BAF53B and actin (ACTB)(PubMed:12368262, PubMed:17640523, PubMed:17920018). Note that the nBAF complex is polymorphic in regard to the ATPase, SMARCA2 and SMARCA4 occupying mutually exclusive positions (PubMed:12368262). May be a component of the SWI/SNF-B (PBAF) chromatin remodeling complex, at least composed of SMARCA4/BRG1, SMARCB1/BAF47/SNF5, ACTL6A/BAF53A or ACTL6B/BAF53B, SMARCE1/BAF57, SMARCD1/BAF60A, SMARCD2/BAF60B, perhaps SMARCD3/BAF60C, SMARCC1/BAF155, SMARCC2/BAF170, PBRM1/BAF180, ARID2/BAF200 and actin (By similarity). {ECO:0000250|UniProtKB:O94805, ECO:0000269|PubMed:12368262, ECO:0000269|PubMed:17640523, ECO:0000269|PubMed:17920018, ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}. TISSUE SPECIFICITY: Restricted to the brain and peripheral nervous tissue (at protein level). Present in virtually all neurons in the cerebral neocortex (layers II-VI), hippocampus (CA1-CA3 region and dentate gyrus), cerebellum (molecular, granular and Purkinje cell layers), spinal cord (dorsally and ventrally), dorsal root ganglion, retina and the olfactory bulb (mitral and granule cell layers). Expressed specifically in postmitotic neurons (at protein level). {ECO:0000269|PubMed:12368262, ECO:0000269|PubMed:12437990, ECO:0000269|PubMed:17640523}. +Q64326 ACTHR_MOUSE Adrenocorticotropic hormone receptor (ACTH receptor) (ACTH-R) (Adrenocorticotropin receptor) (Melanocortin receptor 2) (MC2-R) 296 33,982 Chain (1); Glycosylation (2); Lipidation (1); Topological domain (8); Transmembrane (7) TRANSMEM 24 49 Helical; Name=1. {ECO:0000250}.; TRANSMEM 59 79 Helical; Name=2. {ECO:0000250}.; TRANSMEM 105 126 Helical; Name=3. {ECO:0000250}.; TRANSMEM 148 168 Helical; Name=4. {ECO:0000250}.; TRANSMEM 181 199 Helical; Name=5. {ECO:0000250}.; TRANSMEM 218 244 Helical; Name=6. {ECO:0000250}.; TRANSMEM 257 278 Helical; Name=7. {ECO:0000250}. TOPO_DOM 1 23 Extracellular. {ECO:0000250}.; TOPO_DOM 50 58 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 80 104 Extracellular. {ECO:0000250}.; TOPO_DOM 127 147 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 169 180 Extracellular. {ECO:0000250}.; TOPO_DOM 200 217 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 245 256 Extracellular. {ECO:0000250}.; TOPO_DOM 279 296 Cytoplasmic. {ECO:0000250}. FUNCTION: Receptor for corticotropin (ACTH). This receptor is mediated by G proteins (G(s)) which activate adenylate cyclase (cAMP). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBUNIT: Interacts with MRAP; increasing ligand-sensitivity and generation of cAMP. Interacts with MRAP2; competing with MRAP for binding to MC2R and impairing the binding of corticotropin (ACTH) (By similarity). {ECO:0000250}. +Q811Q4 ADA29_MOUSE Disintegrin and metalloproteinase domain-containing protein 29 (ADAM 29) 763 86,445 Chain (1); Disulfide bond (7); Domain (3); Glycosylation (8); Propeptide (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 685 705 Helical. {ECO:0000255}. TOPO_DOM 201 684 Extracellular. {ECO:0000255}.; TOPO_DOM 706 763 Cytoplasmic. {ECO:0000255}. FUNCTION: May be involved in spermatogenesis and fertilization. Seems to be a non catalytic metalloprotease-like protein (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. +Q9D5P4 ADAD2_MOUSE Adenosine deaminase domain-containing protein 2 478 51,069 Chain (1); Domain (2) +O35598 ADA10_MOUSE Disintegrin and metalloproteinase domain-containing protein 10 (ADAM 10) (EC 3.4.24.81) (Kuzbanian protein homolog) (Mammalian disintegrin-metalloprotease) (CD antigen CD156c) 749 83,968 Active site (1); Chain (1); Compositional bias (1); Disulfide bond (17); Domain (2); Glycosylation (4); Metal binding (4); Modified residue (1); Motif (3); Propeptide (1); Sequence conflict (1); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 674 694 Helical. {ECO:0000255}. TOPO_DOM 20 673 Extracellular. {ECO:0000255}.; TOPO_DOM 695 749 Cytoplasmic. {ECO:0000255}. FUNCTION: Cleaves the membrane-bound precursor of TNF-alpha to its mature soluble form. Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface (By similarity). Responsible for the proteolytic release of several other cell-surface proteins, including heparin-binding epidermal growth-like factor, ephrin-A2, CD44, CDH2 and for constitutive and regulated alpha-secretase cleavage of amyloid precursor protein (APP) at '687-Lys-|-Leu-688' (By similarity). Contributes to the normal cleavage of the cellular prion protein (By similarity). Involved in the cleavage of the adhesion molecule L1 at the cell surface and in released membrane vesicles, suggesting a vesicle-based protease activity (By similarity). Controls also the proteolytic processing of Notch and mediates lateral inhibition during neurogenesis (PubMed:9244301). Responsible for the FasL ectodomain shedding and for the generation of the remnant ADAM10-processed FasL (FasL APL) transmembrane form (By similarity). Also cleaves the ectodomain of the integral membrane proteins CORIN and ITM2B (By similarity). May regulate the EFNA5-EPHA3 signaling (By similarity). {ECO:0000250|UniProtKB:O14672, ECO:0000269|PubMed:9244301}. PTM: The precursor is cleaved by furin and PCSK7. {ECO:0000250|UniProtKB:Q10741}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26668317}; Single-pass type I membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:O14672}; Single-pass type I membrane protein {ECO:0000305}. Note=Is localized in the plasma membrane but is predominantly expressed in the Golgi apparatus and in released membrane vesicles derived likely from the Golgi. {ECO:0000250|UniProtKB:O14672}. SUBUNIT: Forms a ternary EFNA5-EPHA3-ADAM10 complex mediating EFNA5 extracellular domain shedding by ADAM10 which regulates the EFNA5-EPHA3 complex internalization and function, the cleavage occurs in trans, with ADAM10 and its substrate being on the membranes of opposing cells (By similarity). Interacts with EPHA2 (PubMed:10958785). Interacts with NGF in a divalent cation-dependent manner (By similarity). Interacts with TSPAN14; the interaction promotes ADAM10 maturation and cell surface expression (PubMed:26668317, PubMed:23035126). Interacts with TSPAN5, TSPAN10, TSPAN15, TSPAN17 and TSPAN33; these interactions regulate ADAM10 substrate specificity (PubMed:26668317, PubMed:23035126). {ECO:0000250|UniProtKB:O14672, ECO:0000269|PubMed:10958785, ECO:0000269|PubMed:23035126, ECO:0000269|PubMed:26668317}. DOMAIN: The Cys-rich region C-terminal to the disintegrin domain functions as a substrate-recognition module, it recognizes the EFNA5-EPHA3 Complex but not the individual proteins (By similarity). Both Cys-rich and stalk region are necessary for interaction with TSPAN5, TSPAN10, TSPAN14, TSPAN17, TSPAN33 (PubMed:26668317). Stalk region is sufficient for interaction with TSPAN15 (PubMed:26668317). {ECO:0000250|UniProtKB:Q10741, ECO:0000269|PubMed:26668317}.; DOMAIN: The propeptide keeps the metalloprotease in a latent form via a cysteine switch mechanism. This mechanism may be mediated by a highly conserved cysteine (Cys-173) in the propeptide, which interacts and neutralizes the zinc-coordinating HEXGHXXGXXHD catalytic core of the metalloprotease domain. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme. {ECO:0000250|UniProtKB:P03956}. +P37172 ACVR1_MOUSE Activin receptor type-1 (EC 2.7.11.30) (Activin receptor type I) (ACTR-I) (Serine/threonine-protein kinase receptor R1) (SKR1) (TGF-B superfamily receptor type I) (TSR-I) (TSK-7L) 509 57,226 Active site (1); Binding site (1); Chain (1); Domain (2); Glycosylation (1); Modified residue (1); Nucleotide binding (1); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 124 146 Helical. {ECO:0000255}. TOPO_DOM 21 123 Extracellular. {ECO:0000255}.; TOPO_DOM 147 509 Cytoplasmic. {ECO:0000255}. FUNCTION: On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for activin. May be involved in left-right pattern formation during embryogenesis. {ECO:0000269|PubMed:15531373}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Interacts with FKBP1A. Interacts with FCHO1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in normal parenchymal cells, endothelial cells, fibroblasts and tumor-derived epithelial cells. +O88444 ADCY1_MOUSE Adenylate cyclase type 1 (EC 4.6.1.1) (ATP pyrophosphate-lyase 1) (Adenylate cyclase type I) (Adenylyl cyclase 1) (Ca(2+)/calmodulin-activated adenylyl cyclase) 1118 123,373 Binding site (3); Chain (1); Glycosylation (1); Metal binding (5); Modified residue (1); Nucleotide binding (4); Region (2); Sequence conflict (21); Topological domain (3); Transmembrane (12) TRANSMEM 63 83 Helical. {ECO:0000255}.; TRANSMEM 87 107 Helical. {ECO:0000255}.; TRANSMEM 124 144 Helical. {ECO:0000255}.; TRANSMEM 157 177 Helical. {ECO:0000255}.; TRANSMEM 182 202 Helical. {ECO:0000255}.; TRANSMEM 213 233 Helical. {ECO:0000255}.; TRANSMEM 610 630 Helical. {ECO:0000255}.; TRANSMEM 634 654 Helical. {ECO:0000255}.; TRANSMEM 673 693 Helical. {ECO:0000255}.; TRANSMEM 724 744 Helical. {ECO:0000255}.; TRANSMEM 752 772 Helical. {ECO:0000255}.; TRANSMEM 774 793 Helical. {ECO:0000255}. TOPO_DOM 1 62 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 234 609 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 794 1118 Cytoplasmic. {ECO:0000255}. FUNCTION: Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling. Mediates responses to increased cellular Ca(2+)/calmodulin levels (PubMed:9662407, PubMed:7816821). May be involved in regulatory processes in the central nervous system (PubMed:9662407). May play a role in memory and learning (PubMed:7816821). Plays a role in the regulation of the circadian rhythm of daytime contrast sensitivity probably by modulating the rhythmic synthesis of cyclic AMP in the retina (PubMed:24048828). {ECO:0000269|PubMed:24048828, ECO:0000269|PubMed:7816821, ECO:0000269|PubMed:9662407}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:P19754}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:9662407}; Multi-pass membrane protein {ECO:0000305}. Cell membrane {ECO:0000250|UniProtKB:P19754}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P19754}. Cytoplasm {ECO:0000269|PubMed:24482543}. Membrane raft {ECO:0000250|UniProtKB:P19754}. Note=Expressed in the cytoplasm of supporting cells and hair cells of the cochlea vestibule, as well as to the cochlear hair cell nuclei and stereocilia|. {ECO:0000269|PubMed:24482543}. SUBUNIT: Interacts with CALM. {ECO:0000250|UniProtKB:P19754}. DOMAIN: The protein contains two modules with six transmembrane helices each; both are required for catalytic activity. Isolated N-terminal or C-terminal modules have no catalytic activity, but when they are brought together, enzyme activity is restored. The active site is at the interface of the two modules. {ECO:0000250|UniProtKB:P30803}. TISSUE SPECIFICITY: Expressed throughout inner ear development. {ECO:0000269|PubMed:24482543}. +P30545 ADA2B_MOUSE Alpha-2B adrenergic receptor (Alpha-2B adrenoreceptor) (Alpha-2B adrenoceptor) (Alpha-2BAR) 450 50,172 Chain (1); Compositional bias (1); Disulfide bond (1); Erroneous initiation (1); Lipidation (1); Sequence conflict (2); Site (3); Topological domain (8); Transmembrane (7) TRANSMEM 13 37 Helical; Name=1. {ECO:0000250}.; TRANSMEM 50 75 Helical; Name=2. {ECO:0000250}.; TRANSMEM 86 108 Helical; Name=3. {ECO:0000250}.; TRANSMEM 131 153 Helical; Name=4. {ECO:0000250}.; TRANSMEM 170 193 Helical; Name=5. {ECO:0000250}.; TRANSMEM 373 396 Helical; Name=6. {ECO:0000250}.; TRANSMEM 406 429 Helical; Name=7. {ECO:0000250}. TOPO_DOM 1 12 Extracellular. {ECO:0000250}.; TOPO_DOM 38 49 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 76 85 Extracellular. {ECO:0000250}.; TOPO_DOM 109 130 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 154 169 Extracellular. {ECO:0000250}.; TOPO_DOM 194 372 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 397 405 Extracellular. {ECO:0000250}.; TOPO_DOM 430 450 Cytoplasmic. {ECO:0000250}. FUNCTION: Alpha-2 adrenergic receptors mediate the catecholamine-induced inhibition of adenylate cyclase through the action of G proteins. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P18089}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P18089}. Note=Interaction with RAB26, GGA1, GGA2 and GGA3 mediates transport from the Golgi to the cell membrane. {ECO:0000250|UniProtKB:P18089}. SUBUNIT: Interacts with RAB26. Interacts with PPP1R9B. Interacts with GGA1, GGA2 and GGA3. {ECO:0000250|UniProtKB:P18089}. +Q8BM81 ADCL4_MOUSE Arylacetamide deacetylase-like 4 (EC 3.1.1.-) 407 46,220 Active site (3); Chain (1); Erroneous termination (1); Glycosylation (1); Motif (1); Topological domain (2); Transmembrane (1) TRANSMEM 5 25 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 4 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 26 407 Lumenal. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q8R2Z0 ADIPL_MOUSE Adipolin (Adipose-derived insulin-sensitizing factor) (Complement C1q tumor necrosis factor-related protein 12) [Cleaved into: Adipolin fC1QTNF12 (Adipolin fCTRP12) (Adipolin full-length form); Adipolin gC1QTNF12 (Adipolin cleaved form) (Adipolin gCTRP12)] 308 33,267 Chain (2); Compositional bias (1); Domain (1); Glycosylation (1); Mutagenesis (5); Sequence conflict (1); Signal peptide (1); Site (3) FUNCTION: Insulin-sensitizing adipocyte-secreted protein (adipokine) that regulates glucose metabolism in liver and adipose tissue. Promotes glucose uptake in adipocytes and suppresses de novo glucose production in hepatocytes via the PI3K-Akt signaling pathway. Administration lead to reduction of blood glucose. Able to attenuate inflammation in fat tissue (PubMed:21849507, PubMed:22275362). {ECO:0000269|PubMed:21849507, ECO:0000269|PubMed:22275362}.; FUNCTION: Adipolin fC1QTNF12: Acts by activating the Akt signaling in hepatocytes and adipocytes. Not able to increase insulin-stimulated glucose uptake in adipocytes (PubMed:22942287). {ECO:0000269|PubMed:22942287}.; FUNCTION: Adipolin gC1QTNF12: Acts by activating the MAP kinase. Increases insulin-stimulated glucose uptake in adipocytes (PubMed:22942287). {ECO:0000269|PubMed:22942287}. PTM: Processed into Adipolin fC1QTNF12 and Adipolin gC1QTNF12 by FURIN (PubMed:22942287). Insulin enhances endogenous C1QTNF12 cleavage (PubMed:22942287). {ECO:0000269|PubMed:22942287}. SUBCELLULAR LOCATION: Adipolin fC1QTNF12: Secreted {ECO:0000269|PubMed:22275362, ECO:0000269|PubMed:22942287}.; SUBCELLULAR LOCATION: Adipolin gC1QTNF12: Secreted {ECO:0000269|PubMed:22275362, ECO:0000269|PubMed:22942287}. Note=In serum is the predominant form. {ECO:0000269|PubMed:22275362}. SUBUNIT: Homomultimer; disulfide-linked (PubMed:22942287). Adipolin fC1QTNF12: homotrimer; disulfide-linked (PubMed:22942287). Adipolin gC1QTNF12: homodimer; disulfide-linked (PubMed:22942287). May interact with ERFE. {ECO:0000269|PubMed:22942287}. TISSUE SPECIFICITY: Widely expressed, with high expression in subcutaneous and epididymal white adipose tissues and brown adipose tissue. Expressed in adipocytes (at protein level). {ECO:0000269|PubMed:21849507, ECO:0000269|PubMed:22275362}. +Q8BZI0 AF1L1_MOUSE Actin filament-associated protein 1-like 1 (AFAP1-like protein 1) 768 86,638 Alternative sequence (2); Chain (1); Coiled coil (1); Compositional bias (1); Domain (2); Modified residue (9) FUNCTION: May be involved in podosome and invadosome formation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8TED9}. Cell projection, podosome {ECO:0000250|UniProtKB:Q8TED9}. Cell projection, invadopodium {ECO:0000250|UniProtKB:Q8TED9}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:Q8TED9}. SUBUNIT: Interacts with CTTN. {ECO:0000250}. +Q8VC66 ADIP_MOUSE Afadin- and alpha-actinin-binding protein (ADIP) (Afadin DIL domain-interacting protein) 615 70,956 Chain (1); Coiled coil (3); Modified residue (7); Sequence conflict (4) FUNCTION: Belongs to an adhesion system, which plays a role in the organization of homotypic, interneuronal and heterotypic cell-cell adherens junctions (AJs). May connect the nectin-afadin and E-cadherin-catenin system through alpha-actinin and may be involved in organization of the actin cytoskeleton at AJs through afadin and alpha-actinin (PubMed:12446711). Acts as a centrosome maturation factor, probably by maintaining the integrity of the pericentriolar material and proper microtubule nucleation at mitotic spindle poles. The function seems to implicate at least in part WRAP73; the SSX2IP:WRAP73 complex is proposed to act as regulator of spindle anchoring at the mitotic centrosome (By similarity). Involved in cell movement: localizes at the leading edge of moving cells in response to PDGF and is required for the formation of the leading edge and the promotion of cell movement, possibly via activation of Rac signaling (PubMed:22027834). Involved in ciliogenesis (By similarity). It is required for targeted recruitment of the BBSome, CEP290, RAB8, and SSTR3 to the cilia (By similarity). {ECO:0000250|UniProtKB:Q9Y2D8, ECO:0000269|PubMed:12446711, ECO:0000269|PubMed:22027834}. SUBCELLULAR LOCATION: Cell junction, adherens junction {ECO:0000269|PubMed:12446711}. Nucleus {ECO:0000250|UniProtKB:Q9Y2D8}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000269|PubMed:24356449}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:24356449}. Note=Not found at cell-matrix AJs. SUBUNIT: Interacts with SSX2 and SSX3 (By similarity). Does not interact with SSX1 and SSX4 (By similarity). Interacts with afadin and alpha-actinin (PubMed:12446711). Interacts with VAV2 (PubMed:22027834). Interacts with PCM1 (PubMed:24356449). Interacts with WRAP73 (By similarity). {ECO:0000250|UniProtKB:Q9Y2D8, ECO:0000269|PubMed:12446711, ECO:0000269|PubMed:22027834, ECO:0000269|PubMed:24356449}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12446711}. +O55112 AFF2_MOUSE AF4/FMR2 family member 2 (FMR2P) (Fragile X mental retardation protein 2 homolog) (Protein FMR-2) (Protein Ox19) 1272 140,181 Chain (1); Modified residue (2); Sequence conflict (3) FUNCTION: RNA-binding protein. Might be involved in alternative splicing regulation through an interaction with G-quartet RNA structure. {ECO:0000269|PubMed:19136466}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:19136466}. Note=When splicing or transcription are inhibited, accumulates in large, rounded speckles and in the nucleolus. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in the hippocampus, the piriform cortex, Purkinje cells and the cingulate gyrus. +Q9ESC8 AFF4_MOUSE AF4/FMR2 family member 4 1160 126,639 Chain (1); Compositional bias (3); Cross-link (1); Frameshift (2); Modified residue (24); Sequence conflict (3) FUNCTION: Key component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. In the SEC complex, AFF4 acts as a central scaffold that recruits other factors through direct interactions with ELL proteins (ELL, ELL2 or ELL3) and the P-TEFb complex. In case of infection by HIV-1 virus, the SEC complex is recruited by the viral Tat protein to stimulate viral gene expression (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22195968}. Note=Associates to transcriptionally active chromatin but not at snRNA genes. SUBUNIT: Component of the super elongation complex (SEC), at least composed of EAF1, EAF2, CDK9, MLLT3/AF9, AFF (AFF1 or AFF4), the P-TEFb complex and ELL (ELL, ELL2 or ELL3). Interacts with ELL2; the interaction is direct and leads to stabilize ELL2 and prevent ELL2 ubiquitination and degradation (By similarity). Interacts with ELL3; the interaction is direct. {ECO:0000250, ECO:0000269|PubMed:23273992}. TISSUE SPECIFICITY: Highly expressed in testis by Sertoli cells, and at low levels in other tissues. {ECO:0000269|PubMed:16024815}. +Q80YS6 AFAP1_MOUSE Actin filament-associated protein 1 (110 kDa actin filament-associated protein) (AFAP-110) 731 80,615 Chain (1); Coiled coil (1); Compositional bias (1); Domain (2); Erroneous initiation (1); Modified residue (10); Motif (3); Region (1); Sequence conflict (4) FUNCTION: Can cross-link actin filaments into both network and bundle structures. May modulate changes in actin filament integrity and induce lamellipodia formation. May function as an adapter molecule that links other proteins, such as SRC and PKC to the actin cytoskeleton (By similarity). {ECO:0000250}. PTM: Phosphorylated on tyrosine residues by SRC. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:Q8N556}. SUBUNIT: Monomer and homomultimer. Interacts via its C-terminus with F-actin; probably involving AFAP1 multimers. Interacts with activated SRC SH3-SH2 domains. Interacts via its PH 1 domain with PRKCA, PRKCB and PRKCI (By similarity). {ECO:0000250}. +Q61549 AGRE1_MOUSE Adhesion G protein-coupled receptor E1 (Cell surface glycoprotein F4/80) (EGF-like module receptor 1) (EGF-like module-containing mucin-like hormone receptor-like 1) (EMR1 hormone receptor) 931 102,130 Chain (1); Disulfide bond (21); Domain (8); Glycosylation (10); Motif (1); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 645 672 Helical; Name=1. {ECO:0000255}.; TRANSMEM 680 701 Helical; Name=2. {ECO:0000255}.; TRANSMEM 712 735 Helical; Name=3. {ECO:0000255}.; TRANSMEM 755 776 Helical; Name=4. {ECO:0000255}.; TRANSMEM 793 821 Helical; Name=5. {ECO:0000255}.; TRANSMEM 840 859 Helical; Name=6. {ECO:0000255}.; TRANSMEM 875 897 Helical; Name=7. {ECO:0000255}. TOPO_DOM 28 644 Extracellular. {ECO:0000305}.; TOPO_DOM 673 679 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 702 711 Extracellular. {ECO:0000305}.; TOPO_DOM 736 754 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 777 792 Extracellular. {ECO:0000305}.; TOPO_DOM 822 839 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 860 874 Extracellular. {ECO:0000305}.; TOPO_DOM 898 931 Cytoplasmic. {ECO:0000305}. FUNCTION: Orphan receptor involved in cell adhesion and probably in cell-cell interactions specifically involving cells of the immune system. May play a role in regulatory T-cells (Treg) development. {ECO:0000269|PubMed:15883173}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q14246}; Multi-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: In macrophages; but absent from those which are localized within T-cell areas of lymph nodes and spleen. Low level of expression on blood monocytes. +A2AJA7 AEGP_MOUSE Apical endosomal glycoprotein (MAM domain-containing protein 4) 1228 134,830 Alternative sequence (1); Chain (1); Disulfide bond (6); Domain (9); Erroneous gene model prediction (1); Glycosylation (5); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1160 1180 Helical. {ECO:0000255}. TOPO_DOM 23 1159 Extracellular. {ECO:0000255}.; TOPO_DOM 1181 1228 Cytoplasmic. {ECO:0000255}. FUNCTION: Probably involved in the sorting and selective transport of receptors and ligands across polarized epithelia. {ECO:0000250|UniProtKB:Q63191}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. +Q80WC7 AGFG2_MOUSE Arf-GAP domain and FG repeat-containing protein 2 (HIV-1 Rev-binding protein-like protein) (Rev/Rex activation domain-binding protein related) (RAB-R) 479 48,968 Alternative sequence (2); Chain (1); Domain (1); Modified residue (1); Zinc finger (1) SUBUNIT: Interacts with EPS15R. {ECO:0000269|PubMed:9446614}. DOMAIN: Contains FG repeats and 4 N-P-F repeats. +Q7TN31 AGGF1_MOUSE Angiogenic factor with G patch and FHA domains 1 (Angiogenic factor VG5Q) (mVG5Q) 711 79,445 Chain (1); Coiled coil (1); Compositional bias (1); Domain (2); Erroneous initiation (1); Frameshift (2); Initiator methionine (1); Modified residue (5); Sequence conflict (5) FUNCTION: Promotes angiogenesis and the proliferation of endothelial cells. Able to bind to endothelial cells and promote cell proliferation, suggesting that it may act in an autocrine fashion (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Secreted {ECO:0000250}. Note=Cytoplasmic in microvascular endothelial cells. Upon angiogenesis, when endothelial cell tube formation is initiated, it is secreted (By similarity). {ECO:0000250}. SUBUNIT: Interacts with the secreted angiogenic factor TNFSF12. {ECO:0000250}. +Q8VHN7 AGRV1_MOUSE Adhesion G-protein coupled receptor V1 (ADGRV1) (EC 3.4.-.-) (G-protein coupled receptor 98) (Monogenic audiogenic seizure susceptibility protein 1) (MASS1) (Neurepin) (Very large G-protein coupled receptor 1) (VLGR1) [Cleaved into: ADGRV1 subunit alpha; ADGRV1 subunit beta (VLGR1 subunit beta) (Vbeta)] 6298 687,458 Alternative sequence (10); Chain (3); Domain (36); Mutagenesis (3); Repeat (6); Sequence conflict (23); Signal peptide (1); Site (1); Topological domain (8); Transmembrane (7) TRANSMEM 5902 5922 Helical; Name=1. {ECO:0000255}.; TRANSMEM 5933 5953 Helical; Name=2. {ECO:0000255}.; TRANSMEM 5974 5994 Helical; Name=3. {ECO:0000255}.; TRANSMEM 6004 6024 Helical; Name=4. {ECO:0000255}.; TRANSMEM 6053 6073 Helical; Name=5. {ECO:0000255}.; TRANSMEM 6098 6118 Helical; Name=6. {ECO:0000255}.; TRANSMEM 6127 6147 Helical; Name=7. {ECO:0000255}. TOPO_DOM 29 5901 Extracellular. {ECO:0000255}.; TOPO_DOM 5923 5932 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 5954 5973 Extracellular. {ECO:0000255}.; TOPO_DOM 5995 6003 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 6025 6052 Extracellular. {ECO:0000255}.; TOPO_DOM 6074 6097 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 6119 6126 Extracellular. {ECO:0000255}.; TOPO_DOM 6148 6298 Cytoplasmic. {ECO:0000255}. FUNCTION: G-protein coupled receptor which has an essential role in the development of hearing and vision (PubMed:16775142, PubMed:17567809, PubMed:20502675, PubMed:24191038). Couples to G-alpha(i)-proteins, GNAI1/2/3, G-alpha(q)-proteins, GNAQ, as well as G-alpha(s)-proteins, GNAS, inhibiting adenylate cyclase (AC) activity and cAMP production (PubMed:24191038, PubMed:24962568). Required for the hair bundle ankle formation, which connects growing stereocilia in developing cochlear hair cells of the inner ear (PubMed:16775142, PubMed:17567809). In response to extracellular calcium, activates kinases PKA and PKC to regulate myelination by inhibiting the ubiquitination of MAG, thus enhancing the stability of this protein in myelin-forming cells of the auditory pathway (PubMed:24191038). In retina photoreceptors, the USH2 complex is required for the maintenance of periciliary membrane complex that seems to play a role in regulating intracellular protein transport (PubMed:20502675). Involved in the regulation of bone metabolism (PubMed:22419726). {ECO:0000269|PubMed:16775142, ECO:0000269|PubMed:17567809, ECO:0000269|PubMed:20502675, ECO:0000269|PubMed:22419726, ECO:0000269|PubMed:24191038, ECO:0000269|PubMed:24962568}.; FUNCTION: Cleaved ADGRV1 beta-subunit couples with G-alpha(i)-proteins, GNAI1/2/3, and constitutively inhibits adenylate cyclase (AC) activity with a stronger effect than full ADGRV1. {ECO:0000269|PubMed:24962568}. PTM: Autoproteolytically cleaved into 2 subunits, an extracellular alpha subunit and a seven-transmembrane subunit. {ECO:0000269|PubMed:24962568}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15606908}; Multi-pass membrane protein {ECO:0000269|PubMed:15606908}. Cell projection, stereocilium membrane {ECO:0000269|PubMed:16775142, ECO:0000269|PubMed:17567809, ECO:0000269|PubMed:20502675, ECO:0000269|PubMed:24334608, ECO:0000269|PubMed:27525485}. Photoreceptor inner segment {ECO:0000269|PubMed:20502675, ECO:0000269|PubMed:24334608}. Note=Localizes at the ankle region of the stereocilia (PubMed:16775142, PubMed:27525485). In photoreceptors, localizes at a plasma membrane microdomain in the apical inner segment that surrounds the connecting cilia called periciliary membrane complex (PubMed:20502675, PubMed:24334608). {ECO:0000269|PubMed:16775142, ECO:0000269|PubMed:20502675, ECO:0000269|PubMed:24334608, ECO:0000269|PubMed:27525485}.; SUBCELLULAR LOCATION: Isoform 4: Secreted {ECO:0000269|PubMed:15606908}.; SUBCELLULAR LOCATION: Isoform 5: Secreted {ECO:0000269|PubMed:15606908}. SUBUNIT: Forms a heterodimer, consisting of a large extracellular region (alpha subunit) non-covalently linked to a seven-transmembrane moiety (beta subunit) (PubMed:24962568). Interacts (via the cytoplasmic region) with PDZD7 (PubMed:24962568, PubMed:23055499). Component of USH2 complex, composed of ADGRV1, PDZD7, USH2A and WHRN (PubMed:20502675, PubMed:25406310). Interacts with USH2A and WHRN (PubMed:20502675, PubMed:23055499). Interacts (via the cytoplasmic region) with MYO7A (via MyTH4-FERM domains) (PubMed:17567809). {ECO:0000269|PubMed:17567809, ECO:0000269|PubMed:20502675, ECO:0000269|PubMed:23055499, ECO:0000269|PubMed:24962568, ECO:0000269|PubMed:25406310}. DOMAIN: The 7 transmembrane domain is required in hair cells for the hair bundle ankle formation. {ECO:0000269|PubMed:16775142}. TISSUE SPECIFICITY: Expressed by oligodendrocytes. In midbrain, enriched in the myelinated regions of the superior and inferior colliculi (PubMed:24191038). In the cochlea, expressed in develpong hair cells (PubMed:16775142, PubMed:20502675, PubMed:17567809). Expressed by photorecereptors in the retina (PubMed:20502675). {ECO:0000269|PubMed:16775142, ECO:0000269|PubMed:17567809, ECO:0000269|PubMed:20502675, ECO:0000269|PubMed:24191038}. +O88987 AKAP3_MOUSE A-kinase anchor protein 3 (AKAP-3) (A-kinase anchor protein 110 kDa) (AKAP 110) (Protein kinase A-anchoring protein 3) (PRKA3) 864 95,556 Chain (1); Modified residue (3); Region (1); Sequence conflict (1) FUNCTION: May function as a regulator of both motility- and head-associated functions such as capacitation and the acrosome reaction. {ECO:0000250}. PTM: Phosphorylated on tyrosine. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:11278869}. Note=Ribs of the fibrous sheath in the principal piece of the sperm tail. Dorsal margin of the acrosomal segment. SUBUNIT: Interacts with ROPN1 AND ROPN1L. {ECO:0000250}. DOMAIN: RII-binding site, predicted to form an amphipathic helix, could participate in protein-protein interactions with a complementary surface on the R-subunit dimer. +A2ALI5 AJAP1_MOUSE Adherens junction-associated protein 1 412 44,772 Chain (1); Compositional bias (1); Region (1); Topological domain (2); Transmembrane (1) TRANSMEM 285 305 Helical. {ECO:0000255}. TOPO_DOM 1 284 Extracellular. {ECO:0000255}.; TOPO_DOM 306 412 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a role in cell adhesion and cell migration. {ECO:0000250}. SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Apical cell membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Cell junction, adherens junction {ECO:0000250}. Note=Mainly basolateral. Localization is mediated by AP1M2 (By similarity). {ECO:0000250}. SUBUNIT: Forms a complex with CDH1 and CTNNB1; interacts directly with CTNNB1. Interacts with AP1M2 and BSG/CD147 (By similarity). {ECO:0000250}. +O08915 AIP_MOUSE AH receptor-interacting protein (AIP) (Aryl-hydrocarbon receptor-interacting protein) 330 37,605 Chain (1); Domain (1); Modified residue (1); Repeat (3) FUNCTION: May play a positive role in AHR-mediated (aromatic hydrocarbon receptor) signaling, possibly by influencing its receptivity for ligand and/or its nuclear targeting. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Interacts with RET in the pituitary gland; this interaction prevents the formation of the AIP-survivin complex. +P20782 ACHE_MOUSE Acetylcholine receptor subunit epsilon 493 54,914 Chain (1); Disulfide bond (1); Glycosylation (2); Signal peptide (1); Topological domain (5); Transmembrane (4) TRANSMEM 240 264 Helical. {ECO:0000255}.; TRANSMEM 273 291 Helical. {ECO:0000255}.; TRANSMEM 307 328 Helical. {ECO:0000255}.; TRANSMEM 457 480 Helical. {ECO:0000255}. TOPO_DOM 21 239 Extracellular.; TOPO_DOM 265 272 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 292 306 Extracellular. {ECO:0000255}.; TOPO_DOM 329 456 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 481 493 Extracellular. {ECO:0000255}. FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. SUBUNIT: Pentamer of two alpha chains, and one each of the beta, delta, and gamma (in immature muscle) or epsilon (in mature muscle) chains. The muscle heteropentamer composed of alpha-1, beta-1, delta, epsilon subunits interacts with the alpha-conotoxin ImII (By similarity). {ECO:0000250|UniProtKB:Q04844}. +Q9CR21 ACPM_MOUSE Acyl carrier protein, mitochondrial (ACP) (CI-SDAP) (NADH-ubiquinone oxidoreductase 9.6 kDa subunit) 156 17,370 Beta strand (1); Chain (1); Domain (1); Helix (4); Modified residue (2); Sequence conflict (1); Transit peptide (1); Turn (1) FUNCTION: Carrier of the growing fatty acid chain in fatty acid biosynthesis (By similarity). Accessory and non-catalytic subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), which functions in the transfer of electrons from NADH to the respiratory chain (By similarity). {ECO:0000250|UniProtKB:O14561, ECO:0000250|UniProtKB:P52505}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:O14561}. SUBUNIT: Mammalian complex I is composed of 45 different subunits. Interacts with ETFRF1. Identified in a complex composed of MALSU1, MIEF1 upstream open reading frame protein and NDUFAB1; within the trimeric complex MIEF1 upstream open reading frame protein functions as a bridging scaffold that interacts with MALSU1 on one side, and with NDUFAB1 on the other side. The complex interacts with the mitochondrial large ribosomal subunit. {ECO:0000250|UniProtKB:O14561}. +Q9QUJ7 ACSL4_MOUSE Long-chain-fatty-acid--CoA ligase 4 (EC 6.2.1.3) (Long-chain acyl-CoA synthetase 4) (LACS 4) (mACS4) 711 79,077 Alternative sequence (1); Chain (1); Modified residue (1); Sequence conflict (21); Topological domain (1); Transmembrane (1) TRANSMEM 8 28 Helical; Signal-anchor for type III membrane protein. {ECO:0000255}. TOPO_DOM 29 711 Cytoplasmic. {ECO:0000255}. FUNCTION: Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses arachidonate and eicosapentaenoate as substrates. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Peroxisome membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Microsome membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Abundant in steroidogenic tissues, also found in the kidney, brain and liver. +P18762 ADRB2_MOUSE Beta-2 adrenergic receptor (Beta-2 adrenoreceptor) (Beta-2 adrenoceptor) 418 46,998 Binding site (2); Chain (1); Disulfide bond (2); Glycosylation (2); Lipidation (1); Modified residue (10); Motif (1); Region (3); Sequence conflict (4); Topological domain (8); Transmembrane (7) TRANSMEM 35 58 Helical; Name=1. {ECO:0000250}.; TRANSMEM 72 95 Helical; Name=2. {ECO:0000250}.; TRANSMEM 107 129 Helical; Name=3. {ECO:0000250}.; TRANSMEM 151 174 Helical; Name=4. {ECO:0000250}.; TRANSMEM 197 220 Helical; Name=5. {ECO:0000250}.; TRANSMEM 275 298 Helical; Name=6. {ECO:0000250}.; TRANSMEM 306 329 Helical; Name=7. {ECO:0000250}. TOPO_DOM 1 34 Extracellular. {ECO:0000250}.; TOPO_DOM 59 71 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 96 106 Extracellular. {ECO:0000250}.; TOPO_DOM 130 150 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 175 196 Extracellular. {ECO:0000250}.; TOPO_DOM 221 274 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 299 305 Extracellular. {ECO:0000250}.; TOPO_DOM 330 418 Cytoplasmic. {ECO:0000250}. FUNCTION: Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. The beta-2-adrenergic receptor binds epinephrine with an approximately 30-fold greater affinity than it does norepinephrine. {ECO:0000269|PubMed:2834198}. PTM: Palmitoylated; may reduce accessibility of Ser-345 and Ser-346 by anchoring Cys-341 to the plasma membrane. Agonist stimulation promotes depalmitoylation and further allows Ser-345 and Ser-346 phosphorylation (By similarity). {ECO:0000250}.; PTM: Phosphorylated by PKA and BARK upon agonist stimulation, which mediates homologous desensitization of the receptor. PKA-mediated phosphorylation seems to facilitate phosphorylation by BARK.; PTM: Phosphorylation of Tyr-141 is induced by insulin and leads to supersensitization of the receptor. {ECO:0000250}.; PTM: Polyubiquitinated. Agonist-induced ubiquitination leads to sort internalized receptors to the lysosomes for degradation. Deubiquitination by USP20 and USP33, leads to ADRB2 recycling and resensitization after prolonged agonist stimulation. USP20 and USP33 are constitutively associated and are dissociated immediately after agonist stimulation. Ubiquitination by the VHL-E3 ligase complex is oxygen-dependent (By similarity). {ECO:0000250}.; PTM: Hydroxylation by EGLN3 occurs only under normoxia and increases the interaction with VHL and the subsequent ubiquitination and degradation of ADRB2. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2834198}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P07550}. Early endosome {ECO:0000250|UniProtKB:P07550}. Note=Colocalizes with VHL on cell membranes. Activated receptors are internalized into endosomes prior to their degradation in lysosomes. {ECO:0000250|UniProtKB:P07550}. SUBUNIT: Binds SLC9A3R1 and GPRASP1. Interacts with ARRB1 and ARRB2. Interacts with SRC, USP20 and USP33. Interacts with VHL; the interaction, which is increased on hydroxylation of ADRB2, ubiquitinates ADRB2 leading to its degradation. Interacts with EGLN3; the interaction hydroxylates ADRB2 facilitating VHL-E3 ligase-mediated ubiquitination. Interacts (via PDZ-binding motif) with SNX27 (via PDZ domain); the interaction is required when endocytosed to prevent degradation in lysosomes and promote recycling to the plasma membrane. Interacts with CNIH4. Interacts with ARRDC3. {ECO:0000250|UniProtKB:P07550}. +O88573 AFF1_MOUSE AF4/FMR2 family member 1 (Proto-oncogene AF4) (Protein AF-4) 1216 131,558 Chain (1); Compositional bias (5); Modified residue (6); Sequence conflict (4) SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Component of the super elongation complex (SEC), at least composed of EAF1, EAF2, CDK9, MLLT3/AF9, AFF (AFF1 or AFF4), the P-TEFb complex and ELL (ELL, ELL2 or ELL3). {ECO:0000250}. +P55264 ADK_MOUSE Adenosine kinase (AK) (EC 2.7.1.20) (Adenosine 5'-phosphotransferase) 361 40,149 Active site (1); Alternative sequence (1); Beta strand (15); Chain (1); Erroneous initiation (1); Helix (18); Metal binding (1); Modified residue (1); Motif (1); Mutagenesis (4); Sequence conflict (17); Turn (2) Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenosine: step 1/1. FUNCTION: ATP dependent phosphorylation of adenosine and other related nucleoside analogs to monophosphate derivatives. Serves as a potential regulator of concentrations of extracellular adenosine and intracellular adenine nucleotides. SUBCELLULAR LOCATION: Isoform Long: Nucleus {ECO:0000250|UniProtKB:P55263}.; SUBCELLULAR LOCATION: Isoform Short: Cytoplasm {ECO:0000250|UniProtKB:P55263}. SUBUNIT: Monomer. {ECO:0000250}. TISSUE SPECIFICITY: Highest expression in liver, testis, kidney and spleen. Lower expression in brain. Isoform Long is predominant in testis and kidney and isoform Short is predominant in the spleen. {ECO:0000269|PubMed:15317590}. +Q8K2K6 AGFG1_MOUSE Arf-GAP domain and FG repeat-containing protein 1 (HIV-1 Rev-binding protein homolog) (Nucleoporin-like protein RIP) 561 58,043 Alternative sequence (3); Chain (1); Domain (1); Glycosylation (1); Modified residue (4); Sequence conflict (5); Zinc finger (1) FUNCTION: Required for vesicle docking or fusion during acrosome biogenesis. May play a role in RNA trafficking or localization. {ECO:0000269|PubMed:11711676}. PTM: O-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P52594}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:P52594}. Note=Associated with the cytosolic surface of proacrosomic vesicles of early round spermatids. {ECO:0000269|PubMed:11711676}. SUBUNIT: Interacts with FCHO1 (By similarity). Interacts with EPS15R and EPS15. {ECO:0000250, ECO:0000269|PubMed:11711676, ECO:0000269|PubMed:9446614}. DOMAIN: Contains FG repeats. +Q58Y75 AGRF3_MOUSE Adhesion G-protein coupled receptor F3 (G-protein coupled receptor 113) (G-protein coupled receptor PGR23) 991 108,975 Chain (1); Domain (1); Glycosylation (10); Sequence conflict (2); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 695 715 Helical; Name=1. {ECO:0000255}.; TRANSMEM 731 751 Helical; Name=2. {ECO:0000255}.; TRANSMEM 758 778 Helical; Name=3. {ECO:0000255}.; TRANSMEM 800 820 Helical; Name=4. {ECO:0000255}.; TRANSMEM 851 871 Helical; Name=5. {ECO:0000255}.; TRANSMEM 893 913 Helical; Name=6. {ECO:0000255}.; TRANSMEM 917 937 Helical; Name=7. {ECO:0000255}. TOPO_DOM 21 694 Extracellular. {ECO:0000305}.; TOPO_DOM 716 730 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 752 757 Extracellular. {ECO:0000305}.; TOPO_DOM 779 799 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 821 850 Extracellular. {ECO:0000305}.; TOPO_DOM 872 892 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 914 916 Extracellular. {ECO:0000305}.; TOPO_DOM 938 991 Cytoplasmic. {ECO:0000305}. FUNCTION: Orphan receptor. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Expression is restricted to testis and circumvallate papillae. {ECO:0000269|PubMed:15780750}. +Q9D2L6 AGRF4_MOUSE Adhesion G protein-coupled receptor F4 (G-protein coupled receptor 115) 698 77,331 Chain (1); Compositional bias (1); Domain (1); Glycosylation (9); Sequence conflict (5); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 410 430 Helical; Name=1. {ECO:0000255}.; TRANSMEM 445 465 Helical; Name=2. {ECO:0000255}.; TRANSMEM 487 507 Helical; Name=3. {ECO:0000255}.; TRANSMEM 519 539 Helical; Name=4. {ECO:0000255}.; TRANSMEM 567 587 Helical; Name=5. {ECO:0000255}.; TRANSMEM 612 632 Helical; Name=6. {ECO:0000255}.; TRANSMEM 636 656 Helical; Name=7. {ECO:0000255}. TOPO_DOM 20 409 Extracellular. {ECO:0000305}.; TOPO_DOM 431 444 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 466 486 Extracellular. {ECO:0000305}.; TOPO_DOM 508 518 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 540 566 Extracellular. {ECO:0000305}.; TOPO_DOM 588 611 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 633 635 Extracellular. {ECO:0000305}.; TOPO_DOM 657 698 Cytoplasmic. {ECO:0000305}. FUNCTION: Orphan receptor. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Expressed in squamous epithelia. {ECO:0000269|PubMed:22837050}. +Q91VJ1 AIM2_MOUSE Interferon-inducible protein AIM2 (Interferon-inducible protein 210) (Ifi-210) (Interferon-inducible protein p210) 354 40,155 Beta strand (13); Chain (1); Domain (2); Erroneous initiation (1); Helix (9); Turn (2) FUNCTION: Involved in innate immune response by recognizing cytosolic double-stranded DNA and inducing caspase-1-activating inflammasome formation in macrophages. Upon binding to DNA is thought to undergo oligomerization and to associate with PYCARD initiating the recruitment of caspase-1 precusrsor and processing of interleukin-1 beta and interleukin-18. Detects cytosolic dsDNA of viral and bacterial origin in a non-sequence-specific manner. Can also trigger PYCARD-dependent, caspase-1-independent cell death that involves caspase-8. {ECO:0000269|PubMed:19131592, ECO:0000269|PubMed:19158675, ECO:0000269|PubMed:19158676, ECO:0000269|PubMed:20351692, ECO:0000269|PubMed:20351693, ECO:0000269|PubMed:20417169, ECO:0000269|PubMed:20457908, ECO:0000269|PubMed:21902795, ECO:0000269|PubMed:22555457, ECO:0000269|PubMed:23567559}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:22555457}. SUBUNIT: Self-associates; forms homooligomers in response to cytosolic dsDNA and the dsDNA seems to serve as oligomerization platform. Component of the AIM2 inflammasome complex. Interacts with PYCARD. Interacts with IFI16 (By similarity). Interacts with EIF2AK2/PKR (By similarity). Interacts with PYDC5; disrupts assembly of the ALR inflammasome complex (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O14862}. DOMAIN: The HIN-20 domain mediates dsDNA binding via electrostatic interactions. {ECO:0000269|PubMed:23567559}.; DOMAIN: The pyrin domain mediates homotypic interaction with PYCARD. {ECO:0000250}. +Q7TNK8 ADM2_MOUSE ADM2 (Intermedin) [Cleaved into: Adrenomedullin-2 (AM2) (Intermedin-long) (IMDL); Intermedin-short (IMDS)] 150 16,188 Disulfide bond (1); Modified residue (1); Peptide (2); Propeptide (1); Signal peptide (1) FUNCTION: IMDL and IMDS may play a role as physiological regulators of gastrointestinal, cardiovascular bioactivities mediated by the CALCRL/RAMPs receptor complexes. Activates the cAMP-dependent pathway. {ECO:0000269|PubMed:14615490, ECO:0000269|PubMed:14706825}. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: High expression detected in the submaxillary gland, kidney, stomach, and mesentery, followed by the pituitary, lung, pancreas, intestines, spleen, thymus and ovary. Expressed mainly in the intermediate lobe of the pituitary, with sporadic in the anterior lobe. {ECO:0000269|PubMed:14615490, ECO:0000269|PubMed:14706825}. +P51827 AFF3_MOUSE AF4/FMR2 family member 3 (Lymphoid nuclear protein related to AF4) (Protein LAF-4) 1254 136,131 Alternative sequence (2); Chain (1); Compositional bias (3); Modified residue (2); Sequence conflict (4) FUNCTION: Putative transcription activator that may function in lymphoid development and oncogenesis. SUBCELLULAR LOCATION: Nucleus. TISSUE SPECIFICITY: Highest levels found in lymphoid tissues, lower levels in brain and lung. +Q9Z248 AEBP2_MOUSE Zinc finger protein AEBP2 (Adipocyte enhancer-binding protein 2) (AE-binding protein 2) 504 52,963 Alternative sequence (4); Chain (1); Compositional bias (3); Frameshift (3); Initiator methionine (1); Modified residue (9); Mutagenesis (1); Region (2); Sequence conflict (4); Zinc finger (3) FUNCTION: May interact with and stimulate the activity of the PRC2 complex, which methylates 'Lys-9' and 'Lys-27' residues of histone H3 (By similarity). DNA-binding transcriptional repressor. {ECO:0000250, ECO:0000269|PubMed:10329662}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Self-associates (By similarity). Interacts with EED, EZH2, RBBP4 and SUZ12 (By similarity). Component of the PRC2/EED-EZH1 complex, which includes EED, EZH1, SUZ12, RBBP4 and AEBP2. May also interact with RBBP7 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain, brown adipose tissue, white adipose tissue, heart, kidney, lung, skeletal muscle, small intestine and spleen. Expressed at low levels in liver. {ECO:0000269|PubMed:10329662}. +Q9JKV1 ADRM1_MOUSE Proteasomal ubiquitin receptor ADRM1 (110 kDa cell membrane glycoprotein) (Gp110) (Adhesion-regulating molecule 1) (ARM-1) (Rpn13 homolog) 407 42,060 Beta strand (9); Chain (1); Compositional bias (3); Cross-link (1); Helix (1); Initiator methionine (1); Modified residue (6); Region (2); Sequence conflict (4); Turn (2) FUNCTION: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. Within the complex, functions as a proteasomal ubiquitin receptor. Engages and thus activates 19S-associated deubiquitinases UCHL5 and PSMD14 during protein degradation. UCHL5 reversibly associate with the 19S regulatory particle whereas PSMD14 is an intrinsic subunit of the proteasome lid subcomplex. {ECO:0000269|PubMed:15819879, ECO:0000269|PubMed:18497827}. PTM: Not N-glycosylated.; PTM: Not O-glycosylated. {ECO:0000305}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15819879}. Nucleus {ECO:0000250|UniProtKB:Q16186}. SUBUNIT: Component of the 19S proteasome regulatory particle complex. The 26S proteasome consists of a 20S core particle (CP) and two 19S regulatory subunits (RP). Interacts with the proteasomal scaffolding protein PSMD1 (PubMed:18497827). Interacts with deubiquitinase UCHL5; this interaction activates the auto-inhibited UCHL5 by deoligomerizing it. Interacts with UBQLN2 and ubiquitin. {ECO:0000250|UniProtKB:Q16186, ECO:0000269|PubMed:18497827}. DOMAIN: The Pru (pleckstrin-like receptor for ubiquitin) domain mediates interactions with PSMD1 and ubiquitin. Preferential binding to the proximal subunit of K48-linked diubiquitin allows UCHL5 access to the distal subunit. {ECO:0000269|PubMed:18497827}. TISSUE SPECIFICITY: Present in all tissues examined (at protein level). {ECO:0000269|PubMed:16815440, ECO:0000269|PubMed:17139257}. +Q9R1V7 ADA23_MOUSE Disintegrin and metalloproteinase domain-containing protein 23 (ADAM 23) (Metalloproteinase-like, disintegrin-like, and cysteine-rich protein 3) (MDC-3) 829 91,548 Alternative sequence (4); Chain (1); Compositional bias (1); Disulfide bond (7); Domain (3); Glycosylation (8); Propeptide (1); Sequence conflict (5); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 790 810 Helical. {ECO:0000255}. TOPO_DOM 284 789 Extracellular. {ECO:0000255}.; TOPO_DOM 811 829 Cytoplasmic. {ECO:0000255}. FUNCTION: May play a role in cell-cell and cell-matrix interactions. This is a non-catalytic metalloprotease-like protein (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: Isoform Gamma: Secreted. SUBUNIT: Can bind to LGI1 and LGI4. TISSUE SPECIFICITY: Brain specific. {ECO:0000269|PubMed:10433968}. +P48962 ADT1_MOUSE ADP/ATP translocase 1 (ADP,ATP carrier protein 1) (ADP,ATP carrier protein, heart/skeletal muscle isoform T1) (Adenine nucleotide translocator 1) (ANT 1) (Solute carrier family 25 member 4) (mANC1) 298 32,904 Binding site (3); Chain (1); Initiator methionine (1); Modified residue (8); Motif (1); Region (1); Repeat (3); Sequence conflict (1); Transmembrane (6) TRANSMEM 8 37 Helical; Name=1. {ECO:0000250|UniProtKB:P02722}.; TRANSMEM 75 99 Helical; Name=2. {ECO:0000250|UniProtKB:P02722}.; TRANSMEM 110 130 Helical; Name=3. {ECO:0000250|UniProtKB:P02722}.; TRANSMEM 179 199 Helical; Name=4. {ECO:0000250|UniProtKB:P02722}.; TRANSMEM 211 231 Helical; Name=5. {ECO:0000250|UniProtKB:P02722}.; TRANSMEM 274 291 Helical; Name=6. {ECO:0000250|UniProtKB:P02722}. FUNCTION: Involved in mitochondrial ADP/ATP transport. Catalyzes the exchange of cytoplasmic ADP with mitochondrial ATP across the mitochondrial inner membrane. {ECO:0000250|UniProtKB:P12235}. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. Note=The complex formed with ARL2BP, ARL2 and SLC25A4 is expressed in mitochondria. SUBUNIT: Homodimer. Found in a complex with ARL2, ARL2BP and SLC25A4. Interacts with ARL2BP. {ECO:0000269|PubMed:11809823}. DOMAIN: The transmembrane helices are not perpendicular to the plane of the membrane, but cross the membrane at an angle. Odd-numbered transmembrane helices exhibit a sharp kink, due to the presence of a conserved proline residue. {ECO:0000250|UniProtKB:P02722}. +Q9R159 ADA25_MOUSE Disintegrin and metalloproteinase domain-containing protein 25 (ADAM 25) (EC 3.4.24.-) (Testase-2) 760 86,128 Active site (1); Chain (1); Compositional bias (1); Disulfide bond (7); Domain (3); Glycosylation (7); Metal binding (4); Motif (1); Propeptide (1); Sequence conflict (6); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 707 727 Helical. {ECO:0000255}. TOPO_DOM 214 706 Extracellular. {ECO:0000255}.; TOPO_DOM 728 760 Cytoplasmic. {ECO:0000255}. FUNCTION: Sperm surface membrane protein that may be involved in spermatogenesis and fertilization. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. DOMAIN: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme. TISSUE SPECIFICITY: Expressed specifically in testis. +Q61578 ADRO_MOUSE NADPH:adrenodoxin oxidoreductase, mitochondrial (AR) (Adrenodoxin reductase) (EC 1.18.1.6) (Ferredoxin--NADP(+) reductase) (Ferredoxin reductase) 494 54,202 Binding site (7); Chain (1); Modified residue (1); Nucleotide binding (3); Transit peptide (1) Steroid metabolism; cholesterol metabolism. FUNCTION: Serves as the first electron transfer protein in all the mitochondrial P450 systems including cholesterol side chain cleavage in all steroidogenic tissues, steroid 11-beta hydroxylation in the adrenal cortex, 25-OH-vitamin D3-24 hydroxylation in the kidney, and sterol C-27 hydroxylation in the liver. {ECO:0000250|UniProtKB:P08165}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P48360}; Peripheral membrane protein {ECO:0000305}. SUBUNIT: Monomer. Interacts directly with FDX1. {ECO:0000250|UniProtKB:P08165}. TISSUE SPECIFICITY: Expressed in the adrenal, testis and ovary and to a lesser extent in the liver and kidney. {ECO:0000269|PubMed:7495857}. +Q8CJG0 AGO2_MOUSE Protein argonaute-2 (Argonaute2) (mAgo2) (EC 3.1.26.n2) (Argonaute RISC catalytic component 2) (Eukaryotic translation initiation factor 2C 2) (eIF-2C 2) (eIF2C 2) (Piwi/argonaute family protein meIF2C2) (Protein slicer) 860 97,304 Chain (1); Domain (2); Erroneous initiation (1); Metal binding (3); Modified residue (4); Region (7); Sequence conflict (7) FUNCTION: Required for RNA-mediated gene silencing (RNAi) by the RNA-induced silencing complex (RISC). The 'minimal RISC' appears to include AGO2 bound to a short guide RNA such as a microRNA (miRNA) or short interfering RNA (siRNA). These guide RNAs direct RISC to complementary mRNAs that are targets for RISC-mediated gene silencing. The precise mechanism of gene silencing depends on the degree of complementarity between the miRNA or siRNA and its target. Binding of RISC to a perfectly complementary mRNA generally results in silencing due to endonucleolytic cleavage of the mRNA specifically by AGO2. Binding of RISC to a partially complementary mRNA results in silencing through inhibition of translation, and this is independent of endonuclease activity. May inhibit translation initiation by binding to the 7-methylguanosine cap, thereby preventing the recruitment of the translation initiation factor eIF4-E. May also inhibit translation initiation via interaction with EIF6, which itself binds to the 60S ribosomal subunit and prevents its association with the 40S ribosomal subunit. The inhibition of translational initiation leads to the accumulation of the affected mRNA in cytoplasmic processing bodies (P-bodies), where mRNA degradation may subsequently occur. In some cases RISC-mediated translational repression is also observed for miRNAs that perfectly match the 3' untranslated region (3'-UTR). Can also up-regulate the translation of specific mRNAs under certain growth conditions. Binds to the AU element of the 3'-UTR of the TNF (TNF-alpha) mRNA and up-regulates translation under conditions of serum starvation. Also required for transcriptional gene silencing (TGS), in which short RNAs known as antigene RNAs or agRNAs direct the transcriptional repression of complementary promoter regions. Regulates lymphoid and erythroid development and function, and this is independent of endonuclease activity. {ECO:0000255|HAMAP-Rule:MF_03031, ECO:0000269|PubMed:15284456, ECO:0000269|PubMed:17626790, ECO:0000269|PubMed:19174539}. PTM: Hydroxylated. 4-hydroxylation appears to enhance protein stability but is not required for miRNA-binding or endonuclease activity. {ECO:0000255|HAMAP-Rule:MF_03031}. SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000255|HAMAP-Rule:MF_03031}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03031}. Note=Translational repression of mRNAs results in their recruitment to P-bodies. Translocation to the nucleus requires IMP8. {ECO:0000255|HAMAP-Rule:MF_03031}. SUBUNIT: Interacts with DICER1 through its Piwi domain and with TARBP2 during assembly of the RNA-induced silencing complex (RISC). Together, DICER1, AGO2 and TARBP2 constitute the trimeric RISC loading complex (RLC), or micro-RNA (miRNA) loading complex (miRLC). Within the RLC/miRLC, DICER1 and TARBP2 are required to process precursor miRNAs (pre-miRNAs) to mature miRNAs and then load them onto AGO2. AGO2 bound to the mature miRNA constitutes the minimal RISC and may subsequently dissociate from DICER1 and TARBP2. Note however that the term RISC has also been used to describe the trimeric RLC/miRLC. The formation of RISC complexes containing siRNAs rather than miRNAs appears to occur independently of DICER1 (PubMed:16357216). Interacts with AGO1. Also interacts with DDB1, DDX5, DDX6, DDX20, DHX30, DHX36, DDX47, DHX9, ELAVL, FXR1, GEMIN4, HNRNPF, IGF2BP1, ILF3, IMP8, MATR3, PABPC1, PRMT5, P4HA1, P4HB, RBM4, SART3, TNRC6A, TNRC6B, UPF1 and YBX1. Interacts with the P-body components DCP1A and XRN1. Associates with polysomes and messenger ribonucleoproteins (mNRPs). Interacts with RBM4; the interaction is modulated under stress-induced conditions, occurs under both cell proliferation and differentiation conditions and in an RNA- and phosphorylation-independent manner. Interacts with LIMD1, WTIP and AJUBA (By similarity). Interacts with TRIM71 (PubMed:19898466, PubMed:22508726, PubMed:22735451). Interacts with APOBEC3G in an RNA-dependent manner. Interacts with APOBEC3A, APOBEC3C, APOBEC3F and APOBEC3H. Interacts with DICER1, TARBP2, EIF6, MOV10 and RPL7A (60S ribosome subunit); they form a large RNA-induced silencing complex (RISC). Interacts with FMR1. Interacts with ZFP36 (By similarity). Interacts with RC3H1; the interaction is RNA independent (PubMed:25697406). Interacts with FAM172A (PubMed:29311329). Found in a complex composed of AGO2, CHD7 and FAM172A (PubMed:29311329). Interacts with SND1 (By similarity). {ECO:0000250|UniProtKB:Q9UKV8, ECO:0000255|HAMAP-Rule:MF_03031, ECO:0000269|PubMed:16357216, ECO:0000269|PubMed:19898466, ECO:0000269|PubMed:22508726, ECO:0000269|PubMed:22735451, ECO:0000269|PubMed:25697406, ECO:0000269|PubMed:29311329}. DOMAIN: The Piwi domain may perform RNA cleavage by a mechanism similar to that of RNase H. However, while RNase H utilizes a triad of Asp-Asp-Glu (DDE) for metal ion coordination, this protein appears to utilize a triad of Asp-Asp-His (DDH). {ECO:0000255|HAMAP-Rule:MF_03031}. TISSUE SPECIFICITY: Ubiquitous expression in 9.5 day embryos with highest levels in forebrain, heart, limb buds, and branchial arches. {ECO:0000269|PubMed:15284456}. +Q8K3E5 AHI1_MOUSE Jouberin (Abelson helper integration site 1 protein) (AHI-1) 1047 119,650 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (1); Modified residue (2); Region (1); Repeat (7); Sequence conflict (4) FUNCTION: Involved in vesicle trafficking and required for ciliogenesis, formation of primary non-motile cilium, and recruitment of RAB8A to the basal body of primary cilium (PubMed:19625297). Component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes (PubMed:22179047). Involved in neuronal differentiation (PubMed:23658157). As a positive modulator of classical Wnt signaling, may play a crucial role in ciliary signaling during cerebellum embryonic development (PubMed:21623382). {ECO:0000269|PubMed:19625297, ECO:0000269|PubMed:21623382, ECO:0000269|PubMed:22179047, ECO:0000269|PubMed:23658157}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:18633336, ECO:0000269|PubMed:19625297, ECO:0000269|PubMed:21623382}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:19625297}. Cell junction, adherens junction {ECO:0000250|UniProtKB:Q8N157}. SUBUNIT: Self-associates (By similarity). Part of the tectonic-like complex (also named B9 complex) (PubMed:22179047). Interacts with MKS1 (PubMed:21565611). Interacts with NPHP1; probably as heterodimers and/or AHI1(2):NPHP1(2) heterotetramers (PubMed:18633336). Interacts (via SH3 domain) with the dynamin GTPase DNM2 (By similarity). Interacts with HAP1; probably as AHI1(2):HAP1(2) heterotetramers (By similarity) (PubMed:23658157). Interacts with RAB8A (PubMed:19625297). Interacts with CEND1 (PubMed:23658157). {ECO:0000250|UniProtKB:Q8N157, ECO:0000269|PubMed:18633336, ECO:0000269|PubMed:19625297, ECO:0000269|PubMed:21565611, ECO:0000269|PubMed:22179047, ECO:0000269|PubMed:23658157}. TISSUE SPECIFICITY: Highly expressed in the brain and testis. Weakly expressed in the liver. Strongly expressed during periods of both cortical and cerebellar development. {ECO:0000269|PubMed:12186888, ECO:0000269|PubMed:15467982}. +Q8BUE4 AIFM2_MOUSE Apoptosis-inducing factor 2 (EC 1.-.-.-) (Apoptosis-inducing factor homologous mitochondrion-associated inducer of death) (Apoptosis-inducing factor-like mitochondrion-associated inducer of death) 373 40,635 Alternative sequence (1); Binding site (3); Chain (1); Initiator methionine (1); Lipidation (1); Nucleotide binding (1); Sequence caution (1); Transmembrane (1) TRANSMEM 7 27 Helical. {ECO:0000255}. FUNCTION: Oxidoreductase, which may play a role in mediating a p53/TP53-dependent apoptosis response. Probable oxidoreductase that acts as a caspase-independent mitochondrial effector of apoptotic cell death (By similarity). May contribute to genotoxin-induced growth arrest. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion outer membrane {ECO:0000250}. Membrane {ECO:0000250|UniProtKB:Q9BRQ8}; Lipid-anchor {ECO:0000250|UniProtKB:Q9BRQ8}. TISSUE SPECIFICITY: Detected in most normal tissues as two transcripts of 1.8 and 4.0 kb in length, respectively. Highly expressed in liver, testis, and kidney, and expressed at lower levels in pancreas, spleen, brain and lung. {ECO:0000269|PubMed:16186796}. +P35374 AGTR2_MOUSE Type-2 angiotensin II receptor (Angiotensin II type-2 receptor) (AT2) 363 41,374 Chain (1); Disulfide bond (2); Erroneous initiation (1); Glycosylation (5); Modified residue (1); Topological domain (8); Transmembrane (7) TRANSMEM 46 71 Helical; Name=1. {ECO:0000255}.; TRANSMEM 81 102 Helical; Name=2. {ECO:0000255}.; TRANSMEM 120 140 Helical; Name=3. {ECO:0000255}.; TRANSMEM 161 179 Helical; Name=4. {ECO:0000255}.; TRANSMEM 209 234 Helical; Name=5. {ECO:0000255}.; TRANSMEM 257 278 Helical; Name=6. {ECO:0000255}.; TRANSMEM 298 318 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 45 Extracellular. {ECO:0000255}.; TOPO_DOM 72 80 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 103 119 Extracellular. {ECO:0000255}.; TOPO_DOM 141 160 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 180 208 Extracellular. {ECO:0000255}.; TOPO_DOM 235 256 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 279 297 Extracellular. {ECO:0000255}.; TOPO_DOM 319 363 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for angiotensin II. Cooperates with MTUS1 to inhibit ERK2 activation and cell proliferation. {ECO:0000269|PubMed:15539617}. PTM: C-terminal Ser or Thr residues may be phosphorylated. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15539617}; Multi-pass membrane protein {ECO:0000269|PubMed:15539617}. SUBUNIT: Interacts with MTUS1. {ECO:0000269|PubMed:15539617}. TISSUE SPECIFICITY: Expressed at highest levels in adrenal gland and uterus. {ECO:0000269|PubMed:15539617}. +Q91WR5 AK1CL_MOUSE Aldo-keto reductase family 1 member C21 (EC 1.1.1.-) (17-alpha-hydroxysteroid dehydrogenase) (17-alpha-HSD) (3(or 17)-alpha-hydroxysteroid dehydrogenase) (EC 1.1.1.209) (3-alpha-hydroxysteroid dehydrogenase) (Dihydrodiol dehydrogenase type 1) (DD1) (Dihydrodiol dehydrogenase type 3) (DD3) 323 36,877 Active site (1); Beta strand (14); Binding site (4); Chain (1); Helix (17); Mutagenesis (5); Nucleotide binding (4); Sequence conflict (16); Site (1); Turn (3) FUNCTION: NADP-dependent 17-alpha-hydroxysteroid dehydrogenase that converts 5-alpha-androstane-3,17-dione into androsterone. Has lower 3-alpha-hydroxysteroid dehydrogenase activity. Has broad substrate specificity and acts on various 17-alpha-hydroxysteroids, 17-ketosteroids, 3-alpha hydroxysteroids and 3-ketosteroids. Reduction of keto groups is strictly stereoselective. Reduction of 17-ketosteroids yields only 17-alpha-hydroxysteroids. Likewise, reduction of 3-ketosteroids yields only 3-alpha-hydroxysteroids. {ECO:0000269|PubMed:15577209, ECO:0000269|PubMed:16018803, ECO:0000269|PubMed:17034817, ECO:0000269|PubMed:17442338, ECO:0000269|PubMed:20124700}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000269|PubMed:15577209, ECO:0000269|PubMed:17034817, ECO:0000269|PubMed:17442338, ECO:0000269|PubMed:17909281, ECO:0000269|PubMed:19237748}. TISSUE SPECIFICITY: Detected in kidney and brain. {ECO:0000269|PubMed:15577209, ECO:0000269|PubMed:16018803}. +Q7TT36 AGRA3_MOUSE Adhesion G protein-coupled receptor A3 (G-protein coupled receptor 125) 1310 144,697 Chain (1); Compositional bias (2); Disulfide bond (1); Domain (4); Erroneous initiation (1); Glycosylation (13); Motif (1); Repeat (4); Sequence conflict (2); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 748 768 Helical; Name=1. {ECO:0000255}.; TRANSMEM 786 806 Helical; Name=2. {ECO:0000255}.; TRANSMEM 816 836 Helical; Name=3. {ECO:0000255}.; TRANSMEM 866 886 Helical; Name=4. {ECO:0000255}.; TRANSMEM 909 929 Helical; Name=5. {ECO:0000255}.; TRANSMEM 986 1006 Helical; Name=6. {ECO:0000255}.; TRANSMEM 1014 1034 Helical; Name=7. {ECO:0000255}. TOPO_DOM 28 747 Extracellular. {ECO:0000305}.; TOPO_DOM 769 785 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 807 815 Extracellular. {ECO:0000305}.; TOPO_DOM 837 865 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 887 908 Extracellular. {ECO:0000305}.; TOPO_DOM 930 985 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1007 1013 Extracellular. {ECO:0000305}.; TOPO_DOM 1035 1310 Cytoplasmic. {ECO:0000305}. FUNCTION: Orphan receptor that may have a role in planar cell polarity pathway. {ECO:0000250|UniProtKB:S4X0Q8}. SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:S4X0Q8}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Interacts (via PDZ-binding motif) with DLG1. {ECO:0000250|UniProtKB:Q8IWK6}. TISSUE SPECIFICITY: Expressed by spermatogonial progenitor cells located within the outer cell layer of the seminiferous tubule and by multipotent adult spermatogonial-derived stem cells. {ECO:0000269|PubMed:17882221}. +Q80TR1 AGRL1_MOUSE Adhesion G protein-coupled receptor L1 (Calcium-independent alpha-latrotoxin receptor 1) (CIRL-1) (Latrophilin-1) (Lectomedin-2) 1466 161,686 Alternative sequence (1); Beta strand (6); Binding site (1); Chain (1); Compositional bias (2); Disulfide bond (9); Domain (3); Glycosylation (7); Helix (3); Modified residue (5); Mutagenesis (3); Region (1); Signal peptide (1); Site (1); Topological domain (8); Transmembrane (7) TRANSMEM 853 873 Helical; Name=1. {ECO:0000255}.; TRANSMEM 888 908 Helical; Name=2. {ECO:0000255}.; TRANSMEM 915 935 Helical; Name=3. {ECO:0000255}.; TRANSMEM 959 979 Helical; Name=4. {ECO:0000255}.; TRANSMEM 997 1017 Helical; Name=5. {ECO:0000255}.; TRANSMEM 1045 1065 Helical; Name=6. {ECO:0000255}.; TRANSMEM 1070 1090 Helical; Name=7. {ECO:0000255}. TOPO_DOM 29 852 Extracellular. {ECO:0000255}.; TOPO_DOM 874 887 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 909 914 Extracellular. {ECO:0000255}.; TOPO_DOM 936 958 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 980 996 Extracellular. {ECO:0000255}.; TOPO_DOM 1018 1044 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1066 1069 Extracellular. {ECO:0000255}.; TOPO_DOM 1091 1466 Cytoplasmic. {ECO:0000255}. FUNCTION: Calcium-independent receptor of high affinity for alpha-latrotoxin, an excitatory neurotoxin present in black widow spider venom which triggers massive exocytosis from neurons and neuroendocrine cells. Receptor for TENM2 that mediates heterophilic synaptic cell-cell contact and postsynaptic specialization. Receptor probably implicated in the regulation of exocytosis (By similarity). {ECO:0000250}. PTM: Autoproteolytically cleaved into 2 subunits, an extracellular subunit and a seven-transmembrane subunit. This proteolytic processing takes place early in the biosynthetic pathway, either in the endoplasmic reticulum or in the early compartment of the Golgi apparatus. {ECO:0000250|UniProtKB:O88917}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell projection, axon {ECO:0000250|UniProtKB:O88917}. Cell projection, growth cone {ECO:0000250|UniProtKB:O88917}. Cell junction, synapse {ECO:0000250|UniProtKB:O88917}. Cell junction, synapse, presynaptic cell membrane {ECO:0000250|UniProtKB:O88917}. Cell junction, synapse, synaptosome {ECO:0000250|UniProtKB:O88917}. Note=Colocalizes with TENM2 on the cell surface, across intercellular junctions and on nerve terminals near synaptic clefts. {ECO:0000250|UniProtKB:O88917}. SUBUNIT: Forms a heterodimer, consisting of a large extracellular region (p120) non-covalently linked to a seven-transmembrane moiety (p85). Interacts with syntaxin and with proteins of the SHANK family via the PDZ domain (By similarity). Interacts (via extracellular domain) with FLRT1, FLRT2 and FLRT3 (via extracellular domain) (PubMed:22405201). {ECO:0000250|UniProtKB:O88917, ECO:0000269|PubMed:22405201}. DOMAIN: The extracellular domain coupled to the a single transmembrane region are sufficient for full responsiveness to alpha-latrotoxin. {ECO:0000250}. +Q9D081 ALG14_MOUSE UDP-N-acetylglucosamine transferase subunit ALG14 homolog 217 24,429 Chain (1); Topological domain (2); Transmembrane (1) TRANSMEM 4 26 Helical. {ECO:0000255}. TOPO_DOM 1 3 Lumenal. {ECO:0000250|UniProtKB:P38242}.; TOPO_DOM 27 217 Cytoplasmic. {ECO:0000250|UniProtKB:P38242}. FUNCTION: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway. Anchors the catalytic subunit ALG13 to the ER (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P38242}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:P38242}; Single-pass membrane protein {ECO:0000255}. SUBUNIT: Heterodimer with ALG13 to form a functional enzyme. {ECO:0000250}. +Q9CXB8 ALPK1_MOUSE Alpha-protein kinase 1 (EC 2.7.11.1) 1231 136,134 Binding site (6); Chain (1); Compositional bias (1); Domain (1); Region (2); Sequence conflict (3) FUNCTION: Serine/threonine-protein kinase that detects bacterial pathogen-associated molecular pattern metabolites (PAMPs) and initiates an innate immune response, a critical step for pathogen elimination and engagement of adaptive immunity (By similarity). Specifically recognizes and binds ADP-D-glycero-beta-D-manno-heptose (ADP-Heptose), a potent PAMP present in all Gram-negative and some Gram-positive bacteria (PubMed:30111836). ADP-Heptose-binding stimulates its kinase activity to phosphorylate and activate TIFA, triggering proinflammatory NF-kappa-B signaling (By similarity). May be involved in monosodium urate monohydrate (MSU)-induced inflammation by mediating phosphorylation of unconventional myosin MYO9A (By similarity). May also play a role in apical protein transport by mediating phosphorylation of unconventional myosin MYO1A (By similarity). {ECO:0000250|UniProtKB:Q96QP1, ECO:0000269|PubMed:30111836}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q96QP1}. +O09174 AMACR_MOUSE Alpha-methylacyl-CoA racemase (EC 5.1.99.4) (2-methylacyl-CoA racemase) 381 41,704 Active site (1); Chain (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (7); Motif (1); Sequence conflict (1) Lipid metabolism; bile acid biosynthesis. Lipid metabolism; fatty acid metabolism. FUNCTION: Racemization of 2-methyl-branched fatty acid CoA esters. Responsible for the conversion of pristanoyl-CoA and C27-bile acyl-CoAs to their (S)-stereoisomers. SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:10770938}. Mitochondrion {ECO:0000269|PubMed:10770938}. +Q9D6Z0 ALKB7_MOUSE Alpha-ketoglutarate-dependent dioxygenase alkB homolog 7, mitochondrial (EC 1.14.11.-) (Alkylated DNA repair protein alkB homolog 7) 221 24,970 Alternative sequence (1); Binding site (2); Chain (1); Erroneous initiation (1); Metal binding (3); Region (1); Sequence conflict (1); Transit peptide (1) FUNCTION: May function as protein hydroxylase; can catalyze auto-hydroxylation at Leu-110 (in vitro), but this activity may be due to the absence of the true substrate. Required to induce programmed necrosis in response to DNA damage caused by cytotoxic alkylating agents. Acts by triggering the collapse of mitochondrial membrane potential and loss of mitochondrial function that leads to energy depletion and cell death. ALKBH7-mediated necrosis is probably required to prevent the accumulation of cells with DNA damage. Does not display DNA demethylase activity (By similarity). Involved in fatty acid metabolism. {ECO:0000250|UniProtKB:Q9BT30, ECO:0000269|PubMed:23572141}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:23572141}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:23572141}. +Q61288 ACVL1_MOUSE Serine/threonine-protein kinase receptor R3 (SKR3) (EC 2.7.11.30) (Activin receptor-like kinase 1) (ALK-1) (TGF-B superfamily receptor type I) (TSR-I) 502 56,519 Active site (1); Binding site (1); Chain (1); Disulfide bond (5); Domain (2); Glycosylation (2); Modified residue (3); Nucleotide binding (1); Region (1); Sequence conflict (7); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 120 140 Helical. {ECO:0000255}. TOPO_DOM 23 119 Extracellular. {ECO:0000255}.; TOPO_DOM 141 502 Cytoplasmic. {ECO:0000255}. FUNCTION: Type I receptor for TGF-beta family ligands BMP9/GDF2 and BMP10 and important regulator of normal blood vessel development. On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. May bind activin as well. {ECO:0000250|UniProtKB:P37023}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P37023}; Single-pass type I membrane protein {ECO:0000255}. +Q9D9L5 ACTT2_MOUSE Actin-related protein T2 (ARP-T2) (Actin-related protein M2) 377 41,616 Chain (1) SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. +O35227 ADAM7_MOUSE Disintegrin and metalloproteinase domain-containing protein 7 (ADAM 7) 789 89,188 Chain (1); Compositional bias (1); Disulfide bond (4); Domain (2); Glycosylation (6); Propeptide (1); Sequence conflict (11); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 668 689 Helical. {ECO:0000255}. TOPO_DOM 24 667 Extracellular. {ECO:0000255}.; TOPO_DOM 690 789 Cytoplasmic. {ECO:0000255}. FUNCTION: May play an important role in male reproduction including sperm maturation and gonadotrope function. This is a non catalytic metalloprotease-like protein. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. TISSUE SPECIFICITY: Expressed in the apical region of the proximal caput epididymal epithelium and in the anterior pituitary, specifically, in the gonadotrophes. +Q05910 ADAM8_MOUSE Disintegrin and metalloproteinase domain-containing protein 8 (ADAM 8) (EC 3.4.24.-) (Cell surface antigen MS2) (Macrophage cysteine-rich glycoprotein) (CD antigen CD156a) 826 90,046 Active site (1); Chain (1); Disulfide bond (12); Domain (3); Glycosylation (4); Metal binding (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 659 683 Helical. {ECO:0000255}. TOPO_DOM 17 658 Extracellular. {ECO:0000255}.; TOPO_DOM 684 826 Cytoplasmic. {ECO:0000255}. FUNCTION: Possible involvement in extravasation of leukocytes. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Interacts with FST3. {ECO:0000250}. TISSUE SPECIFICITY: Macrophages. +P97717 ADA1B_MOUSE Alpha-1B adrenergic receptor (Alpha-1B adrenoreceptor) (Alpha-1B adrenoceptor) 514 56,418 Chain (1); Compositional bias (1); Disulfide bond (1); Glycosylation (4); Lipidation (1); Modified residue (1); Motif (1); Topological domain (8); Transmembrane (7) TRANSMEM 46 69 Helical; Name=1. {ECO:0000250}.; TRANSMEM 83 104 Helical; Name=2. {ECO:0000250}.; TRANSMEM 115 140 Helical; Name=3. {ECO:0000250}.; TRANSMEM 161 183 Helical; Name=4. {ECO:0000250}.; TRANSMEM 201 223 Helical; Name=5. {ECO:0000250}.; TRANSMEM 295 318 Helical; Name=6. {ECO:0000250}.; TRANSMEM 326 350 Helical; Name=7. {ECO:0000250}. TOPO_DOM 1 45 Extracellular. {ECO:0000250}.; TOPO_DOM 70 82 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 105 114 Extracellular. {ECO:0000250}.; TOPO_DOM 141 160 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 184 200 Extracellular. {ECO:0000250}.; TOPO_DOM 224 294 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 319 325 Extracellular. {ECO:0000250}.; TOPO_DOM 351 514 Cytoplasmic. {ECO:0000250}. FUNCTION: This alpha-adrenergic receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. Its effect is mediated by G(q) and G(11) proteins. Nuclear ADRA1A-ADRA1B heterooligomers regulate phenylephrine (PE)-stimulated ERK signaling in cardiac myocytes (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:22120526}; Multi-pass membrane protein {ECO:0000269|PubMed:22120526}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250|UniProtKB:P35368}. Membrane, caveola {ECO:0000250|UniProtKB:P35368}. Note=Location at the nuclear membrane facilitates heterooligomerization and regulates ERK-mediated signaling in cardiac myocytes. Colocalizes with GNAQ, PLCB1 as well as LAP2 at the nuclear membrane of cardiac myocytes (By similarity). {ECO:0000250}. SUBUNIT: Homo- and heterooligomer. Heterooligomerizes with ADRA1B homooligomers in cardiac myocytes. Interacts with CAVIN4. {ECO:0000250|UniProtKB:P35368}. +Q3V384 AFG1L_MOUSE AFG1-like ATPase (EC 3.6.-.-) (Lactation elevated protein 1) 480 54,313 Chain (1); Nucleotide binding (2); Sequence conflict (1) FUNCTION: Putative mitochondrial ATPase. Plays a role in mitochondrial morphology and mitochondrial protein metabolism. Promotes degradation of excess nuclear-encoded complex IV subunits (COX4I1, COX5A and COX6A1) and normal activity of complexes III and IV of the respiratory chain. Mediates mitochondrial translocation of TP53 and its transcription-independent apoptosis in response to genotoxic stress. {ECO:0000250|UniProtKB:Q8WV93}. SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250|UniProtKB:Q8WV93}. SUBUNIT: Found in several complexes of 140-500 kDa. Interacts with YME1L1. Interacts with COX4I1. Interacts with COX5A. Interacts with TP53; mediates mitochondrial translocation of TP53 in response to genotoxic stress such as mitomycin C treatment. {ECO:0000250|UniProtKB:Q8WV93}. TISSUE SPECIFICITY: Highly expressed in heart, kidney, and lactating breast. Present at reduced levels in virgin, pregnant, and involuting breast. {ECO:0000269|PubMed:12079282}. +Q3UMC0 AFG2H_MOUSE ATPase family protein 2 homolog (EC 3.6.4.10) (Spermatogenesis-associated factor protein) (Spermatogenesis-associated protein 5) 893 97,256 Chain (1); Cross-link (1); Modified residue (3); Nucleotide binding (2); Sequence conflict (11) FUNCTION: ATP-dependent chaperone which uses the energy provided by ATP hydrolysis to generate mechanical force to disassemble protein complexes (By similarity). May be involved in morphological and functional mitochondrial transformations during spermatogenesis (PubMed:10734318). {ECO:0000250|UniProtKB:P32794, ECO:0000269|PubMed:10734318}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10734318}. Mitochondrion {ECO:0000269|PubMed:10734318}. SUBUNIT: Homohexamer; ATP binding induces oligomerization. Forms a ring-shaped particle of about 12 nm diameter, that displays 6-fold radial symmetry. {ECO:0000250|UniProtKB:P32794}. DOMAIN: The first ATP-binding region binds ATP with low affinity whereas the second ATP-binding region binds ATP with high affinity. {ECO:0000250|UniProtKB:P32794}. TISSUE SPECIFICITY: Expressed in testis; with localization to spermatogonia and early spermatocytes in the basal compartment of the seminiferous tubules (at early stages of spermatogenesis). Very weak signals observed in spleen and skin. {ECO:0000269|PubMed:10734318}. +P56473 AGRP_MOUSE Agouti-related protein 131 14,432 Chain (1); Disulfide bond (5); Domain (1); Propeptide (1); Region (1); Signal peptide (1); Site (1) FUNCTION: Plays a role in weight homeostasis. Involved in the control of feeding behavior through the central melanocortin system. Acts as alpha melanocyte-stimulating hormone antagonist by inhibiting cAMP production mediated by stimulation of melanocortin receptors within the hypothalamus and adrenal gland. Has very low activity with MC5R. Is an inverse agonist for MC3R and MC4R being able to suppress their constitutive activity (By similarity). It promotes MC3R and MC4R endocytosis in an arrestin-dependent manner (By similarity). {ECO:0000250, ECO:0000269|PubMed:9892020}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O00253}. Golgi apparatus lumen {ECO:0000250|UniProtKB:O00253}. SUBUNIT: Interacts with melanocortin receptors MC3R, MC4R and MC5R. {ECO:0000269|PubMed:9892020}. DOMAIN: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin. {ECO:0000250|UniProtKB:O00253}. TISSUE SPECIFICITY: Expressed in arcuate nucleus and median eminence, adrenal gland (medulla), hypothalamus, testis, and lung. +B7ZCC9 AGRG4_MOUSE Adhesion G-protein coupled receptor G4 (G-protein coupled receptor 112) 3073 334,211 Alternative sequence (2); Chain (1); Compositional bias (1); Disulfide bond (1); Domain (2); Glycosylation (5); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 2692 2712 Helical; Name=1. {ECO:0000255}.; TRANSMEM 2729 2749 Helical; Name=2. {ECO:0000255}.; TRANSMEM 2756 2776 Helical; Name=3. {ECO:0000255}.; TRANSMEM 2799 2819 Helical; Name=4. {ECO:0000255}.; TRANSMEM 2843 2863 Helical; Name=5. {ECO:0000255}.; TRANSMEM 2893 2913 Helical; Name=6. {ECO:0000255}.; TRANSMEM 2915 2935 Helical; Name=7. {ECO:0000255}. TOPO_DOM 26 2691 Extracellular. {ECO:0000305}.; TOPO_DOM 2713 2728 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 2750 2755 Extracellular. {ECO:0000305}.; TOPO_DOM 2777 2798 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 2820 2842 Extracellular. {ECO:0000305}.; TOPO_DOM 2864 2892 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 2914 2914 Extracellular. {ECO:0000305}.; TOPO_DOM 2936 3073 Cytoplasmic. {ECO:0000305}. FUNCTION: Orphan receptor. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. +Q8JZZ7 AGRL2_MOUSE Adhesion G protein-coupled receptor L2 (Calcium-independent alpha-latrotoxin receptor 2) (CIRL-2) (Latrophilin-2) 1487 166,577 Alternative sequence (2); Chain (1); Domain (3); Erroneous initiation (1); Glycosylation (3); Modified residue (3); Signal peptide (1); Site (1); Topological domain (7); Transmembrane (7) TRANSMEM 856 876 Helical; Name=1. {ECO:0000255}.; TRANSMEM 885 905 Helical; Name=2. {ECO:0000255}.; TRANSMEM 912 932 Helical; Name=3. {ECO:0000255}.; TRANSMEM 956 976 Helical; Name=4. {ECO:0000255}.; TRANSMEM 995 1015 Helical; Name=5. {ECO:0000255}.; TRANSMEM 1065 1085 Helical; Name=6. {ECO:0000255}.; TRANSMEM 1091 1111 Helical; Name=7. {ECO:0000255}. TOPO_DOM 26 855 Extracellular. {ECO:0000305}.; TOPO_DOM 877 884 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 906 911 Extracellular. {ECO:0000305}.; TOPO_DOM 933 955 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 977 994 Extracellular. {ECO:0000305}.; TOPO_DOM 1016 1064 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1086 1090 Extracellular. {ECO:0000305}. FUNCTION: Calcium-independent receptor of low affinity for alpha-latrotoxin, an excitatory neurotoxin present in black widow spider venom which triggers massive exocytosis from neurons and neuroendocrine cells. Receptor probably implicated in the regulation of exocytosis. {ECO:0000250|UniProtKB:O88923, ECO:0000269|PubMed:24273166}. PTM: Proteolytically cleaved into 2 subunits, an extracellular subunit and a seven-transmembrane subunit. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Forms a heterodimer, consisting of a large extracellular region non-covalently linked to a seven-transmembrane moiety. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:24273166}. +Q9JHW9 AL1A3_MOUSE Aldehyde dehydrogenase family 1 member A3 (EC 1.2.1.5) (Aldehyde dehydrogenase 6) (Retinaldehyde dehydrogenase 3) (RALDH-3) (RalDH3) 512 56,157 Active site (2); Binding site (4); Chain (1); Initiator methionine (1); Modified residue (1); Nucleotide binding (1); Sequence conflict (5); Site (1) Cofactor metabolism; retinol metabolism. FUNCTION: NAD-dependent aldehyde dehydrogenase that catalyzes the formation of retinoic acid (PubMed:11044606, PubMed:11013254, PubMed:14623956). Has high activity with all-trans retinal, and has much lower in vitro activity with acetaldehyde (By similarity). Required for the biosynthesis of normal levels of retinoic acid in the embryonic ocular and nasal regions; retinoic acid is required for normal embryonic development of the eye and the nasal region (PubMed:14623956). {ECO:0000250|UniProtKB:P47895, ECO:0000269|PubMed:11013254, ECO:0000269|PubMed:11044606, ECO:0000269|PubMed:14623956}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11013254}. SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P47895}. TISSUE SPECIFICITY: Detected in embryonic head (at protein level) (PubMed:14623956). Ventral retina. {ECO:0000269|PubMed:10906479, ECO:0000269|PubMed:11013254, ECO:0000269|PubMed:11025231, ECO:0000269|PubMed:11044606, ECO:0000269|PubMed:14623956}. +Q8K4E0 ALMS1_MOUSE Alstrom syndrome protein 1 homolog 3251 360,215 Alternative sequence (1); Chain (1); Compositional bias (3); Erroneous initiation (1); Modified residue (6); Region (2); Repeat (17); Sequence conflict (6) FUNCTION: Involved in PCM1-dependent intracellular transport. Required, directly or indirectly, for the localization of NCAPD2 to the proximal ends of centrioles. Required for proper formation and/or maintenance of primary cilia (PC), microtubule-based structures that protrude from the surface of epithelial cells (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. Note=Associated with centrosomes and basal bodies at the base of primary cilia. Specifically locates to the proximal ends of centrioles and basal bodies. Colocalizes partially with NCAPD2 at these sites. During mitosis localizes to both spindle poles (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:11941369}. +Q9JI76 ADA21_MOUSE Disintegrin and metalloproteinase domain-containing protein 21 (ADAM 21) (EC 3.4.24.-) (Disintegrin and metalloproteinase domain-containing protein 31) (ADAM 31) 729 80,850 Active site (1); Chain (1); Compositional bias (1); Disulfide bond (7); Domain (3); Glycosylation (5); Metal binding (4); Motif (1); Propeptide (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 686 706 Helical. {ECO:0000255}. TOPO_DOM 210 685 Extracellular. {ECO:0000255}.; TOPO_DOM 707 729 Cytoplasmic. {ECO:0000255}. FUNCTION: May be involved in sperm maturation and/or fertilization. May also be involved in epithelia functions associated with establishing and maintaining gradients of ions or nutrients. PTM: Has no obvious cleavage site for furin endopeptidase, suggesting that the proteolytic processing is regulated. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. DOMAIN: A tripeptide motif (VGE) within disintegrin-like domain could be involved in the binding to egg integrin receptor and thus could mediate sperm/egg binding.; DOMAIN: The cysteine-rich domain encodes putative cell-fusion peptides, which could be involved in sperm-egg fusion.; DOMAIN: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme. TISSUE SPECIFICITY: Highly expressed in Leydig cells. Expressed also in cauda epididymidis, vas deferens, convoluted tubules, kidney and the parietal cells of stomach. Not detected on developing spermatocytes or mature sperm. +Q9CQF6 ADPPT_MOUSE L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase (EC 2.7.8.7) (4'-phosphopantetheinyl transferase) (Alpha-aminoadipic semialdehyde dehydrogenase-phosphopantetheinyl transferase) (AASD-PPT) 309 35,764 Alternative sequence (1); Binding site (1); Chain (1); Metal binding (2); Region (3); Sequence conflict (2) FUNCTION: Catalyzes the post-translational modification of target proteins by phosphopantetheine. Can transfer the 4'-phosphopantetheine moiety from coenzyme A to a serine residue of a broad range of acceptors, such as the acyl carrier domain of FASN (in vitro) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Monomer. Interacts with FASN (By similarity). {ECO:0000250}. +Q6PAL7 AHDC1_MOUSE AT-hook DNA-binding motif-containing protein 1 1594 168,081 Chain (1); Compositional bias (2); Cross-link (2); DNA binding (2); Erroneous initiation (1); Modified residue (16); Sequence conflict (1) +A2AJA9 AJM1_MOUSE Apical junction component 1 homolog 974 107,186 Alternative sequence (1); Chain (1); Compositional bias (1); Modified residue (9) FUNCTION: May be involved in the control of adherens junction integrity. {ECO:0000250|UniProtKB:A0A1C3NSL9}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:A0A1C3NSL9}. Cell projection, cilium {ECO:0000250|UniProtKB:A0A1C3NSL9}. Cell junction, adherens junction {ECO:0000250|UniProtKB:A0A1C3NSL9}. +Q9JII6 AK1A1_MOUSE Alcohol dehydrogenase [NADP(+)] (EC 1.1.1.2) (Aldehyde reductase) (Aldo-keto reductase family 1 member A1) 325 36,587 Active site (1); Beta strand (14); Binding site (1); Chain (1); Helix (15); Initiator methionine (1); Modified residue (7); Nucleotide binding (2); Sequence conflict (6); Site (1) FUNCTION: Catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols. Catalyzes the reduction of mevaldate to mevalonic acid and of glyceraldehyde to glycerol. Has broad substrate specificity. Plays a role in the activation of procarcinogens, such as polycyclic aromatic hydrocarbon trans-dihydrodiols, and in the metabolism of various xenobiotics and drugs (By similarity). {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10842086}. +J3QMK6 AL3B3_MOUSE Aldehyde dehydrogenase family 3 member B3 (EC 1.2.1.3) 479 53,120 Active site (2); Chain (1); Lipidation (1); Mutagenesis (1); Propeptide (1); Sequence caution (1) FUNCTION: Oxidizes medium and long chain aldehydes into non-toxic fatty acids. {ECO:0000269|PubMed:25286108}. PTM: Geranylgeranylation is important for membrane localization and enzyme activity. {ECO:0000269|PubMed:25286108}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25286108}; Lipid-anchor {ECO:0000305|PubMed:25286108}. TISSUE SPECIFICITY: Expressed in testis, kidney, small intestine, spleen, white adipose tissue, liver and lung. {ECO:0000269|PubMed:25286108}. +P05063 ALDOC_MOUSE Fructose-bisphosphate aldolase C (EC 4.1.2.13) (Aldolase 3) (Brain-type aldolase) (Scrapie-responsive protein 2) (Zebrin II) 363 39,395 Active site (2); Binding site (2); Chain (1); Initiator methionine (1); Modified residue (5); Sequence conflict (10); Site (1) Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. SUBUNIT: Homotetramer. Interacts with ATP6V1E1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed exclusively in Purkinje cells in bands running from anterior to posterior across most of the cerebellum. Expressed at higher levels in the brains of BSE-infected animals. {ECO:0000269|PubMed:10719228, ECO:0000269|PubMed:7925012}. +Q6R0H6 ALEX_MOUSE Protein ALEX (Alternative gene product encoded by XL-exon) 725 79,084 Chain (1); Compositional bias (1); Erroneous initiation (1); Sequence conflict (1) FUNCTION: May inhibit the adenylyl cyclase-stimulating activity of guanine nucleotide-binding protein G(s) subunit alpha which is produced from the same locus in a different open reading frame. {ECO:0000250|UniProtKB:P84996}. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. Cell projection, ruffle {ECO:0000250}. Note=Predominantly associated with cell membrane ruffles. {ECO:0000250}. SUBUNIT: Interacts with the N-terminal region of the XLas isoforms of guanine nucleotide-binding protein G(s) subunit alpha. {ECO:0000250}. +Q9JJW6 ALRF2_MOUSE Aly/REF export factor 2 (Alyref) (RNA and export factor-binding protein 2) 218 23,730 Alternative sequence (1); Beta strand (11); Chain (1); Domain (1); Helix (4); Modified residue (16); Mutagenesis (4); Region (2); Sequence conflict (3); Turn (2) FUNCTION: Export adapter involved in spliced and unspliced mRNA nuclear export. Binds mRNA which is transferred to the NXF1-NXT1 heterodimer for export (TAP/NFX1 pathway); enhances NXF1-NXT1 RNA-binding activity. {ECO:0000269|PubMed:10786854, ECO:0000269|PubMed:11158589, ECO:0000269|PubMed:18364396}. PTM: Arginine methylation reduces RNA binding and enhances mRNA transfer to the NXF1-NXT1 heterodimer for nuclear export. {ECO:0000269|PubMed:20129943}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q86V81}. Cytoplasm {ECO:0000250|UniProtKB:Q86V81}. SUBUNIT: Interacts (via N-terminus and RRM domain) with DDX39B and th NXF1-NXT1 heterodimer. Interacts with HHV-1 ICP27 and HVS ORF57 proteins. {ECO:0000269|PubMed:10786854, ECO:0000269|PubMed:17000901, ECO:0000269|PubMed:18364396, ECO:0000269|PubMed:21253573, ECO:0000269|PubMed:24550725}. DOMAIN: The RRM domain and the N-terminal region (15-58) seem to be involved in RNA binding. {ECO:0000269|PubMed:17000901}. +Q923W9 ADA33_MOUSE Disintegrin and metalloproteinase domain-containing protein 33 (ADAM 33) (EC 3.4.24.-) 797 86,971 Active site (1); Alternative sequence (1); Chain (1); Compositional bias (2); Disulfide bond (7); Domain (3); Glycosylation (6); Metal binding (4); Motif (1); Propeptide (1); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 703 723 Helical. {ECO:0000255}. TOPO_DOM 30 702 Extracellular. {ECO:0000255}.; TOPO_DOM 724 797 Cytoplasmic. {ECO:0000255}. PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. DOMAIN: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme. +P54923 ADPRH_MOUSE [Protein ADP-ribosylarginine] hydrolase (ADP-ribosylarginine hydrolase) (EC 3.2.2.19) (ADP-ribose-L-arginine cleaving enzyme) 362 40,068 Binding site (3); Chain (1); Metal binding (8); Nucleotide binding (4) FUNCTION: Catalyzes the reverse reaction of mono-ADP-ribosylation. SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P54922}. +P63002 AES_MOUSE Amino-terminal enhancer of split (Amino enhancer of split) (Grg-5) (Groucho-related protein 5) (Protein ESP1) (Protein GRG) 197 22,000 Alternative sequence (1); Chain (1); Compositional bias (2); Erroneous initiation (1); Modified residue (1); Region (1) FUNCTION: Transcriptional corepressor. Acts as dominant repressor towards other family members. Inhibits NF-kappa-B-regulated gene expression. May be required for the initiation and maintenance of the differentiated state. Essential for the transcriptional repressor activity of SIX3 during retina and lens development. {ECO:0000269|PubMed:12050133}. PTM: Ubiquitinated by XIAP/BIRC4. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12050133}. SUBUNIT: Homooligomer and heterooligomer with other family members. Binds TCF7 and the NF-kappa-B subunit RELA. Interacts with PHF12 (By similarity). Interacts (via Q domain) with SIX3. Interacts with SIX6. {ECO:0000250, ECO:0000269|PubMed:11266540, ECO:0000269|PubMed:12050133, ECO:0000269|PubMed:9783587}. DOMAIN: Lacks the C-terminal WD repeats. TISSUE SPECIFICITY: Ubiquitously expressed in developing embryos by midgestation, a wide expression is conserved in adult. In mouse, abundantly expressed in muscle, heart and brain. {ECO:0000269|PubMed:8369224}. +Q9R160 ADA24_MOUSE Disintegrin and metalloproteinase domain-containing protein 24 (ADAM 24) (EC 3.4.24.-) (Testase-1) 761 85,054 Active site (1); Chain (1); Compositional bias (1); Disulfide bond (7); Domain (3); Glycosylation (6); Metal binding (4); Motif (1); Propeptide (1); Sequence conflict (12); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 698 718 Helical. {ECO:0000255}. TOPO_DOM 35 697 Extracellular. {ECO:0000255}.; TOPO_DOM 719 761 Cytoplasmic. {ECO:0000255}. FUNCTION: Plasma membrane protease present on mature sperm that may be involved in sperm function during epididymal maturation and/or fertilization. PTM: The prodomain is removed during sperm passage through the caput epididymis after the protein has reached the cell surface. Not processed in the secretory pathway. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Monomer. DOMAIN: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme. TISSUE SPECIFICITY: Expressed exclusively in testis and more specifically on the surface of mature sperm. Localized to the equatorial region of the plasma membrane of cauda epididymal sperm. +Q8CJG1 AGO1_MOUSE Protein argonaute-1 (Argonaute1) (mAgo1) (Argonaute RISC catalytic component 1) (Eukaryotic translation initiation factor 2C 1) (eIF-2C 1) (eIF2C 1) (Piwi/argonaute family protein meIF2C1) 857 97,214 Chain (1); Domain (2); Region (6); Sequence conflict (4) FUNCTION: Required for RNA-mediated gene silencing (RNAi). Binds to short RNAs such as microRNAs (miRNAs) or short interfering RNAs (siRNAs), and represses the translation of mRNAs which are complementary to them. Lacks endonuclease activity and does not appear to cleave target mRNAs. May also be required for transcriptional gene silencing (TGS) of promoter regions which are complementary to bound short antigene RNAs (agRNAs). {ECO:0000269|PubMed:19174539}. SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000250}. SUBUNIT: Interacts with DDB1, DDX5, DDX6, DHX30, DHX36, DDX47, DICER1, AGO2, ELAVL1, HNRNPF, IGF2BP1, ILF3, IMP8, MATR3, MOV10, PABPC1, PRMT5, RBM4, SART3, TNRC6B, UPF1 and YBX1. Associates with polysomes and messenger ribonucleoproteins (mNRPs) (By similarity). Interacts with LIMD1, WTIP and AJUBA (By similarity). Interacts with APOBEC3F, APOBEC3G and APOBEC3H (By similarity). {ECO:0000250}. +Q8VEC3 AGRF1_MOUSE Adhesion G-protein coupled receptor F1 (G protein-coupled receptor 110) 908 101,469 Chain (1); Domain (2); Frameshift (1); Glycosylation (13); Sequence conflict (3); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 589 609 Helical; Name=1. {ECO:0000255}.; TRANSMEM 623 643 Helical; Name=2. {ECO:0000255}.; TRANSMEM 659 679 Helical; Name=3. {ECO:0000255}.; TRANSMEM 698 718 Helical; Name=4. {ECO:0000255}.; TRANSMEM 743 763 Helical; Name=5. {ECO:0000255}.; TRANSMEM 790 810 Helical; Name=6. {ECO:0000255}.; TRANSMEM 819 839 Helical; Name=7. {ECO:0000255}. TOPO_DOM 21 588 Extracellular. {ECO:0000305}.; TOPO_DOM 610 622 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 644 658 Extracellular. {ECO:0000305}.; TOPO_DOM 680 697 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 719 742 Extracellular. {ECO:0000305}.; TOPO_DOM 764 789 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 811 818 Extracellular. {ECO:0000305}.; TOPO_DOM 840 908 Cytoplasmic. {ECO:0000305}. FUNCTION: Orphan receptor. PTM: Glycosylated. {ECO:0000250|UniProtKB:Q5T601}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q5T601}; Multi-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Expressed in liver, kidney and adrenal gland. In kidney strong expression in the renal pelvis and the ureter. {ECO:0000269|PubMed:22837050}. +Q80ZF8 AGRB3_MOUSE Adhesion G protein-coupled receptor B3 (Brain-specific angiogenesis inhibitor 3) 1522 171,314 Chain (1); Disulfide bond (16); Domain (6); Glycosylation (13); Modified residue (3); Sequence conflict (3); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 881 901 Helical; Name=1. {ECO:0000255}.; TRANSMEM 911 931 Helical; Name=2. {ECO:0000255}.; TRANSMEM 940 960 Helical; Name=3. {ECO:0000255}.; TRANSMEM 982 1002 Helical; Name=4. {ECO:0000255}.; TRANSMEM 1024 1044 Helical; Name=5. {ECO:0000255}.; TRANSMEM 1099 1119 Helical; Name=6. {ECO:0000255}.; TRANSMEM 1126 1146 Helical; Name=7. {ECO:0000255}. TOPO_DOM 26 880 Extracellular. {ECO:0000305}.; TOPO_DOM 902 910 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 932 939 Extracellular. {ECO:0000305}.; TOPO_DOM 961 981 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1003 1023 Extracellular. {ECO:0000305}.; TOPO_DOM 1045 1098 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1120 1125 Extracellular. {ECO:0000305}.; TOPO_DOM 1147 1522 Cytoplasmic. {ECO:0000305}. FUNCTION: Receptor that plays a role in the regulation of synaptogenesis and dendritic spine formation at least partly via interaction with ELMO1 and RAC1 activity (PubMed:23628982). Promotes myoblast fusion through ELMO/DOCK1 (By similarity). {ECO:0000250|UniProtKB:O60242, ECO:0000269|PubMed:23628982}. PTM: The endogenous protein is proteolytically cleaved into 2 subunits, an extracellular subunit and a seven-transmembrane subunit. {ECO:0000250|UniProtKB:O60242}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O60242}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Forms a heterodimer, consisting of a large extracellular region non-covalently linked to a seven-transmembrane moiety. Interacts (via its TSRs) with C1QL1, C1QL2, C1QL3 and C1QL4. Interacts via (C-terminus) with ELMO1 (PubMed:23628982), ELMO2 and ELMO3. {ECO:0000250|UniProtKB:O60242, ECO:0000269|PubMed:23628982}. TISSUE SPECIFICITY: Brain-specific expression. {ECO:0000269|PubMed:15225653}. +E9Q4J9 AGRF2_MOUSE Adhesion G-protein coupled receptor F2 (G-protein coupled receptor 111) (G-protein coupled receptor PGR20) 644 71,764 Chain (1); Domain (1); Glycosylation (4); Sequence conflict (1); Signal peptide (1); Topological domain (7); Transmembrane (7) TRANSMEM 387 407 Helical; Name=1. {ECO:0000255}.; TRANSMEM 423 443 Helical; Name=2. {ECO:0000255}.; TRANSMEM 466 486 Helical; Name=3. {ECO:0000255}.; TRANSMEM 494 514 Helical; Name=4. {ECO:0000255}.; TRANSMEM 542 562 Helical; Name=5. {ECO:0000255}.; TRANSMEM 586 606 Helical; Name=6. {ECO:0000255}.; TRANSMEM 611 631 Helical; Name=7. {ECO:0000255}. TOPO_DOM 19 386 Extracellular. {ECO:0000305}.; TOPO_DOM 408 422 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 444 465 Extracellular. {ECO:0000305}.; TOPO_DOM 487 493 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 515 541 Extracellular. {ECO:0000305}.; TOPO_DOM 563 585 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 607 610 Extracellular. {ECO:0000305}. FUNCTION: Orphan receptor. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Mainly expressed in skin and heart, and very weakly in lung and spleen. Detected in all epidermal layers of skin. {ECO:0000269|PubMed:22837050}. +O88312 AGR2_MOUSE Anterior gradient protein 2 homolog (AG-2) (mAG-2) (Protein Gob-4) (Secreted cement gland protein XAG-2 homolog) 175 19,920 Chain (1); Motif (2); Region (1); Signal peptide (1) FUNCTION: Required for MUC2 post-transcriptional synthesis and secretion. May play a role in the production of mucus by intestinal cells. Proto-oncogene that may play a role in cell migration, cell differentiation and cell growth (By similarity). Promotes cell adhesion (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O95994, ECO:0000269|PubMed:19359471}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Endoplasmic reticulum {ECO:0000269|PubMed:19359471}. SUBUNIT: Monomer and homodimer. Interacts with LYPD3 and DAG1 (alphaDAG1). Interacts with MUC2; disulfide-linked. {ECO:0000250|UniProtKB:O95994}. TISSUE SPECIFICITY: Expressed in lung, skeletal muscle, testis, liver, stomach, colon, small intestine, the goblet cells of the intestine and the mucuous neck cells of the stomach. {ECO:0000269|PubMed:10095068, ECO:0000269|PubMed:9790916}. +D3YVF0 AKAP5_MOUSE A-kinase anchor protein 5 (AKAP-5) (A-kinase anchor protein 150 kDa) (AKAP 150) (P150) (cAMP-dependent protein kinase regulatory subunit II high affinity-binding protein) 745 79,397 Chain (1); Compositional bias (1); Domain (1); Lipidation (2); Modified residue (2); Region (3); Repeat (28) FUNCTION: May anchor the PKA kinase to cytoskeletal and/or organelle-associated proteins, targeting the signal carried by cAMP to specific intracellular effectors. {ECO:0000250}. PTM: Palmitoylation at Cys-36 and Cys-123 plays a key role in targeting to lipid rafts. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Note=Associates with lipid rafts. {ECO:0000250}. SUBUNIT: Interacts with ADCY8, and enhances its phosphorylation at lipid rafts. Binds dimer of the RII-beta regulatory subunit of cAMP-dependent protein kinase (By similarity). {ECO:0000250}. DOMAIN: The N-terminal region, which is highly basic, is required for interaction with calmodulin. {ECO:0000250}. +Q8K209 AGRG1_MOUSE Adhesion G-protein coupled receptor G1 (G-protein coupled receptor 56) (Serpentine receptor cyt28) [Cleaved into: ADGRG1 N-terminal fragment (ADGRG1 NT) (GPR56 N-terminal fragment) (GPR56 NT) (GPR56(N)) (GPR56 extracellular subunit) (GPR56 subunit alpha); ADGRG1 C-terminal fragment (ADGRG1-CT) (GPR56 C-terminal fragment) (GPR56 CT) (GPR56(C)) (GPR56 seven-transmembrane subunit) (GPR56 7TM) (GPR56 subunit beta)] 687 77,255 Beta strand (24); Chain (3); Domain (1); Glycosylation (7); Helix (6); Mutagenesis (5); Region (2); Sequence conflict (1); Signal peptide (1); Site (1); Topological domain (8); Transmembrane (7); Turn (2) TRANSMEM 403 423 Helical; Name=1. {ECO:0000255}.; TRANSMEM 443 463 Helical; Name=2. {ECO:0000255}.; TRANSMEM 472 492 Helical; Name=3. {ECO:0000255}.; TRANSMEM 513 533 Helical; Name=4. {ECO:0000255}.; TRANSMEM 571 591 Helical; Name=5. {ECO:0000255}.; TRANSMEM 604 624 Helical; Name=6. {ECO:0000255}.; TRANSMEM 631 651 Helical; Name=7. {ECO:0000255}. TOPO_DOM 26 402 Extracellular. {ECO:0000255}.; TOPO_DOM 424 442 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 464 471 Extracellular. {ECO:0000255}.; TOPO_DOM 493 512 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 534 570 Extracellular. {ECO:0000255}.; TOPO_DOM 592 603 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 625 630 Extracellular. {ECO:0000255}.; TOPO_DOM 652 687 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor involved in cell adhesion and probably in cell-cell interactions. Mediates cell matrix adhesion in developing neurons and hematopoietic stem cells. Receptor for collagen III/COL3A1 in the developing brain and involved in regulation of cortical development, specifically in maintenance of the pial basement membrane integrity and in cortical lamination (PubMed:21768377). Binding to the COL3A1 ligand inhibits neuronal migration and activates the RhoA pathway by coupling to GNA13 and possibly GNA12 (By similarity). Plays a role in the maintenance of hematopoietic stem cells and/or leukemia stem cells in bone marrow niche (PubMed:23478665). Plays a critical role in tumourigenesis (By similarity). Plays essential role in testis development (PubMed:20981830). {ECO:0000250|UniProtKB:Q9Y653, ECO:0000269|PubMed:18378689, ECO:0000269|PubMed:18509043, ECO:0000269|PubMed:19515912, ECO:0000269|PubMed:20981830, ECO:0000269|PubMed:21768377, ECO:0000269|PubMed:23478665, ECO:0000269|PubMed:24531968}. PTM: Autoproteolytically cleaved into 2 fragments; the large extracellular N-terminal fragment and the membroune-bound C-terminal fragment predominantly remain associated and non-covalently linked. {ECO:0000269|PubMed:22238662}.; PTM: N-glycosylated. The secreted ADGRG1 N-terminal fragment is heavily glycosylated. {ECO:0000269|PubMed:17576745}.; PTM: Ubiquitinated. Undergoes polyubiquitination upon activation. {ECO:0000250|UniProtKB:Q9Y653}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17576745, ECO:0000269|PubMed:22238662}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: ADGRG1 N-terminal fragment: Secreted {ECO:0000250|UniProtKB:Q9Y653}.; SUBCELLULAR LOCATION: ADGRG1 C-terminal fragment: Membrane raft {ECO:0000250|UniProtKB:Q9Y653}. Note=Interaction with its ligand COL3A1 leads to the release of ADGRG1 NT from the membrane and triggers the association of ADGRG1 CT with lipid rafts. {ECO:0000250|UniProtKB:Q9Y653}. SUBUNIT: Predominantly non-covalently linked heterodimer of the N-terminal and the C-terminal fragment. ADGRG1 NT self-associates in a trans-trans manner; the homophilic interaction enhances receptor signaling. ADGRG1 CT interacts with ARRB2; the interaction is impaired by ADGRG1 NT. Part of a GPCR-tetraspanin complex at least consisting of ADGRG1, CD81, eventually CD9, and GNA11 in which CD81 is enhancing the association of ADGRG1 with GNA11 (By similarity). Interacts with heparin; leading to the reduction of ADGRG1 shedding (PubMed:27068534). {ECO:0000250|UniProtKB:Q9Y653, ECO:0000269|PubMed:27068534}. TISSUE SPECIFICITY: Expressed in neural progenitor cells in fetal forbrain. Expressed in migrating neurons. Expressed in radial glial endfeet (at protein level) (PubMed:21768377). Expressed in peritubular myoid cells, Sertoli cells, and germ cells of the testis (PubMed:20981830). {ECO:0000269|PubMed:20981830, ECO:0000269|PubMed:21768377}. +Q9WVE0 AICDA_MOUSE Single-stranded DNA cytosine deaminase (EC 3.5.4.38) (Activation-induced cytidine deaminase) (AID) (Cytidine aminohydrolase) 198 24,031 Active site (1); Chain (1); Domain (1); Metal binding (3); Modified residue (2); Motif (2); Mutagenesis (3); Region (3) FUNCTION: Single-stranded DNA-specific cytidine deaminase. Involved in somatic hypermutation (SHM), gene conversion, and class-switch recombination (CSR) in B-lymphocytes by deaminating C to U during transcription of Ig-variable (V) and Ig-switch (S) region DNA. Required for several crucial steps of B-cell terminal differentiation necessary for efficient antibody responses. May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation. {ECO:0000269|PubMed:12692563, ECO:0000269|PubMed:23803409}. PTM: Ser-38 is the major site whereas Thr-27 is the minor site of phosphorylation. Phosphorylation regulates its class-switch recombination activity (By similarity). {ECO:0000250}.; PTM: Probably monoubiquitinated on several residues by RNF126. {ECO:0000250|UniProtKB:Q9GZX7}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9GZX7}. Cytoplasm {ECO:0000269|PubMed:23803409}. Note=Predominantly cytoplasmic but shuttles between the nucleus and the cytoplasm. {ECO:0000250|UniProtKB:Q9GZX7}. SUBUNIT: Interacts with CTNNBL1; the interaction is important for the immunoglobulin switch activity of AICDA. Interacts (via its NLS) with KPNA1. Interacts with PKA/PRKACA and PRKAR1A/PKR1 (By similarity). Interacts with SUPT6H, TRIM28 and NCL. {ECO:0000250|UniProtKB:Q9GZX7, ECO:0000269|PubMed:21518874}. +P29755 AGTRB_MOUSE Type-1B angiotensin II receptor (AT3) (Angiotensin II type-1B receptor) (AT1B) 359 40,950 Chain (1); Disulfide bond (1); Glycosylation (3); Lipidation (1); Sequence conflict (6); Topological domain (8); Transmembrane (7) TRANSMEM 28 52 Helical; Name=1. {ECO:0000255}.; TRANSMEM 65 87 Helical; Name=2. {ECO:0000255}.; TRANSMEM 103 124 Helical; Name=3. {ECO:0000255}.; TRANSMEM 143 162 Helical; Name=4. {ECO:0000255}.; TRANSMEM 193 214 Helical; Name=5. {ECO:0000255}.; TRANSMEM 241 262 Helical; Name=6. {ECO:0000255}.; TRANSMEM 276 296 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 27 Extracellular. {ECO:0000255}.; TOPO_DOM 53 64 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 88 102 Extracellular. {ECO:0000255}.; TOPO_DOM 125 142 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 163 192 Extracellular. {ECO:0000255}.; TOPO_DOM 215 240 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 263 275 Extracellular. {ECO:0000255}.; TOPO_DOM 297 359 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for angiotensin II. Mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. PTM: C-terminal Ser or Thr residues may be phosphorylated. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBUNIT: Interacts with MAS1. {ECO:0000250}. +P45377 ALD2_MOUSE Aldose reductase-related protein 2 (AR) (EC 1.1.1.21) (Aldehyde reductase) (Fibroblast growth factor-regulated protein) (Protein FR-1) 316 36,121 Active site (1); Beta strand (8); Binding site (1); Chain (1); Helix (14); Nucleotide binding (1); Sequence conflict (1); Site (1); Turn (2) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. +Q8BK64 AHSA1_MOUSE Activator of 90 kDa heat shock protein ATPase homolog 1 (AHA1) 338 38,117 Chain (1); Cross-link (2); Modified residue (4); Sequence conflict (1) FUNCTION: Acts as a co-chaperone of HSP90AA1 (PubMed:29127155). Activates the ATPase activity of HSP90AA1 leading to increase in its chaperone activity (PubMed:29127155). Competes with the inhibitory co-chaperone FNIP1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins (By similarity). Competes with the inhibitory co-chaperone TSC1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins (PubMed:29127155). {ECO:0000250|UniProtKB:O95433, ECO:0000269|PubMed:29127155}. PTM: Phosphorylation at Tyr-223 enhances binding to chaperone HSP90AA1. {ECO:0000305|PubMed:29127155}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:O95433}. Endoplasmic reticulum {ECO:0000250|UniProtKB:O95433}. Note=May transiently interact with the endoplasmic reticulum. {ECO:0000250|UniProtKB:O95433}. SUBUNIT: Interacts with HSPCA/HSP90 (By similarity). Interacts with HSP90AA1; the interaction activates HSP90AA1 ATPase activity (PubMed:29127155). Interacts with HSP90AB1 (PubMed:22022502). Interacts with GCH1 (By similarity). Interacts with SRPK1 (By similarity). Interacts with FLCN (By similarity). {ECO:0000250|UniProtKB:O95433, ECO:0000269|PubMed:22022502, ECO:0000269|PubMed:29127155}. +Q60I26 AL2CL_MOUSE ALS2 C-terminal-like protein 952 108,146 Alternative sequence (2); Chain (1); Domain (1); Erroneous initiation (1); Repeat (8); Sequence caution (1); Sequence conflict (14) FUNCTION: Acts as a guanine nucleotide exchange factor (GEF) for Rab5 GTPase. Regulates the ALS2-mediated endosome dynamics (By similarity). {ECO:0000250, ECO:0000269|PubMed:16473597}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15388334, ECO:0000269|PubMed:17239822}. Note=Distributed onto the vesicular compartments in the cytoplasm with strong punctated staining. Colocalizes with RAB5A onto the vesicular/membranous compartments in the cytoplasm, particularly to the leading edges of the cells (By similarity). {ECO:0000250}. SUBUNIT: Homodimer. Forms a heteromeric complex with ALS2. Interacts with ALS2 and RAB5A. {ECO:0000269|PubMed:15388334, ECO:0000269|PubMed:17239822}. TISSUE SPECIFICITY: Expressed in heart, lung, liver and kidney. {ECO:0000269|PubMed:15388334}. +Q9WTQ5 AKA12_MOUSE A-kinase anchor protein 12 (AKAP-12) (Germ cell lineage protein gercelin) (Src-suppressed C kinase substrate) (SSeCKS) 1684 180,695 Alternative sequence (1); Chain (1); Cross-link (1); Domain (3); Frameshift (1); Initiator methionine (1); Lipidation (1); Modified residue (44); Region (2) FUNCTION: Anchoring protein that mediates the subcellular compartmentation of protein kinase A (PKA) and protein kinase C (PKC). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Membrane {ECO:0000250|UniProtKB:Q02952}; Lipid-anchor {ECO:0000250|UniProtKB:Q02952}. SUBUNIT: Binds to dimeric RII-alpha regulatory subunit of PKC. {ECO:0000250}. TISSUE SPECIFICITY: Isoform 1 is predominantly found in the nervous system. Isoform 3 is testis specific. {ECO:0000269|PubMed:11429284}. +P21300 ALD1_MOUSE Aldose reductase-related protein 1 (EC 1.1.1.21) (Aldehyde reductase) (AR) (Aldo-keto reductase family 1 member B7) (MVDP) (Vas deferens androgen-dependent protein) 316 35,988 Active site (1); Binding site (4); Chain (1); Nucleotide binding (4); Sequence conflict (1); Site (1) FUNCTION: Reduces a broad range of aliphatic and aromatic aldehydes to the corresponding alcohols. May play a role in the metabolism of xenobiotic aromatic aldehydes (By similarity). The role of MVDP in sperm maturation and storage may be related to its potential capacity to produce fructose, or MVDP may play an osmoregulatory role by producing sorbitol. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. +Q8VDB2 ALG12_MOUSE Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase (EC 2.4.1.260) (Asparagine-linked glycosylation protein 12 homolog) (Dolichyl-P-Man:Man(7)GlcNAc(2)-PP-dolichyl-alpha-1,6-mannosyltransferase) (Mannosyltransferase ALG12 homolog) 486 54,543 Chain (1); Sequence conflict (2); Transmembrane (11) TRANSMEM 12 32 Helical. {ECO:0000255}.; TRANSMEM 69 89 Helical. {ECO:0000255}.; TRANSMEM 94 114 Helical. {ECO:0000255}.; TRANSMEM 123 143 Helical. {ECO:0000255}.; TRANSMEM 146 166 Helical. {ECO:0000255}.; TRANSMEM 178 198 Helical. {ECO:0000255}.; TRANSMEM 213 233 Helical. {ECO:0000255}.; TRANSMEM 265 285 Helical. {ECO:0000255}.; TRANSMEM 291 311 Helical. {ECO:0000255}.; TRANSMEM 313 333 Helical. {ECO:0000255}.; TRANSMEM 344 364 Helical. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Adds the eighth mannose residue in an alpha-1,6 linkage onto the dolichol-PP-oligosaccharide precursor (dolichol-PP-Man(7)GlcNAc(2)) required for protein glycosylation. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q8CHT0 AL4A1_MOUSE Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial (P5C dehydrogenase) (EC 1.2.1.88) (Aldehyde dehydrogenase family 4 member A1) (L-glutamate gamma-semialdehyde dehydrogenase) 562 61,841 Active site (2); Beta strand (19); Binding site (4); Chain (1); Helix (22); Modified residue (25); Nucleotide binding (1); Sequence conflict (18); Site (1); Transit peptide (1); Turn (6) Amino-acid degradation; L-proline degradation into L-glutamate; L-glutamate from L-proline: step 2/2. FUNCTION: Irreversible conversion of delta-1-pyrroline-5-carboxylate (P5C), derived either from proline or ornithine, to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes (By similarity). {ECO:0000250}. PTM: Acetylation of Lys-98, Lys-113 and Lys-401 is observed in liver mitochondria from fasted mice but not from fed mice. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000269|PubMed:22516612}. +Q9QYC0 ADDA_MOUSE Alpha-adducin (Erythrocyte adducin subunit alpha) 735 80,647 Alternative sequence (2); Chain (1); Modified residue (37); Region (1); Sequence conflict (1) FUNCTION: Membrane-cytoskeleton-associated protein that promotes the assembly of the spectrin-actin network. Binds to calmodulin. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell membrane; Peripheral membrane protein; Cytoplasmic side. SUBUNIT: Heterodimer of an alpha and a beta subunit or an alpha and a gamma subunit. DOMAIN: Each subunit is comprised of three regions: a NH2-terminal protease-resistant globular head region, a short connecting subdomain, and a protease-sensitive tail region. +Q9CZI9 AEN_MOUSE Apoptosis-enhancing nuclease (EC 3.1.-.-) (Interferon-stimulated 20 kDa exonuclease-like 1) 336 37,309 Alternative sequence (1); Chain (1); Domain (1); Erroneous initiation (1); Motif (2); Sequence conflict (2) FUNCTION: Exonuclease with activity against single- and double-stranded DNA and RNA. Mediates p53-induced apoptosis. When induced by p53 following DNA damage, digests double-stranded DNA to form single-stranded DNA and amplifies DNA damage signals, leading to enhancement of apoptosis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Note=Localized predomintly in the nucleolus. Translocates from the nucleolus to the nucleoplasm upon apoptosis induction (By similarity). {ECO:0000250}. +P46656 ADX_MOUSE Adrenodoxin, mitochondrial (Adrenal ferredoxin) (Ferredoxin-1) 188 20,123 Chain (1); Domain (1); Metal binding (4); Modified residue (5); Transit peptide (1) FUNCTION: Essential for the synthesis of various steroid hormones, participates in the reduction of mitochondrial cytochrome P450 for steroidogenesis. Transfers electrons from adrenodoxin reductase to CYP11A1, a cytochrome P450 that catalyzes cholesterol side-chain cleavage. Does not form a ternary complex with adrenodoxin reductase and CYP11A1 but shuttles between the two enzymes to transfer electrons. {ECO:0000250|UniProtKB:P00257}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:P10109}. SUBUNIT: Interacts with CYP11A1. {ECO:0000250|UniProtKB:P10109}. +Q8C0T9 ADCYA_MOUSE Adenylate cyclase type 10 (EC 4.6.1.1) (Germ cell soluble adenylyl cyclase) (sAC) (Testicular soluble adenylyl cyclase) 1614 186,412 Alternative sequence (2); Binding site (7); Chain (1); Compositional bias (1); Domain (2); Metal binding (5); Nucleotide binding (2); Sequence conflict (2) FUNCTION: Catalyzes the formation of the signaling molecule cAMP. May function as sensor that mediates responses to changes in cellular bicarbonate and CO(2) levels (By similarity). Has a critical role in mammalian spermatogenesis by producing the cAMP which regulates cAMP-responsive nuclear factors indispensable for sperm maturation in the epididymis. Induces capacitation, the maturational process that sperm undergo prior to fertilization (PubMed:14976244, PubMed:16054031). Involved in ciliary beat regulation (By similarity). {ECO:0000250|UniProtKB:Q96PN6, ECO:0000269|PubMed:14976244, ECO:0000269|PubMed:16054031}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q96PN6}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q96PN6}; Cytoplasmic side {ECO:0000250|UniProtKB:Q96PN6}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12475901}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:12475901}. Nucleus {ECO:0000269|PubMed:12475901}. Cell projection, cilium {ECO:0000250|UniProtKB:Q96PN6}. Cytoplasm {ECO:0000269|PubMed:12475901}. Mitochondrion {ECO:0000269|PubMed:12475901}. Note=Distributed to subcellular compartments containing cAMP targets. Found as a plasma membrane-associated protein, protein concentrated in the perinuclear region and protein colocalized with actin or tubulin. {ECO:0000250|UniProtKB:Q96PN6, ECO:0000269|PubMed:12475901}. DOMAIN: The N-terminal guanylate cyclase domains are required for enzyme activity. Fragments containing the first 470 amino acid residues are fully active. {ECO:0000250|UniProtKB:Q96PN6}. TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:16054031}. +Q9QZQ1 AFAD_MOUSE Afadin (Afadin adherens junction formation factor) (Protein Af-6) 1820 206,499 Alternative sequence (1); Beta strand (30); Chain (1); Coiled coil (4); Compositional bias (4); Domain (5); Helix (8); Modified residue (30); Sequence conflict (4); Turn (3) FUNCTION: Belongs to an adhesion system, probably together with the E-cadherin-catenin system, which plays a role in the organization of homotypic, interneuronal and heterotypic cell-cell adherens junctions (AJs). Nectin- and actin-filament-binding protein that connects nectin to the actin cytoskeleton. May play a key role in the organization of epithelial structures of the embryonic ectoderm. {ECO:0000269|PubMed:10477764}. SUBCELLULAR LOCATION: Cell junction, adherens junction. Note=Not found at cell-matrix AJs. SUBUNIT: Homodimer. Interacts with F-actin, nectin and NECTIN3. Essential for the association of nectin and E-cadherin. Isoform 2/s-afadin does not interact with F-actin. Interacts with ZO-1 and occludin, but probably in an indirect manner. Interacts with RIT1, RIT2, NRXN1 and BCR (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Isoform 1 is expressed only in a restricted set of epithelial structures during early embryogenesis. {ECO:0000269|PubMed:10477764}. +Q80WT5 AFTIN_MOUSE Aftiphilin 931 101,131 Alternative sequence (1); Chain (1); Erroneous gene model prediction (2); Modified residue (3); Motif (3); Region (1) FUNCTION: May play a role in membrane trafficking. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Colocalizes with AP1G1 and clathrin. {ECO:0000250}. SUBUNIT: Interacts with GGA1, GGA3, AP1G1 and AP1G2 via their GAE domain. {ECO:0000250}. DOMAIN: The WXXF motifs mediate binding of accessory proteins to the ear-domain of AP-1, GGAs and AP-2 through hydrophobic interactions. Selective binding to the GAE domains of AP-1 or to the alpha-ear domain of AP-2 is tuned by the acidic context surrounding the motif and the properties of the second residue of the motif itself (By similarity). {ECO:0000250}. +Q3UGP8 AG10B_MOUSE Putative Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase (EC 2.4.1.256) (Alpha-1,2-glucosyltransferase ALG10-A) (Alpha-2-glucosyltransferase ALG10-B) (Asparagine-linked glycosylation protein 10 homolog B) 474 55,465 Chain (1); Mutagenesis (1); Sequence conflict (3); Topological domain (13); Transmembrane (12) TRANSMEM 7 27 Helical. {ECO:0000255}.; TRANSMEM 65 85 Helical. {ECO:0000255}.; TRANSMEM 98 118 Helical. {ECO:0000255}.; TRANSMEM 127 147 Helical. {ECO:0000255}.; TRANSMEM 151 171 Helical. {ECO:0000255}.; TRANSMEM 176 196 Helical. {ECO:0000255}.; TRANSMEM 257 277 Helical. {ECO:0000255}.; TRANSMEM 284 304 Helical. {ECO:0000255}.; TRANSMEM 318 338 Helical. {ECO:0000255}.; TRANSMEM 366 386 Helical. {ECO:0000255}.; TRANSMEM 393 413 Helical. {ECO:0000255}.; TRANSMEM 437 457 Helical. {ECO:0000255}. TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 28 64 Extracellular. {ECO:0000255}.; TOPO_DOM 86 97 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 119 126 Extracellular. {ECO:0000255}.; TOPO_DOM 148 150 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 172 175 Extracellular. {ECO:0000255}.; TOPO_DOM 197 256 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 278 283 Extracellular. {ECO:0000255}.; TOPO_DOM 305 317 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 339 365 Extracellular. {ECO:0000255}.; TOPO_DOM 387 392 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 414 436 Extracellular. {ECO:0000255}.; TOPO_DOM 458 473 Cytoplasmic. {ECO:0000255}. FUNCTION: Putative alpha-1,2-glucosyltransferase, which adds the third glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Glc(2)Man(9)GlcNAc(2)-PP-Dol (By similarity). When coupled to KCNH2 may reduce KCNH2 sensitivity to classic proarrhythmic drug blockade, possibly by mediating glycosylation of KCNH2 (By similarity). Has a role in maintenance of cochlear outer hair cell function (PubMed:24303013). {ECO:0000250|UniProtKB:O88788, ECO:0000250|UniProtKB:P50076, ECO:0000269|PubMed:24303013}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O88788}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O88788}. SUBUNIT: Interacts with KCNH1 and KCNH2. {ECO:0000250|UniProtKB:O88788}. +Q9WUA6 AKT3_MOUSE RAC-gamma serine/threonine-protein kinase (EC 2.7.11.1) (Protein kinase Akt-3) (Protein kinase B gamma) (PKB gamma) (RAC-PK-gamma) 479 55,714 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Disulfide bond (2); Domain (3); Glycosylation (2); Initiator methionine (1); Modified residue (4); Mutagenesis (1); Nucleotide binding (1) FUNCTION: AKT3 is one of 3 closely related serine/threonine-protein kinases (AKT1, AKT2 and AKT3) called the AKT kinase, and which regulate many processes including metabolism, proliferation, cell survival, growth and angiogenesis. This is mediated through serine and/or threonine phosphorylation of a range of downstream substrates. Over 100 substrate candidates have been reported so far, but for most of them, no isoform specificity has been reported. AKT3 is the least studied AKT isoform. It plays an important role in brain development and is crucial for the viability of malignant glioma cells. AKT3 isoform may also be the key molecule in up-regulation and down-regulation of MMP13 via IL13. Required for the coordination of mitochondrial biogenesis with growth factor-induced increases in cellular energy demands. Down-regulation by RNA interference reduces the expression of the phosphorylated form of BAD, resulting in the induction of caspase-dependent apoptosis. {ECO:0000269|PubMed:15713641, ECO:0000269|PubMed:21159799}. PTM: Phosphorylation on Thr-305 and Ser-472 is required for full activity.; PTM: Ubiquitinated. When fully phosphorylated and translocated into the nucleus, undergoes 'Lys-48'-polyubiquitination catalyzed by TTC3, leading to its degradation by the proteasome (By similarity). {ECO:0000250}.; PTM: O-GlcNAcylation at Thr-302 and Thr-309 inhibits activating phosphorylation at Thr-305 via disrupting the interaction between AKT and PDK1. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm. Membrane; Peripheral membrane protein. Note=Membrane-associated after cell stimulation leading to its translocation. SUBUNIT: Interacts (via PH domain) with TCL1A; this enhances AKT3 phosphorylation and activation. Interacts with TRAF6 (By similarity). Interacts with KCTD20 (PubMed:24156551). Interacts with BTBD10 (PubMed:18160256). {ECO:0000250, ECO:0000269|PubMed:18160256, ECO:0000269|PubMed:24156551}. DOMAIN: Binding of the PH domain to the phosphatidylinositol 3-kinase alpha (PI(3)K) results in its targeting to the plasma membrane. TISSUE SPECIFICITY: Isoform 1 is expressed in prostate, testis, uterus and mammary gland and isoform 2 is expressed in prostate, testis and mammary gland. +Q8CJF8 AGO4_MOUSE Protein argonaute-4 (Argonaute4) (mAgo4) (Argonaute RISC catalytic component 4) (Eukaryotic translation initiation factor 2C 4) (eIF-2C 4) (eIF2C 4) (Piwi/argonaute family protein meIF2C4) 861 97,037 Alternative sequence (1); Chain (1); Domain (2); Erroneous initiation (1); Sequence caution (1); Sequence conflict (6) FUNCTION: Required for RNA-mediated gene silencing (RNAi). Binds to short RNAs such as microRNAs (miRNAs) and represses the translation of mRNAs which are complementary to them. Lacks endonuclease activity and does not appear to cleave target mRNAs. {ECO:0000255|HAMAP-Rule:MF_03033, ECO:0000269|PubMed:19174539}. SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000255|HAMAP-Rule:MF_03033}. SUBUNIT: Interacts with EIF4B, IMP8, PRMT5, TNRC6A and TNRC6B. Interacts with ZFP36. {ECO:0000255|HAMAP-Rule:MF_03033}. +Q8K009 AL1L2_MOUSE Mitochondrial 10-formyltetrahydrofolate dehydrogenase (Mitochondrial 10-FTHFDH) (mtFDH) (EC 1.5.1.6) (Aldehyde dehydrogenase family 1 member L2) 923 101,590 Active site (3); Chain (1); Domain (1); Modified residue (7); Region (2); Sequence conflict (1); Site (1); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. +Q9D1F4 AKTS1_MOUSE Proline-rich AKT1 substrate 1 (Proline-rich AKT substrate) 257 27,483 Chain (1); Compositional bias (2); Modified residue (10) FUNCTION: Subunit of mTORC1, which regulates cell growth and survival in response to nutrient and hormonal signals. mTORC1 is activated in response to growth factors or amino acids. Growth factor-stimulated mTORC1 activation involves a AKT1-mediated phosphorylation of TSC1-TSC2, which leads to the activation of the RHEB GTPase that potently activates the protein kinase activity of mTORC1. Amino acid-signaling to mTORC1 requires its relocalization to the lysosomes mediated by the Ragulator complex and the Rag GTPases. Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. mTORC1 phosphorylates EIF4EBP1 and releases it from inhibiting the elongation initiation factor 4E (eiF4E). mTORC1 phosphorylates and activates S6K1 at 'Thr-389', which then promotes protein synthesis by phosphorylating PDCD4 and targeting it for degradation. Within mTORC1, AKT1S1 negatively regulates mTOR activity in a manner that is dependent on its phosphorylation state and binding to 14-3-3. Inhibits RHEB-GTP-dependent mTORC1 activation. Substrate for AKT1 phosphorylation, but can also be activated by AKT1-independent mechanisms. May also play a role in nerve growth factor-mediated neuroprotection. {ECO:0000269|PubMed:14973226, ECO:0000269|PubMed:16397181}. PTM: Phosphorylated by AKT1. Phosphorylation at Thr-247 by DYRK3 relieves inhibitory function on mTORC1. {ECO:0000250|UniProtKB:Q96B36}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:14973226}. Note=Found in the cytosolic fraction of the brain. Colocalizes with cortical neurons following ischemic/reperfusion injury. SUBUNIT: Part of the mammalian target of rapamycin complex 1 (mTORC1) which contains MTOR, MLST8, RPTOR, AKT1S1/PRAS40 and DEPTOR. mTORC1 binds to and is inhibited by FKBP12-rapamycin. Interacts directly with RPTOR. The phosphorylated form interacts with 14-3-3 proteins and with phosphorylated AKT1 following transient focal cerebral ischemia in vivo. {ECO:0000269|PubMed:14973226}. +Q8BUZ1 ABRA_MOUSE Actin-binding Rho-activating protein (Striated muscle activator of Rho-dependent signaling) (STARS) 375 42,831 Chain (1); Modified residue (2); Region (4); Sequence conflict (4) FUNCTION: Acts as an activator of serum response factor (SRF)-dependent transcription possibly by inducing nuclear translocation of MKL1 or MKL2 and through a mechanism requiring Rho-actin signaling. {ECO:0000269|PubMed:11983702, ECO:0000269|PubMed:15798203}. SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Localized to the I-band of the sarcomere and to a lesser extent to the sarcomeric structure between Z-lines. {ECO:0000250}. SUBUNIT: Binds F-actin and ABLIM1, ABLIM2 AND ABLIM3. Interaction with ABLIM2 AND ABLIM3 enhances activity. DOMAIN: The actin-binding domain 1 (ABD1) is intrinsically disordered, and binds to F-actin with higher affinity than ABD2. {ECO:0000250}. TISSUE SPECIFICITY: Expressed specifically in heart and skeletal muscle. {ECO:0000269|PubMed:11983702}. +Q6PE15 ABHDA_MOUSE Mycophenolic acid acyl-glucuronide esterase, mitochondrial (EC 3.1.1.93) (Alpha/beta hydrolase domain-containing protein 10) (Abhydrolase domain-containing protein 10) 297 33,040 Active site (3); Alternative sequence (2); Chain (1); Domain (1); Sequence conflict (1); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}. +Q9D258 ACBD7_MOUSE Acyl-CoA-binding domain-containing protein 7 88 10,011 Binding site (3); Chain (1); Domain (1); Region (1); Sequence conflict (1) FUNCTION: Binds medium- and long-chain acyl-CoA esters. {ECO:0000250}. +Q8K370 ACD10_MOUSE Acyl-CoA dehydrogenase family member 10 (ACAD-10) (EC 1.3.99.-) 1069 118,979 Binding site (4); Chain (1); Erroneous initiation (1); Frameshift (1); Modified residue (5); Nucleotide binding (1); Sequence conflict (1) FUNCTION: Acyl-CoA dehydrogenase only active with R- and S-2-methyl-C15-CoA. {ECO:0000250}. +P51174 ACADL_MOUSE Long-chain specific acyl-CoA dehydrogenase, mitochondrial (LCAD) (EC 1.3.8.8) 430 47,908 Chain (1); Modified residue (21); Mutagenesis (3); Sequence conflict (15); Transit peptide (1) Lipid metabolism; mitochondrial fatty acid beta-oxidation. PTM: Acetylation at Lys-318 and Lys-322 in proximity of the cofactor-binding sites strongly reduces catalytic activity. These sites are deacetylated by SIRT3. {ECO:0000269|PubMed:24121500}. SUBCELLULAR LOCATION: Mitochondrion matrix. SUBUNIT: Homotetramer. +Q8VD53 ACER2_MOUSE Alkaline ceramidase 2 (AlkCDase 2) (Alkaline CDase 2) (maCER2) (EC 3.5.1.23) (Acylsphingosine deacylase 3-like) (Cancer-related gene liver 1 protein) (CRG-L1) (N-acylsphingosine amidohydrolase 3-like) 275 31,369 Alternative sequence (1); Chain (1); Glycosylation (1); Sequence caution (1); Topological domain (8); Transmembrane (7) TRANSMEM 33 53 Helical. {ECO:0000255}.; TRANSMEM 63 83 Helical. {ECO:0000255}.; TRANSMEM 87 107 Helical. {ECO:0000255}.; TRANSMEM 125 142 Helical. {ECO:0000255}.; TRANSMEM 144 164 Helical. {ECO:0000255}.; TRANSMEM 174 194 Helical. {ECO:0000255}.; TRANSMEM 212 232 Helical. {ECO:0000255}. TOPO_DOM 1 32 Lumenal. {ECO:0000255}.; TOPO_DOM 54 62 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 84 86 Lumenal. {ECO:0000255}.; TOPO_DOM 108 124 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 143 143 Lumenal. {ECO:0000255}.; TOPO_DOM 165 173 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 195 211 Lumenal. {ECO:0000255}.; TOPO_DOM 233 275 Cytoplasmic. {ECO:0000255}. FUNCTION: Hydrolyzes the sphingolipid ceramide into sphingosine and free fatty acid. Unsaturated long-chain ceramides are the best substrates, saturated long-chain ceramides and unsaturated very long-chain ceramides are good substrates, whereas saturated very long-chain ceramides and short-chain ceramides were poor substrates. Inhibits the maturation of protein glycosylation in the Golgi complex, including that of integrin beta-1 (ITGB1) and of LAMP1, by increasing the levels of sphingosine. Inhibits cell adhesion by reducing the level of ITGB1 in the cell surface. May have a role in cell proliferation and apoptosis that seems to depend on the balance between sphingosine and sphingosine-1-phosphate. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q9QY83 ACL7B_MOUSE Actin-like protein 7B (Actin-like-7-beta) (Testis-specific actin-1) (T-actin-1) 418 45,565 Chain (1); Modified residue (1); Sequence conflict (1) SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. TISSUE SPECIFICITY: Testis specific. +Q9ERZ3 ACM3_MOUSE Muscarinic acetylcholine receptor M3 (Mm3 mAChR) 589 66,212 Chain (1); Disulfide bond (2); Glycosylation (5); Modified residue (1); Motif (1); Region (2); Topological domain (8); Transmembrane (7) TRANSMEM 67 90 Helical; Name=1. {ECO:0000250}.; TRANSMEM 104 129 Helical; Name=2. {ECO:0000250}.; TRANSMEM 142 163 Helical; Name=3. {ECO:0000250}.; TRANSMEM 184 205 Helical; Name=4. {ECO:0000250}.; TRANSMEM 229 251 Helical; Name=5. {ECO:0000250}.; TRANSMEM 491 513 Helical; Name=6. {ECO:0000250}.; TRANSMEM 526 545 Helical; Name=7. {ECO:0000250}. TOPO_DOM 1 66 Extracellular. {ECO:0000250}.; TOPO_DOM 91 103 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 130 141 Extracellular. {ECO:0000250}.; TOPO_DOM 164 183 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 206 228 Extracellular. {ECO:0000250}.; TOPO_DOM 252 490 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 514 525 Extracellular. {ECO:0000250}.; TOPO_DOM 546 589 Cytoplasmic. {ECO:0000250}. FUNCTION: The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is Pi turnover. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Basolateral cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Homodimer; the dimers can form tetramers (By similarity). Interacts with NALCN (PubMed:19575010). {ECO:0000250|UniProtKB:P20309, ECO:0000269|PubMed:19575010}. +A2AKK5 ACNT1_MOUSE Acyl-coenzyme A amino acid N-acyltransferase 1 (EC 2.3.1.-) 416 46,071 Active site (3); Alternative sequence (1); Chain (1); Modified residue (2); Motif (1); Sequence conflict (2) FUNCTION: Acyltransferase which efficiently conjugates very long-chain and long-chain fatty acids to taurine. Shows no conjugation activity in the presence of glycine. {ECO:0000269|PubMed:17116739}. SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:17116739}. TISSUE SPECIFICITY: Expressed mainly in liver and kidney with low levels in adrenal and little or no expression in other tissues. {ECO:0000269|PubMed:17116739}. +Q8BFZ3 ACTBL_MOUSE Beta-actin-like protein 2 (Kappa-actin) 376 42,004 Chain (1); Modified residue (2) FUNCTION: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. {ECO:0000250}. PTM: Oxidation of Met-45 and Met-48 by MICALs (MICAL1, MICAL2 or MICAL3) to form methionine sulfoxide promotes actin filament depolymerization. MICAL1 and MICAL2 produce the (R)-S-oxide form. The (R)-S-oxide form is reverted by MSRB1 and MSRB2, which promote actin repolymerization. {ECO:0000269|PubMed:23911929}.; PTM: Monomethylation at Lys-85 (K84me1) regulates actin-myosin interaction and actomyosin-dependent processes. Demethylation by ALKBH4 is required for maintaining actomyosin dynamics supporting normal cleavage furrow ingression during cytokinesis and cell migration (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. SUBUNIT: Polymerization of globular actin (G-actin) leads to a structural filament (F-actin) in the form of a two-stranded helix. Each actin can bind to 4 others (By similarity). Interacts with PFN1 and PFDN1 (By similarity). {ECO:0000250}. +Q9R158 AD26A_MOUSE Disintegrin and metalloproteinase domain-containing protein 26A (ADAM 26A) (EC 3.4.24.-) (Testase-3) 697 78,747 Active site (1); Chain (1); Compositional bias (1); Disulfide bond (6); Domain (3); Glycosylation (8); Metal binding (4); Motif (1); Propeptide (1); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 672 692 Helical. {ECO:0000255}. TOPO_DOM 188 671 Extracellular. {ECO:0000255}.; TOPO_DOM 693 697 Cytoplasmic. {ECO:0000255}. FUNCTION: Sperm surface membrane protein that may be involved in spermatogenesis and fertilization. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. DOMAIN: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme. TISSUE SPECIFICITY: Expressed specifically in testis. +Q8JZR0 ACSL5_MOUSE Long-chain-fatty-acid--CoA ligase 5 (EC 6.2.1.3) (Long-chain acyl-CoA synthetase 5) (LACS 5) 683 76,206 Chain (1); Modified residue (1); Topological domain (1); Transmembrane (1) TRANSMEM 12 32 Helical; Signal-anchor for type III membrane protein. {ECO:0000255}. TOPO_DOM 33 683 Cytoplasmic. {ECO:0000255}. FUNCTION: Acyl-CoA synthetases (ACSL) activates long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. ACSL5 may activate fatty acids from exogenous sources for the synthesis of triacylglycerol destined for intracellular storage (By similarity). It was suggested that it may also stimulate fatty acid oxidation (By similarity). At the villus tip of the crypt-villus axis of the small intestine may sensitize epithelial cells to apoptosis specifically triggered by the death ligand TRAIL (By similarity). May have a role in the survival of glioma cells (By similarity). Utilizes a wide range of saturated fatty acids with a preference for C16-C18 unsaturated fatty acids (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Mitochondrion outer membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. +Q9D9J3 ACTT1_MOUSE Actin-related protein T1 376 42,216 Chain (1) FUNCTION: Negatively regulates the Hedgehog (SHH) signaling. Binds to the promoter of the SHH signaling mediator, GLI1, and inhibits its expression. {ECO:0000250|UniProtKB:Q8TDG2}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q8TDG2}. Cytoplasm {ECO:0000250|UniProtKB:Q8TDG2}. Nucleus {ECO:0000250|UniProtKB:Q8TDG2}. Note=Both detected in the nucleus and cytoplasm, localizes to the nucleus where it binds chromatin upon stimulation of the Hedgehog pathway. {ECO:0000250|UniProtKB:Q8TDG2}. +Q80SY6 ADAL_MOUSE Adenosine deaminase-like protein (EC 3.5.4.-) 360 41,001 Active site (1); Alternative sequence (4); Binding site (3); Chain (1); Erroneous gene model prediction (1); Metal binding (4); Sequence conflict (2); Site (1) FUNCTION: Putative nucleoside deaminase. May catalyze the hydrolytic deamination of adenosine or some similar substrate and play a role in purine metabolism (By similarity). {ECO:0000250}. +Q01337 ADA2C_MOUSE Alpha-2C adrenergic receptor (Alpha-2 adrenergic receptor subtype C4) (Alpha-2C adrenoreceptor) (Alpha-2C adrenoceptor) (Alpha-2CAR) 458 49,906 Chain (1); Compositional bias (1); Disulfide bond (1); Glycosylation (2); Sequence conflict (3); Site (3); Topological domain (8); Transmembrane (7) TRANSMEM 52 76 Helical; Name=1. {ECO:0000250}.; TRANSMEM 89 114 Helical; Name=2. {ECO:0000250}.; TRANSMEM 125 147 Helical; Name=3. {ECO:0000250}.; TRANSMEM 169 191 Helical; Name=4. {ECO:0000250}.; TRANSMEM 208 231 Helical; Name=5. {ECO:0000250}.; TRANSMEM 380 403 Helical; Name=6. {ECO:0000250}.; TRANSMEM 417 437 Helical; Name=7. {ECO:0000250}. TOPO_DOM 1 51 Extracellular. {ECO:0000250}.; TOPO_DOM 77 88 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 115 124 Extracellular. {ECO:0000250}.; TOPO_DOM 148 168 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 192 207 Extracellular. {ECO:0000250}.; TOPO_DOM 232 379 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 404 416 Extracellular. {ECO:0000250}.; TOPO_DOM 438 458 Cytoplasmic. {ECO:0000250}. FUNCTION: Alpha-2 adrenergic receptors mediate the catecholamine-induced inhibition of adenylate cyclase through the action of G proteins. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q6NSR3 ADCK2_MOUSE Uncharacterized aarF domain-containing protein kinase 2 (EC 2.7.11.-) 617 68,677 Active site (1); Binding site (1); Chain (1); Compositional bias (1); Domain (1); Nucleotide binding (1); Sequence conflict (4); Transmembrane (1) TRANSMEM 103 123 Helical. {ECO:0000255}. FUNCTION: The function of this protein is not yet clear. It is not known if it has protein kinase activity and what type of substrate it would phosphorylate (Ser, Thr or Tyr). SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q9Z0F8 ADA17_MOUSE Disintegrin and metalloproteinase domain-containing protein 17 (ADAM 17) (EC 3.4.24.86) (TNF-alpha convertase) (TNF-alpha-converting enzyme) (CD antigen CD156b) 827 93,056 Active site (1); Alternative sequence (2); Chain (1); Compositional bias (2); Disulfide bond (7); Domain (2); Glycosylation (7); Metal binding (4); Modified residue (5); Motif (2); Propeptide (1); Region (1); Sequence conflict (18); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 672 692 Helical. {ECO:0000255}. TOPO_DOM 215 671 Extracellular. {ECO:0000255}.; TOPO_DOM 693 827 Cytoplasmic. {ECO:0000255}. FUNCTION: Cleaves the membrane-bound precursor of TNF-alpha to its mature soluble form. Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface. Plays a role in the proteolytic processing of ACE2 (By similarity). Responsible for the proteolytic release of several other cell-surface proteins, including p75 TNF-receptor, interleukin 1 receptor type II, p55 TNF-receptor, transforming growth factor-alpha, L-selectin, growth hormone receptor, MUC1 and the amyloid precursor protein (PubMed:10799547, PubMed:11108241). Acts as an activator of Notch pathway by mediating cleavage of Notch, generating the membrane-associated intermediate fragment called notch extracellular truncation (NEXT) (PubMed:10882063). {ECO:0000250, ECO:0000269|PubMed:10799547, ECO:0000269|PubMed:10882063, ECO:0000269|PubMed:11108241}. PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}.; PTM: Phosphorylated. Stimulation by growth factor or phorbol 12-myristate 13-acetate induces phosphorylation of Ser-822 but decreases phosphorylation of Ser-794. Phosphorylation at THR-735 by MAPK14 is required for ADAM17-mediated ectodomain shedding (By similarity). {ECO:0000250|UniProtKB:P78536}. SUBCELLULAR LOCATION: Isoform Long: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Isoform Short: Secreted. SUBUNIT: Interacts with MAD2L1, MAPK14 and MUC1. {ECO:0000250|UniProtKB:P78536}. DOMAIN: Must be membrane anchored to cleave the different substrates. The cytoplasmic domain is not required for the this activity. Only the catalytic domain is essential to shed TNF and p75 TNFR.; DOMAIN: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme. TISSUE SPECIFICITY: Ubiquitously expressed. Expressed at highest levels in heart, liver, skeletal muscle, kidney and testes. Expressed at lower levels in brain, spleen and lung. +Q70FJ1 AKAP9_MOUSE A-kinase anchor protein 9 (AKAP-9) (Protein kinase A-anchoring protein 9) (PRKA9) 3797 436,214 Alternative sequence (2); Chain (1); Coiled coil (4); Compositional bias (2); Modified residue (5); Region (1); Sequence conflict (3) FUNCTION: Scaffolding protein that assembles several protein kinases and phosphatases on the centrosome and Golgi apparatus. Required to maintain the integrity of the Golgi apparatus. Required for microtubule nucleation at the cis-side of the Golgi apparatus. Required for association of the centrosomes with the poles of the bipolar mitotic spindle during metaphase. In complex with PDE4DIP isoform 2/MMG8/SMYLE, recruits CAMSAP2 to the Golgi apparatus and tethers non-centrosomal minus-end microtubules to the Golgi, an important step for polarized cell movement. In complex with PDE4DIP isoform 2, EB1/MAPRE1 and CDK5RAP2, contributes to microtubules nucleation and extension also from the centrosome to the cell periphery. {ECO:0000250|UniProtKB:Q99996}. SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:Q99996}. Cytoplasm {ECO:0000250|UniProtKB:Q99996}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q99996}. Note=Cytoplasmic in parietal cells. Recruited to the Golgi apparatus by GM130/GOLGA2. Localization at the centrosome versus Golgi apparatus may be cell type-dependent. Recruited to the centrosome in the presence of CDK5RAP2. {ECO:0000250|UniProtKB:Q99996}. SUBUNIT: Interacts with the regulatory region of protein kinase N (PKN), protein phosphatase 2A (PP2A), protein phosphatase 1 (PP1) and the immature non-phosphorylated form of PKC epsilon. Interacts with CIP4 and FNBP1. Interacts with chloride intracellular channel proteins CLIC1, CLIC4 and CLIC5. CSNK1D binding promotes its centrosomal subcellular location. Interacts with GM130/GOLGA2; leading to recruitment to the Golgi apparatus. Interacts with KCNQ1; targets protein kinase A (PKA) catalytic and regulatory subunits and protein phosphatase 1 (PP1), to the heterodimer KCNQ1-KCNE1. Interacts with PDE4DIP isoform 2; this interaction stabilizes both proteins. In complex with PDE4DIP isoform 2, recruits CAMSAP2 to the Golgi apparatus. Forms a pericentrosomal complex with CDK5RAP2, EB1/MAPRE1 and PDE4DIP isoform 2; within this complex, MAPRE1 binding to CDK5RAP2 may be mediated by PDE4DIP. Interacts with MAPRE1 and MAPRE3. Interacts (via C-terminus) with CAMSAP2; this interaction is much stronger in the presence of PDE4DIP isoform 2. Interacts with CAMSAP3. Interacts (via C-terminus) with the gamma-tubulin ring complex (gamma-TuRC), composed of gamma-tubulin, TUBGCP2, TUBGCP3, TUBGCP4, TUBGCP5 and TUBGCP6. {ECO:0000250|UniProtKB:Q99996}. DOMAIN: RII-binding site, predicted to form an amphipathic helix, could participate in protein-protein interactions with a complementary surface on the R-subunit dimer. {ECO:0000250|UniProtKB:Q28628}. +Q80VQ0 AL3B1_MOUSE Aldehyde dehydrogenase family 3 member B1 (EC 1.2.1.5) (Aldehyde dehydrogenase 7) 468 52,292 Active site (2); Chain (1); Lipidation (3); Modified residue (2); Mutagenesis (3); Nucleotide binding (1); Propeptide (1) Alcohol metabolism; ethanol degradation; acetate from ethanol: step 2/2. FUNCTION: Oxidizes medium and long chain saturated and unsaturated aldehydes (PubMed:25286108). Metabolizes also benzaldehyde (By similarity). Low activity towards acetaldehyde and 3,4-dihydroxyphenylacetaldehyde (By similarity). May not metabolize short chain aldehydes. May use both NADP(+) and NAD(+) as cofactors (By similarity). May have a protective role against the cytotoxicity induced by lipid peroxidation (By similarity). {ECO:0000250|UniProtKB:P43353, ECO:0000269|PubMed:25286108}. PTM: Dually lipidated in the C-terminus; prenylation occurs prior to, and is a prerequisite for palmitoylation. It is also required for activity towards long-chain substrates. {ECO:0000269|PubMed:25286108}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25286108}; Lipid-anchor {ECO:0000269|PubMed:25286108}. Note=Primarily in the plasma membrane as well as in some punctate structures in the cytoplasm. {ECO:0000269|PubMed:25286108}. TISSUE SPECIFICITY: Highly expressed in kidney and liver. In brain is expressed at moderate levels in cortex, striatum and hippocampus, and at lower levels in brainstem and cerebellum. {ECO:0000269|PubMed:17382292}. +Q60823 AKT2_MOUSE RAC-beta serine/threonine-protein kinase (EC 2.7.11.1) (Protein kinase Akt-2) (Protein kinase B beta) (PKB beta) (RAC-PK-beta) 481 55,742 Active site (1); Binding site (8); Chain (1); Disulfide bond (2); Domain (3); Glycosylation (4); Metal binding (2); Modified residue (8); Nucleotide binding (1); Region (3) FUNCTION: AKT2 is one of 3 closely related serine/threonine-protein kinases (AKT1, AKT2 and AKT3) called the AKT kinases, and which regulate many processes including metabolism, proliferation, cell survival, growth and angiogenesis. This is mediated through serine and/or threonine phosphorylation of a range of downstream substrates. Over 100 substrate candidates have been reported so far, but for most of them, no isoform specificity has been reported. AKT is responsible of the regulation of glucose uptake by mediating insulin-induced translocation of the SLC2A4/GLUT4 glucose transporter to the cell surface. Phosphorylation of PTPN1 at 'Ser-50' negatively modulates its phosphatase activity preventing dephosphorylation of the insulin receptor and the attenuation of insulin signaling. Phosphorylation of TBC1D4 triggers the binding of this effector to inhibitory 14-3-3 proteins, which is required for insulin-stimulated glucose transport. AKT regulates also the storage of glucose in the form of glycogen by phosphorylating GSK3A at 'Ser-21' and GSK3B at 'Ser-9', resulting in inhibition of its kinase activity. Phosphorylation of GSK3 isoforms by AKT is also thought to be one mechanism by which cell proliferation is driven. AKT regulates also cell survival via the phosphorylation of MAP3K5 (apoptosis signal-related kinase). Phosphorylation of 'Ser-83' decreases MAP3K5 kinase activity stimulated by oxidative stress and thereby prevents apoptosis. AKT mediates insulin-stimulated protein synthesis by phosphorylating TSC2 at 'Ser-939' and 'Thr-1462', thereby activating mTORC1 signaling and leading to both phosphorylation of 4E-BP1 and in activation of RPS6KB1. AKT is involved in the phosphorylation of members of the FOXO factors (Forkhead family of transcription factors), leading to binding of 14-3-3 proteins and cytoplasmic localization. In particular, FOXO1 is phosphorylated at 'Thr-24', 'Ser-256' and 'Ser-319'. FOXO3 and FOXO4 are phosphorylated on equivalent sites. AKT has an important role in the regulation of NF-kappa-B-dependent gene transcription and positively regulates the activity of CREB1 (cyclic AMP (cAMP)-response element binding protein). The phosphorylation of CREB1 induces the binding of accessory proteins that are necessary for the transcription of pro-survival genes such as BCL2 and MCL1. AKT phosphorylates 'Ser-454' on ATP citrate lyase (ACLY), thereby potentially regulating ACLY activity and fatty acid synthesis. Activates the 3B isoform of cyclic nucleotide phosphodiesterase (PDE3B) via phosphorylation of 'Ser-273', resulting in reduced cyclic AMP levels and inhibition of lipolysis. Phosphorylates PIKFYVE on 'Ser-318', which results in increased PI(3)P-5 activity. The Rho GTPase-activating protein DLC1 is another substrate and its phosphorylation is implicated in the regulation cell proliferation and cell growth. AKT plays a role as key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation. Signals downstream of phosphatidylinositol 3-kinase (PI(3)K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I). AKT mediates the antiapoptotic effects of IGF-I. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. May be involved in the regulation of the placental development.; FUNCTION: One of the few specific substrates of AKT2 identified so far is PITX2. Phosphorylation of PITX2 impairs its association with the CCND1 mRNA-stabilizing complex thus shortening the half-life of CCND1. AKT2 seems also to be the principal isoform responsible of the regulation of glucose uptake. Phosphorylates C2CD5 on 'Ser-197' during insulin-stimulated adipocytes. AKT2 is also specifically involved in skeletal muscle differentiation, one of its substrates in this process being ANKRD2. Phosphorylates CLK2 on 'Thr-343'. PTM: Phosphorylation on Thr-309 and Ser-474 is required for full activity. {ECO:0000250}.; PTM: Ubiquitinated; undergoes both 'Lys-48'- and 'Lys-63'-linked polyubiquitination. TRAF6-induced 'Lys-63'-linked AKT2 ubiquitination. When fully phosphorylated and translocated into the nucleus, undergoes 'Lys-48'-polyubiquitination catalyzed by TTC3, leading to its degradation by the proteasome (By similarity). {ECO:0000250}.; PTM: O-GlcNAcylation at Thr-306 and Thr-313 inhibits activating phosphorylation at Thr-309 via disrupting the interaction between AKT and PDK1. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20189988}. Nucleus {ECO:0000269|PubMed:20189988}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Early endosome {ECO:0000269|PubMed:20189988}. Note=Localizes within both nucleus and cytoplasm of proliferative primary myoblasts and mostly within the nucleus of differentiated primary myoblasts. By virtue of the N-terminal PH domain, is recruited to sites of the plasma membrane containing increased PI(3,4,5)P3 or PI(3,4)P2, cell membrane targeting is also facilitared by interaction with CLIP3. Colocalizes with WDFY2 in early endosomes (PubMed:20189988). {ECO:0000250, ECO:0000269|PubMed:20189988}. SUBUNIT: Interacts (via PH domain) with MTCP1, TCL1A AND TCL1B. Interacts with CLK2, PBH2 and TRAF6. Interacts (when phosphorylated) with CLIP3, the interaction promotes cell membrane localization (By similarity). Interacts with BTBD10 (PubMed:18160256). Interacts with KCTD20 (PubMed:24156551). Interacts with WDFY2 (via WD repeats 1-3) (PubMed:16792529, PubMed:20189988). {ECO:0000250|UniProtKB:P31751, ECO:0000269|PubMed:16792529, ECO:0000269|PubMed:18160256, ECO:0000269|PubMed:20189988, ECO:0000269|PubMed:24156551}. DOMAIN: Binding of the PH domain to the phosphatidylinositol 3-kinase alpha (PIK3CA) results in its targeting to the plasma membrane. {ECO:0000250}. +Q8VHG2 AMOT_MOUSE Angiomotin 1126 120,915 Alternative sequence (2); Chain (1); Coiled coil (2); Compositional bias (1); Cross-link (2); Erroneous initiation (4); Modified residue (1); Motif (1); Sequence conflict (9) FUNCTION: Plays a central role in tight junction maintenance via the complex formed with ARHGAP17, which acts by regulating the uptake of polarity proteins at tight junctions. Appears to regulate endothelial cell migration and tube formation. May also play a role in the assembly of endothelial cell-cell junctions (By similarity). {ECO:0000250}. PTM: Polyubiquitinated by NEDD4, NEDD4L and ITCH, leading to proteasomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000250}. Note=Localized on the cell surface. May act as a transmembrane protein (By similarity). {ECO:0000250}. SUBUNIT: Component of a complex whose core is composed of ARHGAP17, AMOT, MPP5/PALS1, PATJ and PARD3/PAR3. Interacts with MAGI1 and angiostatin (By similarity). {ECO:0000250}. DOMAIN: The angiostatin binding domain (850-1047) allows the binding to angiostatin.; DOMAIN: The coiled coil domain interacts directly with the BAR domain of ARHGAP17. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain, skeletal muscle and placenta. {ECO:0000269|PubMed:12406577}. +Q3V1D3 AMPD1_MOUSE AMP deaminase 1 (EC 3.5.4.6) (AMP deaminase isoform M) (Myoadenylate deaminase) 745 86,105 Active site (1); Binding site (2); Chain (1); Metal binding (4); Modified residue (4); Region (2); Sequence conflict (2) Purine metabolism; IMP biosynthesis via salvage pathway; IMP from AMP: step 1/1. FUNCTION: AMP deaminase plays a critical role in energy metabolism. SUBUNIT: Homotetramer. {ECO:0000250}. +Q9CZK6 ANKS3_MOUSE Ankyrin repeat and SAM domain-containing protein 3 655 72,082 Chain (1); Coiled coil (1); Compositional bias (2); Domain (1); Modified residue (4); Repeat (6); Sequence conflict (2) PTM: Hydroxylated at Asn-96, most probably by HIF1AN. {ECO:0000269|PubMed:25671767}. SUBUNIT: Homooligomer (By similarity). Interacts with ANKS6 (PubMed:25671767). Interacts with BICC1 (PubMed:25671767). Interacts with NPHP1 (PubMed:25671767). Interacts with NEK8 (PubMed:25671767). Interacts with HIF1AN (PubMed:25671767). {ECO:0000250|UniProtKB:Q6ZW76, ECO:0000269|PubMed:25671767}. DOMAIN: The SAM domain mediates homooligomerization and interaction with ANKS6. {ECO:0000250|UniProtKB:Q6ZW76}. +Q8JZQ5 AOC1_MOUSE Amiloride-sensitive amine oxidase [copper-containing] (DAO) (Diamine oxidase) (EC 1.4.3.22) (Amiloride-binding protein 1) (Amine oxidase copper domain-containing protein 1) (Histaminase) 751 85,424 Active site (2); Chain (1); Disulfide bond (2); Glycosylation (4); Metal binding (12); Modified residue (1); Region (3); Sequence conflict (1); Signal peptide (1) FUNCTION: Catalyzes the degradation of compounds such as putrescine, histamine, spermine, and spermidine, substances involved in allergic and immune responses, cell proliferation, tissue differentiation, tumor formation, and possibly apoptosis. {ECO:0000250}. PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue. {ECO:0000250|UniProtKB:P12807}. SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250}. SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250|UniProtKB:P19801}. +P35585 AP1M1_MOUSE AP-1 complex subunit mu-1 (AP-mu chain family member mu1A) (Adaptor protein complex AP-1 subunit mu-1) (Adaptor-related protein complex 1 subunit mu-1) (Clathrin assembly protein complex 1 mu-1 medium chain 1) (Clathrin coat assembly protein AP47) (Clathrin coat-associated protein AP47) (Golgi adaptor HA1/AP1 adaptin mu-1 subunit) (Mu-adaptin 1) (Mu1A-adaptin) 423 48,543 Beta strand (25); Chain (1); Domain (1); Helix (9); Initiator methionine (1); Modified residue (4); Turn (2) FUNCTION: Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the trans-Golgi network (TGN) and endosomes. The AP complexes mediate the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. PTM: Phosphorylation of membrane-bound AP1M1/AP1M2 increases its affinity for sorting signals. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasmic vesicle, clathrin-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex. SUBUNIT: Adaptor protein complex 1 (AP-1) is a heterotetramer composed of two large adaptins (gamma-type subunit AP1G1 and beta-type subunit AP1B1), a medium adaptin (mu-type subunit AP1M1 or AP1M2) and a small adaptin (sigma-type subunit AP1S1 or AP1S2 or AP1S3). Interacts with MARCH11 (By similarity). {ECO:0000250}. +P10107 ANXA1_MOUSE Annexin A1 (Annexin I) (Annexin-1) (Calpactin II) (Calpactin-2) (Chromobindin-9) (Lipocortin I) (Phospholipase A2 inhibitory protein) (p35) 346 38,734 Chain (1); Cross-link (5); Disulfide bond (1); Initiator methionine (1); Metal binding (26); Modified residue (9); Mutagenesis (1); Repeat (4); Sequence conflict (4) FUNCTION: Plays important roles in the innate immune response as effector of glucocorticoid-mediated responses and regulator of the inflammatory process. Has anti-inflammatory activity (PubMed:12475898). Plays a role in glucocorticoid-mediated down-regulation of the early phase of the inflammatory response (PubMed:12475898). Promotes resolution of inflammation and wound healing (PubMed:25664854). Functions at least in part by activating the formyl peptide receptors and downstream signaling cascades. Promotes chemotaxis of granulocytes and monocytes via activation of the formyl peptide receptors (By similarity). Contributes to the adaptive immune response by enhancing signaling cascades that are triggered by T-cell activation, regulates differentiation and proliferation of activated T-cells (PubMed:17948261). Promotes the differentiation of T-cells into Th1 cells and negatively regulates differentiation into Th2 cells (PubMed:17948261). Has no effect on unstimulated T-cells. Promotes rearrangement of the actin cytoskeleton, cell polarization and cell migration. Negatively regulates hormone exocytosis via activation of the formyl peptide receptors and reorganization of the actin cytoskeleton (By similarity). Has high affinity for Ca(2+) and can bind up to eight Ca(2+) ions (By similarity). Displays Ca(2+)-dependent binding to phospholipid membranes (By similarity). Plays a role in the formation of phagocytic cups and phagosomes (PubMed:21245195). Plays a role in phagocytosis by mediating the Ca(2+)-dependent interaction between phagosomes and the actin cytoskeleton (PubMed:21245195). {ECO:0000250|UniProtKB:P04083, ECO:0000250|UniProtKB:P19619, ECO:0000269|PubMed:12475898, ECO:0000269|PubMed:17948261, ECO:0000269|PubMed:21245195, ECO:0000269|PubMed:25664854}. PTM: Phosphorylated by protein kinase C, EGFR and TRPM7. Phosphorylated in response to EGF treatment. {ECO:0000250|UniProtKB:P04083}.; PTM: Sumoylated. {ECO:0000269|PubMed:23727357}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07150}. Cytoplasm {ECO:0000269|PubMed:18802107, ECO:0000269|PubMed:21245195}. Cell projection, cilium {ECO:0000269|PubMed:17384087}. Basolateral cell membrane {ECO:0000250|UniProtKB:P51662}. Lateral cell membrane {ECO:0000269|PubMed:18802107}. Cell membrane {ECO:0000269|PubMed:14506282, ECO:0000269|PubMed:21245195}; Peripheral membrane protein {ECO:0000305}. Apical cell membrane {ECO:0000269|PubMed:17384087, ECO:0000269|PubMed:18802107}. Membrane {ECO:0000269|PubMed:23727357}; Peripheral membrane protein {ECO:0000269|PubMed:23727357}. Early endosome {ECO:0000250|UniProtKB:P19619}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P19619}; Peripheral membrane protein {ECO:0000250|UniProtKB:P19619}. Endosome membrane {ECO:0000250|UniProtKB:P07150}; Peripheral membrane protein {ECO:0000250|UniProtKB:P07150}. Secreted {ECO:0000269|PubMed:25664854}. Secreted, extracellular space {ECO:0000250|UniProtKB:P04083}. Cell membrane {ECO:0000250|UniProtKB:P04083}; Peripheral membrane protein {ECO:0000250|UniProtKB:P04083}; Extracellular side {ECO:0000250|UniProtKB:P04083}. Secreted, exosome {ECO:0000269|PubMed:25664854}. Cytoplasmic vesicle, secretory vesicle lumen {ECO:0000269|PubMed:25664854}. Cell projection, phagocytic cup {ECO:0000269|PubMed:21245195}. Note=Colocalizes with actin fibers at phagocytic cups (PubMed:21245195). Secreted, at least in part via exosomes and other secretory vesicles. Detected in exosomes and other extracellular vesicles (PubMed:25664854). Secretion is increased in response to wounding and inflammation (PubMed:25664854). Detected in gelatinase granules in resting neutrophils. Neutrophil adhesion to endothelial cells stimulates secretion via gelatinase granules, but foreign particle phagocytosis has no effect. Displays calcium-dependent binding to phospholipid membranes (By similarity). {ECO:0000250|UniProtKB:P04083, ECO:0000269|PubMed:25664854}. SUBUNIT: Homodimer; non-covalently linked (By similarity). Homodimer; linked by transglutamylation. Homodimers linked by transglutamylation are observed in placenta, but not in other tissues. Interacts with S100A11. Heterotetramer, formed by two molecules each of S100A11 and ANXA1 (By similarity). Interacts with DYSF (PubMed:14506282). Interacts with EGFR (By similarity). {ECO:0000250|UniProtKB:P04083, ECO:0000250|UniProtKB:P19619, ECO:0000269|PubMed:14506282}. DOMAIN: The full-length protein can bind eight Ca(2+) ions via the annexin repeats. Calcium binding causes a major conformation change that modifies dimer contacts and leads to surface exposure of the N-terminal phosphorylation sites; in the absence of Ca(2+), these sites are buried in the interior of the protein core. The N-terminal region becomes disordered in response to calcium-binding. {ECO:0000250|UniProtKB:P19619}.; DOMAIN: The N-terminal 26 amino acids are sufficient for its extracellular functions in the regulation of inflammation and wound healing. Acylated peptides that contain the first 26 amino acids of the mature protein can activate signaling via the formyl peptide receptors. {ECO:0000250|UniProtKB:P04083}. TISSUE SPECIFICITY: Detected in lung (PubMed:12475898, PubMed:17384087). Detected at the apical membrane of airway epithelial cells (PubMed:17384087). Detected in intestinal epithelial cells (PubMed:18802107). Detected in skeletal muscle (PubMed:14506282). Detected in prostate (PubMed:23727357). Detected in thymus (at protein level) (PubMed:12475898). Detected in stomach, lung, spleen, ovary and uterus, and at lower levels in kidney, thymus and heart (PubMed:12475898). {ECO:0000269|PubMed:12475898, ECO:0000269|PubMed:14506282, ECO:0000269|PubMed:17384087, ECO:0000269|PubMed:23727357}. +Q91ZK0 AP2D_MOUSE Transcription factor AP-2-delta (AP2-delta) (Activating enhancer-binding protein 2-delta) 452 49,548 Chain (1); Modified residue (1); Region (1); Sequence conflict (2) FUNCTION: Sequence-specific DNA-binding protein that interacts with inducible viral and cellular enhancer elements to regulate transcription of selected genes. AP-2 factors bind to the consensus sequence 5'-GCCNNNGGC-3' and activate genes involved in a large spectrum of important biological functions including proper eye, face, body wall, limb and neural tube development. They also suppress a number of genes including MCAM/MUC18, C/EBP alpha and MYC. {ECO:0000269|PubMed:11522791, ECO:0000305}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Binds DNA as a dimer. Can form homodimers or heterodimers with other AP-2 family members. {ECO:0000269|PubMed:11522791}. TISSUE SPECIFICITY: Expressed in both embryonic and newborn brain. {ECO:0000269|PubMed:11522791}. +Q3U1U7 AHRR_MOUSE Aryl hydrocarbon receptor repressor (AhR repressor) (AhRR) 701 77,726 Alternative sequence (2); Chain (1); Cross-link (2); Domain (2); Region (1); Sequence conflict (5) FUNCTION: Mediates dioxin toxicity and is involved in regulation of cell growth and differentiation. Represses the transcription activity of AHR by competing with this transcription factor for heterodimer formation with the ARNT and subsequently binding to the xenobiotic response element (XRE) sequence present in the promoter regulatory region of variety of genes. Represses CYP1A1 by binding the XRE sequence and recruiting ANKRA2, HDAC4 and/or HDAC5. Autoregulates its expression by associating with its own XRE site. {ECO:0000269|PubMed:17949687, ECO:0000269|PubMed:9887096}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9887096}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:9887096}. Note=Predominantly in the nuclear compartment. First cytoplasmic, translocates into the nuclear compartment upon interaction with ARNT in the cytoplasmic compartment. SUBUNIT: Interacts with ARNT, ANKRA2, HDAC4 and HDAC5. Interacts with ARNT; forms a heterodimer with ARNT (By similarity). {ECO:0000250|UniProtKB:A9YTQ3, ECO:0000269|PubMed:17949687, ECO:0000269|PubMed:9887096}. +Q8R0T6 AGRG3_MOUSE Adhesion G protein-coupled receptor G3 (G-protein coupled receptor 97) 542 60,072 Chain (1); Domain (1); Glycosylation (4); Sequence conflict (1); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 268 288 Helical; Name=1. {ECO:0000255}.; TRANSMEM 303 323 Helical; Name=2. {ECO:0000255}.; TRANSMEM 343 363 Helical; Name=3. {ECO:0000255}.; TRANSMEM 373 393 Helical; Name=4. {ECO:0000255}.; TRANSMEM 427 447 Helical; Name=5. {ECO:0000255}.; TRANSMEM 468 488 Helical; Name=6. {ECO:0000255}.; TRANSMEM 495 515 Helical; Name=7. {ECO:0000255}. TOPO_DOM 19 267 Extracellular. {ECO:0000305}.; TOPO_DOM 289 302 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 324 342 Extracellular. {ECO:0000305}.; TOPO_DOM 364 372 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 394 426 Extracellular. {ECO:0000305}.; TOPO_DOM 448 467 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 489 494 Extracellular. {ECO:0000305}.; TOPO_DOM 516 542 Cytoplasmic. {ECO:0000305}. FUNCTION: Orphan receptor that regulates migration of lymphatic endothelial cells via the small GTPases RhoA and CDC42 (By similarity). Regulates B-cell development (PubMed:24113187). Seems to signal through G-alpha(q)-proteins (By similarity). {ECO:0000250|UniProtKB:Q86Y34, ECO:0000269|PubMed:24113187}. SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q86Y34}; Multi-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Specifically expressed in intestinal lymphatic endothelium. {ECO:0000269|PubMed:24178298}. +Q6F3F9 AGRG6_MOUSE Adhesion G-protein coupled receptor G6 (Developmentally regulated G-protein-coupled receptor) (G-protein coupled receptor 126) [Cleaved into: ADGRG6 N-terminal fragment (ADGRG6-NTF); ADGRG6 C-terminal fragment (ADGRG6-CTF)] 1165 129,721 Chain (3); Compositional bias (1); Disulfide bond (3); Domain (3); Glycosylation (23); Modified residue (2); Motif (1); Region (3); Signal peptide (1); Site (2); Topological domain (8); Transmembrane (7) TRANSMEM 833 853 Helical; Name=1. {ECO:0000255}.; TRANSMEM 874 894 Helical; Name=2. {ECO:0000255}.; TRANSMEM 900 920 Helical; Name=3. {ECO:0000255}.; TRANSMEM 941 961 Helical; Name=4. {ECO:0000255}.; TRANSMEM 995 1015 Helical; Name=5. {ECO:0000255}.; TRANSMEM 1040 1060 Helical; Name=6. {ECO:0000255}.; TRANSMEM 1063 1083 Helical; Name=7. {ECO:0000255}. TOPO_DOM 31 832 Extracellular. {ECO:0000255}.; TOPO_DOM 854 873 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 895 899 Extracellular. {ECO:0000255}.; TOPO_DOM 921 940 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 962 994 Extracellular. {ECO:0000255}.; TOPO_DOM 1016 1039 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1061 1062 Extracellular. {ECO:0000255}.; TOPO_DOM 1084 1165 Cytoplasmic. {ECO:0000255}. FUNCTION: G-protein coupled receptor which is activated by type IV collagen, a major constituent of the basement membrane. Essential for normal differentiation of promyelinating Schwann cells and for normal myelination of axons these functions are mediated via G-protein-signaling pathways (PubMed:24227709, PubMed:21613327). Regulates also neural, cardiac and ear development via G-protein- and/or N-terminus-dependent signaling. May act as a receptor for PRNP which may promote myelin homeostasis (PubMed:27501152). {ECO:0000250|UniProtKB:C6KFA3, ECO:0000250|UniProtKB:Q86SQ4, ECO:0000269|PubMed:21613327, ECO:0000269|PubMed:24227709, ECO:0000269|PubMed:27501152}.; FUNCTION: ADGRG6 N-terminal fragment: Plays an important role in heart developmention (PubMed:24082093). Necessary and sufficient for axon sorting by Schwann cells independently of the ADGRG6-CTF (PubMed:25695270). {ECO:0000269|PubMed:24082093, ECO:0000269|PubMed:25695270}. PTM: Proteolytically cleaved into 2 conserved sites: one in the GPS domain (S1 site) and the other in the middle of the extracellular domain (S2 site). The proteolytic cleavage at S1 site generates an N-terminal fragment (NTF) and a seven-transmembrane-containing C-terminal fragment (CTF). The membrane-bound CTF can act as an independent receptor and the soluble NTF can act as a ligand or coreceptor. Furin is involved in the cleavage of the S2 site generating a soluble fragment. Processing at the GPS domain occurred independent of and probably prior to the cleavage at the S2 site. Proteolytic cleavage is required for activation of the receptor (By similarity). {ECO:0000250|UniProtKB:Q86SQ4}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q86SQ4}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Interacts with Laminin-2; this interaction stabilizes the receptor in an inactive state (PubMed:25695270). Laminin-2 polymerization could facilitate ADGRG6-NTF removal, thereby exposing the tethered agonist to drive myelination (PubMed:25695270). Interacts with PRNP (PubMed:27501152). {ECO:0000269|PubMed:25695270, ECO:0000269|PubMed:27501152}. TISSUE SPECIFICITY: Expressed at high levels in the heart, somite and otic vesicle during embryogenesis and in adult lung. {ECO:0000269|PubMed:15189448, ECO:0000269|PubMed:24082093}. +Q9Z0E3 AIRE_MOUSE Autoimmune regulator (Autoimmune polyendocrinopathy candidiasis ectodermal dystrophy protein homolog) (APECED protein homolog) 552 59,042 Alternative sequence (5); Chain (1); Domain (2); Motif (5); Mutagenesis (5); Zinc finger (2) FUNCTION: Transcription factor playing an essential role to promote self-tolerance in the thymus by regulating the expression of a wide array of self-antigens that have the commonality of being tissue-restricted in their expression pattern in the periphery, called tissue restricted antigens (TRA) (Probable). Binds to G-doublets in an A/T-rich environment; the preferred motif is a tandem repeat of 5'-. ATTGGTTA-3' combined with a 5'-TTATTA-3' box. Binds to nucleosomes (By similarity). Binds to chromatin and interacts selectively with histone H3 that is not methylated at 'Lys-4', not phosphorylated at 'Thr-3' and not methylated at 'Arg-2'. Functions as a sensor of histone H3 modifications that are important for the epigenetic regulation of gene expression. Mainly expressed by medullary thymic epithelial cells (mTECs), induces the expression of thousands of tissue-restricted proteins, which are presented on major histocompatibility complex class I (MHC-I) and MHC-II molecules to developing T-cells percolating through the thymic medulla (By similarity). Also induces self-tolerance through other mechanisms such as the regulation of the mTEC differentiation program (PubMed:19015306). Controls the medullary accumulation of thymic dendritic cells and the development of regulatory T-cell through the regulation of XCL1 expression (PubMed:21300913). Regulates the production of CCR4 and CCR7 ligands in medullary thymic epithelial cells and alters the coordinated maturation and migration of thymocytes (PubMed:19923453). In thimic B-cells, allows the presentation of licensing-dependent endogenous self-anitgen for negative selection (PubMed:26070482). In secondary lymphoid organs, induces functional inactivation of CD4(+) T-cells. Expressed by a distinct bone marrow-derived population, induces self-tolerance through a mechanism that does not require regulatory T-cells and is resitant to innate inflammatory stimuli (PubMed:23993652). {ECO:0000250|UniProtKB:O43918, ECO:0000269|PubMed:19015306, ECO:0000269|PubMed:19923453, ECO:0000269|PubMed:21300913, ECO:0000269|PubMed:23993652, ECO:0000269|PubMed:26070482, ECO:0000305|PubMed:19302042}. PTM: Phosphorylated. {ECO:0000269|PubMed:11533054}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00185, ECO:0000255|PROSITE-ProRule:PRU00747, ECO:0000269|PubMed:11156688, ECO:0000269|PubMed:19015306, ECO:0000269|PubMed:26070482}. Cytoplasm {ECO:0000269|PubMed:11156688}. Note=Predominantly nuclear but also cytoplasmic. Found in nuclear body-like structures (dots) and in a filamentous vimentin-like pattern. {ECO:0000250|UniProtKB:O43918, ECO:0000269|PubMed:19015306}. SUBUNIT: Homodimer and homotetramer. Interacts with CREBBP. Interacts preferentially with histone H3 that is not methylated at 'Lys-4'. Binds with lower affinity to histone H3 that is monomethylated at 'Lys-4'. Trimethylation of histone H3 at 'Lys-4' or phosphorylation at 'Thr-3' abolish the interaction. Binds with lower affinity to histone H3 that is acetylated at 'Lys-4', or that is acetylated at 'Lys-9' or trimethylated at 'Lys-9'. Binds histone H3 that is dimethylated at 'Arg-2' with very low affinity (By similarity). {ECO:0000250}. DOMAIN: Interacts via the first PHD domain with the N-terminus of histone H3 that is not methylated at 'Lys-4'. Disruption of the first PHD domain has been shown to lead to reduced transcriptional activity and to localization of the protein mainly in the cytoplasm in small granules. While the PHD zinc fingers are necessary for the transactivation capacity of the protein, other regions also modulate this function (By similarity). {ECO:0000250}.; DOMAIN: The L-X-X-L-L repeats may be implicated in binding to nuclear receptors.; DOMAIN: The N-terminal HSR domain is required for localization on tubular structures. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in a few cells in the medulla of the thymus (medullary epithelial cells) (at protein level) (PubMed:23993652). Expressed in thymic but no peripheral B-cells (PubMed:26070482). In secondary lymphoid organs, expressed in a discrete population of bone marrow-derived toleregenic antigen presenting cells (APCs) called extrathymic AIRE expressing cells (eTAC)(at protein level) (PubMed:23993652). Detected at very low levels in thymus, lymph node, liver, brain, ovary, lung, testis, kidney, heart, spleen, bone marrow, skeletal muscle and adrenal gland. Isoforms 1a to 1d predominate, isoforms 2a to 2d are intermediate and isoforms 3a to 3d are expressed at extremely low levels. {ECO:0000269|PubMed:23993652, ECO:0000269|PubMed:26070482}. +Q9DCT1 AKCL2_MOUSE 1,5-anhydro-D-fructose reductase (AF reductase) (EC 1.1.1.263) (Aldo-keto reductase family 1 member C-like protein 2) (Aldo-keto reductase family 1 member E1) (Aldo-keto reductase family 1 member E2) 301 34,461 Active site (1); Binding site (3); Chain (1); Nucleotide binding (1); Sequence conflict (2); Site (1) FUNCTION: Catalyzes the NADPH-dependent reduction of 1,5-anhydro-D-fructose (AF) to 1,5-anhydro-D-glucitol. {ECO:0000269|PubMed:18323634}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P82125}. +Q9DBE8 ALG2_MOUSE Alpha-1,3/1,6-mannosyltransferase ALG2 (EC 2.4.1.132) (EC 2.4.1.257) (Asparagine-linked glycosylation protein 2 homolog) (GDP-Man:Man(1)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase) (GDP-Man:Man(1)GlcNAc(2)-PP-dolichol mannosyltransferase) (GDP-Man:Man(2)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase) 415 47,405 Chain (1); Sequence conflict (2); Transmembrane (1) TRANSMEM 85 105 Helical. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Mannosylates Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q80UG6 ALKL2_MOUSE ALK and LTK ligand 2 (Protein FAM150B) 151 17,496 Chain (1); Erroneous initiation (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Ligand for receptor tyrosine kinases LTK and ALK. Stimulation of ALK signaling may be involved in regulation of cell proliferation and transformation. {ECO:0000250|UniProtKB:Q6UX46}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q8K1E6 ALKB3_MOUSE Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3 (EC 1.14.11.54) (Alkylated DNA repair protein alkB homolog 3) (mAbh3) 286 33,061 Binding site (3); Chain (1); Domain (1); Metal binding (3); Modified residue (2); Mutagenesis (2); Region (3) FUNCTION: Dioxygenase that mediates demethylation of DNA and RNA containing 1-methyladenosine (m1A) (By similarity). Repairs alkylated DNA containing 1-methyladenosine (m1A) and 3-methylcytosine (m3C) by oxidative demethylation (PubMed:16174769). Has a strong preference for single-stranded DNA (PubMed:16174769). Able to process alkylated m3C within double-stranded regions via its interaction with ASCC3, which promotes DNA unwinding to generate single-stranded substrate needed for ALKBH3. Also acts on RNA. Demethylates N(1)-methyladenosine (m1A) RNA, an epigenetic internal modification of messenger RNAs (mRNAs) highly enriched within 5'-untranslated regions (UTRs) and in the vicinity of start codons. Requires molecular oxygen, alpha-ketoglutarate and iron (By similarity). {ECO:0000250|UniProtKB:Q96Q83, ECO:0000269|PubMed:16174769}. PTM: Ubiquitinated; undergoes 'Lys-48'-linked polyubiquitination. OTUD4 promotes USP7 and USP9X-dependent deubiquitination of 'Lys-48'-polyubiquitinated ALKBH3 promoting the repair of alkylated DNA lesions. {ECO:0000250|UniProtKB:Q96Q83}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96Q83}. Cytoplasm {ECO:0000250|UniProtKB:Q96Q83}. Note=Colocalizes with ASCC2 and ASCC3 in nuclear foci when cells have been exposed to alkylating agents that cause DNA damage. Predominantly localizes to the nucleus. {ECO:0000250|UniProtKB:Q96Q83}. SUBUNIT: Interacts with the ASCC complex composed of ASCC1, ASCC2 and ASCC3. Interacts directly with ASCC3, and is thereby recruited to the ASCC complex. Interacts with OTUD4; the interaction is direct. Interacts with USP7 and USP9X. {ECO:0000250|UniProtKB:Q96Q83}. TISSUE SPECIFICITY: Detected in testis, kidney, liver and heart. {ECO:0000269|PubMed:16174769}. +Q920R0 ALS2_MOUSE Alsin (Amyotrophic lateral sclerosis 2 protein homolog) 1651 182,566 Alternative sequence (2); Chain (1); Domain (3); Modified residue (7); Repeat (13); Sequence conflict (8) FUNCTION: May act as a GTPase regulator. Controls survival and growth of spinal motoneurons. {ECO:0000250}. SUBUNIT: Forms a heteromeric complex with ALS2CL. Interacts with ALS2CL (By similarity). {ECO:0000250}. +Q9WVH6 ANGP4_MOUSE Angiopoietin-4 (ANG-4) (Angiopoietin-3) (ANG-3) 509 57,805 Chain (1); Coiled coil (1); Disulfide bond (2); Domain (1); Glycosylation (8); Signal peptide (1) FUNCTION: Binds to TEK/TIE2, modulating ANGPT1 signaling. Can induce tyrosine phosphorylation of TEK/TIE2. Promotes endothelial cell survival, migration and angiogenesis. {ECO:0000269|PubMed:15284220}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. SUBUNIT: Homodimer; disulfide-linked. Interacts with TEK/TIE2. {ECO:0000269|PubMed:15284220}. TISSUE SPECIFICITY: Widely expressed. +P18293 ANPRA_MOUSE Atrial natriuretic peptide receptor 1 (EC 4.6.1.2) (Atrial natriuretic peptide receptor type A) (ANP-A) (ANPR-A) (NPR-A) (Guanylate cyclase A) (GC-A) 1057 119,109 Binding site (3); Chain (1); Disulfide bond (3); Domain (2); Glycosylation (6); Modified residue (7); Sequence conflict (14); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 470 490 Helical. {ECO:0000255}. TOPO_DOM 29 469 Extracellular. {ECO:0000255}.; TOPO_DOM 491 1057 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for the atrial natriuretic peptide NPPA/ANP and the brain natriuretic peptide NPPB/BNP which are potent vasoactive hormones playing a key role in cardiovascular homeostasis. Has guanylate cyclase activity upon binding of the ligand. PTM: Phosphorylation of the protein kinase-like domain is required for full activation by ANP. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Homodimer. {ECO:0000250}. +Q9JHQ0 ANXA9_MOUSE Annexin A9 (Annexin XXXI) (Annexin-31) (Annexin-9) 345 38,110 Chain (1); Frameshift (1); Repeat (4); Sequence conflict (1) FUNCTION: May act as a low affinity receptor for acetylcholine. {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +Q8BH00 AL8A1_MOUSE 2-aminomuconic semialdehyde dehydrogenase (EC 1.2.1.32) (Aldehyde dehydrogenase family 8 member A1) (Retinal dehydrogenase 4) 487 53,664 Active site (2); Chain (1); Modified residue (1); Natural variant (1); Nucleotide binding (1); Site (1) Amino-acid degradation; L-kynurenine degradation. FUNCTION: Catalyzes the NAD-dependent oxidation of 2-aminomuconic semialdehyde of the kynurenine metabolic pathway in L-tryptophan degradation. {ECO:0000250|UniProtKB:Q9H2A2}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12519776}. TISSUE SPECIFICITY: Detected in hepatocytes and in proximal and distal convoluted tubules in kidney cortex (at protein level). Highly expressed in adult liver and in kidney cortex. First detected in embryonic liver after 15 days of development. {ECO:0000269|PubMed:12519776}. +Q8BGT5 ALAT2_MOUSE Alanine aminotransferase 2 (ALT2) (EC 2.6.1.2) (Glutamate pyruvate transaminase 2) (GPT 2) (Glutamic--alanine transaminase 2) (Glutamic--pyruvic transaminase 2) 522 57,944 Chain (1); Modified residue (4); Sequence conflict (3) Amino-acid degradation; L-alanine degradation via transaminase pathway; pyruvate from L-alanine: step 1/1. FUNCTION: Catalyzes the reversible transamination between alanine and 2-oxoglutarate to form pyruvate and glutamate. {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Specifically induced in fatty liver. Highly expressed in muscle, liver and white adipose tissue. Moderately expressed in brain and kidney and expressed at low levels in the heart. {ECO:0000269|PubMed:15122758}. +Q9D8C3 ALG13_MOUSE Putative bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase ALG13 (EC 2.4.1.141) (EC 3.4.19.12) (Asparagine-linked glycosylation 13 homolog) (Glycosyltransferase 28 domain-containing protein 1) (UDP-N-acetylglucosamine transferase subunit ALG13 homolog) 1166 128,664 Active site (3); Alternative sequence (2); Chain (1); Compositional bias (1); Domain (2); Erroneous gene model prediction (2); Region (2); Sequence conflict (1) FUNCTION: Isoform 1: Possible multifunctional enzyme with both glycosyltransferase and deubiquitinase activities.; FUNCTION: Isoform 2: May be involved in protein N-glycosylation, second step of the dolichol-linked oligosaccharide pathway (By. similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250}. Note=Could be recruited to the cytosolic face of the endoplasmic reticulum membrane through its interaction with ALG14. {ECO:0000250}. SUBUNIT: Isoform 2 may interact with ALG14. {ECO:0000250}. +Q8K2A8 ALG3_MOUSE Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase (EC 2.4.1.258) (Asparagine-linked glycosylation protein 3 homolog) (Dol-P-Man-dependent alpha(1-3)-mannosyltransferase) (Dolichyl-P-Man:Man(5)GlcNAc(2)-PP-dolichyl mannosyltransferase) (Dolichyl-phosphate-mannose--glycolipid alpha-mannosyltransferase) (Not56-like protein) 438 50,186 Chain (1); Modified residue (1); Sequence conflict (1); Transmembrane (11) TRANSMEM 41 61 Helical. {ECO:0000255}.; TRANSMEM 95 115 Helical. {ECO:0000255}.; TRANSMEM 123 143 Helical. {ECO:0000255}.; TRANSMEM 149 169 Helical. {ECO:0000255}.; TRANSMEM 172 192 Helical. {ECO:0000255}.; TRANSMEM 203 223 Helical. {ECO:0000255}.; TRANSMEM 231 251 Helical. {ECO:0000255}.; TRANSMEM 289 309 Helical. {ECO:0000255}.; TRANSMEM 332 352 Helical. {ECO:0000255}.; TRANSMEM 356 376 Helical. {ECO:0000255}.; TRANSMEM 407 427 Helical. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Adds the first Dol-P-Man derived mannose in an alpha-1,3 linkage to Man5GlcNAc2-PP-Dol. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +P97467 AMD_MOUSE Peptidyl-glycine alpha-amidating monooxygenase (PAM) [Includes: Peptidylglycine alpha-hydroxylating monooxygenase (PHM) (EC 1.14.17.3); Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (EC 4.3.2.5) (Peptidylamidoglycolate lyase) (PAL)] 979 108,963 Chain (1); Disulfide bond (7); Glycosylation (1); Metal binding (6); Modified residue (7); Propeptide (1); Region (3); Repeat (5); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 870 893 Helical. {ECO:0000255}. TOPO_DOM 35 869 Intragranular. {ECO:0000255}.; TOPO_DOM 894 979 Cytoplasmic. {ECO:0000255}. FUNCTION: Bifunctional enzyme that catalyzes 2 sequential steps in C-terminal alpha-amidation of peptides. The monooxygenase part produces an unstable peptidyl(2-hydroxyglycine) intermediate that is dismutated to glyoxylate and the corresponding desglycine peptide amide by the lyase part. C-terminal amidation of peptides such as neuropeptides is essential for full biological activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=Secretory granules. SUBUNIT: Monomer. Interacts with RASSF9 (By similarity). {ECO:0000250}. +Q8BVF9 AMZ1_MOUSE Archaemetzincin-1 (EC 3.4.-.-) (Archeobacterial metalloproteinase-like protein 1) 502 55,284 Active site (1); Chain (1); Erroneous initiation (1); Metal binding (6) FUNCTION: Zinc metalloprotease. Exhibits aminopeptidase activity against neurogranin in vitro. Does not hydrolyze angiotensin-2 (By similarity). {ECO:0000250}. +Q9R049 AMFR_MOUSE E3 ubiquitin-protein ligase AMFR (EC 2.3.2.27) (Autocrine motility factor receptor) (AMF receptor) (RING-type E3 ubiquitin transferase AMFR) 643 73,105 Alternative sequence (1); Chain (1); Domain (1); Modified residue (2); Region (1); Sequence conflict (1); Transmembrane (7); Zinc finger (1) TRANSMEM 82 102 Helical. {ECO:0000255}.; TRANSMEM 122 142 Helical. {ECO:0000255}.; TRANSMEM 186 206 Helical. {ECO:0000255}.; TRANSMEM 215 235 Helical. {ECO:0000255}.; TRANSMEM 254 274 Helical. {ECO:0000255}.; TRANSMEM 276 296 Helical. {ECO:0000255}.; TRANSMEM 429 449 Helical. {ECO:0000255}. Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that mediates the polyubiquitination of a number of proteins such as CD3D, CYP3A4, CFTR and APOB for proteasomal degradation. Component of a VCP/p97-AMFR/gp78 complex that participates in the final step of endoplasmic reticulum-associated degradation (ERAD). The VCP/p97-AMFR/gp78 complex is involved in the sterol-accelerated ERAD degradation of HMGCR through binding to the HMGCR-INSIG complex at the ER membrane and initiating ubiquitination of HMGCR. The ubiquitinated HMGCR is then released from the ER by the complex into the cytosol for subsequent destruction. Also regulates ERAD through the ubiquitination of UBL4A a component of the BAG6/BAT3 complex. Also acts as a scaffold protein to assemble a complex that couples ubiquitination, retranslocation and deglycosylation. Mediates tumor invasion and metastasis (By similarity). {ECO:0000250|UniProtKB:Q9UKV5, ECO:0000269|PubMed:16987818, ECO:0000269|PubMed:18216283}. PTM: Palmitoylation of the RING-type zing finger by ZDHHC6 promotes localization to the peripheral endoplasmic reticulum. {ECO:0000250|UniProtKB:Q9UKV5}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts (through a region distinct from the RING finger) with UBE2G2/UBC7. Interacts with DRL1. Interacts (via the VIM) with VCP/p97. Interacts (via its membrane domain) with INSIG1; the interaction initiates the sterol-mediated ubiquitination and degradation of HMGCR by the ERAD pathway (By similarity). Component of the VCP/p97-AMFR/gp78 complex that enhances VCP/p97 binding to polyubiquitinated proteins for their degradation by the endoplasmic reticulum-associated degradation (ERAD) pathway. Interacts (via the VIM) with VCP/p97. Interacts with RNF5. Also forms an ERAD complex containing VCP/p97, NGLY1; PSMC1; SAKS1 AND RAD23B required for coupling retrotranslocation, ubiquitination and deglycosylation. Interacts with BAG6. Interacts with USP13 (via UBA 2 domain); the interaction is direct (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9UKV5, ECO:0000269|PubMed:16709668, ECO:0000269|PubMed:16987818, ECO:0000269|PubMed:18216283}. DOMAIN: The CUE domain is required for recognition of misfolded proteins such as mutant CFTR.; DOMAIN: The VCP/p97-interacting motif (VIM) is sufficient for binding VCP/p97 to form a complex capable of transferring VCP/p97 from the cytosol to microsomes. TISSUE SPECIFICITY: Expressed in heart, brain, liver, lung, skeletal muscle, kidney and testis. Not detected in spleen. {ECO:0000269|PubMed:10456327}. +Q02357 ANK1_MOUSE Ankyrin-1 (ANK-1) (Erythrocyte ankyrin) 1862 204,227 Alternative sequence (9); Chain (1); Domain (3); Modified residue (35); Region (3); Repeat (23); Sequence conflict (8) FUNCTION: Attaches integral membrane proteins to cytoskeletal elements; binds to the erythrocyte membrane protein band 4.2, to Na-K ATPase, to the lymphocyte membrane protein GP85, and to the cytoskeletal proteins fodrin, tubulin, vimentin and desmin. Erythrocyte ankyrins also link spectrin (beta chain) to the cytoplasmic domain of the erythrocytes anion exchange protein; they retain most or all of these binding functions. In skeletal muscle, isoform Mu7 together with obscurin may provide a molecular link between the sarcoplasmic reticulum and myofibrils. PTM: Regulated by phosphorylation. {ECO:0000250}.; PTM: Acylated by palmitic acid group(s). {ECO:0000250}.; PTM: Hydroxylated by HIF1AN at several asparagine and 1 aspartate residue within ANK repeat region; hydroxylation seems to increase the conformational stability of this region and may also modulate protein-protein interactions mediated by the ANK repeat region. {ECO:0000250}. SUBCELLULAR LOCATION: Isoform Er1: Cytoplasm, cytoskeleton {ECO:0000250}. Note=Probably the other erythrocyte (Er) isoforms, are located near the surface of erythrocytic plasma membrane. {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform Mu7: Membrane {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform Mu8: Sarcoplasmic reticulum {ECO:0000250}. SUBUNIT: Interacts with a number of integral membrane proteins and cytoskeletal proteins. Interacts (via N-terminus) with SPTB/spectrin (beta chain). Interacts (via N-terminus ANK repeats) with SLC4A1/erythrocyte membrane protein band 3 (via cytoplasmic N-terminus). Also interacts with TTN/titin. Isoform Mu17 interacts with OBSCN isoform 3/obscurin. Interacts with HIF1AN (By similarity). {ECO:0000250}. DOMAIN: The 55 kDa regulatory domain is involved in regulating binding of SPTB/spectrin (beta chain) and SLC4A1/erythrocyte membrane protein band 3. {ECO:0000250}.; DOMAIN: The ANK repeat region forms a spiral around a large central cavity and is involved in binding of ion transporters. {ECO:0000250}.; DOMAIN: The tandem configuration of the two ZU5 and the UPA domains forms a structural supramodule termed ZZU. ZU5-1 mediates interaction with beta-spectrin, and the ZU5-1/UPA interface is required for ankyrin's function other than binding to spectrin (By similarity). {ECO:0000250}. +P05125 ANF_MOUSE Natriuretic peptides A (Prepronatriodilatin) [Cleaved into: Atrial natriuretic factor (ANF) (Atrial natriuretic peptide) (ANP); Auriculin-B; Auriculin-A; Atriopeptin-1 (Atriopeptin I); Atriopeptin-2 (Atriopeptin II)] 152 16,572 Disulfide bond (1); Mutagenesis (3); Peptide (5); Propeptide (1); Sequence conflict (1); Signal peptide (1); Site (2) FUNCTION: Hormone playing a key role in cardiovascular homeostasis through regulation of natriuresis, diuresis, and vasodilation. Also plays a role in female pregnancy by promoting trophoblast invasion and spiral artery remodeling in uterus. Specifically binds and stimulates the cGMP production of the NPR1 receptor. Binds the clearance receptor NPR3. {ECO:0000269|PubMed:12890708, ECO:0000269|PubMed:22437503, ECO:0000269|PubMed:8760210}. PTM: Cleaved by CORIN upon secretion to produce the functional hormone. {ECO:0000269|PubMed:11884416, ECO:0000269|PubMed:15637153}.; PTM: Atrial natriuretic factor: Cleaved by MME. The cleavage initiates degradation of the factor and thereby regulate its activity. {ECO:0000250|UniProtKB:P01160}. SUBCELLULAR LOCATION: Secreted. +Q6GQX6 ANKS6_MOUSE Ankyrin repeat and SAM domain-containing protein 6 (SamCystin) (Sterile alpha motif domain-containing protein 6) (SAM domain-containing protein 6) 883 93,474 Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (1); Modified residue (3); Repeat (10) FUNCTION: Required for renal function. {ECO:0000250|UniProtKB:Q68DC2}. PTM: Hydroxylated at Asn-129, most probably by HIF1AN. This hydroxylation results in decreased NEK8-binding. {ECO:0000250|UniProtKB:P0C0T2}. SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000269|PubMed:23793029}. Cytoplasm {ECO:0000250|UniProtKB:P0C0T2}. Note=Localizes to the proximal region of the primary cilium in the presence of INVS. {ECO:0000269|PubMed:23793029}. SUBUNIT: Homooligomer (By similarity). Central component of a complex containing at least ANKS6, INVS, NEK8 and NPHP3. ANKS6 may organize complex assembly by linking INVS and NPHP3 to NEK8 and INVS may target the complex to the proximal ciliary axoneme (By similarity). Interacts (via SAM domain) with BICC1 (via KH domains) in an RNA-dependent manner (By similarity). Interacts with ANKS3 (PubMed:25671767). {ECO:0000250|UniProtKB:P0C0T2, ECO:0000269|PubMed:25671767}. DOMAIN: The ankyrin repeats are necessary and sufficient for NEK8-binding. {ECO:0000250|UniProtKB:P0C0T2}.; DOMAIN: The SAM domain mediates interaction with the SAM domain of ANKS3. {ECO:0000250|UniProtKB:P0C0T2}. TISSUE SPECIFICITY: Expressed in kidney (at protein level). {ECO:0000269|PubMed:23793029}. +Q6PB70 ANO8_MOUSE Anoctamin-8 (Transmembrane protein 16H) 1060 119,101 Chain (1); Compositional bias (4); Erroneous initiation (1); Glycosylation (1); Initiator methionine (1); Modified residue (7); Sequence conflict (1); Topological domain (9); Transmembrane (8) TRANSMEM 245 265 Helical. {ECO:0000255}.; TRANSMEM 282 302 Helical. {ECO:0000255}.; TRANSMEM 357 377 Helical. {ECO:0000255}.; TRANSMEM 401 421 Helical. {ECO:0000255}.; TRANSMEM 438 458 Helical. {ECO:0000255}.; TRANSMEM 746 766 Helical. {ECO:0000255}.; TRANSMEM 803 823 Helical. {ECO:0000255}.; TRANSMEM 837 857 Helical. {ECO:0000255}. TOPO_DOM 2 244 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 266 281 Extracellular. {ECO:0000255}.; TOPO_DOM 303 356 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 378 400 Extracellular. {ECO:0000255}.; TOPO_DOM 422 437 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 459 745 Extracellular. {ECO:0000255}.; TOPO_DOM 767 802 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 824 836 Extracellular. {ECO:0000255}.; TOPO_DOM 858 1060 Cytoplasmic. {ECO:0000255}. FUNCTION: Does not exhibit calcium-activated chloride channel (CaCC) activity. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Note=Shows predominantly an intracellular localization with a weak expression in the cell membrane. {ECO:0000250}. TISSUE SPECIFICITY: Predominant expression seen in epithelial tissues. {ECO:0000269|PubMed:20056604}. +Q8VDL4 ADPGK_MOUSE ADP-dependent glucokinase (ADP-GK) (ADPGK) (EC 2.7.1.147) 496 53,902 Active site (1); Alternative sequence (3); Beta strand (20); Chain (1); Domain (1); Helix (17); Metal binding (3); Sequence conflict (3); Signal peptide (1); Turn (4) Carbohydrate degradation; glycolysis. FUNCTION: Catalyzes the phosphorylation of D-glucose to D-glucose 6-phosphate using ADP as the phosphate donor. GDP and CDP can replace ADP, but with reduced efficiency. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. SUBUNIT: Monomer. {ECO:0000269|PubMed:14975750}. +Q8N9S3 AHSA2_MOUSE Activator of 90 kDa heat shock protein ATPase homolog 2 331 37,648 Alternative sequence (2); Chain (1); Erroneous initiation (1); Sequence conflict (4) FUNCTION: Co-chaperone that stimulates HSP90 ATPase activity. {ECO:0000250|UniProtKB:Q12449}. +O70200 AIF1_MOUSE Allograft inflammatory factor 1 (AIF-1) (Ionized calcium-binding adapter molecule 1) 147 16,911 Beta strand (1); Calcium binding (2); Chain (1); Domain (2); Helix (7); Initiator methionine (1); Modified residue (2) FUNCTION: Actin-binding protein that enhances membrane ruffling and RAC activation. Enhances the actin-bundling activity of LCP1. Binds calcium. Plays a role in RAC signaling and in phagocytosis. May play a role in macrophage activation and function. Promotes the proliferation of vascular smooth muscle cells and of T-lymphocytes. Enhances lymphocyte migration. Plays a role in vascular inflammation. {ECO:0000269|PubMed:10934045, ECO:0000269|PubMed:11500035, ECO:0000269|PubMed:11722645, ECO:0000269|PubMed:11916959, ECO:0000269|PubMed:14756805}. PTM: Phosphorylated on serine residues. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10934045}. Cell projection, ruffle membrane {ECO:0000269|PubMed:10934045, ECO:0000269|PubMed:14756805}; Peripheral membrane protein; Cytoplasmic side. Cell projection, phagocytic cup {ECO:0000269|PubMed:10934045, ECO:0000269|PubMed:14756805}. Note=Associated with the actin cytoskeleton at membrane ruffles and at sites of phagocytosis. {ECO:0000269|PubMed:10934045}. SUBUNIT: Homodimer (Potential). Monomer. Interacts with LCP1. {ECO:0000269|PubMed:14756805, ECO:0000269|PubMed:17011575, ECO:0000305}. TISSUE SPECIFICITY: Abundantly expressed in the testis, moderately in the spleen and lymph nodes and at low levels in the liver and thymus. Detected in macrophages. {ECO:0000269|PubMed:11722645}. +Q80Y20 ALKB8_MOUSE Alkylated DNA repair protein alkB homolog 8 (EC 1.14.11.-) (Probable alpha-ketoglutarate-dependent dioxygenase ABH8) (S-adenosyl-L-methionine-dependent tRNA methyltransferase ABH8) (tRNA (carboxymethyluridine(34)-5-O)-methyltransferase ABH8) (EC 2.1.1.-) (EC 2.1.1.229) 664 74,768 Alternative sequence (3); Binding site (2); Chain (1); Domain (2); Frameshift (1); Metal binding (7); Mutagenesis (2); Region (2); Sequence conflict (3) FUNCTION: Catalyzes the methylation of 5-carboxymethyl uridine to 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in tRNA via its methyltransferase domain (PubMed:20123966). Catalyzes the last step in the formation of 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in target tRNA (PubMed:20123966). Has a preference for tRNA(Arg) and tRNA(Glu), and does not bind tRNA(Lys) (By similarity). Binds tRNA and catalyzes the iron and alpha-ketoglutarate dependent hydroxylation of 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in tRNA via its dioxygenase domain, giving rise to 5-(S)-methoxycarbonylhydroxymethyluridine; has a preference for tRNA(Gly) (PubMed:20583019). Required for normal survival after DNA damage (By similarity). May inhibit apoptosis and promote cell survival and angiogenesis (By similarity). {ECO:0000250|UniProtKB:Q96BT7, ECO:0000269|PubMed:20123966, ECO:0000269|PubMed:20583019}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96BT7}. Nucleus {ECO:0000250|UniProtKB:Q96BT7}. Note=Predominantly cytoplasmic. {ECO:0000250|UniProtKB:Q96BT7}. SUBUNIT: Interacts with TRMT112. {ECO:0000250|UniProtKB:Q96BT7}. DOMAIN: The Fe2OG dioxygenase domain does not have demethylase activity with methylated nucleotides. {ECO:0000269|PubMed:20583019}. +P31750 AKT1_MOUSE RAC-alpha serine/threonine-protein kinase (EC 2.7.11.1) (AKT1 kinase) (Protein kinase B) (PKB) (Protein kinase B alpha) (PKB alpha) (Proto-oncogene c-Akt) (RAC-PK-alpha) (Thymoma viral proto-oncogene) 480 55,707 Active site (1); Binding site (7); Chain (1); Cross-link (1); Disulfide bond (2); Domain (3); Glycosylation (5); Modified residue (11); Mutagenesis (4); Nucleotide binding (1); Region (3); Sequence conflict (1) FUNCTION: AKT1 is one of 3 closely related serine/threonine-protein kinases (AKT1, AKT2 and AKT3) called the AKT kinase, and which regulate many processes including metabolism, proliferation, cell survival, growth and angiogenesis. This is mediated through serine and/or threonine phosphorylation of a range of downstream substrates. Over 100 substrate candidates have been reported so far, but for most of them, no isoform specificity has been reported. AKT is responsible of the regulation of glucose uptake by mediating insulin-induced translocation of the SLC2A4/GLUT4 glucose transporter to the cell surface. Phosphorylation of PTPN1 at 'Ser-50' negatively modulates its phosphatase activity preventing dephosphorylation of the insulin receptor and the attenuation of insulin signaling. Phosphorylation of TBC1D4 triggers the binding of this effector to inhibitory 14-3-3 proteins, which is required for insulin-stimulated glucose transport. AKT regulates also the storage of glucose in the form of glycogen by phosphorylating GSK3A at 'Ser-21' and GSK3B at 'Ser-9', resulting in inhibition of its kinase activity. Phosphorylation of GSK3 isoforms by AKT is also thought to be one mechanism by which cell proliferation is driven. AKT regulates also cell survival via the phosphorylation of MAP3K5 (apoptosis signal-related kinase). Phosphorylation of 'Ser-83' decreases MAP3K5 kinase activity stimulated by oxidative stress and thereby prevents apoptosis. AKT mediates insulin-stimulated protein synthesis by phosphorylating TSC2 at 'Ser-939' and 'Thr-1462', thereby activating mTORC1 signaling and leading to both phosphorylation of 4E-BP1 and in activation of RPS6KB1. AKT is involved in the phosphorylation of members of the FOXO factors (Forkhead family of transcription factors), leading to binding of 14-3-3 proteins and cytoplasmic localization. In particular, FOXO1 is phosphorylated at 'Thr-24', 'Ser-256' and 'Ser-319'. FOXO3 and FOXO4 are phosphorylated on equivalent sites. AKT has an important role in the regulation of NF-kappa-B-dependent gene transcription and positively regulates the activity of CREB1 (cyclic AMP (cAMP)-response element binding protein). The phosphorylation of CREB1 induces the binding of accessory proteins that are necessary for the transcription of pro-survival genes such as BCL2 and MCL1. AKT phosphorylates 'Ser-454' on ATP citrate lyase (ACLY), thereby potentially regulating ACLY activity and fatty acid synthesis. Activates the 3B isoform of cyclic nucleotide phosphodiesterase (PDE3B) via phosphorylation of 'Ser-273', resulting in reduced cyclic AMP levels and inhibition of lipolysis. Phosphorylates PIKFYVE on 'Ser-318', which results in increased PI(3)P-5 activity. The Rho GTPase-activating protein DLC1 is another substrate and its phosphorylation is implicated in the regulation cell proliferation and cell growth. AKT plays a role as key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation. Signals downstream of phosphatidylinositol 3-kinase (PI(3)K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I). AKT mediates the antiapoptotic effects of IGF-I. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. May be involved in the regulation of the placental development. Phosphorylates STK4/MST1 at 'Thr-120' and 'Thr-387' leading to inhibition of its: kinase activity, nuclear translocation, autophosphorylation and ability to phosphorylate FOXO3. Phosphorylates STK3/MST2 at 'Thr-117' and 'Thr-384' leading to inhibition of its: cleavage, kinase activity, autophosphorylation at Thr-180, binding to RASSF1 and nuclear translocation. Phosphorylates SRPK2 and enhances its kinase activity towards SRSF2 and ACIN1 and promotes its nuclear translocation (By similarity). Phosphorylates RAF1 at 'Ser-259' and negatively regulates its activity (By similarity). Phosphorylates KAT6A at 'Thr-369' and this phosphorylation inhibits the interaction of KAT6A with PML and negatively regulates its acetylation activity towards p53/TP53 (By similarity). {ECO:0000250}.; FUNCTION: AKT1-specific substrates have been recently identified, including palladin (PALLD), which phosphorylation modulates cytoskeletal organization and cell motility; prohibitin (PHB), playing an important role in cell metabolism and proliferation; and CDKN1A, for which phosphorylation at 'Thr-145' induces its release from CDK2 and cytoplasmic relocalization. These recent findings indicate that the AKT1 isoform has a more specific role in cell motility and proliferation. Phosphorylates CLK2 thereby controlling cell survival to ionizing radiation. {ECO:0000269|PubMed:10454575, ECO:0000269|PubMed:11282895, ECO:0000269|PubMed:11579209, ECO:0000269|PubMed:11994271, ECO:0000269|PubMed:12783884, ECO:0000269|PubMed:18288188, ECO:0000269|PubMed:19778506, ECO:0000269|PubMed:20333297, ECO:0000269|PubMed:22057101, ECO:0000269|PubMed:9415393}. PTM: O-GlcNAcylation at Thr-305 and Thr-312 inhibits activating phosphorylation at Thr-308 via disrupting the interaction between AKT1 and PDPK1. O-GlcNAcylation at Ser-473 also probably interferes with phosphorylation at this site (By similarity). {ECO:0000250}.; PTM: Phosphorylation on Thr-308, Ser-473 and Tyr-474 is required for full activity. Activated TNK2 phosphorylates it on Tyr-176 resulting in its binding to the anionic plasma membrane phospholipid PA. This phosphorylated form localizes to the plasma membrane, where it is targeted by PDPK1 and PDPK2 for further phosphorylations on Thr-308 and Ser-473 leading to its activation. Ser-473 phosphorylation by mTORC2 favors Thr-308 phosphorylation by PDPK1. Phosphorylated at Thr-308 and Ser-473 by IKBKE and TBK1. Ser-473 phosphorylation is enhanced by signaling through activated FLT3. Dephosphorylated at Thr-308 and Ser-473 by PP2A phosphatase. The phosphorylated form of PPP2R5B is required for bridging AKT1 with PP2A phosphatase. Ser-473 is dephosphorylated by CPPED1, leading to termination of signaling (By similarity). {ECO:0000250}.; PTM: Ubiquitinated; undergoes both 'Lys-48'- and 'Lys-63'-linked polyubiquitination. TRAF6-induced 'Lys-63'-linked AKT1 ubiquitination is critical for phosphorylation and activation. When ubiquitinated, it translocates to the plasma membrane, where it becomes phosphorylated. When fully phosphorylated and translocated into the nucleus, undergoes 'Lys-48'-polyubiquitination catalyzed by TTC3, leading to its degradation by the proteasome. Also ubiquitinated by TRIM13 leading to its proteasomal degradation. Ubiquitinated via 'Lys-48'-linked polyubiquitination by ZNRF1, leading to its degradation by the proteasome. Phosphorylated, undergoes 'Lys-48'-linked polyubiquitination preferentially at Lys-284 catalyzed by MUL1, leading to its proteasomal degradation. {ECO:0000269|PubMed:11090077, ECO:0000269|PubMed:12783884, ECO:0000269|PubMed:15753085, ECO:0000269|PubMed:18288188, ECO:0000269|PubMed:20333297, ECO:0000269|PubMed:21045808, ECO:0000269|PubMed:21262971, ECO:0000269|PubMed:22057101}.; PTM: Acetylated on Lys-14 and Lys-20 by the histone acetyltransferases EP300 and KAT2B. Acetylation results in reduced phosphorylation and inhibition of activity. Deacetylated at Lys-14 and Lys-20 by SIRT1. SIRT1-mediated deacetylation relieves the inhibition (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18388859, ECO:0000269|PubMed:19028694, ECO:0000269|PubMed:20189988}. Nucleus {ECO:0000269|PubMed:18388859, ECO:0000269|PubMed:20189988}. Cell membrane {ECO:0000269|PubMed:19028694}. Note=Nucleus after activation by integrin-linked protein kinase 1 (ILK1) (By similarity). Nuclear translocation is enhanced by interaction with TCL1A. Phosphorylation on Tyr-176 by TNK2 results in its localization to the cell membrane where it is targeted for further phosphorylations on Thr-308 and Ser-473 leading to its activation and the activated form translocates to the nucleus. Colocalizes with WDFY2 in intracellular vesicles. {ECO:0000250|UniProtKB:P31749}. SUBUNIT: Interacts with and phosphorylated by PDPK1 (By similarity). Interacts with AGAP2 (isoform 2/PIKE-A); the interaction occurs in the presence of guanine nucleotides. Interacts with AKTIP. Interacts (via PH domain) with MTCP1, TCL1A AND TCL1B. Interacts with CDKN1B; the interaction phosphorylates CDKN1B promoting 14-3-3 binding and cell-cycle progression. Interacts with MAP3K5 and TRAF6. Interacts with BAD, PPP2R5B, STK3 and STK4. Interacts (via PH domain) with SIRT1. Interacts with SRPK2 in a phosphorylation-dependent manner. Interacts with TRIM13; the interaction ubiquitinates AKT1 leading to its proteasomal degradation. Interacts with RAF1 (By similarity). Interacts (via the C-terminus) with CCDC88A (via its C-terminus) and THEM4 (via its C-terminus). Interacts with GRB10; the interaction leads to GRB10 phosphorylation thus promoting YWHAE-binding. Interacts with KCTD20 (PubMed:24156551). Interacts with BTBD10 (PubMed:18160256). Interacts with PA2G4 (By similarity). Interacts with KIF14; the interaction is detected in the plasma membrane upon INS stimulation and promotes AKT1 phosphorylation (By similarity). Interacts with FAM83B; activates the PI3K/AKT signaling cascade (By similarity). Interacts with WDFY2 (via WD repeats 1-3) (PubMed:16792529, PubMed:20189988). Forms a complex with WDFY2 and FOXO1 (PubMed:18388859). Interacts with FAM168A (By similarity). Interacts with SYAP1 (via phosphorylated form and BSD domain); this interaction is enhanced in a mTORC2-mediated manner in response to epidermal growth factor (EGF) stimulation and activates AKT1 (PubMed:23300339). Interacts with PKHM3 (PubMed:19028694). {ECO:0000250|UniProtKB:P31749, ECO:0000250|UniProtKB:P47196, ECO:0000269|PubMed:11598301, ECO:0000269|PubMed:15722337, ECO:0000269|PubMed:15753085, ECO:0000269|PubMed:16792529, ECO:0000269|PubMed:18160256, ECO:0000269|PubMed:18388859, ECO:0000269|PubMed:19028694, ECO:0000269|PubMed:20074525, ECO:0000269|PubMed:20189988, ECO:0000269|PubMed:20333297, ECO:0000269|PubMed:23300339, ECO:0000269|PubMed:24156551}. DOMAIN: Binding of the PH domain to phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P3) following phosphatidylinositol 3-kinase alpha (PIK3CA) activity results in its targeting to the plasma membrane. The PH domain mediates interaction with TNK2 and Tyr-176 is also essential for this interaction.; DOMAIN: The AGC-kinase C-terminal mediates interaction with THEM4. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. Low levels found in liver with slightly higher levels present in thymus and testis. {ECO:0000269|PubMed:8437858}. +Q6NS69 AMER3_MOUSE APC membrane recruitment protein 3 (Amer3) (Protein FAM123C) 780 83,159 Chain (1) FUNCTION: Regulator of the canonical Wnt signaling pathway. Acts by specifically binding phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), translocating to the cell membrane (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Translocates to the cell membrane following binding to PtdIns(4,5)P2. {ECO:0000250}. +P86044 ANO9_MOUSE Anoctamin-9 (Transmembrane protein 16J) 747 87,180 Chain (1); Glycosylation (4); Topological domain (9); Transmembrane (8) TRANSMEM 194 214 Helical. {ECO:0000255}.; TRANSMEM 260 280 Helical. {ECO:0000255}.; TRANSMEM 327 347 Helical. {ECO:0000255}.; TRANSMEM 365 385 Helical. {ECO:0000255}.; TRANSMEM 415 435 Helical. {ECO:0000255}.; TRANSMEM 544 564 Helical. {ECO:0000255}.; TRANSMEM 596 616 Helical. {ECO:0000255}.; TRANSMEM 696 716 Helical. {ECO:0000255}. TOPO_DOM 1 193 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 215 259 Extracellular. {ECO:0000255}.; TOPO_DOM 281 326 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 348 364 Extracellular. {ECO:0000255}.; TOPO_DOM 386 414 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 436 543 Extracellular. {ECO:0000255}.; TOPO_DOM 565 595 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 617 695 Extracellular. {ECO:0000255}.; TOPO_DOM 717 747 Cytoplasmic. {ECO:0000255}. FUNCTION: Has calcium-dependent phospholipid scramblase activity; scrambles phosphatidylserine, phosphatidylcholine and galactosylceramide. Does not exhibit calcium-activated chloride channel (CaCC) activity. Can inhibit the activity of ANO1 (By similarity). {ECO:0000250|UniProtKB:A1A5B4, ECO:0000269|PubMed:23532839}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Note=Shows predominantly an intracellular localization with a weak expression in the cell membrane. {ECO:0000250}. TISSUE SPECIFICITY: Predominant expression seen in epithelial tissues. {ECO:0000269|PubMed:20056604, ECO:0000269|PubMed:23532839}. +Q3TMQ6 ANG4_MOUSE Angiogenin-4 (EC 3.1.27.-) 144 16,425 Active site (2); Beta strand (8); Binding site (1); Chain (1); Disulfide bond (3); Helix (5); Motif (1); Mutagenesis (5); Region (1); Sequence conflict (16); Signal peptide (1); Turn (2) FUNCTION: Has bactericidal activity against E.faecalis and L.monocytogenes, but not against L.innocua and E.coli. Promotes angiogenesis (in vitro). Has low ribonuclease activity (in vitro). Promotes proliferation of melanoma cells, but not of endothelial cells or fibroblasts (in vitro). {ECO:0000269|PubMed:12548285, ECO:0000269|PubMed:17279775}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle lumen {ECO:0000269|PubMed:12548285}. Secreted {ECO:0000250|UniProtKB:P10152}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P03950}. Note=Exposure to bacterial lipopolysaccharide (LPS) triggers secretion from intestinal epithelium cells (PubMed:12548285). Rapidly endocytosed by target cells and translocated to the nucleus where it accumulates in the nucleolus and binds to DNA (By similarity). {ECO:0000250|UniProtKB:P03950, ECO:0000269|PubMed:12548285}. TISSUE SPECIFICITY: Detected in small intestine, caecum and colon, with the highest expression in Paneth cells in the intestinal epithelium. {ECO:0000269|PubMed:12548285}. +Q3V0J4 ANR53_MOUSE Ankyrin repeat domain-containing protein 53 497 56,738 Chain (1); Coiled coil (1); Repeat (3); Sequence conflict (1) FUNCTION: Required for normal progression through mitosis. Involved in chromosome alignment and cytokinesis via regulation of microtubules polymerization. {ECO:0000250|UniProtKB:Q8N9V6}. PTM: Phosphorylated during mitosis. {ECO:0000250|UniProtKB:Q8N9V6}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q8N9V6}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q8N9V6}. Note=Localizes at the spindle around the centrosome at prophase and prometaphase and at the spindle poles at metaphase and anaphase. {ECO:0000250|UniProtKB:Q8N9V6}. SUBUNIT: Interacts with PSRC1; recruited by PSRC1 to the spindle during mitosis. {ECO:0000250|UniProtKB:Q8N9V6}. +Q8K298 ANLN_MOUSE Anillin 1121 122,794 Chain (1); Coiled coil (1); Domain (1); Erroneous initiation (2); Modified residue (29); Region (5); Sequence conflict (2) FUNCTION: Required for cytokinesis. Essential for the structural integrity of the cleavage furrow and for completion of cleavage furrow ingression. Plays a role in bleb assembly during metaphase and anaphase of mitosis. May play a significant role in podocyte cell migration. {ECO:0000250|UniProtKB:Q9NQW6}. PTM: Phosphorylated during mitosis. {ECO:0000250}.; PTM: Ubiquitinated, and this requires FZR1/CDH1. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q9NQW6}. Cell projection, bleb {ECO:0000250|UniProtKB:Q9NQW6}. Note=Mainly found in the nucleus during interphase. Colocalizes with cortical F-actin upon nuclear envelope breakdown in mitosis and subsequently concentrates in the area of the prospective contractile ring in anaphase. This pattern persists until telophase, when the protein becomes concentrated in the midbody. {ECO:0000250|UniProtKB:Q9NQW6}. SUBUNIT: Interacts with F-actin. Interacts with CD2AP. May interact with RHOA. Interacts with FZR1/CDH1 during mitotic exit. {ECO:0000250|UniProtKB:Q9NQW6}. +Q9CR42 ANKR1_MOUSE Ankyrin repeat domain-containing protein 1 (Cardiac ankyrin repeat protein) 319 36,004 Chain (1); Coiled coil (1); Repeat (5); Sequence conflict (5) FUNCTION: May play an important role in endothelial cell activation. May act as a nuclear transcription factor that negatively regulates the expression of cardiac genes. {ECO:0000269|PubMed:9043061}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with TTN/titin and YBX1. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in heart, cardiac muscle. {ECO:0000269|PubMed:9043061}. +O35640 ANXA8_MOUSE Annexin A8 (Annexin VIII) (Annexin-8) 327 36,724 Chain (1); Metal binding (4); Repeat (4); Sequence conflict (5) FUNCTION: This protein is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade. {ECO:0000250}. DOMAIN: A pair of annexin repeats may form one binding site for calcium and phospholipid. +P34056 AP2A_MOUSE Transcription factor AP-2-alpha (AP2-alpha) (AP-2 transcription factor) (Activating enhancer-binding protein 2-alpha) (Activator protein 2) (AP-2) 437 47,971 Alternative sequence (3); Chain (1); Compositional bias (1); Cross-link (4); Modified residue (1); Motif (1); Region (1); Sequence conflict (5) FUNCTION: Sequence-specific DNA-binding protein that interacts with inducible viral and cellular enhancer elements to regulate transcription of selected genes. AP-2 factors bind to the consensus sequence 5'-GCCNNNGGC-3' and activate genes involved in a large spectrum of important biological functions including proper eye, face, body wall, limb and neural tube development. They also suppress a number of genes including MCAM/MUC18, C/EBP alpha and MYC. AP-2-alpha is the only AP-2 protein required for early morphogenesis of the lens vesicle. Together with the CITED2 coactivator, stimulates the PITX2 P1 promoter transcription activation. Associates with chromatin to the PITX2 P1 promoter region. {ECO:0000269|PubMed:15475956}. PTM: Sumoylated on Lys-10; which inhibits transcriptional activity. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Binds DNA as a dimer. Can form homodimers or heterodimers with other AP-2 family members. Interacts with WWOX. Interacts with UBE2I. Interacts with RALBP1 in a complex also containing EPN1 and NUMB during interphase and mitosis (By similarity). Interacts with CITED4. Interacts with KCTD1; this interaction represses transcription activation. Interacts (via C-terminus) with CITED2 (via C-terminus); the interaction stimulates TFAP2A-transcriptional activation. Interacts (via N-terminus) with EP300 (via N-terminus); the interaction requires CITED2 (By similarity). Interacts with KCTD15; this interaction inhibits TFAP2A transcriptional activation (By similarity). {ECO:0000250}. DOMAIN: The PPxY motif mediates interaction with WWOX. {ECO:0000250}. +Q3TY86 AIFM3_MOUSE Apoptosis-inducing factor 3 (EC 1.-.-.-) (Apoptosis-inducing factor-like protein) 605 66,792 Alternative sequence (3); Binding site (5); Chain (1); Domain (1); Metal binding (4); Nucleotide binding (1); Sequence conflict (1) FUNCTION: Induces apoptosis through a caspase dependent pathway. Reduces mitochondrial membrane potential (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion. Note=Does not translocate to the nucleus upon induction of apoptosis. {ECO:0000250}. DOMAIN: The Rieske domain induces apoptosis. {ECO:0000250}. +Q9D8B1 AIG1_MOUSE Androgen-induced gene 1 protein (AIG-1) 262 29,754 Alternative sequence (2); Chain (1); Sequence conflict (1); Transmembrane (6) TRANSMEM 1 21 Helical. {ECO:0000255}.; TRANSMEM 39 59 Helical. {ECO:0000255}.; TRANSMEM 90 110 Helical. {ECO:0000255}.; TRANSMEM 124 144 Helical. {ECO:0000255}.; TRANSMEM 159 179 Helical. {ECO:0000255}.; TRANSMEM 197 217 Helical. {ECO:0000255}. FUNCTION: May play a role in androgen-regulated growth of hair follicles. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q91XC0 AJUBA_MOUSE LIM domain-containing protein ajuba 547 57,920 Chain (1); Domain (3); Modified residue (5); Motif (1); Region (1); Sequence conflict (1) FUNCTION: Adapter or scaffold protein which participates in the assembly of numerous protein complexes and is involved in several cellular processes such as cell fate determination, cytoskeletal organization, repression of gene transcription, mitosis, cell-cell adhesion, cell differentiation, proliferation and migration. Contributes to the linking and/or strengthening of epithelia cell-cell junctions in part by linking adhesive receptors to the actin cytoskeleton. May be involved in signal transduction from cell adhesion sites to the nucleus. Plays an important role in regulation of the kinase activity of AURKA for mitotic commitment. Also a component of the IL-1 signaling pathway modulating IL-1-induced NFKB1 activation by influencing the assembly and activity of the PRKCZ-SQSTM1-TRAF6 multiprotein signaling complex. Functions as an HDAC-dependent corepressor for a subset of GFI1 target genes. Acts as a transcriptional corepressor for SNAI1 and SNAI2/SLUG-dependent repression of E-cadherin transcription. Acts as a hypoxic regulator by bridging an association between the prolyl hydroxylases and VHL enabling efficient degradation of HIF1A. Positively regulates microRNA (miRNA)-mediated gene silencing. Negatively regulates the Hippo signaling pathway and antagonizes phosphorylation of YAP1. {ECO:0000269|PubMed:10330178, ECO:0000269|PubMed:11029037, ECO:0000269|PubMed:15728191, ECO:0000269|PubMed:17909014, ECO:0000269|PubMed:18331720}. PTM: Phosphorylated by LATS2 during mitosis. Phosphorylated by AURKA (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell membrane {ECO:0000250}. Cell junction {ECO:0000250}. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, P-body {ECO:0000250}. Note=Shuttles between the cytoplasm and the nucleus. Localizes on centrosomes during G2-M phase (By similarity). Preferentially colocalizes with cadherin-adhesive complexes at sites of cell-cell contacts (By similarity). Colocalizes with GFI1 in the nucleus (By similarity). {ECO:0000250}. SUBUNIT: Interacts with SLC1A2. Interacts with AURKA; the interaction occurs during mitosis and both proteins are phosphorylated as they form a complex. Interacts with CTNNA1 and with F-actin. Interacts with LATS2; the interaction occurs during mitosis and the complex regulates organization of the spindle apparatus through recruitment of TUBG to the centrosome. Forms a complex with SQSTM1, PRKCZ and TRAF6. Component of the GFI1-AJUBA-HDAC1 repressor complex. Interacts directly (via the LIM domains) with GFI1; the interaction results in the HDAC-dependent corepression of a subset of GFI1 target genes, and is independent of the GFI1 SNAG domain. Interacts with HDAC1, HDAC2 and HDAC3 (By similarity). Interacts with GRB2 and PIP5K1B. Interacts with HDAC1, HDAC2 and HDAC3. Interacts with EIF4E, AGO1, AGO2, DCP2, DDX6, LATS1, LATS2, SAV1, EGLN2/PHD1 and EGLN3/PHD3. Interacts (via LIM domains) with VHL (By similarity). Interacts (via LIM domains) with SNAI1 (via SNAG domain), SNAI2/SLUG (via SNAG domain) and SCRT1 (via SNAG domain). {ECO:0000250, ECO:0000269|PubMed:10330178, ECO:0000269|PubMed:15870270, ECO:0000269|PubMed:18331720}. DOMAIN: LIM region interacts with CTNNA1. The preLIM region binds directly actin filaments (By similarity). {ECO:0000250}.; DOMAIN: LIM-2 and LIM-3 domains mediate the interaction with the N-terminal region of AURKA. The association between LATS2 and AJUBA required the second LIM domain of AJUBA (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in skin, brain and genitourinary organs. {ECO:0000269|PubMed:10330178}. +Q9DBF1 AL7A1_MOUSE Alpha-aminoadipic semialdehyde dehydrogenase (Alpha-AASA dehydrogenase) (EC 1.2.1.31) (Aldehyde dehydrogenase family 7 member A1) (EC 1.2.1.3) (Antiquitin-1) (Betaine aldehyde dehydrogenase) (EC 1.2.1.8) (Delta1-piperideine-6-carboxylate dehydrogenase) (P6c dehydrogenase) 539 58,861 Active site (2); Alternative sequence (1); Chain (1); Erroneous initiation (2); Modified residue (9); Nucleotide binding (1); Sequence conflict (3); Site (1); Transit peptide (1) Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine from betaine aldehyde: step 1/1. FUNCTION: Multifunctional enzyme mediating important protective effects. Metabolizes betaine aldehyde to betaine, an important cellular osmolyte and methyl donor. Protects cells from oxidative stress by metabolizing a number of lipid peroxidation-derived aldehydes. Involved in lysine catabolism (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P49419}. Nucleus {ECO:0000250|UniProtKB:P49419}.; SUBCELLULAR LOCATION: Isoform 1: Mitochondrion {ECO:0000250|UniProtKB:P49419}. SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P83402}. TISSUE SPECIFICITY: Present in liver, kidney, brain and pancreas, and at lower levels in jejunum, duodenum, stomach and testes (at protein level). {ECO:0000269|PubMed:20207735}. +Q91Y97 ALDOB_MOUSE Fructose-bisphosphate aldolase B (EC 4.1.2.13) (Aldolase 2) (Liver-type aldolase) 364 39,507 Active site (2); Binding site (2); Chain (1); Initiator methionine (1); Modified residue (15); Sequence conflict (2); Site (1) Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000250}. SUBUNIT: Homotetramer. Interacts with BBS1, BBS2, BBS4 and BBS7. {ECO:0000250}. +P05064 ALDOA_MOUSE Fructose-bisphosphate aldolase A (EC 4.1.2.13) (Aldolase 1) (Muscle-type aldolase) 364 39,356 Active site (2); Binding site (2); Chain (1); Cross-link (2); Initiator methionine (1); Modified residue (13); Sequence conflict (1); Site (1) Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. FUNCTION: Plays a key role in glycolysis and gluconeogenesis. In addition, may also function as scaffolding protein (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, I band. Cytoplasm, myofibril, sarcomere, M line. Note=In skeletal muscle, accumulates around the M line and within the I band, colocalizing with FBP2 on both sides of the Z line in the absence of Ca(2+). {ECO:0000250}. SUBUNIT: Homotetramer. Interacts with SNX9 and WAS. Interacts with FBP2; the interaction blocks FBP2 inhibition by physiological concentrations of AMP and reduces inhibition by Ca(2+) (By similarity). {ECO:0000250}. +Q8C8B0 ALX1_MOUSE ALX homeobox protein 1 (Cartilage homeoprotein 1) (CART-1) 326 36,931 Chain (1); DNA binding (1); Modified residue (4); Motif (1); Mutagenesis (1); Region (1) FUNCTION: Sequence-specific DNA-binding transcription factor that binds palindromic sequences within promoters and may activate or repress the transcription of a subset of genes (PubMed:12929931). Most probably regulates the expression of genes involved in the development of mesenchyme-derived craniofacial structures. Early on in development, it plays a role in forebrain mesenchyme survival (PubMed:8673125). May also induce epithelial to mesenchymal transition (EMT) through the expression of SNAI1 (By similarity). {ECO:0000250|UniProtKB:Q15699, ECO:0000269|PubMed:12929931, ECO:0000269|PubMed:8673125}. PTM: Acetylated at Lys-131 by EP300; increases interaction with EP300 and stimulates ALX1 transcriptional activity. {ECO:0000269|PubMed:12929931}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12929931}. SUBUNIT: Binds DNA as a homodimer; required for transcriptional activation (By similarity). Interacts (via homeobox domain) with EP300; acetylates ALX1 and stimulates its transcriptional activity (PubMed:12929931). {ECO:0000250|UniProtKB:Q63087, ECO:0000269|PubMed:12929931}. DOMAIN: The OAR motif may negatively regulate DNA-binding and therefore transcriptional activity. It is found in the C-terminal transactivation domain that stimulates transcription. {ECO:0000250|UniProtKB:Q63087}. +P70389 ALS_MOUSE Insulin-like growth factor-binding protein complex acid labile subunit (ALS) 603 66,960 Chain (1); Domain (2); Glycosylation (7); Repeat (19); Sequence conflict (1); Signal peptide (1) FUNCTION: May have an important role in regulating the access of circulating IGFs to the tissues. SUBCELLULAR LOCATION: Secreted, extracellular space. SUBUNIT: Forms a ternary complex of about 140 to 150 kDa with IGF-I or IGF-II and IGFBP-3. {ECO:0000250}. +P40753 ANFB_MOUSE Natriuretic peptides B (Gamma-brain natriuretic peptide) [Cleaved into: Brain natriuretic peptide (BNP)] 121 13,756 Alternative sequence (1); Disulfide bond (1); Peptide (2); Sequence conflict (2); Signal peptide (1); Site (1) FUNCTION: Cardiac hormone which may function as a paracrine antifibrotic factor in the heart. Also plays a key role in cardiovascular homeostasis through natriuresis, diuresis, vasorelaxation, and inhibition of renin and aldosterone secretion. Specifically binds and stimulates the cGMP production of the NPR1 receptor. Binds the clearance receptor NPR3. PTM: The brain natriuretic peptide 32 form is cleaved at Ser-91 by the prolyl endopeptidase FAP (seprase) activity (in vitro). {ECO:0000250|UniProtKB:P16860}. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Expressed abundantly in the ventricle, and in a lesser extent in the atrium. +Q9Z1P8 ANGL4_MOUSE Angiopoietin-related protein 4 (425O18-1) (Angiopoietin-like protein 4) (Fasting-induced adipose factor) (Hepatic fibrinogen/angiopoietin-related protein) (HFARP) (Secreted protein Bk89) 410 45,538 Chain (1); Coiled coil (1); Disulfide bond (2); Domain (1); Glycosylation (3); Sequence conflict (5); Signal peptide (1) FUNCTION: Protein with hypoxia-induced expression in endothelial cells. May act as a regulator of angiogenesis and modulate tumorigenesis. Inhibits proliferation, migration, and tubule formation of endothelial cells and reduces vascular leakage. May exert a protective function on endothelial cells through an endocrine action. It is directly involved in regulating glucose homeostasis, lipid metabolism, and insulin sensitivity (By similarity). In response to hypoxia, the unprocessed form of the protein accumulates in the subendothelial extracellular matrix (ECM). The matrix-associated and immobilized unprocessed form limits the formation of actin stress fibers and focal contacts in the adhering endothelial cells and inhibits their adhesion. It also decreases motility of endothelial cells and inhibits the sprouting and tube formation. {ECO:0000250, ECO:0000269|PubMed:15837923, ECO:0000269|PubMed:17068295, ECO:0000269|PubMed:17130448}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17068295}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:17068295}. Note=The unprocessed form interacts with the extracellular matrix. This may constitute a dynamic reservoir, a regulatory mechanism of the bioavailability of ANGPTL4. SUBUNIT: Homooligomer. The homooligomer undergoes proteolytic processing to release its carboxyl fibrinogen-like domain, which circulates as a monomer (By similarity). The homooligomer unprocessed form is able to interact with the extracellular matrix, this interaction is found to be heparin/heparan sulfate proteoglycan dependent (in competition and direct binding assays). {ECO:0000250}. TISSUE SPECIFICITY: Predominantly expressed in adipose tissue and is strongly up-regulated by fasting in white adipose tissue and liver. {ECO:0000269|PubMed:10862772}. +Q9EST5 AN32B_MOUSE Acidic leucine-rich nuclear phosphoprotein 32 family member B (Proliferation-related acidic leucine-rich protein PAL31) 272 31,079 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (1); Modified residue (3); Repeat (4) FUNCTION: Multifunctional protein working as a cell cycle progression factor as well as a cell survival factor. Required for the progression from the G1 to the S phase. Anti-apoptotic protein which functions as a caspase-3 inhibitor. Has no phosphatase 2A (PP2A) inhibitor activity. Exhibits histone chaperone properties, stimulating core histones to assemble into a nucleosome (By similarity). {ECO:0000250}. PTM: Some glutamate residues are glycylated by TTLL8. This modification occurs exclusively on glutamate residues and results in a glycine chain on the gamma-carboxyl group. SUBCELLULAR LOCATION: Nucleus. Note=Accumulates in the nuclei at the S phase. {ECO:0000250}. SUBUNIT: Monomer. Interacts with histones H3 and H4 (By similarity). {ECO:0000250}. DOMAIN: Histone binding is mediated by the concave surface of the LRR region. {ECO:0000250}. +Q8C2S7 AMGO3_MOUSE Amphoterin-induced protein 3 (AMIGO-3) (Alivin-3) 508 55,625 Chain (1); Disulfide bond (5); Domain (3); Erroneous initiation (1); Frameshift (1); Glycosylation (6); Repeat (6); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 384 404 Helical. {ECO:0000255}. TOPO_DOM 20 383 Extracellular. {ECO:0000255}.; TOPO_DOM 405 508 Cytoplasmic. {ECO:0000255}. FUNCTION: May mediate heterophilic cell-cell interaction. May contribute to signal transduction through its intracellular domain (By similarity). {ECO:0000250|UniProtKB:Q80ZD5}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Binds AMIGO1 or AMIGO2. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12629050}. +Q8K592 AMHR2_MOUSE Anti-Muellerian hormone type-2 receptor (EC 2.7.11.30) (Anti-Muellerian hormone type II receptor) (AMH type II receptor) (MIS type II receptor) (MISRII) (MRII) 568 61,195 Active site (1); Binding site (1); Chain (1); Disulfide bond (2); Domain (1); Glycosylation (2); Nucleotide binding (1); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 148 168 Helical. {ECO:0000255}. TOPO_DOM 16 147 Extracellular. {ECO:0000255}.; TOPO_DOM 169 568 Cytoplasmic. {ECO:0000255}. FUNCTION: On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for anti-Muellerian hormone. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. +Q3UUF8 AN34B_MOUSE Ankyrin repeat domain-containing protein 34B (Dendritic protein of 58 kDa) 508 55,417 Chain (1); Frameshift (1); Modified residue (3); Repeat (4); Sequence conflict (1) PTM: Phosphorylated. {ECO:0000269|PubMed:15358210, ECO:0000269|PubMed:17485271}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17485271}. Nucleus {ECO:0000269|PubMed:17485271}. TISSUE SPECIFICITY: Specifically and constitutively expressed in brain (at protein level). {ECO:0000269|PubMed:17485271}. +G5E8Q8 AGRF5_MOUSE Adhesion G protein-coupled receptor F5 (G-protein coupled receptor 116) 1348 149,387 Chain (1); Compositional bias (2); Disulfide bond (3); Domain (5); Glycosylation (7); Modified residue (3); Signal peptide (1); Site (3); Topological domain (8); Transmembrane (7) TRANSMEM 1020 1040 Helical. {ECO:0000255}.; TRANSMEM 1056 1076 Helical. {ECO:0000255}.; TRANSMEM 1093 1113 Helical. {ECO:0000255}.; TRANSMEM 1131 1151 Helical. {ECO:0000255}.; TRANSMEM 1176 1196 Helical. {ECO:0000255}.; TRANSMEM 1222 1242 Helical. {ECO:0000255}.; TRANSMEM 1251 1271 Helical. {ECO:0000255}. TOPO_DOM 22 1019 Extracellular. {ECO:0000305}.; TOPO_DOM 1041 1055 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1077 1092 Extracellular. {ECO:0000305}.; TOPO_DOM 1114 1130 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1152 1175 Extracellular. {ECO:0000305}.; TOPO_DOM 1197 1221 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1243 1250 Extracellular. {ECO:0000305}.; TOPO_DOM 1272 1348 Cytoplasmic. {ECO:0000305}. FUNCTION: Receptor that plays a critical role in lung surfactant homeostasis (PubMed:23590306, PubMed:23922714, PubMed:23684610). May play a role in controlling adipocyte function (PubMed:22971422). {ECO:0000269|PubMed:22971422, ECO:0000269|PubMed:23590306, ECO:0000269|PubMed:23684610, ECO:0000269|PubMed:23922714}. PTM: Proteolytically cleaved at multiple sites: one in the GPS domain (S1 site) and the other in the SEA domain (S2 site). The proteolytic cleavage at S1 site generates an extracellular subunit and a seven-transmembrane subunit. The proteolytic cleavage at S2 site generates a fragment that undergoes proteolytic cleavage by the processing enzyme furin. {ECO:0000250|UniProtKB:Q9WVT0}.; PTM: Highly glycosylated. {ECO:0000250|UniProtKB:Q9WVT0}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9WVT0}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Homodimer; disulfide-linked. Heterodimer of 2 chains generated by proteolytic processing; the large extracellular N-terminal fragment and the membrane-bound C-terminal fragment predominantly remain associated and non-covalently linked. Fragment generates by the processing enzyme furin remains attached to the extracellular N-terminal fragment. Interacts (via N-terminal extracellular domain) with SFTPD (PubMed:23922714). {ECO:0000250|UniProtKB:Q9WVT0, ECO:0000269|PubMed:23922714}. TISSUE SPECIFICITY: Widely expressed and highly expressed in the lung. In the lung predominantly expressed in the alveolar type II epithelial cells. {ECO:0000269|PubMed:22837050, ECO:0000269|PubMed:22971422, ECO:0000269|PubMed:23590306, ECO:0000269|PubMed:23684610}. +Q60662 AKAP4_MOUSE A-kinase anchor protein 4 (AKAP-4) (A-kinase anchor protein 82 kDa) (AKAP 82) (mAKAP82) (FSC1) (Major sperm fibrous sheath protein) (Protein kinase A-anchoring protein 4) (PRKA4) (p82) 849 93,796 Alternative sequence (1); Chain (1); Modified residue (24); Propeptide (1); Region (2); Sequence conflict (11) FUNCTION: Major structural component of sperm fibrous sheath. Plays a role in sperm motility (PubMed:12167408). {ECO:0000269|PubMed:12167408}. SUBCELLULAR LOCATION: Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q5JQC9}. Note=Localizes to the principle piece of the sperm flagellum. {ECO:0000250|UniProtKB:Q5JQC9}. SUBUNIT: Interacts with PRKAR1A and PRKAR2A (PubMed:9852104). Interacts with ENO4 (PubMed:23446454). {ECO:0000269|PubMed:23446454, ECO:0000269|PubMed:9852104}. DOMAIN: RI-alpha binding site, predicted to form an amphipathic helix, could participate in protein-protein interactions with a complementary surface on the R-subunit dimer. {ECO:0000269|PubMed:9852104}. TISSUE SPECIFICITY: Spermatid. +Q8C4G9 AGRA1_MOUSE Adhesion G protein-coupled receptor A1 (G-protein coupled receptor 123) 578 63,497 Chain (1); Sequence conflict (1); Topological domain (7); Transmembrane (7) TRANSMEM 23 43 Helical; Name=1. {ECO:0000255}.; TRANSMEM 57 77 Helical; Name=2. {ECO:0000255}.; TRANSMEM 88 108 Helical; Name=3. {ECO:0000255}.; TRANSMEM 138 158 Helical; Name=4. {ECO:0000255}.; TRANSMEM 179 199 Helical; Name=5. {ECO:0000255}.; TRANSMEM 263 283 Helical; Name=6. {ECO:0000255}.; TRANSMEM 290 310 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 22 Extracellular. {ECO:0000305}.; TOPO_DOM 44 56 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 78 87 Extracellular. {ECO:0000305}.; TOPO_DOM 109 137 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 159 178 Extracellular. {ECO:0000305}.; TOPO_DOM 200 262 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 284 289 Extracellular. {ECO:0000305}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Predominantly expressed in CNS. {ECO:0000269|PubMed:17212699}. +O88845 AKA10_MOUSE A-kinase anchor protein 10, mitochondrial (AKAP-10) (Dual specificity A kinase-anchoring protein 2) (D-AKAP-2) (Protein kinase A-anchoring protein 10) (PRKA10) 662 73,632 Alternative sequence (4); Chain (1); Domain (2); Erroneous initiation (1); Frameshift (1); Modified residue (3); Region (1); Sequence conflict (5); Transit peptide (1) FUNCTION: Differentially targeted protein that binds to type I and II regulatory subunits of protein kinase A and anchors them to the mitochondria or the plasma membrane. Although the physiological relevance between PKA and AKAPS with mitochondria is not fully understood, one idea is that BAD, a proapoptotic member, is phosphorylated and inactivated by mitochondria-anchored PKA. It cannot be excluded too that it may facilitate PKA as well as G protein signal transduction, by acting as an adapter for assembling multiprotein complexes. With its RGS domain, it could lead to the interaction to G-alpha proteins, providing a link between the signaling machinery and the downstream kinase. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11248059}. Membrane {ECO:0000269|PubMed:11248059}. Cytoplasm {ECO:0000269|PubMed:11248059}. Note=Predominantly mitochondrial but also membrane associated and cytoplasmic. DOMAIN: RII-alpha binding site, predicted to form an amphipathic helix, could participate in protein-protein interactions with a complementary surface on the R-subunit dimer. TISSUE SPECIFICITY: Highly expressed in testis, kidney and lung, followed by brain, skeletal muscle, liver, spleen and heart. Also expressed in brown adipose tissue and pancreas. +Q8VDI9 ALG9_MOUSE Alpha-1,2-mannosyltransferase ALG9 (EC 2.4.1.259) (EC 2.4.1.261) (Dol-P-Man:Man(6)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase) (Dol-P-Man:Man(8)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase) 611 69,561 Chain (1); Compositional bias (1); Frameshift (1); Glycosylation (3); Sequence conflict (1); Topological domain (9); Transmembrane (8) TRANSMEM 136 156 Helical. {ECO:0000255}.; TRANSMEM 172 192 Helical. {ECO:0000255}.; TRANSMEM 214 234 Helical. {ECO:0000255}.; TRANSMEM 250 270 Helical. {ECO:0000255}.; TRANSMEM 311 331 Helical. {ECO:0000255}.; TRANSMEM 343 363 Helical. {ECO:0000255}.; TRANSMEM 371 391 Helical. {ECO:0000255}.; TRANSMEM 406 426 Helical. {ECO:0000255}. TOPO_DOM 1 135 Lumenal. {ECO:0000255}.; TOPO_DOM 157 171 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 193 213 Lumenal. {ECO:0000255}.; TOPO_DOM 235 249 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 271 310 Lumenal. {ECO:0000255}.; TOPO_DOM 332 342 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 364 370 Lumenal. {ECO:0000255}.; TOPO_DOM 392 405 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 427 611 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Catalyzes the transfer of mannose from Dol-P-Man to lipid-linked oligosaccharides. {ECO:0000250|UniProtKB:Q9H6U8}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9H6U8}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9H6U8}. +P0CB42 ALKB1_MOUSE Nucleic acid dioxygenase ALKBH1 (EC 1.14.11.-) (Alkylated DNA repair protein alkB homolog 1) (Alpha-ketoglutarate-dependent dioxygenase ABH1) (DNA 6mA demethylase) (DNA N6-methyl adenine demethylase) (EC 1.14.11.51) (DNA lyase ABH1) (EC 4.2.99.18) (DNA oxidative demethylase ALKBH1) (EC 1.14.11.33) (tRNA N1-methyl adenine demethylase) (EC 1.14.11.-) 389 43,746 Binding site (2); Chain (1); Domain (1); Metal binding (3); Mutagenesis (1); Region (5) FUNCTION: Dioxygenase that acts as on nucleic acids, such as DNA and tRNA (PubMed:27027282, PubMed:27745969). Requires molecular oxygen, alpha-ketoglutarate and iron (PubMed:27027282). A number of activities have been described for this dioxygenase, but recent results suggest that it mainly acts as on tRNAs and mediates their demethylation or oxidation depending on the context and subcellular compartment (By similarity). Mainly acts as a tRNA demethylase by removing N(1)-methyladenine from various tRNAs, with a preference for N(1)-methyladenine at position 58 (m1A58) present on a stem loop structure of tRNAs (PubMed:27745969). Acts as a regulator of translation initiation and elongation in response to glucose deprivation: regulates both translation initiation, by mediating demethylation of tRNA(Met), and translation elongation, N(1)-methyladenine-containing tRNAs being preferentially recruited to polysomes to promote translation elongation (By similarity). In mitochondrion, specifically interacts with mt-tRNA(Met) and mediates oxidation of mt-tRNA(Met) methylated at cytosine(34) to form 5-formylcytosine (f(5)c) at this position (By similarity). mt-tRNA(Met) containing the f(5)c modification at the wobble position enables recognition of the AUA codon in addition to the AUG codon, expanding codon recognition in mitochondrial translation (By similarity). Specifically demethylates DNA methylated on the 6th position of adenine (N(6)-methyladenosine) DNA (PubMed:27027282). N(6)-methyladenosine (m6A) DNA is present at some L1 elements in embryonic stem cells and probably promotes their silencing (PubMed:27027282). Also able to repair alkylated single-stranded DNA and RNA containing 3-methylcytosine by oxidative demethylation, but with low activity (By similarity). Also has DNA lyase activity and introduces double-stranded breaks at abasic sites: cleaves both single-stranded DNA and double-stranded DNA at abasic sites, with the greatest activity towards double-stranded DNA with two abasic sites (By similarity). DNA lyase activity does not require alpha-ketboglutarate and iron and leads to the formation of an irreversible covalent protein-DNA adduct with the 5' DNA product (By similarity). DNA lyase activity is not required during base excision repair and class switch recombination of the immunoglobulin heavy chain during B lymphocyte activation (PubMed:23825659). May play a role in placental trophoblast lineage differentiation (PubMed:18163532). {ECO:0000250|UniProtKB:Q13686, ECO:0000269|PubMed:18163532, ECO:0000269|PubMed:23825659, ECO:0000269|PubMed:27027282, ECO:0000269|PubMed:27745969}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18163532}. Note=Mainly localizes in euchromatin, largely excluded from heterochromatin and nucleoli. {ECO:0000269|PubMed:18163532}. SUBUNIT: Monomer (By similarity). Interacts with DNAJB6 (PubMed:18163532). {ECO:0000250|UniProtKB:Q13686, ECO:0000269|PubMed:18163532}. TISSUE SPECIFICITY: In adult organs, highly expressed in testis, eye, brain and kidney. {ECO:0000269|PubMed:21072209}. +Q6P6J4 ALKB2_MOUSE DNA oxidative demethylase ALKBH2 (EC 1.14.11.33) (Alkylated DNA repair protein alkB homolog 2) (Alpha-ketoglutarate-dependent dioxygenase alkB homolog 2) 239 27,129 Binding site (1); Chain (1); Domain (1); Metal binding (3); Mutagenesis (2); Region (4); Sequence conflict (1) FUNCTION: Dioxygenase that repairs alkylated DNA and RNA containing 1-methyladenine and 3-methylcytosine by oxidative demethylation. Can also repair alkylated DNA containing 1-ethenoadenine. Has strong preference for double-stranded DNA. Has low efficiency with single-stranded substrates. Requires molecular oxygen, alpha-ketoglutarate and iron. {ECO:0000269|PubMed:16174769, ECO:0000269|PubMed:16642038, ECO:0000269|PubMed:18519673}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16642038, ECO:0000269|PubMed:18519673}. TISSUE SPECIFICITY: Detected in liver, testis and kidney (at protein level). Detected in heart and testis. {ECO:0000269|PubMed:16174769, ECO:0000269|PubMed:16642038, ECO:0000269|PubMed:18519673}. +Q9D8F1 ALKB4_MOUSE Alpha-ketoglutarate-dependent dioxygenase alkB homolog 4 (EC 1.14.11.-) (Alkylated DNA repair protein alkB homolog 4) 300 33,394 Alternative sequence (1); Binding site (1); Chain (1); Initiator methionine (1); Metal binding (3); Modified residue (1) FUNCTION: Dioxygenase that mediates demethylation of actin monomethylated at 'Lys-84' (K84me1), thereby acting as a regulator of actomyosin-processes. Demethylation of actin K84me1 is required for maintaining actomyosin dynamics supporting normal cleavage furrow ingression during cytokinesis and cell migration. May be involved in transcription regulation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Midbody {ECO:0000250}. Note=Associates with the contractile ring and midbody. {ECO:0000250}. SUBUNIT: Interacts with ZFHX3, MLLT3, MLLT1, HSF4, EP300, TES, EIF3C, MTMR6 and PSMA6. {ECO:0000250}. +Q3TSG4 ALKB5_MOUSE RNA demethylase ALKBH5 (EC 1.14.11.-) (Alkylated DNA repair protein alkB homolog 5) (Alpha-ketoglutarate-dependent dioxygenase alkB homolog 5) 395 44,411 Binding site (1); Chain (1); Coiled coil (1); Compositional bias (1); Cross-link (1); Initiator methionine (1); Metal binding (3); Modified residue (10); Region (1); Sequence conflict (5) FUNCTION: Dioxygenase that demethylates RNA by oxidative demethylation: specifically demethylates N(6)-methyladenosine (m6A) RNA, the most prevalent internal modification of messenger RNA (mRNA) in higher eukaryotes (PubMed:29279410). Can also demethylate N(6)-methyladenosine in single-stranded DNA (in vitro) (By similarity). Requires molecular oxygen, alpha-ketoglutarate and iron (By similarity). Demethylation of m6A mRNA affects mRNA processing and export (By similarity). Required for the late meiotic and haploid phases of spermatogenesis by mediating m6A demethylation in spermatocytes and round spermatids: m6A demethylation of target transcripts is required for correct splicing and the production of longer 3'-UTR mRNAs in male germ cells (PubMed:23177736, PubMed:29279410). {ECO:0000250|UniProtKB:Q6P6C2, ECO:0000269|PubMed:23177736, ECO:0000269|PubMed:29279410}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:29279410}. SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q6P6C2}. TISSUE SPECIFICITY: Widely expressed, with highest expression in testis (PubMed:23177736). In testis, present in almost all testicular cell types except elongating and elongated spermatids (at protein level) (PubMed:29279410). Among spermatogenic cells, present at high level in spermatocytes; medium levels in spermatogonia and lower levels in round spermatids (at protein level) (PubMed:29279410). {ECO:0000269|PubMed:23177736, ECO:0000269|PubMed:29279410}. +Q7TQF7 AMPH_MOUSE Amphiphysin 686 75,013 Chain (1); Coiled coil (2); Compositional bias (1); Domain (2); Modified residue (9) FUNCTION: May participate in mechanisms of regulated exocytosis in synapses and certain endocrine cell types. May control the properties of the membrane associated cytoskeleton (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. SUBUNIT: Heterodimer with BIN1 (By similarity). Binds SH3GLB1 (By similarity). Interacts with REPS1 and SGIP1 (By similarity). Binds AP2A2. Interacts with AP2B1. Interacts with DNM1 AND SYNJ1 (By similarity). {ECO:0000250|UniProtKB:O08838}. +Q8JZZ6 AMERL_MOUSE AMMECR1-like protein 310 34,516 Chain (1); Domain (1); Modified residue (1) +Q8R1L8 ANGL8_MOUSE Angiopoietin-like protein 8 (Betatrophin) (Lipasin) (Refeeding-induced fat and liver protein) 198 22,063 Chain (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Hormone that acts as a blood lipid regulator by regulating serum triglyceride levels (PubMed:22569073, PubMed:22809513, PubMed:23150577, PubMed:24043787). May be involved in the metabolic transition between fasting and refeeding: required to direct fatty acids to adipose tissue for storage in the fed state (PubMed:24043787). According to a report, may act by promoting ANGPTL3 cleavage (PubMed:23150577). According to another study, not required for cleavage of ANGPTL3 (PubMed:24043787). {ECO:0000269|PubMed:22569073, ECO:0000269|PubMed:22809513, ECO:0000269|PubMed:23150577, ECO:0000269|PubMed:24043787}. PTM: Proteolytically cleaved at the N-terminus. {ECO:0000250|UniProtKB:Q6UXH0}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22569073, ECO:0000269|PubMed:23623304}. SUBUNIT: Interacts with ANGPTL3. {ECO:0000250|UniProtKB:Q6UXH0}. TISSUE SPECIFICITY: Expressed in liver and fat. Enriched in white and brown adipose tissues. {ECO:0000269|PubMed:22569073, ECO:0000269|PubMed:22809513, ECO:0000269|PubMed:23623304}. +Q8C8R3 ANK2_MOUSE Ankyrin-2 (ANK-2) (Ankyrin-B) (Brain ankyrin) 3898 426,261 Alternative sequence (16); Chain (1); Compositional bias (2); Domain (4); Frameshift (1); Modified residue (56); Mutagenesis (4); Region (2); Repeat (24); Sequence conflict (5) FUNCTION: Plays an essential role in the localization and membrane stabilization of ion transporters and ion channels in several cell types, including cardiomyocytes, as well as in striated muscle cells. In skeletal muscle, required for proper localization of DMD and DCTN4 and for the formation and/or stability of a special subset of microtubules associated with costameres and neuromuscular junctions (PubMed:19109891). In cardiomyocytes, required for coordinate assembly of Na/Ca exchanger, SLC8A1/NCX1, Na/K ATPases ATP1A1 and ATP1A2 and inositol 1,4,5-trisphosphate (InsP3) receptors at sarcoplasmic reticulum/sarcolemma sites (PubMed:12571597). Required for expression and targeting of SPTBN1 in neonatal cardiomyocytes and for the regulation of neonatal cardiomyocyte contraction rate (PubMed:15262991). In the inner segment of rod photoreceptors, required for the coordinated expression of the Na/K ATPase, Na/Ca exchanger and beta-2-spectrin (SPTBN1) (PubMed:19007774). Plays a role in endocytosis and intracellular protein transport. Associates with phosphatidylinositol 3-phosphate (PI3P)-positive organelles and binds dynactin to promote long-range motility of cells. Recruits RABGAP1L to (PI3P)-positive early endosomes, where RABGAP1L inactivates RAB22A, and promotes polarized trafficking to the leading edge of the migrating cells. Part of the ANK2/RABGAP1L complex which is required for the polarized recycling of fibronectin receptor ITGA5 ITGB1 to the plasma membrane that enables continuous directional cell migration (PubMed:27718357). {ECO:0000269|PubMed:12571597, ECO:0000269|PubMed:15262991, ECO:0000269|PubMed:19007774, ECO:0000269|PubMed:19109891, ECO:0000269|PubMed:27718357}. PTM: Phosphorylated at multiple sites by different protein kinases and each phosphorylation event regulates the protein's structure and function. {ECO:0000250|UniProtKB:Q01484, ECO:0000305}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q01484}. Cytoplasm, myofibril, sarcomere, M line {ECO:0000269|PubMed:12571597, ECO:0000269|PubMed:19109891}. Cell membrane {ECO:0000269|PubMed:19007774}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000269|PubMed:19109891}. Early endosome {ECO:0000269|PubMed:27718357}. Recycling endosome {ECO:0000269|PubMed:27718357}. Lysosome {ECO:0000269|PubMed:27718357}. Mitochondrion {ECO:0000269|PubMed:27718357}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:12571597}. Cell membrane, sarcolemma, T-tubule {ECO:0000269|PubMed:12571597}. Note=Expressed at the apical membrane of airway lung epithelial cells. Localized to the plasma membrane of the inner segments of photoreceptors in retina (PubMed:19007774). Colocalizes with SPTBN1 in a distinct intracellular compartment of neonatal cardiomyocytes (PubMed:15262991). In skeletal muscle, localizes to neuromuscular junctions (PubMed:19109891). Localizes with puncta at mitochondria ends. Colocalizes and cotransports on motile vesicles with RABGAP1L (PubMed:27718357). {ECO:0000269|PubMed:15262991, ECO:0000269|PubMed:19007774, ECO:0000269|PubMed:19109891, ECO:0000269|PubMed:27718357}. SUBUNIT: Interacts with RHBG (By similarity). Interacts with SPTBN1 (PubMed:15262991, PubMed:19007774). Colocalizes with Na/Ca exchanger (PubMed:19007774). Interacts with Na/K ATPases ATP1A1 and ATP1A2 (PubMed:19007774, PubMed:12571597). Directly interacts with DMD; this interaction is necessary for DMD localization at the sarcolemma. Interacts with DCTN4; this interaction is required for DCTN4 retention at costameres (PubMed:19109891). Identified in complexes that contain VIM, EZR, AHNAK, BFSP1, BFSP2, ANK2, PLEC, PRX and spectrin (PubMed:21745462). Interacts (via death domain) with RABGAP1L (via Rab-GAP TBC domain) (PubMed:27718357). Interacts with SLC8A1/NCX1 (PubMed:12571597). May interact with inositol 1,4,5-trisphosphate receptors (PubMed:12571597). {ECO:0000250|UniProtKB:Q01484, ECO:0000269|PubMed:12571597, ECO:0000269|PubMed:15262991, ECO:0000269|PubMed:19007774, ECO:0000269|PubMed:19109891, ECO:0000269|PubMed:21745462, ECO:0000269|PubMed:27718357}. DOMAIN: The tandem configuration of the two ZU5 and the UPA domains forms a structural supramodule termed ZZU. ZU5-1 mediates interaction with beta-spectrin, and the ZU5-1/UPA interface is required for ankyrin's function other than binding to spectrin (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Detected in eye lens fiber cells (at protein level) (PubMed:21745462). In the retina, expressed in the inner segments of rod photoreceptors (PubMed:19007774). Expressed in cardiomyocytes, as well as in skeletal muscles (PubMed:17940615, PubMed:27718357, PubMed:12571597). Also detected in brain and pancreas, as well as in kidney and spleen (at protein level) (PubMed:8253844, PubMed:17940615, PubMed:12571597). In the pancreas, highly expressed in islets, predominantly in beta cells, but low expression, if any in acinar cells (at protein level) (PubMed:17940615). In the central nervous system, expressed in the corpus callosum and in cerebellar Purkinje neurons (at protein level) (PubMed:17940615, PubMed:27718357). Expressed in lung and, at low levels, in testes (at protein level) (PubMed:17940615). {ECO:0000269|PubMed:12571597, ECO:0000269|PubMed:17940615, ECO:0000269|PubMed:19007774, ECO:0000269|PubMed:21745462, ECO:0000269|PubMed:27718357, ECO:0000269|PubMed:8253844}. +G5E8K5 ANK3_MOUSE Ankyrin-3 (ANK-3) (Ankyrin-G) 1961 214,062 Alternative sequence (5); Chain (1); Domain (3); Erroneous initiation (2); Modified residue (23); Region (1); Repeat (23); Sequence conflict (5) FUNCTION: Membrane-cytoskeleton linker. May participate in the maintenance/targeting of ion channels and cell adhesion molecules at the nodes of Ranvier and axonal initial segments (By similarity). In skeletal muscle, required for costamere localization of DMD and betaDAG1. Regulates KCNA1 channel activity in function of dietary Mg(2+) levels, and thereby contributes to the regulation of renal Mg(2+) reabsorption (PubMed:23903368). {ECO:0000250, ECO:0000269|PubMed:19109891, ECO:0000269|PubMed:23903368}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q12955}. Cell projection, axon {ECO:0000250|UniProtKB:O70511}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:Q12955}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000250|UniProtKB:O70511}. Lysosome {ECO:0000269|PubMed:9060470}. Cell membrane, sarcolemma, T-tubule {ECO:0000250|UniProtKB:O70511}. Note=In skeletal muscle, localized at costameres and neuromuscular junctions. In bone marrow-derived macrophages, isoforms 2 and 3 are associated with lysosomes. SUBUNIT: May be a constituent of a NFASC/NRCAM/ankyrin G complex. Interacts with RHBG (By similarity). Directly interacts with DMD and betaDAG1; this interaction does not interfere with DMD-binding and is required for DMD and betaDAG1 retention at costameres. Interacts (via N-terminal ANK repeats) with SCHIP1 isoform 7 (via C-terminus); this interaction is required for the localization at axon initial segments (AISs) and nodes of Ranvier (NRs). Interacts with PLEC and FLNC (By similarity). Interacts with KCNA1; this inhibits channel activity (PubMed:23903368). Interacts with SCN5A (By similarity). {ECO:0000250|UniProtKB:O70511, ECO:0000250|UniProtKB:Q12955, ECO:0000269|PubMed:18550753, ECO:0000269|PubMed:19109891}. TISSUE SPECIFICITY: Expressed in many epithelial tissues, muscles and axons. Expressed in kidney, brain, skin, lung, liver, intestine, pancreas, heart and testis (at protein level). In testis, expressed in Leydig cells, but very weakly or not at all in Sertoli cells or seminiferous tubules. Expressed in macrophages (at protein level). {ECO:0000269|PubMed:23903368, ECO:0000269|PubMed:7615634, ECO:0000269|PubMed:9060470}. +Q3TPE9 ANKY2_MOUSE Ankyrin repeat and MYND domain-containing protein 2 440 48,774 Alternative sequence (2); Chain (1); Frameshift (1); Repeat (3); Sequence conflict (2); Zinc finger (1) FUNCTION: May be involved in the trafficking of signaling proteins to the cilia. {ECO:0000250}. SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000250}. SUBUNIT: Interacts with the retinal-specific guanylyl cyclase GC1. {ECO:0000269|PubMed:21124868}. +Q8C0W1 ANMY1_MOUSE Ankyrin repeat and MYND domain-containing protein 1 906 101,999 Chain (1); Repeat (10); Sequence conflict (1); Zinc finger (1) +Q9ESW4 AGK_MOUSE Acylglycerol kinase, mitochondrial (EC 2.7.1.107) (EC 2.7.1.94) (Multiple substrate lipid kinase) (MuLK) (Multi-substrate lipid kinase) 421 46,976 Alternative sequence (1); Chain (1); Domain (1); Modified residue (1); Region (1) Lipid metabolism; glycerolipid metabolism. FUNCTION: Lipid kinase that can phosphorylate both monoacylglycerol and diacylglycerol to form lysophosphatidic acid (LPA) and phosphatidic acid (PA), respectively (PubMed:15252046). Does not phosphorylate sphingosine (PubMed:15252046). Independently of its lipid kinase activity, acts as a component of the TIM22 complex (By similarity). The TIM22 complex mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane by forming a twin-pore translocase that uses the membrane potential as the external driving force (By similarity). In the TIM22 complex, required for the import of a subset of metabolite carriers into mitochondria, such as ANT1/SLC25A4 and SLC25A24, while it is not required for the import of TIMM23 (By similarity). Overexpression increases the formation and secretion of LPA, resulting in transactivation of EGFR and activation of the downstream MAPK signaling pathway, leading to increased cell growth (By similarity). {ECO:0000250|UniProtKB:Q53H12, ECO:0000269|PubMed:15252046}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q53H12}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q53H12}. Mitochondrion intermembrane space {ECO:0000250|UniProtKB:Q53H12}. Note=Localizes in the mitochondrion intermembrane space, where it associates with the inner membrane. It is unclear whether the N-terminal hydrophobic region forms a transmembrane region or associates with the membrane without crossing it. {ECO:0000250|UniProtKB:Q53H12}. SUBUNIT: Component of the TIM22 complex, which core is composed of TIMM22, associated with TIMM10 (TIMM10A and/or TIMM10B), TIMM9, AGK and TIMM29. {ECO:0000250|UniProtKB:Q53H12}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:15252046}. +Q3UHD1 AGRB1_MOUSE Adhesion G protein-coupled receptor B1 (Brain-specific angiogenesis inhibitor 1) [Cleaved into: Vasculostatin-120 (Vstat120); Vasculostatin-40 (Vstat-40)] 1582 173,297 Chain (3); Compositional bias (1); Disulfide bond (19); Domain (6); Glycosylation (7); Modified residue (2); Mutagenesis (1); Region (3); Sequence conflict (4); Signal peptide (1); Site (1); Topological domain (8); Transmembrane (7) TRANSMEM 949 969 Helical; Name=1. {ECO:0000255}.; TRANSMEM 981 1001 Helical; Name=2. {ECO:0000255}.; TRANSMEM 1009 1029 Helical; Name=3. {ECO:0000255}.; TRANSMEM 1053 1073 Helical; Name=4. {ECO:0000255}.; TRANSMEM 1094 1114 Helical; Name=5. {ECO:0000255}.; TRANSMEM 1137 1157 Helical; Name=6. {ECO:0000255}.; TRANSMEM 1167 1187 Helical; Name=7. {ECO:0000255}. TOPO_DOM 34 948 Extracellular. {ECO:0000255}.; TOPO_DOM 970 980 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1002 1008 Extracellular. {ECO:0000255}.; TOPO_DOM 1030 1052 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1074 1093 Extracellular. {ECO:0000255}.; TOPO_DOM 1115 1136 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1158 1166 Extracellular. {ECO:0000255}.; TOPO_DOM 1188 1582 Cytoplasmic. {ECO:0000255}. FUNCTION: Phosphatidylserine receptor which enhances the engulfment of apoptotic cells (PubMed:17960134). Also mediates the binding and engulfment of Gram-negative bacteria (PubMed:21245295, PubMed:26838550, PubMed:26838550). Stimulates production of reactive oxygen species by macrophages in response to Gram-negative bacteria, resulting in enhanced microbicidal macrophage activity (By similarity). In the gastric mucosa, required for recognition and engulfment of apoptotic gastric epithelial cells (By similarity). Promotes myoblast fusion (PubMed:23615608). Activates the Rho pathway in a G-protein-dependent manner (By similarity). Inhibits MDM2-mediated ubiquitination and degradation of DLG4/PSD95, promoting DLG4 stability and regulating synaptic plasticity (PubMed:25751059). Required for the formation of dendritic spines by ensuring the correct localization of PARD3 and TIAM1 (By similarity). Potent inhibitor of angiogenesis in brain and may play a significant role as a mediator of the p53/TP53 signal in suppression of glioblastoma (By similarity). {ECO:0000250|UniProtKB:C0HL12, ECO:0000250|UniProtKB:O14514, ECO:0000269|PubMed:11875720, ECO:0000269|PubMed:17960134, ECO:0000269|PubMed:21245295, ECO:0000269|PubMed:23615608, ECO:0000269|PubMed:25751059, ECO:0000269|PubMed:26838550}.; FUNCTION: Vasculostatin-120: Inhibits angiogenesis in a CD36-dependent manner. {ECO:0000250|UniProtKB:O14514}.; FUNCTION: Vasculostatin-40: Inhibits angiogenesis. {ECO:0000250|UniProtKB:O14514}. PTM: Proteolytically cleaved to produce vasculostatin-40 and vasculostatin-120. Vasculostatin-40 is the major form and is produced through proteolytic cleavage by MMP14 between residues 321 and 329 with cleavage likely to be between Ser-326 and Leu-327. {ECO:0000250|UniProtKB:O14514}.; PTM: Ubiquitinated. {ECO:0000250|UniProtKB:O14514}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17960134, ECO:0000269|PubMed:20888903}; Multi-pass membrane protein {ECO:0000255}. Cell projection, phagocytic cup {ECO:0000269|PubMed:17960134}. Cell junction, focal adhesion {ECO:0000269|PubMed:20888903}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:C0HL12}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000269|PubMed:23595754, ECO:0000269|PubMed:23782696}.; SUBCELLULAR LOCATION: Vasculostatin-120: Secreted {ECO:0000250|UniProtKB:O14514}.; SUBCELLULAR LOCATION: Vasculostatin-40: Secreted {ECO:0000250|UniProtKB:O14514}. SUBUNIT: Interacts with ELMO1 and DOCK1 (PubMed:17960134). When bound to ELMO1 and DOCK1, acts as a module to promote apoptotic cell engulfment (PubMed:17960134). Interacts with MDM2; the interaction results in inhibition of MDM2-mediated ubiquitination and degradation of DLG4/PSD95 (PubMed:25751059). Interacts with PARD3 and TIAM1; the interaction is required for correct dendritic localization of PARD3 and TIAM1 and for dendritic spine formation (By similarity). Interacts with MAGI1, MAGI3 and BAIAP2 (By similarity). Interacts with PHYHIP (PubMed:11245925). Interacts with DLG4 (via PDZ domain) (By similarity). Vasculostatin-120: Interacts with CD36 (By similarity). Vasculostatin-120: Interacts with ARRB2 (By similarity). Interacts with BAIAP3; this interaction is direct (By similarity). {ECO:0000250|UniProtKB:C0HL12, ECO:0000250|UniProtKB:O14514, ECO:0000269|PubMed:11245925, ECO:0000269|PubMed:17960134, ECO:0000269|PubMed:25751059}. DOMAIN: The TSP type-1 repeats in the extracellular domain mediate binding to phosphatidylserine (PubMed:17960134). They are also required for bacterial recognition and binding to bacterial outer membrane lipopolysaccharide (PubMed:21245295). {ECO:0000269|PubMed:17960134, ECO:0000269|PubMed:21245295}. TISSUE SPECIFICITY: In brain, widespread expression in all neuropil-rich zones including spinal cord gray matter, cerebellar molecular layer, cerebral cortex, thalamic nuclei and basal ganglia with no expression in white matter (at protein level) (PubMed:20888903). In the cerebellar molecular layer, highly expressed in interneuron processes whereas Purkinje cells and their dendrites show weaker expression (at protein level) (PubMed:20888903). In the olfactory bulb, highly expressed in glomeruli (at protein level) (PubMed:20888903). In the retina, highly concentrated in the outer and inner plexiform layers (at protein level) (PubMed:20888903). Expressed in brain (PubMed:11245925). Enriched in hippocampus and cortex (PubMed:23595754). Also detected in other tissues including bone marrow and spleen (PubMed:17960134). {ECO:0000269|PubMed:11245925, ECO:0000269|PubMed:17960134, ECO:0000269|PubMed:20888903, ECO:0000269|PubMed:23595754}. +Q8BXK8 AGAP1_MOUSE Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 1 (AGAP-1) (Centaurin-gamma-2) (Cnt-g2) 857 94,411 Chain (1); Domain (2); Erroneous initiation (1); Modified residue (5); Nucleotide binding (3); Region (1); Repeat (2); Sequence conflict (4); Zinc finger (1) FUNCTION: GTPase-activating protein for ARF1 and, to a lesser extent, ARF5. Directly and specifically regulates the adapter protein 3 (AP-3)-dependent trafficking of proteins in the endosomal-lysosomal system (By similarity). {ECO:0000250}. PTM: Phosphorylated on tyrosines. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Associates with the endocytic compartment. {ECO:0000250}. SUBUNIT: Homodimer. Interacts with several subunits of the AP-3 protein complex: AP3M1, AP3S1 and AP3S2. Interacts with GUCY1A3 and GUCY1B3 (By similarity). {ECO:0000250}. DOMAIN: The PH domain mediates AP-3 binding. TISSUE SPECIFICITY: Widely expressed, with highest levels in brain and kidney. {ECO:0000269|PubMed:15381706}. +Q3UHD9 AGAP2_MOUSE Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 2 (AGAP-2) (Centaurin-gamma-1) (Cnt-g1) (Phosphatidylinositol 3-kinase enhancer) (PIKE) 1186 124,511 Alternative sequence (1); Chain (1); Domain (2); Modified residue (10); Nucleotide binding (3); Region (4); Repeat (2); Sequence conflict (1); Zinc finger (1) FUNCTION: GTPase-activating protein (GAP) for ARF1 and ARF5, which also shows strong GTPase activity. Participates in the prevention of neuronal apoptosis by enhancing PI3 kinase activity. Aids the coupling of metabotropic glutamate receptor 1 (GRM1) to cytoplasmic PI3 kinase by interacting with Homer scaffolding proteins, and also seems to mediate anti-apoptotic effects of NGF by activating nuclear PI3 kinase (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}. SUBUNIT: Interacts with EPB41L1, PLCG1, NF2, HOMER1 and HOMER2. {ECO:0000250}. DOMAIN: G domain binds GTP and has GTPase activity.; DOMAIN: Arf-GAP domain interacts with G domain and may regulate its GTPase activity.; DOMAIN: PH domain binds phospholipids and is required for nuclear targeting. +Q3UEG6 AGT2_MOUSE Alanine--glyoxylate aminotransferase 2, mitochondrial (AGT 2) (EC 2.6.1.44) ((R)-3-amino-2-methylpropionate--pyruvate transaminase) (EC 2.6.1.40) (Beta-ALAAT II) (Beta-alanine-pyruvate aminotransferase) (D-AIBAT) 513 57,115 Chain (1); Modified residue (13); Transit peptide (1) FUNCTION: Can metabolize asymmetric dimethylarginine (ADMA) via transamination to alpha-keto-delta-(NN-dimethylguanidino) valeric acid (DMGV). ADMA is a potent inhibitor of nitric-oxide (NO) synthase, and this activity provides mechanism through which the kidney regulates blood pressure. {ECO:0000269|PubMed:23023372}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9BYV1}. SUBUNIT: Homotetramer. {ECO:0000250}. +Q9Z0X1 AIFM1_MOUSE Apoptosis-inducing factor 1, mitochondrial (EC 1.1.1.-) (Programmed cell death protein 8) 612 66,765 Beta strand (29); Binding site (6); Chain (1); Cross-link (1); Helix (20); Modified residue (9); Motif (1); Mutagenesis (2); Nucleotide binding (3); Propeptide (1); Region (1); Transit peptide (1); Turn (7) FUNCTION: Functions both as NADH oxidoreductase and as regulator of apoptosis. In response to apoptotic stimuli, it is released from the mitochondrion intermembrane space into the cytosol and to the nucleus, where it functions as a proapoptotic factor in a caspase-independent pathway. In contrast, functions as an antiapoptotic factor in normal mitochondria via its NADH oxidoreductase activity. The soluble form (AIFsol) found in the nucleus induces 'parthanatos' i.e. caspase-independent fragmentation of chromosomal DNA. Interacts with EIF3G,and thereby inhibits the EIF3 machinery and protein synthesis,and activates casapse-7 to amplify apoptosis. Plays a critical role in caspase-independent, pyknotic cell death in hydrogen peroxide-exposed cells. Binds to DNA in a sequence-independent manner (By similarity). {ECO:0000250, ECO:0000269|PubMed:9989411}. PTM: Under normal conditions, a 54-residue N-terminal segment is first proteolytically removed during or just after translocation into the mitochondrial intermembrane space (IMS) by the mitochondrial processing peptidase (MPP) to form the inner-membrane-anchored mature form (AIFmit). During apoptosis, it is further proteolytically processed at amino-acid position 101 leading to the generation of the mature form, which is confined to the mitochondrial IMS in a soluble form (AIFsol). AIFsol is released to the cytoplasm in response to specific death signals, and translocated to the nucleus, where it induces nuclear apoptosis in a caspase-independent manner (By similarity). {ECO:0000250}.; PTM: Ubiquitination by XIAP/BIRC4 does not lead to proteasomal degradation. Ubiquitination at Lys-254 by XIAP/BIRC4 blocks its ability to bind DNA and induce chromatin degradation, thereby inhibiting its ability to induce cell death (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion intermembrane space {ECO:0000269|PubMed:9989411}. Mitochondrion inner membrane {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000269|PubMed:9989411}. Note=Proteolytic cleavage during or just after translocation into the mitochondrial intermembrane space (IMS) results in the formation of an inner-membrane-anchored mature form (AIFmit). During apoptosis, further proteolytic processing leads to a mature form, which is confined to the mitochondrial IMS in a soluble form (AIFsol). AIFsol is released to the cytoplasm in response to specific death signals, and translocated to the nucleus, where it induces nuclear apoptosis. Colocalizes with EIF3G in the nucleus and perinuclear region (By similarity). {ECO:0000250}. SUBUNIT: Monomer (oxidized form). Homodimer (reduced form). Interacts with XIAP/BIRC4. Interacts (via N-terminus) with EIF3G (via C-terminus). Interacts with PRELID1 (By similarity). {ECO:0000250}. +Q8R010 AIMP2_MOUSE Aminoacyl tRNA synthase complex-interacting multifunctional protein 2 (Multisynthase complex auxiliary component p38) (Protein JTV-1) 320 35,378 Chain (1); Domain (1); Modified residue (1); Region (2); Sequence conflict (4) FUNCTION: Required for assembly and stability of the aminoacyl-tRNA synthase complex (PubMed:12060739). Mediates ubiquitination and degradation of FUBP1, a transcriptional activator of MYC, leading to MYC down-regulation which is required for aveolar type II cell differentiation (PubMed:12819782). Blocks MDM2-mediated ubiquitination and degradation of p53/TP53 (PubMed:18695251). Functions as a proapoptotic factor (PubMed:16135753). {ECO:0000269|PubMed:12060739, ECO:0000269|PubMed:12819782, ECO:0000269|PubMed:16135753, ECO:0000269|PubMed:18695251}. PTM: Phosphorylated on serine residues in response to UV irradiation. {ECO:0000269|PubMed:18695251}.; PTM: Ubiquitinated by PRKN, leading to its degradation by the proteasome. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:18695251}. Nucleus {ECO:0000269|PubMed:18695251}. Note=Following DNA damage, dissociates from the aminoacyl-tRNA synthase complex and translocates from the cytoplasm to the nucleus. {ECO:0000269|PubMed:18695251}. SUBUNIT: Part of the multisynthetase complex (MSC), a multisubunit complex that groups tRNA ligases for Arg (RARS), Asp (DARS), Gln (QARS), Ile (IARS), Leu (LARS), Lys (KARS), Met (MARS) the bifunctional ligase for Glu and Pro (EPRS) and the auxiliary subunits AIMP1/p43, AIMP2/p38 and EEF1E1/p18 (PubMed:12060739). Interacts (via N-terminus) with KARS. Interacts with EPRS. Forms a linear complex that contains MARS, EEF1E1, EPRS and AIMP2 that is at the core of the multisubunit complex. Binds FUBP1 (via C-terminus) (By similarity). Interacts in both its unphosphorylated and phosphorylated forms with p53/TP53 (via N-terminus) in the nucleus following UV irradiation. Interacts (via N-terminus) with PRKN/parkin (via first RING-type domain). Interacts with TARSL2. {ECO:0000250|UniProtKB:Q13155, ECO:0000269|PubMed:12060739}. +Q80T32 AGRD1_MOUSE Adhesion G-protein coupled receptor D1 (G-protein coupled receptor 133) (G-protein coupled receptor PGR25) 903 99,277 Chain (1); Domain (2); Erroneous initiation (1); Glycosylation (13); Motif (1); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 600 620 Helical; Name=1. {ECO:0000255}.; TRANSMEM 633 653 Helical; Name=2. {ECO:0000255}.; TRANSMEM 663 683 Helical; Name=3. {ECO:0000255}.; TRANSMEM 702 722 Helical; Name=4. {ECO:0000255}.; TRANSMEM 741 761 Helical; Name=5. {ECO:0000255}.; TRANSMEM 790 810 Helical; Name=6. {ECO:0000255}.; TRANSMEM 814 834 Helical; Name=7. {ECO:0000255}. TOPO_DOM 27 599 Extracellular. {ECO:0000305}.; TOPO_DOM 621 632 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 654 662 Extracellular. {ECO:0000305}.; TOPO_DOM 684 701 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 723 740 Extracellular. {ECO:0000305}.; TOPO_DOM 762 789 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 811 813 Extracellular. {ECO:0000305}.; TOPO_DOM 835 903 Cytoplasmic. {ECO:0000305}. FUNCTION: Orphan receptor. Signals via G(s)-alpha family of G-proteins. {ECO:0000250|UniProtKB:Q6QNK2}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6QNK2}; Multi-pass membrane protein {ECO:0000255}. DOMAIN: A short peptide sequence (termed the Stachel sequence) in the C-terminal part of the extra-cellular domain (ECD) functions as a tethered agonist. Upon structural changes within the ECD, e.g. due to extracellular ligand binding or mechanical movements, this intramolecular agonist is exposed to the 7TM domain, triggering G-protein activation. {ECO:0000250|UniProtKB:Q6QNK2}. +Q99LF1 AKIR1_MOUSE Akirin-1 (Mighty protein) 191 21,676 Chain (1); Compositional bias (1); Erroneous initiation (1); Modified residue (2); Motif (1) FUNCTION: Functions as signal transducer for MSTN during skeletal muscle regeneration and myogenesis (PubMed:19406121, PubMed:18255059). May regulates chemotaxis of both macrophages and myoblasts by reorganising actin cytoskeleton, leading to more efficient lamellipodia formation via a PI3 kinase dependent pathway (PubMed:19406121). {ECO:0000269|PubMed:18255059, ECO:0000269|PubMed:19406121}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H9L7}. TISSUE SPECIFICITY: Expressed in macrophages and satellite cells. {ECO:0000269|PubMed:18255059, ECO:0000269|PubMed:19406121}. +Q80TS3 AGRL3_MOUSE Adhesion G protein-coupled receptor L3 (Latrophilin-3) (Lectomedin-3) 1537 171,080 Alternative sequence (8); Beta strand (31); Chain (1); Compositional bias (1); Disulfide bond (5); Domain (3); Glycosylation (9); Helix (3); Metal binding (4); Modified residue (2); Mutagenesis (10); Region (1); Sequence conflict (4); Signal peptide (1); Topological domain (8); Transmembrane (7); Turn (9) TRANSMEM 950 970 Helical; Name=1. {ECO:0000255}.; TRANSMEM 979 999 Helical; Name=2. {ECO:0000255}.; TRANSMEM 1008 1028 Helical; Name=3. {ECO:0000255}.; TRANSMEM 1051 1071 Helical; Name=4. {ECO:0000255}.; TRANSMEM 1089 1109 Helical; Name=5. {ECO:0000255}.; TRANSMEM 1143 1163 Helical; Name=6. {ECO:0000255}.; TRANSMEM 1170 1190 Helical; Name=7. {ECO:0000255}. TOPO_DOM 20 949 Extracellular. {ECO:0000255}.; TOPO_DOM 971 978 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1000 1007 Extracellular. {ECO:0000255}.; TOPO_DOM 1029 1050 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1072 1088 Extracellular. {ECO:0000255}.; TOPO_DOM 1110 1142 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1164 1169 Extracellular. {ECO:0000255}.; TOPO_DOM 1191 1537 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a role in cell-cell adhesion and neuron guidance via its interactions with FLRT2 and FLRT3 that are expressed at the surface of adjacent cells (PubMed:22405201, PubMed:25728924, PubMed:26235031). Plays a role in the development of glutamatergic synapses in the cortex (PubMed:22405201, PubMed:24739570). Important in determining the connectivity rates between the principal neurons in the cortex (PubMed:24739570). {ECO:0000269|PubMed:22405201, ECO:0000269|PubMed:24739570, ECO:0000269|PubMed:25728924, ECO:0000269|PubMed:26235031}. PTM: Proteolytically cleaved into 2 subunits, an extracellular subunit and a seven-transmembrane subunit. {ECO:0000250}.; PTM: O-glycosylated (major) and N-glycosylated. {ECO:0000269|PubMed:24739570}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22405201, ECO:0000269|PubMed:24739570}; Multi-pass membrane protein {ECO:0000305}. Cell projection, axon {ECO:0000269|PubMed:22405201}. Cell junction {ECO:0000269|PubMed:22405201}. SUBUNIT: Interacts (via olfactomedin-like domain) with FLRT3 (via extracellular domain); the interaction is direct(PubMed:22405201, PubMed:24739570, PubMed:26235031). Identified in a complex with FLRT3 and UNC5B; does not interact with UNC5B by itself. Identified in a complex with FLRT3 and UNC5D; does not interact with UNC5D by itself (By similarity). Interacts (via olfactomedin-like domain) with FLRT1 (via extracellular domain) (PubMed:22405201). Interacts (via olfactomedin-like domain) with FLRT2 (via extracellular domain) (PubMed:22405201, PubMed:25728924). Interacts (via extracellular domain) with TENM1 (PubMed:24739570). Interacts (via extracellular domain) with TENM3 (PubMed:22405201). {ECO:0000250|UniProtKB:Q9HAR2, ECO:0000269|PubMed:22405201, ECO:0000269|PubMed:24739570, ECO:0000269|PubMed:25728924, ECO:0000269|PubMed:26235031}. DOMAIN: The Olfactomedin-like domain is required for the synapse-promoting function and the interaction with FLRT3. The Olfactomedin-like and the SUEL-type lectin domains are required for the interaction with TENM1. {ECO:0000269|PubMed:24739570}. +Q8BS35 ALKMO_MOUSE Alkylglycerol monooxygenase (EC 1.14.16.5) (Transmembrane protein 195) 447 51,778 Alternative sequence (2); Chain (1); Domain (1); Erroneous initiation (1); Motif (3); Sequence caution (1); Transmembrane (6) TRANSMEM 43 63 Helical. {ECO:0000255}.; TRANSMEM 111 131 Helical. {ECO:0000255}.; TRANSMEM 170 190 Helical. {ECO:0000255}.; TRANSMEM 340 360 Helical. {ECO:0000255}.; TRANSMEM 363 383 Helical. {ECO:0000255}.; TRANSMEM 413 433 Helical. {ECO:0000255}. FUNCTION: Glyceryl-ether monooxygenase that cleaves the O-alkyl bond of ether lipids. Ether lipids are essential components of brain membranes (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in lever and small intestine. {ECO:0000269|PubMed:20643956}. +Q9JHX6 ALLC_MOUSE Probable allantoicase (EC 3.5.3.4) (Allantoate amidinohydrolase) 414 46,294 Chain (1); Sequence conflict (2) FUNCTION: The function of this enzyme is unclear as allantoicase activity is not known to exist in mammals. +Q91ZB0 ALPK2_MOUSE Alpha-protein kinase 2 (EC 2.7.11.-) (Heart alpha-protein kinase) 2144 233,298 Chain (1); Disulfide bond (2); Domain (3); Sequence conflict (5) FUNCTION: Kinases that recognize phosphorylation sites in which the surrounding peptides have an alpha-helical conformation. {ECO:0000269|PubMed:10021370}. +Q3UX43 AN13C_MOUSE Ankyrin repeat domain-containing protein 13C 541 60,150 Alternative sequence (2); Chain (1); Modified residue (1); Repeat (3); Sequence conflict (1) FUNCTION: Acts as a molecular chaperone for G protein-coupled receptors, regulating their biogenesis and exit from the ER. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}. Note=Associated with the cytosolic side. {ECO:0000250}. +Q60604 ADSV_MOUSE Adseverin (Gelsolin-like protein) (Scinderin) 715 80,254 Alternative sequence (1); Chain (1); Metal binding (6); Modified residue (2); Region (4); Repeat (6); Sequence conflict (2) FUNCTION: Ca(2+)-dependent actin filament-severing protein that has a regulatory function in exocytosis by affecting the organization of the microfilament network underneath the plasma membrane (PubMed:9671468). Severing activity is inhibited by phosphatidylinositol 4,5-bis-phosphate (PIP2) (By similarity). In vitro, also has barbed end capping and nucleating activities in the presence of Ca(2+) (PubMed:9671468). Required for megakaryocyte differentiation, maturation, polyploidization and apoptosis with the release of platelet-like particles (By similarity). Plays a role in osteoclastogenesis (OCG) and actin cytoskeletal organization in osteoclasts (PubMed:25275604, PubMed:25681458). Regulates chondrocyte proliferation and differentiation (By similarity). Inhibits cell proliferation and tumorigenesis. Signaling is mediated by MAPK, p38 and JNK pathways (By similarity). {ECO:0000250|UniProtKB:Q28046, ECO:0000250|UniProtKB:Q5ZIV9, ECO:0000250|UniProtKB:Q9Y6U3, ECO:0000269|PubMed:25275604, ECO:0000269|PubMed:25681458, ECO:0000269|PubMed:9671468}.; FUNCTION: Isoform 2: fails to nucleate actin polymerization, although it severs and caps actin filaments in a Ca(2+)-dependent manner. {ECO:0000269|PubMed:9671468}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. Cell projection, podosome {ECO:0000269|PubMed:25681458}. TISSUE SPECIFICITY: Ubiquitous. Highly expressed in mature osteoclasts (at protein level) (PubMed:25275604). Isoform 2 is expressed in blood cells (PubMed:9671468). {ECO:0000269|PubMed:25275604, ECO:0000269|PubMed:9671468}. +P97714 ADA1D_MOUSE Alpha-1D adrenergic receptor (Alpha-1A adrenergic receptor) (Alpha-1D adrenoreceptor) (Alpha-1D adrenoceptor) 562 59,858 Chain (1); Compositional bias (2); Glycosylation (2); Lipidation (1); Sequence conflict (1); Topological domain (8); Transmembrane (7) TRANSMEM 91 115 Helical; Name=1. {ECO:0000250}.; TRANSMEM 128 153 Helical; Name=2. {ECO:0000250}.; TRANSMEM 164 186 Helical; Name=3. {ECO:0000250}.; TRANSMEM 208 232 Helical; Name=4. {ECO:0000250}.; TRANSMEM 246 269 Helical; Name=5. {ECO:0000250}.; TRANSMEM 343 367 Helical; Name=6. {ECO:0000250}.; TRANSMEM 375 399 Helical; Name=7. {ECO:0000250}. TOPO_DOM 1 90 Extracellular. {ECO:0000250}.; TOPO_DOM 116 127 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 154 163 Extracellular. {ECO:0000250}.; TOPO_DOM 187 207 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 233 245 Extracellular. {ECO:0000250}.; TOPO_DOM 270 342 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 368 374 Extracellular. {ECO:0000250}.; TOPO_DOM 400 562 Cytoplasmic. {ECO:0000250}. FUNCTION: This alpha-adrenergic receptor mediates its effect through the influx of extracellular calcium. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBUNIT: Interacts with FLNA (via filamin repeat 21); increases PKA-mediated phosphorylation of FLNA. {ECO:0000250|UniProtKB:P25100}. +Q6PDY2 AEDO_MOUSE 2-aminoethanethiol dioxygenase (EC 1.13.11.19) (Cysteamine dioxygenase) 256 28,372 Chain (1); Erroneous initiation (2) TISSUE SPECIFICITY: Ubiquitous, with highest expression in brain, heart and skeletal muscle (at protein level). {ECO:0000269|PubMed:17581819}. +Q9CY02 AHSP_MOUSE Alpha-hemoglobin-stabilizing protein (Erythroid differentiation-related factor) (Erythroid-associated factor) 102 11,832 Chain (1) FUNCTION: Acts as a chaperone to prevent the harmful aggregation of alpha-hemoglobin during normal erythroid cell development. Specifically protects free alpha-hemoglobin from precipitation. {ECO:0000269|PubMed:12066189}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12066189}. SUBUNIT: Monomer. Forms a heterodimer with free alpha-hemoglobin. Does not bind beta-hemoglobin nor alpha(2)beta(2) hemoglobin A. TISSUE SPECIFICITY: Expressed in spleen, bone marrow, and blood, with highest levels in bone marrow. {ECO:0000269|PubMed:11231637, ECO:0000269|PubMed:12066189}. +Q8VHH5 AGAP3_MOUSE Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 3 (AGAP-3) (CRAM-associated GTPase) (CRAG) (Centaurin-gamma-3) (Cnt-g3) (MR1-interacting protein) (MRIP-1) 910 97,965 Alternative sequence (3); Chain (1); Compositional bias (1); Domain (2); Modified residue (4); Mutagenesis (2); Nucleotide binding (3); Region (1); Repeat (3); Zinc finger (1) FUNCTION: GTPase-activating protein for the ADP ribosylation factor family (Potential). GTPase which may be involved in the degradation of expanded polyglutamine proteins through the ubiquitin-proteasome pathway. {ECO:0000269|PubMed:16461359, ECO:0000305}. SUBCELLULAR LOCATION: Cytoplasm. Note=Upon oxidative stress, translocates to PML nuclear bodies. {ECO:0000250}. SUBUNIT: Interacts with PML. Interacts with expanded polyglutamine proteins (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed, with highest levels in brain. {ECO:0000269|PubMed:15381706, ECO:0000269|PubMed:16461359}. +Q8R3W7 AGR3_MOUSE Anterior gradient protein 3 165 19,081 Chain (1); Motif (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Required for calcium-mediated regulation of ciliary beat frequency and mucociliary clearance in the airway. Might be involved in the regulation of intracellular calcium in tracheal epithelial cells. {ECO:0000269|PubMed:25751668}. SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:Q8TD06}. Cytoplasm {ECO:0000250|UniProtKB:Q8TD06}. SUBUNIT: Interacts with LYPD3 and DAG1 (alphaDAG1). {ECO:0000250|UniProtKB:Q8TD06}. TISSUE SPECIFICITY: Expressed in the ciliated cells of the airway epithelium. Not detected in the mucous cells. {ECO:0000269|PubMed:25751668}. +Q8CJF9 AGO3_MOUSE Protein argonaute-3 (Argonaute3) (mAgo3) (EC 3.1.26.n2) (Argonaute RISC catalytic component 3) (Eukaryotic translation initiation factor 2C 3) (eIF-2C 3) (eIF2C 3) (Piwi/argonaute family protein meIF2C3) 860 97,277 Chain (1); Domain (2); Metal binding (4); Modified residue (2); Region (2); Sequence conflict (2) FUNCTION: Required for RNA-mediated gene silencing (RNAi). Binds to short RNAs such as microRNAs (miRNAs) and represses the translation of mRNAs which are complementary to them. Proposed to be involved in stabilization of small RNA derivates (riRNA) derived from processed RNA polymerase III-transcribed Alu repeats containing a DR2 retinoic acid response element (RARE) in stem cells and in the subsequent riRNA-dependent degradation of a subset of RNA polymerase II-transcribed coding mRNAs by recruiting a mRNA decapping complex involving EDC4 (PubMed:19174539). Possesses RNA slicer activity but only on select RNAs bearing 5'- and 3'-flanking sequences to the region of guide-target complementarity (By similarity). {ECO:0000255|HAMAP-Rule:MF_03032, ECO:0000269|PubMed:19174539}. SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000255|HAMAP-Rule:MF_03032}. SUBUNIT: Interacts with EIF4B, IMP8, PRMT5 and TNRC6B (By similarity). Interacts with APOBEC3F, APOBEC3G and APOBEC3H. Interacts with EDC4 (By similarity). {ECO:0000255|HAMAP-Rule:MF_03032}. +Q924K1 AIPL1_MOUSE Aryl-hydrocarbon-interacting protein-like 1 328 38,212 Chain (1); Domain (1); Repeat (3); Sequence conflict (3) FUNCTION: May be important in protein trafficking and/or protein folding and stabilization. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Interacts with NUB1. {ECO:0000250}. +Q8CJ12 AGRG2_MOUSE Adhesion G-protein coupled receptor G2 (G-protein coupled receptor 64) (Mouse epididymis-specific protein 6) (Me6) 1009 110,200 Alternative sequence (4); Chain (1); Compositional bias (4); Domain (1); Glycosylation (20); Modified residue (1); Sequence conflict (1); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 620 640 Helical; Name=1. {ECO:0000255}.; TRANSMEM 660 680 Helical; Name=2. {ECO:0000255}.; TRANSMEM 684 704 Helical; Name=3. {ECO:0000255}.; TRANSMEM 730 750 Helical; Name=4. {ECO:0000255}.; TRANSMEM 782 802 Helical; Name=5. {ECO:0000255}.; TRANSMEM 827 847 Helical; Name=6. {ECO:0000255}.; TRANSMEM 850 870 Helical; Name=7. {ECO:0000255}. TOPO_DOM 38 619 Extracellular. {ECO:0000305}.; TOPO_DOM 641 659 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 681 683 Extracellular. {ECO:0000305}.; TOPO_DOM 705 729 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 751 781 Extracellular. {ECO:0000305}.; TOPO_DOM 803 826 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 848 849 Extracellular. {ECO:0000305}.; TOPO_DOM 871 1009 Cytoplasmic. {ECO:0000305}. FUNCTION: Orphan receptor. Could be involved in a signal transduction pathway controlling epididymal function and male fertility. May regulate fluid exchange within epididymis. {ECO:0000269|PubMed:15367682}. PTM: Proteolytically cleaved into 2 subunits, an extracellular subunit and a seven-transmembrane subunit. {ECO:0000305}.; PTM: Highly glycosylated. {ECO:0000269|PubMed:12420295}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:12420295}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Heterodimer of 2 chains generated by proteolytic processing; the large extracellular N-terminal fragment and the membrane-bound C-terminal fragment predominantly remain associated and non-covalently linked. {ECO:0000305}. TISSUE SPECIFICITY: Epididymis-specific expression (at protein level). Associated with apical membranes of efferent ductule and proximal epididymal duct epithelia. Mainly expressed in the nonciliated principal cells of the proximal excurrent ducts. {ECO:0000269|PubMed:12420295, ECO:0000269|PubMed:18469038}. +O35945 AL1A7_MOUSE Aldehyde dehydrogenase, cytosolic 1 (EC 1.2.1.3) (ALDH class 1) (ALDH-E1) (ALHDII) (Aldehyde dehydrogenase family 1 member A7) (Aldehyde dehydrogenase phenobarbital-inducible) 501 54,588 Active site (2); Chain (1); Initiator methionine (1); Modified residue (10); Nucleotide binding (1); Site (1) Alcohol metabolism; ethanol degradation; acetate from ethanol: step 2/2. FUNCTION: Can oxidize benzaldehyde, propionaldehyde and acetaldehyde (By similarity). No detectable activity with retinal. {ECO:0000250, ECO:0000269|PubMed:10191271}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P13601}. SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P13601}. TISSUE SPECIFICITY: Highest level in liver, high level in lung, low level in kidney and testis. {ECO:0000269|PubMed:10191271}. +Q8VC28 AK1CD_MOUSE Aldo-keto reductase family 1 member C13 (EC 1.1.1.-) 323 37,058 Active site (1); Beta strand (10); Binding site (4); Chain (1); Helix (18); Nucleotide binding (4); Sequence conflict (4); Site (1); Turn (1) FUNCTION: Catalyzes the dehydrogenation of 17-beta-hydroxysteroids. May also exhibit significant activity with a variety of cyclic and alicyclic alcohols. Uses both NAD and NADP, but the activity is much greater with NAD than with NADP (By similarity). {ECO:0000250}. +Q8R0Y6 AL1L1_MOUSE Cytosolic 10-formyltetrahydrofolate dehydrogenase (10-FTHFDH) (FDH) (EC 1.5.1.6) (Aldehyde dehydrogenase family 1 member L1) 902 98,709 Active site (3); Binding site (2); Chain (1); Domain (1); Modified residue (10); Nucleotide binding (5); Region (3); Site (1) SUBCELLULAR LOCATION: Cytoplasm. +Q9EQX4 AIF1L_MOUSE Allograft inflammatory factor 1-like (Ionized calcium-binding adapter molecule 2) 150 17,024 Calcium binding (1); Chain (1); Domain (2); Initiator methionine (1); Modified residue (3); Sequence conflict (1) FUNCTION: Actin-binding protein that promotes actin bundling. May neither bind calcium nor depend on calcium for function (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell projection, ruffle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Colocalizes with F-actin. Partially relocates to membrane ruffles in response to invading bacteria (By similarity). {ECO:0000250}. SUBUNIT: Homodimer (Potential). Monomer (By similarity). {ECO:0000250, ECO:0000305}. +P07724 ALBU_MOUSE Serum albumin 608 68,693 Chain (1); Disulfide bond (17); Domain (3); Metal binding (5); Modified residue (14); Propeptide (1); Sequence conflict (6); Signal peptide (1) FUNCTION: Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc. PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000250|UniProtKB:P02768}. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Plasma. +Q9DB25 ALG5_MOUSE Dolichyl-phosphate beta-glucosyltransferase (DolP-glucosyltransferase) (EC 2.4.1.117) (Asparagine-linked glycosylation protein 5 homolog) 324 36,791 Chain (1); Glycosylation (1); Topological domain (2); Transmembrane (1) TRANSMEM 8 28 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 7 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 29 324 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. +O08715 AKAP1_MOUSE A-kinase anchor protein 1, mitochondrial (Dual specificity A-kinase-anchoring protein 1) (D-AKAP-1) (Protein kinase A-anchoring protein 1) (PRKA1) (Spermatid A-kinase anchor protein) (S-AKAP) 857 92,195 Alternative sequence (7); Chain (1); Domain (2); Modified residue (8); Region (1); Sequence conflict (15); Transit peptide (1) FUNCTION: Differentially targeted protein that binds to type I and II regulatory subunits of protein kinase A. Anchors them to the cytoplasmic face of the mitochondrial outer membrane or allows them to reside in the endoplasmic reticulum. Does not contain the classic KDEL endoplasmic reticulum-targeting sequence. This explains how it is able to switch its localization, either being in the endoplasmic reticulum or in the mitochondria depending on which N-terminal part begins the isoform. The longest N-terminal part only present in isoform 2 and isoform 4 acts as a suppressor of mitochondrial targeting and as an activator of recessive endoplasmic reticulum targeting motif. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:24101730, ECO:0000269|PubMed:9182549}.; SUBCELLULAR LOCATION: Isoform 2: Endoplasmic reticulum.; SUBCELLULAR LOCATION: Isoform 4: Endoplasmic reticulum.; SUBCELLULAR LOCATION: Isoform 1: Mitochondrion outer membrane.; SUBCELLULAR LOCATION: Isoform 3: Mitochondrion outer membrane.; SUBCELLULAR LOCATION: Isoform 5: Mitochondrion outer membrane.; SUBCELLULAR LOCATION: Isoform 6: Mitochondrion outer membrane. SUBUNIT: Interacts with SLC8A3. {ECO:0000269|PubMed:24101730}. DOMAIN: RII-alpha binding site, predicted to form an amphipathic helix, could participate in protein-protein interactions with a complementary surface on the R-subunit dimer. TISSUE SPECIFICITY: Highest expression in testis, heart, liver, skeletal muscle, intestine and kidney, followed by brain and lung. No expression in spleen. Isoform 1/D-AKAP1A is expressed predominantly in testis whereas isoform 4/D-AKAP1D is expressed primarily in liver. {ECO:0000269|PubMed:9065479}. +P47738 ALDH2_MOUSE Aldehyde dehydrogenase, mitochondrial (EC 1.2.1.3) (AHD-M1) (ALDH class 2) (ALDH-E2) (ALDHI) 519 56,538 Active site (2); Chain (1); Modified residue (12); Nucleotide binding (1); Sequence conflict (7); Site (1); Transit peptide (1) Alcohol metabolism; ethanol degradation; acetate from ethanol: step 2/2. FUNCTION: Is capable of converting retinaldehyde to retinoic acid. SUBCELLULAR LOCATION: Mitochondrion matrix. SUBUNIT: Homotetramer. {ECO:0000250}. +P56213 ALR_MOUSE FAD-linked sulfhydryl oxidase ALR (EC 1.8.3.2) (Augmenter of liver regeneration) 198 22,877 Binding site (2); Chain (1); Disulfide bond (4); Domain (1); Erroneous initiation (1); Nucleotide binding (3); Sequence conflict (4) FUNCTION: FAD-dependent sulfhydryl oxidase that regenerates the redox-active disulfide bonds in CHCHD4/MIA40, a chaperone essential for disulfide bond formation and protein folding in the mitochondrial intermembrane space. The reduced form of CHCHD4/MIA40 forms a transient intermolecular disulfide bridge with GFER/ERV1, resulting in regeneration of the essential disulfide bonds in CHCHD4/MIA40, while GFER/ERV1 becomes re-oxidized by donating electrons to cytochrome c or molecular oxygen (By similarity). {ECO:0000250|UniProtKB:P55789}. SUBCELLULAR LOCATION: Mitochondrion intermembrane space {ECO:0000250|UniProtKB:P55789}. Mitochondrion {ECO:0000250|UniProtKB:P55789}. SUBUNIT: Homodimer; disulfide-linked. Interacts with CHCHD4/MIA40. {ECO:0000250|UniProtKB:P55789}. TISSUE SPECIFICITY: Preferentially expressed in the liver and in testis. {ECO:0000269|PubMed:8900538}. +Q924C5 ALPK3_MOUSE Alpha-protein kinase 3 (EC 2.7.11.1) (Myocytic induction/differentiation originator) (Midori) 1678 180,199 Chain (1); Disulfide bond (1); Domain (3); Frameshift (1); Modified residue (2); Sequence conflict (2) FUNCTION: Involved in cardiomyocyte differentiation. {ECO:0000269|PubMed:11418590, ECO:0000269|PubMed:21441111}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11418590}. TISSUE SPECIFICITY: Expressed in the heart and skeletal muscle of adult mice. {ECO:0000269|PubMed:11418590}. +P29754 AGTRA_MOUSE Type-1A angiotensin II receptor (Angiotensin II type-1A receptor) (AT1A) 359 40,856 Chain (1); Disulfide bond (1); Glycosylation (3); Lipidation (1); Sequence conflict (4); Topological domain (8); Transmembrane (7) TRANSMEM 28 52 Helical; Name=1. {ECO:0000255}.; TRANSMEM 65 87 Helical; Name=2. {ECO:0000255}.; TRANSMEM 103 124 Helical; Name=3. {ECO:0000255}.; TRANSMEM 143 162 Helical; Name=4. {ECO:0000255}.; TRANSMEM 193 214 Helical; Name=5. {ECO:0000255}.; TRANSMEM 241 262 Helical; Name=6. {ECO:0000255}.; TRANSMEM 276 296 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 27 Extracellular. {ECO:0000255}.; TOPO_DOM 53 64 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 88 102 Extracellular. {ECO:0000255}.; TOPO_DOM 125 142 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 163 192 Extracellular. {ECO:0000255}.; TOPO_DOM 215 240 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 263 275 Extracellular. {ECO:0000255}.; TOPO_DOM 297 359 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for angiotensin II. Mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. PTM: C-terminal Ser or Thr residues may be phosphorylated. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBUNIT: Interacts with MAS1 (By similarity). Interacts with ARRB1 (By similarity). Interacts with FLNA (via filamin repeat 21); increases PKA-mediated phosphorylation of FLNA (By similarity). {ECO:0000250|UniProtKB:P25095, ECO:0000250|UniProtKB:P30556}. +P30561 AHR_MOUSE Aryl hydrocarbon receptor (Ah receptor) (AhR) 848 95,017 Beta strand (5); Chain (1); Compositional bias (1); Domain (4); Helix (6); Mutagenesis (20); Natural variant (13); Propeptide (1); Region (3); Sequence conflict (7); Turn (1) FUNCTION: Ligand-activated transcriptional activator. Binds to the XRE promoter region of genes it activates. Activates the expression of multiple phase I and II xenobiotic chemical metabolizing enzyme genes (such as the CYP1A1 gene). Mediates biochemical and toxic effects of halogenated aromatic hydrocarbons. Involved in cell-cycle regulation. Likely to play an important role in the development and maturation of many tissues. Regulates the circadian clock by inhibiting the basal and circadian expression of the core circadian component PER1. Inhibits PER1 by repressing the CLOCK-ARNTL/BMAL1 heterodimer mediated transcriptional activation of PER1. The heterodimer ARNT:AHR binds to core DNA sequence 5'-TGCGTG-3' within the dioxin response element (DRE) of target gene promoters and activates their transcription (PubMed:28396409). {ECO:0000269|PubMed:10639156, ECO:0000269|PubMed:10973493, ECO:0000269|PubMed:1314586, ECO:0000269|PubMed:20106950, ECO:0000269|PubMed:28396409, ECO:0000269|PubMed:7961644, ECO:0000269|PubMed:7969080, ECO:0000269|PubMed:8806883, ECO:0000269|PubMed:9427285}. PTM: Mono-ADP-ribosylated, leading to inhibit transcription activator activity of AHR. {ECO:0000250|UniProtKB:P35869}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12215427, ECO:0000269|PubMed:28396409}. Nucleus {ECO:0000269|PubMed:12215427, ECO:0000269|PubMed:20106950, ECO:0000269|PubMed:28396409}. Note=Initially cytoplasmic; upon binding with ligand and interaction with a HSP90, it translocates to the nucleus. {ECO:0000269|PubMed:20106950, ECO:0000269|PubMed:28396409}. SUBUNIT: Homodimer (PubMed:24001774). Interacts with IVNS1ABP (By similarity). Efficient DNA binding requires dimerization with another bHLH protein. Interacts with coactivators including SRC-1, RIP140 and NOCA7, and with the corepressor SMRT. Interacts with MYBBP1A and NEDD8 (PubMed:11956195, PubMed:12215427). Interacts with ARNTL/BMAL1 (PubMed:20106950). Interacts with HSP90AB1 (PubMed:15581363). Interacts with ARNT; the heterodimer ARNT:AHR binds to core DNA sequence 5'-TGCGTG-3' within the dioxin response element (DRE) of target gene promoters and activates their transcription (PubMed:24001774, PubMed:28396409). Interacts with TIPARP; leading to mono-ADP-ribosylation of AHR and subsequent inhibition of AHR (By similarity). {ECO:0000250|UniProtKB:P35869, ECO:0000269|PubMed:11956195, ECO:0000269|PubMed:12215427, ECO:0000269|PubMed:15581363, ECO:0000269|PubMed:20106950, ECO:0000269|PubMed:24001774, ECO:0000269|PubMed:28396409}. DOMAIN: The PAS 1 domain is essential for dimerization and also required for AHR:ARNT heterodimerization. {ECO:0000269|PubMed:24001774}. TISSUE SPECIFICITY: Expressed in all tissues tested including brain, heart, kidney, liver, lung, muscle, ovary, skin, spleen and thymus. {ECO:0000269|PubMed:10639156}. +Q8C4Q6 AIDA_MOUSE Axin interactor, dorsalization-associated protein (Axin interaction partner and dorsalization antagonist) 305 34,888 Alternative sequence (1); Beta strand (12); Chain (1); Coiled coil (1); Helix (8); Region (1); Sequence conflict (3); Turn (2) FUNCTION: Acts as a ventralizing factor during embryogenesis (By similarity). Inhibits axin-mediated JNK activation by binding axin and disrupting axin homodimerization. This in turn antagonizes a Wnt/beta-catenin-independent dorsalization pathway activated by AXIN/JNK-signaling. {ECO:0000250, ECO:0000269|PubMed:17681137}. SUBUNIT: Interacts with AXIN1. {ECO:0000269|PubMed:17681137}. +Q80VW7 AKNA_MOUSE AT-hook-containing transcription factor 1404 153,123 Alternative sequence (5); Chain (1); DNA binding (1); Erroneous initiation (1); Modified residue (16); Region (2); Sequence conflict (21) FUNCTION: Transcription factor that specifically activates the expression of the CD40 receptor and its ligand CD40L/CD154, two cell surface molecules on lymphocytes that are critical for antigen-dependent-B-cell development. Binds to A/T-rich promoters (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +G3UWD5 AKAI1_MOUSE A-kinase anchor protein inhibitor 1 69 7,751 Chain (1) FUNCTION: Protein kinase A (PKA)-binding protein. Binds to type II regulatory subunits of protein kinase A (PKA) and may block the A-kinase anchoring protein (AKAP)-mediated subcellular localization of PKA. {ECO:0000250|UniProtKB:P0CW23}. SUBUNIT: Binds cAMP-dependent protein kinase (PKA). Interacts specifically with RII-regulatory subunits of PKA (PRKAR2A and PRKAR2B). {ECO:0000250|UniProtKB:P0CW23}. DOMAIN: The RII-alpha binding site, predicted to form an amphipathic helix, could participate in protein-protein interactions with a complementary surface on the R-subunit dimer. TISSUE SPECIFICITY: Preferentially expressed in the neural tissues. {ECO:0000269|PubMed:25653177}. +P97793 ALK_MOUSE ALK tyrosine kinase receptor (EC 2.7.10.1) (Anaplastic lymphoma kinase) (CD antigen CD246) 1621 174,948 Active site (1); Binding site (7); Chain (1); Compositional bias (1); Domain (4); Glycosylation (16); Modified residue (6); Nucleotide binding (2); Region (1); Sequence conflict (6); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1043 1063 Helical. {ECO:0000255}. TOPO_DOM 19 1042 Extracellular. {ECO:0000255}.; TOPO_DOM 1064 1621 Cytoplasmic. {ECO:0000255}. FUNCTION: Neuronal receptor tyrosine kinase that is essentially and transiently expressed in specific regions of the central and peripheral nervous systems and plays an important role in the genesis and differentiation of the nervous system. Transduces signals from ligands at the cell surface, through specific activation of the mitogen-activated protein kinase (MAPK) pathway. Phosphorylates almost exclusively at the first tyrosine of the Y-x-x-x-Y-Y motif. Following activation by ligand, ALK induces tyrosine phosphorylation of CBL, FRS2, IRS1 and SHC1, as well as of the MAP kinases MAPK1/ERK2 and MAPK3/ERK1. Acts as a receptor for ligands pleiotrophin (PTN), a secreted growth factor, and midkine (MDK), a PTN-related factor, thus participating in PTN and MDK signal transduction. PTN-binding induces MAPK pathway activation, which is important for the anti-apoptotic signaling of PTN and regulation of cell proliferation. MDK-binding induces phosphorylation of the ALK target insulin receptor substrate (IRS1), activates mitogen-activated protein kinases (MAPKs) and PI3-kinase, resulting also in cell proliferation induction. Drives NF-kappa-B activation, probably through IRS1 and the activation of the AKT serine/threonine kinase. Recruitment of IRS1 to activated ALK and the activation of NF-kappa-B are essential for the autocrine growth and survival signaling of MDK. {ECO:0000269|PubMed:15226403, ECO:0000269|PubMed:16458083, ECO:0000269|PubMed:16878150, ECO:0000269|PubMed:19200234}. PTM: Phosphorylated at tyrosine residues by autocatalysis, which activates kinase activity. In cells not stimulated by a ligand, receptor protein tyrosine phosphatase beta and zeta complex (PTPRB/PTPRZ1) dephosphorylates ALK at the sites in ALK that are undergoing autophosphorylation through autoactivation. {ECO:0000250}.; PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Membrane attachment was crucial for promotion of neuron-like differentiation and cell proliferation arrest through specific activation of the MAP kinase pathway. {ECO:0000250}. SUBUNIT: Homodimer. Homodimerizes when bound to ligand (By similarity). Interacts with CBL, IRS1, PIK3R1, PLCG1 and SHC1. Interacts with FRS2, PTN and MDK. {ECO:0000250, ECO:0000269|PubMed:15226403, ECO:0000269|PubMed:16878150}. TISSUE SPECIFICITY: Mainly expressed in central nervous system (CNS) and other parts of the brain. Expression is also found in peripheral nervous systems, eye, nasal epithelium, olfactory nerve, tongue, skin, tissue surrounding the esophagus, stomach, midgut, as well as testis and ovary. {ECO:0000269|PubMed:16458083}. +O55189 AMBN_MOUSE Ameloblastin 407 43,664 Chain (1); Modified residue (2); Signal peptide (1) FUNCTION: Involved in the mineralization and structural organization of enamel. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. TISSUE SPECIFICITY: Ameloblast-specific. +Q8K2U2 ALKB6_MOUSE Alpha-ketoglutarate-dependent dioxygenase alkB homolog 6 (EC 1.14.11.-) (Alkylated DNA repair protein alkB homolog 6) 238 26,776 Chain (1); Domain (1); Frameshift (1); Metal binding (3); Region (2) FUNCTION: Probable dioxygenase that requires molecular oxygen, alpha-ketoglutarate and iron. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Interacts with VCPKMT. {ECO:0000250}. +O70137 ALX3_MOUSE Homeobox protein aristaless-like 3 (Proline-rich transcription factor ALX3) 343 36,851 Chain (1); DNA binding (1) FUNCTION: Transcriptional regulator with a possible role in patterning of mesoderm during development. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. TISSUE SPECIFICITY: Predominantly in neural crest-derived mesenchyme and in lateral plate mesoderm. Prominent expression in frontonasal head mesenchyme and in the first and second pharyngeal arches and some of their derivatives. High expression is also seen in the tail and in many derivatives of the lateral plate mesoderm including the limbs, the body wall, and the genital tubercle. +Q9JHT5 AMMR1_MOUSE AMME syndrome candidate gene 1 protein homolog 344 36,031 Chain (1); Compositional bias (2); Domain (1); Modified residue (1) SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y4X0}. +Q6PD24 AN13D_MOUSE Ankyrin repeat domain-containing protein 13D 605 68,076 Chain (1); Domain (4); Erroneous initiation (1); Modified residue (2) FUNCTION: Ubiquitin-binding protein that specifically recognizes and binds 'Lys-63'-linked ubiquitin. Does not bind 'Lys-48'-linked ubiquitin. Positively regulates the internalization of ligand-activated EGFR by binding to the Ub moiety of ubiquitinated EGFR at the cell membrane (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane. Late endosome. Note=Interaction with EGFR may enhance association with the cell membrane. {ECO:0000250}. SUBUNIT: Interacts with EGFR (ubiquitinated); the interaction is direct and may regulate EGFR internalization. {ECO:0000250}. +Q00897 A1AT4_MOUSE Alpha-1-antitrypsin 1-4 (Alpha-1 protease inhibitor 4) (Serine protease inhibitor 1-4) (Serine protease inhibitor A1d) (Serpin A1d) 413 45,998 Chain (1); Glycosylation (3); Region (1); Signal peptide (1); Site (1) FUNCTION: Inhibitor of serine proteases. Can inhibit trypsin and chymotrypsin; relatively ineffective against elastase. {ECO:0000269|PubMed:11961105, ECO:0000269|PubMed:8619829}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11961105, ECO:0000269|PubMed:8619829}. DOMAIN: The reactive center loop (RCL) extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site within the RCL, establishing a covalent linkage between the carboxyl group of the serpin reactive site and the serine hydroxyl of the protease. The resulting inactive serpin-protease complex is highly stable (By similarity). Variability within the reactive center loop (RCL) sequences of Serpina1-related genes may determine target protease specificity. {ECO:0000250}. +P63115 AAA1_MOUSE Asc-type amino acid transporter 1 (Asc-1) (D-serine transporter) (Solute carrier family 7 member 10) 530 57,549 Chain (1); Transmembrane (10) TRANSMEM 46 66 Helical. {ECO:0000255}.; TRANSMEM 78 98 Helical. {ECO:0000255}.; TRANSMEM 119 139 Helical. {ECO:0000255}.; TRANSMEM 192 212 Helical. {ECO:0000255}.; TRANSMEM 274 294 Helical. {ECO:0000255}.; TRANSMEM 316 336 Helical. {ECO:0000255}.; TRANSMEM 368 388 Helical. {ECO:0000255}.; TRANSMEM 394 414 Helical. {ECO:0000255}.; TRANSMEM 430 450 Helical. {ECO:0000255}.; TRANSMEM 454 474 Helical. {ECO:0000255}. FUNCTION: Sodium-independent, high affinity transport of small neutral D- and L-amino acids and amino acid-related compounds. May play a role in the modulation of glutamatergic transmission through mobilization of D-serine at the glutamatergic synapse. {ECO:0000269|PubMed:10734121}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Disulfide-linked heterodimer with the amino acid transport protein SLC3A2/4F2hc. {ECO:0000269|PubMed:10734121}. TISSUE SPECIFICITY: Highly expressed in brain and lung, and to a lesser extent in placenta and small intestine. {ECO:0000269|PubMed:10734121}. +P32304 5HT7R_MOUSE 5-hydroxytryptamine receptor 7 (5-HT-7) (5-HT7) (5-HT-X) (Serotonin receptor 7) 448 49,916 Chain (1); Disulfide bond (1); Glycosylation (2); Lipidation (1); Sequence conflict (4); Topological domain (8); Transmembrane (7) TRANSMEM 85 111 Helical; Name=1. {ECO:0000250}.; TRANSMEM 122 147 Helical; Name=2. {ECO:0000250}.; TRANSMEM 160 181 Helical; Name=3. {ECO:0000250}.; TRANSMEM 202 225 Helical; Name=4. {ECO:0000250}.; TRANSMEM 241 263 Helical; Name=5. {ECO:0000250}.; TRANSMEM 332 355 Helical; Name=6. {ECO:0000250}.; TRANSMEM 368 390 Helical; Name=7. {ECO:0000250}. TOPO_DOM 1 84 Extracellular. {ECO:0000250}.; TOPO_DOM 112 121 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 148 159 Extracellular. {ECO:0000250}.; TOPO_DOM 182 201 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 226 240 Extracellular. {ECO:0000250}.; TOPO_DOM 264 331 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 356 367 Extracellular. {ECO:0000250}.; TOPO_DOM 391 448 Cytoplasmic. {ECO:0000250}. FUNCTION: This is one of the several different receptors for 5-hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. The activity of this receptor is mediated by G proteins that stimulate adenylate cyclase. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q60614 AA2BR_MOUSE Adenosine receptor A2b 332 36,120 Chain (1); Disulfide bond (1); Glycosylation (2); Lipidation (1); Region (3); Sequence conflict (2); Topological domain (8); Transmembrane (7) TRANSMEM 9 33 Helical; Name=1. {ECO:0000250}.; TRANSMEM 44 67 Helical; Name=2. {ECO:0000250}.; TRANSMEM 79 101 Helical; Name=3. {ECO:0000250}.; TRANSMEM 122 144 Helical; Name=4. {ECO:0000250}.; TRANSMEM 179 203 Helical; Name=5. {ECO:0000250}.; TRANSMEM 236 259 Helical; Name=6. {ECO:0000250}.; TRANSMEM 268 291 Helical; Name=7. {ECO:0000250}. TOPO_DOM 1 8 Extracellular. {ECO:0000250}.; TOPO_DOM 34 43 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 68 78 Extracellular. {ECO:0000250}.; TOPO_DOM 102 121 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 145 178 Extracellular. {ECO:0000250}.; TOPO_DOM 204 235 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 260 267 Extracellular. {ECO:0000250}.; TOPO_DOM 292 332 Cytoplasmic. {ECO:0000250}. FUNCTION: Receptor for adenosine. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q2XU92 ACBG2_MOUSE Long-chain-fatty-acid--CoA ligase ACSBG2 (EC 6.2.1.3) (Acyl-CoA synthetase bubblegum family member 2) (Bubblegum-related protein) 667 74,319 Binding site (3); Chain (1); Nucleotide binding (2) FUNCTION: Mediates activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Able to activate long-chain fatty acids. Also able to activate very long-chain fatty acids; however, the relevance of such activity is unclear in vivo. Has increased ability to activate oleic and linoleic acid. May play a role in spermatogenesis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein. TISSUE SPECIFICITY: Testis- and brainstem-specific. Expressed in pubertal and adult testis. Enriched in germ cells and Sertoli cells while present at a lower level in Leydig cells. Present in testicular Sertoli cells and large motoneurons in the medulla oblongata and cervical spinal cord (at protein level). {ECO:0000269|PubMed:16371355, ECO:0000269|PubMed:16762313}. +Q9JKX4 AATF_MOUSE Protein AATF (Apoptosis-antagonizing transcription factor) (Rb-binding protein Che-1) (Traube protein) 526 59,482 Alternative sequence (4); Chain (1); Compositional bias (1); Initiator methionine (1); Modified residue (7); Region (3); Sequence conflict (6) FUNCTION: May function as a general inhibitor of the histone deacetylase HDAC1. Binding to the pocket region of RB1 may displace HDAC1 from RB1/E2F complexes, leading to activation of E2F target genes and cell cycle progression. Conversely, displacement of HDAC1 from SP1 bound to the CDKN1A promoter leads to increased expression of this CDK inhibitor and blocks cell cycle progression (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11071758}. SUBUNIT: Binds PAWR, POLR2J, RB1/RB, RBL1/P107, RBL2/P130, and SP1. May also bind MAPT (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in adrenal gland, brain (Purkinje cells), heart, kidney, liver, lung, muscle, ovary and testis (at the protein level). {ECO:0000269|PubMed:11071758, ECO:0000269|PubMed:14636992}. +Q8BYZ1 ABI3_MOUSE ABI gene family member 3 (New molecule including SH3) (Nesh) 367 39,107 Alternative sequence (1); Chain (1); Coiled coil (1); Compositional bias (1); Domain (1); Modified residue (3); Sequence conflict (1) FUNCTION: Inhibits ectopic tumor cell metastasis of SRD cells. In vitro, reduces cell motility. {ECO:0000269|PubMed:11956071}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: May interact with PAK1 and PAK2. Probably interacts with TARSH (By similarity). {ECO:0000250}. +P41233 ABCA1_MOUSE ATP-binding cassette sub-family A member 1 (ATP-binding cassette transporter 1) (ABC-1) (ATP-binding cassette 1) 2261 253,912 Chain (1); Disulfide bond (2); Domain (2); Erroneous initiation (2); Glycosylation (22); Lipidation (4); Modified residue (3); Nucleotide binding (2); Sequence conflict (4); Topological domain (2); Transmembrane (15) TRANSMEM 22 42 Helical. {ECO:0000255}.; TRANSMEM 640 660 Helical. {ECO:0000255}.; TRANSMEM 683 703 Helical. {ECO:0000255}.; TRANSMEM 716 736 Helical. {ECO:0000255}.; TRANSMEM 745 765 Helical. {ECO:0000255}.; TRANSMEM 777 797 Helical. {ECO:0000255}.; TRANSMEM 827 847 Helical. {ECO:0000255}.; TRANSMEM 941 961 Helical. {ECO:0000255}.; TRANSMEM 1351 1371 Helical. {ECO:0000255}.; TRANSMEM 1657 1677 Helical. {ECO:0000255}.; TRANSMEM 1703 1723 Helical. {ECO:0000255}.; TRANSMEM 1735 1755 Helical. {ECO:0000255}.; TRANSMEM 1768 1788 Helical. {ECO:0000255}.; TRANSMEM 1802 1822 Helical. {ECO:0000255}.; TRANSMEM 1852 1872 Helical. {ECO:0000255}. TOPO_DOM 43 639 Extracellular. {ECO:0000250}.; TOPO_DOM 1372 1656 Extracellular. {ECO:0000250}. FUNCTION: cAMP-dependent and sulfonylurea-sensitive anion transporter. Involved in the efflux of intracellular cholesterol and phospholipids and their transfer to apoliproteins to form nascent high density lipoproteins/HDLs. {ECO:0000250|UniProtKB:O95477}. PTM: Phosphorylation on Ser-2054 regulates phospholipid efflux. {ECO:0000250}.; PTM: Palmitoylation by DHHC8 is essential for membrane localization. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Interacts with MEGF10 (PubMed:17205124). May interact with APOE1; functionally associated with APOE1 in the biogenesis of HDLs (By similarity). {ECO:0000250|UniProtKB:O95477, ECO:0000269|PubMed:17205124}. DOMAIN: Multifunctional polypeptide with two homologous halves, each containing a hydrophobic membrane-anchoring domain and an ATP binding cassette (ABC) domain. TISSUE SPECIFICITY: Widely expressed in adult tissues. Highest levels are found in pregnant uterus and uterus. +P31786 ACBP_MOUSE Acyl-CoA-binding protein (ACBP) (Diazepam-binding inhibitor) (DBI) (Endozepine) (EP) 87 10,000 Binding site (4); Chain (1); Domain (1); Initiator methionine (1); Modified residue (12); Region (1) FUNCTION: Binds medium- and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA esters. It is also able to displace diazepam from the benzodiazepine (BZD) recognition site located on the GABA type A receptor. It is therefore possible that this protein also acts as a neuropeptide to modulate the action of the GABA receptor. SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:P07108}. Golgi apparatus {ECO:0000250|UniProtKB:P07108}. Note=Golgi localization is dependent on ligand binding. {ECO:0000250|UniProtKB:P07108}. SUBUNIT: Monomer. +P63101 1433Z_MOUSE 14-3-3 protein zeta/delta (Protein kinase C inhibitor protein 1) (KCIP-1) (SEZ-2) 245 27,771 Chain (1); Modified residue (8); Sequence conflict (4); Site (2) FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. PTM: The delta, brain-specific form differs from the zeta form in being phosphorylated (By similarity). Phosphorylation on Ser-184 by MAPK8; promotes dissociation of BAX and translocation of BAX to mitochondria. Phosphorylation on Thr-232; inhibits binding of RAF1 (By similarity). Phosphorylated on Ser-58 by PKA and protein kinase C delta type catalytic subunit in a sphingosine-dependent fashion. Phosphorylation on Ser-58 by PKA; disrupts homodimerization and heterodimerization with YHAE and TP53. {ECO:0000250, ECO:0000269|PubMed:9705322}. SUBCELLULAR LOCATION: Cytoplasm. Melanosome. Note=Located to stage I to stage IV melanosomes. {ECO:0000250}. SUBUNIT: Homodimer. Heterodimerizes with YWHAE (By similarity). Homo- and hetero-dimerization is inhibited by phosphorylation on Ser-58 (By similarity). Interacts with FOXO4, NOXA1, SSH1 and ARHGEF2. Interacts with CDK16 and with WEE1 (C-terminal). Interacts with MLF1 (phosphorylated form); the interaction retains it in the cytoplasm. Interacts with BSPRY. Interacts with Thr-phosphorylated ITGB2 (By similarity). Interacts with Pseudomonas aeruginosa exoS (unphosphorylated form). Interacts with BAX; the interaction occurs in the cytoplasm. Under stress conditions, MAPK8-mediated phosphorylation releases BAX to mitochondria. Interacts with phosphorylated RAF1; the interaction is inhibited when YWHAZ is phosphorylated on Thr-232. Interacts with TP53; the interaction enhances p53 transcriptional activity. The Ser-58 phosphorylated form inhibits this interaction and p53 transcriptional activity. Interacts with ABL1 (phosphorylated form); the interaction retains ABL1 in the cytoplasm. Interacts with PKA-phosphorylated AANAT; the interaction modulates AANAT enzymatic activity by increasing affinity for arylalkylamines and acetyl-CoA and protecting the enzyme from dephosphorylation and proteasomal degradation (By similarity). It may also prevent thiol-dependent inactivation (By similarity). Interacts with AKT1; the interaction phosphorylates YWHAZ and modulates dimerization (By similarity). Interacts with GAB2 (By similarity). Interacts with SAMSN1. Interacts with BCL2L11 and TLK2. Interacts with the 'Thr-369' phosphorylated form of DAPK2 (PubMed:26047703). Interacts with PI4KB, TBC1D22A and TBC1D22B (By similarity). Interacts with ZFP36L1 (via phosphorylated form); this interaction occurs in a p38 MAPK- and AKT-signaling pathways (PubMed:22701344). Interacts with SLITRK1 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P63104, ECO:0000269|PubMed:10455159, ECO:0000269|PubMed:12176995, ECO:0000269|PubMed:20478393, ECO:0000269|PubMed:21478148, ECO:0000269|PubMed:22701344, ECO:0000269|PubMed:26047703, ECO:0000269|PubMed:9016762, ECO:0000269|PubMed:9197417}. +Q9Z131 3BP5_MOUSE SH3 domain-binding protein 5 (SH3BP-5) (SH3 domain-binding protein that preferentially associates with BTK) 463 51,807 Alternative sequence (2); Chain (1); Coiled coil (4); Compositional bias (2); Erroneous initiation (1); Modified residue (5); Region (1); Sequence conflict (1) FUNCTION: Functions as guanine nucleotide exchange factor (GEF) with specificity for RAB11A and RAB25 (By similarity). Inhibits the auto- and transphosphorylation activity of BTK. Plays a negative regulatory role in BTK-related cytoplasmic signaling in B-cells. May be involved in BCR-induced apoptotic cell death. {ECO:0000250|UniProtKB:O60239, ECO:0000269|PubMed:10339589}. SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:O60239}; Peripheral membrane protein {ECO:0000250|UniProtKB:O60239}. Mitochondrion {ECO:0000250|UniProtKB:O60239}. Note=Colocalizes with RAB11A on cytoplasmic vesicle membranes. {ECO:0000250|UniProtKB:O60239}. SUBUNIT: Interacts with BTK (By similarity). Interacts with all isoforms of MAPK8, MAPK9, MAPK10 and MAPK12 (By similarity). Interacts with GDP-bound and nucleotide-free forms of RAB11A (PubMed:26506309). {ECO:0000250|UniProtKB:O60239, ECO:0000269|PubMed:26506309}. DOMAIN: The N-terminal half of the protein mediates interaction with RAB11A and functions as guanine nucleotide exchange factor. Four long alpha-helices (interrupted by a central kink) assemble into coiled coils, giving rise to a 'V' shape. {ECO:0000250|UniProtKB:O60239}. +Q61694 3BHS5_MOUSE NADPH-dependent 3-keto-steroid reductase Hsd3b5 (3 beta-hydroxysteroid dehydrogenase type 5) (3 beta-hydroxysteroid dehydrogenase type V) (3 beta-HSD V) (EC 1.1.1.270) (Dihydrotestosterone 3-ketoreductase) (EC 1.1.1.210) 373 41,892 Active site (1); Binding site (2); Chain (1); Modified residue (1); Nucleotide binding (1); Sequence conflict (4); Transmembrane (1) TRANSMEM 288 308 Helical. {ECO:0000255}. Steroid metabolism. FUNCTION: Responsible for the reduction of the oxo group on the C-3 of 5alpha-androstane steroids. Catalyzes the conversion of dihydrotestosterone to its inactive form 5alpha-androstanediol, that does not bind androgen receptor/AR. Does not function as an isomerase. {ECO:0000269|PubMed:7491113}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. Mitochondrion membrane; Single-pass membrane protein. TISSUE SPECIFICITY: Expressed in the male liver, starting in late puberty. {ECO:0000269|PubMed:7491113}. +Q8C0J2 A16L1_MOUSE Autophagy-related protein 16-1 (APG16-like 1) 607 68,172 Alternative sequence (5); Chain (1); Coiled coil (1); Erroneous initiation (1); Modified residue (3); Motif (1); Mutagenesis (2); Region (3); Repeat (7); Sequence conflict (4) FUNCTION: Plays an essential role in autophagy: interacts with ATG12-ATG5 to mediate the conjugation of phosphatidylethanolamine (PE) to LC3 (MAP1LC3A, MAP1LC3B or MAP1LC3C), to produce a membrane-bound activated form of LC3 named LC3-II. Thereby, controls the elongation of the nascent autophagosomal membrane (PubMed:18849966, PubMed:12665549, PubMed:24954904, PubMed:24553140, PubMed:23392225). Regulates mitochondrial antiviral signaling (MAVS)-dependent type I interferon (IFN-I) production (By similarity). Negatively regulates NOD1- and NOD2-driven inflammatory cytokine response (PubMed:24238340). Instead, promotes with NOD2 an autophagy-dependent antibacterial pathway. Plays a role in regulating morphology and function of Paneth cell. {ECO:0000250|UniProtKB:Q676U5, ECO:0000269|PubMed:12665549, ECO:0000269|PubMed:18849966, ECO:0000269|PubMed:23392225, ECO:0000269|PubMed:24238340, ECO:0000269|PubMed:24553140, ECO:0000269|PubMed:24954904}. PTM: Proteolytic cleavage by activated CASP3 leads to degradation and may regulate autophagy upon cellular stress and apoptotic stimuli. {ECO:0000269|PubMed:24553140}.; PTM: Phosphorylation at Ser-139 promotes association with the ATG12-ATG5 conjugate to form the ATG12-ATG5-ATG16L1 complex. {ECO:0000250|UniProtKB:Q676U5}. SUBCELLULAR LOCATION: Cytoplasm. Preautophagosomal structure membrane {ECO:0000269|PubMed:24954904}; Peripheral membrane protein {ECO:0000305}. Note=Recruited to omegasomes membranes by WIPI2. Omegasomes are endoplasmic reticulum connected strutures at the origin of preautophagosomal structures. Localized to preautophagosomal structure (PAS) where it is involved in the membrane targeting of ATG5. Localizes also to discrete punctae along the ciliary axoneme. {ECO:0000269|PubMed:24954904}. SUBUNIT: Homodimer (By similarity). Homooligomer (PubMed:12665549). Interacts with WIPI1 (By similarity). Interacts with WIPI2 (PubMed:24954904). Interacts with RB1CC1; the interaction is required for ULK1 complex-dependent autophagy (PubMed:23392225, PubMed:23262492). Interacts with ATG5 (PubMed:12665549). Part of either the minor and major complexes respectively composed of 4 sets of ATG12-ATG5 and ATG16L1 (400 kDa) or 8 sets of ATG12-ATG5 and ATG16L1 (800 kDa). Interacts with RAB33B (PubMed:18448665). Interacts (via WD repeats) with TMEM59; the interaction mediates unconventional autophagic activity of TMEM59 (By similarity). Interacts with TLR2 and NOD2 (By similarity). Interacts (via WD repeats) with MEFV (By similarity). Interacts (via N-terminal) with CLTC (By similarity). Interacts with NOD2 (By similarity). Interacts with TUFM (By similarity). Interacts with TRIM16 (By similarity). {ECO:0000250|UniProtKB:Q676U5, ECO:0000269|PubMed:12665549, ECO:0000269|PubMed:18448665, ECO:0000269|PubMed:23262492, ECO:0000269|PubMed:23392225, ECO:0000269|PubMed:24954904}. TISSUE SPECIFICITY: Widely expressed. Isoform 1: Expressed in liver. Isoform 2: Highly expressed in liver. Isoform 3: Expressed in brain. {ECO:0000269|PubMed:12665549}. +Q9R078 AAKB1_MOUSE 5'-AMP-activated protein kinase subunit beta-1 (AMPK subunit beta-1) (AMPKb) 270 30,308 Chain (1); Initiator methionine (1); Lipidation (1); Modified residue (13); Region (1) FUNCTION: Non-catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Beta non-catalytic subunit acts as a scaffold on which the AMPK complex assembles, via its C-terminus that bridges alpha (PRKAA1 or PRKAA2) and gamma subunits (PRKAG1, PRKAG2 or PRKAG3) (By similarity). {ECO:0000250}. PTM: Phosphorylated when associated with the catalytic subunit (PRKAA1 or PRKAA2). Phosphorylated by ULK1; leading to negatively regulate AMPK activity and suggesting the existence of a regulatory feedback loop between ULK1 and AMPK. {ECO:0000269|PubMed:21460634}. SUBUNIT: AMPK is a heterotrimer of an alpha catalytic subunit (PRKAA1 or PRKAA2), a beta (PRKAB1 or PRKAB2) and a gamma non-catalytic subunits (PRKAG1, PRKAG2 or PRKAG3). Interacts with FNIP1 and FNIP2 (By similarity). {ECO:0000250}. DOMAIN: The glycogen-binding domain may target AMPK to glycogen so that other factors like glycogen-bound debranching enzyme or protein phosphatases can directly affect AMPK activity. {ECO:0000250}. +P62484 ABI2_MOUSE Abl interactor 2 (Abelson interactor 2) (Abi-2) (Abl-binding protein 3) (AblBP3) (Arg-binding protein 1) (ArgBP1) 446 49,387 Chain (1); Compositional bias (1); Domain (2); Modified residue (5) FUNCTION: Regulator of actin cytoskeleton dynamics underlying cell motility and adhesion. Functions as a component of the WAVE complex, which activates actin nucleating machinery Arp2/3 to drive lamellipodia formation (By similarity). Acts as regulator and substrate of nonreceptor tyrosine kinases ABL1 and ABL2 involved in processes linked to cell growth and differentiation. Positively regulates ABL1-mediated phosphorylation of ENAH, which is required for proper polymerization of nucleated actin filaments at the leading edge (By similarity). Contributes to the regulation of actin assembly at the tips of neuron projections. In particular, controls dendritic spine morphogenesis and may promote dendritic spine specification toward large mushroom-type spines known as repositories of memory in the brain (PubMed:15572692). In hippocampal neurons, may mediate actin-dependent BDNF-NTRK2 early endocytic trafficking that triggers dendrite outgrowth (PubMed:27605705). Participates in ocular lens morphogenesis, likely by regulating lamellipodia-driven adherens junction formation at the epithelial cell-secondary lens fiber interface (PubMed:15572692). Also required for nascent adherens junction assembly in epithelial cells (By similarity). {ECO:0000250|UniProtKB:Q9NYB9, ECO:0000269|PubMed:15572692, ECO:0000269|PubMed:27605705}. PTM: Phosphorylated by ABL1. {ECO:0000250|UniProtKB:Q9NYB9}. SUBCELLULAR LOCATION: Cell projection, lamellipodium {ECO:0000269|PubMed:11516653}. Cell projection, filopodium {ECO:0000250|UniProtKB:Q9NYB9}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9NYB9}. Cell junction, adherens junction {ECO:0000269|PubMed:15572692}. Cell projection, dendritic spine {ECO:0000269|PubMed:15572692}. Note=Localized to the protruding lamellipodia and filopodia tips (By similarity). Present at nascent adherens junctions where it clusters adjacent to the tips of F-actin protrusions (By similarity). {ECO:0000250|UniProtKB:Q9NYB9}. SUBUNIT: Component of the WAVE complex composed of ABI2, CYFIP1 or CYFIP2, BRK1, NCKAP1 and WASF1/WAVE1. Within the complex, a heterodimer containing NCKAP1 and CYFIP1 interacts with a heterotrimer formed by WASF1/WAVE1, ABI2 and BRK1. CYFIP2 binds to activated RAC1 which causes the complex to dissociate, releasing activated WASF1 (By similarity). Interacts (via SH3 domain) with ABL1 and ABL2 (By similarity). {ECO:0000250|UniProtKB:Q9NYB9}. DOMAIN: The SH3 domain is critical for binding to ABL1 and ABL2. {ECO:0000250|UniProtKB:Q9NYB9}. TISSUE SPECIFICITY: Expresses in embryonic and adult brain. In adult brain prominently expressed in the neocortex, hippocampus and dentate gyrus. {ECO:0000269|PubMed:10995551}. +Q8K440 ABC8B_MOUSE ATP-binding cassette sub-family A member 8-B 1620 183,039 Alternative sequence (1); Chain (1); Domain (2); Erroneous initiation (1); Glycosylation (1); Nucleotide binding (2); Sequence conflict (2); Transmembrane (15) TRANSMEM 30 50 Helical. {ECO:0000255}.; TRANSMEM 223 243 Helical. {ECO:0000255}.; TRANSMEM 267 287 Helical. {ECO:0000255}.; TRANSMEM 298 318 Helical. {ECO:0000255}.; TRANSMEM 326 346 Helical. {ECO:0000255}.; TRANSMEM 352 372 Helical. {ECO:0000255}.; TRANSMEM 396 416 Helical. {ECO:0000255}.; TRANSMEM 860 880 Helical. {ECO:0000255}.; TRANSMEM 979 999 Helical. {ECO:0000255}.; TRANSMEM 1023 1043 Helical. {ECO:0000255}.; TRANSMEM 1069 1089 Helical. {ECO:0000255}.; TRANSMEM 1105 1125 Helical. {ECO:0000255}.; TRANSMEM 1135 1155 Helical. {ECO:0000255}.; TRANSMEM 1164 1184 Helical. {ECO:0000255}.; TRANSMEM 1194 1214 Helical. {ECO:0000255}. FUNCTION: ATP-dependent lipophilic drug transporter. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Expressed in heart, brain, lung, liver and skeletal muscle. {ECO:0000269|PubMed:12532264}. +Q6ZQK5 ACAP2_MOUSE Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 2 (Centaurin-beta-2) (Cnt-b2) 770 87,211 Alternative sequence (1); Chain (1); Domain (3); Erroneous initiation (1); Modified residue (7); Repeat (3); Sequence conflict (1); Zinc finger (1) FUNCTION: GTPase-activating protein (GAP) for ADP ribosylation factor 6 (ARF6). {ECO:0000250|UniProtKB:Q15057}. SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. SUBUNIT: Interacts with RAB35 (GTP-bound form); the interaction is direct and probably recruits ACAP2 to membranes. Interacts with MICALL1; the interaction is indirect through RAB35. {ECO:0000269|PubMed:23572513}. +Q5SWU9 ACACA_MOUSE Acetyl-CoA carboxylase 1 (ACC1) (EC 6.4.1.2) (ACC-alpha) (Acetyl-CoA carboxylase 265) [Includes: Biotin carboxylase (EC 6.3.4.14)] 2345 265,257 Active site (1); Alternative sequence (1); Binding site (3); Chain (1); Domain (5); Metal binding (4); Modified residue (25); Nucleotide binding (1); Region (1); Sequence conflict (9) Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. FUNCTION: Catalyzes the rate-limiting reaction in the biogenesis of long-chain fatty acids. Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase. {ECO:0000250|UniProtKB:Q13085, ECO:0000269|PubMed:20952656}. PTM: Phosphorylation on Ser-1262 is required for interaction with BRCA1. {ECO:0000250|UniProtKB:Q13085}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12360400, ECO:0000269|PubMed:20952656}. SUBUNIT: Monomer, homodimer, and homotetramer. Can form filamentous polymers. Interacts in its inactive phosphorylated form with the BRCT domains of BRCA1 which prevents ACACA dephosphorylation and inhibits lipid synthesis. Interacts with MID1IP1; interaction with MID1IP1 promotes oligomerization and increases its activity. {ECO:0000269|PubMed:12360400, ECO:0000269|PubMed:20952656}. +O89016 ABCD4_MOUSE ATP-binding cassette sub-family D member 4 (PMP70-related protein) (P70R) (Peroxisomal membrane protein 1-like) (PXMP1-L) (Peroxisomal membrane protein 69) (PMP69) 606 68,583 Chain (1); Domain (2); Nucleotide binding (1); Sequence conflict (1); Transmembrane (5) TRANSMEM 43 63 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 76 96 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 190 210 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 279 299 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 314 334 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}. FUNCTION: May be involved in intracellular processing of vitamin B12 (cobalamin). Could play a role in the lysosomal release of vitamin B12 into the cytoplasm (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Peroxisome membrane; Multi-pass membrane protein. SUBUNIT: Homodimer or heterodimer. {ECO:0000305}. +Q8K4F5 ABHDB_MOUSE Protein ABHD11 (EC 3.-.-.-) (Alpha/beta hydrolase domain-containing protein 11) (Abhydrolase domain-containing protein 11) (Williams-Beuren syndrome chromosomal region 21 protein homolog) 307 33,561 Active site (3); Chain (1); Modified residue (2) TISSUE SPECIFICITY: Expressed in white adipose tissues. {ECO:0000269|PubMed:17215164}. +Q5XG73 ACBD5_MOUSE Acyl-CoA-binding domain-containing protein 5 508 56,614 Alternative sequence (2); Binding site (2); Chain (1); Coiled coil (2); Compositional bias (2); Domain (1); Erroneous initiation (2); Modified residue (9); Region (2); Transmembrane (1) TRANSMEM 480 500 Helical. {ECO:0000255}. FUNCTION: Acyl-CoA binding protein which acts as the peroxisome receptor for pexophagy but is dispensable for aggrephagy and nonselective autophagy. Binds medium- and long-chain acyl-CoA esters (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000269|PubMed:17768142}; Single-pass membrane protein {ECO:0000269|PubMed:17768142}. +Q76MZ3 2AAA_MOUSE Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform (PP2A subunit A isoform PR65-alpha) (PP2A subunit A isoform R1-alpha) 589 65,323 Beta strand (1); Chain (1); Helix (52); Initiator methionine (1); Modified residue (2); Repeat (15); Turn (3) FUNCTION: The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit (PubMed:10100624). Upon interaction with GNA12 promotes dephosphorylation of microtubule associated protein TAU/MAPT (By similarity). Required for proper chromosome segregation and for centromeric localization of SGO1 in mitosis (By similarity). {ECO:0000250|UniProtKB:P30153, ECO:0000269|PubMed:10100624}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q32PI5}. Chromosome, centromere {ECO:0000250|UniProtKB:P30153}. Lateral cell membrane {ECO:0000250|UniProtKB:P30153}. Cell projection, dendrite {ECO:0000250|UniProtKB:P30153}. Note=Centromeric localization requires the presence of BUB1. {ECO:0000250|UniProtKB:P30153}. SUBUNIT: PP2A consists of a common heterodimeric core enzyme, composed of PPP2CA a 36 kDa catalytic subunit (subunit C) and PPP2R1A a 65 kDa constant regulatory subunit (PR65 or subunit A), that associates with a variety of regulatory subunits. Proteins that associate with the core dimer include three families of regulatory subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa variable regulatory subunit, viral proteins, and cell signaling molecules. Interacts with IPO9 (By similarity). Interacts with TP53 and SGO1 (By similarity). Found in a complex with at least ARL2, PPP2CB, PPP2R1A, PPP2R2A, PPP2R5E and TBCD (By similarity). Interacts with PLA2G16; this interaction might decrease PP2A activity (By similarity). Interacts with FOXO1; the interaction dephosphorylates FOXO1 on AKT-mediated phosphorylation sites (PubMed:22417654). Interacts with CTTNBP2NL (By similarity). Interacts with GNA12; the interaction promotes protein phosphatase 2A activation causing dephosphorylation of MAPT (By similarity).Interacts with CIP2A; this interaction stabilizes CIP2A (By similarity). Interacts with FAM122A (By similarity). Interacts with ADCY8; antagonizes interaction between ADCY8 and calmodulin. {ECO:0000250|UniProtKB:P30153, ECO:0000250|UniProtKB:Q32PI5, ECO:0000269|PubMed:22417654}. DOMAIN: Each HEAT repeat appears to consist of two alpha helices joined by a hydrophilic region, the intrarepeat loop. The repeat units may be arranged laterally to form a rod-like structure. +Q925E7 2ABD_MOUSE Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B delta isoform (PP2A subunit B isoform B55-delta) (PP2A subunit B isoform PR55-delta) (PP2A subunit B isoform R2-delta) (PP2A subunit B isoform delta) 453 51,957 Chain (1); Compositional bias (1); Erroneous initiation (1); Modified residue (3); Repeat (7) FUNCTION: B regulatory subunit of protein phosphatase 2A (PP2A) that plays a key role in cell cycle by controlling mitosis entry and exit. The activity of PP2A complexes containing PPP2R2D (PR55-delta) fluctuate during the cell cycle: the activity is high in interphase and low in mitosis. During mitosis, activity of PP2A is inhibited via interaction with phosphorylated ENSA and ARPP19 inhibitors. Within the PP2A complexes, the B regulatory subunits modulate substrate selectivity and catalytic activity, and also may direct the localization of the catalytic enzyme to a particular subcellular compartment (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: PP2A consists of a common heterodimeric core enzyme, composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant regulatory subunit (PR65 or subunit A), that associates with a variety of regulatory subunits. Proteins that associate with the core dimer include three families of regulatory subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa variable regulatory subunit, viral proteins, and cell signaling molecules. Interacts with ENSA (when phosphorylated at 'Ser-67') and ARPP19 (when phosphorylated at 'Ser-62'), leading to inhibit PP2A activity (By similarity). Interacts with IER5 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q66LE6}. +Q571I9 A16A1_MOUSE Aldehyde dehydrogenase family 16 member A1 802 84,756 Chain (1); Erroneous initiation (1); Sequence conflict (18) SUBUNIT: Interacts with SPG21. {ECO:0000250}. +Q3V1N9 A3LT2_MOUSE Alpha-1,3-galactosyltransferase 2 (EC 2.4.1.87) (Isoglobotriaosylceramide synthase) (iGb3 synthase) (iGb3S) 370 42,649 Active site (1); Alternative sequence (1); Chain (1); Glycosylation (2); Metal binding (2); Natural variant (1); Region (4); Topological domain (2); Transmembrane (1) TRANSMEM 43 65 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 42 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 66 370 Lumenal. {ECO:0000255}. FUNCTION: Synthesizes the galactose-alpha(1,3)-galactose group on the glycosphingolipid isoglobotrihexosylceramide or isogloboside 3 (iGb3) by catalyzing the transfer of galactose from UDP-Galactose to its acceptor molecule Gal-beta-1,4-Glc-ceramide. Can also catalyze the addition of galactose to iGb3 itself to form polygalactose structures. Synthesis of iGb3 is the initial step in the formation of the isoglobo-series glycolipid pathway and is the precursor to isogloboside 4 (iGb4) and isoForssman glycolipids. Can glycosylate only lipids and not proteins and is solely responsible for initiating the synthesis of isoglobo-series glycosphingolipids. {ECO:0000269|PubMed:15539565, ECO:0000269|PubMed:16456004}. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:A0A4Z3}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:A0A4Z3}. Note=Also found in numerous large vesicles throughout the cytoplasm of the soma. {ECO:0000250|UniProtKB:A0A4Z3}. DOMAIN: The conserved DXD motif is involved in cofactor binding. The manganese ion interacts with the beta-phosphate group of UDP and may also have a role in catalysis (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Thymus and lung. {ECO:0000269|PubMed:16456004}. +Q3UD01 A7L3B_MOUSE Ataxin-7-like protein 3B 97 10,731 Chain (1); Modified residue (1) FUNCTION: By binding to ENY2, interferes with the nuclear functions of the deubiquitinase (DUB) module of the SAGA complex which consists of ENY2, ATXN7, ATXN7L3 and the histone deubiquitinating component USP22. Affects USP22 DUB activity toward histones indirectly by changing the subcellular distribution of ENY2 and altering ENY2 availability for ATXN7L3 interaction. Regulates H2B monoubiquitination (H2Bub1) levels through cytoplasmic sequestration of ENY2 resulting in loss of nuclear ENY2-ATXN7L3 association which destabilizes ATXN7L3. Affects protein expression levels of ENY2 and ATXN7L3. {ECO:0000250|UniProtKB:Q96GX2}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96GX2}. SUBUNIT: Interacts strongly with ENY2. Interacts weakly with USP22. {ECO:0000250|UniProtKB:Q96GX2}. +Q5F2F2 ABH15_MOUSE Protein ABHD15 (EC 3.1.1.-) (Alpha/beta hydrolase domain-containing protein 15) (Abhydrolase domain-containing protein 15) 459 51,152 Active site (2); Chain (1); Frameshift (2); Modified residue (1); Sequence conflict (4); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q922Q6 ABHEA_MOUSE Protein ABHD14A (EC 3.-.-.-) (Alpha/beta hydrolase domain-containing protein 14A) (Abhydrolase domain-containing protein 14A) (Down-regulated in Zic-1-mutant protein) 247 27,839 Active site (3); Chain (1); Glycosylation (1); Sequence conflict (1); Transmembrane (1) TRANSMEM 11 31 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. FUNCTION: Possible role in granule neuron development. {ECO:0000269|PubMed:14667578}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14667578}. Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Widely expressed. Higher expression is detected in brain, kidney, heart, testis, ovary and uterus. {ECO:0000269|PubMed:14667578}. +Q8R5A3 AB1IP_MOUSE Amyloid beta A4 precursor protein-binding family B member 1-interacting protein (APBB1-interacting protein 1) (Proline-rich EVH1 ligand 1) (PREL-1) (Proline-rich protein 48) 670 74,319 Beta strand (14); Chain (1); Compositional bias (3); Domain (2); Frameshift (1); Helix (11); Modified residue (4); Sequence conflict (10); Turn (3) FUNCTION: Appears to function in the signal transduction from Ras activation to actin cytoskeletal remodeling. Suppresses insulin-induced promoter activities through AP1 and SRE. Mediates Rap1-induced adhesion (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15642358}; Peripheral membrane protein {ECO:0000269|PubMed:15642358}. Cell projection, lamellipodium {ECO:0000269|PubMed:15642358}. Cell junction, focal adhesion {ECO:0000269|PubMed:15642358}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15642358}. Note=Colocalizes with ENA/VASP proteins at lamellipodia tips and focal adhesions, and F-actin at the leading edge. At the membrane surface, associates, via the PH domain, preferentially with the inositol phosphates, PtdIns(5)P and PtdIns(3)P. This binding appears to be necessary for the efficient interaction of the RA domain to Ras-GTPases. SUBUNIT: Interacts, through the N-terminal Pro-rich region, with the WW domain of APBB1. Interacts with RAP1A, PFN1, VASP and ENAH. {ECO:0000269|PubMed:15642358, ECO:0000269|PubMed:9407065}. TISSUE SPECIFICITY: Ubiquitously expressed with high expression in the hematopoietic system. {ECO:0000269|PubMed:15642358, ECO:0000269|PubMed:9407065}. +Q8K4G5 ABLM1_MOUSE Actin-binding LIM protein 1 (abLIM-1) (Actin-binding LIM protein family member 1) 861 96,805 Alternative sequence (9); Chain (1); Coiled coil (1); Cross-link (1); Domain (5); Erroneous initiation (1); Modified residue (19) FUNCTION: May act as scaffold protein (By similarity). May play a role in the development of the retina. Has been suggested to play a role in axon guidance. {ECO:0000250, ECO:0000269|PubMed:11163266, ECO:0000269|PubMed:12849746}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9245787}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9245787}. Note=In a striped pattern along the myofibril axis in cardiac myocytes. Associated with the cytoskeleton. SUBUNIT: Binds F-actin. Interacts with ABRA (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Isoform 1 is detected in adult retina, where it is highly expressed in the ganglion layer. Detected in rod inner segment. Isoform 2 is highly expressed in adult retina, brain, kidney and heart. Isoform 3 is highly expressed in adult retina, brain, kidney, liver, skeletal muscle, spleen and heart. Detected in embryonic retina, brain, spinal cord, peripheral sensory ganglia and thymus. {ECO:0000269|PubMed:11163266, ECO:0000269|PubMed:12849746, ECO:0000269|PubMed:9245787}. +Q9QZC8 ABHD1_MOUSE Protein ABHD1 (EC 3.1.1.-) (Alpha/beta hydrolase domain-containing protein 1) (Abhydrolase domain-containing protein 1) (Lung alpha/beta hydrolase 1) (MmLABH1) 412 45,725 Active site (3); Chain (1); Domain (1); Glycosylation (1); Transmembrane (1) TRANSMEM 25 45 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Widely expressed with higher expression in liver. {ECO:0000269|PubMed:11922611}. +B5X0E4 ABCB5_MOUSE ATP-binding cassette sub-family B member 5 (ABCB5 P-gp) (P-glycoprotein ABCB5) 1255 137,397 Alternative sequence (1); Chain (1); Domain (4); Glycosylation (11); Nucleotide binding (2); Sequence conflict (1); Transmembrane (9) TRANSMEM 46 66 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 104 124 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 290 310 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 314 334 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 694 714 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 738 758 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 814 836 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 841 863 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 955 975 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}. FUNCTION: Drug efflux transporter present in a number of stem cells that acts as a regulator of cellular differentiation. Able to mediate efflux from cells of the rhodamine dye and of the therapeutic drug doxorubicin. Specifically present in limbal stem cells, where it plays a key role in corneal development and repair. {ECO:0000269|PubMed:25030174}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25030174}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000269|PubMed:25030174}. TISSUE SPECIFICITY: In developing eye, expressed in basal limbal epithelium but not in central cornea. Acts as a marker of limbal stem cells. {ECO:0000269|PubMed:25030174}. +P68254 1433T_MOUSE 14-3-3 protein theta (14-3-3 protein tau) 245 27,778 Alternative sequence (1); Chain (1); Cross-link (1); Erroneous initiation (2); Modified residue (9); Sequence conflict (2); Site (2) FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negatively regulates the kinase activity of PDPK1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Homodimer (By similarity). Interacts with CDKN1B ('Thr-198' phosphorylated form); the interaction translocates CDKN1B to the cytoplasm. Interacts with SSH1 (By similarity). Interacts with GAB2. Interacts with RGS7 (phosphorylated form) (By similarity). Interacts with CDK16 (PubMed:9197417). Interacts with the 'Ser-241' phosphorylated form of PDPK1 (By similarity). Interacts with the 'Thr-369' phosphorylated form of DAPK2 (PubMed:26047703). Interacts with PI4KB, TBC1D22A and TBC1D22B (By similarity). Interacts with SLITRK1 (By similarity). Interacts with RIPOR2 (By similarity). Interacts with INAVA; the interaction increases upon PRR (pattern recognition receptor) stimulation and is required for cellular signaling pathway activation and cytokine secretion (By similarity). {ECO:0000250|UniProtKB:P27348, ECO:0000269|PubMed:26047703, ECO:0000269|PubMed:9197417}. +Q19LI2 A1BG_MOUSE Alpha-1B-glycoprotein (Alpha-1-B glycoprotein) 512 56,554 Chain (1); Disulfide bond (5); Domain (5); Glycosylation (7); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Interacts with CRISP3. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the liver hepatocytes of male and female GH transgenic mice and in the liver of female, but not of male, non-transgenic mice. {ECO:0000269|PubMed:16723264}. +Q5YD48 A1CF_MOUSE APOBEC1 complementation factor (APOBEC1-stimulating protein) 595 65,682 Alternative sequence (3); Chain (1); Domain (3); Region (1); Sequence conflict (5) FUNCTION: Essential component of the apolipoprotein B mRNA editing enzyme complex which is responsible for the postranscriptional editing of a CAA codon for Gln to a UAA codon for stop in APOB mRNA. Binds to APOB mRNA and is probably responsible for docking the catalytic subunit, APOBEC1, to the mRNA to allow it to deaminate its target cytosine. The complex also seems to protect the edited APOB mRNA from nonsense-mediated decay (By similarity). {ECO:0000250|UniProtKB:Q9NQ94}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Predominantly nuclear where it localizes to heterochromatin. Also cytoplasmic where it is found at the outer surface of the endoplasmic reticulum. Shuttles between the nucleus and cytoplasm. May be transported into the nucleus by the nuclear import protein TNPO2/TRN2 or by APOBEC1 (By similarity). {ECO:0000250}. SUBUNIT: Part of the apolipoprotein B mRNA editing complex with APOBEC1. Interacts with TNPO2; TNPO2 may be responsible for transport of A1CF into the nucleus. Interacts with SYNCRIP. Interacts with CELF2/CUGBP2 (By similarity). {ECO:0000250}. DOMAIN: The RRM domains are necessary but not sufficient for binding to APOB mRNA. Additional residues in the pre-RRM and C-terminal regions are required for RNA-binding and for complementing APOBEC1 activity (By similarity). {ECO:0000250|UniProtKB:Q9NQ94}. TISSUE SPECIFICITY: Expressed primarily in liver, small intestine and kidney. {ECO:0000269|PubMed:15451168}. +P58742 AAAS_MOUSE Aladin (Adracalin) 546 59,431 Chain (1); Initiator methionine (1); Modified residue (7); Motif (1); Repeat (4) FUNCTION: Plays a role in the normal development of the peripheral and central nervous system. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nuclear pore complex {ECO:0000250}. SUBUNIT: Interacts with NDC1, the interaction is required for nuclear pore localization. {ECO:0000250}. +Q8VCV1 AB17C_MOUSE Alpha/beta hydrolase domain-containing protein 17C (Abhydrolase domain-containing protein 17C) (EC 3.1.2.22) 320 35,098 Active site (3); Chain (1) FUNCTION: Hydrolyzes fatty acids from S-acylated cysteine residues in proteins. Has depalmitoylating activity towards DLG4/PSD95. {ECO:0000269|PubMed:27307232}. PTM: Palmitoylated on cysteine residues located in a cysteine cluster at the N-terminus which promotes membrane localization. Palmitoylation is required for post-synaptic localization and for depalmitoylating activity towards DLG4/PSD95. {ECO:0000250|UniProtKB:Q7M759}. SUBCELLULAR LOCATION: Recycling endosome membrane {ECO:0000250|UniProtKB:B5DFK7}; Lipid-anchor {ECO:0000250|UniProtKB:B5DFK7}; Cytoplasmic side {ECO:0000250|UniProtKB:B5DFK7}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:B5DFK7}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250|UniProtKB:B5DFK7}. +O35600 ABCA4_MOUSE Retinal-specific ATP-binding cassette transporter (ATP-binding cassette sub-family A member 4) (RIM ABC transporter) (RIM protein) (RmP) 2310 260,209 Chain (1); Disulfide bond (2); Domain (2); Glycosylation (7); Nucleotide binding (2); Topological domain (5); Transmembrane (12) TRANSMEM 22 42 Helical. {ECO:0000255}.; TRANSMEM 647 667 Helical. {ECO:0000255}.; TRANSMEM 700 720 Helical. {ECO:0000255}.; TRANSMEM 731 751 Helical. {ECO:0000255}.; TRANSMEM 760 780 Helical. {ECO:0000255}.; TRANSMEM 836 856 Helical. {ECO:0000255}.; TRANSMEM 1376 1396 Helical. {ECO:0000255}.; TRANSMEM 1727 1747 Helical. {ECO:0000255}.; TRANSMEM 1759 1779 Helical. {ECO:0000255}.; TRANSMEM 1792 1812 Helical. {ECO:0000255}.; TRANSMEM 1831 1851 Helical. {ECO:0000255}.; TRANSMEM 1873 1893 Helical. {ECO:0000255}. TOPO_DOM 1 21 Cytoplasmic.; TOPO_DOM 43 646 Extracellular. {ECO:0000250}.; TOPO_DOM 857 1375 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 1397 1726 Extracellular. {ECO:0000250}.; TOPO_DOM 1894 2310 Cytoplasmic. {ECO:0000250}. FUNCTION: In the visual cycle, acts as an inward-directed retinoid flipase, retinoid substrates imported by ABCA4 from the extracellular or intradiscal (rod) membrane surfaces to the cytoplasmic membrane surface are all-trans-retinaldehyde (ATR) and N-retinyl-phosphatidyl-ethanolamine (NR-PE). Once transported to the cytoplasmic surface, ATR is reduced to vitamin A by trans-retinol dehydrogenase (tRDH) and then transferred to the retinal pigment epithelium (RPE) where it is converted to 11-cis-retinal. May play a role in photoresponse, removing ATR/NR-PE from the extracellular photoreceptor surfaces during bleach recovery (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Localized to outer segment disk edges of rods and cones, with around one million copies/photoreceptor. {ECO:0000250}. TISSUE SPECIFICITY: Retinal-specific. Seems to be exclusively found in the rims of rod photoreceptor cells. +P05201 AATC_MOUSE Aspartate aminotransferase, cytoplasmic (cAspAT) (EC 2.6.1.1) (EC 2.6.1.3) (Cysteine aminotransferase, cytoplasmic) (Cysteine transaminase, cytoplasmic) (cCAT) (Glutamate oxaloacetate transaminase 1) (Transaminase A) 413 46,248 Binding site (4); Chain (1); Initiator methionine (1); Modified residue (3); Sequence conflict (4) FUNCTION: Biosynthesis of L-glutamate from L-aspartate or L-cysteine. Important regulator of levels of glutamate, the major excitatory neurotransmitter of the vertebrate central nervous system. Acts as a scavenger of glutamate in brain neuroprotection. The aspartate aminotransferase activity is involved in hepatic glucose synthesis during development and in adipocyte glyceroneogenesis. Using L-cysteine as substrate, regulates levels of mercaptopyruvate, an important source of hydrogen sulfide. Mercaptopyruvate is converted into H(2)S via the action of 3-mercaptopyruvate sulfurtransferase (3MST). Hydrogen sulfide is an important synaptic modulator and neuroprotectant in the brain (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Homodimer. TISSUE SPECIFICITY: Expressed in neurons of the retina. Localizes to the inner and outer plexiform layers, the inner and outer nuclear layer and the outer segments of photoreceptors. {ECO:0000269|PubMed:21937432}. +Q91V24 ABCA7_MOUSE ATP-binding cassette sub-family A member 7 2159 236,884 Chain (1); Disulfide bond (2); Domain (2); Frameshift (1); Glycosylation (1); Nucleotide binding (2); Sequence conflict (3); Topological domain (2); Transmembrane (14) TRANSMEM 22 42 Helical. {ECO:0000255}.; TRANSMEM 547 567 Helical. {ECO:0000255}.; TRANSMEM 590 610 Helical. {ECO:0000255}.; TRANSMEM 623 643 Helical. {ECO:0000255}.; TRANSMEM 652 672 Helical. {ECO:0000255}.; TRANSMEM 678 698 Helical. {ECO:0000255}.; TRANSMEM 732 752 Helical. {ECO:0000255}.; TRANSMEM 846 866 Helical. {ECO:0000255}.; TRANSMEM 1246 1266 Helical. {ECO:0000255}.; TRANSMEM 1552 1572 Helical. {ECO:0000255}.; TRANSMEM 1598 1618 Helical. {ECO:0000255}.; TRANSMEM 1635 1655 Helical. {ECO:0000255}.; TRANSMEM 1663 1683 Helical. {ECO:0000255}.; TRANSMEM 1743 1763 Helical. {ECO:0000255}. TOPO_DOM 43 546 Extracellular. {ECO:0000250}.; TOPO_DOM 1267 1551 Extracellular. {ECO:0000250}. FUNCTION: Probable ATP-binding cassette (ABC) transporter that plays a role in lipid homeostasis and macrophage-mediated phagocytosis (PubMed:12917409, PubMed:15550377, PubMed:16908670, PubMed:27472885, PubMed:27030769, PubMed:20495215). Binds APOA1 and may function in apolipoprotein-mediated phospholipid efflux from cells (PubMed:12917409). May also mediate cholesterol efflux (By similarity). May regulate cellular ceramide homeostasis during keratinocyte differentiation (By similarity). Involved in lipid raft organization and CD1D localization on thymocytes and antigen-presenting cells, which plays an important role in natural killer T-cell development and activation (PubMed:28091533). Plays a role in phagocytosis of apoptotic cells by macrophages (PubMed:16908670). Macrophage phagocytosis is stimulated by APOA1 or APOA2, probably by stabilization of ABCA7 (PubMed:20495215). Also involved in phagocytic clearance of amyloid-beta by microglia cells and macrophages (PubMed:27472885). Further limits amyloid-beta production by playing a role in the regulation of amyloid-beta A4 precursor protein (APP) endocytosis and/or processing (PubMed:26260791, PubMed:27030769). {ECO:0000250|UniProtKB:Q8IZY2, ECO:0000269|PubMed:12917409, ECO:0000269|PubMed:15550377, ECO:0000269|PubMed:16908670, ECO:0000269|PubMed:20495215, ECO:0000269|PubMed:26260791, ECO:0000269|PubMed:27030769, ECO:0000269|PubMed:27472885, ECO:0000269|PubMed:28091533}. PTM: N-glycosylated. {ECO:0000269|PubMed:20495215}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12917409, ECO:0000269|PubMed:20495215, ECO:0000269|PubMed:26260791}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:16908670}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000269|PubMed:16908670}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:27472885}. Cell projection, ruffle membrane {ECO:0000269|PubMed:16908670}. Cell projection, phagocytic cup {ECO:0000269|PubMed:16908670}. Note=Localizes to cell membrane ruffles and phagocytic cups of macrophages stimulated with C1q or apoptotic cells. Localizes to the cytoplasm of resting macrophages, probably in Golgi and endosomes (PubMed:16908670). Localizes to the apical brush border of cells in the proximal tubules of kidney (Probable). {ECO:0000269|PubMed:16908670, ECO:0000305}. TISSUE SPECIFICITY: Widely expressed with higher expression in brain, lung, adrenal gland, spleen and hematopoietic tissues (at protein level) (PubMed:12917409, PubMed:15550377, PubMed:27472885). In the brain, expressed in cortex, cerebellum, hippocampus, olfactory bulb, neurons, astrocytes and microglia (at protein level) (PubMed:26260791). Also expressed in adipocytes and macrophages (at protein level) (PubMed:15550377, PubMed:27472885). Expressed in thymocytes (at protein level) (PubMed:28091533). Highly expressed in spleen and hematopoietic tissues (PubMed:11435699). Expressed in brain, lung, macrophages, microglia, oligodendrocytes and neurons (PubMed:27472885). {ECO:0000269|PubMed:11435699, ECO:0000269|PubMed:12917409, ECO:0000269|PubMed:15550377, ECO:0000269|PubMed:26260791, ECO:0000269|PubMed:27472885, ECO:0000269|PubMed:28091533}. +Q8C1A9 ABD18_MOUSE Protein ABHD18 (Alpha/beta hydrolase domain-containing protein 18) (Abhydrolase domain-containing protein 18) 464 53,168 Alternative sequence (2); Chain (1); Glycosylation (1); Sequence conflict (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q9WV35 ABEC2_MOUSE C->U-editing enzyme APOBEC-2 (EC 3.5.4.36) (mRNA(cytosine(6666)) deaminase 2) 224 25,660 Active site (1); Beta strand (9); Chain (1); Domain (1); Helix (6); Metal binding (4) FUNCTION: Probable C to U editing enzyme whose physiological substrate is not yet known. Does not display detectable apoB mRNA editing. Has a low intrinsic cytidine deaminase activity. May play a role in the epigenetic regulation of gene expression through the process of active DNA demethylation. {ECO:0000250|UniProtKB:Q9Y235}. SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q9Y235}. TISSUE SPECIFICITY: Expressed exclusively in heart and skeletal muscle. {ECO:0000269|PubMed:12859895}. +P50544 ACADV_MOUSE Very long-chain specific acyl-CoA dehydrogenase, mitochondrial (EC 1.3.8.9) (MVLCAD) (VLCAD) 656 70,875 Active site (1); Binding site (3); Chain (1); Modified residue (27); Nucleotide binding (4); Region (4); Sequence conflict (13); Transit peptide (1) Lipid metabolism; mitochondrial fatty acid beta-oxidation. FUNCTION: Active toward esters of long-chain and very long chain fatty acids such as palmitoyl-CoA, myristoyl-CoA and stearoyl-CoA. Can accommodate substrate acyl chain lengths as long as 24 carbons, but shows little activity for substrates of less than 12 carbons (By similarity). {ECO:0000250}. PTM: S-nitrosylation at Cys-238 in liver improves catalytic efficiency. {ECO:0000269|PubMed:23281369}. SUBCELLULAR LOCATION: Mitochondrion inner membrane. SUBUNIT: Homodimer. {ECO:0000250}. +Q7TNP2 2AAB_MOUSE Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform (PP2A subunit A isoform PR65-beta) (PP2A subunit A isoform R1-beta) 601 65,934 Chain (1); Initiator methionine (1); Modified residue (1); Repeat (15); Sequence conflict (4) FUNCTION: The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit. {ECO:0000250}. SUBUNIT: PP2A consists of a common heterodimeric core enzyme, composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant regulatory subunit (PR65 or subunit A), that associates with a variety of regulatory subunits. Proteins that associate with the core dimer include three families of regulatory subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa variable regulatory subunit, viral proteins, and cell signaling molecules. Interacts with IPO9 (By similarity). Interacts with SGO1 (By similarity). Interacts with RAF1 (By similarity). {ECO:0000250}. DOMAIN: Each HEAT repeat appears to consist of two alpha helices joined by a hydrophilic region, the intrarepeat loop. The repeat units may be arranged laterally to form a rod-like structure. +P56379 68MP_MOUSE 6.8 kDa mitochondrial proteolipid 58 6,698 Chain (1); Transmembrane (1) TRANSMEM 15 36 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Mitochondrion membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. SUBUNIT: Component of an ATP synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MD and MP68. {ECO:0000250}. +Q3UHJ0 AAK1_MOUSE AP2-associated protein kinase 1 (EC 2.7.11.1) (Adaptor-associated kinase 1) 959 103,346 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Compositional bias (3); Domain (1); Modified residue (20); Nucleotide binding (1); Sequence conflict (3) FUNCTION: Regulates clathrin-mediated endocytosis by phosphorylating the AP2M1/mu2 subunit of the adaptor protein complex 2 (AP-2) which ensures high affinity binding of AP-2 to cargo membrane proteins during the initial stages of endocytosis. Isoform 1 and isoform 2 display similar levels of kinase activity towards AP2M1. Regulates phosphorylation of other AP-2 subunits as well as AP-2 localization and AP-2-mediated internalization of ligand complexes. Phosphorylates NUMB and regulates its cellular localization, promoting NUMB localization to endosomes. Binds to and stabilizes the activated form of NOTCH1, increases its localization in endosomes and regulates its transcriptional activity (By similarity). {ECO:0000250}. PTM: Autophosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Membrane, clathrin-coated pit {ECO:0000250}. Note=Active when found in clathrin-coated pits at the plasma membrane. In neuronal cells, enriched at presynaptic terminals. In non-neuronal cells, enriched at leading edge of migrating cells (By similarity). {ECO:0000250}. SUBUNIT: Interacts with alpha-adaptin, AP-2, clathrin, NUMB and EPS15 isoform 2 (By similarity). Interacts with membrane-bound activated NOTCH1 but not with the inactive full-length form of NOTCH1. Preferentially interacts with monoubiquitinated activated NOTCH1 compared to the non-ubiquitinated form. {ECO:0000250, ECO:0000269|PubMed:21464124}. +Q9QY30 ABCBB_MOUSE Bile salt export pump (ATP-binding cassette sub-family B member 11) (Sister of P-glycoprotein) 1321 146,749 Chain (1); Domain (4); Glycosylation (4); Modified residue (6); Nucleotide binding (2); Region (1); Sequence conflict (3); Topological domain (12); Transmembrane (12) TRANSMEM 63 83 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 148 168 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 216 236 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 241 261 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 320 340 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 354 374 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 756 776 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 795 815 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 870 890 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 891 911 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 980 1000 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 1012 1032 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}. TOPO_DOM 1 62 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 84 147 Extracellular. {ECO:0000255}.; TOPO_DOM 169 215 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 237 240 Extracellular. {ECO:0000255}.; TOPO_DOM 262 319 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 341 353 Extracellular. {ECO:0000255}.; TOPO_DOM 375 755 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 777 794 Extracellular. {ECO:0000255}.; TOPO_DOM 816 869 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 912 979 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1001 1011 Extracellular. {ECO:0000255}.; TOPO_DOM 1033 1321 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in the ATP-dependent secretion of bile salts into the canaliculus of hepatocytes. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SUBUNIT: Interacts with HAX1. {ECO:0000250}. DOMAIN: Multifunctional polypeptide with two homologous halves, each containing a hydrophobic membrane-anchoring domain and an ATP binding cassette (ABC) domain. TISSUE SPECIFICITY: Expressed predominantly, if not exclusively in the liver, where it was further localized to the canalicular microvilli and to subcanalicular vesicles of the hepatocytes by in situ. +Q811W1 AARD_MOUSE Alanine and arginine-rich domain-containing protein 167 18,923 Chain (1); Compositional bias (1); Sequence conflict (1) TISSUE SPECIFICITY: Preferrentially expressed in testis both in embryo and adult. Expressed at much lower level in other tissues. {ECO:0000269|PubMed:12617826, ECO:0000269|PubMed:17486547}. +Q69ZX8 ABLM3_MOUSE Actin-binding LIM protein 3 (abLIM-3) (Actin-binding LIM protein family member 3) 682 77,630 Chain (1); Domain (5); Erroneous initiation (1); Modified residue (20); Sequence conflict (1) FUNCTION: May act as scaffold protein. May stimulate ABRA activity and ABRA-dependent SRF transcriptional activity. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Directly interacts with F-actin and ABRA. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in heart, brain, lung and liver. In the brain, highly expressed in the olfactory bulb. In the hippocampus, expressed selectively in the CA2 and CA3 fields. In the cerebellum, expressed in internal granular cells. {ECO:0000269|PubMed:17194709}. +P61982 1433G_MOUSE 14-3-3 protein gamma [Cleaved into: 14-3-3 protein gamma, N-terminally processed] 247 28,303 Chain (2); Erroneous initiation (1); Initiator methionine (1); Modified residue (8); Sequence conflict (1); Site (2) FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. PTM: Phosphorylated by various PKC isozymes. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homodimer. Interacts with MDM4 (phosphorylated); negatively regulates MDM4 activity toward TP53. Interacts with RAF1, SSH1 and CRTC2/TORC2. Interacts with ABL1 (phosphorylated form); the interaction retains it in the cytoplasm. Interacts with GAB2. Interacts with PKA-phosphorylated AANAT and SIRT2 (By similarity). Interacts with SAMSN1. Interacts with the 'Thr-369' phosphorylated form of DAPK2 (PubMed:26047703). Interacts with PI4KB, TBC1D22A and TBC1D22B (By similarity). Interacts with SLITRK1 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P61981, ECO:0000269|PubMed:20478393, ECO:0000269|PubMed:26047703}. +Q8BG02 2ABG_MOUSE Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B gamma isoform (PP2A subunit B isoform B55-gamma) (PP2A subunit B isoform PR55-gamma) (PP2A subunit B isoform R2-gamma) (PP2A subunit B isoform gamma) 447 51,462 Chain (1); Repeat (7) FUNCTION: The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment. {ECO:0000250}. SUBUNIT: PP2A consists of a common heterodimeric core enzyme, composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant regulatory subunit (PR65 or subunit A), that associates with a variety of regulatory subunits. Proteins that associate with the core dimer include three families of regulatory subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa variable regulatory subunit, viral proteins, and cell signaling molecules (By similarity). Interacts with IER5 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9Y2T4}. +O70456 1433S_MOUSE 14-3-3 protein sigma (Stratifin) 248 27,706 Chain (1); Modified residue (3); Sequence conflict (1); Site (2) FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. When bound to KRT17, regulates protein synthesis and epithelial cell growth by stimulating Akt/mTOR pathway. May also regulate MDM2 autoubiquitination and degradation and thereby activate p53/TP53. {ECO:0000269|PubMed:16710422}. PTM: Ubiquitinated. Ubiquitination by RFFL induces proteasomal degradation and indirectly regulates p53/TP53 activation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16710422}. Nucleus {ECO:0000269|PubMed:16710422}. Secreted {ECO:0000250}. Note=May be secreted by a non-classical secretory pathway. {ECO:0000250}. SUBUNIT: Homodimer. Found in a complex with XPO7, EIF4A1, ARHGAP1, VPS26A, VPS29 and VPS35. Interacts with GAB2 (By similarity). Interacts with KRT17. Interacts with SAMSN1. Interacts with SRPK2 (By similarity). Interacts with COPS6 (By similarity). Interacts with COP1; this interaction leads to proteasomal degradation (By similarity).Interacts with the 'Thr-369' phosphorylated form of DAPK2 (PubMed:26047703). Interacts with PI4KB (By similarity). Interacts with SLITRK1 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P31947, ECO:0000269|PubMed:26047703}. TISSUE SPECIFICITY: Expressed in the basal layer of skin epithelium and in outer root sheath of hair follicle. {ECO:0000269|PubMed:16710422}. +Q6PD28 2A5B_MOUSE Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit beta isoform (PP2A B subunit isoform B'-beta) (PP2A B subunit isoform B56-beta) (PP2A B subunit isoform PR61-beta) (PP2A B subunit isoform R5-beta) 497 57,342 Chain (1); Modified residue (6); Sequence conflict (1) FUNCTION: As the regulatory component of the serine/threonine-protein phosphatase 2A (PP2A) holoenzyme, modulates substrate specificity, subcellular localization, and responsiveness to phosphorylation. The phosphorylated form mediates the interaction between PP2A and AKT1, leading to AKT1 dephosphorylation. {ECO:0000250|UniProtKB:Q15173}. PTM: Ubiquitinated by CUL3-KLHL15 complex; this modification leads to proteasomal degradation. {ECO:0000250|UniProtKB:Q15173}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q15173}. SUBUNIT: Component of the serine/threonine-protein phosphatase 2A complex (PP2A). This complex consists of a common heterodimeric core enzyme, composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant scaffold subunit (PR65 or subunit A), that associates with a variety of regulatory subunits. Proteins that associate with the core dimer include three families of regulatory subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa variable regulatory subunit, viral proteins, and cell signaling molecules. Interacts with SGO1. Interacts with AKT1. {ECO:0000250|UniProtKB:Q15173}. +Q9EQC1 3BHS7_MOUSE 3 beta-hydroxysteroid dehydrogenase type 7 (3 beta-hydroxysteroid dehydrogenase type VII) (3-beta-HSD VII) (3-beta-hydroxy-Delta(5)-C27 steroid oxidoreductase) (C(27) 3-beta-HSD) (EC 1.1.1.-) (Cholest-5-ene-3-beta,7-alpha-diol 3-beta-dehydrogenase) (EC 1.1.1.181) 369 41,135 Active site (1); Binding site (1); Chain (1); Transmembrane (2) TRANSMEM 289 309 Helical. {ECO:0000255}.; TRANSMEM 312 334 Helical. {ECO:0000255}. Lipid metabolism; steroid biosynthesis. FUNCTION: The 3-beta-HSD enzymatic system plays a crucial role in the biosynthesis of all classes of hormonal steroids. HSD VII is active against four 7-alpha-hydroxylated sterols. Does not metabolize several different C(19/21) steroids as substrates. Involved in bile acid synthesis (PubMed:11067870). Plays a key role in cell positioning and movement in lymphoid tissues by mediating degradation of 7-alpha,25-dihydroxycholesterol (7-alpha,25-OHC): 7-alpha,25-OHC acts as a ligand for the G protein-coupled receptor GPR183/EBI2, a chemotactic receptor for a number of lymphoid cells (PubMed:22999953). {ECO:0000269|PubMed:11067870, ECO:0000269|PubMed:22999953}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Predominantly expressed in liver. {ECO:0000269|PubMed:11067870}. +Q64264 5HT1A_MOUSE 5-hydroxytryptamine receptor 1A (5-HT-1A) (5-HT1A) (Serotonin receptor 1A) 421 46,176 Chain (1); Disulfide bond (1); Glycosylation (4); Motif (2); Natural variant (1); Region (2); Sequence conflict (5); Topological domain (8); Transmembrane (7) TRANSMEM 37 62 Helical; Name=1. {ECO:0000250}.; TRANSMEM 74 98 Helical; Name=2. {ECO:0000250}.; TRANSMEM 111 132 Helical; Name=3. {ECO:0000250}.; TRANSMEM 153 178 Helical; Name=4. {ECO:0000250}.; TRANSMEM 192 217 Helical; Name=5. {ECO:0000250}.; TRANSMEM 346 367 Helical; Name=6. {ECO:0000250}.; TRANSMEM 379 403 Helical; Name=7. {ECO:0000250}. TOPO_DOM 1 36 Extracellular. {ECO:0000250}.; TOPO_DOM 63 73 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 99 110 Extracellular. {ECO:0000250}.; TOPO_DOM 133 152 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 179 191 Extracellular. {ECO:0000250}.; TOPO_DOM 218 345 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 368 378 Extracellular. {ECO:0000250}.; TOPO_DOM 404 421 Cytoplasmic. {ECO:0000250}. FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various drugs and psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Beta-arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways. Signaling inhibits adenylate cyclase activity and activates a phosphatidylinositol-calcium second messenger system that regulates the release of Ca(2+) ions from intracellular stores. Plays a role in the regulation of 5-hydroxytryptamine release and in the regulation of dopamine and 5-hydroxytryptamine metabolism. Plays a role in the regulation of dopamine and 5-hydroxytryptamine levels in the brain, and thereby affects neural activity, mood and behavior. Plays a role in the response to anxiogenic stimuli. {ECO:0000269|PubMed:11080193, ECO:0000269|PubMed:17543467, ECO:0000269|PubMed:18599790, ECO:0000269|PubMed:21508226, ECO:0000269|PubMed:8254366, ECO:0000269|PubMed:9826725}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8254366}; Multi-pass membrane protein {ECO:0000269|PubMed:8254366}. SUBUNIT: Heterodimer; heterodimerizes with GPER1. {ECO:0000250}. TISSUE SPECIFICITY: Most abundantly expressed in midbrain, in dorsal raphe and hippocampus. Detected at lower levels in amygdala and brain cortex. {ECO:0000269|PubMed:9826725}. +Q02152 5HT2B_MOUSE 5-hydroxytryptamine receptor 2B (5-HT-2B) (5-HT2B) (5-HT-2F) (NP75 protein) (Serotonin receptor 2B) 479 53,597 Chain (1); Disulfide bond (2); Erroneous termination (1); Glycosylation (1); Lipidation (1); Motif (4); Region (2); Sequence conflict (4); Site (1); Topological domain (8); Transmembrane (7) TRANSMEM 56 78 Helical; Name=1. {ECO:0000250|UniProtKB:P41595}.; TRANSMEM 90 112 Helical; Name=2. {ECO:0000250|UniProtKB:P41595}.; TRANSMEM 129 150 Helical; Name=3. {ECO:0000250|UniProtKB:P41595}.; TRANSMEM 171 191 Helical; Name=4. {ECO:0000250|UniProtKB:P41595}.; TRANSMEM 216 238 Helical; Name=5. {ECO:0000250|UniProtKB:P41595}.; TRANSMEM 324 344 Helical; Name=6. {ECO:0000250|UniProtKB:P41595}.; TRANSMEM 360 381 Helical; Name=7. {ECO:0000250|UniProtKB:P41595}. TOPO_DOM 1 55 Extracellular. {ECO:0000250|UniProtKB:P41595}.; TOPO_DOM 79 89 Cytoplasmic. {ECO:0000250|UniProtKB:P41595}.; TOPO_DOM 113 128 Extracellular. {ECO:0000250, ECO:0000250|UniProtKB:P41595}.; TOPO_DOM 151 170 Cytoplasmic. {ECO:0000250|UniProtKB:P41595}.; TOPO_DOM 192 215 Extracellular. {ECO:0000250|UniProtKB:P41595}.; TOPO_DOM 239 323 Cytoplasmic. {ECO:0000250|UniProtKB:P41595}.; TOPO_DOM 345 359 Extracellular. {ECO:0000250|UniProtKB:P41595}.; TOPO_DOM 382 479 Cytoplasmic. {ECO:0000250|UniProtKB:P41595}. FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine (serotonin) (PubMed:1426253). Also functions as a receptor for various ergot alkaloid derivatives and psychoactive substances (PubMed:1426253, PubMed:16940156). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors. Beta-arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways. Signaling activates a phosphatidylinositol-calcium second messenger system that modulates the activity of phosphatidylinositol 3-kinase and downstream signaling cascades and promotes the release of Ca(2+) ions from intracellular stores (By similarity). Plays a role in the regulation of dopamine and 5-hydroxytryptamine release, 5-hydroxytryptamine uptake and in the regulation of extracellular dopamine and 5-hydroxytryptamine levels, and thereby affects neural activity (PubMed:16940156, PubMed:18337424). May play a role in the perception of pain (PubMed:21273425). Plays a role in the regulation of behavior, including impulsive behavior (PubMed:21179162). Required for normal proliferation of embryonic cardiac myocytes and normal heart development (PubMed:10944220, PubMed:11413089). Protects cardiomyocytes against apoptosis (PubMed:12738797). Plays a role in the adaptation of pulmonary arteries to chronic hypoxia (PubMed:12244304). Plays a role in vasoconstriction (PubMed:12244304, PubMed:23346101). Required for normal osteoblast function and proliferation, and for maintaining normal bone density (PubMed:17846081). Required for normal proliferation of the interstitial cells of Cajal in the intestine (PubMed:19941613). {ECO:0000250|UniProtKB:P41595, ECO:0000269|PubMed:10944220, ECO:0000269|PubMed:11413089, ECO:0000269|PubMed:12244304, ECO:0000269|PubMed:12738797, ECO:0000269|PubMed:1426253, ECO:0000269|PubMed:16940156, ECO:0000269|PubMed:17846081, ECO:0000269|PubMed:18337424, ECO:0000269|PubMed:19941613, ECO:0000269|PubMed:21179162, ECO:0000269|PubMed:21273425, ECO:0000269|PubMed:23346101}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1426253}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P41595}. Cell junction, synapse, synaptosome {ECO:0000269|PubMed:18337424}. SUBUNIT: Interacts (via C-terminus) with MPDZ. {ECO:0000250|UniProtKB:P41595}. DOMAIN: Ligands are bound in a hydrophobic pocket formed by the transmembrane helices. {ECO:0000250|UniProtKB:P41595}. TISSUE SPECIFICITY: Ubiquitous. Detected in intestine, heart, skeletal muscle, testis, urinary bladder, stomach, liver, lung, brain and kidney. Detected in osteoblasts. Detected in the raphe nucleus in the brain, in dorsal root ganglion neurons, the brain stem, cerebellum and spinal cord. Detected in interstitial cells of Cajal in the small intestine. {ECO:0000269|PubMed:10944220, ECO:0000269|PubMed:1426253, ECO:0000269|PubMed:17846081, ECO:0000269|PubMed:18337424, ECO:0000269|PubMed:19941613, ECO:0000269|PubMed:21273425}. +P48193 41_MOUSE Protein 4.1 (P4.1) (4.1R) (Band 4.1) 858 95,911 Alternative sequence (1); Chain (1); Domain (1); Erroneous initiation (1); Modified residue (25); Region (3); Sequence conflict (5) FUNCTION: Protein 4.1 is a major structural element of the erythrocyte membrane skeleton. It plays a key role in regulating membrane physical properties of mechanical stability and deformability by stabilizing spectrin-actin interaction. Recruits DLG1 to membranes. Required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase. {ECO:0000250|UniProtKB:P11171}. PTM: O-glycosylated; contains N-acetylglucosamine side chains in the C-terminal domain. {ECO:0000250}.; PTM: Phosphorylated at multiple sites by different protein kinases and each phosphorylation event selectively modulates the protein's functions.; PTM: Phosphorylation on Tyr-654 reduces the ability of 4.1 to promote the assembly of the spectrin/actin/4.1 ternary complex. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P11171}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P11171}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:P11171}. SUBUNIT: Binds with a high affinity to glycophorin and with lower affinity to band III protein. Associates with the nuclear mitotic apparatus. Binds calmodulin, CENPJ and DLG1. Also found to associate with contractile apparatus and tight junctions. Interacts with NUMA1; this interaction is negatively regulated by CDK1 during metaphase and promotes anaphase-specific localization of NUMA1 in symmetrically dividing cells. {ECO:0000250|UniProtKB:P11171}. +Q00898 A1AT5_MOUSE Alpha-1-antitrypsin 1-5 (Alpha-1 protease inhibitor 5) (Serine protease inhibitor 1-5) (Serine protease inhibitor A1e) (Serpin A1e) 413 45,891 Chain (1); Erroneous initiation (1); Glycosylation (3); Region (1); Signal peptide (1); Site (1) FUNCTION: Does not inhibit elastase or chymotrypsin. No target protease has been identified to date. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8619829}. DOMAIN: The reactive center loop (RCL) extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site within the RCL, establishing a covalent linkage between the serpin reactive site and the active site of the protease. The resulting inactive serpin-protease complex is highly stable (By similarity). Variability within the reactive center loop (RCL) sequences of Serpina1-related genes may determine target protease specificity. {ECO:0000250}. +Q8BRK8 AAPK2_MOUSE 5'-AMP-activated protein kinase catalytic subunit alpha-2 (AMPK subunit alpha-2) (EC 2.7.11.1) (Acetyl-CoA carboxylase kinase) (ACACA kinase) (EC 2.7.11.27) (Hydroxymethylglutaryl-CoA reductase kinase) (HMGCR kinase) (EC 2.7.11.31) 552 62,022 Active site (1); Binding site (1); Chain (1); Domain (1); Modified residue (4); Mutagenesis (2); Nucleotide binding (1); Region (1); Sequence conflict (5) FUNCTION: Catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Regulates lipid synthesis by phosphorylating and inactivating lipid metabolic enzymes such as ACACA, ACACB, GYS1, HMGCR and LIPE; regulates fatty acid and cholesterol synthesis by phosphorylating acetyl-CoA carboxylase (ACACA and ACACB) and hormone-sensitive lipase (LIPE) enzymes, respectively. Regulates insulin-signaling and glycolysis by phosphorylating IRS1, PFKFB2 and PFKFB3. Involved in insulin receptor/INSR internalization (By similarity). AMPK stimulates glucose uptake in muscle by increasing the translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane, possibly by mediating phosphorylation of TBC1D4/AS160. Regulates transcription and chromatin structure by phosphorylating transcription regulators involved in energy metabolism such as CRTC2/TORC2, FOXO3, histone H2B, HDAC5, MEF2C, MLXIPL/ChREBP, EP300, HNF4A, p53/TP53, SREBF1, SREBF2 and PPARGC1A. Acts as a key regulator of glucose homeostasis in liver by phosphorylating CRTC2/TORC2, leading to CRTC2/TORC2 sequestration in the cytoplasm. In response to stress, phosphorylates 'Ser-36' of histone H2B (H2BS36ph), leading to promote transcription. Acts as a key regulator of cell growth and proliferation by phosphorylating TSC2, RPTOR and ATG1/ULK1: in response to nutrient limitation, negatively regulates the mTORC1 complex by phosphorylating RPTOR component of the mTORC1 complex and by phosphorylating and activating TSC2. In response to nutrient limitation, promotes autophagy by phosphorylating and activating ATG1/ULK1. In that process also activates WDR45. AMPK also acts as a regulator of circadian rhythm by mediating phosphorylation of CRY1, leading to destabilize it. May regulate the Wnt signaling pathway by phosphorylating CTNNB1, leading to stabilize it. Also phosphorylates CFTR, EEF2K, KLC1, NOS3 and SLC12A1. Plays an important role in the differential regulation of pro-autophagy (composed of PIK3C3, BECN1, PIK3R4 and UVRAG or ATG14) and non-autophagy (composed of PIK3C3, BECN1 and PIK3R4) complexes, in response to glucose starvation. Can inhibit the non-autophagy complex by phosphorylating PIK3C3 and can activate the pro-autophagy complex by phosphorylating BECN1 (PubMed:23332761). {ECO:0000250|UniProtKB:P54646, ECO:0000269|PubMed:15331533, ECO:0000269|PubMed:15561936, ECO:0000269|PubMed:16148943, ECO:0000269|PubMed:16308421, ECO:0000269|PubMed:16804075, ECO:0000269|PubMed:16804077, ECO:0000269|PubMed:17609368, ECO:0000269|PubMed:18439900, ECO:0000269|PubMed:19833968, ECO:0000269|PubMed:20361929, ECO:0000269|PubMed:20647423, ECO:0000269|PubMed:21205641, ECO:0000269|PubMed:21258367, ECO:0000269|PubMed:21454484, ECO:0000269|PubMed:21459323, ECO:0000269|PubMed:23332761}. PTM: Ubiquitinated. {ECO:0000250}.; PTM: Phosphorylated at Thr-172 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. Also phosphorylated at Thr-172 by CAMKK2; triggered by a rise in intracellular calcium ions, without detectable changes in the AMP/ATP ratio. CAMKK1 can also phosphorylate Thr-172, but at much lower level. Dephosphorylated by protein phosphatase 2A and 2C (PP2A and PP2C). Phosphorylated by ULK1; leading to negatively regulate AMPK activity and suggesting the existence of a regulatory feedback loop between ULK1 and AMPK. Dephosphorylated by PPM1A and PPM1B at Thr-172 (mediated by STK11/LKB1) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus. Note=In response to stress, recruited by p53/TP53 to specific promoters. SUBUNIT: AMPK is a heterotrimer of an alpha catalytic subunit (PRKAA1 or PRKAA2), a beta (PRKAB1 or PRKAB2) and a gamma non-catalytic subunits (PRKAG1, PRKAG2 or PRKAG3). Interacts with FNIP1 and FNIP2 (By similarity). {ECO:0000250}. DOMAIN: The AIS (autoinhibitory sequence) region shows some sequence similarity with the ubiquitin-associated domains and represses kinase activity. {ECO:0000250}. +Q9D2V5 AAR2_MOUSE Protein AAR2 homolog (AAR2 splicing factor homolog) 384 43,408 Chain (1); Sequence conflict (3) FUNCTION: Component of the U5 snRNP complex that is required for spliceosome assembly and for pre-mRNA splicing. {ECO:0000250|UniProtKB:P32357}. SUBUNIT: Interacts with PRPF8 (via RNase H homology domain) (By similarity). Component of a U5 snRNP complex that contains PRPF8 (By similarity). {ECO:0000250|UniProtKB:P32357, ECO:0000250|UniProtKB:Q9Y312}. +P70170 ABCC9_MOUSE ATP-binding cassette sub-family C member 9 (Sulfonylurea receptor 2) 1546 174,239 Alternative sequence (2); Chain (1); Domain (4); Glycosylation (2); Nucleotide binding (2); Topological domain (16); Transmembrane (15) TRANSMEM 31 51 Helical; Name=1. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 73 93 Helical; Name=2. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 102 122 Helical; Name=3. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 133 153 Helical; Name=4. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 168 188 Helical; Name=5. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 302 322 Helical; Name=6. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 349 369 Helical; Name=7. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 422 442 Helical; Name=8. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 454 474 Helical; Name=9. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 530 550 Helical; Name=10. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 570 590 Helical; Name=11. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 988 1008 Helical; Name=12. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 1032 1052 Helical; Name=13. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 1125 1145 Helical; Name=14. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 1243 1263 Helical; Name=15. {ECO:0000255|PROSITE-ProRule:PRU00441}. TOPO_DOM 1 30 Extracellular. {ECO:0000255}.; TOPO_DOM 52 72 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 94 101 Extracellular. {ECO:0000255}.; TOPO_DOM 123 132 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 154 167 Extracellular. {ECO:0000255}.; TOPO_DOM 189 301 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 323 348 Extracellular. {ECO:0000255}.; TOPO_DOM 370 421 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 443 453 Extracellular. {ECO:0000255}.; TOPO_DOM 475 529 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 551 569 Extracellular. {ECO:0000255}.; TOPO_DOM 591 987 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1009 1031 Extracellular. {ECO:0000255}.; TOPO_DOM 1053 1124 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1146 1242 Extracellular. {ECO:0000255}.; TOPO_DOM 1264 1546 Cytoplasmic. {ECO:0000255}. FUNCTION: Subunit of ATP-sensitive potassium channels (KATP). Can form cardiac and smooth muscle-type KATP channels with KCNJ11. KCNJ11 forms the channel pore while ABCC9 is required for activation and regulation. SUBCELLULAR LOCATION: Membrane {ECO:0000255|PROSITE-ProRule:PRU00441}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. SUBUNIT: Interacts with KCNJ11. TISSUE SPECIFICITY: Isoforms SUR2A and SUR2B are found in cerebellum, eye, atrium, ventricle, urinary bladder and skeletal muscle. Isoform SUR2B is also found in forebrain, liver, lung, pancreas, kidney, spleen, stomach, small intestine, colon, uterus, ovary and fat tissue. Isoform SUR2C is expressed exclusively in the heart. +Q6P1F6 2ABA_MOUSE Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform (PP2A subunit B isoform B55-alpha) (PP2A subunit B isoform PR55-alpha) (PP2A subunit B isoform R2-alpha) (PP2A subunit B isoform alpha) 447 51,692 Chain (1); Initiator methionine (1); Modified residue (1); Repeat (7) FUNCTION: The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment. {ECO:0000250}. SUBUNIT: PP2A consists of a common heterodimeric core enzyme, composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant regulatory subunit (PR65 or subunit A), that associates with a variety of regulatory subunits. Proteins that associate with the core dimer include three families of regulatory subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa variable regulatory subunit, viral proteins, and cell signaling molecules (By similarity). Found in a complex with at least ARL2, PPP2CB, PPP2R1A, PPP2R2A, PPP2R5E and TBCD (By similarity). Interacts with TP53 (By similarity). Interacts with IER5 (By similarity). Interacts with MFHAS1; the interaction is direct (By similarity). Interacts with FAM122A (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P63151}. +Q60996 2A5G_MOUSE Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform (PP2A B subunit isoform B'-alpha-3) (PP2A B subunit isoform B'-gamma) (PP2A B subunit isoform B56-gamma) (PP2A B subunit isoform PR61-gamma) (PP2A B subunit isoform R5-gamma) 524 60,824 Alternative sequence (5); Chain (1); Modified residue (1); Sequence conflict (5) FUNCTION: The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment. The PP2A-PPP2R5C holoenzyme may activate TP53 and play a role in DNA damage-induced inhibition of cell proliferation. PP2A-PPP2R5C may also regulate the ERK signaling pathway through ERK dephosphorylation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, centromere {ECO:0000250}. SUBUNIT: PP2A consists of a common heterodimeric core enzyme, composed of PPP2CA a 36 kDa catalytic subunit (subunit C) and PPP2R1A a 65 kDa constant regulatory subunit (PR65 or subunit A), that associates with a variety of regulatory subunits. Proteins that associate with the core dimer include three families of regulatory subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa variable regulatory subunit, viral proteins, and cell signaling molecules. Interacts with SGO1 (By similarity). Interacts with SGO1; the interaction is direct. May interact with TP53 (By similarity). Interacts with IER3 and/or ERK kinases; regulates ERK dephosphorylation (By similarity). Interacts with CIP2A; this interaction stabilizes CIP2A (By similarity). {ECO:0000250|UniProtKB:Q13362}. TISSUE SPECIFICITY: Highest levels in heart, liver and brain. Lower levels in skeletal muscle, spleen, kidney and lung. Isoform 4 is testis-specific. {ECO:0000269|PubMed:15051958}. +P26150 3BHS3_MOUSE 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 3 (3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type III) (3-beta-HSD III) [Includes: 3-beta-hydroxy-Delta(5)-steroid dehydrogenase (EC 1.1.1.145) (3-beta-hydroxy-5-ene steroid dehydrogenase) (Progesterone reductase); Steroid Delta-isomerase (EC 5.3.3.1) (Delta-5-3-ketosteroid isomerase)] 373 42,031 Active site (1); Binding site (1); Chain (1); Transmembrane (1) TRANSMEM 288 308 Helical. {ECO:0000255}. Lipid metabolism; steroid biosynthesis. FUNCTION: 3-beta-HSD is a bifunctional enzyme, that catalyzes the oxidative conversion of Delta(5)-ene-3-beta-hydroxy steroid, and the oxidative conversion of ketosteroids. The 3-beta-HSD enzymatic system plays a crucial role in the biosynthesis of all classes of hormonal steroids. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. Mitochondrion membrane; Single-pass membrane protein. TISSUE SPECIFICITY: Liver and kidney. Greater expression in liver. +Q60590 A1AG1_MOUSE Alpha-1-acid glycoprotein 1 (AGP 1) (Orosomucoid-1) (OMD 1) 207 23,895 Chain (1); Disulfide bond (1); Glycosylation (5); Modified residue (1); Signal peptide (1) FUNCTION: Functions as transport protein in the blood stream. Binds various ligands in the interior of its beta-barrel domain (By similarity). Appears to function in modulating the activity of the immune system during the acute-phase reaction. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. DOMAIN: Contains a beta-barrel that binds various ligands in its interior. {ECO:0000250}. +P31387 5HT5B_MOUSE 5-hydroxytryptamine receptor 5B (5-HT-5B) (5-HT5B) (Serotonin receptor 5B) 370 41,201 Chain (1); Disulfide bond (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 53 75 Helical; Name=1. {ECO:0000250}.; TRANSMEM 91 111 Helical; Name=2. {ECO:0000250}.; TRANSMEM 129 150 Helical; Name=3. {ECO:0000250}.; TRANSMEM 172 194 Helical; Name=4. {ECO:0000250}.; TRANSMEM 212 232 Helical; Name=5. {ECO:0000250}.; TRANSMEM 296 316 Helical; Name=6. {ECO:0000250}.; TRANSMEM 334 354 Helical; Name=7. {ECO:0000250}. TOPO_DOM 1 52 Extracellular. {ECO:0000250}.; TOPO_DOM 76 90 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 112 128 Extracellular. {ECO:0000250}.; TOPO_DOM 151 171 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 195 211 Extracellular. {ECO:0000250}.; TOPO_DOM 233 295 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 317 333 Extracellular. {ECO:0000250}.; TOPO_DOM 355 370 Cytoplasmic. {ECO:0000250}. FUNCTION: This is one of the several different receptors for 5-hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. The activity of this receptor is mediated by G proteins. Probably involved in anxiety and depression. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed predominantly in the central nervous system; in the hippocampus, habenula, and the doral raphe. +Q9R1C8 5HT6R_MOUSE 5-hydroxytryptamine receptor 6 (5-HT-6) (5-HT6) (Serotonin receptor 6) 440 46,998 Chain (1); Disulfide bond (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 35 57 Helical; Name=1. {ECO:0000250}.; TRANSMEM 65 85 Helical; Name=2. {ECO:0000250}.; TRANSMEM 101 122 Helical; Name=3. {ECO:0000250}.; TRANSMEM 145 166 Helical; Name=4. {ECO:0000250}.; TRANSMEM 185 208 Helical; Name=5. {ECO:0000250}.; TRANSMEM 268 292 Helical; Name=6. {ECO:0000250}.; TRANSMEM 298 322 Helical; Name=7. {ECO:0000250}. TOPO_DOM 1 34 Extracellular. {ECO:0000250}.; TOPO_DOM 58 64 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 86 100 Extracellular. {ECO:0000250}.; TOPO_DOM 123 144 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 167 184 Extracellular. {ECO:0000250}.; TOPO_DOM 209 267 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 293 297 Extracellular. {ECO:0000250}.; TOPO_DOM 323 440 Cytoplasmic. {ECO:0000250}. FUNCTION: This is one of the several different receptors for 5-hydroxytryptamine (serotonin), a biogenic hormone that function as a neurotransmitter, a hormone, and a mitogen. The activity of this receptor is mediated by G proteins that stimulate adenylate cyclase. It has a high affinity for tricyclic psychotropic drugs (By similarity). Controls pyramidal neurons migration during corticogenesis, through the regulation of CDK5 activity (PubMed:25078650). Is an activator of TOR signaling (PubMed:23027611). {ECO:0000250|UniProtKB:P31388, ECO:0000269|PubMed:23027611, ECO:0000269|PubMed:25078650}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBUNIT: Interacts with CDK5 (PubMed:25078650). Interacts with MTOR (PubMed:23027611). Interacts with RPTOR and NF1 (By similarity). {ECO:0000250|UniProtKB:P50406, ECO:0000269|PubMed:23027611, ECO:0000269|PubMed:25078650}. +Q99P81 ABCG3_MOUSE ATP-binding cassette sub-family G member 3 650 73,613 Chain (1); Domain (2); Sequence conflict (1); Topological domain (7); Transmembrane (6) TRANSMEM 388 408 Helical; Name=1. {ECO:0000255}.; TRANSMEM 421 441 Helical; Name=2. {ECO:0000255}.; TRANSMEM 470 490 Helical; Name=3. {ECO:0000255}.; TRANSMEM 499 519 Helical; Name=4. {ECO:0000255}.; TRANSMEM 528 548 Helical; Name=5. {ECO:0000255}.; TRANSMEM 624 644 Helical; Name=6. {ECO:0000255}. TOPO_DOM 1 387 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 409 420 Extracellular. {ECO:0000255}.; TOPO_DOM 442 469 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 491 498 Extracellular. {ECO:0000255}.; TOPO_DOM 520 527 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 549 623 Extracellular. {ECO:0000255}.; TOPO_DOM 645 648 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: May dimerize with another subunit to form a functional transporter. TISSUE SPECIFICITY: Highest levels of expression in thymus and spleen. Detected in lung and small intestine. +Q60613 AA2AR_MOUSE Adenosine receptor A2a 410 44,971 Chain (1); Disulfide bond (4); Glycosylation (2); Region (3); Sequence conflict (8); Topological domain (8); Transmembrane (7) TRANSMEM 5 29 Helical; Name=1. {ECO:0000250}.; TRANSMEM 40 63 Helical; Name=2. {ECO:0000250}.; TRANSMEM 75 97 Helical; Name=3. {ECO:0000250}.; TRANSMEM 118 140 Helical; Name=4. {ECO:0000250}.; TRANSMEM 169 193 Helical; Name=5. {ECO:0000250}.; TRANSMEM 230 253 Helical; Name=6. {ECO:0000250}.; TRANSMEM 262 285 Helical; Name=7. {ECO:0000250}. TOPO_DOM 1 4 Extracellular. {ECO:0000250}.; TOPO_DOM 30 39 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 64 74 Extracellular. {ECO:0000250}.; TOPO_DOM 98 117 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 141 168 Extracellular. {ECO:0000250}.; TOPO_DOM 194 229 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 254 261 Extracellular. {ECO:0000250}.; TOPO_DOM 286 410 Cytoplasmic. {ECO:0000250}. FUNCTION: Receptor for adenosine. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. PTM: Ubiquitinated. Deubiquitinated by USP4; leading to stabilization and expression at the cell surface (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBUNIT: Interacts (via cytoplasmic C-terminal domain) with USP4; the interaction is direct. May interact with DRD4. Interacts with NECAB2 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P29274}. DOMAIN: The cytoplasmic C-terminal domain is necessary for targeting the non-ubiquitinated form of this protein to the cell surface. {ECO:0000250}. +P55194 3BP1_MOUSE SH3 domain-binding protein 1 (3BP-1) 680 74,172 Chain (1); Compositional bias (1); Domain (2); Erroneous initiation (2); Modified residue (6); Motif (1); Region (2); Sequence conflict (10) FUNCTION: GTPase activating protein (GAP) which specifically converts GTP-bound Rho-type GTPases including RAC1 and CDC42 in their inactive GDP-bound form (PubMed:7621827). By specifically inactivating RAC1 at the leading edge of migrating cells, it regulates the spatiotemporal organization of cell protrusions which is important for proper cell migration. Also negatively regulates CDC42 in the process of actin remodeling and the formation of epithelial cell junctions. Through its GAP activity toward RAC1 and/or CDC42 plays a specific role in phagocytosis of large particles. Specifically recruited by a PI3 kinase/PI3K-dependent mechanism to sites of large particles engagement, inactivates RAC1 and/or CDC42 allowing the reorganization of the underlying actin cytoskeleton required for engulfment. It also plays a role in angiogenesis and the process of repulsive guidance as part of a semaphorin-plexin signaling pathway. Following the binding of PLXND1 to extracellular SEMA3E it dissociates from PLXND1 and inactivates RAC1, inducing the intracellular reorganization of the actin cytoskeleton and the collapse of cells (By similarity). {ECO:0000250|UniProtKB:Q9Y3L3, ECO:0000269|PubMed:7621827}. SUBCELLULAR LOCATION: Cell projection {ECO:0000250|UniProtKB:Q9Y3L3}. Cell junction, tight junction {ECO:0000269|PubMed:22891260}. Cell junction, adherens junction {ECO:0000250|UniProtKB:Q9Y3L3}. Cell projection, phagocytic cup {ECO:0000250|UniProtKB:Q9Y3L3}. Nucleus {ECO:0000250|UniProtKB:Q9Y3L3}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9Y3L3}. Note=Localizes at the leading edge of migrating cells. Accumulation at forming phagocytic cups is PI3 kinase/PI3K-dependent and is specific for sites of large particles engagement and their phosphatidylinositol 3,4,5-triphosphate membrane content. {ECO:0000250|UniProtKB:Q9Y3L3}. SUBUNIT: Interacts with RAC1 (PubMed:10508610). Interacts with the exocyst via EXOC4 and EXOC8; required for the localization of both SH3BP1 and the exocyst to the leading edge of migrating cells. Interacts with CD2AP and CGNL1; probably part of a complex at cell junctions. Interacts with CAPZA1; recruits CAPZA1 to forming cell junctions. May interact with AFDN. Interacts with PLXND1; they dissociate upon SEMA3E binding to PLXND1 allowing SH3BP1 to transduce downstream signal through RAC1 inactivation (By similarity). Interacts with ABL1, GRB2 and SRC (via SH3 domain) (PubMed:8438166, PubMed:1379745). {ECO:0000250|UniProtKB:Q9Y3L3, ECO:0000269|PubMed:10508610, ECO:0000269|PubMed:1379745, ECO:0000269|PubMed:8438166}. DOMAIN: The BAR domain mediates interaction with the exocyst components EXOC4 and EXOC8 and is required for the function in cell migration. It also mediates the interaction with PLXND1. {ECO:0000250|UniProtKB:Q9Y3L3}. TISSUE SPECIFICITY: Expressed in all tissues examined. Highest levels found in spleen and brain, lowest in heart and liver. {ECO:0000269|PubMed:7621827}. +Q04841 3MG_MOUSE DNA-3-methyladenine glycosylase (EC 3.2.2.21) (3-alkyladenine DNA glycosylase) (3-methyladenine DNA glycosidase) (ADPG) (N-methylpurine-DNA glycosylase) 333 36,472 Chain (1); Modified residue (2); Sequence conflict (4) FUNCTION: Hydrolysis of the deoxyribose N-glycosidic bond to excise 3-methyladenine, and 7-methylguanine from the damaged DNA polymer formed by alkylation lesions. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Mitochondrion matrix, mitochondrion nucleoid {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Binds MBD1. Binds SSBP1. {ECO:0000250}. +Q3UFY7 5NT3B_MOUSE 7-methylguanosine phosphate-specific 5'-nucleotidase (7-methylguanosine nucleotidase) (EC 3.1.3.91) (Cytosolic 5'-nucleotidase 3B) (Cytosolic 5'-nucleotidase III-like protein) (cN-III-like protein) (EC 3.1.3.5) (N(7)-methylguanylate 5'-phosphatase) 300 34,425 Active site (2); Alternative sequence (5); Binding site (3); Chain (1); Erroneous gene model prediction (2); Erroneous initiation (3); Frameshift (1); Metal binding (3); Modified residue (1); Region (1); Sequence conflict (3) FUNCTION: Specifically hydrolyzes 7-methylguanosine monophosphate (m(7)GMP) to 7-methylguanosine and inorganic phosphate. The specific activity for m(7)GMP may protect cells against undesired salvage of m(7)GMP and its incorporation into nucleic acids. Also has weak activity for CMP. UMP and purine nucleotides are poor substrates (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. SUBUNIT: Monomer. {ECO:0000250}. +Q63805 A1AG3_MOUSE Alpha-1-acid glycoprotein 3 (AGP 3) (Orosomucoid-3) (OMD 3) 206 24,069 Chain (1); Disulfide bond (1); Glycosylation (3); Signal peptide (1) FUNCTION: Functions as transport protein in the blood stream. Binds various ligands in the interior of its beta-barrel domain (By similarity). Appears to function in modulating the activity of the immune system during the acute-phase reaction. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. DOMAIN: Contains a beta-barrel that binds various ligands in its interior. {ECO:0000250}. +Q60612 AA1R_MOUSE Adenosine receptor A1 326 36,638 Chain (1); Disulfide bond (1); Erroneous initiation (1); Glycosylation (2); Lipidation (1); Sequence conflict (3); Topological domain (8); Transmembrane (7) TRANSMEM 11 33 Helical; Name=1. {ECO:0000255}.; TRANSMEM 47 69 Helical; Name=2. {ECO:0000255}.; TRANSMEM 81 102 Helical; Name=3. {ECO:0000255}.; TRANSMEM 124 146 Helical; Name=4. {ECO:0000255}.; TRANSMEM 177 201 Helical; Name=5. {ECO:0000255}.; TRANSMEM 236 259 Helical; Name=6. {ECO:0000255}.; TRANSMEM 268 292 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 10 Extracellular. {ECO:0000255}.; TOPO_DOM 34 46 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 70 80 Extracellular. {ECO:0000255}.; TOPO_DOM 103 123 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 147 176 Extracellular. {ECO:0000255}.; TOPO_DOM 202 235 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 260 267 Extracellular. {ECO:0000255}.; TOPO_DOM 293 326 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for adenosine. The activity of this receptor is mediated by G proteins which inhibit adenylyl cyclase. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q7TMS5 ABCG2_MOUSE ATP-binding cassette sub-family G member 2 (Breast cancer resistance protein 1 homolog) (Urate exporter) (CD antigen CD338) 657 72,978 Chain (1); Disulfide bond (2); Domain (2); Glycosylation (2); Nucleotide binding (1); Sequence conflict (3); Topological domain (7); Transmembrane (6) TRANSMEM 394 414 Helical. {ECO:0000255}.; TRANSMEM 429 449 Helical. {ECO:0000255}.; TRANSMEM 478 498 Helical. {ECO:0000255}.; TRANSMEM 507 527 Helical. {ECO:0000255}.; TRANSMEM 536 556 Helical. {ECO:0000255}.; TRANSMEM 633 653 Helical. {ECO:0000255}. TOPO_DOM 1 393 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 415 428 Extracellular. {ECO:0000255}.; TOPO_DOM 450 477 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 499 506 Extracellular. {ECO:0000255}.; TOPO_DOM 528 535 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 557 632 Extracellular. {ECO:0000255}.; TOPO_DOM 654 657 Cytoplasmic. {ECO:0000255}. FUNCTION: High-capacity urate exporter functioning in both renal and extrarenal urate excretion. Plays a role in porphyrin homeostasis as it is able to mediates the export of protoporhyrin IX (PPIX) both from mitochondria to cytosol and from cytosol to extracellular space, and cellular export of hemin, and heme. Xenobiotic transporter that may play an important role in the exclusion of xenobiotics from the brain (By similarity). May play a role in early stem cell self-renewal by blocking differentiation. {ECO:0000250, ECO:0000269|PubMed:10485464, ECO:0000269|PubMed:11533706}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9UNQ0}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q9UNQ0}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Monomer under reducing conditions, the minimal functional unit is a homodimer; disulfide-linked, but the major oligomeric form in plasma membranes is a homotetramer with possibility of higher order oligomerization up to homododecamers. {ECO:0000250}. DOMAIN: The extracellular loop 3 (ECL3) is involved in binding porphyrins and transfer them to other carriers, probably albumin. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in kidney. Lower expression in liver, colon, heart, spleen, and placenta. {ECO:0000269|PubMed:11036110}. +A2AIG8 1A1L1_MOUSE 1-aminocyclopropane-1-carboxylate synthase-like protein 1 (ACC synthase-like protein 1) 502 56,879 Alternative sequence (1); Binding site (1); Chain (1); Modified residue (1) FUNCTION: Does not catalyze the synthesis of 1-aminocyclopropane-1-carboxylate but is capable of catalyzing the deamination of L-vinylglycine. {ECO:0000250|UniProtKB:Q96QU6}. +Q9EST3 4ET_MOUSE Eukaryotic translation initiation factor 4E transporter (4E-T) (eIF4E transporter) (Eukaryotic translation initiation factor 4E nuclear import factor 1) 983 107,986 Alternative sequence (1); Chain (1); Compositional bias (1); Cross-link (1); Modified residue (17); Motif (3); Region (1); Sequence conflict (2) FUNCTION: Nucleoplasmic shuttling protein, which inhibits translation initiation. Mediates the nuclear import of EIF4E by a piggy-back mechanism. {ECO:0000250|UniProtKB:Q9NRA8}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NRA8}. Nucleus {ECO:0000250|UniProtKB:Q9NRA8}. Nucleus, PML body {ECO:0000250|UniProtKB:Q9NRA8}. Nucleus speckle {ECO:0000250|UniProtKB:Q9NRA8}. Note=Predominantly cytoplasmic. Shuttles between the nucleus and the cytoplasm in a CRM1-dependent manner. Localization to nuclear foci and speckles requires active transcription. {ECO:0000250|UniProtKB:Q9NRA8}. SUBUNIT: Interacts with EIF4E. Interacts with importin beta only in the presence of importin alpha, suggesting a direct interaction with importin alpha. Interacts with APOBEC3G in an RNA-dependent manner. {ECO:0000250|UniProtKB:Q9NRA8}. +P34968 5HT2C_MOUSE 5-hydroxytryptamine receptor 2C (5-HT-2C) (5-HT2C) (5-HTR2C) (5-hydroxytryptamine receptor 1C) (5-HT-1C) (5-HT1C) (Serotonin receptor 2C) 459 51,929 Chain (1); Disulfide bond (2); Glycosylation (3); Motif (3); Region (2); Sequence conflict (2); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 54 79 Helical; Name=1. {ECO:0000250}.; TRANSMEM 91 111 Helical; Name=2. {ECO:0000250}.; TRANSMEM 129 151 Helical; Name=3. {ECO:0000250}.; TRANSMEM 172 194 Helical; Name=4. {ECO:0000250}.; TRANSMEM 215 236 Helical; Name=5. {ECO:0000250}.; TRANSMEM 313 334 Helical; Name=6. {ECO:0000250}.; TRANSMEM 350 372 Helical; Name=7. {ECO:0000250}. TOPO_DOM 33 53 Extracellular. {ECO:0000250}.; TOPO_DOM 80 90 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 112 128 Extracellular. {ECO:0000250}.; TOPO_DOM 152 171 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 195 214 Extracellular. {ECO:0000250}.; TOPO_DOM 237 312 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 335 349 Extracellular. {ECO:0000250}.; TOPO_DOM 373 459 Cytoplasmic. {ECO:0000250}. FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various drugs and psychoactive substances, including ergot alkaloid derivatives, 1-2,5,-dimethoxy-4-iodophenyl-2-aminopropane (DOI) and lysergic acid diethylamide (LSD). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Beta-arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways. Signaling activates a phosphatidylinositol-calcium second messenger system that modulates the activity of phosphatidylinositol 3-kinase and down-stream signaling cascades and promotes the release of Ca(2+) ions from intracellular stores. Regulates neuronal activity via the activation of short transient receptor potential calcium channels in the brain, and thereby modulates the activation of pro-opiomelacortin neurons and the release of CRH that then regulates the release of corticosterone. Plays a role in the regulation of appetite and feeding behavior, responses to anxiogenic stimuli and stress. Plays a role in insulin sensitivity and glucose homeostasis. {ECO:0000269|PubMed:17451451, ECO:0000269|PubMed:17596444, ECO:0000269|PubMed:19038216, ECO:0000269|PubMed:21037584, ECO:0000269|PubMed:21048120, ECO:0000269|PubMed:21835345, ECO:0000269|PubMed:7700379, ECO:0000269|PubMed:9771748}. PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBUNIT: Interacts with MPDZ. Interacts with ARRB2 (By similarity). {ECO:0000250}. DOMAIN: The PDZ domain-binding motif is involved in the interaction with MPDZ. {ECO:0000250}. TISSUE SPECIFICITY: Detected in brain cortex, hypothalamus, brainstem and arcuate nucleus. Detected in the paraventricular nucleus of the hypothalamus. {ECO:0000269|PubMed:17596444, ECO:0000269|PubMed:19038216, ECO:0000269|PubMed:7700379}. +Q91WG5 AAKG2_MOUSE 5'-AMP-activated protein kinase subunit gamma-2 (AMPK gamma2) (AMPK subunit gamma-2) 566 62,949 Alternative sequence (1); Binding site (9); Chain (1); Domain (4); Modified residue (11); Motif (1); Nucleotide binding (6); Sequence conflict (2) FUNCTION: AMP/ATP-binding subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (PRKAA1 or PRKAA2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits. ADP also stimulates phosphorylation, without stimulating already phosphorylated catalytic subunit. ATP promotes dephosphorylation of catalytic subunit, rendering the AMPK enzyme inactive (By similarity). {ECO:0000250}. PTM: Phosphorylated by ULK1; leading to negatively regulate AMPK activity and suggesting the existence of a regulatory feedback loop between ULK1 and AMPK. {ECO:0000269|PubMed:21460634}. SUBUNIT: AMPK is a heterotrimer of an alpha catalytic subunit (PRKAA1 or PRKAA2), a beta (PRKAB1 or PRKAB2) and a gamma non-catalytic subunits (PRKAG1, PRKAG2 or PRKAG3). Interacts with FNIP1 and FNIP2 (By similarity). {ECO:0000250}. DOMAIN: The AMPK pseudosubstrate motif resembles the sequence around sites phosphorylated on target proteins of AMPK, except the presence of a non-phosphorylatable residue in place of Ser. In the absence of AMP this pseudosubstrate sequence may bind to the active site groove on the alpha subunit (PRKAA1 or PRKAA2), preventing phosphorylation by the upstream activating kinase STK11/LKB1 (By similarity). {ECO:0000250}.; DOMAIN: The 4 CBS domains mediate binding to nucleotides. Of the 4 potential nucleotide-binding sites, 3 are occupied, designated as sites 1, 3, and 4 based on the CBS modules that provide the acidic residue for coordination with the 2'- and 3'-hydroxyl groups of the ribose of AMP. Of these, site 4 appears to be a structural site that retains a tightly held AMP molecule (AMP 3). The 2 remaining sites, 1 and 3, can bind either AMP, ADP or ATP. Site 1 (AMP, ADP or ATP 1) is the high-affinity binding site and likely accommodates AMP or ADP. Site 3 (AMP, ADP or ATP 2) is the weakest nucleotide-binding site on the gamma subunit, yet it is exquisitely sensitive to changes in nucleotide levels and this allows AMPK to respond rapidly to changes in cellular energy status. Site 3 is likely to be responsible for protection of a conserved threonine in the activation loop of the alpha catalytic subunit through conformational changes induced by binding of AMP or ADP. {ECO:0000250|UniProtKB:P80385}. +P53368 8ODP_MOUSE 7,8-dihydro-8-oxoguanine triphosphatase (EC 3.6.1.55) (2-hydroxy-dATP diphosphatase) (EC 3.6.1.56) (8-oxo-dGTPase) (Nucleoside diphosphate-linked moiety X motif 1) (Nudix motif 1) 156 17,908 Beta strand (9); Binding site (3); Chain (1); Domain (1); Helix (4); Metal binding (4); Motif (1); Region (2); Sequence conflict (1); Signal peptide (1); Site (3); Turn (1) FUNCTION: Antimutagenic (PubMed:11572992). Plays a redundant role in sanitizing oxidized nucleotide pools, such as 8-oxo-dGTP pools (PubMed:29281266). Acts as a sanitizing enzyme for oxidized nucleotide pools, thus suppressing cell dysfunction and death induced by oxidative stress. Hydrolyzes 8-oxo-dGTP, 8-oxo-dATP and 2-OH-dATP, thus preventing misincorporation of oxidized purine nucleoside triphosphates into DNA and subsequently preventing A:T to C:G and G:C to T:A transversions. Able to hydrolyze also the corresponding ribonucleotides, 2-OH-ATP, 8-oxo-GTP and 8-oxo-ATP (By similarity). Does not play a role in U8 snoRNA decapping activity (PubMed:21070968). Binds U8 snoRNA (PubMed:21070968). {ECO:0000250|UniProtKB:P36639, ECO:0000269|PubMed:11572992, ECO:0000269|PubMed:21070968, ECO:0000269|PubMed:7592783, ECO:0000305|PubMed:29281266}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P53369}. Nucleus {ECO:0000250|UniProtKB:P53369}. Nucleus membrane {ECO:0000250|UniProtKB:P53369}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250|UniProtKB:P53369}. SUBUNIT: Monomer. {ECO:0000305|PubMed:29281266}. TISSUE SPECIFICITY: High expression levels detected in thymus, liver, spleen, kidney, testis and large intestine, with lower levels detected in brain, heart, lung and stomach (at protein level). Expressed in kidney, liver and small intestine. {ECO:0000269|PubMed:7592783}. +P68510 1433F_MOUSE 14-3-3 protein eta 246 28,212 Chain (1); Helix (9); Initiator methionine (1); Modified residue (3); Sequence conflict (1); Site (2); Turn (3) FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negatively regulates the kinase activity of PDPK1 (By similarity). {ECO:0000250}. PTM: Phosphorylated on Ser-59 by protein kinase C delta type catalytic subunit in a sphingosine-dependent fashion. {ECO:0000269|PubMed:9705322}. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Homodimer (By similarity). Interacts with many nuclear hormone receptors and cofactors including AR, ESR1, ESR2, MC2R, NR3C1, NRIP1, PPARBP and THRA. Interacts with ABL1 (phosphorylated form); the interaction retains it in the cytoplasm. Weakly interacts with CDKN1B (By similarity). Interacts with ARHGEF28 and CDK16. Interacts with KCNK18 in a phosphorylation-dependent manner. Interacts with SAMSN1. Interacts with the 'Ser-241' phosphorylated form of PDPK1 (By similarity). Interacts with the 'Thr-369' phosphorylated form of DAPK2 (PubMed:26047703). Interacts with PI4KB, TBC1D22A and TBC1D22B (By similarity). Interacts with SLITRK1 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q04917, ECO:0000269|PubMed:26047703}. +Q6ZWR4 2ABB_MOUSE Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B beta isoform (PP2A subunit B isoform B55-beta) (PP2A subunit B isoform PR55-beta) (PP2A subunit B isoform R2-beta) (PP2A subunit B isoform beta) 443 51,710 Alternative sequence (2); Chain (1); Erroneous gene model prediction (1); Modified residue (3); Repeat (7); Sequence caution (1); Sequence conflict (1) FUNCTION: The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment. Within the PP2A holoenzyme complex, isoform 2 is required to promote proapoptotic activity. Isoform 2 regulates neuronal survival through the mitochondrial fission and fusion balance. {ECO:0000250}. SUBCELLULAR LOCATION: Isoform 1: Cytoplasm. Cytoplasm, cytoskeleton. Membrane.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm {ECO:0000250}. Mitochondrion {ECO:0000250}. Mitochondrion outer membrane {ECO:0000250}. Note=Under basal conditions, localizes to both cytosolic and mitochondrial compartments. Relocalizes from the cytosolic to the mitochondrial compartment during apoptosis. Its targeting to the outer mitochondrial membrane (OMM) involves an association with import receptors of the TOM complex and is required to promote proapoptotic activity (By similarity). {ECO:0000250}. SUBUNIT: PP2A consists of a common heterodimeric core enzyme, composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant regulatory subunit (PR65 or subunit A), that associates with a variety of regulatory subunits. Proteins that associate with the core dimer include three families of regulatory subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa variable regulatory subunit, viral proteins, and cell signaling molecules (By similarity). Interacts with TOMM22 (By similarity). Interacts with IER5 (via N- and C-terminal regions) (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P36877, ECO:0000250|UniProtKB:Q00005}. DOMAIN: The N-terminal 26 residues of isoform 2 constitute a cryptic mitochondrial matrix import signal with critical basic and hydrophobic residues, that is necessary and sufficient for targeting the PP2A holoenzyme to the outer mitochondrial membrane (OMM) and does not affect holoenzyme formation or catalytic activity. {ECO:0000250}.; DOMAIN: The last WD repeat of isoform 2 constitutes a mitochondrial stop-transfer domain that confers resistance to the unfolding step process required for import and therefore prevents PPP2R2B matrix translocation and signal sequence cleavage. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain, testis, lung and spleen. In the brain, expressed in the cortex, hippocampus and cerebellum (at protein level). {ECO:0000269|PubMed:12473071}. +Q78JT3 3HAO_MOUSE 3-hydroxyanthranilate 3,4-dioxygenase (EC 1.13.11.6) (3-hydroxyanthranilate oxygenase) (3-HAO) (3-hydroxyanthranilic acid dioxygenase) (HAD) 286 32,804 Binding site (4); Chain (1); Metal binding (3); Region (3) Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 3/3. FUNCTION: Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate. {ECO:0000255|HAMAP-Rule:MF_03019}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000255|HAMAP-Rule:MF_03019}. SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03019, ECO:0000269|PubMed:28792876}. +P28334 5HT1B_MOUSE 5-hydroxytryptamine receptor 1B (5-HT-1B) (5-HT1B) (Serotonin receptor 1B) 386 43,079 Chain (1); Disulfide bond (1); Glycosylation (2); Lipidation (1); Motif (2); Region (2); Site (1); Topological domain (8); Transmembrane (7) TRANSMEM 46 71 Helical; Name=1. {ECO:0000250}.; TRANSMEM 81 106 Helical; Name=2. {ECO:0000250}.; TRANSMEM 120 141 Helical; Name=3. {ECO:0000250}.; TRANSMEM 162 183 Helical; Name=4. {ECO:0000250}.; TRANSMEM 202 224 Helical; Name=5. {ECO:0000250}.; TRANSMEM 312 332 Helical; Name=6. {ECO:0000250}.; TRANSMEM 346 367 Helical; Name=7. {ECO:0000250}. TOPO_DOM 1 45 Extracellular. {ECO:0000250}.; TOPO_DOM 72 80 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 107 119 Extracellular. {ECO:0000250}.; TOPO_DOM 142 161 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 184 201 Extracellular. {ECO:0000250}.; TOPO_DOM 225 311 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 333 345 Extracellular. {ECO:0000250}.; TOPO_DOM 368 386 Cytoplasmic. {ECO:0000250}. FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various alkaloids and psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity. Arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways. Regulates the release of 5-hydroxytryptamine, dopamine and acetylcholine in the brain, and thereby affects neural activity, nociceptive processing, pain perception, mood and behavior. Besides, plays a role in vasoconstriction of cerebral arteries. {ECO:0000269|PubMed:10651141, ECO:0000269|PubMed:1557407, ECO:0000269|PubMed:16750486, ECO:0000269|PubMed:8091214, ECO:0000269|PubMed:8742487, ECO:0000269|PubMed:9349547}. PTM: Phosphorylated. {ECO:0000250}.; PTM: Palmitoylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1557407}; Multi-pass membrane protein {ECO:0000269|PubMed:1557407}. SUBUNIT: Homodimer. Heterodimer with HTR1D (By similarity). {ECO:0000250}. DOMAIN: Ligands are bound in a hydrophobic pocket formed by the transmembrane helices. {ECO:0000250}. TISSUE SPECIFICITY: Predominantly expressed in striatum and Purkinje cells. {ECO:0000269|PubMed:1557407}. +P07758 A1AT1_MOUSE Alpha-1-antitrypsin 1-1 (AAT) (Alpha-1 protease inhibitor 1) (Alpha-1-antiproteinase) (Serine protease inhibitor 1-1) (Serine protease inhibitor A1a) (Serpin A1a) 413 46,003 Chain (1); Glycosylation (3); Region (1); Sequence conflict (17); Signal peptide (1); Site (1) FUNCTION: Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. {ECO:0000269|PubMed:11961105, ECO:0000269|PubMed:8619829}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11961105, ECO:0000269|PubMed:8619829}. DOMAIN: The reactive center loop (RCL) extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site within the RCL, establishing a covalent linkage between the carboxyl group of the serpin reactive site and the serine hydroxyl of the protease. The resulting inactive serpin-protease complex is highly stable (By similarity). Variability within the reactive center loop (RCL) sequences of Serpina1-related genes may determine target protease specificity. {ECO:0000250}. +Q61224 5HT1D_MOUSE 5-hydroxytryptamine receptor 1D (5-HT-1D) (5-HT1D) (Serotonin receptor 1D) 374 41,594 Chain (1); Disulfide bond (1); Glycosylation (3); Motif (2); Region (2); Sequence conflict (8); Topological domain (8); Transmembrane (7) TRANSMEM 36 61 Helical; Name=1. {ECO:0000250}.; TRANSMEM 73 95 Helical; Name=2. {ECO:0000250}.; TRANSMEM 110 131 Helical; Name=3. {ECO:0000250}.; TRANSMEM 152 173 Helical; Name=4. {ECO:0000250}.; TRANSMEM 192 214 Helical; Name=5. {ECO:0000250}.; TRANSMEM 300 323 Helical; Name=6. {ECO:0000250}.; TRANSMEM 333 357 Helical; Name=7. {ECO:0000250}. TOPO_DOM 1 35 Extracellular. {ECO:0000250}.; TOPO_DOM 62 72 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 96 109 Extracellular. {ECO:0000250}.; TOPO_DOM 132 151 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 174 191 Extracellular. {ECO:0000250}.; TOPO_DOM 215 299 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 324 332 Extracellular. {ECO:0000250}.; TOPO_DOM 358 374 Cytoplasmic. {ECO:0000250}. FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various alkaloids and psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity. Regulates the release of 5-hydroxytryptamine in the brain, and thereby affects neural activity. May also play a role in regulating the release of other neurotransmitters. May play a role in vasoconstriction. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBUNIT: Homodimer. Heterodimer with HTR1B (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Detected in the motor column in spinal cord, and in several cranial motor nuclei, including nucleus ambiguous, oculomotoris, trochelaris and abducens. Detected in gamma motor neurons in the lumbar spinal cord. Detected in proprioceptive sensory neurons in dorsal root ganglia. {ECO:0000269|PubMed:22273508}. +Q02284 5HT1F_MOUSE 5-hydroxytryptamine receptor 1F (5-HT-1F) (5-HT1F) (5-HT-1E-beta) (Serotonin receptor 1F) 366 41,977 Chain (1); Disulfide bond (1); Glycosylation (2); Motif (2); Region (2); Topological domain (8); Transmembrane (7) TRANSMEM 30 50 Helical; Name=1. {ECO:0000250}.; TRANSMEM 61 83 Helical; Name=2. {ECO:0000250}.; TRANSMEM 98 118 Helical; Name=3. {ECO:0000250}.; TRANSMEM 141 161 Helical; Name=4. {ECO:0000250}.; TRANSMEM 179 201 Helical; Name=5. {ECO:0000250}.; TRANSMEM 291 311 Helical; Name=6. {ECO:0000250}.; TRANSMEM 330 350 Helical; Name=7. {ECO:0000250}. TOPO_DOM 1 29 Extracellular. {ECO:0000250}.; TOPO_DOM 51 60 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 84 97 Extracellular. {ECO:0000250}.; TOPO_DOM 119 140 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 162 178 Extracellular. {ECO:0000250}.; TOPO_DOM 202 290 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 312 329 Extracellular. {ECO:0000250}.; TOPO_DOM 351 366 Cytoplasmic. {ECO:0000250}. FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various alkaloids and psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity. {ECO:0000269|PubMed:1328180}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1328180}; Multi-pass membrane protein {ECO:0000269|PubMed:1328180}. TISSUE SPECIFICITY: Detected in hippocampus. {ECO:0000269|PubMed:1328180}. +P24721 ASGR2_MOUSE Asialoglycoprotein receptor 2 (ASGP-R 2) (ASGPR 2) (Hepatic lectin 2) (HL-2) (mHL-2) 301 34,907 Chain (1); Disulfide bond (3); Domain (1); Glycosylation (3); Lipidation (1); Modified residue (1); Topological domain (2); Transmembrane (1) TRANSMEM 59 79 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 58 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 80 301 Extracellular. {ECO:0000255}. FUNCTION: Mediates the endocytosis of plasma glycoproteins to which the terminal sialic acid residue on their complex carbohydrate moieties has been removed. The receptor recognizes terminal galactose and N-acetylgalactosamine units. After ligand binding to the receptor, the resulting complex is internalized and transported to a sorting organelle, where receptor and ligand are disassociated. The receptor then returns to the cell membrane surface. SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. SUBUNIT: Interacts with LASS2. {ECO:0000250}. TISSUE SPECIFICITY: Expressed exclusively in hepatic parenchymal cells. +Q91X20 ASH2L_MOUSE Set1/Ash2 histone methyltransferase complex subunit ASH2 (ASH2-like protein) 623 68,250 Chain (1); Domain (1); Modified residue (3); Region (1); Sequence conflict (3); Zinc finger (2) FUNCTION: Component of the Set1/Ash2 histone methyltransferase (HMT) complex, a complex that specifically methylates 'Lys-4' of histone H3, but not if the neighboring 'Lys-9' residue is already methylated. As part of the MLL1/MLL complex it is involved in methylation and dimethylation at 'Lys-4' of histone H3. May function as a transcriptional regulator. May play a role in hematopoiesis (By similarity). {ECO:0000250}. PTM: Both monomethylated and dimethylated on arginine residues in the C-terminus. Arg-291 is the major site. Methylation is not required for nuclear localization, nor for MLL complex integrity or maintenance of global histone H3K4me3 levels (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Interacts with HCFC1 (By similarity). Component of the SET1 complex, at least composed of the catalytic subunit (SETD1A or SETD1B), WDR5, WDR82, RBBP5, ASH2L/ASH2, CXXC1/CFP1, HCFC1 and DPY30 (By similarity). Interacts with SETD1A and SETD1B (By similarity). Core component of several methyltransferase-containing complexes including MLL1/MLL, MLL2/3 (also named ASCOM complex) and MLL4/WBP7. Each complex is at least composed of ASH2L, RBBP5, WDR5, DPY30, one or more specific histone methyltransferases (KMT2A/MLL1, KMT2D/MLL2, KMT2C/MLL3 and KMT2B/MLL4), and the facultative components PAGR1, BAP18, CHD8, E2F6, HCFC1, HCFC2, HSP70, INO80C, KDM6A, KANSL1, LAS1L, MAX, MCRS1, MEN1, MGA, KAT8/MOF, NCOA6, PAXIP1/PTIP, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9, TEX10 and alpha- and beta-tubulin. {ECO:0000250, ECO:0000269|PubMed:21335234}. TISSUE SPECIFICITY: Ubiquitously expressed, with abundant expression in the heart, skeletal muscle and kidney. Low expression is seen in spleen, lung and testis. {ECO:0000269|PubMed:10393421}. +Q03288 ASIP_MOUSE Agouti-signaling protein (ASP) (Agouti coat color protein) (Agouti switch protein) 131 14,313 Chain (1); Compositional bias (1); Disulfide bond (5); Domain (1); Glycosylation (1); Sequence conflict (8); Signal peptide (1) FUNCTION: Involved in the regulation of melanogenesis. The binding of ASP to MC1R precludes alpha-MSH initiated signaling and thus blocks production of cAMP, leading to a down-regulation of eumelanogenesis (brown/black pigment) and thus increasing synthesis of pheomelanin (yellow/red pigment). Causes hair follicle melanocytes to synthesize phaeomelanin instead of black or brown pigment eumelanin and produces hairs with a subapical yellow band on an otherwise black or brown background when expressed during the mid-portion of hair growth. SUBCELLULAR LOCATION: Secreted. DOMAIN: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin. {ECO:0000250}. TISSUE SPECIFICITY: Epithelial cells of the hair follicles and the epidermis. +Q6IQX7 CHSS2_MOUSE Chondroitin sulfate synthase 2 (EC 2.4.1.175) (EC 2.4.1.226) (Chondroitin glucuronyltransferase 2) (Chondroitin-polymerizing factor) (ChPF) (Glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase II) (N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase II) (N-acetylgalactosaminyltransferase 2) 774 85,534 Alternative sequence (2); Chain (1); Glycosylation (2); Metal binding (1); Topological domain (2); Transmembrane (1) TRANSMEM 16 34 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 15 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 35 774 Lumenal. {ECO:0000255}. FUNCTION: Has both beta-1,3-glucuronic acid and beta-1,4-N-acetylgalactosamine transferase activity. Transfers glucuronic acid (GlcUA) from UDP-GlcUA and N-acetylgalactosamine (GalNAc) from UDP-GalNAc to the non-reducing end of the elongating chondroitin polymer (By similarity). Isoform 2 may facilitate PRKN transport into the mitochondria. In collaboration with PRKN, isoform 2 may enhance cell viability and protect cells from oxidative stress (By similarity). {ECO:0000250|UniProtKB:Q8IZ52}. SUBCELLULAR LOCATION: Isoform 1: Golgi apparatus, Golgi stack membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8IZ52}.; SUBCELLULAR LOCATION: Isoform 3: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8IZ52}. Mitochondrion {ECO:0000250|UniProtKB:Q8IZ52}.; SUBCELLULAR LOCATION: Isoform 2: Mitochondrion matrix {ECO:0000250|UniProtKB:Q8IZ52}. SUBUNIT: Binds CHSY1. Isoform 1, isoform 2 and isoform 3 interact with PRKN. TISSUE SPECIFICITY: Isoform 1, isoform 2 and isoform 3 are expressed in brain (at protein level). {ECO:0000269|PubMed:22082830}. +Q8BQ86 CHST8_MOUSE Carbohydrate sulfotransferase 8 (EC 2.8.2.-) (GalNAc-4-O-sulfotransferase 1) (GalNAc-4-ST1) (GalNAc4ST-1) (N-acetylgalactosamine-4-O-sulfotransferase 1) 417 48,282 Chain (1); Glycosylation (5); Nucleotide binding (2); Sequence conflict (5); Topological domain (2); Transmembrane (1) TRANSMEM 11 31 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 10 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 32 417 Lumenal. {ECO:0000255}. FUNCTION: Catalyzes the transfer of sulfate to position 4 of non-reducing N-acetylgalactosamine (GalNAc) residues in both N-glycans and O-glycans. Required for biosynthesis of glycoprotein hormones lutropin and thyrotropin, by mediating sulfation of their carbohydrate structures. Only active against terminal GalNAcbeta1,GalNAcbeta. Not active toward chondroitin. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Strongly expressed in brain. Weakly expressed in lung and kidney. Weakly expressed in pituitary. {ECO:0000269|PubMed:12944377}. +Q8BFS9 ASND1_MOUSE Asparagine synthetase domain-containing protein 1 627 69,753 Active site (1); Alternative sequence (1); Chain (1); Domain (2); Frameshift (2); Initiator methionine (1); Sequence conflict (4) +Q76EC5 CHST9_MOUSE Carbohydrate sulfotransferase 9 (EC 2.8.2.-) (GalNAc-4-O-sulfotransferase 2) (GalNAc-4-ST2) (GalNAc4ST-2) (N-acetylgalactosamine-4-O-sulfotransferase 2) 413 48,004 Chain (1); Glycosylation (5); Nucleotide binding (2); Topological domain (2); Transmembrane (1) TRANSMEM 6 26 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 5 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 27 413 Lumenal. {ECO:0000255}. FUNCTION: Catalyzes the transfer of sulfate to position 4 of non-reducing N-acetylgalactosamine (GalNAc) residues in both N-glycans and O-glycans. Participates in biosynthesis of glycoprotein hormones lutropin and thyrotropin, by mediating sulfation of their carbohydrate structures. Has a higher activity toward carbonic anhydrase VI than toward lutropin. Only active against terminal GalNAcbeta1,GalNAcbeta. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in kidney and pituitary gland. {ECO:0000269|PubMed:12944377}. +Q6PGK7 CHSTA_MOUSE Carbohydrate sulfotransferase 10 (EC 2.8.2.-) (HNK-1 sulfotransferase) (HNK-1ST) (HNK1ST) 356 42,055 Alternative sequence (3); Chain (1); Erroneous initiation (1); Glycosylation (3); Nucleotide binding (2); Sequence caution (1); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 7 27 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 28 356 Lumenal. {ECO:0000255}. FUNCTION: Catalyzes the transfer of sulfate to position 3 of terminal glucuronic acid of both protein- and lipid-linked oligosaccharides. Participates in biosynthesis of HNK-1 carbohydrate structure, a sulfated glucuronyl-lactosaminyl residue carried by many neural recognition molecules, which is involved in cell interactions during ontogenetic development and in synaptic plasticity in the adult. May be indirectly involved in synapse plasticity of the hippocampus, via its role in HNK-1 biosynthesis. {ECO:0000269|PubMed:12213450, ECO:0000269|PubMed:12358771}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. +Q99LL3 CHSTC_MOUSE Carbohydrate sulfotransferase 12 (EC 2.8.2.5) (Chondroitin 4-O-sulfotransferase 2) (Chondroitin 4-sulfotransferase 2) (C4ST-2) (C4ST2) 419 49,398 Chain (1); Glycosylation (4); Nucleotide binding (2); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 6 26 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 5 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 27 419 Lumenal. {ECO:0000255}. FUNCTION: Catalyzes the transfer of sulfate to position 4 of the N-acetylgalactosamine (GalNAc) residue of chondroitin and desulfated dermatan sulfate. Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage and is distributed on the surfaces of many cells and extracellular matrices. Activity toward partially desulfated dermatan sulfate is however lower. Does not form 4, 6-di-O-sulfated GalNAc when chondroitin sulfate C is used as an acceptor (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. +Q80V53 CHSTE_MOUSE Carbohydrate sulfotransferase 14 (EC 2.8.2.35) (Dermatan 4-sulfotransferase 1) (D4ST-1) 376 43,145 Chain (1); Glycosylation (2); Nucleotide binding (2); Sequence conflict (3); Topological domain (2); Transmembrane (1) TRANSMEM 40 60 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 39 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 61 376 Lumenal. {ECO:0000255}. FUNCTION: Catalyzes the transfer of sulfate to position 4 of the N-acetylgalactosamine (GalNAc) residue of dermatan sulfate. Plays a pivotal role in the formation of 4-0-sulfated IdoA blocks in dermatan sulfate. Transfers sulfate to the C-4 hydroxyl of beta1,4-linked GalNAc that is substituted with an alpha-linked iduronic acid (IdoUA) at the C-3 hydroxyl. Transfers sulfate more efficiently to GalNAc residues in -IdoUA-GalNAc-IdoUA- than in -GlcUA-GalNAc-GlcUA-sequences. Has preference for partially desulfated dermatan sulfate. Addition of sulfate to GalNAc may occur immediately after epimerization of GlcUA to IdoUA. Appears to have an important role in the formation of the cerebellar neural network during postnatal brain development. {ECO:0000269|PubMed:16702220}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. +Q8VBT9 ASPC1_MOUSE Tether containing UBX domain for GLUT4 (Alveolar soft part sarcoma chromosomal region candidate gene 1 protein homolog) 550 59,796 Alternative sequence (2); Beta strand (6); Chain (1); Domain (1); Helix (3); Initiator methionine (1); Modified residue (3); Region (1) FUNCTION: Enhances VCP methylation catalyzed by VCPKMT (By similarity). Tethering protein that sequesters GLUT4-containing vesicles in the cytoplasm in the absence of insulin. Modulates the amount of GLUT4 that is available at the cell surface. {ECO:0000250, ECO:0000269|PubMed:14562105}. SUBCELLULAR LOCATION: Endomembrane system {ECO:0000269|PubMed:14562105}; Peripheral membrane protein {ECO:0000269|PubMed:14562105}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q9BZE9}; Peripheral membrane protein. Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Interacts with VCP. Interacts with VCPKMT (By similarity). Interacts with GLUT4. {ECO:0000250, ECO:0000250|UniProtKB:Q9BZE9, ECO:0000269|PubMed:14562105}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:14562105}. +Q6DG52 CHUR_MOUSE Protein Churchill 112 12,858 Alternative sequence (2); Chain (1); Metal binding (12) FUNCTION: Transcriptional activator that mediates FGF signaling during neural development. Plays a role in the regulation of cell movement. Does not bind DNA by itself (By similarity). {ECO:0000250}. +Q8BSY0 ASPH_MOUSE Aspartyl/asparaginyl beta-hydroxylase (EC 1.14.11.16) (Aspartate beta-hydroxylase) (ASP beta-hydroxylase) (Peptide-aspartate beta-dioxygenase) 741 83,042 Alternative sequence (3); Binding site (3); Calcium binding (1); Chain (1); Compositional bias (3); Disulfide bond (1); Glycosylation (2); Metal binding (2); Modified residue (1); Region (1); Repeat (5); Sequence conflict (4); Topological domain (2); Transmembrane (1) TRANSMEM 63 83 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 62 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 84 741 Lumenal. {ECO:0000255}. FUNCTION: Isoform 1: specifically hydroxylates an Asp or Asn residue in certain epidermal growth factor-like (EGF) domains of a number of proteins. {ECO:0000269|PubMed:11773073}. SUBCELLULAR LOCATION: Isoform 1: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q28056}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q28056}.; SUBCELLULAR LOCATION: Isoform 2: Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:8530521}; Single-pass type II membrane protein {ECO:0000303|PubMed:8530521}. SUBUNIT: Monomer. Isoform 2 interacts with CASQ2. {ECO:0000250|UniProtKB:Q12797, ECO:0000250|UniProtKB:Q28056}. TISSUE SPECIFICITY: Isoform 1 is detected in heart, liver and ovary (at protein level). Detected in heart ventricle. Isoform 1 is widely expressed. Isoform 2 is detected in heart and skeletal muscle. {ECO:0000269|PubMed:10956665, ECO:0000269|PubMed:11773073, ECO:0000269|PubMed:8530521}. +Q8CJ27 ASPM_MOUSE Abnormal spindle-like microcephaly-associated protein homolog (Calmodulin-binding protein Sha1) (Calmodulin-binding protein 1) (Spindle and hydroxyurea checkpoint abnormal protein) 3122 364,218 Alternative sequence (1); Chain (1); Coiled coil (1); Domain (34); Erroneous initiation (1); Modified residue (4); Mutagenesis (3); Region (1); Sequence conflict (15) FUNCTION: Involved in mitotic spindle regulation and coordination of mitotic processes. The function in regulating microtubule dynamics at spindle poles including spindle orientation, astral microtubule density and poleward microtubule flux seem to depend on its association with the katanin complex formed by KATNA1 and KATNB1. Enhances the microtubule lattice severing activity of KATNA1 by recruiting the katanin complex to microtubules. Can block microtubule minus-end growth and reversely this function can be enhanced by the katanin complex (PubMed:28436967). May have a preferential role in regulating neurogenesis. {ECO:0000269|PubMed:12355089, ECO:0000269|PubMed:28436967, ECO:0000269|PubMed:9819352}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9819352}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:28436967}. Nucleus {ECO:0000269|PubMed:9819352}. Note=Localizes to spindle poles during mitosis. Associates with microtubule minus ends (PubMed:28436967). The nuclear-cytoplasmic distribution could be regulated by the availability of calmodulin. {ECO:0000269|PubMed:28436967}. SUBUNIT: Interacts with KATNA1 and KATNB1; katanin complex formation KATNA1:KATNB1 is required for the association. {ECO:0000269|PubMed:28436967}. TISSUE SPECIFICITY: Expressed in fetal brain, peripheral nervous system, liver and spleen. In the adult, expressed exclusively in testis, ovary and spleen. {ECO:0000269|PubMed:12351193, ECO:0000269|PubMed:12355089}. +Q99MQ4 ASPN_MOUSE Asporin (Periodontal ligament-associated protein 1) (PLAP-1) 373 42,573 Chain (1); Compositional bias (2); Disulfide bond (3); Domain (1); Erroneous termination (1); Glycosylation (2); Mutagenesis (3); Propeptide (1); Region (1); Repeat (11); Signal peptide (1) FUNCTION: Binds calcium and plays a role in osteoblast-driven collagen biomineralization activity (By similarity). Critical regulator of TGF-beta in articular cartilage and plays an essential role in cartilage homeostasis and osteoarthritis (OA) pathogenesis. Negatively regulates chondrogenesis in the articular cartilage by blocking the TGF-beta/receptor interaction on the cell surface and inhibiting the canonical TGF-beta/Smad signal. Negatively regulates periodontal ligament (PDL) differentiation and mineralization to ensure that the PDL is not ossified and to maintain homeostasis of the tooth-supporting system. Inhibits BMP2-induced cytodifferentiation of PDL cells by preventing its binding to BMPR1B/BMP type-1B receptor, resulting in inhibition of BMP-dependent activation of SMAD proteins. Inhibits the interaction between TGFB1 and TGF-beta receptor type II in the presence of heparin/heparan sulfate in vitro. {ECO:0000250, ECO:0000269|PubMed:17522060, ECO:0000269|PubMed:17827158, ECO:0000269|PubMed:18407830, ECO:0000269|PubMed:20052601}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. SUBUNIT: Interacts with type I collagen. DCN can inhibit collagen binding (By similarity). Interacts with TGFB1, TGFB2 and TGFB3. DCN, BGN, and FMOD inhibit binding to TGFB1. Interacts with BMP2. Interacts in vitro with type II collagen. {ECO:0000250, ECO:0000269|PubMed:17522060, ECO:0000269|PubMed:17827158, ECO:0000269|PubMed:20052601}. DOMAIN: The repeats LRR 9, LRR 10 and LRR 11 are involved in binding type I collagen. The poly-Asp region is involved in binding calcium (By similarity). The LRR 5 repeat can inhibit BMP2-induced cytodifferentiation and may be involved in the interaction with BMP2. {ECO:0000250, ECO:0000269|PubMed:18407830}. TISSUE SPECIFICITY: Higher expression in heart, also detected in kidney, stomach, testes, and skin but only weakly in lung, skeletal muscle, small intestine, and thymus. Expressed specifically and predominantly in the periodontal ligament (PDL). During tooth development, strong expression is seen in the dental follicle, which is the progenitor tissue that forms cementum, alveolar bone, and the PDL. Expressed in the perichondria of the maxilla, mandible, vertebrae, and long bones. Predominantly expressed in the perichondrium/periosteum of long bones (at protein level). {ECO:0000269|PubMed:17522060, ECO:0000269|PubMed:17804408}. +Q8VCE4 CI040_MOUSE Uncharacterized protein C9orf40 homolog 163 17,985 Chain (1); Modified residue (1); Sequence conflict (1) +P50289 ASPX_MOUSE Acrosomal protein SP-10 (Acrosomal vesicle protein 1) (MSA-63) 261 27,948 Chain (1); Sequence conflict (2); Signal peptide (1) PTM: The N-terminus is blocked. TISSUE SPECIFICITY: Testis. +Q9CQ90 CI085_MOUSE Uncharacterized protein C9orf85 homolog 155 17,730 Chain (1); Compositional bias (1); Initiator methionine (1); Modified residue (4) +Q7TMW6 CIAO3_MOUSE Cytosolic iron-sulfur assembly component 3 (Cytosolic Fe-S cluster assembly factor NARFL) (Iron-only hydrogenase-like protein 1) (IOP1) (Nuclear prelamin A recognition factor-like protein) 476 53,108 Alternative sequence (1); Chain (1); Initiator methionine (1); Metal binding (8); Modified residue (1); Sequence conflict (3) FUNCTION: Component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into extramitochondrial Fe/S proteins. Seems to negatively regulate the level of HIF1A expression, although this effect could be indirect (By similarity). {ECO:0000250|UniProtKB:Q9H6Q4}. SUBUNIT: External component of the CIA complex. In the CIA complex, interacts directly with CIAO1 and MMS19. {ECO:0000250|UniProtKB:Q9H6Q4}. +Q9Z0F4 CIB1_MOUSE Calcium and integrin-binding protein 1 (CIB) (Calmyrin) (DNA-PKcs-interacting protein) (Kinase-interacting protein) (KIP) 191 21,763 Calcium binding (2); Chain (1); Domain (2); Initiator methionine (1); Lipidation (1) FUNCTION: Calcium-binding protein that plays a role in the regulation of numerous cellular processes, such as cell differentiation, cell division, cell proliferation, cell migration, thrombosis, angiogenesis, cardiac hypertrophy and apoptosis. Involved in bone marrow megakaryocyte differentiation by negatively regulating thrombopoietin-mediated signaling pathway. Participates in the endomitotic cell cycle of megakaryocyte, a form of mitosis in which both karyokinesis and cytokinesis are interrupted. Plays a role in integrin signaling by negatively regulating alpha-IIb/beta3 activation in thrombin-stimulated megakaryocytes preventing platelet aggregation. Up-regulates PTK2/FAK1 activity, and is also needed for the recruitment of PTK2/FAK1 to focal adhesions; it thus appears to play an important role in focal adhesion formation. Positively regulates cell migration on fibronectin in a CDC42-dependent manner, the effect being negatively regulated by PAK1. Functions as a negative regulator of stress activated MAP kinase (MAPK) signaling pathways. Down-regulates inositol 1,4,5-trisphosphate receptor-dependent calcium signaling. Involved in sphingosine kinase SPHK1 translocation to the plasma membrane in a N-myristoylation-dependent manner preventing TNF-alpha-induced apoptosis. Regulates serine/threonine-protein kinase PLK3 activity for proper completion of cell division progression. Plays a role in microtubule (MT) dynamics during neuronal development; disrupts the MT depolymerization activity of STMN2 attenuating NGF-induced neurite outgrowth and the MT reorganization at the edge of lamellipodia. Promotes cardiomyocyte hypertrophy via activation of the calcineurin/NFAT signaling pathway. Stimulates calcineurin PPP3R1 activity by mediating its anchoring to the sarcolemma. In ischemia-induced (pathological or adaptive) angiogenesis, stimulates endothelial cell proliferation, migration and microvessel formation by activating the PAK1 and ERK1/ERK2 signaling pathway. Promotes also cancer cell survival and proliferation. May regulate cell cycle and differentiation of spermatogenic germ cells, and/or differentiation of supporting Sertoli cells. {ECO:0000269|PubMed:16982698, ECO:0000269|PubMed:17975111, ECO:0000269|PubMed:19691476, ECO:0000269|PubMed:20804551, ECO:0000269|PubMed:22128142}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Cell membrane. Cell membrane, sarcolemma. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cell projection, filopodium tip {ECO:0000250}. Apical cell membrane {ECO:0000250}. Cell projection, ruffle membrane {ECO:0000250}. Cell projection, growth cone {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Colocalized with NBR1 to the perinuclear region (By similarity). Colocalizes with TAS1R2 in apical regions of taste receptor cells. Colocalized with RAC3 in the perinuclear area and at the cell periphery. Colocalized with PAK1 within membrane ruffles during cell spreading upon readhesion to fibronectin. Redistributed to the cytoskeleton upon platelet aggregation. Translocates from the cytosol to the plasma membrane in a calcium-dependent manner. Colocalized with STMN2 in the cell body, neurites and growth cones of neurons. Colocalized with STMN2 to the leading edge of lamellipodia. Colocalizes with PLK3 at the centrosomes in ductal breast carcinoma cells (By similarity). Colocalized with PPP3R1 at the cell membrane of cardiomyocytes in the hypertrophic heart. {ECO:0000250}. SUBUNIT: Monomer. Interacts with the heterodimeric integrin alpha-IIb/beta3 (ITGA2B-ITGB3). Interacts with ITGA2B (via cytoplasmic domain); the interaction is direct and calcium-dependent. Interacts with the protein kinases PLK2/SNK and PRKDC (via the region immediately upstream of the kinase domain). Interacts with PLK3; the interaction inhibits PLK3 kinase activity. Interacts with PSEN2. Interacts (via C-terminus) with F8. Interacts with NBR1 (via C-terminus). Interacts with FEZ1 (via C-terminus). Interacts with UBR5 (via C-terminus); the interaction is sensitive to DNA damage, and may target CIB1 for ubiquitin-mediated degradation. Interacts with IFI6; the interaction is direct. Interacts with BCL2. Interacts with TAS1R2 (via C-terminus); the interaction is independent of the myristoylation state of CIB1. Interacts with ITPR3; the interaction occurs in a calcium dependent manner. Interacts with PTK2/FAK1. Interacts with MAP3K5; the interaction inhibits MAP3K5 activation by phosphorylation, and its subsequent interaction with TRAF2. Interacts (via C-terminal region) with STMN2 (via the N-terminal region); the interaction is direct, occurs in a calcium-dependent manner and attenuates the STMN2-induced neurite outgrowth inhibition. Interacts with SPHK1, the interaction occurs in a calcium-dependent manner. Interacts with ITGA2B (via C-terminal cytoplasmic tail); the interaction occurs upon platelet aggregation and is stabilized/increased in a calcium and magnesium-dependent manner. Interacts with PAK1 (via N-terminal region); the interaction is direct and occurs in a calcium-dependent manner. Interacts with RAC3 (via C-terminal region); the interaction induces their association with the cytoskeleton upon alpha-IIb/beta3 integrin-mediated adhesion. Interacts with ITGA5 and ITGAV (By similarity). Interacts with MYO1C. Interacts with ITGA2B (via C-terminal cytoplasmic tail region). Interacts (via C-terminal region) with PPP3R1 isoform 1 and isoform 2; the interactions increase upon cardiomyocytes hypertrophy. Interacts with CACNA1C; the interaction increases upon cardiomyocytes hypertrophy. {ECO:0000250, ECO:0000269|PubMed:17994197, ECO:0000269|PubMed:18989529, ECO:0000269|PubMed:20639889}. DOMAIN: The EF-hands may also bind magnesium ions in the presence of high Mg(2+) levels and low Ca(2+) levels. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in testis. Expressed in cardiac myocytes and endothelial cells. Expressed strongly in Sertoli cells, weakly in pachytene spermatocytes, round spermatids and condensing spermatids (at protein level). Ubiquitous. {ECO:0000269|PubMed:17975111, ECO:0000269|PubMed:18989529, ECO:0000269|PubMed:20639889}. +Q0P523 CIB3_MOUSE Calcium and integrin-binding family member 3 160 18,668 Calcium binding (2); Chain (1); Domain (3) SUBUNIT: Interacts with ITGA2B (via C-terminus cytoplasmic tail region); the interaction is stabilized/increased in a calcium and magnesium-dependent manner. {ECO:0000269|PubMed:18989529}. TISSUE SPECIFICITY: Expressed in megakaryocytes and endothelial cells. {ECO:0000269|PubMed:18989529}. +Q9D9N5 CIB4_MOUSE Calcium and integrin-binding family member 4 185 21,637 Calcium binding (2); Chain (1); Domain (3) SUBUNIT: Interacts with ITGA2B (via C-terminus cytoplasmic tail region); the interaction is stabilized/increased in a calcium- and magnesium-dependent manner. {ECO:0000250}. TISSUE SPECIFICITY: Expressed weakly in megakaryocytes and endothelial cells. {ECO:0000269|PubMed:18989529}. +P59242 CING_MOUSE Cingulin 1191 136,447 Alternative sequence (1); Chain (1); Coiled coil (1); Compositional bias (1); Erroneous initiation (3); Erroneous termination (1); Frameshift (1); Modified residue (19); Motif (1); Region (2); Sequence conflict (8) FUNCTION: Probably plays a role in the formation and regulation of the tight junction (TJ) paracellular permeability barrier. {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000269|PubMed:15292197}. Note=Localizes to the apical junction complex composed of tight and adherens junctions. SUBUNIT: Homodimer. Interacts with TJP1/ZO-1 (By similarity). {ECO:0000250}. DOMAIN: Deletion of the ZO-1 interaction motif (ZIM) decreases but does not abolish colocalization with ZO-1. {ECO:0000250}. TISSUE SPECIFICITY: Lung, kidney and intestine. {ECO:0000269|PubMed:15292197}. +D3Z3K2 CIP1_MOUSE E3 ubiquitin-protein ligase CCNB1IP1 (EC 2.3.2.27) (Cyclin-B1-interacting protein 1) (RING-type E3 ubiquitin transferase CCNB1IP1) 276 31,386 Chain (1); Coiled coil (1); Mutagenesis (1); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: Ubiquitin E3 ligase that acts as a limiting factor for crossing-over during meiosis: required during zygonema to limit the colocalization of RNF212 with MutS-gamma-associated recombination sites and thereby establish early differentiation of crossover and non-crossover sites. Later, it is directed by MutL-gamma to stably accumulate at designated crossover sites. Probably promotes the dissociation of RNF212 and MutS-gamma to allow the progression of recombination and the implementation of the final steps of crossing over. Modulates cyclin-B levels and participates in the regulation of cell cycle progression through the G2 phase. Overexpression causes delayed entry into mitosis. {ECO:0000269|PubMed:17784788, ECO:0000269|PubMed:24390283}. PTM: Ubiquitinated; autoubiquitinated. {ECO:0000250}.; PTM: Phosphorylated by CDK1 on serine or threonine residues (in vitro). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24390283}. Chromosome {ECO:0000269|PubMed:24390283}. Note=Associates to the synaptonemal complex. SUBUNIT: Interacts with CCNB1, UBE2L3 and NF2. {ECO:0000250}. TISSUE SPECIFICITY: Expressed predominantly in the testes and 17 day embryos (corresponding to prophase I in females). Weakly or not expressed in other tissues. {ECO:0000269|PubMed:17784788}. +Q8R0W1 CIPC_MOUSE CLOCK-interacting pacemaker (CLOCK-interacting circadian protein) 432 46,320 Alternative sequence (1); Beta strand (1); Chain (1); Coiled coil (1); Compositional bias (1); Erroneous initiation (1); Helix (3); Modified residue (1); Sequence conflict (6) FUNCTION: Transcriptional repressor which may act as a negative-feedback regulator of CLOCK-ARNTL/BMAL1 transcriptional activity in the circadian-clock mechanism. May stimulate ARNTL/BMAL1-dependent phosphorylation of CLOCK (PubMed:17310242, PubMed:19414601). However, the physiogical relevance of these observations is unsure, since experiments in knockout mice showed that CIPC is not critially required for basic circadian clock (PubMed:25862660). {ECO:0000269|PubMed:17310242, ECO:0000269|PubMed:19414601, ECO:0000269|PubMed:25862660}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17310242}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9C0C6}. Note=Predominantly localizes to the nucleus, where it co-localizes with CLOCK. At the G1/S boundary, partially translocated to the cytosol. {ECO:0000250|UniProtKB:Q9C0C6, ECO:0000269|PubMed:17310242}. SUBUNIT: Interacts with CLOCK. Forms a ternary complex with the CLOCK-ARNTL/BMAL1 heterodimer. Interacts with CAD AND HSPA5 (By similarity). {ECO:0000250|UniProtKB:Q9C0C6, ECO:0000269|PubMed:17310242}. TISSUE SPECIFICITY: Expressed in the heart, kidney and liver and shows a circadian oscillation in these tissues with a peak at circadian time 14 hours (at protein level). Expressed in the brain, including the suprachiasmatic nucleus (SCN) of the brain, and in multiple peripheral tissues such as heart, liver and kidney. Exhibits a circadian oscillation in the peripheral tissues with a peak at circadian time 14 hours. {ECO:0000269|PubMed:17310242}. +Q8BIR2 ASTE1_MOUSE Protein asteroid homolog 1 672 76,370 Alternative sequence (2); Chain (1); Erroneous initiation (1); Sequence conflict (3) FUNCTION: Possible role in EGF receptor signaling. {ECO:0000250}. +Q80Z10 ASTN2_MOUSE Astrotactin-2 1352 149,390 Alternative sequence (2); Chain (1); Disulfide bond (17); Domain (4); Erroneous initiation (1); Glycosylation (3); Signal peptide (1); Topological domain (3); Transmembrane (2) TRANSMEM 219 239 Helical. {ECO:0000255}.; TRANSMEM 448 468 Helical. {ECO:0000255}. TOPO_DOM 52 218 Lumenal. {ECO:0000305}.; TOPO_DOM 240 447 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 469 1352 Lumenal. {ECO:0000305|PubMed:20573900}. FUNCTION: Mediates recycling of the neuronal cell adhesion molecule ASTN1 to the anterior pole of the cell membrane in migrating neurons. Promotes ASTN1 internalization and intracellular transport of endocytosed ASTN1 (PubMed:20573900). Selectively binds inositol-4,5-bisphosphate, inositol-3,4,5-trisphosphate and inositol-1,3,4,5-tetrakisphosphate, suggesting it is recruited to membranes that contain lipids with a phosphoinositide headgroup (By similarity). {ECO:0000250|UniProtKB:O75129, ECO:0000269|PubMed:20573900}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:20573900}; Multi-pass membrane protein {ECO:0000305}. Perikaryon {ECO:0000269|PubMed:20573900}. Cytoplasm, cell cortex {ECO:0000269|PubMed:20573900}. Early endosome {ECO:0000269|PubMed:20573900}. Late endosome {ECO:0000269|PubMed:20573900}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000305|PubMed:20573900}. Cytoplasmic vesicle {ECO:0000269|PubMed:20573900}. Note=Integral membrane protein not detected at the cell membrane. Detected in cytoplasmic vesicles in the cell cortex, close to the anterior pole of migrating neurons. Detected at the base of the leading process in migrating neurons. {ECO:0000269|PubMed:20573900}. SUBUNIT: Interacts with ASTN1; the interaction is not calcium-dependent. {ECO:0000269|PubMed:20573900}. DOMAIN: The C-terminal region after the fibronectin type-III domain presents structural similarity to annexin domains and binds calcium ions. {ECO:0000250|UniProtKB:O75129}. TISSUE SPECIFICITY: Detected in cerebellum granule neurons; not detected in astroglia (at protein level). Detected primarily in cerebellum, and at lower levels in brain cortex, olfactory bulb, hindbrain and hippocampus dentate gyrus. Between 6 and 10 days after birth, when granule cell migration occurs in the cerebellum, detected in granule cell precursors in the external germinal layer, the molecular layer, the internal granule layer and in Purkinje neurons. Detected in postmitotic neurons in adult cerebellum. {ECO:0000269|PubMed:20573900}. +Q8VEF1 ASTRA_MOUSE Protein Aster-A (GRAM domain-containing protein 1A) 722 80,699 Alternative sequence (2); Beta strand (9); Chain (1); Domain (2); Erroneous initiation (7); Helix (4); Modified residue (4); Sequence caution (1); Sequence conflict (6); Transmembrane (1); Turn (1) TRANSMEM 609 629 Helical. {ECO:0000255}. FUNCTION: Cholesterol transporter that mediates non-vesicular transport of cholesterol from the plasma membrane (PM) to the endoplasmic reticulum (ER) (PubMed:30220461). Contains unique domains for binding cholesterol and the PM, thereby serving as a molecular bridge for the transfer of cholesterol from the PM to the ER (PubMed:30220461). Plays a crucial role in cholesterol homeostasis and has the unique ability to localize to the PM based on the level of membrane cholesterol (PubMed:30220461). In lipid-poor conditions localizes to the ER membrane and in response to excess cholesterol in the PM is recruited to the endoplasmic reticulum-plasma membrane contact sites (EPCS) which is mediated by the GRAM domain (PubMed:30220461). At the EPCS, the sterol-binding VASt/ASTER domain binds to the cholesterol in the PM and facilitates its transfer from the PM to ER (PubMed:30220461). May play a role in tumor progression (PubMed:27585821). {ECO:0000269|PubMed:27585821, ECO:0000269|PubMed:30220461}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:30220461}; Single-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:30220461}; Single-pass membrane protein {ECO:0000255}. Note=In lipid-poor conditions localizes to the ER membrane and in response to excess cholesterol in the PM is recruited to the endoplasmic reticulum-plasma membrane contact sites (EPCS) (PubMed:30220461). Localizes to distinct EPCS than GRAMD2A and ESYT2/3 (By similarity). {ECO:0000250|UniProtKB:Q96CP6, ECO:0000269|PubMed:30220461}. DOMAIN: GRAM domain binds phosphatidylserine in the PM and mediates protein recruitment to endoplasmic reticulum-plasma membrane contact sites (EPCS) in response to excess cholesterol in the PM. {ECO:0000269|PubMed:30220461}.; DOMAIN: VASt (VAD1 Analog of StAR-related lipid transfer) domain, also known as ASTER (Greek for star) domain is a sterol-binding domain. {ECO:0000269|PubMed:30220461}. TISSUE SPECIFICITY: Highly expressed in the brain. {ECO:0000269|PubMed:30220461}. +Q80TI0 ASTRB_MOUSE Protein Aster-B (GRAM domain-containing protein 1B) 738 85,355 Alternative sequence (4); Chain (1); Domain (2); Erroneous initiation (1); Modified residue (9); Transmembrane (1) TRANSMEM 623 643 Helical. {ECO:0000255}. FUNCTION: Cholesterol transporter that mediates non-vesicular transport of cholesterol from the plasma membrane (PM) to the endoplasmic reticulum (ER) (PubMed:30220461). Contains unique domains for binding cholesterol and the PM, thereby serving as a molecular bridge for the transfer of cholesterol from the PM to the ER (PubMed:30220461). Plays a crucial role in cholesterol homeostasis in the adrenal gland and has the unique ability to localize to the PM based on the level of membrane cholesterol (PubMed:30220461). In lipid-poor conditions localizes to the ER membrane and in response to excess cholesterol in the PM is recruited to the endoplasmic reticulum-plasma membrane contact sites (EPCS) which is mediated by the GRAM domain (PubMed:30220461). At the EPCS, the sterol-binding VASt/ASTER domain binds to the cholesterol in the PM and facilitates its transfer from the PM to ER (PubMed:30220461). {ECO:0000269|PubMed:30220461}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:30220461}; Single-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:30220461}; Single-pass membrane protein {ECO:0000255}. Note=In lipid-poor conditions localizes to the ER membrane and in response to excess cholesterol in the PM is recruited to the endoplasmic reticulum-plasma membrane contact sites (EPCS). {ECO:0000269|PubMed:30220461}. DOMAIN: GRAM domain binds phosphatidylserine in the PM and mediates protein recruitment to endoplasmic reticulum-plasma membrane contact sites (EPCS) in response to excess cholesterol in the PM. {ECO:0000269|PubMed:30220461}.; DOMAIN: VASt (VAD1 Analog of StAR-related lipid transfer) domain, also known as ASTER (Greek for star) domain is a sterol-binding domain. {ECO:0000269|PubMed:30220461}. TISSUE SPECIFICITY: Highly expressed in the adrenal gland (at protein level) and brain. Also found in the kidney, testis and macrophages. {ECO:0000269|PubMed:30220461}. +Q8CI52 ASTRC_MOUSE Protein Aster-C (GRAM domain-containing protein 1C) 662 76,009 Chain (1); Domain (2); Erroneous initiation (2); Transmembrane (1) TRANSMEM 557 577 Helical. {ECO:0000255}. FUNCTION: Cholesterol transporter that mediates non-vesicular transport of cholesterol from the plasma membrane (PM) to the endoplasmic reticulum (ER) (PubMed:30220461). Contains unique domains for binding cholesterol and the PM, thereby serving as a molecular bridge for the transfer of cholesterol from the PM to the ER (PubMed:30220461). Plays a crucial role in cholesterol homeostasis and has the unique ability to localize to the PM based on the level of membrane cholesterol (PubMed:30220461). In lipid-poor conditions localizes to the ER membrane and in response to excess cholesterol in the PM is recruited to the endoplasmic reticulum-plasma membrane contact sites (EPCS) which is mediated by the GRAM domain (PubMed:30220461). At the EPCS, the sterol-binding VASt/ASTER domain binds to the cholesterol in the PM and facilitates its transfer from the PM to ER (PubMed:30220461). {ECO:0000269|PubMed:30220461}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:30220461}; Single-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:30220461}; Single-pass membrane protein {ECO:0000255}. Note=In lipid-poor conditions localizes to the ER membrane and in response to excess cholesterol in the PM is recruited to the endoplasmic reticulum-plasma membrane contact sites (EPCS). {ECO:0000269|PubMed:30220461}. DOMAIN: GRAM domain binds phosphatidylserine in the PM and mediates protein recruitment to endoplasmic reticulum-plasma membrane contact sites (EPCS) in response to excess cholesterol in the PM. {ECO:0000269|PubMed:30220461}.; DOMAIN: VASt (VAD1 Analog of StAR-related lipid transfer) domain, also known as ASTER (Greek for star) domain is a sterol-binding domain. {ECO:0000269|PubMed:30220461}. TISSUE SPECIFICITY: Highly expressed in the liver. Also found in the testis. {ECO:0000269|PubMed:30220461}. +Q61137 ASTN1_MOUSE Astrotactin-1 (Neuronal migration protein GC14) 1302 144,884 Alternative sequence (1); Chain (1); Disulfide bond (17); Domain (4); Frameshift (1); Glycosylation (6); Modified residue (2); Sequence conflict (10); Signal peptide (1); Topological domain (3); Transmembrane (2) TRANSMEM 154 174 Helical. {ECO:0000255}.; TRANSMEM 389 409 Helical. {ECO:0000255}. TOPO_DOM 22 153 Extracellular. {ECO:0000305}.; TOPO_DOM 175 388 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 410 1302 Extracellular. {ECO:0000269|PubMed:20573900, ECO:0000305}. FUNCTION: Neuronal adhesion molecule that is required for normal migration of young postmitotic neuroblasts along glial fibers, especially in the cerebellum. Required for normal rate of migration of granule cells during brain development and for normal cerebellum development. {ECO:0000269|PubMed:11861479, ECO:0000269|PubMed:8602532}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20573900, ECO:0000269|PubMed:8602532}; Multi-pass membrane protein {ECO:0000305}. Perikaryon {ECO:0000269|PubMed:20573900}. Endosome {ECO:0000269|PubMed:20573900}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000305|PubMed:20573900}. Note=Detected close to the anterior pole and at the base of the leading process in migrating neurons. Is internalized from the membrane via clathrin-coated vesicles and endosomes, and recycled to the anterior pole of the migrating cell. {ECO:0000269|PubMed:20573900}. SUBUNIT: Interacts with ASTN2; the interaction is not calcium-dependent. {ECO:0000269|PubMed:20573900}. TISSUE SPECIFICITY: Detected in brain (at protein level) (PubMed:11861479). Expressed specifically in the brain. Expressed in the cerebellum, hippocampus, cerebrum and olfactory bulb (PubMed:8602532). {ECO:0000269|PubMed:11861479, ECO:0000269|PubMed:8602532}. +P59598 ASXL1_MOUSE Putative Polycomb group protein ASXL1 (Additional sex combs-like protein 1) 1514 162,674 Chain (1); Compositional bias (4); Erroneous initiation (1); Modified residue (2); Motif (3); Region (2); Zinc finger (1) FUNCTION: Probable Polycomb group (PcG) protein involved in transcriptional regulation mediated by ligand-bound retinoic acid receptors (RARs) and peroxisome proliferator-activated receptor gamma (PPARG). Acts as a coactivator of RARA and RXRA through association with NCOA1. Acts as a corepressor for PPARG and suppresses its adipocyte differentiation-inducing activity. Non-catalytic component of the PR-DUB complex, a complex that specifically mediates deubiquitination of histone H2A monoubiquitinated at 'Lys-119' (H2AK119ub1). {ECO:0000269|PubMed:16606617, ECO:0000269|PubMed:21047783}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Component of the PR-DUB complex, at least composed of BAP1 and ASXL1 (By similarity). Interacts with RARA, RXRA (PubMed:16606617). Interacts with NCOA1 (By similarity). Interacts with PPARA and PPARG (PubMed:21047783). {ECO:0000250|UniProtKB:Q8IXJ9, ECO:0000269|PubMed:16606617, ECO:0000269|PubMed:21047783}. DOMAIN: Contains two Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs, which may be required for an association with nuclear receptors. {ECO:0000250}. +Q8K2X1 AT10D_MOUSE Probable phospholipid-transporting ATPase VD (EC 7.6.2.1) (ATPase class V type 10D) (P4-ATPase flippase complex alpha subunit ATP10D) 1416 158,330 Active site (1); Alternative sequence (1); Chain (1); Frameshift (1); Metal binding (2); Natural variant (2); Nucleotide binding (2); Sequence conflict (1); Topological domain (11); Transmembrane (10) TRANSMEM 98 118 Helical. {ECO:0000255}.; TRANSMEM 121 141 Helical. {ECO:0000255}.; TRANSMEM 322 342 Helical. {ECO:0000255}.; TRANSMEM 366 386 Helical. {ECO:0000255}.; TRANSMEM 1111 1131 Helical. {ECO:0000255}.; TRANSMEM 1143 1163 Helical. {ECO:0000255}.; TRANSMEM 1193 1213 Helical. {ECO:0000255}.; TRANSMEM 1222 1242 Helical. {ECO:0000255}.; TRANSMEM 1253 1273 Helical. {ECO:0000255}.; TRANSMEM 1290 1310 Helical. {ECO:0000255}. TOPO_DOM 1 97 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 119 120 Exoplasmic loop. {ECO:0000255}.; TOPO_DOM 142 321 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 343 365 Exoplasmic loop. {ECO:0000255}.; TOPO_DOM 387 1110 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1132 1142 Exoplasmic loop. {ECO:0000255}.; TOPO_DOM 1164 1192 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1214 1221 Exoplasmic loop. {ECO:0000255}.; TOPO_DOM 1243 1252 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1274 1289 Exoplasmic loop. {ECO:0000255}.; TOPO_DOM 1311 1416 Cytoplasmic. {ECO:0000255}. FUNCTION: Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}. Note=Exit from the endoplasmic reticulum requires the presence of TMEM30A. {ECO:0000250}. SUBUNIT: Component of a P4-ATPase flippase complex which consists of a catalytic alpha subunit and an accessory beta subunit. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in placenta and kidney. {ECO:0000269|PubMed:12532265}. +Q8C4A5 ASXL3_MOUSE Putative Polycomb group protein ASXL3 (Additional sex combs-like protein 3) 2259 243,673 Alternative sequence (1); Chain (1); Compositional bias (3); Zinc finger (1) FUNCTION: Putative Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. PcG proteins are not required to initiate repression, but to maintain it during later stages of development. They probably act via methylation of histones, rendering chromatin heritably changed in its expressibility (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q9Z1W8 AT12A_MOUSE Potassium-transporting ATPase alpha chain 2 (EC 3.6.3.10) (Non-gastric H(+)/K(+) ATPase subunit alpha) (Proton pump) 1035 114,727 Active site (1); Chain (1); Metal binding (2); Modified residue (1); Sequence conflict (3); Topological domain (11); Transmembrane (10) TRANSMEM 100 120 Helical. {ECO:0000255}.; TRANSMEM 143 163 Helical. {ECO:0000255}.; TRANSMEM 300 319 Helical. {ECO:0000255}.; TRANSMEM 332 349 Helical. {ECO:0000255}.; TRANSMEM 784 803 Helical. {ECO:0000255}.; TRANSMEM 814 834 Helical. {ECO:0000255}.; TRANSMEM 855 877 Helical. {ECO:0000255}.; TRANSMEM 930 949 Helical. {ECO:0000255}.; TRANSMEM 964 982 Helical. {ECO:0000255}.; TRANSMEM 998 1018 Helical. {ECO:0000255}. TOPO_DOM 1 99 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 121 142 Lumenal. {ECO:0000255}.; TOPO_DOM 164 299 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 320 331 Lumenal. {ECO:0000255}.; TOPO_DOM 350 783 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 804 813 Lumenal. {ECO:0000255}.; TOPO_DOM 835 854 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 878 929 Lumenal. {ECO:0000255}.; TOPO_DOM 950 963 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 983 997 Lumenal. {ECO:0000255}.; TOPO_DOM 1019 1035 Cytoplasmic. {ECO:0000255}. FUNCTION: Catalyzes the hydrolysis of ATP coupled with the exchange of H(+) and K(+) ions across the plasma membrane. Responsible for potassium absorption in various tissues. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SUBUNIT: Composed of two subunits: alpha (catalytic) and beta. TISSUE SPECIFICITY: Found in skin, kidney and distal colon. {ECO:0000269|PubMed:9872395}. +Q99ME6 AT1B4_MOUSE Protein ATP1B4 (X,K-ATPase subunit beta-m) (X/potassium-transporting ATPase subunit beta-m) 356 41,401 Alternative sequence (1); Chain (1); Compositional bias (1); Topological domain (2); Transmembrane (1) TRANSMEM 110 130 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 109 Nuclear. {ECO:0000255}.; TOPO_DOM 131 356 Perinuclear space. {ECO:0000255}. FUNCTION: May act as a transcriptional coregulator during muscle development through its interaction with SNW1. Has lost its ancestral function as a Na,K-ATPase beta-subunit (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Detected in nuclear envelops. {ECO:0000250}. SUBUNIT: Associates with a SMAD7-transcriptional complex. Interacts with TOR1AIP1. Does not associate with known Na,K-ATPase alpha-subunits (By similarity). Interacts with SNW1. {ECO:0000250, ECO:0000269|PubMed:17592128}. TISSUE SPECIFICITY: Expressed in skeletal muscle (at protein level). Expressed during postnatal development in skeletal muscle and heart. {ECO:0000269|PubMed:14656723}. +Q8VDN2 AT1A1_MOUSE Sodium/potassium-transporting ATPase subunit alpha-1 (Na(+)/K(+) ATPase alpha-1 subunit) (EC 3.6.3.9) (Sodium pump subunit alpha-1) 1023 112,982 Active site (1); Binding site (1); Chain (1); Metal binding (2); Modified residue (15); Propeptide (1); Region (1); Topological domain (10); Transmembrane (9) TRANSMEM 97 117 Helical. {ECO:0000255}.; TRANSMEM 130 150 Helical. {ECO:0000255}.; TRANSMEM 292 312 Helical. {ECO:0000255}.; TRANSMEM 320 340 Helical. {ECO:0000255}.; TRANSMEM 790 810 Helical. {ECO:0000255}.; TRANSMEM 866 886 Helical. {ECO:0000255}.; TRANSMEM 916 936 Helical. {ECO:0000255}.; TRANSMEM 953 973 Helical. {ECO:0000255}.; TRANSMEM 980 1000 Helical. {ECO:0000255}. TOPO_DOM 6 96 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 118 129 Extracellular. {ECO:0000255}.; TOPO_DOM 151 291 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 313 319 Extracellular. {ECO:0000255}.; TOPO_DOM 341 789 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 811 865 Extracellular. {ECO:0000255}.; TOPO_DOM 887 915 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 937 952 Extracellular. {ECO:0000255}.; TOPO_DOM 974 979 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1001 1023 Extracellular. {ECO:0000255}. FUNCTION: This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients. {ECO:0000250|UniProtKB:P05023}. PTM: Phosphorylation on Tyr-10 modulates pumping activity. Phosphorylation of Ser-943 by PKA modulates the response of ATP1A1 to PKC. Dephosphorylation by protein phosphatase 2A (PP2A) following increases in intracellular sodium, leading to increase catalytic activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P05023}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: The sodium/potassium-transporting ATPase is composed of a catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an additional regulatory subunit. Interacts with regulatory subunit FXYD1 (PubMed:17283221). Interacts with regulatory subunit FXYD3 (PubMed:15743908). Interacts with SIK1 (By similarity). Interacts with SLC35G1 and STIM1 (By similarity). {ECO:0000250|UniProtKB:P05023, ECO:0000250|UniProtKB:P06685, ECO:0000269|PubMed:15743908, ECO:0000269|PubMed:17283221}. +P14231 AT1B2_MOUSE Sodium/potassium-transporting ATPase subunit beta-2 (Adhesion molecule in glia) (AMOG) (Sodium/potassium-dependent ATPase subunit beta-2) 290 33,344 Chain (1); Disulfide bond (3); Glycosylation (7); Region (1); Topological domain (2); Transmembrane (1) TRANSMEM 40 67 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 39 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 68 290 Extracellular. {ECO:0000255}. FUNCTION: This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The exact function of the beta-2 subunit is not known.; FUNCTION: Mediates cell adhesion of neurons and astrocytes, and promotes neurite outgrowth. SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein. SUBUNIT: The sodium/potassium-transporting ATPase is composed of a catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an additional regulatory subunit. {ECO:0000305}. DOMAIN: The C-terminal lobe folds into an immunoglobulin-like domain and mediates cell adhesion properties. {ECO:0000250}. +Q8R429 AT2A1_MOUSE Sarcoplasmic/endoplasmic reticulum calcium ATPase 1 (SERCA1) (SR Ca(2+)-ATPase 1) (EC 3.6.3.8) (Calcium pump 1) (Calcium-transporting ATPase sarcoplasmic reticulum type, fast twitch skeletal muscle isoform) (Endoplasmic reticulum class 1/2 Ca(2+) ATPase) 994 109,425 Active site (1); Chain (1); Disulfide bond (1); Metal binding (13); Modified residue (4); Mutagenesis (3); Region (2); Topological domain (11); Transmembrane (10) TRANSMEM 49 69 Helical; Name=1. {ECO:0000250}.; TRANSMEM 90 110 Helical; Name=2. {ECO:0000250}.; TRANSMEM 254 273 Helical; Name=3. {ECO:0000250}.; TRANSMEM 296 313 Helical; Name=4. {ECO:0000250}.; TRANSMEM 758 777 Helical; Name=5. {ECO:0000250}.; TRANSMEM 788 808 Helical; Name=6. {ECO:0000250}.; TRANSMEM 829 851 Helical; Name=7. {ECO:0000250}.; TRANSMEM 898 917 Helical; Name=8. {ECO:0000250}.; TRANSMEM 931 949 Helical; Name=9. {ECO:0000250}.; TRANSMEM 965 985 Helical; Name=10. {ECO:0000250}. TOPO_DOM 1 48 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 70 89 Lumenal. {ECO:0000250}.; TOPO_DOM 111 253 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 274 295 Lumenal. {ECO:0000250}.; TOPO_DOM 314 757 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 778 787 Lumenal. {ECO:0000250}.; TOPO_DOM 809 828 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 852 897 Lumenal. {ECO:0000250}.; TOPO_DOM 918 930 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 950 964 Lumenal. {ECO:0000250}.; TOPO_DOM 986 994 Cytoplasmic. {ECO:0000250}. FUNCTION: Key regulator of striated muscle performance by acting as the major Ca(2+) ATPase responsible for the reuptake of cytosolic Ca(2+) into the sarcoplasmic reticulum (PubMed:21697544, PubMed:22961106, PubMed:25640239, PubMed:26816378). Catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Contributes to calcium sequestration involved in muscular excitation/contraction (PubMed:21697544, PubMed:22961106, PubMed:25640239, PubMed:26816378). {ECO:0000269|PubMed:21697544, ECO:0000269|PubMed:22961106, ECO:0000269|PubMed:25640239, ECO:0000269|PubMed:26816378}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P04191}; Multi-pass membrane protein {ECO:0000255}. Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:26816378}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Interacts with sarcolipin (SLN) (PubMed:21697544, PubMed:22961106). Interacts with phospholamban (PLN) (PubMed:26816378). Interacts with myoregulin (MRLN) (PubMed:25640239). Interacts with DWORF (PubMed:26816378). {ECO:0000269|PubMed:21697544, ECO:0000269|PubMed:22961106, ECO:0000269|PubMed:25640239, ECO:0000269|PubMed:26816378}. +Q80XR2 AT2C1_MOUSE Calcium-transporting ATPase type 2C member 1 (ATPase 2C1) (EC 3.6.3.8) (ATP-dependent Ca(2+) pump PMR1) 918 100,299 Active site (1); Chain (1); Metal binding (2); Sequence conflict (7); Topological domain (11); Transmembrane (10) TRANSMEM 79 95 Helical. {ECO:0000255}.; TRANSMEM 100 121 Helical. {ECO:0000255}.; TRANSMEM 263 282 Helical. {ECO:0000255}.; TRANSMEM 295 316 Helical. {ECO:0000255}.; TRANSMEM 700 722 Helical. {ECO:0000255}.; TRANSMEM 728 751 Helical. {ECO:0000255}.; TRANSMEM 776 794 Helical. {ECO:0000255}.; TRANSMEM 802 827 Helical. {ECO:0000255}.; TRANSMEM 843 862 Helical. {ECO:0000255}.; TRANSMEM 876 892 Helical. {ECO:0000255}. TOPO_DOM 1 78 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 96 99 Extracellular. {ECO:0000255}.; TOPO_DOM 122 262 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 283 294 Extracellular. {ECO:0000255}.; TOPO_DOM 317 699 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 723 727 Extracellular. {ECO:0000255}.; TOPO_DOM 752 775 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 795 801 Extracellular. {ECO:0000255}.; TOPO_DOM 828 842 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 863 875 Extracellular. {ECO:0000255}.; TOPO_DOM 893 918 Cytoplasmic. {ECO:0000255}. FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of the calcium. {ECO:0000250, ECO:0000269|PubMed:14747290}. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +A2AWT3 AT7L3_MOUSE Ataxin-7-like protein 3 (SAGA-associated factor 11 homolog) 347 38,594 Alternative sequence (1); Chain (1); Domain (1); Erroneous gene model prediction (1); Modified residue (5); Zinc finger (1) FUNCTION: Component of the transcription regulatory histone acetylation (HAT) complex SAGA, a multiprotein complex that activates transcription by remodeling chromatin and mediating histone acetylation and deubiquitination. Within the SAGA complex, participates in a subcomplex that specifically deubiquitinates both histones H2A and H2B. The SAGA complex is recruited to specific gene promoters by activators such as MYC, where it is required for transcription. Required for nuclear receptor-mediated transactivation. Within the complex, it is required to recruit USP22 and ENY2 into the SAGA complex. Regulates H2B monoubiquitination (H2Bub1) levels. Affects subcellular distribution of ENY2, USP22 and ATXN7L3B. {ECO:0000255|HAMAP-Rule:MF_03047}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03047}. SUBUNIT: Component of some SAGA transcription coactivator-HAT complexes, at least composed of ATXN7, ATXN7L3, ENY2, GCN5L2, SUPT3H, TAF10, TRRAP and USP22. Within the SAGA complex, ENY2, ATXN7, ATXN7L3, and USP22 form an additional subcomplex of SAGA called the DUB module (deubiquitination module). Interacts directly with ENY2 and USP22. {ECO:0000255|HAMAP-Rule:MF_03047}. DOMAIN: The long N-terminal helix forms part of the 'assembly lobe' of the SAGA deubiquitination module. {ECO:0000255|HAMAP-Rule:MF_03047}.; DOMAIN: The C-terminal SGF11-type zinc-finger domain together with the C-terminal catalytic domain of USP22 forms the 'catalytic lobe' of the SAGA deubiquitination module. {ECO:0000255|HAMAP-Rule:MF_03047}. +P70704 AT8A1_MOUSE Phospholipid-transporting ATPase IA (EC 7.6.2.1) (ATPase class I type 8A member 1) (Chromaffin granule ATPase II) (P4-ATPase flippase complex alpha subunit ATP8A1) 1164 131,413 Active site (1); Alternative sequence (2); Chain (1); Metal binding (2); Modified residue (5); Mutagenesis (1); Nucleotide binding (2); Topological domain (11); Transmembrane (10) TRANSMEM 76 96 Helical. {ECO:0000255}.; TRANSMEM 101 121 Helical. {ECO:0000255}.; TRANSMEM 298 318 Helical. {ECO:0000255}.; TRANSMEM 340 360 Helical. {ECO:0000255}.; TRANSMEM 867 887 Helical. {ECO:0000255}.; TRANSMEM 891 911 Helical. {ECO:0000255}.; TRANSMEM 940 960 Helical. {ECO:0000255}.; TRANSMEM 978 998 Helical. {ECO:0000255}.; TRANSMEM 1009 1029 Helical. {ECO:0000255}.; TRANSMEM 1045 1065 Helical. {ECO:0000255}. TOPO_DOM 1 75 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 97 100 Exoplasmic loop. {ECO:0000255}.; TOPO_DOM 122 297 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 319 339 Exoplasmic loop. {ECO:0000255}.; TOPO_DOM 361 866 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 888 890 Exoplasmic loop. {ECO:0000255}.; TOPO_DOM 912 939 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 961 977 Exoplasmic loop. {ECO:0000255}.; TOPO_DOM 999 1008 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1030 1044 Exoplasmic loop. {ECO:0000255}.; TOPO_DOM 1066 1164 Cytoplasmic. {ECO:0000255}. FUNCTION: Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. In vitro, its ATPase activity is selectively and stereospecifically stimulated by phosphatidylserine (PS). The flippase complex ATP8A1:TMEM30A seems to play a role in regulation of cell migration probably involving flippase-mediated translocation of phosphatidylethanolamine (PE) at the plasma membrane. Acts as aminophospholipid translocase at the plasma membrane in neuronal cells; the activity is associated with hippocampus-dependent learning. {ECO:0000269|PubMed:16618126, ECO:0000269|PubMed:20224745, ECO:0000269|PubMed:22007859, ECO:0000269|PubMed:23269685}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, chromaffin granule membrane {ECO:0000269|PubMed:16643453}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic granule {ECO:0000269|PubMed:16643453}. Cell membrane {ECO:0000250|UniProtKB:Q9Y2Q0}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9Y2Q0}. Golgi apparatus {ECO:0000250|UniProtKB:Q9Y2Q0}. Note=Exit from the endoplasmic reticulum requires the presence of TMEM30A, but not TMEM30B. In the presence of TMEM30A, predominantly located in cytoplasmic punctate structures (By similarity). Localizes to plasma membranes of red blood cells (PubMed:16643453). {ECO:0000250, ECO:0000269|PubMed:16643453}. SUBUNIT: Component of a P4-ATPase flippase complex which consists of a catalytic alpha subunit and an accessory beta subunit. Interacts with TMEM30A to form a flippase complex. {ECO:0000269|PubMed:23269685}. TISSUE SPECIFICITY: Found in most tissues except liver and testis. Most abundant in brain and lung. Also detected in fetal tissues. Isoform 1 is expressed in brain. Isoform 2 and isoform 3 are expressed in reticulocytes. {ECO:0000269|PubMed:16643453}. +P98200 AT8A2_MOUSE Phospholipid-transporting ATPase IB (EC 7.6.2.1) (ATPase class I type 8A member 2) (P4-ATPase flippase complex alpha subunit ATP8A2) 1148 129,417 Active site (1); Chain (1); Metal binding (2); Modified residue (1); Mutagenesis (1); Natural variant (1); Topological domain (11); Transmembrane (10) TRANSMEM 45 66 Helical. {ECO:0000255}.; TRANSMEM 72 94 Helical. {ECO:0000255}.; TRANSMEM 277 298 Helical. {ECO:0000255}.; TRANSMEM 324 345 Helical. {ECO:0000255}.; TRANSMEM 838 858 Helical. {ECO:0000255}.; TRANSMEM 871 890 Helical. {ECO:0000255}.; TRANSMEM 921 942 Helical. {ECO:0000255}.; TRANSMEM 957 979 Helical. {ECO:0000255}.; TRANSMEM 986 1006 Helical. {ECO:0000255}.; TRANSMEM 1025 1049 Helical. {ECO:0000255}. TOPO_DOM 1 44 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 67 71 Exoplasmic loop. {ECO:0000255}.; TOPO_DOM 95 276 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 299 323 Exoplasmic loop. {ECO:0000255}.; TOPO_DOM 346 837 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 859 870 Exoplasmic loop. {ECO:0000255}.; TOPO_DOM 891 920 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 943 956 Exoplasmic loop. {ECO:0000255}.; TOPO_DOM 980 985 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1007 1024 Exoplasmic loop. {ECO:0000255}.; TOPO_DOM 1050 1148 Cytoplasmic. {ECO:0000255}. FUNCTION: Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. Reconstituted to liposomes, the ATP8A2:TMEM30A flippase complex predomiminantly transports phosphatidylserine (PS) and to a lesser extent phosphatidylethanolamine (PE). ATP8A2:TMEM30A may be involved in regulation of neurite outgrowth. Proposed to function in the generation and maintenance of phospholipid asymmetry in photoreceptor disk membranes and neuronal axon membranes. May be involved in vesicle trafficking in neuronal cells. Required for normal visual and auditory function; involved in photoreceptor and inner ear spiral ganglion cell survival. {ECO:0000269|PubMed:22641037, ECO:0000269|PubMed:22912588, ECO:0000269|PubMed:24413176}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Golgi apparatus {ECO:0000269|PubMed:24413176}. Endosome {ECO:0000269|PubMed:24413176}. Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:24413176}. Cell membrane {ECO:0000269|PubMed:24413176}. Note=Localizes to the Golgi and endosomes in photoreceptor cells. Localizes to disk membranes of rod photoreceptor outer segments (ROS). SUBUNIT: Component of a P4-ATPase flippase complex which consists of a catalytic alpha subunit and an accessory beta subunit. Interacts with TMEM30A to form a flippase complex (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Found in testis, heart and brain. Most abundant in testis. Also detected in fetal tissues. Expressed in retinal photoreceptor cells; detected in retina outer nuclear layer and inner segment (at protein level). {ECO:0000269|PubMed:19778899, ECO:0000269|PubMed:22912588}. DISEASE: Note=Defects in Atp8a2 are the cause of Wabbler-lethal (wl) phenotype. Homozygotes show severe neurological annormalities that include ataxia and body tremors linked to progressive axonal degeneration in several areas of the nervous system. {ECO:0000269|PubMed:22912588}. +O35451 ATF6B_MOUSE Cyclic AMP-dependent transcription factor ATF-6 beta (cAMP-dependent transcription factor ATF-6 beta) (Activating transcription factor 6 beta) (ATF6-beta) (cAMP response element-binding protein-related protein) (Creb-rp) (cAMP-responsive element-binding protein-like 1) [Cleaved into: Processed cyclic AMP-dependent transcription factor ATF-6 beta] 699 76,007 Chain (2); Compositional bias (1); Domain (1); Glycosylation (5); Initiator methionine (1); Modified residue (1); Region (2); Site (3); Topological domain (2); Transmembrane (1) TRANSMEM 394 414 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 2 393 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 415 699 Lumenal. {ECO:0000255}. FUNCTION: Transcriptional factor that acts in the unfolded protein response (UPR) pathway by activating UPR target genes induced during ER stress. Binds DNA on the 5'-CCAC[GA]-3' half of the ER stress response element (ERSE) (5'-CCAATN(9)CCAC[GA]-3') when NF-Y is bound to ERSE (By similarity). {ECO:0000250}. PTM: During unfolded protein response, a fragment of approximately 60 kDa containing the cytoplasmic transcription factor domain is released by proteolysis. The cleavage is probably performed sequentially by site-1 and site-2 protease (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: Processed cyclic AMP-dependent transcription factor ATF-6 beta: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}. Note=Under ER stress the cleaved N-terminal cytoplasmic domain translocates into the nucleus. {ECO:0000250}. SUBUNIT: Homodimer and heterodimer with ATF6-alpha. The dimer interacts with the nuclear transcription factor Y (NF-Y) trimer through direct binding to NF-Y subunit C (NF-YC) (By similarity). {ECO:0000250}. +P81269 ATF1_MOUSE Cyclic AMP-dependent transcription factor ATF-1 (cAMP-dependent transcription factor ATF-1) (Activating transcription factor 1) (TCR-ATF1) 269 29,238 Chain (1); Cross-link (1); Domain (2); Modified residue (2); Region (2) FUNCTION: Binds the cAMP response element (CRE) (consensus: 5'-GTGACGT[AC][AG]-3'), a sequence present in many viral and cellular promoters. Binds to the Tax-responsive element (TRE) of HTLV-I. Mediates PKA-induced stimulation of CRE-reporter genes. Represses the expression of FTH1 and other antioxidant detoxification genes. Triggers cell proliferation and transformation (By similarity). {ECO:0000250}. PTM: Phosphorylated at Ser-196 by HIPK2 in response to genotoxic stress. This phosphorylation promotes transcription repression of FTH1 and other antioxidant detoxification genes. The CDK3-mediated phosphorylation at Ser-63 promotes its transactivation and transcriptional activities (By similarity). Phosphorylated at Ser-63 by RPS6KA4 and RPS6KA5 in response to mitogenic or stress stimuli. {ECO:0000250, ECO:0000269|PubMed:18690222}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Binds DNA as a dimer. Interacts with HIPK2 and CDK3 (By similarity). {ECO:0000250}. +Q80XK6 ATG2B_MOUSE Autophagy-related protein 2 homolog B 2075 231,399 Alternative sequence (2); Chain (1); Erroneous initiation (2); Frameshift (1); Modified residue (12); Sequence conflict (4) FUNCTION: Required for both autophagosome formation and regulation of lipid droplet morphology and dispersion. {ECO:0000250}. SUBCELLULAR LOCATION: Preautophagosomal structure membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Lipid droplet {ECO:0000250}. +Q8BGE6 ATG4B_MOUSE Cysteine protease ATG4B (EC 3.4.22.-) (AUT-like 1 cysteine endopeptidase) (Autophagin-1) (Autophagy-related cysteine endopeptidase 1) (Autophagy-related protein 4 homolog B) 393 44,375 Active site (3); Chain (1); Modified residue (2); Sequence conflict (8) FUNCTION: Cysteine protease required for the cytoplasm to vacuole transport (Cvt) and autophagy. Cleaves the C-terminal amino acid of ATG8 family proteins MAP1LC3, GABARAPL1, GABARAPL2 and GABARAP, to reveal a C-terminal glycine. Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy. Has also an activity of delipidating enzyme for the PE-conjugated forms (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +Q9D2Q3 CJ088_MOUSE Uncharacterized protein C10orf88 homolog 444 48,743 Chain (1); Modified residue (4) +Q99J83 ATG5_MOUSE Autophagy protein 5 (APG5-like) 275 32,402 Chain (1); Cross-link (1); Modified residue (1); Mutagenesis (1) FUNCTION: Involved in autophagic vesicle formation. Conjugation with ATG12, through a ubiquitin-like conjugating system involving ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate acts as an E3-like enzyme which is required for lipidation of ATG8 family proteins and their association to the vesicle membranes. Involved in mitochondrial quality control after oxidative damage, and in subsequent cellular longevity. Plays a critical role in multiple aspects of lymphocyte development and is essential for both B and T lymphocyte survival and proliferation. Required for optimal processing and presentation of antigens for MHC II. Involved in the maintenance of axon morphology and membrane structures, as well as in normal adipocyte differentiation. Promotes primary ciliogenesis through removal of OFD1 from centriolar satellites and degradation of IFT20 via the autophagic pathway. {ECO:0000269|PubMed:11266458, ECO:0000269|PubMed:12890687, ECO:0000269|PubMed:17190837, ECO:0000269|PubMed:17912025, ECO:0000269|PubMed:18188005, ECO:0000269|PubMed:19844159, ECO:0000269|PubMed:20171125, ECO:0000269|PubMed:24089205, ECO:0000269|PubMed:24089209}.; FUNCTION: May play an important role in the apoptotic process, possibly within the modified cytoskeleton. Its expression is a relatively late event in the apoptotic process, occurring downstream of caspase activity. Plays a crucial role in IFN-gamma-induced autophagic cell death by interacting with FADD (By similarity). {ECO:0000250|UniProtKB:Q9H1Y0}.; FUNCTION: (Microbial infection) May act as a proviral factor. In association with ATG12, negatively regulates the innate antiviral immune response by impairing the type I IFN production pathway upon vesicular stomatitis virus (VSV) infection. {ECO:0000269|PubMed:17709747}. PTM: Conjugated to ATG12; which is essential for autophagy, but is not required for association with isolation membrane.; PTM: Acetylated by EP300. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24089209}. Preautophagosomal structure membrane {ECO:0000269|PubMed:24089209}; Peripheral membrane protein {ECO:0000269|PubMed:24089209}. Note=The conjugate detaches from the membrane immediately before or after autophagosome formation is completed. Localizes also to discrete punctae along the ciliary axoneme and to the base of the ciliary axoneme. SUBUNIT: Forms a conjugate with ATG12 (PubMed:11266458, PubMed:12890687, PubMed:12665549, PubMed:18768753, PubMed:19417210). The ATG5-ATG12 conjugate forms a complex with several units of ATG16L (PubMed:12665549). Interacts with TECPR1; the interaction is direct and does not take place when ATG16L is associated with the ATG5-ATG12 conjugate (By similarity). Interacts with DHX58/RIG-1, IFIH1/MDA5 and MAVS/IPS-1 in monomeric form as well as in ATG12-ATG5 conjugate form. The interaction with MAVS is further enhanced upon vesicular stomatitis virus (VSV) infection (PubMed:17709747). Interacts with ATG3 (By similarity). Interacts with ATG7 and ATG10 (PubMed:12482611). Interacts with FADD (By similarity). {ECO:0000250|UniProtKB:Q9H1Y0, ECO:0000269|PubMed:11266458, ECO:0000269|PubMed:12482611, ECO:0000269|PubMed:12665549, ECO:0000269|PubMed:12890687, ECO:0000269|PubMed:17709747, ECO:0000269|PubMed:18768753, ECO:0000269|PubMed:19417210}. TISSUE SPECIFICITY: Ubiquitous. +Q91V76 CK054_MOUSE Ester hydrolase C11orf54 homolog (EC 3.1.-.-) 315 34,996 Chain (1); Metal binding (3) FUNCTION: Exhibits ester hydrolase activity on the substrate p-nitrophenyl acetate. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. +Q9D4W2 CK065_MOUSE Uncharacterized protein C11orf65 homolog 315 36,933 Chain (1); Sequence conflict (1) +Q91VN2 CK071_MOUSE Uncharacterized protein C11orf71 homolog 117 12,629 Chain (1); Sequence conflict (1) +Q9CQI4 CK074_MOUSE Uncharacterized protein C11orf74 homolog (Protein NWC) 244 27,654 Chain (1); Erroneous gene model prediction (2); Modified residue (2); Sequence conflict (2) TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15971274}. +Q78WH7 CK2N2_MOUSE Calcium/calmodulin-dependent protein kinase II inhibitor 2 (CaM-KII inhibitory protein) (CaM-KIIN) 79 8,628 Chain (1); Region (1) FUNCTION: Potent and specific cellular inhibitor of CaM-kinase II (CAMK2). Traps Ca(2+)/calmodulin on CAMK2 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytosol. Note=Excluded from nucleus when coexpressed with activated CAMK2. {ECO:0000250}. SUBUNIT: Interacts with CAMK2A and CAMK2B in the presence of Ca(2+)/calmodulin or after autophosphorylation. {ECO:0000250}. DOMAIN: The inhibitory domain blocks CAMK2 binding to GRIN2B. {ECO:0000250}. +Q9D8Z6 ATGA1_MOUSE Autophagy-related protein 101 218 25,002 Chain (1); Region (1) FUNCTION: Autophagy factor required for autophagosome formation. Stabilizes ATG13, protecting it from proteasomal degradation. {ECO:0000250|UniProtKB:Q9BSB4}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BSB4}. Preautophagosomal structure {ECO:0000250|UniProtKB:Q9BSB4}. Note=Under starvation conditions, it is localized to puncate structures primarily representing the isolation membrane; the isolation membrane sequesters a portion of the cytoplasm resulting in autophagosome formation. {ECO:0000250|UniProtKB:Q9BSB4}. SUBUNIT: Interacts with ATG13. Associates with a complex composed of ATG13, ULK1 and RB1CC1; the association with this complex requires the presence of ATG13. {ECO:0000250|UniProtKB:Q9BSB4}. +Q8K389 CK5P2_MOUSE CDK5 regulatory subunit-associated protein 2 (CDK5 activator-binding protein C48) 1822 205,945 Chain (1); Erroneous initiation (1); Modified residue (9); Region (6) FUNCTION: Potential regulator of CDK5 activity via its interaction with CDK5R1. Negative regulator of centriole disengagement (licensing) which maintains centriole engagement and cohesion (PubMed:20627074). Involved in regulation of mitotic spindle orientation (PubMed:20460369). Plays a role in the spindle checkpoint activation by acting as a transcriptional regulator of both BUBR1 and MAD2 promoter. Required for the recruitment of AKAP9 to centrosomes (By similarity). Plays a role in neurogenesis (PubMed:20471352). Contrary to higher mammalian orthologs, including human, chimpanzee, bovine and dog, does not interact with EB1/MAPRE1, therefore its function in the regulation of microtubule dynamics is unclear (PubMed:19553473). {ECO:0000250|UniProtKB:Q96SN8, ECO:0000269|PubMed:19553473, ECO:0000269|PubMed:20460369, ECO:0000269|PubMed:20471352, ECO:0000269|PubMed:20627074}. PTM: Phosphorylated in vitro by CDK5. {ECO:0000250|UniProtKB:Q9JLH5}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:20466722, ECO:0000269|PubMed:20471352, ECO:0000269|PubMed:20627074, ECO:0000305|PubMed:19553473}. Golgi apparatus {ECO:0000250|UniProtKB:Q96SN8}. Cytoplasm {ECO:0000250|UniProtKB:Q96SN8}. Note=Found in the pericentriolar region adhering to the surface of the centrosome and in the region of the centrosomal appendages. Due to the lack of interaction with EB1/MAPRE1, its localization to microtubule plus ends may not be conserved in mice (Probable). Localization to centrosomes versus Golgi apparatus may be cell type-dependent (By similarity). {ECO:0000250|UniProtKB:Q96SN8, ECO:0000305|PubMed:19553473}. SUBUNIT: Interacts with CDK5R1 (p35 form) (By similarity). CDK5RAP1, CDK5RAP2 and CDK5RAP3 show competitive binding to CDK5R1. May form a complex with CDK5R1 and CDK5 (By similarity). Interacts (via C-terminus) with PCNT; the interaction is leading to centrosomal localization of CDK5RAP2 and PCNT. Interacts with AKAP9; the interaction is leading to Golgi localization of CDK5RAP2 and AKAP9 (By similarity). Interacts with TUBG1; the interaction is leading to the centrosomal localization of CDK5RAP2 and TUBG1 (By similarity). Interacts with TUBGCP3 (By similarity). Interacts with CALM1 (By similarity). Interacts with CDC20 (By similarity). Interacts with CEP68; degradation of CEP68 in early mitosis leads to removal of CDK5RAP2 from the centrosome which promotes centriole disengagement and subsequent centriole separation (By similarity). Interacts with NCKAP5L (By similarity). Interacts with LGALS3BP; this interaction may connect the pericentrosomal complex to the gamma-tubulin ring complex (gamma-TuRC) to promote microtubule assembly and acetylation (By similarity). Contrary to human, chimpanzee, bovine and dog orthologous proteins, does not interact with EB1/MAPRE1, possibly due to a divergence at the level of the critical residue 940, which is a proline in MAPRE1-binding orthologs and a leucine in mouse and rat (PubMed:19553473). {ECO:0000250|UniProtKB:Q96SN8, ECO:0000250|UniProtKB:Q9JLH5, ECO:0000269|PubMed:19553473, ECO:0000269|PubMed:20471352}. TISSUE SPECIFICITY: Expressed in testis, thymus, heart and brain. {ECO:0000269|PubMed:20460369}. +Q504P2 CL12A_MOUSE C-type lectin domain family 12 member A (C-type lectin-like molecule 1) (CLL-1) (Myeloid inhibitory C-type lectin-like receptor) (MICL) (CD antigen CD371) 267 30,757 Chain (1); Disulfide bond (2); Domain (1); Glycosylation (3); Motif (1); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 44 64 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 43 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 65 267 Extracellular. {ECO:0000255}. FUNCTION: Cell surface receptor that modulates signaling cascades and mediates tyrosine phosphorylation of target MAP kinases. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein. Note=Ligand binding leads to internalization. {ECO:0000250}. SUBUNIT: Interacts with PTPN6 and PTPN11. {ECO:0000250}. DOMAIN: Contains 1 copy of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is involved in modulation of cellular responses. The phosphorylated ITIM motif can bind the SH2 domain of several SH2-containing phosphatases (By similarity). {ECO:0000250}. +Q8BH66 ATLA1_MOUSE Atlastin-1 (EC 3.6.5.-) (Spastic paraplegia 3A homolog) 558 63,377 Chain (1); Coiled coil (1); Domain (1); Modified residue (4); Nucleotide binding (4); Region (1); Topological domain (3); Transmembrane (2) TRANSMEM 450 470 Helical. {ECO:0000255}.; TRANSMEM 472 492 Helical. {ECO:0000255}. TOPO_DOM 1 449 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 471 471 Lumenal. {ECO:0000255}.; TOPO_DOM 493 558 Cytoplasmic. {ECO:0000250}. FUNCTION: GTPase tethering membranes through formation of trans-homooligomers and mediating homotypic fusion of endoplasmic reticulum membranes. Functions in endoplasmic reticulum tubular network biogenesis. May also regulate Golgi biogenesis. May regulate axonal development. {ECO:0000250|UniProtKB:Q8WXF7}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8WXF7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8WXF7}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q8WXF7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8WXF7}. Cell projection, axon {ECO:0000250|UniProtKB:Q6PST4}. Note=Localizes to endoplasmic reticulum tubular network. {ECO:0000269|PubMed:24668814}. SUBUNIT: Monomer as apoprotein and in the GDP-bound form. Homodimer in the GTP-bound form. Homooligomer. Interacts (via N-terminal region) with MAP4K4 (via CNH regulatory domain). Interacts with SPAST; interaction is direct (By similarity). Interacts with REEP5, RTN3 and probably RTN4 (via the transmembrane region) (PubMed:19665976). Interacts with REEP1. Interacts with CPT1C. Interacts with ARL6IP1 (By similarity). Interacts with ZFYVE27 (PubMed:24668814). {ECO:0000250|UniProtKB:Q6PST4, ECO:0000250|UniProtKB:Q8WXF7, ECO:0000269|PubMed:19665976, ECO:0000269|PubMed:24668814}. +Q80T21 ATL4_MOUSE ADAMTS-like protein 4 (ADAMTSL-4) (Thrombospondin repeat-containing protein 1) 1036 113,225 Chain (1); Compositional bias (1); Domain (7); Glycosylation (2); Sequence conflict (1); Signal peptide (1) FUNCTION: Positive regulation of apoptosis. May facilitate FBN1 microfibril biogenesis (By similarity). {ECO:0000250}. PTM: Glycosylated (By similarity). Can be O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS family members. Also can be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated. These other glycosylations can also facilitate secretion (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. Note=Colocalizes with FMN1 microfibrils in the eye ECM. {ECO:0000250}. SUBUNIT: Interacts with CTSB. Interacts with FBN1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed in a range of tissues. Especially prevalent in brain, spinal cord, muscle, lung and heart. {ECO:0000269|PubMed:12706885}. +Q7TSQ1 CL18A_MOUSE C-type lectin domain family 18 member A (Mannose receptor-like protein) 534 58,585 Alternative sequence (4); Chain (1); Disulfide bond (4); Domain (3) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q6P9S1 ATMIN_MOUSE ATM interactor (ATM/ATR-substrate CHK2-interacting zinc finger protein) (ASCIZ) 818 87,424 Chain (1); Erroneous initiation (1); Frameshift (1); Region (1); Sequence caution (1); Sequence conflict (2); Zinc finger (2) FUNCTION: Transcription factor. Plays a crucial role in cell survival and RAD51 foci formation in response to methylating DNA damage. Involved in regulating the activity of ATM in the absence of DNA damage. May play a role in stabilizing ATM (By similarity). Binds to the DYNLL1 promoter and activates its transcription. {ECO:0000250, ECO:0000269|PubMed:22167198}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O43313}. Note=Nuclear, in discrete foci during G1 phase. {ECO:0000250|UniProtKB:O43313}. SUBUNIT: Interacts via its C-terminus with ATM. Interacts with DYNLL; this interaction inhibits ATMIN transcriptional activity and hence may play a role in a feedback loop whereby DYNLL1 inhibits transactivation of its own promoter by ATMIN. ATMIN. {ECO:0000250}. +Q8BRT1 CLAP2_MOUSE CLIP-associating protein 2 (Cytoplasmic linker-associated protein 2) 1286 140,739 Alternative sequence (5); Beta strand (1); Chain (1); Compositional bias (1); Frameshift (1); Helix (14); Modified residue (27); Motif (2); Mutagenesis (2); Region (6); Repeat (8); Sequence conflict (4); Turn (1) FUNCTION: Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules. Involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). Required for the polarization of the cytoplasmic microtubule arrays in migrating cells towards the leading edge of the cell. May act at the cell cortex to enhance the frequency of rescue of depolymerizing microtubules by attaching their plus-ends to cortical platforms composed of ERC1 and PHLDB2. This cortical microtubule stabilizing activity is regulated at least in part by phosphatidylinositol 3-kinase signaling. Also performs a similar stabilizing function at the kinetochore which is essential for the bipolar alignment of chromosomes on the mitotic spindle. Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. {ECO:0000250|UniProtKB:O75122, ECO:0000269|PubMed:16914514}. PTM: Phosphorylated by GSK3B. Phosphorylation by GSK3B may negatively regulate binding to microtubule lattices in lamella. Isoform 2 is phosphorylated on Ser-241. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11290329}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Chromosome, centromere, kinetochore. Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, spindle pole. Golgi apparatus {ECO:0000269|PubMed:11290329}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:O75122}. Cell membrane {ECO:0000250|UniProtKB:O75122}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:O75122}. Note=Localizes to microtubule plus ends (PubMed:11290329). Localizes to centrosomes, kinetochores and the mitotic spindle from prometaphase. Subsequently localizes to the spindle midzone from anaphase and to the midbody from telophase. In migrating cells localizes to the plus ends of microtubules within the cell body and to the entire microtubule lattice within the lamella. Localizes to the cell cortex and this requires ERC1 and PHLDB2 (By similarity). Also localizes to meiotic spindle poles. The MEMO1-RHOA-DIAPH1 signaling pathway controls localization of the phosphorylated form to the cell membrane (By similarity). {ECO:0000250|UniProtKB:O75122, ECO:0000269|PubMed:11290329}. SUBUNIT: Interacts with microtubules (PubMed:11290329). Interacts with MAPRE1; probably required for targeting to growing microtubule plus ends. Interacts with ERC1, MAPRE3 and PHLDB2. The interaction with ERC1 may be mediated by PHLDB2. Interacts with GCC2; recruits CLASP2 to Golgi membranes (By similarity). Interacts with CLIP2 and RSN (PubMed:11290329). Interacts with MACF1 (PubMed:18854161). {ECO:0000250|UniProtKB:O75122, ECO:0000269|PubMed:11290329, ECO:0000269|PubMed:18854161}. DOMAIN: The two SXIP sequence motifs mediate interaction with MAPRE1; this is necessary for targeting to growing microtubule plus ends. {ECO:0000250|UniProtKB:O75122}.; DOMAIN: Two TOG regions display structural characteristics similar to HEAT repeat domains and mediate interaction with microtubules. {ECO:0000250|UniProtKB:O75122, ECO:0000269|PubMed:26003921}. TISSUE SPECIFICITY: Highly expressed in brain and at low levels in heart, kidney and lung. {ECO:0000269|PubMed:11290329}. +Q8CFC7 CLASR_MOUSE CLK4-associating serine/arginine rich protein (Clk4-associating SR-related protein) (Serine/arginine-rich splicing factor 16) (Splicing factor, arginine/serine-rich 16) (Suppressor of white-apricot homolog 2) 668 76,825 Alternative sequence (4); Chain (1); Coiled coil (1); Compositional bias (2); Erroneous initiation (2); Modified residue (8) FUNCTION: Probably functions as an alternative splicing regulator. May regulate the mRNA splicing of genes such as CLK1. May act by regulating members of the CLK kinase family. PTM: Phosphorylated in vitro by CLK4. SUBCELLULAR LOCATION: Nucleus. Note=Located in nuclear dots.; SUBCELLULAR LOCATION: Isoform 2: Nucleus, nucleoplasm. SUBUNIT: Probably interacts with CLK4. TISSUE SPECIFICITY: Highly expressed in brain. Expressed at intermediate level in lung and liver. In brain, it is expressed in the hippocampus, cerebellum and olfactory bulb. +Q03059 CLAT_MOUSE Choline O-acetyltransferase (CHOACTase) (ChAT) (Choline acetylase) (EC 2.3.1.6) 641 71,853 Active site (1); Binding site (2); Chain (1); Modified residue (2); Region (1) FUNCTION: Catalyzes the reversible synthesis of acetylcholine (ACh) from acetyl CoA and choline at cholinergic synapses. +P49300 CLC10_MOUSE C-type lectin domain family 10 member A (MMGL) (Macrophage asialoglycoprotein-binding protein 1) (M-ASGP-BP-1) (Macrophage galactose/N-acetylgalactosamine-specific lectin) 304 34,596 Chain (1); Disulfide bond (3); Domain (1); Glycosylation (2); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 36 56 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 35 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 57 304 Extracellular. {ECO:0000255}. FUNCTION: Recognizes terminal galactose and N-acetylgalactosamine units. May participate in the interaction between tumoricidal macrophages and tumor cells. Plays a role in the recruitment of inflammatory monocytes to adipose tissue in diet-induced obesity. {ECO:0000269|PubMed:19995956}. SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. SUBUNIT: Homooligomer. Interacts with SIGLEC1, which may act as a counter-receptor for CLEC10A in lymph node. {ECO:0000269|PubMed:15364954}. TISSUE SPECIFICITY: Detected in lymph node in the subcapsular sinus, interfollicular regions, T and B-cell boundary and in the areas surrounding high endothelial venules (at protein level). Expressed on the surface of activated macrophages. Expressed in heart, lung, testis, skeletal muscle, spleen, brain, kidney and thymus. Expressed in P388, RAW 264.7 and M1 cell lines. {ECO:0000269|PubMed:12016228, ECO:0000269|PubMed:15364954}. +O88200 CLC11_MOUSE C-type lectin domain family 11 member A (Lymphocyte secreted C-type lectin) (Osteolectin) (Stem cell growth factor) 328 36,451 Chain (1); Disulfide bond (2); Domain (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Promotes osteogenesis by stimulating the differentiation of mesenchymal progenitors into mature osteoblasts. Important for repair and maintenance of adult bone. {ECO:0000269|PubMed:27976999}. PTM: O-glycosylated. Probably sulfated on the O-glycans (By similarity). {ECO:0000250|UniProtKB:Q9Y240}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y240}. Secreted {ECO:0000305|PubMed:27976999}. TISSUE SPECIFICITY: Detected in femur where it localizes to trabecular bone of the femur metaphysis, and cortical bone of the proximal femur. Also expressed in trabecular and cortical bone of vertebrae (at protein level). Strongly expressed in osteoblasts and bone marrow stromal cells. Also has very weak expression in B cell progenitors in the bone marrow and T cells in the spleen. {ECO:0000269|PubMed:27976999}. +Q8VCP9 CLC14_MOUSE C-type lectin domain family 14 member A 459 49,066 Chain (1); Disulfide bond (1); Domain (2); Glycosylation (4); Modified residue (1); Sequence conflict (5); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 387 407 Helical. {ECO:0000255}. TOPO_DOM 22 386 Extracellular. {ECO:0000255}.; TOPO_DOM 408 459 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q8BWY2 CLC1A_MOUSE C-type lectin domain family 1 member A 269 30,958 Chain (1); Disulfide bond (2); Domain (1); Glycosylation (4); Sequence conflict (3); Topological domain (2); Transmembrane (1) TRANSMEM 52 72 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 51 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 73 269 Extracellular. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. +Q9JL99 CLC1B_MOUSE C-type lectin domain family 1 member B (C-type lectin-like receptor 2) (CLEC-2) 229 26,239 Alternative sequence (1); Chain (1); Disulfide bond (3); Domain (1); Glycosylation (4); Modified residue (1); Topological domain (2); Transmembrane (1) TRANSMEM 32 52 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 31 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 53 229 Extracellular. {ECO:0000255}. FUNCTION: C-type lectin-like receptor that functions as a platelet receptor for the lymphatic endothelial marker, PDPN. After ligand activation, signals via sequential activation of SRC and SYK tyrosine kinases leading to activation of PLCG2. {ECO:0000250|UniProtKB:Q9P126}. PTM: Glycosylated. {ECO:0000269|PubMed:16174766}.; PTM: Phosphorylated on tyrosine residue in response to rhodocytin binding. {ECO:0000269|PubMed:16174766}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. SUBUNIT: Homodimer. Interacts (via cytoplasmic domain) with RACK1; promotes CLEC1B ubiquitination and proteasome-mediated degradation. Interacts (dimer) with SYK (via SH2 domains) (By similarity). Interacts with PDPN; the interaction is independent of CLEC1B glycosylation and activates CLEC1B (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9P126}. TISSUE SPECIFICITY: Hematopoietic cells, megakaryocytes and platelets. {ECO:0000269|PubMed:10671229, ECO:0000269|PubMed:16174766}. +Q91V08 CLC2D_MOUSE C-type lectin domain family 2 member D (C-type lectin-related protein B) (Clr-b) (Lectin-like transmembrane protein) (Osteoclast inhibitory lectin) 207 23,647 Beta strand (6); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (1); Helix (2); Modified residue (2); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 42 62 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 41 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 63 207 Extracellular. {ECO:0000255}. FUNCTION: Receptor for KLRB1B that protects target cells against natural killer cell-mediated lysis (PubMed:14990792, PubMed:16751398). Inhibits osteoclast formation (PubMed:11278931, PubMed:12374791). Binds high molecular weight sulfated glycosaminoglycans (PubMed:15123656). {ECO:0000269|PubMed:11278931, ECO:0000269|PubMed:12374791, ECO:0000269|PubMed:14990792, ECO:0000269|PubMed:15123656, ECO:0000269|PubMed:16751398}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9UHP7}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14990792, ECO:0000269|PubMed:16751398}; Single-pass type II membrane protein {ECO:0000269|PubMed:14990792}. SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250|UniProtKB:Q9UHP7}. TISSUE SPECIFICITY: Detected in fetal heart, brain, lung, chondrocytes, perichondrium and osteoblasts, and in adult splenocytes, thymocytes, lymph-node cells, osteoblasts, growth plate chondrocytes and skeltal muscle overlying the bone (at protein level). Ubiquitous. Detected in thymus, bone marrow, lung, gut, heart, skeletal muscle, ovary, spleen, ileum, liver and kidney. {ECO:0000269|PubMed:11278931, ECO:0000269|PubMed:11398965, ECO:0000269|PubMed:12374791, ECO:0000269|PubMed:14990792, ECO:0000269|PubMed:16751398}. +Q80XD9 CLC2E_MOUSE C-type lectin domain family 2 member E (C-type lectin-related protein A) (Clr-a) 204 22,754 Chain (1); Disulfide bond (2); Domain (1); Glycosylation (1); Sequence conflict (8); Topological domain (2); Transmembrane (1) TRANSMEM 37 59 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 36 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 60 204 Extracellular. {ECO:0000255}. FUNCTION: Lectin-type cell surface receptor. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. +Q9EPW4 CLC3A_MOUSE C-type lectin domain family 3 member A (C-type lectin superfamily member 1) (Cartilage-derived C-type lectin) 196 22,192 Chain (1); Disulfide bond (3); Domain (1); Signal peptide (1) FUNCTION: Promotes cell adhesion to laminin and fibronectin. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +Q9QZ15 CLC4A_MOUSE C-type lectin domain family 4 member A (C-type lectin superfamily member 6) (Dendritic cell immunoreceptor) (CD antigen CD367) 238 27,323 Binding site (1); Chain (1); Disulfide bond (3); Domain (1); Glycosylation (3); Metal binding (7); Motif (1); Mutagenesis (1); Region (2); Topological domain (2); Transmembrane (1) TRANSMEM 49 69 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 48 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 70 238 Extracellular. {ECO:0000255}. FUNCTION: May be involved in regulating immune reactivity. May play a role in modulating dendritic cells (DC) differentiation and/or maturation (By similarity). May be involved in the inhibition of B-cell-receptor-mediated calcium mobilization and protein tyrosine phosphorylation. {ECO:0000250, ECO:0000269|PubMed:11841542}.; FUNCTION: C-type lectin receptor that binds carbohydrates mannose and fucose but also weakly interacts with N-acetylglucosamine (GlcNAc) in a Ca(2+)-dependent manner. Involved in regulating immune reactivity. Once triggered by antigen, it is internalized by clathrin-dependent endocytosis and delivers its antigenic cargo into the antigen presentation pathway resulting in cross-priming of CD8(+) T cells. This cross-presentation and cross-priming are enhanced by TLR7 and TLR8 agonists with increased expansion of the CD8(+) T cells, high production of IFNG and TNF with reduced levels of IL4, IL5 and IL13. In plasmacytoid dendritic cells, inhibits TLR9-mediated IFNA and TNF production (By similarity). May be involved via its ITIM motif (immunoreceptor tyrosine-based inhibitory motifs) in the inhibition of B-cell-receptor-mediated calcium mobilization and protein tyrosine phosphorylation (PubMed:11841542). {ECO:0000250|UniProtKB:Q9UMR7, ECO:0000269|PubMed:11841542}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9UMR7}; Extracellular side {ECO:0000250|UniProtKB:Q9UMR7}. SUBUNIT: May interact with PTPN6 via its ITIM site. {ECO:0000250|UniProtKB:Q9UMR7}. DOMAIN: Contains 1 copy of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is involved in modulation of cellular responses. The phosphorylated ITIM motif can bind the SH2 domain of several SH2-containing phosphatases. {ECO:0000269|PubMed:11841542}. TISSUE SPECIFICITY: Expressed in splenic antigen-presenting cells including B-cells, monocytes/macrophages, and dendritic cells (at protein level). Expressed in spleen and lymph node and slightly increased with dendritic cell maturation. {ECO:0000269|PubMed:11841542}. +Q9Z2H6 CLC4D_MOUSE C-type lectin domain family 4 member D (C-type lectin superfamily member 8) (Macrophage-restricted C-type lectin) (CD antigen CD368) 219 25,619 Chain (1); Disulfide bond (3); Domain (1); Glycosylation (2); Metal binding (3); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 21 43 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 20 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 44 219 Extracellular. {ECO:0000255}. FUNCTION: A calcium-dependent lectin involved in innate recognition of pathogen-associated molecular patterns (PAMPs). Interacts with signaling adapter Fc receptor gamma chain/FCER1G, likely via CLEC4E, to form a functional complex in antigen presenting cells. Binding of mycobacterial trehalose 6,6'-dimycolate (TDM) to this receptor complex leads to phosphorylation of the immunoreceptor tyrosine-based activation motif (ITAM) of FCER1G, triggering activation of SYK, CARD9 and NF-kappa-B, consequently driving maturation of antigen-presenting cells and shaping antigen-specific priming of T-cells toward effector T-helper 1 and T-helper 17 cell subtypes (PubMed:23602766). Functions as an endocytic receptor. May be involved in antigen uptake at the site of infection, either for clearance of the antigen, or for processing and further presentation to T-cells (By similarity). {ECO:0000250|UniProtKB:Q8WXI8, ECO:0000269|PubMed:23602766}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:23602766}; Single-pass type II membrane protein {ECO:0000305}. SUBUNIT: Heterodimer with CLEC4E; disulfide-linked. CLEC4E acts as a bridge for interaction between CLEC4D and FCER1G to form a functional complex. {ECO:0000250|UniProtKB:Q69FH1}. TISSUE SPECIFICITY: Constitutively expressed in myeloid cells including dendritic cells (at protein level) (PubMed:23602766). Expressed in the macrophage populations of bone marrow, spleen, lung and lymph nodes (PubMed:9660840). {ECO:0000269|PubMed:23602766, ECO:0000269|PubMed:9660840}. +Q9R0Q8 CLC4E_MOUSE C-type lectin domain family 4 member E (C-type lectin superfamily member 9) (Macrophage-inducible C-type lectin) (Mincle) 214 24,431 Chain (1); Disulfide bond (3); Domain (1); Glycosylation (1); Metal binding (7); Motif (1); Mutagenesis (3); Topological domain (2); Transmembrane (1) TRANSMEM 23 45 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 22 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 46 214 Extracellular. {ECO:0000255}. FUNCTION: A calcium-dependent lectin that acts as a pattern recognition receptor of the innate immune system. Recognizes damage-associated molecular patterns (DAMPs) of abnormal self and pathogen-associated molecular patterns (PAMPs) of bacteria and fungi (PubMed:18509109, PubMed:19171887, PubMed:23602766, PubMed:18776906). The PAMPs notably include mycobacterial trehalose 6,6'-dimycolate (TDM), a cell wall glycolipid with potent adjuvant immunomodulatory functions (PubMed:23602766). Interacts with signaling adapter Fc receptor gamma chain/FCER1G to form a functional complex in myeloid cells (PubMed:23602766, PubMed:18776906). Binding of mycobacterial trehalose 6,6'-dimycolate (TDM) to this receptor complex leads to phosphorylation of the immunoreceptor tyrosine-based activation motif (ITAM) of FCER1G, triggering activation of SYK, CARD9 and NF-kappa-B, consequently driving maturation of antigen-presenting cells and shaping antigen-specific priming of T-cells toward effector T-helper 1 and T-helper 17 cell subtypes (PubMed:23602766). Specifically recognizes alpha-mannose residues on pathogenic fungi of the genus Malassezia and mediates macrophage activation (PubMed:19171887). Through recognition of DAMPs released upon nonhomeostatic cell death, enables immune sensing of damaged self and promotes inflammatory cell infiltration into the damaged tissue (PubMed:18776906). {ECO:0000269|PubMed:18509109, ECO:0000269|PubMed:18776906, ECO:0000269|PubMed:19171887, ECO:0000269|PubMed:23602766}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:23602766, ECO:0000305|PubMed:10528209}; Single-pass type II membrane protein {ECO:0000305|PubMed:10528209}. SUBUNIT: Monomer and homodimer (PubMed:18509109). Interacts with signaling adapter Fc receptor gamma chain/FCER1G to form a functional complex; the interaction is direct (PubMed:23602766). Alternatively, acts as a bridge for interaction between CLEC4D and FCER1G. A heterodimer of CLEC4E and CLEC4D associates with FCER1G to form a functional complex (By similarity). Interacts with SAP130 nuclear protein that is released from necrotic cells; the interaction is direct (PubMed:23602766). {ECO:0000250|UniProtKB:Q67EQ1, ECO:0000269|PubMed:18509109, ECO:0000269|PubMed:23602766}. TISSUE SPECIFICITY: Highly expressed in macrophages in response to stimulation with bacterial glycolipids and proinflammatory cytokines (PubMed:10528209). Expressed in dendritic cells (at protein level) in response to stimulation with mycobacterial trehalose 6,6'-dimycolate (TDM) (PubMed:23602766). {ECO:0000269|PubMed:10528209, ECO:0000269|PubMed:23602766}. +O08997 ATOX1_MOUSE Copper transport protein ATOX1 (Metal transport protein ATX1) 68 7,338 Chain (1); Domain (1); Metal binding (2); Modified residue (2) FUNCTION: Binds and deliver cytosolic copper to the copper ATPase proteins. May be important in cellular antioxidant defense (By similarity). {ECO:0000250}. SUBUNIT: Interacts with ATP7B (By similarity). Interacts with ATP7A (By similarity). {ECO:0000250|UniProtKB:O00244}. +Q8BNX1 CLC4G_MOUSE C-type lectin domain family 4 member G 294 33,327 Chain (1); Coiled coil (1); Disulfide bond (1); Domain (1); Glycosylation (4); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 31 51 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 30 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 52 294 Extracellular. {ECO:0000255}. FUNCTION: Binds mannose, N-acetylglucosamine (GlcNAc) and fucose, but not galactose, in a Ca(2+)-dependent manner. {ECO:0000250|UniProtKB:Q6UXB4}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6UXB4}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q6UXB4}. +Q8VBX4 CLC4K_MOUSE C-type lectin domain family 4 member K (Langerin) (CD antigen CD207) 331 37,621 Beta strand (8); Chain (1); Coiled coil (1); Disulfide bond (2); Domain (1); Glycosylation (2); Helix (5); Sequence conflict (1); Topological domain (2); Transmembrane (1); Turn (3) TRANSMEM 42 62 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 41 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 63 331 Extracellular. {ECO:0000255}. FUNCTION: Calcium-dependent lectin displaying mannose-binding specificity. Induces the formation of Birbeck granules (BGs); is a potent regulator of membrane superimposition and zippering. Binds to sulfated as well as mannosylated glycans, keratan sulfate (KS) and beta-glucans. Facilitates uptake of antigens and is involved in the routing and/or processing of antigen for presentation to T cells. {ECO:0000269|PubMed:11777972, ECO:0000269|PubMed:18322168}. SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. Note=Found in Birbeck granules (BGs), which are organelles consisting of superimposed and zippered membranes. {ECO:0000250}. SUBUNIT: Homotrimer. {ECO:0000250}. DOMAIN: The C-type lectin domain mediates dual recognition of both sulfated and mannosylated glycans. {ECO:0000250}. TISSUE SPECIFICITY: Expressed by Langerhans cells. Expressed in dendritic cells and by scattered cells in lymph nodes and spleen. Also detected in some non-lymphoid tissues such as lung, liver and heart. {ECO:0000269|PubMed:11777972}. +Q9JKF4 CLC6A_MOUSE C-type lectin domain family 6 member A (C-type lectin superfamily member 10) (Dendritic cell-associated C-type lectin 2) (DC-associated C-type lectin 2) (Dectin-2) 209 24,324 Alternative sequence (2); Chain (1); Disulfide bond (4); Domain (1); Glycosylation (1); Metal binding (2); Mutagenesis (1); Region (3); Topological domain (2); Transmembrane (1) TRANSMEM 21 43 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 20 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 44 209 Extracellular. {ECO:0000255}. FUNCTION: Binds high-mannose carbohydrates in a Ca(2+)-dependent manner. Functional receptor for alpha-mannans on C.albicans hypheas. Plays an important role in the host defense against C.albicans infection by inducing TH17 cell differentiation. Recognizes also, in a mannose-dependent manner, allergens from house dust mite and fungi, by promoting cysteinyl leukotriene production. Recognizes soluble elements from the eggs of Shistosoma mansoni altering adaptive immune responses. Transduces signals through an Fc receptor gamma chain /FCER1G and Syk-CARD9-NF-kappa-B-dependent pathway. {ECO:0000269|PubMed:17050534, ECO:0000269|PubMed:19124755, ECO:0000269|PubMed:19703985, ECO:0000269|PubMed:20493731, ECO:0000269|PubMed:21059925}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Note=Ligand binding leads to internalization. SUBUNIT: Associated with FCER1G. {ECO:0000269|PubMed:17050534}. DOMAIN: A short stretch of the intracellular domain (AA 8-14) proximal to the transmembrane domain is required for association with Fc receptor gamma chain. {ECO:0000269|PubMed:17050534}. TISSUE SPECIFICITY: Expressed by the XS52 DC (dendritic cell) line (at protein level). Expressed constitutively by the epidermis, and skin resident DC appear to be the major source of this expression. Expressed in the spleen and thymus. Expression was undetectable in non-DC lines, including macrophage lines (J774 and Raw), T-cell lines (7-17, HDK-1, and D10), B-cell hybridoma (5C5), a keratinocyte line (Pam 212), and a fibroblast line (NS01). {ECO:0000269|PubMed:10766825}. +Q6QLQ4 CLC7A_MOUSE C-type lectin domain family 7 member A (Beta-glucan receptor) (C-type lectin superfamily member 12) (Dendritic cell-associated C-type lectin 1) (DC-associated C-type lectin 1) (Dectin-1) (CD antigen CD369) 244 27,420 Beta strand (8); Chain (1); Disulfide bond (3); Domain (1); Glycosylation (2); Helix (4); Metal binding (4); Motif (1); Mutagenesis (3); Sequence conflict (14); Topological domain (2); Transmembrane (1) TRANSMEM 50 70 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 49 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 71 244 Extracellular. {ECO:0000255}. FUNCTION: Lectin that functions as pattern receptor specific for beta-1,3-linked and beta-1,6-linked glucans, such as cell wall constituents from pathogenic bacteria and fungi. Necessary for the TLR2-mediated inflammatory response and for TLR2-mediated activation of NF-kappa-B. Enhances cytokine production in macrophages and dendritic cells. Mediates production of reactive oxygen species in the cell. Mediates phagocytosis of C.albicans conidia. Binds T-cells in a way that does not involve their surface glycans and plays a role in T-cell activation. Stimulates T-cell proliferation. {ECO:0000269|PubMed:10779524, ECO:0000269|PubMed:11544516, ECO:0000269|PubMed:12719479, ECO:0000269|PubMed:15213161, ECO:0000269|PubMed:15729357, ECO:0000269|PubMed:15731053, ECO:0000269|PubMed:15845454, ECO:0000269|PubMed:16825490}. PTM: N-glycosylated. {ECO:0000269|PubMed:10779524}.; PTM: Phosphorylated on tyrosine residues in response to glucan binding. {ECO:0000269|PubMed:12719479}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10779524, ECO:0000269|PubMed:15213161}; Single-pass type II membrane protein {ECO:0000269|PubMed:10779524, ECO:0000269|PubMed:15213161}. Note=Enriched on zymosan phagosomes. Enrichment does not depend on opsonization. SUBUNIT: Homodimer (Probable). Interacts with SYK; participates in leukocyte activation in presence of fungal pathogens. {ECO:0000269|PubMed:15845454, ECO:0000269|PubMed:17473009, ECO:0000305}. TISSUE SPECIFICITY: Detected in spleen (at protein level). Highly expressed in dendritic cells, spleen and thymus. Detected in epidermal Langerhans cells. Detected in macrophages, liver and lung. {ECO:0000269|PubMed:10779524, ECO:0000269|PubMed:11544516, ECO:0000269|PubMed:12719479}. +Q8BRU4 CLC9A_MOUSE C-type lectin domain family 9 member A (Dendritic cell natural killer lectin group receptor 1) (CD antigen CD370) 238 27,014 Alternative sequence (6); Chain (1); Disulfide bond (3); Domain (1); Frameshift (1); Glycosylation (2); Motif (1); Mutagenesis (1); Topological domain (2); Transmembrane (1) TRANSMEM 36 56 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 35 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 57 238 Extracellular. {ECO:0000255}. FUNCTION: Functions as an endocytic receptor on a small subset of myeloid cells specialized for the uptake and processing of material from dead cells. Recognizes filamentous form of actin in association with particular actin-binding domains of cytoskeletal proteins, including spectrin, exposed when cell membranes are damaged, and mediate the cross-presentation of dead-cell associated antigens in a Syk-dependent manner. {ECO:0000269|PubMed:18408006, ECO:0000269|PubMed:18497879, ECO:0000269|PubMed:19219027, ECO:0000269|PubMed:22483802}. PTM: Isoform 1: Not-glycosylated.; PTM: Isoform 4: N-glycosylated. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:18408006}; Single-pass type II membrane protein {ECO:0000269|PubMed:18408006}. SUBUNIT: Isoform 1: Monomer. Isoform 4: Homodimer. {ECO:0000269|PubMed:18408006, ECO:0000269|PubMed:18497879}. TISSUE SPECIFICITY: Isoform 4 expressed at high levels by CD8(+) dendritic cells (DCs), and at low levels by plasmacytoid DCs but not by other hematopoietic cells. {ECO:0000269|PubMed:18408006, ECO:0000269|PubMed:18497879}. +Q8R2R9 AP3M2_MOUSE AP-3 complex subunit mu-2 (Adaptor-related protein complex 3 subunit mu-2) (Clathrin assembly protein assembly protein complex 3 mu-2 medium chain) (Clathrin coat assembly protein AP47 homolog 2) (Clathrin coat-associated protein AP47 homolog 2) (Golgi adaptor AP-1 47 kDa protein homolog 2) (HA1 47 kDa subunit homolog 2) (Mu3B-adaptin) (m3B) (P47B) 418 46,916 Chain (1); Domain (1); Sequence conflict (1) FUNCTION: Component of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. Ap47 is a subunit of the plasma membrane adaptor (By similarity). In concert with the BLOC-1 complex, AP-3 is required to target cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. {ECO:0000250, ECO:0000269|PubMed:21998198}. SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex. {ECO:0000250}. SUBUNIT: Adaptor protein complex 3 (AP-3) is a heterotetramer composed of two large adaptins (delta-type subunit AP3D1 and beta-type subunit AP3B1 or AP3B2), a medium adaptin (mu-type subunit AP3M1 or AP3M2) and a small adaptin (sigma-type subunit APS1 or AP3S2) (By similarity). AP-3 associates with the BLOC-1 complex. {ECO:0000250}. +Q8R1C9 APBB3_MOUSE Amyloid-beta A4 precursor protein-binding family B member 3 486 52,638 Chain (1); Domain (3) FUNCTION: May modulate the internalization of amyloid-beta precursor protein. {ECO:0000250}. SUBUNIT: Binds to the intracellular domain of amyloid-beta precursor protein. Also binds to APP-like proteins (By similarity). {ECO:0000250}. +E9Q414 APOB_MOUSE Apolipoprotein B-100 (Apo B-100) [Cleaved into: Apolipoprotein B-48 (Apo B-48)] 4505 509,432 Chain (2); Disulfide bond (7); Domain (1); Erroneous initiation (3); Glycosylation (14); Modified residue (3); Region (9); Sequence conflict (5); Signal peptide (1) FUNCTION: Apolipoprotein B is a major protein constituent of chylomicrons (apo B-48), LDL (apo B-100) and VLDL (apo B-100). Apo B-100 functions as a recognition signal for the cellular binding and internalization of LDL particles by the apoB/E receptor. PTM: Palmitoylated; structural requirement for proper assembly of the hydrophobic core of the lipoprotein particle. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P04114}. Secreted {ECO:0000250|UniProtKB:P04114}. SUBUNIT: Interacts with PCSK9. Interacts with MTTP. {ECO:0000250|UniProtKB:P04114}. +O35841 API5_MOUSE Apoptosis inhibitor 5 (API-5) (AAC-11) 504 56,785 Chain (1); Modified residue (5); Motif (1); Region (2); Sequence conflict (1) FUNCTION: Antiapoptotic factor that may have a role in protein assembly. Negatively regulates ACIN1. By binding to ACIN1, it suppresses ACIN1 cleavage from CASP3 and ACIN1-mediated DNA fragmentation. Also known to efficiently suppress E2F1-induced apoptosis (By similarity). {ECO:0000250}. PTM: Acetylation at Lys-251 impairs antiapoptotic function. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Mainly nuclear. SUBUNIT: Monomer. Interacts with FGF2 and ACIN1 (By similarity). {ECO:0000250}. +Q8BTZ5 ANR46_MOUSE Ankyrin repeat domain-containing protein 46 (Ankyrin repeat small protein) (ANK-S) 228 25,223 Chain (1); Repeat (4); Sequence conflict (1); Transmembrane (1) TRANSMEM 195 215 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q9DCZ9 APH1C_MOUSE Putative gamma-secretase subunit APH-1C 258 29,045 Chain (1); Transmembrane (7) TRANSMEM 5 25 Helical; Name=1. {ECO:0000255}.; TRANSMEM 32 52 Helical; Name=2. {ECO:0000255}.; TRANSMEM 71 91 Helical; Name=3. {ECO:0000255}.; TRANSMEM 116 136 Helical; Name=4. {ECO:0000255}.; TRANSMEM 161 181 Helical; Name=5. {ECO:0000255}.; TRANSMEM 187 207 Helical; Name=6. {ECO:0000255}.; TRANSMEM 214 234 Helical; Name=7. {ECO:0000255}. FUNCTION: Potential subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral proteins such as Notch receptors and APP (amyloid-beta precursor protein). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Potential component of the gamma-secretase complex. {ECO:0000250}. +Q9D416 AR13A_MOUSE ADP-ribosylation factor-like protein 13A 372 43,463 Chain (1); Nucleotide binding (3); Sequence conflict (1) +Q640N2 AR13B_MOUSE ADP-ribosylation factor-like protein 13B (ADP-ribosylation factor-like protein 2-like 1) (ARL2-like protein 1) (Protein hennin) 427 48,144 Chain (1); Coiled coil (1); Compositional bias (1); Lipidation (2); Modified residue (1); Mutagenesis (2); Nucleotide binding (3); Sequence conflict (1) FUNCTION: Cilium-specific protein required to control the microtubule-based, ciliary axoneme structure. May act by maintaining the association between IFT subcomplexes A and B. Binds GTP but is not able to hydrolyze it; the GTPase activity remains unclear. Required to pattern the neural tube. Involved in cerebral cortex development: required for the initial formation of a polarized radial glial scaffold, the first step in the construction of the cerebral cortex, by regulating ciliary signaling (PubMed:23817546). Regulates the migration and placement of postmitotic interneurons in the developing cerebral cortex (PubMed:23153492). {ECO:0000269|PubMed:17488627, ECO:0000269|PubMed:21539826, ECO:0000269|PubMed:21976698, ECO:0000269|PubMed:22554696, ECO:0000269|PubMed:23014696, ECO:0000269|PubMed:23153492, ECO:0000269|PubMed:23817546}. PTM: Sumoylation is required for PKD2 entry into cilium. {ECO:0000250}. SUBCELLULAR LOCATION: Cell projection, cilium membrane {ECO:0000269|PubMed:17488627, ECO:0000269|PubMed:20231383, ECO:0000269|PubMed:21976698, ECO:0000269|PubMed:23153492, ECO:0000269|PubMed:23817546, ECO:0000269|PubMed:24120134, ECO:0000269|PubMed:24339792}; Lipid-anchor {ECO:0000269|PubMed:17488627, ECO:0000269|PubMed:20231383, ECO:0000269|PubMed:21976698, ECO:0000269|PubMed:23153492, ECO:0000269|PubMed:23817546, ECO:0000269|PubMed:24120134, ECO:0000269|PubMed:24339792}. Cell projection, cilium {ECO:0000269|PubMed:25138100}. Note=Associates to the cilium membrane via palmitoylation. Localizes to proximal ciliary membranes, to an inversin-like subciliary membrane compartment, excluding the transition zone. SUBUNIT: Monomer. Interacts with IFT complex B components IFT46 and IFT74 (By similarity). Interacts with PIFO. {ECO:0000250, ECO:0000269|PubMed:20643351}. TISSUE SPECIFICITY: Cilium-specific protein. Expressed in neuroepithelial cells and developing radial glia of the developing cerebral cortex: present in both neuroepithelial and radial progenitor cells. In radial progenitors, found in the apical, cell soma domains of these cells (at protein level). Expressed in the primary cilia of postmitotic cortical neurons during embryonic and postnatal development. {ECO:0000269|PubMed:23153492, ECO:0000269|PubMed:23817546}. +Q9D385 AR2BP_MOUSE ADP-ribosylation factor-like protein 2-binding protein (ARF-like 2-binding protein) (Binder of ARF2 protein 1) 163 18,754 Alternative sequence (2); Chain (1) FUNCTION: Together with ARL2, plays a role in the nuclear translocation, retention and transcriptional activity of STAT3. May play a role as an effector of ARL2 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23849777}. Mitochondrion intermembrane space {ECO:0000269|PubMed:23849777}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:23849777}. Note=Detected in the midbody matrix. Not detected in the Golgi, nucleus and on the mitotic spindle. Centrosome-associated throughout the cell cycle. Not detected to interphase microtubules (By similarity). The complex formed with ARL2BP, ARL2 and SLC25A4 is expressed in mitochondria. In retina photoreceptor cells, localized in the distal connecting cilia, basal body, ciliary-associated centriole, and ciliary rootlet. Interaction with ARL2 may be required for cilia basal body localization (By similarity). {ECO:0000250}. SUBUNIT: Interacts with GTP bound ARL2 and ARL3; the complex ARL2-ARL2BP as well as ARL2BP alone, binds to ANT1. Interaction with ARL2 may be required for targeting to cilia basal body (By similarity). Interacts with STAT3; interaction is enhanced with ARL2. Found in a complex with ARL2BP, ARL2 and SLC25A6 (By similarity). Found in a complex with ARL2, ARL2BP and SLC25A4. Interacts with STAT2, STAT3 and STAT4. {ECO:0000250, ECO:0000269|PubMed:11809823, ECO:0000269|PubMed:18234692}. TISSUE SPECIFICITY: Widely expressed, with most abundant activity in brain, especially in hippocampus and cortex. Also expressed in lung, cerebellum, liver, kidney, retina, spleen, muscle and heart (at protein level). {ECO:0000269|PubMed:10488091, ECO:0000269|PubMed:11809823, ECO:0000269|PubMed:18234692, ECO:0000269|PubMed:23849777}. +Q8R2N1 AQP3_MOUSE Aquaporin-3 (AQP-3) (Aquaglyceroporin-3) 292 31,568 Chain (1); Erroneous initiation (1); Glycosylation (1); Motif (2); Sequence conflict (3); Topological domain (7); Transmembrane (6) TRANSMEM 29 49 Helical. {ECO:0000255}.; TRANSMEM 54 74 Helical. {ECO:0000255}.; TRANSMEM 110 130 Helical. {ECO:0000255}.; TRANSMEM 158 178 Helical. {ECO:0000255}.; TRANSMEM 189 209 Helical. {ECO:0000255}.; TRANSMEM 245 265 Helical. {ECO:0000255}. TOPO_DOM 1 28 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 50 53 Extracellular. {ECO:0000255}.; TOPO_DOM 75 109 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 131 157 Extracellular. {ECO:0000255}.; TOPO_DOM 179 188 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 210 244 Extracellular. {ECO:0000255}.; TOPO_DOM 266 292 Cytoplasmic. {ECO:0000255}. FUNCTION: Water channel required to promote glycerol permeability and water transport across cell membranes. Acts as a glycerol transporter in skin and plays an important role in regulating SC (stratum corneum) and epidermal glycerol content. Involved in skin hydration, wound healing, and tumorigenesis. Provides kidney medullary collecting duct with high permeability to water, thereby permitting water to move in the direction of an osmotic gradient. Slightly permeable to urea and may function as a water and urea exit mechanism in antidiuresis in collecting duct cells. It may play an important role in gastrointestinal tract water transport and in glycerol metabolism. {ECO:0000269|PubMed:12771381, ECO:0000269|PubMed:17429015}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. DOMAIN: Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA). TISSUE SPECIFICITY: Renal medulla and colon. Predominantly in the inner medulla. Expressed in basal layer of epidermal keratinocytes. +Q921W0 CHM1A_MOUSE Charged multivesicular body protein 1a (Chromatin-modifying protein 1a) (CHMP1a) 196 21,608 Chain (1); Coiled coil (2); Modified residue (3); Motif (1) FUNCTION: Probable peripherally associated component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis. ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. Involved in cytokinesis. Involved in recruiting VPS4A and/or VPS4B to the midbody of dividing cells. May also be involved in chromosome condensation. Targets the Polycomb group (PcG) protein BMI1/PCGF4 to regions of condensed chromatin. May play a role in stable cell cycle progression and in PcG gene silencing (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11559747}. Endosome membrane {ECO:0000269|PubMed:11559747}; Peripheral membrane protein {ECO:0000269|PubMed:11559747}. Nucleus matrix {ECO:0000269|PubMed:11559747}. Note=The cytoplasmic form is partially membrane-associated and localizes to early endosomes. The nuclear form remains associated with the chromosome scaffold during mitosis. On overexpression, it localizes to nuclear bodies characterized by nuclease-resistant condensed chromatin. SUBUNIT: Probable peripherally associated component of the endosomal sorting required for transport complex III (ESCRT-III). ESCRT-III components are thought to multimerize to form a flat lattice on the perimeter membrane of the endosome. Several assembly forms of ESCRT-III may exist that interact and act sequentially. Self-associates. Interacts with CHMP1B. Interacts with VPS4A. Interacts with VPS4B. Interacts with PHF1. Interacts with IST1. Interacts with MITD1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in adult heart, kidney and liver. Expressed at lower levels in adult colon, spleen, lung, brain, testis and muscle. Also expressed in myoblasts and embryo fibroblasts. {ECO:0000269|PubMed:11559747}. +Q8BJF9 CHM2B_MOUSE Charged multivesicular body protein 2b (Chromatin-modifying protein 2b) (CHMP2b) 213 23,935 Chain (1); Coiled coil (1); Initiator methionine (1); Modified residue (2); Motif (1); Sequence conflict (1) FUNCTION: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis. ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Late endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. SUBUNIT: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III). ESCRT-III components are thought to multimerize to form a flat lattice on the perimeter membrane of the endosome. Several assembly forms of ESCRT-III may exist that interact and act sequentially. Interacts with CHMP2A. Interacts with VPS4A. Interacts with VPS4B; the interaction is direct (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: In brain, it is expressed in all neuronal populations with a relatively enhanced expression in the hippocampus, frontal and temporal lobes and in both granule and Purkinje cells of the cerebellum. Not expressed in astrocytes or oligodendrocytes. {ECO:0000269|PubMed:16041373}. +Q9D8B3 CHM4B_MOUSE Charged multivesicular body protein 4b (Chromatin-modifying protein 4b) (CHMP4b) 224 24,936 Chain (1); Coiled coil (1); Erroneous initiation (1); Erroneous termination (1); Initiator methionine (1); Modified residue (5); Region (2); Sequence conflict (1) FUNCTION: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis. Together with SPAST, the ESCRT-III complex promotes nuclear envelope sealing and mitotic spindle disassembly during late anaphase. Plays a role in the endosomal sorting pathway. ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. When overexpressed, membrane-assembled circular arrays of CHMP4B filaments can promote or stabilize negative curvature and outward budding. CHMP4A/B/C are required for the exosomal release of SDCBP, CD63 and syndecan. {ECO:0000250|UniProtKB:Q9H444}. PTM: ISGylated. Isgylation weakens its interaction with VPS4A (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9H444}. Late endosome membrane {ECO:0000250|UniProtKB:Q9H444}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9H444}. Midbody {ECO:0000250|UniProtKB:Q9H444}. Nucleus envelope {ECO:0000250|UniProtKB:Q9H444}. Note=Recruited to the nuclear envelope by CHMP7 during late anaphase. Localizes transiently to the midbody arms immediately before abscission. {ECO:0000250|UniProtKB:Q9H444}. SUBUNIT: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III). ESCRT-III components are thought to multimerize to form a flat lattice on the perimeter membrane of the endosome. Several assembly forms of ESCRT-III may exist that interact and act sequentially. Interacts with CHMP6 and CHMP4C. Interacts with PDCD6IP; the interaction is direct. Interacts with VPS4A; the interaction is direct. Interacts with VPS4B; the interaction is direct. Interacts with CHMP7. Interacts with CFTR; the interaction requires misfolded CFTR. Interacts with PTPN23 (By similarity). {ECO:0000250|UniProtKB:Q9H444}. DOMAIN: The acidic C-terminus and the basic N-termminus are thought to render the protein in a closed, soluble and inactive conformation through an autoinhibitory intramolecular interaction. The open and active conformation, which enables membrane binding and oligomerization, is achieved by interaction with other cellular binding partners, probably including other ESCRT components (By similarity). {ECO:0000250}. +Q9D7F7 CHM4C_MOUSE Charged multivesicular body protein 4c (Chromatin-modifying protein 4c) (CHMP4c) 232 26,280 Chain (1); Coiled coil (2); Modified residue (1); Region (2); Sequence conflict (1) FUNCTION: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis. Key component of the cytokinesis checkpoint, a process required to delay abscission to prevent both premature resolution of intercellular chromosome bridges and accumulation of DNA damage: upon phosphorylation by AURKB, together with ZFYVE19/ANCHR, retains abscission-competent VPS4 (VPS4A and/or VPS4B) at the midbody ring until abscission checkpoint signaling is terminated at late cytokinesis. Deactivation of AURKB results in dephosphorylation of CHMP4C followed by its dissociation from ANCHR and VPS4 and subsequent abscission. ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. CHMP4A/B/C are required for the exosomal release of SDCBP, CD63 and syndecan (By similarity). {ECO:0000250|UniProtKB:Q96CF2}. PTM: Phosphorylated at Ser-210 by AURKB during cytokinesis: together with ZFYVE19/ANCHR, phosphorylated CHMP4C retains abscission-competent VPS4 (VPS4A and/or VPS4B) at the midbody ring until abscission checkpoint signaling is terminated at late cytokinesis. {ECO:0000250|UniProtKB:Q96CF2}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Late endosome membrane {ECO:0000250|UniProtKB:Q96CF2}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q96CF2}. Midbody, Midbody ring {ECO:0000250|UniProtKB:Q96CF2}. Note=Localizes to the midbody during late cytokinesis. During its recruitment, localizes initially to the midbody arms, before being directed to the central region, the midbody ring, also called Flemming body. Phosphorylation at Ser-210 by AURKB triggers localization to midbody ring. {ECO:0000250|UniProtKB:Q96CF2}. SUBUNIT: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III). ESCRT-III components are thought to multimerize to form a flat lattice on the perimeter membrane of the endosome. Several assembly forms of ESCRT-III may exist that interact and act sequentially. Self-associates. Interacts with CHMP2A. Interacts with CHMP4A. Interacts with CHMP4B. Interacts with CHMP6. Interacts with VPS4A. Interacts with PDCD6IP; the interaction is direct (By similarity). {ECO:0000250|UniProtKB:Q96CF2}. DOMAIN: The acidic C-terminus and the basic N-terminus are thought to render the protein in a closed, soluble and inactive conformation through an autoinhibitory intramolecular interaction. The open and active conformation, which enables membrane binding and oligomerization, is achieved by interaction with other cellular binding partners, probably including other ESCRT components (By similarity). {ECO:0000250}. +Q9D7S9 CHMP5_MOUSE Charged multivesicular body protein 5 (Chromatin-modifying protein 5) (SNF7 domain-containing protein 2) 219 24,576 Chain (1); Coiled coil (1); Modified residue (1) FUNCTION: Probable peripherally associated component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis. ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4 (By similarity). {ECO:0000250}. PTM: ISGylated. Isgylation inhibits its interaction with VTA1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Localizes to the midbody of dividing cells. Localized in two distinct rings on either side of the Fleming body (By similarity). {ECO:0000250}. SUBUNIT: Probable peripherally associated component of the endosomal sorting required for transport complex III (ESCRT-III). ESCRT-III components are thought to multimerize to form a flat lattice on the perimeter membrane of the endosome. Several assembly forms of ESCRT-III may exist that interact and act sequentially. Interacts with VTA1. Interacts with CHMP2A. Interacts with VTA1; the interaction involves soluble CHMP5 (By similarity). Interacts with NOD2 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9NZZ3}. +P0C0A3 CHMP6_MOUSE Charged multivesicular body protein 6 (Chromatin-modifying protein 6) 200 23,416 Chain (1); Coiled coil (1); Initiator methionine (1); Lipidation (1); Modified residue (2); Motif (1) FUNCTION: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis. ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. In the ESCRT-III complex, it probably serves as an acceptor for the ESCRT-II complex on endosomal membranes (By similarity). {ECO:0000250}. PTM: ISGylated in a CHMP5-dependent manner. Isgylation weakens its interaction with VPS4A (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}. Endosome membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Late endosome membrane {ECO:0000250}. Membrane {ECO:0000250|UniProtKB:Q96FZ7}; Lipid-anchor {ECO:0000250|UniProtKB:Q96FZ7}. Note=Localizes to endosomal membranes. {ECO:0000250}. SUBUNIT: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III). ESCRT-III components are thought to multimerize to form a flat lattice on the perimeter membrane of the endosome. Several assembly forms of ESCRT-III may exist that interact and act sequentially. Interacts with VPS4A; the interaction is direct. Interacts with VPS4B; the interaction is direct. Interacts with CHMP4A, CHMP4B and CHMP4C. Interacts with SNF8, VPS25 and VPS36 (By similarity). {ECO:0000250}. DOMAIN: The acidic C-terminus and the basic N-termminus are thought to render the protein in a closed, soluble and inactive conformation through an autoinhibitory intramolecular interaction. The open and active conformation, which enables membrane binding and oligomerization, is achieved by interaction with other cellular binding partners, probably including other ESCRT components (By similarity). {ECO:0000250}. +P61161 ARP2_MOUSE Actin-related protein 2 (Actin-like protein 2) 394 44,761 Chain (1); Modified residue (3); Nucleotide binding (3) FUNCTION: ATP-binding component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility. Seems to contact the pointed end of the daughter actin filament. In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA. The Arp2/3 complex promotes homologous recombination (HR) repair in response to DNA damage by promoting nuclear actin polymerization, leading to drive motility of double-strand breaks (DSBs). {ECO:0000250|UniProtKB:P61160}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P61160}. Cell projection {ECO:0000250|UniProtKB:P61160}. Nucleus {ECO:0000250|UniProtKB:P61160}. SUBUNIT: Component of the Arp2/3 complex composed of ACTR2/ARP2, ACTR3/ARP3, ARPC1B/p41-ARC, ARPC2/p34-ARC, ARPC3/p21-ARC, ARPC4/p20-ARC and ARPC5/p16-ARC. {ECO:0000250|UniProtKB:P61160}. +Q641P0 ARP3B_MOUSE Actin-related protein 3B (ARP3-beta) (Actin-like protein 3B) 418 47,580 Alternative sequence (1); Chain (1) FUNCTION: Plays a role in the organization of the actin cytoskeleton. May function as ATP-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. May decrease the metastatic potential of tumors (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell projection {ECO:0000250}. SUBUNIT: Interacts with the Arp2/3 complex composed of ARP2, ARP3, ARPC1B, ARPC1B/p41-ARC, ARPC2/p34-ARC, ARPC3/p21-ARC, ARPC4/p20-ARC and ARPC5/p16-ARC. {ECO:0000250}. +Q9CPW4 ARPC5_MOUSE Actin-related protein 2/3 complex subunit 5 (Arp2/3 complex 16 kDa subunit) (p16-ARC) 151 16,288 Chain (1); Initiator methionine (1); Modified residue (1); Sequence conflict (1) FUNCTION: Component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility. In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA. The Arp2/3 complex promotes homologous recombination (HR) repair in response to DNA damage by promoting nuclear actin polymerization, leading to drive motility of double-strand breaks (DSBs). {ECO:0000250|UniProtKB:O15511}. PTM: Polyubiquitinated by RNF128 with 'Lys-63'-linked chains, leading to proteasomal degradation. {ECO:0000250|UniProtKB:O15511}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O15511}. Cell projection {ECO:0000250|UniProtKB:O15511}. Nucleus {ECO:0000250|UniProtKB:O15511}. SUBUNIT: Component of the Arp2/3 complex composed of ACTR2/ARP2, ACTR3/ARP3, ARPC1B/p41-ARC, ARPC2/p34-ARC, ARPC3/p21-ARC, ARPC4/p20-ARC and ARPC5/p16-ARC. {ECO:0000250|UniProtKB:O15511}. +Q9D1P4 CHRD1_MOUSE Cysteine and histidine-rich domain-containing protein 1 (CHORD domain-containing protein 1) (CHORD-containing protein 1) (Chp-1) (Protein morgana) 331 37,351 Chain (1); Domain (3); Initiator methionine (1); Metal binding (16); Modified residue (3); Region (2) FUNCTION: Regulates centrosome duplication, probably by inhibiting the kinase activity of ROCK2. Proposed to act as co-chaperone for HSP90. May play a role in the regulation of NOD1 via a HSP90 chaperone complex. In vitro, has intrinsic chaperone activity. This function may be achieved by inhibiting association of ROCK2 with NPM1. Involved in stress response. Prevents tumorigenesis (By similarity). {ECO:0000250, ECO:0000269|PubMed:16083881, ECO:0000269|PubMed:20230755, ECO:0000269|PubMed:20493909}. SUBUNIT: Interacts with HSP90AA1, HSP90AB1 and PPP5C. Interacts with ROCK1 and ROCK2 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in spleen, lung and brain (at protein level). Expressed in proliferating myoblasts and its expression remained steady after. Its expression undergoes diurnal and circadian changes in hypothalamus. Highly expressed during the dark-light transition (ZT20.5 (zeitgeber time 20.5) and ZT2.5). {ECO:0000269|PubMed:12965203, ECO:0000269|PubMed:17253150}. +Q9JM76 ARPC3_MOUSE Actin-related protein 2/3 complex subunit 3 (Arp2/3 complex 21 kDa subunit) (p21-ARC) 178 20,525 Chain (1); Cross-link (1); Initiator methionine (1); Modified residue (3) FUNCTION: Component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility. In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA. The Arp2/3 complex promotes homologous recombination (HR) repair in response to DNA damage by promoting nuclear actin polymerization, leading to drive motility of double-strand breaks (DSBs). {ECO:0000250|UniProtKB:O15145}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O15145}. Cell projection {ECO:0000250|UniProtKB:O15145}. Nucleus {ECO:0000250|UniProtKB:O15145}. SUBUNIT: Component of the Arp2/3 complex composed of ACTR2/ARP2, ACTR3/ARP3, ARPC1B/p41-ARC, ARPC2/p34-ARC, ARPC3/p21-ARC, ARPC4/p20-ARC and ARPC5/p16-ARC. {ECO:0000250|UniProtKB:O15145}. +O35085 ARX_MOUSE Homeobox protein ARX (Aristaless-related homeobox) 564 58,490 Chain (1); Compositional bias (4); DNA binding (1); Motif (1); Sequence conflict (5) FUNCTION: Transcription factor required for normal brain development. May be important for maintenance of specific neuronal subtypes in the cerebral cortex and axonal guidance in the floor plate (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-ProRule:PRU00138}. +P50296 ARY3_MOUSE Arylamine N-acetyltransferase 3 (EC 2.3.1.5) (Arylamide acetylase 3) (N-acetyltransferase type 3) (NAT-3) 290 33,686 Active site (3); Binding site (2); Chain (1); Region (1) FUNCTION: Participates in the detoxification of a plethora of hydrazine and arylamine drugs. SUBCELLULAR LOCATION: Cytoplasm. +P98203 ARVC_MOUSE Armadillo repeat protein deleted in velo-cardio-facial syndrome homolog 962 105,066 Alternative sequence (2); Chain (1); Coiled coil (1); Modified residue (13); Motif (1); Repeat (10); Sequence caution (1); Sequence conflict (8) FUNCTION: Involved in protein-protein interactions at adherens junctions. {ECO:0000250}. SUBUNIT: Interacts (via the extreme C-terminus) with FRMPD2 (via the PDZ 2 domain). +Q9WV54 ASAH1_MOUSE Acid ceramidase (AC) (ACDase) (Acid CDase) (EC 3.5.1.23) (Acylsphingosine deacylase) (N-acylsphingosine amidohydrolase) [Cleaved into: Acid ceramidase subunit alpha; Acid ceramidase subunit beta] 394 44,670 Chain (2); Glycosylation (5); Signal peptide (1) FUNCTION: Hydrolyzes the sphingolipid ceramide into sphingosine and free fatty acid. SUBCELLULAR LOCATION: Lysosome. SUBUNIT: Heterodimer of one alpha and one beta subunit. +Q9D8Z1 ASCC1_MOUSE Activating signal cointegrator 1 complex subunit 1 (ASC-1 complex subunit p50) (Trip4 complex subunit p50) 356 41,280 Chain (1); Domain (1); Region (1) FUNCTION: Plays a role in DNA damage repair as component of the ASCC complex. Part of the ASC-1 complex that enhances NF-kappa-B, SRF and AP1 transactivation. In cells responding to gastrin-activated paracrine signals, it is involved in the induction of SERPINB2 expression by gastrin. May also play a role in the development of neuromuscular junction. {ECO:0000250|UniProtKB:Q8N9N2}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8N9N2}. Nucleus speckle {ECO:0000250|UniProtKB:Q8N9N2}. Note=Colocalizes with PRPF8 in nuclear speckles in the absence of DNA damage. {ECO:0000250|UniProtKB:Q8N9N2}. SUBUNIT: Identified in the ASCC complex that contains ASCC1, ASCC2 and ASCC3. Interacts directly with ASCC3. The ASCC complex interacts with ALKBH3. Part of the ASC-1 complex, that contains TRIP4, ASCC1, ASCC2 and ASCC3. Interacts with CSRP1. {ECO:0000250|UniProtKB:Q8N9N2}. TISSUE SPECIFICITY: Expressed in the spinal cord, brain, paraspinal ganglia, thyroid, and submandibular glands. {ECO:0000269|PubMed:26924529}. +Q5U464 ASAP3_MOUSE Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 3 (Development and differentiation-enhancing factor-like 1) 904 99,276 Chain (1); Coiled coil (2); Compositional bias (2); Domain (2); Repeat (2); Zinc finger (1) FUNCTION: Promotes cell proliferation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +Q91ZU0 ASB7_MOUSE Ankyrin repeat and SOCS box protein 7 (ASB-7) 318 35,984 Chain (1); Domain (1); Repeat (7); Sequence conflict (1) Protein modification; protein ubiquitination. FUNCTION: Probable substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000250}. SUBUNIT: Interacts with CUL5 and RNF7. {ECO:0000250}. DOMAIN: The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin-protein ligase complexes. {ECO:0000250}. +Q02067 ASCL1_MOUSE Achaete-scute homolog 1 (ASH-1) (mASH-1) (mASH1) 231 24,741 Chain (1); Compositional bias (2); Domain (1); Modified residue (1); Sequence conflict (2) FUNCTION: Transcription factor that plays a key role in neuronal differentiation: acts as a pioneer transcription factor, accessing closed chromatin to allow other factors to bind and activate neural pathways (PubMed:24243019). Directly binds the E box motif (5'-CANNTG-3') on promoters and promotes transcription of neuronal genes (PubMed:20107439, PubMed:24243019, PubMed:27281220). The combination of three transcription factors, ASCL1, POU3F2/BRN2 and MYT1L, is sufficient to reprogram fibroblasts and other somatic cells into induced neuronal (iN) cells in vitro (PubMed:20107439, PubMed:24243019, PubMed:27281220). Plays a role at early stages of development of specific neural lineages in most regions of the CNS, and of several lineages in the PNS (PubMed:8217843). Essential for the generation of olfactory and autonomic neurons (PubMed:8221886). Acts synergistically with FOXN4 to specify the identity of V2b neurons rather than V2a from bipotential p2 progenitors during spinal cord neurogenesis, probably through DLL4-NOTCH signaling activation (PubMed:16020526, PubMed:17728344). {ECO:0000269|PubMed:16020526, ECO:0000269|PubMed:17728344, ECO:0000269|PubMed:20107439, ECO:0000269|PubMed:24243019, ECO:0000269|PubMed:27281220, ECO:0000269|PubMed:8217843, ECO:0000269|PubMed:8221886}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:1576967}. SUBUNIT: Efficient DNA binding requires dimerization with another bHLH protein. Forms a heterodimer with TCF3. {ECO:0000250|UniProtKB:P50553}. TISSUE SPECIFICITY: Developing CNS and PNS at embryonic and post-natal stages. {ECO:0000269|PubMed:16020526, ECO:0000269|PubMed:8217843, ECO:0000269|PubMed:8424959}. +P34927 ASGR1_MOUSE Asialoglycoprotein receptor 1 (ASGP-R 1) (ASGPR 1) (Hepatic lectin 1) (HL-1) (mHL-1) 284 32,591 Binding site (3); Chain (1); Coiled coil (1); Disulfide bond (3); Domain (1); Glycosylation (3); Lipidation (1); Metal binding (11); Motif (1); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 40 60 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 39 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 61 284 Extracellular. {ECO:0000255}. FUNCTION: Mediates the endocytosis of plasma glycoproteins to which the terminal sialic acid residue on their complex carbohydrate moieties has been removed. The receptor recognizes terminal galactose and N-acetylgalactosamine units. After ligand binding to the receptor, the resulting complex is internalized and transported to a sorting organelle, where receptor and ligand are disassociated. The receptor then returns to the cell membrane surface. PTM: Phosphorylated on a cytoplasmic Ser residue. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. SUBUNIT: Interacts with LASS2. {ECO:0000250}. TISSUE SPECIFICITY: Expressed exclusively in hepatic parenchymal cells. +Q6X1Y6 ASIC3_MOUSE Acid-sensing ion channel 3 (ASIC3) (Amiloride-sensitive cation channel 3) (Dorsal root ASIC) (DRASIC) 530 58,704 Alternative sequence (2); Chain (1); Disulfide bond (7); Glycosylation (2); Motif (1); Site (1); Topological domain (3); Transmembrane (2) TRANSMEM 44 62 Helical. {ECO:0000255}.; TRANSMEM 441 460 Helical. {ECO:0000255}. TOPO_DOM 1 43 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 63 440 Extracellular. {ECO:0000255}.; TOPO_DOM 461 530 Cytoplasmic. {ECO:0000255}. FUNCTION: Cation channel with high affinity for sodium, which is gated by extracellular protons and inhibited by the diuretic amiloride. Generates a biphasic current with a fast inactivating and a slow sustained phase. In sensory neurons is proposed to mediate the pain induced by acidosis that occurs in ischemic, damaged or inflamed tissue. May be involved in hyperalgesia. May play a role in mechanoreception. Heteromeric channel assembly seems to modulate channel properties. {ECO:0000269|PubMed:11754838, ECO:0000269|PubMed:12060708, ECO:0000269|PubMed:14659506}. PTM: Phosphorylated by PKA. Phosphorylated by PKC. In vitro, PRKCABP/PICK-1 is necessary for PKC phosphorylation and activation of a ASIC3/ACCN3-ASIC2/ASIC2b channel, but does not activate a homomeric ASIC3/ACCN3 channel (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15051137}; Multi-pass membrane protein {ECO:0000269|PubMed:15051137}. Cytoplasm {ECO:0000269|PubMed:15051137}. Note=Cell surface expression may be stabilized by interaction with LIN7B and cytoplasmic retention by interaction with DLG4 (By similarity). In part cytoplasmic in cochlea cells. {ECO:0000250}. SUBUNIT: Homotrimer or heterotrimer with other ASIC proteins (By similarity). Interacts with DLG4 and ASIC2 (By similarity). Interacts with LIN7B, MAGI1/BAIAP1 and GOPC. Interacts with STOM; this regulates channel activity. {ECO:0000250, ECO:0000269|PubMed:15317815, ECO:0000269|PubMed:15471860, ECO:0000269|PubMed:22850675}. TISSUE SPECIFICITY: Expressed in liver, lung, kidney, testis, brain, eye and cochlea. Expressed in spiral ganglion and sensory hair cells of the organ of Corti in the cochlea (at protein level). Expressed in dorsal root ganglion innervating muscles and spinal chord. Expressed in peripheral sensory nerve termimals like nerves of the Meissner corpuscle, palisades of lanceolate nerve endings, site of mechanoreception in guard hair follicles, and Merkel cell-neurite complexes. {ECO:0000269|PubMed:11754838, ECO:0000269|PubMed:14659506, ECO:0000269|PubMed:15051137}. +P58242 ASM3B_MOUSE Acid sphingomyelinase-like phosphodiesterase 3b (ASM-like phosphodiesterase 3b) (EC 3.1.4.-) 456 51,600 Beta strand (18); Chain (1); Disulfide bond (2); Glycosylation (5); Helix (20); Metal binding (8); Mutagenesis (1); Signal peptide (1); Turn (2) FUNCTION: Lipid-modulating phosphodiesterase. Active on the surface of macrophages and dendritic cells and strongly influences macrophage lipid composition and membrane fluidity. Acts as a negative regulator of Toll-like receptor signaling (PubMed:26095358). {ECO:0000269|PubMed:26095358}. PTM: N-glycosylated. {ECO:0000269|PubMed:26095358}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Cell membrane; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:26095358}. SUBUNIT: Interacts with TLR4, TLR7, TLR8 and TLR9. {ECO:0000269|PubMed:26095358}. TISSUE SPECIFICITY: Macrophages and dendritic cells. {ECO:0000269|PubMed:26095358}. +Q9JME2 CHSTB_MOUSE Carbohydrate sulfotransferase 11 (EC 2.8.2.5) (Chondroitin 4-O-sulfotransferase 1) (Chondroitin 4-sulfotransferase 1) (C4S-1) (C4ST-1) (C4ST1) 352 41,632 Chain (1); Glycosylation (4); Nucleotide binding (2); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 17 37 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 16 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 38 352 Lumenal. {ECO:0000255}. FUNCTION: Catalyzes the transfer of sulfate to position 4 of the N-acetylgalactosamine (GalNAc) residue of chondroitin. Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage and is distributed on the surfaces of many cells and extracellular matrices. Can also sulfate Gal residues in desulfated dermatan sulfate. Preferentially sulfates in GlcA->GalNAc unit than in IdoA->GalNAc unit. Does not form 4, 6-di-O-sulfated GalNAc when chondroitin sulfate C is used as an acceptor. PTM: N-glycosylated; required for activity and stability. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Predominantly expressed in brain and kidney. Also expressed at weaker level in heart, spleen and lung. Expressed in developing chondrocytes. {ECO:0000269|PubMed:10722746}. +Q64191 ASPG_MOUSE N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase (EC 3.5.1.26) (Aspartylglucosaminidase) (AGA) (Glycosylasparaginase) (N4-(N-acetyl-beta-glucosaminyl)-L-asparagine amidase) [Cleaved into: Glycosylasparaginase alpha chain; Glycosylasparaginase beta chain] 346 37,022 Active site (1); Chain (2); Disulfide bond (4); Glycosylation (2); Region (2); Signal peptide (1) FUNCTION: Cleaves the GlcNAc-Asn bond which joins oligosaccharides to the peptide of asparagine-linked glycoproteins. {ECO:0000269|PubMed:8586423}. PTM: Cleaved into an alpha and beta chain by autocatalysis; this activates the enzyme (PubMed:8586423). The N-terminal residue of the beta subunit is responsible for the nucleophile hydrolase activity. {ECO:0000250|UniProtKB:P20933, ECO:0000269|PubMed:8586423}.; PTM: N-glycosylated. {ECO:0000250|UniProtKB:P20933}. SUBCELLULAR LOCATION: Lysosome. SUBUNIT: Heterotetramer of two alpha and two beta chains arranged as a dimer of alpha/beta heterodimers. {ECO:0000250|UniProtKB:P20933}. +Q2TA57 ASPH1_MOUSE Aspartate beta-hydroxylase domain-containing protein 1 (EC 1.14.11.-) 360 38,266 Alternative sequence (1); Chain (1); Compositional bias (1); Topological domain (2); Transmembrane (1) TRANSMEM 46 68 Helical. {ECO:0000255}. TOPO_DOM 1 45 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 69 360 Lumenal. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. +Q80VP9 ASPH2_MOUSE Aspartate beta-hydroxylase domain-containing protein 2 (EC 1.14.11.-) 343 38,731 Binding site (3); Chain (1); Glycosylation (2); Metal binding (2); Region (1); Topological domain (2); Transmembrane (1) TRANSMEM 32 52 Helical. {ECO:0000255}. TOPO_DOM 1 31 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 53 343 Lumenal. {ECO:0000255}. FUNCTION: May function as 2-oxoglutarate-dependent dioxygenase. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. +Q62415 ASPP1_MOUSE Apoptosis-stimulating of p53 protein 1 (Protein phosphatase 1 regulatory subunit 13B) 1087 119,170 Chain (1); Compositional bias (2); Domain (1); Modified residue (5); Repeat (2) FUNCTION: Regulator that plays a central role in regulation of apoptosis via its interaction with p53/TP53. Regulates TP53 by enhancing the DNA binding and transactivation function of TP53 on the promoters of proapoptotic genes in vivo (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Predominantly cytoplasmic (By similarity). Some fraction is nuclear. {ECO:0000250}. SUBUNIT: Interacts with TP53. {ECO:0000250}. DOMAIN: The ankyrin repeats and the SH3 domain are required for a specific interactions with TP53. {ECO:0000250}. +P58686 CI016_MOUSE UPF0184 protein C9orf16 homolog 83 9,055 Chain (1); Coiled coil (1); Modified residue (1) +Q8CG79 ASPP2_MOUSE Apoptosis-stimulating of p53 protein 2 (Tumor suppressor p53-binding protein 2) (53BP2) (p53-binding protein 2) (p53BP2) 1128 125,301 Chain (1); Compositional bias (2); Domain (1); Frameshift (1); Modified residue (8); Motif (1); Region (2); Repeat (2); Sequence conflict (2) FUNCTION: Regulator that plays a central role in regulation of apoptosis and cell growth via its interactions. Regulates p53/TP53 by enhancing the DNA binding and transactivation function of p53/TP53 on the promoters of proapoptotic genes in vivo. Inhibits the ability of APPBP1 to conjugate NEDD8 to CUL1, and thereby decreases APPBP1 ability to induce apoptosis. Impedes cell cycle progression at G2/M. Its apoptosis-stimulating activity is inhibited by its interaction with DDX42 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000250}. Note=Predominantly found in the perinuclear region. Some small fraction is nuclear. {ECO:0000250}. SUBUNIT: Binds to the central domain of p53/TP53 as well as to BCL2. Interacts with protein phosphatase 1. Interacts with RELA NF-kappa-B subunit. This interaction probably prevents the activation of apoptosis, possibly by preventing its interaction with p53/TP53. Interacts with APC2 and APPBP1. Interacts with DDX42 (via the C-terminus); the interaction is not inhibited by TP53BP2 ubiquitination and is independent of p53/TP53 (By similarity). {ECO:0000250}. DOMAIN: The ankyrin repeats and the SH3 domain are required for a specific interactions with p53/TP53. {ECO:0000250}. +Q6DFW0 CI072_MOUSE Guanine nucleotide exchange C9orf72 homolog 481 54,278 Alternative sequence (1); Chain (1); Domain (3); Sequence conflict (1) FUNCTION: Component of the C9orf72-SMCR8 complex, a complex that has guanine nucleotide exchange factor (GEF) activity and regulates autophagy (PubMed:27193190, PubMed:27617292). In the complex, C9orf72 and SMCR8 probably constitute the catalytic subunits that promote the exchange of GDP to GTP, converting inactive GDP-bound RAB8A and RAB39B into their active GTP-bound form, thereby promoting autophagosome maturation (By similarity). The C9orf72-SMCR8 complex also acts as a regulator of autophagy initiation by interacting with the ATG1/ULK1 kinase complex and modulating its protein kinase activity (PubMed:27193190, PubMed:27617292). Positively regulates initiation of autophagy by regulating the RAB1A-dependent trafficking of the ATG1/ULK1 kinase complex to the phagophore which leads to autophagosome formation (By similarity). Acts as a regulator of mTORC1 signaling by promoting phosphorylation of mTORC1 substrates (PubMed:27875531). Plays a role in endosomal trafficking (PubMed:26989253). May be involved in regulating the maturation of phagosomes to lysosomes (PubMed:26989253). Regulates actin dynamics in motor neurons by inhibiting the GTP-binding activity of ARF6, leading to ARF6 inactivation (PubMed:27723745). This reduces the activity of the LIMK1 and LIMK2 kinases which are responsible for phosphorylation and inactivation of cofilin, leading to cofilin activation (PubMed:27723745). Positively regulates axon extension and axon growth cone size in spinal motor neurons (PubMed:27723745). Plays a role within the hematopoietic system in restricting inflammation and the development of autoimmunity (PubMed:27412785). {ECO:0000250|UniProtKB:Q96LT7, ECO:0000269|PubMed:26989253, ECO:0000269|PubMed:27193190, ECO:0000269|PubMed:27412785, ECO:0000269|PubMed:27617292, ECO:0000269|PubMed:27723745, ECO:0000269|PubMed:27875531}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24549040, ECO:0000269|PubMed:26408000, ECO:0000269|PubMed:27476503}. Cytoplasm {ECO:0000269|PubMed:24549040, ECO:0000269|PubMed:26408000, ECO:0000269|PubMed:27476503, ECO:0000269|PubMed:27617292}. Cytoplasm, P-body {ECO:0000250|UniProtKB:Q96LT7}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q96LT7}. Endosome {ECO:0000250|UniProtKB:Q96LT7}. Lysosome {ECO:0000250|UniProtKB:Q96LT7}. Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:Q96LT7}. Secreted {ECO:0000269|PubMed:24549040}. Cell projection, axon {ECO:0000250|UniProtKB:Q96LT7}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q96LT7}. Perikaryon {ECO:0000269|PubMed:26408000}. Note=Detected in the cytoplasm of neurons from brain tissue (By similarity). Detected in the nucleus in fibroblasts (By similarity). Associates with cytoplasmic stress granules following cellular stress (By similarity). During corticogenesis, transitions from being predominantly cytoplasmic to a more even nucleocytoplasmic distribution (PubMed:27476503). {ECO:0000250|UniProtKB:Q96LT7, ECO:0000269|PubMed:27476503}. SUBUNIT: Interacts with SMCR8; the interaction is direct (PubMed:27875531). Component of the C9orf72-SMCR8 complex, at least composed of C9orf72, SMCR8 and WDR41 (Probable). The C9orf72-SMCR8 complex associates with the ATG1/ULK1 kinase complex (By similarity). Interacts with ATG1/ULK1 kinase complex members ULK1, ATG13 and RB1CC1 (By similarity). Interacts with HNRNPA1, HNRNPA2B1 and UBQLN2 (By similarity). Interacts with small Rab GTPase RAB1A; the interaction mediates recruitment of RAB1A to the ATG1/ULK1 kinase complex (PubMed:24549040). Also interacts with small Rab GTPase RAB7A (PubMed:24549040). Interacts with cofilin (PubMed:27723745). Interacts with GTP-binding proteins ARF1 and ARF6 (PubMed:27723745). {ECO:0000250|UniProtKB:Q96LT7, ECO:0000269|PubMed:24549040, ECO:0000269|PubMed:27723745, ECO:0000269|PubMed:27875531}. TISSUE SPECIFICITY: Expressed in postnatal cerebellum and cortex (at protein level). Neuronal expression is detected in several regions of the adult brain and spinal cord (PubMed:26044557). Prominent expression also observed in embryonic and early postnatal neurons including retinal ganglion cells, sensory neurons in the olfactory epithelium and in dorsal root ganglia, and spinal motor neurons (PubMed:26044557). Expressed in the developing cerebral cortex, cerebellum, olfactory bulb, hippocampus and spinal cord in the embryo and in P0 cortical neurons and astrocytes (PubMed:27476503). Also expressed in non-neuronal tissues such as kidney and tooth (PubMed:26044557). In the spleen, highly expressed in myeloid cells compared to B cell and T cell populations where expression is much lower (PubMed:26989253). In the brain, highly expressed in microglia (PubMed:26989253). {ECO:0000269|PubMed:26044557, ECO:0000269|PubMed:26989253, ECO:0000269|PubMed:27476503}. +Q3UHX9 CI114_MOUSE Putative methyltransferase C9orf114 homolog (EC 2.1.1.-) (Centromere protein 32) (CENP-32) (Kinetochore-associated protein) (SPOUT domain-containing methyltransferase 1) 385 42,958 Alternative sequence (1); Chain (1); Sequence conflict (1) FUNCTION: Required for association of the centrosomes with the poles of the bipolar mitotic spindle during metaphase. Also involved in chromosome alignment. May promote centrosome maturation probably by recruiting A-kinase anchor protein AKAP9 to centrosomes in early mitosis. Binds specifically to miRNA MIR145 hairpin, regulates MIR145 expression at a postranscriptional level (By similarity). {ECO:0000250|UniProtKB:Q5T280}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q5T280}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q5T280}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q5T280}. Note=Associated with the outer kinetochore. {ECO:0000250|UniProtKB:Q5T280}. SUBUNIT: Interacts with INCA1. {ECO:0000250|UniProtKB:Q5T280}. +Q9CQC3 CI135_MOUSE Protein C9orf135 homolog 228 26,594 Chain (1); Topological domain (2); Transmembrane (1) TRANSMEM 123 139 Helical. {ECO:0000255}. TOPO_DOM 1 122 Extracellular. {ECO:0000255}.; TOPO_DOM 140 228 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q5VTT2}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:Q5VTT2}. SUBUNIT: Interacts with MYH9. Interacts with MYH10. {ECO:0000250|UniProtKB:Q5VTT2}. TISSUE SPECIFICITY: Highly expressed in the testis. Weakly or not expressed in embryonic stem cells. {ECO:0000269|PubMed:28345668}. +P16460 ASSY_MOUSE Argininosuccinate synthase (EC 6.3.4.5) (Citrulline--aspartate ligase) 412 46,584 Binding site (12); Chain (1); Modified residue (8); Nucleotide binding (2) Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. Nitrogen metabolism; urea cycle; (N(omega)-L-arginino)succinate from L-aspartate and L-citrulline: step 1/1. FUNCTION: One of the enzymes of the urea cycle, the metabolic pathway transforming neurotoxic amonia produced by protein catabolism into inocuous urea in the liver of ureotelic animals. Catalyzes the formation of arginosuccinate from aspartate, citrulline and ATP and together with ASL it is responsible for the biosynthesis of arginine in most body tissues. {ECO:0000250|UniProtKB:P00966}. PTM: Acetylated by CLOCK in a circadian manner which negatively regulates its enzyme activity. Deacetylated by histone deacetylases. {ECO:0000269|PubMed:28985504}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P00966}. SUBUNIT: Homotetramer. Interacts with NMRAL1 (By similarity). Interacts with CLOCK; in a circadian manner (PubMed:28985504). {ECO:0000250|UniProtKB:P00966, ECO:0000269|PubMed:28985504}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:1708740}. +Q99KN2 CIAO1_MOUSE Probable cytosolic iron-sulfur protein assembly protein CIAO1 (WD repeat-containing protein 39) 339 37,633 Chain (1); Repeat (7); Sequence conflict (2) FUNCTION: Key component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into extramitochondrial Fe/S proteins (By similarity). As a CIA complex component, interacts specifically with CIAO2A or CIAO2B and MMS19 to assist different branches of iron-sulfur protein assembly, depending of its interactors. The complex CIAO1:CIAO2B:MMS19 binds to and facilitates the assembly of most cytosolic-nuclear Fe/S proteins. CIAO1:CIAO2A specifically matures ACO1 and stabilizes IREB2 (By similarity). Seems to specifically modulate the transactivation activity of WT1. As part of the mitotic spindle-associated MMXD complex it may play a role in chromosome segregation (By similarity). {ECO:0000250|UniProtKB:O76071, ECO:0000255|HAMAP-Rule:MF_03037}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O76071}. SUBUNIT: Component of the CIA complex. Interacts with CIAO2A and forms a complex with CIAO2B and MMS19; the interactions with CIAO2A and CIAO2B are mutually exclusive (PubMed:23891004) (By similarity). Interacts with CHD1L, ERCC2, IREB2 and POLD1 (By similarity). Component of the MMXD complex, which includes CIAO1, ERCC2, CIAO2B, MMS19 and SLC25A5. Interacts with WT1 (By similarity). Component of the CIA complex. Interacts with CIAO2A and forms a complex with CIAO2B and MMS19; the interactions with CIAO2A and CIAO2B are mutually exclusive. Interacts with CHD1L, ERCC2, IREB2 and POLD1. Component of the MMXD complex, which includes CIAO1, ERCC2, CIAO2B, MMS19 and SLC25A5. Interacts with WT1. Interacts with CIAO3 (By similarity). {ECO:0000250|UniProtKB:O76071, ECO:0000255|HAMAP-Rule:MF_03037, ECO:0000269|PubMed:23891004}. +Q3TQ03 CIART_MOUSE Circadian-associated transcriptional repressor (ChIP-derived repressor of network oscillator) (Chrono) (Computationally highlighted repressor of the network oscillator) 375 40,408 Chain (1); Compositional bias (2); Sequence conflict (1) FUNCTION: Transcriptional repressor which forms a negative regulatory component of the circadian clock and acts independently of the circadian transcriptional repressors: CRY1, CRY2 and BHLHE41. In a histone deacetylase-dependent manner represses the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer. Abrogates the interaction of ARNTL/BMAL1 with the transcriptional coactivator CREBBP and can repress the histone acetyl-transferase activity of the CLOCK-ARNTL/BMAL1 heterodimer, reducing histone acetylation of its target genes. Rhythmically binds the E-box elements (5'-CACGTG-3') on circadian gene promoters and its occupancy shows circadian oscillation antiphasic to ARNTL/BMAL1. Interacts with the glucocorticoid receptor (NR3C1) and contributes to the repressive function in the glucocorticoid response. {ECO:0000269|PubMed:24385426, ECO:0000269|PubMed:24736997, ECO:0000269|PubMed:24737000}. SUBCELLULAR LOCATION: Nucleus. Nucleus, PML body. Note=Co-localizes with the CLOCK-ARNTL/BMAL1 heterodimer in the PML body. SUBUNIT: Interacts with ARNTL/BMAL1, PER2, CRY2, BHLHE41, HDAC1 NR3C1. {ECO:0000269|PubMed:24385426, ECO:0000269|PubMed:24736997, ECO:0000269|PubMed:24737000}. +Q9Z309 CIB2_MOUSE Calcium and integrin-binding family member 2 (Kinase-interacting protein 2) (KIP 2) 187 21,704 Calcium binding (2); Chain (1); Domain (3) FUNCTION: Calcium-binding protein critical for proper photoreceptor cell maintenance and function. Plays a role in intracellular calcium homeostasis by decreasing ATP-induced calcium release (PubMed:23023331). May be involved in the mechanotransduction process (By similarity). {ECO:0000250, ECO:0000269|PubMed:23023331}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23023331}. Cell projection, stereocilium {ECO:0000269|PubMed:23023331}. Photoreceptor inner segment {ECO:0000269|PubMed:23023331}. Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:23023331}. Cell membrane, sarcolemma {ECO:0000269|PubMed:18611855}. Note=Colocalized with ITGA7 at the myotendinous junctions (MTJ) and at the neuromuscular junctions (NMJ) (PubMed:18611855). Localizes in the cuticular plate along and at the tip of the stereocilia of vestibular sensory hair cells (By similarity). {ECO:0000250|UniProtKB:O75838, ECO:0000269|PubMed:18611855, ECO:0000269|PubMed:23023331}. SUBUNIT: Homodimer (By similarity). Interacts with WHRN and MYO7A (By similarity). Interacts with ITGA2B (via C-terminus cytoplasmic tail region); this interaction is stabilized/increased in a calcium and magnesium-dependent manner (PubMed:18611855). Interacts with ITGA7 (via C-terminus cytoplasmic tail region); this interaction is stabilized/increased in a calcium and magnesium-dependent manner (PubMed:18989529). {ECO:0000250|UniProtKB:O75838, ECO:0000269|PubMed:18611855, ECO:0000269|PubMed:18989529}. TISSUE SPECIFICITY: Expressed in the supporting cells in both the organ of Corti and the vestibular sensory epithelia. Expressed in inner and outer segments of photoreceptor cells, as well as in the pigmented epithelium. Also observed in the inner and outer plexiform layers and in the ganglion cell layer (at protein level) (PubMed:23023331). Widely expressed (PubMed:23023331). Strongly expressed in skeletal muscles, brain, kidney and liver (PubMed:23023331). Also expressed in the skeletal muscle, retina and cochlea (PubMed:18611855, PubMed:23023331). Expressed in megakaryocytes and endothelial cells (PubMed:18989529). {ECO:0000269|PubMed:18611855, ECO:0000269|PubMed:18989529, ECO:0000269|PubMed:23023331}. +O70303 CIDEB_MOUSE Cell death activator CIDE-B (Cell death-inducing DFFA-like effector B) 219 24,800 Chain (1); Domain (1); Modified residue (1); Sequence conflict (2) FUNCTION: Activates apoptosis. SUBUNIT: Inhibited by DFFB. Interacts with DFFA and DFFB (By similarity). {ECO:0000250}. +P56198 CIDEC_MOUSE Cell death activator CIDE-3 (Cell death-inducing DFFA-like effector protein C) (Fat-specific protein FSP27) 239 27,324 Beta strand (4); Chain (1); Domain (1); Helix (2); Mutagenesis (16); Sequence conflict (1); Turn (1) FUNCTION: Binds to lipid droplets and regulates their enlargement, thereby restricting lipolysis and favoring storage. At focal contact sites between lipid droplets, promotes directional net neutral lipid transfer from the smaller to larger lipid droplets. The transfer direction may be driven by the internal pressure difference between the contacting lipid droplet pair. Its role in neutral lipid transfer and lipid droplet enlargement is activated by the interaction with PLIN1. May act as a CEBPB coactivator in the white adipose tissue to control the expression of a subset of CEBPB downstream target genes, including SOCS1, SOCS3, TGFB1, TGFBR1, ID2 and XDH. When overexpressed in preadipocytes, induces apoptosis or increases cell susceptibility to apoptosis induced by serum deprivation or TGFB treatment. As mature adipocytes, that express high CIDEC levels, are quite resistant to apoptotic stimuli, the physiological significance of its role in apoptosis is unclear. May play a role in the modulation of the response to osmotic stress by preventing NFAT5 to translocate into the nucleus and activate its target genes expression. {ECO:0000269|PubMed:18334488, ECO:0000269|PubMed:22144693, ECO:0000269|PubMed:22245780, ECO:0000269|PubMed:23481402}. PTM: Ubiquitinated and targeted to proteasomal degradation, resulting in a short half-life (about 15 minutes in 3T3-L1 cells). Protein stability depends on triaclyglycerol synthesis, fatty acid availability and lipid droplet formation. {ECO:0000269|PubMed:20089860}. SUBCELLULAR LOCATION: Lipid droplet. Endoplasmic reticulum. Nucleus. Note=Diffuses quickly on lipid droplet surface, but becomes trapped and clustered at lipid droplet contact sites, thereby enabling its rapid enrichment at lipid droplet contact sites. SUBUNIT: Homodimer. Interacts with CIDEA. Interacts with NFAT5; this interaction is direct and retains NFAT5 in the cytoplasm (By similarity). Interacts with CEBPB. Interacts with PLIN1. {ECO:0000250, ECO:0000269|PubMed:22245780, ECO:0000269|PubMed:23481402}. DOMAIN: The CIDE-N domain is involved in homodimerization which is crucial for its function in promoting lipid exchange and transfer. {ECO:0000269|PubMed:23481402}. TISSUE SPECIFICITY: Expressed almost exclusively in adipose tissue, including subcutaneous and epididymal white adipose tissue (at protein level). Although abundantly present in brown adipose tissue at the mRNA level, the protein is almost undetectable in this tissue (PubMed:18654663), or at moderate levels (PubMed:22245780, PubMed:12910269). Expressed in the mammary gland, in stromal adipose tissue, but becomes undetectable at the end of pregnancy and during lactation (at protein level). Expressed at low levels in skeletal muscle and heart. {ECO:0000269|PubMed:12910269, ECO:0000269|PubMed:1339452, ECO:0000269|PubMed:18654663, ECO:0000269|PubMed:22245780, ECO:0000269|PubMed:23233732}. +Q66K08 CILP1_MOUSE Cartilage intermediate layer protein 1 (CILP-1) [Cleaved into: Cartilage intermediate layer protein 1 C1; Cartilage intermediate layer protein 1 C2] 1184 132,334 Chain (3); Disulfide bond (4); Domain (2); Frameshift (1); Glycosylation (8); Sequence conflict (4); Signal peptide (1) FUNCTION: Probably plays a role in cartilage scaffolding. May act by antagonizing TGF-beta1 (TGFB1) and IGF1 functions. Has the ability to suppress IGF1-induced proliferation and sulfated proteoglycan synthesis, and inhibits ligand-induced IGF1R autophosphorylation. May inhibit TGFB1-mediated induction of cartilage matrix genes via its interaction with TGFB1. Overexpression may lead to impair chondrocyte growth and matrix repair and indirectly promote inorganic pyrophosphate (PPi) supersaturation in aging and osteoarthritis cartilage (By similarity). {ECO:0000250}. PTM: Cleaved into 2 chains possibly by a furin-like protease upon or preceding secretion. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. SUBUNIT: Monomer. Interacts with TGFB1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in articular and meniscal cartilage (at protein level). Primarily localizes to the superficial and intermediate zones of articular cartilage (at protein level). {ECO:0000269|PubMed:21880736}. +D3Z7H8 CILP2_MOUSE Cartilage intermediate layer protein 2 [Cleaved into: Cartilage intermediate layer protein 2 C1; Cartilage intermediate layer protein 2 C2] 1162 125,934 Chain (3); Disulfide bond (4); Domain (2); Glycosylation (1); Signal peptide (1) FUNCTION: May play a role in cartilage scaffolding. {ECO:0000250|UniProtKB:O75339}. PTM: May be cleaved into 2 chains possibly by a furin-like protease upon or preceding secretion. {ECO:0000305|PubMed:21880736}.; PTM: N-glycosylated. {ECO:0000269|PubMed:21880736}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q8IUL8}. TISSUE SPECIFICITY: Expressed in articulated and meniscal cartilage (at protein level). Also detected in heart, skeletal muscle and brain. Not detected in growth plate cartilage. {ECO:0000269|PubMed:21880736}. +Q9D0V8 CINP_MOUSE Cyclin-dependent kinase 2-interacting protein 212 24,104 Alternative sequence (4); Chain (1); Coiled coil (1); Modified residue (3) FUNCTION: Interacts with the components of the replication complex and 2 kinases, CDK2 and CDC7, thereby providing a functional and physical link between CDK2 and CDC7 during firing of the origins of replication. Regulates ATR-mediated checkpoint signaling (By similarity). {ECO:0000250}. PTM: Phosphorylated by CDC7 but not by CDK2. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Binds to nuclear under G1 conditions, and dissociates from chromatin with the start of DNA replication. {ECO:0000250}. SUBUNIT: Homodimer. Interacts with CDK2 and CDC7. Interacts with the components of the replication complex, MCM2, MCM3, MCM4, MCM5, MCM6, MCM7 and with ORC2-containing complexes (By similarity). Interacts with ATRIP (By similarity). Interacts with CEP152 (By similarity). {ECO:0000250}. +Q9DA19 CIR1_MOUSE Corepressor interacting with RBPJ 1 (CBF1-interacting corepressor) 450 51,838 Alternative sequence (1); Chain (1); Compositional bias (3); Cross-link (2); Modified residue (1); Motif (2); Region (2); Sequence caution (1); Sequence conflict (3) FUNCTION: Regulates transcription and acts as corepressor for RBPJ. Recruits RBPJ to the Sin3-histone deacetylase complex (HDAC). Required for RBPJ-mediated repression of transcription (By similarity). May modulate splice site selection during alternative splicing of pre-mRNAs. {ECO:0000250, ECO:0000269|PubMed:15652350}. PTM: Phosphorylated by NEK6. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:15652350}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Note=Colocalizes with NEK6 in the centrosome. {ECO:0000250}. SUBUNIT: Interacts with RP9, SNW1, SFRS1, SFRS2,U2AF1, RBPJ, SAP30, HDAC2 NKAP and NEK6. Interacts with Epstein-Barr virus RPMS1. Component of the histone deacetylase complex. Component of the Notch corepressor complex. Interacts with NKAPL (PubMed:25875095). {ECO:0000250|UniProtKB:Q86X95, ECO:0000269|PubMed:15652350, ECO:0000269|PubMed:25875095}. +P84078 ARF1_MOUSE ADP-ribosylation factor 1 181 20,697 Beta strand (6); Binding site (1); Chain (1); Helix (8); Initiator methionine (1); Lipidation (1); Modified residue (1); Nucleotide binding (2); Sequence conflict (3); Turn (1) FUNCTION: GTP-binding protein involved in protein trafficking among different compartments (PubMed:11950392). Modulates vesicle budding and uncoating within the Golgi complex. Deactivation induces the redistribution of the entire Golgi complex to the endoplasmic reticulum, suggesting a crucial role in protein trafficking. In its GTP-bound form, its triggers the association with coat proteins with the Golgi membrane. The hydrolysis of ARF1-bound GTP, which is mediated by ARFGAPs proteins, is required for dissociation of coat proteins from Golgi membranes and vesicles. The GTP-bound form interacts with PICK1 to limit PICK1-mediated inhibition of Arp2/3 complex activity; the function is linked to AMPA receptor (AMPAR) trafficking, regulation of synaptic plasicity of excitatory synapses and spine shrinkage during long-term depression (LTD). {ECO:0000269|PubMed:11950392}. SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasm, perinuclear region {ECO:0000250}. Cell junction, synapse, synaptosome {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250}. Membrane {ECO:0000250|UniProtKB:P84077}; Lipid-anchor {ECO:0000250|UniProtKB:P84077}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:11950392}; Lipid-anchor {ECO:0000305}. SUBUNIT: Interacts (when activated) with GGA1, GGA2 and GGA3; the interaction is required for proper subcellular location of GGA1, GGA2 and GGA3 (PubMed:11950392, PubMed:12679809). Interacts with ARHGAP21, ASAP2, HERC1, PRKCABP, PIP5K1B, TMED2, PSCD2, TMED10 and GRIA2 (PubMed:17347647). Interacts with ARFGAP1, which hydrolyzes GTP and thus, regulates its function. Interacts with PI4KB in the Golgi complex. Interacts with NCS1/FREQ in the Golgi and at the plasma membrane. Interacts with PLEKHA3. Interacts with PLEKHA8; the interaction, together with phosphatidylinositol 4-phosphate binding, is required for FAPP2-mediated glucosylceramide transfer activity. Interacts (activated) with PICK1 (via PDZ domain); the interaction blocks Arp2/3 complex inhibition. Interacts with IQSEC1 (By similarity). Interacts with C9orf72 (PubMed:27723745) (By similarity). {ECO:0000250|UniProtKB:P84077, ECO:0000250|UniProtKB:P84079, ECO:0000250|UniProtKB:P84080, ECO:0000269|PubMed:11950392, ECO:0000269|PubMed:12679809, ECO:0000269|PubMed:17347647, ECO:0000269|PubMed:27723745}. +Q91X46 ARHG3_MOUSE Rho guanine nucleotide exchange factor 3 524 59,526 Alternative sequence (2); Beta strand (6); Chain (1); Domain (2); Erroneous initiation (1); Helix (16); Modified residue (2); Sequence conflict (1); Turn (2) FUNCTION: Acts as guanine nucleotide exchange factor (GEF) for RhoA and RhoB GTPases. {ECO:0000269|PubMed:11839749}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11839749}. SUBUNIT: Interacts with RHOA and RHOB. +Q8BM75 ARI5B_MOUSE AT-rich interactive domain-containing protein 5B (ARID domain-containing protein 5B) (Developmentally and sexually retarded with transient immune abnormalities protein) (Desrt) (MRF1-like) (Modulator recognition factor protein 2) (MRF-2) 1188 131,837 Alternative sequence (4); Chain (1); Cross-link (17); Domain (1); Erroneous initiation (1); Erroneous termination (1); Frameshift (1); Modified residue (4); Sequence conflict (12) FUNCTION: Transcription coactivator that binds to the 5'-AATA[CT]-3' core sequence and plays a key role in adipogenesis and liver development. Acts by forming a complex with phosphorylated PHF2, which mediates demethylation at Lys-337, leading to target the PHF2-ARID5B complex to target promoters, where PHF2 mediates demethylation of dimethylated 'Lys-9' of histone H3 (H3K9me2), followed by transcription activation of target genes. The PHF2-ARID5B complex acts as a coactivator of HNF4A in liver (By similarity). Required for adipogenesis: regulates triglyceride metabolism in adipocytes by regulating expression of adipogenic genes. Overexpression leads to induction of smooth muscle marker genes, suggesting that it may also act as a regulator of smooth muscle cell differentiation and proliferation. {ECO:0000250, ECO:0000269|PubMed:12215486, ECO:0000269|PubMed:14651970, ECO:0000269|PubMed:17962384, ECO:0000269|PubMed:18070594, ECO:0000269|PubMed:19913508}. PTM: Methylation at Lys-337 prevents DNA-binding. Demethylation by PHF2 promotes recruitment of the PHF2-ARID5B complex to promoters (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355, ECO:0000269|PubMed:12215486}. DOMAIN: The ARID domain mediates the interaction with DNA. TISSUE SPECIFICITY: Widely expressed. Expressed in lung, heart, small intestine, kidney, muscle and brain. Also expressed in spleen, thymus, endocrine organs and in uterus and testis. {ECO:0000269|PubMed:11483573, ECO:0000269|PubMed:12215486}. +Q3UTH8 ARHG9_MOUSE Rho guanine nucleotide exchange factor 9 (Collybistin) (Rac/Cdc42 guanine nucleotide exchange factor 9) 516 60,927 Alternative sequence (4); Chain (1); Domain (3); Erroneous initiation (1); Modified residue (1); Region (1) FUNCTION: Acts as guanine nucleotide exchange factor (GEF) for CDC42. Promotes formation of GPHN clusters (By similarity). {ECO:0000250|UniProtKB:Q9QX73}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9QX73}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000269|PubMed:27609886}. SUBUNIT: Interacts with GPHN. {ECO:0000250|UniProtKB:Q9QX73}. TISSUE SPECIFICITY: Detected in embryonic and adult brain. {ECO:0000269|PubMed:11168555}. +Q99NG0 ARIP4_MOUSE Helicase ARIP4 (EC 3.6.4.12) (Androgen receptor-interacting protein 4) (RAD54-like protein 2) (Steroid receptor-interacting SNF2 domain-containing protein-like) 1466 162,540 Chain (1); Compositional bias (2); Cross-link (9); Domain (2); Modified residue (3); Motif (3); Mutagenesis (8); Nucleotide binding (1); Sequence conflict (2) FUNCTION: DNA helicase that modulates androgen receptor (AR)-dependent transactivation in a promoter-dependent manner. Not able to remodel mononucleosomes in vitro. Acts as an AR-coregulator in Sertoli cells. {ECO:0000269|PubMed:12058073, ECO:0000269|PubMed:16212558}. PTM: Sumoylated. {ECO:0000269|PubMed:16212558}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12058073, ECO:0000269|PubMed:15199138}. Note=Localizes in speckle-like nuclear compartments. SUBUNIT: Interacts with AR via its N-terminus. Interacts with DYRK1A. Binds DNA and mononucleosomes, but does not seem to form large multiprotein complexes. {ECO:0000269|PubMed:12058073, ECO:0000269|PubMed:15199138, ECO:0000269|PubMed:16212558}. DOMAIN: Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs are known to be important for the association with nuclear receptors. {ECO:0000250}. TISSUE SPECIFICITY: Expressed at relatively low level, with highest expression in testis, liver and kidney. In brain, it is expressed in hippocampal and cerebellar neurons. In testis, it is present at high level in Sertoli cell nuclei. Also present in Leydig cell (at protein level). {ECO:0000269|PubMed:15199138, ECO:0000269|PubMed:17003240}. +Q6P9R4 ARHGI_MOUSE Rho guanine nucleotide exchange factor 18 1405 155,982 Alternative sequence (3); Beta strand (9); Chain (1); Coiled coil (1); Compositional bias (2); Domain (2); Helix (3); Modified residue (4); Sequence conflict (3); Zinc finger (1) FUNCTION: Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPases. May play a role in actin cytoskeleton reorganization in different tissues since its activation induces formation of actin stress fibers. Also acts as a GEF for RAC1, inducing production of reactive oxygen species (ROS). Does not act as a GEF for CDC42. The G protein beta-gamma (Gbetagamma) subunits of heterotrimeric G proteins act as activators, explaining the integrated effects of LPA and other G-protein coupled receptor agonists on actin stress fiber formation, cell shape change and ROS production. Required for EPB41L4B-mediated regulation of the circumferential actomyosin belt in epithelial cells. {ECO:0000250|UniProtKB:Q6ZSZ5}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6ZSZ5}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q6ZSZ5}. Cell membrane {ECO:0000250|UniProtKB:Q6ZSZ5}. Apical cell membrane {ECO:0000250|UniProtKB:Q6ZSZ5}. Note=In unactivated eosinophils, distributed around the cell periphery in the perimembranous region (By similarity). In activated eosinophils, relocates to the tip of the nucleopod, a membrane structure formed during activation when the nucleus moves to one end of the cell, and is also concentrated in membrane protrusions at the opposite end of the cell (By similarity). Localizes to the apical cell membrane in epithelial cells (By similarity). {ECO:0000250|UniProtKB:Q6ZSZ5}. SUBUNIT: Interacts with SEPT9; interaction may inhibit GEF activity. Interacts with Gbetagamma subunits GNB1 and GNG2 (By similarity). Interacts with EPB41L4B. Interacts with PATJ (via C-terminus). {ECO:0000250|UniProtKB:Q6ZSZ5}. +Q9QXJ4 ARL10_MOUSE ADP-ribosylation factor-like protein 10 (ADP-ribosylation factor-like membrane-associated protein) 243 27,303 Chain (1); Nucleotide binding (3); Sequence conflict (1) +Q9D4P0 ARL5B_MOUSE ADP-ribosylation factor-like protein 5B (ADP-ribosylation factor-like protein 8) 179 20,375 Binding site (1); Chain (1); Erroneous initiation (3); Initiator methionine (1); Lipidation (1); Nucleotide binding (3) FUNCTION: Binds and exchanges GTP and GDP. {ECO:0000250}. +P63038 CH60_MOUSE 60 kDa heat shock protein, mitochondrial (EC 3.6.4.9) (60 kDa chaperonin) (Chaperonin 60) (CPN60) (HSP-65) (Heat shock protein 60) (HSP-60) (Hsp60) (Mitochondrial matrix protein P1) 573 60,955 Alternative sequence (1); Binding site (3); Chain (1); Cross-link (1); Modified residue (46); Nucleotide binding (1); Sequence caution (1); Sequence conflict (7); Transit peptide (1) FUNCTION: Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein. {ECO:0000250|UniProtKB:P10809}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:P10809}. SUBUNIT: Homoheptamer arranged in a ring structure. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. Interacts with 2 heptameric Hsp10 rings to form the symmetrical football complex (By similarity). Interacts with HRAS (PubMed:1347942). Interacts with ATAD3A. Interacts with ETFBKMT and METTL21B (By similarity). Interacts with MFHAS1 (By similarity). {ECO:0000250|UniProtKB:P10809, ECO:0000269|PubMed:1347942}. +Q62431 ARI3A_MOUSE AT-rich interactive domain-containing protein 3A (ARID domain-containing protein 3A) (B-cell regulator of IgH transcription) (Bright) (Dead ringer-like protein 1) 601 64,173 Chain (1); Compositional bias (7); Cross-link (4); Domain (2); Modified residue (8); Mutagenesis (13); Region (4); Sequence conflict (1) FUNCTION: Transcription factor involved in B-cell differentiation. Binds a VH promoter proximal site necessary for induced mu-heavy-chain transcription. Binds the minor groove of a restricted ATC sequence that is sufficient for nuclear matrix association. This sequence motif is present in matrix-associating regions (MARS) proximal to the promoter and flanking E mu. Activates E mu-driven transcription by binding these sites. May be involved in the control of cell cycle progression by the RB1/E2F1 pathway. {ECO:0000269|PubMed:11294836, ECO:0000269|PubMed:17312145, ECO:0000269|PubMed:8543152}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Shuttles between nucleus and cytoplasm. SUBUNIT: Homodimer. Heterodimer with ARID3B. Interacts with E2F1 (By similarity). Interacts with GTF2I and BTK. {ECO:0000250, ECO:0000269|PubMed:11120822, ECO:0000269|PubMed:15456761, ECO:0000269|PubMed:16738337}. TISSUE SPECIFICITY: B-cell specific in the adult. Expressed in B-cell progenitors, down-regulated in the immature B-cell stage, and is up-regulated again at later stages of B-lymphocyte differentiation. {ECO:0000269|PubMed:9590220}. +F8VPQ2 ARI4A_MOUSE AT-rich interactive domain-containing protein 4A (ARID domain-containing protein 4A) (Retinoblastoma-binding protein 1) 1261 142,055 Chain (1); Cross-link (3); Domain (1); Modified residue (5); Region (3); Sequence conflict (8) FUNCTION: DNA-binding protein which modulates activity of several transcription factors including RB1 (retinoblastoma-associated protein) and AR (androgen receptor) (PubMed:17043311, PubMed:23487765). May function as part of an mSin3A repressor complex (By similarity). Has no intrinsic transcriptional activity (PubMed:23487765). Plays a role in the regulation of epigenetic modifications at the PWS/AS imprinting center near the SNRPN promoter, where it might function as part of a complex with RB1 and ARID4B (PubMed:17043311). Involved in spermatogenesis, together with ARID4B, where it acts as a transcriptional coactivator for AR and enhances expression of genes required for sperm maturation (PubMed:23487765). Regulates expression of the tight junction protein CLDN3 in the testis, which is important for integrity of the blood-testis barrier (PubMed:23487765). Plays a role in myeloid homeostasis where it regulates the histone methylation state of bone marrow cells and expression of various genes involved in hematopoiesis (PubMed:18728284). May function as a leukemia suppressor (PubMed:18728284). {ECO:0000250|UniProtKB:P29374, ECO:0000269|PubMed:17043311, ECO:0000269|PubMed:18728284, ECO:0000269|PubMed:23487765}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|SAAS:SAAS00704572, ECO:0000305|PubMed:17043311, ECO:0000305|PubMed:23487765}. SUBUNIT: Identified in mSin3A corepressor complexes together with SIN3A, SIN3B, RBBP4, RBBP7, SAP30, BRMS1, HDAC1 and HDAC2 (By similarity). Interacts with BRMS1 (By similarity). Interacts with RB1 (By similarity). Interacts with ARID4B (PubMed:17043311). Interacts with AR (PubMed:23487765). {ECO:0000250|UniProtKB:P29374, ECO:0000269|PubMed:17043311, ECO:0000269|PubMed:23487765}. DOMAIN: The function of the chromodomain-like region is uncertain. One study suggests that it mediates binding to lysine-methlyated histone tails, with strongest affinity for H4K20me3 and H3K36me3. However, another study failed to find any interaction between this domain and histone H4K20me3 peptide. {ECO:0000250|UniProtKB:P29374}. TISSUE SPECIFICITY: Expressed in Sertoli cells of the testis. {ECO:0000269|PubMed:23487765}. +Q91YI0 ARLY_MOUSE Argininosuccinate lyase (ASAL) (EC 4.3.2.1) (Arginosuccinase) 464 51,739 Chain (1); Initiator methionine (1); Modified residue (4) Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. Nitrogen metabolism; urea cycle; L-arginine and fumarate from (N(omega)-L-arginino)succinate: step 1/1. PTM: Acetylation modifies enzyme activity in response to alterations of extracellular nutrient availability. Acetylation increased with trichostin A (TCA) or with nicotinamide (NAM). Glucose increases acetylation by about a factor of 3 with decreasing enzyme activity. Acetylation on Lys-288 is decreased on the addition of extra amino acids resulting in activation of enzyme activity (By similarity). {ECO:0000250}. SUBUNIT: Homotetramer. +Q8R3J5 CHAC1_MOUSE Glutathione-specific gamma-glutamylcyclotransferase 1 (Gamma-GCG 1) (EC 4.3.2.7) (Blocks Notch protein) (Botch) (Cation transport regulator-like protein 1) 223 24,547 Active site (1); Chain (1); Mutagenesis (1); Region (1); Sequence conflict (2) FUNCTION: Catalyzes the cleavage of glutathione into 5-oxo-L-proline and a Cys-Gly dipeptide. Acts specifically on glutathione, but not on other gamma-glutamyl peptides. Glutathione depletion is an important factor for apoptosis initiation and execution. Acts as a pro-apoptotic component of the unfolded protein response pathway by mediating the pro-apoptotic effects of the ATF4-ATF3-DDIT3/CHOP cascade (By similarity). Negative regulator of Notch signaling pathway involved in embryonic neurogenesis: acts by inhibiting Notch cleavage by furin, maintaining Notch in an immature inactive form, thereby promoting neurogenesis in embryos (PubMed:22445366). {ECO:0000250|UniProtKB:Q9BUX1, ECO:0000269|PubMed:22445366, ECO:0000269|PubMed:23070364}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9BUX1}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:22445366}. SUBUNIT: Interacts with NOTCH1 (via extracellular region). {ECO:0000269|PubMed:22445366}. TISSUE SPECIFICITY: Widely expressed, with high expression in forebrain and anterior spinal cord. Expressed at intermediate level in the dorsal aorta and heart. Present throughout adult brain (at protein level). {ECO:0000269|PubMed:22445366}. +Q9CQG1 CHAC2_MOUSE Putative glutathione-specific gamma-glutamylcyclotransferase 2 (Gamma-GCG 2) (EC 4.3.2.7) (Cation transport regulator-like protein 2) 178 20,153 Active site (1); Alternative sequence (1); Chain (1); Region (1); Sequence conflict (1) FUNCTION: Catalyzes the cleavage of glutathione into 5-oxo-L-proline and a Cys-Gly dipeptide (PubMed:27913623). Acts specifically on glutathione, but not on other gamma-glutamyl peptides (By similarity). {ECO:0000250|UniProtKB:Q8WUX2, ECO:0000269|PubMed:27913623}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8WUX2}. SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q8WUX2}. +Q3UJZ3 ARMC7_MOUSE Armadillo repeat-containing protein 7 198 21,639 Chain (1); Modified residue (1); Repeat (2); Sequence conflict (2) +Q9D2I5 ARMC9_MOUSE LisH domain-containing protein ARMC9 817 91,922 Alternative sequence (12); Chain (1); Coiled coil (1); Domain (1); Modified residue (1); Sequence conflict (5) FUNCTION: Required for ciliogenesis. {ECO:0000250|UniProtKB:E7F187}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q7Z3E5}. +A2AU72 ARMC3_MOUSE Armadillo repeat-containing protein 3 881 97,357 Alternative sequence (3); Chain (1); Compositional bias (1); Repeat (12) +Q9D1L0 CHCH2_MOUSE Coiled-coil-helix-coiled-coil-helix domain-containing protein 2 153 15,661 Chain (1); Disulfide bond (2); Domain (1); Motif (2) FUNCTION: Transcription factor. Binds to the oxygen responsive element of COX4I2 and activates its transcription under hypoxia conditions (4% oxygen), as well as normoxia conditions (20% oxygen). {ECO:0000250|UniProtKB:Q9Y6H1}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y6H1}. Mitochondrion {ECO:0000250|UniProtKB:Q9Y6H1}. Mitochondrion intermembrane space {ECO:0000250|UniProtKB:Q9Y6H1}. Note=Mainly localised in the intermembrane space. {ECO:0000250|UniProtKB:Q9Y6H1}. SUBUNIT: Interacts with RBPJ. {ECO:0000250|UniProtKB:Q9Y6H1}. +Q9CQP3 CHCH5_MOUSE Coiled-coil-helix-coiled-coil-helix domain-containing protein 5 110 12,326 Chain (1); Disulfide bond (4); Domain (2); Modified residue (1); Motif (4) SUBCELLULAR LOCATION: Mitochondrion intermembrane space {ECO:0000305}. SUBUNIT: Monomer. {ECO:0000250}. +Q8K2Q5 CHCH7_MOUSE Coiled-coil-helix-coiled-coil-helix domain-containing protein 7 85 10,102 Chain (1); Disulfide bond (2); Domain (1); Motif (2) SUBCELLULAR LOCATION: Mitochondrion intermembrane space {ECO:0000305}. SUBUNIT: Monomer. {ECO:0000250}. +Q8C6B9 AROS_MOUSE Active regulator of SIRT1 (40S ribosomal protein S19-binding protein 1) (RPS19-binding protein 1) (S19BP) 143 15,978 Chain (1); Modified residue (2); Natural variant (1) FUNCTION: Direct regulator of SIRT1. Enhances SIRT1-mediated deacetylation of p53/TP53, thereby participating in inhibition of p53/TP53-mediated transcriptional activity (By similarity). {ECO:0000250}. PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:16289379}. SUBUNIT: Interacts with SIRT1 (By similarity). Interacts with RPS19. {ECO:0000250, ECO:0000269|PubMed:16289379}. TISSUE SPECIFICITY: Widely expressed with higher levels in submaxillary gland and epididymis. {ECO:0000269|PubMed:16289379}. +Q8R2S9 ARP8_MOUSE Actin-related protein 8 624 70,546 Binding site (2); Chain (1); Modified residue (3); Nucleotide binding (1); Sequence conflict (1) FUNCTION: Plays an important role in the functional organization of mitotic chromosomes. Exhibits low basal ATPase activity, and unable to polymerize (By similarity). {ECO:0000250}.; FUNCTION: Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. Required for the recruitment of INO80 (and probably the INO80 complex) to sites of DNA damage Strongly prefer nucleosomes and H3-H4 tetramers over H2A-H2B dimers, suggesting it may act as a nucleosome recognition module within the complex (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}. Note=Specifically localizes to mitotic chromosomes. {ECO:0000250}. SUBUNIT: Component of the chromatin remodeling INO80 complex; specifically part of a complex module associated with the DBINO domain of INO80. Exists as monomers and dimers, but the dimer is most probably the biologically relevant form required for stable interactions with histones that exploits the twofold symmetry of the nucleosome core (By similarity). {ECO:0000250}. +Q91YI4 ARRB2_MOUSE Beta-arrestin-2 (Arrestin beta-2) 410 46,314 Alternative sequence (1); Chain (1); Modified residue (5); Motif (1); Mutagenesis (1); Region (2); Sequence conflict (3) FUNCTION: Functions in regulating agonist-mediated G-protein coupled receptor (GPCR) signaling by mediating both receptor desensitization and resensitization processes. During homologous desensitization, beta-arrestins bind to the GPRK-phosphorylated receptor and sterically preclude its coupling to the cognate G-protein; the binding appears to require additional receptor determinants exposed only in the active receptor conformation. The beta-arrestins target many receptors for internalization by acting as endocytic adapters (CLASPs, clathrin-associated sorting proteins) and recruiting the GPRCs to the adapter protein 2 complex 2 (AP-2) in clathrin-coated pits (CCPs). However, the extent of beta-arrestin involvement appears to vary significantly depending on the receptor, agonist and cell type. Internalized arrestin-receptor complexes traffic to intracellular endosomes, where they remain uncoupled from G-proteins. Two different modes of arrestin-mediated internalization occur. Class A receptors, like ADRB2, OPRM1, ENDRA, D1AR and ADRA1B dissociate from beta-arrestin at or near the plasma membrane and undergo rapid recycling. Class B receptors, like AVPR2, AGTR1, NTSR1, TRHR and TACR1 internalize as a complex with arrestin and traffic with it to endosomal vesicles, presumably as desensitized receptors, for extended periods of time. Receptor resensitization then requires that receptor-bound arrestin is removed so that the receptor can be dephosphorylated and returned to the plasma membrane. Mediates endocytosis of CCR7 following ligation of CCL19 but not CCL21. Involved in internalization of P2RY1, P2RY4, P2RY6 and P2RY11 and ATP-stimulated internalization of P2RY2. Involved in phosphorylation-dependent internalization of OPRD1 and subsequent recycling or degradation. Involved in ubiquitination of IGF1R. Beta-arrestins function as multivalent adapter proteins that can switch the GPCR from a G-protein signaling mode that transmits short-lived signals from the plasma membrane via small molecule second messengers and ion channels to a beta-arrestin signaling mode that transmits a distinct set of signals that are initiated as the receptor internalizes and transits the intracellular compartment. Acts as signaling scaffold for MAPK pathways such as MAPK1/3 (ERK1/2) and MAPK10 (JNK3). ERK1/2 and JNK3 activated by the beta-arrestin scaffold are largely excluded from the nucleus and confined to cytoplasmic locations such as endocytic vesicles, also called beta-arrestin signalosomes. Acts as signaling scaffold for the AKT1 pathway. GPCRs for which the beta-arrestin-mediated signaling relies on both ARRB1 and ARRB2 (codependent regulation) include ADRB2, F2RL1 and PTH1R. For some GPCRs the beta-arrestin-mediated signaling relies on either ARRB1 or ARRB2 and is inhibited by the other respective beta-arrestin form (reciprocal regulation). Increases ERK1/2 signaling in AGTR1- and AVPR2-mediated activation (reciprocal regulation). Involved in CCR7-mediated ERK1/2 signaling involving ligand CCL19. Is involved in type-1A angiotensin II receptor/AGTR1-mediated ERK activity. Is involved in type-1A angiotensin II receptor/AGTR1-mediated MAPK10 activity. Is involved in dopamine-stimulated AKT1 activity in the striatum by disrupting the association of AKT1 with its negative regulator PP2A. Involved in AGTR1-mediated chemotaxis. Appears to function as signaling scaffold involved in regulation of MIP-1-beta-stimulated CCR5-dependent chemotaxis. Involved in attenuation of NF-kappa-B-dependent transcription in response to GPCR or cytokine stimulation by interacting with and stabilizing CHUK. Suppresses UV-induced NF-kappa-B-dependent activation by interacting with CHUK. The function is promoted by stimulation of ADRB2 and dephosphorylation of ARRB2. Involved in IL8-mediated granule release in neutrophils (By similarity). Involved in p53/TP53-mediated apoptosis by regulating MDM2 and reducing the MDM2-mediated degradation of p53/TP53. May serve as nuclear messenger for GPCRs. Upon stimulation of OR1D2, may be involved in regulation of gene expression during the early processes of fertilization. Also involved in regulation of receptors other than GPCRs. Involved in endocytosis of TGFBR2 and TGFBR3 and down-regulates TGF-beta signaling such as NF-kappa-B activation. Involved in endocytosis of low-density lipoprotein receptor/LDLR. Involved in endocytosis of smoothened homolog/Smo, which also requires GRK2. Involved in endocytosis of SLC9A5. Involved in endocytosis of ENG and subsequent TGF-beta-mediated ERK activation and migration of epithelial cells. Involved in Toll-like receptor and IL-1 receptor signaling through the interaction with TRAF6 which prevents TRAF6 autoubiquitination and oligomerization required for activation of NF-kappa-B and JUN. Involved in insulin resistance by acting as insulin-induced signaling scaffold for SRC, AKT1 and INSR. Involved in regulation of inhibitory signaling of natural killer cells by recruiting PTPN6 and PTPN11 to KIR2DL1. Involved in the internalization of the atypical chemokine receptor ACKR3 (By similarity). {ECO:0000250, ECO:0000269|PubMed:12944399, ECO:0000269|PubMed:16051150, ECO:0000269|PubMed:17540773, ECO:0000269|PubMed:18337459, ECO:0000269|PubMed:18604210, ECO:0000269|PubMed:19122674}. PTM: Phosphorylated at Thr-383 in the cytoplasm; probably dephosphorylated at the plasma membrane. The phosphorylation does not regulate internalization and recycling of ADRB2, interaction with clathrin or AP2B1 (By similarity). {ECO:0000250}.; PTM: The ubiquitination status appears to regulate the formation and trafficking of beta-arrestin-GPCR complexes and signaling. Ubiquitination appears to occur GPCR-specific. Ubiquitinated by MDM2; the ubiquitination is required for rapid internalization of ADRB2. Deubiquitinated by USP33; the deubiquitination leads to a dissociation of the beta-arrestin-GPCR complex. Stimulation of a class A GPCR, such as ADRB2, induces transient ubiquitination and subsequently promotes association with USP33. Stimulation of a class B GPCR promotes a sustained ubiquitination (By similarity). {ECO:0000250}.; PTM: Hydroxylation by PHD2 modulates the rate of internalization by slowing down recruitment to the plasma membrane and inhibiting subsequent co-internalization with class A receptors. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12167659}. Nucleus {ECO:0000269|PubMed:12167659}. Cell membrane {ECO:0000269|PubMed:12167659}. Membrane, clathrin-coated pit {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Note=Translocates to the plasma membrane and colocalizes with antagonist-stimulated GPCRs. SUBUNIT: Homooligomer; the self-association is mediated by InsP6-binding (Probable). Heterooligomer with ARRB1; the association is mediated by InsP6-binding. Interacts with ADRB2 AND CHRM2. Interacts with PDE4A. Interacts with PDE4D. Interacts with MAPK10, MAPK1 and MAPK3. Interacts with DRD2. Interacts with FSHR. Interacts with CLTC. Interacts with HTR2C. Interacts with CCR5. Interacts with CXCR4. Interacts with SRC. Interacts with DUSP16; the interaction is interrupted by stimulation of AGTR1 and activation of MAPK10. Interacts with CHUK; the interaction is enhanced stimulation of ADRB2. Interacts with RELA. Interacts with MDM2; the interaction is enhanced by activation of GPCRs. Interacts with SLC9A5. Interacts with TRAF6. Interacts with IGF1R. Interacts with ENG. Interacts with ARRB2. Interacts with KIR2DL1, KIR2DL3 and KIR2DL4. Interacts with LDLR. Interacts with AP2B1. Interacts with C5AR1. Interacts with RAF1. Interacts with MAP2K1. Interacts with MAPK1. Interacts with MAPK10; the interaction enhances MAPK10 activation by MAP3K5. Interacts with MAP2K4; the interaction is enhanced by presence of MAP3K5 and MAPK10. Interacts with MAP3K5. Interacts with AKT1. Interacts with IKBKB and MAP3K14. Interacts with SMO (activated). Interacts with GSK3A and GSK3B. Interacts with CXCR4; the interaction is dependent on C-terminal phosphorylation of CXCR4 and allows activation of MAPK1 and MAPK3. Interacts with GPR143. Interacts with HCK and CXCR1 (phosphorylated) (By similarity). Associates with protein phosphatase 2A (PP2A). Interacts with ACKR3 and ACKR4 (By similarity). Interacts with ARRDC1; the interaction is direct (By similarity). Interacts with GPR61, GPR62 and GPR135 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P32121, ECO:0000305}. TISSUE SPECIFICITY: Predominantly localized in neuronal tissues and in the spleen. +Q32KI9 ARSI_MOUSE Arylsulfatase I (ASI) (EC 3.1.6.-) 573 64,367 Active site (2); Binding site (3); Chain (1); Compositional bias (1); Glycosylation (4); Metal binding (5); Modified residue (1); Signal peptide (1) FUNCTION: Displays arylsulfatase activity at neutral pH, when co-expressed with SUMF1; arylsulfatase activity is measured in the secretion medium of retinal cell line, but no activity is recorded when measured in cell extracts. {ECO:0000250}. PTM: The oxidation of Cys-93 residue to 3-oxoalanine (also known as C(alpha)-formylglycine) by SUMF1/Sulfatase-modifying factor 1, seems critical for catalytic activity. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. Endoplasmic reticulum. Note=Localized in the intracellular granular structures. {ECO:0000250}. +Q9EQP6 ARRC_MOUSE Arrestin-C (Cone arrestin) (cArr) (Retinal cone arrestin-3) 381 41,921 Chain (1) FUNCTION: May play a role in an as yet undefined retina-specific signal transduction. Could binds to photoactivated-phosphorylated red/green opsins. SUBUNIT: Interacts with CXCR4; the interaction is dependent on the C-terminal phosphorylation of CXCR4 and modulates the calcium ion mobilization activity of CXCR4. {ECO:0000250}. TISSUE SPECIFICITY: Inner and outer segments, and the inner plexiform regions of the retina. +Q91WU5 AS3MT_MOUSE Arsenite methyltransferase (EC 2.1.1.137) (Methylarsonite methyltransferase) (S-adenosyl-L-methionine:arsenic(III) methyltransferase) 376 41,794 Chain (1); Modified residue (2); Sequence conflict (3) FUNCTION: Catalyzes the transfer of a methyl group from AdoMet to trivalent arsenicals producing methylated and dimethylated arsenicals. It methylates arsenite to form methylarsonate, Me-AsO(3)H(2), which is reduced by methylarsonate reductase to methylarsonite, Me-As(OH)2. Methylarsonite is also a substrate and it is converted into the much less toxic compound dimethylarsinate (cacodylate), Me(2)As(O)-OH. {ECO:0000250|UniProtKB:Q8VHT6}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8VHT6}. +Q9D738 ASB12_MOUSE Ankyrin repeat and SOCS box protein 12 (ASB-12) 308 33,912 Chain (1); Domain (1); Repeat (5) Protein modification; protein ubiquitination. FUNCTION: Probable substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000250}. SUBUNIT: Interacts with CUL5 and RNF7. {ECO:0000250}. DOMAIN: The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin-protein ligase complexes. {ECO:0000250}. +C0HK80 ARXS2_MOUSE Adipocyte-related X-chromosome expressed sequence 2 180 20,146 Chain (1); Glycosylation (1); Sequence conflict (6); Topological domain (2); Transmembrane (1) TRANSMEM 12 32 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 11 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 33 180 Lumenal. {ECO:0000255}. FUNCTION: Plays a role in adipogenesis. {ECO:0000269|PubMed:21177646}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21177646}; Single-pass type II membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Strongly expressed in epididymal white and brown adipose tissue with low levels in heart. {ECO:0000269|PubMed:21177646}. +Q9EPB4 ASC_MOUSE Apoptosis-associated speck-like protein containing a CARD (mASC) (PYD and CARD domain-containing protein) 193 21,459 Chain (1); Domain (2); Modified residue (1); Sequence conflict (1) FUNCTION: Functions as key mediator in apoptosis and inflammation. Promotes caspase-mediated apoptosis involving predominantly caspase-8 and also caspase-9 in a probable cell type-specific manner. Involved in activation of the mitochondrial apoptotic pathway, promotes caspase-8-dependent proteolytic maturation of BID independently of FADD in certain cell types and also mediates mitochondrial translocation of BAX and activates BAX-dependent apoptosis coupled to activation of caspase-9, -2 and -3. Involved in macrophage pyroptosis, a caspase-1-dependent inflammatory form of cell death and is the major constituent of the ASC pyroptosome which forms upon potassium depletion and rapidly recruits and activates caspase-1. In innate immune response believed to act as an integral adapter in the assembly of the inflammasome which activates caspase-1 leading to processing and secretion of proinflammatory cytokines. The function as activating adapter in different types of inflammasomes is mediated by the pyrin and CARD domains and their homotypic interactions. Required for recruitment of caspase-1 to inflammasomes containing certain pattern recognition receptors, such as NLRP2, NLRP3, AIM2 and probably IFI16. In the NLRP1 and NLRC4 inflammasomes seems not be required but facilitates the processing of procaspase-1. In cooperation with NOD2 involved in an inflammasome activated by bacterial muramyl dipeptide leading to caspase-1 activation. May be involved in DDX58-triggered proinflammatory responses and inflammasome activation. In collaboration with AIM2 which detects cytosolic double-stranded DNA may also be involved in a caspase-1-independent cell death that involves caspase-8. In adaptive immunity may be involved in maturation of dendritic cells to stimulate T-cell immunity and in cytoskeletal rearrangements coupled to chemotaxis and antigen uptake may be involved in post-transcriptional regulation of the guanine nucleotide exchange factor DOCK2; the latter function is proposed to involve the nuclear form. Also involved in transcriptional activation of cytokines and chemokines independent of the inflammasome; this function may involve AP-1, NF-kappa-B, MAPK and caspase-8 signaling pathways. For regulation of NF-kappa-B activating and inhibiting functions have been reported. Modulates NF-kappa-B induction at the level of the IKK complex by inhibiting kinase activity of CHUK and IKBK. Proposed to compete with RIPK2 for association with CASP1 thereby down-regulating CASP1-mediated RIPK2-dependent NF-kappa-B activation and activating interleukin-1 beta processing. Modulates host resistance to DNA virus infection, probably by inducing the cleavage of and inactivating CGAS in presence of cytoplasmic double-stranded DNA (PubMed:28314590). {ECO:0000269|PubMed:15190255, ECO:0000269|PubMed:15507117, ECO:0000269|PubMed:21892172, ECO:0000269|PubMed:22555457, ECO:0000269|PubMed:28314590}. PTM: Phosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21892172, ECO:0000269|PubMed:22555457}. Endoplasmic reticulum {ECO:0000250}. Mitochondrion {ECO:0000250}. Nucleus {ECO:0000250}. Note=Upstream of caspase activation, a redistribution from the cytoplasm to the aggregates occurs. These appear as hollow, perinuclear spherical, ball-like structures. Upon NLRP3 inflammasome activation redistributes to the perinuclear space localizing to endoplasmic reticulum and mitochondria. Localized primarily to the nucleus in resting monocytes/macrophages and rapidly redistributed to the cytoplasm upon pathogen infection (By similarity). Localized to large cytoplasmic aggregate appearing as a speck containing AIM2, PYCARD, CASP8 and bacterial DNA after infection with Francisella tularensis. {ECO:0000250}. SUBUNIT: Self-associates; enforced oligomerization induces apoptosis, NF-kappa-B regulation and interleukin-1 beta secretion. Homooligomers can form disk-like particles of approximately 12 nm diameter and approximately 1 nm height. Component of several inflammasomes containing one pattern recognition receptor/sensor, such as NLRP1, NLRP2, NLRP3, AIM2, MEFV or NOD2, and probably NLRC4, NLRP12 or IFI16. Major component of the ASC pyroptosome, a 1-2 um supramolecular assembly (one per macrophage cell) which consists of oligomerized PYCARD dimers and CASP1. Interacts with CASP1 (precursor form); the interaction induces activation of CASP1 leading to the processing of interleukin-1 beta; PYCARD competes with RIPK2 for binding to CASP1. Interacts with NLRP3; the interaction requires the homooligomerization of NLRP3. Interacts with NLRP2, NLRC4, MEFV, CARD16, AIM2, IFI16, NOD2, DDX58, RIPK2, PYDC1, PYDC2, NLRP10, CASP8, CHUK, IKBKB and BAX. {ECO:0000269|PubMed:22555457}. DOMAIN: The CARD domain mediates interaction with CASP1 and NLRC4. {ECO:0000250}.; DOMAIN: The pyrin domain mediates homotypic interactions with pyrin domains of proteins such as of NLRP3, PYDC1, PYDC2 and AIM2. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in small intestine, colon, thymus, spleen, brain, heart, skeletal muscle, kidney, lung and liver. +Q9CQE6 ASF1A_MOUSE Histone chaperone ASF1A (Anti-silencing function protein 1 homolog A) 204 22,943 Chain (1); Modified residue (1); Motif (1); Region (2) FUNCTION: Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly. Cooperates with chromatin assembly factor 1 (CAF-1) to promote replication-dependent chromatin assembly and with HIRA to promote replication-independent chromatin assembly. Required for the formation of senescence-associated heterochromatin foci (SAHF) and efficient senescence-associated cell cycle exit. {ECO:0000250|UniProtKB:Q9Y294}. PTM: Phosphorylated by TLK1 and TLK2. Highly phosphorylated in S-phase and at lower levels in M-phase. TLK2-mediated phosphorylation at Ser-192 prevents proteasome-dependent degradation (By similarity). {ECO:0000250|UniProtKB:Q9Y294}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y294}. SUBUNIT: Interacts with histone H3 (including both histone H3.1 and H3.3) and histone H4. Interacts with the CHAF1A, CHAF1B and RBBP4 subunits of the CAF-1 complex. Interacts with CABIN1, HAT1, HIRA, NASP, TAF1, TLK1, TLK2 and UBN1 (By similarity). Interacts with CDAN1 (By similarity). Found in a cytosolic complex with CDAN1, ASF1B, IPO4 and histones H3.1 and H4. Interacts with CREBBP (By similarity). {ECO:0000250|UniProtKB:Q9Y294}. +P70158 ASM3A_MOUSE Acid sphingomyelinase-like phosphodiesterase 3a (ASM-like phosphodiesterase 3a) (EC 3.1.4.-) 445 49,858 Beta strand (16); Binding site (4); Chain (1); Disulfide bond (3); Glycosylation (6); Helix (18); Metal binding (8); Mutagenesis (3); Signal peptide (1); Turn (4) FUNCTION: Has in vitro nucleotide phosphodiesterase activity with nucleoside triphosphates, such as ATP (PubMed:26792860). Has in vitro activity with p-nitrophenyl-TMP. Has lower activity with nucleoside diphosphates, and no activity with nucleoside monophosphates. Has in vitro activity with CDP-choline, giving rise to CMP and phosphocholine. Has in vitro activity with CDP-ethanolamine. Does not have sphingomyelin phosphodiesterase activity (By similarity). {ECO:0000250|UniProtKB:Q92484, ECO:0000269|PubMed:26792860}. PTM: N-glycosylated. {ECO:0000269|PubMed:26095358}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25288789, ECO:0000269|PubMed:26095358, ECO:0000269|PubMed:26792860}. TISSUE SPECIFICITY: Detected in blood serum (at protein level). {ECO:0000269|PubMed:25288789}. +O54984 ASNA_MOUSE ATPase Asna1 (EC 3.6.-.-) (Arsenical pump-driving ATPase) (Arsenite-stimulated ATPase) 348 38,823 Active site (1); Binding site (2); Chain (1); Initiator methionine (1); Metal binding (2); Modified residue (1); Nucleotide binding (1) FUNCTION: ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors, where the tail-anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane proteins. ATP hydrolysis is required for insertion. Subsequently, the homodimer reverts towards the open dimer state, lowering its affinity for the membrane-bound receptor, and returning it to the cytosol to initiate a new round of targeting. {ECO:0000255|HAMAP-Rule:MF_03112}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03112}. Endoplasmic reticulum {ECO:0000255|HAMAP-Rule:MF_03112}. Nucleus, nucleolus {ECO:0000255|HAMAP-Rule:MF_03112}. SUBUNIT: Homodimer. Component of a transmembrane domain recognition complex (TRC). Interacts with SERP1 and SEC61B. Interacts with WRB. {ECO:0000255|HAMAP-Rule:MF_03112}. +Q6ZQ11 CHSS1_MOUSE Chondroitin sulfate synthase 1 (EC 2.4.1.175) (EC 2.4.1.226) (Chondroitin glucuronyltransferase 1) (Chondroitin synthase 1) (ChSy-1) (Glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase 1) (N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase 1) (N-acetylgalactosaminyltransferase 1) 800 91,383 Chain (1); Erroneous initiation (1); Glycosylation (2); Metal binding (2); Topological domain (2); Transmembrane (1) TRANSMEM 8 28 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 7 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 29 800 Lumenal. {ECO:0000255}. FUNCTION: Has both beta-1,3-glucuronic acid and beta-1,4-N-acetylgalactosamine transferase activity. Transfers glucuronic acid (GlcUA) from UDP-GlcUA and N-acetylgalactosamine (GalNAc) from UDP-GalNAc to the non-reducing end of the elongating chondroitin polymer. {ECO:0000250|UniProtKB:Q86X52}. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:Q86X52}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q86X52}. Secreted {ECO:0000250|UniProtKB:Q86X52}. SUBUNIT: Binds CHPF. {ECO:0000250}. +Q5DTK1 CHSS3_MOUSE Chondroitin sulfate synthase 3 (EC 2.4.1.175) (EC 2.4.1.226) (Carbohydrate synthase 2) (Chondroitin glucuronyltransferase 3) (Chondroitin synthase 2) (ChSy-2) (Glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase II) (N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase 3) (N-acetylgalactosaminyltransferase 3) 884 100,099 Chain (1); Compositional bias (2); Erroneous initiation (1); Glycosylation (4); Metal binding (2); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 8 28 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 7 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 29 884 Lumenal. {ECO:0000255}. FUNCTION: Has both beta-1,3-glucuronic acid and beta-1,4-N-acetylgalactosamine transferase activity. Transfers glucuronic acid (GlcUA) from UDP-GlcUA and N-acetylgalactosamine (GalNAc) from UDP-GalNAc to the non-reducing end of the elongating chondroitin polymer. Specific activity is much reduced compared to CHSY1. {ECO:0000250|UniProtKB:Q70JA7}. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. +Q9R0K7 AT2B2_MOUSE Plasma membrane calcium-transporting ATPase 2 (PMCA2) (EC 3.6.3.8) (Plasma membrane calcium ATPase isoform 2) (Plasma membrane calcium pump isoform 2) 1198 132,588 Active site (1); Chain (1); Compositional bias (1); Metal binding (2); Modified residue (6); Natural variant (2); Region (2); Topological domain (11); Transmembrane (10) TRANSMEM 95 115 Helical. {ECO:0000255}.; TRANSMEM 153 173 Helical. {ECO:0000255}.; TRANSMEM 346 365 Helical. {ECO:0000255}.; TRANSMEM 399 416 Helical. {ECO:0000255}.; TRANSMEM 831 850 Helical. {ECO:0000255}.; TRANSMEM 861 881 Helical. {ECO:0000255}.; TRANSMEM 902 924 Helical. {ECO:0000255}.; TRANSMEM 943 964 Helical. {ECO:0000255}.; TRANSMEM 984 1005 Helical. {ECO:0000255}.; TRANSMEM 1016 1037 Helical. {ECO:0000255}. TOPO_DOM 1 94 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 116 152 Extracellular. {ECO:0000255}.; TOPO_DOM 174 345 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 366 398 Extracellular. {ECO:0000255}.; TOPO_DOM 417 830 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 851 860 Extracellular. {ECO:0000255}.; TOPO_DOM 882 901 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 925 942 Extracellular. {ECO:0000255}.; TOPO_DOM 965 983 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1006 1015 Extracellular. {ECO:0000255}.; TOPO_DOM 1038 1198 Cytoplasmic. {ECO:0000255}. FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium out of the cell. Plays a role in maintaining balance and hearing. {ECO:0000269|PubMed:9668038}. SUBCELLULAR LOCATION: Cell junction, synapse {ECO:0000269|PubMed:12209837}. Cell membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Interacts with PDZD11. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the retina, with strongest levels in the inner plexiform layer, weaker levels in the outer plexiform layer, and very low levels in the proximal inner nuclear layer (PubMed:12209837). Specifically expressed in the following retinal cell types: rod bipolar cells, horizontal cells, amacrine cells and ganglion cells (PubMed:12209837). Also found in the cochlea (stereocilia and outer wall of hair cells) (at protein level) (PubMed:9697703). Strongly expressed in brain cortex. Found at low levels in heart, liver, lung and testis during late gestation (PubMed:9697703). {ECO:0000269|PubMed:12209837, ECO:0000269|PubMed:9697703}. DISEASE: Note=Atp2b2 null deficient mice are deaf. {ECO:0000269|PubMed:9697703}. +Q4QY64 ATAD5_MOUSE ATPase family AAA domain-containing protein 5 (Chromosome fragility-associated gene 1 protein) 1826 203,909 Alternative sequence (2); Chain (1); Cross-link (1); Erroneous gene model prediction (3); Modified residue (9); Motif (1); Nucleotide binding (1); Sequence caution (1); Sequence conflict (1) FUNCTION: Involved in DNA damage response. Involved in a RAD9A-related damage checkpoint, a pathway that is important in determining whether DNA damage is compatible with cell survival or whether it requires cell elimination by apoptosis. Modulates the RAD9A interaction with BCL2 and thereby induces DNA damages-induced apoptosis. {ECO:0000269|PubMed:15983387}. PTM: ATR may stimulate the RAD9A dissociation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Interacts with BRD4 (By similarity). Interacts with RB1 predominantly in G1 phase via its LXCXE motif. Interacts with RAD9A in growing cells. The interaction with RAD9A is reduced after exposure to DNA replication-inhibiting agents. {ECO:0000250, ECO:0000269|PubMed:15983387}. TISSUE SPECIFICITY: Expressed ubiquitously in all cell lines like teratocarcinoma, cell lymphoma, lymphoma. {ECO:0000269|PubMed:15983387}. +Q8BWU8 AT2L1_MOUSE Ethanolamine-phosphate phospho-lyase (EC 4.2.3.2) (Alanine--glyoxylate aminotransferase 2-like 1) 499 55,496 Chain (1); Modified residue (1); Sequence conflict (2) FUNCTION: Catalyzes the pyridoxal-phosphate-dependent breakdown of phosphoethanolamine, converting it to ammonia, inorganic phosphate and acetaldehyde. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}. SUBUNIT: Homotetramer. {ECO:0000250}. +P98199 AT8B2_MOUSE Phospholipid-transporting ATPase ID (EC 7.6.2.1) (ATPase class I type 8B member 2) (P4-ATPase flippase complex alpha subunit ATP8B2) 1209 136,968 Active site (1); Chain (1); Metal binding (2); Modified residue (1); Sequence conflict (1); Topological domain (11); Transmembrane (10) TRANSMEM 69 89 Helical. {ECO:0000255}.; TRANSMEM 92 112 Helical. {ECO:0000255}.; TRANSMEM 296 316 Helical. {ECO:0000255}.; TRANSMEM 339 359 Helical. {ECO:0000255}.; TRANSMEM 899 919 Helical. {ECO:0000255}.; TRANSMEM 923 943 Helical. {ECO:0000255}.; TRANSMEM 973 993 Helical. {ECO:0000255}.; TRANSMEM 1012 1032 Helical. {ECO:0000255}.; TRANSMEM 1037 1057 Helical. {ECO:0000255}.; TRANSMEM 1083 1103 Helical. {ECO:0000255}. TOPO_DOM 1 68 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 90 91 Exoplasmic loop. {ECO:0000255}.; TOPO_DOM 113 295 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 317 338 Exoplasmic loop. {ECO:0000255}.; TOPO_DOM 360 898 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 920 922 Exoplasmic loop. {ECO:0000255}.; TOPO_DOM 944 972 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 994 1011 Exoplasmic loop. {ECO:0000255}.; TOPO_DOM 1033 1036 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1058 1082 Exoplasmic loop. {ECO:0000255}.; TOPO_DOM 1104 1209 Cytoplasmic. {ECO:0000255}. FUNCTION: Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P98198}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P98198}; Multi-pass membrane protein {ECO:0000255}. Note=TMEM30A, but not TMEM30B, is required for its export from endoplasmic reticulum to the plasma membrane. {ECO:0000250|UniProtKB:P98198}. SUBUNIT: Component of a P4-ATPase flippase complex which consists of a catalytic alpha subunit and an accessory beta subunit (Probable). The probable flippase ATP8B2:TMEM30A complex can form an intermediate phosphoenzyme in vitro (By similarity). {ECO:0000250, ECO:0000305}. +Q8K341 ATAT_MOUSE Alpha-tubulin N-acetyltransferase 1 (Alpha-TAT) (Alpha-TAT1) (TAT) (EC 2.3.1.108) (Acetyltransferase mec-17 homolog) 421 47,164 Alternative sequence (5); Chain (1); Domain (1); Modified residue (9); Mutagenesis (7); Region (3); Sequence conflict (2); Site (1) FUNCTION: Specifically acetylates 'Lys-40' in alpha-tubulin on the lumenal side of microtubules. Promotes microtubule destabilization and accelerates microtubule dynamics; this activity may be independent of acetylation activity. Acetylates alpha-tubulin with a slow enzymatic rate, due to a catalytic site that is not optimized for acetyl transfer. Enters the microtubule through each end and diffuses quickly throughout the lumen of microtubules. Acetylates only long/old microtubules because of its slow acetylation rate since it does not have time to act on dynamically unstable microtubules before the enzyme is released. Required for normal sperm flagellar function. Promotes directional cell locomotion and chemotaxis, through AP2A2-dependent acetylation of alpha-tubulin at clathrin-coated pits that are concentrated at the leading edge of migrating cells. May facilitate primary cilium assembly. {ECO:0000255|HAMAP-Rule:MF_03130, ECO:0000269|PubMed:20829795, ECO:0000269|PubMed:23275437, ECO:0000269|PubMed:23720746, ECO:0000269|PubMed:23748901, ECO:0000269|PubMed:24097348}. PTM: Autoacetylation strongly increases tubulin acetylation. {ECO:0000255|HAMAP-Rule:MF_03130, ECO:0000269|PubMed:23275437}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03130, ECO:0000269|PubMed:23275437}. Membrane, clathrin-coated pit {ECO:0000255|HAMAP-Rule:MF_03130}. Cell junction, focal adhesion {ECO:0000255|HAMAP-Rule:MF_03130}. Cell projection, axon {ECO:0000255|HAMAP-Rule:MF_03130, ECO:0000269|PubMed:23275437}. Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03130, ECO:0000269|PubMed:23275437}. Cytoplasm, cytoskeleton, spindle {ECO:0000255|HAMAP-Rule:MF_03130, ECO:0000269|PubMed:23275437}. Note=In primary root dorsal ganglion neurons, localizes with acetylated tubulin in axons. Recruited to the mitotic spindle during cell division. {ECO:0000269|PubMed:23275437}. SUBUNIT: Component of the BBSome complex (By similarity). Interacts with AP2 alpha-adaptins, including AP2A2, but not with AP1 gamma-adaptin (AP1G1/AP1G2); this interaction is required for efficient alpha-tubulin acetylation, hence clathrin-coated pits are sites of microtubule acetylation. {ECO:0000255|HAMAP-Rule:MF_03130, ECO:0000269|PubMed:24097348}. TISSUE SPECIFICITY: Widely expressed with highest levels in neuronal tissues. In the brain, expressed in the cortex, cerebellum and hippocampus, including the pyramidal layers in CA1 and CA3, as well as the granular cell layers in the lateral blade (suprapyramidal portion) and the medial blade (infrapyramidal portion) of the dentate gyrus. In testis, mainly expressed in the internal cell layers of seminiferous tubules, where spermatocytes and spermatids are located. {ECO:0000269|PubMed:23275437, ECO:0000269|PubMed:23720746}. +P16951 ATF2_MOUSE Cyclic AMP-dependent transcription factor ATF-2 (cAMP-dependent transcription factor ATF-2) (EC 2.3.1.48) (Activating transcription factor 2) (MXBP protein) (cAMP response element-binding protein CRE-BP1) 487 52,298 Alternative sequence (2); Chain (1); Domain (1); Erroneous initiation (2); Modified residue (19); Motif (1); Region (3); Sequence conflict (2); Zinc finger (1) FUNCTION: Transcriptional activator which regulates the transcription of various genes, including those involved in anti-apoptosis, cell growth, and DNA damage response. Dependent on its binding partner, binds to CRE (cAMP response element) consensus sequences (5'-TGACGTCA-3') or to AP-1 (activator protein 1) consensus sequences (5'-TGACTCA-3'). In the nucleus, contributes to global transcription and the DNA damage response, in addition to specific transcriptional activities that are related to cell development, proliferation and death. In the cytoplasm, interacts with and perturbs HK1- and VDAC1-containing complexes at the mitochondrial outer membrane, thereby impairing mitochondrial membrane potential, inducing mitochondrial leakage and promoting cell death. The phosphorylated form (mediated by ATM) plays a role in the DNA damage response and is involved in the ionizing radiation (IR)-induced S phase checkpoint control and in the recruitment of the MRN complex into the IR-induced foci (IRIF). Exhibits histone acetyltransferase (HAT) activity which specifically acetylates histones H2B and H4 in vitro. In concert with CUL3 and RBX1, promotes the degradation of KAT5 thereby attenuating its ability to acetylate and activate ATM. Can elicit oncogenic or tumor suppressor activities depending on the tissue or cell type (By similarity). {ECO:0000250}. PTM: Phosphorylation of Thr-51 by MAPK14 and MAPK11, and at Thr-53 by MAPK1/ERK2, MAPK3/ERK1, MAPK11, MAPK12 and MAPK14 in response to external stimulus like insulin causes increased transcriptional activity (By similarity). Phosphorylated by PLK3 following hyperosmotic stress. Also phosphorylated and activated by JNK and CaMK4 (By similarity). Phosphorylation at Ser-44, Thr-55 and Ser-103 activates its transcriptional activity (By similarity). ATM-mediated phosphorylation at Ser-472 and Ser-480 stimulates its function in DNA damage response. Phosphorylation at Thr-51 or Thr-53 enhances its histone acetyltransferase (HAT) activity. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm {ECO:0000250}. Mitochondrion outer membrane {ECO:0000250}. Note=Shuttles between the cytoplasm and the nucleus and heterodimerization with JUN is essential for the nuclear localization. Localization to the cytoplasm is observed under conditions of cellular stress and in disease states. Localizes at the mitochondrial outer membrane in response to genotoxic stress. Phosphorylation at Thr-34 is required for its nuclear localization and negatively regulates its mitochondrial localization. Colocalizes with the MRN complex in the IR-induced foci (IRIF) (By similarity). {ECO:0000250}. SUBUNIT: Binds DNA as a dimer and can form a homodimer in the absence of DNA. Can form a heterodimer with JUN. Heterodimerization is essential for its transcriptional activity. Interacts with SMAD3 and SMAD4. Interacts with the HK1/VDAC1 complex. Interacts with NBN, MRE11, XPO1, KAT5 and CUL3 (By similarity). Binds through its N-terminal region to UTF1 which acts as a coactivator of ATF2 transcriptional activity. {ECO:0000250, ECO:0000269|PubMed:9524124}. +Q9WUL8 CITE4_MOUSE Cbp/p300-interacting transactivator 4 (MSG1-related protein 2) (MRG-2) 182 18,398 Alternative sequence (2); Chain (1); Compositional bias (1); Sequence conflict (2) FUNCTION: Acts as transcriptional coactivator for TFAP2/AP-2. Enhances estrogen-dependent transactivation mediated by estrogen receptors. May function as an inhibitor of transactivation by HIF1A by disrupting HIF1A interaction with CREBBP. May be involved in regulation of gene expression during development and differentiation of blood cells, endothelial cells and mammary epithelial cells. {ECO:0000269|PubMed:11581164, ECO:0000269|PubMed:12504852}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250|UniProtKB:Q96RK1}. SUBUNIT: Interacts via its C-terminal region with the CH1 domain of CREBBP and EP300. Interacts with all TFAP2/AP-2 isoforms. {ECO:0000250|UniProtKB:Q96RK1, ECO:0000269|PubMed:12504852}. TISSUE SPECIFICITY: Strongly expressed in heart, spleen and testis, and weakly in liver and kidney. {ECO:0000269|PubMed:12504852}. +Q6P4T0 ATG2A_MOUSE Autophagy-related protein 2 homolog A 1914 210,939 Chain (1); Erroneous initiation (1); Frameshift (1); Modified residue (8); Sequence conflict (3) FUNCTION: Involved in autophagosome assembly, regulating the size of nascent autophagosomes. Also regulates lipid droplets morphology and distribution within the cell. {ECO:0000250|UniProtKB:Q2TAZ0}.; FUNCTION: (Microbial infection) Mediates the intracellular lifestyle of Cryptococcus neoformans by supporting infection. {ECO:0000269|PubMed:21698225}. SUBCELLULAR LOCATION: Preautophagosomal structure membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Lipid droplet {ECO:0000250}. SUBUNIT: Interacts with WDR45. {ECO:0000250|UniProtKB:Q2TAZ0}. +Q505B7 ARCH_MOUSE Protein archease (Protein ZBTB8OS) 168 19,727 Alternative sequence (2); Chain (1); Erroneous initiation (2); Initiator methionine (1); Metal binding (3); Modified residue (1); Sequence conflict (1) FUNCTION: Component of the tRNA-splicing ligase complex required to facilitate the enzymatic turnover of catalytic subunit RTCB. Together with DDX1, acts by facilitating the guanylylation of RTCB, a key intermediate step in tRNA ligation (By similarity). {ECO:0000250}. SUBUNIT: Component of the tRNA-splicing ligase complex. {ECO:0000250}. +P97433 ARG28_MOUSE Rho guanine nucleotide exchange factor 28 (190 kDa guanine nucleotide exchange factor) (p190-RhoGEF) (p190RhoGEF) (Rho guanine nucleotide exchange factor) (Rho-interacting protein 2) 1693 190,326 Alternative sequence (2); Chain (1); Coiled coil (1); Domain (2); Erroneous initiation (1); Modified residue (6); Mutagenesis (6); Region (5); Sequence caution (2); Sequence conflict (2); Zinc finger (1) FUNCTION: Functions as a RHOA-specific guanine nucleotide exchange factor regulating signaling pathways downstream of integrins and growth factor receptors. Functions in axonal branching, synapse formation and dendritic morphogenesis. Functions also in focal adhesion formation, cell motility and B-lymphocytes activation. May regulate NEFL expression and aggregation and play a role in apoptosis. {ECO:0000269|PubMed:11058585, ECO:0000269|PubMed:11435431, ECO:0000269|PubMed:12496377, ECO:0000269|PubMed:12702722, ECO:0000269|PubMed:14499478, ECO:0000269|PubMed:15378065, ECO:0000269|PubMed:16236762, ECO:0000269|PubMed:17993462, ECO:0000269|PubMed:18195107, ECO:0000269|PubMed:9199174}. PTM: Phosphorylated on tyrosine upon stimulation of cells by laminin. {ECO:0000269|PubMed:12702722}. SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Note=Colocalizes with the microtubule radial and cortical systems. SUBUNIT: Homooligomer; forms some cytoplasmic aggregates. Forms a complex with MAPK8 and MAPK8IP1. Interacts with RHOA. Interacts with microtubules. Interacts with YWHAE and YWHAH. Interacts with PTK2/FAK1. Interacts with NEFL. Interacts with CTNND2; prevents interaction with RHOA. {ECO:0000269|PubMed:10574993, ECO:0000269|PubMed:11058585, ECO:0000269|PubMed:11533041, ECO:0000269|PubMed:12702722, ECO:0000269|PubMed:14499478, ECO:0000269|PubMed:16236762, ECO:0000269|PubMed:17993462}. TISSUE SPECIFICITY: Highly enriched in the brain (at protein level). Also detected in lung and kidney. {ECO:0000269|PubMed:12702722, ECO:0000269|PubMed:9199174}. +Q61176 ARGI1_MOUSE Arginase-1 (EC 3.5.3.1) (Liver-type arginase) (Type I arginase) 323 34,808 Binding site (3); Chain (1); Erroneous initiation (1); Metal binding (8); Modified residue (8); Region (2); Sequence conflict (2) Nitrogen metabolism; urea cycle; L-ornithine and urea from L-arginine: step 1/1. FUNCTION: Key element of the urea cycle converting L-arginine to urea and L-ornithine, which is further metabolized into metabolites proline and polyamides that drive collagen synthesis and bioenergetic pathways critical for cell proliferation, respectively; the urea cycle takes place primarily in the liver and, to a lesser extent, in the kidneys. {ECO:0000305}.; FUNCTION: Functions in L-arginine homeostasis in nonhepatic tissues characterized by the competition between nitric oxide synthase (NOS) and arginase for the available intracellular substrate arginine. Arginine metabolism is a critical regulator of innate and adaptive immune responses. Involved in an antimicrobial effector pathway in polymorphonuclear granulocytes (PMN). Upon PMN cell death is liberated from the phagolysosome and depletes arginine in the microenvironment leading to suppressed T cell and natural killer (NK) cell proliferation and cytokine secretion (By similarity). In group 2 innate lymphoid cells (ILC2s) promotes acute type 2 inflammation in the lung and is involved in optimal ILC2 proliferation but not survival (PubMed:27043409). Plays a role in the immune response of alternatively activated or M2 macrophages in processes such as wound healing and tissue regeneration, immune defense against multicellular pathogens and parasites, and immune suppression and allergic inflammation; the regulatory outcome seems to be organ specific (PubMed:7537672, PubMed:19360123, PubMed:20483789, PubMed:23552798, PubMed:23637937). In tumor-infiltrating dendritic cells (DCs) and myeloid-derived suppressor cells (MDSCs) plays a role in suppression of T cell-mediated antitumor immunity (PubMed:19414774, PubMed:23248265). {ECO:0000250|UniProtKB:P05089, ECO:0000269|PubMed:15313928, ECO:0000269|PubMed:19360123, ECO:0000269|PubMed:19414774, ECO:0000269|PubMed:20483789, ECO:0000269|PubMed:23248265, ECO:0000269|PubMed:23552798, ECO:0000269|PubMed:23637937, ECO:0000269|PubMed:27043409, ECO:0000269|PubMed:7537672}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P05089}. Cytoplasmic granule {ECO:0000250|UniProtKB:P05089}. SUBUNIT: Homotrimer (By similarity). Interacts with CMTM6 (By similarity). {ECO:0000250|UniProtKB:P05089}. TISSUE SPECIFICITY: Expressed in macrophages (PubMed:7537672, PubMed:12193690, PubMed:19360123). Expressed in precursor and mature group 2 innate lymphoid cells (ILC2s) (PubMed:27043409). Expressed in lung tumor-associated myeloid cells (PubMed:15313928). Expressed in lung tumor-infiltrating dendritic cells (PubMed:19414774). {ECO:0000269|PubMed:12193690, ECO:0000269|PubMed:19360123, ECO:0000269|PubMed:19414774, ECO:0000269|PubMed:27043409, ECO:0000269|PubMed:7537672}. +Q3U5C8 ARHGG_MOUSE Rho guanine nucleotide exchange factor 16 (Ephexin-4) 713 80,381 Chain (1); Domain (3); Erroneous initiation (1); Modified residue (7); Motif (1); Region (1); Sequence conflict (1) FUNCTION: Guanyl-nucleotide exchange factor of the RHOG GTPase stimulating the exchange of RHOG-associated GDP for GTP. May play a role in chemotactic cell migration by mediating the activation of RAC1 by EPHA2. May also activate CDC42 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with ELMO2, EPHA2, RAC1 and RHOG; mediates activation of RAC1 by EPHA2. Interacts with TAX1BP3 (via PDZ domain) (By similarity). {ECO:0000250}. DOMAIN: The PDZ-binding motif mediates interaction with TAX1BP3. +Q9CQW2 ARL8B_MOUSE ADP-ribosylation factor-like protein 8B (ADP-ribosylation factor-like protein 10C) (Novel small G protein indispensable for equal chromosome segregation 1) 186 21,539 Chain (1); Intramembrane (1); Nucleotide binding (3); Sequence conflict (3) INTRAMEM 1 19 Note=Mediates targeting to membranes. {ECO:0000250}. FUNCTION: May play a role in lysosome motility. May play a role in chromosome segregation. {ECO:0000250|UniProtKB:Q9NVJ2}. SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250|UniProtKB:Q9NVJ2}. Lysosome membrane {ECO:0000250|UniProtKB:Q9NVJ2}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9NVJ2}. Note=Localizes with microtubules at the spindle mid-zone during mitosis. {ECO:0000250|UniProtKB:Q9NVJ2}. SUBUNIT: Interacts with tubulin. Interacts with BORCS5; recruits ARL8B to lysosomes. {ECO:0000250|UniProtKB:Q9NVJ2}. +Q6P3A9 ARL11_MOUSE ADP-ribosylation factor-like protein 11 176 19,212 Chain (1); Initiator methionine (1); Lipidation (1); Nucleotide binding (3); Sequence conflict (1) FUNCTION: May play a role in apoptosis. May act as a tumor suppressor (By similarity). {ECO:0000250}. +Q9CWR0 ARHGP_MOUSE Rho guanine nucleotide exchange factor 25 (Guanine nucleotide exchange factor GEFT) (Rac/Cdc42/Rho exchange factor GEFT) (RhoA/Rac/Cdc42 guanine nucleotide exchange factor GEFT) (p63RhoGEF) 618 68,262 Alternative sequence (1); Chain (1); Domain (2); Region (2); Sequence conflict (2) FUNCTION: May play a role in actin cytoskeleton reorganization in different tissues since its activation induces formation of actin stress fibers. It works as a guanine nucleotide exchange factor for Rho family of small GTPases. Links specifically G alpha q/11-coupled receptors to RHOA activation (By similarity). May be an important regulator of processes involved in axon and dendrite formation. In neurons seems to be an exchange factor primarily for RAC1. Involved in skeletal myogenesis. {ECO:0000250, ECO:0000269|PubMed:15322108, ECO:0000269|PubMed:16314529, ECO:0000269|PubMed:16496360}. SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:18541910}. Cytoplasm, myofibril {ECO:0000269|PubMed:18541910}. Note=Highly colocalizes with actin regions. {ECO:0000250}. SUBUNIT: Interacts with activated GNAQ and GNA11 (By similarity). Interacts (via the DH domain) with BVES (via the C-terminus cytoplasmic tail). Interacts with RHOA, CDC42 and RAC1. {ECO:0000250, ECO:0000269|PubMed:15322108, ECO:0000269|PubMed:18541910}. DOMAIN: The guanine nucleotide exchange activity is autoinhibited by the PH domain. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in excitable tissues, such as brain, heart and muscle. Elevated expression in hippocampus and cerebellum. {ECO:0000269|PubMed:15322108, ECO:0000269|PubMed:16314529, ECO:0000269|PubMed:16496360}. +Q9Z1K5 ARI1_MOUSE E3 ubiquitin-protein ligase ARIH1 (EC 2.3.2.31) (Protein ariadne-1 homolog) (ARI-1) (RING-type E3 ubiquitin transferase ARIH1) (UbcH7-binding protein) (UbcM4-interacting protein 77) (Ubiquitin-conjugating enzyme E2-binding protein 1) 555 64,017 Active site (1); Chain (1); Erroneous initiation (1); Metal binding (24); Modified residue (1); Region (3); Sequence conflict (5); Zinc finger (3) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase, which catalyzes ubiquitination of target proteins together with ubiquitin-conjugating enzyme E2 UBE2L3. Acts as an atypical E3 ubiquitin-protein ligase by working together with cullin-RING ubiquitin ligase (CRL) complexes and initiating ubiquitination of CRL substrates: associates with CRL complexes and specifically mediates addition of the first ubiquitin on CRLs targets. The initial ubiquitin is then elongated by CDC34/UBE2R1 and UBE2R2. E3 ubiquitin-protein ligase activity is activated upon binding to neddylated cullin-RING ubiquitin ligase complexes. Plays a role in protein translation in response to DNA damage by mediating ubiquitination of EIF4E2, the consequences of EIF4E2 ubiquitination are however unclear. According to a report, EIF4E2 ubiquitination leads to promote EIF4E2 cap-binding and protein translation arrest. According to another report EIF4E2 ubiquitination leads to its subsequent degradation. Acts as the ligase involved in ISGylation of EIF4E2. {ECO:0000250|UniProtKB:Q9Y4X5}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y4X5}. Nucleus {ECO:0000250|UniProtKB:Q9Y4X5}. Nucleus, Cajal body {ECO:0000250|UniProtKB:Q9Y4X5}. Note=Mainly cytoplasmic. Present in Lewy body. {ECO:0000250|UniProtKB:Q9Y4X5}. SUBUNIT: Interacts (via the first RING-type zinc finger) with UBE2L3. Associates with cullin-RING ubiquitin ligase (CRL) complexes containing CUL1, CUL2 and CUL3. Interacts with neddylated CUL1. Interacts with neddylated CUL2. Interacts with neddylated CUL3. Interacts with neddylated CUL4A. {ECO:0000250|UniProtKB:Q9Y4X5}. DOMAIN: Members of the RBR family are atypical E3 ligases. They interact with the E2 conjugating enzyme UBE2L3 and function like HECT-type E3 enzymes: they bind E2s via the first RING-type zinc finger, but require an obligate trans-thiolation step during the ubiquitin transfer, requiring a conserved active site Cys residue in the second RING-type zinc finger. The active site probably forms a thioester intermediate with ubiquitin taken from the active-site cysteine of the E2 before ultimately transferring it to a Lys residue on the substrate. {ECO:0000250|UniProtKB:Q9Y4X5}.; DOMAIN: The Ariadne domain inhibits activity by masking the second RING-type zinc finger that contains the active site. {ECO:0000250|UniProtKB:Q9Y4X5}. TISSUE SPECIFICITY: Widely expressed. +Q6P068 ARL5C_MOUSE ADP-ribosylation factor-like protein 5C (ADP-ribosylation factor-like protein 12) 179 20,059 Chain (1); Initiator methionine (1); Lipidation (1); Nucleotide binding (3) FUNCTION: Binds and exchanges GTP and GDP. {ECO:0000250}. +Q9D0L7 ARM10_MOUSE Armadillo repeat-containing protein 10 306 33,311 Alternative sequence (1); Chain (1); Frameshift (1); Modified residue (2); Repeat (1); Sequence conflict (2); Transmembrane (1) TRANSMEM 7 29 Helical. {ECO:0000255}. FUNCTION: May play a role in cell survival and cell growth. May suppress the transcriptional activity of p53/TP53 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with the DNA-binding domain of p53/TP53. {ECO:0000250}. +Q9CX83 ARMX1_MOUSE Armadillo repeat-containing X-linked protein 1 456 50,643 Chain (1); Compositional bias (1); Region (2); Repeat (4); Topological domain (2); Transmembrane (1) TRANSMEM 7 29 Helical; Signal-anchor. {ECO:0000255}. TOPO_DOM 1 6 Mitochondrial intermembrane. {ECO:0000250|UniProtKB:Q8BHS6}.; TOPO_DOM 30 456 Cytoplasmic. {ECO:0000250|UniProtKB:Q8BHS6}. FUNCTION: Regulates mitochondrial transport during axon regeneration. Increases the proportion of motile mitochondria by recruiting stationary mitochondria into the motile pool. Enhances mitochondria movement and neurite growth in both adult axons and embryonic neurons. Promotes neuronal survival and axon regeneration after nerve injury. May link mitochondria to the Trak1-kinesin motor complex via its interaction with Miro1. {ECO:0000269|PubMed:28009275}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:22569362, ECO:0000269|PubMed:28009275}. Mitochondrion outer membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000255}. SUBUNIT: Interacts with MIRO1. {ECO:0000269|PubMed:28009275}. TISSUE SPECIFICITY: Widely expressed in the adult nervous tissue, especially in the forebrain, including the cerebral cortex, hippocampus and thalamus. {ECO:0000269|PubMed:22569362}. +Q6A058 ARMX2_MOUSE Armadillo repeat-containing X-linked protein 2 784 81,036 Chain (1); Compositional bias (1); Erroneous initiation (1); Region (2); Repeat (3); Topological domain (2); Transmembrane (1) TRANSMEM 7 27 Helical; Signal-anchor. {ECO:0000255}. TOPO_DOM 1 6 Mitochondrial intermembrane. {ECO:0000250|UniProtKB:Q8BHS6}.; TOPO_DOM 28 784 Cytoplasmic. {ECO:0000250|UniProtKB:Q8BHS6}. FUNCTION: May regulate the dynamics and distribution of mitochondria in neural cells. {ECO:0000269|PubMed:22569362}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:22569362}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q8BHS6}; Single-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Widely expressed in the adult nervous tissue, especially in the forebrain, including the cerebral cortex, hippocampus and thalamus. {ECO:0000269|PubMed:22569362}. +Q8K3A6 ARMX6_MOUSE Protein ARMCX6 301 33,321 Chain (1); Region (2); Topological domain (2); Transmembrane (1) TRANSMEM 8 25 Helical; Signal-anchor. {ECO:0000255}. TOPO_DOM 1 7 Mitochondrial intermembrane. {ECO:0000250|UniProtKB:Q8BHS6}.; TOPO_DOM 26 301 Cytoplasmic. {ECO:0000250|UniProtKB:Q8BHS6}. FUNCTION: May regulate the dynamics and distribution of mitochondria in neural cells. {ECO:0000269|PubMed:22569362}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:22569362}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q8BHS6}; Single-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Highly expressed in the developing neural tissues, neural crest derivatives and hind limbs. Also widely expressed in the adult nervous tissue, especially in the forebrain, including the cerebral cortex, hippocampus and thalamus. {ECO:0000269|PubMed:22569362}. +Q9CXF7 CHD1L_MOUSE Chromodomain-helicase-DNA-binding protein 1-like (EC 3.6.4.12) 900 101,438 Alternative sequence (1); Chain (1); Coiled coil (1); Domain (3); Modified residue (5); Motif (1); Nucleotide binding (1); Sequence conflict (3) FUNCTION: DNA helicase which plays a role in chromatin-remodeling following DNA damage. Targeted to sites of DNA damage through interaction with poly(ADP-ribose) and functions to regulate chromatin during DNA repair. Able to catalyze nucleosome sliding in an ATP-dependent manner. Helicase activity is strongly stimulated upon poly(ADP-ribose)-binding (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Localizes at sites of DNA damage. Probably recruited to DNA damage sites by PARylated PARP1 (By similarity). {ECO:0000250}. SUBUNIT: Interacts with PARP1; interacts only when PARP1; interacts only when PARP1 is poly-ADP-ribosylated (PARylated) (By similarity). Interacts with CIAO1 (By similarity). {ECO:0000250|UniProtKB:Q86WJ1}. DOMAIN: The macro domain mediates non-covalent poly(ADP-ribose)-binding and recruitment to DNA damage sites. {ECO:0000250}. +Q09XV5 CHD8_MOUSE Chromodomain-helicase-DNA-binding protein 8 (CHD-8) (EC 3.6.4.12) (ATP-dependent helicase CHD8) (Axis duplication inhibitor) (Duplin) 2582 290,847 Alternative sequence (2); Chain (1); Compositional bias (4); Cross-link (3); Domain (4); Modified residue (22); Motif (1); Nucleotide binding (1); Region (1); Sequence caution (1); Sequence conflict (3) FUNCTION: DNA helicase that acts as a chromatin remodeling factor and regulates transcription. Acts as a transcription repressor by remodeling chromatin structure and recruiting histone H1 to target genes. Suppresses p53/TP53-mediated apoptosis by recruiting histone H1 and preventing p53/TP53 transactivation activity. Acts as a negative regulator of Wnt signaling pathway by regulating beta-catenin (CTNNB1) activity. Negatively regulates CTNNB1-targeted gene expression by being recruited specifically to the promoter regions of several CTNNB1 responsive genes. Involved in both enhancer blocking and epigenetic remodeling at chromatin boundary via its interaction with CTCF. Acts as a suppressor of STAT3 activity by suppressing the LIF-induced STAT3 transcriptional activity. Also acts as a transcription activator via its interaction with ZNF143 by participating in efficient U6 RNA polymerase III transcription. {ECO:0000255|HAMAP-Rule:MF_03071, ECO:0000269|PubMed:16949368, ECO:0000269|PubMed:19151705}. PTM: Sumoylated. {ECO:0000255|HAMAP-Rule:MF_03071}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03071, ECO:0000269|PubMed:16949368}. Note=Localizes to the promoter regions of several CTNNB1-responsive genes. Also present at known CTCF target sites. {ECO:0000255|HAMAP-Rule:MF_03071}. SUBUNIT: Interacts with CTNNB1 and PIAS3. Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, KAT8/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Interacts with CHD7. Interacts with FAM124B (By similarity). Interacts with p53/TP53 and histone H1 (PubMed:19151705). Interacts with CTCF (PubMed:16949368). {ECO:0000255|HAMAP-Rule:MF_03071, ECO:0000269|PubMed:16949368, ECO:0000269|PubMed:19151705}. +P53762 ARNT_MOUSE Aryl hydrocarbon receptor nuclear translocator (ARNT protein) (Dioxin receptor, nuclear translocator) (Hypoxia-inducible factor 1-beta) (HIF-1-beta) (HIF1-beta) 791 86,963 Alternative sequence (1); Beta strand (13); Chain (1); Compositional bias (3); Cross-link (1); Domain (4); Helix (13); Initiator methionine (1); Modified residue (2); Mutagenesis (19); Region (4); Sequence conflict (4); Turn (4) FUNCTION: Required for activity of the Ah (dioxin) receptor. This protein is required for the ligand-binding subunit to translocate from the cytosol to the nucleus after ligand binding. The complex then initiates transcription of genes involved in the activation of PAH procarcinogens (By similarity). The heterodimer binds to core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters and functions as a transcriptional regulator of the adaptive response to hypoxia (PubMed:26245371, PubMed:27782878). The heterodimer ARNT:AHR binds to core DNA sequence 5'-TGCGTG-3' within the dioxin response element (DRE) of target gene promoters and activates their transcription (PubMed:28602820). {ECO:0000250, ECO:0000269|PubMed:26245371, ECO:0000269|PubMed:27782878, ECO:0000269|PubMed:28602820}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Monomer (PubMed:28602820). Homodimer only upon binding to a DNA (PubMed:26245371, PubMed:28602820). Efficient DNA binding requires dimerization with another bHLH protein (By similarity). Interacts with TACC3 (PubMed:11025203). Interacts with HIF1A, EPAS1, NPAS1 and NPAS3; forms a heterodimer that binds core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters (PubMed:26245371, PubMed:27782878). Forms a heterodimer with AHRR, as well as with other bHLH proteins (PubMed:9887096). Interacts with NOCA7 (By similarity). Interacts with AHR; the heterodimer ARNT:AHR binds to core DNA sequence 5'-TGCGTG-3' within the dioxin response element (DRE) of target gene promoters and activates their transcription (PubMed:28602820, PubMed:24001774, PubMed:27782878). Interacts with SIM1 and NPAS4 (PubMed:27782878). {ECO:0000250, ECO:0000250|UniProtKB:P27540, ECO:0000269|PubMed:11025203, ECO:0000269|PubMed:24001774, ECO:0000269|PubMed:26245371, ECO:0000269|PubMed:27782878, ECO:0000269|PubMed:28602820, ECO:0000269|PubMed:9887096}. TISSUE SPECIFICITY: Ubiquitous. +Q9D869 CHP2_MOUSE Calcineurin B homologous protein 2 (Hepatocellular carcinoma-associated antigen 520 homolog) 196 22,567 Calcium binding (2); Chain (1); Domain (4); Initiator methionine (1); Lipidation (1); Modified residue (1); Motif (1); Sequence conflict (1) FUNCTION: Functions as an integral cofactor in cell pH regulation by controlling plasma membrane-type Na(+)/H(+) exchange activity. Binds to and activates SLC9A1/NHE1 in a serum-independent manner, thus increasing pH and protecting cells from serum deprivation-induced death. Also plays a role in the regulation of cell proliferation and tumor growth by increasing the phosphatase activity of PPP3CA in a calcium-dependent manner. Activator of the calcineurin/NFAT signaling pathway. Involved in the cytoplasmic translocation of the transcription factor NFATC3 to the nucleus (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Exported from the nucleus to the cytoplasm through a nuclear export signal (NES) pathway. May shuttle between nucleus and cytoplasm. Predominantly localized in a juxtanuclear region. Colocalizes with SLC9A3 in the juxtanuclear region and at the plasma membrane (By similarity). {ECO:0000250}. SUBUNIT: Interacts with PPP3CA. Interacts with SLC9A1/NHE1; the interaction occurs in a calcium-dependent manner. Interacts with SLC9A1/NHE1 (By similarity). {ECO:0000250}. +Q9D2L1 ARSK_MOUSE Arylsulfatase K (ASK) (EC 3.1.6.-) 553 62,801 Active site (1); Binding site (2); Chain (1); Erroneous initiation (15); Frameshift (1); Glycosylation (6); Metal binding (4); Modified residue (1); Sequence conflict (1); Signal peptide (1) PTM: The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q99KN1 ARRD1_MOUSE Arrestin domain-containing protein 1 (Alpha-arrestin 1) 434 46,330 Alternative sequence (1); Chain (1); Erroneous initiation (1); Motif (2); Sequence conflict (2) FUNCTION: Functions as an adapter recruiting ubiquitin-protein ligases to their specific substrates (PubMed:23886940, PubMed:27462458). Through an ubiquitination-dependent mechanism plays for instance a role in the incorporation of SLC11A2 into extracellular vesicles (PubMed:27462458). More generally, plays a role in the extracellular transport of proteins between cells through the release in the extracellular space of microvesicles (By similarity). By participating to the ITCH-mediated ubiquitination and subsequent degradation of NOTCH1, negatively regulates the NOTCH signaling pathway (PubMed:23886940). {ECO:0000250|UniProtKB:Q8N5I2, ECO:0000269|PubMed:23886940, ECO:0000269|PubMed:27462458}. PTM: Ubiquitinated. Ubiquitination by WWP2; promotes localization to extracellular microvesicles. Ubiquitinated by WWP1. {ECO:0000250|UniProtKB:Q8N5I2}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8N5I2}. Note=Also found in extracellular vesicles different from exosomes. {ECO:0000250|UniProtKB:Q8N5I2}. SUBUNIT: Interacts (via PPxY motifs) with ITCH (via WW domains); the interaction is direct and participates to the recruitment of the ubiquitin-protein ligase ITCH to the NOTCH1 receptor. Interacts with ARRB1 and ARRB2; the interaction is direct. Interacts with TSG101; may recruit TSG101 to the plasma membrane. Interacts (via PPxY motifs) with WWP2 (via WW domains); ubiquitinates ARRDC1. Interacts with SLC11A2; controls the incorporation of SLC11A2 into extracellular vesicles through an ubiquitination-dependent mechanism. Interacts with WWP1 (via WW domains). Interacts with NEDD4 (via WW domains). Interacts with ALIX. {ECO:0000250|UniProtKB:Q8N5I2}. DOMAIN: The PPxY motifs mediate interaction with WW domain-containing ubiquitin-protein ligases. {ECO:0000250|UniProtKB:Q8N5I2}. +Q7TPQ9 ARRD3_MOUSE Arrestin domain-containing protein 3 414 46,275 Chain (1); Erroneous initiation (1); Motif (2); Sequence conflict (1) FUNCTION: Adapter protein that plays a role in regulating cell-surface expression of adrenergic receptors and probably also other G protein-coupled receptors (PubMed:21982743). Plays a role in NEDD4-mediated ubiquitination and endocytosis af activated ADRB2 and subsequent ADRB2 degradation. May recruit NEDD4 to ADRB2. Alternatively, may function as adapter protein that does not play a major role in recruiting NEDD4 to ADRB2, but rather plays a role in a targeting ADRB2 to endosomes. {ECO:0000250|UniProtKB:Q96B67, ECO:0000305|PubMed:21982743}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96B67}. Cell membrane {ECO:0000250|UniProtKB:Q96B67}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q96B67}; Cytoplasmic side {ECO:0000250|UniProtKB:Q96B67}. Lysosome {ECO:0000250|UniProtKB:Q96B67}. Endosome {ECO:0000250|UniProtKB:Q96B67}. Early endosome {ECO:0000250|UniProtKB:Q96B67}. Note=Associated with plasma membrane, as well as with endosomes and lysosomes during endocytosis. {ECO:0000250|UniProtKB:Q96B67}. SUBUNIT: Interacts (via PPxY motifs) with NEDD4 (via WW domains). Interacts with ADRB2. Interacts with ADRB3. Interacts with HGS (via PPxY motifs). Does not bind TXN (thioredoxin). Interacts with ITCH. {ECO:0000250|UniProtKB:Q96B67}. TISSUE SPECIFICITY: Detected in visceral fat, subcutaneous fat, brown fat and skeletal muscle, and at lower levels in kidney. {ECO:0000269|PubMed:21982743}. +A0A0B4J1F4 ARRD4_MOUSE Arrestin domain-containing protein 4 415 44,970 Alternative sequence (2); Chain (1); Motif (2); Mutagenesis (1) FUNCTION: Functions as an adapter recruiting ubiquitin-protein ligases to their specific substrates (PubMed:27462458). Plays a role in endocytosis of activated G protein-coupled receptors (GPCRs) (By similarity). Through an ubiquitination-dependent mechanism plays also a role in the incorporation of SLC11A2 into extracellular vesicles (PubMed:27462458). May play a role in glucose uptake (By similarity). {ECO:0000250|UniProtKB:Q8NCT1, ECO:0000269|PubMed:27462458}. SUBCELLULAR LOCATION: Early endosome {ECO:0000269|PubMed:19605364}. Cell membrane {ECO:0000269|PubMed:19605364, ECO:0000269|PubMed:27462458}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle {ECO:0000269|PubMed:19605364}. Note=Also found in extracellular vesicles different from exosomes. {ECO:0000269|PubMed:27462458}. SUBUNIT: Interacts with ADRB2. Interacts (via PPxY motifs) with ITCH, NEDD4L and WWP2. Interacts with AVPR2. Identified in a complex containing at least ARRDC4, AVPR2 and HGS (By similarity). Interacts with SLC11A2; controls the incorporation of SLC11A2 into extracellular vesicles through an ubiquitination-dependent mechanism (PubMed:27462458). {ECO:0000250|UniProtKB:Q8NCT1, ECO:0000269|PubMed:27462458}. +Q497K5 ARRD5_MOUSE Arrestin domain-containing protein 5 325 36,788 Chain (1) +P50294 ARY1_MOUSE Arylamine N-acetyltransferase 1 (EC 2.3.1.5) (Arylamide acetylase 1) (N-acetyltransferase type 1) (NAT-1) 290 33,713 Active site (3); Binding site (2); Chain (1); Modified residue (1); Region (1) FUNCTION: Participates in the detoxification of a plethora of hydrazine and arylamine drugs. Isoniazid, 2-aminofluorene and anisidine are preferred substrates for NAT-1. No activity with p-aminobenzoic acid (PABA) nor SMZ. SUBCELLULAR LOCATION: Cytoplasm. +P50295 ARY2_MOUSE Arylamine N-acetyltransferase 2 (EC 2.3.1.5) (Arylamide acetylase 2) (N-acetyltransferase type 2) (NAT-2) 290 33,701 Active site (3); Binding site (3); Chain (1); Natural variant (1); Region (1) FUNCTION: Participates in the detoxification of a plethora of hydrazine and arylamine drugs. 2-aminofluorene and p-aminobenzoic acid (PABA) are preferred substrates for NAT-2. Less activity with anisidine and barely detectable with SMZ. SUBCELLULAR LOCATION: Cytoplasm. +Q8VBX0 ASB13_MOUSE Ankyrin repeat and SOCS box protein 13 (ASB-13) 278 29,896 Chain (1); Domain (1); Repeat (6) Protein modification; protein ubiquitination. FUNCTION: May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000250}. DOMAIN: The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin-protein ligase complexes. {ECO:0000250}. +Q8VHS6 ASB15_MOUSE Ankyrin repeat and SOCS box protein 15 (ASB-15) 583 65,512 Chain (1); Domain (1); Repeat (11); Sequence conflict (1) Protein modification; protein ubiquitination. FUNCTION: May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000250}. DOMAIN: The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin-protein ligase complexes. {ECO:0000250}. +Q9QWY8 ASAP1_MOUSE Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 (130 kDa phosphatidylinositol 4,5-bisphosphate-dependent ARF1 GTPase-activating protein) (ADP-ribosylation factor-directed GTPase-activating protein 1) (ARF GTPase-activating protein 1) (Development and differentiation-enhancing factor 1) (DEF-1) (Differentiation-enhancing factor 1) (PIP2-dependent ARF1 GAP) 1147 127,421 Alternative sequence (3); Beta strand (9); Chain (1); Compositional bias (1); Domain (3); Erroneous initiation (2); Helix (3); Modified residue (10); Mutagenesis (3); Repeat (2); Sequence conflict (4); Zinc finger (1) FUNCTION: May function as a signal transduction protein involved in the differentiation of fibroblasts into adipocytes and possibly other cell types. Plays a role in ciliogenesis (By similarity). Posseses phosphatidylinositol 4,5-bisphosphate-dependent GTPase-activating protein activity for ARF1 (ADP ribosylation factor 1) and ARF5 and a lesser activity towards ARF6. May coordinate membrane trafficking with cell growth or actin cytoskeleton remodeling by binding to both SRC and PIP2. {ECO:0000250}. PTM: Phosphorylated on tyrosine residues by SRC. {ECO:0000269|PubMed:12771146}. SUBCELLULAR LOCATION: Cytoplasm. Membrane. Note=Predominantly cytoplasmic. Partially membrane-associated. SUBUNIT: Homodimer. Interacts with SRC and CRK. Interacts with RAB11FIP3. Interacts with PTK2B/PYK2. {ECO:0000269|PubMed:12771146, ECO:0000269|PubMed:18685082}. DOMAIN: The PH domain most probably contributes to the phosphoinositide-dependent regulation of ADP ribosylation factors. TISSUE SPECIFICITY: Expressed in all tissues examined but a most abundant expression was found in the testis, brain, lung and spleen. A heightened expression was seen in the adipose tissue from obese (ob) and diabetic (db) animals. {ECO:0000269|PubMed:10022919}. +Q8C0M9 ASGL1_MOUSE Isoaspartyl peptidase/L-asparaginase (EC 3.4.19.5) (EC 3.5.1.1) (Asparaginase-like protein 1) (Beta-aspartyl-peptidase) (Isoaspartyl dipeptidase) (L-asparagine amidohydrolase) [Cleaved into: Isoaspartyl peptidase/L-asparaginase alpha chain; Isoaspartyl peptidase/L-asparaginase beta chain] 326 33,950 Active site (1); Chain (2); Erroneous initiation (1); Frameshift (2); Region (2) FUNCTION: Has both L-asparaginase and beta-aspartyl peptidase activity. May be involved in the production of L-aspartate, which can act as an excitatory neurotransmitter in some brain regions. Is highly active with L-Asp beta-methyl ester. Besides, has catalytic activity toward beta-aspartyl dipeptides and their methyl esters, including beta-L-Asp-L-Phe, beta-L-Asp-L-Phe methyl ester (aspartame), beta-L-Asp-L-Ala, beta-L-Asp-L-Leu and beta-L-Asp-L-Lys. Does not have aspartylglucosaminidase activity and is inactive toward GlcNAc-L-Asn. Likewise, has no activity toward glutamine. {ECO:0000250|UniProtKB:Q7L266}. PTM: Cleaved into an alpha and beta chain by autocatalysis; this activates the enzyme. The N-terminal residue of the beta subunit is responsible for the nucleophile hydrolase activity. {ECO:0000250|UniProtKB:Q7L266}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q7L266}. Note=Midpiece of sperm tail. In retina localizes in photoreceptor inner segment (PubMed:27106100). {ECO:0000250|UniProtKB:Q7L266, ECO:0000269|PubMed:27106100}. SUBUNIT: Heterodimer of an alpha and beta chain produced by autocleavage. This heterodimer may then dimerize in turn, giving rise to a heterotetramer. {ECO:0000250|UniProtKB:Q7L266}. TISSUE SPECIFICITY: High expression in the heart and brain while low to minimal expresion in the other tissues. In ocular tissues, high levels is observed in the optic nerve and retina while relatively low levels of expression are detected in the iris-ciliary body, lens or retinal pigment epithelium. {ECO:0000269|PubMed:27106100}. +Q6NXK8 ASIC1_MOUSE Acid-sensing ion channel 1 (ASIC1) (Acid-sensing ion channel) (Amiloride-sensitive cation channel 2, neuronal) (Brain sodium channel 2) (BNaC2) 526 59,668 Alternative sequence (2); Chain (1); Disulfide bond (7); Glycosylation (2); Modified residue (2); Motif (1); Site (3); Topological domain (3); Transmembrane (2) TRANSMEM 46 69 Helical. {ECO:0000250}.; TRANSMEM 426 452 Discontinuously helical. {ECO:0000250}. TOPO_DOM 1 45 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 70 425 Extracellular. {ECO:0000250}.; TOPO_DOM 453 526 Cytoplasmic. {ECO:0000250}. FUNCTION: Proton-gated sodium channel; it is activated by a drop of the extracellular pH and then becomes rapidly desensitized. Generates a biphasic current with a fast inactivating and a slow sustained phase. Has high selectivity for sodium ions and can also transport lithium ions with high efficiency. Can also transport potassium ions, but with lower efficiency. It is nearly impermeable to the larger rubidium and cesium ions. Mediates glutamate-independent Ca(2+) entry into neurons upon acidosis. This Ca(2+) overloading is toxic for cortical neurons and may be in part responsible for ischemic brain injury. Heteromeric channel assembly seems to modulate channel properties. Functions as a postsynaptic proton receptor that influences intracellular Ca(2+) concentration and calmodulin-dependent protein kinase II phosphorylation and thereby the density of dendritic spines. Modulates activity in the circuits underlying innate fear. {ECO:0000269|PubMed:11988176, ECO:0000269|PubMed:12843249, ECO:0000269|PubMed:15369669, ECO:0000269|PubMed:15578512, ECO:0000269|PubMed:17060608, ECO:0000269|PubMed:17662962}. PTM: Phosphorylation by PKA regulates interaction with PRKCABP and subcellular location. Phosphorylation by PKC may regulate the channel (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Localizes in synaptosomes at dendritic synapses of neurons. Colocalizes with DLG4. {ECO:0000269|PubMed:11988176}. SUBUNIT: Homotrimer or heterotrimer with other ASIC proteins (By similarity). Interacts with PRKCABP and ASIC2 (By similarity). Interacts with STOM (PubMed:15471860). {ECO:0000250, ECO:0000269|PubMed:15471860}. DOMAIN: Channel opening involves a conformation change that affects primarily the extracellular domain and the second transmembrane helix and its orientation in the membrane. In the open state, the second transmembrane helix is nearly perpendicular to the plane of the membrane; in the desensitized state it is strongly tilted. Besides, the second transmembrane domain is discontinuously helical in the open state. The GAS motif of the selectivity filter is in an extended conformation, giving rise to a distinct kink in the polypeptide chain. A domain swap between subunits gives rise to a full-length transmembrane helix (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain areas receiving strong excitatory corticofugal input. In hippocampus, expressed in the hilus of the dentate gyrus. In the cerebral cortex expressed in anterior and posterior cingulate cortex, sensory and motor cortices. In the sensory cortex strongest expression is detected in the whisker barrel field. In sensorimotor and cingulate cortex expression is elevated in layer III. Also expressed in basal ganglia, striatum, ventral pallidum, olfactory tubercle, and nucleus accumbens. Weakly expressed in thalamus with the exception of the habenula and the medial septal nuclei. In olfactory bulb, preferentially expressed in the glomerular layer, within glomeruli. Expressed in cerebellum in the molecular and granule cell layers. Strongly expressed in amygdala complex, particularly in the lateral and basolateral nuclei. Isoform 1 is more abundant in brain compared to isoform 2 (at protein level). Expressed in the nodose ganglion and dorsal root ganglion. Expressed in dendritic spine cells. {ECO:0000269|PubMed:11988176, ECO:0000269|PubMed:12843249, ECO:0000269|PubMed:15578512}. +Q7TNS7 ASIC4_MOUSE Acid-sensing ion channel 4 (ASIC4) (Amiloride-sensitive cation channel 4) 539 59,216 Chain (1); Disulfide bond (7); Glycosylation (4); Topological domain (3); Transmembrane (2) TRANSMEM 69 89 Helical. {ECO:0000255}.; TRANSMEM 439 459 Helical. {ECO:0000255}. TOPO_DOM 1 68 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 90 438 Extracellular. {ECO:0000255}.; TOPO_DOM 460 539 Cytoplasmic. {ECO:0000255}. FUNCTION: Probable cation channel with high affinity for sodium. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Homotrimer or heterotrimer with other ASIC proteins. {ECO:0000250}. +Q9R0Y1 ASIC5_MOUSE Acid-sensing ion channel 5 (ASIC5) (Amiloride-sensitive cation channel 5) (Brain-liver-intestine amiloride-sensitive Na(+) channel) (BLINaC) 495 56,523 Chain (1); Disulfide bond (7); Glycosylation (2); Topological domain (3); Transmembrane (2) TRANSMEM 62 82 Helical. {ECO:0000255}.; TRANSMEM 460 480 Helical. {ECO:0000255}. TOPO_DOM 1 61 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 83 459 Extracellular. {ECO:0000255}.; TOPO_DOM 481 495 Cytoplasmic. {ECO:0000255}. FUNCTION: Cation channel that gives rise to very low constitutive currents in the absence of activation. The activated channel exhibits selectivity for sodium and lithium, and is inhibited by amiloride (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Homotrimer or heterotrimer with other ASIC proteins. {ECO:0000250}. TISSUE SPECIFICITY: Detected in cerebellum, brainstem, kidney, liver, hepatocytes, lung, intestine and embryo. In the cerebellum. restricted to interneurons in the granular layer, specifically in GRM1-expressing unipolar brush cells of the vestibulocerebellum. {ECO:0000269|PubMed:10457052, ECO:0000269|PubMed:24663811}. +Q9CR86 CHSP1_MOUSE Calcium-regulated heat stable protein 1 (Calcium-regulated heat-stable protein of 24 kDa) (CRHSP-24) 148 16,062 Chain (1); Domain (1); Initiator methionine (1); Modified residue (8) FUNCTION: Binds mRNA and regulates the stability of target mRNA. {ECO:0000269|PubMed:21078874}. PTM: Can be phosphorylated by DYRK2 (in vitro). Dephosphorylated by calcineurin in a Ca(2+) dependent manner (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21078874}. Cytoplasm, P-body {ECO:0000269|PubMed:21078874}. Cytoplasmic granule {ECO:0000269|PubMed:21078874}. Note=Detected at cytoplasmic stress granules and P-bodies. Detected at exosome granules where mRNA is degraded. SUBUNIT: Homodimer. Interacts with STYX (By similarity). {ECO:0000250}. +Q9EQC0 CHST1_MOUSE Carbohydrate sulfotransferase 1 (EC 2.8.2.21) (Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 1) (GST-1) (Keratan sulfate Gal-6 sulfotransferase) (KS6ST) (KSGal6ST) (KSST) 411 46,904 Chain (1); Glycosylation (4); Motif (1); Nucleotide binding (2); Topological domain (2); Transmembrane (1) TRANSMEM 3 23 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 2 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 24 411 Lumenal. {ECO:0000255}. FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of galactose (Gal) residues of keratan. Has a preference for sulfating keratan sulfate, but it also transfers sulfate to the unsulfated polymer. The sulfotransferase activity on sialyl LacNAc structures is much higher than the corresponding desialylated substrate, and only internal Gal residues are sulfated. May function in the sulfation of sialyl N-acetyllactosamine oligosaccharide chains attached to glycoproteins. Participates in biosynthesis of selectin ligands. Selectin ligands are present in high endothelial cells (HEVs) and play a central role in lymphocyte homing at sites of inflammation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. +Q9R1I1 CHST4_MOUSE Carbohydrate sulfotransferase 4 (EC 2.8.2.-) (Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 3) (GST-3) (High endothelial cells N-acetylglucosamine 6-O-sulfotransferase) (HEC-GlcNAc6ST) (L-selectin ligand sulfotransferase) (LSST) (N-acetylglucosamine 6-O-sulfotransferase 2) (GlcNAc6ST-2) (Gn6st-2) 388 44,636 Chain (1); Glycosylation (3); Nucleotide binding (2); Sequence conflict (4); Topological domain (2); Transmembrane (1) TRANSMEM 8 28 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 7 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 29 388 Lumenal. {ECO:0000255}. FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of non-reducing N-acetylglucosamine (GlcNAc) residues within mucin-associated glycans that ultimately serve as SELL ligands. SELL ligands are present in high endothelial cells (HEVs) and play a central role in lymphocyte homing at sites of inflammation. Participates in biosynthesis of SELL ligand sialyl 6-sulfo Lewis X on SELL counter-receptors SPN/CD43, GLYCAM1 and MADCAM1. Also involved in biosynthesis of SELL ligand recognized by MECA-79 antibody. Plays a central role in lymphocyte trafficking during chronic inflammation. Has a catalytic preference for core 2-branched mucin-type O-glycans. Can use GlcNAcbeta1-6[Galbeta1-3]GalNAc-pNP (core 2), GlcNAcbeta1-6ManOMe and GlcNAcbeta1-2Man oligosaccharide structures as acceptors. Has also activity toward core 3 of GlcNAcbeta1-3GalNAc-pNP. Its substrate specificity may be influenced by its subcellular location. {ECO:0000269|PubMed:10435581, ECO:0000269|PubMed:11520459, ECO:0000269|PubMed:14593101, ECO:0000269|PubMed:14597732, ECO:0000269|PubMed:15111310}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:15111310}; Single-pass type II membrane protein {ECO:0000269|PubMed:15111310}. SUBUNIT: Monomer. {ECO:0000250}. TISSUE SPECIFICITY: Specifically expressed in HEV. {ECO:0000269|PubMed:10435581}. +Q9EP78 CHST7_MOUSE Carbohydrate sulfotransferase 7 (EC 2.8.2.-) (EC 2.8.2.17) (Chondroitin 6-sulfotransferase 2) (C6ST-2) (mC6ST-2) (Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 5) (GST-5) (N-acetylglucosamine 6-O-sulfotransferase 4) (GlcNAc6ST-4) (Gn6st-4) 484 54,767 Chain (1); Glycosylation (3); Modified residue (1); Nucleotide binding (2); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 13 33 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 12 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 34 484 Lumenal. {ECO:0000255}. FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of non-reducing N-acetylglucosamine (GlcNAc) residues. Preferentially acts on mannose-linked GlcNAc. Also able to catalyze the transfer of sulfate to position 6 of the N-acetylgalactosamine (GalNAc) residue of chondroitin. Also acts on core 2 mucin-type oligosaccharide and N-acetyllactosamine oligomer with a lower efficiency. Has weak or no activity toward keratan sulfate and oligosaccharides containing the Galbeta1-4GlcNAc. Catalyzes 6-O-sulfation of beta-benzyl GlcNAc but not alpha- or beta-benzyl GalNAc. {ECO:0000269|PubMed:10913333}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. Highly expressed in kidney. Expressed at lower level in heart, lung and liver. {ECO:0000269|PubMed:10913333}. +Q5XFR0 EPAB2_MOUSE Embryonic polyadenylate-binding protein 2 (Embryonic poly(A)-binding protein 2) (ePABP-2) (ePABP2) (Embryonic poly(A)-binding protein type II) (Poly(A)-binding protein nuclear-like 1) 273 30,263 Chain (1); Domain (1); Frameshift (3); Sequence caution (3); Sequence conflict (1) FUNCTION: Binds the poly(A) tail of mRNA. {ECO:0000250|UniProtKB:Q6TY21}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6TY21}. +Q7TNS8 EPOP_MOUSE Elongin BC and Polycomb repressive complex 2-associated protein (Embryonic stem cell-specific PRC2 subunit p48) (ES cell-specific PRC2 subunit p48) (esPRC2p48) 369 38,095 Chain (1); Compositional bias (1); Erroneous initiation (1); Modified residue (3); Mutagenesis (1); Region (1); Sequence conflict (3) FUNCTION: Scaffold protein that serves as a bridging partner between the PRC2/EED-EZH2 complex and the elongin BC complex: required to fine-tune the transcriptional status of Polycomb group (PcG) target genes in embryonic stem cells (ESCs) (PubMed:27863225, PubMed:27863226). Plays a key role in genomic regions that display both active and repressive chromatin properties in pluripotent stem cells by sustaining low level expression at PcG target genes: acts by recruiting the elongin BC complex, thereby restricting excessive activity of the PRC2/EED-EZH2 complex (PubMed:27863225, PubMed:27863226). Interaction with USP7 promotes deubiquitination of H2B at promoter sites (PubMed:27863226). Acts as a regulator of neuronal differentiation (PubMed:23180766). {ECO:0000269|PubMed:23180766, ECO:0000269|PubMed:27863225, ECO:0000269|PubMed:27863226}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27863225}. Chromosome {ECO:0000269|PubMed:27863225, ECO:0000269|PubMed:27863226}. Note=Localizes at both PRC2/EED-EZH2 sites (H3K27me3) and broad H3K4me3 sites on chromatin of embryonic stem cells (ESCs) (PubMed:27863226). {ECO:0000269|PubMed:27863226}. SUBUNIT: Associates with the PRC2/EED-EZH2 complex (PubMed:21732481, PubMed:27462409, PubMed:27863225, PubMed:27863226). Associates with the elongin BC complex (PubMed:27863225, PubMed:27863226). Interacts with USP7 (PubMed:27863226). {ECO:0000269|PubMed:21732481, ECO:0000269|PubMed:27462409, ECO:0000269|PubMed:27863225, ECO:0000269|PubMed:27863226}. DOMAIN: The BC-box, which mediates binding to the elongin BC complex. {ECO:0000269|PubMed:27863225, ECO:0000269|PubMed:27863226}. TISSUE SPECIFICITY: Highly expressed in embryonic stem cells (ESCs) during embryogenesis and in the adult brain (PubMed:23180766). {ECO:0000269|PubMed:23180766}. +Q8CBF3 EPHB1_MOUSE Ephrin type-B receptor 1 (EC 2.7.10.1) 984 109,881 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Compositional bias (1); Domain (5); Glycosylation (3); Modified residue (2); Motif (1); Nucleotide binding (1); Sequence conflict (5); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 541 563 Helical. {ECO:0000255}. TOPO_DOM 18 540 Extracellular. {ECO:0000255}.; TOPO_DOM 564 984 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor tyrosine kinase which binds promiscuously transmembrane ephrin-B family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Cognate/functional ephrin ligands for this receptor include EFNB1, EFNB2 and EFNB3. During nervous system development, regulates retinal axon guidance redirecting ipsilaterally ventrotemporal retinal ganglion cells axons at the optic chiasm midline. This probably requires repulsive interaction with EFNB2. In the adult nervous system together with EFNB3, regulates chemotaxis, proliferation and polarity of the hippocampus neural progenitors. In addition to its role in axon guidance plays also an important redundant role with other ephrin-B receptors in development and maturation of dendritic spines and synapse formation. May also regulate angiogenesis. More generally, may play a role in targeted cell migration and adhesion. Upon activation by EFNB1 and probably other ephrin-B ligands activates the MAPK/ERK and the JNK signaling cascades to regulate cell migration and adhesion respectively. Involved in the maintenance of the pool of satellite cells (muscle stem cells) by promoting their self-renewal and reducing their activation and differentiation (PubMed:27446912). {ECO:0000269|PubMed:12971893, ECO:0000269|PubMed:14691139, ECO:0000269|PubMed:18057206, ECO:0000269|PubMed:18524895, ECO:0000269|PubMed:27446912}. PTM: Phosphorylated. Autophosphorylation is stimulated by the ligand EFNB1. Required for interaction with SH2 domain-containing interactors, for activation of the MAPK/ERK and JUN signaling cascades and for ubiquitination by CBL (By similarity). {ECO:0000250|UniProtKB:P54762}.; PTM: Ubiquitinated; (EFNB1)ligand-induced poly- and/or multi-ubiquitination by CBL is regulated by SRC and leads to lysosomal degradation. {ECO:0000269|PubMed:18034775}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P54762}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P54762}. Early endosome membrane {ECO:0000250|UniProtKB:P54762}. Cell projection, dendrite {ECO:0000269|PubMed:14691139}. SUBUNIT: Heterotetramer upon binding of the ligand. The heterotetramer is composed of an ephrin dimer and a receptor dimer. Oligomerization is probably required to induce biological responses (By similarity). Interacts with EPHB6; transphosphorylates EPHB6 to form an active signaling complex (By similarity). Interacts with PICK1. Interacts (through Tyr-594) with NCK1 (via SH2 domain); activates the JUN cascade to regulate cell adhesion. The ligand-activated form interacts (through Tyr-928) with GRB7 and GRB10 (via SH2 domains). The ligand-activated form interacts (residues within the catalytic domain) with GRB2 (via SH2 domain). Interacts with GRB2, SHC1 and SRC; activates the MAPK/ERK cascade to regulate cell migration. Interacts with CBL; regulates receptor degradation through ubiquitination. Interacts with ACP1. {ECO:0000250|UniProtKB:P54762, ECO:0000269|PubMed:12223469, ECO:0000269|PubMed:12925710, ECO:0000269|PubMed:18034775, ECO:0000269|PubMed:9430661, ECO:0000269|PubMed:9883737}. TISSUE SPECIFICITY: Expressed in neural stem and progenitor cells in the dentate gyrus (PubMed:18057206). Expressed in myogenic progenitor cells (PubMed:27446912). {ECO:0000269|PubMed:18057206, ECO:0000269|PubMed:27446912}. +Q924X1 EPGN_MOUSE Epigen (Epithelial mitogen) (EPG) 152 16,799 Chain (1); Disulfide bond (3); Domain (1); Glycosylation (2); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 110 130 Helical. {ECO:0000255}. TOPO_DOM 19 109 Extracellular. {ECO:0000255}.; TOPO_DOM 131 152 Cytoplasmic. {ECO:0000255}. FUNCTION: Promotes the growth of epithelial cells. May stimulate the phosphorylation of EGFR and mitogen-activated protein kinases. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed at low levels in testis, heart and liver. {ECO:0000269|PubMed:11278323}. +O54839 EOMES_MOUSE Eomesodermin homolog (T-box brain protein 2) (T-brain-2) (TBR-2) 707 74,801 Alternative sequence (1); Chain (1); Compositional bias (1); DNA binding (1); Modified residue (2); Region (1); Sequence conflict (3) FUNCTION: Functions as a transcriptional activator playing a crucial role during development. Functions in trophoblast differentiation and later in gastrulation, regulating both mesoderm delamination and endoderm specification. Plays a role in brain development being required for the specification and the proliferation of the intermediate progenitor cells and their progeny in the cerebral cortex. Also involved in the differentiation of CD8+ T-cells during immune response regulating the expression of lytic effector genes. {ECO:0000269|PubMed:10716450, ECO:0000269|PubMed:14605368, ECO:0000269|PubMed:18171685, ECO:0000269|PubMed:18940588}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: Expressed in CD8+ T-cells. {ECO:0000269|PubMed:14605368}. +Q99JW5 EPCAM_MOUSE Epithelial cell adhesion molecule (Ep-CAM) (Epithelial glycoprotein 314) (EGP314) (mEGP314) (Protein 289A) (Tumor-associated calcium signal transducer 1) (CD antigen CD326) 315 35,019 Chain (1); Disulfide bond (6); Domain (1); Glycosylation (2); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 267 289 Helical. {ECO:0000255}. TOPO_DOM 24 266 Extracellular. {ECO:0000255}.; TOPO_DOM 290 315 Cytoplasmic. {ECO:0000255}. FUNCTION: May act as a physical homophilic interaction molecule between intestinal epithelial cells (IECs) and intraepithelial lymphocytes (IELs) at the mucosal epithelium for providing immunological barrier as a first line of defense against mucosal infection. Plays a role in embryonic stem cells proliferation and differentiation. Up-regulates the expression of FABP5, MYC and cyclins A and E (By similarity). {ECO:0000250}. PTM: Glycosylation at Asn-198 is crucial for protein stability. {ECO:0000250}. SUBCELLULAR LOCATION: Lateral cell membrane {ECO:0000250|UniProtKB:P16422}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P16422}. Cell junction, tight junction {ECO:0000250|UniProtKB:P16422}. Note=Colocalizes with CLDN7 at the lateral cell membrane and tight junction. {ECO:0000250|UniProtKB:P16422}. SUBUNIT: Monomer. Interacts with phosphorylated CLDN7 (By similarity). {ECO:0000250}. +Q91WL0 ES8L3_MOUSE Epidermal growth factor receptor kinase substrate 8-like protein 3 (EPS8-like protein 3) (Epidermal growth factor receptor pathway substrate 8-related protein 3) (EPS8-related protein 3) 600 68,216 Chain (1); Compositional bias (2); Domain (1); Modified residue (1) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with ABI1. Part of a complex that contains SOS1, ABI1 and EPS8L2. Interacts with FASLG (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Detected in embryonic gut. Detected in adult testis, placenta, adrenal gland and intestine. {ECO:0000269|PubMed:14565974}. +Q69Z69 ESCO1_MOUSE N-acetyltransferase ESCO1 (EC 2.3.1.-) (Establishment of cohesion 1 homolog 1) (ECO1 homolog 1) 843 94,999 Alternative sequence (4); Chain (1); Cross-link (1); Erroneous initiation (2); Frameshift (1); Modified residue (2); Region (3); Sequence conflict (1); Zinc finger (1) FUNCTION: Acetyltransferase required for the establishment of sister chromatid cohesion. Couples the processes of cohesion and DNA replication to ensure that only sister chromatids become paired together. In contrast to the structural cohesins, the deposition and establishment factors are required only during S phase. Acts by mediating the acetylation of cohesin component SMC3. {ECO:0000250|UniProtKB:Q5FWF5}. PTM: Phosphorylated during mitosis. {ECO:0000250|UniProtKB:Q5FWF5}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5FWF5}. Chromosome {ECO:0000250|UniProtKB:Q5FWF5}. Note=Nuclear at interphase, associated with chromosomes during mitosis. {ECO:0000250|UniProtKB:Q5FWF5}. SUBUNIT: The subunit structure is controversial. Monomer. Homodimer. {ECO:0000250|UniProtKB:Q5FWF5}. DOMAIN: The N-terminal region seems to be responsible for association with chromosomes, thus excluding any involvement of the Zn finger in this process. {ECO:0000250|UniProtKB:Q5FWF5}. +Q3LHH8 ESP1_MOUSE Exocrine gland-secreted peptide 1 102 11,346 Beta strand (1); Chain (1); Disulfide bond (1); Helix (4); Mutagenesis (10); Signal peptide (1); Site (1) FUNCTION: Male-specific phermone which is recognized by the Vmn2r116/V2rp5 receptor in the vomeronasal organ (VNO) and enhances female sexual receptive behavior (lordosis) upon male mounting, resulting in successful copulation. {ECO:0000269|PubMed:16208374, ECO:0000269|PubMed:17935991, ECO:0000269|PubMed:20596023, ECO:0000269|PubMed:23576433, ECO:0000269|Ref.3}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16208374, ECO:0000269|PubMed:20596023}. Note=Secreted by the extraorbital lacrimal gland into tears. {ECO:0000269|PubMed:16208374, ECO:0000269|PubMed:20596023}. SUBUNIT: Monomer. {ECO:0000303|PubMed:23576433, ECO:0000305}. TISSUE SPECIFICITY: Expressed in the extraorbital lacrimal gland from where it is secreted into tears. {ECO:0000269|PubMed:16208374}. +Q9QYY7 ESM1_MOUSE Endothelial cell-specific molecule 1 (ESM-1) 184 20,043 Chain (1); Domain (1); Glycosylation (1); Signal peptide (1) FUNCTION: Involved in angiogenesis; promotes angiogenic sprouting. May have potent implications in lung endothelial cell-leukocyte interactions (By similarity). {ECO:0000250}. PTM: O-glycosylated; contains chondroitin sulfate and dermatan sulfate. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +Q8K0G8 ESRP2_MOUSE Epithelial splicing regulatory protein 2 (RNA-binding motif protein 35B) (RNA-binding protein 35B) 717 77,361 Chain (1); Compositional bias (1); Domain (3); Modified residue (2) FUNCTION: mRNA splicing factor that regulates the formation of epithelial cell-specific isoforms. Specifically regulates the expression of FGFR2-IIIb, an epithelial cell-specific isoform of FGFR2. Also regulates the splicing of CD44, CTNND1, ENAH, 3 transcripts that undergo changes in splicing during the epithelial-to-mesenchymal transition (EMT). Acts by directly binding specific sequences in mRNAs. Binds the GU-rich sequence motifs in the ISE/ISS-3, a cis-element regulatory region present in the mRNA of FGFR2 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. TISSUE SPECIFICITY: Epithelial cell-specific. {ECO:0000269|PubMed:14681479}. +O70279 ESS2_MOUSE Splicing factor ESS-2 homolog (ES2 protein) (Expressed sequence 2 embryonic lethal) 479 52,604 Chain (1); Cross-link (1); Modified residue (6); Sequence conflict (4) FUNCTION: May be involved in pre-mRNA splicing. {ECO:0000250|UniProtKB:P34420}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P34420}. SUBUNIT: Identified in the spliceosome C complex. {ECO:0000250|UniProtKB:Q96DF8}. TISSUE SPECIFICITY: In the adult, widely expressed with highest expression in the testis and brain. Also widely expressed in the embryo with highest levels in the anterior pons. +P19785 ESR1_MOUSE Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1) 599 66,955 Chain (1); Compositional bias (1); DNA binding (1); Domain (1); Glycosylation (3); Lipidation (1); Modified residue (6); Mutagenesis (25); Natural variant (1); Region (8); Sequence conflict (1); Zinc finger (2) FUNCTION: Nuclear hormone receptor. The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Ligand-dependent nuclear transactivation involves either direct homodimer binding to a palindromic estrogen response element (ERE) sequence or association with other DNA-binding transcription factors, such as AP-1/c-Jun, c-Fos, ATF-2, Sp1 and Sp3, to mediate ERE-independent signaling. Ligand binding induces a conformational change allowing subsequent or combinatorial association with multiprotein coactivator complexes through LXXLL motifs of their respective components. Mutual transrepression occurs between the estrogen receptor (ER) and NF-kappa-B in a cell-type specific manner. Decreases NF-kappa-B DNA-binding activity and inhibits NF-kappa-B-mediated transcription from the IL6 promoter and displace RELA/p65 and associated coregulators from the promoter. Recruited to the NF-kappa-B response element of the CCL2 and IL8 promoters and can displace CREBBP. Present with NF-kappa-B components RELA/p65 and NFKB1/p50 on ERE sequences. Can also act synergistically with NF-kappa-B to activate transcription involving respective recruitment adjacent response elements; the function involves CREBBP. Can activate the transcriptional activity of TFF1. Also mediates membrane-initiated estrogen signaling involving various kinase cascades. Essential for MTA1-mediated transcriptional regulation of BRCA1 and BCAS3. {ECO:0000269|PubMed:10207113, ECO:0000269|PubMed:10840033}. PTM: Phosphorylated by cyclin A/CDK2 and CK1. Phosphorylation probably enhances transcriptional activity. Dephosphorylation at Ser-122 by PPP5C inhibits its transactivation activity (By similarity). Phosphorylated by LMTK3 (in vitro) (By similarity). {ECO:0000250|UniProtKB:P03372}.; PTM: Ubiquitinated. Deubiquitinated by OTUB1 (By similarity). {ECO:0000250}.; PTM: Dimethylated by PRMT1 at Arg-264. The methylation may favor cytoplasmic localization (By similarity). {ECO:0000250}.; PTM: Palmitoylated at Cys-451 by ZDHHC7 and ZDHHC21. This modification is required for plasma membrane targeting and for rapid intracellular signaling via ERK and AKT kinases and cAMP generation, but not for signaling mediated by the nuclear hormone receptor. {ECO:0000269|PubMed:22031296}.; PTM: Ubiquitinated; regulated by LATS1 via DCAF1 it leads to ESR1 proteasomal degradation. Deubiquitinated by OTUB1. {ECO:0000250|UniProtKB:P03372}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}. Cytoplasm {ECO:0000250}. Golgi apparatus {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Colocalizes with ZDHHC7 and ZDHHC21 in the Golgi apparatus where most probably palmitoylation occurs. Associated with the plasma membrane when palmitoylated. {ECO:0000250}. SUBUNIT: Interacts with BCAS3. Binds DNA as a homodimer (By similarity). Can form a heterodimer with ESR2 (By similarity). Interacts with coactivator NCOA5. Interacts with NCOA7; the interaction is ligand-inducible. Interacts with AKAP13, CUEDC2, HEXIM1, KDM5A, MAP1S, PELP1, SMARD1, and UBE1C. Interacts with MUC1; the interaction is stimulated by 7 beta-estradiol (E2) and enhances ERS1-mediated transcription. Interacts with DNTTIP2, and UIMC1. Interacts with KMT2D/MLL2. Interacts with ATAD2; the interaction is enhanced by estradiol. Interacts with KIF18A and LDB1. Interacts with RLIM (via its C-terminus). Interacts with MACROD1. Interacts with SH2D4A and PLCG. Interacts with SH2D4A; the interaction blocks binding to PLCG and inhibits estrogen-induced cell proliferation. Interacts with DYNLL1. Interacts with CCDC62; the interaction requires estradiol and appears to enhance the transcription of target genes. Interacts with NR2C1; the interaction prevents homodimerization of ESR1 and suppresses its transcriptional activity and cell growth. Interacts with DNAAF4. Interacts with PRMT2. Interacts with PI3KR1 or PIK3R2, SRC and PTK2/FAK1. Interacts with RBFOX2. Interacts with EP300; the interaction is estrogen-dependent and enhanced by CITED1. Interacts with CITED1; the interaction is estrogen-dependent (By similarity). Interacts with FAM120B, FOXL2, PHB2 and SLC30A9. Interacts with coactivators NCOA3 and NCOA6. Interacts with STK3/MST2 only in the presence of SAV1 and vice-versa. Binds to CSNK1D. Interacts with NCOA2; NCOA2 can interact with ESR1 AF-1 and AF-2 domains simultaneously and mediate their transcriptional synergy. Interacts with DDX5. Interacts with NCOA1; the interaction seems to require a self-association of N-terminal and C-terminal regions. Interacts with ZNF366, DDX17, NFKB1, RELA, SP1 and SP3. Interacts with NRIP1 (By similarity). Interacts with GPER1; the interaction occurs in an estrogen-dependent manner. Interacts with CLOCK and the interaction is stimulated by estrogen (By similarity). Interacts with BCAS3. Interacts with TRIP4 (ufmylated); estrogen dependent (By similarity). Interacts with LMTK3; the interaction phosphorylates ESR1 (in vitro) and protects it against proteasomal degradation. Interacts with CCAR2 (via N-terminus) in a ligand-independent manner. Interacts with ZFHX3 (By similarity). Interacts with SFR1 in a ligand-dependent and -independent manner (By similarity). Interacts with DCAF13, LATS1 and DCAF1; regulates ESR1 ubiquitination and ubiquitin-mediated proteasomal degradation (By similarity). Interacts (via DNA-binding domain) with POU4F2 isoform 2 (C-terminus); this interaction increases the estrogen receptor ESR1 transcriptional activity in a DNA- and ligand 17-beta-estradiol-independent manner (PubMed:9448000). Interacts with ESRRB isoform 1 (By similarity). Interacts with UBE3A and WBP2 (By similarity). Interacts with GTF2B (By similarity). Interacts with RBM39 (PubMed:11704680). {ECO:0000250|UniProtKB:P03372, ECO:0000269|PubMed:10207113, ECO:0000269|PubMed:10788465, ECO:0000269|PubMed:10840033, ECO:0000269|PubMed:11704680, ECO:0000269|PubMed:15988012, ECO:0000269|PubMed:17595322, ECO:0000269|PubMed:20005806, ECO:0000269|PubMed:7641693, ECO:0000269|PubMed:9192892, ECO:0000269|PubMed:9448000}. DOMAIN: Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain. The modulating domain, also known as A/B or AF-1 domain has a ligand-independent transactivation function. The C-terminus contains a ligand-dependent transactivation domain, also known as E/F or AF-2 domain which overlaps with the ligand binding domain. AF-1 and AF-2 activate transcription independently and synergistically and act in a promoter- and cell-specific manner (By similarity). {ECO:0000250}. +Q8VCC2 EST1_MOUSE Liver carboxylesterase 1 (EC 3.1.1.1) (Acyl-coenzyme A:cholesterol acyltransferase) (Carboxylesterase 1G) (ES-x) 565 62,680 Active site (3); Chain (1); Disulfide bond (2); Glycosylation (2); Modified residue (1); Sequence conflict (3); Signal peptide (1) FUNCTION: Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. {ECO:0000269|PubMed:9565681}. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250}. Note=Microsomal membrane, lumen of endoplasmic reticulum. {ECO:0000250}. SUBUNIT: Homotrimer and homohexamer. Binds to beta-glucuronidase (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Detected in kidney, liver and lung. {ECO:0000269|PubMed:9565681}. +O08537 ESR2_MOUSE Estrogen receptor beta (ER-beta) (Nuclear receptor subfamily 3 group A member 2) 530 59,070 Alternative sequence (6); Chain (1); DNA binding (1); Domain (1); Erroneous initiation (6); Glycosylation (1); Modified residue (3); Mutagenesis (2); Region (1); Sequence conflict (8); Zinc finger (2) FUNCTION: Nuclear hormone receptor. Binds estrogens with an affinity similar to that of ESR1 (ER-alpha), and activates expression of reporter genes containing estrogen response elements (ERE) in an estrogen-dependent manner. May play a role in ovarian follicular growth and maturation. PTM: Phosphorylation at Ser-87 and Ser-105 recruits NCOA1. {ECO:0000269|PubMed:10230404, ECO:0000269|PubMed:10995228}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Binds DNA as a homodimer. Can form a heterodimer with ESR1. Interacts with NCOA1, NCOA3, NCOA5 and NCOA6 coactivators, leading to a strong increase of transcription of target genes. Interacts with PELP1, UBE1C and AKAP13. Interacts with DNTTIP2 (By similarity). Interacts with CCDC62 in the presence of estradiol/E2; this interaction seems to enhance the transcription of target genes. Interacts with DNAAF4. Interacts with PRMT2. Interacts with CCAR2 (via N-terminus) in a ligand-independent manner (By similarity). Interacts with RBM39, in the presence of estradiol (E2) (PubMed:11704680). {ECO:0000250|UniProtKB:Q62986, ECO:0000250|UniProtKB:Q92731, ECO:0000269|PubMed:11704680}. DOMAIN: Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain. TISSUE SPECIFICITY: Expressed in prostate, ovary, Leydig cells and in epithelium of the efferent ductules and of the initial segment of the epididymis. {ECO:0000269|PubMed:9607809}. +Q91WG0 EST2C_MOUSE Acylcarnitine hydrolase (ACH M1) (EC 3.1.1.28) (Carboxylesterase 2) (CES 2) (Peroxisome proliferator-inducible acylcarnitine hydrolase) 561 62,470 Active site (3); Chain (1); Disulfide bond (2); Motif (1); Signal peptide (1) FUNCTION: Hydrolase with high activity towards palmitoylcarnitine. Is also active with p-nitrophenylacetate and alpha-naphthylacetate. {ECO:0000269|PubMed:12859986}. SUBCELLULAR LOCATION: Microsome {ECO:0000269|PubMed:12859986}. Endoplasmic reticulum {ECO:0000305}. TISSUE SPECIFICITY: Detected in liver (at protein level). {ECO:0000269|PubMed:12859986}. +Q63880 EST3A_MOUSE Carboxylesterase 3A (EC 3.1.1.1) (ES-male) (Liver carboxylesterase 31) (Esterase-31) 571 63,318 Active site (3); Alternative sequence (1); Chain (1); Disulfide bond (2); Erroneous initiation (2); Frameshift (1); Glycosylation (3); Motif (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Note=Microsomal membrane, lumen of endoplasmic reticulum. +Q8VCU1 EST3B_MOUSE Carboxylesterase 3B (EC 3.1.1.1) (Liver carboxylesterase 31-like) 571 63,353 Active site (3); Alternative sequence (1); Chain (1); Compositional bias (1); Disulfide bond (2); Erroneous initiation (2); Glycosylation (1); Motif (1); Signal peptide (1) FUNCTION: Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250}. +Q8R0W5 EST4A_MOUSE Carboxylesterase 4A (EC 3.1.1.-) 563 62,883 Active site (3); Chain (1); Disulfide bond (2); Erroneous initiation (1); Glycosylation (3); Signal peptide (1) FUNCTION: Probable carboxylesterase. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q6AW46 EST5A_MOUSE Carboxylesterase 5A (EC 3.1.1.1) (Carboxylesterase-like urinary excreted protein homolog) (Cauxin) 575 64,167 Active site (3); Chain (1); Disulfide bond (2); Glycosylation (4); Signal peptide (1) FUNCTION: Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. {ECO:0000250}. PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +Q9R0P3 ESTD_MOUSE S-formylglutathione hydrolase (FGH) (EC 3.1.2.12) (Esterase 10) (Esterase D) (Sid 478) 282 31,320 Active site (3); Chain (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (3); Sequence conflict (1) FUNCTION: Serine hydrolase involved in the detoxification of formaldehyde. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Cytoplasmic vesicle {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +P13707 GPDA_MOUSE Glycerol-3-phosphate dehydrogenase [NAD(+)], cytoplasmic (GPD-C) (GPDH-C) (EC 1.1.1.8) 349 37,573 Active site (1); Binding site (7); Chain (1); Erroneous initiation (1); Modified residue (3); Nucleotide binding (1); Region (1); Sequence conflict (5) SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Homodimer. +Q921G7 ETFD_MOUSE Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial (ETF-QO) (ETF-ubiquinone oxidoreductase) (EC 1.5.5.1) (Electron-transferring-flavoprotein dehydrogenase) (ETF dehydrogenase) 616 68,091 Binding site (2); Chain (1); Domain (1); Intramembrane (2); Metal binding (4); Modified residue (6); Nucleotide binding (1); Sequence conflict (2); Transit peptide (1) INTRAMEM 108 129 {ECO:0000250}.; INTRAMEM 427 446 {ECO:0000250}. FUNCTION: Accepts electrons from ETF and reduces ubiquinone. {ECO:0000250}. PTM: Acetylation of Lys-95 and Lys-222 is observed in liver mitochondria from fasted mice but not from fed mice. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. +Q80ZM3 ETKMT_MOUSE Electron transfer flavoprotein beta subunit lysine methyltransferase (EC 2.1.1.-) (ETFB lysine methyltransferase) (ETFB-KMT) (Protein N-lysine methyltransferase METTL20) 255 28,639 Chain (1); Sequence conflict (1); Transit peptide (1) FUNCTION: Protein-lysine methyltransferase that selectively trimethylates the flavoprotein ETFB in mitochondria. Thereby, may negatively regulate the function of ETFB in electron transfer from Acyl-CoA dehydrogenases. {ECO:0000269|PubMed:25023281}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8IXQ9}. Mitochondrion matrix {ECO:0000250|UniProtKB:Q8IXQ9}. Note=Concentrated in cytoplasmic granular foci. {ECO:0000250|UniProtKB:Q8IXQ9}. SUBUNIT: Interacts with HSPD1; this protein may possibly be a methylation substrate. {ECO:0000250|UniProtKB:Q8IXQ9}. +P15037 ETS2_MOUSE Protein C-ets-2 468 52,827 Chain (1); DNA binding (1); Domain (1); Modified residue (5) FUNCTION: Transcription factor activating transcription. Binds specifically the GGA DNA motif in gene promoters and stimulates transcription of those genes (By similarity). {ECO:0000250}. PTM: Phosphorylation by CDK10 at Ser-220 and Ser-225 creates a phosphodegron that targets ETS2 for proteasomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. +P97360 ETV6_MOUSE Transcription factor ETV6 (ETS translocation variant 6) (ETS-related protein Tel1) (Tel) 485 56,406 Beta strand (5); Chain (1); Cross-link (5); DNA binding (1); Domain (1); Helix (6); Modified residue (9); Turn (3) FUNCTION: Transcriptional repressor; binds to the DNA sequence 5'-CCGGAAGT-3'. Plays a role in hematopoiesis and malignant transformation. {ECO:0000250|UniProtKB:P41212}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00237}. SUBUNIT: Can form homodimers or heterodimers with TEL2 or FLI1. Interacts with L3MBTL1 and HDAC9 (By similarity). {ECO:0000250}. +Q8K2Y3 EVA1B_MOUSE Protein eva-1 homolog B (Protein FAM176B) 164 18,291 Chain (1); Modified residue (3); Transmembrane (1) TRANSMEM 29 49 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q8BI71 EX3L1_MOUSE Exocyst complex component 3-like protein 739 81,204 Chain (1); Region (1) FUNCTION: As part of the exocyst, may play a role in regulated exocytosis of insulin granules. {ECO:0000269|PubMed:18480549}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:18480549}. Note=Colocalizes with insulin granules. SUBUNIT: Interacts with EXOC2, EXOC4 and EXOC5; may be part of the exocyst. {ECO:0000269|PubMed:18480549}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:18480549}. +Q6DIA2 EX3L4_MOUSE Exocyst complex component 3-like protein 4 721 81,035 Chain (1); Modified residue (1); Sequence conflict (2) +Q8BMP4 GPER1_MOUSE G-protein coupled estrogen receptor 1 (Chemoattractant receptor-like 2) (G protein-coupled estrogen receptor 1) (G-protein coupled receptor 30) (Membrane estrogen receptor) (mER) 375 42,479 Chain (1); Disulfide bond (1); Glycosylation (2); Modified residue (1); Mutagenesis (1); Sequence conflict (2); Topological domain (8); Transmembrane (7) TRANSMEM 63 84 Helical; Name=1. {ECO:0000255}.; TRANSMEM 97 120 Helical; Name=2. {ECO:0000255}.; TRANSMEM 133 153 Helical; Name=3. {ECO:0000255}.; TRANSMEM 176 194 Helical; Name=4. {ECO:0000255}.; TRANSMEM 221 236 Helical; Name=5. {ECO:0000255}.; TRANSMEM 260 280 Helical; Name=6. {ECO:0000255}.; TRANSMEM 307 327 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 62 Extracellular. {ECO:0000255}.; TOPO_DOM 85 96 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 121 132 Extracellular. {ECO:0000255}.; TOPO_DOM 154 175 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 195 220 Extracellular. {ECO:0000255}.; TOPO_DOM 237 259 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 281 306 Extracellular. {ECO:0000255}.; TOPO_DOM 328 375 Cytoplasmic. {ECO:0000255}. FUNCTION: G-protein coupled estrogen receptor that binds to 17-beta-estradiol (E2) with high affinity, leading to rapid and transient activation of numerous intracellular signaling pathways. Stimulates cAMP production, calcium mobilization and tyrosine kinase Src inducing the release of heparin-bound epidermal growth factor (HB-EGF) and subsequent transactivation of the epidermal growth factor receptor (EGFR), activating downstream signaling pathways such as PI3K/Akt and ERK/MAPK. Mediates pleiotropic functions among others in the cardiovascular, endocrine, reproductive, immune and central nervous systems. Has a role in cardioprotection by reducing cardiac hypertrophy and perivascular fibrosis in a RAMP3-dependent manner. Regulates arterial blood pressure by stimulating vasodilation and reducing vascular smooth muscle and microvascular endothelial cell proliferation. Plays a role in blood glucose homeostasis contributing to the insulin secretion response by pancreatic beta cells. Triggers mitochondrial apoptosis during pachytene spermatocyte differentiation. Stimulates uterine epithelial cell proliferation. Enhances uterine contractility in response to oxytocin. Contributes to thymic atrophy by inducing apoptosis. Attenuates TNF-mediated endothelial expression of leukocyte adhesion molecules. Promotes neuritogenesis in developing hippocampal neurons. Plays a role in acute neuroprotection against NMDA-induced excitotoxic neuronal death. Increases firing activity and intracellular calcium oscillations in luteinizing hormone-releasing hormone (LHRH) neurons. Inhibits early osteoblast proliferation at growth plate during skeletal development. Inhibits mature adipocyte differentiation and lipid accumulation. Involved in the recruitment of beta-arrestin 2 ARRB2 at the plasma membrane in epithelial cells. Functions also as a receptor for aldosterone mediating rapid regulation of vascular contractibility through the PI3K/ERK signaling pathway. Involved in cancer progression regulation. Stimulates cancer-associated fibroblast (CAF) proliferation by a rapid genomic response through the EGFR/ERK transduction pathway. Associated with EGFR, may act as a transcription factor activating growth regulatory genes (c-fos, cyclin D1). Promotes integrin alpha-5/beta-1 and fibronectin (FN) matrix assembly in breast cancer cells. {ECO:0000269|PubMed:18063692, ECO:0000269|PubMed:18845638, ECO:0000269|PubMed:19179659, ECO:0000269|PubMed:19430488, ECO:0000269|PubMed:20734455, ECO:0000269|PubMed:21273787, ECO:0000269|PubMed:21673097, ECO:0000269|PubMed:22492045, ECO:0000269|PubMed:23545157, ECO:0000269|PubMed:23674134, ECO:0000269|PubMed:23871778}. PTM: Ubiquitinated; ubiquitination occurs at the plasma membrane and leads to proteasome-mediated degradation. {ECO:0000250}.; PTM: N-glycosylated. {ECO:0000269|PubMed:21149639}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm. Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Early endosome {ECO:0000250}. Recycling endosome {ECO:0000250}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Cell projection, dendritic spine membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell projection, axon {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250}. Mitochondrion membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Colocalized with BSN to the active zone of presynaptic density. Colocalized with DLG4/PSD95 and neurabin-2 PPP1R9B in neuronal synaptosomes. Endocytosed in an agonist- and arrestin-independent manner. Colocalized with RAMP3 and clathrin-coated pits at the plasma membrane. Colocalized with transferrin receptor at the plasma membrane and perinuclear region. Accumulated and colocalized with RAB11 proteins in recycling endosomes and trans-Golgi network (TGN), but does neither recycle back to the cell surface nor traffics to late endosome or lysosome. Colocalized with calnexin in the endoplasmic reticulum. Traffics to intracellular sites via cytokeratin intermediate filaments like KRT7 and KRT8 after constitutive endocytosis in epithelial cells. Colocalized with EGFR in the nucleus of agonist-induced cancer-associated fibroblasts (CAF) (By similarity). {ECO:0000250}. SUBUNIT: Interacts with RAMP3. Interacts with KRT7 and KRT8. Interacts with EGFR; the interaction increases after agonist-induced stimulation in cancer-associated fibroblasts (CAF). Interacts with EGFR and ESR1. Interacts (via C-terminus tail motif) with DLG4 (via N-terminus tandem pair of PDZ domains); the interaction is direct and induces the increase of GPER1 protein levels residing at the plasma membrane surface in a estradiol-independent manner (By similarity). Homodimer (Probable). Heterodimer; heterodimerizes with other G-protein-coupled receptor (GPCRs) like CRHR1, HTR1A and PAQR8. {ECO:0000250, ECO:0000269|PubMed:23300088, ECO:0000305}. TISSUE SPECIFICITY: Expressed in brain, heart, spleen, preadipocytes, mature adipocytes and primary hippocampal neurons. Expressed in neurons of the hippocampus, hypothalamic paraventricular nucleus (PVH), supraoptic nucleus (SON) and the median eminence. Expressed in the nucleus ambiguous (at protein level). Expressed in brain, pituitary gland, adrenal medulla, renal pelvis, ovary, endothelial cells, visceral fat tissues and islets of Langerhans. {ECO:0000269|PubMed:19420011, ECO:0000269|PubMed:21273787, ECO:0000269|PubMed:22306576, ECO:0000269|PubMed:23545157, ECO:0000269|PubMed:23674134, ECO:0000269|PubMed:23871778}. +Q9CXY9 GPI8_MOUSE GPI-anchor transamidase (GPI transamidase) (EC 3.-.-.-) (Phosphatidylinositol-glycan biosynthesis class K protein) (PIG-K) 395 44,895 Active site (2); Chain (1); Disulfide bond (1); Region (1); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 368 388 Helical. {ECO:0000255}. TOPO_DOM 28 367 Lumenal. {ECO:0000255}.; TOPO_DOM 389 395 Cytoplasmic. {ECO:0000255}. Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis. FUNCTION: Mediates GPI anchoring in the endoplasmic reticulum, by replacing a protein's C-terminal GPI attachment signal peptide with a pre-assembled GPI. During this transamidation reaction, the GPI transamidase forms a carbonyl intermediate with the substrate protein (By similarity). {ECO:0000250}. PTM: The disulfide bond between PIGK/GPI8 and PIGT is important for normal enzyme activity. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Forms a complex with PIGT, PIGS, PIGU and GAA1. {ECO:0000250}. +O88186 GPIX_MOUSE Platelet glycoprotein IX (GP-IX) (GPIX) (Glycoprotein 9) (CD antigen CD42a) 177 19,664 Chain (1); Domain (2); Glycosylation (1); Repeat (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 148 168 Helical. {ECO:0000255}. TOPO_DOM 17 147 Extracellular. {ECO:0000255}.; TOPO_DOM 169 177 Cytoplasmic. {ECO:0000255}. FUNCTION: The GPIb-V-IX complex functions as the vWF receptor and mediates vWF-dependent platelet adhesion to blood vessels. The adhesion of platelets to injured vascular surfaces in the arterial circulation is a critical initiating event in hemostasis. GP-IX may provide for membrane insertion and orientation of GP-Ib (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Two GP-Ib beta are disulfide-linked to one GP-Ib alpha. GP-IX is complexed with the GP-Ib heterodimer via a non covalent linkage (By similarity). {ECO:0000250}. +Q56A08 GPKOW_MOUSE G-patch domain and KOW motifs-containing protein (Protein MOS2 homolog) 488 53,832 Chain (1); Domain (3); Erroneous initiation (4); Initiator methionine (1); Modified residue (4) FUNCTION: RNA-binding protein involved in pre-mRNA splicing. {ECO:0000250|UniProtKB:Q92917}. PTM: Phosphorylation regulates its ability to bind RNA. {ECO:0000250|UniProtKB:Q92917}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92917}. SUBUNIT: Interacts with PRKX, PRKACB and DHX16. {ECO:0000250|UniProtKB:Q92917}. +P35802 GPM6A_MOUSE Neuronal membrane glycoprotein M6-a (M6a) 278 31,149 Chain (1); Disulfide bond (1); Glycosylation (2); Modified residue (3); Topological domain (5); Transmembrane (4) TRANSMEM 23 43 Helical. {ECO:0000255}.; TRANSMEM 85 105 Helical. {ECO:0000255}.; TRANSMEM 128 148 Helical. {ECO:0000255}.; TRANSMEM 214 234 Helical. {ECO:0000255}. TOPO_DOM 1 22 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 44 84 Extracellular. {ECO:0000255}.; TOPO_DOM 106 127 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 149 213 Extracellular. {ECO:0000250}.; TOPO_DOM 235 278 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in neuronal differentiation, including differentiation and migration of neuronal stem cells. Plays a role in neuronal plasticity and is involved in neurite and filopodia outgrowth, filopodia motility and probably synapse formation. Gpm6a-induced filopodia formation involves mitogen-activated protein kinase (MAPK) and Src signaling pathways. Conflictingly, PubMed:22162747 reports that induced cellular protrusions are simple membrane-wrapped tubules without actin or tubulin-based cytoskeletons and with Gpm6a gliding along membrane edges indicative for a function in actin-independent membrane deformation. May be involved in neuronal NGF-dependent Ca(2+) influx. May be involved in regulation of endocytosis and intracellular trafficking of G-protein-coupled receptors (GPCRs); enhances internalization and recycling of mu-type opioid receptor. {ECO:0000269|PubMed:18522499, ECO:0000269|PubMed:18776950, ECO:0000269|PubMed:22162747}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21714103}; Multi-pass membrane protein {ECO:0000269|PubMed:21714103}. Cell projection, axon {ECO:0000269|PubMed:21714103}. Cell projection, dendritic spine {ECO:0000250}. Cell projection, filopodium {ECO:0000250}. Note=Localizes to cholesterol-rich lipid rafts of the plasma membrane of hippocampal neurons. Localized to plasma membrane of cell bodies and neurites of hippocampal neurons. Localized in membrane protrusions (filopodia and spines) of primary hippocampal neurons (By similarity). Localized to the growth cone edge membrane of elongating axons. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed in the CNS. Found especially in the granule cell layer of the cerebellum but not in the molecular layer or white matter. Expressed in the immature embryonic retina including the nerve fiber layer (NFL), inner plexiform layer (IPL), and outer plexiform layer (OPL). Weakly expressed in processes of Mueller glia cells. {ECO:0000269|PubMed:18776950}. +P35803 GPM6B_MOUSE Neuronal membrane glycoprotein M6-b (M6b) 328 36,210 Alternative sequence (8); Chain (1); Glycosylation (2); Modified residue (3); Sequence conflict (1); Transmembrane (4) TRANSMEM 71 91 Helical. {ECO:0000255}.; TRANSMEM 130 150 Helical. {ECO:0000255}.; TRANSMEM 176 196 Helical. {ECO:0000255}.; TRANSMEM 265 285 Helical. {ECO:0000255}. FUNCTION: May be involved in neural development. Involved in regulation of osteoblast function and bone formation. Involved in matrix vesicle release by osteoblasts; this function seems to involve maintenance of the actin cytoskeleton. May be involved in cellular trafficking of SERT and thereby in regulation of serotonin uptake. {ECO:0000269|PubMed:18581270}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Cell membrane. Note=Colocalizes with SERT at the plasma membrane. SUBUNIT: Interacts with SERT. {ECO:0000269|PubMed:18581270}. TISSUE SPECIFICITY: Widely expressed. In the brain, expressed in neurons and oligodendrocytes. {ECO:0000269|PubMed:11749036}. +Q9CXP9 EXO5_MOUSE Exonuclease V (Exo V) (mExo5) (EC 3.1.-.-) (Defects in morphology protein 1 homolog) 373 41,624 Chain (1); Erroneous gene model prediction (2); Metal binding (4) FUNCTION: Single-stranded DNA (ssDNA) bidirectional exonuclease involved in DNA repair. Probably involved in DNA repair following ultraviolet (UV) irradiation and interstrand cross-links (ICLs) damage. Has both 5'-3' and 3'-5' exonuclease activities with a strong preference for 5'-ends. Acts as a sliding exonuclease that loads at ssDNA ends and then slides along the ssDNA prior to cutting; however the sliding and the 3'-5' exonuclease activities are abolished upon binding to the replication protein A (RPA) complex that enforces 5'-directionality activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Note=Localizes to repair foci in response to DNA damage. {ECO:0000250}. SUBUNIT: Monomer; monomeric form has weak exonuclease activity. Homodimer; homodimeric form is unsure but has much higher exonuclease activity, suggesting that it could homodimerize upon DNA-binding. Interacts with the replication protein A (RPA) complex (By similarity). {ECO:0000250}. +O35382 EXOC4_MOUSE Exocyst complex component 4 (Exocyst complex component Sec8) 975 110,545 Chain (1); Coiled coil (1); Initiator methionine (1); Modified residue (6); Sequence conflict (4) FUNCTION: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. SUBCELLULAR LOCATION: Midbody, Midbody ring {ECO:0000250|UniProtKB:Q96A65}. Cell projection {ECO:0000250|UniProtKB:Q62824}. Note=Colocalizes with CNTRL/centriolin at the midbody ring (By similarity). Localizes at the leading edge of migrating cells (By similarity). {ECO:0000250|UniProtKB:Q62824, ECO:0000250|UniProtKB:Q96A65}. SUBUNIT: The exocyst complex is composed of EXOC1, EXOC2, EXOC3, EXOC4, EXOC5, EXOC6, EXOC7 and EXOC8 (By similarity). Interacts with BIRC6/bruce (By similarity). Interacts with MYRIP. Interacts with SH3BP1; required for the localization of both SH3BP1 and the exocyst to the leading edge of migrating cells (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q96A65, ECO:0000269|PubMed:17827149}. +Q3TPX4 EXOC5_MOUSE Exocyst complex component 5 (Exocyst complex component Sec10) 708 81,738 Chain (1); Coiled coil (1); Initiator methionine (1); Modified residue (5); Sequence conflict (1) FUNCTION: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O00471}. Midbody {ECO:0000250|UniProtKB:O00471}. Note=Localization at the midbody requires the presence of RALA, EXOC2 and EXOC3. {ECO:0000250|UniProtKB:O00471}. SUBUNIT: The exocyst complex is composed of EXOC1, EXOC2, EXOC3, EXOC4, EXOC5, EXOC6, EXOC7 and EXOC8 (By similarity). Interacts with EXOC3L1 (PubMed:18480549). {ECO:0000250|UniProtKB:P97878, ECO:0000269|PubMed:18480549}. +Q9D4H1 EXOC2_MOUSE Exocyst complex component 2 (Exocyst complex component Sec5) 924 103,959 Beta strand (9); Chain (1); Coiled coil (1); Domain (1); Modified residue (5); Turn (2) FUNCTION: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. {ECO:0000250}. SUBCELLULAR LOCATION: Midbody, Midbody ring {ECO:0000250|UniProtKB:Q96KP1}. Note=Recruitment to the midbody does not require RALA, nor RALB. Colocalizes with CNTRL/centriolin at the midbody ring. {ECO:0000250|UniProtKB:Q96KP1}. SUBUNIT: The exocyst complex is composed of EXOC1, EXOC2, EXOC3, EXOC4, EXOC5, EXOC6, EXOC7 and EXOC8 (By similarity). Interacts with EXOC3L1. Interacts with GNEFR/DELGEF; this interaction occurs only in the presence of magnesium or manganese and is stimulated by dCTP or GTP (PubMed:18480549). Interacts with GNEFR/DELGEF. Interaction with GNEFR occurs only in the presence of magnesium or manganese and is stimulated by dCTP or GTP (By similarity). Interacts with RALA and RALB (By similarity). {ECO:0000250|UniProtKB:O54921, ECO:0000250|UniProtKB:Q96KP1, ECO:0000269|PubMed:18480549}. DOMAIN: Interacts with RALA through the TIG domain. +Q8R313 EXOC6_MOUSE Exocyst complex component 6 (Exocyst complex component Sec15A) (SEC15-like protein 1) 802 93,077 Chain (1); Erroneous initiation (1) FUNCTION: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. Together with RAB11A, RAB3IP, RAB8A, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O54923}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O54923}. Cell projection, growth cone {ECO:0000250|UniProtKB:O54923}. Midbody, Midbody ring {ECO:0000250|UniProtKB:Q8TAG9}. Note=Perinuclear in undifferentiated cells. Redistributes to growing neurites and growth cones during neuronal differentiation (By similarity). Colocalizes with CNTRL/centriolin at the midbody ring (By similarity). {ECO:0000250|UniProtKB:O54923, ECO:0000250|UniProtKB:Q8TAG9}. SUBUNIT: The exocyst complex is composed of EXOC1, EXOC2, EXOC3, EXOC4, EXOC5, EXOC6, EXOC7 and EXOC8 (By similarity). Interacts with CNTRL (By similarity). Interacts with RAB11A in a GTP-dependent manner. {ECO:0000250, ECO:0000250|UniProtKB:O54923, ECO:0000269|PubMed:15292201}. +O35250 EXOC7_MOUSE Exocyst complex component 7 (Exocyst complex component Exo70) 697 79,960 Alternative sequence (2); Beta strand (1); Chain (1); Coiled coil (2); Helix (27); Modified residue (1); Region (1); Sequence conflict (5); Turn (4) FUNCTION: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. In adipocytes, plays a crucial role in targeting SLC2A4 vesicle to the plasma membrane in response to insulin, perhaps directing the vesicle to the precise site of fusion. {ECO:0000269|PubMed:12687004}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12687004}. Cell membrane {ECO:0000269|PubMed:12687004}; Peripheral membrane protein. Midbody, Midbody ring {ECO:0000250|UniProtKB:Q9UPT5}. Note=Translocates, as a preformed complex with SEC6 and SEC8, to the plasma membrane in response to insulin through the activation of ARHQ (PubMed:12687004). Colocalizes with CNTRL/centriolin at the midbody ring (By similarity). {ECO:0000250|UniProtKB:Q9UPT5, ECO:0000269|PubMed:12687004}. SUBUNIT: The exocyst complex is composed of EXOC1, EXOC2, EXOC3, EXOC4, EXOC5, EXOC6, EXOC7 and EXOC8. Interacts with RAB11FIP3 (By similarity). Interacts with ARHQ in a GTP-dependent manner. {ECO:0000250, ECO:0000269|PubMed:12687004}. DOMAIN: The C-terminus is required for translocation to the plasma membrane. +Q9CRA8 EXOS5_MOUSE Exosome complex component RRP46 (Exosome component 5) (Ribosomal RNA-processing protein 46) 235 25,194 Chain (1); Modified residue (2); Sequence conflict (1) FUNCTION: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Component of the RNA exosome complex. Specifically part of the catalytically inactive RNA exosome core (Exo-9) complex which is believed to associate with catalytic subunits EXOSC10, and DIS3 or DIS3L in cytoplasmic- and nuclear-specific RNA exosome complex forms. Exo-9 is formed by a hexameric ring of RNase PH domain-containing subunits specifically containing the heterodimers EXOSC4-EXOSC9, EXOSC5-EXOSC8 and EXOSC6-EXOSC7, and peripheral S1 domain-containing components EXOSC1, EXOSC2 and EXOSC3 located on the top of the ring structure. Interacts with EXOSC1. Interacts with GTPBP1 (By similarity). Interacts with ZC3HAV1 (By similarity). Interacts with DDX17 only in the presence of ZC3HAV1 in an RNA-independent manner (By similarity). {ECO:0000250}. +Q9D753 EXOS8_MOUSE Exosome complex component RRP43 (Exosome component 8) (Ribosomal RNA-processing protein 43) 276 29,949 Chain (1); Initiator methionine (1); Modified residue (1) FUNCTION: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. EXOSC8 binds to ARE-containing RNAs (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Component of the RNA exosome complex. Specifically part of the catalytically inactive RNA exosome core (Exo-9) complex which is believed to associate with catalytic subunits EXOSC10, and DIS3 or DIS3L in cytoplasmic- and nuclear-specific RNA exosome complex forms. Exo-9 is formed by a hexameric ring of RNase PH domain-containing subunits specifically containing the heterodimers EXOSC4-EXOSC9, EXOSC5-EXOSC8 and EXOSC6-EXOSC7, and peripheral S1 domain-containing components EXOSC1, EXOSC2 and EXOSC3 located on the top of the ring structure (By similarity). {ECO:0000250}. +Q0VAV2 EXPH5_MOUSE Exophilin-5 (Synaptotagmin-like protein homolog lacking C2 domains b) (SlaC2-b) (Slp homolog lacking C2 domains b) 1960 217,643 Chain (1); Domain (1); Modified residue (10); Sequence conflict (2) FUNCTION: May act as Rab effector protein and play a role in vesicle trafficking. {ECO:0000250|UniProtKB:Q8NEV8}. SUBUNIT: Interacts with RAB27A. {ECO:0000269|PubMed:11773082}. +Q8BQS4 F102B_MOUSE Protein FAM102B 339 36,514 Chain (1); Domain (1); Erroneous initiation (1); Modified residue (6) +Q78TU8 F107A_MOUSE Actin-associated protein FAM107A 144 17,510 Chain (1); Coiled coil (1); Motif (1) FUNCTION: Stress-inducible actin-binding protein that plays a role in synaptic and cognitive functions by modulating actin filamentous (F-actin) dynamics (PubMed:21969592). Mediates polymerization of globular actin to F-actin (PubMed:21969592). Also binds to, stabilizes and bundles F-actin (PubMed:21969592). Involved in synaptic function by regulating neurite outgrowth in an actin-dependent manner and for the acquisition of hippocampus-dependent cognitive function, such as learning and long-term memory (PubMed:21969592). Plays a role in the actin and microtubule cytoskeleton organization; negatively regulates focal adhesion (FA) assembly promoting malignant glial cell migration in an actin-, microtubule- and MAP1A-dependent manner. Also involved in neuroblastoma G1/S phase cell cycle progression and cell proliferation inhibition by stimulating ubiquitination of NF-kappa-B subunit RELA and NF-kappa-B degradation in a COMMD1- and actin-dependent manner. May play a role in tumor development (By similarity). {ECO:0000250|UniProtKB:O95990, ECO:0000269|PubMed:21969592}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O95990}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000269|PubMed:21969592}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:O95990}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:O95990}. Cell junction, synapse {ECO:0000269|PubMed:21969592}. Note=Colocalizes with F-actin (PubMed:21969592). Colocalizes with F-actin and COMMD1 in the nucleus. Colocalizes with MAP1A along actin stress fibers and membrane ruffles (By similarity). {ECO:0000250|UniProtKB:O95990, ECO:0000269|PubMed:21969592}. SUBUNIT: Interacts with ACTB (PubMed:21969592). Interacts with F-actin (PubMed:21969592). Interacts with PRDX1 (PubMed:21969592). Interacts with COMMD1; this interaction stabilizes COMMD1 in the nucleus (By similarity). Interacts with MAP1A (By similarity). {ECO:0000250|UniProtKB:O95990, ECO:0000269|PubMed:21969592}. TISSUE SPECIFICITY: Expressed in septum, the neocortex, the CA3 region of the hippocampus and the cerebellum (at protein level). {ECO:0000269|PubMed:21969592}. +Q9DB52 F122A_MOUSE Protein FAM122A 284 30,270 Chain (1); Compositional bias (1); Cross-link (1); Modified residue (14); Sequence conflict (2) FUNCTION: Acts as an inhibitor of serine/threonine-protein phosphatase 2A (PP2A) activity. Potentiates ubiquitin-mediated proteasomal degradation of serine/threonine-protein phosphatase 2A catalytic subunit alpha (PPP2CA). {ECO:0000250|UniProtKB:Q96E09}. SUBUNIT: Interacts with PPP2CA, PPP2R2A and PPP2R1A. {ECO:0000250|UniProtKB:Q96E09}. +Q8VE94 F110C_MOUSE Protein FAM110C 421 45,319 Chain (1); Modified residue (1); Sequence conflict (1) FUNCTION: May play a role in microtubule organization. May play a role in cell spreading and cell migration of epithelial cells; the function may involve the AKT1 signaling pathway. {ECO:0000250|UniProtKB:Q1W6H9}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q1W6H9}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q1W6H9}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q1W6H9}. Nucleus {ECO:0000250|UniProtKB:Q1W6H9}. Note=Colocalizes with microtubules during interphase. Detected at the mitotic spindle poles. Colocalizes with AKT1 at the cell cortex. {ECO:0000250|UniProtKB:Q1W6H9}. SUBUNIT: Interacts with AKT1; the interaction is transient and follows AKT1 activation. Interacts with PPP2CA and alpha-tubulin. {ECO:0000250|UniProtKB:Q1W6H9}. +Q9DAI6 F135B_MOUSE Protein FAM135B 1403 155,524 Chain (1); Erroneous initiation (2); Modified residue (2) +Q8BLQ0 F124B_MOUSE Protein FAM124B 456 52,079 Chain (1) SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23285124}. SUBUNIT: Interacts with CHD7 and CHD8. {ECO:0000250|UniProtKB:Q9H5Z6}. TISSUE SPECIFICITY: Expressed strongly in lung, at slightly lower levels in heart, kidney, brain and testis, and weakly in liver (at protein level). In brain, highly expressed in cortex, hippocampus, dentate gyrus, caudate putamen and cerebellum (at protein level). {ECO:0000269|PubMed:23285124}. +Q9CR98 F136A_MOUSE Protein FAM136A 138 15,674 Chain (1); Initiator methionine (1); Modified residue (3) +Q8C729 F126B_MOUSE Protein FAM126B 530 58,587 Alternative sequence (1); Chain (1); Modified residue (8); Sequence conflict (1) FUNCTION: Component of a complex required to localize phosphatidylinositol 4-kinase (PI4K) to the plasma membrane. {ECO:0000250|UniProtKB:Q8IXS8}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9BYI3}. Cell membrane {ECO:0000250|UniProtKB:Q9BYI3}. SUBUNIT: Component of a phosphatidylinositol 4-kinase (PI4K) complex, composed of PI4KA, EFR3 (EFR3A or EFR3B), TTC7 (TTC7A or TTC7B) and FAM126 (FAM126A or FAM126B). {ECO:0000250|UniProtKB:Q8IXS8}. TISSUE SPECIFICITY: Expressed in the central nervous system. Expressed at much lower level in oligodendrocytes than in neurons. {ECO:0000269|PubMed:26571211}. +Q8BWU3 F131A_MOUSE Protein FAM131A 361 39,033 Chain (1) +Q3TY60 F131B_MOUSE Protein FAM131B 332 35,958 Alternative sequence (2); Chain (1); Compositional bias (1); Erroneous initiation (2); Modified residue (10) +Q8CFV2 F149A_MOUSE Protein FAM149A 787 85,100 Chain (1); Compositional bias (1) +Q9CVI2 F133B_MOUSE Protein FAM133B 245 27,952 Alternative sequence (2); Chain (1); Compositional bias (2); Modified residue (5); Sequence conflict (1) +A2BDP1 F155B_MOUSE Transmembrane protein FAM155B (Protein TED) (Transmembrane protein 28) 471 52,389 Chain (1); Compositional bias (3); Glycosylation (1); Transmembrane (2) TRANSMEM 47 67 Helical. {ECO:0000255}.; TRANSMEM 432 452 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9D6U8 F162A_MOUSE Protein FAM162A (E2-induced gene 5 protein homolog) (Growth and transformation-dependent protein) (HGTD-P) 155 17,725 Chain (1); Region (1); Transmembrane (1) TRANSMEM 104 121 Helical. {ECO:0000255}. FUNCTION: Proposed to be involved in regulation of apoptosis; the exact mechanism may differ between cell types/tissues. May be involved in hypoxia-induced cell death of transformed cells implicating cytochrome C release and caspase activation (such as CASP9) and inducing mitochondrial permeability transition. May be involved in hypoxia-induced cell death of neuronal cells probably by promoting release of AIFM1 from mitochondria to cytoplasm and its translocation to the nucleus; however, the involvement of caspases has been reported conflictingly. {ECO:0000269|PubMed:15082785, ECO:0000269|PubMed:17316997}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Mitochondrion {ECO:0000250}. SUBUNIT: Interacts with HSP90AB1; HSP90AB1 is essential for FAM162A mitochondrial localization and pro-apoptotic activity. Interacts with VDAC2; the interaction is probably involved in inducing mitochondrial permability transition (By similarity). {ECO:0000250}. +Q9CX19 F162B_MOUSE Protein FAM162B 157 17,686 Chain (1); Transmembrane (1) TRANSMEM 104 123 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q8CAA5 F163A_MOUSE Protein FAM163A 168 17,839 Chain (1); Transmembrane (1) TRANSMEM 6 26 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q8BUM6 F163B_MOUSE Protein FAM163B 167 18,306 Chain (1); Modified residue (1); Transmembrane (1) TRANSMEM 6 26 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q8BGZ2 F168A_MOUSE Protein FAM168A 244 26,184 Alternative sequence (1); Chain (1); Modified residue (2); Sequence conflict (1) FUNCTION: In cancer context, protects cells from induced-DNA damage and apoptosis. Acts, at least in part, through PI3K/AKT/NFKB signaling pathway and by preventing POLB degradation. Decreases POLB ubiquitation and stabilizes its protein levels. {ECO:0000250|UniProtKB:Q92567}. SUBUNIT: Interacts with POLB. Interacts with AKT1 and MT1X. May interact with FAM168B. {ECO:0000250|UniProtKB:Q92567}. +Q80XQ8 F168B_MOUSE Myelin-associated neurite-outgrowth inhibitor (Mani) 194 20,194 Chain (1); Erroneous initiation (1); Glycosylation (1); Modified residue (2); Sequence conflict (1); Topological domain (3); Transmembrane (2) TRANSMEM 19 41 Helical. {ECO:0000255}.; TRANSMEM 142 163 Helical. {ECO:0000255}. TOPO_DOM 1 18 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 42 141 Extracellular. {ECO:0000255}.; TOPO_DOM 164 194 Cytoplasmic. {ECO:0000255}. FUNCTION: Inhibitor of neuronal axonal outgrowth. Acts as a negative regulator of CDC42 and STAT3 and a positive regulator of STMN2. Positive regulator of CDC27. {ECO:0000269|PubMed:20716133}. PTM: N-glycosylated. {ECO:0000269|PubMed:20716133}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:D4AEP3}. Cell membrane {ECO:0000269|PubMed:20716133}; Multi-pass membrane protein {ECO:0000269|PubMed:20716133}. Cell projection, axon {ECO:0000269|PubMed:20716133}. Note=Expressed in neuronal cell bodies and axonal fibers. {ECO:0000269|PubMed:20716133}. SUBUNIT: May form homodimers (By similarity). May interact with DAZAP2, FAM168A, PRDX6, RBM6, TMTC1 and YPEL2 (By similarity). Interacts with CDC27 (PubMed:20716133). {ECO:0000250|UniProtKB:A1KXE4, ECO:0000269|PubMed:20716133}. TISSUE SPECIFICITY: Predominantly expressed in the brain, including olfactory bulb, cortex and cerebellum (at protein level). {ECO:0000269|PubMed:20716133}. +Q8CDM8 F16B1_MOUSE Protein FAM160B1 764 86,017 Alternative sequence (1); Chain (1); Frameshift (2); Sequence conflict (8) +Q8VE88 F1142_MOUSE Protein FAM114A2 497 54,045 Alternative sequence (1); Chain (1); Compositional bias (1); Modified residue (2); Sequence conflict (6) +P70695 F16P2_MOUSE Fructose-1,6-bisphosphatase isozyme 2 (FBPase 2) (EC 3.1.3.11) (D-fructose-1,6-bisphosphate 1-phosphohydrolase 2) (Muscle FBPase) (RAE-30) 339 36,947 Binding site (5); Chain (1); Frameshift (1); Metal binding (8); Modified residue (2); Motif (1); Nucleotide binding (2); Region (3); Sequence conflict (2); Site (1) Carbohydrate biosynthesis; gluconeogenesis. FUNCTION: Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate in the presence of divalent cations and probably participates in glycogen synthesis from carbohydrate precursors, such as lactate. {ECO:0000269|PubMed:8034042}. SUBCELLULAR LOCATION: Cell junction {ECO:0000250}. Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250}. Note=In neonatal cardiomyocytes, distributed throughout the cytosol, accumulating in the intercalated disks which occur at the Z line of cardiomyocytes and connect adjacent cells, and also located in the nucleus; dissociates from the Z line following an increase in cytosolic Ca(2+) concentration. In muscle precursor cells, localizes predominantly to the nucleus and to a lesser extent to the cytoplasm at the proliferative phase, while mainly localizing to the cytoplasm at the differentiation phase. Colocalizes with ALDOA and alpha-actinin on both sides of the Z line of skeletal muscle; dissociates rapidly from the Z line following an increase in cytosolic Ca(2+) concentration. {ECO:0000250}. SUBUNIT: Homotetramer. Interacts with ALDOA; the interaction blocks inhibition by physiological concentrations of AMP and reduces inhibition by Ca(2+). Interacts with alpha-actinin and F-actin (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in muscle, intestine, brain and placenta and very weakly in liver. {ECO:0000269|PubMed:11250076, ECO:0000269|PubMed:8034042}. +Q14CH0 F171B_MOUSE Protein FAM171B 825 92,045 Alternative sequence (1); Chain (1); Compositional bias (1); Erroneous initiation (1); Glycosylation (3); Modified residue (1); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 354 374 Helical. {ECO:0000255}. TOPO_DOM 33 353 Extracellular. {ECO:0000255}.; TOPO_DOM 375 825 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q501J2 F173A_MOUSE Protein N-lysine methyltransferase FAM173A (EC 2.1.1.-) 229 24,740 Chain (1); Glycosylation (1); Transmembrane (1) TRANSMEM 20 42 Helical. {ECO:0000255}. FUNCTION: S-adenosyl-L-methionin-dependent protein-lysine N-methyltransferase. {ECO:0000250|UniProtKB:Q6P4H8}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q9D1Z3 F173B_MOUSE Protein N-lysine methyltransferase FAM173B (mFam173b) (EC 2.1.1.-) 247 27,397 Chain (1); Modified residue (1); Sequence conflict (1); Transmembrane (1) TRANSMEM 34 54 Helical. {ECO:0000255}. FUNCTION: Mitochondrial protein-lysine N-methyltransferase that promotes chronic pain (PubMed:29444090). Involved in persistent inflammatory and neuropathic pain: methyltransferase activity in the mitochondria of sensory neurons promotes chronic pain via a pathway that depends on the production of reactive oxygen species (ROS) and on the engagement of spinal cord microglia (PubMed:29444090). Protein-lysine N-methyltransferase activity is dependent on S-adenosyl-L-methionine (By similarity). Target proteins are unknown (By similarity). {ECO:0000250|UniProtKB:Q6P4H8, ECO:0000269|PubMed:29444090}. SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250|UniProtKB:Q6P4H8}; Single-pass membrane protein {ECO:0000255}. Note=Localizes to mitochondrial cristae. {ECO:0000250|UniProtKB:Q6P4H8}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:29444090}. +Q9D3L0 F174A_MOUSE Membrane protein FAM174A (Transmembrane protein 157) 190 19,986 Chain (1); Frameshift (3); Glycosylation (1); Sequence conflict (11); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 124 144 Helical. {ECO:0000255}. TOPO_DOM 32 123 Extracellular. {ECO:0000255}.; TOPO_DOM 145 190 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q0VAY3 F187B_MOUSE Protein FAM187B (Transmembrane protein 162) 358 40,957 Alternative sequence (1); Chain (1); Glycosylation (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 323 343 Helical. {ECO:0000255}. TOPO_DOM 18 322 Extracellular. {ECO:0000255}.; TOPO_DOM 344 358 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q80VF6 F181B_MOUSE Protein FAM181B 417 42,437 Alternative sequence (2); Chain (1); Compositional bias (1); Sequence conflict (2) +Q4FZH1 F1892_MOUSE Protein FAM189A2 290 32,209 Chain (1); Erroneous initiation (1); Modified residue (1) +Q5HZJ5 F189B_MOUSE Protein FAM189B 669 72,016 Chain (1); Compositional bias (2); Glycosylation (1); Modified residue (4); Transmembrane (4) TRANSMEM 34 54 Helical. {ECO:0000255}.; TRANSMEM 67 87 Helical. {ECO:0000255}.; TRANSMEM 91 111 Helical. {ECO:0000255}.; TRANSMEM 174 194 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: May interact with WWOX. {ECO:0000250}. +Q8CGI1 F193A_MOUSE Protein FAM193A 1231 136,714 Chain (1); Coiled coil (2); Compositional bias (6); Modified residue (4) +Q0KK56 F184B_MOUSE Protein FAM184B 942 107,601 Alternative sequence (2); Chain (1); Coiled coil (5); Sequence conflict (1) +Q7TPD2 F185A_MOUSE Protein FAM185A 378 39,992 Alternative sequence (2); Chain (1); Sequence conflict (1) +Q9D9R9 F186A_MOUSE Protein FAM186A 1790 194,550 Alternative sequence (1); Chain (1); Compositional bias (2) +Q7TPG6 F19A3_MOUSE Protein FAM19A3 (Chemokine-like protein TAFA-3) 132 14,426 Chain (1); Signal peptide (1) FUNCTION: Plays a role in the regulation of microglia polarization. {ECO:0000269|PubMed:25595455}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25595455}. TISSUE SPECIFICITY: Highly expressed in brain. {ECO:0000269|PubMed:25595455}. +Q91WE9 F19A5_MOUSE Protein FAM19A5 (Chemokine-like protein TAFA-5) 132 14,331 Alternative sequence (1); Chain (1); Glycosylation (1); Signal peptide (1) FUNCTION: Acts as a chemokine-like protein by regulating cell proliferation and migration through activation of G protein-coupled receptors (GPCRs), such as S1PR2 and FPR2 (PubMed:29453251, PubMed:29138422). Stimulates chemotactic migration of macrophages mediated by the MAPK3/ERK1 and AKT1 pathway (PubMed:29138422). Blocks TNFSF11/RANKL-induced osteoclast formation from macrophages by inhibiting up-regulation of osteoclast fusogenic and differentiation genes (PubMed:29138422). Stimulation of macrophage migration and inhibition of osteoclast formation is mediated through the GPCR FPR2 (PubMed:29138422). Acts as an adipokine by negatively regulating vascular smooth muscle cell (VSMC) proliferation and migration in response to platelet-derived growth factor stimulation via GPCR S1PR2 and G protein GNA12/GNA13-transmitted RHOA signaling (By similarity). Inhibits injury-induced cell proliferation and neointima formation in the femoral arteries (PubMed:29453251). {ECO:0000250|UniProtKB:M0R7X9, ECO:0000269|PubMed:29138422, ECO:0000269|PubMed:29453251}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29453251}. TISSUE SPECIFICITY: Expressed in the subcutaneous, brown, epididymal and perirenal adipose tissue (at protein level). {ECO:0000269|PubMed:29453251}. +Q5DTT3 F208B_MOUSE Protein FAM208B (Peripheral benzodiazepine receptor-associated protein 20) 2382 264,278 Chain (1); Cross-link (1); Erroneous initiation (4); Modified residue (11); Sequence caution (1); Sequence conflict (2) +Q6PGH4 F222A_MOUSE Protein FAM222A 453 47,233 Chain (1); Compositional bias (1) +Q8BGY7 F210A_MOUSE Protein FAM210A 273 31,600 Chain (1); Coiled coil (1); Domain (1); Sequence conflict (1); Transmembrane (1) TRANSMEM 138 158 Helical. {ECO:0000255}. FUNCTION: May play a role in the structure and strength of both muscle and bone. {ECO:0000269|PubMed:29618611}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. Mitochondrion {ECO:0000269|PubMed:29618611}. Cytoplasm {ECO:0000269|PubMed:29618611}. SUBUNIT: Interacts with ATAD3A. {ECO:0000250|UniProtKB:Q96ND0}. TISSUE SPECIFICITY: Expressed in skeletal muscle, heart, brain but not in bone. {ECO:0000269|PubMed:29618611}. +Q8C6C7 F204A_MOUSE Protein FAM204A 236 26,995 Chain (1); Coiled coil (1) +Q9D8B6 F210B_MOUSE Protein FAM210B, mitochondrial 190 20,344 Chain (1); Domain (1); Sequence conflict (2); Transit peptide (1); Transmembrane (2) TRANSMEM 97 117 Helical. {ECO:0000255}.; TRANSMEM 148 168 Helical. {ECO:0000255}. FUNCTION: Plays a role in erythroid differentiation. Involved in cell proliferation and tumor cell growth suppression. Involved in the metabolic reprogramming of cancer cells in a PDK4-dependent manner. {ECO:0000250|UniProtKB:Q96KR6}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q96KR6}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q96KR6}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in late erythroblast differentiation stages (PubMed:26968549). {ECO:0000269|PubMed:26968549}. +Q69ZK7 F214A_MOUSE Protein FAM214A 1075 119,272 Alternative sequence (1); Chain (1); Erroneous initiation (2); Sequence conflict (4) +P70266 F261_MOUSE 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1 (6PF-2-K/Fru-2,6-P2ase 1) (PFK/FBPase 1) (6PF-2-K/Fru-2,6-P2ase liver isozyme) [Includes: 6-phosphofructo-2-kinase (EC 2.7.1.105); Fructose-2,6-bisphosphatase (EC 3.1.3.46)] 471 54,849 Active site (4); Alternative sequence (1); Binding site (18); Chain (1); Initiator methionine (1); Modified residue (3); Nucleotide binding (4); Region (2); Sequence conflict (1); Site (1) FUNCTION: Synthesis and degradation of fructose 2,6-bisphosphate. SUBUNIT: Homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Liver. +Q9D772 F219A_MOUSE Protein FAM219A 157 17,464 Chain (1); Modified residue (6); Sequence conflict (1) +Q8BYI8 F234B_MOUSE Protein FAM234B 624 67,031 Alternative sequence (1); Chain (1); Modified residue (5); Sequence conflict (3); Transmembrane (1) TRANSMEM 107 127 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +A1L3C1 F71E1_MOUSE Protein FAM71E1 212 24,172 Alternative sequence (1); Chain (1); Sequence conflict (1) +P70265 F262_MOUSE 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2 (6PF-2-K/Fru-2,6-P2ase 2) (PFK/FBPase 2) (6PF-2-K/Fru-2,6-P2ase heart-type isozyme) [Includes: 6-phosphofructo-2-kinase (EC 2.7.1.105); Fructose-2,6-bisphosphatase (EC 3.1.3.46)] 519 59,925 Active site (4); Binding site (17); Chain (1); Initiator methionine (1); Modified residue (7); Nucleotide binding (4); Region (2); Sequence conflict (4); Site (3) FUNCTION: Synthesis and degradation of fructose 2,6-bisphosphate. PTM: Phosphorylation by AMPK stimulates activity. {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Highest levels in kidney; also found in heart, brain, spleen, lung, liver, skeletal muscle and testis. +Q6DTY7 F264_MOUSE 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4 (6PF-2-K/Fru-2,6-P2ase 4) (PFK/FBPase 4) (6PF-2-K/Fru-2,6-P2ase testis-type isozyme) [Includes: 6-phosphofructo-2-kinase (EC 2.7.1.105); Fructose-2,6-bisphosphatase (EC 3.1.3.46)] 469 54,067 Active site (4); Alternative sequence (6); Binding site (18); Chain (1); Modified residue (2); Nucleotide binding (4); Region (2); Site (1) FUNCTION: Synthesis and degradation of fructose 2,6-bisphosphate. {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +Q91Y47 FA11_MOUSE Coagulation factor XI (FXI) (EC 3.4.21.27) (Plasma thromboplastin antecedent) (PTA) [Cleaved into: Coagulation factor XIa heavy chain; Coagulation factor XIa light chain] 624 69,789 Active site (3); Chain (2); Disulfide bond (18); Domain (5); Glycosylation (5); Region (1); Sequence conflict (4); Signal peptide (1) FUNCTION: Factor XI triggers the middle phase of the intrinsic pathway of blood coagulation by activating factor IX. {ECO:0000250}. PTM: Activated by factor XIIa (or XII), which cleaves each polypeptide after Arg-389 into the light chain, which contains the active site, and the heavy chain, which associates with high molecular weight (HMW) kininogen. {ECO:0000250}.; PTM: N-glycosylated on both chains. N-glycosylated sites mainly consist of nonfucosylated sialylated biantennary (in high abundance) and/or triantennary (in low abundance) complex structures. {ECO:0000250|UniProtKB:P03951}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Homodimer; disulfide-linked. Forms a heterodimer with SERPINA5. After activation the heavy and light chains are also linked by a disulfide bond (By similarity). {ECO:0000250}. +Q8BGI4 FA13A_MOUSE Protein FAM13A (Precm1 protein) 693 79,424 Chain (1); Modified residue (5) TISSUE SPECIFICITY: Expressed in the mammary gland, with similar levels at all stages of development, including pregnancy, lactation and involution. {ECO:0000269|PubMed:15234000}. +Q8BHZ0 FA49A_MOUSE Protein FAM49A 323 37,343 Chain (1) +Q921M7 FA49B_MOUSE Protein FAM49B 324 36,776 Chain (1); Initiator methionine (1); Lipidation (1) SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9NUQ9}; Lipid-anchor {ECO:0000250|UniProtKB:Q9NUQ9}. +Q9WV03 FA50A_MOUSE Protein FAM50A (Protein XAP-5) 339 40,252 Chain (1); Cross-link (1); Initiator methionine (1); Modified residue (1); Motif (1); Sequence conflict (1) FUNCTION: May be a DNA-binding protein or transcriptional factor. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: Widely expressed in embryonic and adult tissues. +Q9WTJ8 FA50B_MOUSE Protein FAM50B (Protein XAP-5-like) 334 39,594 Chain (1); Frameshift (1); Initiator methionine (1); Modified residue (1); Sequence conflict (1) TISSUE SPECIFICITY: Widely expressed. Abundant in testis, where it is expressed in seminiferous tubules, not in the interstitium. At the cellular level, expressed in primary spermatocytes and round spermatids, but not detectable in spermatogonia, elongating spermatids, mature spermatozoa, Sertoli cells or Leydig cells. +Q8CF27 FA24A_MOUSE Protein FAM24A 98 10,857 Chain (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q7TNV1 FA57B_MOUSE Protein FAM57B 275 30,778 Alternative sequence (2); Chain (1); Domain (1); Frameshift (1); Transmembrane (4) TRANSMEM 130 150 Helical. {ECO:0000255}.; TRANSMEM 159 179 Helical. {ECO:0000255}.; TRANSMEM 194 214 Helical. {ECO:0000255}.; TRANSMEM 232 252 Helical. {ECO:0000255}. FUNCTION: Involved in ceramide synthesis. In vitro, isoform 3 stimulates the production of C16-, C18- and C20-ceramides, isoform 1 slightly increases the levels of C18- and C20-ceramides, while isoform 2 exhibits only minimal activity. May interfere with adipogenesis by stimulating ceramide synthesis. {ECO:0000269|PubMed:23275342}. SUBCELLULAR LOCATION: Isoform 1: Golgi apparatus membrane {ECO:0000269|PubMed:23275342}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: Isoform 2: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23275342}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: Isoform 3: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23275342}; Multi-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Each isoform has a distinct expression pattern. Isoform 1 is highly expressed in brain. Isoform 2 is expressed at low levels, if any, in all analyzed tissues, with slightly higher levels in testis. Isoform 3 is expressed at very high levels in testis and, at lower levels, in white adipose tissue. In epididymal fat, isoform 3 is expressed at higher levels in obese mice compared with lean mice. By contrast, isoform 1 and 2 levels are significantly lower in obese mice compared with lean mice. {ECO:0000269|PubMed:23275342}. +O88783 FA5_MOUSE Coagulation factor V (Activated protein C cofactor) [Cleaved into: Coagulation factor V heavy chain; Coagulation factor V light chain] 2183 247,230 Chain (3); Disulfide bond (2); Domain (11); Erroneous initiation (1); Glycosylation (8); Metal binding (4); Modified residue (4); Mutagenesis (2); Propeptide (1); Region (3); Repeat (33); Signal peptide (1); Site (7) FUNCTION: Central regulator of hemostasis. It serves as a critical cofactor for the prothrombinase activity of factor Xa that results in the activation of prothrombin to thrombin. PTM: Thrombin activates factor V proteolytically to the active cofactor, factor Va (formation of a heavy chain at the N-terminus and a light chain at the C-terminus). {ECO:0000250}.; PTM: Sulfation is required for efficient thrombin cleavage and activation and for full procoagulant activity. {ECO:0000250}.; PTM: Activated protein C inactivates factor V and factor Va by proteolytic degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Factor Va, the activated form of factor V, is composed of a heavy chain and a light chain, non-covalently bound. The interaction between the two chains is calcium-dependent. Forms heterodimer with SERPINA5 (By similarity). {ECO:0000250}. DOMAIN: Domain B contains 32 X 9 AA tandem repeats, and 1 X 17 AA repeats. +Q80XP8 FA76B_MOUSE Protein FAM76B 339 38,556 Alternative sequence (4); Chain (1); Coiled coil (1); Compositional bias (3); Initiator methionine (1); Modified residue (5); Sequence conflict (2) SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}. DOMAIN: The polyhistidine repeat acts as a targeting signal to nuclear speckles. {ECO:0000250}. +Q3UKU4 FA83F_MOUSE Protein FAM83F 495 55,012 Chain (1); Initiator methionine (1); Modified residue (3); Sequence caution (1); Sequence conflict (4) +P70375 FA7_MOUSE Coagulation factor VII (EC 3.4.21.21) (Serum prothrombin conversion accelerator) [Cleaved into: Factor VII light chain; Factor VII heavy chain] 446 50,276 Active site (3); Beta strand (3); Binding site (1); Chain (2); Disulfide bond (12); Domain (4); Glycosylation (4); Helix (1); Modified residue (11); Propeptide (1); Sequence conflict (1); Signal peptide (1); Site (1) FUNCTION: Initiates the extrinsic pathway of blood coagulation. Serine protease that circulates in the blood in a zymogen form. Factor VII is converted to factor VIIa by factor Xa, factor XIIa, factor IXa, or thrombin by minor proteolysis. In the presence of tissue factor and calcium ions, factor VIIa then converts factor X to factor Xa by limited proteolysis. Factor VIIa will also convert factor IX to factor IXa in the presence of tissue factor and calcium (By similarity). {ECO:0000250}. PTM: The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium. {ECO:0000250}.; PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}.; PTM: Can be either O-glucosylated or O-xylosylated at Ser-93 by POGLUT1. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Heterodimer of a light chain and a heavy chain linked by a disulfide bond. {ECO:0000250}. TISSUE SPECIFICITY: Plasma and liver. +Q3UXZ6 FA81A_MOUSE Protein FAM81A 364 41,710 Chain (1); Coiled coil (3); Sequence conflict (6) +Q0VBM2 FA83B_MOUSE Protein FAM83B 1012 114,676 Chain (1); Compositional bias (1); Modified residue (11); Region (1) FUNCTION: Probable proto-oncogene that functions in the epidermal growth factor receptor/EGFR signaling pathway. May activate both the EGFR itself and downstream RAS/MAPK and PI3K/AKT/TOR signaling cascades. {ECO:0000250|UniProtKB:Q5T0W9}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q5T0W9}. Membrane {ECO:0000250|UniProtKB:Q5T0W9}. SUBUNIT: Interacts with EGFR; the interaction is disrupted by EGF stimulation. Interacts with RAF1; displaces 14-3-3 proteins from RAF1 and activates RAF1 within the RAS/MAPK signaling cascade. Interacts with AKT1, PIK3CA and PIK3R1; activates the PI3K/AKT signaling cascade. {ECO:0000250|UniProtKB:Q5T0W9}. +A2ARK0 FA83C_MOUSE Protein FAM83C 776 84,071 Chain (1); Erroneous initiation (2); Sequence conflict (8) FUNCTION: May play a role in MAPK signaling. {ECO:0000250|UniProtKB:Q9BQN1}. SUBUNIT: May interact with RAF1. {ECO:0000250|UniProtKB:Q9BQN1}. +Q06194 FA8_MOUSE Coagulation factor VIII (Procoagulant component) 2319 266,196 Chain (1); Disulfide bond (5); Domain (11); Glycosylation (26); Modified residue (6); Region (1); Sequence conflict (2); Signal peptide (1); Site (5) FUNCTION: Factor VIII, along with calcium and phospholipid, acts as a cofactor for factor IXa when it converts factor X to the activated form, factor Xa. PTM: The binding of vWF and activation depend on the sulfation of Tyr-1669. SUBCELLULAR LOCATION: Secreted, extracellular space. SUBUNIT: Interacts with vWF. vWF binding is essential for the stabilization of F8 in circulation (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Found in most tissues. +Q3TJZ6 FA98A_MOUSE Protein FAM98A 515 55,055 Chain (1); Compositional bias (3); Erroneous initiation (1) FUNCTION: Positively stimulates PRMT1-induced protein arginine methylation (By similarity). Involved in skeletal homeostasis (PubMed:27777970). Positively regulates lysosome peripheral distribution and ruffled border formation in osteoclasts (PubMed:27777970). {ECO:0000250|UniProtKB:Q8NCA5, ECO:0000269|PubMed:27777970}. SUBUNIT: Interacts (via N- and C-terminus) with DDX1 (By similarity). Interacts (via N- and C-terminus) with C14orf166 (By similarity). Interacts with FAM98B (By similarity). Interacts with PLEKHM1 (via N- and C-terminus) (PubMed:27777970). {ECO:0000250|UniProtKB:Q8NCA5, ECO:0000269|PubMed:27777970}. +Q80VD1 FA98B_MOUSE Protein FAM98B 429 45,349 Chain (1); Compositional bias (2) FUNCTION: Positively stimulates PRMT1-induced protein arginine dimethylated arginine methylation. {ECO:0000250|UniProtKB:Q52LJ0}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. SUBUNIT: Homodimer. Component of a tRNA-splicing ligase complex. Interacts with FAM98A. {ECO:0000250|UniProtKB:Q52LJ0}. +P49222 EPB42_MOUSE Erythrocyte membrane protein band 4.2 (Erythrocyte protein 4.2) (P4.2) 691 76,756 Chain (1); Initiator methionine (1); Lipidation (1); Modified residue (2); Region (1); Sequence conflict (6) FUNCTION: Probably plays an important role in the regulation of erythrocyte shape and mechanical properties. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. Cytoplasm, cytoskeleton. Note=Cytoplasmic surface of erythrocyte membranes. SUBUNIT: Oligomer. Interacts with the cytoplasmic domain of SLC4A1/band 3 anion transport protein. +P56400 GP1BB_MOUSE Platelet glycoprotein Ib beta chain (GP-Ib beta) (GPIb-beta) (GPIbB) (CD antigen CD42c) 206 21,763 Chain (1); Disulfide bond (5); Domain (2); Glycosylation (1); Modified residue (4); Repeat (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 148 172 Helical. {ECO:0000255}. TOPO_DOM 27 147 Extracellular. {ECO:0000255}.; TOPO_DOM 173 206 Cytoplasmic. {ECO:0000255}. FUNCTION: Gp-Ib, a surface membrane protein of platelets, participates in the formation of platelet plugs by binding to von Willebrand factor, which is already bound to the subendothelium. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Two GP-Ib beta are disulfide-linked to one GP-Ib alpha. GP-IX is complexed with the GP-Ib heterodimer via a non covalent linkage (By similarity). {ECO:0000250}. +Q91W69 EPN3_MOUSE Epsin-3 (EPS-15-interacting protein 3) 636 68,240 Binding site (6); Chain (1); Compositional bias (1); Domain (3); Modified residue (3); Region (2); Repeat (8); Sequence conflict (2) SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250}. Note=Concentrated in the perinuclear region and associated with clathrin-coated vesicles close to the cell periphery. May shuttle to the nucleus (By similarity). {ECO:0000250}. +O09127 EPHA8_MOUSE Ephrin type-A receptor 8 (EC 2.7.10.1) (EPH- and ELK-related kinase) (Tyrosine-protein kinase receptor EEK) 1004 110,705 Active site (1); Binding site (1); Chain (1); Compositional bias (1); Domain (5); Glycosylation (3); Modified residue (2); Motif (1); Mutagenesis (4); Nucleotide binding (1); Region (2); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 542 562 Helical. {ECO:0000255}. TOPO_DOM 27 541 Extracellular. {ECO:0000255}.; TOPO_DOM 563 1004 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor tyrosine kinase which binds promiscuously GPI-anchored ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. The GPI-anchored ephrin-A EFNA2, EFNA3, and EFNA5 are able to activate EPHA8 through phosphorylation. With EFNA5 may regulate integrin-mediated cell adhesion and migration on fibronectin substrate but also neurite outgrowth. During development of the nervous system plays also a role in axon guidance. Downstream effectors of the EPHA8 signaling pathway include FYN which promotes cell adhesion upon activation by EPHA8 and the MAP kinases in the stimulation of neurite outgrowth. {ECO:0000269|PubMed:10498895, ECO:0000269|PubMed:11416136, ECO:0000269|PubMed:12681484, ECO:0000269|PubMed:15782114, ECO:0000269|PubMed:17875921, ECO:0000269|PubMed:9214628}. PTM: Phosphorylated. Phosphorylation is stimulated upon binding of its ligands including EFNA2, EFNA3 and EFNA5. Autophosphorylation on Tyr-615 is critical for association with FYN. Autophosphorylation on Tyr-838 modulates tyrosine kinase activity. {ECO:0000269|PubMed:10498895, ECO:0000269|PubMed:9053851}.; PTM: Ubiquitinated. Ubiquitination by CBL regulates the receptor stability and activity through proteasomal degradation. ANKS1A prevents ubiquitination and degradation. {ECO:0000269|PubMed:20100865}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9053851}; Single-pass type I membrane protein {ECO:0000255}. Cell projection {ECO:0000269|PubMed:17875921}. Early endosome membrane {ECO:0000269|PubMed:20496116}. Note=Undergoes clathrin-mediated endocytosis upon EFNA5-binding and is targeted to early endosomes (PubMed:20496116). {ECO:0000269|PubMed:20496116}. SUBUNIT: Heterotetramer upon binding of the ligand. The heterotetramer is composed of an ephrin dimer and a receptor dimer. Oligomerization is probably required to induce biological responses (By similarity). May also form heterodimers with other ephrin receptors. Interacts with FYN; possible downstream effector of EPHA8 in regulation of cell adhesion. Interacts with PIK3CG; regulates integrin-mediated cell adhesion to substrate. Interacts with TIAM1; regulates clathrin-mediated endocytosis of EPHA8. Interacts with ANKS1A and ANKS1B; EPHA8 kinase activity-independent but stimulated by EPHA8 ubiquitination. {ECO:0000250, ECO:0000269|PubMed:10498895, ECO:0000269|PubMed:11416136, ECO:0000269|PubMed:17875921, ECO:0000269|PubMed:20100865, ECO:0000269|PubMed:20496116, ECO:0000269|PubMed:9053851}. TISSUE SPECIFICITY: Specifically expressed in the central nervous system. +P35689 ERCC5_MOUSE DNA repair protein complementing XP-G cells homolog (EC 3.1.-.-) (DNA excision repair protein ERCC-5) (Xeroderma pigmentosum group G-complementing protein homolog) 1170 130,715 Chain (1); Metal binding (7); Modified residue (4); Motif (1); Region (2); Sequence conflict (24) FUNCTION: Single-stranded structure-specific DNA endonuclease involved in DNA excision repair. Makes the 3'incision in DNA nucleotide excision repair (NER). Acts as a cofactor for a DNA glycosylase that removes oxidized pyrimidines from DNA. May also be involved in transcription-coupled repair of this kind of damage, in transcription by RNA polymerase II, and perhaps in other processes too (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with PCNA. {ECO:0000250}. +P70424 ERBB2_MOUSE Receptor tyrosine-protein kinase erbB-2 (EC 2.7.10.1) (Proto-oncogene Neu) (Proto-oncogene c-ErbB-2) (p185erbB2) (CD antigen CD340) 1256 138,579 Active site (1); Binding site (1); Chain (1); Compositional bias (2); Disulfide bond (25); Domain (1); Erroneous initiation (1); Glycosylation (7); Modified residue (9); Motif (1); Nucleotide binding (1); Region (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 654 674 Helical. {ECO:0000255}. TOPO_DOM 23 653 Extracellular. {ECO:0000255}.; TOPO_DOM 675 1256 Cytoplasmic. {ECO:0000255}. FUNCTION: Protein tyrosine kinase that is part of several cell surface receptor complexes, but that apparently needs a coreceptor for ligand binding. Essential component of a neuregulin-receptor complex, although neuregulins do not interact with it alone. GP30 is a potential ligand for this receptor. Regulates outgrowth and stabilization of peripheral microtubules (MTs). Upon ERBB2 activation, the MEMO1-RHOA-DIAPH1 signaling pathway elicits the phosphorylation and thus the inhibition of GSK3B at cell membrane. This prevents the phosphorylation of APC and CLASP2, allowing its association with the cell membrane. In turn, membrane-bound APC allows the localization of MACF1 to the cell membrane, which is required for microtubule capture and stabilization (By similarity). {ECO:0000250}.; FUNCTION: In the nucleus is involved in transcriptional regulation. Associates with the 5'-TCAAATTC-3' sequence in the PTGS2/COX-2 promoter and activates its transcription. Implicated in transcriptional activation of CDKN1A; the function involves STAT3 and SRC. Involved in the transcription of rRNA genes by RNA Pol I and enhances protein synthesis and cell growth (By similarity). {ECO:0000250}. PTM: Autophosphorylated. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Ligand-binding increases phosphorylation on tyrosine residues. Signaling via SEMA4C promotes phosphorylation at Tyr-1249. Dephosphorylated by PTPN12. {ECO:0000250|UniProtKB:P04626}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Homodimer. Heterodimer with EGFR, ERBB3 and ERBB4. Part of a complex with EGFR and either PIK3C2A or PIK3C2B. May interact with PIK3C2B when phosphorylated on Tyr-1197. Interacts with PLXNB1. Interacts (when phosphorylated on Tyr-1249) with MEMO1. Interacts with MUC1. Interacts (when phosphorylated on Tyr-1140) with GRB7 (via SH2 domain). Interacts (when phosphorylated on Tyr-1249) with ERBIN. Interacts with KPNB1, RANBP2, EEA1, CRM1, CLTC, PTK6, RPA194 and ACTB. Interacts (preferentially with the tyrosine phosphorylated form) with CPNE3; this interaction occurs at the cell membrane and is increased in a growth factor heregulin-dependent manner. Interacts with HSP90AA1 and HSP90AB1 in an ATP-dependent manner; the interaction suppresses ERBB2 kinase activity (By similarity). Interacts with SRC (PubMed:7542762). Interacts with MYOC (PubMed:23897819). Interacts with PRKCABP (PubMed:11278603). {ECO:0000250|UniProtKB:P04626, ECO:0000269|PubMed:11278603, ECO:0000269|PubMed:23897819, ECO:0000269|PubMed:7542762}. TISSUE SPECIFICITY: Expressed predominantly in uterine epithelial cells. In the muscle, expression localizes to the synaptic sites of muscle fibers. +Q60902 EP15R_MOUSE Epidermal growth factor receptor substrate 15-like 1 (Epidermal growth factor receptor pathway substrate 15-related sequence) (Eps15-rs) (Eps15-related protein) (Eps15R) 907 99,309 Alternative sequence (6); Calcium binding (1); Chain (1); Coiled coil (1); Compositional bias (1); Domain (6); Initiator methionine (1); Modified residue (23); Region (1); Sequence conflict (9) FUNCTION: Seems to be a constitutive component of clathrin-coated pits that is required for receptor-mediated endocytosis. Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but not TFR seems to require association with DAB2 (By similarity). {ECO:0000250}. PTM: Phosphorylated on tyrosine residues by EGFR. {ECO:0000269|PubMed:9446614}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9446614}; Peripheral membrane protein {ECO:0000269|PubMed:9446614}. Nucleus {ECO:0000269|PubMed:9446614}. Membrane, coated pit {ECO:0000269|PubMed:9446614}. Note=Localized to plasma membrane coated pits. SUBUNIT: Interacts with EPS15, AGFG1/HRB and AGFG2/HRBL. Associates with the clathrin-associated adapter protein complex 2 (AP-2). Interacts with FCHO1 (By similarity). Interacts with FCHO2. Interacts (via EH domains) with DAB2. Interacts with UBQLN1 (via ubiquitin-like domain). Interacts with CAVIN3 (via leucine-zipper domain) (By similarity). {ECO:0000250|UniProtKB:Q9UBC2, ECO:0000269|PubMed:20448150, ECO:0000269|PubMed:22648170, ECO:0000269|PubMed:9446614}. +Q8BHK9 ERC6L_MOUSE DNA excision repair protein ERCC-6-like (EC 3.6.4.12) (ATP-dependent helicase ERCC6-like) 1240 138,854 Chain (1); Domain (2); Modified residue (12); Motif (1); Nucleotide binding (1); Repeat (2); Sequence conflict (1) FUNCTION: DNA helicase that acts as an essential component of the spindle assembly checkpoint. Contributes to the mitotic checkpoint by recruiting MAD2 to kinetochores and monitoring tension on centromeric chromatin. Acts as a tension sensor that associates with catenated DNA which is stretched under tension until it is resolved during anaphase. Functions as ATP-dependent DNA translocase. Can promote Holliday junction branch migration (in vitro). {ECO:0000250|UniProtKB:Q2NKX8}. PTM: Phosphorylation by PLK1 prevents the association with chromosome arms and restricts its localization to the kinetochore-centromere region. {ECO:0000250|UniProtKB:Q2NKX8}. SUBCELLULAR LOCATION: Chromosome, centromere {ECO:0000250|UniProtKB:Q2NKX8}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q2NKX8}. Chromosome {ECO:0000250|UniProtKB:Q2NKX8}. Note=Localizes to kinetochores, inner centromeres and thin threads connecting separating chromosomes even during anaphase. In prometaphase cells, it mostly concentrates in between kinetochores. In metaphase, it localizes to numerous thin threads that stretch between sister kinetochores of the aligned chromosomes and are composed of catenated centromeric DNA. Evolution from inner centromeres to thin threads takes place in response to tension. Resolution of thin threads requires topoisomerase 2-alpha (TOP2A) after anaphase onset. {ECO:0000250|UniProtKB:Q2NKX8}. SUBUNIT: Interacts with PLK1, which phosphorylates it. Both proteins are mutually dependent on each other for correct subcellular localization. Interacts (via N-terminal TPR repeat) with BEND3 (via BEN domains 1 and 3); the interaction is direct. {ECO:0000250|UniProtKB:Q2NKX8}. TISSUE SPECIFICITY: Expressed mainly in the neural tube and heart of E10.5 embryo. Significantly down-regulated after alcohol exposure in embryonic brain and heart, but not in embryonic kidney, liver, or lung. {ECO:0000269|PubMed:15917148}. +P07903 ERCC1_MOUSE DNA excision repair protein ERCC-1 298 32,910 Chain (1); Cross-link (3); DNA binding (1); Modified residue (1); Motif (1); Region (1); Sequence conflict (2) FUNCTION: Non-catalytic component of a structure-specific DNA repair endonuclease responsible for the 5'-incision during DNA repair. Responsible, in conjunction with SLX4, for the first step in the repair of interstrand cross-links (ICL). Participates in the processing of anaphase bridge-generating DNA structures, which consist in incompletely processed DNA lesions arising during S or G2 phase, and can result in cytokinesis failure. Also required for homology-directed repair (HDR) of DNA double-strand breaks, in conjunction with SLX4 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Heterodimer composed of ERCC1 and XPF/ERRC4. +O08811 ERCC2_MOUSE General transcription and DNA repair factor IIH helicase subunit XPD (TFIIH subunit XPD) (EC 3.6.4.12) (CXPD) (DNA excision repair protein ERCC-2) (DNA repair protein complementing XP-D cells) (Xeroderma pigmentosum group D-complementing protein) 760 86,842 Chain (1); Domain (1); Erroneous initiation (1); Metal binding (4); Motif (1); Nucleotide binding (1); Region (1); Sequence conflict (2) FUNCTION: ATP-dependent 5'-3' DNA helicase, component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. The ATP-dependent helicase activity of XPD/ERCC2 is required for DNA opening. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module CAK controls the initiation of transcription. XPD/ERCC2 acts by forming a bridge between CAK and the core-TFIIH complex. Involved in the regulation of vitamin-D receptor activity. As part of the mitotic spindle-associated MMXD complex it plays a role in chromosome segregation. Might have a role in aging process and could play a causative role in the generation of skin cancers. {ECO:0000250|UniProtKB:P18074}. PTM: ISGylated. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. SUBUNIT: Component of the 7-subunit TFIIH core complex composed of XPB/ERCC3, XPD/ERCC2, GTF2H1, GTF2H2, GTF2H3, GTF2H4 and GTF2H5, which is active in NER. The core complex associates with the 3-subunit CDK-activating kinase (CAK) module composed of CCNH/cyclin H, CDK7 and MNAT1 to form the 10-subunit holoenzyme (holo-TFIIH) active in transcription. The interaction with GTF2H2 results in the stimulation of the 5'-->3' helicase activity. Component of the MMXD complex, which includes CIAO1, ERCC2, CIAO2B, MMS19 and SLC25A5. Interacts with CIAO1 and CIAO2B; the interaction WITH CIAO2B is direct. Interacts with ATF7IP. Interacts directly with MMS19. {ECO:0000250|UniProtKB:P18074}. +P49135 ERCC3_MOUSE General transcription and DNA repair factor IIH helicase subunit XPB (TFIIH subunit XPB) (EC 3.6.4.12) (Basic transcription factor 2 89 kDa subunit) (BTF2 p89) (DNA excision repair protein ERCC-3) (DNA repair protein complementing XP-B cells) (TFIIH 89 kDa subunit) (Xeroderma pigmentosum group B-complementing protein) 783 89,126 Chain (1); Compositional bias (4); Domain (2); Modified residue (2); Motif (2); Nucleotide binding (1) FUNCTION: ATP-dependent 3'-5' DNA helicase, component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. The ATPase activity of XPB/ERCC3, but not its helicase activity, is required for DNA opening. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. The ATP-dependent helicase activity of XPB/ERCC3 is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module CAK controls the initiation of transcription. {ECO:0000250|UniProtKB:P19447}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Component of the 7-subunit TFIIH core complex composed of XPB/ERCC3, XPD/ERCC2, GTF2H1, GTF2H2, GTF2H3, GTF2H4 and GTF2H5, which is active in NER. The core complex associates with the 3-subunit CDK-activating kinase (CAK) module composed of CCNH/cyclin H, CDK7 and MNAT1 to form the 10-subunit holoenzyme (holo-TFIIH) active in transcription. Interacts with PUF60. Interacts with ATF7IP. {ECO:0000250|UniProtKB:P19447}. +Q9CR89 ERGI2_MOUSE Endoplasmic reticulum-Golgi intermediate compartment protein 2 377 42,482 Alternative sequence (2); Chain (1); Sequence conflict (5); Topological domain (3); Transmembrane (2) TRANSMEM 34 54 Helical. {ECO:0000255}.; TRANSMEM 320 340 Helical. {ECO:0000255}. TOPO_DOM 1 33 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 55 319 Lumenal. {ECO:0000255}.; TOPO_DOM 341 377 Cytoplasmic. {ECO:0000255}. FUNCTION: Possible role in transport between endoplasmic reticulum and Golgi. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Golgi apparatus, cis-Golgi network membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Cycles between the endoplasmic reticulum and the Golgi. SUBUNIT: May interact with EEF1A1. {ECO:0000250}. +P81270 ERG_MOUSE Transcriptional regulator ERG 486 54,614 Alternative sequence (3); Chain (1); Cross-link (1); DNA binding (1); Domain (1); Modified residue (3); Sequence conflict (1) FUNCTION: Transcriptional regulator. May participate in transcriptional regulation through the recruitment of SETDB1 histone methyltransferase and subsequent modification of local chromatin structure. SUBCELLULAR LOCATION: Nucleus. Cytoplasm {ECO:0000250}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. {ECO:0000250}. SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with SETDB1. {ECO:0000269|PubMed:11791185}. +Q9Z2E3 ERN2_MOUSE Serine/threonine-protein kinase/endoribonuclease IRE2 (Endoplasmic reticulum-to-nucleus signaling 2) (Inositol-requiring protein 2) (Ire1-beta) (IRE1b) (mIre1) [Includes: Serine/threonine-protein kinase (EC 2.7.11.1); Endoribonuclease (EC 3.1.26.-)] 911 101,262 Active site (1); Binding site (1); Chain (1); Domain (2); Glycosylation (1); Nucleotide binding (1); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 427 447 Helical. {ECO:0000255}. TOPO_DOM 35 426 Lumenal. {ECO:0000255}.; TOPO_DOM 448 911 Cytoplasmic. {ECO:0000255}. FUNCTION: Role in expression of the DDIT3 transcription factor, required for the unfolded-protein response, growth arrest and apoptosis. Has no effect on 28S ribosomal RNA cleavage, unlike the corresponding human protein. {ECO:0000269|PubMed:9755171}. PTM: Autophosphorylated. {ECO:0000250|UniProtKB:O75460}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:9755171}; Single-pass type I membrane protein {ECO:0000269|PubMed:9755171}. +Q8R180 ERO1A_MOUSE ERO1-like protein alpha (ERO1-L) (ERO1-L-alpha) (EC 1.8.4.-) (Endoplasmic reticulum oxidoreductase alpha) (Endoplasmic reticulum oxidoreductin-1-like protein) (Oxidoreductin-1-L-alpha) 464 54,084 Binding site (7); Chain (1); Disulfide bond (8); Glycosylation (2); Modified residue (2); Sequence conflict (1); Signal peptide (1) FUNCTION: Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme catalyzing protein disulfide formation, in order to allow P4HB to sustain additional rounds of disulfide formation. Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell. Required for the proper folding of immunoglobulins (By similarity). Plays an important role in ER stress-induced, CHOP-dependent apoptosis by activating the inositol 1,4,5-trisphosphate receptor IP3R1. {ECO:0000250, ECO:0000269|PubMed:19752026, ECO:0000269|PubMed:20308425}. PTM: N-glycosylated. {ECO:0000250}.; PTM: The Cys-94/Cys-99 and Cys-390/Cys-393 disulfide bonds constitute the redox-active center. The Cys-94/Cys-99 disulfide bond may accept electron from P4HB and funnel them to the active site disulfide Cys-390/Cys-393. The regulatory Cys-99/Cys-104 disulfide bond stabilizes the other regulatory bond Cys-94/Cys-130 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Lumenal side {ECO:0000250}. Note=The association with ERP44 is essential for its retention in the endoplasmic reticulum. {ECO:0000250}. SUBUNIT: Predominantly monomer. May function both as a monomer and a homodimer. Interacts with PDILT (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed (at protein level). {ECO:0000269|PubMed:20308425}. +Q8BKV1 GPC2_MOUSE Glypican-2 [Cleaved into: Secreted glypican-2] 579 63,344 Chain (2); Glycosylation (5); Lipidation (1); Propeptide (1); Signal peptide (1) FUNCTION: Cell surface proteoglycan that bears heparan sulfate. May fulfill a function related to the motile behaviors of developing neurons (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}; Extracellular side {ECO:0000250}.; SUBCELLULAR LOCATION: Secreted glypican-2: Secreted, extracellular space {ECO:0000250}. +Q5EBJ4 ERMIN_MOUSE Ermin (Juxtanodin) (JN) 281 32,148 Chain (1); Compositional bias (1); Erroneous initiation (1); Frameshift (1); Modified residue (5); Region (1); Sequence conflict (3) FUNCTION: Plays a role in cytoskeletal rearrangements during the late wrapping and/or compaction phases of myelinogenesis as well as in maintenance and stability of myelin sheath in the adult. May play an important role in late-stage oligodendroglia maturation, myelin/Ranvier node formation during CNS development, and in the maintenance and plasticity of related structures in the mature CNS (By similarity). {ECO:0000250, ECO:0000269|PubMed:16421295}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16421295}. SUBUNIT: Binds actin. {ECO:0000269|PubMed:16421295}. TISSUE SPECIFICITY: Brain and spinal cord. Exclusively expressed by the oligodendrocytes. Appears at a late stage during myelination, and in the mature nerves, it is localized to the outer cytoplasmic lip of the myelin sheath and the paranodal loops. {ECO:0000269|PubMed:16421295}. +Q923Z0 GPC5B_MOUSE G-protein coupled receptor family C group 5 member B (Retinoic acid-induced gene 2 protein) (RAIG-2) 410 45,899 Chain (1); Glycosylation (1); Modified residue (1); Sequence conflict (1); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 57 77 Helical; Name=1. {ECO:0000255}.; TRANSMEM 95 115 Helical; Name=2. {ECO:0000255}.; TRANSMEM 127 147 Helical; Name=3. {ECO:0000255}.; TRANSMEM 165 185 Helical; Name=4. {ECO:0000255}.; TRANSMEM 200 220 Helical; Name=5. {ECO:0000255}.; TRANSMEM 235 255 Helical; Name=6. {ECO:0000255}.; TRANSMEM 272 292 Helical; Name=7. {ECO:0000255}. TOPO_DOM 29 56 Extracellular. {ECO:0000255}.; TOPO_DOM 78 94 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 116 126 Extracellular. {ECO:0000255}.; TOPO_DOM 148 164 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 186 199 Extracellular. {ECO:0000255}.; TOPO_DOM 221 234 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 256 271 Extracellular. {ECO:0000255}.; TOPO_DOM 293 410 Cytoplasmic. {ECO:0000255}. FUNCTION: Unknown. This retinoic acid-inducible G-protein coupled receptor provide evidence for a possible interaction between retinoid and G-protein signaling pathways (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q9JIL6 GPC5D_MOUSE G-protein coupled receptor family C group 5 member D 344 39,056 Alternative sequence (2); Chain (1); Frameshift (2); Sequence conflict (3); Topological domain (8); Transmembrane (7) TRANSMEM 28 48 Helical; Name=1. {ECO:0000255}.; TRANSMEM 64 84 Helical; Name=2. {ECO:0000255}.; TRANSMEM 94 114 Helical; Name=3. {ECO:0000255}.; TRANSMEM 125 145 Helical; Name=4. {ECO:0000255}.; TRANSMEM 168 188 Helical; Name=5. {ECO:0000255}.; TRANSMEM 205 225 Helical; Name=6. {ECO:0000255}.; TRANSMEM 240 260 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 27 Extracellular. {ECO:0000255}.; TOPO_DOM 49 63 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 85 93 Extracellular. {ECO:0000255}.; TOPO_DOM 115 124 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 146 167 Extracellular. {ECO:0000255}.; TOPO_DOM 189 204 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 226 239 Extracellular. {ECO:0000255}.; TOPO_DOM 261 344 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q8K4Z6 GPC6A_MOUSE G-protein coupled receptor family C group 6 member A 928 104,213 Alternative sequence (2); Chain (1); Disulfide bond (1); Glycosylation (3); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 595 615 Helical. {ECO:0000255}.; TRANSMEM 631 651 Helical. {ECO:0000255}.; TRANSMEM 670 690 Helical. {ECO:0000255}.; TRANSMEM 707 727 Helical. {ECO:0000255}.; TRANSMEM 751 771 Helical. {ECO:0000255}.; TRANSMEM 785 805 Helical. {ECO:0000255}.; TRANSMEM 813 833 Helical. {ECO:0000255}. TOPO_DOM 21 594 Extracellular. {ECO:0000255}.; TOPO_DOM 616 630 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 652 669 Extracellular. {ECO:0000255}.; TOPO_DOM 691 706 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 728 750 Extracellular. {ECO:0000255}.; TOPO_DOM 772 784 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 806 812 Extracellular. {ECO:0000255}.; TOPO_DOM 834 928 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor activated by amino acids with a preference for basic amino acids such as L-Lys, L-Arg and L-ornithine but also by small and polar amino acids. The L-alpha amino acids respond is augmented by divalent cations Ca(2+) and Mg(2+). Activated by extracellular calcium and osteocalcin. Seems to act through a G(q)/G(11) and G(i)-coupled pathway. Mediates the non-genomic effects of androgens in multiple tissue. May coordinate nutritional and hormonal anabolic signals through the sensing of extracellular amino acids, osteocalcin, divalent ions and its responsiveness to anabolic steroids. {ECO:0000269|PubMed:15576628, ECO:0000269|PubMed:16199532, ECO:0000269|PubMed:19050760, ECO:0000269|PubMed:20947496}. PTM: N-glycosylated. {ECO:0000269|PubMed:15816861}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15816861}; Multi-pass membrane protein {ECO:0000269|PubMed:15816861}. SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:15816861}. TISSUE SPECIFICITY: Expressed at high level in liver, lung, spleen and heart. Expressed at lower level in kidney, skeletal muscle and brain. Expressed in E7, E11, E15 and E17 embryos. {ECO:0000269|PubMed:15816861, ECO:0000269|PubMed:16199532}. +Q9EQY0 ERN1_MOUSE Serine/threonine-protein kinase/endoribonuclease IRE1 (Endoplasmic reticulum-to-nucleus signaling 1) (Inositol-requiring protein 1) (Ire1-alpha) (IRE1a) [Includes: Serine/threonine-protein kinase (EC 2.7.11.1); Endoribonuclease (EC 3.1.26.-)] 977 110,185 Active site (1); Alternative sequence (2); Beta strand (14); Binding site (3); Chain (1); Domain (2); Glycosylation (1); Helix (23); Mutagenesis (5); Nucleotide binding (3); Region (1); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (6) TRANSMEM 446 466 Helical. {ECO:0000255}. TOPO_DOM 21 445 Lumenal. {ECO:0000255}.; TOPO_DOM 467 977 Cytoplasmic. {ECO:0000255}. FUNCTION: Serine/threonine-protein kinase and endoribonuclease that acts as a key sensor for the endoplasmic reticulum unfolded protein response (UPR) (PubMed:11850408, PubMed:25164867). In unstressed cells, the endoplasmic reticulum luminal domain is maintained in its inactive monomeric state by binding to the endoplasmic reticulum chaperone HSPA5/BiP. Accumulation of misfolded protein in the endoplasmic reticulum causes release of HSPA5/BiP, allowing the luminal domain to homodimerize, promoting autophosphorylation of the kinase domain and subsequent activation of the endoribonuclease activity (PubMed:25164867). The endoribonuclease activity is specific for XBP1 mRNA and excises 26 nucleotides from XBP1 mRNA (PubMed:11850408, PubMed:25164867). The resulting spliced transcript of XBP1 encodes a transcriptional activator protein that up-regulates expression of UPR target genes (PubMed:11850408, PubMed:25164867). Acts as an upstream signal for ER stress-induced GORASP2-mediated unconventional (ER/Golgi-independent) trafficking of CFTR to cell membrane by modulating the expression and localization of SEC16A (By similarity). {ECO:0000250|UniProtKB:O75460, ECO:0000269|PubMed:11850408, ECO:0000269|PubMed:25164867}. PTM: Autophosphorylated following homodimerization. Autophosphorylation promotes activation of the endoribonuclease domain. {ECO:0000269|PubMed:25164867}.; PTM: ADP-ribosylated by PARP16 upon ER stress, which increases both kinase and endonuclease activities. {ECO:0000250|UniProtKB:O75460}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11850408}; Single-pass type I membrane protein {ECO:0000269|PubMed:11850408}. SUBUNIT: Monomer (By similarity). Homodimer; disulfide-linked; homodimerization takes place in response to endoplasmic reticulum stress and promotes activation of the kinase and endoribonuclease activities (PubMed:25164867). Dimer formation is driven by hydrophobic interactions within the N-terminal luminal domains and stabilized by disulfide bridges (PubMed:25164867). Interacts (via the luminal region) with DNAJB9/ERdj4; interaction takes place in unstressed cells and promotes recruitment of HSPA5/BiP (By similarity). Interacts (via the luminal region) with HSPA5/BiP; HSPA5/BiP is a negative regulator of the unfolded protein response (UPR) that prevents homodimerization of ERN1/IRE1 and subsequent activation of the protein (By similarity). Interacts with PDIA6, a negative regulator of the UPR; the interaction is direct and disrupts homodimerization (By similarity). Interacts with DAB2IP (via PH domain); the interaction occurs in a endoplasmic reticulum stress-induced dependent manner and is required for subsequent recruitment of TRAF2 to ERN1/IRE1 (PubMed:18281285). Interacts with TAOK3 and TRAF2 (By similarity). {ECO:0000250|UniProtKB:O75460, ECO:0000269|PubMed:18281285, ECO:0000269|PubMed:25164867}. TISSUE SPECIFICITY: Ubiquitously expressed. High levels in thymus, liver and lung. In the brain, preferentially expressed in cortical, hippocampal and olfactory neurons. {ECO:0000269|PubMed:11146108}. +Q3ULJ0 GPD1L_MOUSE Glycerol-3-phosphate dehydrogenase 1-like protein (EC 1.1.1.8) 351 38,226 Active site (1); Alternative sequence (1); Binding site (7); Chain (1); Erroneous initiation (2); Nucleotide binding (1); Region (1); Sequence conflict (4) FUNCTION: Plays a role in regulating cardiac sodium current; decreased enzymatic activity with resulting increased levels of glycerol 3-phosphate activating the DPD1L-dependent SCN5A phosphorylation pathway, may ultimately lead to decreased sodium current; cardiac sodium current may also be reduced due to alterations of NAD(H) balance induced by DPD1L. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. SUBUNIT: Interacts with SCN5A. {ECO:0000250}. +O08580 ERR1_MOUSE Steroid hormone receptor ERR1 (Estrogen receptor-like 1) (Estrogen-related receptor alpha) (ERR-alpha) (Nuclear receptor subfamily 3 group B member 1) 422 45,464 Chain (1); Cross-link (4); DNA binding (1); Domain (1); Modified residue (6); Region (2); Sequence conflict (3); Site (1); Zinc finger (2) FUNCTION: Binds to an ERR-alpha response element (ERRE) containing a single consensus half-site, 5'-TNAAGGTCA-3'. Can bind to the medium-chain acyl coenzyme A dehydrogenase (MCAD) response element NRRE-1 and may act as an important regulator of MCAD promoter. Binds to the C1 region of the lactoferrin gene promoter. Requires dimerization and the coactivator, PGC-1A, for full activity. The ERRalpha/PGC1alpha complex is a regulator of energy metabolism. Induces the expression of PERM1 in the skeletal muscle (By similarity). {ECO:0000250}. PTM: Phosphorylation on Ser-19 enhances sumoylation on Lys-14 increasing repression of transcriptional activity. {ECO:0000250}.; PTM: Sumoylated with SUMO2. Main site is Lys-14 which is enhanced by phosphorylation on Ser-19, cofactor activation, and by interaction with PIAS4. Sumoylation enhances repression of transcriptional activity, but has no effect on subcellular location nor on DNA binding (By similarity). {ECO:0000250}.; PTM: Reversibly acetylated. Acetylation by PCAF/KAT2 at Lys-129, Lys-138, Lys-160 and Lys-162 and PCAF/KAT2 decreases transcriptional activity probably by inhibiting DNA-binding activity; deacetylation involves SIRT1 and HDAC8 and increases DNA-binding (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P11474, ECO:0000255|PROSITE-ProRule:PRU00407}. Cytoplasm {ECO:0000250|UniProtKB:P11474}. Note=Co-localizes to the cytoplasm only in presence of MAPK15. {ECO:0000250|UniProtKB:P11474}. SUBUNIT: Binds DNA as a monomer or a homodimer. Interacts (via the AF2 domain) with coactivator PPARGC1A (via the L3 motif); the interaction greatly enhances transcriptional activity of genes involved in energy metabolism. Interacts with PIAS4; the interaction enhances sumoylation (By similarity). Interacts with MAPK15; promotes re-localization of ESRRA to the cytoplasm through a XPO1-dependent mechanism then inhibits ESRRA transcriptional activity (PubMed:21190936). {ECO:0000250, ECO:0000269|PubMed:21190936}. TISSUE SPECIFICITY: Most highly expressed in kidney, heart, and brown adipocytes. Also found in utERus, cervix and vagina. +Q61539 ERR2_MOUSE Steroid hormone receptor ERR2 (Estrogen receptor-like 2) (Estrogen-related receptor beta) (ERR-beta) (Nuclear receptor subfamily 3 group B member 2) 433 48,328 Chain (1); DNA binding (1); Domain (1); Mutagenesis (3); Region (2); Sequence conflict (1); Site (1); Zinc finger (2) FUNCTION: Transcription factor that binds a canonical ESRRB recognition (ERRE) sequence 5'TCAAGGTCA-3' localized on promoter and enhancer of targets genes regulating their expression or their transcriptional activity (PubMed:27601327, PubMed:23169531, PubMed:23508100, PubMed:26206133, PubMed:20534447, PubMed:18662995, PubMed:18957414, PubMed:27723719, PubMed:23019124). Plays a role, in a LIF-independent manner, in maintainance of self-renewal and pluripotency of embryonic and trophoblast stem cells through different signaling pathways including FGF signaling pathway and Wnt signaling pathways (PubMed:18957414, PubMed:26206133, PubMed:20534447, PubMed:23040478, PubMed:23040477, PubMed:23019124, PubMed:23169531). Upon FGF signaling pathway activation, interacts with KDM1A by directly binding to enhancer site of ELF5 and EOMES and activating their transcription leading to self-renewal of trophoblast stem cells (PubMed:26206133). Also regulates expression of multiple rod-specific genes and is required for survival of this cell type (PubMed:20534447). Plays a role as transcription factor activator of GATA6, NR0B1, POU5F1 and PERM1 (PubMed:18662995, PubMed:23508100, PubMed:18957414). Plays a role as transcription factor repressor of NFE2L2 transcriptional activity and ESR1 transcriptional activity (By similarity). During mitosis remains bound to a subset of interphase target genes, including pluripotency regulators, through the canonical ESRRB recognition (ERRE) sequence, leading to their transcriptional activation in early G1 phase (PubMed:27723719). Can coassemble on structured DNA elements with other transcription factors like SOX2, POU5F1, KDM1A and NCOA3 to trigger ESRRB-dependent gene activation (PubMed:23019124, PubMed:23169531, PubMed:18662995, PubMed:26206133). This mechanism, in the case of SOX2 corecruitment prevents the embryonic stem cells (ESCs) to epiblast stem cells (EpiSC) transition through positive regulation of NR0B1 that inhibits the EpiSC transcriptional program (PubMed:23169531). Also plays a role inner ear development by controlling expression of ion channels and transporters and in early placentation (PubMed:9285590, PubMed:17765677). {ECO:0000250|UniProtKB:O95718, ECO:0000269|PubMed:17765677, ECO:0000269|PubMed:18662995, ECO:0000269|PubMed:18957414, ECO:0000269|PubMed:20534447, ECO:0000269|PubMed:23019124, ECO:0000269|PubMed:23040477, ECO:0000269|PubMed:23040478, ECO:0000269|PubMed:23169531, ECO:0000269|PubMed:23508100, ECO:0000269|PubMed:26206133, ECO:0000269|PubMed:27601327, ECO:0000269|PubMed:27723719, ECO:0000269|PubMed:9285590}. PTM: Acetylated by PCAF/KAT2 (in vitro). {ECO:0000250|UniProtKB:O95718}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18472334}. Cytoplasm {ECO:0000269|PubMed:18472334}. Chromosome {ECO:0000269|PubMed:27723719}. SUBUNIT: Binds DNA as a monomer (By similarity). Interacts with NR0B1; represses ESRRB activity at the GATA6 promoter (PubMed:27601327, PubMed:23508100). Interacts with NANOG; reciprocally modulates their transcriptional activities and activates POU5F1 expression (PubMed:18957414). Interacts with NCOA3; mediates the interaction between ESRRB and RNA polymerase II complexes and allows NCOA3 corecruitment to ESRRB, KLF4, NANOG, and SOX2 enhancer regions to trigger ESRRB-dependent gene activation involved in self-renewal and pluripotency (PubMed:23019124). Interacts with KDM1A; co-occupes the core set of ESRRB targets including ELF5 and EOMES (PubMed:26206133). Interacts with the multiprotein complex Integrator, at least composed of INTS1, INTS2, INTS3, INTS4, INTS5, INTS6, INTS7, INTS8, INTS9/RC74, INTS10, INTS11/CPSF3L and INTS12; ESRRB is probably not a core component of the integrator complex and associates to integrator via its interaction with INTS1 and INTS9; attracts the transcriptional machinery (PubMed:26206133). Interacts with JARID2 (PubMed:26523946). Interacts with POU5F1; recruits ESRRB near the POU5F1-SOX2 element in the NANOG proximal promoter leading to activation of NANOG expression; the intercaction is DNA independent (PubMed:18662995). {ECO:0000250|UniProtKB:O95718, ECO:0000269|PubMed:18662995, ECO:0000269|PubMed:18957414, ECO:0000269|PubMed:23019124, ECO:0000269|PubMed:23508100, ECO:0000269|PubMed:26206133, ECO:0000269|PubMed:26523946, ECO:0000269|PubMed:27601327}. TISSUE SPECIFICITY: Highly expressed in undifferentiated ESCs (PubMed:23508100). Expressed in immature horizontal cells and in rod photoreceptors at intermediate and late stages of differentiation (PubMed:20534447). Expressed in endolymph-producing epithelial cells (PubMed:17765677). {ECO:0000269|PubMed:17765677, ECO:0000269|PubMed:20534447, ECO:0000269|PubMed:23508100}. +P62509 ERR3_MOUSE Estrogen-related receptor gamma (Estrogen receptor-related protein 3) (Nuclear receptor subfamily 3 group B member 3) 458 51,306 Alternative sequence (1); Beta strand (3); Chain (1); Cross-link (1); DNA binding (1); Domain (1); Erroneous initiation (1); Helix (10); Modified residue (1); Mutagenesis (4); Sequence conflict (1); Turn (3); Zinc finger (2) FUNCTION: Orphan receptor that acts as transcription activator in the absence of bound ligand. Binds specifically to an estrogen response element and activates reporter genes controlled by estrogen response elements. Induces the expression of PERM1 in the skeletal muscle. {ECO:0000269|PubMed:10428842}. PTM: Acetylated by PCAF/KAT2 (in vitro). {ECO:0000250}.; PTM: Sumoylation on Lys-40 is enhanced by phosphorylation at Ser-45 and represses transcriptional activity. {ECO:0000250}.; PTM: Phosphorylation on Ser-45 enhances sumoylation on Lys-40 thus repressing transcriptional activity. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Homodimer. Interacts with NRIP1, NCOA1 and NCOR2 (By similarity). Binds TLE1, PNRC1 and PNRC2 (By similarity). Binds GRIP1. {ECO:0000250, ECO:0000269|PubMed:10428842, ECO:0000269|PubMed:15161930}. TISSUE SPECIFICITY: Highly expressed in the heart, brain and kidney and low expression in the liver. {ECO:0000269|PubMed:10428842}. +Q9D952 EVPL_MOUSE Envoplakin (210 kDa cornified envelope precursor protein) (p210) 2035 232,012 Chain (1); Coiled coil (1); Domain (1); Modified residue (3); Region (4); Repeat (8); Sequence conflict (13) FUNCTION: Component of the cornified envelope of keratinocytes. May link the cornified envelope to desmosomes and intermediate filaments. SUBCELLULAR LOCATION: Cell junction, desmosome {ECO:0000250}. Cornified envelope {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Colocalized with DSP at desmosomes and along intermediate filaments. {ECO:0000250}. SUBUNIT: May form a homodimer or a heterodimer with PPL. +P23683 EVX1_MOUSE Homeobox even-skipped homolog protein 1 (EVX-1) 416 43,198 Chain (1); Compositional bias (4); DNA binding (1) FUNCTION: May play a role in the specification of neuronal cell types. May play a role in the dorsoventral specification of mesodermal cell fate. SUBCELLULAR LOCATION: Nucleus. +Q64521 GPDM_MOUSE Glycerol-3-phosphate dehydrogenase, mitochondrial (GPD-M) (GPDH-M) (EC 1.1.5.3) (Protein TISP38) 727 80,954 Calcium binding (1); Chain (1); Domain (2); Modified residue (1); Nucleotide binding (1); Sequence conflict (9); Transit peptide (1) Polyol metabolism; glycerol degradation via glycerol kinase pathway; glycerone phosphate from sn-glycerol 3-phosphate (anaerobic route): step 1/1. SUBCELLULAR LOCATION: Mitochondrion inner membrane. +Q925Q5 GPHA2_MOUSE Glycoprotein hormone alpha-2 (Putative secreted protein Zsig51) (Thyrostimulin subunit alpha) 128 14,030 Chain (1); Disulfide bond (4); Glycosylation (2); Signal peptide (1) FUNCTION: Functions as a heterodimeric glycoprotein hormone with GPHB5 able to bind and activate the thyroid-stimulating hormone receptor (TSHR), leading to increased cAMP production. Plays a central role in controlling thyroid cell metabolism. {ECO:0000250|UniProtKB:Q96T91}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Heterodimer with GPHB5; this heterodimer interacts with thyroid-stimulating hormone receptor (TSHR), and hence stimulates cAMP production. {ECO:0000250|UniProtKB:Q96T91}. +Q812B2 GPHB5_MOUSE Glycoprotein hormone beta-5 (Thyrostimulin subunit beta) 130 14,249 Chain (1); Disulfide bond (5); Frameshift (1); Glycosylation (1); Signal peptide (1) FUNCTION: Functions as a heterodimeric glycoprotein hormone with GPHA2 able to bind and activate the thyroid-stimulating hormone receptor (TSHR), leading to increased cAMP production. Plays a central role in controlling thyroid cell metabolism. {ECO:0000250|UniProtKB:Q86YW7}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q86YW7}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Heterodimer with GPHA2; this heterodimer interacts with thyroid-stimulating hormone receptor (TSHR), and hence stimulates cAMP production. {ECO:0000250|UniProtKB:Q86YW7}. TISSUE SPECIFICITY: Expressed in the anterior lobe of pituitary. +Q8BS95 GPHR_MOUSE Golgi pH regulator (Protein GPR89) 455 52,735 Chain (1); Glycosylation (1); Sequence conflict (1); Transmembrane (9) TRANSMEM 5 25 Helical. {ECO:0000255}.; TRANSMEM 46 66 Helical. {ECO:0000255}.; TRANSMEM 79 99 Helical. {ECO:0000255}.; TRANSMEM 114 134 Helical. {ECO:0000255}.; TRANSMEM 150 170 Helical. {ECO:0000255}.; TRANSMEM 288 308 Helical. {ECO:0000255}.; TRANSMEM 343 363 Helical. {ECO:0000255}.; TRANSMEM 378 398 Helical. {ECO:0000255}.; TRANSMEM 425 445 Helical. {ECO:0000255}. FUNCTION: Voltage dependent anion channel required for acidification and functions of the Golgi apparatus that may function in counter-ion conductance. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Detected at low levels in lysosomes and endosomes. {ECO:0000250}. SUBUNIT: Homotrimer. {ECO:0000250}. +P97464 EXT1_MOUSE Exostosin-1 (EC 2.4.1.224) (EC 2.4.1.225) (Glucuronosyl-N-acetylglucosaminyl-proteoglycan/N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase) (Multiple exostoses protein 1 homolog) 746 86,308 Active site (1); Binding site (2); Chain (1); Disulfide bond (1); Glycosylation (2); Metal binding (1); Region (4); Sequence conflict (5); Topological domain (2); Transmembrane (1) TRANSMEM 8 28 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 7 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 29 746 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Glycosyltransferase required for the biosynthesis of heparan-sulfate. The EXT1/EXT2 complex possesses substantially higher glycosyltransferase activity than EXT1 or EXT2 alone. Required for the exosomal release of SDCBP, CD63 and syndecan (By similarity). {ECO:0000250|UniProtKB:Q16394}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:9620772, ECO:0000269|PubMed:9703997}; Single-pass type II membrane protein {ECO:0000269|PubMed:9620772, ECO:0000269|PubMed:9703997}. Golgi apparatus membrane {ECO:0000269|PubMed:10639137}; Single-pass type II membrane protein {ECO:0000269|PubMed:10639137}. Note=The EXT1/EXT2 complex is localized in the Golgi apparatus. {ECO:0000269|PubMed:10639137}. SUBUNIT: Forms a homo/hetero-oligomeric complex with EXT2. {ECO:0000250|UniProtKB:Q16394}. TISSUE SPECIFICITY: Expressed in maturing chondrocytes. +Q9JKV7 EXTL1_MOUSE Exostosin-like 1 (EC 2.4.1.224) (Exostosin-L) (Glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase) (Multiple exostosis-like protein) 669 74,079 Chain (1); Disulfide bond (1); Glycosylation (2); Sequence conflict (5); Topological domain (2); Transmembrane (1) TRANSMEM 9 29 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 8 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 30 669 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Probable glycosyltransferase. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. +Q9ES89 EXTL2_MOUSE Exostosin-like 2 (EC 2.4.1.223) (Alpha-1,4-N-acetylhexosaminyltransferase EXTL2) (Alpha-GalNAcT EXTL2) (EXT-related protein 2) (Glucuronyl-galactosyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase) 330 37,391 Active site (1); Beta strand (15); Binding site (2); Chain (1); Disulfide bond (1); Glycosylation (1); Helix (9); Metal binding (1); Mutagenesis (3); Region (4); Sequence conflict (1); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 22 42 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 21 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 43 330 Lumenal. {ECO:0000255}. FUNCTION: Glycosyltransferase required for the biosynthesis of heparan-sulfate and responsible for the alternating addition of beta-1-4-linked glucuronic acid (GlcA) and alpha-1-4-linked N-acetylglucosamine (GlcNAc) units to nascent heparan sulfate chains. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. +P70351 EZH1_MOUSE Histone-lysine N-methyltransferase EZH1 (EC 2.1.1.43) (ENX-2) (Enhancer of zeste homolog 1) 747 85,188 Alternative sequence (1); Chain (1); Compositional bias (1); Cross-link (1); Domain (2); Erroneous initiation (9); Motif (1); Sequence conflict (3) FUNCTION: Polycomb group (PcG) protein. Catalytic subunit of the PRC2/EED-EZH1 complex, which methylates 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. Able to mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively. Required for embryonic stem cell derivation and self-renewal, suggesting that it is involved in safeguarding embryonic stem cell identity. Compared to EZH2-containing complexes, it is less abundant in embryonic stem cells, has weak methyltransferase activity and plays a less critical role in forming H3K27me3, which is required for embryonic stem cell identity and proper differentiation. {ECO:0000269|PubMed:19026780}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Colocalizes with trimethylated 'Lys-27' of histone H3. {ECO:0000250}. SUBUNIT: Component of the PRC2/EED-EZH1 complex, which includes EED, EZH1, SUZ12, RBBP4 and AEBP2. The PRC2/EED-EZH1 is less abundant than the PRC2/EED-EZH2 complex, has weak methyltransferase activity and compacts chromatin in the absence of the methyltransferase cofactor S-adenosyl-L-methionine (SAM). {ECO:0000269|PubMed:19026780, ECO:0000269|PubMed:20144788}. TISSUE SPECIFICITY: Expressed at high levels in kidney, adrenal gland, testis and brain. {ECO:0000269|PubMed:9473645}. +Q61188 EZH2_MOUSE Histone-lysine N-methyltransferase EZH2 (EC 2.1.1.43) (ENX-1) (Enhancer of zeste homolog 2) 746 85,292 Alternative sequence (1); Chain (1); Compositional bias (1); Cross-link (1); Domain (2); Erroneous gene model prediction (1); Glycosylation (1); Helix (1); Modified residue (8); Mutagenesis (6); Region (3); Sequence conflict (2) FUNCTION: Polycomb group (PcG) protein. Catalytic subunit of the PRC2/EED-EZH2 complex, which methylates (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene. Able to mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively. Displays a preference for substrates with less methylation, loses activity when progressively more methyl groups are incorporated into H3K27, H3K27me0 > H3K27me1 > H3K27me2. Compared to EZH1-containing complexes, it is more abundant in embryonic stem cells and plays a major role in forming H3K27me3, which is required for embryonic stem cell identity and proper differentiation. The PRC2/EED-EZH2 complex may also serve as a recruiting platform for DNA methyltransferases, thereby linking two epigenetic repression systems. Genes repressed by the PRC2/EED-EZH2 complex include HOXA7, HOXB6 and HOXC8. EZH2 can also methylate non-histone proteins such as the transcription factor GATA4 and the nuclear receptor RORA. Regulates the circadian clock via histone methylation at the promoter of the circadian genes. Essential for the CRY1/2-mediated repression of the transcriptional activation of PER1/2 by the CLOCK-ARNTL/BMAL1 heterodimer; involved in the di and trimethylation of 'Lys-27' of histone H3 on PER1/2 promoters which is necessary for the CRY1/2 proteins to inhibit transcription. {ECO:0000250|UniProtKB:Q15910, ECO:0000269|PubMed:12689588, ECO:0000269|PubMed:15516932, ECO:0000269|PubMed:15520282, ECO:0000269|PubMed:16717091, ECO:0000269|PubMed:18086877, ECO:0000269|PubMed:19026780}. PTM: Phosphorylated by AKT1 (By similarity). Phosphorylation by AKT1 reduces methyltransferase activity. Phosphorylation at Thr-345 by CDK1 and CDK2 promotes maintenance of H3K27me3 levels at EZH2-target loci, thus leading to epigenetic gene silencing (By similarity). {ECO:0000250}.; PTM: Sumoylated. {ECO:0000250}.; PTM: Glycosylated: O-GlcNAcylation at Ser-75 by OGT increases stability of EZH2 and facilitates the formation of H3K27me3 by the PRC2/EED-EZH2 complex. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Localizes to the inactive X chromosome in trophoblast stem cells. SUBUNIT: Component of the PRC2/EED-EZH2 complex, which includes EED, EZH2, SUZ12, RBBP4 and RBBP7 and possibly AEBP2 (By similarity). The minimum components required for methyltransferase activity of the PRC2/EED-EZH2 complex are EED, EZH2 and SUZ12 (By similarity). The PRC2 complex may also interact with DNMT1, DNMT3A, DNMT3B and PHF1 via the EZH2 subunit and with SIRT1 via the SUZ12 subunit (By similarity). Interacts with HDAC1 and HDAC2 (By similarity). Binds ATRX via the SET domain (By similarity). Interacts with PRAME (By similarity). Interacts with CDYL (By similarity). Interacts with EED. Interacts with ARNTL/BMAL1. Interacts with CLOCK and CRY1. Interacts with DNMT3L; the interaction is direct (PubMed:24074865). {ECO:0000250|UniProtKB:Q15910, ECO:0000269|PubMed:16717091, ECO:0000269|PubMed:17259173, ECO:0000269|PubMed:17937919, ECO:0000269|PubMed:19026780, ECO:0000269|PubMed:20144788, ECO:0000269|PubMed:23970558, ECO:0000269|PubMed:24074865, ECO:0000269|PubMed:9742080}. TISSUE SPECIFICITY: Present in actively dividing cells. Widely expressed in early embryos. In later embryogenesis, expression restricted to central and peripheral nervous system, liver and thymus. In adult, highest expression in spleen, testis and placenta. Lower levels in intestine and muscle and very low levels in brain and liver. No expression in heart, thyroid gland, lung and kidney. {ECO:0000269|PubMed:19026781}. +Q9Z191 EYA4_MOUSE Eyes absent homolog 4 (EC 3.1.3.48) 616 66,875 Active site (2); Chain (1); Cross-link (2); Metal binding (3); Modified residue (2); Sequence conflict (1) FUNCTION: Tyrosine phosphatase that specifically dephosphorylates 'Tyr-142' of histone H2AX (H2AXY142ph). 'Tyr-142' phosphorylation of histone H2AX plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress. Promotes efficient DNA repair by dephosphorylating H2AX, promoting the recruitment of DNA repair complexes containing MDC1. Its function as histone phosphatase probably explains its role in transcription regulation during organogenesis. May be involved in development of the eye (By similarity). {ECO:0000250|UniProtKB:Q99502}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q99502}. Nucleus {ECO:0000250|UniProtKB:Q99502}. SUBUNIT: Interacts with SIX3; translocates EYA4 from the cytoplasm to the nucleus and promotes activation of their target genes. {ECO:0000250|UniProtKB:O95677}. TISSUE SPECIFICITY: In the embryo, expressed mainly in the craniofacial mesenchyme, dermamyotome and limb. {ECO:0000269|PubMed:9887327}. +Q3TGF2 F107B_MOUSE Protein FAM107B 131 15,572 Chain (1); Coiled coil (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (2) TISSUE SPECIFICITY: Expressed in the hippocampus and hypothalamus. Expressed in the pontine nuclei and reticulotegmental nucleus. Expressed in Purkinje cell and nuclear layers of the cerebelum. Expressed in the choroid plexus. Expressed in hippocampal granule neurons of the dente gyrus. {ECO:0000269|PubMed:25637808}. +Q6A0A9 F120A_MOUSE Constitutive coactivator of PPAR-gamma-like protein 1 (Oxidative stress-associated Src activator) (Protein FAM120A) 1112 121,646 Chain (1); Erroneous initiation (1); Modified residue (11); Region (2) FUNCTION: Critical component of the oxidative stress-induced survival signaling. Activates src family kinases and acts as a scaffolding protein enabling src family kinases to phosphorylate and activate PI3-kinase. Binds RNA and promotes the secretion of IGF-II (By similarity). May participate in mRNA transport in the cytoplasm. {ECO:0000250, ECO:0000269|PubMed:18413649}. PTM: Arg-980 is dimethylated, probably to asymmetric dimethylarginine. {ECO:0000250}.; PTM: Phosphorylated on tyrosine by src family kinases upon ultraviolet exposure. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Translocates to plasma membrane upon ultraviolet exposure. {ECO:0000250}. SUBUNIT: Interacts with YES1, SRC, FYN. Upon tyrosine phosphorylation, interacts with PIK3R1 (By similarity). Interacts with PURA. {ECO:0000250, ECO:0000269|PubMed:18413649}. TISSUE SPECIFICITY: Present in Purkinje cells in the cerebellum, and in cortical neurons (at protein level). {ECO:0000269|PubMed:18413649}. +Q99L47 F10A1_MOUSE Hsc70-interacting protein (Hip) (Protein FAM10A1) (Protein ST13 homolog) 371 41,656 Chain (1); Compositional bias (1); Domain (1); Modified residue (3); Repeat (3) FUNCTION: One HIP oligomer binds the ATPase domains of at least two HSC70 molecules dependent on activation of the HSC70 ATPase by HSP40. Stabilizes the ADP state of HSC70 that has a high affinity for substrate protein. Through its own chaperone activity, it may contribute to the interaction of HSC70 with various target proteins (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homotetramer. Interacts with HSC70 as well as DNAJ homologs and HSP90 (By similarity). Interacts (via the C-terminus 302- 318 AA) with GRK5 (By similarity). {ECO:0000250}. +Q6RI63 F120B_MOUSE Constitutive coactivator of peroxisome proliferator-activated receptor gamma (Constitutive coactivator of PPAR-gamma) (Constitutive coactivator of PPARG) (Protein FAM120B) 786 89,313 Alternative sequence (2); Chain (1); Erroneous initiation (2); Erroneous translation (1); Region (1); Sequence conflict (3) FUNCTION: Functions as a transactivator of PPARG and ESR1. Functions in adipogenesis through PPARG activation. {ECO:0000269|PubMed:17595322}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17595322}. SUBUNIT: Interacts with ESR1 and RXRA. Interacts with PPARG; in a ligand-independent manner. {ECO:0000269|PubMed:17595322}. TISSUE SPECIFICITY: Ubiquitously expressed (at protein level). {ECO:0000269|PubMed:17595322}. +Q8C3F2 F120C_MOUSE Constitutive coactivator of PPAR-gamma-like protein 2 (Protein FAM120C) 1091 119,718 Alternative sequence (4); Chain (1); Erroneous initiation (1); Modified residue (2); Sequence conflict (3) +Q8BP78 F10C1_MOUSE Protein FRA10AC1 homolog 315 37,202 Chain (1); Erroneous initiation (1); Modified residue (6); Sequence caution (1); Sequence conflict (4) SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +Q8R184 F110A_MOUSE Protein FAM110A 296 31,582 Chain (1); Compositional bias (2); Frameshift (1); Sequence conflict (1) SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle pole. Note=Distributed throughout the cytoplasm during mitosis, accumulating at spindle poles. {ECO:0000250}. SUBUNIT: May interact with CSPP1. {ECO:0000305}. +Q8C739 F110B_MOUSE Protein FAM110B 366 40,360 Chain (1); Modified residue (2); Sequence conflict (1) SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. +Q6NZE7 F122B_MOUSE Protein FAM122B 255 27,686 Alternative sequence (3); Chain (1); Initiator methionine (1); Modified residue (10); Sequence conflict (2) +Q6NS59 F135A_MOUSE Protein FAM135A 1506 166,857 Alternative sequence (1); Chain (1); Erroneous initiation (1); Sequence conflict (7) +Q8BH61 F13A_MOUSE Coagulation factor XIII A chain (Coagulation factor XIIIa) (EC 2.3.2.13) (Protein-glutamine gamma-glutamyltransferase A chain) (Transglutaminase A chain) 732 83,207 Active site (3); Chain (1); Glycosylation (1); Initiator methionine (1); Metal binding (4); Modified residue (1); Propeptide (1); Sequence conflict (1); Site (1) FUNCTION: Factor XIII is activated by thrombin and calcium ion to a transglutaminase that catalyzes the formation of gamma-glutamyl-epsilon-lysine cross-links between fibrin chains, thus stabilizing the fibrin clot. Also cross-link alpha-2-plasmin inhibitor, or fibronectin, to the alpha chains of fibrin. {ECO:0000250|UniProtKB:P00488}. PTM: The activation peptide is released by thrombin. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P00488}. Secreted {ECO:0000250|UniProtKB:P00488}. Note=Secreted into the blood plasma. Cytoplasmic in most tissues, but also secreted in the blood plasma. {ECO:0000250|UniProtKB:P00488}. SUBUNIT: Tetramer of two A chains (F13A1) and two B (F13B) chains. {ECO:0000250|UniProtKB:P00488}. +Q07968 F13B_MOUSE Coagulation factor XIII B chain (Protein-glutamine gamma-glutamyltransferase B chain) (Transglutaminase B chain) 669 76,195 Chain (1); Disulfide bond (20); Domain (10); Erroneous initiation (1); Glycosylation (2); Sequence conflict (1); Signal peptide (1) FUNCTION: The B chain of factor XIII is not catalytically active, but is thought to stabilize the A subunits and regulate the rate of transglutaminase formation by thrombin. {ECO:0000250|UniProtKB:P05160}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P05160}. SUBUNIT: Tetramer of two A chains (F13A1) and two B (F13B) chains. {ECO:0000250|UniProtKB:P05160}. TISSUE SPECIFICITY: Predominantly expressed in liver and kidney. {ECO:0000269|PubMed:8468048}. +Q6NSV7 F149B_MOUSE Protein FAM149B1 578 63,213 Alternative sequence (8); Chain (1); Erroneous initiation (1) +Q8CCS2 F155A_MOUSE Transmembrane protein FAM155A 467 52,739 Alternative sequence (2); Chain (1); Compositional bias (2); Glycosylation (4); Transmembrane (2) TRANSMEM 40 60 Helical. {ECO:0000255}.; TRANSMEM 426 446 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8CHT6 F169B_MOUSE Protein FAM169B 337 38,125 Chain (1) +Q9D4K5 F166A_MOUSE Protein FAM166A 319 36,613 Chain (1) +Q6P1G6 F167A_MOUSE Protein FAM167A 215 24,319 Chain (1); Coiled coil (1) +P17257 F167B_MOUSE Protein FAM167B (Protein SEC) 162 18,529 Chain (1); Erroneous initiation (1); Sequence conflict (2) +Q505K2 F16A1_MOUSE Protein FAM160A1 1081 120,219 Chain (1); Compositional bias (1); Erroneous initiation (1) +Q3U2I3 F16A2_MOUSE FTS and Hook-interacting protein (FHIP) (Protein FAM160A2) 975 106,541 Alternative sequence (3); Chain (1); Erroneous initiation (1); Modified residue (8); Sequence conflict (6) FUNCTION: Component of the FTS/Hook/FHIP complex (FHF complex). The FHF complex may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting complex (the HOPS complex) (By similarity). {ECO:0000250}. SUBUNIT: Component of the FTS/Hook/FHIP complex (FHF complex), composed of AKTIP/FTS, FAM160A2, and one or more members of the Hook family of proteins HOOK1, HOOK2, and HOOK3. The FHF complex associates with the homotypic vesicular sorting complex (the HOPS complex) (By similarity). {ECO:0000250}. +Q80YR2 F16B2_MOUSE Protein FAM160B2 (Retinoic acid-induced protein 16) 744 82,456 Alternative sequence (2); Chain (1); Erroneous initiation (1); Frameshift (1); Sequence conflict (4) +Q9QXD6 F16P1_MOUSE Fructose-1,6-bisphosphatase 1 (FBPase 1) (EC 3.1.3.11) (D-fructose-1,6-bisphosphate 1-phosphohydrolase 1) (Fructose-1,6-bisphosphatase isozyme 3) (FBPase 3) (Liver FBPase) 338 36,912 Binding site (2); Chain (1); Initiator methionine (1); Metal binding (8); Modified residue (5); Nucleotide binding (3); Region (4); Sequence conflict (9) Carbohydrate biosynthesis; gluconeogenesis. FUNCTION: Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate in the presence of divalent cations, acting as a rate-limiting enzyme in gluconeogenesis. Plays a role in regulating glucose sensing and insulin secretion of pancreatic beta-cells. Appears to modulate glycerol gluconeogenesis in liver. Important regulator of appetite and adiposity; increased expression of the protein in liver after nutrient excess increases circulating satiety hormones and reduces appetite-stimulating neuropeptides and thus seems to provide a feedback mechanism to limit weight gain. {ECO:0000269|PubMed:16497803, ECO:0000269|PubMed:18375435, ECO:0000269|PubMed:20719858}. SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P00636}. TISSUE SPECIFICITY: Detected in pancreatic beta-cell lines MIN6 and beta-TC and in liver (at protein level). Preferentially expressed in liver, with lower levels detected in pancreatic islets and intestine, and very low levels in blood, muscle, brain and spleen. {ECO:0000269|PubMed:11250076, ECO:0000269|PubMed:16497803, ECO:0000269|PubMed:18375435, ECO:0000269|PubMed:20719858}. +Q3U3E2 F117B_MOUSE Protein FAM117B (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 13 protein homolog) 584 61,345 Chain (1); Compositional bias (2); Modified residue (10) +Q6P539 F222B_MOUSE Protein FAM222B 562 59,616 Chain (1); Compositional bias (1); Sequence conflict (1) +Q80YD3 F205C_MOUSE Protein FAM205C 371 41,486 Alternative sequence (1); Chain (1); Coiled coil (1); Compositional bias (1); Modified residue (2); Transmembrane (1) TRANSMEM 7 29 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +C0HKD1 F25A2_MOUSE Protein FAM205A-2 1308 146,156 Chain (1); Transmembrane (1) TRANSMEM 7 27 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. +C0HKD2 F25A3_MOUSE Protein FAM205A-3 1308 146,156 Chain (1); Transmembrane (1) TRANSMEM 7 27 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. +C0HKD3 F25A4_MOUSE Protein FAM205A-4 1308 146,156 Chain (1); Transmembrane (1) TRANSMEM 7 27 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. +Q8C0Z1 F234A_MOUSE Protein FAM234A (Protein ITFG3) 555 60,576 Chain (1); Glycosylation (5); Modified residue (1); Sequence conflict (3); Topological domain (2); Transmembrane (1) TRANSMEM 50 70 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 49 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 71 555 Extracellular. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. +Q3UVG3 F91A1_MOUSE Protein FAM91A1 837 93,464 Chain (1); Erroneous initiation (2); Modified residue (5) FUNCTION: As component of the WDR11 complex acts together with TBC1D23 to facilitate the golgin-mediated capture of vesicles generated using AP-1. {ECO:0000250|UniProtKB:Q658Y4}. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q658Y4}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q658Y4}. Note=Recruitment to the TGN requires the presence of GOLGA1, GOLGA4 and TBC1D23. {ECO:0000250|UniProtKB:Q658Y4}. SUBUNIT: Component of the complex WDR11 composed of C17orf75, FAM91A1 and WDR11; FAM91A1 and WDR11 are required for proper location of the complex (By similarity). Interacts with golgins GOLGA1 and GOLGA4 and with TBC1D23; interaction with golgins may be mediated by TBC1D23 and interaction with TBC1D23 recruits TBC1D23 to AP-1-derived vesicles (PubMed:29084197). {ECO:0000250|UniProtKB:Q658Y4, ECO:0000269|PubMed:29084197}. +O88947 FA10_MOUSE Coagulation factor X (EC 3.4.21.6) (Stuart factor) [Cleaved into: Factor X light chain; Factor X heavy chain; Activated factor Xa heavy chain] 481 54,018 Active site (3); Chain (4); Disulfide bond (12); Domain (4); Glycosylation (2); Modified residue (13); Propeptide (2); Sequence conflict (3); Signal peptide (1) FUNCTION: Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting. PTM: The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium.; PTM: N- and O-glycosylated. {ECO:0000250}.; PTM: The activation peptide is cleaved by factor IXa (in the intrinsic pathway), or by factor VIIa (in the extrinsic pathway). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: The two chains are formed from a single-chain precursor by the excision of two Arg residues and are held together by 1 or more disulfide bonds. Forms a heterodimer with SERPINA5 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Plasma; synthesized in the liver. +Q80YC5 FA12_MOUSE Coagulation factor XII (EC 3.4.21.38) (Hageman factor) (HAF) [Cleaved into: Coagulation factor XIIa heavy chain; Coagulation factor XIIa light chain] 597 65,701 Active site (3); Chain (2); Compositional bias (1); Disulfide bond (20); Domain (6); Erroneous initiation (1); Glycosylation (6); Sequence conflict (3); Signal peptide (1) FUNCTION: Factor XII is a serum glycoprotein that participates in the initiation of blood coagulation, fibrinolysis, and the generation of bradykinin and angiotensin. Prekallikrein is cleaved by factor XII to form kallikrein, which then cleaves factor XII first to alpha-factor XIIa and then trypsin cleaves it to beta-factor XIIa. Alpha-factor XIIa activates factor XI to factor XIa (By similarity). {ECO:0000250}. PTM: O- and N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Interacts with HRG; the interaction, which is enhanced in the presence of zinc ions and inhibited by heparin-binding, inhibits factor XII autoactivation and contact-initiated coagulation. {ECO:0000250}. +Q8CID3 FA20A_MOUSE Pseudokinase FAM20A 541 61,526 Chain (1); Disulfide bond (4); Glycosylation (5); Mutagenesis (1); Signal peptide (1) FUNCTION: Pseudokinase that acts as an allosteric activator of the Golgi serine/threonine protein kinase FAM20C and is involved in biomineralization of teeth. Forms a complex with FAM20C and increases the ability of FAM20C to phosphorylate the proteins that form the 'matrix' that guides the deposition of the enamel minerals. {ECO:0000269|PubMed:25789606}. PTM: N-glycosylated. {ECO:0000269|PubMed:15676076}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15676076}. Golgi apparatus {ECO:0000269|PubMed:22900076}. Endoplasmic reticulum {ECO:0000269|PubMed:22900076}. SUBUNIT: Interacts with FAM20C; probably forming a heterotetramer of 2 subunits of FAM20A and 2 subunits of FAM20C. {ECO:0000269|PubMed:25789606}. TISSUE SPECIFICITY: Observed throughout the tissues of the mandibular incisor, including the secretory and maturation stage ameloblasts, the suprabasal layers of the gingival epithelium and the odontoblasts. Weak expression in the enamel matrix. {ECO:0000269|PubMed:21549343, ECO:0000269|PubMed:22732358}. +E9PV82 FA53A_MOUSE Protein FAM53A (Dorsal neural-tube nuclear protein) 402 43,084 Chain (1); Modified residue (3); Motif (1); Sequence conflict (7) FUNCTION: May play an important role in neural development; the dorsomedial roof of the third ventricle. {ECO:0000250|UniProtKB:Q5ZKN5}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5ZKN5}. Note=Subnuclear distribution. {ECO:0000250|UniProtKB:Q5ZKN5}. +Q5MJS3 FA20C_MOUSE Extracellular serine/threonine protein kinase FAM20C (EC 2.7.11.1) (Dentin matrix protein 4) (DMP-4) (Golgi-enriched fraction casein kinase) (GEF-CK) 579 65,766 Active site (1); Binding site (5); Chain (1); Disulfide bond (4); Erroneous initiation (4); Frameshift (2); Glycosylation (1); Metal binding (2); Mutagenesis (8); Nucleotide binding (1); Propeptide (1); Region (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Golgi serine/threonine protein kinase that phosphorylates secretory pathway proteins within Ser-x-Glu/pSer motifs and plays a key role in biomineralization of bones and teeth (PubMed:22900076, PubMed:22732358, PubMed:25789606). Constitutes the main protein kinase for extracellular proteins, generating the majority of the extracellular phosphoproteome (By similarity). Mainly phosphorylates proteins within the Ser-x-Glu/pSer motif, but also displays a broader substrate specificity (By similarity). Phosphorylates casein as well as a number of proteins involved in biomineralization such as AMELX, AMTN, ENAM and SPP1 (PubMed:25789606). In addition to its role in biomineralization, also plays a role in lipid homeostasis, wound healing and cell migration and adhesion (By similarity). {ECO:0000250|UniProtKB:Q8IXL6, ECO:0000269|PubMed:22732358, ECO:0000269|PubMed:22900076, ECO:0000269|PubMed:25789606}. PTM: N-glycosylation is required for folding. {ECO:0000250|UniProtKB:Q8IXL6}.; PTM: Autophosphorylated. {ECO:0000250|UniProtKB:Q8IXL6}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17369251}. Golgi apparatus {ECO:0000269|PubMed:22900076}. SUBUNIT: Interacts with FAM20A; probably forming a heterotetramer of 2 subunits of FAM20A and 2 subunits of FAM20C. {ECO:0000269|PubMed:25789606}. TISSUE SPECIFICITY: Highly expressed in the tooth. No expression in the dental pulp. At the secretory stage of amelogenesis, it is detected in the matrix of the enamel, in the ameloblasts, and within the cells adjoining the stratum intermedium (a tissue layer analogous to the stellate reticulum seen in the developing molar). Strong expression is observed in maturation stage ameloblasts and throughout the non-cornified layers of the gingival epithelium. Expressed at moderate levels in bone and at low levels in kidney, liver, brain and lung. Very low expression, if any, in spleen and skeletal muscle. {ECO:0000269|PubMed:17369251, ECO:0000269|PubMed:21549343}. +Q8CDS7 FA243_MOUSE Protein FAM243A 251 29,348 Chain (1) +Q5ND56 FA57A_MOUSE Protein FAM57A 257 29,467 Chain (1); Domain (1); Transmembrane (7) TRANSMEM 1 21 Helical. {ECO:0000255}.; TRANSMEM 42 62 Helical. {ECO:0000255}.; TRANSMEM 71 91 Helical. {ECO:0000255}.; TRANSMEM 114 134 Helical. {ECO:0000255}.; TRANSMEM 142 162 Helical. {ECO:0000255}.; TRANSMEM 181 201 Helical. {ECO:0000255}.; TRANSMEM 220 240 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with GGT7 isoform 3 and SLC3A2. {ECO:0000250}. +Q5SWY7 FA83G_MOUSE Protein FAM83G 812 89,830 Chain (1); Compositional bias (2); Frameshift (1); Initiator methionine (1); Modified residue (9); Sequence conflict (3) FUNCTION: May regulate the bone morphogenetic proteins (BMP) pathway. {ECO:0000250|UniProtKB:A6ND36}. PTM: BMP signaling induces the phosphorylation of PAWS1 through BMPR1A at Ser-609, Ser-613 and Ser-615. In response to BMP phosphorylation at Ser-609 is necessary for the activation of SMAD4-independent BMP target genes such as NEDD9 and ASNS. {ECO:0000250|UniProtKB:A6ND36}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:A6ND36}. Nucleus {ECO:0000250|UniProtKB:A6ND36}. Note=Detected predominantly in cytosolic. Upon BMP stimulation, a small portion of PAWS1 is detected in the nucleus. {ECO:0000250|UniProtKB:A6ND36}. SUBUNIT: Found in a macromolecular complex with SMAD1. Interacts with SMAD1 (via MH2 domain); in a SMAD4-independent manner. {ECO:0000250|UniProtKB:A6ND36}. +Q148V8 FA83H_MOUSE Protein FAM83H 1209 131,115 Chain (1); Erroneous initiation (1); Modified residue (31); Region (1); Sequence conflict (1) FUNCTION: May play a major role in the structural organization and calcification of developing enamel. May play a role in keratin cytoskeleton disassembly by recruiting CSNK1A1 to keratin filaments. Thereby, it may regulate epithelial cell migration. {ECO:0000250|UniProtKB:Q6ZRV2}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q6ZRV2}. Note=Colocalizes with keratin filaments. {ECO:0000250|UniProtKB:Q6ZRV2}. SUBUNIT: Interacts with CSNK1A1; recruits CSNK1A1 to keratin filaments. Interacts with KRT18 and probably other keratins. {ECO:0000250|UniProtKB:Q6ZRV2}. TISSUE SPECIFICITY: Expressed in tooth follicle, eye, liver and kidney. {ECO:0000269|PubMed:18252228}. +Q9D650 FA84A_MOUSE Protein FAM84A 292 32,676 Chain (1); Compositional bias (1); Sequence conflict (1) +Q8K2P2 FA83A_MOUSE Protein FAM83A 436 48,193 Alternative sequence (2); Chain (1); Modified residue (4); Sequence conflict (1) FUNCTION: Probable proto-oncogene that functions in the epidermal growth factor receptor/EGFR signaling pathway. Activates both RAS/MAPK and PI3K/AKT/TOR signaling cascades downstream of EGFR. Required for the RAS/MAPK signaling cascade activation upon EGFR stimulation, it also activates both signaling cascades independently of EGFR activation. {ECO:0000250|UniProtKB:Q86UY5}. PTM: Phosphorylated upon EGFR activation. {ECO:0000250|UniProtKB:Q86UY5}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q86UY5}. SUBUNIT: Interacts with the regulatory subunit p85 of PI3-kinase; increased by EGFR activation. Interacts with RAF1; increased by EGFR activation it activates RAF1. {ECO:0000250|UniProtKB:Q86UY5}. +Q3V2J0 FA92B_MOUSE Protein FAM92B 292 33,274 Chain (1); Region (1); Sequence conflict (1) FUNCTION: May play a role in ciliogenesis. In cooperation with CBY1 may facilitate ciliogenesis likely by the recruitment and fusion of endosomal vesicles at distal appendages during early stages of ciliogenesis. {ECO:0000250|UniProtKB:A1XBS5, ECO:0000250|UniProtKB:Q6ZTR7}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:27528616}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:27528616}. Note=Extensive colocalization with CBY1 at mother centrioles (PubMed:27528616). {ECO:0000269|PubMed:27528616}. DOMAIN: The BAR-like domain displays limited similarity to other BAR domains. {ECO:0000250|UniProtKB:A1XBS5}. +P55050 FABPI_MOUSE Fatty acid-binding protein, intestinal (Fatty acid-binding protein 2) (Intestinal-type fatty acid-binding protein) (I-FABP) 132 15,126 Binding site (2); Chain (1); Initiator methionine (1); Modified residue (1) FUNCTION: FABP are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters. FABP2 is probably involved in triglyceride-rich lipoprotein synthesis. Binds saturated long-chain fatty acids with a high affinity, but binds with a lower affinity to unsaturated long-chain fatty acids. FABP2 may also help maintain energy homeostasis by functioning as a lipid sensor. {ECO:0000269|PubMed:11023988}. SUBCELLULAR LOCATION: Cytoplasm. DOMAIN: Forms a beta-barrel structure that accommodates the hydrophobic ligand in its interior. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the small intestine. Highest expression levels in the proximal ileum. {ECO:0000269|PubMed:9277406}. +P57791 FACE2_MOUSE CAAX prenyl protease 2 (EC 3.4.22.-) (Farnesylated proteins-converting enzyme 2) (FACE-2) (Prenyl protein-specific endoprotease 2) (RCE1 homolog) 329 35,867 Active site (2); Chain (1); Initiator methionine (1); Modified residue (1); Sequence conflict (2); Site (2); Transmembrane (7) TRANSMEM 36 56 Helical. {ECO:0000255}.; TRANSMEM 75 95 Helical. {ECO:0000255}.; TRANSMEM 112 132 Helical. {ECO:0000255}.; TRANSMEM 193 213 Helical. {ECO:0000255}.; TRANSMEM 226 246 Helical. {ECO:0000255}.; TRANSMEM 254 274 Helical. {ECO:0000255}.; TRANSMEM 282 302 Helical. {ECO:0000255}. FUNCTION: Proteolytically removes the C-terminal three residues of farnesylated and geranylated proteins. Seems to be able to process K-Ras, N-Ras, H-Ras, RAP1B and G-gamma-1 (By similarity). {ECO:0000250|UniProtKB:Q9Y256, ECO:0000305|PubMed:10085069}. PTM: Ubiquitinated. Undergoes 'Lys-48'-and 'Lys-63'-linked ubiquitination. 'Lys-48' ubiquitination induces its degradation. Deubiquitinated by USP17L2/USP17 that cleaves 'Lys-63'-linked ubiquitin chains (By similarity). {ECO:0000250|UniProtKB:Q9Y256}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9Y256}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9Y256}. +Q922J9 FACR1_MOUSE Fatty acyl-CoA reductase 1 (EC 1.2.1.84) 515 59,435 Alternative sequence (4); Chain (1); Region (1); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 466 483 Helical. {ECO:0000255}. TOPO_DOM 1 465 Cytoplasmic. {ECO:0000250|UniProtKB:Q8WVX9}.; TOPO_DOM 484 515 Peroxisomal. {ECO:0000250|UniProtKB:Q8WVX9}. FUNCTION: Catalyzes the reduction of saturated and unsaturated C16 or C18 fatty acyl-CoA to fatty alcohols (PubMed:15220348, PubMed:15220349). It plays an essential role in the production of ether lipids/plasmalogens which synthesis requires fatty alcohols (By similarity). In parallel, it is also required for wax monoesters production since fatty alcohols also constitute a substrate for their synthesis (PubMed:15220349). {ECO:0000250|UniProtKB:Q8WVX9, ECO:0000269|PubMed:15220348, ECO:0000269|PubMed:15220349}. SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000269|PubMed:15220348}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8WVX9}. SUBUNIT: Interacts with PEX19; PEX19 mediates the targeting of FAR1 to peroxisomes. {ECO:0000250|UniProtKB:Q8WVX9}. TISSUE SPECIFICITY: Widely expressed. Expressed in all tissues examined. Highest expression seen in preputial gland. Expressed in the brain where large quantities of ether lipids are synthesized. {ECO:0000269|PubMed:15220348}. +Q6DYE8 ENPP3_MOUSE Ectonucleotide pyrophosphatase/phosphodiesterase family member 3 (E-NPP 3) (Phosphodiesterase I beta) (PD-Ibeta) (Phosphodiesterase I/nucleotide pyrophosphatase 3) (CD antigen CD203c) [Includes: Alkaline phosphodiesterase I (EC 3.1.4.1); Nucleotide pyrophosphatase (NPPase) (EC 3.6.1.9) (Nucleotide diphosphatase)] 874 98,662 Active site (1); Binding site (3); Chain (1); Disulfide bond (19); Domain (2); Glycosylation (9); Metal binding (12); Motif (1); Region (2); Sequence conflict (3); Topological domain (2); Transmembrane (1) TRANSMEM 12 30 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 11 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 31 874 Extracellular. {ECO:0000255}. FUNCTION: Hydrolase that metabolizes extracellular nucleotides, including ATP, GTP, UTP and CTP (By similarity). Limits mast cell and basophil responses during inflammation and during the chronic phases of allergic responses by eliminating the extracellular ATP that functions as signaling molecule and activates basophils and mast cells and induces the release of inflammatory cytokines (PubMed:25692702). Metabolizes extracellular ATP in the lumen of the small intestine, and thereby prevents ATP-induced apoptosis of intestinal plasmacytoid dendritic cells (PubMed:28225814). Has also alkaline phosphodiesterase activity (By similarity). {ECO:0000250|UniProtKB:O14638, ECO:0000269|PubMed:25692702, ECO:0000269|PubMed:28225814}. PTM: N-glycosylated. N-glycosylation is necessary for normal transport to the cell membrane, but is not the apical targeting signal. {ECO:0000250|UniProtKB:P97675}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25692702}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:O14638}. Apical cell membrane {ECO:0000250|UniProtKB:O14638}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:O14638}. Secreted {ECO:0000250|UniProtKB:O14638}. Note=Detected at the cell surface of basophils (PubMed:25692702). Detected at the apical plasma membrane of bile duct cells. Located to the apical surface in intestinal and kidney epithelial cells. Secreted in serum, and in lumen of epithelial cells (By similarity). {ECO:0000250|UniProtKB:O14638, ECO:0000269|PubMed:25692702}. SUBUNIT: Monomer and homodimer. {ECO:0000250|UniProtKB:O14638}. TISSUE SPECIFICITY: Detected at the tip of villi in the small intestine (PubMed:28225814). Detected on basophils and mast cells (at protein level) (PubMed:25692702). Detected in the epithelial layer of the small intestine; expression is higher in the proximal part and lower in the distal part of the small intestine (PubMed:28225814). {ECO:0000269|PubMed:25692702, ECO:0000269|PubMed:28225814}. +Q9DBT4 ENTP4_MOUSE Ectonucleoside triphosphate diphosphohydrolase 4 (NTPDase 4) (EC 3.6.1.6) (Lysosomal apyrase-like protein of 70 kDa) (Uridine-diphosphatase) (UDPase) 613 69,746 Active site (1); Alternative sequence (1); Chain (1); Disulfide bond (1); Glycosylation (2); Topological domain (3); Transmembrane (2) TRANSMEM 34 54 Helical. {ECO:0000255}.; TRANSMEM 560 580 Helical. {ECO:0000255}. TOPO_DOM 1 33 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 55 559 Lumenal. {ECO:0000255}.; TOPO_DOM 581 613 Cytoplasmic. {ECO:0000255}. FUNCTION: Hydrolyzes preferentially nucleoside 5'-diphosphates, nucleoside 5'-triphosphates are hydrolyzed only to a minor extent. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Localizes in the Golgi and autophagic vacuoles/lysosomes. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10858452}. +Q9CRA5 GOLP3_MOUSE Golgi phosphoprotein 3 (Coat protein GPP34) 298 33,752 Alternative sequence (2); Binding site (4); Chain (1); Compositional bias (2); Disulfide bond (1); Frameshift (1); Modified residue (1); Region (1) FUNCTION: Phosphatidylinositol-4-phosphate-binding protein that links Golgi membranes to the cytoskeleton and may participate in the tensile force required for vesicle budding from the Golgi. Thereby, may play a role in Golgi membrane trafficking and could indirectly give its flattened shape to the Golgi apparatus. May also bind to the coatomer to regulate Golgi membrane trafficking. May play a role in anterograde transport from the Golgi to the plasma membrane and regulate secretion. Has also been involved in the control of the localization of Golgi enzymes through interaction with their cytoplasmic part. May play an indirect role in cell migration. Has also been involved in the modulation of mTOR signaling. May also be involved in the regulation of mitochondrial lipids biosynthesis (By similarity). {ECO:0000250}. PTM: Phosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Isoform 2: Golgi apparatus.; SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:17629635}; Peripheral membrane protein {ECO:0000269|PubMed:17629635}; Cytoplasmic side {ECO:0000269|PubMed:17629635}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:17629635}; Peripheral membrane protein {ECO:0000269|PubMed:17629635}; Cytoplasmic side {ECO:0000269|PubMed:17629635}. Mitochondrion intermembrane space {ECO:0000269|PubMed:17629635}. Cell membrane {ECO:0000250}. Endosome {ECO:0000250}. Note=Phosphatidylinositol 4-phosphate-binding and oligomerization participate in the recruitment onto Golgi membranes. {ECO:0000305}. SUBUNIT: Homodimer. Interacts with the coatomer complex. Interacts with MYO18A; the interaction is direct and may link Golgi membranes to the actin cytoskeleton. Interacts with GCNT1; may control its retention in the Golgi. Interacts with VPS35 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in all tissues tested including brain, heart, kidney, liver, lung, salivary gland, skeletal muscle, small intestine, spleen, stomach, skin and testis (at protein level). {ECO:0000269|PubMed:23345592}. +Q3U507 GP174_MOUSE Probable G-protein coupled receptor 174 335 38,761 Chain (1); Disulfide bond (1); Glycosylation (3); Topological domain (8); Transmembrane (7) TRANSMEM 28 48 Helical; Name=1. {ECO:0000255}.; TRANSMEM 54 74 Helical; Name=2. {ECO:0000255}.; TRANSMEM 92 112 Helical; Name=3. {ECO:0000255}.; TRANSMEM 135 155 Helical; Name=4. {ECO:0000255}.; TRANSMEM 183 203 Helical; Name=5. {ECO:0000255}.; TRANSMEM 232 252 Helical; Name=6. {ECO:0000255}.; TRANSMEM 269 289 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 27 Extracellular. {ECO:0000255}.; TOPO_DOM 49 53 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 75 91 Extracellular. {ECO:0000255}.; TOPO_DOM 113 134 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 156 182 Extracellular. {ECO:0000255}.; TOPO_DOM 204 231 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 253 268 Extracellular. {ECO:0000255}.; TOPO_DOM 290 335 Cytoplasmic. {ECO:0000255}. FUNCTION: Putative receptor for purines coupled to G-proteins. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed in spleen and, at low levels, in brain. {ECO:0000269|PubMed:23178570}. +Q9CZU4 ERAL1_MOUSE GTPase Era, mitochondrial (M-ERA) (Conserved ERA-like GTPase) (CEGA) (ERA-W) (ERA-like protein 1) 437 48,187 Chain (1); Domain (2); Modified residue (1); Nucleotide binding (3); Sequence conflict (2); Transit peptide (1) FUNCTION: Probable GTPase that plays a role in the mitochondrial ribosomal small subunit assembly. Specifically binds the 12S mitochondrial rRNA (12S mt-rRNA) to a 33 nucleotide section delineating the 3' terminal stem-loop region. May act as a chaperone that protects the 12S mt-rRNA on the 28S mitoribosomal subunit during ribosomal small subunit assembly (By similarity). {ECO:0000250|UniProtKB:O75616}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. Mitochondrion inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Localizes on the matrix side on the mitochondrial inner membrane. {ECO:0000250}. +Q60750 EPHA1_MOUSE Ephrin type-A receptor 1 (mEpha1) (EC 2.7.10.1) (Embryonic stem cell kinase) (Tyrosine-protein kinase receptor ESK) 977 108,578 Active site (1); Beta strand (7); Binding site (1); Chain (1); Compositional bias (1); Domain (5); Glycosylation (2); Modified residue (5); Motif (1); Nucleotide binding (1); Sequence conflict (11); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 549 569 Helical. {ECO:0000255}. TOPO_DOM 27 548 Extracellular. {ECO:0000255}.; TOPO_DOM 570 977 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor tyrosine kinase which binds promiscuously membrane-bound ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Binds with a low affinity EFNA3 and EFNA4 and with a high affinity to EFNA1 which most probably constitutes its cognate/functional ligand. Upon activation by EFNA1 induces cell attachment to the extracellular matrix inhibiting cell spreading and motility through regulation of ILK and downstream RHOA and RAC. Plays also a role in angiogenesis and regulates cell proliferation. May play a role in apoptosis. {ECO:0000269|PubMed:18802966}. PTM: Phosphorylated. Autophosphorylation is stimulated by its ligand EFNA1 (By similarity). {ECO:0000250}.; PTM: Ubiquitinated. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Homodimer. Forms a signaling complex with LCK; PTK2B/PYK2 and PI3-kinase upon activation by EFNA1; regulates T-lymphocytes migration. Interacts (via SAM domain) with ILK (via ANK repeats); stimulated by EFNA1 but independent of the kinase activity of EPHA1. Interacts (kinase activity-dependent) with PTK2/FAK1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Preferentially expressed in epithelial cells including skin, kidney, liver and thymus (PubMed:11519828, PubMed:18802966). Expressed in myogenic progenitor cells (PubMed:27446912). {ECO:0000269|PubMed:11519828, ECO:0000269|PubMed:18802966, ECO:0000269|PubMed:27446912}. +Q8C0I4 EPC2_MOUSE Enhancer of polycomb homolog 2 (EPC-like) 808 90,960 Chain (1); Compositional bias (2); Cross-link (4); Erroneous initiation (1); Modified residue (1); Sequence conflict (4) FUNCTION: May play a role in transcription or DNA repair. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +Q64695 EPCR_MOUSE Endothelial protein C receptor (Activated protein C receptor) (APC receptor) (Centrocyclin) (Centrosomal protein CCD41) (Endothelial cell protein C receptor) (CD antigen CD201) 242 27,189 Chain (1); Disulfide bond (2); Glycosylation (5); Sequence conflict (5); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 215 235 Helical. {ECO:0000255}. TOPO_DOM 18 214 Extracellular. {ECO:0000255}.; TOPO_DOM 236 242 Cytoplasmic. {ECO:0000255}. FUNCTION: Binds activated protein C. Enhances protein C activation by the thrombin-thrombomodulin complex; plays a role in the protein C pathway controlling blood coagulation. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. TISSUE SPECIFICITY: Expressed in endothelial cells. +P42567 EPS15_MOUSE Epidermal growth factor receptor substrate 15 (Protein Eps15) (Protein AF-1p) 897 98,471 Alternative sequence (2); Beta strand (2); Calcium binding (2); Chain (1); Domain (7); Helix (6); Initiator methionine (1); Modified residue (17); Mutagenesis (6); Region (2); Repeat (13); Turn (2) FUNCTION: Involved in cell growth regulation. May be involved in the regulation of mitogenic signals and control of cell proliferation. Involved in the internalization of ligand-inducible receptors of the receptor tyrosine kinase (RTK) type, in particular EGFR. Plays a role in the assembly of clathrin-coated pits (CCPs). Acts as a clathrin adapter required for post-Golgi trafficking. Seems to be involved in CCPs maturation including invagination or budding. Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but not TFR seems to require association with DAB2. PTM: Phosphorylated on serine upon DNA damage, probably by ATM or ATR (By similarity). Phosphorylation on Tyr-850 is involved in the internalization of EGFR. Not required for membrane translocation after EGF treatment or for targeting to coated pits, but essential for a subsequent step in EGFR endocytosis. {ECO:0000250, ECO:0000269|PubMed:10953014}.; PTM: Ubiquitinated. {ECO:0000269|PubMed:16159959}. SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Membrane, clathrin-coated pit. Note=Recruited to the plasma membrane upon EGFR activation and localizes to coated pits. Colocalizes with UBQLN1 in ubiquitin-rich cytoplasmic aggregates that are not endocytic compartments and in cytoplasmic juxtanuclear structures called aggresomes. {ECO:0000250|UniProtKB:P42566}.; SUBCELLULAR LOCATION: Isoform 2: Early endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Colocalizes with HGS on bilayered clathrin coats on endosomes. {ECO:0000250}. SUBUNIT: Interacts with HGS; the interaction bridges the interaction of STAM or STAM2 with EPS15. Isoform 2 interacts with HGS and AP2A2. Part of a complex at least composed of EPS15, HGS, and either STAM or STAM2. Binds AP2A2. Interacts with AP2B1; clathrin competes with EPS15. Binds STON2 and EPN1. Interacts (via its SH3-binding sites) with CRK. Interacts with SH3BP4/TTP. Interacts with ERBB2. Interacts (via UIM repeats) with CORO7 (when ubiquitinated at 'Lys-472') (By similarity). Interacts with FCHO1 (By similarity). Interacts with FCHO2. Interacts with SGIP1. Interacts (via EH domains) with DAB2. Interacts (via UIM domains) with UBQLN1 (via ubiquitin-like domain) and can interact with both the ubiquitinated and the non-ubiquitinated forms of UBQLN1. Interacts with UBQLN2 (By similarity). {ECO:0000250|UniProtKB:P42566, ECO:0000269|PubMed:12057195, ECO:0000269|PubMed:16159959, ECO:0000269|PubMed:17626015, ECO:0000269|PubMed:20448150, ECO:0000269|PubMed:21762413, ECO:0000269|PubMed:22648170}. DOMAIN: The EH domain interacts with Asn-Pro-Phe (NPF) motifs of target proteins. {ECO:0000250}.; DOMAIN: The UIM (ubiquitin-interacting motif) repeats specifically bind 'Lys-33'-linked ubiquitin. {ECO:0000250}. +Q08509 EPS8_MOUSE Epidermal growth factor receptor kinase substrate 8 821 91,737 Beta strand (5); Chain (1); Compositional bias (5); Domain (3); Helix (2); Modified residue (11); Mutagenesis (8); Region (6); Sequence conflict (2) FUNCTION: Signaling adapter that controls various cellular protrusions by regulating actin cytoskeleton dynamics and architecture. Depending on its association with other signal transducers, can regulate different processes. Together with SOS1 and ABI1, forms a trimeric complex that participates in transduction of signals from Ras to Rac by activating the Rac-specific guanine nucleotide exchange factor (GEF) activity. Acts as a direct regulator of actin dynamics by binding actin filaments and has both barbed-end actin filament capping and actin bundling activities depending on the context. Displays barbed-end actin capping activity when associated with ABI1, thereby regulating actin-based motility process: capping activity is auto-inhibited and inhibition is relieved upon ABI1 interaction. Also shows actin bundling activity when associated with BAIAP2, enhancing BAIAP2-dependent membrane extensions and promoting filopodial protrusions. Involved in the regulation of processes such as axonal filopodia growth, stereocilia length, dendritic cell migration and cancer cell migration and invasion. Acts as a regulator of axonal filopodia formation in neurons: in the absence of neurotrophic factors, negatively regulates axonal filopodia formation via actin-capping activity. In contrast, it is phosphorylated in the presence of BDNF leading to inhibition of its actin-capping activity and stimulation of filopodia formation. Component of a complex with WHRN and MYO15A that localizes at stereocilia tips and is required for elongation of the stereocilia actin core. Indirectly involved in cell cycle progression; its degradation following ubiquitination being required during G2 phase to promote cell shape changes. {ECO:0000269|PubMed:10499589, ECO:0000269|PubMed:11524436, ECO:0000269|PubMed:15558031, ECO:0000269|PubMed:17115031, ECO:0000269|PubMed:19564905, ECO:0000269|PubMed:20532239, ECO:0000269|PubMed:21236676, ECO:0000269|PubMed:21835647, ECO:0000269|PubMed:8404850}. PTM: Ubiquitinated by the SCF(FBXW5) E3 ubiquitin-protein ligase complex during G2 phase, leading to its transient degradation and subsequent cell shape changes required to allow mitotic progression. Reappears at the midzone of dividing cells. {ECO:0000269|PubMed:23314863}.; PTM: Phosphorylation at Ser-624 and Thr-628 by MAPK following BDNF treatment promotes removal from actin and filopodia formation. Phosphorylated by several receptor tyrosine kinases. {ECO:0000269|PubMed:19564905, ECO:0000269|PubMed:8404850}. SUBCELLULAR LOCATION: Cytoplasm, cell cortex. Cell projection, ruffle membrane. Cell projection, growth cone {ECO:0000250}. Cell projection, stereocilium {ECO:0000269|PubMed:23918390, ECO:0000269|PubMed:24741995}. Cell junction, synapse, synaptosome {ECO:0000250}. Note=Localizes at the tips of the stereocilia of the inner and outer hair cells (PubMed:24741995, PubMed:23918390). Localizes to the midzone of dividing cells. {ECO:0000269|PubMed:23918390, ECO:0000269|PubMed:24741995}. SUBUNIT: Homodimer. Part of a complex consisting of ABI1, EPS8 and SOS1. Interacts with BAIAP2. Interacts with SHB and LANCL1. Interacts with EGFR; mediates EPS8 phosphorylation. Interacts with MYO15A and WHRN. {ECO:0000269|PubMed:10499589, ECO:0000269|PubMed:11524436, ECO:0000269|PubMed:15558031, ECO:0000269|PubMed:17115031, ECO:0000269|PubMed:19528316, ECO:0000269|PubMed:21236676, ECO:0000269|PubMed:7537362, ECO:0000269|PubMed:8404850}. DOMAIN: The effector region is required for activating the Rac-specific guanine nucleotide exchange factor (GEF) activity (PubMed:11524436). It mediates both barbed-end actin capping and actin bundling activities (PubMed:20532239). The capping activity is mediated by an amphipathic helix that binds within the hydrophobic pocket at the barbed ends of actin blocking further addition of actin monomers, while the bundling activity is mediated by a compact 4 helix bundle, which contacts 3 actin subunits along the filament (PubMed:20532239). {ECO:0000269|PubMed:11524436, ECO:0000269|PubMed:20532239}.; DOMAIN: The SH3 domain mediates interaction with SHB. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in neuronal cell body and neurites, and prominently enriched in the axonal growth cone (PubMed:19564905). Expressed at the tips of cochlear hair cells stereocilia (PubMed:23918390). {ECO:0000269|PubMed:19564905, ECO:0000269|PubMed:23918390}. +B9EK06 EXC1L_MOUSE Exocyst complex component 1-like 172 20,158 Chain (1) +A6H5Z3 EXC6B_MOUSE Exocyst complex component 6B (Exocyst complex component Sec15B) (SEC15-like protein 2) 810 94,130 Alternative sequence (2); Chain (1); Coiled coil (1) FUNCTION: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. {ECO:0000250}. SUBUNIT: The exocyst complex is composed of SEC3, SEC5, SEC6, SEC8, SEC10, SEC15, EXO70 and EXO84. {ECO:0000250}. +Q8CDF7 EXD1_MOUSE piRNA biogenesis protein EXD1 (Exonuclease 3'-5' domain-containing protein 1) (Exonuclease 3'-5' domain-like-containing protein 1) (Inactive exonuclease EXD1) (mExd1) 570 63,962 Chain (1); Compositional bias (1); Domain (1) FUNCTION: RNA-binding component of the PET complex, a multiprotein complex required for the processing of piRNAs during spermatogenesis. The piRNA metabolic process mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposable elements, preventing their mobilization, which is essential for the germline integrity (PubMed:26669262). The PET complex is required during the secondary piRNAs metabolic process for the PIWIL2 slicing-triggered loading of PIWIL4 piRNAs. In the PET complex, EXD1 probably acts as an RNA adapter. EXD1 is an inactive exonuclease (By similarity). {ECO:0000250|UniProtKB:H9IUR0, ECO:0000269|PubMed:26669262}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:H9IUR0}. Note=Component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis. {ECO:0000250|UniProtKB:H9IUR0}. SUBUNIT: Homodimer (By similarity). Component of the PET complex, at least composed of EXD1, PIWIL2, TDRD12 and piRNAs. {ECO:0000250|UniProtKB:H9IUR0, ECO:0000269|PubMed:26669262}. DOMAIN: The 3'-5' exonuclease domain lacks the conserved Asp-Glu-Asp-Asp (DEDD) residues that coordinates divalent ions essential for exonuclease activity. {ECO:0000305|PubMed:19468303}. +Q8R3S6 EXOC1_MOUSE Exocyst complex component 1 (Exocyst complex component Sec3) 894 101,889 Chain (1); Coiled coil (2); Modified residue (5); Sequence conflict (2) FUNCTION: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. {ECO:0000250}. SUBCELLULAR LOCATION: Midbody, Midbody ring {ECO:0000250|UniProtKB:Q9NV70}. Note=Colocalizes with CNTRL/centriolin at the midbody ring. {ECO:0000250|UniProtKB:Q9NV70}. SUBUNIT: The exocyst complex is composed of EXOC1, EXOC2, EXOC3, EXOC4, EXOC5, EXOC6, EXOC7 and EXOC8. {ECO:0000250}. +Q9DAA6 EXOS1_MOUSE Exosome complex component CSL4 (Exosome component 1) 195 21,424 Alternative sequence (1); Chain (1); Domain (1); Modified residue (1) FUNCTION: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. EXOSC1 as peripheral part of the Exo-9 complex stabilizes the hexameric ring of RNase PH-domain subunits through contacts with EXOSC6 and EXOSC8 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus. Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. SUBUNIT: Component of the RNA exosome complex. Specifically part of the catalytically inactive RNA exosome core (Exo-9) complex which is believed to associate with catalytic subunits EXOSC10, and DIS3 or DIS3L in cytoplasmic- and nuclear-specific RNA exosome complex forms. Exo-9 is formed by a hexameric ring of RNase PH domain-containing subunits specifically containing the heterodimers EXOSC4-EXOSC9, EXOSC5-EXOSC8 and EXOSC6-EXOSC7, and peripheral S1 domain-containing components EXOSC1, EXOSC2 and EXOSC3 located on the top of the ring structure. Interacts with EXOSC5, EXOSC7 and EXOSC10 (By similarity). Interacts with DDX60 (By similarity). {ECO:0000250}. +Q8VBV3 EXOS2_MOUSE Exosome complex component RRP4 (Exosome component 2) (Ribosomal RNA-processing protein 4) 293 32,632 Chain (1); Domain (1); Modified residue (1) FUNCTION: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. EXOSC2 as peripheral part of the Exo-9 complex stabilizes the hexameric ring of RNase PH-domain subunits through contacts with EXOSC4 and EXOSC7 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Component of the RNA exosome complex. Specifically part of the catalytically inactive RNA exosome core (Exo-9) complex which is believed to associate with catalytic subunits EXOSC10, and DIS3 or DIS3L in cytoplasmic- and nuclear-specific RNA exosome complex forms. Exo-9 is formed by a hexameric ring of RNase PH domain-containing subunits specifically containing the heterodimers EXOSC4-EXOSC9, EXOSC5-EXOSC8 and EXOSC6-EXOSC7, and peripheral S1 domain-containing components EXOSC1, EXOSC2 and EXOSC3 located on the top of the ring structure. Interacts with DIS3. Interacts with GTPBP1. Interacts with ZFP36L1 (via N-terminus). {ECO:0000250|UniProtKB:Q13868}. +Q7TQK4 EXOS3_MOUSE Exosome complex component RRP40 (EC 3.1.13.-) (Exosome component 3) (Ribosomal RNA-processing protein 40) 274 29,546 Chain (1); Cross-link (1); Initiator methionine (1); Modified residue (1); Sequence conflict (1) FUNCTION: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. EXOSC3 as peripheral part of the Exo-9 complex stabilizes the hexameric ring of RNase PH-domain subunits through contacts with EXOSC9 and EXOSC5 (By similarity). {ECO:0000250, ECO:0000269|PubMed:21255825}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Component of the RNA exosome complex. Specifically part of the catalytically inactive RNA exosome core (Exo-9) complex which is believed to associate with catalytic subunits EXOSC10, and DIS3 or DIS3L in cytoplasmic- and nuclear-specific RNA exosome complex forms. Exo-9 is formed by a hexameric ring of RNase PH domain-containing subunits specifically containing the heterodimers EXOSC4-EXOSC9, EXOSC5-EXOSC8 and EXOSC6-EXOSC7, and peripheral S1 domain-containing components EXOSC1, EXOSC2 and EXOSC3 located on the top of the ring structure. Interacts with GTPBP1 (By similarity). Interacts with ZC3HAV1 (By similarity). Interacts with DDX17 only in the presence of ZC3HAV1 in an RNA-independent manner (By similarity). Interacts with DHX36; this interaction occurs in a RNase-insensitive manner (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9NQT5}. +Q921I9 EXOS4_MOUSE Exosome complex component RRP41 (Exosome component 4) (Ribosomal RNA-processing protein 41) 245 26,250 Chain (1); Initiator methionine (1); Modified residue (1) FUNCTION: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. EXOSC4 binds to ARE-containing RNAs (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Component of the RNA exosome complex. Specifically part of the catalytically inactive RNA exosome core (Exo-9) complex which is believed to associate with catalytic subunits EXOSC10, and DIS3 or DIS3L in cytoplasmic- and nuclear-specific RNA exosome complex forms. Exo-9 is formed by a hexameric ring of RNase PH domain-containing subunits specifically containing the heterodimers EXOSC4-EXOSC9, EXOSC5-EXOSC8 and EXOSC6-EXOSC7, and peripheral S1 domain-containing components EXOSC1, EXOSC2 and EXOSC3 located on the top of the ring structure (By similarity). Interacts with DDX60 (By similarity). {ECO:0000250}. +P56960 EXOSX_MOUSE Exosome component 10 (EC 3.1.13.-) (Autoantigen PM/Scl 2 homolog) (Polymyositis/scleroderma autoantigen 2 homolog) 887 100,942 Chain (1); Cross-link (7); Domain (1); Modified residue (1); Sequence conflict (3) FUNCTION: Putative catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. EXOSC10 has 3'-5' exonuclease activity (By similarity). EXOSC10 is required for nucleolar localization of C1D and probably mediates the association of MTREX, C1D and MPP6 wth the RNA exosome involved in the maturation of 5.8S rRNA (By similarity). {ECO:0000250|UniProtKB:Q01780}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q01780}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q01780}. Nucleus {ECO:0000250|UniProtKB:Q01780}. SUBUNIT: Component of the RNA exosome complex. The catalytically inactive RNA exosome core (Exo-9) complex is believed to associate with catalytic subunits EXOSC10, and DIS3 or DIS3L in cytoplasmic- and nuclear-specific RNA exosome complex forms. Interacts with C1D and MPHOSPH6 (By similarity). Interacts with ALYREF/THOC4 (By similarity). Interacts with MTREX; the interaction mediates the association of MTREX with nuclear RNA exosomes (By similarity). Interacts with DHX36; this interaction occurs in a RNase-insensitive manner (By similarity). {ECO:0000250|UniProtKB:Q01780}. +O08575 EYA2_MOUSE Eyes absent homolog 2 (EC 3.1.3.48) 532 58,246 Active site (2); Alternative sequence (1); Chain (1); Metal binding (3) FUNCTION: Functions both as protein phosphatase and as transcriptional coactivator for SIX1, and probably also for SIX2, SIX4 and SIX5 (PubMed:10490620, PubMed:17098221). Tyrosine phosphatase that dephosphorylates 'Tyr-142' of histone H2AX (H2AXY142ph) and promotes efficient DNA repair via the recruitment of DNA repair complexes containing MDC1. 'Tyr-142' phosphorylation of histone H2AX plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress. Its function as histone phosphatase may contribute to its function in transcription regulation during organogenesis (By similarity). Plays an important role in hypaxial muscle development together with SIX1 and DACH2; in this it is functionally redundant with EYA1 (By similarity). {ECO:0000250|UniProtKB:O00167, ECO:0000269|PubMed:10490620, ECO:0000269|PubMed:17098221}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10490620}. Nucleus {ECO:0000269|PubMed:10490620}. Note=Retained in the cytoplasm via interaction with GNAZ and GNAI2 (By similarity). Interaction with SIX1, SIX2, SIX4 or SIX5 is required for translocation to the nucleus. {ECO:0000250|UniProtKB:O00167}. SUBUNIT: Probably interacts with SIX2, SIX4 and SIX5. Interacts with DACH2. Interacts with GNAZ and GNAI2; this retains EYA2 in the cytoplasm and prevents its translocation into the nucleus and transcriptional activity (By similarity). Interacts with SIX1. Interacts with CAPN8. {ECO:0000250, ECO:0000269|PubMed:10490620, ECO:0000269|PubMed:11978764, ECO:0000269|PubMed:16476741}. TISSUE SPECIFICITY: Extensively expressed in cranial placodes, branchial arches, CNS and developing eye and nose. Low expression in lung with little or no expression in skin, liver, intestine and kidney. Predominantly expressed in the upper one-third of the oxyntic mucosa and in most regions of the pyloric mucosa. {ECO:0000269|PubMed:16476741}. +P97480 EYA3_MOUSE Eyes absent homolog 3 (EC 3.1.3.48) 510 55,973 Active site (2); Alternative sequence (1); Chain (1); Metal binding (3); Modified residue (4); Mutagenesis (10); Sequence conflict (2) FUNCTION: Tyrosine phosphatase that specifically dephosphorylates 'Tyr-142' of histone H2AX (H2AXY142ph). 'Tyr-142' phosphorylation of histone H2AX plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress. Promotes efficient DNA repair by dephosphorylating H2AX, promoting the recruitment of DNA repair complexes containing MDC1 (By similarity). Its function as histone phosphatase probably explains its role in transcription regulation during organogenesis. The phosphatase activity has been shown in vitro. Coactivates SIX1. Seems to coactivate SIX2, SIX4 and SIX5. The repression of precursor cell proliferation in myoblasts by SIX1 is switched to activation through recruitment of EYA3 to the SIX1-DACH1 complex and seems to be dependent on EYA3 phosphatase activity. May be involved in development of the eye. May play a role in mediating the induction and differentiation of cranial placodes. {ECO:0000250|UniProtKB:Q99504, ECO:0000269|PubMed:10490620}. PTM: Ser-203 phosphorylation is required for localization at sites of DNA damage and directing interaction with H2AX. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10490620}. Nucleus {ECO:0000269|PubMed:10490620, ECO:0000269|PubMed:14628052}. Note=Localizes at sites of DNA damage at double-strand breaks (DSBs). {ECO:0000250|UniProtKB:Q99504}. SUBUNIT: Interacts with SIX1 and DACH1, and probably SIX2, SIX4 and SIX5. {ECO:0000269|PubMed:10490620, ECO:0000269|PubMed:12215533, ECO:0000269|PubMed:14628042}. TISSUE SPECIFICITY: Expressed in branchial arches, CNS and developing eye. +Q78T81 F102A_MOUSE Protein FAM102A 392 42,830 Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (1) FUNCTION: May play a role in estrogen action. {ECO:0000250}. +Q9D2L9 F111A_MOUSE Protein FAM111A 613 69,949 Chain (1); Cross-link (3); Frameshift (1); Modified residue (1); Sequence conflict (35) FUNCTION: Chromatin-associated protein required for PCNA loading on replication sites. Promotes S-phase entry and DNA synthesis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Mainly localizes to nucleus: colocalizes with PCNA on replication sites. {ECO:0000250}. SUBUNIT: Interacts with PCNA; then interaction is direct. {ECO:0000250}. DOMAIN: The PIP-box mediates the interaction with PCNA. {ECO:0000250}. +Q91YN1 F118A_MOUSE Protein FAM118A 357 40,475 Alternative sequence (2); Chain (1); Modified residue (2); Sequence conflict (1); Transmembrane (1) TRANSMEM 30 46 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q8BR21 F180A_MOUSE Protein FAM180A 173 19,449 Chain (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q5NC57 F183B_MOUSE Protein FAM183B 135 16,125 Alternative sequence (1); Chain (1); Erroneous initiation (4); Sequence conflict (1) SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:27914912}. TISSUE SPECIFICITY: Predominantly expressed in tissues containing motile cilia. {ECO:0000269|PubMed:27914912}. +Q3U2K0 F193B_MOUSE Protein FAM193B 892 95,084 Alternative sequence (2); Chain (1); Coiled coil (1); Compositional bias (3); Erroneous initiation (1); Erroneous termination (1); Modified residue (3) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Partly colocalized with an endoplasmic reticulum marker, HSP90B1. Shuttles between nucleus and cytoplasm (By similarity). {ECO:0000250}. +Q8K2D0 F199X_MOUSE Protein FAM199X 388 42,839 Chain (1); Compositional bias (1); Modified residue (2); Sequence conflict (1) +Q3ZN08 F220A_MOUSE Protein FAM220A (Acrosomal protein ACPIN1) (STAT3-interacting protein as a repressor) 260 27,752 Chain (1); Sequence caution (1); Sequence conflict (3) FUNCTION: May negatively regulate STAT3. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|Ref.1}. SUBUNIT: Interacts with STAT3. {ECO:0000269|Ref.1}. +P58468 F207A_MOUSE Protein FAM207A 219 24,814 Chain (1); Modified residue (2) +Q8C790 F221A_MOUSE Protein FAM221A 301 33,346 Alternative sequence (2); Chain (1) +Q9D882 F241B_MOUSE Uncharacterized protein FAM241B 120 13,118 Chain (1); Modified residue (1); Transmembrane (1) TRANSMEM 91 111 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000255}. +Q8BR27 F214B_MOUSE Protein FAM214B 538 57,075 Chain (1); Erroneous gene model prediction (1); Modified residue (2); Sequence conflict (5) +Q9DB54 F216A_MOUSE Protein FAM216A 251 28,339 Chain (1); Sequence conflict (1) +Q8CF36 F229B_MOUSE Protein FAM229B 80 8,765 Chain (1) +Q9D9W6 F217A_MOUSE Protein FAM217A 419 46,769 Chain (1); Compositional bias (1) +Q00558 F8I2_MOUSE Factor VIII intron 22 protein (CpG island protein) 380 40,490 Chain (1); Initiator methionine (1); Modified residue (1) FUNCTION: Not known. Possible housekeeping role. SUBUNIT: Interacts with HTT. {ECO:0000250|UniProtKB:P23610}. TISSUE SPECIFICITY: Produced abundantly in a wide variety of cell types. +Q9CR80 FA32A_MOUSE Protein FAM32A (Ovarian tumor associated gene 12) (OTAG-12) 112 13,215 Chain (1); Compositional bias (1); Sequence conflict (2) FUNCTION: May induce G2 arrest and apoptosis (By similarity). May also increase cell sensitivity to apoptotic stimuli (By similarity). In cell lines, may play a role in the inhibition of anchor-independent cell growth. {ECO:0000250, ECO:0000269|PubMed:21339736}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed, with highest level in pancreas and lowest in muscle. {ECO:0000269|PubMed:21339736}. +Q8BUP8 FA43A_MOUSE Protein FAM43A 424 46,206 Chain (1) +Q9D8N2 FA45A_MOUSE Protein FAM45A 357 40,421 Chain (1); Domain (3); Sequence conflict (3) +Q8K2H3 FA13B_MOUSE Protein FAM13B 851 97,054 Chain (1); Compositional bias (1); Domain (1) +Q9DBR2 FA13C_MOUSE Protein FAM13C 601 66,981 Chain (1); Modified residue (4); Sequence conflict (1) +Q8BGR5 FA53B_MOUSE Protein FAM53B 422 45,939 Alternative sequence (1); Chain (1); Modified residue (8); Motif (1); Sequence conflict (1) FUNCTION: Acts as a regulator of Wnt signaling pathway by regulating beta-catenin (CTNNB1) nuclear localization. {ECO:0000250|UniProtKB:Q14153}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q14153}. SUBUNIT: Interacts with CTNNB1. {ECO:0000250|UniProtKB:Q14153}. +Q8BXQ8 FA53C_MOUSE Protein FAM53C 393 43,261 Chain (1); Modified residue (8) +Q9DAL9 FA24L_MOUSE Protein FAM24A-like 119 12,740 Chain (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q5MPP0 FA2H_MOUSE Fatty acid 2-hydroxylase (EC 1.14.18.-) (Fatty acid alpha-hydroxylase) 372 42,981 Alternative sequence (2); Chain (1); Domain (2); Erroneous initiation (1); Frameshift (1); Metal binding (12); Natural variant (3); Transmembrane (4) TRANSMEM 168 188 Helical. {ECO:0000255}.; TRANSMEM 213 233 Helical. {ECO:0000255}.; TRANSMEM 268 288 Helical. {ECO:0000255}.; TRANSMEM 290 310 Helical. {ECO:0000255}. Sphingolipid metabolism; galactosylceramide biosynthesis. Lipid metabolism; fatty acid metabolism. FUNCTION: Catalyzes stereospecific hydroxylation of free fatty acids at the C-2 position to produce (R)-2-hydroxy fatty acids, which are building blocks of sphingolipids and glycosphingolipids common in neural tissue and epidermis (PubMed:15658937, PubMed:16998236). Plays an essential role in the synthesis of galactosphingolipids of the myelin sheath (PubMed:15658937, PubMed:18815260). Responsible for the synthesis of sphingolipids and glycosphingolipids involved in the formation of epidermal lamellar bodies, critical for skin permeability barrier (By similarity). Participates in the synthesis of glycosphingolipids and a fraction of type II wax diesters in sebaceous gland, specifically regulating hair follicle homeostasis (PubMed:21628453). Involved in the synthesis of sphingolipids of plasma membrane rafts, controlling lipid raft mobility and trafficking of raft-associated proteins (PubMed:22517924). {ECO:0000250|UniProtKB:Q7L5A8, ECO:0000269|PubMed:15658937, ECO:0000269|PubMed:16998236, ECO:0000269|PubMed:18815260, ECO:0000269|PubMed:21628453, ECO:0000269|PubMed:22517924}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15658937}; Multi-pass membrane protein {ECO:0000269|PubMed:15658937}. Microsome membrane {ECO:0000269|PubMed:15658937}; Multi-pass membrane protein {ECO:0000269|PubMed:15658937}. DOMAIN: The histidine box domains may contain the active site and/or be involved in metal ion binding.; DOMAIN: The N-terminal cytochrome b5 heme-binding domain is essential for catalytic activity. {ECO:0000250|UniProtKB:Q7L5A8}. TISSUE SPECIFICITY: Expressed in brain (at protein level) (PubMed:16998236). Detected in cerebellum and forebrain (PubMed:18815260, PubMed:15658937). Expression in the white matter is mainly restricted in oligodendrocytes (PubMed:15658937). Expressed in stomach, kidney, skin and testis (PubMed:15658937). Expressed in sebaceous gland (PubMed:21628453). {ECO:0000269|PubMed:15658937, ECO:0000269|PubMed:16998236, ECO:0000269|PubMed:18815260, ECO:0000269|PubMed:21628453}. +Q5STT6 FA71B_MOUSE Protein FAM71B 665 68,885 Chain (1); Compositional bias (1); Modified residue (1); Motif (1) FUNCTION: May be involved in RNA biogenesis. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Note=Cajal body and speckle localization. {ECO:0000250}. SUBUNIT: Interacts with FRG1. {ECO:0000250}. +Q8BFZ8 FA72A_MOUSE Protein FAM72A 149 16,626 Chain (1); Sequence conflict (1) FUNCTION: May play a role in the regulation of cellular reactive oxygen species metabolism. May participate in cell growth regulation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Mitochondrion {ECO:0000250}. SUBUNIT: Interacts with UNG. {ECO:0000250}. TISSUE SPECIFICITY: Expressed at high levels in stomach and also in kidney and, at low levels, in heart (at protein level). In the stomach, highly expressed in foveolar cells, parietal cells and chief cells (at protein level). In kidney, expressed in endothelial cells, mesangial and epithelial cells (parietal and visceral epithelium) around glomerulus (at protein level). {ECO:0000269|PubMed:21317926}. +Q922G2 FA76A_MOUSE Protein FAM76A 307 35,095 Alternative sequence (1); Chain (1); Coiled coil (1); Compositional bias (1); Sequence conflict (1) +Q9D7I8 FA83D_MOUSE Protein FAM83D 585 64,324 Alternative sequence (2); Chain (1); Compositional bias (1); Modified residue (3); Region (1); Sequence conflict (1) FUNCTION: Probable proto-oncogene that regulates cell proliferation, growth, migration and epithelial to mesenchymal transition. Through the degradation of FBXW7, may act indirectly on the expression and downstream signaling of MTOR, JUN and MYC. May play also a role in cell proliferation through activation of the ERK1/ERK2 signaling cascade. May also be important for proper chromosome congression and alignment during mitosis through its interaction with KIF22. {ECO:0000250|UniProtKB:Q9H4H8}. PTM: Phosphorylated during mitosis. {ECO:0000250|UniProtKB:Q9H4H8}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H4H8}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9H4H8}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q9H4H8}. Note=Primarily cytoplasmic during interphase, but at prophase, associates with spindle microtubules, with a clear concentration toward the spindle poles. It persists on spindle microtubules through metaphase and anaphase. {ECO:0000250|UniProtKB:Q9H4H8}. SUBUNIT: Interacts with FBXW7; promotes FBXW7 degradation. May interact with RAF1. Interacts with KIF22; recruits KIF22 to mitotic spindle microtubules. {ECO:0000250|UniProtKB:Q9H4H8}. +Q80XS7 FA83E_MOUSE Protein FAM83E 481 52,578 Chain (1); Sequence caution (2) FUNCTION: May play a role in MAPK signaling. {ECO:0000250|UniProtKB:Q2M2I3}. SUBUNIT: May interact with RAF1. {ECO:0000250|UniProtKB:Q2M2I3}. +Q8C552 FA78A_MOUSE Protein FAM78A 283 32,068 Chain (1) +Q8BQN5 FA78B_MOUSE Protein FAM78B 261 29,835 Chain (1); Erroneous initiation (3) +Q14BJ1 FA89A_MOUSE Protein FAM89A 175 18,690 Alternative sequence (1); Chain (1) +Q8BP22 FA92A_MOUSE Protein FAM92A 355 39,959 Chain (1); Coiled coil (1); Erroneous gene model prediction (1); Erroneous initiation (2); Frameshift (1); Region (1); Sequence conflict (3) FUNCTION: Seems to play a role in ciliogenesis. In cooperation with CBY1 may facilitate ciliogenesis likely by the recruitment and fusion of endosomal vesicles at distal appendages during early stages of ciliogenesis. {ECO:0000250|UniProtKB:A1XBS5}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A1XBS5}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:A1XBS5}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:27528616}. Note=Weak punctate vesicular distribution throughout the cytoplasm. Localizes at the distal end of mother centrioles. Extensive colocalization with CBY1 at mother centrioles (PubMed:27528616). {ECO:0000250|UniProtKB:A1XBS5, ECO:0000269|PubMed:27528616}. SUBUNIT: Homodimer (via BAR-like domain). Heterodimer with FAM92B (via BAR-like domains). Interacts (via BAR-like domain) with CBY1; this interaction is required for targeting FAM92A to centriole. {ECO:0000250|UniProtKB:A1XBS5}. DOMAIN: The BAR-like domain displays limited similarity to other BAR domains. {ECO:0000250|UniProtKB:A1XBS5}. +P35505 FAAA_MOUSE Fumarylacetoacetase (FAA) (EC 3.7.1.2) (Beta-diketonase) (Fumarylacetoacetate hydrolase) 419 46,176 Active site (1); Beta strand (23); Binding site (5); Chain (1); Helix (19); Initiator methionine (1); Metal binding (7); Modified residue (5); Mutagenesis (1); Sequence conflict (4); Turn (7) Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 6/6. SUBUNIT: Homodimer. {ECO:0000269|PubMed:10508789, ECO:0000269|PubMed:11154690}. TISSUE SPECIFICITY: Mainly in liver and kidney. +Q8R3F5 FABD_MOUSE Malonyl-CoA-acyl carrier protein transacylase, mitochondrial (MCT) (EC 2.3.1.39) (Mitochondrial malonyltransferase) ([Acyl-carrier-protein] malonyltransferase) 381 41,928 Active site (2); Chain (1); Erroneous initiation (1); Modified residue (1); Transit peptide (1) Lipid metabolism; fatty acid biosynthesis. FUNCTION: Catalyzes the transfer of a malonyl moiety from malonyl-CoA to the free thiol group of the phosphopantetheine arm of the mitochondrial ACP protein (NDUFAB1). This suggests the existence of the biosynthesis of fatty acids in mitochondria (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. +P04117 FABP4_MOUSE Fatty acid-binding protein, adipocyte (3T3-L1 lipid-binding protein) (Adipocyte lipid-binding protein) (ALBP) (Adipocyte-type fatty acid-binding protein) (A-FABP) (AFABP) (Fatty acid-binding protein 4) (Myelin P2 protein homolog) (P15) (P2 adipocyte protein) (Protein 422) 132 14,650 Beta strand (11); Chain (1); Helix (3); Initiator methionine (1); Modified residue (3); Motif (1); Mutagenesis (7); Region (1); Sequence conflict (2) FUNCTION: Lipid transport protein in adipocytes. Binds both long chain fatty acids and retinoic acid. Delivers long-chain fatty acids and retinoic acid to their cognate receptors in the nucleus. {ECO:0000269|PubMed:12077340, ECO:0000269|PubMed:16574478, ECO:0000269|PubMed:17516629}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17516629, ECO:0000269|PubMed:17761196}. Nucleus {ECO:0000269|PubMed:17516629, ECO:0000269|PubMed:17761196}. Note=Depending on the nature of the ligand, a conformation change exposes a nuclear localization motif and the protein is transported into the nucleus (PubMed:17516629). Subject to constitutive nuclear export (PubMed:17516629, PubMed:17761196). {ECO:0000269|PubMed:17516629, ECO:0000269|PubMed:17761196}. SUBUNIT: Monomer (By similarity). Homodimer. Interacts with PPARG. {ECO:0000250, ECO:0000269|PubMed:12077340, ECO:0000269|PubMed:14594993, ECO:0000269|PubMed:16574478, ECO:0000269|PubMed:17761196, ECO:0000269|PubMed:7929228, ECO:0000269|PubMed:8161548}. DOMAIN: Forms a beta-barrel structure that accommodates the hydrophobic ligand in its interior. +P51880 FABP7_MOUSE Fatty acid-binding protein, brain (Brain lipid-binding protein) (BLBP) (Brain-type fatty acid-binding protein) (B-FABP) (Fatty acid-binding protein 7) 132 14,893 Chain (1); Initiator methionine (1); Modified residue (1); Region (1) FUNCTION: B-FABP could be involved in the transport of a so far unknown hydrophobic ligand with potential morphogenic activity during CNS development. It is required for the establishment of the radial glial fiber system in developing brain, a system that is necessary for the migration of immature neurons to establish cortical layers. SUBCELLULAR LOCATION: Cytoplasm. DOMAIN: Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain and other neural tissues. +Q920L1 FADS1_MOUSE Acyl-CoA (8-3)-desaturase (EC 1.14.19.44) (Delta(5) fatty acid desaturase) (D5D) (Delta(5) desaturase) (Delta-5 desaturase) (Fatty acid desaturase 1) 447 52,323 Chain (1); Domain (1); Modified residue (1); Motif (3); Sequence conflict (5); Topological domain (5); Transmembrane (4) TRANSMEM 125 145 Helical. {ECO:0000255}.; TRANSMEM 161 180 Helical. {ECO:0000255}.; TRANSMEM 269 289 Helical. {ECO:0000255}.; TRANSMEM 309 329 Helical. {ECO:0000255}. TOPO_DOM 1 124 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 146 160 Lumenal. {ECO:0000255}.; TOPO_DOM 181 268 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 290 308 Lumenal. {ECO:0000255}.; TOPO_DOM 330 447 Cytoplasmic. {ECO:0000255}. Lipid metabolism; polyunsaturated fatty acid biosynthesis. FUNCTION: Acts as a front-end fatty acyl-coenzyme A (CoA) desaturase that introduces a cis double bond at carbon 5 located between a preexisting double bond and the carboxyl end of the fatty acyl chain. Involved in biosynthesis of highly unsaturated fatty acids (HUFA) from the essential polyunsaturated fatty acids (PUFA) linoleic acid (LA) (18:2n-6) and alpha-linolenic acid (ALA) (18:3n-3) precursors. Specifically, desaturates dihomo-gamma-linoleoate (DGLA) (20:3n-6) and eicosatetraenoate (ETA) (20:4n-3) to generate arachidonate (AA) (20:4n-6) and eicosapentaenoate (EPA) (20:5n-3), respectively (Probable). As a rate limiting enzyme for DGLA (20:3n-6) and AA (20:4n-6)-derived eicosanoid biosynthesis, controls the metabolism of inflammatory lipids like prostaglandin E2, critical for efficient acute inflammatory response and maintenance of epithelium homeostasis. Contributes to membrane phospholipid biosynthesis by providing AA (20:4n-6) as a major acyl chain esterified into phospholipids. In particular, regulates phosphatidylinositol-4,5-bisphosphate levels, modulating inflammatory cytokine production in T-cells (PubMed:22534642). Also desaturates (11E)-octadecenoate (trans-vaccenoate)(18:1n-9), a metabolite in the biohydrogenation pathway of LA (18:2n-6) (By similarity). {ECO:0000250|UniProtKB:Q920R3, ECO:0000269|PubMed:22534642, ECO:0000305|PubMed:22534642}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:A4UVI1}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A4UVI1}. Mitochondrion {ECO:0000250|UniProtKB:O60427}. DOMAIN: The histidine box domains may contain the active site and/or be involved in metal ion binding. TISSUE SPECIFICITY: Highly expressed in the adrenal gland, liver, brain, and testis, tissues where lipogenesis and steroidogenesis are active (PubMed:11792729). Expressed in colonic mucosa (PubMed:22534642). {ECO:0000269|PubMed:11792729, ECO:0000269|PubMed:22534642}. +Q80UG1 FADS6_MOUSE Fatty acid desaturase 6 (EC 1.14.19.-) 342 38,831 Alternative sequence (1); Chain (1); Motif (3); Sequence conflict (1); Transmembrane (5) TRANSMEM 39 59 Helical. {ECO:0000255}.; TRANSMEM 63 83 Helical. {ECO:0000255}.; TRANSMEM 100 120 Helical. {ECO:0000255}.; TRANSMEM 151 171 Helical. {ECO:0000255}.; TRANSMEM 185 205 Helical. {ECO:0000255}. Lipid metabolism; fatty acid metabolism. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8R0F8 FAHD1_MOUSE Acylpyruvase FAHD1, mitochondrial (EC 3.7.1.5) (Fumarylacetoacetate hydrolase domain-containing protein 1) (Oxaloacetate decarboxylase) (OAA decarboxylase) (EC 4.1.1.112) 227 25,172 Chain (1); Erroneous initiation (1); Metal binding (3); Modified residue (3); Sequence conflict (3); Transit peptide (1) FUNCTION: Probable mitochondrial acylpyruvase which is able to hydrolyze acetylpyruvate and fumarylpyruvate in vitro (By similarity). Also has oxaloacetate decarboxylase activity (PubMed:25575590). {ECO:0000250|UniProtKB:Q6P587, ECO:0000269|PubMed:25575590}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q6P587}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q6P587}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q6P587}. TISSUE SPECIFICITY: Ubiquitous with higher expression in the liver and the kidney (at protein level). {ECO:0000269|PubMed:21878618}. +Q3TDN2 FAF2_MOUSE FAS-associated factor 2 (UBX domain-containing protein 8) 445 52,471 Alternative sequence (1); Chain (1); Coiled coil (1); Domain (2); Initiator methionine (1); Modified residue (2); Sequence conflict (2) FUNCTION: Plays an important role in endoplasmic reticulum-associated degradation (ERAD) that mediates ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. By controlling the steady-state expression of the IGF1R receptor, indirectly regulates the insulin-like growth factor receptor signaling pathway. Involved in inhibition of lipid droplet degradation by binding to phospholipase PNPL2 and inhibiting its activity by promoting dissociation of PNPL2 from its endogenous activator, ABHD5 which inhibits the rate of triacylglycerol hydrolysis. {ECO:0000250|UniProtKB:Q96CS3}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96CS3}. Lipid droplet {ECO:0000250|UniProtKB:Q96CS3}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q96CS3}. SUBUNIT: Identified in a complex that contains SEL1L, OS9, FAF2/UBXD8, UBE2J1/UBC6E and AUP1. Interacts with YOD1. Interacts (via N-terminus) with UBQLN2 (via C-terminus). Interacts with PNPLA2 and UBAC2 (By similarity). Interacts with ZFAND2B; probably through VCP (PubMed:24160817). {ECO:0000250|UniProtKB:Q96CS3, ECO:0000269|PubMed:24160817}. +Q8VCE2 GPN1_MOUSE GPN-loop GTPase 1 (EC 3.6.5.-) (MBD2-interacting protein) (MBDin) (XPA-binding protein 1) 372 41,598 Chain (1); Initiator methionine (1); Modified residue (6); Motif (1); Nucleotide binding (2); Site (1) FUNCTION: Small GTPase required for proper nuclear import of RNA polymerase II (RNAPII). May act at an RNAP assembly step prior to nuclear import. Forms an interface between the RNA polymerase II enzyme and chaperone/scaffolding proteins, suggesting that it is required to connect RNA polymerase II to regulators of protein complex formation. May be involved in nuclear localization of XPA. {ECO:0000250|UniProtKB:Q9HCN4}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9HCN4}. Nucleus {ECO:0000250|UniProtKB:Q9HCN4}. Note=Shuttles between the nucleus and the cytoplasm. {ECO:0000250|UniProtKB:Q9HCN4}. SUBUNIT: Heterodimer with GPN3. Binds to RNA polymerase II (RNAPII). Interacts directly with RNAPII subunits RPB4 and RPB7 and the CTD of RPB1. Interacts with XPA. {ECO:0000250|UniProtKB:Q9HCN4}. +Q8VEJ1 GPN2_MOUSE GPN-loop GTPase 2 (ATP-binding domain 1 family member B) 310 34,540 Chain (1); Initiator methionine (1); Modified residue (1); Motif (1); Nucleotide binding (2); Sequence conflict (2); Site (1) FUNCTION: Small GTPase required for proper localization of RNA polymerase II and III (RNAPII and RNAPIII). May act at an RNAP assembly step prior to nuclear import. {ECO:0000250|UniProtKB:Q08726}. SUBUNIT: Heterodimers with GPN1 or GPN3. Binds to RNA polymerase II (RNAPII). {ECO:0000250|UniProtKB:Q08726, ECO:0000250|UniProtKB:Q9H9Y4}. +Q9D3W4 GPN3_MOUSE GPN-loop GTPase 3 (ATP-binding domain 1 family member C) 284 32,790 Chain (1); Frameshift (1); Motif (1); Nucleotide binding (2); Site (1) FUNCTION: Small GTPase required for proper localization of RNA polymerase II (RNAPII). May act at an RNAP assembly step prior to nuclear import. {ECO:0000250|UniProtKB:Q9UHW5}. SUBUNIT: Heterodimer with GPN1. Binds to RNA polymerase II (RNAPII). Interacts directly with subunits RPB4 and RPB7 and the CTD of RPB1. {ECO:0000250|UniProtKB:Q9UHW5}. +Q91VU0 FAM3C_MOUSE Protein FAM3C (Interleukin-like EMT inducer) 227 24,753 Beta strand (10); Chain (1); Disulfide bond (2); Helix (4); Sequence conflict (1); Signal peptide (1); Turn (5) FUNCTION: May be involved in retinal laminar formation. Promotes epithelial to mesenchymal transition. {ECO:0000269|PubMed:16959614, ECO:0000269|PubMed:19015638, ECO:0000269|PubMed:20059962}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20059962}. Cytoplasmic vesicle {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in the retina. Up-regulated in mammary epithelial cells and hepatocytes undergoing epithelial to mesenchymal transition (at protein level). {ECO:0000269|PubMed:15194199, ECO:0000269|PubMed:16959614, ECO:0000269|PubMed:20059962}. +E9Q5Z5 FANCF_MOUSE Fanconi anemia group F protein (Protein FACF) 343 38,224 Chain (1) FUNCTION: DNA repair protein that may operate in a postreplication repair or a cell cycle checkpoint function. May be implicated in interstrand DNA cross-link repair and in the maintenance of normal chromosome stability. {ECO:0000269|PubMed:21915857}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NPI8}. SUBUNIT: Belongs to the multisubunit FA complex composed of FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL/PHF9 and FANCM. In complex with FANCA, FANCG and FANCL, but not with FANCC, nor FANCE, interacts with HES1; this interaction may be essential for the stability and nuclear localization of FA core complex proteins. {ECO:0000250|UniProtKB:Q9NPI8}. +Q9EQR6 FANCG_MOUSE Fanconi anemia group G protein homolog (Protein FACG) 623 68,506 Chain (1); Repeat (4) FUNCTION: DNA repair protein that may operate in a postreplication repair or a cell cycle checkpoint function. May be implicated in interstrand DNA cross-link repair and in the maintenance of normal chromosome stability. Candidate tumor suppressor gene (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11918676}. SUBUNIT: Belongs to the multisubunit FA complex composed of FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL/PHF9 and FANCM. In complex with FANCF, FANCA and FANCL, but not with FANCC, nor FANCE, interacts with HES1; this interaction may be essential for the stability and nuclear localization of FA core complex proteins. The complex with FANCC and FANCG may also include EIF2AK2 and HSP70. {ECO:0000250}. TISSUE SPECIFICITY: Highest expression levels in spleen, thymus and testis. {ECO:0000269|PubMed:11918676}. +Q69ZT1 FAN1_MOUSE Fanconi-associated nuclease 1 (EC 3.1.21.-) (EC 3.1.4.1) (FANCD2/FANCI-associated nuclease 1) (mFAN1) (Myotubularin-related protein 15) 1020 112,925 Alternative sequence (6); Chain (1); Coiled coil (1); Domain (1); Metal binding (5); Motif (2); Zinc finger (1) FUNCTION: Nuclease required for the repair of DNA interstrand cross-links (ICL) recruited at sites of DNA damage by monoubiquitinated FANCD2. Specifically involved in repair of ICL-induced DNA breaks by being required for efficient homologous recombination, probably in the resolution of homologous recombination intermediates (By similarity). Not involved in DNA double-strand breaks resection. Acts as a 5'-3' exonuclease that anchors at a cut end of DNA and cleaves DNA successively at every third nucleotide, allowing to excise an ICL from one strand through flanking incisions (PubMed:24981866). Probably keeps excising with 3'-flap annealing until it reaches and unhooks the ICL. Acts at sites that have a 5'-terminal phosphate anchor at a nick or a 1- or 2-nucleotide flap and is augmented by a 3' flap (By similarity). Also has endonuclease activity toward 5'-flaps (PubMed:24981866). {ECO:0000250|UniProtKB:Q9Y2M0, ECO:0000269|PubMed:24981866}. PTM: Ubiquitinated and degraded during mitotic exit by the APC/C-Cdh1 complex. {ECO:0000250|UniProtKB:Q9Y2M0}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y2M0}. Note=Localizes at sites of DNA damage following recruitment by monoubiquitinated FANCD2. Localizes to stalled replication forks via its UBZ-type zinc finger. {ECO:0000250|UniProtKB:Q9Y2M0}. SUBUNIT: Interacts with FANCD2 (when monoubiquitinated). Interacts with FANCI, MLH1, MLH3 and PMS2. {ECO:0000250|UniProtKB:Q9Y2M0}. DOMAIN: The UBZ-type zinc finger specifically binds monoubiquitinated FANCD2. {ECO:0000250|UniProtKB:Q9Y2M0}.; DOMAIN: The KEN box and D-box are required for interaction with FZR1/CDH1 and essential for APC(CDH1)-mediated ubiquitination. {ECO:0000250|UniProtKB:Q9Y2M0}. +Q9CR14 FANCL_MOUSE E3 ubiquitin-protein ligase FANCL (EC 2.3.2.27) (Fanconi anemia group L protein homolog) (Proliferation of germ cells protein) (RING-type E3 ubiquitin transferase FANCL) 375 42,527 Alternative sequence (1); Chain (1); Region (1); Sequence conflict (1); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: Ubiquitin ligase protein that mediates monoubiquitination of FANCD2, a key step in the DNA damage pathway. Also mediates monoubiquitination of FANCI. May stimulate the ubiquitin release from UBE2W. May be required for proper primordial germ cell proliferation in the embryonic stage, whereas it is probably not needed for spermatogonial proliferation after birth. {ECO:0000269|PubMed:12417526, ECO:0000269|PubMed:12606378}. PTM: The RING-type zinc finger domain is monoubiquitinated in the presence of UBE2T and UBE2W. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21229326}. Nucleus {ECO:0000269|PubMed:21229326}. Note=In the nucleus, colocalizes with UBE2W. SUBUNIT: Belongs to the multisubunit FA complex composed of FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL/PHF9 and FANCM (By similarity). In complex with FANCF, FANCA and FANCG, but not with FANCC, nor FANCE, interacts with HES1; this interaction may be essential for the stability and nuclear localization of FA core complex proteins. Interacts with FANCI (By similarity). Interacts with GGN. Interacts (via the RING-type zinc finger) with UBE2T and UBE2W. {ECO:0000250|UniProtKB:Q9NW38, ECO:0000269|PubMed:12574169, ECO:0000269|PubMed:21229326}. DOMAIN: The UBC-RWD region (URD) region mediates interaction with FANCI and FANCD2. {ECO:0000250|UniProtKB:Q9NW38}. DISEASE: Note=Defects in Fancl are a cause of the gcd (germ cell deficient) mutant phenotype, which leads to reduced numbers of precursor germ cells and adult sterility, probably due to a reduced precursor germ cells proliferation. +Q8BZA7 GPR26_MOUSE G-protein coupled receptor 26 337 37,747 Chain (1); Disulfide bond (1); Sequence conflict (1); Topological domain (8); Transmembrane (7) TRANSMEM 11 31 Helical; Name=1. {ECO:0000255}.; TRANSMEM 48 68 Helical; Name=2. {ECO:0000255}.; TRANSMEM 82 102 Helical; Name=3. {ECO:0000255}.; TRANSMEM 124 144 Helical; Name=4. {ECO:0000255}.; TRANSMEM 169 189 Helical; Name=5. {ECO:0000255}.; TRANSMEM 246 266 Helical; Name=6. {ECO:0000255}.; TRANSMEM 277 297 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 10 Extracellular. {ECO:0000255}.; TOPO_DOM 32 47 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 69 81 Extracellular. {ECO:0000255}.; TOPO_DOM 103 123 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 145 168 Extracellular. {ECO:0000255}.; TOPO_DOM 190 245 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 267 276 Extracellular. {ECO:0000255}.; TOPO_DOM 298 337 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan receptor. Displays a significant level of constitutive activity. Its effect is mediated by G(s)-alpha protein that stimulate adenylate cyclase, resulting in an elevation of intracellular cAMP (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Exclusively expressed in the brain. Prominent expression is detected throughout the entire neocortex at all rostrocaudal and dorsoventral levels. Strong expression is detected in olfactory and auditory sensory areas. {ECO:0000269|PubMed:17363172}. +Q3UMF9 FAXC_MOUSE Failed axon connections homolog 409 46,811 Chain (1); Transmembrane (1) TRANSMEM 68 88 Helical. {ECO:0000255}. FUNCTION: May play a role in axonal development. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +O54897 GPR27_MOUSE Probable G-protein coupled receptor 27 (Super conserved receptor expressed in brain 1) 379 40,036 Chain (1); Disulfide bond (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 27 47 Helical; Name=1. {ECO:0000255}.; TRANSMEM 59 79 Helical; Name=2. {ECO:0000255}.; TRANSMEM 101 121 Helical; Name=3. {ECO:0000255}.; TRANSMEM 143 163 Helical; Name=4. {ECO:0000255}.; TRANSMEM 186 206 Helical; Name=5. {ECO:0000255}.; TRANSMEM 290 310 Helical; Name=6. {ECO:0000255}.; TRANSMEM 325 345 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 26 Extracellular. {ECO:0000255}.; TOPO_DOM 48 58 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 80 100 Extracellular. {ECO:0000255}.; TOPO_DOM 122 142 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 164 185 Extracellular. {ECO:0000255}.; TOPO_DOM 207 289 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 311 324 Extracellular. {ECO:0000255}.; TOPO_DOM 346 379 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan receptor. Possible candidate for amine-like G-protein coupled receptor (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +O88416 GPR33_MOUSE Probable G-protein coupled receptor 33 339 38,446 Chain (1); Disulfide bond (1); Glycosylation (3); Topological domain (8); Transmembrane (7) TRANSMEM 31 53 Helical; Name=1. {ECO:0000255}.; TRANSMEM 65 86 Helical; Name=2. {ECO:0000255}.; TRANSMEM 104 124 Helical; Name=3. {ECO:0000255}.; TRANSMEM 144 165 Helical; Name=4. {ECO:0000255}.; TRANSMEM 210 230 Helical; Name=5. {ECO:0000255}.; TRANSMEM 247 268 Helical; Name=6. {ECO:0000255}.; TRANSMEM 284 303 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 30 Extracellular. {ECO:0000255}.; TOPO_DOM 54 64 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 87 103 Extracellular. {ECO:0000255}.; TOPO_DOM 125 143 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 166 209 Extracellular. {ECO:0000255}.; TOPO_DOM 231 246 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 269 283 Extracellular. {ECO:0000255}.; TOPO_DOM 304 339 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan receptor; could be a chemoattractant receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed predominantly in lung, spleen and testis. {ECO:0000269|PubMed:15987686}. +Q80WS3 FBLL1_MOUSE rRNA/tRNA 2'-O-methyltransferase fibrillarin-like protein 1 (EC 2.1.1.-) (Protein-glutamine methyltransferase) 314 33,339 Chain (1); Compositional bias (1); Modified residue (1); Region (4) FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that has the ability to methylate both RNAs and proteins. Involved in pre-rRNA processing by catalyzing the site-specific 2'-hydroxyl methylation of ribose moieties in pre-ribosomal RNA. Also acts as a protein methyltransferase by mediating methylation of glutamine residues (By similarity). {ECO:0000250}. PTM: By homology to other fibrillarins, some or all of the N-terminal domain arginines are modified to asymmetric dimethylarginine (DMA). SUBCELLULAR LOCATION: Nucleus, nucleolus. Note=Fibrillar region of the nucleolus. {ECO:0000250}. +A2A870 FBF1_MOUSE Fas-binding factor 1 (FBF-1) 1173 130,138 Alternative sequence (1); Chain (1); Coiled coil (3); Cross-link (1); Modified residue (1); Sequence conflict (2) FUNCTION: Keratin-binding protein required for epithelial cell polarization. Involved in apical junction complex (AJC) assembly via its interaction with PARD3. Required for ciliogenesis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:10978533}. Cell junction {ECO:0000250}. Note=Localizes specifically to the distal appendage region of the centriole, which anchors the mother centriole to the plasma membrane. Localizes to the apical junction complex (AJC) in epithelial cells (By similarity). {ECO:0000250}. SUBUNIT: Interacts with PARD3 (By similarity). May interact with FAS cytoplasmic domain. {ECO:0000250}. TISSUE SPECIFICITY: Broadly expressed. {ECO:0000269|PubMed:10978533}. +Q99PT1 GDIR1_MOUSE Rho GDP-dissociation inhibitor 1 (Rho GDI 1) (GDI-1) (Rho-GDI alpha) 204 23,407 Beta strand (9); Chain (1); Cross-link (4); Helix (4); Initiator methionine (1); Modified residue (9); Mutagenesis (1); Sequence conflict (1); Turn (2) FUNCTION: Controls Rho proteins homeostasis. Regulates the GDP/GTP exchange reaction of the Rho proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them. Retains Rho proteins such as CDC42, RAC1 and RHOA in an inactive cytosolic pool, regulating their stability and protecting them from degradation. Actively involved in the recycling and distribution of activated Rho GTPases in the cell, mediates extraction from membranes of both inactive and activated molecules due its exceptionally high affinity for prenylated forms. Through the modulation of Rho proteins, may play a role in cell motility regulation. In glioma cells, inhibits cell migration and invasion by mediating the signals of SEMA5A and PLXNB3 that lead to inactivation of RAC1. {ECO:0000269|PubMed:19029984, ECO:0000269|PubMed:22628549, ECO:0000269|PubMed:23434736}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23434736}. SUBUNIT: Monomer (PubMed:22628549). Interacts with FER (By similarity). Interacts with PLXNB3 (PubMed:20696765). Forms a heterodimer with RAC1 (PubMed:23434736). Interacts with RHOA, the affinity is increased by three orders of magnitude when RHOA is prenylated (PubMed:23434736). Interacts with PSMD10; the interaction increases ARHGDIA association with RHOA, leading to ARHGDIA-mediated inactivation of RHOA and ROCK and prolonged AKT activation (By similarity). Interacts with KANK2; the interaction is direct and may regulate the interaction of ARHGDIA with RHOA, RAC1 and CDC42 (By similarity). Interacts with RHOC (By similarity). Interacts with CDC42 (PubMed:23434736). {ECO:0000250|UniProtKB:P52565, ECO:0000269|PubMed:20696765, ECO:0000269|PubMed:22628549, ECO:0000269|PubMed:23434736}. TISSUE SPECIFICITY: In kidney glomerulus, expressed in podocytes and mesangial cells. {ECO:0000269|PubMed:19029984, ECO:0000269|PubMed:23434736}. +Q99JX4 EIF3M_MOUSE Eukaryotic translation initiation factor 3 subunit M (eIF3m) (PCI domain-containing protein 1) 374 42,517 Chain (1); Domain (1); Initiator methionine (1); Modified residue (5); Sequence conflict (3) FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression. {ECO:0000255|HAMAP-Rule:MF_03012}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03012}. SUBUNIT: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B, EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and EIF3M. The eIF-3 complex appears to include 3 stable modules: module A is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D, EIF3E, EIF3K and EIF3L. EIF3C of module C binds EIF3B of module A and EIF3H of module B, thereby linking the three modules. EIF3J is a labile subunit that binds to the eIF-3 complex via EIF3B. The eIF-3 complex interacts with RPS6KB1 under conditions of nutrient depletion. Mitogenic stimulation leads to binding and activation of a complex composed of MTOR and RPTOR, leading to phosphorylation and release of RPS6KB1 and binding of EIF4B to eIF-3. {ECO:0000255|HAMAP-Rule:MF_03012}. +Q60899 ELAV2_MOUSE ELAV-like protein 2 (ELAV-like neuronal protein 1) (Hu-antigen B) (HuB) (Nervous system-specific RNA-binding protein Mel-N1) 360 39,577 Chain (1); Domain (3); Modified residue (1) FUNCTION: Binds RNA. Seems to recognize a GAAA motif. Can bind to its own 3'-UTR, the FOS 3'-UTR and the ID 3'-UTR. {ECO:0000269|PubMed:8668530}. SUBUNIT: Interacts with IGF2BP1. {ECO:0000250}. TISSUE SPECIFICITY: Brain; neural-specific. {ECO:0000269|PubMed:8668530}. +Q3UP87 ELNE_MOUSE Neutrophil elastase (EC 3.4.21.37) (Elastase-2) (Leukocyte elastase) 265 28,648 Active site (3); Chain (1); Disulfide bond (4); Domain (1); Glycosylation (2); Sequence conflict (8); Signal peptide (1) FUNCTION: Medullasin modifies the functions of natural killer cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme release and chemotaxis (By similarity). {ECO:0000250}. SUBUNIT: Interacts with NOTCH2NL. {ECO:0000250}. +Q91W53 GOGA7_MOUSE Golgin subfamily A member 7 137 15,792 Alternative sequence (1); Chain (1); Frameshift (1); Lipidation (2) FUNCTION: May be involved in protein transport from Golgi to cell surface. The ZDHHC9-GOLGA7 complex is a palmitoyltransferase specific for HRAS and NRAS (By similarity). {ECO:0000250}. PTM: Palmitoylated on Cys-69 and Cys-72; which is required for Golgi localization and interaction with GOLGA3. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. SUBUNIT: Interacts with GOLGA3. Interacts with ZDHHC9 (By similarity). {ECO:0000250}. +Q9WUZ9 ENTP5_MOUSE Ectonucleoside triphosphate diphosphohydrolase 5 (NTPDase 5) (EC 3.6.1.6) (CD39 antigen-like 4) (ER-UDPase) (Guanosine-diphosphatase ENTPD5) (GDPase ENTPD5) (EC 3.6.1.42) (Nucleoside diphosphatase) (Uridine-diphosphatase ENTPD5) (UDPase ENTPD5) 427 47,102 Active site (1); Chain (1); Disulfide bond (2); Glycosylation (1); Mutagenesis (1); Sequence conflict (3); Signal peptide (1) Protein modification; protein glycosylation. FUNCTION: Uridine diphosphatase (UDPase) that promotes protein N-glycosylation and ATP level regulation. UDP hydrolysis promotes protein N-glycosylation and folding in the endoplasmic reticulum, as well as elevated ATP consumption in the cytosol via an ATP hydrolysis cycle. Together with CMPK1 and AK1, constitutes an ATP hydrolysis cycle that converts ATP to AMP and results in a compensatory increase in aerobic glycolysis. The nucleotide hydrolyzing preference is GDP > IDP > UDP, but not any other nucleoside di-, mono- or triphosphates, nor thiamine pyrophosphate. Plays a key role in the AKT1-PTEN signaling pathway by promoting glycolysis in proliferating cells in response to phosphoinositide 3-kinase (PI3K) signaling. {ECO:0000269|PubMed:10369669, ECO:0000269|PubMed:21074248}. PTM: N-glycosylated; high-mannose type. {ECO:0000269|PubMed:10369669, ECO:0000269|PubMed:21074248}. SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:10369669, ECO:0000269|PubMed:21074248}. Secreted {ECO:0000250}. SUBUNIT: Exists both as a monomer and a disulfide-linked homodimer, the dimers are enzymatically inactive. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. +P14753 EPOR_MOUSE Erythropoietin receptor (EPO-R) 507 55,194 Alternative sequence (2); Chain (1); Cross-link (2); Disulfide bond (2); Domain (1); Glycosylation (2); Helix (2); Modified residue (8); Motif (3); Mutagenesis (34); Sequence conflict (1); Signal peptide (1); Site (4); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 250 272 Helical. {ECO:0000255}. TOPO_DOM 25 249 Extracellular. {ECO:0000255}.; TOPO_DOM 273 507 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for erythropoietin. Mediates erythropoietin-induced erythroblast proliferation and differentiation. Upon EPO stimulation, EPOR dimerizes triggering the JAK2/STAT5 signaling cascade. In some cell types, can also activate STAT1 and STAT3. May also activate the LYN tyrosine kinase. {ECO:0000269|PubMed:8382775, ECO:0000269|PubMed:8617735}. PTM: The identity of the C-linked hexose on the WXXW motif has not been determined. It is probably mannose.; PTM: On EPO stimulation, phosphorylated on C-terminal tyrosine residues by JAK2. The phosphotyrosine motifs are also recruitment sites for several SH2-containing proteins and adapter proteins which mediate cell proliferation. Phosphorylation on Tyr-453 is required for PTPN6 interaction, Tyr-425 for PTPN11. Tyr-425 is also required for SOCS3 binding, but Tyr-453/Tyr-455 motif is the preferred binding site (By similarity). {ECO:0000250}.; PTM: Ubiquitinated by NOSIP; appears to be either multi-monoubiquitinated or polyubiquitinated. Ubiquitination mediates proliferation and survival of EPO-dependent cells (By similarity). Ubiquitination at Lys-280 mediates receptor internalization, whereas ubiquitination at Lys-452 promotes trafficking of activated receptors to the lysosomes for degradation. {ECO:0000250, ECO:0000269|PubMed:21183685}. SUBCELLULAR LOCATION: Isoform EPOR-F: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Isoform EPOR-S: Secreted. SUBUNIT: Forms homodimers on EPO stimulation. The tyrosine-phosphorylated form interacts with several SH2 domain-containing proteins including LYN, the adapter protein APS, PTPN6, PTPN11, JAK2, PI3 kinases, STAT5A/B, SOCS3 and CRKL. The N-terminal SH2 domain of PTPN6 binds Tyr-453 and inhibits signaling through dephosphorylation of JAK2. APS binding also inhibits the JAK-STAT signaling. Binding to PTPN11, preferentially through the N-terminal SH2 domain, promotes mitogenesis and phosphorylation of PTPN11. Binding of JAK2 (through its N-terminal) promotes cell-surface expression. Interaction with the ubiquitin ligase NOSIP mediates EPO-induced cell proliferation. Interacts with ATXN2L (By similarity). Forms heterooligomers with friend spleen focus-forming virus (FSFFV) gp55, probably via their respective transmembrane domains. Interacts with INPP5D/SHIP1. {ECO:0000250, ECO:0000269|PubMed:10660611, ECO:0000269|PubMed:11443118, ECO:0000269|PubMed:12444928, ECO:0000269|PubMed:12930840, ECO:0000269|PubMed:7889566, ECO:0000269|PubMed:8068943, ECO:0000269|PubMed:8639815, ECO:0000269|PubMed:8657137, ECO:0000269|PubMed:8665851, ECO:0000269|PubMed:9573010}. DOMAIN: The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.; DOMAIN: The box 1 motif is required for JAK interaction and/or activation.; DOMAIN: Contains 1 copy of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is involved in modulation of cellular responses. The phosphorylated ITIM motif can bind the SH2 domain of several SH2-containing phosphatases. TISSUE SPECIFICITY: Expressed in relatively mature erythroid progenitor cells and in EPO-responsive erythroleukemia cells. +Q8BPS4 GP180_MOUSE Integral membrane protein GPR180 441 48,975 Chain (1); Glycosylation (1); Sequence conflict (1); Signal peptide (1); Transmembrane (7) TRANSMEM 174 194 Helical. {ECO:0000255}.; TRANSMEM 206 226 Helical. {ECO:0000255}.; TRANSMEM 250 270 Helical. {ECO:0000255}.; TRANSMEM 285 305 Helical. {ECO:0000255}.; TRANSMEM 322 342 Helical. {ECO:0000255}.; TRANSMEM 361 381 Helical. {ECO:0000255}.; TRANSMEM 390 410 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8CHU3 EPN2_MOUSE Epsin-2 (EPS-15-interacting protein 2) (Intersectin-EH-binding protein 2) (Ibp2) 595 63,472 Alternative sequence (1); Binding site (6); Chain (1); Domain (3); Erroneous initiation (1); Modified residue (7); Region (2); Repeat (9); Sequence conflict (1) FUNCTION: Plays a role in the formation of clathrin-coated invaginations and endocytosis. {ECO:0000250}. PTM: Ubiquitinated. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=In punctate structures throughout the cell and particularly concentrated in the region of the Golgi complex. {ECO:0000250}. SUBUNIT: Binds EPS15, AP-2 and clathrin (By similarity). Interacts with UBQLN2 (By similarity). Interacts with ITSN1. {ECO:0000250|UniProtKB:O95208, ECO:0000250|UniProtKB:Q9Z1Z3, ECO:0000269|PubMed:9813051}. DOMAIN: The NPF repeat domain is involved in EPS15 binding.; DOMAIN: The DPW repeat domain is involved in AP-2 and clathrin binding. +Q99JH8 ERD21_MOUSE ER lumen protein-retaining receptor 1 (KDEL endoplasmic reticulum protein retention receptor 1) (KDEL receptor 1) 212 24,560 Chain (1); Modified residue (1); Topological domain (8); Transmembrane (7) TRANSMEM 3 21 Helical. {ECO:0000255}.; TRANSMEM 36 53 Helical. {ECO:0000255}.; TRANSMEM 62 80 Helical. {ECO:0000255}.; TRANSMEM 97 110 Helical. {ECO:0000255}.; TRANSMEM 118 137 Helical. {ECO:0000255}.; TRANSMEM 150 168 Helical. {ECO:0000255}.; TRANSMEM 179 199 Helical. {ECO:0000255}. TOPO_DOM 1 2 Lumenal. {ECO:0000255}.; TOPO_DOM 22 35 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 54 61 Lumenal. {ECO:0000255}.; TOPO_DOM 81 96 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 111 117 Lumenal. {ECO:0000255}.; TOPO_DOM 138 149 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 169 178 Lumenal. {ECO:0000255}.; TOPO_DOM 200 212 Cytoplasmic. {ECO:0000255}. FUNCTION: Required for the retention of luminal endoplasmic reticulum resident proteins via vesicular recycling. This receptor recognizes the C-terminal K-D-E-L motif. COPI-coated transport intermediates, either in the form of round vesicles or as tubular processes, mediate retrograde traffic of the KDEL receptor-ligand complexes. Also required for normal vesicular traffic through the Golgi (By similarity). {ECO:0000250}. PTM: Phosphorylation by PKA at Ser-209 is required for ER retention function. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane; Multi-pass membrane protein. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250}. SUBUNIT: Upon ligand binding the receptor oligomerizes and interacts with components of the transport machinery such as ARFGAP1 and ARF1. {ECO:0000250}. +Q8R050 ERF3A_MOUSE Eukaryotic peptide chain release factor GTP-binding subunit ERF3A (Eukaryotic peptide chain release factor subunit 3a) (eRF3a) (G1 to S phase transition protein 1 homolog) 636 68,625 Alternative sequence (1); Chain (1); Domain (1); Erroneous initiation (2); Nucleotide binding (3); Region (5); Sequence conflict (3) FUNCTION: Involved in translation termination in response to the termination codons UAA, UAG and UGA (By similarity). Stimulates the activity of ETF1 (By similarity). Involved in regulation of mammalian cell growth (By similarity). Component of the transient SURF complex which recruits UPF1 to stalled ribosomes in the context of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons (By similarity). {ECO:0000250|UniProtKB:P15170, ECO:0000250|UniProtKB:Q8IYD1}. SUBUNIT: Component of the transient SURF (SMG1-UPF1-eRF1-eRF3) complex (By similarity). Interacts with PABPC1 (Ref.7). The ETF1-GSPT1 complex interacts with JMJD4 (By similarity). {ECO:0000250|UniProtKB:P15170, ECO:0000269|Ref.7}. +Q9CQM2 ERD22_MOUSE ER lumen protein-retaining receptor 2 (KDEL endoplasmic reticulum protein retention receptor 2) (KDEL receptor 2) 212 24,454 Chain (1); Topological domain (8); Transmembrane (7) TRANSMEM 3 21 Helical. {ECO:0000255}.; TRANSMEM 36 53 Helical. {ECO:0000255}.; TRANSMEM 62 80 Helical. {ECO:0000255}.; TRANSMEM 97 110 Helical. {ECO:0000255}.; TRANSMEM 118 137 Helical. {ECO:0000255}.; TRANSMEM 150 168 Helical. {ECO:0000255}.; TRANSMEM 179 199 Helical. {ECO:0000255}. TOPO_DOM 1 2 Lumenal. {ECO:0000255}.; TOPO_DOM 22 35 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 54 61 Lumenal. {ECO:0000255}.; TOPO_DOM 81 96 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 111 117 Lumenal. {ECO:0000255}.; TOPO_DOM 138 149 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 169 178 Lumenal. {ECO:0000255}.; TOPO_DOM 200 212 Cytoplasmic. {ECO:0000255}. FUNCTION: Required for the retention of luminal endoplasmic reticulum proteins. Determines the specificity of the luminal ER protein retention system. Also required for normal vesicular traffic through the Golgi. This receptor recognizes K-D-E-L (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +B2RWS6 EP300_MOUSE Histone acetyltransferase p300 (p300 HAT) (EC 2.3.1.48) (E1A-associated protein p300) (Histone butyryltransferase p300) (EC 2.3.1.-) (Histone crotonyltransferase p300) (EC 2.3.1.-) (Protein propionyltransferase p300) (EC 2.3.1.-) 2412 263,305 Binding site (3); Chain (1); Coiled coil (1); Compositional bias (3); Cross-link (2); Domain (3); Initiator methionine (1); Metal binding (12); Modified residue (30); Motif (1); Region (7); Sequence conflict (4); Site (2); Zinc finger (3) FUNCTION: Functions as histone acetyltransferase and regulates transcription via chromatin remodeling (By similarity). Acetylates all four core histones in nucleosomes (By similarity). Histone acetylation gives an epigenetic tag for transcriptional activation (By similarity). Mediates cAMP-gene regulation by binding specifically to phosphorylated CREB protein (PubMed:18486321, PubMed:24216764). Mediates acetylation of histone H3 at 'Lys-122' (H3K122ac), a modification that localizes at the surface of the histone octamer and stimulates transcription, possibly by promoting nucleosome instability (By similarity). Mediates acetylation of histone H3 at 'Lys-27' (H3K27ac) (By similarity). Also functions as acetyltransferase for non-histone targets, such as ALX1, HDAC1, PRMT1 or SIRT2 (PubMed:28883095). Acetylates 'Lys-131' of ALX1 and acts as its coactivator (By similarity). Acetylates SIRT2 and is proposed to indirectly increase the transcriptional activity of TP53 through acetylation and subsequent attenuation of SIRT2 deacetylase function (By similarity). Acetylates HDAC1 leading to its inactivation and modulation of transcription (By similarity). Acts as a TFAP2A-mediated transcriptional coactivator in presence of CITED2 (By similarity). Plays a role as a coactivator of NEUROD1-dependent transcription of the secretin and p21 genes and controls terminal differentiation of cells in the intestinal epithelium (By similarity). Promotes cardiac myocyte enlargement (By similarity). Can also mediate transcriptional repression (By similarity). Acetylates FOXO1 and enhances its transcriptional activity (By similarity). Acetylates BCL6 wich disrupts its ability to recruit histone deacetylases and hinders its transcriptional repressor activity (By similarity). Participates in CLOCK or NPAS2-regulated rhythmic gene transcription; exhibits a circadian association with CLOCK or NPAS2, correlating with increase in PER1/2 mRNA and histone H3 acetylation on the PER1/2 promoter (By similarity). Acetylates MTA1 at 'Lys-626' which is essential for its transcriptional coactivator activity (PubMed:14645221, PubMed:9512516). Acetylates XBP1 isoform 2; acetylation increases protein stability of XBP1 isoform 2 and enhances its transcriptional activity (PubMed:20955178). Acetylates PCNA; acetylation promotes removal of chromatin-bound PCNA and its degradation during nucleotide excision repair (NER) (By similarity). Acetylates MEF2D (By similarity). Acetylates and stabilizes ZBTB7B protein by antagonizing ubiquitin conjugation and degragation, this mechanism may be involved in CD4/CD8 lineage differentiation (PubMed:20810990). In addition to protein acetyltransferase, can use different acyl-CoA substrates, such as (2E)-butenoyl-CoA (crotonyl-CoA), butanoyl-CoA (butyryl-CoA) or propanoyl-CoA (propionyl-CoA), and is able to mediate protein crotonylation, butyrylation or propionylation, respectively (PubMed:27105113). Acts as a histone crotonyltransferase; crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. Histone crotonyltransferase activity is dependent on the concentration of (2E)-butenoyl-CoA (crotonyl-CoA) substrate and such activity is weak when (E)-but-2-enoyl-CoA (crotonyl-CoA) concentration is low (By similarity). Also acts as a histone butyryltransferase; butyrylation marks active promoters (PubMed:27105113). Functions as a transcriptional coactivator for SMAD4 in the TGF-beta signaling pathway (By similarity). Acetylates PCK1 and promotes PCK1 anaplerotic activity (By similarity). {ECO:0000250|UniProtKB:Q09472, ECO:0000269|PubMed:14645221, ECO:0000269|PubMed:18486321, ECO:0000269|PubMed:20810990, ECO:0000269|PubMed:24216764, ECO:0000269|PubMed:27105113, ECO:0000269|PubMed:28883095, ECO:0000269|PubMed:9512516, ECO:0000305|PubMed:20955178}. PTM: Acetylated on Lys at up to 17 positions by intermolecular autocatalysis. Deacetylated in the transcriptional repression domain (CRD1) by SIRT1, preferentially at Lys-1019. Deacetylated by SIRT2, preferentially at Lys-419, Lys-424, Lys-1541, Lys-1545, Lys-1548, Lys-1698, Lys-1703 and Lys-1706. {ECO:0000250|UniProtKB:Q09472}.; PTM: Citrullinated at Arg-2143 by PADI4, which impairs methylation by CARM1 and promotes interaction with NCOA2/GRIP1. {ECO:0000250}.; PTM: Methylated at Arg-581 and Arg-605 in the KIX domain by CARM1, which blocks association with CREB, inhibits CREB signaling and activates apoptotic response. Also methylated at Arg-2143 by CARM1, which impairs interaction with NCOA2/GRIP1 (By similarity). {ECO:0000250}.; PTM: Sumoylated; sumoylation in the transcriptional repression domain (CRD1) mediates transcriptional repression. Desumoylated by SENP3 through the removal of SUMO2 and SUMO3 (By similarity). {ECO:0000250}.; PTM: Probable target of ubiquitination by FBXO3, leading to rapid proteasome-dependent degradation. {ECO:0000250}.; PTM: Phosphorylation at Ser-89 by AMPK reduces interaction with nuclear receptors, such as PPARG (By similarity). Phosphorylated by HIPK2 in a RUNX1-dependent manner. This phosphorylation that activates EP300 happens when RUNX1 is associated with DNA and CBFB. Phosphorylated by ROCK2 and this enhances its activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q09472}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00311, ECO:0000269|PubMed:19324970}. Note=In the presence of ALX1 relocalizes from the cytoplasm to the nucleus. Colocalizes with ROCK2 in the nucleus. {ECO:0000250|UniProtKB:Q09472}. SUBUNIT: Interacts with phosphorylated CREB1. Interacts with HIF1A; the interaction is stimulated in response to hypoxia and inhibited by CITED2. Interacts (via N-terminus) with TFAP2A (via N-terminus); the interaction requires CITED2. Interacts (via CH1 domain) with CITED2 (via C-terminus). Interacts with CITED1 (unphosphorylated form preferentially and via C-terminus). Interacts with ESR1; the interaction is estrogen-dependent and enhanced by CITED1. Interacts with HIPK2, DTX1, EID1, ELF3, FEN1, LEF1, NCOA1, NCOA6, NR3C1, PCAF, PELP1, PRDM6, SP1, SP3, SPIB, SRY, TCF7L2, TP53, DDX5, DDX17, SATB1, SRCAP, TTC5, JMY and TRERF1. The TAZ-type 1 domain interacts with HIF1A. Probably part of a complex with HIF1A and CREBBP. Part of a complex containing CARM1 and NCOA2/GRIP1. Interacts with ING4 and this interaction may be indirect. Interacts with ING5. Interacts with the C-terminal region of CITED4. Non-sumoylated EP300 preferentially interacts with SENP3. Interacts with SS18L1/CREST. Interacts with ALX1 (via homeobox domain). Interacts with NEUROD1; the interaction is inhibited by NR0B2. Interacts with TCF3. Interacts with PPARG. Forms a complex made of CDK9, CCNT1/cyclin-T1, EP300 and GATA4 that stimulates hypertrophy in cardiomyocytes. Interacts with CITED1 and CITED2. Interacts with ROCK2. Interacts with NEUROD1. Interacts (via CREB-binding domain) with MYOCD (via C-terminus). Interacts with IRF1 and this interaction enhances acetylation of p53/TP53 and stimulation of its activity. Interacts with FOXO1; the interaction acetylates FOXO1 and enhances its transcriptional activity. Interacts with ALKBH4 and DDIT3/CHOP. Interacts with KLF15. Interacts with CEBPB and RORA (PubMed:18486321, PubMed:24216764). Interacts with ARNTL/BMAL1 and CLOCK (By similarity). Interacts with SIRT2. Interacts with MTA1. Interacts with HDAC4 and HDAC5 in the presence of TFAP2C (By similarity). Interacts with TRIP4 (By similarity). Interacts with NPAS2. Directly interacts with ZBTB49; this interaction leads to synergistic transactivation of CDKN1A (By similarity). Interacts with NR4A3 (PubMed:12709428). Interacts with ATF5; EP300 is required for ATF5 and CEBPB interaction and DNA binding (PubMed:24216764). Interacts with ZNF451 (By similarity). Interacts with HSF1 (By similarity). Interacts with ZBTB48/TZAP (By similarity). Interacts with STAT1; the interaction is enhanced upon IFN-gamma stimulation (By similarity). Interacts with HNRNPU (via C-terminus); this interaction enhances DNA-binding of HNRNPU to nuclear scaffold/matrix attachment region (S/MAR) elements (By similarity). Interacts with BCL11B (By similarity). Interacts with SMAD4; negatively regulated by ZBTB7A (By similarity). {ECO:0000250|UniProtKB:Q09472, ECO:0000269|PubMed:10593900, ECO:0000269|PubMed:10722728, ECO:0000269|PubMed:12709428, ECO:0000269|PubMed:14645221, ECO:0000269|PubMed:15601857, ECO:0000269|PubMed:16917507, ECO:0000269|PubMed:18486321, ECO:0000269|PubMed:19324970, ECO:0000269|PubMed:24216764, ECO:0000269|PubMed:9512516}. DOMAIN: The CRD1 domain (cell cycle regulatory domain 1) mediates transcriptional repression of a subset of p300 responsive genes; it can be de-repressed by CDKN1A/p21WAF1 at least at some promoters. It conatins sumoylation and acetylation sites and the same lysine residues may be targeted for the respective modifications. It is proposed that deacetylation by SIRT1 allows sumoylation leading to suppressed activity (By similarity). {ECO:0000250}. +Q9JKA5 GPA33_MOUSE Cell surface A33 antigen (Glycoprotein A33) (mA33) 319 35,692 Chain (1); Compositional bias (1); Disulfide bond (3); Domain (2); Glycosylation (4); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 236 256 Helical. {ECO:0000255}. TOPO_DOM 22 235 Extracellular. {ECO:0000255}.; TOPO_DOM 257 319 Cytoplasmic. {ECO:0000255}. FUNCTION: May play a role in cell-cell recognition and signaling. {ECO:0000250}. PTM: Palmitoylated. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. +Q9WTK3 GPAA1_MOUSE Glycosylphosphatidylinositol anchor attachment 1 protein (GPI anchor attachment protein 1) (GAA1 protein homolog) (mGAA1) 621 67,949 Chain (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 24 44 Helical. {ECO:0000255}.; TRANSMEM 368 388 Helical. {ECO:0000255}.; TRANSMEM 427 447 Helical. {ECO:0000255}.; TRANSMEM 458 478 Helical. {ECO:0000255}.; TRANSMEM 500 520 Helical. {ECO:0000255}.; TRANSMEM 543 563 Helical. {ECO:0000255}.; TRANSMEM 599 619 Helical. {ECO:0000255}. TOPO_DOM 1 23 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 45 367 Lumenal. {ECO:0000255}.; TOPO_DOM 389 426 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 448 457 Lumenal. {ECO:0000255}.; TOPO_DOM 479 499 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 521 542 Lumenal. {ECO:0000255}.; TOPO_DOM 564 598 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 620 621 Lumenal. {ECO:0000255}. Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis. FUNCTION: Essential for GPI-anchoring of precursor proteins but not for GPI synthesis. Acts before or during formation of the carbonyl intermediate. {ECO:0000269|PubMed:10793132, ECO:0000269|PubMed:10898732}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Forms a complex with PIGK/GPI8, PIGT, PIGU and PIGS. {ECO:0000269|PubMed:10793132}. TISSUE SPECIFICITY: Ubiquitously expressed in fetal and adult tissues. Expressed at higher levels in fetal tissues than adult tissues. In embryos abundant in the choroid plexus, skeletal muscle,. {ECO:0000269|PubMed:10898732}. +P84089 ERH_MOUSE Enhancer of rudimentary homolog (Mer) 104 12,259 Beta strand (5); Chain (1); Cross-link (1); Helix (3); Initiator methionine (1); Modified residue (2); Turn (2) FUNCTION: May have a role in the cell cycle. SUBUNIT: Homodimer (PubMed:15937287). Component of the methylosome, a 20S complex containing at least CLNS1A/pICln, PRMT5/SKB1, WDR77/MEP50, PRMT1 and ERH. Interacts with CHTOP (By similarity). {ECO:0000250|UniProtKB:P84090, ECO:0000269|PubMed:15937287}. +Q8C0N2 GPAT3_MOUSE Glycerol-3-phosphate acyltransferase 3 (GPAT-3) (EC 2.3.1.15) (1-acyl-sn-glycerol-3-phosphate O-acyltransferase 9) (1-AGP acyltransferase 9) (1-AGPAT 9) (EC 2.3.1.51) (Acyl-CoA:glycerol-3-phosphate acyltransferase 3) (mGPAT3) (Lysophosphatidic acid acyltransferase theta) (LPAAT-theta) 438 49,000 Chain (1); Modified residue (2); Motif (1); Transmembrane (3) TRANSMEM 14 34 Helical. {ECO:0000255}.; TRANSMEM 137 157 Helical. {ECO:0000255}.; TRANSMEM 161 181 Helical. {ECO:0000255}. Glycerolipid metabolism; triacylglycerol biosynthesis. Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 1/3. FUNCTION: May transfer the acyl-group from acyl-coA to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipid biosynthesis. Also transfers the acyl-group from acyl-coA to the sn-2 position of 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic acid, or LPA), forming 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid, or PA). {ECO:0000269|PubMed:17170135}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:17170135}; Multi-pass membrane protein {ECO:0000269|PubMed:17170135}. DOMAIN: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate. {ECO:0000250}. TISSUE SPECIFICITY: Most abundant in epididymal fat, followed by small intestine, brown adipose tissue, kidney, heart and colon. {ECO:0000269|PubMed:17170135}. +P51162 FABP6_MOUSE Gastrotropin (GT) (Fatty acid-binding protein 6) (Ileal lipid-binding protein) (ILBP) 128 14,486 Chain (1); Initiator methionine (1); Modified residue (1) FUNCTION: Binds to bile acids and is involved in enterohepatic bile acid metabolism. Required for efficient apical to basolateral transport of conjugated bile acids in ileal enterocytes (PubMed:23251388). Stimulates gastric acid and pepsinogen secretion (By similarity). {ECO:0000250|UniProtKB:P10289, ECO:0000269|PubMed:23251388}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P80020}. Membrane; Peripheral membrane protein {ECO:0000250|UniProtKB:P50119}; Cytoplasmic side {ECO:0000250|UniProtKB:P50119}. DOMAIN: Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior. Can bind at least two ligands per molecule, however, the stoichiometry is debated. {ECO:0000250|UniProtKB:P10289, ECO:0000250|UniProtKB:P51161}. TISSUE SPECIFICITY: Expressed in ovary granulosa and luteal cells. {ECO:0000269|PubMed:25754072}. +P12710 FABPL_MOUSE Fatty acid-binding protein, liver (14 kDa selenium-binding protein) (Fatty acid-binding protein 1) (Liver-type fatty acid-binding protein) (L-FABP) 127 14,246 Chain (1); Modified residue (14) FUNCTION: Plays a role in lipoprotein-mediated cholesterol uptake in hepatocytes. Binds cholesterol. Binds free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm. May be involved in intracellular lipid transport. {ECO:0000250|UniProtKB:P07148, ECO:0000250|UniProtKB:P82289}. SUBCELLULAR LOCATION: Cytoplasm. DOMAIN: Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior. {ECO:0000250}. +P11404 FABPH_MOUSE Fatty acid-binding protein, heart (Fatty acid-binding protein 3) (Heart-type fatty acid-binding protein) (H-FABP) (Mammary-derived growth inhibitor) (MDGI) 133 14,819 Binding site (2); Chain (1); Initiator methionine (1); Modified residue (6); Sequence conflict (2) FUNCTION: FABP are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters. SUBCELLULAR LOCATION: Cytoplasm. DOMAIN: Forms a beta-barrel structure that accommodates the hydrophobic ligand in its interior. {ECO:0000250}. +Q61160 FADD_MOUSE FAS-associated death domain protein (FAS-associating death domain-containing protein) (Mediator of receptor induced toxicity) (Protein FADD) 205 22,960 Chain (1); Domain (2); Helix (6); Modified residue (1); Sequence conflict (1) FUNCTION: Apoptotic adaptor molecule that recruits caspase-8 or caspase-10 to the activated Fas (CD95) or TNFR-1 receptors. The resulting aggregate called the death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation. Active caspase-8 initiates the subsequent cascade of caspases mediating apoptosis (By similarity). Involved in interferon-mediated antiviral immune response, playing a role in the positive regulation of interferon signaling (By similarity). {ECO:0000250}. PTM: Phosphorylated. SUBUNIT: Interacts with CFLAR, PEA15 and MBD4. When phosphorylated, part of a complex containing HIPK3 and FAS. May interact with MAVS/IPS1. Interacts with PIDD1 (By similarity). Interacts with FAS (By similarity). Interacts directly (via DED domain) with NOL3 (via CARD domain); inhibits death-inducing signaling complex (DISC) assembly by inhibiting the increase in FAS-FADD binding induced by FAS activation. {ECO:0000250, ECO:0000269|PubMed:15383280}. DOMAIN: Contains a death domain involved in the binding of the corresponding domain within Fas receptor. +Q3TC72 FAHD2_MOUSE Fumarylacetoacetate hydrolase domain-containing protein 2A (EC 3.-.-.-) 313 34,690 Chain (1); Metal binding (3); Modified residue (4); Sequence conflict (3) FUNCTION: May have hydrolase activity. {ECO:0000250}. +Q9WUD8 FAIM1_MOUSE Fas apoptotic inhibitory molecule 1 179 20,201 Beta strand (5); Chain (1); Initiator methionine (1); Modified residue (1); Sequence conflict (1); Turn (1) FUNCTION: Plays a role as an inducible effector molecule that mediates Fas resistance produced by surface Ig engagement in B cells. {ECO:0000269|PubMed:10075978}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19168072}. TISSUE SPECIFICITY: Widely expressed, with the highest levels in brain, thymus, kidney, and spleen. {ECO:0000269|PubMed:10075978}. +A1KXC4 FAIM3_MOUSE Fas apoptotic inhibitory molecule 3 (IgM Fc fragment receptor) (Regulator of Fas-induced apoptosis Toso) 422 47,471 Chain (1); Compositional bias (1); Disulfide bond (1); Domain (1); Modified residue (1); Sequence conflict (20); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 263 283 Helical. {ECO:0000255}. TOPO_DOM 18 262 Extracellular. {ECO:0000255}.; TOPO_DOM 284 422 Cytoplasmic. {ECO:0000255}. FUNCTION: May play a role in the immune system processes. Protects cells from FAS-, TNF alpha- and FADD-induced apoptosis without increasing expression of the inhibitors of apoptosis BCL2 and BCLXL. Seems to activate an inhibitory pathway that prevents CASP8 activation following FAS stimulation, rather than blocking apoptotic signals downstream. May inhibit FAS-induced apoptosis by preventing CASP8 processing through CFLAR up-regulation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:O60667}; Single-pass membrane protein {ECO:0000255}. DOMAIN: The Ig-like domain is required for the anti-apoptotic ability. {ECO:0000250}. +Q7TMV3 FAKD5_MOUSE FAST kinase domain-containing protein 5, mitochondrial 762 86,600 Chain (1); Domain (1); Erroneous initiation (2); Modified residue (2); Transit peptide (1) FUNCTION: Plays an important role in the processing of non-canonical mitochondrial mRNA precursors. {ECO:0000250|UniProtKB:Q7L8L6}. SUBCELLULAR LOCATION: Mitochondrion matrix, mitochondrion nucleoid {ECO:0000250|UniProtKB:Q7L8L6}. Note=Localizes to mitochondrial RNA granules found in close proximity to the mitochondrial nucleoids. {ECO:0000250|UniProtKB:Q7L8L6}. SUBUNIT: Found in a complex with GRSF1, DDX28, DHX30 and FASTKD2. Associates with the 12S mitochondrial rRNA (12S mt-rRNA). {ECO:0000250|UniProtKB:Q7L8L6}. TISSUE SPECIFICITY: Expression detected in spleen, testis, colon, heart, smooth muscle, kidney, brain, lung, liver, brown and white adipose tissue. {ECO:0000269|PubMed:20869947}. +P34152 FAK1_MOUSE Focal adhesion kinase 1 (FADK 1) (EC 2.7.10.2) (Focal adhesion kinase-related nonkinase) (FRNK) (Protein-tyrosine kinase 2) (p125FAK) (pp125FAK) 1090 123,537 Active site (1); Alternative sequence (11); Binding site (1); Chain (1); Compositional bias (2); Cross-link (1); Domain (2); Erroneous initiation (2); Helix (7); Initiator methionine (1); Modified residue (21); Mutagenesis (4); Nucleotide binding (2); Region (2); Sequence caution (1); Sequence conflict (9) FUNCTION: Non-receptor protein-tyrosine kinase that plays an essential role in regulating cell migration, adhesion, spreading, reorganization of the actin cytoskeleton, formation and disassembly of focal adhesions and cell protrusions, cell cycle progression, cell proliferation and apoptosis. Required for early embryonic development and placenta development. Required for embryonic angiogenesis, normal cardiomyocyte migration and proliferation, and normal heart development. Regulates axon growth and neuronal cell migration, axon branching and synapse formation; required for normal development of the nervous system. Plays a role in osteogenesis and differentiation of osteoblasts. Functions in integrin signal transduction, but also in signaling downstream of numerous growth factor receptors, G-protein coupled receptors (GPCR), EPHA2, netrin receptors and LDL receptors. Forms multisubunit signaling complexes with SRC and SRC family members upon activation; this leads to the phosphorylation of additional tyrosine residues, creating binding sites for scaffold proteins, effectors and substrates. Regulates numerous signaling pathways. Promotes activation of phosphatidylinositol 3-kinase and the AKT1 signaling cascade. Promotes activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling cascade. Promotes localized and transient activation of guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs), and thereby modulates the activity of Rho family GTPases. Signaling via CAS family members mediates activation of RAC1. Recruits the ubiquitin ligase MDM2 to P53/TP53 in the nucleus, and thereby regulates P53/TP53 activity, P53/TP53 ubiquitination and proteasomal degradation. Phosphorylates SRC; this increases SRC kinase activity. Phosphorylates ACTN1, ARHGEF7, GRB7, RET and WASL. Promotes phosphorylation of PXN and STAT1; most likely PXN and STAT1 are phosphorylated by a SRC family kinase that is recruited to autophosphorylated PTK2/FAK1, rather than by PTK2/FAK1 itself. Promotes phosphorylation of BCAR1; GIT2 and SHC1; this requires both SRC and PTK2/FAK1. Promotes phosphorylation of BMX and PIK3R1. Isoform 9 (FRNK) does not contain a kinase domain and inhibits PTK2/FAK1 phosphorylation and signaling. Its enhanced expression can attenuate the nuclear accumulation of LPXN and limit its ability to enhance serum response factor (SRF)-dependent gene transcription (By similarity). {ECO:0000250, ECO:0000269|PubMed:10373530, ECO:0000269|PubMed:10806474, ECO:0000269|PubMed:11278462, ECO:0000269|PubMed:11369769, ECO:0000269|PubMed:12702722, ECO:0000269|PubMed:12941275, ECO:0000269|PubMed:15967814, ECO:0000269|PubMed:16000375, ECO:0000269|PubMed:16391003, ECO:0000269|PubMed:17093062, ECO:0000269|PubMed:18206965, ECO:0000269|PubMed:19147981, ECO:0000269|PubMed:19473962, ECO:0000269|PubMed:22056317, ECO:0000269|PubMed:7478517, ECO:0000269|PubMed:7997267, ECO:0000269|PubMed:9148935}. PTM: Phosphorylated on tyrosine residues upon activation, e.g. upon integrin signaling. Tyr-428 is the major autophosphorylation site, but other kinases can also phosphorylate this residue. Phosphorylation at Tyr-428 promotes interaction with SRC and SRC family members, leading to phosphorylation at Tyr-614, Tyr-615 and at additional tyrosine residues. FGR promotes phosphorylation at Tyr-428 and Tyr-614. FER promotes phosphorylation at Tyr-615, Tyr-899 and Tyr-963, even when cells are not adherent. Tyr-428, Tyr-614 and Ser-760 are phosphorylated only when cells are adherent. Phosphorylation at Tyr-428 is important for interaction with BMX, PIK3R1 and SHC1. Phosphorylation at Tyr-963 is important for interaction with GRB2. Dephosphorylated by PTPN11; PTPN11 is recruited to PTK2 via EPHA2 (tyrosine phosphorylated). Microtubule-induced dephosphorylation at Tyr-428 is crucial for the induction of focal adhesion disassembly; this dephosphorylation could be catalyzed by PTPN11 and regulated by ZFYVE21. {ECO:0000269|PubMed:10373530, ECO:0000269|PubMed:10806474, ECO:0000269|PubMed:11420674, ECO:0000269|PubMed:12941275, ECO:0000269|PubMed:14676198, ECO:0000269|PubMed:1528852, ECO:0000269|PubMed:7529876, ECO:0000269|PubMed:7997267, ECO:0000269|PubMed:8816475, ECO:0000269|PubMed:8824286, ECO:0000269|PubMed:9148935, ECO:0000269|Ref.6}.; PTM: Sumoylated; this enhances autophosphorylation. {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, focal adhesion. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, perinuclear region. Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Nucleus {ECO:0000250}. Note=Constituent of focal adhesions. Detected at microtubules. SUBUNIT: Interacts with GIT1. Component of a complex that contains at least FER, CTTN and PTK2/FAK1. Interacts with BMX. Interacts with STEAP4. Interacts with ZFYVE21. Interacts with ESR1. Interacts with FGR, FLT4 and RET. Interacts with EPHA2 in resting cells; activation of EPHA2 recruits PTPN11, leading to dephosphorylation of PTK2/FAK1 and dissociation of the complex. Interacts with EPHA1 (kinase activity-dependent) (By similarity). Interacts with MISP (By similarity). Interacts with PIAS1. Interacts with ARHGAP26 and SHC1. Interacts with RB1CC1; this inhibits PTK2/FAK1 activity and activation of downstream signaling pathways. Interacts with P53/TP53. Interacts with STAT1. Interacts with WASL. Interacts with ARHGEF7. Interacts with DCC. Interacts (via first Pro-rich region) with CAS family members (via SH3 domain), including BCAR1, BCAR3, CASS4 and NEDD9. Interacts with SORBS1. Interacts with ARHGEF28. Interacts with SHB. Interacts with PXN and TLN1. Interacts with TGFB1I1. Interacts with PIK3R1 or PIK3R2. Interacts with SRC, GRB2 and GRB7. Interacts with LPXN (via LD motif 3). Interacts with CD36. Interacts with EMP2; regulates PTK2 activation and localization (By similarity). {ECO:0000250|UniProtKB:Q05397, ECO:0000269|PubMed:10896938, ECO:0000269|PubMed:11278462, ECO:0000269|PubMed:11799401, ECO:0000269|PubMed:12221124, ECO:0000269|PubMed:12464388, ECO:0000269|PubMed:12674328, ECO:0000269|PubMed:12702722, ECO:0000269|PubMed:14500712, ECO:0000269|PubMed:14676198, ECO:0000269|PubMed:15494733, ECO:0000269|PubMed:15494734, ECO:0000269|PubMed:17093062, ECO:0000269|PubMed:18206965, ECO:0000269|PubMed:19473962, ECO:0000269|PubMed:7622520, ECO:0000269|PubMed:7997267, ECO:0000269|PubMed:8816475, ECO:0000269|PubMed:8824286, ECO:0000269|PubMed:9148935, ECO:0000269|PubMed:9422762, ECO:0000269|PubMed:9461600, ECO:0000269|PubMed:9756887}. DOMAIN: The first Pro-rich domain interacts with the SH3 domain of CAS family members, such as BCAR1 and NEDD9.; DOMAIN: The C-terminal region is the site of focal adhesion targeting (FAT) sequence which mediates the localization of FAK1 to focal adhesions. +Q9D8T0 FAM3A_MOUSE Protein FAM3A 230 25,394 Chain (1); Disulfide bond (2); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +O35242 FAN_MOUSE Protein FAN (Factor associated with neutral sphingomyelinase activation) (Factor associated with N-SMase activation) 920 104,546 Chain (1); Domain (3); Repeat (6); Sequence conflict (3) FUNCTION: Couples the p55 TNF-receptor (TNF-R55 / TNFR1) to neutral sphingomyelinase (N-SMASE). Specifically binds to the N-smase activation domain of TNF-R55. May regulate ceramide production by N-SMASE. +Q3UN58 FAP20_MOUSE Fanconi anemia core complex-associated protein 20 (FANCA-associated protein of 20 kDa) (Fanconi anemia-associated protein of 20 kDa) 186 20,038 Alternative sequence (2); Chain (1); Modified residue (1); Sequence conflict (1); Zinc finger (1) FUNCTION: Component of the Fanconi anemia (FA) complex required to recruit the FA complex to DNA interstrand cross-links (ICLs) and promote ICLs repair. Following DNA damage recognizes and binds 'Lys-63'-linked ubiquitin generated by RNF8 at ICLs and recruits other components of the FA complex. Promotes translesion synthesis via interaction with REV1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6NZ36}. Chromosome {ECO:0000250|UniProtKB:Q6NZ36}. Note=Following DNA damage, recruited to DNA interstrand cross-links (ICLs) sites by binding to ubiquitin generated by RNF8. {ECO:0000250|UniProtKB:Q6NZ36}. SUBUNIT: Component of the Fanconi anemia (FA) complex. Interacts with FANCA; interaction is direct. Interacts with REV1 (By similarity). {ECO:0000250}. DOMAIN: The UBZ-type zinc finger binds both 'Lys-48'- and 'Lys-63'-linked polyubiquitin with preference for 'Lys-63'-linked polyubiquitin. {ECO:0000250}. +Q9JIX9 FASTK_MOUSE Fas-activated serine/threonine kinase (FAST kinase) (EC 2.7.11.8) 511 57,726 Chain (1); Domain (1) FUNCTION: Phosphorylates the splicing regulator TIA1, thereby promoting the inclusion of FAS exon 6, which leads to an mRNA encoding a pro-apoptotic form of the receptor (By similarity). Required for the biogenesis of some mitochondrial-encoded mRNAs, specifically stabilizes ND6 (NADH dehydrogenase complex subunit 6) mRNA, and regulates its levels. {ECO:0000250|UniProtKB:Q14296, ECO:0000269|PubMed:25704814}. PTM: Autophosphorylated on serine/threonine residues. Activated by dephosphorylation (By similarity). {ECO:0000250|UniProtKB:Q14296}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:25704814}. Note=Colocalizes with mitochondrial RNA granules. {ECO:0000269|PubMed:25704814}. SUBUNIT: Interacts with TIA-1 and TIAR. {ECO:0000250|UniProtKB:Q14296}. DOMAIN: The RAP domain is essential for RNA-binding. {ECO:0000269|PubMed:25704814}. +P19096 FAS_MOUSE Fatty acid synthase (EC 2.3.1.85) [Includes: [Acyl-carrier-protein] S-acetyltransferase (EC 2.3.1.38); [Acyl-carrier-protein] S-malonyltransferase (EC 2.3.1.39); 3-oxoacyl-[acyl-carrier-protein] synthase (EC 2.3.1.41); 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100); 3-hydroxyacyl-[acyl-carrier-protein] dehydratase (EC 4.2.1.59); Enoyl-[acyl-carrier-protein] reductase (EC 1.3.1.39); Oleoyl-[acyl-carrier-protein] hydrolase (EC 3.1.2.14)] 2504 272,428 Active site (5); Beta strand (27); Chain (1); Cross-link (1); Domain (1); Frameshift (1); Helix (46); Modified residue (25); Nucleotide binding (2); Region (5); Sequence conflict (6); Turn (9) FUNCTION: Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. This multifunctional protein has 7 catalytic activities as an acyl carrier protein. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Melanosome {ECO:0000250}. SUBUNIT: Homodimer which is arranged in a head to tail fashion (By similarity). Interacts with CEACAM1; this interaction is insulin and phosphorylation-dependent; reduces fatty-acid synthase activity (By similarity). {ECO:0000250|UniProtKB:P12785, ECO:0000250|UniProtKB:P49327}. +Q5F226 FAT2_MOUSE Protocadherin Fat 2 (FAT tumor suppressor homolog 2) 4351 480,109 Chain (1); Compositional bias (2); Disulfide bond (7); Domain (36); Glycosylation (37); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 4051 4071 Helical. {ECO:0000255}. TOPO_DOM 19 4050 Extracellular. {ECO:0000255}.; TOPO_DOM 4072 4351 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in the regulation of cell migration (By similarity). May be involved in mediating the organization of the parallel fibers of granule cells during cerebellar development (By similarity). {ECO:0000250|UniProtKB:O88277, ECO:0000250|UniProtKB:Q9NYQ8}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Cell junction {ECO:0000250|UniProtKB:Q9NYQ8}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:O88277}. Note=Localized at adhesion zippers (early state of adherens junctions) of keratinocytes. {ECO:0000250|UniProtKB:Q9NYQ8}. SUBUNIT: Homodimer. {ECO:0000250}. +Q8CEK7 FATE1_MOUSE Fetal and adult testis-expressed transcript protein homolog 99 11,726 Chain (1); Transmembrane (1) TRANSMEM 79 98 Helical. {ECO:0000255}. FUNCTION: Involved in the regulation of endoplasmic reticulum (ER)-mitochondria coupling. Negatively regulates the ER-mitochondria distance and Ca(2+) transfer from ER to mitochondria possibly implicating it in the regulation of apoptosis. May collaborate with RNF183 to restrain BIK protein levels thus regulating apoptotic signaling. {ECO:0000250|UniProtKB:Q969F0}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q969F0}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q969F0}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q969F0}; Single-pass membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000250|UniProtKB:Q969F0}. Note=Localized to specific membrane structures termed mitochondria-associated membranes (MAMs) which connect the endoplasmic reticulum (ER) and the mitochondria. Also associated with the outer surface of mitochondria at sites that are not in close contact with the ER. {ECO:0000250|UniProtKB:Q969F0}. SUBUNIT: Interacts with BIK and RNF183. Interacts with IMMT/MIC60and EMD. {ECO:0000250|UniProtKB:Q969F0}. +P35412 GPR12_MOUSE G-protein coupled receptor 12 (GPCR01) 334 36,589 Chain (1); Glycosylation (2); Lipidation (1); Modified residue (2); Topological domain (8); Transmembrane (7) TRANSMEM 49 69 Helical; Name=1. {ECO:0000255}.; TRANSMEM 79 99 Helical; Name=2. {ECO:0000255}.; TRANSMEM 114 134 Helical; Name=3. {ECO:0000255}.; TRANSMEM 159 179 Helical; Name=4. {ECO:0000255}.; TRANSMEM 200 220 Helical; Name=5. {ECO:0000255}.; TRANSMEM 253 273 Helical; Name=6. {ECO:0000255}.; TRANSMEM 283 303 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 48 Extracellular. {ECO:0000255}.; TOPO_DOM 70 78 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 100 113 Extracellular. {ECO:0000255}.; TOPO_DOM 135 158 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 180 199 Extracellular. {ECO:0000255}.; TOPO_DOM 221 252 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 274 282 Extracellular. {ECO:0000255}.; TOPO_DOM 304 334 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor with constitutive G(s) signaling activity that stimulates cyclic AMP production (By similarity). Promotes neurite outgrowth and blocks myelin inhibition in neurons. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed predominantly in the forebrain and a lesser extent in the hindbrain. Lower expression in the liver. +Q0VDU3 GPR15_MOUSE G-protein coupled receptor 15 360 40,542 Chain (1); Sequence conflict (6); Topological domain (8); Transmembrane (7) TRANSMEM 34 54 Helical; Name=1. {ECO:0000255}.; TRANSMEM 70 90 Helical; Name=2. {ECO:0000255}.; TRANSMEM 121 141 Helical; Name=3. {ECO:0000255}.; TRANSMEM 150 170 Helical; Name=4. {ECO:0000255}.; TRANSMEM 193 213 Helical; Name=5. {ECO:0000255}.; TRANSMEM 240 260 Helical; Name=6. {ECO:0000255}.; TRANSMEM 285 305 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 33 Extracellular. {ECO:0000255}.; TOPO_DOM 55 69 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 91 120 Extracellular. {ECO:0000255}.; TOPO_DOM 142 149 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 171 192 Extracellular. {ECO:0000255}.; TOPO_DOM 214 239 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 261 284 Extracellular. {ECO:0000255}.; TOPO_DOM 306 360 Cytoplasmic. {ECO:0000255}. FUNCTION: Probable chemokine receptor. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q6NS65 GPR17_MOUSE Uracil nucleotide/cysteinyl leukotriene receptor (UDP/CysLT receptor) (G-protein coupled receptor 17) 339 37,839 Chain (1); Disulfide bond (1); Glycosylation (2); Topological domain (8); Transmembrane (7) TRANSMEM 37 57 Helical; Name=1. {ECO:0000255}.; TRANSMEM 65 85 Helical; Name=2. {ECO:0000255}.; TRANSMEM 106 126 Helical; Name=3. {ECO:0000255}.; TRANSMEM 148 168 Helical; Name=4. {ECO:0000255}.; TRANSMEM 196 216 Helical; Name=5. {ECO:0000255}.; TRANSMEM 233 253 Helical; Name=6. {ECO:0000255}.; TRANSMEM 281 301 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 36 Extracellular. {ECO:0000255}.; TOPO_DOM 58 64 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 86 105 Extracellular. {ECO:0000255}.; TOPO_DOM 127 147 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 169 195 Extracellular. {ECO:0000255}.; TOPO_DOM 217 232 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 254 280 Extracellular. {ECO:0000255}.; TOPO_DOM 302 339 Cytoplasmic. {ECO:0000255}. FUNCTION: Dual specificity receptor for uracil nucleotides and cysteinyl leukotrienes (CysLTs). Signals through G(i) and inhibition of adenylyl cyclase. May mediate brain damage by nucleotides and CysLTs following ischemia (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein {ECO:0000305}. +Q8K1Z6 GPR18_MOUSE N-arachidonyl glycine receptor (NAGly receptor) (G-protein coupled receptor 18) 331 37,691 Chain (1); Disulfide bond (1); Glycosylation (2); Modified residue (1); Sequence conflict (1); Topological domain (8); Transmembrane (7) TRANSMEM 27 47 Helical; Name=1. {ECO:0000255}.; TRANSMEM 57 77 Helical; Name=2. {ECO:0000255}.; TRANSMEM 96 116 Helical; Name=3. {ECO:0000255}.; TRANSMEM 139 159 Helical; Name=4. {ECO:0000255}.; TRANSMEM 192 212 Helical; Name=5. {ECO:0000255}.; TRANSMEM 237 257 Helical; Name=6. {ECO:0000255}.; TRANSMEM 269 289 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 26 Extracellular. {ECO:0000255}.; TOPO_DOM 48 56 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 78 95 Extracellular. {ECO:0000255}.; TOPO_DOM 117 138 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 160 191 Extracellular. {ECO:0000255}.; TOPO_DOM 213 236 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 258 268 Extracellular. {ECO:0000255}.; TOPO_DOM 290 331 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for endocannabinoid N-arachidonyl glycine (NAGly) (By similarity). However, conflicting results about the role of NAGly as an agonist are reported (PubMed:23104136). Can also be activated by plant-derived and synthetic cannabinoid agonists (By similarity). The activity of this receptor is mediated by G proteins which inhibit adenylyl cyclase (By similarity). May contribute to regulation of the immune system (By similarity). Is required for normal homeostasis of CD8+ subsets of intraepithelial lymphocytes (IELs) (CD8alphaalpha and CD8alphabeta IELs) in small intstine by supporting preferential migration of CD8alphaalpha T-cells to intraepithelial compartment over lamina propria compartment, and by mediating their reconstitution into small intestine after bone marrow transplant (PubMed:25348153, PubMed:26197390). Plays a role in hypotensive responses, mediating reduction in intraocular and blood pressure (PubMed:23461720, PubMed:27893106). Mediates NAGly-induced process of reorganization of actin filaments and induction of acrosomal exocytosis (By similarity). {ECO:0000250|UniProtKB:Q14330, ECO:0000269|PubMed:23104136, ECO:0000269|PubMed:23461720, ECO:0000269|PubMed:25348153, ECO:0000269|PubMed:26197390, ECO:0000269|PubMed:27893106}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23104136}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q14330}. TISSUE SPECIFICITY: Expressed in the eye including cornea, retina, iris and ciliary epithelium (at protein level) (PubMed:23461720). Expressed in spleen, liver and lymphocytes with highest expression levels in intestinal intraepithelial lymphocytes (PubMed:25348153, PubMed:26197390). {ECO:0000269|PubMed:23461720, ECO:0000269|PubMed:25348153, ECO:0000269|PubMed:26197390}. +Q61121 GPR19_MOUSE Probable G-protein coupled receptor 19 415 47,533 Alternative sequence (1); Chain (1); Disulfide bond (1); Glycosylation (2); Sequence conflict (3); Topological domain (8); Transmembrane (7) TRANSMEM 70 90 Helical; Name=1.; TRANSMEM 103 123 Helical; Name=2.; TRANSMEM 153 173 Helical; Name=3.; TRANSMEM 183 203 Helical; Name=4.; TRANSMEM 222 242 Helical; Name=5.; TRANSMEM 278 298 Helical; Name=6.; TRANSMEM 310 332 Helical; Name=7. TOPO_DOM 1 69 Extracellular. {ECO:0000255}.; TOPO_DOM 91 102 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 124 152 Extracellular. {ECO:0000255}.; TOPO_DOM 174 182 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 204 221 Extracellular. {ECO:0000255}.; TOPO_DOM 243 277 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 299 309 Extracellular. {ECO:0000255}.; TOPO_DOM 333 415 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q8K087 GPR1_MOUSE G-protein coupled receptor 1 353 40,951 Chain (1); Disulfide bond (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 42 62 Helical; Name=1. {ECO:0000255}.; TRANSMEM 74 94 Helical; Name=2. {ECO:0000255}.; TRANSMEM 113 133 Helical; Name=3. {ECO:0000255}.; TRANSMEM 155 175 Helical; Name=4. {ECO:0000255}.; TRANSMEM 211 231 Helical; Name=5. {ECO:0000255}.; TRANSMEM 248 268 Helical; Name=6. {ECO:0000255}.; TRANSMEM 287 307 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 41 Extracellular. {ECO:0000255}.; TOPO_DOM 63 73 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 95 112 Extracellular. {ECO:0000255}.; TOPO_DOM 134 154 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 176 210 Extracellular. {ECO:0000255}.; TOPO_DOM 232 247 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 269 286 Extracellular. {ECO:0000255}.; TOPO_DOM 308 353 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for the inflammation-associated leukocyte chemoattractant chemerin/RARRES2 suggesting a role for this receptor in the regulation of inflammation. Can act as a coreceptor for HIV-1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q5U431 GPR39_MOUSE G-protein coupled receptor 39 456 51,589 Chain (1); Disulfide bond (2); Glycosylation (2); Metal binding (2); Modified residue (1); Topological domain (8); Transmembrane (7) TRANSMEM 35 55 Helical; Name=1. {ECO:0000250|UniProtKB:P20789}.; TRANSMEM 70 89 Helical; Name=2. {ECO:0000250|UniProtKB:P20789}.; TRANSMEM 110 131 Helical; Name=3. {ECO:0000250|UniProtKB:P20789}.; TRANSMEM 152 172 Helical; Name=4. {ECO:0000250|UniProtKB:P20789}.; TRANSMEM 218 242 Helical; Name=5. {ECO:0000250|UniProtKB:P20789}.; TRANSMEM 284 305 Helical; Name=6. {ECO:0000250|UniProtKB:P20789}.; TRANSMEM 324 344 Helical; Name=7. {ECO:0000250|UniProtKB:P20789}. TOPO_DOM 1 34 Extracellular. {ECO:0000250|UniProtKB:P20789}.; TOPO_DOM 56 69 Cytoplasmic. {ECO:0000250|UniProtKB:P20789}.; TOPO_DOM 90 109 Extracellular. {ECO:0000250|UniProtKB:P20789}.; TOPO_DOM 132 151 Cytoplasmic. {ECO:0000250|UniProtKB:P20789}.; TOPO_DOM 173 217 Extracellular. {ECO:0000250|UniProtKB:P20789}.; TOPO_DOM 243 283 Cytoplasmic. {ECO:0000250|UniProtKB:P20789}.; TOPO_DOM 306 323 Extracellular. {ECO:0000250|UniProtKB:P20789}.; TOPO_DOM 345 456 Cytoplasmic. {ECO:0000250|UniProtKB:P20789}. FUNCTION: Zn(2+) acts as an agonist (By similarity). This receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. Its effect is mediated mainly through G(q)-alpha and G(12)/G(13) proteins. Involved in regulation of body weight, gastrointestinal mobility, hormone secretion and cell death. {ECO:0000250, ECO:0000269|PubMed:17030183, ECO:0000269|PubMed:18180304}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expression is detected in septumamygdala, parietal cells, enterocytes, neurons and pancreas, in peripheral organs such as the duodenum and kidney but not in the pituitary and hypothalamus. {ECO:0000269|PubMed:16959833, ECO:0000269|PubMed:17030183}. +P35413 GPR3_MOUSE G-protein coupled receptor 3 (GPCR21) 330 35,453 Chain (1); Glycosylation (1); Lipidation (1); Modified residue (3); Topological domain (8); Transmembrane (7) TRANSMEM 43 62 Helical; Name=1. {ECO:0000255}.; TRANSMEM 75 98 Helical; Name=2. {ECO:0000255}.; TRANSMEM 111 132 Helical; Name=3. {ECO:0000255}.; TRANSMEM 154 173 Helical; Name=4. {ECO:0000255}.; TRANSMEM 199 217 Helical; Name=5. {ECO:0000255}.; TRANSMEM 246 272 Helical; Name=6. {ECO:0000255}.; TRANSMEM 278 299 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 42 Extracellular. {ECO:0000255}.; TOPO_DOM 63 74 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 99 110 Extracellular. {ECO:0000255}.; TOPO_DOM 133 153 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 174 198 Extracellular. {ECO:0000255}.; TOPO_DOM 218 245 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 273 277 Extracellular. {ECO:0000255}.; TOPO_DOM 300 330 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan receptor with constitutive G(s) signaling activity that activate cyclic AMP. Has a potential role in modulating a number of brain functions, including behavioral responses to stress, amyloid-beta peptide generation in neurons (By similarity) and neurite outgrowth (By similarity). Maintains also meiotic arrest in oocytes. {ECO:0000250, ECO:0000269|PubMed:15956199, ECO:0000269|PubMed:19259266}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed in both the forebrain and hindbrain, with the highest level in habenula. Lower level expression in the testis. Highly expressed in regions. {ECO:0000269|PubMed:19259266, ECO:0000269|PubMed:8262253}. +Q9EQQ4 GPR45_MOUSE Probable G-protein coupled receptor 45 (PSP24-1) (PSP24-alpha) 373 42,358 Chain (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 39 59 Helical; Name=1. {ECO:0000255}.; TRANSMEM 76 96 Helical; Name=2. {ECO:0000255}.; TRANSMEM 110 130 Helical; Name=3. {ECO:0000255}.; TRANSMEM 150 170 Helical; Name=4. {ECO:0000255}.; TRANSMEM 199 219 Helical; Name=5. {ECO:0000255}.; TRANSMEM 270 290 Helical; Name=6. {ECO:0000255}.; TRANSMEM 307 327 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 38 Extracellular. {ECO:0000255}.; TOPO_DOM 60 75 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 97 109 Extracellular. {ECO:0000255}.; TOPO_DOM 131 149 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 171 198 Extracellular. {ECO:0000255}.; TOPO_DOM 220 269 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 291 306 Extracellular. {ECO:0000255}.; TOPO_DOM 328 373 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan receptor. May play a role in brain function. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Brain specific. +Q8BUD0 GPR4_MOUSE G-protein coupled receptor 4 365 41,105 Chain (1); Disulfide bond (1); Glycosylation (2); Topological domain (8); Transmembrane (7) TRANSMEM 25 45 Helical; Name=1. {ECO:0000255}.; TRANSMEM 56 76 Helical; Name=2. {ECO:0000255}.; TRANSMEM 95 115 Helical; Name=3. {ECO:0000255}.; TRANSMEM 136 156 Helical; Name=4. {ECO:0000255}.; TRANSMEM 180 200 Helical; Name=5. {ECO:0000255}.; TRANSMEM 227 247 Helical; Name=6. {ECO:0000255}.; TRANSMEM 274 291 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 24 Extracellular. {ECO:0000255}.; TOPO_DOM 46 55 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 77 94 Extracellular. {ECO:0000255}.; TOPO_DOM 116 135 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 157 179 Extracellular. {ECO:0000255}.; TOPO_DOM 201 226 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 248 273 Extracellular. {ECO:0000255}.; TOPO_DOM 292 365 Cytoplasmic. {ECO:0000255}. FUNCTION: Proton-sensing receptor coupled to several G-proteins, including G(s), G(13) and G(q)/G(11) proteins, leading to cAMP production. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +P0C5J4 GPR52_MOUSE G-protein coupled receptor 52 361 41,343 Chain (1); Disulfide bond (1); Glycosylation (3); Topological domain (8); Transmembrane (7) TRANSMEM 45 65 Helical; Name=1. {ECO:0000255}.; TRANSMEM 82 102 Helical; Name=2. {ECO:0000255}.; TRANSMEM 116 136 Helical; Name=3. {ECO:0000255}.; TRANSMEM 160 180 Helical; Name=4. {ECO:0000255}.; TRANSMEM 206 226 Helical; Name=5. {ECO:0000255}.; TRANSMEM 266 286 Helical; Name=6. {ECO:0000255}.; TRANSMEM 297 317 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 44 Extracellular. {ECO:0000255}.; TOPO_DOM 66 81 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 103 115 Extracellular. {ECO:0000255}.; TOPO_DOM 137 159 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 181 205 Extracellular. {ECO:0000255}.; TOPO_DOM 227 265 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 287 296 Extracellular. {ECO:0000255}.; TOPO_DOM 318 361 Cytoplasmic. {ECO:0000255}. FUNCTION: G- protein coupled receptor activated by antipsychotics reserpine leading to an increase in intracellular cAMP and its internalization (By similarity). May play a role in locomotor activity through modulation of dopamine, NMDA and ADORA2A-induced locomotor activity. These behavioral changes are accompanied by modulation of the dopamine receptor signaling pathway in striatum (PubMed:24587241, PubMed:28583861). Modulates HTT level via cAMP-dependent but PKA independent mechanisms throught activation of RAB39B that translocates HTT to the endoplasmic reticulum, thus avoiding proteasome degradation (PubMed:25738228). {ECO:0000250|UniProtKB:Q9Y2T5, ECO:0000269|PubMed:24587241, ECO:0000269|PubMed:25738228, ECO:0000269|PubMed:28583861}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed in brain, especially in striatum (PubMed:24587241). Expressed in the striatum, nucleus accumbens, and lateral globus pallidus (PubMed:28583861). {ECO:0000269|PubMed:24587241, ECO:0000269|PubMed:28583861}. +Q3UJF0 GPR55_MOUSE G-protein coupled receptor 55 327 38,090 Chain (1); Glycosylation (2); Sequence conflict (1); Topological domain (8); Transmembrane (7) TRANSMEM 21 41 Helical; Name=1. {ECO:0000255}.; TRANSMEM 58 78 Helical; Name=2. {ECO:0000255}.; TRANSMEM 94 114 Helical; Name=3. {ECO:0000255}.; TRANSMEM 137 157 Helical; Name=4. {ECO:0000255}.; TRANSMEM 180 200 Helical; Name=5. {ECO:0000255}.; TRANSMEM 240 260 Helical; Name=6. {ECO:0000255}.; TRANSMEM 280 300 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 20 Extracellular. {ECO:0000255}.; TOPO_DOM 42 57 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 79 93 Extracellular. {ECO:0000255}.; TOPO_DOM 115 136 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 158 179 Extracellular. {ECO:0000255}.; TOPO_DOM 201 239 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 261 279 Extracellular. {ECO:0000255}.; TOPO_DOM 301 327 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for L-alpha-lysophosphatidylinositol (LPI). LPI induces Ca(2+) release from intracellular stores via the heterotrimeric G protein GNA13 and RHOA (By similarity). Putative cannabinoid receptor (By similarity). May play a role in bone physiology by regulating osteoclast number and function (By similarity). May be involved in hyperalgesia associated with inflammatory and neuropathic pain. {ECO:0000250, ECO:0000269|PubMed:18502582}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q8C010 GPR61_MOUSE G-protein coupled receptor 61 449 49,382 Chain (1); Glycosylation (1); Sequence conflict (1); Topological domain (8); Transmembrane (7) TRANSMEM 45 67 Helical; Name=1. {ECO:0000255}.; TRANSMEM 76 98 Helical; Name=2. {ECO:0000255}.; TRANSMEM 113 135 Helical; Name=3. {ECO:0000255}.; TRANSMEM 156 178 Helical; Name=4. {ECO:0000255}.; TRANSMEM 207 229 Helical; Name=5. {ECO:0000255}.; TRANSMEM 288 310 Helical; Name=6. {ECO:0000255}.; TRANSMEM 325 344 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 44 Extracellular. {ECO:0000255}.; TOPO_DOM 68 75 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 99 112 Extracellular. {ECO:0000255}.; TOPO_DOM 136 155 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 179 206 Extracellular. {ECO:0000255}.; TOPO_DOM 230 287 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 311 324 Extracellular. {ECO:0000255}.; TOPO_DOM 345 449 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan G-protein coupled receptor. Constitutively activates the G(s)-alpha/cAMP signaling pathway (By similarity). Shows a reciprocal regulatory interaction with the melatonin receptor MTNR1B most likely through receptor heteromerization (By similarity). May be involved in the regulation of food intake and body weight (PubMed:21971119). {ECO:0000250|UniProtKB:Q9BZJ8, ECO:0000269|PubMed:21971119}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9BZJ8}; Multi-pass membrane protein {ECO:0000255}. Endosome membrane {ECO:0000250|UniProtKB:Q9BZJ8}; Multi-pass membrane protein {ECO:0000255}. Note=Colocalizes with ARRB2/beta-arrestin-2 in the endosome (By similarity). {ECO:0000250|UniProtKB:Q9BZJ8}. SUBUNIT: Forms heterodimer with MTNR1B. Interacts with ARRB1 and ARRB2 in a spontaneous and agonist-independent manner; leading to the internalization of GPR61 in the endosomal compartment (By similarity). {ECO:0000250|UniProtKB:Q9BZJ8}. TISSUE SPECIFICITY: Predominantly expressed in the brain and testes, with relatively lower expression observed in the eye, adrenal gland and pituitary gland. {ECO:0000269|PubMed:21971119, ECO:0000269|PubMed:28912303}. +Q08879 FBLN1_MOUSE Fibulin-1 (FIBL-1) (Basement-membrane protein 90) (BM-90) 705 78,033 Alternative sequence (1); Chain (1); Disulfide bond (35); Domain (12); Glycosylation (3); Region (1); Sequence conflict (7); Signal peptide (1) FUNCTION: Incorporated into fibronectin-containing matrix fibers. May play a role in cell adhesion and migration along protein fibers within the extracellular matrix (ECM). Could be important for certain developmental processes and contribute to the supramolecular organization of ECM architecture, in particular to those of basement membranes. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SUBUNIT: Homomultimerizes and interacts with various extracellular matrix components such as FN1, LAMA1, LMA2, NID, ACAN, CSPG2 and type IV collagen. Binding analysis demonstrated for isoform C a 100-fold stronger binding to the basement membrane protein NID than for isoform D. Interacts with FBLN7. Interacts with CCN3 (By similarity). {ECO:0000250|UniProtKB:P23142, ECO:0000269|PubMed:10022829, ECO:0000269|PubMed:10400671, ECO:0000269|PubMed:11589703, ECO:0000269|PubMed:17699513}. TISSUE SPECIFICITY: Detected in most organs (brain, heart, lung, spleen, liver and kidney). Neurons are the predominant source of production in the brain. Not expressed significantly by astrocytes or microglia. {ECO:0000269|PubMed:11238726}. +Q9WVH9 FBLN5_MOUSE Fibulin-5 (FIBL-5) (Developmental arteries and neural crest EGF-like protein) (Dance) 448 50,193 Chain (1); Disulfide bond (17); Domain (6); Glycosylation (2); Motif (1); Signal peptide (1) FUNCTION: Essential for elastic fiber formation, is involved in the assembly of continuous elastin (ELN) polymer and promotes the interaction of microfibrils and ELN (By similarity). Stabilizes and organizes elastic fibers in the skin, lung and vasculature. Promotes adhesion of endothelial cells through interaction of integrins and the RGD motif. Vascular ligand for integrin receptors which may play a role in vascular development and remodeling (PubMed:11805835). May act as an adapter that mediates the interaction between FBN1 and ELN (By similarity). {ECO:0000250|UniProtKB:Q9UBX5, ECO:0000269|PubMed:11805835}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9UBX5}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9UBX5}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q9UBX5}. Note=co-localizes with ELN in elastic fibers. {ECO:0000250|UniProtKB:Q9UBX5}. SUBUNIT: Homodimer. Monomer, homodimerizes in presence of Ca(2+). Interacts with ELN (By similarity). Interacts (via N-terminus) with the integrins ITGAV/ITGB3, ITGAV/ITGB5 and ITGA9/ITGB1 (PubMed:11805835). Interacts with FBN1 (via N-terminal domain). Forms a ternary complex with ELN and FBN1 (By similarity). {ECO:0000250|UniProtKB:Q9UBX5, ECO:0000269|PubMed:11805835}. +Q9QZM9 FBX16_MOUSE F-box only protein 16 334 38,987 Chain (1); Domain (1); Sequence conflict (1) FUNCTION: Probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex. {ECO:0000250}. +Q9CQ24 FBX36_MOUSE F-box only protein 36 188 22,075 Chain (1); Domain (1) FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. {ECO:0000250}. SUBUNIT: Directly interacts with SKP1 and CUL1. {ECO:0000250}. +Q3TQF0 FBX31_MOUSE F-box only protein 31 507 57,191 Chain (1); Domain (1); Erroneous initiation (2); Modified residue (3); Sequence conflict (2) Protein modification; protein ubiquitination. FUNCTION: Component of some SCF (SKP1-cullin-F-box) protein ligase complex that plays a central role in G1 arrest following DNA damage. Specifically recognizes phosphorylated cyclin-D1 (CCND1), promoting its ubiquitination and degradation by the proteasome, resulting in G1 arrest (By similarity). {ECO:0000250}. PTM: Phosphorylation by ATM following gamma-irradiation results in its stabilization. {ECO:0000250}. SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex. {ECO:0000250}. +P08101 FCGR2_MOUSE Low affinity immunoglobulin gamma Fc region receptor II (Fc gamma receptor IIB) (Fc-gamma RII) (Fc-gamma-RIIB) (FcRII) (IgG Fc receptor II beta) (Lymphocyte antigen 17) (Ly-17) (CD antigen CD32) 330 36,695 Alternative sequence (2); Chain (1); Disulfide bond (2); Domain (2); Erroneous initiation (1); Glycosylation (4); Modified residue (3); Motif (1); Natural variant (8); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 211 231 Helical. {ECO:0000255}. TOPO_DOM 30 210 Extracellular. {ECO:0000255}.; TOPO_DOM 232 330 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for the Fc region of complexed immunoglobulins gamma. Low affinity receptor. Involved in a variety of effector and regulatory functions such as phagocytosis of antigen-antibody complexes from the circulation and modulation of antibody production by B-cells. Isoform IIB1 and isoform IIB1' form caps but fail to mediate endocytosis or phagocytosis. Isoform IIB2 can mediate the endocytosis of soluble immune complexes via clathrin-coated pits. Isoform IIB1 and isoform IIB2 can down-regulate B-cell, T-cell, and mast cell activation when coaggregated to B-cell receptors for AG (BCR), T-cell receptors for AG (TCR), and Fc receptors, respectively. PTM: Glycosylated.; PTM: When coaggregated to BCR, isoform IIB1 and isoform IIB1' become tyrosine phosphorylated and bind to the SH2 domains of the protein tyrosine phosphatase PTPC1. Phosphorylated by SRC-type Tyr-kinases such as LYN, BLK, FYN and SYK (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Isoform IIB1: Cytoplasm, cytoskeleton. Note=Binds the cytoskeleton and is not localized in endocytotic pits.; SUBCELLULAR LOCATION: Isoform IIB3: Secreted. Note=Released as a soluble molecule. SUBUNIT: Interacts with FGR (By similarity). Interacts with LYN. {ECO:0000250, ECO:0000269|PubMed:9469421}. DOMAIN: Contains 1 copy of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is involved in modulation of cellular responses. The phosphorylated ITIM motif can bind the SH2 domain of several SH2-containing phosphatases. Another tyrosine-containing sequence, more C-terminal, accounts for the ability of isoform IIB2 to trigger the phagocytosis of particulate immuno complexes. TISSUE SPECIFICITY: Widely expressed by cells of hemopoietic origin. The isoforms are differentially expressed. Isoform IIB1 is preferentially expressed by cells of the lymphoid lineage, isoform IIB2 by cells of the myeloid lineage, and isoform IIB3 is released by macrophages and is present in the serum. Isoform IIB1' is expressed in myeloid and lymphoid cell lines, in normal spleen cells, and in resting or LPS-activated B-cells but is not detected in mesenteric lymph node cells. +Q9R1K5 FZR1_MOUSE Fizzy-related protein homolog (Fzr) (Cdh1/Hct1 homolog) 493 54,689 Chain (1); Modified residue (8); Repeat (7) Protein modification; protein ubiquitination. FUNCTION: Substrate-specific adapter for the anaphase promoting complex/cyclosome (APC/C) E3 ubiquitin-protein ligase complex. Associates with the APC/C in late mitosis, in replacement of CDC20, and activates the APC/C during anaphase and telophase. The APC/C remains active in degrading substrates to ensure that positive regulators of the cell cycle do not accumulate prematurely. At the G1/S transition FZR1 is phosphorylated, leading to its dissociation from the APC/C. Following DNA damage, it is required for the G2 DNA damage checkpoint: its dephosphorylation and reassociation with the APC/C leads to the ubiquitination of PLK1, preventing entry into mitosis. Acts as an adapter for APC/C to target the DNA-end resection factor RBBP8/CtIP for ubiquitination and subsequent proteasomal degradation. Through the regulation of RBBP8/CtIP protein turnover, may play a role in DNA damage response, favoring DNA double-strand repair through error-prone non-homologous end joining (NHEJ) over error-free, RBBP8-mediated homologous recombination (HR). {ECO:0000250|UniProtKB:Q9UM11}. PTM: Acetylated. Deacetylated by SIRT2 at Lys-69 and Lys-159; deacetylation enhances the interaction of FZR1 with CDC27, leading to activation of anaphase promoting complex/cyclosome (APC/C).; PTM: Phosphorylated during mitosis, probably by maturation promoting factor (MPF), leading to its dissociation of the APC/C. Following DNA damage, it is dephosphorylated by CDC14B in G2 phase, leading to its reassociation with the APC/C, and allowing an efficient G2 DNA damage checkpoint. Phosphorylated by MAK (By similarity). {ECO:0000250}. SUBUNIT: The unphosphorylated form interacts with APC/C during mitosis. Interacts with NINL. Interacts (in complex with the anaphase promoting complex APC) with MAD2L2; inhibits FZR1-mediated APC/C activation (By similarity). Interacts with SIRT2 (PubMed:22014574). Interacts with USP37 Interacts (via WD repeats) with MAK. Interacts with RBBP8/CtIP; this interaction leads to RBBP8 proteasomal degradation. Interacts with HECW2 (By similarity). {ECO:0000250|UniProtKB:Q9UM11, ECO:0000269|PubMed:22014574}. +Q8C2P3 DUS1L_MOUSE tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like (EC 1.3.1.-) (tRNA-dihydrouridine synthase 1-like) 475 53,512 Active site (1); Binding site (3); Chain (1); Erroneous initiation (2); Nucleotide binding (3); Sequence conflict (1) FUNCTION: Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs. {ECO:0000250}. +P28563 DUS1_MOUSE Dual specificity protein phosphatase 1 (EC 3.1.3.16) (EC 3.1.3.48) (Mitogen-activated protein kinase phosphatase 1) (MAP kinase phosphatase 1) (MKP-1) (Protein-tyrosine phosphatase 3CH134) (Protein-tyrosine phosphatase ERP) 367 39,370 Active site (1); Chain (1); Domain (2); Modified residue (2); Mutagenesis (2) FUNCTION: Dual specificity phosphatase that dephosphorylates MAP kinase MAPK1/ERK2 on both 'Thr-183' and 'Tyr-185', regulating its activity during the meiotic cell cycle. {ECO:0000269|PubMed:8221888}. PTM: Phosphorylation at Ser-359 and Ser-364 by MAPK1/ERK2 and MAPK3/ERK1 reduces its rate of degradation. {ECO:0000269|PubMed:10617468}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q91790}. +Q61599 GDIR2_MOUSE Rho GDP-dissociation inhibitor 2 (Rho GDI 2) (D4) (Rho-GDI beta) 200 22,851 Chain (1); Initiator methionine (1); Modified residue (10) FUNCTION: Regulates the GDP/GTP exchange reaction of the Rho proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them. Regulates reorganization of the actin cytoskeleton mediated by Rho family members. {ECO:0000250|UniProtKB:P52566}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P52566}. SUBUNIT: Interacts with RHOA. Interacts with RAC1. Interacts with RAC2. Interacts with CDC42. {ECO:0000250|UniProtKB:P52566}. TISSUE SPECIFICITY: Preferentially expressed in hematopoietic cells. {ECO:0000269|PubMed:7512369}. +Q62160 GDIR3_MOUSE Rho GDP-dissociation inhibitor 3 (Rho GDI 3) (Rho-GDI gamma) (Rho-GDI2) 225 25,296 Chain (1) FUNCTION: Inhibits GDP/GTP exchange reaction of RhoB. Interacts specifically with the GDP- and GTP-bound forms of post-translationally processed Rhob and Rhog proteins, both of which show a growth-regulated expression in mammalian cells. Stimulates the release of the GDP-bound but not the GTP-bound RhoB protein. Also inhibits the GDP/GTP exchange of RhoB but shows less ability to inhibit the dissociation of prebound GTP. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. TISSUE SPECIFICITY: Detected only in brain, lung, kidney and testis. +Q9CXU9 EIF1B_MOUSE Eukaryotic translation initiation factor 1b (eIF1b) 113 12,824 Chain (1); Initiator methionine (1); Modified residue (2); Sequence conflict (1) FUNCTION: Probably involved in translation. +P48024 EIF1_MOUSE Eukaryotic translation initiation factor 1 (eIF1) (Protein translation factor SUI1 homolog) 113 12,747 Chain (1); Initiator methionine (1); Modified residue (3) FUNCTION: Necessary for scanning and involved in initiation site selection. Promotes the assembly of 48S ribosomal complexes at the authentic initiation codon of a conventional capped mRNA (By similarity). {ECO:0000250}. SUBUNIT: Interacts with RENT2. {ECO:0000250}. +P17182 ENOA_MOUSE Alpha-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 1) (Non-neural enolase) (NNE) 434 47,141 Active site (2); Binding site (5); Chain (1); Cross-link (1); Initiator methionine (1); Metal binding (4); Modified residue (28); Region (2); Sequence conflict (1) Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. FUNCTION: Multifunctional enzyme that, as well as its role in glycolysis, plays a part in various processes such as growth control, hypoxia tolerance and allergic responses (By similarity). May also function in the intravascular and pericellular fibrinolytic system due to its ability to serve as a receptor and activator of plasminogen on the cell surface of several cell-types such as leukocytes and neurons. Stimulates immunoglobulin production (By similarity). {ECO:0000250}. PTM: ISGylated. {ECO:0000269|PubMed:16139798}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Can translocate to the plasma membrane in either the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form (By similarity). ENO1 is localized to the M-band. {ECO:0000250, ECO:0000269|PubMed:11229603}. SUBUNIT: Mammalian enolase is composed of 3 isozyme subunits, alpha, beta and gamma, which can form homodimers or heterodimers which are cell-type and development-specific. ENO1 interacts with PLG in the neuronal plasma membrane and promotes its activation. The C-terminal lysine is required for this binding (By similarity). In vitro, interacts with several glycolytic enzymes including PKM, PGM, CKM and aldolase (PubMed:9169614). Also binds troponin, in vitro (PubMed:9169614). Interacts with ENO4 and PGAM2 (PubMed:23446454). Interacts with CMTM6 (By similarity). {ECO:0000250|UniProtKB:P06733, ECO:0000269|PubMed:23446454, ECO:0000269|PubMed:9169614}. TISSUE SPECIFICITY: Testis. Found in the principal piece of sperm tail (at protein level). The alpha/alpha homodimer is expressed in embryo and in most adult tissues. The alpha/beta heterodimer and the beta/beta homodimer are found in striated muscle, and the alpha/gamma heterodimer and the gamma/gamma homodimer in neurons. In striated muscle, expression of ENO1 appears to be independent of fiber type. {ECO:0000269|PubMed:11229603, ECO:0000269|PubMed:23446454}. +P21279 GNAQ_MOUSE Guanine nucleotide-binding protein G(q) subunit alpha (Guanine nucleotide-binding protein alpha-q) 359 42,158 Beta strand (8); Binding site (1); Chain (1); Helix (20); Lipidation (2); Metal binding (2); Mutagenesis (2); Nucleotide binding (4); Sequence conflict (2); Turn (3) FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Regulates B-cell selection and survival and is required to prevent B-cell-dependent autoimmunity. Regulates chemotaxis of BM-derived neutrophils and dendritic cells (in vitro). {ECO:0000269|PubMed:17938235, ECO:0000269|PubMed:20624888}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18802028}. Membrane {ECO:0000269|PubMed:18802028}. Nucleus membrane {ECO:0000269|PubMed:18802028}. Note=Colocalizes with the adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane of cardiac myocytes. SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site. Binds SLC9A3R1. Forms a complex with PECAM1 and BDKRB2. Interacts with PECAM1 (By similarity). {ECO:0000250}. +Q6R0H7 GNAS1_MOUSE Guanine nucleotide-binding protein G(s) subunit alpha isoforms XLas (Adenylate cyclase-stimulating G alpha protein) (Extra large alphas protein) (XLalphas) 1133 121,505 Alternative sequence (5); Binding site (1); Chain (1); Coiled coil (1); Compositional bias (2); Erroneous initiation (2); Metal binding (2); Modified residue (2); Nucleotide binding (4); Sequence conflict (7) FUNCTION: Guanine nucleotide-binding proteins (G proteins) function as transducers in numerous signaling pathways controlled by G protein-coupled receptors (GPCRs). Signaling involves the activation of adenylyl cyclases, resulting in increased levels of the signaling molecule cAMP. GNAS functions downstream of several GPCRs, including beta-adrenergic receptors. XLas isoforms interact with the same set of receptors as Gnas isoforms. {ECO:0000269|PubMed:12145344}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q63803}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q63803}. Apical cell membrane {ECO:0000250|UniProtKB:Q5JWF2}. SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site. Interacts through its N-terminal region with ALEX which is produced from the same locus in a different open reading frame. This interaction may inhibit its adenylyl cyclase-stimulating activity (By similarity). Interacts with MAGED2. {ECO:0000250|UniProtKB:Q5JWF2, ECO:0000250|UniProtKB:Q63803}. +P50149 GNAT2_MOUSE Guanine nucleotide-binding protein G(t) subunit alpha-2 (Transducin alpha-2 chain) 354 40,118 Binding site (1); Chain (1); Initiator methionine (1); Lipidation (1); Metal binding (2); Nucleotide binding (4) FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Transducin is an amplifier and one of the transducers of a visual impulse that performs the coupling between rhodopsin and cGMP-phosphodiesterase. SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site. TISSUE SPECIFICITY: Retinal rod outer segment. +O70443 GNAZ_MOUSE Guanine nucleotide-binding protein G(z) subunit alpha (G(x) alpha chain) (Gz-alpha) 355 40,850 Binding site (1); Chain (1); Initiator methionine (1); Lipidation (2); Metal binding (2); Nucleotide binding (4); Sequence conflict (1) FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. SUBCELLULAR LOCATION: Membrane; Lipid-anchor. SUBUNIT: G-proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site. Interacts with ADGRB2 (By similarity). {ECO:0000250|UniProtKB:P19086}. +P62881 GNB5_MOUSE Guanine nucleotide-binding protein subunit beta-5 (Gbeta5) (Transducin beta chain 5) 395 43,565 Alternative sequence (1); Beta strand (29); Chain (1); Helix (3); Repeat (7); Turn (6) FUNCTION: Enhances GTPase-activating protein (GAP) activity of regulator of G protein signaling (RGS) proteins, hence involved in the termination of the signaling initiated by the G protein coupled receptors (GPCRs) by accelerating the GTP hydrolysis on the G-alpha subunits, thereby promoting their inactivation (Probable). Increases RGS9 GTPase-activating protein (GAP) activity, hence contributes to the deactivation of G protein signaling initiated by D(2) dopamine receptors (By similarity). May play an important role in neuronal signaling, including in the parasympathetic, but not sympathetic, control of heart rate (By similarity). {ECO:0000250|UniProtKB:A1L271, ECO:0000250|UniProtKB:O14775, ECO:0000305}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:8071339, ECO:0000269|PubMed:8910430}. SUBUNIT: Component of a complex composed of RGS9, GNB5 and RGS9BP; within this complex, the presence of GNB5 stabilizes both itself and RGS9 and increases RGS9 GTPase-activating protein (GAP) activity (By similarity) (PubMed:12119397, PubMed:16908407, PubMed:18204463). Interacts with RGS6 and RGS7 (By similarity). {ECO:0000250|UniProtKB:O14775, ECO:0000269|PubMed:12119397, ECO:0000269|PubMed:16908407, ECO:0000269|PubMed:18204463}. TISSUE SPECIFICITY: Isoform 1 is only detected in retina (PubMed:8910430). Isoform 2 is detected in brain (at protein level) (PubMed:8071339). Isoform 2 is detected in brain (PubMed:8071339). {ECO:0000269|PubMed:8071339, ECO:0000269|PubMed:8910430}. +P98192 GNPAT_MOUSE Dihydroxyacetone phosphate acyltransferase (DAP-AT) (DHAP-AT) (EC 2.3.1.42) (Acyl-CoA:dihydroxyacetonephosphateacyltransferase) (Glycerone-phosphate O-acyltransferase) 678 76,870 Chain (1); Compositional bias (1); Modified residue (3); Motif (2) Membrane lipid metabolism; glycerophospholipid metabolism. SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Matrix side {ECO:0000250}. Note=Exclusively localized to the lumenal side of the peroxisomal membrane. {ECO:0000250}. SUBUNIT: May be part of a heterotrimeric complex composed of DAP-AT, ADAP-S and a modified form of DAP-AT. DOMAIN: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in liver and testis. Lower levels in heart, brain, lung and kidney. Detected in spleen. +Q9JIX0 ENY2_MOUSE Transcription and mRNA export factor ENY2 (Enhancer of yellow 2 transcription factor homolog) 101 11,529 Chain (1); Cross-link (1) FUNCTION: Involved in mRNA export coupled transcription activation by association with both the TREX-2 and the SAGA complexes. The transcription regulatory histone acetylation (HAT) complex SAGA is a multiprotein complex that activates transcription by remodeling chromatin and mediating histone acetylation and deubiquitination. Within the SAGA complex, participates in a subcomplex that specifically deubiquitinates both histones H2A and H2B. The SAGA complex is recruited to specific gene promoters by activators such as MYC, where it is required for transcription. Required for nuclear receptor-mediated transactivation. The TREX-2 complex functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket). TREX-2 participates in mRNA export and accurate chromatin positioning in the nucleus by tethering genes to the nuclear periphery (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000255|HAMAP-Rule:MF_03046}. Nucleus, nuclear pore complex {ECO:0000255|HAMAP-Rule:MF_03046}. SUBUNIT: Component of the nuclear pore complex (NPC)-associated TREX-2 complex (transcription and export complex 2), composed of at least ENY2, GANP, PCID2, SEM1, and either centrin CETN2 or CETN3. TREX-2 contains 2 ENY2 chains. The TREX-2 complex interacts with the nucleoporin NUP153. Component of some SAGA transcription coactivator-HAT complexes, at least composed of ATXN7, ATXN7L3, ENY2, GCN5L2, SUPT3H, TAF10, TRRAP and USP22. Within the SAGA complex, ENY2, ATXN7, ATXN7L3, and USP22 form an additional subcomplex of SAGA called the DUB module (deubiquitination module). Interacts directly with ATXN7L3, GANP and with the RNA polymerase II. Interacts strongly with ATXN7L3 and ATXN7L3B. {ECO:0000255|HAMAP-Rule:MF_03046}. +Q80TA1 EPT1_MOUSE Ethanolaminephosphotransferase 1 (EC 2.7.8.1) (Selenoprotein I) (SelI) 398 45,346 Chain (1); Erroneous termination (3); Initiator methionine (1); Modified residue (1); Non-standard residue (1); Transmembrane (10) TRANSMEM 47 69 Helical. {ECO:0000255}.; TRANSMEM 84 103 Helical. {ECO:0000255}.; TRANSMEM 123 145 Helical. {ECO:0000255}.; TRANSMEM 150 172 Helical. {ECO:0000255}.; TRANSMEM 179 201 Helical. {ECO:0000255}.; TRANSMEM 221 243 Helical. {ECO:0000255}.; TRANSMEM 256 278 Helical. {ECO:0000255}.; TRANSMEM 291 310 Helical. {ECO:0000255}.; TRANSMEM 319 341 Helical. {ECO:0000255}.; TRANSMEM 345 367 Helical. {ECO:0000255}. Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from ethanolamine: step 3/3. FUNCTION: Catalyzes phosphatidylethanolamine biosynthesis from CDP-ethanolamine. It thereby plays a central role in the formation and maintenance of vesicular membranes. Involved in the formation of phosphatidylethanolamine via 'Kennedy' pathway (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9D733 GP2_MOUSE Pancreatic secretory granule membrane major glycoprotein GP2 (Pancreatic zymogen granule membrane protein GP-2) 531 59,154 Chain (1); Disulfide bond (8); Domain (2); Erroneous initiation (1); Glycosylation (6); Propeptide (1); Signal peptide (1) SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. Secreted {ECO:0000250}. Note=Secreted after cleavage. SUBUNIT: Interacts with SYCN. {ECO:0000250}. +Q6IE26 EPHX4_MOUSE Epoxide hydrolase 4 (EC 3.3.-.-) (Abhydrolase domain-containing protein 7) (Epoxide hydrolase-related protein) 359 41,477 Active site (3); Chain (1); Domain (1); Transmembrane (1) TRANSMEM 15 35 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. +Q03137 EPHA4_MOUSE Ephrin type-A receptor 4 (EC 2.7.10.1) (Tyrosine-protein kinase receptor MPK-3) (Tyrosine-protein kinase receptor SEK-1) 986 109,814 Active site (1); Alternative sequence (1); Beta strand (8); Binding site (1); Chain (1); Compositional bias (1); Domain (5); Glycosylation (3); Helix (20); Modified residue (4); Motif (1); Mutagenesis (1); Nucleotide binding (1); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (2) TRANSMEM 548 569 Helical. {ECO:0000255}. TOPO_DOM 20 547 Extracellular. {ECO:0000255}.; TOPO_DOM 570 986 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor tyrosine kinase which binds membrane-bound ephrin family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Highly promiscuous, it has the unique property among Eph receptors to bind and to be physiologically activated by both GPI-anchored ephrin-A and transmembrane ephrin-B ligands including EFNA1 and EFNB3. Upon activation by ephrin ligands, modulates cell morphology and integrin-dependent cell adhesion through regulation of the Rac, Rap and Rho GTPases activity. Plays an important role in the development of the nervous system controlling different steps of axonal guidance including the establishment of the corticospinal projections. May also control the segregation of motor and sensory axons during neuromuscular circuit development. In addition to its role in axonal guidance plays a role in synaptic plasticity. Activated by EFNA1 phosphorylates CDK5 at 'Tyr-15' which in turn phosphorylates NGEF regulating RHOA and dendritic spine morphogenesis. In the nervous system, plays also a role in repair after injury preventing axonal regeneration and in angiogenesis playing a role in central nervous system vascular formation. Additionally, its promiscuity makes it available to participate in a variety of cell-cell signaling regulating for instance the development of the thymic epithelium. {ECO:0000269|PubMed:15537875, ECO:0000269|PubMed:16802330, ECO:0000269|PubMed:16818734, ECO:0000269|PubMed:17143272, ECO:0000269|PubMed:17719550, ECO:0000269|PubMed:17785183, ECO:0000269|PubMed:18094260, ECO:0000269|PubMed:18403711, ECO:0000269|PubMed:9789074}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17143272}; Single-pass type I membrane protein {ECO:0000269|PubMed:17143272}. Cell projection, axon {ECO:0000269|PubMed:17143272}. Cell projection, dendrite {ECO:0000269|PubMed:17143272}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250}. Early endosome {ECO:0000269|PubMed:17143272}. Note=Clustered upon activation and targeted to early endosome. SUBUNIT: Heterotetramer upon binding of the ligand. The heterotetramer is composed of an ephrin dimer and a receptor dimer. Oligomerization is probably required to induce biological responses. Interacts (phosphorylated at position Tyr-602) with FYN. Interacts (via PDZ motif) with SIPA1L1 (via PDZ domain); controls neuronal morphology through regulation of the RAP1 (RAP1A or RAP1B) and RAP2 (RAP2A, RAP2B or RAP2C) GTPases. Interacts with CDK5, CDK5R1 and NGEF; upon activation by EFNA1 induces NGEF phosphorylation by the kinase CDK5. Interacts with CHN1; effector of EPHA4 in axon guidance linking EPHA4 activation to RAC1 regulation. {ECO:0000269|PubMed:11336673, ECO:0000269|PubMed:17143272, ECO:0000269|PubMed:17719550, ECO:0000269|PubMed:17785183, ECO:0000269|PubMed:18094260, ECO:0000269|PubMed:8622893}. DOMAIN: The protein kinase domain mediates interaction with NGEF. TISSUE SPECIFICITY: Highest expression in the adult brain and retina and also detectable in kidney, lung, skeletal muscle and thymus. Not detected in heart and liver. Expressed in myogenic progenitor cells (PubMed:27446912). {ECO:0000269|PubMed:27446912}. +Q91V16 ETFR1_MOUSE Electron transfer flavoprotein regulatory factor 1 (Growth hormone-inducible soluble protein) (LYR motif-containing protein 5) 86 10,391 Chain (1); Natural variant (1) FUNCTION: Acts as a regulator of the electron transfer flavoprotein by promoting the removal of flavin from the ETF holoenzyme (composed of ETFA and ETFB). {ECO:0000250|UniProtKB:Q6IPR1}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q6IPR1}. SUBUNIT: homotetramer. Interacts with NDUFAB1. Interacts with ETFA. Interacts with ETFB. {ECO:0000250|UniProtKB:Q6IPR1}. +Q9DCM0 ETHE1_MOUSE Persulfide dioxygenase ETHE1, mitochondrial (EC 1.13.11.18) (Ethylmalonic encephalopathy protein 1 homolog) (Hepatoma subtracted clone one protein) (Sulfur dioxygenase ETHE1) 254 27,739 Chain (1); Metal binding (3); Modified residue (8); Transit peptide (1) FUNCTION: First described as a protein that can shuttle between the nucleus and the cytoplasm and suppress p53-induced apoptosis by sequestering the transcription factor RELA/NFKB3 in the cytoplasm and preventing its accumulation in the nucleus (By similarity). Sulfur dioxygenase that plays an essential role in hydrogen sulfide catabolism in the mitochondrial matrix. Hydrogen sulfide (H(2)S) is first oxidized by SQRDL, giving rise to cysteine persulfide residues. ETHE1 consumes molecular oxygen to catalyze the oxidation of the persulfide, once it has been transferred to a thiophilic acceptor, such as glutathione (R-SSH). Plays an important role in metabolic homeostasis in mitochondria by metabolizing hydrogen sulfide and preventing the accumulation of supraphysiological H(2)S levels that have toxic effects, due to the inhibition of cytochrome c oxidase. {ECO:0000250|UniProtKB:O95571, ECO:0000269|PubMed:19136963}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O95571}. Nucleus {ECO:0000250|UniProtKB:O95571}. Mitochondrion matrix {ECO:0000250|UniProtKB:O95571}. SUBUNIT: Homodimer. Monomer. Interacts with TST. May interact with RELA. {ECO:0000250|UniProtKB:O95571}. +Q9CXC9 ETV5_MOUSE ETS translocation variant 5 510 57,712 Chain (1); Cross-link (1); DNA binding (1); Modified residue (1); Sequence conflict (3) FUNCTION: Binds to DNA sequences containing the consensus nucleotide core sequence 5'-GGAA.-3'. {ECO:0000250|UniProtKB:P41161}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00237}. SUBUNIT: Interacts (via C-terminal) with ZMYM5 (via N-terminal 120 amino acid region). {ECO:0000250|UniProtKB:P41161}. TISSUE SPECIFICITY: In the brain, expressed predominantly in the cerebral cortex, the amygdala and the hypothalamus. Within the cerebral cortex, there is conspicuously high expression in cortical layers 2, 4 and 6 while expression is almost absent from layers 1, 3 and 5. High expression is also observed in the dorsal and ventral endopiriform claustrum. Strong expression is observed in limited parts of the amygdala including the basolateral amygdaloid nucleus, the bed stria terminalis and the central amygdaloid nucleus. Low to moderate levels are found in the hypothalamus while expression is almost absent in the thalamus. Hypothalamic expression is seen in the dorsomedial hypothalamic nucleus and also the central, dorsomedial and ventrolateral parts of the ventromedial hypothalamic nucleus. Strong expression is also identified in the nigrostriatal tract. In the mesencephalon, expression is restricted to the ventral tegmental area including the parabrachial pigmented nucleus. In the hippocampus, strongly expressed in the pyramidal cell layer. Some expression is also found in the lacunosum moleculare layer. Low levels of expression in the cerebellum, including the granular, molecular and Purkinje cell layers. {ECO:0000269|PubMed:27280443}. +P58659 EVA1C_MOUSE Protein eva-1 homolog C (Protein FAM176C) 440 49,287 Alternative sequence (2); Chain (1); Domain (2); Glycosylation (3); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 322 342 Helical. {ECO:0000255}. TOPO_DOM 49 321 Extracellular. {ECO:0000255}.; TOPO_DOM 343 440 Cytoplasmic. {ECO:0000255}. FUNCTION: Binds heparin. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Ubiquitous. +P57680 EVC_MOUSE Ellis-van Creveld syndrome protein homolog 1005 113,003 Alternative sequence (1); Chain (1); Sequence conflict (5); Topological domain (2); Transmembrane (1) TRANSMEM 22 42 Helical. {ECO:0000255}. TOPO_DOM 1 21 Extracellular. {ECO:0000255}.; TOPO_DOM 43 1005 Cytoplasmic. {ECO:0000255}. FUNCTION: Component of the EvC complex that positively regulates ciliary Hedgehog (Hh) signaling (PubMed:17660199, PubMed:24582806). Involved in endochondral growth and skeletal development (PubMed:17660199). {ECO:0000269|PubMed:17660199, ECO:0000269|PubMed:24582806}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21356043}; Single-pass membrane protein {ECO:0000269|PubMed:21356043}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:17660199}. Cell projection, cilium {ECO:0000269|PubMed:21356043}. Cell projection, cilium membrane {ECO:0000269|PubMed:21356043, ECO:0000269|PubMed:24582806}. Note=EVC2 is required for the localization of EVC at the base of primary cilia (PubMed:21356043). The EvC complex localizes at the base of cilia in the EvC zone of primary cilia in a EFCAB7-dependent manner (PubMed:24582806). {ECO:0000269|PubMed:21356043, ECO:0000269|PubMed:24582806}. SUBUNIT: Component of the EvC complex composed of EFCAB7, IQCE, EVC2 and EVC; built from two subcomplexes, EVC2:EVC and EFCAB7:IQCE (PubMed:24582806). Interacts with EVC2 (PubMed:24582806, PubMed:21356043). Interacts with EFCAB7 (PubMed:24582806). Interacts with IQCE (PubMed:24582806). {ECO:0000269|PubMed:24582806}. TISSUE SPECIFICITY: Expressed in the developing skeleton and the orofacial region. Expression is general to all the cartilaginous components of the skeleton, including the chondrocranium, the vertebrae, the rib cage, and the axial skeleton by day E15.5. {ECO:0000269|PubMed:17660199}. +P70429 EVL_MOUSE Ena/VASP-like protein (Ena/vasodilator-stimulated phosphoprotein-like) 414 44,337 Alternative sequence (1); Beta strand (8); Chain (1); Compositional bias (1); Domain (1); Helix (1); Modified residue (11); Motif (1); Region (5); Turn (3) FUNCTION: Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance and lamellipodial and filopodial dynamics in migrating cells. EVL enhances actin nucleation and polymerization. {ECO:0000269|PubMed:10087267, ECO:0000269|PubMed:10945997}. PTM: Phosphorylated by PKA; phosphorylation abolishes binding to SH3 domains of ABL and SRC. {ECO:0000269|PubMed:10945997}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10945997}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000269|PubMed:10945997}. Cell projection, lamellipodium {ECO:0000269|PubMed:10945997}. Note=Targeted to the leading edge of lamellipodia and the distal tip of stress fibers through interaction with a number of proteins. In activated T-cells, localizes to the F-actin collar and the distal tip of microspikes. {ECO:0000269|PubMed:10945997}. SUBUNIT: Homotetramer (By similarity). Binds to the SH3 domains of ABL1, LYN and SRC (PubMed:10945997). Also binds to profilin, with preference for isoform IIa of PFN2, and the WW domain of APBB1/FE65 (PubMed:10945997). Binds to SEMA6A (PubMed:10993894). Interacts, via the Pro-rich region, with the C-terminal SH3 domain of DNMBP (PubMed:14506234). Interacts with RAPH1 (By similarity). Binds, via the EVH1 domain, the Pro-rich domain of Listeria monocytogenes actA (PubMed:10087267). Binds, via the EVH1 domain, the Pro-rich domain of ZYX. Interacts with FYB1. Interacts with ZDHHC17 (By similarity). {ECO:0000250|UniProtKB:Q9UI08, ECO:0000269|PubMed:10087267, ECO:0000269|PubMed:10404224, ECO:0000269|PubMed:10945997, ECO:0000269|PubMed:10993894, ECO:0000269|PubMed:14506234}. DOMAIN: The EVH2 domain is comprised of 3 regions. Block A is a thymosin-like domain required for G-actin binding. The KLKR motif within this block is essential for the G-actin binding and for actin polymerization. Block B is required for F-actin binding and subcellular location, and Block C for tetramerization. TISSUE SPECIFICITY: Highest expression in thymus and spleen (at protein level). Low levels in placenta, ovary, testis, fat and lung (at protein level). Isoform 1 and isoform 2 are expressed in cortical neurons and glial cells. {ECO:0000269|PubMed:10069337, ECO:0000269|PubMed:10945997}. +Q61545 EWS_MOUSE RNA-binding protein EWS 655 68,462 Chain (1); Compositional bias (3); Domain (2); Modified residue (38); Motif (1); Region (2); Repeat (31); Sequence conflict (2); Zinc finger (1) FUNCTION: Might function as a transcriptional repressor. {ECO:0000250}. PTM: Phosphorylated; calmodulin-binding inhibits phosphorylation of Ser-266. {ECO:0000250}.; PTM: Highly methylated on arginine residues. Methylation is mediated by PRMT1 and, at lower level by PRMT8 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Relocates from cytoplasm to ribosomes upon PTK2B/FAK2 activation. {ECO:0000250}. SUBUNIT: Binds RNA, POLR2C, SF1 and calmodulin. Interacts with PTK2B and TDRD3 (By similarity). {ECO:0000250}. +Q8VEG4 EXD2_MOUSE Exonuclease 3'-5' domain-containing protein 2 (EC 3.1.11.1) (Exonuclease 3'-5' domain-like-containing protein 2) 650 74,332 Alternative sequence (1); Chain (1); Domain (1); Sequence conflict (2) FUNCTION: Exonuclease required for double-strand breaks resection and efficient homologous recombination. Plays a key role in controlling the initial steps of chromosomal break repair, it is recruited to chromatin in a damage-dependent manner and functionally interacts with the MRN complex to accelerate resection through its 3'-5' exonuclease activity, which efficiently processes double-stranded DNA substrates containing nicks. {ECO:0000250|UniProtKB:Q9NVH0}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NVH0}. SUBUNIT: Interacts with RBBP8, MRE11 and BRCA1. {ECO:0000250|UniProtKB:Q9NVH0}. +Q9QZ11 EXO1_MOUSE Exonuclease 1 (mExo1) (EC 3.1.-.-) (Exonuclease I) 837 92,022 Chain (1); Metal binding (7); Modified residue (7); Region (6); Sequence conflict (9) FUNCTION: 5'->3' double-stranded DNA exonuclease which may also possess a cryptic 3'->5' double-stranded DNA exonuclease activity. Functions in DNA mismatch repair (MMR) to excise mismatch-containing DNA tracts directed by strand breaks located either 5' or 3' to the mismatch. Also exhibits endonuclease activity against 5'-overhanging flap structures similar to those generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. Required for somatic hypermutation (SHM) and class switch recombination (CSR) of immunoglobulin genes. Essential for male and female meiosis. {ECO:0000269|PubMed:12629043, ECO:0000269|PubMed:14716311}. PTM: Phosphorylated upon DNA damage and in response to agents stalling DNA replication, probably by ATM or ATR. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Colocalizes with PCNA to discrete nuclear foci in S-phase. {ECO:0000250}. SUBUNIT: Interacts with the MLH1-PMS2 heterodimer via MLH1. Interacts with MSH3. Interacts with the MSH2-MSH6 heterodimer via MSH2, and this interaction may increase the processivity of the 5'->3' exonuclease activity. Interacts with PCNA, and this interaction may both stimulate the cryptic 3'->5' exonuclease activity and suppress the 5'->3' exonuclease activity. Interacts with WRN, and this interaction stimulates both the 5'->3' exonuclease activity and cleavage of 5'-overhanging flap structures. Interacts with RECQL/RECQ1, and this interaction stimulates cleavage of 5'-overhanging flap structures (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in the spleen and testis. Also expressed in the bone marrow, brain, lung, lymph node and thymus. {ECO:0000269|PubMed:10497278}. +Q6KAR6 EXOC3_MOUSE Exocyst complex component 3 (Exocyst complex component Sec6) 755 86,455 Chain (1); Coiled coil (2); Erroneous initiation (1); Modified residue (1) FUNCTION: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O54921}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O54921}. Cell projection, growth cone {ECO:0000250|UniProtKB:O54921}. Midbody {ECO:0000250|UniProtKB:O60645}. Golgi apparatus {ECO:0000250|UniProtKB:O60645}. Note=Perinuclear in undifferentiated cells. Redistributes to growing neurites and growth cones during neuronal differentiation (By similarity). During mitosis, early recruitment to the midbody requires RALA, but not RALB, and EXOC2. In late stages of cytokinesis, localization to the midbody is RALB-dependent (By similarity). {ECO:0000250|UniProtKB:O54921, ECO:0000250|UniProtKB:O60645}. SUBUNIT: The exocyst complex is composed of EXOC1, EXOC2, EXOC3, EXOC4, EXOC5, EXOC6, EXOC7 and EXOC8 (By similarity). Interacts with EXOC3L1 (PubMed:18480549). Interacts with BIRC6/bruce (By similarity). Interacts with MYRIP. {ECO:0000250|UniProtKB:O54921, ECO:0000269|PubMed:17827149, ECO:0000269|PubMed:18480549}. +Q6PGF7 EXOC8_MOUSE Exocyst complex component 8 (Exocyst complex 84 kDa subunit) 716 81,035 Chain (1); Domain (1); Modified residue (2) FUNCTION: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O54924}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O54924}. Cell projection, growth cone {ECO:0000250|UniProtKB:O54924}. Cell projection {ECO:0000250|UniProtKB:O54924}. Note=Binds lipids with phosphatidylinositol 3,4,5-trisphosphate groups (By similarity). Perinuclear in undifferentiated PC12 cells. Redistributes to growing neurites and growth cones during NGF-induced neuronal differentiation (By similarity). Localizes at the leading edge of migrating cells (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O54924}. SUBUNIT: The exocyst complex is composed of EXOC1, EXOC2, EXOC3, EXOC4, EXOC5, EXOC6, EXOC7 and EXOC8 (By similarity). Interacts (via PH domain) with GTP-bound RALA and RALB (By similarity). Interacts with SH3BP1; required for the localization of both SH3BP1 and the exocyst to the leading edge of migrating cells (By similarity). {ECO:0000250|UniProtKB:O54924, ECO:0000250|UniProtKB:Q8IYI6}. +Q8C163 EXOG_MOUSE Nuclease EXOG, mitochondrial (EC 3.1.30.-) (Endonuclease G-like 1) (Endo G-like 1) 368 41,384 Active site (1); Chain (1); Metal binding (1); Sequence conflict (2); Transit peptide (1) FUNCTION: Endo/exonuclease with nicking activity towards supercoiled DNA, a preference for single-stranded DNA and 5'-3' exonuclease activity. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +Q8BTW3 EXOS6_MOUSE Exosome complex component MTR3 (Exosome component 6) (mRNA transport regulator 3 homolog) 273 28,370 Chain (1); Frameshift (1) FUNCTION: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes (By similarity). {ECO:0000250, ECO:0000269|PubMed:21255825}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Component of the RNA exosome complex. Specifically part of the catalytically inactive RNA exosome core (Exo-9) complex which is believed to associate with catalytic subunits EXOSC10, and DIS3 or DIS3L in cytoplasmic- and nuclear-specific RNA exosome complex forms. Exo-9 is formed by a hexameric ring of RNase PH domain-containing subunits specifically containing the heterodimers EXOSC4-EXOSC9, EXOSC5-EXOSC8 and EXOSC6-EXOSC7, and peripheral S1 domain-containing components EXOSC1, EXOSC2 and EXOSC3 located on the top of the ring structure (By similarity). {ECO:0000250}. +Q9D0M0 EXOS7_MOUSE Exosome complex exonuclease RRP42 (Exosome component 7) (Ribosomal RNA-processing protein 42) 291 31,825 Chain (1); Initiator methionine (1); Modified residue (2) FUNCTION: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Component of the RNA exosome complex. Specifically part of the catalytically inactive RNA exosome core (Exo-9) complex which is believed to associate with catalytic subunits EXOSC10, and DIS3 or DIS3L in cytoplasmic- and nuclear-specific RNA exosome complex forms. Exo-9 is formed by a hexameric ring of RNase PH domain-containing subunits specifically containing the heterodimers EXOSC4-EXOSC9, EXOSC5-EXOSC8 and EXOSC6-EXOSC7, and peripheral S1 domain-containing components EXOSC1, EXOSC2 and EXOSC3 located on the top of the ring structure. Interacts with EXOSC1 (By similarity). Interacts with ZC3HAV1 (By similarity). {ECO:0000250}. +Q9JHI7 EXOS9_MOUSE Exosome complex component RRP45 (Autoantigen PM/Scl 1) (Exosome component 9) (P75 polymyositis-scleroderma overlap syndrome-associated autoantigen) (Polymyositis/scleroderma autoantigen 1) (Polymyositis/scleroderma autoantigen 75 kDa) (PM/Scl-75) 438 48,937 Chain (1); Cross-link (2); Modified residue (6) FUNCTION: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. EXOSC9 binds to ARE-containing RNAs (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q06265}. Nucleus {ECO:0000250|UniProtKB:Q06265}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q06265}. Note=Colocalizes with SETX in nuclear foci upon induction of transcription-related DNA damage at the S phase (By similarity). {ECO:0000250|UniProtKB:Q06265}. SUBUNIT: Component of the RNA exosome complex. Specifically part of the catalytically inactive RNA exosome core (Exo-9) complex which is believed to associate with catalytic subunits EXOSC10, and DIS3 or DIS3L in cytoplasmic- and nuclear-specific RNA exosome complex forms. Exo-9 is formed by a hexameric ring of RNase PH domain-containing subunits specifically containing the heterodimers EXOSC4-EXOSC9, EXOSC5-EXOSC8 and EXOSC6-EXOSC7, and peripheral S1 domain-containing components EXOSC1, EXOSC2 and EXOSC3 located on the top of the ring structure. Interacts (via C-terminus region) with SETX (via N-terminus domain); the interaction enhances SETX sumoylation (By similarity). {ECO:0000250|UniProtKB:Q06265}. +P70428 EXT2_MOUSE Exostosin-2 (EC 2.4.1.224) (EC 2.4.1.225) (Glucuronosyl-N-acetylglucosaminyl-proteoglycan/N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase) (Multiple exostoses protein 2 homolog) 718 82,064 Active site (1); Binding site (2); Chain (1); Disulfide bond (1); Glycosylation (2); Metal binding (1); Region (4); Sequence conflict (7); Topological domain (2); Transmembrane (1) TRANSMEM 26 46 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 25 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 47 718 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Glycosyltransferase required for the biosynthesis of heparan-sulfate. The EXT1/EXT2 complex possesses substantially higher glycosyltransferase activity than EXT1 or EXT2 alone. Appears to be a tumor suppressor. Required for the exosomal release of SDCBP, CD63 and syndecan. {ECO:0000250|UniProtKB:Q93063}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q93063}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q93063}. Golgi apparatus membrane {ECO:0000269|PubMed:10639137}; Single-pass type II membrane protein {ECO:0000269|PubMed:10639137}. Note=The EXT1/EXT2 complex is localized in the Golgi apparatus. {ECO:0000269|PubMed:10639137}. SUBUNIT: Interacts with GALNT5 (By similarity). Forms a homo/hetero-oligomeric complex with EXT1. Interacts with NDST1 (By similarity). {ECO:0000250|UniProtKB:Q93063}. TISSUE SPECIFICITY: Expressed in heart, brain, spleen, lung, liver, skeletal muscle and testis. Heart shows a high expression. {ECO:0000269|PubMed:18337501, ECO:0000269|PubMed:9232192}. +Q9WVL6 EXTL3_MOUSE Exostosin-like 3 (EC 2.4.1.223) (Glucuronyl-galactosyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase) (Multiple exostosis-like protein 3) 918 104,474 Active site (1); Binding site (2); Chain (1); Disulfide bond (1); Glycosylation (4); Metal binding (1); Modified residue (1); Region (3); Sequence conflict (4); Topological domain (2); Transmembrane (1) TRANSMEM 31 51 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 30 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 52 918 Lumenal. {ECO:0000255}. Glycan metabolism; heparan sulfate biosynthesis. FUNCTION: Glycosyltransferase which regulates the biosynthesis of heparan sulfate (HS). Important for both skeletal development and hematopoiesis, through the formation of HS proteoglycans (HSPGs). Required for the function of REG3A in regulating keratinocyte proliferation and differentiation (By similarity). {ECO:0000250|UniProtKB:O43909}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O43909}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:O43909}. Golgi apparatus {ECO:0000250|UniProtKB:O43909}. SUBUNIT: Interacts with REG3A. {ECO:0000250|UniProtKB:O43909}. +P97767 EYA1_MOUSE Eyes absent homolog 1 (EC 3.1.3.16) (EC 3.1.3.48) 591 64,324 Active site (2); Alternative sequence (2); Chain (1); Frameshift (1); Metal binding (3); Mutagenesis (2); Sequence conflict (11) FUNCTION: Functions both as protein phosphatase and as transcriptional coactivator for SIX1, and probably also for SIX2, SIX4 and SIX5 (PubMed:10490620). Tyrosine phosphatase that dephosphorylates 'Tyr-142' of histone H2AX (H2AXY142ph) and promotes efficient DNA repair via the recruitment of DNA repair complexes containing MDC1. 'Tyr-142' phosphorylation of histone H2AX plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress (PubMed:19234442). Its function as histone phosphatase may contribute to its function in transcription regulation during organogenesis (PubMed:14628042). Has also phosphatase activity with proteins phosphorylated on Ser and Thr residues (in vitro). Required for normal embryonic development of the craniofacial and trunk skeleton, kidneys and ears (PubMed:10471511). Together with SIX1, it plays an important role in hypaxial muscle development; in this it is functionally redundant with EYA2 (PubMed:17098221). {ECO:0000269|PubMed:10471511, ECO:0000269|PubMed:10490620, ECO:0000269|PubMed:14628042, ECO:0000269|PubMed:17098221, ECO:0000269|PubMed:19234442}. PTM: Sumoylated with SUMO1. {ECO:0000269|PubMed:16990542}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10490620}. Nucleus {ECO:0000269|PubMed:10490620, ECO:0000269|PubMed:19234442}. Note=Localizes at sites of DNA damage at double-strand breaks (DSBs). {ECO:0000250|UniProtKB:Q99502}. SUBUNIT: Probably interacts with SIX2, SIX4 and SIX5. Interacts with H2AX in response to DNA damage. Interacts with SIX3; promotes EYA1 translocation to the nucleus. {ECO:0000269|PubMed:10490620, ECO:0000269|PubMed:16024294, ECO:0000269|PubMed:19234442}. TISSUE SPECIFICITY: Extensively expressed in cranial placodes, branchial arches, CNS and developing eye and nose. {ECO:0000269|PubMed:9006082}. DISEASE: Note=A spontaneous mutation leading to decreased Eya1 expression gives rise to the Eya1-bor phenotype. It is characterized by circling behavior and deafness, due to gross morphological abnormalities of the inner ear, and dysmorphic or missing kidneys. This autosomal recessive trait resembles human branchio-oto-renal (BOR) syndrome. {ECO:0000269|PubMed:10072433}. +P26040 EZRI_MOUSE Ezrin (Cytovillin) (Villin-2) (p81) 586 69,407 Chain (1); Domain (1); Modified residue (7); Motif (1); Region (1); Sequence conflict (3) FUNCTION: Probably involved in connections of major cytoskeletal structures to the plasma membrane. In epithelial cells, required for the formation of microvilli and membrane ruffles on the apical pole. Along with PLEKHG6, required for normal macropinocytosis (By similarity). {ECO:0000250}. PTM: Phosphorylated by tyrosine-protein kinases. Phosphorylation by ROCK2 suppresses the head-to-tail association of the N-terminal and C-terminal halves resulting in an opened conformation which is capable of actin and membrane-binding. {ECO:0000269|PubMed:9456324}.; PTM: S-nitrosylation is induced by interferon-gamma and oxidatively-modified low-densitity lipoprotein (LDL(ox)) possibly implicating the iNOS-S100A8/9 transnitrosylase complex. {ECO:0000250|UniProtKB:P15311}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:P15311}; Peripheral membrane protein {ECO:0000250|UniProtKB:P15311}; Cytoplasmic side {ECO:0000250|UniProtKB:P15311}. Cell projection {ECO:0000250|UniProtKB:P15311}. Cell projection, microvillus membrane {ECO:0000250|UniProtKB:P15311}; Peripheral membrane protein {ECO:0000250|UniProtKB:P15311}; Cytoplasmic side {ECO:0000250|UniProtKB:P15311}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:P15311}; Peripheral membrane protein {ECO:0000250|UniProtKB:P15311}; Cytoplasmic side {ECO:0000250|UniProtKB:P15311}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:P15311}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P15311}. Cell projection, microvillus {ECO:0000269|PubMed:9472040}. Note=Localization to the apical membrane of parietal cells depends on the interaction with MPP5. Microvillar peripheral membrane protein (cytoplasmic side). Localizes to cell extensions and peripheral processes of astrocytes (By similarity). {ECO:0000250|UniProtKB:P15311, ECO:0000250|UniProtKB:P31977}. SUBUNIT: Interacts with MPP5 and SLC9A3R2. Found in a complex with EZR, PODXL and SLC9A3R2 (By similarity). Interacts with MCC, PLEKHG6, PODXL, SCYL3/PACE1, SLC9A3R1 and TMEM8B. Interacts (when phosphorylated) with FES/FPS. Interacts with dimeric S100P, the interaction may be activating through unmasking of F-actin binding sites (By similarity). Identified in complexes that contain VIM, EZR, AHNAK, BFSP1, BFSP2, ANK2, PLEC, PRX and spectrin (PubMed:21745462). Detected in a complex composed of at least EZR, AHNAK, PPL and PRX (By similarity). Interacts with PDPN (via cytoplasmic domain); activates RHOA and promotes epithelial-mesenchymal transition (By similarity). Interacts with SPN (PubMed:9472040, PubMed:21289089). Interacts with CD44 and ICAM2 (PubMed:9472040). {ECO:0000250|UniProtKB:P15311, ECO:0000250|UniProtKB:P31976, ECO:0000250|UniProtKB:P31977, ECO:0000250|UniProtKB:Q8HZQ5, ECO:0000269|PubMed:21289089, ECO:0000269|PubMed:21745462, ECO:0000269|PubMed:9472040}. DOMAIN: The [IL]-x-C-x-x-[DE] motif is a proposed target motif for cysteine S-nitrosylation mediated by the iNOS-S100A8/A9 transnitrosylase complex. {ECO:0000250|UniProtKB:P15311}. TISSUE SPECIFICITY: Detected in eye lens fiber cells (PubMed:21745462). Expressed in cerebrum and cerebellum (at protein level) (PubMed:15797715). Component of the microvilli of intestinal epithelial cells. {ECO:0000269|PubMed:15797715, ECO:0000269|PubMed:21745462}. +Q8C569 F118B_MOUSE Protein FAM118B 351 39,508 Alternative sequence (1); Chain (1); Initiator methionine (1); Modified residue (3); Sequence conflict (1) FUNCTION: May play a role in Cajal bodies formation. {ECO:0000250|UniProtKB:Q9BPY3}. SUBCELLULAR LOCATION: Nucleus, Cajal body {ECO:0000250|UniProtKB:Q9BPY3}. +Q80X91 F110D_MOUSE Protein FAM110D 271 28,712 Chain (1) +Q8R0W0 EPIPL_MOUSE Epiplakin 6548 724,646 Chain (1); Coiled coil (3); Modified residue (17); Region (3); Repeat (76) FUNCTION: Cytoskeletal linker protein that connects to intermediate filaments and controls their reorganization in response to stress (PubMed:16382146, PubMed:20926261, PubMed:18285451, PubMed:25232867, PubMed:25617501, PubMed:23599337). In response to mechanical stress like wound healing, is associated with the machinery for cellular motility by slowing down keratinocyte migration and proliferation and accelerating keratin bundling in proliferating keratinocytes thus contributing to tissue architecture (PubMed:16382146, PubMed:20926261). However in wound healing in corneal epithelium also positively regulates cell differentiation and proliferation and negatively regulates migration thereby controlling corneal epithelium morphogenesis and integrity (PubMed:23599337). In response to cellular stress, plays a role in keratin filament reorganization, probably by protecting keratin filaments against disruption (PubMed:18285451). During liver and pancreas injuries, plays a protective role by chaperoning disease-induced intermediate filament reorganization (PubMed:25232867, PubMed:25617501). {ECO:0000269|PubMed:16382146, ECO:0000269|PubMed:18285451, ECO:0000269|PubMed:20926261, ECO:0000269|PubMed:23599337, ECO:0000269|PubMed:25232867, ECO:0000269|PubMed:25617501}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:20926261, ECO:0000269|PubMed:25617501}. Apicolateral cell membrane {ECO:0000269|PubMed:25232867}. Basolateral cell membrane {ECO:0000269|PubMed:23599337}. Cell junction {ECO:0000269|PubMed:23599337}. Cell junction, hemidesmosome {ECO:0000250|UniProtKB:P58107}. Cell junction, tight junction {ECO:0000250|UniProtKB:P58107}. Cell projection {ECO:0000250|UniProtKB:P58107}. Note=Apicolateral cell membrane localization is keratin filaments-dependent (PubMed:25232867). May move dynamically from bundling intermediate filaments in the cytoplasm or at the cell periphery and reinforcing them. Decorates the keratin intermediate filaments (IF) network and partially that of vimentin (By similarity). {ECO:0000250|UniProtKB:P58107, ECO:0000269|PubMed:25232867}. SUBUNIT: Interacts with KRT5, KRT14 and KRT5/KRT14 heterotetramer; interacts preferentially with assembled filaments rather than keratin monomers (PubMed:18285451). Interacts with KRT8 and KRT18 and KRT8/KRT18 heterotetramer; interacts preferentially with assembled filaments rather than keratin monomers (PubMed:25617501). Interacts with KRT1, VIM and DES; interaction is stronger with KRT1 than with VIM or DES; interaction is dependent of higher-order structure of intermediate filament (By similarity). {ECO:0000250|UniProtKB:P58107, ECO:0000269|PubMed:18285451, ECO:0000269|PubMed:25617501}. DOMAIN: Plectin repeats are important for the binding to keratin and VIM and controls intermediate filament networks organization. {ECO:0000250|UniProtKB:P58107}. TISSUE SPECIFICITY: High levels in skin, small intestine and salivary gland. Lower levels in lung, uterus and liver. Not detected in brain, kidney, muscle, heart or spleen. In skin, expressed in all epidermal layers but not in the dermis. In intestine, expressed exclusively in the epithelial cell layer of the villi. In liver, expressed at hepatocyte margins. Around the region of the wound, expressed in the upper half of the epidermis. Weakly expressed on the basilar side of the suprabasal layer of the epidermis at the wound's edge. Expressed strongly in the upper layer of the epidermis, especially in larger keratinocytes (PubMed:16382146). Expressed in undifferentiated primary keratinocytes (PubMed:18285451). Strongly expressed in ductal cells, and also expressed in acinar cells (PubMed:25232867). Expressed in hepatocytes and cholangiocytes (PubMed:25617501). {ECO:0000269|PubMed:12791695, ECO:0000269|PubMed:16382146, ECO:0000269|PubMed:18285451, ECO:0000269|PubMed:25232867, ECO:0000269|PubMed:25617501}. +Q60629 EPHA5_MOUSE Ephrin type-A receptor 5 (EC 2.7.10.1) (Brain-specific kinase) (CEK-7) (EPH homology kinase 1) (EHK-1) 876 97,056 Active site (1); Binding site (1); Chain (1); Domain (4); Glycosylation (2); Helix (6); Modified residue (4); Motif (1); Mutagenesis (4); Nucleotide binding (1); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 413 433 Helical. {ECO:0000255}. TOPO_DOM 27 412 Extracellular. {ECO:0000255}.; TOPO_DOM 434 876 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor tyrosine kinase which binds promiscuously GPI-anchored ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Among GPI-anchored ephrin-A ligands, EFNA5 most probably constitutes the cognate/functional ligand for EPHA5. Functions as an axon guidance molecule during development and may be involved in the development of the retinotectal, entorhino-hippocampal and hippocamposeptal pathways. Together with EFNA5 plays also a role in synaptic plasticity in adult brain through regulation of synaptogenesis. In addition to its function in the nervous system, the interaction of EPHA5 with EFNA5 mediates communication between pancreatic islet cells to regulate glucose-stimulated insulin secretion. {ECO:0000269|PubMed:12124402, ECO:0000269|PubMed:17448994}. PTM: Phosphorylated. Phosphorylation is stimulated by the ligand EFNA5. Dephosphorylation upon stimulation by glucose, inhibits EPHA5 forward signaling and results in insulin secretion. {ECO:0000269|PubMed:12124402, ECO:0000269|PubMed:17448994}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P54757}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, axon {ECO:0000250|UniProtKB:P54757}. Cell projection, dendrite {ECO:0000250|UniProtKB:P54756}. SUBUNIT: Heterotetramer upon binding of the ligand. The heterotetramer is composed of an ephrin dimer and a receptor dimer. Oligomerization is probably required to induce biological responses (By similarity). Interacts (via SAM domain) with SAMD5 (via SAM domain) (PubMed:29749928). {ECO:0000250, ECO:0000269|PubMed:29749928}. TISSUE SPECIFICITY: Specifically expressed in the brain. Highly expressed in hippocampus, tenia tecta, indusium griseum and piriform cortex. The highest level of expression is found in the CA3 region of the hippocampus and the pyramidal cell layer of the piriform cortex. In addition, elevated levels of expression are also found in amygdala, medial septum, nucleus of the diagonal band, and in olfactory bulb. Expressed in pancreatic islet cells (at protein level). Expressed in myogenic progenitor cells (PubMed:27446912). {ECO:0000269|PubMed:17448994, ECO:0000269|PubMed:27446912, ECO:0000269|PubMed:8145300}. +Q61772 EPHA7_MOUSE Ephrin type-A receptor 7 (EC 2.7.10.1) (Developmental kinase 1) (mDK-1) (EPH homology kinase 3) (EHK-3) (Embryonic brain kinase) (EBK) 998 111,860 Active site (1); Alternative sequence (6); Binding site (1); Chain (1); Compositional bias (1); Domain (5); Glycosylation (2); Modified residue (4); Motif (1); Nucleotide binding (1); Sequence conflict (5); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 556 576 Helical. {ECO:0000255}. TOPO_DOM 28 555 Extracellular. {ECO:0000255}.; TOPO_DOM 577 998 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor tyrosine kinase which binds promiscuously GPI-anchored ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Among GPI-anchored ephrin-A ligands, EFNA5 is a cognate/functional ligand for EPHA7 and their interaction regulates brain development modulating cell-cell adhesion and repulsion. Has a repellent activity on axons and is for instance involved in the guidance of corticothalamic axons and in the proper topographic mapping of retinal axons to the colliculus. May also regulate brain development through a caspase(CASP3)-dependent proapoptotic activity. Forward signaling may result in activation of components of the ERK signaling pathway including MAP2K1, MAP2K2, MAPK1 AND MAPK3 which are phosphorylated upon activation of EPHA7. Isoform 4 which lacks the kinase domain may regulate isoform 1 adhesive properties. {ECO:0000269|PubMed:15902206, ECO:0000269|PubMed:15996548, ECO:0000269|PubMed:16301174}. PTM: Phosphorylated. Isoform 4 inhibits isoform 1 phosphorylation and may regulate its function in adhesion. {ECO:0000269|PubMed:11089974}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:11089974}; Single-pass type I membrane protein {ECO:0000305|PubMed:11089974}. SUBUNIT: Heterotetramer upon binding of the ligand. The heterotetramer is composed of an ephrin dimer and a receptor dimer. Oligomerization is probably required to induce biological responses (By similarity). Interacts (via PDZ-binding motif) with GRIP1 and PICK1 (via PDZ domain). {ECO:0000250, ECO:0000269|PubMed:9883737}. TISSUE SPECIFICITY: Widely expressed in embryo. In adult, expression restricted to hippocampus, testis and spleen. Expressed in myogenic progenitor cells (PubMed:27446912). {ECO:0000269|PubMed:27446912}. +Q8CFD5 ERCC8_MOUSE DNA excision repair protein ERCC-8 (Cockayne syndrome WD repeat protein CSA homolog) 397 43,689 Chain (1); Modified residue (3); Repeat (5); Sequence conflict (2) Protein modification; protein ubiquitination. FUNCTION: Involved in transcription-coupled nucleotide excision repair. It is required for the recruitment of XAB2, HMGN1 and TCEA1/TFIIS to a transcription-coupled repair complex which removes RNA polymerase II-blocking lesions from the transcribed strand of active genes. It is the substrate-recognition component of the CSA complex (DCX(ERCC8) complex) which promotes the ubiquitination and subsequent proteasomal degradation of ERCC6 in a UV-dependent manner; ERCC6 degradation is essential for the recovery of RNA synthesis after transcription-coupled repair. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Part of the CSA complex (DCX(ERCC8) complex), a DCX E3 ubiquitin-protein ligase complex containing ERCC8, RBX1, DDB1 and CUL4A; the CSA complex interacts with RNA polymerase II; upon UV irradiation it interacts with the COP9 signalosome and preferentially with the hyperphosphorylated form of RNA polymerase II. Interacts with ERCC6 and KIAA1530/UVSSA. Interacts with a subunit of RNA polymerase II TFIIH. Interacts with DDB1. {ECO:0000250}. +Q8QZW3 F151A_MOUSE Protein FAM151A 608 66,681 Chain (1); Transmembrane (1) TRANSMEM 14 34 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q8QZV6 F161A_MOUSE Protein FAM161A 448 52,029 Chain (1); Coiled coil (1); Compositional bias (1); Cross-link (1) FUNCTION: Involved in ciliogenesis. {ECO:0000250|UniProtKB:Q3B820}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body. Cell projection, cilium. Note=Localized in the region between the outer and inner photoreceptor segments, corresponding to the photoreceptor connecting cilium. SUBUNIT: Interacts (via C-terminus) with microtubules. Interacts with LCA5, CEP290 and SDCCAG8. Interacts with FAM161B. Interacts with POC1B. Interacts with CEP78. {ECO:0000250|UniProtKB:Q3B820}. TISSUE SPECIFICITY: Expressed in the retina. {ECO:0000269|PubMed:20705278, ECO:0000269|PubMed:20705279}. +Q8CB59 F161B_MOUSE Protein FAM161B 589 66,969 Alternative sequence (2); Chain (1); Coiled coil (1); Sequence conflict (4) SUBUNIT: Interacts with FAM161A. {ECO:0000250}. +A2AIP0 F166B_MOUSE Protein FAM166B 273 30,251 Alternative sequence (4); Chain (1); Sequence conflict (1) +Q5XG69 F169A_MOUSE Soluble lamin-associated protein of 75 kDa (SLAP75) (Protein FAM169A) 665 73,240 Chain (1); Compositional bias (1); Erroneous initiation (2); Modified residue (7); Sequence conflict (2) SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000250}. Nucleus inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Nucleoplasmic side {ECO:0000250}. Note=Enriched at the nuclear lamina. {ECO:0000250}. +Q7TNF9 F117A_MOUSE Protein FAM117A 451 48,054 Alternative sequence (1); Chain (1); Coiled coil (1); Modified residue (9); Sequence conflict (2) +Q66LM6 F170A_MOUSE Protein FAM170A (Zinc finger domain-containing protein) (Zinc finger protein ZNFD) 333 37,392 Alternative sequence (1); Chain (1); Compositional bias (1); Modified residue (2); Zinc finger (1) FUNCTION: Acts as a nuclear transcription factor that positively regulates the expression of heat shock genes. Binds to heat shock promoter elements (HSE). {ECO:0000269|PubMed:22231842}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22231842}. DOMAIN: The N-terminus is necessary for nuclear localization. The C-terminus is necessary for transcriptional activity (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:22231842}. +E9PXT9 F170B_MOUSE Protein FAM170B (Acrosome-related protein) 378 43,766 Chain (1); Compositional bias (1) FUNCTION: Plays a role in fertilization through the acrosome reaction. {ECO:0000269|PubMed:26179146}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:26179146}. Cytoplasmic vesicle, secretory vesicle, acrosome outer membrane {ECO:0000269|PubMed:26179146}. SUBUNIT: Interacts with GOPC. {ECO:0000250|UniProtKB:A6NMN3}. TISSUE SPECIFICITY: Exclusively expressed in adult testis (at protein level). Expression first started at postnatal week 3 in round spermatids, elongated spermatids and mature sperm. {ECO:0000269|PubMed:26179146}. +A2A699 F1712_MOUSE Protein FAM171A2 822 87,487 Alternative sequence (1); Chain (1); Compositional bias (1); Glycosylation (4); Modified residue (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 316 336 Helical. {ECO:0000255}. TOPO_DOM 30 315 Extracellular. {ECO:0000255}.; TOPO_DOM 337 822 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q3TNH5 F172A_MOUSE Cotranscriptional regulator FAM172A 417 48,072 Active site (1); Alternative sequence (3); Chain (1); Glycosylation (1); Motif (1); Mutagenesis (3); Signal peptide (1) FUNCTION: Plays a role in the regulation of alternative splicing, by interacting with AGO2 and CHD7. Seems to be required for stabilizing protein-protein interactions at the chromatin-spliceosome interface (PubMed:29311329). May have hydrolase activity (PubMed:29311329). {ECO:0000269|PubMed:29311329}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29311329}. Cytoplasm {ECO:0000269|PubMed:29311329}. Endoplasmic reticulum {ECO:0000269|PubMed:29311329}. SUBUNIT: Interacts with AGO2 (PubMed:29311329). Found in a complex, composed of AGO2, CHD7 and FAM172A (PubMed:29311329). {ECO:0000269|PubMed:29311329}. +Q8K064 F174B_MOUSE Membrane protein FAM174B 153 16,213 Chain (1); Glycosylation (1); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 85 105 Helical. {ECO:0000255}. TOPO_DOM 28 84 Extracellular. {ECO:0000255}.; TOPO_DOM 106 153 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q8BR63 F177A_MOUSE Protein FAM177A1 207 23,578 Chain (1); Coiled coil (1); Erroneous initiation (1); Modified residue (3) +Q24JP3 F178B_MOUSE Protein FAM178B 464 52,581 Alternative sequence (4); Chain (1); Compositional bias (1); Sequence conflict (1) +Q9D3R5 F187A_MOUSE Ig-like V-type domain-containing protein FAM187A 417 47,878 Chain (1); Compositional bias (1); Disulfide bond (1); Domain (1); Glycosylation (2); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 378 398 Helical. {ECO:0000255}. TOPO_DOM 19 377 Extracellular. {ECO:0000255}.; TOPO_DOM 399 417 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q6A044 F1891_MOUSE Protein FAM189A1 515 54,479 Alternative sequence (1); Chain (1); Compositional bias (1); Erroneous initiation (1); Transmembrane (4) TRANSMEM 31 51 Helical. {ECO:0000255}.; TRANSMEM 65 85 Helical. {ECO:0000255}.; TRANSMEM 89 109 Helical. {ECO:0000255}.; TRANSMEM 176 196 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q7TPG8 F19A1_MOUSE Protein FAM19A1 (Chemokine-like protein TAFA-1) 133 14,873 Chain (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +Q7TPG7 F19A2_MOUSE Protein FAM19A2 (Chemokine-like protein TAFA-2) 131 14,647 Chain (1); Erroneous initiation (1); Signal peptide (1) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +Q80ZQ9 F206A_MOUSE Protein Simiate (Protein FAM206A) 193 21,597 Chain (1); Erroneous initiation (1) FUNCTION: Actin-binding protein that regulates actin polymerization, filopodia dynamics and increases the branching of proximal dendrites of developing neurons. {ECO:0000269|PubMed:24782708}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:24349419}. Cell projection, lamellipodium {ECO:0000269|PubMed:24782708}. Nucleus {ECO:0000269|PubMed:24782708}. Cell projection, growth cone {ECO:0000269|PubMed:24782708}. Cell projection, dendrite {ECO:0000269|PubMed:24782708}. Note=Localizes to somata and dendrites in cortical neurons. Colocalizes with G- and F-actin in growth cones and proximal dendrites (PubMed:24782708). Colocalizes in the nucleus with PTK2 (PubMed:24782708). {ECO:0000269|PubMed:24782708}. SUBUNIT: Interacts with F-actin (PubMed:24782708). Interacts with G-actin (PubMed:24782708). {ECO:0000269|PubMed:24782708}. TISSUE SPECIFICITY: Detected (at protein level) in liver, lung, heart, spleen, kidney, and ovaries. In brain expression is higher in the hippocampus, the nuclear layer of the cerebellum, the cortex and the caudoputamen. {ECO:0000269|PubMed:24349419}. +Q7TPG5 F19A4_MOUSE Protein FAM19A4 (Chemokine-like protein TAFA-4) 135 15,018 Chain (1); Frameshift (1); Sequence conflict (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +Q8C627 F221B_MOUSE Protein FAM221B 487 54,292 Alternative sequence (2); Chain (1); Modified residue (1); Sequence conflict (2) +Q9D518 F227B_MOUSE Protein FAM227B 532 62,785 Chain (1); Coiled coil (1); Sequence caution (1); Sequence conflict (1) +Q8CDW1 F228A_MOUSE Protein FAM228A 299 34,457 Alternative sequence (2); Chain (1); Modified residue (1) +Q497Q6 F228B_MOUSE Protein FAM228B 232 27,823 Alternative sequence (2); Chain (1); Frameshift (1) +B2KGE5 F229A_MOUSE Protein FAM229A 128 13,171 Chain (1) +Q8CC14 F216B_MOUSE Protein FAM216B 138 15,571 Chain (1) +Q14DQ1 F219B_MOUSE Protein FAM219B 197 21,006 Alternative sequence (2); Chain (1); Modified residue (3) +Q3UZD7 F71F1_MOUSE Protein FAM71F1 (Protein FAM137A) 341 38,687 Chain (1) +Q9CZL2 F241A_MOUSE Uncharacterized protein FAM241A 131 14,511 Chain (1); Modified residue (1); Transmembrane (1) TRANSMEM 99 119 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000255}. +O08914 FAAH1_MOUSE Fatty-acid amide hydrolase 1 (EC 3.5.1.99) (Anandamide amidohydrolase 1) (Oleamide hydrolase 1) 579 63,221 Active site (3); Binding site (2); Chain (1); Intramembrane (1); Modified residue (1); Region (1); Sequence conflict (2); Topological domain (2); Transmembrane (1) INTRAMEM 404 433 {ECO:0000250}. TRANSMEM 9 29 Helical. {ECO:0000255}. TOPO_DOM 30 403 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 434 579 Cytoplasmic. {ECO:0000250}. FUNCTION: Degrades bioactive fatty acid amides like oleamide, the endogenous cannabinoid, anandamide and myristic amide to their corresponding acids, thereby serving to terminate the signaling functions of these molecules. Hydrolyzes polyunsaturated substrate anandamide preferentially as compared to monounsaturated substrates (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. Golgi apparatus membrane; Single-pass membrane protein. Note=Seems to be associated with the endoplasmic reticulum and/or Golgi apparatus. SUBUNIT: Homodimer. {ECO:0000250}. +P16294 FA9_MOUSE Coagulation factor IX (EC 3.4.21.22) (Christmas factor) [Cleaved into: Coagulation factor IXa light chain; Coagulation factor IXa heavy chain] 471 52,978 Active site (3); Chain (3); Disulfide bond (11); Domain (4); Glycosylation (8); Metal binding (28); Modified residue (17); Propeptide (2); Sequence conflict (2); Signal peptide (1); Site (2) FUNCTION: Factor IX is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active form in the presence of Ca(2+) ions, phospholipids, and factor VIIIa. {ECO:0000250|UniProtKB:P00740}. PTM: Activated by factor XIa, which excises the activation peptide. The propeptide can also be removed by snake venom protease. {ECO:0000250|UniProtKB:P00740}.; PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000250|UniProtKB:P00740}.; PTM: Predominantly O-glucosylated at Ser-99 by POGLUT1 in vitro. {ECO:0000250|UniProtKB:P00740}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P00740}. SUBUNIT: Heterodimer of a light chain and a heavy chain; disulfide-linked. Interacts with SERPINC1. {ECO:0000250|UniProtKB:P00740}. DOMAIN: Calcium binds to the gamma-carboxyglutamic acid (Gla) residues in the Gla domain. Calcium can also bind, with stronger affinity, to another site beyond the Gla domain. Under physiological ion concentrations, Ca(2+) is displaced by Mg(2+) from some of the gammaglutamate residues in the N-terminal Gla domain. This leads to a subtle conformation change that may affect the interaction with its binding protein. {ECO:0000250|UniProtKB:P00741}. TISSUE SPECIFICITY: Detected in liver. {ECO:0000269|PubMed:2323576}. +Q9Z0R9 FADS2_MOUSE Acyl-CoA 6-desaturase (EC 1.14.19.3) (Delta(6) fatty acid desaturase) (D6D) (Delta(6) desaturase) (Delta-6 desaturase) (Fatty acid desaturase 2) 444 52,387 Chain (1); Domain (1); Motif (3); Topological domain (5); Transmembrane (4) TRANSMEM 131 151 Helical. {ECO:0000255}.; TRANSMEM 153 173 Helical. {ECO:0000255}.; TRANSMEM 265 285 Helical. {ECO:0000255}.; TRANSMEM 306 326 Helical. {ECO:0000255}. TOPO_DOM 1 130 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 152 152 Lumenal. {ECO:0000255}.; TOPO_DOM 174 264 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 286 305 Lumenal. {ECO:0000255}.; TOPO_DOM 327 444 Cytoplasmic. {ECO:0000255}. Lipid metabolism; polyunsaturated fatty acid biosynthesis. FUNCTION: Acts as a fatty acyl-coenzyme A (CoA) desaturase that introduces a cis double bond at carbon 6 of the fatty acyl chain. Involved in biosynthesis of highly unsaturated fatty acids (HUFA) from the essential polyunsaturated fatty acids (PUFA) linoleic acid (LA) (18:2n-6) and alpha-linolenic acid (ALA) (18:3n-3) precursors. Catalyzes the first and rate limiting step in this pathway which is the desaturation of LA (18:2n-6) and ALA (18:3n-3) into gamma-linoleate (GLA) (18:3n-6) and stearidonate (18:4n-3), respectively (PubMed:9867867). Subsequently, in the biosynthetic pathway of HUFA n-3 series, desaturates tetracosapentaenoate (24:5n-3) to tetracosahexaenoate (24:6n-3), which is then converted to docosahexaenoate (DHA)(22:6n-3), an important lipid for nervous system function (By similarity). Desaturates palmitate to produce the mono-unsaturated fatty acid sapienate, the most abundant fatty acid in sebum (By similarity). Also desaturates (11E)-octadecenoate (trans-vaccenoate)(18:1n-9), a metabolite in the biohydrogenation pathway of LA (18:2n-6) (By similarity). {ECO:0000250|UniProtKB:O95864, ECO:0000250|UniProtKB:Q9Z122, ECO:0000269|PubMed:9867867}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. DOMAIN: The histidine box domains may contain the active site and/or be involved in metal ion binding. TISSUE SPECIFICITY: Highly expressed in the adrenal gland, liver, brain, and testis, tissues where lipogenesis and steroidogenesis are active. Also detected in lung, heart, and skeletal muscle. {ECO:0000269|PubMed:11792729, ECO:0000269|PubMed:9867867}. +Q9JJE7 FADS3_MOUSE Fatty acid desaturase 3 (EC 1.14.19.-) (Delta(13) fatty acid desaturase) (Delta(13) desaturase) 449 51,469 Chain (1); Domain (1); Motif (3); Sequence conflict (3); Topological domain (5); Transmembrane (4) TRANSMEM 135 155 Helical. {ECO:0000255}.; TRANSMEM 164 184 Helical. {ECO:0000255}.; TRANSMEM 269 289 Helical. {ECO:0000255}.; TRANSMEM 311 331 Helical. {ECO:0000255}. TOPO_DOM 1 134 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 156 163 Lumenal. {ECO:0000255}.; TOPO_DOM 185 268 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 290 310 Lumenal. {ECO:0000255}.; TOPO_DOM 332 449 Cytoplasmic. {ECO:0000255}. Lipid metabolism; polyunsaturated fatty acid biosynthesis. FUNCTION: Acts as a methyl-end fatty acyl coenzyme A (CoA) desaturase that introduces a cis double bond between the preexisting double bond and the terminal methyl group of the fatty acyl chain. Desaturates (11E)-octadecenoate (trans-vaccenoate) at carbon 13 to generate (11E,13Z)-octadecadienoate, likely participating in the biohydrogenation pathway of linoleic acid (LA) (18:2n-6). {ECO:0000250|UniProtKB:Q8K1P9}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. DOMAIN: The histidine box domains may contain the active site and/or be involved in metal ion binding. TISSUE SPECIFICITY: Highly expressed in liver and kidney (at protein level). {ECO:0000269|PubMed:19752397}. +P54731 FAF1_MOUSE FAS-associated factor 1 649 73,863 Chain (1); Domain (2); Modified residue (3); Sequence conflict (3) FUNCTION: Ubiquitin-binding protein (By similarity). Required for the progression of DNA replication forks by targeting DNA replication licensing factor CDT1 for degradation (By similarity). Potentiates but cannot initiate FAS-induced apoptosis (PubMed:8524870). {ECO:0000250|UniProtKB:Q9UNN5, ECO:0000269|PubMed:8524870}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UNN5}. SUBUNIT: Interacts with CDT1 and ATPase VCP/p97. Interacts (via UBA domain) with FAS (via death domain). Interacts (via UBA domain) with NLRP12 (via DAPIN/PYRIN domain). {ECO:0000250|UniProtKB:Q9UNN5}. +Q8BSN9 FAKD3_MOUSE FAST kinase domain-containing protein 3, mitochondrial 661 75,317 Alternative sequence (3); Chain (1); Domain (1); Frameshift (1); Sequence conflict (7); Transit peptide (1) FUNCTION: Required for normal mitochondrial respiration. Increases steady-state levels and half-lives of a subset of mature mitochondrial mRNAs MT-ND2, MT-ND3, MT-CYTB, MT-CO2, and MT-ATP8/6. Promotes MT-CO1 mRNA translation and increases mitochondrial complex IV assembly and activity. {ECO:0000250|UniProtKB:Q14CZ7}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q14CZ7}. DOMAIN: RAP domain is required for FASTKD3 function in mRNA stability and translation. {ECO:0000250|UniProtKB:Q14CZ7}. TISSUE SPECIFICITY: Expression detected in spleen, testis, colon, heart, smooth muscle, kidney, brain, lung, liver, brown and white adipose tissue with highest expression in testis and smooth muscle. {ECO:0000269|PubMed:20869947}. +Q91YM4 FAKD4_MOUSE FAST kinase domain-containing protein 4 (Protein TBRG4) (Transforming growth factor beta regulator 4) 630 71,513 Alternative sequence (1); Chain (1); Domain (1); Erroneous initiation (2); Erroneous termination (1); Sequence conflict (5); Transit peptide (1) FUNCTION: Plays a role in processing of mitochondrial RNA precursors and in stabilization of a subset of mature mitochondrial RNA species, such as MT-CO1, MT-CO2, MT-CYB, MT-CO3, MT-ND3, MT-ND5 and MT-ATP8/6. May play a role in cell cycle progression. {ECO:0000250|UniProtKB:Q969Z0}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:Q969Z0}. TISSUE SPECIFICITY: Expression detected in spleen, testis, colon, heart, smooth muscle, kidney, brain, lung, liver, brown and white adipose tissue with highest expression in testis, heart, smooth muscle and brown adipose tissue. {ECO:0000269|PubMed:20869947}. +Q9QVP9 FAK2_MOUSE Protein-tyrosine kinase 2-beta (EC 2.7.10.2) (Calcium-dependent tyrosine kinase) (CADTK) (Calcium-regulated non-receptor proline-rich tyrosine kinase) (Cell adhesion kinase beta) (CAK-beta) (CAKB) (Focal adhesion kinase 2) (FADK 2) (Proline-rich tyrosine kinase 2) (Related adhesion focal tyrosine kinase) (RAFTK) 1009 115,794 Active site (1); Binding site (1); Chain (1); Compositional bias (2); Domain (2); Modified residue (15); Mutagenesis (1); Nucleotide binding (2); Region (2); Sequence conflict (2) FUNCTION: Non-receptor protein-tyrosine kinase that regulates reorganization of the actin cytoskeleton, cell polarization, cell migration, adhesion, spreading and bone remodeling. Plays a role in the regulation of the humoral immune response, and is required for normal levels of marginal B-cells in the spleen and normal migration of splenic B-cells. Required for normal macrophage polarization and migration towards sites of inflammation. Regulates cytoskeleton rearrangement and cell spreading in T-cells, and contributes to the regulation of T-cell responses. Promotes osteoclastic bone resorption; this requires both PTK2B/PYK2 and SRC. May inhibit differentiation and activity of osteoprogenitor cells. Functions in signaling downstream of integrin and collagen receptors, immune receptors, G-protein coupled receptors (GPCR), cytokine, chemokine and growth factor receptors, and mediates responses to cellular stress. Forms multisubunit signaling complexes with SRC and SRC family members upon activation; this leads to the phosphorylation of additional tyrosine residues, creating binding sites for scaffold proteins, effectors and substrates. Regulates numerous signaling pathways. Promotes activation of phosphatidylinositol 3-kinase and of the AKT1 signaling cascade. Promotes activation of NOS3. Regulates production of the cellular messenger cGMP. Promotes activation of the MAP kinase signaling cascade, including activation of MAPK1/ERK2, MAPK3/ERK1 and MAPK8/JNK1. Promotes activation of Rho family GTPases, such as RHOA and RAC1. Recruits the ubiquitin ligase MDM2 to P53/TP53 in the nucleus, and thereby regulates P53/TP53 activity, P53/TP53 ubiquitination and proteasomal degradation. Acts as a scaffold, binding to both PDPK1 and SRC, thereby allowing SRC to phosphorylate PDPK1 at 'Tyr-9, 'Tyr-373', and 'Tyr-376' (By similarity). Promotes phosphorylation of NMDA receptors by SRC family members, and thereby contributes to the regulation of NMDA receptor ion channel activity and intracellular Ca(2+) levels. May also regulate potassium ion transport by phosphorylation of potassium channel subunits. Phosphorylates SRC; this increases SRC kinase activity. Phosphorylates ASAP1, NPHP1, KCNA2 and SHC1. Promotes phosphorylation of ASAP2, RHOU and PXN; this requires both SRC and PTK2/PYK2 (By similarity). {ECO:0000250, ECO:0000269|PubMed:10881171, ECO:0000269|PubMed:11238453, ECO:0000269|PubMed:12960403, ECO:0000269|PubMed:14739300, ECO:0000269|PubMed:17537919, ECO:0000269|PubMed:17698736, ECO:0000269|PubMed:17846174, ECO:0000269|PubMed:18587400, ECO:0000269|PubMed:19561089, ECO:0000269|PubMed:19880522, ECO:0000269|PubMed:20688918, ECO:0000269|PubMed:21640103}. PTM: Phosphorylated on tyrosine residues in response to various stimuli that elevate the intracellular calcium concentration; this activation is indirect and may be mediated by production of reactive oxygen species (ROS). Tyr-402 is the major autophosphorylation site, but other kinases can also phosphorylate Tyr-402. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Phosphorylation at Tyr-402 promotes interaction with SRC and SRC family members, leading to phosphorylation at Tyr-579; Tyr-580 and Tyr-881. Phosphorylation at Tyr-881 is important for interaction with GRB2. Phosphorylated on tyrosine residues upon activation of FGR and PKC. Recruitment by NPHP1 to cell matrix adhesions initiates Tyr-402 phosphorylation. In monocytes, adherence to substrata is required for tyrosine phosphorylation and kinase activation. Angiotensin II, thapsigargin and L-alpha-lysophosphatidic acid (LPA) also induce autophosphorylation and increase kinase activity. Phosphorylation by MYLK promotes ITGB2 activation and is thus essential to trigger neutrophil transmigration during lung injury. Dephosphorylated by PTPN12 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell junction, focal adhesion. Cell projection, lamellipodium {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Nucleus {ECO:0000250}. Note=Colocalizes with integrins at the cell periphery (By similarity). Interaction with NPHP1 induces the membrane-association of the kinase. Colocalizes with PXN at the microtubule-organizing center. The tyrosine phosphorylated form is detected at cell-cell contacts. {ECO:0000250}. SUBUNIT: Homodimer, or homooligomer. Interacts with KCNA2 (By similarity). Interacts with NPHP1, ASAP1, ASAP2, ARHGAP26, SKAP2 and TGFB1I1. The Tyr-402 phosphorylated form interacts with SRC (via SH2 domain) and SRC family members. Forms a signaling complex with EPHA1, LCK and phosphatidylinositol 3-kinase; upon activation by EFNA1. Interacts with GRB2 (via SH2 domain). Interacts with P53/TP53 and MDM2. Interacts with MYLK. Interacts with BCAR1. Interacts with RB1CC1. Interacts with RHOU. Interacts with VAV1. Interacts with PDPK1. Interacts with DLG4. Interacts with LPXN and PTPN12. Interacts with SIRPA and SH2D3C. Interacts (hypophosphorylated) with PXN. Interacts with ARHGAP10. {ECO:0000250|UniProtKB:P70600, ECO:0000269|PubMed:10469599, ECO:0000269|PubMed:11238453, ECO:0000269|PubMed:11493697, ECO:0000269|PubMed:12486027, ECO:0000269|PubMed:12674328, ECO:0000269|PubMed:14739300, ECO:0000269|PubMed:17698736, ECO:0000269|PubMed:18587400, ECO:0000269|PubMed:21195757, ECO:0000269|PubMed:8940124, ECO:0000269|PubMed:9422762}. +Q9D309 FAM3B_MOUSE Protein FAM3B (Cytokine-like protein 2-21) (Pancreatic-derived factor) (PANDER) 235 26,152 Beta strand (10); Chain (1); Disulfide bond (2); Glycosylation (1); Helix (4); Sequence conflict (1); Signal peptide (1); Turn (6) FUNCTION: Induces apoptosis of alpha and beta cells in a dose- and time-dependent manner. {ECO:0000269|PubMed:23333428}. PTM: O-glycosylated. {ECO:0000269|PubMed:23333428}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Present in insulin secretory granules and likely cosecreted with insulin. {ECO:0000250}. TISSUE SPECIFICITY: Expressed at high levels in the pancreas and, to a lesser extent, in small intestine and prostate. Also detected in stomach, testis and fetal liver. In the pancreas, localized in the islets of Langerhans; in the testis, found primarily in the round spermatids; in the CNS, found in the Purkinje cell layer of the cerebellum and in nerve cell bodies of numerous brainstem nuclei. +P97805 FAM3D_MOUSE Protein FAM3D (Oncoprotein-induced protein 1) (Protein EF-7) 223 24,988 Chain (1); Disulfide bond (2); Glycosylation (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q8BGE5 FANCM_MOUSE Fanconi anemia group M protein homolog (Protein FACM) (EC 3.6.4.13) (ATP-dependent RNA helicase FANCM) 2021 226,018 Alternative sequence (5); Chain (1); Domain (2); Erroneous initiation (1); Modified residue (2); Motif (1); Nucleotide binding (1); Region (1) FUNCTION: DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. Required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. In complex with CENPS and CENPX, binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA) and Holliday junction substrates. Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX. In complex with FAAP24, efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates. In vitro, on its own, strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA. {ECO:0000250|UniProtKB:Q8IYD8}. PTM: Phosphorylated; hyperphosphorylated in response to genotoxic stress. {ECO:0000250|UniProtKB:Q8IYD8}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8IYD8}. SUBUNIT: Component of the Fanconi anemia (FA) core complex, which consists of CENPS, CENPX, FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL, FANCM, FAAP24 and FAAP100. The FA core complex associates with Bloom syndrome (BLM) complex, which consists of at least BLM, DNA topoisomerase 3-alpha/TOP3A, RMI1/BLAP75, RPA1/RPA70 and RPA2/RPA32. This supercomplex between FA and BLM complexes has been called BRAFT. Forms a discrete complex with CENPS and CENPX, called FANCM-MHF; this interaction stimulates DNA binding and replication fork remodeling by FANCM and stabilizes the binding partners. Forms a heterodimer with FAAP24; this interaction increases FANCM single-stranded DNA-binding activity. {ECO:0000250|UniProtKB:Q8IYD8}. +Q8BX79 GPR21_MOUSE Probable G-protein coupled receptor 21 349 39,509 Chain (1); Glycosylation (2); Topological domain (8); Transmembrane (7) TRANSMEM 33 53 Helical; Name=1. {ECO:0000255}.; TRANSMEM 76 96 Helical; Name=2. {ECO:0000255}.; TRANSMEM 105 125 Helical; Name=3. {ECO:0000255}.; TRANSMEM 148 168 Helical; Name=4. {ECO:0000255}.; TRANSMEM 192 212 Helical; Name=5. {ECO:0000255}.; TRANSMEM 253 273 Helical; Name=6. {ECO:0000255}.; TRANSMEM 284 304 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 32 Extracellular. {ECO:0000255}.; TOPO_DOM 54 75 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 97 104 Extracellular. {ECO:0000255}.; TOPO_DOM 126 147 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 169 191 Extracellular. {ECO:0000255}.; TOPO_DOM 213 252 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 274 283 Extracellular. {ECO:0000255}.; TOPO_DOM 305 349 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q9ES90 GPR35_MOUSE G-protein coupled receptor 35 (Kynurenic acid receptor) (KYNA receptor) 307 34,152 Chain (1); Disulfide bond (1); Glycosylation (2); Topological domain (8); Transmembrane (7) TRANSMEM 19 39 Helical; Name=1. {ECO:0000255}.; TRANSMEM 54 74 Helical; Name=2. {ECO:0000255}.; TRANSMEM 89 110 Helical; Name=3. {ECO:0000255}.; TRANSMEM 130 150 Helical; Name=4. {ECO:0000255}.; TRANSMEM 177 197 Helical; Name=5. {ECO:0000255}.; TRANSMEM 218 238 Helical; Name=6. {ECO:0000255}.; TRANSMEM 258 278 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 18 Extracellular. {ECO:0000255}.; TOPO_DOM 40 53 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 75 88 Extracellular. {ECO:0000255}.; TOPO_DOM 111 129 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 151 176 Extracellular. {ECO:0000255}.; TOPO_DOM 198 217 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 239 257 Extracellular. {ECO:0000255}.; TOPO_DOM 279 307 Cytoplasmic. {ECO:0000255}. FUNCTION: Acts as a receptor for kynurenic acid, an intermediate in the tryptophan metabolic pathway. The activity of this receptor is mediated by G-proteins that elicit calcium mobilization and inositol phosphate production through G(qi/o) proteins. {ECO:0000269|PubMed:16754668}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Predominantly expressed in immune and gastrointestinal tissues. {ECO:0000269|PubMed:16754668}. +Q9QY42 GPR37_MOUSE Prosaposin receptor GPR37 (G-protein coupled receptor 37) 600 66,775 Alternative sequence (3); Chain (1); Compositional bias (2); Disulfide bond (1); Glycosylation (3); Sequence conflict (9); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 253 273 Helical; Name=1. {ECO:0000255}.; TRANSMEM 287 307 Helical; Name=2. {ECO:0000255}.; TRANSMEM 323 343 Helical; Name=3. {ECO:0000255}.; TRANSMEM 367 387 Helical; Name=4. {ECO:0000255}.; TRANSMEM 431 451 Helical; Name=5. {ECO:0000255}.; TRANSMEM 481 501 Helical; Name=6. {ECO:0000255}.; TRANSMEM 519 539 Helical; Name=7. {ECO:0000255}. TOPO_DOM 27 252 Extracellular. {ECO:0000255}.; TOPO_DOM 274 286 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 308 322 Extracellular. {ECO:0000255}.; TOPO_DOM 344 366 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 388 430 Extracellular. {ECO:0000255}.; TOPO_DOM 452 480 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 502 518 Extracellular. {ECO:0000255}.; TOPO_DOM 540 600 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for the neuroprotective and glioprotective factor prosaposin. Ligand binding induces endocytosis, followed by an ERK phosphorylation cascade (By similarity). {ECO:0000250}. PTM: Ubiquitinated by PRKN in the presence of ubiquitin-conjugating enzymes in the endoplasmic reticulum. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Forms a complex with PRKN, STUB1 and HSP70. The amount of STUB1 in the complex increases during ER stress. STUB1 promotes the dissociation of HSP70 from PRKN, thus facilitating PRKN-mediated GPR37 ubiquitination. Interacts with PACRG (By similarity). {ECO:0000250}. +Q71FD7 FBLI1_MOUSE Filamin-binding LIM protein 1 (FBLP-1) (CSX-associated LIM) 375 41,026 Chain (1); Compositional bias (1); Domain (3); Region (3); Sequence conflict (1) FUNCTION: Serves as an anchoring site for cell-ECM adhesion proteins and filamin-containing actin filaments. Is implicated in cell shape modulation (spreading) and motility. May participate in the regulation of filamin-mediated cross-linking and stabilization of actin filaments. May also regulate the assembly of filamin-containing signaling complexes that control actin assembly. Promotes dissociation of FLNA from ITGB3 and ITGB7. Promotes activation of integrins and regulates integrin-mediated cell-cell adhesion (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q8WUP2}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:Q8WUP2}. Note=Associated with actin stress fiber at cell-ECM focal adhesion sites. Recruited and localized at actin stress fibers and clustered at cell-EMC adhesion sites through interaction with FERMT2. {ECO:0000250|UniProtKB:Q8WUP2}. SUBUNIT: Interacts with FERMT2, FLNA, FLNB and FLNC (By similarity). Interacts with NKX2-5. {ECO:0000250, ECO:0000269|PubMed:14757752}. DOMAIN: The N-terminal region is intrinsically disordered. {ECO:0000250}. +Q7TQF2 FBX10_MOUSE F-box only protein 10 950 104,478 Chain (1); Domain (1); Erroneous initiation (1); Modified residue (2); Repeat (17); Sequence conflict (1) Protein modification; protein ubiquitination. FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. The SCF(FBXO10) complex mediates ubiquitination and degradation of BCL2, an antiapoptotic protein, thereby playing a role in apoptosis by controlling the stability of BCL2. {ECO:0000250|UniProtKB:Q9UK96}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UK96}. SUBUNIT: Component of the SCF(FBXO10) complex consisting of CUL1, SKP1 and FBXO10. Interacts with BCL2. Interacts with PRDM1. {ECO:0000250|UniProtKB:Q9UK96}. +Q9QZN0 FBX15_MOUSE F-box only protein 15 433 49,486 Chain (1); Domain (1); Erroneous initiation (1) FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. {ECO:0000250}. SUBUNIT: Directly interacts with SKP1 and CUL1. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:10531037, ECO:0000269|PubMed:12665572}. +Q8VDH1 FBX21_MOUSE F-box only protein 21 627 72,173 Alternative sequence (1); Chain (1); Domain (1); Erroneous initiation (1); Sequence conflict (2) FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. {ECO:0000250}. SUBUNIT: Directly interacts with SKP1 and CUL1. {ECO:0000250}. +Q9D417 FBX24_MOUSE F-box only protein 24 589 65,429 Chain (1); Domain (1); Repeat (1) FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. {ECO:0000250}. SUBUNIT: Directly interacts with SKP1 and CUL1. {ECO:0000250}. +Q3USJ8 FCSD2_MOUSE F-BAR and double SH3 domains protein 2 (SH3 multiple domains protein 3) 740 84,282 Alternative sequence (2); Chain (1); Coiled coil (1); Compositional bias (1); Domain (3); Erroneous initiation (1); Modified residue (2); Sequence conflict (1) SUBUNIT: Interacts with CASK and MAGI1. CASK inhibits interaction with MAGI1 (By similarity). {ECO:0000250}. +Q80UW2 FBX2_MOUSE F-box only protein 2 297 33,676 Beta strand (15); Chain (1); Compositional bias (1); Domain (2); Helix (7); Modified residue (1); Mutagenesis (4); Region (2); Site (2); Turn (3) Protein modification; protein ubiquitination. FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Involved in the endoplasmic reticulum-associated degradation pathway (ERAD) for misfolded lumenal proteins by recognizing and binding sugar chains on unfolded glycoproteins that are retrotranslocated into the cytosol and promoting their ubiquitination and subsequent degradation. Prevents formation of cytosolic aggregates of unfolded glycoproteins that have been retrotranslocated into the cytosol. Able to recognize and bind denatured glycoproteins, preferentially those of the high-mannose type. {ECO:0000269|PubMed:12140560, ECO:0000269|PubMed:14990996, ECO:0000269|PubMed:15723043, ECO:0000269|PubMed:17215248, ECO:0000269|PubMed:17720138}. SUBCELLULAR LOCATION: Cytoplasm. Microsome membrane; Peripheral membrane protein; Cytoplasmic side. SUBUNIT: Component of the SCF(FBXO2) complex consisting of CUL1, RBX1, SKP1 and FBXO2. Predominantly detected as heterodimer with SKP1; the heterodimer with SKP1 is not part of the SCF(FBXO2) complex. {ECO:0000269|PubMed:12140560, ECO:0000269|PubMed:14990996, ECO:0000269|PubMed:17215248}. TISSUE SPECIFICITY: Detected in brain and cochlea, in epithelial support cells and hair cells of the organ of Corti (at protein level). {ECO:0000269|PubMed:17215248, ECO:0000269|PubMed:17494702}. +Q8R089 FBRS_MOUSE Probable fibrosin-1 466 49,038 Chain (1); Compositional bias (2); Cross-link (1); Erroneous initiation (1); Frameshift (1); Modified residue (3); Sequence caution (1); Sequence conflict (1) +P0DJI6 FCOR_MOUSE Foxo1-corepressor (FCoR) (EC 2.3.1.-) (Foxo1 CoRepressor) 106 11,233 Chain (1); Modified residue (1); Motif (1); Mutagenesis (8) FUNCTION: Regulator of adipocytes that acts by repressing FOXO1 transcriptional activity. Acts by promoting acetylation of FOXO1, both by preventing the interaction between FOXO1 and SIRT1 deacetylase, and by mediating acetyltransferase activity in vitro. Regulates insulin sensitivity and energy metabolism. {ECO:0000269|PubMed:22510882}. PTM: Phosphorylated at Thr-93 by PKA, leading to import into the nucleus. {ECO:0000269|PubMed:22510882}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:22510882}. Nucleus {ECO:0000269|PubMed:22510882}. Note=Imported into the nucleus following phosphorylation at Thr-93 upon treatment of cells with forskolin. Probably shuttles between the nucleus and the cytoplasm. SUBUNIT: Interacts with FOXO1 (via N-terminal domain); the interaction is direct, occurs in a forskolin-independent manner that prevents SIRT1 binding to FOXO1. Interacts with FOXO3. Does not interact with FOXO4. {ECO:0000269|PubMed:22510882}. TISSUE SPECIFICITY: Expressed in adipocytes. Expressed in brown and white adipose tissue but not in liver. Protein levels in brown and white adipose tissues decrease following fasting (at protein level). Expressed in white and brown adipose tissues. Expressed in adipocytes. Not expressed in liver, skeletal muscle and brain. {ECO:0000269|PubMed:22510882}. +P20490 FCERB_MOUSE High affinity immunoglobulin epsilon receptor subunit beta (FcERI) (Fc epsilon receptor I beta-chain) (IgE Fc receptor subunit beta) (Membrane-spanning 4-domains subfamily A member 2) 235 25,963 Chain (1); Modified residue (4); Topological domain (5); Transmembrane (4) TRANSMEM 52 71 Helical. {ECO:0000255}.; TRANSMEM 90 109 Helical. {ECO:0000255}.; TRANSMEM 123 142 Helical. {ECO:0000255}.; TRANSMEM 172 191 Helical. {ECO:0000255}. TOPO_DOM 1 51 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 72 89 Extracellular. {ECO:0000255}.; TOPO_DOM 110 122 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 143 171 Extracellular. {ECO:0000255}.; TOPO_DOM 192 235 Cytoplasmic. {ECO:0000255}. FUNCTION: High affinity receptor that binds to the Fc region of immunoglobulins epsilon. Aggregation of FCER1 by multivalent antigens is required for the full mast cell response, including the release of preformed mediators (such as histamine) by degranulation and de novo production of lipid mediators and cytokines. Also mediates the secretion of important lymphokines. Binding of allergen to receptor-bound IgE leads to cell activation and the release of mediators responsible for the manifestations of allergy. {ECO:0000269|PubMed:19001085}. PTM: Phosphorylated on tyrosine residues by LYN. {ECO:0000269|PubMed:16272347}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SUBUNIT: Tetramer of an alpha chain, a beta chain, and two disulfide linked gamma chains. Binds LILRB1. Interacts with FGR (By similarity). Interacts with FGR and FES/FPS. Interacts with LYN. {ECO:0000250, ECO:0000269|PubMed:16272347, ECO:0000269|PubMed:19001085}. +Q8CAT8 FBX48_MOUSE F-box only protein 48 161 18,762 Chain (1); Domain (1); Sequence conflict (1) +Q5SRY7 FBW1B_MOUSE F-box/WD repeat-containing protein 11 (F-box and WD repeats protein beta-TrCP2) (F-box/WD repeat-containing protein 1B) (Homologous to Slimb protein) (HOS) 542 62,063 Alternative sequence (3); Chain (1); Domain (1); Frameshift (1); Region (1); Repeat (7); Sequence conflict (2) FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Probably recognizes and binds to phosphorylated target proteins. SCF(FBXW11) mediates the ubiquitination of phosphorylated CTNNB1 and participates in Wnt signaling. SCF(FBXW11) mediates the ubiquitination of phosphorylated NFKBIA, which degradation frees the associated NFKB1 to translocate into the nucleus and to activate transcription. SCF(FBXW11) mediates the ubiquitination of IFNAR1. SCF(FBXW11) mediates the ubiquitination of CEP68; this is required for centriole separation during mitosis (By similarity). Involved in the oxidative stress-induced a ubiquitin-mediated decrease in RCAN1. Mediates the degradation of CDC25A induced by ionizing radiation in cells progressing through S phase and thus may function in the intra-S-phase checkpoint. Has an essential role in the control of the clock-dependent transcription via degradation of phosphorylated PER1 and phosphorylated PER2. SCF(FBXW11) mediates the ubiquitination of CYTH1, and probably CYTH2 (By similarity). {ECO:0000250|UniProtKB:Q9UKB1, ECO:0000269|PubMed:11896578, ECO:0000269|PubMed:18782782}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18782782}. Nucleus {ECO:0000269|PubMed:18782782}. SUBUNIT: Self-associates. Component of the SCF(FBXW11) complex formed of CUL1, SKP1, RBX1 and a FBXW11 dimer. Interacts with BTRC, BST2, PER1, RCAN1 and USP47. Interacts with phosphorylated ubiquitination substrates CTNNB1, NFKBIA, IFNAR1, PER1 and PER2; the interaction requires the phosphorylation of the two serine residues in the substrates' destruction motif D-S-G-X(2,3,4)-S. Interacts with TRIM21. Interacts with PER3. Interacts with phosphorylated ubiquitination substrate CEP68 (By similarity). Interacts with INAVA (By similarity). {ECO:0000250|UniProtKB:Q9UKB1, ECO:0000269|PubMed:11896578, ECO:0000269|PubMed:15917222, ECO:0000269|PubMed:18782782}. DOMAIN: The N-terminal D domain mediates homodimerization. {ECO:0000250}. +Q8BG67 EFR3A_MOUSE Protein EFR3 homolog A (Protein EFR3-like) 819 92,613 Alternative sequence (1); Chain (1); Erroneous initiation (1); Modified residue (4); Sequence conflict (4) FUNCTION: Component of a complex required to localize phosphatidylinositol 4-kinase (PI4K) to the plasma membrane. The complex acts as a regulator of phosphatidylinositol 4-phosphate (PtdIns(4)P) synthesis. In the complex, EFR3A probably acts as the membrane-anchoring component. Also involved in responsiveness to G-protein-coupled receptors; it is however unclear whether this role is direct or indirect. {ECO:0000250|UniProtKB:Q14156}. PTM: Palmitoylated at its N-terminus, anchoring the protein to the plasma membrane. {ECO:0000250|UniProtKB:Q14156}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15363888}; Lipid-anchor {ECO:0000250|UniProtKB:Q14156}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q14156}. Note=Palmitoylation anchors the protein to the plasma membrane. A small amount is observed in the cytosol. {ECO:0000250|UniProtKB:Q14156}. SUBUNIT: Component of a phosphatidylinositol 4-kinase (PI4K) complex, composed of PI4KA, EFR3 (EFR3A or EFR3B), TTC7 (TTC7A or TTC7B) and FAM126 (FAM126A or FAM126B). {ECO:0000250|UniProtKB:Q14156}. TISSUE SPECIFICITY: Widely expressed (PubMed:25380825). Expressed in neurons of the superior olivary complex of the auditory brainstem. Also expressed at lower levels in the cochlear nucleus, the lateral leminiscal nuclei and the inferior collicus (PubMed:15363888). {ECO:0000269|PubMed:15363888, ECO:0000269|PubMed:25380825}. +Q64355 EFS_MOUSE Embryonal Fyn-associated substrate (SRC-interacting protein) (Signal-integrating protein) 560 58,973 Chain (1); Compositional bias (1); Domain (1); Modified residue (1); Motif (2); Mutagenesis (1); Region (1); Sequence conflict (6) FUNCTION: Docking protein which plays a central coordinating role for tyrosine-kinase-based signaling related to cell adhesion. May serve as an activator of SRC and a downstream effector. Interacts with the SH3 domain of FYN and with CRK, SRC, and YES. PTM: Phosphorylated on multiple tyrosine residues. Phosphorylated on tyrosines by FYN and SRC. {ECO:0000269|PubMed:8647432}. DOMAIN: Contains a central domain (substrate domain) containing multiple potential SH2-binding sites and a C-terminal domain containing a divergent helix-loop-helix (HLH) motif. The SH2-binding sites putatively bind CRK, NCK and ABL SH2 domains.; DOMAIN: The SH3-binding sites that bind to the SRC SH3 domain are required for interaction with CRK and are implicated in promotion of serum response element (SRE) activation. The SH3 domain interacts with PTK2/FAK1. TISSUE SPECIFICITY: Widely expressed. Higher levels found in placenta and embryo. Lower levels found in brain, brainstem, muscle and lung. No expression in liver and intestine. +Q9DBL2 GDAP2_MOUSE Ganglioside-induced differentiation-associated protein 2 498 56,269 Alternative sequence (1); Chain (1); Domain (2); Erroneous translation (1); Frameshift (1); Modified residue (1) TISSUE SPECIFICITY: Expressed at high levels in brain and testis, and at low levels in liver and kidney. {ECO:0000269|PubMed:10217254}. +Q8C0K5 GDC_MOUSE Graves disease carrier protein homolog (GDC) (Mitochondrial solute carrier protein homolog) (Solute carrier family 25 member 16) 332 36,220 Alternative sequence (2); Chain (1); Repeat (3); Transmembrane (6) TRANSMEM 37 57 Helical; Name=1. {ECO:0000255}.; TRANSMEM 88 108 Helical; Name=2. {ECO:0000255}.; TRANSMEM 134 154 Helical; Name=3. {ECO:0000255}.; TRANSMEM 191 211 Helical; Name=4. {ECO:0000255}.; TRANSMEM 244 264 Helical; Name=5. {ECO:0000255}.; TRANSMEM 299 319 Helical; Name=6. {ECO:0000255}. FUNCTION: Required for the accumulation of coenzyme A in the mitochondrial matrix. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +O70194 EIF3D_MOUSE Eukaryotic translation initiation factor 3 subunit D (eIF3d) (Eukaryotic translation initiation factor 3 subunit 7) (eIF-3-zeta) (eIF3 p66) 548 63,989 Chain (1); Compositional bias (1); Modified residue (4); Region (1); Sequence conflict (2) FUNCTION: mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, a complex required for several steps in the initiation of protein synthesis of a specialized repertoire of mRNAs. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression. In the eIF-3 complex, EIF3D specifically recognizes and binds the 7-methylguanosine cap of a subset of mRNAs. {ECO:0000255|HAMAP-Rule:MF_03003}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03003}. SUBUNIT: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B, EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and EIF3M. The eIF-3 complex appears to include 3 stable modules: module A is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D, EIF3E, EIF3K and EIF3L. EIF3C of module C binds EIF3B of module A and EIF3H of module B, thereby linking the three modules. EIF3J is a labile subunit that binds to the eIF-3 complex via EIF3B. The eIF-3 complex may interact with RPS6KB1 under conditions of nutrient depletion. Mitogenic stimulation may lead to binding and activation of a complex composed of MTOR and RPTOR, leading to phosphorylation and release of RPS6KB1 and binding of EIF4B to eIF-3. {ECO:0000255|HAMAP-Rule:MF_03003, ECO:0000269|PubMed:17581632}. DOMAIN: The RNA gate region regulates mRNA cap recognition to prevent promiscuous mRNA-binding before assembly of eif3d into the full eukaryotic translation initiation factor 3 (eIF-3) complex. {ECO:0000255|HAMAP-Rule:MF_03003}. +P23116 EIF3A_MOUSE Eukaryotic translation initiation factor 3 subunit A (eIF3a) (Centrosomin) (Eukaryotic translation initiation factor 3 subunit 10) (eIF-3-theta) (eIF3 p167) (eIF3 p180) (eIF3 p185) (p162) 1344 161,936 Chain (1); Coiled coil (1); Compositional bias (2); Domain (1); Frameshift (2); Modified residue (11); Region (2); Repeat (21); Sequence conflict (12) FUNCTION: RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression. {ECO:0000255|HAMAP-Rule:MF_03000, ECO:0000269|PubMed:17581632}. PTM: Phosphorylated. Phosphorylation is enhanced upon serum stimulation. {ECO:0000255|HAMAP-Rule:MF_03000}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03000}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:9372446}. Nucleus {ECO:0000269|PubMed:9372446}. Note=Centrosomin-A is found in the centrosome. Centrosomin-B is found in the nucleus. SUBUNIT: Interacts with KRT7 (By similarity). Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B, EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and EIF3M. The eIF-3 complex appears to include 3 stable modules: module A is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D, EIF3E, EIF3L and EIF3K. EIF3C of module C binds EIF3B of module A and EIF3H of module B, thereby linking the three modules. EIF3J is a labile subunit that binds to the eIF-3 complex via EIF3B. The eIF-3 complex may interact with RPS6KB1 under conditions of nutrient depletion. Mitogenic stimulation may lead to binding and activation of a complex composed of MTOR and RPTOR, leading to phosphorylation and release of RPS6KB1 and binding of EIF4B to eIF-3. Interacts with EIF4G1 and PIWIL2. {ECO:0000250, ECO:0000269|PubMed:16541103, ECO:0000269|PubMed:17581632, ECO:0000269|PubMed:19114715}. +Q8QZY1 EIF3L_MOUSE Eukaryotic translation initiation factor 3 subunit L (eIF3l) (66 kDa tyrosine-rich heat shock protein) (67 kDa polymerase-associated factor) (Eukaryotic translation initiation factor 3 subunit 6-interacting protein) (Eukaryotic translation initiation factor 3 subunit E-interacting protein) (HSP-66Y) (PAF67) 564 66,613 Chain (1); Domain (1); Initiator methionine (1); Modified residue (3); Sequence conflict (3) FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression. {ECO:0000255|HAMAP-Rule:MF_03011, ECO:0000269|PubMed:17581632}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03011}. SUBUNIT: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B, EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and EIF3M. The eIF-3 complex appears to include 3 stable modules: module A is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D, EIF3E, EIF3K and EIF3L. EIF3C of module C binds EIF3B of module A and EIF3H of module B, thereby linking the three modules. EIF3J is a labile subunit that binds to the eIF-3 complex via EIF3B. The eIF-3 complex may interact with RPS6KB1 under conditions of nutrient depletion. Mitogenic stimulation may lead to binding and activation of a complex composed of MTOR and RPTOR, leading to phosphorylation and release of RPS6KB1 and binding of EIF4B to eIF-3. Interacts with RRN3. {ECO:0000255|HAMAP-Rule:MF_03011, ECO:0000269|PubMed:12393749, ECO:0000269|PubMed:17581632}. +P70372 ELAV1_MOUSE ELAV-like protein 1 (Elav-like generic protein) (Hu-antigen R) (HuR) (MelG) 326 36,169 Chain (1); Cross-link (1); Domain (3); Initiator methionine (1); Modified residue (11); Sequence conflict (5) FUNCTION: RNA-binding protein that binds to the 3'-UTR region of mRNAs and increases their stability. Involved in embryonic stem cells (ESCs) differentiation: preferentially binds mRNAs that are not methylated by N6-methyladenosine (m6A), stabilizing them, promoting ESCs differentiation (PubMed:24394384). Binds to poly-U elements and AU-rich elements (AREs) in the 3'-UTR of target mRNAs. Binds avidly to the AU-rich element in FOS and IL3/interleukin-3 mRNAs. In the case of the FOS AU-rich element, binds to a core element of 27 nucleotides that contain AUUUA, AUUUUA, and AUUUUUA motifs. Binds preferentially to the 5'-UUUU[AG]UUU-3' motif in vitro (By similarity). With ZNF385A, binds the 3'-UTR of p53/TP53 mRNA to control their nuclear export induced by CDKN2A. Hence, may regulate p53/TP53 expression and mediate in part the CDKN2A anti-proliferative activity. May also bind with ZNF385A the CCNB1 mRNA (PubMed:21402775). Increases the stability of the leptin mRNA harboring an AU-rich element (ARE) in its 3' UTR (PubMed:27616329). {ECO:0000250|UniProtKB:Q15717, ECO:0000269|PubMed:21402775, ECO:0000269|PubMed:24394384, ECO:0000269|PubMed:27616329}. PTM: Phosphorylated by MAPKAPK2. Phosphorylated by PRKCD. {ECO:0000250|UniProtKB:Q15717}.; PTM: Methylated at Arg-217 by CARM1 in T-cells in response to LPS challenge. {ECO:0000269|PubMed:12237300}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9763509}. Nucleus {ECO:0000269|PubMed:9763509}. Cytoplasm, Stress granule {ECO:0000269|PubMed:27616329}. Note=Translocates into the cytoplasm following phosphorylation by MAPKAPK2. Likewise, phosphorylation by PRKCD promotes translocation from the nucleus into the cytoplasm, where it is associated with free and cytoskeleton-bound polysomes (By similarity). Localizes to the stress granules in the presence of PLEKHN1. {ECO:0000250|UniProtKB:Q15717, ECO:0000269|PubMed:27616329}. SUBUNIT: Monomer and homodimer (in vitro). Interacts with ANP32A (By similarity). Interacts with ZNF385A; the interaction is indirect and mRNA-dependent and may regulate p53/TP53 expression (PubMed:21402775). Identified in a mRNP complex, at least composed of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1. Interacts with AGO1 and AGO2. Interacts with IGF2BP2 and IGF2BP3. Interacts with HNRNPL (By similarity). Interacts with DHX36; this interaction occurs in a RNA-dependent manner. Interacts with ILF3; this interaction occurs in a RNA-dependent manner (By similarity). Interacts with PLEKHN1 (By similarity). {ECO:0000250|UniProtKB:Q15717, ECO:0000269|PubMed:21402775}. DOMAIN: The first RRM (RNA recognition motif) domain is essential for binding to AU-rich elements. {ECO:0000250|UniProtKB:Q15717}. +P60003 ELOF1_MOUSE Transcription elongation factor 1 homolog 83 9,462 Beta strand (3); Chain (1); Helix (1); Metal binding (4); Turn (2) FUNCTION: Transcription elongation factor implicated in the maintenance of proper chromatin structure in actively transcribed regions. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +Q60900 ELAV3_MOUSE ELAV-like protein 3 (Hu-antigen C) (HuC) 367 39,533 Alternative sequence (1); Beta strand (12); Chain (1); Domain (3); Helix (4); Turn (1) FUNCTION: Binds to AU-rich sequences (AREs) of target mRNAs, including VEGF mRNA. May also bind poly-A tracts via RRM 3. May be involved in neuronal differentiation and maintenance. {ECO:0000269|PubMed:10734193, ECO:0000269|PubMed:9016658}. DOMAIN: RRM 1 and RRM 2 bind cooperatively to AU-rich sequences in target mRNAs. RRM 3 binds to poly-A mRNA sequences. {ECO:0000269|PubMed:10734193, ECO:0000269|PubMed:9016658}. TISSUE SPECIFICITY: Brain specific. {ECO:0000269|PubMed:9016658}. +P54320 ELN_MOUSE Elastin (Tropoelastin) 860 71,938 Chain (1); Disulfide bond (1); Modified residue (45); Sequence conflict (1); Signal peptide (1) FUNCTION: Major structural protein of tissues such as aorta and nuchal ligament, which must expand rapidly and recover completely. Molecular determinant of the late arterial morphogenesis, stabilizing arterial structure by regulating proliferation and organization of vascular smooth muscle. {ECO:0000269|PubMed:9607766}. PTM: Elastin is formed through the cross-linking of its soluble precursor tropoelastin. Cross-linking is initiated through the action of lysyl oxidase on exposed lysines to form allysine. Subsequent spontaneous condensation reactions with other allysine or unmodified lysine residues result in various bi-, tri-, and tetrafunctional cross-links. The most abundant cross-links in mature elastin fibers are lysinonorleucine, allysine aldol, desmosine, and isodesmosine.; PTM: Hydroxylation on proline residues within the sequence motif, GXPG, is most likely to be 4-hydroxy as this fits the requirement for 4-hydroxylation in vertebrates. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P15502}. Note=Extracellular matrix of elastic fibers. {ECO:0000250|UniProtKB:P15502}. SUBUNIT: The polymeric elastin chains are cross-linked together into an extensible 3D network. Forms a ternary complex with BGN and MFAP2. Interacts with MFAP2 via divalent cations (calcium > magnesium > manganese) in a dose-dependent and saturating manner. Interacts with FBLN5 and FBN1. Forms a ternary complex with FBN1 and FBLN2 or FBLN5. Interacts with MFAP4 in a Ca (2+)-dependent manner; this interaction promotes ELN self-assembly. {ECO:0000250|UniProtKB:P04985, ECO:0000250|UniProtKB:P15502}. +Q9JLJ4 ELOV2_MOUSE Elongation of very long chain fatty acids protein 2 (EC 2.3.1.199) (3-keto acyl-CoA synthase Elovl2) (ELOVL fatty acid elongase 2) (ELOVL FA elongase 2) (Very long chain 3-ketoacyl-CoA synthase 2) (Very long chain 3-oxoacyl-CoA synthase 2) 292 34,207 Chain (1); Erroneous initiation (1); Motif (1); Transmembrane (7) TRANSMEM 29 49 Helical. {ECO:0000255|HAMAP-Rule:MF_03202}.; TRANSMEM 67 87 Helical. {ECO:0000255|HAMAP-Rule:MF_03202}.; TRANSMEM 115 135 Helical. {ECO:0000255|HAMAP-Rule:MF_03202}.; TRANSMEM 153 173 Helical. {ECO:0000255|HAMAP-Rule:MF_03202}.; TRANSMEM 175 195 Helical. {ECO:0000255|HAMAP-Rule:MF_03202}.; TRANSMEM 205 225 Helical. {ECO:0000255|HAMAP-Rule:MF_03202}.; TRANSMEM 230 250 Helical. {ECO:0000255|HAMAP-Rule:MF_03202}. Lipid metabolism; polyunsaturated fatty acid biosynthesis. FUNCTION: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Acts specifically toward polyunsaturated acyl-CoA with the higher activity toward C20:4(n-6) acyl-CoA. Condensing enzyme that catalyzes the synthesis of polyunsaturated very long chain fatty acid (C20- and C22-PUFA). May participate in the production of polyunsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. Essential for the formation of C24:5(n-6) up to C30:5(n-6) PUFAs in testis, these fatty acids being indispensable for normal spermatogenesis and fertility. {ECO:0000255|HAMAP-Rule:MF_03202, ECO:0000269|PubMed:12371743, ECO:0000269|PubMed:21106902}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03202}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03202}. DOMAIN: The C-terminal di-lysine motif may confer endoplasmic reticulum localization. {ECO:0000255|HAMAP-Rule:MF_03202}. TISSUE SPECIFICITY: Highly expressed in testis, lower level in liver. Weakly expressed in white adipose tissue, brain and kidney. {ECO:0000269|PubMed:10791983, ECO:0000269|PubMed:12371743}. +O35949 ELOV3_MOUSE Elongation of very long chain fatty acids protein 3 (EC 2.3.1.199) (3-keto acyl-CoA synthase Elovl3) (CIN-2) (Cold-inducible glycoprotein of 30 kDa) (ELOVL fatty acid elongase 3) (ELOVL FA elongase 3) (Very long chain 3-ketoacyl-CoA synthase 3) (Very long chain 3-oxoacyl-CoA synthase 3) 271 32,060 Chain (1); Glycosylation (1); Transmembrane (7) TRANSMEM 30 50 Helical. {ECO:0000255|HAMAP-Rule:MF_03203}.; TRANSMEM 67 87 Helical. {ECO:0000255|HAMAP-Rule:MF_03203}.; TRANSMEM 116 136 Helical. {ECO:0000255|HAMAP-Rule:MF_03203}.; TRANSMEM 141 161 Helical. {ECO:0000255|HAMAP-Rule:MF_03203}.; TRANSMEM 165 187 Helical. {ECO:0000255|HAMAP-Rule:MF_03203}.; TRANSMEM 199 219 Helical. {ECO:0000255|HAMAP-Rule:MF_03203}.; TRANSMEM 236 256 Helical. {ECO:0000255|HAMAP-Rule:MF_03203}. Lipid metabolism; polyunsaturated fatty acid biosynthesis. FUNCTION: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme with higher activity toward C18 acyl-CoAs, especially C18:0 acyl-CoAs. May participate in the production of saturated and monounsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. Participates in the formation of certain VLCFA and triglycerides in certain cells of the hair follicles and the sebaceous glands, required for skin barrier function. Critical enzyme for lipid accumulation and metabolic activity in brown adipocytes during the early phase of the tissue recruitment. Play a role in lipid storage and in resistance to diet-induced obesity. {ECO:0000255|HAMAP-Rule:MF_03203, ECO:0000269|PubMed:10791983, ECO:0000269|PubMed:14581464, ECO:0000269|PubMed:16326704, ECO:0000269|PubMed:20605947}. PTM: N-Glycosylated. {ECO:0000255|HAMAP-Rule:MF_03203, ECO:0000269|PubMed:10429212}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03203, ECO:0000269|PubMed:10429212}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03203}. TISSUE SPECIFICITY: Expressed in brown adipose tissue and liver. In the skin, strong expressed in the cells of the inner layer of the outer root sheath of the hair follicles and in the sebocytes of the sebaceous glands. Hardly detectable in the epidermis and not at all in fibroblasts. {ECO:0000269|PubMed:14581464, ECO:0000269|PubMed:9395518}. +P83940 ELOC_MOUSE Elongin-C (EloC) (Elongin 15 kDa subunit) (RNA polymerase II transcription factor SIII subunit C) (SIII p15) (Stromal membrane-associated protein SMAP1B homolog) (Transcription elongation factor B polypeptide 1) 112 12,473 Beta strand (5); Chain (1); Helix (6); Turn (1) FUNCTION: SIII, also known as elongin, is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. Subunit A is transcriptionally active and its transcription activity is strongly enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex) (By similarity). In embryonic stem cells, the elongin BC complex is recruited by EPOP to Polycomb group (PcG) target genes in order generate genomic region that display both active and repressive chromatin properties, an important feature of pluripotent stem cells (PubMed:27863225, PubMed:27863226). {ECO:0000250|UniProtKB:Q15369, ECO:0000269|PubMed:27863225, ECO:0000269|PubMed:27863226}.; FUNCTION: The elongin BC complex seems to be involved as an adapter protein in the proteasomal degradation of target proteins via different E3 ubiquitin ligase complexes, including the von Hippel-Lindau ubiquitination complex CBC(VHL). By binding to BC-box motifs it seems to link target recruitment subunits, like VHL and members of the SOCS box family, to Cullin/RBX1 modules that activate E2 ubiquitination enzymes. {ECO:0000250|UniProtKB:Q15369}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Heterotrimer of an A (ELOA, ELOA2 or ELOA3), ELOB and ELOC subunit. The elongin BC complex interacts with EPOP; leading to recruit the elongin BC complex to Polycomb group (PcG) target genes, thereby restricting excessive activity of the PRC2/EED-EZH2 complex (PubMed:27863225, PubMed:27863226). Part of E3 ubiquitin ligase complexes with CUL5 or CUL2, RBX1 and a substrate adapter protein that can be either SOCS1, SOCS5, ELOA, VHL or WSB1. The elongin BC complex is part of a complex with hydroxylated HIF1A. Interacts with VHL. Interacts with TMF1. Interacts with SPSB1. posed of LIMD1, VHL, EGLN1/PHD2, ELOB and CUL2. Interacts with SPSB1. Interacts with KLHDC10; which may be an E3 ubiquitin ligase complex substrate recognition component. Interacts with NOS2 in the presence of SPSB1 or SPSB2 or SPSB4 (By similarity). {ECO:0000250|UniProtKB:Q15369, ECO:0000269|PubMed:10051596, ECO:0000269|PubMed:11384984, ECO:0000269|PubMed:16498413, ECO:0000269|PubMed:27863225, ECO:0000269|PubMed:27863226, ECO:0000269|PubMed:9869640}. +Q99L85 ELP5_MOUSE Elongator complex protein 5 (Dermal papilla-derived protein 6 homolog) (Retinoic acid-induced protein 12) 300 33,498 Chain (1); Modified residue (1); Sequence conflict (3) FUNCTION: Acts as subunit of the RNA polymerase II elongator complex, which is a histone acetyltransferase component of the RNA polymerase II (Pol II) holoenzyme and is involved in transcriptional elongation. Elongator may play a role in chromatin remodeling and is involved in acetylation of histones H3 and probably H4. May be involved in TP53-mediated transcriptional regulation. Involved in cell migration. {ECO:0000269|PubMed:22854966}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. SUBUNIT: Component of the RNA polymerase II elongator complex (Elongator), which consists of ELP1, STIP1/ELP2, ELP3, ELP4, ELP5 and ELP6; in the complex, is required for optimal binding of ELP3 to ELP4. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed with highest levels in testis. {ECO:0000269|PubMed:9371513}. +Q7TNG5 EMAL2_MOUSE Echinoderm microtubule-associated protein-like 2 (EMAP-2) 649 70,734 Alternative sequence (1); Chain (1); Frameshift (1); Region (1); Repeat (12); Sequence conflict (1) FUNCTION: Tubulin binding protein that inhibits microtubule nucleation and growth, resulting in shorter microtubules. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Colocalizes with the microtubule cytoskeleton. Colocalizes with the mitotic spindle (By similarity). {ECO:0000250}. SUBUNIT: Binds unpolymerized tubulins via its WD repeat region. Interacts with GRID2 and may also interact with GRID1 (By similarity). {ECO:0000250}. DOMAIN: Contains a tandem atypical propeller in EMLs (TAPE) domain. The N-terminal beta-propeller is formed by canonical WD repeats; in contrast, the second beta-propeller contains one blade that is formed by discontinuous parts of the polypeptide chain (By similarity). {ECO:0000250}. +Q3TAS6 EMC10_MOUSE ER membrane protein complex subunit 10 (Hematopoietic signal peptide-containing membrane domain-containing protein 1) 258 27,053 Alternative sequence (1); Chain (1); Erroneous initiation (2); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 222 242 Helical. {ECO:0000255}. TOPO_DOM 28 221 Extracellular. {ECO:0000255}.; TOPO_DOM 243 258 Cytoplasmic. {ECO:0000255}. FUNCTION: Promotes angiogenesis and tissue repair in the heart after myocardial infarction. Stimulates cardiac endothelial cell migration and outgrowth via the activation of p38 MAPK, PAK and MAPK2 signaling pathways. {ECO:0000269|PubMed:28931551}. SUBCELLULAR LOCATION: Isoform 1: Membrane {ECO:0000250|UniProtKB:Q5UCC4}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: Isoform 2: Secreted {ECO:0000269|PubMed:28931551}. SUBUNIT: Component of the ER membrane protein complex (EMC). {ECO:0000250}. TISSUE SPECIFICITY: Up-regulated in the left ventricle 3 days after myocardial infarction (MI). Expressed predominantly by monocytes and macrophages from bone marrow, spleen, and peripheral blood 3 days after MI (protein level). {ECO:0000269|PubMed:28931551}. +Q8C7X2 EMC1_MOUSE ER membrane protein complex subunit 1 997 111,605 Alternative sequence (2); Chain (1); Glycosylation (1); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 963 983 Helical. {ECO:0000255}. TOPO_DOM 23 962 Extracellular. {ECO:0000255}.; TOPO_DOM 984 997 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Component of the ER membrane protein complex (EMC). {ECO:0000250}. +Q99K41 EMIL1_MOUSE EMILIN-1 (Elastin microfibril interface-located protein 1) (Elastin microfibril interfacer 1) 1017 107,585 Chain (1); Coiled coil (6); Compositional bias (1); Disulfide bond (3); Domain (3); Glycosylation (7); Signal peptide (1) FUNCTION: May be responsible for anchoring smooth muscle cells to elastic fibers, and may be involved not only in the formation of the elastic fiber, but also in the processes that regulate vessel assembly. Has cell adhesive capacity (By similarity). May have a function in placenta formation and initial organogenesis and a later role in interstitial connective tissue. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q9Y6C2}. Note=Found mainly at the interface between amorphous elastin and microfibrils. {ECO:0000250|UniProtKB:Q9Y6C2}. SUBUNIT: Homotrimer associated through a moderately stable interaction of the C-terminal globular C1q domains, allowing the nucleation of the triple helix and then a further quaternary assembly to higher-order polymers via intermolecular disulfide bonds. Interacts with EMILIN2 (By similarity). {ECO:0000250}. +Q7TSV9 ENKD1_MOUSE Enkurin domain-containing protein 1 346 38,967 Chain (1); Domain (1); Modified residue (2) +Q6SP97 ENKUR_MOUSE Enkurin 255 29,527 Chain (1); Domain (2); Motif (1) FUNCTION: Adapter that functions to localize a calcium-sensitive signal transduction machinery in sperm to a calcium-permeable ion channel. {ECO:0000269|PubMed:15385169}. SUBCELLULAR LOCATION: Cell projection, cilium, flagellum {ECO:0000269|PubMed:15385169}. Note=Sperm acrosomal crescent and flagellar principal piece. SUBUNIT: Binds calmodulin via its IQ domain. Interacts with TRPC1, TRPC2, TRPC5, but not TRPC3. {ECO:0000269|PubMed:15385169}. DOMAIN: Residues 160-255 contains the TRPC2 binding site.; DOMAIN: The IQ motif is involved in calmodulin binding. TISSUE SPECIFICITY: High expression in testis and vomeronasal organ and lower expression in ovary, heart, lung, and brain. Not expressed in other tissues. {ECO:0000269|PubMed:15385169}. +B2RSH2 GNAI1_MOUSE Guanine nucleotide-binding protein G(i) subunit alpha-1 (Adenylate cyclase-inhibiting G alpha protein) 354 40,361 Binding site (1); Chain (1); Initiator methionine (1); Lipidation (2); Metal binding (2); Nucleotide binding (5) FUNCTION: Guanine nucleotide-binding proteins (G proteins) function as transducers downstream of G protein-coupled receptors (GPCRs) in numerous signaling cascades. The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state. Signaling by an activated GPCR promotes GDP release and GTP binding. The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal. Both GDP release and GTP hydrolysis are modulated by numerous regulatory proteins (By similarity). Signaling is mediated via effector proteins, such as adenylate cyclase. Inhibits adenylate cyclase activity, leading to decreased intracellular cAMP levels (By similarity). The inactive GDP-bound form prevents the association of RGS14 with centrosomes and is required for the translocation of RGS14 from the cytoplasm to the plasma membrane. Required for normal cytokinesis during mitosis. Required for cortical dynein-dynactin complex recruitment during metaphase (By similarity). {ECO:0000250|UniProtKB:P10824, ECO:0000250|UniProtKB:P63096}. PTM: Myristoylation at Gly-2 is required for membrane anchoring before palmitoylation. {ECO:0000250|UniProtKB:P10824}.; PTM: Palmitoylation at Cys-3 varies with membrane lipid composition. {ECO:0000250|UniProtKB:P10824}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P10824}. Cytoplasm {ECO:0000250|UniProtKB:P10824}. Cell membrane {ECO:0000250|UniProtKB:P10824}; Peripheral membrane protein {ECO:0000250|UniProtKB:P10824}; Cytoplasmic side {ECO:0000250|UniProtKB:P10824}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P10824}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:P63096}. Membrane {ECO:0000250|UniProtKB:P10824}; Lipid-anchor {ECO:0000250|UniProtKB:P10824}. Note=Localizes in the centrosomes of interphase and mitotic cells, but not in centrosomes during cytokinesis. Detected at the cleavage furrow or the midbody. Localized at the plasma membrane throughout mitosis. Colocalizes with RIC8A and RGS14 at the plasma membrane. {ECO:0000250|UniProtKB:P10824}. SUBUNIT: Heterotrimeric G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site. Part of a spindle orientation complex at least composed of GNAI1, GPSM2 and NUMA1. Identified in complex with the beta subunit GNB1 and the gamma subunit GNG1. Identified in complex with the beta subunit GNB1 and the gamma subunit GNG2. GTP binding causes dissociation of the heterotrimer, liberating the individual subunits so that they can interact with downstream effector proteins (By similarity). Interacts (GDP-bound form) with GPSM1; this inhibits guanine nucleotide exchange and GTP binding (By similarity). Interacts (GDP-bound form) with GPSM2 (via GoLoco domains); this inhibits guanine nucleotide exchange. Interacts with RGS10; this strongly enhances GTP hydrolysis. Interacts with RGS1 and RGS16; this strongly enhances GTPase activity. Interacts with RGS4. Interacts with RGS12. Interacts (via active GTP- or inactive GDP-bound forms) with RGS14 (via RGS and GoLoco domains). Interacts with RGS3, RGS6, RGS7, RGS8, RGS17, RGS18 and RGS20 (in vitro) (By similarity). Interacts (GDP-bound form) with RIC8A (via C-terminus) (By similarity). {ECO:0000250|UniProtKB:P10824, ECO:0000250|UniProtKB:P63096}. +Q8R0Z2 ENOX2_MOUSE Ecto-NOX disulfide-thiol exchanger 2 (APK1 antigen) (Cytosolic ovarian carcinoma antigen 1) (Tumor-associated hydroquinone oxidase) (tNOX) [Includes: Hydroquinone [NADH] oxidase (EC 1.-.-.-); Protein disulfide-thiol oxidoreductase (EC 1.-.-.-)] 598 68,285 Alternative sequence (2); Chain (1); Coiled coil (2); Compositional bias (1); Domain (1) FUNCTION: May be involved in cell growth. Probably acts as a terminal oxidase of plasma electron transport from cytosolic NAD(P)H via hydroquinones to acceptors at the cell surface. Hydroquinone oxidase activity alternates with a protein disulfide-thiol interchange/oxidoreductase activity which may control physical membrane displacements associated with vesicle budding or cell enlargement. The activities oscillate with a period length of 22 minutes and play a role in control of the ultradian cellular biological clock (By similarity). {ECO:0000250|UniProtKB:Q16206}. PTM: Glycosylated. {ECO:0000250|UniProtKB:Q16206}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Secreted, extracellular space {ECO:0000250}. Note=Extracellular and plasma membrane-associated. {ECO:0000250}. +P18872 GNAO_MOUSE Guanine nucleotide-binding protein G(o) subunit alpha 354 40,085 Alternative sequence (1); Beta strand (6); Binding site (1); Chain (1); Helix (16); Initiator methionine (1); Lipidation (2); Metal binding (2); Nucleotide binding (4); Turn (5) FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Stimulated by RGS14. The G(o) protein function is not clear. {ECO:0000269|PubMed:10926822}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15585744}. Membrane {ECO:0000250|UniProtKB:P09471}; Lipid-anchor {ECO:0000250|UniProtKB:P09471}. SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site. Interacts with RGS14. {ECO:0000269|PubMed:10926822}. +Q03385 GNDS_MOUSE Ral guanine nucleotide dissociation stimulator (RalGDS) (Ral guanine nucleotide exchange factor) (RalGEF) 852 94,202 Chain (1); Domain (3); Sequence conflict (2) FUNCTION: Stimulates the dissociation of GDP from the Ras-related RalA and RalB GTPases which allows GTP binding and activation of the GTPases. Interacts and acts as an effector molecule for R-Ras, H-Ras, K-Ras, and Rap. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16580637}. Nucleus {ECO:0000269|PubMed:16580637}. Note=Localizes mainly in the peripheral region of the cytoplasmic membrane in oocytes and in preimplantation embryos until the 8-cell stage. Between the late 1-cell and the early 2-cell stages, nuclear localization becomes stronger. After the 4-cell stage, not detected in the nucleus. {ECO:0000269|PubMed:16580637}. SUBUNIT: Interacts with RIT1 and RIT2. Interacts (via Ras-associating domain) with Oog1 (PubMed:16580637). {ECO:0000250, ECO:0000269|PubMed:16580637}. DOMAIN: The Ras-associating domain interacts with Ras. {ECO:0000250}. +P36916 GNL1_MOUSE Guanine nucleotide-binding protein-like 1 (GTP-binding protein MMR1) 607 68,771 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (1); Modified residue (11); Nucleotide binding (3); Sequence conflict (4) FUNCTION: Possible regulatory or functional link with the histocompatibility cluster. {ECO:0000250}. DOMAIN: In contrast to other GTP-binding proteins, this family is characterized by a circular permutation of the GTPase motifs described by a G4-G1-G3 pattern. +Q9D428 GOG7B_MOUSE Golgin subfamily A member 7B 167 18,335 Chain (1); Compositional bias (2); Erroneous initiation (1); Lipidation (2) FUNCTION: May be involved in protein transport from Golgi to cell surface. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. +Q9CW79 GOGA1_MOUSE Golgin subfamily A member 1 (Golgin-97) 758 87,338 Alternative sequence (1); Chain (1); Coiled coil (1); Domain (1); Modified residue (6) FUNCTION: Involved in vesicular trafficking at the Golgi apparatus level. Involved in endosome-to-Golgi trafficking. {ECO:0000250|UniProtKB:Q92805}. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:11412037}; Peripheral membrane protein {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:11412037}. SUBUNIT: Interacts with RAB6A (By similarity). Directly interacts with TBC1D23 (PubMed:29084197). Interacts with FAM91A1; this interaction may mediated by TBC1D23 (Probable). {ECO:0000250|UniProtKB:Q92805, ECO:0000269|PubMed:29084197, ECO:0000305}. DOMAIN: Extended rod-like protein with coiled-coil domains. +Q8BTJ4 ENPP4_MOUSE Bis(5'-adenosyl)-triphosphatase enpp4 (EC 3.6.1.29) (AP3A hydrolase) (AP3Aase) (Ectonucleotide pyrophosphatase/phosphodiesterase family member 4) (E-NPP 4) (NPP-4) 456 51,611 Active site (1); Alternative sequence (1); Binding site (3); Chain (1); Disulfide bond (2); Erroneous initiation (1); Glycosylation (5); Metal binding (7); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 411 431 Helical. {ECO:0000255}. TOPO_DOM 19 410 Extracellular. {ECO:0000255}.; TOPO_DOM 432 456 Cytoplasmic. {ECO:0000255}. FUNCTION: Hydrolyzes extracellular Ap3A into AMP and ADP, and Ap4A into AMP and ATP. Ap3A and Ap4A are diadenosine polyphosphates thought to induce proliferation of vascular smooth muscle cells. Acts as a procoagulant, mediating platelet aggregation at the site of nascent thrombus via release of ADP from Ap3A and activation of ADP receptors (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein. +Q91VW5 GOGA4_MOUSE Golgin subfamily A member 4 (tGolgin-1) 2238 257,564 Chain (1); Coiled coil (1); Compositional bias (2); Domain (1); Erroneous initiation (1); Modified residue (5); Natural variant (8); Region (1) FUNCTION: Involved in vesicular trafficking at the Golgi apparatus level. May play a role in delivery of transport vesicles containing GPI-linked proteins from the trans-Golgi network through its interaction with MACF1. Involved in endosome-to-Golgi trafficking. {ECO:0000250|UniProtKB:Q13439}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12162805}. Golgi apparatus membrane {ECO:0000269|PubMed:12162805}; Peripheral membrane protein {ECO:0000269|PubMed:12162805}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q13439}. SUBUNIT: Homodimer. Interacts with GTP-bound ARL1 and ARL3 (By similarity). Interacts with MACF1 (By similarity). Directly interacts with TBC1D23 (PubMed:29084197). Interacts with FAM91A1; this interaction may mediated by TBC1D23 (By similarity). {ECO:0000250|UniProtKB:Q13439, ECO:0000269|PubMed:29084197}. DOMAIN: Extended rod-like protein with coiled-coil domains. TISSUE SPECIFICITY: Ubiquitous. Highly expressed in oligodendrocyte precursors, particularly at a stage just prior to myelination. {ECO:0000269|PubMed:12162805}. +P10404 ENV1_MOUSE MLV-related proviral Env polyprotein [Cleaved into: Surface protein (SU); Transmembrane protein (TM)] 641 69,613 Chain (2); Coiled coil (2); Compositional bias (1); Disulfide bond (8); Glycosylation (5); Helix (4); Lipidation (1); Motif (3); Natural variant (19); Region (2); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 582 602 Helical. {ECO:0000255}. TOPO_DOM 33 581 Extracellular. {ECO:0000255}.; TOPO_DOM 603 641 Cytoplasmic. {ECO:0000255}. FUNCTION: The surface protein (SU) attaches the virus to the host cell by binding to its receptor. This interaction triggers the refolding of the transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane (By similarity). {ECO:0000250}.; FUNCTION: The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity). {ECO:0000250}. PTM: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as a inactive precursor that is N-glycosylated and processed likely by host cell furin or by a furin-like protease in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires the minimal sequence [KR]-X-[KR]-R. The R-peptide is released from the C-terminus of the cytoplasmic tail of the TM protein upon particle formation as a result of proteolytic cleavage by the viral protease. Cleavage of this peptide is required for TM to become fusogenic (By similarity). {ECO:0000250}.; PTM: The CXXC motif is highly conserved across a broad range of retroviral envelope proteins. It is thought to participate in the formation of a labile disulfide bond possibly with the CX6CC motif present in the transmembrane protein. Isomerization of the intersubunit disulfide bond to an SU intrachain disulfide bond is thought to occur upon receptor recognition in order to allow membrane fusion (By similarity). {ECO:0000250}.; PTM: The transmembrane protein is palmitoylated. {ECO:0000250}.; PTM: The R-peptide is palmitoylated. {ECO:0000250}. SUBCELLULAR LOCATION: Transmembrane protein: Virion membrane; Single-pass type I membrane protein. Cell membrane; Single-pass type I membrane protein. Note=The surface protein is not anchored to the viral envelope, but associates with the extravirion surface through its binding to TM. Both proteins are thought to be concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag. R-peptide: Cell membrane; peripheral membrane protein. The R-peptide is membrane-associated through its palmitate (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: Surface protein: Virion membrane; Peripheral membrane protein. Cell membrane; Peripheral membrane protein. Note=The surface protein is not anchored to the viral envelope, but associates with the extravirion surface through its binding to TM. Both proteins are thought to be concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag. R-peptide: Cell membrane; peripheral membrane protein. The R-peptide is membrane-associated through its palmitate (By similarity). {ECO:0000250}. SUBUNIT: The mature envelope protein (Env) consists of a trimer of SU-TM heterodimers attached by a labile interchain disulfide bond. {ECO:0000250}. DOMAIN: The YXXL motif is involved in determining the exact site of viral release at the surface of infected mononuclear cells and promotes endocytosis.; DOMAIN: The 17 amino acids long immunosuppressive region is present in many retroviral envelope proteins. Synthetic peptides derived from this relatively conserved sequence inhibit immune function in vitro and in vivo (By similarity). {ECO:0000250}. +Q3TCT4 ENTP7_MOUSE Ectonucleoside triphosphate diphosphohydrolase 7 (NTPDase 7) (EC 3.6.1.-) (Lysosomal apyrase-like protein 1) 606 68,974 Active site (1); Alternative sequence (2); Chain (1); Disulfide bond (1); Glycosylation (1); Sequence conflict (2); Topological domain (3); Transmembrane (2) TRANSMEM 29 49 Helical. {ECO:0000255}.; TRANSMEM 549 569 Helical. {ECO:0000255}. TOPO_DOM 1 28 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 50 548 Vesicular. {ECO:0000255}.; TOPO_DOM 570 606 Cytoplasmic. {ECO:0000255}. FUNCTION: Preferentially hydrolyzes nucleoside 5'-triphosphates. The order of activity with respect to possible substrates is UTP > GTP > CTP (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=Localizes to intracellular vesicular compartments. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. Expressed at high level in brain, kidney, liver and testis. Weakly expressed in lung, thymus and heart. {ECO:0000269|PubMed:11278936}. +Q99KN9 EPN4_MOUSE Clathrin interactor 1 (Enthoprotin) (Epsin-4) (Epsin-related protein) (EpsinR) 631 68,513 Alternative sequence (3); Binding site (2); Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (1); Modified residue (10); Region (3) FUNCTION: Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). May have a role in transport via clathrin-coated vesicles from the trans-Golgi network to endosomes. Stimulates clathrin assembly (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Membrane {ECO:0000255|PROSITE-ProRule:PRU00243}; Peripheral membrane protein {ECO:0000250}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250}. Note=Found throughout the cell, with the exception of the cell surface. Concentrated in the perinuclear region and associated with clathrin-coated vesicles close to the trans-Golgi network (By similarity). {ECO:0000250}. SUBUNIT: Binds clathrin heavy chain, GGA2, AP-2 and AP1G1. Interacts with VTI1B. {ECO:0000250|UniProtKB:Q14677}. +Q80WT4 GP176_MOUSE G-protein coupled receptor 176 (G-protein coupled receptor AGR9) 515 57,143 Chain (1); Glycosylation (4); Mutagenesis (2); Topological domain (8); Transmembrane (7) TRANSMEM 42 64 Helical; Name=1. {ECO:0000255}.; TRANSMEM 78 98 Helical; Name=2. {ECO:0000255}.; TRANSMEM 109 129 Helical; Name=3. {ECO:0000255}.; TRANSMEM 158 177 Helical; Name=4. {ECO:0000255}.; TRANSMEM 205 225 Helical; Name=5. {ECO:0000255}.; TRANSMEM 265 285 Helical; Name=6. {ECO:0000255}.; TRANSMEM 302 322 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 41 Extracellular. {ECO:0000255}.; TOPO_DOM 65 77 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 99 108 Extracellular. {ECO:0000305}.; TOPO_DOM 130 157 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 178 204 Extracellular. {ECO:0000305}.; TOPO_DOM 226 264 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 286 301 Extracellular. {ECO:0000305}.; TOPO_DOM 323 515 Cytoplasmic. {ECO:0000305}. FUNCTION: Orphan receptor involved in normal circadian rhythm behavior (PubMed:26882873). Acts through the G-protein subclass G(z)-alpha and has an agonist-independent basal activity to repress cAMP production (PubMed:26882873). {ECO:0000269|PubMed:26882873}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26882873}; Multi-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Expressed mainly in the brain, with prominent expression in the SCN (at protein level) (PubMed:26882873). {ECO:0000269|PubMed:26882873}. +Q8VEH5 EPMIP_MOUSE EPM2A-interacting protein 1 (Laforin-interacting protein) 606 70,096 Chain (1); Modified residue (1) SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250}. SUBUNIT: Interacts with EPM2A. {ECO:0000250}. +Q6PH08 ERC2_MOUSE ERC protein 2 (CAZ-associated structural protein 1) (CAST1) 957 110,639 Alternative sequence (7); Chain (1); Coiled coil (1); Compositional bias (4); Erroneous initiation (1); Modified residue (2) FUNCTION: Thought to be involved in the organization of the cytomatrix at the nerve terminals active zone (CAZ) which regulates neurotransmitter release. Seems to act together with BSN. May recruit liprin-alpha proteins to the CAZ. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12163476}. Cell junction, synapse {ECO:0000269|PubMed:12163476}. Cell junction, synapse, synaptosome {ECO:0000269|PubMed:12163476}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12163476}. Note=Localized to the active zone of presynaptic density. SUBUNIT: Interacts with BSN, ERC1, PPFIA1, PPFIA2, PPFIA3 and PPFIA4. Interacts through its C-terminus with the PDZ domain of RIMS1. Part of a complex consisting of ERC2, RIMS1 and UNC13A. TISSUE SPECIFICITY: Expressed throughout the central nervous system, including hippocampus, cortex, cerebellum and olfactory bulb. {ECO:0000269|PubMed:12163476}. +Q8BLN5 ERG7_MOUSE Lanosterol synthase (EC 5.4.99.7) (2,3-epoxysqualene--lanosterol cyclase) (Oxidosqualene--lanosterol cyclase) (OSC) 733 83,141 Active site (1); Chain (1); Initiator methionine (1); Modified residue (1); Repeat (4); Sequence conflict (2) Terpene metabolism; lanosterol biosynthesis; lanosterol from farnesyl diphosphate: step 3/3. FUNCTION: Catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol nucleus. Through the production of lanosterol may regulate lens protein aggregation and increase transparency. {ECO:0000250|UniProtKB:P48449, ECO:0000250|UniProtKB:P48450}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. +Q9ERY9 ERG28_MOUSE Probable ergosterol biosynthetic protein 28 140 15,806 Chain (1); Transmembrane (4) TRANSMEM 4 24 Helical. {ECO:0000255}.; TRANSMEM 52 72 Helical. {ECO:0000255}.; TRANSMEM 79 99 Helical. {ECO:0000255}.; TRANSMEM 105 125 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q61586 GPAT1_MOUSE Glycerol-3-phosphate acyltransferase 1, mitochondrial (GPAT-1) (EC 2.3.1.15) (P90) 827 93,705 Chain (1); Modified residue (5); Motif (1); Sequence conflict (2); Topological domain (3); Transit peptide (1); Transmembrane (2) TRANSMEM 472 494 Helical. {ECO:0000255}.; TRANSMEM 575 593 Helical. {ECO:0000255}. TOPO_DOM ? 471 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 495 574 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 594 827 Mitochondrial intermembrane. {ECO:0000255}. Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 1/3. FUNCTION: Esterifies acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipid biosynthesis. {ECO:0000250|UniProtKB:P97564, ECO:0000250|UniProtKB:Q9HCL2}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:P97564}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P97564}. DOMAIN: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate. {ECO:0000250}. TISSUE SPECIFICITY: Highest levels in liver, intermediate levels in muscle and kidney, and lowest levels in lung and brain. +Q9DC16 ERGI1_MOUSE Endoplasmic reticulum-Golgi intermediate compartment protein 1 (ER-Golgi intermediate compartment 32 kDa protein) (ERGIC-32) 290 32,562 Chain (1); Glycosylation (1); Topological domain (3); Transmembrane (2) TRANSMEM 27 47 Helical. {ECO:0000255}.; TRANSMEM 255 275 Helical. {ECO:0000255}. TOPO_DOM 1 26 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 48 254 Lumenal. {ECO:0000255}.; TOPO_DOM 276 290 Cytoplasmic. {ECO:0000255}. FUNCTION: Possible role in transport between endoplasmic reticulum and Golgi. {ECO:0000250}. PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Cycles between the endoplasmic reticulum and the Golgi. {ECO:0000250}. SUBUNIT: Interacts with ERGIC3/ERV46. {ECO:0000250}. +Q7TMF2 ERI1_MOUSE 3'-5' exoribonuclease 1 (EC 3.1.-.-) (3'-5' exonuclease ERI1) (Eri-1 homolog) (Histone mRNA 3'-exonuclease 1) 345 39,493 Active site (2); Binding site (3); Chain (1); Domain (2); Metal binding (5); Modified residue (2); Mutagenesis (4); Sequence conflict (9) FUNCTION: RNA exonuclease that binds to the 3'-end of histone mRNAs and degrades them, suggesting that it plays an essential role in histone mRNA decay after replication. A 2' and 3'-hydroxyl groups at the last nucleotide of the histone 3'-end is required for efficient degradation of RNA substrates. Also able to degrade the 3'-overhangs of short interfering RNAs (siRNAs) in vitro, suggesting a possible role as regulator of RNA interference (RNAi). Binds with high affinity to the 3' side of the stem-loop structure and to the downstream cleavage product (DCP) of histone pre-mRNAs. Requires for binding the 5'-ACCCA-3' sequence present in stem-loop structure. Able to bind other mRNAs (By similarity). Required for 5.8S rRNA 3'-end processing. Also binds to 5.8s ribosomal RNA. {ECO:0000250, ECO:0000269|PubMed:18438418}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18438418}. Nucleus {ECO:0000269|PubMed:18438418}. Nucleus, nucleolus {ECO:0000269|PubMed:18438418}. SUBUNIT: Identified in a histone pre-mRNA complex, at least composed of ERI1, LSM11, SLBP, SNRPB, SYNCRIP and YBX1. Binds to 40S and 60S ribosomal subunits and to 80S assembled ribosomes. Interacts in a cooperative manner with SLBP to the mature 3'-end of histone mRNAs. Found in a ternary complex with SLBP and the stem-loop structure of the 3'-end of histone mRNAs (By similarity). {ECO:0000250}. DOMAIN: The SAP domain is necessary for binding to the stem-loop structure of histone mRNAs and to form the ternary complex with SLBP, but not for 3'-end histone mRNA exonuclease activity. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed with high levels in spleen, thymus and testis (at protein level). {ECO:0000269|PubMed:18438418}. +Q14DK4 GPAT2_MOUSE Glycerol-3-phosphate acyltransferase 2, mitochondrial (GPAT-2) (EC 2.3.1.15) (xGPAT1) 801 89,150 Alternative sequence (2); Chain (1); Erroneous initiation (2); Modified residue (4); Motif (1); Mutagenesis (2); Region (1); Sequence conflict (6); Topological domain (3); Transmembrane (2) TRANSMEM 306 332 Helical. {ECO:0000255}.; TRANSMEM 450 472 Helical. {ECO:0000255}. TOPO_DOM 1 305 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 333 449 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 473 801 Cytoplasmic. {ECO:0000255}. Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 1/3. FUNCTION: Esterifies acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipid biosynthesis (PubMed:17013544, PubMed:17689486). Required for primary processing step during piRNA biosynthesis (PubMed:23611983). Molecular mechanisms by which it promotes piRNA biosynthesis are unclear and do not involve its acyltransferase activity (PubMed:23611983). {ECO:0000269|PubMed:17013544, ECO:0000269|PubMed:17689486, ECO:0000269|PubMed:23611983}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:17013544, ECO:0000269|PubMed:17689486, ECO:0000269|PubMed:22285183}; Multi-pass membrane protein {ECO:0000269|PubMed:17013544, ECO:0000269|PubMed:17689486, ECO:0000269|PubMed:22285183}. SUBUNIT: Interacts with PIWIL2 (PubMed:23611983). {ECO:0000269|PubMed:23611983}. DOMAIN: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in the testis (PubMed:26268560). Expressed at lower levels in the heart, liver, kidney, spleen and adipose cells (PubMed:17013544, PubMed:17689486). {ECO:0000269|PubMed:17013544, ECO:0000269|PubMed:17689486, ECO:0000269|PubMed:26268560}. +Q9CQE7 ERGI3_MOUSE Endoplasmic reticulum-Golgi intermediate compartment protein 3 (Serologically defined breast cancer antigen NY-BR-84 homolog) 383 43,208 Alternative sequence (2); Chain (1); Glycosylation (1); Modified residue (2); Topological domain (3); Transmembrane (2) TRANSMEM 26 46 Helical. {ECO:0000255}.; TRANSMEM 342 362 Helical. {ECO:0000255}. TOPO_DOM 1 25 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 47 341 Lumenal. {ECO:0000255}.; TOPO_DOM 363 383 Cytoplasmic. {ECO:0000255}. FUNCTION: Possible role in transport between endoplasmic reticulum and Golgi. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000269|PubMed:12663859}; Multi-pass membrane protein {ECO:0000269|PubMed:12663859}. Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:12663859}; Multi-pass membrane protein {ECO:0000269|PubMed:12663859}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:12663859}; Multi-pass membrane protein {ECO:0000269|PubMed:12663859}. Note=Cycles between the endoplasmic reticulum and the Golgi. SUBUNIT: Interacts with ERGIC1/ERGIC32. {ECO:0000250}. TISSUE SPECIFICITY: Expression is particularly strong in liver, kidney and brain but is almost undetectable in heart. {ECO:0000269|PubMed:12663859}. +Q5BKS4 ERI2_MOUSE ERI1 exoribonuclease 2 (EC 3.1.-.-) (Exonuclease domain-containing protein 1) 688 76,524 Active site (2); Binding site (2); Chain (1); Compositional bias (1); Domain (1); Metal binding (5); Sequence conflict (1) +Q6PGN1 ERFE_MOUSE Erythroferrone (Complement C1q tumor necrosis factor-related protein 15) (Myonectin) 340 36,265 Chain (1); Domain (1); Frameshift (1); Glycosylation (4); Sequence conflict (1); Signal peptide (1) FUNCTION: Iron-regulatory hormone that acts as an erythroid regulator after hemorrhage: produced by erythroblasts following blood loss and mediates suppression of hepcidin (HAMP) expression in the liver, thereby promoting increased iron absorption and mobilization from stores (PubMed:24880340). Promotes lipid uptake into adipocytes and hepatocytes via transcriptional up-regulation of genes involved in fatty acid uptake (PubMed:22351773). {ECO:0000269|PubMed:22351773, ECO:0000269|PubMed:24880340}. PTM: N-glycosylated. {ECO:0000269|PubMed:22351773}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22351773, ECO:0000269|PubMed:24880340}. SUBUNIT: Homodimer; disulfide-linked. May form heteromeric complexes with C1QTNF2 and C1QTNF12 and, to a lesser extent, with C1QTNF5 and C1QTNF10. {ECO:0000269|PubMed:22351773}. TISSUE SPECIFICITY: Predominantly expressed in skeletal muscle and, at much lower levels, in other tissues, including lung, eye, smooth muscle, heart, brain and kidney. Within skeletal muscles, higher expression levels in soleus as compared with plantaris. Found in blood (at protein level). Following EPO treatment, only expressed in bone marrow and spleen (PubMed:24880340). Females tend to have higher circulating levels than males. Obese mice tend to have lower expression and circulating levels as compared to lean animals. {ECO:0000269|PubMed:22351773, ECO:0000269|PubMed:24880340}. +Q8K0S2 ERIC5_MOUSE Glutamate-rich protein 5 362 38,527 Chain (1); Compositional bias (1); Modified residue (1) +Q91X78 ERLN1_MOUSE Erlin-1 (Endoplasmic reticulum lipid raft-associated protein 1) (Protein KE04 homolog) (Stomatin-prohibitin-flotillin-HflC/K domain-containing protein 1) (SPFH domain-containing protein 1) 346 38,937 Chain (1); Erroneous initiation (2); Glycosylation (1); Modified residue (1); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 6 26 Helical. {ECO:0000255}. TOPO_DOM 1 5 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 27 346 Lumenal. {ECO:0000255}. FUNCTION: Component of the ERLIN1/ERLIN2 complex which mediates the endoplasmic reticulum-associated degradation (ERAD) of inositol 1,4,5-trisphosphate receptors (IP3Rs). Involved in regulation of cellular cholesterol homeostasis by regulation the SREBP signaling pathway. Binds cholesterol and may promote ER retention of the SCAP-SREBF complex (By similarity). {ECO:0000250|UniProtKB:O75477}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Associated with lipid raft-like domains of the endoplasmic reticulum membrane. {ECO:0000250}. SUBUNIT: Forms a heteromeric complex with ERLIN2 (By similarity). In complex with ERLIN2, interacts with RNF170 (PubMed:21610068). Interacts with AMFR and SYVN1 (By similarity). {ECO:0000250|UniProtKB:O75477, ECO:0000269|PubMed:21610068}. +Q80SS6 GPBAR_MOUSE G-protein coupled bile acid receptor 1 (Membrane-type receptor for bile acids) (M-BAR) 329 35,650 Chain (1); Disulfide bond (1); Glycosylation (2); Topological domain (8); Transmembrane (7) TRANSMEM 16 36 Helical; Name=1. {ECO:0000255}.; TRANSMEM 50 70 Helical; Name=2. {ECO:0000255}.; TRANSMEM 85 105 Helical; Name=3. {ECO:0000255}.; TRANSMEM 125 145 Helical; Name=4. {ECO:0000255}.; TRANSMEM 165 185 Helical; Name=5. {ECO:0000255}.; TRANSMEM 230 250 Helical; Name=6. {ECO:0000255}.; TRANSMEM 261 281 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 15 Extracellular. {ECO:0000255}.; TOPO_DOM 37 49 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 71 84 Extracellular. {ECO:0000255}.; TOPO_DOM 106 124 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 146 164 Extracellular. {ECO:0000255}.; TOPO_DOM 186 229 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 251 260 Extracellular. {ECO:0000255}.; TOPO_DOM 282 329 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for bile acid. Bile acid-binding induces its internalization, activation of extracellular signal-regulated kinase and intracellular cAMP production. May be involved in the suppression of macrophage functions by bile acids (By similarity). Involved in bile acid promoted GLP1R secretion. {ECO:0000250, ECO:0000269|PubMed:15721318}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q8BFZ9 ERLN2_MOUSE Erlin-2 (Endoplasmic reticulum lipid raft-associated protein 2) (Stomatin-prohibitin-flotillin-HflC/K domain-containing protein 2) (SPFH domain-containing protein 2) 340 37,873 Chain (1); Glycosylation (1); Modified residue (1); Region (1); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 4 24 Helical. {ECO:0000255}. TOPO_DOM 1 3 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 25 340 Lumenal. {ECO:0000255}. FUNCTION: Component of the ERLIN1/ERLIN2 complex which mediates the endoplasmic reticulum-associated degradation (ERAD) of inositol 1,4,5-trisphosphate receptors (IP3Rs) such as ITPR1. Promotes sterol-accelerated ERAD of HMGCR probably implicating an AMFR/gp78-containing ubiquitin ligase complex. Involved in regulation of cellular cholesterol homeostasis by regulation the SREBP signaling pathway. May promote ER retention of the SCAP-SREBF complex (By similarity). {ECO:0000250|UniProtKB:O94905}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Associated with lipid raft-like domains of the endoplasmic reticulum membrane. {ECO:0000250}. SUBUNIT: Forms a heteromeric complex with ERLIN1 (By similarity). In complex with ERLIN1, interacts with RNF170 (PubMed:21610068). Interacts with activated ITPR1, independently of the degree of ITPR1 polyubiquitination (PubMed:17502376). Interacts with SCAP, INSIG1, SREBF1 and SREBF2 under cholesterol sufficiency conditions; indicative for an association with the SCAP-SREBP-INSIG complex (By similarity). Probably part of an AMFR/gp78 and INSIG1-containing ubiquitin ligase complex involved in ERAD of HMGCR (By similarity). Interacts with TMUB1; TMUB1 bridges the association with AMFR (By similarity). Interacts with SYVN1 and RNF139 (By similarity). Interacts with TMEM259 (PubMed:25977983). {ECO:0000250|UniProtKB:O94905, ECO:0000269|PubMed:17502376, ECO:0000269|PubMed:21610068, ECO:0000269|PubMed:25977983}. +Q6NZP2 GPBL1_MOUSE Vasculin-like protein 1 (GC-rich promoter-binding protein 1-like 1) 473 51,966 Chain (1); Erroneous termination (1); Modified residue (6); Sequence conflict (4) FUNCTION: Possible transcription factor. {ECO:0000305}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q9JLN5 ERMAP_MOUSE Erythroid membrane-associated protein 566 63,512 Alternative sequence (3); Chain (1); Disulfide bond (1); Domain (2); Erroneous initiation (3); Glycosylation (2); Modified residue (1); Sequence conflict (8); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 247 267 Helical. {ECO:0000255}. TOPO_DOM 30 246 Extracellular. {ECO:0000255}.; TOPO_DOM 268 566 Cytoplasmic. {ECO:0000255}. FUNCTION: Possible role as a cell-adhesion or receptor molecule of erythroid cells. PTM: Glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q96PL5}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:10721728}. TISSUE SPECIFICITY: Expressed in spleen and bone marrow. {ECO:0000269|PubMed:10721728}. +Q3UVK0 ERMP1_MOUSE Endoplasmic reticulum metallopeptidase 1 (EC 3.4.-.-) (Felix-ina) 898 100,148 Active site (1); Alternative sequence (2); Chain (1); Disulfide bond (1); Erroneous initiation (2); Glycosylation (2); Metal binding (6); Modified residue (1); Sequence conflict (2); Site (1); Topological domain (10); Transmembrane (9) TRANSMEM 67 87 Helical; Name=1. {ECO:0000255}.; TRANSMEM 394 414 Helical; Name=2. {ECO:0000255}.; TRANSMEM 452 472 Helical; Name=3. {ECO:0000255}.; TRANSMEM 481 501 Helical; Name=4. {ECO:0000255}.; TRANSMEM 516 538 Helical; Name=5. {ECO:0000255}.; TRANSMEM 543 562 Helical; Name=6. {ECO:0000255}.; TRANSMEM 574 594 Helical; Name=7. {ECO:0000255}.; TRANSMEM 616 636 Helical; Name=8. {ECO:0000255}.; TRANSMEM 646 666 Helical; Name=9. {ECO:0000255}. TOPO_DOM 1 66 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 88 393 Lumenal. {ECO:0000305}.; TOPO_DOM 415 451 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 473 480 Lumenal. {ECO:0000305}.; TOPO_DOM 502 515 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 539 542 Lumenal. {ECO:0000305}.; TOPO_DOM 563 573 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 595 615 Lumenal. {ECO:0000305}.; TOPO_DOM 637 645 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 667 898 Lumenal. {ECO:0000305}. FUNCTION: Within the ovary, required for the organization of somatic cells and oocytes into discrete follicular structures. {ECO:0000250|UniProtKB:Q6UPR8}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q6UPR8}; Multi-pass membrane protein {ECO:0000255}. +Q9D8U3 ERP27_MOUSE Endoplasmic reticulum resident protein 27 (ER protein 27) (ERp27) 272 30,693 Chain (1); Domain (1); Glycosylation (2); Motif (1); Region (1); Sequence conflict (6); Signal peptide (1) SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138}. SUBUNIT: Interacts with PDIA3. {ECO:0000250}. +P43142 GP182_MOUSE G-protein coupled receptor 182 (G10D) (NOW) 395 45,497 Chain (1); Disulfide bond (1); Glycosylation (2); Modified residue (1); Topological domain (8); Transmembrane (7) TRANSMEM 54 75 Helical; Name=1. {ECO:0000255}.; TRANSMEM 87 109 Helical; Name=2. {ECO:0000255}.; TRANSMEM 124 145 Helical; Name=3. {ECO:0000255}.; TRANSMEM 167 189 Helical; Name=4. {ECO:0000255}.; TRANSMEM 214 235 Helical; Name=5. {ECO:0000255}.; TRANSMEM 255 276 Helical; Name=6. {ECO:0000255}.; TRANSMEM 296 316 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 53 Extracellular. {ECO:0000255}.; TOPO_DOM 76 86 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 110 123 Extracellular. {ECO:0000255}.; TOPO_DOM 146 166 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 190 213 Extracellular. {ECO:0000255}.; TOPO_DOM 236 254 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 277 295 Extracellular. {ECO:0000255}.; TOPO_DOM 317 395 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed in liver and lung. +P54763 EPHB2_MOUSE Ephrin type-B receptor 2 (EC 2.7.10.1) (Neural kinase) (Nuk receptor tyrosine kinase) (Tyrosine-protein kinase receptor EPH-3) (Tyrosine-protein kinase receptor SEK-3) [Cleaved into: EphB2/CTF1; EphB2/CTF2] 986 109,899 Active site (1); Alternative sequence (2); Beta strand (26); Binding site (1); Chain (3); Compositional bias (1); Disulfide bond (2); Domain (5); Erroneous initiation (2); Glycosylation (4); Helix (16); Motif (1); Mutagenesis (2); Nucleotide binding (1); Signal peptide (1); Site (2); Topological domain (2); Transmembrane (1); Turn (4) TRANSMEM 544 564 Helical. {ECO:0000255}. TOPO_DOM 19 543 Extracellular. {ECO:0000255}.; TOPO_DOM 565 986 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor tyrosine kinase which binds promiscuously transmembrane ephrin-B family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Functions in axon guidance during development. Involved in the guidance of commissural axons, that form a major interhemispheric connection between the 2 temporal lobes of the cerebral cortex. Also involved in guidance of contralateral inner ear efferent growth cones at the midline and of retinal ganglion cell axons to the optic disk. In addition to axon guidance, also regulates dendritic spines development and maturation and stimulates the formation of excitatory synapses. Upon activation by EFNB1, abolishes the ARHGEF15-mediated negative regulation on excitatory synapse formation. Controls other aspects of development including angiogenesis, palate development and in inner ear development through regulation of endolymph production. Forward and reverse signaling through the EFNB2/EPHB2 complex regulate movement and adhesion of cells that tubularize the urethra and septate the cloaca. May function as a tumor suppressor. {ECO:0000269|PubMed:10839360, ECO:0000269|PubMed:14691139, ECO:0000269|PubMed:15223334, ECO:0000269|PubMed:21029865, ECO:0000269|PubMed:8689685, ECO:0000269|PubMed:8947026, ECO:0000269|PubMed:9990854}. PTM: Autophosphorylated; ligand binding stimulates autophosphorylation on tyrosine residues. {ECO:0000269|PubMed:17428795}.; PTM: Polyubiquitinated; ligand binding stimulates ubiquitination. {ECO:0000269|PubMed:17428795, ECO:0000269|PubMed:28931592}.; PTM: Ligand binding induces cleavage by matrix metalloproteinases (MMPs) such as MMP7/MMP9, producing an EphB2/N-terminal fragment (NTF) and a C-terminal long fragment (EphB2-LF). EphB2-LF is further cleaved by MMPs, producing EphB2/CTF1 which is further cleaved by the PS1/gamma-secretase producing EphB2/CTF2. {ECO:0000269|PubMed:17428795}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Cell projection, axon. Cell projection, dendrite. SUBUNIT: Heterotetramer upon binding of the ligand (PubMed:11780069). The heterotetramer is composed of an ephrin dimer and a receptor dimer (PubMed:11780069). Interacts (via PDZ-binding motif) with GRIP1 and PICK1 (via PDZ domain) (PubMed:9883737). Interacts with ARHGEF15; mediates ARHGEF15 phosphorylation, ubiquitination and degradation by the proteasome (PubMed:21029865). Interacts with AQP1; involved in endolymph production in the inner ear (PubMed:10839360). Interacts with EFNA5 (PubMed:15107857). Interacts with SPSB1 (By similarity). Interacts with SPSB4 (PubMed:28931592). {ECO:0000250|UniProtKB:P29323, ECO:0000269|PubMed:10839360, ECO:0000269|PubMed:11780069, ECO:0000269|PubMed:15107857, ECO:0000269|PubMed:21029865, ECO:0000269|PubMed:28931592, ECO:0000269|PubMed:9883737}. TISSUE SPECIFICITY: Expressed in the epithelial dark cells of the inner ear. Expressed in the region of the proximal tubules of the kidney nephron. Expressed in myogenic progenitor cells (PubMed:27446912). {ECO:0000269|PubMed:10839360, ECO:0000269|PubMed:27446912}. +Q8C9X6 EPC1_MOUSE Enhancer of polycomb homolog 1 813 90,411 Alternative sequence (1); Chain (1); Cross-link (2); Modified residue (1) FUNCTION: Component of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when directly recruited to sites of DNA damage (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the NuA4 histone acetyltransferase complex which contains the catalytic subunit KAT5/TIP60 and the subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6. HTATTIP/TIP60, EPC1, and ING3 together constitute a minimal HAT complex termed Piccolo NuA4. Component of a NuA4-related complex which contains EP400, TRRAP/PAF400, SRCAP, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, actin, ACTL6A/BAF53A, VPS72 and YEATS4/GAS41. The NuA4 complex interacts with MYC. EPC1 interacts with TRIM27 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in adult brain, heart, kidney, liver, lung, skeletal muscle and testis. {ECO:0000269|PubMed:9735366}. +Q80VP1 EPN1_MOUSE Epsin-1 (EPS-15-interacting protein 1) (Intersectin-EH-binding protein 1) (Ibp1) 575 60,212 Alternative sequence (1); Binding site (5); Chain (1); Compositional bias (1); Domain (4); Modified residue (13); Motif (1); Region (2); Repeat (11) FUNCTION: Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Modifies membrane curvature and facilitates the formation of clathrin-coated invaginations (By similarity). Regulates receptor-mediated endocytosis. {ECO:0000250}. PTM: Phosphorylated on serine and/or threonine residues in mitotic cells. Phosphorylation reduces interaction with REPS2, AP-2 and the membrane fraction. Depolarization of synaptosomes results in dephosphorylation. {ECO:0000269|PubMed:9920862}.; PTM: Ubiquitinated. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Nucleus {ECO:0000250}. Membrane, clathrin-coated pit {ECO:0000250}. Note=Associated with the cytoplasmic membrane at sites where clathrin-coated pits are forming. Colocalizes with clathrin and AP-2 in a punctate pattern on the plasma membrane. Detected in presynaptic nerve terminals and in Golgi stacks. May shuttle to the nucleus when associated with ZBTB16/ZNF145 (By similarity). {ECO:0000250}. SUBUNIT: Monomer. Binds clathrin, ZBTB16/ZNF145, REPS2 and EPS15 (By similarity). Binds ubiquitinated proteins (By similarity). Interacts with RALBP1 in a complex also containing NUMB and TFAP2A during interphase and mitosis (By similarity). Interacts with AP2B1 (By similarity). Interacts with UBQLN2 (By similarity). Interacts with ITSN1. Interacts with AP2A1 and AP2A2. {ECO:0000250|UniProtKB:O88339, ECO:0000250|UniProtKB:Q9Y6I3, ECO:0000269|PubMed:9813051, ECO:0000269|PubMed:9920862}. DOMAIN: The NPF repeat domain is involved in EPS15 binding.; DOMAIN: The DPW repeat domain is involved in AP2A2 and clathrin binding.; DOMAIN: The [DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif mediates interaction the AP-2 complex subunit AP2B1. {ECO:0000250}. +Q03145 EPHA2_MOUSE Ephrin type-A receptor 2 (EC 2.7.10.1) (Epithelial cell kinase) (Tyrosine-protein kinase receptor ECK) (Tyrosine-protein kinase receptor MPK-5) (Tyrosine-protein kinase receptor SEK-2) 977 108,852 Active site (1); Binding site (1); Chain (1); Compositional bias (1); Disulfide bond (2); Domain (5); Glycosylation (2); Helix (6); Modified residue (14); Motif (1); Mutagenesis (11); Nucleotide binding (1); Region (3); Sequence conflict (19); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 539 559 Helical. {ECO:0000255}. TOPO_DOM 26 538 Extracellular. {ECO:0000255}.; TOPO_DOM 560 977 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor tyrosine kinase which binds promiscuously membrane-bound ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Activated by the ligand ephrin-A1/EFNA1 regulates migration, integrin-mediated adhesion, proliferation and differentiation of cells (PubMed:29749928). Regulates cell adhesion and differentiation through DSG1/desmoglein-1 and inhibition of the ERK1/ERK2 signaling pathway. May also participate in UV radiation-induced apoptosis and have a ligand-independent stimulatory effect on chemotactic cell migration. During development, may function in distinctive aspects of pattern formation and subsequently in development of several fetal tissues. Involved for instance in angiogenesis, in early hindbrain development and epithelial proliferation and branching morphogenesis during mammary gland development. Engaged by the ligand ephrin-A5/EFNA5 may regulate lens fiber cells shape and interactions and be important for lens transparency development and maintenance. With ephrin-A2/EFNA2 may play a role in bone remodeling through regulation of osteoclastogenesis and osteoblastogenesis. {ECO:0000269|PubMed:15054110, ECO:0000269|PubMed:16782872, ECO:0000269|PubMed:16849550, ECO:0000269|PubMed:18387945, ECO:0000269|PubMed:18948590, ECO:0000269|PubMed:19299512, ECO:0000269|PubMed:19321667, ECO:0000269|PubMed:29749928}. PTM: Autophosphorylates. Phosphorylated at Ser-898 by PKB; serum-induced phosphorylation which targets EPHA2 to the cell leading edge and stimulates cell migration. Phosphorylation by PKB is inhibited by EFNA1-activated EPHA2 which regulates PKB activity via a reciprocal regulatory loop. Phosphorylated on tyrosine upon binding and activation by EFNA1. Phosphorylated residues Tyr-589 and Tyr-595 are required for binding VAV2 and VAV3 while phosphorylated residues Tyr-736 and Tyr-931 are required for binding PI3-kinase p85 subunit (PIK3R1, PIK3R2 or PIK3R3). These phosphorylated residues are critical for recruitment of VAV2 and VAV3 and PI3-kinase p85 subunit which transduce downstream signaling to activate RAC1 GTPase and cell migration. Dephosphorylation of Tyr-931 by PTPRF prevents the interaction of EPHA2 with NCK1. Phosphorylated at Ser-898 in response to TNF by RPS6KA1 and RPS6KA3; RPS6KA-EPHA2 signaling pathway controls cell migration. Phosphorylated at Ser-898 by PKA; blocks cell retraction induced by EPHA2 kinase activity. Dephosphorylated by ACP1. {ECO:0000250|UniProtKB:P29317, ECO:0000269|PubMed:18387945}.; PTM: Ubiquitinated by CHIP/STUB1. Ubiquitination is regulated by the HSP90 chaperone and regulates the receptor stability and activity through proteasomal degradation. ANKS1A prevents ubiquitination and degradation. {ECO:0000269|PubMed:20100865}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P29317}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:P29317}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, lamellipodium membrane {ECO:0000250|UniProtKB:P29317}; Single-pass type I membrane protein {ECO:0000255}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:P29317}. Note=Present at regions of cell-cell contacts but also at the leading edge of migrating cells. Relocates from the plasma membrane to the cytoplasmic and perinuclear regions in cancer cells. {ECO:0000250|UniProtKB:P29317}. SUBUNIT: Homodimer. Interacts with INPPL1; regulates activated EPHA2 endocytosis and degradation (PubMed:29749928). Interacts (inactivated form) with PTK2/FAK1 and interacts (EFNA1 ligand-activated form) with PTPN11; regulates integrin-mediated adhesion. Interacts with ARHGEF16, DOCK4 and ELMO2; mediates ligand-independent activation of RAC1 which stimulates cell migration. Interacts with CLDN4; phosphorylates CLDN4 and may regulate tight junctions. Interacts with ACP1. Interacts with CEMIP. Interacts with NCK1; may regulate EPHA2 activity in cell migration and adhesion. Interacts with SLA. Interacts (phosphorylated form) with VAV2, VAV3 and PI3-kinase p85 subunit (PIK3R1, PIK3R2 or PIK3R3); critical for the EFNA1-induced activation of RAC1 which stimulates cell migration. Interacts with ANKS1A. {ECO:0000269|PubMed:16782872, ECO:0000269|PubMed:18387945, ECO:0000269|PubMed:20100865, ECO:0000269|PubMed:29749928, ECO:0000269|PubMed:7543898}. TISSUE SPECIFICITY: Expressed in the lung, intestine and liver (PubMed:11287184). Expressed in myogenic progenitor cells (PubMed:27446912). {ECO:0000269|PubMed:11287184, ECO:0000269|PubMed:27446912}. +P70186 EPYC_MOUSE Epiphycan (Dermatan sulfate proteoglycan 3) (Proteoglycan-Lb) (PG-Lb) (Small chondroitin/dermatan sulfate proteoglycan) 322 36,763 Chain (1); Disulfide bond (2); Domain (1); Glycosylation (4); Repeat (6); Signal peptide (1) FUNCTION: May have a role in bone formation and also in establishing the ordered structure of cartilage through matrix organization. PTM: The O-linked polysaccharide on Ser-96 is probably the mucin type linked to GalNAc. There is one glycosaminoglycan chain, known to be dermatan sulfate, and it is probably the O-glycosylation at Ser-64 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. Note=Surrounding resting, proliferating, and hypertrophic chondrocytes. TISSUE SPECIFICITY: Confined to the middle zone of embryonic epiphyseal cartilage consisting of flattened chondrocytes and the ossifying region in the limb buds of chick embryos. Has also been detected in testis. {ECO:0000269|PubMed:8836137}. +Q3V1F8 EPHX3_MOUSE Epoxide hydrolase 3 (EH3) (EC 3.3.2.10) (Abhydrolase domain-containing protein 9) 367 41,853 Active site (3); Chain (1); Erroneous initiation (1); Transmembrane (1) TRANSMEM 22 42 Helical. {ECO:0000255}. FUNCTION: Catalyzes the hydrolysis of epoxide-containing fatty acids. Active in vitro against epoxyeicosatrienoic acids (EETs) including 8,9-EET, 9,10-EET, 11,12-EET and 14,15-EET and leukotoxin. {ECO:0000250|UniProtKB:Q9H6B9}. SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250|UniProtKB:Q9H6B9}; Single-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Predominantly expressed in skin, esophagus, lung and tongue and to a lesser extent in pancreas and eye. {ECO:0000269|PubMed:22798687}. +Q61526 ERBB3_MOUSE Receptor tyrosine-protein kinase erbB-3 (EC 2.7.10.1) (Glial growth factor receptor) (Proto-oncogene-like protein c-ErbB-3) 1339 147,613 Active site (1); Binding site (1); Chain (1); Disulfide bond (21); Domain (1); Glycosylation (10); Modified residue (2); Nucleotide binding (3); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 642 662 Helical. {ECO:0000255}. TOPO_DOM 20 641 Extracellular. {ECO:0000255}.; TOPO_DOM 663 1339 Cytoplasmic. {ECO:0000255}. FUNCTION: Tyrosine-protein kinase that plays an essential role as cell surface receptor for neuregulins. Binds to neuregulin-1 (NRG1) and is activated by it; ligand-binding increases phosphorylation on tyrosine residues and promotes its association with the p85 subunit of phosphatidylinositol 3-kinase. May also be activated by CSPG5. {ECO:0000250|UniProtKB:P21860}. PTM: Autophosphorylated. Ligand-binding increases phosphorylation on tyrosine residues and promotes its association with the p85 subunit of phosphatidylinositol 3-kinase. {ECO:0000250|UniProtKB:P21860}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Monomer and homodimer. Heterodimer with each of the other ERBB receptors (Potential). Interacts with CSPG5, PA2G4, GRB7 and MUC1 (By similarity). Interacts with MYOC (PubMed:23897819). Found in a ternary complex with NRG1 and ITGAV:ITGB3 or ITGA6:ITGB4 (By similarity). {ECO:0000250|UniProtKB:P21860, ECO:0000269|PubMed:23897819, ECO:0000305}. DOMAIN: The cytoplasmic part of the receptor may interact with the SH2 or SH3 domains of many signal-transducing proteins. TISSUE SPECIFICITY: In the muscle, expression localizes to the synaptic sites of muscle fibers. +Q149F3 ERF3B_MOUSE Eukaryotic peptide chain release factor GTP-binding subunit ERF3B (Eukaryotic peptide chain release factor subunit 3b) (eRF3b) (G1 to S phase transition protein 2 homolog) 632 69,147 Chain (1); Domain (1); Erroneous initiation (1); Frameshift (1); Nucleotide binding (3); Region (5); Sequence conflict (5); Site (2) FUNCTION: Involved in translation termination in response to the termination codons UAA, UAG and UGA. May play a role as a potent stimulator of the release factor activity of ETF1. Exhibits GTPase activity, which is ribosome- and ETF1-dependent. May play a role in cell cycle progression. Component of the transient SURF complex which recruits UPF1 to stalled ribosomes in the context of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons (By similarity). {ECO:0000250, ECO:0000269|PubMed:12354098}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. SUBUNIT: Interacts with ETF1. Component of the transient SURF (SMG1-UPF1-eRF1-eRF3) complex. Interacts with UPF1 and PABPC1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in brain. Moderately expressed in spleen and lung. Weakly expressed in heart, liver and kidney. Expression during the cell-cycle progression is constant. {ECO:0000269|PubMed:9712840}. +Q80TH2 ERBIN_MOUSE Erbin (Densin-180-like protein) (Erbb2-interacting protein) (Protein LAP2) 1402 157,248 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (1); Modified residue (22); Mutagenesis (1); Repeat (17); Sequence conflict (3) FUNCTION: Acts as an adapter for the receptor ERBB2, in epithelia. By binding the unphosphorylated ERBB2 'Tyr-1248' receptor, it may contribute to stabilize this unphosphorylated state (By similarity). Inhibits NOD2-dependent NF-kappa-B signaling and proinflammatory cytokine secretion (PubMed:16203728). {ECO:0000250|UniProtKB:Q96RT1, ECO:0000269|PubMed:16203728}. PTM: Isoform 2 is phosphorylated on Ser-1231 and Ser-1234. SUBCELLULAR LOCATION: Cell junction, hemidesmosome {ECO:0000250|UniProtKB:Q96RT1}. Nucleus membrane {ECO:0000269|PubMed:18802028}. Basolateral cell membrane {ECO:0000269|PubMed:16203728}. Note=Found in hemidesmosomes, which are cell-substrate adhesion complexes in stratified epithelia. In transfected cells, either diffusely distributed over the cytoplasm or concentrated at the basolateral membrane (By similarity). Colocalizes with the adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane of cardiac myocytes. {ECO:0000250|UniProtKB:Q96RT1}. SUBUNIT: Interacts with ERBB2, BPAG1 and ITGB4. May favor the localization of ERBB2, by restricting its presence to the basolateral membrane of epithelial cells. Also found to interact with ARVCF and delta catenin. Interacts (via C-terminus) with DST (via N-terminus) (By similarity). Interacts with NOD2 (via CARD domain) (PubMed:16203728). {ECO:0000250|UniProtKB:Q96RT1, ECO:0000269|PubMed:16203728}. +Q8CHI8 EP400_MOUSE E1A-binding protein p400 (EC 3.6.4.-) (Domino homolog) (mDomino) (p400 kDa SWI2/SNF2-related protein) 3072 337,180 Alternative sequence (4); Chain (1); Compositional bias (11); Domain (4); Erroneous initiation (1); Modified residue (20); Motif (1); Nucleotide binding (1); Region (2); Sequence caution (2); Sequence conflict (14) FUNCTION: Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. May be required for transcriptional activation of E2F1 and MYC target genes during cellular proliferation. The NuA4 complex ATPase and helicase activities seem to be, at least in part, contributed by the association of RUVBL1 and RUVBL2 with EP400. Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AFZ from the nucleosome (By similarity). Regulates transcriptional activity of ZNF42. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00549}. SUBUNIT: Component of the NuA4 histone acetyltransferase complex which contains the catalytic subunit KAT5/TIP60 and the subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6. May also participate in the formation of NuA4 related complexes which lack the KAT5/TIP60 catalytic subunit, but which include the SWI/SNF related protein SRCAP. The NuA4 complex interacts with MYC. EP400 interacts with TRRAP, RUVBL1 and RUVBL2. Component of a SWR1-like complex (By similarity). Interacts with ZNF42. Interacts with PHF5A. {ECO:0000250, ECO:0000269|PubMed:12653961, ECO:0000269|PubMed:18758164}. TISSUE SPECIFICITY: Expressed in brain, thymus, lung, liver, spleen, kidney, colon and bone marrow. +P52019 ERG1_MOUSE Squalene monooxygenase (EC 1.14.14.17) (Squalene epoxidase) (SE) 572 63,770 Chain (1); Nucleotide binding (1); Transmembrane (4) TRANSMEM 20 40 Helical. {ECO:0000255}.; TRANSMEM 60 80 Helical. {ECO:0000255}.; TRANSMEM 118 138 Helical. {ECO:0000255}.; TRANSMEM 544 564 Helical. {ECO:0000255}. Terpene metabolism; lanosterol biosynthesis; lanosterol from farnesyl diphosphate: step 2/3. FUNCTION: Catalyzes the first oxygenation step in sterol biosynthesis and is suggested to be one of the rate-limiting enzymes in this pathway. SUBCELLULAR LOCATION: Microsome membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. SUBUNIT: May form a complex with squalene synthase. +Q71KT5 ERG24_MOUSE Delta(14)-sterol reductase (Delta-14-SR) (EC 1.3.1.70) (C-14 sterol reductase) (C14SR) (Sterol C14-reductase) (Transmembrane 7 superfamily member 2) 418 46,521 Binding site (6); Chain (1); Nucleotide binding (2); Sequence conflict (2); Transmembrane (7) TRANSMEM 13 35 Helical. {ECO:0000255}.; TRANSMEM 62 81 Helical. {ECO:0000255}.; TRANSMEM 102 124 Helical. {ECO:0000255}.; TRANSMEM 129 148 Helical. {ECO:0000255}.; TRANSMEM 255 277 Helical. {ECO:0000255}.; TRANSMEM 287 304 Helical. {ECO:0000255}.; TRANSMEM 355 377 Helical. {ECO:0000255}. FUNCTION: Involved in the conversion of lanosterol to cholesterol. {ECO:0000269|Ref.2}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Microsome membrane {ECO:0000269|Ref.2}; Multi-pass membrane protein {ECO:0000269|Ref.2}. TISSUE SPECIFICITY: Strongly expressed in liver, weaker in ovary, testis, kidney and brain. {ECO:0000269|Ref.2}. +Q69ZC8 GPAM1_MOUSE GPALPP motifs-containing protein 1 346 38,955 Chain (1); Compositional bias (1); Cross-link (2); Erroneous initiation (1); Initiator methionine (1); Modified residue (6); Motif (4) +Q61858 GPAN1_MOUSE G patch domain and ankyrin repeat-containing protein 1 (G5 protein) (HLA-B-associated transcript 4) 372 41,011 Chain (1); Cross-link (1); Domain (1); Repeat (2); Sequence conflict (1) +Q8C460 ERI3_MOUSE ERI1 exoribonuclease 3 (EC 3.1.-.-) (Prion interactor 1) (Prion protein-interacting protein) 337 37,189 Active site (2); Alternative sequence (3); Binding site (2); Chain (1); Domain (1); Metal binding (5) SUBUNIT: Interacts with PRNP. {ECO:0000269|PubMed:11571277}. TISSUE SPECIFICITY: Highly expressed in the brain, heart, thyroid and testis. Expressed at low levels in the muscle cells, liver, pancreas and kidney. {ECO:0000269|PubMed:11571277}. +D3Z6S9 ERIP6_MOUSE Glutamate-rich protein 6 (Protein FAM194A) 713 80,949 Chain (1); Compositional bias (1) +Q8K2C8 GPAT4_MOUSE Glycerol-3-phosphate acyltransferase 4 (GPAT4) (EC 2.3.1.15) (1-acylglycerol-3-phosphate O-acyltransferase 6) (1-AGP acyltransferase 6) (1-AGPAT 6) (Acyl-CoA:glycerol-3-phosphate acyltransferase 4) (Lysophosphatidic acid acyltransferase zeta) (LPAAT-zeta) (Testis spermatogenesis apoptosis-related protein 7) 456 52,181 Chain (1); Glycosylation (4); Motif (1); Sequence conflict (1); Signal peptide (1); Transmembrane (2) TRANSMEM 156 176 Helical. {ECO:0000255}.; TRANSMEM 180 200 Helical. {ECO:0000255}. Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 1/3. FUNCTION: Esterifies acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipid biosynthesis. Active against both saturated and unsaturated long-chain fatty acyl-CoAs. {ECO:0000250|UniProtKB:Q86UL3, ECO:0000269|PubMed:18238778}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q86UL3}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q86UL3}. DOMAIN: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in testis. {ECO:0000269|PubMed:15944755}. +Q8VEH8 ERLEC_MOUSE Endoplasmic reticulum lectin 1 (ER lectin) (Erlectin) 483 54,906 Chain (1); Domain (2); Glycosylation (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Probable lectin that binds selectively to improperly folded lumenal proteins. May function in endoplasmic reticulum quality control and endoplasmic reticulum-associated degradation (ERAD) of both non-glycosylated proteins and glycoproteins (By similarity). {ECO:0000250}. PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250}. SUBUNIT: May form a complex with OS9, HSPA5, SYVN1, and SEL1L with which it interacts directly. Interacts (via PRKCSH 2 domain) with KREMEN2 (when glycosylated). Interacts with HSPA5 (By similarity). {ECO:0000250}. +Q6NXH3 GPBP1_MOUSE Vasculin (GC-rich promoter-binding protein 1) (mGPBP) 473 53,423 Alternative sequence (2); Chain (1); Erroneous initiation (1); Modified residue (6); Sequence conflict (2) FUNCTION: Functions as a GC-rich promoter-specific transactivating transcription factor. {ECO:0000269|PubMed:14612417}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14612417}. SUBUNIT: Interacts with GTF2B, GTF2F2, RNA polymerase II and TBP. {ECO:0000269|PubMed:14612417}. TISSUE SPECIFICITY: Ubiquitously expressed (at protein level). {ECO:0000269|PubMed:14612417}. +Q9QZF2 GPC1_MOUSE Glypican-1 [Cleaved into: Secreted glypican-1] 557 61,360 Chain (2); Disulfide bond (7); Glycosylation (5); Lipidation (1); Propeptide (1); Signal peptide (1) FUNCTION: Cell surface proteoglycan that bears heparan sulfate. Binds, via the heparan sulfate side chains, alpha-4 (V) collagen and participates in Schwann cell myelination (By similarity). May act as a catalyst in increasing the rate of conversion of prion protein PRPN(C) to PRNP(Sc) via associating (via the heparan sulfate side chains) with both forms of PRPN, targeting them to lipid rafts and facilitating their interaction. Required for proper skeletal muscle differentiation by sequestering FGF2 in lipid rafts preventing its binding to receptors (FGFRs) and inhibiting the FGF-mediated signaling. Binds Cu(2+) or Zn(2+) ions. {ECO:0000250, ECO:0000269|PubMed:19732411, ECO:0000269|PubMed:19936054, ECO:0000269|PubMed:20100867, ECO:0000269|PubMed:21996748}. PTM: S-nitrosylated in a Cu(2+)-dependent manner. Nitric acid (NO) is released from the nitrosylated cysteines by ascorbate or by some other reducing agent, in a Cu(2+) or Zn(2+) dependent manner. This free nitric oxide is then capable of cleaving the heparan sulfate side chains. {ECO:0000269|PubMed:15677459}.; PTM: N- and O-glycosylated. N-glycosylation is mainly of the complex type containing sialic acid. O-glycosylated with heparan sulfate. The heparan sulfate chains can be cleaved either by the action of heparanase or, degraded by a deaminative process that uses nitric oxide (NO) released from the S-nitrosylated cysteines. This process is triggered by ascorbate, or by some other reducing agent, in a Cu(2+)- or Zn(2+) dependent manner. Cu(2+) ions are provided by ceruloproteins such as APP, PRNP or CP which associate with GCP1 in intracellular compartments or lipid rafts. {ECO:0000269|PubMed:12732622, ECO:0000269|PubMed:15677459, ECO:0000269|PubMed:16971378, ECO:0000269|PubMed:18717736, ECO:0000269|PubMed:19656770}.; PTM: This cell-associated glypican is further processed to give rise to a medium-released species. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor; Extracellular side. Endosome. Note=S-nitrosylated form recycled in endosomes. Localizes to CAV1-containing vesicles close to the cell surface. Cleavage of heparan sulfate side chains takes place mainly in late endosomes. Associates with both forms of PRNP in lipid rafts. Colocalizes with APP in perinuclear compartments and with CP in intracellular compartments. Associates with fibrillar APP amyloid-beta peptides in lipid rafts in Alzheimer disease brains.; SUBCELLULAR LOCATION: Secreted glypican-1: Secreted, extracellular space. +Q8R2E9 ERO1B_MOUSE ERO1-like protein beta (ERO1-L-beta) (EC 1.8.4.-) (Endoplasmic reticulum oxidoreductase beta) (Endoplasmic reticulum oxidoreductin-1-like protein B) (Oxidoreductin-1-L-beta) 467 53,518 Binding site (7); Chain (1); Disulfide bond (6); Glycosylation (4); Mutagenesis (1); Signal peptide (1) FUNCTION: Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme catalyzing protein disulfide formation, in order to allow P4HB to sustain additional rounds of disulfide formation. Other protein disulfide isomerase family members can also be reoxidized, but at lower rates compared to P4HB, including PDIA2, PDIA3, PDIA4, PDIA6 and NXNDC12. Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell (By similarity). Involved in oxidative proinsulin folding in pancreatic cells, hence required for glucose homeostasis in vivo. {ECO:0000250, ECO:0000269|PubMed:20308425}. PTM: N-glycosylated. {ECO:0000250}.; PTM: The Cys-90/Cys-95 and Cys-393/Cys-396 disulfide bonds constitute the redox-active center. The Cys-90/Cys-95 disulfide bond may accept electron from P4HB and funnel them to the active site disulfide Cys-393/Cys-396 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Lumenal side {ECO:0000250}. Note=The association with ERP44 may be essential for its retention in the endoplasmic reticulum. {ECO:0000250}. SUBUNIT: Homodimer; disulfide-linked (By similarity). Heterodimer with ERO1A; disulfide-linked (By similarity). Also detected as monomer. Homodimers may be somewhat less active than monomers. The abundance of monomers and homodimers may be tissue-specific. Interacts with P4HB (By similarity). Interacts with ERP44 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Predominantly expressed in stomach and pancreas (mostly in the islets of Langerhans) (at protein level). {ECO:0000269|PubMed:16012172, ECO:0000269|PubMed:20308425}. +Q8CFZ4 GPC3_MOUSE Glypican-3 [Cleaved into: Glypican-3 alpha subunit; Glypican-3 beta subunit] 579 65,332 Chain (2); Disulfide bond (7); Glycosylation (5); Lipidation (1); Modified residue (2); Propeptide (1); Signal peptide (1) FUNCTION: Cell surface proteoglycan that bears heparan sulfate (By similarity). Negatively regulates the hedgehog signaling pathway when attached via the GPI-anchor to the cell surface by competing with the hedgehog receptor PTC1 for binding to hedgehog proteins (PubMed:18477453, PubMed:23665349). Binding to the hedgehog protein SHH triggers internalization of the complex by endocytosis and its subsequent lysosomal degradation (PubMed:18477453). Positively regulates the canonical Wnt signaling pathway by binding to the Wnt receptor Frizzled and stimulating the binding of the Frizzled receptor to Wnt ligands (By similarity). Positively regulates the non-canonical Wnt signaling pathway (PubMed:15537637). Binds to CD81 which decreases the availability of free CD81 for binding to the transcriptional repressor HHEX, resulting in nuclear translocation of HHEX and transcriptional repression (PubMed:23665349). Inhibits the dipeptidyl peptidase activity of DPP4 (By similarity). Plays a role in limb patterning and skeletal development by controlling the cellular response to BMP4 (PubMed:10964473). Modulates the effects of growth factors BMP2, BMP7 and FGF7 on renal branching morphogenesis (PubMed:11180950). Required for coronary vascular development (PubMed:19733558). Plays a role in regulating cell movements during gastrulation (By similarity). {ECO:0000250|UniProtKB:P51654, ECO:0000250|UniProtKB:Q6V9Y8, ECO:0000269|PubMed:10964473, ECO:0000269|PubMed:11180950, ECO:0000269|PubMed:15537637, ECO:0000269|PubMed:18477453, ECO:0000269|PubMed:19733558, ECO:0000269|PubMed:23665349}. PTM: O-glycosylated; contains heparan sulfate. {ECO:0000250|UniProtKB:P51654}.; PTM: Cleaved intracellularly by a furin-like convertase to generate 2 subunits, alpha and beta, which remain associated through disulfide bonds and are associated with the cell surface via the GPI-anchor. This processing is essential for its role in inhibition of hedgehog signaling. A second proteolytic event may result in cleavage of the protein on the cell surface, separating it from the GPI-anchor and leading to its shedding from the cell surface. {ECO:0000250|UniProtKB:P51654}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P13265}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P13265}; Extracellular side {ECO:0000250|UniProtKB:P13265}. SUBUNIT: Heterodimer; disulfide-linked (By similarity). Cleavage by a furin-like convertase results in production of alpha and beta chains which form a disulfide-linked heterodimer (By similarity). Interacts with DPP4 (By similarity). Interacts with FGF2 (By similarity). Interacts with WNT5A (By similarity). Also interacts with WNT3A and WNT7B (By similarity). Interacts with hedgehog protein SHH; the heparan sulfate chains are not required for the interaction (PubMed:18477453). Also interacts with hedgehog protein IHH (PubMed:23665349). Interacts with CD81 (PubMed:23665349). Interacts with Wnt receptors FZD4, FZD7 and FZD8; the heparan sulfate chains are required for the interaction (By similarity). {ECO:0000250|UniProtKB:P13265, ECO:0000250|UniProtKB:P51654, ECO:0000269|PubMed:18477453, ECO:0000269|PubMed:23665349}. TISSUE SPECIFICITY: In the developing limb, absent from the apical epidermal ridge at 11 dpc but highly expressed in the underlying mesenchyme (PubMed:10964473). Expression in the mesenchyme at this stage is asymmetric with highest levels in the regions of the distal mesenchyme within the progress zone and within the proximal anterior and posterior limb bud (PubMed:10964473). At later developmental stages including 12.5 and 13.5 dpc, expression is restricted to the interdigital webs and the regions of chondrocytic differentiation of the developing bones (PubMed:10964473). In the embryonic kidney, expressed in both the ureteric bud and mesenchymal cells as early as 13.5 dpc (PubMed:11180950). Expression at 16.5 dpc is similar to that at 13.5 dpc but decreases by 18.5 dpc (PubMed:11180950). {ECO:0000269|PubMed:10964473, ECO:0000269|PubMed:11180950}. +P51655 GPC4_MOUSE Glypican-4 (K-glypican) [Cleaved into: Secreted glypican-4] 557 62,586 Chain (2); Glycosylation (4); Lipidation (1); Modified residue (1); Propeptide (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Cell surface proteoglycan that bears heparan sulfate. May be involved in the development of kidney tubules and of the central nervous system. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor; Extracellular side.; SUBCELLULAR LOCATION: Secreted glypican-4: Secreted, extracellular space {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in developing brain and kidney. +Q8K3J9 GPC5C_MOUSE G-protein coupled receptor family C group 5 member C (Retinoic acid-induced gene 3 protein) (RAIG-3) 440 48,422 Chain (1); Glycosylation (1); Modified residue (6); Sequence conflict (1); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 50 70 Helical; Name=1. {ECO:0000255}.; TRANSMEM 85 105 Helical; Name=2. {ECO:0000255}.; TRANSMEM 120 140 Helical; Name=3. {ECO:0000255}.; TRANSMEM 156 176 Helical; Name=4. {ECO:0000255}.; TRANSMEM 208 228 Helical; Name=5. {ECO:0000255}.; TRANSMEM 241 261 Helical; Name=6. {ECO:0000255}.; TRANSMEM 279 299 Helical; Name=7. {ECO:0000255}. TOPO_DOM 23 49 Extracellular. {ECO:0000255}.; TOPO_DOM 71 84 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 106 119 Extracellular. {ECO:0000255}.; TOPO_DOM 141 155 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 177 207 Extracellular. {ECO:0000255}.; TOPO_DOM 229 240 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 262 278 Extracellular. {ECO:0000255}.; TOPO_DOM 300 440 Cytoplasmic. {ECO:0000255}. FUNCTION: This retinoic acid-inducible G-protein coupled receptor provide evidence for a possible interaction between retinoid and G-protein signaling pathways. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +P57759 ERP29_MOUSE Endoplasmic reticulum resident protein 29 (ERp29) 262 28,823 Chain (1); Modified residue (2); Motif (1); Signal peptide (1) FUNCTION: Does not seem to be a disulfide isomerase. Plays an important role in the processing of secretory proteins within the endoplasmic reticulum (ER), possibly by participating in the folding of proteins in the ER. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138}. Melanosome {ECO:0000250}. SUBUNIT: Homodimer. Part of a large chaperone multiprotein complex comprising CABP1, DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PPIB, SDF2L1, UGT1A1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX (By similarity). {ECO:0000250}. +Q8CAL5 GPC5_MOUSE Glypican-5 [Cleaved into: Secreted glypican-5] 572 63,792 Chain (2); Glycosylation (8); Propeptide (1); Signal peptide (1) FUNCTION: Cell surface proteoglycan that bears heparan sulfate. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}; Extracellular side {ECO:0000250}.; SUBCELLULAR LOCATION: Secreted glypican-5: Secreted, extracellular space {ECO:0000250}. +Q9D1Q6 ERP44_MOUSE Endoplasmic reticulum resident protein 44 (ER protein 44) (ERp44) (Thioredoxin domain-containing protein 4) 406 46,853 Chain (1); Disulfide bond (2); Domain (1); Erroneous initiation (1); Motif (1); Mutagenesis (1); Region (1); Signal peptide (1) FUNCTION: Mediates thiol-dependent retention in the early secretory pathway, forming mixed disulfides with substrate proteins through its conserved CRFS motif. Inhibits the calcium channel activity of ITPR1. May have a role in the control of oxidative protein folding in the endoplasmic reticulum. Required to retain ERO1A and ERO1B in the endoplasmic reticulum (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138, ECO:0000269|PubMed:15652484}. SUBUNIT: Forms mixed disulfides with both ERO1A and ERO1B and cargo folding intermediates (By similarity). Directly interacts with ITPR1 in a pH-, redox state- and calcium-dependent manner, but not with ITPR2 or ITPR3. The strength of this interaction inversely correlates with calcium concentration. {ECO:0000250, ECO:0000269|PubMed:15652484}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15652484}. +Q9R087 GPC6_MOUSE Glypican-6 [Cleaved into: Secreted glypican-6] 555 63,057 Chain (2); Lipidation (1); Propeptide (1); Signal peptide (1) FUNCTION: Cell surface proteoglycan that bears heparan sulfate. Putative cell surface coreceptor for growth factors, extracellular matrix proteins, proteases and anti-proteases. Enhances migration and invasion of cancer cells through WNT5A signaling (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}; Extracellular side {ECO:0000250}.; SUBCELLULAR LOCATION: Secreted glypican-6: Secreted, extracellular space {ECO:0000250}. TISSUE SPECIFICITY: In the cartilage growth-plate, gradient of expression with highest levels from the proliferative and pre-hypertrophic zones to lowest, if any, in the hypertrophic zones (at protein level). {ECO:0000269|PubMed:19481194}. +P83854 GPCR_MOUSE Putative G-protein coupled receptor (Fragment) 10 1,192 Chain (1); Non-terminal residue (1) SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q99JZ7 ERRFI_MOUSE ERBB receptor feedback inhibitor 1 (Mitogen-inducible gene 6 protein homolog) (MIG-6) 461 50,075 Chain (1); Initiator methionine (1); Modified residue (7); Region (1) FUNCTION: Negative regulator of EGFR signaling in skin morphogenesis. Acts as a negative regulator for several EGFR family members, including ERBB2, ERBB3 and ERBB4. Inhibits EGFR catalytic activity by interfering with its dimerization. Inhibits autophosphorylation of EGFR, ERBB2 and ERBB4. Important for normal keratinocyte proliferation and differentiation. Plays a role in modulating the response to steroid hormones in the uterus. Required for normal response to progesterone in the uterus and for fertility. Mediates epithelial estrogen responses in the uterus by regulating ESR1 levels and activation. Important for regulation of endometrium cell proliferation. Important for normal prenatal and perinatal lung development. {ECO:0000269|PubMed:16648858, ECO:0000269|PubMed:19439667, ECO:0000269|PubMed:19683494, ECO:0000269|PubMed:19710174, ECO:0000269|PubMed:20018910}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16648858}. Cell membrane {ECO:0000269|PubMed:16648858}; Peripheral membrane protein {ECO:0000269|PubMed:16648858}; Cytoplasmic side {ECO:0000269|PubMed:16648858}. Nucleus {ECO:0000305|PubMed:16648858}. Note=Associated with the plasma membrane of basal skin keratinocytes. Translocates into the nucleus of differentiating suprabasal keratinocytes. SUBUNIT: Interacts with EGFR (By similarity). Interacts with ERBB2. {ECO:0000250}. DOMAIN: The EGFR-binding region prevents binding of a cyclin-like activator to the EGFR kinase domain, and thereby keeps EGFR in an inactive conformation. Also maintains EGFR in an inactive conformation by preventing formation of an asymmetric homodimer (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Detected in lung, in airway epithelial cells and alveolar type 2 cells (at protein level). Detected in uterus stroma, luminal epithelium and glandular epithelium. {ECO:0000269|PubMed:16648858, ECO:0000269|PubMed:19710174}. +Q8R5F8 ES8L1_MOUSE Epidermal growth factor receptor kinase substrate 8-like protein 1 (EPS8-like protein 1) (Epidermal growth factor receptor pathway substrate 8-related protein 1) (EPS8-related protein 1) 716 80,028 Beta strand (8); Chain (1); Coiled coil (1); Compositional bias (2); Domain (1); Frameshift (1); Helix (3); Modified residue (2); Sequence conflict (2); Turn (2) FUNCTION: Stimulates guanine exchange activity of SOS1. May play a role in membrane ruffling and remodeling of the actin cytoskeleton (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with ABI1. Part of a complex that contains SOS1, ABI1 and EPS8L2. Associates with F-actin (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Detected in placenta, skin, mammary gland, bone marrow and stomach. {ECO:0000269|PubMed:14565974}. +Q99K30 ES8L2_MOUSE Epidermal growth factor receptor kinase substrate 8-like protein 2 (EPS8-like protein 2) (Epidermal growth factor receptor pathway substrate 8-related protein 2) (EPS8-related protein 2) 729 82,229 Alternative sequence (2); Chain (1); Domain (2); Modified residue (3); Sequence conflict (1) FUNCTION: Stimulates guanine exchange activity of SOS1. May play a role in membrane ruffling and remodeling of the actin cytoskeleton (By similarity). In the cochlea, is required for stereocilia maintenance in adult hair cells (PubMed:23918390). {ECO:0000250|UniProtKB:Q9H6S3, ECO:0000269|PubMed:23918390}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H6S3}. Cell projection, stereocilium {ECO:0000269|PubMed:23918390}. Note=Localizes at the tips of the stereocilia of the inner and outer hair cells. {ECO:0000269|PubMed:23918390}. SUBUNIT: Interacts with ABI1. Part of a complex that contains SOS1, ABI1 and EPS8L2. Associates with F-actin (By similarity). {ECO:0000250|UniProtKB:Q9H6S3}. TISSUE SPECIFICITY: Detected in fetal kidney, adrenal gland, salivary gland, stomach, gut, cartilage and skin. Detected in adult ovary, placenta, skin, adrenal gland, salivary gland, kidney, intestine and stomach. Expressed at the tips of cochlear hair cells stereocilia (PubMed:23918390). {ECO:0000269|PubMed:14565974, ECO:0000269|PubMed:23918390}. +Q925F2 ESAM_MOUSE Endothelial cell-selective adhesion molecule 394 41,810 Chain (1); Disulfide bond (1); Domain (2); Glycosylation (4); Modified residue (7); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 252 272 Helical. {ECO:0000255}. TOPO_DOM 30 251 Extracellular. {ECO:0000255}.; TOPO_DOM 273 394 Cytoplasmic. {ECO:0000255}. FUNCTION: Can mediate aggregation most likely through a homophilic molecular interaction. {ECO:0000269|PubMed:11279107, ECO:0000269|PubMed:11847224}. SUBCELLULAR LOCATION: Cell junction, adherens junction {ECO:0000305}. Cell junction, tight junction {ECO:0000305}. Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Interacts with BAIAP1. {ECO:0000269|PubMed:15383320}. TISSUE SPECIFICITY: Highly expressed in the heart and lung. Weakly expressed in the kidney and skin. Expression is restricted to the vascular endothelial cells. Expressed in the kidney, heart and tongue (at protein level). Also expressed on megakaryocytes and activated platelets. {ECO:0000269|PubMed:11279107, ECO:0000269|PubMed:11847224}. +Q8VDI1 ESIP1_MOUSE Epithelial-stromal interaction protein 1 314 36,098 Alternative sequence (2); Chain (1); Coiled coil (1); Modified residue (1); Sequence conflict (12) FUNCTION: Plays a role in M1 macrophage polarization and is required for the proper regulation of gene expression during M1 versus M2 macrophage differentiation (PubMed:29217193). Might play a role in RELA/p65 and STAT1 phosphorylation and nuclear localization upon activation of macrophages (PubMed:29217193). {ECO:0000269|PubMed:29217193}. TISSUE SPECIFICITY: Expressed in the spleen, with expression in T cells, B cells, natural killer cells and natural killer T cells and high expression in monocytes and macrophages. {ECO:0000269|PubMed:29217193}. +Q3UYR4 ESPNL_MOUSE Espin-like protein 1005 108,868 Chain (1); Coiled coil (1); Compositional bias (1); Repeat (10) FUNCTION: Binds to but does not cross-link actin. Required for the formation and maintenance of inner ear hair cell stereocilia and staircase formation. Essential for normal hearing. {ECO:0000269|PubMed:26926603}. SUBCELLULAR LOCATION: Cell projection, stereocilium {ECO:0000269|PubMed:26926603}. SUBUNIT: Interacts with MYO3A (via C-terminus). Interacts with MYO3B (via C-terminus). {ECO:0000269|PubMed:26926603}. TISSUE SPECIFICITY: Expressed in inner ear hair cells (PubMed:25582750). Expressed in utricle hair bundles (at protein level). Expressed in choclea (at protein level) (PubMed:26926603). {ECO:0000269|PubMed:25582750, ECO:0000269|PubMed:26926603}. +P60330 ESPL1_MOUSE Separin (EC 3.4.22.49) (Caspase-like protein ESPL1) (Extra spindle poles-like 1 protein) (Separase) 2118 233,035 Active site (1); Chain (1); Domain (1); Erroneous initiation (1); Modified residue (4); Site (2) FUNCTION: Caspase-like protease, which plays a central role in the chromosome segregation by cleaving the SCC1/RAD21 subunit of the cohesin complex at the onset of anaphase. During most of the cell cycle, it is inactivated by different mechanisms (By similarity). {ECO:0000250}. PTM: Autocleaves. This function, which is not essential for its protease activity, is unknown (By similarity). {ECO:0000250}.; PTM: Phosphorylated by CDK1. There is 8 Ser/Thr phosphorylation sites. Among them, only Ser-1121 phosphorylation is the major site, which conducts to the enzyme inactivation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Interacts with PTTG1. Interacts with RAD21 (By similarity). {ECO:0000250}. +P61406 EST1A_MOUSE Telomerase-binding protein EST1A (EC 3.1.-.-) (EST1-like protein A) (Ever shorter telomeres 1A) (Smg-6 homolog) (Telomerase subunit EST1A) 1418 160,496 Chain (1); Coiled coil (2); Domain (1); Metal binding (3); Modified residue (9); Region (2) FUNCTION: Component of the telomerase ribonucleoprotein (RNP) complex that is essential for the replication of chromosome termini. May have a general role in telomere regulation. Promotes in vitro the ability of TERT to elongate telomeres. Overexpression induces telomere uncapping, chromosomal end-to-end fusions (telomeric DNA persists at the fusion points) and did not perturb TRF2 telomeric localization. Binds to the single-stranded 5'-(GTGTGG)(4)GTGT-3' telomeric DNA, but not to a telomerase RNA template component (TER). {ECO:0000250|UniProtKB:Q86US8}.; FUNCTION: Plays a role in nonsense-mediated mRNA decay. Is thought to provide a link to the mRNA degradation machinery as it has endonuclease activity required to initiate NMD, and to serve as an adapter for UPF1 to protein phosphatase 2A (PP2A), thereby triggering UPF1 dephosphorylation. Degrades single-stranded RNA (ssRNA), but not ssDNA or dsRNA. {ECO:0000250|UniProtKB:Q86US8}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Chromosome, telomere {ECO:0000305}. Cytoplasm, cytosol {ECO:0000250}. Note=Particularly enriched in the nucleolus. {ECO:0000250}. SUBUNIT: May form homooligomers. Associated component of the telomerase holoenzyme complex. Interacts with TERT, independently of the telomerase RNA. Interacts with SMG1, SMG5, SMG7, UPF1, UPF2, UPF3B and the PP2A catalytic subunits. Also interacts with the exon junction complex (EJC) composed at least of CASC3, EIF4A3, MAGOH and RBM8A; required for the process of nonsense-mediated mRNA decay. {ECO:0000250|UniProtKB:Q86US8}. DOMAIN: The PINc domain confers endonuclease activity and is expected to bind the catalytic metal ion. {ECO:0000250}. +P23953 EST1C_MOUSE Carboxylesterase 1C (EC 3.1.1.1) (Liver carboxylesterase N) (Lung surfactant convertase) (PES-N) 554 61,056 Active site (3); Chain (1); Disulfide bond (2); Frameshift (1); Glycosylation (5); Modified residue (1); Motif (1); Sequence caution (1); Sequence conflict (25); Signal peptide (1) FUNCTION: Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. Involved in the extracellular metabolism of lung surfactant. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Note=Microsomal membrane, lumen of endoplasmic reticulum. TISSUE SPECIFICITY: Expressed in lung, kidney and liver. {ECO:0000269|PubMed:9815115}. +Q64176 EST1E_MOUSE Carboxylesterase 1E (EC 3.1.1.1) (Egasyn) (Liver carboxylesterase 22) (Es-22) (Esterase-22) 562 61,582 Active site (3); Chain (1); Disulfide bond (2); Glycosylation (3); Motif (1); Signal peptide (1) FUNCTION: Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Note=Microsomal membrane, lumen of endoplasmic reticulum. +Q8BK48 EST2E_MOUSE Pyrethroid hydrolase Ces2e (EC 3.1.1.88) (carboxylesterase 2E) 559 62,318 Active site (3); Chain (1); Disulfide bond (2); Glycosylation (1); Modified residue (1); Sequence conflict (3); Signal peptide (1) FUNCTION: Carboxylesterase that catalyzes the hydrolysis of pyrethroids pesticides. Hydrolyzes trans-permethrin at a rate about 22-fold higher than cis-permethrin. Also hydrolyzes trans-cypermethrin. {ECO:0000269|PubMed:15123619}. PTM: Glycosylated. {ECO:0000269|PubMed:15123619}. SUBCELLULAR LOCATION: Microsome {ECO:0000269|PubMed:15123619}. +Q3U7R1 ESYT1_MOUSE Extended synaptotagmin-1 (E-Syt1) (Membrane-bound C2 domain-containing protein) 1092 121,554 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (6); Metal binding (12); Modified residue (7); Mutagenesis (1); Region (1); Sequence conflict (3); Topological domain (3); Transmembrane (2) TRANSMEM 29 49 Helical. {ECO:0000255}.; TRANSMEM 53 73 Helical. {ECO:0000255}. TOPO_DOM 1 28 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 50 52 Lumenal. {ECO:0000255}.; TOPO_DOM 74 1092 Cytoplasmic. {ECO:0000255}. FUNCTION: Binds glycerophospholipids in a barrel-like domain and may play a role in cellular lipid transport (By similarity). Binds calcium (via the C2 domains) and translocates to sites of contact between the endoplasmic reticulum and the cell membrane in response to increased cytosolic calcium levels. Helps tether the endoplasmic reticulum to the cell membrane and promotes the formation of appositions between the endoplasmic reticulum and the cell membrane (By similarity). {ECO:0000250}. PTM: Phosphorylated on Ser residues in insulin-treated adipocytes (in vitro); this promotes interaction with SLC2A4. {ECO:0000269|PubMed:19255425}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Localizes primarily to the endoplasmic reticulum. Recruited to sites of contact between the endoplasmic reticulum and the cell membrane in response to increased cytosolic calcium levels (By similarity). {ECO:0000250}. SUBUNIT: Interacts with ESYT2 and ESYT3 (By similarity). Interacts (phosphorylated form) with SLC2A4. {ECO:0000250, ECO:0000269|PubMed:19255425}. DOMAIN: Anchored to the endoplasmic reticulum membrane by a transmembrane hairpin structure; both N-terminus and C-terminus are cytoplasmic. {ECO:0000250}.; DOMAIN: The C2 domains mediate lipid and calcium binding. The N-terminal C2 domain binds calcium ions and is important for calcium-dependent lipid binding and interaction with membranes. Two calcium ions are bound at a high-affinity site and a third calcium ion is bound with lower affinity. May bind up to four calcium ions. In contrast, the second C2 domain apparently does not bind calcium. The third C2 domain mediates interaction with membranes enriched in phosphatidylinositol 4,5-bisphosphate and is required for translocation to the cell membrane in response to increased cytosolic calcium levels (By similarity). {ECO:0000250}.; DOMAIN: The SMP-LTD domain is a barrel-like domain that binds glycerophospholipids in its interior (By similarity). {ECO:0000250|UniProtKB:A0FGR8}. +Q3TZZ7 ESYT2_MOUSE Extended synaptotagmin-2 (E-Syt2) 845 94,139 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (4); Metal binding (13); Modified residue (10); Region (1); Topological domain (3); Transmembrane (2) TRANSMEM 28 48 Helical. {ECO:0000255}.; TRANSMEM 52 72 Helical. {ECO:0000255}. TOPO_DOM 1 27 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 49 51 Lumenal. {ECO:0000255}.; TOPO_DOM 73 845 Cytoplasmic. {ECO:0000255}. FUNCTION: Tethers the endoplasmic reticulum to the cell membrane and promotes the formation of appositions between the endoplasmic reticulum and the cell membrane. Binds glycerophospholipids in a barrel-like domain and may play a role in cellular lipid transport. Plays a role in FGF signaling via its role in the rapid internalization of FGFR1 that has been activated by FGF1 binding; this occurs most likely via the AP-2 complex (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:A0FGR8}; Peripheral membrane protein {ECO:0000250|UniProtKB:A0FGR8}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:A0FGR8}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to endoplasmic reticulum-plasma membrane contact sites (EPCS). Recruited to the cell membrane via the third C2 domain (By similarity). {ECO:0000250|UniProtKB:A0FGR8}. SUBUNIT: Homodimer. Interacts with ESYT1 and ESYT3. Interacts with FGFR1 that has been activated by FGF1 binding. Interacts with the AP-2 complex; identified in a complex with the AP-2 complex and FGFR1 (By similarity). {ECO:0000250}. DOMAIN: Anchored to the endoplasmic reticulum membrane by a transmembrane hairpin structure; both N-terminus and C-terminus are cytoplasmic. {ECO:0000250}.; DOMAIN: The C2 domains mediate lipid and calcium binding. The N-terminal C2 domain binds calcium ions and is important for calcium-dependent lipid binding and interaction with membranes. Two calcium ions are bound at a high-affinity site and a third calcium ion is bound with lower affinity. May bind up to four calcium ions. In contrast, the second C2 domain apparently does not bind calcium. The third C2 domain mediates interaction with membranes enriched in phosphatidylinositol 4,5-bisphosphate and is required for location at the cell membrane (By similarity). {ECO:0000250}.; DOMAIN: The SMP-LTD domain is a barrel-like domain that binds glycerophospholipids in its interior; can bind two lipid molecules simultaneously. Binds a variety of lipids, including phosphatidylethanolamine, phosphatidylcholine and phosphatidylinositol (By similarity). {ECO:0000250|UniProtKB:A0FGR8}. +Q5DTI8 ESYT3_MOUSE Extended synaptotagmin-3 (E-Syt3) 891 100,068 Alternative sequence (1); Chain (1); Domain (4); Erroneous initiation (1); Frameshift (1); Metal binding (13); Region (1); Topological domain (3); Transmembrane (2) TRANSMEM 33 53 Helical. {ECO:0000255}.; TRANSMEM 55 75 Helical. {ECO:0000255}. TOPO_DOM 1 32 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 54 54 Lumenal. {ECO:0000255}.; TOPO_DOM 76 891 Cytoplasmic. {ECO:0000255}. FUNCTION: Tethers the endoplasmic reticulum to the cell membrane and promotes the formation of appositions between the endoplasmic reticulum and the cell membrane. Binds glycerophospholipids in a barrel-like domain and may play a role in cellular lipid transport (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:A0FGR9}; Peripheral membrane protein {ECO:0000250|UniProtKB:A0FGR9}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:A0FGR9}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to endoplasmic reticulum-plasma membrane contact sites (EPCS). Recruited to the cell membrane via the third C2 domain (By similarity). {ECO:0000250|UniProtKB:A0FGR9}. DOMAIN: The SMP-LTD domain is a barrel-like domain that binds glycerophospholipids in its interior (By similarity). {ECO:0000250|UniProtKB:A0FGR8}. +Q5SVT3 ETAA1_MOUSE Ewing's tumor-associated antigen 1 homolog 877 96,552 Alternative sequence (2); Chain (1); Coiled coil (2); Cross-link (4); Modified residue (1); Motif (3); Sequence conflict (5) FUNCTION: Replication stress response protein that accumulates at DNA damage sites and promotes replication fork progression and integrity. Recruited to stalled replication forks via interaction with the RPA complex and directly stimulates ATR kinase activity independently of TOPBP1. Probably only regulates a subset of ATR targets. {ECO:0000250|UniProtKB:Q9NY74}. PTM: Phosphorylated by ATR. {ECO:0000250|UniProtKB:Q9NY74}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NY74}. Note=Localizes at sites of DNA damage following replication stress. Recruited to stalled replication forks via interaction with RPA1 and RPA2 subunits of the RPA complex. {ECO:0000250|UniProtKB:Q9NY74}. SUBUNIT: Interacts (via RBM1 motif) with RPA1. Interacts (via RBM2 motif) with RPA2. Interacts (via the ATR-activation domain motif) with ATR. {ECO:0000250|UniProtKB:Q9NY74}. DOMAIN: The RBM1 (RPA1-binding, also named RPA70N-binding) motif mediates interaction with RPA1. The RBM2 (RPA2-binding, also named RPA32C-binding) motif mediates interaction with RPA2. {ECO:0000250|UniProtKB:Q9NY74}.; DOMAIN: The ATR-activation domain (AAD) motif is required to bind and activate ATR. {ECO:0000250|UniProtKB:Q9NY74}. +Q80SW5 ETD_MOUSE Embryonic testis differentiation protein 59 6,981 Chain (1) TISSUE SPECIFICITY: Specifically expressed in testis. {ECO:0000269|PubMed:12617826}. +Q99LC5 ETFA_MOUSE Electron transfer flavoprotein subunit alpha, mitochondrial (Alpha-ETF) 333 35,009 Binding site (3); Chain (1); Modified residue (24); Nucleotide binding (3); Region (2); Sequence conflict (5); Transit peptide (1) FUNCTION: Heterodimeric electron transfer flavoprotein that accepts electrons from several mitochondrial dehydrogenases, including acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase. It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase). Required for normal mitochondrial fatty acid oxidation and normal amino acid metabolism. {ECO:0000250|UniProtKB:P13804}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:P13804}. SUBUNIT: Heterodimer composed of ETFA and ETFB. Identified in a complex that contains ETFA, ETFB and ETFRF1. Interaction with ETFRF1 promotes dissociation of the bound FAD and loss of electron transfer activity. {ECO:0000250|UniProtKB:P13804}. DOMAIN: Domain I shares an identical polypeptide fold with the beta subunit ETFB though there is no sequence similarity. {ECO:0000250|UniProtKB:P13804}. +Q9DCW4 ETFB_MOUSE Electron transfer flavoprotein subunit beta (Beta-ETF) 255 27,623 Binding site (2); Chain (1); Initiator methionine (1); Modified residue (12); Nucleotide binding (2); Region (1); Sequence conflict (1) FUNCTION: Heterodimeric electron transfer flavoprotein that accepts electrons from several mitochondrial dehydrogenases, including acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase. It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (By similarity). Required for normal mitochondrial fatty acid oxidation and normal amino acid metabolism (PubMed:25023281). ETFB binds an AMP molecule that probably has a purely structural role (By similarity). {ECO:0000250|UniProtKB:P38117, ECO:0000269|PubMed:25023281}. PTM: Methylated (PubMed:25023281). Trimethylation at Lys-200 and Lys-203 may negatively regulate the activity in electron transfer from acyl-CoA dehydrogenases. {ECO:0000250|UniProtKB:P38117, ECO:0000269|PubMed:25023281}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:P38117}. SUBUNIT: Heterodimer composed of ETFA and ETFB. Identified in a complex that contains ETFA, ETFB and ETFRF1. Interacts with ACADM. {ECO:0000250|UniProtKB:P38117}. DOMAIN: The recognition loop recognizes a hydrophobic patch at the surface of interacting dehydrogenases and acts as a static anchor at the interface. {ECO:0000250|UniProtKB:P38117}. +P27577 ETS1_MOUSE Protein C-ets-1 (p54) 440 50,202 Beta strand (6); Chain (1); Cross-link (5); DNA binding (1); Domain (1); Helix (14); Modified residue (12); Region (1); Sequence conflict (19); Turn (5) FUNCTION: Transcription factor. Directly controls the expression of cytokine and chemokine genes in a wide variety of different cellular contexts. May control the differentiation, survival and proliferation of lymphoid cells. May also regulate angiogenesis through regulation of expression of genes controlling endothelial cell migration and invasion (By similarity). {ECO:0000250}. PTM: Sumoylated on Lys-15 and Lys-227, preferentially with SUMO2; which inhibits transcriptional activity. {ECO:0000269|PubMed:16862185}.; PTM: Ubiquitinated; which induces proteasomal degradation. {ECO:0000269|PubMed:16862185}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P14921}. Nucleus {ECO:0000250|UniProtKB:P14921}. Note=Delocalizes from nucleus to cytoplasm when coexpressed with isoform Ets-1 p27. {ECO:0000250|UniProtKB:P14921}. SUBUNIT: Binds DNA as a homodimer; homodimerization is required for transcription activation. Interacts with DAXX (By similarity). Interacts with UBE2I (By similarity). Interacts with SP100; the interaction is direct and modulates ETS1 transcriptional activity (By similarity). Interacts with MAF and MAFB. Interacts with PAX5; the interaction alters DNA-binding properties. {ECO:0000250, ECO:0000269|PubMed:10790365, ECO:0000269|PubMed:11779502, ECO:0000269|PubMed:9566892}. +P41164 ETV1_MOUSE ETS translocation variant 1 (Ets-related protein 81) 477 55,041 Chain (1); Cross-link (1); DNA binding (1); Modified residue (3) FUNCTION: Transcriptional activator that binds to DNA sequences containing the consensus pentanucleotide 5'-CGGA[AT]-3'. PTM: Sumoylated. {ECO:0000250}.; PTM: Phosphorylated at Ser-191 and Ser-216 by RPS6KA1 and RPS6KA5; phosphorylation activates transcriptional activity. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. TISSUE SPECIFICITY: Abundant in kidney. Moderate levels seen in the heart, brain, lung, embryo and lower levels seen in spleen, intestine, testis and thymus. +P41163 ETV2_MOUSE ETS translocation variant 2 (Ets-related protein 71) 335 37,083 Chain (1); DNA binding (1); Sequence conflict (1) FUNCTION: Binds to DNA sequences containing the consensus pentanucleotide 5'-CGGA[AT]-3'. SUBCELLULAR LOCATION: Nucleus. TISSUE SPECIFICITY: Testis. +Q8R4Z4 ETV3_MOUSE ETS translocation variant 3 (ETS domain transcriptional repressor PE1) (PE-1) (Mitogenic Ets transcriptional suppressor) 513 57,026 Chain (1); Cross-link (2); DNA binding (1); Modified residue (4); Sequence conflict (10) FUNCTION: Transcriptional repressor that contribute to growth arrest during terminal macrophage differentiation by repressing target genes involved in Ras-dependent proliferation. Represses MMP1 promoter activity. {ECO:0000269|PubMed:10913304, ECO:0000269|PubMed:12007404}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00237}. +P28322 ETV4_MOUSE ETS translocation variant 4 (Polyomavirus enhancer activator 3) (Protein PEA3) 485 54,008 Alternative sequence (3); Chain (1); Compositional bias (2); Cross-link (6); DNA binding (1); Modified residue (4); Sequence conflict (1) FUNCTION: Transcriptional activator that binds to the enhancer of the adenovirus E1A gene; the core-binding sequence is 5'[AC]GGA[AT]GT-3'. May play a regulatory role during embryogenesis. PTM: Phosphorylated.; PTM: Sumoylated; enhanced upon ERK/MAP kinase pathway activation it positively regulates the transcriptional activator capacity. Sumoylation at Lys-95 probably requires phosphorylation at Ser-100. Transiently polysumoylated and desumoylated by SENP1. Sumoylation is a prerequisite to polyubiquitination which in turn increases proteasomal-mediated degradation. Probably polyubiquitinated by RNF4 and deubiquitinated by USP2 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. TISSUE SPECIFICITY: Epididymis and brain. +Q9D7G4 EURL_MOUSE Protein EURL homolog 290 32,883 Chain (1); Coiled coil (1) FUNCTION: Plays a role in cortical progenitor cell proliferation and differentiation (PubMed:27404227). Promotes dendritic spine development of post-migratory cortical projection neurons by modulating the beta-catenin signaling pathway (PubMed:27404227). {ECO:0000269|PubMed:27404227}. SUBUNIT: Interacts with CCDC85B (PubMed:27404227). {ECO:0000269|PubMed:27404227}. TISSUE SPECIFICITY: Expressed in brain (at protein level) (PubMed:27404227). Expressed in neural progenitor cells and postmitotic neurons of the embryonic cerebral cortex (PubMed:27404227). {ECO:0000269|PubMed:27404227}. +Q9D9S1 EVG1_MOUSE UPF0193 protein EVG1 homolog 216 24,737 Chain (1) +Q91WM6 EVA1A_MOUSE Protein eva-1 homolog A (Protein FAM176A) (Transmembrane protein 166) 156 17,810 Chain (1); Modified residue (2); Sequence conflict (3); Transmembrane (1) TRANSMEM 40 60 Helical. {ECO:0000255}. FUNCTION: Acts as a regulator of programmed cell death, mediating both autophagy and apoptosis. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Lysosome membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. +P20934 EVI2A_MOUSE Protein EVI2A (Ecotropic viral integration site 2A protein) (EVI-2A) 223 24,087 Chain (1); Glycosylation (4); Modified residue (2); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 126 151 Helical. {ECO:0000255}. TOPO_DOM 20 125 Extracellular. {ECO:0000255}.; TOPO_DOM 152 223 Cytoplasmic. {ECO:0000255}. FUNCTION: May complex with itself or/and other proteins within the membrane, to function as part of a cell-surface receptor. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. DISEASE: Note=Expression of this gene is altered by viral integration and this altered expression may predispose cells to myeloid disease (PubMed:2167436). {ECO:0000269|PubMed:2167436}. +Q8VD58 EVI2B_MOUSE Protein EVI2B (Ecotropic viral integration site 2B protein) (EVI-2B) (CD antigen CD361) 444 47,993 Chain (1); Compositional bias (1); Glycosylation (4); Modified residue (5); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 204 224 Helical. {ECO:0000255}. TOPO_DOM 24 203 Extracellular. {ECO:0000255}.; TOPO_DOM 225 444 Cytoplasmic. {ECO:0000255}. FUNCTION: Required for granulocyte differentiation and functionality of hematopoietic progenitor cells through the control of cell cycle progression and survival of hematopoietic progenitor cells. {ECO:0000269|PubMed:28186500}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Expressed in myeloid and lymphoid progenitors and increased in mature hematopoietic populations with the highest levels in granulocytes. {ECO:0000269|PubMed:28186500}. +P97366 EVI5_MOUSE Ecotropic viral integration site 5 protein (EVI-5) 809 92,943 Chain (1); Coiled coil (1); Compositional bias (1); Domain (1); Modified residue (6); Region (4); Sequence conflict (1) FUNCTION: Functions as a regulator of cell cycle progression by stabilizing the FBXO5 protein and promoting cyclin-A accumulation during interphase. May play a role in cytokinesis (By similarity). {ECO:0000250}. PTM: Probably phosphorylated by PLK1; may be required for degradation during mitosis. {ECO:0000250}.; PTM: Ubiquitinated. Degradation during prophase is ubiquitin-dependent (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Associates with the mitotic spindle through anaphase and remains within the midzone and midbody until completion of cytokinesis. {ECO:0000250}. SUBUNIT: Dimeric and monomeric. Interacts with alpha- and gamma-tubulin. Interacts with FBXO5. Interacts with the chromosome passenger complex (CPC) which is at least composed of AURKB/aurora-B, BIRC5/survivin, CDCA8/borealin and INCENP (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9070650}. +P49749 EVX2_MOUSE Homeobox even-skipped homolog protein 2 (EVX-2) 475 47,902 Chain (1); Compositional bias (8); DNA binding (1) SUBCELLULAR LOCATION: Nucleus. +O08689 GDF8_MOUSE Growth/differentiation factor 8 (GDF-8) (Myostatin) 376 42,921 Beta strand (8); Chain (1); Disulfide bond (5); Glycosylation (1); Helix (2); Mutagenesis (2); Propeptide (1); Signal peptide (1); Site (1); Turn (1) FUNCTION: Acts specifically as a negative regulator of skeletal muscle growth. {ECO:0000269|PubMed:14671324, ECO:0000269|PubMed:24076600, ECO:0000269|PubMed:9139826}. PTM: Synthesized as large precursor molecule that undergoes proteolytic cleavage to generate an N-terminal propeptide and a disulfide linked C-terminal dimer, which is the biologically active molecule. The circulating form consists of a latent complex of the C-terminal dimer and other proteins, including its propeptide, which maintain the C-terminal dimer in a latent, inactive state. Ligand activation requires additional cleavage of the prodomain by a tolloid-like metalloproteinase (PubMed:14671324). {ECO:0000269|PubMed:14671324}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14671324}. SUBUNIT: Homodimer; disulfide-linked (PubMed:19644449). Interacts with WFIKKN2, leading to inhibit its activity (PubMed:12595574). Interacts with FSTL3 (PubMed:22052913). {ECO:0000269|PubMed:12595574, ECO:0000269|PubMed:19644449, ECO:0000269|PubMed:22052913}. TISSUE SPECIFICITY: Expressed specifically in developing and adult skeletal muscle. Weak expression in adipose tissue. {ECO:0000269|PubMed:9139826}. +Q07105 GDF9_MOUSE Growth/differentiation factor 9 (GDF-9) 441 49,649 Chain (1); Disulfide bond (3); Glycosylation (4); Propeptide (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Required for ovarian folliculogenesis. PTM: Phosphorylated; phosphorylation is critical for GDF9 function. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Homodimer or heterodimer (Potential). But, in contrast to other members of this family, cannot be disulfide-linked. {ECO:0000305}. TISSUE SPECIFICITY: Ovary. +Q91WK2 EIF3H_MOUSE Eukaryotic translation initiation factor 3 subunit H (eIF3h) (Eukaryotic translation initiation factor 3 subunit 3) (eIF-3-gamma) (eIF3 p40 subunit) 352 39,832 Chain (1); Cross-link (1); Domain (1); Modified residue (3) FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression. {ECO:0000255|HAMAP-Rule:MF_03007, ECO:0000269|PubMed:17581632}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03007}. SUBUNIT: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B, EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and EIF3M. The eIF-3 complex appears to include 3 stable modules: module A is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D, EIF3E, EIF3K and EIF3L. EIF3C of module C binds EIF3B of module A and EIF3H of module B, thereby linking the three modules. EIF3J is a labile subunit that binds to the eIF-3 complex via EIF3B. The eIF-3 complex may interact with RPS6KB1 under conditions of nutrient depletion. Mitogenic stimulation may lead to binding and activation of a complex composed of MTOR and RPTOR, leading to phosphorylation and release of RPS6KB1 and binding of EIF4B to eIF-3. Interacts with RNF139; the interaction leads to protein translation inhibitions in a ubiquitination-dependent manner (By similarity). Interacts with DHX33; the interaction is independent of RNA (PubMed:26100019). {ECO:0000255|HAMAP-Rule:MF_03007, ECO:0000269|PubMed:17581632, ECO:0000269|PubMed:26100019}. +Q8BJW6 EIF2A_MOUSE Eukaryotic translation initiation factor 2A (eIF-2A) [Cleaved into: Eukaryotic translation initiation factor 2A, N-terminally processed] 581 64,403 Alternative sequence (2); Chain (2); Coiled coil (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (6); Repeat (3) FUNCTION: Functions in the early steps of protein synthesis of a small number of specific mRNAs. Acts by directing the binding of methionyl-tRNAi to 40S ribosomal subunits. In contrast to the eIF-2 complex, it binds methionyl-tRNAi to 40S subunits in a codon-dependent manner, whereas the eIF-2 complex binds methionyl-tRNAi to 40S subunits in a GTP-dependent manner. {ECO:0000250|UniProtKB:Q9BY44}. +Q9QZD9 EIF3I_MOUSE Eukaryotic translation initiation factor 3 subunit I (eIF3i) (Eukaryotic translation initiation factor 3 subunit 2) (TGF-beta receptor-interacting protein 1) (TRIP-1) (eIF-3-beta) (eIF3 p36) 325 36,461 Chain (1); Cross-link (1); Modified residue (3); Repeat (5) FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression. {ECO:0000255|HAMAP-Rule:MF_03008, ECO:0000269|PubMed:17581632}. PTM: Phosphorylated by TGF-beta type II receptor. {ECO:0000255|HAMAP-Rule:MF_03008}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03008}. SUBUNIT: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B, EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and EIF3M. The eIF-3 complex appears to include 3 stable modules: module A is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D, EIF3E, EIF3K and EIF3L. EIF3C of module C binds EIF3B of module A and EIF3H of module B, thereby linking the three modules. EIF3J is a labile subunit that binds to the eIF-3 complex via EIF3B. The eIF-3 complex may interact with RPS6KB1 under conditions of nutrient depletion. Mitogenic stimulation may lead to binding and activation of a complex composed of MTOR and RPTOR, leading to phosphorylation and release of RPS6KB1 and binding of EIF4B to eIF-3. {ECO:0000255|HAMAP-Rule:MF_03008, ECO:0000269|PubMed:16541103, ECO:0000269|PubMed:17581632}. +Q3UGC7 EI3JA_MOUSE Eukaryotic translation initiation factor 3 subunit J-A (eIF3j-A) (Eukaryotic translation initiation factor 3 subunit 1-A) (eIF-3-alpha-A) (eIF3 p35) 261 29,344 Chain (1); Coiled coil (1); Cross-link (1); Modified residue (6); Region (2) FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression. This subunit binds directly within the mRNA entry channel of the 40S ribosome to the aminoacyl (A) site. It may regulate the interaction between the 43S PIC and mRNA. {ECO:0000255|HAMAP-Rule:MF_03009}. PTM: Phosphorylated. Phosphorylation is enhanced upon serum stimulation. {ECO:0000250|UniProtKB:O75822, ECO:0000255|HAMAP-Rule:MF_03009}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O75822, ECO:0000255|HAMAP-Rule:MF_03009}. SUBUNIT: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B, EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and EIF3M. The eIF-3 complex appears to include 3 stable modules: module A is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D, EIF3E, EIF3K and EIF3L. EIF3C of module C binds EIF3B of module A and EIF3H of module B, thereby linking the three modules. EIF3J is a labile subunit that binds to the eIF-3 complex via EIF3B. The eIF-3 complex interacts with RPS6KB1 under conditions of nutrient depletion. Mitogenic stimulation leads to binding and activation of a complex composed of MTOR and RPTOR, leading to phosphorylation and release of RPS6KB1 and binding of EIF4B to eIF-3. {ECO:0000250|UniProtKB:O75822, ECO:0000255|HAMAP-Rule:MF_03009}. +Q9DCR4 EID1_MOUSE EP300-interacting inhibitor of differentiation 1 (CREBBP/EP300 inhibitory protein 1) (E1A-like inhibitor of differentiation 1) (EID-1) 169 18,921 Alternative sequence (1); Chain (1); Helix (2); Motif (1); Region (1); Sequence conflict (4) FUNCTION: Interacts with RB1 and EP300 and acts as a repressor of MYOD1 transactivation. Inhibits EP300 and CBP histone acetyltransferase activity. May be involved in coupling cell cycle exit to the transcriptional activation of genes required for cellular differentiation. May act as a candidate coinhibitory factor for NR0B2 that can be directly linked to transcription inhibitory mechanisms. {ECO:0000269|PubMed:11964378}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11964378}. Cytoplasm {ECO:0000269|PubMed:11964378}. Note=May shuttle between nucleus and cytoplasm. {ECO:0000269|PubMed:11964378}. SUBUNIT: Interacts via its LXCXE motif with the entire pocket region of RB1. Interacts with EP300, NR0B2 and TRIM27. {ECO:0000250|UniProtKB:Q9Y6B2, ECO:0000269|PubMed:11964378}. TISSUE SPECIFICITY: Expressed in all adult tissues examined and during embryogenesis. {ECO:0000269|PubMed:11964378}. +P97481 EPAS1_MOUSE Endothelial PAS domain-containing protein 1 (EPAS-1) (HIF-1-alpha-like factor) (HLF) (mHLF) (HIF-related factor) (HRF) (Hypoxia-inducible factor 2-alpha) (HIF-2-alpha) (HIF2-alpha) 874 96,712 Beta strand (12); Chain (1); Compositional bias (1); Domain (4); Helix (14); Modified residue (4); Mutagenesis (11); Region (4); Sequence conflict (15); Turn (1) FUNCTION: Transcription factor involved in the induction of oxygen regulated genes. Heterodimerizes with ARNT; heterodimer binds to core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters (PubMed:26245371). Regulates the vascular endothelial growth factor (VEGF) expression and seems to be implicated in the development of blood vessels and the tubular system of lung. May also play a role in the formation of the endothelium that gives rise to the blood brain barrier. Potent activator of the Tie-2 tyrosine kinase expression. Activation requires recruitment of transcriptional coactivators such as CREBBP and probably EP300. Interaction with redox regulatory protein APEX seems to activate CTAD (By similarity). {ECO:0000250, ECO:0000269|PubMed:26245371}. PTM: In normoxia, is probably hydroxylated on Pro-405 and Pro-530 by EGLN1/PHD1, EGLN2/PHD2 and/or EGLN3/PHD3. The hydroxylated prolines promote interaction with VHL, initiating rapid ubiquitination and subsequent proteasomal degradation. Under hypoxia, proline hydroxylation is impaired and ubiquitination is attenuated, resulting in stabilization (By similarity). {ECO:0000250}.; PTM: In normoxia, is hydroxylated on Asn-851 by HIF1AN thus probably abrogating interaction with CREBBP and EP300 and preventing transcriptional activation. {ECO:0000269|PubMed:11823643}.; PTM: Phosphorylated on multiple sites in the CTAD. {ECO:0000269|PubMed:11983697}.; PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of asparagine is (S) stereospecific within HIF CTAD domains. {ECO:0000269|PubMed:11823643}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:21546903}. Nucleus speckle {ECO:0000269|PubMed:21546903}. Note=Colocalizes with HIF3A isoform 2 in the nucleus and speckles. {ECO:0000269|PubMed:21546903}. SUBUNIT: Interacts with HIF3A isoform 2 (PubMed:21546903). Efficient DNA binding requires dimerization with another bHLH protein. Heterodimerizes with ARNT; heterodimer binds to core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters (PubMed:26245371). Interacts with CREBBP (PubMed:11983697). Interacts with EGLN1. Interacts with VHL (By similarity). {ECO:0000250|UniProtKB:Q99814, ECO:0000269|PubMed:11983697, ECO:0000269|PubMed:21546903, ECO:0000269|PubMed:26245371}. TISSUE SPECIFICITY: Expressed in most tissues, with highest levels in lung, followed by heart, kidney, brain and liver. Predominantly expressed in endothelial cells. Also found in smooth muscle cells of the uterus, neurons, and brown adipose tissue. High expression in embryonic choroid plexus and kidney glomeruli. +Q9EQH2 ERAP1_MOUSE Endoplasmic reticulum aminopeptidase 1 (EC 3.4.11.-) (ARTS-1) (Adipocyte-derived leucine aminopeptidase) (A-LAP) (Aminopeptidase PILS) (Puromycin-insensitive leucyl-specific aminopeptidase) (PILS-AP) (VEGF-induced aminopeptidase) 930 106,599 Active site (1); Binding site (1); Chain (1); Disulfide bond (2); Glycosylation (6); Metal binding (3); Region (1); Sequence conflict (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 3 23 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 2 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 24 930 Lumenal. {ECO:0000255}. FUNCTION: Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I-binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Strongly prefers substrates 9-16 residues long. Rapidly degrades 13-mer to a 9-mer and then stops. Preferentially hydrolyzes the residue Leu and peptides with a hydrophobic C-terminus, while it has weak activity toward peptides with charged C-terminus. May play a role in the inactivation of peptide hormones. May be involved in the regulation of blood pressure through the inactivation of angiotensin II and/or the generation of bradykinin in the kidney (By similarity). {ECO:0000250}. PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. SUBUNIT: Monomer. May also exist as a heterodimer; with ERAP2. Interacts with RBMX (By similarity). {ECO:0000250}. +Q3U6B2 GP183_MOUSE G-protein coupled receptor 183 (Epstein-Barr virus-induced G-protein coupled receptor 2 homolog) (EBI2) (EBV-induced G-protein coupled receptor 2 homolog) 357 40,185 Binding site (4); Chain (1); Disulfide bond (1); Glycosylation (1); Modified residue (2); Region (1); Sequence conflict (3); Topological domain (8); Transmembrane (7) TRANSMEM 28 53 Helical; Name=1. {ECO:0000255}.; TRANSMEM 74 91 Helical; Name=2. {ECO:0000255}.; TRANSMEM 102 123 Helical; Name=3. {ECO:0000255}.; TRANSMEM 146 164 Helical; Name=4. {ECO:0000255}.; TRANSMEM 189 211 Helical; Name=5. {ECO:0000255}.; TRANSMEM 238 261 Helical; Name=6. {ECO:0000255}.; TRANSMEM 284 308 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 27 Extracellular. {ECO:0000255}.; TOPO_DOM 54 73 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 92 101 Extracellular. {ECO:0000255}.; TOPO_DOM 124 145 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 165 188 Extracellular. {ECO:0000255}.; TOPO_DOM 212 237 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 262 283 Extracellular. {ECO:0000255}.; TOPO_DOM 309 357 Cytoplasmic. {ECO:0000255}. FUNCTION: G-protein coupled receptor expressed in lymphocytes that acts as a chemotactic receptor for B-cells, T-cells, splenic dendritic cells, monocytes/macrophages and astrocytes (PubMed:19597478, PubMed:19615922, PubMed:21844396, PubMed:21796211, PubMed:21796212, PubMed:27147029). Receptor for oxysterol 7-alpha,25-dihydroxycholesterol (7-alpha,25-OHC) and other related oxysterols (PubMed:21796211, PubMed:21796212). Mediates cell positioning and movement of a number of cells by binding the 7-alpha,25-OHC ligand that forms a chemotactic gradient (PubMed:21796211, PubMed:21796212, PubMed:27147029). Binding of 7-alpha,25-OHC mediates the correct localization of B-cells during humoral immune responses (PubMed:21796211, PubMed:21796212). Collaborates with CXCR5 to mediate B-cell migration; probably by forming a heterodimer with CXCR5 that affects the interaction between of CXCL13 and CXCR5 (PubMed:21948984, PubMed:22913878). Guides B-cell movement along the B-cell zone-T-cell zone boundary and later to interfollicular and outer follicular regions (PubMed:19615922, PubMed:19597478, PubMed:21844396). Its specific expression during B-cell maturation helps position B-cells appropriately for mounting T-dependent antibody responses (PubMed:19615922). Also acts as a chemotactic receptor for some T-cells upon binding to 7-alpha,25-OHC ligand (PubMed:27147029). Promotes follicular helper T (Tfh) cells differentiation by positioning activated T-cells at the follicle-T-zone interface, promoting contact of newly activated CD4 T-cells with activated dendritic cells and exposing them to Tfh-cell-promoting inducible costimulator (ICOS) ligand (PubMed:27147029). Expression in splenic dendritic cells is required for their homeostasis, localization and ability to induce B- and T-cell responses: GPR183 acts as a chemotactic receptor in dendritic cells that mediates the accumulation of CD4(+) dendritic cells in bridging channels (PubMed:23682316, PubMed:23502855). Regulates migration of astrocytes and is involved in communication between astrocytes and macrophages (PubMed:25297897, PubMed:27166278). Promotes osteoclast precursor migration to bone surfaces (PubMed:26438360). Signals constitutively through G(i)-alpha, but not G(s)-alpha or G(q)-alpha (By similarity). Signals constitutively also via MAPK1/3 (ERK1/2) (By similarity). {ECO:0000250|UniProtKB:P32249, ECO:0000269|PubMed:19597478, ECO:0000269|PubMed:19615922, ECO:0000269|PubMed:21796211, ECO:0000269|PubMed:21796212, ECO:0000269|PubMed:21844396, ECO:0000269|PubMed:21948984, ECO:0000269|PubMed:22913878, ECO:0000269|PubMed:23502855, ECO:0000269|PubMed:23682316, ECO:0000269|PubMed:25297897, ECO:0000269|PubMed:26438360, ECO:0000269|PubMed:27147029, ECO:0000269|PubMed:27166278}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P32249}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Homodimer and heterodimer. Heterodimerizes with CXCR5; leading to modulate the interaction between of CXCL13 and CXCR5. {ECO:0000250|UniProtKB:P32249}. TISSUE SPECIFICITY: Expressed in mature B-cells and increases in expression early after activation, before being down-regulated in germinal center B-cells (PubMed:19597478). Expressed in astrocytes (PubMed:25297897). Specifically expressed in CD4(+) dendritic cells but not in CD8(+) dendritic cells (PubMed:23682316, PubMed:23502855). Expressed in monocyte/osteoclasts precursors and mature osteoclasts (PubMed:26438360). {ECO:0000269|PubMed:19597478, ECO:0000269|PubMed:23502855, ECO:0000269|PubMed:23682316, ECO:0000269|PubMed:25297897, ECO:0000269|PubMed:26438360}. +O08644 EPHB6_MOUSE Ephrin type-B receptor 6 (MEP) (Tyrosine-protein kinase-defective receptor EPH-6) 1014 110,107 Alternative sequence (4); Chain (1); Compositional bias (3); Domain (5); Glycosylation (1); Motif (1); Nucleotide binding (1); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 592 612 Helical. {ECO:0000255}. TOPO_DOM 33 591 Extracellular. {ECO:0000255}.; TOPO_DOM 613 1014 Cytoplasmic. {ECO:0000255}. FUNCTION: Kinase-defective receptor for members of the ephrin-B family. Binds to ephrin-B1 and ephrin-B2. Modulates cell adhesion and migration by exerting both positive and negative effects upon stimulation with ephrin-B2. Inhibits JNK activation, T-cell receptor-induced IL-2 secretion and CD25 expression upon stimulation with ephrin-B2 (By similarity). {ECO:0000250}. PTM: Ligand-binding increases phosphorylation on tyrosine residues. Phosphorylation on tyrosine residues is mediated by transphosphorylation by the catalytically active EPHB1 in a ligand-independent manner. Tyrosine phosphorylation of the receptor may act as a switch on the functional transition from cell adhesion/attraction to de-adhesion/repulsion (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Isoform 2: Secreted.; SUBCELLULAR LOCATION: Isoform 3: Secreted. SUBUNIT: Interacts with CBL and EPHB1. Interacts with FYN; this interaction takes place in a ligand-independent manner (By similarity). {ECO:0000250}. DOMAIN: The protein kinase domain is predicted to be catalytically inactive. Its extracellular domain is capable of promoting cell adhesion and migration in response to low concentrations of ephrin-B2, but its cytoplasmic domain is essential for cell repulsion and inhibition of migration induced by high concentrations of ephrin-B2 (By similarity). {ECO:0000255|PROSITE-ProRule:PRU00159}. TISSUE SPECIFICITY: High level in thymus, and brain. Very low levels of expression in kidney, lung, liver, bone marrow, skeletal muscle, spleen from 2 week old and adult mice, heart, testes and embryonic stem cells. {ECO:0000269|PubMed:8761299}. +P29319 EPHA3_MOUSE Ephrin type-A receptor 3 (EC 2.7.10.1) (EPH-like kinase 4) (EK4) (mEK4) (Tyrosine-protein kinase TYRO4) (Tyrosine-protein kinase receptor ETK1) 983 109,955 Active site (1); Alternative sequence (2); Binding site (1); Chain (1); Compositional bias (1); Domain (5); Glycosylation (5); Modified residue (5); Motif (1); Nucleotide binding (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 541 564 Helical. {ECO:0000255}. TOPO_DOM 21 540 Extracellular. {ECO:0000255}.; TOPO_DOM 565 983 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor tyrosine kinase which binds promiscuously membrane-bound ephrin family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Highly promiscuous for ephrin-A ligands it binds preferentially EFNA5. Upon activation by EFNA5 regulates cell-cell adhesion, cytoskeletal organization and cell migration. Plays a role in cardiac cells migration and differentiation and regulates the formation of the atrioventricular canal and septum during development probably through activation by EFNA1. Involved in the retinotectal mapping of neurons. May also control the segregation but not the guidance of motor and sensory axons during neuromuscular circuit development. {ECO:0000269|PubMed:17046737, ECO:0000269|PubMed:18403711, ECO:0000269|PubMed:19505147}. PTM: Autophosphorylates upon activation by EFNA5. Phosphorylation on Tyr-602 mediates interaction with NCK1. Dephosphorylated by PTPN1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Isoform Long: Cell membrane {ECO:0000250|UniProtKB:P29320}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: Isoform Short: Secreted {ECO:0000250|UniProtKB:P29320}. SUBUNIT: Heterotetramer upon binding of the ligand. The heterotetramer is composed of an ephrin dimer and a receptor dimer. Oligomerization is probably required to induce biological responses. Forms a ternary EFNA5-EPHA3-ADAM10 complex mediating EFNA5 extracellular domain shedding by ADAM10 which regulates the EFNA5-EPHA3 complex internalization and function. Interacts (phosphorylated) with PTPN1; dephosphorylates EPHA3 and may regulate its trafficking and function (By similarity). Interacts (phosphorylated) with CRK; mediates EFNA5-EPHA3 signaling through RHOA GTPase activation. Interacts with NCK1 (via SH2 domain); mediates EFNA5-EPHA3 signaling. {ECO:0000250, ECO:0000269|PubMed:11870224, ECO:0000269|PubMed:19505147}. TISSUE SPECIFICITY: Greatest levels of expression occurring in the brain, also detected in testis. Expressed in myogenic progenitor cells (PubMed:27446912). {ECO:0000269|PubMed:27446912}. +Q99M71 EPDR1_MOUSE Mammalian ependymin-related protein 1 (MERP-1) 224 25,485 Alternative sequence (1); Chain (1); Glycosylation (2); Sequence conflict (2); Signal peptide (1) SUBCELLULAR LOCATION: Secreted. +Q9DA01 EPPI_MOUSE Eppin (Epididymal protease inhibitor) (Serine protease inhibitor-like with Kunitz and WAP domains 1) 134 15,470 Chain (1); Disulfide bond (7); Domain (2); Region (2); Signal peptide (1) FUNCTION: Serine protease inhibitor that plays an essential role in male reproduction and fertility. Modulates the hydrolysis of SEMG1 by KLK3/PSA (a serine protease), provides antimicrobial protection for spermatozoa in the ejaculate coagulum, and binds SEMG1 thereby inhibiting sperm motility (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. Cell surface. Note=Present on the surface of spermatozoa both before and after capacitation. SUBUNIT: Monomer. Homodimer. Homomultimers. Interacts (via C-terminus) with SEMG1 (via 164-283 AA). Interacts with LTF. Found in a complex with LTF, CLU, EPPIN and SEMG1. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in differentiated spermatogonia in testis. Expressed in spermatogonia cell lines GC-1 spg and GC-2spd(ts) as well as in the Leydig tumor cell line MLTC-1 (at protein level). Expressed specifically in epididymis and testis. Expressed predominantly on the postacrosomal region of mouse spermatozoa, in Sertoli cells, Leydig cells, and round spermatids in the testis, and in the principal cells of the cauda epididymidis epithelium. {ECO:0000269|PubMed:12909348, ECO:0000269|PubMed:21461566}. +Q61527 ERBB4_MOUSE Receptor tyrosine-protein kinase erbB-4 (EC 2.7.10.1) (Proto-oncogene-like protein c-ErbB-4) [Cleaved into: ERBB4 intracellular domain (4ICD) (E4ICD) (s80HER4)] 1308 146,855 Active site (1); Alternative sequence (2); Binding site (1); Chain (2); Compositional bias (3); Disulfide bond (23); Domain (1); Glycosylation (10); Modified residue (10); Motif (4); Nucleotide binding (3); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 653 673 {ECO:0000255}. TOPO_DOM 26 652 Extracellular. {ECO:0000255}.; TOPO_DOM 674 1308 Cytoplasmic. {ECO:0000255}. FUNCTION: Tyrosine-protein kinase that plays an essential role as cell surface receptor for neuregulins and EGF family members and regulates development of the heart, the central nervous system and the mammary gland, gene transcription, cell proliferation, differentiation, migration and apoptosis. Required for normal cardiac muscle differentiation during embryonic development, and for postnatal cardiomyocyte proliferation. Required for normal development of the embryonic central nervous system, especially for normal neural crest cell migration and normal axon guidance. Required for mammary gland differentiation, induction of milk proteins and lactation. Acts as cell-surface receptor for the neuregulins NRG1, NRG2, NRG3 and NRG4 and the EGF family members BTC, EREG and HBEGF. Ligand binding triggers receptor dimerization and autophosphorylation at specific tyrosine residues that then serve as binding sites for scaffold proteins and effectors. Ligand specificity and signaling is modulated by alternative splicing, proteolytic processing, and by the formation of heterodimers with other ERBB family members, thereby creating multiple combinations of intracellular phosphotyrosines that trigger ligand- and context-specific cellular responses. Mediates phosphorylation of SHC1 and activation of the MAP kinases MAPK1/ERK2 and MAPK3/ERK1. Isoform JM-A CYT-1 and isoform JM-B CYT-1 phosphorylate PIK3R1, leading to the activation of phosphatidylinositol 3-kinase and AKT1 and protect cells against apoptosis. Isoform JM-A CYT-1 and isoform JM-B CYT-1 mediate reorganization of the actin cytoskeleton and promote cell migration in response to NRG1. Isoform JM-A CYT-2 and isoform JM-B CYT-2 lack the phosphotyrosine that mediates interaction with PIK3R1, and hence do not phosphorylate PIK3R1, do not protect cells against apoptosis, and do not promote reorganization of the actin cytoskeleton and cell migration. Proteolytic processing of isoform JM-A CYT-1 and isoform JM-A CYT-2 gives rise to the corresponding soluble intracellular domains (4ICD) that translocate to the nucleus, promote nuclear import of STAT5A, activation of STAT5A, mammary epithelium differentiation, cell proliferation and activation of gene expression. The ERBB4 soluble intracellular domains (4ICD) colocalize with STAT5A at the CSN2 promoter to regulate transcription of milk proteins during lactation. The ERBB4 soluble intracellular domains can also translocate to mitochondria and promote apoptosis. {ECO:0000269|PubMed:10508857, ECO:0000269|PubMed:10655590, ECO:0000269|PubMed:15543145, ECO:0000269|PubMed:15863494, ECO:0000269|PubMed:16837552, ECO:0000269|PubMed:19596786, ECO:0000269|PubMed:19632177, ECO:0000269|PubMed:7477376}. PTM: Isoform JM-A CYT-1 and isoform JM-A CYT-2 are processed by ADAM17. Proteolytic processing in response to ligand or 12-O-tetradecanoylphorbol-13-acetate stimulation results in the production of 120 kDa soluble receptor forms and intermediate membrane-anchored 80 kDa fragments (m80HER4), which are further processed by a presenilin-dependent gamma-secretase to release a cytoplasmic intracellular domain (E4ICD; E4ICD1/s80Cyt1 or E4ICD2/s80Cyt2, depending on the isoform). Membrane-anchored 80 kDa fragments of the processed isoform JM-A CYT-1 are more readily degraded by the proteasome than fragments of isoform JM-A CYT-2, suggesting a prevalence of E4ICD2 over E4ICD1. Isoform JM-B CYT-1 and isoform JM-B CYT-2 lack the ADAM17 cleavage site and are not processed by ADAM17, precluding further processing by gamma-secretase (By similarity). {ECO:0000250}.; PTM: Autophosphorylated on tyrosine residues in response to ligand binding. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Ligands trigger phosphorylation at specific tyrosine residues, thereby creating binding sites for scaffold proteins and effectors. Constitutively phosphorylated at a basal level when overexpressed in heterologous systems; ligand binding leads to increased phosphorylation. Phosphorylation at Tyr-1035 is important for interaction with STAT1. Phosphorylation at Tyr-1056 is important for interaction with PIK3R1. Phosphorylation at Tyr-1242 is important for interaction with SHC1. Phosphorylation at Tyr-1188 may also contribute to the interaction with SHC1. Isoform JM-A CYT-2 is constitutively phosphorylated on tyrosine residues in a ligand-independent manner. E4ICD2 but not E4ICD1 is phosphorylated on tyrosine residues (By similarity). {ECO:0000250}.; PTM: Ubiquitinated. During mitosis, the ERBB4 intracellular domain is ubiquitinated by the APC/C complex and targeted to proteasomal degradation. Isoform JM-A CYT-1 and isoform JM-B CYT-1 are ubiquitinated by WWP1. The ERBB4 intracellular domain (E4ICD1) is ubiquitinated, and this involves NEDD4 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16837552}; Single-pass type I membrane protein {ECO:0000269|PubMed:16837552}. Note=In response to NRG1 treatment, the activated receptor is internalized.; SUBCELLULAR LOCATION: ERBB4 intracellular domain: Nucleus. Mitochondrion {ECO:0000250}. Note=Following proteolytical processing E4ICD (E4ICD1 or E4ICD2 generated from the respective isoforms) is translocated to the nucleus. Significantly more E4ICD2 than E4ICD1 is found in the nucleus. E4ICD2 colocalizes with YAP1 in the nucleus (By similarity). {ECO:0000250}. SUBUNIT: Monomer in the absence of bound ligand. Homodimer or heterodimer with another ERBB family member upon ligand binding, thus forming heterotetramers. Interacts with EGFR and ERBB2. Interacts with DLG2 (via its PDZ domain), DLG3 (via its PDZ domain), DLG4 (via its PDZ domain) and SNTB2 (via its PDZ domain). Interacts with MUC1. Interacts (via its PPxy motifs) with WWOX. Interacts (via the PPxY motif 3 of isoform JM-A CYT-2) with YAP1 (via the WW domain 1 of isoform 1). Interacts (isoform JM-A CYT-1 and isoform JM-B CYT-1) with WWP1. Interacts (via its intracellular domain) with TRIM28. Interacts (via the intracellular domains of both CYT-1 and CYT-2 isoforms) with KAP1; the interaction does not phosphorylate KAP1 but represses ERBB4-mediated transcriptional activity. Interacts with PRPU, DDX23, MATR3, RBM15, ILF3, KAP1, U5S1, U2SURP, ITCH, HNRNPU, AP2A1, NULC, LEO1, WWP2, IGHG1, HXK1, GRB7 AND ARS2. Interacts (phosphorylated isoform JM-A CYT-1 and isoform JM-B CYT-1) with PIK3R1. Interacts with SHC1. Interacts with GRB2. Interacts (soluble intracellular domain) with BCL2. Interacts (phosphorylated) with STAT1 (By similarity). Interacts with CBFA2T3. Interacts (soluble intracellular domain) with STAT5A. {ECO:0000250, ECO:0000269|PubMed:10508857, ECO:0000269|PubMed:16815842}. TISSUE SPECIFICITY: Isoform JM-A CYT-2 and isoform JM-B CYT-2 are expressed in cerebellum, cerebral cortex, spinal cord, medulla oblongata and eye, but the kidney expresses solely isoform JM-A CYT-2 and the heart solely isoform JM-B CYT-2. {ECO:0000269|PubMed:10353604}. +Q8BWY3 ERF1_MOUSE Eukaryotic peptide chain release factor subunit 1 (Eukaryotic release factor 1) (eRF1) 437 49,031 Beta strand (9); Chain (1); Cross-link (2); Helix (5); Initiator methionine (1); Modified residue (4); Motif (1); Sequence conflict (2) FUNCTION: Directs the termination of nascent peptide synthesis (translation) in response to the termination codons UAA, UAG and UGA (By similarity). Component of the transient SURF complex which recruits UPF1 to stalled ribosomes in the context of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons (By similarity). {ECO:0000250|UniProtKB:P62495}. PTM: Hydroxylation at Lys-63 by JMJD4 promotes its translational termination efficiency. {ECO:0000305|PubMed:24486019}.; PTM: Methylated at Gln-185 by N6AMT1. {ECO:0000305|PubMed:20606008}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P62495}. SUBUNIT: Heterodimer of two subunits, one of which binds GTP (By similarity). Component of the transient SURF (SMG1-UPF1-eRF1-eRF3) complex (By similarity). Interacts with JMJD4 (By similarity). The ETF1-GSPT1 complex interacts with JMJD4 (By similarity). {ECO:0000250|UniProtKB:P62495}.; SUBUNIT: (Microbial infection) Interacts with Moloney murine leukemia virus (MoLV) reverse transcriptase/Ribonuclease H p80 (via RT and RNase domains); this interaction is essential for translational readthrough of amber codon between viral gag and pol genes. Interacts with MoLV Gag-Pol precursor. {ECO:0000269|PubMed:14636559}. +Q99P91 GPNMB_MOUSE Transmembrane glycoprotein NMB (DC-HIL) (Dendritic cell-associated transmembrane protein) (Osteoactivin) 574 63,676 Chain (1); Domain (1); Glycosylation (11); Modified residue (1); Motif (1); Sequence conflict (7); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 503 523 Helical. {ECO:0000255}. TOPO_DOM 23 502 Extracellular. {ECO:0000255}.; TOPO_DOM 524 574 Cytoplasmic. {ECO:0000255}. FUNCTION: Could be a melanogenic enzyme. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q14956}. Melanosome membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q14956}. Early endosome membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q14956}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. {ECO:0000250|UniProtKB:Q14956}. TISSUE SPECIFICITY: May be up-regulated in bone metastatic breast cancer cells. {ECO:0000269|PubMed:17951401}. +Q6DI86 FAKD1_MOUSE FAST kinase domain-containing protein 1, mitochondrial 829 95,398 Alternative sequence (4); Chain (1); Domain (1); Modified residue (1); Sequence conflict (5); Transit peptide (1) FUNCTION: Regulates the stability of mitochondrial MT-ND3 mRNA. {ECO:0000250|UniProtKB:Q53R41}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q53R41}. Note=Preferentially localizes to mitochondrial RNA granules, platforms for post-transcriptional RNA modification and ribosome assembly. {ECO:0000250|UniProtKB:Q53R41}. DOMAIN: The RAP domain is essential to regulate MT-ND3 mRNA levels. {ECO:0000250|UniProtKB:Q53R41}. TISSUE SPECIFICITY: Expression detected in spleen, testis, colon, heart, smooth muscle, kidney, brain, lung, liver, brown and white adipose tissue with highest expression in heart and brown adipose tissue. {ECO:0000269|PubMed:20869947}. +Q922E6 FAKD2_MOUSE FAST kinase domain-containing protein 2, mitochondrial 689 78,948 Chain (1); Domain (1); Modified residue (2); Sequence conflict (6); Transit peptide (1) FUNCTION: Plays an important role in assembly of the mitochondrial large ribosomal subunit. As a component of a functional protein-RNA module, consisting of RCC1L, NGRN, RPUSD3, RPUSD4, TRUB2, FASTKD2 and 16S mitochondrial ribosomal RNA (16S mt-rRNA), controls 16S mt-rRNA abundance and is required for intra-mitochondrial translation. {ECO:0000250|UniProtKB:Q9NYY8}. SUBCELLULAR LOCATION: Mitochondrion matrix, mitochondrion nucleoid {ECO:0000250|UniProtKB:Q9NYY8}. Note=Localizes to mitochondrial RNA granules found in close proximity to the mitochondrial nucleoids. {ECO:0000250|UniProtKB:Q9NYY8}. SUBUNIT: Monomer. Found in a complex with GRSF1, DDX28, DHX30 and FASTKD5. Associates with the 16S mitochondrial rRNA (16S mt-rRNA). Forms a regulatory protein-RNA complex, consisting of RCC1L, NGRN, RPUSD3, RPUSD4, TRUB2, FASTKD2 and 16S mt-rRNA. {ECO:0000250|UniProtKB:Q9NYY8}. TISSUE SPECIFICITY: Expression detected in spleen, testis, colon, heart, smooth muscle, kidney, brain, lung, liver, brown and white adipose tissue with highest expression in testis, heart and smooth muscle. {ECO:0000269|PubMed:20869947}. +Q8K368 FANCI_MOUSE Fanconi anemia group I protein homolog (Protein FACI) 1330 149,326 Alternative sequence (3); Beta strand (11); Chain (1); Cross-link (1); Erroneous initiation (1); Helix (70); Modified residue (5); Sequence conflict (1); Turn (12) FUNCTION: Plays an essential role in the repair of DNA double-strand breaks by homologous recombination and in the repair of interstrand DNA cross-links (ICLs) by promoting FANCD2 monoubiquitination by FANCL and participating in recruitment to DNA repair sites. Required for maintenance of chromosomal stability. Specifically binds branched DNA: binds both single-stranded DNA (ssDNA) and double-stranded DNA (dsDNA). Participates in S phase and G2 phase checkpoint activation upon DNA damage. PTM: Monoubiquitinated by FANCL on Lys-522 during S phase and upon genotoxic stress. Deubiquitinated by USP1 as cells enter G2/M, or once DNA repair is completed. Monoubiquitination requires the FANCA-FANCB-FANCC-FANCE-FANCF-FANCG-FANCM complex. Ubiquitination is required for binding to chromatin, DNA repair, and normal cell cycle progression. Monoubiquitination is stimulated by DNA-binding (By similarity). {ECO:0000250}.; PTM: Phosphorylated in response to DNA damage by ATM and/or ATR. {ECO:0000269|PubMed:17412408}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Observed in spots localized in pairs on the sister chromatids of mitotic chromosome arms and not centromeres, one on each chromatids. These foci coincide with common fragile sites. They are frequently interlinked through BLM-associated ultra-fine DNA bridges (By similarity). {ECO:0000250}. SUBUNIT: Interacts with FANCD2; the interaction is direct. Interacts with FANCL. Interacts with MTMR15/FAN1. Interacts with POLN. {ECO:0000250|UniProtKB:Q9NVI1}. DOMAIN: The C-terminal 30 residues are probably required for function in DNA repair. {ECO:0000250}. +Q5SXJ3 FANCJ_MOUSE Fanconi anemia group J protein homolog (Protein FACJ) (EC 3.6.4.13) (ATP-dependent RNA helicase BRIP1) (BRCA1-associated C-terminal helicase 1) (BRCA1-interacting protein C-terminal helicase 1) (BRCA1-interacting protein 1) 1174 131,360 Chain (1); Domain (1); Metal binding (4); Modified residue (4); Motif (2); Nucleotide binding (1); Region (1) FUNCTION: DNA-dependent ATPase and 5' to 3' DNA helicase required for the maintenance of chromosomal stability. Acts late in the 'Fanconi anemia' pathway, after FANCD2 ubiquitination. Involved in the repair of DNA double-strand breaks by homologous recombination in a manner that depends on its association with BRCA1 (By similarity). {ECO:0000250|UniProtKB:Q9BX63}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BX63}. Cytoplasm {ECO:0000250|UniProtKB:Q9BX63}. SUBUNIT: Binds directly to the BRCT domains of BRCA1. Interacts with the CIA complex components CIAO1, CIAO2B and MMS19. {ECO:0000250|UniProtKB:Q9BX63}. +Q9JL70 FANCA_MOUSE Fanconi anemia group A protein homolog (Protein FACA) 1439 161,213 Chain (1); Motif (1); Sequence conflict (30) FUNCTION: DNA repair protein that may operate in a postreplication repair or a cell cycle checkpoint function. May be involved in interstrand DNA cross-link repair and in the maintenance of normal chromosome stability (By similarity). {ECO:0000250}. PTM: Phosphorylated primarily on serine residues. Phosphorylation is required for the formation of the nuclear complex (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=The major form is nuclear. The minor form is cytoplasmic. SUBUNIT: Belongs to the multisubunit FA complex composed of FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL/PHF9 and FANCM (By similarity). In complex with FANCF, FANCG and FANCL, but not with FANCC, nor FANCE, interacts with HES1; this interaction may be essential for the stability and nuclear localization of FA core complex proteins (By similarity). The complex with FANCC and FANCG may also include EIF2AK2 and HSP70. Interacts with FAAP20; interaction is direct (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Mainly expressed in testis and lymphoid tissues like thymus, lymph nodes, and spleen, and at lower levels in kidney and ovary. {ECO:0000269|PubMed:10754110}. +Q5XJY6 FANCB_MOUSE Fanconi anemia group B protein homolog (Protein FACB) 703 80,088 Chain (1); Erroneous initiation (1) FUNCTION: DNA repair protein required for FANCD2 ubiquitination. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Belongs to the multisubunit FA complex composed of FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL/PHF9 and FANCM. {ECO:0000250}. +Q9DAM9 FANK1_MOUSE Fibronectin type 3 and ankyrin repeat domains 1 protein (Germ cell-specific gene 1 protein) (GSG1) 344 38,260 Beta strand (8); Chain (1); Domain (1); Helix (1); Repeat (6); Sequence conflict (3); Turn (1) FUNCTION: Through the activation of JUN and AP-1-mediated transcription, may regulate apoptosis. {ECO:0000250|UniProtKB:Q8TC84}. PTM: Polyubiquitinated. Polyubiquitination leads to proteasomal degradation. {ECO:0000250|UniProtKB:Q8TC84}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17604233}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8TC84}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:27914912}. Cell projection, cilium {ECO:0000269|PubMed:27914912}. Note=Weakly detected in the cytoplasm of elongated spermatids. {ECO:0000269|PubMed:17604233}. SUBUNIT: Interacts with COPS5; regulates the phosphorylation of JUN and the transcriptional activity of AP-1. Interacts with RYBP; may prevent the ubiquitin-mediated proteasomal degradation of FANK1. {ECO:0000250|UniProtKB:Q8TC84}. DOMAIN: The fibronectin type-III domain mediates interaction with COPS5 and RYBP. {ECO:0000250|UniProtKB:Q8TC84}. TISSUE SPECIFICITY: Mostly restricted to testis (at protein level), including mid to late pachytene spermatocytes (stages VI-X), diplotene spermatocytes (stage XI), meiotically dividing spermatocytes (stage XII) and spermatids in steps 1-14. Highest levels in late pachytene spermatocytes and spermatids in steps 1-9. {ECO:0000269|PubMed:17604233}. +F8VPU2 FARP1_MOUSE FERM, ARHGEF and pleckstrin domain-containing protein 1 (FERM, RhoGEF and pleckstrin domain-containing protein 1) 1048 118,875 Chain (1); Compositional bias (1); Domain (4); Modified residue (19); Sequence conflict (3) FUNCTION: Functions as guanine nucleotide exchange factor for RAC1. May play a role in semaphorin signaling. Plays a role in the assembly and disassembly of dendritic filopodia, the formation of dendritic spines, regulation of dendrite length and ultimately the formation of synapses (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23209303}; Peripheral membrane protein {ECO:0000269|PubMed:23209303}; Cytoplasmic side {ECO:0000269|PubMed:23209303}. Cell junction, synapse {ECO:0000269|PubMed:23209303}. Cell junction, synapse, synaptosome {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Cell projection, filopodium {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cell projection, dendritic spine {ECO:0000250}. Note=Recruited to the cell membrane via interaction with CADM1. {ECO:0000250}. SUBUNIT: Interacts with CADM1. Interacts with RAC1 (By similarity). {ECO:0000250}. DOMAIN: Intramolecular interaction between the DH domain and the PH domains can stabilize the protein in an autoinhibited conformation. {ECO:0000250}. TISSUE SPECIFICITY: Detected in brain cortex, hippocampus, striatum, olfactory bulb, cerebellum and hindbrain (at protein level). {ECO:0000269|PubMed:23209303}. +Q91VS8 FARP2_MOUSE FERM, ARHGEF and pleckstrin domain-containing protein 2 (FERM domain including RhoGEF) (FIR) (FERM, RhoGEF and pleckstrin domain-containing protein 2) 1065 121,281 Beta strand (30); Chain (1); Compositional bias (1); Domain (4); Helix (31); Modified residue (4); Mutagenesis (2); Sequence conflict (4); Turn (4) FUNCTION: Functions as guanine nucleotide exchange factor that activates RAC1. May have relatively low activity (PubMed:23375260 and PubMed:20702777). Plays a role in the response to class 3 semaphorins and remodeling of the actin cytoskeleton. Plays a role in TNFSF11-mediated osteoclast differentiation, especially in podosome rearrangement and reorganization of the actin cytoskeleton. Regulates the activation of ITGB3, integrin signaling and cell adhesion. {ECO:0000269|PubMed:12351724, ECO:0000269|PubMed:16286926, ECO:0000269|PubMed:20702777, ECO:0000269|PubMed:23375260}. SUBUNIT: Interacts with PLXNA1. Interaction with PLXNA1 or PIP5K1C lowers its guanine nucleotide exchange activity. Dissociates from PLXNA1 when SEMA3A binds to the receptor. Interacts with PIP5K1C via its FERM domain. The interaction with PIP5K1C is enhanced by SEMA3A binding. Interacts with RAC1. {ECO:0000269|PubMed:12351724, ECO:0000269|PubMed:16286926, ECO:0000269|PubMed:23375260}. DOMAIN: Intramolecular interaction between the DH domain and the PH domains can stabilize the protein in an autoinhibited conformation. {ECO:0000269|PubMed:23375260}. TISSUE SPECIFICITY: Detected in adult brain, lung and testis. Detected in embryonic hippocampus and brain cortex. {ECO:0000269|PubMed:12351724}. +Q8BNA6 FAT3_MOUSE Protocadherin Fat 3 (FAT tumor suppressor homolog 3) 4555 502,011 Alternative sequence (5); Chain (1); Compositional bias (1); Disulfide bond (13); Domain (38); Glycosylation (26); Modified residue (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 4154 4174 Helical. {ECO:0000255}. TOPO_DOM 32 4153 Extracellular. {ECO:0000255}.; TOPO_DOM 4175 4555 Cytoplasmic. {ECO:0000255}. FUNCTION: May play a role in the interactions between neurites derived from specific subsets of neurons during development. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Restricted to the nervous system, mainly in brain. In brain, it is highly expressed in the olfactory bulb and retina. In the developing olfactory bulb, it localizes along the dendrites of these cells as well as in their axons to some extent. In retina, it cocentrates in the inner plexiform layer throughout development (at protein level). {ECO:0000269|PubMed:16059920, ECO:0000269|PubMed:17131403}. +Q2PZL6 FAT4_MOUSE Protocadherin Fat 4 (FAT tumor suppressor homolog 4) (Fat-like cadherin protein FAT-J) 4981 540,316 Alternative sequence (2); Chain (1); Disulfide bond (20); Domain (42); Erroneous initiation (2); Glycosylation (38); Modified residue (1); Region (1); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 4506 4526 Helical. {ECO:0000255}. TOPO_DOM 43 4505 Extracellular. {ECO:0000255}.; TOPO_DOM 4527 4981 Cytoplasmic. {ECO:0000255}. FUNCTION: Cadherins are cell-cell interaction molecules. FAT4 plays a role in the maintenance of planar cell polarity as well as in inhibition of YAP1-mediated neuroprogenitor cell proliferation and differentiation. {ECO:0000269|PubMed:18604206, ECO:0000269|PubMed:24056717}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=In the kidney, localizes to primary cilia. {ECO:0000250}. SUBUNIT: Heterophilic interaction with DCHS1; this interaction affects their respective protein levels. Interacts (via cytoplasmic domain) with MPDZ. Forms a complex with MPP5 and MPDZ. {ECO:0000269|PubMed:19506035}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:16059920}. +P0C5I1 GPR25_MOUSE Probable G-protein coupled receptor 25 358 38,754 Chain (1); Disulfide bond (1); Topological domain (8); Transmembrane (7) TRANSMEM 44 64 Helical; Name=1. {ECO:0000255}.; TRANSMEM 77 97 Helical; Name=2. {ECO:0000255}.; TRANSMEM 114 134 Helical; Name=3. {ECO:0000255}.; TRANSMEM 156 176 Helical; Name=4. {ECO:0000255}.; TRANSMEM 201 221 Helical; Name=5. {ECO:0000255}.; TRANSMEM 240 260 Helical; Name=6. {ECO:0000255}.; TRANSMEM 285 307 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 43 Extracellular. {ECO:0000255}.; TOPO_DOM 65 76 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 98 113 Extracellular. {ECO:0000255}.; TOPO_DOM 135 155 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 177 200 Extracellular. {ECO:0000255}.; TOPO_DOM 222 239 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 261 284 Extracellular. {ECO:0000255}.; TOPO_DOM 308 358 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan receptor. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +A2AV25 FBCD1_MOUSE Fibrinogen C domain-containing protein 1 459 50,602 Alternative sequence (1); Chain (1); Disulfide bond (2); Domain (1); Glycosylation (1); Metal binding (2); Sequence conflict (1); Site (4); Topological domain (2); Transmembrane (1) TRANSMEM 34 54 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 33 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 55 459 Extracellular. {ECO:0000255}. FUNCTION: Acetyl group-binding receptor which shows a high-affinity and calcium-dependent binding to acetylated structures such as chitin, some N-acetylated carbohydrates, and amino acids, but not to their non-acetylated counterparts. Can facilitate the endocytosis of acetylated components (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. SUBUNIT: Homotetramer; disulfide-linked. {ECO:0000250}. +Q60584 FBXW2_MOUSE F-box/WD repeat-containing protein 2 (F-box and WD-40 domain-containing protein 2) (Protein MD6) 422 47,896 Chain (1); Domain (1); Modified residue (1); Repeat (4); Sequence conflict (3) FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. SUBUNIT: Directly interacts with SKP1 and CUL1. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed during embryogenesis and in adult tissues. {ECO:0000269|PubMed:10531037}. +Q9QXW2 FBXW5_MOUSE F-box/WD repeat-containing protein 5 (F-box and WD-40 domain-containing protein 5) 573 64,646 Alternative sequence (2); Chain (1); Domain (1); Erroneous gene model prediction (1); Modified residue (1); Motif (1); Repeat (3) Protein modification; protein ubiquitination. FUNCTION: Substrate recognition component of both SCF (SKP1-CUL1-F-box protein) and DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes. Substrate-specific adapter of the DCX(FBXW5) E3 ubiquitin-protein ligase complex which mediates the polyubiquitination and subsequent degradation of TSC2. May also act as a negative regulator of MAP3K7/TAK1 signaling in the interleukin-1B (IL1B) signaling pathway. Substrate recognition component of the SCF(FBXW5) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of SASS6 during S phase, leading to prevent centriole reduplication (By similarity). The SCF(FBXW5) complex also mediates ubiquitination and degradation of actin-regulator EPS8 during G2 phase, leading to the transient degradation of EPS8 and subsequent cell shape changes required to allow mitotic progression. {ECO:0000250, ECO:0000269|PubMed:23314863}. PTM: Phosphorylated at Ser-151 by PLK4 during the G1/S transition, leading to inhibit its ability to ubiquitinate SASS6. {ECO:0000250}.; PTM: Ubiquitinated and degraded by the APC/C complex during mitosis and G1 phase. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q969U6}. SUBUNIT: Part of the SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase complex SCF(FBXW5) composed of CUL1, SKP1, RBX1 and FBXW5. Component of the DCX(FBXW5) E3 ubiquitin ligase complex, at least composed of (CUL4A or CUL4B), DDB1, FBXW5 and RBX1. Interacts with CDC20, TSC1, TSC2 and SASS6 (By similarity). Interacts with EPS8. Interacts with TNFAIP8L1; TNFAIP8L1 competes with TSC2 to bind FBXW5 increasing TSC2 stability by preventing its ubiquitination. {ECO:0000250, ECO:0000269|PubMed:10531037, ECO:0000269|PubMed:23314863, ECO:0000269|PubMed:24444419}. DOMAIN: The F-box domain mediates interaction with components of SCF (SKP1-CUL1-F-box protein) complexes, while WD repeats mediate interaction with components of DCX (DDB1-CUL4-X-box) complexes. {ECO:0000250}.; DOMAIN: The D-box (destruction box) mediate the interaction with APC proteins, and acts as a recognition signal for degradation via the ubiquitin-proteasome pathway. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed in adult and embryonal tissues. {ECO:0000269|PubMed:10531037}. +Q61554 FBN1_MOUSE Fibrillin-1 [Cleaved into: Asprosin] 2873 312,298 Chain (2); Compositional bias (1); Disulfide bond (155); Domain (56); Glycosylation (15); Modified residue (3); Motif (1); Propeptide (1); Region (6); Sequence conflict (32); Signal peptide (1); Site (2) FUNCTION: Fibrillin-1: Structural component of the 10-12 nm diameter microfibrils of the extracellular matrix, which conveys both structural and regulatory properties to load-bearing connective tissues. Fibrillin-1-containing microfibrils provide long-term force bearing structural support. In tissues such as the lung, blood vessels and skin, microfibrils form the periphery of the elastic fiber, acting as a scaffold for the deposition of elastin. In addition, microfibrils can occur as elastin-independent networks in tissues such as the ciliary zonule, tendon, cornea and glomerulus where they provide tensile strength and have anchoring roles. Fibrillin-1 also plays a key role in tissue homeostasis through specific interactions with growth factors, such as the bone morphogenetic proteins (BMPs), growth and differentiation factors (GDFs) and latent transforming growth factor-beta-binding proteins (LTBPs), cell-surface integrins and other extracellular matrix protein and proteoglycan components (By similarity). Regulates osteoblast maturation by controlling TGF-beta bioavailability and calibrating TGF-beta and BMP levels, respectively (PubMed:20855508). Negatively regulates osteoclastogenesis by binding and sequestering an osteoclast differentiation and activation factor TNFSF11. This leads to disruption of TNFSF11-induced Ca(2+) signaling and impairment of TNFSF11-mediated nuclear translocation and activation of transcription factor NFATC1 which regulates genes important for osteoclast differentiation and function (PubMed:24039232). Mediates cell adhesion via its binding to cell surface receptors integrins ITGAV:ITGB3 and ITGA5:ITGB1. Binds heparin and this interaction plays an important role in the assembly of microfibrils (By similarity). {ECO:0000250|UniProtKB:P35555, ECO:0000269|PubMed:20855508, ECO:0000269|PubMed:24039232}.; FUNCTION: Asprosin: Hormone that targets the liver to increase plasma glucose levels. Secreted by white adipose tissue and circulates in the plasma. Acts in response to fasting and promotes blood glucose elevation by binding to the surface of hepatocytes. Promotes hepatocyte glucose release by activating the protein kinase A activity in the liver, resulting in rapid glucose release into the circulation. {ECO:0000250|UniProtKB:P35555}. PTM: Fibrillin-1: Cleavage of N- and C-terminus by furin is required for incorporation into the extracellular matrix and assembly into microfibrils. The C-terminus, which corresponds to the Asprosin chain, was initially thought to constitute a propeptide. Fibrillin-1 and Asprosin chains are still linked together during the secretion from cells, but are subsequently separated by furin, an essential step for incorporation of Fibrillin-1 into the nascent microfibrils. {ECO:0000250|UniProtKB:P35555}.; PTM: Fibrillin-1: Forms intermolecular disulfide bonds either with other fibrillin-1 molecules or with other components of the microfibrils. {ECO:0000250|UniProtKB:P35555}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P35555}. Note=Fibrillin-1 and Asprosin chains are still linked together during the secretion from cells, but are subsequently separated by furin. {ECO:0000250|UniProtKB:P35555}.; SUBCELLULAR LOCATION: Asprosin: Secreted {ECO:0000250|UniProtKB:P35555}. Note=Secreted into the plasma. {ECO:0000250|UniProtKB:P35555}.; SUBCELLULAR LOCATION: Fibrillin-1: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:24039232}. SUBUNIT: Interacts with COL16A1. Interacts with integrin alpha-V/beta-3. Interacts with ADAMTS10; this interaction promotes microfibril assembly (By similarity). Interacts with THSD4; this interaction promotes fibril formation (PubMed:19940141). Interacts (via N-terminal domain) with FBLN2, FBLN4 and FBLN5. Interacts with ELN. Forms a ternary complex with ELN and FBLN2 or FBLN5 and a significant interaction with ELN seen only in the presence of FBLN2 or FBLN5. Interacts (via N-terminal domain) with LTBP2 (via C-terminal domain) in a Ca(+2)-dependent manner. Interacts (via N-terminal domain) with LTBP1 (via C-terminal domain). Interacts with integrins ITGA5:ITGB1, ITGAV:ITGB3 and ITGAV:ITGB6. Interacts (via N-terminal domain) with BMP2, BMP4, BMP7, BMP10 and GDF5. Interacts (via N-terminal domain) with MFAP2 and MFAP5. Interacts with ADAMTSL5. Interacts with MFAP4. Interacts (via N-terminal domain) with TNFSF11 in a Ca(+2)-dependent manner (By similarity). {ECO:0000250|UniProtKB:P35555, ECO:0000269|PubMed:19940141}. TISSUE SPECIFICITY: Asprosin: Secreted by white adipose tissue (at protein level) (PubMed:27087445). Fibrillin-1: Strongly expressed during the first week of osteoblast differentiation (PubMed:24039232). {ECO:0000269|PubMed:24039232, ECO:0000269|PubMed:27087445}. +Q61555 FBN2_MOUSE Fibrillin-2 [Cleaved into: Fibrillin-2 C-terminal peptide] 2907 313,818 Chain (2); Disulfide bond (141); Domain (56); Glycosylation (12); Propeptide (1); Region (2); Sequence conflict (21); Signal peptide (1) FUNCTION: Fibrillin-2: Fibrillins are structural components of 10-12 nm extracellular calcium-binding microfibrils, which occur either in association with elastin or in elastin-free bundles. Fibrillin-2-containing microfibrils regulate the early process of elastic fiber assembly. Regulates osteoblast maturation by controlling TGF-beta bioavailability and calibrating TGF-beta and BMP levels, respectively (PubMed:20855508). {ECO:0000269|PubMed:20855508}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:24039232}. SUBUNIT: Interacts with BMP2, BMP4, BMP7, BMP10 and GDF5. Interacts with MFAP2 and MFAP5. Interacts with ADAMTSL5. Interacts with MFAP4. {ECO:0000250|UniProtKB:P35556}. TISSUE SPECIFICITY: Strongly expressed during the first week of osteoblast differentiation. {ECO:0000269|PubMed:24039232}. +Q9DAK4 FBP12_MOUSE Fatty acid-binding protein 12 132 14,758 Binding site (1); Chain (1); Region (1) FUNCTION: May play a role in lipid transport. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in adult retina and testis. {ECO:0000269|PubMed:18786628}. +Q8K012 FBP1L_MOUSE Formin-binding protein 1-like (Transducer of Cdc42-dependent actin assembly protein 1) (Toca-1) 605 69,885 Alternative sequence (2); Chain (1); Coiled coil (2); Domain (3); Erroneous initiation (1); Modified residue (4); Region (4); Site (1) FUNCTION: Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during endocytosis. May bind to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promote membrane invagination and the formation of tubules. Also promotes CDC42-induced actin polymerization by activating the WASL-WASPIP complex, the predominant form of WASL/N-WASP in cells. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. Essential for autophagy of intracellular bacterial pathogens (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. SUBUNIT: Homodimerizes, the dimers can polymerize end-to-end to form filamentous structures. Interacts with GTP-bound CDC42. Interacts with DAAM1, DIAPH1, DIAPH2, DNM1, DNM2 and WASL/N-WASP. Interacts with ATG3. Interacts (via SH3 domain) with ABI1, WASF2, CDC42 and WIPF1. {ECO:0000250, ECO:0000250|UniProtKB:Q5T0N5}. DOMAIN: The F-BAR domain binds the phospholipid membrane with its concave surface. The end-to-end polymerization of dimers of these domains provides a curved surface that fits best membranes with around 600 A diameter, and may drive tubulation (By similarity). {ECO:0000250}. +Q9WTX7 FHL5_MOUSE Four and a half LIM domains protein 5 (FHL-5) (Activator of cAMP-responsive element modulator in testis) (Activator of CREM in testis) 284 32,907 Chain (1); Domain (3); Zinc finger (1) FUNCTION: May be involved in the regulation of spermatogenesis. Stimulates CREM transcriptional activity in a phosphorylation-independent manner (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10086359}. Note=Nuclei of round and elongated spermatids. SUBUNIT: Interacts with CREM (via the third LIM domain) (PubMed:10086359). Interacts (via second LIM domain) with SPAG8 (PubMed:20488182). {ECO:0000269|PubMed:10086359, ECO:0000269|PubMed:20488182}. TISSUE SPECIFICITY: Testis-specific, temporal expression is coordinated with CREM. {ECO:0000269|PubMed:10086359}. +Q05816 FABP5_MOUSE Fatty acid-binding protein 5 (Epidermal-type fatty acid-binding protein) (E-FABP) (Fatty acid-binding protein, epidermal) (Keratinocyte lipid-binding protein) (Psoriasis-associated fatty acid-binding protein homolog) (PA-FABP) 135 15,137 Beta strand (10); Binding site (2); Chain (1); Disulfide bond (1); Helix (3); Initiator methionine (1); Modified residue (3); Motif (1); Region (1) FUNCTION: Intracellular carrier for long-chain fatty acids and related active lipids, such as the endocannabinoid, that regulates the metabolism and actions of the ligands they bind (PubMed:8608126, PubMed:12540600). In addition to the cytosolic transport, selectively delivers specific fatty acids from the cytosol to the nucleus, wherein they activate nuclear receptors (By similarity). Delivers retinoic acid to the nuclear receptor peroxisome proliferator-activated receptor delta; which promotes proliferation and survival (PubMed:17512406). May also serve as a synaptic carrier of endocannabinoid at central synapses and thus controls retrograde endocannabinoid signaling (PubMed:29531087). Modulates inflammation by regulating PTGES induction via NF-kappa-B activation, and prostaglandin E2 (PGE2) biosynthesis during inflammation (PubMed:29440395). May be involved in keratinocyte differentiation (By similarity). {ECO:0000250|UniProtKB:Q01469, ECO:0000269|PubMed:12540600, ECO:0000269|PubMed:17512406, ECO:0000269|PubMed:29440395, ECO:0000269|PubMed:29531087, ECO:0000269|PubMed:8608126}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17512406, ECO:0000269|PubMed:29531087}. Nucleus {ECO:0000269|PubMed:17512406}. Cell junction, synapse {ECO:0000269|PubMed:29531087}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000269|PubMed:29531087}. Secreted {ECO:0000269|PubMed:29531087}. Note=Localizes primarily to the cytoplasm. Upon certain ligand binding, a conformation change exposes a nuclear localization motif and the protein is transported into nucleus (By similarity). Secreted by astrocytes, but not by neurons (PubMed:29531087). {ECO:0000250|UniProtKB:Q01469, ECO:0000269|PubMed:29531087}. SUBUNIT: Monomer. {ECO:0000269|PubMed:8608126}. DOMAIN: Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:8349619}. +O08716 FABP9_MOUSE Fatty acid-binding protein 9 (15 kDa perforatorial protein) (PERF 15) (Testis lipid-binding protein) (TLBP) (Testis-type fatty acid-binding protein) (T-FABP) 132 15,017 Chain (1); Modified residue (6); Sequence conflict (7) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. TISSUE SPECIFICITY: Testis. +Q80V62 FACD2_MOUSE Fanconi anemia group D2 protein homolog (Protein FACD2) 1450 163,618 Alternative sequence (2); Beta strand (9); Chain (1); Cross-link (1); Helix (63); Modified residue (7); Region (2); Turn (10) FUNCTION: Required for maintenance of chromosomal stability. Promotes accurate and efficient pairing of homologs during meiosis. Involved in the repair of DNA double-strand breaks, both by homologous recombination and single-strand annealing. May participate in S phase and G2 phase checkpoint activation upon DNA damage. Plays a role in preventing breakage and loss of missegregating chromatin at the end of cell division, particularly after replication stress (By similarity). Promotes BRCA2/FANCD1 loading onto damaged chromatin. May also be involved in B-cell immunoglobulin isotype switching. {ECO:0000250, ECO:0000269|PubMed:12893777}. PTM: Monoubiquitinated on Lys-559 during S phase and upon genotoxic stress by FANCL in complex with E2 ligases UBE2T or UBE2W. Deubiquitinated by USP1 as cells enter G2/M, or once DNA repair is completed. Monoubiquitination requires the joint intervention of the FANC core complex, including FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL and FANCM, and proteins involved in cell cycle checkpoints and DNA repair, including RPA1, ATR, CHEK1 and BRCA1. Ubiquitination is required for binding to chromatin, interaction with BRCA1, BRCA2 and MTMR15/FAN1, DNA repair, and normal cell cycle progression (By similarity). {ECO:0000250}.; PTM: Phosphorylated on several sites including Ser-220 and Ser-1399 in response to genotoxic stress. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Concentrates in nuclear foci during S phase and upon genotoxic stress. {ECO:0000250}. SUBUNIT: Interacts directly with FANCE and FANCI. Interacts with USP1 and MEN1. The ubiquitinated form specifically interacts with BRCA1 and BLM. Both the nonubiquitinated and the monoubiquitinated forms interact with BRCA2; this interaction is mediated by phosphorylated FANCG and the complex also includes XCCR3. The ubiquitinated form specifically interacts with MTMR15/FAN1 (via UBZ-type zinc finger), leading to recruit MTMR15/FAN1 to sites of DNA damage. Interacts with DCLRE1B/Apollo. Interacts with POLN. {ECO:0000250|UniProtKB:Q9BXW9}. +Q80W54 FACE1_MOUSE CAAX prenyl protease 1 homolog (EC 3.4.24.84) (Farnesylated proteins-converting enzyme 1) (FACE-1) (Prenyl protein-specific endoprotease 1) (Zinc metalloproteinase Ste24 homolog) 475 54,735 Active site (2); Chain (1); Metal binding (3); Sequence conflict (3); Topological domain (8); Transmembrane (7) TRANSMEM 19 39 Helical. {ECO:0000255}.; TRANSMEM 82 102 Helical. {ECO:0000255}.; TRANSMEM 124 144 Helical. {ECO:0000255}.; TRANSMEM 171 191 Helical. {ECO:0000255}.; TRANSMEM 196 216 Helical. {ECO:0000255}.; TRANSMEM 348 368 Helical. {ECO:0000255}.; TRANSMEM 383 405 Helical. {ECO:0000255}. TOPO_DOM 1 18 Lumenal. {ECO:0000255}.; TOPO_DOM 40 81 Nuclear. {ECO:0000255}.; TOPO_DOM 103 123 Lumenal. {ECO:0000255}.; TOPO_DOM 145 170 Nuclear. {ECO:0000255}.; TOPO_DOM 192 195 Lumenal. {ECO:0000255}.; TOPO_DOM 217 347 Nuclear. {ECO:0000255}.; TOPO_DOM 369 382 Lumenal. {ECO:0000255}.; TOPO_DOM 406 475 Nuclear. {ECO:0000255}. FUNCTION: Proteolytically removes the C-terminal three residues of farnesylated proteins. Acts on lamin A/C. {ECO:0000269|PubMed:11923874}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Nucleus inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. DOMAIN: The metalloprotease domain is constituted by the two C-terminal nuclear regions. {ECO:0000250}. +Q9D4K4 FACOS_MOUSE FANCD2 opposite strand protein (Fanconi anemia group D2 protein opposite strand transcript protein) 178 20,255 Chain (1); Sequence conflict (2) +Q8R123 FAD1_MOUSE FAD synthase (EC 2.7.7.2) (FAD pyrophosphorylase) (FMN adenylyltransferase) (Flavin adenine dinucleotide synthase) [Includes: Molybdenum cofactor biosynthesis protein-like region; FAD synthase region] 492 54,766 Alternative sequence (1); Chain (1); Modified residue (3); Region (2); Sequence conflict (2) Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1. FUNCTION: Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. DOMAIN: The molybdenum cofactor biosynthesis protein-like region may not be functional. +Q7TNT2 FACR2_MOUSE Fatty acyl-CoA reductase 2 (EC 1.2.1.84) 515 59,167 Alternative sequence (1); Chain (1); Sequence conflict (3); Topological domain (2); Transmembrane (1) TRANSMEM 465 484 Helical. {ECO:0000255}. TOPO_DOM 1 464 Cytoplasmic. {ECO:0000250|UniProtKB:Q96K12}.; TOPO_DOM 485 515 Peroxisomal. {ECO:0000250|UniProtKB:Q96K12}. FUNCTION: Catalyzes the reduction of saturated but not unsaturated C16 or C18 fatty acyl-CoA to fatty alcohols. A lower activity can be observed with shorter fatty acyl-CoA substrates (PubMed:15220348). It may play a role in the production of ether lipids/plasmalogens and wax monoesters which synthesis requires fatty alcohols as substrates (By similarity). {ECO:0000250|UniProtKB:Q8WVX9, ECO:0000269|PubMed:15220348}. SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000269|PubMed:15220348}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q96K12}. TISSUE SPECIFICITY: Specifically expressed in the meibomian glands of the eyelid and the sebaceous glands of the skin. Also expressed in the brain where large quantities of ether lipids are synthesized. {ECO:0000269|PubMed:15220348}. +P50652 FANCC_MOUSE Fanconi anemia group C protein homolog (Protein FACC) 591 66,979 Chain (1); Frameshift (1); Sequence caution (1); Sequence conflict (4) FUNCTION: DNA repair protein that may operate in a postreplication repair or a cell cycle checkpoint function. May be implicated in interstrand DNA cross-link repair and in the maintenance of normal chromosome stability. Upon IFNG induction, may facilitate STAT1 activation by recruiting STAT1 to IFNGR1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=The major form is nuclear. The minor form is cytoplasmic. SUBUNIT: Belongs to the multisubunit FA complex composed of FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL/PHF9 and FANCM. This complex may also include HSP70. Interacts with ZBTB32. Upon IFNG induction, interacts with STAT1. Interacts with CDK1. Interacts with EIF2AK2 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. +Q8BHL6 FAP24_MOUSE Fanconi anemia core complex-associated protein 24 (Fanconi anemia-associated protein of 24 kDa) 221 24,641 Chain (1); Sequence conflict (2) FUNCTION: Plays a role in DNA repair through recruitment of the FA core complex to damaged DNA. Regulates FANCD2 monoubiquitination upon DNA damage. Induces chromosomal instability as well as hypersensitivity to DNA cross-linking agents, when repressed. Targets FANCM/FAAP24 complex to the DNA, preferentially to single strand DNA (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Belongs to the multisubunit FA complex composed of FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL/PHF9, FANCM and FAAP24. Interacts with FANCM (By similarity). {ECO:0000250}. DOMAIN: The C-terminal region is distantly related to RuvA domain 2, a DNA-binding domain. +Q8BPB5 FBLN3_MOUSE EGF-containing fibulin-like extracellular matrix protein 1 (Fibulin-3) (FIBL-3) 493 54,953 Chain (1); Disulfide bond (15); Domain (6); Glycosylation (1); Region (1); Signal peptide (1) FUNCTION: Binds EGFR, the EGF receptor, inducing EGFR autophosphorylation and the activation of downstream signaling pathways. May play a role in cell adhesion and migration. May function as a negative regulator of chondrocyte differentiation. In the olfactory epithelium, it may regulate glial cell migration, differentiation and the ability of glial cells to support neuronal neurite outgrowth (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250}. Secreted, extracellular space, extracellular matrix {ECO:0000250}. Note=Localizes to the lamina propria underneath the olfactory epithelium. {ECO:0000250}. SUBUNIT: Interacts with ECM1. Interacts with TIMP3. {ECO:0000250}. +Q9WVJ9 FBLN4_MOUSE EGF-containing fibulin-like extracellular matrix protein 2 (Fibulin-4) (FIBL-4) (Mutant p53-binding protein 1) 443 49,425 Chain (1); Disulfide bond (18); Domain (6); Glycosylation (2); Signal peptide (1) SUBCELLULAR LOCATION: Secreted. SUBUNIT: Binds preferentially to p53 mutants (PubMed:10380882). Interacts with FBN1 (via N-terminal domain) (By similarity). {ECO:0000250|UniProtKB:O95967, ECO:0000269|PubMed:10380882}. +Q501P1 FBLN7_MOUSE Fibulin-7 (FIBL-7) (Protein TM14) 440 47,927 Chain (1); Coiled coil (1); Disulfide bond (11); Domain (4); Frameshift (2); Glycosylation (2); Sequence conflict (4); Signal peptide (1) FUNCTION: An adhesion molecule that interacts with extracellular matrix molecules in developing teeth and may play important roles in differentiation and maintenance of odontoblasts as well as in dentin formation. {ECO:0000269|PubMed:17699513}. PTM: N-glycosylated. {ECO:0000269|PubMed:17699513}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SUBUNIT: Interacts with heparin, FBLN1, FN1 and DSPP. Preferentially binds dental mesenchyme cells and odontoblasts but not dental epithelial cells or nondental cells. Binding requires a heparan sulfate-containing receptor on the cell surface as well as an integrin. {ECO:0000269|PubMed:17699513}. TISSUE SPECIFICITY: Highly expressed in newborn incisors and molars. A weaker expression is seen in the brain, kidneys, muscles and bones. {ECO:0000269|PubMed:17699513}. +Q8K3B1 FBSP1_MOUSE F-box/SPRY domain-containing protein 1 (F-box only protein 45) (mFbxo45) 286 30,605 Chain (1); Domain (2); Initiator methionine (1); Modified residue (1); Mutagenesis (1); Sequence conflict (1) Protein modification; protein ubiquitination. FUNCTION: Component of E3 ubiquitin ligase complexes. Required for normal neuromuscular synaptogenesis, axon pathfinding and neuronal migration. Plays a role in the regulation of neurotransmission at mature neurons (By similarity). May control synaptic activity by controlling UNC13A via ubiquitin dependent pathway. Specifically recognizes TP73, promoting its ubiquitination and degradation (By similarity). {ECO:0000250, ECO:0000269|PubMed:19398581}. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane {ECO:0000250}. Cell junction, synapse, presynaptic cell membrane {ECO:0000250}. SUBUNIT: Forms a complex with MYCBP2 and SKP1 but does not appear to form an authentic SCF (SKP1-CUL1-F-box protein) complex. Interacts (via B30.2/SPRY domain) with TP73 (via SAM domain); leading to its ubiquitination and degradation (By similarity). Interacts (via SRY domain) with UNC13A; leading to its degradation by the proteasome. {ECO:0000250, ECO:0000269|PubMed:19398581, ECO:0000269|PubMed:19996097}. TISSUE SPECIFICITY: Expressed speciffically in the central nervous system, including cerebellum, medulla oblongata, olfactory bulb, hippocampus, cortex and brain stem. {ECO:0000269|PubMed:19398581, ECO:0000269|PubMed:19996097}. +P35550 FBRL_MOUSE rRNA 2'-O-methyltransferase fibrillarin (EC 2.1.1.-) (Histone-glutamine methyltransferase) (Nucleolar protein 1) 327 34,307 Chain (1); Compositional bias (1); Cross-link (6); Modified residue (9); Region (4); Sequence conflict (4) FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that has the ability to methylate both RNAs and proteins. Involved in pre-rRNA processing by catalyzing the site-specific 2'-hydroxyl methylation of ribose moieties in pre-ribosomal RNA. Site specificity is provided by a guide RNA that base pairs with the substrate. Methylation occurs at a characteristic distance from the sequence involved in base pairing with the guide RNA. Also acts as a protein methyltransferase by mediating methylation of 'Gln-105' of histone H2A (H2AQ104me), a modification that impairs binding of the FACT complex and is specifically present at 35S ribosomal DNA locus (By similarity). {ECO:0000250}. PTM: By homology to other fibrillarins, some or all of the N-terminal domain arginines are modified to asymmetric dimethylarginine (DMA).; PTM: Ubiquitinated. Ubiquitination leads to proteasomal degradation. Deubiquitinated by USP36. {ECO:0000250|UniProtKB:P22087}. SUBCELLULAR LOCATION: Nucleus, nucleolus. Note=Fibrillar region of the nucleolus. SUBUNIT: Component of box C/D small nucleolar ribonucleoprotein (snoRNP) particles that contain SNU13, FBL, NOP5 and NOP56, plus a guide RNA. It is associated with the U3, U8, U13, X and Y small nuclear RNAs. Component of several ribosomal and nucleolar protein complexes. Interacts with PRMT5, NOLC1 and UTP20. Interacts with DDX5 and C1QBP. Interacts with NOL11. Interacts with PHI1D1. Interacts with RRP1B. {ECO:0000250|UniProtKB:P22087}. +Q8BJL1 FBX30_MOUSE F-box only protein 30 (Muscle ubiquitin ligase of SCF complex in atrophy-1) (MUSA1) 746 82,687 Chain (1); Domain (1); Erroneous initiation (1); Modified residue (1); Sequence conflict (4); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. Required for muscle atrophy following denervation. {ECO:0000269|PubMed:24076600}. PTM: Auto-ubiquitinated. {ECO:0000269|PubMed:24076600}.; PTM: May be neddylated. Neddylation may be required for E3 ligase activity, since it was observed only after purification with o-phenanthroline (PubMed:24076600). {ECO:0000269|PubMed:24076600}. SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex. Interacts with SKP1, CUL1 and RBX1/ROC1. {ECO:0000269|PubMed:24076600}. +Q5NBU5 FBX39_MOUSE F-box only protein 39 443 52,554 Chain (1); Domain (1) FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. {ECO:0000250}. SUBUNIT: Directly interacts with SKP1 and CUL1. {ECO:0000250}. +P26151 FCGR1_MOUSE High affinity immunoglobulin gamma Fc receptor I (IgG Fc receptor I) (Fc-gamma RI) (FcRI) (CD antigen CD64) 404 44,888 Chain (1); Disulfide bond (3); Domain (3); Glycosylation (5); Modified residue (2); Region (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 298 320 Helical. {ECO:0000255}. TOPO_DOM 25 297 Extracellular. {ECO:0000255}.; TOPO_DOM 321 404 Cytoplasmic. {ECO:0000255}. FUNCTION: High affinity receptor for the Fc region of immunoglobulins gamma. Functions in both innate and adaptive immune responses. {ECO:0000269|PubMed:11911823, ECO:0000269|PubMed:11911824}. PTM: N-glycosylated. {ECO:0000269|PubMed:8478020}.; PTM: Phosphorylated on serine residues. {ECO:0000269|PubMed:8478020}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Note=Stabilized at the cell membrane through interaction with FCER1G. {ECO:0000250}. SUBUNIT: Interacts with FCERG1; forms a functional signaling complex (By similarity). Interacts with FLNA; prevents FCGR1A degradation (By similarity). Interacts with EPB41L2, LAT and PPL. Interacts with HCK and LYN (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Macrophage-specific. +P62932 FBX40_MOUSE F-box only protein 40 710 79,951 Chain (1); Domain (1); Frameshift (1); Zinc finger (1) FUNCTION: Probable substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex that may function in myogenesis. {ECO:0000269|PubMed:17928169}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17928169}. SUBUNIT: Directly interacts with SKP1 and CUL1. {ECO:0000250}. TISSUE SPECIFICITY: Expressed only in heart and skeletal muscle. {ECO:0000269|PubMed:17928169}. +Q8CDI2 FBX43_MOUSE F-box only protein 43 (Endogenous meiotic inhibitor 2) 640 71,171 Beta strand (3); Chain (1); Domain (1); Modified residue (2); Sequence conflict (3); Turn (4); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: Required to establish and maintain the arrest of oocytes at the second meiotic metaphase until fertilization. Probably acts by inhibiting the anaphase-promoting complex/cyclosome (APC/C) ubiquitin ligase. Probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. {ECO:0000269|PubMed:16456547}. PTM: Phosphorylated on Thr-176 and Ser-275 in response to calcium, which is a prerequisite for ubiquitination and proteasomal degradation. {ECO:0000250}.; PTM: Ubiquitinated in response to calcium, which promotes proteasomal degradation. {ECO:0000250}. SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex (By similarity). Interacts with CDC20 (Probable). {ECO:0000250, ECO:0000305}. TISSUE SPECIFICITY: Present in testis and ovary (at protein level). Expression is high in immature oocytes, and diminishes after oocyte activation. {ECO:0000269|PubMed:16456547}. +Q8K285 FCHO1_MOUSE F-BAR domain only protein 1 873 95,122 Chain (1); Coiled coil (1); Domain (2); Modified residue (5); Region (3); Sequence conflict (1) FUNCTION: Functions in an early step of clathrin-mediated endocytosis. Has both a membrane binding/bending activity and the ability to recruit proteins essential to the formation of functional clathrin-coated pits. May regulate Bmp signaling by regulating clathrin-mediated endocytosis of Bmp receptors (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane, clathrin-coated pit {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Associated with forming but not mature clathrin-coated vesicles. The recruitment to coated-pits precede the one of clathrin and the adaptor protein complex AP-2 (By similarity). {ECO:0000250}. SUBUNIT: May oligomerize and form homotetramer. Interacts with AP2A2 and AP2B1; 2 subunits of the adaptor protein complex AP-2. Interacts with DAB2 (By similarity). Interacts with clathrin (CLTC or CLTCL1) (By similarity). Interacts with EPS15, EPS15R and ITSN1 (By similarity). Interacts with AGFG1 and CALM (By similarity). May interact with ACVR1; linking this receptor to clathrin-mediated endocytosis (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Mainly detected in brain and spleen. {ECO:0000269|PubMed:21762413}. +P53798 FDFT_MOUSE Squalene synthase (SQS) (SS) (EC 2.5.1.21) (FPP:FPP farnesyltransferase) (Farnesyl-diphosphate farnesyltransferase) 416 48,154 Chain (1); Sequence conflict (1); Transmembrane (2) TRANSMEM 284 304 Helical. {ECO:0000255}.; TRANSMEM 384 404 Helical. {ECO:0000255}. Terpene metabolism; lanosterol biosynthesis; lanosterol from farnesyl diphosphate: step 1/3. FUNCTION: Critical branch point enzyme of isoprenoid biosynthesis that is thought to regulate the flux of isoprene intermediates through the sterol pathway. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. +G3X9C2 FBX50_MOUSE F-box only protein 50 (NCC receptor protein 1) (NCCRP-1) (Non-specific cytotoxic cell receptor protein 1 homolog) 266 30,408 Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (1); Modified residue (5); Sequence conflict (1) FUNCTION: Promotes cell proliferation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. TISSUE SPECIFICITY: Strongly expressed in kidney. Weakly expressed in stomach, colon, duodenum and prostate. {ECO:0000269|PubMed:22087255}. +Q9Z2G0 FEM1B_MOUSE Protein fem-1 homolog B (FEM1b) (FEM1-beta) (Fem-1-like death receptor-binding protein alpha) (Fem-1-like in apoptotic pathway protein alpha) (F1A-alpha) (mt-Fem) 627 70,223 Chain (1); Repeat (9); Sequence conflict (4); Site (1) Protein modification; protein ubiquitination. FUNCTION: Component of an E3 ubiquitin-protein ligase complex, in which it may act as a substrate recognition subunit. Involved in apoptosis by acting as a death receptor-associated protein that mediates apoptosis. Also involved in glucose homeostasis in pancreatic islet. Functions as an adapter/mediator in replication stress-induced signaling that leads to the activation of CHEK1 (By similarity). {ECO:0000250, ECO:0000269|PubMed:16024793}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15601915}. Nucleus {ECO:0000250}. Note=Associated with chromatin. {ECO:0000250}. SUBUNIT: Homooligomer. Component of a probable ECS E3 ubiquitin-protein ligase complex containing CUL2, RBX1, ELOB, ELOC and FEM1B. Interacts with PPM1F and PHTF1. Interacts with the death domain of FAS/TNFRSF6 and TNFRSF1A (By similarity). Interacts with CHEK1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in pancreatic islets, within both beta cells and non-beta cells (at protein level). Highly expressed in adult testis. {ECO:0000269|PubMed:9828124}. +Q9CPW2 FDX2_MOUSE Ferredoxin-2, mitochondrial (Adrenodoxin-like protein) (Ferredoxin-1-like protein) 174 18,766 Alternative sequence (1); Chain (1); Domain (1); Frameshift (1); Metal binding (4); Sequence conflict (1); Transit peptide (1) FUNCTION: Essential for heme A and Fe/S protein biosynthesis. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. +Q3UY23 FDXA1_MOUSE Ferredoxin-fold anticodon-binding domain-containing protein 1 homolog (FDX-ACDB domain-containing protein 1) 622 70,120 Alternative sequence (3); Chain (1); Domain (1); Sequence conflict (1) +Q8VCK6 FFAR2_MOUSE Free fatty acid receptor 2 (G-protein coupled receptor 43) (Leukocyte-specific STAT-induced GPCR) 330 37,124 Chain (1); Compositional bias (1); Glycosylation (2); Mutagenesis (1); Topological domain (8); Transmembrane (7) TRANSMEM 9 29 Helical; Name=1. {ECO:0000255}.; TRANSMEM 44 64 Helical; Name=2. {ECO:0000255}.; TRANSMEM 80 100 Helical; Name=3. {ECO:0000255}.; TRANSMEM 127 147 Helical; Name=4. {ECO:0000255}.; TRANSMEM 185 205 Helical; Name=5. {ECO:0000255}.; TRANSMEM 220 240 Helical; Name=6. {ECO:0000255}.; TRANSMEM 256 276 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 8 Extracellular. {ECO:0000255}.; TOPO_DOM 30 43 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 65 79 Extracellular. {ECO:0000255}.; TOPO_DOM 101 126 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 148 184 Extracellular. {ECO:0000255}.; TOPO_DOM 206 219 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 241 255 Extracellular. {ECO:0000255}.; TOPO_DOM 277 330 Cytoplasmic. {ECO:0000255}. FUNCTION: G protein-coupled receptor that is activated by a major product of dietary fiber digestion, the short chain fatty acids (SCFAs), and that plays a role in the regulation of whole-body energy homeostasis and in intestinal immunity. In omnivorous mammals, the short chain fatty acids acetate, propionate and butyrate are produced primarily by the gut microbiome that metabolizes dietary fibers. SCFAs serve as a source of energy but also act as signaling molecules. That G protein-coupled receptor is probably coupled to the pertussis toxin-sensitive, G(i/o)-alpha family of G proteins but also to the Gq family (PubMed:23589301). Its activation results in the formation of inositol 1,4,5-trisphosphate, the mobilization of intracellular calcium, the phosphorylation of the MAPK3/ERK1 and MAPK1/ERK2 kinases and the inhibition of intracellular cAMP accumulation. May play a role in glucose homeostasis by regulating the secretion of GLP-1, in response to short-chain fatty acids accumulating in the intestine (PubMed:22190648, PubMed:23589301). May also regulate the production of LEP/Leptin, a hormone acting on the central nervous system to inhibit food intake (PubMed:20399779). Finally, may also regulate whole-body energy homeostasis through adipogenesis regulating both differentiation and lipid storage of adipocytes (PubMed:16123168, PubMed:23589301). In parallel to its role in energy homeostasis, may also mediate the activation of the inflammatory and immune responses by SCFA in the intestine, regulating the rapid production of chemokines and cytokines (PubMed:23665276). May also play a role in the resolution of the inflammatory response and control chemotaxis in neutrophils (PubMed:19917676, PubMed:19865172). In addition to SCFAs, may also be activated by the extracellular lectin FCN1 in a process leading to activation of monocytes and inducing the secretion of interleukin-8/IL-8 in response to the presence of microbes. {ECO:0000269|PubMed:12684041, ECO:0000269|PubMed:16123168, ECO:0000269|PubMed:18499755, ECO:0000269|PubMed:19865172, ECO:0000269|PubMed:19917676, ECO:0000269|PubMed:20399779, ECO:0000269|PubMed:22190648, ECO:0000269|PubMed:23589301, ECO:0000269|PubMed:23665276}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Interacts with FCN1 (via Fibrinogen C-terminal domain). {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in hematopoietic tissues, such as spleen and bone marrow, with highest levels in a subset of immune cells, including monocytes or neutrophils. Expressed in adipose tissues with high expression in differentiating adipocytes. Expressed by intestinal endocrine cells. {ECO:0000269|PubMed:12393494, ECO:0000269|PubMed:16123168, ECO:0000269|PubMed:22190648}. +Q9EQ21 HEPC_MOUSE Hepcidin 83 9,352 Disulfide bond (4); Peptide (1); Propeptide (1); Signal peptide (1) FUNCTION: Liver-produced hormone that constitutes the main circulating regulator of iron absorption and distribution across tissues. Acts by promoting endocytosis and degradation of ferroportin, leading to the retention of iron in iron-exporting cells and decreased flow of iron into plasma. Controls the major flows of iron into plasma: absorption of dietary iron in the intestine, recycling of iron by macrophages, which phagocytose old erythrocytes and other cells, and mobilization of stored iron from hepatocytes. {ECO:0000269|PubMed:11447267, ECO:0000269|PubMed:24880340}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11113132}. TISSUE SPECIFICITY: Highly expressed in the liver and to a much lesser extent in the heart. {ECO:0000269|PubMed:11113132, ECO:0000269|PubMed:12729891}. +P61329 FGF12_MOUSE Fibroblast growth factor 12 (FGF-12) (Fibroblast growth factor homologous factor 1) (FHF-1) (Myocyte-activating factor) 243 27,399 Alternative sequence (1); Chain (1); Motif (1); Sequence conflict (2) FUNCTION: Involved in nervous system development and function. Promote neuronal excitability by elevating the voltage dependence of neuronal sodium channel SCN8A fast inactivation. {ECO:0000250|UniProtKB:P61328}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Interacts with the C-terminal region of SCN9A. {ECO:0000250}. +Q8BY35 FGD2_MOUSE FYVE, RhoGEF and PH domain-containing protein 2 655 74,634 Chain (1); Domain (3); Erroneous gene model prediction (1); Frameshift (1); Modified residue (5); Mutagenesis (4); Sequence caution (1); Sequence conflict (4); Zinc finger (1) FUNCTION: Activates CDC42, a member of the Ras-like family of Rho- and Rac proteins, by exchanging bound GDP for free GTP. Activates JNK1 via CDC42 but not RAC1. Binds to phosphatidylinositol 4,5-bisphosphate, phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 5-monophosphate, phosphatidylinositol 4-monophosphate and phosphatidylinositol 3-monophosphate. {ECO:0000269|Ref.2}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|Ref.2}. Nucleus {ECO:0000269|Ref.2}. Early endosome {ECO:0000269|Ref.2}. Early endosome membrane {ECO:0000269|Ref.2}. Cell projection, ruffle membrane {ECO:0000269|Ref.2}. Cytoplasm, cytoskeleton {ECO:0000305|Ref.2}. Note=Recruitment to the endosome and ruffle membrane requires the presence of phosphoinositides. DOMAIN: The FYVE-type zinc-finger is necessary for early endosome localization. Recruitment to endosomal membranes via this domain requires the presence of phosphatidylinositol 3-phosphate or other phosphatidylinositides. {ECO:0000269|Ref.2}.; DOMAIN: The PH domain is necessary for localization to the ruffle membrane. Recruitment to ruffle membrane occurs through binding of phosphoinositides by the PH domain. This domain also contributes to the lipid-binding properties of the protein. {ECO:0000269|Ref.2}.; DOMAIN: The DH domain is necessary for its ability to activate JNK1 via CDC42. {ECO:0000269|Ref.2}. TISSUE SPECIFICITY: Lymph node, spleen, B-lymphocytes and macrophages (at protein level). Expressed at high levels in lymph node, spleen, B-lymphocytes and bone marrow macrophages. Expressed at lower levels in mature bone marrow dendritic cells. In both immature and mature B-cells, expression is down-regulated by prior B-cell receptor signaling. Expression remains high in resting B and memory cells but declines upon differentiation into plasma cells. {ECO:0000269|PubMed:10458911, ECO:0000269|Ref.2}. +O89101 FGF18_MOUSE Fibroblast growth factor 18 (FGF-18) (zFGF5) 207 23,921 Chain (1); Disulfide bond (1); Glycosylation (2); Signal peptide (1) FUNCTION: Plays an important role in the regulation of cell proliferation, cell differentiation and cell migration. Required for normal ossification and bone development. Stimulates hepatic and intestinal proliferation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Interacts with FGFR3 and FGFR4. {ECO:0000250}. +P05524 FGF3_MOUSE Fibroblast growth factor 3 (FGF-3) (Heparin-binding growth factor 3) (HBGF-3) (Proto-oncogene Int-2) 245 27,214 Alternative sequence (1); Chain (1); Erroneous initiation (1); Glycosylation (1); Mutagenesis (1); Signal peptide (1) FUNCTION: Plays an important role in the regulation of embryonic development, cell proliferation, and cell differentiation. Required for normal ear development (By similarity). {ECO:0000250}. PTM: Glycosylated. SUBCELLULAR LOCATION: Isoform 1: Nucleus.; SUBCELLULAR LOCATION: Isoform 2: Endoplasmic reticulum. Golgi apparatus. SUBUNIT: Interacts with FGFR1 and FGFR2. Affinity between fibroblast growth factors (FGFs) and their receptors is increased by heparan sulfate glycosaminoglycans that function as coreceptors (By similarity). {ECO:0000250}. +Q61657 HES3_MOUSE Transcription factor HES-3 (Hairy and enhancer of split 3) 175 19,294 Chain (1); Compositional bias (1); Domain (2); Motif (1); Sequence conflict (4) FUNCTION: Transcriptional repressor of genes that require a bHLH protein for their transcription. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Transcription repression requires formation of a complex with a corepressor protein of the Groucho/TLE family. {ECO:0000250}. DOMAIN: Has a particular type of basic domain (presence of a helix-interrupting proline) that binds to the N-box (CACNAG), rather than the canonical E-box (CANNTG).; DOMAIN: The C-terminal WRPW motif is a transcriptional repression domain necessary for the interaction with Groucho/TLE family members, transcriptional corepressors recruited to specific target DNA by Hairy-related proteins. {ECO:0000250}. +Q9ESL9 FGF20_MOUSE Fibroblast growth factor 20 (FGF-20) 211 23,614 Chain (1); Sequence conflict (4) FUNCTION: Neurotrophic factor that regulates central nervous development and function. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Homodimer. Interacts with FGFR2 and FGFR4. Affinity between fibroblast growth factors (FGFs) and their receptors is increased by heparan sulfate glycosaminoglycans that function as coreceptors (By similarity). {ECO:0000250}. +Q6P6L0 FIL1L_MOUSE Filamin A-interacting protein 1-like (Protein down-regulated in ovarian cancer 1 homolog) (DOC-1) 1131 129,772 Alternative sequence (3); Chain (1); Coiled coil (2); Erroneous initiation (3); Modified residue (4); Sequence caution (1); Sequence conflict (4) FUNCTION: Acts as a regulator of the antiangiogenic activity on endothelial cells. When overexpressed in endothelial cells, leads to inhibition of cell proliferation and migration and an increase in apoptosis. Inhibits melanoma growth When expressed in tumor-associated vasculature (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}. Nucleus {ECO:0000250}. +Q2VIS4 FILA2_MOUSE Filaggrin-2 (FLG-2) (Intermediate filament-associated protein) 2362 251,372 Calcium binding (1); Chain (1); Compositional bias (3); Domain (2); Erroneous initiation (1); Modified residue (30); Region (1); Repeat (12); Sequence conflict (1) PTM: Deiminated by PADI1, PADI2 or PADI3 in vitro. The deiminated form is degraded by calpain-1/CAPN1 more quickly and into shorter peptides than the intact protein. {ECO:0000250|UniProtKB:Q5D862}.; PTM: May be processed by calpain-1/CAPN1. {ECO:0000250|UniProtKB:Q5D862}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q5D862}. Cytoplasmic granule {ECO:0000250|UniProtKB:Q5D862}. +P12804 FGL2_MOUSE Fibroleukin (Cytotoxic T-lymphocyte-specific protein) (Fibrinogen-like protein 2) (Prothrombinase) 432 48,951 Chain (1); Coiled coil (1); Disulfide bond (2); Domain (1); Glycosylation (5); Sequence conflict (1); Signal peptide (1) FUNCTION: Converts prothrombin to thrombin. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Homotetramer; disulfide-linked. {ECO:0000250}. TISSUE SPECIFICITY: Constitutively expressed in cytotoxic T-cells. +Q9R059 FHL3_MOUSE Four and a half LIM domains protein 3 (FHL-3) (Skeletal muscle LIM-protein 2) (SLIM-2) 289 31,795 Chain (1); Domain (4); Initiator methionine (1); Modified residue (3); Sequence conflict (12); Zinc finger (1) TISSUE SPECIFICITY: In the adult, expressed at high levels in skeletal muscle and, to a lesser extent, in heart, lung, skin and kidney. During embryonic development, expressed ubiquitously at low levels. {ECO:0000269|PubMed:10049693, ECO:0000269|PubMed:10906474}. +O35732 CFLAR_MOUSE CASP8 and FADD-like apoptosis regulator (Caspase homolog) (CASH) (Caspase-eight-related protein) (Casper) (Caspase-like apoptosis regulatory protein) (CLARP) (Cellular FLICE-like inhibitory protein) (c-FLIP) (FADD-like antiapoptotic molecule 1) (FLAME-1) (Inhibitor of FLICE) (I-FLICE) (MACH-related inducer of toxicity) (MRIT) (Usurpin) [Cleaved into: CASP8 and FADD-like apoptosis regulator subunit p43; CASP8 and FADD-like apoptosis regulator subunit p12] 481 54,875 Alternative sequence (2); Chain (2); Compositional bias (1); Domain (2); Region (1); Sequence conflict (2) FUNCTION: Apoptosis regulator protein which may function as a crucial link between cell survival and cell death pathways in mammalian cells. Acts as an inhibitor of TNFRSF6 mediated apoptosis. A proteolytic fragment (p43) is likely retained in the death-inducing signaling complex (DISC) thereby blocking further recruitment and processing of caspase-8 at the complex. Full length and shorter isoforms have been shown either to induce apoptosis or to reduce TNFRSF-triggered apoptosis. Lacks enzymatic (caspase) activity (By similarity). {ECO:0000250, ECO:0000269|PubMed:10602037, ECO:0000269|PubMed:10894163}. PTM: Proteolytically processed; probably by caspase-8. Processing likely occurs at the DISC and generates subunit p43 and p12 (By similarity). {ECO:0000250}. SUBUNIT: TNFRSF6 stimulation triggers recruitment to the death-inducing signaling complex (DISC) formed by TNFRSF6, FADD and caspase-8. A proteolytic fragment (p43) stays associated with the DISC (By similarity). {ECO:0000250}. DOMAIN: The caspase domain lacks the active site residues involved in catalysis. TISSUE SPECIFICITY: Highly expressed in heart. +Q9Z0F5 CH25H_MOUSE Cholesterol 25-hydroxylase (EC 1.14.99.38) (Cholesterol 25-monooxygenase) (m25OH) 298 34,672 Chain (1); Domain (1); Glycosylation (2); Motif (3); Mutagenesis (1); Sequence conflict (3); Transmembrane (3) TRANSMEM 38 58 Helical. {ECO:0000255}.; TRANSMEM 88 108 Helical. {ECO:0000255}.; TRANSMEM 124 144 Helical. {ECO:0000255}. FUNCTION: Catalyzes the formation of 25-hydroxycholesterol from cholesterol, leading to repress cholesterol biosynthetic enzymes (PubMed:9852097). Plays a key role in cell positioning and movement in lymphoid tissues: 25-hydroxycholesterol is an intermediate in biosynthesis of 7-alpha,25-dihydroxycholesterol (7-alpha,25-OHC), an oxysterol that acts as a ligand for the G protein-coupled receptor GPR183/EBI2, a chemotactic receptor for a number of lymphoid cells (PubMed:22999953). May play an important role in regulating lipid metabolism by synthesizing a corepressor that blocks sterol regulatory element binding protein (SREBP) processing (PubMed:9852097). In testis, production of 25-hydroxycholesterol by macrophages may play a role in Leydig cell differentiation (PubMed:9852097). {ECO:0000269|PubMed:22999953, ECO:0000269|PubMed:9852097}. PTM: N-glycosylated. {ECO:0000269|PubMed:9852097}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:9852097}; Multi-pass membrane protein {ECO:0000269|PubMed:9852097}. TISSUE SPECIFICITY: Widely expressed at low level and at higher level in the lung. Weakly expressed in the heart, lung and kidney. {ECO:0000269|PubMed:9852097}. +Q9D6G9 CKLF5_MOUSE CKLF-like MARVEL transmembrane domain-containing protein 5 (Chemokine-like factor superfamily member 5) 156 17,389 Alternative sequence (1); Chain (1); Domain (1); Transmembrane (4) TRANSMEM 35 55 Helical. {ECO:0000255}.; TRANSMEM 56 76 Helical. {ECO:0000255}.; TRANSMEM 93 113 Helical. {ECO:0000255}.; TRANSMEM 119 139 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. +Q9CZR4 CKLF8_MOUSE CKLF-like MARVEL transmembrane domain-containing protein 8 (Chemokine-like factor superfamily member 8) 173 19,527 Chain (1); Domain (1); Transmembrane (4) TRANSMEM 41 61 Helical. {ECO:0000255}.; TRANSMEM 70 90 Helical. {ECO:0000255}.; TRANSMEM 105 125 Helical. {ECO:0000255}.; TRANSMEM 147 167 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. +Q9DAS1 CKLF_MOUSE Chemokine-like factor 152 17,254 Alternative sequence (4); Chain (1); Domain (1); Sequence caution (1); Transmembrane (4) TRANSMEM 19 39 Helical. {ECO:0000255}.; TRANSMEM 46 66 Helical. {ECO:0000255}.; TRANSMEM 81 101 Helical. {ECO:0000255}.; TRANSMEM 108 128 Helical. {ECO:0000255}. FUNCTION: May play an important role in inflammation and regeneration of skeletal muscle. {ECO:0000250|UniProtKB:Q9UBR5}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q91YN0 CL004_MOUSE Protein C12orf4 homolog 552 63,644 Chain (1); Modified residue (1) FUNCTION: Plays a role in mast cell degranulation. {ECO:0000250|UniProtKB:D4A770}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:D4A770}. +Q9CX66 CL045_MOUSE Uncharacterized protein C12orf45 homolog 185 19,967 Chain (1); Modified residue (3); Sequence conflict (1) +Q8BTG6 CL049_MOUSE UPF0454 protein C12orf49 homolog 205 23,477 Chain (1); Compositional bias (1); Glycosylation (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q8R1G2 CMBL_MOUSE Carboxymethylenebutenolidase homolog (EC 3.1.-.-) 245 27,902 Active site (3); Chain (1); Frameshift (1); Initiator methionine (1); Modified residue (2); Sequence conflict (3) FUNCTION: Cysteine hydrolase. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. +Q8BH59 CMC1_MOUSE Calcium-binding mitochondrial carrier protein Aralar1 (Mitochondrial aspartate glutamate carrier 1) (Solute carrier family 25 member 12) 677 74,570 Calcium binding (3); Chain (1); Domain (4); Initiator methionine (1); Metal binding (5); Modified residue (1); Region (4); Repeat (3); Transmembrane (6) TRANSMEM 330 347 Helical; Name=1. {ECO:0000250|UniProtKB:O75746}.; TRANSMEM 391 410 Helical; Name=2. {ECO:0000250|UniProtKB:O75746}.; TRANSMEM 434 447 Helical; Name=3. {ECO:0000250|UniProtKB:O75746}.; TRANSMEM 483 502 Helical; Name=4. {ECO:0000250|UniProtKB:O75746}.; TRANSMEM 522 539 Helical; Name=5. {ECO:0000250|UniProtKB:O75746}.; TRANSMEM 579 598 Helical; Name=6. {ECO:0000250|UniProtKB:O75746}. FUNCTION: Mitochondrial and calcium-binding carrier that catalyzes the calcium-dependent exchange of cytoplasmic glutamate with mitochondrial aspartate across the mitochondrial inner membrane. May have a function in the urea cycle. {ECO:0000250|UniProtKB:O75746}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:O75746}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O75746}. SUBUNIT: Homodimer (via N-terminus). {ECO:0000250|UniProtKB:O75746}. DOMAIN: Upon calcium binding, the EF-hand-containing regulatory N-terminal domain binds to the C-terminal domain, opening a vestibule which allows the substrates to be translocated through the carrier domain. In the absence of calcium, the linker loop domain may close the vestibule, which may prevent substrates from entering the carrier domain. {ECO:0000250|UniProtKB:O75746}. +Q9QXX4 CMC2_MOUSE Calcium-binding mitochondrial carrier protein Aralar2 (Citrin) (Mitochondrial aspartate glutamate carrier 2) (Solute carrier family 25 member 13) 676 74,467 Calcium binding (3); Chain (1); Domain (4); Initiator methionine (1); Metal binding (4); Modified residue (10); Region (4); Repeat (3); Sequence conflict (2); Transmembrane (6) TRANSMEM 333 350 Helical; Name=1. {ECO:0000250|UniProtKB:O75746}.; TRANSMEM 394 413 Helical; Name=2. {ECO:0000250|UniProtKB:O75746}.; TRANSMEM 437 450 Helical; Name=3. {ECO:0000250|UniProtKB:O75746}.; TRANSMEM 486 505 Helical; Name=4. {ECO:0000250|UniProtKB:O75746}.; TRANSMEM 525 542 Helical; Name=5. {ECO:0000250|UniProtKB:O75746}.; TRANSMEM 582 601 Helical; Name=6. {ECO:0000250|UniProtKB:O75746}. FUNCTION: Mitochondrial and calcium-binding carrier that catalyzes the calcium-dependent exchange of cytoplasmic glutamate with mitochondrial aspartate across the mitochondrial inner membrane. May have a function in the urea cycle. {ECO:0000250|UniProtKB:Q9UJS0}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9UJS0}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9UJS0}. SUBUNIT: Homodimer (via N-terminus). {ECO:0000250|UniProtKB:Q9UJS0}. DOMAIN: Upon calcium binding, the EF-hand-containing regulatory N-terminal domain binds to the C-terminal domain, opening a vestibule which allows the substrates to be translocated through the carrier domain (By similarity). In the absence of calcium, the helix loop domain may close the vestibule, which may prevent substrates from entering the carrier domain (By similarity). {ECO:0000250|UniProtKB:O75746, ECO:0000250|UniProtKB:Q9UJS0}. TISSUE SPECIFICITY: At E10.5, expressed in branchial arches, a well as in the limb and tail buds. At E13.5 expression is predominant in epithelial structures and the forebrain, kidney and liver. Expression in liver is maintained into adulthood. {ECO:0000269|PubMed:10610724}. +Q61908 CMC4_MOUSE Cx9C motif-containing protein 4 (Mature T-cell proliferation 1 neighbor protein) (Mature T-cell proliferation-1 type A) (MTCP-1 type A) (Protein p8 MTCP-1) (p8MTCP1) 68 7,743 Chain (1); Compositional bias (1); Disulfide bond (3); Domain (1); Motif (2) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:7784073}. DOMAIN: The twin Cx9C motifs are involved in the recognition by the mitochondrial disulfide relay system. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in many tissues. +Q8BUG2 CNDP1_MOUSE Beta-Ala-His dipeptidase (EC 3.4.13.20) (CNDP dipeptidase 1) (Carnosine dipeptidase 1) 492 55,090 Active site (2); Chain (1); Metal binding (6); Modified residue (1); Sequence conflict (1) SUBUNIT: Homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Detected exclusively in kidney. {ECO:0000269|PubMed:12473676}. +Q6PCW6 CNFN_MOUSE Cornifelin 111 12,302 Chain (1); Compositional bias (1) FUNCTION: Part of the insoluble cornified cell envelope (CE) of stratified squamous epithelia. {ECO:0000269|PubMed:15147942}. SUBCELLULAR LOCATION: Cytoplasm. Note=Constituent of the scaffolding of the cornified envelope. {ECO:0000250}. SUBUNIT: Directly or indirectly cross-linked to CE proteins loricin and involucrin (IVL). +Q9JJZ8 CNGA3_MOUSE Cyclic nucleotide-gated cation channel alpha-3 (Cone photoreceptor cGMP-gated channel subunit alpha) (Cyclic nucleotide-gated channel alpha-3) (CNG channel alpha-3) (CNG-3) (CNG3) 631 72,702 Binding site (2); Chain (1); Coiled coil (1); Nucleotide binding (1); Sequence conflict (2); Transmembrane (3) TRANSMEM 112 133 Helical. {ECO:0000255}.; TRANSMEM 244 264 Helical. {ECO:0000255}.; TRANSMEM 320 340 Helical. {ECO:0000255}. FUNCTION: Visual signal transduction is mediated by a G-protein coupled cascade using cGMP as second messenger. This protein can be activated by cyclic GMP which leads to an opening of the cation channel and thereby causing a depolarization of cone photoreceptors. Essential for the generation of light-evoked electrical responses in the red-, green- and blue sensitive cones (By similarity). Induced a flickering channel gating, weakened the outward rectification in the presence of extracellular calcium, increased sensitivity for L-cis diltiazem and enhanced the cAMP efficacy of the channel when coexpressed with CNGB3. {ECO:0000250, ECO:0000269|PubMed:10662822}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SUBUNIT: Tetramer formed of three CNGA3 and one CNGB3 modulatory subunits. {ECO:0000250}. DOMAIN: The C-terminal coiled-coil domain mediates homotrimerization of CNGA subunits. {ECO:0000250}. TISSUE SPECIFICITY: Prominently expressed in retina. +Q3UW12 CNGA4_MOUSE Cyclic nucleotide-gated cation channel alpha-4 (Cyclic nucleotide-gated channel alpha-4) (CNG channel alpha-4) (CNG-4) (CNG4) 575 65,835 Alternative sequence (1); Chain (1); Coiled coil (1); Motif (1); Nucleotide binding (1); Topological domain (7); Transmembrane (6) TRANSMEM 34 54 Helical; Name=H1. {ECO:0000255}.; TRANSMEM 66 86 Helical; Name=H2. {ECO:0000255}.; TRANSMEM 113 133 Helical; Name=H3. {ECO:0000255}.; TRANSMEM 169 189 Helical; Name=H4. {ECO:0000255}.; TRANSMEM 219 239 Helical; Name=H5. {ECO:0000255}.; TRANSMEM 245 265 Helical; Name=H6. {ECO:0000255}. TOPO_DOM 1 33 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 55 65 Extracellular. {ECO:0000255}.; TOPO_DOM 87 112 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 134 168 Extracellular. {ECO:0000255}.; TOPO_DOM 190 218 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 240 244 Extracellular. {ECO:0000255}.; TOPO_DOM 266 575 Cytoplasmic. {ECO:0000255}. FUNCTION: Second messenger, cAMP, causes the opening of cation-selective cyclic nucleotide-gated (CNG) channels and depolarization of the neuron (olfactory sensory neurons, OSNs). CNGA4 is the modulatory subunit of this channel which is known to play a central role in the transduction of odorant signals and subsequent adaptation. By accelerating the calcium-mediated negative feedback in olfactory signaling it allows rapid adaptation to odor stimulation and extends its range of odor detection. {ECO:0000269|PubMed:11739959, ECO:0000269|PubMed:12649326}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Heterotetramer composed of two subunits of CNGA2, one of CNGA4 and one of CNGB1b. The complex forms the cyclic nucleotide-gated (CNG) channel of olfactory neurons (By similarity). {ECO:0000250}. DOMAIN: The C-terminal coiled-coil domain mediates trimerization of CNGA subunits. {ECO:0000250}. +Q7TQ07 DPOLN_MOUSE DNA polymerase nu (EC 2.7.7.7) 864 96,675 Alternative sequence (1); Chain (1); Erroneous initiation (2) FUNCTION: DNA polymerase with very low fidelity that catalyzes considerable misincorporation by inserting dTTP opposite a G template, and dGTP opposite a T template. Is the least accurate of the DNA polymerase A family (i.e. POLG, POLN and POLQ). Can perform accurate translesion DNA synthesis (TLS) past a 5S-thymine glycol. Can perform efficient strand displacement past a nick or a gap and gives rise to an amount of product similar to that on non-damaged template. Has no exonuclease activity. Error-prone DNA polymerase that preferentially misincorporates dT regardless of template sequence. May play a role in TLS during interstrand cross-link (ICL) repair. May be involved in TLS when genomic replication is blocked by extremely large major groove DNA lesions. May function in the bypass of some DNA-protein and DNA-DNA cross-links. May have a role in cellular tolerance to DNA cross-linking agents. Involved in the repair of DNA cross-links and double-strand break (DSB) resistance. Participates in FANCD2-mediated repair. Forms a complex with HELQ helicase that participates in homologous recombination (HR) repair and is essential for cellular protection against DNA cross-links. {ECO:0000250|UniProtKB:Q7Z5Q5}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q7Z5Q5}. SUBUNIT: Interacts with FANCD2, FANCI, PCNA, RAD51 and HELQ. {ECO:0000250|UniProtKB:Q7Z5Q5}. TISSUE SPECIFICITY: Expressed only in testis namely in primary spermatocytes and in round spermatids. {ECO:0000269|PubMed:12794064}. +Q6NXK7 DPP10_MOUSE Inactive dipeptidyl peptidase 10 (Dipeptidyl peptidase X) (DPP X) 797 90,827 Chain (1); Erroneous initiation (1); Glycosylation (8); Modified residue (2); Topological domain (2); Transmembrane (1) TRANSMEM 35 55 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 34 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 56 797 Extracellular. {ECO:0000255}. FUNCTION: Promotes cell surface expression of the potassium channel KCND2 (PubMed:22311982). Modulates the activity and gating characteristics of the potassium channel KCND2 (PubMed:22311982). Has no dipeptidyl aminopeptidase activity (Probable). {ECO:0000250|UniProtKB:Q8N608, ECO:0000269|PubMed:22311982, ECO:0000305}. PTM: N-glycosylation is important for cell surface expression, specially at Asn-258, which is crucial. {ECO:0000250|UniProtKB:Q8N608}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22311982}; Single-pass type II membrane protein {ECO:0000305}. SUBUNIT: May form oligomers. Interacts with KCND1 and KCND2 (By similarity). {ECO:0000250|UniProtKB:Q8N608}. TISSUE SPECIFICITY: Detected in brain cortex (at protein level) (PubMed:22311982). Expressed in the brain, predominantly by neurons and not by glia. {ECO:0000269|PubMed:15671030, ECO:0000269|PubMed:22311982}. +Q9ET22 DPP2_MOUSE Dipeptidyl peptidase 2 (EC 3.4.14.2) (Dipeptidyl aminopeptidase II) (Dipeptidyl peptidase 7) (Dipeptidyl peptidase II) (DPP II) (Quiescent cell proline dipeptidase) 506 56,254 Active site (3); Chain (1); Glycosylation (6); Propeptide (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Plays an important role in the degradation of some oligopeptides. SUBCELLULAR LOCATION: Lysosome {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Secreted {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +Q99KK7 DPP3_MOUSE Dipeptidyl peptidase 3 (EC 3.4.14.4) (Dipeptidyl aminopeptidase III) (Dipeptidyl arylamidase III) (Dipeptidyl peptidase III) (DPP III) (Enkephalinase B) 738 82,898 Active site (1); Chain (1); Initiator methionine (1); Metal binding (3); Modified residue (1); Sequence conflict (3) FUNCTION: Cleaves and degrades bioactive peptides, including angiotensin, Leu-enkephalin and Met-enkephalin. Also cleaves Arg-Arg-beta-naphthylamide (in vitro). {ECO:0000250|UniProtKB:Q9NY33}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9NY33}. +P28843 DPP4_MOUSE Dipeptidyl peptidase 4 (EC 3.4.14.5) (Dipeptidyl peptidase IV) (DPP IV) (T-cell activation antigen CD26) (Thymocyte-activating molecule) (THAM) (CD antigen CD26) [Cleaved into: Dipeptidyl peptidase 4 membrane form (Dipeptidyl peptidase IV membrane form); Dipeptidyl peptidase 4 soluble form (Dipeptidyl peptidase IV soluble form)] 760 87,437 Active site (3); Chain (2); Compositional bias (1); Disulfide bond (5); Glycosylation (9); Topological domain (2); Transmembrane (1) TRANSMEM 7 28 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 29 760 Extracellular. {ECO:0000255}. FUNCTION: Cell surface glycoprotein receptor involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Acts as a positive regulator of T-cell coactivation, by binding at least ADA, CAV1, IGF2R, and PTPRC. Its binding to CAV1 and CARD11 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. Its interaction with ADA also regulates lymphocyte-epithelial cell adhesion. In association with FAP is involved in the pericellular proteolysis of the extracellular matrix (ECM), the migration and invasion of endothelial cells into the ECM. May be involved in the promotion of lymphatic endothelial cells adhesion, migration and tube formation. When overexpressed, enhanced cell proliferation, a process inhibited by GPC3. Acts also as a serine exopeptidase with a dipeptidyl peptidase activity that regulates various physiological processes by cleaving peptides in the circulation, including many chemokines, mitogenic growth factors, neuropeptides and peptide hormones. Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline. {ECO:0000250|UniProtKB:P27487}. PTM: The soluble form (Dipeptidyl peptidase 4 soluble form also named SDPP) derives from the membrane form (Dipeptidyl peptidase 4 membrane form also named MDPP) by proteolytic processing. {ECO:0000250}.; PTM: N- and O-Glycosylated. {ECO:0000250}.; PTM: Phosphorylated. Mannose 6-phosphate residues in the carbohydrate moiety are necessary for interaction with IGF2R in activated T-cells. Mannose 6-phosphorylation is induced during T-cell activation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Dipeptidyl peptidase 4 soluble form: Secreted. Note=Detected in the serum and the seminal fluid. {ECO:0000250}.; SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein. Apical cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Cell projection, invadopodium membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Cell projection, lamellipodium membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Cell junction {ECO:0000250}. Membrane raft {ECO:0000250}. Note=Translocated to the apical membrane through the concerted action of N- and O-Glycans and its association with lipid microdomains containing cholesterol and sphingolipids. Redistributed to membrane rafts in T-cell in a interleukin-12-dependent activation. Its interaction with CAV1 is necessary for its translocation to membrane rafts. Colocalized with PTPRC in membrane rafts. Colocalized with FAP in invadopodia and lamellipodia of migratory activated endothelial cells in collagenous matrix. Colocalized with FAP on endothelial cells of capillary-like microvessels but not large vessels within invasive breast ductal carcinoma. Colocalized with ADA at the cell junction in lymphocyte-epithelial cell adhesion. Colocalized with IGF2R in internalized cytoplasmic vesicles adjacent to the cell surface (By similarity). {ECO:0000250}. SUBUNIT: Monomer. Homodimer. Heterodimer with Seprase (FAP). Requires homodimerization for optimal dipeptidyl peptidase activity and T-cell costimulation. Found in a membrane raft complex, at least composed of BCL10, CARD11, DPP4 and IKBKB. Associates with collagen. Interacts with PTPRC; the interaction is enhanced in a interleukin-12-dependent manner in activated lymphocytes. Interacts (via extracellular domain) with ADA; does not inhibit its dipeptidyl peptidase activity. Interacts with CAV1 (via the N-terminus); the interaction is direct. Interacts (via cytoplasmic tail) with CARD11 (via PDZ domain); its homodimerization is necessary for interaction with CARD11. Interacts with IGF2R; the interaction is direct. Interacts with GPC3. {ECO:0000250|UniProtKB:P27487}. +Q9Z218 DPP6_MOUSE Dipeptidyl aminopeptidase-like protein 6 (DPPX) (Dipeptidyl aminopeptidase-related protein) (Dipeptidyl peptidase 6) (Dipeptidyl peptidase IV-like protein) (Dipeptidyl peptidase VI) (DPP VI) 804 91,260 Chain (1); Disulfide bond (4); Glycosylation (8); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 35 55 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 34 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 56 804 Extracellular. {ECO:0000255}. FUNCTION: Promotes cell surface expression of the potassium channel KCND2 (PubMed:22311982). Modulates the activity and gating characteristics of the potassium channel KCND2 (PubMed:22311982). Has no dipeptidyl aminopeptidase activity (By similarity). {ECO:0000250|UniProtKB:P42658, ECO:0000269|PubMed:22311982}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:P42658}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22311982}; Single-pass type II membrane protein {ECO:0000305}. SUBUNIT: Homodimer (in vitro). Interacts with KCND2. Identified in a complex with KCND2 and KCNIP2. Forms an octameric complex composed of four DPP6 subunits bound to the KCND2 tetramer. {ECO:0000250|UniProtKB:P42658}. TISSUE SPECIFICITY: Detected in brain cortex (at protein level). {ECO:0000269|PubMed:22311982}. +Q80YA7 DPP8_MOUSE Dipeptidyl peptidase 8 (DP8) (EC 3.4.14.5) (Dipeptidyl peptidase VIII) (DPP VIII) 892 102,186 Active site (3); Chain (1); Sequence conflict (1) FUNCTION: Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. May play a role in T-cell activation and immune function (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +Q8BVG4 DPP9_MOUSE Dipeptidyl peptidase 9 (DP9) (EC 3.4.14.5) (Dipeptidyl peptidase IX) (DPP IX) (Dipeptidyl peptidase-like protein 9) (DPLP9) 862 98,001 Active site (3); Alternative sequence (3); Chain (1); Frameshift (1); Sequence conflict (3) FUNCTION: Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +Q9CWH0 DPPA2_MOUSE Developmental pluripotency-associated protein 2 (Embryonic stem cell-associated transcript 15-2 protein) (ECAT15-2) (Pluripotent embryonic stem cell-related gene 1 protein) 301 34,116 Chain (1); Domain (1) FUNCTION: Binds to target gene promoters, including NKX2-5 and SYCE1, but not GATA4, and may be involved in the maintenance of the active epigenetic status of these genes. {ECO:0000269|PubMed:21896782}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21896782}. SUBUNIT: Interacts with DPPA4. {ECO:0000269|PubMed:21896782}. TISSUE SPECIFICITY: Not detected in adult tissues. {ECO:0000269|PubMed:12620990}. +Q8QZY3 DPPA3_MOUSE Developmental pluripotency-associated protein 3 (Compaction-associated protein 1) (Primordial germ cell protein 7) 150 17,670 Chain (1); Mutagenesis (2); Region (2) FUNCTION: Primordial germ cell (PGCs)-specific protein involved in epigenetic chromatin reprogramming in the zygote following fertilization. In zygotes, DNA demethylation occurs selectively in the paternal pronucleus before the first cell division, while the adjacent maternal pronucleus and certain paternally-imprinted loci are protected from this process. Participates in protection of DNA methylation in the maternal pronucleus by preventing conversion of 5mC to 5hmC: specifically recognizes and binds histone H3 dimethylated at 'Lys-9' (H3K9me2) on maternal genome, and protects maternal genome from TET3-mediated conversion to 5hmC and subsequent DNA demethylation. Does not bind paternal chromatin, which is mainly packed into protamine and does not contain much H3K9me2 mark. Also protects imprinted loci that are marked with H3K9me2 in mature sperm from DNA demethylation in early embryogenesis. May be important for the totipotent/pluripotent states continuing through preimplantation development. Also involved in chromatin condensation in oocytogenesis. {ECO:0000269|PubMed:12124616, ECO:0000269|PubMed:12620990, ECO:0000269|PubMed:14654002, ECO:0000269|PubMed:17143267, ECO:0000269|PubMed:21407207, ECO:0000269|PubMed:22034526, ECO:0000269|PubMed:22722204}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Localized in the cytoplasm at the primary oocyte stage and in oocytes within mono-laminar follicles. Expressed in the nucleus and cytoplasm of oocytes in bi-laminar and Graafian follicles and during the 2-cell and morula stages. In E3.5 blastocysts localization is mainly nuclear. Mainly localizes in the female pronucleus, localization to the male pronucleus in much weaker. DOMAIN: Mediates binding to H3K9me2 via N-terminal region, while ability to exclude TET3 from the maternal pronucleus requires the C-terminal part. {ECO:0000269|PubMed:22722204}. TISSUE SPECIFICITY: Expressed in the immature oocytes and in newborn ovaries. Subsequently detected in maturing oocytes and in preimplantation embryos. Expressed in pluripotent embryonic but not in differentiated somatic cells. Expressed in blastocysts, epiblasts, primordial germ cells, embryonic gonads and primitive spermatogonia. No expression is detected in adult testes. {ECO:0000269|PubMed:11900980, ECO:0000269|PubMed:12124616, ECO:0000269|PubMed:12620990}. +Q8CCG4 DPPA4_MOUSE Developmental pluripotency-associated protein 4 (Embryonic stem cell-associated transcript 15-1 protein) (ECAT15-1) 296 32,699 Chain (1); Sequence conflict (7) FUNCTION: May be involved in the maintenance of active epigenetic status of target genes. May inhibit differentiation of embryonic stem (ES) cells into a primitive ectoderm lineage. {ECO:0000269|PubMed:17855347, ECO:0000269|PubMed:21896782}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17855347, ECO:0000269|PubMed:21896782}. Note=Associated with transcriptionally active chromatin. SUBUNIT: Interacts with DPPA2 (PubMed:21896782). Interacts with PCGF1 (By similarity). {ECO:0000250|UniProtKB:Q7L190, ECO:0000269|PubMed:21896782}. TISSUE SPECIFICITY: Expressed in pluripotent embryonic cells, but not in differentiated somatic tissues. {ECO:0000269|PubMed:12620990, ECO:0000269|PubMed:17855347, ECO:0000269|PubMed:21896782}. +Q33DR2 DPS1_MOUSE Decaprenyl-diphosphate synthase subunit 1 (EC 2.5.1.91) (All-trans-decaprenyl-diphosphate synthase subunit 1) (Decaprenyl pyrophosphate synthase subunit 1) (Solanesyl-diphosphate synthase subunit 1) (Trans-prenyltransferase 1) (TPT 1) 409 45,895 Binding site (9); Chain (1); Erroneous initiation (2); Metal binding (5); Sequence conflict (1) Cofactor biosynthesis; ubiquinone biosynthesis. FUNCTION: Supplies decaprenyl diphosphate, the precursor for the side chain of the isoprenoid quinones ubiquinone-10. {ECO:0000269|PubMed:16262699}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}. SUBUNIT: Heterotetramer of 2 DPS1/TPRT and 2 DLP1 subunits. {ECO:0000269|PubMed:16262699}. +Q570Y9 DPTOR_MOUSE DEP domain-containing mTOR-interacting protein (DEP domain-containing protein 6) 409 46,120 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (3); Erroneous initiation (1); Modified residue (15); Sequence conflict (4) FUNCTION: Negative regulator of the mTORC1 and mTORC2 signaling pathways. Inhibits the kinase activity of both complexes (By similarity). {ECO:0000250}. PTM: Phosphorylation weakens interaction with MTOR within mTORC1 and mTORC2. {ECO:0000250}.; PTM: Ubiquitinated; ubiquitination leads to proteasomal degradation. {ECO:0000250|UniProtKB:Q8TB45}. SUBUNIT: Part of the mammalian target of rapamycin complex 1 (mTORC1) which contains MTOR, MLST8, RPTOR, AKT1S1/PRAS40 and DEPTOR. Part of the mammalian target of rapamycin complex 2 (mTORC2) which contains MTOR, MLST8, PROTOR1, RICTOR, MAPKAP1 and DEPTOR. Interacts (via PDZ domain) with MTOR; interacts with MTOR within both mammalian target of rapamycin complexes mTORC1 and mTORC2 (By similarity). Interacts (via PDZ domain) with MINAR1 (via N-terminus) (By similarity). {ECO:0000250|UniProtKB:Q8TB45}. +Q99LT0 DPY30_MOUSE Protein dpy-30 homolog (Dpy-30-like protein) (Dpy-30L) 99 11,213 Chain (1); Cross-link (1); Modified residue (3) FUNCTION: As part of the MLL1/MLL complex, involved in the methylation of histone H3 at 'Lys-4', particularly trimethylation. Histone H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. May play some role in histone H3 acetylation. In embryonic stem (ES) cells, plays a crucial role in the differentiation potential, particularly along the neural lineage, regulating gene induction and histone H3 'Lys-4' methylation at key developmental loci, including that mediated by retinoic acid. Does not affect ES cell self-renewal. May also play an indirect or direct role in endosomal transport. {ECO:0000269|PubMed:21335234}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21335234}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Note=Associated with chromatin at regions enriched in histone H3 trimethylated at 'Lys-4'. Highly enriched in gene promoter regions and 5' UTRs, but not in downstream regions of genes or 3' UTRs. SUBUNIT: Homodimer. Core component of several methyltransferase-containing complexes including MLL1/MLL, MLL2/3 (also named ASCOM complex) and MLL4/WBP7. Each complex is at least composed of ASH2L, RBBP5, WDR5, DPY30, one or more specific histone methyltransferases (KMT2A/MLL1, KMT2D/MLL2, KMT2C/MLL3 and KMT2B/MLL4), and the facultative components MEN1, HCFC1, HCFC2, NCOA6, KDM6A, PAXIP1/PTIP, PAGR1 and alpha- and beta-tubulin PAXIP1/PTIP, PAGR1 and alpha- and beta-tubulin. Interacts with ASH2L. The interaction with ASH2L is direct (By similarity). Interacts with ARFGEF1 (By similarity). Component of the SET1 complex, at least composed of the catalytic subunit (SETD1A or SETD1B), WDR5, WDR82, RBBP5, ASH2L/ASH2, CXXC1/CFP1, HCFC1 and DPY30 (By similarity). {ECO:0000250}. +Q8CHR6 DPYD_MOUSE Dihydropyrimidine dehydrogenase [NADP(+)] (DHPDHase) (DPD) (EC 1.3.1.2) (Dihydrothymine dehydrogenase) (Dihydrouracil dehydrogenase) 1025 111,253 Active site (1); Binding site (8); Chain (1); Domain (3); Metal binding (16); Modified residue (2); Nucleotide binding (10); Region (2) Amino-acid biosynthesis; beta-alanine biosynthesis. FUNCTION: Involved in pyrimidine base degradation. Catalyzes the reduction of uracil and thymine (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +P97427 DPYL1_MOUSE Dihydropyrimidinase-related protein 1 (DRP-1) (Collapsin response mediator protein 1) (CRMP-1) (Unc-33-like phosphoprotein 3) (ULIP-3) 572 62,168 Beta strand (18); Chain (1); Helix (19); Modified residue (11); Sequence conflict (4); Turn (6) FUNCTION: Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance, invasive growth and cell migration. May participate in cytokinesis. {ECO:0000269|PubMed:14685275}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Associated with centrosomes and the mitotic spindle during metaphase. {ECO:0000250}. SUBUNIT: Homotetramer, and heterotetramer with DPYSL2, DPYSL3, DPYSL4 or DPYSL5. Interacts with PLXNA1. {ECO:0000269|PubMed:10956643, ECO:0000269|PubMed:14685275}. +O08553 DPYL2_MOUSE Dihydropyrimidinase-related protein 2 (DRP-2) (Unc-33-like phosphoprotein 2) (ULIP-2) 572 62,278 Beta strand (16); Chain (1); Helix (19); Modified residue (21); Mutagenesis (1); Sequence conflict (3); Turn (6) FUNCTION: Plays a role in neuronal development and polarity, as well as in axon growth and guidance, neuronal growth cone collapse and cell migration. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. May play a role in endocytosis. {ECO:0000269|PubMed:22057101}. PTM: Phosphorylation by DYRK2 at Ser-522 is required for subsequent phosphorylation by GSK3B (By similarity). Phosphorylation at Thr-514 by GSK3B abolishes tubulin-binding leading to destabilization of microtubule assembly in axons and neurodegeneration. {ECO:0000250, ECO:0000269|PubMed:22057101}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Membrane {ECO:0000250}. Note=Tightly but non-covalently associated with membranes. {ECO:0000250}. SUBUNIT: Homotetramer, and heterotetramer with CRMP1, DPYSL3, DPYSL4 or DPYSL5. Interacts through its C-terminus with the C-terminus of CYFIP1/SRA1. Interacts with HTR4. Interacts with CLN6. Interacts with MICALL1. {ECO:0000269|PubMed:10956643, ECO:0000269|PubMed:15466885, ECO:0000269|PubMed:9375656}. +Q62188 DPYL3_MOUSE Dihydropyrimidinase-related protein 3 (DRP-3) (Unc-33-like phosphoprotein 1) (ULIP-1) 570 61,936 Chain (1); Modified residue (11) FUNCTION: Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance, neuronal growth cone collapse and cell migration (By similarity). {ECO:0000250}. PTM: Phosphorylation on Ser-522 by DYRK2 promotes subsequent phosphorylation on Thr-509, Thr-514 and Ser-518 by GSK3. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell projection, growth cone {ECO:0000250}. Note=Colocalizes with synaptic vesicle protein 2 in the central region of the growth cone. {ECO:0000250}. SUBUNIT: Homotetramer, and heterotetramer with CRMP1, DPYSL2, DPYSL4 or DPYSL5. Interacts with synaptic vesicle protein 2 and SH3A domain of intersectin (By similarity). {ECO:0000250}. +O35098 DPYL4_MOUSE Dihydropyrimidinase-related protein 4 (DRP-4) (Collapsin response mediator protein 3) (CRMP-3) (UNC33-like phosphoprotein 4) (ULIP-4) 572 61,962 Alternative sequence (1); Chain (1); Modified residue (2); Sequence conflict (4) FUNCTION: Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance, neuronal growth cone collapse and cell migration (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homotetramer, and heterotetramer with CRMP1, DPYSL2, DPYSL3 or DPYSL5. Interacts with PLEXA1. {ECO:0000269|PubMed:10956643, ECO:0000269|PubMed:14685275, ECO:0000269|PubMed:9375656}. +Q9EQF6 DPYL5_MOUSE Dihydropyrimidinase-related protein 5 (DRP-5) (Collapsin response mediator protein 5) (CRMP-5) 564 61,516 Chain (1); Modified residue (5) FUNCTION: May have a function in neuronal differentiation and/or axon growth. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Translocates into the mitochondria upon interaction with SEPT4 isoform 4. {ECO:0000269|PubMed:12581152}. SUBUNIT: Homotetramer, and heterotetramer with other DPYS-like proteins. Interacts with DPYSL2, DPYSL3 and DPYSL4. Interacts with SEPT4 isoform 4. {ECO:0000269|PubMed:10956643, ECO:0000269|PubMed:12581152}. TISSUE SPECIFICITY: Detected in brain. {ECO:0000269|PubMed:10956643}. +Q9D3V1 DRC10_MOUSE Dynein regulatory complex protein 10 (IQ domain-containing protein D) 458 53,351 Alternative sequence (1); Chain (1); Coiled coil (3); Domain (1); Frameshift (1); Sequence conflict (3) FUNCTION: Component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. {ECO:0000250|UniProtKB:A8J0N6}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:A8J0N6}. SUBUNIT: Component of the nexin-dynein regulatory complex (N-DRC). {ECO:0000250|UniProtKB:A8J0N6}. +Q9CUL5 DRC11_MOUSE Dynein regulatory complex protein 11 (IQ and AAA domain-containing protein 1) 857 99,875 Alternative sequence (5); Chain (1); Compositional bias (1); Domain (1); Nucleotide binding (1); Sequence conflict (2) FUNCTION: Component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. {ECO:0000250|UniProtKB:A8IHT2}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:A8IHT2}. SUBUNIT: Component of the nexin-dynein regulatory complex (N-DRC). {ECO:0000250|UniProtKB:A8IHT2}. +Q3USS3 DRC1_MOUSE Dynein regulatory complex protein 1 (Coiled-coil domain-containing protein 164) 753 88,507 Chain (1); Coiled coil (2); Sequence conflict (1) FUNCTION: Component of the nexin-dynein regulatory complex (N-DRC) a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. Plays a critical role in the assembly of N-DRC and also stabilizes the assembly of multiple inner dynein arms and radial spokes. Coassembles with CCDC65/DRC2 to form a central scaffold needed for assembly of the N-DRC and its attachment to the outer doublet microtubules. {ECO:0000250|UniProtKB:P0DL09, ECO:0000250|UniProtKB:Q96MC2}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:P0DL09}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:P0DL09}. SUBUNIT: Component of the nexin-dynein regulatory complex (N-DRC). {ECO:0000250|UniProtKB:P0DL09}. +Q8VHI7 DRC2_MOUSE Dynein regulatory complex subunit 2 (Coiled-coil domain-containing protein 65) (Testis development protein NYD-SP28) 493 58,170 Alternative sequence (1); Chain (1); Coiled coil (2); Sequence conflict (2) FUNCTION: Component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. Plays a critical role in the assembly of N-DRC and also stabilizes the assembly of multiple inner dynein arms and radial spokes. Coassembles with DRC1 to form a central scaffold needed for assembly of the N-DRC and its attachment to the outer doublet microtubules. {ECO:0000250|UniProtKB:A8JB22, ECO:0000250|UniProtKB:Q8IXS2}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum basal body {ECO:0000250|UniProtKB:A8JB22}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:A8JB22}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:A8JB22}. SUBUNIT: Component of the nexin-dynein regulatory complex (N-DRC). {ECO:0000250|UniProtKB:A8JB22}. +Q9D5E4 DRC3_MOUSE Dynein regulatory complex subunit 3 (Leucine-rich repeat-containing protein 48) 523 60,827 Chain (1); Coiled coil (2); Domain (1); Repeat (5) FUNCTION: Component of the nexin-dynein regulatory complex (N-DRC) a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. {ECO:0000250|UniProtKB:A8IVX2}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q9H069}. Cell projection, cilium {ECO:0000250|UniProtKB:Q9H069}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:A8IVX2}. SUBUNIT: Component of the nexin-dynein regulatory complex (N-DRC). Interacts with TCTE1/DRC5 (PubMed:28630322). {ECO:0000269|PubMed:28630322}. +Q60779 DRC4_MOUSE Dynein regulatory complex subunit 4 (Growth arrest-specific protein 11) (GAS-11) (Growth arrest-specific protein 8) (GAS-8) 478 56,264 Chain (1); Coiled coil (2); Frameshift (1); Mutagenesis (1); Region (3); Sequence conflict (5) FUNCTION: Component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. Plays an important role in the assembly of the N-DRC linker (By similarity). Plays dual roles at both the primary (or non-motile) cilia to regulate hedgehog signaling and in motile cilia to coordinate cilia movement. Required for proper motile cilia functioning. Positively regulates ciliary smoothened (SMO)-dependent Hedgehog (Hh) signaling pathway by faciltating the trafficking of SMO into the cilium and the stimulation of SMO activity in a GRK2-dependent manner (PubMed:17366626, PubMed:21659505, PubMed:27472056). May play a role in the spermatozoa motility (PubMed:11751847). {ECO:0000250|UniProtKB:Q7XJ96, ECO:0000269|PubMed:11751847, ECO:0000269|PubMed:17366626, ECO:0000269|PubMed:21659505, ECO:0000269|PubMed:27472056}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11751847, ECO:0000269|PubMed:21659505}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17366626}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:11751847}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:11751847, ECO:0000269|PubMed:26387594, ECO:0000269|PubMed:27472056}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:16643277, ECO:0000269|PubMed:21659505}. Golgi apparatus {ECO:0000269|PubMed:18396146}. Cell projection, cilium {ECO:0000269|PubMed:27472056}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:Q7XJ96}. Note=Associates with microtubules (PubMed:17366626). Localized to the cytoplasm of round spermatids, the tails of elongating spermatids, and mature spermatid tail bundles protruding into the lumen, and in the flagellum of epididymal spermatozoa (PubMed:11751847). {ECO:0000269|PubMed:11751847, ECO:0000269|PubMed:17366626}. SUBUNIT: Component of the nexin-dynein regulatory complex (N-DRC) (By similarity). Interacts with microtubules (PubMed:17366626). Interacts with SMO (PubMed:21659505). Interacts (via coiled-coil domains) with RAB3B (in GTP-bound form) (PubMed:18396146). {ECO:0000250|UniProtKB:Q7XJ96, ECO:0000269|PubMed:17366626, ECO:0000269|PubMed:18396146, ECO:0000269|PubMed:21659505}. TISSUE SPECIFICITY: Highly expressed in adult testes and lung. Weakly or not expressed in other tested tissues. {ECO:0000269|PubMed:11751847, ECO:0000269|PubMed:18396146}. +A6H639 DRC5_MOUSE Dynein regulatory complex subunit 5 (T-complex-associated testis-expressed protein 1) (Tcte-1) 498 55,518 Chain (1); Frameshift (1); Repeat (6); Sequence conflict (2) FUNCTION: Component of the nexin-dynein regulatory complex (N-DRC) a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. May play a role in the assembly of N-DRC (By similarity). Required for sperm motility (PubMed:28630322). {ECO:0000250|UniProtKB:A8HMZ4, ECO:0000269|PubMed:28630322}. SUBCELLULAR LOCATION: Cell projection, cilium, flagellum {ECO:0000269|Ref.2}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:A8HMZ4}. Note=Detected along the length of the sperm flagellum. {ECO:0000269|Ref.2}. SUBUNIT: Component of the nexin-dynein regulatory complex (N-DRC) Interacts with FBXL13/DRC6, DRC3 and DRC7 (PubMed:28630322). {ECO:0000269|PubMed:28630322}. TISSUE SPECIFICITY: Testis-specific (at protein level). {ECO:0000269|PubMed:2568335, ECO:0000269|Ref.2}. +Q8CDU4 DRC6_MOUSE Dynein regulatory complex subunit 6 (F-box and leucine-rich repeat protein 13) (F-box/LRR-repeat protein 13) 790 90,657 Alternative sequence (3); Chain (1); Domain (1); Frameshift (2); Repeat (6); Sequence conflict (3) FUNCTION: Component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. {ECO:0000250, ECO:0000250|UniProtKB:A8JHD7}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:A8JHD7}. SUBUNIT: Component of the nexin-dynein regulatory complex (N-DRC). Directly interacts with SKP1 and CUL1 (By similarity). Interacts with TCTE1/DRC5 (PubMed:28630322). {ECO:0000250, ECO:0000250|UniProtKB:A8JHD7, ECO:0000269|PubMed:28630322}. +Q6V3W6 DRC7_MOUSE Dynein regulatory complex subunit 7 (Coiled-coil domain-containing protein 135) (Coiled-coil domain-containing protein lobo homolog) (Spermatogenesis-related gene in late stages of spermatogenesis cells protein) 876 103,269 Alternative sequence (2); Chain (1); Coiled coil (4); Sequence conflict (2) FUNCTION: Component of the nexin-dynein regulatory complex (N-DRC) a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. Involved in the regulation of flagellar motility. {ECO:0000250|UniProtKB:A8JAM0}. SUBCELLULAR LOCATION: Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:A8JAM0}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:A8JAM0}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:A8JAM0}. Note=Associated with the outer doublet microtubules (OD). {ECO:0000250|UniProtKB:A8JAM0}. SUBUNIT: Component of the nexin-dynein regulatory complex (N-DRC) (By similarity). Interacts with TCTE1/DRC5 (PubMed:28630322). {ECO:0000250|UniProtKB:A8JAM0, ECO:0000269|PubMed:28630322}. TISSUE SPECIFICITY: Isoform 1 is expressed in diplotene and pachytene spermytocytes, and in round and elongating spermatids (at protein level). Isoform 1 is strongly expressed in spleen and testis, faintly expressed in kidney, ovary and thymus. Isoform 1 is expressed in diplotene and pachytene spermytocytes, round and elongating spermatids. Expressed in testis, kidney, ovary, thymus and spleen. Expressed in ciliated cells. {ECO:0000269|PubMed:15156272, ECO:0000269|PubMed:16804880, ECO:0000269|PubMed:17971504}. +Q9CQ46 DRC8_MOUSE Dynein regulatory complex protein 8 (EF-hand calcium-binding domain-containing protein 2) 164 18,929 Chain (1); Domain (2) FUNCTION: Component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. {ECO:0000250|UniProtKB:A8J3A0}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:A8J3A0}. SUBUNIT: Component of the nexin-dynein regulatory complex (N-DRC). {ECO:0000250|UniProtKB:A8J3A0}. +Q80W32 DRC9_MOUSE Dynein regulatory complex protein 9 (IQ domain-containing protein G) 419 49,168 Chain (1); Domain (1) FUNCTION: Component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. Binds calmodulin when cellular Ca(2+) levels are low and thereby contributes to the regulation of calcium and calmodulin-dependent protein kinase IV (CAMK4) activity; contributes to the regulation of CAMK4 signaling cascades (By similarity). Required for normal axoneme assembly in sperm flagella, normal sperm tail formation and for male fertility (PubMed:24362311, PubMed:24849454). {ECO:0000250|UniProtKB:A3KQH2, ECO:0000250|UniProtKB:A8HQ54, ECO:0000269|PubMed:24362311, ECO:0000269|PubMed:24849454}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24849454}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:24849454}. Cell projection, cilium {ECO:0000269|PubMed:24849454}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:24849454}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:A8HQ54}. Note=First detected in the cytoplasm of pachytene spermatocytes. Colocalizes with alpha-tubulin at the manchette in developing spermatids. Detected in the flagellum of mature testicular spermatozoa, and in the flagellum and post-acrosomal region of the head of epididymal spermatozoa. Detected in cilia in trachea and oviduct. {ECO:0000269|PubMed:24849454}. SUBUNIT: Component of the nexin-dynein regulatory complex (N-DRC) (By similarity). Interacts (via IQ domain) with CALM when calcium levels are low. Does not interact with CALM in the presence of Ca(2+) (PubMed:24849454). Interacts with the HSP70 proteins HSPA1L and HSPA8 (By similarity). May form a complex with CAMK4 and HSP70 (Probable). {ECO:0000250|UniProtKB:A8HQ54, ECO:0000250|UniProtKB:Q9H095, ECO:0000269|PubMed:24849454, ECO:0000305|PubMed:24787902}. DOMAIN: The IQ domain mediates interaction with calmodulin when cellular Ca(2+) levels are low. {ECO:0000250|UniProtKB:Q9H095}. TISSUE SPECIFICITY: Detected in testis (PubMed:24362311, PubMed:24849454). Also detected in oviduct (at protein level) (PubMed:24849454). Detected in testis (PubMed:24362311, PubMed:24849454). Also detected in oviduct and trachea (PubMed:24849454). {ECO:0000269|PubMed:24362311, ECO:0000269|PubMed:24849454}. +Q61616 DRD1_MOUSE D(1A) dopamine receptor (Dopamine D1 receptor) 446 49,612 Chain (1); Disulfide bond (1); Glycosylation (1); Lipidation (2); Modified residue (1); Sequence conflict (2); Topological domain (8); Transmembrane (7) TRANSMEM 23 48 Helical; Name=1. {ECO:0000255}.; TRANSMEM 60 86 Helical; Name=2. {ECO:0000255}.; TRANSMEM 96 118 Helical; Name=3. {ECO:0000255}.; TRANSMEM 138 162 Helical; Name=4. {ECO:0000255}.; TRANSMEM 193 218 Helical; Name=5. {ECO:0000255}.; TRANSMEM 273 299 Helical; Name=6. {ECO:0000255}.; TRANSMEM 313 337 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 22 Extracellular. {ECO:0000255}.; TOPO_DOM 49 59 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 87 95 Extracellular. {ECO:0000255}.; TOPO_DOM 119 137 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 163 192 Extracellular. {ECO:0000255}.; TOPO_DOM 219 272 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 300 312 Extracellular. {ECO:0000255}.; TOPO_DOM 338 446 Cytoplasmic. {ECO:0000255}. FUNCTION: Dopamine receptor whose activity is mediated by G proteins which activate adenylyl cyclase. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P18901}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P18901}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P18901}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P18901}. Cell projection, dendrite {ECO:0000269|PubMed:25865831}. Cell projection, dendritic spine {ECO:0000269|PubMed:25865831}. Note=Transport from the endoplasmic reticulum to the cell surface is regulated by interaction with DNAJC14. {ECO:0000250|UniProtKB:P18901}. SUBUNIT: Interacts with DNAJC14 via its C-terminus (By similarity). Interacts with DRD2 (PubMed:25865831). {ECO:0000250|UniProtKB:P18901, ECO:0000269|PubMed:25865831}. +P61168 DRD2_MOUSE D(2) dopamine receptor (Dopamine D2 receptor) 444 50,930 Alternative sequence (1); Binding site (1); Chain (1); Disulfide bond (2); Glycosylation (3); Region (3); Sequence conflict (1); Site (2); Topological domain (8); Transmembrane (7) TRANSMEM 38 60 Helical; Name=1. {ECO:0000250}.; TRANSMEM 71 93 Helical; Name=2. {ECO:0000250}.; TRANSMEM 109 130 Helical; Name=3. {ECO:0000250}.; TRANSMEM 152 172 Helical; Name=4. {ECO:0000250}.; TRANSMEM 189 213 Helical; Name=5. {ECO:0000250}.; TRANSMEM 375 396 Helical; Name=6. {ECO:0000250}.; TRANSMEM 411 432 Helical; Name=7. {ECO:0000250}. TOPO_DOM 1 37 Extracellular. {ECO:0000250}.; TOPO_DOM 61 70 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 94 108 Extracellular. {ECO:0000250}.; TOPO_DOM 131 151 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 173 188 Extracellular. {ECO:0000250}.; TOPO_DOM 214 374 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 397 410 Extracellular. {ECO:0000250}.; TOPO_DOM 433 444 Cytoplasmic. {ECO:0000250}. FUNCTION: Dopamine receptor whose activity is mediated by G proteins which inhibit adenylyl cyclase. {ECO:0000250|UniProtKB:P14416}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBUNIT: Forms homo- and heterooligomers with DRD4 (By similarity). The interaction with DRD4 may modulate agonist-induced downstream signaling (By similarity). Interacts with CADPS and CADPS2 (By similarity). Interacts with GPRASP1, PPP1R9B and CLIC6 (By similarity). Interacts with ARRB2 (By similarity). Interacts with HTR2A (By similarity). Isoform 1 and isoform 2 interact both with KCNA2 (PubMed:21233214). Interacts with DRD1 (PubMed:25865831). {ECO:0000250|UniProtKB:P14416, ECO:0000250|UniProtKB:P61169, ECO:0000269|PubMed:21233214, ECO:0000269|PubMed:25865831}. TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in the pituitary and brain. Isoform 1 is expressed seven times more than isoform 2 in the caudate nucleus. +P30728 DRD3_MOUSE D(3) dopamine receptor (Dopamine D3 receptor) 446 49,669 Alternative sequence (1); Binding site (1); Chain (1); Disulfide bond (2); Glycosylation (4); Region (2); Topological domain (8); Transmembrane (7) TRANSMEM 33 55 Helical; Name=1. {ECO:0000250|UniProtKB:P35462}.; TRANSMEM 66 88 Helical; Name=2. {ECO:0000250|UniProtKB:P35462}.; TRANSMEM 105 126 Helical; Name=3. {ECO:0000250|UniProtKB:P35462}.; TRANSMEM 150 170 Helical; Name=4. {ECO:0000250|UniProtKB:P35462}.; TRANSMEM 188 209 Helical; Name=5. {ECO:0000250|UniProtKB:P35462}.; TRANSMEM 376 397 Helical; Name=6. {ECO:0000250|UniProtKB:P35462}.; TRANSMEM 413 432 Helical; Name=7. {ECO:0000250|UniProtKB:P35462}. TOPO_DOM 1 32 Extracellular. {ECO:0000250|UniProtKB:P35462}.; TOPO_DOM 56 65 Cytoplasmic. {ECO:0000250|UniProtKB:P35462}.; TOPO_DOM 89 104 Extracellular. {ECO:0000250|UniProtKB:P35462}.; TOPO_DOM 127 149 Cytoplasmic. {ECO:0000250|UniProtKB:P35462}.; TOPO_DOM 171 187 Extracellular. {ECO:0000250|UniProtKB:P35462}.; TOPO_DOM 210 375 Cytoplasmic. {ECO:0000250|UniProtKB:P35462}.; TOPO_DOM 398 412 Extracellular. {ECO:0000250|UniProtKB:P35462}.; TOPO_DOM 433 446 Cytoplasmic. {ECO:0000250|UniProtKB:P35462}. FUNCTION: Dopamine receptor whose activity is mediated by G proteins which inhibit adenylyl cyclase. Promotes cell proliferation (By similarity). {ECO:0000250}. PTM: Phosphorylated by GRK4. {ECO:0000250|UniProtKB:P35462}.; PTM: Palmitoylated. {ECO:0000250|UniProtKB:P35462}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBUNIT: Interacts with CLIC6 (By similarity). Interacts with GRK4. Interacts with PALM. Interacts with FLNA (via filamin repeat 21); increases PKA-mediated phosphorylation of FLNA (By similarity). {ECO:0000250|UniProtKB:P19020, ECO:0000250|UniProtKB:P35462}. +P51436 DRD4_MOUSE D(4) dopamine receptor (D(2C) dopamine receptor) (Dopamine D4 receptor) 387 41,487 Binding site (1); Chain (1); Disulfide bond (2); Glycosylation (1); Lipidation (1); Metal binding (2); Sequence conflict (3); Topological domain (8); Transmembrane (7) TRANSMEM 35 57 Helical; Name=1. {ECO:0000250|UniProtKB:P21917}.; TRANSMEM 68 90 Helical; Name=2. {ECO:0000250|UniProtKB:P21917}.; TRANSMEM 107 128 Helical; Name=3. {ECO:0000250|UniProtKB:P21917}.; TRANSMEM 147 170 Helical; Name=4. {ECO:0000250|UniProtKB:P21917}.; TRANSMEM 187 208 Helical; Name=5. {ECO:0000250|UniProtKB:P21917}.; TRANSMEM 315 337 Helical; Name=6. {ECO:0000250|UniProtKB:P21917}.; TRANSMEM 347 369 Helical; Name=7. {ECO:0000250|UniProtKB:P21917}. TOPO_DOM 1 34 Extracellular. {ECO:0000250|UniProtKB:P21917}.; TOPO_DOM 58 67 Cytoplasmic. {ECO:0000250|UniProtKB:P21917}.; TOPO_DOM 91 106 Extracellular. {ECO:0000250|UniProtKB:P21917}.; TOPO_DOM 129 146 Cytoplasmic. {ECO:0000250|UniProtKB:P21917}.; TOPO_DOM 171 186 Extracellular. {ECO:0000250|UniProtKB:P21917}.; TOPO_DOM 209 314 Cytoplasmic. {ECO:0000250|UniProtKB:P21917}.; TOPO_DOM 338 346 Extracellular. {ECO:0000250|UniProtKB:P21917}.; TOPO_DOM 370 387 Cytoplasmic. {ECO:0000250|UniProtKB:P21917}. FUNCTION: Dopamine receptor responsible for neuronal signaling in the mesolimbic system of the brain, an area of the brain that regulates emotion and complex behavior. Activated by dopamine, but also by epinephrine and norepinephrine, and by numerous synthetic agonists and drugs. Agonist binding triggers signaling via G proteins that inhibit adenylyl cyclase (By similarity). Modulates the circadian rhythm of contrast sensitivity by regulating the rhythmic expression of NPAS2 in the retinal ganglion cells (PubMed:24048828). {ECO:0000250|UniProtKB:P21917, ECO:0000269|PubMed:24048828}. PTM: Polyubiquitinated by the BCR(KLHL12) E3 ubiquitin ligase complex: polyubiquitination does not lead to degradation of DRD4 protein. {ECO:0000250|UniProtKB:P21917}.; PTM: Palmitoylated. Palmitoylation of the C-terminal Cys is important for normal expression at the cell membrane. {ECO:0000250|UniProtKB:P21917}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P21917}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P21917}. SUBUNIT: Forms homo- and heterooligomers with DRD2. D4.7 allele exhibits higher affinity for homodimers compared to DRD2 heterodimers, while alleles D42. and 4.4 have similar affinities for both. The interaction with DRD2 may modulate agonist-induced downstream signaling (By similarity). Interacts with CLIC6 (By similarity). Interacts with GPRASP1. May interact with ADORA2A. Interacts with KLHL12 (By similarity). {ECO:0000250|UniProtKB:P21917, ECO:0000250|UniProtKB:P30729}. TISSUE SPECIFICITY: Detected in olfactory bulb, hypothalamus, olfactory tubercle, brainstem and striatum. {ECO:0000269|PubMed:7698326}. +Q8BLD9 DRD5_MOUSE D(1B) dopamine receptor (D(5) dopamine receptor) (Dopamine D5 receptor) 478 53,076 Chain (1); Disulfide bond (1); Glycosylation (1); Lipidation (1); Sequence conflict (1); Topological domain (8); Transmembrane (7) TRANSMEM 39 64 Helical; Name=1. {ECO:0000255}.; TRANSMEM 76 102 Helical; Name=2. {ECO:0000255}.; TRANSMEM 112 134 Helical; Name=3. {ECO:0000255}.; TRANSMEM 154 179 Helical; Name=4. {ECO:0000255}.; TRANSMEM 216 240 Helical; Name=5. {ECO:0000255}.; TRANSMEM 290 317 Helical; Name=6. {ECO:0000255}.; TRANSMEM 336 357 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 38 Extracellular. {ECO:0000255}.; TOPO_DOM 65 75 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 103 111 Extracellular. {ECO:0000255}.; TOPO_DOM 135 153 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 180 215 Extracellular. {ECO:0000255}.; TOPO_DOM 241 289 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 318 335 Extracellular. {ECO:0000255}.; TOPO_DOM 358 478 Cytoplasmic. {ECO:0000255}. FUNCTION: Dopamine receptor whose activity is mediated by G proteins which activate adenylyl cyclase. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q9QXS6 DREB_MOUSE Drebrin (Developmentally-regulated brain protein) 706 77,287 Alternative sequence (3); Chain (1); Domain (1); Initiator methionine (1); Modified residue (14); Sequence conflict (4) FUNCTION: Actin cytoskeleton-organizing protein that plays a role in the formation of cell projections (By similarity). Required for actin polymerization at immunological synapses (IS) and for the recruitment of the chemokine receptor CXCR4 to IS (By similarity). Plays a role in dendritic spine morphogenesis and organization, including the localization of the dopamine receptor DRD1 to the dendritic spines (PubMed:25865831). Involved in memory-related synaptic plasticity in the hippocampus (PubMed:25865831). {ECO:0000250|UniProtKB:Q16643, ECO:0000269|PubMed:25865831}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q16643}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q16643}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q16643}. Cell junction {ECO:0000250|UniProtKB:Q16643}. Cell projection {ECO:0000269|PubMed:24720729}. Cell projection, growth cone {ECO:0000269|PubMed:24720729}. Note=In the absence of antigen, evenly distributed throughout subcortical regions of the T-cell membrane and cytoplasm. In the presence of antigen, distributes to the immunological synapse forming at the T-cell-APC contact area, where it localizes at the peripheral and distal supramolecular activation clusters (SMAC) (By similarity). Colocalized with RUFY3 and F-actin at the transitional domain of the axonal growth cone (PubMed:24720729). {ECO:0000250|UniProtKB:Q16643, ECO:0000269|PubMed:24720729}. SUBUNIT: Interacts with RUFY3 (PubMed:24720729). Interacts with CXCR4; this interaction is enhanced by antigenic stimulation (By similarity). Interacts (via ADF-H domain) with ZMYND8 (via PHD-type Zinc finger, Bromo and PWWP domains); the interaction leads to sequestering of ZMYND8 in the cytoplasm (By similarity). {ECO:0000250|UniProtKB:Q16643}. TISSUE SPECIFICITY: Expressed in the hippocampus, with expression in the pyramidal cells of CA1, CA2 and CA3 and in the granule cells of the dentate gyrus (at protein level) (PubMed:25865831). Highly expressed in brain, also present in stomach and to a lesser degree in kidney, colon, and urinary bladder (PubMed:10633083). The E2 isoform is specifically expressed in adult stomach, kidney, and cultured cells (PubMed:10633083). {ECO:0000269|PubMed:10633083, ECO:0000269|PubMed:25865831}. +P32233 DRG1_MOUSE Developmentally-regulated GTP-binding protein 1 (DRG-1) (Neural precursor cell expressed developmentally down-regulated protein 3) (NEDD-3) (Translation factor GTPase DRG1) (TRAFAC GTPase DRG1) (EC 3.6.5.-) 367 40,512 Chain (1); Compositional bias (1); Domain (2); Initiator methionine (1); Metal binding (2); Modified residue (3); Nucleotide binding (5); Region (1) FUNCTION: Catalyzes the conversion of GTP to GDP through hydrolysis of the gamma-phosphate bond in GTP. Appears to have an intrinsic GTPase activity that is stimulated by ZC3H15/DFRP1 binding likely by increasing the affinity for the potassium ions. When hydroxylated at C-3 of 'Lys-22' by JMJD7, may bind to RNA and play a role in translation. Binds to microtubules and promotes microtubule polymerization and bundling that are required for mitotic spindle assembly during prophase to anaphase transition. GTPase activity is not necessary for these microtubule-related functions. {ECO:0000250|UniProtKB:Q9Y295}. PTM: Polyubiquitinated; this modification induces proteolytic degradation and is impaired by interaction with ZC3H15. {ECO:0000305|PubMed:15676025}.; PTM: Sumoylated by UBE2I in response to MEKK1-mediated stimuli. {ECO:0000250|UniProtKB:Q9Y295}.; PTM: Hydroxylated (with S stereochemistry) at C-3 of Lys-22 by JMJD7. {ECO:0000250|UniProtKB:Q9Y295}.; PTM: Phosphorylated at Thr-100 by STK16. {ECO:0000250|UniProtKB:Q9Y295}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y295}. Cytoplasm {ECO:0000269|PubMed:1280421}. Note=The DRG1-DFRP2/ZC3H15 complex associates with polysomes. {ECO:0000250|UniProtKB:Q9Y295}. SUBUNIT: Interacts (via its C-terminal) with TAL1 (By similarity). Interacts with DFRP1/ZC3H15; this interaction prevents DRG1 poly-ubiquitination and degradation by proteasome. DRG1-DFRP1/ZC3H15 complex co-sediments with polysomes (By similarity) (PubMed:15676025). Interacts with STK16. Interacts with JMJD7 (By similarity). {ECO:0000250|UniProtKB:Q9Y295, ECO:0000269|PubMed:15676025}. DOMAIN: Its C-terminal domain interacts with TAL1.; DOMAIN: The ThrRS, GTPase, SpoT (TGS) domain is not necessary for GTP binding nor for the GTPase activity. It appears to play a regulatory role favoring GTP hydrolysis mediated by DFRP1/ZC3H15. {ECO:0000250|UniProtKB:Q9Y295}. TISSUE SPECIFICITY: Fairly high levels in liver, heart, kidney, testis and brain. Very low levels in lung, spleen, and skeletal muscle. {ECO:0000269|PubMed:1280421}. +Q9QXB9 DRG2_MOUSE Developmentally-regulated GTP-binding protein 2 (DRG-2) (Translation factor GTPase DRG2) (TRAFAC GTPase DRG2) (EC 3.6.5.-) 364 40,718 Chain (1); Domain (1); Metal binding (2); Modified residue (1); Nucleotide binding (5) FUNCTION: Catalyzes the conversion of GTP to GDP through hydrolysis of the gamma-phosphate bond in GTP. When hydroxylated at C-3 of 'Lys-21' by JMJD7, may bind to RNA and play a role in translation. {ECO:0000250|UniProtKB:P55039}. PTM: Polyubiquitinated. {ECO:0000305|PubMed:15676025}.; PTM: Hydroxylated (with S stereochemistry) at C-3 of Lys-21 by JMJD7. {ECO:0000250|UniProtKB:P55039}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P55039}. Cytoplasm {ECO:0000250|UniProtKB:P55039}. SUBUNIT: Interacts with RWDD1; this interaction confers protection to polyubiquitination and proteolytic degradation (PubMed:15676025). Interacts with JMJD7; this interaction is direct (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P55039, ECO:0000269|PubMed:15676025}. TISSUE SPECIFICITY: Fairly high levels in liver, heart, kidney, and brain. Very low levels in lung, spleen, testis and skeletal muscle. +Q8BYH0 DRGX_MOUSE Dorsal root ganglia homeobox protein (Dorsal root ganglion 11) (Homeobox protein DRG11) (Paired-related homeobox protein-like 1) 263 28,717 Alternative sequence (1); Chain (1); DNA binding (1); Motif (1) FUNCTION: Transcription factor required for the formation of correct projections from nociceptive sensory neurons to the dorsal horn of the spinal cord and normal perception of pain. {ECO:0000269|PubMed:11498051}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P54821, ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-ProRule:PRU00138}. SUBUNIT: Interacts with RGMB. {ECO:0000269|PubMed:14985445}. TISSUE SPECIFICITY: Expressed in the dorsal horn of the spinal cord and dorsal root ganglia. Isoform 1 is higher expressed than isoform 2 both in the dorsal root ganglia and in the spinal cord. Isoform 2 is exclusively localized in neurons primarily involved in the processing of the pain somatosensory modality. {ECO:0000269|PubMed:11498051, ECO:0000269|PubMed:19598127}. +Q99J47 DRS7B_MOUSE Dehydrogenase/reductase SDR family member 7B (EC 1.1.-.-) (Short-chain dehydrogenase/reductase family 32C member 1) 323 34,987 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Erroneous initiation (1); Nucleotide binding (1); Topological domain (2); Transmembrane (1) TRANSMEM 18 38 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 17 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 39 323 Lumenal. {ECO:0000255}. FUNCTION: Putative oxidoreductase. {ECO:0000305}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. +Q8CHS7 DRS7C_MOUSE Dehydrogenase/reductase SDR family member 7C (EC 1.1.-.-) (Short-chain dehydrogenase/reductase family 32C member 2) 311 34,468 Active site (1); Chain (1); Nucleotide binding (1); Signal peptide (1) FUNCTION: Putative oxidoreductase. {ECO:0000305}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q6B8I0 DS13A_MOUSE Dual specificity protein phosphatase 13 isoform A (DUSP13A) (EC 3.1.3.16) (EC 3.1.3.48) (Muscle-restricted DSP) 188 20,646 Active site (1); Chain (1); Domain (1) FUNCTION: Probable protein tyrosine phosphatase. Has phosphatase activity with synthetic substrates. Has a phosphatase activity-independent regulatory role in MAP3K5/ASK1-mediated apoptosis, preventing MAP3K5/ASK1 inhibition by AKT1. Shows no phosphatase activity on MAPK1/ERK2, MAPK8/JNK, MAPK14/p38 and MAP3K5/ASK1. {ECO:0000250|UniProtKB:Q6B8I1}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Monomer. Interacts with MAP3K5/ASK1; may compete with AKT1 preventing MAP3K5/ASK1 phosphorylation by AKT1. {ECO:0000250|UniProtKB:Q6B8I1}. TISSUE SPECIFICITY: Skeletal muscle-specific. {ECO:0000269|PubMed:15252030}. +Q9QYJ7 DS13B_MOUSE Dual specificity protein phosphatase 13 isoform B (DUSP13B) (EC 3.1.3.16) (EC 3.1.3.48) (Dual specificity tyrosine phosphatase TS-DSP6) (Testis- and skeletal muscle-specific DSP) 198 22,481 Active site (1); Chain (1); Domain (1) FUNCTION: Dual specificity phosphatase that dephosphorylates MAPK8/JNK and MAPK14/p38, but not MAPK1/ERK2, in vitro. Exhibits intrinsic phosphatase activity towards both phospho-seryl/threonyl and -tyrosyl residues, with similar specific activities in vitro (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Most abundantly expressed in the testis. {ECO:0000269|PubMed:15252030}. +Q91WZ8 DTBP1_MOUSE Dysbindin (Biogenesis of lysosome-related organelles complex 1 subunit 8) (BLOC-1 subunit 8) (Dysbindin-1) (Dystrobrevin-binding protein 1) (Hermansky-Pudlak syndrome 7 protein homolog) (HPS7 protein homolog) 352 39,651 Alternative sequence (2); Chain (1); Coiled coil (1); Erroneous initiation (1); Frameshift (1); Modified residue (4); Motif (1); Region (1); Sequence conflict (2) FUNCTION: Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. Associates with the BLOC-2 complex to facilitate the transport of TYRP1 independent of AP-3 function. Plays a role in synaptic vesicle trafficking and in neurotransmitter release. Plays a role in the regulation of cell surface exposure of DRD2. May play a role in actin cytoskeleton reorganization and neurite outgrowth. May modulate MAPK8 phosphorylation. Appears to promote neuronal transmission and viability through regulating the expression of SNAP25 and SYN1, modulating PI3-kinase-Akt signaling and influencing glutamatergic release. Regulates the expression of SYN1 through binding to its promoter. Modulates prefrontal cortical activity via the dopamine/D2 pathway. {ECO:0000269|PubMed:12923531, ECO:0000269|PubMed:15345706, ECO:0000269|PubMed:16448387, ECO:0000269|PubMed:16760431, ECO:0000269|PubMed:16837549, ECO:0000269|PubMed:18504299, ECO:0000269|PubMed:18555792, ECO:0000269|PubMed:18984010, ECO:0000269|PubMed:19094965, ECO:0000269|PubMed:19428785, ECO:0000269|PubMed:19546860, ECO:0000269|PubMed:19887632, ECO:0000269|PubMed:20045719, ECO:0000269|PubMed:20921223, ECO:0000269|PubMed:20956979, ECO:0000269|PubMed:21998198}. PTM: Ubiquitinated by TRIM32. Ubiquitination leads to DTNBP1 degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Isoform 1: Cytoplasm. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Endosome membrane; Peripheral membrane protein; Cytoplasmic side. Melanosome membrane; Peripheral membrane protein; Cytoplasmic side. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density. Endoplasmic reticulum {ECO:0000250}. Nucleus. Note=Mainly cytoplasmic but shuttles between the cytoplasm and nucleus. Exported out of the nucleus via its NES in a XPO1-dependent manner. Nuclear localization is required for regulation of the expression of genes such as SYN1. Detected in neuron cell bodies, axons and dendrites. Mainly located to the postsynaptic density. Detected at tubulovesicular elements in the vicinity of the Golgi apparatus and of melanosomes. Occasionally detected at the membrane of pigmented melanosomes in cultured melanoma cells (By similarity). The BLOC-1 complex associates with the BLOC-2 complex in early endosome-associated tubules. Associated with the AP-3 complex at presynaptic terminals. {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 3: Cytoplasm. Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Melanosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane. Endoplasmic reticulum {ECO:0000250}. Note=Exclusivley cytoplasmic. Predominantly found in the postsynaptic density (PSD). Little association with synaptic vesicles (By similarity). The BLOC-1 complex associates with the BLOC-2 complex in early endosome-associated tubules. vesicle membranes and microtubules. Associated with the AP-3 complex at presynaptic terminals. {ECO:0000250}. SUBUNIT: Interacts with AP3M1 and TRIM32. Interacts (isoform 1 and isoform 2 only) with the DNA-dependent protein kinase complex DNA-PK; the interaction phosphorylates DTNBP1 in vitro. Interacts directly in this complex with XRCC5 and XRCC6. Interacts with XPO1; the interaction exports DTNBP1 out of the nucleus (By similarity). Component of the biogenesis of lysosome-related organelles complex 1 (BLOC-1) composed of BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. The BLOC-1 complex associates with the AP-3 protein complex and membrane protein cargos. This BLOC-1 complex also associates with the BLOC-2 complex in endosomes. Binds to DTNA and DTNB but may not be a physiological binding partner (PubMed:16448387 and PubMed:16980328). Interacts (via its coiled coil domain) with KXD1. Interacts with AP3B2, BLOC1S5, BLOC1S6, CMYA5, PI4K2, RNF151 and SNAPIN/BLOC1S8. Interacts with XPO1; the interaction exports DTNBP1 out of the nucleus. {ECO:0000250, ECO:0000269|PubMed:11316798, ECO:0000269|PubMed:12923531, ECO:0000269|PubMed:14688250, ECO:0000269|PubMed:16448387, ECO:0000269|PubMed:16837549, ECO:0000269|PubMed:16980328, ECO:0000269|PubMed:17577571, ECO:0000269|PubMed:19142223, ECO:0000269|PubMed:19428785, ECO:0000269|PubMed:19546860, ECO:0000269|PubMed:21998198, ECO:0000269|PubMed:22554196}. TISSUE SPECIFICITY: Detected in brain, in hippocampus and dentate gyrus neurons. Detected at axon bundles and axon terminals, notably in the cerebellum and hippocampus. Detected in neuropil in hippocampus, lateral septum, basal ganglia and substantia nigra. Highly expressed in pyramidal cells of hippocampus CA2 and CA3. Detected at the heart and skeletal muscle sarcolemma (at protein level). Ubiquitously expressed. The highest expression is observed in testis, liver, kidney, brain, heart and lung. Expressed at lower levels in stomach and small intestine. {ECO:0000269|PubMed:11316798, ECO:0000269|PubMed:12923531, ECO:0000269|PubMed:16760431, ECO:0000269|PubMed:16980328, ECO:0000269|PubMed:19428785, ECO:0000269|PubMed:19546860}. DISEASE: Note=Defects in Dtnbp1 are the cause of the sandy (sdy) mutant phenotype, a model for human Hermansky-Pudlak syndrome (HPS). Sdy mice lack dysbindin expression; they have a characteristic sandy coat color and have much fewer melanosomes in the retinal pigment epithelium and choroid. They are fully viable, but present behavioral abnormalities. They have prolonged bleeding times due to platelet storage pool deficiency, and lysosomal storage defects. The number of electron-opaque platelet dense granules is severely reduced, and the platelet serotonin content is strongly reduced. Secretion of lysosomal enzymes from kidney and from thrombin-stimulated platelets is depressed 2- and 3-fold, and ceroid pigment is present in kidney. Sandy mice also display impaired long-term memory retention and working memory and schizophrenia-like behavioral abnormalities. Vesicle morphology and kinetics of transmitter release are affected in both neuroendocrine cells and hippocampal synapses, characterized by larger vesicle size, slower quantal release, fewer release events and reduced readily releasable pool (RRP). Expression levels of SYN1 are lower in both the cortex and the hippocampal formation (HF). {ECO:0000269|PubMed:12923531, ECO:0000269|PubMed:18504299, ECO:0000269|PubMed:18555792, ECO:0000269|PubMed:18945333, ECO:0000269|PubMed:18984010, ECO:0000269|PubMed:19220483, ECO:0000269|PubMed:1936982, ECO:0000269|PubMed:20921223}. +Q9DD18 DTD1_MOUSE D-aminoacyl-tRNA deacylase 1 (DTD) (EC 3.1.1.96) (DNA-unwinding element-binding protein B) (DUE-B) (Gly-tRNA(Ala) deacylase) (EC 3.1.1.-) 209 23,384 Alternative sequence (1); Chain (1); Frameshift (1); Modified residue (3); Motif (1); Sequence conflict (3) FUNCTION: An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo and helps enforce protein L-homochirality. {ECO:0000250|UniProtKB:Q8IIS0}.; FUNCTION: ATPase involved in DNA replication, may facilitate loading of CDC45 onto pre-replication complexes. {ECO:0000250|UniProtKB:Q8TEA8}. PTM: Preferentially phosphorylated in cells arrested early in S phase. Phosphorylation in the C-terminus weakens the interaction with CDC45 (By similarity). {ECO:0000250|UniProtKB:Q8TEA8}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8TEA8}. Cytoplasm {ECO:0000250|UniProtKB:Q8IIS0}. Note=Associated with chromatin at some replication origins containing functional DNA-unwinding elements (By similarity). {ECO:0000250|UniProtKB:Q8TEA8}. SUBUNIT: Homodimer. Interacts with CDC45 and TOPBP1 (By similarity). {ECO:0000250|UniProtKB:Q8TEA8}. DOMAIN: A Gly-cisPro motif from one monomer fits into the active site of the other monomer to allow specific chiral rejection of L-amino acids. {ECO:0000250|UniProtKB:Q8IIS0}. +Q9D700 DUS26_MOUSE Dual specificity protein phosphatase 26 (EC 3.1.3.16) (EC 3.1.3.48) (Dual specificity phosphatase SKRP3) 211 23,946 Active site (1); Chain (1); Domain (1) FUNCTION: Inactivates MAPK1 and MAPK3 which leads to dephosphorylation of heat shock factor protein 4 and a reduction in its DNA-binding activity. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Golgi apparatus {ECO:0000250}. SUBUNIT: Interacts with HSF4. {ECO:0000250}. TISSUE SPECIFICITY: Brain and skeletal muscle. In the brain it is expressed ubiquitously except in the hippocampus. {ECO:0000269|PubMed:16581800, ECO:0000269|PubMed:17001450}. +Q8VC74 COX18_MOUSE Cytochrome c oxidase assembly protein COX18, mitochondrial 331 36,303 Chain (1); Sequence caution (1); Sequence conflict (11); Topological domain (4); Transit peptide (1); Transmembrane (3) TRANSMEM 165 185 Helical. {ECO:0000255}.; TRANSMEM 221 241 Helical. {ECO:0000255}.; TRANSMEM 260 280 Helical. {ECO:0000255}. TOPO_DOM 64 164 Mitochondrial intermembrane. {ECO:0000305}.; TOPO_DOM 186 220 Mitochondrial matrix. {ECO:0000305}.; TOPO_DOM 242 259 Mitochondrial intermembrane. {ECO:0000305}.; TOPO_DOM 281 331 Mitochondrial matrix. {ECO:0000305}. FUNCTION: Mitochondrial membrane insertase required for the translocation of the C-terminus of cytochrome c oxidase subunit II (MT-CO2/COX2) across the mitochondrial inner membrane. Plays a role in MT-CO2/COX2 maturation following the COX20-mediated stabilization of newly synthesized MT-CO2/COX2 protein and before the action of the metallochaperones SCO1/2. Essential for the assembly and stability of the mitochondrial respiratory chain complex IV (also known as cytochrome c oxidase). {ECO:0000250|UniProtKB:Q8N8Q8}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q8N8Q8}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Found in a complex with TMEM177, COA6, MT-CO2/COX2, COX20, SCO1 and SCO2. Interacts transiently with MT-CO2/COX2 during its maturation. Interacts with COX20 in a MT-CO2/COX2-dependent manner. {ECO:0000250|UniProtKB:Q8N8Q8}. +Q8K0C8 COX19_MOUSE Cytochrome c oxidase assembly protein COX19 92 10,821 Chain (1); Disulfide bond (2); Domain (1); Initiator methionine (1); Modified residue (1); Motif (2) FUNCTION: Required for the transduction of an SCO1-dependent redox signal from the mitochondrion to ATP7A to regulate cellular copper homeostasis. May be required for the assembly of mitochondrial cytochrome c oxidase. {ECO:0000250|UniProtKB:Q3E731, ECO:0000250|UniProtKB:Q49B96}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q49B96}. Mitochondrion intermembrane space {ECO:0000250|UniProtKB:Q49B96}. Mitochondrion {ECO:0000250|UniProtKB:Q49B96}. Note=Partitions between mitochondria and the cytosol in a copper-dependent manner. Enriched in the cytosol when intracellular copper concentrations are elevated. {ECO:0000250|UniProtKB:Q49B96}. SUBUNIT: Interacts with CHCHD4/MIA40 forming transient intermolecular disulfide bridges. {ECO:0000250|UniProtKB:Q49B96}. +Q91XI1 DUS3L_MOUSE tRNA-dihydrouridine(47) synthase [NAD(P)(+)]-like (EC 1.3.1.-) (tRNA-dihydrouridine synthase 3-like) 637 71,078 Active site (1); Alternative sequence (2); Binding site (3); Chain (1); Cross-link (1); Modified residue (3); Nucleotide binding (3); Sequence conflict (1); Zinc finger (2) FUNCTION: Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs. {ECO:0000250}. +Q8BJ03 COX15_MOUSE Cytochrome c oxidase assembly protein COX15 homolog 413 45,853 Alternative sequence (1); Chain (1); Erroneous initiation (1); Transmembrane (7) TRANSMEM 72 92 Helical. {ECO:0000255}.; TRANSMEM 157 174 Helical. {ECO:0000255}.; TRANSMEM 187 207 Helical. {ECO:0000255}.; TRANSMEM 230 250 Helical. {ECO:0000255}.; TRANSMEM 272 292 Helical. {ECO:0000255}.; TRANSMEM 360 380 Helical. {ECO:0000255}.; TRANSMEM 385 405 Helical. {ECO:0000255}. FUNCTION: May be involved in the biosynthesis of heme A. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q64462 CP4B1_MOUSE Cytochrome P450 4B1 (EC 1.14.14.1) (CYPIVB1) 511 58,900 Binding site (1); Chain (1); Metal binding (1) FUNCTION: Responsible for mutagenic activation of 3-methoxy-4-aminoazobenzene (3-MeO-AAB); a potent procarcinogen. Also active on 2-aminofluorene and 2-aminoanthracene. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. TISSUE SPECIFICITY: Present abundantly in renal microsomes of male mice but not in those of female mice. Also present in pulmonary microsomes of male and female mice. Not found in liver. +Q8BTV2 CPSF7_MOUSE Cleavage and polyadenylation specificity factor subunit 7 471 52,011 Alternative sequence (2); Chain (1); Compositional bias (3); Cross-link (1); Domain (1); Modified residue (4); Region (1); Sequence conflict (1) FUNCTION: Component of the cleavage factor Im (CFIm) complex that functions as an activator of the pre-mRNA 3'-end cleavage and polyadenylation processing required for the maturation of pre-mRNA into functional mRNAs. CFIm contributes to the recruitment of multiprotein complexes on specific sequences on the pre-mRNA 3'-end, so called cleavage and polyadenylation signals (pA signals). Most pre-mRNAs contain multiple pA signals, resulting in alternative cleavage and polyadenylation (APA) producing mRNAs with variable 3'-end formation. The CFIm complex acts as a key regulator of cleavage and polyadenylation site choice during APA through its binding to 5'-UGUA-3' elements localized in the 3'-untranslated region (UTR) for a huge number of pre-mRNAs. CPSF7 activates directly the mRNA 3'-processing machinery. Binds to pA signals in RNA substrates. {ECO:0000250|UniProtKB:Q8N684}. PTM: Phosphorylated. {ECO:0000250|UniProtKB:Q8N684}.; PTM: Asymmetrically dimethylated on arginine residues by PRMT1. {ECO:0000250|UniProtKB:Q8N684}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8N684}. Cytoplasm {ECO:0000250|UniProtKB:Q8N684}. Note=Shuttles between the nucleus and the cytoplasm in a transcription- and XPO1/CRM1-independent manner, most probably in complex with the cleavage factor Im complex (CFIm). {ECO:0000250|UniProtKB:Q8N684}. SUBUNIT: Component of the cleavage factor Im (CFIm) complex which is an heterotetramer composed of two subunits of NUDT21/CPSF5 and two subunits of CPSF6 or CPSF7 or an heterodimer of CPSF6 and CPSF7. The cleavage factor Im (CFIm) complex associates with the CPSF and CSTF complexes to promote the assembly of the core mRNA 3'-processing machinery. Interacts with NUDT21/CPSF5. Interacts (via Arg/Ser-rich domain) with FIP1L1 (preferentially via unphosphorylated form and Arg/Glu/Asp-rich region); this interaction mediates, at least in part, the interaction between the CFIm and CPSF complexes and may be inhibited by CPSF7 hyper-phosphorylation. {ECO:0000250|UniProtKB:Q8N684}. DOMAIN: Contains an Arg/Ser-rich domain composed of arginine-serine dipeptide repeats within the C-terminal region that is necessary and sufficient for activating mRNA 3'-processing. {ECO:0000250|UniProtKB:Q8N684}. +Q8BT60 CPNE3_MOUSE Copine-3 (Copine III) 533 59,585 Chain (1); Domain (3); Erroneous initiation (1); Modified residue (3); Sequence conflict (2) FUNCTION: Calcium-dependent phospholipid-binding protein that plays a role in ERBB2-mediated tumor cell migration in response to growth factor heregulin stimulation. {ECO:0000250|UniProtKB:O75131}. PTM: Phosphorylated on serine and threonine residues. {ECO:0000250|UniProtKB:O75131}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O75131}. Cytoplasm {ECO:0000250|UniProtKB:O75131}. Cell membrane {ECO:0000250|UniProtKB:O75131}. Cell junction {ECO:0000250|UniProtKB:O75131}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:O75131}. Note=Associates to the membrane in a calcium-dependent manner. Translocates to the cell membrane and the nucleus in a calcium- or growth factor heregulin-dependent manner. Colocalizes with the tyrosine phosphorylated ERBB2 form at cell membrane and focal adhesions in a calcium- or growth factor heregulin-dependent manner. {ECO:0000250|UniProtKB:O75131}. SUBUNIT: Monomer. Interacts with ERBB2 (preferentially with the tyrosine phosphorylated form); this interaction occurs at the cell membrane and is increased in a growth factor heregulin-dependent manner. Interacts with SHC1; this interaction may mediate the binding of CPNE3 with ERBB2. Interacts with RACK1. {ECO:0000250|UniProtKB:O75131}. +A2A825 CPLN2_MOUSE Ciliogenesis and planar polarity effector 2 (REM2- and Rab-like small GTPase 1) 258 28,422 Chain (1); Nucleotide binding (2); Region (1) FUNCTION: Potential effector of the planar cell polarity signaling pathway. Plays a role in targeted membrane trafficking most probably at the level of vesicle fusion with membranes. Involved in cilium biogenesis by regulating the transport of cargo proteins to the basal body and to the apical tips of cilia. More generally involved in exocytosis in secretory cells (By similarity). {ECO:0000250|UniProtKB:Q6GNL4}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q6GNL4}. +P63040 CPLX1_MOUSE Complexin-1 (921-S) (Complexin I) (CPX I) (Synaphin-2) 134 15,122 Chain (1); Coiled coil (1); Region (1); Sequence conflict (1) FUNCTION: Positively regulates a late step in exocytosis of various cytoplasmic vesicles, such as synaptic vesicles and other secretory vesicles (PubMed:23345244). Organizes the SNAREs into a cross-linked zigzag topology that, when interposed between the vesicle and plasma membranes, is incompatible with fusion, thereby preventing SNAREs from releasing neurotransmitters until an action potential arrives at the synapse (PubMed:23345244). Also involved in glucose-induced secretion of insulin by pancreatic beta-cells. Essential for motor behavior (PubMed:15126625, PubMed:16000319). {ECO:0000269|PubMed:15126625, ECO:0000269|PubMed:16000319, ECO:0000269|PubMed:23345244}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:15126625, ECO:0000269|PubMed:7635198}. Note=Enriched at synaptic-releasing sites in mature neurons. SUBUNIT: Binds to the SNARE core complex containing SNAP25, VAMP2 and STX1A. {ECO:0000250|UniProtKB:O14810}. TISSUE SPECIFICITY: Nervous system, and pancreatic islet cells. Present in many brain regions, including hippocampus and cerebellum. In the retina, present at conventional amacrine cell synapses (at protein level). {ECO:0000269|PubMed:15126625, ECO:0000269|PubMed:15911881, ECO:0000269|PubMed:7635198}. +Q9D979 CQ064_MOUSE Uncharacterized protein C17orf64 homolog 236 27,118 Alternative sequence (1); Chain (1); Erroneous initiation (1); Sequence conflict (1) +Q6PIX9 CQ080_MOUSE Uncharacterized protein C17orf80 homolog 558 60,276 Alternative sequence (1); Chain (1); Erroneous termination (1); Sequence conflict (7); Topological domain (2); Transmembrane (1) TRANSMEM 528 548 Helical. {ECO:0000255}. TOPO_DOM 1 527 Extracellular. {ECO:0000255}.; TOPO_DOM 549 558 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q9CQF3 CPSF5_MOUSE Cleavage and polyadenylation specificity factor subunit 5 (Nucleoside diphosphate-linked moiety X motif 21) (Nudix motif 21) (Nudix hydrolase 21) 227 26,240 Chain (1); Domain (1); Initiator methionine (1); Modified residue (6); Motif (1); Region (3); Sequence conflict (1); Site (2) FUNCTION: Component of the cleavage factor Im (CFIm) complex that functions as an activator of the pre-mRNA 3'-end cleavage and polyadenylation processing required for the maturation of pre-mRNA into functional mRNAs. CFIm contributes to the recruitment of multiprotein complexes on specific sequences on the pre-mRNA 3'-end, so called cleavage and polyadenylation signals (pA signals). Most pre-mRNAs contain multiple pA signals, resulting in alternative cleavage and polyadenylation (APA) producing mRNAs with variable 3'-end formation. The CFIm complex acts as a key regulator of cleavage and polyadenylation site choice during APA through its binding to 5'-UGUA-3' elements localized in the 3'-untranslated region (UTR) for a huge number of pre-mRNAs. NUDT21/CPSF5 activates indirectly the mRNA 3'-processing machinery by recruiting CPSF6 and/or CPSF7. Binds to 5'-UGUA-3' elements localized upstream of pA signals that act as enhancers of pre-mRNA 3'-end processing. The homodimer mediates simultaneous sequence-specific recognition of two 5'-UGUA-3' elements within the pre-mRNA (By similarity). Plays a role in somatic cell fate transitions and pluripotency by regulating widespread changes in gene expression through an APA-dependent function(PubMed:29249356). Binds to chromatin (PubMed:18032416). Binds to, but does not hydrolyze mono- and di-adenosine nucleotides (By similarity). {ECO:0000250|UniProtKB:O43809, ECO:0000269|PubMed:18032416, ECO:0000269|PubMed:29249356}. PTM: Acetylated mainly by p300/CBP, recruited to the complex by CPSF6. Acetylation decreases interaction with PAPAO. Deacetylated by the class I/II HDACs, HDAC1, HDAC3 and HDAC10, and by the class III HDACs, SIRT1 AND SIRT2. {ECO:0000250|UniProtKB:O43809}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18032416}. Cytoplasm {ECO:0000250|UniProtKB:O43809}. Note=Shuttles between the nucleus and the cytoplasm in a transcription- and XPO1/CRM1-independent manner, most probably in complex with the cleavage factor Im complex (CFIm). In punctate subnuclear structures localized adjacent to nuclear speckles, called paraspeckles. {ECO:0000250|UniProtKB:O43809}. SUBUNIT: Homodimer (via N- and C-terminus); binds RNA as homodimer. Component of the cleavage factor Im (CFIm) complex which is an heterotetramer composed of two subunits of NUDT21/CPSF5 and two subunits of CPSF6 or CPSF7 or an heterodimer of CPSF6 and CPSF7. The cleavage factor Im (CFIm) complex associates with the CPSF and CSTF complexes to promote the assembly of the core mRNA 3'-processing machinery. Interacts with CPSF6 (via the RRM domain); this interaction is direct and enhances binding to RNA. Interacts with CPSF7. Interacts with FIP1L1; this interaction occurs in a RNA sequence-specific manner. Interacts with PABPN1 (By similarity). Interacts (via N-terminus) with PAPOLA (via C-terminus); this interaction is direct and diminished by acetylation (PubMed:11716503). Interacts with SNRNP70 (By similarity). Interacts with VIRMA (By similarity). {ECO:0000250|UniProtKB:O43809, ECO:0000269|PubMed:11716503}. TISSUE SPECIFICITY: Expressed in testis (PubMed:18032416). Expressed in male germ cells (at protein level) (PubMed:18032416). {ECO:0000269|PubMed:18032416}. +O88843 CRADD_MOUSE Death domain-containing protein CRADD (Caspase and RIP adapter with death domain) (RIP-associated protein with a death domain) 199 22,656 Chain (1); Domain (2); Mutagenesis (1); Sequence conflict (1) FUNCTION: Adapter protein that associates with PIDD1 and the caspase CASP2 to form the PIDDosome, a complex that activates CASP2 and triggers apoptosis. Also recruits CASP2 to the TNFR-1 signaling complex through its interaction with RIPK1 and TRADD and may play a role in the tumor necrosis factor-mediated signaling pathway. {ECO:0000250|UniProtKB:P78560}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22279524}. Nucleus {ECO:0000269|PubMed:22279524}. SUBUNIT: Forms a complex named the PIDDosome with PIDD1 and CASP2 (PubMed:22279524). Interacts (via Death domain) with RIPK1 (via Death domain); the interaction is direct. Interacts with TRADD. Interacts with TNFRSF1A (By similarity). {ECO:0000250|UniProtKB:P78560, ECO:0000269|PubMed:22279524}. DOMAIN: The Death domain mediates the interaction with PIDD1 and the formation of a complex composed of 5 PIDD1 and 7 CRADD proteins which in turn probably recruit 7 CASP2 to form the PIDDosome. The Death domain mediates a direct interaction with the Death domain of RIPK1. {ECO:0000250|UniProtKB:P78560}.; DOMAIN: The CARD domain mediates a direct interaction with CASP2. {ECO:0000250|UniProtKB:P78560}. +Q9D3S9 CPVL_MOUSE Probable serine carboxypeptidase CPVL (EC 3.4.16.-) 478 54,763 Active site (3); Alternative sequence (1); Chain (1); Glycosylation (4); Propeptide (1); Signal peptide (1) FUNCTION: May be involved in the digestion of phagocytosed particles in the lysosome, participation in an inflammatory protease cascade, and trimming of peptides for antigen presentation. {ECO:0000250}. +Q9Z2B5 E2AK3_MOUSE Eukaryotic translation initiation factor 2-alpha kinase 3 (EC 2.7.11.1) (PRKR-like endoplasmic reticulum kinase) (Pancreatic eIF2-alpha kinase) 1114 124,682 Active site (1); Beta strand (22); Binding site (1); Chain (1); Compositional bias (2); Domain (1); Glycosylation (1); Helix (15); Modified residue (4); Mutagenesis (1); Nucleotide binding (1); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (3) TRANSMEM 511 531 Helical. {ECO:0000255}. TOPO_DOM 29 510 Lumenal. {ECO:0000255}.; TOPO_DOM 532 1114 Cytoplasmic. {ECO:0000255}. FUNCTION: Metabolic-stress sensing protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (eIF-2-alpha/EIF2S1) on 'Ser-52' during the unfolded protein response (UPR) and in response to low amino acid availability (PubMed:11106749). Converts phosphorylated eIF-2-alpha/EIF2S1 either in a global protein synthesis inhibitor, leading to a reduced overall utilization of amino acids, or to a translation initiation activator of specific mRNAs, such as the transcriptional activator ATF4, and hence allowing ATF4-mediated reprogramming of amino acid biosynthetic gene expression to alleviate nutrient depletion (PubMed:23921556). Serves as a critical effector of unfolded protein response (UPR)-induced G1 growth arrest due to the loss of cyclin-D1 (CCND1) (PubMed:11035797). Involved in control of mitochondrial morphology and function (PubMed:23921556). {ECO:0000269|PubMed:11035797, ECO:0000269|PubMed:11106749, ECO:0000269|PubMed:23921556}. PTM: Autophosphorylated. Phosphorylated at Tyr-615 following endoplasmic reticulum stress, leading to activate its tyrosine-protein kinase activity. Dephosphorylated by PTPN1/TP1B, leading to inactivate its enzyme activity (By similarity). Oligomerization of the N-terminal ER luminal domain by ER stress promotes PERK trans-autophosphorylation of the C-terminal cytoplasmic kinase domain at multiple residues including Thr-980 on the kinase activation loop. {ECO:0000250, ECO:0000269|PubMed:21543844}.; PTM: N-glycosylated.; PTM: ADP-ribosylated by PARP16 upon ER stress, which increases kinase activity. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein. SUBUNIT: Forms dimers with HSPA5/BIP in resting cells (PubMed:21543844). Oligomerizes in ER-stressed cells (PubMed:10854322). Interacts with DNAJC3 (PubMed:12446838). Interacts with MFN2 (PubMed:23921556). Interacts with TMEM33 (By similarity). Interacts with PDIA6 (By similarity). {ECO:0000250|UniProtKB:Q9NZJ5, ECO:0000269|PubMed:10854322, ECO:0000269|PubMed:12446838, ECO:0000269|PubMed:21543844, ECO:0000269|PubMed:23921556}. DOMAIN: The lumenal domain senses perturbations in protein folding in the ER, probably through reversible interaction with HSPA5/BIP. TISSUE SPECIFICITY: Ubiquitous. +Q01147 CREB1_MOUSE Cyclic AMP-responsive element-binding protein 1 (CREB-1) (cAMP-responsive element-binding protein 1) 341 36,674 Alternative sequence (1); Chain (1); Cross-link (3); Domain (2); Helix (1); Modified residue (3); Mutagenesis (3); Region (2); Site (1) FUNCTION: Phosphorylation-dependent transcription factor that stimulates transcription upon binding to the DNA cAMP response element (CRE), a sequence present in many viral and cellular promoters. Transcription activation is enhanced by the TORC coactivators which act independently of Ser-133 phosphorylation. Involved in different cellular processes including the synchronization of circadian rhythmicity and the differentiation of adipose cells. {ECO:0000269|PubMed:11970866, ECO:0000269|PubMed:21728997}. PTM: Phosphorylation of Ser-133 allows CREBBP binding. Stimulated by phosphorylation. Phosphorylated Ser-142 can be detected in the suprachiasmatic nucleus (SCN), the amygdala, the cortex, and the hippocampus but not in the striatum nor in the cerebellum. In the SCN, phosphorylation of Ser-142 and Ser-133 are stimulated by light exposure and submitted to circadian oscillations. In the retina, only phosphorylation of Ser-133 can be detected upon light exposure. Phosphorylation of both Ser-133 and Ser-142 in the SCN regulates the activity of CREB and participates in circadian rhythm generation. Phosphorylated upon calcium influx by CaMK4 and CaMK2 on Ser-133. CaMK4 is much more potent than CAMK2 in activating CREB. Phosphorylated by CaMK2 on Ser-142. Phosphorylation of Ser-142 blocks CREB-mediated transcription even when Ser-133 is phosphorylated. Phosphorylated by CaMK1. Phosphorylation of Ser-271 by HIPK2 in response to genotoxic stress promotes CREB1 activity, facilitating the recruitment of the coactivator CBP (By similarity). Phosphorylated at Ser-133 by RPS6KA3, RPS6KA4 and RPS6KA5 in response to mitogenic or stress stimuli. CREBL2 positively regulates phosphorylation at Ser-133 thereby stimulating CREB1 transcriptional activity. In liver, phosphorylation is induced by fasting or glucagon in a circadian fashion. Phosphorylated by TSSK4 on Ser-133 (By similarity). {ECO:0000250|UniProtKB:P16220, ECO:0000269|PubMed:11970866, ECO:0000269|PubMed:18690222, ECO:0000269|PubMed:20852621, ECO:0000269|PubMed:8552098}.; PTM: Sumoylated with SUMO1. Sumoylation on Lys-304, but not on Lys-285, is required for nuclear localization of this protein. Sumoylation is enhanced under hypoxia, promoting nuclear localization and stabilization (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00312, ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:21728997}. SUBUNIT: Interacts with PPRC1. Binds DNA as a dimer. This dimer is stabilized by magnesium ions. Interacts, through the bZIP domain, with the coactivators TORC1/CRTC1, TORC2/CRTC2 and TORC3/CRTC3. Interacts (phosphorylated form) with TOX3 (By similarity). When phosphorylated on Ser-133, binds CREBBP. Interacts with ARRB1. Binds to HIPK2 (By similarity). Interacts with SGK1 (By similarity). Interacts with CREBL2; regulates CREB1 phosphorylation, stability and transcriptional activity. Interacts with TSSK4; this interaction facilitates phosphorylation on Ser-133 (By similarity). {ECO:0000250|UniProtKB:P16220, ECO:0000269|PubMed:10952992, ECO:0000269|PubMed:21728997, ECO:0000269|PubMed:8552098}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:1387109}. +Q8VEA6 CRDL2_MOUSE Chordin-like protein 2 426 47,765 Chain (1); Domain (3); Frameshift (1); Glycosylation (2); Modified residue (1); Sequence conflict (2); Signal peptide (1) FUNCTION: Implicated in tumor angiogenesis (By similarity). May inhibits BMPs activity by blocking their interaction with their receptors. Has a negative regulator effect on the cartilage formation/regeneration from immature mesenchymal cells, by preventing or reducing the rate of matrix accumulation. May play a role during myoblast and osteoblast differentiation, and maturation. {ECO:0000250, ECO:0000269|PubMed:14660436, ECO:0000269|PubMed:15094188}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Interacts with GDF5. May interact with INHBA, BMP2, BMP4, BMP5, BMP6, and BMP7. {ECO:0000269|PubMed:14660436}. TISSUE SPECIFICITY: Weakly expressed in the liver and kidney. In reproductive organs expressed in connective tissues such as ligaments of the ovary and oviduct in females, and of testis, epididymis and certain male accessory sex glands in males. Expression was high in uterine myometrium. Weakly expressed in cartilage of the femoral head, patella, articular facets of vertebrae, in the annulus fibrosus of intervertebral disks. In normal cartilage, expression was confined to articular chondrocytes especially in the superficial zone. {ECO:0000269|PubMed:14660436}. +P47941 CRKL_MOUSE Crk-like protein 303 33,830 Chain (1); Domain (3); Modified residue (2); Sequence conflict (1) FUNCTION: May mediate the transduction of intracellular signals. PTM: Phosphorylated on tyrosine. Phosphorylation is prominent during early development, but decreases at later embryonic stages and in newborn mice. SUBUNIT: Interacts with DOCK2 and EPOR. Interacts with phosphorylated CBLB and IRS4 (By similarity). Interacts with INPP5D/SHIP1. {ECO:0000250, ECO:0000269|PubMed:11031258}. +Q8CJ40 CROCC_MOUSE Rootletin (Ciliary rootlet coiled-coil protein) 2009 226,945 Alternative sequence (3); Chain (1); Coiled coil (6); Erroneous initiation (1); Modified residue (9); Sequence conflict (7) FUNCTION: Major structural component of the ciliary rootlet, a cytoskeletal-like structure in ciliated cells which originates from the basal body at the proximal end of a cilium and extends proximally toward the cell nucleus (PubMed:12427867). Furthermore, is required for the correct positioning of the cilium basal body relative to the cell nucleus, to allow for ciliogenesis (By similarity). Contributes to centrosome cohesion before mitosis (By similarity). {ECO:0000250|UniProtKB:Q5TZA2, ECO:0000269|PubMed:12427867}. PTM: Phosphorylated by NEK2 which may regulate its association with centrosomes. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:12427867, ECO:0000269|PubMed:16339073}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q5TZA2}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q5TZA2}. Note=In ciliated cells, associated with ciliary rootlets. In non-ciliated cells, localized between, around and at the proximal ends of the centrioles. Dissociates from the centrioles at the onset of mitosis and reassociates with them at anaphase. {ECO:0000269|PubMed:12427867, ECO:0000269|PubMed:16339073}. SUBUNIT: Homopolymer. Interacts with KLC3, NEK2 and the N-terminus of CEP250. {ECO:0000269|PubMed:12427867, ECO:0000269|PubMed:16339073}. TISSUE SPECIFICITY: Highest expression detected in photoreceptor cells of retina. Expressed at lower levels in brain, trachea and kidney. Detected in all major ciliated epithelia. During embryonic development, enriched along the apical domains of neuroepithelium in brain ventricular zone, in primordia of retinal pigment epithelia and in neural retina. {ECO:0000269|PubMed:12427867}. +Q9JMC8 E41LB_MOUSE Band 4.1-like protein 4B (Protein EHM2) 527 59,564 Chain (1); Domain (1); Mutagenesis (4); Sequence conflict (1) FUNCTION: Up-regulates the activity of the Rho guanine nucleotide exchange factor ARHGEF18 (PubMed:22006950). Involved in the regulation of the circumferential actomyosin belt in epithelial cells (PubMed:22006950). Promotes cellular adhesion, migration and motility in vitro and may play a role in wound healing (By similarity). May have a role in mediating cytoskeletal changes associated with steroid-induced cell differentiation (By similarity). {ECO:0000250|UniProtKB:Q9H329, ECO:0000269|PubMed:22006950}. PTM: May be negatively regulated by phosphorylation. {ECO:0000269|PubMed:22006950}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H329}. Cell junction, tight junction {ECO:0000250|UniProtKB:Q9H329}. Note=Accumulates along apical cell-cell boundaries and is also detected in the cytoplasm in a punctate manner. {ECO:0000250|UniProtKB:Q9H329}. SUBUNIT: Interacts (via FERM domain) with ARHGEF18 (via C-terminus); the interaction activates ARHGEF18. {ECO:0000269|PubMed:22006950}. TISSUE SPECIFICITY: Expressed in mouse liver cells, with lower amounts in lung, kidney and in 7- to 17-day embryos. Expression not detected in adult mouse heart, brain, spleen, skeletal muscle or testis. {ECO:0000269|PubMed:10783258}. +Q8CCE9 E4F1_MOUSE Transcription factor E4F1 (EC 2.3.2.27) (E4F transcription factor 1) (Putative E3 ubiquitin-protein ligase E4F1) (RING-type E3 ubiquitin transferase E4F1) (Transcription factor E4F) (Transcription factor phi AP3) (p120E4F) 783 84,296 Alternative sequence (6); Chain (1); Erroneous initiation (2); Frameshift (2); Modified residue (1); Region (6); Sequence conflict (31); Zinc finger (9) Protein modification; protein ubiquitination. FUNCTION: May function as a transcriptional repressor. May also function as a ubiquitin ligase mediating ubiquitination of chromatin-associated TP53. Functions in cell survival and proliferation through control of the cell cycle. Functions in the p53 and pRB tumor suppressor pathways and regulates the cyclin CCNA2 transcription. {ECO:0000269|PubMed:10644996, ECO:0000269|PubMed:15226446, ECO:0000269|PubMed:17557114, ECO:0000269|PubMed:8262041}. PTM: Phosphorylated; phosphorylation is cell cycle-dependent and regulates DNA-binding activity and function. {ECO:0000269|PubMed:8262041}.; PTM: May be sumoylated by UBE2I upon interaction with CDKN2A. {ECO:0000250|UniProtKB:Q66K89}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:15226446, ECO:0000269|PubMed:8262041}. Cytoplasm {ECO:0000250}. Note=A small fraction is detected in the cytoplasm (By similarity). Excluded from the nucleolus where it is targeted upon CDKN2A overexpression. Localizes to the mitotic spindle during embryogenesis. {ECO:0000250}. SUBUNIT: Homodimer; binds DNA as a dimer (By similarity). Forms a complex with CDKN2A and TP53. Interacts with HDAC1, HMGA2 and RASSF1 (By similarity). Interactions with TP53, RB1, ANP32A and probably BMI1 and FHL2 regulate E4F1 activity. {ECO:0000250|UniProtKB:Q66K89, ECO:0000269|PubMed:10644996, ECO:0000269|PubMed:10869426, ECO:0000269|PubMed:17557114}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:8262041, ECO:0000269|PubMed:9530632}. +Q6ZPS2 CRNS1_MOUSE Carnosine synthase 1 (EC 6.3.2.11) (ATP-grasp domain-containing protein 1) 827 89,281 Alternative sequence (3); Chain (1); Domain (1); Erroneous initiation (1); Metal binding (4); Nucleotide binding (1); Sequence conflict (2) FUNCTION: Catalyzes the synthesis of carnosine and homocarnosine. Carnosine is synthesized more efficiently than homocarnosine. {ECO:0000269|PubMed:20097752}. SUBUNIT: Homotetramer. {ECO:0000305|PubMed:20097752}. +Q9D1E4 CRTP1_MOUSE Cysteine-rich tail protein 1 142 15,108 Chain (1); Compositional bias (1); Sequence conflict (1) +P23927 CRYAB_MOUSE Alpha-crystallin B chain (Alpha(B)-crystallin) (P23) 175 20,069 Chain (1); Domain (1); Metal binding (5); Modified residue (8) FUNCTION: May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P02511}. Nucleus {ECO:0000250|UniProtKB:P02511}. Note=Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles. Localizes at the Z-bands and the intercalated disk in cardiomyocytes. {ECO:0000250|UniProtKB:P02511}. SUBUNIT: Heteropolymer composed of three CRYAA and one CRYAB subunits. Aggregates with homologous proteins, including the small heat shock protein HSPB1, to form large heteromeric complexes. Inter-subunit bridging via zinc ions enhances stability, which is crucial as there is no protein turn over in the lens (By similarity). Interacts with HSPBAP1 (PubMed:10751411). Interacts with TTN/titin. Interacts with TMEM109. Interacts with DES; binds rapidly during early stages of DES filament assembly and a reduced binding seen in the later stages (By similarity). {ECO:0000250|UniProtKB:P02511, ECO:0000269|PubMed:10751411}. TISSUE SPECIFICITY: Lens as well as other tissues. +Q9D7E4 CS025_MOUSE UPF0449 protein C19orf25 homolog 109 12,112 Chain (1); Coiled coil (1); Modified residue (1) +Q922C1 CS044_MOUSE Uncharacterized protein C19orf44 homolog 641 69,273 Chain (1); Modified residue (2); Sequence conflict (8) +O35486 CRYGS_MOUSE Gamma-crystallin S (Beta-crystallin S) (Gamma-S-crystallin) 178 20,850 Beta strand (15); Chain (1); Domain (4); Helix (3); Initiator methionine (1); Modified residue (1); Region (2); Turn (4) FUNCTION: Crystallins are the dominant structural components of the vertebrate eye lens. SUBUNIT: Monomer. {ECO:0000250}. DOMAIN: Has a two-domain beta-structure, folded into four very similar Greek key motifs. +Q8CH19 CS2IP_MOUSE Casein kinase II subunit alpha'-interacting protein (CK2 target protein 2) 720 79,205 Chain (1); Compositional bias (2); Erroneous gene model prediction (1); Erroneous initiation (2) FUNCTION: May play a role in chromatin regulation of male germ cells. {ECO:0000305|PubMed:19273531}. PTM: Phosphorylated by CK2 (casein kinase II), specifically by complexes containing catalytic subunit CSNK2A2. {ECO:0000269|PubMed:19273531}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19273531}. Note=Present in nuclei of spermatids during chromatin condensation. {ECO:0000269|PubMed:19273531}. SUBUNIT: Interacts (via C-terminus) with CSNK2A2. {ECO:0000269|PubMed:19273531}. TISSUE SPECIFICITY: Expressed exclusively in testis (at protein level). Within testis, expressed mainly in the intermediate compartment of the seminiferous tubules with weaker expression in the basal and adluminal compartments. {ECO:0000269|PubMed:19273531}. +Q02862 CS2LA_MOUSE Alpha-S2-casein-like A (Casein alpha S2-like A) (Gamma-casein) (PP22) 184 21,101 Chain (1); Modified residue (4); Signal peptide (1) FUNCTION: Important role in the capacity of milk to transport calcium phosphate. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Mammary gland-specific. Secreted in milk. +P02664 CS2LB_MOUSE Alpha-S2-casein-like B (Casein alpha S2-like B) (Epsilon-casein) 143 16,911 Chain (1); Sequence conflict (3); Signal peptide (1) FUNCTION: Important role in the capacity of milk to transport calcium phosphate. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Mammary gland specific. Secreted in milk. +Q8CG14 CS1A_MOUSE Complement C1s-A subcomponent (EC 3.4.21.42) (C1 esterase) (Complement component 1 subcomponent s-A) [Cleaved into: Complement C1s-A subcomponent heavy chain; Complement C1s-A subcomponent light chain] 688 76,858 Active site (3); Chain (3); Disulfide bond (13); Domain (6); Erroneous initiation (1); Glycosylation (2); Metal binding (9); Modified residue (1); Sequence conflict (7); Signal peptide (1) FUNCTION: C1s B chain is a serine protease that combines with C1q and C1r to form C1, the first component of the classical pathway of the complement system. C1r activates C1s so that it can, in turn, activate C2 and C4 (By similarity). {ECO:0000250}. PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}. SUBUNIT: C1 is a calcium-dependent trimolecular complex of C1q, C1r and C1s in the molar ration of 1:2:2. Activated C1s is an disulfide-linked heterodimer of a heavy chain and a light chain (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Predominantly expressed in liver. {ECO:0000269|PubMed:12513694}. +Q0V8T8 CTP5B_MOUSE Contactin-associated protein like 5-2 (Cell recognition molecule Caspr5-2) (Cell recognition molecule Caspr5b) (Contactin-associated protein-like 5b) 1292 144,260 Alternative sequence (1); Chain (1); Compositional bias (2); Disulfide bond (11); Domain (8); Frameshift (1); Glycosylation (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1225 1245 Helical. {ECO:0000255}. TOPO_DOM 25 1224 Extracellular. {ECO:0000255}.; TOPO_DOM 1246 1292 Cytoplasmic. {ECO:0000255}. FUNCTION: May play a role in the correct development and proper functioning of the peripheral and central nervous system and be involved in cell adhesion and intercellular communication. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in brain. {ECO:0000269|PubMed:16845472}. +Q8BY89 CTL2_MOUSE Choline transporter-like protein 2 (Solute carrier family 44 member 2) 706 80,110 Alternative sequence (1); Chain (1); Glycosylation (3); Modified residue (1); Topological domain (11); Transmembrane (10) TRANSMEM 34 54 Helical. {ECO:0000255}.; TRANSMEM 233 253 Helical. {ECO:0000255}.; TRANSMEM 257 277 Helical. {ECO:0000255}.; TRANSMEM 316 336 Helical. {ECO:0000255}.; TRANSMEM 365 385 Helical. {ECO:0000255}.; TRANSMEM 455 477 Helical. {ECO:0000255}.; TRANSMEM 505 525 Helical. {ECO:0000255}.; TRANSMEM 564 584 Helical. {ECO:0000255}.; TRANSMEM 600 620 Helical. {ECO:0000255}.; TRANSMEM 639 659 Helical. {ECO:0000255}. TOPO_DOM 1 33 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 55 232 Extracellular. {ECO:0000255}.; TOPO_DOM 254 256 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 278 315 Extracellular. {ECO:0000255}.; TOPO_DOM 337 364 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 386 454 Extracellular. {ECO:0000255}.; TOPO_DOM 478 504 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 526 563 Extracellular. {ECO:0000255}.; TOPO_DOM 585 599 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 621 638 Extracellular. {ECO:0000255}.; TOPO_DOM 660 706 Cytoplasmic. {ECO:0000255}. FUNCTION: Choline transporter. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with COCH. {ECO:0000250}. TISSUE SPECIFICITY: Expressed at high levels in lung, colon, inner ear and spleen (at protein level). Progressively lower levels in brain, tongue, liver and kidney (at protein level). In the kidney, prominent expression in glomeruli in the lining of Bowman's capsule and on the mesangial cells adjacent to the vessels within the glomerulus (at protein level). Strongly expressed on the membranes of splenocytes and in lung parenchyme (at protein level). Isoform 1 is expressed at higher levels than isoform 2 in colon, heart, kidney, lung, cochlea, tongue and muscle, as well as in the inner ear. Isoform 2 is predominant in brain, liver and spleen. {ECO:0000269|PubMed:20665236}. +Q921V7 CTL3_MOUSE Choline transporter-like protein 3 (Solute carrier family 44 member 3) 656 73,414 Chain (1); Glycosylation (5); Transmembrane (8) TRANSMEM 37 57 Helical. {ECO:0000255}.; TRANSMEM 216 236 Helical. {ECO:0000255}.; TRANSMEM 242 262 Helical. {ECO:0000255}.; TRANSMEM 288 308 Helical. {ECO:0000255}.; TRANSMEM 337 357 Helical. {ECO:0000255}.; TRANSMEM 381 401 Helical. {ECO:0000255}.; TRANSMEM 537 557 Helical. {ECO:0000255}.; TRANSMEM 566 586 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q80YR6 CTIP_MOUSE DNA endonuclease RBBP8 (EC 3.1.-.-) (CtBP-interacting protein) (CtIP) (Retinoblastoma-binding protein 8) (RBBP-8) (Retinoblastoma-interacting protein and myosin-like) (RIM) (Sporulation in the absence of SPO11 protein 2 homolog) (SAE2) 893 100,831 Chain (1); Coiled coil (1); Cross-link (21); Modified residue (15); Motif (1); Region (3) FUNCTION: Endonuclease that cooperates with the MRE11-RAD50-NBN (MRN) complex in DNA-end resection, the first step of double-strand break (DSB) repair through the homologous recombination (HR) pathway. HR is restricted to S and G2 phases of the cell cycle and preferentially repairs DSBs resulting from replication fork collapse. Key determinant of DSB repair pathway choice, as it commits cells to HR by preventing classical non-homologous end-joining (NHEJ). Functions downstream of the MRN complex and ATM, promotes ATR activation and its recruitment to DSBs in the S/G2 phase facilitating the generation of ssDNA. Component of the BRCA1-RBBP8 complex that regulates CHEK1 activation and controls cell cycle G2/M checkpoints on DNA damage. During immunoglobulin heavy chain class-switch recombination, promotes microhomology-mediated alternative end joining (A-NHEJ) and plays an essential role in chromosomal translocations. {ECO:0000269|PubMed:20829486, ECO:0000269|PubMed:21131978, ECO:0000269|PubMed:21131982}. PTM: Hyperphosphorylation upon ionizing radiation results in dissociation from BRCA1. Phosphorylation at Thr-843 by CDK1 is essential for the recruitment to DNA and the DNA repair function. Phosphorylated at Ser-326 as cells enter G2 phase. This phosphorylation is required for binding BRCA1 and for the G2/M DNA damage transition checkpoint control (By similarity). Phosphorylation at Thr-315 is required for PIN1-binding, while phosphorylation at Ser-276 serves as a PIN1 isomerization site. Phosphorylation at Thr-315 is cell-cycle dependent. It steadily increases during S phase, peaks at late S/G2 phase, and drops at G1 (By similarity). {ECO:0000250|UniProtKB:Q99708}.; PTM: Acetylated. Deacetylation by SIRT6 upon DNA damage promotes DNA end resection. {ECO:0000250|UniProtKB:Q99708}.; PTM: Ubiquitinated. Ubiquitination at multiple sites by BRCA1 (via its N-terminal RING domain) does not lead to its proteosomal degradation but instead the ubiquitinated RBBP8 binds to chromatin following DNA damage and may play a role in G2/M checkpoint control. Ubiquitinated by RNF138 at its N-terminus. Ubiquitinated through 'Lys-48' by the E3 CUL3-KLHL15 complex; this modification leads to proteasomal degradation. Ubiquitinated by the E3 FZR1/APC/C complex; this modification leads to proteasomal degradation. {ECO:0000250|UniProtKB:Q99708}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q99708}. Chromosome {ECO:0000250|UniProtKB:Q99708}. Note=Associates with sites of DNA damage in S/G2 phase. Ubiquitinated RBBP8 binds to chromatin following DNA damage. {ECO:0000250|UniProtKB:Q99708}. SUBUNIT: Homodimer; dimerizes via the coiled coil domain. Interacts (via the PXDLS motif) with CTBP1; the interaction is disrupted via binding of the adenovirus E1A to CTBP1. Component of the BRCA1-RBBP8 complex. Interacts (the Ser-326 phosphorylated form) with BRCA1 (via the C-terminal BRCA1 domains): the interaction occurs in the G2 phase, ubiquitinates RBBP8 and involves RBBP8 in BRCA1-dependent G2/M checkpoint control on DNA damage. Interacts with RB1. Interacts with the MRN complex. Interacts directly with MRE11; the interaction is required for efficient homologous recombination (HR) and regulation of the MRN complex. Interacts directly with RAD50. Interacts directly with NBN. Interacts with SIRT6; the interaction deacetylates RBBP8 upon DNA damage. Interacts with LM04 (via the LIM zinc-binding 1 domain). Interacts with SIAH1. Interacts with RNF138. Interacts with EXD2. Interacts with CUL3 and KLHL15; this interaction leads to RBBP8 proteasomal degradation. Directly interacts with PIN1; this interaction depends upon RBBP8 phosphorylation, predominantly at Thr-315. Interacts with FZR1; this interaction leads to APC/C-mediated RBBP8 proteasomal degradation. Interacts with AUNIP; leading to recruit RBBP8 to sites of DNA damage. Interacts with SAMHD1. {ECO:0000250|UniProtKB:Q99708}. DOMAIN: The damage-recruitment motif is required for DNA binding and translocation to sites of DNA damage. {ECO:0000250}.; DOMAIN: The PXDLS motif binds to a cleft in CtBP proteins. {ECO:0000250|UniProtKB:Q99708}. +P18581 CTR2_MOUSE Cationic amino acid transporter 2 (CAT-2) (CAT2) (20.5) (Low affinity cationic amino acid transporter 2) (Solute carrier family 7 member 2) (T-cell early activation protein) (TEA) 657 71,856 Alternative sequence (1); Chain (1); Glycosylation (3); Modified residue (3); Sequence conflict (59); Topological domain (15); Transmembrane (14) TRANSMEM 38 59 Helical. {ECO:0000255}.; TRANSMEM 64 84 Helical. {ECO:0000255}.; TRANSMEM 105 125 Helical. {ECO:0000255}.; TRANSMEM 164 184 Helical. {ECO:0000255}.; TRANSMEM 193 213 Helical. {ECO:0000255}.; TRANSMEM 249 269 Helical. {ECO:0000255}.; TRANSMEM 290 309 Helical. {ECO:0000255}.; TRANSMEM 340 360 Helical. {ECO:0000255}.; TRANSMEM 386 406 Helical. {ECO:0000255}.; TRANSMEM 410 430 Helical. {ECO:0000255}.; TRANSMEM 490 510 Helical. {ECO:0000255}.; TRANSMEM 524 548 Helical. {ECO:0000255}.; TRANSMEM 557 577 Helical. {ECO:0000255}.; TRANSMEM 582 602 Helical. {ECO:0000255}. TOPO_DOM 1 37 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 60 63 Extracellular. {ECO:0000255}.; TOPO_DOM 85 104 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 126 163 Extracellular. {ECO:0000255}.; TOPO_DOM 185 192 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 214 248 Extracellular. {ECO:0000255}.; TOPO_DOM 270 289 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 310 339 Extracellular. {ECO:0000255}.; TOPO_DOM 361 385 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 407 409 Extracellular. {ECO:0000255}.; TOPO_DOM 431 489 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 511 523 Extracellular. {ECO:0000255}.; TOPO_DOM 549 556 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 578 581 Extracellular. {ECO:0000255}.; TOPO_DOM 603 657 Cytoplasmic. {ECO:0000255}. FUNCTION: Isoform 1 functions as low-affinity, high capacity permease involved in the transport of the cationic amino acids (arginine, lysine and ornithine). Isoform 2 also functions as permease that mediates the transport of the cationic amino acids (arginine, lysine and ornithine), but it has much higher affinity for arginine than isoform 1. May play a role in classical or alternative activation of macrophages via its role in arginine transport. {ECO:0000269|PubMed:16670299, ECO:0000269|PubMed:8195186, ECO:0000269|PubMed:8385111}. PTM: N-glycosylated. {ECO:0000269|PubMed:8385111}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8195186, ECO:0000269|PubMed:8385111}; Multi-pass membrane protein {ECO:0000269|PubMed:8195186, ECO:0000269|PubMed:8385111}. TISSUE SPECIFICITY: Detected in liver (at protein level) (PubMed:8385111). Highest expression in liver and T-cells. Also expressed in brain and lung. {ECO:0000269|PubMed:16239143, ECO:0000269|PubMed:8385111}. +Q3UJB9 EDC4_MOUSE Enhancer of mRNA-decapping protein 4 1406 152,484 Alternative sequence (1); Chain (1); Coiled coil (1); Compositional bias (1); Initiator methionine (1); Modified residue (26); Repeat (4); Sequence conflict (4) FUNCTION: In the process of mRNA degradation, seems to play a role in mRNA decapping. Component of a complex containing DCP2 and DCP1A which functions in decapping of ARE-containing mRNAs. Promotes complex formation between DCP1A and DCP2. Enhances the catalytic activity of DCP2 (in vitro). {ECO:0000250|UniProtKB:Q6P2E9}. SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000250|UniProtKB:Q6P2E9}. Nucleus {ECO:0000250|UniProtKB:Q6P2E9}. SUBUNIT: Part of a decapping complex consisting of DCP1A, DCP2, EDC3, EDC4 and probably DDX6. Part of a complex consisting of DCP1A, EDC3, EDC4 and DDX6. Part of a complex consisting of DCP1B, EDC3, EDC4 and DDX6. Interacts with DCP2 (By similarity). Interacts with RC3H1 (PubMed:20639877, PubMed:23583643). Interacts with NBDY (By similarity). Interacts with Tex19.1 and, probably, Tex19.2 (PubMed:28254886). {ECO:0000250|UniProtKB:Q6P2E9, ECO:0000269|PubMed:20639877, ECO:0000269|PubMed:23583643, ECO:0000269|PubMed:28254886}. +Q91ZR5 CTSR1_MOUSE Cation channel sperm-associated protein 1 (CatSper1) 686 78,706 Chain (1); Compositional bias (1); Intramembrane (1); Natural variant (5); Topological domain (8); Transmembrane (6) INTRAMEM 522 542 Helical; Pore-forming. {ECO:0000255}. TRANSMEM 350 370 Helical; Name=Segment S1. {ECO:0000255}.; TRANSMEM 384 404 Helical; Name=Segment S2. {ECO:0000255}.; TRANSMEM 418 438 Helical; Name=Segment S3. {ECO:0000255}.; TRANSMEM 448 468 Helical; Name=Segment S4. {ECO:0000255}.; TRANSMEM 486 506 Helical; Name=Segment S5. {ECO:0000255}.; TRANSMEM 553 573 Helical; Name=Segment S6. {ECO:0000255}. TOPO_DOM 1 349 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 371 383 Extracellular. {ECO:0000255}.; TOPO_DOM 405 417 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 439 447 Extracellular. {ECO:0000255}.; TOPO_DOM 469 485 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 507 521 Extracellular. {ECO:0000255}.; TOPO_DOM 543 552 Extracellular. {ECO:0000255}.; TOPO_DOM 574 686 Cytoplasmic. {ECO:0000255}. FUNCTION: Voltage-gated calcium channel that plays a central role in sperm cell hyperactivation. Controls calcium entry to mediate the hyperactivated motility, a step needed for sperm motility which is essential late in the preparation of sperm for fertilization. Activated by intracellular alkalinization. {ECO:0000269|PubMed:11595941, ECO:0000269|PubMed:14657352, ECO:0000269|PubMed:16036917, ECO:0000269|PubMed:16467839, ECO:0000269|PubMed:17174296}. SUBCELLULAR LOCATION: Cell projection, cilium, flagellum membrane {ECO:0000269|PubMed:11595941}; Multi-pass membrane protein {ECO:0000269|PubMed:11595941}. Note=Specifically located in the principal piece of sperm tail. SUBUNIT: Heterotetramer; possibly composed of CATSPER1, CATSPER2, CATSPER3 and CATSPER4 (Potential). Interacts with Ca(v)3.3/CACNA1I, leading to suppress T-type calcium channel activity (By similarity). Component of the CatSper complex. Interacts with CATSPER3 and CATSPER4. {ECO:0000250, ECO:0000269|PubMed:17227845, ECO:0000269|PubMed:17478420, ECO:0000269|PubMed:19516020, ECO:0000269|PubMed:21224844, ECO:0000305}. TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:11595941}. +Q3SYP2 CTRC_MOUSE Chymotrypsin-C (EC 3.4.21.2) 268 29,470 Active site (3); Chain (1); Disulfide bond (5); Domain (1); Glycosylation (4); Propeptide (1); Signal peptide (1) FUNCTION: Has chymotrypsin-type protease activity and hypocalcemic activity. {ECO:0000250}. +Q80W99 CTSR3_MOUSE Cation channel sperm-associated protein 3 (CatSper3) 395 45,486 Alternative sequence (1); Chain (1); Intramembrane (1); Sequence caution (1); Sequence conflict (1); Topological domain (8); Transmembrane (6) INTRAMEM 210 230 Helical; Pore-forming. {ECO:0000255}. TRANSMEM 50 70 Helical; Name=Segment S1. {ECO:0000255}.; TRANSMEM 88 108 Helical; Name=Segment S2. {ECO:0000255}.; TRANSMEM 111 131 Helical; Name=Segment S3. {ECO:0000255}.; TRANSMEM 142 161 Helical; Name=Segment S4. {ECO:0000255}.; TRANSMEM 180 200 Helical; Name=Segment S5. {ECO:0000255}.; TRANSMEM 249 269 Helical; Name=Segment S6. {ECO:0000255}. TOPO_DOM 1 49 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 71 87 Extracellular. {ECO:0000255}.; TOPO_DOM 109 110 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 132 141 Extracellular. {ECO:0000255}.; TOPO_DOM 162 179 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 201 209 Extracellular. {ECO:0000255}.; TOPO_DOM 231 248 Extracellular. {ECO:0000255}.; TOPO_DOM 270 395 Cytoplasmic. {ECO:0000255}. FUNCTION: Voltage-gated calcium channel that plays a central role in sperm cell hyperactivation. Controls calcium entry to mediate the hyperactivated motility, a step needed for sperm motility which is essential late in the preparation of sperm for fertilization. Activated by intracellular alkalinization. {ECO:0000269|PubMed:17227845, ECO:0000269|PubMed:17344468}. SUBCELLULAR LOCATION: Cell projection, cilium, flagellum membrane {ECO:0000269|PubMed:16107607, ECO:0000269|PubMed:17227845}; Multi-pass membrane protein {ECO:0000269|PubMed:16107607, ECO:0000269|PubMed:17227845}. Note=Specifically located in the principal piece of sperm tail. SUBUNIT: Heterotetramer; possibly composed of CATSPER1, CATSPER2, CATSPER3 and CATSPER4 (Potential). Component of the CatSper complex. Interacts with CATSPER1. {ECO:0000269|PubMed:17227845, ECO:0000269|PubMed:21224844, ECO:0000305}. TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:16107607, ECO:0000269|PubMed:17227845}. +P49025 CTRO_MOUSE Citron Rho-interacting kinase (CRIK) (EC 2.7.11.1) (Rho-interacting, serine/threonine-protein kinase 21) 2055 235,389 Active site (1); Alternative sequence (7); Binding site (1); Chain (1); Coiled coil (3); Compositional bias (2); Domain (4); Frameshift (4); Modified residue (10); Motif (1); Mutagenesis (1); Nucleotide binding (1); Region (1); Sequence conflict (4); Zinc finger (1) FUNCTION: Plays a role in cytokinesis. Required for KIF14 localization to the central spindle and midbody. Probable RHO/RAC effector that binds to the GTP-bound forms of RHO and RAC1. It probably binds p21 with a tighter specificity in vivo. Displays serine/threonine protein kinase activity. Plays an important role in the regulation of cytokinesis and the development of the central nervous system. Phosphorylates MYL9/MLC2. {ECO:0000269|PubMed:11086988, ECO:0000269|PubMed:8543060, ECO:0000269|PubMed:9697773, ECO:0000269|PubMed:9792683}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9792683}. SUBUNIT: Interacts with TTC3 (By similarity). Homodimer (Probable). Directly interacts with KIF14 depending on the activation state (stronger interaction with the kinase-dead form). {ECO:0000250, ECO:0000305}. TISSUE SPECIFICITY: A major signal was observed in testis and brain, but it was also detected in thymus, spleen, kidney, heart and lung. {ECO:0000269|PubMed:11086988, ECO:0000269|PubMed:9792683}. +O35474 EDIL3_MOUSE EGF-like repeat and discoidin I-like domain-containing protein 3 (Developmentally-regulated endothelial cell locus 1 protein) (Integrin-binding protein DEL1) 480 53,712 Alternative sequence (2); Chain (1); Disulfide bond (12); Domain (5); Glycosylation (3); Metal binding (5); Motif (1); Sequence conflict (2); Signal peptide (1) FUNCTION: Promotes adhesion of endothelial cells through interaction with the alpha-v/beta-3 integrin receptor. Inhibits formation of vascular-like structures. May be involved in regulation of vascular morphogenesis of remodeling in embryonic development. SUBCELLULAR LOCATION: Secreted. DOMAIN: EGF2 and EGF3 form a rigid rod via an interdomain calcium ion binding site, while the long linker between EGF1 and EGF2 lends considerable flexibility to EGF1. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in angioblasts and early endothelial cells. By embryonic day 13.5, also expressed in a restricted group of non-endothelial cells including chondrocytes and retinal neurons. +P48299 EDN3_MOUSE Endothelin-3 (ET-3) (Preproendothelin-3) (PPET3) 214 23,322 Disulfide bond (2); Peptide (1); Propeptide (2); Region (1); Signal peptide (1); Site (1) FUNCTION: Endothelins are endothelium-derived vasoconstrictor peptides. SUBCELLULAR LOCATION: Secreted. +O35927 CTND2_MOUSE Catenin delta-2 (Neural plakophilin-related ARM-repeat protein) (NPRAP) (Neurojungin) 1247 135,000 Alternative sequence (1); Chain (1); Coiled coil (1); Compositional bias (4); Modified residue (15); Repeat (9) FUNCTION: Has a critical role in neuronal development, particularly in the formation and/or maintenance of dendritic spines and synapses (PubMed:17993462) (PubMed:25807484). Involved in the regulation of canonical Wnt signaling (By similarity). It probably acts on beta-catenin turnover, facilitating beta-catenin interaction with GSK3B, phosphorylation, ubiquitination and degradation (PubMed:20623542). May be involved in neuronal cell adhesion and tissue morphogenesis and integrity by regulating adhesion molecules. Functions as a transcriptional activator when bound to ZBTB33 (PubMed:15282317). {ECO:0000250|UniProtKB:Q9UQB3, ECO:0000269|PubMed:15282317, ECO:0000269|PubMed:17993462, ECO:0000269|PubMed:20623542, ECO:0000269|PubMed:25807484, ECO:0000269|PubMed:9971746}. PTM: O-glycosylated. {ECO:0000269|PubMed:16452088}.; PTM: Phosphorylated by CDK5 (By similarity). Phosphorylated by GSK3B (PubMed:19706605). {ECO:0000250|UniProtKB:O35116, ECO:0000269|PubMed:19706605}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15282317}. Cell junction, adherens junction {ECO:0000269|PubMed:10753311}. Cell projection, dendrite {ECO:0000250|UniProtKB:O35116}. Perikaryon {ECO:0000250|UniProtKB:O35116}. SUBUNIT: Binds to E-cadherin at a juxtamembrane site within the cytoplasmic domain. Binds to PSEN1. Interacts with PDZD2 (By similarity). Interacts (via the extreme C-terminus) with FRMPD2 (via the PDZ 2 domain) (By similarity). Interacts with ZBTB33. Interacts with ARHGEF28 (PubMed:17993462). Interacts with CDK5 (By similarity). Interacts with CTNNB1 (By similarity). Interacts with GSK3A and GSK3B (PubMed:20623542) (PubMed:19706605). Interacts with DNM2 (By similarity). {ECO:0000250|UniProtKB:O35116, ECO:0000250|UniProtKB:Q9UQB3, ECO:0000269|PubMed:15282317, ECO:0000269|PubMed:17993462, ECO:0000269|PubMed:19706605, ECO:0000269|PubMed:20623542, ECO:0000269|PubMed:9971746}. TISSUE SPECIFICITY: Expressed in neurons and glial cells. Isoform 2 was found to be the most predominant isoform in various brain regions. Expressed at neuromuscular junctions. {ECO:0000269|PubMed:10753311, ECO:0000269|PubMed:15282317}. +Q9D5V5 CUL5_MOUSE Cullin-5 (CUL-5) 780 90,974 Chain (1); Cross-link (1); Helix (20); Modified residue (2); Sequence conflict (1); Turn (2) Protein modification; protein ubiquitination. FUNCTION: Core component of multiple SCF-like ECS (Elongin BC-Cullin 2/5-SOCS-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition component. ECS(SOCS1) seems to direct ubiquitination of JAK2. Seems to be involved in proteosomal degradation of p53/TP53 stimulated by adenovirus E1B-55 kDa protein. May form a cell surface vasopressin receptor. {ECO:0000269|PubMed:23806657}. PTM: Neddylated; which enhances the ubiquitination activity of SCF and prevents binding of the inhibitor CAND1. Deneddylated via its interaction with the COP9 signalosome (CSN). {ECO:0000250|UniProtKB:Q93034}. SUBUNIT: Component of multiple ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complexes formed of CUL5, Elongin BC (ELOB and ELOC), RBX2 and a variable SOCS box domain-containing protein as substrate-specific recognition component. Component of the probable ECS(LRRC41) complex with the substrate recognition component LRRC41. Component of the probable ECS(SOCS1) complex with the substrate recognition component SOCS1. Component of the probable ECS(WSB1) complex with the substrate recognition subunit WSB1. Component of the probable ECS(SOCS3) complex with the substrate recognition component SOCS3. Component of the probable ECS(SPSB1) complex with the substrate recognition component SPSB1. Component of the probable ECS(SPSB2) complex with the substrate recognition component SPSB2. Component of the probable ECS(SPSB4) complex with the substrate recognition component SPSB4. Component of the probable ECS(RAB40C) complex with the substrate recognition subunit RAB40C. May also form complexes containing CUL5, elongin BC complex (ELOB and ELOC), RBX1 and ELOA. May also form complexes containing CUL5, Elongin BC (ELOB and ELOC), RBX1 and VHL. Interacts with RNF7/RBX2, LRRC41, SOCS3, SPSB1, SPSB2, SPSB4 and RAB40C. Interacts with ASB1, ASB2, ASB6, ASB7 and ASB12. Interacts (when neddylated) with ARIH2; leading to activate the E3 ligase activity of ARIH1. Interacts with NOS2 in the presence of SPSB1 or SPSB2 or SPSB4 (By similarity). {ECO:0000250|UniProtKB:Q93034}. +P57776 EF1D_MOUSE Elongation factor 1-delta (EF-1-delta) 281 31,293 Alternative sequence (2); Chain (1); Initiator methionine (1); Modified residue (15); Region (2); Sequence conflict (3) FUNCTION: Isoform 1: EF-1-beta and EF-1-delta stimulate the exchange of GDP bound to EF-1-alpha to GTP, regenerating EF-1-alpha for another round of transfer of aminoacyl-tRNAs to the ribosome. {ECO:0000250}.; FUNCTION: Isoform 3: Regulates induction of heat-shock-responsive genes through association with heat shock transcription factors and direct DNA-binding at heat shock promoter elements (HSE). {ECO:0000250|UniProtKB:P29692}. SUBCELLULAR LOCATION: Isoform 3: Nucleus {ECO:0000250|UniProtKB:P29692}. SUBUNIT: EF-1 is composed of 4 subunits: alpha, beta, delta isoform 1, and gamma. Isoform 3 interacts with HSF1 and NFE2L2. {ECO:0000250|UniProtKB:P29692}. +Q3TKY6 CWC27_MOUSE Spliceosome-associated protein CWC27 homolog (Probable inactive peptidyl-prolyl cis-trans isomerase CWC27 homolog) (PPIase CWC27) 469 53,543 Chain (1); Coiled coil (2); Domain (1); Erroneous initiation (3); Frameshift (1); Initiator methionine (1); Modified residue (1); Sequence conflict (2) FUNCTION: As part of the spliceosome, plays a role in pre-mRNA splicing. Probable inactive PPIase with no peptidyl-prolyl cis-trans isomerase activity. {ECO:0000250|UniProtKB:Q6UX04}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6UX04}. SUBUNIT: Part of the activated spliceosome B/catalytic step 1 spliceosome, one of the forms of the spliceosome which has a well-formed active site but still cannot catalyze the branching reaction and is composed at least of 52 proteins, the U2, U5 and U6 snRNAs and the pre-mRNA. Recruited during early steps of activated spliceosome B maturation, it is probably one of the first proteins released from this complex as he matures to the spliceosome C complex. {ECO:0000250|UniProtKB:Q6UX04}. +P58252 EF2_MOUSE Elongation factor 2 (EF-2) 858 95,314 Chain (1); Cross-link (3); Domain (1); Initiator methionine (1); Modified residue (21); Nucleotide binding (3) FUNCTION: Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. PTM: Phosphorylation by EF-2 kinase completely inactivates EF-2; it requires prior phosphorylation by CDK2 at Ser-595 during mitotic prometaphase. Phosphorylation by CSK promotes SUMOylation, proteolytic cleavage, and nuclear translocation if the C-terminal fragment. {ECO:0000250|UniProtKB:P13639}.; PTM: Diphthamide is 2-[3-carboxyamido-3-(trimethyl-ammonio)propyl]histidine. Diphthamide can be ADP-ribosylated by diphtheria toxin and by Pseudomonas exotoxin A, thus arresting protein synthesis (By similarity). {ECO:0000250|UniProtKB:P05197}.; PTM: ISGylated. {ECO:0000269|PubMed:16139798}.; PTM: Proteolytically processed at two sites following phosphorylation by CSK. {ECO:0000250|UniProtKB:P13639}.; PTM: SUMOylated following phosphorylation by CSK, promotes proteolytic cleavage. {ECO:0000250|UniProtKB:P13639}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P13639}. Nucleus {ECO:0000250|UniProtKB:P13639}. Note=Phosphorylation by CSK promotes cleavage and SUMOylation-dependent nuclear translocation of the C-terminal cleavage product. {ECO:0000250|UniProtKB:P13639}. SUBUNIT: Component of the mRNA surveillance SURF complex, at least composed of ERF1, ERF3 (ERF3A or ERF3B), EEF2, UPF1/RENT1, SMG1, SMG8 and SMG9. Interacts with RBPMS2. {ECO:0000250|UniProtKB:P13639}. +Q9D581 EFC10_MOUSE EF-hand calcium-binding domain-containing protein 10 132 15,562 Chain (1); Domain (2) +Q9D0E5 EFC11_MOUSE EF-hand calcium-binding domain-containing protein 11 162 18,470 Alternative sequence (1); Calcium binding (1); Chain (1); Domain (3) +Q8BGQ6 EFC14_MOUSE EF-hand calcium-binding domain-containing protein 14 484 53,694 Alternative sequence (1); Calcium binding (1); Chain (1); Domain (2); Sequence conflict (2) +Q80ZJ8 EFC4A_MOUSE EF-hand calcium-binding domain-containing protein 4A (Calcium release-activated channel regulator 2B) 394 44,438 Chain (1); Coiled coil (1); Compositional bias (2); Domain (2); Erroneous initiation (1); Modified residue (1); Sequence conflict (1) FUNCTION: Plays a role in store-operated Ca(2+) entry (SOCE). {ECO:0000250}. +Q8VDY4 EFCB7_MOUSE EF-hand calcium-binding domain-containing protein 7 628 71,442 Calcium binding (1); Chain (1); Domain (3); Erroneous initiation (2); Modified residue (2); Sequence conflict (2) FUNCTION: Component of the EvC complex that positively regulates ciliary Hedgehog (Hh) signaling (PubMed:24582806). Required for the localization of the EVC2:EVC subcomplex at the base of primary cilia (PubMed:24582806). {ECO:0000269|PubMed:24582806}. SUBCELLULAR LOCATION: Cell projection, cilium membrane {ECO:0000269|PubMed:24582806}; Peripheral membrane protein {ECO:0000269|PubMed:24582806}; Cytoplasmic side {ECO:0000269|PubMed:24582806}. Note=The EvC complex localizes at the base of cilia in the EvC zone of primary cilia in a EFCAB7-dependent manner (PubMed:24582806). {ECO:0000269|PubMed:24582806}. SUBUNIT: Component of the EvC complex composed of EFCAB7, IQCE, EVC2 and EVC; built from two subcomplexes, EVC2:EVC and EFCAB7:IQCE (PubMed:24582806). Interacts (via EF-hand 1 and 2) with IQCE (via N-terminus); this interaction anchors the EVC-EVC2 complex in a signaling microdomain at the base of cilia and stimulates the Hedgehog (Hh) pathway (PubMed:24582806). Interacts with EVC2 (via N-terminal end) (PubMed:24582806). Interacts with EVC (PubMed:24582806). {ECO:0000269|PubMed:24582806}. +P43024 CX6A1_MOUSE Cytochrome c oxidase subunit 6A1, mitochondrial (Cytochrome c oxidase polypeptide VIa-liver) 111 12,352 Chain (1); Erroneous initiation (2); Transit peptide (1) FUNCTION: This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. SUBCELLULAR LOCATION: Mitochondrion inner membrane. +Q8VDP2 CX056_MOUSE UPF0428 protein CXorf56 homolog 222 25,594 Alternative sequence (1); Chain (1); Coiled coil (1); Erroneous gene model prediction (1); Sequence conflict (2) SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29374277}. Cytoplasm {ECO:0000269|PubMed:29374277}. Note=Detected in the nucleus and cell soma of pyramidal neurons in the brain cortex and Purkinje cells, as well as in neurons in the granular layer in the cerebellum. {ECO:0000269|PubMed:29374277}. TISSUE SPECIFICITY: Expressed in neurons in the brain cortex and cerebellum (at protein level). {ECO:0000269|PubMed:29374277}. +P43023 CX6A2_MOUSE Cytochrome c oxidase subunit 6A2, mitochondrial (Cytochrome c oxidase polypeptide VIa-heart) (COXVIAH) 97 10,749 Chain (1); Sequence conflict (1); Transit peptide (1) FUNCTION: This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. SUBCELLULAR LOCATION: Mitochondrion inner membrane. +Q9JJF6 EFCC1_MOUSE EF-hand and coiled-coil domain-containing protein 1 (Coiled-coil domain-containing protein 48) 558 61,881 Alternative sequence (1); Chain (1); Coiled coil (2); Compositional bias (2); Domain (1) +P0DPD9 EFCE2_MOUSE EEF1AKMT4-ECE2 readthrough transcript protein (EC 3.4.24.71) [Includes: Methyltransferase-like region (EC 2.1.1.-); Endothelin-converting enzyme 2 region (EC 3.4.24.71)] 881 99,480 Active site (2); Alternative sequence (1); Binding site (5); Chain (1); Erroneous initiation (2); Glycosylation (9); Metal binding (3); Modified residue (2); Region (4); Sequence conflict (10); Topological domain (2); Transmembrane (1) TRANSMEM 179 199 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 178 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 200 881 Lumenal. {ECO:0000305}. FUNCTION: Converts big endothelin-1 to endothelin-1. May also have methyltransferase activity (By similarity). May play a role in amyloid-beta processing (PubMed:12464614). {ECO:0000250|UniProtKB:P0DPE2, ECO:0000269|PubMed:12464614}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:P0DPE2}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P0DPE2}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:P0DPE2}. TISSUE SPECIFICITY: Expressed at high levels in central nervous system. Expressed in adrenal glands, ovary and uterus, and at low levels in heart. {ECO:0000269|PubMed:10811845}. +P56391 CX6B1_MOUSE Cytochrome c oxidase subunit 6B1 (Cytochrome c oxidase subunit VIb isoform 1) (COX VIb-1) 86 10,071 Chain (1); Disulfide bond (2); Domain (1); Initiator methionine (1); Modified residue (2); Motif (2) FUNCTION: Connects the two COX monomers into the physiological dimeric form. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion intermembrane space {ECO:0000250}. +P48771 CX7A2_MOUSE Cytochrome c oxidase subunit 7A2, mitochondrial (Cytochrome c oxidase subunit VIIa-liver/heart) (Cytochrome c oxidase subunit VIIa-L) 83 9,291 Chain (1); Modified residue (1); Sequence conflict (2); Transit peptide (1) FUNCTION: This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. SUBCELLULAR LOCATION: Mitochondrion inner membrane. SUBUNIT: Interacts with PET100. {ECO:0000250}. +Q9WUS4 CXA10_MOUSE Gap junction alpha-10 protein (Connexin-57) (Cx57) 505 57,127 Alternative sequence (1); Chain (1); Sequence conflict (3); Topological domain (5); Transmembrane (4) TRANSMEM 17 37 Helical. {ECO:0000255}.; TRANSMEM 77 97 Helical. {ECO:0000255}.; TRANSMEM 166 186 Helical. {ECO:0000255}.; TRANSMEM 210 230 Helical. {ECO:0000255}. TOPO_DOM 1 16 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 38 76 Extracellular. {ECO:0000255}.; TOPO_DOM 98 165 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 187 209 Extracellular. {ECO:0000255}.; TOPO_DOM 231 505 Cytoplasmic. {ECO:0000255}. FUNCTION: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. Involved in tracer coupling between horizontal cells of the retina. May play a role in the regulation of horizontal cell patterning. {ECO:0000269|PubMed:15147297, ECO:0000269|PubMed:16820008, ECO:0000269|PubMed:17681699, ECO:0000269|PubMed:18320035}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17681699}; Multi-pass membrane protein {ECO:0000269|PubMed:17681699}. Cell junction, gap junction {ECO:0000269|PubMed:17681699}. SUBUNIT: A connexon is composed of a hexamer of connexins. {ECO:0000250}. TISSUE SPECIFICITY: Low levels were detected in skin, heart, kidney, testis, ovary, intestine. Expression not detected in brain, sciatic nerve or liver. According to PubMed:15147297 expression is detected only in horizontal cells in the inner nuclear layer of the retina and not in other neurons of the central nervous system or tissues. Detected in the outer plexiform layer of the retina (at protein level). {ECO:0000269|PubMed:12881038, ECO:0000269|PubMed:15147297, ECO:0000269|PubMed:17681699}. +Q810W6 CXCR1_MOUSE C-X-C chemokine receptor type 1 (CXC-R1) (CXCR-1) (High affinity interleukin-8 receptor A) (IL-8R A) (CD antigen CD181) 351 40,032 Chain (1); Disulfide bond (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 45 71 Helical; Name=1. {ECO:0000255}.; TRANSMEM 81 101 Helical; Name=2. {ECO:0000255}.; TRANSMEM 117 138 Helical; Name=3. {ECO:0000255}.; TRANSMEM 160 179 Helical; Name=4. {ECO:0000255}.; TRANSMEM 205 225 Helical; Name=5. {ECO:0000255}.; TRANSMEM 248 269 Helical; Name=6. {ECO:0000255}.; TRANSMEM 291 313 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 44 Extracellular. {ECO:0000255}.; TOPO_DOM 72 80 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 102 116 Extracellular. {ECO:0000255}.; TOPO_DOM 139 159 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 180 204 Extracellular. {ECO:0000255}.; TOPO_DOM 226 247 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 270 290 Extracellular. {ECO:0000255}.; TOPO_DOM 314 351 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor to interleukin-8, which is a powerful neutrophils chemotactic factor. Binding of IL-8 to the receptor causes activation of neutrophils. This response is mediated via a G-protein that activate a phosphatidylinositol-calcium second messenger system (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q02739 CXB5_MOUSE Gap junction beta-5 protein (Connexin-31.1) (Cx31.1) 271 31,195 Chain (1); Topological domain (5); Transmembrane (4) TRANSMEM 21 40 Helical. {ECO:0000255}.; TRANSMEM 76 98 Helical. {ECO:0000255}.; TRANSMEM 125 147 Helical. {ECO:0000255}.; TRANSMEM 184 206 Helical. {ECO:0000255}. TOPO_DOM 1 20 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 41 75 Extracellular. {ECO:0000255}.; TOPO_DOM 99 124 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 148 183 Extracellular. {ECO:0000255}.; TOPO_DOM 207 271 Cytoplasmic. {ECO:0000255}. FUNCTION: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell junction, gap junction. SUBUNIT: A connexon is composed of a hexamer of connexins. TISSUE SPECIFICITY: Expressed in skin, much lower in testis. +Q01231 CXA5_MOUSE Gap junction alpha-5 protein (Connexin-40) (Cx40) 358 40,413 Chain (1); Modified residue (2); Topological domain (5); Transmembrane (4) TRANSMEM 20 40 Helical. {ECO:0000255}.; TRANSMEM 77 97 Helical. {ECO:0000255}.; TRANSMEM 165 185 Helical. {ECO:0000255}.; TRANSMEM 206 226 Helical. {ECO:0000255}. TOPO_DOM 1 19 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 41 76 Extracellular. {ECO:0000255}.; TOPO_DOM 98 164 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 186 205 Extracellular. {ECO:0000255}.; TOPO_DOM 227 358 Cytoplasmic. {ECO:0000255}. FUNCTION: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell junction, gap junction. SUBUNIT: A connexon is composed of a hexamer of connexins. TISSUE SPECIFICITY: Kidney, heart and skin, but most abundant in lung. +P10889 CXCL2_MOUSE C-X-C motif chemokine 2 (Macrophage inflammatory protein 2) (MIP2) 100 10,621 Beta strand (6); Chain (1); Disulfide bond (2); Helix (2); Signal peptide (1); Turn (1) FUNCTION: Chemotactic for human polymorphonuclear leukocytes but does not induce chemokinesis or an oxidative burst. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Homotetramer. +Q9WUQ5 CXL14_MOUSE C-X-C motif chemokine 14 (B-cell and monocyte-activating chemokine) (Chemokine BRAK) (Kidney-expressed chemokine CXC) (MIP-2G) (Small-inducible cytokine B14) 99 11,716 Chain (1); Disulfide bond (2); Motif (1); Sequence conflict (5); Signal peptide (1) FUNCTION: Chemotactic for CESS B-cells and THP-1 monocytes, but not T-cells. {ECO:0000269|PubMed:10784614}. PTM: Ubiquitinated, followed by degradation by the proteasome. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. DOMAIN: The destruction box (D-box) acts as a recognition signal for degradation via the ubiquitin-proteasome pathway. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in brain, lung, ovary, muscle and in kidney and liver parenchyma, and at lower levels in bone marrow. {ECO:0000269|PubMed:10784614, ECO:0000269|PubMed:10946286}. +Q5UW37 CXL17_MOUSE C-X-C motif chemokine 17 (6-Cys CXCL17) (13.6 kDa protein) (VEGF coregulated chemokine 1) [Cleaved into: 4-Cys CXCL17] 119 13,627 Chain (2); Disulfide bond (2); Signal peptide (1); Site (1) FUNCTION: Chemokine that acts as chemoattractant for monocytes, macrophages and dendritic cells (PubMed:24973458). Plays a role in angiogenesis and possibly in the development of tumors (PubMed:16989774). Acts as an anti-inflammatory in the stomach. May play a role in the innate defense against infections. Activates the C-X-C chemokine receptor GPR35 to induce a rapid and transient rise in the level of intracellular calcium ions. {ECO:0000250|UniProtKB:Q6UXB2, ECO:0000269|PubMed:16989774, ECO:0000269|PubMed:24973458}. PTM: Likely to undergo an endoproteolytic process to form a four-cysteine-containing mature peptide with a canonical CXC chemokine scaffold after secretion. {ECO:0000250|UniProtKB:D4A875}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q6UXB2}. TISSUE SPECIFICITY: Detected in lung, trachea, lung, tongue thyroid, submaxillary gland, epididymis, and uterus tissues and at a lower level in ovary, prostate and in intestinal tissues. {ECO:0000269|PubMed:16989774, ECO:0000269|PubMed:24973458}. +Q6NXI8 CXXC4_MOUSE CXXC-type zinc finger protein 4 (Inhibition of the Dvl and axin complex protein) 198 20,978 Chain (1); Compositional bias (1); Region (1); Zinc finger (1) FUNCTION: Acts as a negative regulator of the Wnt signaling pathway via its interaction with DVL1. {ECO:0000269|PubMed:11113207}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with the PDZ domain of DVL1. {ECO:0000250}. +Q91X77 CY250_MOUSE Cytochrome P450 2C50 (EC 1.14.14.1) (CYPIIC50) 490 55,765 Alternative sequence (1); Chain (1); Metal binding (1); Modified residue (3); Sequence conflict (8) FUNCTION: Metabolizes arachidonic acid to several midchain and omega-terminal hydroxyeicosatetraenoic acids (HETE). {ECO:0000269|PubMed:15102943}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15102943}; Peripheral membrane protein {ECO:0000269|PubMed:15102943}. Microsome membrane {ECO:0000269|PubMed:15102943}; Peripheral membrane protein {ECO:0000269|PubMed:15102943}. TISSUE SPECIFICITY: Expressed in heart and liver. {ECO:0000269|PubMed:15102943}. +Q60720 CY561_MOUSE Cytochrome b561 (Cytochrome b-561) 250 27,822 Chain (1); Domain (1); Metal binding (6); Modified residue (3); Sequence conflict (5); Topological domain (2); Transmembrane (6) TRANSMEM 16 36 Helical. {ECO:0000255}.; TRANSMEM 51 71 Helical. {ECO:0000255}.; TRANSMEM 84 104 Helical. {ECO:0000255}.; TRANSMEM 124 144 Helical. {ECO:0000255}.; TRANSMEM 158 178 Helical. {ECO:0000255}.; TRANSMEM 198 218 Helical. {ECO:0000255}. TOPO_DOM 1 15 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 219 250 Cytoplasmic. {ECO:0000255}. FUNCTION: Secretory vesicle-specific electron transport protein. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Secretory vesicle containing catecholamines and amidated peptides. {ECO:0000250}. TISSUE SPECIFICITY: Abundantly distributed in a number of neuroendocrine tissues. +Q9CQX2 CYB5B_MOUSE Cytochrome b5 type B (Cytochrome b5 outer mitochondrial membrane isoform) 146 16,318 Chain (1); Domain (1); Initiator methionine (1); Metal binding (2); Modified residue (5); Propeptide (1); Sequence conflict (2); Transmembrane (1) TRANSMEM 119 136 Helical. {ECO:0000255}. FUNCTION: Cytochrome b5 is a membrane bound hemoprotein which function as an electron carrier for several membrane bound oxygenases. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250}. SUBUNIT: Component of a complex composed of cytochrome b5, NADH-cytochrome b5 reductase (CYB5R3) and MOSC2. {ECO:0000250}. +P56395 CYB5_MOUSE Cytochrome b5 134 15,241 Chain (1); Domain (1); Initiator methionine (1); Metal binding (2); Modified residue (4); Transmembrane (1) TRANSMEM 109 131 Helical. {ECO:0000255}. FUNCTION: Cytochrome b5 is a membrane bound hemoprotein which function as an electron carrier for several membrane bound oxygenases. It is also involved in several steps of the sterol biosynthesis pathway, particularly in the C-5 double bond introduction during the C-5 desaturation. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Microsome membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. +Q925G2 CYBR1_MOUSE Cytochrome b reductase 1 (EC 1.-.-.-) (Duodenal cytochrome b) 290 31,844 Alternative sequence (2); Chain (1); Domain (1); Glycosylation (1); Metal binding (5); Modified residue (2); Sequence conflict (1); Transmembrane (6) TRANSMEM 12 32 Helical; Name=1. {ECO:0000255}.; TRANSMEM 49 69 Helical; Name=2. {ECO:0000255}.; TRANSMEM 85 105 Helical; Name=3. {ECO:0000255}.; TRANSMEM 127 147 Helical; Name=4. {ECO:0000255}.; TRANSMEM 158 178 Helical; Name=5. {ECO:0000255}.; TRANSMEM 199 219 Helical; Name=6. {ECO:0000255}. FUNCTION: Ferric-chelate reductase that reduces Fe(3+) to Fe(2+). Present at the brush border of duodenal enterocytes where it probably reduces dietary Fe(3+) thereby facilitating its transport into the mucosal cells. Uses ascorbate as electron donor. May be involved in extracellular ascorbate recycling in erythrocyte membranes. May also act as a ferrireductase in airway epithelial cells. {ECO:0000269|PubMed:11230685, ECO:0000269|PubMed:12547225}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11230685, ECO:0000269|PubMed:12547225}; Multi-pass membrane protein {ECO:0000269|PubMed:11230685, ECO:0000269|PubMed:12547225}. TISSUE SPECIFICITY: Highly expressed in the brush-border membrane of duodenal enterocytes (at protein level). Also expressed in liver and spleen. {ECO:0000269|PubMed:11230685, ECO:0000269|PubMed:12547225}. +Q64481 CP3AG_MOUSE Cytochrome P450 3A16 (EC 1.14.14.1) (CYPIIIA16) 504 57,870 Chain (1); Metal binding (1); Sequence conflict (1) FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. +Q9DBX6 CP2S1_MOUSE Cytochrome P450 2S1 (EC 1.14.14.1) (CYPIIS1) 501 55,632 Chain (1); Metal binding (1) FUNCTION: Has a potential importance for extrahepatic xenobiotic metabolism. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Microsome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. +Q64458 CP2CT_MOUSE Cytochrome P450 2C29 (EC 1.14.14.1) (Aldehyde oxygenase) (CYPIIC29) (Cytochrome P-450 MUT-2) 490 55,716 Chain (1); Metal binding (1); Modified residue (3); Sequence conflict (2) FUNCTION: Metabolizes arachidonic acid to produce 14,15-cis-epoxyeicosatrienoic acid (EET). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. +E9Q816 CP2W1_MOUSE Cytochrome P450 2W1 (EC 1.14.14.-) 493 54,438 Chain (1); Glycosylation (1); Metal binding (1); Signal peptide (1) FUNCTION: Seems to have broad catalytic activity towards several chemicals, including polycyclic aromatic hydrocarbon dihydrodiols and aromatic amines. Active also in the metabolism of indoline substrates and is able to activate aflatoxin B1 into cytotoxic products. Furthermore, it seems to be involved in the oxydation of lysophospholipids and fatty acids. {ECO:0000250|UniProtKB:Q8TAV3}. SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q8TAV3}. Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:Q8TAV3}. Cell membrane {ECO:0000250|UniProtKB:Q8TAV3}. TISSUE SPECIFICITY: Detected in colon, ileum, and testes. {ECO:0000269|PubMed:21920951}. +Q91ZU6 DYST_MOUSE Dystonin (Bullous pemphigoid antigen 1) (BPA) (Dystonia musculorum protein) (Hemidesmosomal plaque protein) (Microtubule actin cross-linking factor 2) 7393 834,218 Alternative sequence (12); Beta strand (1); Calcium binding (2); Chain (1); Compositional bias (1); Cross-link (1); Domain (6); Frameshift (1); Helix (10); Modified residue (14); Motif (2); Mutagenesis (2); Region (1); Repeat (37); Sequence caution (3); Sequence conflict (1); Turn (2) FUNCTION: Cytoskeletal linker protein. Acts as an integrator of intermediate filaments, actin and microtubule cytoskeleton networks. Required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. The proteins may self-aggregate to form filaments or a two-dimensional mesh. Regulates the organization and stability of the microtubule network of sensory neurons to allow axonal transport. Mediates docking of the dynein/dynactin motor complex to vesicle cargos for retrograde axonal transport through its interaction with TMEM108 and DCTN1. {ECO:0000269|PubMed:17287360}.; FUNCTION: Isoform 5: plays a structural role in the assembly of hemidesmosomes of epithelial cells; anchors keratin-containing intermediate filaments to the inner plaque of hemidesmosomes. Required for the regulation of keratinocyte polarity and motility; mediates integrin ITGB4 regulation of RAC1 activity.; FUNCTION: Isoform 6: required for bundling actin filaments around the nucleus. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, stress fiber. Cell projection, axon {ECO:0000269|PubMed:17287360}. Note=Associates with axonal microtubules at the growing distal tip and intermediate filaments, but not with actin cytoskeleton, in sensory neurons (By similarity). Associates with intermediate filaments, actin and microtubule cytoskeletons. Localizes to actin stress fibers and to actin-rich ruffling at the cortex of cells. {ECO:0000250, ECO:0000269|PubMed:14576348}.; SUBCELLULAR LOCATION: Isoform 1: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19932097}. Note=Colocalizes both cortical and cytoplasmic actin filaments (PubMed:19932097). Localizes to vesicule-like structures associated with microtubules (PubMed:14581450, PubMed:17287360). {ECO:0000269|PubMed:14581450, ECO:0000269|PubMed:17287360, ECO:0000269|PubMed:19932097}.; SUBCELLULAR LOCATION: Isoform 2: Cell membrane, sarcolemma. Cytoplasm, myofibril, sarcomere, Z line. Cytoplasm, myofibril, sarcomere, H zone. Cytoplasm, cytoskeleton. Note=Localizes to microtubules and actin microfilaments throughout the cytoplasm and at focal contact attachments at the plasma membrane.; SUBCELLULAR LOCATION: Isoform 5: Cytoplasm, cytoskeleton. Cell junction, hemidesmosome. Note=Colocalizes with the epidermal KRT5-KRT14 intermediate filaments network of keratins. Colocalizes with ITGB4 at the leading edge of migrating keratinocytes (By similarity). Localizes to actin and intermediate filaments cytoskeletons. {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 6: Nucleus. Nucleus envelope. Membrane; Single-pass membrane protein. Endoplasmic reticulum membrane; Single-pass membrane protein. Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, stress fiber {ECO:0000269|PubMed:14576348}. Note=Associates with actin cytoskeleton in sensory neurons (By similarity). Localizes to actin and intermediate filaments cytoskeletons. Localizes to central actin stress fibers around the nucleus and is excluded form focal contact sites in myoblast cells. Translocates to the nucleus. {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 7: Cytoplasm, cytoskeleton. Cytoplasm, cell cortex. Cell membrane; Lipid-anchor. SUBUNIT: Homodimer. Interacts with MAPRE1; probably required for targeting to the growing microtubule plus ends. Isoform 2 interacts (via N-terminus) with ACTN2. Isoform 2 interacts (via N-terminus) with PLEC (via N-terminus). Isoform 5 interacts (via N-terminus) with COL17A1 (via cytoplasmic region). Isoform 5 interacts (via N-terminus) with ITGB4 isoform beta-4a (via cytoplasmic region). Isoform 5 interacts (via N-terminus) with ERBIN (via C-terminus). Isoform 5 associates (via C-terminal) with KRT5-KRT14 (via rod region) intermediate filaments of keratins (By similarity). Isoform 2 and isoform 6 can homodimerize (via N-terminus). Isoform 2 interacts (via N-terminus) with PLEC (via N-terminus). Interacts with the neuronal intermediate filament protein, PRPH. Interacts with DES. Interacts with SYNE3. Isoform 1 interacts with TMEM108 (PubMed:17287360). {ECO:0000250|UniProtKB:Q03001, ECO:0000269|PubMed:10357897, ECO:0000269|PubMed:17287360, ECO:0000269|PubMed:18638474, ECO:0000269|PubMed:19932097, ECO:0000269|PubMed:9971739}. DOMAIN: Its association with epidermal and simple keratins is dependent on the tertiary structure induced by heterodimerization of these intermedaite filaments proteins and most likely involves recognition sites located in the rod domain of these keratins.; DOMAIN: The microtubule tip localization signal (MtLS) motif; mediates interaction with MAPRE1 and targeting to the growing microtubule plus ends. {ECO:0000250}. TISSUE SPECIFICITY: Isoform 1 and 2 are expressed in striated and heart muscle cells. Isoform 5 is expressed in the skin. Isoform 6 is expressed in sensory neural cells of the dorsal root ganglion and with low level in the skin (at protein level). Isoform 1 is expressed predominantly in the brain and spinal cord with low levels in the heart (PubMed:14581450). Isoform 2 is predominantly expressed in muscle and heart and with low levels in the brain. Isoform 5 is expressed in the skin and with low levels in myoblast cells. Isoform 6 is expressed in neurons. Isoform 7 is expressed in lung and with low levels in the brain. {ECO:0000269|PubMed:11514586, ECO:0000269|PubMed:14576348, ECO:0000269|PubMed:14581450, ECO:0000269|PubMed:16797530, ECO:0000269|PubMed:18638474, ECO:0000269|PubMed:19932097, ECO:0000269|PubMed:20209123, ECO:0000269|PubMed:7670468, ECO:0000269|PubMed:7736575, ECO:0000269|PubMed:8752219}. +O55127 CP26A_MOUSE Cytochrome P450 26A1 (EC 1.14.13.-) (Cytochrome P450RAI) (Retinoic acid 4-hydroxylase) (Retinoic acid-metabolizing cytochrome) 497 56,178 Chain (1); Metal binding (1); Sequence conflict (4) FUNCTION: Plays a key role in retinoic acid metabolism. Acts on retinoids, including all-trans-retinoic acid (RA) and its stereoisomer 9-cis-RA. Capable of both 4-hydroxylation and 18-hydroxylation. Responsible for generation of several hydroxylated forms of RA, including 4-OH-RA, 4-oxo-RA and 18-OH-RA. {ECO:0000269|PubMed:9250660, ECO:0000269|PubMed:9442090}.; FUNCTION: Has also a significant activity in oxidation of tazarotenic acid and may therefore metabolize that xenobiotic in vivo. {ECO:0000250|UniProtKB:O43174}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. +Q8K0C4 CP51A_MOUSE Lanosterol 14-alpha demethylase (LDM) (EC 1.14.14.154) (CYPLI) (Cytochrome P450 51A1) (Cytochrome P450-14DM) (Cytochrome P45014DM) (Cytochrome P450LI) (Sterol 14-alpha demethylase) 503 56,776 Chain (1); Erroneous initiation (1); Metal binding (1); Sequence conflict (4); Transmembrane (1) TRANSMEM 24 44 Helical. {ECO:0000255}. Steroid biosynthesis; zymosterol biosynthesis; zymosterol from lanosterol: step 1/6. FUNCTION: Catalyzes C14-demethylation of lanosterol; it transforms lanosterol into 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol. {ECO:0000250|UniProtKB:Q16850}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}. Microsome membrane {ECO:0000305}. +Q8BFS6 CPPED_MOUSE Serine/threonine-protein phosphatase CPPED1 (EC 3.1.3.16) (Calcineurin-like phosphoesterase domain-containing protein 1) 312 35,248 Alternative sequence (7); Chain (1); Erroneous initiation (1); Metal binding (4); Modified residue (2); Region (1) FUNCTION: Protein phosphatase that dephosphorylates AKT family kinase specifically at 'Ser-473', blocking cell cycle progression and promoting cell apoptosis. May play an inhibitory role in glucose uptake by adipocytes (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +Q60991 CP7B1_MOUSE 25-hydroxycholesterol 7-alpha-hydroxylase (EC 1.14.14.29) (Cytochrome P450 7B1) (Hippocampal transcript 1 protein) (HCT-1) (Oxysterol 7-alpha-hydroxylase) 507 58,470 Chain (1); Metal binding (1); Sequence conflict (4) Lipid metabolism; bile acid biosynthesis. FUNCTION: Oxysterol 7alpha-hydroxylase that mediates formation of 7-alpha,25-dihydroxycholesterol (7-alpha,25-OHC) from 25-hydroxycholesterol (PubMed:9295351). Plays a key role in cell positioning and movement in lymphoid tissues: 7-alpha,25-dihydroxycholesterol (7-alpha,25-OHC) acts as a ligand for the G protein-coupled receptor GPR183/EBI2, a chemotactic receptor for a number of lymphoid cells (PubMed:22999953). {ECO:0000269|PubMed:22999953, ECO:0000269|PubMed:9295351}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. TISSUE SPECIFICITY: Highly expressed in brain; also expressed in liver and kidney. +P70166 CPEB1_MOUSE Cytoplasmic polyadenylation element-binding protein 1 (CPE-BP1) (CPE-binding protein 1) (mCPEB) (mCPEB-1) 561 61,917 Chain (1); Compositional bias (1); Domain (2); Metal binding (8); Modified residue (2); Mutagenesis (1); Region (1); Site (1) FUNCTION: Sequence-specific RNA-binding protein that regulates mRNA cytoplasmic polyadenylation and translation initiation during oocyte maturation, early development and at postsynapse sites of neurons. Binds to the cytoplasmic polyadenylation element (CPE), an uridine-rich sequence element (consensus sequence 5'-UUUUUAU-3') within the 3'-UTR of mRNAs. In absence of phosphorylation and in association with TACC3 is also involved as a repressor of translation of CPE-containing mRNA; a repression that is relieved by phosphorylation or degradation (By similarity). Involved in the transport of CPE-containing mRNA to dendrites; those mRNAs may be transported to dendrites in a translationally dormant form and translationally activated at synapses. Its interaction with APLP1 promotes local CPE-containing mRNA polyadenylation and translation activation. Induces the assembly of stress granules in the absence of stress (By similarity). Required for cell cycle progression, specifically for prophase entry (By similarity). {ECO:0000250|UniProtKB:Q9BZB8, ECO:0000269|PubMed:11526086, ECO:0000269|PubMed:11980711, ECO:0000269|PubMed:12629046}. PTM: Phosphorylated on serine/threonine residues by AURKA within positions 165 and 196 (By similarity). Phosphorylation and dephosphorylation on Thr-171 regulates cytoplasmic polyadenylation and translation of CPE-containing mRNAs. Phosphorylation on Thr-171 by AURKA in embryonic ovaries at 16.5 dpc (mostly pachytene oocytes) activates CPEB1. Not phosphorylated on Thr-171 in embryonic ovaries between 18.5 dpc (diplotene oocytes) and metaphase I. Dephosphorylation on Thr-171 by PP1 in embryonic ovaries at 18.5 dpc (mostly diplotene oocytes) inactivates CPEB1. In maturing oocytes, re-phosphorylation on Thr-171 by AURKA reactivates CPEB1. Phosphorylation on Thr-171 by CAMK2A in depolarized hippocampal neurons activates CPEB1. Dephosphorylation on Thr-171 (indirectly by PP1) in hippocampal neurons inactivates CPEB1. Phosphorylation on Thr-171 may be promoted by APLP1. Phosphorylation increases binding to RNA. {ECO:0000250, ECO:0000269|PubMed:11526086, ECO:0000269|PubMed:11980711, ECO:0000269|PubMed:12815066, ECO:0000269|PubMed:15175389, ECO:0000269|PubMed:15944388, ECO:0000269|PubMed:16314516}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell junction, synapse {ECO:0000250}. Cytoplasm, P-body {ECO:0000250}. Cytoplasmic granule {ECO:0000250}. Membrane {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250}. Note=Localizes in synaptosomes at dendritic synapses of neurons. Strongly enriched in postsynaptic density (PSD) fractions. Transported into dendrites in a microtubule-dependent fashion and colocalizes in mRNA-containing particles with TACC3, dynein and kinesin. Membrane-associated. Colocalizes at excitatory synapses with members of the polyadenylation and translation complex factors (CPSF, APLP1, TACC3, AURKA, SYP, etc.) including CPE-containing RNAs. In P-bodies and stress granules (By similarity). Recruited to stress granules (SGs) upon arsenite treatment (By similarity). {ECO:0000250}. SUBUNIT: Interacts with kinesin, dynein, APLP1, APLP2, TENT2/GLD2 and APP. Both phosphorylated and non phosphorylated forms interact with APLP1 (PubMed:12629046, PubMed:16314516, PubMed:16705177, PubMed:17927953). Interacts with TENT4B; the interaction is required for TENT4B-mediated translational control (By similarity). {ECO:0000250|UniProtKB:Q9BZB8, ECO:0000269|PubMed:12629046, ECO:0000269|PubMed:16314516, ECO:0000269|PubMed:16705177, ECO:0000269|PubMed:17927953}. DOMAIN: The 2 RRM domains and the C-terminal region mediate interaction with CPE-containing RNA. The interdomain linker (411-429) acts as a hinge to fix the relative orientation of the 2 RRMs. The ZZ domain (509-566) coordinates 2 Zn ions and is probably implicated in mediating interactions with other proteins in addition to increasing the affinity of the RRMs for the CPEs. A continuous hydrophobic interface is formed between the 2 RRM. {ECO:0000250|UniProtKB:Q9BZB8}. TISSUE SPECIFICITY: Expressed in hippocampus, cerebral cortex and oocytes (at protein level). Expressed in brain, heart, kidney, lung and ovary and testis. Weakly expressed in granular cells of dentate gyrus and the pyramidal cells of CA3 and CA1 of the hippocampus. {ECO:0000269|PubMed:11526086, ECO:0000269|PubMed:11980711, ECO:0000269|PubMed:12871996, ECO:0000269|PubMed:8962099, ECO:0000269|PubMed:9856468}. +P97742 CPT1A_MOUSE Carnitine O-palmitoyltransferase 1, liver isoform (CPT1-L) (EC 2.3.1.21) (Carnitine O-palmitoyltransferase I, liver isoform) (CPT I) (CPTI-L) (Carnitine palmitoyltransferase 1A) 773 88,251 Active site (1); Binding site (2); Chain (1); Initiator methionine (1); Modified residue (7); Region (1); Sequence conflict (7); Topological domain (3); Transmembrane (2) TRANSMEM 48 73 Helical. {ECO:0000255}.; TRANSMEM 103 122 Helical. {ECO:0000255}. TOPO_DOM 2 47 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 74 102 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 123 773 Cytoplasmic. {ECO:0000255}. Lipid metabolism; fatty acid beta-oxidation. FUNCTION: Catalyzes the transfer of the acyl group of long-chain fatty acid-CoA conjugates onto carnitine, an essential step for the mitochondrial uptake of long-chain fatty acids and their subsequent beta-oxidation in the mitochondrion. Plays an important role in triglyceride metabolism. {ECO:0000269|PubMed:16169268, ECO:0000269|PubMed:17030509}. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Multi-pass membrane protein. SUBUNIT: Homohexamer and homotrimer. Identified in a complex that contains at least CPT1A, ACSL1 and VDAC1. Also identified in complexes with ACSL1 and VDAC2 and VDAC3 (By similarity). {ECO:0000250}. DOMAIN: A conformation change in the N-terminal region spanning the first 42 residues plays an important role in the regulation of enzyme activity by malonyl-CoA. {ECO:0000250}. +P19070 CR2_MOUSE Complement receptor type 2 (Cr2) (Complement C3d receptor) (CD antigen CD21) 1025 112,995 Chain (1); Disulfide bond (30); Domain (15); Glycosylation (17); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 964 990 Helical. {ECO:0000255}. TOPO_DOM 12 963 Extracellular. {ECO:0000255}.; TOPO_DOM 991 1025 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for complement C3d and for HNRNPU. Participates in B lymphocytes activation. {ECO:0000250|UniProtKB:P20023}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P20023}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P20023}. SUBUNIT: Interacts (via Sushi domain 1 and 2) with C3. Interacts with CD19. Part of a complex composed of CD19, CR2/CD21, CD81 and IFITM1/CD225 in the membrane of mature B-cells. {ECO:0000250|UniProtKB:P20023}. TISSUE SPECIFICITY: B-lymphocytes. +Q8BH52 CR3L2_MOUSE Cyclic AMP-responsive element-binding protein 3-like protein 2 (cAMP-responsive element-binding protein 3-like protein 2) [Cleaved into: Processed cyclic AMP-responsive element-binding protein 3-like protein 2] 521 57,469 Chain (2); Cross-link (1); Domain (1); Glycosylation (3); Modified residue (2); Motif (1); Mutagenesis (4); Region (2); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 379 399 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 378 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 400 521 Lumenal. {ECO:0000255}. FUNCTION: Transcription factor involved in unfolded protein response (UPR). In the absence of endoplasmic reticulum (ER) stress, inserted into ER membranes, with N-terminal DNA-binding and transcription activation domains oriented toward the cytosolic face of the membrane. In response to ER stress, transported to the Golgi, where it is cleaved in a site-specific manner by resident proteases S1P/MBTPS1 and S2P/MBTPS2. The released N-terminal cytosolic domain is translocated to the nucleus to effect transcription of specific target genes. Plays a critical role in chondrogenesis by activating the transcription of SEC23A, which promotes the transport and secretion of cartilage matrix proteins, and possibly that of ER biogenesis-related genes (PubMed:19767744). In a neuroblastoma cell line, protects cells from ER stress-induced death (PubMed:17178827). In vitro activates transcription of target genes via direct binding to the CRE site (PubMed:17178827). {ECO:0000269|PubMed:17178827, ECO:0000269|PubMed:19767744}. PTM: Upon ER stress, translocated to the Golgi apparatus, where it is processed by regulated intramembrane proteolysis (RIP) to release the cytosol-facing N-terminal transcription factor domain. The cleavage is performed sequentially by site-1 and site-2 proteases (S1P/MBTPS1 and S2P/MBTPS2). {ECO:0000269|PubMed:17178827}.; PTM: N-glycosylated. {ECO:0000269|PubMed:17178827}.; PTM: Ubiquitinated by HRD1/SYVN1; undergoes 'Lys-48'-linked ubiquitination, followed by rapid proteasomal degradation under normal conditions. Upon ER stress, SYVN1 E3 ubiquitin-protein ligase dissociates from its substrate, ubiquitination does not occur and CREB3L2 is stabilized. {ECO:0000269|PubMed:22705851}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:17178827}; Single-pass type II membrane protein. Note=ER membrane resident protein. Upon ER stress, translocated to the Golgi apparatus where it is cleaved. The cytosolic N-terminal fragment (processed cyclic AMP-responsive element-binding protein 3-like protein 1) is transported into the nucleus. {ECO:0000269|PubMed:17178827}.; SUBCELLULAR LOCATION: Processed cyclic AMP-responsive element-binding protein 3-like protein 2: Nucleus {ECO:0000269|PubMed:17178827}. Note=Upon ER stress, translocated into the nucleus. {ECO:0000269|PubMed:17178827}. SUBUNIT: Binds DNA as a dimer. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed, including in lung, bladder, ovary, testis and spleen (PubMed:17178827). Highly expressed in chondrocytes (PubMed:19767744). {ECO:0000269|PubMed:17178827, ECO:0000269|PubMed:19767744}. +Q32M00 CRBL2_MOUSE cAMP-responsive element-binding protein-like 2 123 14,002 Chain (1); Domain (1); Region (2); Sequence conflict (2) FUNCTION: Probable regulator of CREB1 transcriptional activity which is involved in adipose cells differentiation. May also play a regulatory role in the cell cycle. {ECO:0000269|PubMed:21728997}. PTM: Phosphorylated by AMPK. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21728997}. SUBUNIT: Interacts with CREB1; regulates CREB1 phosphorylation, stability and transcriptional activity. {ECO:0000269|PubMed:21728997}. TISSUE SPECIFICITY: Widely expressed with higher expression in adipose tissue, skeletal muscle, and liver (at protein level). {ECO:0000269|PubMed:21728997}. +Q0V8T7 CTP5C_MOUSE Contactin-associated protein like 5-3 (Cell recognition molecule Caspr5-3) (Cell recognition molecule Caspr5c) (Contactin-associated protein-like 5c) 1305 146,242 Chain (1); Compositional bias (1); Disulfide bond (10); Domain (8); Glycosylation (5); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1236 1256 Helical. {ECO:0000255}. TOPO_DOM 25 1235 Extracellular. {ECO:0000255}.; TOPO_DOM 1257 1305 Cytoplasmic. {ECO:0000255}. FUNCTION: May play a role in the correct development and proper functioning of the peripheral and central nervous system and be involved in cell adhesion and intercellular communication. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in brain. {ECO:0000269|PubMed:16845472}. +Q9R187 EDAR_MOUSE Tumor necrosis factor receptor superfamily member EDAR (Anhidrotic ectodysplasin receptor 1) (Downless) (Ectodermal dysplasia receptor) (Ectodysplasin-A receptor) 448 48,434 Chain (1); Disulfide bond (6); Domain (1); Erroneous initiation (1); Glycosylation (1); Natural variant (1); Repeat (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 188 208 Helical. {ECO:0000255}. TOPO_DOM 27 187 Extracellular. {ECO:0000255}.; TOPO_DOM 209 448 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for EDA isoform TAA, but not for EDA isoform TA-2 (By similarity). May mediate the activation of NF-kappa-B and JNK. May promote caspase-independent cell death. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Binds to EDARADD. Associates with TRAF1, TRAF2, TRAF3 and NIK. DISEASE: Note=Defects in Edar are a cause of the downless phenotype in mice (the equivalent of anhidrotic ectodermal dysplasia in humans). The disease is characterized by sparse hair (atrichosis or hypotrichosis), abnormal or missing teeth and the inability to sweat due to the absence of sweat glands. +O54693 EDA_MOUSE Ectodysplasin-A (EDA protein homolog) (Tabby protein) [Cleaved into: Ectodysplasin-A, membrane form; Ectodysplasin-A, secreted form] 391 41,603 Alternative sequence (7); Chain (2); Domain (1); Glycosylation (2); Sequence conflict (2); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 42 62 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 41 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 63 391 Extracellular. {ECO:0000255}. FUNCTION: Cytokine which is involved in epithelial-mesenchymal signaling during morphogenesis of ectodermal organs. Functions as a ligand activating the DEATH-domain containing receptors EDAR and EDA2R. Isoform TAA binds only to the receptor EDAR, while isoform TA-A2 binds exclusively to the receptor EDA2R (By similarity). May also play a role in cell adhesion (PubMed:10534613). {ECO:0000250|UniProtKB:Q92838, ECO:0000269|PubMed:10534613}.; FUNCTION: Isoform TAA binds only to the receptor EDAR, while isoform TA-A2 binds exclusively to the receptor EDA2R. {ECO:0000250|UniProtKB:Q92838}.; FUNCTION: Isoform TA-A2 binds exclusively to the receptor EDA2R. {ECO:0000250|UniProtKB:Q92838}. PTM: N-glycosylated. {ECO:0000269|PubMed:10534613}.; PTM: Processing by furin produces a secreted form. {ECO:0000250|UniProtKB:Q92838}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10534613}; Single-pass type II membrane protein {ECO:0000269|PubMed:10534613}.; SUBCELLULAR LOCATION: Ectodysplasin-A, secreted form: Secreted {ECO:0000250|UniProtKB:Q92838}. SUBUNIT: Homotrimer. The homotrimers may then dimerize and form higher-order oligomers. {ECO:0000269|PubMed:10534613}. DISEASE: Note=Defects in Eda are the cause of the tabby phenotype in mice (the equivalent of anhidrotic ectodermal dysplasia in humans). The disease is characterized by sparse hair (atrichosis or hypotrichosis), abnormal or missing teeth and the inability to sweat due to the absence of sweat glands. +Q8K2D3 EDC3_MOUSE Enhancer of mRNA-decapping protein 3 (YjeF domain-containing protein 1) 508 55,957 Chain (1); Domain (2); Modified residue (4); Region (2); Sequence conflict (2) FUNCTION: Binds single-stranded RNA. Involved in the process of mRNA degradation and in the positive regulation of mRNA decapping (By similarity). {ECO:0000250|UniProtKB:Q96F86}. SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000250}. Note=Processing bodies (PB). {ECO:0000250}. SUBUNIT: Homodimer (via YjeF N-terminal domain). Forms a complex with DCP1A, DCP2, DDX6 and EDC4/HEDLS, within this complex directly interacts with DCP1A and DDX6. Interacts with ZFP36 (By similarity). {ECO:0000250}. DOMAIN: The DFDF domain is unstructured by itself. It assumes a helical fold upon interaction with DDX6 (By similarity). {ECO:0000250}. +P70423 CTR3_MOUSE Cationic amino acid transporter 3 (CAT-3) (CAT3) (Cationic amino acid transporter y+) (Solute carrier family 7 member 3) 618 67,460 Chain (1); Glycosylation (1); Modified residue (2); Topological domain (15); Transmembrane (14) TRANSMEM 37 57 Helical; Name=1. {ECO:0000255}.; TRANSMEM 62 82 Helical; Name=2. {ECO:0000255}.; TRANSMEM 108 128 Helical; Name=3. {ECO:0000255}.; TRANSMEM 163 183 Helical; Name=4. {ECO:0000255}.; TRANSMEM 192 212 Helical; Name=5. {ECO:0000255}.; TRANSMEM 245 265 Helical; Name=6. {ECO:0000255}.; TRANSMEM 286 306 Helical; Name=7. {ECO:0000255}.; TRANSMEM 336 356 Helical; Name=8. {ECO:0000255}.; TRANSMEM 381 401 Helical; Name=9. {ECO:0000255}.; TRANSMEM 407 427 Helical; Name=10. {ECO:0000255}.; TRANSMEM 475 495 Helical; Name=11. {ECO:0000255}.; TRANSMEM 507 527 Helical; Name=12. {ECO:0000255}.; TRANSMEM 540 560 Helical; Name=13. {ECO:0000255}.; TRANSMEM 569 589 Helical; Name=14. {ECO:0000255}. TOPO_DOM 1 36 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 58 61 Extracellular. {ECO:0000255}.; TOPO_DOM 83 107 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 129 162 Extracellular. {ECO:0000255}.; TOPO_DOM 184 191 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 213 244 Extracellular. {ECO:0000255}.; TOPO_DOM 266 285 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 307 335 Extracellular. {ECO:0000255}.; TOPO_DOM 357 380 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 402 406 Extracellular. {ECO:0000255}.; TOPO_DOM 428 474 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 496 506 Extracellular. {ECO:0000255}.; TOPO_DOM 528 539 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 561 568 Extracellular. {ECO:0000255}.; TOPO_DOM 590 618 Cytoplasmic. {ECO:0000255}. FUNCTION: Mediates the uptake of the cationic amino acids arginine, lysine and ornithine in a sodium-independent manner. {ECO:0000269|PubMed:9334265}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed in adult brain and in a wide variety of embryonic tissues. {ECO:0000269|PubMed:9334265}. +Q9CR35 CTRB1_MOUSE Chymotrypsinogen B (EC 3.4.21.1) [Cleaved into: Chymotrypsin B chain A; Chymotrypsin B chain B; Chymotrypsin B chain C] 263 27,822 Active site (3); Chain (4); Disulfide bond (5); Domain (1); Modified residue (1); Sequence conflict (2); Signal peptide (1) SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250}. +Q8BLQ7 CTR4_MOUSE Cationic amino acid transporter 4 (CAT-4) (CAT4) (Solute carrier family 7 member 4) 635 68,350 Chain (1); Glycosylation (4); Modified residue (2); Transmembrane (13) TRANSMEM 42 62 Helical. {ECO:0000255}.; TRANSMEM 66 86 Helical. {ECO:0000255}.; TRANSMEM 113 133 Helical. {ECO:0000255}.; TRANSMEM 197 217 Helical. {ECO:0000255}.; TRANSMEM 229 249 Helical. {ECO:0000255}.; TRANSMEM 270 290 Helical. {ECO:0000255}.; TRANSMEM 318 338 Helical. {ECO:0000255}.; TRANSMEM 365 385 Helical. {ECO:0000255}.; TRANSMEM 391 411 Helical. {ECO:0000255}.; TRANSMEM 478 498 Helical. {ECO:0000255}.; TRANSMEM 508 528 Helical. {ECO:0000255}.; TRANSMEM 539 559 Helical. {ECO:0000255}.; TRANSMEM 567 587 Helical. {ECO:0000255}. FUNCTION: Involved in the transport of the cationic amino acids (arginine, lysine and ornithine). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q8BVN3 CTSR4_MOUSE Cation channel sperm-associated protein 4 (CatSper4) 442 51,130 Chain (1); Erroneous gene model prediction (1); Intramembrane (1); Topological domain (8); Transmembrane (6) INTRAMEM 223 243 Helical; Pore-forming. {ECO:0000255}. TRANSMEM 67 87 Helical; Name=Segment S1. {ECO:0000255}.; TRANSMEM 107 127 Helical; Name=Segment S2. {ECO:0000255}.; TRANSMEM 137 157 Helical; Name=Segment S3. {ECO:0000255}.; TRANSMEM 159 173 Helical; Name=Segment S4. {ECO:0000255}.; TRANSMEM 196 216 Helical; Name=Segment S5.; TRANSMEM 261 281 Helical; Name=Segment S6. {ECO:0000255}. TOPO_DOM 1 66 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 88 106 Extracellular. {ECO:0000255}.; TOPO_DOM 128 136 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 158 158 Extracellular. {ECO:0000255}.; TOPO_DOM 174 195 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 217 222 Extracellular. {ECO:0000255}.; TOPO_DOM 244 260 Extracellular. {ECO:0000255}.; TOPO_DOM 282 442 Cytoplasmic. {ECO:0000255}. FUNCTION: Voltage-gated calcium channel that plays a central role in sperm cell hyperactivation. Controls calcium entry to mediate the hyperactivated motility, a step needed for sperm motility which is essential late in the preparation of sperm for fertilization. Activated by intracellular alkalinization. {ECO:0000269|PubMed:17227845, ECO:0000269|PubMed:17344468}. SUBCELLULAR LOCATION: Cell projection, cilium, flagellum membrane {ECO:0000269|PubMed:16107607, ECO:0000269|PubMed:17227845}; Multi-pass membrane protein {ECO:0000269|PubMed:16107607, ECO:0000269|PubMed:17227845}. Note=Specifically located in the principal piece of sperm tail. SUBUNIT: Heterotetramer; possibly composed of CATSPER1, CATSPER2, CATSPER3 and CATSPER4 (Potential). Component of the CatSper complex. Interacts with CATSPER1. {ECO:0000269|PubMed:17227845, ECO:0000269|PubMed:21224844, ECO:0000305}. TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:16107607, ECO:0000269|PubMed:17227845}. +A2RTF1 CTSRB_MOUSE Cation channel sperm-associated protein subunit beta (CatSper-beta) 1109 126,108 Chain (1); Glycosylation (5); Sequence conflict (2); Transmembrane (4) TRANSMEM 3 23 Helical. {ECO:0000255}.; TRANSMEM 73 93 Helical. {ECO:0000255}.; TRANSMEM 244 264 Helical. {ECO:0000255}.; TRANSMEM 1060 1080 Helical. {ECO:0000255}. FUNCTION: Probably involved in sperm cell hyperactivation via its association with CATSPER1. Sperm cell hyperactivation is needed for sperm motility which is essential late in the preparation of sperm for fertilization. {ECO:0000269|PubMed:17478420}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Component of the CatSper complex. {ECO:0000269|PubMed:17478420, ECO:0000269|PubMed:19516020, ECO:0000269|PubMed:21224844}. TISSUE SPECIFICITY: Testis-specific. Specifically present in the principal piece of sperm tail (at protein level). Specifically expressed in the seminiferous tubules but not in the interstitial cells. Within the tubules, it is expressed in spermatocytes and spermatids, but not in spermatogonia. {ECO:0000269|PubMed:17478420}. +P0DP43 CTSRE_MOUSE Cation channel sperm-associated protein subunit epsilon (CatSper-epsilon) (CatSperepsilon) (C1orf101-like protein) 985 113,803 Chain (1); Glycosylation (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 938 958 Helical. {ECO:0000255}. TOPO_DOM 36 937 Extracellular. {ECO:0000305}.; TOPO_DOM 959 985 Cytoplasmic. {ECO:0000305}. FUNCTION: Auxiliary component of the CatSper complex, a complex involved in sperm cell hyperactivation (PubMed:28226241). Sperm cell hyperactivation is needed for sperm motility which is essential late in the preparation of sperm for fertilization (PubMed:28226241). {ECO:0000269|PubMed:28226241}. SUBCELLULAR LOCATION: Cell projection, cilium, flagellum membrane {ECO:0000269|PubMed:28226241}; Single-pass type I membrane protein {ECO:0000255}. Note=Specifically located in the principal piece of sperm tail. {ECO:0000269|PubMed:28226241}. SUBUNIT: Component of the CatSper complex. {ECO:0000269|PubMed:28226241}. TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:28226241}. +Q8BG15 CTSL2_MOUSE CTD small phosphatase-like protein 2 (CTDSP-like 2) (EC 3.1.3.-) 465 52,813 Alternative sequence (6); Chain (1); Domain (1); Erroneous initiation (1); Modified residue (9); Sequence conflict (2) FUNCTION: Probable phosphatase. {ECO:0000250}. +B9EJA2 CTTB2_MOUSE Cortactin-binding protein 2 (CortBP2) 1648 178,774 Alternative sequence (6); Chain (1); Coiled coil (1); Modified residue (2); Mutagenesis (4); Repeat (6); Sequence caution (1); Sequence conflict (3) FUNCTION: Regulates the dendritic spine distribution of CTTN/cortactin in hippocampal neurons, and thus controls dendritic spinogenesis and dendritic spine maintenance. {ECO:0000269|PubMed:23015759}. SUBCELLULAR LOCATION: Cytoplasm, cell cortex. Cell projection, dendritic spine. Note=Remains associated with dendritic spines even after glutamate stimulation. {ECO:0000250}. SUBUNIT: Interacts with CTTN/cortactin SH3 domain. Interacts with STRN, STRN4/zinedin and MOB4/phocein; this interaction may regulate dendritic spine distribution of STRN and STRN4 in hippocampal neurons (By similarity). Activation of glutamate receptors weakens the interaction with STRN and STRN4 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Isoform 2 is predominantly expressed in brain (at protein level). In the brain, expressed at high levels in hypothalamus and striatum and at lower levels in cerebellum and cortex. {ECO:0000269|PubMed:22262902, ECO:0000269|PubMed:23015759}. +P22387 EDN1_MOUSE Endothelin-1 (ET-1) (Preproendothelin-1) (PPET1) [Cleaved into: Big endothelin-1] 202 22,809 Disulfide bond (2); Peptide (2); Propeptide (2); Region (1); Sequence conflict (2); Signal peptide (1); Site (1) FUNCTION: Endothelins are endothelium-derived vasoconstrictor peptides. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Highest expression in the adult is in lung. Lower levels found in heart, kidney, brain and intestine. In the embryo, expressed in outer and inner pharyngeal arch surfaces. Also expressed in endothelium of dorsal aorta and arch arteries, and in epithelium of pharyngeal pouches. {ECO:0000269|PubMed:8824799}. +Q02248 CTNB1_MOUSE Catenin beta-1 (Beta-catenin) 781 85,471 Beta strand (4); Chain (1); Erroneous initiation (1); Glycosylation (1); Helix (42); Initiator methionine (1); Modified residue (20); Mutagenesis (4); Region (3); Repeat (12); Sequence conflict (3); Turn (4) FUNCTION: Key downstream component of the canonical Wnt signaling pathway. In the absence of Wnt, forms a complex with AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on N-terminal Ser and Thr residues and ubiquitination of CTNNB1 via BTRC and its subsequent degradation by the proteasome. In the presence of Wnt ligand, CTNNB1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the TCF/LEF family, leading to activate Wnt responsive genes. Involved in the regulation of cell adhesion, as component of an E-cadherin:catenin adhesion complex. Acts as a negative regulator of centrosome cohesion. Involved in the CDK2/PTPN6/CTNNB1/CEACAM1 pathway of insulin internalization. Blocks anoikis of malignant kidney and intestinal epithelial cells and promotes their anchorage-independent growth by down-regulating DAPK2. Disrupts PML function and PML-NB formation by inhibiting RANBP2-mediated sumoylation of PML (By similarity). Promotes neurogenesis by maintaining sympathetic neuroblasts within the cell cycle (PubMed:21325504). {ECO:0000250|UniProtKB:P35222, ECO:0000269|PubMed:16325582, ECO:0000269|PubMed:18093941, ECO:0000269|PubMed:21325504}. PTM: Phosphorylation by GSK3B requires prior phosphorylation of Ser-45 by another kinase. Phosphorylation proceeds then from Thr-41 to Ser-33. Phosphorylated by NEK2. EGF stimulates tyrosine phosphorylation. Phosphorylation on Tyr-654 decreases CDH1 binding and enhances TBP binding (By similarity). Phosphorylated on Ser-33 and Ser-37 by HIPK2. This phosphorylation triggers proteasomal degradation. Phosphorylation at Ser-552 by AMPK promotes stabilizion of the protein, enhancing TCF/LEF-mediated transcription. Phosphorylation on Ser-191 and Ser-246 by CDK5. Phosphorylation by CDK2 regulates insulin internalization (By similarity). Phosphorylation by PTK6 at Tyr-64, Tyr-142, Tyr-331 and/or Tyr-333 with the predominant site at Tyr-64 is not essential for inhibition of transcriptional activity (By similarity). {ECO:0000250}.; PTM: Ubiquitinated by the SCF(BTRC) E3 ligase complex when phosphorylated by GSK3B, leading to its degradation. Ubiquitinated by a E3 ubiquitin ligase complex containing UBE2D1, SIAH1, CACYBP/SIP, SKP1, APC and TBL1X, leading to its subsequent proteasomal degradation (By similarity). {ECO:0000250}.; PTM: S-nitrosylation at Cys-619 within adherens junctions promotes VEGF-induced, NO-dependent endothelial cell permeability by disrupting interaction with E-cadherin, thus mediating disassembly adherens junctions. {ECO:0000269|PubMed:20705246}.; PTM: O-glycosylation at Ser-23 decreases nuclear localization and transcriptional activity, and increases localization to the plasma membrane and interaction with E-cadherin CDH1. {ECO:0000250|UniProtKB:Q96S06}.; PTM: Deacetylated at Lys-49 by SIRT1. {ECO:0000250|UniProtKB:P35222}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton. Cell junction, adherens junction {ECO:0000269|PubMed:20705246}. Cell junction {ECO:0000250|UniProtKB:B6V8E6}. Cell membrane {ECO:0000250|UniProtKB:P35222}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P35222}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:P35222}. Cell junction, synapse {ECO:0000269|PubMed:20705246}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:21623382}. Note=Colocalized with RAPGEF2 and TJP1 at cell-cell contacts (By similarity). Cytoplasmic when it is unstabilized (high level of phosphorylation) or bound to CDH1. Translocates to the nucleus when it is stabilized (low level of phosphorylation). Interaction with GLIS2 and MUC1 promotes nuclear translocation. Interaction with EMD inhibits nuclear localization. The majority of beta-catenin is localized to the cell membrane. In interphase, colocalizes with CROCC between CEP250 puncta at the proximal end of centrioles, and this localization is dependent on CROCC and CEP250. In mitosis, when NEK2 activity increases, it localizes to centrosomes at spindle poles independent of CROCC. Colocalizes with CDK5 in the cell-cell contacts and plasma membrane of undifferentiated and differentiated neuroblastoma cells. Interaction with FAM53B promotes translocation to the nucleus (By similarity). {ECO:0000250|UniProtKB:B6V8E6, ECO:0000250|UniProtKB:P35222}. SUBUNIT: Two separate complex-associated pools are found in the cytoplasm. The majority is present as component of an E-cadherin/ catenin adhesion complex composed of at least E-cadherin/CDH1 and beta-catenin/CTNNB1, and possibly alpha-catenin/CTNNA1; the complex is located to adherens junctions. The stable association of CTNNA1 is controversial as CTNNA1 was shown not to bind to F-actin when assembled in the complex. Alternatively, the CTNNA1-containing complex may be linked to F-actin by other proteins such as LIMA1. Binds SLC9A3R1. Interacts with PTPRU (via the cytoplasmic juxtamembrane domain) and with EMD. Interacts with SESTD1 and TRPC4. Interacts with CAV1. Interacts with PTPRJ. Interacts with PKT7. Interacts with FAT1 (via the cytoplasmic domain). Interacts with CDK2, NDRG2 and NANOS1. Interacts with NEK2 and CDK5. Interacts with CARM1, CXADR, PCDH11Y and PTK6. Interacts with RAPGEF2. Interacts with SOX7; this interaction may lead to proteasomal degradation of active CTNNB1 and thus inhibition of Wnt/beta-catenin-stimulated transcription. Identified in a complex with HINT1 and MITF. Interacts with FHIT. Interacts with FERMT2. Identified in a complex with TCF4 and FERMT2. Another cytoplasmic pool is part of a large complex containing AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on N-terminal Ser and Thr residues and ubiquitination of CTNNB1 via BTRC and its subsequent degradation by the proteasome. Wnt-dependent activation of DVL antagonizes the action of GSK3B. When GSK3B activity is inhibited the complex dissociates, CTNNB1 is dephosphorylated and is no longer targeted for destruction. The stabilized protein translocates to the nucleus, where it binds TCF/LEF-1 family members, TBP, BCL9, BCL9L and possibly also RUVBL1 and CHD8. Interacts with TAX1BP3 (via the PDZ domain); this interaction inhibits the transcriptional activity of CTNNB1. Interacts with AJAP1, BAIAP1 and CTNNA3. Interacts with TRPV4; the TRPV4 and CTNNB1 complex can interact with CDH1. Interacts with VCL. The CTNNB1 and TCF4 complex interacts with PML. Interacts with XIRP1. Binds CTNNBIP and EP300. CTNNB1 forms a ternary complex with LEF1 and EP300 that is disrupted by CTNNBIP1 binding. Interacts directly with AXIN1; the interaction is regulated by CDK2 phosphorylation of AXIN1. Interacts with GLIS2. Interacts with SCRIB. Interacts with TNIK and TCF7L2. Interacts with SLC30A9. Interacts with RORA. May interact with P-cadherin/CDH3. Interacts with RNF220 (By similarity). Interacts with CTNND2 (By similarity). Interacts (via the C-terminal region) with CBY1 (By similarity). The complex composed, at least, of APC, CTNNB1 and GSK3B interacts with JPT1; the interaction requires the inactive form of GSK3B (phosphorylated at 'Ser-9') (By similarity). Interacts with DLG5 (PubMed:25232112). Interacts with FAM53B; promoting translocation to the nucleus. Interacts with TMEM170B (By similarity). Interacts with AHI1 (By similarity). Interacts with GID8 (By similarity). Component of an cadherin:catenin adhesion complex composed of at least of CDH26, beta-catenin/CTNNB1, alpha-catenin/CTNNA1 and p120 catenin/CTNND1 (By similarity). {ECO:0000250|UniProtKB:P35222, ECO:0000269|PubMed:10581160, ECO:0000269|PubMed:10772923, ECO:0000269|PubMed:10882138, ECO:0000269|PubMed:11348595, ECO:0000269|PubMed:11590244, ECO:0000269|PubMed:11707392, ECO:0000269|PubMed:12408825, ECO:0000269|PubMed:12874278, ECO:0000269|PubMed:14687547, ECO:0000269|PubMed:15063782, ECO:0000269|PubMed:17052462, ECO:0000269|PubMed:17289029, ECO:0000269|PubMed:17344318, ECO:0000269|PubMed:17925400, ECO:0000269|PubMed:19458197, ECO:0000269|PubMed:19816403, ECO:0000269|PubMed:20086044, ECO:0000269|PubMed:20413591, ECO:0000269|PubMed:25232112, ECO:0000269|PubMed:7982500, ECO:0000269|PubMed:9783587}. TISSUE SPECIFICITY: Expressed in cerebellar granule neurons (at protein level). {ECO:0000269|PubMed:21623382}. +Q3U308 CTU2_MOUSE Cytoplasmic tRNA 2-thiolation protein 2 514 56,105 Chain (1); Erroneous initiation (1); Frameshift (1); Initiator methionine (1); Modified residue (3) tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis. FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). May act by forming a heterodimer with CTU1/ATPBD3 that ligates sulfur from thiocarboxylated URM1 onto the uridine of tRNAs at wobble position. {ECO:0000255|HAMAP-Rule:MF_03054}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03054}. SUBUNIT: Component of a complex at least composed of URM1, CTU2/NCS2 and CTU1/ATPBD3. {ECO:0000255|HAMAP-Rule:MF_03054}. +Q99J10 CTU1_MOUSE Cytoplasmic tRNA 2-thiolation protein 1 (EC 2.7.7.-) (ATP-binding domain-containing protein 3) (Cytoplasmic tRNA adenylyltransferase 1) 420 43,823 Chain (1); Modified residue (1) tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis. FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Directly binds tRNAs and probably acts by catalyzing adenylation of tRNAs, an intermediate required for 2-thiolation. It is unclear whether it acts as a sulfurtransferase that transfers sulfur from thiocarboxylated URM1 onto the uridine of tRNAs at wobble position. {ECO:0000255|HAMAP-Rule:MF_03053}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03053}. SUBUNIT: Component of a complex at least composed of URM1, CTU2/NCS2 and CTU1/ATPBD3. May form a heterodimer with CTU2/NCS2. {ECO:0000255|HAMAP-Rule:MF_03053}. +P22389 EDN2_MOUSE Endothelin-2 (ET-2) (Preproendothelin-2) (PPET2) (Vasoactive intestinal contractor) (VIC) 175 19,538 Disulfide bond (2); Peptide (1); Propeptide (2); Region (1); Sequence conflict (2); Signal peptide (1); Site (1) FUNCTION: Vasoconstrictor. SUBCELLULAR LOCATION: Secreted. +O88327 CTNL1_MOUSE Alpha-catulin (Alpha-catenin-related protein) (ACRP) (Catenin alpha-like protein 1) 731 81,462 Chain (1); Compositional bias (1); Modified residue (2); Sequence conflict (3) FUNCTION: May modulate the Rho pathway signaling by providing a scaffold for the Lbc Rho guanine nucleotide exchange factor (ARHGEF1). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. SUBUNIT: Interacts with ARHGEF1. {ECO:0000250}. +Q8BXZ0 CTXN3_MOUSE Cortexin-3 80 8,832 Chain (1); Transmembrane (1) TRANSMEM 28 48 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q9D4G1 CU062_MOUSE Uncharacterized protein C21orf62 homolog 230 25,918 Chain (1); Glycosylation (1); Signal peptide (1) +P48302 EDNRB_MOUSE Endothelin receptor type B (ET-B) (ET-BR) (Endothelin receptor non-selective type) 442 49,561 Chain (1); Disulfide bond (1); Glycosylation (1); Lipidation (3); Modified residue (6); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 102 126 Helical; Name=1. {ECO:0000255}.; TRANSMEM 138 163 Helical; Name=2. {ECO:0000255}.; TRANSMEM 176 197 Helical; Name=3. {ECO:0000255}.; TRANSMEM 219 243 Helical; Name=4. {ECO:0000255}.; TRANSMEM 272 296 Helical; Name=5. {ECO:0000255}.; TRANSMEM 325 350 Helical; Name=6. {ECO:0000255}.; TRANSMEM 363 389 Helical; Name=7. {ECO:0000255}. TOPO_DOM 27 101 Extracellular. {ECO:0000255}.; TOPO_DOM 127 137 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 164 175 Extracellular. {ECO:0000255}.; TOPO_DOM 198 218 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 244 271 Extracellular. {ECO:0000255}.; TOPO_DOM 297 324 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 351 362 Extracellular. {ECO:0000255}.; TOPO_DOM 390 442 Cytoplasmic. {ECO:0000255}. FUNCTION: Non-specific receptor for endothelin 1, 2, and 3. Mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. Essential component in the normal development of two neuronal crest-derived cell lineages. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P24530}; Multi-pass membrane protein. Note=internalized after activation by endothelins. {ECO:0000250|UniProtKB:P24530}. +Q8BL66 EEA1_MOUSE Early endosome antigen 1 1411 160,915 Chain (1); Coiled coil (1); Compositional bias (1); Erroneous termination (1); Modified residue (2); Sequence conflict (1); Zinc finger (2) FUNCTION: Binds phospholipid vesicles containing phosphatidylinositol 3-phosphate and participates in endosomal trafficking. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Early endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. SUBUNIT: Homodimer. Binds STX6. Binds RAB5A, RAB5B, RAB5C and RAB22A that have been activated by GTP-binding. Interacts with ERBB2 (By similarity). Interacts with RAB31. Interacts with SAMD9 AND SAMD9L (By similarity). May interact with PLEKHF2 (By similarity). {ECO:0000250|UniProtKB:Q15075}. DOMAIN: The FYVE-type zinc finger domain mediates interactions with phosphatidylinositol 3-phosphate in membranes of early endosomes and penetrates bilayers. The FYVE domain insertion into PtdIns(3)P-enriched membranes is substantially increased in acidic conditions (By similarity). {ECO:0000250}. +Q9JLB4 CUBN_MOUSE Cubilin (Intrinsic factor-cobalamin receptor) 3623 399,097 Chain (1); Disulfide bond (68); Domain (34); Glycosylation (39); Metal binding (16); Modified residue (1); Propeptide (1); Sequence conflict (10); Signal peptide (1); Site (1) FUNCTION: Cotransporter which plays a role in lipoprotein, vitamin and iron metabolism, by facilitating their uptake. Binds to ALB, MB, Kappa and lambda-light chains, TF, hemoglobin, GC, SCGB1A1, APOA1, high density lipoprotein, and the CBLIF-cobalamin complex. The binding of all ligands requires calcium. Serves as important transporter in several absorptive epithelia, including intestine, renal proximal tubules and embryonic yolk sac. Interaction with LRP2 mediates its trafficking throughout vesicles and facilitates the uptake of specific ligands like GC, hemoglobin, ALB, TF and SCGB1A1. Interaction with AMN controls its trafficking to the plasma membrane and facilitates endocytosis of ligands. May play an important role in the development of the peri-implantation embryo through internalization of APOA1 and cholesterol. Binds to LGALS3 at the maternal-fetal interface. {ECO:0000269|PubMed:10766831, ECO:0000269|PubMed:11278724, ECO:0000269|PubMed:11856751, ECO:0000269|PubMed:15342463}. PTM: The precursor is cleaved by a trans-Golgi proteinase furin. The result is a propeptide cleaved off (By similarity). {ECO:0000250}.; PTM: N-glycosylated. {ECO:0000269|PubMed:11856751, ECO:0000269|PubMed:19349973}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:15342463}; Peripheral membrane protein {ECO:0000305}. Cell membrane {ECO:0000250|UniProtKB:O60494}; Peripheral membrane protein {ECO:0000250|UniProtKB:O60494}. Membrane, coated pit {ECO:0000250|UniProtKB:O60494}. Endosome {ECO:0000250|UniProtKB:O60494}. Lysosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Colocalizes with AMN and LRP2 in the endocytotic apparatus of epithelial cells. {ECO:0000250}. SUBUNIT: Interacts with LRP2 in a dual-receptor complex in a calcium-dependent manner (By similarity). Component of the cubam complex composed of CUBN and AMN. The cubam complex can oligomerize and form cubam trimers. Found in a complex with PID1/PCLI1, LRP1 and CUBNI (By similarity). Interacts with LRP1 and PID1/PCLI1 (By similarity). {ECO:0000250}. DOMAIN: The CUB domains 5 to 8 mediate binding to CBLIF and ALB. CUB domains 1 and 2 mediate interaction with LRP2 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in kidney, thymus, ileum, placenta, small intestine and yolk sac. In kidney expressed on the apical brush border surface of proximal tubular cells, in particular in endosomes and recycling membranes vesicles, so-called dense apical tubules, which carry internalized receptors back to the cell surface. Expressed in fetal membranes of yolk sac, placenta of pregnant females. {ECO:0000269|PubMed:10766831, ECO:0000269|PubMed:11856751}. +Q8R3V6 CUED1_MOUSE CUE domain-containing protein 1 388 42,780 Chain (1); Compositional bias (1); Domain (1); Sequence conflict (2) +Q9WTX6 CUL1_MOUSE Cullin-1 (CUL-1) 776 89,692 Chain (1); Cross-link (1); Modified residue (1); Sequence conflict (5) Protein modification; protein ubiquitination. FUNCTION: Core component of multiple cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination of proteins involved in cell cycle progression, signal transduction and transcription. SCF complexes and ARIH1 collaborate in tandem to mediate ubiquitination of target proteins. In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. May contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and exchange of the substrate recognition component is mediated by TIP120A/CAND1. The functional specificity of the SCF complex depends on the F-box protein as substrate recognition component. SCF(BTRC) and SCF(FBXW11) direct ubiquitination of CTNNB1 and participate in Wnt signaling. SCF(FBXW11) directs ubiquitination of phosphorylated NFKBIA. SCF(BTRC) directs ubiquitination of NFKBIB, NFKBIE, ATF4, SMAD3, SMAD4, CDC25A, FBXO5 and probably NFKB2. SCF(BTRC) and/or SCF(FBXW11) direct ubiquitination of CEP68. SCF(SKP2) directs ubiquitination of phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition. SCF(SKP2) directs ubiquitination of ORC1, CDT1, RBL2, ELF4, CDKN1A, RAG2, FOXO1A, and probably MYC and TAL1. SCF(FBXW7) directs ubiquitination of cyclin E, NOTCH1 released notch intracellular domain (NICD), and probably PSEN1. SCF(FBXW2) directs ubiquitination of GCM1. SCF(FBXO32) directs ubiquitination of MYOD1. SCF(FBXO7) directs ubiquitination of BIRC2 and DLGAP5. SCF(FBXO33) directs ubiquitination of YBX1. SCF(FBXO1) directs ubiquitination of BCL6 and DTL but does not seem to direct ubiquitination of TP53. SCF(BTRC) mediates the ubiquitination of NFKBIA at 'Lys-21' and 'Lys-22'; the degradation frees the associated NFKB1-RELA dimer to translocate into the nucleus and to activate transcription. SCF(CCNF) directs ubiquitination of CCP110. SCF(FBXL3) and SCF(FBXL21) direct ubiquitination of CRY1 and CRY2. SCF(FBXO9) directs ubiquitination of TTI1 and TELO2. SCF(FBXO10) directs ubiquitination of BCL2. {ECO:0000250|UniProtKB:Q13616, ECO:0000269|PubMed:12140560, ECO:0000269|PubMed:23452855}. PTM: Neddylated; which enhances the ubiquitination activity of SCF. Deneddylated via its interaction with the COP9 signalosome (CSN) complex. {ECO:0000269|PubMed:20190741}.; PTM: (Microbial infection) Deneddylated by murine cytomegalovirus M48 leading to a S-phase-like environment that is required for efficient replication of the viral genome. {ECO:0000269|PubMed:20190741}. SUBUNIT: Component of multiple SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase complexes formed of CUL1, SKP1, RBX1 and a variable F-box domain-containing protein as substrate-specific subunit (PubMed:10097128, PubMed:12140560, PubMed:16880526, PubMed:23452855, PubMed:23452856). Component of the SCF(FBXW11) complex containing FBXW11. Component of the SCF(SKP2) complex containing SKP2, in which it interacts directly with SKP1, SKP2 and RBX1. Component of the SCF(FBXW2) complex containing FBXW2. Component of the SCF(FBXO32) complex containing FBXO32. Component of the probable SCF(FBXO7) complex containing FBXO7. Component of the SCF(FBXO10) complex containing FBXO10. Component of the SCF(FBXO11) complex containing FBXO11. Component of the SCF(FBXO25) complex containing FBXO25. Component of the SCF(FBXO33) complex containing FBXO33. Component of the probable SCF(FBXO4) complex containing FBXO4. Component of the SCF(FBXO44) complex, composed of SKP1, CUL1 and FBXO44 (By similarity). Component of the SCF(BTRC) complex, composed of SKP1, CUL1 and BTRC (PubMed:10097128, PubMed:11735228). This complex binds phosphorylated NFKBIA (PubMed:10097128). Part of a SCF complex consisting of CUL1, RBX1, SKP1 and FBXO2. Component of a SCF(SKP2)-like complex containing CUL1, SKP1, TRIM21 and SKP2. Component of the SCF(FBXO17) complex, composed of SKP1, CUL1 and FBXO17. Component of the SCF(FBXO27) complex, composed of SKP1, CUL1 and FBXO27. Component of the SCF(CCNF) complex consisting of CUL1, RBX1, SKP1 and CCNF. Component of the SCF(FBXL3) complex composed of CUL1, SKP1, RBX1 and FBXL3. Component of the SCF(FBXL21) complex composed of CUL1, SKP1, RBX1 and FBXL21. Component of the SCF(FBXO9) composed of CUL1, SKP1, RBX1 and FBXO9. Component of the SCF(FBXW7) composed of CUL1, SKP1, RBX1 and FBXW7. Interacts with CHEK2; mediates CHEK2 ubiquitination and regulates its function. Part of a complex with TIP120A/CAND1 and RBX1. The unneddylated form interacts with TIP120A/CAND1 and the interaction mediates the exchange of the F-box substrate-specific subunit. Can self-associate (By similarity). Interacts with FBXW8 (PubMed:16880526). Interacts with RNF7 (By similarity). Interacts with CUL7; the interaction seems to be mediated by FBXW8 (PubMed:16880526). Interacts with TRIM21 (By similarity). Interacts with COPS2 (PubMed:11967155). Interacts with DCUN1D1 and UBE2M. Interacts with DCUN1D3. Interacts with DCUN1D4 (By similarity). Identified in a complex with RBX1 and GLMN (By similarity). Interacts with CEP68 as part of the SCF(FBXW11) complex; the interaction is probably mediated by FBXW11 and the complex also contains CDK5RAP2 and PCNT. Interacts (when neddylated) with ARIH1; leading to activate the E3 ligase activity of ARIH1. Interacts with COPS9. Interacts with UBXN1 (By similarity). Interacts with KAT7, probably as part of an SCF complex; the interaction mediates KAT7 ubiquitination (PubMed:23319590). Interacts with NOTCH2 (By similarity). {ECO:0000250|UniProtKB:Q13616, ECO:0000269|PubMed:10097128, ECO:0000269|PubMed:11735228, ECO:0000269|PubMed:11967155, ECO:0000269|PubMed:12140560, ECO:0000269|PubMed:16880526, ECO:0000269|PubMed:23319590, ECO:0000269|PubMed:23452855, ECO:0000269|PubMed:23452856}.; SUBUNIT: (Microbial infection) Interacts with murine cytomegalovirus M48. {ECO:0000269|PubMed:20190741}. TISSUE SPECIFICITY: Embryo fibroblasts and embryo preadipocytes. {ECO:0000269|PubMed:9663463}. +Q9D4H8 CUL2_MOUSE Cullin-2 (CUL-2) 745 86,877 Alternative sequence (1); Chain (1); Cross-link (1); Modified residue (2); Sequence conflict (1) Protein modification; protein ubiquitination. FUNCTION: Core component of multiple cullin-RING-based ECS (ElonginB/C-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination of target proteins. ECS complexes and ARIH1 collaborate in tandem to mediate ubiquitination of target proteins (By similarity). May serve as a rigid scaffold in the complex and may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and is inhibited by the association of the deneddylated cullin subunit with TIP120A/CAND1 (By similarity). The functional specificity of the ECS complex depends on the substrate recognition component. ECS(VHL) mediates the ubiquitination of hypoxia-inducible factor (HIF) (By similarity). {ECO:0000250|UniProtKB:Q13617}. PTM: Neddylated; which enhances the ubiquitination activity of ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complexes. CBC(VHL) complex formation seems to promote neddylation (By similarity). Deneddylated via its interaction with the COP9 signalosome (CSN) complex. {ECO:0000250|UniProtKB:Q13617}. SUBUNIT: Component of multiple ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complexes formed of CUL2, Elongin BC (ELOB and ELOC), RBX1 and a variable substrate-specific adapter. Component of the ECS(VHL) or CBC(VHL) complex containing VHL. Component of the ECS(MED8) complex with the probable substrate recognition component MED8. Component of the ECS(LRR1) complex with the probable substrate recognition component LRR1. Component of a probable ECS E3 ubiquitin-protein ligase complex containing CUL2, RBX1, ELOB, ELOC and FEM1B. Part of an E3 ubiquitin-protein ligase complex including ZYG11B, CUL2 and Elongin BC. Part of an E3 ubiquitin-protein ligase complex including ZYG11BL, CUL2 and Elongin BC. Interacts with RBX1, RNF7, FEM1B and TIP120A/CAND1. Interacts with COPS2, and MED8. Found in a complex composed of LIMD1, VHL, EGLN1/PHD2, ELOB and CUL2. Interacts with KLHDC10; which may be an E3 ubiquitin ligase complex substrate recognition component. Interacts (when neddylated) with ARIH1; leading to activate the E3 ligase activity of ARIH1 (By similarity). {ECO:0000250|UniProtKB:Q13617, ECO:0000269|PubMed:11967155, ECO:0000269|PubMed:12149480}. +Q80TT8 CUL9_MOUSE Cullin-9 (CUL-9) (p53-associated parkin-like cytoplasmic protein) 1865 209,160 Active site (1); Alternative sequence (5); Chain (1); Coiled coil (1); Compositional bias (2); Domain (1); Frameshift (1); Metal binding (24); Modified residue (3); Nucleotide binding (1); Region (1); Sequence conflict (5); Zinc finger (3) FUNCTION: Core component of a Cul9-RING ubiquitin-protein ligase complex, a complex that mediates ubiquitination and subsequent degradation of BIRC5 and is required to maintain microtubule dynamics and genome integrity. Acts downstream of the 3M complex, which inhibits CUL9 activity, leading to prevent ubiquitination of BIRC5 (PubMed:24793696). Cytoplasmic anchor protein in p53/TP53-associated protein complex. Regulates the subcellular localization of p53/TP53 and subsequent function. {ECO:0000269|PubMed:24793696}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21487039}. SUBUNIT: Part of a Cul9-RING complex at least composed of CUL9 and RBX1. Interacts with CUL7: interaction with CUL7 component of the 3M complex leads to inhibition of CUL9 activity. The CUL7-CUL9 heterodimer seems to interact specifically with TP53. Forms a complex with p53/TP53 in the cytoplasm of unstressed cells. Interacts with UBCH7 and UBCH8 (By similarity). {ECO:0000250}. DOMAIN: The IBR domain is required for interaction with UBCH7 and UBCH8. +Q9D8X1 CUTC_MOUSE Copper homeostasis protein cutC homolog 272 29,004 Chain (1) FUNCTION: May play a role in copper homeostasis. Can bind one Cu(1+) per subunit (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Homotetramer. {ECO:0000250}. +Q8C5N3 CWC22_MOUSE Pre-mRNA-splicing factor CWC22 homolog (Nucampholin homolog) 908 104,773 Alternative sequence (1); Chain (1); Compositional bias (5); Domain (2); Erroneous initiation (1); Modified residue (4); Sequence conflict (9) FUNCTION: Required for pre-mRNA splicing and for exon-junction complex (EJC) assembly. Hinders EIF4A3 from non-specifically binding RNA and escorts it to the splicing machinery to promote EJC assembly on mature mRNAs. Through its role in EJC assembly, required for nonsense-mediated mRNA decay (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus speckle {ECO:0000250}. Note=Concentrates around speckles, which are sites of pre-mRNA synthesis and processing, where it colocalizes with EJC core proteins. {ECO:0000250}. SUBUNIT: Component of the spliceosome C complex (By similarity). Interacts with EIF4A3 and PRPF19 in an RNA-independent manner (By similarity). Direct interaction with EIF4A3 is mediated by the MIF4G domain. Full interaction with EIF4A3 occurs only when EIF4A3 is not part of the EJC and prevents EIF4A3 binding to RNA (By similarity). {ECO:0000250}. +Q9D8N0 EF1G_MOUSE Elongation factor 1-gamma (EF-1-gamma) (eEF-1B gamma) 437 50,061 Chain (1); Cross-link (2); Domain (3); Initiator methionine (1); Modified residue (6); Sequence conflict (5) FUNCTION: Probably plays a role in anchoring the complex to other cellular components. {ECO:0000250}. SUBUNIT: EF-1 is composed of four subunits: alpha, beta, delta, and gamma. {ECO:0000250}. +Q3UZW7 EF2KT_MOUSE Protein-lysine N-methyltransferase EEF2KMT (EC 2.1.1.-) (eEF2-lysine methyltransferase) (eEF2-KMT) 335 36,940 Alternative sequence (2); Binding site (3); Chain (1); Modified residue (1); Region (1); Sequence conflict (1) FUNCTION: Catalyzes the trimethylation of eukaryotic elongation factor 2 (EEF2) on 'Lys-525'. {ECO:0000250|UniProtKB:Q96G04}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with FAM86B2 and FAM86C1. {ECO:0000250}. +O08796 EF2K_MOUSE Eukaryotic elongation factor 2 kinase (eEF-2 kinase) (eEF-2K) (EC 2.7.11.20) (Calcium/calmodulin-dependent eukaryotic elongation factor 2 kinase) 724 81,739 Chain (1); Domain (1); Initiator methionine (1); Modified residue (19); Nucleotide binding (1); Region (1) FUNCTION: Threonine kinase that regulates protein synthesis by controlling the rate of peptide chain elongation. Upon activation by a variety of upstream kinases including AMPK or TRPM7, phosphorylates the elongation factor EEF2 at a single site, renders it unable to bind ribosomes and thus inactive. In turn, the rate of protein synthesis is reduced. {ECO:0000269|PubMed:9144159}. PTM: Autophosphorylated at multiple residues, Thr-347 being the major site. Phosphorylated by AMP-activated protein kinase AMPK at Ser-397 leading to EEF2K activation and protein synthesis inhibition. Phosphorylated by TRPM7 at Ser-77 resulting in improved protein stability, higher EE2F phosphorylated and subsequently reduced rate of protein synthesis. Phosphorylation by other kinases such as CDK1 and MAPK13 at Ser-358 or RPS6KA1 and RPS6KB1 at Ser-365 instead decrease EEF2K activity and promote protein synthesis (By similarity). {ECO:0000250}. SUBUNIT: Monomer or homodimer (Probable). Interacts with Calmodulin/CALM1; this interaction is strictly required for phosphorylation activity (By similarity). {ECO:0000250|UniProtKB:O00418, ECO:0000305}. DOMAIN: The catalytic domain is located to N-terminal region. The neighbor region contains the calmodulin-binding domain (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed. Particularly abundant in skeletal muscle and heart. +Q3UP38 EFC4B_MOUSE EF-hand calcium-binding domain-containing protein 4B (Calcium release-activated channel regulator 2A) 310 35,840 Calcium binding (1); Chain (1); Coiled coil (1); Domain (2); Sequence conflict (1) FUNCTION: Ca(2+)-binding protein that plays a key role in store-operated Ca(2+) entry (SOCE) in T-cells by regulating CRAC channel activation. Acts as a cytoplasmic calcium-sensor that facilitates the clustering of ORAI1 and STIM1 at the junctional regions between the plasma membrane and the endoplasmic reticulum upon low Ca(2+) concentration. It thereby regulates CRAC channel activation, including translocation and clustering of ORAI1 and STIM1. Upon increase of cytoplasmic Ca(2+) resulting from opening of CRAC channels, dissociates from ORAI1 and STIM1, thereby destabilizing the ORAI1-STIM1 complex (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with ORAI1 and STIM1; the interaction is direct and takes place in absence of Ca(2+). Forms a complex with ORAI1 and STIM1 at low concentration of Ca(2+), the complex dissociates at elevated Ca(2+) concentrations. Interacts with ORAI2 and ORAI3 (By similarity). {ECO:0000250}. +Q9D3N2 EFCB1_MOUSE EF-hand calcium-binding domain-containing protein 1 212 24,606 Alternative sequence (5); Calcium binding (3); Chain (1); Domain (3); Sequence conflict (3) +Q8C5K5 CX038_MOUSE Uncharacterized protein CXorf38 homolog 320 36,589 Alternative sequence (1); Chain (1); Modified residue (2); Sequence conflict (1) +Q9D1F3 CX040_MOUSE Uncharacterized protein CXorf40 homolog 157 18,059 Chain (1) +Q6P1E8 EFCB6_MOUSE EF-hand calcium-binding domain-containing protein 6 (DJ-1-binding protein) (DJBP) 1516 175,771 Alternative sequence (3); Calcium binding (4); Chain (1); Domain (15); Erroneous initiation (2); Modified residue (5); Region (2); Sequence conflict (4) FUNCTION: Negatively regulates the androgen receptor by recruiting histone deacetylase complex, and protein DJ-1 antagonizes this inhibition by abrogation of this complex. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Binds PARK7. Part of a ternary complex containing PARK7, EFCAB6/DJBP and AR (By similarity). {ECO:0000250}. +Q9D454 CX049_MOUSE Uncharacterized protein CXorf49 homolog 513 55,249 Chain (1); Modified residue (3) +Q8C9R9 EFCB8_MOUSE EF-hand calcium-binding domain-containing protein 8 203 23,313 Chain (1); Domain (2) +Q80ZN9 CX6B2_MOUSE Cytochrome c oxidase subunit 6B2 (Cytochrome c oxidase subunit VIb isoform 2) (COX VIb-2) (Cytochrome c oxidase subunit VIb, testis-specific isoform) 88 10,521 Chain (1); Disulfide bond (2); Domain (1); Motif (2) FUNCTION: This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. This protein may be one of the heme-binding subunits of the oxidase (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. TISSUE SPECIFICITY: Testis specific. {ECO:0000269|PubMed:12874793}. +Q9Z0D9 CX3C1_MOUSE CX3C chemokine receptor 1 (C-X3-C CKR-1) (CX3CR1) (Fractalkine receptor) 354 40,266 Chain (1); Disulfide bond (1); Modified residue (1); Topological domain (8); Transmembrane (7) TRANSMEM 33 60 Helical; Name=1. {ECO:0000255}.; TRANSMEM 71 91 Helical; Name=2. {ECO:0000255}.; TRANSMEM 105 126 Helical; Name=3. {ECO:0000255}.; TRANSMEM 144 168 Helical; Name=4. {ECO:0000255}.; TRANSMEM 197 216 Helical; Name=5. {ECO:0000255}.; TRANSMEM 233 257 Helical; Name=6. {ECO:0000255}.; TRANSMEM 275 298 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 32 Extracellular. {ECO:0000255}.; TOPO_DOM 61 70 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 92 104 Extracellular. {ECO:0000255}.; TOPO_DOM 127 143 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 169 196 Extracellular. {ECO:0000255}.; TOPO_DOM 217 232 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 258 274 Extracellular. {ECO:0000255}.; TOPO_DOM 299 354 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for the CX3C chemokine fractalkine (CX3CL1); binds to CX3CL1 and mediates both its adhesive and migratory functions. {ECO:0000269|PubMed:9918795}. PTM: This protein is not N-glycosylated which is unusual for G-protein-coupled receptors. {ECO:0000250|UniProtKB:P35411}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P49238}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Found in a ternary complex with CX3CL1 and ITGAV:ITGB3 or ITGA4:ITGB1. {ECO:0000250|UniProtKB:P49238}. +Q6W5C0 CXCL3_MOUSE C-X-C motif chemokine 3 (Dendritic cell inflammatory protein 1) 100 10,686 Chain (1); Disulfide bond (2); Frameshift (1); Signal peptide (1) FUNCTION: Ligand for CXCR2. Has chemotactic activity for neutrophils. May play a role in inflammation and exert its effects on endothelial cells in an autocrine fashion. {ECO:0000250|UniProtKB:Q10746, ECO:0000269|PubMed:14764687}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q10746}. +P23242 CXA1_MOUSE Gap junction alpha-1 protein (Connexin-43) (Cx43) (Gap junction 43 kDa heart protein) 382 43,004 Chain (1); Cross-link (2); Disulfide bond (2); Modified residue (18); Region (2); Sequence conflict (2); Topological domain (5); Transmembrane (4) TRANSMEM 14 36 Helical. {ECO:0000255}.; TRANSMEM 77 99 Helical. {ECO:0000255}.; TRANSMEM 155 177 Helical. {ECO:0000255}.; TRANSMEM 209 231 Helical. {ECO:0000255}. TOPO_DOM 1 13 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 37 76 Extracellular. {ECO:0000255}.; TOPO_DOM 100 154 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 178 208 Extracellular. {ECO:0000255}.; TOPO_DOM 232 382 Cytoplasmic. {ECO:0000255}. FUNCTION: Gap junction protein that acts as a regulator of bladder capacity. A gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. Negative regulator of bladder functional capacity: acts by enhancing intercellular electrical and chemical transmission, thus sensitizing bladder muscles to cholinergic neural stimuli and causing them to contract. May play a role in cell growth inhibition through the regulation of NOV expression and localization (PubMed:15181016). Plays an essential role in gap junction communication in the ventricles (PubMed:26403541). {ECO:0000269|PubMed:15181016, ECO:0000269|PubMed:22549838, ECO:0000269|PubMed:26403541}.; FUNCTION: Connexin 43 is possibly the ATP-induced pore of mouse macrophages. {ECO:0000269|PubMed:22549838}. PTM: Phosphorylation at Ser-325, Ser-328 and Ser-330 by CK1 modulates gap junction assembly. Phosphorylated at Ser-368 by PRKCG; phosphorylation induces disassembly of gap junction plaques and inhibition of gap junction activity. Phosphorylation at Ser-368 by PRKCD triggers its internalization into small vesicles leading to proteasome-mediated degradation (By similarity). {ECO:0000250|UniProtKB:P08050, ECO:0000250|UniProtKB:P17302, ECO:0000250|UniProtKB:Q6TYA7}.; PTM: Sumoylated with SUMO1, SUMO2 and SUMO3, which may regulate the level of functional Cx43 gap junctions at the plasma membrane. May be desumoylated by SENP1 or SENP2 (By similarity). {ECO:0000250}.; PTM: S-nitrosylation at Cys-271 is enriched at the muscle endothelial gap junction in arteries, it augments channel permeability and may regulate of smooth muscle cell to endothelial cell communication. {ECO:0000269|PubMed:21071693}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26403541}; Multi-pass membrane protein {ECO:0000255}. Cell junction, gap junction {ECO:0000250|UniProtKB:P17302}. Endoplasmic reticulum {ECO:0000269|PubMed:18079109, ECO:0000269|PubMed:20940304}. Note=Localizes at the intercalated disk (ICD) in cardiomyocytes and proper localization at ICD is dependent on TMEM65. {ECO:0000269|PubMed:26403541}. SUBUNIT: A connexon is composed of a hexamer of connexins. Interacts with CSNK1D (By similarity). Interacts with RIC1/CIP150 (By similarity). Interacts (via C-terminus) with TJP1 (By similarity). Interacts (via C-terminus) with SRC (via SH3 domain) (By similarity). Interacts (not ubiquitinated) with UBQLN4 (via UBA domain). Interacts with CNST. Interacts with SGSM3. Interacts with NOV (By similarity). Interacts with TMEM65 (PubMed:26403541). {ECO:0000250|UniProtKB:P08050, ECO:0000250|UniProtKB:P17302, ECO:0000269|PubMed:15709751, ECO:0000269|PubMed:18079109, ECO:0000269|PubMed:19864490, ECO:0000269|PubMed:20940304, ECO:0000269|PubMed:26403541}. TISSUE SPECIFICITY: Expressed in heart, non-sensory epithelial cells, and in fibrocytes of the spiral ligament and the spiral limbus. Expressed in bladder smooth muscle cells (at protein level). Expressed in astrocytes (at protein level) (PubMed:15213231). {ECO:0000269|PubMed:11741837, ECO:0000269|PubMed:15213231, ECO:0000269|PubMed:2178193, ECO:0000269|PubMed:22549838}. +P28230 CXB1_MOUSE Gap junction beta-1 protein (Connexin-32) (Cx32) 283 32,004 Chain (1); Modified residue (4); Sequence conflict (2); Topological domain (5); Transmembrane (4) TRANSMEM 23 45 Helical. {ECO:0000255}.; TRANSMEM 76 95 Helical. {ECO:0000255}.; TRANSMEM 131 153 Helical. {ECO:0000255}.; TRANSMEM 192 214 Helical. {ECO:0000255}. TOPO_DOM 1 22 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 46 75 Extracellular. {ECO:0000255}.; TOPO_DOM 96 130 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 154 191 Extracellular. {ECO:0000255}.; TOPO_DOM 215 283 Cytoplasmic. {ECO:0000255}. FUNCTION: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell junction, gap junction. SUBUNIT: A connexon is composed of a hexamer of connexins. Interacts with CNST. {ECO:0000269|PubMed:19864490}. +O54851 CXD2_MOUSE Gap junction delta-2 protein (Connexin-36) (Cx36) (Gap junction alpha-9 protein) 321 36,082 Chain (1); Sequence conflict (3); Topological domain (5); Transmembrane (4) TRANSMEM 20 42 Helical. {ECO:0000255}.; TRANSMEM 76 98 Helical. {ECO:0000255}.; TRANSMEM 198 220 Helical. {ECO:0000255}.; TRANSMEM 253 275 Helical. {ECO:0000255}. TOPO_DOM 1 19 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 43 75 Extracellular. {ECO:0000255}.; TOPO_DOM 99 197 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 221 252 Extracellular. {ECO:0000255}.; TOPO_DOM 276 321 Cytoplasmic. {ECO:0000255}. FUNCTION: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell junction, gap junction. SUBUNIT: A connexon is composed of a hexamer of connexins. TISSUE SPECIFICITY: Highly expressed in neurons. +P28231 CXB3_MOUSE Gap junction beta-3 protein (Connexin-31) (Cx31) 270 30,902 Chain (1); Topological domain (5); Transmembrane (4) TRANSMEM 21 40 Helical. {ECO:0000255}.; TRANSMEM 76 98 Helical. {ECO:0000255}.; TRANSMEM 127 149 Helical. {ECO:0000255}.; TRANSMEM 189 211 Helical. {ECO:0000255}. TOPO_DOM 1 20 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 41 75 Extracellular. {ECO:0000255}.; TOPO_DOM 99 126 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 150 188 Extracellular. {ECO:0000255}.; TOPO_DOM 212 270 Cytoplasmic. {ECO:0000255}. FUNCTION: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell junction, gap junction. SUBUNIT: A connexon is composed of a hexamer of connexins. Interacts with CNST. {ECO:0000269|PubMed:19864490}. +Q921C1 CXG3_MOUSE Gap junction gamma-3 protein (Connexin-29) (Cx29) (Gap junction epsilon-1 protein) 269 30,293 Chain (1); Modified residue (1); Topological domain (5); Transmembrane (4) TRANSMEM 34 54 Helical. {ECO:0000255}.; TRANSMEM 87 107 Helical. {ECO:0000255}.; TRANSMEM 146 166 Helical. {ECO:0000255}.; TRANSMEM 206 226 Helical. {ECO:0000255}. TOPO_DOM 1 33 Extracellular. {ECO:0000255}.; TOPO_DOM 55 86 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 108 145 Extracellular. {ECO:0000255}.; TOPO_DOM 167 205 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 227 269 Extracellular. {ECO:0000255}. FUNCTION: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell junction, gap junction {ECO:0000250}. SUBUNIT: A connexon is composed of a hexamer of connexins. {ECO:0000250}. TISSUE SPECIFICITY: CNS specific. Expression is restricted to brain, spinal cord, and sciatic nerve. +Q8K0D5 EFGM_MOUSE Elongation factor G, mitochondrial (EF-Gmt) (Elongation factor G 1, mitochondrial) (mEF-G 1) (Elongation factor G1) 751 83,550 Chain (1); Domain (1); Modified residue (2); Nucleotide binding (3); Sequence conflict (4); Transit peptide (1) Protein biosynthesis; polypeptide chain elongation. FUNCTION: Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. Does not mediate the disassembly of ribosomes from messenger RNA at the termination of mitochondrial protein biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03061}. SUBCELLULAR LOCATION: Mitochondrion. +Q8CDU5 EFHB_MOUSE EF-hand domain-containing family member B 853 95,743 Calcium binding (2); Chain (1); Domain (2); Sequence conflict (1) +P52795 EFNB1_MOUSE Ephrin-B1 (CEK5 receptor ligand) (CEK5-L) (EFL-3) (ELK ligand) (ELK-L) (EPH-related receptor tyrosine kinase ligand 2) (LERK-2) (Stimulated by retinoic acid gene 1 protein) [Cleaved into: Ephrin-B1 C-terminal fragment (Ephrin-B1 CTF); Ephrin-B1 intracellular domain (Ephrin-B1 ICD)] 345 37,859 Chain (3); Disulfide bond (2); Domain (1); Glycosylation (1); Modified residue (2); Motif (2); Region (1); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 237 257 Helical. {ECO:0000255}. TOPO_DOM 25 236 Extracellular. {ECO:0000255}.; TOPO_DOM 258 345 Cytoplasmic. {ECO:0000255}. FUNCTION: Cell surface transmembrane ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development (PubMed:7929389, PubMed:10704386). Binding to Eph receptors residing on adjacent cells leads to contact-dependent bidirectional signaling into neighboring cells (PubMed:7929389, PubMed:10704386). Shows high affinity for the receptor tyrosine kinase EPHB1/ELK (By similarity). Can also bind EPHB2 and EPHB3 (PubMed:7929389). Binds to, and induces the collapse of, commissural axons/growth cones in vitro (PubMed:10704386). May play a role in constraining the orientation of longitudinally projecting axons (PubMed:10704386). {ECO:0000250|UniProtKB:P98172, ECO:0000269|PubMed:10704386, ECO:0000269|PubMed:7929389}. PTM: Inducible phosphorylation of tyrosine residues in the cytoplasmic domain. {ECO:0000250|UniProtKB:P98172}.; PTM: Proteolytically processed. The ectodomain is cleaved, probably by a metalloprotease, to produce a membrane-tethered C-terminal fragment. This fragment is then further processed by the gamma-secretase complex to yield a soluble intracellular domain peptide which can translocate to the nucleus. The intracellular domain peptide is highly labile suggesting that it is targeted for degradation by the proteasome. {ECO:0000250|UniProtKB:P98172}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7929389, ECO:0000305|PubMed:10704386}; Single-pass type I membrane protein {ECO:0000255}. Membrane raft {ECO:0000269|PubMed:10197531}. Note=May recruit GRIP1 and GRIP2 to membrane raft domains. {ECO:0000269|PubMed:10197531}.; SUBCELLULAR LOCATION: Ephrin-B1 C-terminal fragment: Cell membrane {ECO:0000250|UniProtKB:P98172}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: Ephrin-B1 intracellular domain: Nucleus {ECO:0000269|PubMed:19515908}. Note=Colocalizes with ZHX2 in the nucleus. {ECO:0000269|PubMed:19515908}. SUBUNIT: Interacts (via PDZ-binding motif) with GRIP1 and GRIP2 (via PDZ domain 6) (By similarity). Interacts with TLE1 (PubMed:21429299). The intracellular domain peptide interacts with ZHX2; the interaction enhances ZHX2 transcriptional repression activity (PubMed:19515908). {ECO:0000250|UniProtKB:P98172, ECO:0000269|PubMed:19515908, ECO:0000269|PubMed:21429299}. TISSUE SPECIFICITY: Expressed on lateral floor plate cells, specifically on commissural axon segments that have passed through the floor plate. Expressed in cells of the retinal ganglion cell layer during retinal axon guidance to the optic disk (PubMed:10704386). Expressed in myogenic progenitor cells (PubMed:27446912). {ECO:0000269|PubMed:10704386, ECO:0000269|PubMed:27446912}. +P52800 EFNB2_MOUSE Ephrin-B2 (ELF-2) (EPH-related receptor tyrosine kinase ligand 5) (LERK-5) (HTK ligand) (HTK-L) 336 37,202 Beta strand (8); Chain (1); Disulfide bond (2); Domain (1); Erroneous initiation (1); Glycosylation (2); Helix (3); Modified residue (3); Motif (1); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 233 253 Helical. {ECO:0000255}. TOPO_DOM 29 232 Extracellular. {ECO:0000255}.; TOPO_DOM 254 336 Cytoplasmic. {ECO:0000255}. FUNCTION: Cell surface transmembrane ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Binds to receptor tyrosine kinase including EPHA4, EPHA3 and EPHB4. Together with EPHB4 plays a central role in heart morphogenesis and angiogenesis through regulation of cell adhesion and cell migration. EPHB4-mediated forward signaling controls cellular repulsion and segregation from EFNB2-expressing cells. May play a role in constraining the orientation of longitudinally projecting axons. {ECO:0000269|PubMed:10704386}. PTM: Inducible phosphorylation of tyrosine residues in the cytoplasmic domain. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P52799}; Single-pass type I membrane protein {ECO:0000255}. SUBUNIT: Interacts with PDZRN3. Binds to the ephrin receptor EPHA3, EPHA4 and EPHB4 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed on lateral floor plate cells, specifically on commissural axon segments that have passed through the floor plate. Expressed in cells of the retinal ganglion cell layer during retinal axon guidance to the optic disk (PubMed:7651410, PubMed:10704386). Expressed in myogenic progenitor cells (PubMed:27446912). {ECO:0000269|PubMed:10704386, ECO:0000269|PubMed:27446912, ECO:0000269|PubMed:7651410}. +O35393 EFNB3_MOUSE Ephrin-B3 340 35,885 Beta strand (8); Chain (1); Disulfide bond (2); Domain (1); Glycosylation (1); Helix (2); Modified residue (2); Motif (1); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 228 248 Helical. {ECO:0000255}. TOPO_DOM 28 227 Extracellular. {ECO:0000255}.; TOPO_DOM 249 340 Cytoplasmic. {ECO:0000255}. FUNCTION: Cell surface transmembrane ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. May play a pivotal role in forebrain function. Binds to, and induce the collapse of, commissural axons/growth cones in vitro. May play a role in constraining the orientation of longitudinally projecting axons. {ECO:0000269|PubMed:10704386}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Interacts with GRIP1 and GRIP2. {ECO:0000250}. TISSUE SPECIFICITY: Expressed on lateral floor plate cells, specifically on commissural axon segments that have passed through the floor plate. Expressed in cells of the retinal ganglion cell layer during retinal axon guidance to the optic disk (PubMed:9484836, PubMed:10704386). Expressed in myogenic progenitor cells (PubMed:27446912). {ECO:0000269|PubMed:10704386, ECO:0000269|PubMed:27446912, ECO:0000269|PubMed:9484836}. +Q6NS52 DGKB_MOUSE Diacylglycerol kinase beta (DAG kinase beta) (EC 2.7.1.107) (Diglyceride kinase beta) (DGK-beta) 802 90,272 Alternative sequence (1); Calcium binding (2); Chain (1); Domain (3); Modified residue (3); Zinc finger (2) FUNCTION: Exhibits high phosphorylation activity for long-chain diacylglycerols. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +Q8VCR2 DHB13_MOUSE 17-beta-hydroxysteroid dehydrogenase 13 (17-beta-HSD 13) (EC 1.1.-.-) (Alcohol dehydrogenase PAN1B-like) (Short-chain dehydrogenase/reductase 9) 304 33,458 Active site (1); Alternative sequence (1); Binding site (2); Chain (1); Modified residue (2); Nucleotide binding (1); Sequence conflict (2); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q61488 DHH_MOUSE Desert hedgehog protein (DHH) (HHG-3) [Cleaved into: Desert hedgehog protein N-product; Desert hedgehog protein C-product] 396 43,542 Chain (3); Lipidation (2); Metal binding (12); Signal peptide (1); Site (4) FUNCTION: Intercellular signal essential for a variety of patterning events during development. May function as a spermatocyte survival factor in the testes. Essential for testes development. PTM: The C-terminal domain displays an autoproteolysis activity and a cholesterol transferase activity. Both activities result in the cleavage of the full-length protein and covalent attachment of a cholesterol moiety to the C-terminal of the newly generated N-terminal fragment (N-product). This covalent modification appears to play an essential role in restricting the spatial distribution of the protein activity to the cell surface. The N-product is the active species in both local and long-range signaling, whereas the C-product has no signaling activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Desert hedgehog protein N-product: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Extracellular side {ECO:0000250}. Note=The N-terminal peptide remains associated with the cell surface. {ECO:0000250}.; SUBCELLULAR LOCATION: Desert hedgehog protein C-product: Secreted, extracellular space {ECO:0000250}. Note=The C-terminal peptide diffuses from the cell. {ECO:0000250}. SUBUNIT: Interacts with BOC and CDON. Interacts with HHIP (By similarity). {ECO:0000250}. DOMAIN: The desert hedgehog protein N-product binds calcium and zinc ions; this stabilizes the protein fold and is essential for protein-protein interactions mediated by this domain. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in adult testes. Not expressed in limb buds. +O88876 DHRS3_MOUSE Short-chain dehydrogenase/reductase 3 (EC 1.1.1.300) (Retinal short-chain dehydrogenase/reductase 1) (retSDR1) 302 33,652 Active site (1); Alternative sequence (2); Binding site (1); Chain (1); Sequence conflict (3); Transmembrane (4) TRANSMEM 9 29 Helical. {ECO:0000255}.; TRANSMEM 170 190 Helical. {ECO:0000255}.; TRANSMEM 195 215 Helical. {ECO:0000255}.; TRANSMEM 258 278 Helical. {ECO:0000255}. FUNCTION: Catalyzes the reduction of all-trans-retinal to all-trans-retinol in the presence of NADPH. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: In the embryo, expressed in developing osteogenic and chondrogenic tissues of vertebra, rib, tooth and limb bud. {ECO:0000269|PubMed:9853961}. +Q8R418 DICER_MOUSE Endoribonuclease Dicer (EC 3.1.26.3) (Double-strand-specific ribonuclease mDCR-1) 1916 216,821 Alternative sequence (1); Beta strand (3); Chain (1); Domain (7); Erroneous initiation (2); Frameshift (1); Helix (12); Metal binding (6); Modified residue (8); Motif (1); Mutagenesis (1); Nucleotide binding (1); Region (1); Sequence conflict (16); Site (1); Turn (3) FUNCTION: Double-stranded RNA (dsRNA) endoribonuclease playing a central role in short dsRNA-mediated post-transcriptional gene silencing. Cleaves naturally occurring long dsRNAs and short hairpin pre-microRNAs (miRNA) into fragments of twenty-one to twenty-three nucleotides with 3' overhang of two nucleotides, producing respectively short interfering RNAs (siRNA) and mature microRNAs. SiRNAs and miRNAs serve as guide to direct the RNA-induced silencing complex (RISC) to complementary RNAs to degrade them or prevent their translation. Gene silencing mediated by siRNAs, also called RNA interference, controls the elimination of transcripts from mobile and repetitive DNA elements of the genome but also the degradation of exogenous RNA of viral origin for instance. The miRNA pathway on the other side is a mean to specifically regulate the expression of target genes (By similarity). {ECO:0000250|UniProtKB:Q9UPY3}.; FUNCTION: Isoform 2: More active than isoform 1 to process long double-stranded RNA into siRNAs. Responsible for the accumulation of endogenous siRNAs observed in mouse oocytes compared to somatic cells and it regulates meiotic spindle organization in female germline. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UPY3}. SUBUNIT: Component of the RISC loading complex (RLC), or micro-RNA (miRNA) loading complex (miRLC), which is composed of DICER1, AGO2 and TARBP2; DICER1 and TARBP2 are required to process precursor miRNAs (pre-miRNAs) to mature miRNAs and then load them onto AGO2. Note that the trimeric RLC/miRLC is also referred to as RISC. Interacts with DHX9, AGO1, PIWIL1 and PRKRA. Interacts with AGO2, TARBP2, EIF6, MOV10 and RPL7A (60S ribosome subunit); they form a large RNA-induced silencing complex (RISC). Interacts with BCDIN3D (By similarity). {ECO:0000250|UniProtKB:Q9UPY3}. TISSUE SPECIFICITY: Isoform 1 is expressed in a wide variety of tissues. Isoform 2 is specifically expressed in oocytes during their growth (at protein level). +O35286 DHX15_MOUSE Pre-mRNA-splicing factor ATP-dependent RNA helicase DHX15 (EC 3.6.4.13) (DEAH box protein 15) 795 91,007 Chain (1); Compositional bias (3); Cross-link (1); Domain (2); Frameshift (1); Modified residue (2); Motif (1); Nucleotide binding (1); Sequence conflict (4) FUNCTION: Pre-mRNA processing factor involved in disassembly of spliceosomes after the release of mature mRNA. In cooperation with TFIP11 seem to be involved in the transition of the U2, U5 and U6 snRNP-containing IL complex to the snRNP-free IS complex leading to efficient debranching and turnover of excised introns (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9342318}. Nucleus, nucleolus {ECO:0000269|PubMed:9342318}. SUBUNIT: Interacts with SSB/La. Component of the U11/U12 snRNPs that are part of the U12-type spliceosome. Identified in the Intron Large (IL) complex, a post-mRNA release spliceosomal complex containing the excised intron, U2, U5 and U6 snRNPs, and splicing factors; the association may be transient. Interacts with TFIP11; indicative for a recruitment to the IL complex. Interacts with GPATCH2. {ECO:0000250|UniProtKB:O43143}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9342318}. +Q9Z207 DIAP3_MOUSE Protein diaphanous homolog 3 (Diaphanous-related formin-3) (DRF3) (p134mDIA2) (mDIA2) 1171 133,686 Chain (1); Coiled coil (4); Compositional bias (1); Domain (4); Modified residue (6); Motif (2); Mutagenesis (10) FUNCTION: Actin nucleation and elongation factor required for the assembly of F-actin structures, such as actin cables and stress fibers (PubMed:10678165, PubMed:23558171). Required for cytokinesis, stress fiber formation and transcriptional activation of the serum response factor (PubMed:10678165, PubMed:23558171). Binds to GTP-bound form of Rho and to profilin: acts in a Rho-dependent manner to recruit profilin to the membrane, where it promotes actin polymerization (PubMed:10678165). DFR proteins couple Rho and Src tyrosine kinase during signaling and the regulation of actin dynamics (PubMed:10678165). Also acts as an actin nucleation and elongation factor in the nucleus by promoting nuclear actin polymerization inside the nucleus to drive serum-dependent SRF-MRTFA activity (PubMed:23558171). {ECO:0000269|PubMed:10678165, ECO:0000269|PubMed:23558171}. PTM: Ubiquitinated. {ECO:0000269|PubMed:19457867}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19117945, ECO:0000269|PubMed:23558171}. Nucleus {ECO:0000269|PubMed:19117945, ECO:0000269|PubMed:23558171}. Note=During mitosis, co-localizes with the actin-rich cleavage furrow and with the microtubule-rich central spindle during cytokinesis (By similarity). Shuttles between the cytoplasm and the nucleus (PubMed:19117945). {ECO:0000250|UniProtKB:Q9NSV4, ECO:0000269|PubMed:19117945}. DOMAIN: The DAD domain regulates activation via by an autoinhibitory interaction with the GBD/FH3 domain (PubMed:23558171). This autoinhibition is released upon competitive binding of an activated GTPase (PubMed:23558171). The release of DAD allows the FH2 domain to then nucleate and elongate nonbranched actin filaments (PubMed:23558171). {ECO:0000269|PubMed:23558171}. +Q8BQT2 DIK1C_MOUSE Divergent protein kinase domain 1C (Protein FAM69C) 410 45,976 Alternative sequence (1); Chain (1); Erroneous initiation (2); Motif (1); Topological domain (2); Transmembrane (1) TRANSMEM 20 40 Helical. {ECO:0000255}. TOPO_DOM 1 19 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 41 410 Lumenal. {ECO:0000255}. PTM: Among the many cysteines in the lumenal domain, most are probably involved in disulfide bonds. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21334309}; Single-pass type II membrane protein {ECO:0000269|PubMed:21334309}. TISSUE SPECIFICITY: Mainly expressed in the brain and eye, some expression in kidney and skeletal muscle. {ECO:0000269|PubMed:21334309}. +E9Q8D0 DJC21_MOUSE DnaJ homolog subfamily C member 21 531 61,735 Chain (1); Domain (1); Modified residue (4); Zinc finger (2) FUNCTION: May act as a co-chaperone for HSP70. May play a role in ribosomal RNA (rRNA) biogenesis, possibly in the maturation of the 60S subunit. Binds the precursor 45S rRNA. {ECO:0000250|UniProtKB:Q5F1R6}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q5F1R6}. Nucleus {ECO:0000250|UniProtKB:Q5F1R6}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q5F1R6}. Note=Within the nucleus, localizes primarily to the nucleolus. {ECO:0000250|UniProtKB:Q5F1R6}. SUBUNIT: Interacts with HSPA8, PA2G4 and ZNF622. {ECO:0000250|UniProtKB:Q5F1R6}. +Q99KV1 DJB11_MOUSE DnaJ homolog subfamily B member 11 (APOBEC1-binding protein 2) (ABBP-2) (ER-associated DNAJ) (ER-associated Hsp40 co-chaperone) (Endoplasmic reticulum DNA J domain-containing protein 3) (ER-resident protein ERdj3) (ERdj3) (ERj3p) 358 40,555 Chain (1); Domain (1); Glycosylation (1); Modified residue (1); Sequence conflict (5); Signal peptide (1) FUNCTION: As a co-chaperone for HSPA5 it is required for proper folding, trafficking or degradation of proteins. Binds directly to both unfolded proteins that are substrates for ERAD and nascent unfolded peptide chains, but dissociates from the HSPA5-unfolded protein complex before folding is completed. May help recruiting HSPA5 and other chaperones to the substrate. Stimulates HSPA5 ATPase activity. It is necessary for maturation and correct trafficking of PKD1. {ECO:0000250|UniProtKB:Q9UBS4}. PTM: Contains high-mannose Endo H-sensitive carbohydrates. {ECO:0000250}.; PTM: Cys-169, Cys-171, Cys-193 and Cys-196 form intramolecular disulfide bonds. The preferential partner for each Cys is not known (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000269|PubMed:15525676}. SUBUNIT: Part of a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX. Binds to denatured substrates in an ATP-independent manner. Interacts via the J domain with HSPA5 in an ATP-dependent manner (By similarity). {ECO:0000250}. +Q80Y83 DIXC1_MOUSE Dixin (Coiled-coil protein DIX1) (Coiled-coil-DIX1) (DIX domain-containing protein 1) 711 80,215 Alternative sequence (14); Beta strand (5); Chain (1); Coiled coil (1); Domain (2); Helix (1); Lipidation (1); Modified residue (5); Region (1); Sequence conflict (2); Turn (2) FUNCTION: Positive effector of the Wnt signaling pathway; activates WNT3A signaling via DVL2. Regulates JNK activation by AXIN1 and DVL2. {ECO:0000269|PubMed:15262978, ECO:0000269|PubMed:15857680}. PTM: Phosphorylated on tyrosine and serine residues. {ECO:0000250}.; PTM: Polyubiquitinated, leading to its proteasomal degradation. WNT3A signaling increases DIXDC1 protein levels by inhibiting its ubiquitination and subsequent degradation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q155Q3}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:Q155Q3}. Cytoplasm {ECO:0000250|UniProtKB:Q155Q3}. Note=Colocalizes with gamma-tubulin at the centrosome, both during interphase and mitosis. Associated with actin stress fiber at the filament ends. {ECO:0000250|UniProtKB:Q155Q3}. SUBUNIT: May bind filamentous actin. Directly interacts (via DIX domain) with DVL2 (via DIX domain). Interacts with gamma-tubulin (By similarity). Interacts with the complex composed of DVL2 and Rac. Interacts with AXIN1; competes with MAP3K1. Interacts with MAP3K4 preventing MAP3K4 interaction with AXIN1. {ECO:0000250, ECO:0000269|PubMed:15262978}. DOMAIN: The coiled-coil domain mediates interaction with MAP3K4 and inhibition of AXIN1-mediated JNK activation through MAP3K4. {ECO:0000250}.; DOMAIN: The DIX domain mediates interaction with AXIN1 and inhibition of AXIN1-mediated JNK activation through MAP3K1. Mediates interaction with DVL2; this interaction is required for activation of Wnt signaling (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Abundantly expressed in brain and testis and to a lower extent in lung, kidney, colon, ovary and urinary bladder. Expressed in brain, liver, testis and spleen (at protein level). Expressed throughout the brain with strong expression in main and accessory olfactory bulbs, cerebral cortex, piriform cortex, hippocampus, habenular nucleus, dorsal thalamus, superior and inferior colliculi and cerebellum. {ECO:0000269|PubMed:15857680}. +Q149L6 DJB14_MOUSE DnaJ homolog subfamily B member 14 379 42,326 Alternative sequence (3); Chain (1); Domain (1); Topological domain (2); Transmembrane (1) TRANSMEM 245 265 Helical. {ECO:0000255}. TOPO_DOM 1 244 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 266 379 Lumenal. {ECO:0000255}. FUNCTION: Acts as a co-chaperone with HSPA8/Hsc70; required to promote protein folding and trafficking, prevent aggregation of client proteins, and promote unfolded proteins to endoplasmic reticulum-associated degradation (ERAD) pathway. Acts by determining HSPA8/Hsc70's ATPase and polypeptide-binding activities. Can also act independently of HSPA8/Hsc70: together with DNAJB12, acts as a chaperone that promotes maturation of potassium channels KCND2 and KCNH2 by stabilizing nascent channel subunits and assembling them into tetramers. While stabilization of nascent channel proteins is dependent on HSPA8/Hsc70, the process of oligomerization of channel subunits is independent of HSPA8/Hsc70. When overexpressed, forms membranous structures together with DNAJB12 and HSPA8/Hsc70 within the nucleus; the role of these structures, named DJANGOs, is still unclear. {ECO:0000250|UniProtKB:Q8TBM8}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8TBM8}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:Q8TBM8}; Single-pass membrane protein {ECO:0000255}. Note=Localizes to the endoplasmic reticulum membrane. When overexpressed, forms membranous structures in the nucleus. {ECO:0000250|UniProtKB:Q8TBM8}. SUBUNIT: Interacts (via J domain) with HSPA8/Hsc70. Forms a multiprotein complex, at least composed of DNAJB12, DNAJB14, HSPA8/Hsc70 and SGTA; interaction with DNAJB14 and HSPA8/Hsc70 is direct. {ECO:0000250|UniProtKB:Q8TBM8}. +Q8BFQ6 DIRC2_MOUSE Solute carrier family 49 member 4 (Disrupted in renal carcinoma protein 2 homolog) 478 51,909 Chain (1); Glycosylation (1); Motif (1); Topological domain (13); Transmembrane (12) TRANSMEM 52 72 Helical. {ECO:0000255}.; TRANSMEM 90 110 Helical. {ECO:0000255}.; TRANSMEM 118 138 Helical. {ECO:0000255}.; TRANSMEM 153 173 Helical. {ECO:0000255}.; TRANSMEM 185 205 Helical. {ECO:0000255}.; TRANSMEM 230 250 Helical. {ECO:0000255}.; TRANSMEM 282 302 Helical. {ECO:0000255}.; TRANSMEM 315 335 Helical. {ECO:0000255}.; TRANSMEM 348 368 Helical. {ECO:0000255}.; TRANSMEM 385 405 Helical. {ECO:0000255}.; TRANSMEM 415 435 Helical. {ECO:0000255}.; TRANSMEM 443 463 Helical. {ECO:0000255}. TOPO_DOM 1 51 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 73 89 Lumenal. {ECO:0000255}.; TOPO_DOM 111 117 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 139 152 Lumenal. {ECO:0000255}.; TOPO_DOM 174 184 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 206 229 Lumenal. {ECO:0000255}.; TOPO_DOM 251 281 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 303 314 Lumenal. {ECO:0000255}.; TOPO_DOM 336 347 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 369 384 Lumenal. {ECO:0000255}.; TOPO_DOM 406 414 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 436 442 Lumenal. {ECO:0000255}.; TOPO_DOM 464 478 Cytoplasmic. {ECO:0000255}. FUNCTION: Electrogenic metabolite transporter. {ECO:0000250}. PTM: Cleaved in lysosomes by cathepsin L between Leu-214 and Ala-261, generating a N-glycosylated N-terminal and a non-glycosylated C-terminal fragment. {ECO:0000250}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +O88516 DLL3_MOUSE Delta-like protein 3 (Drosophila Delta homolog 3) (Delta3) (M-Delta-3) 592 62,069 Alternative sequence (1); Chain (1); Disulfide bond (18); Domain (7); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 491 511 Helical. {ECO:0000255}. TOPO_DOM 33 490 Extracellular. {ECO:0000255}.; TOPO_DOM 512 592 Cytoplasmic. {ECO:0000255}. FUNCTION: Inhibits primary neurogenesis. May be required to divert neurons along a specific differentiation pathway. Plays a role in the formation of somite boundaries during segmentation of the paraxial mesoderm. PTM: Ubiquitinated by MIB (MIB1 or MIB2), leading to its endocytosis and subsequent degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Can bind and activate Notch-1 or another Notch receptor. {ECO:0000305}. DOMAIN: The DSL domain is required for binding to the Notch receptor. TISSUE SPECIFICITY: Predominantly expressed in the neuroectoderm and paraxial mesoderm during embryogenesis. DISEASE: Note=A truncating mutation in Dll3 is the cause of the pudgy (pu) phenotype. Pudgy mice exhibit patterning defects at the earliest stages of somitogenesis. Adult pudgy mice present severe vertebral and rib deformities. {ECO:0000269|PubMed:9662403}. +Q8BZE1 DMBTL_MOUSE Putative DMBT1-like protein 841 90,689 Chain (1); Compositional bias (1); Disulfide bond (14); Domain (6); Glycosylation (1); Sequence conflict (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +Q91ZK4 DMBX1_MOUSE Diencephalon/mesencephalon homeobox protein 1 (Diencephalon/mesencephalon-expressed brain homeobox gene 1 protein) (Orthodenticle homolog 3) (Paired-like homeobox protein DMBX1) (Paired-type homeobox Atx) 381 41,115 Alternative sequence (1); Chain (1); DNA binding (1); Erroneous initiation (1); Motif (1); Region (1); Sequence conflict (2) FUNCTION: Functions as a transcriptional repressor. May repress OTX2-mediated transactivation by forming a heterodimer with OTX2 on the P3C (5'-TAATCCGATTA-3') sequence. Required for brain development, neonatal survival, postnatal growth, and nursing ability. {ECO:0000269|PubMed:11914943, ECO:0000269|PubMed:12055180, ECO:0000269|PubMed:15314164, ECO:0000269|PubMed:15890343}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O35137, ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-ProRule:PRU00138}. SUBUNIT: Homodimer or heterodimer. Forms heterodimers with OTX2. {ECO:0000269|PubMed:15890343}. TISSUE SPECIFICITY: Expressed in adult brain, stomach, and testis. Expressed in the developing diencephalon, midbrain and hindbrain. During limb development, expressed in a temporal pattern with expression being first restricted to the forelimbs and then subsequently to the hindlimbs. {ECO:0000269|PubMed:11744391, ECO:0000269|PubMed:11914943, ECO:0000269|PubMed:12111214, ECO:0000269|PubMed:12175514}. +P70436 DLX4_MOUSE Homeobox protein DLX-4 (Homeobox protein DLX-7) 240 26,579 Chain (1); DNA binding (1); Sequence conflict (2) FUNCTION: May play a role in determining the production of hemoglobin S. May act as a repressor. During embryonic development, plays a role in palatogenesis. {ECO:0000250|UniProtKB:Q92988}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92988}. TISSUE SPECIFICITY: Branchial arches, molar and incisor teeth and limbs. +Q33DR3 DLP1_MOUSE Decaprenyl-diphosphate synthase subunit 2 (EC 2.5.1.91) (All-trans-decaprenyl-diphosphate synthase subunit 2) (Decaprenyl pyrophosphate synthase subunit 2) (Solanesyl-diphosphate synthase subunit 2) 401 43,980 Alternative sequence (4); Chain (1); Sequence conflict (2) Cofactor biosynthesis; ubiquinone biosynthesis. FUNCTION: Supplies decaprenyl diphosphate, the precursor for the side chain of the isoprenoid quinones ubiquinone-10. {ECO:0000269|PubMed:16262699}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}. SUBUNIT: Heterotetramer of 2 DPS1/TPRT and 2 DLP1 subunits. {ECO:0000269|PubMed:16262699}. +P70397 DLX6_MOUSE Homeobox protein DLX-6 175 19,677 Alternative sequence (1); Chain (1); DNA binding (1) SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. +Q6PFD5 DLGP3_MOUSE Disks large-associated protein 3 (DAP-3) (PSD-95/SAP90-binding protein 3) (SAP90/PSD-95-associated protein 3) (SAPAP3) 977 105,873 Beta strand (1); Chain (1); Compositional bias (1); Modified residue (10); Sequence conflict (1) FUNCTION: May play a role in the molecular organization of synapses and neuronal cell signaling. Could be an adapter protein linking ion channel to the subsynaptic cytoskeleton. May induce enrichment of PSD-95/SAP90 at the plasma membrane. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15024750}; Peripheral membrane protein {ECO:0000269|PubMed:15024750}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000269|PubMed:15024750}. Cell junction, synapse {ECO:0000269|PubMed:15024750}. Note=Postsynaptic density of neuronal cells. SUBUNIT: Interacts with DLG4/PSD-95. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in central and peripherical nervous system (at protein level). {ECO:0000269|PubMed:15024750}. +Q8BZ98 DYN3_MOUSE Dynamin-3 (EC 3.6.5.5) 863 97,190 Alternative sequence (1); Chain (1); Domain (3); Modified residue (7); Nucleotide binding (3); Region (5); Sequence conflict (2) FUNCTION: Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP. Most probably involved in vesicular trafficking processes, in particular endocytosis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Microtubule-associated. {ECO:0000250}. +P0C6F1 DYH2_MOUSE Dynein heavy chain 2, axonemal (Axonemal beta dynein heavy chain 2) (Ciliary dynein heavy chain 2) 4456 511,565 Chain (1); Coiled coil (4); Erroneous initiation (1); Nucleotide binding (4); Region (8); Repeat (5); Sequence conflict (8) FUNCTION: Force generating protein of respiratory cilia. Produces force towards the minus ends of microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Involved in sperm motility; implicated in sperm flagellar assembly (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000305}. SUBUNIT: Consists of at least two heavy chains and a number of intermediate and light chains. DOMAIN: Dynein heavy chains probably consist of an N-terminal stem (which binds cargo and interacts with other dynein components), and the head or motor domain. The motor contains six tandemly-linked AAA domains in the head, which form a ring. A stalk-like structure (formed by two of the coiled coil domains) protrudes between AAA 4 and AAA 5 and terminates in a microtubule-binding site. A seventh domain may also contribute to this ring; it is not clear whether the N-terminus or the C-terminus forms this extra domain. There are four well-conserved and two non-conserved ATPase sites, one per AAA domain. Probably only one of these (within AAA 1) actually hydrolyzes ATP, the others may serve a regulatory function (By similarity). {ECO:0000250}. +P63168 DYL1_MOUSE Dynein light chain 1, cytoplasmic (8 kDa dynein light chain) (DLC8) (Dynein light chain LC8-type 1) (Protein inhibitor of neuronal nitric oxide synthase) (PIN) (mPIN) 89 10,366 Chain (1); Cross-link (1); Modified residue (2); Region (1) FUNCTION: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in changing or maintaining the spatial distribution of cytoskeletal structures (By similarity). {ECO:0000250}.; FUNCTION: Binds and inhibits the catalytic activity of neuronal nitric oxide synthase. {ECO:0000250}.; FUNCTION: Promotes transactivation functions of ESR1 and plays a role in the nuclear localization of ESR1. {ECO:0000250}.; FUNCTION: Regulates apoptotic activities of BCL2L11 by sequestering it to microtubules. Upon apoptotic stimuli the BCL2L11-DYNLL1 complex dissociates from cytoplasmic dynein and translocates to mitochondria and sequesters BCL2 thus neutralizing its antiapoptotic activity (By similarity). {ECO:0000250}. PTM: Phosphorylation at Ser-88 appears to control the dimer-monomer transition. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Nucleus {ECO:0000250}. Mitochondrion {ECO:0000250}. SUBUNIT: Homodimer. Monomer; the monomeric form is incapable of binding to target proteins. The cytoplasmic dynein 1 complex consists of two catalytic heavy chains (HCs) and a number of non-catalytic subunits presented by intermediate chains (ICs), light intermediate chains (LICs) and light chains (LCs); the composition seems to vary in respect to the IC, LIC and LC composition. The heavy chain homodimer serves as a scaffold for the probable homodimeric assembly of the respective non-catalytic subunits. The ICs and LICs bind directly to the HC dimer and the LCs assemble on the IC dimer. Interacts with TXNDC17. Interacts with WWC1 and ESR1. The interaction with WWC1 is mandatory for the recruitment and transactivation functions of ESR1 or DYNLL1 to the target chromatin. Interacts with BCL2; the interaction is greatly enhanced in the nucleus and in mitochondria upon induction of apoptosis. Interacts with PAK1; the interaction requires dimeric DYNLL1. Interacts with MYZAP. Part of an astrin (SPAG5)-kinastrin (SKAP) complex containing KNSTRN, SPAG5, PLK1, DYNLL1 and SGO2. Interacts with ATMIN; this interaction inhibits ATMIN transcriptional activity and hence may play a role in a feedback loop whereby DYNLL1 inhibits transactivation of its own promoter by ATMIN. Interacts with NEK9 (not phosphorylated at 'Ser-944') (By similarity). Interacts with BCL2L11 (PubMed:21478148). Interacts with BICD2 (PubMed:22956769). Interacts with BCAS1 (By similarity). {ECO:0000250|UniProtKB:P63167, ECO:0000250|UniProtKB:P63170, ECO:0000269|PubMed:21478148, ECO:0000269|PubMed:22956769}. +Q8VHE6 DYH5_MOUSE Dynein heavy chain 5, axonemal (Axonemal beta dynein heavy chain 5) (mDNAH5) (Ciliary dynein heavy chain 5) 4621 527,558 Chain (1); Coiled coil (8); Nucleotide binding (2); Region (8); Sequence conflict (3) FUNCTION: Force generating protein of respiratory cilia. Produces force towards the minus ends of microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Required for structural and functional integrity of the cilia of ependymal cells lining the brain ventricles. {ECO:0000269|PubMed:15269178}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme. SUBUNIT: Interacts with DNAL1 (By similarity). Consists of at least two heavy chains and a number of intermediate and light chains. {ECO:0000250|UniProtKB:M0R8U1}. DOMAIN: Dynein heavy chains probably consist of an N-terminal stem (which binds cargo and interacts with other dynein components), and the head or motor domain. The motor contains six tandemly-linked AAA domains in the head, which form a ring. A stalk-like structure (formed by two of the coiled coil domains) protrudes between AAA 4 and AAA 5 and terminates in a microtubule-binding site. A seventh domain may also contribute to this ring; it is not clear whether the N-terminus or the C-terminus forms this extra domain. There are four well-conserved and two non-conserved ATPase sites, one per AAA domain. Probably only one of these (within AAA 1) actually hydrolyzes ATP, the others may serve a regulatory function. TISSUE SPECIFICITY: Strongly expressed in lung and kidney and weaker expression seen in brain, heart and testis. In the brain, expressed in ependymal cells lining the brain ventricles and the aqueduct. {ECO:0000269|PubMed:11788826, ECO:0000269|PubMed:15269178}. DISEASE: Note=Defects in Dnah5 are the cause of primary ciliary dyskinesia (PCD). PCD is characterized by recurrent respiratory infections, situs inversus and ciliary immotility and hydrocephalus. {ECO:0000269|PubMed:11912187}. +Q920S3 GATD1_MOUSE GATA zinc finger domain-containing protein 1 (Ocular development-associated gene protein) 266 28,535 Alternative sequence (2); Chain (1); Compositional bias (1); Cross-link (1); Erroneous termination (1); Sequence conflict (2); Zinc finger (1) FUNCTION: Component of some chromatin complex recruited to chromatin sites methylated 'Lys-4' of histone H3 (H3K4me). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of a chromatin complex, at least composed of KDM5A, GATAD1 and EMSY. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the eye (lens, ciliary body, retina, sclera and conjunctiva) at postnatal day 2 and 10. Not detected anywhere at postnatal day 14. {ECO:0000269|PubMed:12062807}. +Q9D0M5 DYL2_MOUSE Dynein light chain 2, cytoplasmic (8 kDa dynein light chain b) (DLC8) (DLC8b) (Dynein light chain LC8-type 2) 89 10,350 Beta strand (5); Chain (1); Helix (2); Site (1) FUNCTION: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in changing or maintaining the spatial distribution of cytoskeletal structures (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:14561217}. SUBUNIT: Homodimer (By similarity). The cytoplasmic dynein 1 complex consists of two catalytic heavy chains (HCs) and a number of non-catalytic subunits which present intermediate chains (ICs), light intermediate chains (LICs) and light chains (LCs); the composition seems to vary in respect to the IC, LIC and LC composition. The heavy chain homodimer serves as a scaffold for the probable homodimeric assembly of the respective non-catalytic subunits. Dynein ICs and LICs bind directly to the HC dimer and the LCs assemble on the IC dimer (PubMed:11546872). Interacts with DYNC1I1 (PubMed:11148209). Interacts with BMF (PubMed:11546872). Component of the myosin V motor complex (PubMed:11546872). Interacts with BCAS1 (By similarity). {ECO:0000250|UniProtKB:Q78P75, ECO:0000269|PubMed:11148209, ECO:0000269|PubMed:11546872}. +Q9JHU4 DYHC1_MOUSE Cytoplasmic dynein 1 heavy chain 1 (Cytoplasmic dynein heavy chain 1) (Dynein heavy chain, cytosolic) 4644 532,045 Chain (1); Coiled coil (10); Helix (11); Initiator methionine (1); Modified residue (9); Natural variant (2); Nucleotide binding (4); Region (10); Sequence conflict (5); Turn (2) FUNCTION: Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Plays a role in mitotic spindle assembly and metaphase plate congression. {ECO:0000250|UniProtKB:Q14204}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SUBUNIT: Homodimer. The cytoplasmic dynein 1 complex consists of two catalytic heavy chains (HCs) and a number of non-catalytic subunits presented by intermediate chains (ICs), light intermediate chains (LICs) and light chains (LCs); the composition seems to vary in respect to the IC, LIC and LC composition. The heavy chain homodimer serves as a scaffold for the probable homodimeric assembly of the respective non-catalytic subunits. The ICs and LICs bind directly to the HC dimer and dynein LCs assemble on the IC dimer. Interacts with DYNC1LI1; DYNC1LI1 and DYNC1LI2 bind mutually exclusive to DYNC1H1. Interacts with DYNC1LI2; DYNC1LI1 and DYNC1LI2 bind mutually exclusive to DYNC1H1. Interacts with DYNC1I2 (By similarity). Interacts with BICD2 (PubMed:22956769). {ECO:0000250|UniProtKB:P38650, ECO:0000269|PubMed:22956769}. DOMAIN: Dynein heavy chains probably consist of an N-terminal stem (which binds cargo and interacts with other dynein components), and the head or motor domain. The motor contains six tandemly-linked AAA domains in the head, which form a ring. A stalk-like structure (formed by two of the coiled coil domains) protrudes between AAA 4 and AAA 5 and terminates in a microtubule-binding site. A seventh domain may also contribute to this ring; it is not clear whether the N-terminus or the C-terminus forms this extra domain. There are four well-conserved and two non-conserved ATPase sites, one per AAA domain. Probably only one of these (within AAA 1) actually hydrolyzes ATP, the others may serve a regulatory function. DISEASE: Note=Defects in Dync1h1 are the cause of the 'Legs at odd angles' (LOA) phenotype, an autosomal dominant trait where affected animals display unusual twisting of the body and clenching of the hindlimbs when suspended by the tail. Heterozygotes suffer age-related progressive loss of muscle tone and locomotor ability without major reduction in life-span while homozygotes show a more severe phenotype with an inability to move or feed, and die within 24 hours of birth. LOA mutants display defects in migration of facial motor neuron cell bodies and impaired retrograde transport in spinal cord motor neurons. {ECO:0000269|PubMed:12730604}.; DISEASE: Note=Defects in Dync1h1 are the cause of the Cramping 1 (Cra1) phenotype, an autosomal dominant trait where affected animals display unusual twisting of the body and clenching of the hindlimbs when suspended by the tail. Heterozygotes suffer age-related progressive loss of muscle tone and locomotor ability without major reduction in life-span while homozygotes show a more severe phenotype with an inability to move or feed, and die within 24 hours of birth. {ECO:0000269|PubMed:12730604}. +P51807 DYLT1_MOUSE Dynein light chain Tctex-type 1 (Activator of G-protein signaling 2) (AGS2) (T-complex testis-specific protein 1) (TCTEX-1) 113 12,483 Beta strand (4); Chain (1); Helix (3); Modified residue (1); Natural variant (1); Region (1); Turn (1) FUNCTION: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Binds to transport cargos and is involved in apical cargo transport such as rhodopsin-bearing vesicles in polarized epithelia (By similarity). May also be a accessory component of axonemal dynein. Plays an important role in male germ cell development and function. Candidate for involvement in male sterility. {ECO:0000250, ECO:0000269|PubMed:9490726}.; FUNCTION: Plays a role in neuronal morphogenesis; the function is independent of cytoplasmic dynein and seems to be coupled to regulation of the actin cytoskeleton by enhancing Rac1 activity. The function in neurogenesis may be regulated by association with a G-protein beta-gamma dimer. May function as a receptor-independent activator of heterotrimeric G-protein signaling; the activation appears to be independent of a nucleotide exchange. Plays a role in regulating neurogenesis; inhibits the genesis of neurons from precursor cells during cortical development presumably by antagonizing ARHGEF2. Unrelated to the role in retrograde microtubule-associated movement may play a role in the dimerization of cytoplasmic proteins/domains such as for ACVR2B. Binds to the cytoplasmic domain of ACVR2B and, in vitro, inhibits ACVR2B signaling. Involved in the regulation of mitotic spindle orientation. {ECO:0000269|PubMed:10559191, ECO:0000269|PubMed:19448628}. PTM: Phosphorylated by BMPR2. The phosphorylation status is proposed to regulate the association with the cytoplasmic dynein complex and may have role in cytoplasmic dynein cargo release (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Localizes to mitotic spindles. {ECO:0000250}. SUBUNIT: Homodimer (Probable). The cytoplasmic dynein 1 complex consists of two catalytic heavy chains (HCs) and a number of non-catalytic subunits presented by intermediate chains (ICs), light intermediate chains (LICs) and light chains (LCs); the composition seems to vary in respect to the IC, LIC and LC composition. The heavy chain homodimer serves as a scaffold for the probable homodimeric assembly of the respective non-catalytic subunits. The ICs and LICs bind directly to the HC dimer and the LCs assemble on the IC dimer. DYNLT1 and DYNLT3 compete for association with dynein IC (DYNC1I1 or DYNC1I2). Self-associates. Interacts with RHO (By similarity). Interacts with DYNC1I1 and DYNC1I2. Interacts with DOC2A, DOC2B and SCN10A. Interacts with PVR. Interacts with SVIL isoform 2. Interacts with GNB1; the interaction occurs in presence of guanine nucleotide-binding protein G(T) subunit gamma; the interaction diminishes the association of DYNLT1 with dynein IC (DYNC1I1 or DYNC1I2). Interacts with GNB2, GNB3 and GNB5; the interactions occur in presence of guanine nucleotide-binding protein G(T) subunit gamma. Interacts with ACVR2B and ARHGEF2 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P63172, ECO:0000269|PubMed:27502274, ECO:0000305}. TISSUE SPECIFICITY: High level in testis (germ cell-specific). Expressed in sperm (at protein level). 200-fold lower in liver, brain, heart, spleen, and kidney. Levels in thymus and two embryonal carcinoma cell lines were several-fold higher than this low constitutive level. {ECO:0000269|PubMed:9490726}. +Q8CHY3 DYM_MOUSE Dymeclin 669 75,848 Alternative sequence (2); Chain (1); Erroneous initiation (2); Erroneous termination (1); Initiator methionine (1); Lipidation (1); Sequence conflict (2) FUNCTION: Necessary for correct organization of Golgi apparatus. Involved in bone development. {ECO:0000250}. PTM: Myristoylated in vitro; myristoylation is not essential for protein targeting to Golgi compartment. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus {ECO:0000250}. Membrane {ECO:0000250|UniProtKB:Q7RTS9}; Lipid-anchor {ECO:0000250|UniProtKB:Q7RTS9}. Note=Sequence analysis programs predict 1 transmembrane region. However, it has been shown in human that it is not a stably anchored transmembrane protein but it weakly associates with the Golgi apparatus and shuttles between the Golgi and the cytosol (By similarity). {ECO:0000250}. SUBUNIT: Interacts with GOLM1 and PPIB. {ECO:0000250}. +Q69Z23 DYH17_MOUSE Dynein heavy chain 17, axonemal (Axonemal beta dynein heavy chain 17) (Ciliary dynein heavy chain 17) 4481 511,603 Alternative sequence (2); Chain (1); Coiled coil (3); Nucleotide binding (4); Region (8); Repeat (8) FUNCTION: Force generating protein of respiratory cilia. Produces force towards the minus ends of microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Involved in sperm motility; implicated in sperm flagellar assembly (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000305}. SUBUNIT: Consists of at least two heavy chains and a number of intermediate and light chains. DOMAIN: Dynein heavy chains probably consist of an N-terminal stem (which binds cargo and interacts with other dynein components), and the head or motor domain. The motor contains six tandemly-linked AAA domains in the head, which form a ring. A stalk-like structure (formed by two of the coiled coil domains) protrudes between AAA 4 and AAA 5 and terminates in a microtubule-binding site. A seventh domain may also contribute to this ring; it is not clear whether the N-terminus or the C-terminus forms this extra domain. There are four well-conserved and two non-conserved ATPase sites, one per AAA domain. Probably only one of these (within AAA 1) actually hydrolyzes ATP, the others may serve a regulatory function (By similarity). {ECO:0000250}. +Q69ZF3 GBA2_MOUSE Non-lysosomal glucosylceramidase (NLGase) (EC 3.2.1.45) (Beta-glucocerebrosidase 2) (Beta-glucosidase 2) (Glucosylceramidase 2) 918 103,294 Chain (1); Erroneous initiation (1); Modified residue (1); Sequence conflict (1) FUNCTION: Non-lysosomal glucosylceramidase that catalyzes the conversion of glucosylceramide (GlcCer) to free glucose and ceramide. Involved in sphingomyelin generation and prevention of glycolipid accumulation. May also catalyze the hydrolysis of bile acid 3-O-glucosides, however, the relevance of such activity is unclear in vivo. Plays a role in central nevous system development (By similarity). Required for proper formation of motor neuron axons (By similarity). {ECO:0000250, ECO:0000269|PubMed:17080196}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23250757}; Peripheral membrane protein {ECO:0000269|PubMed:23250757}; Cytoplasmic side {ECO:0000269|PubMed:23250757}. Golgi apparatus membrane {ECO:0000269|PubMed:23250757}; Peripheral membrane protein {ECO:0000269|PubMed:23250757}; Cytoplasmic side {ECO:0000269|PubMed:23250757}. Note=Not localized to lipid rafts. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed at low level. Highly expressed in testis and brain. {ECO:0000269|PubMed:17080196, ECO:0000269|PubMed:23250757}. +P62874 GBB1_MOUSE Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 (Transducin beta chain 1) 340 37,377 Chain (1); Initiator methionine (1); Modified residue (3); Repeat (7) FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction (By similarity). {ECO:0000250}. PTM: Phosphorylation at His-266 by NDKB contributes to G protein activation by increasing the high energetic phosphate transfer onto GDP. {ECO:0000250}. SUBUNIT: G proteins are composed of 3 units, alpha, beta and gamma. Interacts with ARHGEF18 and RASD2. The heterodimer formed by GNB1 and GNG2 interacts with ARHGEF5 (By similarity). {ECO:0000250|UniProtKB:P62873}. +Q61011 GBB3_MOUSE Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-3 (Transducin beta chain 3) 340 37,240 Chain (1); Repeat (7) FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. SUBUNIT: G proteins are composed of 3 units, alpha, beta and gamma. Interacts with RASD2 (By similarity). {ECO:0000250}. +Q78JN3 ECI3_MOUSE Enoyl-CoA delta isomerase 3, peroxisomal (EC 5.3.3.8) (Delta(3),delta(2)-enoyl-CoA isomerase) (D3,D2-enoyl-CoA isomerase) (Dodecenoyl-CoA isomerase) 317 35,231 Chain (1); Domain (1); Motif (1); Region (1); Sequence conflict (2); Site (1) FUNCTION: Catalyzes the isomerization of trans-3-nonenoyl-CoA into trans-2-nonenoyl-CoA (PubMed:24344334). May also have activity towards other enoyl-CoA species (Probable). {ECO:0000269|PubMed:24344334, ECO:0000305}. SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:24344334}. DOMAIN: The ACB (acyl-CoA-binding) domain is truncated and may be non-functional. {ECO:0000305}. TISSUE SPECIFICITY: Expressed at high levels in the kidney. Also detected at very low levels in the duodenum, jejunum, ileum, heart, liver, lung, and brown adipose tissue (at protein level). In the kidney, expression seems to be localized mainly to the proximal tubule. {ECO:0000269|PubMed:24344334}. +Q61508 ECM1_MOUSE Extracellular matrix protein 1 (Secretory component p85) 559 62,832 Alternative sequence (1); Chain (1); Glycosylation (3); Modified residue (1); Region (1); Repeat (2); Sequence conflict (3); Signal peptide (1) FUNCTION: Involved in endochondral bone formation as negative regulator of bone mineralization. Stimulates the proliferation of endothelial cells and promotes angiogenesis. Inhibits MMP9 proteolytic activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SUBUNIT: Interacts (via C-terminus) with HSPG2 (via C-terminus). Interacts with EFEMP1/FBLN3 and LAMB3. Interacts with MMP9. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the connective tissues surronding developing long bones, but not in the cartilage. The long isoform is expressed in a number of tissues including liver, heart and lungs. The short isoform is expressed in skin and cartilage-containing tissues such as tail and front paw. No expression is found in brain. {ECO:0000269|PubMed:11165938}. +Q91X44 GCKR_MOUSE Glucokinase regulatory protein (Glucokinase regulator) 587 64,679 Binding site (2); Chain (1); Domain (2); Region (4) FUNCTION: Inhibits glucokinase (GCK) by forming an inactive complex with this enzyme. The affinity of GCKR for GCK is modulated by fructose metabolites: GCKR with bound fructose 6-phosphate has increased affinity for GCK, while GCKR with bound fructose 1-phosphate has strongly decreased affinity for GCK and does not inhibit GCK activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Under low glucose concentrations, GCK associates with GKRP and the inactive complex is recruited to the hepatocyte nucleus. {ECO:0000250}. SUBUNIT: Interacts (fructose 6-phosphate bound form) with GCK. {ECO:0000250}. DOMAIN: Fructose 1-phosphate and fructose 6-phosphate compete for the same binding site. {ECO:0000250}. +P70348 GCM1_MOUSE Chorion-specific transcription factor GCMa (GCM motif protein 1) (mGCM1) (mGCMa) (Glial cells missing homolog 1) 436 49,589 Beta strand (8); Chain (1); DNA binding (1); Helix (3); Metal binding (8); Mutagenesis (11); Sequence conflict (4) FUNCTION: Transcription factor that is necessary for placental development (PubMed:8962155). Involved in the control of expression of placental growth factor (PGF) and other placenta-specific genes. Binds to the trophoblast-specific element 2 (TSE2) of the aromatase gene enhancer. Binds to the SYDE1 promoter. Has a central role in mediating the differentiation of trophoblast cells along both the villous and extravillous pathways in placental development (By similarity). {ECO:0000250|UniProtKB:Q9NP62, ECO:0000269|PubMed:8962155}. PTM: Polyubiquitinated in the presence of UBE2D2 and FBXW2 (in vitro). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00245}. TISSUE SPECIFICITY: Placenta specific. {ECO:0000269|PubMed:8814290}. +O09102 GCM2_MOUSE Chorion-specific transcription factor GCMb (mGCMb) (GCM motif protein 2) (Glial cells missing homolog 2) 504 56,039 Chain (1); DNA binding (1); Metal binding (8); Region (1); Sequence conflict (10) FUNCTION: Transcription factor that binds specific sequences on gene promoters and activate their transcription. Through the regulation of gene transcription, may play a role in parathyroid gland development. {ECO:0000250|UniProtKB:O75603}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O75603}. DOMAIN: The C-terminal conserved inhibitory domain (CCID) negatively regulates the transcriptional activity of the protein. {ECO:0000250|UniProtKB:O75603}. +E9PVA8 GCN1_MOUSE eIF-2-alpha kinase activator GCN1 (GCN1 eIF-2-alpha kinase activator homolog) (GCN1-like protein 1) (General control of amino-acid synthesis 1-like protein 1) (Translational activator GCN1) 2671 293,021 Chain (1); Coiled coil (1); Initiator methionine (1); Modified residue (4); Repeat (47); Sequence conflict (5) FUNCTION: Acts as a positive activator of the GCN2 protein kinase activity in response to amino acid starvation (PubMed:15937339). Forms a complex with EIF2AK4/GCN2 on translating ribosomes; during this process, GCN1 seems to act as a chaperone to facilitate delivery of uncharged tRNAs that enter the A site of ribosomes to the tRNA-binding domain of EIF2AK4/GCN2, and hence stimulating EIF2AK4/GCN2 kinase activity (By similarity). Participates in the repression of global protein synthesis and in gene-specific mRNA translation activation, such as the transcriptional activator ATF4, by promoting the EIF2AK4/GCN2-mediated phosphorylation of eukaryotic translation initiation factor 2 (eIF-2-alpha/EIF2S1) on 'Ser-52', and hence allowing ATF4-mediated reprogramming of amino acid biosynthetic gene expression to alleviate nutrient depletion (PubMed:24333428). {ECO:0000250|UniProtKB:P33892, ECO:0000269|PubMed:15937339, ECO:0000269|PubMed:24333428}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:23447528}. Note=Associates with ribosomes in undifferentiated neuroblastoma cells and increases after neuronal differentiation (PubMed:23447528). SUBUNIT: Interacts with EIF2AK4/GCN2; this interaction stimulates the EIF2AK4/GCN2 kinase activity and is impaired by IMPACT upon a variety of stress conditions, such as amino acid depletion, UV-C irradiation, proteasome inhibitor treatment and glucose deprivation (PubMed:24333428). Interacts with IMPACT; this prevents the interaction of GCN1 with EIF2AK4/GCN2 and inhibits EIF2AK4/GCN2 kinase activity (PubMed:15937339, PubMed:22404850). {ECO:0000269|PubMed:15937339, ECO:0000269|PubMed:22404850, ECO:0000269|PubMed:24333428}. TISSUE SPECIFICITY: Expressed in the hypothalamus, cortex and hippocampus (PubMed:15937339). {ECO:0000269|PubMed:15937339}. +Q09324 GCNT1_MOUSE Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase (EC 2.4.1.102) (Core 2-branching enzyme) (Core2-GlcNAc-transferase) (C2GNT) 428 49,839 Active site (1); Beta strand (14); Chain (1); Disulfide bond (4); Glycosylation (2); Helix (21); Region (3); Sequence conflict (17); Topological domain (2); Transmembrane (1); Turn (4) TRANSMEM 10 32 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 9 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 33 428 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Glycosyltransferase that catalyzes the transfer of an N-acetylglucosamine moiety onto mucin-type core 1 O-glycan to form the branched mucin-type core 2 O-glycan. Mucin-type core 2 O-glycans play an important role in leukocyte extravasation as they serve as scaffolds for the display of the selectin ligand sialyl Lewis X by leukocytes. {ECO:0000269|PubMed:7983056}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Also detected in the trans-Golgi network. {ECO:0000250}. SUBUNIT: Interacts with GOLPH3; may control GCNT1 retention in the Golgi. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in kidney, liver, stomach, spleen, lung and brain. {ECO:0000269|PubMed:9341170}. +P97402 GCNT2_MOUSE N-acetyllactosaminide beta-1,6-N-acetylglucosaminyl-transferase (N-acetylglucosaminyltransferase) (EC 2.4.1.150) (I-branching enzyme) (IGNT) (Large I antigen-forming beta-1,6-N-acetylglucosaminyltransferase) 401 45,697 Chain (1); Glycosylation (4); Sequence conflict (8); Topological domain (2); Transmembrane (1) TRANSMEM 8 28 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 7 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 29 401 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Branching enzyme that converts linear into branched poly-N-acetyllactosaminoglycans. Introduces the blood group I antigen during embryonic development. It is closely associated with the development and maturation of erythroid cells. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein. +Q5JCT0 GCNT3_MOUSE Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 3 (EC 2.4.1.102) (EC 2.4.1.148) (EC 2.4.1.150) (C2GnT-mucin type) (C2GnT-M) (Mucus-type core 2 beta-1,6-N-acetylglucosaminyltransferase) 437 50,698 Chain (1); Disulfide bond (4); Erroneous initiation (1); Erroneous termination (1); Glycosylation (1); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 13 30 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 12 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 31 437 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Glycosyltransferase that can synthesize all known mucin beta 6 N-acetylglucosaminides. Mediates core 2 and core 4 O-glycan branching, 2 important steps in mucin-type biosynthesis. Has also I-branching enzyme activity by converting linear into branched poly-N-acetyllactosaminoglycans, leading to introduce the blood group I antigen during embryonic development. {ECO:0000250|UniProtKB:O95395}. PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. +E9Q649 GCNT4_MOUSE Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 4 (EC 2.4.1.102) (Core 2-branching enzyme 3) (Core2-GlcNAc-transferase 3) (C2GnT3) 455 52,832 Chain (1); Disulfide bond (4); Glycosylation (3); Topological domain (2); Transmembrane (1) TRANSMEM 14 34 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 13 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 35 455 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Glycosyltransferase that mediates core 2 O-glycan branching, an important step in mucin-type biosynthesis. Does not have core 4 O-glycan or I-branching enzyme activity. {ECO:0000250|UniProtKB:Q9P109}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. +Q3V3K7 GCNT7_MOUSE Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 7 (EC 2.4.1.-) 433 48,580 Alternative sequence (1); Chain (1); Disulfide bond (4); Glycosylation (1); Topological domain (2); Transmembrane (1) TRANSMEM 9 25 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 8 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 26 433 Extracellular. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Glycosyltransferase. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. +Q921G8 GCP2_MOUSE Gamma-tubulin complex component 2 (GCP-2) 905 103,223 Chain (1); Modified residue (1); Sequence conflict (2) FUNCTION: Gamma-tubulin complex is necessary for microtubule nucleation at the centrosome. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. SUBUNIT: Gamma-tubulin complex is composed of gamma-tubulin, TUBGCP2, TUBGCP3, TUBGCP4, TUBGCP5 and TUBGCP6. Interacts with ATF5; the ATF5:PCNT:polyglutamylated tubulin (PGT) tripartite unites the mother centriole and the pericentriolar material (PCM) in the centrosome. {ECO:0000250|UniProtKB:Q9BSJ2}. +P58854 GCP3_MOUSE Gamma-tubulin complex component 3 (GCP-3) 905 103,469 Chain (1); Compositional bias (1); Initiator methionine (1); Modified residue (2); Sequence conflict (1) FUNCTION: Gamma-tubulin complex is necessary for microtubule nucleation at the centrosome. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. SUBUNIT: Gamma-tubulin complex is composed of gamma-tubulin, TUBGCP2, TUBGCP3, TUBGCP4, TUBGCP5 and TUBGCP6 (By similarity). Interacts with CDK5RAP2; the interaction is leading to centrosomal localization of TUBTUBGCP3 and CDK5RAP2 (By similarity). Interacts with NIN (via N-terminus); the interaction may promote recruitment of the gamma-tubulin ring complex to the centrosome (PubMed:15784680). {ECO:0000250, ECO:0000269|PubMed:15784680}. +Q9D4F8 GCP4_MOUSE Gamma-tubulin complex component 4 (GCP-4) 667 76,126 Chain (1) FUNCTION: Gamma-tubulin complex is necessary for microtubule nucleation at the centrosome. {ECO:0000250|UniProtKB:Q9UGJ1}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9UGJ1}. SUBUNIT: Gamma-tubulin complex is composed of gamma-tubulin, TUBGCP2, TUBGCP3, TUBGCP4, TUBGCP5 and TUBGCP6. Interacts with NINL. Interacts with ATF5; the ATF5:PCNT:polyglutamylated tubulin (PGT) tripartite unites the mother centriole and the pericentriolar material (PCM) in the centrosome. {ECO:0000250|UniProtKB:Q9UGJ1}. +Q8BKN5 GCP5_MOUSE Gamma-tubulin complex component 5 (GCP-5) 1024 117,977 Alternative sequence (2); Chain (1); Sequence conflict (9) FUNCTION: Gamma-tubulin complex is necessary for microtubule nucleation at the centrosome. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. SUBUNIT: Gamma-tubulin complex is composed of gamma-tubulin, TUBGCP2, TUBGCP3, TUBGCP4, TUBGCP5 and TUBGCP6. {ECO:0000250}. +Q8BMP6 GCP60_MOUSE Golgi resident protein GCP60 (Acyl-CoA-binding domain-containing protein 3) (Golgi complex-associated protein 1) (GOCAP1) (Golgi phosphoprotein 1) (GOLPH1) (PBR- and PKA-associated protein 7) (Peripheral benzodiazepine receptor-associated protein PAP7) 525 60,181 Chain (1); Coiled coil (2); Compositional bias (3); Domain (2); Initiator methionine (1); Modified residue (5); Region (1) FUNCTION: Involved in the maintenance of Golgi structure by interacting with giantin, affecting protein transport between the endoplasmic reticulum and Golgi (By similarity). Involved in hormone-induced steroid biosynthesis in testicular Leydig cells (PubMed:12711385). Recruits PI4KB to the Golgi apparatus membrane; enhances the enzyme activity of PI4KB activity via its membrane recruitment thereby increasing the local concentration of the substrate in the vicinity of the kinase (By similarity). {ECO:0000250|UniProtKB:Q9H3P7, ECO:0000269|PubMed:12711385}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:12711385}; Peripheral membrane protein {ECO:0000269|PubMed:12711385}; Cytoplasmic side {ECO:0000269|PubMed:12711385}. Mitochondrion {ECO:0000269|PubMed:12711385}. Note=Also mitochondrial (via its interaction with PBR). SUBUNIT: Interacts with the C-terminal cytoplasmic domain of giantin/GOLGB1 (By similarity). Interacts with PBR and PKA regulatory subunit RI-alpha. Does not interact with PKA regulatory subunit RI-beta nor PKA regulatory subunit RII-alpha (PubMed:11731621). Interacts with PI4KB, TBC1D22A AND TBC1D22B; interactions with PI4KB and with TBC1D22A and TBC1D22B are mutually exclusive. Interacts with C10ORF76 and RAB11B (By similarity). {ECO:0000250|UniProtKB:Q9H3P7, ECO:0000269|PubMed:11731621}. DOMAIN: The GOLD domain is essential for giantin binding. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain (hippocampus, olfactory bulb, neuronal and glial cells of the cortex), eye, submaxillary gland, testis (interstitial and tubular compartments), ovary (granulosa cells, theca cells at late stages and primary follicles), adrenal gland (fasciculata and glomerulosa cells), heart, liver, and steroidogenic cell lines. {ECO:0000269|PubMed:11731621}. +G5E8P0 GCP6_MOUSE Gamma-tubulin complex component 6 (GCP-6) 1769 197,192 Alternative sequence (2); Chain (1); Erroneous initiation (1) FUNCTION: Gamma-tubulin complex is necessary for microtubule nucleation at the centrosome. {ECO:0000250|UniProtKB:Q96RT7}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q96RT7}. SUBUNIT: Gamma-tubulin complex is composed of gamma-tubulin, TUBGCP2, TUBGCP3, TUBGCP4, TUBGCP5 and TUBGCP6. {ECO:0000250|UniProtKB:Q96RT7}. +P06537 GCR_MOUSE Glucocorticoid receptor (GR) (Nuclear receptor subfamily 3 group C member 1) 783 86,053 Alternative sequence (4); Beta strand (4); Chain (1); Compositional bias (2); Cross-link (6); DNA binding (1); Domain (1); Helix (11); Modified residue (16); Mutagenesis (6); Region (4); Sequence conflict (3); Turn (1); Zinc finger (2) FUNCTION: Receptor for glucocorticoids (GC). Has a dual mode of action: as a transcription factor that binds to glucocorticoid response elements (GRE), both for nuclear and mitochondrial DNA, and as a modulator of other transcription factors. Affects inflammatory responses, cellular proliferation and differentiation in target tissues. Involved in chromatin remodeling (PubMed:10678832). Plays a role in rapid mRNA degradation by binding to the 5' UTR of target mRNAs and interacting with PNRC2 in a ligand-dependent manner which recruits the RNA helicase UPF1 and the mRNA-decapping enzyme DCP1A, leading to RNA decay (By similarity). Could act as a coactivator for STAT5-dependent transcription upon growth hormone (GH) stimulation and could reveal an essential role of hepatic GR in the control of body growth (PubMed:15037546). {ECO:0000250|UniProtKB:P04150, ECO:0000269|PubMed:10678832, ECO:0000269|PubMed:15037546}.; FUNCTION: Isoform 1: Has transcriptional activation and repression activity (By similarity). Mediates glucocorticoid-induced apoptosis (By similarity). Promotes accurate chromosome segregation during mitosis (PubMed:25847991). May act as a tumor suppressor (PubMed:25847991). May play a negative role in adipogenesis through the regulation of lipolytic and antilipogenic gene expression (PubMed:21994940). {ECO:0000250|UniProtKB:P04150, ECO:0000269|PubMed:21994940, ECO:0000269|PubMed:25847991}.; FUNCTION: Isoform 3: Acts as a dominant negative inhibitor of isoform 1 (PubMed:20660300). Has intrinsic transcriptional activity independent of isoform Alpha when both isoforms are coexpressed (By similarity). Loses this transcription modulator function on its own (By similarity). Has no hormone-binding activity (PubMed:20660300). May play a role in controlling glucose metabolism by maintaining insulin sensitivity (PubMed:20660300). Reduces hepatic gluconeogenesis through down-regulation of PEPCK in an isoform Alpha-dependent manner (By similarity). Directly regulates STAT1 expression in isoform Alpha-independent manner (By similarity). {ECO:0000250|UniProtKB:P04150, ECO:0000269|PubMed:20660300}. PTM: Acetylation by CLOCK reduces its binding to glucocorticoid response elements and its transcriptional activity. {ECO:0000250|UniProtKB:P04150}.; PTM: Increased proteasome-mediated degradation in response to glucocorticoids. {ECO:0000269|PubMed:11555652}.; PTM: Phosphorylated in the absence of hormone; becomes hyperphosphorylated in the presence of glucocorticoids. Phosphorylated in the absence of hormone; becomes hyperphosphorylated in the presence of glucocorticoid. The Ser-212, Ser-234 and Ser-412-phosphorylated forms are mainly cytoplasmic, and the Ser-220-phosphorylated form is nuclear (By similarity). Phosphorylation at Ser-220 increases transcriptional activity (By similarity). Phosphorylation at Ser-212, Ser-234 and Ser-412 decreases signaling capacity (By similarity). Phosphorylation at Ser-412 may protect from glucocorticoid-induced apoptosis (By similarity). Phosphorylation at Ser-212 and Ser-220 is not required in regulation of chromosome segregation (By similarity). May be dephosphorylated by PPP5C, attenuates NR3C1 action (PubMed:21994940). {ECO:0000250|UniProtKB:P04150, ECO:0000269|PubMed:2019585, ECO:0000269|PubMed:21994940}.; PTM: Sumoylation at Lys-285 and Lys-301 negatively regulates its transcriptional activity. Sumoylation at Lys-709 positively regulates its transcriptional activity in the presence of RWDD3. Sumoylation at Lys-285 and Lys-301 is dispensable whereas sumoylation at Lys-709 is critical for the stimulatory effect of RWDD3 on its transcriptional activity. Heat shock increases sumoylation in a RWDD3-dependent manner. {ECO:0000250|UniProtKB:P06536}.; PTM: Ubiquitinated; restricts glucocorticoid-mediated transcriptional signaling. {ECO:0000269|PubMed:11555652}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11278753, ECO:0000269|PubMed:25676786}. Nucleus {ECO:0000269|PubMed:10678832, ECO:0000269|PubMed:11278753, ECO:0000269|PubMed:25676786}. Note=Cytoplasmic in the absence of ligand, nuclear after ligand-binding (PubMed:11278753). The hormone-occupied receptor undergoes rapid exchange between chromatin and the nucleoplasmic compartment (PubMed:10678832). {ECO:0000269|PubMed:10678832, ECO:0000269|PubMed:11278753}.; SUBCELLULAR LOCATION: Isoform 1: Cytoplasm {ECO:0000250|UniProtKB:P04150}. Nucleus {ECO:0000250|UniProtKB:P04150}. Mitochondrion {ECO:0000250|UniProtKB:P04150}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P04150}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P04150}. Note=After ligand activation, translocates from the cytoplasm to the nucleus. {ECO:0000250|UniProtKB:P04150}.; SUBCELLULAR LOCATION: Isoform 3: Nucleus {ECO:0000269|PubMed:20660300}. Cytoplasm {ECO:0000269|PubMed:20660300}. Note=Expressed predominantly in the nucleus with some expression also detected in the cytoplasm. {ECO:0000269|PubMed:20660300}. SUBUNIT: Heteromultimeric cytoplasmic complex with HSP90AA1, HSPA1A/HSPA1B, and FKBP5 or another immunophilin such as PPID, STIP1, or the immunophilin homolog PPP5C (PubMed:9195923, PubMed:21994940). Upon ligand binding FKBP5 dissociates from the complex and FKBP4 takes its place, thereby linking the complex to dynein and mediating transport to the nucleus, where the complex dissociates (PubMed:9195923, PubMed:11278753). Probably forms a complex composed of chaperones HSP90 and HSP70, co-chaperones CDC37, PPP5C, TSC1 and client protein TSC2, CDK4, AKT, RAF1 and NR3C1; this complex does not contain co-chaperones STIP1/HOP and PTGES3/p23 (By similarity). Directly interacts with UNC45A (By similarity). Binds to DNA as a homodimer, and as heterodimer with NR3C2 or the retinoid X receptor. Binds STAT5A and STAT5B homodimers and heterodimers (PubMed:9528750). Interacts with NRIP1, POU2F1, POU2F2 and TRIM28 (PubMed:9742105). Interacts with several coactivator complexes, including the SMARCA4 complex, CREBBP/EP300, TADA2L (Ada complex) and p160 coactivators such as NCOA2 and NCOA6 (By similarity). Interaction with BAG1 inhibits transactivation (By similarity). Interacts with HEXIM1, PELP1 and TGFB1I1 (PubMed:10848625). Interacts with NCOA1 (By similarity). Interacts with NCOA3, SMARCA4, SMARCC1, SMARCD1, and SMARCE1 (By similarity). Interacts with CLOCK, CRY1 and CRY2 in a ligand-dependent fashion (PubMed:22170608). Interacts with CIART (PubMed:24736997). Interacts with RWDD3 (By similarity). Interacts with UBE2I/UBC9 and this interaction is enhanced in the presence of RWDD3 (By similarity). Interacts with GRIP1 (By similarity). Interacts with NR4A3 (via nuclear receptor DNA-binding domain), represses transcription activity of NR4A3 on the POMC promoter Nur response element (NurRE) (By similarity). Directly interacts with PNRC2 to attract and form a complex with UPF1 and DCP1A; the interaction leads to rapid mRNA degradation (By similarity). Interacts with GSK3B (By similarity). Interacts with FNIP1 and FNIP2 (By similarity). Interacts (via C-terminus) with HNRNPU (via C-terminus) (By similarity). {ECO:0000250|UniProtKB:P04150, ECO:0000250|UniProtKB:P06536, ECO:0000269|PubMed:10678832, ECO:0000269|PubMed:10848625, ECO:0000269|PubMed:11278753, ECO:0000269|PubMed:21994940, ECO:0000269|PubMed:22170608, ECO:0000269|PubMed:24736997, ECO:0000269|PubMed:9195923, ECO:0000269|PubMed:9528750, ECO:0000269|PubMed:9742105}. DOMAIN: Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain. The ligand-binding domain is required for correct chromosome segregation during mitosis although ligand binding is not required. {ECO:0000250|UniProtKB:P04150}. TISSUE SPECIFICITY: Expressed in spleen, kidney and liver. Isoform 3: Expressed at highest level in spleen with lesser amounts in kidney and liver. {ECO:0000269|PubMed:20660300}. +Q6RFH4 GCSAM_MOUSE Germinal center-associated signaling and motility protein (Germinal center B-cell-expressed transcript 2 protein) 181 20,988 Alternative sequence (1); Chain (1); Modified residue (2); Sequence conflict (1) FUNCTION: Involved in the negative regulation of lymphocyte motility. It mediates the migration-inhibitory effects of IL6. Serves as a positive regulator of the RhoA signaling pathway. Enhancement of RhoA activation results in inhibition of lymphocyte and lymphoma cell motility by activation of its downstream effector ROCK. Is a regulator of B-cell receptor signaling, that acts through SYK kinase activation. {ECO:0000250}. PTM: Phosphorylation on tyrosine residues can be induced by IL6. Phosphorylation is mediated by LYN. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=It relocalizes from the cytoplasm to podosome-like structures upon cell treatment with IL6. {ECO:0000250}. SUBUNIT: Interacts with ACTB and MYH2; the interaction with MYH2 is increased by IL6-induced phosphorylation. Interacts (via C-terminus) with ARHGEF11 (via DH domain). Interacts with ARHGEF12. Interacts with SYK; the interaction increases after B-cell receptor stimulation, resulting in enhanced SYK autophosphorylation and activity. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in normal germinal center (GC) B-cells. Expressed in spleen and, to a lesser extent, bone marrow. {ECO:0000269|PubMed:7981148, ECO:0000269|Ref.2}. +Q91W43 GCSP_MOUSE Glycine dehydrogenase (decarboxylating), mitochondrial (EC 1.4.4.2) (Glycine cleavage system P protein) (Glycine decarboxylase) (Glycine dehydrogenase (aminomethyl-transferring)) 1025 113,267 Chain (1); Modified residue (5); Transit peptide (1) FUNCTION: The glycine cleavage system catalyzes the degradation of glycine. The P protein (GLDC) binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein (GCSH) (By similarity). {ECO:0000250|UniProtKB:P15505}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P15505}. SUBUNIT: Interacts with GCSH (By similarity). Homodimer. The glycine cleavage system is composed of four proteins: P (GLDC), T (GCST), L (DLD) and H (GCSH) (By similarity). {ECO:0000250|UniProtKB:P15505}. +Q8CFA2 GCST_MOUSE Aminomethyltransferase, mitochondrial (EC 2.1.2.10) (Glycine cleavage system T protein) (GCVT) 403 44,009 Binding site (3); Chain (1); Modified residue (1); Transit peptide (1) FUNCTION: The glycine cleavage system catalyzes the degradation of glycine. {ECO:0000250|UniProtKB:P48728}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P48728}. SUBUNIT: The glycine cleavage system is composed of four proteins: P, T, L and H. {ECO:0000250|UniProtKB:P48728}. +Q9ERL9 GCYA1_MOUSE Guanylate cyclase soluble subunit alpha-1 (GCS-alpha-1) (EC 4.6.1.2) (Guanylate cyclase soluble subunit alpha-3) (GCS-alpha-3) (Soluble guanylate cyclase large subunit) 691 77,588 Chain (1); Domain (1); Modified residue (1); Sequence conflict (1) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. SUBUNIT: The active enzyme is formed by a heterodimer of an alpha and a beta subunit. Heterodimer with GUCY1B1. {ECO:0000250|UniProtKB:Q02108}. +O54865 GCYB1_MOUSE Guanylate cyclase soluble subunit beta-1 (GCS-beta-1) (EC 4.6.1.2) (Guanylate cyclase soluble subunit beta-3) (GCS-beta-3) (Soluble guanylate cyclase small subunit) 620 70,598 Chain (1); Domain (1); Metal binding (1) FUNCTION: Mediates responses to nitric oxide (NO) by catalyzing the biosynthesis of the signaling molecule cGMP. {ECO:0000250|UniProtKB:P16068}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P16068}. SUBUNIT: The active enzyme is formed by a heterodimer of an alpha and a beta subunit. Heterodimer with GUCY1A1. Can also form inactive homodimers in vitro. {ECO:0000250|UniProtKB:Q02153}. +Q91WL5 CP4CA_MOUSE Cytochrome P450 4A12A (EC 1.14.14.1) (CYPIVA12) 508 58,350 Binding site (1); Chain (1); Frameshift (1); Metal binding (1); Sequence conflict (7) FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. {ECO:0000305}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. +Q9Z100 CPXM1_MOUSE Probable carboxypeptidase X1 (EC 3.4.17.-) (Metallocarboxypeptidase CPX-1) 722 80,907 Active site (1); Chain (1); Compositional bias (2); Disulfide bond (1); Domain (1); Glycosylation (5); Metal binding (3); Sequence conflict (1); Signal peptide (1) FUNCTION: May be involved in cell-cell interactions. No carboxypeptidase activity was found yet. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Strongly expressed in testis and spleen. Moderatly expressed in salivary gland, brain, heart, lung, and kidney. Extremely low expression in liver and muscle. No expression in eye, adrenal, and white adipose tissues. {ECO:0000269|PubMed:10073577}. +Q0VE82 CPNE7_MOUSE Copine-7 (Copine VII) 557 61,891 Chain (1); Domain (3) FUNCTION: Calcium-dependent phospholipid-binding protein that may play a role in calcium-mediated intracellular processes. {ECO:0000250|UniProtKB:Q99829}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UBL6}. Nucleus {ECO:0000250|UniProtKB:Q9UBL6}. Cell membrane {ECO:0000250|UniProtKB:Q9UBL6}. Note=Translocates to the cell membrane in a calcium-dependent manner. {ECO:0000250|UniProtKB:Q9UBL6}. DOMAIN: The C2 domain 1 is not necessary for calcium-mediated translocation and association to the plasma membrane. The C2 domain 2 is necessary for calcium-mediated translocation and association to the plasma membrane. {ECO:0000250|UniProtKB:H1UBN0}. +Q5QR91 CQ078_MOUSE Uncharacterized protein C17orf78 homolog 290 32,583 Chain (1); Sequence conflict (1); Transmembrane (1) TRANSMEM 202 222 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q9JJV0 CRBA4_MOUSE Beta-crystallin A4 (Beta-A4 crystallin) 196 22,469 Chain (1); Domain (4); Initiator methionine (1); Modified residue (1); Region (2) FUNCTION: Crystallins are the dominant structural components of the vertebrate eye lens. SUBUNIT: Homo/heterodimer, or complexes of higher-order. The structure of beta-crystallin oligomers seems to be stabilized through interactions between the N-terminal arms (By similarity). {ECO:0000250}. DOMAIN: Has a two-domain beta-structure, folded into four very similar Greek key motifs. +Q9WVJ5 CRBB1_MOUSE Beta-crystallin B1 (Beta-B1 crystallin) [Cleaved into: Beta-crystallin B1B] 250 28,003 Chain (2); Domain (4); Initiator methionine (1); Modified residue (3); Region (3) FUNCTION: Crystallins are the dominant structural components of the vertebrate eye lens. PTM: Specific cleavages in the N-terminal arm occur during lens maturation and give rise to truncated forms, leading to impaired oligomerization and protein insolubilization. The protease responsible for this partial degradation could be calpain II. SUBUNIT: Homo/heterodimer, or complexes of higher-order. The structure of beta-crystallin oligomers seems to be stabilized through interactions between the N-terminal arms. DOMAIN: Has a two-domain beta-structure, folded into four very similar Greek key motifs. +Q8C7D2 CRBN_MOUSE Protein cereblon (Protein PiL) 445 50,880 Alternative sequence (2); Beta strand (7); Chain (1); Domain (2); Frameshift (1); Helix (4); Metal binding (4); Modified residue (1); Region (1); Sequence conflict (9); Turn (2) Protein modification; protein ubiquitination. FUNCTION: Substrate recognition component of a DCX (DDB1-CUL4-X-box) E3 protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as MEIS2. Normal degradation of key regulatory proteins is required for normal limb outgrowth and expression of the fibroblast growth factor FGF8 (By similarity). May play a role in memory and learning by regulating the assembly and neuronal surface expression of large-conductance calcium-activated potassium channels in brain regions involved in memory and learning via its interaction with KCNT1 (By similarity). {ECO:0000250|UniProtKB:Q96SW2, ECO:0000305}. PTM: Ubiquitinated, ubiquitination is mediated by its own DCX protein ligase complex. {ECO:0000250|UniProtKB:Q96SW2}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96SW2}. Nucleus {ECO:0000250|UniProtKB:Q96SW2}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. SUBUNIT: Component of a DCX (DDB1-CUL4-X-box) protein ligase complex, at least composed of CRBN, CUL4A, DDB1 and RBX1. Interacts directly with DDB1 (By similarity). Interacts with KCNT1 (By similarity). {ECO:0000250|UniProtKB:Q56AP7, ECO:0000250|UniProtKB:Q96SW2}. DOMAIN: The CULT domain binds thalidomide and related drugs. Thalidomide binding leads to a change in substrate specificity of the human DCX (DDB1-CUL4-X-box) E3 protein ligase complex, while no such change is observed in rodents. {ECO:0000269|PubMed:25108355}. TISSUE SPECIFICITY: Highly expressed in brain. {ECO:0000269|PubMed:20131966}. +Q9D2A5 CR3L4_MOUSE Cyclic AMP-responsive element-binding protein 3-like protein 4 (cAMP-responsive element-binding protein 3-like protein 4) (Attaching to CRE-like 1) (ATCE1) (Acre1) (Transcript induced in spermiogenesis protein 40) (Tisp40) (mJAL) [Cleaved into: Processed cyclic AMP-responsive element-binding protein 3-like protein 4] 370 41,025 Alternative sequence (1); Chain (2); Domain (1); Glycosylation (2); Mutagenesis (2); Region (3); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 272 292 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 271 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 293 370 Lumenal. {ECO:0000255}. FUNCTION: Transcriptional activator that may play a role in the unfolded protein response of the testis. Proposed to be involved in spermiogenesis. May be involved in regulating the maturation of sperm head nuclei. Alternatively proposed to be a paternally delivered transcription factor that may function in early zygotic gene activation. Increases the binding of CREM isoform Tau with CRE. The CREM isoform Tau-CREB3L4 heterodimer functions through CRE but not through UPRE and may recruit HIRA to CRE to regulate histone exchange. {ECO:0000269|PubMed:16107712, ECO:0000269|PubMed:16595651, ECO:0000269|PubMed:16925989, ECO:0000269|PubMed:16999736}. PTM: Controlled by regulated intramembrane proteolysis (RIP). Following ER stress a fragment containing the cytoplasmic transcription factor domain is released by proteolysis. The cleavage seems to be performed sequentially by site-1 and site-2 proteases (PS1 and PS2). PS1 cleavage may be suppressed by a determinant in the C-terminal region. {ECO:0000269|PubMed:15938716}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16925989}; Single-pass type II membrane protein {ECO:0000269|PubMed:16925989}. Cytoplasmic vesicle, secretory vesicle, acrosome inner membrane {ECO:0000269|PubMed:16925989}; Single-pass type II membrane protein {ECO:0000269|PubMed:16925989}. Note=According to PubMed:16925989 is not observed within nuclei of haploid spermatids at any spermiogenic stage.; SUBCELLULAR LOCATION: Processed cyclic AMP-responsive element-binding protein 3-like protein 4: Nucleus. Note=Under ER stress the cleaved N-terminal cytoplasmic domain translocates into the nucleus. SUBUNIT: Binds DNA as a dimer (By similarity). Forms a heterodimer with CREM isoform Tau. {ECO:0000250}. TISSUE SPECIFICITY: Predominantly expressed at high levels in testis with isoform 2 being the predominant isoform. Specifically expressed in postmeiotic spermatids and accumulates in the mid/late stage (at protein level). Ubiquitously expressed at low levels. {ECO:0000269|PubMed:11956138, ECO:0000269|PubMed:15938716, ECO:0000269|PubMed:16107712, ECO:0000269|PubMed:16728718, ECO:0000269|PubMed:16925989}. +Q03963 E2AK2_MOUSE Interferon-induced, double-stranded RNA-activated protein kinase (EC 2.7.11.1) (Eukaryotic translation initiation factor 2-alpha kinase 2) (eIF-2A protein kinase 2) (Interferon-inducible RNA-dependent protein kinase) (P1/eIF-2A protein kinase) (Protein kinase RNA-activated) (PKR) (Protein kinase R) (Serine/threonine-protein kinase TIK) (Tyrosine-protein kinase EIF2AK2) (EC 2.7.10.2) (p68 kinase) 515 58,280 Active site (1); Beta strand (8); Binding site (1); Chain (1); Compositional bias (2); Cross-link (2); Domain (3); Helix (4); Initiator methionine (1); Modified residue (9); Nucleotide binding (1); Region (1); Sequence conflict (7) FUNCTION: IFN-induced dsRNA-dependent serine/threonine-protein kinase which plays a key role in the innate immune response to viral infection and is also involved in the regulation of signal transduction, apoptosis, cell proliferation and differentiation. Exerts its antiviral activity on a wide range of DNA and RNA viruses including west nile virus (WNV), sindbis virus (SV), foot-and-mouth virus (FMDV), semliki Forest virus (SFV) and lymphocytic choriomeningitis virus (LCMV). Inhibits viral replication via phosphorylation of the alpha subunit of eukaryotic initiation factor 2 (EIF2S1), this phosphorylation impairs the recycling of EIF2S1 between successive rounds of initiation leading to inhibition of translation which eventually results in shutdown of cellular and viral protein synthesis. Also phosphorylates other substrates including p53/TP53, PPP2R5A, DHX9, ILF3 and IRS1. In addition to serine/threonine-protein kinase activity, also has tyrosine-protein kinase activity and phosphorylates CDK1 at 'Tyr-4' upon DNA damage, facilitating its ubiquitination and proteosomal degradation. Either as an adapter protein and/or via its kinase activity, can regulate various signaling pathways (p38 MAP kinase, NF-kappa-B and insulin signaling pathways) and transcription factors (JUN, STAT1, STAT3, IRF1, ATF3) involved in the expression of genes encoding proinflammatory cytokines and IFNs. Activates the NF-kappa-B pathway via interaction with IKBKB and TRAF family of proteins and activates the p38 MAP kinase pathway via interaction with MAP2K6. Can act as both a positive and negative regulator of the insulin signaling pathway (ISP). Negatively regulates ISP by inducing the inhibitory phosphorylation of insulin receptor substrate 1 (IRS1) at 'Ser-312' and positively regulates ISP via phosphorylation of PPP2R5A which activates FOXO1, which in turn up-regulates the expression of insulin receptor substrate 2 (IRS2). Can regulate NLRP3 inflammasome assembly and the activation of NLRP3, NLRP1, AIM2 and NLRC4 inflammasomes. Can trigger apoptosis via FADD-mediated activation of CASP8. Plays a role in the regulation of the cytoskeleton by binding to gelsolin (GSN), sequestering the protein in an inactive conformation away from actin. Regulates proliferation, differentiation and survival of hematopoietic stem/progenitor cells, induction of cytokines and chemokines and plays a role in cortex-dependent memory consolidation. {ECO:0000269|PubMed:19229320, ECO:0000269|PubMed:19264662, ECO:0000269|PubMed:20038207, ECO:0000269|PubMed:20478537, ECO:0000269|PubMed:20585572, ECO:0000269|PubMed:20631127, ECO:0000269|PubMed:21123651, ECO:0000269|PubMed:21994357, ECO:0000269|PubMed:22633459, ECO:0000269|PubMed:22801494, ECO:0000269|PubMed:22948222, ECO:0000269|PubMed:23392680, ECO:0000269|PubMed:23401008, ECO:0000269|PubMed:23403623}. PTM: Autophosphorylated on several Ser, Thr and Tyr residues. Autophosphorylation of Thr-414 is dependent on Thr-409 and is stimulated by dsRNA binding and dimerization. Autophosphorylation apparently leads to the activation of the kinase. Tyrosine autophosphorylation is essential for efficient dsRNA-binding, dimerization, and kinase activation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. SUBUNIT: Homodimer. Interacts with DNAJC3 and STRBP (By similarity). Forms a complex with FANCA, FANCC, FANCG and HSP70 (By similarity). Interacts with ADAR/ADAR1. The inactive form interacts with NCK1. Interacts (via the kinase catalytic domain) with STAT3 (via SH2 domain), TRAF2 (C-terminus), TRAF5 (C-terminus) and TRAF6 (C-terminus). Interacts with MAP2K6, TARBP2, NLRP1, NLRC4 and AIM2. Interacts (via DRBM 1 domain) with DUS2L (via DRBM domain) (By similarity). Interacts with DHX9 (via N-terminus) and this interaction is dependent upon activation of the kinase. The inactive form interacts with GSN. Interacts with IKBKB/IKKB, NPM1, NLRP3 and IRS1. {ECO:0000250, ECO:0000269|PubMed:10848580, ECO:0000269|PubMed:12882984, ECO:0000269|PubMed:17079286, ECO:0000269|PubMed:19229320, ECO:0000269|PubMed:22633459, ECO:0000269|PubMed:22801494, ECO:0000269|PubMed:22948222}. TISSUE SPECIFICITY: Expressed in heart, lung, brain, kidney, testes, thymus and bone marrow. +Q8BWG9 CRCM1_MOUSE Calcium release-activated calcium channel protein 1 (Protein orai-1) (Transmembrane protein 142A) 304 33,062 Chain (1); Compositional bias (1); Erroneous initiation (1); Glycosylation (1); Modified residue (1); Region (2); Sequence conflict (1); Topological domain (5); Transmembrane (4) TRANSMEM 90 107 Helical. {ECO:0000255}.; TRANSMEM 122 142 Helical. {ECO:0000255}.; TRANSMEM 176 196 Helical. {ECO:0000255}.; TRANSMEM 238 258 Helical. {ECO:0000255}. TOPO_DOM 1 89 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 108 121 Extracellular. {ECO:0000255}.; TOPO_DOM 143 175 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 197 237 Extracellular. {ECO:0000255}.; TOPO_DOM 259 304 Cytoplasmic. {ECO:0000250}. FUNCTION: Ca(2+) release-activated Ca(2+) (CRAC) channel subunit which mediates Ca(2+) influx following depletion of intracellular Ca(2+) stores and channel activation by the Ca(2+) sensor, STIM1. CRAC channels are the main pathway for Ca(2+) influx in T-cells and promote the immune response to pathogens by activating the transcription factor NFAT. {ECO:0000250|UniProtKB:Q96D31}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q96D31}.; PTM: Ubiquitinated. {ECO:0000250|UniProtKB:Q96D31}.; PTM: Cys-197 is oxidated, leading to inactivate channel activity. {ECO:0000250|UniProtKB:Q96D31}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q96D31}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q96D31}. Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:Q96D31}. Note=Colocalizes with UBQLN1 in the autophagosome. Colocalizes with STIM1 at the cell membrane. {ECO:0000250|UniProtKB:Q96D31}. SUBUNIT: Interacts with STIM1 and STIM2; this regulates channel activity. Interacts with CALM; this may displace STIM1 and STIM2 and might thereby modulate channel activity. Interacts with CRACR2A/EFCAB4B; the interaction is direct and takes place in absence of Ca(2+). Forms a complex with CRACR2A/EFCAB4B and STIM1 at low concentration of Ca(2+), the complex dissociates at elevated Ca(2+) concentrations. Interacts with SLC35G1. Interacts with UBQLN1. Interacts with ADCY8; interaction is calcium store depletion independent; interaction occurs in membrane raft; interaction increases markedly after store depletion; positively regulates SOCE-induced adenylate cyclase activity; contributes to the targeting of ADCY8 to discrete regions of the plasma membrane that are shielded from other calcium events (By similarity). {ECO:0000250|UniProtKB:Q96D31}. +O88668 CREG1_MOUSE Protein CREG1 (Cellular repressor of E1A-stimulated genes 1) 220 24,452 Chain (1); Glycosylation (2); Sequence conflict (1); Signal peptide (1) FUNCTION: May contribute to the transcriptional control of cell growth and differentiation. Antagonizes transcriptional activation and cellular transformation by the adenovirus E1A protein. The transcriptional control activity of cell growth requires interaction with IGF2R (By similarity). {ECO:0000250}. PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Homodimer. Interacts with IGF2R; the interaction is dependent on glycosylation (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10815803}. +Q9CYA0 CREL2_MOUSE Cysteine-rich with EGF-like domain protein 2 350 38,220 Chain (1); Disulfide bond (6); Domain (2); Glycosylation (1); Repeat (2); Signal peptide (1) FUNCTION: May regulate transport of alpha4-beta2 neuronal acetylcholine receptor. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. Endoplasmic reticulum {ECO:0000250}. SUBUNIT: May interact with CHRNA4. {ECO:0000250}. +Q61817 CREB3_MOUSE Cyclic AMP-responsive element-binding protein 3 (CREB-3) (cAMP-responsive element-binding protein 3) (Transcription factor LZIP) [Cleaved into: Processed cyclic AMP-responsive element-binding protein 3] 404 45,112 Alternative sequence (1); Chain (2); Domain (1); Glycosylation (2); Motif (3); Region (2); Sequence conflict (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 262 282 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 261 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 283 404 Lumenal. {ECO:0000255}. FUNCTION: Endoplasmic reticulum (ER)-bound sequence-specific transcription factor that directly binds DNA and activates transcription. Plays a role in the unfolded protein response (UPR), promoting cell survival versus ER stress-induced apoptotic cell death. Also involved in cell proliferation, migration and differentiation, tumor suppression and inflammatory gene expression. Acts as a positive regulator of LKN-1/CCL15-induced chemotaxis signaling of leukocyte cell migration. Associates with chromatin to the HERPUD1 promoter. Also induces transcriptional activation of chemokine receptors. Functions as a negative transcriptional regulator in ligand-induced transcriptional activation of the glucocorticoid receptor NR3C1 by recruiting and activating histone deacetylases (HDAC1, HDAC2 and HDAC6). Also decreases the acetylation level of histone H4. Does not promote the chemotactic activity of leukocyte cells. {ECO:0000250|UniProtKB:O43889}.; FUNCTION: Processed cyclic AMP-responsive element-binding protein 3: This is the transcriptionally active form that translocates to the nucleus and activates unfolded protein response (UPR) target genes during endoplasmic reticulum (ER) stress response. Binds the cAMP response element (CRE) (consensus: 5'-GTGACGT[AG][AG]-3') and C/EBP sequences present in many promoters to activate transcription of the genes. Binds to the unfolded protein response element (UPRE) consensus sequences sites. Binds DNA to the 5'-CCAC[GA]-3'half of ERSE II (5'-ATTGG-N-CCACG-3'). {ECO:0000250|UniProtKB:O43889}. PTM: First proteolytically cleaved by site-1 protease (S1P) that generates membrane-associated N-terminus and a luminal C-terminus forms. The membrane-associated N-terminus form is further proteolytically processed probably by the site-2 protease (S2P) through a regulated intramembrane proteolysis (RIP), releasing the transcriptional active processed cyclic AMP-responsive element-binding protein 3 form, which is transported to the nucleus. The proteolytic cleavage is strongly induced during dendritic cell (DC) maturation and inhibited by DCSTAMP. That form is rapidly degraded. {ECO:0000250|UniProtKB:O43889}.; PTM: N-glycosylated. {ECO:0000250|UniProtKB:O43889}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O43889}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:O43889, ECO:0000255}. Golgi apparatus {ECO:0000250|UniProtKB:O43889}. Nucleus {ECO:0000250|UniProtKB:O43889}. Cytoplasm {ECO:0000250|UniProtKB:O43889}. Note=Colocalizes with HCFC1 in neuronal cell bodies of the trigeminal ganglia. Colocalizes with DCSTAMP in the ER membrane of immature dendritic cell (DC). Colocalizes with CANX, CCR1, HCFC1 in the ER membrane. {ECO:0000250|UniProtKB:O43889}.; SUBCELLULAR LOCATION: Processed cyclic AMP-responsive element-binding protein 3: Nucleus {ECO:0000250|UniProtKB:O43889}. Note=Upon RIP activation the transcriptional active processed cyclic AMP-responsive element-binding protein 3 form translocates into the nucleus. Detected in the nucleus upon dendritic cell maturation and RIP activation. Colocalizes with CREBRF in nuclear foci. Colocalizes with CREBZF in promyelocytic leukemia protein nuclear bodies (PML-NB). {ECO:0000250|UniProtKB:O43889}. SUBUNIT: Homodimer. Interacts with HCFC1; the interaction is required to stimulate CREB3 transcriptional activity. Interacts with CREBZF; the interaction occurs only in combination with HCFC1. Interacts (via central part and transmembrane region) with DCSTAMP (via C-terminus cytoplasmic domain). Interacts with OS9. Interacts (via leucine-zipper domain) with CREBRF (via leucine-zipper domain); the interaction occurs only after CREB3 activation and promotes CREB3 degradation. Interacts (via C-terminal domain) with CCR1. {ECO:0000250|UniProtKB:O43889}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:8112612}. +P27699 CREM_MOUSE cAMP-responsive element modulator (Inducible cAMP early repressor) (ICER) 357 38,516 Alternative sequence (8); Chain (1); Domain (2); Erroneous initiation (9); Modified residue (5); Mutagenesis (1); Region (2) FUNCTION: Transcriptional regulator that binds the cAMP response element (CRE), a sequence present in many viral and cellular promoters. Isoforms are either transcriptional activators or repressors. Isoform 2, isoform 3 and isoform 4 are repressors, while isoform 1 is an activator. Plays a role in spermatogenesis and is involved in spermatid maturation. Binding of isoform 1 (activator) to CRE is increased by CREB3L4. The CREM isoform 1-CREB3L4 heterodimer functions through CRE and may recruit HIRA to CRE to regulate histone exchange (PubMed:16595651). {ECO:0000269|PubMed:16595651}.; FUNCTION: Isoform 11: Plays a role in the regulation of the circadian clock: acts as a transcriptional repressor of the core circadian component PER1 by directly binding to cAMP response elements in its promoter. {ECO:0000269|PubMed:16595651, ECO:0000269|PubMed:23443664}. PTM: Stimulated by phosphorylation (By similarity). Phosphorylated on Ser-116 by TSSK4 in vitro. {ECO:0000250|UniProtKB:Q01147, ECO:0000269|PubMed:26940607}.; PTM: Ubiquitinated by CDC34 and RAD6B in order to be degraded by the proteasome. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23443664, ECO:0000269|PubMed:8252624}.; SUBCELLULAR LOCATION: Isoform 11: Cytoplasm. Nucleus. SUBUNIT: Binds DNA as a dimer (By similarity). Interacts with CDC34 (By similarity). Interacts with FHL5 (PubMed:10086359). May interact with TSSK4 (PubMed:26940607). Isoform 1 forms a heterodimer with CREB3L4 (PubMed:16595651). {ECO:0000250|UniProtKB:Q03060, ECO:0000269|PubMed:10086359, ECO:0000269|PubMed:16595651, ECO:0000269|PubMed:26940607}. TISSUE SPECIFICITY: Expressed in the testis. {ECO:0000269|PubMed:26940607}. +Q61501 E2F1_MOUSE Transcription factor E2F1 (E2F-1) 430 46,323 Chain (1); DNA binding (1); Modified residue (4); Motif (1); Region (7) FUNCTION: Transcription activator that binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. The DRTF1/E2F complex functions in the control of cell-cycle progression from G1 to S phase. E2F1 binds preferentially RB1 in a cell-cycle dependent manner. It can mediate both cell proliferation and TP53/p53-dependent apoptosis. Blocks adipocyte differentiation by binding to specific promoters repressing CEBPA binding to its target gene promoters (PubMed:11672531, PubMed:20176812). Positively regulates transcription of RRP1B (By similarity). {ECO:0000250|UniProtKB:Q01094, ECO:0000269|PubMed:11672531, ECO:0000269|PubMed:20176812, ECO:0000269|PubMed:9674698}. PTM: Phosphorylated by CDK2 and cyclin A-CDK2 in the S-phase. Phosphorylation by CHEK2 stabilizes E2F1 upon DNA damage and regulates its effect on transcription and apoptosis (By similarity). {ECO:0000250}.; PTM: Acetylation stimulates DNA-binding. Enhanced under stress conditions such as DNA damage and inhibited by retinoblastoma protein RB1. Regulated by KAP1/TRIM28 which recruits HDAC1 to E2F1 resulting in deacetylation. Acetylated by P/CAF/KAT2B (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q01094}. SUBUNIT: Component of the DRTF1/E2F transcription factor complex. Forms heterodimers with DP family members. The E2F1 complex binds specifically hypophosphorylated retinoblastoma protein RB1. During the cell cycle, RB1 becomes phosphorylated in mid-to-late G1 phase, detaches from the DRTF1/E2F complex, rendering E2F transcriptionally active. Interacts with TRRAP, which probably mediates its interaction with histone acetyltransferase complexes, leading to transcription activation. Binds TOPBP1 and EAPP. Interacts with ARID3A. Interacts with TRIM28; the interaction inhibits E2F1 acetylation through recruiting HDAC1 and represses its transcriptional activity. Interaction with KAT2B; the interaction acetylates E2F1 enhancing its DNA-binding and transcriptional activity. Interacts with BIRC2/c-IAP1 (via BIR domains). The complex TFDP1:E2F1 interacts with CEBPA; the interaction prevents CEBPA binding to target genes promoters and represses its transcriptional activity. Interacts with RRP1B (By similarity). Interacts with HCFC1 (By similarity). Interacts with KMT2E; the interaction is probably indirect and is mediated via HCFC1 (By similarity). {ECO:0000250|UniProtKB:Q01094, ECO:0000269|PubMed:15716352}. +Q8CDG5 CRERF_MOUSE CREB3 regulatory factor (Luman recruitment factor) (LRF) 640 72,598 Chain (1); Compositional bias (1); Domain (1); Region (2); Sequence conflict (1) FUNCTION: Acts as a negative regulator of the endoplasmic reticulum stress response or unfolded protein response (UPR). Represses the transcriptional activity of CREB3 during the UPR. Recruits CREB3 into nuclear foci (By similarity). {ECO:0000250}. PTM: Probably degraded by the proteasome. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Colocalizes with CREB3 in nuclear foci. {ECO:0000250}. SUBUNIT: Interacts (via leucine-zipper domain) with CREB3 (via leucine-zipper domain); the interaction promotes CREB3 degradation. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in intestin, testis, heart and kidney, weakly in brain adipose, colon, liver, lung and skeletal. {ECO:0000269|PubMed:18391022}. +P56931 E2F2_MOUSE Transcription factor E2F2 (E2F-2) 443 48,499 Chain (1); DNA binding (1); Motif (1); Region (5) FUNCTION: Transcription activator that binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. The DRTF1/E2F complex functions in the control of cell-cycle progression from g1 to s phase. E2F2 binds specifically to RB1 in a cell-cycle dependent manner. PTM: Phosphorylated by CDK2 and cyclin A-CDK2 in the S-phase. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Component of the DRTF1/E2F transcription factor complex. Forms heterodimers with DP family members. The E2F2 complex binds specifically hypophosphorylated retinoblastoma protein RB1. During the cell cycle, RB1 becomes phosphorylated in mid-to-late G1 phase, detaches from the DRTF1/E2F complex, rendering E2F transcriptionally active. Viral oncoproteins, notably E1A, T-antigen and HPV E7, are capable of sequestering RB protein, thus releasing the active complex. Binds EAPP. +O35261 E2F3_MOUSE Transcription factor E2F3 (E2F-3) 457 48,757 Chain (1); Compositional bias (2); DNA binding (1); Motif (1); Region (5); Sequence conflict (2) FUNCTION: Transcription activator that binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. The DRTF1/E2F complex functions in the control of cell-cycle progression from G1 to S phase. E2F3 binds specifically to RB1 in a cell-cycle dependent manner. Inhibits adipogenesis, probably through the repression of CEBPA binding to its target gene promoters (PubMed:20176812). {ECO:0000269|PubMed:20176812}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Component of the DRTF1/E2F transcription factor complex. Binds cooperatively with TFDP1/Dp-1 to E2F sites. Interacts with retinoblastoma protein RB1 and related proteins (such as RBL1) that inhibit the E2F transactivation domain. Binds EAPP. {ECO:0000269|PubMed:15716352}. +Q9JM58 CRLF1_MOUSE Cytokine receptor-like factor 1 (Cytokine receptor-like molecule 3) (CRLM-3) (Cytokine-like factor 1) (CLF-1) (Novel cytokine receptor 6) (NR6) 425 46,662 Chain (1); Disulfide bond (2); Domain (3); Glycosylation (6); Modified residue (1); Motif (1); Signal peptide (1) FUNCTION: Cytokine receptor subunit, possibly playing a regulatory role in the immune system and during fetal development. May be involved in nervous system development (By similarity). Plays an essential role in the initiation and/or maintenance of suckling in neonatal mice. {ECO:0000250, ECO:0000269|PubMed:10359701}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Forms covalently linked di- and tetramers. Forms a heteromeric complex with cardiotrophin-like cytokine (CLC); the CRLF1/CLC complex is a ligand for the ciliary neurotrophic factor receptor (CNTFR) (By similarity). {ECO:0000250}. DOMAIN: The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding. TISSUE SPECIFICITY: Widely expressed in the embryo. Not detected in the brain of adult mice. {ECO:0000269|PubMed:10359701}. +Q8CII9 CRLF2_MOUSE Cytokine receptor-like factor 2 (Cytokine receptor-like molecule 2) (CRLM-2) (Thymic stromal lymphopoietin protein receptor) (TSLP receptor) (Type I cytokine receptor delta 1) 359 37,762 Alternative sequence (5); Beta strand (16); Chain (1); Disulfide bond (3); Domain (1); Glycosylation (2); Helix (3); Motif (2); Sequence conflict (10); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 233 253 Helical. {ECO:0000255}. TOPO_DOM 20 232 Extracellular. {ECO:0000255}.; TOPO_DOM 254 359 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for thymic stromal lymphopoietin (TSLP). Forms a functional complex with TSLP and IL7R which is capable of stimulating cell proliferation through activation of STAT3 and STAT5. Also activates JAK2. Implicated in the development of the hematopoietic system. {ECO:0000269|PubMed:10974032}. SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Isoform 3: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Isoform 2: Secreted. SUBUNIT: The TSLP receptor is a heterodimer of CRLF2 and IL7R. Binding of TSLP to CRLF2/TSLPR is a mechanistic prerequisite for recruitment of IL7R to the high-affinity ternary complex. {ECO:0000269|PubMed:24632570}. DOMAIN: The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.; DOMAIN: The box 1 motif is required for JAK interaction and/or activation. TISSUE SPECIFICITY: High level of expression in liver, lung and testis. Also expressed in heart, brain, spleen, thymus and bone marrow. Highly expressed in progenitors and myeloid cells. Isoform 2 is expressed in primary hemotopoietic cells. +P63154 CRNL1_MOUSE Crooked neck-like protein 1 (Crooked neck homolog) 690 83,416 Chain (1); Compositional bias (1); Modified residue (2); Motif (1); Region (1); Repeat (16) FUNCTION: Involved in pre-mRNA splicing process. {ECO:0000250|UniProtKB:Q9BZJ0}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BZJ0}. Nucleus speckle {ECO:0000250|UniProtKB:Q9BZJ0}. Note=Colocalizes with core spliceosomal snRNP proteins. {ECO:0000250|UniProtKB:Q9BZJ0}. SUBUNIT: Identified in the spliceosome C complex. Present in a spliceosome complex assembled in vitro containing CRNKL1, HPRP8BP and SNRPB2 (By similarity). Interacts with PPIL2 (via the PPIase cyclophilin-type domain); they may form a trimeric complex with HSP90 (PubMed:15189447). {ECO:0000250|UniProtKB:Q9BZJ0, ECO:0000269|PubMed:15189447}. +Q80YA8 CRUM2_MOUSE Protein crumbs homolog 2 (crumbs2) (Crumbs-like protein 2) 1282 134,760 Chain (1); Disulfide bond (48); Domain (18); Glycosylation (13); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1222 1242 Helical. {ECO:0000255}. TOPO_DOM 36 1221 Extracellular. {ECO:0000305}.; TOPO_DOM 1243 1282 Cytoplasmic. {ECO:0000305}. FUNCTION: Apical polarity protein that plays a central role during the epithelial-to-mesenchymal transition (EMT) at gastrulation, when newly specified mesodermal cells move inside the embryo (PubMed:26496195, PubMed:27870829). Acts by promoting cell ingression, the process by which cells leave the epithelial epiblast and move inside the embryo to form a new tissue layer (PubMed:27870829). The anisotropic distribution of CRB2 and MYH10/myosin-IIB at cell edges define which cells will ingress: cells with high apical CRB2 are probably extruded from the epiblast by neighboring cells with high levels of apical MYH10/myosin-IIB (PubMed:27870829). Also required for maintenance of the apical polarity complex during development of the cortex. {ECO:0000269|PubMed:26496195, ECO:0000269|PubMed:26802325, ECO:0000269|PubMed:27870829}. PTM: O-glucosylated by POGLUT1 at Ser-271; consists of an O-glucose trisaccharide, in which the O-glucose is elongated by the addition of two xylose residues (PubMed:26496195). O-glucosylation is required for localization at the plasma membrane (PubMed:26496195). {ECO:0000269|PubMed:26496195}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:26496195, ECO:0000269|PubMed:27870829}; Single-pass type I membrane protein {ECO:0000255}. Note=O-glucosylation is required for localization at the apical plasma membrane (PubMed:26496195). Distributed in a complex anisotropic pattern on apical cell edges: the level of CRB2 on a cell edge is inversely correlated with the level of MYH10/myosin-IIB (PubMed:27870829). {ECO:0000269|PubMed:26496195, ECO:0000269|PubMed:27870829}. TISSUE SPECIFICITY: In the adult eye, strongly expressed in the outer nuclear layer, containing the cell bodies of the photoreceptor cells, and in the inner nuclear layer, containing the cell bodies of the horizontal, bipolar, amacrine, and Mueller glial cells (PubMed:15851977). Also expressed in some cells in the ganglion cell layer (or may be displaced amacrine cells rather than ganglion cells) (PubMed:15851977). {ECO:0000269|PubMed:15851977}. +Q6DIA7 CS057_MOUSE Uncharacterized protein C19orf57 homolog 600 64,421 Alternative sequence (1); Chain (1); Modified residue (4); Sequence conflict (2) +D3Z070 CS081_MOUSE Putative uncharacterized protein C19orf81 homolog 196 22,145 Chain (1); Frameshift (1) +H3BKT1 CS084_MOUSE Uncharacterized protein C19orf84 homolog 185 19,979 Chain (1); Compositional bias (1) +P56564 EAA1_MOUSE Excitatory amino acid transporter 1 (Glial high affinity glutamate transporter) (High-affinity neuronal glutamate transporter) (GluT-1) (Sodium-dependent glutamate/aspartate transporter 1) (GLAST-1) (Solute carrier family 1 member 3) 543 59,622 Binding site (3); Chain (1); Compositional bias (1); Glycosylation (2); Intramembrane (2); Metal binding (5); Modified residue (1); Region (2); Topological domain (11); Transmembrane (8) INTRAMEM 346 376 Discontinuously helical. {ECO:0000250|UniProtKB:P43003}.; INTRAMEM 426 459 Discontinuously helical. {ECO:0000250|UniProtKB:P43003}. TRANSMEM 48 68 Helical; Name=1. {ECO:0000250|UniProtKB:P43003}.; TRANSMEM 87 108 Helical; Name=2. {ECO:0000250|UniProtKB:P43003}.; TRANSMEM 123 145 Helical; Name=3. {ECO:0000250|UniProtKB:P43003}.; TRANSMEM 237 260 Helical; Name=4. {ECO:0000250|UniProtKB:P43003}.; TRANSMEM 270 297 Helical; Name=5. {ECO:0000250|UniProtKB:P43003}.; TRANSMEM 319 340 Helical; Name=6. {ECO:0000250|UniProtKB:P43003}.; TRANSMEM 386 412 Helical; Name=7. {ECO:0000250|UniProtKB:P43003}.; TRANSMEM 473 494 Helical; Name=8. {ECO:0000250|UniProtKB:P43003}. TOPO_DOM 1 47 Cytoplasmic. {ECO:0000250|UniProtKB:P43003}.; TOPO_DOM 69 86 Extracellular. {ECO:0000250|UniProtKB:P43003}.; TOPO_DOM 109 122 Cytoplasmic. {ECO:0000250|UniProtKB:P43003}.; TOPO_DOM 146 236 Extracellular. {ECO:0000250|UniProtKB:P43003}.; TOPO_DOM 261 269 Cytoplasmic. {ECO:0000250|UniProtKB:P43003}.; TOPO_DOM 298 318 Extracellular. {ECO:0000250|UniProtKB:P43003}.; TOPO_DOM 341 345 Cytoplasmic. {ECO:0000250|UniProtKB:P43003}.; TOPO_DOM 377 385 Cytoplasmic. {ECO:0000250|UniProtKB:P43003}.; TOPO_DOM 413 425 Extracellular. {ECO:0000250|UniProtKB:P43003}.; TOPO_DOM 460 472 Extracellular. {ECO:0000250|UniProtKB:P43003}.; TOPO_DOM 495 543 Cytoplasmic. {ECO:0000250|UniProtKB:P43003}. FUNCTION: Sodium-dependent, high-affinity amino acid transporter that mediates the uptake of L-glutamate and also L-aspartate and D-aspartate (PubMed:7903437, PubMed:28032905). Functions as a symporter that transports one amino acid molecule together with two or three Na(+) ions and one proton, in parallel with the counter-transport of one K(+) ion (By similarity). Plays a redundant role in the rapid removal of released glutamate from the synaptic cleft, which is essential for terminating the postsynaptic action of glutamate (PubMed:15363892, PubMed:15390100,PubMed:16880397). {ECO:0000250|UniProtKB:O57321, ECO:0000269|PubMed:15363892, ECO:0000269|PubMed:15390100, ECO:0000269|PubMed:16880397, ECO:0000269|PubMed:28032905, ECO:0000269|PubMed:7903437}. PTM: Glycosylated. {ECO:0000269|PubMed:19656770}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28032905, ECO:0000269|PubMed:7903437}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:P43003}. DOMAIN: Contains eight transmembrane regions plus two helical hairpins that dip into the membrane. These helical hairpin structures play an important role in the transport process. The first enters the membrane from the cytoplasmic side, the second one from the extracellular side. During the transport cycle, the regions involved in amino acid transport, and especially the helical hairpins, move vertically by about 15-18 Angstroms, alternating between exposure to the aqueous phase and reinsertion in the lipid bilayer. In contrast, the regions involved in trimerization do not move. {ECO:0000250|UniProtKB:P43003}. TISSUE SPECIFICITY: Detected in brain, in Bergmann glia arborising into the molecular layer of the cerebellum (at protein level) (PubMed:15363892). Localized in brain and is highly enriched in the Purkinje cell layer in cerebellum. Intermediate level in lung, low level in spleen, skeletal muscle and testis. {ECO:0000269|PubMed:7903437}. +Q91W50 CSDE1_MOUSE Cold shock domain-containing protein E1 798 88,791 Chain (1); Cross-link (1); Domain (9); Modified residue (6) FUNCTION: RNA-binding protein. May be involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Component of a multi subunit autoregulatory ribonucleoprotein complex (ARC), at least composed of IGF2BP1, PABPC1 and CSDE1. Interacts with STRAP. Part of a complex associated with the FOS mCRD domain and consisting of PABPC1, PAIP1, HNRPD and SYNCRIP. The interaction with PABPC1 is direct and RNA-independent (By similarity). {ECO:0000250}. +Q91YQ3 CSDC2_MOUSE Cold shock domain-containing protein C2 (RNA-binding protein PIPPin) 154 16,853 Chain (1); Domain (1); Modified residue (1); Sequence conflict (1) FUNCTION: RNA-binding factor which binds specifically to the very 3'-UTR ends of both histone H1 and H3.3 mRNAs, encompassing the polyadenylation signal. Might play a central role in the negative regulation of histone variant synthesis in the developing brain (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=PIPPin-RNA complexes are located to the nucleus. {ECO:0000250}. +Q9D4C5 EAF1_MOUSE ELL-associated factor 1 268 28,967 Chain (1); Compositional bias (2); Modified residue (1); Region (1) FUNCTION: Acts as a transcriptional transactivator of ELL and ELL2 elongation activities. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q96JC9}. Nucleus, Cajal body {ECO:0000250|UniProtKB:Q96JC9}. SUBUNIT: Component of the super elongation complex (SEC), at least composed of EAF1, EAF2, CDK9, MLLT3/AF9, AFF (AFF1 or AFF4), the P-TEFb complex and ELL (ELL, ELL2 or ELL3). Interacts with ELL and ELL2 (By similarity). {ECO:0000250}. +P07141 CSF1_MOUSE Macrophage colony-stimulating factor 1 (CSF-1) (MCSF) [Cleaved into: Processed macrophage colony-stimulating factor 1] 552 60,649 Alternative sequence (1); Beta strand (2); Chain (2); Disulfide bond (6); Glycosylation (3); Helix (7); Natural variant (2); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (3) TRANSMEM 493 515 Helical. {ECO:0000255}. TOPO_DOM 33 492 Extracellular. {ECO:0000255}.; TOPO_DOM 516 552 Cytoplasmic. {ECO:0000255}. FUNCTION: Cytokine that plays an essential role in the regulation of survival, proliferation and differentiation of hematopoietic precursor cells, especially mononuclear phagocytes, such as macrophages and monocytes. Promotes the release of proinflammatory chemokines, and thereby plays an important role in innate immunity and in inflammatory processes. Plays an important role in the regulation of osteoclast proliferation and differentiation, the regulation of bone resorption, and is required for normal bone development. Required for normal male and female fertility. Promotes reorganization of the actin cytoskeleton, regulates formation of membrane ruffles, cell adhesion and cell migration. Plays a role in lipoprotein clearance. PTM: N-glycosylated. The predominant soluble form is a chondroitin sulfate-containing proteoglycan. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: Processed macrophage colony-stimulating factor 1: Secreted, extracellular space {ECO:0000250}. SUBUNIT: Homodimer or heterodimer; disulfide-linked. Interacts with CSF1R. {ECO:0000269|PubMed:19017797}. DISEASE: Note=A defect in Csf1 is the cause of osteopetrosis. Osteopetrotic mice (op/op) are severely deficient in mature macrophages and osteoclasts, display failed tooth eruption, and have a restricted capacity for bone remodeling. {ECO:0000269|PubMed:2188141}. +Q00941 CSF2R_MOUSE Granulocyte-macrophage colony-stimulating factor receptor subunit alpha (GM-CSF-R-alpha) (GMCSFR-alpha) (GMR-alpha) (CD antigen CD116) 388 41,769 Chain (1); Domain (1); Glycosylation (6); Motif (2); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 328 348 Helical. {ECO:0000255}. TOPO_DOM 30 327 Extracellular. {ECO:0000255}.; TOPO_DOM 349 388 Cytoplasmic. {ECO:0000255}. FUNCTION: Low affinity receptor for granulocyte-macrophage colony-stimulating factor. Transduces a signal that results in the proliferation, differentiation, and functional activation of hematopoietic cells. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Heterodimer of an alpha and a beta subunit. The beta subunit is common to the IL3, IL5 and GM-CSF receptors. The signaling GM-CSF receptor complex is a dodecamer of two head-to-head hexamers of two alpha, two beta, and two ligand subunits (By similarity). {ECO:0000250}. DOMAIN: The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.; DOMAIN: The box 1 motif is required for JAK interaction and/or activation. +P01587 CSF2_MOUSE Granulocyte-macrophage colony-stimulating factor (GM-CSF) (Colony-stimulating factor) (CSF) 141 16,091 Chain (1); Disulfide bond (2); Erroneous initiation (1); Glycosylation (4); Mutagenesis (5); Sequence conflict (9); Signal peptide (1) FUNCTION: Cytokine that stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Monomer. The signaling GM-CSF receptor complex is a dodecamer of two head-to-head hexamers of two alpha, two beta, and two ligand subunits (By similarity). {ECO:0000250}. +Q60737 CSK21_MOUSE Casein kinase II subunit alpha (CK II alpha) (EC 2.7.11.1) 391 45,134 Active site (1); Binding site (1); Chain (1); Domain (1); Modified residue (4); Nucleotide binding (1); Region (1); Sequence conflict (5) FUNCTION: Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response. During mitosis, functions as a component of the p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in response to spindle damage. Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation. Can also negatively regulate apoptosis. Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3. Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8. Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV. Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, SRF, MAX, JUN, FOS, MYC and MYB. Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function. Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1. Acts as an ectokinase that phosphorylates several extracellular proteins. Phosphorylates PML at 'Ser-565' and primes it for ubiquitin-mediated degradation. Plays an important role in the circadian clock function by phosphorylating ARNTL/BMAL1 at 'Ser-90' which is pivotal for its interaction with CLOCK and which controls CLOCK nuclear entry. Phosphorylates CCAR2 at 'Thr-454' (By similarity). {ECO:0000250|UniProtKB:P68400, ECO:0000269|PubMed:10806215, ECO:0000269|PubMed:18467326}. PTM: Phosphorylated at Thr-344, Thr-360, Ser-362 and Ser-370 by CDK1 in prophase and metaphase and dephosphorylated during anaphase. Phosphorylation does not directly affect casein kinase 2 activity, but may contribute to its regulation by forming binding sites for interacting proteins and/or targeting it to different compartments (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P68400}. SUBUNIT: Heterotetramer composed of two catalytic subunits (alpha chain and/or alpha' chain) and two regulatory subunits (beta chains). The tetramer can exist as a combination of 2 alpha/2 beta, 2 alpha'/2 beta or 1 alpha/1 alpha'/2 beta subunits. Also part of a CK2-SPT16-SSRP1 complex composed of SSRP1, SUPT16H, CSNK2A1, CSNK2A2 and CSNK2B, which forms following UV irradiation (By similarity). Interacts with RNPS1 (By similarity). Interacts with SNAI1 (PubMed:19923321). Interacts with PML and CCAR2 (By similarity). {ECO:0000250|UniProtKB:P68400, ECO:0000269|PubMed:19923321}. +Q5BU09 EAPP_MOUSE E2F-associated phosphoprotein (EAPP) 281 32,494 Alternative sequence (1); Chain (1); Compositional bias (1); Modified residue (5); Sequence conflict (1) FUNCTION: May play an important role in the fine-tuning of both major E2F1 activities, the regulation of the cell-cycle and the induction of apoptosis. Promotes S-phase entry, and inhibits p14(ARP) expression (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Interacts with E2F1. The C-terminal half binds the N-terminal of E2F1. Also interacts with E2F2 and E2F3, but not E2F4. {ECO:0000269|PubMed:15716352}. +P41241 CSK_MOUSE Tyrosine-protein kinase CSK (EC 2.7.10.2) (C-Src kinase) (Protein-tyrosine kinase MPK-2) (p50CSK) 450 50,716 Active site (1); Beta strand (5); Binding site (1); Chain (1); Domain (3); Helix (1); Initiator methionine (1); Modified residue (5); Nucleotide binding (1); Region (1); Sequence conflict (3) FUNCTION: Non-receptor tyrosine-protein kinase that plays an important role in the regulation of cell growth, differentiation, migration and immune response. Phosphorylates tyrosine residues located in the C-terminal tails of Src-family kinases (SFKs) including LCK, SRC, HCK, FYN, LYN, CSK or YES1. Upon tail phosphorylation, Src-family members engage in intramolecular interactions between the phosphotyrosine tail and the SH2 domain that result in an inactive conformation. To inhibit SFKs, CSK is recruited to the plasma membrane via binding to transmembrane proteins or adapter proteins located near the plasma membrane. Suppresses signaling by various surface receptors, including T-cell receptor (TCR) and B-cell receptor (BCR) by phosphorylating and maintaining inactive several positive effectors such as FYN or LCK (By similarity). {ECO:0000250}. PTM: Phosphorylated at Ser-364 by PKA, leading to increased activity. Autophosphorylated (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16166631}. Cell membrane {ECO:0000269|PubMed:16166631}. Note=Mainly cytoplasmic, also present in lipid rafts. SUBUNIT: Homodimer (via SH3-domain) (By similarity). Interacts with PTPN22 (PubMed:8890164). Interacts with phosphorylated SIT1, PAG1, LIME1 and TGFB1I1; these interactions serve to recruit CSK to the membrane where it can phosphorylate and inhibit Src-family kinases (PubMed:9858471, PubMed:12218089, PubMed:12612075, PubMed:16166631). Interacts with SRCIN1 (By similarity). Interacts with RHOH (By similarity). Interacts (via SH2 domain) with SCIMP (By similarity). Interacts (via SH2 domain) with PRAG1 (when phosphorylated at 'Tyr-391'); this interaction prevents translocation of CSK from the cytoplasm to the membrane leading to increased activity of CSK (By similarity). {ECO:0000250|UniProtKB:P32577, ECO:0000250|UniProtKB:P41240, ECO:0000269|PubMed:12218089, ECO:0000269|PubMed:12612075, ECO:0000269|PubMed:16166631, ECO:0000269|PubMed:8890164, ECO:0000269|PubMed:9858471}. DOMAIN: The architecture of this protein is similar to that of Src-family kinases (SFKs) with one N-terminal SH3 domain, one SH2 domain, and a C-terminal kinase domain. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous, but most abundant in thymus and spleen, as well as in neonatal brain. +Q923L3 CSMD1_MOUSE CUB and sushi domain-containing protein 1 (CUB and sushi multiple domains protein 1) 3564 387,862 Alternative sequence (2); Chain (1); Disulfide bond (70); Domain (42); Erroneous initiation (1); Glycosylation (40); Sequence conflict (8); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 3488 3508 Helical. {ECO:0000255}. TOPO_DOM 30 3487 Extracellular. {ECO:0000255}.; TOPO_DOM 3509 3564 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +O88545 CSN6_MOUSE COP9 signalosome complex subunit 6 (SGN6) (Signalosome subunit 6) (JAB1-containing signalosome subunit 6) 324 35,880 Chain (1); Domain (1) FUNCTION: Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. Has some glucocorticoid receptor-responsive activity (By similarity). Stabilizes COP1 through reducing COP1 auto-ubiquitination and decelerating COP1 turnover rate, hence regulates the ubiquitination of COP1 targets, including SFN (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Component of the CSN complex, composed of COPS1/GPS1, COPS2, COPS3, COPS4, COPS5, COPS6, COPS7 (COPS7A or COPS7B), COPS8 and COPS9 (PubMed:9707402). In the complex, it probably interacts directly with COPS2, COPS4, COPS5, COPS7 (COPS7A or COPS7B) and COPS9. Interacts with the translation initiation factor EIF3S6. Interacts weakly with RBX1. Directly interacts with COP1 and 14-3-3 protein sigma/SFN (By similarity). {ECO:0000250|UniProtKB:Q7L5N1, ECO:0000269|PubMed:9707402}. +P70245 EBP_MOUSE 3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase (EC 5.3.3.5) (Cholestenol Delta-isomerase) (Delta(8)-Delta(7) sterol isomerase) (D8-D7 sterol isomerase) (Emopamil-binding protein) 230 26,215 Chain (1); Domain (1); Initiator methionine (1); Modified residue (1); Natural variant (1); Transmembrane (4) TRANSMEM 29 49 Helical. {ECO:0000255}.; TRANSMEM 66 86 Helical. {ECO:0000255}.; TRANSMEM 121 141 Helical. {ECO:0000255}.; TRANSMEM 185 205 Helical. {ECO:0000255}. Steroid biosynthesis; cholesterol biosynthesis. FUNCTION: Catalyzes the conversion of Delta(8)-sterols to their corresponding Delta(7)-isomers. {ECO:0000269|PubMed:8798407}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q15125}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q15125}. Nucleus envelope {ECO:0000250|UniProtKB:Q15125}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q15125}. Note=During interphase, detected on the endoplasmic reticulum and the nuclear envelope. During mitosis, detected on cytoplasmic vesicles. {ECO:0000250|UniProtKB:Q15125}. DISEASE: Note=Defects in Ebp are a cause of 'Tattered' (Td) which is an X-linked, semidominant mouse mutation associated with prenatal male lethality. Heterozygous females are small and at 4 to 5 days of age develop patches of hyperkeratotic skin where no hair grows, resulting in a striping of the coat in adults. Craniofacial anomalies and twisted toes have also been observed in some affected females. +P97314 CSRP2_MOUSE Cysteine and glycine-rich protein 2 (Cysteine-rich protein 2) (CRP2) (Double LIM protein 1) (DLP-1) 193 20,926 Chain (1); Compositional bias (2); Cross-link (1); Domain (2); Modified residue (5); Motif (1); Sequence conflict (1) FUNCTION: Drastically down-regulated in response to PDGF-BB or cell injury, that promote smooth muscle cell proliferation and dedifferentiation. Seems to play a role in the development of the embryonic vascular system (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with KAT14. The LIM domain 1 is necessary and sufficient for this interaction (By similarity). Interacts with GLRX3. {ECO:0000250, ECO:0000269|PubMed:18258855}. +Q9EPL2 CSTN1_MOUSE Calsyntenin-1 (Alcadein-alpha) (Alc-alpha) [Cleaved into: Soluble Alc-alpha (SAlc-alpha); CTF1-alpha (C-terminal fragment 1-alpha)] 979 108,900 Alternative sequence (1); Chain (3); Compositional bias (1); Domain (2); Erroneous initiation (1); Glycosylation (3); Mutagenesis (7); Signal peptide (1); Site (2); Topological domain (2); Transmembrane (1) TRANSMEM 860 880 Helical. {ECO:0000255}. TOPO_DOM 29 859 Extracellular. {ECO:0000255}.; TOPO_DOM 881 979 Cytoplasmic. {ECO:0000255}. FUNCTION: Induces KLC1 association with vesicles and functions as a cargo in axonal anterograde transport. Complex formation with APBA2 and APP, stabilizes APP metabolism and enhances APBA2-mediated suppression of beta-APP40 secretion, due to the retardation of intracellular APP maturation. In complex with APBA2 and C99, a C-terminal APP fragment, abolishes C99 interaction with PSEN1 and thus APP C99 cleavage by gamma-secretase, most probably through stabilization of the direct interaction between APBA2 and APP. As intracellular fragment AlcICD, suppresses APBB1-dependent transactivation stimulated by APP C-terminal intracellular fragment (AICD), most probably by competing with AICD for APBB1-binding. May modulate calcium-mediated postsynaptic signals. {ECO:0000269|PubMed:12972431, ECO:0000269|PubMed:17332754}. PTM: Proteolytically processed under normal cellular conditions. A primary zeta-cleavage generates a large extracellular (soluble) N-terminal domain (sAlc) and a short C-terminal transmembrane fragment (CTF1). A secondary cleavage catalyzed by presenilin gamma-secretase within the transmembrane domain releases the beta-Alc-alpha chain in the extracellular milieu and produces an intracellular fragment (AlcICD). Beta-Alc-alpha secretion is largely dependent upon PSEN1 and PSEN2. This processing is strongly suppressed in the tripartite complex formed with APBA2 and APP, which seems to prevent the association with PSEN1. {ECO:0000269|PubMed:11161476, ECO:0000269|PubMed:15037614}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein. Golgi apparatus membrane. Cell projection. Cell junction, synapse, postsynaptic cell membrane; Single-pass type I membrane protein. Nucleus {ECO:0000250}. Note=Neurite tips. Localized in the postsynaptic membrane of both excitatory and inhibitory synapses. The AlcICD fragment is translocated to the nucleus upon interaction with APBB1 (By similarity). {ECO:0000250}. SUBUNIT: Directly interacts with APBA2. Forms a tripartite complex with APBA2 and APP. The CTF1 chain interacts with PSEN1. The intracellular fragment AlcICD interacts with APBB1; this interaction stabilizes AlcICD metabolism. Interacts with KLC1 and APBB1. {ECO:0000269|PubMed:12972431, ECO:0000269|PubMed:16760430, ECO:0000269|PubMed:17332754}. DOMAIN: The cytoplasmic domain is involved in interaction with APBA2, as well as the binding of synaptic Ca(2+). {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in the brain (at protein level), with over 90% of the neurons expressing detectable amounts. In the brain, relatively high levels in the cerebral cortex, striatum, hippocampus and thalamus. Moderate levels in the cerebellum. Low levels in the olfactory bulb, midbrain and pons (at protein level). Not detected in Purkinje cells. Expressed at low levels in the lung (at protein level). At the mRNA level, weakly detected in the kidney, lung, skeletal muscle, heart and testis. Not expressed in the sciatic nerve fiber. {ECO:0000269|PubMed:12498782, ECO:0000269|PubMed:12972431, ECO:0000269|PubMed:16760430}. +Q9DAN8 CST12_MOUSE Cystatin-12 (Cystatin TE-1) 128 15,036 Chain (1); Disulfide bond (2); Glycosylation (1); Signal peptide (1) FUNCTION: May play a specialized role in spermatogenesis. {ECO:0000269|PubMed:12444065}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Located at the very proximal caput epididymis (at protein level). Expressed in epididymis, Sertoli cells and testis. Also found to be weakly expressed in ovary and prostate. {ECO:0000269|PubMed:12444065}. +Q80ZN5 CST13_MOUSE Cystatin-13 (Cystatin-T) 141 16,825 Chain (1); Disulfide bond (2); Region (1); Sequence conflict (1); Signal peptide (1); Site (1) FUNCTION: May perform a specialized role during sperm development and maturation. {ECO:0000303|PubMed:15645076}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:15645076}. Note=According to PubMed:15645076 it is cytoplasmic. TISSUE SPECIFICITY: Expressed exclusively in testis. Found in spermatagonia, spermatocytes, round spermatids, elongating spermatids and spermatozoa. {ECO:0000269|PubMed:15645076}. +Q3UY34 CSTOS_MOUSE Protein CUSTOS 256 27,631 Chain (1); Compositional bias (2); Modified residue (3); Motif (1) FUNCTION: Plays a role in the regulation of Wnt signaling pathway during early development. {ECO:0000250|UniProtKB:A9C3N6}. SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000250|UniProtKB:A9C3N6}. +Q99LC2 CSTF1_MOUSE Cleavage stimulation factor subunit 1 (CF-1 50 kDa subunit) (Cleavage stimulation factor 50 kDa subunit) (CSTF 50 kDa subunit) (CstF-50) 431 48,382 Chain (1); Frameshift (1); Repeat (6) FUNCTION: One of the multiple factors required for polyadenylation and 3'-end cleavage of mammalian pre-mRNAs. May be responsible for the interaction of CSTF with other factors to form a stable complex on the pre-mRNA (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Homodimer. The CSTF complex is composed of CSTF1 (50 kDa subunit), CSTF2 (64 kDa subunit) and CSTF3 (77 kDa subunit). Interacts directly with CSTF3. Interacts with BARD1 (By similarity). {ECO:0000250}. DOMAIN: The WD6 domain is required for interaction with BARD1. WD domains are responsible for interaction with CSTF3 (By similarity). {ECO:0000250}.; DOMAIN: N-terminus mediates homodimerization. {ECO:0000250}. +P97426 ECP1_MOUSE Eosinophil cationic protein 1 (ECP 1) (EC 3.1.27.-) (Eosinophil secondary granule ribonuclease 1) (EAR-1) (Ribonuclease 3-1) (RNase 3-1) 155 17,296 Active site (2); Binding site (1); Chain (1); Disulfide bond (4); Glycosylation (4); Region (1); Signal peptide (1) FUNCTION: Cytotoxin and helminthotoxin with ribonuclease activity. Possesses a wide variety of biological activities (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasmic granule {ECO:0000250}. Note=Matrix of eosinophil's large specific granule. {ECO:0000250}. +Q07139 ECT2_MOUSE Protein ECT2 (Epithelial cell-transforming sequence 2 oncogene) 913 103,131 Alternative sequence (3); Beta strand (3); Chain (1); Cross-link (1); Domain (4); Helix (3); Initiator methionine (1); Modified residue (12); Motif (2); Sequence caution (1); Sequence conflict (5); Turn (2) FUNCTION: Guanine nucleotide exchange factor (GEF) that catalyzes the exchange of GDP for GTP. Promotes guanine nucleotide exchange on the Rho family members of small GTPases, like RHOA, RHOC, RAC1 and CDC42. Required for signal transduction pathways involved in the regulation of cytokinesis. Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Regulates the translocation of RHOA from the central spindle to the equatorial region. Plays a role in the control of mitotic spindle assembly; regulates the activation of CDC42 in metaphase for the process of spindle fibers attachment to kinetochores before chromosome congression. Involved in the regulation of epithelial cell polarity; participates in the formation of epithelial tight junctions in a polarity complex PARD3-PARD6-protein kinase PRKCQ-dependent manner. Plays a role in the regulation of neurite outgrowth. Inhibits phenobarbital (PB)-induced NR1I3 nuclear translocation. Stimulates the activity of RAC1 through its association with the oncogenic PARD6A-PRKCI complex in cancer cells, thereby acting to coordinately drive tumor cell proliferation and invasion. Also stimulates genotoxic stress-induced RHOB activity in breast cancer cells leading to their cell death. {ECO:0000269|PubMed:17904126, ECO:0000269|PubMed:21350944}. PTM: Phosphorylated by PLK1 in vitro. Hyperphosphorylated during the G2 phase of the cell cycle. Phosphorylation at Thr-373 occurs during the G2/M phase, relieves its auto-inhibition status and stimulates its GEF activity. Phosphorylation at Thr-444 in G2/M phase is required for subsequent binding with PLK1 and Rho exchange activation. Dephosphorylated at the time of cytokinesis. Phosphorylation at Thr-359 is required for its transformation activity in cancer cells (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17904126}. Cytoplasm {ECO:0000269|PubMed:17904126}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Cleavage furrow {ECO:0000250}. Midbody {ECO:0000250}. Cell junction {ECO:0000250}. Cell junction, tight junction {ECO:0000250}. Note=Sequestered within the nucleus during interphase. Dispersed throughout the cytoplasm upon breakdown of the nuclear envelope during mitosis. Colocalizes with the centralspindlin complex to the mitotic spindles during anaphase/metaphase, the cleavage furrow during telophase and at the midbody at the end of cytokinesis. Colocalized with RhoA at the midbody. Its subcellular localization to tight junction is increased by calcium. Localized predominantly in the cytoplasm of numerous carcinoma cells (By similarity). {ECO:0000250}. SUBUNIT: Homodimer. Homooligomer. Found in the centralspindlin complex. Interacts (Thr-359 phosphorylated form) with PARD6A; the interaction is observed in cancer cells. Interacts (Thr-359 phosphorylated form) with PRKCI; the interaction is observed in cancer cells. Interacts with PKP4; the interaction is observed at the midbody. Interacts with RACGAP1; the interaction is direct, occurs in a microtubule-dependent manner, is inhibited in metaphase by phosphorylation of ECT2 on Thr-373 and is stimulated in early anaphase by dephosphorylation of ECT2 probably on Thr-373 through CDK1 activity. Interacts with PLK1; the interaction is stimulated upon its phosphorylation on Thr-444. Associates with RACGAP1 at anaphase and during cytokinesis. Interacts with KIF23, PARD3, PARD6A, PARD6B and PRKCQ (By similarity). Interacts with NR1I3. {ECO:0000250, ECO:0000269|PubMed:17904126}. DOMAIN: The BRCT domain 1 and 2 are required for the intramolecular interaction, but not for the intermolecular oligomerization. The BRCT domains negatively inhibit its GEF activity in interphase cells. The same BRCT domains may act as a positive regulatory motif for the completion of cytokinesis after the breakdown of nuclear membrane during mitosis (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highest expression in testis. Also detectable in brain, kidney, liver and spleen. {ECO:0000269|PubMed:21350944}. +Q5SUQ9 CTC1_MOUSE CST complex subunit CTC1 (Alpha-accessory factor of 132 kDa) (AAF-132) (AAF132) (Conserved telomere maintenance component 1) 1212 134,028 Alternative sequence (2); Chain (1); Erroneous initiation (5); Sequence conflict (3) FUNCTION: Component of the CST complex proposed to act as a specialized replication factor promoting DNA replication under conditions of replication stress or natural replication barriers such as the telomere duplex. The CST complex binds single-stranded DNA with high affinity in a sequence-independent manner, while isolated subunits bind DNA with low affinity by themselves. Initially the CST complex has been proposed to protect telomeres from DNA degradation (PubMed:19854130). However, the CST complex has been shown to be involved in several aspects of telomere replication. The CST complex inhibits telomerase and is involved in telomere length homeostasis; it is proposed to bind to newly telomerase-synthesized 3' overhangs and to terminate telomerase action implicating the association with the ACD:POT1 complex thus interfering with its telomerase stimulation activity. The CST complex is also proposed to be involved in fill-in synthesis of the telomeric C-strand probably implicating recruitment and activation of DNA polymerase alpha. The CST complex facilitates recovery from many forms of exogenous DNA damage; seems to be involved in the re-initiation of DNA replication at repaired forks and/or dormant origins. Involved in telomere maintenance. Involved in genome stability (By similarity). May be in involved in telomeric C-strand fill-in during late S/G2 phase (PubMed:22748632). {ECO:0000250|UniProtKB:Q2NKJ3, ECO:0000269|PubMed:19854130, ECO:0000269|PubMed:22748632}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19119139, ECO:0000269|PubMed:19854130}. Chromosome, telomere {ECO:0000269|PubMed:19854130}. Note=A transmembrane region is predicted by sequence analysis tools (ESKW, MEMSAT and Phobius); however, given the telomeric localization of the protein, the relevance of the transmembrane region is unsure in vivo. {ECO:0000305}. SUBUNIT: Component of the CST complex, composed of TEN1/C17orf106, CTC1/C17orf68 and STN1; in the complex interacts directly with STN1. Interacts with ACD and POT1 (By similarity). {ECO:0000250|UniProtKB:Q2NKJ3, ECO:0000269|PubMed:19119139, ECO:0000269|PubMed:19854130}. +A2APF3 CTCFL_MOUSE Transcriptional repressor CTCFL (Brother of the regulator of imprinted sites) (CCCTC-binding factor) (CTCF paralog) (CTCF-like protein) 636 73,108 Alternative sequence (1); Chain (1); Sequence conflict (2); Zinc finger (11) FUNCTION: Testis-specific DNA binding protein responsible for insulator function, nuclear architecture and transcriptional control, which probably acts by recruiting epigenetic chromatin modifiers. Plays a key role in gene imprinting in male germline, by participating in the establishment of differential methylation at the IGF2/H19 imprinted control region (ICR). Directly binds the unmethylated H19 ICR and recruits the PRMT7 methyltransferase, leading to methylate histone H4 'Arg-3' to form H4R3sme2. This probably leads to recruit de novo DNA methyltransferases at these sites. Seems to act as tumor suppressor. In association with DNMT1 and DNMT3B, involved in activation of BAG1 gene expression by binding to its promoter. Required for dimethylation of H3 lysine 4 (H3K4me2) of MYC and BRCA1 promoters. {ECO:0000269|PubMed:17048991}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000269|PubMed:17048991}. SUBUNIT: Interacts with histones, PRMT7 and SETD1A. Interacts (via N-terminus) with BAG6/BAT3 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:17048991}. +Q61164 CTCF_MOUSE Transcriptional repressor CTCF (11-zinc finger protein) (CCCTC-binding factor) (CTCFL paralog) 736 83,745 Chain (1); Compositional bias (1); Cross-link (5); Modified residue (8); Mutagenesis (2); Sequence conflict (2); Zinc finger (11) FUNCTION: Chromatin binding factor that binds to DNA sequence specific sites. Involved in transcriptional regulation by binding to chromatin insulators and preventing interaction between promoter and nearby enhancers and silencers. Acts as transcriptional repressor binding to promoters of vertebrate MYC gene and BAG1 gene. Also binds to the PLK and PIM1 promoters. Acts as a transcriptional activator of APP. Regulates APOA1/C3/A4/A5 gene cluster and controls MHC class II gene expression. Plays an essential role in oocyte and preimplantation embryo development by activating or repressing transcription. Seems to act as tumor suppressor. Plays a critical role in the epigenetic regulation. Participates in the allele-specific gene expression at the imprinted IGF2/H19 gene locus. On the maternal allele, binding within the H19 imprinting control region (ICR) mediates maternally inherited higher-order chromatin conformation to restrict enhancer access to IGF2. Plays a critical role in gene silencing over considerable distances in the genome. Preferentially interacts with unmethylated DNA, preventing spreading of CpG methylation and maintaining methylation-free zones. Inversely, binding to target sites is prevented by CpG methylation. Plays a important role in chromatin remodeling. Can dimerize when it is bound to different DNA sequences, mediating long-range chromatin looping (By similarity). Mediates interchromosomal association between IGF2/H19 and WSB1/NF1 and may direct distant DNA segments to a common transcription factory. Causes local loss of histone acetylation and gain of histone methylation in the beta-globin locus, without affecting transcription. When bound to chromatin, it provides an anchor point for nucleosomes positioning. Seems to be essential for homologous X-chromosome pairing. May participate with Tsix in establishing a regulatable epigenetic switch for X chromosome inactivation. May play a role in preventing the propagation of stable methylation at the escape genes from X-inactivation. Involved in sister chromatid cohesion. Associates with both centromeres and chromosomal arms during metaphase and required for cohesin localization to CTCF sites. Regulates asynchronous replication of IGF2/H19. Plays a role in the recruitment of CENPE to the pericentromeric/centromeric regions of the chromosome during mitosis (By similarity). {ECO:0000250|UniProtKB:P49711, ECO:0000269|PubMed:11743158, ECO:0000269|PubMed:15669143, ECO:0000269|PubMed:16614224, ECO:0000269|PubMed:16951251, ECO:0000269|PubMed:17329968, ECO:0000269|PubMed:17952071, ECO:0000269|PubMed:18614575}. PTM: Sumoylated on Lys-74 and Lys-698; sumoylation of CTCF contributes to the repressive function of CTCF on the MYC P2 promoter. {ECO:0000269|PubMed:19029252}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000305|PubMed:8649389}. Chromosome {ECO:0000250|UniProtKB:P49711}. Chromosome, centromere {ECO:0000250|UniProtKB:P49711}. Note=May translocate to the nucleolus upon cell differentiation. Associates with both centromeres and chromosomal arms during metaphase. Associates with the H19 ICR in mitotic chromosomes. May be preferentially excluded from heterochromatin during interphase. {ECO:0000250|UniProtKB:P49711}. SUBUNIT: Interacts with CHD8 (PubMed:16949368). Interacts with LLPH (PubMed:26961175). Interacts with CENPE (By similarity). {ECO:0000250|UniProtKB:P49711, ECO:0000269|PubMed:16949368, ECO:0000269|PubMed:26961175}. +P56546 CTBP2_MOUSE C-terminal-binding protein 2 (CtBP2) 445 48,957 Active site (3); Alternative sequence (1); Binding site (3); Chain (1); Frameshift (1); Modified residue (2); Nucleotide binding (4); Sequence conflict (3) FUNCTION: Corepressor targeting diverse transcription regulators. Isoform 2 probably acts as a scaffold for specialized synapses (By similarity). Functions in brown adipose tissue (BAT) differentiation. {ECO:0000250, ECO:0000269|PubMed:18483224}. PTM: Phosphorylation by HIPK2 on Ser-428 induces proteasomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Cell junction, synapse {ECO:0000250}. SUBUNIT: Interacts with HIPK2 and PNN (By similarity). Interacts with the transcription factors ZNF217, BKLF, delta EF1/AREB6/ZEB, EVI-1 and Friend of GATA (FOG) via the consensus motif P-X-[DNS]-L-[STVA]. Interacts also with the C-terminus of adenovirus E1A protein. Can form a complex with BKLF on a CACCC-box oligonucleotide. Can form homodimers or heterodimers of CTBP1 and CTBP2. Interacts with NRIP1 and WIZ. Interacts with PRDM16; represses white adipose tissue (WAT)-specific genes expression. Interacts with MCRIP1 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P56545, ECO:0000269|PubMed:14736873, ECO:0000269|PubMed:16702210, ECO:0000269|PubMed:16940172, ECO:0000269|PubMed:18483224}. TISSUE SPECIFICITY: Found in all tissues except spleen and liver. +Q60753 CTF1_MOUSE Cardiotrophin-1 (CT-1) 203 21,509 Chain (1) FUNCTION: Induces cardiac myocyte hypertrophy in vitro. Binds to and activates the ILST/gp130 receptor. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle, liver, lung and kidney. Lower levels in testis and brain. No expression in spleen. +P09793 CTLA4_MOUSE Cytotoxic T-lymphocyte protein 4 (Cytotoxic T-lymphocyte-associated antigen 4) (CTLA-4) (CD antigen CD152) 223 24,993 Beta strand (11); Chain (1); Disulfide bond (3); Domain (1); Glycosylation (3); Helix (1); Modified residue (1); Region (3); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 162 182 Helical. {ECO:0000255}. TOPO_DOM 36 161 Extracellular. {ECO:0000255}.; TOPO_DOM 183 223 Cytoplasmic. {ECO:0000255}. FUNCTION: Inhibitory receptor acting as a major negative regulator of T-cell responses. The affinity of CTLA4 for its natural B7 family ligands, CD80 and CD86, is considerably stronger than the affinity of their cognate stimulatory coreceptor CD28. {ECO:0000250|UniProtKB:P16410}. PTM: N-glycosylation is important for dimerization. {ECO:0000250|UniProtKB:P16410}.; PTM: Phosphorylation at Tyr-201 prevents binding to the AP-2 adapter complex, blocks endocytosis, and leads to retention of CTLA4 on the cell surface. {ECO:0000250|UniProtKB:P16410}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P16410}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P16410}. Note=Exists primarily an intracellular antigen whose surface expression is tightly regulated by restricted trafficking to the cell surface and rapid internalisation;. {ECO:0000250|UniProtKB:P16410}. SUBUNIT: Homodimer; disulfide-linked. Binds to CD80/B7-1 and CD86/B7.2. Interacts with ICOSLG. {ECO:0000250|UniProtKB:P16410}. TISSUE SPECIFICITY: Widely expressed with highest levels in lymphoid tissues. {ECO:0000269|PubMed:10493833}. +P0CG14 CTF8A_MOUSE Chromosome transmission fidelity protein 8 homolog isoform 2 533 52,244 Chain (1); Compositional bias (2); Modified residue (4) FUNCTION: Potential tumor suppressor. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +Q8VHX2 EDAD_MOUSE Ectodysplasin-A receptor-associated adapter protein (EDAR-associated death domain protein) (Protein crinkled) 208 23,753 Chain (1); Domain (1); Mutagenesis (1); Sequence conflict (1) FUNCTION: Adapter protein that interacts with EDAR DEATH domain and couples the receptor to EDA signaling pathway during morphogenesis of ectodermal organs. Mediates the activation of NF-kappa-B (By similarity). {ECO:0000250, ECO:0000269|PubMed:11882293}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. SUBUNIT: Binds EDAR. Self-associates and binds TRAF1, TRAF2 and TRAF3 (By similarity). {ECO:0000250}. +Q9D1D6 CTHR1_MOUSE Collagen triple helix repeat-containing protein 1 245 26,460 Chain (1); Domain (1); Glycosylation (1); Sequence conflict (1); Signal peptide (1) FUNCTION: May act as a negative regulator of collagen matrix deposition. {ECO:0000250}. PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. +Q5RJI2 CTL5_MOUSE Choline transporter-like protein 5 (Solute carrier family 44 member 5) 710 81,429 Chain (1); Glycosylation (2); Topological domain (11); Transmembrane (10) TRANSMEM 33 53 Helical. {ECO:0000255}.; TRANSMEM 237 257 Helical. {ECO:0000255}.; TRANSMEM 261 281 Helical. {ECO:0000255}.; TRANSMEM 320 340 Helical. {ECO:0000255}.; TRANSMEM 346 366 Helical. {ECO:0000255}.; TRANSMEM 369 389 Helical. {ECO:0000255}.; TRANSMEM 455 475 Helical. {ECO:0000255}.; TRANSMEM 510 530 Helical. {ECO:0000255}.; TRANSMEM 605 625 Helical. {ECO:0000255}.; TRANSMEM 644 664 Helical. {ECO:0000255}. TOPO_DOM 1 32 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 54 236 Extracellular. {ECO:0000255}.; TOPO_DOM 258 260 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 282 319 Extracellular. {ECO:0000255}.; TOPO_DOM 341 345 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 367 368 Extracellular. {ECO:0000255}.; TOPO_DOM 390 454 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 476 509 Extracellular. {ECO:0000255}.; TOPO_DOM 531 604 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 626 643 Extracellular. {ECO:0000255}.; TOPO_DOM 665 710 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q925U4 EDEM1_MOUSE ER degradation-enhancing alpha-mannosidase-like protein 1 652 73,701 Chain (1); Glycosylation (4); Topological domain (2); Transmembrane (1) TRANSMEM 5 25 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 4 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 26 652 Lumenal. {ECO:0000255}. FUNCTION: Extracts misfolded glycoproteins, but not glycoproteins undergoing productive folding, from the calnexin cycle. It is directly involved in endoplasmic reticulum-associated degradation (ERAD) and targets misfolded glycoproteins for degradation in an N-glycan-independent manner, probably by forming a complex with SEL1L. It has low mannosidase activity, catalyzing mannose trimming from Man8GlcNAc2 to Man7GlcNAc2. {ECO:0000250|UniProtKB:Q92611, ECO:0000269|PubMed:11375934}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000305}. SUBUNIT: Interacts with DERL2 and DERL3. Binds to SEL1L (By similarity). Interacts with DNAJC10. {ECO:0000250, ECO:0000269|PubMed:18653895, ECO:0000269|PubMed:21329881}. +A2ARP9 CTSR2_MOUSE Cation channel sperm-associated protein 2 (CatSper2) 588 68,572 Chain (1); Compositional bias (1); Erroneous gene model prediction (1); Intramembrane (1); Sequence conflict (10); Topological domain (8); Transmembrane (6) INTRAMEM 281 301 Helical; Pore-forming. {ECO:0000255}. TRANSMEM 107 127 Helical; Name=Segment S1. {ECO:0000255}.; TRANSMEM 150 170 Helical; Name=Segment S2. {ECO:0000255}.; TRANSMEM 177 197 Helical; Name=Segment S3. {ECO:0000255}.; TRANSMEM 204 224 Helical; Name=Segment S4. {ECO:0000255}.; TRANSMEM 241 261 Helical; Name=Segment S5. {ECO:0000255}.; TRANSMEM 319 339 Helical; Name=Segment S6. {ECO:0000255}. TOPO_DOM 1 106 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 128 149 Extracellular. {ECO:0000255}.; TOPO_DOM 171 176 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 198 203 Extracellular. {ECO:0000255}.; TOPO_DOM 225 240 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 262 280 Extracellular. {ECO:0000255}.; TOPO_DOM 302 318 Extracellular. {ECO:0000255}.; TOPO_DOM 340 588 Cytoplasmic. {ECO:0000255}. FUNCTION: Voltage-gated calcium channel that plays a central role in sperm cell hyperactivation. Controls calcium entry to mediate the hyperactivated motility, a step needed for sperm motility which is essential late in the preparation of sperm for fertilization. Activated by intracellular alkalinization. {ECO:0000269|PubMed:14657366, ECO:0000269|PubMed:16036917, ECO:0000269|PubMed:17174296}. SUBCELLULAR LOCATION: Cell projection, cilium, flagellum membrane {ECO:0000269|PubMed:11675491}; Multi-pass membrane protein {ECO:0000269|PubMed:11675491}. Note=Specifically located in the principal piece of sperm tail. SUBUNIT: Heterotetramer; possibly composed of CATSPER1, CATSPER2, CATSPER3 and CATSPER4 (Potential). Interacts with Ca(v)3.3/CACNA1I, leading to suppress T-type calcium channel activity (By similarity). Component of the CatSper complex. {ECO:0000250, ECO:0000269|PubMed:21224844, ECO:0000305}. TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:11675491}. +Q62018 CTR9_MOUSE RNA polymerase-associated protein CTR9 homolog (SH2 domain-binding protein 1) (Tetratricopeptide repeat-containing, SH2-binding phosphoprotein of 150 kDa) (TPR-containing, SH2-binding phosphoprotein of 150 kDa) (p150TSP) 1173 133,408 Alternative sequence (4); Chain (1); Compositional bias (6); Modified residue (15); Repeat (16); Sequence caution (1); Sequence conflict (7) FUNCTION: Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and is involved in transcriptional elongation, acting both indepentently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1. PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B ubiquitination is proposed to be coupled to transcription. PAF1C is involved in mRNA 3' end formation probably through association with cleavage and poly(A) factors. Required for mono- and trimethylation on histone H3 'Lys-4' (H3K4me3) and dimethylation on histone H3 'Lys-79' (H3K4me3). Required for Hox gene transcription (By similarity). Required for the trimethylation of histone H3 'Lys-4' (H3K4me3) on genes involved in stem cell pluripotency; this function is synergistic with CXXC1 indicative for an involvement of the SET1 complex. Involved in transcriptional regulation of IL6-responsive genes and in JAK-STAT pathway; may regulate DNA-association of STAT3. {ECO:0000250, ECO:0000269|PubMed:17911113, ECO:0000269|PubMed:19345177}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:8636124}. SUBUNIT: Component of the PAF1 complex, which consists of CDC73, PAF1, LEO1, CTR9, RTF1 and WDR61. The PAF1 complex interacts with PHF5A (PubMed:27749823). Interacts with KMT2A/MLL1 (By similarity). Interacts with STAT3 (PubMed:17911113). Interacts with SETD5 (PubMed:27864380). {ECO:0000250|UniProtKB:Q6PD62, ECO:0000269|PubMed:17911113, ECO:0000269|PubMed:27749823, ECO:0000269|PubMed:27864380}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12465718}. +E9Q9F6 CTSRD_MOUSE Cation channel sperm-associated protein subunit delta (CatSper-delta) (CatSperdelta) (Transmembrane protein 146) 805 91,096 Alternative sequence (3); Chain (1); Erroneous gene model prediction (1); Erroneous initiation (2); Glycosylation (2); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 755 775 Helical. {ECO:0000255}. TOPO_DOM 17 754 Extracellular. {ECO:0000255}.; TOPO_DOM 776 805 Cytoplasmic. {ECO:0000255}. FUNCTION: Auxiliary component of the CatSper complex, a complex involved in sperm cell hyperactivation. Sperm cell hyperactivation is needed for sperm motility which is essential late in the preparation of sperm for fertilization. Required for CATSPER1 stability before intraflagellar transport and/or incorporation of the CatSper complex channel into the flagellar membrane. {ECO:0000269|PubMed:21224844}. SUBCELLULAR LOCATION: Cell projection, cilium, flagellum membrane {ECO:0000269|PubMed:21224844}; Single-pass type I membrane protein {ECO:0000269|PubMed:21224844}. Note=Specifically located in the principal piece of sperm tail. {ECO:0000269|PubMed:21224844}. SUBUNIT: Component of the CatSper complex. {ECO:0000269|PubMed:21224844}. TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:21224844}. +Q9CQP8 CTSRZ_MOUSE Cation channel sperm-associated protein subunit zeta (CatSper-zeta) (CatSperzeta) (Protein expressed in male leptotene and zygotene spermatocytes 622) (MLZ-622) (Testis-expressed protein 40) 194 22,741 Chain (1); Sequence conflict (3) FUNCTION: Auxiliary component of the CatSper complex, a complex involved in sperm cell hyperactivation (PubMed:28226241). Sperm cell hyperactivation is needed for sperm motility which is essential late in the preparation of sperm for fertilization (PubMed:28226241). Required for a distribution of the CatSper complex in linear quadrilateral nanodomains along the flagellum, maximizing fertilization inside the mammalian female reproductive tract (PubMed:28226241). {ECO:0000269|PubMed:28226241}. SUBCELLULAR LOCATION: Cell projection, cilium, flagellum membrane {ECO:0000269|PubMed:28226241}; Peripheral membrane protein {ECO:0000305}. Note=Specifically located in the principal piece of sperm tail (PubMed:28226241). Although it does not contain a transmembrane domain, localizes with the CatSper complex at the flagellum membrane (PubMed:28226241). {ECO:0000269|PubMed:28226241}. SUBUNIT: Component of the CatSper complex. {ECO:0000269|PubMed:28226241}. TISSUE SPECIFICITY: Testis-specific (PubMed:20339383, PubMed:28226241). Expressed in adult but not in fetal testis (PubMed:20339383). Not expressed in ovary. Within testis, expression is restricted to spermatids (PubMed:20339383). {ECO:0000269|PubMed:20339383, ECO:0000269|PubMed:28226241}. +Q61301 CTNA2_MOUSE Catenin alpha-2 (Alpha N-catenin) 953 105,286 Alternative sequence (2); Beta strand (4); Chain (1); Helix (26); Modified residue (5); Sequence conflict (16); Turn (1) FUNCTION: May function as a linker between cadherin adhesion receptors and the cytoskeleton to regulate cell-cell adhesion and differentiation in the nervous system. Regulates morphological plasticity of synapses and cerebellar and hippocampal lamination during development. Functions in the control of startle modulation. {ECO:0000269|PubMed:12089526, ECO:0000269|PubMed:12123610, ECO:0000269|PubMed:15034585}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16457793}; Peripheral membrane protein {ECO:0000305|PubMed:16457793}; Cytoplasmic side {ECO:0000305|PubMed:16457793}. Cytoplasm {ECO:0000269|PubMed:16457793}. Cytoplasm, cytoskeleton {ECO:0000305|PubMed:15034585}. Cell junction, adherens junction {ECO:0000269|PubMed:16457793, ECO:0000269|PubMed:16691566}. Cell projection, axon {ECO:0000269|PubMed:16457793, ECO:0000269|PubMed:16691566}. Nucleus {ECO:0000250|UniProtKB:P26232}. SUBUNIT: Interacts with CDH1 and CDH2 (By similarity). Interacts with ZNF639; recruits CTNNA2 to the nucleus (By similarity). {ECO:0000250|UniProtKB:P26232, ECO:0000250|UniProtKB:P30997}. TISSUE SPECIFICITY: Expressed almost exclusively in the nervous system. {ECO:0000269|PubMed:8174789}. +P30999 CTND1_MOUSE Catenin delta-1 (Cadherin-associated Src substrate) (CAS) (p120 catenin) (p120(ctn)) (p120(cas)) 938 104,925 Alternative sequence (2); Chain (1); Coiled coil (1); Cross-link (3); Erroneous initiation (1); Modified residue (41); Mutagenesis (1); Repeat (10); Sequence conflict (4); Site (2) FUNCTION: Binds to and inhibits the transcriptional repressor ZBTB33, which may lead to activation of target genes of the Wnt signaling pathway (By similarity). Associates with and regulates the cell adhesion properties of both C-, E- and N-cadherins, being critical for their surface stability. Implicated both in cell transformation by SRC and in ligand-induced receptor signaling through the EGF, PDGF, CSF-1 and ERBB2 receptors. Promotes GLIS2 C-terminal cleavage. {ECO:0000250, ECO:0000269|PubMed:15138284, ECO:0000269|PubMed:15817151, ECO:0000269|PubMed:17344476}. PTM: Phosphorylated by FER and other protein-tyrosine kinases. Phosphorylated at Ser-288 by PAK5. Dephosphorylated by PTPRJ (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15138284, ECO:0000269|PubMed:17344476}. Nucleus {ECO:0000269|PubMed:15138284, ECO:0000269|PubMed:17344476}. Cell membrane {ECO:0000269|PubMed:17344476}. Note=Interaction with GLIS2 promotes nuclear translocation (PubMed:17344476). Detected at cell-cell contacts (By similarity). NANOS1 induces its translocation from sites of cell-cell contact to the cytoplasm (By similarity). CDH1 enhances cell membrane localization (By similarity). {ECO:0000250|UniProtKB:O60716, ECO:0000269|PubMed:17344476}.; SUBCELLULAR LOCATION: Isoform 2: Nucleus {ECO:0000269|PubMed:15138284}. SUBUNIT: Belongs to a multiprotein cell-cell adhesion complex that also contains E-cadherin/CDH1, alpha-catenin/CTNNA1, beta-catenin/CTNNB1, and gamma-catenin/JUP. Binds to the C-terminal fragment of PSEN1 and mutually competes for CDH1 (By similarity). Interacts with ZBTB33 (PubMed:10207085, PubMed:12087177). Interacts with GLIS2 (PubMed:17344476). Interacts with FER (By similarity). Interacts with NANOS1 (via N-terminal region) (By similarity). Interacts (via N-terminus) with GNA12; the interaction regulates CDH1-mediated cell-cell adhesion (PubMed:15240885). Interacts with GNA13 (PubMed:15240885). Component of a cadherin:catenin adhesion complex composed of at least of CDH26, beta-catenin/CTNNB1, alpha-catenin/CTNNA1 and p120 catenin/CTNND1 (By similarity). {ECO:0000250|UniProtKB:O60716, ECO:0000269|PubMed:10207085, ECO:0000269|PubMed:12087177, ECO:0000269|PubMed:15240885, ECO:0000269|PubMed:17344476}. DOMAIN: ARM repeats 1 to 5 mediate interaction with cadherins. {ECO:0000250}. +Q61614 EDNRA_MOUSE Endothelin-1 receptor (Endothelin receptor type A) (ET-A) (ET-AR) 427 48,578 Chain (1); Disulfide bond (1); Glycosylation (3); Modified residue (1); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 81 102 Helical; Name=1. {ECO:0000255}.; TRANSMEM 113 132 Helical; Name=2. {ECO:0000255}.; TRANSMEM 160 181 Helical; Name=3. {ECO:0000255}.; TRANSMEM 206 229 Helical; Name=4. {ECO:0000255}.; TRANSMEM 257 278 Helical; Name=5. {ECO:0000255}.; TRANSMEM 307 328 Helical; Name=6. {ECO:0000255}.; TRANSMEM 348 372 Helical; Name=7. {ECO:0000255}. TOPO_DOM 21 80 Extracellular. {ECO:0000255}.; TOPO_DOM 103 112 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 133 159 Extracellular. {ECO:0000255}.; TOPO_DOM 182 205 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 230 256 Extracellular. {ECO:0000255}.; TOPO_DOM 279 306 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 329 347 Extracellular. {ECO:0000255}.; TOPO_DOM 373 427 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for endothelin-1. Mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. The rank order of binding affinities for ET-A is: ET1 > ET2 >> ET3 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBUNIT: Interacts with HDAC7 and KAT5. {ECO:0000250}. +Q3URE8 CTXN2_MOUSE Cortexin-2 81 8,987 Chain (1); Erroneous initiation (1); Transmembrane (1) TRANSMEM 29 49 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q921E6 EED_MOUSE Polycomb protein EED 441 50,198 Alternative sequence (2); Beta strand (30); Chain (1); Erroneous initiation (3); Helix (2); Initiator methionine (1); Modified residue (16); Mutagenesis (5); Region (1); Repeat (7); Turn (4) FUNCTION: Polycomb group (PcG) protein. Component of the PRC2/EED-EZH2 complex, which methylates 'Lys-9' and 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. Also recognizes 'Lys-26' trimethylated histone H1 with the effect of inhibiting PRC2 complex methyltransferase activity on nucleosomal histone H3 'Lys-27', whereas H3 'Lys-27' recognition has the opposite effect, enabling the propagation of this repressive mark (By similarity). The PRC2/EED-EZH2 complex may also serve as a recruiting platform for DNA methyltransferases, thereby linking two epigenetic repression systems (By similarity). Genes repressed by the PRC2/EED-EZH2 complex include HOXA7, HOXB6 and HOXC8. Plays a role in X chromosome inactivation (XCI), in which one of the two X chromosomes in female mammals is transcriptionally silenced to equalize X-linked gene dosage with XY males. Required for stable maintenance of XCI in both embryonic and extraembryonic tissues. May prevent transcriptional activation of facultative heterochromatin during differentiation. Required for development of secondary trophoblast giant cells during placental development. May regulate hippocampal synaptic plasticity in the developing brain. {ECO:0000250|UniProtKB:O75530, ECO:0000269|PubMed:11479595, ECO:0000269|PubMed:12370779, ECO:0000269|PubMed:12627233, ECO:0000269|PubMed:12649488, ECO:0000269|PubMed:12689588, ECO:0000269|PubMed:15516932, ECO:0000269|PubMed:15916951, ECO:0000269|PubMed:16415857, ECO:0000269|PubMed:16618801, ECO:0000269|PubMed:17259173, ECO:0000269|PubMed:17997413, ECO:0000269|PubMed:18201968, ECO:0000269|PubMed:9234727, ECO:0000269|PubMed:9742080}. PTM: Methylated. Binding to histone H1 'Lys-26' promotes mono-, di-, and trimethylation of internal lysines (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Localizes to the inactive X chromosome in cells of the early embryo and in stem cells of the extraembryonic trophectoderm lineage. Recruitment to the inactive X-chromosome requires XIST. SUBUNIT: Component of the PRC2/EED-EZH2 complex, which includes EED, EZH2, SUZ12, RBBP4 and RBBP7 and possibly AEBP2 (By similarity). The minimum components required for methyltransferase activity of the PRC2/EED-EZH2 complex are EED, EZH2 and SUZ12 (By similarity). Component of the PRC2/EED-EZH1 complex, which includes EED, EZH1, SUZ12, RBBP4 and AEBP2. The PRC2 complex may also interact with DNMT1, DNMT3A, DNMT3B and PHF1 via the EZH2 subunit and with SIRT1 via the SUZ12 subunit (By similarity). Interacts with HDAC, HDAC2, histone H1 and YY1 (By similarity). May interact with ITGA4, ITGAE and ITGB7 (By similarity). Interacts with CDYL (By similarity). Interacts with EZH2. Interacts with KMT2A/MLL1 in adult brain. Interacts with ARNTL/BMAL1. {ECO:0000250|UniProtKB:O75530, ECO:0000269|PubMed:16224021, ECO:0000269|PubMed:17259173, ECO:0000269|PubMed:17937919, ECO:0000269|PubMed:17997413, ECO:0000269|PubMed:19026780, ECO:0000269|PubMed:20144788, ECO:0000269|PubMed:23970558, ECO:0000269|PubMed:9742080}. DOMAIN: The WD repeat domain mediates recognition of trimethylated histone peptides at the consensus sequence Ala-Arg-Lys-Ser. This is achieved through an aromatic cage encircling the methyllysine, and involving Phe-97, Tyr-148 and Tyr-365 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver, lung, muscle, ovary, spleen and testis. Expressed throughout the brain. {ECO:0000269|PubMed:17259173, ECO:0000269|PubMed:8805699, ECO:0000269|PubMed:9234727}. +Q3TGW2 EEPD1_MOUSE Endonuclease/exonuclease/phosphatase family domain-containing protein 1 569 62,953 Chain (1); Domain (1); Erroneous initiation (1); Initiator methionine (1); Lipidation (1); Modified residue (7); Sequence conflict (2) +P10126 EF1A1_MOUSE Elongation factor 1-alpha 1 (EF-1-alpha-1) (Elongation factor Tu) (EF-Tu) (Eukaryotic elongation factor 1 A-1) (eEF1A-1) 462 50,114 Chain (1); Domain (1); Initiator methionine (1); Modified residue (20); Nucleotide binding (3); Region (5); Sequence conflict (13) FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. With PARP1 and TXK, forms a complex that acts as a T helper 1 (Th1) cell-specific transcription factor and binds the promoter of IFN-gamma to directly regulate its transcription, and is thus involved importantly in Th1 cytokine production. {ECO:0000250|UniProtKB:P68104}. PTM: ISGylated. {ECO:0000269|PubMed:16139798}.; PTM: Phosphorylated by TXK. Phosphorylation by PASK increases translation efficiency. Phosphorylated by ROCK2. {ECO:0000250|UniProtKB:P68104}.; PTM: Trimethylated at Lys-79 by EEF1AKMT1 (By similarity). Methylated at Lys-165 by EEF1AKMT3, methylation by EEF1AKMT3 is dynamic as well as inducible by stress conditions, such as ER-stress, and plays a regulatory role on mRNA translation (PubMed:28108655). Trimethylated at Lys-318 by EEF1AKMT2 (By similarity). Mono-, di-, and trimethylated at Lys-36 by EEF1AKMT4; trimethylated form is predominant. Methylation by EEF1AKMT4 contributes to the fine-tuning of translation rates for a subset of tRNAs (By similarity). {ECO:0000250|UniProtKB:P68104, ECO:0000269|PubMed:28108655}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19856081}. Nucleus {ECO:0000250|UniProtKB:P68104}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P68104}. Cell membrane {ECO:0000250|UniProtKB:P68104}. Note=Colocalizes with DLC1 at actin-rich regions in the cell periphery. Translocates together with ZPR1 from the cytoplasm to the nucleus and nucleolus after treatment with mitogens. Localization at the cell membrane depends on EEF1A1 phosphorylation status and the presence of PPP1R16B. {ECO:0000250|UniProtKB:P68104}. SUBUNIT: Found in a nuclear export complex with XPO5, EEF1A1, Ran and aminoacylated tRNA. Interacts with PARP1, TXK, XPO5 and KARS. May interact with ERGIC2 (By similarity). Interacts with IFIT1 (via TPR repeats 4-7) (PubMed:19856081). Interacts with DLC1, facilitating distribution to the membrane periphery and ruffles upon growth factor stimulation. Interacts with ZPR1; the interaction occurs in a epidermal growth factor (EGF)-dependent manner (By similarity). Interacts with PPP1R16B (By similarity). {ECO:0000250|UniProtKB:P68104, ECO:0000269|PubMed:19856081}. +Q9CXX9 CUED2_MOUSE CUE domain-containing protein 2 284 31,852 Chain (1); Domain (1); Sequence conflict (2) FUNCTION: Controls PGR and ESR1 protein levels through their targeting for ubiquitination and subsequent proteasomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Interacts with PGR and ESR1. {ECO:0000250}. DOMAIN: The CUE domain mediates interaction with PGR and ESR1. {ECO:0000250}. +P62631 EF1A2_MOUSE Elongation factor 1-alpha 2 (EF-1-alpha-2) (Eukaryotic elongation factor 1 A-2) (eEF1A-2) (Statin-S1) 463 50,454 Chain (1); Domain (1); Initiator methionine (1); Modified residue (14); Nucleotide binding (3); Region (5) FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. PTM: Trimethylated at Lys-165 by EEF1AKMT3. Mono-, di-, and trimethylated at Lys-36 by EEF1AKMT4; trimethylated form is predominant. Methylation by EEF1AKMT4 contributes to the fine-tuning of translation rates for a subset of tRNAs. {ECO:0000250|UniProtKB:Q05639}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Monomer. TISSUE SPECIFICITY: Found in a wide range of tissues. +Q9JLV5 CUL3_MOUSE Cullin-3 (CUL-3) 768 88,948 Beta strand (3); Chain (1); Cross-link (1); Helix (3); Initiator methionine (1); Modified residue (2); Turn (1) Protein modification; protein ubiquitination. FUNCTION: Core component of multiple cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). BCR complexes and ARIH1 collaborate in tandem to mediate ubiquitination of target proteins (By similarity). As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme (By similarity). The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and is inhibited by the association of the deneddylated cullin subunit with TIP120A/CAND1 (By similarity). The functional specificity of the BCR complex depends on the BTB domain-containing protein as the substrate recognition component (By similarity). BCR(KLHL42) is involved in ubiquitination of KATNA1 (By similarity). BCR(SPOP) is involved in ubiquitination of BMI1/PCGF4, BRMS1, H2AFY and DAXX, GLI2 and GLI3 (By similarity). Can also form a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex containing homodimeric SPOPL or the heterodimer formed by SPOP and SPOPL; these complexes have lower ubiquitin ligase activity (By similarity). BCR(KLHL9-KLHL13) controls the dynamic behavior of AURKB on mitotic chromosomes and thereby coordinates faithful mitotic progression and completion of cytokinesis (By similarity). BCR(KLHL12) is involved in ER-Golgi transport by regulating the size of COPII coats, thereby playing a key role in collagen export, which is required for embryonic stem (ES) cells division: BCR(KLHL12) acts by mediating monoubiquitination of SEC31 (SEC31A or SEC31B) (PubMed:22358839). BCR(KLHL3) acts as a regulator of ion transport in the distal nephron; by mediating ubiquitination of WNK4 (By similarity). The BCR(KLHL20) E3 ubiquitin ligase complex is involved in interferon response and anterograde Golgi to endosome transport: it mediates both ubiquitination leading to degradation and 'Lys-33'-linked ubiquitination (By similarity). The BCR(KLHL21) E3 ubiquitin ligase complex regulates localization of the chromosomal passenger complex (CPC) from chromosomes to the spindle midzone in anaphase and mediates the ubiquitination of AURKB (By similarity). The BCR(KLHL22) ubiquitin ligase complex mediates monoubiquitination of PLK1, leading to PLK1 dissociation from phosphoreceptor proteins and subsequent removal from kinetochores, allowing silencing of the spindle assembly checkpoint (SAC) and chromosome segregation. The BCR(KLHL22) ubiquitin ligase complex is also responsible for the amino acid-stimulated 'Lys-48' polyubiquitination and proteasomal degradation of DEPDC5. Through the degradation of DEPDC5, releases the GATOR1 complex-mediated inhibition of the TORC1 pathway (By similarity). The BCR(KLHL25) ubiquitin ligase complex is involved in translational homeostasis by mediating ubiquitination and subsequent degradation of hypophosphorylated EIF4EBP1 (4E-BP1) (By similarity). The BCR(KBTBD8) complex acts by mediating monoubiquitination of NOLC1 and TCOF1, leading to remodel the translational program of differentiating cells in favor of neural crest specification (By similarity). Involved in ubiquitination of cyclin E and of cyclin D1 (in vitro) thus involved in regulation of G1/S transition (By similarity). Involved in the ubiquitination of KEAP1, ENC1 and KLHL41 (By similarity). In concert with ATF2 and RBX1, promotes degradation of KAT5 thereby attenuating its ability to acetylate and activate ATM (By similarity). The BCR(KCTD17) E3 ubiquitin ligase complex mediates ubiquitination and degradation of TCHP, a down-regulator of cilium assembly, thereby inducing ciliogenesis (By similarity). The BCR(KLHL24) E3 ubiquitin ligase complex mediates ubiquitination of KRT14, controls KRT14 levels during keratinocytes differentiation, and is essential for skin integrity (By similarity). {ECO:0000250|UniProtKB:Q13618, ECO:0000269|PubMed:22358839}. PTM: Neddylated. Attachment of NEDD8 is required for the E3 ubiquitin-protein ligase activity of the BCR complex. Deneddylated via its interaction with the COP9 signalosome (CSN) complex. {ECO:0000250|UniProtKB:Q13618}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10500095}. Golgi apparatus {ECO:0000269|PubMed:10500095}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q13618}. Cytoplasm {ECO:0000250|UniProtKB:Q13618}. Note=Detected along the length of the sperm flagellum and in the cytoplasm of the germ cells. {ECO:0000250|UniProtKB:Q13618}. SUBUNIT: Forms neddylation-dependent homodimers. Component of multiple BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes formed of CUL3, RBX1 and a variable BTB domain-containing protein acting as both, adapter to cullin and substrate recognition subunit. The BCR complex may be active as a heterodimeric complex, in which NEDD8, covalently attached to one CUL3 molecule, binds to the C-terminus of a second CUL3 molecule. Interacts with RBX1, RNF7, CYCE and TIP120A/CAND1. Part of the BCR(SPOP) containing SPOP, and of BCR containing homodimeric SPOPL or the heterodimer formed by SPOP and SPOPL. Part of the probable BCR(KLHL9-KLHL13) complex with BTB domain proteins KLHL9 and KLHL13. Part of the BCR(KLHL41) complex containing KLHL41. Component of the BCR(KLHL12) E3 ubiquitin ligase complex, at least composed of CUL3 and KLHL12 and RBX1. Component of the BCR(KLHL3) E3 ubiquitin ligase complex, at least composed of CUL3 and KLHL3 and RBX1 (By similarity). Part of the BCR(ENC1) complex containing ENC1. Part of a complex consisting of BMI1/PCGF4, CUL3 and SPOP. Part of a complex consisting of BRMS1, CUL3 and SPOP. Component of the BCR(KLHL21) E3 ubiquitin ligase complex, at least composed of CUL3, KLHL21 and RBX1. Component of the BCR(KLHL22) E3 ubiquitin ligase complex, at least composed of CUL3, KLHL22 and RBX1. Component of the BCR(KLHL25) E3 ubiquitin ligase complex, at least composed of CUL3, KLHL25 and RBX1. Part of a complex consisting of H2AFY, CUL3 and SPOP. Component of the BCR(KLHL42) E3 ubiquitin ligase complex, at least composed of CUL3 and KLHL42. Component of the BCR(KBTBD8) E3 ubiquitin ligase complex, at least composed of CUL3, KBTBD8 and RBX1. Interacts with KLHL42 (via the BTB domain). Interacts with KATNA1; the interaction is enhanced by KLHL42. Interacts with KCTD5, KLHL9, KLHL11, KLHL13, GAN, ZBTB16, KLHL3, KLHL15, KLHL20, KLHL36, GMCL2, BTBD1. Part of a complex that contains CUL3, RBX1 and GAN. Interacts (via BTB domain) with KLHL17; the interaction regulates surface GRIK2 expression. Interacts with KCTD7. Part of the BCR(GAN) complex containing GAN. Part of the BCR(KEAP1) complex containing KEAP1. Interacts with KLHL10 (By similarity). Interacts with KAT5 and ATF2. Interacts with DCUN1D3. Interacts with KCTD17 in the BCR(KCTD17) E3 ubiquitin ligase complex, at least composed of CUL3, KCTD17 and RBX1. Interacts (when neddylated) with ARIH1; leading to activate the E3 ligase activity of ARIH1 (By similarity). Interacts with COPS9 (By similarity). Interacts with PPP2R5B; this interaction is indirect and mediated through KLHL15-binding and leads to PPP2R5B proteasomal degradation (By similarity). Interacts with RBBP8/CtIP; this interaction is indirect and mediated through KLHL15-binding and leads to RBBP8 proteasomal degradation (By similarity). Interacts with KLHL24 in the BCR(KLHL24) E3 ubiquitin ligase complex, composed of CUL3, RBX1 and KLHL24. Interacts with RHOBTB2. {ECO:0000250, ECO:0000250|UniProtKB:Q13618}. TISSUE SPECIFICITY: Widely expressed, with highest expression in brain, spleen and testis. In the testis, it is mainly expressed in spermatids. {ECO:0000269|PubMed:10500095, ECO:0000269|PubMed:16162871}. +A2A432 CUL4B_MOUSE Cullin-4B (CUL-4B) 970 110,699 Alternative sequence (1); Chain (1); Compositional bias (2); Cross-link (2); Erroneous initiation (3); Modified residue (8); Motif (1); Sequence conflict (6) Protein modification; protein ubiquitination. FUNCTION: Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition subunit. CUL4B may act within the complex as a scaffold protein, contributing to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. Plays a role as part of the E3 ubiquitin-protein ligase complex in polyubiquitination of CDT1, histone H2A, histone H3 and histone H4 in response to radiation-induced DNA damage. Targeted to UV damaged chromatin by DDB2 and may be important for DNA repair and DNA replication. Required for ubiquitination of cyclin E, and consequently, normal G1 cell cycle progression. Regulates the mammalian target-of-rapamycin (mTOR) pathway involved in control of cell growth, size and metabolism. Specific CUL4B regulation of the mTORC1-mediated pathway is dependent upon 26S proteasome function and requires interaction between CUL4B and MLST8 (By similarity). {ECO:0000250|UniProtKB:Q13620}. PTM: Neddylated. Deneddylated via its interaction with the COP9 signalosome (CSN) complex (By similarity). {ECO:0000250|UniProtKB:Q13620}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13620}. SUBUNIT: Component of multiple DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes that seem to be formed of DDB1, CUL4A or CUL4B, RBX1 and a variable substrate recognition component which seems to belong to a protein family described as DCAF (Ddb1- and Cul4-associated factor) or CDW (CUL4-DDB1-associated WD40-repeat) proteins. Component of the DCX(DTL) complex with the putative substrate recognition component DTL. Component of the DCX(DDB2) complex with the putative substrate recognition component DDB2. Part of a complex with RBX1 and TIP120A/CAND1. Interacts with RBX1 GRWD1, MLST8, SMU1, TLE2, TLE3, DCAF1, DDA1, DCAF6, DCAF17, DDB2, DCAF8, TIP120A/CAND1 and TMEM113. Interacts with cyclin E and with importins alpha-1 (KPNA2), alpha-3 (KPNA4), alpha-5 (KPNA1) and beta-1 (KPNB1). May interact with WDR26, WDR51B, SNRNP40, WDR61, WDR76 and WDR5 (By similarity). {ECO:0000250|UniProtKB:Q13620}. +Q5U458 DJC11_MOUSE DnaJ homolog subfamily C member 11 559 63,233 Chain (1); Coiled coil (1); Domain (1); Initiator methionine (1); Modified residue (2); Sequence caution (1); Sequence conflict (5) FUNCTION: Required for mitochondrial inner membrane organization. Seems to function through its association with the MICOS complex and the mitochondrial outer membrane sorting assembly machinery (SAM) complex. {ECO:0000269|PubMed:25111180, ECO:0000305}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9NVH1, ECO:0000269|PubMed:25111180}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q9NVH1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9NVH1}. SUBUNIT: Associates with the mitochondrial contact site and cristae organizing system (MICOS) complex, composed of at least MINOS1/MIC10, CHCHD3/MIC19, CHCHD6/MIC25, APOOL/MIC27, IMMT/MIC60, APOO/MIC23/MIC26 and QIL1/MIC13. This complex was also known under the names MINOS or MitOS complex. The MICOS complex associates with mitochondrial outer membrane proteins SAMM50, MTX1 and MTX2 (together described as components of the mitochondrial outer membrane sorting assembly machinery (SAM) complex) and DNAJC11, mitochondrial inner membrane protein TMEM11 and with HSPA9. The MICOS and SAM complexes together with DNAJC11 are part of a large protein complex spanning both membranes termed the mitochondrial intermembrane space bridging (MIB) complex. {ECO:0000250|UniProtKB:Q9NVH1, ECO:0000305, ECO:0000305|PubMed:25111180}. +Q9R022 DJC12_MOUSE DnaJ homolog subfamily C member 12 (J domain-containing protein 1) 198 22,853 Chain (1); Domain (1); Modified residue (4) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UKB3}. SUBUNIT: Interacts with HSPA8. {ECO:0000250|UniProtKB:Q9UKB3}. TISSUE SPECIFICITY: Ubiquitous. Highest levels of expression in kidney. +Q78YY6 DJC15_MOUSE DnaJ homolog subfamily C member 15 149 15,953 Chain (1); Domain (1); Modified residue (1); Topological domain (2); Transmembrane (1) TRANSMEM 38 54 Helical. {ECO:0000255}. TOPO_DOM 1 37 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 55 149 Mitochondrial matrix. {ECO:0000255}. FUNCTION: Acts as an import component of the TIM23 translocase complex. Stimulates the ATPase activity of HSPA9 (By similarity). Negative regulator of the mitochondrial respiratory chain. Prevents mitochondrial hyperpolarization state and restricts mitochondrial generation of ATP. {ECO:0000250, ECO:0000269|PubMed:23530063}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:23530063}; Single-pass membrane protein {ECO:0000269|PubMed:23530063}. SUBUNIT: Interacts with the TIM23 complex. Directly interacts with PAM16/MAGMAS; this interaction counteracts DNAJC15-dependent stimulation of HSPA9 ATPase activity (By similarity). Associates with complex I of the mitochondrial electron transfer chain; this interaction may interfere with the formation of supercomplexes that facilitate the transfer of electrons between complexes. {ECO:0000250}. TISSUE SPECIFICITY: Expressed at high levels in liver, heart, at moderate levels in kidney and, at very low levels, in lung (at protein level). High expression levels in testis. Highly expressed in CD8+ T-cells, but barely detectable in CD4+ T-cells (at protein level). Almost undetectable in B-cells. {ECO:0000269|PubMed:23530063}. +O54908 DKK1_MOUSE Dickkopf-related protein 1 (Dickkopf-1) (Dkk-1) (mDkk-1) 272 29,298 Chain (1); Disulfide bond (10); Glycosylation (2); Mutagenesis (4); Region (2); Sequence conflict (2); Signal peptide (1) FUNCTION: Antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by forming a ternary complex with the transmembrane protein KREMEN that promotes internalization of LRP5/6 (PubMed:18524778). Inhibits the pro-apoptotic function of KREMEN1 in a Wnt-independent manner, and has anti-apoptotic activity (PubMed:26206087). Plays a role in limb development; attenuates Wnt signaling in the developing limb to allow normal limb patterning (PubMed:18505822). {ECO:0000269|PubMed:18505822, ECO:0000269|PubMed:18524778, ECO:0000269|PubMed:26206087}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Interacts (via the C-termianl Cys-rich domain) with LRP5 (via beta-propeller regions 3 and 4); the interaction, enhanced by MESD and or KREMEN, antagonizes Wnt-mediated signaling. Interacts with LRP6 (PubMed:18524778). Forms a ternary complex with LRP6 and KREM1. Interacts with KREM1 (By similarity). {ECO:0000250|UniProtKB:O94907, ECO:0000269|PubMed:18524778}. DOMAIN: The C-terminal cysteine-rich domain mediates interaction with LRP5 and LRP6. +Q9QZL9 DKKL1_MOUSE Dickkopf-like protein 1 (Protein soggy-1) (SGY-1) 230 26,639 Chain (1); Glycosylation (3); Sequence conflict (3); Signal peptide (1) FUNCTION: Involved in fertilization by facilitating sperm penetration of the zona pellucida (PubMed:19596312, PubMed:22817830). May promotes spermatocyte apoptosis, thereby limiting sperm production. In adults, may reduces testosterone synthesis in Leydig cells (PubMed:18818293). Is not essential either for development or fertility (PubMed:19596310). {ECO:0000269|PubMed:18818293, ECO:0000269|PubMed:19596310, ECO:0000269|PubMed:19596312, ECO:0000269|PubMed:22817830}. PTM: N-glycosylated during spermatogenesis. Not N-glycosylated in mature sperm. {ECO:0000269|PubMed:15892050, ECO:0000269|PubMed:19596310}. SUBCELLULAR LOCATION: Secreted. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:15892050, ECO:0000269|PubMed:19176879}. Note=Localized specifically to the crescent shaped acrosome at the apex of the sperm head. {ECO:0000269|PubMed:15892050}. SUBUNIT: Interacts with SLXL1; Co-localize in seminiferous tubules (PubMed:21698294). Interacts with SLY (PubMed:19176879). {ECO:0000269|PubMed:19176879, ECO:0000269|PubMed:21698294}. DOMAIN: Contains a N-terminal domain similar to that of the N-terminal section of DKK3. TISSUE SPECIFICITY: Testis-specific. Abundant in the seminiferous tubules where it is associated with developing spermatocytes. Expressed only in testis (at protein level) (PubMed:15892050, PubMed:19596310). Not detectable on postnatal days 4 and 9 but after day 18 it gradually increased as the development of testes progressed. Expressed at high levels in testis and at weak levels in epididymis (PubMed:22817830). {ECO:0000269|PubMed:11024178, ECO:0000269|PubMed:15892050, ECO:0000269|PubMed:19596310, ECO:0000269|PubMed:22817830}. +P70396 DLX5_MOUSE Homeobox protein DLX-5 289 31,396 Alternative sequence (3); Chain (1); DNA binding (1); Modified residue (2); Mutagenesis (2); Sequence conflict (2) FUNCTION: Transcriptional factor involved in bone development. Acts as an immediate early BMP-responsive transcriptional activator essential for osteoblast differentiation. Stimulates ALPL promoter activity in a RUNX2-independent manner during osteoblast differentiation. Stimulates SP7 promoter activity during osteoblast differentiation. Promotes cell proliferation by up-regulating MYC promoter activity. Involved as a positive regulator of both chondrogenesis and chondrocyte hypertrophy in the endochondral skeleton. Binds to the homeodomain-response element of the ALPL and SP7 promoter. Binds to the MYC promoter. Requires the 5'-TAATTA-3' consensus sequence for DNA-binding. {ECO:0000269|PubMed:15383550, ECO:0000269|PubMed:18056716, ECO:0000269|PubMed:19956613}. PTM: Phosphorylated. Phosphorylation of Ser-34 and Ser-217 by MAPK14 enhances its transcriptional activity. Phosphorylation by CaMK2 increases its protein stability. {ECO:0000269|PubMed:18056716, ECO:0000269|PubMed:19393622}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:18056716}. SUBUNIT: Interacts with XRCC6 (Ku70). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in osteoblasts and chondrocytes. {ECO:0000269|PubMed:19956613}. +O08749 DLDH_MOUSE Dihydrolipoyl dehydrogenase, mitochondrial (EC 1.8.1.4) (Dihydrolipoamide dehydrogenase) 509 54,272 Active site (1); Binding site (6); Chain (1); Disulfide bond (1); Modified residue (26); Nucleotide binding (4); Sequence conflict (4); Site (2); Transit peptide (1) FUNCTION: Lipoamide dehydrogenase is a component of the glycine cleavage system as well as an E3 component of three alpha-ketoacid dehydrogenase complexes (pyruvate-, alpha-ketoglutarate-, and branched-chain amino acid-dehydrogenase complex) (By similarity). The 2-oxoglutarate dehydrogenase complex is mainly active in the mitochondrion (By similarity). A fraction of the 2-oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation of histones: associates with KAT2A on chromatin and provides succinyl-CoA to histone succinyltransferase KAT2A (By similarity). In monomeric form may have additional moonlighting function as serine protease (PubMed:17404228). Involved in the hyperactivation of spermatazoa during capacitation and in the spermatazoal acrosome reaction (By similarity). {ECO:0000250|UniProtKB:P09622, ECO:0000250|UniProtKB:Q811C4, ECO:0000269|PubMed:17404228}. PTM: Tyrosine phosphorylated. {ECO:0000250|UniProtKB:Q811C4}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000305|PubMed:9169128}. Nucleus {ECO:0000250|UniProtKB:P09622}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q811C4}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:15888450}. Note=Mainly localizes in the mitochondrion. A small fraction localizes to the nucleus, where the 2-oxoglutarate dehydrogenase complex is required for histone succinylation. {ECO:0000250|UniProtKB:P09622}. SUBUNIT: Homodimer. Part of the multimeric pyruvate dehydrogenase complex that contains multiple copies of pyruvate dehydrogenase (subunits PDHA (PDHA1 or PDHA2) and PDHB, E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3). These subunits are bound to an inner core composed of about 48 DLAT and 12 PDHX molecules (by non covalent bonds). The 2-oxoglutarate dehydrogenase complex is composed of OGDH (2-oxoglutarate dehydrogenase; E1), DLST (dihydrolipoamide succinyltransferase; E2) and DLD (dihydrolipoamide dehydrogenase; E3). It contains multiple copies of the three enzymatic components (E1, E2 and E3). In the nucleus, the 2-oxoglutarate dehydrogenase complex associates with KAT2A. Interacts with PDHX. {ECO:0000250|UniProtKB:P09622}. TISSUE SPECIFICITY: Expressed in liver (at protein level). {ECO:0000269|PubMed:17404228}. +Q80WT2 DMRT3_MOUSE Doublesex- and mab-3-related transcription factor 3 476 51,518 Chain (1); DNA binding (1); Sequence conflict (3) FUNCTION: Probable transcription factor that plays a role in configuring the spinal circuits controlling stride in vertebrates. Involved in neuronal specification within specific subdivision of spinal cord neurons and in the development of a coordinated locomotor network controlling limb movements. May regulate transcription during sexual development. {ECO:0000269|PubMed:22932389}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00070}. TISSUE SPECIFICITY: Expressed in the ventral spinal cord, in a restrical population of neurons migrating ventrically in the developing spinal cord at E11.5. {ECO:0000269|PubMed:22932389}. +Q8C0M8 DNAI1_MOUSE Dynein intermediate chain 1, axonemal (Axonemal dynein intermediate chain 1) 701 79,758 Chain (1); Compositional bias (1); Modified residue (2); Repeat (5); Sequence conflict (1) FUNCTION: Part of the dynein complex of respiratory cilia. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q9UI46}. SUBUNIT: Consists of at least two heavy chains and a number of intermediate and light chains. Interacts with BICD2. {ECO:0000250}. +Q61585 G0S2_MOUSE G0/G1 switch protein 2 (G0S2-like protein) 103 11,118 Chain (1) FUNCTION: Promotes apoptosis by binding to BCL2, hence preventing the formation of protective BCL2-BAX heterodimers. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. SUBUNIT: Directly interacts with BCL2; this interaction prevents the formation of the anti-apoptotic BAX-BCL2 complex. {ECO:0000250}. +Q8BNQ3 G137B_MOUSE Integral membrane protein GPR137B (Transmembrane 7 superfamily member 1 protein) 385 44,055 Chain (1); Glycosylation (2); Sequence conflict (2); Topological domain (8); Transmembrane (7) TRANSMEM 33 53 Helical. {ECO:0000255}.; TRANSMEM 65 85 Helical. {ECO:0000255}.; TRANSMEM 97 117 Helical. {ECO:0000255}.; TRANSMEM 145 165 Helical. {ECO:0000255}.; TRANSMEM 174 194 Helical. {ECO:0000255}.; TRANSMEM 223 243 Helical. {ECO:0000255}.; TRANSMEM 278 298 Helical. {ECO:0000255}. TOPO_DOM 1 32 Extracellular. {ECO:0000255}.; TOPO_DOM 54 64 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 86 96 Extracellular. {ECO:0000255}.; TOPO_DOM 118 144 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 166 173 Extracellular. {ECO:0000255}.; TOPO_DOM 195 222 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 244 277 Extracellular. {ECO:0000255}.; TOPO_DOM 299 385 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250}; Multi-pass membrane protein. +Q9QYJ0 DNJA2_MOUSE DnaJ homolog subfamily A member 2 (mDj3) 412 45,746 Chain (1); Cross-link (1); Domain (1); Lipidation (1); Metal binding (8); Modified residue (8); Propeptide (1); Repeat (4); Zinc finger (1) FUNCTION: Co-chaperone of Hsc70. Stimulates ATP hydrolysis and the folding of unfolded proteins mediated by HSPA1A/B (in vitro). {ECO:0000250|UniProtKB:O60884}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. +Q99M87 DNJA3_MOUSE DnaJ homolog subfamily A member 3, mitochondrial (DnaJ protein Tid-1) (mTid-1) (Tumorous imaginal discs protein Tid56 homolog) 480 52,443 Alternative sequence (3); Chain (1); Domain (1); Metal binding (8); Modified residue (5); Repeat (4); Sequence conflict (2); Transit peptide (1); Zinc finger (1) FUNCTION: Modulates apoptotic signal transduction or effector structures within the mitochondrial matrix. Affect cytochrome C release from the mitochondria and caspase 3 activation, but not caspase 8 activation. Isoform 1 increases apoptosis triggered by both TNF and the DNA-damaging agent mytomycin C; in sharp contrast, isoform 2 suppresses apoptosis. Can modulate IFN-gamma-mediated transcriptional activity (By similarity). Isoform 2 may play a role in neuromuscular junction development as an effector of the MUSK signaling pathway. {ECO:0000250, ECO:0000269|PubMed:19038220}. PTM: Tyrosine phosphorylated. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. Cytoplasm, cytosol {ECO:0000269|PubMed:19038220}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000269|PubMed:19038220}; Peripheral membrane protein {ECO:0000269|PubMed:19038220}. Note=Recruited to the postsynaptic cell membrane of the neuromuscular junction through interaction with MUSK. SUBUNIT: Interacts with JAK2, HSPA9B and IFN-gammaR2 chain. Interacts with Ras GTPase-activating protein 1 (RASA1). Isoform 2 interacts with MUSK (via the cytoplasmic domain). {ECO:0000269|PubMed:11116152, ECO:0000269|PubMed:19038220}. DOMAIN: Modulation of apoptosis, i.e. proapoptotic activity of isoform 1 and antiapoptotic activity of isoform 2, is J domain-dependent (By similarity). {ECO:0000250}. +Q9JMC3 DNJA4_MOUSE DnaJ homolog subfamily A member 4 (MmDjA4) 397 44,902 Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (1); Lipidation (1); Metal binding (8); Modified residue (2); Propeptide (1); Repeat (4); Zinc finger (1) SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. TISSUE SPECIFICITY: Specifically expressed in testis and heart. +Q9QYI5 DNJB2_MOUSE DnaJ homolog subfamily B member 2 (DnaJ homolog subfamily B member 10) (mDj8) 324 35,593 Alternative sequence (3); Chain (1); Compositional bias (1); Domain (3); Initiator methionine (1); Lipidation (1); Modified residue (3); Motif (1); Propeptide (1); Sequence conflict (4) FUNCTION: Functions as a co-chaperone, regulating the substrate binding and activating the ATPase activity of chaperones of the HSP70/heat shock protein 70 family. In parallel, also contributes to the ubiquitin-dependent proteasomal degradation of misfolded proteins. Thereby, may regulate the aggregation and promote the functional recovery of misfolded proteins like HTT, MC4R, PRKN, RHO and SOD1 and be crucial for many biological processes. Isoform 1 which is localized to the endoplasmic reticulum membranes may specifically function in ER-associated protein degradation of misfolded proteins. {ECO:0000250|UniProtKB:P25686}. PTM: Ubiquitinated by STUB1; does not lead to proteasomal degradation. {ECO:0000250|UniProtKB:P25686}. SUBCELLULAR LOCATION: Isoform 2: Cytoplasm {ECO:0000250|UniProtKB:P25686}. Nucleus {ECO:0000250|UniProtKB:P25686}.; SUBCELLULAR LOCATION: Isoform 1: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P25686}; Lipid-anchor {ECO:0000250|UniProtKB:P25686}; Cytoplasmic side {ECO:0000250|UniProtKB:P25686}. SUBUNIT: Interacts with HSP70 (HSPA1A or HSPA1B). Interacts with HSPA8/Hsc70. Interacts with PSMA3 and most probably with the whole proteasomal complex. {ECO:0000250|UniProtKB:P25686}. DOMAIN: The J domain is sufficient to interact with HSP70 (HSPA1A or HSPA1B) and activate its ATPase activity. The J domain is also required for the HSP70-mediated and ubiquitin-dependent proteasomal degradation of proteins like ATXN3. The J domain is required to reduce PRKN cytoplasmic aggregation. {ECO:0000250|UniProtKB:P25686}.; DOMAIN: The UIM domains mediate interaction with ubiquitinated chaperone clients and with the proteasome. The UIM domains may have an opposite activity to the J domain, binding ubiquitinated proteins and protecting them from HSP70-mediated proteasomal degradation. The UIM domains are not required to reduce PRKN cytoplasmic aggregation. {ECO:0000250|UniProtKB:P25686}. +O35723 DNJB3_MOUSE DnaJ homolog subfamily B member 3 (DnaJ protein homolog 3) (Heat shock protein J3) (HSJ-3) (MSJ-1) 242 26,679 Chain (1); Domain (1); Sequence conflict (4) FUNCTION: May operate as a co-chaperone of the male germ cell- and haploid stage-specific Hsp70 proteins. {ECO:0000305}. TISSUE SPECIFICITY: Testis specific. Expression is confined to the germline without any contribution of the somatic components. +Q9D832 DNJB4_MOUSE DnaJ homolog subfamily B member 4 337 37,782 Chain (1); Domain (1); Modified residue (2); Sequence conflict (3) FUNCTION: Probable chaperone. Stimulates ATP hydrolysis and the folding of unfolded proteins mediated by HSPA1A/B (in vitro). {ECO:0000250|UniProtKB:Q9UDY4}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UDY4}. Cell membrane {ECO:0000250|UniProtKB:Q9UDY4}. SUBUNIT: Homodimer. The C-terminal section interacts with the C-terminal tail of OPRM1. Interacts also with SDIM1 (By similarity). {ECO:0000250|UniProtKB:Q9UDY4}. +O89114 DNJB5_MOUSE DnaJ homolog subfamily B member 5 (Heat shock protein Hsp40-3) (Heat shock protein cognate 40) (Hsc40) 348 39,119 Chain (1); Domain (1) +Q9QYI8 DNJB7_MOUSE DnaJ homolog subfamily B member 7 (mDj5) 312 35,626 Chain (1); Domain (1); Frameshift (1); Sequence conflict (4) FUNCTION: Probably acts as a co-chaperone. {ECO:0000250}. +Q9QYI7 DNJB8_MOUSE DnaJ homolog subfamily B member 8 (mDj6) 227 25,230 Chain (1); Compositional bias (1); Domain (1) FUNCTION: Efficient suppressor of aggregation and toxicity of disease-associated polyglutamine proteins. {ECO:0000250}. SUBUNIT: Interacts with histone deacetylases HDAC4, HDAC6, and SIRT2, HDAC activity is required for antiaggregation. {ECO:0000250}. DOMAIN: The antiaggregation activity resides in the serine-rich region and the C-terminus. {ECO:0000250}. +Q9QYI6 DNJB9_MOUSE DnaJ homolog subfamily B member 9 (Endoplasmic reticulum DNA J domain-containing protein 4) (ER-resident protein ERdj4) (ERdj4) (mDj7) 222 25,616 Chain (1); Domain (1); Modified residue (1); Mutagenesis (1); Region (1); Sequence conflict (2); Signal peptide (1) FUNCTION: Co-chaperone for Hsp70 protein HSPA5/BiP that acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR) (By similarity). J domain-containing co-chaperones stimulate the ATPase activity of Hsp70 proteins and are required for efficient substrate recognition by Hsp70 proteins (PubMed:11836248). In the unstressed endoplasmic reticulum, interacts with the luminal region of ERN1/IRE1 and selectively recruits HSPA5/BiP: HSPA5/BiP disrupts the dimerization of the active ERN1/IRE1 luminal region, thereby inactivating ERN1/IRE1 (By similarity). Also involved in endoplasmic reticulum-associated degradation (ERAD) of misfolded proteins (PubMed:22267725). Required for survival of B-cell progenitors and normal antibody production (PubMed:25222125). {ECO:0000250|UniProtKB:G3H0N9, ECO:0000269|PubMed:11836248, ECO:0000269|PubMed:22267725, ECO:0000269|PubMed:25222125}. PTM: Not N-glycosylated. {ECO:0000269|PubMed:11836248}. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000269|PubMed:22267725, ECO:0000305|PubMed:11836248}. SUBUNIT: Interacts with HSPA5/BiP; interaction is direct (PubMed:11836248). Interacts with ERN1/IRE1 (via the luminal region) (By similarity). Interacts with DERL1 (PubMed:22267725). {ECO:0000250|UniProtKB:G3H0N9, ECO:0000269|PubMed:11836248, ECO:0000269|PubMed:22267725}. DOMAIN: The J domain stimulates the ATPase activity of HSPA5/BiP, while the divergent targeting domain is required for efficient substrate recognition by HSPA5/BiP. The divergent targeting domain specifically recognizes and binds to aggregation-prone sequences. {ECO:0000269|PubMed:27546788}. +Q91YW3 DNJC3_MOUSE DnaJ homolog subfamily C member 3 (Interferon-induced, double-stranded RNA-activated protein kinase inhibitor) (Protein kinase inhibitor of 58 kDa) (Protein kinase inhibitor p58) 504 57,464 Chain (1); Disulfide bond (2); Domain (1); Helix (19); Modified residue (1); Mutagenesis (5); Region (1); Repeat (9); Sequence conflict (3); Signal peptide (1) FUNCTION: Involved in the unfolded protein response (UPR) during endoplasmic reticulum (ER) stress. Acts as a negative regulator of the EIF2AK4/GCN2 kinase activity by preventing the phosphorylation of eIF-2-alpha at 'Ser-52' and hence attenuating general protein synthesis under ER stress, hypothermic and amino acid starving stress conditions (PubMed:25329545). Co-chaperone of HSPA8/HSC70, it stimulates its ATPase activity. May inhibit both the autophosphorylation of EIF2AK2/PKR and the ability of EIF2AK2 to catalyze phosphorylation of the EIF2A. May inhibit EIF2AK3/PERK activity (By similarity). {ECO:0000250|UniProtKB:Q13217, ECO:0000250|UniProtKB:Q27968, ECO:0000269|PubMed:12446838, ECO:0000269|PubMed:20184891, ECO:0000269|PubMed:25329545}. SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:12446838}. SUBUNIT: Interacts with EIF2AK4/GCN2; this interaction occurs under endoplasmic reticulum (ER) stress, hypothermic and amino acid starving stress conditions and inhibits EIF2AK4/GCN2 kinase activity (PubMed:25329545). Interacts with EIF2AK3 (PubMed:12446838). Interacts with EIF2AK2. Forms a trimeric complex with DNAJB1 and HSPA8. Interacts with THAP12 (By similarity). {ECO:0000250|UniProtKB:Q13217, ECO:0000269|PubMed:12446838, ECO:0000269|PubMed:25329545}. DOMAIN: The J domain mediates interaction with HSPA8. {ECO:0000250}.; DOMAIN: Binding to misfolded proteins is mediated by a hydrophobic patch forming a large groove within the first two TPR repeats. TISSUE SPECIFICITY: Widely expressed, with high level in the liver. {ECO:0000269|PubMed:8666242}. +Q99JG2 G37L1_MOUSE G-protein coupled receptor 37-like 1 (Endothelin B receptor-like protein 2) (ETBR-LP-2) 481 52,729 Chain (1); Compositional bias (1); Disulfide bond (1); Erroneous initiation (1); Glycosylation (1); Modified residue (2); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 135 155 Helical; Name=1. {ECO:0000255}.; TRANSMEM 168 188 Helical; Name=2. {ECO:0000255}.; TRANSMEM 206 226 Helical; Name=3. {ECO:0000255}.; TRANSMEM 252 272 Helical; Name=4. {ECO:0000255}.; TRANSMEM 311 331 Helical; Name=5. {ECO:0000255}.; TRANSMEM 361 381 Helical; Name=6. {ECO:0000255}.; TRANSMEM 399 419 Helical; Name=7. {ECO:0000255}. TOPO_DOM 25 134 Extracellular. {ECO:0000255}.; TOPO_DOM 156 167 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 189 205 Extracellular. {ECO:0000255}.; TOPO_DOM 227 251 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 273 310 Extracellular. {ECO:0000255}.; TOPO_DOM 332 360 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 382 398 Extracellular. {ECO:0000255}.; TOPO_DOM 420 481 Cytoplasmic. {ECO:0000255}. FUNCTION: G-protein coupled receptor (PubMed:27072655). Has been shown to bind the neuroprotective and glioprotective factor prosaposin (PSAP), leading to endocytosis followed by an ERK phosphorylation cascade (By similarity). However, other studies have shown that prosaposin does not increase activity (By similarity). It has been suggested that GPR37L1 is a constitutively active receptor which signals through the guanine nucleotide-binding protein G(s) subunit alpha (By similarity). Participates in the regulation of postnatal cerebellar development by modulating the Shh pathway (PubMed:24062445). Regulates baseline blood pressure in females and protects against cardiovascular stress in males (PubMed:29625592). Mediates inhibition of astrocyte glutamate transporters and reduction in neuronal N-methyl-D-aspartate receptor activity (PubMed:28795439). {ECO:0000250|UniProtKB:O60883, ECO:0000269|PubMed:24062445, ECO:0000269|PubMed:27072655, ECO:0000269|PubMed:28795439, ECO:0000269|PubMed:29625592}. PTM: Undergoes metalloprotease-mediated cleavage which reduces its constitutive activity. {ECO:0000269|PubMed:27072655}.; PTM: Ubiquitinated. {ECO:0000250|UniProtKB:O60883}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24062445, ECO:0000269|PubMed:27072655}; Multi-pass membrane protein {ECO:0000255}. Cell projection, cilium membrane {ECO:0000269|PubMed:24062445}; Multi-pass membrane protein {ECO:0000255}. Note=Associates with the basal membrane of Bergmann glia cell primary cilia. {ECO:0000269|PubMed:24062445}. SUBUNIT: Interacts with the PTCH1 receptor. {ECO:0000269|PubMed:24062445}. DOMAIN: The N-terminal region is required for constitutive signal transduction. {ECO:0000250|UniProtKB:O60883}. TISSUE SPECIFICITY: Highly expressed in brain but not in heart or kidney (at protein level) (PubMed:29625592). In the brain, highly expressed in cerebellar Bergmann glia (at protein level) (PubMed:24062445, PubMed:29625592). Detected in the hippocampus but not in the brain stem or neocortex (at protein level) (PubMed:29625592). In several key cardiovascular centers of the central nervous system including the caudal and rostral ventrolateral medulla, the nucleus of the solitary tract, and the A5 nucleus, detected close to, but not within, tyrosine hydroxylase-positive catecholaminergic neurons (at protein level) (PubMed:29625592). Expressed in astrocytes in both gray and white matter and is also detected throughout the brain in some oligodendrocyte precursors (PubMed:28795439). {ECO:0000269|PubMed:24062445, ECO:0000269|PubMed:28795439, ECO:0000269|PubMed:29625592}. +P97855 G3BP1_MOUSE Ras GTPase-activating protein-binding protein 1 (G3BP-1) (EC 3.6.4.12) (EC 3.6.4.13) (ATP-dependent DNA helicase VIII) (GAP SH3 domain-binding protein 1) (HDH-VIII) 465 51,829 Chain (1); Compositional bias (2); Cross-link (1); Domain (2); Modified residue (18) FUNCTION: ATP- and magnesium-dependent helicase (By similarity). Unwinds preferentially partial DNA and RNA duplexes having a 17 bp annealed portion and either a hanging 3' tail or hanging tails at both 5'- and 3'-ends (By similarity). Unwinds DNA/DNA, RNA/DNA, and RNA/RNA substrates with comparable efficiency (By similarity). Acts unidirectionally by moving in the 5' to 3' direction along the bound single-stranded DNA (By similarity). Phosphorylation-dependent sequence-specific endoribonuclease in vitro (PubMed:11604510). Cleaves exclusively between cytosine and adenine and cleaves MYC mRNA preferentially at the 3'-UTR (PubMed:11604510). May be a regulated effector of stress granule assembly (By similarity). {ECO:0000250|UniProtKB:Q13283, ECO:0000269|PubMed:11604510}. PTM: Phosphorylated exclusively on serine residues. Hyperphosphorylated in quiescent fibroblasts. Hypophosphorylation leads to a decrease in endoribonuclease activity. RASA1-dependent phosphorylation of Ser-149 induces a conformational change that prevents self-association. Dephosphorylation after HRAS activation is required for stress granule assembly. Ser-149 phosphorylation induces partial nuclear localization (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:15086518, ECO:0000269|PubMed:8649363}. Perikaryon {ECO:0000269|PubMed:15086518}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q13283}. Nucleus {ECO:0000250|UniProtKB:Q13283}. Note=Cytoplasmic in proliferating cells, can be recruited to the plasma membrane in exponentially growing cells. Cytosolic and partially nuclear in resting cells. Recruited to stress granules in response to arsenite treatment. The unphosphorylated form is recruited to stress granules. HRAS signaling contributes to this process by regulating G3BP dephosphorylation. {ECO:0000250|UniProtKB:Q13283}. SUBUNIT: Homodimer and oligomer (By similarity). Component of a TAU mRNP complex, at least composed of IGF2BP1, ELAVL4 and G3BP1 (PubMed:15086518). Binds to the SH3 domain of Ras GTPase-activating protein (RASA1) in proliferating cells (PubMed:8649363). No interaction in quiescent cells (PubMed:8649363). Interacts with USP10, and may regulate it (By similarity). Interacts with RPTOR and SPAG5; this complex is increased by oxidative stress (By similarity). Interacts with ATXN2L (By similarity). Interacts with STYXL1 (By similarity). {ECO:0000250|UniProtKB:Q13283, ECO:0000269|PubMed:8649363}. DOMAIN: The NTF2 domain mediates multimerization. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. +Q64467 G3PT_MOUSE Glyceraldehyde-3-phosphate dehydrogenase, testis-specific (EC 1.2.1.12) (Spermatogenic cell-specific glyceraldehyde 3-phosphate dehydrogenase 2) (GAPDH-2) (Spermatogenic glyceraldehyde-3-phosphate dehydrogenase) 440 47,657 Active site (1); Beta strand (19); Binding site (7); Chain (1); Compositional bias (3); Helix (13); Modified residue (1); Nucleotide binding (1); Region (3); Sequence conflict (2); Site (1); Turn (8) Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5. FUNCTION: May play an important role in regulating the switch between different pathways for energy production during spermiogenesis and in the spermatozoon. Required for sperm motility and male fertility. {ECO:0000269|PubMed:15546993}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homotetramer. {ECO:0000250}. DOMAIN: The testis-specific N-terminal extension mediates tight association with the cytoskeletal fibrous sheath of the spermatozoa flagellum, possibly via interchain disulfide-bonding of Cys-33 with sheath components. {ECO:0000250}. TISSUE SPECIFICITY: Testis specific. +Q9JHE4 G3ST1_MOUSE Galactosylceramide sulfotransferase (GalCer sulfotransferase) (EC 2.8.2.11) (3'-phosphoadenosine-5'-phosphosulfate:GalCer sulfotransferase) (3'-phosphoadenylylsulfate:galactosylceramide 3'-sulfotransferase) (Cerebroside sulfotransferase) 423 48,968 Chain (1); Glycosylation (2); Sequence conflict (8); Topological domain (2); Transmembrane (1) TRANSMEM 13 35 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 12 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 36 423 Lumenal. {ECO:0000255}. Lipid metabolism; sphingolipid metabolism. FUNCTION: Catalyzes the sulfation of membrane glycolipids. Seems to prefer beta-glycosides at the non-reducing termini of sugar chains attached to a lipid moiety. Catalyzes the synthesis of HSO3-3-galactosylceramide (sulfatide), a major lipid component of the myelin sheath and of HSO3-3-monogalactosylalkylacylglycerol (seminolipid), present in spermatocytes. Also acts on lactosylceramide, galactosyl 1-alkyl-2-sn-glycerol and galactosyl diacylglycerol (in vitro). {ECO:0000269|PubMed:11917099}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain, testis, kidney, stomach, small intestine, liver, and lung. Not detected in heart, skeletal muscle, and spleen. {ECO:0000269|PubMed:10727929}. +Q9CR59 G45IP_MOUSE Growth arrest and DNA damage-inducible proteins-interacting protein 1 (39S ribosomal protein L59, mitochondrial) (MRP-L59) 222 25,820 Chain (1); Coiled coil (1); Compositional bias (1); Motif (1); Sequence conflict (1) FUNCTION: Acts as a negative regulator of G1 to S cell cycle phase progression by inhibiting cyclin-dependent kinases. Inhibitory effects are additive with GADD45 proteins but occurs also in the absence of GADD45 proteins. Acts as a repressor of the orphan nuclear receptor NR4A1 by inhibiting AB domain-mediated transcriptional activity. May be involved in the hormone-mediated regulation of NR4A1 transcriptional activity. May play a role in mitochondrial protein synthesis. {ECO:0000250|UniProtKB:Q8TAE8}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q8TAE8}. Nucleus {ECO:0000250|UniProtKB:Q8TAE8}. Note=Using N-terminally tagged constructs, has been found in the nucleus. C-terminally tagged constructs are targeted exclusively to mitochondria. This discrepancy may be explained by masking of a potential N-terminal mitochondrial targeting signal by the tag. {ECO:0000250|UniProtKB:Q8TAE8}. SUBUNIT: Component of the mitochondrial ribosome large subunit (39S) which comprises a 16S rRNA and about 50 distinct proteins. Interacts with GADD45A, GADD45B and GADD45G. Interacts with NR4A1 via the NR4A1 AB domain. Interacts with ATAD3A and ATAD3B. {ECO:0000250|UniProtKB:Q8TAE8}. +P06745 G6PI_MOUSE Glucose-6-phosphate isomerase (GPI) (EC 5.3.1.9) (Autocrine motility factor) (AMF) (Neuroleukin) (NLK) (Phosphoglucose isomerase) (PGI) (Phosphohexose isomerase) (PHI) 558 62,767 Active site (3); Beta strand (14); Chain (1); Erroneous initiation (1); Helix (36); Initiator methionine (1); Modified residue (12); Sequence conflict (13); Turn (4) Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 2/4. FUNCTION: Besides it's role as a glycolytic enzyme, mammalian GPI can function as a tumor-secreted cytokine and an angiogenic factor (AMF) that stimulates endothelial cell motility. GPI is also a neurotrophic factor (Neuroleukin) for spinal and sensory neurons. PTM: ISGylated. {ECO:0000269|PubMed:16139798}. SUBCELLULAR LOCATION: Cytoplasm. Secreted. SUBUNIT: Homodimer in the catalytically active form, monomer in the secreted form. {ECO:0000269|PubMed:15342241, ECO:0000269|PubMed:16375918}. +Q61010 DTX1_MOUSE E3 ubiquitin-protein ligase DTX1 (EC 2.3.2.27) (FXI-T1) (Protein deltex-1) (Deltex1) (mDTX1) (RING-type E3 ubiquitin transferase DTX1) 627 68,119 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (2); Motif (1); Sequence conflict (1); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: Regulator of Notch signaling, a signaling pathway involved in cell-cell communications that regulates a broad spectrum of cell-fate determinations. Mainly acts as a positive regulator of Notch, but it also acts as a negative regulator, depending on the developmental and cell context. Mediates the antineural activity of Notch, possibly by inhibiting the transcriptional activation mediated by MATCH1. Involved in neurogenesis, lymphogenesis and myogenesis, and may also be involved in MZB (Marginal zone B) cell differentiation. Promotes B-cell development at the expense of T-cell development, suggesting that it can antagonize NOTCH1. Functions as an ubiquitin ligase protein in vivo, mediating ubiquitination and promoting degradation of MEKK1, suggesting that it may regulate the Notch pathway via some ubiquitin ligase activity. {ECO:0000269|PubMed:15684388}. PTM: Ubiquitinated; undergoes 'Lys-29'-linked polyubiquitination catalyzed by ITCH. {ECO:0000250|UniProtKB:Q86Y01}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q86Y01}. Nucleus {ECO:0000250|UniProtKB:Q86Y01}. Note=Predominantly cytoplasmic. Associates with endocytic vesicles. Partially nuclear. {ECO:0000250|UniProtKB:Q86Y01}. SUBUNIT: Homodimer. May form a heterodimer with other members of the Deltex family. Interacts with NOTCH1 via its N-terminal region and EIF3F, the interaction is required for NOTCH1 deubiquitination. Interacts with EP300. Forms a heterodimer with BBAP; the heterodimerization leading to an increase of in vitro ubiquitin ligase activity. Interacts with ITCH. {ECO:0000250|UniProtKB:Q86Y01}. DOMAIN: The WWE domains are thought to mediate some protein-protein interaction, and are frequently found in ubiquitin ligases. {ECO:0000250}. TISSUE SPECIFICITY: Predominantly expressed in the brain and testis. Weakly expressed in the thymus, spleen and ovary. Predominantly expressed in regions containing post-mitotic differentiating neurons. {ECO:0000269|PubMed:11226752, ECO:0000269|PubMed:11731257}. +Q6PDK8 DTX4_MOUSE E3 ubiquitin-protein ligase DTX4 (EC 2.3.2.27) (Protein deltex-4) (Deltex4) (RING-type E3 ubiquitin transferase DTX4) 616 66,821 Chain (1); Domain (2); Frameshift (1); Sequence conflict (1); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: Functions as a ubiquitin ligase protein in vivo, mediating 'Lys48'-linked polyubiquitination and promoting degradation of TBK1, targeting to TBK1 requires interaction with NLRP4 (By similarity). Regulator of Notch signaling, a signaling pathway involved in cell-cell communications that regulates a broad spectrum of cell-fate determinations. {ECO:0000250, ECO:0000269|PubMed:16923970}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with NLRP4. {ECO:0000250|UniProtKB:Q9Y2E6}. DOMAIN: The WWE domains are thought to mediate some protein-protein interaction, and are frequently found in ubiquitin ligases. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain, testis, embryonic fibroblasts and thymocytes. {ECO:0000269|PubMed:15684394, ECO:0000269|PubMed:16923970}. +Q8BK84 DUPD1_MOUSE Dual specificity phosphatase DUPD1 (EC 3.1.3.16) (EC 3.1.3.48) 215 24,192 Active site (1); Chain (1); Domain (1); Region (1) FUNCTION: Dual specificity phosphatase able to dephosphorylate phosphotyrosine, phosphoserine and phosphothreonine residues, with a preference for phosphotyrosine as a substrate. {ECO:0000250|UniProtKB:Q68J44}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q68J44}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q68J44}. TISSUE SPECIFICITY: Skeletal muscle, liver and adipose tissue. {ECO:0000269|PubMed:17498703}. +Q6NXK5 DUS11_MOUSE RNA/RNP complex-1-interacting phosphatase (EC 3.1.3.-) (Dual specificity protein phosphatase 11) (Phosphatase that interacts with RNA/RNP complex 1) 321 37,851 Active site (2); Chain (1); Domain (1); Region (1); Sequence conflict (5) FUNCTION: Possesses RNA 5'-triphosphatase and diphosphatase activities, but displays a poor protein-tyrosine phosphatase activity. In addition, has phosphatase activity with ATP, ADP and O-methylfluorescein phosphate (in vitro). Binds to RNA. May participate in nuclear mRNA metabolism. {ECO:0000250|UniProtKB:O75319}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O75319}. Nucleus speckle {ECO:0000250|UniProtKB:O75319}. SUBUNIT: Monomer. May interact with SFRS7 and SFRS9/SRP30C. {ECO:0000250|UniProtKB:O75319}. +Q8R4V2 DUS15_MOUSE Dual specificity protein phosphatase 15 (EC 3.1.3.16) (EC 3.1.3.48) (Dual specificity protein phosphatase T-DSP10) 235 26,186 Active site (1); Alternative sequence (2); Chain (1); Domain (1); Frameshift (1); Initiator methionine (1); Lipidation (1) FUNCTION: May dephosphorylate MAPK13, ATF2, ERBB3, PDGFRB and SNX6 (By similarity). {ECO:0000250|UniProtKB:Q9H1R2}.; FUNCTION: Isoform 1: May play a role in the regulation of oligodendrocyte differentiation (PubMed:22792334). May play a role in the regulation of myelin formation (By similarity). Involved in the regulation of Erk1/2 phosphorylation in Schwann cells; the signaling may be linked to the regulation of myelination (By similarity). {ECO:0000250|UniProtKB:B4F7B7, ECO:0000269|PubMed:22792334}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9H1R2}; Lipid-anchor; Cytoplasmic side. TISSUE SPECIFICITY: Isoform 1 is expressed in testis; predominantly in developing spermatocytes (at protein level) (PubMed:15138252). Isoform 2 is highly expressed in testis (PubMed:11432789). Expressed in spinal chord and specifically in oligodendroglial cells (PubMed:27532821). Expressed in embryonic brain cortex; down-regulated in mice with experimental autoimmune encephalomyelitis (EAE) (PubMed:22792334). {ECO:0000269|PubMed:11432789, ECO:0000269|PubMed:22792334, ECO:0000269|PubMed:27532821}. +Q8VE01 DUS18_MOUSE Dual specificity protein phosphatase 18 (EC 3.1.3.16) (EC 3.1.3.48) 188 21,119 Active site (1); Chain (1); Domain (1); Region (1) FUNCTION: Can dephosphorylate single and diphosphorylated synthetic MAPK peptides, with preference for the phosphotyrosine and diphosphorylated forms over phosphothreonine. In vitro, dephosphorylates p-nitrophenyl phosphate (pNPP). {ECO:0000250|UniProtKB:Q8NEJ0}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18385140}. Nucleus {ECO:0000250|UniProtKB:Q8NEJ0}. Mitochondrion inner membrane {ECO:0000269|PubMed:18385140}; Peripheral membrane protein {ECO:0000269|PubMed:18385140}; Intermembrane side {ECO:0000269|PubMed:18385140}. Note=Translocates to cytoplasm in response to apoptotic stimuli such as staurosporine treatment. {ECO:0000269|PubMed:18385140}. +P0DN83 DWORF_MOUSE Sarcoplasmic/endoplasmic reticulum calcium ATPase regulator DWORF (SERCA regulator DWORF) (Dwarf open reading frame) (DWORF) 34 3,815 Chain (1); Transmembrane (1) TRANSMEM 12 32 Helical. {ECO:0000255}. FUNCTION: Enhances the activity of ATP2A1/SERCA1 ATPase in sarcoplasmic reticulum by displacing ATP2A1/SERCA1 inhibitors, thereby acting as a key regulator of skeletal muscle activity. Does not directly stimulate SERCA pump activity. Enhances sarcoplasmic reticulum Ca(2+) uptake and myocyte contractility by displacing the SERCA inhibitory peptides sarcolipin (SLN), phospholamban (PLN) and myoregulin (MRLN). {ECO:0000269|PubMed:26816378}. SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:26816378}; Single-pass membrane protein {ECO:0000255}. SUBUNIT: Interacts with ATP2A1/SERCA1. {ECO:0000269|PubMed:26816378}. TISSUE SPECIFICITY: Highly expressed in heart (at protein level). Detected in heart and soleus, a postural muscle group of the hindlimb containing the highest enrichment of slow-twitch muscle fibers. Also expressed in diaphragm, which contains some slow-twitch fibers. Not detected in the quadriceps, a fast-twitch muscle group, or in cardiac atrial muscle. Not expressed in the prenatal heart but gradually increases in abundance postnatally. {ECO:0000269|PubMed:26816378}. +Q8VDW0 DX39A_MOUSE ATP-dependent RNA helicase DDX39A (EC 3.6.4.13) (DEAD box protein 39) 427 49,067 Alternative sequence (1); Chain (1); Cross-link (6); Domain (2); Initiator methionine (1); Modified residue (5); Motif (2); Nucleotide binding (1) FUNCTION: Involved in pre-mRNA splicing. Required for the export of mRNA out of the nucleus (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Can translocate to the cytoplasm in the presence of MX1. {ECO:0000250}. SUBUNIT: Binds ALYREF/THOC4 and DDX39B/BAT1. Interacts with SARNP (By similarity). Interacts with MX1 (By similarity). {ECO:0000250}. +Q9Z111 GA45G_MOUSE Growth arrest and DNA damage-inducible protein GADD45 gamma (Cytokine-responsive protein CR6) 159 17,211 Beta strand (4); Chain (1); Helix (7); Region (1) FUNCTION: Involved in the regulation of growth and apoptosis. Mediates activation of stress-responsive MTK1/MEKK4 MAPKKK. SUBUNIT: Undergoes concentration-dependent homodimerization, which is required for growth inhibititory activity and enhances interaction with PCNA. Interacts with GADD45GIP1. Interacts with PCNA (By similarity). {ECO:0000250}. DOMAIN: Two central helices mediate homodimerization through parallel packing. {ECO:0000250}. +Q91XQ0 DYH8_MOUSE Dynein heavy chain 8, axonemal (Axonemal beta dynein heavy chain 8) (Ciliary dynein heavy chain 8) 4731 541,238 Alternative sequence (2); Chain (1); Coiled coil (5); Compositional bias (1); Erroneous initiation (1); Modified residue (1); Nucleotide binding (2); Region (7); Sequence conflict (60) FUNCTION: Force generating protein of respiratory cilia. Produces force towards the minus ends of microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Involved in sperm motility; implicated in sperm flagellar assembly. {ECO:0000269|PubMed:10602986, ECO:0000269|PubMed:12297094}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 1: Cell projection, cilium, flagellum. Cytoplasm. Note=Detected in sperm tail, with almost exclusive localization to the principal piece. Also detected in the cytoplasm of primary spermatocytes. Location determined using antibody against peptide common to isoform 1 and isoform 2.; SUBCELLULAR LOCATION: Isoform 2: Cell projection, cilium, flagellum. Cytoplasm. Note=Detected in sperm tail, with almost exclusive localization to the principal piece. Also detected in the cytoplasm of primary spermatocytes. Location determined using antibody against peptide common to isoform 1 and isoform 2. SUBUNIT: Consists of at least two heavy chains and a number of intermediate and light chains. DOMAIN: Dynein heavy chains probably consist of an N-terminal stem (which binds cargo and interacts with other dynein components), and the head or motor domain. The motor contains six tandemly-linked AAA domains in the head, which form a ring. A stalk-like structure (formed by two of the coiled coil domains) protrudes between AAA 4 and AAA 5 and terminates in a microtubule-binding site. A seventh domain may also contribute to this ring; it is not clear whether the N-terminus or the C-terminus forms this extra domain. There are four well-conserved and two non-conserved ATPase sites, one per AAA domain. Probably only one of these (within AAA 1) actually hydrolyzes ATP, the others may serve a regulatory function. TISSUE SPECIFICITY: Isoform 1 and/or isoform 2 are expressed in spermatocytes and mature sperm (at protein level). Testis-specific. Accumulates exclusively in mid to late spermatocytes. {ECO:0000269|PubMed:10602986, ECO:0000269|PubMed:12297094, ECO:0000269|PubMed:16054618}. +Q9D9T0 DYDC1_MOUSE DPY30 domain-containing protein 1 175 20,494 Alternative sequence (1); Chain (1); Sequence conflict (1) FUNCTION: Plays a crucial role during acrosome biogenesis. {ECO:0000269|PubMed:19545932}. SUBUNIT: Interacts with SH3GL3. {ECO:0000250}. +Q45VK7 DYHC2_MOUSE Cytoplasmic dynein 2 heavy chain 1 (Cytoplasmic dynein 2 heavy chain) (Dynein cytoplasmic heavy chain 2) (Dynein heavy chain 11) (mDHC11) (Dynein heavy chain isotype 1B) 4306 492,339 Alternative sequence (3); Chain (1); Coiled coil (4); Erroneous initiation (2); Mutagenesis (2); Nucleotide binding (5); Region (8); Sequence conflict (10) FUNCTION: May function as a motor for intraflagellar retrograde transport. Functions in cilia biogenesis. According to PubMed:8666668, it may play a role in transport between endoplasmic reticulum and Golgi or organization of the Golgi in cells. {ECO:0000269|PubMed:16061793, ECO:0000269|PubMed:16229832, ECO:0000269|PubMed:8666668}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:8666668}. Cell membrane {ECO:0000269|PubMed:8666668}; Peripheral membrane protein {ECO:0000269|PubMed:8666668}. Cytoplasm {ECO:0000269|PubMed:8666668}. Note=Localizes to the apical cytoplasm (By similarity). According to PubMed:8666668, it localizes to Golgi apparatus, cytoplasmic vesicle and endoplasmic reticulum (PubMed:8666668). {ECO:0000250|UniProtKB:Q9JJ79, ECO:0000269|PubMed:8666668}. SUBUNIT: The cytoplasmic dynein complex 2 is probably composed by a heavy chain DYNC2H1 homodimer and a number of DYNC2LI1 light intermediate chains. {ECO:0000250}. TISSUE SPECIFICITY: Detected in brain, lung, spleen and kidney (at protein level). Enriched in the ependymal layer lining the lateral ventricles (at protein level). {ECO:0000269|PubMed:11907264, ECO:0000269|PubMed:12432068}. +P50704 DEFA6_MOUSE Alpha-defensin 6/12 (Defensin-related cryptdin-6/12) (Cryptdin-2) 93 10,426 Disulfide bond (3); Natural variant (3); Peptide (1); Propeptide (1); Signal peptide (1) FUNCTION: Has broad-spectrum antimicrobial properties. Has antibacterial activity against the Gram-positive bacterium L.monocytogenes EGD and the Gram-negative bacteria E.coli ML-35p and avirulent S.typhimurium 7953, but not against the mouse-virulent S.typhimurium 14028S. Probably contributes to the antimicrobial barrier function of the small bowel mucosa. {ECO:0000269|PubMed:1500163, ECO:0000269|PubMed:7927786}. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Paneth cells of the small bowel. +A6H8H2 DEN4C_MOUSE DENN domain-containing protein 4C 1906 211,458 Alternative sequence (1); Chain (1); Domain (4); Modified residue (25); Repeat (1) FUNCTION: Guanine nucleotide exchange factor (GEF) activating RAB10. Promotes the exchange of GDP to GTP, converting inactive GDP-bound RAB10 into its active GTP-bound form. Thereby, stimulates SLC2A4/GLUT4 glucose transporter-enriched vesicles delivery to the plasma membrane in response to insulin. {ECO:0000269|PubMed:21454697}. PTM: Phosphorylated in response to insulin. {ECO:0000269|PubMed:21454697}. SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:21454697}. Cell membrane {ECO:0000269|PubMed:21454697}. Cytoplasm, cytosol {ECO:0000269|PubMed:21454697}. Note=Associates with SLC2A4/GLUT4 storage vesicles. +Q91WS7 DEPD7_MOUSE DEP domain-containing protein 7 (Protein TR2/D15) 511 58,479 Chain (1); Domain (1); Sequence conflict (1) TISSUE SPECIFICITY: Strongly expressed in liver and to a lower extent in kidney. {ECO:0000269|PubMed:10568747}. +Q8K2F3 DEPP1_MOUSE Protein DEPP1 (Fat-specific-expressed gene protein) (Protein DEPP) 205 22,525 Chain (1); Sequence conflict (1) FUNCTION: Acts as a critical modulator of FOXO3-induced autophagy via increased cellular ROS. {ECO:0000250|UniProtKB:Q9NTK1}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NTK1}. Peroxisome {ECO:0000250|UniProtKB:Q9NTK1}. Mitochondrion {ECO:0000250|UniProtKB:Q9NTK1}. Note=May localize to aggresomes. {ECO:0000250|UniProtKB:Q9NTK1}. +E9Q557 DESP_MOUSE Desmoplakin (DP) 2883 332,912 Chain (1); Coiled coil (1); Domain (1); Lipidation (1); Modified residue (24); Region (8); Repeat (24) FUNCTION: Major high molecular weight protein of desmosomes. Involved in the organization of the desmosomal cadherin-plakoglobin complexes into discrete plasma membrane domains and in the anchoring of intermediate filaments to the desmosomes. PTM: Ser-2860 is probably phosphorylated by a cAMP-dependent protein kinase. Phosphorylation on Ser-2860 probably affects its association with epidermal, simple cytokeratins and VIM intermediate filaments (By similarity). {ECO:0000250}.; PTM: Substrate of transglutaminase. Some glutamines and lysines are cross-linked to other desmoplakin molecules, to other proteins such as keratin, envoplakin, periplakin and involucrin, and to lipids like omega-hydroxyceramide (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, desmosome {ECO:0000250|UniProtKB:P15924}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P15924}. Cell membrane {ECO:0000269|PubMed:26403541}. Note=Innermost portion of the desmosomal plaque. Colocalizes with epidermal KRT5-KRT14 and simple KRT8-KRT18 keratins and VIM intermediate filaments network (By similarity). Localizes at the intercalated disk in cardiomyocytes (PubMed:26403541). {ECO:0000250|UniProtKB:P15924, ECO:0000269|PubMed:26403541}. SUBUNIT: Homodimer. Interacts with COL17A1 (via cytoplasmic region). Associates (via C-terminal) with KRT5-KRT14 (via rod region), KRT8-KRT18 and VIM intermediate filaments. Interacts with PKP2 (By similarity). Interacts weakly with TMEM65 (PubMed:26403541). {ECO:0000250|UniProtKB:P15924, ECO:0000269|PubMed:26403541}. DOMAIN: Its association with epidermal and simple keratins is dependent on the tertiary structure induced by heterodimerization of these intermediate filaments proteins and most likely involves recognition sites located in the rod domain of these keratins. {ECO:0000250}.; DOMAIN: The N-terminal region is required for localization to the desmosomal plaque and interacts with the N-terminal region of plakophilin 1. {ECO:0000250}.; DOMAIN: The three tandem plakin repeat regions in the C-terminus mediate binding to intermediate filaments. {ECO:0000250}. +Q9CQT7 DESI1_MOUSE Desumoylating isopeptidase 1 (DeSI-1) (EC 3.4.-.-) (PPPDE peptidase domain-containing protein 2) (Protein FAM152B) 168 18,385 Active site (2); Beta strand (5); Chain (1); Domain (1); Helix (7); Sequence conflict (1); Turn (3) FUNCTION: Protease which deconjugates SUMO1, SUMO2 and SUMO3 from some substrate proteins. Has isopeptidase but not SUMO-processing activity. Desumoylates ZBTB46. {ECO:0000269|PubMed:22370726, ECO:0000269|PubMed:22498933}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22370726}. Nucleus {ECO:0000269|PubMed:22370726}. SUBUNIT: Homodimer. {ECO:0000269|PubMed:22370726, ECO:0000269|PubMed:22498933}. +Q30KN4 DFB30_MOUSE Beta-defensin 30 (BD-30) (mBD-30) (Defensin, beta 30) 75 8,734 Chain (1); Disulfide bond (3); Signal peptide (1) FUNCTION: Has antibacterial activity. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +Q7TNV8 DFB34_MOUSE Beta-defensin 34 (BD-34) (mBD-34) (Defensin, beta 34) 81 9,268 Chain (1); Disulfide bond (3); Signal peptide (1) FUNCTION: Has antibacterial activity. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. TISSUE SPECIFICITY: Only expressed in epididymis (caput, corpus and cauda). {ECO:0000269|PubMed:14718547}. +Q8R2I3 DFB35_MOUSE Beta-defensin 35 (BD-35) (mBD-35) (Defensin, beta 35) 63 7,397 Chain (1); Disulfide bond (3); Signal peptide (1) FUNCTION: Has antibacterial activity. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. TISSUE SPECIFICITY: Expressed in testis, epididymis (caput, corpus and cauda), kidney and neonatal and adult brain. {ECO:0000269|PubMed:12644567, ECO:0000269|PubMed:14718547}. +Q5G866 DFA23_MOUSE Alpha-defensin 23 (Defensin-related cryptdin-23) 93 10,510 Disulfide bond (3); Peptide (1); Propeptide (1); Sequence conflict (6); Signal peptide (1) FUNCTION: May have microbicidal activities. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +Q5G864 DFA25_MOUSE Alpha-defensin 25 (Defensin-related cryptdin-25) 92 10,457 Disulfide bond (3); Peptide (1); Propeptide (1); Signal peptide (1) FUNCTION: May have microbicidal activities. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +Q70KL3 DFB39_MOUSE Beta-defensin 39 (BD-39) (mBD-39) (Defensin, beta 39) 74 8,552 Chain (1); Disulfide bond (3); Sequence conflict (1); Signal peptide (1) FUNCTION: Has antibacterial activity. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. TISSUE SPECIFICITY: Only expressed in epididymis (caput, corpus and cauda). {ECO:0000269|PubMed:14718547}. +Q8R2I4 DFB13_MOUSE Beta-defensin 13 (BD-13) (mBD-13) (Defensin, beta 13) 64 7,520 Chain (1); Disulfide bond (3); Signal peptide (1) FUNCTION: Has antibacterial activity. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. TISSUE SPECIFICITY: Expressed in testis and to a lesser extent in epididymis (caput, corpus and cauda). Also weakly expressed in kidneys. {ECO:0000269|PubMed:12644567, ECO:0000269|PubMed:14718547}. +Q7TNV9 DFB14_MOUSE Beta-defensin 14 (BD-14) (mBD-14) (Defensin, beta 14) 67 7,718 Chain (1); Disulfide bond (3); Signal peptide (1) FUNCTION: Has antibacterial activity. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +Q30KP5 DFB18_MOUSE Beta-defensin 18 (BD-18) (mBD-18) (Defensin, beta 18) 85 9,887 Chain (1); Disulfide bond (3); Signal peptide (1) FUNCTION: Has antibacterial activity. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +Q8K3I8 DFB19_MOUSE Beta-defensin 19 (BD-19) (mBD-19) (Defensin, beta 19) (Testis-specific beta-defensin-like protein) 83 9,568 Disulfide bond (3); Peptide (1); Signal peptide (1) FUNCTION: Has antibacterial activity. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. TISSUE SPECIFICITY: Specifically expressed in male gonads (Sertoli cells). {ECO:0000269|PubMed:12128228}. +P50708 DFA10_MOUSE Alpha-defensin 10 (Defensin-related cryptdin-10) 93 10,429 Disulfide bond (3); Peptide (1); Propeptide (1); Signal peptide (1) FUNCTION: Probably contributes to the antimicrobial barrier function of the small bowel mucosa. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Paneth cells of the small bowel. +P50709 DFA11_MOUSE Alpha-defensin 11 (Defensin-related cryptdin-11) (Fragment) 85 9,542 Disulfide bond (3); Non-terminal residue (1); Peptide (1); Propeptide (1); Signal peptide (1) FUNCTION: Probably contributes to the antimicrobial barrier function of the small bowel mucosa. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Paneth cells of the small bowel. +Q64442 DHSO_MOUSE Sorbitol dehydrogenase (EC 1.1.1.14) (L-iditol 2-dehydrogenase) 357 38,249 Binding site (4); Chain (1); Erroneous initiation (1); Initiator methionine (1); Metal binding (3); Modified residue (2); Sequence conflict (2) FUNCTION: Converts sorbitol to fructose. Part of the polyol pathway that plays an important role in sperm physiology. May play a role in the sperm motility by providing an energetic source for sperm. {ECO:0000269|PubMed:18799757}. SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000269|PubMed:18799757}; Peripheral membrane protein {ECO:0000269|PubMed:18799757}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:18799757}. Note=Associated with mitochondria of the midpiece and near the plasma membrane in the principal piece of the flagellum. Also found in the epididymosome, secreted by the epididymal epithelium and that transfers proteins from the epididymal fluid to the sperm surface. SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P07846}. TISSUE SPECIFICITY: Testis has the highest level of expression, followed by kidney, liver, and lung. Low levels of expression are also observed in lens, brain, and skeletal muscle. Expressed in sperm flagellum and very low expression in the sperm head. {ECO:0000269|PubMed:18799757, ECO:0000269|PubMed:7601136}. +P50171 DHB8_MOUSE Estradiol 17-beta-dehydrogenase 8 (EC 1.1.1.62) (17-beta-hydroxysteroid dehydrogenase 8) (17-beta-HSD 8) (3-ketoacyl-[acyl-carrier-protein] reductase alpha subunit) (KAR alpha subunit) (3-oxoacyl-[acyl-carrier-protein] reductase) (EC 1.1.1.-) (Protein Ke6) (Ke-6) (Testosterone 17-beta-dehydrogenase 8) (EC 1.1.1.239) 259 26,588 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Erroneous gene model prediction (1); Modified residue (4); Nucleotide binding (5); Sequence conflict (2) Lipid metabolism; fatty acid biosynthesis. Steroid biosynthesis; estrogen biosynthesis. FUNCTION: NAD-dependent 17-beta-hydroxysteroid dehydrogenase with highest activity towards estradiol. Has very low activity towards testosterone (PubMed:9712896). The heterotetramer with CBR4 has NADH-dependent 3-ketoacyl-acyl carrier protein reductase activity, and thereby plays a role in mitochondrial fatty acid biosynthesis. Within the heterotetramer, HSD17B8 binds NADH; CBR4 binds NADPD. {ECO:0000250|UniProtKB:Q92506, ECO:0000269|PubMed:9712896}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:Q92506}. SUBUNIT: Heterotetramer with CBR4; contains two molecules of HSD17B8 and CBR4. {ECO:0000250|UniProtKB:Q92506}. TISSUE SPECIFICITY: Kidney, liver, testis, ovary, oviduct, uterus, mammary gland, vagina, prostate, clitoral gland and moderately in spleen, heart, dorsal skin, brain and lung. +Q99J87 DHX58_MOUSE Probable ATP-dependent RNA helicase DHX58 (EC 3.6.4.13) (Probable ATP-dependent helicase LGP2) (Protein D11Lgp2) (RIG-I-like receptor 3) (RLR-3) (RIG-I-like receptor Lgp2) (RLR) 678 76,709 Chain (1); Coiled coil (1); Domain (3); Metal binding (4); Motif (1); Mutagenesis (1); Nucleotide binding (1); Region (1); Sequence conflict (3) FUNCTION: Acts as a regulator of DDX58/RIG-I and IFIH1/MDA5 mediated antiviral signaling. Cannot initiate antiviral signaling as it lacks the CARD domain required for activating MAVS/IPS1-dependent signaling events. Can have both negative and positive regulatory functions related to DDX58/RIG-I and IFIH1/MDA5 signaling and this role in regulating signaling may be complex and could probably depend on characteristics of the infecting virus or target cells, or both. Its inhibitory action on DDX58/RIG-I signaling may involve the following mechanisms: competition with DDX58/RIG-I for binding to the viral RNA, binding to DDX58/RIG-I and inhibiting its dimerization and interaction with MAVS/IPS1, competing with IKBKE in its binding to MAVS/IPS1 thereby inhibiting activation of interferon regulatory factor 3 (IRF3). Its positive regulatory role may involve unwinding or stripping nucleoproteins of viral RNA thereby facilitating their recognition by DDX58/RIG-I and IFIH1/MDA5. Involved in the innate immune response to various RNA viruses and some DNA viruses such as poxviruses, and also to the bacterial pathogen Listeria monocytogenes. Can bind both ssRNA and dsRNA, with a higher affinity for dsRNA. Shows a preference to 5'-triphosphorylated RNA, although it can recognize RNA lacking a 5'-triphosphate. {ECO:0000269|PubMed:17475874, ECO:0000269|PubMed:20080593, ECO:0000269|PubMed:21525357, ECO:0000269|PubMed:21533147}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11735219}. SUBUNIT: Monomer in the absence of dsRNA. Homodimer in the presence of dsRNA. Interacts with DDX58/RIG-I (via CARD domain), MAVS/IPS1 and DDX60. Found in a complex with DDX58/RIG-I and IFIH1/MDA5. Interacts with ANKRD17. Directly interacts with ATG5 and ATG12, either as ATG5 and ATG12 monomers or as ATG12-ATG5 conjugates (By similarity). {ECO:0000250|UniProtKB:Q96C10}. DOMAIN: The RLR CTR domain is capable of inhibiting dimerization and signaling of DDX58/RIG-I and also facilitates binding of dsRNA. TISSUE SPECIFICITY: Highly expressed in mammary tissues. Expressed in liver and testis. Expressed at lower level in spleen, embryo, mammary gland and breast tumors. {ECO:0000269|PubMed:11735219}. +Q8BWT5 DIP2A_MOUSE Disco-interacting protein 2 homolog A (DIP2 homolog A) 1523 165,255 Chain (1); Compositional bias (2); Domain (1); Modified residue (2); Sequence conflict (2) FUNCTION: May provide positional cues for axon pathfinding and patterning in the central nervous system. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: Developing nervous system. {ECO:0000269|PubMed:12137943}. +Q61483 DLL1_MOUSE Delta-like protein 1 (Drosophila Delta homolog 1) (Delta1) [Cleaved into: Dll1-soluble form (Dll1-EC) (Shed form); Dll1-derived cell-associated form (Dll1-TMIC) (Membrane-associated fragment); Dll1-intracellular form (Dll1-IC)] 722 78,449 Chain (4); Cross-link (1); Disulfide bond (27); Domain (9); Glycosylation (1); Modified residue (3); Mutagenesis (8); Region (1); Sequence conflict (1); Signal peptide (1); Site (2); Topological domain (2); Transmembrane (1) TRANSMEM 546 568 Helical. {ECO:0000255}. TOPO_DOM 18 545 Extracellular. {ECO:0000255}.; TOPO_DOM 569 722 Cytoplasmic. {ECO:0000255}. FUNCTION: Transmembrane ligand protein of NOTCH1, NOTCH2 and NOTCH3 receptors that binds the extracellular domain (ECD) of Notch receptor in a cis and trans fashion manner (PubMed:21985982, PubMed:10958687). Following transinteraction, ligand cells produce mechanical force that depends of a clathrin-mediated endocytosis, requiring ligand ubiquitination, EPN1 interaction, and actin polymerisation; these events promote Notch receptor extracellular domain (NECD) transendocytosis and triggers Notch signaling through induction of cleavage, hyperphosphorylation, and nuclear accumulation of the intracellular domain of Notch receptors (NICD) (PubMed:10958687, PubMed:18676613). Is required for embryonic development and maintenance of adult stem cells in many different tissues and immune systeme; the DLL1-induced Notch signaling is mediated through an intercellular communication that regulates cell lineage, cell specification, cell patterning and morphogenesis through effects on differentiation and proliferation (PubMed:17194759, PubMed:19562077, PubMed:18997111, PubMed:23695674, PubMed:16495313, PubMed:21238454, PubMed:22282195, PubMed:7671806, PubMed:17960184, PubMed:22529374, PubMed:19389377, PubMed:23699523, PubMed:19144989, PubMed:23688253, PubMed:23806616, PubMed:26114479, PubMed:22940113, PubMed:25220152, PubMed:20081190, PubMed:21572390, PubMed:22096075). Plays a role in brain development at different level, namely by regulating neuronal differentiation of neural precursor cells via cell-cell interaction, most likely through the lateral inhibitory system in an endogenous level dependent-manner (PubMed:7671806, PubMed:18997111). During neocortex development, Dll1-Notch signaling transmission is mediated by dynamic interactions between intermediate neurogenic progenitors and radial glia; the cell-cell interactions are mediated via dynamic and transient elongation processes, likely to reactivate/maintain Notch activity in neighboring progenitors, and coordinate progenitor cell division and differentiation across radial and zonal boundaries (PubMed:23699523). During cerebellar development, regulates Bergmann glial monolayer formation and its morphological maturation through a Notch signaling pathway (PubMed:23688253). At the retina and spinal cord level, regulates neurogenesis by preventing the premature differentiation of neural progenitors and also by maintaining progenitors in spinal cord through Notch signaling pathway (PubMed:19389377, PubMed:26114479). Also controls neurogenesis of the neural tube in a progenitor domain-specific fashion along the dorsoventral axis (PubMed:20081190). Maintains quiescence of neural stem cells and plays a role as a fate determinant that segregates asymmetrically to one daughter cell during neural stem cells mitosis, resulting in neuronal differentiation in Dll1-inheriting cell (PubMed:23695674). Plays a role in immune systeme development, namely the development of all T-cells and marginal zone (MZ) B cells (PubMed:15146182, PubMed:19217325). Blocks the differentiation of progenitor cells into the B-cell lineage while promoting the emergence of a population of cells with the characteristics of a T-cell/NK-cell precursor (By similarity). Upon MMP14 cleavage, negatively regulates Notch signaling in haematopoietic progenitor cells to specifically maintain normal B-cell development in bone marrow (PubMed:21572390). Also plays a role during muscle development. During early development, inhibits myoblasts differentiation from the medial dermomyotomal lip and later regulates progenitor cell differentiation (PubMed:17194759). Directly modulates cell adhesion and basal lamina formation in satellite cells through Notch signaling. Maintains myogenic progenitors pool by suppressing differentiation through down-regulation of MYOD1 and is required for satellite cell homing and PAX7 expression (PubMed:22940113). During craniofacial and trunk myogenesis suppresses differentiation of cranial mesoderm-derived and somite-derived muscle via MYOD1 regulation but in cranial mesoderm-derived progenitors, is neither required for satellite cell homing nor for PAX7 expression (PubMed:25220152). Also plays a role during pancreatic cell development. During type B pancreatic cell development, may be involved in the initiation of proximodistal patterning in the early pancreatic epithelium (PubMed:22529374). Stimulates multipotent pancreatic progenitor cells proliferation and pancreatic growth by maintaining HES1 expression and PTF1A protein levels (PubMed:22096075). During fetal stages of development, is required to maintain arterial identity and the responsiveness of arterial endothelial cells for VEGFA through regulation of KDR activation and NRP1 expression (PubMed:19144989). Controls sprouting angiogenesis and subsequent vertical branch formation througth regulation on tip cell differentiation (PubMed:22282195). Negatively regulates goblet cell differentiation in intestine and controls secretory fat commitment through lateral inhibition in small intestine (PubMed:21238454, PubMed:21915337). Plays a role during inner ear development; negatively regulates auditory hair cell differentiation (PubMed:16495313). Plays a role during nephron development through Notch signaling pathway (PubMed:23806616). Regulates growth, blood pressure and energy homeostasis (PubMed:19562077). {ECO:0000250|UniProtKB:O00548, ECO:0000250|UniProtKB:P97677, ECO:0000269|PubMed:10958687, ECO:0000269|PubMed:15146182, ECO:0000269|PubMed:16495313, ECO:0000269|PubMed:17194759, ECO:0000269|PubMed:17960184, ECO:0000269|PubMed:18676613, ECO:0000269|PubMed:18997111, ECO:0000269|PubMed:19144989, ECO:0000269|PubMed:19217325, ECO:0000269|PubMed:19389377, ECO:0000269|PubMed:19562077, ECO:0000269|PubMed:20081190, ECO:0000269|PubMed:21238454, ECO:0000269|PubMed:21572390, ECO:0000269|PubMed:21915337, ECO:0000269|PubMed:21985982, ECO:0000269|PubMed:22096075, ECO:0000269|PubMed:22282195, ECO:0000269|PubMed:22529374, ECO:0000269|PubMed:22940113, ECO:0000269|PubMed:23688253, ECO:0000269|PubMed:23695674, ECO:0000269|PubMed:23699523, ECO:0000269|PubMed:23806616, ECO:0000269|PubMed:25220152, ECO:0000269|PubMed:26114479, ECO:0000269|PubMed:7671806}. PTM: Ubiquitinated by MIB (MIB1 or MIB2), leading to its endocytosis and subsequent degradation. Ubiquitinated; promotes recycling back to the plasma membrane and confers a strong affinity for NOTCH1 (PubMed:18676613). Multi-ubiquitination of LYS-613 by MIB1 promotes both cis and trans-interaction with NOTCH1, as well as activation of Notch signaling (PubMed:21985982). Ubiquitinated by NEURL1B (PubMed:17003037). {ECO:0000250|UniProtKB:P10041, ECO:0000269|PubMed:17003037, ECO:0000269|PubMed:18676613, ECO:0000269|PubMed:21985982}.; PTM: Phosphorylated in a membrane association-dependent manner. Phosphorylation at Ser-696 requires the presence of Ser-693, whereas phosphorylation at Thr-638 and Ser-693 occurs independently of the other sites. Phosphorylation is required for full ligand activity in vitro and affects surface presentation, ectodomain shedding, and endocytosis. {ECO:0000269|PubMed:24449764}.; PTM: Cleaved by MMP14; negatively regulates DLL1-induced Notch signaling in HPCs, modulating B-lymphocyte differentiation in bone marrow (PubMed:21572390). Undergoes two consecutive processing events: a shedding event, partially by ADAM10, that generates a soluble extracellular form and an intracellular membrane-anchored form, followed by a gamma-secretase cleavage releasing an intracellular fragment (PubMed:12794186). {ECO:0000269|PubMed:12794186, ECO:0000269|PubMed:21572390}.; PTM: O-fucosylated. Can be elongated to a disaccharide by MFNG. {ECO:0000250|UniProtKB:P97677}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:24715457}; Single-pass type I membrane protein {ECO:0000269|PubMed:24715457}. Cell junction, adherens junction {ECO:0000269|PubMed:15908431, ECO:0000269|PubMed:24715457}. Membrane raft {ECO:0000269|PubMed:18676613, ECO:0000269|PubMed:21985982}. Note=Distributed around adherens junction in the apical endfeet through interactions with MAGI1. {ECO:0000269|PubMed:15908431, ECO:0000269|PubMed:24715457}.; SUBCELLULAR LOCATION: Dll1-derived cell-associated form: Cell membrane {ECO:0000269|PubMed:12794186}.; SUBCELLULAR LOCATION: Dll1-intracellular form: Nucleus {ECO:0000269|PubMed:12794186}. SUBUNIT: Homodimer (PubMed:12794186). Interacts with TJP1 (PubMed:24715457). Interacts with MMP14; inhibits DLL1-induced Notch signaling (PubMed:21572390). Interacts with MAGI1 (via PDZ domain); forms a complex with CTNNB1 and CDH2 and promotes recruitment to the adherens junction and stabilization on the cell surface (PubMed:15908431). Interacts with PSEN1; undergoes a presenilin-dependent gamma-secretase cleavage that releases a Dll1-intracellular form (PubMed:12794186). Interacts with MFAP5 (PubMed:15788413). Interacts with MIB1 (PubMed:21985982). Interacts with NEURL1B; leads to ubiquitination (PubMed:17003037, PubMed:19723503). Interacts with NEURL1 (PubMed:19723503). Interacts with SYNJ2BP; enhances DLL1 protein stability, and promotes Notch signaling in endothelial cells (By similarity). Interacts with MAGI1, MAGI2, MAGI3 and MPDZ (By similarity). Interacts (via ubiquitin) with EPN1 (via IUM domain); binding with NOTCH1 attached to neighboring cell, promotes ligand ubiquitination and EPN1 interaction, leading to NECD transendocytosis and Notch signaling. Interacts with NOTCH1 (By similarity). {ECO:0000250|UniProtKB:O00548, ECO:0000250|UniProtKB:P97677, ECO:0000269|PubMed:12794186, ECO:0000269|PubMed:15788413, ECO:0000269|PubMed:15908431, ECO:0000269|PubMed:17003037, ECO:0000269|PubMed:19723503, ECO:0000269|PubMed:21572390, ECO:0000269|PubMed:21985982, ECO:0000269|PubMed:24715457}. TISSUE SPECIFICITY: In the embryo, expressed in the paraxial mesoderm and nervous system. Expressed at high levels in adult heart and at lower levels, in adult lung. Highly expressed in satellite cells from masseter and tongue than in satellite cells from leg and extraocular muscle.? (PubMed:25220152). {ECO:0000269|PubMed:25220152, ECO:0000269|PubMed:7671806}. +Q9QYZ8 DKK2_MOUSE Dickkopf-related protein 2 (Dickkopf-2) (Dkk-2) (mDkk-2) 259 28,432 Beta strand (8); Chain (1); Disulfide bond (5); Glycosylation (1); Helix (1); Region (2); Sequence conflict (1); Signal peptide (1) FUNCTION: Antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by forming a ternary complex with the transmembrane protein KREMEN that promotes internalization of LRP5/6. DKKs play an important role in vertebrate development, where they locally inhibit Wnt regulated processes such as antero-posterior axial patterning, limb development, somitogenesis and eye formation. In the adult, Dkks are implicated in bone formation and bone disease, cancer and Alzheimer disease. {ECO:0000269|PubMed:18524778}. PTM: May be proteolytically processed by a furin-like protease. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Interacts with LRP5 and LRP6. {ECO:0000269|PubMed:18524778}. DOMAIN: The C-terminal cysteine-rich domain mediates interaction with LRP5 and LRP6. +Q8BLA1 DLEC1_MOUSE Deleted in lung and esophageal cancer protein 1 homolog 635 71,183 Chain (1) FUNCTION: May act as a tumor suppressor by inhibiting cell proliferation. {ECO:0000250|UniProtKB:Q9Y238}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +Q9D7K5 DMAC2_MOUSE Distal membrane-arm assembly complex protein 2 (ATP synthase subunit s-like protein) 258 29,179 Chain (1) FUNCTION: Required for the assembly of the mitochondrial NADH:ubiquinone oxidoreductase complex (complex I). Involved in the assembly of the distal region of complex I. {ECO:0000250|UniProtKB:Q9NW81}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:18614015}. SUBUNIT: Interacts with incompletely assembled mitochondrial NADH:ubiquinone oxidoreductase complex (complex I). {ECO:0000250|UniProtKB:Q9NW81}. +B1AZP2 DLGP4_MOUSE Disks large-associated protein 4 (DAP-4) (PSD-95/SAP90-binding protein 4) (SAP90/PSD-95-associated protein 4) (SAPAP-4) 992 108,037 Alternative sequence (3); Chain (1); Modified residue (18); Sequence caution (1); Sequence conflict (7) FUNCTION: May play a role in the molecular organization of synapses and neuronal cell signaling. Could be an adapter protein linking ion channel to the subsynaptic cytoskeleton. May induce enrichment of PSD-95/SAP90 at the plasma membrane (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. SUBUNIT: Interacts with DLG1 and DLG4/PSD-95. {ECO:0000250}. +Q9EQD0 FZD5_MOUSE Frizzled-5 (Fz-5) (mFz5) 585 64,138 Chain (1); Disulfide bond (5); Domain (1); Frameshift (1); Glycosylation (2); Motif (1); Sequence conflict (9); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 239 259 Helical; Name=1. {ECO:0000255}.; TRANSMEM 271 291 Helical; Name=2. {ECO:0000255}.; TRANSMEM 316 336 Helical; Name=3. {ECO:0000255}.; TRANSMEM 359 379 Helical; Name=4. {ECO:0000255}.; TRANSMEM 403 423 Helical; Name=5. {ECO:0000255}.; TRANSMEM 450 470 Helical; Name=6. {ECO:0000255}.; TRANSMEM 501 521 Helical; Name=7. {ECO:0000255}. TOPO_DOM 27 238 Extracellular. {ECO:0000255}.; TOPO_DOM 260 270 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 292 315 Extracellular. {ECO:0000255}.; TOPO_DOM 337 358 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 380 402 Extracellular. {ECO:0000255}.; TOPO_DOM 424 449 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 471 500 Extracellular. {ECO:0000255}.; TOPO_DOM 522 585 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for Wnt proteins (PubMed:11092808, PubMed:18230341). Can activate WNT2, WNT10B, WNT5A, but not WNT2B or WNT4 (in vitro); the in vivo situation may be different since not all of these are known to be coexpressed (PubMed:11092808). In neurons, activation of WNT7A promotes formation of synapses (By similarity). Functions in the canonical Wnt/beta-catenin signaling pathway (PubMed:18230341). The canonical Wnt/beta-catenin signaling pathway leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes (PubMed:18230341). A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues (Probable). Plays a role in yolk sac angiogenesis and in placental vascularization (PubMed:11092808). {ECO:0000250|UniProtKB:Q8CHL0, ECO:0000269|PubMed:11092808, ECO:0000269|PubMed:18230341, ECO:0000305}. PTM: Ubiquitinated by RNF43 and ZNRF3, leading to its degradation by the proteasome. {ECO:0000250|UniProtKB:Q13467}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11520064, ECO:0000269|PubMed:20530549}; Multi-pass membrane protein {ECO:0000305}. Golgi apparatus membrane {ECO:0000269|PubMed:11520064}; Multi-pass membrane protein {ECO:0000305}. Cell junction, synapse {ECO:0000269|PubMed:20530549}. Perikaryon {ECO:0000250|UniProtKB:Q8CHL0}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q8CHL0}. Cell projection, axon {ECO:0000250|UniProtKB:Q8CHL0}. Note=Localized at the plasma membrane and also found at the Golgi. {ECO:0000269|PubMed:11520064}. SUBUNIT: Binding of unsaturated fatty acid molecules (via FZ domain) promotes homodimerization (via FZ domain). Interacts with WNT2B (By similarity). Interacts with WNT7A (PubMed:18230341, PubMed:20530549). Interacts with GOPC (PubMed:11520064). {ECO:0000250|UniProtKB:Q13467, ECO:0000269|PubMed:11520064, ECO:0000269|PubMed:18230341, ECO:0000269|PubMed:20530549}. DOMAIN: The PDZ-binding motif mediates interaction with GOPC. {ECO:0000250}.; DOMAIN: The FZ domain is involved in binding with Wnt ligands. {ECO:0000250}. TISSUE SPECIFICITY: Detected in hippocampus (at protein level) (PubMed:20530549). Expressed in eye, kidney, lung, chondrocytes, epithelial cells of the small intestine and gobelet cells of the colon (PubMed:8626800). {ECO:0000269|PubMed:20530549, ECO:0000269|PubMed:8626800}. +Q8CFX1 G6PE_MOUSE GDH/6PGL endoplasmic bifunctional protein [Includes: Glucose 1-dehydrogenase (EC 1.1.1.47) (Glucose-6-phosphate dehydrogenase) (EC 1.1.1.363); 6-phosphogluconolactonase (6PGL) (EC 3.1.1.31)] 789 88,928 Active site (1); Binding site (4); Chain (1); Erroneous initiation (1); Glycosylation (3); Modified residue (3); Region (3); Sequence conflict (9); Signal peptide (1) FUNCTION: Oxidizes glucose-6-phosphate and glucose, as well as other hexose-6-phosphates. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250}. Note=Microsomes, endoplasmic reticulum lumen. {ECO:0000250}. +Q05AA6 DRP2_MOUSE Dystrophin-related protein 2 (DRP-2) 957 108,050 Chain (1); Domain (1); Modified residue (2); Repeat (2); Sequence conflict (2); Zinc finger (1) FUNCTION: Required for normal myelination and for normal organization of the cytoplasm and the formation of Cajal bands in myelinating Schwann cells (PubMed:22764250). Required for normal PRX location at appositions between the abaxonal surface of the myelin sheath and the Schwann cell plasma membrane (PubMed:22764250). Possibly involved in membrane-cytoskeleton interactions of the central nervous system. {ECO:0000250, ECO:0000269|PubMed:22764250}. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250|UniProtKB:Q9EPA0}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9EPA0}. Perikaryon {ECO:0000250|UniProtKB:Q9EPA0}. Cell membrane {ECO:0000269|PubMed:11430802, ECO:0000269|PubMed:22764250, ECO:0000269|PubMed:23152929}; Peripheral membrane protein {ECO:0000269|PubMed:22764250}. Note=Detected in Schwann cells at periaxonal myelin membranes. {ECO:0000269|PubMed:22764250}. SUBUNIT: Interacts with PRX; this enhances phosphorylation (PubMed:22764250). Identified in a dystroglycan complex that contains at least PRX, DRP2, UTRN, DMD and DAG1 (PubMed:11430802). {ECO:0000269|PubMed:11430802, ECO:0000269|PubMed:22764250}. TISSUE SPECIFICITY: Detected in quadriceps nerve Schwann cells (PubMed:22764250). Detected in sciatic nerve (PubMed:11430802, PubMed:22764250). Detected in trigeminal nerve Schwann cells (at protein level) (PubMed:11430802). Detected in brain and spinal cord (PubMed:8640231). {ECO:0000269|PubMed:11430802, ECO:0000269|PubMed:22764250, ECO:0000269|PubMed:8640231}. +Q8R3P2 DTX2_MOUSE Probable E3 ubiquitin-protein ligase DTX2 (EC 2.3.2.27) (Protein deltex-2) (Deltex2) (mDTX2) (RING-type E3 ubiquitin transferase DTX2) 619 67,195 Alternative sequence (3); Beta strand (5); Chain (1); Domain (2); Helix (2); Modified residue (5); Sequence conflict (1); Turn (3); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: Regulator of Notch signaling, a signaling pathway involved in cell-cell communications that regulates a broad spectrum of cell-fate determinations. Probably acts both as a positive and negative regulator of Notch, depending on the developmental and cell context. Mediates the antineural activity of Notch, possibly by inhibiting the transcriptional activation mediated by MATCH1. Functions as a ubiquitin ligase protein in vitro, suggesting that it may regulate the Notch pathway via some ubiquitin ligase activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q86UW9}. Nucleus {ECO:0000250|UniProtKB:Q86UW9}. Note=Predominantly cytoplasmic. Partially nuclear. {ECO:0000250|UniProtKB:Q86UW9}. SUBUNIT: Homodimer. May form a heterodimer with other members of the Deltex family. Interacts with NOTCH1. {ECO:0000269|PubMed:11226752}. DOMAIN: The WWE domains are thought to mediate some protein-protein interaction, and are frequently found in ubiquitin ligases. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in testis and the CNS. {ECO:0000269|PubMed:11226752}. DISEASE: Note=Recurrent site of retroviral integration in murine B-cell lymphomas. +Q3UIR3 DTX3L_MOUSE E3 ubiquitin-protein ligase DTX3L (EC 2.3.2.27) (Protein deltex-3-like) (RING-type E3 ubiquitin transferase DTX3L) 748 83,044 Alternative sequence (1); Chain (1); Frameshift (1); Initiator methionine (1); Modified residue (4); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase which, in association with ADP-ribosyltransferase PARP9, plays a role in DNA damage repair and in interferon-mediated antiviral responses. Monoubiquitinates several histones, including histone H2A, H2B, H3 and H4. In response to DNA damage, mediates monoubiquitination of 'Lys-91' of histone H4 (H4K91ub1). The exact role of H4K91ub1 in DNA damage response is still unclear but it may function as a licensing signal for additional histone H4 post-translational modifications such as H4 'Lys-20' methylation (H4K20me). PARP1-dependent PARP9-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage sites. By monoubiquitinating histone H2B HIST1H2BH/H2BJ and thereby promoting chromatin remodeling, positively regulates STAT1-dependent interferon-stimulated gene transcription and thus STAT1-mediated control of viral replication. Independently of its catalytic activity, promotes the sorting of chemokine receptor CXCR4 from early endosome to lysosome following CXCL12 stimulation by reducing E3 ligase ITCH activity and thus ITCH-mediated ubiquitination of endosomal sorting complex required for transport ESCRT-0 components HGS and STAM. In addition, required for the recruitment of HGS and STAM to early endosomes. {ECO:0000250|UniProtKB:Q8TDB6}. PTM: Autoubiquitinated. {ECO:0000250|UniProtKB:Q8TDB6}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8TDB6}. Nucleus {ECO:0000250|UniProtKB:Q8TDB6}. Early endosome membrane {ECO:0000250|UniProtKB:Q8TDB6}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8TDB6}; Cytoplasmic side {ECO:0000250|UniProtKB:Q8TDB6}. Lysosome membrane {ECO:0000250|UniProtKB:Q8TDB6}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8TDB6}; Cytoplasmic side {ECO:0000250|UniProtKB:Q8TDB6}. Note=Translocates to the nucleus in response to IFNG or IFNB1 stimulation. Localizes at sites of DNA damage in a PARP1-dependent manner. Localization to early endosomes is increased upon CXCL12 stimulation where it co-localizes with ITCH, CXCL4, HGS and STAM. A minor proportion localizes to lysosomes. {ECO:0000250|UniProtKB:Q8TDB6}. SUBUNIT: Homodimer and heterodimer. Can heterodimerize with DTX1, enhancing its ubiquitin ligase activity in vitro. Interacts (via N-terminus) with ADP ribosyltransferase PARP9/BAL1 (via PARP catalytic domain) forming a stable complex; the interaction is required to activate PARP9 but is dispensable for DTX3L catalytic activity. Forms a complex with STAT1 and PARP9 independently of IFNB1 or IFNG-mediated STAT1 'Tyr-701' phosphorylation. Found in a complex with PARP9, STAT1 and HIST1H2BH. Found in a complex with E3 ligase ITCH and ESCRT-0 components HGS and STAM. Interacts (via C-terminus) with ITCH; the interaction is increased upon CXCL12 stimulation and inhibits ITCH catalytic activity; the interaction is direct. Interacts with HGS and STAM; the interaction brings together HGS and STAM and promotes their recruitment to early endosomes. {ECO:0000250|UniProtKB:Q8TDB6}. +Q80V91 DTX3_MOUSE Probable E3 ubiquitin-protein ligase DTX3 (EC 2.3.2.27) (Protein deltex-3) (Deltex3) (mDTX3) (RING-type E3 ubiquitin transferase DTX3) 347 37,982 Chain (1); Compositional bias (1); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: Regulator of Notch signaling, a signaling pathway involved in cell-cell communications that regulates a broad spectrum of cell-fate determinations. Probably acts both as a positive and negative regulator of Notch, depending on the developmental and cell context. Functions as a ubiquitin ligase protein in vitro, suggesting that it may regulate the Notch pathway via some ubiquitin ligase activity. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. SUBUNIT: Homodimer. May form a heterodimer with other members of the Deltex family. Interacts with NOTCH1. TISSUE SPECIFICITY: Strongly expressed in testis and brain. Weakly expressed in kidney. {ECO:0000269|PubMed:11226752}. +Q9ESS0 DUS10_MOUSE Dual specificity protein phosphatase 10 (EC 3.1.3.16) (EC 3.1.3.48) (Mitogen-activated protein kinase phosphatase 5) (MAP kinase phosphatase 5) (MKP-5) 483 52,532 Active site (1); Chain (1); Domain (2); Region (1); Sequence conflict (3) FUNCTION: Protein phosphatase involved in the inactivation of MAP kinases. Has a specificity for the MAPK11/MAPK12/MAPK13/MAPK14 subfamily. It preferably dephosphorylates p38. {ECO:0000250|UniProtKB:Q9Y6W6}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y6W6}. Nucleus {ECO:0000250|UniProtKB:Q9Y6W6}. SUBUNIT: Monomer. Interacts with MAPK14. {ECO:0000250|UniProtKB:Q9Y6W6}. +Q9D0T2 DUS12_MOUSE Dual specificity protein phosphatase 12 (EC 3.1.3.16) (EC 3.1.3.48) (Dual specificity phosphatase T-DSP4) (Dual specificity phosphatase VH1) 339 37,159 Active site (1); Chain (1); Domain (1); Modified residue (2); Region (1); Sequence conflict (1) FUNCTION: Dual specificity phosphatase; can dephosphorylate both phosphotyrosine and phosphoserine or phosphothreonine residues. Can dephosphorylate glucokinase (in vitro). Has phosphatase activity with the synthetic substrate 6,8-difluoro-4-methylumbelliferyl phosphate and other in vitro substrates. {ECO:0000250|UniProtKB:Q9JIM4}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UNI6}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9UNI6}. Note=Primarily nuclear. Detected in a mesh-like pattern in the cytosol. {ECO:0000250|UniProtKB:Q9UNI6}. SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9UNI6}. +Q9JLY7 DUS14_MOUSE Dual specificity protein phosphatase 14 (EC 3.1.3.16) (EC 3.1.3.48) (Mitogen-activated protein kinase phosphatase 6) (MAP kinase phosphatase 6) (MKP-6) 198 22,311 Active site (1); Chain (1); Domain (1); Sequence conflict (4) FUNCTION: Involved in the inactivation of MAP kinases. Dephosphorylates ERK, JNK and p38 MAP-kinases. +Q8K4T5 DUS19_MOUSE Dual specificity protein phosphatase 19 (EC 3.1.3.16) (EC 3.1.3.48) (Protein phosphatase SKRP1) (Stress-activated protein kinase pathway-regulating phosphatase 1) 220 24,181 Active site (1); Chain (1); Domain (1); Modified residue (1) FUNCTION: Has a dual specificity toward Ser/Thr and Tyr-containing proteins. {ECO:0000250}. +Q6P253 DMKN_MOUSE Dermokine (Epidermis-specific secreted protein SK30/SK89) 517 51,661 Alternative sequence (4); Chain (1); Compositional bias (2); Sequence conflict (6); Signal peptide (1) FUNCTION: May act as a soluble regulator of keratinocyte differentiation. {ECO:0000305}. PTM: O-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15256262}. SUBUNIT: Homooligomer. Seems to be able to homodimerize and homotrimerize (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in stratified epithelia; such as the skin, tongue, esophagus, forestomach and vagina. Also found in lung, trachea and urinary bladder. {ECO:0000269|PubMed:15234001, ECO:0000269|PubMed:15256262}. +Q9CQ00 DMAC1_MOUSE Distal membrane-arm assembly complex protein 1 (Transmembrane protein 261) 111 11,344 Chain (1); Transmembrane (2) TRANSMEM 51 68 Helical. {ECO:0000255}.; TRANSMEM 81 101 Helical. {ECO:0000255}. FUNCTION: Required for the assembly of the mitochondrial NADH:ubiquinone oxidoreductase complex (complex I). Involved in the assembly of the distal region of complex I. {ECO:0000250|UniProtKB:Q96GE9}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q96GE9}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q96GE9}. SUBUNIT: Interacts with incompletely assembled mitochondrial NADH:ubiquinone oxidoreductase complex (complex I). {ECO:0000250|UniProtKB:Q96GE9}. +Q8K4R9 DLGP5_MOUSE Disks large-associated protein 5 (DAP-5) (Discs large homolog 7) (Disks large-associated protein DLG7) (Hepatoma up-regulated protein homolog) (HURP) 808 90,196 Alternative sequence (4); Chain (1); Coiled coil (1); Erroneous initiation (1); Modified residue (15); Sequence conflict (23) FUNCTION: Potential cell cycle regulator that may play a role in carcinogenesis of cancer cells. Mitotic phosphoprotein regulated by the ubiquitin-proteasome pathway. Key regulator of adherens junction integrity and differentiation that may be involved in CDH1-mediated adhesion and signaling in epithelial cells (By similarity). {ECO:0000250|UniProtKB:Q15398}. PTM: Ubiquitinated, leading to its degradation. {ECO:0000250}.; PTM: Decreased phosphorylation levels are associated with the differentiation of intestinal epithelial cells. {ECO:0000250|UniProtKB:Q15398}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Localizes to the spindle in mitotic cells. Colocalizes with CDH1 at sites of cell-cell contact in intestinal epithelial cells (By similarity). {ECO:0000250}. SUBUNIT: Interacts with CDC2. Interacts with the C-terminal proline-rich region of FBXO7. Recruited by FBXO7 to a SCF (SKP1-CUL1-F-box) protein complex in a CDC2/Cyclin B-phosphorylation dependent manner. Interacts with CDH1 (By similarity). {ECO:0000250|UniProtKB:Q15398}. TISSUE SPECIFICITY: Expressed at low levels in normal resting liver. Up-regulated in regenerating liver after partial hepatectomy. {ECO:0000269|PubMed:12527899}. +Q62108 DLG4_MOUSE Disks large homolog 4 (Postsynaptic density protein 95) (PSD-95) (Synapse-associated protein 90) (SAP-90) (SAP90) 724 80,472 Alternative sequence (2); Chain (1); Domain (5); Lipidation (2); Modified residue (15); Sequence conflict (1) FUNCTION: Interacts with the cytoplasmic tail of NMDA receptor subunits and shaker-type potassium channels. Required for synaptic plasticity associated with NMDA receptor signaling. Overexpression or depletion of DLG4 changes the ratio of excitatory to inhibitory synapses in hippocampal neurons. May reduce the amplitude of ASIC3 acid-evoked currents by retaining the channel intracellularly. May regulate the intracellular trafficking of ADR1B. Also regulates AMPA-type glutamate receptor (AMPAR) immobilization at postsynaptic density keeping the channels in an activated state in the presence of glutamate and preventing synaptic depression (Probable). {ECO:0000269|PubMed:15358775, ECO:0000269|PubMed:9853749, ECO:0000305|PubMed:26931375, ECO:0000305|PubMed:29199957}. PTM: Palmitoylated. Palmitoylation is required for targeting to postsynaptic density, plasma membrane and synapses. Palmitoylation may play a role in glutamate receptor GRIA1 synapse clustering. Depalmitoylated by ABHD17A and ABHD17B and to a lesser extent by ABHD17C, ABHD12, ABHD13, LYPLA1 and LYPLA2. Undergoes rapid synaptic palmitoylation/depalmitoylation cycles during neuronal development which slow down in mature neurons. {ECO:0000250|UniProtKB:P31016}.; PTM: Ubiquitinated by MDM2 in response to NMDA receptor activation, leading to proteasome-mediated degradation of DLG4 which is required for AMPA receptor endocytosis. {ECO:0000250|UniProtKB:P31016}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P31016}; Lipid-anchor {ECO:0000250|UniProtKB:P31016}; Cytoplasmic side {ECO:0000250|UniProtKB:P31016}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000269|PubMed:26931375, ECO:0000269|PubMed:29199957}. Cell junction, synapse {ECO:0000269|PubMed:24153177}. Cytoplasm {ECO:0000250|UniProtKB:P31016}. Cell projection, axon {ECO:0000250|UniProtKB:P31016}. Note=High levels in postsynaptic density of neurons in the forebrain. Also in presynaptic region of inhibitory synapses formed by cerebellar basket cells on axon hillocks of Purkinje cells. {ECO:0000250|UniProtKB:P31016}. SUBUNIT: Interacts through its PDZ domains with ANO2 and NETO1 (PubMed:19474308, PubMed:19243221). Interacts with KCNJ4 (By similarity). Interacts through its first two PDZ domains with GRIN2A, GRIN2B, GRIN2C, GRIN2D (By similarity). Interacts with ERBB4 (By similarity). Interacts with KCNA1, KCNA2, KCNA3 and KCNA4 (By similarity). Interacts with SYNGAP1 (By similarity). Interacts with ASIC3 (By similarity). Interacts with CXADR (By similarity). Interacts with KCND2 (By similarity). Interacts with SEMA4C (PubMed:11134026). Interacts with LRRC4 and LRRC4B (PubMed:16980967). Interacts through its first PDZ domain with GRIK2 and CRIPT (By similarity). Interacts through its second PDZ domain with the PDZ domain of NOS1 or the C-terminus of CAPON (By similarity). Interacts through its third PDZ domain with NLGN1 and CRIPT, and probably with NLGN2 and NLGN3 (By similarity). Interacts through its guanylate kinase-like domain with DLGAP1/GKAP, DLGAP2, DLGAP3, DLGAP4, MAP1A, BEGAIN, SIPA1L1 and KIF13B (By similarity). Isoform 2 interacts through an L27 domain with HGS/HRS and the first L27 domain of CASK (By similarity). Interacts with ADR1B (PubMed:15358775). Interacts with ANKS1B and PRR7 (By similarity). May interact with HTR2A (PubMed:14988405). Interacts with ADAM22, KLHL17 and LGI1 (PubMed:20089912) (By similarity). Interacts with FRMPD4 (via C-terminus) (By similarity). Interacts with LRFN1, LRFN2 and LRFN4 (PubMed:16828986). Interacts (via N-terminal tandem pair of PDZ domains) with GPER1 (via C-terminus tail motif); the interaction is direct and induces the increase of GPER1 protein levels residing at the plasma membrane surface in a estradiol-independent manner (By similarity). Interacts (via N-terminus tandem pair of PDZ domains) with NOS1 (via N-terminal domain) (By similarity). Interacts with SHANK3 (PubMed:24153177). Interacts with KCNJ4 (PubMed:11997254). Interacts with GPR85 (By similarity). Interacts with CACNG2 and MPP2 (via the SH3-Guanylate kinase-like sub-module) (By similarity). Interacts with ADGRB1 (By similarity). Found in a complex with PRR7 and GRIN1 (By similarity). Interacts (via PDZ3 domain and to lesser degree via PDZ2 domain) with PRR7 (By similarity). Component of the postsynaptic hippocampal AMPA-type glutamate receptor (AMPAR) complex, at least composed of pore forming AMPAR subunits GRIA1, GRIA2 and GRIA3 and AMPAR auxiliary proteins SHISA6 and SHISA7. Interacts (via its first two PDZ domains) with SHISA6 and SHISA7 (via PDZ-binding motif); the interaction is direct (PubMed:26931375, PubMed:29199957). {ECO:0000250|UniProtKB:P31016, ECO:0000250|UniProtKB:P78352, ECO:0000269|PubMed:11134026, ECO:0000269|PubMed:11997254, ECO:0000269|PubMed:14988405, ECO:0000269|PubMed:15358775, ECO:0000269|PubMed:16828986, ECO:0000269|PubMed:16980967, ECO:0000269|PubMed:19243221, ECO:0000269|PubMed:19474308, ECO:0000269|PubMed:20089912, ECO:0000269|PubMed:24153177, ECO:0000269|PubMed:26931375, ECO:0000269|PubMed:29199957}. DOMAIN: The PDZ domain 3 mediates interaction with ADR1B. {ECO:0000269|PubMed:15358775}.; DOMAIN: The L27 domain near the N-terminus of isoform 2 is required for HGS/HRS-dependent targeting to postsynaptic density. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in CA1 stratum oriens and stratum radiatum hippocampal neurons. {ECO:0000269|PubMed:26931375}. +Q9D9R7 DMRTC_MOUSE Doublesex- and mab-3-related transcription factor C1 (Doublesex- and mab-3-related transcription factor 8.1) 182 19,230 Alternative sequence (3); Chain (1); Modified residue (1); Sequence conflict (2) TISSUE SPECIFICITY: Expressed in Sertoli cells in male testis. {ECO:0000269|PubMed:16488114}. +P28078 DMA_MOUSE Class II histocompatibility antigen, M alpha chain 261 28,950 Beta strand (11); Chain (1); Disulfide bond (2); Domain (1); Glycosylation (1); Helix (3); Region (3); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (4) TRANSMEM 232 252 Helical. {ECO:0000255}. TOPO_DOM 27 231 Lumenal. {ECO:0000255}.; TOPO_DOM 253 261 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a critical role in catalyzing the release of class II HLA-associated invariant chain-derived peptides (CLIP) from newly synthesized class II HLA molecules and freeing the peptide binding site for acquisition of antigenic peptides. SUBCELLULAR LOCATION: Late endosome membrane; Single-pass type I membrane protein. Lysosome membrane; Single-pass type I membrane protein. Note=Localizes to late endocytic compartment. Associates with lysosome membranes. SUBUNIT: Heterodimer of an alpha chain (DMA) and a beta chain (DMB). {ECO:0000269|PubMed:9768758}. +Q6PNC0 DMXL1_MOUSE DmX-like protein 1 (X-like 1 protein) 3013 336,008 Chain (1); Erroneous initiation (1); Modified residue (11); Repeat (15); Sequence conflict (2) +Q80ZU9 G137A_MOUSE Integral membrane protein GPR137 (Transmembrane 7 superfamily member 1-like 1 protein) 396 43,574 Chain (1); Glycosylation (2); Topological domain (8); Transmembrane (7) TRANSMEM 32 52 Helical. {ECO:0000255}.; TRANSMEM 61 81 Helical. {ECO:0000255}.; TRANSMEM 90 110 Helical. {ECO:0000255}.; TRANSMEM 141 161 Helical. {ECO:0000255}.; TRANSMEM 176 196 Helical. {ECO:0000255}.; TRANSMEM 218 242 Helical. {ECO:0000255}.; TRANSMEM 275 295 Helical. {ECO:0000255}. TOPO_DOM 1 31 Extracellular. {ECO:0000255}.; TOPO_DOM 53 60 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 82 89 Extracellular. {ECO:0000255}.; TOPO_DOM 111 140 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 162 175 Extracellular. {ECO:0000255}.; TOPO_DOM 197 217 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 243 274 Extracellular. {ECO:0000255}.; TOPO_DOM 296 396 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q05A62 DNAL1_MOUSE Dynein light chain 1, axonemal 190 21,465 Alternative sequence (3); Chain (1); Domain (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (2); Repeat (4); Sequence conflict (1) FUNCTION: Part of the multisubunit axonemal ATPase complexes that generate the force for cilia motility and govern beat frequency (By similarity). Component of the outer arm dynein (ODA). May be involved in a mechanosensory feedback mechanism controlling ODA activity based on external conformational cues by tethering the outer arm dynein heavy chain (DNAH5) to the microtubule within the axoneme (By similarity). Important for ciliary function in the airways and for the function of the cilia that produce the nodal flow essential for the determination of the left-right asymmetry (By similarity). {ECO:0000250|UniProtKB:Q4LDG9, ECO:0000250|UniProtKB:Q9XHH2}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q4LDG9}. SUBUNIT: Interacts with ZMYND10 (via C-terminus). Interacts with DNAH5, a outer arm dynein heavy chain. Interacts with tubulin located within the A-tubule of the outer doublets in a ATP-independent manner. {ECO:0000250|UniProtKB:Q4LDG9}. TISSUE SPECIFICITY: Expressed in the respiratory epithelium of the upper airways and the ependymal cells lining the brain ventricles. {ECO:0000269|PubMed:15845866}. +Q9DCM4 DNAL4_MOUSE Dynein light chain 4, axonemal 105 12,023 Chain (1); Frameshift (1); Sequence conflict (2) FUNCTION: Force generating protein of respiratory cilia. Produces force towards the minus ends of microtubules. Dynein has ATPase activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250}. SUBUNIT: Consists of at least two heavy chains and a number of intermediate and light chains. +P49183 DNAS1_MOUSE Deoxyribonuclease-1 (EC 3.1.21.1) (Deoxyribonuclease I) (DNase I) 284 32,027 Active site (2); Chain (1); Disulfide bond (2); Glycosylation (2); Sequence conflict (1); Signal peptide (1); Site (3) FUNCTION: Serum endocuclease secreted into body fluids by a wide variety of exocrine and endocrine organs (PubMed:29191910). Expressed by non-hematopoietic tissues and preferentially cleaves protein-free DNA. Among other functions, seems to be involved in cell death by apoptosis. Binds specifically to G-actin and blocks actin polymerization (By similarity). Together with DNASE1L3, plays a key role in degrading neutrophil extracellular traps (NETs) (PubMed:29191910). NETs are mainly composed of DNA fibers and are released by neutrophils to bind pathogens during inflammation (PubMed:29191910). Degradation of intravascular NETs by DNASE1 and DNASE1L3 is required to prevent formation of clots that obstruct blood vessels and cause organ damage following inflammation (PubMed:29191910). {ECO:0000250|UniProtKB:P00639, ECO:0000250|UniProtKB:P21704, ECO:0000250|UniProtKB:P24855, ECO:0000269|PubMed:29191910}. PTM: N-glycosylated. {ECO:0000269|PubMed:15015938}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P24855}. Nucleus envelope {ECO:0000250|UniProtKB:P24855}. Note=Secretory protein, stored in zymogen granules and found in the nuclear envelope. {ECO:0000250|UniProtKB:P24855}. TISSUE SPECIFICITY: Highly expressed in the parotid and submandibular gland as well as in the kidney and duodenum (at protein level) (PubMed:15015938). Expressed at intermediate level in the ileum, mesenterial lymph nodes, liver, ventral prostate, epididymis, ovary and stomach (at protein level) (PubMed:15015938). Expressed at low level in the sublingual, preputial, coagulation and pituitary gland (at protein level) (PubMed:15015938). Also present in the lachrymal and thyroid glands, striated muscle, intestine, the urinary bladder and the eye (PubMed:7857306, PubMed:9192086, PubMed:15015938). {ECO:0000269|PubMed:15015938, ECO:0000269|PubMed:7857306, ECO:0000269|PubMed:9192086}. +Q9QYJ3 DNJB1_MOUSE DnaJ homolog subfamily B member 1 (Heat shock 40 kDa protein 1) (HSP40) (Heat shock protein 40) 340 38,167 Chain (1); Domain (1); Modified residue (1) FUNCTION: Interacts with HSP70 and can stimulate its ATPase activity. Stimulates the association between HSC70 and HIP. Negatively regulates heat shock-induced HSF1 transcriptional activity during the attenuation and recovery phase period of the heat shock response. Stimulates ATP hydrolysis and the folding of unfolded proteins mediated by HSPA1A/B (in vitro). {ECO:0000250|UniProtKB:P25685}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P25685}. Nucleus {ECO:0000250|UniProtKB:P25685}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P25685}. Note=Translocates rapidly from the cytoplasm to the nucleus, and especially to the nucleoli, upon heat shock. {ECO:0000250|UniProtKB:P25685}. SUBUNIT: Interacts with DNAJC3. Interacts with HSF1 (via transactivation domain); this interaction results in the inhibition of heat shock- and HSF1-induced transcriptional activity during the attenuation and recovery phase period of the heat shock response. {ECO:0000250|UniProtKB:P25685}. +O54946 DNJB6_MOUSE DnaJ homolog subfamily B member 6 (Heat shock protein J2) (HSJ-2) (MRJ) (mDj4) 365 39,807 Alternative sequence (2); Chain (1); Compositional bias (6); Domain (1); Modified residue (1); Region (2); Sequence conflict (5) FUNCTION: Plays an indispensable role in the organization of KRT8/KRT18 filaments. Acts as an endogenous molecular chaperone for neuronal proteins including huntingtin. Suppresses aggregation and toxicity of polyglutamine-containing, aggregation-prone proteins (By similarity). Has a stimulatory effect on the ATPase activity of HSP70 in a dose-dependent and time-dependent manner and hence acts as a co-chaperone of HSP70. Also reduces cellular toxicity and caspase-3 activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O75190}. Nucleus {ECO:0000250|UniProtKB:O75190}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:O75190}. SUBUNIT: Homooligomer (By similarity). Interacts with BAG3, HSPB8 and STUB1 (By similarity). Interacts with HSP70, KRT18 and PTTG. Isoform B interacts with histone deacetylases HDAC4, HDAC6, and SIRT2, HDAC activity is required for antiaggregation (By similarity). Interacts with ALKBH1. {ECO:0000250, ECO:0000269|PubMed:18163532}. DOMAIN: The antiaggregation activity of resides in the serine-rich region and the C-terminus. {ECO:0000250}. +Q5RJY2 G2E3_MOUSE G2/M phase-specific E3 ubiquitin-protein ligase (EC 2.3.2.26) (G2/M phase-specific HECT-type E3 ubiquitin transferase) 716 81,784 Chain (1); Domain (1); Erroneous initiation (1); Sequence conflict (1); Zinc finger (4) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates (By similarity). Required for prevention of apoptotic death in early embryogenesis. {ECO:0000250|UniProtKB:Q7L622, ECO:0000269|PubMed:18511420}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q7L622}. Cytoplasm {ECO:0000250|UniProtKB:Q7L622}. Note=Shuttles between the nucleus and the cytoplasm. In the nucleus, delocalizes from the nucleolus to the nucleoplasm in response to DNA damage. {ECO:0000250|UniProtKB:Q7L622}. DOMAIN: Ubiquitin ligase activity is mediated by two distinct domains, PHD-type zinc fingers 2 and 3. The use of these distinct domains may allow ubiquitination of different targets by each domain. The HECT domain is catalytically inactive and does not contribute to this activity. {ECO:0000250|UniProtKB:Q7L622}. TISSUE SPECIFICITY: In the developing embryo, expressed predominantly in the central nervous system and early limb bud. In the adult, highest expression in Purkinje cell bodies and cells lining the ductus deferens. {ECO:0000269|PubMed:18511420}. +Q9D844 DNJC4_MOUSE DnaJ homolog subfamily C member 4 (Multiple endocrine neoplasia type 1 candidate protein number 18 homolog) 244 28,206 Chain (1); Domain (1); Sequence conflict (1); Transmembrane (1) TRANSMEM 159 178 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +P97379 G3BP2_MOUSE Ras GTPase-activating protein-binding protein 2 (G3BP-2) (GAP SH3 domain-binding protein 2) 482 54,088 Alternative sequence (1); Chain (1); Compositional bias (2); Cross-link (1); Domain (2); Erroneous initiation (1); Modified residue (12); Sequence conflict (1) FUNCTION: Probable scaffold protein that may be involved in mRNA transport. {ECO:0000305}. +P16858 G3P_MOUSE Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (EC 1.2.1.12) (Peptidyl-cysteine S-nitrosylase GAPDH) (EC 2.6.99.-) 333 35,810 Active site (1); Binding site (6); Chain (1); Cross-link (1); Modified residue (41); Motif (1); Mutagenesis (1); Nucleotide binding (1); Region (3); Sequence conflict (9); Site (1) Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5. FUNCTION: Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively. Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate. Modulates the organization and assembly of the cytoskeleton. Facilitates the CHP1-dependent microtubule and membrane associations through its ability to stimulate the binding of CHP1 to microtubules. Also participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis. Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma treatment assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation. {ECO:0000269|PubMed:23071094}. PTM: ISGylated. {ECO:0000250}.; PTM: S-nitrosylation of Cys-150 leads to interaction with SIAH1, followed by translocation to the nucleus S-nitrosylation of Cys-245 is induced by interferon-gamma and LDL(ox) implicating the iNOS-S100A8/9 transnitrosylase complex and seems to prevent interaction with phosphorylated RPL13A and to interfere with GAIT complex activity (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P04406}.; PTM: Sulfhydration at Cys-150 increases catalytic activity.; PTM: Oxidative stress can promote the formation of high molecular weight disulfide-linked GAPDH aggregates, through a process called nucleocytoplasmic coagulation. {ECO:0000250|UniProtKB:P04406}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Translocates to the nucleus following S-nitrosylation and interaction with SIAH1, which contains a nuclear localization signal. {ECO:0000250}. SUBUNIT: Homotetramer. Interacts with EIF1AD, USP25, PRKCI and WARS. Interacts with TPPP; the interaction is direct. Interacts (when S-nitrosylated) with SIAH1; leading to nuclear translocation. Interacts with RILPL1/GOSPEL, leading to prevent the interaction between GAPDH and SIAH1 and prevent nuclear translocation. Interacts with CHP1; the interaction increases the binding of CHP1 with microtubules. Associates with microtubules. Interacts with FKBP6; leading to inhibit GAPDH catalytic activity (By similarity). Interacts with phosphorylated RPL13A (By similarity). Component of the GAIT complex. {ECO:0000250, ECO:0000250|UniProtKB:P04406, ECO:0000269|PubMed:23071094}. DOMAIN: The [IL]-x-C-x-x-[DE] motif is a proposed target motif for cysteine S-nitrosylation mediated by the iNOS-S100A8/A9 transnitrosylase complex. {ECO:0000250|UniProtKB:P04406}. +Q9EQF5 DPYS_MOUSE Dihydropyrimidinase (DHP) (DHPase) (EC 3.5.2.2) (Dihydropyrimidine amidohydrolase) (Hydantoinase) 519 56,725 Binding site (2); Chain (1); Metal binding (7); Modified residue (4); Sequence conflict (7) FUNCTION: Catalyzes the second step of the reductive pyrimidine degradation, the reversible hydrolytic ring opening of dihydropyrimidines. Can catalyze the ring opening of 5,6-dihydrouracil to N-carbamyl-alanine and of 5,6-dihydrothymine to N-carbamyl-amino isobutyrate (By similarity). {ECO:0000250}. PTM: Carbamylation allows a single lysine to coordinate two zinc ions. {ECO:0000250}. SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q55DL0}. +Q924H9 DQX1_MOUSE ATP-dependent RNA helicase DQX1 (EC 3.6.4.12) (DEAQ box polypeptide 1) 718 78,799 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (2); Motif (1); Nucleotide binding (1) SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11353393}. +Q6XQH0 G3ST2_MOUSE Galactose-3-O-sulfotransferase 2 (Gal3ST-2) (EC 2.8.2.-) (Beta-galactose-3-O-sulfotransferase 2) (Gal-beta-1, 3-GalNAc 3'-sulfotransferase 2) 394 46,909 Chain (1); Glycosylation (4); Topological domain (2); Transmembrane (1) TRANSMEM 9 29 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 8 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 30 394 Lumenal. {ECO:0000255}. Protein modification; carbohydrate sulfation. FUNCTION: Transfers a sulfate group to the hydroxyl group at C3 of non-reducing beta-galactosyl residues. Acts both on type 1 (Gal-beta-1,3-GlcNAc) and type 2 (Gal-beta-1,4-GlcNAc) chains with similar efficiency (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. +Q8K3P0 DR9C7_MOUSE Short-chain dehydrogenase/reductase family 9C member 7 (EC 1.1.1.-) (Orphan short-chain dehydrogenase/reductase) (SDR-O) (RDH-S) 313 35,149 Active site (1); Binding site (1); Chain (1); Modified residue (1); Nucleotide binding (1) FUNCTION: Displays weak conversion of all-trans-retinal to all-trans-retinol in the presence of NADH. Has apparently no steroid dehydrogenase activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:12234675}. TISSUE SPECIFICITY: Highly expressed in liver. {ECO:0000269|PubMed:12234675}. +P61315 G3ST3_MOUSE Galactose-3-O-sulfotransferase 3 (Gal3ST-3) (EC 2.8.2.-) (Beta-galactose-3-O-sulfotransferase 3) (Gal-beta-1, 3-GalNAc 3'-sulfotransferase 3) 431 49,277 Chain (1); Glycosylation (4); Topological domain (2); Transmembrane (1) TRANSMEM 20 40 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 19 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 41 431 Lumenal. {ECO:0000255}. Protein modification; carbohydrate sulfation. FUNCTION: Transfers a sulfate to position 3 of non-reducing beta-galactosyl residues in N-glycans and core2-branched O-glycans. Has high activity towards Gal-beta-1,4-GlcNAc, Gal-beta-1,4(Fuc-alpha-1,3)GlcNAc and lower activity towards Gal-beta-1,3(Fuc-alpha-1,4)GlcNAc (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. +Q9DC58 DRAM1_MOUSE DNA damage-regulated autophagy modulator protein 1 (Damage-regulated autophagy modulator) 238 26,201 Alternative sequence (1); Chain (1); Transmembrane (6) TRANSMEM 9 29 Helical. {ECO:0000255}.; TRANSMEM 53 73 Helical. {ECO:0000255}.; TRANSMEM 91 111 Helical. {ECO:0000255}.; TRANSMEM 116 136 Helical. {ECO:0000255}.; TRANSMEM 161 181 Helical. {ECO:0000255}.; TRANSMEM 200 220 Helical. {ECO:0000255}. FUNCTION: Lysosomal modulator of autophagy that plays a central role in p53/TP53-mediated apoptosis. Not involved in p73/TP73-mediated autophagy (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q9CR48 DRAM2_MOUSE DNA damage-regulated autophagy modulator protein 2 (Transmembrane protein 77) 267 30,228 Chain (1); Sequence conflict (1); Transmembrane (6) TRANSMEM 8 28 Helical. {ECO:0000255}.; TRANSMEM 53 73 Helical. {ECO:0000255}.; TRANSMEM 87 107 Helical. {ECO:0000255}.; TRANSMEM 118 138 Helical. {ECO:0000255}.; TRANSMEM 160 180 Helical. {ECO:0000255}.; TRANSMEM 203 223 Helical. {ECO:0000255}. FUNCTION: Plays a role in the initiation of autophagy. In the retina, might be involved in the process of photoreceptor cells renewal and recycling to preserve visual function. Induces apoptotic cell death when coexpressed with DRAM1. {ECO:0000250|UniProtKB:Q6UX65}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q6UX65}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q6UX65}. Photoreceptor inner segment {ECO:0000269|PubMed:25983245}. Apical cell membrane {ECO:0000269|PubMed:25983245}. Note=Localized to photoreceptor inner segments and to the apical surface of retinal pigment epithelial cells. {ECO:0000269|PubMed:25983245}. TISSUE SPECIFICITY: Expressed in the retina. {ECO:0000269|PubMed:25983245}. +Q6PAL1 DRAXI_MOUSE Draxin (Dorsal inhibitory axon guidance protein) (Dorsal repulsive axon guidance protein) (Neucrin) 343 38,363 Chain (1); Glycosylation (1); Sequence conflict (7); Signal peptide (1) FUNCTION: Chemorepulsive axon guidance protein required for the development of spinal cord and forebrain commissures. Acts as a chemorepulsive guidance protein for commissural axons during development. Able to inhibit or repel neurite outgrowth from dorsal spinal cord. Inhibits the stabilization of cytosolic beta-catenin (CTNNB1) via its interaction with LRP6, thereby acting as an antagonist of Wnt signaling pathway. {ECO:0000255|HAMAP-Rule:MF_03060, ECO:0000269|PubMed:19857465}. SUBCELLULAR LOCATION: Secreted {ECO:0000255|HAMAP-Rule:MF_03060}. SUBUNIT: Interacts with LRP6. {ECO:0000255|HAMAP-Rule:MF_03060, ECO:0000269|PubMed:19857465}. TISSUE SPECIFICITY: Predominantly expressed in developing neural tissues. Expressed in many brain regions, including the olfactory bulb, cortex, midbrain, cerebellum and pontine nuclei in postnatal day 0 (P0). Detected in the dorsal spinal cord and commissural axons. In the forebrain commissures, it is expressed in the regions that surround the corpus callosum, hippocampal commissure, and anterior commissure, such as the midline glial cells, indusium griseum glia, and glial wedge. {ECO:0000269|PubMed:19150847, ECO:0000269|PubMed:19857465}. +D7PDD4 G6B_MOUSE Megakaryocyte and platelet inhibitory receptor G6b (ITIM-receptor G6b-B) (Immunoreceptor tyrosine-based inhibitory motif (ITIM)-containing platelet receptor) 242 26,010 Chain (1); Glycosylation (2); Modified residue (1); Motif (2); Signal peptide (1); Transmembrane (1) TRANSMEM 141 161 Helical. {ECO:0000255}. FUNCTION: Inhibitory receptor that acts as a critical regulator of hematopoietic lineage differentiation, megakaryocyte function and platelet production (PubMed:23112346). Inhibits platelet aggregation and activation by agonists such as ADP and collagen-related peptide (By similarity). This regulation of megakaryocate function as well as platelet production ann activation is done through the inhibition (via the 2 ITIM motifs) of the receptors CLEC1B and GP6:FcRgamma signaling (PubMed:23112346). Appears to operate in a calcium-independent manner (By similarity). {ECO:0000250|UniProtKB:O95866, ECO:0000269|PubMed:23112346}. PTM: N-glycosylated. {ECO:0000269|PubMed:23112346}.; PTM: May be O-glycosylated. {ECO:0000250|UniProtKB:O95866}.; PTM: Phosphorylated. {ECO:0000269|PubMed:23112346}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:23112346}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:O95866, ECO:0000255}. SUBUNIT: Interacts (via ITIM motif) with PTPN6 and PTPN11 (PubMed:23112346). Binds to heparin (By similarity). {ECO:0000250|UniProtKB:O95866, ECO:0000269|PubMed:23112346}. DOMAIN: Contains both a transmembrane region and 2 copies of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is involved in modulation of cellular responses. The phosphorylated ITIM motif can bind the SH2 domain of several SH2-containing phosphatases. The 2 ITIM motifs of isoform B are required for the inhibition of CLEC1B and GP6:FCER1G signaling and platelet activation. {ECO:0000305|PubMed:23112346}. TISSUE SPECIFICITY: Espressed in mature megakaryocytes and platelets. Not expressed by immature megakaryocytes. {ECO:0000269|PubMed:23112346}. +Q9Z186 G6PC2_MOUSE Glucose-6-phosphatase 2 (G-6-Pase 2) (G6Pase 2) (EC 3.1.3.9) (Islet-specific glucose-6-phosphatase catalytic subunit-related protein) 355 40,681 Active site (2); Alternative sequence (2); Binding site (2); Chain (1); Erroneous translation (1); Glycosylation (1); Motif (1); Topological domain (10); Transmembrane (9) TRANSMEM 25 45 Helical. {ECO:0000255}.; TRANSMEM 57 77 Helical. {ECO:0000255}.; TRANSMEM 116 136 Helical. {ECO:0000255}.; TRANSMEM 147 167 Helical. {ECO:0000255}.; TRANSMEM 169 189 Helical. {ECO:0000255}.; TRANSMEM 212 232 Helical. {ECO:0000255}.; TRANSMEM 253 273 Helical. {ECO:0000255}.; TRANSMEM 291 307 Helical. {ECO:0000255}.; TRANSMEM 319 339 Helical. {ECO:0000255}. TOPO_DOM 1 24 Lumenal. {ECO:0000255}.; TOPO_DOM 46 56 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 78 115 Lumenal. {ECO:0000255}.; TOPO_DOM 137 146 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 168 168 Lumenal. {ECO:0000255}.; TOPO_DOM 190 211 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 233 252 Lumenal. {ECO:0000255}.; TOPO_DOM 274 290 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 308 318 Lumenal. {ECO:0000255}.; TOPO_DOM 340 355 Cytoplasmic. {ECO:0000255}. Carbohydrate biosynthesis; gluconeogenesis. FUNCTION: May hydrolyze glucose-6-phosphate to glucose in the endoplasmic reticulum. May be responsible for glucose production through glycogenolysis and gluconeogenesis (By similarity). {ECO:0000250}. PTM: N-glycosylated; the non-glycosylated form is more unstable and is degraded through the proteasome. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Specifically expressed in pancreatic islet cells, in particular those of beta-cell origin. Not detected in testis, kidney, muscle, liver, lung, spleen, brain, pituitary, gastric fundus or heart. {ECO:0000269|PubMed:10078553, ECO:0000269|PubMed:12878201, ECO:0000269|PubMed:14722102}. +Q6NSQ9 G6PC3_MOUSE Glucose-6-phosphatase 3 (G-6-Pase 3) (G6Pase 3) (EC 3.1.3.9) (Ubiquitous glucose-6-phosphatase catalytic subunit-related protein) 346 38,782 Active site (2); Binding site (2); Chain (1); Sequence conflict (2); Topological domain (10); Transmembrane (9) TRANSMEM 25 45 Helical. {ECO:0000255}.; TRANSMEM 57 77 Helical. {ECO:0000255}.; TRANSMEM 109 129 Helical. {ECO:0000255}.; TRANSMEM 139 159 Helical. {ECO:0000255}.; TRANSMEM 168 186 Helical. {ECO:0000255}.; TRANSMEM 198 218 Helical. {ECO:0000255}.; TRANSMEM 255 273 Helical. {ECO:0000255}.; TRANSMEM 284 304 Helical. {ECO:0000255}.; TRANSMEM 308 328 Helical. {ECO:0000255}. TOPO_DOM 1 24 Lumenal. {ECO:0000255}.; TOPO_DOM 46 56 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 78 108 Lumenal. {ECO:0000255}.; TOPO_DOM 130 138 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 160 167 Lumenal. {ECO:0000255}.; TOPO_DOM 187 197 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 219 254 Lumenal. {ECO:0000255}.; TOPO_DOM 274 283 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 305 307 Lumenal. {ECO:0000255}.; TOPO_DOM 329 346 Cytoplasmic. {ECO:0000255}. Carbohydrate biosynthesis; gluconeogenesis. FUNCTION: Hydrolyzes glucose-6-phosphate to glucose in the endoplasmic reticulum. May form with the glucose-6-phosphate transporter (SLC37A4/G6PT) a ubiquitously expressed complex responsible for glucose production through glycogenolysis and gluconeogenesis. Probably required for normal neutrophil function. {ECO:0000269|PubMed:15087461, ECO:0000269|PubMed:15661744, ECO:0000269|PubMed:17023421, ECO:0000269|PubMed:17318259}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. Highly expressed in heart, brain, kidney and testis and to a lower extent in lung, spleen, stomach, small intestine, skeletal muscle and uterus. Expressed in muscle, brain, thymus, lung, kidney, spleen and pancreas (at protein level). {ECO:0000269|PubMed:14765991, ECO:0000269|PubMed:15087461, ECO:0000269|PubMed:15661744}. +P35576 G6PC_MOUSE Glucose-6-phosphatase (G-6-Pase) (G6Pase) (EC 3.1.3.9) 357 40,473 Active site (2); Binding site (2); Chain (1); Glycosylation (1); Motif (1); Sequence conflict (1); Topological domain (10); Transmembrane (9) TRANSMEM 29 49 Helical. {ECO:0000255}.; TRANSMEM 61 81 Helical. {ECO:0000255}.; TRANSMEM 118 138 Helical. {ECO:0000255}.; TRANSMEM 148 168 Helical. {ECO:0000255}.; TRANSMEM 180 202 Helical. {ECO:0000255}.; TRANSMEM 212 232 Helical. {ECO:0000255}.; TRANSMEM 255 275 Helical. {ECO:0000255}.; TRANSMEM 292 312 Helical. {ECO:0000255}.; TRANSMEM 321 341 Helical. {ECO:0000255}. TOPO_DOM 1 28 Lumenal. {ECO:0000255}.; TOPO_DOM 50 60 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 82 117 Lumenal. {ECO:0000255}.; TOPO_DOM 139 147 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 169 179 Lumenal. {ECO:0000255}.; TOPO_DOM 203 211 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 233 254 Lumenal. {ECO:0000255}.; TOPO_DOM 276 291 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 313 320 Lumenal. {ECO:0000255}.; TOPO_DOM 342 357 Cytoplasmic. {ECO:0000255}. Carbohydrate biosynthesis; gluconeogenesis. FUNCTION: Hydrolyzes glucose-6-phosphate to glucose in the endoplasmic reticulum. Forms with the glucose-6-phosphate transporter (SLC37A4/G6PT) the complex responsible for glucose production through glycogenolysis and gluconeogenesis. Hence, it is the key enzyme in homeostatic regulation of blood glucose levels. {ECO:0000269|PubMed:8640227}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Liver and kidney. +Q00612 G6PD1_MOUSE Glucose-6-phosphate 1-dehydrogenase X (G6PD) (EC 1.1.1.49) 515 59,263 Active site (1); Binding site (16); Chain (1); Initiator methionine (1); Modified residue (2); Nucleotide binding (3); Region (1); Sequence conflict (1) Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3. FUNCTION: Catalyzes the rate-limiting step of the oxidative pentose-phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis. The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis (By similarity). {ECO:0000250}. PTM: Acetylated by ELP3 at Lys-403; acetylation inhibits its homodimerization and enzyme activity. Deacetylated by SIRT2 at Lys-403; deacetylation stimulates its enzyme activity (By similarity). {ECO:0000250}. SUBUNIT: Homotetramer; dimer of dimers. Interacts with SIRT2; the interaction is enhanced by H(2)O(2) treatment (By similarity). {ECO:0000250}. +P97324 G6PD2_MOUSE Glucose-6-phosphate 1-dehydrogenase 2 (G6PD) (EC 1.1.1.49) 513 59,126 Active site (1); Binding site (15); Chain (1); Initiator methionine (1); Modified residue (7); Nucleotide binding (3); Region (1) Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3. FUNCTION: Catalyzes the rate-limiting step of the oxidative pentose-phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis. The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis. {ECO:0000269|PubMed:9169132}. PTM: Acetylated by ELP3; acetylation inhibits its homodimerization and enzyme activity. Deacetylated by SIRT2; deacetylation stimulates its enzyme activity (By similarity). {ECO:0000250}. SUBUNIT: Interacts with SIRT2; the interaction is enhanced by H(2)O(2) treatment (By similarity). Homotetramer; dimer of dimers. {ECO:0000250, ECO:0000269|PubMed:9169132}. TISSUE SPECIFICITY: Testis. {ECO:0000269|PubMed:9169132}. +Q9QX60 DGUOK_MOUSE Deoxyguanosine kinase, mitochondrial (dGK) (EC 2.7.1.113) 277 32,281 Active site (1); Alternative sequence (1); Binding site (7); Chain (1); Nucleotide binding (2); Sequence conflict (3); Transit peptide (1) FUNCTION: Phosphorylates deoxyguanosine and deoxyadenosine in the mitochondrial matrix, with the highest efficiency for deoxyguanosine. In non-replicating cells, where cytosolic dNTP synthesis is down-regulated, mtDNA synthesis depends solely on DGUOK and TK2. Phosphorylates certain nucleoside analogs. Widely used as target of antiviral and chemotherapeutic agents. {ECO:0000250|UniProtKB:Q16854}. SUBCELLULAR LOCATION: Isoform 1: Mitochondrion {ECO:0000269|PubMed:10455141}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm {ECO:0000269|PubMed:10455141}. SUBUNIT: Homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Spleen and thymus. Expressed at much lower levels in the brain and liver. {ECO:0000269|PubMed:10455141}. +Q6WQJ1 DGLA_MOUSE Sn1-specific diacylglycerol lipase alpha (DGL-alpha) (EC 3.1.1.-) (Neural stem cell-derived dendrite regulator) 1044 115,375 Active site (2); Chain (1); Compositional bias (1); Glycosylation (1); Modified residue (11); Sequence conflict (3); Topological domain (5); Transmembrane (4) TRANSMEM 23 43 Helical. {ECO:0000255}.; TRANSMEM 61 81 Helical. {ECO:0000255}.; TRANSMEM 102 122 Helical. {ECO:0000255}.; TRANSMEM 137 157 Helical. {ECO:0000255}. TOPO_DOM 1 22 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 44 60 Extracellular. {ECO:0000255}.; TOPO_DOM 82 101 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 123 136 Extracellular. {ECO:0000255}.; TOPO_DOM 158 1044 Cytoplasmic. {ECO:0000255}. FUNCTION: Catalyzes the hydrolysis of diacylglycerol (DAG) to 2-arachidonoyl-glycerol (2-AG), the most abundant endocannabinoid in tissues. Required for axonal growth during development and for retrograde synaptic signaling at mature synapses (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed by principal cells in the hyppocampus. In embryonic brains, it is present in axonal tracts, while in adults it localizes to dendritic fields, correlating with the developmental change in requirement for 2-AG synthesis from the pre- to the postsynaptic compartment. Concentrated in heads of dendritic spines throughout the hippocampal formation. Highly compartmentalized into a wide perisynaptic annulus around the postsynaptic density of axospinous contacts but not intrasynaptically (at protein level). {ECO:0000269|PubMed:14610053, ECO:0000269|PubMed:16723519}. +Q8C0S1 DI3L1_MOUSE DIS3-like exonuclease 1 (EC 3.1.13.-) 1053 120,284 Alternative sequence (1); Chain (1); Erroneous initiation (2); Modified residue (1) FUNCTION: Putative cytoplasm-specific catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Component of the RNA exosome complex. The catalytically inactive RNA exosome core (Exo-9) complex is believed to associate with catalytic subunits EXOSC10, and DIS3 or DIS3L in cytoplasmic- and nuclear-specific RNA exosome complex forms (By similarity). {ECO:0000250}. +Q9D0D4 DIM1_MOUSE Probable dimethyladenosine transferase (EC 2.1.1.183) (DIM1 dimethyladenosine transferase 1 homolog) (DIM1 dimethyladenosine transferase 1-like) (Probable 18S rRNA (adenine(1779)-N(6)/adenine(1780)-N(6))-dimethyltransferase) (Probable 18S rRNA dimethylase) (Probable S-adenosylmethionine-6-N',N'-adenosyl(rRNA) dimethyltransferase) 313 35,274 Binding site (6); Chain (1); Sequence caution (1) FUNCTION: Specifically dimethylates two adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 18S rRNA in the 40S particle. Involved in the pre-rRNA processing steps leading to small-subunit rRNA production independently of its RNA-modifying catalytic activity. {ECO:0000250|UniProtKB:Q9UNQ2}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9UNQ2}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9UNQ2}. +A3KFU9 DISP3_MOUSE Protein dispatched homolog 3 (Patched domain-containing protein 2) (RND-type protein RNDEu-2) 1347 148,446 Alternative sequence (3); Chain (1); Domain (1); Glycosylation (2); Sequence conflict (10); Topological domain (13); Transmembrane (12) TRANSMEM 68 88 Helical. {ECO:0000255}.; TRANSMEM 418 438 Helical. {ECO:0000255}.; TRANSMEM 440 460 Helical. {ECO:0000255}.; TRANSMEM 464 484 Helical. {ECO:0000255}.; TRANSMEM 529 549 Helical. {ECO:0000255}.; TRANSMEM 551 571 Helical. {ECO:0000255}.; TRANSMEM 685 705 Helical. {ECO:0000255}.; TRANSMEM 1138 1158 Helical. {ECO:0000255}.; TRANSMEM 1160 1180 Helical. {ECO:0000255}.; TRANSMEM 1247 1267 Helical. {ECO:0000255}.; TRANSMEM 1282 1302 Helical. {ECO:0000255}.; TRANSMEM 1311 1331 Helical. {ECO:0000255}. TOPO_DOM 1 67 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 89 417 Extracellular. {ECO:0000255}.; TOPO_DOM 439 439 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 461 463 Extracellular. {ECO:0000255}.; TOPO_DOM 485 528 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 550 550 Extracellular. {ECO:0000255}.; TOPO_DOM 572 684 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 706 1137 Extracellular. {ECO:0000255}.; TOPO_DOM 1159 1159 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1181 1246 Extracellular. {ECO:0000255}.; TOPO_DOM 1268 1281 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1303 1310 Extracellular. {ECO:0000255}.; TOPO_DOM 1332 1347 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a role in neuronal proliferation and differentiation. Plays a role in the accumulation of cellular cholesterol. Involved in intracellular lipid droplet formation. May contribute to cholesterol homeostasis in neuronal cells. {ECO:0000250|UniProtKB:B9U3F2, ECO:0000250|UniProtKB:Q9P2K9}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9P2K9}; Multi-pass membrane protein {ECO:0000305}. Nucleus membrane {ECO:0000250|UniProtKB:Q9P2K9}; Multi-pass membrane protein {ECO:0000305}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:B9U3F2}; Multi-pass membrane protein {ECO:0000305}. Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Note=Predominantly localized to cholesterol-enriched domains within the membrane (By similarity). Localizes to cytoplasmic punctate vesicular structures (By similarity). {ECO:0000250|UniProtKB:B9U3F2, ECO:0000250|UniProtKB:Q9P2K9}. DOMAIN: The SSD (sterol-sensing) domain is necessary for the increase in cellular cholesterol uptake. {ECO:0000250|UniProtKB:B9U3F2}. TISSUE SPECIFICITY: Expressed in brain, retina, testis and thymus (PubMed:19179482). {ECO:0000269|PubMed:19179482}. +P59041 DJC30_MOUSE DnaJ homolog subfamily C member 30, mitochondrial (Williams-Beuren syndrome chromosomal region 18 protein homolog) 219 24,762 Chain (1); Domain (1); Transit peptide (1); Transmembrane (1) TRANSMEM 202 218 Helical. {ECO:0000255}. FUNCTION: Mitochondrial protein enriched in neurons that acts as a regulator of mitochondrial respiration (PubMed:30318146). Associates with the ATP synthase complex and facilitates ATP synthesis (PubMed:30318146). {ECO:0000269|PubMed:30318146}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q96LL9}; Single-pass membrane protein {ECO:0000255}. SUBUNIT: Associates with the ATP synthase complex. Interacts with MT-ATP6; interaction is direct. Interacts with ATP5MC2; interaction is direct. {ECO:0000250|UniProtKB:Q96LL9}. TISSUE SPECIFICITY: In brain, expressed in gray matter structures. {ECO:0000269|PubMed:30318146}. +Q9ESX5 DKC1_MOUSE H/ACA ribonucleoprotein complex subunit DKC1 (EC 5.4.99.-) (Dyskerin) (Nopp140-associated protein of 57 kDa) (Nucleolar protein NAP57) (Nucleolar protein family A member 4) (snoRNP protein DKC1) 509 57,402 Active site (1); Chain (1); Compositional bias (1); Cross-link (8); Domain (1); Initiator methionine (1); Modified residue (9); Mutagenesis (2); Region (2); Sequence conflict (1) FUNCTION: Catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA (PubMed:12522253, PubMed:15240872). This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Each rRNA can contain up to 100 pseudouridine ('psi') residues, which may serve to stabilize the conformation of rRNAs (PubMed:12522253, PubMed:15240872). Required for ribosome biogenesis and telomere maintenance (By similarity). Also required for correct processing or intranuclear trafficking of TERC, the RNA component of the telomerase reverse transcriptase (TERT) holoenzyme (By similarity). {ECO:0000250|UniProtKB:O60832, ECO:0000269|PubMed:12522253, ECO:0000269|PubMed:15240872}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:O60832}. Nucleus, Cajal body {ECO:0000250|UniProtKB:P40615}. Note=Also localized to Cajal bodies (coiled bodies). {ECO:0000250|UniProtKB:P40615}. SUBUNIT: Part of the H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which contains NHP2/NOLA2, GAR1/NOLA1, NOP10/NOLA3, and DKC1/NOLA4, which is presumed to be the catalytic subunit. The complex contains a stable core formed by binding of one or two NOP10-DKC1 heterodimers to NHP2; GAR1 subsequently binds to this core via DKC1. The complex binds a box H/ACA small nucleolar RNA (snoRNA), which may target the specific site of modification within the RNA substrate. During assembly, the complex contains NAF1 instead of GAR1/NOLA1. The complex also interacts with TERC, which contains a 3'-terminal domain related to the box H/ACA snoRNAs. Specific interactions with snoRNAs or TERC are mediated by GAR1 and NHP2. Associates with NOLC1/NOPP140. H/ACA snoRNPs interact with the SMN complex, consisting of SMN1 or SMN2, GEMIN2/SIP1, DDX20/GEMIN3, and GEMIN4. This is mediated by interaction between GAR1 and SMN1 or SMN2. The SMN complex may be required for correct assembly of the H/ACA snoRNP complex. Component of the telomerase holoenzyme complex composed of one molecule of TERT, one molecule of WRAP53/TCAB1, two molecules of H/ACA ribonucleoprotein complex subunits DKC1, NOP10, NHP2 and GAR1, and a telomerase RNA template component (TERC). The telomerase holoenzyme complex is associated with TEP1, SMG6/EST1A and POT1. Interacts with SHQ1; this interaction may lead to the stabilization of DKC1, from the time of its synthesis until its association with NOP10, NHP2, and NAF1 at the nascent H/ACA RNA (By similarity). Interacts with HMBOX1 (By similarity). Interacts with DHX36 (By similarity). {ECO:0000250|UniProtKB:O60832}. TISSUE SPECIFICITY: Ubiquitously expressed, with elevated levels in Purkinje cells, the olfactory bulb, and Leydig cells of the testis. {ECO:0000269|PubMed:10903840}. +Q8BPN8 DMXL2_MOUSE DmX-like protein 2 (Rabconnectin-3) 3032 338,209 Alternative sequence (4); Chain (1); Coiled coil (1); Modified residue (15); Repeat (16); Sequence conflict (1) FUNCTION: May serve as a scaffold protein for MADD and RAB3GA on synaptic vesicles of neuronal and endocrine homeostatic processes (By similarity). Plays a role in the brain as a key controller of neuronal and endocrine homeostatic processes (PubMed:25248098). {ECO:0000250|UniProtKB:Q8TDJ6, ECO:0000269|PubMed:25248098}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q8TDJ6}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8TDJ6}. Note=The external layer of the inferior boundary for the hypothalamus part of the human brain (the so called median eminence (ME)) displayed a punctate pattern of expression; expression also observed in the cell bodies lining the third ventricle, in the long processes extending from these cell bodies toward the external layer of the ME, in small clear vesicles, and in large dense core vesicles. {ECO:0000269|PubMed:25248098}. SUBUNIT: Interacts with MADD and RAB3GAP. {ECO:0000250|UniProtKB:Q8TDJ6}. TISSUE SPECIFICITY: Expressed in the brain and pituitary gland. Detected in the hippocampus, dentate gyrus, hypothalamus, pyriform cortex and the granular and molecular layers of the cerebellum of adult animals. In the hypothalamus, expression is observed in the arcuate nucleus, the ME, the organum vasculosum of the lamina terminalis, and the subfornical organ, the subcommissural organ, and the suprachiasmatic nucleus. Both tanycytes and hypothalamic neurosecretory neurons express the protein (PubMed:25248098). Expressed in the inner and outer hair cells as well as in the spiral ganglion neurons (PubMed:27657680). Expressed in insulin-secreting cells of the islets of Langerhans in the pancreas (PubMed:25248098). {ECO:0000269|PubMed:25248098, ECO:0000269|PubMed:27657680}. +O70348 DXO_MOUSE Decapping and exoribonuclease protein (DXO) (EC 3.1.13.-) (EC 3.6.1.-) (Dom-3 homolog Z) 397 45,280 Beta strand (16); Binding site (6); Chain (1); Helix (13); Metal binding (7); Modified residue (2); Mutagenesis (2); Sequence conflict (2); Turn (5) FUNCTION: Ribonuclease that specifically degrades pre-mRNAs with a defective 5' end cap and is part of a pre-mRNA capping quality control. Has decapping, pyrophosphohydrolase and 5'-3' exonuclease activities. Has decapping activity toward incomplete 5' end cap mRNAs such as unmethylated 5' end-capped RNA to release GpppN and 5' end monophosphate RNA. The 5' end monophosphate RNA is then degraded by the 5'-3' exoribonuclease activity, enabling this enzyme to decap and degrade incompletely capped mRNAs. Also possesses RNA 5'-pyrophosphohydrolase activity by hydrolyzing the 5' end triphosphate to release pyrophosphates. {ECO:0000269|PubMed:23523372}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +Q61062 DVL3_MOUSE Segment polarity protein dishevelled homolog DVL-3 (Dishevelled-3) (DSH homolog 3) 716 78,123 Chain (1); Domain (3); Modified residue (15); Sequence conflict (2) FUNCTION: Involved in the signal transduction pathway mediated by multiple Wnt genes. {ECO:0000269|PubMed:22227309}. PTM: Ubiquitinated. Deubiquitinated by CYLD, which acts on 'Lys-63'-linked ubiquitin chains (By similarity). {ECO:0000250|UniProtKB:Q92997}.; PTM: Phosphorylated by CSNK1D. {ECO:0000250|UniProtKB:Q92997}.; PTM: Arginine methylation may function as a switch in regulation of function in Wnt signaling. {ECO:0000250|UniProtKB:Q92997}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O14641}. SUBUNIT: Interacts (via the PDZ domain) with the C-terminal regions of VANGL1 and VANGL2. Interacts (via the region containing both the PDZ and DEP domains) with LRRFIP2; the DIX domain may inhibit this interaction. Interacts with CYLD. Interacts with CEP164 and DAB2. Interacts with DCDC2. Interacts with FOXK1 and FOXK2 (By similarity). Interacts with DAAM2 (PubMed:22227309). {ECO:0000250|UniProtKB:Q92997, ECO:0000269|PubMed:12805222, ECO:0000269|PubMed:15456783, ECO:0000269|PubMed:22227309}. TISSUE SPECIFICITY: Ubiquitous. +Q8JZP9 GA2L1_MOUSE GAS2-like protein 1 (Growth arrest-specific protein 2-like 1) 678 72,411 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (2); Initiator methionine (1); Modified residue (17) FUNCTION: Seems to be involved in the cross-linking of microtubules and microfilaments. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. +Q5SSG4 GA2L2_MOUSE GAS2-like protein 2 (Growth arrest-specific protein 2-like 2) 860 94,318 Chain (1); Domain (2) FUNCTION: Seems to be involved in the cross-linking of microtubules and microfilaments. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. +Q3UWW6 GA2L3_MOUSE GAS2-like protein 3 (Growth arrest-specific protein 2-like 3) 683 74,235 Chain (1); Domain (2); Modified residue (2); Sequence conflict (1) FUNCTION: Cytoskeletal linker protein. May promote and stabilize the formation of the actin and microtubule network (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Localizes to microtubule and actin cytoskeletons. {ECO:0000250}. SUBUNIT: Interacts (via CH domain) with F-actin. Interacts (via C terminus) with microtubules (By similarity). {ECO:0000250}. DOMAIN: The GAR domain modulates the binding strength to each cytoskeletal network. {ECO:0000250}. +Q9Z1S8 GAB2_MOUSE GRB2-associated-binding protein 2 (GRB2-associated binder 2) (Growth factor receptor bound protein 2-associated protein 2) (PH domain-containing adaptor molecule p97) 665 73,208 Chain (1); Domain (1); Modified residue (30); Motif (2); Mutagenesis (1); Sequence conflict (1) FUNCTION: Adapter protein which acts downstream of several membrane receptors including cytokine, antigen, hormone, cell matrix and growth factor receptors to regulate multiple signaling pathways. Regulates osteoclast differentiation mediating the TNFRSF11A/RANK signaling. In allergic response, it plays a role in mast cells activation and degranulation through PI-3-kinase regulation. Also involved in the regulation of cell proliferation and hematopoiesis. {ECO:0000269|PubMed:10068651, ECO:0000269|PubMed:11449275, ECO:0000269|PubMed:15750601, ECO:0000269|PubMed:17374739, ECO:0000269|PubMed:9885561}. PTM: Phosphorylated upon EGF stimulation. Phosphorylated on tyrosine residues by HCK upon IL6 signaling (By similarity). Phosphorylated on tyrosine residue(s) by the thrombopoietin receptor (TPOR), stem cell factor receptor (SCFR), and T-cell and B-cell antigen receptors, gp130, IL-2R and IL-3R. Phosphorylated upon stimulation of TNFRSF11A/RANK by TNFSF11/RANKL. {ECO:0000250, ECO:0000269|PubMed:10068651, ECO:0000269|PubMed:15750601, ECO:0000269|PubMed:19172738, ECO:0000269|PubMed:9885561}.; PTM: Dephosphorylated by PTPN11. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. SUBUNIT: Interacts with HCK (By similarity). Interacts with SHC1; may mediate interaction with receptors. Interacts with SYK. Interacts with PI-3 kinase. Interacts with GRB2 (via SH3 2 domain). Interacts (phosphorylated) with PTPN11. Interacts with TNFRSF11A (via cytoplasmic domain). Interacts (phosphorylated) with 14-3-3 family proteins SFN, YWHAB, YWHAE, YWHAG, YWHAH, YWHAQ and YWHAZ; prevents interaction with GRB2 and attenuates GAB2 signaling. {ECO:0000250, ECO:0000269|PubMed:10068651, ECO:0000269|PubMed:15750601, ECO:0000269|PubMed:16456001, ECO:0000269|PubMed:9885561}. DOMAIN: The SH3-binding motifs mediate interaction with SHC1 and GRB2.; DOMAIN: The PH domain mediates phosphatidylinositol 3,4,5-trisphosphate and phosphatidylinositol 3,4-bisphosphate binding. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:10068651, ECO:0000269|PubMed:9885561}. +Q8BSM5 GAB3_MOUSE GRB2-associated-binding protein 3 (GRB2-associated binder 3) (Growth factor receptor bound protein 2-associated protein 3) 595 67,840 Chain (1); Compositional bias (1); Domain (1); Modified residue (2); Sequence conflict (3) PTM: Phosphorylated on tyrosine residue(s) after macrophage colony-stimulating factor (M-CSF) receptor stimulation. {ECO:0000269|PubMed:11739737}. SUBUNIT: Interacts with PIK3R/p85, SHP2 and GRAP2/MONA. May interact with Grb2. {ECO:0000269|PubMed:11739737, ECO:0000269|PubMed:11997510}. TISSUE SPECIFICITY: Highly expressed in spleen and thymus and weakly in brain, heart, lung, kidney, uterus, and embryonic stem cells. Also expressed in myeloid and macrophage cell lines. +Q8QZV0 DEDD2_MOUSE DNA-binding death effector domain-containing protein 2 (DED-containing protein FLAME-3) (FADD-like anti-apoptotic molecule 3) 330 36,786 Chain (1); Domain (1); Motif (2) FUNCTION: May play a critical role in death receptor-induced apoptosis and may target CASP8 and CASP10 to the nucleus. May regulate degradation of intermediate filaments during apoptosis. May play a role in the general transcription machinery in the nucleus and might be an important regulator of the activity of GTF3C3. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Note=Nuclear, accumulated in subnuclear structures resembling nucleoli. {ECO:0000250}. SUBUNIT: Interacts with CASP8, CASP10 and GTF3C3. Homodimerizes and heterodimerizes with DEDD (By similarity). {ECO:0000250}. DOMAIN: Interactions with CASP8 and CASP10 are mediated by the DED domain. {ECO:0000250}. TISSUE SPECIFICITY: Expression is high in liver, heart, kidney, and testis but low in brain, spleen, lung, and skeleton muscle. +P28311 DEFA4_MOUSE Alpha-defensin 4 (Defensin-related cryptdin-4) 92 10,272 Beta strand (3); Disulfide bond (3); Peptide (1); Propeptide (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Probably contributes to the antimicrobial barrier function of the small bowel mucosa. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Paneth cells of the small bowel. +Q8C2K1 DEFI6_MOUSE Differentially expressed in FDCP 6 (DEF-6) (IRF4-binding protein) (SWAP-70-like adapter of T-cells) 630 73,454 Alternative sequence (1); Chain (1); Compositional bias (2); Domain (1); Modified residue (3); Sequence conflict (7) FUNCTION: Phosphatidylinositol 3,4,5-trisphosphate-dependent guanine nucleotide exchange factor (GEF) which plays a role in the activation of Rho GTPases RAC1, RhoA and CDC42. Can regulate cell morphology in cooperation with activated RAC1. Plays a role in Th2 (T helper cells) development and/or activation, perhaps by interfering with ZAP70 signaling. Required for optimal T-cell effector function, lymphocyte homeostasis and the prevention of systemic autoimmunity (By similarity). {ECO:0000250, ECO:0000269|PubMed:12648457, ECO:0000269|PubMed:12923183}. PTM: Tyrosine-phosphorylated by tyrosine-protein kinase LCK in response to T-cell activation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12648457}. Cell membrane {ECO:0000269|PubMed:12648457}. Nucleus {ECO:0000250|UniProtKB:Q9H4E7}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9H4E7}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9H4E7}. Cell projection, filopodium {ECO:0000250|UniProtKB:Q9H4E7}. Note=Recruited to the plasma membrane upon binding phosphatidylinositol 3,4,5-trisphosphate. Binds to actin filaments. {ECO:0000250|UniProtKB:Q9H4E7}. SUBUNIT: Interacts with IRF4, activated RAC1 and F-actin. Both the phosphorylated and non-phosphorylated forms bind phosphatidylinositol 3,4,5-trisphosphate (PtdInsP3) (By similarity). Interacts with ZAP70. {ECO:0000250, ECO:0000269|PubMed:12648457}. DOMAIN: The PH domain is essential for phosphatidylinositol 3,4,5-trisphosphate binding. TISSUE SPECIFICITY: Thymus. {ECO:0000269|PubMed:12648457}. DISEASE: Note=Defects in Def6 results in spontaneous development of a lupus-like syndrome in aging female mice. It is characterized by the accumulation of effector/memory T-cells and IgG B-cells, profound hypergammaglobulinemia, autoantibody production, and glomerulonephritis. {ECO:0000269|PubMed:12923183}. +Q9DCV6 DELE1_MOUSE DAP3-binding cell death enhancer 1 (Death ligand signal enhancer) 510 55,430 Chain (1); Erroneous initiation (1); Repeat (7); Transit peptide (1) FUNCTION: Essential for the induction of death receptor-mediated apoptosis through the regulation of caspase activation. {ECO:0000250|UniProtKB:Q14154}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q14154}. SUBUNIT: Interacts with DAP3. {ECO:0000250|UniProtKB:Q14154}. +Q8K382 DEN1A_MOUSE DENN domain-containing protein 1A (Connecdenn 1) (Connecdenn) 1016 111,538 Chain (1); Compositional bias (1); Domain (3); Modified residue (11); Motif (2); Sequence conflict (2) FUNCTION: Guanine nucleotide exchange factor (GEF) regulating clathrin-mediated endocytosis through RAB35 activation. Promotes the exchange of GDP to GTP, converting inactive GDP-bound RAB35 into its active GTP-bound form. Regulates clathrin-mediated endocytosis of synaptic vesicles and mediates exit from early endosomes (PubMed:17182770, PubMed:20159556). Binds phosphatidylinositol-phosphates (PtdInsPs), with some preference for PtdIns(3)P (PubMed:20159556). {ECO:0000269|PubMed:17182770, ECO:0000269|PubMed:20159556}. PTM: Phosphorylated on serine and/or threonine in an Akt-dependent manner. Phosphorylation probably regulates the guanine nucleotide exchange factor (GEF) activity, possibly by disrupting an intramolecular interaction between the DENN domain and the C-terminus of the protein, thereby relieving the autoinhibition. {ECO:0000250|UniProtKB:Q8TEH3}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000269|PubMed:17182770, ECO:0000269|PubMed:20159556}; Peripheral membrane protein {ECO:0000269|PubMed:17182770, ECO:0000269|PubMed:20159556}. Cell junction, synapse, presynaptic cell membrane {ECO:0000269|PubMed:17182770}. Note=Associates to membranes via lipid-binding activity. {ECO:0000269|PubMed:20159556}. SUBUNIT: Interacts with RAB35 (PubMed:20159556). Interacts with clathrin and with the adapter protein complex 2, AP-2 (By similarity). Interacts with ITSN1 AND SH3GL2 (PubMed:17182770). Interacts (when phosphorylated) with YWHAE (By similarity). {ECO:0000250|UniProtKB:Q8TEH3, ECO:0000269|PubMed:17182770, ECO:0000269|PubMed:20159556}. +Q99J56 DERL1_MOUSE Derlin-1 (Degradation in endoplasmic reticulum protein 1) (Der1-like protein 1) 251 28,835 Chain (1); Initiator methionine (1); Modified residue (4); Sequence conflict (3); Topological domain (5); Transmembrane (4) TRANSMEM 23 43 Helical; Name=1. {ECO:0000255}.; TRANSMEM 60 80 Helical; Name=2. {ECO:0000255}.; TRANSMEM 106 126 Helical; Name=3. {ECO:0000255}.; TRANSMEM 155 175 Helical; Name=4. {ECO:0000255}. TOPO_DOM 2 22 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 44 59 Lumenal. {ECO:0000255}.; TOPO_DOM 81 105 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 127 154 Lumenal. {ECO:0000255}.; TOPO_DOM 176 251 Cytoplasmic. {ECO:0000255}. FUNCTION: Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins. May act by forming a channel that allows the retrotranslocation of misfolded proteins into the cytosol where they are ubiquitinated and degraded by the proteasome. May mediate the interaction between VCP and the misfolded protein. Also involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for proteasomal degradation. By controlling the steady-state expression of the IGF1R receptor, indirectly regulates the insulin-like growth factor receptor signaling pathway. {ECO:0000250|UniProtKB:Q9BUN8}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9BUN8}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9BUN8}. SUBUNIT: Forms homo- and heterooligomers with DERL2 and DERL3; binding to DERL3 is poorer than that between DERL2 and DERL3. Interacts with AMFR, SELENOS, SEL1L, SELENOK, SYVN1 and VCP, as well as with SEL1L-SYVN1 and VCP-SELENOS protein complexes; this interaction is weaker than that observed between DERL2 and these complexes. Interacts with NGLY1 and YOD1. Does not bind to EDEM1 (By similarity). Interacts with DNAJB9 (PubMed:22267725). Interacts with RNF103. Interacts with HM13. Interacts with XBP1 isoform 1 (via luminal/ectodomain domain); the interaction obviates the need for ectodomain shedding prior HM13/SPP-mediated XBP1 isoform 1 cleavage. Interacts with the signal recognition particle/SRP and the SRP receptor; in the process of endoplasmic reticulum stress-induced pre-emptive quality control. May interact with UBXN6 (By similarity). Interacts with ZFAND2B; probably through VCP (PubMed:24160817). {ECO:0000250|UniProtKB:Q9BUN8, ECO:0000269|PubMed:22267725, ECO:0000269|PubMed:24160817}. TISSUE SPECIFICITY: Widely expressed, with lowest levels in brain and heart. {ECO:0000269|PubMed:16186509}. +Q9R0P5 DEST_MOUSE Destrin (Actin-depolymerizing factor) (ADF) (Sid 23) 165 18,522 Chain (1); Domain (1); Initiator methionine (1); Modified residue (3); Motif (1) FUNCTION: Actin-depolymerizing protein. Severs actin filaments (F-actin) and binds to actin monomers (G-actin). Acts in a pH-independent manner. PTM: ISGylated. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. Not found in skeletal muscle. {ECO:0000269|PubMed:11809832}. +Q64016 DFA17_MOUSE Alpha-defensin 17 (Defensin-related cryptdin-17) (CRYP17) (Fragment) 82 9,349 Disulfide bond (3); Non-terminal residue (1); Peptide (1); Propeptide (1); Signal peptide (1) FUNCTION: Probably contributes to the antimicrobial barrier function of the small bowel mucosa. SUBCELLULAR LOCATION: Secreted. +Q8BGW9 DFB29_MOUSE Beta-defensin 29 (BD-29) (mBD-29) (Defensin, beta 29) 78 9,067 Chain (1); Disulfide bond (3); Signal peptide (1) FUNCTION: Has antibacterial activity. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in the cauda epididymis. {ECO:0000269|PubMed:23765988}. +Q45VN2 DFA20_MOUSE Alpha-defensin 20 (Cryptdin-4) (Defensin-related cryptdin-20) 95 10,601 Disulfide bond (3); Peptide (1); Propeptide (1); Sequence conflict (2); Signal peptide (1) FUNCTION: May have microbicidal activities. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +Q30KN3 DFB33_MOUSE Beta-defensin 33 (BD-33) (mBD-33) (Defensin, beta 33) 62 7,105 Chain (1); Disulfide bond (3); Signal peptide (1) FUNCTION: Has antibacterial activity. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +Q8C1N8 DFA22_MOUSE Alpha-defensin 22 (Defensin-related cryptdin-22) 93 10,548 Disulfide bond (3); Peptide (1); Propeptide (1); Signal peptide (1) FUNCTION: May have microbicidal activities. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +Q5G865 DFA24_MOUSE Alpha-defensin 24 (Defensin-related cryptdin-24) 93 10,327 Disulfide bond (3); Peptide (1); Propeptide (1); Signal peptide (1) FUNCTION: May have microbicidal activities. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +Q7TMD2 DFB37_MOUSE Beta-defensin 37 (BD-37) (mBD-37) (Defensin, beta 37) 62 7,052 Chain (1); Disulfide bond (3); Signal peptide (1) FUNCTION: Has antibacterial activity. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. TISSUE SPECIFICITY: Only expressed in epididymis (corpus and cauda). {ECO:0000269|PubMed:14718547}. +P17533 DFAR1_MOUSE Alpha-defensin-related sequence 1 (CRS1C) (Cryptdin-related protein 1C) (Defensin-related cryptdin-related sequence 1) 116 12,941 Chain (1); Propeptide (1); Region (3); Repeat (9); Signal peptide (1) FUNCTION: Apparent precursor of a secreted, cationic, proline- and cysteine-rich peptide that contains Cys-Pro-Xaa repeats. Unlike cryptdin, the proposed mature peptide region lacks the structural motif characteristic of defensins. It may have microbicidal activities. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Small bowel. +Q80UP3 DGKZ_MOUSE Diacylglycerol kinase zeta (DAG kinase zeta) (EC 2.7.1.107) (Diglyceride kinase zeta) (DGK-zeta) 929 104,031 Chain (1); Compositional bias (3); Domain (1); Modified residue (2); Motif (1); Region (1); Repeat (2); Sequence conflict (1); Zinc finger (2) FUNCTION: Displays a strong preference for 1,2-diacylglycerols over 1,3-diacylglycerols, but lacks substrate specificity among molecular species of long chain diacylglycerols. Regulates RASGRP1 activity (By similarity). Positively regulates insulin-induced translocation of SLC2A4 to the cell membrane in adipocytes. Activates PIP5K1A activity via generation of phosphatidic acid (PubMed:27739494). {ECO:0000250|UniProtKB:Q13574, ECO:0000269|PubMed:27739494}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20023381}. Nucleus {ECO:0000269|PubMed:20023381}. Cell membrane {ECO:0000250|UniProtKB:Q13574}. SUBUNIT: Interacts with the PDZ domain of the syntrophin SNTG1 and that of SNX27. Forms a signaling complex with RASGRP1 and HRAS (By similarity). Interacts with IRS1 in the absence of insulin; insulin stimulation decreases this interaction (PubMed:27739494). Found in a ternary complex with IRS1 and PIP5K1A in the absence of insulin (PubMed:27739494). {ECO:0000250|UniProtKB:Q13574, ECO:0000269|PubMed:27739494}. +Q5SS80 DHR13_MOUSE Dehydrogenase/reductase SDR family member 13 (EC 1.1.-.-) (Short chain dehydrogenase/reductase family 7C member 5) 376 40,745 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Compositional bias (1); Frameshift (1); Nucleotide binding (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Putative oxidoreductase. {ECO:0000305}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q8BVI4 DHPR_MOUSE Dihydropteridine reductase (EC 1.5.1.34) (HDHPR) (Quinoid dihydropteridine reductase) 241 25,570 Active site (1); Chain (1); Modified residue (4); Nucleotide binding (1); Sequence conflict (1) FUNCTION: The product of this enzyme, tetrahydrobiopterin (BH-4), is an essential cofactor for phenylalanine, tyrosine, and tryptophan hydroxylases. {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +Q8VBZ0 DHRSX_MOUSE Dehydrogenase/reductase SDR family member on chromosome X homolog (EC 1.1.-.-) (DHRSXY) (SCAD family protein) 335 35,957 Active site (1); Binding site (1); Chain (1); Compositional bias (1); Nucleotide binding (1); Sequence conflict (3) FUNCTION: Involved in the positive regulation of starvation-induced autophagy. {ECO:0000250|UniProtKB:Q8N5I4}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8N5I4}. Note=Secreted in a non-classical form. A signal peptide sequence at position 1-23 is predicted. {ECO:0000250|UniProtKB:Q8N5I4}. +O08808 DIAP1_MOUSE Protein diaphanous homolog 1 (Diaphanous-related formin-1) (DRF1) (p140mDIA) (mDIA1) 1255 139,343 Beta strand (10); Chain (1); Coiled coil (2); Compositional bias (1); Domain (4); Helix (45); Modified residue (7); Turn (9) FUNCTION: Actin nucleation and elongation factor required for the assembly of F-actin structures, such as actin cables and stress fibers (PubMed:10678165, PubMed:15044801, PubMed:18572016, PubMed:23558171). Binds to the barbed end of the actin filament and slows down actin polymerization and depolymerization (PubMed:10678165, PubMed:15044801, PubMed:18572016). Required for cytokinesis, and transcriptional activation of the serum response factor (PubMed:10678165, PubMed:15044801, PubMed:18572016). DFR proteins couple Rho and Src tyrosine kinase during signaling and the regulation of actin dynamics (PubMed:10678165, PubMed:15044801, PubMed:18572016). Functions as a scaffold protein for MAPRE1 and APC to stabilize microtubules and promote cell migration (PubMed:15311282). Has neurite outgrowth promoting activity (PubMed:10678165, PubMed:15044801, PubMed:18572016). Acts in a Rho-dependent manner to recruit PFY1 to the membrane (PubMed:9214622). The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex (By similarity). It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity (By similarity). In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization (By similarity). Required in the control of cell shape (By similarity). Also acts as an actin nucleation and elongation factor in the nucleus by promoting nuclear actin polymerization inside the nucleus to drive serum-dependent SRF-MRTFA activity (PubMed:23558171). {ECO:0000250|UniProtKB:O60610, ECO:0000269|PubMed:10678165, ECO:0000269|PubMed:15044801, ECO:0000269|PubMed:15311282, ECO:0000269|PubMed:18572016, ECO:0000269|PubMed:23558171, ECO:0000269|PubMed:9214622}. PTM: Phosphorylation at Thr-751 is stimulated by cAMP and regulates stability, complex formation and mitochondrial movement (By similarity). {ECO:0000250|UniProtKB:O60610}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9214622}. Cell projection, ruffle membrane {ECO:0000269|PubMed:9214622}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9214622}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:O60610}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:O60610}. Cytoplasm {ECO:0000269|PubMed:23558171}. Nucleus {ECO:0000269|PubMed:23558171}. Note=Membrane ruffles, especially at the tip of ruffles, of motile cells. {ECO:0000269|PubMed:9214622}. SUBUNIT: Homodimer (PubMed:14992721, PubMed:15864301). Interacts with the GTP-bound form of RHOA (PubMed:9214622). Interacts with RHOC, PFY1, MAPRE1, BAIAP2 and APC (PubMed:10814512, PubMed:15311282, PubMed:15864301). Interacts with SCAI (PubMed:19350017). Interacts with DCAF7, via FH2 domain (By similarity). Interacts with NCDN (PubMed:18572016). Interacts with OSBPL10, OSBPL2, VIM, TUBB and DYN1 (By similarity). {ECO:0000250|UniProtKB:O60610, ECO:0000269|PubMed:10814512, ECO:0000269|PubMed:14992721, ECO:0000269|PubMed:15311282, ECO:0000269|PubMed:15864301, ECO:0000269|PubMed:18572016, ECO:0000269|PubMed:19350017, ECO:0000269|PubMed:9214622}. DOMAIN: The DAD domain regulates activation via by an autoinhibitory interaction with the GBD/FH3 domain. This autoinhibition is released upon competitive binding of an activated GTPase. The release of DAD allows the FH2 domain to then nucleate and elongate nonbranched actin filaments. {ECO:0000269|PubMed:16292343}. TISSUE SPECIFICITY: Widely expressed. In the organ of Corti, it is expressed at the outer and inner hair cell layers. Expression at the inner hair cell layer is restricted to inner pillar cells. Detected in cochlear spiral ganglion neurons (PubMed:27808407). {ECO:0000269|PubMed:27808407}. +Q6PGC1 DHX29_MOUSE ATP-dependent RNA helicase DHX29 (EC 3.6.4.13) (DEAH box protein 29) 1365 153,975 Chain (1); Coiled coil (1); Compositional bias (3); Domain (2); Modified residue (3); Motif (1); Nucleotide binding (1) FUNCTION: ATP-binding RNA helicase involved in translation initiation. Part of the 43S pre-initiation complex that is required for efficient initiation on mRNAs of higher eukaryotes with structured 5'-UTRs by promoting efficient NTPase-dependent 48S complex formation. Specifically binds to the 40S ribosome near the mRNA entrance. Does not possess a processive helicase activity. {ECO:0000255|HAMAP-Rule:MF_03068}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03068}. SUBUNIT: Part of the 43S pre-initiation complex (PIC) that contains at least Met-tRNA, EIF1, EIF1A (EIF1AX or EIF1AY), EIF2S1, EIF2S2, EIF2S3, EIF3A, EIF3B, EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L, EIF3M, DHX29 and the 40S ribosomal subunit. {ECO:0000255|HAMAP-Rule:MF_03068}. +Q3USZ8 DIK2A_MOUSE Divergent protein kinase domain 2A (Deleted in autism protein 1 homolog) (Golgi Protein of 49 kDa) (GoPro49) (Hypoxia and AKT-induced stem cell factor) (HASF) 430 49,463 Chain (1); Sequence conflict (2); Signal peptide (1) FUNCTION: May play a role in cardiomyocyte proliferation through paracrine signaling and activation of the PI3-kinase signaling cascade. {ECO:0000269|PubMed:23784961}. SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasmic vesicle, COPI-coated vesicle. Secreted. TISSUE SPECIFICITY: Expressed in heart, brain, liver, spleen, kidney, lung, thymus, testis, ovary and muscle. {ECO:0000269|PubMed:23784961}. +Q8BTT6 DIEXF_MOUSE Digestive organ expansion factor homolog 772 88,818 Chain (1); Compositional bias (1); Modified residue (1); Sequence conflict (6) FUNCTION: Regulates the p53 pathway to control the expansion growth of digestive organs. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. +Q91ZF0 DJC24_MOUSE DnaJ homolog subfamily C member 24 (CSL-type zinc finger-containing protein 3) (Diphthamide biosynthesis protein 4) (J domain protein DjC7) 148 16,922 Beta strand (3); Chain (1); Domain (1); Helix (4); Sequence caution (1); Sequence conflict (2); Zinc finger (1) Protein modification; peptidyl-diphthamide biosynthesis. FUNCTION: The iron-bound form is redox-active and can function as electron carrier (By similarity). Stimulates the ATPase activity of several Hsp70-type chaperones. This ability is enhanced by iron-binding. Plays a role in the diphthamide biosynthesis, a post-translational modification of histidine which occurs in translation elongation factor 2 (EEF2). {ECO:0000250, ECO:0000269|PubMed:11595173, ECO:0000269|PubMed:18765564}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:18765564}. SUBUNIT: Monomer and homooligomer. Iron binding promotes oligomerization (By similarity). {ECO:0000250}. DOMAIN: The DPH-type zinc finger can also bind iron ions instead of the expected zinc ions. {ECO:0000250}. TISSUE SPECIFICITY: Detected in heart, brain, spleen, lung, liver, kidney and testis. {ECO:0000269|PubMed:11595173}. +Q811T9 DISC1_MOUSE Disrupted in schizophrenia 1 homolog 852 92,525 Alternative sequence (4); Beta strand (2); Chain (1); Coiled coil (2); Helix (2); Region (8); Sequence conflict (36); Turn (1) FUNCTION: Involved in the regulation of multiple aspects of embryonic and adult neurogenesis. Required for neural progenitor proliferation in the ventrical/subventrical zone during embryonic brain development and in the adult dentate gyrus of the hippocampus. Participates in the Wnt-mediated neural progenitor proliferation as a positive regulator by modulating GSK3B activity and CTNNB1 abundance. Plays a role as a modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including neuron positioning, dendritic development and synapse formation. Inhibits the activation of AKT-mTOR signaling upon interaction with CCDC88A. Regulates the migration of early-born granule cell precursors toward the dentate gyrus during the hippocampal development. Plays a role, together with PCNT, in the microtubule network formation. {ECO:0000269|PubMed:17825401, ECO:0000269|PubMed:19303846, ECO:0000269|PubMed:19502360, ECO:0000269|PubMed:19778506}. PTM: Ubiquitinated. Ubiquitination with 'Lys-48'-linked polyubiquitin chains leads to its proteasomal degradation. {ECO:0000250|UniProtKB:Q9NRI5}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14962739}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9NRI5}. Mitochondrion {ECO:0000250|UniProtKB:Q9NRI5}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9NRI5}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000269|PubMed:22072671}. Note=Colocalizes with NDEL1 in the perinuclear region and the centrosome (PubMed:14962739). Localizes to punctate cytoplasmic foci which overlap in part with mitochondria. Colocalizes with PCNT at the centrosome (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9NRI5, ECO:0000269|PubMed:14962739}. SUBUNIT: Interacts with NDEL1 (PubMed:14962739). Interacts with CCDC88A (via C-terminus); the interaction is direct (PubMed:19778506). Interacts with GSK3B (PubMed:19303846). Interacts with tubulin alpha, ACTN2, ANKHD1, ATF4, ATF5, CEP63, EIF3S3, MAP1A, NDEL1, PAFAH1B1, RANBP9, SPTBN4, SYNE1 and TRAF3IP1. Interaction with microtubules may be mediated in part by TRAF3IP1. Interacts (via C-terminal) with PCNT. Interacts with CHCHD6 (By similarity). Interacts with CCDC141 (PubMed:20956536). Interacts with FBXW7, the substrate-recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex; the interaction targets DISC1 for proteasomal degradation (By similarity). Interacts with ZNF365 (By similarity). {ECO:0000250|UniProtKB:Q9NRI5, ECO:0000269|PubMed:14962739, ECO:0000269|PubMed:19303846, ECO:0000269|PubMed:19778506, ECO:0000269|PubMed:20956536}. TISSUE SPECIFICITY: Expressed in granule cell precursors within the dentate migratory stream during the first week of postnatal life and in differentiated granule cells of the hippocampus (at protein level). Detected in heart, brain, kidney, and testis (PubMed:12504857). Expressed in dentate gyrus, hippocampus and in the olfactory bulb. {ECO:0000269|PubMed:12504857, ECO:0000269|PubMed:17825401, ECO:0000269|PubMed:19502360}. +Q3TDN0 DISP1_MOUSE Protein dispatched homolog 1 (Mdispa) 1521 170,130 Alternative sequence (2); Chain (1); Domain (1); Glycosylation (5); Mutagenesis (5); Sequence conflict (8); Transmembrane (12) TRANSMEM 189 209 Helical. {ECO:0000255}.; TRANSMEM 499 519 Helical. {ECO:0000255}.; TRANSMEM 524 544 Helical. {ECO:0000255}.; TRANSMEM 548 568 Helical. {ECO:0000255}.; TRANSMEM 603 623 Helical. {ECO:0000255}.; TRANSMEM 637 657 Helical. {ECO:0000255}.; TRANSMEM 717 737 Helical. {ECO:0000255}.; TRANSMEM 986 1006 Helical. {ECO:0000255}.; TRANSMEM 1008 1028 Helical. {ECO:0000255}.; TRANSMEM 1038 1058 Helical. {ECO:0000255}.; TRANSMEM 1081 1101 Helical. {ECO:0000255}.; TRANSMEM 1109 1129 Helical. {ECO:0000255}. FUNCTION: Functions in hedgehog (Hh) signaling. Regulates the release and extracellular accumulation of cholesterol-modified hedgehog proteins and is hence required for effective production of the Hh signal. Synergizes with SCUBE2 to cause a increase in SHH secretion (PubMed:22902404). {ECO:0000269|PubMed:12372258, ECO:0000269|PubMed:12372301, ECO:0000269|PubMed:12421714, ECO:0000269|PubMed:22902404}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Interacts with SHH; via the cholesterol anchor of the dually lipid-modified SHH (ShhNp) (PubMed:22902404). {ECO:0000269|PubMed:22902404}. +Q5PR73 DIRA2_MOUSE GTP-binding protein Di-Ras2 (Distinct subgroup of the Ras family member 2) 199 22,498 Chain (1); Lipidation (1); Modified residue (3); Motif (1); Nucleotide binding (5); Propeptide (1) FUNCTION: Displays low GTPase activity and exists predominantly in the GTP-bound form. {ECO:0000250|UniProtKB:Q96HU8}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. +Q9QUN9 DKK3_MOUSE Dickkopf-related protein 3 (Dickkopf-3) (Dkk-3) (mDkk-3) 349 38,388 Chain (1); Coiled coil (1); Disulfide bond (4); Glycosylation (4); Region (2); Signal peptide (1) FUNCTION: Antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by forming a ternary complex with the transmembrane protein KREMEN that promotes internalization of LRP5/6. DKKs play an important role in vertebrate development, where they locally inhibit Wnt regulated processes such as antero-posterior axial patterning, limb development, somitogenesis and eye formation. In the adult, Dkks are implicated in bone formation and bone disease, cancer and Alzheimer disease (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Interacts with LRP5 and LRP6. {ECO:0000250}. DOMAIN: The C-terminal cysteine-rich domain mediates interaction with LRP5 and LRP6. {ECO:0000250}. TISSUE SPECIFICITY: Highest expression in brain, eye and heart. +P40764 DLX2_MOUSE Homeobox protein DLX-2 (Homeobox protein TES-1) 332 34,746 Chain (1); Compositional bias (4); DNA binding (1); Modified residue (1) FUNCTION: Acts as a transcriptional activator (PubMed:21875655). Plays a role in terminal differentiation of interneurons, such as amacrine and bipolar cells in the developing retina (PubMed:21875655). Likely to play a regulatory role in the development of the ventral forebrain (PubMed:1678612). May play a role in craniofacial patterning and morphogenesis (PubMed:1678612). {ECO:0000269|PubMed:1678612, ECO:0000269|PubMed:21875655}. PTM: Phosphorylated by serine/threonine kinases. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Interacts (via homeobox DNA-binding domain) with POU4F2; this interaction enhances retinal ganglion cell (RGC) differentiation (PubMed:21875655). {ECO:0000269|PubMed:21875655}. TISSUE SPECIFICITY: Expressed only in neural and other ectodermal structures of the head: the brain, the vomeronasal organ, and the preameloblasts of the teeth (PubMed:8098616). Primarily expressed in the germinal cells of the ventral forebrain in the midgestational embryo, and in both dorsal and ventral ventricular zones in late embryogenesis and early postnatal life (PubMed:8098616). Expressed in the inner nuclear layer of the retina (PubMed:21875655). {ECO:0000269|PubMed:21875655, ECO:0000269|PubMed:8098616}. +Q6ZQJ5 DNA2_MOUSE DNA replication ATP-dependent helicase/nuclease DNA2 (DNA replication ATP-dependent helicase-like homolog) [Includes: DNA replication nuclease DNA2 (EC 3.1.-.-); DNA replication ATP-dependent helicase DNA2 (EC 3.6.4.12)] 1062 119,447 Alternative sequence (2); Beta strand (41); Chain (1); Erroneous initiation (1); Helix (56); Metal binding (4); Nucleotide binding (1); Region (2); Sequence conflict (8); Turn (8) FUNCTION: Key enzyme involved in DNA replication and DNA repair in nucleus and mitochondrion. Involved in Okazaki fragments processing by cleaving long flaps that escape FEN1: flaps that are longer than 27 nucleotides are coated by replication protein A complex (RPA), leading to recruit DNA2 which cleaves the flap until it is too short to bind RPA and becomes a substrate for FEN1. Also involved in 5'-end resection of DNA during double-strand break (DSB) repair: recruited by BLM and mediates the cleavage of 5'-ssDNA, while the 3'-ssDNA cleavage is prevented by the presence of RPA. Also involved in DNA replication checkpoint independently of Okazaki fragments processing. Possesses different enzymatic activities, such as single-stranded DNA (ssDNA)-dependent ATPase, 5'-3' helicase and endonuclease activities. While the ATPase and endonuclease activities are well-defined and play a key role in Okazaki fragments processing and DSB repair, the 5'-3' DNA helicase activity is subject to debate. According to various reports, the helicase activity is weak and its function remains largely unclear. Helicase activity may promote the motion of DNA2 on the flap, helping the nuclease function (By similarity). {ECO:0000250}. PTM: Acetylated by EP300, leading to stimulate the 5'-3' endonuclease, the 5'-3' helicase and DNA-dependent ATPase activities, possibly by increasing DNA substrate affinity. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Mitochondrion {ECO:0000250}. SUBUNIT: Interacts with BLM and WDHD1. {ECO:0000250}. +A2A9I7 DMRTB_MOUSE Doublesex- and mab-3-related transcription factor B1 (Doublesex- and mab-3-related transcription factor 6) 359 38,424 Chain (1); Compositional bias (1); DNA binding (1) SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00070}. TISSUE SPECIFICITY: Brain. {ECO:0000269|PubMed:12609607}. +Q61880 DMC1_MOUSE Meiotic recombination protein DMC1/LIM15 homolog 340 37,821 Binding site (5); Chain (1); Nucleotide binding (1) FUNCTION: May participate in meiotic recombination, specifically in homologous strand assimilation, which is required for the resolution of meiotic double-strand breaks. {ECO:0000269|PubMed:17639081}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome {ECO:0000269|PubMed:22549958}. SUBUNIT: Double stacked ring-shaped homooctamer (By similarity). Interacts with the MND1-PSMC3IP heterodimer. Interacts with BRCA2 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Testis. +P59108 CPNE2_MOUSE Copine-2 (Copine II) 548 61,036 Chain (1); Domain (3); Mutagenesis (8); Region (1); Sequence conflict (1) FUNCTION: Calcium-dependent phospholipid-binding protein that plays a role in calcium-mediated intracellular processes. Exhibits calcium-dependent cell membrane binding properties (PubMed:21087455, PubMed:26175110). {ECO:0000269|PubMed:21087455, ECO:0000269|PubMed:26175110}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21087455, ECO:0000269|PubMed:26175110}. Nucleus {ECO:0000269|PubMed:21087455, ECO:0000269|PubMed:26175110}. Cell membrane {ECO:0000269|PubMed:21087455, ECO:0000269|PubMed:26175110}. Note=Translocates to the cell membrane and the nucleus in a calcium-dependent manner (PubMed:21087455, PubMed:26175110). Colocalizes with CD2 at the cell membrane (PubMed:21087455). {ECO:0000269|PubMed:21087455, ECO:0000269|PubMed:26175110}. DOMAIN: The C2 domain 2, but not the C2 domain 1, is necessary for calcium-mediated membrane association (PubMed:21087455, PubMed:26175110). The linker region is necessary for calcium-dependent cell membrane association (PubMed:21087455). {ECO:0000269|PubMed:21087455, ECO:0000269|PubMed:26175110}. +Q3V0P1 CPXCR_MOUSE CPX chromosomal region candidate gene 1 protein homolog 322 37,706 Chain (1); Sequence conflict (1) +Q812E0 CPEB2_MOUSE Cytoplasmic polyadenylation element-binding protein 2 (CPE-BP2) (CPE-binding protein 2) (mCPEB-2) 521 58,442 Chain (1); Domain (2); Modified residue (1) FUNCTION: May play a role in translational regulation of stored mRNAs in transcriptionally inactive haploid spermatids. Binds to poly(U) RNA oligomers (PubMed:12672660). Required for cell cycle progression, specifically for the transition from metaphase to anaphase (By similarity). {ECO:0000250|UniProtKB:Q7Z5Q1, ECO:0000269|PubMed:12672660}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12672660}. SUBUNIT: Interacts with TENT2/GLD2. {ECO:0000269|PubMed:17927953}. TISSUE SPECIFICITY: Expressed in embryo, cerebellum, salivary gland, thymus, heart, liver, lung, spleen, kidney, intestine, ovary and round spermatids. Weakly expressed in granular cells of dentate gyrus and the pyramidal cells of CA3 and CA1 of the hippocampus. {ECO:0000269|PubMed:12672660, ECO:0000269|PubMed:12871996}. +Q9JJV1 CRBA2_MOUSE Beta-crystallin A2 (Beta-A2 crystallin) 197 22,237 Chain (1); Domain (4); Region (2) FUNCTION: Crystallins are the dominant structural components of the vertebrate eye lens. SUBUNIT: Homo/heterodimer, or complexes of higher-order. The structure of beta-crystallin oligomers seems to be stabilized through interactions between the N-terminal arms (By similarity). {ECO:0000250}. DOMAIN: Has a two-domain beta-structure, folded into four very similar Greek key motifs. +P52825 CPT2_MOUSE Carnitine O-palmitoyltransferase 2, mitochondrial (EC 2.3.1.21) (Carnitine palmitoyltransferase II) (CPT II) 658 73,981 Active site (1); Binding site (3); Chain (1); Intramembrane (1); Modified residue (14); Region (1); Sequence conflict (2); Topological domain (2); Transit peptide (1) INTRAMEM 179 208 Note=Mitochondrial inner membrane. {ECO:0000250}. TOPO_DOM 26 178 Mitochondrial matrix. {ECO:0000250}.; TOPO_DOM 209 658 Mitochondrial matrix. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Matrix side {ECO:0000250}. +Q9Z125 CR3L1_MOUSE Cyclic AMP-responsive element-binding protein 3-like protein 1 (cAMP-responsive element-binding protein 3-like protein 1) (Old astrocyte specifically-induced substance) (OASIS) [Cleaved into: Processed cyclic AMP-responsive element-binding protein 3-like protein 1 (Oasis N-terminal fragment) (OA-N)] 519 56,959 Alternative sequence (1); Chain (2); Cross-link (1); Domain (1); Glycosylation (3); Motif (2); Mutagenesis (3); Region (3); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 377 397 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 376 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 398 519 Lumenal. {ECO:0000255}. FUNCTION: Transcription factor involved in unfolded protein response (UPR). Binds the DNA consensus sequence 5'-GTGXGCXGC-3' (By similarity). In the absence of endoplasmic reticulum (ER) stress, inserted into ER membranes, with N-terminal DNA-binding and transcription activation domains oriented toward the cytosolic face of the membrane. In response to ER stress, transported to the Golgi, where it is cleaved in a site-specific manner by resident proteases S1P/MBTPS1 and S2P/MBTPS2. The released N-terminal cytosolic domain is translocated to the nucleus to effect transcription of specific target genes. Plays a critical role in bone formation through the transcription of COL1A1, and possibly COL1A2, and the secretion of bone matrix proteins. Directly binds to the UPR element (UPRE)-like sequence in an osteoblast-specific COL1A1 promoter region and induces its transcription. Does not regulate COL1A1 in other tissues, such as skin (PubMed:19767743). Required to protect astrocytes from ER stress-induced cell death. In astrocytes, binds to the cAMP response element (CRE) of the BiP/HSPA5 promoter and participate in its transcriptional activation (PubMed:15665855). Inhibits cell-cycle progression by binding to promoters and activating transcription of genes encoding cell-cycle inhibitors, such as p21/CDKN1A (By similarity). Required for TGFB1 to activate genes involved in the assembly of collagen extracellular matrix (By similarity). {ECO:0000250|UniProtKB:Q96BA8, ECO:0000269|PubMed:12480185, ECO:0000269|PubMed:15665855, ECO:0000269|PubMed:19767743}. PTM: N-glycosylated. {ECO:0000269|PubMed:15665855}.; PTM: Ubiquitinated by HRD1/SYVN1; undergoes 'Lys-48'-linked ubiquitination, followed by rapid proteasomal degradation under normal conditions. Upon ER stress, SYVN1 E3 ubiquitin-protein ligase dissociates from its substrate, ubiquitination does not occur and CREB3L1 is stabilized. {ECO:0000269|PubMed:22705851}.; PTM: Upon ER stress, translocated to the Golgi apparatus, where it is processed by regulated intramembrane proteolysis (RIP) to release the cytosol-facing N-terminal transcription factor domain (PubMed:19767743). The cleavage is performed sequentially by site-1 and site-2 proteases (S1P/MBTPS1 and S2P/MBTPS2). RIP is induced by TGFB1 and ceramide. {ECO:0000250|UniProtKB:Q96BA8, ECO:0000269|PubMed:19767743}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15665855, ECO:0000269|PubMed:19767743}; Single-pass type II membrane protein {ECO:0000269|PubMed:15665855}. Note=ER membrane resident protein. Upon ER stress, translocated to the Golgi apparatus where it is cleaved. The cytosolic N-terminal fragment (processed cyclic AMP-responsive element-binding protein 3-like protein 1) is transported into the nucleus. {ECO:0000269|PubMed:15665855, ECO:0000269|PubMed:19767743}.; SUBCELLULAR LOCATION: Processed cyclic AMP-responsive element-binding protein 3-like protein 1: Nucleus {ECO:0000269|PubMed:15665855, ECO:0000269|PubMed:19767743}. Note=Upon ER stress, transported into the nucleus. {ECO:0000269|PubMed:15665855, ECO:0000269|PubMed:19767743}. SUBUNIT: Interacts with SMAD4, the interaction takes place upon TGFB1 induction and SMAD4 acts as CREB3L1 coactivator to induce the expression of genes involved in assembly of collagen extracellular matrix. {ECO:0000250|UniProtKB:Q96BA8}. TISSUE SPECIFICITY: Expressed in cortical and trabecular bones. Highly expressed in osteoblasts, but not detected in osteoclasts, nor in macrophages (PubMed:19767743). Expressed at relatively low levels in lung and kidney. Weakly expressed in brain and spleen. {ECO:0000269|PubMed:10350641, ECO:0000269|PubMed:19767743}. +Q8BS40 CPTP_MOUSE Ceramide-1-phosphate transfer protein (CPTP) (Glycolipid transfer protein domain-containing protein 1) 216 24,597 Binding site (5); Chain (1); Helix (12); Sequence conflict (1); Turn (1) FUNCTION: Mediates the intracellular transfer of ceramide-1-phosphate (C1P) between organelle membranes and the cell membrane. Required for normal structure of the Golgi stacks. Can bind phosphoceramides with a variety of aliphatic chains, but has a preference for lipids with saturated C16:0 or monounsaturated C18:1 aliphatic chains, and is inefficient with phosphoceramides containing lignoceryl (C24:0). Plays a role in the regulation of the cellular levels of ceramide-1-phosphate, and thereby contributes to the regulation of phospholipase PLA2G4A activity and the release of arachidonic acid. Has no activity with galactosylceramide, lactosylceramide, sphingomyelin, phosphatidylcholine, phosphatidic acid and ceramide. C1P transfer is stimulated by phosphatidylserine in C1P source vesicles (By similarity). Regulates autophagy, inflammasome mediated IL1B and IL18 processing, and pyroptosis, but not apoptosis (PubMed:29164996). {ECO:0000250|UniProtKB:Q5TA50, ECO:0000269|PubMed:29164996}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q5TA50}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q5TA50}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q5TA50}. Cell membrane {ECO:0000250|UniProtKB:Q5TA50}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q5TA50}; Cytoplasmic side {ECO:0000250|UniProtKB:Q5TA50}. Endosome membrane {ECO:0000250|UniProtKB:Q5TA50}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q5TA50}. Nucleus outer membrane {ECO:0000250|UniProtKB:Q5TA50}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q5TA50}. +Q9JJU9 CRBB3_MOUSE Beta-crystallin B3 (Beta-B3 crystallin) [Cleaved into: Beta-crystallin B3, N-terminally processed] 211 24,291 Chain (2); Domain (4); Initiator methionine (1); Modified residue (2); Region (3) FUNCTION: Crystallins are the dominant structural components of the vertebrate eye lens. SUBUNIT: Homo/heterodimer, or complexes of higher-order. The structure of beta-crystallin oligomers seems to be stabilized through interactions between the N-terminal arms (By similarity). {ECO:0000250}. DOMAIN: Has a two-domain beta-structure, folded into four very similar Greek key motifs. +Q8BGC9 CREG2_MOUSE Protein CREG2 288 31,764 Chain (1); Erroneous initiation (1); Frameshift (1); Glycosylation (1); Mutagenesis (3); Sequence conflict (3); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12408961}. TISSUE SPECIFICITY: Brain specific. {ECO:0000269|PubMed:12408961}. +Q91XD7 CREL1_MOUSE Cysteine-rich with EGF-like domain protein 1 420 45,718 Chain (1); Disulfide bond (6); Domain (2); Glycosylation (1); Repeat (2); Signal peptide (1); Topological domain (3); Transmembrane (2) TRANSMEM 363 383 Helical. {ECO:0000255}.; TRANSMEM 385 405 Helical. {ECO:0000255}. TOPO_DOM 30 362 Extracellular. {ECO:0000255}.; TOPO_DOM 384 384 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 406 420 Extracellular. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9QZ05 E2AK4_MOUSE eIF-2-alpha kinase GCN2 (Eukaryotic translation initiation factor 2-alpha kinase 4) (EC 2.7.11.1) (GCN2-like protein) (mGCN2) 1648 186,487 Active site (1); Alternative sequence (12); Beta strand (10); Binding site (1); Chain (1); Coiled coil (1); Compositional bias (1); Domain (3); Helix (9); Modified residue (6); Mutagenesis (3); Nucleotide binding (1); Region (1); Sequence conflict (62); Turn (2) FUNCTION: Metabolic-stress sensing protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (eIF-2-alpha/EIF2S1) on 'Ser-52' in response to low amino acid availability (PubMed:10504407, PubMed:10655230, PubMed:12176355, PubMed:12215525, PubMed:15213227, PubMed:16054071, PubMed:16176978, PubMed:16121183, PubMed:15774759, PubMed:16601681, PubMed:26102367). Plays a role as an activator of the integrated stress response (ISR) required for adapatation to amino acid starvation. Converts phosphorylated eIF-2-alpha/EIF2S1 either to a competitive inhibitor of the translation initiation factor eIF-2B, leading to a global protein synthesis repression, and thus to a reduced overall utilization of amino acids, or to a translational initiation activation of specific mRNAs, such as the transcriptional activator ATF4, and hence allowing ATF4-mediated reprogramming of amino acid biosynthetic gene expression to alleviate nutrient depletion (PubMed:10655230, PubMed:11106749, PubMed:12176355, PubMed:15213227, PubMed:16176978, PubMed:26102367). Binds uncharged tRNAs (By similarity). Involved in cell cycle arrest by promoting cyclin D1 mRNA translation repression after the unfolded protein response pathway (UPR) activation or cell cycle inhibitor CDKN1A/p21 mRNA translation activation in response to amino acid deprivation (PubMed:16176978, PubMed:26102367). Plays a role in the consolidation of synaptic plasticity, learning as well as formation of long-term memory (PubMed:16121183). Plays a role in neurite outgrowth inhibition (PubMed:23447528). Plays a role in feeding behavior to maintain amino acid homeostasis; contributes to the innate aversion toward diets of imbalanced amino acid composition (PubMed:16054071, PubMed:15774759). Plays a proapoptotic role in response to glucose deprivation (PubMed:20660158). Promotes global cellular protein synthesis repression in response to UV irradiation independently of the stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK) and p38 MAPK signaling pathways (PubMed:12176355). {ECO:0000250|UniProtKB:P15442, ECO:0000269|PubMed:10504407, ECO:0000269|PubMed:10655230, ECO:0000269|PubMed:11106749, ECO:0000269|PubMed:12176355, ECO:0000269|PubMed:12215525, ECO:0000269|PubMed:15213227, ECO:0000269|PubMed:15774759, ECO:0000269|PubMed:16054071, ECO:0000269|PubMed:16121183, ECO:0000269|PubMed:16176978, ECO:0000269|PubMed:16601681, ECO:0000269|PubMed:20660158, ECO:0000269|PubMed:23447528, ECO:0000269|PubMed:26102367}.; FUNCTION: (Microbial infection) Plays a role in the antiviral response against alphavirus infection; impairs early viral mRNA translation of the incoming genomic virus RNA, thus preventing alphavirus replication. {ECO:0000269|PubMed:16601681}.; FUNCTION: (Microbial infection) Plays a role in modulating the adaptive immune response to Yellow fever virus infection; promotes dendritic cells to initiate autophagy and antigene presentation to both CD4(+) and CD8(+) T-cells under amino acid starvation. {ECO:0000269|PubMed:24310610}. PTM: Autophosphorylated; autophosphorylation on Thr-898 is increased upon amino acid starvation and in UV irradiation cells and inhibited in presence of IMPACT (PubMed:10504407, PubMed:10655230, PubMed:11106749, PubMed:12176355, PubMed:16601681, PubMed:24333428). {ECO:0000269|PubMed:10504407, ECO:0000269|PubMed:10655230, ECO:0000269|PubMed:11106749, ECO:0000269|PubMed:12176355, ECO:0000269|PubMed:16601681, ECO:0000269|PubMed:24333428}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:23447528}. SUBUNIT: Homodimer; homodimerization is important for kinase activation by uncharged tRNAs (By similarity). Interacts with GCN1; this interaction stimulates EIF2AK4/GCN2 kinase activity and is impaired by IMPACT upon a variety of stress conditions, such as amino acid depletion, UV-C irradiation, proteasome inhibitor treatment and glucose deprivation (PubMed:24333428). Interacts with DNAJC3; this interaction inhibits EIF2AK4/GCN2 kinase activity during endoplasmic reticulum (ER), hypothermic and amino acid-starving stress conditions (PubMed:25329545). {ECO:0000250|UniProtKB:P15442, ECO:0000269|PubMed:24333428, ECO:0000269|PubMed:25329545}. DOMAIN: The histidyl-tRNA synthetase-like region and protein kinase domains are necessary for eIF-2-alpha kinase activity and eIF-2-alpha-mediated translational control (PubMed:10655230). The histidyl-tRNA synthetase-like domain is necessary for binding to uncharged tRNAs (PubMed:16601681). Kinase domain 1 is a degenerate kinase domain (PubMed:10504407). {ECO:0000269|PubMed:10504407, ECO:0000269|PubMed:10655230}. TISSUE SPECIFICITY: Expressed in liver (PubMed:10504407). Expressed predominantly in the hippocampal CA1 region and the dentate gyrus, and to a lesser degree in CA3 (at protein level) (PubMed:16121183). Expressed in liver, lung, brain, kidney, skeletal muscle and testis (PubMed:10504407, PubMed:10655230). Expressed weakly in heart and spleen (PubMed:10655230). Expressed in the hippocampal CA1 and CA3 regions, the dentate gyrus and cerebellum (PubMed:16121183). Isoform 1 is widely expressed (PubMed:12215525). Isoform 1 is expressed in brain, liver, skeletal muscle and testis (PubMed:10655230). Isoform 3 is expressed in lung, brain, testis, prostate and choroid plexus (PubMed:12215525). Isoform 4 is expressed in muscle, lung, kidney, brain, testis and prostate (PubMed:10655230, PubMed:12215525). {ECO:0000269|PubMed:10504407, ECO:0000269|PubMed:10655230, ECO:0000269|PubMed:12215525, ECO:0000269|PubMed:16121183}. +Q920C1 CRDL1_MOUSE Chordin-like protein 1 (Neuralin-1) (Neurogenesin-1) (Ventroptin) 447 50,732 Alternative sequence (2); Chain (1); Domain (3); Glycosylation (2); Motif (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Seems to antagonize the function of BMP4 by binding to it and preventing its interaction with receptors. Alters the fate commitment of neural stem cells from gliogenesis to neurogenesis. Contributes to neuronal differentiation of neural stem cells in the brain by preventing the adoption of a glial fate. May play a crucial role in dorsoventral axis formation (By similarity). Antagonizes the function of BMP7 and may thus play an important role in the embryonic bone formation. Shows no inhibitory effect on the inducing activity of BMP2. Plays a role during anterior segment eye development (By similarity). {ECO:0000250, ECO:0000269|PubMed:16630536}. PTM: May be glycosylated. {ECO:0000269|PubMed:16630536}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Expressed in heart, brain, lung, liver, kidney and testis. +Q8K1L0 CREB5_MOUSE Cyclic AMP-responsive element-binding protein 5 (CREB-5) (cAMP-responsive element-binding protein 5) (CRE-BPa) 357 39,955 Alternative sequence (3); Chain (1); Compositional bias (2); Domain (1); Erroneous initiation (1); Region (2); Sequence conflict (1) FUNCTION: Binds to the cAMP response element and activates transcription. {ECO:0000250|UniProtKB:Q02930}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Binds DNA as a homodimer or as a heterodimer with JUN or ATF2/CREBP1. {ECO:0000250}. +P35347 CRFR1_MOUSE Corticotropin-releasing factor receptor 1 (CRF-R-1) (CRF-R1) (CRFR-1) (Corticotropin-releasing hormone receptor 1) (CRH-R-1) (CRH-R1) 415 47,769 Chain (1); Disulfide bond (4); Glycosylation (5); Modified residue (1); Region (2); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 112 142 Helical; Name=1. {ECO:0000250}.; TRANSMEM 150 174 Helical; Name=2. {ECO:0000250}.; TRANSMEM 190 218 Helical; Name=3. {ECO:0000250}.; TRANSMEM 226 253 Helical; Name=4. {ECO:0000250}.; TRANSMEM 270 295 Helical; Name=5. {ECO:0000250}.; TRANSMEM 307 331 Helical; Name=6. {ECO:0000250}.; TRANSMEM 339 368 Helical; Name=7. {ECO:0000250}. TOPO_DOM 24 111 Extracellular. {ECO:0000250}.; TOPO_DOM 143 149 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 175 189 Extracellular. {ECO:0000250}.; TOPO_DOM 219 225 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 254 269 Extracellular. {ECO:0000250}.; TOPO_DOM 296 306 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 332 338 Extracellular. {ECO:0000250}.; TOPO_DOM 369 415 Cytoplasmic. {ECO:0000250}. FUNCTION: G-protein coupled receptor for CRH (corticotropin-releasing factor) and UCN (urocortin). Has high affinity for CRH and UCN. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and down-stream effectors, such as adenylate cyclase. Promotes the activation of adenylate cyclase, leading to increased intracellular cAMP levels. Inhibits the activity of the calcium channel CACNA1H. Required for normal embryonic development of the adrenal gland and for normal hormonal responses to stress. Plays a role in the response to anxiogenic stimuli. {ECO:0000269|PubMed:8243652, ECO:0000269|PubMed:9655498}. PTM: C-terminal Ser or Thr residues may be phosphorylated.; PTM: Phosphorylation at Ser-301 by PKA prevents maximal coupling to Gq-protein, and thereby negatively regulates downstream signaling. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8243652}; Multi-pass membrane protein {ECO:0000269|PubMed:8243652}. Endosome {ECO:0000250}. Note=Agonist-binding promotes endocytosis. {ECO:0000250}. SUBUNIT: Heterodimer; heterodimerizes with GPER1 (By similarity). Interacts (via N-terminal extracellular domain) with CRH and UCN. Interacts with DLG1; this inhibits endocytosis of CRHR1 after agonist binding. {ECO:0000250, ECO:0000269|PubMed:23576434}. DOMAIN: The transmembrane domain is composed of seven transmembrane helices that are arranged in V-shape. Transmembrane helix 7 assumes a sharply kinked structure (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Detected in brain cortex (at protein level). {ECO:0000269|PubMed:23576434}. +Q60748 CRFR2_MOUSE Corticotropin-releasing factor receptor 2 (CRF-R-2) (CRF-R2) (CRFR-2) (CRF-RB) (Corticotropin-releasing hormone receptor 2) (CRH-R-2) (CRH-R2) 411 47,623 Alternative sequence (1); Beta strand (5); Chain (1); Disulfide bond (4); Glycosylation (5); Mutagenesis (1); Sequence conflict (5); Signal peptide (1); Topological domain (8); Transmembrane (7); Turn (1) TRANSMEM 109 139 Helical; Name=1. {ECO:0000250}.; TRANSMEM 147 171 Helical; Name=2. {ECO:0000250}.; TRANSMEM 186 214 Helical; Name=3. {ECO:0000250}.; TRANSMEM 222 249 Helical; Name=4. {ECO:0000250}.; TRANSMEM 266 291 Helical; Name=5. {ECO:0000250}.; TRANSMEM 303 327 Helical; Name=6. {ECO:0000250}.; TRANSMEM 335 364 Helical; Name=7. {ECO:0000250}. TOPO_DOM 1 108 Extracellular. {ECO:0000250}.; TOPO_DOM 140 146 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 172 185 Extracellular. {ECO:0000250}.; TOPO_DOM 215 221 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 250 265 Extracellular. {ECO:0000250}.; TOPO_DOM 292 302 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 328 334 Extracellular. {ECO:0000250}.; TOPO_DOM 365 411 Cytoplasmic. {ECO:0000250}. FUNCTION: G-protein coupled receptor for CRH (corticotropin-releasing factor), UCN (urocortin), UCN2 and UCN3. Has high affinity for UCN. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and down-stream effectors, such as adenylate cyclase. Promotes the activation of adenylate cyclase, leading to increased intracellular cAMP levels. PTM: A N-glycosylation site within the signal peptide impedes its proper cleavage and function. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBUNIT: Monomer. Interacts with CRF, UCN, UCN2 and UCN3 (By similarity). {ECO:0000250}. DOMAIN: The transmembrane domain is composed of seven transmembrane helices that are arranged in V-shape. Transmembrane helix 7 assumes a sharply kinked structure (By similarity). {ECO:0000250}.; DOMAIN: The uncleaved pseudo signal peptide prevents receptor's oligomerization and coupling to G(i) subunits. It is also responsible for the rather low receptor localization at the plasma membrane (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in the heart. Also expressed in lungs, skeletal muscle, gastrointestinal tract, epididymis, and brain. +O54917 E2F6_MOUSE Transcription factor E2F6 (E2F-6) (E2F-binding site-modulating activity protein) (EMA) 272 30,852 Chain (1); DNA binding (1); Motif (1); Region (4); Sequence conflict (1) FUNCTION: Inhibitor of E2F-dependent transcription. Binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3'. Has a preference for the 5'-TTTCCCGC-3' E2F recognition site. E2F6 lacks the transcriptional activation and pocket protein binding domains. Appears to regulate a subset of E2F-dependent genes whose products are required for entry into the cell cycle but not for normal cell cycle progression. May silence expression via the recruitment of a chromatin remodeling complex containing histone H3-K9 methyltransferase activity. Overexpression delays the exit of cells from the S-phase (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Component of the DRTF1/E2F transcription factor complex. Forms heterodimers with DP family members. Part of the E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1, RING1, RNF2, MBLR, L3MBTL2 and YAF2. Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10 (By similarity). {ECO:0000250}. +Q9CXV3 CRGF_MOUSE Gamma-crystallin F (Gamma-F-crystallin) 174 21,249 Chain (1); Domain (4); Region (1); Sequence conflict (4) FUNCTION: Crystallins are the dominant structural components of the vertebrate eye lens. DOMAIN: Has a two-domain beta-structure, folded into four very similar Greek key motifs. +Q60571 CRHBP_MOUSE Corticotropin-releasing factor-binding protein (CRF-BP) (CRF-binding protein) (Corticotropin-releasing hormone-binding protein) (CRH-BP) 322 36,048 Chain (1); Disulfide bond (5); Glycosylation (1); Signal peptide (1) FUNCTION: Binds CRF and inactivates it. May prevent inappropriate pituitary-adrenal stimulation in pregnancy. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +Q58FA4 E2F8_MOUSE Transcription factor E2F8 (E2F-8) 860 93,276 Chain (1); DNA binding (2); Modified residue (4); Mutagenesis (2); Sequence conflict (4) FUNCTION: Atypical E2F transcription factor that participates in various processes such as angiogenesis and polyploidization of specialized cells. Mainly acts as a transcription repressor that binds DNA independently of DP proteins and specifically recognizes the E2 recognition site 5'-TTTC[CG]CGC-3'. Directly represses transcription of classical E2F transcription factors such as E2F1: component of a feedback loop in S phase by repressing the expression of E2F1, thereby preventing p53/TP53-dependent apoptosis. Plays a key role in polyploidization of cells in placenta and liver by regulating the endocycle, probably by repressing genes promoting cytokinesis and antagonizing action of classical E2F proteins (E2F1, E2F2 and/or E2F3). Required for placental development by promoting polyploidization of trophoblast giant cells. Acts as a promoter of sprouting angiogenesis, possibly by acting as a transcription activator: associates with HIF1A, recognizes and binds the VEGFA promoter, which is different from canonical E2 recognition site, and activates expression of the VEGFA gene. {ECO:0000269|PubMed:18194653, ECO:0000269|PubMed:22516201, ECO:0000269|PubMed:22903062, ECO:0000269|PubMed:23064264, ECO:0000269|PubMed:23064266}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15722552}. SUBUNIT: Interacts with HIF1A (By similarity). Homodimer and heterodimer: mainly forms homodimers and, to a lesser extent, heterodimers with E2F8. Dimerization is important for DNA-binding. {ECO:0000250}. DOMAIN: In contrast to classical members of the E2F transcription factor, atypical members contain 2 DNA-binding domains and regulate transcription in a DP-independent manner. Both DNA-binding domains are required for DNA-binding and are proposed to form an intramolecular structure that is similar to the winged helix structure of the E2F-DP heterodimer (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in liver, skin, thymus and testis. Expressed in trophoblast giant cells throughout placenta development (at protein level). {ECO:0000269|PubMed:15722552, ECO:0000269|PubMed:22516201, ECO:0000269|PubMed:23064266}. +Q9JLL0 CRIM1_MOUSE Cysteine-rich motor neuron 1 protein (CRIM-1) 1037 114,066 Chain (1); Domain (11); Glycosylation (1); Modified residue (1); Motif (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 941 961 Helical. {ECO:0000255}. TOPO_DOM 35 940 Extracellular. {ECO:0000255}.; TOPO_DOM 962 1037 Cytoplasmic. {ECO:0000255}. FUNCTION: May play a role in CNS development by interacting with growth factors implicated in motor neuron differentiation and survival. May play a role in capillary formation and maintenance during angiogenesis. Modulates BMP activity by affecting its processing and delivery to the cell surface (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Interacts with BMP4 and BMP7. {ECO:0000250}. TISSUE SPECIFICITY: Expressed during embryonic development in brain, kidney, spinal chord, testis, lens, vibrissae, pinna, tooth primordia and in specific regions of the CNS. Expressed in adult lens. Displays male-specific expression in the fetal gonads with the strongest expression in the Sertoli cells of developing testis. {ECO:0000269|PubMed:10642437, ECO:0000269|PubMed:10842084, ECO:0000269|PubMed:11084657}. +O70333 CRIPT_MOUSE Cysteine-rich PDZ-binding protein (Cysteine-rich interactor of PDZ three) (Cysteine-rich interactor of PDZ3) 101 11,271 Chain (1); Region (2); Sequence conflict (1) FUNCTION: Involved in the cytoskeletal anchoring of DLG4 in excitatory synapses. {ECO:0000250|UniProtKB:Q792Q4}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell junction, synapse {ECO:0000250}. Cell projection, dendritic spine {ECO:0000250}. Note=Colocalizes with DLG4 in asymmetric synapses. {ECO:0000250}. SUBUNIT: Interacts with TUBB1. Interacts strongly with the PDZ3 domain of members of the DLG4 family. Associates with microtubules (By similarity). Interacts with DLG4. {ECO:0000250, ECO:0000269|PubMed:17474715}. +Q8BZQ2 CRLD2_MOUSE Cysteine-rich secretory protein LCCL domain-containing 2 (Coffeecrisp) 495 55,432 Alternative sequence (1); Chain (1); Disulfide bond (4); Domain (3); Glycosylation (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Promotes matrix assembly. {ECO:0000269|PubMed:18757743}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18757743}. SUBUNIT: Binds to heparin, dermatan sulfate and chondroitin sulfate. {ECO:0000269|PubMed:18757743}. TISSUE SPECIFICITY: Present in kidney renal tubules (at protein level). {ECO:0000269|PubMed:18757743}. +Q9Z2L7 CRLF3_MOUSE Cytokine receptor-like factor 3 (Cytokine receptor-like molecule 9) (CREME-9) (Cytokine receptor-related factor 4) 442 49,559 Alternative sequence (2); Chain (1); Coiled coil (1); Domain (1); Erroneous gene model prediction (1) FUNCTION: May play a role in the negative regulation of cell cycle progression. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +Q6PG95 CRML_MOUSE Protein cramped-like (Cramped chromatin regulator homolog 1) (Hematological and neurological expressed 1-like protein) 1285 137,121 Chain (1); Compositional bias (1); Domain (1); Frameshift (1); Modified residue (2); Sequence conflict (3) SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00624}. +Q9WV92 E41L3_MOUSE Band 4.1-like protein 3 (4.1B) (Differentially expressed in adenocarcinoma of the lung protein 1) (DAL-1) (DAL1P) (mDAL-1) [Cleaved into: Band 4.1-like protein 3, N-terminally processed] 929 103,338 Alternative sequence (6); Chain (2); Domain (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (20); Region (3); Sequence conflict (4) FUNCTION: Tumor suppressor that inhibits cell proliferation and promotes apoptosis. Modulates the activity of protein arginine N-methyltransferases, including PRMT3 and PRMT5 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:10652311}; Peripheral membrane protein {ECO:0000269|PubMed:10652311}; Cytoplasmic side {ECO:0000269|PubMed:10652311}. Cytoplasm {ECO:0000250}. Cell junction {ECO:0000269|PubMed:10652311}. Note=Detected in the cytoplasm of actively dividing cells. SUBUNIT: Interacts (via FERM domain) with CADM1. Interacts with PRMT3, PRMT5 and PRMT6 (By similarity). Isoform 2 (heart-specific) has the complete spectrin--actin-binding (SAB) domain and fully interacts with spectrin and actin. {ECO:0000250, ECO:0000269|PubMed:10652311}. TISSUE SPECIFICITY: Detected in brain (at protein level). Highest expression in brain, lower in testis, adrenal gland, heart and kidney. Also present in muscle and epithelial cells. Isoform 1 is expressed in brain, isoform 2 is expressed in heart and isoform 3 is mostly expressed in kidney but also in heart and brain. Isoform 6 seems to be most abundant in kidney while isoform 4 and isoform 5 are predominantly expressed in heart and brain. {ECO:0000269|PubMed:10652311}. +Q8BGS1 E41L5_MOUSE Band 4.1-like protein 5 731 81,636 Alternative sequence (3); Chain (1); Domain (1); Erroneous initiation (1); Modified residue (1); Sequence conflict (2) FUNCTION: May contribute to the correct positioning of tight junctions during the establishment of polarity in epithelial cells. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17920587}. Cell junction, adherens junction {ECO:0000269|PubMed:17920587}. Note=Associated with the plasma membrane. During embryonic development, tends to be associated with the basolateral side of the plasma membrane in various tissues. In the adult kidney, found at the basolateral and apical sides of the tubules. In the adult retina, colocalizes with CTNNB1, an adherens junction marker. SUBUNIT: Interacts with MPP5, CRB2 and CRB3. {ECO:0000250}. DOMAIN: The FERM domain binds to CRB1. {ECO:0000250}. TISSUE SPECIFICITY: In the retina, expressed at the region of the outer limiting membrane, as well as in the retinal pigment epithelium, outer nuclear and outer plexiform layers. Also detected in the inner segments (at protein level). Expressed in the kidney (at protein level). {ECO:0000269|PubMed:17920587}. +Q64010 CRK_MOUSE Adapter molecule crk (Proto-oncogene c-Crk) (p38) 304 33,815 Alternative sequence (1); Beta strand (20); Chain (1); Domain (3); Helix (4); Initiator methionine (1); Modified residue (9); Site (1) FUNCTION: Isoform Crk-II: Regulates cell adhesion, spreading and migration. Mediates attachment-induced MAPK8 activation, membrane ruffling and cell motility in a Rac-dependent manner. Involved in phagocytosis of apoptotic cells and cell motility via its interaction with DOCK1 and DOCK4. May regulate the EFNA5-EPHA3 signaling. {ECO:0000250|UniProtKB:P46108}. PTM: Isoform Crk-II is phosphorylated by KIT. Phosphorylated on Tyr-221 upon cell adhesion. Results in the negative regulation of the association with SH2- and SH3-binding partners, possibly by the formation of an intramolecular interaction of phosphorylated Tyr-221 with the SH2 domain. This leads finally to the down-regulation of the Crk signaling pathway. {ECO:0000269|PubMed:12878163, ECO:0000269|PubMed:8194526}.; PTM: Proline isomerization at Pro-237 by PPIA acts as a switch between two conformations: an autoinhibitory conformation in the cis form, where the tandem SH3 domains interact intramolecularly, and an activated conformation in the trans form. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Translocated to the plasma membrane upon cell adhesion. {ECO:0000250}. SUBUNIT: Interacts with ABL1, C3G, DOCK3, DOCK5, MAP4K1, MAPK8 and SOS via its first SH3 domain. Interacts (via SH2 domain) with BCAR1, CBL, CBLB, PXN, IRS4 and GAB1 upon stimulus-induced tyrosine phosphorylation. Interacts (via SH2 domain) with several tyrosine-phosphorylated growth factor receptors such as EGFR and INSR. Interacts with FLT1 (tyrosine-phosphorylated). Interacts with DOCK1 and DOCK4. Interacts with SHB. Interacts with PEAK1. Interacts with FASLG. Isoform Crk-II interacts with KIT. Interacts with EPHA3; upon activation of EPHA3 by the ligand EFNA5 and EPHA3 tyrosine kinase activity-dependent. Interacts with EPHA3 (phosphorylated); mediates EFNA5-EPHA3 signaling through RHOA GTPase activation. Interacts with FLT4 (tyrosine-phosphorylated). Isoform Crk-II (via SH2 domain) interacts with PDGFRA (tyrosine phosphorylated) and PDGFRB (tyrosine phosphorylated). Part of a collagen stimulated complex involved in cell migration composed of CDC42, CRK, TNK2 and p130cas/BCAR1. Interacts (via SH2 domain) with the 'Tyr-9' phosphorylated form of PDPK1. Interacts with CBLC. Found in a complex with ABL1, ABL2, CRK and UNC119; leading to the inhibition of CRK phosphorylation by ABL kinases (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P46108}. DOMAIN: The C-terminal SH3 domain function as a negative modulator for transformation and the N-terminal SH3 domain appears to function as a positive regulator for transformation. {ECO:0000250}.; DOMAIN: The SH2 domain mediates interaction with tyrosine phosphorylated proteins. Mediates interaction with SHB. TISSUE SPECIFICITY: Ubiquitous. +Q8CGD2 CRLD1_MOUSE Cysteine-rich secretory protein LCCL domain-containing 1 (CocoaCrisp) 500 56,918 Chain (1); Disulfide bond (4); Domain (3); Frameshift (1); Sequence conflict (7); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q68ED7 CRTC1_MOUSE CREB-regulated transcription coactivator 1 (Mucoepidermoid carcinoma translocated protein 1 homolog) (Transducer of regulated cAMP response element-binding protein 1) (TORC-1) (Transducer of CREB protein 1) 630 66,945 Chain (1); Compositional bias (1); Erroneous initiation (1); Modified residue (5); Motif (1); Mutagenesis (3); Site (1) FUNCTION: Transcriptional coactivator for CREB1 which activates transcription through both consensus and variant cAMP response element (CRE) sites (PubMed:29211348). Acts as a coactivator, in the SIK/TORC signaling pathway, being active when dephosphorylated (PubMed:29211348). Acts independently of CREB1 'Ser-133' phosphorylation. Enhances the interaction of CREB1 with TAF4. Regulates the expression of specific CREB-activated genes such as the steroidogenic gene, StAR. Potent coactivator of PGC1alpha and inducer of mitochondrial biogenesis in muscle cells (By similarity). In the hippocampus, involved in late-phase long-term potentiation (L-LTP) maintenance at the Schaffer collateral-CA1 synapses. May be required for dendritic growth of developing cortical neurons. In concert with SIK1, regulates the light-induced entrainment of the circadian clock. In response to light stimulus, coactivates the CREB-mediated transcription of PER1 which plays an important role in the photic entrainment of the circadian clock. {ECO:0000250|UniProtKB:Q157S1, ECO:0000250|UniProtKB:Q6UUV9, ECO:0000269|PubMed:17360587, ECO:0000269|PubMed:23699513, ECO:0000269|PubMed:23993098, ECO:0000269|PubMed:29211348}. PTM: Phosphorylation/dephosphorylation states of Ser-151 are required for regulating transduction of CREB activity. TORCs are inactive when phosphorylated, and active when dephosphorylated at this site. This primary site of phosphorylation is mediated by SIKs (SIK1 and SIK2), is regulated by cAMP and calcium levels and is dependent on the phosphorylation of SIKs by LKB1. {ECO:0000269|PubMed:23993098}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17360587, ECO:0000269|PubMed:23993098}. Nucleus {ECO:0000269|PubMed:17360587, ECO:0000269|PubMed:23699513, ECO:0000269|PubMed:23993098}. Note=Cytoplasmic when phosphorylated by SIK or AMPK and when sequestered by 14-3-3 proteins (By similarity). Translocated to the nucleus on Ser-151 dephosphorylation, instigated by a number of factors including calcium ion and cAMP levels (By similarity). Light stimulation triggers a nuclear accumulation in the suprachiasmatic nucleus (SCN) of the brain (PubMed:23699513). {ECO:0000250|UniProtKB:Q6UUV9, ECO:0000269|PubMed:23699513}. SUBUNIT: Binds, as a tetramer, through its N-terminal region, with the bZIP domain of CREB1 (By similarity). 'Arg-314' in the bZIP domain of CREB1 is essential for this interaction (By similarity). Interaction, via its C-terminal, with TAF4, enhances recruitment of TAF4 to CREB1 (By similarity). Interacts with 14-3-3 proteins (PubMed:28235073). {ECO:0000250|UniProtKB:Q6UUV9, ECO:0000269|PubMed:28235073}. TISSUE SPECIFICITY: Highly expressed in specific regions of the brain including the cortex, hippocampus and striatum. {ECO:0000269|PubMed:17360587}. +Q91X84 CRTC3_MOUSE CREB-regulated transcription coactivator 3 (Transducer of regulated cAMP response element-binding protein 3) (TORC-3) (Transducer of CREB protein 3) 619 67,027 Alternative sequence (1); Chain (1); Cross-link (1); Modified residue (12); Mutagenesis (2) FUNCTION: Transcriptional coactivator for CREB1 which activates transcription through both consensus and variant cAMP response element (CRE) sites (PubMed:29211348). Acts as a coactivator, in the SIK/TORC signaling pathway, being active when dephosphorylated (PubMed:29211348). Acts independently of CREB1 'Ser-133' phosphorylation (By similarity). Enhances the interaction of CREB1 with TAF4 (By similarity). Regulates the expression of specific CREB-activated genes such as the steroidogenic gene, StAR (By similarity). Potent coactivator of PPARGC1A and inducer of mitochondrial biogenesis in muscle cells (By similarity). {ECO:0000250|UniProtKB:Q6UUV7, ECO:0000269|PubMed:29211348}. PTM: Phosphorylation/dephosphorylation states of Ser-273 are required for regulating transduction of CREB activity (PubMed:29211348). TORCs are inactive when phosphorylated, and active when dephosphorylated at this site (PubMed:29211348). {ECO:0000269|PubMed:29211348}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6UUV7}. Cytoplasm {ECO:0000250|UniProtKB:Q6UUV7}. Note=Appears to be mainly nuclear. {ECO:0000250|UniProtKB:Q6UUV7}. SUBUNIT: Binding, as a tetramer, through its N-terminal region, with the bZIP domain of CREB1 enhances recruitment of TAF4 to the promoter (By similarity). 'Arg-314' in the bZIP domain of CREB1 is essential for this interaction (By similarity). Interacts with 14-3-3 proteins (PubMed:28235073). {ECO:0000250|UniProtKB:Q6UUV7, ECO:0000269|PubMed:28235073}. +Q8WUR0 CS012_MOUSE Protein C19orf12 homolog 141 15,087 Chain (1); Erroneous initiation (1); Sequence conflict (11); Transmembrane (1) TRANSMEM 33 53 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9NSK7}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q9NSK7}; Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9NSK7}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9NSK7}. Note=In response to oxidative stress, relocates to the cytosol forming aggregates that partially co-localize with mitochondria. {ECO:0000250|UniProtKB:Q9NSK7}. +P24622 CRYAA_MOUSE Alpha-crystallin A chain 196 22,489 Alternative sequence (1); Chain (1); Domain (1); Glycosylation (1); Metal binding (5); Modified residue (11) FUNCTION: Contributes to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions (By similarity). {ECO:0000250}. PTM: Acetylation at Lys-93 seems to increase chaperone activity. {ECO:0000250}.; PTM: Undergoes age-dependent proteolytical cleavage at the C-terminus. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles. {ECO:0000250}. SUBUNIT: Heteropolymer composed of three CRYAA and one CRYAB subunits. Inter-subunit bridging via zinc ions enhances stability, which is crucial as there is no protein turn over in the lens. Can also form homodimers and higher homooligomers (By similarity). {ECO:0000250}. +Q99KP3 CRYL1_MOUSE Lambda-crystallin homolog (EC 1.1.1.45) (L-gulonate 3-dehydrogenase) (Gul3DH) 319 35,209 Binding site (3); Chain (1); Frameshift (1); Initiator methionine (1); Modified residue (2); Nucleotide binding (1) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed, with highest levels in liver. Undetectable in skeletal muscle. {ECO:0000269|PubMed:12527201}. +Q9DBE0 CSAD_MOUSE Cysteine sulfinic acid decarboxylase (EC 4.1.1.29) (Aspartate 1-decarboxylase) (EC 4.1.1.11) (Cysteine-sulfinate decarboxylase) (Sulfinoalanine decarboxylase) 493 55,145 Chain (1); Modified residue (1); Sequence conflict (1) Organosulfur biosynthesis; taurine biosynthesis; hypotaurine from L-cysteine: step 2/2. FUNCTION: Catalyzes the decarboxylation of L-aspartate, 3-sulfino-L-alanine (cysteine sulfinic acid), and L-cysteate to beta-alanine, hypotaurine and taurine, respectively. The preferred substrate is 3-sulfino-L-alanine. Does not exhibit any decarboxylation activity toward glutamate. {ECO:0000269|PubMed:26327310}. SUBUNIT: Homodimer. {ECO:0000269|PubMed:26327310}. TISSUE SPECIFICITY: Expressed in kidney and liver not detected in lymphoid tissues and lung. Expressed in kidney, liver and brain. 7 and 4 times higher expression in kidney and liver than in brain, respectively. Low level of detection in skeletal muscle. Expressed in brain, olfactory bulb, liver, skeletal muscle and kidney with the highest expression in liver and lowest in skeletal muscle (at protein level) (PubMed:26327310). {ECO:0000269|PubMed:11997111, ECO:0000269|PubMed:26327310}. +Q91YT8 CSCL1_MOUSE CSC1-like protein 1 (Transmembrane protein 63A) 804 91,860 Chain (1); Erroneous initiation (1); Erroneous termination (1); Modified residue (1); Transmembrane (10) TRANSMEM 50 70 Helical. {ECO:0000255}.; TRANSMEM 145 165 Helical. {ECO:0000255}.; TRANSMEM 191 211 Helical. {ECO:0000255}.; TRANSMEM 421 441 Helical. {ECO:0000255}.; TRANSMEM 461 481 Helical. {ECO:0000255}.; TRANSMEM 507 527 Helical. {ECO:0000255}.; TRANSMEM 552 572 Helical. {ECO:0000255}.; TRANSMEM 619 639 Helical. {ECO:0000255}.; TRANSMEM 664 684 Helical. {ECO:0000255}.; TRANSMEM 697 717 Helical. {ECO:0000255}. FUNCTION: Acts as an osmosensitive calcium-permeable cation channel. {ECO:0000250}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q3TWI9 CSCL2_MOUSE CSC1-like protein 2 (Transmembrane protein 63B) 832 94,775 Chain (1); Erroneous initiation (2); Modified residue (4); Sequence conflict (2); Transmembrane (10) TRANSMEM 41 61 Helical. {ECO:0000255}.; TRANSMEM 158 178 Helical. {ECO:0000255}.; TRANSMEM 203 223 Helical. {ECO:0000255}.; TRANSMEM 435 455 Helical. {ECO:0000255}.; TRANSMEM 481 501 Helical. {ECO:0000255}.; TRANSMEM 521 541 Helical. {ECO:0000255}.; TRANSMEM 560 580 Helical. {ECO:0000255}.; TRANSMEM 630 650 Helical. {ECO:0000255}.; TRANSMEM 678 698 Helical. {ECO:0000255}.; TRANSMEM 711 731 Helical. {ECO:0000255}. FUNCTION: Acts as an osmosensitive calcium-permeable cation channel. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +P51906 EAA3_MOUSE Excitatory amino acid transporter 3 (Excitatory amino-acid carrier 1) (Sodium-dependent glutamate/aspartate transporter 3) (Solute carrier family 1 member 1) 523 56,694 Binding site (3); Chain (1); Glycosylation (3); Intramembrane (2); Metal binding (5); Modified residue (2); Region (2); Sequence conflict (2); Topological domain (11); Transmembrane (8) INTRAMEM 313 343 Discontinuously helical. {ECO:0000250|UniProtKB:P43003}.; INTRAMEM 393 426 Discontinuously helical. {ECO:0000250|UniProtKB:P43003}. TRANSMEM 19 38 Helical. {ECO:0000255}.; TRANSMEM 62 82 Helical. {ECO:0000255}.; TRANSMEM 94 114 Helical. {ECO:0000255}.; TRANSMEM 205 228 Helical; Name=4. {ECO:0000250|UniProtKB:P43003}.; TRANSMEM 238 265 Helical; Name=5. {ECO:0000250|UniProtKB:P43003}.; TRANSMEM 286 307 Helical; Name=6. {ECO:0000250|UniProtKB:P43003}.; TRANSMEM 353 379 Helical; Name=7. {ECO:0000250|UniProtKB:P43003}.; TRANSMEM 440 461 Helical; Name=8. {ECO:0000250|UniProtKB:P43003}. TOPO_DOM 1 18 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 39 61 Extracellular. {ECO:0000305}.; TOPO_DOM 83 93 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 115 204 Extracellular. {ECO:0000305}.; TOPO_DOM 229 237 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 266 285 Extracellular. {ECO:0000305}.; TOPO_DOM 308 312 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 344 352 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 380 392 Extracellular. {ECO:0000305}.; TOPO_DOM 427 439 Extracellular. {ECO:0000305}.; TOPO_DOM 462 523 Cytoplasmic. {ECO:0000305}. FUNCTION: Sodium-dependent, high-affinity amino acid transporter that mediates the uptake of L-glutamate and also L-aspartate and D-aspartate (PubMed:12119102, PubMed:18684713). Can also transport L-cysteine. Functions as a symporter that transports one amino acid molecule together with two or three Na(+) ions and one proton, in parallel with the counter-transport of one K(+) ion. Mediates Cl(-) flux that is not coupled to amino acid transport; this avoids the accumulation of negative charges due to aspartate and Na(+) symport (By similarity). Plays an important role in L-glutamate and L-aspartate reabsorption in renal tubuli (PubMed:9233792). Plays a redundant role in the rapid removal of released glutamate from the synaptic cleft, which is essential for terminating the postsynaptic action of glutamate (PubMed:9233792). Negatively regulated by ARL6IP5 (PubMed:12119102). {ECO:0000250|UniProtKB:P43005, ECO:0000269|PubMed:12119102, ECO:0000269|PubMed:18684713, ECO:0000269|PubMed:9233792}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12119102, ECO:0000269|PubMed:18684713, ECO:0000269|PubMed:9233792}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P43003}. Apical cell membrane {ECO:0000250|UniProtKB:P43005}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P43003}. SUBUNIT: Homotrimer (Probable). Interacts with ARL6IP5 (PubMed:12119102, PubMed:18684713). {ECO:0000269|PubMed:12119102, ECO:0000269|PubMed:18684713, ECO:0000305}. DOMAIN: Contains eight transmembrane regions plus two helical hairpins that dip into the membrane. These helical hairpin structures play an important role in the transport process. The first enters the membrane from the cytoplasmic side, the second one from the extracellular side. During the transport cycle, the regions involved in amino acid transport, and especially the helical hairpins, move vertically by about 15-18 Angstroms, alternating between exposure to the aqueous phase and reinsertion in the lipid bilayer. In contrast, the regions involved in trimerization do not move. {ECO:0000250|UniProtKB:P43003}. TISSUE SPECIFICITY: Expressed in whole brain, brain cortex, hippocampus, cerebellum, lung, kidney, small intestine and skeletal muscle. {ECO:0000269|PubMed:7766664, ECO:0000269|PubMed:9233792}. +Q8JZR4 EAA5_MOUSE Excitatory amino acid transporter 5 (Solute carrier family 1 member 7) 559 60,106 Chain (1); Erroneous initiation (1); Glycosylation (2); Topological domain (2); Transmembrane (10) TRANSMEM 17 37 Helical. {ECO:0000255}.; TRANSMEM 60 80 Helical. {ECO:0000255}.; TRANSMEM 94 114 Helical. {ECO:0000255}.; TRANSMEM 216 236 Helical. {ECO:0000255}.; TRANSMEM 259 279 Helical. {ECO:0000255}.; TRANSMEM 298 318 Helical. {ECO:0000255}.; TRANSMEM 329 349 Helical. {ECO:0000255}.; TRANSMEM 371 391 Helical. {ECO:0000255}.; TRANSMEM 413 433 Helical. {ECO:0000255}.; TRANSMEM 456 476 Helical. {ECO:0000255}. TOPO_DOM 1 16 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 115 215 Extracellular. {ECO:0000255}. FUNCTION: Transports L-glutamate; the L-glutamate uptake is sodium- and voltage-dependent and chloride-independent. Its associated chloride conductance may participate in visual processing (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with the PDZ domains of DLG4. {ECO:0000250}. +Q80T79 CSMD3_MOUSE CUB and sushi domain-containing protein 3 (CUB and sushi multiple domains protein 3) 3707 405,762 Alternative sequence (5); Chain (1); Disulfide bond (70); Domain (42); Glycosylation (18); Sequence conflict (2); Topological domain (3); Transmembrane (2) TRANSMEM 43 63 Helical. {ECO:0000255}.; TRANSMEM 3631 3651 Helical. {ECO:0000255}. TOPO_DOM 1 42 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 64 3630 Extracellular. {ECO:0000255}.; TOPO_DOM 3652 3707 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in dendrite development. {ECO:0000269|PubMed:27033969}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27033969}; Multi-pass membrane protein {ECO:0000305}. DOMAIN: The intracellular region is dispensable for its function. {ECO:0000269|PubMed:27033969}. TISSUE SPECIFICITY: Expressed in the apical dendrites of postnatal hippocampal neurons (at protein level). {ECO:0000269|PubMed:27033969}. +Q99LD4 CSN1_MOUSE COP9 signalosome complex subunit 1 (SGN1) (Signalosome subunit 1) (G protein pathway suppressor 1) (GPS-1) (JAB1-containing signalosome subunit 1) 471 53,442 Alternative sequence (1); Chain (1); Domain (1); Modified residue (4) FUNCTION: Essential component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. Suppresses G-protein- and mitogen-activated protein kinase-mediated signal transduction (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Component of the CSN complex, composed of COPS1/GPS1, COPS2, COPS3, COPS4, COPS5, COPS6, COPS7 (COPS7A or COPS7B), COPS8 and COPS9 (PubMed:9707402). In the complex, it probably interacts directly with COPS2, COPS3, COPS4 and COPS5 (By similarity). Interacts directly with inositol kinase ITPK1 (By similarity). Interacts with CAPN8 (PubMed:16476741). {ECO:0000250|UniProtKB:Q13098, ECO:0000269|PubMed:16476741, ECO:0000269|PubMed:9707402}. DOMAIN: The PCI domain is necessary and sufficient for the interactions with other CSN subunits of the complex (By similarity). Mediates the interaction with CAPN8. {ECO:0000250, ECO:0000269|PubMed:16476741}.; DOMAIN: The N-terminal part (1-196), which is not required for deneddylating activity and CSN complex formation, is nevertheless essential for other aspects of CSN complex function, such as repression of c-fos/FOS expression. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the base region of the oxyntic and pyloric mucosae. {ECO:0000269|PubMed:16476741}. +P61202 CSN2_MOUSE COP9 signalosome complex subunit 2 (SGN2) (Signalosome subunit 2) (Alien homolog) (JAB1-containing signalosome subunit 2) (Thyroid receptor-interacting protein 15) (TR-interacting protein 15) (TRIP-15) 443 51,597 Alternative sequence (1); Chain (1); Domain (1); Erroneous initiation (1); Region (1); Sequence conflict (3) FUNCTION: Essential component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. Involved in early stage of neuronal differentiation via its interaction with NIF3L1. {ECO:0000269|PubMed:11967155, ECO:0000269|PubMed:12522100, ECO:0000269|PubMed:12972599}. PTM: Phosphorylated by CK2 and PKD kinases. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10087198}. Nucleus {ECO:0000269|PubMed:10087198}. SUBUNIT: Component of the CSN complex, composed of COPS1/GPS1, COPS2, COPS3, COPS4, COPS5, COPS6, COPS7 (COPS7A or COPS7B), COPS8 and COPS9 (PubMed:9707402). In the complex, it probably interacts directly with COPS1, COPS4, COPS5, COPS6 and COPS7 (COPS7A or COPS7B) (PubMed:9707402). Specifically interacts with the ligand binding domain of the thyroid receptor (TR). Does not require the presence of thyroid hormone for its interaction. Interacts with CUL1 and CUL2 (PubMed:11967155). Interacts with IRF8/ICSBP1 and with nuclear receptors NR2F1 and NR0B1 (By similarity). Interacts with NIF3L1 (PubMed:12522100). {ECO:0000250|UniProtKB:P61201, ECO:0000269|PubMed:11967155, ECO:0000269|PubMed:12522100, ECO:0000269|PubMed:9707402}. TISSUE SPECIFICITY: Widely expressed in embryonic, fetal and adult tissues, except cartilage and smooth muscle. {ECO:0000269|PubMed:10087198}. +Q9CZ04 CSN7A_MOUSE COP9 signalosome complex subunit 7a (SGN7a) (Signalosome subunit 7a) (JAB1-containing signalosome subunit 7a) 275 30,224 Alternative sequence (1); Chain (1); Coiled coil (1); Domain (1); Frameshift (2); Initiator methionine (1); Modified residue (1); Sequence conflict (1) FUNCTION: Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, JUN, I-kappa-B-alpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively (By similarity). {ECO:0000250}. PTM: Phosphorylated by CK2 and PKD kinases. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Component of the CSN complex, composed of COPS1/GPS1, COPS2, COPS3, COPS4, COPS5, COPS6, COPS7 (COPS7A or COPS7B), COPS8 and COPS9 (PubMed:9707402). In the complex, it probably interacts directly with COPS1, COPS2, COPS4, COPS5, COPS6 and COPS8. Interacts with PMF1. Interacts with the translation initiation factor EIF3S6. Interacts with CK2 and PKD (By similarity). Interacts directly with ID3 (PubMed:15451666). {ECO:0000250|UniProtKB:Q9UBW8, ECO:0000269|PubMed:15451666, ECO:0000269|PubMed:9707402}. +Q8BV13 CSN7B_MOUSE COP9 signalosome complex subunit 7b (SGN7b) (Signalosome subunit 7b) (JAB1-containing signalosome subunit 7b) 264 29,689 Chain (1); Coiled coil (1); Domain (1); Initiator methionine (1); Modified residue (1); Sequence conflict (3) FUNCTION: Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, JUN, I-kappa-B-alpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Component of the CSN complex, composed of COPS1/GPS1, COPS2, COPS3, COPS4, COPS5, COPS6, COPS7 (COPS7A or COPS7B) and COPS8 and COPS9 (PubMed:9707402). In the complex, it probably interacts directly with COPS1, COPS2, COPS4, COPS5, COPS6 and COPS8. Interacts with EIF3S6 (By similarity). {ECO:0000250|UniProtKB:Q9H9Q2, ECO:0000269|PubMed:9707402}. +Q9D903 EBP2_MOUSE Probable rRNA-processing protein EBP2 306 34,703 Chain (1); Coiled coil (1); Cross-link (3); Modified residue (8) FUNCTION: Required for the processing of the 27S pre-rRNA. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. SUBUNIT: Interacts with WDR46. {ECO:0000250|UniProtKB:Q99848}. +Q8VBV7 CSN8_MOUSE COP9 signalosome complex subunit 8 (SGN8) (Signalosome subunit 8) (COP9 homolog) (JAB1-containing signalosome subunit 8) 209 23,256 Chain (1); Domain (1); Modified residue (1); Sequence conflict (3) FUNCTION: Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Component of the CSN complex, composed of COPS1/GPS1, COPS2, COPS3, COPS4, COPS5, COPS6, COPS7 (COPS7A or COPS7B), COPS8 and COPS9 (PubMed:9707402). In the complex, it probably interacts directly with COPS3, COPS4 and COPS7 (COPS7A or COPS7B) (By similarity). {ECO:0000250|UniProtKB:Q99627, ECO:0000269|PubMed:9707402}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:14636993}. +O88544 CSN4_MOUSE COP9 signalosome complex subunit 4 (SGN4) (Signalosome subunit 4) (JAB1-containing signalosome subunit 4) 406 46,285 Beta strand (3); Chain (1); Domain (1); Helix (3); Initiator methionine (1); Modified residue (2); Turn (1) FUNCTION: Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. Also involved in the deneddylation of non-cullin subunits such as STON2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1, IRF8/ICSBP and SNAPIN, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250}. SUBUNIT: Component of the CSN complex, composed of COPS1/GPS1, COPS2, COPS3, COPS4, COPS5, COPS6, COPS7 (COPS7A or COPS7B), COPS8 and COPS9 (PubMed:9707402). In the complex, it probably interacts directly with COPS1, COPS2, COPS3, COPS5, COPS6, COPS7 (COPS7A or COPS7B) and COPS8. Interacts with TOR1A; the interaction is direct and associates TOR1A and SNAPIN with the CSN complex. Interacts with STON2; controls STON2 neddylation levels (By similarity). {ECO:0000250|UniProtKB:Q9BT78, ECO:0000269|PubMed:9707402}. +Q4PZA2 ECE1_MOUSE Endothelin-converting enzyme 1 (ECE-1) (EC 3.4.24.71) 769 87,073 Active site (2); Alternative sequence (3); Chain (1); Disulfide bond (1); Glycosylation (10); Metal binding (3); Modified residue (1); Topological domain (2); Transmembrane (1) TRANSMEM 68 88 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 67 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 89 769 Extracellular. {ECO:0000255}. FUNCTION: Converts big endothelin-1 to endothelin-1. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. SUBUNIT: Homodimer; disulfide-linked (By similarity). Interacts with PPP1R16B (By similarity). {ECO:0000250|UniProtKB:P42891, ECO:0000250|UniProtKB:P42893}. +Q99388 CSPRS_MOUSE Component of Sp100-rs 208 24,061 Chain (1); Domain (1) +Q8CID0 CSR2B_MOUSE Cysteine-rich protein 2-binding protein (CSRP2-binding protein) (ADA2A-containing complex subunit 2) (ATAC2) (CRP2-binding partner) (CRP2BP) (Lysine acetyltransferase 14) 779 88,217 Chain (1); Domain (1); Modified residue (5); Sequence conflict (2) FUNCTION: Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4. May function as a scaffold for the ATAC complex to promote ATAC complex stability. Has also weak histone acetyltransferase activity toward histone H4. Required for the normal progression through G1 and G2/M phases of the cell cycle (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Mainly nuclear. {ECO:0000250}. SUBUNIT: Interacts with the LIM 1 domain of CSRP2. Component of the ADA2A-containing complex (ATAC), composed of CSRP2BP, KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1. In the complex, it probably interacts directly with KAT2A, MBIP and WDR5. {ECO:0000250}. +O35459 ECH1_MOUSE Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial (EC 5.3.3.-) 327 36,118 Binding site (1); Chain (1); Modified residue (5); Motif (1); Region (1); Site (2); Transit peptide (1) Lipid metabolism; fatty acid beta-oxidation. FUNCTION: Isomerization of 3-trans,5-cis-dienoyl-CoA to 2-trans,4-trans-dienoyl-CoA. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Peroxisome {ECO:0000250}. SUBUNIT: Homohexamer. {ECO:0000250}. +Q8BMS1 ECHA_MOUSE Trifunctional enzyme subunit alpha, mitochondrial (TP-alpha) [Includes: Long-chain enoyl-CoA hydratase (EC 4.2.1.17); Long chain 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.211)] 763 82,670 Chain (1); Modified residue (60); Sequence conflict (2); Site (2); Transit peptide (1) Lipid metabolism; fatty acid beta-oxidation. FUNCTION: Bifunctional subunit. PTM: Acetylation of Lys-569 and Lys-728 is observed in liver mitochondria from fasted mice but not from fed mice. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. SUBUNIT: Octamer of 4 alpha (HADHA) and 4 beta (HADHB) subunits. {ECO:0000250}. +Q3TLP5 ECHD2_MOUSE Enoyl-CoA hydratase domain-containing protein 2, mitochondrial 296 31,852 Alternative sequence (2); Chain (1); Erroneous initiation (1); Frameshift (2); Modified residue (2); Sequence conflict (12); Site (2); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}. +Q9D7J9 ECHD3_MOUSE Enoyl-CoA hydratase domain-containing protein 3, mitochondrial 300 32,402 Chain (1); Modified residue (1); Sequence conflict (2); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}. +Q8BH95 ECHM_MOUSE Enoyl-CoA hydratase, mitochondrial (EC 4.2.1.17) (Enoyl-CoA hydratase 1) (Short-chain enoyl-CoA hydratase) (SCEH) 290 31,474 Binding site (1); Chain (1); Modified residue (9); Region (1); Sequence conflict (2); Site (1); Transit peptide (1) Lipid metabolism; fatty acid beta-oxidation. FUNCTION: Straight-chain enoyl-CoA thioesters from C4 up to at least C16 are processed, although with decreasing catalytic rate (By similarity). Has high substrate specificity for crotonyl-CoA and moderate specificity for acryloyl-CoA, 3-methylcrotonyl-CoA and methacrylyl-CoA. It is noteworthy that binds tiglyl-CoA, but hydrates only a small amount of this substrate (By similarity). {ECO:0000250|UniProtKB:P30084}. PTM: Acetylation of Lys-101 is observed in liver mitochondria from fasted mice but not from fed mice. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. SUBUNIT: Homohexamer; dimer of trimers. {ECO:0000250}. +Q8BGQ2 CSRN2_MOUSE Cysteine/serine-rich nuclear protein 2 (CSRNP-2) (Protein FAM130A1) (TGF-beta-induced apoptosis protein 12) (TAIP-12) 534 58,504 Chain (1); Compositional bias (1); Modified residue (1) FUNCTION: Binds to the consensus sequence 5'-AGAGTG-3' and has transcriptional activator activity. May play a role in apoptosis. {ECO:0000269|PubMed:17726538}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17726538}. TISSUE SPECIFICITY: Highest expression detected in thymus, brain and ovary. Low levels detected in naive T-cells. {ECO:0000269|PubMed:17726538}. +Q9DBM2 ECHP_MOUSE Peroxisomal bifunctional enzyme (PBE) (PBFE) [Includes: Enoyl-CoA hydratase/3,2-trans-enoyl-CoA isomerase (EC 4.2.1.17) (EC 5.3.3.8); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35)] 718 78,301 Binding site (1); Chain (1); Modified residue (32); Motif (1); Region (2); Sequence conflict (1); Site (2) Lipid metabolism; fatty acid beta-oxidation. PTM: Acetylated, leading to enhanced enzyme activity. Acetylation is enhanced by up to 80% after treatment either with trichostin A (TCA) or with nicotinamide (NAM) with highest increase on Lys-344. Acetylation and enzyme activity increased by about 1.5% on addition of fatty acids (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. +P97315 CSRP1_MOUSE Cysteine and glycine-rich protein 1 (Cysteine-rich protein 1) (CRP) (CRP1) 193 20,583 Chain (1); Compositional bias (2); Cross-link (1); Domain (2); Modified residue (7); Motif (1) FUNCTION: Could play a role in neuronal development. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P21291}. SUBUNIT: Interacts with ASCC1; ASCC2 AND TRIP4. {ECO:0000250|UniProtKB:P21291}. +P50462 CSRP3_MOUSE Cysteine and glycine-rich protein 3 (Cysteine-rich protein 3) (CRP3) (LIM domain protein, cardiac) (Muscle LIM protein) 194 20,895 Chain (1); Compositional bias (2); Domain (2); Modified residue (3); Motif (1); Mutagenesis (1); Region (2) FUNCTION: Positive regulator of myogenesis. Acts as cofactor for myogenic bHLH transcription factors such as MYOD1, and probably MYOG and MYF6. Enhances the DNA-binding activity of the MYOD1:TCF3 isoform E47 complex and may promote formation of a functional MYOD1:TCF3 isoform E47:MEF2A complex involved in myogenesis (By similarity). Plays a crucial and specific role in the organization of cytosolic structures in cardiomyocytes. Could play a role in mechanical stretch sensing. May be a scaffold protein that promotes the assembly of interacting proteins at Z-line structures. It is essential for calcineurin anchorage to the Z line. Required for stress-induced calcineurin-NFAT activation (PubMed:9039266, PubMed:15665106). The role in regulation of cytoskeleton dynamics by association with CFL2 is reported conflictingly. Proposed to contribute to the maintenance of muscle cell integerity through an actin-based mechanism. Can directly bind to actin filaments, cross-link actin filaments into bundles without polarity selectivity and protect them from dilution- and cofilin-mediated depolymerization; the function seems to involve its self-association (By similarity). In vitro can inhibit PKC/PRKCA activity. Proposed to be involved in cardiac stress signaling by down-regulating excessive PKC/PRKCA signaling (PubMed:27353086). {ECO:0000250|UniProtKB:P50461, ECO:0000250|UniProtKB:P50463, ECO:0000269|PubMed:15665106, ECO:0000269|PubMed:27353086, ECO:0000269|PubMed:9039266}. PTM: Phosphorylated by PKC/PRKCA. {ECO:0000250|UniProtKB:P50461}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P50463}. Cytoplasm {ECO:0000269|PubMed:18258855}. Cytoplasm, cytoskeleton {ECO:0000305}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:18258855}. Cytoplasm, myofibril, sarcomere {ECO:0000250|UniProtKB:P50461}. Note=Nucleocytoplasmic shuttling protein (By similarity). Mainly cytoplasmic. In the Z line, found associated with GLRX3 (via C-terminus). {ECO:0000250|UniProtKB:P50463, ECO:0000269|PubMed:18258855}. SUBUNIT: Self-associates. Oligomeric in the cytoplasm and monomeric in the nucleus. Homooligomers preferentially form along the actin cytoskeleton (By similarity). Interacts with TCAP (PubMed:20044516). Interacts with LDHD, MYOD1, MYOG, ACTN2, NRAP, MYF6 (By similarity). Interacts (via N-terminus)D with GLRX3 (via C-terminus) and PPP3CA; GLRX3 and calcineurin compete for interaction with CSRP3 (PubMed:18258855). Interacts with CFL2; the stoichiometry influences F-actin depolymerization and possibly two molecules of CFL2 can interact with one molecule of CSRP3 resulting in the highest functional impact; the interaction is stronger with phosphorylated CFL2 (By similarity). {ECO:0000250|UniProtKB:P50461, ECO:0000250|UniProtKB:P50463, ECO:0000269|PubMed:18258855, ECO:0000269|PubMed:20044516}. DOMAIN: LIM zinc-binding domain 1 is required for self-association. LIM zinc-binding domain 1 and LIM zinc-binding domain 2 both are required for optimal actin-bundling activity. LIM zinc-binding domain 1 mediates binding to MYOD1. LIM zinc-binding domain 2 mediates binding to SPTB. {ECO:0000250|UniProtKB:P50461, ECO:0000250|UniProtKB:P50463}. +Q9D269 CST11_MOUSE Cystatin-11 (Cystatin-E1) (Cystatin-related epididymal spermatogenic protein 2) 139 16,217 Chain (1); Disulfide bond (2); Glycosylation (1); Signal peptide (1) FUNCTION: Has antibacterial activity against the Gram-negative bacteria E.coli. May play a role in sperm maturation and fertilization. {ECO:0000250|UniProtKB:Q9H112}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9H112}. Note=Probably secreted into the epididymis lumen, where it localizes to the outer surface of sperm. Specifically localizes to the postacrosomal and tail regions of sperm. {ECO:0000250|UniProtKB:Q9H112}. TISSUE SPECIFICITY: Expressed in epididymis, where it localizes to the proximal caput and also part of the midcaput. Not detected in other tissues tested. {ECO:0000269|PubMed:12586767, ECO:0000269|PubMed:12700194}. +Q7TT23 CT194_MOUSE Uncharacterized protein C20orf194 homolog 1179 132,207 Chain (1); Sequence conflict (2) FUNCTION: May act as an effector for ARL3. {ECO:0000250}. SUBUNIT: Interacts with ARL3. {ECO:0000250}. +P57757 CTNS_MOUSE Cystinosin 367 42,203 Chain (1); Domain (2); Glycosylation (6); Motif (1); Topological domain (8); Transmembrane (7) TRANSMEM 122 142 Helical. {ECO:0000255}.; TRANSMEM 162 182 Helical. {ECO:0000255}.; TRANSMEM 206 226 Helical. {ECO:0000255}.; TRANSMEM 238 258 Helical. {ECO:0000255}.; TRANSMEM 262 282 Helical. {ECO:0000255}.; TRANSMEM 298 318 Helical. {ECO:0000255}.; TRANSMEM 336 356 Helical. {ECO:0000255}. TOPO_DOM 1 121 Lumenal. {ECO:0000255}.; TOPO_DOM 143 161 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 183 205 Lumenal. {ECO:0000255}.; TOPO_DOM 227 237 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 259 261 Lumenal. {ECO:0000255}.; TOPO_DOM 283 297 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 319 335 Lumenal. {ECO:0000255}.; TOPO_DOM 357 367 Cytoplasmic. {ECO:0000255}. FUNCTION: Cystine/H(+) symporter thought to transport cystine out of lysosomes. Plays an important role in melanin synthesis, possibly by preventing melanosome acidification and subsequent degradation of tyrosinase TYR. {ECO:0000269|PubMed:22649030}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:O60931}; Multi-pass membrane protein. Melanosome {ECO:0000269|PubMed:22649030}. +P26231 CTNA1_MOUSE Catenin alpha-1 (102 kDa cadherin-associated protein) (Alpha E-catenin) (CAP102) 906 100,106 Beta strand (1); Chain (1); Cross-link (2); Helix (19); Initiator methionine (1); Modified residue (11); Mutagenesis (5); Region (3); Turn (1) FUNCTION: Associates with the cytoplasmic domain of a variety of cadherins. The association of catenins to cadherins produces a complex which is linked to the actin filament network, and which seems to be of primary importance for cadherins cell-adhesion properties. Can associate with both E- and N-cadherins. Originally believed to be a stable component of E-cadherin/catenin adhesion complexes and to mediate the linkage of cadherins to the actin cytoskeleton at adherens junctions. In contrast, cortical actin was found to be much more dynamic than E-cadherin/catenin complexes and CTNNA1 was shown not to bind to F-actin when assembled in the complex suggesting a different linkage between actin and adherens junctions components. The homodimeric form may regulate actin filament assembly and inhibit actin branching by competing with the Arp2/3 complex for binding to actin filaments. May play a crucial role in cell differentiation. {ECO:0000269|PubMed:16325583}. PTM: Sumoylated. {ECO:0000250|UniProtKB:P35221}.; PTM: Phosphorylation seems to contribute to the strength of cell-cell adhesion rather than to the basic capacity for cell-cell adhesion. {ECO:0000305|PubMed:25653389}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell junction, adherens junction. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell junction. Note=Found at cell-cell boundaries and probably at cell-matrix boundaries. SUBUNIT: Monomer and homodimer; the monomer preferentially binds to CTNNB1 and the homodimer to actin. Binds AFDN and F-actin (PubMed:11907041). Possible component of an E-cadherin/ catenin adhesion complex together with E-cadherin/CDH1 and beta-catenin/CTNNB1 or gamma-catenin/JUP; the complex is located to adherens junctions (PubMed:7982500, PubMed:16325582, PubMed:16325583, PubMed:18093941, PubMed:25653389, PubMed:10882138). The stable association of CTNNA1 is controversial as CTNNA1 was shown not to bind to F-actin when assembled in the complex. Alternatively, the CTNNA1-containing complex may be linked to F-actin by other proteins such as LIMA1 (PubMed:18093941). Interacts with LIMA1 (PubMed:18093941). Interacts with ARHGAP21 and with AJUBA (By similarity). Interacts with vinculin/VCL (By similarity). Component of an cadherin:catenin adhesion complex composed of at least of CDH26, beta-catenin/CTNNB1, alpha-catenin/CTNNA1 and p120 catenin/CTNND1 (By similarity). {ECO:0000250|UniProtKB:P35221, ECO:0000269|PubMed:10882138, ECO:0000269|PubMed:11907041, ECO:0000269|PubMed:16325582, ECO:0000269|PubMed:16325583, ECO:0000269|PubMed:18093941, ECO:0000269|PubMed:25653389, ECO:0000269|PubMed:7982500}. TISSUE SPECIFICITY: Expressed ubiquitously in normal tissues. +Q6ZQ06 CE162_MOUSE Centrosomal protein of 162 kDa (Cep162) (Protein QN1 homolog) 1403 160,855 Chain (1); Coiled coil (2); Modified residue (2) FUNCTION: Required to promote assembly of the transition zone in primary cilia. Acts by specifically recognizing and binding the axonemal microtubule. Localizes to the distal ends of centrioles before ciliogenesis and directly binds to axonemal microtubule, thereby promoting and restricting transition zone formation specifically at the cilia base. Required to mediate CEP290 association with microtubules (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Nucleus {ECO:0000250}. Note=Localizes to the distal end of centrioles throughout the cell cycle. During ciliogenesis, found at the cilia base. Localizes to spindle microtubules during mitosis (By similarity). {ECO:0000250}. SUBUNIT: Interacts with CPNE4 (PubMed:12522145). Interacts with alpha-tubulin. Interacts with CEP290 (By similarity). {ECO:0000250|UniProtKB:Q4KLH6, ECO:0000250|UniProtKB:Q5TB80, ECO:0000269|PubMed:12522145}. +Q5PR68 CE112_MOUSE Centrosomal protein of 112 kDa (Cep112) (Coiled-coil domain-containing protein 46) 954 112,676 Alternative sequence (2); Chain (1); Coiled coil (1); Erroneous initiation (1) SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Note=Localizes around spindle poles in some cells. {ECO:0000250}. +Q8BI22 CE128_MOUSE Centrosomal protein of 128 kDa (Cep128) 1102 128,503 Alternative sequence (2); Chain (1); Coiled coil (2); Erroneous initiation (1); Modified residue (3) SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. Note=Associates with the mother centriole. {ECO:0000250}. +P05208 CEL2A_MOUSE Chymotrypsin-like elastase family member 2A (EC 3.4.21.71) (Elastase-2) (Elastase-2A) 271 28,914 Active site (3); Chain (1); Disulfide bond (4); Domain (1); Propeptide (1); Signal peptide (1) FUNCTION: Acts upon elastin. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Pancreas. +Q9ESN5 CENPK_MOUSE Centromere protein K (CENP-K) (SoxLZ/Sox6 leucine zipper-binding protein in testis) 271 31,686 Alternative sequence (3); Chain (1); Coiled coil (2); Erroneous initiation (1); Sequence caution (1); Sequence conflict (1) FUNCTION: Component of the CENPA-CAD (nucleosome distal) complex, a complex recruited to centromeres which is involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation. May be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex. Acts in coordination with KNL1 to recruit the NDC80 complex to the outer kinetochore (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, centromere {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Note=Localizes exclusively in the centromeres. The CENPA-CAD complex is probably recruited on centromeres by the CENPA-NAC complex (By similarity). {ECO:0000250}. SUBUNIT: Component of the CENPA-CAD complex, composed of CENPI, CENPK, CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS. The CENPA-CAD complex interacts with the CENPA-NAC complex, at least composed of CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and CENPU. May interact with Sox6. TISSUE SPECIFICITY: Highly expressed in testis. {ECO:0000269|PubMed:10996314}. +Q91ZI0 CELR3_MOUSE Cadherin EGF LAG seven-pass G-type receptor 3 3301 358,478 Chain (1); Compositional bias (1); Disulfide bond (27); Domain (21); Frameshift (1); Glycosylation (15); Modified residue (4); Sequence conflict (4); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 2532 2552 Helical; Name=1. {ECO:0000255}.; TRANSMEM 2564 2584 Helical; Name=2. {ECO:0000255}.; TRANSMEM 2593 2613 Helical; Name=3. {ECO:0000255}.; TRANSMEM 2635 2655 Helical; Name=4. {ECO:0000255}.; TRANSMEM 2674 2694 Helical; Name=5. {ECO:0000255}.; TRANSMEM 2717 2737 Helical; Name=6. {ECO:0000255}.; TRANSMEM 2745 2765 Helical; Name=7. {ECO:0000255}. TOPO_DOM 32 2531 Extracellular. {ECO:0000255}.; TOPO_DOM 2553 2563 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 2585 2592 Extracellular. {ECO:0000255}.; TOPO_DOM 2614 2634 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 2656 2673 Extracellular. {ECO:0000255}.; TOPO_DOM 2695 2716 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 2738 2744 Extracellular. {ECO:0000255}.; TOPO_DOM 2766 3301 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor that may have an important role in cell/cell signaling during nervous system formation. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed in the CNS and in the eye. {ECO:0000269|PubMed:10790539}. +Q6RT24 CENPE_MOUSE Centromere-associated protein E (Centromere protein E) (CENP-E) (Kinesin superfamily protein 10) (KIF10) (Motor domain of KIF10) 2474 286,525 Chain (1); Coiled coil (1); Domain (1); Frameshift (1); Lipidation (1); Modified residue (4); Nucleotide binding (1); Propeptide (1); Region (2); Sequence caution (2); Sequence conflict (2) FUNCTION: Microtubule plus-end-directed kinetochore motor which plays an important role in chromosome congression, microtubule-kinetochore conjugation and spindle assembly checkpoint activation. Drives chromosome congression (alignment of chromosomes at the spindle equator resulting in the formation of the metaphase plate) by mediating the lateral sliding of polar chromosomes along spindle microtubules towards the spindle equator and by aiding the establishment and maintenance of connections between kinetochores and spindle microtubules. The transport of pole-proximal chromosomes towards the spindle equator is favored by microtubule tracks that are detyrosinated. Acts as a processive bi-directional tracker of dynamic microtubule tips; after chromosomes have congressed, continues to play an active role at kinetochores, enhancing their links with dynamic microtubule ends. Suppresses chromosome congression in NDC80-depleted cells and contributes positively to congression only when microtubules are stabilized (By similarity). Plays an important role in the formation of stable attachments between kinetochores and spindle microtubules (PubMed:12925705). The stabilization of kinetochore-microtubule attachment also requires CENPE-dependent localization of other proteins to the kinetochore including BUB1B, MAD1 and MAD2. Plays a role in spindle assembly checkpoint activation (SAC) via its interaction with BUB1B resulting in the activation of its kinase activity, which is important for activating SAC (PubMed:12361599). Necessary for the mitotic checkpoint signal at individual kinetochores to prevent aneuploidy due to single chromosome loss (PubMed:12925705). {ECO:0000250|UniProtKB:Q02224, ECO:0000269|PubMed:12361599, ECO:0000269|PubMed:12925705}. PTM: The C-terminal inhibitory domain is phosphorylated. Phosphorylation relieves autoinhibition of the kinetochore motor (By similarity). {ECO:0000250}.; PTM: Sumoylated with SUMO2 and SUMO3. The sumoylation mediates the association to the kinetochore. {ECO:0000250|UniProtKB:Q02224}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:12361599, ECO:0000269|PubMed:12925705}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:12361599, ECO:0000269|PubMed:12925705}. Chromosome, centromere {ECO:0000250|UniProtKB:Q02224}. Note=Associates with kinetochores during congression (as early as prometaphase), relocates to the spindle midzone at anaphase, and is quantitatively discarded at the end of the cell division (PubMed:12361599, PubMed:12925705). Recruited to the kinetochore in a SEPT7, CENPQ and TRAPPC12-dependent manner. Recruited to the pericentromeric/centromeric regions of the chromosome in a CTCF-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q02224, ECO:0000269|PubMed:12361599, ECO:0000269|PubMed:12925705}. SUBUNIT: Monomer. Interacts with CENPF, SEPT7 KIF18A and PRC1 (By similarity). Interacts with BUB1B (PubMed:12925705). Interacts with SKAP; this interaction greatly favors SKAP binding to microtubules. Interacts with TRAPPC12 and CTCF (By similarity). {ECO:0000250|UniProtKB:Q02224, ECO:0000269|PubMed:12925705}. DOMAIN: The protein is composed of a N-terminal kinesin-motor domain involved in the chromosome movements, a long coil-coiled region involved in the homodimerization and an inhibitory C-tail involved in autoinhibition of the N-terminal catalytic part. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in hippocampus. Also detected in liver and fibroblasts (at protein level). {ECO:0000269|PubMed:12361599, ECO:0000269|PubMed:9275178}. +O55233 CER1_MOUSE Cerberus (Cerberus-like protein) (Cer-l) (Cerberus-related protein) 272 30,431 Chain (1); Disulfide bond (4); Domain (1); Glycosylation (2); Sequence conflict (1); Signal peptide (1) FUNCTION: Cytokine that may play a role in anterior neural induction and somite formation during embryogenesis in part, through a BMP-inhibitory mechanism. Can regulate Nodal signaling during gastrulation as well as the formation and patterning of the primitive streak. {ECO:0000269|PubMed:12431380, ECO:0000269|PubMed:9431803, ECO:0000269|PubMed:9501024, ECO:0000269|PubMed:9600941}. PTM: N-glycosylated. {ECO:0000269|PubMed:9501024}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9431803}. SUBUNIT: Forms monomers and predominantly dimers. +Q61147 CERU_MOUSE Ceruloplasmin (EC 1.16.3.1) (Ferroxidase) 1061 121,151 Chain (1); Disulfide bond (5); Domain (9); Glycosylation (6); Metal binding (19); Sequence conflict (19); Signal peptide (1) FUNCTION: Ceruloplasmin is a blue, copper-binding (6-7 atoms per molecule) glycoprotein. It has ferroxidase activity oxidizing Fe(2+) to Fe(3+) without releasing radical oxygen species. It is involved in iron transport across the cell membrane. Provides Cu(2+) ions for the ascorbate-mediated deaminase degradation of the heparan sulfate chains of GPC1. May also play a role in fetal lung development or pulmonary antioxidant defense (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. Note=Colocalizes with GCP1 in secretory intracellular compartments. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in many tissues, including liver, eye and brain. {ECO:0000269|PubMed:8690795}. +Q0VEJ0 CEP76_MOUSE Centrosomal protein of 76 kDa (Cep76) 659 74,303 Chain (1); Modified residue (2) FUNCTION: Centrosomal protein involved in regulation of centriole duplication. Required to limit centriole duplication to once per cell cycle by preventing centriole reduplication (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250}. Note=Does not localize along the ciliary axoneme. {ECO:0000250}. SUBUNIT: Interacts with CCP110 and CEP97. {ECO:0000250}. +Q9D727 CF226_MOUSE Uncharacterized protein C6orf226 homolog 114 12,013 Chain (1); Modified residue (1); Sequence conflict (1) +E9Q5M6 CFA44_MOUSE Cilia- and flagella-associated protein 44 1843 211,546 Chain (1); Coiled coil (2); Modified residue (1); Repeat (10) FUNCTION: Flagellar protein involved in sperm flagellum axoneme organization and function. {ECO:0000269|PubMed:28552195, ECO:0000269|PubMed:29449551}. SUBCELLULAR LOCATION: Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q57WH1}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:Q57WH1}. TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:28552195}. +Q8BHG9 CGBP1_MOUSE CGG triplet repeat-binding protein 1 (CGG-binding protein 1) (20 kDa CGG-binding protein) (p20-CGGBP DNA-binding protein) 167 18,761 Chain (1); Modified residue (2); Motif (1) FUNCTION: Binds to nonmethylated 5'-d(CGG)(n)-3' trinucleotide repeats in the FMR1 promoter. May play a role in regulating FMR1 promoter (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +Q8BWQ6 CP062_MOUSE UPF0505 protein C16orf62 homolog 963 109,077 Alternative sequence (4); Chain (1); Compositional bias (1); Modified residue (1); Sequence conflict (6); Transmembrane (1) TRANSMEM 699 719 Helical. {ECO:0000255}. FUNCTION: Involved in copper-dependent ATP7A trafficking between the trans-Golgi network and vesicles in the cell periphery; the function is proposed to depend on its association within the CCC complex and cooperation with the WASH complex on early endosomes. Seems not to be required for CCC complex stability. {ECO:0000250|UniProtKB:Q7Z3J2}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Early endosome {ECO:0000250|UniProtKB:Q7Z3J2}. SUBUNIT: Interacts with COMMD1, CCDC93 and CCDC22; proposed to be a component of the CCC (COMMD/CCDC22/CCDC93) complex which contains at least COMMD1 (and possibly other COMM domain-containing proteins), CCDC22, CCDC93 and C16orf62 homolog. Interacts with WASHC1 and WASHC2. {ECO:0000250|UniProtKB:Q7Z3J2}. +Q9QZ82 CP11A_MOUSE Cholesterol side-chain cleavage enzyme, mitochondrial (EC 1.14.15.6) (CYPXIA1) (Cholesterol desmolase) (Cytochrome P450 11A1) (Cytochrome P450(scc)) 526 60,315 Chain (1); Metal binding (1); Transit peptide (1) Lipid metabolism; C21-steroid hormone metabolism. FUNCTION: Catalyzes the side-chain cleavage reaction of cholesterol to pregnenolone, the precursor of most steroid hormones. {ECO:0000250|UniProtKB:P05108}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P14137}; Peripheral membrane protein {ECO:0000305}. Note=Localizes to the matrix side of the mitochondrion inner membrane. {ECO:0000250|UniProtKB:P14137}. SUBUNIT: Interacts with FDX1/adrenodoxin. {ECO:0000250}. +Q8K1L6 CP074_MOUSE Uncharacterized protein C16orf74 homolog 76 8,286 Chain (1); Erroneous initiation (2); Modified residue (2) +Q8BT88 CP090_MOUSE Uncharacterized protein C16orf90 homolog 171 18,157 Alternative sequence (3); Chain (1); Frameshift (1) +Q64429 CP1B1_MOUSE Cytochrome P450 1B1 (EC 1.14.14.1) (CYPIB1) (Cytochrome P450CMEF) (Cytochrome P450EF) 543 60,537 Chain (1); Metal binding (1); Sequence conflict (5) FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, retinoid and xenobiotics. Preferentially oxidizes 17beta-estradiol to the carcinogenic 4-hydroxy derivative, and a variety of procarcinogenic compounds to their activated forms, including polycyclic aromatic hydrocarbons. Promotes angiogenesis by removing cellular oxygenation products, thereby decreasing oxidative stress, release of antiangiogenic factor THBS2, then allowing endothelial cells migration, cell adhesion and capillary morphogenesis. These changes are concommitant with the endothelial nitric oxide synthase activity and nitric oxide synthesis. Plays an important role in the regulation of perivascular cell proliferation, migration, and survival through modulation of the intracellular oxidative state and NF-kappa-B expression and/or activity, during angiogenesis. Contributes to oxidative homeostasis and ultrastructural organization and function of trabecular meshwork tissue through modulation of POSTN expression. {ECO:0000269|PubMed:15258110, ECO:0000269|PubMed:19005183, ECO:0000269|PubMed:20032512, ECO:0000269|PubMed:23568032, ECO:0000269|PubMed:23821647, ECO:0000269|PubMed:23979599}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23692925}; Peripheral membrane protein {ECO:0000269|PubMed:23692925}. Microsome membrane {ECO:0000269|PubMed:23692925}; Peripheral membrane protein {ECO:0000269|PubMed:23692925}. Mitochondrion {ECO:0000269|PubMed:23692925}. TISSUE SPECIFICITY: Constitutively expressed in retinal, heart and kidney pericytes cells. {ECO:0000269|PubMed:23568032}. +Q8BKE6 CP20A_MOUSE Cytochrome P450 20A1 (EC 1.14.-.-) 462 52,149 Chain (1); Metal binding (1); Transmembrane (1) TRANSMEM 4 24 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q64459 CP3AB_MOUSE Cytochrome P450 3A11 (EC 1.14.14.1) (CYPIIIA11) (Cytochrome P-450IIIAM1) (Cytochrome P-450UT) 504 57,855 Chain (1); Metal binding (1) FUNCTION: Catalyzes erythromycin N-demethylation, nifedipine oxidation and testosterone 6 beta-hydroxylation. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. TISSUE SPECIFICITY: Highly expressed in liver. +O54749 CP2J5_MOUSE Cytochrome P450 2J5 (EC 1.14.14.1) (Arachidonic acid epoxygenase) (CYPIIJ5) 501 57,784 Chain (1); Metal binding (1) SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. +O09158 CP3AP_MOUSE Cytochrome P450 3A25 (EC 1.14.14.1) (CYPIIIA25) 503 58,122 Chain (1); Metal binding (1) FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. +Q9WVK8 CP46A_MOUSE Cholesterol 24-hydroxylase (CH24H) (EC 1.14.14.25) (Cytochrome P450 46A1) 500 56,814 Chain (1); Compositional bias (1); Metal binding (1); Transmembrane (1) TRANSMEM 3 23 Helical. {ECO:0000255}. FUNCTION: Involved in the turnover of cholesterol. It converts cholesterol into 24S-hydroxycholesterol and, to a lesser extent, 25-hydroxycholesterol. Has also activity with xenobiotic compounds. {ECO:0000250|UniProtKB:Q9Y6A2}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. Microsome membrane; Single-pass membrane protein. TISSUE SPECIFICITY: Expressed in high level in brain (cerebral cortex, hippocampus, dentate gyrus and thalamus) and in lower levels in testis and liver. Brain's expression increased linearly with age. +Q8CIM7 CP2DQ_MOUSE Cytochrome P450 2D26 (EC 1.14.14.1) (CYPIID26) 500 56,976 Chain (1); Metal binding (1); Modified residue (1); Sequence conflict (1) FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. {ECO:0000250|UniProtKB:P10634}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Microsome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. +O35218 CPSF2_MOUSE Cleavage and polyadenylation specificity factor subunit 2 (Cleavage and polyadenylation specificity factor 100 kDa subunit) (CPSF 100 kDa subunit) 782 88,383 Chain (1); Modified residue (4) FUNCTION: Component of the cleavage and polyadenylation specificity factor (CPSF) complex that play a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. Involved in the histone 3' end pre-mRNA processing (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Component of the cleavage and polyadenylation specificity factor (CPSF) complex, composed of CPSF1, CPSF2, CPSF3, CPSF4 and FIP1L1. Interacts with CPSF3, CSTF2 and SYMPK (By similarity). Interacts with ZC3H3 (PubMed:16115198). {ECO:0000250|UniProtKB:Q9P2I0, ECO:0000269|PubMed:16115198}. +O88456 CPNS1_MOUSE Calpain small subunit 1 (CSS1) (Calcium-activated neutral proteinase small subunit) (CANP small subunit) (Calcium-dependent protease small subunit) (CDPS) (Calcium-dependent protease small subunit 1) (Calpain regulatory subunit) 269 28,463 Calcium binding (3); Chain (1); Compositional bias (4); Domain (5); Metal binding (16); Modified residue (3); Sequence conflict (4) FUNCTION: Regulatory subunit of the calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Translocates to the plasma membrane upon calcium binding. {ECO:0000250}. SUBUNIT: Homodimer or heterodimer of a large (catalytic) and a small (regulatory) subunit. In presence of calcium, the heterodimer dissociates (By similarity). {ECO:0000250}. DOMAIN: The contact of the 5th EF-hand domain from each monomer allows the formation of the homodimer and also appears to mediate the contact between the large catalytic subunit and small regulatory subunit for the formation of the heterodimer. {ECO:0000250}.; DOMAIN: EF-hand domains are paired. EF-hand 1 is paired with EF-hand 2 and EF-hand 3 is paired with EF-hand 4. The fifth EF-hand domain, left unpaired, does not bind the calcium but is responsible of the dimerization by EF-embrace. The first four EF-hand domains bind calcium, however it is not sure if the binding of EF-hand 4 to calcium is physiologically relevant. +Q924X2 CPT1B_MOUSE Carnitine O-palmitoyltransferase 1, muscle isoform (CPT1-M) (EC 2.3.1.21) (Carnitine O-palmitoyltransferase I, muscle isoform) (CPT I) (CPTI-M) (Carnitine palmitoyltransferase 1B) 772 88,217 Active site (1); Binding site (2); Chain (1); Region (1); Sequence conflict (2); Topological domain (3); Transmembrane (2) TRANSMEM 48 73 Helical. {ECO:0000255}.; TRANSMEM 103 122 Helical. {ECO:0000255}. TOPO_DOM 1 47 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 74 102 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 123 772 Cytoplasmic. {ECO:0000255}. Lipid metabolism; fatty acid beta-oxidation. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q80Y72 CSTL1_MOUSE Cystatin-like 1 140 16,199 Alternative sequence (1); Chain (1); Disulfide bond (2); Domain (1); Glycosylation (1); Sequence conflict (3); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Highly expressed in testis where it localizes to spermatogonium, spermatocyes and round spermatids. Not detected in spermatozoa. Also detected in epididymis, cerebrum and pituitary. {ECO:0000269|PubMed:18300157}. +Q9JM84 CST10_MOUSE Cystatin 10 (Carminerin) 148 16,451 Alternative sequence (1); Chain (1); Disulfide bond (2); Domain (1); Signal peptide (1) FUNCTION: May play a role in the last steps of the chondrocyte differentiation pathway as an inducer of maturation (PubMed:13679380). Induces chondrocyte calcification during endochondral ossification by playing a role in the transcriptional inhibition of ENPP1, a generator of pyrophosphate which inhibits calcification (PubMed:16680148). Possibly impairs the binding of a transcription factor to the ENPP1 promoter (PubMed:16680148). Unlike other cystatins, does not have thiol protease inhibitor activity (PubMed:16680148). {ECO:0000269|PubMed:13679380, ECO:0000269|PubMed:16680148}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:13679380}. TISSUE SPECIFICITY: In cartilage, expressed mainly in mature chondrocytes including prehypertrophic and hypertrophic cells (at protein level) (PubMed:13679380). Expressed exclusively in cartilage (PubMed:11856874). {ECO:0000269|PubMed:11856874, ECO:0000269|PubMed:13679380}. +Q9D1K7 CT027_MOUSE UPF0687 protein C20orf27 homolog 174 19,476 Chain (1); Initiator methionine (1); Modified residue (2) +Q9DA42 CT085_MOUSE Uncharacterized protein C20orf85 homolog 136 15,588 Chain (1); Sequence conflict (4) +Q8VII3 CST14_MOUSE Cystatin-14 (Cystatin SC) 130 15,077 Chain (1); Disulfide bond (2); Sequence conflict (1); Signal peptide (1) FUNCTION: May play a specialized role in spermatogenesis. {ECO:0000269|PubMed:12444065}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Located only in seminiferous tubules (at protein level). Expressed in testis and Sertoli cells. {ECO:0000269|PubMed:12444065}. +P32766 CST8_MOUSE Cystatin-8 (Cystatin-related epididymal spermatogenic protein) (Cystatin-related epididymal-specific protein) 142 16,288 Chain (1); Disulfide bond (2); Glycosylation (2); Motif (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Performs a specialized role during sperm development and maturation. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Proximal caput region of the epididymis. Lower expression in the testis. Within the testis it is localized to the elongating spermatids, whereas within the epididymis it is exclusively synthesized by the proximal caput epithelium. +Q3TZW0 ECSCR_MOUSE Endothelial cell-specific chemotaxis regulator (Apoptosis regulator through modulating IAP expression) (ARIA) (Endothelial cell-specific molecule 2) 214 22,689 Alternative sequence (2); Chain (1); Compositional bias (2); Modified residue (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 131 151 Helical. {ECO:0000255}. TOPO_DOM 19 130 Extracellular. {ECO:0000255}.; TOPO_DOM 152 214 Cytoplasmic. {ECO:0000255}. FUNCTION: Regulates endothelial chemotaxis and tube formation (By similarity). Has a role in angiogenesis and apoptosis via modulation of the actin cytoskeleton and facilitation of proteasomal degradation of the apoptosis inhibitors BIRC3/IAP1 and BIRC2/IAP2. {ECO:0000250, ECO:0000269|PubMed:19416853}. PTM: May be heavily O-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with FLNA. Interacts with the 20S proteasome subunit PSMA7. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in all tissues examined, highest expression was observed in lung and spleen endothelial cells. {ECO:0000269|PubMed:19416853}. +Q9QZH6 ECSIT_MOUSE Evolutionarily conserved signaling intermediate in Toll pathway, mitochondrial (Protein SITPEC) 435 49,799 Chain (1); Sequence conflict (1); Transit peptide (1) FUNCTION: Adapter protein of the Toll-like and IL-1 receptor signaling pathway that is involved in the activation of NF-kappa-B via MAP3K1. Promotes proteolytic activation of MAP3K1. Involved in the BMP signaling pathway. Required for normal embryonic development. {ECO:0000269|PubMed:10465784, ECO:0000269|PubMed:14633973}.; FUNCTION: Required for efficient assembly of mitochondrial NADH:ubiquinone oxidoreductase. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14633973}. Nucleus {ECO:0000269|PubMed:14633973}. Mitochondrion {ECO:0000250}. SUBUNIT: Interacts with NDUFAF1 (By similarity). Interacts with ACAD9 (By similarity). Part of the mitochondrial complex I assembly (MCIA) complex. The complex comprises at least TMEM126B, NDUFAF1, ECSIT, and ACAD9 (By similarity). Interacts with MAP3K1, SMAD4 and TRAF6. Interacts with SMAD1 only after BMP4-treatment. Interacts with TRIM59 (PubMed:22588174). {ECO:0000250|UniProtKB:Q5XIC2, ECO:0000250|UniProtKB:Q9BQ95, ECO:0000269|PubMed:10465784, ECO:0000269|PubMed:14633973, ECO:0000269|PubMed:22588174}. TISSUE SPECIFICITY: Detected in heart, brain, lung, liver, skeletal muscle, kidney and testis. Detected in embryonic mesoderm and epiblast, and in extraembryonic ectoderm. {ECO:0000269|PubMed:10465784, ECO:0000269|PubMed:14633973}. +Q9CWL8 CTBL1_MOUSE Beta-catenin-like protein 1 (Nuclear-associated protein) (NAP) 563 64,980 Chain (1); Coiled coil (1); Compositional bias (2); Modified residue (4); Motif (2); Repeat (7); Sequence conflict (4) FUNCTION: Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May induce apoptosis (By similarity). Participates in AID/AICDA-mediated Ig class switching recombination (CSR). {ECO:0000250, ECO:0000269|PubMed:20585033}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the PRP19-CDC5L splicing complex composed of a core complex comprising a homotetramer of PRPF19, CDC5L, PLRG1 and BCAS2, and at least three less stably associated proteins CTNNBL1, CWC15 and HSPA8. Interacts directly with CWC15 and CDC5L in the complex. Interacts with AICDA; the interaction is important for the antibody diversification activity of AICDA. Interacts with PRPF31 (via its NLS). Interacts (via its N-terminal NLS) with KPNA1 and KPNA2 (By similarity). {ECO:0000250}. DOMAIN: The surface residues of the concave side of the superhelical ARM repeat region contribute to, but are not essential for NLS binding. {ECO:0000250}. +P0CG15 CTF8_MOUSE Chromosome transmission fidelity protein 8 homolog 121 13,228 Chain (1); Erroneous translation (3) FUNCTION: Chromosome cohesion factor involved in sister chromatid cohesion and fidelity of chromosome transmission. Component of one of the cell nuclear antigen loader complexes, CTF18-replication factor C (CTF18-RFC), which consists of CTF18, CTF8, DCC1, RFC2, RFC3, RFC4 and RFC5. The CTF18-RFC complex binds to single-stranded and primed DNAs and has weak ATPase activity that is stimulated the presence of primed DNA, replication protein A (RPA) and proliferating cell nuclear antigen (PCNA). The CTF18-RFC complex catalyzes the ATP-dependent loading of PCNA onto primed and gapped DNA. It also interacts with and stimulates POLH, which is suggestive of a protein network that coordinates DNA repair, recombination and chromosome cohesion reactions with replication fork progression (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Note=Associates with chromatin during S phase. {ECO:0000250}. SUBUNIT: Component of the CTF18-RFC complex, which consists of CTF18, CTF8, DCC1, RFC2, RFC3, RFC4 and RFC5. The CTF18-RFC complex does not interact with the Rad9/Rad1/Hus1 complex. The CTF18-RFC complex interacts with POLH. CTF18/CTF8/DCC1 associate with PCNA. CTF8 exists as a dimer with DCC1 (By similarity). {ECO:0000250}. +P58465 CTDSL_MOUSE CTD small phosphatase-like protein (CTDSP-like) (EC 3.1.3.16) (Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 3) (NIF-like protein) (Nuclear LIM interactor-interacting factor 1) (NLI-interacting factor 1) (Small C-terminal domain phosphatase 3) (SCP3) (Small CTD phosphatase 3) 276 31,156 Active site (2); Chain (1); Domain (1); Metal binding (3); Sequence conflict (1); Site (2) FUNCTION: Preferentially catalyzes the dephosphorylation of 'Ser-5' within the tandem 7 residue repeats in the C-terminal domain (CTD) of the largest RNA polymerase II subunit POLR2A. Negatively regulates RNA polymerase II transcription, possibly by controlling the transition from initiation/capping to processive transcript elongation. Recruited by REST to neuronal genes that contain RE-1 elements, leading to neuronal gene silencing in non-neuronal cells (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Monomer. Interacts with REST. {ECO:0000250}. +P29268 CTGF_MOUSE Connective tissue growth factor (CCN family member 2) (Hypertrophic chondrocyte-specific protein 24) (Protein FISP-12) 348 37,824 Chain (1); Disulfide bond (5); Domain (4); Region (1); Sequence conflict (6); Signal peptide (1) FUNCTION: Major connective tissue mitoattractant secreted by vascular endothelial cells. Promotes proliferation and differentiation of chondrocytes (By similarity). Mediates heparin- and divalent cation-dependent cell adhesion in many cell types including fibroblasts, myofibroblasts, endothelial and epithelial cells (By similarity). Enhances fibroblast growth factor-induced DNA synthesis (By similarity). {ECO:0000250, ECO:0000269|PubMed:10082563, ECO:0000269|PubMed:9184077}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:9184077}. Secreted {ECO:0000269|PubMed:9184077}. SUBUNIT: Monomer. {ECO:0000250}. TISSUE SPECIFICITY: Testis, spleen, kidney, lung, heart, and brain (lowest level in testis and highest in lung). +Q6X893 CTL1_MOUSE Choline transporter-like protein 1 (Solute carrier family 44 member 1) (CD antigen CD92) 653 73,067 Alternative sequence (1); Chain (1); Compositional bias (1); Erroneous initiation (1); Initiator methionine (1); Lipidation (1); Sequence conflict (6); Topological domain (10); Transmembrane (9) TRANSMEM 30 50 Helical. {ECO:0000255}.; TRANSMEM 212 232 Helical. {ECO:0000255}.; TRANSMEM 238 258 Helical. {ECO:0000255}.; TRANSMEM 288 308 Helical. {ECO:0000255}.; TRANSMEM 315 335 Helical. {ECO:0000255}.; TRANSMEM 338 358 Helical. {ECO:0000255}.; TRANSMEM 380 400 Helical. {ECO:0000255}.; TRANSMEM 537 557 Helical. {ECO:0000255}.; TRANSMEM 566 586 Helical. {ECO:0000255}. TOPO_DOM 2 29 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 51 211 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 233 237 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 259 287 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 309 314 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 336 337 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 359 379 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 401 536 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 558 565 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 587 653 Mitochondrial intermembrane. {ECO:0000255}. FUNCTION: Choline transporter. May be involved in membrane synthesis and myelin production. {ECO:0000269|PubMed:15474312, ECO:0000269|PubMed:19357133}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Mitochondrion outer membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Specifically abundant in skeletal muscle (at protein level). {ECO:0000269|PubMed:15474312}. +P12400 CTL2B_MOUSE Protein CTLA-2-beta (Cytotoxic T-lymphocyte-associated protein 2-beta) 113 13,122 Chain (1); Erroneous initiation (3); Region (1); Repeat (2); Sequence conflict (1) FUNCTION: Not known, expressed in activated T-cell. +E9Q7F5 EDD13_MOUSE Epididymal protein 13 164 18,665 Chain (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Highly expressed in segments II-V of the caput epididymis. {ECO:0000269|PubMed:12920233}. +Q8BJT9 EDEM2_MOUSE ER degradation-enhancing alpha-mannosidase-like protein 2 577 64,610 Chain (1); Glycosylation (4); Sequence conflict (4); Signal peptide (1) FUNCTION: Involved in the endoplasmic reticulum-associated degradation (ERAD) pathway that targets misfolded glycoproteins for degradation in an N-glycan-dependent manner (PubMed:15579471, PubMed:25655076). May initiate ERAD by promoting the first mannose trimming step of ERAD substrates, from Man9GlcNAc2 to Man8GlcNAc2 (By similarity). Seems to recognize and bind to exposed hydrophobic regions in target proteins (PubMed:25655076). {ECO:0000250|UniProtKB:Q9BV94, ECO:0000269|PubMed:15579471, ECO:0000269|PubMed:25655076}. PTM: N-glycosylated. {ECO:0000269|PubMed:15579471}. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000269|PubMed:15579471}. +Q2HXL6 EDEM3_MOUSE ER degradation-enhancing alpha-mannosidase-like protein 3 (EC 3.2.1.113) (Alpha-1,2-mannosidase EDEM3) 931 104,200 Active site (4); Chain (1); Domain (1); Glycosylation (7); Metal binding (1); Motif (1); Mutagenesis (1); Sequence conflict (1); Signal peptide (1) Protein modification; protein glycosylation. FUNCTION: Involved in endoplasmic reticulum-associated degradation (ERAD). Accelerates the glycoprotein ERAD by proteasomes, by catalyzing mannose trimming from Man8GlcNAc2 to Man7GlcNAc2 in the N-glycans. Seems to have alpha 1,2-mannosidase activity. {ECO:0000250|UniProtKB:Q9BZQ6, ECO:0000269|PubMed:16431915}. PTM: N-glycosylated. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138, ECO:0000269|PubMed:16431915}. DOMAIN: Contains a protease-associated domain of unknown function. TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in liver, heart and kidney. {ECO:0000269|PubMed:16431915}. +Q9JMG1 EDF1_MOUSE Endothelial differentiation-related factor 1 (EDF-1) (Multiprotein-bridging factor 1) (MBF1) 148 16,369 Chain (1); DNA binding (1); Domain (1); Initiator methionine (1); Modified residue (3); Motif (1); Region (2); Sequence conflict (1) FUNCTION: Transcriptional coactivator stimulating NR5A1 and ligand-dependent NR1H3/LXRA and PPARG transcriptional activities. Enhances the DNA-binding activity of ATF1, ATF2, CREB1 and NR5A1. Regulates nitric oxid synthase activity probably by sequestering calmodulin in the cytoplasm. Might function in endothelial cells differentiation, hormone-induced cardiomyocytes hypertrophy and lipid metabolism (By similarity). {ECO:0000250}. PTM: Phosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Also nuclear upon binding to NR5A1 and treatment of cells with TPA or forskolin. {ECO:0000250}. SUBUNIT: Interacts with TBP and the transcription factor IID (TFIID) complex, NR5A2, NR1H3 and PPARG. Interaction with TBP is regulated by phosphorylation. Binds NR5A1, ATF1, FOS and JUN via their conserved basic region. Binding to calmodulin is regulated by calcium and phosphorylation of the IQ motif (By similarity). {ECO:0000250}. DOMAIN: The IQ motif, which is involved in calmodulin binding, overlaps with the binding domain for nuclear receptors and transcription factors. Its phosphorylation probably allows a switch between the two activities of the protein (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain, liver, kidney and heart (at protein level). Also expressed in testis. {ECO:0000269|PubMed:11587857}. +A0A0A6YXX9 CTSEL_MOUSE Cation channel sperm-associated protein subunit epsilon-like protein (CatSper-epsilon-like) (CatSperepsilon-like) 775 89,594 Alternative sequence (2); Chain (1); Glycosylation (2); Sequence conflict (2); Signal peptide (1) +E9Q355 CTSG1_MOUSE Cation channel sperm-associated protein subunit gamma 1 1151 132,352 Alternative sequence (12); Chain (1); Glycosylation (1); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1064 1084 Helical. {ECO:0000255}. TOPO_DOM 39 1063 Extracellular. {ECO:0000255}.; TOPO_DOM 1085 1151 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +C6KI89 CTSG2_MOUSE Cation channel sperm-associated protein subunit gamma 2 1145 131,417 Chain (1); Glycosylation (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1064 1084 Helical. {ECO:0000255}. TOPO_DOM 39 1063 Extracellular. {ECO:0000255}.; TOPO_DOM 1085 1145 Cytoplasmic. {ECO:0000255}. FUNCTION: Probably involved in sperm cell hyperactivation via its association with CATSPER1. Sperm cell hyperactivation is needed for sperm motility which is essential late in the preparation of sperm for fertilization. {ECO:0000269|PubMed:19516020}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}. SUBUNIT: Component of the CatSper complex. {ECO:0000269|PubMed:19516020, ECO:0000269|PubMed:21224844}. TISSUE SPECIFICITY: Testis-specific. Specifically expressed in the principal piece of the sperm tail (at protein level). Expressed in spermatocytes and spermatids within the seminiferous tubule but not in interstitial cells. {ECO:0000269|PubMed:19516020}. +Q65CL1 CTNA3_MOUSE Catenin alpha-3 (Alpha T-catenin) (Cadherin-associated protein) 895 99,803 Chain (1); Coiled coil (2); Modified residue (5); Sequence conflict (4) FUNCTION: May be involved in formation of stretch-resistant cell-cell adhesion complexes. {ECO:0000250|UniProtKB:Q9UI47}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Note=Localizes to intercalated disks of cardiomyocytes and in peritubular myoid cells of testis, and colocalizes with CTNNA1 and CTNNA2. {ECO:0000250}. SUBUNIT: Interacts with CTNNB1. {ECO:0000269|PubMed:11590244}. +Q8K129 CTXN1_MOUSE Cortexin-1 82 9,059 Chain (1); Transmembrane (1) TRANSMEM 30 50 Helical. {ECO:0000255}. FUNCTION: May mediate extracellular or intracellular signaling of cortical neurons during forebrain development. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +A0A1B0GST9 CTXD1_MOUSE Cortexin domain-containing 1 59 6,734 Chain (1); Transmembrane (1) TRANSMEM 17 37 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. +A0A1B0GQX3 CTXD2_MOUSE Cortexin domain containing 2 59 6,518 Chain (1); Transmembrane (1) TRANSMEM 20 40 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. +Q6GQV7 EDRF1_MOUSE Erythroid differentiation-related factor 1 1239 138,834 Chain (1); Erroneous initiation (2); Repeat (2) FUNCTION: Transcription factor involved in erythroid differentiation. Involved in transcriptional activation of the globin gene (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q8VE73 CUL7_MOUSE Cullin-7 (CUL-7) (p185) (p193) 1689 192,292 Alternative sequence (1); Chain (1); Compositional bias (1); Cross-link (1); Domain (1); Region (1); Sequence conflict (8) Protein modification; protein ubiquitination. FUNCTION: Core component of the 3M and Cul7-RING(FBXW8) complexes, which mediates the ubiquitination of target proteins. Core component of the 3M complex, a complex required to regulate microtubule dynamics and genome integrity. It is unclear how the 3M complex regulates microtubules, it could act by controlling the level of a microtubule stabilizer. Interaction with CUL9 is required to inhibit CUL9 activity and ubiquitination of BIRC5. Core component of a Cul7-RING ubiquitin-protein ligase with FBXW8, which mediates ubiquitination and consequent degradation of target proteins such as GORASP1, IRS1 and MAP4K1/HPK1. Ubiquitination of GORASP1 regulates Golgi morphogenesis and dendrite patterning in brain. Mediates ubiquitination and degradation of IRS1 in a mTOR-dependent manner: the Cul7-RING(FBXW8) complex recognizes and binds IRS1 previously phosphorylated by S6 kinase (RPS6KB1 or RPS6KB2). The Cul7-RING(FBXW8) complex also mediates ubiquitination of MAP4K1/HPK1: recognizes and binds autophosphorylated MAP4K1/HPK1, leading to its degradation, thereby affecting cell proliferation and differentiation. Acts as a regulator in trophoblast cell epithelial-mesenchymal transition and placental development. Does not promote polyubiquitination and proteasomal degradation of p53/TP53. While the Cul7-RING(FBXW8) and the 3M complexes are associated and involved in common processes, CUL7 and the Cul7-RING(FBXW8) complex may be have additional functions (By similarity). Probably plays a role in the degradation of proteins involved in endothelial proliferation and/or differentiation. {ECO:0000250, ECO:0000269|PubMed:12904573}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Golgi apparatus {ECO:0000250}. Note=Colocalizes with FBXW8 at the Golgi apparatus in neurons; localization to Golgi is mediated by OBSL1. During mitosis, localizes to the mitotic apparatus. CCDC8 is required for centrosomal location (By similarity). {ECO:0000250}. SUBUNIT: Component of the 3M complex, composed of core components CUL7, CCDC8 and OBSL1. Part of a Cul7-RING complex consisting of CUL7, RBX1, SKP1 and FBXW8. Interacts with a complex of SKP1 and FBXW8, but not with SKP1 alone. Interacts with CUL9; leading to inhibit CUL9 activity. Interacts with FBXW8; interaction is mutually exclusive of binding to CUL9 or p53/TP53. Interacts with p53/TP53; the interaction preferentially involves tetrameric and dimeric p53/TP53. The CUL7-CUL9 heterodimer seems to interact specifically with p53/TP53. Interacts with OBSL1 (By similarity). Interacts with CUL1; the interactions seems to be mediated by FBXW8. Interacts (as part of the 3M complex) with HDAC4 and HDAC5; it is negatively regulated by ANKRA2 (By similarity). {ECO:0000250, ECO:0000269|PubMed:16880526}. +Q3TCH7 CUL4A_MOUSE Cullin-4A (CUL-4A) 759 87,753 Chain (1); Cross-link (3); Modified residue (1); Sequence conflict (1) Protein modification; protein ubiquitination. FUNCTION: Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and is inhibited by the association of the deneddylated cullin subunit with TIP120A/CAND1. The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition component. DCX(DET1-COP1) directs ubiquitination of JUN. DCX(DDB2) directs ubiquitination of XPC. In association with RBX1, DDB1 and DDB2 is required for histone H3 and histone H4 ubiquitination in response to ultraviolet and may be important for subsequent DNA repair. DCX(DTL) plays a role in PCNA-dependent polyubiquitination of CDT1 and MDM2-dependent ubiquitination of TP53 in response to radiation-induced DNA damage and during DNA replication. In association with DDB1 and SKP2 probably is involved in ubiquitination of CDKN1B/p27kip. Is involved in ubiquitination of HOXA9. DCX(DTL) directs autoubiquitination of DTL (By similarity). {ECO:0000250}. PTM: Neddylated. Deneddylated via its interaction with the COP9 signalosome (CSN) complex. {ECO:0000269|PubMed:20190741}.; PTM: (Microbial infection) Deneddylated by murine cytomegalovirus M48 leading to a S-phase-like environment that is required for efficient replication of the viral genome. {ECO:0000269|PubMed:20190741}. SUBUNIT: Component of multiple DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes that seem to consist of DDB1, CUL4A or CUL4B, RBX1 and a variable substrate recognition component which seems to belong to a protein family described as DCAF (Ddb1- and Cul4-associated factor) or CDW (CUL4-DDB1-associated WD40-repeat) proteins. Component of the CSA complex (DCX(ERCC8) complex) containing ERCC8, RBX1, DDB1 and CUL4A; the CSA complex interacts with RNA polymerase II; upon UV irradiation it interacts with the COP9 signalosome and preferentially with the hyperphosphorylated form of RNA polymerase II. Component of the DCX(DET1-COP1) complex with the substrate recognition component DET1 and COP1. Component of the DCX(DDB2) complex with the substrate recognition component DDB2. Component of the DCX(DTL) complex with the putative substrate recognition component DTL. Interacts with DDB1, RBX1, RNF7, CTD1, TIP120A/CAND1, SKP2, CDKN1B, MDM2, TP53 and HOXA9. Interacts with DDB2; the interactions with DDB2 and CAND1 are mutually exclusive. Interacts with DCAF1, DTL, DDA1, DCAF6, DCAF4, DCAF16, DCAF17, DET1, WDTC1, DCAF5, DCAF11, WDR24A, COP1, PAFAH1B1, ERCC8, GRWD1, FBXW5, RBBP7, GNB2, WSB1, WSB2, NUP43, PWP1, FBXW8, ATG16L1, KATNB1, RBBP4, RBBP5, LRWD1 and DCAF8. May interact with WDR26, WDR51B, SNRNP40, WDR61, WDR76, WDR5. Can self-associate. Interacts (when neddylated) with ARIH1; leading to activate the E3 ligase activity of ARIH1. {ECO:0000250|UniProtKB:Q13619}.; SUBUNIT: (Microbial infection) Interacts with murine cytomegalovirus M48. {ECO:0000269|PubMed:20190741}. +Q80X60 EFCB3_MOUSE EF-hand calcium-binding domain-containing protein 3 432 49,710 Calcium binding (1); Chain (1); Domain (2); Modified residue (1) +A0JP43 EFCB5_MOUSE EF-hand calcium-binding domain-containing protein 5 1406 159,935 Alternative sequence (3); Calcium binding (1); Chain (1); Domain (1); Frameshift (2) +Q9DAM2 EFCB9_MOUSE EF-hand calcium-binding domain-containing protein 9 216 26,125 Chain (1); Domain (2); Sequence conflict (1) +Q3V2K1 CX065_MOUSE Uncharacterized protein CXorf65 homolog 191 21,587 Chain (1) +P56392 CX7A1_MOUSE Cytochrome c oxidase subunit 7A1, mitochondrial (Cytochrome c oxidase subunit VIIa-heart) (Cytochrome c oxidase subunit VIIa-H) (Cytochrome c oxidase subunit VIIa-muscle) (Cytochrome c oxidase subunit VIIa-M) 80 8,986 Chain (1); Topological domain (2); Transit peptide (1); Transmembrane (1) TRANSMEM 47 75 Helical. {ECO:0000250}. TOPO_DOM 22 46 Mitochondrial matrix. {ECO:0000250}.; TOPO_DOM 76 80 Mitochondrial intermembrane. {ECO:0000250}. FUNCTION: This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. SUBCELLULAR LOCATION: Mitochondrion inner membrane. +P97792 CXAR_MOUSE Coxsackievirus and adenovirus receptor homolog (CAR) (mCAR) 365 39,948 Alternative sequence (3); Beta strand (15); Chain (1); Disulfide bond (3); Domain (2); Glycosylation (1); Helix (5); Lipidation (2); Modified residue (6); Motif (1); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 238 258 Helical. {ECO:0000255}. TOPO_DOM 20 237 Extracellular. {ECO:0000255}.; TOPO_DOM 259 365 Cytoplasmic. {ECO:0000255}. FUNCTION: Component of the epithelial apical junction complex that may function as a homophilic cell adhesion molecule and is essential for tight junction integrity. Also involved in transepithelial migration of leukocytes through adhesive interactions with JAML a transmembrane protein of the plasma membrane of leukocytes. The interaction between both receptors also mediates the activation of gamma-delta T-cells, a subpopulation of T-cells residing in epithelia and involved in tissue homeostasis and repair. Upon epithelial CXADR-binding, JAML induces downstream cell signaling events in gamma-delta T-cells through PI3-kinase and MAP kinases. It results in proliferation and production of cytokines and growth factors by T-cells that in turn stimulate epithelial tissues repair. {ECO:0000269|PubMed:10814828, ECO:0000269|PubMed:20813954, ECO:0000269|PubMed:9036860, ECO:0000269|PubMed:9420240}. PTM: Palmitoylated on Cys-259 and/or Cys-260; required for proper localization to the plasma membrane. {ECO:0000250}. SUBCELLULAR LOCATION: Isoform 1: Cell membrane {ECO:0000269|PubMed:15533241}; Single-pass type I membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:P78310}; Single-pass type I membrane protein {ECO:0000255}. Cell junction, tight junction {ECO:0000250|UniProtKB:P78310}. Cell junction, adherens junction {ECO:0000250|UniProtKB:P78310}. Note=In epithelial cells localizes to the apical junction complex composed of tight and adherens junctions. In airway epithelial cells localized to basolateral membrane but not to apical surface. {ECO:0000250|UniProtKB:P78310}.; SUBCELLULAR LOCATION: Isoform 3: Secreted {ECO:0000305}. SUBUNIT: Monomer. May form homodimer. Interacts with LNX, BAIAP1, DLG4, PRKCABP, TJP1 and CTNNB1. Interacts with MPDZ; recruits MPDZ to intercellular contact sites. Interacts with JAML (homodimeric form). {ECO:0000269|PubMed:20813954, ECO:0000269|PubMed:20813955}. DOMAIN: The Ig-like C2-type 1 domain mediates homodimerization and interaction with JAML. {ECO:0000269|PubMed:20813955}.; DOMAIN: The PDZ-binding motif mediates interaction with MPDZ and BAIAP1. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in liver, kidney, heart, lung, and brain. In skeletal muscle is found at the neuromuscular junction. In cardiac muscle, isoform 1 and isoform 2 are found at intercalated disks. {ECO:0000269|PubMed:10814828, ECO:0000269|PubMed:12763576, ECO:0000269|PubMed:15533241, ECO:0000269|PubMed:9096397}. +P50228 CXCL5_MOUSE C-X-C motif chemokine 5 (Cytokine LIX) (Small-inducible cytokine B5) [Cleaved into: GCP-2(1-78); GCP-2(9-78)] 132 14,235 Chain (3); Disulfide bond (2); Sequence conflict (5); Signal peptide (1) FUNCTION: May participate in the recruitment of inflammatory cells by injured or infected tissue. GCP-2(1-78) and, more potent, GCP-2(9-78) attract neutrophils and are involved in neutrophil activation. {ECO:0000269|PubMed:10570306}. PTM: GCP-2(1-78) and GCP-2(9-78) are produced by proteolytic cleavage after secretion from fibroblasts and epithelial cells. GCP-2(9-78) is the most prominent form. A number of additional N-terminal (processed between pos. 41 and 48) and C-terminal (processed between pos. 118 and 132) processed forms have been identified, probably also representing intermediate states. {ECO:0000269|PubMed:10570306, ECO:0000269|PubMed:8759763}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Monomer. Homodimer. {ECO:0000250|UniProtKB:P42830}. +Q64448 CXA3_MOUSE Gap junction alpha-3 protein (Connexin-46) (Cx46) 417 46,321 Chain (1); Sequence conflict (3); Topological domain (5); Transmembrane (4) TRANSMEM 20 40 Helical. {ECO:0000255}.; TRANSMEM 77 97 Helical. {ECO:0000255}.; TRANSMEM 159 179 Helical. {ECO:0000255}.; TRANSMEM 208 228 Helical. {ECO:0000255}. TOPO_DOM 1 19 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 41 76 Extracellular. {ECO:0000255}.; TOPO_DOM 98 158 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 180 207 Extracellular. {ECO:0000255}.; TOPO_DOM 229 417 Cytoplasmic. {ECO:0000255}. FUNCTION: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell junction, gap junction. "SUBUNIT: A connexon is composed of a hexamer of connexins. This particular connexin is a component of lens fiber gap junctions, can form both junctional and non-junctional (""hemi-"") channels." +P70689 CXB6_MOUSE Gap junction beta-6 protein (Connexin-30) (Cx30) 261 30,366 Chain (1); Topological domain (5); Transmembrane (4) TRANSMEM 23 45 Helical. {ECO:0000255}.; TRANSMEM 76 98 Helical. {ECO:0000255}.; TRANSMEM 132 154 Helical. {ECO:0000255}.; TRANSMEM 193 215 Helical. {ECO:0000255}. TOPO_DOM 1 22 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 46 75 Extracellular. {ECO:0000255}.; TOPO_DOM 99 131 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 155 192 Extracellular. {ECO:0000255}.; TOPO_DOM 216 261 Cytoplasmic. {ECO:0000255}. FUNCTION: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell junction, gap junction. SUBUNIT: A connexon is composed of a hexamer of connexins. Interacts with CNST. {ECO:0000269|PubMed:19864490}. TISSUE SPECIFICITY: Highly expressed in adult brain and skin. Less in uterus, lung and eye. Very low in testis and sciatic nerve. No expression before birth. +Q8R2G6 CCD80_MOUSE Coiled-coil domain-containing protein 80 (Up-regulated in BRS-3 deficient mouse) 949 107,613 Chain (1); Coiled coil (1); Compositional bias (2); Cross-link (2); Erroneous initiation (1); Frameshift (3); Glycosylation (1); Sequence conflict (22); Signal peptide (1) FUNCTION: Promotes cell adhesion and matrix assembly. {ECO:0000269|PubMed:18757743}. PTM: Phosphorylated. {ECO:0000269|PubMed:15325258}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:15325258, ECO:0000269|PubMed:18757743}. SUBUNIT: Binds to various extracellular matrix proteins. {ECO:0000269|PubMed:18757743}. TISSUE SPECIFICITY: Expressed in brain, stomach, colon, rectum, liver, lung, kidney, adipocytes and testis. +D3YZP9 CCDC6_MOUSE Coiled-coil domain-containing protein 6 469 52,939 Chain (1); Coiled coil (1); Compositional bias (1); Initiator methionine (1); Modified residue (14); Motif (1); Region (1); Repeat (5) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=May be a cytoskeletal protein. {ECO:0000250}. DOMAIN: The protein has mostly an alpha helical conformation similar to myosin heavy-chain tail that might adopt a coiled-coil conformation. {ECO:0000250}. +Q6NS45 CCD66_MOUSE Coiled-coil domain-containing protein 66 935 107,372 Alternative sequence (3); Chain (1); Coiled coil (1); Erroneous initiation (3); Frameshift (1); Modified residue (3); Sequence caution (1); Sequence conflict (2) FUNCTION: Microtubule-binding protein required for ciliogenesis. May function in ciliogenesis by mediating the transport of proteins like BBS4 to the cilium, but also through the organization of the centriolar satellites (By similarity). Plays a role in retina morphogenesis and/or homeostasis (PubMed:21680557). {ECO:0000250|UniProtKB:A2RUB6, ECO:0000269|PubMed:21680557}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:A2RUB6}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000250|UniProtKB:A2RUB6}. Cell projection, cilium {ECO:0000250|UniProtKB:A2RUB6}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:A2RUB6}. Photoreceptor inner segment {ECO:0000269|PubMed:19777273}. Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:19777273}. Note=Restricted to the centrosomes and the spindle microtubules during mitosis (By similarity). Enriched in the inner segment of the photoreceptor (PubMed:19777273). {ECO:0000250|UniProtKB:A2RUB6, ECO:0000269|PubMed:19777273}. SUBUNIT: Homodimer; disulfide-linked (Probable). Interacts with CEP290. Interacts with PCM1 (By similarity). {ECO:0000250|UniProtKB:A2RUB6, ECO:0000305|PubMed:19777273}. TISSUE SPECIFICITY: Widely expressed (PubMed:19777273). Expressed in retina by rod photoreceptors but also detected in outer plexiform and ganglion cell layers (at protein level) (PubMed:21680557, PubMed:19777273). {ECO:0000269|PubMed:19777273, ECO:0000269|PubMed:21680557}. +Q9D024 CCD47_MOUSE Coiled-coil domain-containing protein 47 (Adipocyte-specific protein 4) 483 55,844 Alternative sequence (2); Chain (1); Coiled coil (1); Glycosylation (1); Sequence conflict (3); Signal peptide (1); Transmembrane (1) TRANSMEM 136 156 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q8K2Y9 CCM2_MOUSE Cerebral cavernous malformations protein 2 homolog (Malcavernin) (Osmosensing scaffold for MEKK3) 453 49,917 Alternative sequence (2); Chain (1); Domain (1); Modified residue (7); Region (1) FUNCTION: Component of the CCM signaling pathway which is a crucial regulator of heart and vessel formation and integrity. May act through the stabilization of endothelial cell junctions. May also function as a scaffold protein for MAP2K3-MAP3K3 signaling. Seems to play a major role in the modulation of MAP3K3-dependent p38 activation induced by hyperosmotic shock. {ECO:0000269|PubMed:14634666, ECO:0000269|PubMed:19151727}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14634666}. Note=Treatment with sorbitol caused relocalization to ruffle-like structures. SUBUNIT: Part of a complex with MAP2K3, MAP3K3 and RAC1. Binds RAC1 directly and independently of its nucleotide-bound state. Interacts with PDCD10 (By similarity). Interacts with HEG1 and KRIT1; KRIT1 greatly facilitates the interaction with HEG1. {ECO:0000250, ECO:0000269|PubMed:14634666, ECO:0000269|PubMed:19151727}. DOMAIN: The C-terminal region constitutes an independently folded domain that has structural similarity with the USH1C (harmonin) N-terminus, despite very low sequence similarity. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in heart, lower expression in kidney, lung and liver (at protein level). {ECO:0000269|PubMed:14634666}. +Q7TQK5 CCD93_MOUSE Coiled-coil domain-containing protein 93 629 72,603 Chain (1); Coiled coil (2); Modified residue (3); Region (2); Sequence conflict (2) FUNCTION: Involved in copper-dependent ATP7A trafficking between the trans-Golgi network and vesicles in the cell periphery; the function is proposed to depend on its association within the CCC complex and cooperation with the WASH complex on early endosomes and is dependent on its interaction with WASHC2. {ECO:0000250|UniProtKB:Q567U6}. SUBCELLULAR LOCATION: Early endosome {ECO:0000250|UniProtKB:Q567U6}. SUBUNIT: Interacts with COMMD1, COMMD2 COMMD3, COMMD4, COMMD5, COMMD6, COMMD7, COMMD8, COMMD9, COMMD10, WASHC1. Interacts directly with WASHC2. Interacts with CCDC93 and C16orf62 homolog; proposed to be a component of the CCC (COMMD/CCDC22/CCDC93) complex which contains at least COMMD1 (and possibly other COMM domain-containing proteins), CCDC22, CCDC93 and C16orf62 homolog; in the complex interacts directly with CCDC22. {ECO:0000250|UniProtKB:Q567U6}. +Q8C0C4 CCSE1_MOUSE Serine-rich coiled-coil domain-containing protein 1 (Coiled-coil serine-rich protein 1) 895 98,217 Alternative sequence (4); Chain (1); Coiled coil (1); Compositional bias (1); Erroneous initiation (1); Sequence conflict (1) +Q8BGU5 CCNY_MOUSE Cyclin-Y (Cyclin fold protein 1) 341 39,395 Alternative sequence (1); Chain (1); Domain (1); Initiator methionine (1); Lipidation (1); Modified residue (18); Sequence conflict (1) FUNCTION: Positive regulatory subunit of the cyclin-dependent kinase CDK14/PFTK1. Acts as a cell-cycle regulator of Wnt signaling pathway during G2/M phase by recruiting CDK14/PFTK1 to the plasma membrane and promoting phosphorylation of LRP6, leading to the activation of the Wnt signaling pathway (By similarity). Recruits CDK16 to the plasma membrane (By similarity). Positive regulatory subunit of the cyclin-dependent kinase CDK16. {ECO:0000250, ECO:0000269|PubMed:22184064}. PTM: Ubiquitinated; leading to its degradation. {ECO:0000250}.; PTM: Heavily phosphorylated. Phosphorylation at Ser-71 and Ser-73 by CDK14 is enhanced during the G2 and M cell cycle phases, and creates a phosphodegron triggering SCF-dependent ubiquitination. {ECO:0000250|UniProtKB:Q8ND76}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. SUBUNIT: Found in a complex with CAPRIN2, LRP6 AND CDK14 during G2/M stage; CAPRIN2 functions as a scaffold for the complex by binding to CCNY via its N terminus and to CDK14 via its C terminus (By similarity). Interacts with CDK14 (By similarity). Interacts with CDK16 (PubMed:22184064). Interacts with LRP6 (By similarity). {ECO:0000250|UniProtKB:Q8ND76, ECO:0000269|PubMed:22184064}. TISSUE SPECIFICITY: Detected in brain, heart, lung, skeletal muscle, ovary, thymus and testis (at protein level). {ECO:0000269|PubMed:22184064}. +Q61451 CD53_MOUSE Leukocyte surface antigen CD53 (Cell surface glycoprotein CD53) (CD antigen CD53) 219 24,164 Chain (1); Glycosylation (3); Topological domain (5); Transmembrane (4) TRANSMEM 12 32 Helical. {ECO:0000255}.; TRANSMEM 55 69 Helical. {ECO:0000255}.; TRANSMEM 81 106 Helical. {ECO:0000255}.; TRANSMEM 182 206 Helical. {ECO:0000255}. TOPO_DOM 1 11 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 33 54 Extracellular. {ECO:0000255}.; TOPO_DOM 70 80 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 107 181 Extracellular. {ECO:0000255}.; TOPO_DOM 207 219 Cytoplasmic. {ECO:0000255}. FUNCTION: Required for efficient formation of myofibers in regenerating muscle at the level of cell fusion. May be involved in growth regulation in hematopoietic cells. {ECO:0000269|PubMed:22847234}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22847234}. Cell junction {ECO:0000269|PubMed:22847234}. Membrane {ECO:0000269|PubMed:22847234}; Multi-pass membrane protein {ECO:0000269|PubMed:22847234}. Note=Concentrates in localized microdomains along the plasma membrane at the contact sites between cells of fused myotubes. SUBUNIT: Interacts with SCIMP. {ECO:0000250}. +Q08857 CD36_MOUSE Platelet glycoprotein 4 (Glycoprotein IIIb) (GPIIIB) (PAS IV) (PAS-4) (Platelet glycoprotein IV) (GPIV) (CD antigen CD36) 472 52,698 Chain (1); Cross-link (2); Disulfide bond (3); Glycosylation (8); Lipidation (4); Region (2); Site (1); Topological domain (3); Transmembrane (2) TRANSMEM 8 29 Helical. {ECO:0000255}.; TRANSMEM 440 461 Helical. {ECO:0000255}. TOPO_DOM 1 7 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 30 439 Extracellular. {ECO:0000255}.; TOPO_DOM 462 472 Cytoplasmic. {ECO:0000255}. FUNCTION: Multifunctional glycoprotein that acts as receptor for a broad range of ligands. Ligands can be of proteinaceous nature like thrombospondin, fibronectin, collagen or amyloid-beta as well as of lipidic nature such as oxidized low-density lipoprotein (oxLDL), anionic phospholipids, long-chain fatty acids and bacterial diacylated lipopeptides (PubMed:7685021). They are generally multivalent and can therefore engage multiple receptors simultaneously, the resulting formation of CD36 clusters initiates signal transduction and internalization of receptor-ligand complexes. The dependency on coreceptor signaling is strongly ligand specific. Cellular responses to these ligands are involved in angiogenesis, inflammatory response, fatty acid metabolism, taste and dietary fat processing in the intestine (Probable) (PubMed:19847289, PubMed:20037584, PubMed:23395392). Binds long-chain fatty acids and facilitates their transport into cells, thus participating in muscle lipid utilization, adipose energy storage, and gut fat absorption (By similarity). In the small intestine, plays a role in proximal absorption of dietary fatty acid and cholesterol for optimal chylomicron formation, possibly through the activation of MAPK1/3 (ERK1/2) signaling pathway (By similarity) (PubMed:17507371, PubMed:18753675, PubMed:21610069). Involved in oral fat perception and preferences (PubMed:16276419). Detection into the tongue of long-chain fatty acids leads to a rapid and sustained rise in flux and protein content of pancreatobiliary secretions (By similarity) (PubMed:16276419). In taste receptor cells, mediates the induction of an increase in intracellular calcium levels by long-chain fatty acids, leading to the activation of the gustatory neurons in the nucleus of the solitary tract (PubMed:18162488). Important factor in both ventromedial hypothalamus neuronal sensing of long-chain fatty acid and the regulation of energy and glucose homeostasis (By similarity) (PubMed:23557700). Receptor for thombospondins, THBS1 and THBS2, mediating their antiangiogenic effects (PubMed:15748999). As a coreceptor for TLR4:TLR6 heterodimer, promotes inflammation in monocytes/macrophages. Upon ligand binding, such as oxLDL or amyloid-beta 42, interacts with the heterodimer TLR4:TLR6, the complex is internalized and triggers inflammatory response, leading to NF-kappa-B-dependent production of CXCL1, CXCL2 and CCL9 cytokines, via MYD88 signaling pathway, and CCL5 cytokine, via TICAM1 signaling pathway, as well as IL1B secretion, through the priming and activation of the NLRP3 inflammasome (PubMed:20037584, PubMed:23812099). Selective and nonredundant sensor of microbial diacylated lipopeptide that signal via TLR2:TLR6 heterodimer, this cluster triggers signaling from the cell surface, leading to the NF-kappa-B-dependent production of TNF, via MYD88 signaling pathway and subsequently is targeted to the Golgi in a lipid-raft dependent pathway (By similarity) (PubMed:15690042, PubMed:19847289). {ECO:0000250|UniProtKB:P16671, ECO:0000250|UniProtKB:Q07969, ECO:0000269|PubMed:15690042, ECO:0000269|PubMed:15748999, ECO:0000269|PubMed:16276419, ECO:0000269|PubMed:17507371, ECO:0000269|PubMed:18162488, ECO:0000269|PubMed:18753675, ECO:0000269|PubMed:19847289, ECO:0000269|PubMed:20037584, ECO:0000269|PubMed:21610069, ECO:0000269|PubMed:23395392, ECO:0000269|PubMed:23557700, ECO:0000269|PubMed:23812099, ECO:0000269|PubMed:7685021, ECO:0000305|PubMed:19471024}.; FUNCTION: (Microbial infection) Acts as an accessory receptor for M.tuberculosis lipoprotein LprA, in conjunction with coreceptors TLR2 and TLR1; the lipoprotein acts as an agonist to modulate antigen presenting cell functions in response to the pathogen (PubMed:19362712). Directly mediates cytoadherence of Plasmodium falciparum parasitized erythrocytes and the internalization of particles independently of TLR signaling (PubMed:19864601, PubMed:23395392). Mediates uptake of E.coli and S.aureus but has no effect on uptake of M.fortuitum (PubMed:16020694). {ECO:0000269|PubMed:16020694, ECO:0000269|PubMed:19362712, ECO:0000269|PubMed:19864601, ECO:0000269|PubMed:23395392}. PTM: Ubiquitinated at Lys-469 and Lys-472. Ubiquitination is induced by fatty acids such as oleic acid and leads to degradation by the proteasome (PubMed:21610069, PubMed:18353783). Ubiquitination and degradation are inhibited by insulin which blocks the effect of fatty acids (PubMed:18353783). {ECO:0000269|PubMed:18353783, ECO:0000269|PubMed:21610069}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23395392}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:16276419, ECO:0000269|PubMed:21610069}. Membrane raft {ECO:0000250|UniProtKB:P16671}. Golgi apparatus {ECO:0000250|UniProtKB:P16671}. Note=Upon ligand-binding, internalized through dynamin-dependent endocytosis. {ECO:0000250|UniProtKB:P16671}. SUBUNIT: Interacts with THBS1 and THBS2; the interactions mediate the THBS antiangiogenic activity (By similarity) (PubMed:15748999). Upon interaction with a ligand, such as oxidized low-density lipoprotein (oxLDL) or amyloid-beta 42, rapidly forms a complex with TLR4 and TLR6; the complex is internalized and triggers an inflammatory signal. Through its C-terminus, interacts with PTK2, PXN and LYN, but not with SRC. LYN kinase activity is required for facilitating TLR4-TLR6 heterodimerization and signal initiation (By similarity). Interacts with CD9, CD81, FCER1G, ITGB2 and/or ITGB2; forming a membrane heteromeric complex required for the internalization of CD36 and its ligands (PubMed:23395392). {ECO:0000250|UniProtKB:P16671, ECO:0000269|PubMed:15748999, ECO:0000269|PubMed:23395392}. TISSUE SPECIFICITY: Expressed in the apical side of lingual taste bud cells of the circumvallate papillae (PubMed:16276419, PubMed:21901153). Highly expressed in the intestine on the luminal surface of enterocytes. In small intestines expression levels follow a steep decreasing gradient from proximal to distal segments (PubMed:17507371). Expressed in macrophages (PubMed:23395392, PubMed:23812099). Cell surface expression detected in lung alveolar macrophages, dendritic macrophages and lung macrophages (at protein level) (PubMed:19362712). {ECO:0000269|PubMed:16276419, ECO:0000269|PubMed:17507371, ECO:0000269|PubMed:19362712, ECO:0000269|PubMed:21901153, ECO:0000269|PubMed:23395392, ECO:0000269|PubMed:23812099}. +P11610 CD1D2_MOUSE Antigen-presenting glycoprotein CD1d2 (CD antigen CD1d.2) 336 38,477 Beta strand (13); Binding site (3); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (5); Helix (7); Motif (1); Region (1); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (3) TRANSMEM 306 326 Helical. {ECO:0000255}. TOPO_DOM 22 305 Extracellular. {ECO:0000255}.; TOPO_DOM 327 336 Cytoplasmic. {ECO:0000255}. FUNCTION: Antigen-presenting protein that binds self and non-self glycolipids and presents them to T-cell receptors on natural killer T-cells. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P11609}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P11609}. Endosome membrane {ECO:0000250|UniProtKB:P11609}. Lysosome membrane {ECO:0000250|UniProtKB:P11609}. Note=Subject to intracellular trafficking between the cell membrane, endosomes and lysosomes. {ECO:0000250|UniProtKB:P11609}. SUBUNIT: Heterodimer with B2M (beta-2-microglobulin). Interacts with MHC II and CD74. TISSUE SPECIFICITY: Expressed on cortical thymocytes, on certain T-cell leukemias, and in various other tissues. +P31041 CD28_MOUSE T-cell-specific surface glycoprotein CD28 (CD antigen CD28) 218 25,243 Beta strand (1); Chain (1); Disulfide bond (2); Domain (1); Glycosylation (4); Modified residue (3); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 151 177 Helical. {ECO:0000255}. TOPO_DOM 20 150 Extracellular. {ECO:0000255}.; TOPO_DOM 178 218 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in T-cell activation, the induction of cell proliferation and cytokine production and promotion of T-cell survival. Enhances the production of IL4 and IL10 in T-cells in conjunction with TCR/CD3 ligation and CD40L costimulation. {ECO:0000250|UniProtKB:P10747}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Homodimer; disulfide-linked. Interacts with DUSP14. Binds to CD80/B7-1 and CD86/B7-2/B70. Interacts with GRB2 (By similarity). {ECO:0000250}. +P01731 CD8A_MOUSE T-cell surface glycoprotein CD8 alpha chain (T-cell surface glycoprotein Lyt-2) (CD antigen CD8a) 247 27,456 Beta strand (12); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (3); Helix (2); Natural variant (1); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (2) TRANSMEM 197 217 Helical. {ECO:0000255}. TOPO_DOM 28 196 Extracellular. {ECO:0000255}.; TOPO_DOM 218 247 Cytoplasmic. {ECO:0000255}. FUNCTION: Integral membrane glycoprotein that plays an essential role in the immune response and serves multiple functions in responses against both external and internal offenses. In T-cells, functions primarily as a coreceptor for MHC class I molecule:peptide complex. The antigens presented by class I peptides are derived from cytosolic proteins while class II derived from extracellular proteins. Interacts simultaneously with the T-cell receptor (TCR) and the MHC class I proteins presented by antigen presenting cells (APCs). In turn, recruits the Src kinase LCK to the vicinity of the TCR-CD3 complex. LCK then initiates different intracellular signaling pathways by phosphorylating various substrates ultimately leading to lymphokine production, motility, adhesion and activation of cytotoxic T-lymphocytes (CTLs). This mechanism enables CTLs to recognize and eliminate infected cells and tumor cells. In NK-cells, the presence of CD8A homodimers at the cell surface provides a survival mechanism allowing conjugation and lysis of multiple target cells. CD8A homodimer molecules also promote the survival and differentiation of activated lymphocytes into memory CD8 T-cells. {ECO:0000250|UniProtKB:P01732, ECO:0000269|PubMed:15105501, ECO:0000269|PubMed:1673361}. PTM: Palmitoylated, but association with CD8B seems to be more important for the enrichment of CdD8A in lipid rafts. {ECO:0000250|UniProtKB:P01732}.; PTM: Phosphorylated in cytotoxic T-lymphocytes (CTLs) following activation. {ECO:0000269|PubMed:2512251}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P01732}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P01732}. Note=Cd8a localizes to lipid rafts only when associated with its partner Cd8b. {ECO:0000250|UniProtKB:P01732}. SUBUNIT: Forms disulfide-linked heterodimers with CD8B at the cell surface. Forms also homodimers in several cell types including NK-cells or peripheral blood T-lymphocytes. Interacts with the MHC class I HLA-A/B2M dimer. Interacts with LCK in a zinc-dependent manner. {ECO:0000250|UniProtKB:P01732, ECO:0000269|PubMed:18929574, ECO:0000269|PubMed:9806638}. +Q8JZM7 CDC73_MOUSE Parafibromin (Cell division cycle protein 73 homolog) (Hyperparathyroidism 2 protein homolog) 531 60,577 Chain (1); Compositional bias (1); Cross-link (4); Initiator methionine (1); Modified residue (2); Motif (1); Region (2) FUNCTION: Tumor suppressor probably involved in transcriptional and post-transcriptional control pathways. May be involved in cell cycle progression through the regulation of cyclin D1/PRAD1 expression. Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and is involved in transcriptional elongation, acting both indepentently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1. PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B ubiquitination is proposed to be coupled to transcription. PAF1C is involved in mRNA 3' end formation probably through association with cleavage and poly(A) factors. Connects PAF1C with the cleavage and polyadenylation specificity factor (CPSF) complex and the cleavage stimulation factor (CSTF) complex, and with Wnt signaling. Involved in polyadenylation of mRNA precursors (By similarity). {ECO:0000250, ECO:0000269|PubMed:19345177}. PTM: Phosphorylated. Dephosphorylated by PTPN11. {ECO:0000250|UniProtKB:Q6P1J9}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the PAF1 complex, which consists of CDC73, PAF1, LEO1, CTR9, RTF1 and WDR61. The PAF1 complex interacts with PHF5A (PubMed:27749823). Within the PAF1 complex interacts directly with PHF5A (PubMed:27749823). Interacts with POLR2A, CPSF1, CPSF4, CSTF2, KMT2A/MLL1 and CTNNB1. Interacts with a Set1-like complex that has histone methyltransferase activity and methylates histone H3. Found in a complex with BCL9L or BCL9, CDC73, CTNNB1 and PYGO1 indicative for the participation in a nuclear Wnt signaling complex. Interacts with PTPN11 (By similarity). Interacts with SETD5 (PubMed:27864380). {ECO:0000250|UniProtKB:Q6P1J9, ECO:0000269|PubMed:27749823, ECO:0000269|PubMed:27864380}. TISSUE SPECIFICITY: Found in the adrenal gland, kidney, heart, ovary and liver. {ECO:0000269|PubMed:15580289}. +P30285 CDK4_MOUSE Cyclin-dependent kinase 4 (EC 2.7.11.22) (CRK3) (Cell division protein kinase 4) (PSK-J3) 303 33,751 Active site (1); Binding site (1); Chain (1); Domain (1); Initiator methionine (1); Modified residue (3); Nucleotide binding (1); Region (1) FUNCTION: Ser/Thr-kinase component of cyclin D-CDK4 (DC) complexes that phosphorylate and inhibit members of the retinoblastoma (RB) protein family including RB1 and regulate the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complexes and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also phosphorylates SMAD3 in a cell-cycle-dependent manner and represses its transcriptional activity. Component of the ternary complex, cyclin D/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex (By similarity). {ECO:0000250}. PTM: Phosphorylation at Thr-172 is required for enzymatic activity. Phosphorylated, in vitro, at this site by CCNH-CDK7, but, in vivo, appears to be phosphorylated by a proline-directed kinase. In the cyclin D-CDK4-CDKN1B complex, this phosphorylation and consequent CDK4 enzyme activity, is dependent on the tyrosine phosphorylation state of CDKN1B. Thus, in proliferating cells, CDK4 within the complex is phosphorylated on Thr-172 in the T-loop. In resting cells, phosphorylation on Thr-172 is prevented by the non-tyrosine-phosphorylated form of CDKN1B (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Membrane {ECO:0000250}. Note=Cytoplasmic when non-complexed. Forms a cyclin D-CDK4 complex in the cytoplasm as cells progress through G(1) phase. The complex accumulates on the nuclear membrane and enters the nucleus on transition from G(1) to S phase. Also present in nucleoli and heterochromatin lumps. Colocalizes with RB1 after release into the nucleus (By similarity). {ECO:0000250}. SUBUNIT: Component of the D-CDK4 complex, composed of CDK4 and some D-type G1 cyclin (CCND1, CCND2 or CCND3). Interacts directly in the complex with CCND1, CCND2 or CCND3. Interacts with ZNF655. Forms a ternary complex, cyclin D-CDK4-CDKN1B, involved in modulating CDK4 enzymatic activity. Interacts directly with CDKN1B (phosphorylated on 'Tyr-88' and 'Tyr-89'); the interaction allows assembly of the cyclin D-CDK4 complex, Thr-172 phosphorylation, nuclear translocation and enhances the cyclin D-CDK4 complex activity. CDK4 activity is either inhibited or enhanced depending on stoichiometry of complex. The non-tyrosine-phosphorylated form of CDKN1B prevents T-loop phosphorylation of CDK4 producing inactive CDK4. Interacts (unphosphorylated form) with CDK2. Also forms ternary complexes with CDKN1A or CDKN2A. Interacts directly with CDKN1A (via its N-terminal); the interaction promotes the assembly of the cyclin D-CDK4 complex, its nuclear translocation and promotes the cyclin D-dependent enzyme activity of CDK4. Interacts with CCND1; the interaction is prevented with the binding of CCND1 to INSM1 during cell cycle progression (By similarity). Interacts with SEI1 and CCND1. Probably forms a complex composed of chaperones HSP90 and HSP70, co-chaperones CDC37, PPP5C, TSC1 and client protein TSC2, CDK4, AKT, RAF1 and NR3C1; this complex does not contain co-chaperones STIP1/HOP and PTGES3/p23 (By similarity). Interacts with CEBPA (when phosphorylated) (PubMed:15107404). Interacts with FNIP1 and FNIP2 (By similarity). {ECO:0000250|UniProtKB:P11802, ECO:0000269|PubMed:10580009, ECO:0000269|PubMed:15107404, ECO:0000269|PubMed:19767775}. +Q9DA64 CDRT4_MOUSE CMT1A duplicated region transcript 4 protein homolog 179 20,473 Chain (1); Sequence conflict (2) +P98191 CDS1_MOUSE Phosphatidate cytidylyltransferase 1 (EC 2.7.7.41) (CDP-DAG synthase 1) (CDP-DG synthase 1) (CDP-diacylglycerol synthase 1) (CDS 1) (CDP-diglyceride pyrophosphorylase 1) (CDP-diglyceride synthase 1) (CTP:phosphatidate cytidylyltransferase 1) 461 52,875 Chain (1); Modified residue (3); Transmembrane (6) TRANSMEM 96 116 Helical. {ECO:0000255}.; TRANSMEM 149 169 Helical. {ECO:0000255}.; TRANSMEM 183 203 Helical. {ECO:0000255}.; TRANSMEM 230 250 Helical. {ECO:0000255}.; TRANSMEM 279 299 Helical. {ECO:0000255}.; TRANSMEM 357 377 Helical. {ECO:0000255}. Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3. FUNCTION: Provides CDP-diacylglycerol, an important precursor for the synthesis of phosphatidylinositol (PtdIns), phosphatidylglycerol, and cardiolipin. Overexpression may amplify cellular signaling responses from cytokines. May also play an important role in the signal transduction mechanism of retina and neural cells (By similarity). {ECO:0000250, ECO:0000269|PubMed:9407135}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Cytoplasmic aspect of the endoplasmic reticulum. {ECO:0000250}. SUBUNIT: Interacts with FOS; this interaction may enhance catalytic activity. {ECO:0000269|PubMed:22105363}. TISSUE SPECIFICITY: Highly expressed in the inner segment of the photoreceptor layer of adult retina. {ECO:0000269|PubMed:9889000}. +Q8CC36 CDNF_MOUSE Cerebral dopamine neurotrophic factor (ARMET-like protein 1) (Conserved dopamine neurotrophic factor) 187 21,032 Chain (1); Disulfide bond (3); Signal peptide (1) FUNCTION: Trophic factor for dopamine neurons. Prevents the 6-hydroxydopamine (6-OHDA)-induced degeneration of dopaminergic neurons. When administered after 6-OHDA-lesioning, restores the dopaminergic function and prevents the degeneration of dopaminergic neurons in substantia nigra (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17611540}. TISSUE SPECIFICITY: Expressed at high levels in the heart, skeletal muscle, testis and brain (at protein level). In the brain, detected in the cerebral cortex neurons through layers II to VI. In the hippocampus, detected in the CA1 to CA3 pyramidal regions and in the granule and polymorph layers of dentate gyrus. Weak expression in the striatum. In substantia nigra, detected in solitary cells that did not express tyrosine hydroxylase, a marker for dopaminergic neurons. Relatively high expression in the Purkinje cells of the cerebellum and in regions of the brain stem, including the locus coeruleus. {ECO:0000269|PubMed:17611540}. +Q9D5D8 CDYL2_MOUSE Chromodomain Y-like protein 2 (CDY-like 2) 503 56,142 Chain (1); Domain (1) SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18450745}. SUBUNIT: Interacts (via chromo domain) with histone H3K9me3. {ECO:0000269|PubMed:18450745}. +Q8R3L8 CDK8_MOUSE Cyclin-dependent kinase 8 (EC 2.7.11.22) (EC 2.7.11.23) (Cell division protein kinase 8) (Mediator complex subunit CDK8) (Mediator of RNA polymerase II transcription subunit CDK8) 464 53,210 Active site (1); Alternative sequence (3); Binding site (1); Chain (1); Compositional bias (1); Domain (1); Nucleotide binding (1); Region (1) FUNCTION: Component of the Mediator complex, a coactivator involved in regulated gene transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. Phosphorylates the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNAp II), which may inhibit the formation of a transcription initiation complex. Phosphorylates CCNH leading to down-regulation of the TFIIH complex and transcriptional repression. Recruited through interaction with MAML1 to hyperphosphorylate the intracellular domain of NOTCH, leading to its degradation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Component of the Mediator complex, which is composed of MED1, MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L, MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23, MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8 subunits form a distinct module termed the CDK8 module. Mediator containing the CDK8 module is less active than Mediator lacking this module in supporting transcriptional activation. Individual preparations of the Mediator complex lacking one or more distinct subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and TRAP. The cylin/CDK pair formed by CCNC/CDK8 also associates with the large subunit of RNA polymerase II. Interacts with CTNNB1, GLI3 and MAML1 (By similarity). {ECO:0000250}. +Q810P3 CDKN3_MOUSE Cyclin-dependent kinase inhibitor 3 (EC 3.1.3.16) (EC 3.1.3.48) (CDK2-associated dual-specificity phosphatase) (Kinase-associated phosphatase) 211 23,793 Active site (1); Chain (1); Region (1); Sequence caution (2) FUNCTION: May play a role in cell cycle regulation. Dual specificity phosphatase active toward substrates containing either phosphotyrosine or phosphoserine residues. Dephosphorylates CDK2 at 'Thr-160' in a cyclin-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q16667}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q16667}. SUBUNIT: Interacts with cyclin-dependent kinases such as CDK1, CDK2 and CDK3. Does not interact with CDK4. Interacts (via C-terminus) with phosphorylated CDK2 (via C-terminal helix). Interacts with MS4A3 (via C-terminus); the interaction enhances CDKN3 enzymatic activity (By similarity). {ECO:0000250|UniProtKB:Q16667}. +Q9CR34 CE052_MOUSE Uncharacterized protein C5orf52 homolog 168 19,722 Alternative sequence (1); Chain (1); Erroneous initiation (1) +A2A6T1 CDR2L_MOUSE Cerebellar degeneration-related protein 2-like 465 53,213 Chain (1); Coiled coil (4); Modified residue (4) +P97817 CDR2_MOUSE Cerebellar degeneration-related protein 2 455 52,090 Chain (1); Coiled coil (2); Modified residue (1); Sequence conflict (1) TISSUE SPECIFICITY: Expressed in brain and testis (at protein level). Expressed in the cerebellum, cerebral cortex, heart, lung, spleen, ovary, kidney and testis. {ECO:0000269|PubMed:9006982}. +Q925P2 CEAM2_MOUSE Carcinoembryonic antigen-related cell adhesion molecule 2 (CEA-related cell adhesion molecule 2) (Biliary glycoprotein 2) (BGP-2) 520 57,202 Alternative sequence (2); Chain (1); Disulfide bond (3); Domain (4); Glycosylation (16); Modified residue (3); Sequence conflict (9); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 423 443 Helical. {ECO:0000255}. TOPO_DOM 35 422 Extracellular. {ECO:0000255}.; TOPO_DOM 444 520 Cytoplasmic. {ECO:0000255}. FUNCTION: Controls energy balance and peripheral insulin action. Involved in the regulation of feeding behavior particularly in the ventromedial nucleus of hypothalamus (VMH) regulation of food intake. Has a role in the regulation of metabolic rate and insulin sensitivity or resistance via effects on brown adipogenesis, sympathetic nervous outflow to brown adipose tissue, spontaneous activity and energy expenditure in skeletal muscle. In case of murine coronavirus (MHV) infection, does probably not serve as functional receptor for the virus.; FUNCTION: Isoform 2 may be an adhesion molecule contributing to cell to cell adhesion between elongating spermatids and Sertoli cells within the seminiferous epithelium. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23070997}; Single-pass type I membrane protein {ECO:0000269|PubMed:23070997}. Note=Localizes to sites on the plasma membrane of elongating spermatids where Sertoli cells make contact. SUBUNIT: Interacts weakly with MHV spike protein in tissue culture. {ECO:0000269|PubMed:8207827, ECO:0000269|PubMed:9696818}. TISSUE SPECIFICITY: Isoform 2 is detected in elongating spermatids within the seminiferous epithelium (at protein level). Expressed in kidney, colon, uterus, gut mononuclear cells, crypt epithelia of intestinal tissues, and to a lesser extent, in spleen. Expressed in brain including VMH, globus pallidus, ventral pallidum, striatum, olfactory bulb and hippocampus. Also detected in rectal carcinoma cell line CMT93. Isoform 2 and isoform 3 are expressed in testis. Isoform 2 is detected in seminiferous tubule, not detected in epididymal spermatozoa. Also not observed on spermatogonia, spermatocytes, round spermatids or somatic Sertoli cells. During stages I-VII of spermatogenesis, detected on the elongating spermatids. At spermiation (stage VIII) and subsequent stages IX-XII, levels are drastically reduced or absent in the seminiferous tubules. Sometimes weakly detected in the apical region of stage-VIII seminiferous epithelium. Isoform 2 level is very low in stomach, kidney, intestine, liver and spleen. {ECO:0000269|PubMed:10491101, ECO:0000269|PubMed:11284729, ECO:0000269|PubMed:20381490, ECO:0000269|PubMed:23070997, ECO:0000269|PubMed:8207827}. +Q61400 CEAMA_MOUSE Carcinoembryonic antigen-related cell adhesion molecule 10 (CEA-related cell adhesion molecule 10) (CEA10) (Carcinoembryonic antigen 10) 265 29,474 Chain (1); Domain (2); Glycosylation (3); Sequence conflict (2); Signal peptide (1); Site (1) FUNCTION: May interact with other CEACAM proteins on the sperm surface. {ECO:0000269|PubMed:15901639}. SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000269|PubMed:15901639}. TISSUE SPECIFICITY: Abundant in seminal vesicle and traces in epididymis and prostate (at protein level). Highly expressed in seminal vesicle, minor in colon and placenta and, to a lesser extent, in small intestine, caecum, stomach, salivary gland and bone marrow. {ECO:0000269|PubMed:15901639}. +Q8BTE5 CEBOS_MOUSE Protein CEBPZOS 80 9,286 Chain (1); Transmembrane (1) TRANSMEM 15 31 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250|UniProtKB:A8MTT3}; Single-pass membrane protein {ECO:0000255}. +O88693 CEGT_MOUSE Ceramide glucosyltransferase (EC 2.4.1.80) (GLCT-1) (Glucosylceramide synthase) (GCS) (UDP-glucose ceramide glucosyltransferase) (UDP-glucose:N-acylsphingosine D-glucosyltransferase) 394 44,839 Active site (1); Chain (1); Modified residue (1); Motif (4); Site (1); Topological domain (6); Transmembrane (5) TRANSMEM 11 32 Helical. {ECO:0000255}.; TRANSMEM 196 215 Helical. {ECO:0000255}.; TRANSMEM 288 304 Helical. {ECO:0000255}.; TRANSMEM 310 328 Helical. {ECO:0000255}.; TRANSMEM 349 369 Helical. {ECO:0000255}. TOPO_DOM 1 10 Lumenal. {ECO:0000255}.; TOPO_DOM 33 195 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 216 287 Lumenal. {ECO:0000255}.; TOPO_DOM 305 309 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 329 348 Lumenal. {ECO:0000255}.; TOPO_DOM 370 394 Cytoplasmic. {ECO:0000255}. Lipid metabolism; sphingolipid metabolism. "FUNCTION: Catalyzes the first glycosylation step in glycosphingolipid biosynthesis, the transfer of glucose to ceramide. May also serve as a ""flippase"" (By similarity). {ECO:0000250}." SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. DOMAIN: The D1, D2, D3, (Q/R)XXRW motif is a critical part of the GCS active site, involved in catalysis and UDP-sugar binding. {ECO:0000250|UniProtKB:Q9R0E0}. +P28033 CEBPB_MOUSE CCAAT/enhancer-binding protein beta (C/EBP beta) (AGP/EBP) (Interleukin-6-dependent-binding protein) (IL-6DBP) (Liver-enriched transcriptional activator) (LAP) 296 31,446 Alternative sequence (2); Chain (1); Compositional bias (2); Cross-link (7); Domain (1); Glycosylation (2); Helix (1); Modified residue (12); Mutagenesis (16); Region (4) FUNCTION: Important transcription factor regulating the expression of genes involved in immune and inflammatory responses (PubMed:16585579, PubMed:17911624, PubMed:18486321, PubMed:20111005). Plays also a significant role in adipogenesis, as well as in the gluconeogenic pathway, liver regeneration, and hematopoiesis (PubMed:9727068, PubMed:10635333, PubMed:17301242, PubMed:17601773, PubMed:19478079, PubMed:24061474, PubMed:24216764). The consensus recognition site is 5'-T[TG]NNGNAA[TG]-3'. Its functional capacity is governed by protein interactions and post-translational protein modifications. During early embryogenesis, plays essential and redundant functions with CEBPA (PubMed:15509779). Has a promitotic effect on many cell types such as hepatocytes and adipocytes but has an antiproliferative effect on T-cells by repressing MYC expression, facilitating differentiation along the T-helper 2 lineage (PubMed:9727068, PubMed:10635333, PubMed:16585579). Binds to regulatory regions of several acute-phase and cytokines genes and plays a role in the regulation of acute-phase reaction and inflammation. Plays also a role in intracellular bacteria killing (PubMed:17911624). During adipogenesis, is rapidly expressed and, after activation by phosphorylation, induces CEBPA and PPARG, which turn on the series of adipocyte genes that give rise to the adipocyte phenotype. The delayed transactivation of the CEBPA and PPARG genes by CEBPB appears necessary to allow mitotic clonal expansion and thereby progression of terminal differentiation (PubMed:15985551, PubMed:17301242, PubMed:17601773, PubMed:20194620). Essential for female reproduction because of a critical role in ovarian follicle development (PubMed:9303532). Restricts osteoclastogenesis (PubMed:19440205). Together with NFE2L1; represses expression of DSPP during odontoblast differentiation (By similarity). {ECO:0000250|UniProtKB:P17676, ECO:0000250|UniProtKB:P21272, ECO:0000269|PubMed:10635333, ECO:0000269|PubMed:1314426, ECO:0000269|PubMed:15509779, ECO:0000269|PubMed:15985551, ECO:0000269|PubMed:16585579, ECO:0000269|PubMed:17301242, ECO:0000269|PubMed:17601773, ECO:0000269|PubMed:17911624, ECO:0000269|PubMed:18486321, ECO:0000269|PubMed:19440205, ECO:0000269|PubMed:19478079, ECO:0000269|PubMed:20111005, ECO:0000269|PubMed:20194620, ECO:0000269|PubMed:24061474, ECO:0000269|PubMed:24216764, ECO:0000269|PubMed:9303532, ECO:0000269|PubMed:9727068, ECO:0000303|PubMed:25451943}.; FUNCTION: Isoform 2: Essential for gene expression induction in activated macrophages. Plays a major role in immune responses such as CD4(+) T-cell response, granuloma formation and endotoxin shock. Not essential for intracellular bacteria killing. {ECO:0000269|PubMed:17911624}.; FUNCTION: Isoform 3: Acts as a dominant negative through heterodimerization with isoform 2 (By similarity). Promotes osteoblast differentiation and osteoclastogenesis (PubMed:19440205). {ECO:0000250|UniProtKB:P17676, ECO:0000250|UniProtKB:P21272, ECO:0000269|PubMed:19440205}. PTM: Sumoylated by polymeric chains of SUMO2 or SUMO3. Sumoylation at Lys-133 is required for inhibition of T-cells proliferation (PubMed:16585579). In adipocytes, sumoylation at Lys-133 by PIAS1 leads to ubiquitination and subsequent proteasomal degradation (PubMed:24061474). Desumoylated by SENP2, which abolishes ubiquitination and stabilizes protein levels (PubMed:20194620). {ECO:0000250|UniProtKB:P17676, ECO:0000269|PubMed:16585579, ECO:0000269|PubMed:20194620, ECO:0000269|PubMed:24061474}.; PTM: Ubiquitinated, leading to proteasomal degradation. {ECO:0000269|PubMed:24061474}.; PTM: Phosphorylated at Thr-188 by MAPK and CDK2, serves to prime phosphorylation at Thr-179 and Ser-184 by GSK3B and acquire DNA-binding as well as transactivation activities, required to induce adipogenesis. MAPK and CDK2 act sequentially to maintain Thr-188 in the primed phosphorylated state during mitotical cloning expansion and thereby progression of terminal differentiation. Phosphorylation at Thr-217 enhances transactivation activity. Phosphorylation at Ser-276 in response to calcium increases transactivation activity (PubMed:1314426). Phosphorylated at Thr-188 by RPS6KA1 (By similarity). {ECO:0000250|UniProtKB:P17676, ECO:0000269|PubMed:1314426, ECO:0000269|PubMed:15985551, ECO:0000269|PubMed:17601773}.; PTM: O-glycosylated, glycosylation at Ser-180 and Ser-181 prevents phosphorylation on Thr-188, Ser-184 and Thr-179 and DNA binding activity which delays the adipocyte differentiation program. {ECO:0000269|PubMed:19478079}.; PTM: Acetylated. Acetylation at Lys-39 is an important and dynamic regulatory event that contributes to its ability to transactivate target genes, including those associated with adipogenesis and adipocyte function. Deacetylation by HDAC1 represses its transactivation activity (PubMed:18486321). Acetylated by KAT2A and KAT2B within a cluster of lysine residues between amino acids 98-102, this acetylation is strongly induced by glucocorticoid treatment and enhances transactivation activity (PubMed:17301242). {ECO:0000269|PubMed:17301242, ECO:0000269|PubMed:18486321}.; PTM: Methylated. Methylation at Arg-3 by CARM1 and at Lys-39 by EHMT2, inhibits transactivation activity. Methylation is probably inhibited by phosphorylation at Thr-188. {ECO:0000269|PubMed:20111005, ECO:0000305|PubMed:18647749}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16585579, ECO:0000269|PubMed:19015024}. Cytoplasm {ECO:0000250|UniProtKB:P17676}. Note=In T-cells when sumoylated drawn to pericentric heterochromatin thereby allowing proliferation (PubMed:16585579). Translocates to the nucleus when phosphorylated at Ser-288 (By similarity). {ECO:0000250|UniProtKB:P17676, ECO:0000269|PubMed:16585579}. SUBUNIT: Binds DNA as a homodimer and as a heterodimer. Interacts with ATF4. Binds DNA as a heterodimer with ATF4 (PubMed:11018027). Interacts with MYB; within the complex, MYB and CEBPB bind to different promoter regions (PubMed:11792321). Can form stable heterodimers with CEBPA, CEBPD and CEBPE (By similarity). Isoform 2 and isoform 3 also form heterodimers (By similarity). Interacts with TRIM28 and PTGES2 (PubMed:9742105, PubMed:15879117). Interacts with PRDM16 (PubMed:19641492). Interacts with CCDC85B (PubMed:15644333). Forms a complex with THOC5 (PubMed:19015024). Interacts with ZNF638; this interaction increases transcriptional activation (PubMed:21602272). Interacts with CIDEA and CIDEC (PubMed:22245780). Interaction with CIDEA increases transcriptional activation of a subset of CEBPB downstream target genes, including ID2, IGF1, PRLR, SOCS1, SOCS3, XDH. Interaction with CIDEC increases transcriptional activation of SOCS1, SOCS3, TGFB1, TGFBR1, ID2 and XDH. Interacts with DDIT3/CHOP. Interacts with EP300; recruits EP300 to chromatin. Interacts with RORA; the interaction disrupts interaction with EP300 (PubMed:19324970). Interacts (not methylated) with MED23, MED26, SMARCA2, SMARCB1 and SMARCC1 (PubMed:20111005). Interacts with KAT2A and KAT2B (PubMed:17301242). Interacts with ATF5; EP300 is required for ATF5 and CEBPB interaction and DNA binding (PubMed:24216764). Interacts with NFE2L1; the heterodimer represses expression of DSPP during odontoblast differentiation (By similarity). {ECO:0000250|UniProtKB:P21272, ECO:0000269|PubMed:11018027, ECO:0000269|PubMed:11792321, ECO:0000269|PubMed:15644333, ECO:0000269|PubMed:15879117, ECO:0000269|PubMed:17301242, ECO:0000269|PubMed:18486321, ECO:0000269|PubMed:19015024, ECO:0000269|PubMed:19324970, ECO:0000269|PubMed:19641492, ECO:0000269|PubMed:20111005, ECO:0000269|PubMed:21602272, ECO:0000269|PubMed:22245780, ECO:0000269|PubMed:24216764, ECO:0000269|PubMed:9742105}. TISSUE SPECIFICITY: Abundantly expressed in myoblasts. Enriched in brown adipose tissue (BAT) versus white adipose tissue (WAT). Expressed in hepatocytes (at protein level). Expressed in T lymphocytes (PubMed:16585579). The expression in granulosa cells of antral follicles is induced by luteinizing hormone (PubMed:9303532). Expressed in chondrocytes and osteoblasts (at protein level) (PubMed:19440205). {ECO:0000269|PubMed:10635333, ECO:0000269|PubMed:16585579, ECO:0000269|PubMed:19440205, ECO:0000269|PubMed:19641492, ECO:0000269|PubMed:9303532}. +Q3U3S3 CENPL_MOUSE Centromere protein L (CENP-L) 329 37,725 Chain (1); Modified residue (2); Sequence conflict (2) FUNCTION: Component of the CENPA-CAD (nucleosome distal) complex, a complex recruited to centromeres which is involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation. May be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, centromere {ECO:0000250}. Note=Localizes exclusively in the centromeres. The CENPA-CAD complex is probably recruited on centromeres by the CENPA-NAC complex (By similarity). {ECO:0000250}. SUBUNIT: Component of the CENPA-CAD complex, composed of CENPI, CENPK, CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS. The CENPA-CAD complex interacts with the CENPA-NAC complex, at least composed of CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and CENPU (By similarity). {ECO:0000250}. +Q8BMK0 CEP85_MOUSE Centrosomal protein of 85 kDa (Cep85) (Coiled-coil domain-containing protein 21) 761 85,340 Chain (1); Coiled coil (2); Compositional bias (1); Modified residue (2); Region (2); Sequence conflict (2) FUNCTION: Acts as a negative regulator of NEK2 to maintain the centrosome integrity in interphase. Suppresses centrosome disjunction by inhibiting NEK2 kinase activity. {ECO:0000250|UniProtKB:Q6P2H3}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q6P2H3}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q6P2H3}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q6P2H3}. Note=Localizes to centrosomes and nucleolus in interphase. Upon entry into mitosis, relocates from nucleolus and accumulates at spindle poles. Associated with the pericentriolar material. Localizes to centrosomes at a low level in G1 phase and a slightly increased level in S phase, with gradually elevated levels during G2 phase. The levels at centrosomes further increase at G2/M, reaching a peak at spindle poles at early mitotic stages and remain high until the end of anaphase. {ECO:0000250|UniProtKB:Q6P2H3}. +Q9CZX2 CEP89_MOUSE Centrosomal protein of 89 kDa (Cep89) (Coiled-coil domain-containing protein 123) 791 90,320 Chain (1); Coiled coil (3); Compositional bias (1); Frameshift (1); Modified residue (1) FUNCTION: Required for ciliogenesis. Also plays a role in mitochondrial metabolism where it may modulate complex IV activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250}. Mitochondrion intermembrane space {ECO:0000250}. Note=Localizes to the distal appendage region of the centriole, which anchors the mother centriole to the plasma membrane. {ECO:0000250}. +Q8K015 CENPO_MOUSE Centromere protein O (CENP-O) 298 34,154 Alternative sequence (2); Chain (1); Coiled coil (1); Modified residue (1); Sequence conflict (4) FUNCTION: Component of the CENPA-CAD (nucleosome distal) complex, a complex recruited to centromeres which is involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation. May be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex. Modulates the kinetochore-bound levels of NDC80 complex (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, centromere {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Note=Localizes exclusively in the centromeres. The CENPA-CAD complex is probably recruited on centromeres by the CENPA-NAC complex (By similarity). {ECO:0000250}. SUBUNIT: Component of the CENPA-CAD complex, composed of CENPI, CENPK, CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS. The CENPA-CAD complex interacts with the CENPA-NAC complex, at least composed of CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and CENPU (By similarity). {ECO:0000250}. +Q9CXS4 CENPV_MOUSE Centromere protein V (CENP-V) (Proline-rich protein 6) 252 27,541 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (1); Modified residue (4); Sequence conflict (2) FUNCTION: Required for distribution of pericentromeric heterochromatin in interphase nuclei and for centromere formation and organization, chromosome alignment and cytokinesis. {ECO:0000250}. SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q7Z7K6}. Nucleus {ECO:0000250|UniProtKB:Q7Z7K6}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q7Z7K6}. Note=Enriched at the nuclear periphery and around the nucleolus. In mitotic cells, localizes to kinetochores from prometaphase to metaphase. At anaphase onset, transfers to the spindle midzone and then to the mid-body in telophase and cytokinesis. {ECO:0000250|UniProtKB:Q7Z7K6}. +Q3URR0 CENPW_MOUSE Centromere protein W (CENP-W) (Cancer-up-regulated gene 2 protein) 86 9,734 Chain (1) FUNCTION: Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation (By similarity). The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres (By similarity). Part of a nucleosome-associated complex that binds specifically to histone H3-containing nucleosomes at the centromere, as opposed to nucleosomes containing CENPA. Component of the heterotetrameric CENP-T-W-S-X complex that binds and supercoils DNA, and plays an important role in kinetochore assembly. CENPW has a fundamental role in kinetochore assembly and function. It is one of the inner kinetochore proteins, with most further proteins binding downstream. Required for normal chromosome organization and normal progress through mitosis (By similarity). {ECO:0000250, ECO:0000269|PubMed:17610844}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5EE01}. Chromosome, centromere {ECO:0000250|UniProtKB:Q5EE01}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q5EE01}. Nucleus matrix {ECO:0000250|UniProtKB:Q5EE01}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q5EE01}. Note=Constitutively localizes to centromeres throughout the cell cycle, and to the inner kinetochore during mitosis. {ECO:0000250|UniProtKB:P0DJH6}. SUBUNIT: Heterodimer with CENPT; this dimer coassembles with CENPS-CENPX heterodimers at centromeres to form the tetrameric CENP-T-W-S-X complex, which is a subcomplex of the large constitutive centromere-associated network (CCAN, also known as the interphase centromere complex or ICEN). Interacts with NPM1. {ECO:0000250|UniProtKB:Q5EE01}. +Q9D6K9 CERS5_MOUSE Ceramide synthase 5 (CerS5) (EC 2.3.1.24) (LAG1 longevity assurance homolog 5) (Translocating chain-associating membrane protein homolog 4) (TRAM homolog 4) 414 48,167 Alternative sequence (2); Chain (1); DNA binding (1); Domain (1); Glycosylation (1); Helix (3); Sequence conflict (2); Topological domain (7); Transmembrane (6) TRANSMEM 44 64 Helical. {ECO:0000255}.; TRANSMEM 148 168 Helical. {ECO:0000255}.; TRANSMEM 187 207 Helical. {ECO:0000255}.; TRANSMEM 214 234 Helical. {ECO:0000255}.; TRANSMEM 272 292 Helical. {ECO:0000255}.; TRANSMEM 312 332 Helical. {ECO:0000255}. TOPO_DOM 1 43 Lumenal. {ECO:0000255}.; TOPO_DOM 65 147 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 169 186 Lumenal. {ECO:0000255}.; TOPO_DOM 208 213 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 235 271 Lumenal. {ECO:0000255}.; TOPO_DOM 293 311 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 333 414 Lumenal. {ECO:0000255}. Lipid metabolism; sphingolipid metabolism. FUNCTION: Dihydroceramide synthase. Catalyzes the acylation of sphingosine to form dihydroceramide, with high selectivity toward palmitoyl-CoA as acyl donor compared to stearoyl-CoA. Inhibited by fumonisin B1. {ECO:0000269|PubMed:12912983, ECO:0000269|PubMed:16100120}. SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000255|PROSITE-ProRule:PRU00108}; Multi-pass membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:12912983}; Multi-pass membrane protein {ECO:0000269|PubMed:12912983}. TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in testis and kidney. {ECO:0000269|PubMed:12912983, ECO:0000269|PubMed:15823095}. +Q9CQ82 CENPR_MOUSE Centromere protein R (CENP-R) (Nuclear receptor-interacting factor 3) 176 20,026 Alternative sequence (2); Chain (1); Coiled coil (1); Cross-link (2); Modified residue (3); Motif (2); Region (1); Sequence conflict (3) FUNCTION: Transcription coregulator that can have both coactivator and corepressor functions. Involved in the coactivation of nuclear receptors for retinoid X (RXRs) and thyroid hormone (TRs) in a ligand-dependent fashion. In contrast, it does not coactivate nuclear receptors for retinoic acid, vitamin D, progesterone receptor, nor glucocorticoid. Acts as a coactivator for estrogen receptor alpha. Acts as a transcriptional corepressor via its interaction with the NFKB1 NF-kappa-B subunit, possibly by interfering with the transactivation domain of NFKB1. Induces apoptosis in breast cancer cells, but not in other cancer cells, via a caspase-2 mediated pathway that involves mitochondrial membrane permeabilization but does not require other caspases. May also act as an inhibitor of cyclin A-associated kinase. Also acts a component of the CENPA-CAD (nucleosome distal) complex, a complex recruited to centromeres which is involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation. May be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, centromere {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. SUBUNIT: Homodimer; mediated by the coiled coil domain. Interacts with CCNA2 and MTA1. Interacts with NFKB1 NF-kappa-B subunit. Component of the CENPA-CAD complex, composed of CENPI, CENPK, CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS. The CENPA-CAD complex interacts with the CENPA-NAC complex, at least composed of CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and CENPU (By similarity). {ECO:0000250}. DOMAIN: The DD1 domain (also called RepD1 domain) mediates the corepressor function and is essential in the triggering of apoptosis. {ECO:0000250}.; DOMAIN: Contains one Leu-Xaa-Xaa-Ile-Leu (LXXIL) motif, which is essential for the association with nuclear receptors. {ECO:0000250}. +Q3UPP8 CEP63_MOUSE Centrosomal protein of 63 kDa (Cep63) 700 80,449 Alternative sequence (4); Chain (1); Coiled coil (2); Frameshift (1); Modified residue (4) FUNCTION: Required for normal spindle assembly. Plays a key role in mother-centriole-dependent centriole duplication; the function seems also to involve CEP152, CDK5RAP2 and WDR62 through a stepwise assembled complex at the centrosome that recruits CDK2 required for centriole duplication. Also recruits CDK1 to centrosomes. Plays a role in DNA damage response. Following DNA damage, such as double-strand breaks (DSBs), is removed from centrosomes; this leads to the inactivation of spindle assembly and in delay mitotic progression. {ECO:0000250|UniProtKB:Q96MT8, ECO:0000269|PubMed:24240477}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:21983783}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:24240477}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000250|UniProtKB:Q96MT8}. Note=Colocalizes with CDK5RAP2, CEP152 and WDR62in a discrete ring around the proximal end of the parental centriole. At this site, a cohesive structure is predicted to engage parental centrioles and procentrioles. {ECO:0000250|UniProtKB:Q96MT8, ECO:0000269|PubMed:21983783, ECO:0000269|PubMed:24240477}. SUBUNIT: Interacts with CEP152 and CDK1; these interactions recruit both ligands to centrosomes. Interacts with CDK2, CDK5RAP2, WDR62, CEP90, KIAA0753/moonraker and CCDC14. CEP63, CDK5RAP2, CEP152, WDR62 are proposed to form a stepwise assembled complex at the centrosome forming a ring near parental centrioles. {ECO:0000250|UniProtKB:Q96MT8}. +Q8C0D9 CEP68_MOUSE Centrosomal protein of 68 kDa (Cep68) 733 78,749 Alternative sequence (1); Chain (1); Modified residue (3); Sequence conflict (1) FUNCTION: Involved in maintenance of centrosome cohesion, probably as part of a linker structure which prevents centrosome splitting. Required for localization of CDK5RAP2 to the centrosome during interphase. {ECO:0000250|UniProtKB:Q76N32}. PTM: Phosphorylation by PLK1 is required for binding to BTRC in prometaphase. Phosphorylated directly or indirectly by NEK2. NEK2-mediated phosphorylation promotes CEP68 dissociation from the centrosome and its degradation at the onset of mitosis. {ECO:0000250|UniProtKB:Q76N32}.; PTM: Ubiquitinated and targeted for proteasomal degradation in early mitosis by the SCF(BTRC) and/or SCF(FBXW11) E3 ubiquitin-protein ligase complexes. Degradation is complete by prometaphase and is required for removal of CDK5RAP2 from the peripheral pericentriolar material and subsequent centriole separation. {ECO:0000250|UniProtKB:Q76N32}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Note=Localizes to thin fibers protruding away from the proximal ends of the two centrioles. Dissociates from interphase centrosomes at the onset of mitosis. {ECO:0000250|UniProtKB:Q76N32}. SUBUNIT: Interacts with CNTLN; the interaction recruits CEP68 to the centrosome. Interacts with the SCF(FBXW11) complex which contains SKP1, CUL1 and FBXW11; the interaction is probably mediated by FBXW11 and the complex also contains CDK5RAP2 and PCNT. Also interacts with F-box protein BTRC. Interacts with serine/threonine-protein kinase PLK1; the interaction leads to phosphorylation of CEP68 and its subsequent degradation. Interacts with NEK2; the interaction leads to phosphorylation of CEP68. {ECO:0000250|UniProtKB:Q76N32}. +Q9CQA8 CEP19_MOUSE Centrosomal protein of 19 kDa (Cep19) 163 19,170 Chain (1) FUNCTION: Required for ciliation. Recruits the RABL2B GTPase to the ciliary base to initiate ciliation. After specifically capturing the activated GTP-bound RABL2B, the CEP19-RABL2B complex binds intraflagellar transport (IFT) complex B from the large pool pre-docked at the base of the cilium and thus triggers its entry into the cilia. Involved in the early steps in cilia formation by recruiting the ciliary vesicles (CVs) to the distal end of the mother centriole where they fuse to initiate cilium assembly. Involved in microtubule (MT) anchoring at centrosomes. {ECO:0000250|UniProtKB:Q96LK0}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q96LK0}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q96LK0}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q96LK0}. Note=Associates with the mother centriole in early interphase. Localizes to spindle poles during mitosis, and to distinct foci oriented towards the midbody at telophase. Localizes slightly apical to the subdistal appendage on the mother centriole, but below the distal appendage. {ECO:0000250|UniProtKB:Q96LK0}. SUBUNIT: Interacts with FGFR1OP; this interaction is required for its localization to the mother centriole. Interacts (via residues 121-150) with RABL2B. Interacts (via C-terminus) with CEP350; this interaction is required for its localization to the mother centriole. {ECO:0000250|UniProtKB:Q96LK0}. +Q6IRU7 CEP78_MOUSE Centrosomal protein of 78 kDa (Cep78) 790 86,890 Chain (1); Coiled coil (1); Modified residue (2) FUNCTION: May be required for efficient PLK4 centrosomal localization and PLK4-induced overduplication of centrioles. May play a role in cilium biogenesis. {ECO:0000250|UniProtKB:Q5JTW2}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q5JTW2}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q5JTW2}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q5JTW2}. Note=Mainly localizes at the centriolar wall, but also found in the pericentriolar material. Expressed in photoreceptor inner segment. {ECO:0000269|PubMed:27588452}. SUBUNIT: Interacts with PLK4. Interacts with FAM161A. {ECO:0000250|UniProtKB:Q5JTW2}. TISSUE SPECIFICITY: Expressed by photoreceptor cells in the retina. {ECO:0000269|PubMed:27588452}. +P27545 CERS1_MOUSE Ceramide synthase 1 (CerS1) (LAG1 longevity assurance homolog 1) (Longevity assurance gene 1 protein homolog 1) (Protein UOG-1) 350 40,100 Chain (1); Compositional bias (1); Domain (1); Initiator methionine (1); Modified residue (1); Transmembrane (6) TRANSMEM 53 73 Helical. {ECO:0000255}.; TRANSMEM 103 123 Helical. {ECO:0000255}.; TRANSMEM 148 168 Helical. {ECO:0000255}.; TRANSMEM 176 196 Helical. {ECO:0000255}.; TRANSMEM 239 259 Helical. {ECO:0000255}.; TRANSMEM 287 307 Helical. {ECO:0000255}. FUNCTION: May be either a bona fide (dihydro)ceramide synthase or a modulator of its activity. When overexpressed in cells is involved in the production of sphingolipids containing mainly one fatty acid donor (N-linked stearoyl- (C18) ceramide) in a fumonisin B1-independent manner. {ECO:0000269|PubMed:12105227}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Brain-specific. {ECO:0000269|PubMed:15823095}. +Q6P8Y0 CF161_MOUSE Cilia- and flagella-associated protein 161 303 34,388 Chain (1); Sequence conflict (1) FUNCTION: May play a role in motile cilia function, possibly by acting on dynein arm assembly. {ECO:0000250|UniProtKB:Q568D2}. +E9Q743 CF251_MOUSE Cilia- and flagella-associated protein 251 (CFAP251) (WD repeat-containing protein 66) 1299 148,608 Chain (1); Compositional bias (1); Erroneous initiation (2); Repeat (14); Sequence conflict (2) FUNCTION: Involved in spermatozoa motility (By similarity). May also regulate cilium motility through its role in the assembly of the axonemal radial spokes (By similarity). {ECO:0000250|UniProtKB:A8IRK7, ECO:0000250|UniProtKB:Q24DE2, ECO:0000250|UniProtKB:Q8TBY9}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:A8IRK7}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q8TBY9}. +Q6ZPR1 CFA97_MOUSE Cilia- and flagella-associated protein 97 541 60,837 Chain (1); Coiled coil (1); Compositional bias (1); Erroneous initiation (1); Modified residue (7) +Q8C6G1 CF410_MOUSE Cilia- and flagella-associated protein 410 249 28,239 Chain (1); Domain (1); Repeat (3); Sequence conflict (2) FUNCTION: Plays a role in cilia formation and/or maintenance (PubMed:21289087). Plays a role in the regulation of cell morphology and cytoskeletal organization (By similarity). Involved in DNA damage repair (By similarity). {ECO:0000250|UniProtKB:O43822, ECO:0000269|PubMed:21289087}. SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000269|PubMed:26294103, ECO:0000269|PubMed:26974433, ECO:0000269|PubMed:27548899}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:26167768, ECO:0000269|PubMed:26294103}. Mitochondrion {ECO:0000250|UniProtKB:O43822}. Cell projection, cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:O43822}. Cytoplasm {ECO:0000250|UniProtKB:O43822}. Note=Localized to the connecting cilium of the cone and rod photoreceptors (PubMed:27548899, PubMed:26974433). Colocalizes with NEK1 and SPATA7 at the basal body (By similarity). {ECO:0000250|UniProtKB:O43822, ECO:0000269|PubMed:26167768, ECO:0000269|PubMed:26974433, ECO:0000269|PubMed:27548899}. SUBUNIT: Found in a complex with CFAP410, NEK1 and SPATA7 (By similarity). Interacts with NEK1 (By similarity). {ECO:0000250|UniProtKB:O43822}. TISSUE SPECIFICITY: Expressed in the retina. {ECO:0000269|PubMed:26167768, ECO:0000269|PubMed:26294103}. +Q8C6S9 CFA54_MOUSE Cilia- and flagella-associated protein 54 3106 353,760 Alternative sequence (1); Chain (1); Sequence conflict (2) FUNCTION: Required for assembly and function of cilia and flagella (PubMed:26224312). {ECO:0000269|PubMed:26224312}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:A8J666}. TISSUE SPECIFICITY: Expressed at high level in the testis and at a low level in the lung and brain. {ECO:0000269|PubMed:26224312}. +Q9D180 CFA57_MOUSE Cilia- and flagella-associated protein 57 (WD repeat-containing protein 65) 1249 144,934 Chain (1); Coiled coil (2); Erroneous initiation (2); Repeat (8) TISSUE SPECIFICITY: Predominanly expressed in testis, lung and skin. Weak expression in brain and kidney. {ECO:0000269|PubMed:21574244}. +O88271 CFDP1_MOUSE Craniofacial development protein 1 (27 kDa craniofacial protein) (Bucentaur) (Protein Cp27) 295 32,921 Chain (1); Compositional bias (1); Cross-link (1); Domain (1); Modified residue (7); Region (1); Sequence conflict (2) FUNCTION: May play a role during embryogenesis. May modulate tooth organogenesis since alterations of this protein function affect tooth organs size as well as individual cell fate and survival. In embryonic cells, blockage of the function results in increased number of apoptotic cells, reduced proliferation, alterations in cell shape and fibronection matrix synthesis. {ECO:0000269|PubMed:10415329, ECO:0000269|PubMed:11992732, ECO:0000269|PubMed:12153613}. SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q9UEE9}. TISSUE SPECIFICITY: Expressed in lung, liver and heart, with higher expression in teeth. {ECO:0000269|PubMed:10415329}. +P26361 CFTR_MOUSE Cystic fibrosis transmembrane conductance regulator (CFTR) (ATP-binding cassette sub-family C member 7) (Channel conductance-controlling ATPase) (EC 3.6.3.49) (cAMP-dependent chloride channel) 1476 167,870 Alternative sequence (4); Beta strand (11); Binding site (3); Chain (1); Domain (4); Glycosylation (2); Helix (17); Lipidation (2); Modified residue (14); Motif (1); Mutagenesis (5); Nucleotide binding (2); Region (2); Sequence conflict (6); Topological domain (13); Transmembrane (12); Turn (2) TRANSMEM 78 98 Helical; Name=1. {ECO:0000250|UniProtKB:P13569}.; TRANSMEM 123 146 Helical; Name=2. {ECO:0000250|UniProtKB:P13569}.; TRANSMEM 196 216 Helical; Name=3. {ECO:0000250|UniProtKB:P13569}.; TRANSMEM 223 243 Helical; Name=4. {ECO:0000250|UniProtKB:P13569}.; TRANSMEM 299 319 Helical; Name=5. {ECO:0000250|UniProtKB:P13569}.; TRANSMEM 340 358 Helical; Name=6. {ECO:0000250|UniProtKB:P13569}.; TRANSMEM 854 874 Helical; Name=7. {ECO:0000250|UniProtKB:P13569}.; TRANSMEM 914 934 Discontinuously helical; Name=8. {ECO:0000250|UniProtKB:P13569}.; TRANSMEM 986 1006 Helical; Name=9. {ECO:0000250|UniProtKB:P13569}.; TRANSMEM 1009 1029 Helical; Name=10. {ECO:0000250|UniProtKB:P13569}.; TRANSMEM 1091 1111 Helical; Name=11. {ECO:0000250|UniProtKB:P13569}.; TRANSMEM 1126 1146 Helical; Name=12. {ECO:0000250|UniProtKB:P13569}. TOPO_DOM 1 77 Cytoplasmic. {ECO:0000250|UniProtKB:P13569}.; TOPO_DOM 99 122 Extracellular. {ECO:0000250|UniProtKB:P13569}.; TOPO_DOM 147 195 Cytoplasmic. {ECO:0000250|UniProtKB:P13569}.; TOPO_DOM 217 222 Extracellular. {ECO:0000250|UniProtKB:P13569}.; TOPO_DOM 244 298 Cytoplasmic. {ECO:0000250|UniProtKB:P13569}.; TOPO_DOM 320 339 Extracellular. {ECO:0000250|UniProtKB:P13569}.; TOPO_DOM 359 853 Cytoplasmic. {ECO:0000250|UniProtKB:P13569}.; TOPO_DOM 875 913 Extracellular. {ECO:0000250|UniProtKB:P13569}.; TOPO_DOM 935 985 Cytoplasmic. {ECO:0000250|UniProtKB:P13569}.; TOPO_DOM 1007 1008 Extracellular. {ECO:0000250|UniProtKB:P13569}.; TOPO_DOM 1030 1090 Cytoplasmic. {ECO:0000250|UniProtKB:P13569}.; TOPO_DOM 1112 1125 Extracellular. {ECO:0000250|UniProtKB:P13569}.; TOPO_DOM 1147 1476 Cytoplasmic. {ECO:0000250|UniProtKB:P13569}. FUNCTION: Epithelial ion channel that plays an important role in the regulation of epithelial ion and water transport and fluid homeostasis (PubMed:26823428). Mediates the transport of chloride ions across the cell membrane (PubMed:20231442, PubMed:22265409). Channel activity is coupled to ATP hydrolysis. The ion channel is also permeable to HCO(3-); selectivity depends on the extracellular chloride concentration. Exerts its function also by modulating the activity of other ion channels and transporters. Contributes to the regulation of the pH and the ion content of the epithelial fluid layer. Modulates the activity of the epithelial sodium channel (ENaC) complex, in part by regulating the cell surface expression of the ENaC complex. May regulate bicarbonate secretion and salvage in epithelial cells by regulating the transporter SLC4A7. Can inhibit the chloride channel activity of ANO1 (By similarity). Plays a role in the chloride and bicarbonate homeostasis during sperm epididymal maturation and capacitation (PubMed:21976599). {ECO:0000250|UniProtKB:P13569, ECO:0000269|PubMed:19033647, ECO:0000269|PubMed:20231442, ECO:0000269|PubMed:21976599, ECO:0000269|PubMed:22265409, ECO:0000269|PubMed:26823428}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:P13569}.; PTM: Phosphorylated; cAMP treatment promotes phosphorylation and activates the channel. Dephosphorylation decreases the ATPase activity (in vitro). Phosphorylation at PKA sites activates the channel. Phosphorylation at PKC sites enhances the response to phosphorylation by PKA. Phosphorylated by AMPK; this inhibits channel activity. {ECO:0000250|UniProtKB:P13569}.; PTM: Ubiquitinated, leading to its degradation in the lysosome. Deubiquitination by USP10 in early endosomes enhances its endocytic recycling to the cell membrane. Ubiquitinated by RNF185 during ER stress. {ECO:0000250|UniProtKB:P13569}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:20231442, ECO:0000269|PubMed:21884936}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P13569}. Early endosome membrane {ECO:0000250|UniProtKB:P13569}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P13569}. Cell membrane {ECO:0000269|PubMed:20231442, ECO:0000269|PubMed:22265409}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P13569}. Recycling endosome membrane {ECO:0000250|UniProtKB:P13569}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P13569}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P13569}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P13569}. Nucleus {ECO:0000250|UniProtKB:P34158}. Note=The channel is internalized from the cell surface into an endosomal recycling compartment, from where it is recycled to the cell membrane. In the oviduct and bronchus, detected on the apical side of epithelial cells, but not associated with cilia. In Sertoli cells, a processed product is detected in the nucleus. ER stress induces GORASP2-mediated unconventional (ER/Golgi-independent) trafficking of core-glycosylated CFTR to cell membrane (PubMed:21884936). {ECO:0000250|UniProtKB:P13569, ECO:0000250|UniProtKB:P34158, ECO:0000269|PubMed:21884936}. SUBUNIT: Monomer; does not require oligomerization for channel activity. May form oligomers in the membrane (By similarity). Interacts with SLC26A3, SLC26A6 and SLC9A3R1 (PubMed:21976599). Interacts with SHANK2 (By similarity). Interacts with MYO6 (By similarity). Interacts (via C-terminus) with GOPC (via PDZ domain); this promotes CFTR internalization and thereby decreases channel activity. Interacts with SLC4A7 through SLC9A3R1. Found in a complex with MYO5B and RAB11A. Interacts with ANO1. Interacts with SLC26A8 (By similarity). Interacts with AHCYL1; the interaction increases CFTR activity (PubMed:19033647, PubMed:23542070). Interacts with CSE1L (By similarity). The core-glycosylated form interacts with GORASP2 (via PDZ GRASP-type 1 domain) in respone to ER stress (By similarity). {ECO:0000250|UniProtKB:P13569, ECO:0000250|UniProtKB:P34158, ECO:0000269|PubMed:19033647, ECO:0000269|PubMed:21976599, ECO:0000269|PubMed:23542070}. DOMAIN: Binds and hydrolyzes ATP via the two cytoplasmic ABC transporter nucleotide-binding domains. The two ATP-binding domains interact with each other, forming a head-to-tail dimer. Normal ATPase activity requires interaction between the two domains (By similarity). The first ABC transporter nucleotide-binding domain has no ATPase activity by itself (PubMed:14685259, PubMed:15619636). {ECO:0000250|UniProtKB:P13569, ECO:0000269|PubMed:14685259, ECO:0000269|PubMed:15619636}.; DOMAIN: The PDZ-binding motif mediates interactions with GOPC and with the SLC4A7, SLC9A3R1/EBP50 complex. {ECO:0000250|UniProtKB:P13569}.; DOMAIN: The R region is intrinsically disordered. It mediates channel activation when it is phosphorylated, but not in the absence of phosphorylation. {ECO:0000250|UniProtKB:P13569}. TISSUE SPECIFICITY: Isoform 1 is expressed in a variety of epithelial tissues including colon, kidney, lung, small intestine, pancreatic duct and testis. Isoforms 2 and 3 are expressed only in testis. {ECO:0000269|PubMed:19033647}. +Q3V0B4 CFA65_MOUSE Cilia- and flagella-associated protein 65 (Coiled-coil domain-containing protein 108) 1847 209,134 Chain (1); Coiled coil (1); Compositional bias (1); Domain (1); Transmembrane (1) TRANSMEM 112 132 Helical. {ECO:0000255}. FUNCTION: May play a role in sperm motility. {ECO:0000250|UniProtKB:I6WQT8}. SUBCELLULAR LOCATION: Cell projection, cilium, flagellum membrane {ECO:0000250|UniProtKB:A8JFU2}; Single-pass membrane protein {ECO:0000305}. +Q8BM15 CF015_MOUSE Uncharacterized protein C6orf15 homolog (Extracellular matrix protein with prion homology) (Emprin) (Protein STG) 349 36,654 Chain (1); Compositional bias (1); Sequence conflict (3); Signal peptide (1) SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:18757743}. SUBUNIT: Binds to numerous extracellular matrix proteins. {ECO:0000269|PubMed:18757743}. +J3QPZ5 CFA73_MOUSE Cilia- and flagella-associated protein 73 (Coiled-coil domain-containing protein 42B) 306 35,671 Chain (1); Coiled coil (2) FUNCTION: May play a role in ciliary/flagellar motility by regulating the assembly and the activity of axonemal inner dynein arm. {ECO:0000250|UniProtKB:M1V4Y8}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:M1V4Y8}. +Q3UJP5 CH037_MOUSE Protein C8orf37 homolog 209 23,848 Chain (1); Sequence conflict (1) FUNCTION: May be involved in photoreceptor outer segment disk morphogenesis. {ECO:0000269|PubMed:29440555}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22177090, ECO:0000269|PubMed:29440555}. Photoreceptor inner segment {ECO:0000269|PubMed:29440555}. Note=In the retina, located at the base of the primary cilium (PubMed:22177090). Expressed throughout photoreceptors cell body including the basal body, inner segment and synaptic terminus, but not in the outer segment (at the protein level). {ECO:0000269|PubMed:29440555}. TISSUE SPECIFICITY: Expressed in multiple tissues, including the brain, kidney, lung, spleen, heart, trachea and testis (PubMed:29440555). Expressed in the retina (at protein level) (PubMed:22177090, PubMed:29440555). {ECO:0000269|PubMed:22177090, ECO:0000269|PubMed:29440555}. +Q8BJQ9 CGAT1_MOUSE Chondroitin sulfate N-acetylgalactosaminyltransferase 1 (CsGalNAcT-1) (EC 2.4.1.174) (Chondroitin beta-1,4-N-acetylgalactosaminyltransferase 1) (Beta4GalNAcT-1) 530 60,917 Chain (1); Coiled coil (1); Erroneous termination (1); Glycosylation (2); Metal binding (2); Sequence conflict (4); Topological domain (2); Transmembrane (1) TRANSMEM 13 33 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 12 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 34 530 Lumenal. {ECO:0000255}. FUNCTION: Transfers 1,4-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to the non-reducing end of glucuronic acid (GlcUA). Required for addition of the first GalNAc to the core tetrasaccharide linker and for elongation of chondroitin chains. Important role in chondroitin chain biosynthesis in cartilage formation, and subsequent endochondral ossification (PubMed:17145758, PubMed:21148564). Moreover, is involved in the metabolism of aggrecan (PubMed:21148564). {ECO:0000269|PubMed:17145758, ECO:0000269|PubMed:21148564}. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. +Q9D1A2 CNDP2_MOUSE Cytosolic non-specific dipeptidase (EC 3.4.13.18) (CNDP dipeptidase 2) (Glutamate carboxypeptidase-like protein 1) 475 52,767 Active site (2); Beta strand (19); Binding site (6); Chain (1); Helix (17); Metal binding (6); Modified residue (2); Mutagenesis (1); Region (1); Sequence conflict (3); Site (1); Turn (4) FUNCTION: Hydrolyzes a variety of dipeptides including L-carnosine but has a strong preference for Cys-Gly. Catalyzes the production of N-lactoyl-amino acids from lactate and amino acids by reverse proteolysis. {ECO:0000250|UniProtKB:Q96KP4}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96KP4}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q96KP4}. TISSUE SPECIFICITY: Highly expressed in the parafascicular nucleus of the thalamus, tuberomammillary nucleus of the hypothalamus and the mitral cell layer of the olfactory bulb. {ECO:0000269|PubMed:15749831}. +Q3TP92 CNEP1_MOUSE CTD nuclear envelope phosphatase 1 (EC 3.1.3.16) (Serine/threonine-protein phosphatase dullard) 244 28,391 Chain (1); Domain (1); Sequence conflict (1); Transmembrane (1) TRANSMEM 7 29 Helical. {ECO:0000255}. FUNCTION: Serine/threonine protein phosphatase forming with CNEP1R1 an active phosphatase complex that dephosphorylates and may activate LPIN1 and LPIN2. LPIN1 and LPIN2 are phosphatidate phosphatases that catalyze the conversion of phosphatidic acid to diacylglycerol and control the metabolism of fatty acids at different levels. May indirectly modulate the lipid composition of nuclear and/or endoplasmic reticulum membranes and be required for proper nuclear membrane morphology and/or dynamics. May also indirectly regulate the production of lipid droplets and triacylglycerol. May antagonize BMP signaling (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with CNEP1R1; the complex dephosphorylates LPIN1 and LPIN2. {ECO:0000250}. TISSUE SPECIFICITY: Muscle specific with lower expression in other metabolic tissues. {ECO:0000269|PubMed:22134922}. +P29974 CNGA1_MOUSE cGMP-gated cation channel alpha-1 (Cyclic nucleotide-gated cation channel 1) (Cyclic nucleotide-gated channel alpha-1) (CNG channel alpha-1) (CNG-1) (CNG1) (Cyclic nucleotide-gated channel, photoreceptor) (Rod photoreceptor cGMP-gated channel subunit alpha) 684 79,460 Binding site (2); Chain (1); Coiled coil (1); Glycosylation (1); Nucleotide binding (1); Sequence conflict (4); Topological domain (7); Transmembrane (6) TRANSMEM 157 177 Helical; Name=H1. {ECO:0000255}.; TRANSMEM 191 209 Helical; Name=H2. {ECO:0000255}.; TRANSMEM 234 253 Helical; Name=H3. {ECO:0000255}.; TRANSMEM 292 314 Helical; Name=H4. {ECO:0000255}.; TRANSMEM 367 386 Helical; Name=H5. {ECO:0000255}.; TRANSMEM 471 491 Helical; Name=H6. {ECO:0000255}. TOPO_DOM 1 156 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 178 190 Extracellular. {ECO:0000255}.; TOPO_DOM 210 233 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 254 291 Extracellular. {ECO:0000255}.; TOPO_DOM 315 366 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 387 470 Extracellular. {ECO:0000255}.; TOPO_DOM 492 684 Cytoplasmic. {ECO:0000255}. FUNCTION: Visual signal transduction is mediated by a G-protein coupled cascade using cGMP as second messenger. This protein can be activated by cyclic GMP which leads to an opening of the cation channel and thereby causing a depolarization of rod photoreceptors. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SUBUNIT: Tetramer formed of three CNGA1 and one CNGB1 modulatory subunits. {ECO:0000250}. DOMAIN: The C-terminal coiled-coil domain mediates homotrimerization of CNGA subunits. {ECO:0000250}. TISSUE SPECIFICITY: Rod cells in the retina and inner medulla of kidney. +Q62398 CNGA2_MOUSE Cyclic nucleotide-gated olfactory channel (Cyclic nucleotide-gated cation channel 2) (Cyclic nucleotide-gated channel alpha-2) (CNG channel alpha-2) (CNG-2) (CNG2) 664 76,193 Binding site (2); Chain (1); Coiled coil (1); Glycosylation (1); Nucleotide binding (1); Sequence conflict (3); Topological domain (7); Transmembrane (6) TRANSMEM 143 163 Helical; Name=H1. {ECO:0000255}.; TRANSMEM 176 194 Helical; Name=H2. {ECO:0000255}.; TRANSMEM 219 238 Helical; Name=H3. {ECO:0000255}.; TRANSMEM 277 299 Helical; Name=H4. {ECO:0000255}.; TRANSMEM 352 371 Helical; Name=H5. {ECO:0000255}.; TRANSMEM 456 476 Helical; Name=H6. {ECO:0000255}. TOPO_DOM 1 142 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 164 175 Extracellular. {ECO:0000255}.; TOPO_DOM 195 218 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 239 276 Extracellular. {ECO:0000255}.; TOPO_DOM 300 351 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 372 455 Extracellular. {ECO:0000255}.; TOPO_DOM 477 664 Cytoplasmic. {ECO:0000255}. FUNCTION: Odorant signal transduction is probably mediated by a G-protein coupled cascade using cAMP as second messenger. The olfactory channel can be shown to be activated by cyclic nucleotides which leads to a depolarization of olfactory sensory neurons. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SUBUNIT: Heterotetramer composed of two subunits of CNGA2, one of CNGA4 and one of CNGB1b. The complex forms the cyclic nucleotide-gated (CNG) channel of olfactory sensory neurons (By similarity). {ECO:0000250}. DOMAIN: The C-terminal coiled-coil domain mediates trimerization of CNGA subunits. {ECO:0000250}. +P33611 DPOA2_MOUSE DNA polymerase alpha subunit B (DNA polymerase alpha 70 kDa subunit) 600 66,214 Chain (1); Compositional bias (2); Modified residue (7); Sequence conflict (1) FUNCTION: May play an essential role at the early stage of chromosomal DNA replication by coupling the polymerase alpha/primase complex to the cellular replication machinery. {ECO:0000250}. PTM: Phosphorylated in a cell cycle-dependent manner, in G2/M phase. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: DNA polymerase alpha:primase is a four subunit enzyme complex, which is assembled throughout the cell cycle, and consists of the two DNA polymerase subunits A and B, and the DNA primase large and small subunits. Subunit B binds to subunit A. +P52431 DPOD1_MOUSE DNA polymerase delta catalytic subunit (EC 2.7.7.7) (EC 3.1.11.-) 1105 123,790 Chain (1); Cross-link (1); Metal binding (8); Modified residue (1); Motif (2); Sequence conflict (8); Zinc finger (1) FUNCTION: As the catalytic component of the trimeric (Pol-delta3 complex) and tetrameric DNA polymerase delta complexes (Pol-delta4 complex), plays a crucial role in high fidelity genome replication, including in lagging strand synthesis, and repair. Exhibits both DNA polymerase and 3'- to 5'-exonuclease activities. Requires the presence of accessory proteins POLD2, POLD3 and POLD4 for full activity. Depending upon the absence (Pol-delta3) or the presence of POLD4 (Pol-delta4), displays differences in catalytic activity. Most notably, expresses higher proofreading activity in the context of Pol-delta3 compared with that of Pol-delta4. Although both Pol-delta3 and Pol-delta4 process Okazaki fragments in vitro, Pol-delta3 may be better suited to fulfill this task, exhibiting near-absence of strand displacement activity compared to Pol-delta4 and stalling on encounter with the 5'-blocking oligonucleotides. Pol-delta3 idling process may avoid the formation of a gap, while maintaining a nick that can be readily ligated. Along with DNA polymerase kappa, DNA polymerase delta carries out approximately half of nucleotide excision repair (NER) synthesis following UV irradiation. Under conditions of DNA replication stress, in the presence of POLD3 and POLD4, may catalyze the repair of broken replication forks through break-induced replication (BIR). Involved in the translesion synthesis (TLS) of templates carrying O6-methylguanine or abasic sites. {ECO:0000250|UniProtKB:P28340}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P28340}. Note=Colocalizes with PCNA and POLD3 at S phase replication sites. After UV irradiation, recruited to DNA damage sites within 2 hours, independently on the cell cycle phase, nor on PCNA ubiquitination. This recruitement requires POLD3, PCNA and RFC1-replication factor C complex. {ECO:0000250|UniProtKB:P28340}. SUBUNIT: Component of the tetrameric DNA polymerase delta complex (Pol-delta4), which consists of POLD1/p125, POLD2/p50, POLD3/p66/p68 and POLD4/p12, with POLD1 bearing both DNA polymerase and 3' to 5' proofreading exonuclease activities. Within Pol-delta4, directly interacts with POLD2 and POLD4. Following genotoxic stress by DNA-damaging agents, such as ultraviolet light and methyl methanesulfonate, or by replication stress induced by treatment with hydroxyurea or aphidicolin, Pol-delta4 is converted into a trimeric form of the complex (Pol-delta3) by POLD4 degradation. Pol-delta3 is the major form at S phase replication sites and DNA damage sites. POLD1 displays different catalytic properties depending upon the complex it is found in. It exhibits higher proofreading activity and fidelity than Pol-delta4, making it particularly well suited to respond to DNA damage. Directly interacts with PCNA, as do POLD3 and POLD4; this interaction stimulates Pol-delta4 polymerase activity. As POLD2 and POLD4, directly interacts with WRNIP1; this interaction stimulates DNA polymerase delta-mediated DNA synthesis, independently of the presence of PCNA. This stimulation may be due predominantly to an increase of initiation frequency and also to increased processivity. Also observed as a dimeric complex with POLD2 (Pol-delta2). Pol-delta2 is relatively insensitive to the PCNA stimulation (2-5-fold) compared to Pol-delta4 that is stimulated by over 50-fold. The DNA polymerase delta complex interacts with POLDIP2; this interaction is probably mediated through direct binding to POLD2. Interacts with CIAO1 (By similarity). {ECO:0000250|UniProtKB:P28340}. DOMAIN: The CysB motif binds 1 4Fe-4S cluster and is required for the formation of polymerase complexes. {ECO:0000250}. +O35654 DPOD2_MOUSE DNA polymerase delta subunit 2 (DNA polymerase delta subunit p50) 469 51,355 Chain (1); Modified residue (2); Sequence conflict (1) FUNCTION: As a component of the trimeric and tetrameric DNA polymerase delta complexes (Pol-delta3 and Pol-delta4, respectively), plays a role in high fidelity genome replication, including in lagging strand synthesis, and repair. Pol-delta3 and Pol-delta4 are characterized by the absence or the presence of POLD4. They exhibit differences in catalytic activity. Most notably, Pol-delta3 shows higher proofreading activity than Pol-delta4. Although both Pol-delta3 and Pol-delta4 process Okazaki fragments in vitro, Pol-delta3 may also be better suited to fulfill this task, exhibiting near-absence of strand displacement activity compared to Pol-delta4 and stalling on encounter with the 5'-blocking oligonucleotides. Pol-delta3 idling process may avoid the formation of a gap, while maintaining a nick that can be readily ligated. Along with DNA polymerase kappa, DNA polymerase delta carries out approximately half of nucleotide excision repair (NER) synthesis following UV irradiation. Under conditions of DNA replication stress, required for the repair of broken replication forks through break-induced replication (BIR). Involved in the translesion synthesis (TLS) of templates carrying O6-methylguanine or abasic sites performed by Pol-delta4, independently of DNA polymerase zeta (REV3L) or eta (POLH). Facilitates abasic site bypass by DNA polymerase delta by promoting extension from the nucleotide inserted opposite the lesion. Also involved in TLS as a component of the POLZ complex. Along with POLD3, dramatically increases the efficiency and processivity of DNA synthesis of the minimal DNA polymerase zeta complex, consisting of only REV3L and REV7. {ECO:0000250|UniProtKB:P49005}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P49005}. Note=Recruited to DNA damage sites within 2 hours following UV irradiation. {ECO:0000250|UniProtKB:P49005}. SUBUNIT: Component of the tetrameric DNA polymerase delta complex (Pol-delta4), which consists of POLD1/p125, POLD2/p50, POLD3/p66/p68 and POLD4/p12, with POLD1 bearing DNA polymerase and 3' to 5' proofreading exonuclease activities. Within Pol-delta4, directly interacts with POLD1, POLD3 and POLD4. Following stress caused by DNA damaging agents or by replication stress, POLD4 is degraded and Pol-delta4 is converted into a trimeric form of the complex (Pol-delta3), which consists of POLD1, POLD2 and POLD3. Pol-delta3 is the major form occurring at S phase replication sites, as well as DNA damage sites. Also observed as a dimeric complex with POLD2 (Pol-delta2 complex). Pol-delta2 is relatively insensitive to the PCNA stimulation (2-5-fold) compared to Pol-delta4 that is stimulated by over 50-fold. Contrary to the other components of Pol-delta4, does not directly interact with PCNA. As POLD1 and POLD4, directly interacts with WRNIP1; this interaction stimulates DNA polymerase delta-mediated DNA synthesis, independently of the presence of PCNA. This stimulation may be due predominantly to an increase of initiation frequency and also to increased processivity. Directly interacts with POLDIP2 and POLDIP3. Directly interacts with KCTD13/PDIP1; in the presence of PCNA, this interaction may stimulate DNA polymerase activity. Component of the DNA polymerase zeta complex (POLZ), which consists of REV3L, MAD2L2, POLD2 and POLD3, with REV3L bearing DNA polymerase catalytic activity (By similarity). Interacts with KCTD10 (By similarity). {ECO:0000250|UniProtKB:P49005, ECO:0000250|UniProtKB:Q7TPL3}. +Q9EQ28 DPOD3_MOUSE DNA polymerase delta subunit 3 (DNA polymerase delta subunit p66) 462 50,836 Chain (1); Cross-link (5); Erroneous initiation (1); Initiator methionine (1); Modified residue (7); Region (1) FUNCTION: As a component of the trimeric and tetrameric DNA polymerase delta complexes (Pol-delta3 and Pol-delta4, respectively), plays a role in high fidelity genome replication, including in lagging strand synthesis, and repair (PubMed:10219083, PubMed:27524497). Required for optimal Pol-delta activity. Stabilizes the Pol-delta complex and plays a major role in Pol-delta stimulation by PCNA. Pol-delta3 and Pol-delta4 are characterized by the absence or the presence of POLD4. They exhibit differences in catalytic activity. Most notably, Pol-delta3 shows higher proofreading activity than Pol-delta4. Although both Pol-delta3 and Pol-delta4 process Okazaki fragments in vitro, Pol-delta3 may also be better suited to fulfill this task, exhibiting near-absence of strand displacement activity compared to Pol-delta4 and stalling on encounter with the 5'-blocking oligonucleotides. Pol-delta3 idling process may avoid the formation of a gap, while maintaining a nick that can be readily ligated. Along with DNA polymerase kappa, DNA polymerase delta carries out approximately half of nucleotide excision repair (NER) synthesis following UV irradiation. In this context, POLD3, along with PCNA and RFC1-replication factor C complex, is required to recruit POLD1, the catalytic subunit of the polymerase delta complex, to DNA damage sites. Under conditions of DNA replication stress, required for the repair of broken replication forks through break-induced replication (BIR). Involved in the translesion synthesis (TLS) of templates carrying O6-methylguanine or abasic sites performed by Pol-delta4, independently of DNA polymerase zeta (REV3L) or eta (POLH). Facilitates abasic site bypass by DNA polymerase delta by promoting extension from the nucleotide inserted opposite the lesion. Also involved in TLS, as a component of the POLZ complex. Along with POLD2, dramatically increases the efficiency and processivity of DNA synthesis of the minimal DNA polymerase zeta complex, consisting of only REV3L and REV7 (By similarity). {ECO:0000250|UniProtKB:Q15054, ECO:0000269|PubMed:10219083, ECO:0000269|PubMed:27524497}. PTM: Ubiquitinated, but not targeted to the proteasome. Sumoylated. Sumoylation by SUMO3 may be predominant. {ECO:0000250|UniProtKB:Q15054}.; PTM: Phosphorylation at Ser-454 is thought to decrease the affinity for PCNA and Pol-delta4 processivity. May be phosphorylated by CDK1-cyclin-A complex, as well as CDK2-cyclin-A and CDK2-cyclin-E complexes. PCNA interferes with CDK-cyclin phosphorylation. {ECO:0000250|UniProtKB:Q15054}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27524497}. Nucleus {ECO:0000269|PubMed:27524497}. Note=Partially colocalizes with PCNA and POLD1 at S phase replication sites. Recruited to DNA damage sites within 2 hours following UV irradiation. {ECO:0000250|UniProtKB:Q15054}. SUBUNIT: Component of the tetrameric DNA polymerase delta complex (Pol-delta4), which consists of POLD1/p125, POLD2/p50, POLD3/p66/p68 and POLD4/p12, with POLD1 bearing DNA polymerase and 3' to 5' proofreading exonuclease activities (PubMed:27524497). Within this complex, directly interacts with POLD2. Following stress caused by DNA damaging agents or by replication stress, POLD4 is degraded and Pol-delta4 is converted into a trimeric form of the complex (Pol-delta3), which consists of POLD1, POLD2 and POLD3. Pol-delta3 is the major form occurring at S phase replication sites, as well as DNA damage sites. Directly interacts with PCNA, as do POLD1 and POLD4; this interaction stimulates Pol-delta polymerase activity. POLD3 phosphorylation at Ser-454 impairs PCNA binding. Component of the DNA polymerase zeta complex (POLZ), which consists of REV3L, MAD2L2, POLD2 and POLD3, with REV3L bearing DNA polymerase catalytic activity. The DNA polymerase delta complex interacts with POLDIP2; this interaction is probably mediated through direct binding to POLD2 (By similarity). {ECO:0000250|UniProtKB:Q15054, ECO:0000269|PubMed:27524497}. +Q9CWP8 DPOD4_MOUSE DNA polymerase delta subunit 4 (DNA polymerase delta subunit p12) 107 12,403 Chain (1); Motif (1) FUNCTION: As a component of the tetrameric DNA polymerase delta complex (Pol-delta4), plays a role in high fidelity genome replication and repair. Within this complex, increases the rate of DNA synthesis and decreases fidelity by regulating POLD1 polymerase and proofreading 3' to 5' exonuclease activity. Pol-delta4 participates in Okazaki fragment processing, through both the short flap pathway, as well as a nick translation system. Under conditions of DNA replication stress, required for the repair of broken replication forks through break-induced replication (BIR), a mechanism that may induce segmental genomic duplications of up to 200 kb. Involved in Pol-delta4 translesion synthesis (TLS) of templates carrying O6-methylguanine or abasic sites. Its degradation in response to DNA damage is required for the inhibition of fork progression and cell survival. {ECO:0000250|UniProtKB:Q9HCU8}. PTM: Ubiquitinated; undergoes 'Lys-48'-linked polyubiquitination in response to UV irradiation or treatment with an alkylating agent, leading to proteasomal degradation. This modification is mediated, at least in part, by RNF8. {ECO:0000269|PubMed:23233665}.; PTM: Ubiquitinated; undergoes 'Lys-48'-linked ubiquitination in response to UV irradiation, leading to proteasomal degradation. This modification is partly mediated by RNF8 and by the DCX(DTL) E3 ubiquitin ligase complex (also called CRL4(CDT2)). Efficient degradation requires the presence of PCNA and is required for the inhibition of fork progression after DNA damage. {ECO:0000250|UniProtKB:Q9HCU8}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9HCU8}. Note=Partially recruited to DNA damage sites within 2 hours following UV irradiation, before degradation. {ECO:0000250|UniProtKB:Q9HCU8}. SUBUNIT: Component of the tetrameric DNA polymerase delta complex (Pol-delta4), which consists of POLD1/p125, POLD2/p50, POLD3/p66/p68 and POLD4/p12, with POLD1 bearing DNA polymerase and 3' to 5' proofreading exonuclease activities. Within this complex, directly interacts with POLD1 and POLD2. Directly interacts with PCNA, as do POLD1 and POLD3; this interaction stimulates Pol-delta4 polymerase activity. As POLD1 and POLD2, directly interacts with WRNIP1; this interaction stimulates DNA polymerase delta-mediated DNA synthesis, independently of the presence of PCNA, possibly by increasing initiation frequency. Upon genotoxic stress induced by DNA damaging agents or by replication stress, POLD4 is proteolytically degraded and Pol-delta4 is converted into a trimeric form of the complex (Pol-delta3) that has a increased proofreading activity. The DNA polymerase delta complex interacts with POLDIP2; this interaction is probably mediated through direct binding to POLD2. {ECO:0000250|UniProtKB:Q9HCU8}. +Q9WVF7 DPOE1_MOUSE DNA polymerase epsilon catalytic subunit A (EC 2.7.7.7) (DNA polymerase II subunit A) 2283 262,100 Chain (1); Metal binding (8); Modified residue (3); Motif (1); Sequence conflict (11); Zinc finger (1) FUNCTION: Participates in DNA repair and in chromosomal DNA replication. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Catalytic and central component of the epsilon DNA polymerase complex consisting of four subunits: POLE, POLE2, POLE3 and POLE4. Interacts with RAD17 and TOPBP1 (By similarity). {ECO:0000250}. DOMAIN: The DNA polymerase activity domain resides in the N-terminal half of the protein, while the C-terminus is necessary for complexing subunits B and C. The C-terminus may also regulate the catalytic activities of the enzyme.; DOMAIN: The CysB motif binds 1 4Fe-4S cluster and is required for the formation of polymerase complexes. {ECO:0000250}. +O54956 DPOE2_MOUSE DNA polymerase epsilon subunit 2 (EC 2.7.7.7) (DNA polymerase II subunit 2) (DNA polymerase epsilon subunit B) 527 59,387 Chain (1); Sequence conflict (1) FUNCTION: Participates in DNA repair and in chromosomal DNA replication. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Component of the epsilon DNA polymerase complex consisting of four subunits: POLE, POLE2, POLE3 and POLE4. +Q9JKP7 DPOE3_MOUSE DNA polymerase epsilon subunit 3 (EC 2.7.7.7) (DNA polymerase II subunit 3) (DNA polymerase epsilon subunit p17) (NF-YB-like protein) (YB-like protein 1) (YBL1) 145 16,629 Chain (1); Coiled coil (1); Initiator methionine (1); Modified residue (3); Sequence conflict (2) FUNCTION: Forms a complex with DNA polymerase epsilon subunit CHRAC1 and binds naked DNA, which is then incorporated into chromatin, aided by the nucleosome-remodeling activity of ISWI/SNF2H and ACF1. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Component of the epsilon DNA polymerase complex consisting of four subunits: POLE, POLE2, POLE3 and POLE4. Interaction with POLE4 is a prerequisite for further binding with POLE and POLE2. Interacts with CHRAC1. Together with CHRAC1, ACF1 and ISWI/SNF2H proteins, it forms the ISWI chromatin-remodeling complex, CHRAC (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed. +Q9CQ36 DPOE4_MOUSE DNA polymerase epsilon subunit 4 (EC 2.7.7.7) (DNA polymerase II subunit 4) (DNA polymerase epsilon subunit p12) 118 12,240 Chain (1); Initiator methionine (1); Modified residue (3) FUNCTION: May play a role in allowing polymerase epsilon to carry out its replication and/or repair function. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Component of the epsilon DNA polymerase complex consisting of four subunits: POLE, POLE2, POLE3 and POLE4. Interaction with POLE3 is a prerequisite for further binding with POLE and POLE2 (By similarity). {ECO:0000250}. +P54099 DPOG1_MOUSE DNA polymerase subunit gamma-1 (EC 2.7.7.7) (Mitochondrial DNA polymerase catalytic subunit) (PolG-alpha) 1218 136,758 Chain (1); Compositional bias (1); Erroneous gene model prediction (1); Frameshift (1); Sequence conflict (14) FUNCTION: Involved in the replication of mitochondrial DNA. Associates with mitochondrial DNA (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion matrix, mitochondrion nucleoid {ECO:0000250}. SUBUNIT: Heterotrimer composed of a catalytic subunit and a homodimer of accessory subunits. +Q9QZM2 DPOG2_MOUSE DNA polymerase subunit gamma-2, mitochondrial (EC 2.7.7.7) (DNA polymerase gamma accessory 55 kDa subunit) (p55) (Mitochondrial DNA polymerase accessory subunit) (MtPolB) (PolG-beta) 459 51,467 Beta strand (18); Chain (1); Helix (18); Sequence conflict (2); Transit peptide (1); Turn (5) FUNCTION: Mitochondrial polymerase processivity subunit. Stimulates the polymerase and exonuclease activities, and increases the processivity of the enzyme. Binds to ss-DNA. SUBCELLULAR LOCATION: Mitochondrion. SUBUNIT: Heterotrimer composed of a catalytic subunit and a homodimer of accessory subunits. {ECO:0000269|PubMed:11172710}. +P33609 DPOLA_MOUSE DNA polymerase alpha catalytic subunit (EC 2.7.7.7) (DNA polymerase alpha catalytic subunit p180) 1465 167,340 Chain (1); Metal binding (8); Modified residue (5); Motif (1); Natural variant (1); Region (2); Zinc finger (1) FUNCTION: Plays an essential role in the initiation of DNA replication. During the S phase of the cell cycle, the DNA polymerase alpha complex (composed of a catalytic subunit POLA1/p180, a regulatory subunit POLA2/p70 and two primase subunits PRIM1/p49 and PRIM2/p58) is recruited to DNA at the replicative forks via direct interactions with MCM10 and WDHD1. The primase subunit of the polymerase alpha complex initiates DNA synthesis by oligomerising short RNA primers on both leading and lagging strands. These primers are initially extended by the polymerase alpha catalytic subunit and subsequently transferred to polymerase delta and polymerase epsilon for processive synthesis on the lagging and leading strand, respectively. The reason this transfer occurs is because the polymerase alpha has limited processivity and lacks intrinsic 3' exonuclease activity for proofreading error, and therefore is not well suited for replicating long complexes. In the cytosol, responsible for a substantial proportion of the physiological concentration of cytosolic RNA:DNA hybrids, which are necessary to prevent spontaneous activation of type I interferon responses. {ECO:0000250|UniProtKB:P09884}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P09884}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P09884}. Note=In the cytosol, colocalizes with RNA:DNA hybrids with a speckled pattern. {ECO:0000250|UniProtKB:P09884}. SUBUNIT: The DNA polymerase alpha complex is composed of four subunits: the catalytic subunit POLA1, the regulatory subunit POLA2, and the small and the large primase subunits PRIM1 and PRIM2 respectively. Interacts with PARP1; this interaction functions as part of the control of replication fork progression. Interacts with MCM10 and WDHD1; these interactions recruit the polymerase alpha complex to the pre-replicative complex bound to DNA. Interacts with RPA1; this interaction stabilizes the replicative complex and reduces the misincorporation rate of DNA polymerase alpha by acting as a fidelity clamp (By similarity). {ECO:0000250}. DOMAIN: The CysB motif binds 1 4Fe-4S cluster and is required for the formation of polymerase complexes. {ECO:0000250}. +Q8K409 DPOLB_MOUSE DNA polymerase beta (EC 2.7.7.7) (EC 4.2.99.-) 335 38,288 Active site (1); Chain (1); Cross-link (3); Frameshift (1); Metal binding (8); Modified residue (3); Region (1) FUNCTION: Repair polymerase that plays a key role in base-excision repair. Has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity that removes the 5' sugar phosphate and also acts as a DNA polymerase that adds one nucleotide to the 3' end of the arising single-nucleotide gap. Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases (By similarity). {ECO:0000250}. PTM: Methylation by PRMT6 stimulates the polymerase activity by enhancing DNA binding and processivity. {ECO:0000250}.; PTM: Ubiquitinated at Lys-41, Lys-61 and Lys-81: monoubiquitinated by HUWE1/ARF-BP1. Monoubiquitinated protein is then the target of STUB1/CHIP, which catalyzes polyubiquitination from monoubiquitin, leading to degradation by the proteasome. USP47 mediates the deubiquitination of monoubiquitinated protein, preventing polyubiquitination by STUB1/CHIP and its subsequent degradation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Cytoplasmic in normal conditions. Translocates to the nucleus following DNA damage (By similarity). {ECO:0000250}. SUBUNIT: Monomer. Interacts with APEX1, HUWE1/ARF-BP1, STUB1/CHIP and USP47 (By similarity). Interacts with FAM168A (By similarity). {ECO:0000250|UniProtKB:P06746}. DOMAIN: Residues 239-252 form a flexible loop which appears to affect the polymerase fidelity. {ECO:0000250}. +Q9QXE2 DPOLL_MOUSE DNA polymerase lambda (Pol Lambda) (EC 2.7.7.7) (EC 4.2.99.-) (DNA polymerase kappa) 573 62,943 Active site (1); Binding site (2); Chain (1); Domain (1); Metal binding (3); Nucleotide binding (2); Region (4) FUNCTION: DNA polymerase that functions in several pathways of DNA repair. Involved in base excision repair (BER) responsible for repair of lesions that give rise to abasic (AP) sites in DNA. Also contributes to DNA double-strand break repair by non-homologous end joining and homologous recombination. Has both template-dependent and template-independent (terminal transferase) DNA polymerase activities. Has also a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity. {ECO:0000250|UniProtKB:Q9UGP5}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UGP5}. SUBUNIT: Binds PCNA. {ECO:0000250|UniProtKB:Q9UGP5}. +Q9JIW4 DPOLM_MOUSE DNA-directed DNA/RNA polymerase mu (Pol Mu) (EC 2.7.7.7) (Terminal transferase) 496 55,490 Beta strand (5); Chain (1); Domain (1); Helix (18); Metal binding (5); Modified residue (1); Region (1); Sequence conflict (2); Site (1); Turn (1) FUNCTION: Gap-filling polymerase involved in repair of DNA double-strand breaks by non-homologous end joining (NHEJ). Participates in immunoglobulin (Ig) light chain gene rearrangement in V(D)J recombination. {ECO:0000269|PubMed:16860755, ECO:0000269|PubMed:17483519}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +Q8CGS6 DPOLQ_MOUSE DNA polymerase theta (EC 2.7.7.7) (Chromosome aberrations occurring spontaneously protein 1) (DNA polymerase eta) 2544 280,714 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (2); Modified residue (1); Motif (1); Mutagenesis (3); Nucleotide binding (1); Region (4) FUNCTION: DNA polymerase that promotes microhomology-mediated end-joining (MMEJ), an alternative non-homologous end-joining (NHEJ) machinery triggered in response to double-strand breaks in DNA. MMEJ is an error-prone repair pathway that produces deletions of sequences from the strand being repaired and promotes genomic rearrangements, such as telomere fusions, some of them leading to cellular transformation (PubMed:25275444, PubMed:25642963). POLQ acts as an inhibitor of homology-recombination repair (HR) pathway by limiting RAD51 accumulation at resected ends (PubMed:25642963). POLQ-mediated MMEJ may be required to promote the survival of cells with a compromised HR repair pathway, thereby preventing genomic havoc by resolving unrepaired lesions (PubMed:25642963). The polymerase acts by binding directly the 2 ends of resected double-strand breaks, allowing microhomologous sequences in the overhangs to form base pairs. It then extends each strand from the base-paired region using the opposing overhang as a template. Requires partially resected DNA containing 2 to 6 base pairs of microhomology to perform MMEJ. The polymerase activity is highly promiscuous: unlike most polymerases, promotes extension of ssDNA and partial ssDNA (pssDNA) substrates. Also exhibits low-fidelity DNA synthesis, translesion synthesis and lyase activity, and it is implicated in interstrand-cross-link repair, base excision repair and DNA end-joining (By similarity). Involved in somatic hypermutation of immunoglobulin genes, a process that requires the activity of DNA polymerases to ultimately introduce mutations at both A/T and C/G base pairs (PubMed:16222339, PubMed:16172387, PubMed:16890500, PubMed:17449470). However, POLQ does not play a major role in somatic hypermutation (PubMed:18485835). {ECO:0000250|UniProtKB:O75417, ECO:0000269|PubMed:16172387, ECO:0000269|PubMed:16222339, ECO:0000269|PubMed:16890500, ECO:0000269|PubMed:17449470, ECO:0000269|PubMed:18485835, ECO:0000269|PubMed:21883722, ECO:0000269|PubMed:25275444, ECO:0000269|PubMed:25642963}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O18475}. Chromosome {ECO:0000250|UniProtKB:O75417}. Note=Enriched in chromatin in response to ultaviolet (UV) light. Binds to chromatin during early G1. {ECO:0000250|UniProtKB:O75417}. SUBUNIT: Homomultimer; forms dimers and multimers. Interacts with RAD51. Interacts with ORC2 and ORC4. {ECO:0000250|UniProtKB:O75417}. DOMAIN: The loop 2 region is involved in the binding of the 2 ends of resected double-strand breaks and homomultimerization. {ECO:0000250|UniProtKB:O75417}. +Q8BZJ8 CH034_MOUSE Uncharacterized protein C8orf34 homolog 459 51,086 Alternative sequence (6); Chain (1); Compositional bias (1) +Q7TS74 CKP2L_MOUSE Cytoskeleton-associated protein 2-like (Radial fiber and mitotic spindle protein) (Radmis) 745 82,999 Alternative sequence (2); Chain (1); Cross-link (2); Modified residue (1); Motif (1); Mutagenesis (1); Sequence conflict (4) FUNCTION: Microtubule-associated protein required for mitotic spindle formation and cell-cycle progression in neural progenitor cells. {ECO:0000269|PubMed:24260314}. PTM: Ubiquitinated by the anaphase promoting complex/cyclosome (APC/C). {ECO:0000269|PubMed:24260314}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:24260314, ECO:0000269|PubMed:25439729}. Note=Uniformly distributed along each microtubule bundle of spindles in addition to centrioles during mitosis, expression promptly diminishes at interphase. DOMAIN: The KEN box is required for the association with the APC/C-Cdh1 complex, ubiquitination and degradation. {ECO:0000269|PubMed:24260314}. TISSUE SPECIFICITY: Highly expressed in regions of active neurogenesis and neural stem/progenitor cells (NSPCs), both embryonic and adult, not detected in lung, liver, kidney, heart, and skeletal muscle. {ECO:0000269|PubMed:24260314}. +P61025 CKS1_MOUSE Cyclin-dependent kinases regulatory subunit 1 (CKS-1) (Sid 1334) 79 9,660 Chain (1); Initiator methionine (1); Modified residue (1) FUNCTION: Binds to the catalytic subunit of the cyclin dependent kinases and is essential for their biological function. {ECO:0000250}. SUBUNIT: Forms a homohexamer that can probably bind six kinase subunits. {ECO:0000250}. +Q8BHN7 CL029_MOUSE Uncharacterized protein C12orf29 homolog 327 37,418 Alternative sequence (2); Chain (1); Sequence conflict (1) +Q9D113 DNLZ_MOUSE DNL-type zinc finger protein (Hsp70-escort protein 1) (HEP1) (mtHsp70-escort protein) 177 19,403 Chain (1); Transit peptide (1); Zinc finger (1) FUNCTION: May function as a co-chaperone towards HSPA9/mortalin which, by itself, is prone to self-aggregation. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. SUBUNIT: Oligomerizes in a concentration-dependent fashion. Interacts with HSPA9 (By similarity). {ECO:0000250}. +Q8K1M6 DNM1L_MOUSE Dynamin-1-like protein (EC 3.6.5.5) (Dynamin family member proline-rich carboxyl-terminal domain less) (Dymple) (Dynamin-related protein 1) 742 82,658 Alternative sequence (7); Chain (1); Cross-link (8); Domain (2); Glycosylation (2); Modified residue (7); Mutagenesis (1); Nucleotide binding (3); Region (10); Sequence conflict (3) FUNCTION: Functions in mitochondrial and peroxisomal division. Mediates membrane fission through oligomerization into membrane-associated tubular structures that wrap around the scission site to constrict and sever the mitochondrial membrane through a GTP hydrolysis-dependent mechanism. The specific recruitment at scission sites is mediated by membrane receptors like MFF, MIEF1 and MIEF2 for mitochondrial membranes. While the recruitment by the membrane receptors is GTP-dependent, the following hydrolysis of GTP induces the dissociation from the receptors and allows DNM1L filaments to curl into closed rings that are probably sufficient to sever a double membrane. Through its function in mitochondrial division, ensures the survival of at least some types of postmitotic neurons, including Purkinje cells, by suppressing oxidative damage. Required for normal brain development, including that of cerebellum. Facilitates developmentally regulated apoptosis during neural tube formation. Required for a normal rate of cytochrome c release and caspase activation during apoptosis; this requirement may depend upon the cell type and the physiological apoptotic cues. Plays an important role in mitochondrial fission during mitosis. Required for formation of endocytic vesicles. Proposed to regulate synaptic vesicle membrane dynamics through association with BCL2L1 isoform Bcl-X(L) which stimulates its GTPase activity in synaptic vesicles; the function may require its recruitment by MFF to clathrin-containing vesicles. Required for programmed necrosis execution. {ECO:0000250|UniProtKB:O00429, ECO:0000269|PubMed:19578372, ECO:0000269|PubMed:19752021, ECO:0000269|PubMed:22564413, ECO:0000269|PubMed:23283981, ECO:0000269|PubMed:24508339}. PTM: Phosphorylation/dephosphorylation events on two sites near the GED domain regulate mitochondrial fission. Phosphorylation on Ser-643 inhibits mitochondrial fission probably through preventing intramolecular interaction. Dephosphorylated on this site by PPP3CA which promotes mitochondrial fission. Phosphorylation on Ser-622 also promotes mitochondrial fission (By similarity). {ECO:0000250}.; PTM: Sumoylated on various lysine residues within the B domain, probably by MUL1. Sumoylation positively regulates mitochondrial fission. Desumoylated by SENP5 during G2/M transition of mitosis. Appears to be linked to its catalytic activity (By similarity). {ECO:0000250}.; PTM: S-nitrosylation increases DNM1L dimerization, mitochondrial fission and causes neuronal damage. {ECO:0000250}.; PTM: O-GlcNAcylation augments the level of the GTP-bound active form of DRP1 and induces translocation from the cytoplasm to mitochondria in cardiomyocytes. It also decreases phosphorylation at Ser-643 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol. Golgi apparatus {ECO:0000250}. Endomembrane system; Peripheral membrane protein. Mitochondrion outer membrane; Peripheral membrane protein. Peroxisome {ECO:0000250}. Membrane, clathrin-coated pit {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250}. Note=Mainly cytosolic. Translocated to the mitochondrial membrane through O-GlcNAcylation and interaction with FIS1. Colocalized with MARCH5 at mitochondrial membrane. Localizes to mitochondria at sites of division. Localizes to mitochondria following necrosis induction. Associated with peroxisomal membranes, partly recruited there by PEX11B. May also be associated with endoplasmic reticulum tubules and cytoplasmic vesicles and found to be perinuclear. In some cell types, localizes to the Golgi complex (By similarity). Recruited to the mitochondrial outer membrane by interaction with MIEF1. Binds to phospholipid membranes. {ECO:0000250}. SUBUNIT: Homotetramer; dimerizes through the N-terminal GTP-middle region of one molecule binding to the GED domain of another DNM1L molecule. Oligomerizes in a GTP-dependent manner to form membrane-associated tubules with a spiral pattern. Interacts with GSK3B and MARCH5. Interacts (via the GTPase and B domains) with UBE2I; the interaction promotes sumoylation of DNM1L, mainly in its B domain. Interacts with PPP3CA; the interaction dephosphorylates DNM1L and regulates its transition to mitochondria. Interacts with BCL2L1 isoform BCL-X(L) and CLTA; DNM1L and BCL2L1 isoform BCL-X(L) may form a complex in synaptic vesicles that also contains clathrin and MFF. Interacts with FIS1. Interacts with MIEF2 and MIEF1; GTP-dependent this regulates GTP hydrolysis and DNM1L oligomerization (PubMed:24508339). Interacts with PGAM5; this interaction leads to dephosphorylation at Ser-656 and activation of GTPase activity and eventually to mitochondria fragmentation. {ECO:0000250|UniProtKB:O00429, ECO:0000269|PubMed:24508339}. DOMAIN: The GED domain folds back to interact, in cis, with the GTP-binding domain and middle domain, and interacts, in trans, with the GED domains of other DNM1L molecules, and is thus critical for activating GTPase activity and for DNM1L dimerization. {ECO:0000250|UniProtKB:O00429}. TISSUE SPECIFICITY: Expressed in the cerebellum and in several regions of the cerebrum and diencephalon. Strongly expressed in the cerebellar Purkinje cells and in the pontile giant neurons. {ECO:0000269|PubMed:9422767}. +O88508 DNM3A_MOUSE DNA (cytosine-5)-methyltransferase 3A (Dnmt3a) (EC 2.1.1.37) (DNA methyltransferase MmuIIIA) (DNA MTase MmuIIIA) (M.MmuIIIA) 908 101,672 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Cross-link (1); Domain (3); Erroneous initiation (1); Modified residue (8); Mutagenesis (19); Region (5); Sequence conflict (6); Zinc finger (2) FUNCTION: Required for genome-wide de novo methylation and is essential for the establishment of DNA methylation patterns during development. DNA methylation is coordinated with methylation of histones. It modifies DNA in a non-processive manner and also methylates non-CpG sites. May preferentially methylate DNA linker between 2 nucleosomal cores and is inhibited by histone H1. Plays a role in paternal and maternal imprinting. Required for methylation of most imprinted loci in germ cells. Acts as a transcriptional corepressor for ZBTB18. Recruited to trimethylated 'Lys-36' of histone H3 (H3K36me3) sites. Can actively repress transcription through the recruitment of HDAC activity. {ECO:0000269|PubMed:10555141, ECO:0000269|PubMed:11350943, ECO:0000269|PubMed:11399089, ECO:0000269|PubMed:11919202, ECO:0000269|PubMed:15215868, ECO:0000269|PubMed:16567415, ECO:0000269|PubMed:17713477, ECO:0000269|PubMed:18823905}. PTM: Sumoylated; sumoylation disrupts the ability to interact with histone deacetylases (HDAC1 and HDAC2) and repress transcription. {ECO:0000269|PubMed:14752048}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12138111, ECO:0000269|PubMed:15456878, ECO:0000269|PubMed:20547484}. Cytoplasm {ECO:0000250}. Note=Accumulates in the major satellite repeats at pericentric heterochromatin. SUBUNIT: Heterotetramer composed of 1 DNMT3A homodimer and 2 DNMT3L subunits (DNMT3L-DNMT3A-DNMT3A-DNMT3L). Interacts with DNMT1 and DNMT3B. Interacts with MPHOSPH8. Interacts with histone H3 that is not methylated at 'Lys-4' (H3K4) (By similarity). Binds the ZBTB18 transcriptional repressor. Interacts with SETDB1. Associates with HDAC1 through its ADD domain. Interacts with the PRC2/EED-EZH2 complex. Interacts with UBC9, PIAS1 and PIAS2. {ECO:0000250, ECO:0000269|PubMed:11350943, ECO:0000269|PubMed:12616525, ECO:0000269|PubMed:14752048, ECO:0000269|PubMed:16357870, ECO:0000269|PubMed:19798101}. DOMAIN: The PWWP domain is essential for targeting to pericentric heterochromatin. It specifically recognizes and binds trimethylated 'Lys-36' of histone H3 (H3K36me3) (PubMed:20547484). {ECO:0000269|PubMed:20547484}. TISSUE SPECIFICITY: Isoform 1 is expressed ubiquitously at low levels. Expression of isoform 2 is restricted to tissues containing cells which are undergoing active de novo methylation, including spleen, testis and thymus. {ECO:0000269|PubMed:12138111}. +O88509 DNM3B_MOUSE DNA (cytosine-5)-methyltransferase 3B (Dnmt3b) (EC 2.1.1.37) (DNA methyltransferase MmuIIIB) (DNA MTase MmuIIIB) (M.MmuIIIB) 859 97,228 Active site (1); Alternative sequence (2); Beta strand (5); Binding site (1); Chain (1); Compositional bias (1); Cross-link (2); Domain (3); Helix (7); Modified residue (5); Mutagenesis (9); Region (5); Sequence conflict (2); Turn (3); Zinc finger (2) FUNCTION: Required for genome-wide de novo methylation and is essential for the establishment of DNA methylation patterns during development. DNA methylation is coordinated with methylation of histones. May preferentially methylates nucleosomal DNA within the nucleosome core region. May function as transcriptional co-repressor by associating with CBX4 and independently of DNA methylation. Seems to be involved in gene silencing. In association with DNMT1 and via the recruitment of CTCFL/BORIS, involved in activation of BAG1 gene expression by modulating dimethylation of promoter histone H3 at H3K4 and H3K9. Function as transcriptional corepressor by associating with ZHX1 (By similarity). Required for DUX4 silencing in somatic cells (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9UBC3, ECO:0000269|PubMed:10555141, ECO:0000269|PubMed:11836534, ECO:0000269|PubMed:11919202, ECO:0000269|PubMed:16567415, ECO:0000269|PubMed:18056424, ECO:0000269|PubMed:18567530}. PTM: Sumoylated. {ECO:0000250}.; PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15456878}. Note=Accumulates in the major satellite repeats at pericentric heterochromatin. SUBUNIT: Interacts with CBX4, DNMT1, DNMT3A, SETDB1, UBE2I9, UBL1 and ZHX1 (By similarity). Interacts with SUV39H1 and BAZ2A/TIP5. Interacts with the PRC2/EED-EZH2 complex. Interacts with UHRF1. {ECO:0000250, ECO:0000269|PubMed:11836534, ECO:0000269|PubMed:12867029, ECO:0000269|PubMed:16085498, ECO:0000269|PubMed:16357870, ECO:0000269|PubMed:18567530, ECO:0000269|PubMed:19798101}. DOMAIN: The PWWP domain is essential for targeting to pericentric heterochromatin. +P0DOY1 DNM3C_MOUSE DNA (cytosine-5)-methyltransferase 3C (Dnmt3c) (EC 2.1.1.37) 740 82,921 Active site (1); Binding site (1); Chain (1); Domain (2); Mutagenesis (2); Region (3); Zinc finger (2) FUNCTION: DNA methyltransferase that specifically methylates the promoters of evolutionarily young retrotransposons in the male germline (PubMed:27856912, PubMed:28854222). De novo methylation and subsequent repression of transposable elements prevents their mobilization, which is essential for germline integrity (PubMed:27856912, PubMed:28854222). {ECO:0000269|PubMed:27856912, ECO:0000269|PubMed:28854222}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: Specifically expressed in testis. {ECO:0000269|PubMed:27856912}. +Q9CWR8 DNM3L_MOUSE DNA (cytosine-5)-methyltransferase 3-like 421 47,993 Chain (1); Domain (1); Mutagenesis (1); Zinc finger (2) FUNCTION: Catalytically inactive regulatory factor of DNA methyltransferases that can either promote or inhibit DNA methylation depending on the context (PubMed:11719692, PubMed:15318244, PubMed:15671018, PubMed:24074865). Essential for the function of DNMT3A and DNMT3B: activates DNMT3A and DNMT3B by binding to their catalytic domain (PubMed:15671018). Acts by accelerating the binding of DNA and S-adenosyl-L-methionine (AdoMet) to the methyltransferases and dissociates from the complex after DNA binding to the methyltransferases (PubMed:15671018). Recognizes unmethylated histone H3 lysine 4 (H3K4me0) and induces de novo DNA methylation by recruitment or activation of DNMT3 (By similarity). Plays a key role in embryonic stem cells and germ cells (PubMed:11719692, PubMed:15318244, PubMed:24074865). In germ cells, required for the methylation of imprinted loci together with DNMT3A (PubMed:11719692). In male germ cells, specifically required to methylate retrotransposons, preventing their mobilization (PubMed:15318244). Plays a key role in embryonic stem cells (ESCs) by acting both as an positive and negative regulator of DNA methylation (PubMed:24074865). While it promotes DNA methylation of housekeeping genes together with DNMT3A and DNMT3B, it also acts as an inhibitor of DNA methylation at the promoter of bivalent genes (PubMed:24074865). Interacts with the EZH2 component of the PRC2/EED-EZH2 complex, preventing interaction of DNMT3A and DNMT3B with the PRC2/EED-EZH2 complex, leading to maintain low methylation levels at the promoters of bivalent genes (PubMed:24074865). Promotes differentiation of ESCs into primordial germ cells by inhibiting DNA methylation at the promoter of RHOX5, thereby activating its expression (PubMed:24074865). {ECO:0000250|UniProtKB:Q9UJW3, ECO:0000269|PubMed:11719692, ECO:0000269|PubMed:15318244, ECO:0000269|PubMed:15671018, ECO:0000269|PubMed:24074865}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Homodimer (By similarity). Heterotetramer composed of 1 DNMT3A homodimer and 2 DNMT3L subunits (DNMT3L-DNMT3A-DNMT3A-DNMT3L) (By similarity). Interacts with histone H3 (via N-terminus); interaction is strongly inhibited by methylation at lysine 4 (H3K4me) (By similarity). Interacts with EZH2; the interaction is direct (PubMed:24074865). {ECO:0000250|UniProtKB:Q9UJW3, ECO:0000269|PubMed:24074865}. TISSUE SPECIFICITY: Expressed in testis, thymus, ovary, and heart (PubMed:11306809). {ECO:0000269|PubMed:11306809}. +Q6TXD4 DNMBP_MOUSE Dynamin-binding protein (Scaffold protein Tuba) 1580 177,277 Alternative sequence (3); Chain (1); Coiled coil (1); Compositional bias (1); Domain (8); Erroneous initiation (1); Frameshift (1); Modified residue (2); Sequence conflict (2) FUNCTION: Scaffold protein that links dynamin with actin-regulating proteins. May play a role in membrane trafficking between the cell surface and the Golgi. {ECO:0000269|PubMed:14506234}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14506234}. Golgi apparatus, Golgi stack {ECO:0000269|PubMed:14506234}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:14506234}. Cell junction, synapse {ECO:0000269|PubMed:14506234}. Note=Localized to synapses and Golgi stacks. SUBUNIT: Interacts with DNM1 via its N-terminal SH3 domains. The C-terminal SH3 domain binds a complex containing actin, tubulin, Hsp70 and actin-regulatory proteins, such as ENAH, EVL, WASL, WIRE, CR16, WAVE1 and NAP1L1. Interacts with FASLG (By similarity). {ECO:0000250}. +P13864 DNMT1_MOUSE DNA (cytosine-5)-methyltransferase 1 (Dnmt1) (Met-1) (EC 2.1.1.37) (DNA methyltransferase MmuI) (DNA MTase MmuI) (M.MmuI) (MCMT) 1620 183,189 Active site (1); Alternative sequence (1); Beta strand (59); Binding site (2); Chain (1); Cross-link (2); Domain (4); Erroneous initiation (1); Helix (42); Metal binding (4); Modified residue (32); Motif (1); Mutagenesis (5); Region (15); Repeat (7); Sequence conflict (20); Turn (17); Zinc finger (1) FUNCTION: Methylates CpG residues. Preferentially methylates hemimethylated DNA. Associates with DNA replication sites in S phase maintaining the methylation pattern in the newly synthesized strand, that is essential for epigenetic inheritance. Associates with chromatin during G2 and M phases to maintain DNA methylation independently of replication. It is responsible for maintaining methylation patterns established in development. DNA methylation is coordinated with methylation of histones. Mediates transcriptional repression by direct binding to HDAC2. In association with DNMT3B and via the recruitment of CTCFL/BORIS, involved in activation of BAG1 gene expression by modulating dimethylation of promoter histone H3 at H3K4 and H3K9. Probably forms a corepressor complex required for activated KRAS-mediated promoter hypermethylation and transcriptional silencing of tumor suppressor genes (TSGs) or other tumor-related genes in colorectal cancer (CRC) cells (By similarity). Also required to maintain a transcriptionally repressive state of genes in undifferentiated embryonic stem cells (ESCs) (By similarity). Associates at promoter regions of tumor suppressor genes (TSGs) leading to their gene silencing (By similarity). Promotes tumor growth (By similarity). {ECO:0000250|UniProtKB:P26358, ECO:0000269|PubMed:11290321, ECO:0000269|PubMed:15550930, ECO:0000269|PubMed:17576694}. PTM: Sumoylated. {ECO:0000250}.; PTM: Phosphorylation at Ser-146 by CK1 reduces DNA-binding activity. {ECO:0000269|PubMed:17965600, ECO:0000269|PubMed:20192920, ECO:0000269|PubMed:9211941}.; PTM: Acetylation on multiple lysines, mainly by KAT2B/PCAF, regulates cell cycle G(2)/M transition. Deacetylation of Lys-1352 and Lys-1418 by SIRT1 increases methyltransferase activity (By similarity). {ECO:0000250}.; PTM: Phosphorylation of Ser-152 by CDKs is important for enzymatic activity and protein stability. Phosphorylation of Ser-140 by AKT1 prevents methylation by SETD7 therebye increasing DNMT1 stability (By similarity). {ECO:0000250}.; PTM: Methylation at Lys-139 by SETD7 promotes DNMT1 proteasomal degradation. {ECO:0000250}.; PTM: Ubiquitinated by UHRF1; interaction with USP7 counteracts ubiquitination by UHRF1 by promoting deubiquitination and preventing degradation by the proteasome. {ECO:0000269|PubMed:21268065}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11290321}. Cytoplasm {ECO:0000269|PubMed:11290321}. Note=It is nucleoplasmic through most of the cell cycle and associates with replication foci during S-phase. In germ cells, spermatogonia, preleptotene and leptotene spermatocytes all express high levels of nuclear protein, while the protein is not detected in pachytene spermatocytes, despite the fact they expressed high levels of mRNA. In females, the protein is not detected in non-growing oocytes, in contrast to the growing oocytes. During the growing, the protein is no longer detectable in nuclei but accumulates to very high levels first throughout the cytoplasm. At the time of ovulation, all the protein is cytoplasmic and is actively associated with the oocyte cortex. After fecondation, in the preimplantation embryo, the protein remains cytoplasmic and after implantation, it is exclusively nuclear in all tissue types. Isoform 2 is sequestered in the cytoplasm of maturing oocytes and of preimplantation embryos, except for the 8-cell stage, while isoform 1 is exclusively nuclear. SUBUNIT: Homodimer (By similarity). Forms a stable complex with E2F1, BB1 and HDAC1 (By similarity). Forms a complex with DMAP1 and HDAC2, with direct interaction (PubMed:10888872). Interacts with the PRC2/EED-EZH2 complex (PubMed:16357870). Probably part of a corepressor complex containing ZNF304, TRIM28, SETDB1 and DNMT1 (By similarity). Interacts with UHRF1; promoting its recruitment to hemimethylated DNA (PubMed:21268065). Interacts with USP7, promoting its deubiquitination (PubMed:21268065). Interacts with BAZ2A/TIP5 (PubMed:16085498). Interacts with PCNA (By similarity). Interacts with MBD2 and MBD3 (By similarity). Interacts with DNMT3A and DNMT3B (By similarity). Interacts with UBC9 (By similarity). Interacts with HDAC1 (PubMed:10615135). Interacts with CSNK1D (PubMed:20192920). {ECO:0000250|UniProtKB:P26358, ECO:0000269|PubMed:10615135, ECO:0000269|PubMed:10888872, ECO:0000269|PubMed:16085498, ECO:0000269|PubMed:16357870, ECO:0000269|PubMed:20192920, ECO:0000269|PubMed:21268065}. DOMAIN: The N-terminal part is required for homodimerization and acts as a regulatory domain.; DOMAIN: The CXXC-type zinc finger specifically binds to unmethylated CpG dinucleotides, positioning the autoinhibitory linker between the DNA and the active site, thus providing a mechanism to ensure that only hemimethylated CpG dinucleotides undergo methylation. {ECO:0000269|PubMed:21163962}. TISSUE SPECIFICITY: Isoform 1 is expressed in embryonic stem cells and in somatic tissues. Isoform 2 is expressed in oocytes, preimplantation embryos, testis and in skeletal muscle during myogenesis. +Q9Z2W0 DNPEP_MOUSE Aspartyl aminopeptidase (EC 3.4.11.21) 473 52,207 Binding site (6); Chain (1); Metal binding (6); Modified residue (1); Sequence conflict (2) FUNCTION: Aminopeptidase with specificity towards an acidic amino acid at the N-terminus. Likely to play an important role in intracellular protein and peptide metabolism (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Tetrahedron-shaped homododecamer built from six homodimers. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. +Q80VJ3 DNPH1_MOUSE 2'-deoxynucleoside 5'-phosphate N-hydrolase 1 (EC 3.2.2.-) (c-Myc-responsive protein Rcl) 173 18,977 Binding site (3); Chain (1); Initiator methionine (1); Modified residue (7); Region (2); Sequence conflict (2) FUNCTION: Catalyzes the cleavage of the N-glycosidic bond of deoxyribonucleoside 5'-monophosphates to yield deoxyribose 5-phosphate and a purine or pyrimidine base. Deoxyribonucleoside 5'-monophosphates containing purine bases are preferred to those containing pyrimidine bases. {ECO:0000255|HAMAP-Rule:MF_03036}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03036}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03036}. SUBUNIT: Monomer and homodimer. {ECO:0000255|HAMAP-Rule:MF_03036}. +P56542 DNS2A_MOUSE Deoxyribonuclease-2-alpha (EC 3.1.22.1) (Acid DNase) (Deoxyribonuclease II alpha) (DNase II alpha) (Lysosomal DNase II) 353 38,811 Active site (1); Chain (1); Disulfide bond (3); Glycosylation (4); Signal peptide (1) FUNCTION: Hydrolyzes DNA under acidic conditions with a preference for double-stranded DNA. Plays a major role in the degradation of nuclear DNA in cellular apoptosis during development. Necessary for proper fetal development and for definitive erythropoiesis in fetal liver, where it degrades nuclear DNA expelled from erythroid precursor cells. {ECO:0000269|PubMed:11375492, ECO:0000269|PubMed:12181746}. SUBCELLULAR LOCATION: Lysosome. TISSUE SPECIFICITY: Highly expressed in fetal liver macrophages. {ECO:0000269|PubMed:11375492}. DISEASE: Note=Absence of Dnase2 is a cause of severe fetal anemia and of perinatal lethality due to malformation of the diaphragm. {ECO:0000269|PubMed:11375492, ECO:0000269|PubMed:12181746}. +Q9QY48 DNS2B_MOUSE Deoxyribonuclease-2-beta (EC 3.1.22.1) (DNase II-like acid DNase) (DNase2-like acid DNase) (Deoxyribonuclease II beta) (DNase II beta) (Endonuclease DLAD) 354 40,794 Chain (1); Glycosylation (9); Sequence conflict (1); Signal peptide (1) FUNCTION: Hydrolyzes DNA under acidic conditions. Does not require divalent cations for activity. Participates in the degradation of nuclear DNA during lens cell differentiation. {ECO:0000269|PubMed:10497274, ECO:0000269|PubMed:12944971}. SUBCELLULAR LOCATION: Lysosome {ECO:0000305}. TISSUE SPECIFICITY: Highly expressed in the eye lens. Detected in liver, but not in the other tissues tested. {ECO:0000269|PubMed:10497274, ECO:0000269|PubMed:12944971}. +Q9D7J6 DNSL1_MOUSE Deoxyribonuclease-1-like 1 (EC 3.1.21.-) (DNase X) (Deoxyribonuclease I-like 1) (DNase I-like 1) 314 35,604 Active site (2); Chain (1); Disulfide bond (1); Glycosylation (3); Signal peptide (1) SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in heart and skeletal muscles. Low expression in brain and thymus. Intermediated expression in other tissues. {ECO:0000269|PubMed:16107205}. +Q9D1G0 DNSL2_MOUSE Deoxyribonuclease-1-like 2 (EC 3.1.21.-) (Deoxyribonuclease I-like 2) (DNase I-like 2) 278 31,138 Active site (2); Chain (1); Disulfide bond (1); Sequence conflict (2); Signal peptide (1) FUNCTION: Divalent cation-dependent acid DNA endonuclease involved in the breakdown of the nucleus during corneocyte formation of epidermal keratinocytes. May play an immune role by eliminating harmful DNA released into the extracellular environment by damaged epidermal cells (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Secreted {ECO:0000305}. +O55070 DNSL3_MOUSE Deoxyribonuclease gamma (DNase gamma) (EC 3.1.21.-) (DNase I homolog protein DHP2) (Deoxyribonuclease I-like 3) (DNase I-like 3) (Liver and spleen DNase) (LS-DNase) (LSD) 310 35,760 Active site (2); Chain (1); Disulfide bond (1); Motif (2); Natural variant (1); Region (1); Signal peptide (1) FUNCTION: Has DNA hydrolytic activity. Is capable of both single- and double-stranded DNA cleavage, producing DNA fragments with 3'-OH ends (By similarity). Can cleave chromatin to nucleosomal units and cleaves nucleosomal and liposome-coated DNA (PubMed:15796714, PubMed:19154352, PubMed:12095301). Acts in internucleosomal DNA fragmentation (INDF) during apoptosis and necrosis. The role in apoptosis includes myogenic and neuronal differentiation, and BCR-mediated clonal deletion of self-reactive B cells (PubMed:12050166, PubMed:15167901, PubMed:17218958, PubMed:24312463). Is active on chromatin in apoptotic cell-derived membrane-coated microparticles and thus suppresses anti-DNA autoimmunity (PubMed:15796714, PubMed:27293190). Together with DNASE1, plays a key role in degrading neutrophil extracellular traps (NETs) (PubMed:29191910). NETs are mainly composed of DNA fibers and are released by neutrophils to bind pathogens during inflammation (PubMed:29191910). Degradation of intravascular NETs by DNASE1 and DNASE1L3 is required to prevent formation of clots that obstruct blood vessels and cause organ damage following inflammation (PubMed:29191910). {ECO:0000250|UniProtKB:O89107, ECO:0000269|PubMed:12050166, ECO:0000269|PubMed:15167901, ECO:0000269|PubMed:17218958, ECO:0000269|PubMed:24312463, ECO:0000269|PubMed:27293190, ECO:0000269|PubMed:29191910, ECO:0000305|PubMed:15796714}. PTM: Poly-ADP-ribosylated by PARP1. ADP-ribosylation negatively regulates enzymatic activity during apoptosis. {ECO:0000250|UniProtKB:Q13609}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13609, ECO:0000269|PubMed:12050166}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q13609}. Secreted {ECO:0000269|PubMed:12095301, ECO:0000269|PubMed:15796714, ECO:0000269|PubMed:27293190}. Note=Contradictory reports exist about the subcellular localization under normal physiological conditions. Shown to translocate to rough endoplasmic reticulum and to be transported through the entire secretory pathway for secretion. However, under conditions of cell death, may diffuse and/or be actively transported to the nucleus. {ECO:0000305|PubMed:15796714, ECO:0000305|PubMed:27293190}. TISSUE SPECIFICITY: Expressed at high levels in liver, spleen and testes. Expressed at lower levels in heart, lungs, skeletal muscle and kidney. Not expressed in brain. Predominantly expressed in macrophages; at protein level. Secreted by mononuclear phagocytes. {ECO:0000269|PubMed:10807908, ECO:0000269|PubMed:12050166, ECO:0000269|PubMed:12095301, ECO:0000269|PubMed:27293190}. +Q8BZN6 DOC10_MOUSE Dedicator of cytokinesis protein 10 (Zizimin-3) 2150 245,758 Alternative sequence (5); Chain (1); Domain (3); Erroneous initiation (1); Modified residue (13); Sequence conflict (1) FUNCTION: Guanine nucleotide-exchange factor (GEF) that activates CDC42 and RAC1 by exchanging bound GDP for free GTP. Essential for dendritic spine morphogenesis in Purkinje cells and in hippocampal neurons, via a CDC42-mediated pathway (PubMed:25851601). Sustains B-cell lymphopoiesis in secondary lymphoid tissues and regulates FCER2/CD23 expression (PubMed:27502165). {ECO:0000269|PubMed:25851601, ECO:0000269|PubMed:27502165}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96BY6}. Cytoplasm {ECO:0000250|UniProtKB:Q96BY6}. Cell projection, dendritic spine {ECO:0000269|PubMed:25851601}. DOMAIN: The DHR-2 domain may mediate some GEF activity. {ECO:0000269|PubMed:25851601}. TISSUE SPECIFICITY: Expressed in brain, lung, spleen, mesenteric lymph nodes (MLN) and thymus (PubMed:15710388, PubMed:25729399). Expressed by B and T splenocytes (PubMed:21514340). In brain, expressed by Purkinje cells during postnatal development and hippocampal neurons (PubMed:25851601). {ECO:0000269|PubMed:15710388, ECO:0000269|PubMed:21514340, ECO:0000269|PubMed:25729399, ECO:0000269|PubMed:25851601}. +A2AF47 DOC11_MOUSE Dedicator of cytokinesis protein 11 (Activated Cdc42-associated guanine nucleotide exchange factor) (ACG) (Zizimin-2) 2073 237,771 Chain (1); Domain (3); Modified residue (9); Region (1); Sequence conflict (1) FUNCTION: Guanine nucleotide-exchange factor (GEF) that activates CDC42 by exchanging bound GDP for free GTP (PubMed:15710388, PubMed:16968698, PubMed:25851601). Required for marginal zone (MZ) B-cell development, is associated with early bone marrow B-cell development, MZ B-cell formation, MZ B-cell number and marginal metallophilic macrophages morphology (PubMed:25729399). Facilitates filopodia formation through the activation of CDC42 (PubMed:22494997). {ECO:0000269|PubMed:15710388, ECO:0000269|PubMed:16968698, ECO:0000269|PubMed:22494997, ECO:0000269|PubMed:25729399, ECO:0000269|PubMed:25851601}. SUBUNIT: Interacts with CDC42. {ECO:0000269|PubMed:15710388, ECO:0000269|PubMed:16968698}. DOMAIN: The DHR-2 domain is necessary for the GEF activity. {ECO:0000269|PubMed:25851601}. TISSUE SPECIFICITY: Expressed in spleen, thymus, mesenteric lymph nodes (MLN), bone marrow and peripheral blood lymphocytes. Enriched in B-cells from germinal centers. Expressed in B-, T- and dendritic cells as well as Purkinje cells (PubMed:22494997, PubMed:25851601). {ECO:0000269|PubMed:15710388, ECO:0000269|PubMed:22494997, ECO:0000269|PubMed:25729399, ECO:0000269|PubMed:25851601}. +Q7TNF0 DOC2A_MOUSE Double C2-like domain-containing protein alpha (Doc2-alpha) 405 44,609 Chain (1); Domain (2); Region (2) FUNCTION: Calcium sensor which most probably regulates fusion of vesicles with membranes. Binds calcium and phospholipids. May be involved in calcium dependent neurotransmitter release through the interaction with UNC13A. May be involved in calcium-dependent spontaneous release of neurotransmitter in absence of action potentials in neuronal cells. Regulates Ca(2+)-dependent secretory lysosome exocytosis in mast cells. {ECO:0000269|PubMed:18354201, ECO:0000269|PubMed:20150444}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell junction, synapse, synaptosome {ECO:0000250}. Lysosome {ECO:0000250}. SUBUNIT: Interacts (via N-terminus) with UNC13A. Interacts with cytoplasmic dynein light chain DYNLT1 (By similarity). Interacts with UNC13D (By similarity). {ECO:0000250}. DOMAIN: C2 domain 1 is involved in binding calcium and phospholipids. {ECO:0000250}. TISSUE SPECIFICITY: Brain and mast cells. {ECO:0000269|PubMed:18354201}. +P70169 DOC2B_MOUSE Double C2-like domain-containing protein beta (Doc2-beta) 412 45,853 Chain (1); Domain (2); Modified residue (1); Mutagenesis (4); Region (3); Sequence conflict (1) FUNCTION: Calcium sensor which positively regulates SNARE-dependent fusion of vesicles with membranes. Binds phospholipids in a calcium-dependent manner and may act at the priming stage of fusion by modifying membrane curvature to stimulate fusion. Involved in calcium-triggered exocytosis in chromaffin cells and calcium-dependent spontaneous release of neurotransmitter in absence of action potentials in neuronal cells. Involved both in glucose-stimulated insulin secretion in pancreatic cells and insulin-dependent GLUT4 transport to the plasma membrane in adipocytes. {ECO:0000269|PubMed:19033398, ECO:0000269|PubMed:19410553, ECO:0000269|PubMed:20150444, ECO:0000269|PubMed:8902635}. SUBCELLULAR LOCATION: Cytoplasm. Cytoplasmic granule. Cell membrane; Peripheral membrane protein. Note=Translocates to the plasma membrane in a calcium-dependent manner. SUBUNIT: Interacts with cytoplasmic dynein light chain DYNLT1. May interact with UNC13A; the interaction mediates targeting to the plasma membrane (By similarity). Probably interacts with the SNARE (soluble N-ethylmaleimide-sensitive factor attached protein receptor) complex composed of SNAP25, STX1A and VAMP2; the interaction is calcium-dependent and competitive with SYT1. Interacts with STX4; the interaction is calcium-dependent, increased by insulin and glucose, and mediates vesicle fusion with plasma membrane in pancreatic cells and adipocytes. Interacts with STXBP3; the interaction is direct, occurs at the cell membrane and regulates glucose-stimulated insulin secretion. {ECO:0000250, ECO:0000269|PubMed:17548353, ECO:0000269|PubMed:18596155, ECO:0000269|PubMed:19033398, ECO:0000269|PubMed:19410553}. DOMAIN: C2 domain 1 is involved in binding calcium and phospholipids. According to PubMed:19033398, the C2 domain 2 may also play a role in the calcium-dependent targeting to membranes. TISSUE SPECIFICITY: Widely expressed. Expressed in pancreatic islet cells (at protein level). {ECO:0000269|PubMed:17548353, ECO:0000269|PubMed:8902635}. +Q9ESN1 DOC2G_MOUSE Double C2-like domain-containing protein gamma (Doc2-gamma) 387 43,347 Chain (1); Domain (2); Sequence conflict (2) FUNCTION: May be involved in regulation of vesicular trafficking. In vitro, does not bind calcium and phospholipids. +Q8BUR4 DOCK1_MOUSE Dedicator of cytokinesis protein 1 (180 kDa protein downstream of CRK) (DOCK180) 1865 215,085 Alternative sequence (2); Beta strand (7); Chain (1); Domain (3); Helix (1); Modified residue (8); Motif (2); Region (4); Sequence conflict (1) FUNCTION: Involved in cytoskeletal rearrangements required for phagocytosis of apoptotic cells and cell motility. Along with DOCK1, mediates CRK/CRKL regulation of epithelial and endothelial cell spreading and migration on type IV collagen. Functions as a guanine nucleotide exchange factor (GEF), which activates Rac Rho small GTPases by exchanging bound GDP for free GTP. Its GEF activity may be enhanced by ELMO1. {ECO:0000250|UniProtKB:Q14185}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}. Note=Recruited to membranes via its interaction with phosphatidylinositol 3,4,5-trisphosphate. {ECO:0000250}. SUBUNIT: Interacts with the SH3 domains of CRK and NCK2 via multiple sites. Interacts with nucleotide-free RAC1 via its DHR-2 domain. Interacts with ELMO1, ELMO2 and probably ELMO3 via its SH3 domain. Interacts with RAC1 (By similarity). Interacts with ELMO1 and ADGRB1 (PubMed:17960134). Identified in a complex with AUTS2 and ELMO2 (PubMed:25533347). {ECO:0000250|UniProtKB:Q14185, ECO:0000269|PubMed:17960134, ECO:0000269|PubMed:25533347}. DOMAIN: The DHR-2 domain is necessary and sufficient for the GEF activity. +Q8C3J5 DOCK2_MOUSE Dedicator of cytokinesis protein 2 (Protein Hch) 1828 211,704 Chain (1); Domain (3); Modified residue (8); Sequence conflict (2) FUNCTION: Involved in cytoskeletal rearrangements required for lymphocyte migration in response of chemokines. Activates RAC1 and RAC2, but not CDC42, by functioning as a guanine nucleotide exchange factor (GEF), which exchanges bound GDP for free GTP. May also participate in IL2 transcriptional activation via the activation of RAC2. {ECO:0000269|PubMed:11518968}. SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Colocalizes with F-actin. {ECO:0000250}. SUBUNIT: Homodimer (Probable). Interacts with RAC1 and RAC2. Interacts with CRKL and VAV. Interacts with CD3Z (By similarity). {ECO:0000250, ECO:0000305}. DOMAIN: The DHR-2 domain probably mediates the GEF activity. {ECO:0000250}. TISSUE SPECIFICITY: Specifically expressed in hematopoietic cells. {ECO:0000269|PubMed:11518968}. +Q8CIQ7 DOCK3_MOUSE Dedicator of cytokinesis protein 3 (Modifier of cell adhesion) (Presenilin-binding protein) (PBP) 2027 232,910 Chain (1); Compositional bias (1); Domain (3); Modified residue (1); Motif (1) FUNCTION: Potential guanine nucleotide exchange factor (GEF). GEF proteins activate some small GTPases by exchanging bound GDP for free GTP. Its interaction with presenilin proteins as well as its ability to stimulate Tau/MAPT phosphorylation suggest that it may be involved in Alzheimer disease. Ectopic expression in nerve cells decreases the secretion of amyloid-beta APBA1 protein and lowers the rate of cell-substratum adhesion, suggesting that it may affect the function of some small GTPase involved in the regulation of actin cytoskeleton or cell adhesion receptors. {ECO:0000269|PubMed:12093789}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10854253}. SUBUNIT: Interacts with presenilin proteins PSEN1 and PSEN2. Interacts with CRK. {ECO:0000269|PubMed:10854253, ECO:0000269|PubMed:12093789}. DOMAIN: The DHR-2 domain may mediate some GEF activity. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain. Not expressed in heart, liver, kidney, spleen and lung. In brain, it is highly expressed in the cerebral cortex and hippocampus, while it is absent in other tissues, except in spinal cord. In the cerebral cortex, it is found within the intermediate (III and IV) and deep (V and VI) layers, whereas it is weakly expressed in superficial layer I. It is also abundant in the piriform cortex. Within the hippocampus, it is expressed in the pyramidal neurons of the CA1, CA2, and CA3 regions and the dentate gyrus. {ECO:0000269|PubMed:10854253}. +P59764 DOCK4_MOUSE Dedicator of cytokinesis protein 4 1978 226,550 Chain (1); Compositional bias (2); Domain (3); Modified residue (9); Motif (1) FUNCTION: Involved in regulation of adherens junction between cells. Plays a role in cell migration. Functions as a guanine nucleotide exchange factor (GEF), which activates Rap1 small GTPase by exchanging bound GDP for free GTP (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8N1I0}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8N1I0}. Note=Colocalizes with EPHA2, RhoG and CTTN/cortactin at the tip of protrusions in migrating cells. {ECO:0000250|UniProtKB:Q8N1I0}. SUBUNIT: Interacts with the SH3 domain of CRK. Interacts with nucleotide-free Rap1. Interacts with FASLG. Interacts with ELMO2 and EPHA2; mediates activation of RAC1 by EPHA2 (By similarity). {ECO:0000250}. DOMAIN: The DHR-2 domain probably mediates the GEF activity. {ECO:0000250}. DISEASE: Note=Defects in Dock4 are involved in the cause of some cancers, which are probably due to lack of Rap1 activation. {ECO:0000269|PubMed:12628187}. +B2RY04 DOCK5_MOUSE Dedicator of cytokinesis protein 5 (Lens rupture protein 2) (Rupture of lens cataract protein) 1868 214,429 Chain (1); Compositional bias (1); Domain (3); Modified residue (10); Sequence conflict (3) FUNCTION: Guanine nucleotide exchange factor (GEF) for Rho and Rac. GEF proteins activate small GTPases by exchanging bound GDP for free GTP (PubMed:18396277). Along with DOCK1, mediates CRK/CRKL regulation of epithelial and endothelial cell spreading and migration on type IV collagen (By similarity). {ECO:0000250|UniProtKB:Q9H7D0, ECO:0000269|PubMed:18396277}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18396277}. Cell membrane {ECO:0000250|UniProtKB:Q9H7D0}. Note=Associated with the edge of the plasma membrane in intestinal epithelial cells spreading on type IV collagen. {ECO:0000250|UniProtKB:Q9H7D0}. SUBUNIT: Interacts with CRK and CRKL. {ECO:0000250|UniProtKB:Q9H7D0}. DOMAIN: The DHR-2 domain may mediate some GEF activity. {ECO:0000250|UniProtKB:Q14185}. TISSUE SPECIFICITY: Highly expressed in lens, where it predominantly localizes to anterior epithelial cells, and is weakly expressed in lens fiber (at protein level). Expressed in brain, eye, lung, spleen and kidney, but not in thymus or peripheral blood leukocytes. {ECO:0000269|PubMed:18396277}. DISEASE: Note=Defects in Dock5 are the cause of rupture of lens cataract. It affects both eyes and is inherited as an autosomal recessive trait. Homozygotes spontaneously develop opacity of the lens at 35-60 days of age. The initial pathological changes appear at about 35 days of age in the deep layer of the posterior cortex as irregular swelling, condensation, degeneration and fragmentation of the lens fibers, leading to rupture of the lens capsule at the posterior pole at 45-100 days of age. Following rupture, the lens nucleus becomes dislocated behind the lens or occasionally in the anterior chamber. {ECO:0000269|PubMed:9093026, ECO:0000269|PubMed:9230506}. +Q8VDR9 DOCK6_MOUSE Dedicator of cytokinesis protein 6 2080 233,267 Alternative sequence (5); Chain (1); Domain (2); Erroneous initiation (1); Frameshift (1); Modified residue (9); Sequence caution (1); Sequence conflict (1) FUNCTION: Acts as guanine nucleotide exchange factor (GEF) for CDC42 and RAC1 small GTPases (By similarity). Through its activation of CDC42 and RAC1, regulates neurite outgrowth in an vitro differentiation system. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Mainly located near the cell surface. {ECO:0000250}. DOMAIN: The DHR-2 domain may mediate some GEF activity. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed with highest levels in lung and heart. {ECO:0000269|PubMed:21820096}. +Q8R1A4 DOCK7_MOUSE Dedicator of cytokinesis protein 7 (Protein moonlight) 2130 241,438 Alternative sequence (1); Chain (1); Coiled coil (2); Domain (2); Erroneous initiation (3); Modified residue (25) FUNCTION: Functions as a guanine nucleotide exchange factor (GEF), which activates Rac1 and Rac3 Rho small GTPases by exchanging bound GDP for free GTP. Does not have a GEF activity for CDC42. Required for STMN1 'Ser-15' phosphorylation during axon formation and consequently for neuronal polarization (By similarity). Has a role in pigmentation (PubMed:19202056). Involved in the regulation of cortical neurogenesis through the control of radial glial cells (RGCs) proliferation versus differentiation; negatively regulates the basal-to-apical interkinetic nuclear migration of RGCs by antagonizing the microtubule growth-promoting function of TACC3 (PubMed:22842144). {ECO:0000250|UniProtKB:Q96N67, ECO:0000269|PubMed:19202056, ECO:0000269|PubMed:22842144}. SUBCELLULAR LOCATION: Cell projection, axon {ECO:0000250|UniProtKB:Q96N67}. Note=Enriched in the developing axons of hippocampal neurons. {ECO:0000250|UniProtKB:Q96N67}. SUBUNIT: Interacts with TSC1 (By similarity). Interacts with nucleotide-free RAC1 and RAC3 (By similarity). Interacts with TACC3. Interacts with CRY1. Interacts with NOD2 (By similarity). {ECO:0000250|UniProtKB:Q96N67, ECO:0000269|PubMed:19129230, ECO:0000269|PubMed:22842144}. DOMAIN: The DHR-2 domain mediates GEF activity. {ECO:0000250|UniProtKB:Q96N67}. DISEASE: Note=Defects in Dock7 are responsible for the moonlight phenotype (mnlt). mnlt/mnlt mice display an overall lightened coat color and hypopigmentation of the belly and distal extremities, particularly the paws, tail tip, and genitalia. {ECO:0000269|PubMed:19202056}. +Q8C147 DOCK8_MOUSE Dedicator of cytokinesis protein 8 2100 238,978 Alternative sequence (3); Beta strand (9); Chain (1); Domain (2); Erroneous initiation (4); Helix (12); Modified residue (8); Mutagenesis (1); Sequence conflict (2) FUNCTION: Guanine nucleotide exchange factor (GEF) which specifically activates small GTPase CDC42 by exchanging bound GDP for free GTP (PubMed:28028151, PubMed:22461490). During immune responses, required for interstitial dendritic cell (DC) migration by locally activating CDC42 at the leading edge membrane of DC (PubMed:22461490, PubMed:25713392). Required for CD4(+) T-cell migration in response to chemokine stimulation by promoting CDC42 activation at T cell leading edge membrane (PubMed:28028151). Is involved in NK cell cytotoxicity controlling polarization of microtubule-organizing center (MTOC), and possibly regulating CCDC88B-mediated lytic granule transport to MTOC during cell killing (By similarity). {ECO:0000250|UniProtKB:Q8NF50, ECO:0000269|PubMed:22461490, ECO:0000269|PubMed:25713392, ECO:0000269|PubMed:28028151}. PTM: In response to chemokine CXCL12/SDF-1-alpha stimulation, phosphorylated by PRKCA/PKC-alpha which promotes DOCK8 dissociation from LRCH1. {ECO:0000250|UniProtKB:Q8NF50}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8NF50}. Cell membrane {ECO:0000269|PubMed:22461490}; Peripheral membrane protein {ECO:0000305|PubMed:22461490}; Cytoplasmic side {ECO:0000305}. Cell projection, lamellipodium membrane {ECO:0000305|PubMed:22461490}; Peripheral membrane protein {ECO:0000305|PubMed:22461490}; Cytoplasmic side {ECO:0000305}. Note=Enriched and co-localizes with GTPase CDC42 at the immunological synapse formed during T cell/antigen presenting cell cognate interaction. Translocates from the cytoplasm to the plasma membrane in response to chemokine CXCL12/SDF-1-alpha stimulation. {ECO:0000250|UniProtKB:Q8NF50}. SUBUNIT: Interacts (via DHR-2 domain) with GTPase CDC42; the interaction activates CDC42 by exchanging GDP for GTP (PubMed:22461490). The unphosphorylated form interacts (via DHR-2 domain) with LRCH1 (via LRR repeats); the interaction prevents the association between DOCK8 and CDC42 (PubMed:28028151). Interacts with CCDC88B (By similarity). {ECO:0000250|UniProtKB:Q8NF50, ECO:0000269|PubMed:22461490, ECO:0000269|PubMed:28028151}. DOMAIN: The DHR-2 domain is necessary and sufficient for the GEF activity. {ECO:0000269|PubMed:22461490}. TISSUE SPECIFICITY: Expressed in T cells (PubMed:28028151). Expressed in bone marrow-derived dendritic cells (PubMed:25713392). {ECO:0000269|PubMed:25713392, ECO:0000269|PubMed:28028151}. +Q8BIK4 DOCK9_MOUSE Dedicator of cytokinesis protein 9 (Cdc42 guanine nucleotide exchange factor zizimin-1) (Zizimin-1) 2055 235,312 Alternative sequence (5); Chain (1); Domain (3); Erroneous initiation (2); Modified residue (10); Sequence conflict (3) FUNCTION: Guanine nucleotide-exchange factor (GEF) that activates CDC42 by exchanging bound GDP for free GTP (PubMed:25851601). Overexpression induces filopodia formation (By similarity). {ECO:0000250|UniProtKB:Q9BZ29, ECO:0000269|PubMed:25851601}. SUBCELLULAR LOCATION: Endomembrane system {ECO:0000305}. Note=Associated with membranes. {ECO:0000305}. SUBUNIT: Homodimer. Interacts preferentially with nucleotide-depleted CDC42 (By similarity). {ECO:0000250|UniProtKB:Q9BZ29}. DOMAIN: The DHR-2 domain is necessary and sufficient for the GEF activity. {ECO:0000269|PubMed:25851601}. TISSUE SPECIFICITY: Expressed in lung (PubMed:25729399, PubMed:22494997). Also detected in Peyers patches, thymus, brain and lymph nodes (PubMed:22494997). Expressed in Purkinje cells (PubMed:25851601). {ECO:0000269|PubMed:22494997, ECO:0000269|PubMed:25729399, ECO:0000269|PubMed:25851601}. +Q99LN9 DOHH_MOUSE Deoxyhypusine hydroxylase (DOHH) (EC 1.14.99.29) (Deoxyhypusine dioxygenase) (Deoxyhypusine monooxygenase) 302 32,905 Alternative sequence (2); Chain (1); Frameshift (1); Metal binding (6); Modified residue (1); Repeat (5); Sequence conflict (3) Protein modification; eIF5A hypusination. FUNCTION: Catalyzes the hydroxylation of the N(6)-(4-aminobutyl)-L-lysine intermediate produced by deoxyhypusine synthase/DHPS on a critical lysine of the eukaryotic translation initiation factor 5A/eIF-5A. This is the second step of the post-translational modification of that lysine into an unusual amino acid residue named hypusine. Hypusination is unique to mature eIF-5A factor and is essential for its function. {ECO:0000255|HAMAP-Rule:MF_03101, ECO:0000269|PubMed:24832488}. +P97465 DOK1_MOUSE Docking protein 1 (Downstream of tyrosine kinase 1) (p62(dok)) 482 52,452 Beta strand (7); Chain (1); Compositional bias (2); Domain (2); Helix (3); Modified residue (13); Sequence conflict (3); Turn (1) FUNCTION: DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK1 appears to be a negative regulator of the insulin signaling pathway. Modulates integrin activation by competing with talin for the same binding site on ITGB3 (By similarity). {ECO:0000250}. PTM: Constitutively tyrosine-phosphorylated. Phosphorylated by TEC. Phosphorylated on tyrosine residues by the insulin receptor kinase. Results in the negative regulation of the insulin signaling pathway (By similarity). Phosphorylated by LYN. Phosphorylated on tyrosine residues by SRMS (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Interacts with RasGAP, INPP5D/SHIP1 and ABL1. Interacts directly with phosphorylated ITGB3 (By similarity). Interacts with SRMS (via the SH2 and SH3 domains) (By similarity). {ECO:0000250}. DOMAIN: PTB domain mediates receptor interaction. TISSUE SPECIFICITY: Expressed in lung, spleen, skeletal muscle and kidney. +O70469 DOK2_MOUSE Docking protein 2 (Dok-related protein) (Dok-R) (Downstream of tyrosine kinase 2) (IL-four receptor-interacting protein) (FRIP) (p56(dok-2)) 412 45,522 Chain (1); Compositional bias (2); Domain (2); Modified residue (3); Mutagenesis (3); Sequence conflict (4) FUNCTION: DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK2 may modulate the cellular proliferation induced by IL-4, as well as IL-2 and IL-3. May be involved in modulating Bcr-Abl signaling. Attenuates EGF-stimulated MAP kinase activation. PTM: On immunoreceptor stimulation, phosphorylated on C-terminal tyrosine residues. Phosphorylation on Tyr-351 is required for binding to the SH2 domain of NCK. Phosphorylation on both Tyr-276 and Tyr-304 is required for interaction with RASGAP. Phosphorylated on tyrosine residues by TEK/TIE2. {ECO:0000269|PubMed:10508618, ECO:0000269|PubMed:11470823, ECO:0000269|PubMed:12665569, ECO:0000269|PubMed:9697832}. SUBUNIT: Interacts with phosphorylated RASGAP and EGFR. Interacts with RET and NCK. Interacts (via PH domain) with TEK/TIE2 (tyrosine phosphorylated). {ECO:0000269|PubMed:10508618, ECO:0000269|PubMed:11470823, ECO:0000269|PubMed:12665569}. DOMAIN: PTB domain mediates receptor interaction. TISSUE SPECIFICITY: Highly expressed in spleen and lung. {ECO:0000269|PubMed:11470823, ECO:0000269|PubMed:9478921}. +Q9QZK7 DOK3_MOUSE Docking protein 3 (Downstream of tyrosine kinase 3) (p62(dok)-like protein) (DOK-L) 444 48,027 Chain (1); Compositional bias (2); Domain (2); Modified residue (6); Mutagenesis (6) FUNCTION: DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK3 is a negative regulator of JNK signaling in B-cells through interaction with INPP5D/SHIP1. May modulate ABL1 function. {ECO:0000269|PubMed:14993273}. PTM: Constitutively tyrosine-phosphorylated.; PTM: On IL2 stimulation, phosphorylated on C-terminal tyrosine residues possibly by Src kinases. Can also be phosphorylated by ABL1 kinase. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. SUBUNIT: On tyrosine phosphorylation, interacts with CSK and INPP5D/SHIP1 via their SH2 domains. Both Tyr-325 and Tyr-343 are required for interaction with INPP5D. Only Tyr-325 is required for interaction with CSK. Binds ABL1 through the PTB domain and in a kinase-dependent manner. Does not interact with RasGAP. {ECO:0000269|PubMed:10567556, ECO:0000269|PubMed:10733577, ECO:0000269|PubMed:14993273}. DOMAIN: PTB domain mediates receptor interaction. {ECO:0000250}. TISSUE SPECIFICITY: Predominantly expressed in bone marrow, spleen and lung. Low levels in heart, brain, liver, muscle, thymus, kidney and testis. Highly expressed in B-cells and macrophages. {ECO:0000269|PubMed:10567556, ECO:0000269|PubMed:10733577}. +Q99KE3 DOK4_MOUSE Docking protein 4 (Downstream of tyrosine kinase 4) 325 37,040 Chain (1); Domain (2); Motif (1) FUNCTION: DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK4 functions in RET-mediated neurite outgrowth and plays a positive role in activation of the MAP kinase pathway (By similarity). Putative link with downstream effectors of RET in neuronal differentiation. May be involved in the regulation of the immune response induced by T-cells (By similarity). {ECO:0000250}. PTM: Phosphorylated on tyrosine residues in response to insulin, IGF1 or RET stimulation. {ECO:0000250}. SUBUNIT: Interacts with RET and TEK/TIE2. Interaction with RET is mediated through the PTB domain and requires phosphorylation of RET 'Tyr-1062'. {ECO:0000269|PubMed:11470823}. DOMAIN: PTB domain mediates receptor interaction. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. Highest levels in heart, lung and kidney. {ECO:0000269|PubMed:11470823}. +Q91ZM9 DOK5_MOUSE Docking protein 5 (Downstream of tyrosine kinase 5) 306 35,453 Chain (1); Domain (2); Motif (1); Sequence conflict (1) FUNCTION: DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK5 functions in RET-mediated neurite outgrowth and plays a positive role in activation of the MAP kinase pathway. Putative link with downstream effectors of RET in neuronal differentiation. {ECO:0000269|PubMed:11470823}. PTM: Phosphorylated on tyrosine residues in response to insulin, IGF1 and GDNF. {ECO:0000250}. SUBUNIT: Interacts with phosphorylated RET. In contrast to other DOK proteins, it does not interact with RASGAP. {ECO:0000269|PubMed:11470823}. DOMAIN: PTB domain mediates receptor interaction. TISSUE SPECIFICITY: Specifically expressed in the brain, with a high specificity for neurons. {ECO:0000269|PubMed:11470823}. +Q2MHE5 DOK6_MOUSE Docking protein 6 (Downstream of tyrosine kinase 6) 331 38,287 Chain (1); Domain (2); Motif (1) FUNCTION: DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK6 promotes Ret-mediated neurite growth. May have a role in brain development and/or maintenance (By similarity). {ECO:0000250}. PTM: On Ret activation, phosphorylated on one or more C-terminal tyrosine residues by an Src family kinase. {ECO:0000250}. SUBUNIT: Interacts via its PTB domain with phosphorylated RET. {ECO:0000250}. DOMAIN: PTB domain mediates receptor interaction. {ECO:0000250}. +Q18PE0 DOK7_MOUSE Protein Dok-7 (Downstream of tyrosine kinase 7) 504 53,177 Alternative sequence (2); Beta strand (16); Chain (1); Compositional bias (1); Domain (2); Erroneous initiation (2); Helix (5); Mutagenesis (2); Turn (3) FUNCTION: Probable muscle-intrinsic activator of MUSK that plays an essential role in neuromuscular synaptogenesis. Acts in aneural activation of MUSK and subsequent acetylcholine receptor (AchR) clustering in myotubes. Induces autophosphorylation of MUSK. {ECO:0000269|PubMed:16794080, ECO:0000269|PubMed:20603078}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16794080}; Peripheral membrane protein {ECO:0000269|PubMed:16794080}. Cell junction, synapse {ECO:0000269|PubMed:16794080}. Note=Accumulates at neuromuscular junctions. SUBUNIT: Homodimer. Forms a heterotetramer composed of 2 DOK7 and 2 MUSK molecules which facilitates MUSK trans-autophosphorylation on tyrosine residue and activation. Interacts (via IRS-type PTB domain) with MUSK (via cytoplasmic part); requires MUSK phosphorylation. {ECO:0000269|PubMed:16794080, ECO:0000269|PubMed:20603078}. DOMAIN: The PH domain mediated binding to phospholipids with phosphoinositol headgroups. Affinity is highest for phosphatidyl 3,4,5-trisphosphate, followed by phosphatidylinositol 3,4-bisphosphate and phosphatidylinositol 4,5-bisphosphate. {ECO:0000269|PubMed:20603078}. +Q8R2Y3 DOLK_MOUSE Dolichol kinase (EC 2.7.1.108) (Transmembrane protein 15) 534 59,145 Chain (1); Region (1); Topological domain (16); Transmembrane (15) TRANSMEM 17 37 Helical. {ECO:0000255}.; TRANSMEM 73 93 Helical. {ECO:0000255}.; TRANSMEM 110 130 Helical. {ECO:0000255}.; TRANSMEM 133 153 Helical. {ECO:0000255}.; TRANSMEM 162 182 Helical. {ECO:0000255}.; TRANSMEM 187 207 Helical. {ECO:0000255}.; TRANSMEM 221 241 Helical. {ECO:0000255}.; TRANSMEM 253 273 Helical. {ECO:0000255}.; TRANSMEM 294 314 Helical. {ECO:0000255}.; TRANSMEM 334 350 Helical. {ECO:0000255}.; TRANSMEM 356 376 Helical. {ECO:0000255}.; TRANSMEM 398 418 Helical. {ECO:0000255}.; TRANSMEM 433 453 Helical. {ECO:0000255}.; TRANSMEM 469 489 Helical. {ECO:0000255}.; TRANSMEM 492 512 Helical. {ECO:0000255}. TOPO_DOM 1 16 Lumenal. {ECO:0000255}.; TOPO_DOM 38 72 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 94 109 Lumenal. {ECO:0000255}.; TOPO_DOM 131 132 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 154 161 Lumenal. {ECO:0000255}.; TOPO_DOM 183 186 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 208 220 Lumenal. {ECO:0000255}.; TOPO_DOM 242 252 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 274 293 Lumenal. {ECO:0000255}.; TOPO_DOM 315 333 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 351 355 Lumenal. {ECO:0000255}.; TOPO_DOM 377 397 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 419 432 Lumenal. {ECO:0000255}.; TOPO_DOM 454 468 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 490 491 Lumenal. {ECO:0000255}.; TOPO_DOM 513 534 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in the synthesis of the sugar donor Dol-P-Man which is required in the synthesis of N-linked and O-linked oligosaccharides and for that of GPI anchors. {ECO:0000250|UniProtKB:P20048}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9UPQ8}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9UPQ8}. +Q9QXP4 DONS_MOUSE Protein downstream neighbor of Son (Protein 3SG) 560 61,987 Chain (1); Sequence conflict (6) FUNCTION: Replisome component that maintains genome stability by protecting stalled or damaged replication forks. After the induction of replication stress, required for the stabilization of stalled replication forks, the efficient activation of the intra-S-phase and G/2M cell-cycle checkpoints and the maintenance of genome stability. {ECO:0000250|UniProtKB:Q9NYP3}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NYP3}. Note=Localizes at DNA replication sites. {ECO:0000250|UniProtKB:Q9NYP3}. SUBUNIT: Component of the replisome complex composed of at least MCM2, MCM7, PCNA and TICRR; interaction at least with PCNA occurs during DNA replication. {ECO:0000250|UniProtKB:Q9NYP3}. +Q8BL99 DOP1_MOUSE Protein dopey-1 2399 269,257 Alternative sequence (12); Chain (1); Modified residue (1) FUNCTION: May be involved in protein traffic between late Golgi and early endosomes. {ECO:0000250|UniProtKB:Q03921}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q03921}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q03921}. +Q3UHQ6 DOP2_MOUSE Protein dopey-2 2295 257,483 Alternative sequence (1); Chain (1); Modified residue (3); Sequence conflict (5) FUNCTION: May be involved in protein traffic between late Golgi and early endosomes. {ECO:0000250|UniProtKB:Q03921}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q03921}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q03921}. TISSUE SPECIFICITY: Expressed in liver, heart and brain. {ECO:0000269|PubMed:12767918}. +O35215 DOPD_MOUSE D-dopachrome decarboxylase (EC 4.1.1.84) (D-dopachrome tautomerase) 118 13,077 Beta strand (6); Chain (1); Helix (7); Initiator methionine (1); Modified residue (3) FUNCTION: Tautomerization of D-dopachrome with decarboxylation to give 5,6-dihydroxyindole (DHI). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Homotrimer. {ECO:0000250}. +Q64237 DOPO_MOUSE Dopamine beta-hydroxylase (EC 1.14.17.1) (Dopamine beta-monooxygenase) [Cleaved into: Soluble dopamine beta-hydroxylase] 622 70,314 Active site (2); Chain (2); Disulfide bond (8); Domain (1); Glycosylation (4); Metal binding (6); Modified residue (1); Sequence conflict (8); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 21 41 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 20 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 42 621 Intragranular. {ECO:0000255}. Catecholamine biosynthesis; (R)-noradrenaline biosynthesis; (R)-noradrenaline from dopamine: step 1/1. FUNCTION: Conversion of dopamine to noradrenaline. {ECO:0000269|PubMed:27148966, ECO:0000269|PubMed:7715704}. PTM: Proteolytic cleavage after the membrane-anchor leads to the release of the soluble form. {ECO:0000250|UniProtKB:P15101}.; PTM: N-glycosylated. {ECO:0000250|UniProtKB:P09172}. SUBCELLULAR LOCATION: Soluble dopamine beta-hydroxylase: Cytoplasmic vesicle, secretory vesicle lumen {ECO:0000269|PubMed:7961964}. Cytoplasmic vesicle, secretory vesicle, chromaffin granule lumen {ECO:0000269|PubMed:7961964}.; SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000269|PubMed:7961964}; Single-pass type II membrane protein {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle, chromaffin granule membrane {ECO:0000269|PubMed:7961964}; Single-pass type II membrane protein {ECO:0000305}. SUBUNIT: Homotetramer; composed of two disulfide-linked dimers. {ECO:0000250|UniProtKB:P09172}. TISSUE SPECIFICITY: Detected in adrenal gland secretory granules (at protein level) (PubMed:7961964). Detected in adrenal gland (PubMed:1280432). {ECO:0000269|PubMed:1280432, ECO:0000269|PubMed:7961964}. +Q9JMF7 DOPP1_MOUSE Dolichyldiphosphatase 1 (EC 3.6.1.43) (Dolichyl pyrophosphate phosphatase 1) (Protein 2-23) 238 27,099 Chain (1); Sequence conflict (2); Transmembrane (4) TRANSMEM 33 53 Helical. {ECO:0000255}.; TRANSMEM 100 120 Helical. {ECO:0000255}.; TRANSMEM 130 150 Helical. {ECO:0000255}.; TRANSMEM 162 182 Helical. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Required for efficient N-glycosylation. Necessary for maintaining optimal levels of dolichol-linked oligosaccharides. Hydrolyzes dolichyl pyrophosphate at a very high rate and dolichyl monophosphate at a much lower rate. Does not act on phosphatidate. {ECO:0000269|PubMed:12198133}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12198133}; Multi-pass membrane protein {ECO:0000269|PubMed:12198133}. TISSUE SPECIFICITY: Widely expressed with highest levels in brain, kidney, lung and intestine. {ECO:0000269|PubMed:12198133}. +Q8VE49 DOXA1_MOUSE Dual oxidase maturation factor 1 (Dual oxidase activator 1) 341 37,588 Chain (1); Glycosylation (3); Sequence conflict (3); Topological domain (6); Transmembrane (5) TRANSMEM 25 45 Helical. {ECO:0000255}.; TRANSMEM 52 72 Helical. {ECO:0000255}.; TRANSMEM 184 204 Helical. {ECO:0000255}.; TRANSMEM 206 226 Helical. {ECO:0000255}.; TRANSMEM 250 270 Helical. {ECO:0000255}. TOPO_DOM 1 24 Extracellular. {ECO:0000255}.; TOPO_DOM 46 51 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 73 183 Extracellular. {ECO:0000255}.; TOPO_DOM 205 205 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 227 249 Extracellular. {ECO:0000255}.; TOPO_DOM 271 341 Cytoplasmic. {ECO:0000255}. FUNCTION: May be required for the maturation and the transport from the endoplasmic reticulum to the plasma membrane of functional DUOX1. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: May interact with NUMB. {ECO:0000250}. +Q9D311 DOXA2_MOUSE Dual oxidase maturation factor 2 320 35,427 Chain (1); Disulfide bond (2); Frameshift (1); Glycosylation (3); Sequence conflict (7); Topological domain (5); Transmembrane (5) TRANSMEM 22 42 Helical. {ECO:0000255}.; TRANSMEM 52 72 Helical. {ECO:0000255}.; TRANSMEM 184 204 Helical. {ECO:0000255}.; TRANSMEM 207 227 Helical. {ECO:0000255}.; TRANSMEM 250 270 Helical. {ECO:0000255}. TOPO_DOM 43 51 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 73 183 Extracellular. {ECO:0000255}.; TOPO_DOM 205 206 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 228 249 Extracellular. {ECO:0000255}.; TOPO_DOM 271 320 Cytoplasmic. {ECO:0000255}. FUNCTION: Required for the maturation and the transport from the endoplasmic reticulum to the plasma membrane of functional DUOX2. May play a role in thyroid hormone synthesis (By similarity). {ECO:0000250}. PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Heterodimer with DUXA2; disulfide-linked. {ECO:0000250}. +Q8K3H0 DP13A_MOUSE DCC-interacting protein 13-alpha (Dip13-alpha) (Adapter protein containing PH domain, PTB domain and leucine zipper motif 1) 707 79,328 Chain (1); Coiled coil (2); Domain (2); Erroneous initiation (2); Modified residue (5); Motif (1); Region (1); Sequence conflict (4) FUNCTION: Adapter protein that interacts with proteins involved in different cellular signaling pathways. Required for the regulation of cell proliferation in response to extracellular signals from an early endosomal compartment. Links Rab5 to nuclear signal transduction. Involved in the regulation of the insulin receptor signaling pathway. {ECO:0000250|UniProtKB:Q9UKG1}.; FUNCTION: Required for the regulation of cell proliferation in response to extracellular signals from an early endosomal compartment. Links Rab5 to nuclear signal transduction (By similarity). {ECO:0000250}. PTM: Phosphorylation at Ser-410 by PKA severely impairs binding to OCRL. {ECO:0000250|UniProtKB:Q9UKG1}. SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000269|PubMed:21849472}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9UKG1}. Nucleus {ECO:0000250|UniProtKB:Q9UKG1}. Note=Early endosomal membrane-bound and nuclear. Translocated into the nucleus upon release from endosomal membranes following internalization of EGF (By similarity). {ECO:0000250|UniProtKB:Q9UKG1}. SUBUNIT: Binds RAB5A/Rab5 through an N-terminal domain. This interaction is essential for its recruitment to endosomal membranes as well as its role in cell proliferation. Binds DCC and the catalytic domain of the inactive form of AKT2 through its PID domain. Binds PIK3CA and subunits of the NuRD/MeCP1 complex (By similarity). Interacts with OCRL and INPP5B. Interacts with NTRK2 (PubMed:21849472). {ECO:0000250|UniProtKB:Q9UKG1, ECO:0000269|PubMed:20133602, ECO:0000269|PubMed:21849472}. DOMAIN: Overexpression of an N-terminal domain (residues 1-319) or a C-terminal region (residues 273-707) has a proapoptotic effect. {ECO:0000250|UniProtKB:Q9UKG1}.; DOMAIN: The F&H motif, an approximately 12-13 amino-acid sequence centered around Phe and His residues, is essential for binding to OCRL and INPP5B. {ECO:0000250|UniProtKB:Q9UKG1}. +Q8K3G9 DP13B_MOUSE DCC-interacting protein 13-beta (Dip13-beta) (Adapter protein containing PH domain, PTB domain and leucine zipper motif 2) 662 73,854 Chain (1); Domain (2); Region (1); Sequence conflict (1) FUNCTION: Required for the regulation of cell proliferation in response to extracellular signals mediated by an early endosomal compartment. Links Rab5 to nuclear signal transduction (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Nucleus {ECO:0000250}. Note=Early endosomal membrane-bound and nuclear. Translocated into the nucleus upon release from endosomal membranes following internalization of EGF (By similarity). {ECO:0000250}. SUBUNIT: Binds RAB5A/Rab5 through an N-terminal domain. This interaction is essential for its recruitment to endosomal membranes as well as its role in cell proliferation. Binds subunits of the NuRD/MeCP1 complex (By similarity). {ECO:0000250}. +Q9CQS7 DPA5A_MOUSE Developmental pluripotency-associated protein 5A (mDppa5) (ES cell-associated transcript 2 protein) (Embryonal stem cell-specific gene 1 protein) (ESG-1) (Protein pH 34) 118 13,810 Chain (1); Domain (1) FUNCTION: Involved in the maintenance of embryonic stem (ES) cell pluripotency. Dispensable for self-renewal of pluripotent ES cells and establishment of germ cells. Associates with specific target mRNAs. {ECO:0000269|PubMed:16504174}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16166252, ECO:0000269|PubMed:16872451}. +P85965 DPA5B_MOUSE Developmental pluripotency-associated protein 5B/5C 119 13,948 Chain (1); Domain (1) FUNCTION: Involved in the maintenance of embryonic stem (ES) cell pluripotency. Dispensable for self-renewal of pluripotent ES cells and establishment of germ cells. Associates with specific target mRNAs (By similarity). {ECO:0000250|UniProtKB:Q9CQS7}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9CQS7}. +Q8BPA8 DPCD_MOUSE Protein DPCD 203 23,034 Alternative sequence (2); Chain (1) FUNCTION: May play a role in the formation or function of ciliated cells. {ECO:0000250}. +P31428 DPEP1_MOUSE Dipeptidase 1 (EC 3.4.13.19) (Membrane-bound dipeptidase 1) (MBD-1) (Microsomal dipeptidase) (Renal dipeptidase) 410 45,722 Binding site (3); Chain (1); Disulfide bond (3); Glycosylation (3); Lipidation (1); Metal binding (6); Propeptide (1); Sequence conflict (2); Signal peptide (1) FUNCTION: Hydrolyzes a wide range of dipeptides. Implicated in the renal metabolism of glutathione and its conjugates. Converts leukotriene D4 to leukotriene E4; it may play an important role in the regulation of leukotriene activity. SUBCELLULAR LOCATION: Apical cell membrane; Lipid-anchor, GPI-anchor. Cell projection, microvillus membrane; Lipid-anchor, GPI-anchor. Note=Brush border membrane. SUBUNIT: Homodimer; disulfide-linked. +Q8C255 DPEP2_MOUSE Dipeptidase 2 (EC 3.4.13.19) (Membrane-bound dipeptidase 2) (MBD-2) 478 52,664 Alternative sequence (4); Binding site (3); Chain (1); Disulfide bond (3); Glycosylation (2); Lipidation (1); Metal binding (6); Propeptide (1); Sequence conflict (3); Signal peptide (1) FUNCTION: Probable metalloprotease which hydrolyzes leukotriene D4 (LTD4) into leukotriene E4 (LTE4). SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12738806}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:12738806}. SUBUNIT: Homodimer; disulfide-linked. {ECO:0000255|PROSITE-ProRule:PRU10073}. TISSUE SPECIFICITY: Expressed in heart, lung, testis, spleen and skeletal muscle. {ECO:0000269|PubMed:12738806}. +Q9DA79 DPEP3_MOUSE Dipeptidase 3 (EC 3.4.13.19) (Membrane-bound dipeptidase 3) (MBD-3) (Protein expressed in male leptotene and zygotene spermatocytes 136) (MLZ-136) 493 54,247 Chain (1); Disulfide bond (3); Glycosylation (1); Lipidation (1); Metal binding (6); Propeptide (1); Signal peptide (1) FUNCTION: Probable metalloprotease which hydrolyzes cystinyl-bis-glycine. May be involved in meiosis. {ECO:0000269|PubMed:20339383}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12738806}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:12738806}. SUBUNIT: Homodimer; disulfide-linked (By similarity). Interacts with TEX101; co-localized on the cell surface of spermatocytes, spermatids, and testicular spermatozoa, co-localized only in cytoplasmic droplets of caput and corpus epididymal sperm (PubMed:21724266). {ECO:0000255|PROSITE-ProRule:PRU10073, ECO:0000269|PubMed:21724266}. TISSUE SPECIFICITY: Expressed in testis but not ovary. {ECO:0000269|PubMed:12738806, ECO:0000269|PubMed:20339383}. +Q9QX66 DPF1_MOUSE Zinc finger protein neuro-d4 (BRG1-associated factor 45B) (BAF45B) (D4, zinc and double PHD fingers family 1) 387 44,239 Alternative sequence (2); Chain (1); Cross-link (3); Natural variant (1); Zinc finger (3) FUNCTION: May have an important role in developing neurons by participating in regulation of cell survival, possibly as a neurospecific transcription factor. Belongs to the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth. {ECO:0000269|PubMed:17640523}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}. SUBUNIT: Component of neuron-specific chromatin remodeling complex (nBAF complex) composed of at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, DPF1/BAF45B, DPF3/BAF45C, ACTL6B/BAF53B and actin. {ECO:0000269|PubMed:17640523}. TISSUE SPECIFICITY: At embryonic stages, predominant expression in the nervous system. Expressed specifically in post-mitotic neurons (at protein level). {ECO:0000269|PubMed:17640523}. +P58269 DPF3_MOUSE Zinc finger protein DPF3 (BRG1-associated factor 45C) (BAF45C) (Zinc finger protein cer-d4) 378 43,070 Alternative sequence (3); Chain (1); Cross-link (1); Zinc finger (3) FUNCTION: Muscle-specific component of the BAF complex, a multiprotein complex involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Specifically binds acetylated lysines on histone 3 and 4 (H3K14ac, H3K9ac, H4K5ac, H4K8ac, H4K12ac, H4K16ac). In the complex, it acts as a tissue-specific anchor between histone acetylations and methylations and chromatin remodeling. It thereby probably plays an essential role in heart and skeletal muscle development (By similarity). Belongs to the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth. {ECO:0000250, ECO:0000269|PubMed:17640523}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the BAF complex, which includes at least actin (ACTB), ARID1A, ARID1B/BAF250, SMARCA2, SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57, SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more of SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C. In muscle cells, the BAF complex also contains DPF3. Interacts with acetylated histones H3 and H4 (By similarity). Component of neuron-specific chromatin remodeling complex (nBAF complex) composed of at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, DPF1/BAF45B, DPF3/BAF45C, ACTL6B/BAF53B and actin. {ECO:0000250, ECO:0000269|PubMed:17640523}. DOMAIN: The PHD-type zinc fingers mediate the binding to acetylated histones. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the heart and somites. Expressed in cerebellum and spinal cord, but not in cerebral cortex. Expressed specifically in post-mitotic neurons (at protein level). {ECO:0000269|PubMed:17640523, ECO:0000269|PubMed:18765789, ECO:0000269|PubMed:8812431}. +Q5NCQ5 DPH1_MOUSE 2-(3-amino-3-carboxypropyl)histidine synthase subunit 1 (EC 2.5.1.108) (Diphthamide biosynthesis protein 1) (Diphtheria toxin resistance protein 1) (Ovarian cancer-associated gene 1 protein homolog) (S-adenosyl-L-methionine:L-histidine 3-amino-3-carboxypropyltransferase 1) 438 48,004 Chain (1); Modified residue (1); Sequence conflict (3) Protein modification; peptidyl-diphthamide biosynthesis. FUNCTION: Required for the first step in the synthesis of diphthamide, a post-translational modification of histidine which occurs in translation elongation factor 2 (EEF2). Acts also as a tumor suppressor in lung and breast cancers. Plays a role in embryonic growth, organogenesis and postnatal survival. When overexpressed, suppresses colony formation ability and growth rate of ovarian cancer cells (By similarity). {ECO:0000250|UniProtKB:Q9BZG8, ECO:0000269|PubMed:14744934, ECO:0000269|PubMed:15485916}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11527402}. Cytoplasm {ECO:0000269|PubMed:11527402}. Note=Punctate, primarily perinuclear localization. SUBUNIT: Interacts with RBM8A (By similarity). Interacts with DPH2. {ECO:0000250|UniProtKB:Q9BZG8, ECO:0000269|PubMed:15485916}. TISSUE SPECIFICITY: Strongly expressed in kidney and liver. Moderately expressed in brain, skin and testis. Weakly expressed in heart, lung, small intestine, spleen, stomach and thymus. {ECO:0000269|PubMed:11527402}. +Q9CR25 DPH2_MOUSE 2-(3-amino-3-carboxypropyl)histidine synthase subunit 2 (EC 2.5.1.108) (Diphthamide biosynthesis protein 2) (Diphtheria toxin resistance protein 2) (MmDph2) (S-adenosyl-L-methionine:L-histidine 3-amino-3-carboxypropyltransferase DPH2) 489 52,365 Chain (1); Compositional bias (1); Modified residue (5); Sequence conflict (1) Protein modification; peptidyl-diphthamide biosynthesis. FUNCTION: Required for the first step in the synthesis of diphthamide, a post-translational modification of histidine which occurs in translation elongation factor 2 (EEF2). {ECO:0000269|PubMed:15485916}. SUBUNIT: Interacts with DPH1. {ECO:0000269|PubMed:15485916}. +Q8K0W9 DPH3_MOUSE DPH3 homolog (CSL-type zinc finger-containing protein 2) (DelGEF-interacting protein 1) (DelGIP1) 82 9,286 Beta strand (6); Chain (1); Helix (3); Turn (3); Zinc finger (1) Protein modification; peptidyl-diphthamide biosynthesis. FUNCTION: Essential for the first step in the synthesis of diphthamide, a post-translational modification of histidine which occurs in elongation factor 2.; FUNCTION: Down-regulation increases extracellular release of proteoglycans, indicating a possible role in the secretion process. Stimulates binding of GNEFR to SEC5 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed with highest levels in heart, liver, kidney and testis. {ECO:0000269|PubMed:14527407}. +Q9CWQ0 DPH5_MOUSE Diphthine methyl ester synthase (EC 2.1.1.314) (Diphthamide biosynthesis methyltransferase) 281 31,218 Binding site (6); Chain (1); Modified residue (1); Region (1); Sequence conflict (1) Protein modification; peptidyl-diphthamide biosynthesis. FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that catalyzes four methylations of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine methyl ester. The four successive methylation reactions represent the second step of diphthamide biosynthesis. {ECO:0000250|UniProtKB:P32469, ECO:0000269|PubMed:15485916}. +Q9CQ28 DPH6_MOUSE Diphthine--ammonia ligase (EC 6.3.1.14) (ATP-binding domain-containing protein 4) (Diphthamide synthase) (Diphthamide synthetase) (Protein DPH6 homolog) 267 29,922 Alternative sequence (2); Chain (1); Modified residue (1) Protein modification; peptidyl-diphthamide biosynthesis. FUNCTION: Amidase that catalyzes the last step of diphthamide biosynthesis using ammonium and ATP. Diphthamide biosynthesis consists in the conversion of an L-histidine residue in the translation elongation factor 2 (EEF2) to diphthamide (By similarity). {ECO:0000250}. +Q9CYU6 DPH7_MOUSE Diphthine methyltransferase (EC 3.1.1.97) (Diphthamide biosynthesis protein 7) (DPH7) (WD repeat-containing protein 85) 477 53,201 Alternative sequence (2); Chain (1); Erroneous termination (1); Repeat (3); Sequence conflict (7) Protein modification; peptidyl-diphthamide biosynthesis. FUNCTION: Catalyzes the demethylation of diphthine methyl ester to form diphthine, an intermediate diphthamide biosynthesis, a post-translational modification of histidine which occurs in translation elongation factor 2 (EEF2). {ECO:0000250|UniProtKB:Q9BTV6}. SUBUNIT: Interacts with INCA1. {ECO:0000250|UniProtKB:Q9BTV6}. +O70152 DPM1_MOUSE Dolichol-phosphate mannosyltransferase subunit 1 (EC 2.4.1.83) (Dolichol-phosphate mannose synthase subunit 1) (DPM synthase subunit 1) (Dolichyl-phosphate beta-D-mannosyltransferase subunit 1) (Mannose-P-dolichol synthase subunit 1) (MPD synthase) 260 29,175 Chain (1); Initiator methionine (1); Modified residue (3); Sequence conflict (2) Protein modification; protein glycosylation. FUNCTION: Transfers mannose from GDP-mannose to dolichol monophosphate to form dolichol phosphate mannose (Dol-P-Man) which is the mannosyl donor in pathways leading to N-glycosylation, glycosyl phosphatidylinositol membrane anchoring, and O-mannosylation of proteins; catalytic subunit of the dolichol-phosphate mannose (DPM) synthase complex. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum. SUBUNIT: Component of the dolichol-phosphate mannose (DPM) synthase complex composed of DPM1, DPM2 and DPM3; in the complex interacts directly with DPM3. {ECO:0000250}. +Q9Z324 DPM2_MOUSE Dolichol phosphate-mannose biosynthesis regulatory protein (Dolichol-phosphate mannose synthase subunit 2) (DPM synthase subunit 2) 84 9,376 Chain (1); Transmembrane (2) TRANSMEM 11 31 Helical. {ECO:0000255}.; TRANSMEM 49 69 Helical. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Regulates the biosynthesis of dolichol phosphate-mannose. Regulatory subunit of the dolichol-phosphate mannose (DPM) synthase complex; essential for the ER localization and stable expression of DPM1. When associated with the GPI-GlcNAc transferase (GPI-GnT) complex enhances but is not essential for its activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SUBUNIT: Component of the dolichol-phosphate mannose (DPM) synthase complex composed of DPM1, DPM2 and DPM3; in the complex interacts directly with DPM3. Associates with the GPI-GlcNAc transferase (GPI-GnT) complex (By similarity). {ECO:0000250}. +Q9D1Q4 DPM3_MOUSE Dolichol-phosphate mannosyltransferase subunit 3 (Dolichol-phosphate mannose synthase subunit 3) (DPM synthase subunit 3) (Dolichyl-phosphate beta-D-mannosyltransferase subunit 3) (Mannose-P-dolichol synthase subunit 3) (MPD synthase subunit 3) 92 10,139 Chain (1); Transmembrane (2) TRANSMEM 8 28 Helical. {ECO:0000255}.; TRANSMEM 37 57 Helical. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Stabilizer subunit of the dolichol-phosphate mannose (DPM) synthase complex; tethers catalytic subunit DPM1 to the ER. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Component of the dolichol-phosphate mannose (DPM) synthase complex composed of DPM1, DPM2 and DPM3; in the complex associated with DPM1 via its C-terminal domain and with DPM2 via its N-terminal portion. {ECO:0000250}. +Q61419 CMAH_MOUSE Cytidine monophosphate-N-acetylneuraminic acid hydroxylase (CMP-N-acetylneuraminic acid hydroxylase) (EC 1.14.18.2) (CMP-N-acetylneuraminate monooxygenase) (CMP-Neu5Ac hydroxylase) (CMP-NeuAc hydroxylase) 577 66,936 Alternative sequence (1); Chain (1); Domain (1); Erroneous initiation (3); Metal binding (4); Propeptide (1); Sequence conflict (1) Amino-sugar metabolism; N-acetylneuraminate metabolism. FUNCTION: Sialic acids are components of carbohydrate chains of glycoconjugates and are involved in cell-cell recognition and cell-pathogen interactions. Catalyzes the conversion of CMP-N-acetylneuraminic acid (CMP-Neu5Ac) into its hydroxylated derivative CMP-N-glycolylneuraminic acid (CMP-Neu5Gc), a sialic acid abundantly expressed at the surface of many cells. {ECO:0000269|PubMed:22692205}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7608218, ECO:0000269|PubMed:8781965}.; SUBCELLULAR LOCATION: Isoform 2: Endoplasmic reticulum {ECO:0000305}. TISSUE SPECIFICITY: Expressed in all tissues tested, except in brain. {ECO:0000269|PubMed:7608218}. +A3KGF9 CCD9B_MOUSE Coiled-coil domain-containing protein 9B 545 58,688 Chain (1); Coiled coil (1); Erroneous initiation (1); Modified residue (1); Sequence conflict (1) +Q9D4K7 CC105_MOUSE Coiled-coil domain-containing protein 105 499 57,304 Chain (1); Coiled coil (2); Frameshift (1); Modified residue (2); Sequence conflict (3) +Q9DCC3 CC107_MOUSE Coiled-coil domain-containing protein 107 242 26,579 Alternative sequence (1); Chain (1); Coiled coil (1); Frameshift (1); Signal peptide (1); Transmembrane (1) TRANSMEM 65 85 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q8VDP4 CCAR2_MOUSE Cell cycle and apoptosis regulator protein 2 (Cell division cycle and apoptosis regulator protein 2) 922 103,002 Chain (1); Coiled coil (2); Cross-link (2); Erroneous initiation (2); Modified residue (17); Region (2); Sequence conflict (3) FUNCTION: Core component of the DBIRD complex, a multiprotein complex that acts at the interface between core mRNP particles and RNA polymerase II (RNAPII) and integrates transcript elongation with the regulation of alternative splicing: the DBIRD complex affects local transcript elongation rates and alternative splicing of a large set of exons embedded in (A + T)-rich DNA regions. Inhibits SIRT1 deacetylase activity leading to increasing levels of p53/TP53 acetylation and p53-mediated apoptosis (By similarity). As part of a histone H3-specific methyltransferase complex may mediate ligand-dependent transcriptional activation by nuclear hormone receptors (By similarity). Inhibits SUV39H1 methyltransferase activity. Plays a critical role in maintaining genomic stability and cellular integrity following UV-induced genotoxic stress (By similarity) Regulates the circadian expression of the core clock components NR1D1 and ARNTL/BMAL1. Enhances the transcriptional repressor activity of NR1D1 through stabilization of NR1D1 protein levels by preventing its ubiquitination and subsequent degradation. Acts as a regulator of PCK1 expression and gluconeogenesis by a mechanism that involves, at least in part, both NR1D1 and SIRT1 (PubMed:24415752). Negatively regulates the deacetylase activity of HDAC3 and can alter its subcellular localization (PubMed:21030595). Plays an important role in tumor suppression through p53/TP53 regulation; stabilizes p53/TP53 by affecting its interaction with ubiquitin ligase MDM2 (PubMed:25732823). Represses the ligand-dependent transcriptional activation function of ESR2. Positively regulates the beta-catenin pathway (canonical Wnt signaling pathway) and is required for MCC-mediated repression of the beta-catenin pathway. Represses ligand-dependent transcriptional activation function of NR1H2 and NR1H3 and inhibits the interaction of SIRT1 with NR1H3. Represses the transcriptional activator activity of BRCA1. Inhibits SIRT1 in a CHEK2 and PSEM3-dependent manner and inhibits the activity of CHEK2 in vitro (By similarity). {ECO:0000250|UniProtKB:Q8N163, ECO:0000269|PubMed:23398316}. PTM: Acetylation at Lys-112 and Lys-215 by KAT8 prevents inhibitory binding to SIRT1 and increases its deacetylase activity. {ECO:0000250|UniProtKB:Q8N163}.; PTM: Genotoxic stress induces its sumoylation and sumoylation promotes the SIRT1-CCAR2 interaction which in turn inhibits SIRT1-mediated deacetylation of p53/TP53. Sumoylation leads to transcriptional activation of p53/TP53 by sequestering SIRT1 from p53/TP53. Desumoylated by SENP1. {ECO:0000250|UniProtKB:Q8N163}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8N163}. Cytoplasm {ECO:0000250|UniProtKB:Q8N163}. Note=Recruited to chromatin, post-UV irradiation. Sequestered to the cytoplasm in the presence of MCC. Translocated to the cytoplasm during UV-induced apoptosis. {ECO:0000250|UniProtKB:Q8N163}. SUBUNIT: Component of the DBIRD complex. Interacts with ZNF326/ZIRD; the interaction is direct. Interacts (via N-terminus) with SIRT1, which inhibits the deacetylation of substrates. Interacts (via N-terminus) with SUV39H1; this interaction abolishes the interaction with SIRT1. Part of a complex composed at least of ASCL2, EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; this complex may have a histone H3-specific methyltransferase activity. Interacts with NR1D1. Interacts (via N-terminus) with ESR1 and ESR2. Interacts (via N-terminus) with HDAC3 (via C-terminus). Interacts with HDAC1 and MED2F. Interacts with MCC. Interacts (via N-terminus) with NR1H2 and NR1H3 in a ligand-independent manner. Interacts with CSNK2A1. Interacts (via N-terminus) with p53/TP53. Interacts (via N-terminus) with BRCA1 (via the BRCT domains). Interacts (via N-terminus) with CHEK2 (via protein kinase domain). Interacts with PSEM3. Interacts (via N-terminus) with PSIA3 and SENP1. The sumoylated form shows a preferential interaction with SIRT1 as compared to its unmodified form (By similarity). {ECO:0000250|UniProtKB:Q8N163, ECO:0000269|PubMed:19218236, ECO:0000269|PubMed:21030595, ECO:0000269|PubMed:23398316, ECO:0000269|PubMed:24415752, ECO:0000269|PubMed:25732823}. +P48298 CCL11_MOUSE Eotaxin (C-C motif chemokine 11) (Eosinophil chemotactic protein) (Small-inducible cytokine A11) 97 10,893 Chain (1); Disulfide bond (2); Glycosylation (1); Signal peptide (1) FUNCTION: In response to the presence of allergens, this protein directly promotes the accumulation of eosinophils (a prominent feature of allergic inflammatory reactions), but not lymphocytes, macrophages or neutrophils. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Expressed constitutively in the thymus. Expression inducible in the lung (type I alveolar epithelial cells), intestine, heart, spleen, kidney. +O35903 CCL25_MOUSE C-C motif chemokine 25 (Chemokine TECK) (Small-inducible cytokine A25) (Thymus-expressed chemokine) 144 16,733 Chain (1); Disulfide bond (2); Sequence conflict (1); Signal peptide (1) FUNCTION: Potentially involved in T-cell development. Recombinant protein shows chemotactic activity on thymocytes, macrophages, THP-1 cells, and dendritics cells but is inactive on peripheral blood lymphocytes and neutrophils. Binds to CCR9. Binds to atypical chemokine receptor ACKR4 and mediates the recruitment of beta-arrestin (ARRB1/2) to ACKR4. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Specifically expressed by thymic dendritic cells. High levels in thymus and small intestine. +Q3V036 CCD27_MOUSE Coiled-coil domain-containing protein 27 639 73,651 Chain (1); Coiled coil (1); Compositional bias (1) +Q8VDP6 CDIPT_MOUSE CDP-diacylglycerol--inositol 3-phosphatidyltransferase (EC 2.7.8.11) (Phosphatidylinositol synthase) (PI synthase) (PtdIns synthase) 213 23,599 Chain (1); Transmembrane (5) TRANSMEM 6 26 Helical. {ECO:0000255}.; TRANSMEM 29 49 Helical. {ECO:0000255}.; TRANSMEM 74 94 Helical. {ECO:0000255}.; TRANSMEM 140 160 Helical. {ECO:0000255}.; TRANSMEM 175 195 Helical. {ECO:0000255}. FUNCTION: Catalyzes the biosynthesis of phosphatidylinositol (PtdIns) as well as PtdIns:inositol exchange reaction. May thus act to reduce an excessive cellular PtdIns content. The exchange activity is due to the reverse reaction of PtdIns synthase and is dependent on CMP, which is tightly bound to the enzyme (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Membrane {ECO:0000250}. +P49615 CDK5_MOUSE Cyclin-dependent-like kinase 5 (EC 2.7.11.1) (CR6 protein kinase) (CRK6) (Cell division protein kinase 5) (Serine/threonine-protein kinase PSSALRE) (Tau protein kinase II catalytic subunit) (TPKII catalytic subunit) 292 33,288 Active site (1); Binding site (1); Chain (1); Domain (1); Modified residue (5); Mutagenesis (1); Nucleotide binding (1) FUNCTION: Proline-directed serine/threonine-protein kinase essential for neuronal cell cycle arrest and differentiation and may be involved in apoptotic cell death in neuronal diseases by triggering abortive cell cycle re-entry. Interacts with D1 and D3-type G1 cyclins. Phosphorylates SRC, NOS3, VIM/vimentin, p35/CDK5R1, MEF2A, SIPA1L1, SH3GLB1, PXN, PAK1, MCAM/MUC18, SEPT5, SYN1, DNM1, AMPH, SYNJ1, CDK16, RAC1, RHOA, CDC42, TONEBP/NFAT5, MAPT/TAU, MAP1B, histone H1, p53/TP53, HDAC1, APEX1, PTK2/FAK1, huntingtin/HTT, ATM, MAP2, NEFH and NEFM. Regulates several neuronal development and physiological processes including neuronal survival, migration and differentiation, axonal and neurite growth, synaptogenesis, oligodendrocyte differentiation, synaptic plasticity and neurotransmission, by phosphorylating key proteins. Activated by interaction with CDK5R1 (p35) and CDK5R2 (p39), especially in post-mitotic neurons, and promotes CDK5R1 (p35) expression in an autostimulation loop. Phosphorylates many downstream substrates such as Rho and Ras family small GTPases (e.g. PAK1, RAC1, RHOA, CDC42) or microtubule-binding proteins (e.g. MAPT/TAU, MAP2, MAP1B), and modulates actin dynamics to regulate neurite growth and/or spine morphogenesis. Phosphorylates also exocytosis associated proteins such as MCAM/MUC18, SEPT5, SYN1, and CDK16/PCTAIRE1 as well as endocytosis associated proteins such as DNM1, AMPH and SYNJ1 at synaptic terminals. In the mature central nervous system (CNS), regulates neurotransmitter movements by phosphorylating substrates associated with neurotransmitter release and synapse plasticity; synaptic vesicle exocytosis, vesicles fusion with the presynaptic membrane, and endocytosis. Promotes cell survival by activating anti-apoptotic proteins BCL2 and STAT3, and negatively regulating of JNK3/MAPK10 activity. Phosphorylation of p53/TP53 in response to genotoxic and oxidative stresses enhances its stabilization by preventing ubiquitin ligase-mediated proteasomal degradation, and induces transactivation of p53/TP53 target genes, thus regulating apoptosis. Phosphorylation of p35/CDK5R1 enhances its stabilization by preventing calpain-mediated proteolysis producing p25/CDK5R1 and avoiding ubiquitin ligase-mediated proteasomal degradation. During aberrant cell-cycle activity and DNA damage, p25/CDK5 activity elicits cell-cycle activity and double-strand DNA breaks that precedes neuronal death by deregulating HDAC1. DNA damage triggered phosphorylation of huntingtin/HTT in nuclei of neurons protects neurons against polyglutamine expansion as well as DNA damage mediated toxicity. Phosphorylation of PXN reduces its interaction with PTK2/FAK1 in matrix-cell focal adhesions (MCFA) during oligodendrocytes (OLs) differentiation. Negative regulator of Wnt/beta-catenin signaling pathway. Activator of the GAIT (IFN-gamma-activated inhibitor of translation) pathway, which suppresses expression of a post-transcriptional regulon of proinflammatory genes in myeloid cells; phosphorylates the linker domain of glutamyl-prolyl tRNA synthetase (EPRS) in a IFN-gamma-dependent manner, the initial event in assembly of the GAIT complex. Phosphorylation of SH3GLB1 is required for autophagy induction in starved neurons. Phosphorylation of TONEBP/NFAT5 in response to osmotic stress mediates its rapid nuclear localization. MEF2 is inactivated by phosphorylation in nucleus in response to neurotoxin, thus leading to neuronal apoptosis. APEX1 AP-endodeoxyribonuclease is repressed by phosphorylation, resulting in accumulation of DNA damage and contributing to neuronal death. NOS3 phosphorylation down regulates NOS3-derived nitrite (NO) levels. SRC phosphorylation mediates its ubiquitin-dependent degradation and thus leads to cytoskeletal reorganization. May regulate endothelial cell migration and angiogenesis via the modulation of lamellipodia formation. Involved in dendritic spine morphogenesis by mediating the EFNA1-EPHA4 signaling. The complex p35/CDK5 participates in the regulation of the circadian clock by modulating the function of CLOCK protein: phosphorylates CLOCK at 'Thr-451' and 'Thr-461' and regulates the transcriptional activity of the CLOCK-ARNTL/BMAL1 heterodimer in association with altered stability and subcellular distribution. {ECO:0000269|PubMed:12941275, ECO:0000269|PubMed:17143272, ECO:0000269|PubMed:20473298, ECO:0000269|PubMed:21210220, ECO:0000269|PubMed:24235147}. PTM: Phosphorylation on Tyr-15 by ABL1 and FYN, and on Ser-159 by casein kinase 1 promotes kinase activity. By contrast, phosphorylation at Thr-14 inhibits activity (By similarity). {ECO:0000250}.; PTM: Phosphorylation at Ser-159 is essential for maximal catalytic activity. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:11517264}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Perikaryon {ECO:0000250}. Cell projection, lamellipodium {ECO:0000269|PubMed:11517264}. Cell projection, growth cone {ECO:0000269|PubMed:11517264}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250}. Note=In axonal growth cone with extension to the peripheral lamellipodia. Under neurotoxic stress and neuronal injury conditions, CDK5R1 (p35) is cleaved by calpain to generate CDK5R1 (p25) in response to increased intracellular calcium. The elevated level of p25, when in complex with CDK5, leads to its subcellular misallocation as well as its hyperactivation. Colocalizes with CTNND2 in the cell body of neuronal cells, and with CTNNB1 in the cell-cell contacts and plasma membrane of undifferentiated and differentiated neuroblastoma cells. Reversibly attached to the plasma membrane in an inactive form when complexed to dephosphorylated p35 or CDK5R2 (p39), p35 phosphorylation releases this attachment and activates CDK5 (By similarity). {ECO:0000250}. SUBUNIT: Heterodimer composed of a catalytic subunit CDK5 and a regulatory subunit CDK5R1 (p25) and macromolecular complex composed of at least CDK5, CDK5R1 (p35) and CDK5RAP1 or CDK5RAP2 or CDK5RAP3. Only the heterodimer shows kinase activity. Under neurotoxic stress and neuronal injury conditions, p35 is cleaved by calpain to generate p25 that hyperactivates CDK5, that becomes functionally disabled and often toxic. Found in a trimolecular complex with CABLES1 and ABL1. Interacts with CABLES1 and CABLES2. Interacts with AATK and GSTP1. Binds to HDAC1 when in complex with p25. Interaction with myristoylation p35 promotes CDK5 association with membranes. Both isoforms 1 and 2 interacts with beta-catenin/CTNNB1. Interacts with delta-catenin/CTNND2 and APEX1. Interacts with P53/TP53 in neurons (By similarity). Interacts with EPHA4; may mediate the activation of NGEF by EPHA4M. Interacts with PTK2/FAK1. The complex p35/CDK5 interacts with CLOCK (By similarity). Interacts with HTR6 (PubMed:25078650). {ECO:0000250, ECO:0000269|PubMed:25078650}. TISSUE SPECIFICITY: Specifically expressed in post-mitotic neurons and postsynaptic muscle. {ECO:0000269|PubMed:16203963}. +Q8R3A2 CDPF1_MOUSE Cysteine-rich DPF motif domain-containing protein 1 119 13,300 Chain (1); Sequence conflict (2) +P46414 CDN1B_MOUSE Cyclin-dependent kinase inhibitor 1B (Cyclin-dependent kinase inhibitor p27) (p27Kip1) 197 22,193 Chain (1); Modified residue (7); Motif (1); Mutagenesis (4); Region (1); Sequence conflict (6); Site (1) FUNCTION: Important regulator of cell cycle progression (PubMed:8033213, PubMed:12972555). Inhibits the kinase activity of CDK2 bound to cyclin A, but has little inhibitory activity on CDK2 bound to SPDYA (By similarity). Involved in G1 arrest. Potent inhibitor of cyclin E- and cyclin A-CDK2 complexes (PubMed:8033213). Forms a complex with cyclin type D-CDK4 complexes and is involved in the assembly, stability, and modulation of CCND1-CDK4 complex activation. Acts either as an inhibitor or an activator of cyclin type D-CDK4 complexes depending on its phosphorylation state and/or stoichometry. {ECO:0000250|UniProtKB:P46527, ECO:0000269|PubMed:12093740, ECO:0000269|PubMed:12972555, ECO:0000269|PubMed:15528185, ECO:0000269|PubMed:20228253, ECO:0000269|PubMed:8033213, ECO:0000269|PubMed:9399644}. PTM: Phosphorylated; phosphorylation occurs on serine, threonine and tyrosine residues. Phosphorylation on Ser-10 is the major site of phosphorylation in resting cells, takes place at the G(0)-G(1) phase and leads to protein stability. Phosphorylation on other sites is greatly enhanced by mitogens, growth factors, MYC and in certain cancer cell lines. The phosphorylated form found in the cytoplasm is inactivate. Phosphorylation on Thr-197 is required for interaction with 14-3-3 proteins. Phosphorylation on Thr-187, by CDK1 and CDK2 leads to protein ubiquitination and proteasomal degradation. Tyrosine phosphorylation promotes this process. Phosphorylation by PKB/AKT1 can be suppressed by LY294002, an inhibitor of the catalytic subunit of PI3K. Phosphorylation on Tyr-88 and Tyr-89 has no effect on binding CDK2, but is required for binding CDK4. Dephosphorylated on tyrosine residues by G-CSF (By similarity). Dephosphorylated on Thr-187 by PPM1H, leading to CDKN1B stability (By similarity). {ECO:0000250|UniProtKB:P46527}.; PTM: Ubiquitinated; in the cytoplasm by the KPC complex (composed of RNF123/KPC1 and UBAC1/KPC2) and, in the nucleus, by SCF(SKP2). The latter requires prior phosphorylation on Thr-187. Ubiquitinated; by a TRIM21-containing SCF(SKP2)-like complex; leads to its degradation (By similarity). {ECO:0000250}.; PTM: Subject to degradation in the lysosome. Interaction with SNX6 promotes lysosomal degradation. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Endosome {ECO:0000269|PubMed:20228253}. Note=Nuclear and cytoplasmic in quiescent cells. AKT- or RSK-mediated phosphorylation on Thr-197, binds 14-3-3, translocates to the cytoplasm and promotes cell cycle progression. Mitogen-activated UHMK1 phosphorylation on Ser-10 also results in translocation to the cytoplasm and cell cycle progression. Phosphorylation on Ser-10 facilitates nuclear export. Translocates to the nucleus on phosphorylation of Tyr-88 and Tyr-89 (By similarity). Colocalizes at the endosome with SNX6; this leads to lysosomal degradation (PubMed:20228253). {ECO:0000250, ECO:0000269|PubMed:20228253}. SUBUNIT: Forms a ternary complex composed of CCNE1, CDK2 and CDKN1B. Interacts directly with CCNE1; the interaction is inhibited by CDK2-dependent phosphorylation on Thr-187. Interacts with COPS5, subunit of the COP9 signalosome complex; the interaction leads to CDKN1B degradation. Interacts with NUP50; the interaction leads to nuclear import and degradation of phosphorylated CDKN1B. Interacts with CCND1 and SNX6 (By similarity). Interacts (Thr-197-phosphorylated form) with 14-3-3 proteins, binds strongly YWHAQ, weakly YWHAE and YWHAH, but not YWHAB nor YWHAZ; the interaction with YWHAQ results in translocation to the cytoplasm. Interacts with AKT1 and LYN; the interactions lead to cytoplasmic mislocation, phosphorylation of CDKN1B and inhibition of cell cycle arrest. Forms a ternary complex with CCNA2 and CDK2; CDKN1B inhibits the kinase activity of CDK2 through conformational rearrangements. Interacts (unphosphorylated form) with CDK2. Forms a complex with CDK2 and SPDYA, but does not directly interact with SPDYA. Forms a ternary complex composed of cyclin D, CDK4 and CDKN1B. Interacts (phosphorylated on Tyr-88 and Tyr-89) with CDK4; the interaction is required for cyclin D and CDK4 complex assembly, induces nuclear translocation and activates the CDK4 kinase activity. Interacts with GRB2. Interacts with PIM1. Identified in a complex with SKP1, SKP2 and CKS1B. Interacts with UHMK1; the interaction leads to cytoplasmic mislocation, phosphorylation of CDKN1B and inhibition of cell cycle arrest. Interacts also with CDK1. Dephosphorylated on Thr-187 by PPM1H, leading to CDKN1B stability (By similarity). {ECO:0000250|UniProtKB:P46527, ECO:0000269|PubMed:10086358, ECO:0000269|PubMed:10811608, ECO:0000269|PubMed:12093740, ECO:0000269|PubMed:12972555, ECO:0000269|PubMed:19767775, ECO:0000269|PubMed:20228253, ECO:0000269|PubMed:8534916, ECO:0000269|PubMed:9399644}. DOMAIN: A peptide sequence containing only AA 28-79 retains substantial Kip1 cyclin A/CDK2 inhibitory activity. {ECO:0000250}. +Q7TPC1 CDSN_MOUSE Corneodesmosin 561 54,313 Chain (1); Compositional bias (1); Sequence conflict (9); Signal peptide (1) FUNCTION: Important for the epidermal barrier integrity. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. Note=Found in corneodesmosomes, the intercellular structures that are involved in desquamation. {ECO:0000250}. +Q8BGC1 CE022_MOUSE UPF0489 protein C5orf22 homolog 442 49,430 Alternative sequence (2); Chain (1); Modified residue (2); Sequence conflict (1) +Q24JP4 CE047_MOUSE Uncharacterized protein C5orf47 homolog 165 18,286 Chain (1); Sequence conflict (2) +Q9DAR0 CE049_MOUSE Uncharacterized protein C5orf49 homolog (Y regulated sperm protein) 182 20,848 Chain (1) TISSUE SPECIFICITY: Expressed in sperm (at protein level). {ECO:0000269|Ref.3}. +E9Q2Z1 CECR2_MOUSE Cat eye syndrome critical region protein 2 homolog 1453 161,530 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (1); Modified residue (7) FUNCTION: Chromatin reader component of histone-modifying complexes, such as the CERF (CECR2-containing-remodeling factor) complex and ISWI-type complex (By similarity). It thereby plays a role in various processes during development: required during embryogenesis for neural tube closure and inner ear development (PubMed:15640247, PubMed:20589882, PubMed:21246654). In adults, required for spermatogenesis, via the formation of ISWI-type chromatin complexes (PubMed:22154806). In histone-modifying complexes, CECR2 recognizes and binds acylated histones: binds histones that are acetylated and/or butyrylated (By similarity). May also be involved through its interaction with LRPPRC in the integration of cytoskeletal network with vesicular trafficking, nucleocytosolic shuttling, transcription, chromosome remodeling and cytokinesis (By similarity). {ECO:0000250|UniProtKB:Q9BXF3, ECO:0000269|PubMed:15640247, ECO:0000269|PubMed:20589882, ECO:0000269|PubMed:21246654, ECO:0000269|PubMed:22154806}. SUBUNIT: Part of the CECR2-containing remodeling factor (CERF) complex which contains CECR2 and SMARCA1. Interacts with acetylated lysine residues on histone H2A and H3 (in vitro). Interacts with LRPPRC. {ECO:0000250|UniProtKB:Q9BXF3}. DOMAIN: The Bromo domain recognizes and binds acetylated histones. Also recognizes and binds histones that are butyrylated. {ECO:0000250|UniProtKB:Q9BXF3}. +Q6A078 CE290_MOUSE Centrosomal protein of 290 kDa (Cep290) (Bardet-Biedl syndrome 14 protein homolog) (Nephrocystin-6) 2472 289,077 Alternative sequence (2); Chain (1); Coiled coil (3); Mutagenesis (1); Region (3); Sequence conflict (11) FUNCTION: Involved in early and late steps in cilia formation (PubMed:21565611). Its association with CCP110 is required for inhibition of primary cilia formation by CCP110 (By similarity). May play a role in early ciliogenesis in the disappearance of centriolar satellites and in the transition of primary ciliar vesicles (PCVs) to capped ciliary vesicles (CCVs). Required for the centrosomal recruitment of RAB8A and for the targeting of centriole satellite proteins to centrosomes such as of PCM1 (By similarity). Required for the correct localization of ciliary and phototransduction proteins in retinal photoreceptor cells; may play a role in ciliary transport processes (PubMed:16632484). Required for efficient recruitment of RAB8A to primary cilium (By similarity). In the ciliary transition zone is part of the tectonic-like complex (also named B9 complex) which is required for tissue-specific ciliogenesis and may regulate ciliary membrane composition (PubMed:21725307). Involved in regulation of the BBSome complex integrity, specifically for presence of BBS2, BBS5 and BBS8/TTC8 in the complex, and in ciliary targeting of selected BBSome cargos. May play a role in controlling entry of the BBSome complex to cilia possibly implicating IQCB1/NPHP5 (By similarity). Activates ATF4-mediated transcription (By similarity). {ECO:0000250|UniProtKB:O15078, ECO:0000269|PubMed:16632484, ECO:0000269|PubMed:21565611, ECO:0000269|PubMed:21725307}. PTM: Ubiquitinated. May undergo monoubiquitination; monoubiquitination is inhibited in response to cellular stress, such as ultraviolet light (UV) radiation or heat shock, but does not cause it displacement from centriolar satellites (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:16632484, ECO:0000269|PubMed:16682970, ECO:0000269|PubMed:16682973}. Cytoplasm {ECO:0000269|PubMed:16682973}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000269|PubMed:21725307}. Nucleus {ECO:0000269|PubMed:16632484, ECO:0000269|PubMed:16682973}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:16632484, ECO:0000269|PubMed:16682970, ECO:0000269|PubMed:23807208}. Cell projection, cilium {ECO:0000269|PubMed:16632484, ECO:0000269|PubMed:16682970, ECO:0000269|PubMed:23943788}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:23807208}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:O15078}. Note=Displaced from centriolar satellites in response to cellular stress, such as ultraviolet light (UV) radiation or heat shock (By similarity). Found in the connecting cilium of photoreceptor cells (PubMed:16632484, PubMed:23943788), base of cilium in kidney intramedullary collecting duct cells (PubMed:16682970). Localizes at the transition zone, a region between the basal body and the ciliary axoneme (PubMed:21725307). Localization at the ciliary transition zone as well as at centriolar satellites is BBsome-dependent (By similarity). {ECO:0000250|UniProtKB:O15078, ECO:0000269|PubMed:16632484, ECO:0000269|PubMed:16682970, ECO:0000269|PubMed:21725307, ECO:0000269|PubMed:23943788}. SUBUNIT: Part of the tectonic-like complex (also named B9 complex) (PubMed:21725307). Interacts with ATF4 via its N-terminal region (By similarity). Associates with the BBSome complex, interacting (via N-terminus) with BBS4 (By similarity). Interacts with IQCB1/NPHP5; IQCB1 and CEP290/NPHP6 are proposed to form a functional NPHP5-6 module localized to the centrosome. Interacts with NPHP4; the interaction likely requires additional interactors (PubMed:21565611). Interacts with ZNF423, FAM161A, CEP162, CEP162, CEP131, TALPID3, CCDC13, CC2D2A, RPGRIP1 (By similarity). Can self-associate (homo- or heteromeric) (By similarity). Interacts with CCP110; required for suppressing cilia formation (By similarity). Interacts with RPGR (PubMed:16632484). Associates (via C-terminus) with microtubules; association to microtubule is reduced in response to cellular stress, such as ultraviolet light (UV) radiation or heat shock, in a process that requires p38 MAP kinase signaling (By similarity). Interacts with FAM161A (By similarity). Interacts with PCM1 (PubMed:17705300). Interacts with CCDC66 (By similarity). {ECO:0000250|UniProtKB:O15078, ECO:0000250|UniProtKB:Q9TU23, ECO:0000269|PubMed:16632484, ECO:0000269|PubMed:17705300, ECO:0000269|PubMed:21565611, ECO:0000269|PubMed:21725307}. TISSUE SPECIFICITY: Expressed in multiple organs during early postnatal development, with highest levels in hindbrain. {ECO:0000269|PubMed:16682970}. DISEASE: Note=Defects in Cep290 are a cause of early-onset retinal degeneration with autosomal recessive inheritance. The rd16 mutant carries a deletion of residues 1599-1897 in the Cep290 protein. Homozygous rd16 mice are characterized by the appearance of white retinal vessels at 1 month of age and large pigment patches at 2 months. Retinal degeneration is apparent as early as postnatal day 19 and progresses with age. The rd16 retina exhibits altered disitribution of Rpgr and phototransduction proteins within the photoreceptor cells. +Q7TSG1 CE120_MOUSE Centrosomal protein of 120 kDa (Cep120) (Coiled-coil domain-containing protein 100) 988 112,579 Alternative sequence (5); Beta strand (11); Chain (1); Coiled coil (1); Helix (3); Modified residue (2); Sequence conflict (1) FUNCTION: Plays a role in the microtubule-dependent coupling of the nucleus and the centrosome. Involved in the processes that regulate centrosome-mediated interkinetic nuclear migration (INM) of neural progenitors and for proper positioning of neurons during brain development. Also implicated in the migration and selfrenewal of neural progenitors. Required for centriole duplication and maturation during mitosis and subsequent ciliogenesis. Required for the recruitment of CEP295 to the proximal end of new-born centrioles at the centriolar microtubule wall during early S phase in a PLK4-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q8N960, ECO:0000269|PubMed:17920017, ECO:0000269|PubMed:20360068, ECO:0000269|PubMed:25251415}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:17920017}. Note=Regulates the localization of TACC3 to the centrosome in neural progenitors in vivo. SUBUNIT: Interacts with TACC2, TACC3, CCDC52, TALPID3. {ECO:0000269|PubMed:17920017, ECO:0000269|PubMed:20360068, ECO:0000269|PubMed:25251415}. TISSUE SPECIFICITY: Ubiquitous. Highly expressed in brain, lung and kidney and weakly expressed in heart, liver, small intestine and limb (at protein level). Expressed in brain. {ECO:0000269|PubMed:17920017}. +Q9CPY4 CDKA2_MOUSE Cyclin-dependent kinase 2-associated protein 2 (CDK2-associated protein 2) (DOC-1-related protein) (DOC-1R) 127 13,202 Chain (1); Region (1) FUNCTION: Plays a role in regulating the self-renewal of embryonic stem cells (ESCs) and in maintaining cell survival during terminal differentiation of ESCs (PubMed:22548356). Regulates microtubule organization of metaphase II oocytes (PubMed:12944431). Inhibits cell cycle G1/S phase transition by repressing CDK2 expression and activation; represses CDK2 activation by inhibiting its interaction with cyclin E and A (By similarity). {ECO:0000250|UniProtKB:O75956, ECO:0000269|PubMed:12944431, ECO:0000269|PubMed:22548356}. PTM: Phosphorylated by MAPK1 and CDK2. {ECO:0000269|PubMed:12944431}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12944431}. Nucleus {ECO:0000269|PubMed:12944431}. Note=Accumulates in immature oocytes in the nucleus. During the first meiotic division, accumulates in the cytoplasm and localizes in dots in the vicinity of the chromosomes in a region enriched in microtubules. {ECO:0000269|PubMed:12944431}. SUBUNIT: Interacts with MAPK1 (PubMed:12944431). Interacts with CDK2 and CDK2AP1 (By similarity). {ECO:0000250|UniProtKB:O75956, ECO:0000269|PubMed:12944431}. TISSUE SPECIFICITY: Oocytes (at protein level). {ECO:0000269|PubMed:12944431}. +Q8CIN6 CELF3_MOUSE CUGBP Elav-like family member 3 (CELF-3) (Bruno-like protein 1) (CUG-BP- and ETR-3-like factor 3) (ELAV-type RNA-binding protein 1) (ETR-1) (RNA-binding protein BRUNOL-1) (Trinucleotide repeat-containing gene 4 protein) 465 50,520 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (3) FUNCTION: RNA-binding protein involved in the regulation of pre-mRNA alternative splicing. Mediates exon inclusion and/or exclusion in pre-mRNA that are subject to tissue-specific and developmentally regulated alternative splicing. Specifically activates exon 5 inclusion of cardiac isoforms of TNNT2 during heart remodeling at the juvenile to adult transition. Activates the splicing of MAPT/Tau exon 10. Binds to muscle-specific splicing enhancer (MSE) intronic sites flanking the alternative exon 5 of TNNT2 pre-mRNA (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. +Q9R0M0 CELR2_MOUSE Cadherin EGF LAG seven-pass G-type receptor 2 (Flamingo homolog) 2920 317,593 Alternative sequence (1); Chain (1); Compositional bias (1); Disulfide bond (23); Domain (20); Glycosylation (17); Modified residue (1); Sequence conflict (9); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 2382 2402 Helical; Name=1. {ECO:0000255}.; TRANSMEM 2415 2434 Helical; Name=2. {ECO:0000255}.; TRANSMEM 2440 2460 Helical; Name=3. {ECO:0000255}.; TRANSMEM 2482 2502 Helical; Name=4. {ECO:0000255}.; TRANSMEM 2520 2540 Helical; Name=5. {ECO:0000255}.; TRANSMEM 2565 2585 Helical; Name=6. {ECO:0000255}.; TRANSMEM 2593 2613 Helical; Name=7. {ECO:0000255}. TOPO_DOM 32 2381 Extracellular. {ECO:0000255}.; TOPO_DOM 2403 2414 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 2435 2439 Extracellular. {ECO:0000255}.; TOPO_DOM 2461 2481 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 2503 2519 Extracellular. {ECO:0000255}.; TOPO_DOM 2541 2564 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 2586 2592 Extracellular. {ECO:0000255}.; TOPO_DOM 2614 2920 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor that may have an important role in cell/cell signaling during nervous system formation. PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed in the CNS and in the eye. {ECO:0000269|PubMed:10790539}. +Q8BGS7 CEPT1_MOUSE Choline/ethanolaminephosphotransferase 1 (mCEPT1) (EC 2.7.8.1) (EC 2.7.8.2) 416 46,434 Alternative sequence (1); Chain (1); Glycosylation (1); Modified residue (2); Transmembrane (8) TRANSMEM 87 107 Helical. {ECO:0000255}.; TRANSMEM 115 135 Helical. {ECO:0000255}.; TRANSMEM 186 206 Helical. {ECO:0000255}.; TRANSMEM 209 229 Helical. {ECO:0000255}.; TRANSMEM 239 259 Helical. {ECO:0000255}.; TRANSMEM 283 303 Helical. {ECO:0000255}.; TRANSMEM 317 337 Helical. {ECO:0000255}.; TRANSMEM 365 385 Helical. {ECO:0000255}. Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from ethanolamine: step 3/3. Phospholipid metabolism; phosphatidylcholine biosynthesis; phosphatidylcholine from phosphocholine: step 2/2. FUNCTION: Catalyzes both phosphatidylcholine and phosphatidylethanolamine biosynthesis from CDP-choline and CDP-ethanolamine, respectively. Involved in protein-dependent process of phospholipid transport to distribute phosphatidyl choline to the lumenal surface. Has a higher cholinephosphotransferase activity than ethanolaminephosphotransferase activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q8C4M7 CENPU_MOUSE Centromere protein U (CENP-U) (MLF1-interacting protein) 410 46,370 Alternative sequence (2); Chain (1); Coiled coil (1); Compositional bias (1); Modified residue (11); Motif (2); Sequence conflict (1) FUNCTION: Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. Plays an important role in the correct PLK1 localization to the mitotic kinetochores. A scaffold protein responsible for the initial recruitment and maintenance of the kinetochore PLK1 population until its degradation. Involved in transcriptional repression (By similarity). {ECO:0000250}. PTM: Phosphorylated by PLK1 at Thr-74, creating a self-tethering site that specifically interacts with the polo-box domain of PLK1. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Note=Localizes in the kinetochore domain of centromeres. Colocalizes with PLK1 at the interzone between the inner and the outer kinetochore plates (By similarity). {ECO:0000250}. SUBUNIT: Component of the CENPA-NAC complex, at least composed of CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and CENPU. The CENPA-NAC complex interacts with the CENPA-CAD complex, composed of CENPI, CENPK, CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS. Interacts with MLF1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Testis, spleen, heart, kidney, liver, lung, brain and CFU-E erythroid precursor cells. {ECO:0000269|PubMed:15116101}. +Q5HZK1 CEP44_MOUSE Centrosomal protein of 44 kDa (Cep44) 386 43,255 Chain (1); Coiled coil (2); Sequence conflict (3) SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. Midbody {ECO:0000250}. Note=Localizes to centrosomes, spindle poles, and weakly in midbody. {ECO:0000250}. +Q8K1K4 CENPI_MOUSE Centromere protein I (CENP-I) (FSH primary response protein 1) (Follicle-stimulating hormone primary response protein) 746 85,403 Chain (1); Sequence conflict (2) FUNCTION: Component of the CENPA-CAD (nucleosome distal) complex, a complex recruited to centromeres which is involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation. May be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex. Required for the localization of CENPF, MAD1L1 and MAD2 (MAD2L1 or MAD2L2) to kinetochores. Involved in the response of gonadal tissues to follicle-stimulating hormone (By similarity). {ECO:0000250}. PTM: Sumoylated. Sumoylated form can be polyubiquitinated by RNF4, leading to its degradation. Desumoylation by SENP6 prevents its degradation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, centromere {ECO:0000250}. Note=Localizes exclusively in the centromeres. The CENPA-CAD complex is probably recruited on centromeres by the CENPA-NAC complex (By similarity). {ECO:0000250}. SUBUNIT: Component of the CENPA-CAD complex, composed of CENPI, CENPK, CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS. The CENPA-CAD complex interacts with the CENPA-NAC complex, at least composed of CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and CENPU. Interacts with SENP6 (By similarity). {ECO:0000250}. +Q8CEE0 CEP57_MOUSE Centrosomal protein of 57 kDa (Cep57) (Testis-specific protein 57) (Translokin) 500 56,909 Alternative sequence (2); Chain (1); Coiled coil (2); Compositional bias (1); Erroneous initiation (2); Modified residue (1); Region (2); Sequence conflict (9) FUNCTION: Centrosomal protein which may be required for microtubule attachment to centrosomes. May act by forming ring-like structures around microtubules. Mediates nuclear translocation and mitogenic activity of the internalized growth factor FGF2. {ECO:0000269|PubMed:12717444, ECO:0000269|PubMed:18294141}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:12954732, ECO:0000269|PubMed:18294141}. SUBUNIT: Interacts with FGF2 and RAP80. Does not interact with FGF1 or FGF2 isoform 24 kDa (By similarity). Homodimer and homooligomer. Interacts with microtubules. {ECO:0000250, ECO:0000269|PubMed:12954732, ECO:0000269|PubMed:18294141}. DOMAIN: The C-terminal region mediates the interaction with microtubules and is able to nucleate and bundles microtubules in vitro. {ECO:0000269|PubMed:18294141}.; DOMAIN: The centrosome localization domain (CLD) region mediates the localization to centrosomes and homooligomerization. {ECO:0000269|PubMed:18294141}. TISSUE SPECIFICITY: Ubiquitous (at protein level). Expressed in testis, predominantly in round spermatids. Low expression is detected in other tissues. {ECO:0000269|PubMed:12954732, ECO:0000269|PubMed:18294141}. +Q9R1K9 CETN2_MOUSE Centrin-2 (Caltractin isoform 1) 172 19,797 Calcium binding (2); Chain (1); Cross-link (1); Domain (4); Erroneous gene model prediction (1); Initiator methionine (1); Modified residue (3); Region (1); Sequence conflict (2) FUNCTION: Plays a fundamental role in microtubule organizing center structure and function. Required for centriole duplication and correct spindle formation. Has a role in regulating cytokinesis and genome stability via cooperation with CALM1 and CCP110 (By similarity). {ECO:0000250}.; FUNCTION: Involved in global genome nucleotide excision repair (GG-NER) by acting as component of the XPC complex. Cooperatively with Rad23b appears to stabilize Xpc. In vitro, stimulates DNA binding of the Xpc:Rad23b dimer (By similarity). {ECO:0000250}.; FUNCTION: The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, Xpa, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair (By similarity). {ECO:0000250}.; FUNCTION: Component of the TREX-2 complex (transcription and export complex 2), composed of at least ENY2, GANP, PCID2, SEM1, and either centrin CETN2 or CETN3. The TREX-2 complex functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket). TREX-2 participates in mRNA export and accurate chromatin positioning in the nucleus by tethering genes to the nuclear periphery. {ECO:0000250|UniProtKB:P41208}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:11250075}. Nucleus {ECO:0000250}. Note=Centrosome of S-phase, interphase and mitotic cells. SUBUNIT: Monomer. Homooligomer. Interacts with CCP110, SFI1. Component of the XPC complex composed of XPC, RAD23B and CETN2 (By similarity). Component of the TREX-2 complex (transcription and export complex 2), composed of at least ENY2, GANP, PCID2, SEM1, and either centrin CETN2 or CETN3 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P41208}. TISSUE SPECIFICITY: Ubiquitously expressed in all adult tissues tested, with strongest expression in brain, spleen, kidney, small intestine and ovary. Also expressed in the NIH 3T3 fibroblast cell line and peripheral blood lymphocytes. {ECO:0000269|PubMed:11250075}. +Q8K4Q7 CERK1_MOUSE Ceramide kinase (mCERK) (EC 2.7.1.138) (Acylsphingosine kinase) 531 59,843 Active site (1); Binding site (3); Chain (1); Domain (1); Modified residue (2); Nucleotide binding (4); Region (2); Sequence conflict (2) FUNCTION: Catalyzes specifically the phosphorylation of ceramide to form ceramide 1-phosphate. Acts efficiently on natural and analog ceramides (C6, C8, C16 ceramides, and C8-dihydroceramide), to a lesser extent on C2-ceramide and C6-dihydroceramide, but not on other lipids, such as various sphingosines (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. TISSUE SPECIFICITY: High level expression in heart, brain and testis; low expression in spleen, liver and lung; not detected in skeletal muscle. +Q9D3R3 CEP72_MOUSE Centrosomal protein of 72 kDa (Cep72) 646 72,433 Alternative sequence (2); Chain (1); Coiled coil (1); Domain (1); Erroneous initiation (1); Modified residue (4); Repeat (3); Sequence caution (1); Sequence conflict (2) FUNCTION: Involved in the recruitment of key centrosomal proteins to the centrosome. Provides centrosomal microtubule-nucleation activity on the gamma-tubulin ring complexes (gamma-TuRCs) and has critical roles in forming a focused bipolar spindle, which is needed for proper tension generation between sister chromatids. Required for localization of KIZ, AKAP9 and gamma-tubulin ring complexes (gamma-TuRCs) (By similarity). Involved in centriole duplication. Required for CDK5RAP22, CEP152, WDR62 and CEP63 centrosomal localization and promotes the centrosomal localization of CDK2 (By similarity). {ECO:0000250|UniProtKB:Q9P209}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9P209}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000250|UniProtKB:Q9P209}. Note=Localizes to the centrosome and centrosome-surrounding particles throughout the cell cycle. These particles disappear after microtubules are depolymerized using nocodazole, suggesting that CEP72-associating particles localize in a microtubule-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q9P209}. SUBUNIT: Interacts with KIZ, PCM1 and CDK5RAP2. {ECO:0000250|UniProtKB:Q9P209}. +Q0VFX2 CF157_MOUSE Cilia- and flagella-associated protein 157 523 61,048 Chain (1); Coiled coil (3); Frameshift (1); Modified residue (1); Sequence conflict (1) FUNCTION: Specifically required during spermatogenesis for flagellum morphogenesis and sperm motility (PubMed:27965440). May be required to suppress the formation of supernumerary axonemes and ensure a correct ultrastructure (PubMed:27965440). {ECO:0000269|PubMed:27965440}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:27965440}. SUBUNIT: Interacts with TUBB and TUBA4A (PubMed:27965440). Interacts with CEP350 (PubMed:27965440). {ECO:0000269|PubMed:27965440}. TISSUE SPECIFICITY: Specifically expressed in tissues containing motile cilia. {ECO:0000269|PubMed:27965440}. +Q8C6E0 CFA36_MOUSE Cilia- and flagella-associated protein 36 (Coiled-coil domain-containing protein 104) 343 39,600 Beta strand (1); Chain (1); Coiled coil (1); Helix (8); Modified residue (3); Sequence conflict (1) FUNCTION: May act as an effector for ARL3. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96G28}. Cytoplasm {ECO:0000250|UniProtKB:Q96G28}. Cell projection, cilium, flagellum {ECO:0000305}. SUBUNIT: Interacts with ARL3. {ECO:0000250}. +P97766 CFC1_MOUSE Cryptic protein 202 21,792 Chain (1); Disulfide bond (3); Domain (1); Glycosylation (1); Lipidation (1); Propeptide (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Nodal coreceptor involved in the correct establishment of the left-right axis. May play a role in mesoderm and/or neural patterning during gastrulation. {ECO:0000269|PubMed:10574770, ECO:0000269|PubMed:9053319}. PTM: N-glycosylated. {ECO:0000269|PubMed:9053319}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. Secreted {ECO:0000250}. TISSUE SPECIFICITY: No expressed in adult tissues. {ECO:0000269|PubMed:9053319}. +Q9D439 CFA53_MOUSE Cilia- and flagella-associated protein 53 (Coiled-coil domain-containing protein 11) 514 61,911 Alternative sequence (1); Chain (1); Coiled coil (2); Erroneous initiation (1) FUNCTION: May play a role in the beating of primary cilia and thereby be involved in the establishment of organ laterality during embryogenesis. {ECO:0000250|UniProtKB:Q96M91}. SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000250|UniProtKB:Q96M91}. +Q8BTU1 CFA20_MOUSE Cilia- and flagella-associated protein 20 (Gene trap locus 3 protein) 193 22,748 Alternative sequence (1); Chain (1); Sequence conflict (1) FUNCTION: Cilium- and flagellum-specific protein that plays a role in axonemal structure organization and motility. Involved in the regulation of the size and morphology of cilia. Required for axonemal microtubules polyglutamylation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250}. Cell projection, cilium {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed, with highest levels in testis and lowest in muscle. {ECO:0000269|PubMed:8688464}. +P03953 CFAD_MOUSE Complement factor D (EC 3.4.21.46) (28 kDa adipocyte protein) (Adipsin) (C3 convertase activator) (Properdin factor D) 259 28,057 Active site (3); Alternative sequence (1); Beta strand (14); Chain (1); Disulfide bond (4); Domain (1); Glycosylation (5); Helix (4); Propeptide (1); Signal peptide (1); Turn (1) FUNCTION: Factor D cleaves factor B when the latter is complexed with factor C3b, activating the C3bbb complex, which then becomes the C3 convertase of the alternate pathway. Its function is homologous to that of C1s in the classical pathway. PTM: N-glycosylated. {ECO:0000269|PubMed:16944957, ECO:0000269|PubMed:17330941}. SUBCELLULAR LOCATION: Secreted. +Q8BH53 CFA69_MOUSE Cilia- and flagella-associated protein 69 942 106,233 Alternative sequence (6); Chain (1); Sequence conflict (1) FUNCTION: Cilium- and flagellum-associated protein (PubMed:28495971, PubMed:29606301). In the olfactory epithelium, regulates the speed of activation and termination of the odor response and thus contributes to the robustness of olfactory transduction pathways (PubMed:28495971). Required for sperm flagellum assembly and stability (PubMed:29606301). {ECO:0000269|PubMed:28495971, ECO:0000269|PubMed:29606301}. SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000269|PubMed:28495971}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:29606301}. Note=Localizes to the midpiece of the sperm flagellum. {ECO:0000269|PubMed:29606301}. TISSUE SPECIFICITY: Expressed in ciliated olfactory sensory neurons (at protein level) (PubMed:28495971). Expressed in testis, specifically in sperm (at protein level) (PubMed:29606301). {ECO:0000269|PubMed:28495971, ECO:0000269|PubMed:29606301}. +Q8C6L5 CGAS_MOUSE Cyclic GMP-AMP synthase (cGAMP synthase) (cGAS) (m-cGAS) (EC 2.7.7.86) (2'3'-cGAMP synthase) (Mab-21 domain-containing protein 1) 507 58,194 Beta strand (14); Binding site (5); Chain (1); Helix (16); Metal binding (7); Modified residue (4); Motif (1); Mutagenesis (10); Nucleotide binding (2); Region (4); Sequence conflict (2); Turn (5) FUNCTION: Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (cGAMP) from ATP and GTP and plays a key role in innate immunity (PubMed:23258413, PubMed:23647843, PubMed:23722158, PubMed:26829768, PubMed:28214358). Catalysis involves both the formation of a 2',5' phosphodiester linkage at the GpA step and the formation of a 3',5' phosphodiester linkage at the ApG step, producing c[G(2',5')pA(3',5')p] (PubMed:23258413, PubMed:23647843, PubMed:23722158, PubMed:26829768, PubMed:28214358). Acts as a key cytosolic DNA sensor, the presence of double-stranded DNA (dsDNA) in the cytoplasm being a danger signal that triggers the immune responses (PubMed:23722158, PubMed:28363908, PubMed:28314590). Binds cytosolic DNA directly, leading to activation and synthesis of cGAMP, a second messenger that binds to and activates TMEM173/STING, thereby triggering type-I interferon production (PubMed:23722158, PubMed:28363908, PubMed:28314590). Preferentially binds long dsDNA (around 45 bp) and forms ladder-like networks that function cooperatively to stabilize individual cGAS-dsDNA complexes (PubMed:28902841). Has antiviral activity by sensing the presence of dsDNA from DNA viruses in the cytoplasm (PubMed:23258413, PubMed:23647843, PubMed:23722158). Also acts as an innate immune sensor of infection by retroviruses by detecting the presence of reverse-transcribed DNA in the cytosol (PubMed:23929945). Detection of retroviral reverse-transcribed DNA in the cytosol may be indirect and be mediated via interaction with PQBP1, which directly binds reverse-transcribed retroviral DNA (By similarity). Also detects the presence of DNA from bacteria (By similarity). cGAMP can be transferred from producing cells to neighboring cells through gap junctions, leading to promote TMEM173/STING activation and convey immune response to connecting cells (PubMed:24077100). cGAMP can also be transferred between cells by virtue of packaging within viral particles contributing to IFN-induction in newly infected cells in a cGAS-independent but TMEM173/STING-dependent manner (PubMed:26229117). In addition to antiviral activity, also involved in the response to cellular stresses, such as senescence, DNA damage or genome instability (PubMed:28738408, PubMed:28759028). Acts as a regulator of cellular senescence by binding to cytosolic chromatin fragments that are present in senescent cells, leading to trigger type-I interferon production via TMEM173/STING and promote cellular senescence (PubMed:28759028). Also involved in the inflammatory response to genome instability and double-stranded DNA breaks: acts by localizing to micronuclei arising from genome instability (PubMed:28738408). Micronuclei, which as frequently found in cancer cells, consist of chromatin surrounded by its own nuclear membrane: following breakdown of the micronuclear envelope, a process associated with chromothripsis, CGAS binds self-DNA exposed to the cytosol, leading to cGAMP synthesis and subsequent activation of TMEM173/STING and type-I interferon production (PubMed:28738408). Acts as a suppressor of DNA repair in response to DNA damage: translocates to the nucleus following dephosphorylation at Tyr-201 and inhibits homologous recombination repair by interacting with PARP1, the CGAS-PARP1 interaction leading to impede the formation of the PARP1-TIMELESS complex (PubMed:30356214). {ECO:0000250|UniProtKB:Q8N884, ECO:0000269|PubMed:23258413, ECO:0000269|PubMed:23647843, ECO:0000269|PubMed:23722158, ECO:0000269|PubMed:23929945, ECO:0000269|PubMed:24077100, ECO:0000269|PubMed:26229117, ECO:0000269|PubMed:26829768, ECO:0000269|PubMed:28214358, ECO:0000269|PubMed:28314590, ECO:0000269|PubMed:28363908, ECO:0000269|PubMed:28738408, ECO:0000269|PubMed:28759028, ECO:0000269|PubMed:28902841, ECO:0000269|PubMed:30356214}. PTM: Polyglutamylated by TTLL6 at Glu-272, leading to impair DNA-binding activity. Monoglutamylated at Glu-302 by TTLL4, leading to impair the nucleotidyltransferase activity. Deglutamylated by AGBL5/CCP5 and AGBL6/CCP6. {ECO:0000269|PubMed:26829768}.; PTM: Cleaved by CASP1 upon DNA virus infection; the cleavage impairs cGAMP production (PubMed:28314590). Also cleaved by the pyroptotic CASP4 during non-canonical inflammasome activation; does not cut at the same sites than CASP1 (PubMed:28314590). {ECO:0000269|PubMed:28314590}.; PTM: Phosphorylation at Tyr-201 by BLK promotes cytosolic retention. Translocates into the nucleus following dephosphorylation at Tyr-201. {ECO:0000250|UniProtKB:Q8N884}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:23258413}. Nucleus {ECO:0000250|UniProtKB:Q8N884}. Note=Mainly localizes in the cytosol. Upon transfection with dsDNA forms punctate structures that co-localize with DNA and Beclin-1 (BECN1) (By similarity). Phosphorylation at Tyr-201 promotes cytosolic retention; translocates into the nucleus following dephosphorylation (By similarity). {ECO:0000250|UniProtKB:Q8N884}. SUBUNIT: Monomer in the absence of DNA (PubMed:28214358). Homodimer in presence of dsDNA: forms a 2:2 dimer with two enzymes binding to two DNA molecules (PubMed:28902841). Interacts with PQBP1 (via WW domain) (By similarity). Interacts with TRIM14; this interaction stabilizes CGAS and promotes type I interferon production (By similarity). Interacts with ZCCHC3; promoting sensing of dsDNA by CGAS (By similarity). Interacts with PARP1; interaction takes place in the nucleus and prevents the formation of the PARP1-TIMELESS complex (By similarity). {ECO:0000250|UniProtKB:Q8N884, ECO:0000269|PubMed:28214358, ECO:0000269|PubMed:28902841}. DOMAIN: The N-terminal part (1-146) binds unspecifically dsDNA and expand the binding and moving range of CGAS on dsDNA. Enhances the enzyme activity and activation of innate immune signaling upon cytosolic recognition of dsDNA (PubMed:28363908, PubMed:28214358, PubMed:28314590). When the N-terminal part (1-146) is missing the protein bound to dsDNA homodimerizes (PubMed:28214358). {ECO:0000269|PubMed:28214358, ECO:0000269|PubMed:28314590, ECO:0000269|PubMed:28363908}. +Q99LU8 CF062_MOUSE Uncharacterized protein C6orf62 homolog 229 27,083 Chain (1) +Q3UTZ3 CG043_MOUSE Uncharacterized protein C7orf43 homolog 580 62,780 Chain (1); Compositional bias (1); Erroneous initiation (1); Modified residue (4) +Q99LU0 CH1B1_MOUSE Charged multivesicular body protein 1b-1 (Chromatin-modifying protein 1b-1) (CHMP1b-1) 199 22,124 Chain (1); Coiled coil (2); Motif (1); Region (5); Sequence conflict (1) FUNCTION: Probable peripherally associated component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis. ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. Involved in cytokinesis. Involved in recruiting VPS4A and/or VPS4B and SPAST to the midbody of dividing cells (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Endosome {ECO:0000250}. Late endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Localizes to the midbody of dividing cells, colocalizing with CEP55 and CHMP5. Localized at the periphery of the Fleming body (By similarity). {ECO:0000250}. SUBUNIT: Probable peripherally associated component of the endosomal sorting required for transport complex III (ESCRT-III). ESCRT-III components are thought to multimerize to form a flat lattice on the perimeter membrane of the endosome. Several assembly forms of ESCRT-III may exist that interact and act sequentially. Interacts with CHMP1A. Interacts with VTA1; the interaction probably involves the open conformation of CHMP1B. Interacts with CHMP2A. Interacts with VPS4A; the interaction is direct. Interacts with VPS4B; the interaction is direct. Interacts with SPAST (via MIT domain); the interaction is direct. Interacts with IST1. Interacts with MITD1. Interacts with STAMBP (By similarity). {ECO:0000250}. +Q9CQD4 CH1B2_MOUSE Charged multivesicular body protein 1b-2 (Chromatin-modifying protein 1b-2) (CHMP1b-2) 199 22,161 Chain (1); Coiled coil (2); Motif (1); Region (5) FUNCTION: Probable peripherally associated component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis. ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. Involved in cytokinesis. Involved in recruiting VPS4A and/or VPS4B and SPAST to the midbody of dividing cells (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Endosome {ECO:0000250}. Late endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Localizes to the midbody of dividing cells, colocalizing with CEP55 and CHMP5. Localized at the periphery of the Fleming body (By similarity). {ECO:0000250}. SUBUNIT: Probable peripherally associated component of the endosomal sorting required for transport complex III (ESCRT-III). ESCRT-III components are thought to multimerize to form a flat lattice on the perimeter membrane of the endosome. Several assembly forms of ESCRT-III may exist that interact and act sequentially. Interacts with CHMP1A. Interacts with VTA1; the interaction probably involves the open conformation of CHMP1B. Interacts with CHMP2A. Interacts with VPS4A; the interaction is direct. Interacts with VPS4B; the interaction is direct. Interacts with SPAST (via MIT domain); the interaction is direct. Interacts with IST1. Interacts with MITD1. Interacts with STAMBP (By similarity). {ECO:0000250}. +Q61362 CH3L1_MOUSE Chitinase-3-like protein 1 (BRP39 protein) (Breast regression protein 39) (Cartilage glycoprotein 39) (CGP-39) (GP-39) 389 43,893 Alternative sequence (2); Beta strand (13); Binding site (2); Chain (1); Disulfide bond (2); Erroneous initiation (4); Glycosylation (1); Helix (18); Mutagenesis (1); Region (4); Sequence conflict (4); Signal peptide (1); Turn (3) FUNCTION: Carbohydrate-binding lectin with a preference for chitin. Has no chitinase activity. May play a role in tissue remodeling and in the capacity of cells to respond to and cope with changes in their environment. Plays a role in T-helper cell type 2 (Th2) inflammatory response and IL-13-induced inflammation, regulating allergen sensitization, inflammatory cell apoptosis, dendritic cell accumulation and M2 macrophage differentiation. Facilitates invasion of pathogenic enteric bacteria into colonic mucosa and lymphoid organs. Mediates activation of AKT1 signaling pathway and subsequent IL8 production in colonic epithelial cells. Regulates antibacterial responses in lung by contributing to macrophage bacterial killing, controlling bacterial dissemination and augmenting host tolerance. Also regulates hyperoxia-induced injury, inflammation and epithelial apoptosis in lung. {ECO:0000269|PubMed:16472595, ECO:0000269|PubMed:19041398, ECO:0000269|PubMed:19414556, ECO:0000269|PubMed:20558631, ECO:0000269|PubMed:21546314, ECO:0000269|PubMed:22817986}. SUBCELLULAR LOCATION: Secreted, extracellular space. Cytoplasm. Endoplasmic reticulum. Note=Detected in bronchoalveolar lavage (BAL) fluids. Localizes mainly to endoplasmic reticulum when overexpressed in cells, with some protein also detected throughout the cytoplasm. SUBUNIT: Monomer. {ECO:0000250}. TISSUE SPECIFICITY: Detected in lung in pulmonary macrophages and alveolar type 2 cells and in bronchoalveolar lavage (BAL) fluids. Expressed in mammary tumor cells (at protein level). Expressed in lung. Not detected in non-inflammatory colon. {ECO:0000269|PubMed:16472595, ECO:0000269|PubMed:19414556, ECO:0000269|PubMed:20558631, ECO:0000269|PubMed:21866546}. +Q6VY05 DND1_MOUSE Dead end protein homolog 1 (RNA-binding motif, single-stranded-interacting protein 4) 352 39,076 Alternative sequence (1); Chain (1); Domain (2); Modified residue (1) FUNCTION: RNA-binding factor that positively regulates gene expression by prohibiting miRNA-mediated gene suppression (By similarity). Relieves miRNA repression in germline cells (By similarity). Prohibits the function of several miRNAs by blocking the accessibility of target mRNAs (By similarity). Sequence-specific RNA-binding factor that binds specifically to U-rich regions (URRs) in the 3' untranslated region (3'-UTR) of several mRNAs (By similarity). Does not bind to miRNAs (By similarity). Isoform 1 may play a role during primordial germ cell (PGC) survival. However, does not seem to be essential for PGC migration. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Perinuclear germ granules, also called germ plasm or chromatoid body (By similarity). Colocalizes in perinuclear sites with APOBEC3. {ECO:0000250}. SUBUNIT: Interacts with APOBEC3. {ECO:0000269|PubMed:18509452}. TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in testis. Isoform 1 is expressed continuously in post natal (PN) testis although levels are low between PN1 to PN6. Isoform 2 is expressed from PN 20 onwards. Isoform 2 is strongly expressed in meiotic and in post-meiotic germ cells of the testis with highest expression at the elongated spermatid stage (at protein level). Expressed in testis and heart. Expressed in germ cells and genital ridges. Not detected in testicular tumors. {ECO:0000269|PubMed:15902260, ECO:0000269|PubMed:17291453}. DISEASE: Note=Defects in Dnd1 are the cause of the Ter mutation phenotype. Ter mice are characterized by primordial germ cell loss and susceptibility to spontaneous testicular germ cell tumors (TGCT). They are sterile, but viable. Isoform 1 defects may be the cause of tumor development. {ECO:0000269|PubMed:15902260}. +Q8JZM4 DNER_MOUSE Delta and Notch-like epidermal growth factor-related receptor (Brain EGF repeat-containing transmembrane protein) 737 78,747 Chain (1); Disulfide bond (29); Domain (10); Frameshift (2); Glycosylation (2); Modified residue (5); Mutagenesis (1); Region (2); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 641 661 Helical. {ECO:0000255}. TOPO_DOM 26 640 Extracellular. {ECO:0000255}.; TOPO_DOM 662 737 Cytoplasmic. {ECO:0000255}. FUNCTION: Mediates neuron-glia interaction during astrocytogenesis. May promote differentiation of Bergmann glia during cerebellar development by activating DELTEX-dependent NOTCH1 signaling. {ECO:0000269|PubMed:15965470, ECO:0000269|PubMed:16298139}. PTM: N-glycosylated. {ECO:0000269|PubMed:11997712}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11950833, ECO:0000269|PubMed:11997712}; Single-pass type I membrane protein {ECO:0000269|PubMed:11950833, ECO:0000269|PubMed:11997712}. Note=Present on the membrane of dendrites and cell bodies but excluded from axonal membrane. Also found in early endosomes in the somatodendritic region. SUBUNIT: Interacts with AP1G1. Interacts with NOTCH1. {ECO:0000269|PubMed:11950833, ECO:0000269|PubMed:15965470}. TISSUE SPECIFICITY: Specifically expressed in brain neurons (at protein level). {ECO:0000269|PubMed:11950833, ECO:0000269|PubMed:11997712}. +Q9CQ94 DNJ5B_MOUSE DnaJ homolog subfamily C member 5B (Cysteine string protein beta) (CSP-beta) 199 22,662 Chain (1); Compositional bias (2); Domain (1); Modified residue (2); Sequence conflict (1) PTM: Palmitoylated. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. SUBUNIT: Interacts with the chaperone complex consisting of HSC70 and SGTA. {ECO:0000269|PubMed:17034881}. +P63037 DNJA1_MOUSE DnaJ homolog subfamily A member 1 (DnaJ protein homolog 2) (Heat shock 40 kDa protein 4) (Heat shock protein J2) (HSJ-2) 397 44,868 Chain (1); Compositional bias (1); Domain (1); Lipidation (1); Metal binding (8); Modified residue (5); Propeptide (1); Repeat (4); Zinc finger (1) FUNCTION: Co-chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro). Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV (By similarity). Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. {ECO:0000250, ECO:0000269|PubMed:14752510}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Cytoplasm {ECO:0000250}. Microsome {ECO:0000250}. Mitochondrion {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Primarily cytoplasmic and associated with microsomes. A minor proportion is associated with nuclei and mitochondria (By similarity). {ECO:0000250}. SUBUNIT: Identified in a complex with HSPA1B and BAX (PubMed:14752510). Interacts with RNF207 (By similarity). {ECO:0000250|UniProtKB:P31689, ECO:0000269|PubMed:14752510}. +P60904 DNJC5_MOUSE DnaJ homolog subfamily C member 5 (Cysteine string protein) (CSP) 198 22,101 Chain (1); Compositional bias (1); Domain (1); Helix (6); Modified residue (7); Mutagenesis (7); Turn (1) FUNCTION: Acts as a co-chaperone for the SNARE protein SNAP-25 (PubMed:22187053). Involved in the calcium-mediated control of a late stage of exocytosis (PubMed:20847230). Acts as a general chaperone in regulated exocytosis (By similarity). May have an important role in presynaptic function (By similarity). May be involved in calcium-dependent neurotransmitter release at nerve endings (By similarity). {ECO:0000250|UniProtKB:Q29455, ECO:0000269|PubMed:20847230, ECO:0000269|PubMed:22187053}. PTM: Fatty acylated (PubMed:17034881). Heavily palmitoylated in the cysteine string motif (PubMed:17034881). Palmitoylation is not required for membrane association (PubMed:17034881). {ECO:0000269|PubMed:17034881}.; PTM: Formation of the chaperone complex DNAJC5/HSC70 is not regulated by phosphorylation (PubMed:20847230). Ser-10 phosphorylation induces an order-to-disorder transition triggering the interaction with Lys-58 (By similarity). This conformational switch modulates DNAJC5's cellular functions by reducing binding to syntaxin and synaptogamin without altering HSC70 interactions (By similarity). {ECO:0000250|UniProtKB:Q9H3Z4, ECO:0000269|PubMed:20847230}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:17034881}; Lipid-anchor {ECO:0000269|PubMed:17034881}. Melanosome {ECO:0000250|UniProtKB:Q9H3Z4}. Cell membrane {ECO:0000250|UniProtKB:Q9H3Z4}. Note=Colocalizes with insulin granules, when overexpressed in a islet cell line. {ECO:0000269|PubMed:17034881}. SUBUNIT: Homodimer (Probable). Interacts with the chaperone complex consisting of HSC70 and SGTA (PubMed:17034881, PubMed:20847230). Interacts with ZDHHC13 (via ANK repeats) (PubMed:25253725, PubMed:26198635). Interacts with ZDHHC17 (via ANK repeats) (PubMed:25253725, PubMed:26198635). Interacts with SYT1, SYT5 and SYT7, and with SYT9, forming a complex with SNAP25 (PubMed:20847230). The interaction with SYT9 is stimulated tenfold in presence of calcium (PubMed:20847230). {ECO:0000269|PubMed:17034881, ECO:0000269|PubMed:20847230, ECO:0000269|PubMed:25253725, ECO:0000269|PubMed:26198635, ECO:0000305}. +Q9QYI3 DNJC7_MOUSE DnaJ homolog subfamily C member 7 (Cytoplasmic CAR retention protein) (CCRP) (MDj11) (Tetratricopeptide repeat protein 2) (TPR repeat protein 2) 494 56,476 Chain (1); Domain (1); Initiator methionine (1); Modified residue (2); Repeat (8); Sequence conflict (7) FUNCTION: Acts as co-chaperone regulating the molecular chaperones HSP70 and HSP90 in folding of steroid receptors, such as the glucocorticoid receptor and the progesterone receptor. Proposed to act as a recycling chaperone by facilitating the return of chaperone substrates to early stages of chaperoning if further folding is required. In vitro, induces ATP-independent dissociation of HSP90 but not of HSP70 from the chaperone-substrate complexes (By similarity). Recruits NR1I3 to the cytoplasm. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14573755}. Nucleus {ECO:0000250|UniProtKB:Q99615}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:14573755}. Note=Colocalizes with NR1I3 at microtubules. {ECO:0000269|PubMed:14573755}. SUBUNIT: Associates with complexes containing chaperones HSP70 and HSP90. Interacts with the GAP domain of NF1. Interacts with HSP90AA1. Interacts with HSPA1A/B; the interaction is enhanced by ATP. Interacts with HSP90AB1. Interacts with PGR. Interacts with RAD9A; the interaction is interrupted by UV and heat shock treatments. Interacts with HUS1 and RAD1 (By similarity). Interacts with NR1I3; this complex may also include HSP90 Interacts with HSPA8 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed with high levels in liver, skeletal muscle, kidney and testis. {ECO:0000269|PubMed:14573755}. +Q6NZB0 DNJC8_MOUSE DnaJ homolog subfamily C member 8 253 29,813 Chain (1); Domain (1); Frameshift (1); Initiator methionine (1); Modified residue (4); Motif (2); Region (1); Sequence conflict (1) FUNCTION: Suppresses polyglutamine (polyQ) aggregation of ATXN3 in neuronal cells. {ECO:0000250|UniProtKB:O75937}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O75937}. SUBUNIT: Interacts with SRPK1. Interacts with HSP70 (HSPA1A or HSPA1B). {ECO:0000250|UniProtKB:O75937}. +Q91WN1 DNJC9_MOUSE DnaJ homolog subfamily C member 9 259 30,059 Chain (1); Domain (1); Modified residue (1) FUNCTION: May play a role as co-chaperone of the Hsp70 family proteins HSPA1A, HSPA1B and HSPA8. {ECO:0000250|UniProtKB:Q8WXX5}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8WXX5}. Cytoplasm {ECO:0000250|UniProtKB:Q8WXX5}. Cell membrane {ECO:0000250|UniProtKB:Q8WXX5}. Note=Predominantly nuclear. Translocates to the cytoplasm and membrane after heat shock. {ECO:0000250|UniProtKB:Q8WXX5}. SUBUNIT: Interacts (via J domain) with HSPA1A, HSPA1B and HSPA8. {ECO:0000250|UniProtKB:Q8WXX5}. +P37913 DNLI1_MOUSE DNA ligase 1 (EC 6.5.1.1) (DNA ligase I) (Polydeoxyribonucleotide synthase [ATP] 1) 916 102,290 Active site (1); Binding site (6); Chain (1); Metal binding (2); Modified residue (15); Region (2); Site (4) FUNCTION: DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with PCNA. {ECO:0000250|UniProtKB:P12004}. +P97386 DNLI3_MOUSE DNA ligase 3 (EC 6.5.1.1) (DNA ligase III) (Polydeoxyribonucleotide synthase [ATP] 3) 1015 113,072 Active site (1); Alternative sequence (1); Binding site (6); Chain (1); Domain (1); Metal binding (2); Modified residue (5); Region (4); Sequence conflict (8); Zinc finger (1) FUNCTION: The alpha isoform interacts with DNA-repair protein XRCC1 and can correct defective DNA strand-break repair and sister chromatid exchange following treatment with ionizing radiation and alkylating agents. The beta isoform does not interact with XRCC1 and may be specifically involved in the completion of homologous recombination events that occur during meiotic prophase. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts (via BRCT domain) with the nuclear DNA-repair protein XRCC1. {ECO:0000250|UniProtKB:P49916}. DOMAIN: The PARP-type zinc finger is required for DNA ligase activity. {ECO:0000250|UniProtKB:P49916}. TISSUE SPECIFICITY: The alpha isoform is expressed in all tissues, while the beta isoform is expressed only in the testis. +Q8BTF7 DNLI4_MOUSE DNA ligase 4 (EC 6.5.1.1) (DNA ligase IV) (Polydeoxyribonucleotide synthase [ATP] 4) 911 104,120 Active site (1); Binding site (6); Chain (1); Domain (2); Metal binding (2); Sequence conflict (2) FUNCTION: Efficiently joins single-strand breaks in a double-stranded polydeoxynucleotide in an ATP-dependent reaction. Involved in DNA nonhomologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. The LIG4-XRCC4 complex is responsible for the NHEJ ligation step, and XRCC4 enhances the joining activity of LIG4. Binding of the LIG4-XRCC4 complex to DNA ends is dependent on the assembly of the DNA-dependent protein kinase complex DNA-PK to these DNA ends. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with XRCC4. The LIG4-XRCC4 complex has probably a 1:2 stoichiometry. The LIG4-XRCC4 complex associates in a DNA-dependent manner with the DNA-PK complex composed of PRKDC, XRCC6/Ku70 and XRCC5/Ku86 to form the core non-homologous end joining (NHEJ) complex. Additional components of the NHEJ complex include NHEJ1/XLF and PAXX. Interacts with APLF. {ECO:0000250|UniProtKB:P49917}. +Q8CJ61 CKLF4_MOUSE CKLF-like MARVEL transmembrane domain-containing protein 4 (Chemokine-like factor superfamily member 4) 208 22,921 Chain (1); Domain (1); Modified residue (1); Transmembrane (4) TRANSMEM 59 79 Helical. {ECO:0000255}.; TRANSMEM 85 105 Helical. {ECO:0000255}.; TRANSMEM 123 143 Helical. {ECO:0000255}.; TRANSMEM 151 171 Helical. {ECO:0000255}. FUNCTION: Acts as a backup for CMTM6 to regulate plasma membrane expression of PD-L1/CD274, an immune inhibitory ligand critical for immune tolerance to self and antitumor immunity. May protect PD-L1/CD274 from being polyubiquitinated and targeted for degradation. {ECO:0000250|UniProtKB:Q8IZR5}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Interacts with PD1L1 and CMTM6. {ECO:0000250|UniProtKB:Q8IZR5}. +P56390 CKS2_MOUSE Cyclin-dependent kinases regulatory subunit 2 (CKS-2) 79 9,874 Chain (1); Modified residue (1) FUNCTION: Binds to the catalytic subunit of the cyclin dependent kinases and is essential for their biological function. SUBUNIT: Forms a homohexamer that can probably bind six kinase subunits. +B2RW38 CFA58_MOUSE Cilia- and flagella-associated protein 58 873 103,524 Chain (1); Coiled coil (2) SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000250|UniProtKB:A8HUA1}. +Q3TTJ4 CH048_MOUSE Uncharacterized protein C8orf48 homolog 293 33,319 Chain (1) +Q0VG62 CH059_MOUSE Uncharacterized protein C8orf59 homolog 139 15,810 Chain (1); Modified residue (3) +Q80ZQ3 CH074_MOUSE Uncharacterized protein C8orf74 homolog 298 33,958 Chain (1); Frameshift (2) +Q9D2X8 CH076_MOUSE Uncharacterized protein C8orf76 homolog 372 41,643 Chain (1) +Q8R1U2 CGRE1_MOUSE Cell growth regulator with EF hand domain protein 1 (Cell growth regulatory gene 11 protein) (Hydrophobestin) 281 30,847 Calcium binding (2); Chain (1); Domain (2); Modified residue (2); Sequence conflict (2); Signal peptide (1) FUNCTION: Mediates cell-cell adhesion in a calcium-dependent manner. Able to inhibit growth in several cell lines (By similarity). {ECO:0000250}. PTM: Probably digested extracellularly by an unknown serine protease generating extremely hydrophobic bioactive peptides. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. DOMAIN: Both EF-hands are required for function. {ECO:0000250}. +P55849 DSC1_MOUSE Desmocollin-1 886 98,938 Alternative sequence (2); Chain (1); Domain (5); Glycosylation (4); Modified residue (1); Propeptide (1); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 692 714 Helical. {ECO:0000255}. TOPO_DOM 135 691 Extracellular. {ECO:0000255}.; TOPO_DOM 715 886 Cytoplasmic. {ECO:0000255}. FUNCTION: Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion. May contribute to epidermal cell positioning (stratification) by mediating differential adhesiveness between cells that express different isoforms. Linked to the keratinization of epithelial tissues. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Cell junction, desmosome. SUBUNIT: Binds to JUP/plakoglobin. {ECO:0000250}. DOMAIN: Calcium may be bound by the cadherin-like repeats. {ECO:0000305}. +P55292 DSC2_MOUSE Desmocollin-2 (Epithelial type 2 desmocollin) 902 99,961 Alternative sequence (2); Chain (1); Domain (5); Glycosylation (4); Modified residue (3); Propeptide (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 695 715 Helical. {ECO:0000255}. TOPO_DOM 136 694 Extracellular. {ECO:0000255}.; TOPO_DOM 716 902 Cytoplasmic. {ECO:0000255}. FUNCTION: Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion. May contribute to epidermal cell positioning (stratification) by mediating differential adhesiveness between cells that express different isoforms. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Cell junction, desmosome. DOMAIN: Calcium may be bound by the cadherin-like repeats. {ECO:0000305}.; DOMAIN: Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain. {ECO:0000250}. TISSUE SPECIFICITY: In all epithelia tested and heart. +P55850 DSC3_MOUSE Desmocollin-3 896 100,203 Alternative sequence (2); Chain (1); Domain (5); Frameshift (1); Glycosylation (4); Propeptide (1); Sequence conflict (10); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 696 716 Helical. {ECO:0000255}. TOPO_DOM 136 695 Extracellular. {ECO:0000255}.; TOPO_DOM 717 896 Cytoplasmic. {ECO:0000255}. FUNCTION: Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion. May contribute to epidermal cell positioning (stratification) by mediating differential adhesiveness between cells that express different isoforms. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Cell junction, desmosome {ECO:0000250}. DOMAIN: Calcium may be bound by the cadherin-like repeats. {ECO:0000305}.; DOMAIN: Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain. {ECO:0000250}. TISSUE SPECIFICITY: First expressed at E13.0 in epithelium of whisker pads and external nares, and in most mature vibrissa follicles. 12 hours later, prominently expressed in whiskers and tactile follicles above the eye. At E14.5, also expressed in developing nails and teeth and, at low levels, in ventral and lateral skin. At E15.5, highly expressed in general body epidermis and at E16.5, detected over entire embryo. In the adult, highly expressed in basal layers of stratified cells. {ECO:0000269|PubMed:9389456, ECO:0000269|PubMed:9404003}. +Q9ERC8 DSCAM_MOUSE Down syndrome cell adhesion molecule homolog 2013 222,268 Chain (1); Compositional bias (1); Disulfide bond (10); Domain (16); Glycosylation (5); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1595 1615 Helical. {ECO:0000255}. TOPO_DOM 18 1594 Extracellular. {ECO:0000255}.; TOPO_DOM 1616 2013 Cytoplasmic. {ECO:0000255}. FUNCTION: Cell adhesion molecule that plays a role in neuronal self-avoidance. Promotes repulsion between specific neuronal processes of either the same cell or the same subtype of cells. Mediates within retinal amacrine and ganglion cell subtypes both isoneuronal self-avoidance for creating an orderly dendritic arborization and heteroneuronal self-avoidance to maintain the mosaic spacing between amacrine and ganglion cell bodies (PubMed:18216855, PubMed:19196994, PubMed:19945391). Receptor for netrin required for axon guidance independently of and in collaboration with the receptor DCC (PubMed:18585357). In spinal chord development plays a role in guiding commissural axons projection and pathfinding across the ventral midline to reach the floor plate upon ligand binding. Enhances netrin-induced phosphorylation of PAK1 and FYN. Mediates intracellular signaling by stimulating the activation of MAPK8 and MAP kinase p38. Adhesion molecule that promotes lamina-specific synaptic connections in the retina: expressed in specific subsets of interneurons and retinal ganglion cells (RGCs) and promotes synaptic connectivity via homophilic interactions (By similarity). {ECO:0000250|UniProtKB:F1NY98, ECO:0000250|UniProtKB:O60469, ECO:0000269|PubMed:18216855, ECO:0000269|PubMed:18585357, ECO:0000269|PubMed:19196994, ECO:0000269|PubMed:19945391}. PTM: Phosphorylated at tyrosine residues. Phosphorylation is enhanced by netrin. {ECO:0000250|UniProtKB:O60469}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19196994}; Single-pass type I membrane protein {ECO:0000305}. Cell projection, axon {ECO:0000269|PubMed:19196994}. Cell junction, synapse {ECO:0000250|UniProtKB:F1NY98}. Note=Localized in the soma, cell membrane, axon and growth cone of dissociated commissural axons. {ECO:0000269|PubMed:19196994}. SUBUNIT: Homodimer; mediates homophilic interactions to promote cell adhesion (By similarity). Probably found in a ternary complex composed of DSCAM, PAK1 and RAC1. The interaction with PAK1 is direct and enhanced in presence of RAC1 (PubMed:15169762). Interacts with RAC1; the interaction requires PAK1 (By similarity). Interacts (via cytoplasmic domain) with PAK1. Interacts (via extracellular domain) with NTN1 (PubMed:18585357). Interacts with DCC; the interaction is abolished in response to NTN1 (PubMed:18585357). {ECO:0000250|UniProtKB:F1NY98, ECO:0000250|UniProtKB:O60469, ECO:0000269|PubMed:15169762, ECO:0000269|PubMed:18585357}. DOMAIN: Ig-like C2-type domains 7 to 9 are sufficient for interaction with NTN1 and commissural axon outgrowth. The transmembrane domain is necessary for interaction with DCC. TISSUE SPECIFICITY: In the retina, expressed in dopaminergic and Nos1-positive amacrine cells and most retinal ganglion cells (at protein level). Expressed in the brain with highest levels in the cortex, olfactory bulb, hippocampus, thalamus, cerebellum and spinal cord. Expressed in the retinal ganglion layer (RGL). {ECO:0000269|PubMed:11237714, ECO:0000269|PubMed:11856873, ECO:0000269|PubMed:18216855, ECO:0000269|PubMed:19945391}. +Q4VA61 DSCL1_MOUSE Down syndrome cell adhesion molecule-like protein 1 homolog 2053 224,240 Chain (1); Compositional bias (1); Disulfide bond (10); Domain (16); Erroneous initiation (1); Glycosylation (10); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1592 1612 Helical. {ECO:0000255}. TOPO_DOM 19 1591 Extracellular. {ECO:0000255}.; TOPO_DOM 1613 2053 Cytoplasmic. {ECO:0000255}. FUNCTION: Cell adhesion molecule that plays a role in neuronal self-avoidance. Promotes repulsion between specific neuronal processes of either the same cell or the same subtype of cells. Promotes both isoneuronal self-avoidance for creating an orderly neurite arborization in retinal rod bipolar cells and heteroneuronal self-avoidance to maintain mosaic spacing between AII amacrine cells (PubMed:19945391). Adhesion molecule that promotes lamina-specific synaptic connections in the retina: expressed in specific subsets of interneurons and retinal ganglion cells (RGCs) and promotes synaptic connectivity via homophilic interactions (By similarity). {ECO:0000250|UniProtKB:E1C8P7, ECO:0000269|PubMed:19945391}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8TD84}; Single-pass type I membrane protein {ECO:0000305}. Cell junction, synapse {ECO:0000250|UniProtKB:E1C8P7}. SUBUNIT: Homodimer; mediates homophilic interactions to promote cell adhesion. {ECO:0000250|UniProtKB:E1C8P7}. TISSUE SPECIFICITY: In the retina, expressed in the rod photoreceptors, AII amacrine cells and rod bipolar cells (at protein level). {ECO:0000269|PubMed:19945391}. +O35075 DSCR3_MOUSE Down syndrome critical region protein 3 homolog (Down syndrome critical region protein A homolog) 297 32,970 Chain (1) +Q924S9 DSCR6_MOUSE Protein ripply3 (Down syndrome critical region protein 6) 152 16,965 Chain (1); Motif (1); Region (1); Sequence conflict (3) FUNCTION: Acts as a transcriptional corepressor. Negative regulator of the transcriptional activity of TBX1. Plays a role in the development of the pharyngeal apparatus and derivatives. {ECO:0000269|PubMed:21177346}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q2WG80}. SUBUNIT: Interacts with TBX1. {ECO:0000269|PubMed:21177346}. DOMAIN: The Ripply homology domain and the WRPW motif are both necessary for its transcriptional corepressor activity on the transcription activator TBX1.; DOMAIN: The WRPW motif is required for binding to tle/groucho proteins. {ECO:0000250|UniProtKB:Q2WG80}. +Q0VBN2 DSEL_MOUSE Dermatan-sulfate epimerase-like protein (EC 5.1.-.-) 1207 138,868 Chain (1); Glycosylation (5); Signal peptide (1); Transmembrane (2) TRANSMEM 761 781 Helical. {ECO:0000255}.; TRANSMEM 798 818 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8BLI4 DSE_MOUSE Dermatan-sulfate epimerase (DS epimerase) (EC 5.1.3.19) (Chondroitin-glucuronate 5-epimerase) (Squamous cell carcinoma antigen recognized by T-cells 2) (SART-2) 958 109,755 Chain (1); Erroneous initiation (1); Glycosylation (1); Sequence conflict (2); Signal peptide (1); Transmembrane (2) TRANSMEM 903 923 Helical. {ECO:0000255}.; TRANSMEM 934 954 Helical. {ECO:0000255}. Glycan metabolism; chondroitin sulfate biosynthesis. Glycan metabolism; heparan sulfate biosynthesis. FUNCTION: Converts D-glucuronic acid to L-iduronic acid (IdoUA) residues. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q61495 DSG1A_MOUSE Desmoglein-1-alpha (Desmoglein-1) (Dsg1-alpha) (DG1) (DGI) (Desmosomal glycoprotein I) 1057 114,597 Chain (1); Domain (4); Frameshift (1); Glycosylation (2); Propeptide (1); Repeat (5); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 565 585 Helical. {ECO:0000255}. TOPO_DOM 50 564 Extracellular. {ECO:0000255}.; TOPO_DOM 586 1057 Cytoplasmic. {ECO:0000255}. FUNCTION: Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cell junction, desmosome. SUBUNIT: Binds to JUP/plakoglobin. {ECO:0000250}. DOMAIN: Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:12631242}. +Q7TSF1 DSG1B_MOUSE Desmoglein-1-beta (Dsg1-beta) (Desmoglein-5) 1060 114,454 Chain (1); Compositional bias (2); Domain (4); Glycosylation (2); Propeptide (1); Repeat (5); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 568 588 Helical. {ECO:0000255}. TOPO_DOM 50 567 Extracellular. {ECO:0000255}.; TOPO_DOM 589 1060 Cytoplasmic. {ECO:0000255}. FUNCTION: Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cell junction, desmosome {ECO:0000269|PubMed:12631242}. DOMAIN: Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in epidermis. {ECO:0000269|PubMed:12631242, ECO:0000269|PubMed:12787123}. +Q7TSF0 DSG1C_MOUSE Desmoglein-1-gamma (Dsg1-gamma) (Desmoglein-6) 911 100,516 Alternative sequence (2); Chain (1); Domain (3); Glycosylation (3); Propeptide (1); Repeat (5); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 520 540 Helical. {ECO:0000255}. TOPO_DOM 50 519 Extracellular. {ECO:0000255}.; TOPO_DOM 541 911 Cytoplasmic. {ECO:0000255}. FUNCTION: Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cell junction, desmosome. DOMAIN: Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in epidermis, brain, liver, skeletal, muscle and testis. {ECO:0000269|PubMed:12631243, ECO:0000269|PubMed:12787123}. +O55111 DSG2_MOUSE Desmoglein-2 1122 122,385 Chain (1); Domain (4); Glycosylation (4); Modified residue (9); Propeptide (1); Repeat (6); Sequence conflict (6); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 619 639 Helical. {ECO:0000255}. TOPO_DOM 55 618 Extracellular. {ECO:0000255}.; TOPO_DOM 640 1122 Cytoplasmic. {ECO:0000255}. FUNCTION: Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cell junction, desmosome {ECO:0000250}. DOMAIN: Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in epidermis, heart, brain, spleen, lung, liver skeletal muscle, kidney and testis. {ECO:0000269|PubMed:12787123}. +O35902 DSG3_MOUSE Desmoglein-3 (130 kDa pemphigus vulgaris antigen homolog) 993 107,889 Alternative sequence (2); Chain (1); Domain (4); Glycosylation (4); Propeptide (1); Repeat (2); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 618 638 Helical. {ECO:0000255}. TOPO_DOM 50 617 Extracellular. {ECO:0000255}.; TOPO_DOM 639 993 Cytoplasmic. {ECO:0000255}. FUNCTION: Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cell junction, desmosome {ECO:0000250}. DOMAIN: Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in epidermis. {ECO:0000269|PubMed:12787123}. +Q7TMD7 DSG4_MOUSE Desmoglein-4 1041 114,449 Chain (1); Domain (4); Glycosylation (2); Natural variant (1); Propeptide (1); Repeat (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 635 655 Helical. {ECO:0000255}. TOPO_DOM 50 634 Extracellular. {ECO:0000255}.; TOPO_DOM 656 1041 Cytoplasmic. {ECO:0000255}. FUNCTION: Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion. Coordinates the transition from proliferation to differentiation in hair follicle keratinocytes. {ECO:0000269|PubMed:12705872}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cell junction, desmosome {ECO:0000250}. DOMAIN: Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain. {ECO:0000250}. TISSUE SPECIFICITY: Strongly expressed in the skin; during the anagen stage of hair follicles in the matrix, precortex and inner rooth sheath. {ECO:0000269|PubMed:12787123}. DISEASE: Note=Defects in Dsg4 are the cause of an autosomal recessive phenotype lanceolate hair (lah). Lah mice pups develop only a few short hairs on the head and neck which form a lance head at the tip and disappear within a few month. They have thickened skin and do not exhibit any growth retardation. +Q9CYC5 DSN1_MOUSE Kinetochore-associated protein DSN1 homolog 348 39,553 Chain (1); Cross-link (1); Modified residue (6); Sequence conflict (2) FUNCTION: Part of the MIS12 complex which is required for normal chromosome alignment and segregation and kinetochore formation during mitosis. {ECO:0000250|UniProtKB:Q9H410}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H410}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q9H410}. Note=Associated with the kinetochore. {ECO:0000250|UniProtKB:Q9H410}. SUBUNIT: Component of the MIS12 complex composed of MIS12, DSN1, NSL1 and PMF1. Also interacts with KNL1, CBX3 and CBX5. Interacts with KNSTRN. {ECO:0000250|UniProtKB:Q9H410}. +P97399 DSPP_MOUSE Dentin sialophosphoprotein (Dentin matrix protein 3) (DMP-3) [Cleaved into: Dentin phosphoprotein (Dentin phosphophoryn) (DPP); Dentin sialoprotein (DSP)] 934 93,903 Chain (3); Compositional bias (1); Glycosylation (6); Modified residue (8); Motif (1); Signal peptide (1) FUNCTION: DSP may be an important factor in dentinogenesis. DPP may bind high amount of calcium and facilitate initial mineralization of dentin matrix collagen as well as regulate the size and shape of the crystals. PTM: DSP is glycosylated. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. SUBUNIT: Interacts with FBLN7. {ECO:0000269|PubMed:17699513}. TISSUE SPECIFICITY: Expressed in teeth, mainly in odontoblasts and transiently in pre-ameloblasts. Found in the inner ear. {ECO:0000269|PubMed:11175790, ECO:0000269|PubMed:9395101}. +Q99MU3 DSRAD_MOUSE Double-stranded RNA-specific adenosine deaminase (DRADA) (EC 3.5.4.37) (RNA adenosine deaminase 1) 1178 130,447 Active site (1); Alternative sequence (3); Chain (1); Cross-link (4); Domain (4); Metal binding (3); Modified residue (12); Natural variant (4); Region (3); Repeat (2); Sequence conflict (8) FUNCTION: Catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA) referred to as A-to-I RNA editing. This may affect gene expression and function in a number of ways that include mRNA translation by changing codons and hence the amino acid sequence of proteins; pre-mRNA splicing by altering splice site recognition sequences; RNA stability by changing sequences involved in nuclease recognition; genetic stability in the case of RNA virus genomes by changing sequences during viral RNA replication; and RNA structure-dependent activities such as microRNA production or targeting or protein-RNA interactions. Can edit both viral and cellular RNAs and can edit RNAs at multiple sites (hyper-editing) or at specific sites (site-specific editing). Its cellular RNA substrates include: bladder cancer-associated protein (BLCAP), neurotransmitter receptors for glutamate (GRIA2) and serotonin (HTR2C) and GABA receptor (GABRA3). Site-specific RNA editing of transcripts encoding these proteins results in amino acid substitutions which consequently alters their functional activities. Exhibits low-level editing at the GRIA2 Q/R site, but edits efficiently at the R/G site and HOTSPOT1. Does not affect polyomavirus replication but provides protection against virus-induced cytopathic effects. Essential for embryonic development and cell survival and plays a critical role in the maintenance of hematopoietic stem cells. {ECO:0000269|PubMed:15556947, ECO:0000269|PubMed:17079286, ECO:0000269|PubMed:17369310}. PTM: Sumoylation reduces RNA-editing activity. {ECO:0000250|UniProtKB:P55265}. SUBCELLULAR LOCATION: Isoform 1: Cytoplasm. Nucleus, nucleolus. Note=Long forms starting at Met-1 are found predominantly in cytoplasm. Shuttles between the cytoplasm and nucleus.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Nucleus, nucleolus. Note=Long forms starting at Met-1 are found predominantly in cytoplasm.; SUBCELLULAR LOCATION: Isoform 3: Nucleus, nucleolus. Note=Short forms starting at Met-519 are found exclusively in the nucleolus.; SUBCELLULAR LOCATION: Isoform 4: Nucleus, nucleolus. Note=Short forms starting at Met-519 are found exclusively in the nucleolus. SUBUNIT: Homodimer. Homodimerization is essential for its catalytic activity (PubMed:12618436). Isoform 5 can form heterodimers with ADARB1/ADAR2. Isoform 1 and isoform 5 (via DRBM 3 domain) interact with TNPO1. Isoform 5 (via DRBM domains) interacts with XPO5. Isoform 1 and isoform 5 can interact with UPF1 (By similarity). Isoform 1 interacts with ILF2/NF45 and ILF3/NF90 (PubMed:16055709). Binding to ILF3/NF90 up-regulates ILF3-mediated gene expression. Isoform 1 and isoform 5 interact with EIF2AK2/PKR (PubMed:17079286). {ECO:0000250|UniProtKB:P55265, ECO:0000269|PubMed:12618436, ECO:0000269|PubMed:16055709, ECO:0000269|PubMed:17079286}. DOMAIN: The first DRADA repeat binds Z-DNA. {ECO:0000250|UniProtKB:P55265}.; DOMAIN: The third dsRNA-binding domain (DRBM 3) contains an additional N-terminal alpha-helix that is part of a bi-partite nuclear localization signal, together with the sequence immediately C-terminal to DRBM 3. The presence of DRBM 3 is important to bring together the N-terminal and the C-terminal part of the bi-partite nuclear localization signal for import mediated by TNPO1. RNA binding interferes with nuclear import. {ECO:0000250|UniProtKB:P55265}. TISSUE SPECIFICITY: Highest levels in brain and spleen. Lowest levels in liver. {ECO:0000269|PubMed:12954622}. +Q8BHA3 DTD2_MOUSE D-aminoacyl-tRNA deacylase 2 (EC 3.1.1.96) (Animalia-specific tRNA deacylase) (ATD) (D-tyrosyl-tRNA deacylase 2) (L-alanyl-tRNA deacylase) (EC 3.1.1.-) 168 18,236 Alternative sequence (1); Beta strand (9); Chain (1); Frameshift (1); Helix (4); Motif (1); Turn (1) FUNCTION: Deacylates mischarged D-aminoacyl-tRNAs. Probably acts by rejecting L-amino acids from its binding site rather than specific recognition of D-amino acids. Catalyzes the hydrolysis of D-tyrosyl-tRNA(Tyr), has no activity on correctly charged L-tyrosyl-tRNA(Tyr). By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo and helps enforce protein L-homochirality. In contrast to DTD1, deacylates L-Ala mischarged on tRNA(Thr)(G4.U69) by alanine-tRNA ligase AARS. Can deacylate L-Ala due to a relaxed specificity for substrate chirality caused by the trans conformation of the Gly-Pro motif in the active site. Also hydrolyzes correctly charged, achiral, glycyl-tRNA(Gly) in vitro, although in vivo EEF1A1/EF-Tu may protect cognate achiral glycyl-tRNA(Gly) from DTD2-mediated deacetylation. {ECO:0000269|PubMed:29410408}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. SUBUNIT: Homodimer. {ECO:0000269|PubMed:29410408}. DOMAIN: A Gly-transPro motif from one monomer fits into the active site of the other monomer to allow specific chiral rejection of most L-amino acids except L-Ala. The trans conformation of the motif is maintained by Arg-151. {ECO:0000269|PubMed:29410408}. +Q3TLR7 DTL_MOUSE Denticleless protein homolog (Lethal(2) denticleless protein homolog) (Meth A retinoic acid-regulated nuclear matrix-associated protein) (Meth A RAMP) (Retinoic acid-regulated nuclear matrix-associated protein) 729 79,131 Alternative sequence (3); Chain (1); Compositional bias (1); Erroneous initiation (1); Frameshift (1); Modified residue (15); Motif (3); Repeat (7); Sequence conflict (8) Protein modification; protein ubiquitination. FUNCTION: Substrate-specific adapter of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex required for cell cycle control, DNA damage response and translesion DNA synthesis. The DCX(DTL) complex, also named CRL4(CDT2) complex, mediates the polyubiquitination and subsequent degradation of CDT1, CDKN1A/p21(CIP1), FBH1, KMT5A and SDE2. CDT1 degradation in response to DNA damage is necessary to ensure proper cell cycle regulation of DNA replication. CDKN1A/p21(CIP1) degradation during S phase or following UV irradiation is essential to control replication licensing. KMT5A degradation is also important for a proper regulation of mechanisms such as TGF-beta signaling, cell cycle progression, DNA repair and cell migration. Most substrates require their interaction with PCNA for their polyubiquitination: substrates interact with PCNA via their PIP-box, and those containing the 'K+4' motif in the PIP box, recruit the DCX(DTL) complex, leading to their degradation. In undamaged proliferating cells, the DCX(DTL) complex also promotes the 'Lys-164' monoubiquitination of PCNA, thereby being involved in PCNA-dependent translesion DNA synthesis. {ECO:0000250|UniProtKB:Q9NZJ0}. PTM: Ubiquitinated by the anaphase promoting complex/cyclosome (APC/C). Autoubiquitinated through 'Lys-48'-polyubiquitin chains in a PCNA-independent reaction, allowing proteasomal turnover. Polyubiquitinated by SCF(FBXO11) when not phosphorylated, leading to its degradation. A tight regulation of the polyubiquitination by SCF(FBXO11) is involved in the control of different processes such as TGF-beta signaling, cell cycle progression and exit (By similarity). {ECO:0000250|UniProtKB:Q9NZJ0}.; PTM: Phosphorylated at Thr-463 by CDK1/Cyclin B and CDK2/Cycnlin A but not by CDK2/Cyclin E, MAPK1 or PLK1. Phosphorylation at Thr-463 inhibits the interaction with FBXO11 and decreases upon cell cycle exit induced by TGF-beta or serum starvation (By similarity). {ECO:0000250|UniProtKB:Q9NZJ0}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NZJ0}. Nucleus membrane {ECO:0000250|UniProtKB:Q9NZJ0}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9NZJ0}; Nucleoplasmic side {ECO:0000250|UniProtKB:Q9NZJ0}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9NZJ0}. Chromosome {ECO:0000250|UniProtKB:Q9NZJ0}. Note=Nuclear matrix-associated protein. Translocates from the interphase nucleus to the metaphase cytoplasm during mitosis (By similarity). {ECO:0000250|UniProtKB:Q9NZJ0}. SUBUNIT: Component of the DCX(DTL) E3 ubiquitin ligase complex (also called CRL4(CDT2)), at least composed of CUL4 (CUL4A or CUL4B), DDB1, DTL/CDT2 and RBX1. Interacts with CDKN1A and CDT1. Interacts with FBXO11; SCF(FBXWO11) controls DTL stability but DCX(DTL) does not control FBXO11 stability (By similarity). {ECO:0000250|UniProtKB:Q9NZJ0}. +Q9D2N4 DTNA_MOUSE Dystrobrevin alpha (DTN-A) (Alpha-dystrobrevin) 746 84,067 Alternative sequence (9); Chain (1); Coiled coil (1); Modified residue (1); Region (2); Sequence conflict (5); Zinc finger (1) FUNCTION: Involved in synapse maturation and required for normal muscle function. PTM: Phosphorylation of isoform 2 on tyrosine kinase substrate domain present in the C-terminus. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14623885}. Cell junction, synapse {ECO:0000269|PubMed:14623885}. Cell membrane {ECO:0000269|PubMed:14623885}. Note=In peripheral nerves, colocalizes with MAGEE1 in the Schwann cell membrane. SUBUNIT: Interacts with dystrophin, utrophin and the syntrophins SNTA1, SNTB1, SNTB2, SNTG1 and SNTG2. Isoforms 5 and 6 do not interact with syntrophin. Isoforms 3 and 4 do not interact with utrophin. Binds dystrobrevin binding protein 1. Interacts with MAGEE1. {ECO:0000269|PubMed:11316798, ECO:0000269|PubMed:14623885, ECO:0000269|PubMed:7547961, ECO:0000269|PubMed:9214383}. DOMAIN: The coiled coil domain mediates the interaction with dystrophin and utrophin. TISSUE SPECIFICITY: Expressed in skeletal muscle, heart, lung and brain. Sarcolemma and neuromuscular junction in skeletal muscle. Isoform 2 is restricted to the neuromuscular junction. Isoforms 5 and 6 are only expressed in muscle. +O70585 DTNB_MOUSE Dystrobrevin beta (DTN-B) (mDTN-B) (Beta-dystrobrevin) 659 74,399 Alternative sequence (3); Chain (1); Coiled coil (1); Erroneous initiation (1); Frameshift (1); Modified residue (2); Region (1); Sequence conflict (3); Zinc finger (1) SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Interacts with dystrophin short form DP71 and syntrophins SNTG1 and SNTG2 (By similarity). Binds dystrobrevin binding protein 1. {ECO:0000250, ECO:0000269|PubMed:11316798}. DOMAIN: The coiled coil domain may mediate the interaction with dystrophin. TISSUE SPECIFICITY: Expressed mainly in brain, kidney, liver and lung. In brain expressed in neurons of the cortex and hippocampus. +Q9D8U7 DTWD1_MOUSE DTW domain-containing protein 1 304 34,734 Chain (1); Motif (1) DOMAIN: Contains 1 DXTW motif. +Q9D0U1 DTWD2_MOUSE DTW domain-containing protein 2 298 33,102 Chain (1); Modified residue (2); Motif (1) DOMAIN: Contains 1 DXTW motif. +Q9D9D8 DUS21_MOUSE Dual specificity phosphatase 21 (EC 3.1.3.16) (EC 3.1.3.48) 189 21,509 Active site (1); Chain (1); Domain (1); Region (1) FUNCTION: Can dephosphorylate single and diphosphorylated synthetic MAPK peptides, with preference for the phosphotyrosine and diphosphorylated forms over phosphothreonine. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Mitochondrion inner membrane {ECO:0000269|PubMed:18385140}; Peripheral membrane protein {ECO:0000269|PubMed:18385140}; Matrix side {ECO:0000269|PubMed:18385140}. TISSUE SPECIFICITY: Selectively expressed in testis. {ECO:0000269|PubMed:18385140}. +Q99N11 DUS22_MOUSE Dual specificity protein phosphatase 22 (EC 3.1.3.16) (EC 3.1.3.48) (Low molecular weight dual specificity phosphatase 2) (LMW-DSP2) 184 20,997 Active site (1); Alternative sequence (1); Chain (1); Domain (1); Erroneous gene model prediction (1); Initiator methionine (1); Lipidation (1); Mutagenesis (2) FUNCTION: Activates the Jnk signaling pathway. Dephosphorylates and deactivates p38 and stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK). {ECO:0000269|PubMed:11346645}. PTM: Myristoylation regulates subcellular location, and is necessary for activation of JNK. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11346645}. Nucleus {ECO:0000269|PubMed:11346645}. SUBUNIT: Monomer. {ECO:0000250}. TISSUE SPECIFICITY: Specifically expressed in the testis. {ECO:0000269|PubMed:11346645}. +Q6NT99 DUS23_MOUSE Dual specificity protein phosphatase 23 (EC 3.1.3.16) (EC 3.1.3.48) (Low molecular mass dual specificity phosphatase 3) (LDP-3) 150 16,637 Active site (1); Chain (1); Domain (1); Sequence conflict (1) FUNCTION: Protein phosphatase that mediates dephosphorylation of proteins phosphorylated on Tyr and Ser/Thr residues. In vitro, it can dephosphorylate p44-ERK1 (MAPK3) but not p54 SAPK-beta (MAPK10) in vitro. Able to enhance activation of JNK and p38 (MAPK14). {ECO:0000269|PubMed:15281913}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Nucleus {ECO:0000250}. Note=Mainly cytosolic. Weakly nuclear (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15281913}. +P56394 COX17_MOUSE Cytochrome c oxidase copper chaperone 63 6,784 Chain (1); Compositional bias (1); Disulfide bond (2); Domain (1); Metal binding (2); Motif (2); Mutagenesis (3) FUNCTION: Copper metallochaperone essential for the assembly of the mitochondrial respiratory chain complex IV (CIV), also known as cytochrome c oxidase. Binds two copper ions and delivers them to the metallochaperone SCO1 which transports the copper ions to the Cu(A) site on the cytochrome c oxidase subunit II (MT-CO2/COX2). {ECO:0000269|PubMed:12370308}. SUBCELLULAR LOCATION: Mitochondrion intermembrane space {ECO:0000250|UniProtKB:Q14061}. Cytoplasm {ECO:0000250|UniProtKB:Q14061}. SUBUNIT: Interacts with COA1. Interacts with the chaperone CHCHD4; this is important for correct folding and the formation of disulfide bonds that stabilize the structure. {ECO:0000250|UniProtKB:Q14061}. +O09112 DUS8_MOUSE Dual specificity protein phosphatase 8 (EC 3.1.3.16) (EC 3.1.3.48) (Neuronal tyrosine threonine phosphatase 1) 663 68,847 Active site (1); Chain (1); Compositional bias (5); Domain (2) FUNCTION: Has phosphatase activity with synthetic phosphatase substrates and negatively regulates mitogen-activated protein kinase activity, presumably by catalysing their dephosphorylation (PubMed:7561881). Expected to display protein phosphatase activity toward phosphotyrosine, phosphoserine and phosphothreonine residues (Probable). {ECO:0000269|PubMed:7561881, ECO:0000305}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8733137}. Nucleus {ECO:0000269|PubMed:8733137}. SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q13202}. TISSUE SPECIFICITY: Expressed predominantly in brain and lung. {ECO:0000269|PubMed:8733137}. +Q922R1 CP070_MOUSE UPF0183 protein C16orf70 homolog 422 47,416 Chain (1); Sequence conflict (1) +Q7TSH4 CP110_MOUSE Centriolar coiled-coil protein of 110 kDa (Centrosomal protein of 110 kDa) (Cep110) (Cp110) 1004 111,139 Chain (1); Coiled coil (2); Modified residue (5); Region (6) FUNCTION: Necessary for centrosome duplication at different stages of procentriole formation. Acts as a key negative regulator of ciliogenesis in collaboration with CEP97 by capping the mother centriole thereby preventing cilia formation (PubMed:23141541). Also involved in promoting ciliogenesis. May play a role in the assembly of the mother centriole subdistal appendages (SDA) thereby effecting the fusion of recycling endosomes to basal bodies during cilia formation (PubMed:26965371). Required for correct spindle formation and has a role in regulating cytokinesis and genome stability via cooperation with CALM1 and CETN2 (By similarity). {ECO:0000250, ECO:0000269|PubMed:23141541, ECO:0000269|PubMed:26965371}. PTM: Phosphorylated by CDKs. {ECO:0000250}.; PTM: Ubiquitinated by the SCF(CCNF) during G2 phase, leading to its degradation by the proteasome and preventing centrosome reduplication. Deubiquitinated by USP33 in S and G2/M phase, leading to stabilize CCP110 during the period which centrioles duplicate and elongate (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:O43303}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:23807208}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:23807208}. Note=Recruited early and then associates with the growing distal tips (PubMed:23141541). Recruited to the mother centriole by KIF24 (By similarity). Removed from centrioles by TTBK2, leading to initiation of ciliogenesis and localizes only to the daughter centriole in ciliated cells (PubMed:23141541). In cytotoxic T lymphocytes remains associated with the mother centriole during docking of the centrosome at the immunological synapse upon target contact (PubMed:26670998). {ECO:0000250|UniProtKB:O43303, ECO:0000269|PubMed:23141541, ECO:0000269|PubMed:26670998}. SUBUNIT: Interacts with CALM1, CETN2, CEP76, CEP97, CEP104, CEP290, TALPID3. Seems to associate with discrete CETN2, CEP97 and CEP290-containing complexes. Interacts with NEURL4 and CCNF; these interactions are not mutually exclusive and both lead to CCP110 ubiquitination and proteasome-dependent degradation. Via its interaction with NEURL4, may indirectly interact with HERC2. Interacts with KIF24, leading to its recruitment to centrioles. Interacts with USP20 and USP33 (By similarity). {ECO:0000250|UniProtKB:O43303}. +Q05421 CP2E1_MOUSE Cytochrome P450 2E1 (EC 1.14.13.-) (4-nitrophenol 2-hydroxylase) (EC 1.14.13.n7) (CYPIIE1) (Cytochrome P450-ALC) (Cytochrome P450-J) 493 56,805 Chain (1); Metal binding (1); Region (1) FUNCTION: Metabolizes several precarcinogens, drugs, and solvents to reactive metabolites. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. TISSUE SPECIFICITY: Highest level in the liver and to a lesser extent in the kidney, with a higher level in the male kidney than in the female. +Q7TPV2 DZIP3_MOUSE E3 ubiquitin-protein ligase DZIP3 (EC 2.3.2.27) (DAZ-interacting protein 3 homolog) (RING-type E3 ubiquitin transferase DZIP3) 1204 138,021 Alternative sequence (5); Chain (1); Coiled coil (2); Compositional bias (3); Erroneous initiation (1); Sequence conflict (2); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: E3 Ubiquitin ligase proteins mediate ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Able to specifically bind RNA. {ECO:0000250|UniProtKB:Q86Y13}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q86Y13}. SUBUNIT: Probably interacts with DAZL. {ECO:0000250|UniProtKB:Q86Y13}. +Q8BH50 CR025_MOUSE Uncharacterized protein C18orf25 homolog 245 26,446 Alternative sequence (2); Chain (1); Coiled coil (1); Compositional bias (1); Modified residue (5) TISSUE SPECIFICITY: Detected in brain, liver, lung, kidney, heart, spleen, skeletal muscle and spinal cord. {ECO:0000269|PubMed:15722956}. +Q7TN98 CPEB4_MOUSE Cytoplasmic polyadenylation element-binding protein 4 (CPE-BP4) (CPE-binding protein 4) (mCPEB-4) 729 80,122 Alternative sequence (4); Chain (1); Compositional bias (2); Domain (2); Metal binding (8); Modified residue (8); Region (2); Site (2) FUNCTION: Sequence-specific RNA-binding protein that binds to the cytoplasmic polyadenylation element (CPE), an uridine-rich sequence element (consensus sequence 5'-UUUUUAU-3') within the mRNA 3'-UTR (PubMed:17024188). RNA binding results in a clear conformational change analogous to the Venus fly trap mechanism (By similarity). Regulates activation of unfolded protein response (UPR) in the process of adaptation to ER stress in liver, by maintaining translation of CPE-regulated mRNAs in conditions in which global protein synthesis is inhibited (PubMed:28092655). Required for cell cycle progression, specifically for cytokinesis and chromosomal segregation (By similarity). Plays a role as an oncogene promoting tumor growth and progression by positively regulating translation of t-plasminogen activator/PLAT (PubMed:22138752). Stimulates proliferation of melanocytes (By similarity). In contrast to CPEB1 and CPEB3, does not play role in synaptic plasticity, learning and memory (PubMed:24386439). {ECO:0000250|UniProtKB:Q17RY0, ECO:0000269|PubMed:17024188, ECO:0000269|PubMed:22138752, ECO:0000269|PubMed:24386439, ECO:0000269|PubMed:28092655}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27381259}. Cell projection, dendrite {ECO:0000269|PubMed:17024188, ECO:0000269|PubMed:24386439}. Cell projection, dendritic spine {ECO:0000269|PubMed:24386439}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000269|PubMed:17024188}. Cell projection, axon {ECO:0000269|PubMed:27381259}. Cell projection, growth cone {ECO:0000269|PubMed:27381259}. Endoplasmic reticulum {ECO:0000269|PubMed:28092655}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:28092655}. SUBUNIT: Interacts with TOB1. {ECO:0000250|UniProtKB:Q17RY0}. DOMAIN: The 2 RRM domains and the C-terminal region mediate interaction with CPE-containing RNA. The interdomain linker (564-579) acts as a hinge to fix the relative orientation of the 2 RRMs. The ZZ domain (509-566) coordinates 2 Zn ions and is probably implicated in mediating interactions with other proteins in addition to increasing the affinity of the RRMs for the CPEs. Unlike in CPEB1, a continuous polar interface is formed between the 2 RRMs. {ECO:0000250|UniProtKB:Q17RY0, ECO:0000250|UniProtKB:Q9BZB8}. TISSUE SPECIFICITY: Highly expressed in brain, including hippocampus, amygdala, granule and Purkinje cells of the cerebellum (at protein level) (PubMed:17024188, PubMed:24386439). Expressed in spinal cord (at protein level) (PubMed:27381259). Expressed in kidney, lung and heart (at protein level) (PubMed:12871996, PubMed:27381259, PubMed:24386439). Expressed in liver (at protein level) (PubMed:28092655, PubMed:12871996, PubMed:27381259, PubMed:24386439). Expressed in spleen and testis (at protein level) (PubMed:24386439, PubMed:12871996). Weakly expressed in ovary and in granular cells of dentate gyrus and the pyramidal cells of CA3 and CA1 of the hippocampus (PubMed:12871996). {ECO:0000269|PubMed:12871996, ECO:0000269|PubMed:17024188, ECO:0000269|PubMed:24386439, ECO:0000269|PubMed:27381259, ECO:0000269|PubMed:28092655}. +O54751 CRX_MOUSE Cone-rod homeobox protein 299 32,374 Chain (1); DNA binding (1) FUNCTION: Transcription factor that binds and transactivates the sequence 5'-TAATC[CA]-3' which is found upstream of several photoreceptor-specific genes, including the opsin genes. Acts synergistically with other transcription factors, such as NRL, RORB and RAX, to regulate photoreceptor cell-specific gene transcription. Essential for the maintenance of mammalian photoreceptors. {ECO:0000269|PubMed:16574740}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:16574740}. SUBUNIT: Interacts (via the homeobox) with NRL (via the leucine-zipper domain). Interacts with PDC, RAX2, RORB and SCA7. {ECO:0000269|PubMed:16574740}. TISSUE SPECIFICITY: Retina. {ECO:0000269|PubMed:16574740}. +Q0V8T9 CTP5A_MOUSE Contactin-associated protein like 5-1 (Cell recognition molecule Caspr5-1) (Cell recognition molecule Caspr5a) (Contactin-associated protein-like 5a) 1304 145,711 Chain (1); Compositional bias (2); Disulfide bond (10); Domain (8); Glycosylation (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1237 1257 Helical. {ECO:0000255}. TOPO_DOM 25 1236 Extracellular. {ECO:0000255}.; TOPO_DOM 1258 1304 Cytoplasmic. {ECO:0000255}. FUNCTION: May play a role in the correct development and proper functioning of the peripheral and central nervous system and be involved in cell adhesion and intercellular communication. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in brain. {ECO:0000269|PubMed:16845472}. +Q91VA1 CTL4_MOUSE Choline transporter-like protein 4 (Solute carrier family 44 member 4) (Thiamine pyrophosphate transporter 1) (mTPPT1) 707 78,723 Chain (1); Glycosylation (8); Sequence conflict (1); Topological domain (11); Transmembrane (10) TRANSMEM 33 53 Helical. {ECO:0000255}.; TRANSMEM 228 248 Helical. {ECO:0000255}.; TRANSMEM 251 271 Helical. {ECO:0000255}.; TRANSMEM 308 328 Helical. {ECO:0000255}.; TRANSMEM 357 377 Helical. {ECO:0000255}.; TRANSMEM 453 473 Helical. {ECO:0000255}.; TRANSMEM 499 519 Helical. {ECO:0000255}.; TRANSMEM 558 578 Helical. {ECO:0000255}.; TRANSMEM 595 615 Helical. {ECO:0000255}.; TRANSMEM 636 656 Helical. {ECO:0000255}. TOPO_DOM 1 32 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 54 227 Extracellular. {ECO:0000255}.; TOPO_DOM 249 250 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 272 307 Extracellular. {ECO:0000255}.; TOPO_DOM 329 356 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 378 452 Extracellular. {ECO:0000255}.; TOPO_DOM 474 498 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 520 557 Extracellular. {ECO:0000255}.; TOPO_DOM 579 594 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 616 635 Extracellular. {ECO:0000255}.; TOPO_DOM 657 707 Cytoplasmic. {ECO:0000255}. FUNCTION: Choline transporter that plays a role in the choline-acetylcholine system and is required to the efferent innervation of hair cells in the olivocochlear bundle for the maintenance of physiological function of outer hair cells and the protection of hair cells from acoustic injury (By similarity). Also described as a thiamine pyrophosphate transporter in colon, may mediate the absorption of microbiota-generated thiamine pyrophosphate and contribute to host thiamine (vitamin B1) homeostasis (PubMed:24379411). {ECO:0000250|UniProtKB:Q53GD3, ECO:0000250|UniProtKB:Q7T2B0, ECO:0000269|PubMed:24379411}. PTM: N-glycosylated; N-glycosylation of Asn-67 and Asn-391 is required for a proper thiamine pyrophosphate uptake. {ECO:0000250|UniProtKB:Q53GD3}. SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q53GD3}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q53GD3}. Apical cell membrane {ECO:0000250|UniProtKB:Q53GD3}. TISSUE SPECIFICITY: Expressed in colon and cecum. {ECO:0000269|PubMed:24379411}. +Q6PEE2 CTIF_MOUSE CBP80/20-dependent translation initiation factor 600 67,831 Alternative sequence (1); Chain (1); Domain (1); Modified residue (4); Region (1); Sequence conflict (1) FUNCTION: Specifically required for the pioneer round of mRNA translation mediated by the cap-binding complex (CBC), that takes place during or right after mRNA export via the nuclear pore complex (NPC). Acts via its interaction with the NCBP1/CBP80 component of the CBC complex and recruits the 40S small subunit of the ribosome via eIF3. In contrast, it is not involved in steady state translation, that takes place when the CBC complex is replaced by cytoplasmic cap-binding protein eIF4E. Also required for nonsense-mediated mRNA decay (NMD), the pioneer round of mRNA translation mediated by the cap-binding complex playing a central role in nonsense-mediated mRNA decay (NMD) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}. SUBUNIT: Interacts with NCBP1/CBP80; the interaction is direct. Associates with the eukaryotic translation initiation factor 3 (eIF-3) complex (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:19648179}. +Q09143 CTR1_MOUSE High affinity cationic amino acid transporter 1 (CAT-1) (CAT1) (Ecotropic retroviral leukemia receptor) (Ecotropic retrovirus receptor) (ERR) (Solute carrier family 7 member 1) (System Y+ basic amino acid transporter) 622 67,092 Chain (1); Glycosylation (2); Modified residue (1); Topological domain (15); Transmembrane (14) TRANSMEM 36 57 Helical. {ECO:0000255}.; TRANSMEM 62 82 Helical. {ECO:0000255}.; TRANSMEM 103 123 Helical. {ECO:0000255}.; TRANSMEM 163 183 Helical. {ECO:0000255}.; TRANSMEM 192 212 Helical. {ECO:0000255}.; TRANSMEM 240 260 Helical. {ECO:0000255}.; TRANSMEM 281 300 Helical. {ECO:0000255}.; TRANSMEM 331 351 Helical. {ECO:0000255}.; TRANSMEM 378 398 Helical. {ECO:0000255}.; TRANSMEM 402 422 Helical. {ECO:0000255}.; TRANSMEM 486 506 Helical. {ECO:0000255}.; TRANSMEM 520 544 Helical. {ECO:0000255}.; TRANSMEM 553 573 Helical. {ECO:0000255}.; TRANSMEM 578 598 Helical. {ECO:0000255}. TOPO_DOM 1 35 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 58 61 Extracellular. {ECO:0000255}.; TOPO_DOM 83 102 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 124 162 Extracellular. {ECO:0000255}.; TOPO_DOM 184 191 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 213 239 Extracellular. {ECO:0000255}.; TOPO_DOM 261 280 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 301 330 Extracellular. {ECO:0000255}.; TOPO_DOM 352 377 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 399 401 Extracellular. {ECO:0000255}.; TOPO_DOM 423 485 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 507 519 Extracellular. {ECO:0000255}.; TOPO_DOM 545 552 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 574 577 Extracellular. {ECO:0000255}.; TOPO_DOM 599 622 Cytoplasmic. {ECO:0000255}. FUNCTION: High-affinity, low capacity permease involved in the transport of the cationic amino acids (arginine, lysine and ornithine) in non-hepatic tissues. {ECO:0000269|PubMed:1652100}.; FUNCTION: (Microbial infection) Acts as a receptor for the ecotropic murine retroviral leukemia virus. {ECO:0000269|PubMed:2541919}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25683716, ECO:0000269|PubMed:28973536}; Multi-pass membrane protein {ECO:0000255}. Note=In the absence of SCO1 in cardiomyocytes a mislocalization to the cytoplasm is seen. {ECO:0000269|PubMed:28973536}. TISSUE SPECIFICITY: Highest levels found in the testis and bone marrow. Not found in the liver. +Q9CQ89 CUTA_MOUSE Protein CutA (Brain acetylcholinesterase putative membrane anchor) 177 18,865 Alternative sequence (2); Chain (1); Erroneous initiation (3); Sequence conflict (1); Signal peptide (1) SUBUNIT: Homotrimer. {ECO:0000250}. +P53564 CUX1_MOUSE Homeobox protein cut-like 1 (CCAAT displacement protein) (CDP) (Homeobox protein cux-1) 1515 165,596 Alternative sequence (5); Chain (1); Coiled coil (1); Compositional bias (1); Cross-link (4); DNA binding (4); Erroneous initiation (1); Modified residue (10); Sequence conflict (5) FUNCTION: Probably has a broad role in mammalian development as a repressor of developmentally regulated gene expression. May act by preventing binding of positively-activing CCAAT factors to promoters. Component of nf-munr repressor; binds to the matrix attachment regions (MARs) (5' and 3') of the immunoglobulin heavy chain enhancer. Represses T-cell receptor (TCR) beta enhancer function by binding to MARbeta, an ATC-rich DNA sequence located upstream of the TCR beta enhancer. Binds to the TH enhancer; may require the basic helix-loop-helix protein TCF4 as a coactivator. {ECO:0000269|PubMed:11544187, ECO:0000269|PubMed:15371550, ECO:0000269|PubMed:9858552}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-ProRule:PRU00374, ECO:0000269|PubMed:15371550}. SUBUNIT: Interacts with BANP. Interacts with SATB1 (via DNA-binding domains); the interaction inhibits the attachment of both proteins to DNA. {ECO:0000269|PubMed:10373541, ECO:0000269|PubMed:15371550}. TISSUE SPECIFICITY: Isoform 6 is testis-specific where it is expressed in germ cells. {ECO:0000269|PubMed:8879483}. +P70298 CUX2_MOUSE Homeobox protein cut-like 2 (Homeobox protein Cux-2) 1426 154,664 Chain (1); Coiled coil (2); DNA binding (4); Modified residue (1); Sequence conflict (4) FUNCTION: May be a transcription factor involved in neural specification. Binds to DNA in a sequence-specific manner. SUBCELLULAR LOCATION: Nucleus. TISSUE SPECIFICITY: Restricted to neural tissues. Expressed exclusively in the central and peripheral nervous systems. +P70412 CUZD1_MOUSE CUB and zona pellucida-like domain-containing protein 1 (CUB and ZP domain-containing protein 1) (Integral membrane-associated protein 1) 606 68,082 Chain (1); Disulfide bond (5); Domain (3); Glycosylation (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 568 588 Helical. {ECO:0000255}. TOPO_DOM 20 567 Extracellular. {ECO:0000255}.; TOPO_DOM 589 606 Cytoplasmic. {ECO:0000255}. FUNCTION: CUZD1 antiserum inhibits cell attachment and proliferation of ovarian cancer cells so may be involved in these processes (By similarity). May also play a role in the uterus during late pregnancy and/or in trypsin activation in pancreatic acinar cells. {ECO:0000250|UniProtKB:Q86UP6, ECO:0000269|PubMed:12401800, ECO:0000269|PubMed:9480914}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Associated with zymogen granule membranes. {ECO:0000269|PubMed:12401800}. TISSUE SPECIFICITY: Highly expressed in pancreatic acinar cells. Also expressed in epithelium of the uterus during late pregnancy but not detected in non-pregnant uterus or in a variety of other adult and fetal tissues. {ECO:0000269|PubMed:12401800, ECO:0000269|PubMed:9480914}. +Q3U595 CV039_MOUSE UPF0545 protein C22orf39 homolog 105 12,503 Chain (1) +O70251 EF1B_MOUSE Elongation factor 1-beta (EF-1-beta) 225 24,694 Chain (1); Cross-link (1); Domain (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (6); Sequence conflict (3) FUNCTION: EF-1-beta and EF-1-delta stimulate the exchange of GDP bound to EF-1-alpha to GTP. {ECO:0000250}. PTM: Phosphorylation affects the GDP/GTP exchange rate. {ECO:0000250}. SUBUNIT: EF-1 is composed of 4 subunits: alpha, beta, delta, and gamma. {ECO:0000250}. +Q9JHS9 CWC15_MOUSE Spliceosome-associated protein CWC15 homolog (Embryonic development factor 1) (mED1) 229 26,624 Chain (1); Coiled coil (1); Initiator methionine (1); Modified residue (5); Sequence conflict (2) FUNCTION: Involved in pre-mRNA splicing as component of the spliceosome. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. {ECO:0000250|UniProtKB:Q9P013}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9P013}. SUBUNIT: Identified in the spliceosome C complex. Component of the PRP19-CDC5L splicing complex composed of a core complex comprising a homotetramer of PRPF19, CDC5L, PLRG1 and BCAS2, and at least three less stably associated proteins CTNNBL1, CWC15 and HSPA8. Interacts directly with CTNNBL1 in the complex. {ECO:0000250|UniProtKB:Q9P013}. +Q9DBF7 CWC25_MOUSE Pre-mRNA-splicing factor CWC25 homolog (Coiled-coil domain-containing protein 49) (Spliceosome-associated protein homolog CWC25) 416 48,811 Alternative sequence (2); Chain (1); Coiled coil (2); Compositional bias (1); Cross-link (1); Modified residue (2); Sequence conflict (1) +Q9D3J9 CX021_MOUSE Uncharacterized protein CXorf21 homolog 298 33,057 Chain (1) +Q9EQ16 CXCR6_MOUSE C-X-C chemokine receptor type 6 (CXC-R6) (CXCR-6) (CD antigen CD186) 351 40,468 Chain (1); Disulfide bond (1); Glycosylation (2); Sequence conflict (5); Topological domain (8); Transmembrane (7) TRANSMEM 42 68 Helical; Name=1. {ECO:0000255}.; TRANSMEM 78 98 Helical; Name=2. {ECO:0000255}.; TRANSMEM 113 134 Helical; Name=3. {ECO:0000255}.; TRANSMEM 153 173 Helical; Name=4. {ECO:0000255}.; TRANSMEM 197 224 Helical; Name=5. {ECO:0000255}.; TRANSMEM 241 268 Helical; Name=6. {ECO:0000255}.; TRANSMEM 285 302 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 41 Extracellular. {ECO:0000255}.; TOPO_DOM 69 77 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 99 112 Extracellular. {ECO:0000255}.; TOPO_DOM 135 152 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 174 196 Extracellular. {ECO:0000255}.; TOPO_DOM 225 240 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 269 284 Extracellular. {ECO:0000255}.; TOPO_DOM 303 351 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for the C-X-C chemokine CXCL16. {ECO:0000269|PubMed:11017100}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q00977 CXB2_MOUSE Gap junction beta-2 protein (Connexin-26) (Cx26) 226 26,411 Chain (1); Disulfide bond (3); Topological domain (5); Transmembrane (4) TRANSMEM 21 40 Helical. {ECO:0000255}.; TRANSMEM 76 98 Helical. {ECO:0000255}.; TRANSMEM 140 162 Helical. {ECO:0000255}.; TRANSMEM 193 215 Helical. {ECO:0000255}. TOPO_DOM 1 20 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 41 75 Extracellular. {ECO:0000255}.; TOPO_DOM 99 139 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 163 192 Extracellular. {ECO:0000255}.; TOPO_DOM 216 226 Cytoplasmic. {ECO:0000255}. FUNCTION: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell junction, gap junction. SUBUNIT: A connexon is composed of a hexamer of connexins. Interacts with CNST. {ECO:0000269|PubMed:19864490}. TISSUE SPECIFICITY: Liver, kidney, intestine, lung, spleen, stomach, testis and brain, but not heart and adult skeletal muscle. +Q8BSD4 CXD4_MOUSE Gap junction delta-4 protein (Connexin-39) (Cx39) 364 40,042 Chain (1); Sequence conflict (3); Topological domain (5); Transmembrane (4) TRANSMEM 20 40 Helical. {ECO:0000255}.; TRANSMEM 77 97 Helical. {ECO:0000255}.; TRANSMEM 129 149 Helical. {ECO:0000255}.; TRANSMEM 174 194 Helical. {ECO:0000255}. TOPO_DOM 1 19 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 41 76 Extracellular. {ECO:0000255}.; TOPO_DOM 98 128 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 150 173 Extracellular. {ECO:0000255}.; TOPO_DOM 195 364 Cytoplasmic. {ECO:0000255}. FUNCTION: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell junction, gap junction {ECO:0000250}. SUBUNIT: A connexon is composed of a hexamer of connexins. {ECO:0000250}. +Q02738 CXB4_MOUSE Gap junction beta-4 protein (Connexin-30.3) (Cx30.3) 266 30,389 Chain (1); Topological domain (5); Transmembrane (4) TRANSMEM 21 40 Helical. {ECO:0000255}.; TRANSMEM 76 98 Helical. {ECO:0000255}.; TRANSMEM 127 149 Helical. {ECO:0000255}.; TRANSMEM 188 210 Helical. {ECO:0000255}. TOPO_DOM 1 20 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 41 75 Extracellular. {ECO:0000255}.; TOPO_DOM 99 126 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 150 187 Extracellular. {ECO:0000255}.; TOPO_DOM 211 266 Cytoplasmic. {ECO:0000255}. FUNCTION: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell junction, gap junction. SUBUNIT: A connexon is composed of a hexamer of connexins. TISSUE SPECIFICITY: Expressed in skin. +Q6S5G4 CXA6_MOUSE Gap junction alpha-6 protein (Connexin-33) (Cx33) 283 32,660 Chain (1); Sequence conflict (1); Topological domain (5); Transmembrane (4) TRANSMEM 24 41 Helical. {ECO:0000255}.; TRANSMEM 77 99 Helical. {ECO:0000255}.; TRANSMEM 151 173 Helical. {ECO:0000255}.; TRANSMEM 209 231 Helical. {ECO:0000255}. TOPO_DOM 1 23 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 42 76 Extracellular. {ECO:0000255}.; TOPO_DOM 100 150 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 174 208 Extracellular. {ECO:0000255}.; TOPO_DOM 232 283 Cytoplasmic. {ECO:0000255}. FUNCTION: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell junction, gap junction. SUBUNIT: A connexon is composed of a hexamer of connexins. +O88410 CXCR3_MOUSE C-X-C chemokine receptor type 3 (CXC-R3) (CXCR-3) (Interferon-inducible protein 10 receptor) (IP-10 receptor) (CD antigen CD183) 367 41,018 Chain (1); Disulfide bond (1); Glycosylation (2); Modified residue (2); Sequence conflict (3); Topological domain (8); Transmembrane (7) TRANSMEM 53 79 Helical; Name=1. {ECO:0000255}.; TRANSMEM 89 109 Helical; Name=2. {ECO:0000255}.; TRANSMEM 125 146 Helical; Name=3. {ECO:0000255}.; TRANSMEM 169 188 Helical; Name=4. {ECO:0000255}.; TRANSMEM 212 232 Helical; Name=5. {ECO:0000255}.; TRANSMEM 255 276 Helical; Name=6. {ECO:0000255}.; TRANSMEM 298 320 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 52 Extracellular. {ECO:0000255}.; TOPO_DOM 80 88 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 110 124 Extracellular. {ECO:0000255}.; TOPO_DOM 147 168 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 189 211 Extracellular. {ECO:0000255}.; TOPO_DOM 233 254 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 277 297 Extracellular. {ECO:0000255}.; TOPO_DOM 321 367 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for the C-X-C chemokine CXCL9, CXCL10 and CXCL11 and mediates the proliferation, survival and angiogenic activity of mesangial cells through a heterotrimeric G-protein signaling pathway. Probably promotes cell chemotaxis response (By similarity). Binds to CCL21. {ECO:0000250, ECO:0000269|PubMed:9653165, ECO:0000269|PubMed:9790904}. PTM: Sulfation on Tyr-27 and Tyr-29 is essential for CXCL10 binding. {ECO:0000250}.; PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Homomer. Forms heteromers with ACKR4 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expresses in lymphoid organs and Th1 cells. {ECO:0000269|PubMed:9790904}. +Q8BQU6 CXG2_MOUSE Gap junction gamma-2 protein (Connexin-47) (Cx47) (Gap junction alpha-12 protein) 440 47,008 Chain (1); Erroneous initiation (2); Modified residue (1); Sequence conflict (3); Topological domain (5); Transmembrane (4) TRANSMEM 22 42 Helical. {ECO:0000255}.; TRANSMEM 79 99 Helical. {ECO:0000255}.; TRANSMEM 224 244 Helical. {ECO:0000255}.; TRANSMEM 265 285 Helical. {ECO:0000255}. TOPO_DOM 1 21 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 43 78 Extracellular. {ECO:0000255}.; TOPO_DOM 100 223 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 245 264 Extracellular. {ECO:0000255}.; TOPO_DOM 286 440 Cytoplasmic. {ECO:0000255}. FUNCTION: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. May play a role in myelination in central and peripheral nervous systems. {ECO:0000269|PubMed:11160382, ECO:0000269|PubMed:12843301}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15183511}; Multi-pass membrane protein {ECO:0000269|PubMed:15183511}. Cell junction, gap junction {ECO:0000269|PubMed:15183511}. SUBUNIT: A connexon is composed of a hexamer of connexins. Interacts with TJP1. {ECO:0000269|PubMed:15183511}. TISSUE SPECIFICITY: Mainly expressed by oligodendrocytes in the central nervous system (at protein level). {ECO:0000269|PubMed:12805295, ECO:0000269|PubMed:12843301, ECO:0000269|PubMed:15183511}. +Q9WVL7 CXL15_MOUSE C-X-C motif chemokine 15 (Lungkine) (Small-inducible cytokine B15) 167 19,091 Chain (1); Disulfide bond (2); Modified residue (1); Signal peptide (1) FUNCTION: Chemotactic for neutrophils. Involved in lung-specific neutrophil trafficking during normal and inflammatory conditions. {ECO:0000269|PubMed:11207292}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10228029}. TISSUE SPECIFICITY: Expression restricted to the lung, produced by bronchoepithelial cells and is released into the airways. Expressed at low levels in fetal lung. {ECO:0000269|PubMed:10228029, ECO:0000269|PubMed:11207292}. +Q8BSU2 CXL16_MOUSE C-X-C motif chemokine 16 (Scavenger receptor for phosphatidylserine and oxidized low density lipoprotein) (SR-PSOX) (Small-inducible cytokine B16) (Transmembrane chemokine CXCL16) 246 26,896 Chain (1); Disulfide bond (2); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 202 222 Helical. {ECO:0000255}. TOPO_DOM 27 201 Extracellular. {ECO:0000255}.; TOPO_DOM 223 246 Cytoplasmic. {ECO:0000255}. FUNCTION: Induces a strong chemotactic response. Induces calcium mobilization. Binds to CXCR6/Bonzo. Also acts as a scavenger receptor on macrophages, which specifically binds to OxLDL (oxidized low density lipoprotein), suggesting that it may be involved in pathophysiology such as atherogenesis. {ECO:0000269|PubMed:11060282}. PTM: Glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Widely expressed. Not detected in purified B- and T-cells. {ECO:0000269|PubMed:11017100, ECO:0000269|PubMed:20675388}. +Q61462 CY24A_MOUSE Cytochrome b-245 light chain (Cytochrome b(558) alpha chain) (Cytochrome b558 subunit alpha) (Neutrophil cytochrome b 22 kDa polypeptide) (Superoxide-generating NADPH oxidase light chain subunit) (p22 phagocyte B-cytochrome) (p22-phox) (p22phox) 192 20,748 Alternative sequence (1); Chain (1); Cross-link (1); Intramembrane (1); Metal binding (1); Modified residue (3); Sequence conflict (1) INTRAMEM 91 127 {ECO:0000250}. FUNCTION: Critical component of the membrane-bound oxidase of phagocytes that generates superoxide. Associates with NOX3 to form a functional NADPH oxidase constitutively generating superoxide. {ECO:0000269|PubMed:19755709}. PTM: The heme prosthetic group could be coordinated with residues of the light chain, the heavy chain, or both, and it is possible that more than one heme is present per cytochrome b-245. {ECO:0000250}.; PTM: Phosphorylation at Thr-147 enhances NADPH oxidase activity by promoting p47phox binding. {ECO:0000250}.; PTM: Ubiquitinated at Lys-149 likely by RNF145. {ECO:0000269|PubMed:26194095}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P13498}. Note=As unassembled monomer may localize to the endoplasmic reticulum. {ECO:0000305|PubMed:19755709}. SUBUNIT: Composed of a heavy chain (beta) and a light chain (alpha). Component of an NADPH oxidase complex composed of a heterodimer formed by the membrane proteins CYBA and CYBB and the cytosolic subunits NCF1, NCF2 and NCF4. Interacts with NCF1 (via SH3 domain). Interacts with DUOX1, DUOX2 and TPO. Interacts with NOX3 and NOX4. Interacts with calprotectin (S100A8/9) (By similarity). Interacts with SH3PXD2A. {ECO:0000250, ECO:0000269|PubMed:19755709}. TISSUE SPECIFICITY: The strongest level of expression is found in kidney, peritoneal neutrophils and peritoneal macrophages, and a lower level in spleen and small intestine. Very low level of expression can be noted in brain, liver, testis, and heart. {ECO:0000269|PubMed:2597164}. +Q9CXW3 CYBP_MOUSE Calcyclin-binding protein (CacyBP) (Siah-interacting protein) 229 26,510 Chain (1); Domain (2); Erroneous initiation (1); Helix (4); Initiator methionine (1); Modified residue (7); Region (3); Turn (1) FUNCTION: May be involved in calcium-dependent ubiquitination and subsequent proteasomal degradation of target proteins. Probably serves as a molecular bridge in ubiquitin E3 complexes. Participates in the ubiquitin-mediated degradation of beta-catenin (CTNNB1) (By similarity). {ECO:0000250}. PTM: Phosphorylated on serine residues. Phosphorylated upon induction by RA or at high calcium concentrations. {ECO:0000269|PubMed:11927578}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11927578}. Cytoplasm {ECO:0000269|PubMed:11927578}. Note=Cytoplasmic in unstimulated cultured neurons. Upon increase of calcium, it localizes to a ring around the nucleus. In neuroblastoma cells, after a Retinoic acid (RA) induction and calcium increase, it localizes in both the nucleus and cytoplasm. The nuclear and perinuclear fractions may be phosphorylated. SUBUNIT: Monomer or homodimer. Component of some large E3 complex at least composed of UBE2D1, SIAH1, CACYBP/SIP, SKP1, APC and TBL1X. Interacts directly with SIAH1, SIAH2 and SKP1 (By similarity). Interacts with proteins of the S100 family S100A1, S100A6, S100B, S100P and S100A12 in a calcium-dependent manner (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in brain and EAT cells. Expressed at low level in heart, muscle, and at very low level in the liver, spleen, lung, kidney and stomach. {ECO:0000269|PubMed:9572262}. +Q3TYS2 CYBC1_MOUSE Cytochrome b-245 chaperone 1 (Essential for reactive oxygen species protein) (Eros) 187 20,921 Chain (1); Modified residue (2); Sequence conflict (1); Transmembrane (1) TRANSMEM 20 42 Helical. {ECO:0000255}. FUNCTION: Necessary for a stable expression of the CYBA and CYBB subunits of the cytochrome b-245 hetrodimer. Controls the phagocyte respiratory burst and is essential for innate immunity. {ECO:0000269|PubMed:28351984}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305|PubMed:28351984}; Single-pass membrane protein {ECO:0000305}. SUBUNIT: Interacts with CYBB; CYBC1 may act as a chaperone stabilizing Cytochrome b-245 heterodimer. {ECO:0000250|UniProtKB:Q9BQA9}. +P62897 CYC_MOUSE Cytochrome c, somatic 105 11,605 Binding site (2); Chain (1); Initiator methionine (1); Metal binding (2); Modified residue (7) FUNCTION: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain. {ECO:0000269|PubMed:12062423}.; FUNCTION: Plays a role in apoptosis. Suppression of the anti-apoptotic members or activation of the pro-apoptotic members of the Bcl-2 family leads to altered mitochondrial membrane permeability resulting in release of cytochrome c into the cytosol. Binding of cytochrome c to Apaf-1 triggers the activation of caspase-9, which then accelerates apoptosis by activating other caspases. {ECO:0000269|PubMed:12062423}. PTM: Binds 1 heme group per subunit.; PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the turnover in the reaction with cytochrome c oxidase, down-regulating mitochondrial respiration. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely associated with the inner membrane. TISSUE SPECIFICITY: Found in embryos and in adult liver and heart. +Q9QXT5 EGFL7_MOUSE Epidermal growth factor-like protein 7 (EGF-like protein 7) (Multiple epidermal growth factor-like domains protein 7) (Multiple EGF-like domains protein 7) (NOTCH4-like protein) (Vascular endothelial statin) (VE-statin) (Zneu1) 275 29,765 Alternative sequence (1); Chain (1); Coiled coil (1); Disulfide bond (8); Domain (3); Erroneous initiation (3); Motif (1); Signal peptide (1) FUNCTION: Regulates vascular tubulogenesis in vivo. Inhibits platelet-derived growth factor (PDGF)-BB-induced smooth muscle cell migration and promotes endothelial cell adhesion to the extracellular matrix and angiogenesis. {ECO:0000269|PubMed:14592969, ECO:0000269|PubMed:15085134}. SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000269|PubMed:14592969, ECO:0000269|PubMed:15162510}. SUBUNIT: Interacts with ITGAV/ITGB3 in an RGD-dependent manner, increasing endothelial cell's motility. {ECO:0000250}. TISSUE SPECIFICITY: Expressed specifically by endothelial cells of the highly vascularized organs heart, lung and kidney. {ECO:0000269|PubMed:14592969, ECO:0000269|PubMed:15162510}. +Q4VBE4 EGFLA_MOUSE Pikachurin (EGF-like, fibronectin type-III and laminin G-like domain-containing protein) (Nectican) 1017 110,735 Alternative sequence (1); Chain (1); Disulfide bond (11); Domain (8); Glycosylation (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Involved in both the retinal photoreceptor ribbon synapse formation and physiological functions of visual perception. Necessary for proper bipolar dendritic tip apposition to the photoreceptor ribbon synapse. Promotes matrix assembly and cell adhesiveness. {ECO:0000269|PubMed:18641643, ECO:0000269|PubMed:18757743}. PTM: O-glycosylated; contains chondroitin sulfate and heparan sulfate. {ECO:0000269|PubMed:18757743}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:18641643, ECO:0000269|PubMed:18757743}. Cell junction, synapse {ECO:0000269|PubMed:18641643}. Note=Detected in the synaptic cleft of the ribbon synapse around the postsynaptic terminals of bipolar cells (PubMed:18641643). Colocalizes with BSN, CTBP2 and DAG1 in photoreceptor synaptic terminals (PubMed:18641643). SUBUNIT: Interacts with DAG1 alpha-dystroglycan. {ECO:0000269|PubMed:18641643}. TISSUE SPECIFICITY: Expressed in the outer plexiform layer (first synaptic region) but not in the inner plexiform layer (second synaptic region) of the retina (at protein level). Strongly expressed in the photoreceptor layer of the retina. Moderately expressed in pineal gland and brain. Weakly expressed in lung and ovary. {ECO:0000269|PubMed:18641643}. +Q8R4T1 CYS1_MOUSE Cystin-1 (Cilia-associated protein) 145 15,506 Chain (1); Compositional bias (1); Initiator methionine (1); Lipidation (1); Modified residue (1); Motif (1); Sequence conflict (1) SUBCELLULAR LOCATION: Cell projection, cilium membrane; Lipid-anchor. Cytoplasm, cytoskeleton, cilium axoneme. Note=Localization to cilium is mediated via interaction with UNC119 and UNC119B, which bind to the myristoyl moiety of the N-terminus (By similarity). Expression is enriched in the ciliary axoneme. {ECO:0000250}. SUBUNIT: Interacts (when myristoylated) with UNC119 and UNC119B; interaction is required for localization to cilium. {ECO:0000250}. TISSUE SPECIFICITY: Expressed primarily in the kidney and liver. Expressed at lower levels in the lung, brain and heart. {ECO:0000269|PubMed:11854326}. DISEASE: Note=Defects in Cys1 are a cause of polycystic kidney disease. {ECO:0000269|PubMed:11854326}. +Q9EQP2 EHD4_MOUSE EH domain-containing protein 4 (PAST homolog 2) (mPAST2) 541 61,481 Beta strand (11); Binding site (2); Calcium binding (1); Chain (1); Domain (3); Helix (22); Modified residue (5); Nucleotide binding (1); Region (5); Turn (4) FUNCTION: ATP- and membrane-binding protein that probably controls membrane reorganization/tubulation upon ATP hydrolysis. Plays a role in early endosomal transport. {ECO:0000269|PubMed:15930129}. SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000250|UniProtKB:Q9H223}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Recycling endosome membrane {ECO:0000250|UniProtKB:Q9H223}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:21177873}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. SUBUNIT: Homooligomer, and heterooligomer with EHD1, EHD2 and EHD3. {ECO:0000250|UniProtKB:Q9H223}. DOMAIN: The EH domain interacts with Asn-Pro-Phe (NPF) motifs of target proteins. {ECO:0000250|UniProtKB:Q9WVK4}. +Q61070 EI24_MOUSE Etoposide-induced protein 2.4 (p53-induced gene 8 protein) 340 38,933 Chain (1); Compositional bias (2); Erroneous initiation (4); Initiator methionine (1); Modified residue (7); Region (1); Sequence conflict (3); Transmembrane (5) TRANSMEM 77 97 Helical. {ECO:0000255}.; TRANSMEM 117 137 Helical. {ECO:0000255}.; TRANSMEM 179 199 Helical. {ECO:0000255}.; TRANSMEM 238 255 Helical. {ECO:0000255}.; TRANSMEM 257 277 Helical. {ECO:0000255}. FUNCTION: Acts as a negative growth regulator via p53-mediated apoptosis pathway. Regulates formation of degradative autolysosomes during autophagy (By similarity). {ECO:0000250, ECO:0000269|PubMed:10594026, ECO:0000269|PubMed:15781622}. SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:15781622}; Multi-pass membrane protein {ECO:0000269|PubMed:15781622}. SUBUNIT: Interacts with BCL2. {ECO:0000269|PubMed:15781622}. TISSUE SPECIFICITY: Found in all the examined tissues. High expression was found in liver, skeletal muscle, pancreas, kidney heart and to a lesser extent in brain, placenta and lung. +Q9JMA7 CP341_MOUSE Cytochrome P450 3A41 (EC 1.14.14.1) 504 57,987 Chain (1); Metal binding (1); Sequence conflict (3) SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Microsome membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in liver. Also expressed in the kidneys of female mice, with traces in the stomach, ovary, and heart of female mice and in the testis of male mice. +Q8BLR2 CPNE4_MOUSE Copine-4 (Copine IV) 557 62,408 Chain (1); Domain (3) FUNCTION: Probable calcium-dependent phospholipid-binding protein that may play a role in calcium-mediated intracellular processes. {ECO:0000250|UniProtKB:Q99829}. SUBUNIT: Interacts (via VWFA domain) with ACTB, BCOR, BICD2, CCDC22, CDC42BPB, CEP162, MYCBP2, NONO, PDCD6, PITPNM2, RDX, SKIL, SKT, SPTBN1, UBE2O and WTAP. {ECO:0000250|UniProtKB:Q96A23}. +Q9JKJ9 CP39A_MOUSE 24-hydroxycholesterol 7-alpha-hydroxylase (EC 1.14.14.26) (Cytochrome P450 39A1) (mCYP39A1) (Oxysterol 7-alpha-hydroxylase) 470 53,575 Chain (1); Metal binding (1) FUNCTION: Involved in the bile acid metabolism. Has a preference for 24-hydroxycholesterol, and converts it into a 7-alpha-hydroxylated product. {ECO:0000269|PubMed:10748047}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. TISSUE SPECIFICITY: Liver specific. Hepatic expression is sexually dimorphic (female > male). +Q08AU9 CQ058_MOUSE UPF0450 protein C17orf58 homolog 97 11,284 Chain (1) +Q8R1B5 CPLX3_MOUSE Complexin-3 (Complexin III) (CPX III) 158 17,586 Chain (1); Coiled coil (1); Lipidation (1); Modified residue (1); Propeptide (1) FUNCTION: Positively regulates a late step in synaptic vesicle exocytosis. {ECO:0000269|PubMed:15911881}. PTM: Farnesylation mediates presynaptic targeting. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:15911881}; Lipid-anchor {ECO:0000269|PubMed:15911881}. Cell junction, synapse {ECO:0000269|PubMed:15911881}. Cell membrane {ECO:0000269|PubMed:15911881}; Lipid-anchor {ECO:0000269|PubMed:15911881}. Note=Enriched at the synaptic terminal. SUBUNIT: Binds to the SNARE core complex containing SNAP25, VAMP2 and STX1A. {ECO:0000269|PubMed:15911881}. TISSUE SPECIFICITY: Present in many brain regions, including hippocampus and cerebellum. In the retina, present both at conventional amacrine cell synapses and at photoreceptor ribbon synapses (at protein level). {ECO:0000269|PubMed:15911881}. +Q80WM3 CPLX4_MOUSE Complexin-4 (Complexin IV) (CPX IV) 160 18,351 Chain (1); Lipidation (1); Modified residue (1); Propeptide (1); Sequence conflict (2) FUNCTION: Positively regulates a late step in synaptic vesicle exocytosis. {ECO:0000269|PubMed:15911881}. PTM: Farnesylation mediates presynaptic targeting and is important for function in neurotransmitter release. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:15911881}; Lipid-anchor {ECO:0000269|PubMed:15911881}. Cell junction, synapse {ECO:0000269|PubMed:15911881}. Cell membrane {ECO:0000269|PubMed:15911881}; Lipid-anchor {ECO:0000269|PubMed:15911881}. Note=Enriched at the synaptic terminal. SUBUNIT: Weakly binds to the SNARE core complex containing SNAP25, VAMP2 and STX1A. {ECO:0000269|PubMed:15911881}. TISSUE SPECIFICITY: Present specifically in the retina, at rod photoreceptor ribbon synapses. Not expressed at conventional amacrine cell synapses, nor at cone photoreceptor ribbon synapses (at protein level). {ECO:0000269|PubMed:15911881}. +Q8BQZ5 CPSF4_MOUSE Cleavage and polyadenylation specificity factor subunit 4 (Cleavage and polyadenylation specificity factor 30 kDa subunit) (CPSF 30 kDa subunit) (Clipper homolog) (Clipper/CPSF 30K) 211 23,653 Alternative sequence (6); Chain (1); Erroneous initiation (2); Modified residue (1); Zinc finger (4) FUNCTION: Component of the cleavage and polyadenylation specificity factor (CPSF) complex that play a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. CPSF4 binds RNA polymers with a preference for poly(U) (By similarity). {ECO:0000250, ECO:0000269|PubMed:9512528}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the cleavage and polyadenylation specificity factor (CPSF) complex, composed of CPSF1, CPSF2, CPSF3, CPSF4 and FIP1L1. Interacts with FIP1L1 (By similarity). {ECO:0000250}. +Q91XE9 CR3L3_MOUSE Cyclic AMP-responsive element-binding protein 3-like protein 3 (cAMP-responsive element-binding protein 3-like protein 3) (Transcription factor CREB-H) [Cleaved into: Processed cyclic AMP-responsive element-binding protein 3-like protein 3] 479 52,145 Chain (2); Domain (1); Glycosylation (3); Region (2); Sequence conflict (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 318 338 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 317 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 339 479 Lumenal. {ECO:0000255}. FUNCTION: Transcription factor that may act during endoplasmic reticulum stress by activating unfolded protein response target genes. Activated in response to cAMP stimulation. Binds to the cAMP response element (CRE). Activates transcription through box-B element (By similarity). Activates transcription through CRE. Seems to function synergistically with ATF6. In acute inflammatory response, may activate expression of acute phase response (APR) genes. May be involved in growth suppression. {ECO:0000250, ECO:0000269|PubMed:15800215}. PTM: Following ER stress a fragment containing the cytoplasmic transcription factor domain is released by proteolysis. The cleavage seems to be performed sequentially by site-1 and site-2 proteases (By similarity). {ECO:0000250}.; PTM: N-glycosylation is required for optimal proteolytic activation. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: Processed cyclic AMP-responsive element-binding protein 3-like protein 3: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}. Note=Under ER stress the cleaved N-terminal cytoplasmic domain translocates into the nucleus. {ECO:0000250}. SUBUNIT: Binds DNA as a dimer. Probably homodimerizes. Probably forms a heterodimer with ATF6. Interacts with ATF6 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Exclusively expressed in adult liver. Differentially expressed in cancer cell lines. {ECO:0000269|PubMed:15800215}. +Q8R0K9 E2F4_MOUSE Transcription factor E2F4 (E2F-4) 410 43,833 Chain (1); Compositional bias (2); DNA binding (1); Initiator methionine (1); Modified residue (2); Motif (2); Region (4); Sequence conflict (1) FUNCTION: Transcription activator that binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. The DRTF1/E2F complex functions in the control of cell-cycle progression from G1 to S phase. E2F4 binds with high affinity to RBL1 and RBL2. In some instances can also bind RB1. Specifically required for multiciliate cell differentiation: together with MCIDAS and E2F5, binds and activate genes required for centriole biogenesis. {ECO:0000250|UniProtKB:Q16254, ECO:0000250|UniProtKB:Q6DE14, ECO:0000269|PubMed:17383628}. PTM: Differentially phosphorylated in vivo. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q16254}. SUBUNIT: Component of the DRTF1/E2F transcription factor complex. Binds cooperatively with TFDP1/Dp-1 to E2F sites. The E2F4/TFDP1 dimer interacts preferentially with pocket protein RBL1, which inhibits the E2F transactivation domain. Lower affinity interaction has been found with retinoblastoma protein RB1. Interacts with TRRAP, which probably mediates its interaction with histone acetyltransferase complexes, leading to transcription activation. Interacts with HCFC1. Component of the DREAM complex (also named LINC complex) at least composed of E2F4, E2F5, LIN9, LIN37, LIN52, LIN54, MYBL1, MYBL2, RBL1, RBL2, RBBP4, TFDP1 and TFDP2. The complex exists in quiescent cells where it represses cell cycle-dependent genes. It dissociates in S phase when LIN9, LIN37, LIN52 and LIN54 form a subcomplex that binds to MYBL2. Interacts with PML. Interacts with CEBPA (when phosphorylated) (By similarity). {ECO:0000250|UniProtKB:Q16254}. +Q61597 CRGC_MOUSE Gamma-crystallin C (Gamma-C-crystallin) 174 20,917 Beta strand (15); Chain (1); Domain (4); Helix (4); Modified residue (1); Natural variant (3); Region (1); Turn (4) FUNCTION: Crystallins are the dominant structural components of the vertebrate eye lens. DOMAIN: Has a two-domain beta-structure, folded into four very similar Greek key motifs. +Q8VHL5 CRGN_MOUSE Gamma-crystallin N (Gamma-N-crystallin) 183 21,392 Chain (1); Domain (4); Sequence conflict (1) FUNCTION: Crystallins are the dominant structural components of the vertebrate eye lens (Probable). Plays also an important role for integrity and function of auditory nuclei (PubMed:27517863). {ECO:0000269|PubMed:27517863, ECO:0000305}. SUBUNIT: Monomer. {ECO:0000269|PubMed:15853812}. DOMAIN: Has a two-domain beta-structure, folded into four very similar Greek key motifs. {ECO:0000305}. TISSUE SPECIFICITY: Primordially eye-specific. Present in lens nucleus. In the retina, expression in observed in the outer plexiform layer (containing photoreceptors axons and synapses) and photoreceptor outer segments (at protein level) (PubMed:15853812). Also detected in the auditory hindbrain where it is highly expressed in the medial nucleus of the trapezoid body, but also present in other nuclei of the superior olivary complex (PubMed:27517863). {ECO:0000269|PubMed:15853812, ECO:0000269|PubMed:27517863}. +P04345 CRGA_MOUSE Gamma-crystallin A (Gamma-A-crystallin) (Gamma-crystallin 4) 174 21,149 Chain (1); Domain (4); Region (1) FUNCTION: Crystallins are the dominant structural components of the vertebrate eye lens. DOMAIN: Has a two-domain beta-structure, folded into four very similar Greek key motifs. +P63254 CRIP1_MOUSE Cysteine-rich protein 1 (CRP-1) (Cysteine-rich intestinal protein) (CRIP) 77 8,550 Chain (1); Compositional bias (1); Domain (1); Modified residue (3) FUNCTION: Seems to have a role in zinc absorption and may function as an intracellular zinc transport protein. +Q9DCT8 CRIP2_MOUSE Cysteine-rich protein 2 (CRP-2) (Heart LIM protein) 208 22,727 Chain (1); Compositional bias (2); Domain (2); Modified residue (4) SUBUNIT: Interacts with TGFB1I1. {ECO:0000269|PubMed:15713747}. +Q6Q6R3 CRIP3_MOUSE Cysteine-rich protein 3 (CRP-3) (Thymus LIM protein) (m17TLP) 243 26,915 Alternative sequence (3); Chain (1); Domain (2) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11713292}. TISSUE SPECIFICITY: Expressed specifically by the thymus. {ECO:0000269|PubMed:11713292}. +Q03402 CRIS3_MOUSE Cysteine-rich secretory protein 3 (CRISP-3) (Acidic epididymal glycoprotein 2) (Sperm-coating glycoprotein 2) (SCP 2) 241 27,314 Chain (1); Disulfide bond (5); Domain (2); Glycosylation (3); Signal peptide (1) FUNCTION: This protein is supposed to help spermatozoa undergo functional maturation while they move from the testis to the ductus deferens. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle. Note=Stored in secretory granules of granular convoluted tubules cells. SUBUNIT: Interacts with A1BG (By similarity). Interacts with KNG1 isoform LMW. {ECO:0000250, ECO:0000269|PubMed:15461460}. TISSUE SPECIFICITY: Expressed in submandibular gland. +Q80ZM8 CRLS1_MOUSE Cardiolipin synthase (CMP-forming) (CLS) (EC 2.7.8.41) 303 32,502 Chain (1); Erroneous initiation (1); Transmembrane (5) TRANSMEM 110 130 Helical. {ECO:0000255}.; TRANSMEM 134 154 Helical. {ECO:0000255}.; TRANSMEM 191 213 Helical. {ECO:0000255}.; TRANSMEM 251 271 Helical. {ECO:0000255}.; TRANSMEM 272 290 Helical. {ECO:0000255}. FUNCTION: Catalyzes the synthesis of cardiolipin (CL) (diphosphatidylglycerol) by specifically transferring a phosphatidyl group from CDP-diacylglycerol to phosphatidylglycerol (PG). CL is a key phospholipid in mitochondrial membranes and plays important roles in maintaining the functional integrity and dynamics of mitochondria under both optimal and stress conditions. {ECO:0000250|UniProtKB:Q9UJA2}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +O70318 E41L2_MOUSE Band 4.1-like protein 2 (Generally expressed protein 4.1) (4.1G) 988 109,940 Chain (1); Domain (1); Initiator methionine (1); Modified residue (18); Region (3); Sequence conflict (2) FUNCTION: Required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase. {ECO:0000250|UniProtKB:O43491}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:O43491}. Cell membrane {ECO:0000250|UniProtKB:O43491}. SUBUNIT: Interacts with FCGR1A. Interacts with TRPC4 (By similarity). Interacts (via CTD domain) with FKBP2 (PubMed:9531554). Interacts with NUMA1; this interaction is negatively regulated by CDK1 during metaphase and promotes anaphase-specific localization of NUMA1 in symmetrically dividing cells (By similarity). {ECO:0000250|UniProtKB:O43491, ECO:0000269|PubMed:9531554}. TISSUE SPECIFICITY: Widely expressed. +A2A5I3 CRSPL_MOUSE Peptidase inhibitor R3HDML (Cysteine-rich secretory protein R3HDML) 253 28,269 Chain (1); Domain (1); Glycosylation (2); Propeptide (1); Signal peptide (1) FUNCTION: Putative serine protease inhibitor. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q3U182 CRTC2_MOUSE CREB-regulated transcription coactivator 2 (Transducer of regulated cAMP response element-binding protein 2) (TORC-2) (Transducer of CREB protein 2) 692 73,216 Chain (1); Compositional bias (2); Cross-link (1); Helix (2); Initiator methionine (1); Modified residue (27); Motif (1); Mutagenesis (7); Region (1); Sequence conflict (2); Site (1) FUNCTION: Transcriptional coactivator for CREB1 which activates transcription through both consensus and variant cAMP response element (CRE) sites (PubMed:29211348). Acts as a coactivator, in the SIK/TORC signaling pathway, being active when dephosphorylated (PubMed:29211348). Acts independently of CREB1 'Ser-133' phosphorylation. Enhances the interaction of CREB1 with TAF4. Regulates gluconeogenesis as a component of the LKB1/AMPK/TORC2 signaling pathway. Regulates the expression of specific genes such as the steroidogenic gene, StAR. Potent coactivator of PPARGC1A and inducer of mitochondrial biogenesis in muscle cells (By similarity). {ECO:0000250|UniProtKB:Q53ET0, ECO:0000269|PubMed:16148943, ECO:0000269|PubMed:16308421, ECO:0000269|PubMed:29211348}. PTM: Phosphorylation/dephosphorylation states of Ser-171 are required for regulating transduction of CREB activity (PubMed:29211348). TORCs are inactive when phosphorylated, and active when dephosphorylated at this site (PubMed:29211348). This primary site of phosphorylation, is regulated by cAMP and calcium levels and is dependent on the phosphorylation of SIKs (SIK1 and SIK2) by LKB1 (By similarity). Phosphorylation at Ser-275 by MARK2 is induced under low glucose conditions and dephosphorylated in response to glucose influx (By similarity). Both insulin and AMPK increase this phosphorylation of CRTC2 while glucagon suppresses it (By similarity). Phosphorylation at Ser-275 promotes interaction with 14-3-3 proteins and translocation to the cytoplasm (By similarity). {ECO:0000250|UniProtKB:Q53ET0, ECO:0000269|PubMed:29211348}.; PTM: Asymmetric dimethylation of arginine resisues by PRMT6 enhances the association of CRTC2 with CREB on the promoters of gluconeogenic genes. {ECO:0000269|PubMed:24570487}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16148943, ECO:0000269|PubMed:16308421, ECO:0000269|PubMed:17805301, ECO:0000269|PubMed:29211348}. Nucleus {ECO:0000269|PubMed:16148943, ECO:0000269|PubMed:16308421, ECO:0000269|PubMed:17805301, ECO:0000269|PubMed:29211348}. Note=Translocated from the nucleus to the cytoplasm on interaction of the phosphorylated form with 14-3-3 protein (By similarity). In response to cAMP levels and glucagon, relocated to the nucleus (PubMed:16148943). {ECO:0000250|UniProtKB:Q53ET0, ECO:0000269|PubMed:16148943}. SUBUNIT: Binds, as a tetramer, through its N-terminal region, with the bZIP domain of CREB1. 'Arg-314' in the bZIP domain of CREB1 is essential for this interaction. Interaction, via its C-terminal, with TAF4, enhances recruitment of TAF4 to CREB1 (By similarity). Interacts with PPP3CA/calcineurin alpha, and SIK2 (By similarity). Interacts with 14-3-3 proteins, YWHAB and YWHAG (PubMed:28235073). Interaction with COP1 mediates nuclear export and degradation of CRTC2 (PubMed:17805301). {ECO:0000250|UniProtKB:Q53ET0, ECO:0000269|PubMed:17805301, ECO:0000269|PubMed:28235073}. TISSUE SPECIFICITY: Expressed in the suprachiasmatic nucleus (SCN) of the brain. {ECO:0000269|PubMed:23699513}. +Q149L7 CRTAM_MOUSE Cytotoxic and regulatory T-cell molecule (Class-I MHC-restricted T-cell-associated molecule) (CD antigen CD355) 393 43,907 Alternative sequence (3); Chain (1); Disulfide bond (2); Domain (2); Erroneous initiation (1); Frameshift (1); Glycosylation (2); Sequence conflict (11); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 290 310 Helical. {ECO:0000255}. TOPO_DOM 17 289 Extracellular. {ECO:0000305}.; TOPO_DOM 311 393 Cytoplasmic. {ECO:0000305}. FUNCTION: Interaction with CADM1 promotes natural killer (NK) cell cytotoxicity and interferon-gamma (IFN-gamma) secretion by CD8+ cells in vitro as well as NK cell-mediated rejection of tumors expressing CADM3 in vivo. {ECO:0000250|UniProtKB:O95727, ECO:0000269|PubMed:15811952}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}. SUBUNIT: Interacts with CADM1. {ECO:0000269|PubMed:15781451, ECO:0000269|PubMed:15811952}. TISSUE SPECIFICITY: In the immune system, expression is restricted to activated class-I MHC-restricted cells, including NKT and CD8 cells. Also expressed in spleen, brain and testis. {ECO:0000269|PubMed:10811014, ECO:0000269|PubMed:15811952}. +Q8QZT4 CRUM3_MOUSE Protein crumbs homolog 3 113 11,921 Alternative sequence (1); Chain (1); Glycosylation (1); Motif (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 50 70 Helical. {ECO:0000255}. TOPO_DOM 25 49 Extracellular. {ECO:0000255}.; TOPO_DOM 71 113 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in the establishment of cell polarity in mammalian epithelial cells. Regulates the morphogenesis of tight junctions (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cell junction, tight junction {ECO:0000250}. Note=Localizes primarily to the apical membrane with a small fraction in the upper part of tight junctions of epithelial cells. {ECO:0000250}. SUBUNIT: Interacts with MPP5, PARD6A and PATJ. {ECO:0000250}. DOMAIN: The PDZ-binding motif is involved in the interactions with PARD6A and MPP5. {ECO:0000250}. +P97784 CRY1_MOUSE Cryptochrome-1 606 68,001 Beta strand (7); Binding site (3); Chain (1); Cross-link (5); Domain (1); Helix (24); Modified residue (4); Motif (13); Mutagenesis (26); Nucleotide binding (1); Region (2); Turn (8) FUNCTION: Transcriptional repressor which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, ARNTL/BMAL1, ARNTL2/BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and ARNTL/BMAL1 or ARNTL2/BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-ARNTL/BMAL1|ARNTL2/BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress ARNTL/BMAL1 transcription, respectively. CRY1 and CRY2 have redundant functions but also differential and selective contributions at least in defining the pace of the SCN circadian clock and its circadian transcriptional outputs. More potent transcriptional repressor in cerebellum and liver than CRY2, though more effective in lengthening the period of the SCN oscillator. On its side, CRY2 seems to play a critical role in tuning SCN circadian period by opposing the action of CRY1. With CRY2, is dispensable for circadian rhythm generation but necessary for the development of intercellular networks for rhythm synchrony. Capable of translocating circadian clock core proteins such as PER proteins to the nucleus. Interacts with CLOCK-ARNTL/BMAL1 independently of PER proteins and is found at CLOCK-ARNTL/BMAL1-bound sites, suggesting that CRY may act as a molecular gatekeeper to maintain CLOCK-ARNTL/BMAL1 in a poised and repressed state until the proper time for transcriptional activation. Represses the CLOCK-ARNTL/BMAL1 induced transcription of BHLHE40/DEC1, ATF4, MTA1, KLF10 and NAMPT. May repress circadian target genes expression in collaboration with HDAC1 and HDAC2 through histone deacetylation. Mediates the clock-control activation of ATR and modulates ATR-mediated DNA damage checkpoint. In liver, mediates circadian regulation of cAMP signaling and gluconeogenesis by binding to membrane-coupled G proteins and blocking glucagon-mediated increases in intracellular cAMP concentrations and CREB1 phosphorylation. Inhibits hepatic gluconeogenesis by decreasing nuclear FOXO1 levels that downregulates gluconeogenic gene expression. Besides its role in the maintenance of the circadian clock, is also involved in the regulation of other processes. Represses glucocorticoid receptor NR3C1/GR-induced transcriptional activity by binding to glucocorticoid response elements (GREs). Plays a key role in glucose and lipid metabolism modulation, in part, through the transcriptional regulation of genes involved in these pathways, such as LEP or ACSL4. {ECO:0000269|PubMed:10428031, ECO:0000269|PubMed:15226430, ECO:0000269|PubMed:16478995, ECO:0000269|PubMed:16628007, ECO:0000269|PubMed:17310242, ECO:0000269|PubMed:19129230, ECO:0000269|PubMed:19299583, ECO:0000269|PubMed:20385766, ECO:0000269|PubMed:20852621, ECO:0000269|PubMed:21236481, ECO:0000269|PubMed:21768648, ECO:0000269|PubMed:22170608, ECO:0000269|PubMed:23133559, ECO:0000269|PubMed:23531614, ECO:0000269|PubMed:23575670, ECO:0000269|PubMed:23616524, ECO:0000269|PubMed:23746849, ECO:0000269|PubMed:24089055, ECO:0000269|PubMed:24158435, ECO:0000269|PubMed:24378737, ECO:0000269|PubMed:24385426, ECO:0000269|PubMed:24489120, ECO:0000269|PubMed:29937374}. PTM: Phosphorylation on Ser-247 by MAPK is important for the inhibition of CLOCK-ARNTL/BMAL1-mediated transcriptional activity. Phosphorylation by CSNK1E requires interaction with PER1 or PER2. Phosphorylation at Ser-71 and Ser-280 by AMPK decreases protein stability. Phosphorylation at Ser-588 exhibits a robust circadian rhythm with a peak at CT8, increases protein stability, prevents SCF(FBXL3)-mediated degradation and is antagonized by interaction with PRKDC. {ECO:0000269|PubMed:11875063, ECO:0000269|PubMed:15298678, ECO:0000269|PubMed:19833968, ECO:0000269|PubMed:24158435}.; PTM: Ubiquitinated by the SCF(FBXL3) and SCF(FBXL21) complexes, regulating the balance between degradation and stabilization. The SCF(FBXL3) complex is mainly nuclear and mediates ubiquitination and subsequent degradation of CRY1. In contrast, cytoplasmic SCF(FBXL21) complex-mediated ubiquitination leads to stabilize CRY1 and counteract the activity of the SCF(FBXL3) complex. The SCF(FBXL3) and SCF(FBXL21) complexes probably mediate ubiquitination at different Lys residues. Ubiquitination at Lys-11 and Lys-107 are specifically ubiquitinated by the SCF(FBXL21) complex but not by the SCF(FBXL3) complex. Ubiquitination may be inhibited by PER2. {ECO:0000269|PubMed:11889036, ECO:0000269|PubMed:17462724, ECO:0000269|PubMed:18953409, ECO:0000269|PubMed:23452855, ECO:0000269|PubMed:23452856}.; PTM: Undergoes autophagy-mediated degradation in the liver in a time-dependent manner. Autophagic degradation of CRY1 (an inhibitor of gluconeogenesis) occurs during periods of reduced feeding allowing induction of gluconeogenesis and maintenance of blood glucose levels. {ECO:0000269|PubMed:29937374}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000269|PubMed:19129230}. Note=Transloctaed to the nucleus through interaction with other clock proteins such as PER2 or ARNTL/BMAL1. SUBUNIT: Component of the circadian core oscillator, which includes the CRY proteins, CLOCK or NPAS2, ARNTL/BMAL1 or ARNTL2/BMAL2, CSNK1D and/or CSNK1E, TIMELESS, and the PER proteins. Interacts directly with TIMELESS. Interacts directly with PER1 and PER2 C-terminal domains. Interaction with PER2 inhibits its ubiquitination and vice versa. Interacts with FBXL21. Interacts with FBXL3. Interacts with PPP5C (via TPR repeats). Interacts with the CLOCK-ARNTL/BMAL1 independently of PER2 and DNA. Interacts with HDAC1, HDAC2 and SIN3B. Interacts with nuclear receptors AR, NR1D1, NR3C1/GR, RORA and RORC; the interaction with at least NR3C1/GR is ligand dependent. Interacts with PRKDC. Interacts with the G protein subunit alpha GNAS; the interaction may block GPCR-mediated regulation of cAMP concentrations. Interacts with PRMT5. Interacts with EZH2. Interacts with MYBBP1A, DOCK7, HNRNPU, RPL7A, RPL8 and RPS3. Interacts with MAP1LC3B (PubMed:29937374). {ECO:0000269|PubMed:10428031, ECO:0000269|PubMed:11875063, ECO:0000269|PubMed:11889036, ECO:0000269|PubMed:14701732, ECO:0000269|PubMed:15226430, ECO:0000269|PubMed:16478995, ECO:0000269|PubMed:16717091, ECO:0000269|PubMed:17462724, ECO:0000269|PubMed:18953409, ECO:0000269|PubMed:19129230, ECO:0000269|PubMed:19917250, ECO:0000269|PubMed:20159955, ECO:0000269|PubMed:21613214, ECO:0000269|PubMed:22170608, ECO:0000269|PubMed:23133559, ECO:0000269|PubMed:23418588, ECO:0000269|PubMed:23452855, ECO:0000269|PubMed:23452856, ECO:0000269|PubMed:23746849, ECO:0000269|PubMed:24158435, ECO:0000269|PubMed:24489120, ECO:0000269|PubMed:29937374}. DOMAIN: The LIR motifs (LC3-interacting region) 3 and 5 are required for its interaction with MAP1LC3B and for its autophagy-mediated degradation. {ECO:0000269|PubMed:29937374}. TISSUE SPECIFICITY: Expressed in all tissues examined including heart, brain, spleen, lung, liver, skeletal muscle, kidney and testis. Higher levels in brain, liver and testis. In the retina, highly expressed in the ganglion cell layer (GCL) and in the inner nuclear layer (INL). Evenly distributed in central and peripheral retina. In the brain, highly expressed in the suprachiasmatic nucleus (SCN). High levels in cerebral cortical layers particularly in the pyramidial cell layer of the hippocampus, the granular cell layer of the dentate gyrus (DG) and the pyramidal cell layer of the piriform cortex (PFC). {ECO:0000269|PubMed:10428031, ECO:0000269|PubMed:10521578, ECO:0000269|PubMed:16790549, ECO:0000269|PubMed:9600923, ECO:0000269|PubMed:9801304}. +Q9QXT8 CSEN_MOUSE Calsenilin (A-type potassium channel modulatory protein 3) (DRE-antagonist modulator) (DREAM) (Kv channel-interacting protein 3) (KChIP3) 256 29,463 Alternative sequence (2); Beta strand (3); Calcium binding (2); Chain (1); Cross-link (2); Domain (4); Helix (10); Lipidation (2); Modified residue (2); Mutagenesis (2); Natural variant (1); Region (1); Sequence conflict (1) FUNCTION: Calcium-dependent transcriptional repressor that binds to the DRE element of genes including PDYN and FOS. Affinity for DNA is reduced upon binding to calcium and enhanced by binding to magnesium. Seems to be involved in nociception. {ECO:0000269|PubMed:11792319, ECO:0000269|PubMed:14534243}.; FUNCTION: Regulatory subunit of Kv4/D (Shal)-type voltage-gated rapidly inactivating A-type potassium channels, such as KCND2/Kv4.2 and KCND3/Kv4.3. Modulates channel expression at the cell membrane, gating characteristics, inactivation kinetics and rate of recovery from inactivation in a calcium-dependent and isoform-specific manner. {ECO:0000269|PubMed:20943905, ECO:0000269|PubMed:22311982}.; FUNCTION: May play a role in the regulation of PSEN2 proteolytic processing and apoptosis. Together with PSEN2 involved in modulation of amyloid-beta formation (By similarity). {ECO:0000250|UniProtKB:Q9Y2W7}. PTM: Palmitoylated. Palmitoylation enhances association with the plasma membrane (By similarity). {ECO:0000250}.; PTM: Proteolytically cleaved by caspase-3. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22311982}. Cell membrane {ECO:0000250|UniProtKB:Q9Y2W7}; Lipid-anchor. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9Y2W7}. Golgi apparatus {ECO:0000250|UniProtKB:Q9Y2W7}. Nucleus {ECO:0000250|UniProtKB:Q9Y2W7}. Note=The sumoylated form is present only in the nucleus. In the presence of PSEN2, associated with the endoplasmic reticulum and Golgi. {ECO:0000250|UniProtKB:Q9Y2W7}. SUBUNIT: Binds to DNA as a homomultimer. Dimerization is induced by binding to calcium (PubMed:18201103). Interacts with the C-terminus of PSEN1 and PSEN2 and with PSEN2 CTF subunit. Associates with KCN1. Component of heteromultimeric potassium channels (PubMed:19713751). Identified in potassium channel complexes containing KCND1, KCND2, KCND3, KCNIP1, KCNIP2, KCNIP3, KCNIP4, DPP6 and DPP10 (PubMed:19713751). Interacts with KCND2 and KCND3 (PubMed:11598014, PubMed:12451113, PubMed:20943905). {ECO:0000269|PubMed:11598014, ECO:0000269|PubMed:12451113, ECO:0000269|PubMed:15746104, ECO:0000269|PubMed:18201103, ECO:0000269|PubMed:20943905, ECO:0000305}. TISSUE SPECIFICITY: Highly expressed in brain. Isoform 1 or isoform 4 (T+ forms) are expressed at equal levels with isoform 2 or isoform 3 (T- forms). Primarily detected in the layer V and deep layer VI of the cerebral cortex, the hippocampus, and the entire cerebellum. Expressed at low levels in testis. Also expressed in heart. {ECO:0000269|PubMed:10676964, ECO:0000269|PubMed:11161465, ECO:0000269|PubMed:12646414, ECO:0000269|PubMed:15363885}. +P0C092 CSEN4_MOUSE Calsenilin isoform 4 89 9,471 Chain (1) FUNCTION: Unknown for isoform 4. Csen is involved in calcium-dependent transcriptional repression, regulation of potassium channels, and perhaps in processing of PSEN2 and apoptosis. TISSUE SPECIFICITY: Isoform 1 or isoform 4 (T+ forms) are expressed at equal levels with isoform 2 or isoform 3 (T- forms) in brain. {ECO:0000269|PubMed:11161465}. +P09581 CSF1R_MOUSE Macrophage colony-stimulating factor 1 receptor (CSF-1 receptor) (CSF-1-R) (CSF-1R) (M-CSF-R) (EC 2.7.10.1) (Proto-oncogene c-Fms) (CD antigen CD115) 977 109,179 Active site (1); Beta strand (28); Binding site (1); Chain (1); Disulfide bond (4); Domain (6); Glycosylation (9); Helix (4); Modified residue (9); Mutagenesis (10); Nucleotide binding (1); Region (2); Sequence conflict (11); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 516 536 Helical. {ECO:0000255}. TOPO_DOM 20 515 Extracellular. {ECO:0000255}.; TOPO_DOM 537 977 Cytoplasmic. {ECO:0000255}. FUNCTION: Tyrosine-protein kinase that acts as cell-surface receptor for CSF1 and IL34 and plays an essential role in the regulation of survival, proliferation and differentiation of hematopoietic precursor cells, especially mononuclear phagocytes, such as macrophages and monocytes. Promotes the release of proinflammatory chemokines in response to IL34 and CSF1, and thereby plays an important role in innate immunity and in inflammatory processes. Plays an important role in the regulation of osteoclast proliferation and differentiation, the regulation of bone resorption, and is required for normal bone and tooth development. Required for normal male and female fertility, and for normal development of milk ducts and acinar structures in the mammary gland during pregnancy. Promotes reorganization of the actin cytoskeleton, regulates formation of membrane ruffles, cell adhesion and cell migration, and promotes cancer cell invasion. Activates several signaling pathways in response to ligand binding. Phosphorylates PIK3R1, PLCG2, GRB2, SLA2 and CBL. Activation of PLCG2 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate, that then lead to the activation of protein kinase C family members, especially PRKCD. Phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, leads to activation of the AKT1 signaling pathway. Activated CSF1R also mediates activation of the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1, and of the SRC family kinases SRC, FYN and YES1. Activated CSF1R transmits signals both via proteins that directly interact with phosphorylated tyrosine residues in its intracellular domain, or via adapter proteins, such as GRB2. Promotes activation of STAT family members STAT3, STAT5A and/or STAT5B. Promotes tyrosine phosphorylation of SHC1 and INPP5D/SHIP-1. Receptor signaling is down-regulated by protein phosphatases, such as INPP5D/SHIP-1, that dephosphorylate the receptor and its downstream effectors, and by rapid internalization of the activated receptor. {ECO:0000269|PubMed:10958675, ECO:0000269|PubMed:11756160, ECO:0000269|PubMed:1652061, ECO:0000269|PubMed:16950670, ECO:0000269|PubMed:17353186, ECO:0000269|PubMed:17420255, ECO:0000269|PubMed:17420256, ECO:0000269|PubMed:17972959, ECO:0000269|PubMed:18814279, ECO:0000269|PubMed:20181277, ECO:0000269|PubMed:20504948, ECO:0000269|PubMed:21610095, ECO:0000269|PubMed:21727904, ECO:0000269|PubMed:8007983, ECO:0000269|PubMed:8262059, ECO:0000269|PubMed:9312046}. PTM: Autophosphorylated in response to CSF1 or IL34 binding. Phosphorylation at Tyr-559 is important for normal down-regulation of signaling by ubiquitination, internalization and degradation. Phosphorylation at Tyr-559 and Tyr-807 is important for interaction with SRC family members, including FYN, YES1 and SRC, and for subsequent activation of these protein kinases. Phosphorylation at Tyr-697 and Tyr-921 is important for interaction with GRB2. Phosphorylation at Tyr-721 is important for interaction with PIK3R1. Phosphorylation at Tyr-721 and Tyr-807 is important for interaction with PLCG2. Phosphorylation at Tyr-974 is important for interaction with CBL. Dephosphorylation by PTPN2 negatively regulates downstream signaling and macrophage differentiation. {ECO:0000269|PubMed:11850825, ECO:0000269|PubMed:15297464, ECO:0000269|PubMed:1652061, ECO:0000269|PubMed:17420255, ECO:0000269|PubMed:20504948, ECO:0000269|PubMed:2160591, ECO:0000269|PubMed:21610095, ECO:0000269|PubMed:8007983, ECO:0000269|PubMed:8262059}.; PTM: Ubiquitinated. Becomes rapidly polyubiquitinated after autophosphorylation, leading to its degradation. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17353186, ECO:0000269|PubMed:8007983}; Single-pass type I membrane protein {ECO:0000269|PubMed:17353186, ECO:0000269|PubMed:8007983}. Note=The autophosphorylated receptor is ubiquitinated and internalized, leading to its degradation. SUBUNIT: Monomer. Homodimer. Interacts with CSF1 and IL34. Interaction with dimeric CSF1 or IL34 leads to receptor homodimerization. Interacts with INPPL1/SHIP2 and THOC5. Interacts (tyrosine phosphorylated) with PLCG2 (via SH2 domain). Interacts (tyrosine phosphorylated) with PIK3R1 (via SH2 domain). Interacts (tyrosine phosphorylated) with FYN, YES1 and SRC (via SH2 domain). Interacts (tyrosine phosphorylated) with CBL, GRB2 and SLA2. {ECO:0000269|PubMed:10597251, ECO:0000269|PubMed:11850825, ECO:0000269|PubMed:15557176, ECO:0000269|PubMed:1652061, ECO:0000269|PubMed:17353186, ECO:0000269|PubMed:19017797, ECO:0000269|PubMed:21610095, ECO:0000269|PubMed:8007983, ECO:0000269|PubMed:8262059, ECO:0000269|PubMed:9312046}. DOMAIN: The juxtamembrane domain functions as autoinhibitory region. Phosphorylation of tyrosine residues in this region leads to a conformation change and activation of the kinase (By similarity). {ECO:0000250}.; DOMAIN: The activation loop plays an important role in the regulation of kinase activity. Phosphorylation of tyrosine residues in this region leads to a conformation change and activation of the kinase (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:20504948}. +Q91ZD6 EAF2_MOUSE ELL-associated factor 2 (Ehrlich S-II transcriptional activator factor) (Testosterone-regulated apoptosis inducer and tumor suppressor protein) 262 29,187 Alternative sequence (1); Chain (1); Compositional bias (2); Erroneous initiation (2); Modified residue (3); Region (3) FUNCTION: Acts as a transcriptional transactivator of ELL and ELL2 elongation activities (By similarity). Acts as a transcriptional transactivator of TCEA1 elongation activity. {ECO:0000250, ECO:0000269|PubMed:12761297}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q96CJ1}. SUBUNIT: Component of the super elongation complex (SEC), at least composed of EAF1, EAF2, CDK9, MLLT3/AF9, AFF (AFF1 or AFF4), the P-TEFb complex and ELL (ELL, ELL2 or ELL3). Interacts with ELL and ELL2 (By similarity). Isoform 1 and isoform 2 interact with TCEA1. {ECO:0000250, ECO:0000269|PubMed:12761297}. TISSUE SPECIFICITY: Isoform 1 is expressed in ovary, uterus, mammary glands, brain, spleen, liver, lung, thymus, kidney, skeletal muscle, skin and testis. Isoform 2 is expressed in kidney. {ECO:0000269|PubMed:12761297, ECO:0000269|PubMed:14517999}. +P40223 CSF3R_MOUSE Granulocyte colony-stimulating factor receptor (G-CSF receptor) (G-CSF-R) (CD antigen CD114) 837 93,379 Beta strand (17); Chain (1); Disulfide bond (7); Domain (6); Glycosylation (11); Helix (4); Motif (2); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 627 650 Helical. {ECO:0000255}. TOPO_DOM 26 626 Extracellular. {ECO:0000255}.; TOPO_DOM 651 837 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for granulocyte colony-stimulating factor (CSF3). In addition it may function in some adhesion or recognition events at the cell surface. PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q99062}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Homodimer. The dimeric receptor binds two CSF3 molecules. Interacts with CEACAM1; down-regulates the CSF3R-STAT3 pathway through recruitment of PTPN6 that dephosphorylates CSF3R (PubMed:21029969). {ECO:0000269|PubMed:10537111, ECO:0000269|PubMed:21029969}. DOMAIN: The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.; DOMAIN: The box 1 motif is required for JAK interaction and/or activation. TISSUE SPECIFICITY: Found in bone marrow. +P09920 CSF3_MOUSE Granulocyte colony-stimulating factor (G-CSF) 208 22,421 Chain (1); Disulfide bond (2); Glycosylation (1); Signal peptide (1) FUNCTION: Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This CSF induces granulocytes. PTM: O-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Monomer. +Q2VPQ9 EAF6_MOUSE Chromatin modification-related protein MEAF6 (MYST/Esa1-associated factor 6) (Esa1-associated factor 6 homolog) (Protein EAF6 homolog) 191 21,649 Alternative sequence (1); Chain (1); Coiled coil (1); Cross-link (3); Initiator methionine (1); Modified residue (7) FUNCTION: Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histone H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. Component of the HBO1 complex which has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3 and is responsible for the bulk of histone H4 acetylation in vivo. Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9HAF1}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q9HAF1}. SUBUNIT: Component of the NuA4 histone acetyltransferase complex which contains the catalytic subunit KAT5 and the subunits EP400, TRRAP, BRD8, EPC1, DMAP1, RUVBL1, RUVBL2, ING3, actin, ACTL6A, MORF4L1, MORF4L2, MRGBP, YEATS4, VPS72 and MEAF6. Component of the HBO1 complex composed at least of ING4 or ING5, MYST2/HBO1, MEAF6, and one of JADE1, JADE2 and JADE3. Component of the MOZ/MORF complex composed at least of ING5, KAT6A, KAT6B, MEAF6 and one of BRPF1, BRD1/BRPF2 and BRPF3 (By similarity). {ECO:0000250}. +Q8VHK1 CSKI2_MOUSE Caskin-2 1201 126,779 Chain (1); Compositional bias (1); Domain (3); Erroneous initiation (1); Modified residue (14); Repeat (6); Sequence conflict (10) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: May not bind CASK. +O70589 CSKP_MOUSE Peripheral plasma membrane protein CASK (EC 2.7.11.1) (Calcium/calmodulin-dependent serine protein kinase) 926 105,109 Active site (1); Alternative sequence (5); Binding site (1); Chain (1); Domain (6); Helix (3); Modified residue (7); Nucleotide binding (1); Region (1); Sequence conflict (20) FUNCTION: Multidomain scaffolding protein with a role in synaptic transmembrane protein anchoring and ion channel trafficking. Contributes to neural development and regulation of gene expression via interaction with the transcription factor TBR1. Binds to cell-surface proteins, including amyloid precursor protein, neurexins, and syndecans. May mediate a link between the extracellular matrix and the actin cytoskeleton via its interaction with syndecan and with the actin/spectrin-binding protein 4.1. {ECO:0000269|PubMed:10749215}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. SUBUNIT: Binds WHRN and NRXN1 cytosolic tail. Interacts with CASKIN1, APBA1, LIN7(A/B/C), and L27 domain of DLG1 and isoform 2 of DLG4 (By similarity). CASK and LIN7 form two mutually exclusive tripartite complexes with APBA1 or CASKIN1. Interacts with FCHSD2 (By similarity). Interacts with KIRREL3 (By similarity). Identified in a complex with ACTN4, IQGAP1, MAGI2, NPHS1, SPTAN1 and SPTBN1 (By similarity). Interacts with TSPYL2. Part of a complex containing CASK, TBR1 and TSPYL2. {ECO:0000250, ECO:0000269|PubMed:10749215, ECO:0000269|PubMed:15066269, ECO:0000269|PubMed:15863617}. DOMAIN: The first L27 domain binds DLG1 and the second L27 domain probably binds LIN7. {ECO:0000250}.; DOMAIN: The protein kinase domain mediates the interaction with FCHSD2. {ECO:0000250}. +P67871 CSK2B_MOUSE Casein kinase II subunit beta (CK II beta) (Phosvitin) 215 24,942 Chain (1); Compositional bias (1); Cross-link (1); Initiator methionine (1); Metal binding (4); Modified residue (8); Region (1) FUNCTION: Plays a complex role in regulating the basal catalytic activity of the alpha subunit (By similarity). Participates in Wnt signaling. {ECO:0000250, ECO:0000269|PubMed:10806215, ECO:0000269|PubMed:16818610}. PTM: Phosphorylated by alpha subunit. {ECO:0000250}. SUBUNIT: Tetramer composed of an alpha subunit, an alpha' subunit and two beta subunits. The beta subunit dimerization is mediated by zinc ions. Interacts with CD163. Also component of a CK2-SPT16-SSRP1 complex composed of SSRP1, SUPT16H, CSNK2A1, CSNK2A2 and CSNK2B, the complex associating following UV irradiation (By similarity). Interacts with TCTEX1D3. Interacts with MUSK; mediates phosphorylation of MUSK by CK2. Interacts with FGF1; this interaction is increased in the presence of FIBP, suggesting a possible cooperative interaction between CSNKB and FIBP in binding to FGF1 (By similarity). {ECO:0000250}. +Q6RUT7 CSMT1_MOUSE Protein CCSMST1 136 15,348 Chain (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 81 97 Helical. {ECO:0000255}. TOPO_DOM 16 80 Extracellular. {ECO:0000255}.; TOPO_DOM 98 136 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q3U898 CSN9_MOUSE COP9 signalosome complex subunit 9 57 6,197 Chain (1); Compositional bias (1); Modified residue (1) FUNCTION: Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. Plays a role in cell proliferation. {ECO:0000250|UniProtKB:Q8WXC6}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8WXC6}. Cytoplasm {ECO:0000250|UniProtKB:Q8WXC6}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q8WXC6}. Note=Excluded from the nucleolus. Recruited to the nucleoplasm and chromatin following DNA damage induction. {ECO:0000250|UniProtKB:Q8WXC6}. SUBUNIT: Component of the CSN complex, composed of COPS1/GPS1, COPS2, COPS3, COPS4, COPS5, COPS6, COPS7 (COPS7A or COPS7B), COPS8 and COPS9. In the complex, it interacts directly with COPS3, COPS5 and COPS6. {ECO:0000250|UniProtKB:Q8WXC6}. DOMAIN: The Phe/Asp-rich domain at the C-terminus is necessary for its incorporation into the CSN complex. {ECO:0000250|UniProtKB:Q8WXC6}. +Q9D0P0 EBPL_MOUSE Emopamil-binding protein-like (Emopamil-binding-related protein) 206 23,307 Chain (1); Domain (1); Sequence conflict (3); Transmembrane (4) TRANSMEM 10 30 Helical. {ECO:0000255}.; TRANSMEM 42 62 Helical. {ECO:0000255}.; TRANSMEM 101 121 Helical. {ECO:0000255}.; TRANSMEM 165 185 Helical. {ECO:0000255}. FUNCTION: Does not possess sterol isomerase activity and does not bind sigma ligands. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +Q62059 CSPG2_MOUSE Versican core protein (Chondroitin sulfate proteoglycan core protein 2) (Chondroitin sulfate proteoglycan 2) (Large fibroblast proteoglycan) (PG-M) 3357 366,787 Alternative sequence (4); Chain (1); Disulfide bond (16); Domain (7); Glycosylation (17); Modified residue (2); Region (2); Sequence conflict (3); Signal peptide (1) FUNCTION: May play a role in intercellular signaling and in connecting cells with the extracellular matrix. May take part in the regulation of cell motility, growth and differentiation. Binds hyaluronic acid. PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000250|UniProtKB:P13611}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SUBUNIT: Interacts with FBLN1. {ECO:0000269|PubMed:10400671}. TISSUE SPECIFICITY: Isoform V2 is found only in brain. +Q71M36 CSPG5_MOUSE Chondroitin sulfate proteoglycan 5 (Acidic leucine-rich EGF-like domain-containing brain protein) (Neuroglycan C) 566 60,406 Alternative sequence (3); Chain (1); Disulfide bond (3); Domain (1); Erroneous initiation (2); Glycosylation (13); Modified residue (10); Mutagenesis (2); Region (2); Sequence conflict (5); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 424 444 Helical. {ECO:0000255}. TOPO_DOM 31 423 Extracellular. {ECO:0000255}.; TOPO_DOM 445 566 Cytoplasmic. {ECO:0000255}. FUNCTION: May function as a growth and differentiation factor involved in neuritogenesis. May induce ERBB3 activation. {ECO:0000269|PubMed:15848802}. PTM: N-glycosylated. {ECO:0000250}.; PTM: O-glycosylated; contains chondroitin sulfate glycans. Part-time proteoglycan, expressed in part as a proteoglycan exhibiting chondroitin sulfate glycans and in part as a non-proteoglycan form. The relative amount of both forms depends on tissues and tissues maturation. In the cerebellum the 2 forms coexist while in the cerebrum the proteoglycan form is predominant. {ECO:0000269|PubMed:10617623, ECO:0000269|PubMed:15331613}.; PTM: Phosphorylated; in intracellular and extracellular parts. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10617623}; Single-pass type I membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:10617623}; Single-pass type I membrane protein {ECO:0000305}. Golgi apparatus membrane {ECO:0000269|PubMed:12885772}; Single-pass type I membrane protein {ECO:0000305}. Cell surface {ECO:0000269|PubMed:15331613}. Note=Partially enriched in lipid rafts (By similarity). In neurons, localizes to synaptic junctions. Also detected in the endoplasmic reticulum and the Golgi (PubMed:10617623). {ECO:0000250|UniProtKB:Q9ERQ6, ECO:0000269|PubMed:10617623}. SUBUNIT: Binds TNR and probably TNC (By similarity). Interacts with ERBB3 and GOPC. {ECO:0000250, ECO:0000269|PubMed:11069908}. TISSUE SPECIFICITY: Expressed in olfactory bulb, hippocampus, brain stem, spinal cord, cerebrum and cerebellum. Expressed by Purkinje cells in the cerebellum (at protein level). Expressed in immature and mature cerebellum (isoform 1, isoform 2 and isoform 3). {ECO:0000269|PubMed:10617623, ECO:0000269|PubMed:15331613, ECO:0000269|PubMed:9950058}. +Q9CS74 ECD_MOUSE Protein ecdysoneless homolog 641 71,710 Chain (1); Modified residue (3); Region (3) FUNCTION: Regulator of p53/TP53 stability and function. Inhibits MDM2-mediated degradation of p53/TP53 possibly by cooperating in part with TXNIP. May be involved transcriptional regulation. In vitro has intrinsic transactivation activity enhanced by EP300. May be a transcriptional activator required for the expression of glycolytic genes (By similarity). Involved in regulation of cell cycle progression (PubMed:26711270). Proposed to disrupt Rb-E2F binding leading to transcriptional activation of E2F proteins (PubMed:19640839). The cell cycle -regulating function may depend on its RUVBL1-mediated association with the R2TP complex. May play a role in regulation of pre-mRNA splicing (By similarity). {ECO:0000250|UniProtKB:O95905}. PTM: Phosphorylated predominantly by CK2 on two serine-containing clusters; involved in cell cycle regulation activity. {ECO:0000250|UniProtKB:O95905}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250|UniProtKB:O95905}. SUBUNIT: Interacts with TP53, MDM2, TXNIP. Interacts (phosphorylated) with PIH1D1. Interacts with RUVBL1 mediating the PIH1D1-independent association with the R2TP complex. Interacts with RB1, RBL1 and RBL2; ECD competes with E2F1 for binding to hypophospshorylated RB1. Interacts with EP300. {ECO:0000250|UniProtKB:O95905}. +B2RX88 CSPP1_MOUSE Centrosome and spindle pole associated protein 1 1205 138,312 Alternative sequence (7); Chain (1); Coiled coil (7); Compositional bias (3); Modified residue (4); Sequence conflict (5) FUNCTION: May play a role in cell-cycle-dependent microtubule organization. {ECO:0000250}. PTM: Phosphorylated. Phosphorylation increases in colcemide-treated cells (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:19129481}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:19129481}. Note=Associated with mitotic spindles. {ECO:0000250}. SUBUNIT: Interacts with PLEKHG6. {ECO:0000269|PubMed:19129481}. +Q8BL00 CDHR3_MOUSE Cadherin-related family member 3 (Cadherin-like protein 28) 831 92,084 Chain (1); Domain (6); Glycosylation (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 712 732 Helical. {ECO:0000255}. TOPO_DOM 20 711 Extracellular. {ECO:0000255}.; TOPO_DOM 733 831 Cytoplasmic. {ECO:0000255}. FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6ZTQ4}; Single-pass type I membrane protein {ECO:0000250}. +P49919 CDN1C_MOUSE Cyclin-dependent kinase inhibitor 1C (Cyclin-dependent kinase inhibitor p57) (p57Kip2) 348 37,372 Alternative sequence (1); Chain (1); Compositional bias (2); Modified residue (1); Motif (1); Sequence conflict (1) FUNCTION: Potent tight-binding inhibitor of several G1 cyclin/CDK complexes (cyclin E-CDK2, cyclin D2-CDK4, and cyclin A-CDK2) and, to lesser extent, of the mitotic cyclin B-CDC2. Negative regulator of cell proliferation. May play a role in maintenance of the non-proliferative state throughout life. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with PCNA. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the heart, brain, lung, skeletal muscle, kidney, pancreas and testis. High levels are seen in the placenta while low levels are seen in the liver. +Q64261 CDK6_MOUSE Cyclin-dependent kinase 6 (EC 2.7.11.22) (CR2 protein kinase) (CRK2) (Cell division protein kinase 6) (Serine/threonine-protein kinase PLSTIRE) 326 37,028 Active site (1); Binding site (1); Chain (1); Domain (1); Modified residue (9); Mutagenesis (2); Natural variant (1); Nucleotide binding (1) FUNCTION: Serine/threonine-protein kinase involved in the control of the cell cycle and differentiation; promotes G1/S transition. Phosphorylates pRB/RB1 and NPM1. Interacts with D-type G1 cyclins during interphase at G1 to form a pRB/RB1 kinase and controls the entrance into the cell cycle. Involved in initiation and maintenance of cell cycle exit during cell differentiation; prevents cell proliferation and regulates negatively cell differentiation, but is required for the proliferation of specific cell types (e.g. erythroid and hematopoietic cells). Essential for cell proliferation within the dentate gyrus of the hippocampus and the subventricular zone of the lateral ventricles. Required during thymocyte development. Promotes the production of newborn neurons, probably by modulating G1 length. Promotes, at least in astrocytes, changes in patterns of gene expression, changes in the actin cytoskeleton including loss of stress fibers, and enhanced motility during cell differentiation. Prevents myeloid differentiation by interfering with RUNX1 and reducing its transcription transactivation activity, but promotes proliferation of normal myeloid progenitors. Delays senescence. Promotes the proliferation of beta-cells in pancreatic islets of Langerhans (By similarity). May play a role in the centrosome organization during the cell cycle phases. {ECO:0000250|UniProtKB:Q00534, ECO:0000269|PubMed:16767702, ECO:0000269|PubMed:21319271, ECO:0000269|PubMed:21508411}. PTM: Thr-177 phosphorylation and Tyr-24 dephosphorylation promotes kinase activity. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q00534}. Nucleus {ECO:0000250|UniProtKB:Q00534}. Cell projection, ruffle {ECO:0000250|UniProtKB:Q00534}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q00534}. Note=Localized to the ruffling edge of spreading fibroblasts. Kinase activity only in nucleus (By similarity). Present in the cytosol and in the nucleus in interphase cells and at the centrosome during mitosis from prophase to telophase (By similarity). Localized to the cytosol of neurons and showed prominent staining around either side of the nucleus. {ECO:0000250|UniProtKB:Q00534, ECO:0000269|PubMed:23918663}. SUBUNIT: Interaction with D-type G1 cyclins. Cyclin binding promotes enzyme activation by phosphorylation at Thr-177 (By similarity). Binds to RUNX1, CDKN2D, FBXO7 and CDKN2C/p18-INK4c. Forms a cytoplasmic complex with Hsp90/HSP90AB1 and CDC37. FBXO7-binding promotes D-type cyclin binding (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in subgranular zone (SGZ) of the hippocampal dentate gyrus (DG) and the subventricular zone (SVZ) of the lateral ventricles whose neural precursor cells (NPC) give rise to dentate granule neurons and olfactory bulb (OB) interneurons, respectively. Expressed in the neuroepithelium of the cerebral cortex of the developing brain. {ECO:0000269|PubMed:21319271, ECO:0000269|PubMed:23918663}. +P18111 CDX1_MOUSE Homeobox protein CDX-1 (Caudal-type homeobox protein 1) 268 28,436 Chain (1); Compositional bias (2); DNA binding (1); Region (2); Sequence conflict (3) FUNCTION: Plays a role in transcriptional regulation. Involved in activated KRAS-mediated transcriptional activation of PRKD1 in colorectal cancer (CRC) cells. Binds to the PRKD1 promoter in colorectal cancer (CRC) cells. Could play a role in the terminal differentiation of the intestine. Binds preferentially to methylated DNA. {ECO:0000250|UniProtKB:P47902}. SUBCELLULAR LOCATION: Nucleus. TISSUE SPECIFICITY: Intestinal epithelium. +P55271 CDN2B_MOUSE Cyclin-dependent kinase 4 inhibitor B (p14-INK4b) (p15-INK4b) 130 13,789 Beta strand (1); Chain (1); Helix (7); Modified residue (1); Repeat (4); Turn (2) FUNCTION: Interacts strongly with CDK4 and CDK6. Potent inhibitor. Potential effector of TGF-beta induced cell cycle arrest (By similarity). {ECO:0000250}. SUBUNIT: Heterodimer of CDKN2B with CDK4 or CDK6. {ECO:0000250}. TISSUE SPECIFICITY: Expressed ubiquitously. +P97377 CDK2_MOUSE Cyclin-dependent kinase 2 (EC 2.7.11.22) (Cell division protein kinase 2) 346 38,978 Active site (1); Alternative sequence (1); Binding site (3); Chain (1); Domain (1); Metal binding (2); Modified residue (7); Mutagenesis (1); Nucleotide binding (3); Site (3) FUNCTION: Serine/threonine-protein kinase involved in the control of the cell cycle; essential for meiosis, but dispensable for mitosis. Phosphorylates CTNNB1, USP37, p53/TP53, NPM1, CDK7, RB1, BRCA2, MYC, NPAT, EZH2. Triggers duplication of centrosomes and DNA. Acts at the G1-S transition to promote the E2F transcriptional program and the initiation of DNA synthesis, and modulates G2 progression; controls the timing of entry into mitosis/meiosis by controlling the subsequent activation of cyclin B/CDK1 by phosphorylation, and coordinates the activation of cyclin B/CDK1 at the centrosome and in the nucleus. Crucial role in orchestrating a fine balance between cellular proliferation, cell death, and DNA repair in human embryonic stem cells (hESCs). Activity of CDK2 is maximal during S phase and G2; activated by interaction with cyclin E during the early stages of DNA synthesis to permit G1-S transition, and subsequently activated by cyclin A2 (cyclin A1 in germ cells) during the late stages of DNA replication to drive the transition from S phase to mitosis, the G2 phase. EZH2 phosphorylation promotes H3K27me3 maintenance and epigenetic gene silencing. Phosphorylates CABLES1 (By similarity). Cyclin E/CDK2 prevents oxidative stress-mediated Ras-induced senescence by phosphorylating MYC. Involved in G1-S phase DNA damage checkpoint that prevents cells with damaged DNA from initiating mitosis; regulates homologous recombination-dependent repair by phosphorylating BRCA2, this phosphorylation is low in S phase when recombination is active, but increases as cells progress towards mitosis. In response to DNA damage, double-strand break repair by homologous recombination a reduction of CDK2-mediated BRCA2 phosphorylation. Phosphorylation of RB1 disturbs its interaction with E2F1. NPM1 phosphorylation by cyclin E/CDK2 promotes its dissociates from unduplicated centrosomes, thus initiating centrosome duplication. Cyclin E/CDK2-mediated phosphorylation of NPAT at G1-S transition and until prophase stimulates the NPAT-mediated activation of histone gene transcription during S phase. Required for vitamin D-mediated growth inhibition by being itself inactivated. Involved in the nitric oxide- (NO) mediated signaling in a nitrosylation/activation-dependent manner. USP37 is activated by phosphorylation and thus triggers G1-S transition. CTNNB1 phosphorylation regulates insulin internalization. Phosphorylates FOXP3 and negatively regulates its transcriptional activity and protein stability (PubMed:23853094). Phosphorylates CDK2AP2 (By similarity). {ECO:0000250|UniProtKB:P24941, ECO:0000269|PubMed:11733001, ECO:0000269|PubMed:12923533, ECO:0000269|PubMed:14561402, ECO:0000269|PubMed:17942597, ECO:0000269|PubMed:23853094}. PTM: Phosphorylated at Thr-160 by CDK7 in a CAK complex. Phosphorylation at Thr-160 promotes kinase activity, whereas phosphorylation at Tyr-15 by WEE1 reduces slightly kinase activity. Phosphorylated on Thr-14 and Tyr-15 during S and G2 phases before being dephosphorylated by CDC25A. {ECO:0000250|UniProtKB:P24941}.; PTM: Nitrosylated after treatment with nitric oxide (DETA-NO). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Nucleus, Cajal body {ECO:0000250}. Cytoplasm {ECO:0000250}. Endosome {ECO:0000250}. Note=Localized at the centrosomes in late G2 phase after separation of the centrosomes but before the start of prophase. Nuclear-cytoplasmic trafficking is mediated during the inhibition by 1,25-(OH)(2)D(3) (By similarity). {ECO:0000250}. SUBUNIT: Found in a complex with CABLES1, CCNA1 and CCNE1. Interacts with CABLES1 (PubMed:11585773). Interacts with UHRF2. Part of a complex consisting of UHRF2, CDK2 and CCNE1. Interacts with the Speedy/Ringo proteins SPDYA and SPDYC. Interaction with SPDYA promotes kinase activation via a conformation change that alleviates obstruction of the substrate-binding cleft by the T-loop. Found in a complex with both SPDYA and CDKN1B/KIP1. Binds to RB1 and CDK7. Binding to CDKN1A (p21) leads to CDK2/cyclin E inactivation at the G1-S phase DNA damage checkpoint, thereby arresting cells at the G1-S transition during DNA repair. Associated with PTPN6 and beta-catenin/CTNNB1. Interacts with CACUL1. May interact with CEP63. Interacts with ANKRD17 (By similarity). Interacts with CEBPA (when phosphorylated) (PubMed:15107404). Forms a ternary complex with CCNA2 and CDKN1B; CDKN1B inhibits the kinase activity of CDK2 through conformational rearrangements. Interacts with cyclins A, B1, B3, D, or E. Interacts with CDK2AP2 (By similarity). {ECO:0000250|UniProtKB:P24941, ECO:0000250|UniProtKB:Q63699, ECO:0000269|PubMed:11585773, ECO:0000269|PubMed:15107404}. +Q6A065 CE170_MOUSE Centrosomal protein of 170 kDa (Cep170) 1588 175,050 Alternative sequence (4); Chain (1); Coiled coil (1); Domain (1); Modified residue (46); Region (2) FUNCTION: Plays a role in microtubule organization. Required for centriole subdistal appendage assembly. {ECO:0000250|UniProtKB:Q5SW79}. PTM: Phosphorylated; probably by PLK1. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:23386061}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q5SW79}. Note=Associated with the mature mother centriole. Associated with spindle microtubules during mitosis (By similarity). Localizes to the distal appendage region of the centriole. {ECO:0000250|UniProtKB:Q5SW79, ECO:0000269|PubMed:23386061}. SUBUNIT: Interacts with CCDC68 and CCDC120; leading to recruitment to centrosomes (By similarity). Interacts with PLK1 (By similarity). Interacts with NIN (PubMed:27565344). Interacts with FHDC1 (PubMed:29742020). {ECO:0000250|UniProtKB:Q5SW79, ECO:0000269|PubMed:27565344, ECO:0000269|PubMed:29742020}. +Q99J95 CDK9_MOUSE Cyclin-dependent kinase 9 (EC 2.7.11.22) (EC 2.7.11.23) (Cell division protein kinase 9) 372 42,762 Active site (1); Alternative sequence (2); Binding site (2); Chain (1); Domain (1); Frameshift (1); Modified residue (11); Nucleotide binding (2); Region (1); Sequence conflict (2) FUNCTION: Protein kinase involved in the regulation of transcription. Member of the cyclin-dependent kinase pair (CDK9/cyclin-T) complex, also called positive transcription elongation factor b (P-TEFb), which facilitates the transition from abortive to productive elongation by phosphorylating the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNAP II) POLR2A, SUPT5H and RDBP. This complex is inactive when in the 7SK snRNP complex form. Phosphorylates EP300, MYOD1, RPB1/POLR2A and AR, and the negative elongation factors DSIF and NELF. Regulates cytokine inducible transcription networks by facilitating promoter recognition of target transcription factors (e.g. TNF-inducible RELA/p65 activation and IL-6-inducible STAT3 signaling). Promotes RNA synthesis in genetic programs for cell growth, differentiation and viral pathogenesis. P-TEFb is also involved in cotranscriptional histone modification, mRNA processing and mRNA export. Modulates a complex network of chromatin modifications including histone H2B monoubiquitination (H2Bub1), H3 lysine 4 trimethylation (H3K4me3) and H3K36me3; integrates phosphorylation during transcription with chromatin modifications to control co-transcriptional histone mRNA processing. The CDK9/cyclin-K complex has also a kinase activity towards CTD of RNAP II and can substitute for CDK9/cyclin-T P-TEFb in vitro. Replication stress response protein; the CDK9/cyclin-K complex is required for genome integrity maintenance, by promoting cell cycle recovery from replication arrest and limiting single-stranded DNA amount in response to replication stress, thus reducing the breakdown of stalled replication forks and avoiding DNA damage. In addition, probable function in DNA repair of isoform 2 via interaction with KU70/XRCC6. Promotes cardiac myocyte enlargement. RPB1/POLR2A phosphorylation on 'Ser-2' in CTD activates transcription. AR phosphorylation modulates AR transcription factor promoter selectivity and cell growth. DSIF and NELF phosphorylation promotes transcription by inhibiting their negative effect. The phosphorylation of MYOD1 enhances its transcriptional activity and thus promotes muscle differentiation (By similarity). {ECO:0000250}. PTM: Autophosphorylation at Thr-186, Ser-347, Thr-350, Ser-353, Thr-354 and Ser-357 triggers kinase activity by promoting cyclin and substrate binding upon conformational changes. Thr-186 phosphorylation requires the calcium Ca(2+) signaling pathway, including CaMK1D and calmodulin. This inhibition is relieved by Thr-29 dephosphorylation. Phosphorylation at Ser-175 inhibits kinase activity. Can be phosphorylated on either Thr-362 or Thr-363 but not on both simultaneously (By similarity). {ECO:0000250}.; PTM: Dephosphorylation of Thr-186 by PPM1A and PPM1B blocks CDK9 activity and may lead to CDK9 proteasomal degradation. However, PPP1CA-mediated Thr-186 dephosphorylation is required to release P-TEFb from its inactive P-TEFb/7SK snRNP complex. Dephosphorylation of C-terminus Thr and Ser residues by protein phosphatase-1 (PP1) triggers CDK9 activity (By similarity). {ECO:0000250}.; PTM: N6-acetylation of Lys-44 by CBP/p300 promotes kinase activity, whereas acetylation of both Lys-44 and Lys-48 mediated by PCAF/KAT2B and GCN5/KAT2A reduces kinase activity. The acetylated form associates with PML bodies in the nuclear matrix; deacetylated upon transcription stimulation (By similarity). {ECO:0000250}.; PTM: Polyubiquitinated and thus activated by UBR5. This ubiquitination is promoted by TFIIS/TCEA1 and favors 'Ser-2' phosphorylation of RPB1/POLR2A CTD (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22767893}. Cytoplasm {ECO:0000250}. Nucleus, PML body {ECO:0000250}. Note=Accumulates on chromatin in response to replication stress. Complexed with CCNT1 in nuclear speckles, but uncomplexed form in the cytoplasm. The translocation from nucleus to cytoplasm is XPO1/CRM1-dependent. Associates with PML body when acetylated (By similarity). {ECO:0000250}. SUBUNIT: Component of the super elongation complex (SEC), at least composed of EAF1, EAF2, CDK9, MLLT3/AF9, AFF (AFF1 or AFF4), the P-TEFb complex and ELL (ELL, ELL2 or ELL3). Associates with CCNT1/cyclin-T1, CCNT2/cyclin-T2 (isoform A and isoform B) or CCNK/cyclin-K to form active P-TEFb. P-TEFb forms a complex with AFF4/AF5Q31 and is part of the super elongation complex (SEC). Component of a complex which is composed of at least 5 members: HTATSF1/Tat-SF1, P-TEFb complex, RNA pol II, SUPT5H, and NCL/nucleolin. Associates with UBR5 and forms a transcription regulatory complex composed of CDK9, RNAP II, UBR5 and TFIIS/TCEA1 that can stimulate target gene transcription (e.g. gamma fibrinogen/FGG) by recruiting their promoters. Component of the 7SK snRNP inactive complex which is composed of at least 8 members: P-TEFb (composed of CDK9 and CCNT1/cyclin-T1), HEXIM1, HEXIM2, LARP7, BCDIN3, SART3 proteins and 7SK and U6 snRNAs. This inactive 7SK snRNP complex can also interact with NCOR1 and HDAC3, probably to regulate CDK9 acetylation. Release of P-TEFb from P-TEFb/7SK snRNP complex requires both PP2B to transduce calcium Ca(2+) signaling in response to stimuli (e.g. UV or hexamethylene bisacetamide (HMBA)), and PPP1CA to dephosphorylate Thr-186. This released P-TEFb remains inactive in the pre-initiation complex with BRD4 until new Thr-186 phosphorylation occurs after the synthesis of a short RNA. Interacts with BRD4, probably to target chromatin binding. Interacts with activated nuclear STAT3 and RELA/p65. Binds to AR and MYOD1. Forms a complex composed of CDK9, CCNT1/cyclin-T1, EP300 and GATA4 that stimulates hypertrophy in cardiomyocytes. The large PER complex involved in the repression of transcriptional termination is composed of at least PER2, CDK9, DDX5, DHX9, NCBP1 and POLR2A (active). Interacts with HSF1 (By similarity). Interacts with TBX21 (PubMed:27292648). {ECO:0000250|UniProtKB:P50750, ECO:0000269|PubMed:22767893, ECO:0000269|PubMed:27292648}. TISSUE SPECIFICITY: Expressed at high levels in brain and kidney. {ECO:0000269|PubMed:9766517}. +P31809 CEAM1_MOUSE Carcinoembryonic antigen-related cell adhesion molecule 1 (Biliary glycoprotein 1) (BGP-1) (Biliary glycoprotein D) (MHVR1) (Murine hepatitis virus receptor) (MHV-R) (CD antigen CD66a) 521 57,016 Alternative sequence (5); Beta strand (17); Chain (1); Disulfide bond (3); Domain (4); Glycosylation (16); Helix (4); Modified residue (3); Mutagenesis (5); Region (5); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 429 447 Helical. {ECO:0000255}. TOPO_DOM 35 428 Extracellular. {ECO:0000255}.; TOPO_DOM 448 521 Cytoplasmic. {ECO:0000255}. FUNCTION: Isoform 1: Cell adhesion protein that mediates homophilic cell adhesion in a calcium-independent manner (By similarity). Plays a role as coinhibitory receptor in immune response, insulin action and functions also as an activator during angiogenesis (PubMed:16680193, PubMed:17081782, PubMed:18544705, PubMed:21029969, PubMed:21081647, PubMed:22496641, PubMed:22962327, PubMed:23696226). Its coinhibitory receptor function is phosphorylation- and PTPN6 -dependent, which in turn, suppress signal transduction of associated receptors by dephosphorylation of their downstream effectors (PubMed:17081782, PubMed:21029969, PubMed:22496641). Plays a role in immune response, of T-cells, natural killer (NK) and neutrophils (PubMed:17081782, PubMed:23696226, PubMed:22496641, PubMed:21029969). Upon TCR/CD3 complex stimulation, inhibits TCR-mediated cytotoxicity by blocking granule exocytosis by mediating homophilic binding to adjacent cells, allowing interaction with and phosphorylation by LCK and interaction with the TCR/CD3 complex which recruits PTPN6 resulting in dephosphorylation of CD247 and ZAP70 (PubMed:22496641). Also inhibits T-cell proliferation and cytokine production through inhibition of JNK cascade and plays a crucial role in regulating autoimmunity and anti-tumor immunity by inhibiting T-cell through its interaction with HAVCR2 (PubMed:17081782). Upon natural killer (NK) cells activation, inhibit KLRK1-mediated cytolysis of CEACAM1-bearing tumor cells by trans-homophilic interactions with CEACAM1 on the target cell and lead to cis-interaction between CEACAM1 and KLRK1, allowing PTPN6 recruitment and then VAV1 dephosphorylation (PubMed:23696226). Upon neutrophils activation negatively regulates IL1B production by recruiting PTPN6 to a SYK-TLR4-CEACAM1 complex, that dephosphorylates SYK, reducing the production of reactive oxygen species (ROS) and lysosome disruption, which in turn, reduces the activity of the inflammasome (PubMed:22496641). Downregulates neutrophil production by acting as a coinhibitory receptor for CSF3R by downregulating the CSF3R-STAT3 pathway through recruitment of PTPN6 that dephosphorylates CSF3R (PubMed:21029969). Also regulates insulin action by promoting INS clearance and regulating lipogenesis in liver through regulating insulin signaling (PubMed:18544705). Upon INS stimulation, undergoes phosphorylation by INSR leading to INS clearance by increasing receptor-mediated insulin endocytosis. This inernalization promotes interaction with FASN leading to receptor-mediated insulin degradation and to reduction of FASN activity leading to negative regulation of fatty acid synthesis. INSR-mediated phosphorylation also provokes a down-regulation of cell proliferation through SHC1 interaction resulting in decrease coupling of SHC1 to the MAPK3/ERK1-MAPK1/ERK2 and phosphatidylinositol 3-kinase pathways (By similarity). Functions as activator in angiogenesis by promoting blood vessel remodeling through endothelial cell differentiation and migration and in arteriogenesis by increasing the number of collateral arteries and collateral vessel calibers after ischemia (PubMed:16680193, PubMed:22962327). Also regulates vascular permeability through the VEGFR2 signaling pathway resulting in control of nitric oxide production (PubMed:21081647). Downregulates cell growth in response to EGF through its interaction with SHC1 that mediates interaction with EGFR resulting in decrease coupling of SHC1 to the MAPK3/ERK1-MAPK1/ERK2 pathway (PubMed:15467833). Negatively regulates platelet aggregation by decreasing platelet adhesion on type I collagen through the GPVI-FcRgamma complex (PubMed:19008452). Inhibits cell migration and cell scattering through interaction with FLNA; interfers with the interaction of FLNA with RALA (By similarity). Mediates bile acid transport activity in a phosphorylation dependent manner (By similarity). Negatively regulates osteoclastogenesis (PubMed:25490771). {ECO:0000250|UniProtKB:P13688, ECO:0000250|UniProtKB:P16573, ECO:0000269|PubMed:15467833, ECO:0000269|PubMed:16680193, ECO:0000269|PubMed:17081782, ECO:0000269|PubMed:18544705, ECO:0000269|PubMed:19008452, ECO:0000269|PubMed:21029969, ECO:0000269|PubMed:21081647, ECO:0000269|PubMed:22496641, ECO:0000269|PubMed:22962327, ECO:0000269|PubMed:23696226, ECO:0000269|PubMed:25490771}.; FUNCTION: Isoform 2: Cell adhesion protein that mediates homophilic cell adhesion in a calcium-independent manner (PubMed:1633107). Promotes populations of T-cells regulating IgA production and secretion associated with control of the commensal microbiota and resistance to enteropathogens (PubMed:23123061). {ECO:0000269|PubMed:1633107, ECO:0000269|PubMed:23123061}.; FUNCTION: (Microbial infection) In case of murine coronavirus (MHV) infection, serves as receptor for MHV S1 spike glycoprotein. {ECO:0000269|PubMed:15331748, ECO:0000269|PubMed:1719235}. PTM: Isoform 1: Phosphorylated on serine and tyrosine (By similarity). Isoform 1 is phosphorylated on tyrosine by Src family kinases like SRC and LCK and by receptor like CSF3R, EGFR and INSR upon stimulation (PubMed:9867848, PubMed:21029969). Phosphorylated at Ser-503; mediates activity. Phosphorylated at Tyr-488; regulates activity (By similarity). Phosphorylated at Tyr-488 by EGFR and INSR upon stimulation; this phosphorylation is Ser-503-phosphorylation-dependent; mediates cellular internalization; increases interaction with FASN (By similarity). Phosphorylated at Tyr-488 and Tyr-515 by LCK; mediates PTPN6 association and is regulated by homophilic ligation of CEACAM1 in the absence of T-cell activation (By similarity). Phosphorylated at Tyr-515; mediates interaction with PTPN11 (PubMed:9867848). {ECO:0000250|UniProtKB:P13688, ECO:0000250|UniProtKB:P16573, ECO:0000269|PubMed:21029969, ECO:0000269|PubMed:9867848}.; PTM: Isoform 2: Phosphorylated on serine and threonine. {ECO:0000250|UniProtKB:P13688, ECO:0000250|UniProtKB:P16573}. SUBCELLULAR LOCATION: Isoform 1: Cell membrane {ECO:0000269|PubMed:19008452, ECO:0000269|PubMed:8380065}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P16573}. Lateral cell membrane {ECO:0000250|UniProtKB:P16573}. Apical cell membrane {ECO:0000250|UniProtKB:P16573}. Basal cell membrane {ECO:0000250|UniProtKB:P16573}. Cell junction {ECO:0000250|UniProtKB:P16573}. Cell junction, adherens junction {ECO:0000250|UniProtKB:P16573}. Note=Canalicular domain of hepatocyte plasma membranes. Found as a mixture of monomer, dimer and oligomer in the plasma membrane. Occurs predominantly as cis-dimers and/or small cis-oligomers in the cell junction regions. Found as dimer in the solution. Predominantly localized to the lateral cell membranes. {ECO:0000250|UniProtKB:P16573}.; SUBCELLULAR LOCATION: Isoform 2: Cell membrane {ECO:0000269|PubMed:1633107, ECO:0000269|PubMed:8380065}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P16573}. Lateral cell membrane {ECO:0000250|UniProtKB:P16573}. Apical cell membrane {ECO:0000250|UniProtKB:P16573}. Basal cell membrane {ECO:0000250|UniProtKB:P16573}. Cell junction {ECO:0000250|UniProtKB:P16573}. Cell junction, adherens junction {ECO:0000250|UniProtKB:P16573}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniProtKB:P13688}. Note=Predominantly localized to the lateral cell membranes. Found as a mixture of monomer, dimer and oligomer in the plasma membrane. Occurs predominantly as cis-dimers and/or small cis-oligomers in the cell junction regions (By similarity). Co-localizes with ANXA2 in secretory vesicles and with S100A10/p11 at the plasma membrane (By similarity). {ECO:0000250|UniProtKB:P13688, ECO:0000250|UniProtKB:P16573}.; SUBCELLULAR LOCATION: Cell projection, microvillus membrane {ECO:0000269|PubMed:25908210}; Single-pass type I membrane protein {ECO:0000305}. Apical cell membrane {ECO:0000269|PubMed:25908210}; Single-pass type I membrane protein {ECO:0000305}. Note=Localized to the apical glycocalyx surface (By similarity). Colocalizes with CEACAM20 at the apical brush border of intestinal cells (PubMed:25908210). {ECO:0000250|UniProtKB:P13688, ECO:0000269|PubMed:25908210}. SUBUNIT: (Microbial infection) Interacts with MHV S1 spike glycoprotein. {ECO:0000269|PubMed:11980704, ECO:0000269|PubMed:1719235, ECO:0000269|PubMed:8380065}.; SUBUNIT: Monomer. Oligomer. Heterodimer. Homodimer (By similarity). Cis-dimer/oligomer (via Ig-like C2-type and/or via cytoplasmic domains); induced by trans-homophilic cell adhesion through an allosteric mechanism transmitted by the Ig-like V-type domain, and is regulated by intracellular calcium and calmodulin. Interacts (via cytoplasmic domain) with calmodulin in a calcium dependent manner; reduces homophilic cell adhesion through dissociation of dimer (By similarity). Isoform 1 interacts (via cytoplasmic domain) with PTPN11 (preferentially) and PTPN6; cis-homodimer form is preferred; this interaction is decreased by formation of isoform 1 / isoform 2 cis-heterodimers and is dependent on the monomer/dimer equilibrium; this interaction is phosphorylation-dependent (PubMed:9867848). Isoform 1 interacts with LYN (PubMed:22496641). Isoform 1 interacts (via cytoplasmic domain) with SRC (via SH2 domain); this interaction is regulated by trans-homophilic cell adhesion (By similarity). Isoform 1 interacts with LCK; mediates phosphorylation at Tyr-488 and Tyr-515 resulting in PTPN6 association. Isoform 1 interacts with PTPN6; this interaction is phosphorylation-dependent and causes a profound decrease in TCR stimulation-induced CD247 and ZAP70 phosphorylation. Isoform 1 interacts with TCR/CD3 complex through TCR beta chain and CD3E; colocalizes at the cell surface and upon stimulation of the TCR/CD3 complex recuits PTPN6 in the TCR/CD3 complex, resulting in dephosphorylation of CD247 and ZAP70 (By similarity). Isoform 1 interacts (via cytoplasmic domain) with SHC1 (via SH2 domain); SHC1 mediates interaction with INSR or EGFR in a Ser-503 phosphorylation-dependent manner (PubMed:15467833). Isoform 1 interacts with EGFR; the interaction is indirect (By similarity). Isoform 1 interacts with CSF3R; down-regulates the CSF3R-STAT3 pathway through recruitment of PTPN6 that dephosphorylates CSF3R (PubMed:21029969). Isoform 1 (phosphorylated form) interacts with TLR4 and SYK; recruits PTPN6 that dephosphorylates SYK, reducing the production of reactive oxygen species (ROS) and lysosome disruption, leading to a reduction of the inflammasome activity (PubMed:22496641). Isoform 1 interacts with FLNA; inhibits cell migration and cell scattering by interfering with the interaction of FLNA with RALA. Isoform 1 interacts (via cytoplasmic domain) with PXN; the interaction is phosphotyrosyl-dependent. Isoform 1 interacts with KLRK1; recruits PTPN6 that dephosphorylates VAV1. Isoform 1 interacts with CEACAM8 (By similarity). Isoform 1 interacts with FASN; this interaction is insulin and phosphorylation-dependent; reduces fatty-acid synthase activity (By similarity). Interacts (via Ig-like V-type) with HAVCR2 (via Ig-like V-type); facilitates the maturation and cell surface expression of HAVCR2 thereby regulating T-cell tolerance induction (By similarity) (PubMed:25363763). Isoform 2 interacts (via the cytoplasmic domain) with ANXA2; this interaction is regulated by phosphorylation and appears in the AIIt complex. Interacts (via Lewis X moieties) with CD209 (via C-type lectin domain); this interaction is regulated by the glycosylation pattern of CEACAM1 on cell types and regulates contact between dendritic cells and neutrophils (By similarity). {ECO:0000250|UniProtKB:P13688, ECO:0000250|UniProtKB:P16573, ECO:0000269|PubMed:15467833, ECO:0000269|PubMed:21029969, ECO:0000269|PubMed:22496641, ECO:0000269|PubMed:25363763, ECO:0000269|PubMed:9867848}. DOMAIN: Ig-like V-type domain mediates trans-homophilic cell adhesion through homodimerization and this active process is regulated by tyrosine kinase, PTPN11 AND PTPN6. Ig-like C2-type and/or cytoplasmic domains mediate cis-dimer/oligomer. {ECO:0000250|UniProtKB:P16573}. TISSUE SPECIFICITY: Expressed in granulocytes, lymphocytes, granulocytes, B cells, and T-cells (PubMed:11994468). Expressed in bone. Highly expressed in liver and femur (PubMed:25490771). Highly expressed in neutrophils, and to a lesser extent inmonocytes, and macrophages. Slightly higher expressed in peripheral blood neutrophils (PBNs) (PubMed:21029969). Intestinal T-cells predominantly express isoform 2 while extraintestinal T-cells mainly express isoform 1 (PubMed:23123061). Expressed in small intestine and colon (PubMed:25908210). {ECO:0000269|PubMed:11994468, ECO:0000269|PubMed:21029969, ECO:0000269|PubMed:23123061, ECO:0000269|PubMed:25490771, ECO:0000269|PubMed:25908210}. +Q8BQ48 CE295_MOUSE Centrosomal protein of 295 kDa 2412 272,779 Alternative sequence (7); Chain (1); Coiled coil (8); Erroneous initiation (3); Modified residue (3); Region (2); Sequence conflict (3) FUNCTION: Centriole-enriched microtubule-binding protein involved in centriole biogenesis. Essential for the generation of the distal portion of new-born centrioles in a CENPJ- and CEP120-mediated elongation dependent manner during the cell cycle S/G2 phase after formation of the initiating cartwheel structure. Required for the recruitment of centriolar proteins, such as POC1B, POC5 and CEP135, into the distal portion of centrioles. Also required for centriole-to-centrosome conversion during mitotic progression, but is dispensable for cartwheel removal or centriole disengagement. Binds to and stabilizes centriolar microtubule. {ECO:0000250|UniProtKB:Q9C0D2}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q9C0D2}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9C0D2}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9C0D2}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9C0D2}. Note=Associates with both of the converted centrioles during G1 but becomes more enriched at the newly formed daughter (or unconverted) centrioles during S, G2, and early M phases. In early S phase, localized at the procentriolar microtubule wall and enriched at the proximal ends of the centrioles in CENPJ- and CEP135-dependent manner. Colocalizes with SASS6 and CEP250 proteins. Colocalizes with CEP135 and CEP192 at the centrosomes. Associates with interphase microtubules and mitotic spindles. Colocalizes with centriolar acetylated tubulin. {ECO:0000250|UniProtKB:Q9C0D2}. SUBUNIT: Interacts (via ALMS motif) with microtubules; this interaction is direct. {ECO:0000250|UniProtKB:Q9C0D2}. DOMAIN: The N-terminal and the ALMS motif-containing C-terminal regions are essential for CEP295-mediated centriole elongation. {ECO:0000250|UniProtKB:Q9C0D2}. +P60334 CDO1_MOUSE Cysteine dioxygenase type 1 (EC 1.13.11.20) (Cysteine dioxygenase type I) (CDO) (CDO-I) 200 23,026 Beta strand (14); Chain (1); Cross-link (1); Helix (5); Metal binding (3); Turn (2) Organosulfur biosynthesis; taurine biosynthesis; hypotaurine from L-cysteine: step 1/2. PTM: The thioether cross-link between Cys-93 and Tyr-157 plays a structural role through stabilizing the Fe(2+) ion, and prevents the production of highly damaging free hydroxyl radicals by holding the oxygen radical via hydroxyl hydrogen. {ECO:0000269|PubMed:16492780}. SUBUNIT: Monomer. {ECO:0000269|PubMed:16492780}. TISSUE SPECIFICITY: Highest expression in liver. Also expressed in kidney, lung, brain and small intestine. {ECO:0000269|PubMed:11602353}. +E9QA28 CEA16_MOUSE Carcinoembryonic antigen-related cell adhesion molecule 16 426 46,352 Chain (1); Disulfide bond (2); Domain (2); Glycosylation (2); Mutagenesis (1); Sequence conflict (2); Signal peptide (1) FUNCTION: Required for proper hearing, it may play a role in maintaining the integrity of the tectorial membrane. {ECO:0000250|UniProtKB:Q2WEN9}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21368133}. Note=Localizes at the tip of cochlear outer hair cells and to the tectorial membrane. {ECO:0000269|PubMed:21368133}. SUBUNIT: Homooligomer; can for homodimers and homotetramers. Interacts with TECTA. {ECO:0000250|UniProtKB:Q2WEN9}. TISSUE SPECIFICITY: Expressed in cochlear outer hair cells (OHC). {ECO:0000269|PubMed:21368133}. +D3Z1D3 CEFIP_MOUSE Cardiac-enriched FHL2-interacting protein 1412 154,478 Chain (1); Modified residue (4) FUNCTION: Plays an important role in cardiomyocyte hypertrophy via activation of the calcineurin/NFAT signaling pathway. {ECO:0000269|PubMed:28717008}. SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:28717008}. SUBUNIT: Interacts with FHL2. {ECO:0000250|UniProtKB:Q711Q0}. TISSUE SPECIFICITY: Expressed in the heart and skeletal muscle (at protein level). {ECO:0000269|PubMed:28717008}. +Q9CQ52 CEL3B_MOUSE Chymotrypsin-like elastase family member 3B (EC 3.4.21.70) (Elastase IIIB) (Elastase-3B) (Protease E) 269 28,905 Active site (3); Chain (1); Disulfide bond (4); Domain (1); Erroneous initiation (1); Propeptide (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Efficient protease with alanine specificity but only little elastolytic activity. {ECO:0000250}. +P28659 CELF1_MOUSE CUGBP Elav-like family member 1 (CELF-1) (50 kDa nuclear polyadenylated RNA-binding protein) (Brain protein F41) (Bruno-like protein 2) (CUG triplet repeat RNA-binding protein 1) (CUG-BP1) (CUG-BP- and ETR-3-like factor 1) (Deadenylation factor CUG-BP) (Deadenylation factor EDEN-BP) (Embryo deadenylation element-binding protein homolog) (EDEN-BP homolog) (RNA-binding protein BRUNOL-2) 486 52,107 Alternative sequence (3); Chain (1); Compositional bias (1); Cross-link (1); Domain (3); Frameshift (1); Modified residue (5); Mutagenesis (1); Sequence conflict (7) FUNCTION: RNA-binding protein implicated in the regulation of several post-transcriptional events. Involved in pre-mRNA alternative splicing, mRNA translation and stability. Mediates exon inclusion and/or exclusion in pre-mRNA that are subject to tissue-specific and developmentally regulated alternative splicing (By similarity). Specifically activates exon 5 inclusion of cardiac isoforms of TNNT2 during heart remodeling at the juvenile to adult transition (By similarity). Acts as both an activator and repressor of a pair of coregulated exons: promotes inclusion of the smooth muscle (SM) exon but exclusion of the non-muscle (NM) exon in actinin pre-mRNAs (By similarity). Activates SM exon 5 inclusion by antagonizing the repressive effect of PTB (By similarity). Promotes exclusion of exon 11 of the INSR pre-mRNA (By similarity). Inhibits, together with HNRNPH1, insulin receptor (IR) pre-mRNA exon 11 inclusion in myoblast (By similarity). Increases translation and controls the choice of translation initiation codon of CEBPB mRNA (By similarity). Increases mRNA translation of CEBPB in aging liver. Increases translation of CDKN1A mRNA by antagonizing the repressive effect of CALR3 (By similarity). Mediates rapid cytoplasmic mRNA deadenylation (By similarity). Recruits the deadenylase PARN to the poly(A) tail of EDEN-containing mRNAs to promote their deadenylation (By similarity). Required for completion of spermatogenesis. Binds to (CUG)n triplet repeats in the 3'-UTR of transcripts such as DMPK and to Bruno response elements (BREs) (By similarity). Binds to muscle-specific splicing enhancer (MSE) intronic sites flanking the alternative exon 5 of TNNT2 pre-mRNA (By similarity). Binds to AU-rich sequences (AREs or EDEN-like) localized in the 3'-UTR of JUN and FOS mRNAs. Binds to the IR RNA (By similarity). Binds to the 5'-region of CDKN1A and CEBPB mRNAs (By similarity). Binds with the 5'-region of CEBPB mRNA in aging liver. May be a specific regulator of miRNA biogenesis. Binds to primary microRNA pri-MIR140 and, with CELF2, negatively regulates the processing to mature miRNA (By similarity). {ECO:0000250|UniProtKB:Q92879, ECO:0000269|PubMed:15082764, ECO:0000269|PubMed:16931514, ECO:0000269|PubMed:17130239}. PTM: Phosphorylated. Phosphorylated by CDK4 on Ser-302. Its phosphorylation status increases in aging liver and is important for the formation of the EIF2 complex and activation of CEBPB mRNA translation. Hyperphosphorylated in the EIF2 complex. EGFR signaling regulates its phosphorylation status in epithelial cells. {ECO:0000269|PubMed:15082764, ECO:0000269|PubMed:16931514}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=RNA-binding activity is detected in both nuclear and cytoplasmic compartments. {ECO:0000250}. SUBUNIT: Associates with polysomes (By similarity). Interacts with HNRNPH1; the interaction in RNA-dependent. Interacts with PARN (By similarity). Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5. {ECO:0000250, ECO:0000269|PubMed:16931514}. DOMAIN: RRM1 and RRM2 domains preferentially target UGU(U/G)-rich mRNA elements. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in skeletal muscle, uterus, diaphragm, lung, spleen, testis, mammary gland, adipose, eye and brain (at protein level). Strongly expressed in aging liver (at protein level). Expressed in lung, stomach, heart to very low levels (at protein level). Expressed in germ cells of the seminiferous tubules except in the central region that contains the elongated spermatids and spermatozoa (at protein level). Expressed in Leydig cells of the interstitial tissue (at protein level). Expressed in the heart, skeletal muscle, testis (from spermatogonia to round spermatids), spleen, lung, neocortex, cerebellar cortex, hippocampus and other areas, abundant in the putamen, and poorly expressed in the thalamus and in the brain stem. {ECO:0000269|PubMed:11158314, ECO:0000269|PubMed:11686919, ECO:0000269|PubMed:15830352, ECO:0000269|PubMed:16931514, ECO:0000269|PubMed:17130239}. +Q9Z0H4 CELF2_MOUSE CUGBP Elav-like family member 2 (CELF-2) (Bruno-like protein 3) (CUG triplet repeat RNA-binding protein 2) (CUG-BP2) (CUG-BP- and ETR-3-like factor 2) (ELAV-type RNA-binding protein 3) (ETR-3) (mETR-3) (Neuroblastoma apoptosis-related RNA-binding protein) (mNapor) (RNA-binding protein BRUNOL-3) 508 54,271 Alternative sequence (7); Chain (1); Compositional bias (1); Domain (3); Erroneous initiation (1); Frameshift (1); Region (2); Sequence conflict (4) FUNCTION: RNA-binding protein implicated in the regulation of several post-transcriptional events. Involved in pre-mRNA alternative splicing, mRNA translation and stability. Mediates exon inclusion and/or exclusion in pre-mRNA that are subject to tissue-specific and developmentally regulated alternative splicing (By similarity). Specifically activates exon 5 inclusion of TNNT2 in embryonic, but not adult, skeletal muscle (By similarity). Activates TNNT2 exon 5 inclusion by antagonizing the repressive effect of PTB (By similarity). Acts as both an activator and repressor of a pair of coregulated exons: promotes inclusion of the smooth muscle (SM) exon but exclusion of the non-muscle (NM) exon in actinin pre-mRNAs (By similarity). Promotes inclusion of exonS 21 and exclusion of exon 5 of the NMDA receptor R1 pre-mRNA (By similarity). Involved in the apoB RNA editing activity (By similarity). Increases COX2 mRNA stability and inhibits COX2 mRNA translation in epithelial cells after radiation injury. Modulates the cellular apoptosis program by regulating COX2-mediated prostaglandin E2 (PGE2) expression. Binds to (CUG)n triplet repeats in the 3'-UTR of transcripts such as DMPK (By similarity). Binds to the muscle-specific splicing enhancer (MSE) intronic sites flanking the TNNT2 alternative exon 5 (By similarity). Binds preferentially to UG-rich sequences, in particular UG repeat and UGUU motifs (By similarity). Binds to apoB mRNA, specifically to AU-rich sequences located immediatly upstream of the edited cytidine (By similarity). Binds AU-rich sequences in the 3'-UTR of COX2 mRNA. Binds to an intronic RNA element responsible for the silencing of exon 21 splicing. Binds to (CUG)n repeats. May be a specific regulator of miRNA biogenesis. Binds to primary microRNA pri-MIR140 and, with CELF1, negatively regulates the processing to mature miRNA (By similarity). {ECO:0000250|UniProtKB:O95319, ECO:0000269|PubMed:12022233, ECO:0000269|PubMed:12535526, ECO:0000269|PubMed:15358864}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Colocalizes with APOBEC1 and A1CF (By similarity). RNA-binding activity is detected in both nuclear and cytoplasmic compartments (By similarity). Accumulates in the cytoplasm after ionizing radiation. {ECO:0000250}. SUBUNIT: Interacts with A1CF. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in tongue, spleen and brain (at protein level). Expressed in liver, thigh, stomach, lung and heart to very low levels (at protein level). Expressed in heart, brain, lung and muscle. {ECO:0000269|PubMed:10524244, ECO:0000269|PubMed:11158314, ECO:0000269|PubMed:15358864, ECO:0000269|PubMed:15830352}. +Q9JKC6 CEND_MOUSE Cell cycle exit and neuronal differentiation protein 1 (BM88 antigen) 149 14,987 Chain (1); Modified residue (3); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 125 145 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 1 124 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 146 149 Extracellular. {ECO:0000255}. FUNCTION: Involved in neuronal differentiation. {ECO:0000269|PubMed:23658157}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}. SUBUNIT: Homodimer (By similarity). Interacts with AHI1 (PubMed:23658157). {ECO:0000250|UniProtKB:Q8N111, ECO:0000269|PubMed:23658157}. TISSUE SPECIFICITY: Expressed in the brain, including hypothalamus, brainstem, and hippocampus. Expression is high in 1-month-old mouse brain and then declines in mature mouse brains at the age of 3 and 7 months. {ECO:0000269|PubMed:23658157}. +Q00322 CEBPD_MOUSE CCAAT/enhancer-binding protein delta (C/EBP delta) (C/EBP-related protein 3) 268 28,631 Chain (1); Cross-link (1); Domain (1); Initiator methionine (1); Modified residue (1); Region (2); Sequence conflict (2) FUNCTION: Transcription activator that recognizes two different DNA motifs: the CCAAT homology common to many promoters and the enhanced core homology common to many enhancers (PubMed:7594592, PubMed:19641492). Important transcription factor regulating the expression of genes involved in immune and inflammatory responses. Transcriptional activator that enhances IL6 transcription alone and as heterodimer with CEBPB (By similarity). {ECO:0000250|UniProtKB:P49716, ECO:0000269|PubMed:19641492, ECO:0000269|PubMed:7594592}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:7594592}. SUBUNIT: Binds DNA as a homodimer and as a heterodimer. Can form stable heterodimers with CEBPA, CEBPB and CEBPE (PubMed:1884998). Interacts with SPI1/PU.1 (PubMed:7594592). Interacts with PRDM16 (PubMed:19641492). {ECO:0000269|PubMed:1884998, ECO:0000269|PubMed:19641492, ECO:0000269|PubMed:7594592}. +Q6PZD9 CEBPE_MOUSE CCAAT/enhancer-binding protein epsilon (C/EBP epsilon) 281 30,617 Chain (1); Cross-link (1); Domain (1); Modified residue (1); Region (2) FUNCTION: Transcriptional activator. C/EBP are DNA-binding proteins that recognize two different motifs: the CCAAT homology common to many promoters and the enhanced core homology common to many enhancers. Required for the promyelocyte-myelocyte transition in myeloid differentiation. {ECO:0000250|UniProtKB:Q15744}. PTM: Phosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}. SUBUNIT: Binds DNA as a homodimer and as a heterodimer. Can form stable heterodimers with CEBPA, CEBPB and CEBPD (By similarity). Interacts with GATA1 AND SPI1 (By similarity). Interacts with SMARCD2 (By similarity). {ECO:0000250|UniProtKB:P56261, ECO:0000250|UniProtKB:Q15744}. +O35216 CENPA_MOUSE Histone H3-like centromeric protein A (Centromere protein A) (CENP-A) 134 15,509 Chain (1); Initiator methionine (1); Modified residue (4); Region (3) FUNCTION: Histone H3-like nucleosomal protein that is specifically found in centromeric nucleosomes. Replaces conventional H3 in the nucleosome core of centromeric chromatin at the inner plate of the kinetochore. The presence of CENPA subtly modifies the nucleosome structure and the way DNA is wrapped around the nucleosome and gives rise to protruding DNA ends that are less well-ordered and rigid compared to nucleosomes containing histone H3. May serve as an epigenetic mark that propagates centromere identity through replication and cell division (By similarity). Required for recruitment and assembly of kinetochore proteins, and as a consequence required for progress through mitosis, chromosome segregation and cytokinesis (PubMed:27499292). {ECO:0000250|UniProtKB:P49450, ECO:0000269|PubMed:27499292}. PTM: Poly-ADP-ribosylated by PARP1.; PTM: Trimethylated by NTMT1 at the N-terminal glycine after cleavage of Met-1. Methylation is low before incorporation into nucleosomes and increases with cell cycle progression, with the highest levels in mitotic nucleosomes. {ECO:0000250|UniProtKB:P49450}.; PTM: Phosphorylated by CDK1 at Ser-62 during early mitosis; this abolishes association with chromatin and centromeres, prevents interaction with HJURP and thereby prevents premature assembly of CENPA into centromeres. Dephosphorylated at Ser-62 by PPP1CA during late mitosis. {ECO:0000250|UniProtKB:P49450}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P49450}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:P49450}. Chromosome, centromere {ECO:0000250|UniProtKB:P49450}. Note=Localizes exclusively in the kinetochore domain of centromeres. Occupies a compact domain at the inner kinetochore plate stretching across 2 thirds of the length of the constriction but encompassing only one third of the constriction width and height. Phosphorylation at Ser-62 during early mitosis abolishes association with chromatin and centromeres and results in dispersed nuclear location. {ECO:0000250|UniProtKB:P49450}. SUBUNIT: Component of centromeric nucleosomes, where DNA is wrapped around a histone octamer core. The octamer contains two molecules each of H2A, H2B, CENPA and H4 assembled in one CENPA-H4 heterotetramer and two H2A-H2B heterodimers. CENPA modulates the DNA-binding characteristics of nucleosomes so that protruding DNA ends have higher flexibility than in nucleosomes containing conventional histone H3. Inhibits binding of histone H1 to nucleosomes, since histone H1 binds preferentially to rigid DNA linkers that protrude from nucleosomes. Nucleosomes containing CENPA also contain histone H2A variants such as macroH2A H2AFY and H2A.Z/H2AFZ. The CENPA-H4 heterotetramer is more compact and structurally more rigid than corresponding H3-H4 heterotetramers. Can assemble into nucleosomes that contain both CENPA and histone H3.3; these nucleosomes interact with a single CENPC chain. Heterotrimer composed of HJURP, CENPA and histone H4, where HJURP interacts with the dimer formed by CENPA and histone H4 and prevents tetramerization of CENPA and H4. Component of the CENPA-NAC complex, at least composed of CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and CENPU. Interacts (via CATD domain) with HJURP; the interaction is direct and is required for its localization to centromeres. Interacts with CENPC, CENPN and CENPT; interaction is direct. Part of a centromere complex consisting of CENPA, CENPT and CENPW. Identified in centromere complexes containing histones H2A, H2B and H4, and at least CENPA, CENPB, CENPC, CENPT, CENPN, HJURP, SUPT16H, SSRP1 and RSF1. Can self-associate. The CENPA-H4 heterotetramer can bind DNA by itself (in vitro). Interacts with CDK1, PPP1CA and RBBP7. {ECO:0000250|UniProtKB:P49450}. DOMAIN: The CATD (CENPA targeting domain) region is responsible for the more compact structure of nucleosomes containing CENPA. It is necessary and sufficient to mediate the localization into centromeres. {ECO:0000250|UniProtKB:P49450}. +Q5SS90 CG057_MOUSE Uncharacterized protein C7orf57 homolog 291 32,895 Chain (1); Modified residue (1) +Q8CEL2 CFA61_MOUSE Cilia- and flagella-associated protein 61 1252 143,289 Alternative sequence (2); Chain (1); Frameshift (1); Sequence conflict (5) FUNCTION: May regulate cilium motility through its role in the assembly of the axonemal radial spokes. {ECO:0000250|UniProtKB:A8IF44, ECO:0000250|UniProtKB:Q23F13}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:A8IF44}. +Q6AW69 CGNL1_MOUSE Cingulin-like protein 1 (Junction-associated coiled-coil protein) 1298 148,231 Alternative sequence (4); Chain (1); Coiled coil (1); Compositional bias (2); Modified residue (11); Motif (1); Region (2); Sequence conflict (4) FUNCTION: May be involved in anchoring the apical junctional complex, especially tight junctions, to actin-based cytoskeletons. {ECO:0000269|PubMed:15292197}. SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000269|PubMed:15292197}. Note=Localizes to the apical junction complex composed of tight and adherens junctions. In the liver and kidney, it is also found along non-junctional actin filament bundles in addition to the apical junction. {ECO:0000269|PubMed:15292197}. SUBUNIT: Homodimer or oligomer (Probable). Interacts with CD2AP and SH3BP1; probably part of a complex at cell junctions (By similarity). {ECO:0000250|UniProtKB:Q0VF96, ECO:0000305|PubMed:15292197}. DOMAIN: The head region is responsible for both junction and actin filament-based distribution. {ECO:0000269|PubMed:15292197}. TISSUE SPECIFICITY: Widely expressed. Highly expressed in the kidney and lung. {ECO:0000269|PubMed:15292197}. +Q99KU6 CF089_MOUSE Bombesin receptor-activated protein C6orf89 homolog 348 39,486 Chain (1); Erroneous gene model prediction (1); Sequence conflict (3); Topological domain (2); Transmembrane (1) TRANSMEM 59 79 Helical. {ECO:0000255}. TOPO_DOM 1 58 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 80 348 Extracellular. {ECO:0000305}. FUNCTION: Exhibits histone deacetylase (HDAC) enhancer properties. May play a role in cell cycle progression and wound repair of bronchial epithelial cells. {ECO:0000250|UniProtKB:Q6UWU4}. PTM: Glycosylated. {ECO:0000250|UniProtKB:Q6UWU4}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q6UWU4}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q6UWU4}. Cytoplasm {ECO:0000250|UniProtKB:Q6UWU4}. SUBUNIT: Homodimer (By similarity). Interacts with BRS3. Interacts (via N-terminus) with SIN3B. {ECO:0000250|UniProtKB:Q6UWU4}. +Q8C1F4 CGAT2_MOUSE Chondroitin sulfate N-acetylgalactosaminyltransferase 2 (EC 2.4.1.174) (Chondroitin beta-1,4-N-acetylgalactosaminyltransferase 2) (Beta4GalNAcT-2) (GalNAcT-2) 542 62,530 Chain (1); Coiled coil (1); Glycosylation (2); Metal binding (2); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 14 34 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 13 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 35 542 Lumenal. {ECO:0000255}. FUNCTION: Transfers 1,4-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to the non-reducing end of glucuronic acid (GlcUA). Required for addition of the first GalNAc to the core tetrasaccharide linker and for elongation of chondroitin chains (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. +Q91WD4 CG025_MOUSE UPF0415 protein C7orf25 homolog 421 46,541 Chain (1); Frameshift (1); Sequence conflict (2) +Q8BGA7 CG026_MOUSE Uncharacterized protein C7orf26 homolog 448 49,908 Chain (1); Sequence conflict (2) +Q9D7J4 COX20_MOUSE Cytochrome c oxidase assembly protein COX20, mitochondrial 117 13,163 Chain (1); Initiator methionine (1); Modified residue (1); Topological domain (3); Transmembrane (2) TRANSMEM 33 50 Helical. {ECO:0000255}.; TRANSMEM 60 76 Helical. {ECO:0000255}. TOPO_DOM 2 32 Mitochondrial intermembrane. {ECO:0000305}.; TOPO_DOM 51 59 Mitochondrial matrix. {ECO:0000305}.; TOPO_DOM 77 117 Mitochondrial intermembrane. {ECO:0000305}. FUNCTION: Essential for the assembly of the mitochondrial respiratory chain complex IV (CIV), also known as cytochrome c oxidase. Acts as a chaperone in the early steps of cytochrome c oxidase subunit II (MT-CO2/COX2) maturation, stabilizing the newly synthesized protein and presenting it to metallochaperones SCO1/2 which in turn facilitates the incorporation of the mature MT-CO2/COX2 into the assembling CIV holoenzyme. {ECO:0000250|UniProtKB:Q5RI15}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q5RI15}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Found in a complex with TMEM177, COA6, MT-CO2/COX2, COX18, SCO1 and SCO2. Interacts with SCO1, SCO2 and COA6 in a MT-CO2/COX2- and COX18-dependent manner. Interacts with COX18 in a MT-CO2/COX2-dependent manner. Interacts with MT-CO2/COX2 and TMEM177. {ECO:0000250|UniProtKB:Q5RI15}. +Q6XUX1 DUSTY_MOUSE Dual serine/threonine and tyrosine protein kinase (EC 2.7.12.1) (Dusty protein kinase) (Dusty PK) (Receptor-interacting serine/threonine-protein kinase 5) 927 104,901 Active site (1); Alternative sequence (5); Binding site (1); Chain (1); Coiled coil (1); Compositional bias (2); Domain (1); Erroneous initiation (2); Nucleotide binding (1); Sequence conflict (1) FUNCTION: Acts as a positive regulator of ERK phosphorylation downstream of fibroblast growth factor-receptor activation. Involved in the regulation of both caspase-dependent apoptosis and caspase-independent cell death. In the skin, it plays a predominant role in suppressing caspase-dependent apoptosis in response to UV stress in a range of dermal cell types. {ECO:0000250|UniProtKB:Q6XUX3}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23862974}. Cell membrane {ECO:0000269|PubMed:23862974}. Apical cell membrane {ECO:0000269|PubMed:23862974}. Basolateral cell membrane {ECO:0000269|PubMed:23862974}. Cell junction {ECO:0000269|PubMed:23862974}. Note=Detected in basolateral and apical membranes of all tubular epithelia. Detected at apical cell-cell junctions. Colocalized with FGF receptors to the cell membrane. {ECO:0000269|PubMed:23862974}. TISSUE SPECIFICITY: Expressed in brain, heart, skeletal muscle, kidney and lung. Expressed in maturing tubular epithelia, with the most prominent expression in the medulla and the papilla. Expressed in thin ascending limb of the loop of Henle and the distal convoluted tubule. Expressed in all layers of transitional ureteric epithelium and in the ureteric smooth-muscle cells (at protein level). Widely expressed. Highly expressed in many brain regions, including in cerebellum, olfactory, hippocampus and cerebral cortex. {ECO:0000269|PubMed:17123648, ECO:0000269|PubMed:23862974}. +Q8C708 CP054_MOUSE Transmembrane protein C16orf54 homolog 225 24,532 Chain (1); Modified residue (3); Sequence conflict (1); Transmembrane (1) TRANSMEM 32 52 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +P27786 CP17A_MOUSE Steroid 17-alpha-hydroxylase/17,20 lyase (EC 1.14.14.19) (EC 1.14.14.32) (17-alpha-hydroxyprogesterone aldolase) (CYPXVII) (Cytochrome P450 17A1) (Cytochrome P450-C17) (Cytochrome P450c17) 507 57,638 Chain (1); Metal binding (1) Lipid metabolism; steroid biosynthesis. FUNCTION: Conversion of pregnenolone and progesterone to their 17-alpha-hydroxylated products and subsequently to dehydroepiandrosterone (DHEA) and androstenedione. Catalyzes both the 17-alpha-hydroxylation and the 17,20-lyase reaction. Involved in sexual development during fetal life and at puberty. SUBCELLULAR LOCATION: Membrane {ECO:0000305}. +Q62036 CP131_MOUSE Centrosomal protein of 131 kDa (5-azacytidine-induced protein 1) (Pre-acrosome localization protein 1) 1060 120,313 Chain (1); Domain (1); Modified residue (11); Sequence conflict (2) FUNCTION: Component of centriolar satellites contributing to the building of a complex and dynamic network required to regulate cilia/flagellum formation. In proliferating cells, MIB1-mediated ubiquitination induces its sequestration within centriolar satellites, precluding untimely cilia formation initiation. In contrast, during normal and ultraviolet or heat shock cellular stress-induced ciliogenesis, its non-ubiquitinated form is rapidly displaced from centriolar satellites and recruited to centrosome/basal bodies in a microtubule- and p38 MAPK-dependent manner. Acts also as a negative regulator of BBSome ciliary trafficking (By similarity). Plays a role in sperm flagellar formation; may be involved in the regulation of intraflagellar transport (IFT) and/or intramanchette (IMT) trafficking, which are important for axoneme extension and/or cargo delivery to the nascent sperm tail (PubMed:24415959). Required for optimal cell proliferation and cell cycle progression; may play a role in the regulation of genome stability and centriole duplication in non-ciliogenic cells (By similarity). Involved in centriole duplication (PubMed:26297806). Required for CEP152, WDR62 and CEP63 centrosomal localization and promotes the centrosomal localization of CDK2 (By similarity). {ECO:0000250|UniProtKB:Q9UPN4, ECO:0000269|PubMed:24185901, ECO:0000269|PubMed:24415959, ECO:0000269|PubMed:26297806}. PTM: Ubiquitinated. Undergoes monoubiquitination catalyzed by the E3 ubiquitin-protein ligase MIB1 in proliferating cells, preventing cilia formation. Monoubiquitination by MIB1 is inhibited in response to cellular stress, such as ultraviolet light (UV) radiation or heat shock, resulting in ciliogenesis restoration (By similarity). {ECO:0000250|UniProtKB:Q9UPN4}.; PTM: MAPKAPK2-dependent phosphorylation at Ser-47 and Ser-78 occurs in response to cellular stress such as exposure to ultraviolet irradiation and promotes binding to 14-3-3 proteins which leads to cytoplasmic sequestration of CEP131 and blocks formation of new centriolar satellites. {ECO:0000250|UniProtKB:Q9UPN4}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:24415959}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000269|PubMed:24415959}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:24415959}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:24415959}. Note=Ubiquitinated form is sequestered and colocalized with BBS4, CEP290, PCM1 and PCNT at centriolar satellites in proliferating cells. Traffics towards and away from centriolar satellites and centrosome in a microtubule- and dynein-dependent manner in interphase cells. Displaced from centriolar satellites but still remained associated with centrosome in response to cellular stress, such as ultraviolet light (UV) radiation or heat shock, in a process that requires p38 MAPK signaling (By similarity). Colocalized with pericentriolar material protein PCM1 at centriolar satellites. During spermiogenesis, becomes enriched with nephrocystin NPHP1 at the transition zone, a structure at the base of the ciliary axoneme important for regulating traffic into the ciliary compartment. Traffics towards and away from the centrosome/basal bodies and the transition zone of the ciliary axoneme in a microtubule-dependent manner. Localized at the Golgi-derived acrosome and the centrosome-containing head-tail coupling apparatus (HTCA). {ECO:0000250}. SUBUNIT: Self-associates (By similarity). Associates with the centriolar satellite BBSome protein complex (PubMed:24550735) Interacts with BBS4; the interaction limits BBS4 availability for association with the BBSome complex, and hence negatively regulates ciliary localization of the BBSome complex. Interacts with MIB1. Interacts with PCM1; the interaction increases in response to ultraviolet light (UV) radiation. Associates with microtubule; association to microtubule is reduced in response to cellular stress, such as UV stimulation, in a process that requires p38 MAP kinase signaling. Interacts with CEP290, DCTN1, MAP1LC3B, PCNT, PCM1 and CEP152 (By similarity). Interacts with 14-3-3 proteins following UV-induced phosphorylation by MAPKAPK2; this inhibits formation of novel centriolar satellites (By similarity). {ECO:0000250|UniProtKB:Q9UPN4, ECO:0000269|PubMed:24550735}. TISSUE SPECIFICITY: Localized to the pre-acrosome region of round and elongated spermatids in testis but also present in ovary, brain and adipose tissue. {ECO:0000269|PubMed:8529672}. +Q9CX98 CP2U1_MOUSE Cytochrome P450 2U1 (EC 1.14.14.1) 530 60,578 Alternative sequence (5); Chain (1); Frameshift (1); Metal binding (1); Transmembrane (5) TRANSMEM 21 41 Helical. {ECO:0000255}.; TRANSMEM 99 119 Helical. {ECO:0000255}.; TRANSMEM 247 267 Helical. {ECO:0000255}.; TRANSMEM 328 348 Helical. {ECO:0000255}.; TRANSMEM 481 501 Helical. {ECO:0000255}. FUNCTION: Catalyzes the hydroxylation of arachidonic acid, docosahexaenoic acid and other long chain fatty acids. May modulate the arachidonic acid signaling pathway and play a role in other fatty acid signaling processes (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Microsome membrane {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15752708}. +Q6XVG2 CP254_MOUSE Cytochrome P450 2C54 (EC 1.14.14.1) (CYPIIC54) 490 55,858 Chain (1); Metal binding (1); Modified residue (3) FUNCTION: Metabolizes arachidonic acid mainly to 12-hydroxyeicosatetraenoic acid (HETE). {ECO:0000269|PubMed:15102943}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15102943}; Peripheral membrane protein {ECO:0000269|PubMed:15102943}. Microsome membrane {ECO:0000269|PubMed:15102943}; Peripheral membrane protein {ECO:0000269|PubMed:15102943}. TISSUE SPECIFICITY: Expressed in liver. {ECO:0000269|PubMed:15102943}. +A2CI98 DYTN_MOUSE Dystrotelin 653 74,059 Chain (1); Coiled coil (1); Zinc finger (1) SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17233888}. TISSUE SPECIFICITY: Strongly expressed in the nervous and muscular tissues. {ECO:0000269|PubMed:17233888}. +O35728 CP4AE_MOUSE Cytochrome P450 4A14 (CYPIVA14) (Cytochrome P450-LA-omega 3) (Lauric acid omega-hydroxylase 3) (Long-chain fatty acid omega-monooxygenase) (EC 1.14.14.80) 507 58,720 Binding site (1); Chain (1); Erroneous termination (1); Metal binding (1); Modified residue (1); Propeptide (1); Sequence conflict (3) FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. {ECO:0000305}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. TISSUE SPECIFICITY: Very low level in liver, kidney and spleen. {ECO:0000269|PubMed:9271096}. +Q9EPU4 CPSF1_MOUSE Cleavage and polyadenylation specificity factor subunit 1 (Cleavage and polyadenylation specificity factor 160 kDa subunit) (CPSF 160 kDa subunit) 1441 160,818 Chain (1); Modified residue (2) FUNCTION: Component of the cleavage and polyadenylation specificity factor (CPSF) complex that plays a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. This subunit is involved in the RNA recognition step of the polyadenylation reaction (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}. SUBUNIT: Component of the cleavage and polyadenylation specificity factor (CPSF) complex, composed of CPSF1, CPSF2, CPSF3, CPSF4 and FIP1L1. Found in a complex with CPSF1, FIP1L1 and PAPOLA. Interacts with FIP1L1 and SRRM1. Interacts with TUT1; the interaction is direct and mediates the recruitment of the CPSF complex on the 3'UTR of selected pre-mRNAs (By similarity). Interacts with TENT2/GLD2. {ECO:0000250, ECO:0000269|PubMed:17927953}. +Q8JZW4 CPNE5_MOUSE Copine-5 (Copine V) 593 65,592 Chain (1); Domain (3); Modified residue (3) FUNCTION: Probable calcium-dependent phospholipid-binding protein that may play a role in calcium-mediated intracellular processes. Plays a role in dendrite formation by melanocytes. {ECO:0000250|UniProtKB:Q99829, ECO:0000250|UniProtKB:Q9HCH3}. SUBCELLULAR LOCATION: Perikaryon {ECO:0000269|PubMed:18614158}. Cell projection {ECO:0000269|PubMed:18614158}. TISSUE SPECIFICITY: Expressed in the cerebra and cerebellum of newborn brain. Expressed in the eye, lung and muscles but weakly expressed in the adult brain (at protein level) (PubMed:18614158). {ECO:0000269|PubMed:18614158}. +Q3V3I5 CQ067_MOUSE Uncharacterized protein C17orf67 homolog 90 10,620 Chain (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +P86793 CC21C_MOUSE C-C motif chemokine 21c (6Ckine) (Beta-chemokine exodus-2) (Small-inducible cytokine A21c) (Thymus-derived chemotactic agent 4) (TCA4) 133 14,584 Chain (1); Disulfide bond (3); Region (1); Signal peptide (1) FUNCTION: Inhibits hemopoiesis and stimulates chemotaxis. Chemotactic in vitro for thymocytes and activated T-cells, but not for B-cells, macrophages, or neutrophils. Potent mesangial cell chemoattractant. Shows preferential activity towards naive T-cells. May play a role in mediating homing of lymphocytes to secondary lymphoid organs. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Binds to CCR7 and to CXCR3. Interacts with PDPN; relocalizes PDPN to the basolateral membrane. {ECO:0000250|UniProtKB:O00585}. TISSUE SPECIFICITY: Expressed strongly in lung, spleen, thymus, peripheral and mesentric lymph nodes. Also expressed in the testis, kidney, liver, and heart. +Q8BS39 CCD32_MOUSE Coiled-coil domain-containing protein 32 179 19,928 Alternative sequence (1); Chain (1); Coiled coil (1); Erroneous initiation (1); Sequence conflict (1) +Q9CR92 CCD96_MOUSE Coiled-coil domain-containing protein 96 584 67,256 Chain (1); Coiled coil (2); Compositional bias (1) SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q2M329}. +Q3URS9 CCD51_MOUSE Coiled-coil domain-containing protein 51 406 45,132 Alternative sequence (1); Chain (1); Coiled coil (1); Sequence conflict (1); Transmembrane (2) TRANSMEM 199 219 Helical. {ECO:0000255}.; TRANSMEM 383 403 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9JJV4 CCG4_MOUSE Voltage-dependent calcium channel gamma-4 subunit (Neuronal voltage-gated calcium channel gamma-4 subunit) (Transmembrane AMPAR regulatory protein gamma-4) (TARP gamma-4) 327 36,535 Chain (1); Glycosylation (2); Modified residue (1); Topological domain (5); Transmembrane (4) TRANSMEM 10 30 Helical. {ECO:0000255}.; TRANSMEM 108 128 Helical. {ECO:0000255}.; TRANSMEM 137 157 Helical. {ECO:0000255}.; TRANSMEM 187 207 Helical. {ECO:0000255}. TOPO_DOM 1 9 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 31 107 Extracellular. {ECO:0000255}.; TOPO_DOM 129 136 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 158 186 Extracellular. {ECO:0000255}.; TOPO_DOM 208 327 Cytoplasmic. {ECO:0000255}. FUNCTION: Regulates the activity of L-type calcium channels that contain CACNA1C as pore-forming subunit (By similarity). Regulates the trafficking and gating properties of AMPA-selective glutamate receptors (AMPARs), including GRIA1 and GRIA4. Promotes their targeting to the cell membrane and synapses and modulates their gating properties by slowing their rates of activation, deactivation and desensitization and by mediating their resensitization (PubMed:17880894). {ECO:0000250|UniProtKB:Q9UBN1, ECO:0000269|PubMed:17880894}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11389205}; Multi-pass membrane protein {ECO:0000269|PubMed:11389205}. SUBUNIT: Interacts with CACNA1C. Identified in a complex with the L-type calcium channel subunits CACNA1C, CACNA2D1 and either CACNB1 or CACNB2 (By similarity). Acts as an auxiliary subunit for AMPA-selective glutamate receptors (AMPARs). Interacts with GRIA1 (By similarity). {ECO:0000250|UniProtKB:Q8VHW9, ECO:0000250|UniProtKB:Q9UBN1}. +Q9JIG7 CCD22_MOUSE Coiled-coil domain-containing protein 22 627 70,844 Chain (1); Coiled coil (1); Modified residue (1); Region (2); Sequence conflict (2) FUNCTION: Involved in regulation of NF-kappa-B signaling. Promotes ubiquitination of I-kappa-B-kinase subunit IKBKB and its subsequent proteasomal degradation leading to NF-kappa-B activation; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. May down-regulate NF-kappa-B activity via association with COMMD1 and involving a CUL2-dependent E3 ubiquitin ligase complex. Regulates the cellular localization of COMM domain-containing proteins, such as COMMD1 and COMMD10. Plays a role in copper ion homeostasis. Involved in copper-dependent ATP7A trafficking between the trans-Golgi network and vesicles in the cell periphery; the function is proposed to depend on its association within the CCC complex and cooperation with the WASH complex on early endosomes. SUBCELLULAR LOCATION: Endosome {ECO:0000305}. SUBUNIT: Interacts with CPNE1 and CPNE4 (PubMed:12522145). Interacts with COMMD1, COMMD2 COMMD3, COMMD4, COMMD5, COMMD6, COMMD7, COMMD8, COMMD9, COMMD10. Interacts with CUL1, CUL2, CUL3, SKP1, BTRC. Interacts with CCDC93 and C16orf62 homolog; proposed to be a component of the CCC (COMMD/CCDC22/CCDC93) complex which contains at least COMMD1 (and possibly other COMM domain-containing proteins), CCDC22, CCDC93 and C16orf62 homolog; in the complex interacts directly with CCDC93 (By similarity). {ECO:0000250|UniProtKB:O60826, ECO:0000269|PubMed:12522145}. +Q9D4V3 CCD83_MOUSE Coiled-coil domain-containing protein 83 305 35,642 Alternative sequence (3); Chain (1); Coiled coil (1); Sequence conflict (3) +Q9JJ89 CCD86_MOUSE Coiled-coil domain-containing protein 86 (Cytokine-induced protein with coiled-coil domain) (mCyclon) 426 46,487 Chain (1); Coiled coil (1); Compositional bias (1); Modified residue (15); Sequence conflict (3) PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17300783}. TISSUE SPECIFICITY: Highly expressed in testis. Also expressed in heart, liver, kidney. {ECO:0000269|PubMed:17300783}. +P10146 CCL1_MOUSE C-C motif chemokine 1 (P500) (SIS-epsilon) (Small-inducible cytokine A1) (T-cell activation protein 3) (TCA-3) (TCA3) 92 10,276 Alternative sequence (1); Chain (1); Disulfide bond (3); Glycosylation (1); Natural variant (4); Sequence conflict (1); Signal peptide (1) FUNCTION: Cytokine that is chemotactic for neutrophils. +Q9JJV3 CCGL_MOUSE Voltage-dependent calcium channel gamma-like subunit (Neuronal voltage-gated calcium channel gamma-like subunit) (Transmembrane protein 37) 211 23,230 Chain (1); Transmembrane (4) TRANSMEM 25 45 Helical. {ECO:0000255}.; TRANSMEM 96 116 Helical. {ECO:0000255}.; TRANSMEM 131 151 Helical. {ECO:0000255}.; TRANSMEM 155 175 Helical. {ECO:0000255}. FUNCTION: Thought to stabilize the calcium channel in an inactivated (closed) state (By similarity). Modulates calcium current when coexpressed with CACNA1G. {ECO:0000250, ECO:0000269|PubMed:10734232}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: The L-type calcium channel is composed of five subunits: alpha-1, alpha-2/delta, beta and gamma. {ECO:0000250}. +Q8BVC4 CCD68_MOUSE Coiled-coil domain-containing protein 68 333 37,992 Alternative sequence (1); Chain (1); Coiled coil (2) FUNCTION: Centriolar protein required for centriole subdistal appendage assembly and microtubule anchoring in interphase cells (PubMed:28422092). Together with CCDC120, cooperate with subdistal appendage components ODF2, NIN and CEP170 for hierarchical subdistal appendage assembly (PubMed:28422092). {ECO:0000269|PubMed:28422092}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q9H2F9}. Note=Localizes to the subdistal appendages of centrioles. {ECO:0000250|UniProtKB:Q9H2F9}. SUBUNIT: Interacts with CEP170. {ECO:0000250|UniProtKB:Q9H2F9}. +Q78PG9 CCD25_MOUSE Coiled-coil domain-containing protein 25 208 24,480 Chain (1); Coiled coil (1); Modified residue (2); Sequence conflict (1) +Q8QZT2 CCSAP_MOUSE Centriole, cilia and spindle-associated protein 252 28,379 Chain (1); Frameshift (1); Modified residue (3); Motif (2); Sequence conflict (2) FUNCTION: Plays a role in microtubule (MT) stabilization and this stabilization involves the maintenance of NUMA1 at the spindle poles. Colocalizes with polyglutamylated MTs to promote MT stabilization and regulate bipolar spindle formation in mitosis. Binding of CCSAP to centrosomes and the spindle around centrosomes during mitosis inhibits MT depolymerization, thereby stabilizing the mitotic spindle. May play a role in embryonic development. May be required for proper cilia beating (By similarity). {ECO:0000250|UniProtKB:Q6IQ19, ECO:0000250|UniProtKB:Q6P3G4}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q6IQ19}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q6IQ19}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q6IQ19}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q6IQ19}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q6IQ19}. Cell projection, axon {ECO:0000250|UniProtKB:Q6IQ19}. Cell projection, cilium {ECO:0000250|UniProtKB:Q6IQ19}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q6IQ19}. Note=Localizes to two to four centrioles throughout the cell cycle. Localizes to mitotic spindle microtubules during prometaphase and throughout the remainder of mitosis. Localizes to cytoskeleton on interphase. Localizes at the ciliary transition zone which connects the basal bodies to ciliary microtubules. Colocalizes with polyglutamylated tubulin (By similarity). {ECO:0000250|UniProtKB:Q6IQ19}. SUBUNIT: Associates with microtubules; the association occurs on polyglutamylated tubulin. {ECO:0000250|UniProtKB:Q6IQ19}. +E0CYV9 CD054_MOUSE Uncharacterized protein C4orf54 homolog 1786 189,749 Chain (1); Compositional bias (1); Modified residue (3) +P24788 CD11B_MOUSE Cyclin-dependent kinase 11B (Cell division cycle 2-like protein kinase 1) (Cell division protein kinase 11) (Cyclin-dependent kinase 11) (EC 2.7.11.22) (Galactosyltransferase-associated protein kinase p58/GTA) (PITSLRE serine/threonine-protein kinase CDC2L1) 784 91,513 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Compositional bias (2); Cross-link (1); Domain (1); Frameshift (1); Modified residue (11); Nucleotide binding (1); Sequence conflict (6) FUNCTION: Plays multiple roles in cell cycle progression, cytokinesis and apoptosis. Involved in pre-mRNA splicing in a kinase activity-dependent manner. May act as a negative regulator of normal cell cycle progression. {ECO:0000250|UniProtKB:P21127}. PTM: Phosphorylation at Ser-115 creates a binding site for 14-3-3 proteins. {ECO:0000250}. SUBUNIT: May interact PAK1 and RANBP9. p110C interacts with RNPS1. Interacts with CCND3. Interacts with CCNL1 and CCNL2. Forms complexes with pre-mRNA-splicing factors, including at least SRSF1, SRSF2 AND SRSF7/SLU7. {ECO:0000250|UniProtKB:P21127}. +Q9DAA3 CD036_MOUSE Uncharacterized protein C4orf36 homolog 117 13,552 Chain (1) +P35329 CD22_MOUSE B-cell receptor CD22 (B-lymphocyte cell adhesion molecule) (BL-CAM) (Sialic acid-binding Ig-like lectin 2) (Siglec-2) (T-cell surface antigen Leu-14) (CD antigen CD22) 862 96,582 Alternative sequence (2); Binding site (1); Chain (1); Disulfide bond (8); Domain (7); Glycosylation (11); Modified residue (7); Motif (3); Mutagenesis (1); Natural variant (30); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 703 721 Helical. {ECO:0000255}. TOPO_DOM 22 702 Extracellular. {ECO:0000255}.; TOPO_DOM 722 862 Cytoplasmic. {ECO:0000255}. FUNCTION: Mediates B-cell B-cell interactions. May be involved in the localization of B-cells in lymphoid tissues. Binds sialylated glycoproteins; one of which is CD45. Preferentially binds to alpha-2,6-linked sialic acid. The sialic acid recognition site can be masked by cis interactions with sialic acids on the same cell surface. Upon ligand induced tyrosine phosphorylation in the immune response seems to be involved in regulation of B-cell antigen receptor signaling. Plays a role in positive regulation through interaction with Src family tyrosine kinases and may also act as an inhibitory receptor by recruiting cytoplasmic phosphatases via their SH2 domains that block signal transduction through dephosphorylation of signaling molecules. PTM: Phosphorylated on tyrosine residues by LYN. {ECO:0000305}.; PTM: Phosphorylation of Tyr-777 and Tyr-837 are involved in binding to SYK. Phosphorylation of Tyr-822 is involved in binding to GRB2. Phosphorylation of Tyr-857 is involved in binding to SYK, PLCG2 and PIK3R1/PIK3R2. {ECO:0000269|PubMed:10373493}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SUBUNIT: Interacts with LYN, SYK, PIK3R1/PIK3R2, PLCG1, SHC1, INPP5D and GRB2 upon phosphorylation. May form a complex with INPP5D/SHIP, GRB2 and SHC1. Interacts with PTPN6/SHP-1 upon phosphorylation (By similarity). {ECO:0000250}. DOMAIN: Contains 3 copies of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is involved in modulation of cellular responses. The phosphorylated ITIM motif can bind the SH2 domain of several SH2-containing phosphatases. TISSUE SPECIFICITY: B-lymphocytes. +Q8R349 CDC16_MOUSE Cell division cycle protein 16 homolog (Anaphase-promoting complex subunit 6) (APC6) (Cyclosome subunit 6) 620 71,460 Chain (1); Modified residue (3); Repeat (14); Sequence caution (1) Protein modification; protein ubiquitination. FUNCTION: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By similarity). {ECO:0000250}. PTM: Phosphorylated. Phosphorylation on Ser-560 occurs specifically during mitosis (By similarity). {ECO:0000250}. SUBUNIT: V-shaped homodimer. The mammalian APC/C is composed at least of 14 distinct subunits ANAPC1, ANAPC2, CDC27/APC3, ANAPC4, ANAPC5, CDC16/APC6, ANAPC7, CDC23/APC8, ANAPC10, ANAPC11, CDC26/APC12, ANAPC13, ANAPC15 and ANAPC16 that assemble into a complex of at least 19 chains with a combined molecular mass of around 1.2 MDa; APC/C interacts with FZR1 and FBXO5. Interacts with PPP5C and CDC20. Interacts with CDC26. {ECO:0000250|UniProtKB:Q13042}. DOMAIN: TPR repeats 1-7 mediate homodimerization, while the C-terminal TPR repeats bind to CDC26, burying its hydrophobic N-terminus. {ECO:0000250|UniProtKB:Q13042}. +O35926 CD5R2_MOUSE Cyclin-dependent kinase 5 activator 2 (CDK5 activator 2) (Cyclin-dependent kinase 5 regulatory subunit 2) (p39) (p39I) 369 38,924 Chain (1); Compositional bias (3); Initiator methionine (1); Lipidation (1); Modified residue (1); Propeptide (1); Sequence conflict (7) FUNCTION: Activator of CDK5/TPKII. PTM: Myristoylated. The Gly-2-Ala mutant is absent of the cell periphery, suggesting that a proper myristoylation signal is essential for the proper distribution of CDK5R2 (p39) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. SUBUNIT: Heterodimer of a catalytic subunit and a regulatory subunit. +Q8BQH6 CDCP2_MOUSE CUB domain-containing protein 2 427 46,319 Chain (1); Disulfide bond (6); Domain (3); Glycosylation (2); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q9CPY3 CDCA5_MOUSE Sororin (Cell division cycle-associated protein 5) 264 28,991 Alternative sequence (1); Chain (1); Modified residue (11); Motif (2) FUNCTION: Regulator of sister chromatid cohesion in mitosis stabilizing cohesin complex association with chromatin. May antagonize the action of WAPL which stimulates cohesin dissociation from chromatin. Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair. Required for efficient DNA double-stranded break repair. {ECO:0000269|PubMed:21111234}. PTM: Phosphorylated. Phosphorylation, as cells enter mitosis, disrupts the interaction with PDS5A and relieves the inhibition of WAPL by CDCA5 (By similarity). {ECO:0000250}.; PTM: Ubiquitinated by the APC/C complex in G1, leading to its degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21111234}. Chromosome {ECO:0000269|PubMed:21111234}. Cytoplasm {ECO:0000269|PubMed:21111234}. Note=Associates with nuclear chromatin from S phase until metaphase and is released in the cytoplasm upon nuclear envelope breakdown. SUBUNIT: Interacts with the APC/C complex (By similarity). Interacts with the chromatin-bound cohesin complex; the interaction is indirect, occurs after DNA replication and requires acetylation of the cohesin component SMC3. Interacts (via the FGF motif) with PDS5A and PDS5B; the interaction is direct and prevents the interaction of PDS5A with WAPL. {ECO:0000250, ECO:0000269|PubMed:21111234}. DOMAIN: The KEN box is required for the association with the APC/C complex. {ECO:0000250}. +Q60773 CDN2D_MOUSE Cyclin-dependent kinase 4 inhibitor D (p19-INK4d) 166 17,809 Chain (1); Helix (11); Modified residue (1); Repeat (4); Sequence conflict (2); Turn (1) FUNCTION: Interacts strongly with CDK4 and CDK6 and inhibits them. {ECO:0000269|PubMed:7739547, ECO:0000269|PubMed:7739548}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with CDK6. {ECO:0000250}. +Q07424 CDX4_MOUSE Homeobox protein CDX-4 (Caudal-type homeobox protein 4) 282 30,465 Chain (1); DNA binding (1) SUBCELLULAR LOCATION: Nucleus. +Q9WTK2 CDYL_MOUSE Chromodomain Y-like protein (CDY-like) (Crotonyl-CoA hydratase) (EC 4.2.1.-) (Putative histone acetyltransferase Cdyl) (EC 2.3.1.48) 593 65,211 Alternative sequence (2); Chain (1); Domain (1); Modified residue (7); Mutagenesis (2); Region (2); Sequence conflict (1) FUNCTION: Isoform 2: Chromatin reader protein that recognizes and binds histone H3 trimethylated at 'Lys-9', dimethylated at 'Lys-27' and trimethylated at 'Lys-27' (H3K9me3, H3K27me2 and H3K27me3, respectively) (PubMed:12947414). Part of multimeric repressive chromatin complexes, where it is required for transmission and restoration of repressive histone marks, thereby preserving the epigenetic landscape (PubMed:12947414). Required for chromatin targeting and maximal enzymatic activity of Polycomb repressive complex 2 (PRC2); acts as a positive regulator of PRC2 activity by bridging the pre-existing histone H3K27me3 and newly recruited PRC2 on neighboring nucleosomes (By similarity). Acts as a corepressor for REST by facilitating histone-lysine N-methyltransferase EHMT2 recruitment and H3K9 dimethylation at REST target genes for repression (By similarity). Involved X chromosome inactivation in females: recruited to Xist RNA-coated X chromosome and facilitates propagation of H3K9me2 by anchoring EHMT2 (PubMed:24144980). Required for neuronal migration during brain development by repressing expression of RHOA (PubMed:28076783). In addition to act as a chromatin reader, acts as a hydro-lyase (By similarity). Shows crotonyl-coA hydratase activity by mediating the conversion of crotonyl-CoA ((2E)-butenoyl-CoA) to beta-hydroxybutyryl-CoA (3-hydroxybutanoyl-CoA), thereby acting as a negative regulator of histone crotonylation (By similarity). Histone crotonylation is required during spermatogenesis; down-regulation of histone crotonylation by CDYL regulates the reactivation of sex chromosome-linked genes in round spermatids and histone replacement in elongating spermatids (PubMed:28803779). May have histone acetyltransferase activity; such activity is however unsure in vivo (PubMed:12072557). {ECO:0000250|UniProtKB:Q9Y232, ECO:0000269|PubMed:12072557, ECO:0000269|PubMed:12947414, ECO:0000269|PubMed:24144980, ECO:0000269|PubMed:28076783, ECO:0000269|PubMed:28803779}.; FUNCTION: Isoform 1: Not able to recognize and bind histone H3K9me3, histone H3K27me2 and histone H3K27me3, due to the presence of a N-terminal extension that inactivates the chromo domain. {ECO:0000250|UniProtKB:Q9Y232}. SUBCELLULAR LOCATION: Isoform 2: Nucleus {ECO:0000269|PubMed:12072557, ECO:0000269|PubMed:12947414, ECO:0000269|PubMed:24144980}. Chromosome {ECO:0000269|PubMed:12947414, ECO:0000269|PubMed:24144980}. Note=Recognizes and binds histone H3 trimethylated at 'Lys-9', dimethylated at 'Lys-27' and trimethylated at 'Lys-27' (H3K9me3, H3K27me2 and H3K27me3, respectively) on chromatin (PubMed:24144980). Multimerization is required for chromatin-binding (By similarity). Recruited to Xist RNA-coated X chromosome (PubMed:24144980). {ECO:0000250|UniProtKB:Q9Y232, ECO:0000269|PubMed:24144980}. SUBUNIT: Forms multimers and multimerization is required for stable binding to chromatin (By similarity). Interacts with HDAC1 and HDAC2 via its C-terminal acetyl-CoA-binding domain (PubMed:12947414). Interacts with EZH2, EED, SUZ12, REST, EHMT1 and EHMT2 (By similarity). Part of a complex containing at least CDYL, REST, WIZ, SETB1, EHMT1 and EHMT2 (By similarity). Part of a complex containing at least CDYL, MIER1, MIER2, HDAC1 and HDAC2 (By similarity). Interacts with CHAF1A and CHAF1B; bridging the CAF-1 complex to the MCM2-7 (MCM) complex (By similarity). Interacts with MCM3 and MCM5; bridging the CAF-1 complex to the MCM2-7 (MCM) complex (By similarity). {ECO:0000250|UniProtKB:Q9Y232, ECO:0000269|PubMed:12947414}. DOMAIN: The chromo domain recognizes and binds histone H3K9me3, histone H3K27me2 and histone H3K27me3. {ECO:0000250|UniProtKB:Q9Y232}.; DOMAIN: The acetyl-CoA-binding domain mediates crotonyl-coA hydratase activity. {ECO:0000250|UniProtKB:Q9Y232}. TISSUE SPECIFICITY: Highly expressed in testis (at protein level) (PubMed:10192397). Isoform 1: Expressed as 2 transcripts encoding the same protein, a ubiquitous transcript and a highly expressed testis-specific transcript (PubMed:10192397). {ECO:0000269|PubMed:10192397}. +Q8VEB3 CE030_MOUSE UNC119-binding protein C5orf30 homolog 207 23,130 Chain (1); Compositional bias (1); Modified residue (3); Sequence conflict (1) FUNCTION: Probably plays a role in trafficking of proteins via its interaction with UNC119 and UNC119B cargo adapters: may help the release of UNC119 and UNC119B cargo or the recycling of UNC119 and UNC119B. May play a role in ciliary membrane localization via its interaction with UNC119B and protein transport into photoreceptor cells (By similarity). {ECO:0000250|UniProtKB:Q96GV9}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96GV9}. Cell projection, cilium {ECO:0000250|UniProtKB:Q96GV9}. Note=Localizes to the transition zone and proximal cilium in addition to being found throughout the cytoplasm. {ECO:0000250|UniProtKB:Q96GV9}. SUBUNIT: Interacts with UNC119 and UNC119B; interaction preferentially takes place when UNC119 and UNC119B are unliganded with myristoylated proteins. {ECO:0000250|UniProtKB:Q96GV9}. TISSUE SPECIFICITY: Highly expressed in photoreceptors. {ECO:0000269|PubMed:22085962}. +Q3UJC8 CE034_MOUSE Uncharacterized protein C5orf34 homolog 639 72,263 Alternative sequence (2); Chain (1); Frameshift (2); Sequence conflict (15) +Q3UTQ8 CDKL5_MOUSE Cyclin-dependent kinase-like 5 (EC 2.7.11.22) 938 105,489 Active site (1); Alternative sequence (2); Binding site (1); Chain (1); Compositional bias (1); Domain (1); Modified residue (4); Nucleotide binding (1) FUNCTION: Mediates phosphorylation of MECP2. May regulate ciliogenesis. {ECO:0000250|UniProtKB:O76039}. PTM: Autophosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O76039}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:O76039}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:O76039}. SUBUNIT: Interacts with MECP2. {ECO:0000250|UniProtKB:O76039}. +Q80V31 CE104_MOUSE Centrosomal protein of 104 kDa (Cep104) 926 103,946 Chain (1); Coiled coil (2); Repeat (2) FUNCTION: Required for ciliogenesis and for structural integrity at the ciliary tip. {ECO:0000250|UniProtKB:O60308}. SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000250|UniProtKB:O60308}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:O60308}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:O60308}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:O60308}. Note=In interphase non-ciliated cells, localizes to the distal ends of both the mother and daughter centrioles. In ciliated cells, present at the distal end of the daughter centriole, but not on the mother centriole, and at the tip of primary cilium. Localization at the ciliary tip is also observed in motile cilia. Throughout S phase, associated with both mother and daughter centrioles in each centrosome. During metaphase and telophase, present at both spindle poles. {ECO:0000250|UniProtKB:O60308}. SUBUNIT: Interacts with CCP110 and CEP97. {ECO:0000250|UniProtKB:O60308}. +Q5FWI3 CEIP2_MOUSE Cell surface hyaluronidase (EC 3.2.1.35) (Cell migration-inducing hyaluronidase 2) (Transmembrane protein 2) 1383 153,801 Chain (1); Domain (1); Erroneous initiation (1); Glycosylation (3); Modified residue (3); Repeat (3); Sequence conflict (9); Topological domain (2); Transmembrane (1) TRANSMEM 83 103 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 82 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 104 1383 Extracellular. {ECO:0000305}. FUNCTION: Cell surface hyaluronidase that mediates the initial cleavage of extracellular high-molecular-weight hyaluronan into intermediate-size hyaluronan of approximately 5 kDa fragments (By similarity). Acts as a regulator of angiogenesis and heart morphogenesis by mediating degradation of extracellular hyaluronan, thereby regulating VEGF signaling (By similarity). Is very specific to hyaluronan; not able to cleave chondroitin sulfate or dermatan sulfate (By similarity). {ECO:0000250|UniProtKB:A3KPQ7, ECO:0000250|UniProtKB:Q9UHN6}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9UHN6}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9UHN6}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10767548, ECO:0000269|PubMed:28246172}. +Q91X79 CELA1_MOUSE Chymotrypsin-like elastase family member 1 (EC 3.4.21.36) (Elastase-1) 266 28,901 Active site (3); Chain (1); Disulfide bond (4); Domain (1); Glycosylation (1); Metal binding (3); Propeptide (1); Sequence conflict (8); Signal peptide (1) FUNCTION: Acts upon elastin. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +Q7TSY6 CELF4_MOUSE CUGBP Elav-like family member 4 (CELF-4) (Bruno-like protein 4) (CUG-BP- and ETR-3-like factor 4) (RNA-binding protein BRUNOL-4) 486 51,932 Alternative sequence (8); Chain (1); Compositional bias (1); Domain (3); Frameshift (1); Region (2); Sequence conflict (6) FUNCTION: RNA-binding protein implicated in the regulation of pre-mRNA alternative splicing. Mediates exon inclusion and/or exclusion in pre-mRNA that are subject to tissue-specific and developmentally regulated alternative splicing. Specifically activates exon 5 inclusion of cardiac isoforms of TNNT2 during heart remodeling at the juvenile to adult transition. Promotes exclusion of both the smooth muscle (SM) and non-muscle (NM) exons in actinin pre-mRNAs. Activates the splicing of MAPT/Tau exon 10. Binds to muscle-specific splicing enhancer (MSE) intronic sites flanking the alternative exon 5 of TNNT2 pre-mRNA (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. TISSUE SPECIFICITY: Expressed strongly in skeletal muscle, heart and adipose tissue (at protein level). Expressed in the brain and cerebellum. {ECO:0000269|PubMed:11158314, ECO:0000269|PubMed:12438720}. +Q8BI06 CEMIP_MOUSE Cell migration-inducing and hyaluronan-binding protein (EC 3.2.1.35) (Protein 12H19.01.T7) 1361 153,034 Alternative sequence (2); Chain (1); Domain (1); Erroneous initiation (1); Frameshift (1); Glycosylation (6); Region (1); Repeat (4); Sequence conflict (5); Signal peptide (1) FUNCTION: Mediates depolymerization of hyaluronic acid (HA) via the cell membrane-associated clathrin-coated pit endocytic pathway. Binds to hyaluronic acid. Hydrolyzes high molecular weight hyaluronic acid to produce an intermediate-sized product, a process that may occur through rapid vesicle endocytosis and recycling without intracytoplasmic accumulation or digestion in lysosomes. Involved in hyaluronan catabolism in the dermis of the skin and arthritic synovium. Positively regulates epithelial-mesenchymal transition (EMT), and hence tumor cell growth, invasion and cancer dissemination. In collaboration with HSPA5/BIP, promotes cancer cell migration in a calcium and PKC-dependent manner. May be involved in hearing. {ECO:0000269|PubMed:24251095}. PTM: N-glycosylated; glycosylation is not necessary for HA-binding. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Cell membrane {ECO:0000250}. Membrane, clathrin-coated pit {ECO:0000269|PubMed:18448257, ECO:0000269|PubMed:24251095}. Secreted {ECO:0000250}. Note=Retained in the endoplasmic reticulum (ER) in a HSPA5/BIP-dependent manner. Strongly detected in the cytoplasm of breast carcinoma cells, whereas poorly detected in adjacent normal epithelial cells, stromal cells, or benign breast tissues. Localized in the nucleus and cytoplasm of colon adenocarcinomas (By similarity). Colocalized with clathrin heavy chain/CLTC in clathrin-coated vesicles. {ECO:0000250}. SUBUNIT: Interacts with EPHA2 and ITPR3. Interacts with HSPA5/BIP; the interaction induces calcium leakage from the endoplasmic reticulum and cell migration. Interacts with clathrin heavy chain/CLTC (By similarity). {ECO:0000250}. DOMAIN: The signal sequence is essential in mediating its proper translocation, hyaluronic acid (HA) degradation activity and secretion. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in Deiters' cells and various supporting cells in the organ of Corti including inner phalangeal, border, inner and outer pillar cells (at protein level). Weakly expressed in brain and testis. In ear, it is specifically expressed in inner ear. Expressed in Deiters' cells in the organ of Corti at P0 (postnatal day zero) before the onset of hearing, but disappears by day P7. Also expressed in fibrocytes of the spiral ligament and the spiral limbus through to P21, when the cochlea matures. {ECO:0000269|PubMed:11247670, ECO:0000269|PubMed:14577002, ECO:0000269|PubMed:18448257}. +Q9CZW2 CENPN_MOUSE Centromere protein N (CENP-N) 337 39,240 Alternative sequence (3); Chain (1); Modified residue (2) FUNCTION: Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. CENPN is the first protein to bind specifically to CENPA nucleosomes and the direct binding of CENPA nucleosomes by CENPN is required for centromere assembly. Required for chromosome congression and efficiently align the chromosomes on a metaphase plate. {ECO:0000250|UniProtKB:Q96H22}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, centromere {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Note=Localizes exclusively in the kinetochore domain of centromeres. Kinetochore-bound levels decrease when cells enter mitosis and increase again when cells exit mitosis. {ECO:0000250}. SUBUNIT: Component of the CENPA-NAC complex, at least composed of CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and CENPU. The CENPA-NAC complex interacts with the CENPA-CAD complex, composed of CENPI, CENPK, CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS. Interacts directly with CENPA. Identified in a centromere complex containing histones H2A, H2B and H4, and at least CENPA, CENPB, CENPC, CENPT, CENPN, HJURP, SUPT16H, SSRP1 and RSF1. {ECO:0000250|UniProtKB:Q96H22}. +P53569 CEBPZ_MOUSE CCAAT/enhancer-binding protein zeta (CCAAT-box-binding transcription factor) (CBF) (CCAAT-binding factor) 1052 120,262 Alternative sequence (2); Chain (1); Frameshift (2); Modified residue (6); Sequence conflict (15) FUNCTION: Stimulates transcription from the HSP70 promoter. SUBCELLULAR LOCATION: Nucleus. TISSUE SPECIFICITY: Ubiquitous. +Q99NF3 CEP41_MOUSE Centrosomal protein of 41 kDa (Cep41) (Testis-specific gene A14 protein) 373 41,442 Alternative sequence (2); Chain (1); Domain (1); Modified residue (6) FUNCTION: Required during ciliogenesis for tubulin glutamylation in cilium. Probably acts by participating in the transport of TTLL6, a tubulin polyglutamylase, between the basal body and the cilium. {ECO:0000269|PubMed:22246503}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cell projection, cilium {ECO:0000269|PubMed:22246503}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:22246503}. Note=Localizes mainly to the cilium basal body and in primary cilia. SUBUNIT: Found in a complex with TTLL6. {ECO:0000250}. +Q9CZ92 CENPP_MOUSE Centromere protein P (CENP-P) 286 33,288 Alternative sequence (2); Chain (1); Coiled coil (1); Erroneous initiation (1); Frameshift (3); Modified residue (1); Sequence conflict (1) FUNCTION: Component of the CENPA-CAD (nucleosome distal) complex, a complex recruited to centromeres which is involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation. May be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, centromere {ECO:0000250}. Note=Localizes exclusively in the centromeres. The CENPA-CAD complex is probably recruited on centromeres by the CENPA-NAC complex (By similarity). {ECO:0000250}. SUBUNIT: Component of the CENPA-CAD complex, composed of CENPI, CENPK, CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS. The CENPA-CAD complex interacts with the CENPA-NAC complex, at least composed of CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and CENPU (By similarity). {ECO:0000250}. +Q9QYM8 CENPH_MOUSE Centromere protein H (CENP-H) 241 28,135 Chain (1); Coiled coil (1); Cross-link (1); Frameshift (2); Modified residue (2); Sequence conflict (1) FUNCTION: Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. Required for chromosome congression and efficiently align the chromosomes on a metaphase plate (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10488063}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:10488063}. Note=Associates with active centromere-kinetochore complexes throughout the cell cycle. Colocalizes with inner kinetochore plate proteins CENPA and CENPC during both interphase and metaphase. SUBUNIT: Self-associates. Component of the CENPA-NAC complex, at least composed of CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and CENPU. The CENPA-NAC complex interacts with the CENPA-CAD complex, composed of CENPI, CENPK, CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS (By similarity). Interacts directly with CENPK (By similarity). Interacts with KIF2C and NDC80 (By similarity). Interacts with TRIM36. {ECO:0000250, ECO:0000269|PubMed:19232519}. TISSUE SPECIFICITY: Abundantly expressed in thymus, spleen, uterus, ovary, testis and muscle, and weakly expressed in small intestine, lung and stomach. Barely detectable expression in kidney, liver, skin and prostate gland. Not detected in brain, heart or adrenal gland. Also expressed weakly in various hematopoietic cell lines. {ECO:0000269|PubMed:10488063}. +Q8BRC6 CFA91_MOUSE Cilia- and flagella-associated protein 91 (CFAP91) (AMY-1-associating protein expressed in testis 1 homolog) (AAT-1) (MYCBP/AMY-1-associated testis-expressed protein 1) (Protein MAATS1) 783 91,623 Alternative sequence (2); Chain (1); Sequence conflict (1) FUNCTION: May regulate cilium motility through its role in the assembly of the axonemal radial spokes (By similarity). May play a role in spermatogenesis (PubMed:12223483). {ECO:0000250|UniProtKB:A8IH47, ECO:0000269|PubMed:12223483}. PTM: Phosphorylated by PKA. {ECO:0000250|UniProtKB:Q7Z4T9}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q7Z4T9}. Mitochondrion {ECO:0000250|UniProtKB:Q7Z4T9}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:A8IH47}. SUBUNIT: Part of a complex containing MYCBP, AKAP1 and PRKAR2B. {ECO:0000250|UniProtKB:Q7Z4T9}. TISSUE SPECIFICITY: Expressed in the testis, in cells involved in spermatogenesis. {ECO:0000269|PubMed:12223483}. +Q8CC70 CF300_MOUSE Cilia- and flagella-associated protein 300 267 30,901 Chain (1) FUNCTION: Cilium- and flagellum-specific protein that plays a role in axonemal structure organization and motility. May play a role in outer and inner dynein arm assembly. {ECO:0000250|UniProtKB:A0CY51}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A0CY51}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:A0CY51}. SUBUNIT: Interacts with DNAAF2. {ECO:0000250|UniProtKB:Q9BRQ4}. TISSUE SPECIFICITY: Expressed in the left-right organiser (LRO) node at 8.25 dpc. {ECO:0000269|PubMed:29727693}. +Q3UY96 CFA74_MOUSE Cilia- and flagella-associated protein 74 1578 178,928 Alternative sequence (2); Chain (1); Coiled coil (2); Erroneous initiation (1); Sequence caution (3) FUNCTION: As part of the central apparatus of the cilium axoneme may play a role in cilium movement. {ECO:0000250|UniProtKB:D4P3R7}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:D4P3R7}. +Q9DBB1 DUS6_MOUSE Dual specificity protein phosphatase 6 (EC 3.1.3.16) (EC 3.1.3.48) (Mitogen-activated protein kinase phosphatase 3) (MAP kinase phosphatase 3) (MKP-3) 381 42,408 Active site (1); Chain (1); Domain (2); Sequence conflict (2) FUNCTION: Inactivates MAP kinases. Has a specificity for the ERK family (By similarity). Plays an important role in alleviating acute postoperative pain (PubMed:24155322, PubMed:28405172). Necessary for the normal dephosphorylation of the long-lasting phosphorylated forms of spinal MAPK1/3 and MAP kinase p38 induced by peripheral surgery, which drives the resolution of acute postoperative allodynia (PubMed:24155322). Also important for dephosphorylation of MAPK1/3 in local wound tissue, which further contributes to resolution of acute pain (PubMed:28405172). {ECO:0000250|UniProtKB:Q16828, ECO:0000269|PubMed:24155322, ECO:0000269|PubMed:28405172}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q16828}. +Q91Z46 DUS7_MOUSE Dual specificity protein phosphatase 7 (EC 3.1.3.16) (EC 3.1.3.48) 422 45,220 Active site (1); Alternative sequence (1); Chain (1); Domain (2); Erroneous initiation (1); Mutagenesis (2); Region (2); Sequence conflict (1) FUNCTION: Dual specificity protein phosphatase (PubMed:27783954). Shows high activity towards MAPK1/ERK2 (By similarity). Also has lower activity towards MAPK14 and MAPK8 (By similarity). In arrested oocytes, plays a role in meiotic resumption (PubMed:27783954). Promotes nuclear envelope breakdown and activation of the CDK1/Cyclin-B complex in oocytes, probably by dephosphorylating and inactivating the conventional protein kinase C (cPKC) isozyme PRKCB (PubMed:27783954). May also inactivate PRKCA and/or PRKCG (PubMed:27783954). Also important in oocytes for normal chromosome alignment on the metaphase plate and progression to anaphase, where it might regulate activity of the spindle-assembly checkpoint (SAC) complex (PubMed:27783954). {ECO:0000250|UniProtKB:Q16829, ECO:0000269|PubMed:27783954}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q16829}. SUBUNIT: Interacts with MAPK1/ERK2; the interaction enhances DUSP7 phosphatase activity. {ECO:0000269|PubMed:27783954}. +Q8BHB7 CP046_MOUSE Uncharacterized protein C16orf46 homolog 409 45,038 Alternative sequence (2); Chain (1); Sequence conflict (1) +Q3UST5 CP089_MOUSE UPF0764 protein C16orf89 homolog 385 43,079 Chain (1); Sequence conflict (1); Signal peptide (1) PTM: Glycosylated. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20578903}. SUBUNIT: Homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Predominantly expressed in thyroid tissue. {ECO:0000269|PubMed:20578903}. +E9QMW4 CP096_MOUSE Uncharacterized protein C16orf96 homolog 1145 127,660 Alternative sequence (1); Chain (1); Coiled coil (3); Compositional bias (2); Frameshift (1) +P00375 DYR_MOUSE Dihydrofolate reductase (EC 1.5.1.3) 187 21,606 Beta strand (14); Binding site (3); Chain (1); Domain (1); Helix (6); Initiator methionine (1); Modified residue (2); Natural variant (2); Nucleotide binding (4); Region (1); Sequence conflict (7); Turn (1) Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. FUNCTION: Key enzyme in folate metabolism. Contributes to the de novo mitochondrial thymidylate biosynthesis pathway (PubMed:25980602). Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (PubMed:25980602). Binds its own mRNA. {ECO:0000250|UniProtKB:P00374, ECO:0000269|PubMed:25980602}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25980602}. Cytoplasm {ECO:0000269|PubMed:25980602}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P00374}. +P00184 CP1A1_MOUSE Cytochrome P450 1A1 (EC 1.14.14.1) (CYPIA1) (Cytochrome P450-P1) 524 59,230 Binding site (1); Chain (1); Erroneous initiation (1); Glycosylation (1); Metal binding (1) FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. +P03940 CP21A_MOUSE Steroid 21-hydroxylase (EC 1.14.14.16) (21-OHase) (Cytochrome P-450c21) (Cytochrome P450 21) (Cytochrome P450 XXI) (Cytochrome P450-C21) 487 55,328 Chain (1); Metal binding (1); Region (1); Sequence conflict (7) FUNCTION: Specifically catalyzes the 21-hydroxylation of steroids. Required for the adrenal synthesis of mineralocorticoids and glucocorticoids. {ECO:0000250|UniProtKB:P00191}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. DOMAIN: The leucine-rich hydrophobic amino acid N-terminal region probably helps to anchor the protein to the microsomal membrane. +Q64464 CP3AD_MOUSE Cytochrome P450 3A13 (EC 1.14.14.1) (CYPIIIA13) 503 57,492 Chain (1); Metal binding (1) FUNCTION: Can activate aflatoxin B1 to a genotoxic product. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. +P56655 CP238_MOUSE Cytochrome P450 2C38 (EC 1.14.14.1) (CYPIIC38) 490 56,229 Chain (1); Metal binding (1); Sequence conflict (18) FUNCTION: Metabolizes arachidonic acid to produce 11,12-epoxyeicosatrienoic acid (EET). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. TISSUE SPECIFICITY: Liver, brain, kidney, and intestine, with trace amounts in lung and heart. +Q6VVW9 CP2R1_MOUSE Vitamin D 25-hydroxylase (EC 1.14.14.24) (Cytochrome P450 2R1) 501 57,313 Binding site (1); Chain (1); Metal binding (1) FUNCTION: Has a D-25-hydroxylase activity on both forms of vitamin D, vitamin D(2) and D(3). {ECO:0000269|PubMed:12867411}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. SUBUNIT: Homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in the liver and testis. {ECO:0000269|PubMed:12867411}. +Q9ESD7 DYSF_MOUSE Dysferlin (Dystrophy-associated fer-1-like protein) (Fer-1-like protein 1) 2090 237,911 Alternative sequence (4); Chain (1); Compositional bias (1); Domain (7); Erroneous initiation (1); Metal binding (4); Modified residue (5); Sequence caution (1); Sequence conflict (19); Topological domain (2); Transmembrane (1) TRANSMEM 2057 2077 Helical. {ECO:0000255}. TOPO_DOM 1 2056 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 2078 2090 Extracellular. {ECO:0000255}. FUNCTION: Key calcium ion sensor involved in the Ca(2+)-triggered synaptic vesicle-plasma membrane fusion. Plays a role in the sarcolemma repair mechanism of both skeletal muscle and cardiomyocytes that permits rapid resealing of membranes disrupted by mechanical stress. {ECO:0000269|PubMed:12736685, ECO:0000269|PubMed:14506282, ECO:0000269|PubMed:17607357}. SUBCELLULAR LOCATION: Cell membrane, sarcolemma; Single-pass type II membrane protein. Cytoplasmic vesicle membrane; Single-pass type II membrane protein. Cell membrane {ECO:0000250}. Note=Colocalizes, during muscle differentiation, with BIN1 in the T-tubule system of myotubules and at the site of contact between two myotubes or a myoblast and a myotube (By similarity). Accumulates and colocalizes with fusion vesicles at the sarcolemma disruption sites. Wounding of myotubes led to its focal enrichment to the site of injury and to its relocalization in a Ca(2+)-dependent manner toward the plasma membrane (By similarity). Colocalizes with ANXA1 and ANXA2 at the sarcolemma in skeletal muscle. Colocalizes with PARVB at the sarcolemma of skeletal muscle (By similarity). Retained by caveolin at the plasmma membrane. Reaches the plasmma membrane through a caveolin-independent mechanism. Colocalizes, during muscle differentiation, with CACNA1S in the T-tubule system of myotubules. Detected on the apical plasma membrane of the syncytiotrophoblast (By similarity). {ECO:0000250}. SUBUNIT: Interacts with CAV3. Interacts with AHNAK; the interaction is direct and Ca(2+)-independent. Interacts with AHNAK2; the interaction is direct and Ca(2+)-independent (By similarity). Interacts with ANXA1; the interaction is Ca(2+)- and injury state-dependent. Interacts with ANXA2; the interaction is Ca(2+)- and injury state-dependent. Interacts with CACNA1S and PARVB. Interacts with TRIM72/MG53; interaction is required for transport to sites of cell injury during repair patch formation. Interacts with RIPOR2; this interaction occurs during early myogenic differentiation (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O75923, ECO:0000269|PubMed:14506282, ECO:0000269|PubMed:15835269, ECO:0000269|PubMed:16550931, ECO:0000269|PubMed:19380584}. DOMAIN: All seven C2 domains associate with lipid membranes in a calcium-dependent manner. Domains C2 1 and 3 have the highest affinity for calcium, the C2 domain 1 seems to be largely unstructured in the absence of bound ligands (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in skeletal and cardiac muscles (at protein level). Expressed in skeletal muscle and heart. Also found in brain, liver and kidney. {ECO:0000269|PubMed:11234777, ECO:0000269|PubMed:12736685}. DISEASE: Note=Defects in Dysf are the cause of a slowly progressive muscular dystrophy observed in SJL mice. It affects primarily the proximal muscles and it is inherited as autosomal recessive trait. {ECO:0000269|PubMed:10508505, ECO:0000269|PubMed:11234777}. +P11714 CP2D9_MOUSE Cytochrome P450 2D9 (EC 1.14.14.1) (CYPIID9) (Cytochrome P450-16-alpha) (Cytochrome P450CA) (Testosterone 16-alpha hydroxylase) 504 56,950 Chain (1); Metal binding (1); Modified residue (1); Sequence conflict (5) FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. +P24456 CP2DA_MOUSE Cytochrome P450 2D10 (EC 1.14.14.1) (CYPIID10) (Cytochrome P450-16-alpha) (Cytochrome P450CB) (Testosterone 16-alpha hydroxylase) 504 57,233 Chain (1); Metal binding (1); Modified residue (1); Sequence conflict (2) FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. +Q499E4 DZI1L_MOUSE Zinc finger protein DZIP1L (DAZ-interacting protein 1-like protein) (Protein warpy) 774 87,594 Alternative sequence (1); Chain (1); Coiled coil (1); Modified residue (2); Mutagenesis (1); Sequence conflict (2); Zinc finger (1) FUNCTION: Involved in primary cilium formation (PubMed:28530676). Probably acts as a transition zone protein required for localization of PKD1/PC1 and PKD2/PC2 to the ciliary membrane (By similarity). {ECO:0000250|UniProtKB:Q8IYY4, ECO:0000305|PubMed:28530676}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q8IYY4}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q8IYY4}. Note=Localizes to centrioles and to the distal ends of basal bodies. {ECO:0000250|UniProtKB:Q8IYY4}. SUBUNIT: Interacts with SEPT2. {ECO:0000250|UniProtKB:Q8IYY4}. +Q8C1R3 CQ050_MOUSE Uncharacterized protein C17orf50 homolog 189 21,117 Chain (1); Compositional bias (1); Sequence conflict (1) +Q8BGD5 CPT1C_MOUSE Carnitine O-palmitoyltransferase 1, brain isoform (CPT1-B) (EC 2.3.1.21) (CPT IC) (Carnitine O-palmitoyltransferase I, brain isoform) (CPTI-B) (Carnitine palmitoyltransferase 1C) 798 90,030 Active site (1); Binding site (3); Chain (1); Region (1); Sequence conflict (4); Topological domain (3); Transmembrane (2) TRANSMEM 53 75 Helical. {ECO:0000255}.; TRANSMEM 104 126 Helical. {ECO:0000255}. TOPO_DOM 1 52 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 76 103 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 127 798 Cytoplasmic. {ECO:0000255}. Lipid metabolism; fatty acid beta-oxidation. FUNCTION: May play a role in lipid metabolic process. {ECO:0000250|UniProtKB:Q8TCG5}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell junction, synapse {ECO:0000305|PubMed:22632720}. Cell projection, axon {ECO:0000269|PubMed:25751282}. Cell projection, dendrite {ECO:0000269|PubMed:25751282}. Endoplasmic reticulum {ECO:0000269|PubMed:25751282}. Note=Localized in the soma and dendritic and axonal projections. {ECO:0000269|PubMed:25751282}. SUBUNIT: Peripherally associated with AMPAR complex. AMPAR complex consists of an inner core made of 4 pore-forming GluA/GRIA proteins (GRIA1, GRIA2, GRIA3 and GRIA4) and 4 major auxiliary subunits arranged in a twofold symmetry. One of the two pairs of distinct binding sites is occupied either by CNIH2, CNIH3 or CACNG2, CACNG3. The other harbors CACNG2, CACNG3, CACNG4, CACNG8 or GSG1L. This inner core of AMPAR complex is complemented by outer core constituents binding directly to the GluA/GRIA proteins at sites distinct from the interaction sites of the inner core constituents. Outer core constituents include at least PRRT1, PRRT2, CKAMP44/SHISA9, FRRS1L and NRN1. The proteins of the inner and outer core serve as a platform for other, more peripherally associated AMPAR constituents, including CPT1C. Alone or in combination, these auxiliary subunits control the gating and pharmacology of the AMPAR complex and profoundly impact their biogenesis and protein processing. Interacts with ATL1 (By similarity). {ECO:0000250|UniProtKB:Q8TCG5, ECO:0000269|PubMed:22632720}. TISSUE SPECIFICITY: Predominantly expressed in brain (at protein level) and testis. Expressed in motor neurons (PubMed:25751282). Expressed in the ventral horn from spinal cords (PubMed:25751282). {ECO:0000269|PubMed:12376098, ECO:0000269|PubMed:22632720, ECO:0000269|PubMed:25751282}. +Q64735 CR1L_MOUSE Complement component receptor 1-like protein (Complement regulatory protein Crry) (Protein p65) 483 53,763 Alternative sequence (1); Chain (1); Disulfide bond (10); Domain (5); Frameshift (2); Glycosylation (2); Modified residue (5); Sequence conflict (9); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 406 426 Helical. {ECO:0000255}. TOPO_DOM 41 405 Extracellular. {ECO:0000255}.; TOPO_DOM 427 483 Cytoplasmic. {ECO:0000255}. FUNCTION: Acts as a cofactor for complement factor I, a serine protease which protects autologous cells against complement-mediated injury by cleaving C3b and C4b deposited on host tissue. Also acts as a decay-accelerating factor, preventing the formation of C4b2a and C3bBb, the amplification convertases of the complement cascade. Plays a crucial role in early embryonic development by maintaining fetomaternal tolerance. Also acts as a costimulatory factor for T-cells which favors IL-4 secretion. {ECO:0000269|PubMed:10642554, ECO:0000269|PubMed:10779754, ECO:0000269|PubMed:11986227, ECO:0000269|PubMed:1730912, ECO:0000269|PubMed:7528766}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Interacts with C3b. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed (at protein level). {ECO:0000269|PubMed:2911011, ECO:0000269|PubMed:7691944}. +Q80W49 CRBG3_MOUSE Beta/gamma crystallin domain-containing protein 3 1005 114,262 Alternative sequence (3); Beta strand (7); Chain (1); Domain (10); Helix (3); Modified residue (5); Turn (2) +P02525 CRBA1_MOUSE Beta-crystallin A1 (Beta-A1-crystallin) 198 23,401 Chain (1); Domain (4); Modified residue (5); Region (2); Sequence conflict (2) FUNCTION: Crystallins are the dominant structural components of the vertebrate eye lens. SUBUNIT: Homo/heterodimer, or complexes of higher-order. The structure of beta-crystallin oligomers seems to be stabilized through interactions between the N-terminal arms (By similarity). {ECO:0000250}. DOMAIN: Has a two-domain beta-structure, folded into four very similar Greek key motifs. +Q7TN12 INAVA_MOUSE Innate immunity activator protein 663 72,693 Chain (1); Coiled coil (1); Compositional bias (1); Motif (3); Sequence conflict (2) FUNCTION: Expressed in peripheral macrophages and intestinal myeloid-derived cells, is required for optimal PRR (pattern recognition receptor)-induced signaling, cytokine secretion, and bacterial clearance. Upon stimulation of a broad range of PRRs (pattern recognition receptor) such as NOD2 or TLR2, TLR3, TLR4, TLR5, TLR7 and TLR9, associates with YWHAQ/14-3-3T, which in turn leads to the recruitment and activation of MAP kinases and NF-kappa-B signaling complexes that amplifies PRR-induced downstream signals and cytokine secretion (By similarity). In the intestine, regulates adherens junction stability by regulating the degradation of CYTH1 and CYTH2, probably acting as substrate cofactor for SCF E3 ubiquitin-protein ligase complexes. Stabilizes adherens junctions by limiting CYTH1-dependent ARF6 activation (PubMed:29420262). {ECO:0000250|UniProtKB:Q3KP66, ECO:0000269|PubMed:29420262}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q3KP66}. Cytoplasm {ECO:0000250|UniProtKB:Q3KP66}. Note=Translocates to the nucleus upon NOD2 stimulation. {ECO:0000250|UniProtKB:Q3KP66}. SUBUNIT: Interacts with IRAK1, NOD2 and RIPK2; the interaction takes place upon PRR stimulation. Interacts with YWHAQ/14-3-3T; the interaction increases upon PRR stimulation and is required for cellular signaling pathway activation and cytokine secretion. Interacts (via N-terminal domain) with CYTH1 and CYTH2 (via their N-terminal domains). Interacts with FBXW11 and BTRC; associates with SCF E3 ubiquitin-protein ligase complexes (By similarity). {ECO:0000250|UniProtKB:Q3KP66}. +O55023 IMPA1_MOUSE Inositol monophosphatase 1 (IMP 1) (IMPase 1) (EC 3.1.3.25) (D-galactose 1-phosphate phosphatase) (EC 3.1.3.94) (Inositol-1(or 4)-monophosphatase 1) (Lithium-sensitive myo-inositol monophosphatase A1) 277 30,436 Beta strand (13); Binding site (3); Chain (1); Helix (9); Metal binding (6); Region (2); Turn (3) Polyol metabolism; myo-inositol biosynthesis; myo-inositol from D-glucose 6-phosphate: step 2/2. FUNCTION: Responsible for the provision of inositol required for synthesis of phosphatidylinositol and polyphosphoinositides and has been implicated as the pharmacological target for lithium action in brain. Has broad substrate specificity and can use myo-inositol monophosphates, myo-inositol 1,3-diphosphate, myo-inositol 1,4-diphosphate, scyllo-inositol-phosphate, D-galactose 1-phosphate, glucose-1-phosphate, glucose-6-phosphate, fructose-1-phosphate, beta-glycerophosphate, and 2'-AMP as substrates. {ECO:0000250|UniProtKB:P29218}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P29218}. SUBUNIT: Homodimer. {ECO:0000269|PubMed:23027737}. TISSUE SPECIFICITY: Mostly expressed in brain, small intestine, testis, kidney, and spleen (at protein level). {ECO:0000269|PubMed:17068342}. +O35164 MCPT9_MOUSE Mast cell protease 9 (mMCP-9) (EC 3.4.21.-) 246 26,652 Active site (3); Chain (1); Disulfide bond (3); Domain (1); Propeptide (1); Signal peptide (1) TISSUE SPECIFICITY: Selectively expressed in uterine mast cells. +Q00356 MCPTX_MOUSE Mast cell protease-like protein (EC 3.4.21.-) 246 26,775 Active site (3); Chain (1); Disulfide bond (3); Domain (1); Propeptide (1); Signal peptide (1) +Q8CGK5 INLR1_MOUSE Interferon lambda receptor 1 (IFN-lambda R1) (Cytokine receptor class-II member 12) (Cytokine receptor family 2 member 12) (CRF2-12) (Interleukin-28 receptor subunit alpha) (IL-28 receptor subunit alpha) (IL-28R-alpha) (IL-28RA) 535 59,976 Chain (1); Disulfide bond (3); Domain (1); Glycosylation (4); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 228 248 Helical. {ECO:0000255}. TOPO_DOM 21 227 Extracellular. {ECO:0000255}.; TOPO_DOM 249 535 Cytoplasmic. {ECO:0000255}. FUNCTION: The IFNLR1/IL10RB dimer is a receptor for the cytokine ligands IFNL2 and IFNL3 and mediates their antiviral activity. The ligand/receptor complex stimulate the activation of the JAK/STAT signaling pathway leading to the expression of IFN-stimulated genes (ISG), which contribute to the antiviral state. Determines the cell type specificity of the lambda interferon action. Shows a more restricted pattern of expression in the epithelial tissues thereby limiting responses to lambda interferons primarily to epithelial cells of the respiratory, gastrointestinal, and reproductive tracts. Seems not to be essential for early virus-activated host defense in vaginal infection, but plays an important role in Toll-like receptor (TLR)-induced antiviral defense. Plays a significant role in the antiviral immune defense in the intestinal epithelium. {ECO:0000269|PubMed:18250457, ECO:0000269|PubMed:21518880}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Heterodimer with IL10RB. {ECO:0000250}. +P55104 INHBC_MOUSE Inhibin beta C chain (Activin beta-C chain) 352 39,401 Chain (1); Disulfide bond (5); Glycosylation (4); Propeptide (1); Sequence conflict (2); Signal peptide (1) FUNCTION: Inhibins and activins inhibit and activate, respectively, the secretion of follitropin by the pituitary gland. Inhibins/activins are involved in regulating a number of diverse functions such as hypothalamic and pituitary hormone secretion, gonadal hormone secretion, germ cell development and maturation, erythroid differentiation, insulin secretion, nerve cell survival, embryonic axial development or bone growth, depending on their subunit composition. Inhibins appear to oppose the functions of activins. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Homodimeric or heterodimeric through association with alpha and beta subunits, linked by one or more disulfide bonds. Inhibins are heterodimers of one alpha and one beta subunit. Activins are homo- or heterodimers of beta subunits only (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Mainly expressed in the adult liver. +P40936 INMT_MOUSE Indolethylamine N-methyltransferase (Indolamine N-methyltransferase) (EC 2.1.1.49) (EC 2.1.1.96) (Aromatic alkylamine N-methyltransferase) (Amine N-methyltransferase) (Arylamine N-methyltransferase) (Thioether S-methyltransferase) (TEMT) 264 29,460 Binding site (6); Chain (1); Modified residue (2); Region (2); Sequence conflict (1) FUNCTION: Catalyzes the N-methylation of tryptamine and structurally related compounds (By similarity). Functions as thioether S-methyltransferase and is active with a variety of thioethers and the corresponding selenium and tellurium compounds, including 3-methylthiopropionaldehyde, dimethyl selenide, dimethyl telluride, 2-methylthioethylamine, 2-methylthioethanol, methyl-n-propyl sulfide and diethyl sulfide. Plays an important role in the detoxification of selenium compounds. {ECO:0000250, ECO:0000269|PubMed:3350800}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:3350800}. SUBUNIT: Monomer. {ECO:0000269|PubMed:3350800}. TISSUE SPECIFICITY: Detected in lung and liver (at protein level). {ECO:0000269|PubMed:3350800}. +P01325 INS1_MOUSE Insulin-1 [Cleaved into: Insulin-1 B chain; Insulin-1 A chain] 108 12,160 Disulfide bond (3); Peptide (2); Propeptide (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Heterodimer of a B chain and an A chain linked by two disulfide bonds. {ECO:0000250|UniProtKB:P01308}. +Q3UGS4 MCRI1_MOUSE Mapk-regulated corepressor-interacting protein 1 (Protein FAM195B) 97 11,101 Chain (1); Erroneous initiation (1); Modified residue (4); Motif (1) FUNCTION: The phosphorylation status of MCRIP1 functions as a molecular switch to regulate epithelial-mesenchymal transition. Unphosphorylated MCRIP1 binds to and inhibits the transcriptional corepressor CTBP(s). When phosphorylated by MAPK/ERK, MCRIP1 releases CTBP(s) resulting in transcriptional silencing of the E-cadherin gene and induction of epithelial-mesenchymal transition. {ECO:0000250|UniProtKB:C9JLW8}. PTM: Phosphorylation by MAPK3/1 (ERK1/2) regulates MCRIP1 binding to CTBP(s). {ECO:0000250|UniProtKB:C9JLW8}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:C9JLW8}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:C9JLW8}. SUBUNIT: Interacts (unphosphorylated form, via the PXDLS motif) with CTBP1, competitively inhibiting CTBP-ZEB1 interaction. Interacts with CTBP2. Interacts with MCRIP2. Interacts with DDX6. {ECO:0000250|UniProtKB:C9JLW8}. TISSUE SPECIFICITY: Widely expressed (at protein level). {ECO:0000269|PubMed:25728771}. +Q9WUG6 INSL5_MOUSE Insulin-like peptide INSL5 (Insulin-like peptide 5) (Relaxin/insulin-like factor 2) (Relaxin/insulin-like protein) [Cleaved into: Insulin-like peptide INSL5 B chain; Insulin-like peptide INSL5 A chain] 135 15,524 Chain (1); Disulfide bond (3); Erroneous initiation (1); Peptide (1); Propeptide (1); Signal peptide (1) FUNCTION: May have a role in gut contractility or in thymic development and regulation. Activates RXFP4 with high potency and appears to be the endogenous ligand for this receptor (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Heterodimer of a B chain and an A chain linked by two disulfide bonds. {ECO:0000250}. TISSUE SPECIFICITY: Highest expression in colon with lower levels in thymus. Minimal levels in testis. {ECO:0000269|PubMed:10458910}. +Q9JII1 INP5E_MOUSE 72 kDa inositol polyphosphate 5-phosphatase (EC 3.1.3.36) (Phosphatidylinositol 4,5-bisphosphate 5-phosphatase) (Phosphatidylinositol polyphosphate 5-phosphatase type IV) 647 71,915 Chain (1); Compositional bias (1); Lipidation (1); Modified residue (5); Propeptide (1); Region (1); Repeat (3) FUNCTION: Converts phosphatidylinositol 3,4,5-trisphosphate (PtdIns 3,4,5-P3) to PtdIns-P2, and phosphatidylinositol 4,5-bisphosphate to phosphatidylinositol 4-phosphate. Specific for lipid substrates, inactive towards water soluble inositol phosphates. {ECO:0000269|PubMed:10806194}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:19668215}. Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:10806194}; Peripheral membrane protein {ECO:0000269|PubMed:10806194}; Cytoplasmic side {ECO:0000269|PubMed:10806194}. Cell projection, ruffle {ECO:0000250|UniProtKB:Q9WVR1}. Cell membrane {ECO:0000250|UniProtKB:Q9WVR1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9WVR1}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9WVR1}. Cytoplasm {ECO:0000250|UniProtKB:Q9WVR1}. Note=Peripheral membrane protein associated with Golgi stacks. {ECO:0000269|PubMed:10806194}. SUBUNIT: Interacts (when prenylated) with PDE6D; this is important for normal location in cilia. {ECO:0000250|UniProtKB:Q9NRR6}. TISSUE SPECIFICITY: Highly expressed in testis, in pachytene and diplotene spermatocytes, but not in more mature elongating spermatids. Detected in neurons throughout the brain. {ECO:0000269|PubMed:10806194}. +Q63ZV0 INSM1_MOUSE Insulinoma-associated protein 1 (Zinc finger protein IA-1) 521 54,050 Chain (1); Compositional bias (2); Frameshift (1); Region (2); Sequence conflict (11); Zinc finger (5) FUNCTION: Sequence-specific DNA-binding transcriptional regulator that plays a key role in neurogenesis and neuroendocrine cell differentiation during embryonic and/or fetal development. Binds to the consensus sequence 5'-[TG][TC][TC][TT][GA]GGG[CG]A-3' in target promoters. Acts as a transcriptional repressor of NEUROD1 and INS expression via its interaction with cyclin CCND1 in a cell cycle-independent manner. Negatively regulates skeletal muscle-specific gene expression in endocrine cells of the pituitary by inhibiting the Notch signaling pathway. Represses target gene transcription by recruiting chromatin-modifying factors, such as HDAC1, HDAC2, HDAC3, KDM1A and RCOR1 histone deacetylases. Binds to its own promoter, suggesting autoregulation as a self-control feedback mechanism. Promotes the generation and expansion of neuronal basal progenitor cells in the developing neocortex. Involved in the differentiation of endocrine cells of the developing anterior pituitary gland, of the pancreas and intestine, and of sympatho-adrenal cells in the peripheral nervous system. Promotes cell cycle signaling arrest and inhibition of cellular proliferation. {ECO:0000269|PubMed:16511571, ECO:0000269|PubMed:16951258, ECO:0000269|PubMed:18094025, ECO:0000269|PubMed:18940587, ECO:0000269|PubMed:24227653}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12079283, ECO:0000269|PubMed:24227653}. SUBUNIT: Interacts (via the N-terminal region) with CCND1 (via cyclin N-terminal domain); the interaction competes with the binding of CCND1 to CDK4 during cell cycle progression and increases its transcriptional repressor activity. Interacts with HDAC3; the interaction increases its transcriptional repressor activity (By similarity). Interacts (via the SNAG domain) with HDAC1. Interacts (via the SNAG domain) with HDAC2. Interacts (via the SNAG domain) with KDM1A. Interacts (via the SNAG domain) with RCOR1. Interacts with SORBS1. {ECO:0000250, ECO:0000269|PubMed:12079283, ECO:0000269|PubMed:24227653}. DOMAIN: The C-terminal region is necessary for NEUROD1 promoter DNA-binding and transcriptional repressor activity. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in adrenal gland. Expressed in the dentate gyrus of the hippocampus and the wall of the lateral ventricle. Expressed in pancreatic and intestinal endocrine cells. {ECO:0000269|PubMed:16951258, ECO:0000269|PubMed:18094025, ECO:0000269|PubMed:18940587}. +Q8CD60 INSY1_MOUSE Inhibitory synaptic factor 1 (InSyn1) 292 31,813 Chain (1); Coiled coil (1); Compositional bias (1) FUNCTION: Component of the protein machinery at the inhibitory synapses, probably acting as a scaffold. Inhibitory synapses dampen neuronal activity through postsynaptic hyperpolarization. This synaptic inhibition is fundamental for the functioning of the central nervous system, shaping and orchestrating the flow of information through neuronal networks to generate a precise neural code. {ECO:0000269|PubMed:27609886}. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000269|PubMed:27609886}. SUBUNIT: Interacts with GPHN. {ECO:0000269|PubMed:27609886}. +P21447 MDR1A_MOUSE Multidrug resistance protein 1A (EC 7.6.2.2) (ATP-binding cassette sub-family B member 1A) (MDR1A) (Multidrug resistance protein 3) (P-glycoprotein 3) 1276 140,647 Beta strand (28); Chain (1); Domain (4); Glycosylation (3); Helix (50); Modified residue (1); Nucleotide binding (2); Sequence conflict (4); Topological domain (13); Transmembrane (12); Turn (8) TRANSMEM 44 66 Helical.; TRANSMEM 113 133 Helical.; TRANSMEM 183 204 Helical.; TRANSMEM 212 232 Helical.; TRANSMEM 291 312 Helical.; TRANSMEM 327 348 Helical.; TRANSMEM 708 728 Helical.; TRANSMEM 753 773 Helical.; TRANSMEM 829 849 Helical.; TRANSMEM 851 870 Helical.; TRANSMEM 931 953 Helical.; TRANSMEM 970 991 Helical. TOPO_DOM 1 43 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 67 112 Extracellular. {ECO:0000250}.; TOPO_DOM 134 182 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 205 211 Extracellular. {ECO:0000250}.; TOPO_DOM 233 290 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 313 326 Extracellular. {ECO:0000250}.; TOPO_DOM 349 707 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 729 752 Extracellular. {ECO:0000250}.; TOPO_DOM 774 828 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 850 850 Extracellular. {ECO:0000250}.; TOPO_DOM 871 930 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 954 969 Extracellular. {ECO:0000250}.; TOPO_DOM 992 1276 Cytoplasmic. {ECO:0000250}. FUNCTION: Energy-dependent efflux pump responsible for decreased drug accumulation in multidrug-resistant cells. {ECO:0000269|PubMed:19325113}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBUNIT: Interacts with PSMB5. {ECO:0000250}. +P06795 MDR1B_MOUSE Multidrug resistance protein 1B (EC 7.6.2.2) (ATP-binding cassette sub-family B member 1B) (P-glycoprotein 1) (CD antigen CD243) 1276 140,994 Chain (1); Domain (4); Glycosylation (4); Modified residue (2); Nucleotide binding (2); Topological domain (13); Transmembrane (12) TRANSMEM 44 66 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 116 136 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 186 207 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 215 235 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 294 315 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 330 351 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 710 730 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 755 775 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 831 851 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 853 872 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 933 955 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 972 993 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}. TOPO_DOM 1 43 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 67 115 Extracellular. {ECO:0000250}.; TOPO_DOM 137 185 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 208 214 Extracellular. {ECO:0000250}.; TOPO_DOM 236 293 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 316 329 Extracellular. {ECO:0000250}.; TOPO_DOM 352 709 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 731 754 Extracellular. {ECO:0000250}.; TOPO_DOM 776 830 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 852 852 Extracellular. {ECO:0000250}.; TOPO_DOM 873 932 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 956 971 Extracellular. {ECO:0000250}.; TOPO_DOM 994 1276 Cytoplasmic. {ECO:0000250}. FUNCTION: Energy-dependent efflux pump responsible for decreased drug accumulation in multidrug-resistant cells. PTM: Several phosphorylated serine residues are present in the linker domain. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. SUBUNIT: Interacts with PSMB5. {ECO:0000250}. +Q8CAC8 ISK10_MOUSE Serine protease inhibitor Kazal-type 10 162 18,520 Chain (1); Disulfide bond (5); Domain (2); Site (1); Transmembrane (2) TRANSMEM 6 26 Helical. {ECO:0000255}.; TRANSMEM 80 100 Helical. {ECO:0000255}. FUNCTION: Probable serine protease inhibitor. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in epydiymis, in the cauda and corpus. Also expressed in brain. {ECO:0000269|PubMed:16930550}. +Q09TK7 ISK11_MOUSE Serine protease inhibitor Kazal-type 11 88 10,090 Chain (1); Disulfide bond (3); Domain (1); Erroneous initiation (1); Glycosylation (1); Signal peptide (1); Site (1) FUNCTION: Probable serine protease inhibitor. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Expressed in epydiymis, in the caput. Also expressed in seminal vesicles. {ECO:0000269|PubMed:16930550}. +Q9D256 ISK12_MOUSE Serine protease inhibitor Kazal-type 12 87 9,353 Chain (1); Disulfide bond (3); Domain (1); Erroneous initiation (5); Signal peptide (1); Site (1) FUNCTION: Inhibits trypsin. {ECO:0000269|PubMed:16930550}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Expressed in epydiymis, in the caput. {ECO:0000269|PubMed:16930550}. +P09036 ISK1_MOUSE Serine protease inhibitor Kazal-type 1 (P12) (Prostatic secretory glycoprotein) (Serine protease inhibitor Kazal-type 3) 80 8,488 Chain (1); Disulfide bond (3); Domain (1); Mutagenesis (6); Signal peptide (1); Site (2) FUNCTION: Serine protease inhibitor which exhibits anti-trypsin activity (PubMed:3428272, PubMed:14645103, PubMed:22228629). In the pancreas, protects against trypsin-catalyzed premature activation of zymogens (PubMed:16083722). {ECO:0000269|PubMed:14645103, ECO:0000269|PubMed:16083722, ECO:0000269|PubMed:22228629, ECO:0000269|PubMed:3428272}.; FUNCTION: In the male reproductive tract, binds to sperm heads where it modulates sperm capacitance by inhibiting calcium uptake and nitrogen oxide (NO) production (PubMed:9828198, PubMed:14645103, PubMed:16083722, PubMed:22228629). {ECO:0000269|PubMed:14645103, ECO:0000269|PubMed:16083722, ECO:0000269|PubMed:22228629, ECO:0000269|PubMed:9828198}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1929395}. TISSUE SPECIFICITY: In the genital tract, expressed only in male accessory glands including seminal vesicle, coagulating gland and prostate. {ECO:0000269|PubMed:9828198}. +Q60929 MEF2A_MOUSE Myocyte-specific enhancer factor 2A 498 53,579 Alternative sequence (2); Chain (1); Compositional bias (4); Cross-link (1); DNA binding (1); Domain (1); Modified residue (16); Region (2); Sequence conflict (12); Site (3) FUNCTION: Transcriptional activator which binds specifically to the MEF2 element, 5'-YTA[AT](4)TAR-3', found in numerous muscle-specific genes. Also involved in the activation of numerous growth factor- and stress-induced genes. Mediates cellular functions not only in skeletal and cardiac muscle development, but also in neuronal differentiation and survival. Plays diverse roles in the control of cell growth, survival and apoptosis via p38 MAPK signaling in muscle-specific and/or growth factor-related transcription. In cerebellar granule neurons, phosphorylated and sumoylated MEF2A represses transcription of NUR77 promoting synaptic differentiation. Associates with chromatin to the ZNF16 promoter (By similarity). {ECO:0000250}. PTM: Constitutive phosphorylation on Ser-406 promotes Lys-401 sumoylation thus preventing acetylation at this site. Dephosphorylation on Ser-406 by PPP3CA upon neuron depolarization promotes a switch from sumoylation to acetylation on residue Lys-403 leading to inhibition of dendrite claw differentiation. Phosphorylation on Thr-312 and Thr-319 are the main sites involved in p38 MAPK signaling and activate transcription. Phosphorylated on these sites by MAPK14/p38alpha and MAPK11/p38beta, but not by MAPK13/p38delta nor by MAPK12/p38gamma. Phosphorylation on Ser-408 by CDK5 induced by neurotoxicity inhibits MEF2A transcriptional activation leading to apoptosis of cortical neurons. Phosphorylation on Thr-312, Thr-319 and Ser-355 can be induced by EGF (By similarity). Isoform 3 is phosphorylated on Ser-98 and Thr-108. {ECO:0000250, ECO:0000269|PubMed:17785444}.; PTM: Sumoylation on Lys-401 is enhanced by PIAS1 and represses transcriptional activity. Phosphorylation on Ser-406 is required for sumoylation. Has no effect on nuclear location nor on DNA binding. Sumoylated with SUMO1 and, to a lesser extent with SUMO2 and SUMO3. PIASx facilitates sumoylation in postsynaptic dendrites in the cerebellar cortex and promotes their morphogenesis (By similarity). {ECO:0000250}.; PTM: Acetylation on Lys-401 activates transcriptional activity. Acetylated by p300 on several sites in diffentiating myocytes. Acetylation on Lys-4 increases DNA binding and transactivation. Hyperacetylation by p300 leads to enhanced cardiac myocyte growth and heart failure (By similarity). {ECO:0000250}.; PTM: Proteolytically cleaved in cerebellar granule neurons on several sites by caspase 3 and caspase 7 following neurotoxicity. Preferentially cleaves the CDK5-mediated hyperphosphorylated form which leads to neuron apoptosis and transcriptional inactivation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Binds DNA as a homo- or heterodimer. Dimerizes with MEF2D. Interacts with HDAC7. Interacts with PIAS1; the interaction enhances sumoylation. Interacts with HDAC4, HDAC9 and SLC2A4RG. Interacts (via the N-terminal) with MAPK7; the interaction results in the phosphorylation and transcriptional activity of MEF2A (By similarity). {ECO:0000250}. DOMAIN: The beta domain, missing in a number of isoforms, is required for enhancement of transcriptional activity. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed though mainly restricted to skeletal and cardiac muscle, brain, neurons and lymphocytes. Differentially expressed depending on if isoforms contain the beta domain or not, with the total expression of the beta domain-lacking isoforms vastly exceding that of the beta domain-containing isoforms. Isoforms containing the beta domain are expressed primarily in skeletal and cardiac muscle and in brain. Also present in lung and testis. Splicing to include the beta domain is induced in differentiating myocytes. Isoforms lacking the beta domain are expressed less abundantly in skeletal muscle, brain and lymphocytes, and are uniquely found in ovary, liver, spleen and kidney. In embryos, the beta domain-containing and beta domain-lacking isoforms are equally expressed. Also expressed cerebellar granule neurons and other regions of the CNS. Highest levels in the olfactory bulb, cortex, hippocampus, thalamus and cerebellum. {ECO:0000269|PubMed:15834131, ECO:0000269|PubMed:9013788}. +P97367 MEIS2_MOUSE Homeobox protein Meis2 (Meis1-related protein 1) 477 51,728 Alternative sequence (3); Chain (1); Compositional bias (3); DNA binding (1); Region (3); Sequence conflict (2) FUNCTION: Involved in transcriptional regulation. Binds to HOX or PBX proteins to form dimers, or to a DNA-bound dimer of PBX and HOX proteins and thought to have a role in stabilization of the homeoprotein-DNA complex. Isoform Meis2B is required for the activity of a PDX1:PBX1b:MEIS2b complex in pancreatic acinar cells involved in the transcriptional activation of the ELA1 enhancer; the complex binds to the enhancer B element and cooperates with the transcription factor 1 complex (PTF1) bound to the enhancer A element; MEIS2 is not involved in complex DNA-binding. Probably in complex with PBX1, is involved in transcriptional regulation by KLF4. Isoforms Meis2B and Meis2D can bind to a EPHA8 promoter sequence containing the DNA motif 5'-CGGTCA-3'; in cooperation with a PBX protein (such as PBX2) is proposed to be involved in the transcriptional activation of EPHA8 in the developing midbrain. May be involved in regulation of myeloid differentiation. Can bind to the DNA sequence 5'-TGACAG-3'in the activator ACT sequence of the D(1A) dopamine receptor (DRD1) promoter and activate DRD1 transcription. {ECO:0000269|PubMed:11279116, ECO:0000269|PubMed:11438208, ECO:0000269|PubMed:17178831}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:9710595}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:21059917}. SUBUNIT: Monomer and homodimer. Heterodimer with HOXB13 (By similarity). Isoform Meis2A interacts with TLX1. Isoform Meis2B interacts with HOXA13 and PBX1 isoform PBX1b. Isoform Meis2D interacts with SP1, SP3 and KLF4. Isoform Meis2D interacts with PBX1 isoform PBX1a; the interaction partially relieves MEIS2 autoinhibition. Isoform Meis2B is part of a PDX1:PBX1b:MEIS2b complex; Meis2B is recruited by PBX1b and can be replaced by isoform Meis2D in a small fraction of complexes. Can form trimeric complexes including HOXB8 and PBX2 or PBX3. {ECO:0000250|UniProtKB:O14770, ECO:0000269|PubMed:11279116, ECO:0000269|PubMed:11438208, ECO:0000269|PubMed:15617687, ECO:0000269|PubMed:9710595}. TISSUE SPECIFICITY: Displays spatially restricted expression patterns in the developing nervous system, limbs, face, and in various viscera. In adult, it is mainly expressed in the brain and female genital tract, with a different distribution of the alternative splice forms in these organs. Lower expression in lung and only basal level in heart, liver, kidney, spleen, and testis. Expressed in pancreatic islets (beta-cells only) (PubMed:21059917). {ECO:0000269|PubMed:21059917}. +P97368 MEIS3_MOUSE Homeobox protein Meis3 (Meis1-related protein 2) 378 41,726 Alternative sequence (1); Chain (1); Compositional bias (2); DNA binding (1); Sequence conflict (2) FUNCTION: Transcriptional regulator which directly modulates PDPK1 expression, thus promoting survival of pancreatic beta-cells. Also regulates expression of NDFIP1, BNIP3, and CCNG1. {ECO:0000269|PubMed:21059917}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21059917}. TISSUE SPECIFICITY: Expressed at high levels in the brain. Significant expression also observed in the heart, spleen and lung. Expressed in pancreatic islets (beta-cells and non-beta-cells) (PubMed:21059917). {ECO:0000269|PubMed:21059917}. +Q8BFT6 JMJD4_MOUSE 2-oxoglutarate and iron-dependent oxygenase JMJD4 (EC 1.14.11.-) (JmjC domain-containing protein 4) (Jumonji domain-containing protein 4) (Lysyl-hydroxylase JMJD4) 427 49,152 Alternative sequence (3); Chain (1); Domain (1); Metal binding (3) FUNCTION: Catalyzes the 2-oxoglutarate and iron-dependent C4-lysyl hydroxylation of ETF1 at 'Lys-63' thereby promoting the translational termination efficiency of ETF1 (By similarity). Not essential for embryonic stem cell (ESC) maintenance and the embryonic and postnatal development (PubMed:27147518). {ECO:0000250|UniProtKB:Q9H9V9, ECO:0000269|PubMed:27147518}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H9V9}. SUBUNIT: Interacts with ETF1 (By similarity). Interacts with the ETF1-GSPT1 complex (By similarity). {ECO:0000250|UniProtKB:Q9H9V9}. +P05627 JUN_MOUSE Transcription factor AP-1 (AH119) (Activator protein 1) (AP1) (Proto-oncogene c-Jun) (V-jun avian sarcoma virus 17 oncogene homolog) (Jun A) 334 35,944 Chain (1); Cross-link (5); Domain (1); Modified residue (14); Region (2); Sequence conflict (1); Site (1) FUNCTION: Transcription factor that recognizes and binds to the enhancer heptamer motif 5'-TGA[CG]TCA-3'. Promotes activity of NR5A1 when phosphorylated by HIPK3 leading to increased steroidogenic gene expression upon cAMP signaling pathway stimulation. Involved in activated KRAS-mediated transcriptional activation of USP28 in colorectal cancer (CRC) cells. Binds to the USP28 promoter in colorectal cancer (CRC) cells (By similarity). {ECO:0000250|UniProtKB:P05412, ECO:0000269|PubMed:14707112, ECO:0000269|PubMed:17210646}. PTM: Phosphorylated by CaMK4 and PRKDC; phosphorylation enhances the transcriptional activity. Phosphorylated by HIPK3. Phosphorylated by DYRK2 at Ser-246; this primes the protein for subsequent phosphorylation by GSK3B at Thr-242. Phosphorylated at Thr-242, Ser-246 and Ser-252 by GSK3B; phosphorylation reduces its ability to bind DNA. Phosphorylated by PAK2 at Thr-2, Thr-8, Thr-89, Thr-93 and Thr-289 thereby promoting JUN-mediated cell proliferation and transformation. Phosphorylated by PLK3 following hypoxia or UV irradiation, leading to increase DNA-binding activity (By similarity). {ECO:0000250|UniProtKB:P05412}.; PTM: Ubiquitinated by the SCF(FBXW7), leading to its degradation. Ubiquitination takes place following phosphorylation, that promotes interaction with FBXW7. {ECO:0000250|UniProtKB:P05412}.; PTM: Acetylated at Lys-271 by EP300. {ECO:0000250|UniProtKB:P05412}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P05412}. SUBUNIT: Heterodimer with either FOS or BATF3 or ATF7 (By similarity). The ATF7/JUN heterodimer is essential for ATF7 transactivation activity. Interacts with SP1, SPIB and TCF20. Interacts with COPS5; the interaction leads indirectly to its phosphorylation. Component of the SMAD3/SMAD4/JUN/FOS/complex which forms at the AP1 promoter site. The SMAD3/SMAD4 heterodimer acts synergistically with the JUN/FOS heterodimer to activate transcription in response to TGF-beta (By similarity). Interacts (via its basic DNA binding and leucine zipper domains) with SMAD3 (via an N-terminal domain); the interaction is required for TGF-beta-mediated transactivation of the SMAD3/SMAD4/JUN/FOS/complex (By similarity). Interacts with DSIPI; the interaction inhibits the binding of active AP1 to its target DNA (PubMed:11397794). Interacts with HIVEP3 and MYBBP1A (PubMed:9447996, PubMed:14707112). Interacts with methylated RNF187 (PubMed:20852630). Binds to HIPK3. Interacts (when phosphorylated) with FBXW7 (By similarity). Interacts with PRR7 (PubMed:27458189). Found in a complex with PRR7 and FBXW7 (By similarity). Interacts with PRR7 and FBXW7; the interaction inhibits ubiquitination-mediated JUN degradation promoting its phosphorylation and transcriptional activity (By similarity). Interacts with RBM39 (PubMed:11704680). {ECO:0000250|UniProtKB:P05412, ECO:0000250|UniProtKB:P17325, ECO:0000269|PubMed:11397794, ECO:0000269|PubMed:11704680, ECO:0000269|PubMed:14707112, ECO:0000269|PubMed:20852630, ECO:0000269|PubMed:27458189, ECO:0000269|PubMed:9447996}. +B8JK39 ITA9_MOUSE Integrin alpha-9 1036 114,416 Calcium binding (3); Chain (1); Disulfide bond (9); Glycosylation (4); Motif (1); Repeat (7); Sequence conflict (2); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 982 1002 Helical. {ECO:0000255}. TOPO_DOM 29 981 Extracellular. {ECO:0000305}.; TOPO_DOM 1003 1036 Cytoplasmic. {ECO:0000305}. FUNCTION: Integrin alpha-9/beta-1 (ITGA9:ITGB1) is a receptor for VCAM1, cytotactin and osteopontin. It recognizes the sequence A-E-I-D-G-I-E-L in cytotactin. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}. SUBUNIT: Heterodimer of an alpha and a beta subunit. Alpha-9 (ITGA9) associates with beta-1 (ITGB1) (Probable). Integrin ITGA9:ITGB1 interacts with FBLN5 (via N-terminus) (PubMed:11805835). {ECO:0000269|PubMed:11805835, ECO:0000305|PubMed:11805835}. +Q80WT0 JPH4_MOUSE Junctophilin-4 (JP-4) (Junctophilin-like 1 protein) 628 66,000 Alternative sequence (2); Chain (1); Compositional bias (1); Repeat (8); Topological domain (1); Transmembrane (1) TRANSMEM 607 628 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 1 606 Cytoplasmic. {ECO:0000255}. FUNCTION: Junctophilins contribute to the formation of junctional membrane complexes (JMCs) which link the plasma membrane with the endoplasmic or sarcoplasmic reticulum in excitable cells. Provides a structural foundation for functional cross-talk between the cell surface and intracellular calcium release channels. JPH4 is brain-specific and appears to have an active role in certain neurons involved in motor coordination and memory. {ECO:0000269|PubMed:16809425}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:16809425}; Single-pass type IV membrane protein {ECO:0000269|PubMed:16809425}. Note=Localized predominantly on the plasma membrane. The transmembrane domain is anchored in endoplasmic reticulum membrane, while the N-terminal part associates with the plasma membrane (By similarity). {ECO:0000250}. DOMAIN: The MORN (membrane occupation and recognition nexus) repeats contribute to the plasma membrane binding, possibly by interacting with phospholipids. {ECO:0000250}. TISSUE SPECIFICITY: Specifically expressed in brain. Highest levels in the olfactory tubercle, caudate putamen, nucleus accumbens, hippocampal formation, piriform cortex and cerebellar cortex. Expressed in disctete neurons sites. In hippocampal formation, expressed in dendrites of hippocampal pyramidal and denate granule cells. In cerebellum, it is highly expressed in Purkinje cells, while it is weakly expressed in granular cells. {ECO:0000269|PubMed:14559359, ECO:0000269|PubMed:16809425}. +Q3MI48 JSPR1_MOUSE Junctional sarcoplasmic reticulum protein 1 (Junctional-face membrane protein of 45 kDa homolog) (JP-45) 332 36,093 Alternative sequence (2); Chain (1); Compositional bias (2); Frameshift (1); Modified residue (3); Region (1); Sequence conflict (2) FUNCTION: Involved in skeletal muscle excitation/contraction coupling (EC), probably acting as a regulator of the voltage-sensitive calcium channel CACNA1S (By similarity). EC is a physiological process whereby an electrical signal (depolarization of the plasma membrane) is converted into a chemical signal, a calcium gradient, by the opening of ryanodine receptor calcium release channels. May regulate CACNA1S membrane targeting and activity. {ECO:0000250, ECO:0000269|PubMed:16423849, ECO:0000269|PubMed:16638807}. SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane. Endoplasmic reticulum membrane. Note=Colocalizes with ryanodine receptors at the sarcoplasmic reticulum triad membranes. SUBUNIT: Interacts with CACNA1S, CACNB1 and calsequestrin. {ECO:0000269|PubMed:12871958, ECO:0000269|PubMed:16638807}. TISSUE SPECIFICITY: Specifically expressed in skeletal muscle. Detected in skeletal muscle and tongue (at protein level). {ECO:0000269|PubMed:12871958}. +E9Q0C6 K1210_MOUSE Acrosomal protein KIAA1210 1637 181,033 Chain (1) SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:28203736}. Note=Localizes to the sex body in spermatocyte, acrosome, and near the ectoplasmic specialization. {ECO:0000269|PubMed:28203736}. SUBUNIT: Interacts with TOP2B. {ECO:0000269|PubMed:28203736}. TISSUE SPECIFICITY: Predominantly expressed in testis (at protein level). {ECO:0000269|PubMed:28203736}. +Q5SZV5 K0319_MOUSE Dyslexia-associated protein KIAA0319 homolog 1081 117,988 Chain (1); Domain (6); Erroneous initiation (1); Glycosylation (10); Modified residue (1); Motif (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 965 985 Helical. {ECO:0000255}. TOPO_DOM 23 964 Extracellular. {ECO:0000255}.; TOPO_DOM 986 1081 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in neuronal migration during development of the cerebral neocortex. May function in a cell autonomous and a non-cell autonomous manner and play a role in appropriate adhesion between migrating neurons and radial glial fibers. May also regulate growth and differentiation of dendrites (By similarity). {ECO:0000250}. PTM: N-glycosylated. {ECO:0000250}.; PTM: O-glycosylated. {ECO:0000250}.; PTM: Shedding of the extracellular domain and intramembrane cleavage produce several proteolytic products. The intramembrane cleavage releases a soluble cytoplasmic polypeptide that translocates to the nucleolus (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q5VV43}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q5VV43}. Early endosome membrane {ECO:0000250|UniProtKB:Q5VV43}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q5VV43}. SUBUNIT: Homodimer. Interacts with AP2M1; required for clathrin-mediated endocytosis (By similarity). {ECO:0000250}. +Q3UZV7 K132L_MOUSE UPF0577 protein KIAA1324-like homolog (Estrogen-induced gene 121-like protein) (EIG121L) 1028 113,660 Alternative sequence (9); Chain (1); Disulfide bond (3); Erroneous translation (1); Frameshift (1); Glycosylation (3); Modified residue (1); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 929 949 Helical. {ECO:0000255}. TOPO_DOM 48 928 Extracellular. {ECO:0000255}.; TOPO_DOM 950 1028 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q8BWG4 K1755_MOUSE Uncharacterized protein KIAA1755 homolog 1187 129,087 Chain (1); Sequence conflict (1) +Q8C4P0 K1958_MOUSE Uncharacterized protein KIAA1958 homolog 716 79,148 Alternative sequence (1); Chain (1); Cross-link (5); Frameshift (1); Modified residue (1) +P08730 K1C13_MOUSE Keratin, type I cytoskeletal 13 (47 kDa cytokeratin) (Cytokeratin-13) (CK-13) (Keratin-13) (K13) 437 47,754 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (1); Modified residue (2); Region (7) PTM: O-glycosylated; glycans consist of single N-acetylglucosamine residues. {ECO:0000250}. SUBUNIT: Heterotetramer of two type I and two type II keratins. Keratin-4 is generally associated with keratin-13 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the suprabasal layers of internal stratified squamous epithelia that line the oral cavity and the upper digestive tract, including tongue and esophagus. {ECO:0000269|PubMed:1695590}. +Q8K039 K1143_MOUSE Uncharacterized protein KIAA1143 homolog 155 17,479 Chain (1); Modified residue (5); Sequence conflict (1) +Q61414 K1C15_MOUSE Keratin, type I cytoskeletal 15 (Cytokeratin-15) (CK-15) (Keratin-15) (K15) 452 49,138 Chain (1); Compositional bias (3); Cross-link (3); Domain (1); Modified residue (8); Region (7); Sequence conflict (3) FUNCTION: In the absence of KRT14, makes a bona fide, but ultrastructurally distinct keratin filament network with KRT5. {ECO:0000269|PubMed:10623468, ECO:0000269|PubMed:7539810}. SUBUNIT: Heterotetramer of two type I and two type II keratins. Interacts with NOD2 (By similarity). {ECO:0000250|UniProtKB:P19012}. TISSUE SPECIFICITY: Expressed strongly in the basal cell layer at the tips of rete-like prominences (RLPs) of adult dorsal tongue, outer root sheath (ORS) of hair follicle and skin epidermis (at protein level). {ECO:0000269|PubMed:10623468, ECO:0000269|PubMed:14506658}. +P15945 K1KB5_MOUSE Kallikrein 1-related peptidase b5 (EC 3.4.21.35) (Glandular kallikrein K5) (mGK-5) (Tissue kallikrein-5) 261 28,748 Active site (3); Chain (1); Disulfide bond (5); Domain (1); Glycosylation (1); Propeptide (1); Signal peptide (1) FUNCTION: Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin. +P07628 K1KB8_MOUSE Kallikrein 1-related peptidase b8 (EC 3.4.21.35) (Glandular kallikrein K8) (mGK-8) (Tissue kallikrein-8) 261 28,531 Active site (3); Chain (1); Disulfide bond (5); Domain (1); Glycosylation (1); Propeptide (1); Signal peptide (1) FUNCTION: Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin. +Q6RHW0 K1C9_MOUSE Keratin, type I cytoskeletal 9 (Cytokeratin-9) (CK-9) (Keratin-9) (K9) 743 72,495 Chain (1); Compositional bias (3); Domain (1); Modified residue (4); Region (7); Sequence conflict (7) FUNCTION: May serve an important special function either in the mature palmar and plantar skin tissue or in the morphogenetic program of the formation of these tissues. Plays a role in keratin filament assembly (By similarity). Plays an essential role in the correct development of sperm. {ECO:0000250|UniProtKB:P35527, ECO:0000269|PubMed:16015579}. SUBUNIT: Heterotetramer of two type I and two type II keratins. {ECO:0000305}. TISSUE SPECIFICITY: Expressed in footpad epidermis and testis (at protein level). {ECO:0000269|PubMed:16015579}. +Q61765 K1H1_MOUSE Keratin, type I cuticular Ha1 (HKA-1) (Hair keratin, type I Ha1) (Keratin-31) (K31) 416 47,117 Chain (1); Domain (1); Region (7); Sequence conflict (1); Site (1) +Q6IFZ9 K2C74_MOUSE Keratin, type II cytoskeletal 74 (Keratin-74) (K74) (Type-II keratin Kb37) 495 54,747 Chain (1); Compositional bias (2); Domain (1); Region (7); Site (1) FUNCTION: Has a role in hair formation. Specific component of keratin intermediate filaments in the inner root sheath (IRS) of the hair follicle (By similarity). {ECO:0000250|UniProtKB:Q7RT57}. SUBUNIT: Heterotetramer of two type I and two type II keratins. {ECO:0000305}. TISSUE SPECIFICITY: Expressed in epidermis with a particularly strong staining in the nail matrix, nail bed and hyponychium (at protein level). {ECO:0000269|PubMed:24714551}. +Q8BGZ7 K2C75_MOUSE Keratin, type II cytoskeletal 75 (Cytokeratin-75) (CK-75) (Keratin-6 hair follicle) (mK6hf) (Keratin-75) (K75) (Type II keratin-K6hf) (Type-II keratin Kb18) 551 59,741 Chain (1); Compositional bias (1); Domain (1); Mutagenesis (1); Region (7); Site (1) FUNCTION: Plays a central role in hair and nail formation. Essential component of keratin intermediate filaments in the companion layer of the hair follicle (By similarity). {ECO:0000250, ECO:0000269|PubMed:17851587}. SUBUNIT: Heterodimer of a type I and a type II keratin (By similarity). May associate with KRT17. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the companion layer and upper germinative matrix region of the hair follicle and the medulla of the hair shaft. Also expressed in epithelia of the nail bed and fungiform papillae of dorsal tongue epithelium (at protein level). {ECO:0000269|PubMed:11489919, ECO:0000269|PubMed:14675170, ECO:0000269|PubMed:17851587}. +P15946 K1B11_MOUSE Kallikrein 1-related peptidase b11 (EC 3.4.21.35) (Glandular kallikrein K11) (mGK-11) (Tissue kallikrein-11) 261 28,727 Active site (3); Chain (1); Disulfide bond (5); Domain (1); Glycosylation (1); Propeptide (1); Signal peptide (1) FUNCTION: Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin. +P04071 K1B16_MOUSE Kallikrein 1-related peptidase b16 (EC 3.4.21.54) (Gamma-renin, submandibular gland) (Glandular kallikrein K16) (mGK-16) 261 28,722 Active site (3); Chain (1); Disulfide bond (5); Domain (1); Glycosylation (1); Propeptide (1); Sequence conflict (2); Signal peptide (1) +Q569E4 MENT_MOUSE Protein MENT (Methylated in normal thymocytes protein) 350 38,118 Chain (1); Signal peptide (1) FUNCTION: Involved in control of cellular proliferation. Onconcogenic modifier contributing to the tumor suppressor function of DNMT3B. {ECO:0000269|PubMed:22133874}. PTM: Phosphorylation sites are present in the extracellular medium. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: High expression in testis, but low in other tissues. {ECO:0000269|PubMed:22133874}. +P15948 K1B22_MOUSE Kallikrein 1-related peptidase b22 (EC 3.4.21.35) (Beta-NGF-endopeptidase) (Epidermal growth factor-binding protein type A) (EGF-BP A) (Glandular kallikrein K22) (mGK-22) (Nerve growth factor beta chain endopeptidase) (Tissue kallikrein 22) 259 28,384 Active site (3); Chain (1); Disulfide bond (5); Domain (1); Glycosylation (1); Propeptide (1); Signal peptide (1) FUNCTION: Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin. +P36369 K1B26_MOUSE Kallikrein 1-related peptidase b26 (EC 3.4.21.35) (Glandular kallikrein K26) (mGK-26) (Prorenin-converting enzyme 2) (PRECE-2) (Tissue kallikrein 26) 261 28,463 Active site (3); Chain (1); Disulfide bond (5); Domain (1); Glycosylation (1); Propeptide (1); Sequence conflict (4); Signal peptide (1) FUNCTION: Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin.; FUNCTION: Prorenin-converting enzyme cleaves mouse REN-2 prorenin at a dibasic site to yield mature renin. +P11679 K2C8_MOUSE Keratin, type II cytoskeletal 8 (Cytokeratin endo A) (Cytokeratin-8) (CK-8) (Keratin-8) (K8) (Type-II keratin Kb8) 490 54,565 Chain (1); Compositional bias (1); Cross-link (12); Domain (1); Erroneous initiation (1); Modified residue (39); Region (8); Sequence conflict (12); Site (1) FUNCTION: Together with KRT19, helps to link the contractile apparatus to dystrophin at the costameres of striated muscle. {ECO:0000250}. PTM: Phosphorylation on serine residues is enhanced during EGF stimulation and mitosis. Ser-80 phosphorylation plays an important role in keratin filament reorganization (By similarity). {ECO:0000250}.; PTM: O-glycosylated. O-GlcNAcylation at multiple sites increases solubility, and decreases stability by inducing proteasomal degradation (By similarity). {ECO:0000250}.; PTM: O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Nucleus matrix {ECO:0000250}. SUBUNIT: Heterotetramer of two type I and two type II keratins. KRT8 associates with KRT18. Associates with KRT20. Interacts with PNN. When associated with KRT19, interacts with DMD. Interacts with TCHP. Interacts with APEX1 (By similarity). Interacts with GPER1 (By similarity). Interacts with EPPK1 (PubMed:25617501). {ECO:0000250, ECO:0000269|PubMed:25617501}. TISSUE SPECIFICITY: Expressed in abundance in the epithelia of colon, bladder, ileum, and stomach, with lower expression observed in earskin (at protein level). Also expressed in pancreas, liver, dudenum and jejunum. {ECO:0000269|PubMed:12857878}. +P28825 MEP1A_MOUSE Meprin A subunit alpha (EC 3.4.24.18) (Endopeptidase-2) (MEP-1) 747 84,231 Active site (1); Chain (1); Disulfide bond (8); Domain (4); Erroneous initiation (2); Glycosylation (9); Metal binding (3); Mutagenesis (5); Propeptide (1); Sequence conflict (4); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 714 741 Helical. {ECO:0000255}. TOPO_DOM 65 713 Extracellular. {ECO:0000255}.; TOPO_DOM 742 747 Cytoplasmic. {ECO:0000255}. PTM: N-glycosylated; contains GlcNAc, galactose, mannose and a small amount of fucose. {ECO:0000269|PubMed:17040911, ECO:0000269|PubMed:1894622}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Homotetramer consisting of disulfide-linked alpha subunits, homooligomer consisting of disulfide-linked alpha subunit homodimers, or heterotetramer of two alpha and two beta subunits formed by non-covalent association of two disulfide-linked heterodimers. Genetic factors determine which oligomer(s) will be formed (strain-specific). Interacts with MBL2 through its carbohydrate moiety. This interaction may inhibit its catalytic activity. {ECO:0000269|PubMed:16116208, ECO:0000269|PubMed:17040911, ECO:0000269|PubMed:1929422}. TISSUE SPECIFICITY: Kidney, intestinal brush borders and salivary ducts. +Q61847 MEP1B_MOUSE Meprin A subunit beta (EC 3.4.24.63) (Endopeptidase-2) (Meprin B) 704 79,501 Active site (1); Alternative sequence (1); Chain (1); Disulfide bond (9); Domain (4); Glycosylation (9); Metal binding (3); Propeptide (1); Sequence conflict (5); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 655 678 Helical. {ECO:0000255}. TOPO_DOM 21 654 Extracellular. {ECO:0000255}.; TOPO_DOM 679 704 Cytoplasmic. {ECO:0000255}. FUNCTION: Membrane metallopeptidase that sheds many membrane-bound proteins. Exhibits a strong preference for acidic amino acids at the P1' position (PubMed:11278902). Known substrates include: FGF19, VGFA, IL1B, IL18, procollagen I and III, E-cadherin, KLK7, gastrin, ADAM10, tenascin-C. The presence of several pro-inflammatory cytokine among substrates implicate MEP1B in inflammation. It is also involved in tissue remodeling due to its capability to degrade extracellular matrix components (By similarity). {ECO:0000250|UniProtKB:Q16820, ECO:0000269|PubMed:11278902}. PTM: Proteolytically activated by trypsin in the intestinal lumen and kallikrein-related peptidases in other tissues. {ECO:0000250}.; PTM: N-glycosylated; contains high mannose and/or complex biantennary structures. {ECO:0000269|PubMed:1894622}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q16820}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q16820}. Secreted {ECO:0000250|UniProtKB:Q16820}. Note=Homodimers are essentially membrane bound but may also be shed from the surface by ADAM-10 and ADAM-17. {ECO:0000250|UniProtKB:Q16820}. SUBUNIT: Homotetramer consisting of disulfide-linked beta subunits, or heterotetramer of two alpha and two beta subunits formed by non-covalent association of two disulfide-linked heterodimers. Interacts with MBL2 through its carbohydrate moiety. This interaction may inhibit its catalytic activity. {ECO:0000269|PubMed:16116208, ECO:0000269|PubMed:1929422}. TISSUE SPECIFICITY: Isoform 1 is expressed in kidney, intestinal brush borders, and salivary ducts. Isoform 2 has been found in carcinoma cells. +Q99J09 MEP50_MOUSE Methylosome protein 50 (MEP-50) (WD repeat-containing protein 77) 342 36,943 Chain (1); Modified residue (1); Repeat (7); Sequence conflict (2) FUNCTION: Non-catalytic component of the methylosome complex, composed of PRMT5, WDR77 and CLNS1A, which modifies specific arginines to dimethylarginines in several spliceosomal Sm proteins and histones. This modification targets Sm proteins to the survival of motor neurons (SMN) complex for assembly into small nuclear ribonucleoprotein core particles. Might play a role in transcription regulation. The methylosome complex also methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the interaction with Tudor domain-containing proteins and subsequent localization to the meiotic nuage (PubMed:19584108). {ECO:0000250|UniProtKB:Q9BQA1, ECO:0000269|PubMed:19584108}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BQA1}. Cytoplasm {ECO:0000250|UniProtKB:Q9BQA1}. SUBUNIT: Component of the methylosome complex composed of PRMT5, WDR77 and CLNS1A (By similarity). Found in a complex composed of PRMT5, WDR77 and RIOK1 (By similarity). RIOK1 and CLNS1A bound directly to PRMT5 at the same binding site, in a mutually exclusive manner, which allows the recruitment of distinct methylation substrates, such as nucleolin/NCL and Sm proteins, respectively (By similarity). Found in a complex with the component of the methylosome, PRMT5, CLNS1A, WDR77, PRMT1 and ERH. Directly interacts with PRMT5, as well as with several Sm proteins, including SNRPB and SNRPD2 and, more weakly, SNRPD3 and SNRPE. Forms a compact hetero-octamer with PRMT5, decorating the outer surface of a PRMT5 tetramer. Interacts with SUZ12 and histone H2A/HIST2H2AC, but not with histones H2B, H3 nor H4 (PubMed:16712789). Interacts with CTDP1 and LSM11. Interacts with APEX1, AR and NKX3-1. Interacts with CHTOP. {ECO:0000250|UniProtKB:Q9BQA1, ECO:0000269|PubMed:16712789}. +Q9ERE7 MESD_MOUSE LRP chaperone MESD (LDLR chaperone MESD) (Mesoderm development candidate 2) (Mesoderm development protein) 224 25,207 Beta strand (9); Chain (1); Erroneous initiation (1); Frameshift (1); Glycosylation (1); Helix (8); Motif (1); Region (2); Sequence conflict (1); Signal peptide (1); Turn (1) FUNCTION: Chaperone specifically assisting the folding of beta-propeller/EGF modules within the family of low-density lipoprotein receptors (LDLRs). Acts as a modulator of the Wnt pathway through chaperoning the coreceptors of the canonical Wnt pathway, LRP5 and LRP6, to the plasma membrane. Essential for specification of embryonic polarity and mesoderm induction (PubMed:12581525). Plays an essential role in neuromuscular junction (NMJ) formation by promoting cell-surface expression of LRP4 (PubMed:24140340). May regulate phagocytosis of apoptotic retinal pigment epithelium (RPE) cells (PubMed:27184668). {ECO:0000269|PubMed:12581525, ECO:0000269|PubMed:21397183, ECO:0000269|PubMed:24140340, ECO:0000269|PubMed:27184668}. SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:12581525}. Note=Released from apoptotic cells and shed photoreceptor outer segments (PubMed:27184668). {ECO:0000269|PubMed:27184668}. SUBUNIT: Monomer. Interacts with LRP5; the interaction prevents LRP5 from forming aggregates and chaperones LRP6 to the plasma membrane. Interacts with LRP6; the interaction prevents LRP6 from forming aggregates and chaperones LRP6 to the plasma membrane. Interacts with LRP4; the interaction promotes glycosylation of LRP4 and its cell-surface expression (PubMed:24140340). {ECO:0000269|PubMed:12581525, ECO:0000269|PubMed:17342452, ECO:0000269|PubMed:21397184, ECO:0000269|PubMed:24140340}. DOMAIN: The chaperone domain provides a folding template for proper folding of the beta-propeller (BP) domains of LRP5/6. {ECO:0000269|PubMed:21397183}.; DOMAIN: The escort domain ensures LRP5/6 safe-trafficking from the ER to the Golgi by preventing premature ligand-binding. {ECO:0000269|PubMed:21397183}. TISSUE SPECIFICITY: Expressed in many tissues, but not in skeletal muscles (PubMed:11247670). In the retina expressed in retinal ganglion cells, inner and outer plexiform layers, photoreceptor inner and outer segments and retinal pigment epithelium (at protein level) (PubMed:27184668). {ECO:0000269|PubMed:11247670, ECO:0000269|PubMed:27184668}. +Q9CZ09 MET18_MOUSE Histidine protein methyltransferase 1 homolog (Methyltransferase-like protein 18) (EC 2.1.1.-) 362 40,448 Chain (1); Modified residue (2); Sequence conflict (1) FUNCTION: Probable histidine methyltransferase. {ECO:0000250}. SUBUNIT: Interacts with GRWD1, RPL3 and members of the heat shock protein 90 and 70 families; these proteins may possibly be methylation substrates for the enzyme. {ECO:0000250}. +Q8R1C6 MET22_MOUSE Methyltransferase-like protein 22 (EC 2.1.1.-) 393 43,586 Chain (1); Frameshift (1); Modified residue (1) FUNCTION: Protein N-lysine methyltransferase. In vitro methylates KIN (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with members of the heat shock protein 90 and 70 families; these proteins probably are methylation substrates. {ECO:0000250}. +A2AA28 MET23_MOUSE Methyltransferase-like protein 23 (EC 2.1.1.-) 253 28,289 Chain (1); Erroneous initiation (2); Sequence conflict (1); Transmembrane (1) TRANSMEM 62 79 Helical. {ECO:0000255}. FUNCTION: Probable methyltransferase. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Note=Detected in cytoplasmic membrane-like structures. {ECO:0000250}. SUBUNIT: Interacts with HSPA5, HSP90B1, TUBULIN, UGGT1 and UGGT2. {ECO:0000250}. +Q8CCB5 MET24_MOUSE Methyltransferase-like protein 24 (EC 2.1.1.-) 363 40,631 Chain (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q6NXH8 MET25_MOUSE Methyltransferase-like protein 25 (EC 2.1.1.-) 597 66,736 Chain (1); Sequence conflict (2) FUNCTION: Putative methyltransferase. {ECO:0000250}. +Q9DD20 MET7B_MOUSE Methyltransferase-like protein 7B (EC 2.1.1.-) 244 28,049 Chain (1); Erroneous initiation (1); Signal peptide (1) FUNCTION: Probable methyltransferase. {ECO:0000250}. +Q91X83 METK1_MOUSE S-adenosylmethionine synthase isoform type-1 (AdoMet synthase 1) (EC 2.5.1.6) (Methionine adenosyltransferase 1) (MAT 1) 396 43,509 Binding site (9); Chain (1); Disulfide bond (1); Metal binding (2); Modified residue (1); Nucleotide binding (3); Region (1) Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. FUNCTION: Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate. {ECO:0000269|PubMed:8314764}. PTM: S-nitrosylation of Cys-121 inactivates the enzyme. {ECO:0000250|UniProtKB:P13444}.; PTM: An intrachain disulfide bond can be formed. The protein structure shows that the relevant Cys residues are in a position that would permit formation of a disulfide bond. {ECO:0000250|UniProtKB:P13444}. SUBUNIT: Homotetramer (MAT-I); dimer of dimers. Homodimer (MAT-III). {ECO:0000250|UniProtKB:P13444}. +Q3THS6 METK2_MOUSE S-adenosylmethionine synthase isoform type-2 (AdoMet synthase 2) (EC 2.5.1.6) (Methionine adenosyltransferase 2) (MAT 2) 395 43,689 Binding site (9); Chain (1); Cross-link (2); Metal binding (2); Modified residue (3); Nucleotide binding (3); Region (1); Sequence conflict (4) Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. FUNCTION: Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate. {ECO:0000250|UniProtKB:P31153}. SUBUNIT: Heterotrimer; composed of a catalytic MAT2A homodimer that binds one regulatory MAT2B chain. Heterohexamer; composed of a central, catalytic MAT2A homotetramer flanked on either side by a regulatory MAT2B chain. {ECO:0000250|UniProtKB:P31153}. +Q9Z2T1 KCNK7_MOUSE Potassium channel subfamily K member 7 (Double-pore K(+) channel 3) (Neuromuscular two p domain potassium channel) (Putative potassium channel DP3) 307 32,199 Chain (1); Glycosylation (1); Intramembrane (2); Sequence conflict (5); Topological domain (3); Transmembrane (4) INTRAMEM 92 118 Pore-forming; Name=Pore-forming 1. {ECO:0000255}.; INTRAMEM 199 227 Pore-forming; Name=Pore-forming 2. {ECO:0000255}. TRANSMEM 11 31 Helical. {ECO:0000255}.; TRANSMEM 120 140 Helical. {ECO:0000255}.; TRANSMEM 173 193 Helical. {ECO:0000255}.; TRANSMEM 233 253 Helical. {ECO:0000255}. TOPO_DOM 1 10 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 141 172 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 254 307 Cytoplasmic. {ECO:0000255}. FUNCTION: Probable potassium channel subunit. No channel activity observed in vitro as protein remains in the endoplasmic reticulum. May need to associate with an as yet unknown partner in order to reach the plasma membrane. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Homodimer. {ECO:0000305}. TISSUE SPECIFICITY: Detected in embryo, eye, lung and liver. Weakly expressed in colon, testis, atria, kidney, intestine, bladder, uterus, ovary, salivary gland, thymus and brain stem. Not detected in brain, cerebellum, spinal cord, heart, ventricle, skeletal muscle, liver, placenta and pancreas. In the eye, highly expressed in the retinal ganglion cell layer and inner nuclear layer. +Q9CQU8 IMP1L_MOUSE Mitochondrial inner membrane protease subunit 1 (EC 3.4.21.-) (IMP1-like protein) 166 18,502 Active site (2); Chain (1); Sequence conflict (2) FUNCTION: Catalyzes the removal of transit peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space. Known to process the nuclear encoded protein DIABLO (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}. SUBUNIT: Heterodimer of 2 subunits, IMMPL1 and IMMPL2. {ECO:0000250}. +Q9QXV3 ING1_MOUSE Inhibitor of growth protein 1 279 32,109 Alternative sequence (1); Binding site (4); Chain (1); Cross-link (1); Metal binding (8); Region (1); Sequence conflict (1); Zinc finger (1) FUNCTION: Isoform 1 inhibits p53-dependent transcriptional activation and may function as an oncoprotein. Isoform 2 acts as a negative growth regulator by cooperating with p53 in transcriptional activation of p53-responsive genes and may act as a tumor suppressor. {ECO:0000269|PubMed:10542254}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with H3K4me3 and to a lesser extent with H3K4me2. Isoform 2 interacts with RSL1D1. {ECO:0000250|UniProtKB:Q9UK53}. DOMAIN: The PHD-type zinc finger mediates the binding to H3K4me3. {ECO:0000250}.; DOMAIN: The polybasic region (PBR) is responsive to the binding to phosphoinositides (PtdInsPs), including phosphatidylinositol 5-phosphate (PtdIns(5)P). {ECO:0000250|UniProtKB:Q9UK53}. TISSUE SPECIFICITY: In the adult, widely expressed with highest levels in thymus and testis. {ECO:0000269|PubMed:10542254}. +Q04998 INHBA_MOUSE Inhibin beta A chain (Activin beta-A chain) 424 47,392 Chain (1); Disulfide bond (5); Glycosylation (1); Propeptide (1); Signal peptide (1) FUNCTION: Inhibins and activins inhibit and activate, respectively, the secretion of follitropin by the pituitary gland. Inhibins/activins are involved in regulating a number of diverse functions such as hypothalamic and pituitary hormone secretion, gonadal hormone secretion, germ cell development and maturation, erythroid differentiation, insulin secretion, nerve cell survival, embryonic axial development or bone growth, depending on their subunit composition. Inhibins appear to oppose the functions of activins. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Dimeric, linked by one or more disulfide bonds. Inhibin A is a dimer of alpha and beta-A. Inhibin B is a dimer of alpha and beta-B. Activin A is a homodimer of beta-A. Activin B is a homodimer of beta-B. Activin AB is a dimer of beta-A and beta-B. Interacts with FST and FSTL3 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Uterus, ovary and liver. +Q80V26 IMPA3_MOUSE Inositol monophosphatase 3 (IMP 3) (IMPase 3) (EC 3.1.3.25) (EC 3.1.3.7) (Golgi 3-prime phosphoadenosine 5-prime phosphate 3-prime phosphatase) (Golgi-resident PAP phosphatase) (gPAPP) (Inositol monophosphatase domain-containing protein 1) (Inositol-1(or 4)-monophosphatase 3) (Myo-inositol monophosphatase A3) 356 38,616 Binding site (2); Chain (1); Glycosylation (1); Metal binding (6); Modified residue (1); Region (1); Topological domain (2); Transmembrane (1) TRANSMEM 13 33 Helical. {ECO:0000255}. TOPO_DOM 1 12 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 34 356 Lumenal. {ECO:0000255}. Polyol metabolism; myo-inositol biosynthesis; myo-inositol from D-glucose 6-phosphate: step 2/2. FUNCTION: May play a role in the formation of skeletal elements derived through endochondral ossification, possibly by clearing adenosine 3',5'-bisphosphate produced by Golgi sulfotransferases during glycosaminoglycan sulfation. {ECO:0000269|PubMed:18695242}. PTM: Contains N-linked glycan resistant to endoglycosydase H. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:18695242}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. +P43430 MCPT8_MOUSE Mast cell protease 8 (mMCP-8) (EC 3.4.21.-) 247 27,122 Active site (3); Chain (1); Disulfide bond (3); Domain (1); Glycosylation (5); Propeptide (1); Sequence conflict (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Cytoplasmic granule {ECO:0000250}. Note=Secretory granules. {ECO:0000250}. +O08717 INHBE_MOUSE Inhibin beta E chain (Activin beta-E chain) 350 39,002 Chain (1); Disulfide bond (5); Glycosylation (1); Propeptide (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Inhibins and activins inhibit and activate, respectively, the secretion of follitropin by the pituitary gland. Inhibins/activins are involved in regulating a number of diverse functions such as hypothalamic and pituitary hormone secretion, gonadal hormone secretion, germ cell development and maturation, erythroid differentiation, insulin secretion, nerve cell survival, embryonic axial development or bone growth, depending on their subunit composition. Inhibins appear to oppose the functions of activins. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Homodimeric or heterodimeric through association with alpha and beta subunits, linked by one or more disulfide bonds. Inhibins are heterodimers of one alpha and one beta subunit. Activins are homo- or heterodimers of beta subunits only (By similarity). {ECO:0000250}. +O88174 MCP_MOUSE Membrane cofactor protein (CD antigen CD46) 365 40,881 Alternative sequence (2); Chain (1); Disulfide bond (6); Domain (4); Glycosylation (6); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 330 350 Helical. {ECO:0000255}. TOPO_DOM 45 329 Extracellular. {ECO:0000255}.; TOPO_DOM 351 365 Cytoplasmic. {ECO:0000255}. FUNCTION: May be involved in the fusion of the spermatozoa with the oocyte during fertilization. {ECO:0000269|PubMed:12640142}. PTM: May be O-glycosylated. {ECO:0000250}.; PTM: N-glycosylated. {ECO:0000269|PubMed:12640142}. SUBCELLULAR LOCATION: Isoform 1: Cytoplasmic vesicle, secretory vesicle, acrosome inner membrane; Single-pass type I membrane protein. Note=Inner acrosomal membrane of spermatozoa.; SUBCELLULAR LOCATION: Isoform 2: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Present only in testis (at protein level). {ECO:0000269|PubMed:12640142, ECO:0000269|PubMed:9461505, ECO:0000269|PubMed:9799332}. +Q9D168 INT12_MOUSE Integrator complex subunit 12 (Int12) (PHD finger protein 22) 461 48,568 Beta strand (5); Chain (1); Compositional bias (1); Cross-link (2); Helix (3); Modified residue (1); Turn (1); Zinc finger (1) FUNCTION: Component of the Integrator complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes. Mediates recruitment of cytoplasmic dynein to the nuclear envelope, probably as component of the INT complex. {ECO:0000250|UniProtKB:Q96CB8}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96CB8}. SUBUNIT: Belongs to the multiprotein complex Integrator, at least composed of INTS1, INTS2, INTS3, INTS4, INTS5, INTS6, INTS7, INTS8, INTS9/RC74, INTS10, INTS11/CPSF3L and INTS12. {ECO:0000250|UniProtKB:Q96CB8}. +Q80UK8 INT2_MOUSE Integrator complex subunit 2 (Int2) 1198 133,515 Alternative sequence (2); Chain (1); Erroneous initiation (1); Sequence conflict (8); Transmembrane (1) TRANSMEM 421 437 Helical. {ECO:0000255}. FUNCTION: Component of the Integrator (INT) complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes. Mediates recruitment of cytoplasmic dynein to the nuclear envelope, probably as component of the INT complex. {ECO:0000250|UniProtKB:Q9H0H0}. SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250|UniProtKB:Q9H0H0}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9H0H0}. SUBUNIT: Belongs to the multiprotein complex Integrator, at least composed of INTS1, INTS2, INTS3, INTS4, INTS5, INTS6, INTS7, INTS8, INTS9/RC74, INTS10, INTS11/CPSF3L and INTS12. {ECO:0000250|UniProtKB:Q9H0H0}. +Q8R3P6 INT14_MOUSE Integrator complex subunit 14 (von Willebrand factor A domain-containing protein 9) 515 57,237 Alternative sequence (2); Chain (1); Domain (1); Frameshift (1); Modified residue (1); Sequence conflict (2) FUNCTION: Probable component of the Integrator (INT) complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. {ECO:0000250|UniProtKB:Q9VPY0}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9VPY0}. +Q8CIM8 INT4_MOUSE Integrator complex subunit 4 (Int4) 964 108,193 Alternative sequence (3); Chain (1); Cross-link (2); Erroneous initiation (1); Frameshift (1); Modified residue (1); Repeat (8) FUNCTION: Component of the Integrator (INT) complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes. Mediates recruitment of cytoplasmic dynein to the nuclear envelope, probably as component of the INT complex. {ECO:0000250|UniProtKB:Q96HW7}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96HW7}. SUBUNIT: Belongs to the multiprotein complex Integrator, at least composed of INTS1, INTS2, INTS3, INTS4, INTS5, INTS6, INTS7, INTS8, INTS9/RC74, INTS10, INTS11/CPSF3L and INTS12. {ECO:0000250|UniProtKB:Q96HW7}. +Q8BND4 INT6L_MOUSE Integrator complex subunit 6-like (Protein DDX26B) 861 96,941 Chain (1); Domain (1); Modified residue (1) +Q5RJH2 MCTP2_MOUSE Multiple C2 and transmembrane domain-containing protein 2 878 100,178 Chain (1); Domain (3); Transmembrane (2) TRANSMEM 694 714 Helical. {ECO:0000255}.; TRANSMEM 794 814 Helical. {ECO:0000255}. FUNCTION: Might play a role in the development of cardiac outflow tract. {ECO:0000250|UniProtKB:Q6DN12}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q61153 IOD1_MOUSE Type I iodothyronine deiodinase (EC 1.21.99.4) (5DI) (DIOI) (Type 1 DI) (Type-I 5'-deiodinase) 257 29,568 Active site (1); Chain (1); Erroneous termination (1); Non-standard residue (1); Sequence conflict (7); Transmembrane (1) TRANSMEM 13 33 Helical. {ECO:0000255}. FUNCTION: Responsible for the deiodination of T4 (3,5,3',5'-tetraiodothyronine) into T3 (3,5,3'-triiodothyronine) and of T3 into T2 (3,3'-diiodothyronine). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. +Q91ZI8 IOD3_MOUSE Thyroxine 5-deiodinase (EC 1.21.99.3) (5DIII) (DIOIII) (Type 3 DI) (Type III iodothyronine deiodinase) 304 34,111 Active site (1); Beta strand (9); Chain (1); Erroneous initiation (5); Helix (6); Non-standard residue (1); Topological domain (2); Transmembrane (1); Turn (2) TRANSMEM 45 67 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 44 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 68 304 Extracellular. {ECO:0000255}. FUNCTION: Responsible for the deiodination of T4 (3,5,3',5'-tetraiodothyronine) into RT3 (3,3',5'-triiodothyronine) and of T3 (3,5,3'-triiodothyronine) into T2 (3,3'-diiodothyronine). RT3 and T2 are inactive metabolites. May play a role in preventing premature exposure of developing fetal tissues to adult levels of thyroid hormones. Can regulate circulating fetal thyroid hormone concentrations throughout gestation. Essential role for regulation of thyroid hormone inactivation during embryological development. {ECO:0000250|UniProtKB:P49897}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Endosome membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. SUBUNIT: Homodimer. May undergo minor heretodimerization with DIO1 and DIO2 (By similarity). {ECO:0000250}. +P48997 INVO_MOUSE Involucrin 467 54,919 Chain (1) FUNCTION: Part of the insoluble cornified cell envelope (CE) of stratified squamous epithelia. PTM: Substrate of transglutaminase. Specific glutamines or lysines are cross-linked to keratins, desmoplakin and to inter involucrin molecules. SUBCELLULAR LOCATION: Cytoplasm. Note=Constituent of the scaffolding of the cornified envelope. SUBUNIT: Directly or indirectly cross-linked to cornifelin (CNFN). TISSUE SPECIFICITY: Keratinocytes of epidermis and other stratified squamous epithelia. +O89019 INVS_MOUSE Inversin (Inversion of embryo turning protein) (Nephrocystin-2) 1062 117,129 Alternative sequence (9); Chain (1); Domain (2); Modified residue (1); Motif (2); Mutagenesis (2); Repeat (16); Sequence conflict (7) FUNCTION: Required for normal renal development and establishment of left-right axis. Probably acts as a molecular switch between different Wnt signaling pathways. Inhibits the canonical Wnt pathway by targeting cytoplasmic disheveled (DVL1) for degradation by the ubiquitin-proteasome. This suggests that it is required in renal development to oppose the repression of terminal differentiation of tubular epithelial cells by Wnt signaling (By similarity). Involved in the organization of apical junctions in kidney cells together with NPHP1, NPHP4 and RPGRIP1L/NPHP8. Does not seem to be strictly required for ciliogenesis. {ECO:0000250, ECO:0000269|PubMed:21565611, ECO:0000269|PubMed:9744276, ECO:0000269|PubMed:9771707}. PTM: May be ubiquitinated via its interaction with APC2.; PTM: Hydroxylated at Asn-75, most probably by HIF1AN. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Membrane; Peripheral membrane protein. Nucleus. Cytoplasm, perinuclear region. Cytoplasm, cytoskeleton, spindle. Note=Associates with several components of the cytoskeleton including ciliary, random and polarized microtubules. During mitosis, it is recruited to mitotic spindle (By similarity). Membrane localization is dependent upon cell-cell contacts and is redistributed when cell adhesion is disrupted after incubation of the cell monolayer with low-calcium/EGTA medium. Also nuclear and perinuclear. {ECO:0000250}. SUBUNIT: Interacts with microtubules. Interacts with NPHP1. Interacts with DVL1, PRICKLE (PRICKLE1 or PRICKLE2) and Strabismus (VANGL1 or VANGL2) (By similarity). Binds calmodulin via its IQ domains. Interacts with APC2. Interacts with alpha-, beta-, and gamma-catenin. Interacts with N-cadherin (CDH2). Interacts with NPHP3 (By similarity). Interacts with IQCB1; the interaction likely requires additional interactors (By similarity). Component of a complex containing at least ANKS6, INVS, NEK8 and NPHP3. ANKS6 may organize complex assembly by linking INVS and NPHP3 to NEK8 and INVS may target the complex to the proximal ciliary axoneme (By similarity). {ECO:0000250}. DOMAIN: The D-box 1 (destruction box 1) mediates the interaction with APC2, and may act as a recognition signal for degradation via the ubiquitin-proteasome pathway. TISSUE SPECIFICITY: Strongly expressed in the primary cilia of renal cells, especially in the varicosities, swellings observed in the cilia. Localizes in the node monocilia and in other 9+0 monocilia, including those of kidney epithelial cells and the pituitary gland, but it does not localize to 9+2 cilia (at protein level). In adult, it is expressed at high level in liver and kidney. Weakly or not expressed in other tissues. {ECO:0000269|PubMed:12471060, ECO:0000269|PubMed:9744276}. +Q6JPI3 MD13L_MOUSE Mediator of RNA polymerase II transcription subunit 13-like (Mediator complex subunit 13-like) (Thyroid hormone receptor-associated protein 2) (Thyroid hormone receptor-associated protein complex 240 kDa component-like) 2207 241,758 Chain (1); Compositional bias (1); Frameshift (1); Modified residue (6); Motif (2); Region (1); Sequence conflict (3) FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. This subunit may specifically regulate transcription of targets of the Wnt signaling pathway and SHH signaling pathway (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Component of the Mediator complex, which is composed of MED1, MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L, MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23, MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8 subunits form a distinct module termed the CDK8 module. Mediator containing the CDK8 module is less active than Mediator lacking this module in supporting transcriptional activation. Individual preparations of the Mediator complex lacking one or more distinct subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and TRAP (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in heart and weakly expressed in brain, spleen, lung, liver, kidney and testis. {ECO:0000269|PubMed:15145061}. +Q9WTX8 MD1L1_MOUSE Mitotic spindle assembly checkpoint protein MAD1 (Mitotic arrest deficient 1-like protein 1) (MAD1-like protein 1) 717 83,541 Alternative sequence (1); Chain (1); Coiled coil (1); Cross-link (1); Modified residue (5); Region (1) FUNCTION: Component of the spindle-assembly checkpoint that prevents the onset of anaphase until all chromosomes are properly aligned at the metaphase plate. May recruit MAD2L1 to unattached kinetochores. Has a role in the correct positioning of the septum. Required for anchoring MAD2L1 to the nuclear periphery. Binds to the TERT promoter and represses telomerase expression, possibly by interfering with MYC binding. {ECO:0000250|UniProtKB:Q9Y6D9}. PTM: Phosphorylated; by BUB1. Become hyperphosphorylated in late S through M phases or after mitotic spindle damage. {ECO:0000250|UniProtKB:Q9Y6D9}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q9Y6D9}. Nucleus envelope {ECO:0000250|UniProtKB:Q9Y6D9}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q9Y6D9}. Note=Detected at the nucleus envelope during interphase. From the beginning to the end of mitosis, it is seen to move from a diffusely nuclear distribution to the centrosome, to the spindle midzone and finally to the midbody. Detected at kinetochores during prometaphase. Colocalizes with NEK2 at the kinetochore. Colocalizes with IK at spindle poles during metaphase and anaphase. {ECO:0000250|UniProtKB:Q9Y6D9}. SUBUNIT: Homodimer. Heterodimerizes with MAD2L1 in order to form a tetrameric MAD1L1-MAD2L1 core complex. Perturbation of the original MAD1L1-MAD2L1 structure by the spindle checkpoint may decrease MAD2L1 affinity for MAD1L1. CDC20 can compete with MAD1L1 for MAD2L1 binding, until the attachment and/or tension dampen the checkpoint signal, preventing further release of MAD2L1 on to CDC20. Also able to interact with the BUB1/BUB3 complex. Interacts with NEK2. Interacts with TPR; the interactions occurs in a microtubule-independent manner. Interacts with IK. {ECO:0000250|UniProtKB:Q9Y6D9}. +Q5PSV9 MDC1_MOUSE Mediator of DNA damage checkpoint protein 1 1707 184,670 Beta strand (10); Chain (1); Compositional bias (1); Cross-link (3); Domain (3); Modified residue (51); Region (2); Sequence conflict (1); Turn (1) FUNCTION: Required for checkpoint mediated cell cycle arrest in response to DNA damage within both the S phase and G2/M phases of the cell cycle. May serve as a scaffold for the recruitment of DNA repair and signal transduction proteins to discrete foci of DNA damage marked by 'Ser-139' phosphorylation of histone H2AFX. Also required for downstream events subsequent to the recruitment of these proteins. These include phosphorylation and activation of the ATM, CHEK1 and CHEK2 kinases, and stabilization of TP53 and apoptosis. ATM and CHEK2 may also be activated independently by a parallel pathway mediated by TP53BP1 (By similarity). {ECO:0000250}. PTM: Phosphorylated upon exposure to ionizing radiation (IR), ultraviolet radiation (UV), and hydroxyurea (HU). Phosphorylation in response to IR requires ATM, NBN, and possibly CHEK2. Also phosphorylated during the G2/M phase of the cell cycle and during activation of the mitotic spindle checkpoint. Phosphorylation at Thr-4 by ATM stabilizes and enhances homodimerization via the FHA domain (By similarity). {ECO:0000250}.; PTM: Sumoylation at Lys-1461 by PIAS4 following DNA damage promotes ubiquitin-mediated degradation. {ECO:0000250}.; PTM: Ubiquitinated by RNF4, leading to proteasomal degradation; undergoes 'Lys-48'-linked polyubiquitination. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Associated with chromatin. Relocalizes to discrete nuclear foci following DNA damage, this requires phosphorylation of H2AFX. Colocalizes with APTX at sites of DNA double-strand breaks (By similarity). {ECO:0000250}. SUBUNIT: Homodimer. Interacts with several proteins involved in the DNA damage response, although not all these interactions may be direct. Interacts with CHEK2, which requires ATM-mediated phosphorylation within the FHA domain of CHEK2. Interacts constitutively with the BRCA1-BARD1 complex, SMC1A and TP53BP1. Interacts with ATM and FANCD2, and these interactions are reduced upon DNA damage. Also interacts with the PRKDC complex, composed of XRCC6/KU70, XRCC5/KU80 and PRKDC/XRCC7. This interaction may be required for PRKDC autophosphorylation, which is essential for DNA double strand break (DSB) repair. When phosphorylated by ATM, interacts with RNF8 (via FHA domain). Interacts with CEP164. When phosphorylated, interacts with APTX (via FHA-like domain) (By similarity). Interacts with H2AFX, which requires phosphorylation of H2AFX. Interacts with the MRN complex, composed of MRE11, RAD50, and NBN. {ECO:0000250, ECO:0000269|PubMed:15611643}. DOMAIN: Tandemly repeated BRCT domains are characteristic of proteins involved in DNA damage signaling. In MDC1, these repeats are required for localization to chromatin which flanks sites of DNA damage marked by 'Ser-139' phosphorylation of H2AFX (By similarity). {ECO:0000250}. +Q8BX65 MDFIC_MOUSE MyoD family inhibitor domain-containing protein (I-mfa domain-containing protein) (Kidney cell line-derived transcript 1) 247 26,094 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (3); Modified residue (2) FUNCTION: Acts as a transcriptional activator or repressor. Inhibits the transcriptional activation of Zic family proteins ZIC1, ZIC2 and ZIC3. Retains nuclear Zic proteins ZIC1, ZIC2 and ZIC3 in the cytoplasm. Modulates the expression from cellular promoters. Binds to the axin complex, resulting in an increase in the level of free beta-catenin. Affects axin-regulation of the WNT and JNK signaling pathways. {ECO:0000269|PubMed:15207726, ECO:0000269|PubMed:15465018}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Nucleus, nucleolus {ECO:0000250}. SUBUNIT: Interacts with HAND1; leading to sequester HAND1 into the nucleolus and prevent its activity (PubMed:17891141). Interacts with ZIC2 (PubMed:15207726, PubMed:15465018). The C-terminus interacts with AXIN1, the histidine-rich region of CCNT1/cyclin-T and weakly with LEF1. Interacts with CCNT2 (By similarity). {ECO:0000250|UniProtKB:Q9P1T7, ECO:0000269|PubMed:15207726, ECO:0000269|PubMed:15465018, ECO:0000269|PubMed:17891141}. DOMAIN: The cysteine-rich C-terminus is involved in its granular distribution in the cytoplasm (By similarity). The C2H2-type 3, 4 and 5 zinc finger domains are necessary for transcription activation. {ECO:0000250}. +P70331 MDFI_MOUSE MyoD family inhibitor (Myogenic repressor I-mf) 251 26,013 Alternative sequence (3); Chain (1) FUNCTION: Inhibits the transactivation activity of the Myod family of myogenic factors and represses myogenesis. Acts by associating with Myod family members and retaining them in the cytoplasm by masking their nuclear localization signals. Can also interfere with the DNA-binding activity of Myod family members. Plays an important role in trophoblast and chondrogenic differentiation. Regulates the transcriptional activity of TCF7L1/TCF3 by interacting directly with TCF7L1/TCF3 and preventing it from binding DNA. Binds to the axin complex, resulting in an increase in the level of free beta-catenin. Affects axin regulation of the WNT and JNK signaling pathways. {ECO:0000269|PubMed:11238923, ECO:0000269|PubMed:12192039, ECO:0000269|PubMed:8797820, ECO:0000269|PubMed:9799236}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. SUBUNIT: The C-terminus interacts with AXIN1 and LEF1 (PubMed:12192039). Interacts with CCNT2 (By similarity). {ECO:0000250|UniProtKB:Q99750, ECO:0000269|PubMed:12192039}. TISSUE SPECIFICITY: In the embryo, highly expressed in the sclerotome. Also expressed in the notochord, neural tube, limb buds, heart, branchial arches and head mesenchyme. In the adult, highly expressed in skeletal muscle. Expressed at lower levels in most other tissues. {ECO:0000269|PubMed:8797820}. +Q8R071 IP3KA_MOUSE Inositol-trisphosphate 3-kinase A (EC 2.7.1.127) (Inositol 1,4,5-trisphosphate 3-kinase A) (IP3 3-kinase A) (IP3K A) (InsP 3-kinase A) 459 50,935 Binding site (8); Chain (1); Modified residue (5); Nucleotide binding (1); Region (2) +P60755 MDGA2_MOUSE MAM domain-containing glycosylphosphatidylinositol anchor protein 2 (MAM domain-containing protein 1) 949 106,689 Chain (1); Disulfide bond (6); Domain (8); Glycosylation (8); Lipidation (1); Propeptide (1); Signal peptide (1) FUNCTION: May be involved in cell-cell interactions. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}. SUBUNIT: Interacts (through the Ig-like domains) with NLGN2. {ECO:0000269|PubMed:23248271, ECO:0000269|PubMed:23358245}. +A2ASA8 IPIL1_MOUSE Inositol 1,4,5-trisphosphate receptor-interacting protein-like 1 547 62,217 Chain (1); Coiled coil (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 97 117 Helical. {ECO:0000255}. TOPO_DOM 23 96 Extracellular. {ECO:0000255}.; TOPO_DOM 118 547 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q3UV16 IPIL2_MOUSE Inositol 1,4,5-trisphosphate receptor-interacting protein-like 2 535 58,665 Chain (1); Compositional bias (1); Frameshift (1); Modified residue (1); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 44 64 Helical. {ECO:0000255}. TOPO_DOM 33 43 Extracellular. {ECO:0000255}.; TOPO_DOM 65 535 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. +P63248 IPKA_MOUSE cAMP-dependent protein kinase inhibitor alpha (PKI-alpha) (cAMP-dependent protein kinase inhibitor, muscle/brain isoform) 76 7,960 Chain (1); Helix (1); Initiator methionine (1); Modified residue (1); Site (3) FUNCTION: Extremely potent competitive inhibitor of cAMP-dependent protein kinase activity, this protein interacts with the catalytic subunit of the enzyme after the cAMP-induced dissociation of its regulatory chains. TISSUE SPECIFICITY: Present at high levels in skeletal muscle and brain but is present at lower levels in heart, testis and liver. +Q04758 IPKB_MOUSE cAMP-dependent protein kinase inhibitor beta (PKI-beta) (cAMP-dependent protein kinase inhibitor, testis isoform) 92 9,682 Alternative sequence (1); Chain (1); Modified residue (1); Site (3) FUNCTION: Extremely potent competitive inhibitor of cAMP-dependent protein kinase activity, this protein interacts with the catalytic subunit of the enzyme after the cAMP-induced dissociation of its regulatory chains. +O70139 IPKG_MOUSE cAMP-dependent protein kinase inhibitor gamma (PKI-gamma) 76 7,943 Chain (1) FUNCTION: Extremely potent competitive inhibitor of cAMP-dependent protein kinase activity, this protein interacts with the catalytic subunit of the enzyme after the cAMP-induced dissociation of its regulatory chains. {ECO:0000250}. +Q7TT16 IPMK_MOUSE Inositol polyphosphate multikinase (EC 2.7.1.151) (Inositol 1,3,4,6-tetrakisphosphate 5-kinase) 396 44,453 Alternative sequence (2); Chain (1); Initiator methionine (1); Modified residue (2); Motif (1); Region (1); Sequence conflict (4) FUNCTION: Inositol phosphate kinase with a broad substrate specificity. Has a preference for inositol 1,4,5-trisphosphate (Ins(1,4,5)P3) and inositol 1,3,4,6-tetrakisphosphate (Ins(1,3,4,6)P4) (By similarity). Plays an important role in MLKL-mediated necroptosis. Produces highly phosphorylated inositol phosphates such as inositolhexakisphosphate (InsP6) which bind to MLKL mediating the release of an N-terminal auto-inhibitory region leading to its activation. Essential for activated phospho-MLKL to oligomerize and localize to the cell membrane during necroptosis (By similarity). {ECO:0000250|UniProtKB:Q8NFU5}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +Q8K0C1 IPO13_MOUSE Importin-13 (Imp13) 963 108,229 Alternative sequence (2); Chain (1); Domain (1); Repeat (20) FUNCTION: Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (By similarity). Mediates the nuclear import of UBC9, the RBM8A/MAGOH complex, PAX6 and probably other members of the paired homeobox family. Also mediates nuclear export of eIF-1A, and the cytoplasmic release of eIF-1A is triggered by the loading of import substrates onto IPO13 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Interacts with UBC9, RAN, RBM8A, eIF-1A and PAX6. {ECO:0000250}. +Q8BKC5 IPO5_MOUSE Importin-5 (Imp5) (Importin subunit beta-3) (Karyopherin beta-3) (Ran-binding protein 5) (RanBP5) 1097 123,591 Alternative sequence (1); Chain (1); Domain (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (2); Region (1); Repeat (24); Sequence conflict (4) FUNCTION: Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Mediates the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5. Binds to a beta-like import receptor binding (BIB) domain of RPL23A. In vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones. Binds to CPEB3 and mediates its nuclear import following neuronal stimulation (PubMed:22730302). {ECO:0000269|PubMed:11493596, ECO:0000269|PubMed:17143267, ECO:0000269|PubMed:22730302}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17143267}. Nucleus {ECO:0000269|PubMed:17143267}. SUBUNIT: Interacts with H2A, H2B, H3 and H4 histones (PubMed:11493596). Binds RPL23A, RPS7 and RPL5 (By similarity). Interacts with CPEB3; this mediates CPEB3 nuclear import following neuronal stimulation which enhances the interaction in a RAN-regulated manner (By similarity). {ECO:0000250|UniProtKB:O00410, ECO:0000269|PubMed:11493596}. +Q91YE6 IPO9_MOUSE Importin-9 (Imp9) (Importin-9a) (Imp9a) (Importin-9b) (Imp9b) (Ran-binding protein 9) (RanBP9) 1041 116,052 Chain (1); Domain (1); Initiator methionine (1); Modified residue (1); Sequence conflict (5) FUNCTION: Functions in nuclear protein import as nuclear transport receptor (PubMed:11823430). Serves as receptor for nuclear localization signals (NLS) in cargo substrates (PubMed:11823430). Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism (PubMed:11823430). At the nucleoplasmic side of the NPC, Ran binds to the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran (PubMed:11823430). The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (PubMed:11823430). Mediates the nuclear import of RPS7, RPL18A, RPL6, histone H2A, histone H2B and histone (PubMed:11493596). Prevents the cytoplasmic aggregation of RPS7 and RPL18A by shielding exposed basic domains (PubMed:11823430). Mediates the nuclear import of actin (PubMed:22323606). {ECO:0000269|PubMed:11493596, ECO:0000269|PubMed:11823430, ECO:0000269|PubMed:22323606}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96P70}. Nucleus {ECO:0000250|UniProtKB:Q96P70}. SUBUNIT: Interacts with PPP2R1A and PPP2R1B (By similarity). Binds with high affinity to RPS7, RPL18A and H2B histone (PubMed:11493596, PubMed:11823430). The binding is coupled to RanGTP cycles (PubMed:11493596, PubMed:11823430). May bind RPL4, RPL6, H2A, H3 and H4 histones with low affinity (PubMed:11493596, PubMed:11823430). {ECO:0000250|UniProtKB:Q96P70, ECO:0000269|PubMed:11493596, ECO:0000269|PubMed:11823430}. +Q9DCL8 IPP2_MOUSE Protein phosphatase inhibitor 2 (IPP-2) 206 23,119 Chain (1); Helix (4); Initiator methionine (1); Modified residue (10); Region (3); Sequence conflict (1) FUNCTION: Inhibitor of protein-phosphatase 1. {ECO:0000250}. PTM: Phosphorylation on Ser-45 by ATM activates PP1 by dissociating the PP1-PPP1R2 complex. Phosphorylation on Thr-74 by GSK3 activates PP1 by dissociating the PP1-PPP1R2 complex. {ECO:0000250}. SUBUNIT: Heterodimer with PP1. {ECO:0000250}. +Q3TNL8 IPRI_MOUSE Inositol 1,4,5-trisphosphate receptor-interacting protein 555 63,238 Alternative sequence (1); Chain (1); Coiled coil (1); Glycosylation (2); Sequence conflict (2); Signal peptide (1) FUNCTION: Enhances Ca(2+)-mediated inhibition of inositol 1,4,5-triphosphate receptor (ITPR) Ca(2+) release. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. SUBUNIT: Interacts with ITPR. {ECO:0000250}. +Q9D819 IPYR_MOUSE Inorganic pyrophosphatase (EC 3.6.1.1) (Pyrophosphate phospho-hydrolase) (PPase) 289 32,667 Chain (1); Initiator methionine (1); Metal binding (4); Modified residue (4) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +A6H690 IQCAL_MOUSE IQ and AAA domain-containing protein 1-like (Protein IQCA1P1) 825 95,956 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (1); Erroneous termination (1); Nucleotide binding (1); Sequence conflict (1) +A2ADZ8 IQCC_MOUSE IQ domain-containing protein C 418 46,912 Chain (1); Coiled coil (1); Domain (1) +Q9D9K8 IQCF1_MOUSE IQ domain-containing protein F1 182 21,456 Alternative sequence (1); Chain (1); Domain (2) FUNCTION: Involved in sperm capacitation and acrosome reaction. {ECO:0000269|PubMed:25380116}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:25380116}. SUBUNIT: Interacts with calmodulin. {ECO:0000269|PubMed:25380116}. TISSUE SPECIFICITY: Specifically expressed in testes and mature spermatozoa (at protein level). {ECO:0000269|PubMed:25380116}. +Q9D498 IQCF3_MOUSE IQ domain-containing protein F3 (Testis-specific IQ motif-containing protein 2) 203 23,500 Chain (1); Coiled coil (1); Domain (1) +Q9D2K4 IQCH_MOUSE IQ domain-containing protein H 1071 122,605 Alternative sequence (1); Chain (1); Domain (1); Sequence conflict (4) FUNCTION: May play a regulatory role in spermatogenesis. {ECO:0000269|PubMed:15897968}. TISSUE SPECIFICITY: Expressed in fetal and adult testis, in the spermatocytes and spermatids but not in somatic cells. {ECO:0000269|PubMed:15897968}. +Q8R0S2 IQEC1_MOUSE IQ motif and SEC7 domain-containing protein 1 961 108,015 Alternative sequence (1); Chain (1); Coiled coil (1); Domain (3); Modified residue (12); Sequence conflict (1) FUNCTION: Guanine nucleotide exchange factor for ARF1 and ARF6. Guanine nucleotide exchange factor activity is enhanced by lipid binding. Accelerates GTP binding by ARFs of all three classes. Guanine nucleotide exchange protein for ARF6, mediating internalisation of beta-1 integrin. {ECO:0000250|UniProtKB:Q6DN90}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6DN90}. Nucleus {ECO:0000250|UniProtKB:Q6DN90}. Note=At steady state, may be preferentially cytosolic. {ECO:0000250|UniProtKB:Q6DN90}. SUBUNIT: Interacts with ARF1 and ARF6. {ECO:0000250|UniProtKB:Q6DN90}. DOMAIN: The PH domain mediates interaction with lipid membranes that contain phosphatidylinositol-4,5-bisphosphate, but does not bind membranes that lack phosphatidylinositol-4,5-bisphosphate. {ECO:0000250|UniProtKB:Q6DN90}. +Q5DU25 IQEC2_MOUSE IQ motif and SEC7 domain-containing protein 2 1478 161,787 Chain (1); Coiled coil (1); Compositional bias (4); Domain (3); Modified residue (19); Sequence conflict (1) FUNCTION: Is a guanine nucleotide exchange factor for the ARF GTP-binding proteins. {ECO:0000250|UniProtKB:Q5JU85}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. +Q3TES0 IQEC3_MOUSE IQ motif and SEC7 domain-containing protein 3 1195 129,119 Chain (1); Coiled coil (1); Compositional bias (4); Domain (3); Modified residue (1); Sequence conflict (3) FUNCTION: Acts as a guanine nucleotide exchange factor (GEF) for ARF1. {ECO:0000250|UniProtKB:Q9UPP2}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UPP2}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000269|PubMed:27609886}. SUBUNIT: Interacts with DLG1 and DLG4 (By similarity). Interacts with GPHN (PubMed:27609886). {ECO:0000250|UniProtKB:Q76M68, ECO:0000269|PubMed:27609886}. TISSUE SPECIFICITY: Expressed specifically in the adult brain, but not in the fetal brain at 14 dpc. {ECO:0000269|PubMed:17981261}. +Q9JKF1 IQGA1_MOUSE Ras GTPase-activating-like protein IQGAP1 1657 188,742 Chain (1); Domain (7); Initiator methionine (1); Modified residue (5); Region (2); Sequence conflict (1) FUNCTION: Plays a crucial role in regulating the dynamics and assembly of the actin cytoskeleton. Binds to activated CDC42 but does not stimulate its GTPase activity (PubMed:16968698). It associates with calmodulin. Could serve as an assembly scaffold for the organization of a multimolecular complex that would interface incoming signals to the reorganization of the actin cytoskeleton at the plasma membrane. May promote neurite outgrowth. May play a possible role in cell cycle regulation by contributing to cell cycle progression after DNA replication arrest. {ECO:0000250|UniProtKB:P46940, ECO:0000269|PubMed:16968698}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P46940}. Nucleus {ECO:0000269|PubMed:20883816}. Cytoplasm {ECO:0000269|PubMed:20883816}. Note=Subcellular distribution is regulated by the cell cycle, nuclear levels increase at G1/S phase (PubMed:20883816). SUBUNIT: Interacts with CDC42; the interaction is demonstrated with IQGAP1 in GTP-bound and in nucleotide-free state (PubMed:16968698). Interacts with RAC1 (By similarity). Does not interact with RHOA (By similarity). Interacts with TSG101 (By similarity). Interacts with PAK6 (By similarity). {ECO:0000250|UniProtKB:P46940, ECO:0000269|PubMed:16968698}.; SUBUNIT: (Microbial infection) In case of infection, interacts with S.typhimurium protein sseI (PubMed:19956712). {ECO:0000269|PubMed:19956712}. DOMAIN: Regions C1 and C2 can either interact with nucleotide-free CDC42, or interact together. {ECO:0000250|UniProtKB:P46940}. +Q8CDK3 IQUB_MOUSE IQ and ubiquitin-like domain-containing protein 788 92,130 Chain (1); Domain (2); Sequence conflict (2) FUNCTION: May play roles in cilia formation and/or maintenance. {ECO:0000269|PubMed:21289087}. SUBUNIT: Interacts with ZMYND10. {ECO:0000250|UniProtKB:Q8NA54}. +Q8R4K2 IRAK4_MOUSE Interleukin-1 receptor-associated kinase 4 (IRAK-4) (EC 2.7.11.1) 459 50,872 Active site (1); Beta strand (1); Binding site (2); Chain (1); Domain (2); Helix (10); Modified residue (5); Nucleotide binding (2); Sequence conflict (1); Turn (1) FUNCTION: Serine/threonine-protein kinase that plays a critical role in initiating innate immune response against foreign pathogens. Involved in Toll-like receptor (TLR) and IL-1R signaling pathways. Is rapidly recruited by MYD88 to the receptor-signaling complex upon TLR activation to form the Myddosome together with IRAK2. Phosphorylates initially IRAK1, thus stimulating the kinase activity and intensive autophosphorylation of IRAK1. Phosphorylates E3 ubiquitin ligases Pellino proteins (PELI1, PELI2 and PELI3) to promote pellino-mediated polyubiquitination of IRAK1. Then, the ubiquitin-binding domain of IKBKG/NEMO binds to polyubiquitinated IRAK1 bringing together the IRAK1-MAP3K7/TAK1-TRAF6 complex and the NEMO-IKKA-IKKB complex. In turn, MAP3K7/TAK1 activates IKKs (CHUK/IKKA and IKBKB/IKKB) leading to NF-kappa-B nuclear translocation and activation. Alternatively, phosphorylates TIRAP to promote its ubiquitination and subsequent degradation. Phosphorylates NCF1 and regulates NADPH oxidase activation after LPS stimulation suggesting a similar mechanism during microbial infections (By similarity). {ECO:0000250}. PTM: Phosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Associates with MYD88 and IRAK2 to form a ternary complex called the Myddosome. Once phosphorylated, IRAK4 dissociates from the receptor complex and then associates with the TNF receptor-associated factor 6 (TRAF6), IRAK1, and PELI1; this intermediate complex is required for subsequent NF-kappa-B activation. Direct binding of SMAD6 to PELI1 prevents complex formation and hence negatively regulates IL1R-TLR signaling and eventually NF-kappa-B-mediated gene expression. Interacts with IL1RL1 (By similarity). {ECO:0000250}. +P15314 IRF1_MOUSE Interferon regulatory factor 1 (IRF-1) 329 37,319 Beta strand (6); Chain (1); Cross-link (2); DNA binding (1); Helix (3); Modified residue (1); Turn (1) FUNCTION: Transcriptional regulator which displays a remarkable functional diversity in the regulation of cellular responses. These include the regulation of IFN and IFN-inducible genes, host response to viral and bacterial infections, regulation of many genes expressed during hematopoiesis, inflammation, immune responses and cell proliferation and differentiation, regulation of the cell cycle and induction of growth arrest and programmed cell death following DNA damage. Stimulates both innate and acquired immune responses through the activation of specific target genes and can act as a transcriptional activator and repressor regulating target genes by binding to an interferon-stimulated response element (ISRE) in their promoters. Its target genes for transcriptional activation activity are: genes involved in anti-viral response, such as IFN-alpha/beta, DDX58/RIG-I, TNFSF10/TRAIL, OAS1/2, PIAS1/GBP, EIF2AK2/PKR and RSAD2/viperin; antibacterial response, such as NOS2/INOS; anti-proliferative response, such as p53/TP53, LOX and CDKN1A; apoptosis, such as BBC3/PUMA, CASP1, CASP7 and CASP8; immune response, such as IL7, IL12A/B and IL15, PTGS2/COX2 and CYBB; DNA damage responses and DNA repair, such as POLQ/POLH; MHC class I expression, such as TAP1, PSMB9/LMP2, PSME1/PA28A, PSME2/PA28B and B2M and MHC class II expression, such as CIITA. Represses genes involved in anti-proliferative response, such as BIRC5/survivin, CCNB1, CCNE1, CDK1, CDK2 and CDK4 and in immune response, such as FOXP3, IL4, ANXA2 and TLR4. Stimulates p53/TP53-dependent transcription through enhanced recruitment of EP300 leading to increased acetylation of p53/TP53. Plays an important role in immune response directly affecting NK maturation and activity, macrophage production of IL12, Th1 development and maturation of CD8+ T-cells. Also implicated in the differentiation and maturation of dendritic cells and in the suppression of regulatory T (Treg) cells development. Acts as a tumor suppressor and plays a role not only in antagonism of tumor cell growth but also in stimulating an immune response against tumor cells. {ECO:0000269|PubMed:12387893, ECO:0000269|PubMed:17018642, ECO:0000269|PubMed:18641303, ECO:0000269|PubMed:18955028, ECO:0000269|PubMed:20308629, ECO:0000269|PubMed:21909274}. PTM: Phosphorylated by CK2 and this positively regulates its activity. {ECO:0000250}.; PTM: Sumoylation represses the transcriptional activity and displays enhanced resistance to protein degradation. Inactivates the tumor suppressor activity. Elevated levels in tumor cells. Major site is Lys-276. Sumoylation is enhanced by PIAS3. Desumoylated by SENP1 in tumor cells and appears to compete with ubiquitination on C-terminal sites (By similarity). {ECO:0000250}.; PTM: Ubiquitinated. Appears to compete with sumoylation on C-terminal sites (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17018642}. Cytoplasm {ECO:0000269|PubMed:17018642}. Note=MYD88-associated IRF1 migrates into the nucleus more efficiently than non-MYD88-associated IRF1. SUBUNIT: Monomer. Homodimer. Interacts with EP300 (By similarity). Interacts with MYD88 and PIAS3. {ECO:0000250, ECO:0000269|PubMed:12387893, ECO:0000269|PubMed:17018642}. +Q811J3 IREB2_MOUSE Iron-responsive element-binding protein 2 (IRE-BP 2) (Iron regulatory protein 2) (IRP2) 963 104,920 Chain (1); Metal binding (3); Sequence conflict (1) FUNCTION: RNA-binding protein that binds to iron-responsive elements (IRES), which are stem-loop structures found in the 5'-UTR of ferritin, and delta aminolevulinic acid synthase mRNAs, and in the 3'-UTR of transferrin receptor mRNA. Binding to the IRE element in ferritin results in the repression of its mRNA translation. Binding of the protein to the transferrin receptor mRNA inhibits the degradation of this otherwise rapidly degraded mRNA. {ECO:0000250|UniProtKB:P48200}. PTM: Ubiquitinated and degraded by the proteasome in presence of high level of iron and oxygen. Ubiquitinated by a SCF complex containing FBXL5. Upon iron and oxygen depletion FBXL5 is degraded, preventing ubiquitination and allowing its RNA-binding activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with RBCK1 only in iron-rich conditions. Interacts (when associated with the 4Fe-4S) with FBXL5 (By similarity). Interacts with CIAO1 and CIAO2A (PubMed:23891004). {ECO:0000250|UniProtKB:P48200, ECO:0000269|PubMed:23891004}. +Q9ERS6 IRPL2_MOUSE X-linked interleukin-1 receptor accessory protein-like 2 (IL-1 receptor accessory protein-like 2) (IL-1-RAPL-2) (IL-1RAPL-2) (IL1RAPL-2) (IL1RAPL-2-related protein) (Three immunoglobulin domain-containing IL-1 receptor-related 1) (TIGIRR-1) 686 78,798 Alternative sequence (2); Chain (1); Disulfide bond (3); Domain (4); Glycosylation (5); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 355 375 Helical. {ECO:0000255}. TOPO_DOM 17 354 Extracellular. {ECO:0000255}.; TOPO_DOM 376 686 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. TISSUE SPECIFICITY: Detected in fetal brain after day 12.5, in particular in parts of the diencephalon and in the basal plate of the spinal cord. In postnatal brain detected in cerebral cortex, olfactory bulb, in the CA1 region of the hippocampus and in Purkinje cells of the Xth cerebellar lobule. {ECO:0000269|PubMed:11587848}. +Q61179 IRF9_MOUSE Interferon regulatory factor 9 (IRF-9) (IFN-alpha-responsive transcription factor subunit) (ISGF3 p48 subunit) (Interferon-stimulated gene factor 3 gamma) (ISGF-3 gamma) (Transcriptional regulator ISGF3 subunit gamma) 399 44,610 Beta strand (12); Chain (1); Compositional bias (1); DNA binding (1); Helix (3); Modified residue (2) FUNCTION: Transcription factor that mediates signaling by type I IFNs (IFN-alpha and IFN-beta). Following type I IFN binding to cell surface receptors, Jak kinases (TYK2 and JAK1) are activated, leading to tyrosine phosphorylation of STAT1 and STAT2. IRF9/ISGF3G associates with the phosphorylated STAT1:STAT2 dimer to form a complex termed ISGF3 transcription factor, that enters the nucleus. ISGF3 binds to the IFN stimulated response element (ISRE) to activate the transcription of interferon stimulated genes, which drive the cell in an antiviral state. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with STAT2 in the cytoplasm. Forms the interferon-stimulated gene factor 3 complex (ISGF3) with the heterodimer STAT1:STAT2; upon stimulation. {ECO:0000269|PubMed:17332413}. +Q9Z0Y7 IRS4_MOUSE Insulin receptor substrate 4 (IRS-4) (Phosphoprotein of 160 kDa) (pp160) 1216 130,147 Chain (1); Compositional bias (9); Domain (2); Erroneous initiation (1); Modified residue (1); Motif (7); Region (2); Sequence conflict (3) FUNCTION: Acts as an interface between multiple growth factor receptors possessing tyrosine kinase activity, such as insulin receptor, IGF1R and FGFR1, and a complex network of intracellular signaling molecules containing SH2 domains. Involved in the IGF1R mitogenic signaling pathway. Promotes the AKT1 signaling pathway and BAD phosphorylation during insulin stimulation without activation of RPS6KB1 or the inhibition of apoptosis. Interaction with GRB2 enhances insulin-stimulated mitogen-activated protein kinase activity. May be involved in nonreceptor tyrosine kinase signaling in myoblasts. Plays a pivotal role in the proliferation/differentiation of hepatoblastoma cell through EPHB2 activation upon IGF1 stimulation. May play a role in the signal transduction in response to insulin and to a lesser extent in response to IL4 and GH on mitogenesis. Plays a role in growth, reproduction and glucose homeostasis. May act as negative regulators of the IGF1 signaling pathway by suppressing the function of IRS1 and IRS2. {ECO:0000269|PubMed:10403832, ECO:0000269|PubMed:10644546, ECO:0000269|PubMed:11113178, ECO:0000269|PubMed:12618213}. PTM: Phosphorylated on tyrosine residues in response to both insulin and IGF1 signaling. Phosphorylated on Tyr-894 in response to FGF2 signaling. Phosphorylation of Tyr-894 is required for GRB2, phospholipase C-gamma and phosphatidylinositol 3-kinase interaction (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. SUBUNIT: Interacts with CRK and CRKL. Interaction with CRK is stronger than with CRKL. Interacts with CRK via the phosphorylated YXXM motifs. Interacts with PLC-gamma, SHC1, PTK6, PPP4C and NISCH (By similarity). Interacts with SOCS6 in response to stimulation with either insulin or IGF1. Interacts with PIK3R1 and GRB2. {ECO:0000250, ECO:0000269|PubMed:11113178, ECO:0000269|PubMed:12052866, ECO:0000269|PubMed:12618213}. TISSUE SPECIFICITY: Expressed in skeletal muscle, brain, heart, kidney and liver. {ECO:0000269|PubMed:10067860, ECO:0000269|PubMed:10644546}. +Q9DCB8 ISCA2_MOUSE Iron-sulfur cluster assembly 2 homolog, mitochondrial (HESB-like domain-containing protein 1) 154 16,718 Chain (1); Erroneous initiation (1); Metal binding (3); Transit peptide (1) FUNCTION: Involved in the maturation of mitochondrial 4Fe-4S proteins functioning late in the iron-sulfur cluster assembly pathway. May be involved in the binding of an intermediate of Fe/S cluster assembly. {ECO:0000250|UniProtKB:Q86U28}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q86U28}. +Q9JKQ4 IRX5_MOUSE Iroquois-class homeodomain protein IRX-5 (Homeodomain protein IRXB2) (Iroquois homeobox protein 5) 484 50,755 Chain (1); Compositional bias (4); DNA binding (1); Frameshift (1); Modified residue (2) FUNCTION: Establishes the cardiac repolarization gradient by its repressive actions on the KCND2 potassium-channel gene. Required for retinal cone bipolar cell differentiation. May regulate contrast adaptation in the retina and control specific aspects of visual function in circuits of the mammalian retina. Involved in craniofacial and gonadal development (By similarity). Modulates the migration of progenitor cell populations in branchial arches and gonads by repressing CXCL12. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. TISSUE SPECIFICITY: Not expressed in the developing metanephric kidney or adult kidney. +Q9D7P6 ISCU_MOUSE Iron-sulfur cluster assembly enzyme ISCU, mitochondrial (NifU-like N-terminal domain-containing protein) (NifU-like protein) 168 18,098 Beta strand (3); Chain (1); Helix (5); Transit peptide (1); Turn (1) FUNCTION: Scaffold protein for the de novo synthesis of iron-sulfur (Fe-S) clusters within mitochondria, which is required for maturation of both mitochondrial and cytoplasmic [2Fe-2S] and [4Fe-4S] proteins. First, a [2Fe-2S] cluster is transiently assembled on the scaffold protein ISCU. In a second step, the cluster is released from ISCU, transferred to a glutaredoxin GLRX5, followed by the formation of mitochondrial [2Fe-2S] proteins, the synthesis of [4Fe-4S] clusters and their target-specific insertion into the recipient apoproteins. Cluster assembly on ISCU depends on the function of the cysteine desulfurase complex NFS1-LYRM4/ISD11, which serves as the sulfur donor for cluster synthesis, the iron-binding protein frataxin as the putative iron donor, and the electron transfer chain comprised of ferredoxin reductase and ferredoxin, which receive their electrons from NADH (By similarity). {ECO:0000250|UniProtKB:Q03020, ECO:0000250|UniProtKB:Q9H1K1}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9H1K1}. SUBUNIT: Binds NFS1. Interacts with HSCB. Interacts with GLRX5. Interacts with HSPA9. {ECO:0000250|UniProtKB:Q9H1K1}. +O35679 ISK4_MOUSE Serine protease inhibitor Kazal-type 4 (MPGC60 protein) (Peptide PEC-60 homolog) 86 9,729 Chain (1); Disulfide bond (3); Domain (1); Sequence conflict (1); Signal peptide (1); Site (1) SUBCELLULAR LOCATION: Secreted {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the intestinal tract. +Q8BT20 ISK6_MOUSE Serine protease inhibitor Kazal-type 6 105 11,609 Chain (1); Disulfide bond (3); Domain (1); Modified residue (1); Signal peptide (1); Site (1) FUNCTION: Serine protease inhibitor selective for kallikreins. Efficiently inhibits KLK5 and human KLK2, KLK4, KLK5, KLK6, KLK7, KLK12, KLK13 and KLK14. Doesn't inhibit human KLK1 and KLK8. {ECO:0000269|PubMed:24352040}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24352040}. TISSUE SPECIFICITY: Expressed in the upper epidermis and in skin appendages. {ECO:0000269|PubMed:24352040}. +Q6IE32 ISK7_MOUSE Serine protease inhibitor Kazal-type 7 (Esophagus cancer-related gene 2 protein) (ECRG-2) 85 9,282 Chain (1); Disulfide bond (3); Domain (1); Erroneous gene model prediction (1); Signal peptide (1); Site (1) FUNCTION: Probable serine protease inhibitor. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q09TK9 ISK8_MOUSE Serine protease inhibitor Kazal-type 8 105 11,778 Chain (1); Disulfide bond (3); Domain (1); Signal peptide (1); Site (1) FUNCTION: Probable serine protease inhibitor. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Expressed in epydiymis, in the cauda, corpus and caput. {ECO:0000269|PubMed:16930550}. +Q64339 ISG15_MOUSE Ubiquitin-like protein ISG15 (Interferon-induced 15 kDa protein) (Interferon-induced 17 kDa protein) (IP17) (Ubiquitin cross-reactive protein) 161 17,898 Beta strand (10); Binding site (1); Chain (1); Cross-link (1); Domain (2); Helix (6); Mass spectrometry (1); Modified residue (2); Motif (1); Propeptide (1); Region (1); Sequence conflict (2); Turn (1) FUNCTION: Ubiquitin-like protein which plays a key role in the innate immune response to viral infection either via its conjugation to a target protein (ISGylation) or via its action as a free or unconjugated protein. ISGylation involves a cascade of enzymatic reactions involving E1, E2, and E3 enzymes which catalyze the conjugation of ISG15 to a lysine residue in the target protein. Its target proteins include SERPINA3G/SPI2A, JAK1, MAPK3/ERK1, PLCG1, TRIM25, STAT5A, MAPK1/ERK2 and globin. Can also isgylate: DDX58/RIG-I which inhibits its function in antiviral signaling response and EIF4E2 which enhances its cap structure-binding activity and translation-inhibition activity. Exhibits antiviral activity towards both DNA and RNA viruses, including influenza A and B virus, sindbis virus (SV) and herpes simplex type-1 (HHV-1). Plays a significant role in the control of neonatal Chikungunya virus (CHIKV) infection by acting as a putative immunomodulator of proinflammatory cytokines. Protects mice against the consequences of Chikungunya virus infection by downregulating the pathogenic cytokine response, often denoted as the cytokine storm. Plays a role in erythroid differentiation. The secreted form of ISG15 can: induce natural killer cell proliferation, act as a chemotactic factor for neutrophils and act as a IFN-gamma-inducing cytokine playing an essential role in antimycobacterial immunity. {ECO:0000269|PubMed:16254333, ECO:0000269|PubMed:17222803, ECO:0000269|PubMed:17227866, ECO:0000269|PubMed:17289916, ECO:0000269|PubMed:18057259, ECO:0000269|PubMed:22022510, ECO:0000269|PubMed:22028657, ECO:0000269|PubMed:22859821}. PTM: S-nitrosylation decreases its dimerization, thereby increasing the availability as well as the solubility of monomeric ISG15 for its conjugation to cellular proteins. {ECO:0000269|PubMed:18606809}.; PTM: Induced as an inactive, precursor protein that is cleaved by specific proteases to expose the C-terminal diglycine (LRLRGG) motif. This motif is essential not only for its conjugation to substrates but also for its recognition by the relevant processing proteases (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Secreted {ECO:0000250}. Note=Exists in three distinct states: free within the cell, released into the extracellular space, or conjugated to target proteins. {ECO:0000250}. SUBUNIT: Homodimer; disulfide-linked. Interacts with, and is conjugated to its targets by the UBE1L (E1 enzyme) and UBE2E2 (E2 enzyme). Interacts with NEDD4 (By similarity). {ECO:0000250}. DOMAIN: Both the Ubiquitin-like 1 and Ubiquitin-like 2 domains are required for its efficient conjugation to cellular proteins. The two domains play different roles in the ISGylation pathway: Ubiquitin-like 2 domain is necessary for the first two steps allowing the linking of ISG15 to the E1 and E2 enzymes while Ubiquitin-like 1 domain is essential for the final, E3-mediated transfer of ISG15, from the E2 to the Lys of the target protein (By similarity). {ECO:0000250}. +Q9JL16 ISG20_MOUSE Interferon-stimulated gene 20 kDa protein (EC 3.1.13.1) (Promyelocytic leukemia nuclear body-associated protein ISG20) (Protein DnaQL) 300 32,503 Alternative sequence (2); Chain (1); Metal binding (4) FUNCTION: Interferon-induced antiviral exoribonuclease that acts on single-stranded RNA and also has minor activity towards single-stranded DNA. Exhibits antiviral activity against RNA viruses in an exonuclease-dependent manner. May also play additional roles in the maturation of snRNAs and rRNAs, and in ribosome biogenesis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Cytoplasm {ECO:0000250}. Nucleus, Cajal body {ECO:0000250}. SUBUNIT: Associates with PML and SP100 in the PML NB complex. Associates with survival motor neuron protein (SMN)-containing macromolecular nuclear complexes and U1 and U2 snRNAs and U3 snoRNA (By similarity). {ECO:0000250}. +Q9CXV0 ISL2_MOUSE Insulin gene enhancer protein ISL-2 (Islet-2) 359 39,728 Beta strand (2); Chain (1); DNA binding (1); Domain (2); Helix (1); Modified residue (3); Region (1); Sequence conflict (4) FUNCTION: Transcriptional factor that defines subclasses of motoneurons that segregate into columns in the spinal cord and select distinct axon pathways. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. SUBUNIT: Interacts with LHX4. {ECO:0000269|PubMed:22025611}. +Q6GU68 ISLR_MOUSE Immunoglobulin superfamily containing leucine-rich repeat protein 428 45,615 Chain (1); Disulfide bond (1); Domain (3); Glycosylation (2); Repeat (5); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Detected in thyroid, heart, retina and spinal cord. {ECO:0000269|PubMed:10512678}. +Q8BMY7 ISK2_MOUSE Serine protease inhibitor Kazal-type 2 86 9,722 Chain (1); Disulfide bond (3); Domain (1); Signal peptide (1); Site (1) FUNCTION: As a strong inhibitor of acrosin, it is required for normal spermiogenesis. It probably hinders premature activation of proacrosin and other proteases, thus preventing the cascade of events leading to spermiogenesis defects (PubMed:21705336, PubMed:28554943). May be involved in the regulation of serine protease-dependent germ cell apoptosis (PubMed:21705336). It also inhibits trypsin (PubMed:21705336). {ECO:0000269|PubMed:21705336, ECO:0000269|PubMed:28554943}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P20155}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:28554943}. TISSUE SPECIFICITY: Expressed in sperm (at protein level). Expressed in testis but not in ovary, brain, heart, kidney or lung. Within testis, expressed in epididymis and germ cells. {ECO:0000269|PubMed:21705336, ECO:0000269|Ref.3}. +P01793 HVM24_MOUSE Ig heavy chain V region HPCG13 123 13,808 Chain (1); Domain (1); Non-terminal residue (1) +P01796 HVM27_MOUSE Ig heavy chain V-III region A4 113 12,675 Chain (1); Disulfide bond (1); Domain (1); Non-terminal residue (1) +P23463 HXD8_MOUSE Homeobox protein Hox-D8 (Homeobox protein Hox-4.3) (Homeobox protein Hox-5.4) 289 31,363 Chain (1); Compositional bias (3); DNA binding (1); Motif (1) FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. SUBCELLULAR LOCATION: Nucleus. +P01820 HVM44_MOUSE Ig heavy chain V region PJ14 115 12,447 Beta strand (10); Chain (1); Domain (1); Helix (3); Non-terminal residue (1); Signal peptide (1); Turn (2) +P01823 HVM47_MOUSE Ig heavy chain V region 36-60 113 12,734 Beta strand (10); Chain (1); Helix (3); Non-terminal residue (1); Turn (2) +P03980 HVM48_MOUSE Ig heavy chain V region TEPC 1017 138 15,576 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (7); Signal peptide (1) +O08650 HYAS3_MOUSE Hyaluronan synthase 3 (EC 2.4.1.212) (Hyaluronate synthase 3) (Hyaluronic acid synthase 3) (HA synthase 3) 554 63,349 Chain (1); Glycosylation (1); Sequence conflict (1); Topological domain (8); Transmembrane (7) TRANSMEM 16 36 Helical; Name=1. {ECO:0000255}.; TRANSMEM 45 65 Helical; Name=2. {ECO:0000255}.; TRANSMEM 379 399 Helical; Name=3. {ECO:0000255}.; TRANSMEM 410 430 Helical; Name=4. {ECO:0000255}.; TRANSMEM 442 462 Helical; Name=5. {ECO:0000255}.; TRANSMEM 475 495 Helical; Name=6. {ECO:0000255}.; TRANSMEM 517 537 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 15 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 37 44 Extracellular. {ECO:0000255}.; TOPO_DOM 66 378 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 400 409 Extracellular. {ECO:0000255}.; TOPO_DOM 431 441 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 463 474 Extracellular. {ECO:0000255}.; TOPO_DOM 496 516 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 538 554 Extracellular. {ECO:0000255}. Glycan biosynthesis; hyaluronan biosynthesis. FUNCTION: Catalyzes the addition of GlcNAc or GlcUA monosaccharides to the nascent hyaluronan polymer. Therefore, it is essential to hyaluronan synthesis a major component of most extracellular matrices that has a structural role in tissues architectures and regulates cell adhesion, migration and differentiation. This is one of the isozymes catalyzing that reaction. {ECO:0000269|PubMed:10455188}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8BGY3 LUZP2_MOUSE Leucine zipper protein 2 345 39,020 Chain (1); Coiled coil (1); Glycosylation (2); Region (1); Sequence conflict (3); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Expression found only in the brain and spinal cord. {ECO:0000269|PubMed:12856284}. +P70217 HXD13_MOUSE Homeobox protein Hox-D13 (Homeobox protein Hox-4.8) 339 35,889 Chain (1); Compositional bias (4); DNA binding (1); Mutagenesis (2); Sequence conflict (4) FUNCTION: Sequence-specific transcription factor that binds gene promoters and activates their transcription (PubMed:23995701). Part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis (By similarity). {ECO:0000250|UniProtKB:P24344, ECO:0000269|PubMed:23995701}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:15489334}. +P01723 LV1A_MOUSE Ig lambda-1 chain V region 117 12,222 Beta strand (8); Chain (1); Domain (1); Helix (2); Modified residue (1); Non-terminal residue (1); Signal peptide (1); Turn (2) +P31313 HXC11_MOUSE Homeobox protein Hox-C11 (Homeobox protein Hox-3.7) 304 33,708 Chain (1); Cross-link (3); DNA binding (1) FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. SUBCELLULAR LOCATION: Nucleus. +Q08624 HXC4_MOUSE Homeobox protein Hox-C4 (Homeobox protein Hox-3.5) 264 29,865 Chain (1); Compositional bias (2); DNA binding (1); Motif (1); Sequence conflict (2) FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. SUBCELLULAR LOCATION: Nucleus. +P28776 I23O1_MOUSE Indoleamine 2,3-dioxygenase 1 (IDO-1) (EC 1.13.11.52) (Indoleamine-pyrrole 2,3-dioxygenase) 407 45,641 Chain (1); Metal binding (1) FUNCTION: Catalyzes the first and rate limiting step of the catabolism of the essential amino acid tryptophan along the kynurenine pathway. Involved in the peripheral immune tolerance, contributing to maintain homeostasis by preventing autoimmunity or immunopathology that would result from uncontrolled and overreacting immune responses. Tryptophan shortage inhibits T lymphocytes division and accumulation of tryptophan catabolites induces T-cell apoptosis and differentiation of regulatory T-cells. Acts as a suppressor of anti-tumor immunity (PubMed:25691885). Limits the growth of intracellular pathogens by depriving tryptophan. Protects the fetus from maternal immune rejection (Ref. 3). {ECO:0000250|UniProtKB:P14902, ECO:0000269|PubMed:15063630, ECO:0000303|PubMed:25691885}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:19741271}. SUBUNIT: Monomer. {ECO:0000303|PubMed:25691885}. TISSUE SPECIFICITY: Highly expressed in epididymis, duodemum, jejunum, ileum, colon and spleen (PubMed:19741271). Highly expressed in epididymis, prostate, duodemum, jejunum, ileum, colon and spleen, not detected in the liver (at protein level) (PubMed:19741271). Expressed in tumors only upon exposure to IFN gamma (PubMed:25691885). Constitutively expressed in placenta in trophoblast cells (PubMed:15063630). Expression is restricted to perinuclear regions of primary trophoblast giant cells (TGCs) of fetal origin at mid-gestation (E10.5). After placentation (E14), no IDO expression was detected at the maternal-fetal interface (PubMed:15063630). {ECO:0000269|PubMed:15063630, ECO:0000269|PubMed:19741271, ECO:0000303|PubMed:25691885}. +P09025 HXC8_MOUSE Homeobox protein Hox-C8 (Homeobox protein Hox-3.1) (Homeobox protein M31) 242 27,740 Chain (1); DNA binding (1); Motif (1); Sequence conflict (2) FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with HOMEZ. {ECO:0000250}. +O88786 I13R2_MOUSE Interleukin-13 receptor subunit alpha-2 (IL-13 receptor subunit alpha-2) (IL-13R subunit alpha-2) (IL-13R-alpha-2) (IL-13RA2) (CD antigen CD213a2) 383 44,483 Alternative sequence (2); Chain (1); Disulfide bond (4); Domain (3); Glycosylation (4); Motif (1); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 335 355 Helical. {ECO:0000255}. TOPO_DOM 22 334 Extracellular. {ECO:0000255}.; TOPO_DOM 356 383 Cytoplasmic. {ECO:0000255}. FUNCTION: Binds as a monomer with high affinity to interleukin-13 (IL13). {ECO:0000269|PubMed:9725226}. SUBCELLULAR LOCATION: Isoform 1: Membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Isoform 2: Secreted. DOMAIN: The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding. {ECO:0000250}. +Q8K337 I5P2_MOUSE Type II inositol 1,4,5-trisphosphate 5-phosphatase (EC 3.1.3.36) (Inositol polyphosphate-5-phosphatase B) (Phosphoinositide 5-phosphatase) (5PTase) 993 112,762 Alternative sequence (4); Beta strand (8); Binding site (1); Chain (1); Domain (2); Erroneous initiation (1); Helix (4); Lipidation (1); Metal binding (2); Modified residue (1); Propeptide (1); Region (5); Sequence conflict (1); Turn (1) FUNCTION: Hydrolyzes phosphatidylinositol 4,5-bisphosphate (PtIns(4,5)P2) and the signaling molecule phosphatidylinositol 1,4,5-trisphosphate (PtIns(1,4,5)P3), and thereby modulates cellular signaling events. {ECO:0000269|PubMed:11311145, ECO:0000269|PubMed:9525932}. PTM: Isoprenylation at Cys-990 may be required for localization at the membrane. {ECO:0000250}.; PTM: May be proteolytically cleaved after Lys-320 as inferred from N-terminal protein sequence of the 75 kda form. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:9525932}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250|UniProtKB:P32019}. Early endosome membrane {ECO:0000250|UniProtKB:P32019}. Membrane {ECO:0000250|UniProtKB:P32019}; Peripheral membrane protein {ECO:0000250|UniProtKB:P32019}; Cytoplasmic side {ECO:0000250|UniProtKB:P32019}. Cytoplasmic vesicle, phagosome membrane {ECO:0000269|PubMed:9525932}. SUBUNIT: Interacts with APPL1, PHETA1 and PHETA2. Interacts with several Rab GTPases, at least RAB1A, RAB2A, RAB5A, RAB6A, RAB8A, RAB9A and RAB33B; these interactions may play a dual role in targeting INPP5B to the specific membranes and stimulating the phosphatase activity (By similarity). Interacts with INPP5F (PubMed:25869668). {ECO:0000250|UniProtKB:P32019, ECO:0000269|PubMed:25869668}. DOMAIN: The ASH (ASPM-SPD2-Hydin) and RhoGAP (Rho GTPase activating) domains form a single folding module. The ASH domain has an immunoglobulin-like fold, the Rho-GAP domain lacks the catalytic arginine and is catalytically inactive. The ASH-RhoGAP module regulates the majority of the protein-protein interactions currently described. The ASH domain mediates association with membrane-targeting Rab GTPases. The Rho-GAP domain interacts with the endocytic adapter APPL1, which is then displaced by PHETA1 and PHETA2 as endosomes mature, all three interactions rely on F&H motifs, an approximately 12-13 amino-acid sequence centered around Phe and His residues essential for binding (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Detected in kidney, liver, brain, lung and testis (at protein level). Detected in kidney and liver, and at lower levels in brain, lung and testis. {ECO:0000269|PubMed:9525932}. +Q60960 IMA5_MOUSE Importin subunit alpha-5 (Importin alpha-S1) (Karyopherin subunit alpha-1) (Nucleoprotein interactor 1) (NPI-1) (RAG cohort protein 2) (SRP1-beta) 538 60,183 Chain (1); Compositional bias (1); Domain (1); Modified residue (3); Motif (1); Region (3); Repeat (10); Sequence conflict (1) FUNCTION: Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. PTM: Polyubiquitinated in the presence of RAG1 (in vitro). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. SUBUNIT: Heterodimer; with KPNB1 (By similarity). Interacts with NSMF; the interaction occurs in a calcium-independent manner after synaptic NMDA receptor stimulation and is required for nuclear import of NSMF but is competed by CABP1 (By similarity). Interacts with APEX1 (via its N-terminus) (By similarity). Interacts with CTNNBL1 (via its N-terminal) (By similarity). Interacts with AICDA (via its NLS) (By similarity). Interacts with ANP32E (PubMed:10692581). Interacts with ZIC3 (PubMed:18716025). Interacts with SNAI1 (via zinc fingers) (By similarity). Interacts with DCAF8 (By similarity). Interacts with ITSN1 isoform 2 (PubMed:29599122). {ECO:0000250|UniProtKB:P52294, ECO:0000250|UniProtKB:P83953, ECO:0000269|PubMed:10692581, ECO:0000269|PubMed:18716025, ECO:0000269|PubMed:29599122}. DOMAIN: Consists of an N-terminal hydrophilic region, a hydrophobic central region composed of 10 repeats, and a short hydrophilic C-terminus. The N-terminal hydrophilic region contains the importin beta binding domain (IBB domain), which is sufficient for binding importin beta and essential for nuclear protein import.; DOMAIN: The IBB domain is thought to act as an intrasteric autoregulatory sequence by interacting with the internal autoinhibitory NLS. Binding of KPNB1 probably overlaps the internal NLS and contributes to a high affinity for cytoplasmic NLS-containing cargo substrates. After dissociation of the importin/substrate complex in the nucleus the internal autohibitory NLS contributes to a low affinity for nuclear NLS-containing proteins (By similarity). {ECO:0000250}.; DOMAIN: The major and minor NLS binding sites are mainly involved in recognition of simple or bipartite NLS motifs. Structurally located within in a helical surface groove they contain several conserved Trp and Asn residues of the corresponding third helices (H3) of ARM repeats which mainly contribute to binding (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Low levels in all tissues examined. +Q91UZ5 IMPA2_MOUSE Inositol monophosphatase 2 (IMP 2) (IMPase 2) (EC 3.1.3.25) (Inositol-1(or 4)-monophosphatase 2) (Myo-inositol monophosphatase A2) 290 31,716 Binding site (3); Chain (1); Metal binding (6); Region (2) Polyol metabolism; myo-inositol biosynthesis; myo-inositol from D-glucose 6-phosphate: step 2/2. FUNCTION: Can use myo-inositol monophosphates, scylloinositol 1,4-diphosphate, glucose-1-phosphate, beta-glycerophosphate, and 2'-AMP as substrates. Has been implicated as the pharmacological target for lithium Li(+) action in brain (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Mostly expressed in brain, small intestine, heart, kidney, and spleen (at protein level). {ECO:0000269|PubMed:17068342}. +Q9D8Y8 ING5_MOUSE Inhibitor of growth protein 5 240 27,799 Alternative sequence (2); Binding site (4); Chain (1); Metal binding (8); Modified residue (2); Zinc finger (1) FUNCTION: Component of the HBO1 complex which has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3 and is responsible for the bulk of histone H4 acetylation in vivo. Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. May function as a transcriptional coactivator for RUNX2. Inhibits cell growth, induces a delay in S-phase progression and enhances Fas-induced apoptosis in an INCA1-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q8WYH8}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8WYH8}. SUBUNIT: Interacts with H3K4me3 and to a lesser extent with H3K4me2 (By similarity). Component of the HBO1 complex composed at least of ING4 or ING5, MYST2/HBO1, MEAF6, and one of JADE1, JADE2 and JADE3. Component of the MOZ/MORF complex composed at least of ING5, KAT6A, KAT6B, MEAF6 and one of BRPF1, BRD1/BRPF2 and BRPF3. Interacts with INCA1 (By similarity). {ECO:0000250|UniProtKB:Q8WYH8}. DOMAIN: The PHD-type zinc finger mediates the binding to H3K4me3. {ECO:0000250|UniProtKB:Q8WYH8}. +Q9JHU9 INO1_MOUSE Inositol-3-phosphate synthase 1 (IPS 1) (EC 5.5.1.4) (Myo-inositol 1-phosphate synthase) (MI-1-P synthase) (MIP synthase) 557 60,932 Chain (1) Polyol metabolism; myo-inositol biosynthesis; myo-inositol from D-glucose 6-phosphate: step 1/2. FUNCTION: Key enzyme in myo-inositol biosynthesis pathway that catalyzes the conversion of glucose 6-phosphate to 1-myo-inositol 1-phosphate in a NAD-dependent manner. Rate-limiting enzyme in the synthesis of all inositol-containing compounds (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. TISSUE SPECIFICITY: In testis, it is expressed in Sertoli cells. Highly expressed in 2 types of germ cells, pachytene spermatocytes and round spermatids. {ECO:0000269|PubMed:14613899}. +Q9EPW0 INP4A_MOUSE Type I inositol 3,4-bisphosphate 4-phosphatase (EC 3.1.3.66) (Inositol polyphosphate 4-phosphatase type I) 939 105,540 Alternative sequence (4); Chain (1); Domain (1); Modified residue (2); Sequence conflict (8) Signal transduction; phosphatidylinositol signaling pathway. FUNCTION: Catalyzes the hydrolysis of the 4-position phosphate of phosphatidylinositol 3,4-bisphosphate, inositol 1,3,4-trisphosphate and inositol 1,4-bisphosphate. Involved in the regulation of megakaryocyte and fibroblast proliferation. Regulates cell growth downstream of transcription factor GATA-1. {ECO:0000269|PubMed:11087841}. SUBUNIT: Interacts with INPP5F. {ECO:0000269|PubMed:25869668}. TISSUE SPECIFICITY: Spleen, skeletal muscle, lung and uterus. {ECO:0000269|PubMed:11485317}. +Q6P1Y8 INP4B_MOUSE Type II inositol 3,4-bisphosphate 4-phosphatase (EC 3.1.3.66) (Inositol polyphosphate 4-phosphatase type II) 924 104,531 Chain (1); Domain (1) Signal transduction; phosphatidylinositol signaling pathway. FUNCTION: Catalyzes the hydrolysis of the 4-position phosphate of phosphatidylinositol 3,4-bisphosphate, inositol 1,3,4-trisphosphate and inositol 1,4-bisphosphate (By similarity). Plays a role in the late stages of macropinocytosis by dephosphorylating phosphatidylinositol 3,4-bisphosphate in membrane ruffles (By similarity). {ECO:0000250|UniProtKB:O15327, ECO:0000250|UniProtKB:Q9QWG5}. +O09107 INSL3_MOUSE Insulin-like 3 (Leydig insulin-like peptide) (Ley-I-L) (Relaxin-like factor) [Cleaved into: Insulin-like 3 B chain; Insulin-like 3 A chain] 122 13,586 Disulfide bond (3); Peptide (2); Propeptide (1); Sequence conflict (4); Signal peptide (1) FUNCTION: Seems to play a role in testicular function. May be a trophic hormone with a role in testicular descent in fetal life. Is a ligand for LGR8 receptor (By similarity). {ECO:0000250, ECO:0000269|PubMed:10391220, ECO:0000269|PubMed:11342953}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Heterodimer of a B chain and an A chain linked by two disulfide bonds. {ECO:0000250}. TISSUE SPECIFICITY: Expressed exclusively in Leydig cells of the testis. +Q8VII8 MCR_MOUSE Mineralocorticoid receptor (MR) (Nuclear receptor subfamily 3 group C member 2) 978 106,447 Binding site (4); Chain (1); DNA binding (1); Domain (1); Modified residue (5); Region (3); Sequence conflict (2); Zinc finger (2) FUNCTION: Receptor for both mineralocorticoids (MC) such as aldosterone and glucocorticoids (GC) such as corticosterone or cortisol. Binds to mineralocorticoid response elements (MRE) and transactivates target genes. The effect of MC is to increase ion and water transport and thus raise extracellular fluid volume and blood pressure and lower potassium levels. {ECO:0000269|PubMed:19029984}. PTM: Phosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407, ECO:0000269|PubMed:19029984}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Cytoplasmic and nuclear in the absence of ligand; nuclear after ligand-binding. When bound to HSD11B2, it is found associated with the endoplasmic reticulum membrane (By similarity). {ECO:0000250}. SUBUNIT: Heteromultimeric cytoplasmic complex with HSP90, HSP70, and FKBP4, in the absence of ligand. After ligand binding, it translocates to the nucleus and binds to DNA as a homodimer and as a heterodimer with NR3C1. Binds the coactivator NCOA2. May interact with HSD11B2 in the absence of ligand. Binds the coactivators NCOA1, TIF1 and NRIP1 (By similarity). {ECO:0000250}. DOMAIN: Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain. TISSUE SPECIFICITY: Expressed in heart and kidney. {ECO:0000269|PubMed:19029984}. +Q9D4I2 MEII1_MOUSE Meiosis inhibitor protein 1 (Meiosis defective protein 1) 1268 140,874 Alternative sequence (1); Chain (1); Sequence conflict (5) FUNCTION: Required for normal meiotic chromosome synapsis. May be involved in the formation of meiotic double-strand breaks (DSBs) in spermatocytes. {ECO:0000269|PubMed:14668445, ECO:0000269|PubMed:15928951}. TISSUE SPECIFICITY: Strongly expressed in testis, weakly in brain, and not detected in spleen, liver, kidney, small intestine or colon. {ECO:0000269|PubMed:14668445}. +Q9R000 ITBP2_MOUSE Integrin beta-1-binding protein 2 (Melusin) 350 38,768 Chain (1); Compositional bias (3); Domain (3); Metal binding (16); Motif (5); Sequence conflict (3) FUNCTION: May play a role during maturation and/or organization of muscles cells. SUBUNIT: Interacts with beta-1 integrin subunit. This interaction is regulated by divalent cations, and it occurs only in absence of calcium. DOMAIN: The tail domain binds to the cytoplasmic domain of both integrin beta-1a and beta-1d isoforms. The presence of Ca(2+) ions does not prevent binding of a fragment consisting of the second cysteine rich repeat and the tail domain but prevents the binding of the full-length protein. TISSUE SPECIFICITY: Expressed in skeletal and cardiac muscles but not in other tissues. Is localized in rows flanking the Z line containing alpha-actinin. +Q60976 JERKY_MOUSE Jerky protein 557 62,478 Chain (1); DNA binding (2); Domain (3) FUNCTION: May bind DNA. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00320, ECO:0000255|PROSITE-ProRule:PRU00583}. TISSUE SPECIFICITY: Brain; highest in the temporal and brainstem regions. +Q6ZQF7 JADE2_MOUSE E3 ubiquitin-protein ligase Jade-2 (EC 2.3.2.27) (Jade family PHD finger protein 2) (PHD finger protein 15) 829 92,174 Alternative sequence (2); Chain (1); Erroneous initiation (1); Modified residue (6); Zinc finger (3) Protein modification; protein ubiquitination. FUNCTION: Component of the HBO1 complex which has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3 and is responsible for the bulk of histone H4 acetylation in vivo (By similarity). Acts as a E3 ubiquitin-protein ligase mediating the ubiquitination and subsequent proteasomal degradation of target protein histone demethylase KDM1A. Also acts as a ubiquitin ligase E3 toward itself. Positive regulator of neurogenesis (PubMed:25018020). {ECO:0000250|UniProtKB:Q9NQC1, ECO:0000269|PubMed:25018020}. SUBUNIT: Component of the HBO1 complex composed at least of ING4 or ING5, MYST2/HBO1, MEAF6, and one of JADE1, JADE2 and JADE3 (By similarity). Interacts (via C-terminus) with KDM1A (via AOD/Tower domain) (PubMed:25018020). {ECO:0000250|UniProtKB:Q9NQC1, ECO:0000269|PubMed:25018020}. DOMAIN: The first PHD domain is essential for its E3 ubiquitin ligase activity. {ECO:0000250|UniProtKB:Q9NQC1}. +Q5DTN8 JKIP3_MOUSE Janus kinase and microtubule-interacting protein 3 (Neuroendocrine long coiled-coil protein 2) 844 98,715 Alternative sequence (4); Chain (1); Coiled coil (4); Erroneous initiation (1); Modified residue (1); Sequence conflict (1) SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:17572408}. +Q5XKN4 JAGN1_MOUSE Protein jagunal homolog 1 183 21,102 Chain (1); Frameshift (1); Modified residue (1); Sequence conflict (4); Topological domain (5); Transmembrane (4) TRANSMEM 40 60 Helical. {ECO:0000255}.; TRANSMEM 72 92 Helical. {ECO:0000255}.; TRANSMEM 97 117 Helical. {ECO:0000255}.; TRANSMEM 138 158 Helical. {ECO:0000255}. TOPO_DOM 1 39 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 61 71 Lumenal. {ECO:0000255}.; TOPO_DOM 93 96 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 118 137 Lumenal. {ECO:0000255}.; TOPO_DOM 159 183 Cytoplasmic. {ECO:0000255}. FUNCTION: Endoplasmic reticulum transmembrane protein involved in vesicle-mediated transport, which is required for neutrophil function. Required for vesicle-mediated transport; it is however unclear whether it is involved in early secretory pathway or intracellular protein transport. Acts as a regulator of neutrophil function, probably via its role in vesicle-mediated transport: required for defense against fungal pathogens and for granulocyte colony-stimulating factor (GM-CSF) signaling pathway; possibly by regulating glycosylation and/or targeting of proteins contributing to the viability and migration of neutrophils. {ECO:0000269|PubMed:25129145, ECO:0000305}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8N5M9}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Interacts with COPA, COPB2 and COPG2. {ECO:0000250|UniProtKB:Q8N5M9}. +Q9QXM1 JMY_MOUSE Junction-mediating and -regulatory protein 983 110,586 Alternative sequence (3); Chain (1); Coiled coil (3); Compositional bias (1); Domain (1); Modified residue (5); Mutagenesis (1); Region (2); Sequence caution (1); Sequence conflict (14) FUNCTION: Acts both as a nuclear p53/TP53-cofactor and a cytoplasmic regulator of actin dynamics depending on conditions. In nucleus, acts as a cofactor that increases p53/TP53 response via its interaction with p300/EP300. Increases p53/TP53-dependent transcription and apoptosis, suggesting an important role in p53/TP53 stress response such as DNA damage. In cytoplasm, acts as a nucleation-promoting factor for both branched and unbranched actin filaments. Activates the Arp2/3 complex to induce branched actin filament networks. Also catalyzes actin polymerization in the absence of Arp2/3, creating unbranched filaments. Contributes to cell motility by controlling actin dynamics. May promote the rapid formation of a branched actin network by first nucleating new mother filaments and then activating Arp2/3 to branch off these filaments. The p53/TP53-cofactor and actin activator activities are regulated via its subcellular location. {ECO:0000269|PubMed:10518217, ECO:0000269|PubMed:11511361, ECO:0000269|PubMed:19287377, ECO:0000269|PubMed:19897726}. PTM: Ubiquitinated by MDM2, leading to its subsequent degradation by the proteasome. In case of DNA damage, the interaction with MDM2 is altered, preventing degradation and allowing interaction with p300/EP300 and its function in p53/TP53 stress response. {ECO:0000269|PubMed:17170761}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19287377, ECO:0000269|PubMed:19897726}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Localizes to the nucleus in most cell types. In primary neutrophils, it colocalizes with actin filaments at the leading edge and is excluded from the nucleus. Localization correlates with motility, because it moves from the nucleus to the cytoplasmic compartment when cells are differentiated from nonmotile cells into highly motile neutrophil-like cells (By similarity). Accumulates in nucleus under DNA damage conditions, increasing p53/TP53 transcription response and reducing its influence on cell motility. {ECO:0000250}. SUBUNIT: Interacts with p300/EP300, the complex being recruited to activated p53/TP53. Interacts with TTC5. {ECO:0000269|PubMed:10518217, ECO:0000269|PubMed:11511361}. TISSUE SPECIFICITY: Widely expressed, except in testis where it is expressed at low level. {ECO:0000269|PubMed:10518217}. +Q5DTX6 JCAD_MOUSE Junctional protein associated with coronary artery disease (JCAD) 1320 144,798 Chain (1); Compositional bias (2); Modified residue (7) SUBCELLULAR LOCATION: Cell junction, adherens junction {ECO:0000269|PubMed:21884682}. Note=Colocalizes with VE-Cadherin, in endothelial cells but not in epithelial cells. +Q9DBJ6 JOS1_MOUSE Josephin-1 (EC 3.4.19.12) (Josephin domain-containing protein 1) 202 23,152 Active site (2); Chain (1); Domain (1); Modified residue (1) FUNCTION: Deubiquitinates monoubiquitinated probes (in vitro). When ubiquitinated, cleaves 'Lys-63'-linked and 'Lys-48'-linked poly-ubiquitin chains (in vitro), hence may act as a deubiquitinating enzyme. May increase macropinocytosis and suppress clathrin- and caveolae-mediated endocytosis. May enhance membrane dynamics and cell motility independently of its catalytic activity (By similarity). {ECO:0000250}. PTM: Monoubiquitinated. Ubiquitination activates deubiquitination activity in vitro. {ECO:0000269|PubMed:23625928}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Ubiquitination increases localization the plasma membrane. In the cytosol, the unubiquitinated form may be associated with the cytoskeleton via ACTB-binding. {ECO:0000250}. SUBUNIT: Interacts with beta-actin/ACTB. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed (at protein level). {ECO:0000269|PubMed:23625928}. +Q9WVI9 JIP1_MOUSE C-Jun-amino-terminal kinase-interacting protein 1 (JIP-1) (JNK-interacting protein 1) (Islet-brain-1) (IB-1) (JNK MAP kinase scaffold protein 1) (Mitogen-activated protein kinase 8-interacting protein 1) 707 77,282 Alternative sequence (4); Chain (1); Compositional bias (3); Domain (2); Modified residue (29); Motif (2); Natural variant (1); Region (4); Sequence conflict (6) FUNCTION: The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. Required for JNK activation in response to excitotoxic stress. Cytoplasmic MAPK8IP1 causes inhibition of JNK-regulated activity by retaining JNK in the cytoplasm and thus inhibiting the JNK phosphorylation of c-Jun. May also participate in ApoER2-specific reelin signaling. Directly, or indirectly, regulates GLUT2 gene expression and beta-cell function. Appears to have a role in cell signaling in mature and developing nerve terminals. May function as a regulator of vesicle transport, through interactions with the JNK-signaling components and motor proteins. Functions as an anti-apoptotic protein and whose level seems to influence the beta-cell death or survival response (By similarity). Acts as a scaffold protein that coordinates with SH3RF1 in organizing different components of the JNK pathway, including RAC1 or RAC2, MAP3K11/MLK3 or MAP3K7/TAK1, MAP2K7/MKK7, MAPK8/JNK1 and/or MAPK9/JNK2 into a functional multiprotein complex to ensure the effective activation of the JNK signaling pathway. Regulates the activation of MAPK8/JNK1 and differentiation of CD8(+) T-cells (PubMed:23963642). {ECO:0000250, ECO:0000269|PubMed:11562351, ECO:0000269|PubMed:23963642}. PTM: Phosphorylated by MAPK8, MAPK9 and MAPK10. Phosphorylation on Thr-103 is also necessary for the dissociation and activation of MAP3K12. Phosphorylated by VRK2. Hyperphosphorylated during mitosis following activation of stress-activated and MAP kinases (By similarity). {ECO:0000250}.; PTM: Ubiquitinated. Two preliminary events are required to prime for ubiquitination; phosphorylation and an increased in intracellular calcium concentration. Then, the calcium influx initiates ubiquitination and degradation by the ubiquitin-proteasome pathway. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}. Mitochondrion membrane {ECO:0000250}. Note=Accumulates in cell surface projections. Under certain stress conditions, translocates to the perinuclear region of neurons. In insulin-secreting cells, detected in both the cytoplasm and nucleus (By similarity). {ECO:0000250}. SUBUNIT: Forms homo- or heterooligomeric complexes. Binds specific components of the JNK signaling pathway namely MAPK8/JNK1, MAPK9/JNK2, MAPK10/JNK3, MAP2K7/MKK7, MAP3K11/MLK3 and DLK1. Also binds the proline-rich domain-containing splice variant of apolipoprotein E receptor 2 (ApoER2) (By similarity). Binds the cytoplasmic tails of LRP1 and LRP2 (Megalin). Binds the TPR motif-containing C-terminal of kinesin light chain, KLC1. Pre-assembled MAPK8IP1 scaffolding complexes are then transported as a cargo of kinesin, to the required subcellular location. Interacts with the cytoplasmic domain of APP (By similarity). Interacts, via the PID domain, with ARHGEF28. Interacts with MAP3K7/TAK1 and VRK2 (By similarity). Interacts with DCLK2 (PubMed:16628014). Found in a complex with SH3RF1, RAC1, MAP3K11/MLK3, MAP2K7/MKK7 and MAPK8/JNK1 (PubMed:23963642). Found in a complex with SH3RF1, RAC2, MAP3K7/TAK1, MAP2K7/MKK7, MAPK8/JNK1 and MAPK9/JNK2 (PubMed:27084103). Interacts with SH3RF2 (By similarity). {ECO:0000250|UniProtKB:Q9R237, ECO:0000250|UniProtKB:Q9UQF2, ECO:0000269|PubMed:10574993, ECO:0000269|PubMed:10827173, ECO:0000269|PubMed:11238452, ECO:0000269|PubMed:16628014, ECO:0000269|PubMed:23963642, ECO:0000269|PubMed:27084103}. DOMAIN: The SH3 domain mediates homodimerization. {ECO:0000250}. TISSUE SPECIFICITY: Expressed predominantly in the brain and insulin-secreting cells. In the brain, high expression found in the cerebral cortex and hippocampus. Localizes in the synaptic regions of the olfactory bulb, retina, cerebral and cerebellar cortex and hippocampus. Also expressed in a restricted number of axons, including mossy fibers from the hippocampal dentate gyrus, soma, dendrites and axons of cerebellar Purkinje cells. Also expressed in kidney, testis and prostate. Low levels in heart, ovary and small intestine. Isoform JIP-1b is more predominant in the brain than isoform JIP-1a. Isoform Jip1-a is expressed both in the brain and kidney, isoform JIP-1c, isoform JIP-1d and isoform JIP-1e are brain specific. {ECO:0000269|PubMed:10712642}. +Q9ET78 JPH2_MOUSE Junctophilin-2 (JP-2) (Junctophilin type 2) 696 74,692 Chain (1); Compositional bias (2); Modified residue (13); Repeat (8); Topological domain (1); Transmembrane (1) TRANSMEM 675 695 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 1 674 Cytoplasmic. {ECO:0000255}. FUNCTION: Junctophilins contribute to the formation of junctional membrane complexes (JMCs) which link the plasma membrane with the endoplasmic or sarcoplasmic reticulum in excitable cells. Provides a structural foundation for functional cross-talk between the cell surface and intracellular calcium release channels. JPH2 is necessary for proper intracellular Ca(2+) signaling in cardiac myocytes via its involvement in ryanodine receptor-mediated calcium ion release. Contributes to the construction of skeletal muscle triad junctions. {ECO:0000269|PubMed:10949023, ECO:0000269|PubMed:19095005, ECO:0000269|PubMed:21339484}. PTM: Phosphorylation on Ser-165, probably by PKC, affects RYR1-mediated calcium ion release, interaction with TRPC3, and skeletal muscle myotubule development. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10949023}; Peripheral membrane protein {ECO:0000269|PubMed:10949023}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:10949023}; Single-pass type IV membrane protein {ECO:0000269|PubMed:10949023}. Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:10949023}; Single-pass type IV membrane protein {ECO:0000269|PubMed:10949023}. Note=Localized predominantly on the plasma membrane. The transmembrane domain is anchored in endoplasmic/sarcoplasmic reticulum membrane, while the N-terminal part associates with the plasma membrane. In heart cells, it predominantly associates along Z lines within myocytes. In skeletal muscle, it is specifically localized at the junction of A and I bands. SUBUNIT: Interacts with TRPC3. {ECO:0000250|UniProtKB:Q9BR39}. DOMAIN: The MORN (membrane occupation and recognition nexus) repeats contribute to the plasma membrane binding, by interacting with phospholipids. Has affinity for phosphatidylserine, and phosphorylated phosphatidylinositols including PtdIns3P, PtdIns4P, PtdIns5P, PtdIns(3,5)P2 and PtdIns(3,4,5)P3 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Abundantly expressed in skeletal muscle and heart. Weak expression in stomach and lung. {ECO:0000269|PubMed:10949023}. +Q3V0T4 ITAD_MOUSE Integrin alpha-D (CD antigen CD11d) 1168 127,829 Calcium binding (3); Chain (1); Disulfide bond (7); Domain (1); Glycosylation (10); Motif (1); Repeat (7); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1108 1128 Helical. {ECO:0000255}. TOPO_DOM 27 1107 Extracellular. {ECO:0000255}.; TOPO_DOM 1129 1168 Cytoplasmic. {ECO:0000255}. FUNCTION: Integrin alpha-D/beta-2 is a receptor for ICAM3 and VCAM1. May play a role in the atherosclerotic process such as clearing lipoproteins from plaques and in phagocytosis of blood-borne pathogens, particulate matter, and senescent erythrocytes from the blood (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Heterodimer of an alpha and a beta subunit. Alpha-D associates with beta-2 (By similarity). {ECO:0000250}. DOMAIN: The integrin I-domain (insert) is a VWFA domain. Integrins with I-domains do not undergo protease cleavage. +O88824 JTB_MOUSE Protein JTB 146 16,329 Chain (1); Mutagenesis (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 106 126 Helical. {ECO:0000255}. TOPO_DOM 31 105 Extracellular. {ECO:0000255}.; TOPO_DOM 127 146 Cytoplasmic. {ECO:0000255}. FUNCTION: Required for normal cytokinesis during mitosis. Plays a role in the regulation of cell proliferation. May be a component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Increases AURKB activity (By similarity). Inhibits apoptosis induced by TGFB1. Overexpression induces swelling of mitochondria and reduces mitochondrial membrane potential. {ECO:0000250, ECO:0000269|PubMed:17369841}. PTM: Undergoes N-terminal proteolytic processing, removing a peptide of about 1 kDa from the N-terminus of the protein. {ECO:0000269|PubMed:17369841}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Mitochondrion {ECO:0000269|PubMed:17369841}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Detected at the centrosome and along spindle fibers during prophase and metaphase. Detected at the midbody during telophase (By similarity). {ECO:0000250}. SUBUNIT: Interacts with AURKA, AURKB, BIRC5 and INCENP. May be a component of the CPC at least composed of BIRC5/survivin, CDCA8/borealin, INCENP and AURKB/Aurora-B (By similarity). {ECO:0000250}. +P05555 ITAM_MOUSE Integrin alpha-M (CD11 antigen-like family member B) (CR-3 alpha chain) (Cell surface glycoprotein MAC-1 subunit alpha) (Leukocyte adhesion receptor MO1) (CD antigen CD11b) 1153 127,481 Alternative sequence (1); Calcium binding (3); Chain (1); Disulfide bond (6); Domain (1); Glycosylation (16); Motif (1); Repeat (7); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1106 1129 Helical. {ECO:0000255}. TOPO_DOM 17 1105 Extracellular. {ECO:0000255}.; TOPO_DOM 1130 1153 Cytoplasmic. {ECO:0000255}. FUNCTION: Integrin ITGAM/ITGB2 is implicated in various adhesive interactions of monocytes, macrophages and granulocytes as well as in mediating the uptake of complement-coated particles and pathogens (By similarity). It is identical with CR-3, the receptor for the iC3b fragment of the third complement component. It probably recognizes the R-G-D peptide in C3b. Integrin ITGAM/ITGB2 is also a receptor for fibrinogen, factor X and ICAM1. It recognizes P1 and P2 peptides of fibrinogen gamma chain. Regulates neutrophil migration. In association with beta subunit ITGB2/CD18, required for CD177-PRTN3-mediated activation of TNF primed neutrophils (By similarity). May regulate phagocytosis-induced apoptosis in extravasated neutrophils (By similarity). May play a role in mast cell development (By similarity). {ECO:0000250|UniProtKB:P11215, ECO:0000269|PubMed:8986723, ECO:0000269|PubMed:9382884, ECO:0000269|PubMed:9862668}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8986723, ECO:0000269|PubMed:9862668}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P11215}. Membrane raft {ECO:0000250|UniProtKB:P11215}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P11215}. SUBUNIT: Heterodimer of an alpha and a beta subunit. ITGAM associates with ITGB2. Found in a complex with CD177 and ITGB2/CD18. Interacts with JAM3. Interacts with THBD. Interacts with complement factor H/CFH; this interaction mediates adhesion of neutrophils to pathogens leading to pathogen clearance. {ECO:0000250|UniProtKB:P11215}. DOMAIN: The integrin I-domain (insert) is a VWFA domain. Integrins with I-domains do not undergo protease cleavage. TISSUE SPECIFICITY: Predominantly expressed in monocytes and granulocytes (PubMed:3887182, PubMed:8986723). Expressed in a subset of peritoneal mast cells (PubMed:9862668). {ECO:0000269|PubMed:3887182, ECO:0000269|PubMed:8986723, ECO:0000269|PubMed:9862668}. +P09450 JUNB_MOUSE Transcription factor jun-B (MyD21) 344 35,765 Chain (1); Cross-link (8); Domain (1); Modified residue (7); Region (2); Sequence conflict (2) FUNCTION: Transcription factor involved in regulating gene activity following the primary growth factor response. Binds to the DNA sequence 5'-TGA[CG]TCA-3'. PTM: Ubiquitinated by ITCH, leading to its degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Binds DNA as a homodimer or as a heterodimer with another member of the Jun/Fos family. Interacts with NFE2 (via its WW domains). {ECO:0000250}. +Q9QXH4 ITAX_MOUSE Integrin alpha-X (CD11 antigen-like family member C) (Leukocyte adhesion glycoprotein p150,95 alpha chain) (Leukocyte adhesion receptor p150,95) (CD antigen CD11c) 1169 129,151 Calcium binding (3); Chain (1); Disulfide bond (10); Domain (1); Glycosylation (7); Metal binding (16); Motif (1); Repeat (7); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1117 1137 Helical. {ECO:0000255}. TOPO_DOM 20 1116 Extracellular. {ECO:0000255}.; TOPO_DOM 1138 1169 Cytoplasmic. {ECO:0000255}. FUNCTION: Integrin alpha-X/beta-2 is a receptor for fibrinogen. It recognizes the sequence G-P-R in fibrinogen. It mediates cell-cell interaction during inflammatory responses. It is especially important in monocyte adhesion and chemotaxis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Heterodimer of an alpha and a beta subunit. Alpha-X associates with beta-2 (By similarity). {ECO:0000250}. DOMAIN: The integrin I-domain (insert) is a VWFA domain. Integrins with I-domains do not undergo protease cleavage. +Q6NZK5 K1328_MOUSE Protein hinderin 612 69,793 Alternative sequence (2); Chain (1); Coiled coil (2); Modified residue (5) FUNCTION: Competes with SMC1 for binding to SMC3. May affect the availability of SMC3 to engage in the formation of multimeric protein complexes. {ECO:0000250|UniProtKB:Q86T90}. SUBUNIT: Interacts (via N- and C-terminal domains) with SMC3 (via central hinge region). {ECO:0000250|UniProtKB:Q86T90}. +Q69ZZ9 K0754_MOUSE Uncharacterized protein KIAA0754 979 104,640 Chain (1); Compositional bias (2) +Q5DTW7 K1551_MOUSE Uncharacterized protein KIAA1551 1521 169,044 Alternative sequence (1); Chain (1); Cross-link (2); Erroneous initiation (1); Erroneous termination (1); Frameshift (3); Modified residue (5); Sequence conflict (4) +Q68FF0 K1841_MOUSE Uncharacterized protein KIAA1841 718 81,996 Alternative sequence (1); Chain (1); Erroneous gene model prediction (3); Erroneous initiation (1); Frameshift (1); Sequence conflict (2) +Q99NG9 K199B_MOUSE Keratin-associated protein 19-9b (High-glycine/tyrosine protein type I E5) (Keratin-associated protein 16-10-like) (Keratin-associated protein 16-10b) 58 6,031 Chain (1); Region (1) FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins. {ECO:0000305}. SUBUNIT: Interacts with hair keratins. {ECO:0000250}. +A2AAE1 K1109_MOUSE Transmembrane protein KIAA1109 (Fragile site-associated protein homolog) 5005 555,365 Alternative sequence (7); Chain (1); Compositional bias (8); Erroneous gene model prediction (2); Erroneous initiation (5); Frameshift (1); Modified residue (15); Sequence conflict (12); Transmembrane (1) TRANSMEM 27 47 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Highly expressed in testis and ovary. Weakly or not expressed in other tissues. {ECO:0000269|PubMed:16545529}. +Q61781 K1C14_MOUSE Keratin, type I cytoskeletal 14 (Cytokeratin-14) (CK-14) (Keratin-14) (K14) 484 52,867 Chain (1); Disulfide bond (1); Domain (1); Erroneous initiation (1); Modified residue (1); Region (8); Site (1) FUNCTION: The nonhelical tail domain is involved in promoting KRT5-KRT14 filaments to self-organize into large bundles and enhances the mechanical properties involved in resilience of keratin intermediate filaments in vitro. {ECO:0000250}. PTM: A disulfide bond is formed between rather than within filaments and promotes the formation of a keratin filament cage around the nucleus.; PTM: Ubiquitinated by the BCR(KLHL24) E3 ubiquitin ligase complex. {ECO:0000250|UniProtKB:P02533}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Expressed in both as a filamentous pattern. {ECO:0000250}. SUBUNIT: Heterotetramer of two type I and two type II keratins. disulfide-linked keratin-14 associates with keratin-5. Interacts with TRADD and with keratin filaments. Associates with other type I keratins. Interacts with EPPK1 (PubMed:18285451). Interacts with KLHL24 (By similarity). {ECO:0000250|UniProtKB:P02533, ECO:0000269|PubMed:16702408, ECO:0000269|PubMed:18285451, ECO:0000269|PubMed:22705788}. TISSUE SPECIFICITY: Basal cells of epidermis and other stratified epithelia. +Q9Z2K1 K1C16_MOUSE Keratin, type I cytoskeletal 16 (Cytokeratin-16) (CK-16) (Keratin-16) (K16) 469 51,606 Chain (1); Domain (1); Region (7) FUNCTION: Epidermis-specific type I keratin that plays a key role in skin (PubMed:22336941, PubMed:24218583). Acts as a regulator of innate immunity in response to skin barrier breach: required for some inflammatory checkpoint for the skin barrier maintenance (PubMed:24218583). {ECO:0000269|PubMed:11029038, ECO:0000269|PubMed:22336941, ECO:0000269|PubMed:24218583}. SUBUNIT: Heterodimer of a type I and a type II keratin. KRT16 associates with KRT6 isomers (KRT6A or KRT6B) (PubMed:8636216). Interacts with TCHP (By similarity). Interacts with TRADD (PubMed:16702408). {ECO:0000250|UniProtKB:P08779, ECO:0000269|PubMed:16702408, ECO:0000269|PubMed:8636216}. TISSUE SPECIFICITY: Epidermis-specific. Expressed in stratified epithelia of glabrous skin, the oral mucosa and several appendages. In mature hair follicles, expressed in the companion layer of the outer root sheath during anagen and in the club hair sheath during catagen and telogen. {ECO:0000269|PubMed:12445204}. +Q9D312 K1C20_MOUSE Keratin, type I cytoskeletal 20 (Cytokeratin-20) (CK-20) (Keratin-20) (K20) 431 49,034 Chain (1); Compositional bias (1); Domain (1); Modified residue (3); Region (7); Sequence conflict (3); Site (1) FUNCTION: Plays a significant role in maintaining keratin filament organization in intestinal epithelia. When phosphorylated, plays a role in the secretion of mucin in the small intestine. {ECO:0000269|PubMed:12857878, ECO:0000269|PubMed:16608857}. PTM: Hyperphosphorylation at Ser-13 occurs during the early stages of apoptosis but becomes less prominent during the later stages (By similarity). Phosphorylation at Ser-13 also increases in response to stress brought on by cell injury. {ECO:0000250|UniProtKB:P35900, ECO:0000269|PubMed:16608857, ECO:0000269|PubMed:20724476}.; PTM: Proteolytically cleaved by caspases during apoptosis. Cleavage occurs at Asp-235 (By similarity). {ECO:0000250|UniProtKB:P35900}. SUBUNIT: Heterotetramer of two type I and two type II keratins. Associates with KRT8. {ECO:0000269|PubMed:12857878, ECO:0000305}. TISSUE SPECIFICITY: Expressed at low levels in the more differentiated suprabasal regions of the small intestine, and at higher levels in the colon, mainly in the upper region and in scattered cells throughout the remaining epithelium. Also expressed in epithelial cells of bladder, ileum and stomach and at lower levels in pancreas and earskin. The phosphorylated form is nearly exclusively expressed in goblet cells of the small intestine and in the lumen-proximal cells of the colon (at protein level). Also expressed in jejunum and duodenum. {ECO:0000269|PubMed:12857878, ECO:0000269|PubMed:16608857}. +Q9QWL7 K1C17_MOUSE Keratin, type I cytoskeletal 17 (Cytokeratin-17) (CK-17) (Keratin-17) (K17) 433 48,162 Chain (1); Cross-link (9); Domain (1); Modified residue (10); Mutagenesis (3); Region (7) "FUNCTION: Type I keratin involved in the formation and maintenance of various skin appendages, specifically in determining shape and orientation of hair (PubMed:14714564, PubMed:16702408). Required for the correct growth of hair follicles, in particular for the persistence of the anagen (growth) state (PubMed:16702408). Modulates the function of TNF-alpha in the specific context of hair cycling. Regulates protein synthesis and epithelial cell growth through binding to the adapter protein SFN and by stimulating Akt/mTOR pathway (PubMed:16710422). Involved in tissue repair. May be a marker of basal cell differentiation in complex epithelia and therefore indicative of a certain type of epithelial ""stem cells"". Acts as a promoter of epithelial proliferation by acting a regulator of immune response in skin: promotes Th1/Th17-dominated immune environment contributing to the development of basaloid skin tumors (PubMed:20871598). May act as an autoantigen in the immunopathogenesis of psoriasis, with certain peptide regions being a major target for autoreactive T-cells and hence causing their proliferation. {ECO:0000269|PubMed:14714564, ECO:0000269|PubMed:16702408, ECO:0000269|PubMed:16710422, ECO:0000269|PubMed:20871598, ECO:0000269|PubMed:9786956}." PTM: Phosphorylation at Ser-44 occurs in a growth- and stress-dependent fashion in skin keratinocytes, it has no effect on filament organization. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16702408, ECO:0000269|PubMed:16710422}. SUBUNIT: Heterodimer of a type I and a type II keratin. KRT17 associates with KRT6 isomers (KRT6A or KRT6B) (By similarity). Interacts with TRADD and SFN. {ECO:0000250, ECO:0000269|PubMed:16702408, ECO:0000269|PubMed:16710422}. TISSUE SPECIFICITY: Expressed strongly in outer root sheath and medulla region of hair follicle and in the early differentiating epithelial cells (trichocytes) within the hair bulb region. Weak expression in the matrix cells of hair bulb. Also present in the sweat gland within the skin, vibrissae follicle, salivary gland, tooth and thymus. {ECO:0000269|PubMed:10844551, ECO:0000269|PubMed:14714564, ECO:0000269|PubMed:2433272}. +A1L317 K1C24_MOUSE Keratin, type I cytoskeletal 24 (Cytokeratin-24) (CK-24) (Keratin-24) (K24) (Type I keratin-24) 512 54,041 Chain (1); Domain (1); Region (7); Sequence conflict (2) SUBUNIT: Heterotetramer of two type I and two type II keratins. +P00755 K1KB1_MOUSE Kallikrein 1-related peptidase b1 (EC 3.4.21.35) (Glandular kallikrein K1) (mGK-1) (Tissue kallikrein-1) 261 29,022 Active site (3); Chain (1); Disulfide bond (5); Domain (1); Glycosylation (1); Propeptide (1); Signal peptide (1) FUNCTION: Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin. +P00756 K1KB3_MOUSE Kallikrein 1-related peptidase b3 (EC 3.4.21.35) (7S nerve growth factor gamma chain) (Gamma-NGF) (Glandular kallikrein K3) (mGK-3) (Tissue kallikrein-3) [Cleaved into: Nerve growth factor gamma chain 1; Nerve growth factor gamma chain 2] 261 28,998 Active site (3); Beta strand (14); Chain (3); Disulfide bond (5); Domain (1); Glycosylation (1); Helix (6); Metal binding (2); Propeptide (1); Region (4); Sequence conflict (1); Signal peptide (1) FUNCTION: 7S NGF alpha chain stabilizes the 7S complex. The beta dimer promotes neurite growth. The gamma chain is an arginine-specific protease; it may also have plasminogen activator activity, as well as mitogenic activity for chick embryo fibroblasts. SUBUNIT: 7S nerve growth factor is composed of two alpha chains, a beta dimer composed of identical chains, and two gamma chains. +P05784 K1C18_MOUSE Keratin, type I cytoskeletal 18 (Cytokeratin endo B) (Keratin D) (Cytokeratin-18) (CK-18) (Keratin-18) (K18) 423 47,538 Chain (1); Cross-link (4); Domain (1); Glycosylation (3); Initiator methionine (1); Modified residue (27); Region (10); Sequence conflict (7); Site (3) FUNCTION: When phosphorylated, plays a role in filament reorganization. Involved in the delivery of mutated CFTR to the plasma membrane. Involved in the uptake of thrombin-antithrombin complexes by hepatic cells (By similarity). Together with KRT8, is involved in interleukin-6 (IL-6)-mediated barrier protection. {ECO:0000250, ECO:0000269|PubMed:17213200}. PTM: Phosphorylation increases by IL-6. {ECO:0000269|PubMed:17213200, ECO:0000269|PubMed:20724476}.; PTM: Proteolytically cleaved by caspases during epithelial cell apoptosis. Cleavage occurs at Asp-231 by either caspase-3, caspas-6 or caspase-7. {ECO:0000269|PubMed:9298992}.; PTM: O-GlcNAcylation increases solubility, and decreases stability by inducing proteasomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Cytoplasm {ECO:0000250}. SUBUNIT: Heterotetramer of two type I and two type II keratins. KRT18 associates with KRT8. Interacts with PNN and mutated CFTR. Interacts with YWHAE, YWHAH and YWHAZ only when phosphorylated. Interacts with the thrombin-antithrombin complex. Interacts with DNAJB6, TCHP and TRADD (By similarity). Interacts with FAM83H (By similarity). Interacts with EPPK1 (PubMed:25617501). {ECO:0000250, ECO:0000250|UniProtKB:P05783, ECO:0000269|PubMed:25617501}. TISSUE SPECIFICITY: Expressed in endoderm, intestinal epithelial cells and in most extraembryonic tissues. {ECO:0000269|PubMed:17213200, ECO:0000269|PubMed:2416755, ECO:0000269|PubMed:2454868, ECO:0000269|PubMed:7504637}. +P15949 K1KB9_MOUSE Kallikrein 1-related peptidase b9 (EC 3.4.21.35) (Epidermal growth factor-binding protein type C) (EGF-BP C) (Glandular kallikrein K9) (mGK-9) (Tissue kallikrein-9) 261 28,900 Active site (3); Chain (1); Disulfide bond (5); Domain (1); Glycosylation (1); Propeptide (1); Signal peptide (1) FUNCTION: Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin. +Q9R0H5 K2C71_MOUSE Keratin, type II cytoskeletal 71 (Cytokeratin-6G) (CK-6G) (Cytokeratin-71) (CK-71) (Keratin-6G) (K6G) (Keratin-71) (K71) (Type II inner root sheath-specific keratin-K6irs1) (mK6irs) (mK6irs1/Krt2-6g) (Type-II keratin Kb34) 524 57,383 Chain (1); Compositional bias (1); Domain (1); Mutagenesis (4); Region (7); Site (1) FUNCTION: Plays a central role in hair formation. Essential component of keratin intermediate filaments in the inner root sheath (IRS) of the hair follicle. {ECO:0000269|PubMed:14573483}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q3SY84}. SUBUNIT: Heterodimer of a type I and a type II keratin. Associates with KRT16 and/or KRT17. TISSUE SPECIFICITY: Specifically expressed in the inner root sheath (IRS) of the hair follicle. Present in Henle and the Huxley layers of the IRS, while expression in the cuticle is unsure (at protein level). {ECO:0000269|PubMed:11231308, ECO:0000269|PubMed:11703281, ECO:0000269|PubMed:14573483}. +Q6NXH9 K2C73_MOUSE Keratin, type II cytoskeletal 73 (Cytokeratin-73) (CK-73) (Keratin-73) (K73) (Type II inner root sheath-specific keratin-K6irs3) (Type-II keratin Kb36) 539 58,911 Chain (1); Compositional bias (1); Domain (1); Region (7); Site (1) FUNCTION: Has a role in hair formation. Specific component of keratin intermediate filaments in the inner root sheath (IRS) of the hair follicle (By similarity). {ECO:0000250}. SUBUNIT: Heterotetramer of two type I and two type II keratins. +Q3UV17 K22O_MOUSE Keratin, type II cytoskeletal 2 oral (Keratin-76) (K76) (Type-II keratin Kb9) 594 62,845 Chain (1); Compositional bias (2); Domain (1); Modified residue (3); Region (7) FUNCTION: Probably contributes to terminal cornification. {ECO:0000250|UniProtKB:Q01546}. SUBUNIT: Heterotetramer of two type I and two type II keratins. {ECO:0000305}. +Q6IFZ6 K2C1B_MOUSE Keratin, type II cytoskeletal 1b (Cytokeratin-1B) (CK-1B) (Embryonic type II keratin-1) (Keratin-77) (K77) (Type-II keratin Kb39) 572 61,359 Chain (1); Domain (1); Modified residue (4); Region (7); Site (1) PTM: Undergoes deimination of some arginine residues (citrullination). {ECO:0000269|PubMed:15619433}. TISSUE SPECIFICITY: Expressed in stratified epithelia. {ECO:0000269|PubMed:15085952}. +Q8VED5 K2C79_MOUSE Keratin, type II cytoskeletal 79 (Cytokeratin-79) (CK-79) (Keratin-79) (K79) (Type-II keratin Kb38) 531 57,552 Chain (1); Domain (1); Region (7); Site (1) SUBUNIT: Heterotetramer of two type I and two type II keratins. +Q9DCV7 K2C7_MOUSE Keratin, type II cytoskeletal 7 (Cytokeratin-7) (CK-7) (Keratin-7) (K7) (Type-II keratin Kb7) 457 50,709 Chain (1); Cross-link (5); Domain (1); Initiator methionine (1); Modified residue (12); Region (7); Site (1) FUNCTION: Blocks interferon-dependent interphase and stimulates DNA synthesis in cells. {ECO:0000250}. PTM: Arg-15 is dimethylated, probably to asymmetric dimethylarginine. {ECO:0000250|UniProtKB:P08729}. SUBUNIT: Heterotetramer of two type I and two type II keratins. Interacts with eukaryotic translation initiator factor 3 (eIF3) subunit EIF3S10. Interacts with GPER1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in most simple epithelia tested including liver, lactating mammary gland, lung, kidney, stomach, duodenum, colon, oviduct, uterus, pancreas, epididymis, prostate, preputial gland and mesothelium, and in most stratified epithelia tested including dorsal skin, paw/toe, tail, tongue, cervix, forestomach, and bladder. Also expressed in Henle layer of the inner root sheath of whisker follicle. {ECO:0000269|PubMed:12359226}. +Q61754 K1B24_MOUSE Kallikrein 1-related peptidase b24 (EC 3.4.21.35) (Glandular kallikrein K24) (mGK-24) (Tissue kallikrein 24) 263 28,926 Active site (3); Chain (1); Disulfide bond (5); Domain (1); Glycosylation (3); Propeptide (1); Signal peptide (1) FUNCTION: Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin. {ECO:0000305}. +P59111 KCNH8_MOUSE Potassium voltage-gated channel subfamily H member 8 (Ether-a-go-go-like potassium channel 3) (ELK channel 3) (ELK3) (Voltage-gated potassium channel subunit Kv12.1) 1102 123,277 Chain (1); Compositional bias (1); Domain (2); Glycosylation (2); Intramembrane (1); Motif (1); Nucleotide binding (1); Sequence conflict (2); Topological domain (8); Transmembrane (6) INTRAMEM 420 440 Pore-forming; Name=Segment H5. {ECO:0000255}. TRANSMEM 226 246 Helical; Name=Segment S1. {ECO:0000255}.; TRANSMEM 256 276 Helical; Name=Segment S2. {ECO:0000255}.; TRANSMEM 299 319 Helical; Name=Segment S3. {ECO:0000255}.; TRANSMEM 328 348 Helical; Voltage-sensor; Name=Segment S4. {ECO:0000255}.; TRANSMEM 358 378 Helical; Name=Segment S5. {ECO:0000255}.; TRANSMEM 449 469 Helical; Name=Segment S6. {ECO:0000255}. TOPO_DOM 1 225 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 247 255 Extracellular. {ECO:0000255}.; TOPO_DOM 277 298 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 320 327 Extracellular. {ECO:0000255}.; TOPO_DOM 349 357 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 379 419 Extracellular. {ECO:0000255}.; TOPO_DOM 441 448 Extracellular. {ECO:0000255}.; TOPO_DOM 470 1102 Cytoplasmic. {ECO:0000255}. FUNCTION: Pore-forming (alpha) subunit of voltage-gated potassium channel. Elicits a slowly activating, outward rectifying current (By similarity). Channel properties may be modulated by cAMP and subunit assembly (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SUBUNIT: The potassium channel is probably composed of a homo- or heterotetrameric complex of pore-forming alpha subunits that can associate with modulating beta subunits. DOMAIN: The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position. +Q17ST2 KCNA7_MOUSE Potassium voltage-gated channel subfamily A member 7 (Voltage-gated potassium channel subunit Kv1.7) 489 53,948 Alternative sequence (1); Chain (1); Frameshift (2); Glycosylation (1); Lipidation (1); Motif (1); Sequence conflict (4); Transmembrane (6) TRANSMEM 176 196 Helical; Name=Segment S1. {ECO:0000255}.; TRANSMEM 242 262 Helical; Name=Segment S2. {ECO:0000255}.; TRANSMEM 274 294 Helical; Name=Segment S3. {ECO:0000255}.; TRANSMEM 309 328 Helical; Voltage-sensor; Name=Segment S4. {ECO:0000255}.; TRANSMEM 345 365 Helical; Name=Segment S5. {ECO:0000255}.; TRANSMEM 406 426 Helical; Name=Segment S6. {ECO:0000255}. FUNCTION: Mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient. Channels formed by isoform 1 inactivate faster than channels formed by isoform 2. {ECO:0000269|PubMed:11896454, ECO:0000269|PubMed:16801386, ECO:0000269|PubMed:9488722}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11896454, ECO:0000269|PubMed:16801386, ECO:0000269|PubMed:9488722}; Multi-pass membrane protein {ECO:0000269|PubMed:11896454, ECO:0000269|PubMed:16801386, ECO:0000269|PubMed:9488722}. SUBUNIT: Heterotetramer of potassium channel proteins. {ECO:0000250}. DOMAIN: The N-terminus may be important in determining the rate of inactivation of the channel while the tail may play a role in modulation of channel activity and/or targeting of the channel to specific subcellular compartments.; DOMAIN: The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position. TISSUE SPECIFICITY: Detected in heart, skeletal muscle, brain, and pancreatic islet cells. {ECO:0000269|PubMed:16801386, ECO:0000269|PubMed:9488722}. +Q8BQZ8 KCNS3_MOUSE Potassium voltage-gated channel subfamily S member 3 (Voltage-gated potassium channel subunit Kv9.3) 491 55,993 Chain (1); Intramembrane (2); Motif (1); Topological domain (8); Transmembrane (6) INTRAMEM 358 369 Helical; Name=Pore helix. {ECO:0000250|UniProtKB:P63142}.; INTRAMEM 370 377 {ECO:0000250|UniProtKB:P63142}. TRANSMEM 183 204 Helical; Name=Segment S1. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 221 243 Helical; Name=Segment S2. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 255 275 Helical; Name=Segment S3. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 286 306 Helical; Voltage-sensor; Name=Segment S4. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 322 343 Helical; Name=Segment S5. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 385 413 Helical; Name=Segment S6. {ECO:0000250|UniProtKB:P63142}. TOPO_DOM 1 182 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 205 220 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 244 254 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 276 285 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 307 321 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 344 357 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 378 384 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 414 491 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}. FUNCTION: Potassium channel subunit that does not form functional channels by itself. Can form functional heterotetrameric channels with KCNB1; modulates the delayed rectifier voltage-gated potassium channel activation and deactivation rates of KCNB1. Heterotetrameric channel activity formed with KCNB1 show increased current amplitude with the threshold for action potential activation shifted towards more negative values in hypoxic-treated pulmonary artery smooth muscle cells. {ECO:0000250|UniProtKB:O88759, ECO:0000250|UniProtKB:Q9BQ31}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9BQ31}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9BQ31}. Note=May not reach the plasma membrane but remain in an intracellular compartment in the absence of KCNB1. {ECO:0000250|UniProtKB:Q9BQ31}. SUBUNIT: Heterotetramer with KCNB1. Does not form homomultimers. {ECO:0000250|UniProtKB:Q9BQ31}. DOMAIN: The transmembrane segment S4 functions as voltage-sensor and is characterized by a series of positively charged amino acids at every third position. Channel opening and closing is effected by a conformation change that affects the position and orientation of the voltage-sensor paddle formed by S3 and S4 within the membrane. A transmembrane electric field that is positive inside would push the positively charged S4 segment outwards, thereby opening the pore, while a field that is negative inside would pull the S4 segment inwards and close the pore. Changes in the position and orientation of S4 are then transmitted to the activation gate formed by the inner helix bundle via the S4-S5 linker region. {ECO:0000250|UniProtKB:P63142}. +Q8K201 KCT2_MOUSE Keratinocyte-associated transmembrane protein 2 259 28,050 Chain (1); Erroneous gene model prediction (1); Glycosylation (2); Modified residue (3); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 191 211 Helical. {ECO:0000255}. TOPO_DOM 45 190 Extracellular. {ECO:0000255}.; TOPO_DOM 212 259 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q8VC57 KCTD5_MOUSE BTB/POZ domain-containing protein KCTD5 234 26,164 Chain (1); Domain (1); Initiator methionine (1); Modified residue (1); Sequence conflict (1) FUNCTION: Its interaction with CUL3 suggests that it may act as a substrate adapter in some E3 ligase complex. Does not affect the function of Kv channel Kv2.1/KCNB1, Kv1.2/KCNA2, Kv4.2/KCND2 and Kv3.4/KCNC4 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. SUBUNIT: Homopentamer (By similarity). Interacts (via C-terminus) with GRASP55/GORASP2. Interacts with CUL3 and with ubiquitinated proteins (By similarity). {ECO:0000250}. DOMAIN: The BTB (POZ) domain is atypical and mediates the formation of a homopentamer instead of a homotetramer. Homopentamerization is due to the presence of 4 residues in the BTB (POZ) domain: Leu-56, Gly-100, Val-112 and Ala-118 (By similarity). {ECO:0000250}. +P97794 KCNJ8_MOUSE ATP-sensitive inward rectifier potassium channel 8 (Inward rectifier K(+) channel Kir6.1) (Potassium channel, inwardly rectifying subfamily J member 8) (uKATP-1) 424 47,980 Chain (1); Intramembrane (2); Modified residue (1); Motif (1); Site (1); Topological domain (4); Transmembrane (2) INTRAMEM 127 138 Helical; Pore-forming; Name=H5. {ECO:0000250}.; INTRAMEM 139 145 Pore-forming. {ECO:0000250}. TRANSMEM 70 94 Helical; Name=M1. {ECO:0000250}.; TRANSMEM 155 176 Helical; Name=M2. {ECO:0000250}. TOPO_DOM 1 69 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 95 126 Extracellular. {ECO:0000250}.; TOPO_DOM 146 154 Extracellular. {ECO:0000250}.; TOPO_DOM 177 424 Cytoplasmic. {ECO:0000250}. FUNCTION: This potassium channel is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by external barium (By similarity). {ECO:0000250|UniProtKB:Q63664}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein {ECO:0000305}. +Q6ZQ88 KDM1A_MOUSE Lysine-specific histone demethylase 1A (EC 1.-.-.-) (BRAF35-HDAC complex protein BHC110) (Flavin-containing amine oxidase domain-containing protein 2) 853 92,851 Binding site (5); Chain (1); Coiled coil (2); Compositional bias (2); Cross-link (3); Domain (1); Erroneous initiation (2); Modified residue (9); Nucleotide binding (1); Region (1); Sequence conflict (1) FUNCTION: Histone demethylase that demethylates both 'Lys-4' (H3K4me) and 'Lys-9' (H3K9me) of histone H3, thereby acting as a coactivator or a corepressor, depending on the context. Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed. Acts as a corepressor by mediating demethylation of H3K4me, a specific tag for epigenetic transcriptional activation. Demethylates both mono- (H3K4me1) and di-methylated (H3K4me2) H3K4me. May play a role in the repression of neuronal genes. Alone, it is unable to demethylate H3K4me on nucleosomes and requires the presence of RCOR1/CoREST to achieve such activity. Also acts as a coactivator of androgen receptor (ANDR)-dependent transcription, by being recruited to ANDR target genes and mediating demethylation of H3K9me, a specific tag for epigenetic transcriptional repression. The presence of PRKCB in ANDR-containing complexes, which mediates phosphorylation of 'Thr-6' of histone H3 (H3T6ph), a specific tag that prevents demethylation H3K4me, prevents H3K4me demethylase activity of KDM1A. Demethylates di-methylated 'Lys-370' of p53/TP53 which prevents interaction of p53/TP53 with TP53BP1 and represses p53/TP53-mediated transcriptional activation (By similarity). Demethylates and stabilizes the DNA methylase DNMT1. Required for gastrulation during embryogenesis. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. Effector of SNAI1-mediated transcription repression of E-cadherin/CDH1, CDN7 and KRT8. Required for the maintenance of the silenced state of the SNAI1 target genes E-cadherin/CDH1 and CDN7. {ECO:0000250, ECO:0000269|PubMed:17707228, ECO:0000269|PubMed:19098913}. PTM: Polyubiquitinated by JADE2; which leads to its proteasomal degradation. {ECO:0000269|PubMed:25018020}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of a BHC histone deacetylase complex that contains HDAC1, HDAC2, HMG20B, KDM1A, RCOR1 and PHF21A. The BHC complex may also contain ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I. In the complex, RCOR1 strongly enhances the demethylase activity and protects it from the proteasome while PHF21A inhibits the demethylase activity. Interacts with the androgen receptor (AR) (By similarity). Component of a RCOR/GFI/KDM1A/HDAC complex. Interacts directly with GFI1 and GFI1B (PubMed:17707228). Interacts with SNAI1 (via SNAG domain) (By similarity). Interacts with INSM1 (PubMed:24227653). Interacts (via AOD/Tower domain) with JADE2 (via C-terminus) (PubMed:25018020). Interacts with ESRRB; co-occupes the core set of ESRRB targets (PubMed:26206133). {ECO:0000250|UniProtKB:O60341, ECO:0000269|PubMed:17707228, ECO:0000269|PubMed:24227653, ECO:0000269|PubMed:25018020, ECO:0000269|PubMed:26206133}. DOMAIN: The SWIRM domain may act as an anchor site for a histone tail. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:16079795}. +Q8VCD7 KDM4C_MOUSE Lysine-specific demethylase 4C (EC 1.14.11.-) (JmjC domain-containing histone demethylation protein 3C) (Jumonji domain-containing protein 2C) 1054 119,966 Binding site (4); Chain (1); Domain (4); Erroneous initiation (1); Metal binding (7); Sequence conflict (2); Zinc finger (3) FUNCTION: Histone demethylase that specifically demethylates 'Lys-9' and 'Lys-36' residues of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27' nor H4 'Lys-20'. Demethylates trimethylated H3 'Lys-9' and H3 'Lys-36' residue, while it has no activity on mono- and dimethylated residues. Demethylation of Lys residue generates formaldehyde and succinate (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00537}. DOMAIN: The 2 Tudor domains recognize and bind methylated histones. Double Tudor domain has an interdigitated structure and the unusual fold is required for its ability to bind methylated histone tails (By similarity). {ECO:0000250}. +Q3U2K5 KDM4D_MOUSE Lysine-specific demethylase 4D (EC 1.14.11.-) (JmjC domain-containing histone demethylation protein 3D) (Jumonji domain-containing protein 2D) 510 57,212 Binding site (4); Chain (1); Compositional bias (1); Domain (2); Erroneous initiation (1); Erroneous termination (1); Frameshift (1); Metal binding (7); Modified residue (2); Sequence conflict (1) FUNCTION: Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27', H3 'Lys-36' nor H4 'Lys-20'. Demethylates both di- and trimethylated H3 'Lys-9' residue, while it has no activity on monomethylated residues. Demethylation of Lys residue generates formaldehyde and succinate (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00537}. +Q80Y84 KDM5B_MOUSE Lysine-specific demethylase 5B (EC 1.14.11.-) (Histone demethylase JARID1B) (Jumonji/ARID domain-containing protein 1B) (PLU-1) 1544 175,555 Alternative sequence (1); Beta strand (2); Binding site (4); Chain (1); Cross-link (8); Domain (3); Erroneous initiation (1); Helix (6); Metal binding (3); Modified residue (4); Mutagenesis (1); Sequence conflict (6); Turn (1); Zinc finger (4) FUNCTION: Histone demethylase that demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-9' or H3 'Lys-27'. Demethylates trimethylated, dimethylated and monomethylated H3 'Lys-4'. Acts as a transcriptional corepressor for FOXG1B and PAX9. Represses the CLOCK-ARNTL/BMAL1 heterodimer-mediated transcriptional activation of the core clock component PER2. {ECO:0000269|PubMed:17310255, ECO:0000269|PubMed:17320160, ECO:0000269|PubMed:21960634}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355, ECO:0000255|PROSITE-ProRule:PRU00537, ECO:0000269|PubMed:14579128}. SUBUNIT: Interacts with FOXG1B, PAX9, MYC, MYCN and RB1. Interacts with HDAC1, HDAC4, HDAC5 and HDAC7. Interacts (via PHD-type 1 zinc finger) with histone H3 unmodified at 'Lys-4'; the interaction is inhibited when histone H3 is methylated at 'Arg-2' or 'Lys-4' (By similarity). {ECO:0000250|UniProtKB:Q9UGL1}. DOMAIN: Both the JmjC domain and the JmjN domain are required for enzymatic activity. However ARID and PHD-type 1 domain are not required for activity per se but contributed to recognition of the H3(1-21)K4me2 substrate peptide. {ECO:0000250|UniProtKB:Q9UGL1}.; DOMAIN: The 2 first PHD-type zinc finger domains are required for transcription repression activity. {ECO:0000250}. TISSUE SPECIFICITY: Present at highest levels in testis, where it is enriched in spermatogonia and pachytene cells (at protein level). {ECO:0000269|PubMed:12237901, ECO:0000269|PubMed:14516692, ECO:0000269|PubMed:14579128}. +Q5NCY0 KDM6B_MOUSE Lysine-specific demethylase 6B (EC 1.14.11.-) (JmjC domain-containing protein 3) (Jumonji domain-containing protein 3) 1641 176,355 Beta strand (20); Chain (1); Compositional bias (5); Cross-link (1); Domain (1); Erroneous initiation (1); Helix (21); Metal binding (7); Modified residue (1); Mutagenesis (3); Sequence conflict (3); Turn (5) FUNCTION: Histone demethylase that specifically demethylates 'Lys-27' of histone H3, thereby playing a central role in histone code. Demethylates trimethylated and dimethylated H3 'Lys-27'. Plays a central role in regulation of posterior development, by regulating HOX gene expression. Involved in inflammatory response by participating in macrophage differentiation in case of inflammation by regulating gene expression and macrophage differentiation (PubMed:17825402). Plays a demethylase-independent role in chromatin remodeling to regulate T-box family member-dependent gene expression by acting as a link between T-box factors and the SMARCA4-containing SWI/SNF remodeling complex (PubMed:21095589). {ECO:0000269|PubMed:17825402, ECO:0000269|PubMed:21095589}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with TLE1 (PubMed:21095589). Component of the MLL4 complex, at least composed of KMT2B/MLL4, ASH2L, RBBP5, WDR5, and KDM6B (By similarity). Interacts with TBX21, SMARCA4, SMARCC1 and SMARCC2 (PubMed:21095589). {ECO:0000250|UniProtKB:O15054, ECO:0000269|PubMed:21095589, ECO:0000269|PubMed:9854018}. +Q3UWM4 KDM7A_MOUSE Lysine-specific demethylase 7A (EC 1.14.11.-) (JmjC domain-containing histone demethylation protein 1D) (Lysine-specific demethylase 7) 940 106,075 Binding site (2); Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (2); Metal binding (3); Modified residue (1); Region (1); Sequence conflict (1); Zinc finger (1) FUNCTION: Histone demethylase required for brain development. Specifically demethylates dimethylated 'Lys-9' and 'Lys-27' (H3K9me2 and H3K27me2, respectively) of histone H3 and monomethylated histone H4 'Lys-20' residue (H4K20Me1), thereby playing a central role in histone code. Specifically binds trimethylated 'Lys-4' of histone H3 (H3K4me3), affecting histone demethylase specificity: in presence of H3K4me3, it has no demethylase activity toward H3K9me2, while it has high activity toward H3K27me2. Demethylates H3K9me2 in absence of H3K4me3. Has activity toward H4K20Me1 only when nucleosome is used as a substrate and when not histone octamer is used as substrate (By similarity). {ECO:0000250, ECO:0000269|PubMed:20194436}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. DOMAIN: The PHD-type zinc finger mediates the binding to H3K4me3. Binding to H3K4me3 prevents its access to H3K9me2 (By similarity). {ECO:0000250}.; DOMAIN: The linker region is a critical determinant of demethylase specificity. It prevents the active site of JmjC to reach the target H3K9me2 when the PHD-type zinc finger binds to H3K4me3, while it favors selectivity toward H3K27me2 (By similarity). {ECO:0000250}. +Q8BVH9 METL6_MOUSE Methyltransferase-like protein 6 (EC 2.1.1.-) 282 32,786 Alternative sequence (2); Chain (1) FUNCTION: Probable methyltransferase. {ECO:0000250}. +A2AUU0 METL8_MOUSE Methyltransferase-like protein 8 (EC 2.1.1.-) (Tension-induced/inhibited protein) 281 31,670 Alternative sequence (5); Chain (1); Erroneous initiation (3); Sequence caution (1); Sequence conflict (19) FUNCTION: Probable methyltransferase (By similarity). Isoform 5 overexpression in lung progenitor cells stimulates smooth muscle-specific gene expression and suppresses adipogenic gene expression. Isoform 4 and isoform 7 stimulate adipogenesis. {ECO:0000250, ECO:0000269|PubMed:15992539, ECO:0000269|PubMed:18710950}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15992539}. Nucleus {ECO:0000269|PubMed:15992539}. Note=Isoform 5 localizes to the nucleus upon cell stretch in embryonic lung progenitor cells. SUBUNIT: Interacts with EP300. {ECO:0000269|PubMed:18710950}. TISSUE SPECIFICITY: Isoform 5 is absent in undifferentiated embryonic lung mesenchymal cells, but expression is induced by stretch. Isoform 4 is expressed in undifferentiated progenitor cells, while its expression is inhibited by stretch. Isoform 2 is absent in embryonic lung but is induced in a fibroblast cell line by stretch. Isoform 7 is expressed in mature adipose tissue. {ECO:0000269|PubMed:15992539}. +Q9EPL4 METL9_MOUSE Methyltransferase-like protein 9 (DORA reverse strand protein) (DREV) 318 36,426 Chain (1); Compositional bias (1); Erroneous initiation (1); Frameshift (1); Glycosylation (1); Sequence conflict (4); Signal peptide (1) TISSUE SPECIFICITY: Expressed in liver, colon, small intestine, skin, kidney and to a lesser extent in spleen, lung, thymus and stomach. Not detected in fibroblast and endothelial cells. {ECO:0000269|PubMed:11132146}. +Q8C1Q4 METRN_MOUSE Meteorin (Hypoxia/reoxygenation regulatory factor) 291 31,469 Alternative sequence (2); Chain (1); Disulfide bond (5); Erroneous initiation (1); Signal peptide (1) FUNCTION: Involved in both glial cell differentiation and axonal network formation during neurogenesis. Promotes astrocyte differentiation and transforms cerebellar astrocytes into radial glia. Also induces axonal extension in small and intermediate neurons of sensory ganglia by activating nearby satellite glia. {ECO:0000269|PubMed:15085178}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15085178}. SUBUNIT: Monomer. {ECO:0000269|PubMed:19259827}. TISSUE SPECIFICITY: Highly expressed in brain. Expressed in undifferentiated neural progenitors and in astrocyte lineage, particulary in Bergmann glia, a subtype of radial glia, and a few discrete neuronal populations residing in the superior colliculus, the ocular motor nucleus, the raphe and pontine nuclei, and in various thalamic nuclei. Weakly expressed in heart, kidney, skeletal muscle, spleen, testis, gut and lung. {ECO:0000269|PubMed:15085178, ECO:0000269|PubMed:19259827}. +O35345 IMA7_MOUSE Importin subunit alpha-7 (Importin alpha-S2) (Karyopherin subunit alpha-6) 536 59,964 Chain (1); Compositional bias (1); Domain (1); Modified residue (3); Motif (1); Region (2); Repeat (10); Sequence conflict (3) FUNCTION: Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Forms a complex with importin subunit beta-1 (By similarity). Interacts with ZIC3. {ECO:0000250, ECO:0000269|PubMed:18716025}. DOMAIN: Consists of an N-terminal hydrophilic region, a hydrophobic central region composed of 10 repeats, and a short hydrophilic C-terminus. The N-terminal hydrophilic region contains the importin beta binding domain (IBB domain), which is sufficient for binding importin beta and essential for nuclear protein import.; DOMAIN: The IBB domain is thought to act as an intrasteric autoregulatory sequence by interacting with the internal autoinhibitory NLS. Binding of KPNB1 probably overlaps the internal NLS and contributes to a high affinity for cytoplasmic NLS-containing cargo substrates. After dissociation of the importin/substrate complex in the nucleus the internal autohibitory NLS contributes to a low affinity for nuclear NLS-containing proteins (By similarity). {ECO:0000250}.; DOMAIN: The major and minor NLS binding sites are mainly involved in recognition of simple or bipartite NLS motifs. Structurally located within in a helical surface groove they contain several conserved Trp and Asn residues of the corresponding third helices (H3) of ARM repeats which mainly contribute to binding (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Only slightly detected in Ehrlich ascites tumor cells, thymus and skeletal muscle, clearly detected in kidney, spleen, liver, heart, and lung. High expression in testis. +Q8K2V6 IPO11_MOUSE Importin-11 (Imp11) (Ran-binding protein 11) (RanBP11) 975 112,416 Alternative sequence (1); Chain (1); Domain (1); Modified residue (2); Repeat (14); Sequence conflict (1) FUNCTION: Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (By similarity). Mediates the nuclear import of RPL12, and of UBE2E3 (By similarity). {ECO:0000250, ECO:0000269|PubMed:11809816}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Interacts with UBE2E3 and RPL12. {ECO:0000269|PubMed:11809816}. +Q8VI75 IPO4_MOUSE Importin-4 (Imp4) (Importin-4a) (Imp4a) (Ran-binding protein 4) (RanBP4) 1082 119,275 Chain (1); Domain (1); Erroneous initiation (2); Modified residue (1); Repeat (6) FUNCTION: Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (By similarity). Mediates the nuclear import of RPS3A. Acts as chaperone for exposed basic domains. {ECO:0000250, ECO:0000269|PubMed:11823430}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Binds with high affinity to RPS3A. The binding is coupled to RanGTP cycles. Found in a cytosolic complex with ASF1A, ASF1B, CDAN1 and histones H3.1 and H4 (By similarity). {ECO:0000250}. +Q9EPL8 IPO7_MOUSE Importin-7 (Imp7) (Ran-binding protein 7) (RanBP7) 1038 119,486 Chain (1); Compositional bias (1); Domain (1); Modified residue (5); Sequence conflict (2) FUNCTION: Functions in nuclear protein import, either by acting as autonomous nuclear transport receptor or as an adapter-like protein in association with the importin-beta subunit KPNB1. Acting autonomously is thought to serve itself as receptor for nuclear localization signals (NLS) and to promote translocation of import substrates through the nuclear pore complex (NPC) by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. Mediates autonomously the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5. Binds to a beta-like import receptor binding (BIB) domain of RPL23A. In association with KPNB1 mediates the nuclear import of H1 histone and the Ran-binding site of IPO7 is not required but synergizes with that of KPNB1 in importin/substrate complex dissociation (By similarity). In vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones. {ECO:0000250, ECO:0000269|PubMed:11493596}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Forms a heterodimer with KPNB1. Interacts with KPNB1, RNUT1, XPO1, RPL23A, RPS7 and RPL5. Binds directly to nuclear pore complexes (By similarity). Interacts with H2A, H2B, H3 and H4 histones. Interacts with SMAD4 and NUP93; translocates SMAD4 to the nucleus through the NPC upon BMP7 stimulation resulting in activation of SMAD4 signaling (By similarity). {ECO:0000250|UniProtKB:O95373, ECO:0000269|PubMed:11493596}. +Q7TMY7 IPO8_MOUSE Importin-8 (Imp8) (Ran-binding protein 8) (RanBP8) 1010 117,078 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (1); Modified residue (2); Sequence conflict (2) FUNCTION: Seems to function in nuclear protein import, either by acting as autonomous nuclear transport receptor or as an adapter-like protein in association with the importin-beta subunit KPNB1. Acting autonomously, is thought to serve itself as receptor for nuclear localization signals (NLS) and to promote translocation of import substrates through the nuclear pore complex (NPC) by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. In vitro mediates the nuclear import of SRP19 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Forms a heterodimer with KPNB1. Interacts with SRP19. Binds directly to nuclear pore complexes (By similarity). {ECO:0000250}. +Q6P1C1 IPPK_MOUSE Inositol-pentakisphosphate 2-kinase (EC 2.7.1.158) (Inositol-1,3,4,5,6-pentakisphosphate 2-kinase) (Ins(1,3,4,5,6)P5 2-kinase) (InsP5 2-kinase) 489 55,928 Beta strand (15); Chain (1); Helix (18); Motif (1); Sequence conflict (1); Turn (6) FUNCTION: Phosphorylates Ins(1,3,4,5,6)P5 at position 2 to form Ins(1,2,3,4,5,6)P6 (InsP6 or phytate). InsP6 is involved in many processes such as mRNA export, non-homologous end-joining, endocytosis, ion channel regulation. It also protects cells from TNF-alpha-induced apoptosis. {ECO:0000269|PubMed:15939868}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. DOMAIN: The EXKPK motif is conserved in inositol-pentakisphosphate 2-kinases of both family 1 and 2. TISSUE SPECIFICITY: In brain, it is expressed throughout the hippocampus (CA1, CA2, CA3 and dentate gyrus), inner layers of the cerebral cortex, and Purkinje cells of the cerebellum. In heart, it is expressed in cardiomyocytes but not in interstitial cells, blood vessels, or valves. Also expressed in testis. {ECO:0000269|PubMed:15939868}. +P28575 IPP_MOUSE Actin-binding protein IPP (Intracisternal A particle-promoted polypeptide) (IPP) (Murine IAP-promoted placenta-expressed protein) (Protein MIPP) 584 65,216 Chain (1); Domain (1); Frameshift (3); Repeat (6); Sequence conflict (5) FUNCTION: May play a role in organizing the actin cytoskeleton. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. TISSUE SPECIFICITY: Expression seems confined to tissues derived from trophectoderm and primitive endoderm. {ECO:0000269|PubMed:1905535}. +P70458 IPSP_MOUSE Plasma serine protease inhibitor (Plasminogen activator inhibitor 3) (PAI-3) (PAI3) (Protein C inhibitor) (PCI) (Serpin A5) 405 45,600 Chain (1); Glycosylation (1); Propeptide (1); Sequence conflict (8); Signal peptide (1); Site (1) FUNCTION: Heparin-dependent serine protease inhibitor acting in body fluids and secretions. Inactivates serine proteases by binding irreversibly to their serine activation site. Involved in the regulation of intravascular and extravascular proteolytic activities. Plays hemostatic roles in the blood plasma. Acts as a procoagulant and proinflammatory factor by inhibiting the anticoagulant activated protein C factor as well as the generation of activated protein C factor by the thrombin/thrombomodulin complex. Acts as an anticoagulant factor by inhibiting blood coagulation factors like prothrombin, factor XI, factor Xa, plasma kallikrein and fibrinolytic enzymes such as tissue- and urinary-type plasminogen activators. In seminal plasma, inactivates several serine proteases implicated in the reproductive system. Inhibits the serpin acrosin; indirectly protects component of the male genital tract from being degraded by excessive released acrosin. Inhibits tissue-and urinary-type plasminogen activator, prostate-specific antigen and kallikrein activities; has a control on the sperm motility and fertilization. Inhibits the activated protein C-catalyzed degradation of SEMG1 and SEMG2; regulates the degradation of semenogelin during the process of transfer of spermatozoa from the male reproductive tract into the female tract. In urine, inhibits urinary-type plasminogen activator and kallikrein activities. Inactivates membrane-anchored serine proteases activities such as MPRSS7 and TMPRSS11E. Inhibits urinary-type plasminogen activator-dependent tumor cell invasion and metastasis. May also play a non-inhibitory role in seminal plasma and urine as a hydrophobic hormone carrier by its binding to retinoic acid (By similarity). {ECO:0000250}. PTM: N-glycosylated; glycans consist of a mixture of sialylated bi- (including sialyl-Lewis X epitopes), tri- and tetra-antennary complex-type chains; affects the maximal heparin- and thrombomodulin-enhanced rates of thrombin inhibition. O-glycosylated; further modified with 2 sialic acid residues. Proteolytically cleaved at the N-terminus; inhibits slightly the heparin- and thrombomodulin-enhanced rates of thrombin inhibition (By similarity). {ECO:0000250}.; PTM: Proteolytically cleaved. Inhibition of proteases is accompanied by formation of a stable enzyme-inhibitor complex and by degradation of the serpin to lower molecular weight derivatives (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250}. Note=Localized on the plasma membrane overlying the acrosomal head of spermatozoa of ependymal spermatozoa and ejaculated sperm. Localized at the equatorial segment of acrosome-reacted spematozoa. Localized in alpha granules in resting platelets and on the external plasma membrane and within the surface-connected cannalicular system in activated platelets (By similarity). {ECO:0000250}. SUBUNIT: Forms protease inhibiting heterodimers in extracellular body fluids with serine proteases such as activated protein C/coagulation factor V/F5, acrosin/ACR, chymotrypsinogen B/CTRB1, prothrombin/F2, factor Xa/F10, factor XI/F11, kallikrein/KLKB1, tissue kallikrein, trypsin/PRSS1, prostate specific antigen/KLK3, tissue plasminogen activator/PLAT and urinary plasminogen activator/PLAU. Forms membrane-anchored serine proteases inhibiting heterodimers with TMPRSS7 and TMPRSS11E. Interacts with SEMG2 (By similarity). {ECO:0000250}. DOMAIN: The reactive center loop (RCL) extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site within the RCL, establishing a covalent linkage between the carboxyl group of the serpin reactive site and the serine hydroxyl of the protease. The resulting inactive serpin-protease complex is highly stable (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Not detected in blood plasma (at protein level). Expressed in testis, epididymis, seminal vesicles, prostate and ovaries. {ECO:0000269|PubMed:15140131}. +Q91VM9 IPYR2_MOUSE Inorganic pyrophosphatase 2, mitochondrial (EC 3.6.1.1) (Pyrophosphate phospho-hydrolase 2) (PPase 2) 330 38,115 Alternative sequence (2); Chain (1); Metal binding (4); Modified residue (4); Sequence conflict (3); Transit peptide (1) FUNCTION: Hydrolyzes inorganic pyrophosphate. This activity is essential for correct regulation of mitochondrial membrane potential, and mitochondrial organization and function. {ECO:0000250|UniProtKB:Q9H2U2}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}. SUBUNIT: Homodimer. {ECO:0000250}. +Q8CFA1 IRAK2_MOUSE Interleukin-1 receptor-associated kinase-like 2 (IRAK-2) (mu-IRAK-2) 622 69,047 Alternative sequence (4); Binding site (1); Chain (1); Domain (2); Nucleotide binding (2); Sequence conflict (19) FUNCTION: Binds to the IL-1 type I receptor following IL-1 engagement, triggering intracellular signaling cascades leading to transcriptional up-regulation and mRNA stabilization. {ECO:0000250}. SUBUNIT: Interacts with MYD88. IL-1 stimulation leads to the formation of a signaling complex which dissociates from the IL-1 receptor following the binding of PELI1 (By similarity). {ECO:0000250}. DOMAIN: The protein kinase domain is predicted to be catalytically inactive. TISSUE SPECIFICITY: Ubiquitously expressed, with a higher expression observed in brain, spleen and liver. Isoform 1 and isoform 2 are considered agonist and isoform 3 and isoform 4 are considered antagonist. +Q8K4B2 IRAK3_MOUSE Interleukin-1 receptor-associated kinase 3 (IRAK-3) (EC 2.7.11.1) (IL-1 receptor-associated kinase M) (IRAK-M) 609 68,455 Binding site (2); Chain (1); Domain (2); Modified residue (1); Nucleotide binding (2); Sequence conflict (7) FUNCTION: Inhibits dissociation of IRAK1 and IRAK4 from the Toll-like receptor signaling complex by either inhibiting the phosphorylation of IRAK1 and IRAK4 or stabilizing the receptor complex. {ECO:0000269|PubMed:12054681, ECO:0000269|PubMed:12150927, ECO:0000303|PubMed:12150927}. TISSUE SPECIFICITY: Highly expressed in liver and thymus and at lower levels in heart, brain, spleen and kidney. {ECO:0000269|PubMed:12054681}. +P59823 IRPL1_MOUSE Interleukin-1 receptor accessory protein-like 1 (IL-1-RAPL-1) (IL-1RAPL-1) (IL1RAPL-1) (X-linked interleukin-1 receptor accessory protein-like 1) 695 79,630 Beta strand (30); Chain (1); Disulfide bond (5); Domain (4); Glycosylation (6); Helix (4); Mutagenesis (5); Region (1); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1); Turn (2) TRANSMEM 358 378 Helical. {ECO:0000255}. TOPO_DOM 25 357 Extracellular. {ECO:0000255}.; TOPO_DOM 379 695 Cytoplasmic. {ECO:0000255}. FUNCTION: May regulate secretion and presynaptic differentiation through inhibition of the activity of N-type voltage-gated calcium channel. May activate the MAP kinase JNK (By similarity). Plays a role in neurite outgrowth (By similarity). During dendritic spine formation can bidirectionally induce pre- and post-synaptic differentiation of neurons by trans-synaptically binding to PTPRD (PubMed:25908590, PubMed:21940441). {ECO:0000250|UniProtKB:P59824, ECO:0000250|UniProtKB:Q9NZN1, ECO:0000269|PubMed:21940441, ECO:0000269|PubMed:25908590}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell projection, axon {ECO:0000269|PubMed:21940441}. Cell projection, dendrite {ECO:0000269|PubMed:21940441}. Note=May localize to the cell body and growth cones of dendrite-like processes. SUBUNIT: Homodimer (PubMed:25908590). Interacts (calcium-independent) with NCS1/FREQ (By similarity). Interacts (via the first immunoglobilin domain) with PTPRD (via the second immunoglobilin domain); this interaction is PTPRD-splicing-dependent and induces pre- and post-synaptic differentiation of neurons and is required for IL1RAPL1-mediated synapse formation (PubMed:25908590, PubMed:21940441). {ECO:0000250|UniProtKB:Q9NZN1, ECO:0000269|PubMed:21940441, ECO:0000269|PubMed:25908590}. TISSUE SPECIFICITY: Detected in total brain extracts, olfactory bulb, hippocampus and striatum (at protein level). {ECO:0000269|PubMed:12783849}. +Q64287 IRF4_MOUSE Interferon regulatory factor 4 (IRF-4) (Lymphocyte-specific interferon regulatory factor) (LSIRF) (NF-EM5) (PU.1 interaction partner) (Transcriptional activator PIP) 450 51,577 Alternative sequence (1); Beta strand (13); Chain (1); DNA binding (1); Helix (4); Modified residue (2) FUNCTION: Transcriptional activator. Binds to the interferon-stimulated response element (ISRE) of the MHC class I promoter. Binds the immunoglobulin lambda light chain enhancer, together with PU.1. Probably plays a role in ISRE-targeted signal transduction mechanisms specific to lymphoid cells. Involved in CD8(+) dendritic cell differentiation by forming a complex with the BATF-JUNB heterodimer in immune cells, leading to recognition of AICE sequence (5'-TGAnTCA/GAAA-3'), an immune-specific regulatory element, followed by cooperative binding of BATF and IRF4 and activation of genes. {ECO:0000269|PubMed:22983707, ECO:0000269|PubMed:22992523, ECO:0000269|PubMed:22992524}. PTM: Phosphorylation by ROCK2 regulates IL-17 and IL-21 production. {ECO:0000269|PubMed:20697158}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with SPIB and DEF6 (By similarity). Interacts with the BATF-JUNB heterodimer. Interacts with BATF (via bZIP domain); the interaction is direct. Directly interacts with NLRP3 in the nucleus of Th2 cells; this interaction enhances IRF4 ability to bind to the IL4 promoter and is required for optimal IRF4-dependent IL4 transcription (PubMed:26098997). {ECO:0000250, ECO:0000269|PubMed:22983707, ECO:0000269|PubMed:22992523, ECO:0000269|PubMed:22992524, ECO:0000269|PubMed:26098997}. TISSUE SPECIFICITY: Lymphoid cells. +P70434 IRF7_MOUSE Interferon regulatory factor 7 (IRF-7) 457 51,222 Beta strand (4); Chain (1); Cross-link (2); DNA binding (1); Helix (5); Modified residue (8); Mutagenesis (17) FUNCTION: Key transcriptional regulator of type I interferon (IFN)-dependent immune responses and plays a critical role in the innate immune response against DNA and RNA viruses. Regulates the transcription of type I IFN genes (IFN-alpha and IFN-beta) and IFN-stimulated genes (ISG) by binding to an interferon-stimulated response element (ISRE) in their promoters. Can efficiently activate both the IFN-beta (IFNB) and the IFN-alpha (IFNA) genes and mediate their induction via both the virus-activated, MyD88-independent pathway and the TLR-activated, MyD88-dependent pathway. Required during both the early and late phases of the IFN gene induction but is more critical for the late than for the early phase. Exists in an inactive form in the cytoplasm of uninfected cells and following viral infection, double-stranded RNA (dsRNA), or toll-like receptor (TLR) signaling, becomes phosphorylated by IKBKE and TBK1 kinases. This induces a conformational change, leading to its dimerization and nuclear localization where along with other coactivators it can activate transcription of the type I IFN and ISG genes. Can also play a role in regulating adaptive immune responses by inducing PSMB9/LMP2 expression, either directly or through induction of IRF1. Binds to the Q promoter (Qp) of EBV nuclear antigen 1 a (EBNA1) and may play a role in the regulation of EBV latency. Can activate distinct gene expression programs in macrophages and regulate the anti-tumor properties of primary macrophages. {ECO:0000269|PubMed:15361868, ECO:0000269|PubMed:15743772, ECO:0000269|PubMed:15800576, ECO:0000269|PubMed:18562536}. PTM: Acetylation inhibits its DNA-binding ability and activity. {ECO:0000250}.; PTM: In response to a viral infection, phosphorylated by TBK1 and IKBKE1. Phosphorylation, and subsequent activation is inhibited by vaccinia virus protein E3. In TLR7- and TLR9-mediated signaling pathway, phosphorylated by IRAK1 (By similarity). {ECO:0000250}.; PTM: TRAF6-mediated ubiquitination is required for IRF7 activation. {ECO:0000269|PubMed:15361868}.; PTM: Sumoylated by TRIM28, which inhibits its transactivation activity. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15361868}. Cytoplasm {ECO:0000269|PubMed:15361868}. Note=The phosphorylated and active form accumulates selectively in the nucleus. SUBUNIT: Monomer. Homodimer; phosphorylation-induced. Heterodimer with IRF3. Interacts with TICAM1 and TICAM2. Interacts with MYD88 AND TRAF6. {ECO:0000269|PubMed:15361868}. +P23611 IRF8_MOUSE Interferon regulatory factor 8 (IRF-8) (Interferon consensus sequence-binding protein) (ICSBP) 424 48,237 Chain (1); DNA binding (1) FUNCTION: Plays a role as a transcriptional activator or repressor (By similarity). Specifically binds to the upstream regulatory region of type I IFN and IFN-inducible MHC class I genes (the interferon consensus sequence (ICS)). Plays a negative regulatory role in cells of the immune system. Involved in CD8(+) dendritic cell differentiation by forming a complex with the BATF-JUNB heterodimer in immune cells, leading to recognition of AICE sequence (5'-TGAnTCA/GAAA-3'), an immune-specific regulatory element, followed by cooperative binding of BATF and IRF8 and activation of genes (PubMed:22992524). Positively regulates macroautophagy in dendritic cells (By similarity). {ECO:0000250|UniProtKB:Q02556, ECO:0000269|PubMed:22992524}. PTM: Ubiquitinated (PubMed:17579016). Ubiquitination by TRIM21 in macrophages, a process that is strongly increased upon interferon gamma stimulation, leds to the enhanced transcriptional activity of target cytokine genes (PubMed:17579016). Ubiquitination leads to its degradation by the proteasome (By similarity). {ECO:0000250|UniProtKB:Q02556, ECO:0000269|PubMed:17579016}.; PTM: Sumoylated with SUMO3. Desumoylated by SENP1. {ECO:0000250|UniProtKB:Q02556}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17579016}. Cytoplasm {ECO:0000250|UniProtKB:Q02556}. Note=In resting macrophages, localizes in the cytoplasm. Translocated in the nucleus upon IFN-gamma induction. {ECO:0000250|UniProtKB:Q02556}. SUBUNIT: Interacts with COPS2 (By similarity). Interacts (via C-terminus) with TRIM21 (via C-terminus). Interacts with the BATF-JUNB heterodimer. Interacts with BATF (via bZIP domain); the interaction is direct. {ECO:0000250, ECO:0000269|PubMed:17579016, ECO:0000269|PubMed:22992524}. TISSUE SPECIFICITY: Predominantly in lymphoid tissues. +P54987 IRG1_MOUSE Cis-aconitate decarboxylase (CAD) (EC 4.1.1.6) (Aconitate decarboxylase) (Aconitate decarboxylase 1) (Cis-aconitic acid decarboxylase) (Immune-responsive gene 1 protein) 488 53,758 Chain (1); Frameshift (1); Sequence conflict (12) FUNCTION: Involved in the inhibition of the inflammatory response. Acts as a negative regulator of the Toll-like receptors (TLRs)-mediated inflammatory innate response by stimulating the tumor necrosis factor alpha-induced protein TNFAIP3 expression via reactive oxygen species (ROS) in LPS-tolerized macrophages. Involved in antimicrobial response of innate immune cells; ACOD1-mediated itaconic acid production contributes to the antimicrobial activity of macrophages. Plays a role in the embryo implantation. {ECO:0000269|PubMed:14500577, ECO:0000269|PubMed:23609450, ECO:0000269|PubMed:23610393}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:19014335}. TISSUE SPECIFICITY: Expressed in LPS-tolerized macrophages (at protein level). Expressed in the luminal epithelial cells of pregnant uterus. Expressed in microglia and macrophage cells. {ECO:0000269|PubMed:14500577, ECO:0000269|PubMed:23609450, ECO:0000269|PubMed:23610393}. +Q9QY61 IRX4_MOUSE Iroquois-class homeodomain protein IRX-4 (Homeodomain protein IRXA3) (Iroquois homeobox protein 4) 515 54,701 Chain (1); Compositional bias (3); DNA binding (1); Sequence conflict (1) FUNCTION: Likely to be an important mediator of ventricular differentiation during cardiac development. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Interacts with the vitamin D receptor VDR but doesn't affect its transactivation activity. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the developing central nervous system, skin, and vibrissae, but predominantly expressed in the cardiac ventricles of the developing heart. Not expressed in the developing metanephric kidney or adult kidney. {ECO:0000269|PubMed:10625552, ECO:0000269|PubMed:10926765}. +Q9ER75 IRX6_MOUSE Iroquois-class homeodomain protein IRX-6 (Homeodomain protein IRXB3) (Iroquois homeobox protein 6) 438 47,352 Chain (1); Compositional bias (1); DNA binding (1); Sequence conflict (4) SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. +Q9D924 ISCA1_MOUSE Iron-sulfur cluster assembly 1 homolog, mitochondrial (HESB-like domain-containing protein 2) (Iron-sulfur assembly protein IscA) 129 14,188 Chain (1); Metal binding (3); Transit peptide (1) FUNCTION: Involved in the maturation of mitochondrial 4Fe-4S proteins functioning late in the iron-sulfur cluster assembly pathway. Probably involved in the binding of an intermediate of Fe/S cluster assembly. {ECO:0000250|UniProtKB:Q9BUE6}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9BUE6}. SUBUNIT: Interacts with CRY2, but not with CRY1 (in vitro). {ECO:0000250|UniProtKB:Q9BUE6}. +O35618 MDM4_MOUSE Protein Mdm4 (Double minute 4 protein) (Mdm2-like p53-binding protein) (Protein Mdmx) (p53-binding protein Mdm4) 489 54,963 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (1); Modified residue (3); Motif (1); Region (2); Sequence conflict (2); Zinc finger (2) FUNCTION: Inhibits p53/TP53- and TP73/p73-mediated cell cycle arrest and apoptosis by binding its transcriptional activation domain. Inhibits degradation of MDM2. Can reverse MDM2-targeted degradation of TP53 while maintaining suppression of TP53 transactivation and apoptotic functions. The short isoform is a more potent inhibitor of TP53 activity than the long isoform. PTM: Phosphorylated. Phosphorylation at Ser-367 promotes interaction with YWHAG and subsequent ubiquitination and degradation. Phosphorylation at Ser-341 also induces ubiquitination and degradation but to a lower extent (By similarity). {ECO:0000250}.; PTM: Ubiquitinated and degraded by MDM2. Deubiquitination by USP2 on the other hand stabilizes the MDM4 protein (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Found in a trimeric complex with USP2, MDM2 and MDM4. Interacts with USP2. Interacts (phosphorylated) with YWHAG; negatively regulates MDM4 activity toward TP53 (By similarity). Interacts with MDM2, TP53 and TP73. {ECO:0000250}. DOMAIN: Region I is sufficient for binding TP53 and inhibiting its G1 arrest and apoptosis functions. It also binds TP73. Region II contains most of a central acidic region and a putative C4-type zinc finger. The RING finger domain which coordinates two molecules of zinc mediates the heterooligomerization with MDM2. TISSUE SPECIFICITY: In all tissues tested. The short isoform is expressed in a variety of transformed cell lines. +Q9DCS3 MECR_MOUSE Enoyl-[acyl-carrier-protein] reductase, mitochondrial (EC 1.3.1.104) (2-enoyl thioester reductase) (Nuclear receptor-binding factor 1) (NRBF-1) 373 40,343 Active site (1); Binding site (2); Chain (1); Modified residue (7); Nucleotide binding (4); Sequence conflict (1); Transit peptide (1) FUNCTION: Catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis (fatty acid synthesis type II). Fatty acid chain elongation in mitochondria uses acyl carrier protein (ACP) as an acyl group carrier, but the enzyme accepts both ACP and CoA thioesters as substrates in vitro. Has a preference for short and medium chain substrates, including trans-2-hexenoyl-CoA (C6), trans-2-decenoyl-CoA (C10), and trans-2-hexadecenoyl-CoA (C16). {ECO:0000250|UniProtKB:Q9BV79}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9BV79}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9BV79}. +Q8VCD5 MED17_MOUSE Mediator of RNA polymerase II transcription subunit 17 (Cofactor required for Sp1 transcriptional activation subunit 6) (CRSP complex subunit 6) (Mediator complex subunit 17) (Thyroid hormone receptor-associated protein complex 80 kDa component) 649 72,462 Chain (1); Sequence conflict (1) FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Component of the Mediator complex, which is composed of MED1, MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L, MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23, MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8 subunits form a distinct module termed the CDK8 module. Mediator containing the CDK8 module is less active than Mediator lacking this module in supporting transcriptional activation. Individual preparations of the Mediator complex lacking one or more distinct subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and TRAP. Interacts with STAT2 (By similarity). Interacts with GATA1 and PPARG. {ECO:0000250, ECO:0000269|PubMed:12037571, ECO:0000269|PubMed:17132730}. +Q925J9 MED1_MOUSE Mediator of RNA polymerase II transcription subunit 1 (Mediator complex subunit 1) (Peroxisome proliferator-activated receptor-binding protein) (PBP) (PPAR-binding protein) (Thyroid hormone receptor-associated protein complex 220 kDa component) (Trap220) (Thyroid receptor-interacting protein 2) (TR-interacting protein 2) (TRIP-2) 1575 167,141 Alternative sequence (5); Chain (1); Compositional bias (2); Erroneous initiation (1); Helix (1); Modified residue (26); Motif (2); Natural variant (2); Region (10); Sequence conflict (9) FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. Essential for embryogenesis, including development of the central nervous system, heart, liver and placenta and for erythropoiesis. Also required for normal transcriptional control of thyroid-stimulating hormone beta (TSHB) in the pituitary. Acts as a coactivator for GATA1-mediated transcriptional activation during erythroid differentiation of K562 erythroleukemia cells (By similarity). {ECO:0000250|UniProtKB:Q15648, ECO:0000269|PubMed:10882104, ECO:0000269|PubMed:11867769, ECO:0000269|PubMed:12037571, ECO:0000269|PubMed:14500757, ECO:0000269|PubMed:14636573, ECO:0000269|PubMed:15150259, ECO:0000269|PubMed:15340084, ECO:0000269|PubMed:16137621, ECO:0000269|PubMed:17132730, ECO:0000269|PubMed:9325263}. PTM: Phosphorylated by MAPK1 or MAPK3 during G2/M phase which may enhance protein stability and promote entry into the nucleolus. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15150259}. Note=A subset of the protein may enter the nucleolus subsequent to phosphorylation by MAPK1 or MAPK3. {ECO:0000250}. SUBUNIT: Component of the Mediator complex, which is composed of MED1, MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L, MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23, MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8 subunits form a distinct module termed the CDK8 module. Mediator containing the CDK8 module is less active than Mediator lacking this module in supporting transcriptional activation. Individual preparations of the Mediator complex lacking one or more distinct subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and TRAP. This subunit specifically interacts with a number of nuclear receptors in a ligand-dependent fashion including AR, ESR1, ESR2, PPARA, PPARG, RORA, RXRA, RXRG, THRA, THRB and VDR. Interacts with CTNNB1, GABPA, GLI3, PPARGC1A and TP53. Interacts with GATA1 and YWHAH. Interacts with CLOCK; this interaction requires the presence of THRAP3. Interacts with CCAR1 (By similarity). Interacts with NR4A3 (PubMed:12709428). {ECO:0000250|UniProtKB:Q15648, ECO:0000269|PubMed:11266503, ECO:0000269|PubMed:11867769, ECO:0000269|PubMed:12709428, ECO:0000269|PubMed:14636573, ECO:0000269|PubMed:15340084, ECO:0000269|PubMed:15528208, ECO:0000269|PubMed:17132730, ECO:0000269|PubMed:24043798, ECO:0000269|PubMed:9325263}. TISSUE SPECIFICITY: Widely expressed in the adult, with high levels of expression in the liver, lung, intestinal mucosa, kidney cortex, thymic cortex, splenic follicle and seminiferous epithelium in testis. Also expressed in the adult heart, brain, spleen and skeletal muscle. {ECO:0000269|PubMed:14500757, ECO:0000269|PubMed:9325263}. +Q9R0X0 MED20_MOUSE Mediator of RNA polymerase II transcription subunit 20 (Mediator complex subunit 20) (TRF-proximal protein homolog) 212 23,192 Alternative sequence (4); Chain (1) FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Component of the Mediator complex, which is composed of MED1, MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L, MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23, MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8 subunits form a distinct module termed the CDK8 module. Mediator containing the CDK8 module is less active than Mediator lacking this module in supporting transcriptional activation. Individual preparations of the Mediator complex lacking one or more distinct subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and TRAP (By similarity). Interacts with PPARG. {ECO:0000250, ECO:0000269|PubMed:12037571}. +Q9CQ39 MED21_MOUSE Mediator of RNA polymerase II transcription subunit 21 (Mediator complex subunit 21) (RNA polymerase II holoenzyme component SRB7) (RNAPII complex component SRB7) 144 15,588 Chain (1); Sequence conflict (1) FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Component of the Mediator complex, which is composed of MED1, MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L, MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23, MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8 subunits form a distinct module termed the CDK8 module. Mediator containing the CDK8 module is less active than Mediator lacking this module in supporting transcriptional activation. Individual preparations of the Mediator complex lacking one or more distinct subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and TRAP. Interacts with THRA in a ligand-dependent fashion (By similarity). Interacts with PPARG. {ECO:0000250, ECO:0000269|PubMed:12037571}. TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver, lung, skeletal muscles, spleen and testis. {ECO:0000269|PubMed:10500093}. +Q62276 MED22_MOUSE Mediator of RNA polymerase II transcription subunit 22 (Mediator complex subunit 22) (Surfeit locus protein 5) (Surf-5) 200 22,282 Alternative sequence (2); Chain (1); Coiled coil (1) FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Component of the Mediator complex, which is composed of MED1, MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L, MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23, MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8 subunits form a distinct module termed the CDK8 module. Mediator containing the CDK8 module is less active than Mediator lacking this module in supporting transcriptional activation. Individual preparations of the Mediator complex lacking one or more distinct subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and TRAP (By similarity). {ECO:0000250}. +Q80YQ2 MED23_MOUSE Mediator of RNA polymerase II transcription subunit 23 (Cofactor required for Sp1 transcriptional activation subunit 3) (CRSP complex subunit 3) (Mediator complex subunit 23) (Protein sur-2 homolog) (mSur-2) 1367 156,087 Alternative sequence (3); Chain (1); Erroneous initiation (3); Erroneous translation (1); Sequence conflict (13) FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional pre-initiation complex with RNA polymerase II and the general transcription factors (By similarity). Also required for transcriptional activation subsequent to the assembly of the pre-initiation complex. Required for transcriptional activation by adenovirus E1A protein. Required for ELK1-dependent transcriptional activation in response to activated Ras signaling. {ECO:0000250, ECO:0000269|PubMed:11934987, ECO:0000269|PubMed:14759369, ECO:0000269|PubMed:15542641, ECO:0000269|PubMed:15749018}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Component of the Mediator complex, which is composed of MED1, MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L, MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23, MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8 subunits form a distinct module termed the CDK8 module. Mediator containing the CDK8 module is less active than Mediator lacking this module in supporting transcriptional activation. Individual preparations of the Mediator complex lacking one or more distinct subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and TRAP. Interacts with CEBPB (when not methylated), CTNNB1, and GLI3. Interacts with CDK8 and ELK1. {ECO:0000250|UniProtKB:Q9ULK4, ECO:0000269|PubMed:11934987, ECO:0000269|PubMed:15542641, ECO:0000269|PubMed:20111005}. +Q9D7W5 MED8_MOUSE Mediator of RNA polymerase II transcription subunit 8 (Activator-recruited cofactor 32 kDa component) (ARC32) (Mediator complex subunit 8) 268 29,199 Chain (1); Coiled coil (2); Modified residue (1); Region (1); Sequence conflict (1) Protein modification; protein ubiquitination. FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. May play a role as a target recruitment subunit in E3 ubiquitin-protein ligase complexes and thus in ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Component of the Mediator complex, which is composed of MED1, MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L, MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23, MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8 subunits form a distinct module termed the CDK8 module. Mediator containing the CDK8 module is less active than Mediator lacking this module in supporting transcriptional activation. Individual preparations of the Mediator complex lacking one or more distinct subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and TRAP. May be part of a multisubunit E3 ubiquitin-protein ligase complex with the Elongin BC complex (ELOB and ELOC), CUL2 and RBX1 (By similarity). {ECO:0000250}. +Q14BA6 MEDAG_MOUSE Mesenteric estrogen-dependent adipogenesis protein (Activated in W/Wv mouse stomach 3) (mAWMS3) (Mesenteric estrogen-dependent adipose 4) (MEDA-4) 303 34,364 Alternative sequence (1); Chain (1); Erroneous initiation (3); Frameshift (1); Sequence conflict (7) FUNCTION: Involved in processes that promote adipocyte differentiation, lipid accumulation, and glucose uptake in mature adipocytes. {ECO:0000269|PubMed:22510272}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22510272}. TISSUE SPECIFICITY: Highly expressed in white adipose tissue compared with other organs with higher expression in mature adipocyte fraction. Significant expression is also detected in the heart, brain, and pancreas. {ECO:0000269|PubMed:22510272}. +A2AG06 MEIOC_MOUSE Meiosis-specific coiled-coil domain-containing protein MEIOC (Meiosis-specific with coiled-coil domain protein) 965 108,830 Alternative sequence (1); Chain (1) FUNCTION: Is required for meiosis completion in both male and female germ cells. Confers stability to numerous meiotic mRNAs in gonads allowing proper initiation and progression into meiosis prophase I. The function may involve YTHDC2 and is independent of induction by retinoic acid (RA). Maintains an extended meiotic prophase I by properly promoting the transition from a mitotic to a meiotic cell cycle program by binding transcripts through its interaction with YTHDC2 that regulate the mitotic cell cycle (PubMed:28380054). {ECO:0000269|PubMed:26742488, ECO:0000269|PubMed:28380054}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:26742488, ECO:0000269|PubMed:28380054}. Nucleus {ECO:0000269|PubMed:28380054}. Note=at late pachytene a fraction is nuclear. {ECO:0000269|PubMed:28380054}. SUBUNIT: Interacts with YTHDC2; binds transcripts that regulate the mitotic cell cycle inhibiting progression into metaphase, thereby allowing meiotic prophase to proceed normally (PubMed:26742488, PubMed:28380054, PubMed:29033321). {ECO:0000269|PubMed:26742488, ECO:0000269|PubMed:28380054, ECO:0000269|PubMed:29033321}. TISSUE SPECIFICITY: Expressed specifically in fetal ovary and postnatal and adult testes (at protein level) (PubMed:26742488). In adult testis expressed in spermatocytes, beginning in preleptotene and extending through most stages of meiotic prophase I, including leptotene, zygotene, and pachytene (PubMed:28380054). {ECO:0000269|PubMed:26742488, ECO:0000269|PubMed:28380054}. +Q91V27 MELPH_MOUSE Melanophilin (Exophilin-3) (Leaden protein) (Slp homolog lacking C2 domains a) (SlaC2-a) (Synaptotagmin-like protein 2a) 590 65,052 Beta strand (2); Chain (1); Coiled coil (1); Domain (1); Helix (8); Sequence conflict (6); Turn (2); Zinc finger (1) FUNCTION: Rab effector protein involved in melanosome transport. Serves as link between melanosome-bound RAB27A and the motor protein MYO5A. {ECO:0000269|PubMed:11504925, ECO:0000269|PubMed:11887186}. SUBCELLULAR LOCATION: Melanosome. SUBUNIT: Binds RAB27A that has been activated by GTP-binding via its N-terminus. Binds MYO5A via its C-terminal coiled coil domain. {ECO:0000269|PubMed:18940604, ECO:0000269|PubMed:23798443}. TISSUE SPECIFICITY: Highly expressed in embryos at day 7; not detectable at day 11. Highly expressed in adult stomach; detected at lower levels in kidney, lung, skin and small intestine. Detected in melanocytes. {ECO:0000269|PubMed:11504925}. +Q9QXX0 JAG1_MOUSE Protein jagged-1 (Jagged1) (CD antigen CD339) 1218 134,164 Chain (1); Disulfide bond (51); Domain (17); Glycosylation (9); Region (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1068 1093 Helical. {ECO:0000255}. TOPO_DOM 34 1067 Extracellular. {ECO:0000255}.; TOPO_DOM 1094 1218 Cytoplasmic. {ECO:0000255}. FUNCTION: Ligand for multiple Notch receptors and involved in the mediation of Notch signaling. May be involved in cell-fate decisions during hematopoiesis. Seems to be involved in early and late stages of mammalian cardiovascular development. Inhibits myoblast differentiation (By similarity). May regulate fibroblast growth factor-induced angiogenesis. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Interacts with NOTCH1, NOTCH2 and NOTCH3. {ECO:0000269|PubMed:10551863}. DOMAIN: The DSL domain is indispensable and sufficient for binding to NOTCH2. TISSUE SPECIFICITY: Widely expressed in many tissues, with highest expression in brain, heart, muscle and thymus. {ECO:0000269|PubMed:10556292}. +Q69ZK6 JHD2C_MOUSE Probable JmjC domain-containing histone demethylation protein 2C (EC 1.14.11.-) (Jumonji domain-containing protein 1C) 2350 260,639 Chain (1); Cross-link (1); Domain (1); Erroneous initiation (2); Erroneous termination (1); Frameshift (1); Metal binding (3); Modified residue (15); Motif (1); Sequence caution (1); Sequence conflict (3); Zinc finger (1) FUNCTION: Probable histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. Demethylation of Lys residue generates formaldehyde and succinate. May be involved in hormone-dependent transcriptional activation, by participating in recruitment to androgen-receptor target genes (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. DOMAIN: Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs are known to mediate the association with nuclear receptors. {ECO:0000250}. +Q80UL9 JAML_MOUSE Junctional adhesion molecule-like (Dendritic cell-specific protein CREA7) (mCrea7) 379 42,533 Beta strand (20); Chain (1); Disulfide bond (2); Domain (2); Glycosylation (3); Helix (4); Modified residue (1); Mutagenesis (8); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (3) TRANSMEM 282 302 Helical. {ECO:0000255}. TOPO_DOM 21 281 Extracellular. {ECO:0000255}.; TOPO_DOM 303 379 Cytoplasmic. {ECO:0000255}. FUNCTION: Transmembrane protein of the plasma membrane of leukocytes that control their migration and activation through interaction with CXADR, a plasma membrane receptor found on adjacent epithelial and endothelial cells. The interaction between both receptors mediates the activation of gamma-delta T-cells, a subpopulation of T-cells residing in epithelia and involved in tissue homeostasis and repair. Upon epithelial CXADR-binding, JAML induces downstream cell signaling events in gamma-delta T-cells through PI3-kinase and MAP kinases. It results in proliferation and production of cytokines and growth factors by T-cells that in turn stimulate epithelial tissues repair. It also controls the transmigration of leukocytes within epithelial and endothelial tissues through adhesive interactions with epithelial and endothelial CXADR. {ECO:0000269|PubMed:20813954}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20813954}; Single-pass type I membrane protein {ECO:0000269|PubMed:20813954}. Cell junction {ECO:0000250|UniProtKB:Q86YT9}. Note=Localized at the plasma membrane and enriched in areas of cell-cell contacts. {ECO:0000250|UniProtKB:Q86YT9}. SUBUNIT: Homodimer; active form in leukocyte-endothelial cell adhesion. Interacts (homodimeric form) with CXADR. Interacts (via cytoplasmic domain) with the PI3 kinase; upon CXADR-binding. Interacts with ITGA4 and ITGB1; integrin alpha-4/beta-1 may regulate leukocyte to endothelial cells adhesion by controlling JAML homodimerization. {ECO:0000269|PubMed:20813954, ECO:0000269|PubMed:20813955}. DOMAIN: The Ig-like V-type domain 1 mediates interaction with CXADR (PubMed:20813954). The Ig-like V-type domain 2 may also play a role in the interaction (PubMed:20813955). {ECO:0000269|PubMed:20813954, ECO:0000269|PubMed:20813955}. TISSUE SPECIFICITY: Expressed by gamma-delta intraepithelial T cells (at protein level). {ECO:0000269|PubMed:20813954}. +Q9CR30 JOS2_MOUSE Josephin-2 (EC 3.4.19.12) (Josephin domain-containing protein 2) 188 20,776 Active site (2); Chain (1); Domain (1) FUNCTION: Cleaves 'Lys-63'-linked poly-ubiquitin chains, and with lesser efficiency 'Lys-48'-linked poly-ubiquitin chains (in vitro). May act as a deubiquitinating enzyme (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. +Q9ET80 JPH1_MOUSE Junctophilin-1 (JP-1) (Junctophilin type 1) 660 71,905 Chain (1); Compositional bias (3); Modified residue (8); Repeat (7); Topological domain (1); Transmembrane (1) TRANSMEM 639 659 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 1 638 Cytoplasmic. {ECO:0000255}. FUNCTION: Junctophilins contribute to the formation of junctional membrane complexes (JMCs) which link the plasma membrane with the endoplasmic or sarcoplasmic reticulum in excitable cells. Provides a structural foundation for functional cross-talk between the cell surface and intracellular calcium release channels. JPH1 contributes to the construction of the skeletal muscle triad by linking the t-tubule (transverse-tubule) and SR (sarcoplasmic reticulum) membranes. {ECO:0000269|PubMed:11535622, ECO:0000269|PubMed:12135771, ECO:0000269|PubMed:12729900}. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Single-pass type IV membrane protein. Sarcoplasmic reticulum membrane; Single-pass type IV membrane protein. Note=Predominantly on the plasma membrane. The transmembrane domain is anchored in endoplasmic/sarcoplasmic reticulum membrane, while the N-terminal part associates with the plasma membrane. In skeletal muscle cells, it is predominantly localized at the junction of the A and I bands. DOMAIN: The MORN (membrane occupation and recognition nexus) repeats contribute to the plasma membrane binding, possibly by interacting with phospholipids. {ECO:0000250}. TISSUE SPECIFICITY: Specifically expressed in skeletal muscle. Weakly expressed in embryos and neonates. Abundant in young adult muscles. {ECO:0000269|PubMed:10949023, ECO:0000269|PubMed:11535622}. +P0C872 JMJD7_MOUSE Bifunctional peptidase and (3S)-lysyl hydroxylase Jmjd7 (EC 1.14.11.-) (EC 3.4.-.-) (JmjC domain-containing protein 7) (Jumonji domain-containing protein 7) (L-lysine (3S)-hydroxylase Jmjd7) 316 35,917 Beta strand (20); Chain (1); Disulfide bond (1); Domain (1); Helix (11); Metal binding (3); Turn (3) FUNCTION: Bifunctional enzyme that acts both as an endopeptidase and 2-oxoglutarate-dependent monoxygenase (PubMed:28847961) (By similarity). Endopeptidase that cleaves histones N-terminal tails at the carboxyl side of methylated arginine or lysine residues, to generate 'tailless nucleosomes', which may trigger transcription elongation (PubMed:28847961). Preferentially recognizes and cleaves monomethylated and dimethylated arginine residues of histones H2, H3 and H4. After initial cleavage, continues to digest histones tails via its aminopeptidase activity (PubMed:28847961). Additionally, may play a role in protein biosynthesis by modifying the translation machinery. Acts as Fe(2+) and 2-oxoglutarate-dependent monoxygenase, catalyzing (S)-stereospecific hydroxylation at C-3 of 'Lys-22' of DRG1 and 'Lys-21' of DRG2 translation factors (TRAFAC), promoting their interaction with ribonucleic acids (RNA) (By similarity). {ECO:0000250|UniProtKB:P0C870, ECO:0000269|PubMed:28847961}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P0C870}. Cytoplasm {ECO:0000250|UniProtKB:P0C870}. SUBUNIT: Homodimer; disulfide-linked. Interacts with DRG1 and DRG2. {ECO:0000250|UniProtKB:P0C870}. +Q9ET77 JPH3_MOUSE Junctophilin-3 (JP-3) (Junctophilin type 3) 744 81,229 Chain (1); Compositional bias (2); Erroneous termination (1); Modified residue (8); Repeat (8); Topological domain (1); Transmembrane (1) TRANSMEM 724 744 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 1 723 Cytoplasmic. {ECO:0000255}. FUNCTION: Junctophilins contribute to the formation of junctional membrane complexes (JMCs) which link the plasma membrane with the endoplasmic or sarcoplasmic reticulum in excitable cells. Provides a structural foundation for functional cross-talk between the cell surface and intracellular calcium release channels. JPH3 is brain-specific and appears to have an active role in certain neurons involved in motor coordination and memory. {ECO:0000269|PubMed:11906164, ECO:0000269|PubMed:16809425}. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Single-pass type IV membrane protein. Note=Localized predominantly on the plasma membrane. The transmembrane domain is anchored in endoplasmic reticulum membrane, while the N-terminal part associates with the plasma membrane. DOMAIN: The MORN (membrane occupation and recognition nexus) repeats contribute to the plasma membrane binding, possibly by interacting with phospholipids. {ECO:0000250}. TISSUE SPECIFICITY: Specifically expressed in brain. Highest levels in the olfactory tubercle, caudate putamen, nucleus accumbens, hippocampal formation, piriform cortex and cerebellar cortex. Expressed in disctete neurons sites. In hippocampal formation, expressed in dendrites of hippocampal pyramidal and denate granule cells. In cerebellum, it is highly expressed in Purkinge cells, while it is weakly expressed in granular cells. {ECO:0000269|PubMed:11906164, ECO:0000269|PubMed:16809425}. +P23299 KCNE1_MOUSE Potassium voltage-gated channel subfamily E member 1 (Delayed rectifier potassium channel subunit IsK) (mISK) (IKs producing slow voltage-gated potassium channel subunit beta Mink) (Minimal potassium channel) 129 14,578 Chain (1); Glycosylation (3); Modified residue (1); Topological domain (1); Transmembrane (1) TRANSMEM 44 66 Helical. {ECO:0000255}. TOPO_DOM 67 129 Cytoplasmic. {ECO:0000255}. FUNCTION: Ancillary protein that assembles as a beta subunit with a voltage-gated potassium channel complex of pore-forming alpha subunits. Modulates the gating kinetics and enhances stability of the channel complex. Assembled with KCNB1 modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1. Assembled with KCNQ1/KVLQT1 is proposed to form the slowly activating delayed rectifier cardiac potassium (IKs) channel. The outward current reaches its steady state only after 50 seconds. Assembled with KCNH2/HERG may modulate the rapidly activating component of the delayed rectifying potassium current in heart (IKr). {ECO:0000250|UniProtKB:P15382, ECO:0000250|UniProtKB:P15383}. PTM: Phosphorylation inhibits the potassium current. {ECO:0000250}.; PTM: N-glycosylation at Asn-26 occurs post-translationally, and requires prior cotranslational glycosylation at Asn-5. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P15382, ECO:0000250|UniProtKB:P15383}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P15382}. Apical cell membrane {ECO:0000250|UniProtKB:P15383}. Membrane raft {ECO:0000250|UniProtKB:P15382}. Note=Colocalizes with KCNB1 at the plasma membrane (By similarity). Targets to the membrane raft when associated with KCNQ1 (By similarity). {ECO:0000250|UniProtKB:P15382, ECO:0000250|UniProtKB:P15383}. SUBUNIT: Interacts with KCNB1. Interacts with KCNC2 (By similarity). Associates with KCNH2/HERG. Interacts with KCNQ1; targets the complex KCNQ1-KCNE1 to the membrane raft (By similarity) (PubMed:8900282). {ECO:0000250|UniProtKB:P15382, ECO:0000250|UniProtKB:P15383, ECO:0000269|PubMed:8900282}. TISSUE SPECIFICITY: Restrictively localized in the apical membrane portion of epithelial cells. +Q61762 KCNA5_MOUSE Potassium voltage-gated channel subfamily A member 5 (Voltage-gated potassium channel subunit Kv1.5) (KV1-5) 602 66,580 Alternative sequence (2); Chain (1); Compositional bias (1); Cross-link (2); Glycosylation (1); Intramembrane (2); Lipidation (1); Modified residue (4); Motif (2); Region (1); Sequence conflict (13); Topological domain (8); Transmembrane (6) INTRAMEM 457 468 Helical; Name=Pore helix. {ECO:0000250|UniProtKB:P63142}.; INTRAMEM 469 476 {ECO:0000250|UniProtKB:P63142}. TRANSMEM 239 260 Helical; Name=Segment S1. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 315 336 Helical; Name=Segment S2. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 348 368 Helical; Name=Segment S3. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 385 405 Helical; Voltage-sensor; Name=Segment S4. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 421 442 Helical; Name=Segment S5. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 484 512 Helical; Name=Segment S6. {ECO:0000250|UniProtKB:P63142}. TOPO_DOM 1 238 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 261 314 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 337 347 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 369 384 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 406 420 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 443 456 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 477 483 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 513 602 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}. FUNCTION: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes. Forms tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane (PubMed:8226976, PubMed:11349004). Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNA1, KCNA2, KCNA4, KCNA5, and possibly other family members as well; channel properties depend on the type of alpha subunits that are part of the channel (By similarity). Channel properties are modulated by cytoplasmic beta subunits that regulate the subcellular location of the alpha subunits and promote rapid inactivation (By similarity). Homotetrameric channels display rapid activation and slow inactivation (PubMed:8226976, PubMed:11349004). May play a role in regulating the secretion of insulin in normal pancreatic islets (By similarity). {ECO:0000250|UniProtKB:P22460, ECO:0000269|PubMed:11349004, ECO:0000269|PubMed:8226976}. PTM: Sumoylated on Lys-212, and Lys-525, preferentially with SUMO3. Sumoylation regulates the voltage sensitivity of the channel (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11349004, ECO:0000269|PubMed:8226976}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Homotetramer and heterotetramer of potassium channel proteins. Interacts with DLG1, which enhances channel currents. Forms a ternary complex with DLG1 and CAV3 (By similarity). Interacts with KCNAB1 (By similarity). Interacts with UBE2I (By similarity). {ECO:0000250|UniProtKB:P19024, ECO:0000250|UniProtKB:P22460}. DOMAIN: The amino terminus may be important in determining the rate of inactivation of the channel while the C-terminal PDZ-binding motif may play a role in modulation of channel activity and/or targeting of the channel to specific subcellular compartments. {ECO:0000250}.; DOMAIN: The transmembrane segment S4 functions as voltage-sensor and is characterized by a series of positively charged amino acids at every third position. Channel opening and closing is effected by a conformation change that affects the position and orientation of the voltage-sensor paddle formed by S3 and S4 within the membrane. A transmembrane electric field that is positive inside would push the positively charged S4 segment outwards, thereby opening the pore, while a field that is negative inside would pull the S4 segment inwards and close the pore. Changes in the position and orientation of S4 are then transmitted to the activation gate formed by the inner helix bundle via the S4-S5 linker region. {ECO:0000250|UniProtKB:P63142}. TISSUE SPECIFICITY: Highly expressed in heart and moderately in brain. Low levels in thymus, skeletal muscle and spleen. Not expressed in liver, lung or kidney. +Q9WTW2 KCNE3_MOUSE Potassium voltage-gated channel subfamily E member 3 (MinK-related peptide 2) (Minimum potassium ion channel-related peptide 2) (Potassium channel subunit beta MiRP2) 103 11,720 Chain (1); Glycosylation (3); Topological domain (1); Transmembrane (1) TRANSMEM 58 78 Helical. {ECO:0000255}. TOPO_DOM 79 103 Cytoplasmic. {ECO:0000255}. FUNCTION: Ancillary protein that assembles as a beta subunit with a voltage-gated potassium channel complex of pore-forming alpha subunits. Modulates the gating kinetics and enhances stability of the channel complex. Assembled with KCNB1 modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1. Associated with KCNC4/Kv3.4 is proposed to form the subthreshold voltage-gated potassium channel in skeletal muscle and to establish the resting membrane potential (RMP) in muscle cells. Associated with KCNQ1/KCLQT1 may form the intestinal cAMP-stimulated potassium channel involved in chloride secretion that produces a current with nearly instantaneous activation with a linear current-voltage relationship. {ECO:0000250|UniProtKB:Q9JJV7, ECO:0000250|UniProtKB:Q9Y6H6}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9JJV7, ECO:0000250|UniProtKB:Q9Y6H6}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9Y6H6}. Cytoplasm {ECO:0000250|UniProtKB:Q9JJV7, ECO:0000250|UniProtKB:Q9Y6H6}. Perikaryon {ECO:0000250|UniProtKB:Q9Y6H6}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9Y6H6}. Membrane raft {ECO:0000250|UniProtKB:Q9Y6H6}. Note=Colocalizes with KCNB1 at high-density somatodendritic clusters on the surface of hippocampal neurons. {ECO:0000250|UniProtKB:Q9Y6H6}. SUBUNIT: Interacts with KCNB1. Interacts with KCNC2 (By similarity). Associates with KCNC4/Kv3.4 (By similarity). Interacts with KCNQ1; produces a current with nearly instantaneous activation with a linear current-voltage relationship and alters membrane raft localization (By similarity). {ECO:0000250|UniProtKB:Q9JJV7, ECO:0000250|UniProtKB:Q9Y6H6}. +Q03717 KCNB1_MOUSE Potassium voltage-gated channel subfamily B member 1 (Voltage-gated potassium channel subunit Kv2.1) (mShab) 857 95,591 Chain (1); Compositional bias (1); Cross-link (1); Intramembrane (2); Modified residue (19); Motif (1); Region (2); Sequence conflict (2); Topological domain (8); Transmembrane (6) INTRAMEM 365 376 Helical; Name=Pore helix. {ECO:0000250|UniProtKB:P63142}.; INTRAMEM 377 384 {ECO:0000250|UniProtKB:P63142}. TRANSMEM 187 208 Helical; Name=Segment S1. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 229 250 Helical; Name=Segment S2. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 260 280 Helical; Name=Segment S3. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 295 316 Helical; Voltage-sensor; Name=Segment S4. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 331 351 Helical; Name=Segment S5. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 392 420 Helical; Name=Segment S6. {ECO:0000250|UniProtKB:P63142}. TOPO_DOM 1 186 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 209 228 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 251 259 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 281 294 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 317 330 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 352 364 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 385 391 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 421 857 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}. FUNCTION: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain, but also in the pancreas and cardiovascular system. Contributes to the regulation of the action potential (AP) repolarization, duration and frequency of repetitive AP firing in neurons, muscle cells and endocrine cells and plays a role in homeostatic attenuation of electrical excitability throughout the brain (PubMed:14684365, PubMed:19383458, PubMed:24494598). Plays also a role in the regulation of exocytosis independently of its electrical function (By similarity). Forms tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane. Homotetrameric channels mediate a delayed-rectifier voltage-dependent outward potassium current that display rapid activation and slow inactivation in response to membrane depolarization (PubMed:22056818). Can form functional homotetrameric and heterotetrameric channels that contain variable proportions of KCNB2; channel properties depend on the type of alpha subunits that are part of the channel (By similarity). Can also form functional heterotetrameric channels with other alpha subunits that are non-conducting when expressed alone, such as KCNF1, KCNG1, KCNG3, KCNG4, KCNH1, KCNH2, KCNS1, KCNS2, KCNS3 and KCNV1, creating a functionally diverse range of channel complexes (By similarity). Heterotetrameric channel activity formed with KCNS3 show increased current amplitude with the threshold for action potential activation shifted towards more negative values in hypoxic-treated pulmonary artery smooth muscle cells (By similarity). Channel properties are also modulated by cytoplasmic ancillary beta subunits, such as AMIGO1, KCNE1, KCNE2 and KCNE3, slowing activation and inactivation rate of the delayed rectifier potassium channels (PubMed:22056818). In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes, making it difficult to assign currents observed in intact tissues to any particular potassium channel family member. Major contributor to the delayed-rectifier voltage-gated potassium current in neurons of the central nervous system, sympathetic ganglion neurons, neuroendocrine cells, pancreatic beta cells, cardiomyocytes and smooth muscle (PubMed:10506487, PubMed:12270920, PubMed:17767909, PubMed:23161216, PubMed:24494598). Mediates the major part of the somatodendritic delayed-rectifier potassium current in hippocampal and cortical pyramidal neurons and sympathetic superior cervical ganglion (CGC) neurons that acts to slow down periods of firing, especially during high frequency stimulation (By similarity). Plays a role in the induction of long-term potentiation (LTP) of neuron excitability in the CA3 layer of the hippocampus (PubMed:24494598). Contributes to the regulation of the glucose-induced amplitude and duration of action potentials in pancreatic beta-cells, hence limiting calcium influx and insulin secretion (PubMed:12270920, PubMed:17767909, PubMed:19383458, PubMed:23161216). Plays a role in the regulation of resting membrane potential and contraction in hypoxia-treated pulmonary artery smooth muscle cells (By similarity). May contribute to the regulation of the duration of both the action potential of cardiomyocytes and the heart ventricular repolarization QT interval (PubMed:10506487, PubMed:14684365). Contributes to the pronounced pro-apoptotic potassium current surge during neuronal apoptotic cell death in response to oxidative injury (By similarity). May confer neuroprotection in response to hypoxia/ischemic insults by suppressing pyramidal neurons hyperexcitability in hippocampal and cortical regions (By similarity). Promotes trafficking of KCNG3, KCNH1 and KCNH2 to the cell surface membrane, presumably by forming heterotetrameric channels with these subunits (By similarity). Plays a role in the calcium-dependent recruitment and release of fusion-competent vesicles from the soma of neurons, neuroendocrine and glucose-induced pancreatic beta cells by binding key components of the fusion machinery in a pore-independent manner (By similarity). {ECO:0000250|UniProtKB:P15387, ECO:0000250|UniProtKB:Q14721, ECO:0000269|PubMed:10506487, ECO:0000269|PubMed:12270920, ECO:0000269|PubMed:14684365, ECO:0000269|PubMed:17767909, ECO:0000269|PubMed:19383458, ECO:0000269|PubMed:22056818, ECO:0000269|PubMed:23161216, ECO:0000269|PubMed:24494598}. PTM: Phosphorylated. Differential C-terminal phosphorylation on a subset of serines allows graded activity-dependent regulation of channel gating in hippocampal neurons. Ser-607 and Tyr-128 are significant sites of voltage-gated regulation through phosphorylation/dephosphorylation activities. Tyr-128 can be phosphorylated by Src and dephosphorylated by cytoplasmic form of the phosphatase PTPRE. CDK5-induced Ser-607 phosphorylation increases in response to acute blockade of neuronal activity. Phosphorylated on Tyr-128 by Src and on Ser-804 by MAPK14/P38MAPK; phosphorylations are necessary and sufficient for an increase in plasma membrane insertion, apoptotic potassium current surge and completion of the neuronal cell death program. Phosphorylated on Ser-520, Ser-655, Ser-607 and Ser-804 by CDK5; phosphorylation is necessary for KCNB1 channel clustering formation. The Ser-607 phosphorylation state differs between KCNB1-containing clusters on the proximal and distal portions of the axon initial segment (AIS). Highly phosphorylated on serine residues in the C-terminal cytoplasmic tail in resting neurons. Phosphorylated in pancreatic beta cells in response to incretin hormones stimulation in a PKA- and RPS6KA5/MSK1-dependent signaling pathway, promoting beta cell survival. Phosphorylation on Ser-567 is reduced during postnatal development with low levels at P2 and P5; levels then increase to reach adult levels by P14. Phosphorylation on Ser-457, Ser-541, Ser-567, Ser-607, Ser-655 and Ser-719 as well as the N-terminal Ser-15 are sensitive to calcineurin-mediated dephosphorylation contributing to the modulation of the voltage-dependent gating properties. Dephosphorylation by phosphatase PTPRE confers neuroprotection by its inhibitory influence on the neuronal apoptotic potassium current surge in a Zn(2+)-dependent manner. Dephosphorylated at Ser-607 by protein phosphatase PPP1CA. Hypoxia-, seizure- or glutamate-induced neuronal activities promote calcium/calcineurin-dependent dephosphorylation resulting in a loss of KCNB1-containing clustering and enhanced channel activity. In response to brain ischemia, Ser-567 and Ser-607 are strongly dephosphorylated while Ser-457 and Ser-719 are less dephosphorylated. In response to brain seizures, phosphorylation levels on Ser-567 and Ser-607 are greatly reduced (By similarity). Phosphorylated/dephosphorylated by Src or FYN tyrosine-protein kinases and tyrosine phosphatase PTPRE in primary Schwann cells and sciatic nerve tissue (PubMed:10921884). {ECO:0000250|UniProtKB:P15387, ECO:0000269|PubMed:10921884}.; PTM: Acetylated. Acetylation occurs in pancreatic beta cells in response to stimulation by incretin hormones in a histone acetyltransferase (HAT)/histone deacetylase (HDAC)-dependent signaling pathway, promoting beta cell survival. {ECO:0000250|UniProtKB:P15387}.; PTM: Sumoylated on Lys-474, preferentially with SUMO1; sumoylation induces a positive shift in the voltage-dependence of activation and inhibits channel activity. Sumoylation increases the frequency of repetitive action potential firing at the cell surface of hippocampal neurons and decreases its frequency in pancreatic beta cells. Desumoylated by SENP1. {ECO:0000250|UniProtKB:P15387, ECO:0000250|UniProtKB:Q14721}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10506487, ECO:0000269|PubMed:12270920, ECO:0000269|PubMed:14684365, ECO:0000269|PubMed:17767909, ECO:0000269|PubMed:19357235, ECO:0000269|PubMed:22056818, ECO:0000269|PubMed:24477962}. Perikaryon {ECO:0000269|PubMed:22056818, ECO:0000269|PubMed:24477962}. Cell projection, axon {ECO:0000269|PubMed:24477962}. Cell projection, dendrite {ECO:0000269|PubMed:22056818, ECO:0000269|PubMed:24477962}. Membrane; Multi-pass membrane protein. Cell junction, synapse, postsynaptic cell membrane {ECO:0000250|UniProtKB:P15387}. Cell junction, synapse {ECO:0000250|UniProtKB:P15387}. Cell junction, synapse, synaptosome {ECO:0000250|UniProtKB:P15387}. Lateral cell membrane {ECO:0000250|UniProtKB:P15387}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P15387}. Note=Localizes to high-density somatodendritic clusters and non-clustered sites on the surface of neocortical and hippocampal pyramidal neurons in a cortical actin cytoskeleton-dependent manner (PubMed:24477962). Localizes also to high-density clusters in the axon initial segment (AIS), at ankyrin-G-deficient sites, on the surface of neocortical and hippocampal pyramidal neurons (PubMed:24477962). KCNB1-containing AIS clusters localize either in close apposition to smooth endoplasmic reticulum cisternal organelles or with GABA-A receptor-containing synapses of hippocampal and cortical pyramidal neurons, respectively (PubMed:24477962). Localizes to high-density clusters on the cell surface of atrial and ventricular myocytes and at the lateral plasma membrane in epithelial cells. Localizes both to the axial and transverse tubules (T tubule) and sarcolemma in ventricular myocytes. Associated with lipid raft domains. In cortical neurons, apoptotic injuries induce de novo plasma membrane insertion in a SNARE-dependent manner causing an apoptotic potassium current surge (By similarity). {ECO:0000250|UniProtKB:P15387, ECO:0000250|UniProtKB:Q14721, ECO:0000269|PubMed:19357235, ECO:0000269|PubMed:22056818, ECO:0000269|PubMed:24477962}. SUBUNIT: Homotetramer or heterotetramer with KCNB2. Heterotetramer with non-conducting channel-forming alpha subunits such as KCNF1, KCNG1, KCNG3, KCNG4, KCNH1, KCNH2, KCNS1, KCNS2, KCNS3 and KCNV1 (By similarity). Channel activity is regulated by association with ancillary beta subunits such as AMIGO1, KCNE1, KCNE2 and KCNE3 (PubMed:22056818). Self-associates (via N-terminus and C-terminus); self-association is required to regulate trafficking, gating and C-terminal phosphorylation-dependent modulation of the channel. Interacts (via C-terminus) with STX1A (via C-terminus); this decreases the rate of channel activation and increases the rate of channel inactivation in pancreatic beta cells, induces also neuronal apoptosis in response to oxidative injury as well as pore-independent enhancement of exocytosis in neuroendocrine cells, chromaffin cells, pancreatic beta cells and from the soma of dorsal root ganglia (DRG) neurons. Interacts (via N-terminus) with SNAP25; this decreases the rate of channel inactivation in pancreatic beta cells and also increases interaction during neuronal apoptosis in a N-methyl-D-aspartate receptor (NMDAR)-dependent manner. Interacts (via N-terminus and C-terminus) with VAMP2 (via N-terminus); stimulates channel inactivation rate. Interacts with CREB1; this promotes channel acetylation in response to stimulation by incretin hormones. Interacts (via N-terminus and C-terminus) with MYL12B. Interacts (via N-terminus) with PIAS3; this increases the number of functional channels at the cell surface. Interacts with SUMO1 (By similarity). Interacts (via phosphorylated form) with PTPRE isoform 2; this reduces phosphorylation and channel activity in heterologous cells (PubMed:10921884). {ECO:0000250|UniProtKB:P15387, ECO:0000250|UniProtKB:Q14721, ECO:0000269|PubMed:10921884, ECO:0000269|PubMed:22056818}. DOMAIN: The transmembrane segment S4 functions as voltage-sensor and is characterized by a series of positively charged amino acids at every third position. Channel opening and closing is effected by a conformation change that affects the position and orientation of the voltage-sensor paddle formed by S3 and S4 within the membrane. A transmembrane electric field that is positive inside would push the positively charged S4 segment outwards, thereby opening the pore, while a field that is negative inside would pull the S4 segment inwards and close the pore. Changes in the position and orientation of S4 are then transmitted to the activation gate formed by the inner helix bundle via the S4-S5 linker region. {ECO:0000250|UniProtKB:P63142}.; DOMAIN: The N-terminal and C-terminal cytoplasmic regions mediate homooligomerization; self-association is required to regulate trafficking, gating and C-terminal phosphorylation-dependent modulation of the channel (By similarity). The N-terminal cytoplasmic region is important for interaction with other channel-forming alpha subunits and with ancillary beta subunits (PubMed:22056818). The C-terminus is necessary and sufficient for the restricted localization to, and clustering within, both in soma and proximal portions of dendrite of neurons and in lateral membrane of non-neuronal polarized cells. The C-terminus is both necessary and sufficient as a mediator of cholinergic and calcium-stimulated modulation of channel cell membrane clustering localization and activity in hippocampal neurons (By similarity). {ECO:0000250|UniProtKB:P15387, ECO:0000250|UniProtKB:Q14721, ECO:0000269|PubMed:22056818}. TISSUE SPECIFICITY: Expressed in the brain (PubMed:17767909, PubMed:22056818). Expressed in the heart (PubMed:14684365). Expressed in pyramidal neurons and interneurons of the hippocampus (PubMed:22056818, PubMed:24494598). Expressed in neocortical pyramidal neurons (PubMed:22056818, PubMed:24477962). Expressed in dorsal root ganglia (DRG) neurons (PubMed:19357235). Expressed in pancreatic beta cells (PubMed:12270920, PubMed:17767909). Expressed in Schwann cells (PubMed:10921884). Expressed in ventricular myocytes (at protein level) (PubMed:14684365, PubMed:10506487). {ECO:0000269|PubMed:10506487, ECO:0000269|PubMed:10921884, ECO:0000269|PubMed:12270920, ECO:0000269|PubMed:14684365, ECO:0000269|PubMed:17767909, ECO:0000269|PubMed:19357235, ECO:0000269|PubMed:22056818, ECO:0000269|PubMed:24477962, ECO:0000269|PubMed:24494598}. +P48543 KCNJ9_MOUSE G protein-activated inward rectifier potassium channel 3 (GIRK-3) (Inward rectifier K(+) channel Kir3.3) (Potassium channel, inwardly rectifying subfamily J member 9) 393 43,974 Chain (1); Intramembrane (2); Motif (2); Sequence conflict (3); Site (1); Topological domain (4); Transmembrane (2) INTRAMEM 107 118 Helical; Pore-forming; Name=H5. {ECO:0000250}.; INTRAMEM 119 125 Pore-forming. {ECO:0000250}. TRANSMEM 58 82 Helical; Name=M1. {ECO:0000250}.; TRANSMEM 135 156 Helical; Name=M2. {ECO:0000250}. TOPO_DOM 1 57 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 83 106 Extracellular. {ECO:0000250}.; TOPO_DOM 126 134 Extracellular. {ECO:0000250}.; TOPO_DOM 157 393 Cytoplasmic. {ECO:0000250}. FUNCTION: This receptor is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SUBUNIT: Associates with GIRK1 to form a G-protein-activated heteromultimer pore-forming unit. The resulting inward current is much larger. When alone, fail to give functional channels in Xenopus oocytes. Interacts (via PDZ-binding motif) with SNX27 (via PDZ domain); the interaction is required when endocytosed to prevent degradation in lysosomes and promote recycling to the plasma membrane. DOMAIN: The PDZ-binding motif specifically binds the PDZ domain of SNX27: the specificity for SNX27 is provided by the 2 residues located upstream (Glu-388 and Ser-389) of the PDZ-binding motif. {ECO:0000250}. TISSUE SPECIFICITY: Expressed mainly in the brain, some expression in the skeletal muscle. +P15388 KCNC1_MOUSE Potassium voltage-gated channel subfamily C member 1 (NGK2) (Voltage-gated potassium channel subunit Kv3.1) (Voltage-gated potassium channel subunit Kv4) 511 57,928 Alternative sequence (1); Chain (1); Glycosylation (2); Modified residue (7); Motif (1); Topological domain (4); Transmembrane (6) TRANSMEM 191 209 Helical; Name=Segment S1. {ECO:0000255}.; TRANSMEM 248 267 Helical; Name=Segment S2. {ECO:0000255}.; TRANSMEM 277 295 Helical; Name=Segment S3. {ECO:0000255}.; TRANSMEM 309 331 Helical; Voltage-sensor; Name=Segment S4. {ECO:0000255}.; TRANSMEM 345 366 Helical; Name=Segment S5. {ECO:0000255}.; TRANSMEM 415 436 Helical; Name=Segment S6. {ECO:0000255}. TOPO_DOM 1 190 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 268 276 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 332 344 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 437 511 Cytoplasmic. {ECO:0000255}. FUNCTION: Voltage-gated potassium channel that plays an important role in the rapid repolarization of fast-firing brain neurons. The channel opens in response to the voltage difference across the membrane, forming a potassium-selective channel through which potassium ions pass in accordance with their electrochemical gradient (PubMed:2599109, PubMed:1400413). Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNC2, and possibly other family members as well. Contributes to fire sustained trains of very brief action potentials at high frequency in pallidal neurons. {ECO:0000250|UniProtKB:P25122, ECO:0000269|PubMed:1400413, ECO:0000269|PubMed:2599109}. PTM: N-glycosylated; contains sialylated glycans. {ECO:0000250|UniProtKB:P25122}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1400413, ECO:0000269|PubMed:2599109}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Heteromultimer with KCNG3, KCNG4 and KCNV2 (By similarity). Heteromultimer with KCNC2 (By similarity). Heterotetramer with KCNC3 (By similarity). Interacts with the ancillary subunits KCNE1 and KCNE2; the interaction modulates channel activity (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P48547}. DOMAIN: The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position. {ECO:0000305}.; DOMAIN: The tail may be important in modulation of channel activity and/or targeting of the channel to specific subcellular compartments. {ECO:0000305}. TISSUE SPECIFICITY: Detected in cerebellum (PubMed:11517255, PubMed:15217387). Detected in brain (at protein level) (PubMed:9037088). Detected in brain (PubMed:9037088). {ECO:0000269|PubMed:11517255, ECO:0000269|PubMed:15217387, ECO:0000269|PubMed:9037088}. +P97438 KCNK2_MOUSE Potassium channel subfamily K member 2 (Outward rectifying potassium channel protein TREK-1) (TREK-1 K(+) channel subunit) (Two pore potassium channel TPKC1) 426 46,844 Alternative sequence (1); Beta strand (4); Chain (1); Disulfide bond (1); Glycosylation (2); Helix (9); Intramembrane (2); Modified residue (1); Mutagenesis (1); Region (2); Sequence conflict (1); Topological domain (3); Transmembrane (4); Turn (3) INTRAMEM 144 170 Pore-forming; Name=Pore-forming 1. {ECO:0000255}.; INTRAMEM 253 283 Pore-forming; Name=Pore-forming 2. {ECO:0000255}. TRANSMEM 62 82 Helical. {ECO:0000255}.; TRANSMEM 172 192 Helical. {ECO:0000255}.; TRANSMEM 223 243 Helical. {ECO:0000255}.; TRANSMEM 288 308 Helical. {ECO:0000255}. TOPO_DOM 1 61 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 193 222 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 309 426 Cytoplasmic. {ECO:0000255}. FUNCTION: Ion channel that contributes to passive transmembrane potassium transport. Reversibly converts between a voltage-insensitive potassium leak channel and a voltage-dependent outward rectifying potassium channel in a phosphorylation-dependent manner. In astrocytes, forms mostly heterodimeric potassium channels with KCNK1, with only a minor proportion of functional channels containing homodimeric KCNK2 (PubMed:24496152). In astrocytes, the heterodimer formed by KCNK1 and KCNK2 is required for rapid glutamate release in response to activation of G-protein coupled receptors, such as F2R and CNR1 (PubMed:24496152). {ECO:0000269|PubMed:10321245, ECO:0000269|PubMed:16636285, ECO:0000269|PubMed:24496152, ECO:0000269|PubMed:9003761}. PTM: Phosphorylation at Ser-348 controls the reversible conversion from a leak channel to a voltage-dependent channel. {ECO:0000250}. SUBCELLULAR LOCATION: Isoform 1: Cell membrane {ECO:0000269|PubMed:10321245, ECO:0000269|PubMed:16636285, ECO:0000269|PubMed:22354168, ECO:0000269|PubMed:24496152}; Multi-pass membrane protein {ECO:0000305}. Note=Location at the cell membrane requires interaction with KCNK1. Is not detected at the cell membrane when KCNK1 is absent. {ECO:0000269|PubMed:24496152}.; SUBCELLULAR LOCATION: Isoform 2: Cell membrane {ECO:0000269|PubMed:9003761}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Homodimer; disulfide-linked (PubMed:24496152). Heterodimer with KCNK1; disulfide-linked (PubMed:24496152). Interacts with BVES; the interaction enhances KCNK2 surface expression and is inhibited by cAMP (PubMed:22354168, PubMed:26642364). {ECO:0000269|PubMed:22354168, ECO:0000269|PubMed:24496152, ECO:0000269|PubMed:26642364, ECO:0000305}. TISSUE SPECIFICITY: Detected in hippocampus astrocytes (at protein level) (PubMed:24496152). High expression in brain and lung. Also detected in kidney, heart and skeletal muscle. Not detected in liver. In the brain, highest expression in olfactory bulb, hippocampus and cerebellum. {ECO:0000269|PubMed:22354168, ECO:0000269|PubMed:24496152, ECO:0000269|PubMed:9003761}. +O35111 KCNK3_MOUSE Potassium channel subfamily K member 3 (Acid-sensitive potassium channel protein TASK-1) (Cardiac two pore background K(+) channel) (TWIK-related acid-sensitive K(+) channel 1) (Two pore potassium channel KT3.1) (Two pore K(+) channel KT3.1) (cTBAK-1) 409 45,068 Chain (1); Glycosylation (1); Intramembrane (2); Sequence conflict (2); Topological domain (3); Transmembrane (4) INTRAMEM 78 101 Pore-forming; Name=Pore-forming 1. {ECO:0000255}.; INTRAMEM 184 207 Pore-forming; Name=Pore-forming 2. {ECO:0000255}. TRANSMEM 9 29 Helical. {ECO:0000255}.; TRANSMEM 108 128 Helical. {ECO:0000255}.; TRANSMEM 159 179 Helical. {ECO:0000255}.; TRANSMEM 223 243 Helical. {ECO:0000255}. TOPO_DOM 1 8 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 129 158 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 244 409 Cytoplasmic. {ECO:0000255}. FUNCTION: pH-dependent, voltage-insensitive, background potassium channel protein. Rectification direction results from potassium ion concentration on either side of the membrane. Acts as an outward rectifier when external potassium concentration is low. When external potassium concentration is high, current is inward. {ECO:0000250|UniProtKB:O14649}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O14649}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O14649}. SUBUNIT: Homodimer. Heterodimer with KCNK1. {ECO:0000250|UniProtKB:O14649}. TISSUE SPECIFICITY: Very strong expression in heart, also detected in kidney, brain, skin, testis, lung, skeletal muscle, small intestine and stomach. Not detected in liver, thymus or spleen. +Q9ER47 KCNH7_MOUSE Potassium voltage-gated channel subfamily H member 7 (Ether-a-go-go-related gene potassium channel 3) (ERG-3) (Eag-related protein 3) (Ether-a-go-go-related protein 3) (Voltage-gated potassium channel subunit Kv11.3) 1195 135,062 Chain (1); Domain (2); Glycosylation (1); Intramembrane (1); Modified residue (5); Motif (1); Nucleotide binding (1); Sequence conflict (5); Topological domain (8); Transmembrane (6) INTRAMEM 615 635 Pore-forming; Name=Segment H5. {ECO:0000255}. TRANSMEM 413 433 Helical; Name=Segment S1. {ECO:0000255}.; TRANSMEM 450 470 Helical; Name=Segment S2. {ECO:0000255}.; TRANSMEM 495 515 Helical; Name=Segment S3. {ECO:0000255}.; TRANSMEM 522 542 Helical; Voltage-sensor; Name=Segment S4. {ECO:0000255}.; TRANSMEM 550 570 Helical; Name=Segment S5. {ECO:0000255}.; TRANSMEM 642 662 Helical; Name=Segment S6. {ECO:0000255}. TOPO_DOM 1 412 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 434 449 Extracellular. {ECO:0000255}.; TOPO_DOM 471 494 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 516 521 Extracellular. {ECO:0000255}.; TOPO_DOM 543 549 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 571 614 Extracellular. {ECO:0000255}.; TOPO_DOM 636 641 Extracellular. {ECO:0000255}.; TOPO_DOM 663 1195 Cytoplasmic. {ECO:0000255}. FUNCTION: Pore-forming (alpha) subunit of voltage-gated potassium channel (By similarity). Channel properties may be modulated by cAMP and subunit assembly. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SUBUNIT: The potassium channel is probably composed of a homo- or heterotetrameric complex of pore-forming alpha subunits that can associate with modulating beta subunits. Heteromultimer with KCNH2/ERG1 and KCNH6/ERG2 (By similarity). {ECO:0000250}. DOMAIN: The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position. +Q80ZQ5 JAZF1_MOUSE Juxtaposed with another zinc finger protein 1 243 27,098 Alternative sequence (1); Chain (1); Modified residue (2); Region (1); Sequence conflict (1); Zinc finger (3) FUNCTION: Acts as a transcriptional corepressor of orphan nuclear receptor NR2C2 (By similarity). Inhibits expression of the gluconeogenesis enzyme PCK2 through inhibition of NR2C2 activity (PubMed:24380856). Also involved in transcriptional activation of NAMPT by promoting expression of PPARA and PPARD (PubMed:24930994). Plays a role in lipid metabolism by suppressing lipogenesis, increasing lipolysis and decreasing lipid accumulation in adipose tissue (PubMed:24380856, PubMed:25614086). Plays a role in glucose homeostasis by improving glucose metabolism and insulin sensitivity (PubMed:25614086, PubMed:24380856). {ECO:0000250|UniProtKB:Q86VZ6, ECO:0000269|PubMed:24380856, ECO:0000269|PubMed:24930994, ECO:0000269|PubMed:25614086}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q86VZ6}. SUBUNIT: Interacts with NR2C2 (via ligand-binding region). {ECO:0000250|UniProtKB:Q86VZ6}. TISSUE SPECIFICITY: Expressed in range of tissues with highest expression levels in testis, liver, muscle and fat and lowest levels in kidney (PubMed:25614086). Detected in liver and white adipose tissue (at protein level) (PubMed:24380856). {ECO:0000269|PubMed:24380856, ECO:0000269|PubMed:25614086}. +Q9QYE5 JAG2_MOUSE Protein jagged-2 (Jagged2) 1247 134,745 Chain (1); Disulfide bond (51); Domain (17); Glycosylation (5); Modified residue (1); Sequence conflict (15); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1083 1103 Helical. {ECO:0000255}. TOPO_DOM 24 1082 Extracellular. {ECO:0000255}.; TOPO_DOM 1104 1247 Cytoplasmic. {ECO:0000255}. FUNCTION: Putative Notch ligand involved in the mediation of Notch signaling. Plays an essential role during limb, craniofacial and thymic development. May be involved in myogenesis and in the development of peripheral and central nervous systems. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. TISSUE SPECIFICITY: Found to be highest in fetal thymus, epidermis, foregut dorsal root ganglia and inner ear. In 2-weeK-old mice, abundant in heart, lung, thymus, skeletal muscle, brain and testis. Expression overlaps partially with Notch1 expression. {ECO:0000269|PubMed:9315665}. +Q9JI59 JAM2_MOUSE Junctional adhesion molecule B (JAM-B) (Junctional adhesion molecule 2) (JAM-2) (Vascular endothelial junction-associated molecule) (VE-JAM) (CD antigen CD322) 298 33,047 Beta strand (1); Chain (1); Disulfide bond (2); Domain (2); Glycosylation (1); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 237 257 Helical. {ECO:0000255}. TOPO_DOM 29 236 Extracellular. {ECO:0000255}.; TOPO_DOM 258 298 Cytoplasmic. {ECO:0000255}. FUNCTION: May play a role in the processes of lymphocyte homing to secondary lymphoid organs. {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000269|PubMed:11036763}. Cell membrane {ECO:0000269|PubMed:11036763}; Single-pass type I membrane protein {ECO:0000269|PubMed:11036763}. Note=Localized at tight junctions of both epithelial and endothelial cells. SUBUNIT: Interacts with JAM3. {ECO:0000250}. +Q9ERI5 JMJD6_MOUSE Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6 (EC 1.14.11.-) (Histone arginine demethylase JMJD6) (JmjC domain-containing protein 6) (Jumonji domain-containing protein 6) (Lysyl-hydroxylase JMJD6) (Peptide-lysine 5-dioxygenase JMJD6) (Phosphatidylserine receptor) (Protein PTDSR) 403 46,567 Alternative sequence (2); Binding site (4); Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (1); Metal binding (3); Motif (5); Sequence conflict (2) FUNCTION: Dioxygenase that can both act as a histone arginine demethylase and a lysyl-hydroxylase. Acts as a lysyl-hydroxylase that catalyzes 5-hydroxylation on specific lysine residues of target proteins such as U2AF2/U2AF65 and LUC7L2. Acts as a regulator of RNA splicing by mediating 5-hydroxylation of U2AF2/U2AF65, affecting the pre-mRNA splicing activity of U2AF2/U2AF65. In addition to peptidyl-lysine 5-dioxygenase activity, may act as an RNA hydroxylase, as suggested by its ability to bind single strand RNA. Also acts as an arginine demethylase which demethylates histone H3 at 'Arg-2' (H3R2me) and histone H4 at 'Arg-3' (H4R3me), thereby playing a role in histone code. However, histone arginine demethylation may not constitute the primary activity in vivo. Has no histone lysine demethylase activity. Required for differentiation of multiple organs during embryogenesis. Acts as a key regulator of hematopoietic differentiation: required for angiogenic sprouting by regulating the pre-mRNA splicing activity of U2AF2/U2AF65. Seems to be necessary for the regulation of macrophage cytokine responses (By similarity). {ECO:0000250, ECO:0000269|PubMed:15345036, ECO:0000269|PubMed:21300889}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:14729065}. Nucleus, nucleolus {ECO:0000250}. Note=Mainly found throughout the nucleoplasm outside of regions containing heterochromatic DNA, with some localization in nucleolus. During mitosis, excluded from the nucleus and reappears in the telophase of the cell cycle (By similarity). {ECO:0000250}. SUBUNIT: Interacts with LUC7L2 and LUC7L3. Interacts with BRD4 (By similarity). Interacts with U2AF2/U2AF65. Interacts with LIAT1. {ECO:0000250, ECO:0000269|PubMed:21300889, ECO:0000269|PubMed:25369936}. DOMAIN: The nuclear localization signal motifs are necessary and sufficient to target it into the nucleus. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. Expressed in brain, eye, spinal chord, thymus, lung, liver, kidney and intestine. {ECO:0000269|PubMed:14645847, ECO:0000269|PubMed:15345036}. +A2ARA8 ITA8_MOUSE Integrin alpha-8 [Cleaved into: Integrin alpha-8 heavy chain; Integrin alpha-8 light chain] 1062 117,556 Alternative sequence (2); Calcium binding (3); Chain (3); Disulfide bond (9); Glycosylation (16); Motif (1); Repeat (7); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1011 1031 Helical. {ECO:0000255}. TOPO_DOM 36 1010 Extracellular. {ECO:0000255}.; TOPO_DOM 1032 1062 Cytoplasmic. {ECO:0000255}. FUNCTION: Integrin alpha-8/beta-1 functions in the genesis of kidney and probably of other organs by regulating the recruitment of mesenchymal cells into epithelial structures. It recognizes the sequence R-G-D in a wide array of ligands including TNC, FN1, SPP1 TGFB1, TGFB3 and VTN. NPNT is probably its functional ligand in kidney genesis. Neuronal receptor for TNC it mediates cell-cell interactions and regulates neurite outgrowth of sensory and motor neurons. {ECO:0000269|PubMed:10742111, ECO:0000269|PubMed:11470831, ECO:0000269|PubMed:11891185, ECO:0000269|PubMed:12787402, ECO:0000269|PubMed:17537792, ECO:0000269|PubMed:9054500, ECO:0000269|PubMed:9548928, ECO:0000269|PubMed:9614184}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10742111}; Single-pass type I membrane protein {ECO:0000269|PubMed:10742111}. Cell membrane {ECO:0000250}. SUBUNIT: Heterodimer of an alpha and a beta subunit. The alpha subunit is composed of a heavy and a light chain linked by a disulfide bond. Alpha-8 associates with beta-1. TISSUE SPECIFICITY: In brain, expressed in deep cortex, hippocampal CA1, basolateral amygdala and striatum. In kidney, expressed in glomerular mesengium (at protein level). {ECO:0000269|PubMed:10024342, ECO:0000269|PubMed:10504498}. +Q6PGH2 JUPI2_MOUSE Jupiter microtubule associated homolog 2 (Hematological and neurological expressed 1-like protein) (HN1-like protein) 190 20,020 Chain (1); Modified residue (7) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H910}. Nucleus {ECO:0000250|UniProtKB:Q9H910}. +P15066 JUND_MOUSE Transcription factor jun-D 341 34,905 Chain (1); Domain (1); Modified residue (3); Region (2); Sequence conflict (3) FUNCTION: Transcription factor binding AP-1 sites. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Binds DNA as a dimer (By similarity). Interacts with MEN1. {ECO:0000250, ECO:0000269|PubMed:9989505}. TISSUE SPECIFICITY: Brain and kidney. +Q5SYL3 K0100_MOUSE Protein KIAA0100 2234 254,469 Chain (1); Coiled coil (1); Erroneous initiation (1); Modified residue (3); Sequence caution (1); Sequence conflict (6); Signal peptide (1) FUNCTION: May be involved in membrane trafficking. {ECO:0000250|UniProtKB:K7VLR4}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q80U59 K0232_MOUSE Uncharacterized protein KIAA0232 1396 154,778 Alternative sequence (4); Chain (1); Compositional bias (2); Modified residue (4); Nucleotide binding (1); Sequence conflict (7) +A2AFS3 K1324_MOUSE UPF0577 protein KIAA1324 1009 110,682 Alternative sequence (3); Chain (1); Disulfide bond (3); Frameshift (1); Glycosylation (3); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 907 927 Helical. {ECO:0000255}. TOPO_DOM 36 906 Extracellular. {ECO:0000255}.; TOPO_DOM 928 1009 Cytoplasmic. {ECO:0000255}. FUNCTION: May protect cells from cell death by inducing cytosolic vacuolization and upregulating the autophagy pathway. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Late endosome membrane {ECO:0000250}; Single-pass type I membrane protein. Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Single-pass type I membrane protein. Lysosome membrane {ECO:0000250}; Single-pass membrane protein. +P09055 ITB1_MOUSE Integrin beta-1 (Fibronectin receptor subunit beta) (VLA-4 subunit beta) (CD antigen CD29) 798 88,231 Alternative sequence (2); Beta strand (1); Chain (1); Cross-link (1); Disulfide bond (28); Domain (1); Erroneous initiation (1); Glycosylation (12); Metal binding (10); Modified residue (5); Mutagenesis (2); Region (5); Repeat (4); Sequence conflict (7); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 729 751 Helical. {ECO:0000255}. TOPO_DOM 21 728 Extracellular. {ECO:0000255}.; TOPO_DOM 752 798 Cytoplasmic. {ECO:0000255}. FUNCTION: Integrins alpha-1/beta-1, alpha-2/beta-1, alpha-10/beta-1 and alpha-11/beta-1 are receptors for collagen. Integrins alpha-1/beta-1 and alpha-2/beta-2 recognize the proline-hydroxylated sequence G-F-P-G-E-R in collagen. Integrins alpha-2/beta-1, alpha-3/beta-1, alpha-4/beta-1, alpha-5/beta-1, alpha-8/beta-1, alpha-10/beta-1, alpha-11/beta-1 and alpha-V/beta-1 are receptors for fibronectin. Alpha-4/beta-1 recognizes one or more domains within the alternatively spliced CS-1 and CS-5 regions of fibronectin. Integrin alpha-5/beta-1 is a receptor for fibrinogen. Integrin alpha-1/beta-1, alpha-2/beta-1, alpha-6/beta-1 and alpha-7/beta-1 are receptors for lamimin. Integrin alpha-6/beta-1 (ITGA6:ITGB1) is present in oocytes and is involved in sperm-egg fusion (PubMed:10634791). Integrin alpha-4/beta-1 is a receptor for VCAM1 and recognizes the sequence Q-I-D-S in VCAM1. Integrin alpha-9/beta-1 is a receptor for VCAM1, cytotactin and osteopontin. It recognizes the sequence A-E-I-D-G-I-E-L in cytotactin. Integrin alpha-3/beta-1 is a receptor for epiligrin, thrombospondin and CSPG4. Integrin alpha-3/beta-1 provides a docking site for FAP (seprase) at invadopodia plasma membranes in a collagen-dependent manner and hence may participate in the adhesion, formation of invadopodia and matrix degradation processes, promoting cell invasion. Alpha-3/beta-1 may mediate with LGALS3 the stimulation by CSPG4 of endothelial cells migration. Integrin alpha-V/beta-1 is a receptor for vitronectin. Beta-1 integrins recognize the sequence R-G-D in a wide array of ligands. When associated with alpha-7/beta-1 integrin, regulates cell adhesion and laminin matrix deposition (PubMed:12941630). Involved in promoting endothelial cell motility and angiogenesis (PubMed:15181153). Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process and the formation of mineralized bone nodules (PubMed:21768292). May be involved in up-regulation of the activity of kinases such as PKC via binding to KRT1. Together with KRT1 and RACK1, serves as a platform for SRC activation or inactivation. Plays a mechanistic adhesive role during telophase, required for the successful completion of cytokinesis (PubMed:18804435). ITGA4:ITGB1 binds to fractalkine (CX3CL1) and may act as its coreceptor in CX3CR1-dependent fractalkine signaling (By similarity). ITGA4:ITGB1 and ITGA5:ITGB1 bind to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational changes and enhanced ligand binding to site 1 (By similarity). ITGA5:ITGB1 acts as a receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell adhesion to FBN1 (By similarity). ITGA5:ITGB1 is a receptor for IL1B and binding is essential for IL1B signaling (By similarity). {ECO:0000250|UniProtKB:P05556, ECO:0000269|PubMed:10634791, ECO:0000269|PubMed:12941630, ECO:0000269|PubMed:15181153, ECO:0000269|PubMed:18804435, ECO:0000269|PubMed:19903482, ECO:0000269|PubMed:21768292}.; FUNCTION: Isoform 2: Isoform 2 displaces isoform 1 in striated muscles. {ECO:0000269|PubMed:8567725}. PTM: The cysteine residues are involved in intrachain disulfide bonds. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P05556}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, invadopodium membrane {ECO:0000250|UniProtKB:P05556}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:P05556}; Single-pass type I membrane protein {ECO:0000255}. Recycling endosome {ECO:0000269|PubMed:21768292, ECO:0000269|PubMed:8567725}. Melanosome {ECO:0000250|UniProtKB:P05556}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:P05556}. Cell projection, ruffle {ECO:0000250|UniProtKB:P05556}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:P05556}. Cell surface {ECO:0000250|UniProtKB:P05556}. Note=Colocalizes with ITGB1BP1 and metastatic suppressor protein NME2 at the edge or peripheral ruffles and lamellipodia during the early stages of cell spreading on fibronectin or collagen. Translocates from peripheral focal adhesions to fibrillar adhesions in an ITGB1BP1-dependent manner. Enriched preferentially at invadopodia, cell membrane protrusions that correspond to sites of cell invasion, in a collagen-dependent manner. Localized at plasma and ruffle membranes in a collagen-independent manner. {ECO:0000250|UniProtKB:P05556}.; SUBCELLULAR LOCATION: Isoform 2: Cell membrane, sarcolemma. Cell junction. Note=In cardiac muscle, isoform 2 is found in costameres and intercalated disks. SUBUNIT: Interacts with seprase FAP (seprase); the interaction occurs at the cell surface of invadopodia membrane in a collagen-dependent manner (By similarity). Heterodimer of an alpha and a beta subunit. Beta-1 associates with either alpha-1, alpha-2, alpha-3, alpha-4, alpha-5, alpha-6, alpha-7, alpha-8, alpha-9, alpha-10, alpha-11 or alpha-V. ITGA6:ITGB1 is found in a complex with CD9; interaction takes place in oocytes and is involved in sperm-egg fusion (PubMed:10634791). Binds LGALS3BP and NMRK2, when associated with alpha-7, but not with alpha-5. Interacts with FLNA, FLNB, FLNC and RANBP9. Interacts with KRT1 in the presence of RACK1 and SRC. Interacts with JAML; integrin alpha-4/beta-1 may regulate leukocyte to endothelial cells adhesion by controlling JAML homodimerization. Interacts with RAB21. Interacts (via the cytoplasmic region) with RAB25 (via the hypervariable C-terminal region). Interacts with MYO10. Interacts with ITGB1BP1 (via C-terminal region); the interaction is a prerequisite for focal adhesion disassembly. Interacts with TLN1; the interaction is prevented by competitive binding of ITGB1BP1. Interacts with ACAP1; required for ITGB1 recycling. Interacts with ASAP3. Interacts with FERMT2; the interaction is inhibited in presence of ITGB1BP1. Interacts with DAB2. Interacts with FGR and HCK. Isoform 2 interacts with alpha-7A and alpha-7B in adult skeletal muscle. Isoform 2 interacts with alpha-7B in cardiomyocytes of adult heart. Interacts with EMP2; the interaction may be direct or indirect and ITGB1 has an heterodimer form (PubMed:12189152). ITGA5:ITGB1 interacts with CCN3 (By similarity). ITGA4:ITGB1 is found in a ternary complex with CX3CR1 and CX3CL1 (By similarity). ITGA5:ITGB1 interacts with FBN1 (By similarity). ITGA5:ITGB1 interacts with IL1B. {ECO:0000250|UniProtKB:P05556, ECO:0000269|PubMed:10634791, ECO:0000269|PubMed:12189152, ECO:0000269|PubMed:12941630, ECO:0000269|PubMed:15181153, ECO:0000269|PubMed:15734730, ECO:0000269|PubMed:18483218, ECO:0000269|PubMed:19903482, ECO:0000269|PubMed:8567725}. TISSUE SPECIFICITY: Isoform 2 is expressed in skeletal and cardiac muscles only (at protein level). Isoform 1 is very weakly expressed in striated muscles and not detected in adult skeletal muscle fibers and cardiomyocytes. {ECO:0000269|PubMed:8567725}. +Q8R0A7 K0513_MOUSE Uncharacterized protein KIAA0513 407 46,318 Chain (1); Erroneous initiation (1); Modified residue (1); Sequence conflict (3) +A2A7S8 K1522_MOUSE Uncharacterized protein KIAA1522 1013 104,842 Alternative sequence (3); Chain (1); Compositional bias (3); Erroneous initiation (1); Modified residue (31); Sequence conflict (2) +Q68FD9 K1549_MOUSE UPF0606 protein KIAA1549 1940 209,221 Chain (1); Compositional bias (1); Modified residue (6); Sequence caution (1); Transmembrane (2) TRANSMEM 988 1008 Helical. {ECO:0000255}.; TRANSMEM 1288 1308 Helical. {ECO:0000255}. PTM: O-glycosylated. O-mannosylated by POMT1 and POMT2 and elongated by POMGNT1. {ECO:0000250|UniProtKB:Q9HCM3}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q7TQE7 K0895_MOUSE Uncharacterized protein KIAA0895 519 59,404 Alternative sequence (1); Chain (1); Erroneous initiation (1) +Q8BRV5 K1671_MOUSE Uncharacterized protein KIAA1671 308 34,668 Chain (1); Modified residue (6) +P02535 K1C10_MOUSE Keratin, type I cytoskeletal 10 (56 kDa cytokeratin) (Cytokeratin-10) (CK-10) (Keratin, type I cytoskeletal 59 kDa) (Keratin-10) (K10) 570 57,770 Alternative sequence (4); Chain (1); Compositional bias (1); Disulfide bond (1); Domain (1); Frameshift (1); Modified residue (8); Region (7); Sequence conflict (34); Site (1) FUNCTION: Plays a role in the establishment of the epidermal barrier on plantar skin. {ECO:0000269|PubMed:26603179}.; FUNCTION: (Microbial infection) Acts as a mediator of S.aureus adherence to desquamated nasal epithelial cells via clfB, and hence may play a role in nasal colonization. {ECO:0000269|PubMed:15385531}. SUBUNIT: (Microbial infection) Interacts (via C-terminal tail domain) with the S.aureus clumping factor, clfB; this interaction probably mediates S.aureus attachment to the highly keratinized squamous epithelial cells from the nasal cavity. {ECO:0000269|PubMed:15385531}.; SUBUNIT: Heterotetramer of two type I and two type II keratins. Heterodimer with KRT1. Two heterodimers of KRT1 and KRT10 form a heterotetramer. The KRT10 subunit in the heterotetramer is probably disulfide-linked. {ECO:0000250|UniProtKB:P13645}. TISSUE SPECIFICITY: Expressed in the suprabasal layers of the epidermis throughout the entire sole (at protein level). {ECO:0000269|PubMed:26603179}. +Q64291 K1C12_MOUSE Keratin, type I cytoskeletal 12 (Cytokeratin-12) (CK-12) (Keratin-12) (K12) 487 52,464 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (1); Frameshift (2); Region (7); Sequence conflict (7) FUNCTION: May play a unique role in maintaining the normal corneal epithelial function. Together with KRT3, essential for the maintenance of corneal epithelium integrity. {ECO:0000269|PubMed:7508359, ECO:0000269|PubMed:8977471}. SUBUNIT: Heterotetramer of two type I and two type II keratins. Keratin-3 associates with keratin-12. TISSUE SPECIFICITY: Cornea specific. Associated mainly with all layers of the central corneal epithelium and also found in the suprabasal limbal epithelium. {ECO:0000269|PubMed:7508359}. +Q3TRJ4 K1C26_MOUSE Keratin, type I cytoskeletal 26 (Cytokeratin-26) (CK-26) (Keratin-26) (K26) (Type I inner root sheath-specific keratin-K25irs2) 462 51,118 Chain (1); Compositional bias (1); Domain (1); Region (7); Sequence conflict (1) SUBUNIT: Heterotetramer of two type I and two type II keratins. {ECO:0000305}. +Q6IFX4 K1C39_MOUSE Keratin, type I cytoskeletal 39 (Cytokeratin-39) (CK-39) (Keratin-39) (K39) (Type I hair keratin Ka35) 482 54,287 Chain (1); Domain (1); Erroneous gene model prediction (1); Region (7); Sequence conflict (1); Site (1) FUNCTION: May play a role in late hair differentiation. {ECO:0000250}. SUBUNIT: Heterotetramer of two type I and two type II keratins. +P50446 K2C6A_MOUSE Keratin, type II cytoskeletal 6A (Cytokeratin-6A) (CK-6A) (Keratin-6-alpha) (mK6-alpha) (Keratin-6A) (K6A) 553 59,335 Chain (1); Domain (1); Region (7); Sequence conflict (16); Site (1) FUNCTION: Epidermis-specific type I keratin involved in wound healing (PubMed:10866680). Involved in the activation of follicular keratinocytes after wounding, while it does not play a major role in keratinocyte proliferation or migration (PubMed:10866680). Participates in the regulation of epithelial migration by inhibiting the activity of SRC during wound repair (PubMed:22529101). {ECO:0000269|PubMed:10866680, ECO:0000269|PubMed:22529101}. SUBUNIT: Heterodimer of a type I and a type II keratin. KRT6 isomers associate with KRT16 and/or KRT17 (PubMed:8636216). Interacts with TCHP (By similarity). {ECO:0000250, ECO:0000269|PubMed:8636216}. TISSUE SPECIFICITY: Predominates in the adult trunk skin, tongue, trachea/esophagus and eye. In adult skin, localization is restricted to hair follicles, where it is localized predominantly in the outer root sheath. {ECO:0000269|PubMed:11069616, ECO:0000269|PubMed:9790766}. +Q6IFX3 K1C40_MOUSE Keratin, type I cytoskeletal 40 (Cytokeratin-40) (CK-40) (Keratin-40) (K40) (Type I hair keratin Ka36) 439 48,928 Chain (1); Domain (1); Region (7); Sequence conflict (2); Site (1) FUNCTION: May play a role in late hair differentiation. {ECO:0000250}. SUBUNIT: Heterotetramer of two type I and two type II keratins. +Q6IFX2 K1C42_MOUSE Keratin, type I cytoskeletal 42 (Cytokeratin-42) (CK-42) (Keratin-17n) (Keratin-42) (K42) (Type I keratin Ka22) 452 50,133 Chain (1); Compositional bias (1); Domain (1); Region (7); Sequence conflict (5) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15102087}. SUBUNIT: Heterodimer of a type I and a type II keratin. Colocalizes with KRT8/KRT18 filament network. {ECO:0000269|PubMed:15102087, ECO:0000305}. TISSUE SPECIFICITY: Expressed in nail matrix and nail bed epithelium (at protein level). Also expressed in tongue and digits with weak expression in vibrissae and in both filiform and fungiform papillae of oral mucosa. {ECO:0000269|PubMed:15102087}. +Q91X21 K2013_MOUSE Uncharacterized protein KIAA2013 634 69,425 Alternative sequence (2); Chain (1); Erroneous initiation (1); Glycosylation (1); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 590 610 Helical. {ECO:0000255}. TOPO_DOM 41 589 Extracellular. {ECO:0000255}.; TOPO_DOM 611 634 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q6IME9 K2C72_MOUSE Keratin, type II cytoskeletal 72 (Cytokeratin-72) (CK-72) (Keratin-72) (K72) (Type II inner root sheath-specific keratin-K6irs2) (Type-II keratin Kb35) 520 56,750 Chain (1); Compositional bias (1); Domain (1); Region (7); Site (1) FUNCTION: Has a role in hair formation. Specific component of keratin intermediate filaments in the inner root sheath (IRS) of the hair follicle (By similarity). {ECO:0000250}. SUBUNIT: Heterotetramer of two type I and two type II keratins. +Q62168 K1H2_MOUSE Keratin, type I cuticular Ha2 (Hair keratin, type I Ha2) (Keratin-32) (K32) 407 46,422 Chain (1); Domain (1); Region (7); Sequence conflict (1); Site (1) TISSUE SPECIFICITY: Cuticle of the hair shaft. +Q3TTY5 K22E_MOUSE Keratin, type II cytoskeletal 2 epidermal (Cytokeratin-2e) (CK-2e) (Epithelial keratin-2e) (Keratin-2 epidermis) (Keratin-2e) (K2e) (Type-II keratin Kb2) 707 70,923 Chain (1); Compositional bias (1); Domain (1); Modified residue (9); Natural variant (1); Region (7); Sequence conflict (9); Site (1) FUNCTION: Probably contributes to terminal cornification (By similarity). Associated with keratinocyte activation, proliferation and keratinization (By similarity). Plays a role in the establishment of the epidermal barrier on plantar skin (PubMed:26603179). {ECO:0000250|UniProtKB:P35908, ECO:0000269|PubMed:26603179}. SUBUNIT: Heterotetramer of two type I and two type II keratins. Associates with KRT10. {ECO:0000269|PubMed:9378767, ECO:0000305}. TISSUE SPECIFICITY: Expressed predominantly in the suprabasal layers of the plantar epidermis outside of the footpads (at protein level) (PubMed:26603179). Expressed mainly in the middle spinous and granular cells of the epidermis of adult tail, nipple and footsole skin. Also found in ear. {ECO:0000269|PubMed:15118396, ECO:0000269|PubMed:2448177, ECO:0000269|PubMed:26603179, ECO:0000269|PubMed:7508961}. DISEASE: Note=Defects in Krt2 are a cause of ichthyosis bullosa of siemens (IBS). IBS is a rare autosomal dominant disorder displaying a type of epidermolytic hyperkeratosis characterized by extensive blistering from birth. Hyperkeratoses and shedding of the outer layers of the epidermis (molting) are observed in later weeks. +P04104 K2C1_MOUSE Keratin, type II cytoskeletal 1 (67 kDa cytokeratin) (Cytokeratin-1) (CK-1) (Keratin-1) (K1) (Type-II keratin Kb1) 637 65,606 Chain (1); Coiled coil (2); Compositional bias (2); Domain (1); Modified residue (10); Natural variant (1); Region (7); Sequence conflict (15); Site (1) FUNCTION: May regulate the activity of kinases such as PKC and SRC via binding to integrin beta-1 (ITB1) and the receptor of activated protein C kinase 1 (RACK1). In complex with C1QBP is a high affinity receptor for kininogen-1/HMWK (By similarity). {ECO:0000250}. PTM: Undergoes deimination of some arginine residues (citrullination). {ECO:0000269|PubMed:11841545}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. SUBUNIT: Heterotetramer of two type I and two type II keratins. Heterodimer with KRT10. Two heterodimers of KRT1 and KRT10 form a heterotetramer. Interacts with ITGB1 in the presence of RACK1 and SRC, and with RACK1. Interacts with C1QBP; the association represents a cell surface kininogen receptor. Interacts with EPPK1; interaction is dependent of higher-order structure of intermediate filament. {ECO:0000250|UniProtKB:P04264}. DISEASE: Note=Defects in Krt1 are a cause of epidermolytic hyperkeratosis (EHK); also known as bullous congenital ichthyosiform erythroderma (BIE). EHK is a hereditary skin disorder characterized by intraepidermal blistering, a marked thickening of the stratum corneum, pigmentation of the skin and erosions at sites of trauma which are all present from birth. +Q61759 K1B21_MOUSE Kallikrein 1-related peptidase b21 (EC 3.4.21.35) (Glandular kallikrein K21) (mGK-21) (Tissue kallikrein 21) 261 28,690 Active site (3); Chain (1); Disulfide bond (5); Domain (1); Glycosylation (1); Propeptide (1); Signal peptide (1) FUNCTION: Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin. Displays trypsin-like substrate specificity and shows activity towards casein, gelatin, fibronectin and IGFBP3. {ECO:0000269|PubMed:11606460}. TISSUE SPECIFICITY: Expressed in testis and submaxillary gland. In the testis, expression localized specifically to Leydig cells in the interstitial tissues. {ECO:0000269|PubMed:11606460}. +Q0VBK2 K2C80_MOUSE Keratin, type II cytoskeletal 80 (Cytokeratin-80) (CK-80) (Keratin-80) (K80) (Type-II keratin Kb20) 452 50,660 Chain (1); Domain (1); Modified residue (1); Region (7); Site (1) SUBUNIT: Heterotetramer of two type I and two type II keratins. +P32442 MEOX1_MOUSE Homeobox protein MOX-1 (Mesenchyme homeobox 1) 253 27,980 Chain (1); DNA binding (1); Mutagenesis (1) FUNCTION: Mesodermal transcription factor that plays a key role in somitogenesis and is specifically required for sclerotome development. Required for maintenance of the sclerotome polarity and formation of the cranio-cervical joints (PubMed:19520072). Binds specifically to the promoter of target genes and regulates their expression. Activates expression of NKX3-2 in the sclerotome (PubMed:15024065). Activates expression of CDKN1A and CDKN2A in endothelial cells, acting as a regulator of vascular cell proliferation. While it activates CDKN1A in a DNA-dependent manner, it activates CDKN2A in a DNA-independent manner (PubMed:22206000). Required for hematopoietic stem cell (HSCs) induction via its role in somitogenesis: specification of HSCs occurs via the deployment of a specific endothelial precursor population, which arises within a sub-compartment of the somite named endotome (By similarity). {ECO:0000250|UniProtKB:F1Q4R9, ECO:0000269|PubMed:12925591, ECO:0000269|PubMed:1363541, ECO:0000269|PubMed:15024065, ECO:0000269|PubMed:15039437, ECO:0000269|PubMed:18417617, ECO:0000269|PubMed:19520072, ECO:0000269|PubMed:22206000}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22206000}. Cytoplasm {ECO:0000269|PubMed:22206000}. Note=Localizes predominantly in the nucleus. {ECO:0000269|PubMed:22206000}. TISSUE SPECIFICITY: Heart, lateral plate derivatives, kidney, loose connective tissue at sites of bone formation and skeletal muscle-connective tissue apposition. {ECO:0000269|PubMed:1363541}. +Q922U2 K2C5_MOUSE Keratin, type II cytoskeletal 5 (Cytokeratin-5) (CK-5) (Keratin-5) (K5) (Type-II keratin Kb5) 580 61,767 Chain (1); Compositional bias (3); Domain (1); Modified residue (13); Region (7); Sequence conflict (1); Site (1) SUBUNIT: Heterodimer of a type I and a type II keratin. Heterodimer with type I keratin KRT25 leading to the formation of keratin intermediate filament (KIF) network. Heterodimer with KRT14. Interacts with TCHP (By similarity). Interacts with EPPK1 (PubMed:18285451). {ECO:0000250|UniProtKB:P13647, ECO:0000269|PubMed:18285451}. TISSUE SPECIFICITY: Expressed in epidermis. {ECO:0000269|PubMed:11408584}. +P32443 MEOX2_MOUSE Homeobox protein MOX-2 (Mesenchyme homeobox 2) 303 33,506 Chain (1); Compositional bias (4); DNA binding (1) FUNCTION: Mesodermal transcription factor that plays a key role in somitogenesis and is required for sclerotome development. Activates expression of CDKN1A and CDKN2A in endothelial cells, acting as a regulator of vascular cell proliferation. While it activates CDKN1A in a DNA-dependent manner, it activates CDKN2A in a DNA-independent manner. May have a regulatory role when quiescent vascular smooth muscle cells reenter the cell cycle. {ECO:0000250|UniProtKB:P50222, ECO:0000269|PubMed:12925591, ECO:0000269|PubMed:1363541}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P50222}. Nucleus speckle {ECO:0000255|PROSITE-ProRule:PRU00108}. SUBUNIT: Interacts with RNF10. {ECO:0000250|UniProtKB:P50222}. DOMAIN: The polyhistidine repeat may act as a targeting signal to nuclear speckles. {ECO:0000250|UniProtKB:P50222}. +Q9JK45 KCNQ5_MOUSE Potassium voltage-gated channel subfamily KQT member 5 (KQT-like 5) (Potassium channel subunit alpha KvLQT5) (Voltage-gated potassium channel subunit Kv7.5) 933 102,258 Chain (1); Intramembrane (1); Modified residue (3); Motif (1); Sequence conflict (2); Topological domain (8); Transmembrane (6) INTRAMEM 300 320 Pore-forming; Name=Segment H5. {ECO:0000255}. TRANSMEM 127 147 Helical; Name=Segment S1. {ECO:0000255}.; TRANSMEM 158 178 Helical; Name=Segment S2. {ECO:0000255}.; TRANSMEM 202 222 Helical; Name=Segment S3. {ECO:0000255}.; TRANSMEM 231 253 Helical; Voltage-sensor; Name=Segment S4. {ECO:0000255}.; TRANSMEM 268 288 Helical; Name=Segment S5. {ECO:0000255}.; TRANSMEM 327 347 Helical; Name=Segment S6. {ECO:0000255}. TOPO_DOM 1 126 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 148 157 Extracellular. {ECO:0000255}.; TOPO_DOM 179 201 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 223 230 Extracellular. {ECO:0000255}.; TOPO_DOM 254 267 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 289 299 Extracellular. {ECO:0000255}.; TOPO_DOM 321 326 Extracellular. {ECO:0000255}.; TOPO_DOM 348 933 Cytoplasmic. {ECO:0000255}. FUNCTION: Associates with KCNQ3 to form a potassium channel which contributes to M-type current, a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons. Therefore, it is important in the regulation of neuronal excitability. May contribute, with other potassium channels, to the molecular diversity of a heterogeneous population of M-channels, varying in kinetic and pharmacological properties, which underlie this physiologically important current. {ECO:0000269|PubMed:15963599}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15963599}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Heteromultimer with KCNQ3. Heterotetramer with KCNQ1; has a voltage-gated potassium channel activity. {ECO:0000250|UniProtKB:Q9NR82}. DOMAIN: The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position. {ECO:0000250}. +Q9D808 KCNE2_MOUSE Potassium voltage-gated channel subfamily E member 2 (MinK-related peptide 1) (Minimum potassium ion channel-related peptide 1) (Potassium channel subunit beta MiRP1) 123 14,370 Chain (1); Glycosylation (2); Sequence conflict (1); Topological domain (1); Transmembrane (1) TRANSMEM 49 69 Helical. {ECO:0000255}. TOPO_DOM 70 123 Cytoplasmic. {ECO:0000255}. FUNCTION: Ancillary protein that assembles as a beta subunit with a voltage-gated potassium channel complex of pore-forming alpha subunits. Modulates the gating kinetics and enhances stability of the channel complex. Assembled with KCNB1 modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1. Associated with KCNH2/HERG is proposed to form the rapidly activating component of the delayed rectifying potassium current in heart (IKr). May associate with KCNQ2 and/or KCNQ3 and modulate the native M-type current. May associate with HCN1 and HCN2 and increase potassium current (By similarity). Interacts with KCNQ1; forms a heterooligomer complex leading to currents with an apparently instantaneous activation, a rapid deactivation process and a linear current-voltage relationship and decreases the amplitude of the outward current (By similarity). {ECO:0000250|UniProtKB:P63161, ECO:0000250|UniProtKB:Q9Y6J6}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P63161, ECO:0000250|UniProtKB:Q9Y6J6}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P63161}. Note=Colocalizes with KCNB1 at the plasma membrane. {ECO:0000250|UniProtKB:P63161}. SUBUNIT: Interacts with KCNB1. Associates with KCNH2/ERG1. May associate with KCNQ2 and KCNQ3. Associates with HCN1 and probably HCN2. Heteromultimer with KCNC2. Interacts with KCNC2 (By similarity). Interacts with KCNQ1; forms a heterooligomer complex that targets to the membrane raft and leading to currents with an apparently instantaneous activation, a rapid deactivation process and a linear current-voltage relationship and decreases the amplitude of the outward current (By similarity). {ECO:0000250|UniProtKB:P63161, ECO:0000250|UniProtKB:Q9Y6J6}. +P58390 KCNN2_MOUSE Small conductance calcium-activated potassium channel protein 2 (SK2) (SKCa 2) (SKCa2) (KCa2.2) 839 91,604 Chain (1); Compositional bias (6); Erroneous gene model prediction (1); Erroneous initiation (4); Frameshift (1); Intramembrane (1); Modified residue (1); Region (1); Sequence conflict (3); Transmembrane (6) INTRAMEM 605 625 Pore-forming; Name=Segment H5. {ECO:0000255}. TRANSMEM 398 418 Helical; Name=Segment S1. {ECO:0000255}.; TRANSMEM 428 448 Helical; Name=Segment S2. {ECO:0000255}.; TRANSMEM 474 494 Helical; Name=Segment S3. {ECO:0000255}.; TRANSMEM 516 536 Helical; Name=Segment S4. {ECO:0000255}.; TRANSMEM 565 585 Helical; Name=Segment S5. {ECO:0000255}.; TRANSMEM 634 654 Helical; Name=Segment S6. {ECO:0000255}. FUNCTION: Forms a voltage-independent potassium channel activated by intracellular calcium. Activation is followed by membrane hyperpolarization. Thought to regulate neuronal excitability by contributing to the slow component of synaptic afterhyperpolarization. The channel is blocked by apamin. {ECO:0000269|PubMed:11557517, ECO:0000269|PubMed:13679367, ECO:0000269|PubMed:14657188}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SUBUNIT: Heterooligomer. The complex is composed of 4 channel subunits each of which binds to a calmodulin subunit which regulates the channel activity through calcium-binding (By similarity). Interacts (via N-terminal domain) with MPP2 (PubMed:26880549). {ECO:0000250|UniProtKB:P70604, ECO:0000269|PubMed:26880549}. TISSUE SPECIFICITY: Expressed in atrial and ventricular myocytes with higher levels in atrial myocytes (at protein level). Highly expressed in brain, liver and colon with low levels in kidney and testis. In colon, detected in smooth muscle cells. {ECO:0000269|PubMed:11557517, ECO:0000269|PubMed:13679367, ECO:0000269|PubMed:16055520}. +Q6ZPR4 KCNT1_MOUSE Potassium channel subfamily T member 1 1224 138,106 Chain (1); Domain (1); Glycosylation (2); Intramembrane (1); Topological domain (8); Transmembrane (6) INTRAMEM 268 288 Pore-forming. {ECO:0000255}. TRANSMEM 84 104 Helical; Name=Segment S1. {ECO:0000255}.; TRANSMEM 142 162 Helical; Name=Segment S2. {ECO:0000255}.; TRANSMEM 174 194 Helical; Name=Segment S3. {ECO:0000255}.; TRANSMEM 200 212 Helical; Name=Segment S4. {ECO:0000255}.; TRANSMEM 238 258 Helical; Name=Segment S5. {ECO:0000255}.; TRANSMEM 291 311 Helical; Name=Segment S6. {ECO:0000255}. TOPO_DOM 1 83 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 105 141 Extracellular. {ECO:0000255}.; TOPO_DOM 163 173 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 195 199 Extracellular. {ECO:0000255}.; TOPO_DOM 213 237 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 259 267 Extracellular. {ECO:0000255}.; TOPO_DOM 289 290 Extracellular. {ECO:0000255}.; TOPO_DOM 312 1224 Cytoplasmic. {ECO:0000255}. FUNCTION: Outwardly rectifying potassium channel subunit that may coassemble with other Slo-type channel subunits. Activated by high intracellular sodium or chloride levels. Activated upon stimulation of G-protein coupled receptors, such as CHRM1 and GRIA1. May be regulated by calcium in the absence of sodium ions (in vitro) (By similarity). {ECO:0000250}. PTM: Phosphorylated by protein kinase C. Phosphorylation of the C-terminal domain increases channel activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts (via C-terminus) with FMR1; this interaction alters gating properties of KCNT1 (By similarity). Interacts with CRBN via its cytoplasmic C-terminus (By similarity). {ECO:0000250|UniProtKB:Q5JUK3, ECO:0000250|UniProtKB:Q9Z258}. +P48542 KCNJ6_MOUSE G protein-activated inward rectifier potassium channel 2 (GIRK-2) (Inward rectifier K(+) channel Kir3.2) (Potassium channel, inwardly rectifying subfamily J member 6) 425 48,652 Alternative sequence (6); Beta strand (19); Chain (1); Helix (8); Intramembrane (2); Modified residue (2); Motif (2); Natural variant (3); Sequence conflict (6); Site (1); Topological domain (4); Transmembrane (2); Turn (6) INTRAMEM 141 152 Helical; Pore-forming; Name=H5. {ECO:0000250}.; INTRAMEM 153 159 Pore-forming. {ECO:0000250}. TRANSMEM 92 116 Helical; Name=M1. {ECO:0000250}.; TRANSMEM 169 190 Helical; Name=M2. {ECO:0000250}. TOPO_DOM 1 91 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 117 140 Extracellular. {ECO:0000250}.; TOPO_DOM 160 168 Extracellular. {ECO:0000250}.; TOPO_DOM 191 425 Cytoplasmic. {ECO:0000250}. FUNCTION: This potassium channel is controlled by G proteins. It plays a role in granule cell differentiation, possibly via membrane hyperpolarization. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SUBUNIT: May associate with GIRK1 or GIRK4 to form a G-protein-activated heteromultimer pore-forming unit. The resulting inward current is much larger. Interacts (via PDZ-binding motif) with SNX27 (via PDZ domain); the interaction is required when endocytosed to prevent degradation in lysosomes and promote recycling to the plasma membrane (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Cerebellum, testes, cortex and substentia nigra. DISEASE: Note=Defects in Kcnj6 are the cause of the weaver (wv) phenotype. Homozygous animals suffer from severe ataxia that is obvious by about the second postnatal week. The cerebellum of these animals is drastically reduced in size due to depletion of the major cell type of cerebellum, the granule cell neuron. Heterozygous animals are not ataxic but have an intermediate number of surviving granule cells. Male homozygotes are sterile, because of complete failure of sperm production. Both hetero- and homozygous animals undergo sporadic tonic-clonic seizures. +Q80XM3 KCNG4_MOUSE Potassium voltage-gated channel subfamily G member 4 (Voltage-gated potassium channel subunit Kv6.4) 506 57,177 Chain (1); Intramembrane (2); Motif (1); Topological domain (8); Transmembrane (6) INTRAMEM 404 415 Helical; Name=Pore helix. {ECO:0000250|UniProtKB:P63142}.; INTRAMEM 416 423 {ECO:0000250|UniProtKB:P63142}. TRANSMEM 217 238 Helical; Name=Segment S1. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 260 281 Helical; Name=Segment S2. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 293 312 Helical; Name=Segment S3. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 327 351 Helical; Voltage-sensor; Name=Segment S4. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 367 388 Helical; Name=Segment S5. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 431 459 Helical; Name=Segment S6. {ECO:0000250|UniProtKB:P63142}. TOPO_DOM 1 216 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 239 259 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 282 292 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 313 326 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 352 366 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 389 403 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 424 430 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 460 506 Cytoplasmic. {ECO:0000305}. FUNCTION: Potassium channel subunit that does not form functional channels by itself. Can form functional heterotetrameric channels with KCNB1; modulates the delayed rectifier voltage-gated potassium channel activation and deactivation rates of KCNB1. {ECO:0000250|UniProtKB:Q8TDN1}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8TDN1}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8TDN1}. Note=Has to be associated with KCNB1 or possibly another partner to get inserted in the plasma membrane. Colocalizes with KCNB1 at the plasma membrane. Remains intracellular in the absence of KCNB1. {ECO:0000250|UniProtKB:Q8TDN1}. SUBUNIT: Heterotetramer with KCNB1. {ECO:0000250|UniProtKB:Q8TDN1}. DOMAIN: The transmembrane segment S4 functions as voltage-sensor and is characterized by a series of positively charged amino acids at every third position. Channel opening and closing is effected by a conformation change that affects the position and orientation of the voltage-sensor paddle formed by S3 and S4 within the membrane. A transmembrane electric field that is positive inside would push the positively charged S4 segment outwards, thereby opening the pore, while a field that is negative inside would pull the S4 segment inwards and close the pore. Changes in the position and orientation of S4 are then transmitted to the activation gate formed by the inner helix bundle via the S4-S5 linker region. {ECO:0000250|UniProtKB:P63142}. +Q8K3F6 KCNQ3_MOUSE Potassium voltage-gated channel subfamily KQT member 3 (KQT-like 3) (Potassium channel subunit alpha KvLQT3) (Voltage-gated potassium channel subunit Kv7.3) 873 96,852 Chain (1); Compositional bias (1); Intramembrane (1); Modified residue (1); Motif (1); Region (1); Sequence conflict (1); Topological domain (8); Transmembrane (6) INTRAMEM 305 325 Pore-forming; Name=Segment H5. {ECO:0000255}. TRANSMEM 123 143 Helical; Name=Segment S1. {ECO:0000255}.; TRANSMEM 154 174 Helical; Name=Segment S2. {ECO:0000255}.; TRANSMEM 198 218 Helical; Name=Segment S3. {ECO:0000255}.; TRANSMEM 227 248 Helical; Voltage-sensor; Name=Segment S4. {ECO:0000255}.; TRANSMEM 263 283 Helical; Name=Segment S5. {ECO:0000255}.; TRANSMEM 332 352 Helical; Name=Segment S6. {ECO:0000255}. TOPO_DOM 1 122 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 144 153 Extracellular. {ECO:0000255}.; TOPO_DOM 175 197 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 219 226 Extracellular. {ECO:0000255}.; TOPO_DOM 249 262 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 284 304 Extracellular. {ECO:0000255}.; TOPO_DOM 326 331 Extracellular. {ECO:0000255}.; TOPO_DOM 353 873 Cytoplasmic. {ECO:0000255}. FUNCTION: Associates with KCNQ2 or KCNQ5 to form a potassium channel with essentially identical properties to the channel underlying the native M-current, a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons as well as the responsiveness to synaptic inputs. Therefore, it is important in the regulation of neuronal excitability. {ECO:0000250|UniProtKB:O43525}. PTM: KCNQ2/KCNQ3 are ubiquitinated by NEDD4L. Ubiquitination leads to protein degradation. Degradation induced by NEDD4L is inhibited by USP36. {ECO:0000250|UniProtKB:O43525}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O43525}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Heterotetramer with KCNQ2; form the heterotetrameric M potassium channel. Interacts with calmodulin; the interaction is calcium-independent, constitutive and participates to the proper assembly of a functional heterotetrameric M channel. Heteromultimer with KCNQ5. May associate with KCNE2. Interacts with IQCJ-SCHIP1 (PubMed:27979964). {ECO:0000250|UniProtKB:O43525, ECO:0000269|PubMed:27979964}. DOMAIN: The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position. {ECO:0000250}. +Q920E3 KCNH5_MOUSE Potassium voltage-gated channel subfamily H member 5 (Ether-a-go-go potassium channel 2) (Eag2) (Voltage-gated potassium channel subunit Kv10.2) 988 111,810 Chain (1); Cross-link (1); Domain (2); Glycosylation (1); Intramembrane (1); Modified residue (1); Motif (1); Nucleotide binding (1); Region (2); Sequence conflict (1); Topological domain (8); Transmembrane (6) INTRAMEM 420 440 Pore-forming; Name=Segment H5. {ECO:0000255}. TRANSMEM 218 238 Helical; Name=Segment S1. {ECO:0000255}.; TRANSMEM 244 264 Helical; Name=Segment S2. {ECO:0000255}.; TRANSMEM 292 312 Helical; Name=Segment S3. {ECO:0000255}.; TRANSMEM 320 340 Helical; Voltage-sensor; Name=Segment S4. {ECO:0000255}.; TRANSMEM 347 367 Helical; Name=Segment S5. {ECO:0000255}.; TRANSMEM 447 467 Helical; Name=Segment S6. {ECO:0000255}. TOPO_DOM 1 217 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 239 243 Extracellular. {ECO:0000255}.; TOPO_DOM 265 291 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 313 319 Extracellular. {ECO:0000255}.; TOPO_DOM 341 346 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 368 419 Extracellular. {ECO:0000255}.; TOPO_DOM 441 446 Extracellular. {ECO:0000255}.; TOPO_DOM 468 988 Cytoplasmic. {ECO:0000255}. FUNCTION: Pore-forming (alpha) subunit of voltage-gated potassium channel. Elicits a non-inactivating outward rectifying current (By similarity). Channel properties may be modulated by cAMP and subunit assembly. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SUBUNIT: The potassium channel is probably composed of a homo- or heterotetrameric complex of pore-forming alpha subunits that can associate with modulating beta subunits. Heteromultimer with KCNH1/EAG (By similarity). {ECO:0000250}. DOMAIN: The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position. +Q91VY5 KDM4B_MOUSE Lysine-specific demethylase 4B (EC 1.14.11.-) (JmjC domain-containing histone demethylation protein 3B) (Jumonji domain-containing protein 2B) 1086 121,604 Alternative sequence (2); Binding site (4); Chain (1); Domain (4); Erroneous initiation (1); Metal binding (7); Modified residue (1); Sequence conflict (2); Zinc finger (3) FUNCTION: Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27', H3 'Lys-36' nor H4 'Lys-20'. Only able to demethylate trimethylated H3 'Lys-9', with a weaker activity than KDM4A, KDM4C and KDM4D. Demethylation of Lys residue generates formaldehyde and succinate (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00537}. DOMAIN: The 2 Tudor domains recognize and bind methylated histones. Double Tudor domain has an interdigitated structure and the unusual fold is required for its ability to bind methylated histone tails (By similarity). {ECO:0000250}. +Q9CXT6 KDM8_MOUSE Bifunctional peptidase and arginyl-hydroxylase JMJD5 (EC 1.14.11.-) (EC 3.4.-.-) (JmjC domain-containing protein 5) (Jumonji C domain-containing protein 5) (L-arginine (3R)-hydroxylase KDM8) (Lysine-specific demethylase 8) 414 47,145 Binding site (10); Chain (1); Domain (1); Metal binding (3); Region (1) FUNCTION: Bifunctional enzyme that acts both as an endopeptidase and 2-oxoglutarate-dependent monoxygenase. Endopeptidase that cleaves histones N-terminal tails at the carboxyl side of methylated arginine or lysine residues, to generate 'tailless nucleosomes', which may trigger transcription elongation. Preferentially recognizes and cleaves monomethylated and dimethylated arginine residues of histones H2, H3 and H4. After initial cleavage, continues to digest histones tails via its aminopeptidase activity. Upon DNA damage, cleaves the N-terminal tail of histone H3 at monomethylated lysine residues, preferably at monomethylated 'Lys-9' (H3K9me1). The histone variant H3F3A is the major target for cleavage. Additionnally, acts as Fe(2+) and 2-oxoglutarate-dependent monoxygenase, catalyzing (R)-stereospecific hydroxylation at C-3 of 'Arg-137' of RPS6 and 'Arg-141' of RCCD1, but the biological significance of this activity remains to be established. Regulates mitosis through different mechanisms: Plays a role in transcriptional repression of satellite repeats, possibly by regulating H3K36 methylation levels in centromeric regions together with RCCD1. Possibly together with RCCD1, is involved in proper mitotic spindle organization and chromosome segregation. Negatively regulates cell cycle repressor CDKN1A/p21, which controls G1/S phase transition. Required for G2/M phase cell cycle progression. Regulates expression of CCNA1/cyclin-A1, leading to cancer cell proliferation. Also, plays a role in regulating alpha-tubulin acetylation and cytoskeletal microtubule stability involved in epithelial to mesenchymal transition. {ECO:0000250|UniProtKB:Q8N371}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8N371}. Chromosome {ECO:0000250|UniProtKB:Q8N371}. Note=Colocalizes with trimethylated 'Lys-9' of histone H3 (H3K9me3). {ECO:0000250|UniProtKB:Q8N371}. SUBUNIT: Can form homodimers (via JmjC domain). Found in a complex with RCCD1. Interacts (via N-terminus) with RCCD1 (via N-terminus); this interaction stimulates H3K36me3 and H3K36me2 demethylation. Interacts (via JmjC domain) with HIST1H3A. {ECO:0000250|UniProtKB:Q8N371}. +Q8VE43 METRL_MOUSE Meteorin-like protein (Subfatin) 311 34,530 Alternative sequence (1); Chain (1); Disulfide bond (5); Glycosylation (1); Signal peptide (1) FUNCTION: Hormone induced following exercise or cold exposure that promotes energy expenditure. Induced either in the skeletal muscle after exercise or in adipose tissue following cold exposure and is present in the circulation. Able to stimulate energy expenditure associated with the browning of the white fat depots and improves glucose tolerance. Does not promote an increase in a thermogenic gene program via direct action on adipocytes, but acts by stimulating several immune cell subtypes to enter the adipose tissue and activate their prothermogenic actions. Stimulates an eosinophil-dependent increase in IL4 expression and promotes alternative activation of adipose tissue macrophages, which are required for the increased expression of the thermogenic and anti-inflammatory gene programs in fat. Required for some cold-induced thermogenic responses, suggesting a role in metabolic adaptations to cold temperatures. {ECO:0000269|PubMed:24906147}. PTM: N-glycosylated. {ECO:0000269|PubMed:24393292}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24393292, ECO:0000269|PubMed:24906147}. TISSUE SPECIFICITY: Highly expressed in subcutaneous adipose tissue. {ECO:0000269|PubMed:24393292, ECO:0000269|PubMed:24906147}. +Q05A36 MEX3C_MOUSE RNA-binding E3 ubiquitin-protein ligase MEX3C (EC 2.3.2.27) (RING finger and KH domain-containing protein 2) (RING-type E3 ubiquitin transferase MEX3C) 652 68,574 Chain (1); Domain (2); Erroneous initiation (1); Modified residue (2); Zinc finger (1) FUNCTION: RNA-binding protein. May be involved in post-transcriptional regulatory mechanisms, modulating levels of some mRNAs by promoting their degradation in a way involving ubiquitin ligase activity. May act as suppressor of replication stress and chromosome missegregation. {ECO:0000250}. PTM: Phosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Predominantly expressed in the cytoplasm and shuttles between the cytoplasm and the nucleus through the CRM1 export pathway. SUBUNIT: Interacts with USP7, which antagonizes the ability to degrade mRNA. {ECO:0000250}. DOMAIN: Binds RNA through its KH domains. {ECO:0000250}. +Q3UE17 MEX3D_MOUSE RNA-binding protein MEX3D (RING finger and KH domain-containing protein 1) 643 65,329 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (2); Modified residue (2); Zinc finger (1) FUNCTION: RNA binding protein, may be involved in post-transcriptional regulatory mechanisms. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Predominantly expressed in the cytoplasm and shuttles between the cytoplasm and the nucleus through the CRM1 export pathway. {ECO:0000250}. DOMAIN: Binds RNA through its KH domains. {ECO:0000250}. +C0HKD8 MFA1A_MOUSE Microfibrillar-associated protein 1A (Spliceosome B complex protein MFAP1A) 439 51,954 Chain (1); Compositional bias (1); Cross-link (7); Erroneous termination (1); Initiator methionine (1); Modified residue (11) FUNCTION: Involved in pre-mRNA splicing as a component of the spliceosome. {ECO:0000250|UniProtKB:P55081}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P55081}. SUBUNIT: Component of the spliceosome B complex. Interacts with PRPF38A (via N-terminal interaction domain). {ECO:0000250|UniProtKB:P55081}. +C0HKD9 MFA1B_MOUSE Microfibrillar-associated protein 1B (Spliceosome B complex protein MFAP1B) 439 51,954 Chain (1); Compositional bias (1); Cross-link (7); Initiator methionine (1); Modified residue (11) FUNCTION: Involved in pre-mRNA splicing as a component of the spliceosome. {ECO:0000250|UniProtKB:P55081}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P55081}. SUBUNIT: Component of the spliceosome B complex. Interacts with PRPF38A (via N-terminal interaction domain). {ECO:0000250|UniProtKB:P55081}. +Q9D3X9 MFA3L_MOUSE Microfibrillar-associated protein 3-like 409 45,342 Alternative sequence (1); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (5); Modified residue (5); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 149 169 Helical. {ECO:0000255}. TOPO_DOM 29 148 Extracellular. {ECO:0000255}.; TOPO_DOM 170 409 Cytoplasmic. {ECO:0000255}. FUNCTION: May participate in the nuclear signaling of EGFR and MAPK1/ERK2. {ECO:0000250|UniProtKB:O75121}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O75121}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:O75121}. Nucleus {ECO:0000250|UniProtKB:O75121}. Cytoplasm {ECO:0000250|UniProtKB:O75121}. Note=Mainly localized in the nucleus. {ECO:0000250|UniProtKB:O75121}. +Q922T2 MFAP3_MOUSE Microfibril-associated glycoprotein 3 349 38,406 Chain (1); Disulfide bond (1); Domain (1); Glycosylation (4); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 140 160 Helical. {ECO:0000255}. TOPO_DOM 22 139 Extracellular. {ECO:0000255}.; TOPO_DOM 161 349 Cytoplasmic. {ECO:0000255}. FUNCTION: Component of the elastin-associated microfibrils. {ECO:0000250}. PTM: Glycosylated. {ECO:0000305}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q9D1H9 MFAP4_MOUSE Microfibril-associated glycoprotein 4 257 28,938 Alternative sequence (1); Chain (1); Domain (1); Glycosylation (2); Motif (1); Signal peptide (1) FUNCTION: Could be involved in calcium-dependent cell adhesion or intercellular interactions. May contribute to the elastic fiber assembly and/or maintenance. {ECO:0000250|UniProtKB:P55083}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P55083}. SUBUNIT: Homodimer. Can also form higher oligomers. Interacts with FBN1, FBN2 and LOX. Interacts with COL1A1 in a Ca (2+)-dependent manner. Interacts with ELN in a Ca (2+)-dependent manner; this interaction promotes ELN self-assembly. {ECO:0000250|UniProtKB:P55083}. +Q6GV12 KDSR_MOUSE 3-ketodihydrosphingosine reductase (KDS reductase) (EC 1.1.1.102) (3-dehydrosphinganine reductase) (Follicular variant translocation protein 1 homolog) (FVT-1) 332 35,956 Active site (2); Binding site (1); Chain (1); Nucleotide binding (1); Signal peptide (1); Topological domain (3); Transmembrane (2) TRANSMEM 271 291 Helical. {ECO:0000255}.; TRANSMEM 294 314 Helical. {ECO:0000255}. TOPO_DOM 26 270 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 292 293 Lumenal. {ECO:0000255}.; TOPO_DOM 315 332 Cytoplasmic. {ECO:0000255}. Lipid metabolism; sphingolipid metabolism. FUNCTION: Catalyzes the reduction of 3-ketodihydrosphingosine (KDS) to dihydrosphingosine (DHS). {ECO:0000269|PubMed:15328338}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. +Q3V1N1 MFHA1_MOUSE Malignant fibrous histiocytoma-amplified sequence 1 homolog 1048 116,599 Chain (1); Domain (1); Initiator methionine (1); Modified residue (2); Region (2); Repeat (13); Sequence conflict (3) FUNCTION: Probable GTP-binding protein (By similarity). Functions in innate immunity and more specifically the inflammatory response as a regulator of the Toll-like receptor TLR2 and TLR4 signaling pathways (PubMed:20616063, PubMed:26599367). Negatively regulates the part of the TLR4 signaling pathway that leads to the activation of the transcription factor AP-1. By retaining the phosphatase complex PP2A into the cytoplasm, prevents the dephosphorylation of the AP-1 subunit JUN which is required for proper activation of the transcription factor (By similarity). Both inhibits and activates the TLR2-dependent signaling pathway (PubMed:26599367). Positively regulates the TLR2 signaling pathway to activate specifically the downstream p38 and JNK MAP kinases and promote the polarization of macrophages toward the pro-inflammatory M1 phenotype. It may also play a role in the regulation of inflammation induced by high glucose through the PKB/AKT signaling pathway. Also involved in erythrocyte differentiation through activation of the ERK1/ERK2 signaling pathway (By similarity). {ECO:0000250|UniProtKB:Q9Y4C4, ECO:0000269|PubMed:20616063, ECO:0000269|PubMed:26599367}. PTM: Ubiquitinated. Ubiquitination by PJA2 does not lead MFHAS1 to proteasomal degradation but positively regulates its function in polarization of macrophages. {ECO:0000250|UniProtKB:Q9Y4C4}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y4C4}. SUBUNIT: Interacts with RAF1. Interacts with HSPD1. Interacts with PPP2CA; retains PPP2CA into the cytoplasm and excludes it from the nucleus. Interacts with PPP2R2A; the interaction is direct. Interacts with PJA2. {ECO:0000250|UniProtKB:Q9Y4C4}. +Q9Z2X8 KEAP1_MOUSE Kelch-like ECH-associated protein 1 (Cytosolic inhibitor of Nrf2) (INrf2) 624 69,553 Beta strand (29); Chain (1); Domain (2); Erroneous initiation (1); Motif (1); Mutagenesis (3); Repeat (6); Sequence conflict (7); Turn (6) Protein modification; protein ubiquitination. FUNCTION: Acts as a substrate adapter protein for the E3 ubiquitin ligase complex formed by CUL3 and RBX1 and targets NFE2L2/NRF2 for ubiquitination and degradation by the proteasome, thus resulting in the suppression of its transcriptional activity and the repression of antioxidant response element-mediated detoxifying enzyme gene expression. Retains NFE2L2/NRF2 and may also retain BPTF in the cytosol. Targets PGAM5 for ubiquitination and degradation by the proteasome (By similarity). {ECO:0000250, ECO:0000269|PubMed:12682069, ECO:0000269|PubMed:9887101}. PTM: Ubiquitinated by the E3 ubiquitin ligase complex formed by CUL3 and RBX1 and is subject to proteasomal-independent degradation. Quinone-induced oxidative stress, but not sulforaphane, increases its ubiquitination. Ubiquitination and subsequent degradation is most pronounced following prolonged exposure of cells to oxidative stress, particularly in glutathione-deficient cells that are highly susceptible to oxidative stress (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15379550}. Nucleus {ECO:0000269|PubMed:15379550}. Note=Shuttles between cytoplasm and nucleus. {ECO:0000250}. SUBUNIT: Homodimer. Forms a ternary complex with NFE2L2 and PGAM5. Interacts with the N-terminal regulatory domain of NFE2L2/NRF2. Interacts with BPTF and PTMA. Interacts with CUL3. Part of a complex that contains KEAP1, CUL3 and RBX1. Interacts indirectly with ENC1. Interacts with MAP1LC3B. Interacts with SESN1 and SESN2. Interacts with HSP90AA1 and HSP90AB1. {ECO:0000250|UniProtKB:Q14145}. DOMAIN: The Kelch repeats mediate interaction with NF2L2/NRF2, BPTF and PGAM5. {ECO:0000250}. +Q920G8 MFRN1_MOUSE Mitoferrin-1 (Mitochondrial iron transporter 1) (Mitochondrial solute carrier protein) (Solute carrier family 25 member 37) 338 37,510 Alternative sequence (8); Chain (1); Erroneous initiation (1); Frameshift (1); Repeat (3); Sequence conflict (3); Transmembrane (6) TRANSMEM 45 64 Helical; Name=1. {ECO:0000255}.; TRANSMEM 106 125 Helical; Name=2. {ECO:0000255}.; TRANSMEM 143 162 Helical; Name=3. {ECO:0000255}.; TRANSMEM 200 219 Helical; Name=4. {ECO:0000255}.; TRANSMEM 234 253 Helical; Name=5. {ECO:0000255}.; TRANSMEM 301 320 Helical; Name=6. {ECO:0000255}. FUNCTION: Mitochondrial iron transporter that specifically mediates iron uptake in developing erythroid cells, thereby playing an essential role in heme biosynthesis. The iron delivered into the mitochondria, presumably as Fe(2+), is then probably delivered to ferrochelatase to catalyze Fe(2+) incorporation into protoprophyrin IX to make heme. {ECO:0000269|PubMed:16511496}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in hematopoietic organs, fetal liver, bone marrow and spleen. {ECO:0000269|PubMed:11845285, ECO:0000269|PubMed:16511496}. +Q8R0Z5 MFRN2_MOUSE Mitoferrin-2 (Mitochondrial RNA-splicing protein 3/4 homolog) (MRS3/4) (Mitochondrial iron transporter 2) (Solute carrier family 25 member 28) 364 39,358 Alternative sequence (1); Chain (1); Repeat (3); Sequence conflict (1); Transmembrane (6) TRANSMEM 72 91 Helical; Name=1. {ECO:0000255}.; TRANSMEM 133 152 Helical; Name=2. {ECO:0000255}.; TRANSMEM 170 189 Helical; Name=3. {ECO:0000255}.; TRANSMEM 227 246 Helical; Name=4. {ECO:0000255}.; TRANSMEM 261 280 Helical; Name=5. {ECO:0000255}.; TRANSMEM 327 346 Helical; Name=6. {ECO:0000255}. FUNCTION: Mitochondrial iron transporter that mediates iron uptake. Probably required for heme synthesis of hemoproteins and Fe-S cluster assembly in non-erythroid cells. The iron delivered into the mitochondria, presumably as Fe(2+), is then probably delivered to ferrochelatase to catalyze Fe(2+) incorporation into protoprophyrin IX to make heme (Probable). {ECO:0000305|PubMed:11297739, ECO:0000305|PubMed:16511496}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:11297739}; Multi-pass membrane protein {ECO:0000269|PubMed:11297739}. Note=Isoform 1 and isoform 2 are both localized in the mitochondrion. TISSUE SPECIFICITY: Ubiquitously expressed at low level. Expressed at higher level in heart, liver, kidney and testis. Expression does not vary during erythroid maturation. {ECO:0000269|PubMed:11297739, ECO:0000269|PubMed:16511496}. +P28357 HXD9_MOUSE Homeobox protein Hox-D9 (Homeobox protein Hox-4.4) (Homeobox protein Hox-5.2) 339 34,992 Chain (1); Compositional bias (3); DNA binding (1) FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. SUBCELLULAR LOCATION: Nucleus. +P01811 HVM41_MOUSE Ig heavy chain V region UPC10 117 13,001 Chain (1); Domain (1); Non-terminal residue (1) +P0C1T1 HXB2_MOUSE Homeobox protein Hox-B2 (Homeobox protein Hox-2.8) 354 38,096 Chain (1); DNA binding (1); Modified residue (1); Motif (1) FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. SUBUNIT: Part of the nuclear protein complex gamma-globin promoter and enhancer binding factor (gamma-PE) composed at least by SATB1 and HOXB2. {ECO:0000250}. +Q9D379 HYEP_MOUSE Epoxide hydrolase 1 (EC 3.3.2.9) (Epoxide hydratase) (Microsomal epoxide hydrolase) (mEH) 455 52,577 Active site (3); Chain (1); Modified residue (3); Sequence conflict (1); Topological domain (1); Transmembrane (1) TRANSMEM 1 21 Helical; Signal-anchor for type III membrane protein. {ECO:0000255}. TOPO_DOM 22 455 Cytoplasmic. {ECO:0000250|UniProtKB:P07687}. FUNCTION: Biotransformation enzyme that catalyzes the hydrolysis of arene and aliphatic epoxides to less reactive and more water soluble dihydrodiols by the trans addition of water. May play a role in the metabolism of endogenous lipids such as epoxide-containing fatty acids. {ECO:0000250|UniProtKB:P07687}. SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250|UniProtKB:P07687}; Single-pass type III membrane protein {ECO:0000250|UniProtKB:P07687}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P07687}; Single-pass type III membrane protein {ECO:0000250|UniProtKB:P07687}. +P09023 HXB6_MOUSE Homeobox protein Hox-B6 (Homeobox protein Hox-2.2) (Homeobox protein MH-22A) 224 25,310 Chain (1); Compositional bias (1); DNA binding (1); Modified residue (1); Motif (1); Sequence conflict (1) FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. SUBCELLULAR LOCATION: Nucleus. +P18337 LYAM1_MOUSE L-selectin (CD62 antigen-like family member L) (Leukocyte adhesion molecule 1) (LAM-1) (Leukocyte-endothelial cell adhesion molecule 1) (LECAM1) (Lymph node homing receptor) (Lymphocyte antigen 22) (Ly-22) (Lymphocyte surface MEL-14 antigen) (CD antigen CD62L) 372 42,288 Chain (1); Disulfide bond (10); Domain (4); Glycosylation (10); Metal binding (5); Propeptide (1); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 333 355 Helical. {ECO:0000255}. TOPO_DOM 39 332 Extracellular. {ECO:0000255}.; TOPO_DOM 356 372 Cytoplasmic. {ECO:0000255}. FUNCTION: Calcium-dependent lectin that mediates cell adhesion by binding to glycoproteins on neighboring cells. Mediates the adherence of lymphocytes to endothelial cells of high endothelial venules in peripheral lymph nodes (PubMed:1693096). Promotes initial tethering and rolling of leukocytes in endothelia (By similarity). {ECO:0000250|UniProtKB:P14151, ECO:0000269|PubMed:1693096}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:P14151}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1693096, ECO:0000269|PubMed:2646713}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Interaction with SELPLG/PSGL1 and PODXL2 is required for promoting recruitment and rolling of leukocytes. This interaction is dependent on the sialyl Lewis X glycan modification of SELPLG and PODXL2, and tyrosine sulfation modifications of SELPLG. Sulfation on 'Tyr-51' of SELPLG is important for L-selectin binding. {ECO:0000250|UniProtKB:P14151}. TISSUE SPECIFICITY: Predominantly expressed in lymphoid tissue. {ECO:0000269|PubMed:2646713}. +Q01102 LYAM3_MOUSE P-selectin (CD62 antigen-like family member P) (Granule membrane protein 140) (GMP-140) (Leukocyte-endothelial cell adhesion molecule 3) (LECAM3) (Platelet activation dependent granule-external membrane protein) (PADGEM) (CD antigen CD62P) 768 83,099 Beta strand (1); Binding site (3); Chain (1); Disulfide bond (21); Domain (10); Glycosylation (5); Lipidation (2); Metal binding (5); Motif (1); Region (1); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 710 733 Helical. {ECO:0000255}. TOPO_DOM 42 709 Extracellular. {ECO:0000255}.; TOPO_DOM 734 768 Cytoplasmic. {ECO:0000255}. FUNCTION: Ca(2+)-dependent receptor for myeloid cells that binds to carbohydrates on neutrophils and monocytes. Mediates the interaction of activated endothelial cells or platelets with leukocytes. The ligand recognized is sialyl-Lewis X. Mediates rapid rolling of leukocyte rolling over vascular surfaces during the initial steps in inflammation through interaction with SELPLG. {ECO:0000250|UniProtKB:P16109, ECO:0000269|PubMed:12370362}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P16109}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P16109}. SUBUNIT: Interacts with SNX17. Interacts with SELPLG/PSGL1 and PODXL2 and mediates neutrophil adhesion and leukocyte rolling. This interaction requires the sialyl-Lewis X epitope of SELPLG and PODXL2, and specific tyrosine sulfation on SELPLG. {ECO:0000250|UniProtKB:P16109, ECO:0000269|PubMed:12393631}. TISSUE SPECIFICITY: Stored in the alpha-granules of platelets and Weibel-Palade bodies of endothelial cells. Upon cell activation by agonists, P-selectin is transported rapidly to the cell surface. +Q08288 LYAR_MOUSE Cell growth-regulating nucleolar protein (Ly1 antibody-reactive protein) (Protein expressed in male leptotene and zygotene spermatocytes 264) (MLZ-264) 388 43,736 Beta strand (4); Chain (1); Coiled coil (1); Compositional bias (1); Cross-link (2); Helix (2); Metal binding (8); Sequence conflict (6); Turn (2); Zinc finger (2) FUNCTION: Plays a role in the maintenance of the appropriate processing of 47S/45S pre-rRNA to 32S/30S pre-rRNAs and their subsequent processing to produce 18S and 28S rRNAs (By similarity). Also acts at the level of transcription regulation. Along with PRMT5, binds embryonic globin promoter (By similarity). Represses the expression of embryonic globin Hbb-y gene (PubMed:25092918). In neuroblastoma cells, may also repress the expression of oxidative stress genes, including CHAC1, HMOX1, SLC7A11, ULBP1 and that encoding the small nucleolar RNA SNORD41 (By similarity). Preferentially binds to a DNA motif containing 5'-GGTTAT-3' (By similarity). Stimulates phagocytosis of photoreceptor outer segments by retinal pigment epithelial cells (PubMed:25735755). Prevents NCL self-cleavage, maintaining a normal steady-state level of NCL protein in undifferentiated embryonic stem cells (ESCs), which in turn is essential for ESC self-renewal (PubMed:19489080). {ECO:0000250|UniProtKB:Q9NX58, ECO:0000269|PubMed:19489080, ECO:0000269|PubMed:25092918, ECO:0000269|PubMed:25735755}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:19489080, ECO:0000269|PubMed:23212345, ECO:0000269|PubMed:24990247, ECO:0000269|PubMed:8491376}. Cytoplasm {ECO:0000269|PubMed:24990247}. Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:25735755}. Note=Component of pre-ribosomal particles, including pre-40S, pre-60S and pre-90S (By similarity). Associated with cytoplasmic ribosomes, but not polysomes, as a component of the 60S subunit (PubMed:24990247). In the retina, predominantly expressed in photoreceptor outer segments (PubMed:25735755). In the nucleolus, colocalizes with nucleolin/NCL, therefore may reside in the dense fibrillar component (DFC) (PubMed:19489080). {ECO:0000250|UniProtKB:Q9NX58, ECO:0000269|PubMed:19489080, ECO:0000269|PubMed:24990247, ECO:0000269|PubMed:25735755}. SUBUNIT: Interacts with PRMT5; this interaction is direct (By similarity). Interacts with GNL2 and RPL23A (By similarity). Interacts with nucleolin/NCL; this interaction is direct (PubMed:19489080, PubMed:23212345). {ECO:0000250|UniProtKB:Q9NX58, ECO:0000269|PubMed:19489080, ECO:0000269|PubMed:23212345}. DOMAIN: The N-terminal zinc-finger domains are required for the appropriate production of 28S rRNA and the formation of pre-60S particles. {ECO:0000250|UniProtKB:Q9NX58}. TISSUE SPECIFICITY: Predominantly expressed in testis, in germ cells, and at a moderate level in spleen, liver and lung (at protein level) (PubMed:19489080, PubMed:23212345, PubMed:24990247). Very high levels in spermatogonia, spermatocytes and round spermatids, but not in testicular sperm and mature sperm (at protein level) (PubMed:20339383, PubMed:23212345, PubMed:24990247). Expressed in ovary (PubMed:20339383). Expressed in the retina, including in photoreceptor outer segments (at protein level) (PubMed:25735755). Expressed in undifferentiated embryonic stem cells (PubMed:19489080, PubMed:23212345). {ECO:0000269|PubMed:19489080, ECO:0000269|PubMed:20339383, ECO:0000269|PubMed:23212345, ECO:0000269|PubMed:24990247, ECO:0000269|PubMed:25735755}. +P70404 IDHG1_MOUSE Isocitrate dehydrogenase [NAD] subunit gamma 1, mitochondrial (Isocitric dehydrogenase subunit gamma) (NAD(+)-specific ICDH subunit gamma) 393 42,785 Binding site (8); Chain (1); Metal binding (1); Modified residue (3); Transit peptide (1) FUNCTION: Regulatory subunit which plays a role in the allosteric regulation of the enzyme catalyzing the decarboxylation of isocitrate (ICT) into alpha-ketoglutarate. The heterodimer composed of the alpha (IDH3A) and beta (IDH3B) subunits and the heterodimer composed of the alpha (IDH3A) and gamma (IDH3G) subunits, have considerable basal activity but the full activity of the heterotetramer (containing two subunits of IDH3A, one of IDH3B and one of IDH3G) requires the assembly and cooperative function of both heterodimers. {ECO:0000250|UniProtKB:P51553}. SUBCELLULAR LOCATION: Mitochondrion. SUBUNIT: Heterooligomer of subunits alpha (IDH3A), beta (IDH3B), and gamma (IDH3G) in the apparent ratio of 2:1:1. The heterodimer containing one IDH3A and one IDH3B subunit and the heterodimer containing one IDH3A and one IDH3G subunit assemble into a heterotetramer (which contains two subunits of IDH3A, one of IDH3B and one of IDH3G) and further into the heterooctamer. {ECO:0000250|UniProtKB:P51553}. +Q8BFZ6 IDI2_MOUSE Isopentenyl-diphosphate delta-isomerase 2 (EC 5.3.3.2) (Isopentenyl pyrophosphate isomerase 2) (IPP isomerase 2) (IPPI2) 227 26,665 Active site (2); Binding site (4); Chain (1); Domain (1); Metal binding (4); Motif (1); Sequence conflict (2) Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate: step 1/1. FUNCTION: Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). {ECO:0000250}. SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}. +O89113 IER5_MOUSE Immediate early response gene 5 protein 308 31,784 Chain (1) FUNCTION: Plays a role as a transcription factor. Mediates positive transcriptional regulation of several chaperone gene during the heat shock response in a HSF1-dependent manner. Mediates negative transcriptional regulation of CDC25B expression. Plays a role in the dephosphorylation of the heat shock factor HSF1 and ribosomal protein S6 kinase (S6K) by the protein phosphatase PP2A. Involved in the regulation of cell proliferation and resistance to thermal stress. Involved in the cell cycle checkpoint and survival in response to ionizing radiation. Associates with chromatin to the CDC25B promoter. {ECO:0000250|UniProtKB:Q5VY09}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5VY09}. Cytoplasm {ECO:0000250|UniProtKB:Q5VY09}. Note=Predominantly cytoplasmic. Translocated in the nucleus during heat shock. {ECO:0000250|UniProtKB:Q5VY09}. SUBUNIT: Monomer. Homodimer. Associates with the catalytic subunit of protein phosphatase PP2A. Interacts (via N- and C-terminal regions) with PPP2R2B. Interacts with PPP2R2A, PPP2R2C and PPP2R2D. Interacts (via N-terminus) with RPS6KB1. Interacts (via central region) with HSF1; this interaction promotes PPP2CA-induced HSF1 dephosphorylation, leading to enhanced HSF1 transcriptional activity. {ECO:0000250|UniProtKB:Q5VY09}. +Q8BVN8 IDLC_MOUSE Axonemal dynein light intermediate polypeptide 1 (Inner dynein arm light chain, axonemal) 258 29,680 Chain (1); Coiled coil (1) FUNCTION: May play a dynamic role in flagellar motility. {ECO:0000250}. SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000250|UniProtKB:O14645}. +Q8BLC3 LYPD1_MOUSE Ly6/PLAUR domain-containing protein 1 (Ly-6/neurotoxin-like protein 2) (Lynx2) 141 15,261 Chain (1); Disulfide bond (5); Domain (1); Glycosylation (1); Lipidation (1); Propeptide (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Believed to act as a modulator of nicotinic acetylcholine receptors (nAChRs) activity. In vitro increases receptor desensitization and decreases affinity for ACh of alpha-4:beta-2-containing nAChRs (PubMed:19246390). May play a role in the intracellular trafficking of alpha-4:beta-2 and alpha-7-containing nAChRs and may inhibit their expression at the cell surface (PubMed:26276394, PubMed:25716842). May be involved in the control of anxiety (PubMed:19246390). {ECO:0000269|PubMed:19246390, ECO:0000269|PubMed:25716842, ECO:0000269|PubMed:26276394}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}. SUBUNIT: Interacts with CHRNA4 and nAChRs containing alpha-4:beta-2 (CHRNA4:CHRNB2) and alpha-7 (CHRNA7) subunits. {ECO:0000269|PubMed:19246390, ECO:0000269|PubMed:25716842, ECO:0000269|PubMed:26276394}. TISSUE SPECIFICITY: Preferentially expressed in the nervous system. Expressed in embryonic and postnatal postmitotic central and peripheral neurons including subpopulations of motor neurons, sensory neurons, interneurons and neurons of the autonomous nervous system. Expressed around the growing nerves in the limb bud (PubMed:16236524). Expressed at high levels in specific brain regions such as the prefrontal cortex, amygdala, hippocampus, mediodorsal thalamus, dentate gyrus and specific brainstem nuclei (at protein level) (PubMed:19246390). {ECO:0000269|PubMed:16236524, ECO:0000269|PubMed:19246390}. +Q9DD23 LYPD2_MOUSE Ly6/PLAUR domain-containing protein 2 (Protein H8C4) 127 13,280 Chain (1); Domain (1); Glycosylation (1); Lipidation (1); Propeptide (1); Signal peptide (1) SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}. +Q91YK8 LYPD3_MOUSE Ly6/PLAUR domain-containing protein 3 (GPI-anchored metastasis-associated protein C4.4A homolog) 363 37,489 Chain (1); Compositional bias (1); Domain (2); Glycosylation (4); Lipidation (1); Propeptide (1); Signal peptide (1) FUNCTION: Supports cell migration. May be involved in tumor progression (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. SUBUNIT: Binds laminin-1 and laminin-5. Interacts with LGALS3. Interacts with AGR2 and AGR3 (By similarity). {ECO:0000250}. +Q8BVP6 LYPD4_MOUSE Ly6/PLAUR domain-containing protein 4 246 26,996 Chain (1); Domain (1); Glycosylation (1); Lipidation (1); Propeptide (1); Signal peptide (1) SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}. +Q9D7S0 LYPD8_MOUSE Ly6/PLAUR domain-containing protein 8 255 27,524 Chain (1); Domain (1); Glycosylation (13); Lipidation (1); Mutagenesis (13); Propeptide (1); Signal peptide (1) FUNCTION: Secreted protein specifically required to prevent invasion of Gram-negative bacteria in the inner mucus layer of the colon epithelium, a portion of the large intestine which is free of commensal microbiota. Prevents invasion of flagellated microbiota by binding to the flagellum of bacteria, such as P.mirabilis, thereby inhibiting bacterial motility in the intestinal lumen. Segregation of intestinal bacteria and epithelial cells in the colon is required to preserve intestinal homeostasis. {ECO:0000269|PubMed:27027293}. PTM: Highly N-glycosylated. Not O-glycosylated. {ECO:0000269|PubMed:27027293}.; PTM: GPI-anchored. The GPI-anchor is cleaved, leading to secretion into the colonic lumen. {ECO:0000269|PubMed:27027293}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:27027293}. Secreted {ECO:0000269|PubMed:27027293}. Note=Secreted into the lumen of the colon following cleavage of the GPI-anchor. {ECO:0000269|PubMed:27027293}. TISSUE SPECIFICITY: Specifically present in enterocytes located at the uppermost epithelial layer of the colon (at protein level). Exclusively expressed in the large intestine: specifically expressed on the apical surface of epithelial cells located at the uppermost layer of the colonic gland. {ECO:0000269|PubMed:27027293}. +Q8K215 LYRM4_MOUSE LYR motif-containing protein 4 91 10,855 Chain (1); Modified residue (1) Cofactor biosynthesis; iron-sulfur cluster biosynthesis. FUNCTION: Required for nuclear and mitochondrial iron-sulfur protein biosynthesis. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Interacts with FXN. Interaction is increased by nickel. Interaction is inhibited by calcium, magnesium, manganese, copper, cobalt, zinc, and iron. Forms a complex with the cytosolic/nuclear form of NFS1. The complex increased the stability of NFS1. {ECO:0000250}. +Q99L45 IF2B_MOUSE Eukaryotic translation initiation factor 2 subunit 2 (Eukaryotic translation initiation factor 2 subunit beta) (eIF-2-beta) 331 38,092 Chain (1); Compositional bias (3); Cross-link (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (10); Zinc finger (1) FUNCTION: eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form a 43S preinitiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by eIF-2B (By similarity). {ECO:0000250}. SUBUNIT: Heterotrimer composed of an alpha, a beta and a gamma chain (By similarity). Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5. {ECO:0000250, ECO:0000269|PubMed:16931514}. +Q91YJ5 IF2M_MOUSE Translation initiation factor IF-2, mitochondrial (IF-2(Mt)) (IF-2Mt) (IF2(mt)) 727 81,289 Beta strand (8); Chain (1); Domain (1); Modified residue (1); Nucleotide binding (3); Region (5); Sequence conflict (1); Transit peptide (1) FUNCTION: One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. +Q9CPN8 IF2B3_MOUSE Insulin-like growth factor 2 mRNA-binding protein 3 (IGF2 mRNA-binding protein 3) (IMP-3) (mIMP-3) (IGF-II mRNA-binding protein 3) (VICKZ family member 3) 579 63,575 Chain (1); Cross-link (2); Domain (6); Modified residue (3); Sequence conflict (3) FUNCTION: RNA-binding factor that may recruit target transcripts to cytoplasmic protein-RNA complexes (mRNPs). This transcript 'caging' into mRNPs allows mRNA transport and transient storage. It also modulates the rate and location at which target transcripts encounter the translational apparatus and shields them from endonuclease attacks or microRNA-mediated degradation. Binds to the 3'-UTR of CD44 mRNA and stabilizes it, hence promotes cell adhesion and invadopodia formation (By similarity). Binds to beta-actin/ACTB and MYC transcripts (By similarity). Binds to the 5'-UTR of the insulin-like growth factor 2 (IGF2) mRNAs. {ECO:0000250, ECO:0000269|PubMed:15753088}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11288142, ECO:0000269|PubMed:12921532}. Cytoplasm {ECO:0000250}. Note=Found in lamellipodia of the leading edge, in the perinuclear region, and beneath the plasma membrane. The subcytoplasmic localization is cell specific and regulated by cell contact and growth. Localized at the connecting piece and the tail of the spermatozoa. In response to cellular stress, such as oxidative stress, recruited to stress granules. {ECO:0000250}. SUBUNIT: Homodimer and multimer. Interacts with IGF2BP1 (By similarity). {ECO:0000250}. DOMAIN: All KH domains contribute binding to target mRNA. They are also required for RNA-dependent homo- and heterooligomerization. The integrity of KH domains seems not to be required for localization to stress granules (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in oocytes, spermatogonia and spermatocytes (at protein level). {ECO:0000269|PubMed:10525192, ECO:0000269|PubMed:12161597, ECO:0000269|PubMed:16049158}. +Q9CZD5 IF3M_MOUSE Translation initiation factor IF-3, mitochondrial (IF-3(Mt)) (IF-3Mt) (IF3(mt)) (IF3mt) 276 31,739 Beta strand (5); Chain (1); Helix (3); Propeptide (1); Sequence conflict (2); Transit peptide (1); Turn (1) FUNCTION: IF-3 binds to the 28S ribosomal subunit and shifts the equilibrum between 55S ribosomes and their 39S and 28S subunits in favor of the free subunits, thus enhancing the availability of 28S subunits on which protein synthesis initiation begins. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}. +Q8R3C0 MCMBP_MOUSE Mini-chromosome maintenance complex-binding protein (MCM-BP) (MCM-binding protein) 642 72,891 Chain (1); Modified residue (4) FUNCTION: Associated component of the MCM complex that acts as a regulator of DNA replication. Binds to the MCM complex during late S phase and promotes the disassembly of the MCM complex from chromatin, thereby acting as a key regulator of pre-replication complex (pre-RC) unloading from replicated DNA. Can dissociate the MCM complex without addition of ATP; probably acts by destabilizing interactions of each individual subunits of the MCM complex. Required for sister chromatid cohesion (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Associates with chromatin. Highly associated with chromatin in G1/S and S phases, reduced binding to chromatin in G2, and further decreased binding in early M phase. It then reassociates with chromatin in late M phase. Dissociates from chromatin later than component of the MCM complex (By similarity). {ECO:0000250}. SUBUNIT: Interacts with the MCM complex: associates with the MCM3-7 complex which lacks MCM2, while it does not interact with the MCM complex when MCM2 is present (MCM2-7 complex). Interacts with the RPA complex, when composed of all RPA1, RPA2 and RPA3 components, but not with RPA1 or RPA2 alone (By similarity). {ECO:0000250}. +E9Q956 MCMD2_MOUSE Minichromosome maintenance domain-containing protein 2 (MCM domain-containing protein 2) 681 76,015 Alternative sequence (3); Chain (1); Domain (1); Modified residue (1) FUNCTION: Plays an important role in meiotic recombination and associated DNA double-strand break repair. {ECO:0000269|PubMed:27760146, ECO:0000269|PubMed:27986806}. TISSUE SPECIFICITY: Predominantly expressed in the gonads and the brain. Not detected in the heart, lung, nor embryonic fibroblasts. {ECO:0000269|PubMed:27760146, ECO:0000269|PubMed:27986806}. +Q8BPT6 IMP2L_MOUSE Mitochondrial inner membrane protease subunit 2 (EC 3.4.21.-) (IMP2-like protein) 175 19,601 Active site (2); Chain (1); Sequence conflict (2); Transmembrane (1) TRANSMEM 19 37 Helical. {ECO:0000255}. FUNCTION: Catalyzes the removal of transit peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space. Known to process the nuclear encoded protein DIABLO (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. SUBUNIT: Heterodimer of 2 subunits, IMMPL1 and IMMPL2. {ECO:0000250}. +Q921Y2 IMP3_MOUSE U3 small nucleolar ribonucleoprotein protein IMP3 (U3 snoRNP protein IMP3) 184 21,777 Chain (1); Compositional bias (1); Domain (1) FUNCTION: Component of the 60-80S U3 small nucleolar ribonucleoprotein (U3 snoRNP). Required for the early cleavages during pre-18S ribosomal RNA processing (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. SUBUNIT: Component of a heterotrimeric complex containing IMP3, IMP4 and MPHOSPH10. Interacts with MPHOSPH10 (By similarity). {ECO:0000250}. +Q8VHZ7 IMP4_MOUSE U3 small nucleolar ribonucleoprotein protein IMP4 (U3 snoRNP protein IMP4) 291 33,656 Chain (1); Compositional bias (1); Domain (1); Frameshift (1); Sequence conflict (1) FUNCTION: Component of the 60-80S U3 small nucleolar ribonucleoprotein (U3 snoRNP). Required for the early cleavages during pre-18S ribosomal RNA processing (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. SUBUNIT: Component of a heterotrimeric complex containing IMP3, IMP4 and MPHOSPH10. Interacts with MPHOSPH10 (By similarity). {ECO:0000250}. +Q66JY2 IN80D_MOUSE INO80 complex subunit D 873 97,497 Alternative sequence (1); Chain (1); Cross-link (1); Erroneous initiation (1); Modified residue (1); Sequence caution (1); Sequence conflict (1) FUNCTION: Putative regulatory component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the chromatin remodeling INO80 complex; specifically part of a complex module associated with the N-terminus of INO80. {ECO:0000250}. +P24547 IMDH2_MOUSE Inosine-5'-monophosphate dehydrogenase 2 (IMP dehydrogenase 2) (IMPD 2) (IMPDH 2) (EC 1.1.1.205) (IMPDH-II) 514 55,815 Active site (2); Binding site (2); Chain (1); Cross-link (3); Domain (2); Metal binding (6); Modified residue (5); Natural variant (2); Nucleotide binding (2); Region (3); Sequence conflict (3) Purine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1. FUNCTION: Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Could also have a single-stranded nucleic acid-binding activity and could play a role in RNA and/or DNA metabolism. It may also have a role in the development of malignancy and the growth progression of some tumors. {ECO:0000255|HAMAP-Rule:MF_03156}. PTM: Acetylated by CLOCK in a circadian manner. {ECO:0000250|UniProtKB:P12268}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03156}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03156}. SUBUNIT: Homotetramer. Interacts with CLOCK; in a circadian manner. {ECO:0000250|UniProtKB:P12268}. +A2AGH6 MED12_MOUSE Mediator of RNA polymerase II transcription subunit 12 (Mediator complex subunit 12) (OPA-containing protein) (Thyroid hormone receptor-associated protein complex 230 kDa component) (Trap230) (Trinucleotide repeat-containing gene 11 protein) 2190 244,561 Alternative sequence (4); Chain (1); Erroneous initiation (1); Modified residue (14); Region (1); Sequence conflict (3) FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. This subunit may specifically regulate transcription of targets of the Wnt signaling pathway and SHH signaling pathway (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Component of the Mediator complex, which is composed of MED1, MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L, MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23, MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8 subunits form a distinct module termed the CDK8 module. Mediator containing the CDK8 module is less active than Mediator lacking this module in supporting transcriptional activation. Individual preparations of the Mediator complex lacking one or more distinct subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and TRAP. Also interacts with CTNNB1 and GLI3 (By similarity). {ECO:0000250}. +Q8C1S0 MED19_MOUSE Mediator of RNA polymerase II transcription subunit 19 (Mediator complex subunit 19) 244 26,263 Chain (1); Compositional bias (2); Modified residue (2); Sequence conflict (1) FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Component of the Mediator complex, which is composed of MED1, MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L, MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23, MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8 subunits form a distinct module termed the CDK8 module. Mediator containing the CDK8 module is less active than Mediator lacking this module in supporting transcriptional activation. Individual preparations of the Mediator complex lacking one or more distinct subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and TRAP (By similarity). {ECO:0000250}. +Q61845 MEIG1_MOUSE Meiosis-expressed gene 1 protein (Protein expressed in male leptotene and zygotene spermatocytes 278) (MLZ-278) 88 10,823 Beta strand (4); Chain (1); Helix (3); Turn (1) FUNCTION: Essential for spermiogenesis. {ECO:0000269|PubMed:1390336, ECO:0000269|PubMed:19805151}. SUBUNIT: Interacts with PACRG. {ECO:0000269|PubMed:19805151}. TISSUE SPECIFICITY: Several isoforms have been identified differing in their 5'-untranslated exons. These isoforms show different tissue expression. Some are expressed in various tissues, including lung, liver, brain, testis, oviduct and oocytes. Some are testis-specific. {ECO:0000269|PubMed:1390336, ECO:0000269|PubMed:19805151, ECO:0000269|PubMed:20339383}. +Q9D513 MEIOB_MOUSE Meiosis-specific with OB domain-containing protein (EC 3.1.-.-) (Protein expressed in male leptotene and zygotene spermatocytes 675) (MLZ-675) 470 52,975 Chain (1); DNA binding (1); Erroneous initiation (3); Mutagenesis (2) FUNCTION: Single-stranded DNA-binding protein required for homologous recombination in meiosis I. Required for double strand breaks (DSBs) repair and crossover formation and promotion of faithful and complete synapsis. Not required for the initial loading of recombinases but required to maintain a proper number of RAD51 and DMC1 foci after the zygotene stage. May act by ensuring the stabilization of recombinases, which is required for successful homology search and meiotic recombination. Displays Single-stranded DNA 3'-5' exonuclease activity in vitro. {ECO:0000269|PubMed:20339383, ECO:0000269|PubMed:24068956, ECO:0000269|PubMed:24240703}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Chromosome. Note=Co-localizes with the RPA complex on meiotic chromosome axes. Accumulates on resected DNA. Localization is dependent on SPATA22. SUBUNIT: Component of a multiprotein complex with RPA2 and SPATA22. TISSUE SPECIFICITY: Sprecifically expressed in early meiotic germ cells: in adult and fetal tissues, detected in fetal ovary, postnatal testis and liver. In the ovary, expression starts at 12.5 dpc, reaches a maximum at 15.5 dpc and decreases to become undetectable in post natal life. In testis, expression starts at 10 days post partum (dpp), reaches a maximum at 20 dpp and is maintained throughout adult life. {ECO:0000269|PubMed:24068956, ECO:0000269|PubMed:24240703}. +Q60954 MEIS1_MOUSE Homeobox protein Meis1 (Myeloid ecotropic viral integration site 1) 390 43,002 Alternative sequence (2); Chain (1); Compositional bias (3); DNA binding (1); Mutagenesis (2); Region (2) FUNCTION: Acts as a transcriptional regulator of PAX6. Also acts as a transcriptional activator of PF4 in complex with PBX1 or PBX2. Required for hematopoiesis, megakaryocyte lineage development and vascular patterning. May function as a cofactor for HOXA7 and HOXA9 in the induction of myeloid leukemias. {ECO:0000269|PubMed:12183364, ECO:0000269|PubMed:15882575}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:10082572, ECO:0000269|PubMed:15882575}. SUBUNIT: Interacts with the N-terminal region of PBX1 to form a heterodimer which binds DNA including a cAMP-responsive sequence in CYP17. Also forms heterodimers with PBX2. Forms heterotrimers with PBX1 or PBX2 and a number of HOX proteins including HOXA9, HOXD4 and HOXD9 where it acts as a non-DNA-binding partner. Also forms heterotrimers with PBX1 and HOX proteins including HOXD9 and HOXD10 where PBX1 is the non-DNA-binding partner. Heterodimer with DLX3. Heterodimer with HOXB13 (By similarity). {ECO:0000250|UniProtKB:O00470, ECO:0000269|PubMed:10082572, ECO:0000269|PubMed:10523646, ECO:0000269|PubMed:9315626, ECO:0000269|PubMed:9525891}. TISSUE SPECIFICITY: Expressed at high levels in the lung with lower levels detected in the heart and brain. Expressed in pancreatic islets (beta-cells and non-beta-cells) (PubMed:21059917). {ECO:0000269|PubMed:21059917}. DISEASE: Note=Meis1 serves as a site of viral integration in 15% of the tumors arising in BXH-2 mice that develop myeloid leukemia as a result of the expression of an ecotropic murine leukemia virus. {ECO:0000269|PubMed:7565694}. +A1A535 MELT_MOUSE Ventricular zone-expressed PH domain-containing protein 1 (Protein melted homolog) 833 94,502 Alternative sequence (1); Chain (1); Domain (1); Region (2); Sequence conflict (9) FUNCTION: Interacts with TGF-beta receptor type-1 (TGFBR1) and inhibits dissociation of activated SMAD2 from TGFBR1, impeding its nuclear accumulation and resulting in impaired TGF-beta signaling. May also affect FOXO, Hippo and Wnt signaling. {ECO:0000250|UniProtKB:Q14D04}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q14D04}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9VS24}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9VS24}. SUBUNIT: Interacts with TGFBR1. {ECO:0000250|UniProtKB:Q14D04}. DOMAIN: The PH domain is required for membrane targeting. {ECO:0000250}. TISSUE SPECIFICITY: Specifically expressed in kidney and eye. In the eye, expressed in retinal pigmented epithelium but not in the neural retina. {ECO:0000269|PubMed:15388229}. +Q91VH6 MEMO1_MOUSE Protein MEMO1 (Mediator of ErbB2-driven cell motility 1) (Memo-1) 297 33,692 Chain (1); Modified residue (1) FUNCTION: May control cell migration by relaying extracellular chemotactic signals to the microtubule cytoskeleton. Mediator of ERBB2 signaling. The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization (By similarity). {ECO:0000250}. SUBUNIT: Interacts with ERBB2 phosphorylated on 'Tyr-1249'. {ECO:0000250}. +A1A546 ISX_MOUSE Intestine-specific homeobox 240 27,169 Alternative sequence (1); Chain (1); DNA binding (1); Sequence conflict (1) FUNCTION: Transcription factor that regulates gene expression in intestine. May participate in vitamin A metabolism most likely by regulating BCO1 expression in the intestine. {ECO:0000269|PubMed:16971476, ECO:0000269|PubMed:18093975}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. TISSUE SPECIFICITY: Expressed in intestinal epithelial cells from the duodenum to the proximal colon. {ECO:0000269|PubMed:16971476, ECO:0000269|PubMed:18093975}. +P61622 ITA11_MOUSE Integrin alpha-11 1188 133,012 Calcium binding (3); Chain (1); Disulfide bond (7); Domain (1); Glycosylation (16); Repeat (7); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1142 1164 Helical. {ECO:0000255}. TOPO_DOM 23 1141 Extracellular. {ECO:0000255}.; TOPO_DOM 1165 1188 Cytoplasmic. {ECO:0000255}. FUNCTION: Integrin alpha-11/beta-1 is a receptor for collagen. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Heterodimer of an alpha and a beta subunit. Alpha-11 associates with beta-1 (By similarity). Interacts with RAB21 (By similarity). {ECO:0000250}. DOMAIN: The integrin I-domain (insert) is a VWFA domain. Integrins with I-domains do not undergo protease cleavage. +O70309 ITB5_MOUSE Integrin beta-5 798 87,909 Alternative sequence (1); Chain (1); Disulfide bond (28); Domain (2); Glycosylation (7); Modified residue (1); Region (1); Repeat (4); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 720 742 Helical. {ECO:0000255}. TOPO_DOM 24 719 Extracellular. {ECO:0000255}.; TOPO_DOM 743 798 Cytoplasmic. {ECO:0000255}. FUNCTION: Integrin alpha-V/beta-5 (ITGAV:ITGB5) is a receptor for fibronectin. It recognizes the sequence R-G-D in its ligand. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Heterodimer of an alpha and a beta subunit. Beta-5 (ITGB5) associates with alpha-V (ITGAV) (Probable). Interacts with MYO10 (By similarity). Interacts with DAB2. Integrin ITGAV:ITGB5 interacts with FBLN5 (via N-terminus) (PubMed:11805835). ITGAV:ITGB5 interacts with CCN3 (By similarity). {ECO:0000250|UniProtKB:P18084, ECO:0000269|PubMed:11805835, ECO:0000269|PubMed:12606711, ECO:0000305|PubMed:11805835}. +Q9Z0T9 ITB6_MOUSE Integrin beta-6 787 86,042 Chain (1); Disulfide bond (28); Domain (1); Glycosylation (9); Region (2); Repeat (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 709 729 Helical. {ECO:0000255}. TOPO_DOM 22 708 Extracellular. {ECO:0000255}.; TOPO_DOM 730 787 Cytoplasmic. {ECO:0000255}. FUNCTION: Integrin alpha-V:beta-6 (ITGAV:ITGB6) is a receptor for fibronectin and cytotactin (By similarity). It recognizes the sequence R-G-D in its ligands (PubMed:10025398). ITGAV:ITGB6 acts as a receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell adhesion to FBN1 (By similarity). Integrin alpha-V:beta-6 (ITGAV:ITGB6) mediates R-G-D-dependent release of transforming growth factor beta-1 (TGF-beta-1) from regulatory Latency-associated peptide (LAP), thereby playing a key role in TGF-beta-1 activation (PubMed:10025398). {ECO:0000250|UniProtKB:P18564, ECO:0000269|PubMed:10025398}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. Cell junction, focal adhesion {ECO:0000250|UniProtKB:P18564}. SUBUNIT: Heterodimer of an alpha and a beta subunit (PubMed:10025398). Interacts with FLNB (By similarity). Interacts with HAX1 (By similarity). ITGAV:ITGB6 interacts with FBN1 (By similarity). ITGAV:ITGB6 interacts with TGFB1 (PubMed:10025398). {ECO:0000250|UniProtKB:P18564, ECO:0000269|PubMed:10025398}. +P11688 ITA5_MOUSE Integrin alpha-5 (CD49 antigen-like family member E) (Fibronectin receptor subunit alpha) (Integrin alpha-F) (VLA-5) (CD antigen CD49e) [Cleaved into: Integrin alpha-5 heavy chain; Integrin alpha-5 light chain] 1053 115,043 Binding site (2); Calcium binding (4); Chain (3); Disulfide bond (9); Glycosylation (14); Metal binding (20); Modified residue (1); Motif (1); Repeat (7); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1000 1025 Helical. {ECO:0000255}. TOPO_DOM 45 999 Extracellular. {ECO:0000255}.; TOPO_DOM 1026 1053 Cytoplasmic. {ECO:0000255}. FUNCTION: Integrin alpha-5/beta-1 (ITGA5:ITGB1) is a receptor for fibronectin and fibrinogen. It recognizes the sequence R-G-D in its ligands. ITGA5:ITGB1 binds to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational changes and enhanced ligand binding to site 1. ITGA5:ITGB1 acts as a receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell adhesion to FBN1. ITGA5:ITGB1 is a receptor for IL1B and binding is essential for IL1B signaling. {ECO:0000250|UniProtKB:P08648}. PTM: Proteolytic cleavage by PCSK5 mediates activation of the precursor. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. Cell junction, focal adhesion {ECO:0000250|UniProtKB:P08648}. Cell surface {ECO:0000250|UniProtKB:P08648}. SUBUNIT: Heterodimer of an alpha and a beta subunit. The alpha subunit is composed of a heavy and a light chain linked by a disulfide bond. Alpha-5 associates with beta-1. Interacts with NISCH (PubMed:11121431, PubMed:14535848, PubMed:15229651). Interacts with HPS5 (By similarity). Interacts with RAB21 and COMP. Interacts with CIB1 (By similarity). ITGA5:ITGB1 interacts with CCN3 (By similarity). ITGA5:ITGB1 interacts with FBN1 (By similarity). ITGA5:ITGB1 interacts with IL1B (By similarity). {ECO:0000250|UniProtKB:P08648, ECO:0000269|PubMed:11121431, ECO:0000269|PubMed:14535848, ECO:0000269|PubMed:15229651}. +Q9QUM0 ITA2B_MOUSE Integrin alpha-IIb (GPalpha IIb) (GPIIb) (Platelet membrane glycoprotein IIb) (CD antigen CD41) [Cleaved into: Integrin alpha-IIb heavy chain; Integrin alpha-IIb light chain] 1033 112,678 Calcium binding (4); Chain (3); Disulfide bond (9); Glycosylation (5); Motif (1); Repeat (7); Sequence conflict (16); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 989 1014 Helical. {ECO:0000255}. TOPO_DOM 32 988 Extracellular. {ECO:0000255}.; TOPO_DOM 1015 1033 Cytoplasmic. {ECO:0000255}. FUNCTION: Integrin alpha-IIb/beta-3 is a receptor for fibronectin, fibrinogen, plasminogen, prothrombin, thrombospondin and vitronectin. It recognizes the sequence R-G-D in a wide array of ligands. It recognizes the sequence H-H-L-G-G-G-A-K-Q-A-G-D-V in fibrinogen gamma chain. Following activation integrin alpha-IIb/beta-3 brings about platelet/platelet interaction through binding of soluble fibrinogen. This step leads to rapid platelet aggregation which physically plugs ruptured endothelial cell surface. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Heterodimer of an alpha and a beta subunit. The alpha subunit is composed of a heavy and a light chain linked by a disulfide bond. Alpha-IIb associates with beta-3. Directly interacts with RNF181. Interacts (via C-terminus cytoplasmic tail region) with CIB1; the interaction is direct and calcium-dependent. Interacts (via C-terminus cytoplasmic tail region) with CIB2, CIB3 and CIB4; the interactions are stabilized/increased in a calcium and magnesium-dependent manner (By similarity). {ECO:0000250}. +O35671 ITBP1_MOUSE Integrin beta-1-binding protein 1 (Bodenin) 200 21,644 Chain (1); Compositional bias (1); Domain (1); Modified residue (2); Motif (1); Region (2) FUNCTION: Key regulator of the integrin-mediated cell-matrix interaction signaling by binding to the ITGB1 cytoplasmic tail and preventing the activation of integrin alpha-5/beta-1 (heterodimer of ITGA5 and ITGB1) by talin or FERMT1. Plays a role in cell proliferation, differentiation, spreading, adhesion and migration in the context of mineralization and bone development and angiogenesis. Stimulates cellular proliferation in a fibronectin-dependent manner. Involved in the regulation of beta-1 integrin-containing focal adhesion (FA) site dynamics by controlling its assembly rate during cell adhesion; inhibits beta-1 integrin clustering within FA by directly competing with talin TLN1, and hence stimulates osteoblast spreading and migration in a fibronectin-and/or collagen-dependent manner. Acts as a guanine nucleotide dissociation inhibitor (GDI) by regulating Rho family GTPases during integrin-mediated cell matrix adhesion; reduces the level of active GTP-bound form of both CDC42 and RAC1 GTPases upon cell adhesion to fibronectin. Stimulates the release of active CDC42 from the membranes to maintain it in an inactive cytoplasmic pool. Participates in the translocation of the Rho-associated protein kinase ROCK1 to membrane ruffles at cell leading edges of the cell membrane, leading to an increase of myoblast cell migration on laminin. Plays a role in bone mineralization at a late stage of osteoblast differentiation; modulates the dynamic formation of focal adhesions into fibrillar adhesions, which are adhesive structures responsible for fibronectin deposition and fibrillogenesis. Plays a role in blood vessel development; acts as a negative regulator of angiogenesis by attenuating endothelial cell proliferation and migration, lumen formation and sprouting angiogenesis by promoting AKT phosphorylation and inhibiting ERK1/2 phosphorylation through activation of the Notch signaling pathway. Promotes transcriptional activity of the MYC promoter. {ECO:0000269|PubMed:16741948, ECO:0000269|PubMed:17567669, ECO:0000269|PubMed:17654484, ECO:0000269|PubMed:18227284, ECO:0000269|PubMed:21768292}. PTM: Phosphorylation at Thr-38 seems to enhance integrin alpha5beta1-mediated cell adhesion. The degree of phosphorylation is regulated by integrin-dependent cell-matrix interaction (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16741948}. Cell membrane {ECO:0000269|PubMed:16741948}. Cell projection, lamellipodium {ECO:0000269|PubMed:16741948}. Cell projection, ruffle {ECO:0000269|PubMed:16741948}. Note=Nucleocytoplasmic shuttling protein; shuttles between nucleus and cytoplasm in a integrin-dependent manner; probably sequestered in the cytosol by ITGB1. Its localization is dependent on the stage of cell spreading on fibronectin; cytoplasmic in case of round cells, corresponding to the initial step of cell spreading, or nuclear in case of well spread cells. Colocalizes with ROCK1 and NME2 at beta-1 integrin engagement sites. Together with ITGB1 and NME2 is recruited to beta-1 integrin-rich peripheral ruffles and lamellipodia during initial cell spreading on fibronectin and/or collagen (By similarity). {ECO:0000250}. SUBUNIT: Found in a complex, at least composed of ITGB1BP1, KRIT1 and RAP1A. Interacts (via C-terminal region) with ITGB1 (via C-terminal cytoplasmic tail); the interaction prevents talin TLN1 binding to ITGB1 and KRIT1 and ITGB1 compete for the same binding site. Interacts with KRIT1 (via N-terminal NPXY motif); the interaction induces the opening conformation of KRIT1 and KRIT1 and ITGB1 compete for the same binding site. Isoform 2 does not interact with ITGB1. Interacts with CDC42 (GTP- or GDP-bound form); the interaction is increased with the CDC42-membrane bound forms and prevents both CDC42 activation and cell spreading. Interacts (via C-terminal domain region) with NME2. Interacts with FERMT2 and RAC1 (By similarity). Interacts (via N-terminus and PTB domain) with ROCK1. {ECO:0000250, ECO:0000269|PubMed:16741948, ECO:0000269|PubMed:17654484}. TISSUE SPECIFICITY: Expressed in the brain. +P56477 IRF5_MOUSE Interferon regulatory factor 5 (IRF-5) 497 56,005 Chain (1); Compositional bias (2); Cross-link (2); DNA binding (1); Modified residue (6); Motif (2) FUNCTION: Transcription factor involved in the induction of interferons IFNA and INFB and inflammatory cytokines upon virus infection. Activated by TLR7 or TLR8 signaling (By similarity). {ECO:0000250}. PTM: 'Lys-63'-linked polyubiquitination by TRAF6 is required for activation. {ECO:0000269|PubMed:18824541}.; PTM: Phosphorylation of serine and threonine residues in a C-terminal autoinhibitory region, stimulates dimerization, transport into the nucleus, assembly with the coactivator CBP/p300 and initiation of transcription. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18824541}. Nucleus {ECO:0000269|PubMed:18824541}. Note=Shuttles between the nucleus and the cytoplasm. SUBUNIT: Homodimer, when phosphorylated. {ECO:0000250}. +P97431 IRF6_MOUSE Interferon regulatory factor 6 (IRF-6) 467 53,111 Chain (1); DNA binding (1); Mutagenesis (1); Sequence conflict (1) FUNCTION: Probable DNA-binding transcriptional activator. Key determinant of the keratinocyte proliferation-differentiation switch involved in appropriate epidermal development. Plays a role in regulating mammary epithelial cell proliferation. May regulate WDR65 transcription. {ECO:0000269|PubMed:17041603, ECO:0000269|PubMed:18212048, ECO:0000269|PubMed:19036739, ECO:0000269|PubMed:21574244}. PTM: Phosphorylated. Phosphorylation status depends on the cell cycle and is a signal for ubiquitination and proteasome-mediated degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:19036739}. Note=Translocates to nucleus in response to an activating signal. {ECO:0000305}. SUBUNIT: Interacts with SERPINB5. {ECO:0000250}. TISSUE SPECIFICITY: High levels of expression along the medial edge of the fusing palate, tooth buds, hair follicles, genitalia and skin. {ECO:0000269|PubMed:12219090}. +P35569 IRS1_MOUSE Insulin receptor substrate 1 (IRS-1) 1233 130,723 Chain (1); Compositional bias (4); Domain (2); Modified residue (27); Motif (9); Region (2); Sequence conflict (2) FUNCTION: May mediate the control of various cellular processes by insulin. When phosphorylated by the insulin receptor binds specifically to various cellular proteins containing SH2 domains such as phosphatidylinositol 3-kinase p85 subunit or GRB2. Activates phosphatidylinositol 3-kinase when bound to the regulatory p85 subunit (By similarity). {ECO:0000250}. PTM: Serine phosphorylation of IRS1 is a mechanism for insulin resistance. Ser-307 phosphorylation inhibits insulin action through disruption of IRS1 interaction with the insulin receptor (By similarity). Phosphorylation of Tyr-891 is required for GRB2-binding (By similarity). Phosphorylated by ALK. Phosphorylated at Ser-265, Ser-302, Ser-632 and Ser-1097 by RPS6KB1; phosphorylation induces accelerated degradation of IRS1 (By similarity). Phosphorylated on tyrosine residues in response to insulin (PubMed:25586176). {ECO:0000250|UniProtKB:P35568, ECO:0000250|UniProtKB:P35570, ECO:0000269|PubMed:25586176}.; PTM: Ubiquitinated by the Cul7-RING(FBXW8) complex in a mTOR-dependent manner, leading to its degradation: the Cul7-RING(FBXW8) complex recognizes and binds IRS1 previously phosphorylated by S6 kinase (RPS6KB1 or RPS6KB2). {ECO:0000250}. SUBUNIT: Interacts (via phosphorylated YXXM motifs) with PIK3R1 (By similarity). Interacts with ROCK1 (By similarity). Interacts with GRB2 (By similarity). Interacts with SOCS7 (By similarity). Interacts (via IRS-type PTB domain) with IGF1R and INSR (via the tyrosine-phosphorylated NPXY motif) (By similarity). Interacts with UBTF and PIK3CA (PubMed:15197263). Interacts (via PH domain) with PHIP (PubMed:11018022). Interacts with FER (PubMed:11006284). Interacts with ALK (By similarity). Interacts with EIF2AK2/PKR (PubMed:22948222). Interacts with GKAP1 (PubMed:25586176). Interacts with DGKZ in the absence of insulin; insulin stimulation decreases this interaction (PubMed:27739494). Found in a ternary complex with DGKZ and PIP5K1A in the absence of insulin stimulation (PubMed:27739494). {ECO:0000250|UniProtKB:P35568, ECO:0000250|UniProtKB:P35570, ECO:0000269|PubMed:11006284, ECO:0000269|PubMed:11018022, ECO:0000269|PubMed:15197263, ECO:0000269|PubMed:22948222, ECO:0000269|PubMed:25586176, ECO:0000269|PubMed:27739494}. TISSUE SPECIFICITY: Expressed in osteoblasts, but not in osteoclasts. {ECO:0000269|PubMed:10749573}. +P81122 IRS2_MOUSE Insulin receptor substrate 2 (IRS-2) (4PS) 1321 136,763 Beta strand (1); Chain (1); Compositional bias (4); Domain (2); Helix (1); Modified residue (43); Motif (7); Sequence conflict (8) FUNCTION: May mediate the control of various cellular processes by insulin. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:17636024}. SUBUNIT: Interacts with PHIP. {ECO:0000269|PubMed:11018022}. TISSUE SPECIFICITY: Skeletal muscle, lung, brain, liver, kidney, heart and spleen. +P81066 IRX2_MOUSE Iroquois-class homeodomain protein IRX-2 (Homeodomain protein IRXA2) (Iroquois homeobox protein 2) (Iroquois-class homeobox protein Irx6) 474 49,484 Chain (1); Compositional bias (1); DNA binding (1); Frameshift (1); Modified residue (1); Sequence conflict (2) SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: Expressed in specific and overlapping patterns with Irx1 and Irx3 in the developing and adult metanephric kidney. In the adult metanephros, renal expression is found in the loop of Henle in the S3 proximal tubule segment and in the thick ascending limb (TAL) of the distal tubule. {ECO:0000269|PubMed:17875669}. +Q60766 IRGM1_MOUSE Immunity-related GTPase family M protein 1 (EC 3.6.5.-) (Interferon-inducible GTPase 3) (Interferon-inducible protein 1) (LPS-stimulated RAW 264.7 macrophage protein 47) (LRG-47) 409 46,552 Alternative sequence (1); Chain (1); Domain (1); Modified residue (1); Mutagenesis (13); Nucleotide binding (4); Region (2); Sequence conflict (1) FUNCTION: Putative GTPase which is required for IFNG-mediated clearance of acute protozoan and bacterial infections. Functions in innate immune response probably through regulation of autophagy. May regulate proinflammatory cytokine production and prevent endotoxemia upon infection. Required for macrophage motility and possibly also for adhesion. {ECO:0000269|PubMed:11457893, ECO:0000269|PubMed:14576437, ECO:0000269|PubMed:14707092, ECO:0000269|PubMed:15607973, ECO:0000269|PubMed:15908352, ECO:0000269|PubMed:16339555, ECO:0000269|PubMed:17911638, ECO:0000269|PubMed:17982087, ECO:0000269|PubMed:19920210}. SUBCELLULAR LOCATION: Golgi apparatus membrane. Cell membrane. Cytoplasmic vesicle, phagosome membrane. Cytoplasmic vesicle, autophagosome membrane. Lysosome membrane. Late endosome membrane. Cell projection, phagocytic cup. Note=Behaves like an integral membrane protein. Recruited to the plasma membrane around forming phagocytic cups, it remains associated with maturing phagosomes. Association with phagosomes is dependent on nucleotide-binding but is IFNG-independent. Preferentially associated with cis- and medial-Golgi. Also detected in late endosomes and lysosomes. TISSUE SPECIFICITY: Expressed in lung and primary macrophages. {ECO:0000269|PubMed:14576437}. +Q9DCC7 ISC2B_MOUSE Isochorismatase domain-containing protein 2B 210 23,151 Chain (1); Modified residue (1); Sequence conflict (2) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Localizes to the nucleus in the presence of CDKN2A. {ECO:0000250}. SUBUNIT: Interacts with CDKN2A. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. Expressed predominantly in uterus, stomach and urinary tract. {ECO:0000269|PubMed:17658461}. +Q9D067 MDM1_MOUSE Nuclear protein MDM1 (Mdm4 transformed 3T3 cell double minute 1 protein) (Mouse double minute 1) 708 79,689 Alternative sequence (5); Chain (1); Coiled coil (1); Modified residue (9); Motif (4); Sequence conflict (5) FUNCTION: Microtubule-binding protein that negatively regulates centriole duplication. Binds to and stabilizes microtubules. {ECO:0000250|UniProtKB:Q8TC05}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:3182840}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q8TC05}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:26337392}. Note=Localizes to the centriole lumen. {ECO:0000269|PubMed:26337392}. TISSUE SPECIFICITY: Widely expressed. Expressed at high levels in the testis. {ECO:0000269|PubMed:3182840}. +P61372 ISL1_MOUSE Insulin gene enhancer protein ISL-1 (Islet-1) 349 39,036 Alternative sequence (1); Beta strand (9); Chain (1); Compositional bias (1); DNA binding (1); Domain (2); Helix (4); Region (1); Turn (6) FUNCTION: DNA-binding transcriptional activator (PubMed:14664703, PubMed:24643061, PubMed:25775587, PubMed:22343712). Recognizes and binds to the consensus octamer binding site 5'-ATAATTAA-3' in promoter of target genes (PubMed:24643061, PubMed:25775587). Plays a fundamental role in the gene regulatory network essential for retinal ganglion cell (RGC) differentiation (PubMed:25775587). Cooperates with the transcription factor POU4F2 to achieve maximal levels of expression of RGC target genes and RGC fate specification in the developing retina (PubMed:24643061, PubMed:25775587). Involved in the specification of motor neurons in cooperation with LHX3 and LDB1 (PubMed:18583962). Binds to insulin gene enhancer sequences (By similarity). Essential for heart development. Marker of one progenitor cell population that give rise to the outflow tract, right ventricle, a subset of left ventricular cells, and a large number of atrial cells as well, its function is required for these progenitors to contribute to the heart. Controls the expression of FGF and BMP growth factors in this cell population and is required for proliferation and survival of cells within pharyngeal foregut endoderm and adjacent splanchnic mesoderm as well as for migration of cardiac progenitors into the heart (PubMed:14667410). {ECO:0000250|UniProtKB:P61374, ECO:0000269|PubMed:14664703, ECO:0000269|PubMed:14667410, ECO:0000269|PubMed:18583962, ECO:0000269|PubMed:22343712, ECO:0000269|PubMed:24643061, ECO:0000269|PubMed:25775587}. PTM: Isoform 1 is phosphorylated. {ECO:0000269|PubMed:14664703}. SUBCELLULAR LOCATION: Isoform 1: Nucleus {ECO:0000269|PubMed:14664703}.; SUBCELLULAR LOCATION: Isoform 2: Nucleus {ECO:0000269|PubMed:14664703}. SUBUNIT: At neuronal promoters, displaces LDB1 from LHX3 LIM domain to form a ternary complex in which ISL1 contacts both LHX3 and LDB1 (PubMed:18583962). Interacts (via C-terminus) with POU4F2 (via C-terminus) isoform 1 (PubMed:24643061). Interacts with POU3F2 (PubMed:24643061). Interacts with POU4F3 (PubMed:24643061). Interacts (via N-terminal domain) with MLIP; the interaction represses ISL1 transactivator activity (PubMed:22343712). {ECO:0000269|PubMed:18583962, ECO:0000269|PubMed:22343712, ECO:0000269|PubMed:24643061}. +Q3UTS8 ISK13_MOUSE Serine protease inhibitor Kazal-type 13 (Serine protease inhibitor Kazal-type 5-like 3) 97 11,530 Chain (1); Disulfide bond (3); Domain (1); Glycosylation (1); Signal peptide (1); Site (1) FUNCTION: May be a serine protease inhibitor (By similarity). Essential for sperm maturation and fertility. Inhibits sperm acrosome reaction, protecting sperm from premature reaction (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Secreted into the lumen of the initial segment of the epididymis and binds to sperm. In the initial segment of epididymis, localizes on the dorsal surface of the acrosomal region of sperm, gradually becomes more restricted to the acrosomal region in spermatozoa during epididymal transit (By similarity). {ECO:0000250}. +P21440 MDR3_MOUSE Phosphatidylcholine translocator ABCB4 (ATP-binding cassette sub-family B member 4) (Multidrug resistance protein 2) (Multidrug resistance protein 3) (EC 7.6.2.2) (P-glycoprotein 2) (P-glycoprotein 3) 1276 140,377 Chain (1); Domain (4); Glycosylation (2); Modified residue (1); Nucleotide binding (2); Region (1); Sequence conflict (2); Topological domain (13); Transmembrane (12) TRANSMEM 48 70 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 116 136 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 186 207 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 213 235 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 294 315 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 330 351 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 709 729 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 753 773 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 829 849 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 851 870 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 931 953 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}.; TRANSMEM 970 991 Helical. {ECO:0000255|PROSITE-ProRule:PRU00441}. TOPO_DOM 1 47 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 71 115 Extracellular. {ECO:0000250}.; TOPO_DOM 137 185 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 208 212 Extracellular. {ECO:0000250}.; TOPO_DOM 236 293 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 316 329 Extracellular. {ECO:0000250}.; TOPO_DOM 352 708 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 730 752 Extracellular. {ECO:0000250}.; TOPO_DOM 774 828 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 850 850 Extracellular. {ECO:0000250}.; TOPO_DOM 871 930 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 954 969 Extracellular. {ECO:0000250}.; TOPO_DOM 992 1276 Cytoplasmic. {ECO:0000250}. FUNCTION: Energy-dependent phospholipid efflux translocator that acts as a positive regulator of biliary lipid secretion. Functions as a floppase that translocates specifically phosphatidylcholine (PC) from the inner to the outer leaflet of the canalicular membrane bilayer into the canaliculi between hepatocytes. Translocation of PC makes the biliary phospholipids available for extraction into the canaliculi lumen by bile salt mixed micelles and therefore protects the biliary tree from the detergent activity of bile salts (PubMed:8106172, PubMed:7912658, PubMed:7592705, PubMed:7814632, PubMed:8725158, PubMed:9366571). Plays a role in the recruitment of phosphatidylcholine (PC), phosphatidylethanolamine (PE) and sphingomyelin (SM) molecules to nonraft membranes and to further enrichment of SM and cholesterol in raft membranes in hepatocytes (By similarity). Required for proper phospholipid bile formation (PubMed:8106172). Indirectly involved in cholesterol efflux activity from hepatocytes into the canalicular lumen in the presence of bile salts in an ATP-dependent manner (PubMed:7814632, PubMed:8725158). May promote biliary phospholipid secretion as canaliculi-containing vesicles from the canalicular plasma membrane (PubMed:9366571). In cooperation with ATP8B1, functions to protect hepatocytes from the deleterious detergent activity of bile salts (PubMed:21820390). Does not confer multidrug resistance (PubMed:1990275). {ECO:0000250|UniProtKB:P21439, ECO:0000269|PubMed:1990275, ECO:0000269|PubMed:21820390, ECO:0000269|PubMed:7592705, ECO:0000269|PubMed:7814632, ECO:0000269|PubMed:7912658, ECO:0000269|PubMed:8106172, ECO:0000269|PubMed:8725158, ECO:0000269|PubMed:9366571}. PTM: Phosphorylated. Phosphorylation is required for PC efflux activity. Phosphorylation occurs on serine and threonine residues in a protein kinase A- or C-dependent manner. May be phosphorylated on Thr-41 and Ser-46. {ECO:0000250|UniProtKB:P21439}.; PTM: Glycosylated. {ECO:0000250|UniProtKB:P21439}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23468132, ECO:0000269|PubMed:8106172, ECO:0000269|PubMed:8615769}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. Apical cell membrane {ECO:0000269|PubMed:1381362}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. Membrane raft {ECO:0000250|UniProtKB:P21439}. Cytoplasm {ECO:0000250|UniProtKB:P21439}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:Q08201}. Note=Transported from the Golgi to the apical bile canalicular membrane in a RACK1-dependent manner. Redistributed into pseudocanaliculi formed between cells in a bezafibrate- or PPARA-dependent manner (By similarity). Localized at the apical canalicular membrane of the epithelial cells lining the lumen of the bile canaliculi and biliary ductules (PubMed:1381362, PubMed:8106172, PubMed:8615769). Localized preferentially in lipid nonraft domains of canalicular plasma membranes (PubMed:23468132). {ECO:0000250|UniProtKB:P21439, ECO:0000269|PubMed:1381362, ECO:0000269|PubMed:23468132, ECO:0000269|PubMed:8106172, ECO:0000269|PubMed:8615769}. SUBUNIT: May interact with RACK1. Interacts with HAX1. {ECO:0000250|UniProtKB:P21439, ECO:0000250|UniProtKB:Q08201}. TISSUE SPECIFICITY: Expressed in the liver (PubMed:1381362, PubMed:8615769) (at protein level). Expressed in adrenal, liver, muscle, spleen and heart (PubMed:2471060). Expressed in multidrug-resistant cell lines (PubMed:1969609). {ECO:0000269|PubMed:1381362, ECO:0000269|PubMed:1969609, ECO:0000269|PubMed:2471060, ECO:0000269|PubMed:8615769}. +Q5RKR3 ISLR2_MOUSE Immunoglobulin superfamily containing leucine-rich repeat protein 2 (Leucine-rich repeat domain and immunoglobulin domain-containing axon extension protein) 745 79,758 Chain (1); Disulfide bond (1); Domain (3); Erroneous initiation (1); Glycosylation (7); Modified residue (2); Repeat (5); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 590 610 Helical. {ECO:0000255}. TOPO_DOM 20 589 Extracellular. {ECO:0000255}.; TOPO_DOM 611 745 Cytoplasmic. {ECO:0000255}. FUNCTION: Required for axon extension during neural development. {ECO:0000269|PubMed:19755105}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19755105}; Single-pass membrane protein {ECO:0000269|PubMed:19755105}. SUBUNIT: Homomultimer. Interacts with NTRK1/TrkA. {ECO:0000269|PubMed:19755105}. TISSUE SPECIFICITY: At E11.5, expressed in spinal nerves, their roots and the ventral spinal cord. At E12.5, detected in the ventral spinal cord, dorsal root ganglia (DRG), dorsal and ventral roots and sympathetic chain ganglia. At E12.5, expressed in almost all motor neurons which also express RET and in almost all DRG sensory neurons which also express NTRK1. At E18.5, expressed only in a subset of NTRK1-expressing neurons but still expressed in nearly all RET-expressing neurons. {ECO:0000269|PubMed:19755105}. +A2ATD1 ISM1_MOUSE Isthmin-1 454 51,145 Chain (1); Disulfide bond (3); Domain (2); Signal peptide (1) FUNCTION: Acts as an angiogenesis inhibitor. {ECO:0000269|PubMed:19874420}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. SUBUNIT: Interacts with integrin ITGAV/ITGB5. {ECO:0000269|PubMed:19874420}. DOMAIN: The C-terminal AMOP domain plays an important role in the anti-angiogenic function of ISM1. {ECO:0000269|PubMed:19874420}. +Q91V64 ISOC1_MOUSE Isochorismatase domain-containing protein 1 297 32,033 Chain (1); Modified residue (2); Sequence conflict (2) +Q5RJG7 ISPD_MOUSE D-ribitol-5-phosphate cytidylyltransferase (EC 2.7.7.40) (2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase-like protein) (Isoprenoid synthase domain-containing protein) 447 49,136 Alternative sequence (7); Chain (1); Frameshift (1); Sequence conflict (4); Site (4) Protein modification; protein glycosylation. FUNCTION: Cytidylyltransferase required for protein O-linked mannosylation (By similarity). Catalyzes the formation of CDP-ribitol nucleotide sugar from D-ribitol 5-phosphate (By similarity). CDP-ribitol is a substrate of FKTN during the biosynthesis of the phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-3-N-acetylglucosamine-beta-4-(phosphate-6-)mannose), a carbohydrate structure present in alpha-dystroglycan (DAG1), which is required for binding laminin G-like domain-containing extracellular proteins with high affinity (By similarity). Shows activity toward other pentose phosphate sugars and mediates formation of CDP-ribulose or CDP-ribose using CTP and ribulose-5-phosphate or ribose-5-phosphate, respectively (By similarity). Not Involved in dolichol production (By similarity). {ECO:0000250|UniProtKB:A4D126}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:A4D126}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:A4D126}. +P14404 MECOM_MOUSE MDS1 and EVI1 complex locus protein (Ecotropic virus integration site 1 protein) (EVI-1) (Myelodysplasia syndrome 1 protein homolog) 1232 138,100 Alternative sequence (3); Chain (1); Compositional bias (1); Cross-link (37); Domain (1); Erroneous initiation (1); Modified residue (5); Motif (3); Region (1); Zinc finger (10) FUNCTION: Isoform 1: Functions as a transcriptional regulator binding to DNA sequences in the promoter region of target genes and regulating positively or negatively their expression. Oncogene which plays a role in development, cell proliferation and differentiation. May also play a role in apoptosis through regulation of the JNK and TGF-beta signaling. Involved in hematopoiesis. {ECO:0000269|PubMed:15889140, ECO:0000269|PubMed:18619962, ECO:0000269|PubMed:19767769}. PTM: May be acetylated by CREBBP and KAT2B. {ECO:0000250|UniProtKB:Q03112}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:2106070}. Nucleus speckle {ECO:0000250}. SUBUNIT: Isoform 1: Homooligomer. Interacts with CTBP1. Interacts with SMAD3 (via MH2 domain); the interaction is direct. Interacts with SMAD4; through interaction with SMAD3. Interacts with CREBBP, KAT2B and histone deacetylases. Interacts with MAPK8 and MAPK9; inhibits JNK signaling (By similarity). Interacts with SUV39H1 (via SET domain); enhances MECOM transcriptional repression activity. {ECO:0000250|UniProtKB:Q03112, ECO:0000269|PubMed:18619962}. DOMAIN: Both zinc finger regions are required for the transcriptional activation of PBX1. {ECO:0000250}. +Q9Z2D6 MECP2_MOUSE Methyl-CpG-binding protein 2 (MeCp-2 protein) (MeCp2) 484 52,307 Alternative sequence (1); Chain (1); Compositional bias (2); DNA binding (2); Domain (1); Helix (2); Modified residue (10); Mutagenesis (5); Region (2); Sequence conflict (1) FUNCTION: Chromosomal protein that binds to methylated DNA. It can bind specifically to a single methyl-CpG pair. It is not influenced by sequences flanking the methyl-CpGs. Mediates transcriptional repression through interaction with histone deacetylase and the corepressor SIN3. Binds both 5-methylcytosine (5mC) and 5-hydroxymethylcytosine (5hmC)-containing DNA, with a preference for 5-methylcytosine (5mC). {ECO:0000269|PubMed:23434322}. PTM: Phosphorylated on Ser-421 by CaMK2 in brain upon synaptic activity, which attenuates its repressor activity and seems to regulate dendritic growth and spine maturation. Does not seem to be phosphorylated on Ser-421 in other tissues. {ECO:0000269|PubMed:17046689}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15034150, ECO:0000269|PubMed:17296936}. Note=Colocalized with methyl-CpG in the genome. Colocalized with TBL1X to the heterochromatin foci. {ECO:0000250|UniProtKB:P51608}. SUBUNIT: Interacts with FNBP3 (PubMed:9171351). Interacts with CDKL5 (By similarity). Interacts with ATRX; MECP2 recruits ATRX to pericentric heterochromatin in neuronal cells (PubMed:17296936). Interacts with NCOR2 (PubMed:23770565). Interacts with TBL1XR1; bridges interaction between MECP2 and NCOR1 (PubMed:28348241). Interacts with TBL1X; recuits TBL1X to the heterochromatin foci (By similarity). {ECO:0000250|UniProtKB:P51608, ECO:0000269|PubMed:17296936, ECO:0000269|PubMed:23770565, ECO:0000269|PubMed:28348241, ECO:0000269|PubMed:9171351}. +Q9D8C6 MED11_MOUSE Mediator of RNA polymerase II transcription subunit 11 (Mediator complex subunit 11) 117 13,131 Chain (1); Initiator methionine (1); Modified residue (1); Sequence conflict (1) FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Component of the Mediator complex, which is composed of MED1, MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L, MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23, MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8 subunits form a distinct module termed the CDK8 module. Mediator containing the CDK8 module is less active than Mediator lacking this module in supporting transcriptional activation. Individual preparations of the Mediator complex lacking one or more distinct subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and TRAP (By similarity). {ECO:0000250}. +Q5SWW4 MED13_MOUSE Mediator of RNA polymerase II transcription subunit 13 (Thyroid hormone receptor-associated protein 1) (Thyroid hormone receptor-associated protein complex 240 kDa component) (Trap240) 2171 238,591 Chain (1); Compositional bias (2); Modified residue (8); Motif (2); Sequence conflict (1) FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the Mediator complex, which is composed of MED1, MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L, MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23, MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8 subunits form a distinct module termed the CDK8 module. Mediator containing the CDK8 module is less active than Mediator lacking this module in supporting transcriptional activation. Individual preparations of the Mediator complex lacking one or more distinct subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and TRAP (By similarity). {ECO:0000250}. +Q8VCS6 MED9_MOUSE Mediator of RNA polymerase II transcription subunit 9 (Mediator complex subunit 9) 142 15,709 Chain (1); Coiled coil (1); Compositional bias (1); Initiator methionine (1); Modified residue (2); Sequence conflict (2) FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Component of the Mediator complex, which is composed of MED1, MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L, MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23, MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8 subunits form a distinct module termed the CDK8 module. Mediator containing the CDK8 module is less active than Mediator lacking this module in supporting transcriptional activation. Individual preparations of the Mediator complex lacking one or more distinct subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and TRAP (By similarity). {ECO:0000250}. +Q8BRM6 MEI4_MOUSE Meiosis-specific protein MEI4 389 44,471 Alternative sequence (1); Chain (1); Frameshift (1); Sequence conflict (1) FUNCTION: Required for DNA double-strand breaks (DSBs) formation in unsynapsed regions during meiotic recombination (PubMed:20551173, PubMed:25795304, PubMed:27723721). Probably acts by forming a complex with IHO1/CCDC36 and REC114, which activates DSBs formation in unsynapsed regions, an essential step to ensure completion of synapsis (PubMed:27723721). {ECO:0000269|PubMed:20551173, ECO:0000269|PubMed:25795304, ECO:0000269|PubMed:27723721}. SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:20551173, ECO:0000269|PubMed:25795304}. Note=Specifically localizes to unsynapsed chromosomal regions during meiosis (PubMed:25795304, PubMed:27723721). Located in discrete foci on the axes of meiotic chromosomes. The number of foci is highest at leptonema, decreases at zygonema and is strongly reduced in pachynema and subsequent stages (PubMed:20551173). {ECO:0000269|PubMed:20551173, ECO:0000269|PubMed:25795304, ECO:0000269|PubMed:27723721}. SUBUNIT: Interacts with REC114 (PubMed:20551173). Part of the MCD recombinosome complex, at least composed of IHO1/CCDC36, REC114 and MEI4 (PubMed:27723721). {ECO:0000269|PubMed:20551173, ECO:0000269|PubMed:27723721}. TISSUE SPECIFICITY: Expressed in adult testis and brain and in embryonic ovary. {ECO:0000269|PubMed:20551173}. +Q61846 MELK_MOUSE Maternal embryonic leucine zipper kinase (EC 2.7.11.1) (Protein kinase PK38) (mPK38) (Tyrosine-protein kinase MELK) (EC 2.7.10.2) 643 72,729 Active site (1); Beta strand (7); Binding site (1); Chain (1); Domain (2); Helix (17); Modified residue (16); Mutagenesis (1); Nucleotide binding (1); Region (2); Sequence conflict (2); Turn (3) FUNCTION: Serine/threonine-protein kinase involved in various processes such as cell cycle regulation, self-renewal of stem cells, apoptosis and splicing regulation. Has a broad substrate specificity; phosphorylates BCL2L14, CDC25B, MAP3K5/ASK1 and ZNF622. Acts as an activator of apoptosis by phosphorylating and activating MAP3K5/ASK1. Acts as a regulator of cell cycle, notably by mediating phosphorylation of CDC25B, promoting localization of CDC25B to the centrosome and the spindle poles during mitosis. Plays a key role in cell proliferation. Required for proliferation of embryonic and postnatal multipotent neural progenitors. Phosphorylates and inhibits BCL2L14. Also involved in the inhibition of spliceosome assembly during mitosis by phosphorylating ZNF622, thereby contributing to its redirection to the nucleus. May also play a role in primitive hematopoiesis. {ECO:0000269|PubMed:16061694, ECO:0000269|PubMed:18948261}. PTM: Autophosphorylated: autophosphorylation of the T-loop at Thr-167 and Ser-171 is required for activation. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. SUBUNIT: Monomer. Interacts with ZNF622 and PPP1R8 (By similarity). {ECO:0000250}. DOMAIN: The KA1 domain mediates binding to phospholipids and targeting to membranes. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in testis, ovary, thymus, spleen and T-cell. Expressed by neural progenitors: highly enriched in cultures containing multipotent progenitors. {ECO:0000269|PubMed:16061694, ECO:0000269|PubMed:9136115, ECO:0000269|PubMed:9305775}. +Q9ESN9 JIP3_MOUSE C-Jun-amino-terminal kinase-interacting protein 3 (JIP-3) (JNK-interacting protein 3) (JNK MAP kinase scaffold protein 3) (JNK/SAPK-associated protein 1) (JSAP1) (Mitogen-activated protein kinase 8-interacting protein 3) (Sunday driver 2) 1337 147,561 Alternative sequence (5); Chain (1); Coiled coil (2); Domain (2); Erroneous initiation (1); Helix (1); Modified residue (8); Mutagenesis (8); Region (4); Sequence conflict (6) FUNCTION: The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. May function as a regulator of vesicle transport, through interactions with the JNK-signaling components and motor proteins (PubMed:10523642, PubMed:10629060). Promotes neuronal axon elongation in a kinesin- and JNK-dependent manner (PubMed:23576431, PubMed:25944905, PubMed:28259553). Activates cofilin at axon tips via local activation of JNK, thereby regulating filopodial dynamics and enhancing axon elongation (PubMed:23576431, PubMed:25944905, PubMed:28259553). Its binding to kinesin heavy chains (KHC), promotes kinesin-1 motility along microtubules and is essential for axon elongation and regeneration (PubMed:23576431, PubMed:25944905, PubMed:28259553). Regulates cortical neuronal migration by mediating NTRK2/TRKB anterograde axonal transport during brain development (PubMed:23576431, PubMed:25944905, PubMed:28259553). Acts as an adapter that bridges the interaction between NTRK2/TRKB and KLC1 and drives NTRK2/TRKB axonal but not dendritic anterograde transport, which is essential for subsequent BDNF-triggered signaling and filopodia formation (PubMed:23576431, PubMed:25944905, PubMed:28259553). {ECO:0000269|PubMed:10523642, ECO:0000269|PubMed:10629060, ECO:0000269|PubMed:23576431, ECO:0000269|PubMed:25944905, ECO:0000269|PubMed:28259553}. PTM: Phosphorylation by ROCK1 is crucial for the recruitment of JNK. {ECO:0000250|UniProtKB:Q9UPT6}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10629060}. Golgi apparatus {ECO:0000269|PubMed:11106729}. Cytoplasmic vesicle {ECO:0000269|PubMed:11106729}. Cell projection, growth cone {ECO:0000269|PubMed:10629060}. Cell projection, axon {ECO:0000269|PubMed:25944905}. Cell projection, dendrite {ECO:0000250|UniProtKB:E9PSK7}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:E9PSK7}. Note=Localized in the soma and growth cones of differentiated neurites and the Golgi and vesicles of the early secretory compartment of epithelial cells (PubMed:10629060, PubMed:11106729). KIF5A/B/C-mediated transportation to axon tips is essential for its function in enhancing neuronal axon elongation (By similarity). {ECO:0000250|UniProtKB:E9PSK7, ECO:0000269|PubMed:10629060, ECO:0000269|PubMed:11106729}. SUBUNIT: Forms homo- or heterooligomeric complexes. The central region of MAPK8IP3 interacts with the C-terminal of MAPK8IP2 but not MAPK8IP1. Binds specific components of the JNK signaling pathway namely MAPK8/JNK1, MAPK9/JNK2 and MAPK10/JNK3 to the N-terminal region, MAP2K4/MKK4 and MAP2K7/MKK7 to the central region and MAP3K11 to the C-terminal region. Binds the TPR motif-containing C-terminal of kinesin light chain, KLC1. Pre-assembled MAPK8IP1 scaffolding complexes are then transported as a cargo of kinesin, to the required subcellular location (PubMed:10523642, PubMed:10629060, PubMed:11238452, PubMed:11106729). Interacts with ROCK1 and this interaction is enhanced by ultraviolet-B (UVB) radiation. Interacts with SH3RF2 (By similarity). Interacts with NTRK2/TRKB and NTRK3/TRKC (PubMed:21775604). {ECO:0000250|UniProtKB:E9PSK7, ECO:0000250|UniProtKB:Q9UPT6, ECO:0000269|PubMed:10523642, ECO:0000269|PubMed:10629060, ECO:0000269|PubMed:11106729, ECO:0000269|PubMed:11238452, ECO:0000269|PubMed:21775604}. TISSUE SPECIFICITY: Highly expressed throughout many regions of the brain and at lower levels in the heart, liver, lung, testes and kidney. All isoforms have been identified in the brain, isoform 1a is also expressed in the spleen and lung. {ECO:0000269|PubMed:10629060, ECO:0000269|PubMed:11024282}. +O88792 JAM1_MOUSE Junctional adhesion molecule A (JAM-A) (Junctional adhesion molecule 1) (JAM-1) (CD antigen CD321) 300 32,424 Beta strand (21); Chain (1); Disulfide bond (2); Domain (2); Glycosylation (2); Helix (3); Modified residue (3); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (2) TRANSMEM 239 259 Helical. {ECO:0000255}. TOPO_DOM 27 238 Extracellular. {ECO:0000255}.; TOPO_DOM 260 299 Cytoplasmic. {ECO:0000255}. FUNCTION: Seems to play a role in epithelial tight junction formation. Appears early in primordial forms of cell junctions and recruits PARD3 (PubMed:11447115). The association of the PARD6-PARD3 complex may prevent the interaction of PARD3 with JAM1, thereby preventing tight junction assembly (PubMed:11447115). Plays a role in regulating monocyte transmigration involved in integrity of epithelial barrier (PubMed:9660867). Ligand for integrin alpha-L/beta-2 involved in memory T-cell and neutrophil transmigration (By similarity). Involved in platelet activation (By similarity). {ECO:0000250|UniProtKB:Q9Y624, ECO:0000269|PubMed:11447115, ECO:0000269|PubMed:9660867}. SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000269|PubMed:11036763}. Cell membrane {ECO:0000269|PubMed:11036763}; Single-pass type I membrane protein {ECO:0000269|PubMed:11036763}. Note=Localized at tight junctions of both epithelial and endothelial cells. SUBUNIT: Interacts with the ninth PDZ domain of MPDZ (By similarity). Interacts with the first PDZ domain of PARD3 (PubMed:11447115). The association between PARD3 and PARD6B probably disrupts this interaction (PubMed:11447115). Interacts with ITGAL (via I-domain) (By similarity). {ECO:0000250|UniProtKB:Q9Y624, ECO:0000269|PubMed:11447115}. DOMAIN: The Ig-like V-type 2 domain is necessary and sufficient for interaction with integrin alpha-L/beta-2. {ECO:0000250|UniProtKB:Q9Y624}. +P43406 ITAV_MOUSE Integrin alpha-V (Vitronectin receptor subunit alpha) (CD antigen CD51) [Cleaved into: Integrin alpha-V heavy chain; Integrin alpha-V light chain] 1044 115,360 Calcium binding (4); Chain (3); Disulfide bond (9); Glycosylation (11); Motif (1); Repeat (7); Sequence conflict (5); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 989 1012 Helical. {ECO:0000255}. TOPO_DOM 31 988 Extracellular. {ECO:0000255}.; TOPO_DOM 1013 1044 Cytoplasmic. {ECO:0000255}. FUNCTION: The alpha-V (ITGAV) integrins are receptors for vitronectin, cytotactin, fibronectin, fibrinogen, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin, TGFB1 and vWF (PubMed:9827803, PubMed:10025398). They recognize the sequence R-G-D in a wide array of ligands. Alpha-V integrins may play a role in embryo implantation, angiogenesis and wound healing (PubMed:9827803). ITGAV:ITGB3 binds to fractalkine (CX3CL1) and may act as its coreceptor in CX3CR1-dependent fractalkine signaling (By similarity). ITGAV:ITGB3 binds to NRG1 (via EGF domain) and this binding is essential for NRG1-ERBB signaling. ITGAV:ITGB3 binds to FGF1 and this binding is essential for FGF1 signaling (By similarity). ITGAV:ITGB3 binds to FGF2 and this binding is essential for FGF2 signaling (By similarity). ITGAV:ITGB3 binds to IGF1 and this binding is essential for IGF1 signaling (By similarity). ITGAV:ITGB3 binds to IGF2 and this binding is essential for IGF2 signaling (By similarity). ITGAV:ITGB3 binds to IL1B and this binding is essential for IL1B signaling (By similarity). ITGAV:ITGB3 binds to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational changes and enhanced ligand binding to site 1 (By similarity). ITGAV:ITGB3 and ITGAV:ITGB6 act as a receptor for fibrillin-1 (FBN1) and mediate R-G-D-dependent cell adhesion to FBN1 (By similarity). Integrin alpha-V/beta-6 or alpha-V/beta-8 (ITGAV:ITGB6 or ITGAV:ITGB8) mediates R-G-D-dependent release of transforming growth factor beta-1 (TGF-beta-1) from regulatory Latency-associated peptide (LAP), thereby playing a key role in TGF-beta-1 activation (PubMed:10025398, PubMed:25127859). {ECO:0000250|UniProtKB:P06756, ECO:0000269|PubMed:10025398, ECO:0000269|PubMed:25127859, ECO:0000269|PubMed:9827803}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. Cell junction, focal adhesion {ECO:0000250|UniProtKB:P06756}. SUBUNIT: Heterodimer of an alpha and a beta subunit. The alpha subunit is composed of a heavy and a light chain linked by a disulfide bond. Alpha-V (ITGAV) associates with either beta-1 (ITGB1), beta-3 (ITGB3), beta-5 (ITGB5), beta-6 (ITGB6) or beta-8 (ITGB8) (Probable). Interacts with RAB25. Interacts with CIB1 (By similarity). Integrins ITGAV:ITGB3 and ITGAV:ITGB5 interact with FBLN5 (via N-terminus) (PubMed:11805835). ITGAV:ITGB3 and ITGAV:ITGB5 interact with CCN3 (By similarity). ITGAV:ITGB3 interacts with ADGRA2 (By similarity). ITGAV:ITGB3 interacts with FGF2; it is likely that FGF2 can simultaneously bind ITGAV:ITGB3 and FGF receptors (By similarity). ITGAV:ITGB3 is found in a ternary complex with CX3CR1 and CX3CL1. ITGAV:ITGB3 is found in a ternary complex with NRG1 and ERBB3. ITGAV:ITGB3 is found in a ternary complex with FGF1 and FGFR1. ITGAV:ITGB3 is found in a ternary complex with IGF1 and IGF1R (By similarity). ITGAV:ITGB3 interacts with IGF2 (By similarity). ITGAV:ITGB3 and ITGAV:ITGB6 interact with FBN1 (By similarity). ITGAV:ITGB3 interacts with CD9, CD81 and CD151 (via second extracellular domain) (By similarity). ITGAV:ITGB6 interacts with TGFB1 (PubMed:10025398). {ECO:0000250|UniProtKB:P06756, ECO:0000269|PubMed:10025398, ECO:0000269|PubMed:11805835, ECO:0000305|PubMed:11805835}. +Q9EQF4 JUNO_MOUSE Sperm-egg fusion protein Juno (Folate receptor 4) (Folate receptor delta) (FR-delta) (Folate-binding protein 3) (IZUMO1 receptor protein JUNO) 244 28,203 Alternative sequence (1); Beta strand (10); Chain (1); Disulfide bond (8); Glycosylation (2); Helix (9); Lipidation (1); Mutagenesis (9); Propeptide (1); Region (1); Signal peptide (1); Turn (2) FUNCTION: Receptor for IZUMO1 present at the cell surface of oocytes (oolemma), which is essential for species-specific gamete recognition and fertilization (PubMed:24739963, PubMed:26859261, PubMed:27309808, PubMed:27416963). The IZUMO1:IZUMO1R/JUNO interaction is a necessary adhesion event between sperm and egg that is required for fertilization but is not sufficient for cell fusion (PubMed:24739963, PubMed:26859261, PubMed:27309808). The ligand-receptor interaction probably does not act as a membrane 'fusogen' (PubMed:24739963, PubMed:26859261, PubMed:27309808). Does not bind folate (PubMed:24739963). {ECO:0000269|PubMed:24739963, ECO:0000269|PubMed:26859261, ECO:0000269|PubMed:27309808, ECO:0000269|PubMed:27416963}. PTM: The protein is rapidly cleaved following fertilization, being only weakly detectable in zona-intact fertilized eggs at telophase II and undetectable at the pronuclear stage (PubMed:24739963). Sheding is probably required to block to polyspermy and ensuring egg fusion with a single sperm (PubMed:24739963). {ECO:0000269|PubMed:24739963}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24739963, ECO:0000269|PubMed:25209248, ECO:0000269|PubMed:27309808}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:24739963}. Note=GPI-anchored at the oolemma. {ECO:0000269|PubMed:24739963}. SUBUNIT: Monomer (PubMed:26859261). Interacts with IZUMO1; the interaction is direct (PubMed:24739963, PubMed:26859261, PubMed:27309808, PubMed:25209248, PubMed:27416963). IZUMO1 and IZUMO1R/JUNO form a complex with 1:1 stoichiometry (By similarity). {ECO:0000250|UniProtKB:A6ND01, ECO:0000269|PubMed:24739963, ECO:0000269|PubMed:25209248, ECO:0000269|PubMed:26859261, ECO:0000269|PubMed:27309808, ECO:0000269|PubMed:27416963}. TISSUE SPECIFICITY: Widely expressed with higher expression in thymus, spleen and lung (PubMed:11111049). Present at the cell surface of unfertilized oocytes, while it is barely detectable 30 to 40 minutes after fertilization (at protein level) (PubMed:24739963). {ECO:0000269|PubMed:11111049, ECO:0000269|PubMed:24739963}. +P06330 HVM51_MOUSE Ig heavy chain V region AC38 205.12 118 12,934 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (3) +P18526 HVM55_MOUSE Ig heavy chain V region 345 117 12,902 Beta strand (7); Chain (1); Disulfide bond (1); Helix (2); Non-terminal residue (1); Region (5); Signal peptide (1); Turn (2) +P18527 HVM56_MOUSE Ig heavy chain V region 914 97 10,661 Beta strand (9); Chain (1); Domain (1); Helix (3); Non-terminal residue (1); Turn (2) +O35632 HYAL2_MOUSE Hyaluronidase-2 (Hyal-2) (EC 3.2.1.35) (Hyaluronoglucosaminidase-2) 473 53,618 Active site (1); Chain (1); Disulfide bond (5); Domain (1); Glycosylation (5); Lipidation (1); Propeptide (1); Sequence conflict (9); Signal peptide (1) FUNCTION: Hydrolyzes high molecular weight hyaluronic acid to produce an intermediate-sized product which is further hydrolyzed by sperm hyaluronidase to give small oligosaccharides. Displays very low levels of activity. Associates with and negatively regulates MST1R (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. SUBUNIT: Interacts with MST1R. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. In the brain, expressed during embryonic stages but expression decreases after birth and is barely detectable in adult brain. {ECO:0000269|PubMed:9790770}. +P01729 LV2B_MOUSE Ig lambda-2 chain V region MOPC 315 129 13,418 Chain (1); Domain (1); Modified residue (1); Non-terminal residue (1); Signal peptide (1) +Q80XF5 I22R2_MOUSE Interleukin-22 receptor subunit alpha-2 (IL-22 receptor subunit alpha-2) (IL-22R-alpha-2) (IL-22RA2) (Cytokine receptor family type 2, soluble 1) (CRF2-S1) (Interleukin-22-binding protein) (IL-22BP) (IL22BP) (ZcytoR16) 230 26,613 Chain (1); Disulfide bond (1); Domain (2); Mutagenesis (2); Sequence conflict (2); Signal peptide (1); Site (2) FUNCTION: Receptor for IL22. Binds to IL22, prevents interaction with the functional IL-22R complex and blocks the activity of IL22 (in vitro). May play an important role as an IL22 antagonist in the regulation of inflammatory responses. {ECO:0000269|PubMed:12700595}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12700595}. TISSUE SPECIFICITY: Highly expressed in lymph nodes and at lower levels in lung, spleen, and thymus. Not expressed in kidney, liver and heart. {ECO:0000269|PubMed:15201862}. +P32043 HXC5_MOUSE Homeobox protein Hox-C5 (Homeobox protein Hox-3.4) (Homeobox protein Hox-6.2) 222 24,992 Chain (1); DNA binding (1); Motif (1); Sequence conflict (2) FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. SUBCELLULAR LOCATION: Nucleus. +P10629 HXC6_MOUSE Homeobox protein Hox-C6 (Homeobox protein Hox-3.3) (Homeobox protein Hox-6.1) 235 26,915 Alternative sequence (1); Chain (1); Compositional bias (1); DNA binding (1); Motif (1); Sequence conflict (7) FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. SUBCELLULAR LOCATION: Nucleus. +P97411 ICA69_MOUSE Islet cell autoantigen 1 (69 kDa islet cell autoantigen) (ICA69) (Islet cell autoantigen p69) (ICAp69) (p69) 478 54,324 Alternative sequence (2); Chain (1); Domain (1); Sequence conflict (13) FUNCTION: May play a role in neurotransmitter secretion. {ECO:0000303|PubMed:11029035}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:11029035}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Predominantly cytosolic. Also exists as a membrane-bound form which has been found associated with synaptic vesicles and also with the Golgi complex and immature secretory granules. TISSUE SPECIFICITY: Predominantly expressed in brain, pancreas and stomach mucosa. High expression also found in stomach muscle and testis. {ECO:0000269|PubMed:11029035}. +Q61189 ICLN_MOUSE Methylosome subunit pICln (Chloride channel, nucleotide sensitive 1A) (Chloride conductance regulatory protein ICln) (I(Cln)) (Chloride ion current inducer protein) (ClCI) 236 26,021 Chain (1); Initiator methionine (1); Modified residue (8) FUNCTION: Involved in both the assembly of spliceosomal snRNPs and the methylation of Sm proteins (By similarity). Chaperone that regulates the assembly of spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus. May also indirectly participate in cellular volume control by activation of a swelling-induced chloride conductance pathway. {ECO:0000250|UniProtKB:P54105}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P54105}. Nucleus {ECO:0000250|UniProtKB:P54105}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P54105}. Note=A small fraction is also associated with the cytoskeleton. {ECO:0000250|UniProtKB:P54105}. SUBUNIT: Component of the methylosome, a 20S complex containing at least PRMT5/SKB1, WDR77/MEP50 and CLNS1A/pICln. May mediate SNRPD1 and SNRPD3 methylation. Forms a 6S pICln-Sm complex composed of CLNS1A/pICln, SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG; ring-like structure where CLNS1A/pICln mimics additional Sm proteins and which is unable to assemble into the core snRNP. Interacts with LSM10 and LSM11. {ECO:0000250|UniProtKB:P54105}. +Q61581 IBP7_MOUSE Insulin-like growth factor-binding protein 7 (IBP-7) (IGF-binding protein 7) (IGFBP-7) (MAC25 protein) 281 28,969 Chain (1); Disulfide bond (3); Domain (3); Erroneous initiation (1); Glycosylation (1); Modified residue (1); Natural variant (2); Sequence conflict (1); Signal peptide (1) FUNCTION: Binds IGF-I and IGF-II with a relatively low affinity Stimulates prostacyclin (PGI2) production. Stimulates cell adhesion (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Expressed at high levels in lung, kidney, small intestine, testis and uterus and at moderate levels in liver. {ECO:0000269|PubMed:10623583}. +P97290 IC1_MOUSE Plasma protease C1 inhibitor (C1 Inh) (C1Inh) (C1 esterase inhibitor) (C1-inhibiting factor) (Serpin G1) 504 55,585 Chain (1); Disulfide bond (2); Glycosylation (5); Sequence conflict (2); Signal peptide (1); Site (1) FUNCTION: Activation of the C1 complex is under control of the C1-inhibitor. It forms a proteolytically inactive stoichiometric complex with the C1r or C1s proteases. May play a potentially crucial role in regulating important physiological pathways including complement activation, blood coagulation, fibrinolysis and the generation of kinins. Very efficient inhibitor of FXIIa. May inhibit chymotrypsin and kallikrein. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Interacts with MASP1. {ECO:0000250}. +Q00690 LYAM2_MOUSE E-selectin (CD62 antigen-like family member E) (Endothelial leukocyte adhesion molecule 1) (ELAM-1) (Leukocyte-endothelial cell adhesion molecule 2) (LECAM2) (CD antigen CD62E) 612 66,750 Chain (1); Disulfide bond (19); Domain (8); Erroneous initiation (1); Glycosylation (9); Metal binding (5); Region (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 558 579 Helical. {ECO:0000255}. TOPO_DOM 22 557 Extracellular. {ECO:0000255}.; TOPO_DOM 580 612 Cytoplasmic. {ECO:0000255}. FUNCTION: Cell-surface glycoprotein having a role in immunoadhesion. Mediates in the adhesion of blood neutrophils in cytokine-activated endothelium through interaction with SELPLG/PSGL1 (PubMed:1375914). May have a role in capillary morphogenesis. {ECO:0000250|UniProtKB:P16581, ECO:0000269|PubMed:1375914}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1375914}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P16581}. SUBUNIT: Interacts with SELPLG/PSGL1 and PODXL2 through the sialyl Lewis X epitope. SELPLG sulfation appears not to be required for this interaction. {ECO:0000250|UniProtKB:P16581}. +Q9D6R2 IDH3A_MOUSE Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial (EC 1.1.1.41) (Isocitric dehydrogenase subunit alpha) (NAD(+)-specific ICDH subunit alpha) 366 39,639 Alternative sequence (1); Binding site (3); Chain (1); Metal binding (3); Modified residue (6); Sequence conflict (1); Site (2); Transit peptide (1) FUNCTION: Catalytic subunit of the enzyme which catalyzes the decarboxylation of isocitrate (ICT) into alpha-ketoglutarate. The heterodimer composed of the alpha (IDH3A) and beta (IDH3B) subunits and the heterodimer composed of the alpha (IDH3A) and gamma (IDH3G) subunits, have considerable basal activity but the full activity of the heterotetramer (containing two subunits of IDH3A, one of IDH3B and one of IDH3G) requires the assembly and cooperative function of both heterodimers. {ECO:0000250|UniProtKB:P50213}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. SUBUNIT: Heterooligomer of subunits alpha (IDH3A), beta (IDH3B), and gamma (IDH3G) in the apparent ratio of 2:1:1. The heterodimer containing one IDH3A and one IDH3B subunit and the heterodimer containing one IDH3A and one IDH3G subunit assemble into a heterotetramer (which contains two subunits of IDH3A, one of IDH3B and one of IDH3G) and further into the heterooctamer. {ECO:0000250|UniProtKB:P50213}. +P41136 ID2_MOUSE DNA-binding protein inhibitor ID-2 (Inhibitor of DNA binding 2) (Inhibitor of differentiation 2) 134 14,959 Chain (1); Domain (1); Erroneous initiation (1); Modified residue (2); Motif (1); Region (1); Sequence conflict (2) FUNCTION: Transcriptional regulator (lacking a basic DNA binding domain) which negatively regulates the basic helix-loop-helix (bHLH) transcription factors by forming heterodimers and inhibiting their DNA binding and transcriptional activity. Implicated in regulating a variety of cellular processes, including cellular growth, senescence, differentiation, apoptosis, angiogenesis, and neoplastic transformation. Inhibits skeletal muscle and cardiac myocyte differentiation. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer. Restricts the CLOCK and ARNTL/BMAL1 localization to the cytoplasm. Plays a role in both the input and output pathways of the circadian clock: in the input component, is involved in modulating the magnitude of photic entrainment and in the output component, contributes to the regulation of a variety of liver clock-controlled genes involved in lipid metabolism. {ECO:0000269|PubMed:16556596, ECO:0000269|PubMed:19217292, ECO:0000269|PubMed:19740747, ECO:0000269|PubMed:20861012}. PTM: Polyubiquitinated; which is favored by Ifi204 and leads to proteasomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15563451, ECO:0000269|PubMed:20861012}. Nucleus {ECO:0000269|PubMed:15563451}. SUBUNIT: Heterodimer with other HLH proteins. Interacts with NR0B2. Interacts with CLOCK and ARNTL/BMAL1 (By similarity). Interacts with GATA4, IFI204 and NKX2-5. {ECO:0000250, ECO:0000269|PubMed:11940648, ECO:0000269|PubMed:16556596}. DOMAIN: The bHLH domain is essential for its repressor activity towards the CLOCK-ARNTL/BMAL1 heterodimer. +P41133 ID3_MOUSE DNA-binding protein inhibitor ID-3 (ID-like protein inhibitor HLH 462) (Inhibitor of DNA binding 3) (Inhibitor of differentiation 3) 119 13,089 Chain (1); Domain (1); Region (1) FUNCTION: Transcriptional regulator (lacking a basic DNA binding domain) which negatively regulates the basic helix-loop-helix (bHLH) transcription factors by forming heterodimers and inhibiting their DNA binding and transcriptional activity. Implicated in regulating a variety of cellular processes, including cellular growth, senescence, differentiation, apoptosis, angiogenesis, and neoplastic transformation. Involved in myogenesis by inhibiting skeletal muscle and cardiac myocyte differentiation and promoting muscle precursor cells proliferation. Inhibits the binding of E2A-containing protein complexes to muscle creatine kinase E-box enhancer. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer. {ECO:0000269|PubMed:19217292, ECO:0000269|PubMed:22862948, ECO:0000269|PubMed:23824195}. PTM: Polyubiquitinated; which is favored by Ifi204 and leads to proteasomal degradation. {ECO:0000269|PubMed:16556596}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:16556596}. Cytoplasm {ECO:0000269|PubMed:16556596}. Note=Nuclear in proliferating cells, translocates to cytosol during cell differentiation. SUBUNIT: Homodimer, and heterodimer with other HLH proteins. Interacts with CLOCK and ARNTL/BMAL1 (By similarity). Interacts with COPS5 and COPS7A. Interacts with IFI204. Interacts with GATA4 and NKX2-5. Interacts with ANKRD2; both proteins cooperate in myoblast differentiation. {ECO:0000250, ECO:0000269|PubMed:11940648, ECO:0000269|PubMed:15451666, ECO:0000269|PubMed:16556596, ECO:0000269|PubMed:23824195}. TISSUE SPECIFICITY: Expressed by myoblasts (at protein level). {ECO:0000269|PubMed:23824195}. +O88844 IDHC_MOUSE Isocitrate dehydrogenase [NADP] cytoplasmic (IDH) (EC 1.1.1.42) (Cytosolic NADP-isocitrate dehydrogenase) (IDP) (NADP(+)-specific ICDH) (Oxalosuccinate decarboxylase) 414 46,674 Beta strand (14); Binding site (7); Chain (1); Helix (18); Initiator methionine (1); Metal binding (3); Modified residue (10); Mutagenesis (2); Nucleotide binding (2); Region (1); Sequence conflict (1); Site (2); Turn (3) PTM: Acetylation at Lys-374 dramatically reduces catalytic activity. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P41562}. SUBUNIT: Homodimer. {ECO:0000269|PubMed:29923039}. +P28301 LYOX_MOUSE Protein-lysine 6-oxidase (EC 1.4.3.13) (Lysyl oxidase) (Ras excision protein) 411 46,701 Chain (1); Cross-link (1); Disulfide bond (5); Glycosylation (2); Metal binding (3); Modified residue (1); Mutagenesis (1); Propeptide (1); Region (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Responsible for the post-translational oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin. Regulator of Ras expression. May play a role in tumor suppression. Plays a role in the aortic wall architecture (PubMed:27432961). {ECO:0000269|PubMed:27432961}. PTM: The lysine tyrosylquinone cross-link (LTQ) is generated by condensation of the epsilon-amino group of a lysine with a topaquinone produced by oxidation of tyrosine. {ECO:0000250|UniProtKB:P33072}.; PTM: Proteolytically activated by BMP1. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:27432961}. Secreted, extracellular space. SUBUNIT: Interacts with MFAP4. {ECO:0000250|UniProtKB:P28300}. TISSUE SPECIFICITY: Expressed in aorta (at protein level). Expressed in embryonic, juvenil and adult aorta. {ECO:0000269|PubMed:27432961}. +Q9Z0N1 IF2G_MOUSE Eukaryotic translation initiation factor 2 subunit 3, X-linked (Eukaryotic translation initiation factor 2 subunit gamma, X-linked) (eIF-2-gamma X) 472 51,065 Chain (1); Domain (1); Initiator methionine (1); Modified residue (2); Nucleotide binding (3); Region (5) FUNCTION: As a subunit of eukaryotic initiation factor 2 (eIF2), involved in the early steps of protein synthesis. In the presence of GTP, eIF2 forms a ternary complex with initiator tRNA Met-tRNAi and then recruits the 40S ribosomal complex, a step that determines the rate of protein translation. This step is followed by mRNA binding to form the 43S pre-initiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF2 and release of an eIF2-GDP binary complex. In order for eIF2 to recycle and catalyze another round of initiation, the GDP bound to eIF2 must exchange with GTP by way of a reaction catalyzed by eIF2B (By similarity). Along with its paralog on chromosome Y, may contribute to spermatogenesis up to the round spermatid stage (PubMed:26823431). {ECO:0000250, ECO:0000269|PubMed:26823431}. SUBUNIT: The eukaryotic translation initiation factor 2 complex/eIF2 is a heterotrimer composed of an alpha subunit, also called subunit 1 (encoded by EIF2S1), a beta subunit, also called subunit 2 (encoded by EIF2S2) and a gamma subunit, also called subunit 3 (encoded by 2 homologous genes Eif2s3x and Eif2s3y). {ECO:0000250|UniProtKB:P41091}. TISSUE SPECIFICITY: Widely expressed. In the brain, high mRNA levels are observed in specific regions, including the habenula, anterodorsal thalamic nucleus, hippocampus, hypothalamus, and cerebellum. Also expressed in the embryonic brain. There is a differential expression between males and females, wich is tissue-specific. Females tend to have higher expression levels than males in the brain (cortex, hippocampus and paraventricular nucleus, but not in the habenula), as well as in other tissues. The up-regulation observed in females at the mRNA level may be due to the presence of 2 active copies of the gene. {ECO:0000269|PubMed:12023983, ECO:0000269|PubMed:16325480, ECO:0000269|PubMed:9736774}. +P52293 IMA1_MOUSE Importin subunit alpha-1 (Importin alpha P1) (Karyopherin subunit alpha-2) (Pendulin) (Pore targeting complex 58 kDa subunit) (PTAC58) (RAG cohort protein 1) (SRP1-alpha) 529 57,928 Beta strand (4); Chain (1); Compositional bias (2); Domain (1); Helix (33); Initiator methionine (1); Modified residue (2); Motif (1); Region (2); Repeat (10); Sequence conflict (3); Turn (1) FUNCTION: Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P52292}. Nucleus {ECO:0000250|UniProtKB:P52292}. SUBUNIT: Heterodimer; with KPNB1 (By similarity). Component of a complex containing CSE1L, RAN and KPNA2 (By similarity). Interacts directly with CSE1L (By similarity). Interacts with PLAG1 (By similarity). Interacts with APEX1 (via N-terminus) (By similarity). Interacts with FRG1 (via N-terminus) (By similarity). Interacts with ARL4A, CTNNBL1 and NBN (By similarity). Interacts with ANP32E (PubMed:10692581). Interacts with SNAI1 (via zinc fingers) (PubMed:21454664). Interacts with SNAI2 (via zinc fingers) (By similarity). Interacts with BAG6 (By similarity). {ECO:0000250|UniProtKB:P52292, ECO:0000269|PubMed:10692581, ECO:0000269|PubMed:21454664}. DOMAIN: Consists of an N-terminal hydrophilic region, a hydrophobic central region composed of 10 repeats, and a short hydrophilic C-terminus. The N-terminal hydrophilic region contains the importin beta binding domain (IBB domain), which is sufficient for binding importin beta and essential for nuclear protein import.; DOMAIN: The IBB domain is thought to act as an intrasteric autoregulatory sequence by interacting with the internal autoinhibitory NLS. Binding of KPNB1 probably overlaps the internal NLS and contributes to a high affinity for cytoplasmic NLS-containing cargo substrates. After dissociation of the importin/substrate complex in the nucleus the internal autohibitory NLS contributes to a low affinity for nuclear NLS-containing proteins.; DOMAIN: The major and minor NLS binding sites are mainly involved in recognition of simple or bipartite NLS motifs. Structurally located within in a helical surface groove they contain several conserved Trp and Asn residues of the corresponding third helices (H3) of ARM repeats which mainly contribute to binding. TISSUE SPECIFICITY: Slightly detected in brain but not in cerebellum and skeletal muscle, highly expressed in testis and spleen. +O35343 IMA3_MOUSE Importin subunit alpha-3 (Importin alpha Q1) (Qip1) (Karyopherin subunit alpha-4) 521 57,923 Chain (1); Compositional bias (1); Domain (1); Initiator methionine (1); Modified residue (2); Motif (1); Region (2); Repeat (10) FUNCTION: Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Forms a complex with importin subunit beta-1. Interacts with SNAI1 (By similarity). {ECO:0000250}. DOMAIN: Consists of an N-terminal hydrophilic region, a hydrophobic central region composed of 10 repeats, and a short hydrophilic C-terminus. The N-terminal hydrophilic region contains the importin beta binding domain (IBB domain), which is sufficient for binding importin beta and essential for nuclear protein import.; DOMAIN: The IBB domain is thought to act as an intrasteric autoregulatory sequence by interacting with the internal autoinhibitory NLS. Binding of KPNB1 probably overlaps the internal NLS and contributes to a high affinity for cytoplasmic NLS-containing cargo substrates. After dissociation of the importin/substrate complex in the nucleus the internal autohibitory NLS contributes to a low affinity for nuclear NLS-containing proteins (By similarity). {ECO:0000250}.; DOMAIN: The major and minor NLS binding sites are mainly involved in recognition of simple or bipartite NLS motifs. Structurally located within in a helical surface groove they contain several conserved Trp and Asn residues of the corresponding third helices (H3) of ARM repeats which mainly contribute to binding (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Detected more or less in all tissues examined (Ehrlich ascites tumor cells, testis, kidney, spleen, liver, heart, lung, thymus, skeletal muscle, cerebellum and brain (without cerebellum)). Multiple-sized transcripts were highly expressed, especially in testis. +Q8BHA0 IN80C_MOUSE INO80 complex subunit C 191 20,405 Chain (1) FUNCTION: Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the chromatin remodeling INO80 complex; specifically part of a complex module associated with the helicase ATP-binding and the helicase C-terminal domain of INO80. Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10 (By similarity). {ECO:0000250}. +Q9CX62 INKA1_MOUSE PAK4-inhibitor INKA1 (Induced in neural crest by AP2-alpha protein homolog) (MInca) (Inka box actin regulator 1) 282 31,804 Chain (1); Compositional bias (1); Region (2); Sequence conflict (2) FUNCTION: Inhibitor of the serine/threonine-protein kinase PAK4. Acts by binding PAK4 in a substrate-like manner, inhibiting the protein kinase activity. {ECO:0000250|UniProtKB:Q96EL1}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96EL1}. Cytoplasm {ECO:0000250|UniProtKB:Q96EL1}. Note=Mainly nuclear. Relocalizes to the cytoplasm following interaction with PAK4. {ECO:0000250|UniProtKB:Q96EL1}. SUBUNIT: Interacts with PAK4 (PubMed:17314132). {ECO:0000269|PubMed:17314132}. DOMAIN: Contains 2 Inka boxes (also named iBox or inca box). The Inka boxes bind and inhibit PAK4 by binding a substrate-like manner. {ECO:0000250|UniProtKB:Q96EL1}. TISSUE SPECIFICITY: Expressed in tissues of the developing head during neurulation. {ECO:0000269|PubMed:20175189}. +Q8BGI3 INSI1_MOUSE Insulin-induced gene 1 protein (INSIG-1) 259 28,213 Chain (1); Cross-link (2); Sequence conflict (3); Topological domain (7); Transmembrane (6) TRANSMEM 70 90 Helical. {ECO:0000255}.; TRANSMEM 109 129 Helical. {ECO:0000255}.; TRANSMEM 143 159 Helical. {ECO:0000255}.; TRANSMEM 165 185 Helical. {ECO:0000255}.; TRANSMEM 192 212 Helical. {ECO:0000255}.; TRANSMEM 224 244 Helical. {ECO:0000255}. TOPO_DOM 1 69 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 91 108 Lumenal. {ECO:0000255}.; TOPO_DOM 130 142 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 160 164 Lumenal. {ECO:0000255}.; TOPO_DOM 186 191 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 213 223 Lumenal. {ECO:0000255}.; TOPO_DOM 245 259 Cytoplasmic. {ECO:0000250}. FUNCTION: Mediates feedback control of cholesterol synthesis by controlling SCAP and HMGCR. Functions by blocking the processing of sterol regulatory element-binding proteins (SREBPs). Capable of retaining the SCAP-SREBF2 complex in the ER thus preventing it from escorting SREBPs to the Golgi. Initiates the sterol-mediated ubiquitin-mediated endoplasmic reticulum-associated degradation (ERAD) of HMGCR via recruitment of the reductase to the ubiquitin ligase, AMFR/gp78. May play a role in growth and differentiation of tissues involved in metabolic control. May play a regulatory role during G0/G1 transition of cell growth. {ECO:0000250|UniProtKB:O15503}. PTM: Ubiquitinated. Subsequent to sterol deprivation, the SCAP-SREBF2 complex becomes dissociated from INSIG1, is then ubiquitinated and degraded in proteasomes. Although ubiquitination is required for rapid INSIG1 degradation, it is not required for release of the SCAP-SREBP complex. Ubiquitinated by RNF139. {ECO:0000250|UniProtKB:O15503}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O15503}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O15503}. SUBUNIT: Binds to the SCAP-SREBF2 complex only in the presence of sterols. Interacts with RNF139. Interacts with HMGCR (via its SSD); the interaction, accelerated by sterols, leads to the recruitment of HMGCR to AMFR/gp78 for its ubiquitination by the sterol-mediated ERAD pathway. Interacts with AMFR/gp78 (via its membrane domain); the interaction recruits HMCR at the ER membrane for its ubiquitination and degradation by the sterol-mediated ERAD pathway. Interacts with RNF145. {ECO:0000250|UniProtKB:O15503}. +Q91WG1 INSI2_MOUSE Insulin-induced gene 2 protein (INSIG-2) 225 24,915 Chain (1); Sequence conflict (2); Transmembrane (5) TRANSMEM 26 46 Helical. {ECO:0000255}.; TRANSMEM 71 91 Helical. {ECO:0000255}.; TRANSMEM 131 148 Helical. {ECO:0000255}.; TRANSMEM 154 174 Helical. {ECO:0000255}.; TRANSMEM 186 206 Helical. {ECO:0000255}. FUNCTION: Mediates feedback control of cholesterol synthesis by controlling SCAP and HMGCR. Functions by blocking the processing of sterol regulatory element-binding proteins (SREBPs). Capable of retaining the SCAP-SREBF2 complex in the ER thus preventing it from escorting SREBPs to the Golgi. Seems to regulate the ubiquitin-mediated proteasomal degradation of HMGCR. {ECO:0000269|PubMed:12242332, ECO:0000269|PubMed:12624180}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Binds to the SCAP-SREBF2 complex only in the presence of sterols. Interacts with RNF139 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in liver, testis, kidney, spleen, intestine, brain and adrenal gland. {ECO:0000269|PubMed:12624180}. +Q9CQB2 MCRI2_MOUSE MAPK regulated corepressor interacting protein 2 (Protein FAM195A) 160 17,871 Chain (1); Modified residue (5) SUBCELLULAR LOCATION: Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q9BUT9}. Nucleus {ECO:0000250|UniProtKB:Q9BUT9}. Note=Upon cellular stress, relocalizes to stress granules. {ECO:0000250|UniProtKB:Q9BUT9}. SUBUNIT: Interacts with DDX6. Interacts with MCRIP1. {ECO:0000250|UniProtKB:Q9BUT9}. +P15208 INSR_MOUSE Insulin receptor (IR) (EC 2.7.10.1) (CD antigen CD220) [Cleaved into: Insulin receptor subunit alpha; Insulin receptor subunit beta] 1372 155,610 Active site (1); Binding site (3); Chain (2); Compositional bias (1); Disulfide bond (19); Domain (4); Glycosylation (18); Modified residue (9); Mutagenesis (1); Nucleotide binding (2); Region (3); Sequence conflict (1); Signal peptide (1); Site (1); Topological domain (3); Transmembrane (1) TRANSMEM 947 967 Helical. {ECO:0000255}. TOPO_DOM 28 748 Extracellular. {ECO:0000305}.; TOPO_DOM 753 946 Extracellular. {ECO:0000305}.; TOPO_DOM 968 1372 Cytoplasmic. {ECO:0000305}. FUNCTION: Receptor tyrosine kinase which mediates the pleiotropic actions of insulin. Binding of insulin leads to phosphorylation of several intracellular substrates, including, insulin receptor substrates (IRS1, 2, 3, 4), SHC, GAB1, CBL and other signaling intermediates. Each of these phosphorylated proteins serve as docking proteins for other signaling proteins that contain Src-homology-2 domains (SH2 domain) that specifically recognize different phosphotyrosine residues, including the p85 regulatory subunit of PI3K and SHP2. Phosphorylation of IRSs proteins lead to the activation of two main signaling pathways: the PI3K-AKT/PKB pathway, which is responsible for most of the metabolic actions of insulin, and the Ras-MAPK pathway, which regulates expression of some genes and cooperates with the PI3K pathway to control cell growth and differentiation. Binding of the SH2 domains of PI3K to phosphotyrosines on IRS1 leads to the activation of PI3K and the generation of phosphatidylinositol-(3, 4, 5)-triphosphate (PIP3), a lipid second messenger, which activates several PIP3-dependent serine/threonine kinases, such as PDPK1 and subsequently AKT/PKB. The net effect of this pathway is to produce a translocation of the glucose transporter SLC2A4/GLUT4 from cytoplasmic vesicles to the cell membrane to facilitate glucose transport. Moreover, upon insulin stimulation, activated AKT/PKB is responsible for: anti-apoptotic effect of insulin by inducing phosphorylation of BAD; regulates the expression of gluconeogenic and lipogenic enzymes by controlling the activity of the winged helix or forkhead (FOX) class of transcription factors. Another pathway regulated by PI3K-AKT/PKB activation is mTORC1 signaling pathway which regulates cell growth and metabolism and integrates signals from insulin. AKT mediates insulin-stimulated protein synthesis by phosphorylating TSC2 thereby activating mTORC1 pathway. The Ras/RAF/MAP2K/MAPK pathway is mainly involved in mediating cell growth, survival and cellular differentiation of insulin. Phosphorylated IRS1 recruits GRB2/SOS complex, which triggers the activation of the Ras/RAF/MAP2K/MAPK pathway. In addition to binding insulin, the insulin receptor can bind insulin-like growth factors (IGFI and IGFII). When present in a hybrid receptor with IGF1R, binds IGF1 (By similarity). {ECO:0000250}. PTM: Autophosphorylated on tyrosine residues in response to insulin (By similarity). Phosphorylation of Tyr-989 is required for IRS1-, SHC1-, and STAT5B-binding (By similarity). Dephosphorylated by PTPRE on Tyr-989, Tyr-1175, Tyr-1179 and Tyr-1180 residues (By similarity). Dephosphorylated by PTPRF and PTPN1 (By similarity). Dephosphorylated by PTPN2; down-regulates insulin-induced signaling. {ECO:0000250, ECO:0000269|PubMed:12612081}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SUBUNIT: Tetramer of 2 alpha and 2 beta chains linked by disulfide bonds. The alpha chains carry the insulin-binding regions, while the beta chains carry the kinase domain. Forms a hybrid receptor with IGF1R, the hybrid is a tetramer consisting of 1 alpha chain and 1 beta chain of INSR and 1 alpha chain and 1 beta chain of IGF1R. Interacts with SORBS1 but dissociates from it following insulin stimulation. Binds SH2B2 (By similarity). Activated form of INSR interacts (via Tyr-989) with the PTB/PID domains of IRS1 and SHC1. The sequences surrounding the phosphorylated NPXY motif contribute differentially to either IRS1 or SHC1 recognition. Interacts (via tyrosines in the C-terminus) with IRS2 (via PTB domain and 591-786 AA); the 591-786 would be the primary anchor of IRS2 to INSR while the PTB domain would have a stabilizing action on the interaction with INSR. Interacts with the SH2 domains of the 85 kDa regulatory subunit of PI3K (PIK3R1) in vitro, when autophosphorylated on tyrosine residues. Interacts with SOCS7 (By similarity). Interacts (via the phosphorylated Tyr-989), with SOCS3. Interacts (via the phosphorylated Tyr-1175, Tyr-1179, Tyr-1180) with SOCS1. Interacts with CAV2 (tyrosine-phosphorylated form); the interaction is increased with 'Tyr-27'phosphorylation of CAV2 (By similarity). Interacts with ARRB2. Interacts with GRB10; this interaction blocks the association between IRS1/IRS2 and INSR, significantly reduces insulin-stimulated tyrosine phosphorylation of IRS1 and IRS2 and thus decreases insulin signaling (By similarity). Interacts with GRB7 (By similarity). Interacts with PDPK1 (By similarity). Interacts (via Tyr-1180) with GRB14 (via BPS domain); this interaction protects the tyrosines in the activation loop from dephosphorylation, but promotes dephosphorylation of Tyr-989, this results in decreased interaction with, and phosphorylation of, IRS1 (By similarity). Interacts (via subunit alpha) with ENPP1 (via 485-599 AA); this interaction blocks autophosphorylation (By similarity). Interacts with PTPRE; this interaction is dependent of Tyr-1175, Tyr-1179 and Tyr-1180 of the INSR (By similarity). Interacts with STAT5B (via SH2 domain) (By similarity). Interacts with PTPRF (By similarity). {ECO:0000250}. DOMAIN: The tetrameric insulin receptor binds insulin via non-identical regions from two alpha chains, primarily via the C-terminal region of the first INSR alpha chain. Residues from the leucine-rich N-terminus of the other INSR alpha chain also contribute to this insulin binding site. A secondary insulin-binding site is formed by residues at the junction of fibronectin type-III domain 1 and 2 (By similarity). {ECO:0000250}. +Q9CWS4 INT11_MOUSE Integrator complex subunit 11 (Int11) (EC 3.1.27.-) (Cleavage and polyadenylation-specific factor 3-like protein) (CPSF3-like protein) 600 67,844 Chain (1); Erroneous initiation (1); Motif (1); Sequence conflict (3) FUNCTION: Catalytic component of the Integrator complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes. Mediates the snRNAs 3' cleavage. Mediates recruitment of cytoplasmic dynein to the nuclear envelope, probably as component of the INT complex. {ECO:0000250|UniProtKB:Q5TA45}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5TA45}. Cytoplasm {ECO:0000250|UniProtKB:Q5TA45}. SUBUNIT: Belongs to the multiprotein complex Integrator, at least composed of INTS1, INTS2, INTS3, INTS4, INTS5, INTS6, INTS7, INTS8, INTS9/RC74, INTS10, INTS11/CPSF3L and INTS12. {ECO:0000250|UniProtKB:Q5TA45}. DOMAIN: The HXHXDH motif is essential for the endoribonuclease activity of the CPSF complex. {ECO:0000250|UniProtKB:Q9VAH9}. +Q8CHT3 INT5_MOUSE Integrator complex subunit 5 (Int5) 1018 108,348 Chain (1); Initiator methionine (1); Modified residue (2); Sequence conflict (2); Transmembrane (3) TRANSMEM 533 553 Helical. {ECO:0000255}.; TRANSMEM 855 875 Helical. {ECO:0000255}.; TRANSMEM 929 949 Helical. {ECO:0000255}. FUNCTION: Component of the Integrator (INT) complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes. Mediates recruitment of cytoplasmic dynein to the nuclear envelope, probably as component of the INT complex. {ECO:0000250|UniProtKB:Q6P9B9}. SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. Nucleus {ECO:0000250|UniProtKB:Q6P9B9}. Cytoplasm {ECO:0000250|UniProtKB:Q6P9B9}. SUBUNIT: Belongs to the multiprotein complex Integrator, at least composed of INTS1, INTS2, INTS3, INTS4, INTS5, INTS6, INTS7, INTS8, INTS9/RC74, INTS10, INTS11/CPSF3L and INTS12. {ECO:0000250|UniProtKB:Q6P9B9}. +Q059U7 INTU_MOUSE Protein inturned (Inturned planar cell polarity effector homolog) (PDZ domain-containing protein 6) 942 104,821 Alternative sequence (3); Chain (1); Domain (1); Modified residue (2); Sequence conflict (1) FUNCTION: Plays a key role in ciliogenesis and embryonic development. Regulator of cilia formation by controlling the organization of the apical actin cytoskeleton and the positioning of the basal bodies at the apical cell surface, which in turn is essential for the normal orientation of elongating ciliary microtubules. Plays a key role in definition of cell polarity via its role in ciliogenesis but not via conversion extension. Has an indirect effect on hedgehog signaling (PubMed:20067783, PubMed:21761479). Proposed to function as core component of the CPLANE (ciliogenesis and planar polarity effectors) complex involved in the recruitment of peripheral IFT-A proteins to basal bodies (By similarity). {ECO:0000250|UniProtKB:Q9ULD6, ECO:0000269|PubMed:20067783, ECO:0000269|PubMed:21761479}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20067783}. Cell surface {ECO:0000250|UniProtKB:Q2I0E5}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q2I0E5}. Note=Enriched at the apical surface in ciliated cells. SUBUNIT: Interacts with CPLANE1. Interacts with FUZ and WDPCP; FUZ, INTU and WDPCP probably form the core CPLANE (ciliogenesis and planar polarity effectors) complex. {ECO:0000269|PubMed:27158779}. TISSUE SPECIFICITY: Widely expressed in E8.5 and E9.5 wild type embryos. Present in various adult organs (at protein level). {ECO:0000269|PubMed:20067783}. +Q80V86 INT8_MOUSE Integrator complex subunit 8 (Int8) 995 113,353 Chain (1); Erroneous initiation (2); Frameshift (1); Modified residue (1); Repeat (4); Sequence conflict (4) FUNCTION: Component of the Integrator complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q75QN2}. SUBUNIT: Belongs to the multiprotein complex Integrator, at least composed of INTS1, INTS2, INTS3, INTS4, INTS5, INTS6, INTS7, INTS8, INTS9/RC74, INTS10, INTS11/CPSF3L and INTS12. {ECO:0000250|UniProtKB:Q75QN2}. +Q9DCX1 MD2BP_MOUSE MAD2L1-binding protein 276 31,140 Chain (1); Region (1); Sequence conflict (2) FUNCTION: May function to silence the spindle checkpoint and allow mitosis to proceed through anaphase by binding MAD2L1 after it has become dissociated from the MAD2L1-CDC20 complex. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=During early mitosis, unevenly distributed throughout the nucleoplasm. From metaphase to anaphase, concentrated on the spindle (By similarity). {ECO:0000250}. SUBUNIT: Interacts with MAD2L1. {ECO:0000250}. +Q9Z1B5 MD2L1_MOUSE Mitotic spindle assembly checkpoint protein MAD2A (Mitotic arrest deficient 2-like protein 1) (MAD2-like protein 1) 205 23,598 Chain (1); Domain (1); Initiator methionine (1); Modified residue (5); Region (1); Sequence conflict (3) FUNCTION: Component of the spindle-assembly checkpoint that prevents the onset of anaphase until all chromosomes are properly aligned at the metaphase plate. Required for the execution of the mitotic checkpoint which monitors the process of kinetochore-spindle attachment and inhibits the activity of the anaphase promoting complex by sequestering CDC20 until all chromosomes are aligned at the metaphase plate (By similarity). {ECO:0000250}. PTM: Phosphorylated on multiple serine residues. The level of phosphorylation varies during the cell cycle and is highest during mitosis. Phosphorylation abolishes interaction with MAD1L1 and reduces interaction with CDC20. Phosphorylated by NEK2 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. Note=Recruited by MAD1L1 to unattached kinetochores (By similarity). Recruited to the nuclear pore complex by TPR during interphase (By similarity). Recruited to kinetochores in late prometaphase after BUB1, CENPF, BUB1B and CENPE. Kinetochore association requires the presence of NEK2 (By similarity). {ECO:0000250}. SUBUNIT: Monomer and homodimer. Heterotetramer with MAD1L1. Formation of a heterotetrameric core complex containing two molecules each of MAD1L1 and of MAD2L1 promotes binding of another molecule of MAD2L1 to each MAD2L1, resulting in a heterohexamer. Interacts with CDC20, MAD2L1BP and with ADAM17/TACE. Dimeric MAD2L1 in the closed conformation interacts with CDC20. Monomeric MAD2L1 in the open conformation does not interact with CDC20. CDC20 competes with MAD1L1 for MAD2L1 binding. Interacts with TPR. Binds to UBD (via ubiquitin-like 1 domain) during mitosis. Kinetochore association is repressed by UBD (By similarity). Interacts with NEK2 (By similarity). Interacts with HSF1; this interaction occurs in mitosis (By similarity). {ECO:0000250|UniProtKB:Q13257}. DOMAIN: The protein has two highly different native conformations, an inactive open conformation that cannot bind CDC20 and that predominates in cytosolic monomers, and an active closed conformation. The protein in the closed conformation preferentially dimerizes with another molecule in the open conformation, but can also form a dimer with a molecule in the closed conformation. Formation of a heterotetrameric core complex containing two molecules of MAD1L1 and of MAD2L1 in the closed conformation promotes binding of another molecule of MAD2L1 in the open conformation and the conversion of the open to the closed form, and thereby promotes interaction with CDC20 (By similarity). {ECO:0000250}. +Q8BP00 IQCB1_MOUSE IQ calmodulin-binding motif-containing protein 1 598 68,734 Alternative sequence (1); Chain (1); Coiled coil (1); Domain (4); Region (3); Sequence conflict (5) FUNCTION: Involved in ciliogenesis. The function in an early step in cilia formation depends on its association with CEP290/NPHP6 (By similarity). Involved in regulation of the BBSome complex integrity, specifically for presence of BBS2 and BBS5 in the complex, and in ciliary targeting of selected BBSome cargos. May play a role in controlling entry of the BBSome complex to cilia possibly implicating CEP290/NPHP6 (By similarity). {ECO:0000250|UniProtKB:Q15051, ECO:0000269|PubMed:21565611}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q15051}. Note=Localization to the centrosome depends on the interaction with CEP290. {ECO:0000250|UniProtKB:Q15051}. SUBUNIT: Interacts with calmodulin (PubMed:15723066). Interacts with CEP290/NPHP6; IQCB1/NPHP5 and CEP290/NPHP6; are proposed to form a functional NPHP5-6 module localized to the centrosome. Interacts with ATXN10. Interacts with NPHP1, INVS, NPHP4 and RPGRIP1L; these interactions likely require additional interactors (PubMed:21565611). Associates with the BBSome complex; interacts with BBS1, BBS2, BBS4, BBS5, BBS7, BBS8 and BBS9 (By similarity). {ECO:0000250|UniProtKB:Q15051, ECO:0000269|PubMed:15723066, ECO:0000269|PubMed:21565611}. DOMAIN: The IQ domains mediate the interaction with calmodulin. {ECO:0000250|UniProtKB:Q15051}. TISSUE SPECIFICITY: Localized to the outer segment and connecting cilia of photoreceptor cells. {ECO:0000269|PubMed:15723066}. +Q6PCQ0 IQCE_MOUSE IQ domain-containing protein E 778 86,356 Alternative sequence (4); Chain (1); Coiled coil (2); Compositional bias (1); Domain (2); Modified residue (2); Sequence conflict (1) FUNCTION: Component of the EvC complex that positively regulates ciliary Hedgehog (Hh) signaling (PubMed:24582806). Required for proper limb morphogenesis (By similarity). {ECO:0000250|UniProtKB:Q6IPM2, ECO:0000269|PubMed:24582806}. SUBCELLULAR LOCATION: Cell projection, cilium membrane {ECO:0000269|PubMed:24582806}; Peripheral membrane protein {ECO:0000269|PubMed:24582806}; Cytoplasmic side {ECO:0000269|PubMed:24582806}. Note=The EvC complex localizes at the base of cilia in the EvC zone of primary cilia in a EFCAB7-dependent manner (PubMed:24582806). {ECO:0000269|PubMed:24582806}. SUBUNIT: Component of the EvC complex composed of EFCAB7, IQCE, EVC2 and EVC; built from two subcomplexes, EVC2:EVC and EFCAB7:IQCE (PubMed:24582806). Interacts (via N-terminus) with EFCAB7 (via EF-hands 1 and 2); this interaction anchors the EVC-EVC2 complex in a signaling microdomain at the base of cilia and stimulates the Hedgehog (Hh) pathway. Interacts with EVC2 (via N-terminal end) (PubMed:24582806). Interacts with EVC (PubMed:24582806). {ECO:0000269|PubMed:24582806}. +Q9DAL7 IQCF5_MOUSE IQ domain-containing protein F5 148 17,809 Chain (1); Domain (2) +Q8BPW0 IQCJ_MOUSE IQ domain-containing protein J 110 12,662 Chain (1); Domain (1) +Q3UQ44 IQGA2_MOUSE Ras GTPase-activating-like protein IQGAP2 1575 180,528 Chain (1); Domain (6); Frameshift (1); Modified residue (10); Sequence conflict (2) FUNCTION: Binds to activated CDC42 and RAC1 but does not seem to stimulate their GTPase activity. Associates with calmodulin. +A0A088MLT8 IQIP1_MOUSE IQCJ-SCHIP1 readthrough transcript protein 559 61,917 Alternative sequence (1); Chain (1); Coiled coil (1); Compositional bias (1); Domain (1); Mutagenesis (1); Region (1) FUNCTION: May play a role in action potential conduction in myelinated cells through the organization of molecular complexes at nodes of Ranvier and axon initial segments (PubMed:25953347, PubMed:25950943, PubMed:27979964). May also play a role in axon outgrowth and guidance (PubMed:25953347). {ECO:0000269|PubMed:25950943, ECO:0000269|PubMed:25953347, ECO:0000269|PubMed:27979964}. SUBCELLULAR LOCATION: Cell projection, axon {ECO:0000269|PubMed:18550753}. Cytoplasm {ECO:0000250|UniProtKB:B3KU38}. Note=Localizes to the axon initial segments (AIS) and nodes of Ranvier of neurons and is absent from dendrites. {ECO:0000269|PubMed:18550753}. SUBUNIT: Homooligomer (via coiled coil domain) (PubMed:27979964). Interacts (via IQ domain) with calmodulin; the interaction is direct and lost in presence of calcium (PubMed:18550753). Interacts with ANK3 (via ANK repeats); required for its localization at axon initial segments (AIS) and nodes of Ranvier (PubMed:18550753). Interacts with SPTBN4 (PubMed:27979964). Interacts with KCNQ2 and KCNQ3 (PubMed:27979964). {ECO:0000269|PubMed:18550753, ECO:0000269|PubMed:27979964}. +Q9CR20 IR3IP_MOUSE Immediate early response 3-interacting protein 1 82 9,017 Chain (1); Transmembrane (2) TRANSMEM 2 22 Helical. {ECO:0000255}.; TRANSMEM 62 82 Helical. {ECO:0000255}. FUNCTION: May be implicated in the regulation of apoptosis. May be involved in protein transport between endoplasmic reticulum and Golgi apparatus. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q62406 IRAK1_MOUSE Interleukin-1 receptor-associated kinase 1 (IRAK) (IRAK-1) (EC 2.7.11.1) (Pelle-like protein kinase) (mPLK) 710 77,269 Active site (1); Alternative sequence (1); Binding site (2); Chain (1); Cross-link (2); Domain (2); Erroneous initiation (1); Modified residue (6); Mutagenesis (2); Nucleotide binding (2); Region (1); Sequence conflict (1) FUNCTION: Serine/threonine-protein kinase that plays a critical role in initiating innate immune response against foreign pathogens. Involved in Toll-like receptor (TLR) and IL-1R signaling pathways. Is rapidly recruited by MYD88 to the receptor-signaling complex upon TLR activation. Association with MYD88 leads to IRAK1 phosphorylation by IRAK4 and subsequent autophosphorylation and kinase activation. Phosphorylates E3 ubiquitin ligases Pellino proteins (PELI1, PELI2 and PELI3) to promote pellino-mediated polyubiquitination of IRAK1. Then, the ubiquitin-binding domain of IKBKG/NEMO binds to polyubiquitinated IRAK1 bringing together the IRAK1-MAP3K7/TAK1-TRAF6 complex and the NEMO-IKKA-IKKB complex. In turn, MAP3K7/TAK1 activates IKKs (CHUK/IKKA and IKBKB/IKKB) leading to NF-kappa-B nuclear translocation and activation. Alternatively, phosphorylates TIRAP to promote its ubiquitination and subsequent degradation. Phosphorylates the interferon regulatory factor 7 (IRF7) to induce its activation and translocation to the nucleus, resulting in transcriptional activation of type I IFN genes, which drive the cell in an antiviral state. When sumoylated, translocates to the nucleus and phosphorylates STAT3 (By similarity). {ECO:0000250, ECO:0000269|PubMed:8663605}. PTM: Following recruitment on the activated receptor complex, phosphorylated on Thr-209, probably by IRAK4, resulting in a conformational change of the kinase domain, allowing further phosphorylations to take place. Thr-387 phosphorylation in the activation loop is required to achieve full enzymatic activity (By similarity). {ECO:0000250}.; PTM: Polyubiquitinated by TRAF6 after cell stimulation with IL-1-beta by PELI1, PELI2 and PELI3. Polyubiquitination occurs with polyubiquitin chains linked through 'Lys-63'. Ubiquitination promotes interaction with NEMO/IKBKG. Also sumoylated; leading to nuclear translocation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Lipid droplet {ECO:0000269|PubMed:21435586}. Note=Translocates to the nucleus when sumoylated (By similarity). RSAD2/viperin recruits it to the lipid droplet. {ECO:0000250}. SUBUNIT: Homodimer (By similarity). Forms a complex with TRAF6, PELI1, IRAK4 and MYD88 (PubMed:16951688). Direct binding of SMAD6 to PELI1 prevents complex formation and hence negatively regulates IL1R-TLR signaling and eventually NF-kappa-B-mediated gene expression (By similarity). The TRAF6-PELI1-IRAK4-MYD88 complex recruits MAP3K7/TAK1, TAB1 and TAB2 to mediate NF-kappa-B activation (By similarity). Interaction with MYD88 recruits IRAK1 to the stimulated receptor complex (By similarity). Interacts with TOLLIP; this interaction occurs in the cytosol prior to receptor activation (By similarity). Interacts with IL1RL1 (By similarity). Interacts (when polyubiquitinated) with IKBKG/NEMO (By similarity). Interacts with RSAD2/viperin (PubMed:21435586). Interacts with IRAK1BP1 (PubMed:11096118). Interacts with PELI2 (PubMed:12370331). Interacts with ZC3H12A; this interaction increases the interaction between ZC3H12A and IKBKB/IKKB (PubMed:22037600). Interacts with IRAK4 (By similarity). Interacts with PELI3 (By similarity). Interacts with PELI1 and TRAF6 (By similarity). Interacts with INAVA; the interaction takes place upon PRR stimulation (By similarity). {ECO:0000250|UniProtKB:P51617, ECO:0000269|PubMed:11096118, ECO:0000269|PubMed:12370331, ECO:0000269|PubMed:16951688, ECO:0000269|PubMed:21435586, ECO:0000269|PubMed:22037600}. DOMAIN: The ProST region is composed of many proline and serine residues (more than 20 of each) and some threonines. This region is the site of IRAK-1 hyperphosphorylation (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in liver, followed by kidney and skeletal muscle. {ECO:0000269|PubMed:8663605}. +Q3HNM7 INSC_MOUSE Protein inscuteable homolog (Minsc) 579 63,615 Alternative sequence (1); Chain (1); Helix (1); Motif (1); Mutagenesis (4); Region (1); Sequence conflict (1) FUNCTION: May function as an adapter linking the Par3 complex to the GPSM1/GPSM2 complex. Involved in spindle orientation during mitosis (PubMed:16301171, PubMed:21816348). May regulate cell proliferation and differentiation in the developing nervous system (PubMed:16301171). May play a role in the asymmetric division of fibroblasts and participate in the process of stratification of the squamous epithelium (PubMed:16094321). {ECO:0000269|PubMed:16094321, ECO:0000269|PubMed:16301171, ECO:0000269|PubMed:21816348}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16094321, ECO:0000269|PubMed:16301171, ECO:0000269|PubMed:21816348}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q1MX18}. Note=Uniformly distributed in the cytoplasm during interphase. During metaphase, detected in the cell cortex, adjacent to the mitotic spindle poles. {ECO:0000250|UniProtKB:Q1MX18}. SUBUNIT: Interacts with ALS2CR19/PAR3-beta and GPSM1/AGS3 (By similarity). Interacts with F2RL2/PAR3 (PubMed:16094321). Interacts with GPSM2/LGN (via TPR repeat region) (PubMed:16094321, PubMed:21816348). {ECO:0000250|UniProtKB:Q1MX18, ECO:0000269|PubMed:16094321, ECO:0000269|PubMed:21816348}. TISSUE SPECIFICITY: Expressed in brain, kidney, liver, testis and skin. {ECO:0000269|PubMed:16094321, ECO:0000269|PubMed:16301171}. +P01326 INS2_MOUSE Insulin-2 [Cleaved into: Insulin-2 B chain; Insulin-2 A chain] 110 12,364 Disulfide bond (3); Peptide (2); Propeptide (1); Signal peptide (1) FUNCTION: Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Heterodimer of a B chain and an A chain linked by two disulfide bonds. {ECO:0000250|UniProtKB:P01308}. +Q9JMC2 INSM2_MOUSE Insulinoma-associated protein 2 (Methylated in liver tumor 1) 493 52,225 Chain (1); Region (1); Sequence conflict (2); Zinc finger (5) FUNCTION: May function as a growth suppressor or tumor suppressor in liver cells and in certain neurons. {ECO:0000269|PubMed:11221845}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21343251}. Nucleus {ECO:0000269|PubMed:21343251}. TISSUE SPECIFICITY: Expressed in spleen, stomach, liver, kidney and testis. In the pancreas, expressed in islet cells, including insulin-producing beta-cells, but not in acinar cells (at protein level). In the brain, expressed in the neuronal cells of the cerebral cortex, the Purkinje cells of the cerebellum and the hippocampal region including CA1 and CA3 (at protein level). {ECO:0000269|PubMed:11221845, ECO:0000269|PubMed:21343251}. +Q8K2A7 INT10_MOUSE Integrator complex subunit 10 (Int10) 710 82,020 Chain (1); Compositional bias (1); Cross-link (1); Erroneous initiation (1); Modified residue (3); Sequence conflict (3) FUNCTION: Component of the Integrator (INT) complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes. May be not involved in the recruitment of cytoplasmic dynein to the nuclear envelope by different components of the INT complex. {ECO:0000250|UniProtKB:Q9NVR2}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NVR2}. SUBUNIT: Belongs to the multiprotein complex Integrator, at least composed of INTS1, INTS2, INTS3, INTS4, INTS5, INTS6, INTS7, INTS8, INTS9/RC74, INTS10, INTS11/CPSF3L and INTS12. Interacts with POLR2A. {ECO:0000250|UniProtKB:Q9NVR2}. +Q9QY05 INSL6_MOUSE Insulin-like peptide INSL6 (Insulin-like peptide 6) [Cleaved into: Insulin-like peptide INSL6 B chain; Insulin-like peptide INSL6 A chain] 191 22,215 Chain (1); Disulfide bond (3); Peptide (2); Propeptide (1); Signal peptide (1) FUNCTION: May have a role in sperm development and fertilization. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +Q8C5L6 INP5K_MOUSE Inositol polyphosphate 5-phosphatase K (EC 3.1.3.56) (Skeletal muscle and kidney-enriched inositol phosphatase) 468 54,159 Chain (1); Region (3); Sequence conflict (1) FUNCTION: Inositol 5-phosphatase which acts on inositol 1,4,5-trisphosphate, inositol 1,3,4,5-tetrakisphosphate, phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate. Has 6-fold higher affinity for phosphatidylinositol 4,5-bisphosphate than for inositol 1,4,5-trisphosphate (By similarity). Negatively regulates assembly of the actin cytoskeleton. Controls insulin-dependent glucose uptake among inositol 3,4,5-trisphosphate phosphatases; therefore, is the specific regulator for insulin signaling in skeletal muscle (PubMed:22247557, PubMed:22751929). {ECO:0000250|UniProtKB:Q9BT40, ECO:0000269|PubMed:22247557, ECO:0000269|PubMed:22751929}. SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:22247557, ECO:0000269|PubMed:22751929}. Note=Following stimulation with EGF, translocates to membrane ruffles. {ECO:0000250|UniProtKB:Q9BT40}. SUBUNIT: Interacts with GPR78; necessary for INPP5K localization at the endoplasmic reticulum. Interacts with PAK1; competes with GPR78. {ECO:0000250|UniProtKB:Q9BT40}. TISSUE SPECIFICITY: Expressed in the skeletal muscle and the eye. {ECO:0000269|PubMed:28190456}. +Q3USH1 INSY2_MOUSE Inhibitory synaptic factor 2A (InSyn2) 422 46,222 Chain (1); Coiled coil (1); Modified residue (1) FUNCTION: Component of the protein machinery at the inhibitory synapses, probably acting as a scaffold. Inhibitory synapses dampen neuronal activity through postsynaptic hyperpolarization. This synaptic inhibition is fundamental for the functioning of the central nervous system, shaping and orchestrating the flow of information through neuronal networks to generate a precise neural code. {ECO:0000269|PubMed:27609886}. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000269|PubMed:27609886}. SUBUNIT: Interacts with GPHN. {ECO:0000269|PubMed:27609886}. +Q7TPD0 INT3_MOUSE Integrator complex subunit 3 (Int3) (SOSS complex subunit A) (Sensor of single-strand DNA complex subunit A) (SOSS-A) (Sensor of ssDNA subunit A) 1041 117,938 Alternative sequence (2); Chain (1); Compositional bias (1); Erroneous initiation (1); Modified residue (4); Sequence conflict (2) FUNCTION: Component of the Integrator (INT) complex. The Integrator complex is involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes. Mediates recruitment of cytoplasmic dynein to the nuclear envelope, probably as component of the INT complex. {ECO:0000250|UniProtKB:Q68E01}.; FUNCTION: Component of the SOSS complex, a multiprotein complex that functions downstream of the MRN complex to promote DNA repair and G2/M checkpoint. The SOSS complex associates with single-stranded DNA at DNA lesions and influences diverse endpoints in the cellular DNA damage response including cell-cycle checkpoint activation, recombinational repair and maintenance of genomic stability. The SOSS complex is required for efficient homologous recombination-dependent repair of double-strand breaks (DSBs) and ATM-dependent signaling pathways. In the SOSS complex, it is required for the assembly of the complex and for stabilization of the complex at DNA damage sites. {ECO:0000250|UniProtKB:Q68E01}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q68E01}. Cytoplasm {ECO:0000250|UniProtKB:Q68E01}. Note=Localizes to nuclear foci following DNA damage. {ECO:0000250|UniProtKB:Q68E01}. SUBUNIT: Belongs to the multiprotein complex Integrator, at least composed of INTS1, INTS2, INTS3, INTS4, INTS5, INTS6, INTS7, INTS8, INTS9/RC74, INTS10, INTS11/CPSF3L and INTS12. Component of the SOSS complex, composed of SOSS-B (SOSS-B1/NABP2 or SOSS-B2/NABP1), SOSS-A/INTS3 and SOSS-C/INIP. SOSS complexes containing SOSS-B1/NABP2 are more abundant than complexes containing SOSS-B2/NABP1. Interacts with SOSS-B1/NABP2, SOSS-B2/NABP1 and SOSS-C/INIP; the interaction is direct. Interacts with NBN/NBS1. {ECO:0000250|UniProtKB:Q68E01}. +P15265 MCSP_MOUSE Sperm mitochondrial-associated cysteine-rich protein 143 14,945 Chain (1); Erroneous initiation (5); Modified residue (4) FUNCTION: Involved in sperm motility. Its absence is associated with genetic background dependent male infertility. Infertility may be due to reduced sperm motility in the female reproductive tract and inability to penetrate the oocyte zona pellucida. {ECO:0000269|PubMed:11940662}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8916043}. Mitochondrion membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Becomes associated with the spermatid mitochondrion capsule at step 16 of spermatogenesis. TISSUE SPECIFICITY: Testis. Is selectively expressed in the spermatids of seminiferous tubules. {ECO:0000269|PubMed:2303168, ECO:0000269|PubMed:8916043, ECO:0000269|PubMed:9409512}. +E9PV86 MCTP1_MOUSE Multiple C2 and transmembrane domain-containing protein 1 951 106,795 Chain (1); Compositional bias (1); Domain (3); Transmembrane (2) TRANSMEM 763 783 Helical. {ECO:0000255}.; TRANSMEM 866 886 Helical. {ECO:0000255}. FUNCTION: Calcium sensor which is essential for the stabilization of normal baseline neurotransmitter release and for the induction and long-term maintenance of presynaptic homeostatic plasticity. {ECO:0000250|UniProtKB:A1ZBD6}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:D4ABL6}; Multi-pass membrane protein {ECO:0000255}. Recycling endosome {ECO:0000250|UniProtKB:D4ABL6}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:A1ZBD6}. +Q9DB27 MCTS1_MOUSE Malignant T-cell-amplified sequence 1 (MCT-1) (Multiple copies T-cell malignancies 1) 181 20,555 Alternative sequence (1); Chain (1); Domain (1); Modified residue (2) FUNCTION: Anti-oncogene that plays a role in cell cycle regulation; decreases cell doubling time and anchorage-dependent growth; shortens the duration of G1 transit time and G1/S transition. When constitutively expressed, increases CDK4 and CDK6 kinases activity and CCND1/cyclin D1 protein level, as well as G1 cyclin/CDK complex formation. Involved in translation initiation; promotes recruitment of aminoacetyled initiator tRNA to P site of 40S ribosomes. Can promote release of deacylated tRNA and mRNA from recycled 40S subunits following ABCE1-mediated dissociation of post-termination ribosomal complexes into subunits. Plays a role as translation enhancer; recruits the density-regulated protein/DENR and binds to the cap complex of the 5'-terminus of mRNAs, subsequently altering the mRNA translation profile; up-regulates protein levels of BCL2L2, TFDP1, MRE11, CCND1 and E2F1, while mRNA levels remains constant. Hyperactivates DNA damage signaling pathway; increased gamma-irradiation-induced phosphorylation of histone H2AX, and induces damage foci formation. Increases the overall number of chromosomal abnormalities such as larger chromosomes formation and multiples chromosomal fusions when overexpressed in gamma-irradiated cells. May play a role in promoting lymphoid tumor development: lymphoid cell lines overexpressing MCTS1 exhibit increased growth rates and display increased protection against apoptosis. May contribute to the pathogenesis and progression of breast cancer via promotion of angiogenesis through the decline of inhibitory THBS1/thrombospondin-1, and inhibition of apoptosis. Involved in the process of proteasome degradation to down-regulate Tumor suppressor p53/TP53 in breast cancer cell; Positively regulates phosphorylation of MAPK1 and MAPK3 (By similarity). {ECO:0000250}. PTM: Phosphorylation is critical for stabilization and promotion of cell proliferation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Interacts (via PUA domain) with DENR. {ECO:0000250}. DOMAIN: The PUA RNA-binding domain is critical for cap binding, but not sufficient for translation enhancer function. MCT1 N-terminal region is required to enhance translation possibly through interaction with other proteins (By similarity). {ECO:0000250}. +Q9CQ21 MCTS2_MOUSE Malignant T-cell-amplified sequence 2 (MCT-2) (Multiple copies T-cell malignancies 2) 181 20,437 Chain (1); Domain (1) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. DOMAIN: The PUA RNA-binding domain is critical for cap binding, but not sufficient for translation enhancer function. MCT1 N-terminal region is required to enhance translation possibly through interaction with other proteins. +Q9Z1Y9 IOD2_MOUSE Type II iodothyronine deiodinase (EC 1.21.99.4) (5DII) (DIOII) (Type 2 DI) (Type-II 5'-deiodinase) 266 29,929 Active site (1); Chain (1); Non-standard residue (2); Transmembrane (1) TRANSMEM 10 34 Helical. {ECO:0000255}. FUNCTION: Responsible for the deiodination of T4 (3,5,3',5'-tetraiodothyronine) into T3 (3,5,3'-triiodothyronine). Essential for providing the brain with appropriate levels of T3 during the critical period of development. {ECO:0000250}. PTM: Ubiquitinated by MARCH6, leading to its degradation by the proteasome. Deubiquitinated by USP20 and USP33 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. SUBUNIT: Interacts with USP20 and USP33. Interacts with MARCH6 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in mammary gland and in brain. {ECO:0000269|PubMed:10715551}. +Q810S1 MCUB_MOUSE Calcium uniporter regulatory subunit MCUb, mitochondrial (MCUb) (Coiled-coil domain-containing protein 109B) 345 39,799 Chain (1); Coiled coil (2); Erroneous initiation (1); Sequence conflict (5); Transit peptide (1); Transmembrane (2) TRANSMEM 229 249 Helical. {ECO:0000255}.; TRANSMEM 259 279 Helical. {ECO:0000255}. FUNCTION: Negatively regulates the activity of MCU, the mitochondrial inner membrane calcium uniporter, and thereby modulates calcium uptake into the mitochondrion. Does not form functional calcium channels by itself. Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenergetics, cytoplasmic calcium signals and activation of cell death pathways. {ECO:0000269|PubMed:23900286}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:23900286}; Multi-pass membrane protein {ECO:0000269|PubMed:23900286}. SUBUNIT: Component of the uniplex complex, composed of MCU, MCUB, MICU1, MICU2 and EMRE/SMDT1 (By similarity). Heterooligomer with MCU; this reduces MCU channel activity. Homooligomer. {ECO:0000250|UniProtKB:Q9NWR8, ECO:0000269|PubMed:23900286}. TISSUE SPECIFICITY: Detected in lung, brain and heart, and at lower levels in white fat, skeletal muscle and spleen. Detected at very low levels in kidney and liver. {ECO:0000269|PubMed:23900286}. +Q9CXD6 MCUR1_MOUSE Mitochondrial calcium uniporter regulator 1 (MCU regulator 1) (Coiled-coil domain-containing protein 90A, mitochondrial) 340 37,849 Alternative sequence (3); Chain (1); Coiled coil (1); Modified residue (1); Sequence conflict (1); Topological domain (3); Transmembrane (2) TRANSMEM 55 74 Helical. {ECO:0000255}.; TRANSMEM 317 339 Helical. {ECO:0000255}. TOPO_DOM 1 54 Mitochondrial intermembrane. {ECO:0000250|UniProtKB:Q96AQ8}.; TOPO_DOM 75 316 Mitochondrial matrix. {ECO:0000250|UniProtKB:Q96AQ8}.; TOPO_DOM 340 340 Mitochondrial intermembrane. {ECO:0000250|UniProtKB:Q96AQ8}. FUNCTION: Key regulator of mitochondrial calcium uniporter (MCU) required for calcium entry into mitochondrion. Plays a direct role in uniporter-mediated calcium uptake via a direct interaction with MCU. Probably involved in the assembly of the membrane components of the uniporter complex (uniplex). {ECO:0000250|UniProtKB:Q96AQ8}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q96AQ8}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q96AQ8}. SUBUNIT: Interacts (via coiled coil regions) with MCU; the interaction is direct. Interacts with SMDT1/EMRE; the interaction is direct. Interacts with PPIF. {ECO:0000250|UniProtKB:Q96AQ8}. +Q3UMR5 MCU_MOUSE Calcium uniporter protein, mitochondrial 350 39,682 Alternative sequence (2); Chain (1); Coiled coil (2); Modified residue (3); Motif (1); Mutagenesis (2); Region (3); Topological domain (3); Transit peptide (1); Transmembrane (2) TRANSMEM 233 256 Helical. {ECO:0000255}.; TRANSMEM 265 282 Helical. {ECO:0000255}. TOPO_DOM 50 232 Mitochondrial matrix. {ECO:0000250|UniProtKB:Q8NE86}.; TOPO_DOM 257 264 Mitochondrial intermembrane. {ECO:0000250|UniProtKB:Q8NE86}.; TOPO_DOM 283 350 Mitochondrial matrix. {ECO:0000250|UniProtKB:Q8NE86}. FUNCTION: Mitochondrial inner membrane calcium uniporter that mediates calcium uptake into mitochondria (PubMed:21685886, PubMed:23900286, PubMed:24212091). Constitutes the pore-forming and calcium-conducting subunit of the uniporter complex (uniplex) (By similarity). Activity is regulated by MICU1 and MICU2 (By similarity). At low Ca(2+) levels MCU activity is down-regulated by MICU1 and MICU2; at higher Ca(2+) levels MICU1 increases MCU activity (By similarity). Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenergetics, cytoplasmic calcium signals and activation of cell death pathways (By similarity). Involved in buffering the amplitude of systolic calcium rises in cardiomyocytes (By similarity). While dispensable for baseline homeostatic cardiac function, acts as a key regulator of short-term mitochondrial calcium loading underlying a 'fight-or-flight' response during acute stress: acts by mediating a rapid increase of mitochondrial calcium in pacemaker cells (PubMed:26119742, PubMed:26119731, PubMed:25603276). Participates in mitochondrial permeability transition during ischemia-reperfusion injury (PubMed:26119731). Regulates glucose-dependent insulin secretion in pancreatic beta-cells by regulating mitochondrial calcium uptake (By similarity). Mitochondrial calcium uptake in skeletal muscle cells is involved in muscle size in adults (PubMed:25732818). Regulates synaptic vesicle endocytosis kinetics in central nerve terminal (PubMed:26644474). Involved in antigen processing and presentation (PubMed:25251370). {ECO:0000250|UniProtKB:Q8NE86, ECO:0000269|PubMed:21685886, ECO:0000269|PubMed:23900286, ECO:0000269|PubMed:24212091, ECO:0000269|PubMed:25251370, ECO:0000269|PubMed:25603276, ECO:0000269|PubMed:25732818, ECO:0000269|PubMed:26119731, ECO:0000269|PubMed:26119742, ECO:0000269|PubMed:26644474}. PTM: Phosphorylation by CaMK2 in heart leads to increased MCU current. The regulation of MCU by CaMK2 is however subject to discussion: another group was unable to reproduce these results. Phosphorylated on tyrosines by PTK2B/PYK2, promoting oligomerization. {ECO:0000250|UniProtKB:Q8NE86}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:23900286, ECO:0000305|PubMed:26057074}; Multi-pass membrane protein {ECO:0000269|PubMed:23900286}. SUBUNIT: Component of the uniplex complex, composed of MCU, MCUB, MICU1, MICU2 and EMRE/SMDT1 (By similarity). Heterooligomer with CCDC109B/MCUB; this inhibits channel activity (PubMed:23900286). Homooligomer. Homotetramer (PubMed:23900286). Interacts with MICU1; MICU1 acts as an essential regulator for MCU. Interacts with MCUR1. Interactions with MICU1 and MCUR1 are mutually exclusive. Interacts with MICU2 (By similarity). Interacts with SLC25A23 (By similarity). {ECO:0000250|UniProtKB:Q8NE86, ECO:0000269|PubMed:23409044, ECO:0000269|PubMed:23900286}. DOMAIN: The N-terminal domain is required for efficient Ca(2+) uptake and for interaction with MCUR1. It is not required for targeting to the mitochondria, oligomerization, interaction with MICU1 and MICU2, or assembly of the uniplex complex. {ECO:0000250|UniProtKB:Q8NE86}.; DOMAIN: Forms a well-packed pentamer with an overall cylindrical shape. The inner core of the pentamer is formed with the second transmembrane region and the second coiled-coil region: while the transmembrane regions pack into a five-helix bundle having a largely polar pore across the membrane, the coiled-coil outside the membrane forms a pentamer with a hydrophobic core. The inner core is wrapped by the first transmembrane region through contacts between the first and the second transmembrane regions. The second transmembrane is followed by the inner juxtamembrane region (IJMH) that orients at a wide angle relative to the second transmembrane. The two core domains are held together on the periphery by the outer juxtamembrane helix (OJMH). {ECO:0000250|UniProtKB:Q21121}.; DOMAIN: The critical DXXE motif connecting the transmembrane regions forms a pentameric barrel that constitutes the mouth of the pore. Inside the barrel, two acidic residues are in position to form two carboxylate rings. In absence of SMDT1/EMRE regulator, the calcium ions cannot exit the channel, suggesting that SMDT1/EMRE-binding induces conformational rearrangements to allow calcium to exit. {ECO:0000250|UniProtKB:Q21121}. TISSUE SPECIFICITY: Detected in heart muscle (at protein level) (PubMed:26057074). Expressed in skeletal muscle, heart, kidney, liver, brain, lung, white fat and spleen. {ECO:0000269|PubMed:21685888, ECO:0000269|PubMed:23409044, ECO:0000269|PubMed:23900286, ECO:0000269|PubMed:26057074}. +Q8BQM9 MD12L_MOUSE Mediator of RNA polymerase II transcription subunit 12-like protein (Mediator complex subunit 12-like protein) 2157 241,426 Alternative sequence (6); Chain (1); Compositional bias (1); Erroneous initiation (1); Modified residue (1) FUNCTION: May be a component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: May be a component of the Mediator complex, which is known to be composed of MED1, MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L, MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23, MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8 subunits form a distinct module termed the CDK8 module. Mediator containing the CDK8 module is less active than Mediator lacking this module in supporting transcriptional activation. Individual preparations of the Mediator complex lacking one or more distinct subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and TRAP (By similarity). {ECO:0000250}. +P23906 IRF2_MOUSE Interferon regulatory factor 2 (IRF-2) 349 39,453 Beta strand (6); Chain (1); Cross-link (5); DNA binding (1); Helix (4); Modified residue (3); Turn (3) FUNCTION: Specifically binds to the upstream regulatory region of type I IFN and IFN-inducible MHC class I genes (the interferon consensus sequence (ICS)) and represses those genes. Also acts as an activator for several genes including H4 and IL7. Constitutively binds to the ISRE promoter to activate IL7. Involved in cell cycle regulation through binding the site II (HiNF-M) promoter region of H4 and activating transcription during cell growth. Antagonizes IRF1 transcriptional activation. PTM: Acetylated by CBP/ p300 during cell-growth. Acetylation on Lys-75 is required for stimulation of H4 promoter activity (By similarity). {ECO:0000250}.; PTM: The major sites of sumoylation are Lys-137 and Lys-293. Sumoylation with SUMO1 increases its transcriptional repressor activity on IRF1 and diminishes its ability to activate ISRE and H4 promoter (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with BRD7, IRF2BP1 and IRF2BP2. Interacts with CREBBP in growing cells; the interaction acetylates IRF2 and regulates IRF2-dependent H4 promoter activity (By similarity). {ECO:0000250}. +P70671 IRF3_MOUSE Interferon regulatory factor 3 (IRF-3) 419 46,852 Chain (1); Cross-link (3); DNA binding (1); Modified residue (13) FUNCTION: Key transcriptional regulator of type I interferon (IFN)-dependent immune responses which plays a critical role in the innate immune response against DNA and RNA viruses. Regulates the transcription of type I IFN genes (IFN-alpha and IFN-beta) and IFN-stimulated genes (ISG) by binding to an interferon-stimulated response element (ISRE) in their promoters. Acts as a more potent activator of the IFN-beta (IFNB) gene than the IFN-alpha (IFNA) gene and plays a critical role in both the early and late phases of the IFNA/B gene induction. Found in an inactive form in the cytoplasm of uninfected cells and following viral infection, double-stranded RNA (dsRNA), or toll-like receptor (TLR) signaling, is phosphorylated by IKBKE and TBK1 kinases. This induces a conformational change, leading to its dimerization and nuclear localization and association with CREB binding protein (CREBBP) to form dsRNA-activated factor 1 (DRAF1), a complex which activates the transcription of the type I IFN and ISG genes. Can activate distinct gene expression programs in macrophages and can induce significant apoptosis in primary macrophages. {ECO:0000269|PubMed:15800576}. PTM: Constitutively phosphorylated on many Ser/Thr residues. C-terminal serine/threonine cluster is phosphorylated in response of induction by IKBKE and TBK1. Phosphorylated at Ser-388 by IKBKE upon ssRNA viral infection. Ser-378 and Ser-379 may be specifically phosphorylated in response to induction. Phosphorylation at Ser-379 by TBK1 results in oligomerization. An alternate model propose that the five serine/threonine residues between 388 and 397 are phosphorylated in response to a viral infection. {ECO:0000269|PubMed:22065572}.; PTM: Ubiquitinated; ubiquitination involves RBCK1 leading to proteasomal degradation. Polyubiquitinated; ubiquitination involves TRIM21 leading to proteasomal degradation. {ECO:0000250|UniProtKB:Q14653}.; PTM: ISGylated by HERC5 resulting in sustained IRF3 activation and in the inhibition of IRF3 ubiquitination by disrupting PIN1 binding. The phosphorylation state of IRF3 does not alter ISGylation. {ECO:0000250|UniProtKB:Q14653}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14653}. Nucleus {ECO:0000250|UniProtKB:Q14653}. Note=Shuttles between cytoplasmic and nuclear compartments, with export being the prevailing effect. When activated, IRF3 interaction with CREBBP prevents its export to the cytoplasm. {ECO:0000250|UniProtKB:Q14653}. SUBUNIT: Monomer. Homodimer; phosphorylation-induced. Heterodimer with IRF7. Interacts with CREBBP. May interact with MAVS. Interacts with IKBKE and TBK1. Interacts with TICAM1 and TICAM2. Interacts with RBCK1. Interacts with HERC5. Interacts with DDX3X (phosphorylated at 'Ser-102'); the interaction allows the phosphorylation and activation of IRF3 by IKBKE. Interacts with TRIM21 and ULK1, in the presence of TRIM21; this interaction leads to IRF3 degradation by autophagy. Interacts with RIOK3; RIOK3 probybly mediates the interaction of TBK1 with IRF3. {ECO:0000250|UniProtKB:Q14653}. +P81068 IRX1_MOUSE Iroquois-class homeodomain protein IRX-1 (Homeodomain protein IRXA1) (Iroquois homeobox protein 1) 480 50,169 Chain (1); Compositional bias (3); DNA binding (1); Modified residue (1); Sequence conflict (3) SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: Expressed in specific and overlapping patterns with Irx1 and Irx2 in the developing and adult metanephric kidney. In the adult metanephros, renal expression is found in the loop of Henle in the S3 proximal tubule segment and in the thick ascending limb (TAL) of the distal tubule. {ECO:0000269|PubMed:17875669}. +P81067 IRX3_MOUSE Iroquois-class homeodomain protein IRX-3 (Homeodomain protein IRXB1) (Iroquois homeobox protein 3) 507 52,693 Alternative sequence (1); Chain (1); Compositional bias (5); DNA binding (1); Frameshift (1); Modified residue (2); Sequence conflict (1) FUNCTION: Transcription factor involved in SHH-dependent neural patterning (PubMed:10830170, PubMed:15201216). Together with NKX2-2 and NKX6-1 acts to restrict the generation of motor neurons to the appropriate region of the neural tube (PubMed:10830170, PubMed:15201216). Belongs to the class I proteins of neuronal progenitor factors, which are repressed by SHH signals (PubMed:10830170, PubMed:15201216). Involved in the transcriptional repression of MNX1 in non-motor neuron cells (PubMed:15201216). Acts as a regulator of energy metabolism (PubMed:24646999). {ECO:0000269|PubMed:10830170, ECO:0000269|PubMed:15201216, ECO:0000269|PubMed:24646999}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: Expressed by neural progenitor cells in discrete domains of the ventral neural tube. Also expressed in specific and overlapping patterns with Irx1 and Irx2 in the developing and adult metanephric kidney. In the adult metanephros, renal expression is confined to the S3 segment of the proximal tubule, in the loop of Henle. {ECO:0000269|PubMed:10830170, ECO:0000269|PubMed:17875669}. +Q8VIM9 IRGQ_MOUSE Immunity-related GTPase family Q protein 583 59,323 Chain (1); Coiled coil (1); Compositional bias (1); Domain (1); Modified residue (1); Sequence conflict (1) +P85094 ISC2A_MOUSE Isochorismatase domain-containing protein 2A 206 22,417 Chain (1); Modified residue (7) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Localizes to the nucleus in the presence of CDKN2A. {ECO:0000250}. SUBUNIT: Interacts with CDKN2A. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. Expressed predominantly in uterus, stomach and urinary tract. {ECO:0000269|PubMed:17658461}. +P23804 MDM2_MOUSE E3 ubiquitin-protein ligase Mdm2 (EC 2.3.2.27) (Double minute 2 protein) (Oncoprotein Mdm2) (RING-type E3 ubiquitin transferase Mdm2) (p53-binding protein Mdm2) 489 54,558 Alternative sequence (1); Chain (1); Compositional bias (2); Domain (1); Modified residue (12); Motif (3); Region (7); Sequence conflict (4); Zinc finger (2) FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination of p53/TP53, leading to its degradation by the proteasome (PubMed:15195100, PubMed:21804542). Inhibits p53/TP53- and p73/TP73-mediated cell cycle arrest and apoptosis by binding its transcriptional activation domain (By similarity). Also acts as a ubiquitin ligase E3 toward itself, ARRB1 and ARBB2 (PubMed:11588219). Permits the nuclear export of p53/TP53 (By similarity). Promotes proteasome-dependent ubiquitin-independent degradation of retinoblastoma RB1 protein (By similarity). Inhibits DAXX-mediated apoptosis by inducing its ubiquitination and degradation (By similarity). Component of the TRIM28/KAP1-MDM2-p53/TP53 complex involved in stabilizing p53/TP53 (By similarity). Also component of the TRIM28/KAP1-ERBB4-MDM2 complex which links growth factor and DNA damage response pathways (By similarity). Mediates ubiquitination and subsequent proteasome degradation of DYRK2 in nucleus (By similarity). Ubiquitinates IGF1R and SNAI1 and promotes them to proteasomal degradation (By similarity). Ubiquitinates DCX, leading to DCX degradation and reduction of the dendritic spine density of olfactory bulb granule cells (PubMed:25088421). Ubiquitinates DLG4, leading to proteasomal degradation of DLG4 which is required for AMPA receptor endocytosis (PubMed:14642282). {ECO:0000250|UniProtKB:Q00987, ECO:0000269|PubMed:11588219, ECO:0000269|PubMed:14642282, ECO:0000269|PubMed:15195100, ECO:0000269|PubMed:21804542, ECO:0000269|PubMed:25088421}. PTM: Phosphorylation on Ser-163 by SGK1 activates ubiquitination of p53/TP53. Phosphorylated at multiple sites near the RING domain by ATM upon DNA damage; this prevents oligomerization and E3 ligase processivity and impedes constitutive p53/TP53 degradation (By similarity). {ECO:0000250}.; PTM: Autoubiquitination leads to proteasomal degradation; resulting in p53/TP53 activation it may be regulated by SFN. Also ubiquitinated by TRIM13. Deubiquitinated by USP2 leads to its accumulation and increases deubiquitination and degradation of p53/TP53. Deubiquitinated by USP7 leading to its stabilization (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:15195100, ECO:0000269|PubMed:21804542}. Cytoplasm {ECO:0000269|PubMed:15195100}. Nucleus, nucleolus {ECO:0000269|PubMed:15195100}. Note=Colocalizes with RASSF1 isoform A in the nucleus (By similarity). Expressed predominantly in the nucleoplasm. Interaction with ARF(P14) results in the localization of both proteins to the nucleolus. The nucleolar localization signals in both ARF(P14) and MDM2 may be necessary to allow efficient nucleolar localization of both proteins. {ECO:0000250}. SUBUNIT: Interacts with p53/TP53, TP73/p73, RBL5 and RP11. Binds specifically to RNA. Can interact with RB1, E1A-associated protein EP300 and the E2F1 transcription factor. Forms a ternary complex with p53/TP53 and WWOX. Interacts with CDKN2AIP, RFWD3, USP7, PYHIN1 and RBBP6. Interacts with ARRB1 and ARRB2. Interacts with PSMA3. Found in a trimeric complex with MDM2, MDM4 and USP2. Interacts with USP2 (via N-terminus and C-terminus). Interacts with MDM4. Part of a complex with MDM2, DAXX, RASSF1 and USP7. Part of a complex with DAXX, MDM2 and USP7. Interacts directly with DAXX and USP7. Interacts (via C-terminus) with RASSF1 isoform A (via N-terminus); the interaction is independent of TP53. Interacts with APEX1; leading to its ubiquitination and degradation. Interacts with RYBP; this inhibits ubiquitination of TP53. Identified in a complex with RYBP and p53/TP53. Also component of the TRIM28/KAP1-MDM2-p53/TP53 complex involved in regulating p53/TP53 stabilization and activity. Binds directly both p53/TP53 and TRIM28. Component of the TRIM28/KAP1-ERBB4-MDM2 complex involved in connecting growth factor responses with DNA damage. Interacts directly with both TRIM28 and ERBB4 in the complex. Interacts with DYRK2. Interacts with IGF1R. Interacts with TRIM13; the interaction ubiquitinates MDM2 leading to its proteasomal degradation. Interacts with SNAI1; this interaction promotes SNAI1 ubiquitination. Interacts with NOTCH1 (via intracellular domain). Interacts with FHIT. Interacts with RFFL and RNF34; the interaction stabilizes MDM2. Interacts with CDK5RAP3 and CDKN2A/ARF; form a ternary complex involved in regulation of p53/TP53. Interacts with MTA1 (By similarity). Interacts with AARB2 (PubMed:11588219). Interacts with MTBP (PubMed:10906133). Interacts with PML (PubMed:15195100). Interacts with TBRG1 (PubMed:17110379). Interacts with the 5S RNP which is composed of the 5S RNA, RPL5 and RPL11; the interaction is direct occurs in the nucleoplasm and negatively regulates MDM2-mediated TP53 ubiquitination and degradation (PubMed:15195100, PubMed:21804542). Interacts with ADGRB1; the interaction results in inhibition of MDM2-mediated ubiquitination and degradation of DLG4/PSD95, promoting DLG4 stability and regulating synaptic plasticity (PubMed:25751059). Interacts with RPL23A; this interaction may promote p53/TP53 polyubiquitination (By similarity). {ECO:0000250|UniProtKB:Q00987, ECO:0000269|PubMed:10906133, ECO:0000269|PubMed:11588219, ECO:0000269|PubMed:15195100, ECO:0000269|PubMed:17110379, ECO:0000269|PubMed:21804542, ECO:0000269|PubMed:25751059}. DOMAIN: Region I is sufficient for binding p53 and inhibiting its G1 arrest and apoptosis functions. It also binds p73 and E2F1. Region II contains most of a central acidic region required for interaction with ribosomal protein L5 and a putative C4-type zinc finger. The RING finger domain which coordinates two molecules of zinc interacts specifically with RNA whether or not zinc is present and mediates the heterooligomerization with MDM4. It is also essential for its ubiquitin ligase E3 activity toward p53 and itself. TISSUE SPECIFICITY: Ubiquitously expressed at low-level throughout embryo development and in adult tissues. MDM2-p90 is much more abundant than MDM2-p76 in testis, brain, heart, and kidney, but in the thymus, spleen, and intestine, the levels of the MDM2 proteins are roughly equivalent. {ECO:0000269|PubMed:10075719}. +Q64327 MEA1_MOUSE Male-enhanced antigen 1 (MEA-1) 174 18,584 Chain (1); Modified residue (1) FUNCTION: May play an important role in spermatogenesis and/or testis development. TISSUE SPECIFICITY: Highly expressed in testis. Transcripts can be found in primary and secondary spermatocytes, and spermatids, but the protein itself is only detected in spermatids. No expression in Leydig cells, spermatogonia, or sperm. Very weak expression in the heart, kidney, spleen, thymus and ovary. {ECO:0000269|PubMed:12444059}. +Q9CXU0 MED10_MOUSE Mediator of RNA polymerase II transcription subunit 10 (Mediator complex subunit 10) 135 15,661 Chain (1); Sequence conflict (1) FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Component of the Mediator complex, which is composed of MED1, MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L, MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23, MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8 subunits form a distinct module termed the CDK8 module. Mediator containing the CDK8 module is less active than Mediator lacking this module in supporting transcriptional activation. Individual preparations of the Mediator complex lacking one or more distinct subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and TRAP (By similarity). {ECO:0000250}. +Q9CZ82 MED18_MOUSE Mediator of RNA polymerase II transcription subunit 18 (Mediator complex subunit 18) 208 23,645 Chain (1); Modified residue (1) FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Component of the Mediator complex, which is composed of MED1, MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L, MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23, MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8 subunits form a distinct module termed the CDK8 module. Mediator containing the CDK8 module is less active than Mediator lacking this module in supporting transcriptional activation. Individual preparations of the Mediator complex lacking one or more distinct subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and TRAP (By similarity). {ECO:0000250}. +Q5F2C3 MEIKN_MOUSE Meiosis-specific kinetochore protein 434 47,423 Alternative sequence (1); Chain (1); Motif (1); Region (1); Sequence conflict (1) FUNCTION: Key regulator of kinetochore function during meiosis I: required both for mono-orientation of kinetochores on sister chromosomes and protection of centromeric cohesin from separase-mediated cleavage. Acts by facilitating kinetochore mono-orientation during meiosis I, when kinetochores on sister chromosomes face the same direction and are thus captured and pulled by spindle fibers from the same pole. Also required to prevent cleavage of cohesin at centromeres during meiosis I, possibly by acting as a regulator of the shugoshin-dependent protection pathway. Acts in collaboration with PLK1: required for PLK1 enrichment to kinetochores. Not required during meiosis II or mitosis. {ECO:0000269|PubMed:25533956}. SUBCELLULAR LOCATION: Chromosome, centromere {ECO:0000269|PubMed:25533956}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:25533956}. Note=Localizes at kinetochores in meiosis I but undetectable in meiosis II. {ECO:0000269|PubMed:25533956}. SUBUNIT: Interacts with CENPC. Interacts with PLK1; required for recruitment of PLK1 at kinetochores. {ECO:0000269|PubMed:25533956}. TISSUE SPECIFICITY: Germ cell-specific. Expressed in both testis and ovary. Not expressed in other tissues. {ECO:0000269|PubMed:25533956}. +Q8JZS7 HMGC2_MOUSE 3-hydroxymethyl-3-methylglutaryl-CoA lyase, cytoplasmic (EC 4.1.3.4) (3-hydroxymethyl-3-methylglutaryl-CoA lyase-like protein 1) 343 36,650 Active site (1); Binding site (1); Chain (1); Domain (1); Initiator methionine (1); Lipidation (1); Metal binding (4) Metabolic intermediate metabolism; (S)-3-hydroxy-3-methylglutaryl-CoA degradation; acetoacetate from (S)-3-hydroxy-3-methylglutaryl-CoA: step 1/1. FUNCTION: Non-mitochondrial 3-hydroxymethyl-3-methylglutaryl-CoA lyase that catalyzes a cation-dependent cleavage of (S)-3-hydroxy-3-methylglutaryl-CoA into acetyl-CoA and acetoacetate, a key step in ketogenesis, the products of which support energy production in nonhepatic animal tissues. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. +Q01237 HMDH_MOUSE 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMG-CoA reductase) (EC 1.1.1.34) 887 97,040 Active site (4); Chain (1); Compositional bias (1); Cross-link (2); Domain (1); Glycosylation (3); Modified residue (1); Motif (1); Region (2); Sequence conflict (1); Transmembrane (7) TRANSMEM 10 39 Helical. {ECO:0000255}.; TRANSMEM 57 78 Helical. {ECO:0000255}.; TRANSMEM 90 114 Helical. {ECO:0000255}.; TRANSMEM 124 149 Helical. {ECO:0000255}.; TRANSMEM 160 187 Helical. {ECO:0000255}.; TRANSMEM 192 220 Helical. {ECO:0000255}.; TRANSMEM 315 339 Helical. {ECO:0000255}. Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 3/3. FUNCTION: Transmembrane glycoprotein that is the rate-limiting enzyme in cholesterol biosynthesis as well as in the biosynthesis of nonsterol isoprenoids that are essential for normal cell function including ubiquinone and geranylgeranyl proteins. PTM: Undergoes sterol-mediated ubiquitination and ER-associated degradation (ERAD). Accumulation of sterols in the endoplasmic reticulum (ER) membrane, triggers binding of the reductase to the ER membrane protein INSIG1. This INSIG1 binding leads to the recruitment of the ubiquitin ligase, AMFR/gp78 or RNF145, initiating ubiquitination of the reductase. The ubiquitinated reductase is then extracted from the ER membrane and delivered to cytosolic 26S proteosomes by a mechanism probably mediated by the ATPase Valosin-containing protein VCP/p97. Lys-248 is the main site of ubiquitination. Ubiquitination is enhanced by the presence of a geranylgeranylated protein. {ECO:0000250|UniProtKB:P00347, ECO:0000250|UniProtKB:P04035}.; PTM: N-glycosylated. Deglycosylated by NGLY1 on release from the endoplasmic reticulum (ER) in a sterol-mediated manner. {ECO:0000250|UniProtKB:P04035}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Homodimer. Interacts with INSIG1 (via its SSD); the interaction, accelerated by sterols, leads to the recruitment of HMGCR to AMFR/gp78 for its ubiquitination by the sterol-mediated ERAD pathway. Interacts with UBIAD1 (By similarity). {ECO:0000250}. +Q00547 HMMR_MOUSE Hyaluronan mediated motility receptor (Intracellular hyaluronic acid-binding protein) (Receptor for hyaluronan-mediated motility) (CD antigen CD168) 794 91,785 Alternative sequence (1); Chain (1); Glycosylation (9); Modified residue (2); Region (3); Repeat (5); Sequence conflict (14) FUNCTION: Receptor for hyaluronic acid (HA) (PubMed:1376732). Involved in cell motility (PubMed:1376732). When hyaluronan binds to HMMR, the phosphorylation of a number of proteins, including the PTK2/FAK1 occurs. May also be involved in cellular transformation and metastasis formation, and in regulating extracellular-regulated kinase (ERK) activity. May act as a regulator of adipogenesis (PubMed:22666460). {ECO:0000269|PubMed:1376732, ECO:0000269|PubMed:22666460}. SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:1376732, ECO:0000269|PubMed:9556628}. Cytoplasm {ECO:0000269|PubMed:9556628, ECO:0000269|PubMed:9601097}. SUBUNIT: Subunit of the HARC complex. Interacts with ANKRD26. {ECO:0000250|UniProtKB:O75330}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:9889313}. +Q9Z2X1 HNRPF_MOUSE Heterogeneous nuclear ribonucleoprotein F (hnRNP F) [Cleaved into: Heterogeneous nuclear ribonucleoprotein F, N-terminally processed] 415 45,730 Alternative sequence (1); Beta strand (7); Chain (2); Cross-link (6); Domain (3); Erroneous initiation (2); Erroneous termination (1); Helix (5); Initiator methionine (1); Modified residue (12); Region (3); Sequence conflict (1); Site (12); Turn (1) FUNCTION: Component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes which provide the substrate for the processing events that pre-mRNAs undergo before becoming functional, translatable mRNAs in the cytoplasm. Plays a role in the regulation of alternative splicing events. Binds G-rich sequences in pre-mRNAs and keeps target RNA in an unfolded state (By similarity). {ECO:0000250}. PTM: Sumoylated. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}. SUBUNIT: Identified in the spliceosome C complex. Interacts with AGO1, AGO2, TBP and TXNL4/DIM1 (By similarity). {ECO:0000250}. DOMAIN: The N-terminal RRM domains are responsible for recognizing the G-tract of BCL-X RNA. {ECO:0000250}. +P42581 HMX3_MOUSE Homeobox protein HMX3 (Homeobox protein H6 family member 3) (Homeobox protein Nkx-5.1) 356 37,859 Chain (1); Compositional bias (3); DNA binding (1); Modified residue (2); Mutagenesis (1); Sequence caution (1); Sequence conflict (1) FUNCTION: Transcription factor involved in specification of neuronal cell types and which is required for inner ear and hypothalamus development. Binds to the 5'-CAAGTG-3' core sequence. Controls semicircular canal formation in the inner ear. Also required for hypothalamic/pituitary axis of the CNS. {ECO:0000269|PubMed:15363417, ECO:0000269|PubMed:9389661, ECO:0000269|PubMed:9435283}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: Expressed in the developing CNS, including a specific expression in vestibular structures throughout inner ear development. {ECO:0000269|PubMed:11748138, ECO:0000269|PubMed:9389661, ECO:0000269|PubMed:9435283}. +Q9QUP5 HPLN1_MOUSE Hyaluronan and proteoglycan link protein 1 (Cartilage-linking protein 1) (Cartilage-link protein) (Proteoglycan link protein) 356 40,478 Chain (1); Disulfide bond (5); Domain (3); Glycosylation (1); Propeptide (1); Sequence conflict (2) FUNCTION: Stabilizes the aggregates of proteoglycan monomers with hyaluronic acid in the extracellular cartilage matrix. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:12732630}. +Q9ESM3 HPLN2_MOUSE Hyaluronan and proteoglycan link protein 2 (Brain link protein 1) 341 37,925 Chain (1); Disulfide bond (5); Domain (3); Signal peptide (1) FUNCTION: Mediates a firm binding of versican V2 to hyaluronic acid. May play a pivotal role in the formation of the hyaluronan-associated matrix in the central nervous system (CNS) which facilitates neuronal conduction and general structural stabilization. Binds to hyaluronic acid. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. TISSUE SPECIFICITY: Brain. Predominantly expressed by neurons. Colocalizes with versican V2 in developing and adult cerebellar white matter and at the nodes of Ranvier. {ECO:0000269|PubMed:11027579}. +Q80WM4 HPLN4_MOUSE Hyaluronan and proteoglycan link protein 4 (Brain link protein 2) 400 42,809 Chain (1); Disulfide bond (5); Domain (3); Glycosylation (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Binds to hyaluronic acid and may be involved in formation of the extracellular matrix. {ECO:0000269|PubMed:14550776, ECO:0000303|PubMed:14550776}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. TISSUE SPECIFICITY: Expressed predominantly in brain where it is found mainly throughout the midbrain and hindbrain in a perineuronal net pattern. {ECO:0000269|PubMed:14550776}. +Q9CQZ1 HSBP1_MOUSE Heat shock factor-binding protein 1 76 8,611 Chain (1) FUNCTION: Negative regulator of the heat shock response. Negatively affects HSF1 DNA-binding activity. May have a role in the suppression of the activation of the stress response during the aging process (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Homohexamer. Associates with heptad repeats of HSF1 trimers and probably also HSF1 monomers, and with HSP70. Association with HSF1 trimers and HSP70 coincides with attenuation of heat shock response and the conversion of HSF1 trimer to monomer (By similarity). {ECO:0000250}. +P18533 HVM62_MOUSE Ig heavy chain V region 733 117 13,223 Chain (1); Disulfide bond (1); Domain (1); Non-terminal residue (1); Signal peptide (1) +P10628 HXD4_MOUSE Homeobox protein Hox-D4 (Homeobox protein Hox-4.2) (Homeobox protein Hox-5.1) 250 27,371 Chain (1); Compositional bias (1); DNA binding (1); Erroneous initiation (1); Motif (1); Sequence conflict (3) FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. SUBCELLULAR LOCATION: Nucleus. +P01791 HVM22_MOUSE Ig heavy chain V region HPCM6 123 13,896 Chain (1); Domain (1); Non-terminal residue (1) +P09092 HXA6_MOUSE Homeobox protein Hox-A6 (Homeobox protein Hox-1.2) (Homeobox protein M5-4) 232 26,335 Chain (1); DNA binding (1); Motif (1); Sequence conflict (1) FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. SUBCELLULAR LOCATION: Nucleus. +P06329 HVM50_MOUSE Ig heavy chain V region AC38 15.3 120 13,311 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (3) +P18525 HVM54_MOUSE Ig heavy chain V region 5-84 117 12,872 Beta strand (9); Chain (1); Disulfide bond (1); Helix (3); Non-terminal residue (1); Region (5); Signal peptide (1); Turn (1) +P23812 HXD12_MOUSE Homeobox protein Hox-D12 (Homeobox protein Hox-4.7) (Homeobox protein Hox-5.6) 268 29,198 Chain (1); DNA binding (1); Erroneous gene model prediction (1) FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. SUBCELLULAR LOCATION: Nucleus. +P18529 HVM58_MOUSE Ig heavy chain V region 5-76 117 12,991 Beta strand (9); Chain (1); Disulfide bond (1); Helix (3); Non-terminal residue (1); Region (5); Signal peptide (1); Turn (1) +P04219 HYIG_MOUSE Putative uncharacterized Ig-region protein 140 15,424 Chain (1) +P02831 HXA3_MOUSE Homeobox protein Hox-A3 (Homeobox protein Hox-1.5) (Homeobox protein MO-10) 443 46,430 Chain (1); Compositional bias (1); DNA binding (1); Motif (1); Sequence conflict (8) FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Binds 5' to its own homeobox. SUBCELLULAR LOCATION: Nucleus. +P17710 HXK1_MOUSE Hexokinase-1 (EC 2.7.1.1) (Hexokinase type I) (HK I) (Hexokinase, tumor isozyme) 974 108,303 Alternative sequence (3); Binding site (15); Chain (1); Domain (2); Modified residue (1); Mutagenesis (6); Nucleotide binding (6); Region (17); Sequence conflict (2) Carbohydrate metabolism; hexose metabolism. PTM: Isoform HK1-SC is tyrosine-phosphorylated. {ECO:0000269|PubMed:9450953}. SUBCELLULAR LOCATION: Isoform HK1: Mitochondrion outer membrane; Peripheral membrane protein.; SUBCELLULAR LOCATION: Isoform HK1-SC: Membrane. Note=Isoform HK1-SC is an integral membrane protein. SUBUNIT: Monomer. Interacts with VDAC1. The HK1-VDAC1 complex interacts with ATF2 (By similarity). Interacts with RABL2/RABL2A; binds preferentially to GTP-bound RABL2. Interacts (via N-terminal spermatogenic cell-specific region) with PFKM isoform 2 and isoform 3 (via C-terminus) (PubMed:19889946). {ECO:0000250, ECO:0000269|PubMed:19889946, ECO:0000269|PubMed:23055941}. DOMAIN: The N- and C-terminal halves of this hexokinase show extensive sequence similarity to each other. The catalytic activity is associated with the C-terminus while regulatory function is associated with the N-terminus. Each domain can bind a single glucose and Gluc-6-P molecule (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: In rapidly growing tumor cells exhibiting high glucose catabolic rates, isoform HK1 is markedly elevated. Isoform HK1-SA, isoform HK1-SB and isoform HK1-SC are found only in spermatogenic cells. Isoform HK1-SC is detected in round spermatids, condensing spermatids and mature sperm where it is found in the head membranes, mitochondria of the midpiece and the fibrous sheath of the flagellum. Expressed within the principal piece and midpiece of sperm tail (at protein level). {ECO:0000269|PubMed:23055941}. +O70394 I27RA_MOUSE Interleukin-27 receptor subunit alpha (IL-27 receptor subunit alpha) (IL-27R subunit alpha) (IL-27R-alpha) (IL-27RA) (Type I T-cell cytokine receptor) (TCCR) (WSX-1) 623 69,093 Chain (1); Domain (4); Glycosylation (6); Motif (2); Sequence conflict (12); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 511 531 Helical. {ECO:0000255}. TOPO_DOM 25 510 Extracellular. {ECO:0000255}.; TOPO_DOM 532 623 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for IL27. Requires IL6ST/gp130 to mediate signal transduction in response to IL27. This signaling system acts through STAT3 and STAT1. Involved in the regulation of Th1-type immune responses. Also appears to be involved in innate defense mechanisms. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. DOMAIN: The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.; DOMAIN: The box 1 motif is required for JAK interaction and/or activation. TISSUE SPECIFICITY: Expressed in CD4+ and CD8+ T-cells, B-cells, natural killer cells and macrophages. Highest levels in CD4+ T-cells and natural killer cells. Expression highest in Th0 cells. {ECO:0000269|PubMed:11057672}. +Q5I1X5 IASPP_MOUSE RelA-associated inhibitor (Inhibitor of ASPP protein) (Protein iASPP) (NFkB-interacting protein 1) (PPP1R13B-like protein) 824 88,976 Chain (1); Compositional bias (1); Domain (1); Modified residue (30); Repeat (2) FUNCTION: Regulator that plays a central role in regulation of apoptosis and transcription via its interaction with NF-kappa-B and p53/TP53 proteins. Inhibits p53/TP53 function, possibly by preventing the association between p53/TP53 and ASPP1 or ASPP2, and therefore suppressing the subsequent activation of apoptosis (By similarity). {ECO:0000250|UniProtKB:Q8WUF5}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8WUF5}. Nucleus {ECO:0000250|UniProtKB:Q8WUF5}. Note=Predominantly cytoplasmic but also nuclear. {ECO:0000250|UniProtKB:Q8WUF5}. SUBUNIT: Interacts with TP63 and TP73 (By similarity). Interacts with RELA NF-kappa-B subunit and with SP1 via its C-terminal part. Interacts with p53/TP53. {ECO:0000250, ECO:0000269|PubMed:15661756}. DOMAIN: The N-terminal region is required for cytoplasmic localization. {ECO:0000250|UniProtKB:Q8WUF5}. TISSUE SPECIFICITY: Most abundant in skin with high levels also found in heart, testis and stomach. In E15.5 embryonic heart, expressed at higher levels in atria than ventricles. {ECO:0000269|PubMed:15661756}. DISEASE: Note=Defects in Ppp1r13l are the cause of the waved 3 phenotype, a recessive mutation characterized by abnormalities of the heart and skin. Affected animals have open eyes at birth and hair abnormalities. They develop focal cardiac necrosis at an early age which progresses to fatal dilated cardiomyopathy. This is due to a 14-bp deletion which gives rise to a truncated protein. {ECO:0000269|PubMed:15661756}. +P13597 ICAM1_MOUSE Intercellular adhesion molecule 1 (ICAM-1) (MALA-2) (MyD10) (CD antigen CD54) 537 58,844 Alternative sequence (1); Chain (1); Disulfide bond (8); Domain (5); Glycosylation (10); Motif (2); Sequence conflict (2); Signal peptide (1); Site (2); Topological domain (2); Transmembrane (1) TRANSMEM 486 509 Helical. {ECO:0000255}. TOPO_DOM 28 485 Extracellular. {ECO:0000255}.; TOPO_DOM 510 537 Cytoplasmic. {ECO:0000255}. FUNCTION: ICAM proteins are ligands for the leukocyte adhesion protein LFA-1 (integrin alpha-L/beta-2). During leukocyte trans-endothelial migration, ICAM1 engagement promotes the assembly of endothelial apical cups through ARHGEF26/SGEF and RHOG activation (By similarity). {ECO:0000250}. PTM: Monoubiquitinated, which is promoted by MARCH9 and leads to endocytosis. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Homodimer. Interacts with MUC1 and promotes cell aggregation in epithelial cells. Interacts with ARHGEF26/SGEF (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed at low level on a subpopulation of lymphocytes, macrophages, and endothelial cells, but is strongly induced on these cells, and on fibroblasts and epithelial cells. +Q64253 LY6E_MOUSE Lymphocyte antigen 6E (Ly-6E) (Stem cell antigen 2) (Thymic shared antigen 1) (TSA-1) 130 13,800 Chain (1); Disulfide bond (5); Domain (1); Erroneous initiation (2); Glycosylation (1); Lipidation (1); Propeptide (1); Signal peptide (1) FUNCTION: Involved in T-cell development (PubMed:8258699). Believed to act as a modulator of nicotinic acetylcholine receptors (nAChRs) activity. In vitro inhibits alpha-3:beta-4-containing nAChRs maximum response (PubMed:26276394). {ECO:0000269|PubMed:26276394, ECO:0000305|PubMed:8258699}. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. SUBUNIT: Interacts with CHRNA4. {ECO:0000269|PubMed:26276394}. +P47879 IBP4_MOUSE Insulin-like growth factor-binding protein 4 (IBP-4) (IGF-binding protein 4) (IGFBP-4) 254 27,807 Chain (1); Disulfide bond (10); Domain (2); Glycosylation (1); Modified residue (1); Sequence conflict (4); Signal peptide (1) FUNCTION: IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Binds IGF2 more than IGF1. +H3BJG9 LY6L_MOUSE Lymphocyte antigen 6L (Lymphocyte antigen 6 complex locus protein L) 140 15,540 Chain (1); Disulfide bond (2); Domain (1); Lipidation (1); Propeptide (1); Signal peptide (1) SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Lipid-anchor, GPI-anchor {ECO:0000255}. +P47880 IBP6_MOUSE Insulin-like growth factor-binding protein 6 (IBP-6) (IGF-binding protein 6) (IGFBP-6) 238 25,347 Chain (1); Disulfide bond (8); Domain (2); Sequence conflict (2); Signal peptide (1) FUNCTION: IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. PTM: O-glycosylated. SUBCELLULAR LOCATION: Secreted. +Q6ZPR6 IBTK_MOUSE Inhibitor of Bruton tyrosine kinase (IBtk) 1352 149,569 Alternative sequence (1); Chain (1); Domain (2); Frameshift (1); Modified residue (11); Repeat (5); Sequence conflict (2) FUNCTION: Acts as an inhibitor of BTK tyrosine kinase activity, thereby playing a role in B-cell development. Down-regulates BTK kinase activity, leading to interference with BTK-mediated calcium mobilization and NF-kappa-B-driven transcription (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Translocates to the plasma membrane upon IgM stimulation. {ECO:0000250}. SUBUNIT: Interacts with the PH domain of BTK. {ECO:0000250}. +Q99J23 GHDC_MOUSE GH3 domain-containing protein 532 58,508 Chain (1); Glycosylation (2); Sequence conflict (1); Signal peptide (1) SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:11735219}. Nucleus envelope {ECO:0000269|PubMed:11735219}. TISSUE SPECIFICITY: Highly expressed in mammary tissues from mature virgins and at day 13 of pregnancy, and at lower level during lactation. Expressed at intermediate level in liver. Expressed at lower level in kidney, heart and brain. {ECO:0000269|PubMed:11735219}. +P01573 IFNA2_MOUSE Interferon alpha-2 (IFN-alpha-2) 190 21,922 Chain (1); Disulfide bond (2); Glycosylation (1); Sequence conflict (3); Signal peptide (1) FUNCTION: Produced by macrophages, IFN-alpha have antiviral activities. {ECO:0000269|PubMed:2987810}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Interacts with IFNAR2. {ECO:0000250}. +Q8BZM1 GLMN_MOUSE Glomulin (FK506-binding protein-associated protein) (FAP) (FKBP-associated protein) 596 67,756 Chain (1); Compositional bias (2); Initiator methionine (1); Modified residue (1); Region (2); Sequence conflict (1) FUNCTION: Regulatory component of cullin-RING-based SCF (SKP1-Cullin-F-box protein) E3 ubiquitin-protein ligase complexes. Inhibits E3 ubiquitin ligase activity by binding to the RING domain of RBX1 and inhibiting its interaction with the E2 ubiquitin-conjugating enzyme CDC34. Inhibits RBX1-mediated neddylation of CUL1 (By similarity). Required for normal stability and normal cellular levels of key components of SCF ubiquitin ligase complexes, including FBXW7, RBX1, CUL1, CUL2, CUL3, CUL4A, and thereby contributes to the regulation of CCNE1 and MYC levels (PubMed:22405651). Essential for normal development of the vasculature (PubMed:22405651). Contributes to the regulation of RPS6KB1 phosphorylation (By similarity). {ECO:0000250|UniProtKB:Q92990, ECO:0000269|PubMed:22405651}. PTM: Phosphorylated on tyrosine residues. {ECO:0000250|UniProtKB:Q92990}. SUBUNIT: Interacts with FKBP4 and FKBP1A. Interacts with RBX1 (via RING domain). Identified in complexes that contain RBX1 plus one of the cullins CUL1, CUL2, CUL3, and CUL4A. Identified in a SCF complex composed of CUL1, RBX1, SKP1, FBXW7 and GLMN. Component of a SCF-like complex consisting of CUL7, RBX1, SKP1, FBXW8 and GLMN. Interacts with unphosphorylated MET and is released upon MET phosphorylation. {ECO:0000250|UniProtKB:Q92990}. DOMAIN: The C-terminal half of the protein is important for interaction with RBX1. {ECO:0000250|UniProtKB:Q92990}. TISSUE SPECIFICITY: Ubiquitous. Detected in embryonic vasculature and embryonic perichondrium, and in adult eye, brain, heart, testis, kidney, smooth muscle and skeletal muscle. {ECO:0000269|PubMed:15053987}. +Q8CGK6 IFNL3_MOUSE Interferon lambda-3 (IFN-lambda-3) (Interleukin-28B) (IL-28B) 193 21,664 Chain (1); Disulfide bond (3); Sequence conflict (2); Signal peptide (1) FUNCTION: Cytokine with antiviral, antitumour and immunomodulatory activities. Plays a critical role in the antiviral host defense, predominantly in the epithelial tissues. Acts as a ligand for the heterodimeric class II cytokine receptor composed of IL10RB and IFNLR1, and receptor engagement leads to the activation of the JAK/STAT signaling pathway resulting in the expression of IFN-stimulated genes (ISG), which mediate the antiviral state. Has a restricted receptor distribution and therefore restricted targets: is primarily active in epithelial cells and this cell type-selective action is because of the epithelial cell-specific expression of its receptor IFNLR1. Seems not to be essential for early virus-activated host defense in vaginal infection, but plays an important role in Toll-like receptor (TLR)-induced antiviral defense. Plays a significant role in the antiviral immune defense in the intestinal epithelium. Exerts an immunomodulatory effect by up-regulating MHC class I antigen expression. {ECO:0000269|PubMed:15914836, ECO:0000269|PubMed:16618774, ECO:0000269|PubMed:18250457, ECO:0000269|PubMed:21518880}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +Q60751 IGF1R_MOUSE Insulin-like growth factor 1 receptor (EC 2.7.10.1) (Insulin-like growth factor I receptor) (IGF-I receptor) (CD antigen CD221) [Cleaved into: Insulin-like growth factor 1 receptor alpha chain; Insulin-like growth factor 1 receptor beta chain] 1373 155,788 Active site (1); Binding site (1); Chain (2); Cross-link (2); Disulfide bond (15); Domain (5); Glycosylation (16); Modified residue (6); Motif (1); Nucleotide binding (1); Sequence conflict (8); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 937 960 Helical. {ECO:0000255}. TOPO_DOM 742 936 Extracellular. {ECO:0000255}.; TOPO_DOM 961 1373 Cytoplasmic. {ECO:0000250}. FUNCTION: Receptor tyrosine kinase which mediates actions of insulin-like growth factor 1 (IGF1). Binds IGF1 with high affinity and IGF2 and insulin (INS) with a lower affinity. The activated IGF1R is involved in cell growth and survival control. IGF1R is crucial for tumor transformation and survival of malignant cell. Ligand binding activates the receptor kinase, leading to receptor autophosphorylation, and tyrosines phosphorylation of multiple substrates, that function as signaling adapter proteins including, the insulin-receptor substrates (IRS1/2), Shc and 14-3-3 proteins. Phosphorylation of IRSs proteins lead to the activation of two main signaling pathways: the PI3K-AKT/PKB pathway and the Ras-MAPK pathway. The result of activating the MAPK pathway is increased cellular proliferation, whereas activating the PI3K pathway inhibits apoptosis and stimulates protein synthesis. Phosphorylated IRS1 can activate the 85 kDa regulatory subunit of PI3K (PIK3R1), leading to activation of several downstream substrates, including protein AKT/PKB. AKT phosphorylation, in turn, enhances protein synthesis through mTOR activation and triggers the antiapoptotic effects of IGFIR through phosphorylation and inactivation of BAD. In parallel to PI3K-driven signaling, recruitment of Grb2/SOS by phosphorylated IRS1 or Shc leads to recruitment of Ras and activation of the ras-MAPK pathway. In addition to these two main signaling pathways IGF1R signals also through the Janus kinase/signal transducer and activator of transcription pathway (JAK/STAT). Phosphorylation of JAK proteins can lead to phosphorylation/activation of signal transducers and activators of transcription (STAT) proteins. In particular activation of STAT3, may be essential for the transforming activity of IGF1R. The JAK/STAT pathway activates gene transcription and may be responsible for the transforming activity. JNK kinases can also be activated by the IGF1R. IGF1 exerts inhibiting activities on JNK activation via phosphorylation and inhibition of MAP3K5/ASK1, which is able to directly associate with the IGF1R (By similarity). When present in a hybrid receptor with INSR, binds IGF1 (By similarity). {ECO:0000250}. PTM: Autophosphorylated on tyrosine residues in response to ligand binding. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Autophosphorylation occurs in a sequential manner; Tyr-1167 is predominantly phosphorylated first, followed by phosphorylation of Tyr-1163 and Tyr-1168. While every single phosphorylation increases kinase activity, all three tyrosine residues in the kinase activation loop (Tyr-1163, Tyr-1167 and Tyr-1168) have to be phosphorylated for optimal activity. Can be autophosphorylated at additional tyrosine residues (in vitro). Autophosphorylated is followed by phosphorylation of juxtamembrane tyrosines and C-terminal serines. Phosphorylation of Tyr-981 is required for IRS1- and SHC1-binding (By similarity). Phosphorylation of Ser-1280 by GSK-3beta restrains kinase activity and promotes cell surface expression, it requires a priming phosphorylation at Ser-1284. Dephosphorylated by PTPN1. {ECO:0000250, ECO:0000269|PubMed:22685298}.; PTM: Polyubiquitinated at Lys-1170 and Lys-1173 through both 'Lys-48' and 'Lys-29' linkages, promoting receptor endocytosis and subsequent degradation by the proteasome. Ubiquitination is facilitated by pre-existing phosphorylation (By similarity). {ECO:0000250}.; PTM: Sumoylated with SUMO1. {ECO:0000250}.; PTM: Controlled by regulated intramembrane proteolysis (RIP). Undergoes metalloprotease-dependent constitutive ectodomain shedding to produce a membrane-anchored 52 kDa C-Terminal fragment which is further processed by presenilin gamma-secretase to yield an intracellular 50 kDa fragment (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Tetramer of 2 alpha and 2 beta chains linked by disulfide bonds. The alpha chains contribute to the formation of the ligand-binding domain, while the beta chain carries the kinase domain. Interacts with PIK3R1 and with the PTB/PID domains of IRS1 and SHC1 in vitro when autophosphorylated on tyrosine residues. Forms a hybrid receptor with INSR, the hybrid is a tetramer consisting of 1 alpha chain and 1 beta chain of INSR and 1 alpha chain and 1 beta chain of IGF1R. Interacts with ARRB1 and ARRB2. Interacts with GRB10. Interacts with RACK1. Interacts with SOCS1, SOCS2 and SOCS3. Interacts with 14-3-3 proteins. Interacts with NMD2. Interacts with MAP3K5. Interacts with STAT3. Found in a ternary complex with IGF1 and ITGAV:ITGB3 or ITGA6:ITGB4 (By similarity). Interacts (nascent precursor form) with ZFAND2B (PubMed:26692333). {ECO:0000250|UniProtKB:P08069, ECO:0000269|PubMed:26692333}. +Q6B9Z0 IGFL_MOUSE Insulin growth factor-like family member 140 15,667 Chain (1); Signal peptide (1) FUNCTION: Probable ligand of the IGFLR1 cell membrane receptor. {ECO:0000269|PubMed:21454693}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21454693}. SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:21454693}. TISSUE SPECIFICITY: Highly expressed in skin. Also detected in colon, thymus, mammary gland, lymph node and lung. {ECO:0000269|PubMed:21454693}. +Q3KNY0 IGFN1_MOUSE Immunoglobulin-like and fibronectin type III domain-containing protein 1 2849 303,658 Alternative sequence (5); Chain (1); Coiled coil (1); Compositional bias (1); Domain (9); Erroneous initiation (2); Sequence conflict (4) SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20206623}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:20206623}. SUBUNIT: Interacts with FLNC. Interacts with KY. {ECO:0000269|PubMed:20206623}. TISSUE SPECIFICITY: Isoform 1, isoform 3 and isoform 4 are expressed in skeletal muscle while isoform 2 is detected in both skeletal muscle and heart (at protein level). {ECO:0000269|PubMed:20206623}. +P01878 IGHA_MOUSE Ig alpha chain C region 344 36,876 Chain (1); Disulfide bond (4); Domain (3); Erroneous initiation (1); Glycosylation (5); Natural variant (15); Non-terminal residue (1) FUNCTION: Ig alpha is the major immunoglobulin class in body secretions. It may serve both to defend against local infection and to prevent access of foreign antigens to the general immunologic system. +P06336 IGHE_MOUSE Ig epsilon chain C region 421 47,321 Chain (1); Disulfide bond (4); Glycosylation (9); Non-terminal residue (1); Region (4) +P01592 IGJ_MOUSE Immunoglobulin J chain 159 18,014 Chain (1); Disulfide bond (5); Glycosylation (1); Sequence conflict (4); Signal peptide (1) FUNCTION: Serves to link two monomer units of either IgM or IgA. In the case of IgM, the J chain-joined dimer is a nucleating unit for the IgM pentamer, and in the case of IgA it induces larger polymers. It also help to bind these immunoglobulins to secretory component. {ECO:0000269|PubMed:1517233}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1517233}. +Q7TNC8 GLRA2_MOUSE Glycine receptor subunit alpha-2 452 52,062 Chain (1); Disulfide bond (2); Glycosylation (2); Metal binding (3); Region (1); Signal peptide (1); Site (1); Topological domain (5); Transmembrane (4) TRANSMEM 257 278 Helical; Name=1. {ECO:0000250|UniProtKB:P23415}.; TRANSMEM 284 304 Helical; Name=2. {ECO:0000250|UniProtKB:P23415}.; TRANSMEM 316 336 Helical; Name=3. {ECO:0000250|UniProtKB:P23415}.; TRANSMEM 421 441 Helical; Name=4. {ECO:0000250|UniProtKB:P23415}. TOPO_DOM 28 256 Extracellular. {ECO:0000250|UniProtKB:P23415}.; TOPO_DOM 279 283 Cytoplasmic. {ECO:0000250|UniProtKB:P23415}.; TOPO_DOM 305 315 Extracellular. {ECO:0000250|UniProtKB:P23415}.; TOPO_DOM 337 420 Cytoplasmic. {ECO:0000250|UniProtKB:P23415}.; TOPO_DOM 442 452 Extracellular. {ECO:0000250|UniProtKB:P23415}. FUNCTION: Glycine receptors are ligand-gated chloride channels. Channel opening is triggered by extracellular glycine. Channel opening is also triggered by taurine and beta-alanine. Plays a role in the down-regulation of neuronal excitability. Contributes to the generation of inhibitory postsynaptic currents. Plays a role in cellular responses to ethanol. {ECO:0000250|UniProtKB:P23416}. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane {ECO:0000305|PubMed:15329889}; Multi-pass membrane protein {ECO:0000305}. Cell junction, synapse {ECO:0000269|PubMed:15329889}. Cell membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P23415}. Cell projection {ECO:0000269|PubMed:15329889}. SUBUNIT: Homopentamer (in vitro). Interacts with GLRB. Heteropentamer composed of GLRA2 and GLRB. Both homopentamers and heteropentamers form functional ion channels, but their characteristics are subtly different. {ECO:0000250|UniProtKB:P23416}. TISSUE SPECIFICITY: Detected in the retina inner plexiform layer (at protein level) (PubMed:15329889). Detected in neonate retina. Detected in brain (PubMed:21924294). Detected in spinal cord, with higher levels in the dorsal horn (PubMed:16847326, PubMed:21924294). {ECO:0000269|PubMed:15329889, ECO:0000269|PubMed:16847326, ECO:0000269|PubMed:21924294}. +Q6EAL8 IL31_MOUSE Interleukin-31 (IL-31) 163 18,120 Chain (1); Glycosylation (3); Signal peptide (1) FUNCTION: Activates STAT3 and possibly STAT1 and STAT5 through the IL31 heterodimeric receptor composed of IL31RA and OSMR (PubMed:15184896). May function in skin immunity (PubMed:15184896). Enhances myeloid progenitor cell survival in vitro (PubMed:17379091). Induces RETNLA and serum amyloid A protein expression in macrophages (PubMed:25847241). {ECO:0000269|PubMed:15184896, ECO:0000269|PubMed:17379091, ECO:0000269|PubMed:25847241}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q8R1R4 IL34_MOUSE Interleukin-34 (IL-34) 235 26,764 Alternative sequence (2); Beta strand (5); Chain (1); Glycosylation (1); Helix (9); Signal peptide (1); Turn (3) FUNCTION: Cytokine that promotes the proliferation, survival and differentiation of monocytes and macrophages. Promotes the release of proinflammatory chemokines, and thereby plays an important role in innate immunity and in inflammatory processes. Plays an important role in the regulation of osteoclast proliferation and differentiation, and in the regulation of bone resorption. Signaling via CSF1R and its downstream effectors stimulates phosphorylation of MAPK1/ERK2 AND MAPK3/ERK1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Homodimer. Interacts with CSF1R (By similarity). {ECO:0000250}. +Q9JLA2 IL36A_MOUSE Interleukin-36 alpha (FIL1 epsilon) (Interleukin-1 epsilon) (IL-1 epsilon) (Interleukin-1 family member 6) (IL-1F6) (Interleukin-1 homolog 1) (IL-1H1) 160 18,015 Chain (1); Modified residue (1); Propeptide (1) FUNCTION: Cytokine that binds to and signals through the IL1RL2/IL-36R receptor which in turn activates NF-kappa-B and MAPK signaling pathways in target cells linked to a pro-inflammatory response. Part of the IL-36 signaling system that is thought to be present in epithelial barriers and to take part in local inflammatory response; similar to the IL-1 system with which it shares the coreceptor IL1RAP. Seems to be involved in skin inflammatory response by acting on keratinocytes, dendritic cells and indirectly on T-cells to drive tissue infiltration, cell maturation and cell proliferation. Induces the production of proinflammatory cytokines, including IL-12, Il-1 beta, IL-6, TNF-alpha and IL-23 in bone marrow-derived dendritic cells (BMDCs). Involved in dendritic cell maturation by stimulating the surface expression of CD80, CD86 and MHC class II. Induces the production of IFN-gamma, IL-4 and IL-17 by cultured CD4(+) T-cells and splenocytes. May play a role in proinflammatory effects in the lung: induces the expression of CXCL1 and CXCL2 in the lung, and the expression of TNF-alpha, IL-36c, IL-1A, IL-1B, CXCL1 and CXCL2 in isolated splenic CD11c(+) alveolar macrophages. May be involved in T-cell maturation by stimulating the surface expression of CD40 and modestly CD80 and CD86 in splenic CD11c(+) cells. May be involved in CD4(+) T-cell proliferation. Induces NF-kappa B activation in macrophages. {ECO:0000269|PubMed:21860022, ECO:0000269|PubMed:21965679, ECO:0000269|PubMed:23029241, ECO:0000269|PubMed:24829417}. PTM: N-terminal truncation leads to a dramatic enhancement of its activity (>1000-fold). {ECO:0000269|PubMed:21965679}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Highly expressed in embryonic tissue and in tissues containing epithelial cells. Elevated expression levels are detected in chronic kidney disease; expressed inepithelia from the distal convoluted tubules (DCTs) to the cortical collecting ducts (CCDs) in single nephrons (at protein level). {ECO:0000269|PubMed:11466363, ECO:0000269|PubMed:20101239}. +Q9D6Z6 IL36B_MOUSE Interleukin-36 beta (Interleukin-1 family member 8) (IL-1F8) 183 20,878 Chain (1); Erroneous initiation (1); Propeptide (1) FUNCTION: Cytokine that binds to and signals through the IL1RL2/IL-36R receptor which in turn activates NF-kappa-B and MAPK signaling pathways in target cells linked to a pro-inflammatory response. Part of the IL-36 signaling system that is thought to be present in epithelial barriers and to take part in local inflammatory response; similar to the IL-1 system with which it shares the coreceptor IL1RAP. Stimulates production of interleukin-6 and interleukin-8 in synovial fibrobasts, articular chondrocytes and mature adipocytes. Induces expression of a number of antimicrobial peptides including beta-defensin 4 and beta-defensin 103 as well as a number of matrix metalloproteases (By similarity). Seems to be involved in skin inflammatory response by acting on keratinocytes, dendritic cells and indirectly on T-cells to drive tissue infiltration, cell maturation and cell proliferation. Induces the production of proinflammatory cytokines in bone marrow-derived dendritic cells (BMDCs), including IL-12, Il-1 beta, IL-6, TNF-alpha and IL-23, and activates p38 MAPK phosphorylation in BMDCs. Involved in dendritic cell maturation by stimulating the surface expression of CD80, CD86 and MHC class II. Induces the production of IFN-gamma, IL-4 and IL-17 by T-helper 1 (Th1) cells, cultured CD4(+) T-cells and splenocytes. {ECO:0000250|UniProtKB:Q9NZH7, ECO:0000269|PubMed:21860022, ECO:0000269|PubMed:21965679}. PTM: N-terminal truncation leads to a dramatic enhancement of its activity (>1000-fold). {ECO:0000269|PubMed:21965679}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19717513}. Note=Secreted upon LPS treatment followed by ATP-induced activation of P2rx7. {ECO:0000269|PubMed:19717513}. +P01586 IL3_MOUSE Interleukin-3 (IL-3) (Hematopoietic growth factor) (Mast cell growth factor) (MCGF) (Multipotential colony-stimulating factor) (P-cell-stimulating factor) 166 18,540 Beta strand (3); Chain (1); Disulfide bond (2); Glycosylation (2); Helix (6); Signal peptide (1); Turn (2) FUNCTION: Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages.; FUNCTION: This CSF induces granulocytes, macrophages, mast cells, stem cells, erythroid cells, eosinophils and megakaryocytes. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Monomer. TISSUE SPECIFICITY: Activated T-cells, mast cells, natural killer cells. +Q7TT15 GLT17_MOUSE Polypeptide N-acetylgalactosaminyltransferase 17 (EC 2.4.1.41) (Polypeptide GalNAc transferase-like protein 3) (GalNAc-T-like protein 3) (pp-GaNTase-like protein 3) (Protein-UDP acetylgalactosaminyltransferase-like protein 3) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 3) (Williams-Beuren syndrome chromosomal region 17 protein homolog) 598 67,691 Alternative sequence (1); Binding site (4); Chain (1); Disulfide bond (5); Domain (1); Glycosylation (3); Metal binding (3); Region (2); Sequence conflict (3); Topological domain (2); Transmembrane (1) TRANSMEM 7 27 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 28 598 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: May catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. {ECO:0000250|UniProtKB:Q9HCQ5}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. DOMAIN: There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding. {ECO:0000250}.; DOMAIN: The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity. {ECO:0000250}. +P07750 IL4_MOUSE Interleukin-4 (IL-4) (B-cell IgG differentiation factor) (B-cell growth factor 1) (B-cell stimulatory factor 1) (BSF-1) (IGG1 induction factor) (Lymphocyte stimulatory factor 1) 140 15,834 Chain (1); Disulfide bond (3); Glycosylation (3); Signal peptide (1) FUNCTION: Participates in at least several B-cell activation processes as well as of other cell types (PubMed:3083412). It is a costimulator of DNA-synthesis. It induces the expression of class II MHC molecules on resting B-cells (PubMed:3498301). It enhances both secretion and cell surface expression of IgE and IgG1 (PubMed:3498301). It also regulates the expression of the low affinity Fc receptor for IgE (CD23) on both lymphocytes and monocytes. Positively regulates IL31RA expression in macrophages (PubMed:25847241). Stimulates autophagy in dendritic cells by interfering with mTORC1 signaling and through the induction of RUFY4 (PubMed:26416964). {ECO:0000269|PubMed:25847241, ECO:0000269|PubMed:26416964, ECO:0000269|PubMed:3083412, ECO:0000269|PubMed:3498301}. SUBCELLULAR LOCATION: Secreted. +Q6X632 GPR75_MOUSE Probable G-protein coupled receptor 75 540 59,531 Chain (1); Compositional bias (1); Erroneous initiation (1); Glycosylation (3); Sequence conflict (1); Topological domain (8); Transmembrane (7) TRANSMEM 47 67 Helical; Name=1. {ECO:0000255}.; TRANSMEM 87 107 Helical; Name=2. {ECO:0000255}.; TRANSMEM 121 141 Helical; Name=3. {ECO:0000255}.; TRANSMEM 161 181 Helical; Name=4. {ECO:0000255}.; TRANSMEM 206 226 Helical; Name=5. {ECO:0000255}.; TRANSMEM 319 339 Helical; Name=6. {ECO:0000255}.; TRANSMEM 351 371 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 46 Extracellular. {ECO:0000255}.; TOPO_DOM 68 86 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 108 120 Extracellular. {ECO:0000255}.; TOPO_DOM 142 160 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 182 205 Extracellular. {ECO:0000255}.; TOPO_DOM 227 318 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 340 350 Extracellular. {ECO:0000255}.; TOPO_DOM 372 540 Cytoplasmic. {ECO:0000255}. FUNCTION: G protein-coupled receptor that is activated by the chemokine CCL5/RANTES. Probably coupled to heterotrimeric Gq proteins, it stimulates inositol trisphosphate production and calcium mobilization upon activation. Together with CCL5/RANTES, may play a role in neuron survival through activation of a downstream signaling pathway involving the PI3, Akt and MAP kinases. CCL5/RANTES may also regulate insulin secretion by pancreatic islet cells through activation of this receptor. {ECO:0000269|PubMed:17001303, ECO:0000303|PubMed:23979485}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein {ECO:0000305|PubMed:17001303}. TISSUE SPECIFICITY: Highly expressed in brain and heart. Also detected in skeletal muscle, liver and kidney. Also expressed by islet cells (at protein level). {ECO:0000269|PubMed:17001303, ECO:0000269|PubMed:23979485}. +O88310 ITL1A_MOUSE Intelectin-1a (Galactofuranose-binding lectin) (Intestinal lactoferrin receptor) 313 34,953 Binding site (1); Chain (1); Disulfide bond (4); Domain (1); Lipidation (1); Mass spectrometry (1); Metal binding (11); Propeptide (1); Region (1); Signal peptide (1) FUNCTION: Lectin that specifically recognizes microbial carbohydrate chains in a calcium-dependent manner (PubMed:26148048). Binds to microbial glycans that contain a terminal acyclic 1,2-diol moiety, including beta-linked D-galactofuranose (beta-Galf), D-phosphoglycerol-modified glycans, D-glycero-D-talo-oct-2-ulosonic acid (KO) and 3-deoxy-D-manno-oct-2-ulosonic acid (KDO). Binds to glycans from Gram-positive and Gram-negative bacteria, including K.pneumoniae, S.pneumoniae, Y.pestis, P.mirabilis and P.vulgaris. Does not bind mammalian glycans. Probably plays a role in the defense system against microorganisms. May function as adipokine that has no effect on basal glucose uptake but enhances insulin-stimulated glucose uptake in adipocytes. Increases AKT phosphorylation in the absence and presence of insulin. May interact with lactoferrin/LTF and increase its uptake, and may thereby play a role in iron absorption (By similarity). {ECO:0000250|UniProtKB:Q8WWA0, ECO:0000269|PubMed:26148048}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8WWA0}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q8WWA0}. Secreted {ECO:0000250|UniProtKB:Q8WWA0}. Note=Enriched in lipid rafts. {ECO:0000269|PubMed:16866365}. SUBUNIT: Monomer (PubMed:17621593). May interact with LTF (By similarity). {ECO:0000250|UniProtKB:Q8WWA0, ECO:0000269|PubMed:17621593}. TISSUE SPECIFICITY: Expressed in small intestinal Paneth cells in uninfected mice. Expression also detected in various other tissues including stomach, kidney, ovary and brain. {ECO:0000269|PubMed:15222482, ECO:0000269|PubMed:15265922, ECO:0000269|PubMed:16866365, ECO:0000269|PubMed:16936804, ECO:0000269|PubMed:9790983}. +Q9DBM1 GPTC1_MOUSE G patch domain-containing protein 1 930 103,008 Chain (1); Cross-link (1); Domain (1); Initiator methionine (1); Modified residue (5); Sequence conflict (1) +Q9JJA9 GRASP_MOUSE General receptor for phosphoinositides 1-associated scaffold protein (GRP1-associated scaffold protein) 392 42,337 Chain (1); Compositional bias (1); Domain (1); Modified residue (5); Region (1); Sequence conflict (1) FUNCTION: Plays a role in intracellular trafficking and contributes to the macromolecular organization of group 1 metabotropic glutamate receptors (mGluRs) at synapses. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10828067}. Cell membrane {ECO:0000269|PubMed:10828067}. Note=Primarily localized to the plasma membrane but also distributed diffusely throughout the cytoplasm. SUBUNIT: Heteromer. Composed of GRASP, PSCD2 and at least one GRM1. Also interacts with GRM2, GRM3 and GRM5 (By similarity). Interacts with PSCD3. {ECO:0000250, ECO:0000269|PubMed:10828067}. TISSUE SPECIFICITY: Highly expressed in brain, heart and lung, and to a lower extent in embryo, kidney and ovary. {ECO:0000269|PubMed:10828067, ECO:0000269|PubMed:11850456}. +O35205 GRAK_MOUSE Granzyme K (EC 3.4.21.-) 263 29,251 Active site (3); Chain (1); Disulfide bond (4); Domain (1); Propeptide (1); Signal peptide (1) SUBCELLULAR LOCATION: Cytoplasmic granule. +Q925T6 GRIP1_MOUSE Glutamate receptor-interacting protein 1 (GRIP-1) 1127 122,058 Alternative sequence (7); Beta strand (8); Chain (1); Domain (7); Helix (2); Lipidation (1); Modified residue (1); Sequence conflict (2); Turn (1) FUNCTION: May play a role as a localized scaffold for the assembly of a multiprotein signaling complex and as mediator of the trafficking of its binding partners at specific subcellular location in neurons (By similarity). Through complex formation with NSG1, GRIA2 and STX12 controls the intracellular fate of AMPAR and the endosomal sorting of the GRIA2 subunit toward recycling and membrane targeting (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P97879}. PTM: Palmitoylation of isoform 2. {ECO:0000269|PubMed:11335060}. SUBCELLULAR LOCATION: Cytoplasmic vesicle. Endoplasmic reticulum. Cell junction, synapse, postsynaptic cell membrane {ECO:0000250}. Note=Cytoplasmic and membrane-associated with vesicles, peri-Golgi complexes and endoplasmic reticulum. Enriched in postsynaptic plasma membrane and postsynaptic densities (By similarity). The palmitoylated form of isoform 2 is exclusively membrane-associated. {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 2: Membrane; Lipid-anchor. SUBUNIT: Interacts with EFNB3, GRIA2, GRIA3, GRIPAP1/GRASP1, PPFIA1, PPFIA4, FRAS1, PTPRF, liprins-alpha and the C-terminal tail of PRLHR. Can form homomultimers or heteromultimers with GRIP2 (By similarity). Interacts with EFNB1, EPHA7, EPHB2, KIF5A, KIF5B and KIF5C. Forms a ternary complex with GRIA2 and CSPG4. Interacts with ATAD1 in an ATP-dependent manner. ATAD1-catalyzed ATP hydrolysis disrupts binding to ATAD1 and to GRIA2 and leads to AMPAR complex disassembly. Interacts with SLC30A9 and PLCD4. Interacts with BUD23 (By similarity). Forms a complex with NSG1, GRIA2 and STX12; controls the intracellular fate of AMPAR and the endosomal sorting of the GRIA2 subunit toward recycling and membrane targeting. Interacts with NSG1 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P97879}. DOMAIN: PDZ 6 mediates interaction with the PDZ recognition motif of EFNB1 and EPHB2 and with the C-terminus of PPFIA1 and PPFIA4. PDZ 4 and PDZ 5 mediate interaction with the C-terminus of GRIA2 and GRIA3. PDZ 4, PDZ 5 and PDZ 6 mediate homomultimers. PDZ 7 mediates interaction with PDZ domain of GRASP1. PDZ 6 mediates interaction with the C-terminal of liprins-alpha. PDZ 1, PDZ 2 and PDZ 3 mediate interaction with the PDZ-binding motif of FRAS1. PDZ 4 and PDZ 5 mediate interaction with PRLHR (By similarity). PDZ 7 domain binds CSPG4. {ECO:0000250, ECO:0000269|PubMed:12458226}. TISSUE SPECIFICITY: Expressed in brain. Isoform 2 is the major isoform in brain. Expressed in oligodendrocyte lineage cells. {ECO:0000269|PubMed:11335060, ECO:0000269|PubMed:12458226}. +Q61627 GRID1_MOUSE Glutamate receptor ionotropic, delta-1 (GluD1) (GluR delta-1 subunit) 1009 112,210 Beta strand (17); Chain (1); Disulfide bond (3); Glycosylation (3); Helix (13); Mutagenesis (1); Region (1); Sequence conflict (1); Signal peptide (1); Site (1); Topological domain (4); Transmembrane (3); Turn (5) TRANSMEM 563 583 Helical. {ECO:0000255}.; TRANSMEM 638 658 Helical. {ECO:0000255}.; TRANSMEM 831 851 Helical. {ECO:0000255}. TOPO_DOM 21 562 Extracellular. {ECO:0000255}.; TOPO_DOM 584 637 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 659 830 Extracellular. {ECO:0000255}.; TOPO_DOM 852 1009 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for glutamate. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Dimer (PubMed:27418511). Interacts (via extracellular N-terminal domain) with CBLN1 (via C1q domain), and more weakly with CBLN2 (PubMed:22220752, PubMed:27418511). {ECO:0000269|PubMed:22220752, ECO:0000269|PubMed:27418511}. TISSUE SPECIFICITY: Equally in forebrain and cerebellum. {ECO:0000269|PubMed:1372507}. +P42867 GPT_MOUSE UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase (EC 2.7.8.15) (GlcNAc-1-P transferase) (G1PT) (GPT) (N-acetylglucosamine-1-phosphate transferase) 410 46,412 Binding site (8); Chain (1); Glycosylation (1); Metal binding (2); Natural variant (1); Region (3); Topological domain (11); Transmembrane (10) TRANSMEM 11 40 Helical; Name=Helix 1. {ECO:0000250|UniProtKB:Q9H3H5}.; TRANSMEM 61 80 Helical; Name=Helix 2. {ECO:0000250|UniProtKB:Q9H3H5}.; TRANSMEM 94 120 Helical; Name=Helix 3. {ECO:0000250|UniProtKB:Q9H3H5}.; TRANSMEM 124 145 Helical; Name=Helix 4. {ECO:0000250|UniProtKB:Q9H3H5}.; TRANSMEM 169 188 Helical; Name=Helix 5. {ECO:0000250|UniProtKB:Q9H3H5}.; TRANSMEM 195 215 Helical; Name=Helix 6. {ECO:0000250|UniProtKB:Q9H3H5}.; TRANSMEM 221 244 Helical; Name=Helix 7. {ECO:0000250|UniProtKB:Q9H3H5}.; TRANSMEM 253 271 Helical; Name=Helix 8. {ECO:0000250|UniProtKB:Q9H3H5}.; TRANSMEM 274 295 Helical; Name=Helix 9. {ECO:0000250|UniProtKB:Q9H3H5}.; TRANSMEM 378 402 Helical; Name=Helix 10. {ECO:0000250|UniProtKB:Q9H3H5}. TOPO_DOM 1 10 Lumenal. {ECO:0000305}.; TOPO_DOM 41 60 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 81 93 Lumenal. {ECO:0000305}.; TOPO_DOM 121 123 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 146 168 Lumenal. {ECO:0000305}.; TOPO_DOM 189 194 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 216 220 Lumenal. {ECO:0000305}.; TOPO_DOM 245 252 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 272 273 Lumenal. {ECO:0000305}.; TOPO_DOM 296 377 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 403 410 Lumenal. {ECO:0000305}. Protein modification; protein glycosylation. FUNCTION: Catalyzes the initial step of dolichol-linked oligosaccharide biosynthesis in N-linked protein glycosylation pathway: transfers GlcNAc-1-P from UDP-GlcNAc onto the carrier lipid dolichyl phosphate (P-dolichol), yielding GlcNAc-P-P-dolichol. {ECO:0000250|UniProtKB:Q9H3H5}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9H3H5}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9H3H5}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9H3H5}. +P51855 GSHB_MOUSE Glutathione synthetase (GSH synthetase) (GSH-S) (EC 6.3.2.3) (Glutathione synthase) 474 52,247 Binding site (9); Chain (1); Initiator methionine (1); Metal binding (3); Modified residue (2); Nucleotide binding (2); Region (4) Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 2/2. SUBUNIT: Homodimer. {ECO:0000250}. +Q2NL51 GSK3A_MOUSE Glycogen synthase kinase-3 alpha (GSK-3 alpha) (EC 2.7.11.26) (Serine/threonine-protein kinase GSK3A) (EC 2.7.11.1) 490 51,661 Active site (1); Binding site (1); Chain (1); Compositional bias (1); Domain (1); Initiator methionine (1); Modified residue (7); Mutagenesis (1); Nucleotide binding (1) FUNCTION: Constitutively active protein kinase that acts as a negative regulator in the hormonal control of glucose homeostasis, Wnt signaling and regulation of transcription factors and microtubules, by phosphorylating and inactivating glycogen synthase (GYS1 or GYS2), CTNNB1/beta-catenin, APC and AXIN1. Requires primed phosphorylation of the majority of its substrates. Contributes to insulin regulation of glycogen synthesis by phosphorylating and inhibiting GYS1 activity and hence glycogen synthesis. Regulates glycogen metabolism in liver, but not in muscle. May also mediate the development of insulin resistance by regulating activation of transcription factors. In Wnt signaling, regulates the level and transcriptional activity of nuclear CTNNB1/beta-catenin. Facilitates amyloid precursor protein (APP) processing and the generation of APP-derived amyloid plaques found in Alzheimer disease. May be involved in the regulation of replication in pancreatic beta-cells. Is necessary for the establishment of neuronal polarity and axon outgrowth. Through phosphorylation of the anti-apoptotic protein MCL1, may control cell apoptosis in response to growth factors deprivation. {ECO:0000269|PubMed:15791206, ECO:0000269|PubMed:16543145, ECO:0000269|PubMed:17391670, ECO:0000269|PubMed:17908561}. PTM: Phosphorylated by AKT1 at Ser-21: upon insulin-mediated signaling, the activated PKB/AKT1 protein kinase phosphorylates and desactivates GSK3A, resulting in the dephosphorylation and activation of GYS1. Activated by phosphorylation at Tyr-279. {ECO:0000269|PubMed:15791206}. SUBUNIT: Monomer. Interacts with AXIN1 and CTNNB1/beta-catenin (By similarity). Interacts with ARRB2 (PubMed:16051150). Interacts with CTNND2 (By similarity). {ECO:0000250|UniProtKB:P49840, ECO:0000269|PubMed:16051150}. +Q9JI57 GT2D1_MOUSE General transcription factor II-I repeat domain-containing protein 1 (GTF2I repeat domain-containing protein 1) (Binding factor for early enhancer) 1104 123,483 Alternative sequence (5); Chain (1); Compositional bias (1); Cross-link (23); Frameshift (1); Modified residue (1); Motif (1); Repeat (6); Sequence conflict (13) FUNCTION: May be a transcription regulator involved in cell-cycle progression and skeletal muscle differentiation. May repress GTF2I transcriptional functions, by preventing its nuclear residency, or by inhibiting its transcriptional activation. May contribute to slow-twitch fiber type specificity during myogenesis and in regenerating muscles. Binds troponin I slow-muscle fiber enhancer (USE B1). Binds specifically and with high affinity to the EFG sequences derived from the early enhancer of HOXC8. {ECO:0000269|PubMed:11438732}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00484, ECO:0000269|PubMed:12780350}. SUBUNIT: Interacts with the retinoblastoma protein (RB1) via its C-terminus. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. +Q3UHH8 GXLT1_MOUSE Glucoside xylosyltransferase 1 (EC 2.4.2.42) (Glycosyltransferase 8 domain-containing protein 3) 404 46,491 Alternative sequence (1); Chain (1); Glycosylation (1); Topological domain (2); Transmembrane (1) TRANSMEM 7 29 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 30 404 Lumenal. {ECO:0000255}. FUNCTION: Glycosyltransferase which elongates the O-linked glucose attached to EGF-like repeats in the extracellular domain of Notch proteins by catalyzing the addition of xylose. {ECO:0000250|UniProtKB:Q4G148}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. +P43277 H13_MOUSE Histone H1.3 (H1 VAR.4) (H1d) 221 22,100 Chain (1); Domain (1); Initiator methionine (1); Modified residue (14); Sequence conflict (1) FUNCTION: Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity). {ECO:0000250, ECO:0000269|PubMed:12808097}. PTM: H1 histones are progressively phosphorylated during the cell cycle, becoming maximally phosphorylated during late G2 phase and M phase, and being dephosphorylated sharply thereafter. {ECO:0000250|UniProtKB:P43275}.; PTM: Hydroxybutyrylation of histones is induced by starvation. {ECO:0000269|PubMed:27105115}.; PTM: Citrullination at Arg-55 (H1R54ci) by PADI4 takes place within the DNA-binding site of H1 and results in its displacement from chromatin and global chromatin decondensation, thereby promoting pluripotency and stem cell maintenance. {ECO:0000269|PubMed:24463520}. SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Mainly localizes in euchromatin. {ECO:0000250}. DOMAIN: The C-terminal domain is required for high-affinity binding to chromatin. {ECO:0000250}. +P43274 H14_MOUSE Histone H1.4 (H1 VAR.2) (H1e) 219 21,977 Chain (1); Domain (1); Initiator methionine (1); Modified residue (18) FUNCTION: Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation. {ECO:0000269|PubMed:12808097, ECO:0000269|PubMed:16377562}. PTM: Citrullination at Arg-54 (H1R54ci) by PADI4 takes place within the DNA-binding site of H1 and results in its displacement from chromatin and global chromatin decondensation, thereby promoting pluripotency and stem cell maintenance. {ECO:0000269|PubMed:24463520}.; PTM: ADP-ribosylated on Ser-55, Ser-113 and Ser-150 in response to DNA damage. {ECO:0000250|UniProtKB:P10412}.; PTM: H1 histones are progressively phosphorylated during the cell cycle, becoming maximally phosphorylated during late G2 phase and M phase, and being dephosphorylated sharply thereafter. {ECO:0000250|UniProtKB:P43275}.; PTM: Acetylated at Lys-26. Deacetylated at Lys-26 by SIRT1. {ECO:0000250|UniProtKB:P10412}.; PTM: Hydroxybutyrylation of histones is induced by starvation. {ECO:0000250|UniProtKB:P43277}. SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Mainly localizes in heterochromatin. Dysplays a punctuate staining pattern in the nucleus. {ECO:0000250}. DOMAIN: The C-terminal domain is required for high-affinity binding to chromatin. {ECO:0000250}. +Q3UHD2 GFOD1_MOUSE Glucose-fructose oxidoreductase domain-containing protein 1 (EC 1.-.-.-) 390 43,286 Chain (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +J3KML8 GFY_MOUSE Golgi-associated olfactory signaling regulator (Protein Goofy) 504 53,786 Chain (1); Compositional bias (2); Glycosylation (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 398 418 Helical. {ECO:0000255}. TOPO_DOM 23 397 Extracellular. {ECO:0000255}.; TOPO_DOM 419 504 Cytoplasmic. {ECO:0000255}. FUNCTION: Required for proper function of the olfactory system. May be involved in establishing the acuity of olfactory sensory signaling. {ECO:0000269|PubMed:23926254}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:23926254}; Single-pass type I membrane protein {ECO:0000269|PubMed:23926254}. TISSUE SPECIFICITY: Specifically expressed in the olfactory epithelium and vomeronasal organ throughout development. Expressed in both immature and mature olfactory sensory neurons in the olfactory epithelium (at protein level). {ECO:0000269|PubMed:23926254}. +Q99JY3 GIMA4_MOUSE GTPase IMAP family member 4 (Immunity-associated nucleotide 1 protein) (IAN-1) (Immunity-associated protein 4) 219 24,554 Binding site (2); Chain (1); Domain (1); Nucleotide binding (2) FUNCTION: Exhibits intrisinic GTPase activity. Shows a higher affinity for GDP over GTP (about 12-fold higher), and binding shows an absolute requirement for magnesium (By similarity). May play a role in regulating lymphocyte apoptosis. {ECO:0000250, ECO:0000269|PubMed:16569770}. PTM: Phosphorylated at very low levels in resting splenocytes. Rapidly and transiently phosphorylated in response to splenocyte activation. Phosphorylation is increased in cells undergoing apoptosis. {ECO:0000269|PubMed:16569770}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:16569770}. TISSUE SPECIFICITY: Detected on splenocytes, B-cells and T-cells (at protein level). {ECO:0000269|PubMed:16569770}. +Q9JMB0 GKAP1_MOUSE G kinase-anchoring protein 1 (cGMP-dependent protein kinase-anchoring protein of 42 kDa) 366 41,763 Chain (1); Coiled coil (4); Modified residue (4); Mutagenesis (3); Region (1); Sequence conflict (2) FUNCTION: Regulates insulin-dependent IRS1 tyrosine phosphorylation in adipocytes by modulating the availability of IRS1 to IR tyrosine kinase. Its association with IRS1 is required for insulin-induced translocation of SLC2A4 to the cell membrane. Involved in TNF-induced impairment of insulin-dependent IRS1 tyrosine phosphorylation. {ECO:0000269|PubMed:25586176}. SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:10671526}. SUBUNIT: Interacts with PRKG1 (PubMed:10671526). Interacts with IRS1 (PubMed:25586176). {ECO:0000269|PubMed:10671526, ECO:0000269|PubMed:25586176}. TISSUE SPECIFICITY: Predominantly expressed in testis. Expressed in the adipose tissue (at protein level) (PubMed:25586176). In the testis it is restricted to spermatocytes and early round spermatids. Also expressed in cardiac fibroblasts. {ECO:0000269|PubMed:15028281, ECO:0000269|PubMed:25586176}. +P10630 IF4A2_MOUSE Eukaryotic initiation factor 4A-II (eIF-4A-II) (eIF4A-II) (EC 3.6.4.13) (ATP-dependent RNA helicase eIF4A-2) 407 46,402 Alternative sequence (1); Chain (1); Domain (2); Modified residue (1); Motif (2); Nucleotide binding (1); Sequence conflict (4) FUNCTION: ATP-dependent RNA helicase which is a subunit of the eIF4F complex involved in cap recognition and is required for mRNA binding to ribosome. In the current model of translation initiation, eIF4A unwinds RNA secondary structures in the 5'-UTR of mRNAs which is necessary to allow efficient binding of the small ribosomal subunit, and subsequent scanning for the initiator codon. SUBUNIT: eIF4F is a multi-subunit complex, the composition of which varies with external and internal environmental conditions. It is composed of at least EIF4A, EIF4E and EIF4G1/EIFFG3. Interacts with EIF4E. May interact with NOM1 (By similarity). {ECO:0000250}. +Q2NKH9 GL6D1_MOUSE Glycosyltransferase 6 domain-containing protein 1 (EC 2.4.1.-) 311 37,081 Active site (1); Chain (1); Glycosylation (1); Region (3); Topological domain (2); Transmembrane (1) TRANSMEM 6 26 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 5 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 27 311 Lumenal. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. +Q8K3I9 GLCI1_MOUSE Glucocorticoid-induced transcript 1 protein (Glucocorticoid-induced gene 18 protein) (Testhymin) (Thymocyte/spermatocyte selection protein 1) 537 57,479 Alternative sequence (3); Chain (1); Coiled coil (1); Compositional bias (3); Modified residue (21); Sequence conflict (2) TISSUE SPECIFICITY: Predominantly expressed in thymus and testis, especially in CD4+CD8+ cells and at specific stages of spermatogenesis. {ECO:0000269|PubMed:12557054}. +Q8R322 GLE1_MOUSE Nucleoporin GLE1 (GLE1-like protein) 699 79,574 Chain (1); Coiled coil (2); Compositional bias (1); Frameshift (2); Modified residue (4); Region (3); Sequence conflict (9) FUNCTION: Required for the export of mRNAs containing poly(A) tails from the nucleus into the cytoplasm. May be involved in the terminal step of the mRNA transport through the nuclear pore complex (NPC) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q53GS7}. Cytoplasm {ECO:0000250|UniProtKB:Q53GS7}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q53GS7}. Note=Shuttles between the nucleus and the cytoplasm. Shuttling is essential for its mRNA export function. {ECO:0000250|UniProtKB:Q53GS7}. SUBUNIT: Associated with the NPC, it however may not be a stable component of the NPC complex since it shuttles between the nucleus and the cytoplasm. Interacts with nuclear pore complex proteins NUP155 and NUPL2 (By similarity). {ECO:0000250}. +Q9WUK2 IF4H_MOUSE Eukaryotic translation initiation factor 4H (eIF-4H) (Williams-Beuren syndrome chromosomal region 1 protein homolog) 248 27,341 Alternative sequence (1); Beta strand (6); Chain (1); Domain (1); Helix (3); Initiator methionine (1); Modified residue (12); Turn (1) FUNCTION: Stimulates the RNA helicase activity of EIF4A in the translation initiation complex. Binds weakly mRNA (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. TISSUE SPECIFICITY: Expressed at high levels in heart, liver and testis and at lower levels in brain, spleen, lung, skeletal muscle, kidney and embryonic tissues. Both isoforms are expressed at similar levels. {ECO:0000269|PubMed:11003705}. +Q8BGY2 IF5A2_MOUSE Eukaryotic translation initiation factor 5A-2 (eIF-5A-2) (eIF-5A2) (Eukaryotic initiation factor 5A isoform 2) 153 16,793 Chain (1); Initiator methionine (1); Modified residue (2) FUNCTION: mRNA-binding protein involved in translation elongation. Has an important function at the level of mRNA turnover, probably acting downstream of decapping. Involved in actin dynamics and cell cycle progression, mRNA decay and probably in a pathway involved in stress response and maintenance of cell wall integrity. Functions as a regulator of apoptosis. Mediates effects of polyamines on neuronal process extension and survival. May play an important role in brain development and function, and in skeletal muscle stem cell differentiation (By similarity). {ECO:0000250}. PTM: eIF-5A seems to be the only eukaryotic protein to have a hypusine residue which is a post-translational modification of a lysine by the addition of a butylamino group (from spermidine). SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250}. Note=Hypusine modification promotes the nuclear export and cytoplasmic localization and there was a dynamic shift in the localization from predominantly cytoplasmic to primarily nuclear under apoptotic inducing conditions. {ECO:0000250}. +P47806 GLI1_MOUSE Zinc finger protein GLI1 (Glioma-associated oncogene homolog) 1111 118,560 Chain (1); Compositional bias (1); Cross-link (1); Modified residue (1); Region (4); Sequence conflict (20); Zinc finger (5) FUNCTION: Acts as a transcriptional activator. Binds to the DNA consensus sequence 5'-GACCACCCA-3'. May regulate the transcription of specific genes during normal development. May play a role in craniofacial development and digital development, as well as development of the central nervous system and gastrointestinal tract. Mediates SHH signaling. Plays a role in cell proliferation and differentiation via its role in SHH signaling. {ECO:0000250|UniProtKB:P08151}. PTM: Phosphorylated in vitro by ULK3. {ECO:0000250|UniProtKB:P08151}.; PTM: Acetylation at Lys-520 down-regulates transcriptional activity. Deacetylated by HDAC1. {ECO:0000250|UniProtKB:P08151}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P08151}. Nucleus {ECO:0000250|UniProtKB:P08151}. Note=Tethered in the cytoplasm by binding to SUFU. Activation and translocation to the nucleus is promoted by interaction with STK36. Phosphorylation by ULK3 may promote nuclear localization. Translocation to the nucleus is promoted by interaction with ZIC1. {ECO:0000250|UniProtKB:P08151}. SUBUNIT: Interacts with KIF7 (PubMed:19592253). Interacts with STK36. Interacts with ZIC1; the interaction enhances transcription activation. Interacts with SUFU; this inhibits transcriptional activation by GLI1 (By similarity). {ECO:0000250|UniProtKB:P08151, ECO:0000269|PubMed:19592253}. +Q61602 GLI3_MOUSE Transcriptional activator GLI3 (GLI3 form of 190 kDa) (GLI3-190) (GLI3 full-length protein) (GLI3FL) [Cleaved into: Transcriptional repressor GLI3R (GLI3 C-terminally truncated form) (GLI3 form of 83 kDa) (GLI3-83)] 1583 171,655 Chain (2); Compositional bias (3); Cross-link (7); Frameshift (1); Modified residue (9); Sequence conflict (7); Zinc finger (5) FUNCTION: Has a dual function as a transcriptional activator and a repressor of the sonic hedgehog (Shh) pathway, and plays a role in limb development. The full-length GLI3 form (GLI3FL) after phosphorylation and nuclear translocation, acts as an activator (GLI3A) while GLI3R, its C-terminally truncated form, acts as a repressor. A proper balance between the GLI3 activator and the repressor GLI3R, rather than the repressor gradient itself or the activator/repressor ratio gradient, specifies limb digit number and identity. In concert with TRPS1, plays a role in regulating the size of the zone of distal chondrocytes, in restricting the zone of PTHLH expression in distal cells and in activating chondrocyte proliferation. Binds to the minimal GLI-consensus sequence 5'-GGGTGGTC-3'. {ECO:0000269|PubMed:10693759, ECO:0000269|PubMed:11053430, ECO:0000269|PubMed:17400206, ECO:0000269|PubMed:19389374, ECO:0000269|PubMed:20360384}. PTM: Phosphorylated by DYRK2 (in vitro) (By similarity). Phosphorylated on multiple sites by protein kinase A (PKA) and phosphorylation by PKA primes further phosphorylation by CK1 and GSK3. Phosphorylation is essential for its proteolytic processing. {ECO:0000250, ECO:0000269|PubMed:20360384}.; PTM: Transcriptional repressor GLI3R, a C-terminally truncated form, is generated from the full-length GLI3 protein (GLI3FL/GLI3-190) through proteolytic processing. This process requires PKA-primed phosphorylation of GLI3, ubiquitination of GLI3 and the presence of BTRC. GLI3FL is complexed with SUFU in the cytoplasm and is maintained in a neutral state. Without the Hh signal, the SUFU-GLI3 complex is recruited to cilia, leading to the efficient processing of GLI3FL into GLI3R. GLI3R formation leads to its dissociation from SUFU, allowing it to translocate into the nucleus, and repress Hh target genes. When Hh signaling is initiated, SUFU dissociates from GLI3FL and this has two consequences. First, GLI3R production is halted. Second, free GLI3FL translocates to the nucleus, where it is phosphorylated, destabilized, and converted to a transcriptional activator (GLI3A). Phosphorylated in vitro by ULK3. {ECO:0000269|PubMed:20360384}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20360384}. Cytoplasm {ECO:0000269|PubMed:20360384}. Cell projection, cilium {ECO:0000269|PubMed:20360384}. Note=Translocation to the nucleus is promoted by interaction with ZIC1 (By similarity). GLI3FL is localized predominantly in the cytoplasm while GLI3R resides mainly in the nucleus. Ciliary accumulation requires the presence of KIF7 and SMO. {ECO:0000250}. SUBUNIT: The phosphorylated form interacts with BTRC (By similarity). The full-length GLI3 form (GLI3FL) interacts with SUFU and this interaction regulates the formation of either repressor or activator forms of GLI3. Its association with SUFU is regulated by Hh signaling and dissociation of the SUFU-GLI3 interaction requires the presence of the ciliary motor KIF3A. Interacts with KIF7. The activator form of GLI3 (GLI3A) but not the repressor form (GLI3R) can interact with TRPS1. Interacts with ZIC1. Interacts with ZIC3 (via C2H2-type domains 3, 4 and 5); the interaction enhances its transcriptional activity (By similarity). Interacts with WRD11; the interaction associates EMX1 with GLI3 (PubMed:29263200). {ECO:0000250|UniProtKB:P10071, ECO:0000269|PubMed:29263200}. DISEASE: Note=Several mutations result in developmental defects of cranofacial and limb structures. In particular the add (anterior digit-pattern deformity) and pdn (polydactyly Nagoya) alleles. {ECO:0000269|PubMed:10051311, ECO:0000269|PubMed:1983115}. +Q9CWG1 GLIP1_MOUSE Glioma pathogenesis-related protein 1 (GliPR 1) 255 29,129 Chain (1); Domain (1); Signal peptide (1); Transmembrane (1) TRANSMEM 224 244 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q9JL62 GLTP_MOUSE Glycolipid transfer protein (GLTP) 209 23,690 Binding site (2); Chain (1); Initiator methionine (1); Modified residue (1); Region (2); Repeat (2); Sequence conflict (1) FUNCTION: Accelerates the intermembrane transfer of various glycolipids. Catalyzes the transfer of various glycosphingolipids between membranes but does not catalyze the transfer of phospholipids. May be involved in the intracellular translocation of glucosylceramides (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. +P21183 IL5RA_MOUSE Interleukin-5 receptor subunit alpha (IL-5 receptor subunit alpha) (IL-5R subunit alpha) (IL-5R-alpha) (IL-5RA) (CD antigen CD125) 415 46,989 Chain (1); Disulfide bond (3); Domain (2); Glycosylation (4); Motif (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 340 361 Helical. {ECO:0000255}. TOPO_DOM 18 339 Extracellular. {ECO:0000255}.; TOPO_DOM 362 415 Cytoplasmic. {ECO:0000255}. FUNCTION: This is the receptor for interleukin-5. The alpha chain binds to IL5. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Heterodimer of an alpha and a beta subunit. The beta subunit is common to the IL3, IL5 and GM-CSF receptors. Interacts with SDCBP. DOMAIN: The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.; DOMAIN: The box 1 motif is required for JAK interaction and/or activation. TISSUE SPECIFICITY: Expressed on eosinophils and basophils. Also on B-cells. +Q91XE0 GLYAT_MOUSE Glycine N-acyltransferase (EC 2.3.1.13) (Acyl-CoA:glycine N-acyltransferase) (AAc) (Aralkyl acyl-CoA N-acyltransferase) (Aralkyl acyl-CoA:amino acid N-acyltransferase) (Benzoyl-coenzyme A:glycine N-acyltransferase) (Glycine N-benzoyltransferase) (EC 2.3.1.71) 296 34,098 Alternative sequence (1); Chain (1); Modified residue (17) FUNCTION: Mitochondrial acyltransferase which transfers an acyl group to the N-terminus of glycine and glutamine, although much less efficiently. Can conjugate a multitude of substrates to form a variety of N-acylglycines, thereby detoxify xenobiotics, such as benzoic acid or salicylic acid, and endogenous organic acids, such as isovaleric acid. {ECO:0000250|UniProtKB:Q6IB77}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q6IB77}. +B5TVM2 ILDR2_MOUSE Immunoglobulin-like domain-containing receptor 2 (Lisch-like isoform 1) 661 73,235 Chain (1); Compositional bias (1); Disulfide bond (1); Domain (1); Modified residue (3); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 202 222 Helical. {ECO:0000255}. TOPO_DOM 36 201 Lumenal. {ECO:0000255}.; TOPO_DOM 223 661 Cytoplasmic. {ECO:0000255}. FUNCTION: May be involved in lipid homeostasis and ER stress pathways. {ECO:0000269|PubMed:23826244}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23826244}; Single-pass type I membrane protein {ECO:0000269|PubMed:23826244}. +Q5SV42 ILEUC_MOUSE Leukocyte elastase inhibitor C (Serine protease inhibitor EIC) (Serpin B1c) 375 41,920 Chain (1); Erroneous gene model prediction (1); Sequence conflict (1); Site (1) FUNCTION: Regulates the activity of the neutrophil proteases. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in heart. {ECO:0000269|PubMed:12189154}. +Q9CXY6 ILF2_MOUSE Interleukin enhancer-binding factor 2 (Nuclear factor of activated T-cells 45 kDa) 390 43,062 Beta strand (11); Chain (1); Compositional bias (2); Cross-link (2); Domain (1); Helix (16); Modified residue (6); Sequence caution (1); Turn (3) FUNCTION: Appears to function predominantly as a heterodimeric complex with ILF3. This complex may regulate transcription of the IL2 gene during T-cell activation. It can also promote the formation of stable DNA-dependent protein kinase holoenzyme complexes on DNA (By similarity). Essential for the efficient reshuttling of ILF3 into the nucleus (By similarity). {ECO:0000250, ECO:0000269|PubMed:10574923}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11804788}. Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. {ECO:0000250}. SUBUNIT: Forms heterodimers with ILF3. ILF2-ILF3 heterodimers may also bind to PRKDC/XRCC7: this may stabilize the interaction of PRKDC/XRCC7 and the heterodimeric complex of G22P1/KU70 and XRCC5/KU80. Forms a complex with ILF3, YLPM1, KHDRBS1, RBMX, NCOA5 and PPP1CA. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with IGF2BP1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain, kidney and ovary; highly expressed in testis, particularly within pachytene cells. {ECO:0000269|PubMed:11804788}. +O55222 ILK_MOUSE Integrin-linked protein kinase (EC 2.7.11.1) 452 51,373 Binding site (1); Chain (1); Domain (1); Modified residue (3); Nucleotide binding (1); Region (2); Repeat (5); Sequence conflict (2) FUNCTION: Receptor-proximal protein kinase regulating integrin-mediated signal transduction. May act as a mediator of inside-out integrin signaling. Focal adhesion protein part of the complex ILK-PINCH. This complex is considered to be one of the convergence points of integrin- and growth factor-signaling pathway. Could be implicated in mediating cell architecture, adhesion to integrin substrates and anchorage-dependent growth in epithelial cells. Phosphorylates beta-1 and beta-3 integrin subunit on serine and threonine residues, but also AKT1 and GSK3B. {ECO:0000250|UniProtKB:Q13418}. PTM: Autophosphorylated on serine residues. {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000269|PubMed:18325335, ECO:0000269|PubMed:18483218}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250|UniProtKB:Q13418}. Cytoplasm, myofibril, sarcomere {ECO:0000250|UniProtKB:Q13418}. Cell projection, lamellipodium {ECO:0000269|PubMed:18325335}. SUBUNIT: Interacts with FERMT2 (PubMed:18483218). Interacts with the cytoplasmic domain of ITGB1 (By similarity). Could also interact with integrin ITGB2, ITGB3 and/or ITGB5 (By similarity). Interacts (via ANK repeats) with LIMS1 and LIMS2 (By similarity). Interacts with PARVA and PARVB; these compete for the same binding site (By similarity). Interacts probably also with TGFB1I1 (PubMed:16737959). Interacts (via ANK repeats) with EPHA1 (via SAM domain); stimulated by EFNA1 but independent of the kinase activity of EPHA1 (By similarity). Interacts with LIMD2; leading to activate the protein kinase activity (By similarity). {ECO:0000250|UniProtKB:Q13418, ECO:0000269|PubMed:16737959, ECO:0000269|PubMed:18483218}. DOMAIN: A PH-like domain is involved in phosphatidylinositol phosphate binding. {ECO:0000250|UniProtKB:Q13418}. TISSUE SPECIFICITY: Highly expressed in lung, heart, kidney, liver, brain, spleen and skeletal muscle. Weakly expressed in testis. +P14719 ILRL1_MOUSE Interleukin-1 receptor-like 1 (Interleukin-33 receptor alpha chain) (Lymphocyte antigen 84) (Protein ST2) (Protein T1) 567 64,801 Alternative sequence (2); Beta strand (23); Chain (1); Disulfide bond (5); Domain (4); Glycosylation (9); Helix (5); Natural variant (1); Region (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 333 355 Helical. {ECO:0000255}. TOPO_DOM 27 332 Extracellular. {ECO:0000255}.; TOPO_DOM 356 567 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for interleukin-33 (IL-33); signaling requires association of the coreceptor IL1RAP (PubMed:18450470, PubMed:17675517). Its stimulation recruits MYD88, IRAK1, IRAK4, and TRAF6, followed by phosphorylation of MAPK3/ERK1 and/or MAPK1/ERK2, MAPK14, and MAPK8 (By similarity). Possibly involved in helper T-cell function. {ECO:0000250|UniProtKB:Q01638, ECO:0000269|PubMed:17675517, ECO:0000269|PubMed:18450470}.; FUNCTION: Isoform B: Inhibits IL-33 signaling. {ECO:0000269|PubMed:18450470}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Isoform B: Secreted. SUBUNIT: Interacts with MYD88, IRAK1, IRAK4, and TRAF6 (By similarity). Bound to its ligand IL-33, interacts with IL1RAP to form the minimal interleukin-33 signaling complex with a 1:1:1 stoichiometry. Interacts with KIT (bound to KITLG/SCF). A mast cell-specific KITLG/SCF-induced interleukin-33 signaling complex contains IL1RL1, IL1RAP, KIT and MYD88. {ECO:0000250|UniProtKB:Q01638, ECO:0000269|PubMed:17675517, ECO:0000269|PubMed:18003919, ECO:0000269|PubMed:18450470, ECO:0000269|PubMed:20200353}. TISSUE SPECIFICITY: Predominantly expressed in hematopoietic tissues, and in macrophage, erythroid, epithelial and fibroblast cell lines. Isoform A is expressed in brain astrocytes and microglia. Isoform B is expressed in brain endothelial cells. {ECO:0000269|PubMed:21349253, ECO:0000269|PubMed:8131748}. +Q9DB00 GON4L_MOUSE GON-4-like protein (GON-4 homolog) 2260 248,742 Beta strand (2); Chain (1); Compositional bias (6); Domain (3); Erroneous initiation (2); Helix (3); Modified residue (4); Region (1); Sequence caution (1); Sequence conflict (12); Turn (1) FUNCTION: Has transcriptional repressor activity, probably as part of a complex with YY1, SIN3A AND HDAC1 (PubMed:21454521). Required for B cell lymphopoiesis (PubMed:20530203). {ECO:0000269|PubMed:20530203, ECO:0000269|PubMed:21454521}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00810, ECO:0000269|PubMed:21454521}. SUBUNIT: Found in a complex with YY1, SIN3A and HDAC1. {ECO:0000269|PubMed:21454521}. TISSUE SPECIFICITY: Expressed in thymus. Specifically expressed in B cells and their precursors (at protein level). Also detected in brain, heart, spleen and bone marrow. {ECO:0000269|PubMed:20530203}. +Q80T62 GP101_MOUSE Probable G-protein coupled receptor 101 511 56,245 Chain (1); Disulfide bond (1); Glycosylation (2); Topological domain (8); Transmembrane (7) TRANSMEM 36 56 Helical; Name=1. {ECO:0000255}.; TRANSMEM 68 90 Helical; Name=2. {ECO:0000255}.; TRANSMEM 107 127 Helical; Name=3. {ECO:0000255}.; TRANSMEM 150 170 Helical; Name=4. {ECO:0000255}.; TRANSMEM 197 217 Helical; Name=5. {ECO:0000255}.; TRANSMEM 399 419 Helical; Name=6. {ECO:0000255}.; TRANSMEM 433 453 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 35 Extracellular. {ECO:0000255}.; TOPO_DOM 57 67 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 91 106 Extracellular. {ECO:0000255}.; TOPO_DOM 128 149 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 171 196 Extracellular. {ECO:0000255}.; TOPO_DOM 218 398 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 420 432 Extracellular. {ECO:0000255}.; TOPO_DOM 454 511 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed in the brain in hypothalamus. {ECO:0000269|PubMed:25470569}. +Q8K0Z9 GP153_MOUSE Probable G-protein coupled receptor 153 (G-protein coupled receptor PGR1) 631 68,459 Chain (1); Topological domain (8); Transmembrane (7) TRANSMEM 12 32 Helical; Name=1. {ECO:0000255}.; TRANSMEM 42 62 Helical; Name=2. {ECO:0000255}.; TRANSMEM 85 105 Helical; Name=3. {ECO:0000255}.; TRANSMEM 127 147 Helical; Name=4. {ECO:0000255}.; TRANSMEM 163 183 Helical; Name=5. {ECO:0000255}.; TRANSMEM 244 264 Helical; Name=6. {ECO:0000255}.; TRANSMEM 277 297 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 11 Extracellular. {ECO:0000255}.; TOPO_DOM 33 41 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 63 84 Extracellular. {ECO:0000255}.; TOPO_DOM 106 126 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 148 162 Extracellular. {ECO:0000255}.; TOPO_DOM 184 243 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 265 276 Extracellular. {ECO:0000255}.; TOPO_DOM 298 631 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q6PCP7 GP156_MOUSE Probable G-protein coupled receptor 156 (GABAB-related G-protein coupled receptor) 798 87,040 Chain (1); Coiled coil (1); Compositional bias (3); Glycosylation (1); Sequence conflict (8); Topological domain (8); Transmembrane (7) TRANSMEM 50 70 Helical; Name=1. {ECO:0000255}.; TRANSMEM 87 107 Helical; Name=2. {ECO:0000255}.; TRANSMEM 119 139 Helical; Name=3. {ECO:0000255}.; TRANSMEM 165 185 Helical; Name=4. {ECO:0000255}.; TRANSMEM 223 243 Helical; Name=5. {ECO:0000255}.; TRANSMEM 258 278 Helical; Name=6. {ECO:0000255}.; TRANSMEM 289 309 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 49 Extracellular. {ECO:0000255}.; TOPO_DOM 71 86 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 108 118 Extracellular. {ECO:0000255}.; TOPO_DOM 140 164 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 186 222 Extracellular. {ECO:0000255}.; TOPO_DOM 244 257 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 279 288 Extracellular. {ECO:0000255}.; TOPO_DOM 310 798 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein. +Q8C206 GP157_MOUSE G-protein coupled receptor 157 330 36,344 Chain (1); Compositional bias (1); Sequence conflict (2); Topological domain (8); Transmembrane (7) TRANSMEM 16 36 Helical; Name=1. {ECO:0000255}.; TRANSMEM 49 69 Helical; Name=2. {ECO:0000255}.; TRANSMEM 88 108 Helical; Name=3. {ECO:0000255}.; TRANSMEM 120 140 Helical; Name=4. {ECO:0000255}.; TRANSMEM 167 187 Helical; Name=5. {ECO:0000255}.; TRANSMEM 228 248 Helical; Name=6. {ECO:0000255}.; TRANSMEM 260 280 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 15 Extracellular. {ECO:0000255}.; TOPO_DOM 37 48 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 70 87 Extracellular. {ECO:0000255}.; TOPO_DOM 109 119 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 141 166 Extracellular. {ECO:0000255}.; TOPO_DOM 188 227 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 249 259 Extracellular. {ECO:0000255}.; TOPO_DOM 281 330 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan receptor that promotes neuronal differentiation of radial glial progenitors (RGPs) (PubMed:27142930). The activity of this receptor is mediated by a G(q)-protein that activates a phosphatidylinositol-calcium second messenger (PubMed:27142930). {ECO:0000269|PubMed:27142930}. SUBCELLULAR LOCATION: Cell projection, cilium membrane {ECO:0000269|PubMed:27142930}; Multi-pass membrane protein {ECO:0000255}. Note=Expressed in the primary cilia of radial glial progenitors (RGPs) exposed to the cerebrospinal fluid. {ECO:0000269|PubMed:27142930}. TISSUE SPECIFICITY: Expressed in the primary cilia of radial glial progenitors (RGPs) in the developing neocortex (PubMed:27142930). {ECO:0000269|PubMed:27142930}. +A0A0B4J1N3 GP15L_MOUSE Protein GPR15L 78 8,899 Chain (1); Disulfide bond (2); Signal peptide (1) FUNCTION: Chemotactic factor that mediates lymphocytes recruitement to epithelia through binding and activation of the G-protein coupled receptor GPR15 (PubMed:28900043,PubMed:28936214). May be a tumor suppressor; together with SUSD2 has a growth inhibitory effect on colon cancer cells which includes G1 cell cycle arrest (By similarity). {ECO:0000250|UniProtKB:Q6UWK7, ECO:0000269|PubMed:28900043, ECO:0000269|PubMed:28936214}.; FUNCTION: Has antimicrobial activity against Gram-positive bacteria, including Staphylococcus aureus and Actinomyces spec., and Mycoplasma hominis and lentivirus. {ECO:0000250|UniProtKB:Q6UWK7}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q6UWK7}. SUBUNIT: Interacts with SUSD2; the interaction is direct. {ECO:0000250|UniProtKB:Q6UWK7}. TISSUE SPECIFICITY: Highly abundant in the testis, colon, eye, and tongue. Detected in the epithelial layer of the colon, but not the small intestine. {ECO:0000269|PubMed:28900043, ECO:0000269|PubMed:28936214}. +Q3U3F9 GP160_MOUSE Probable G-protein coupled receptor 160 336 38,922 Chain (1); Frameshift (1); Glycosylation (1); Sequence conflict (5); Topological domain (8); Transmembrane (7) TRANSMEM 21 41 Helical; Name=1. {ECO:0000255}.; TRANSMEM 57 77 Helical; Name=2. {ECO:0000255}.; TRANSMEM 96 116 Helical; Name=3. {ECO:0000255}.; TRANSMEM 137 157 Helical; Name=4. {ECO:0000255}.; TRANSMEM 187 207 Helical; Name=5. {ECO:0000255}.; TRANSMEM 244 264 Helical; Name=6. {ECO:0000255}.; TRANSMEM 273 293 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 20 Extracellular. {ECO:0000255}.; TOPO_DOM 42 56 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 78 95 Extracellular. {ECO:0000255}.; TOPO_DOM 117 136 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 158 186 Extracellular. {ECO:0000255}.; TOPO_DOM 208 243 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 265 272 Extracellular. {ECO:0000255}.; TOPO_DOM 294 336 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q7TQN9 GP142_MOUSE Probable G-protein coupled receptor 142 365 40,758 Chain (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 67 87 Helical; Name=1. {ECO:0000255}.; TRANSMEM 103 123 Helical; Name=2. {ECO:0000255}.; TRANSMEM 141 161 Helical; Name=3. {ECO:0000255}.; TRANSMEM 186 206 Helical; Name=4. {ECO:0000255}.; TRANSMEM 225 245 Helical; Name=5. {ECO:0000255}.; TRANSMEM 265 285 Helical; Name=6. {ECO:0000255}.; TRANSMEM 305 325 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 66 Extracellular. {ECO:0000255}.; TOPO_DOM 88 102 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 124 140 Extracellular. {ECO:0000255}.; TOPO_DOM 162 185 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 207 224 Extracellular. {ECO:0000255}.; TOPO_DOM 246 264 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 286 304 Extracellular. {ECO:0000255}.; TOPO_DOM 326 365 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +P70259 GP143_MOUSE G-protein coupled receptor 143 (MOA1) (Ocular albinism type 1 protein homolog) 405 44,564 Chain (1); Glycosylation (2); Motif (2); Region (1); Sequence conflict (3); Topological domain (8); Transmembrane (7) TRANSMEM 28 48 Helical; Name=1. {ECO:0000255}.; TRANSMEM 79 99 Helical; Name=2. {ECO:0000255}.; TRANSMEM 125 145 Helical; Name=3. {ECO:0000255}.; TRANSMEM 154 174 Helical; Name=4. {ECO:0000255}.; TRANSMEM 192 212 Helical; Name=5. {ECO:0000255}.; TRANSMEM 249 269 Helical; Name=6. {ECO:0000255}.; TRANSMEM 293 313 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 27 Extracellular. {ECO:0000255}.; TOPO_DOM 49 78 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 100 124 Extracellular. {ECO:0000255}.; TOPO_DOM 146 153 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 175 191 Extracellular. {ECO:0000255}.; TOPO_DOM 213 248 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 270 292 Extracellular. {ECO:0000255}.; TOPO_DOM 314 405 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for tyrosine, L-DOPA and dopamine. After binding to L-DOPA, stimulates Ca(2+) influx into the cytoplasm, increases secretion of the neurotrophic factor SERPINF1 and relocalizes beta arrestin at the plasma membrane; this ligand-dependent signaling occurs through a G(q)-mediated pathway in melanocytic cells. Its activity is mediated by G proteins which activate the phosphoinositide signaling pathway. Plays also a role as an intracellular G protein-coupled receptor involved in melanosome biogenesis, organization and transport. {ECO:0000269|PubMed:18697795}. PTM: Glycosylated. {ECO:0000250}.; PTM: Phosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Melanosome membrane {ECO:0000250|UniProtKB:P51810}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:P51810}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:P51810}; Multi-pass membrane protein {ECO:0000255}. Note=Distributed throughout the endo-melanosomal system but most of endogenous protein is localized in unpigmented stage II melanosomes. Its expression on the apical cell membrane is sensitive to tyrosine. {ECO:0000250|UniProtKB:P51810}. SUBUNIT: Interacts with heterotrimeric G(i) proteins. Interacts with ARRB1 and ARRB2. Interacts with MLANA (By similarity). {ECO:0000250}. DOMAIN: The cytoplasmic domain 3 and the C-terminus tail domain contain the lysosomal sorting signals and are necessary and sufficient for intracellular retention and delivery to lysosomal and melanosomal, respectively in melanocytic and non-melanocytic cells. {ECO:0000250}. +Q99LJ1 FUCO_MOUSE Tissue alpha-L-fucosidase (EC 3.2.1.51) (Alpha-L-fucosidase I) (Alpha-L-fucoside fucohydrolase 1) (Alpha-L-fucosidase 1) 452 52,281 Chain (1); Glycosylation (4); Sequence conflict (2); Signal peptide (1); Site (1) FUNCTION: Alpha-L-fucosidase is responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins. {ECO:0000250}. SUBCELLULAR LOCATION: Lysosome {ECO:0000250}. SUBUNIT: Homotetramer. {ECO:0000250}. +P97807 FUMH_MOUSE Fumarate hydratase, mitochondrial (Fumarase) (EC 4.2.1.2) (EF-3) 507 54,357 Alternative sequence (1); Binding site (1); Chain (1); Initiator methionine (1); Modified residue (21); Region (2); Sequence conflict (2); Transit peptide (1) Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate from fumarate: step 1/1. PTM: Isoform Cytoplasmic is acetylated at position 2. {ECO:0000250}.; PTM: Acetylation of Lys-474 is observed in liver mitochondria from fasted mice but not from fed mice. SUBCELLULAR LOCATION: Isoform Mitochondrial: Mitochondrion.; SUBCELLULAR LOCATION: Isoform Cytoplasmic: Cytoplasm. SUBUNIT: Homotetramer. {ECO:0000250}. +Q9WUU9 GANP_MOUSE Germinal-center associated nuclear protein (GANP) (GC-associated DNA primase) 1971 217,363 Chain (1); Coiled coil (1); Domain (1); Modified residue (7); Mutagenesis (2); Region (2); Sequence conflict (6) FUNCTION: Involved in the nuclear export of poly(A)-containing mRNAs by acting as a scaffold for the TREX-2 complex. The TREX-2 complex functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket). TREX-2 participates in mRNA export and accurate chromatin positioning in the nucleus by tethering genes to the nuclear periphery (By similarity). Essential for the generation of high-affinity B-cells against T-cell-dependent antigens by affecting somatic hypermutation at the IgV-regions. May have stimulation-dependent DNA primase activity that would generate extra RNA primers in very rapidely proliferating cells and would support clonal expansion of differentiating B-cells. {ECO:0000250, ECO:0000269|PubMed:11526238, ECO:0000269|PubMed:21388430}. PTM: Phosphorylation at Ser-502 by CDKs is required for DNA primase activity. {ECO:0000269|PubMed:11526238}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21388430}. Nucleus {ECO:0000269|PubMed:21388430}. Nucleus, nuclear pore complex {ECO:0000250}. Note=In B-cells nuclear import depends on interaction with AICDA/AID, and GANP is selectively targeted to the IgV-region gene. SUBUNIT: Component of the nuclear pore complex (NPC)-associated TREX-2 complex (transcription and export complex 2), composed of at least GANP, two copies of ENY2, PCID2, SEM1, and either centrin CETN2 or CETN3. Interacts with NXF1 (By via FG-repeats) (By similarity). Interacts with MCM3. Interacts with AICDA/AID. {ECO:0000250, ECO:0000269|PubMed:10733502, ECO:0000269|PubMed:21388430}. TISSUE SPECIFICITY: Ubiquitous, up-regulated in B-cells germinal centers during T-cell-dependent immune response. {ECO:0000269|PubMed:10733502, ECO:0000269|PubMed:21388430}. +Q571E4 GALNS_MOUSE N-acetylgalactosamine-6-sulfatase (EC 3.1.6.4) (Chondroitinsulfatase) (Chondroitinase) (Galactose-6-sulfate sulfatase) (N-acetylgalactosamine-6-sulfate sulfatase) (GalNAc6S sulfatase) 520 57,673 Active site (2); Chain (1); Disulfide bond (3); Erroneous initiation (1); Glycosylation (2); Metal binding (5); Modified residue (1); Region (1); Sequence conflict (7); Signal peptide (1) PTM: The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity. {ECO:0000250}. SUBCELLULAR LOCATION: Lysosome {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. Higher expression in liver and kidney. {ECO:0000269|PubMed:10699374}. +Q6PAJ3 GARE2_MOUSE GRB2-associated and regulator of MAPK protein 2 (GRB2-associated and regulator of MAPK1-like) 880 93,510 Alternative sequence (3); Chain (1); Compositional bias (2); Domain (1); Modified residue (1); Region (1) FUNCTION: Probable adapter protein that provides a critical link between cell surface epidermal growth factor receptor and the MAPK/ERK signaling pathway. {ECO:0000250}. +Q61169 GATA6_MOUSE Transcription factor GATA-6 (GATA-binding factor 6) 589 59,307 Alternative sequence (1); Chain (1); Compositional bias (3); Cross-link (3); Frameshift (2); Modified residue (1); Sequence conflict (7); Zinc finger (2) FUNCTION: Transcriptional activator that regulates SEMA3C and PLXNA2 (PubMed:19666519). May regulate genes that protect epithelial cells from bacterial infection (By similarity). Involved in gene regulation specifically in the gastric epithelium (By similarity). Involved in bone morphogenetic protein (BMP)-mediated cardiac-specific gene expression (PubMed:15329343). Binds to BMP response element (BMPRE) DNA sequences within cardiac activating regions (PubMed:15329343). {ECO:0000250|UniProtKB:Q92908, ECO:0000269|PubMed:15329343, ECO:0000269|PubMed:19666519}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16199866}. SUBUNIT: Interacts with LMCD1. {ECO:0000269|PubMed:16199866}. DOMAIN: The GATA-type zinc fingers mediate interaction with LMCD1. {ECO:0000269|PubMed:16199866}. TISSUE SPECIFICITY: Expressed in myocardium, vascular smooth muscle, gut epithelium, and osteoclasts. +Q61017 GBGT2_MOUSE Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-T2 (G gamma-C) (G-gamma-8) 69 7,802 Chain (1); Lipidation (1); Modified residue (1); Propeptide (1) FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. SUBUNIT: G proteins are composed of 3 units, alpha, beta and gamma. +Q8QZW7 GBRP_MOUSE Gamma-aminobutyric acid receptor subunit pi (GABA(A) receptor subunit pi) 440 50,436 Chain (1); Disulfide bond (1); Glycosylation (5); Signal peptide (1); Topological domain (2); Transmembrane (4) TRANSMEM 243 266 Helical. {ECO:0000255}.; TRANSMEM 270 292 Helical. {ECO:0000255}.; TRANSMEM 305 327 Helical. {ECO:0000255}.; TRANSMEM 417 438 Helical. {ECO:0000255}. TOPO_DOM 22 242 Extracellular. {ECO:0000255}.; TOPO_DOM 328 416 Cytoplasmic. {ECO:0000255}. FUNCTION: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel. In the uterus, the function of the receptor appears to be related to tissue contractility. The binding of this pI subunit with other GABA(A) receptor subunits alters the sensitivity of recombinant receptors to modulatory agents such as pregnanolone (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Generally pentameric. There are five types of GABA(A) receptor chains: alpha, beta, gamma, delta, and epsilon. A sixth class of subunit: Rho form homomeric GABA receptors that do not appear to coexist with GABA(A) receptor subunits but with GABA(C) receptor subunits. Subunit Pi can also bind this complex (By similarity). {ECO:0000250}. +P56476 GBRR2_MOUSE Gamma-aminobutyric acid receptor subunit rho-2 (GABA(A) receptor subunit rho-2) (GABA(C) receptor) 465 54,231 Alternative sequence (1); Chain (1); Disulfide bond (1); Glycosylation (2); Sequence conflict (14); Signal peptide (1); Topological domain (2); Transmembrane (4) TRANSMEM 261 281 Helical. {ECO:0000255}.; TRANSMEM 294 314 Helical. {ECO:0000255}.; TRANSMEM 326 346 Helical. {ECO:0000255}.; TRANSMEM 444 464 Helical. {ECO:0000255}. TOPO_DOM 21 260 Extracellular. {ECO:0000305}.; TOPO_DOM 347 443 Cytoplasmic. {ECO:0000305}. FUNCTION: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel. Rho-2 GABA receptor could play a role in retinal neurotransmission (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Generally pentameric. There are five types of GABA(A) receptor chains: alpha, beta, gamma, delta, and rho. Interacts with SQSTM1 (By similarity). {ECO:0000250}. +P62812 GBRA1_MOUSE Gamma-aminobutyric acid receptor subunit alpha-1 (GABA(A) receptor subunit alpha-1) 455 51,754 Chain (1); Disulfide bond (1); Glycosylation (2); Helix (7); Signal peptide (1); Topological domain (2); Transmembrane (4) TRANSMEM 251 272 Helical. {ECO:0000305}.; TRANSMEM 278 299 Helical. {ECO:0000305}.; TRANSMEM 312 333 Helical. {ECO:0000305}.; TRANSMEM 421 442 Helical. {ECO:0000305}. TOPO_DOM 28 250 Extracellular. {ECO:0000305}.; TOPO_DOM 334 420 Cytoplasmic. {ECO:0000305}. FUNCTION: Component of the heteropentameric receptor for GABA, the major inhibitory neurotransmitter in the vertebrate brain. Functions also as histamine receptor and mediates cellular responses to histamine. Functions as receptor for diazepines and various anesthetics, such as pentobarbital; these are bound at a separate allosteric effector binding site. Functions as ligand-gated chloride channel (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane {ECO:0000269|PubMed:16380713, ECO:0000269|PubMed:25579817}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P62813}. SUBUNIT: Heteropentamer, formed by a combination of alpha, beta, gamma, delta and rho chains (By similarity). Interacts with UBQLN1 (By similarity). Interacts with TRAK1 (PubMed:16380713). Interacts with KIF21B (By similarity). Identified in a complex of 720 kDa composed of LHFPL4, NLGN2, GABRA1, GABRB2, GABRG2 and GABRB3 (By similarity). Interacts with LHFPL4 (By similarity). Interacts with NLGN2 (By similarity). {ECO:0000250|UniProtKB:P14867, ECO:0000250|UniProtKB:P62813, ECO:0000269|PubMed:16380713}. +Q60759 GCDH_MOUSE Glutaryl-CoA dehydrogenase, mitochondrial (GCD) (EC 1.3.8.6) 438 48,606 Active site (1); Binding site (8); Chain (1); Modified residue (4); Nucleotide binding (5); Region (2); Sequence conflict (6); Transit peptide (1) Amino-acid metabolism; lysine degradation. Amino-acid metabolism; tryptophan metabolism. FUNCTION: Catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and CO(2) in the degradative pathway of L-lysine, L-hydroxylysine, and L-tryptophan metabolism. It uses electron transfer flavoprotein as its electron acceptor. SUBCELLULAR LOCATION: Mitochondrion matrix. SUBUNIT: Homotetramer. +P63216 GBG3_MOUSE Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-3 75 8,305 Chain (1); Lipidation (1); Modified residue (5); Propeptide (1) FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. SUBUNIT: G proteins are composed of 3 units, alpha, beta and gamma. Interacts with SCN8A. {ECO:0000250|UniProtKB:P63215}. TISSUE SPECIFICITY: Abundantly expressed in brain. Low levels in testis. +P22933 GBRD_MOUSE Gamma-aminobutyric acid receptor subunit delta (GABA(A) receptor subunit delta) 449 50,522 Chain (1); Disulfide bond (1); Glycosylation (2); Modified residue (1); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (4) TRANSMEM 249 271 Helical. {ECO:0000305}.; TRANSMEM 275 297 Helical. {ECO:0000305}.; TRANSMEM 309 331 Helical. {ECO:0000305}.; TRANSMEM 427 449 Helical. {ECO:0000305}. TOPO_DOM 17 248 Extracellular. {ECO:0000305}.; TOPO_DOM 332 426 Cytoplasmic. {ECO:0000305}. FUNCTION: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. SUBUNIT: Generally pentameric. There are five types of GABA(A) receptor subunits: alpha, beta, gamma, delta, and rho. +Q640P4 GL8D2_MOUSE Glycosyltransferase 8 domain-containing protein 2 (EC 2.4.1.-) 349 39,933 Chain (1); Glycosylation (1); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 7 24 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 25 349 Lumenal. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. +Q9ES17 IL21_MOUSE Interleukin-21 (IL-21) 146 16,811 Chain (1); Disulfide bond (2); Glycosylation (1); Signal peptide (1) FUNCTION: Cytokine with immunoregulatory activity. May promote the transition between innate and adaptive immunity. Induces the production of IgG(1) and IgG(3) in B-cells. May play a role in proliferation and maturation of natural killer (NK) cells in synergy with IL15. May regulate proliferation of mature B- and T-cells in response to activating stimuli. In synergy with IL15 and IL18 stimulates interferon gamma production in T-cells and NK cells (By similarity). During T-cell mediated immune response may inhibit dendritic cells (DC) activation and maturation. {ECO:0000250, ECO:0000269|PubMed:11970879, ECO:0000269|PubMed:12893770, ECO:0000269|PubMed:15100251}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11970879}. +Q9JJY8 IL22B_MOUSE Interleukin-22b (IL-22b) (IL-10-related T-cell-derived-inducible factor beta) (IL-TIF beta) (IL-TIFb) 179 20,179 Chain (1); Disulfide bond (2); Glycosylation (3); Sequence conflict (8); Signal peptide (1) FUNCTION: Cytokine that contributes to the inflammatory response in vivo. SUBCELLULAR LOCATION: Secreted. +Q9JJY9 IL22_MOUSE Interleukin-22 (IL-22) (IL-10-related T-cell-derived-inducible factor) (IL-TIF) (IL-TIF alpha) (Interleukin-22a) (IL-22a) 179 20,106 Chain (1); Disulfide bond (2); Glycosylation (3); Signal peptide (1) FUNCTION: Cytokine that contributes to the inflammatory response in vivo. SUBCELLULAR LOCATION: Secreted. +Q9EQ14 IL23A_MOUSE Interleukin-23 subunit alpha (IL-23 subunit alpha) (IL-23-A) (Interleukin-23 subunit p19) (IL-23p19) 196 22,071 Chain (1); Signal peptide (1) FUNCTION: Associates with IL12B to form the IL-23 interleukin, a heterodimeric cytokine which functions in innate and adaptive immunity. IL-23 may constitute with IL-17 an acute response to infection in peripheral tissues. IL-23 binds to a heterodimeric receptor complex composed of IL12RB1 and IL23R, activates the Jak-Stat signaling cascade, stimulates memory rather than naive T-cells and promotes production of proinflammatory cytokines. IL-23 induces autoimmune inflammation and thus may be responsible for autoimmune inflammatory diseases and may be important for tumorigenesis. {ECO:0000269|PubMed:11114383, ECO:0000269|PubMed:11390512, ECO:0000269|PubMed:12610626, ECO:0000269|PubMed:12847224, ECO:0000269|PubMed:14662908, ECO:0000269|PubMed:14978083, ECO:0000269|PubMed:16157683, ECO:0000269|PubMed:16648837, ECO:0000269|PubMed:16670770, ECO:0000269|PubMed:16688182}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11114383}. Note=Secreted upon association with IL12B. SUBUNIT: Heterodimer with IL12B; disulfide-linked. The heterodimer is known as interleukin IL-23. TISSUE SPECIFICITY: Secreted by activated dendritic cells (at protein level). Detected in various tissues with higher expression in polarized Th1 cells and activated macrophages. {ECO:0000269|PubMed:11114383}. +Q925S4 IL24_MOUSE Interleukin-24 (IL-24) (IL-4-induced secreted protein) (Melanoma differentiation-associated gene 7 protein) (MDA-7) (Th2-specific cytokine FISP) 181 20,812 Chain (1); Cross-link (1); Erroneous initiation (1); Glycosylation (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Has antiproliferative properties on melanoma cells and may contribute to terminal cell differentiation. {ECO:0000250}. PTM: Ubiquitination at Lys-97 promotes proteasomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Selectively expressed by Th2 cells. {ECO:0000269|PubMed:11342597}. +Q8K3I6 IL27A_MOUSE Interleukin-27 subunit alpha (IL-27 subunit alpha) (IL-27-A) (IL27-A) (p28) 234 26,542 Chain (1); Compositional bias (1); Glycosylation (1); Signal peptide (1) FUNCTION: Associates with EBI3 to form the IL-27 interleukin, a heterodimeric cytokine which functions in innate immunity. IL-27 has pro- and anti-inflammatory properties, that can regulate T-helper cell development, suppress T-cell proliferation, stimulate cytotoxic T-cell activity, induce isotype switching in B-cells, and that has diverse effects on innate immune cells. Among its target cells are CD4 T-helper cells which can differentiate in type 1 effector cells (TH1), type 2 effector cells (TH2) and IL17 producing helper T-cells (TH17). It drives rapid clonal expansion of naive but not memory CD4 T-cells. It also strongly synergizes with IL-12 to trigger interferon-gamma/IFN-gamma production of naive CD4 T-cells, binds to the cytokine receptor WSX-1/TCCR which appears to be required but not sufficient for IL-27-mediated signal transduction. IL-27 potentiate the early phase of TH1 response and suppress TH2 and TH17 differentiation. It induces the differentiation of TH1 cells via two distinct pathways, p38 MAPK/TBX21- and ICAM1/ITGAL/ERK-dependent pathways. It also induces STAT1, STAT3, STAT4 and STAT5 phosphorylation and activates TBX21/T-Bet via STAT1 with resulting IL12RB2 up-regulation, an event crucial to TH1 cell commitment. It suppresses the expression of GATA3, the inhibitor TH1 cells development. In CD8 T-cells, it activates STATs as well as GZMB. IL-27 reveals to be a potent inhibitor of TH17 cell development and of IL-17 production. Indeed IL27 alone is also able to inhibit the production of IL17 by CD4 and CD8 T-cells. While IL-27 suppressed the development of proinflammatory Th17 cells via STAT1, it inhibits the development of anti-inflammatory inducible regulatory T-cells, iTreg, independently of STAT1. IL-27 has also an effect on cytokine production, it suppresses proinflammatory cytokine production such as IL2, IL4, IL5 and IL6 and activates suppressors of cytokine signaling such as SOCS1 and SOCS3. Apart from suppression of cytokine production, IL-27 also antagonizes the effects of some cytokines such as IL6 through direct effects on T-cells. Another important role of IL-27 is its antitumor activity as well as its antiangiogenic activity with activation of production of antiangiogenic chemokines such as IP-10/CXCL10 and MIG/CXCL9. {ECO:0000269|PubMed:12121660, ECO:0000269|PubMed:14565860, ECO:0000269|PubMed:14657353, ECO:0000269|PubMed:14871851, ECO:0000269|PubMed:15585838, ECO:0000269|PubMed:15688376, ECO:0000269|PubMed:16034109, ECO:0000269|PubMed:16365415, ECO:0000269|PubMed:16493033, ECO:0000269|PubMed:16751375, ECO:0000269|PubMed:16906166, ECO:0000269|PubMed:16906167, ECO:0000269|PubMed:17015723, ECO:0000269|PubMed:17114427, ECO:0000269|PubMed:17549733}. PTM: O-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12121660}. Note=Poorly secreted without coexpression of EBI3. SUBUNIT: Heterodimer with EBI3; not disulfide-linked. This heterodimer is known as interleukin IL-27. {ECO:0000269|PubMed:12121660}. TISSUE SPECIFICITY: Expressed in macrophages and dendritic cells. {ECO:0000269|PubMed:12121660}. +Q64516 GLPK_MOUSE Glycerol kinase (GK) (Glycerokinase) (EC 2.7.1.30) (ATP:glycerol 3-phosphotransferase) 559 61,227 Alternative sequence (2); Binding site (7); Chain (1); Nucleotide binding (1); Sequence conflict (1) Polyol metabolism; glycerol degradation via glycerol kinase pathway; sn-glycerol 3-phosphate from glycerol: step 1/1. FUNCTION: Key enzyme in the regulation of glycerol uptake and metabolism. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Bound to the mitochondrial surface or cytoplasmic. {ECO:0000250}. +P04351 IL2_MOUSE Interleukin-2 (IL-2) (T-cell growth factor) (TCGF) 169 19,400 Beta strand (3); Chain (1); Compositional bias (1); Disulfide bond (1); Glycosylation (1); Helix (7); Natural variant (4); Sequence conflict (1); Signal peptide (1) FUNCTION: Produced by T-cells in response to antigenic or mitogenic stimulation, this protein is required for T-cell proliferation and other activities crucial to regulation of the immune response. Can stimulate B-cells, monocytes, lymphokine-activated killer cells, natural killer cells, and glioma cells. SUBCELLULAR LOCATION: Secreted. +Q61603 GLRA4_MOUSE Glycine receptor subunit alpha-4 456 52,514 Chain (1); Disulfide bond (2); Glycosylation (1); Region (1); Sequence conflict (2); Signal peptide (1); Site (1); Topological domain (5); Transmembrane (4) TRANSMEM 257 278 Helical; Name=1. {ECO:0000250|UniProtKB:P23415}.; TRANSMEM 284 304 Helical; Name=2. {ECO:0000250|UniProtKB:P23415}.; TRANSMEM 316 336 Helical; Name=3. {ECO:0000250|UniProtKB:P23415}.; TRANSMEM 424 444 Helical; Name=4. {ECO:0000250|UniProtKB:P23415}. TOPO_DOM 28 256 Extracellular. {ECO:0000250|UniProtKB:P23415}.; TOPO_DOM 279 283 Cytoplasmic. {ECO:0000250|UniProtKB:P23415}.; TOPO_DOM 305 315 Extracellular. {ECO:0000250|UniProtKB:P23415}.; TOPO_DOM 337 423 Cytoplasmic. {ECO:0000250|UniProtKB:P23415}.; TOPO_DOM 445 456 Extracellular. {ECO:0000250|UniProtKB:P23415}. FUNCTION: Glycine receptors are ligand-gated chloride channels. Channel opening is triggered by extracellular glycine. Channel opening is also triggered by taurine and beta-alanine (PubMed:10762330). Plays a role in the down-regulation of neuronal excitability. Contributes to the generation of inhibitory postsynaptic currents (Probable). {ECO:0000269|PubMed:10762330, ECO:0000305}. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane {ECO:0000305|PubMed:17154252}; Multi-pass membrane protein {ECO:0000305}. Cell junction, synapse {ECO:0000269|PubMed:17154252, ECO:0000269|PubMed:22592841}. Perikaryon {ECO:0000269|PubMed:17154252}. Cell projection, dendrite {ECO:0000269|PubMed:17154252}. Cell membrane {ECO:0000269|PubMed:10762330, ECO:0000269|PubMed:22592841, ECO:0000305|PubMed:17154252}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Homopentamer (in vitro). Heteropentamer composed of GLRA4 and GLRB. {ECO:0000305}. TISSUE SPECIFICITY: Detected in the retina inner plexiform layer, especially at the border between layer three and four (at protein level) (PubMed:17154252). {ECO:0000269|PubMed:17154252, ECO:0000269|PubMed:22592841}. +P22272 IL6RA_MOUSE Interleukin-6 receptor subunit alpha (IL-6 receptor subunit alpha) (IL-6R subunit alpha) (IL-6R-alpha) (IL-6RA) (IL-6R 1) (CD antigen CD126) 460 50,455 Chain (1); Compositional bias (1); Disulfide bond (4); Domain (3); Glycosylation (3); Motif (1); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 365 385 Helical. {ECO:0000255}. TOPO_DOM 20 364 Extracellular. {ECO:0000255}.; TOPO_DOM 386 460 Cytoplasmic. {ECO:0000255}. FUNCTION: Part of the receptor for interleukin 6. Binds to IL6 with low affinity, but does not transduce a signal. Signal activation necessitate an association with IL6ST. Activation may lead to the regulation of the immune response, acute-phase reactions and hematopoiesis. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Hexamer of two molecules each of IL6, IL6R and IL6ST. {ECO:0000250}. DOMAIN: The two fibronectin type-III-like domains contained in the C-terminal part form together a cytokine-binding domain.; DOMAIN: The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding. +Q00560 IL6RB_MOUSE Interleukin-6 receptor subunit beta (IL-6 receptor subunit beta) (IL-6R subunit beta) (IL-6R-beta) (IL-6RB) (Interleukin-6 signal transducer) (Membrane glycoprotein 130) (gp130) (Oncostatin-M receptor subunit alpha) (CD antigen CD130) 917 102,451 Chain (1); Compositional bias (1); Disulfide bond (5); Domain (6); Glycosylation (9); Modified residue (6); Motif (2); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 618 639 Helical. {ECO:0000255}. TOPO_DOM 23 617 Extracellular. {ECO:0000255}.; TOPO_DOM 640 917 Cytoplasmic. {ECO:0000255}. FUNCTION: Signal-transducing molecule. The receptor systems for IL6, LIF, OSM, CNTF, IL11, CTF1 and BSF3 can utilize IL6ST for initiating signal transmission. Binding of IL6 to IL6R induces IL6ST homodimerization and formation of a high-affinity receptor complex, which activates Janus kinases (PubMed:1602143). That causes phosphorylation of IL6ST tyrosine residues which in turn activates STAT3 (PubMed:10661409). Mediates signals which regulate immune response, hematopoiesis, pain control and bone metabolism (PubMed:10661409, PubMed:26255596, PubMed:25057188, PubMed:8552649). Has a role in embryonic development (PubMed:10661409). Does not bind IL6 (By similarity). Essential for survival of motor and sensory neurons and for differentiation of astrocytes (PubMed:10377352). Required for expression of TRPA1 in nociceptive neurons (PubMed:25057188). Required for the maintenance of PTH1R expression in the osteoblast lineage and for the stimulation of PTH-induced osteoblast differentiation (PubMed:25228504). Required for normal trabecular bone mass and cortical bone composition (PubMed:24339143, PubMed:9348227, PubMed:26255596). {ECO:0000250|UniProtKB:P40189, ECO:0000269|PubMed:10377352, ECO:0000269|PubMed:10661409, ECO:0000269|PubMed:1602143, ECO:0000269|PubMed:24339143, ECO:0000269|PubMed:25057188, ECO:0000269|PubMed:25228504, ECO:0000269|PubMed:26255596, ECO:0000269|PubMed:8552649, ECO:0000269|PubMed:9348227}. PTM: Phosphorylation of Ser-780 down-regulates cell surface expression. {ECO:0000250|UniProtKB:P40189}.; PTM: Heavily N-glycosylated. Glycosylation is required for protein stability and localization in plasma membrane but not for ligand binding. {ECO:0000250|UniProtKB:P40189}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P40189}; Single-pass type I membrane protein {ECO:0000255}. SUBUNIT: Component of a hexamer of two molecules each of IL6, IL6R and IL6ST. Forms heterodimers composed of LIFR and IL6ST (type I OSM receptor) which are activated by LIF and OSM. Also forms heterodimers composed of OSMR and IL6ST (type II receptor) which are activated by OSM but not by LIF. Interacts with HCK (By similarity). Interacts with INPP5D/SHIP1 (PubMed:17105399). {ECO:0000250|UniProtKB:P40189, ECO:0000269|PubMed:17105399, ECO:0000269|PubMed:9920829}. DOMAIN: The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.; DOMAIN: The box 1 motif is required for JAK interaction and/or activation. TISSUE SPECIFICITY: Found in tissues such as brain, heart, thymus, spleen, kidney, lung and liver. Found in all the cell lines tested except BaF-B03. Expression not restricted to IL6-responsive cells. {ECO:0000269|PubMed:1602143}. +P08505 IL6_MOUSE Interleukin-6 (IL-6) (B-cell hybridoma growth factor) (Interleukin HP-1) 211 24,384 Beta strand (1); Chain (1); Disulfide bond (2); Helix (7); Signal peptide (1); Turn (2) FUNCTION: Cytokine with a wide variety of biological functions. It is a potent inducer of the acute phase response. Plays an essential role in the final differentiation of B-cells into Ig-secreting cells Involved in lymphocyte and monocyte differentiation. Acts on B-cells, T-cells, hepatocytes, hematopoietic progenitor cells and cells of the CNS. Required for the generation of T(H)17 cells. Also acts as a myokine. It is discharged into the bloodstream after muscle contraction and acts to increase the breakdown of fats and to improve insulin resistance. It induces myeloma and plasmacytoma growth and induces nerve cells differentiation. {ECO:0000269|PubMed:16990136}. SUBCELLULAR LOCATION: Secreted. +P10168 IL7_MOUSE Interleukin-7 (IL-7) 154 17,727 Chain (1); Disulfide bond (3); Glycosylation (2); Signal peptide (1) FUNCTION: Hematopoietic growth factor capable of stimulating the proliferation of lymphoid progenitors. It is important for proliferation during certain stages of B-cell maturation. PTM: Three disulfide bonds are present. {ECO:0000305}. SUBCELLULAR LOCATION: Secreted. +Q01114 IL9R_MOUSE Interleukin-9 receptor (IL-9 receptor) (IL-9R) (CD antigen CD129) 468 52,261 Chain (1); Compositional bias (2); Domain (1); Glycosylation (2); Motif (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 271 291 Helical. {ECO:0000255}. TOPO_DOM 38 270 Extracellular. {ECO:0000255}.; TOPO_DOM 292 468 Cytoplasmic. {ECO:0000255}. FUNCTION: This is a receptor for interleukin-9. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Secreted. DOMAIN: The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.; DOMAIN: The box 1 motif is required for JAK interaction and/or activation. +Q8CBR1 ILDR1_MOUSE Immunoglobulin-like domain-containing receptor 1 537 61,277 Alternative sequence (3); Chain (1); Compositional bias (2); Disulfide bond (1); Domain (1); Modified residue (2); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 167 187 Helical. {ECO:0000255}. TOPO_DOM 23 166 Extracellular. {ECO:0000255}.; TOPO_DOM 188 537 Cytoplasmic. {ECO:0000255}. FUNCTION: Putative membrane receptor. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q86SU0}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q86SU0}. SUBUNIT: Homooligomer. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the vestibule and in hair cells and supporting cells of the cochlea. {ECO:0000269|PubMed:21255762}. +Q99LE2 GP146_MOUSE Probable G-protein coupled receptor 146 333 36,572 Chain (1); Compositional bias (1); Glycosylation (1); Sequence conflict (4); Topological domain (8); Transmembrane (7) TRANSMEM 23 43 Helical; Name=1. {ECO:0000255}.; TRANSMEM 65 85 Helical; Name=2. {ECO:0000255}.; TRANSMEM 102 122 Helical; Name=3. {ECO:0000255}.; TRANSMEM 146 166 Helical; Name=4. {ECO:0000255}.; TRANSMEM 189 209 Helical; Name=5. {ECO:0000255}.; TRANSMEM 233 253 Helical; Name=6. {ECO:0000255}.; TRANSMEM 278 298 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 22 Extracellular. {ECO:0000255}.; TOPO_DOM 44 64 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 86 101 Extracellular. {ECO:0000255}.; TOPO_DOM 123 145 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 167 188 Extracellular. {ECO:0000255}.; TOPO_DOM 210 232 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 254 277 Extracellular. {ECO:0000255}.; TOPO_DOM 299 333 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q9CR60 GOT1B_MOUSE Vesicle transport protein GOT1B (Golgi transport 1 homolog B) 138 15,422 Chain (1); Compositional bias (1); Erroneous initiation (1); Modified residue (1); Topological domain (5); Transmembrane (3) TRANSMEM 10 30 Helical; Name=1. {ECO:0000255}.; TRANSMEM 33 53 Helical; Name=2. {ECO:0000255}.; TRANSMEM 91 109 Helical; Name=4. {ECO:0000255}. TOPO_DOM 1 9 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 31 32 Lumenal. {ECO:0000255}.; TOPO_DOM 54 68 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 90 90 Lumenal. {ECO:0000255}.; TOPO_DOM 110 138 Cytoplasmic. {ECO:0000255}. FUNCTION: May be involved in fusion of ER-derived transport vesicles with the Golgi complex. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q8BL07 GP150_MOUSE Probable G-protein coupled receptor 150 (G-protein coupled receptor PGR11) 427 46,519 Chain (1); Compositional bias (1); Topological domain (8); Transmembrane (7) TRANSMEM 4 24 Helical; Name=1. {ECO:0000255}.; TRANSMEM 51 71 Helical; Name=2. {ECO:0000255}.; TRANSMEM 90 110 Helical; Name=3. {ECO:0000255}.; TRANSMEM 171 191 Helical; Name=4. {ECO:0000255}.; TRANSMEM 231 251 Helical; Name=5. {ECO:0000255}.; TRANSMEM 287 307 Helical; Name=6. {ECO:0000255}.; TRANSMEM 328 348 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 3 Extracellular. {ECO:0000255}.; TOPO_DOM 25 50 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 72 89 Extracellular. {ECO:0000255}.; TOPO_DOM 111 170 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 192 230 Extracellular. {ECO:0000255}.; TOPO_DOM 252 286 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 308 327 Extracellular. {ECO:0000255}.; TOPO_DOM 349 427 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q8BXS7 GP152_MOUSE Probable G-protein coupled receptor 152 511 55,420 Chain (1); Disulfide bond (1); Topological domain (8); Transmembrane (7) TRANSMEM 34 54 Helical; Name=1. {ECO:0000255}.; TRANSMEM 66 86 Helical; Name=2. {ECO:0000255}.; TRANSMEM 106 126 Helical; Name=3. {ECO:0000255}.; TRANSMEM 149 169 Helical; Name=4. {ECO:0000255}.; TRANSMEM 195 215 Helical; Name=5. {ECO:0000255}.; TRANSMEM 259 279 Helical; Name=6. {ECO:0000255}.; TRANSMEM 283 303 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 33 Extracellular. {ECO:0000255}.; TOPO_DOM 55 65 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 87 105 Extracellular. {ECO:0000255}.; TOPO_DOM 127 148 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 170 194 Extracellular. {ECO:0000255}.; TOPO_DOM 216 258 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 280 282 Extracellular. {ECO:0000255}.; TOPO_DOM 304 511 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q8BUV8 GP107_MOUSE Protein GPR107 551 62,056 Chain (1); Disulfide bond (1); Glycosylation (2); Modified residue (1); Sequence conflict (4); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 263 283 Helical; Name=1. {ECO:0000255}.; TRANSMEM 293 313 Helical; Name=2. {ECO:0000255}.; TRANSMEM 337 357 Helical; Name=3. {ECO:0000255}.; TRANSMEM 368 388 Helical; Name=4. {ECO:0000255}.; TRANSMEM 402 422 Helical; Name=5. {ECO:0000255}.; TRANSMEM 450 470 Helical; Name=6. {ECO:0000255}.; TRANSMEM 476 495 Helical; Name=7. {ECO:0000255}. TOPO_DOM 40 262 Lumenal. {ECO:0000255}.; TOPO_DOM 284 292 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 314 336 Lumenal. {ECO:0000255}.; TOPO_DOM 358 367 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 389 401 Lumenal. {ECO:0000255}.; TOPO_DOM 423 449 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 471 475 Lumenal. {ECO:0000255}.; TOPO_DOM 496 551 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in Golgi-to-ER retrograde transport. {ECO:0000250|UniProtKB:Q5VW38}. PTM: Cleaved by a furin endopeptidase to yield two fragments that remain associated via a disulfide bond. {ECO:0000250|UniProtKB:Q5VW38}. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q5VW38}; Multi-pass membrane protein {ECO:0000255}. +Q91WD0 GP108_MOUSE Protein GPR108 (Lung seven transmembrane receptor 2) 569 63,981 Alternative sequence (1); Chain (1); Glycosylation (5); Sequence conflict (3); Signal peptide (1); Transmembrane (7) TRANSMEM 289 309 Helical; Name=1. {ECO:0000255}.; TRANSMEM 318 338 Helical; Name=2. {ECO:0000255}.; TRANSMEM 362 382 Helical; Name=3. {ECO:0000255}.; TRANSMEM 393 413 Helical; Name=4. {ECO:0000255}.; TRANSMEM 427 447 Helical; Name=5. {ECO:0000255}.; TRANSMEM 475 495 Helical; Name=6. {ECO:0000255}.; TRANSMEM 499 519 Helical; Name=7. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q7TQP3 GP119_MOUSE Glucose-dependent insulinotropic receptor (G-protein coupled receptor 119) 335 36,995 Chain (1); Compositional bias (1); Topological domain (8); Transmembrane (7) TRANSMEM 7 27 Helical; Name=1. {ECO:0000255}.; TRANSMEM 38 58 Helical; Name=2. {ECO:0000255}.; TRANSMEM 82 102 Helical; Name=3. {ECO:0000255}.; TRANSMEM 126 146 Helical; Name=4. {ECO:0000255}.; TRANSMEM 165 185 Helical; Name=5. {ECO:0000255}.; TRANSMEM 227 247 Helical; Name=6. {ECO:0000255}.; TRANSMEM 263 283 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 6 Extracellular. {ECO:0000255}.; TOPO_DOM 28 37 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 59 81 Extracellular. {ECO:0000255}.; TOPO_DOM 103 125 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 147 164 Extracellular. {ECO:0000255}.; TOPO_DOM 186 226 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 248 262 Extracellular. {ECO:0000255}.; TOPO_DOM 284 335 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for the endogenous fatty-acid ethanolamide oleoylethanolamide (OEA) and lysophosphatidylcholine (LPC). Functions as a glucose-dependent insulinotropic receptor. The activity of this receptor is mediated by G proteins which activate adenylate cyclase. Seems to act through a G(s) mediated pathway. {ECO:0000269|PubMed:17289847}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expression restricted to the beta-cells of pancreatic islets. {ECO:0000269|PubMed:17070774, ECO:0000269|PubMed:17289847}. +Q9EQQ3 GPR63_MOUSE Probable G-protein coupled receptor 63 (PSP24-2) (PSP24-beta) 425 47,788 Chain (1); Glycosylation (3); Sequence conflict (1); Topological domain (8); Transmembrane (7) TRANSMEM 88 112 Helical; Name=1. {ECO:0000255}.; TRANSMEM 124 148 Helical; Name=2. {ECO:0000255}.; TRANSMEM 166 190 Helical; Name=3. {ECO:0000255}.; TRANSMEM 203 222 Helical; Name=4. {ECO:0000255}.; TRANSMEM 248 272 Helical; Name=5. {ECO:0000255}.; TRANSMEM 322 345 Helical; Name=6. {ECO:0000255}.; TRANSMEM 358 379 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 87 Extracellular. {ECO:0000255}.; TOPO_DOM 113 123 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 149 165 Extracellular. {ECO:0000255}.; TOPO_DOM 191 202 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 223 247 Extracellular. {ECO:0000255}.; TOPO_DOM 273 321 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 346 357 Extracellular. {ECO:0000255}.; TOPO_DOM 380 425 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan receptor. May play a role in brain function. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Brain specific. +Q03526 ITK_MOUSE Tyrosine-protein kinase ITK/TSK (EC 2.7.10.2) (IL-2-inducible T-cell kinase) (Kinase EMT) (Kinase TLK) (T-cell-specific kinase) 625 72,292 Active site (1); Beta strand (21); Binding site (1); Chain (1); Domain (4); Helix (3); Metal binding (4); Modified residue (3); Nucleotide binding (1); Sequence conflict (5); Turn (1); Zinc finger (1) FUNCTION: Tyrosine kinase that plays an essential role in regulation of the adaptive immune response. Regulates the development, function and differentiation of conventional T-cells and nonconventional NKT-cells. When antigen presenting cells (APC) activate T-cell receptor (TCR), a series of phosphorylation lead to the recruitment of ITK to the cell membrane, in the vicinity of the stimulated TCR receptor, where it is phosphorylated by LCK. Phosphorylation leads to ITK autophosphorylation and full activation. Once activated, phosphorylates PLCG1, leading to the activation of this lipase and subsequent cleavage of its substrates. In turn, the endoplasmic reticulum releases calcium in the cytoplasm and the nuclear activator of activated T-cells (NFAT) translocates into the nucleus to perform its transcriptional duty. Phosphorylates 2 essential adapter proteins: the linker for activation of T-cells/LAT protein and LCP2. Then, a large number of signaling molecules such as VAV1 are recruited and ultimately lead to lymphokine production, T-cell proliferation and differentiation. Phosphorylates TBX21 at 'Tyr-525' and mediates its interaction with GATA3 (PubMed:15662016). {ECO:0000269|PubMed:15662016, ECO:0000269|PubMed:21036902}. PTM: Phosphorylated at Tyr-517 in the activation loop of the kinase domain by LCK. Subsequent autophosphorylation at Tyr-186 leads to the kinase activation. The autophosphorylated Tyr-186 lies within the substrate binding sequence of the SH3 domain (By similarity). {ECO:0000250}.; PTM: Ubiquitinated. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000269|PubMed:15662016}. Note=Localizes in the vicinity of cell surface receptors in the plasma membrane after receptor stimulation. {ECO:0000250}. SUBUNIT: Homooligomerizes; this association negatively regulates kinase activity. Interacts with PPIA/CYPA; this interaction regulates TCR signal strength via a proline-directed conformational switch in ITK. Interacts with THEMIS (By similarity). Interacts with FASLG. Interacts with VAV1; this interaction is important for VAV1 localization and TCR-induced actin polarization. Interacts with TBX21 (PubMed:15662016). {ECO:0000250|UniProtKB:Q08881, ECO:0000269|PubMed:15662016, ECO:0000269|PubMed:19597499, ECO:0000269|PubMed:20237289}. DOMAIN: The N-terminal PH domain allows ITK to be recruited to the plasma membrane by an activated PI3 kinase. This domain contains also a proline-rich region (PRR). The adjoining domain is a SH3 domain, which binds to PRR (from itself or from other proteins). Next, a SH2 domain is required for binding tyrosine-phosphorylated substrates. In the C-terminal region, the kinase domain is required for tyrosine phosphorylation (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Is detected in the thymus, lymph node and very faintly in the spleen, but is not detected in the liver, lung, kidney, heart, brain, intestine or testis. Expressed in T-lymphocytes and mast cells. It may also be expressed in natural killer cells. +Q99LJ6 GPX7_MOUSE Glutathione peroxidase 7 (GPx-7) (GSHPx-7) (EC 1.11.1.9) 186 21,061 Active site (1); Chain (1); Signal peptide (1) FUNCTION: It protects esophageal epithelia from hydrogen peroxide-induced oxidative stress. It suppresses acidic bile acid-induced reactive oxigen species (ROS) and protects against oxidative DNA damage and double-strand breaks (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q8CIM5 GPR84_MOUSE G-protein coupled receptor 84 396 43,717 Chain (1); Glycosylation (2); Modified residue (2); Sequence conflict (1); Topological domain (8); Transmembrane (7) TRANSMEM 22 42 Helical; Name=1. {ECO:0000255}.; TRANSMEM 58 78 Helical; Name=2. {ECO:0000255}.; TRANSMEM 95 115 Helical; Name=3. {ECO:0000255}.; TRANSMEM 136 156 Helical; Name=4. {ECO:0000255}.; TRANSMEM 181 201 Helical; Name=5. {ECO:0000255}.; TRANSMEM 321 341 Helical; Name=6. {ECO:0000255}.; TRANSMEM 353 373 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 21 Extracellular. {ECO:0000255}.; TOPO_DOM 43 57 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 79 94 Extracellular. {ECO:0000255}.; TOPO_DOM 116 135 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 157 180 Extracellular. {ECO:0000255}.; TOPO_DOM 202 320 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 342 352 Extracellular. {ECO:0000255}.; TOPO_DOM 374 396 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for medium-chain free fatty acid (FFA) with carbon chain lengths of C9 to C14. Capric acid (C10:0), undecanoic acid (C11:0) and lauric acid (C12:0) are the most potent agonists. Not activated by short-chain and long-chain saturated and unsaturated FFAs. Activation by medium-chain free fatty acid is coupled to a pertussis toxin sensitive G(i/o) protein pathway. May have important roles in processes from fatty acid metabolism to regulation of the immune system (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed predominantly in hematopoietic tissues. Expressed mainly in the bone marrow with transcripts also detected in spleen, the lymph node, liver and the lung. {ECO:0000269|PubMed:11273702, ECO:0000269|PubMed:16966319}. +P0C191 GPVI_MOUSE Platelet glycoprotein VI (GPVI) (Glycoprotein 5) 313 34,595 Chain (1); Compositional bias (1); Disulfide bond (2); Domain (2); Glycosylation (2); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 266 286 Helical. {ECO:0000255}. TOPO_DOM 22 265 Extracellular. {ECO:0000255}.; TOPO_DOM 287 313 Cytoplasmic. {ECO:0000255}. FUNCTION: Collagen receptor involved in collagen-induced platelet adhesion and activation (PubMed:16139873, PubMed:24368846). Plays a key role in platelet procoagulant activity and subsequent thrombin and fibrin formation. This procoagulant function may contribute to arterial and venous thrombus formation. The signaling pathway involves the FcR gamma-chain, the Src kinases (likely FYN or LYN) and SYK, the adapter protein LAT and leads to the activation of PLCG2. {ECO:0000269|PubMed:10961879, ECO:0000269|PubMed:16139873, ECO:0000269|PubMed:16254207, ECO:0000269|PubMed:24368846}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:24368846}; Single-pass membrane protein {ECO:0000255}. SUBUNIT: Associated with Fc receptor gamma chain. The GPVI:FcRgamma complex is associated with the Src kinase family FYN and LYN (By similarity). Interacts with COL1A1, but not with COL4A4 (PubMed:24368846). {ECO:0000250|UniProtKB:Q9HCN6, ECO:0000269|PubMed:24368846}. TISSUE SPECIFICITY: Megakaryocytes and platelets. {ECO:0000269|PubMed:10961879}. +Q8BLX4 FUCT1_MOUSE GDP-fucose transporter 1 (Solute carrier family 35 member C1) 363 39,967 Chain (1); Sequence conflict (2); Transmembrane (8) TRANSMEM 33 55 Helical. {ECO:0000255}.; TRANSMEM 75 97 Helical. {ECO:0000255}.; TRANSMEM 110 129 Helical. {ECO:0000255}.; TRANSMEM 139 161 Helical. {ECO:0000255}.; TRANSMEM 166 184 Helical. {ECO:0000255}.; TRANSMEM 194 213 Helical. {ECO:0000255}.; TRANSMEM 226 248 Helical. {ECO:0000255}.; TRANSMEM 263 285 Helical. {ECO:0000255}. FUNCTION: Involved in GDP-fucose import from the cytoplasm into the Golgi lumen. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q3UY90 GAK1A_MOUSE Golgi-associated kinase 1A (Protein FAM198A) 562 62,298 Alternative sequence (2); Chain (1); Propeptide (2); Sequence conflict (1); Signal peptide (1); Site (2) PTM: Proteolytically cleaved. Cleaved at Arg-112 and Arg-424 leading to a processed mature product of 35 kDa. The cleavage takes place in the Golgi apparatus. {ECO:0000269|PubMed:30188967}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30188967}. Endoplasmic reticulum {ECO:0000269|PubMed:30188967}. Golgi apparatus {ECO:0000269|PubMed:30188967}. Membrane, caveola {ECO:0000269|PubMed:30188967}. Note=Requires caveolae biogenesis to be secreted from the endoplasmic reticulum going through the Golgi apparatus where is post-translationally processed to the mature form. {ECO:0000269|PubMed:30188967}. TISSUE SPECIFICITY: Expressed in tracheal serous gland, heart, muscle, fat, lung, ovary, liver, kidney, adrenal gland and brain (at protein level). {ECO:0000269|PubMed:30188967}. +Q80T41 GABR2_MOUSE Gamma-aminobutyric acid type B receptor subunit 2 (GABA-B receptor 2) (GABA-B-R2) (GABA-BR2) (GABABR2) (Gb2) (G-protein coupled receptor 51) 940 105,666 Chain (1); Coiled coil (1); Compositional bias (1); Disulfide bond (3); Glycosylation (5); Modified residue (9); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 483 503 Helical; Name=1. {ECO:0000255}.; TRANSMEM 522 542 Helical; Name=2. {ECO:0000255}.; TRANSMEM 551 571 Helical; Name=3. {ECO:0000255}.; TRANSMEM 597 617 Helical; Name=4. {ECO:0000255}.; TRANSMEM 654 674 Helical; Name=5. {ECO:0000255}.; TRANSMEM 691 711 Helical; Name=6. {ECO:0000255}.; TRANSMEM 720 740 Helical; Name=7. {ECO:0000255}. TOPO_DOM 41 482 Extracellular. {ECO:0000255}.; TOPO_DOM 504 521 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 543 550 Extracellular. {ECO:0000255}.; TOPO_DOM 572 596 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 618 653 Extracellular. {ECO:0000255}.; TOPO_DOM 675 690 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 712 719 Extracellular. {ECO:0000255}.; TOPO_DOM 741 940 Cytoplasmic. {ECO:0000255}. FUNCTION: Component of a heterodimeric G-protein coupled receptor for GABA, formed by GABBR1 and GABBR2 (PubMed:10075644). Within the heterodimeric GABA receptor, only GABBR1 seems to bind agonists, while GABBR2 mediates coupling to G proteins (By similarity). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase (PubMed:10075644). Signaling inhibits adenylate cyclase, stimulates phospholipase A2, activates potassium channels, inactivates voltage-dependent calcium-channels and modulates inositol phospholipid hydrolysis (PubMed:10075644). Plays a critical role in the fine-tuning of inhibitory synaptic transmission (By similarity). Pre-synaptic GABA receptor inhibits neurotransmitter release by down-regulating high-voltage activated calcium channels, whereas postsynaptic GABA receptor decreases neuronal excitability by activating a prominent inwardly rectifying potassium (Kir) conductance that underlies the late inhibitory postsynaptic potentials (PubMed:10075644). Not only implicated in synaptic inhibition but also in hippocampal long-term potentiation, slow wave sleep, muscle relaxation and antinociception (By similarity). {ECO:0000250|UniProtKB:O75899, ECO:0000269|PubMed:10075644}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Coexpression of GABBR1 and GABBR2 is required for GABBR1 maturation and transport to the plasma membrane. In contrast, GABBR2 does not depend on GABBR1 for transport to the cell membrane (By similarity). {ECO:0000250}. SUBUNIT: Heterodimer of GABBR1 and GABBR2 (PubMed:10075644). Homodimers may form, but are inactive (By similarity). Interacts (via C-terminus) with ATF4 (via leucine zipper domain) (By similarity). {ECO:0000250|UniProtKB:O88871, ECO:0000269|PubMed:10075644}. DOMAIN: Alpha-helical parts of the C-terminal intracellular region mediate heterodimeric interaction with GABBR1. {ECO:0000250}. +Q3UPI1 GAK1B_MOUSE Golgi-associated kinase 1B (Expressed in nerve and epithelium during development) (Protein FAM198B) 517 58,298 Chain (1); Erroneous initiation (1); Glycosylation (2); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 37 56 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 36 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 57 517 Extracellular. {ECO:0000255}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q6UWH4}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q6UWH4}. TISSUE SPECIFICITY: At E9.5, detected in heart and midgut. At later gestation stages, expressed in floor plate, peripheral nervous system, lens epithelium, skin, midline dorsal aorta, lung, kidney and testis. {ECO:0000269|PubMed:18956345}. +P47212 GALA_MOUSE Galanin peptides [Cleaved into: Galanin; Galanin message-associated peptide (GMAP)] 124 13,471 Modified residue (3); Peptide (2); Propeptide (1); Signal peptide (1) FUNCTION: Endocrine hormone of the central and peripheral nervous systems that binds and activates the G protein-coupled receptors GALR1, GALR2, and GALR3. This small neuropeptide may regulate diverse physiologic functions including contraction of smooth muscle of the gastrointestinal and genitourinary tract, growth hormone and insulin release and adrenal secretion. {ECO:0000250|UniProtKB:P07480, ECO:0000250|UniProtKB:P22466}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P07480, ECO:0000250|UniProtKB:P22466}. +P63137 GBRB2_MOUSE Gamma-aminobutyric acid receptor subunit beta-2 (GABA(A) receptor subunit beta-2) 512 59,197 Alternative sequence (1); Binding site (1); Chain (1); Disulfide bond (1); Glycosylation (3); Modified residue (1); Region (3); Signal peptide (1); Topological domain (2); Transmembrane (4) TRANSMEM 245 266 Helical. {ECO:0000305}.; TRANSMEM 270 292 Helical. {ECO:0000305}.; TRANSMEM 304 326 Helical. {ECO:0000305}.; TRANSMEM 490 511 Helical. {ECO:0000305}. TOPO_DOM 26 244 Extracellular. {ECO:0000305}.; TOPO_DOM 327 489 Cytoplasmic. {ECO:0000305}. FUNCTION: Component of the heteropentameric receptor for GABA, the major inhibitory neurotransmitter in the vertebrate brain. Functions also as histamine receptor and mediates cellular responses to histamine. Functions as receptor for diazepines and various anesthetics, such as pentobarbital; these are bound at a separate allosteric effector binding site. Functions as ligand-gated chloride channel. {ECO:0000269|PubMed:20400944}. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane {ECO:0000269|PubMed:20400944}; Multi-pass membrane protein {ECO:0000269|PubMed:20400944}. Cell membrane {ECO:0000269|PubMed:20400944}; Multi-pass membrane protein {ECO:0000269|PubMed:20400944}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:P63138}. SUBUNIT: Heteropentamer, formed by a combination of alpha, beta, gamma, delta and rho chains. Interacts with UBQLN1 (By similarity). Interacts with KCTD8, KCTD12 and KCTD16; this interaction determines the pharmacology and kinetics of the receptor response, the KCTD proteins markedly accelerating the GABA-B response, although to different extents (PubMed:20400944). May interact with KIF21B (By similarity). Identified in a complex of 720 kDa composed of LHFPL4, NLGN2, GABRA1, GABRB2, GABRG2 and GABRB3 (By similarity). {ECO:0000250|UniProtKB:P63138, ECO:0000269|PubMed:20400944}. +Q8R0H9 GGA1_MOUSE ADP-ribosylation factor-binding protein GGA1 (Gamma-adaptin-related protein 1) (Golgi-localized, gamma ear-containing, ARF-binding protein 1) 635 69,972 Chain (1); Domain (3); Modified residue (4); Motif (1); Region (2) FUNCTION: Plays a role in protein sorting and trafficking between the trans-Golgi network (TGN) and endosomes (PubMed:25405894). Mediates the ARF-dependent recruitment of clathrin to the TGN and binds ubiquitinated proteins and membrane cargo molecules with a cytosolic acidic cluster-dileucine (DXXLL) motif. Mediates export of the GPCR receptor ADRA2B to the cell surface (By similarity). Required for targeting PKD1:PKD2 complex from the trans-Golgi network to the cilium membrane (PubMed:25405894). Regulates retrograde transport of proteins such as phosphorylated form of BACE1 from endosomes to the trans-Golgi network (By similarity). {ECO:0000250|UniProtKB:Q9UJY5, ECO:0000269|PubMed:25405894}. PTM: Phosphorylated by CK2 and dephosphorylated by PP2A. Phosphorylation of GGA1 allows the internal DXXLL motif to bind the VHS domain and to inhibit the recognition of cargo signals.; PTM: Ubiquitinated. {ECO:0000250|UniProtKB:Q9UJY5}. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q9UJY5}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9UJY5}. Endosome membrane {ECO:0000250|UniProtKB:Q9UJY5}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9UJY5}. Early endosome membrane {ECO:0000250|UniProtKB:Q9UJY5}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9UJY5}. SUBUNIT: Monomer. Interacts with GGA2 and GGA3 (By similarity). Binds to clathrin and activated ARFs, including ARF1, ARF5 and ARF6 (PubMed:22522702, PubMed:11950392). Interacts with RABEP1 and RABGEF1 (PubMed:25405894). Interacts with the type-I membrane proteins SORT1, SORL1, LRP3, M6PR/CD-MPR and IGF2R/CI-MPR. Interacts with EPN4. Binds CCDC91, P200 and SYNRG. Interacts with NECAP1, NECAP2 and AFTPH/aftiphilin. Interacts with TSG101 and UBC. Interacts with RNF11. Interacts (via VHS domain) with BACE1 (via DXXLL motif); the interaction highly increases when BACE1 is phosphorylated at 'Ser-498' (By similarity). Interacts with CNST (PubMed:19864490). Interacts with ADRA2B (By similarity). Interacts with ARL3; the interaction recruits, in collaboration with RABEP1, PKD1:PKD2 complex to trans-Golgi network and is required for ciliary targeting (PubMed:25405894). {ECO:0000250|UniProtKB:Q9UJY5, ECO:0000269|PubMed:11950392, ECO:0000269|PubMed:19864490, ECO:0000269|PubMed:22522702, ECO:0000269|PubMed:25405894}. DOMAIN: The VHS domain functions as a recognition module for sorting signals composed of an acidic cluster followed by two leucines (DXXLL motif).; DOMAIN: The GAT domain is responsible for interaction with ARF-GTP, UBC and RABEP1. Required for recruitment to the TGN it prevents ARF-GTP hydrolysis. {ECO:0000250|UniProtKB:Q9UJY5}.; DOMAIN: The unstructured hinge region contains clathrin-binding but no autoinhibitory (DXXLL) motifs. {ECO:0000250|UniProtKB:Q9UJY5}.; DOMAIN: The GAE domain binds accessory proteins regulating GGAs function. +O08842 GFRA2_MOUSE GDNF family receptor alpha-2 (GDNF receptor alpha-2) (GDNFR-alpha-2) (GFR-alpha-2) (GDNF receptor beta) (GDNFR-beta) (Neurturin receptor alpha) (NRTNR-alpha) (NTNR-alpha) (TGF-beta-related neurotrophic factor receptor 2) 464 51,727 Alternative sequence (2); Chain (1); Erroneous termination (4); Glycosylation (3); Lipidation (1); Propeptide (1); Sequence conflict (5); Signal peptide (1) FUNCTION: Receptor for neurturin. Mediates the NRTN-induced autophosphorylation and activation of the RET receptor. Also able to mediate GDNF signaling through the RET tyrosine kinase receptor. {ECO:0000269|PubMed:9182803}.; FUNCTION: Isoform 2: participates in NRTN-induced 'Ser-727' phosphorylation of STAT3. {ECO:0000269|PubMed:23872421}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:9182803}; Lipid-anchor, GPI-anchor {ECO:0000305|PubMed:9182803}. TISSUE SPECIFICITY: Neurons of the superior cervical and dorsal root ganglia, and adult brain and testis. Low level in the substantia nigra, spleen and adrenal gland (PubMed:9182803). Isoform 1, isoform 2 and isoform 3 are all expressed in brain, liver, ileum, spleen, heart and kidney (PubMed:9875703). In brain, isoform 1 is most abundant, isoform 2 slightly less and isoform 3 is lowest. No significant levels of isoform 1, isoform 2 or isoform 3 expression in testis (PubMed:12829325). {ECO:0000269|PubMed:12829325, ECO:0000269|PubMed:9182803, ECO:0000269|PubMed:9875703}. +Q9CR36 GKN1_MOUSE Gastrokine-1 (18 kDa antrum mucosa protein) (AMP-18) (Protein CA11 homolog) 201 21,887 Chain (1); Disulfide bond (1); Domain (1); Erroneous initiation (10); Sequence conflict (3); Signal peptide (1) FUNCTION: Has mitogenic activity and may be involved in maintaining the integrity of the gastric mucosal epithelium. {ECO:0000269|PubMed:12851218}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12851218}. TISSUE SPECIFICITY: Highly expressed specifically in surface cells of the antrum mucosa from where it is secreted. {ECO:0000269|PubMed:12851218}. +Q9D0T7 GKN3_MOUSE Gastrokine-3 191 20,772 Chain (1); Disulfide bond (1); Domain (1); Glycosylation (1); Mutagenesis (2); Signal peptide (1) FUNCTION: Inhibits gastric epithelial cell proliferation. {ECO:0000269|PubMed:20138039}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20138039}. TISSUE SPECIFICITY: Expressed in stomach. Present in mucus cells at the base of antral glands, and Brunner glands of the duodenum. Present at lower levels in the mucus neck cell region of the fundus (at protein level). {ECO:0000269|PubMed:20138039}. +Q7TSN7 IGSF5_MOUSE Immunoglobulin superfamily member 5 (IgSF5) (Junctional adhesion molecule 4) (JAM-4) 370 40,292 Beta strand (1); Chain (1); Compositional bias (1); Disulfide bond (2); Domain (2); Glycosylation (5); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 240 260 Helical. {ECO:0000255}. TOPO_DOM 25 239 Extracellular. {ECO:0000255}.; TOPO_DOM 261 370 Cytoplasmic. {ECO:0000255}. FUNCTION: Provides, together with MAGI1, an adhesion machinery at tight junctions, which may regulate the permeability of kidney glomerulus and small intestinal epithelial cells. Mediates calcium-independent homophilic cell adhesion. In testis, it may function as a cell adhesion molecule rather than a tight-junction protein. It may participate in the adhesion between spermatogonia-spermatogonia, spermatogonia-Sertoli cells, and Sertoli cells-Sertoli cells. {ECO:0000269|PubMed:12773569, ECO:0000269|PubMed:16982697}. PTM: N-glycosylated. {ECO:0000269|PubMed:12773569}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:Q5VJ70}; Single-pass type I membrane protein {ECO:0000255}. Cell junction, tight junction {ECO:0000250|UniProtKB:Q5VJ70}. SUBUNIT: Interacts with MAGI1 at tight junctions, forms a tripartite complex with NPHS1 (By similarity). Interacts with LNX1 isoform 2 via its PDZ 2 domain, it may also interact with other isoforms containing this domain. {ECO:0000250, ECO:0000269|PubMed:12773569, ECO:0000269|PubMed:16832352}. TISSUE SPECIFICITY: Localized to kidney glomeruli and small intestinal epithelial cells. In kidney glomeruli, it is localized at slit diaphragm. Also found in spermatogonia, gonocytes, hematopoietic stem cells and Sertoli cells. {ECO:0000269|PubMed:12773569, ECO:0000269|PubMed:16982697}. +Q9CPV4 GLOD4_MOUSE Glyoxalase domain-containing protein 4 298 33,317 Alternative sequence (3); Chain (1); Domain (2); Modified residue (3); Sequence conflict (3) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. SUBUNIT: Interacts with NUDT9. {ECO:0000250}. +Q9D8I3 GLOD5_MOUSE Glyoxalase domain-containing protein 5 148 16,595 Chain (1); Domain (1) +P97812 IHH_MOUSE Indian hedgehog protein (IHH) (HHG-2) [Cleaved into: Indian hedgehog protein N-product; Indian hedgehog protein C-product] 411 45,485 Chain (3); Erroneous initiation (1); Glycosylation (1); Lipidation (2); Metal binding (12); Sequence conflict (1); Signal peptide (1); Site (4) FUNCTION: Intercellular signal essential for a variety of patterning events during development. Binds to the patched (PTC) receptor, which functions in association with smoothened (SMO), to activate the transcription of target genes. Implicated in endochondral ossification: may regulate the balance between growth and ossification of the developing bones. Induces the expression of parathyroid hormone-related protein (PTHRP). PTM: The C-terminal domain displays an autoproteolysis activity and a cholesterol transferase activity. Both activities result in the cleavage of the full-length protein and covalent attachment of a cholesterol moiety to the C-terminal of the newly generated N-terminal fragment (N-product). The N-product is the active species in both local and long-range signaling, whereas the C-product has no signaling activity (By similarity). {ECO:0000250}.; PTM: Cholesterylation is required for N-product targeting to lipid rafts and multimerization. {ECO:0000250}.; PTM: N-palmitoylation is required for N-product multimerization and full activity. {ECO:0000250}. SUBCELLULAR LOCATION: Indian hedgehog protein N-product: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Extracellular side {ECO:0000250}. Note=The N-terminal peptide remains associated with the cell surface. {ECO:0000250}.; SUBCELLULAR LOCATION: Indian hedgehog protein C-product: Secreted, extracellular space {ECO:0000250}. Note=The C-terminal peptide diffuses from the cell. {ECO:0000250}.; SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. SUBUNIT: Homooligomer (indian hedgehog protein N-product). Interacts with BOC and CDON. Interacts with PTCH1 (By similarity). Interacts with glypican GPC3 (PubMed:23665349). {ECO:0000250, ECO:0000269|PubMed:23665349}. DOMAIN: The indian hedgehog protein N-product binds calcium and zinc ions; this stabilizes the protein fold and is essential for protein-protein interactions mediated by this domain. {ECO:0000250}. TISSUE SPECIFICITY: In the embryo, detected in the developing gut, the growth zone of cartilage of developing long bones, epithelium and urogenital sinus. In the adult kidney, found in proximal convoluted and proximal straight tubule. +Q6PDM4 IHO1_MOUSE Interactor of HORMAD1 protein 1 (Coiled-coil domain-containing protein 36) 574 63,340 Chain (1); Coiled coil (1); Erroneous initiation (1); Modified residue (3) FUNCTION: Required for DNA double-strand breaks (DSBs) formation in unsynapsed regions during meiotic recombination (PubMed:27723721). Probably acts by forming a complex with MEI4 and REC114, which activates DSBs formation in unsynapsed regions, an essential step to ensure completion of synapsis (PubMed:27723721). Not required for HORMAD1 functions in pairing-independent synaptonemal complex formation, ATR recruitment to unsynapsed axes, meiotic silencing of unsynapsed chromatin (MSUC) or meiotic surveillance (PubMed:27723721). {ECO:0000269|PubMed:27723721}. SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:27723721}. Note=Specifically localizes to unsynapsed chromosomal regions during meiosis (PubMed:27723721). Appears on chromatin during preleptotene, when pre-meiotic replication occurs and axes have not yet developed (PubMed:27723721). Remains associated with unsynapsed axesn zygotene, when axes elongate and synapsis begins but disappears from synapsed axes (PubMed:27723721). Localization diverges in the two sexes beyond zygotene (PubMed:27723721). In spermatocytes, synapsis between the largely non-homologous X and Y chromosomes is mostly constrained to their short pseudoautosomal regions (PARs) (PubMed:27723721). At the zygotene-to-pachytene transition, high levels remain on unsynapsed sex chromosome axes but also on PARs (PubMed:27723721). However, by early pachytene disappears from both the synapsed and unsynapsed regions of sex chromosomes (PubMed:27723721). Reaccumulates on unsynapsed axes of sex chromosomes in mid-late pachytene and on desynapsing autosome axes in diplotene, but disappears from chromatin concomitant with axis disassembly after diplotene (PubMed:27723721). In oocytes, disappears from axes after all chromosomes synapsed and is undetectable on chromatin beyond zygotene (PubMed:27723721). Ovarian levels also dramatically decrease as oocytes progress to late prophase (PubMed:27723721). HORMAD1 is required for robust accumulation on chromatin and unsynapsed axes, suggesting that HORMAD1 recruits IHO1/CCDC36 to unsynapsed axes (PubMed:27723721). {ECO:0000269|PubMed:27723721}. SUBUNIT: Interacts with HORMAD1 (PubMed:27723721). Interacts with REC114 (PubMed:27723721). Part of the MCD recombinosome complex, at least composed of IHO1/CCDC36, REC114 and MEI4 (PubMed:27723721). {ECO:0000269|PubMed:27723721}. TISSUE SPECIFICITY: Detected in spermatocytes and testis (at protein level) (PubMed:27723721). {ECO:0000269|PubMed:27723721}. +Q9QZ85 IIGP1_MOUSE Interferon-inducible GTPase 1 (EC 3.6.5.-) 413 47,572 Beta strand (12); Chain (1); Domain (1); Helix (23); Initiator methionine (1); Lipidation (1); Mutagenesis (3); Nucleotide binding (4); Sequence conflict (1); Turn (2) FUNCTION: GTPase with low activity. Has higher affinity for GDP than for GTP. Plays a role in resistance to intracellular pathogens. Required for disruption of the parasitophorous vacuole formed following T.gondii infection and subsequent killing of the parasite. Mediates resistance to C.trachomatis infection by targeting bacterial inclusions to autophagosomes for subsequent lysosomal destruction. {ECO:0000269|PubMed:11907101, ECO:0000269|PubMed:12732635, ECO:0000269|PubMed:16304607, ECO:0000269|PubMed:19242543}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Peripheral membrane protein. Golgi apparatus, Golgi stack membrane; Peripheral membrane protein. Parasitophorous vacuole membrane. Note=Localizes to the bacterial inclusions formed following C.trachomatis infection. Accumulates in a GTP-bound form on the parasitophorous vacuole membranes formed following T.gondii infection but exists in a GDP-bound form in uninfected cells. SUBUNIT: Monomer, as apoenzyme and in the GDP-bound form. Homooligomer, upon GTP binding. Interacts with HOOK3. {ECO:0000269|PubMed:12732635, ECO:0000269|PubMed:15075236, ECO:0000269|PubMed:18784077}. +Q60778 IKBB_MOUSE NF-kappa-B inhibitor beta (NF-kappa-BIB) (I-kappa-B-beta) (IkB-B) (IkB-beta) (IkappaBbeta) 359 37,965 Beta strand (1); Chain (1); Helix (15); Modified residue (4); Repeat (6); Sequence conflict (1); Turn (2) FUNCTION: Inhibits NF-kappa-B by complexing with and trapping it in the cytoplasm. However, the unphosphorylated form resynthesized after cell stimulation is able to bind NF-kappa-B allowing its transport to the nucleus and protecting it to further NFKBIA-dependent inactivation. Association with inhibitor kappa B-interacting NKIRAS1 and NKIRAS2 prevent its phosphorylation rendering it more resistant to degradation, explaining its slower degradation. PTM: Phosphorylated by RPS6KA1; followed by degradation. Interaction with NKIRAS1 and NKIRAS2 probably prevents phosphorylation. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. SUBUNIT: Interacts with THRB (via ligand-binding domain) (By similarity). Interacts with RELA and REL (PubMed:8816457). Interacts with COMMD1 (By similarity). Interacts with inhibitor kappa B-interacting Ras-like NKIRAS1 and NKIRAS2 (PubMed:10657303). {ECO:0000250|UniProtKB:Q15653, ECO:0000269|PubMed:10657303, ECO:0000269|PubMed:8816457}. TISSUE SPECIFICITY: Highly expressed in testis followed by spleen. +Q2TB02 IKBD_MOUSE NF-kappa-B inhibitor delta (I-kappa-B-delta) (IkB-delta) (IkappaBdelta) (IkappaBNS) 327 34,942 Chain (1); Frameshift (1); Repeat (6); Sequence conflict (1) FUNCTION: Regulates the expression of IL-2, IL-6, and other cytokines through regulation on NF-kappa-B activity. Functions in the regulation of inflammatory responses (PubMed:11931770, PubMed:15749903, PubMed:16410444, PubMed:16413922, PubMed:17641034). Involved in the induction of T helper 17 cells (Th17) differentiation upon recognition of antigen by T cell antigen receptor (TCR) (PubMed:25282160). According to PubMed:11931770, it may also regulate TCR-induced negative selection of thymocytes (PubMed:11931770). {ECO:0000269|PubMed:11931770, ECO:0000269|PubMed:15749903, ECO:0000269|PubMed:16410444, ECO:0000269|PubMed:16413922, ECO:0000269|PubMed:17641034, ECO:0000269|PubMed:25282160}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11931770}. SUBUNIT: Interacts with NFKB1, RELA and RELB; in the nucleus. {ECO:0000269|PubMed:11931770}. TISSUE SPECIFICITY: Specifically expressed in spleen and at low levels in thymus. Expressed in a population of antigen-presenting dendritic cells which may act as regulators of systemic inflammatory response. {ECO:0000269|PubMed:11931770, ECO:0000269|PubMed:16410444}. +Q03267 IKZF1_MOUSE DNA-binding protein Ikaros (Ikaros family zinc finger protein 1) (Lymphoid transcription factor LyF-1) 517 57,336 Alternative sequence (4); Chain (1); Compositional bias (1); Cross-link (2); Modified residue (19); Mutagenesis (52); Region (3); Sequence conflict (2); Site (3); Zinc finger (6) FUNCTION: Transcription regulator of hematopoietic cell differentiation. Binds gamma-satellite DNA. Binds with higher affinity to gamma satellite A. Plays a role in the development of lymphocytes, B- and T-cells. Binds and activates the enhancer (delta-A element) of the CD3-delta gene. Repressor of the TDT (terminal deoxynucleotidyltransferase) gene during thymocyte differentiation. Regulates transcription through association with both HDAC-dependent and HDAC-independent complexes. Targets the 2 chromatin-remodeling complexes, NuRD and BAF (SWI/SNF), in a single complex (PYR complex), to the beta-globin locus in adult erythrocytes. Increases normal apoptosis in adult erythroid cells (By similarity). Confers early temporal competence to retinal progenitor cells (RPCs). Function is isoform-specific and is modulated by dominant-negative inactive isoforms (By similarity). {ECO:0000250|UniProtKB:Q13422, ECO:0000269|PubMed:11003653, ECO:0000269|PubMed:1439790, ECO:0000269|PubMed:15024069, ECO:0000269|PubMed:15767674, ECO:0000269|PubMed:16369973, ECO:0000269|PubMed:18223295, ECO:0000269|PubMed:18940586}. PTM: Phosphorylation at Ser-357 and Ser-360 downstream of SYK induces nuclear translocation (By similarity). Phosphorylation controls cell-cycle progression from late G(1) stage to S stage. Hyperphosphorylated during G2/M phase. Dephosphorylated state during late G(1) phase. Phosphorylation on Thr-140 is required for DNA and pericentromeric location during mitosis. CK2 is the main kinase, in vitro. GSK3 and CDK may also contribute to phosphorylation of the C-terminal serine and threonine residues. Phosphorylation on these C-terminal residues reduces the DNA-binding ability. Phosphorylation/dephosphorylation events on Ser-13 and Ser-293 regulate TDT expression during thymocyte differentiation. Dephosphorylation by protein phosphatase 1 regulates stability and pericentromeric heterochromatin location. Phosphorylated in both lymphoid and non-lymphoid tissues. {ECO:0000250, ECO:0000269|PubMed:12464629, ECO:0000269|PubMed:15024069, ECO:0000269|PubMed:18223295, ECO:0000269|PubMed:19282287}.; PTM: Sumoylated. Simulataneous sumoylation on the 2 sites results in a loss of both HDAC-dependent and HDAC-independent repression. Has no effect on pericentromeric heterochromatin location. Desumoylated by SENP1. {ECO:0000269|PubMed:15767674}.; PTM: Polyubiquitinated. {ECO:0000269|PubMed:19282287}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10970879, ECO:0000269|PubMed:12464629, ECO:0000269|PubMed:18223295, ECO:0000269|PubMed:19282287}. Note=In resting lymphocytes, distributed diffusely throughout the nucleus. Localizes to pericentromeric heterochromatin in proliferating cells. This localization requires DNA binding which is regulated by phosphorylation / dephosphorylation events.; SUBCELLULAR LOCATION: Isoform V: Nucleus. Note=In resting lymphocytes, distributed diffusely throughout the nucleus. Localizes to pericentromeric heterochromatin in proliferating cells. This localization requires DNA binding which is regulated by phosphorylation / dephosphorylation events.; SUBCELLULAR LOCATION: Isoform I: Cytoplasm. SUBUNIT: Heterodimer with other IKAROS family members. Interacts with IKZF4 AND IKZF5 (By similarity). Component of the chromatin-remodeling NuRD repressor complex which includes at least HDAC1, HDAC2, RBBP4, RBBP7, IKZF1, MTA2, MBD2, MBD3, MTA1L1, CHD3 and CHD4. Interacts directly with the CHD4 component of the NuRD complex. Interacts directly with SMARCA4; the interaction associates IKFZ1 with the BAF complex. Interacts with SUMO1; the interaction sumoylates IKAROS, promoted by PIAS2 and PIAS3. Interacts with PIAS2 (isoform alpha); the interaction promotes sumoylation and reduces transcription repression. Interacts, to a lesser extent, with PIAS3. Interacts with PPP1CC; the interaction targets PPP1CC to pericentromeric heterochromatin, dephosphorylates IKAROS, stabilizes it and prevents it from degradation. Interacts with IKZF3. {ECO:0000250|UniProtKB:Q13422, ECO:0000269|PubMed:11003653, ECO:0000269|PubMed:15767674, ECO:0000269|PubMed:19282287, ECO:0000269|PubMed:9155026}. DOMAIN: The N-terminal zinc-fingers 2 and 3 are required for DNA binding as well as for targeting IKFZ1 to pericentromeric heterochromatin.; DOMAIN: The C-terminal zinc-finger domain is required for dimerization. TISSUE SPECIFICITY: Strongly expressed in T-cells and their progenitors,in B-cells, and in all early embryonic retinal progenitor cells (RPCs). Isoforms V and VI are the predominant isoforms in lymphocytes. {ECO:0000269|PubMed:1439790, ECO:0000269|PubMed:18940586, ECO:0000269|PubMed:7935426}. +P81183 IKZF2_MOUSE Zinc finger protein Helios (Ikaros family zinc finger protein 2) 526 59,401 Alternative sequence (1); Chain (1); Cross-link (3); Modified residue (4); Sequence conflict (1); Zinc finger (6) FUNCTION: Associates with Ikaros at centromeric heterochromatin. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with IKZF4 AND IKZF5. {ECO:0000250}. TISSUE SPECIFICITY: Restricted to the T-cell lineage. Abundant in thymus, low expression in bone marrow and brain and no detectable expression in spleen, liver, kidney or muscle. +O08900 IKZF3_MOUSE Zinc finger protein Aiolos (Ikaros family zinc finger protein 3) 507 57,967 Chain (1); Cross-link (4); Modified residue (5); Sequence conflict (3); Zinc finger (6) FUNCTION: Transcription factor that plays an important role in the regulation of lymphocyte differentiation. Binds to GGGAA. Plays an essential role in regulation of B-cell differentiation, proliferation and maturation to an effector state. Involved in regulating BCL2 expression and controlling apoptosis in T-cells in an IL2-dependent manner. {ECO:0000269|PubMed:9155026, ECO:0000269|PubMed:9806640}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9155026}. Cytoplasm {ECO:0000269|PubMed:9155026}. SUBUNIT: Homodimer, and heterodimer with other IKAROS family members. Interacts with IKZF4 AND IKZF5. Interacts with HRAS. Interacts with FOXP3; this interaction may be required for silencing target genes and regulating the suppressive activity of FOXP3-positive regulatory T-cells (Treg). Interacts with BCL21L isoform Bcl-X(L); this interaction blocks the anti-apoptotic role of BCL21L. Associates with histone deacetylase complexes containing HDAC1, MTA2 and SIN3A (By similarity). Interacts with IKZF1. {ECO:0000250, ECO:0000269|PubMed:9155026}. TISSUE SPECIFICITY: Expression is restricted to lymphoid tissues. Expressed at highest levels in spleen and at lower levels in the thymus and bone marrow. First detected in more committed lymphoid progenitors and strongly up-regulated as these differentiate into pre-T and pre-B cell precursors. {ECO:0000269|PubMed:9155026}. +Q8C208 IKZF4_MOUSE Zinc finger protein Eos (Ikaros family zinc finger protein 4) 586 64,155 Alternative sequence (3); Chain (1); Cross-link (2); Frameshift (1); Modified residue (2); Motif (1); Region (1); Sequence conflict (4); Zinc finger (6) FUNCTION: DNA-binding protein that binds to the 5'GGGAATRCC-3' Ikaros-binding sequence. Interacts with SPI1 and MITF to repress transcription of the CTSK and ACP5 promoters via recruitment of corepressors SIN3A and CTBP2. May be involved in the development of central and peripheral nervous systems. Essential for the inhibitory function of regulatory T-cells (Treg). Mediates FOXP3-mediated gene silencing in regulatory T-cells (Treg) via recruitment of corepressor CTBP1 (PubMed:19696312). {ECO:0000269|PubMed:10218586, ECO:0000269|PubMed:17403896, ECO:0000269|PubMed:19696312}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Self-associates. Interacts with other family members; IKZF1, IKZF2, IKZF3 AND IKZF5 (By similarity). Interacts with CTBP2, SPI1 and MITF. Interacts with FOXP3 and CTBP1. {ECO:0000250|UniProtKB:Q9H2S9, ECO:0000269|PubMed:10218586, ECO:0000269|PubMed:12444977, ECO:0000269|PubMed:17403896, ECO:0000269|PubMed:19696312}. DOMAIN: The N-terminal zinc fingers are involved in sequence-specific DNA binding.; DOMAIN: C-terminal zinc fingers mediate homodimerization. TISSUE SPECIFICITY: Expressed mainly in the brain. Up-regulated in long term cultured astrocytes. Down-regulated during osteoclast differentiation. {ECO:0000269|PubMed:10218586, ECO:0000269|PubMed:17403896}. +Q8BU00 IKZF5_MOUSE Zinc finger protein Pegasus (Ikaros family zinc finger protein 5) 419 46,400 Alternative sequence (3); Chain (1); Cross-link (2); Sequence conflict (1); Zinc finger (5) FUNCTION: DNA-binding protein that binds to the 5'GNNTGTNG-3' core sequence. Transcriptional repressor (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Self-associates. Interacts with other family members; IKZF1, IKZF2, IKZF3 AND IKZF4 (By similarity). {ECO:0000250}. DOMAIN: The N-terminal zinc fingers are involved in sequence-specific DNA binding and heterotypic associations with other family members. {ECO:0000250}.; DOMAIN: C-terminal zinc fingers mediate homodimerization. {ECO:0000250}. +P47873 IL11_MOUSE Interleukin-11 (IL-11) 199 21,522 Chain (1); Mutagenesis (4); Region (1); Signal peptide (1); Site (1) FUNCTION: Cytokine that stimulates the proliferation of hematopoietic stem cells and megakaryocyte progenitor cells and induces megakaryocyte maturation resulting in increased platelet production (PubMed:8913282). Also promotes the proliferation of hepatocytes in response to liver damage (PubMed:22253262). Binding to its receptor formed by IL6ST and either IL11RA1 or IL11RA2 activates a signaling cascade that promotes cell proliferation, also in the context of various cancers (PubMed:10026196, PubMed:23948300). Signaling leads to the activation of intracellular protein kinases and the phosphorylation of STAT3 (PubMed:23948300, PubMed:22253262). {ECO:0000269|PubMed:10026196, ECO:0000269|PubMed:22253262, ECO:0000269|PubMed:23948300, ECO:0000269|PubMed:8913282}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22253262}. SUBUNIT: Interacts with IL6ST and either IL11RA1 or IL11RA2, giving rise to a multimeric signaling complex. {ECO:0000269|PubMed:10026196}. +P43431 IL12A_MOUSE Interleukin-12 subunit alpha (IL-12A) (Cytotoxic lymphocyte maturation factor 35 kDa subunit) (CLMF p35) (IL-12 subunit p35) 215 24,179 Chain (1); Disulfide bond (3); Glycosylation (1); Signal peptide (1) FUNCTION: Cytokine that can act as a growth factor for activated T and NK cells, enhance the lytic activity of NK/lymphokine-activated killer cells, and stimulate the production of IFN-gamma by resting PBMC. {ECO:0000250|UniProtKB:P29459}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1350290}. SUBUNIT: Heterodimer with IL12B; disulfide-linked (PubMed:1350290). This heterodimer is known as interleukin IL-12 (PubMed:1350290). Heterodimer with EBI3/IL27B; not disulfide-linked (By similarity). This heterodimer is known as interleukin IL-35 (By similarity). {ECO:0000250|UniProtKB:P29459, ECO:0000269|PubMed:1350290}. +P20109 IL13_MOUSE Interleukin-13 (IL-13) (T-cell activation protein P600) 131 14,108 Chain (1); Disulfide bond (2); Glycosylation (3); Signal peptide (1) FUNCTION: Cytokine. Inhibits inflammatory cytokine production. Synergizes with IL2 in regulating interferon-gamma synthesis. May be critical in regulating inflammatory and immune responses (By similarity). Positively regulates IL31RA expression in macrophages (PubMed:25847241). {ECO:0000250|UniProtKB:P35225, ECO:0000269|PubMed:25847241}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Interacts with IL13RA2. {ECO:0000250}. +Q61098 IL18R_MOUSE Interleukin-18 receptor 1 (IL-18R-1) (IL-18R1) (CD218 antigen-like family member A) (IL1 receptor-related protein) (IL-1Rrp) (IL1R-rp) (Interleukin-18 receptor alpha) (IL-18R-alpha) (IL-18Ralpha) (CD antigen CD218a) 537 61,601 Chain (1); Disulfide bond (4); Domain (4); Glycosylation (10); Natural variant (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 327 347 Helical. {ECO:0000255}. TOPO_DOM 20 326 Extracellular. {ECO:0000255}.; TOPO_DOM 348 537 Cytoplasmic. {ECO:0000255}. FUNCTION: Within the IL18 receptor complex, responsible for the binding of the proinflammatory cytokine IL18, but not IL1A nor IL1B. Involved in IL18-mediated IFNG synthesis from T-helper 1 (Th1) cells (By similarity). Contributes to IL18-induced cytokine production, either independently of SLC12A3, or as a complex with SLC12A3 (PubMed:26099046). {ECO:0000250|UniProtKB:Q13478, ECO:0000269|PubMed:26099046}. SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q13478}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Forms a ternary complex with IL18 and IL18RAP (By similarity). Within this complex, IL18R1 is involved in ligand-binding and IL18RAP in signaling leading to NF-kappa-B and JNK activation (By similarity). Interacts with SLC12A3 in peritoneal macrophages; this interaction is increased by IL18 treatment (PubMed:26099046). {ECO:0000250|UniProtKB:Q13478, ECO:0000269|PubMed:26099046}. +P70380 IL18_MOUSE Interleukin-18 (IL-18) (Interferon gamma-inducing factor) (IFN-gamma-inducing factor) (Interleukin-1 gamma) (IL-1 gamma) 192 22,135 Chain (1); Propeptide (1); Sequence conflict (1) FUNCTION: A proinflammatory cytokine primarily involved in polarized T-helper 1 (Th1) cell and natural killer (NK) cell immune responses. Upon binding to IL18R1 and IL18RAP, forms a signaling ternary complex which activates NF-kappa-B, triggering synthesis of inflammatory mediators. Synergizes with IL12/interleukin-12 to induce IFNG synthesis from T-helper 1 (Th1) cells and natural killer (NK) cells. {ECO:0000250|UniProtKB:Q14116}. PTM: The pro-IL-18 precursor is processed by CASP1 or CASP4 to yield the active form. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q14116}. SUBUNIT: Forms a ternary complex with ligand-binding receptor subunit IL18R1 and signaling receptor subunit IL18RAP at the plasma membrane. Mature IL18 first binds to IL18R1 forming a low affinity binary complex, which then interacts with IL18RAP to form a high affinity ternary complex that signals inside the cell. {ECO:0000250|UniProtKB:Q14116}. +Q8CJ70 IL19_MOUSE Interleukin-19 (IL-19) 176 20,288 Chain (1); Disulfide bond (3); Glycosylation (3); Signal peptide (1) FUNCTION: May play some important roles in inflammatory responses. Up-regulates IL-6 and TNF-alpha and induces apoptosis. {ECO:0000269|PubMed:12370360}. SUBCELLULAR LOCATION: Secreted. +Q61730 IL1AP_MOUSE Interleukin-1 receptor accessory protein (IL-1 receptor accessory protein) (IL-1RAcP) (Interleukin-33 receptot beta chain) 570 65,741 Alternative sequence (3); Beta strand (26); Chain (1); Disulfide bond (5); Domain (4); Glycosylation (7); Helix (6); Mutagenesis (6); Region (1); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 368 388 Helical. {ECO:0000255}. TOPO_DOM 21 367 Extracellular. {ECO:0000255}.; TOPO_DOM 389 570 Cytoplasmic. {ECO:0000255}. FUNCTION: Coreceptor for IL1RL2 in the IL-36 signaling system. Coreceptor with IL1R1 in the IL-1 signaling system. Associates with IL1R1 bound to IL1B to form the high affinity interleukin-1 receptor complex which mediates interleukin-1-dependent activation of NF-kappa-B and other pathways. Signaling involves the recruitment of adapter molecules such as TOLLIP, MYD88, and IRAK1 or IRAK2 via the respective TIR domains of the receptor/coreceptor subunits. Recruits TOLLIP to the signaling complex. Does not bind to interleukin-1 alone; binding of IL1RN to IL1R1, prevents its association with IL1R1 to form a signaling complex. The cellular response is modulated through a non-signaling association with the membrane IL1R2 decoy receptor. Secreted forms (isoforms 2 and 3) associate with secreted ligand-bound IL1R2 and increase the affinity of secreted IL1R2 for IL1B; this complex formation may be the dominant mechanism for neutralization of IL1B by secreted/soluble receptors. Coreceptor for IL1RL1 in the IL-33 signaling system. Can bidirectionally induce pre- and postsynaptic differentiation of neurons by trans-synaptically binding to PTPRD (PubMed:25908590). May play a role in IL1B-mediated costimulation of IFNG production from T-helper 1 (Th1) cells (By similarity). {ECO:0000250|UniProtKB:Q9NPH3, ECO:0000269|PubMed:11880380, ECO:0000269|PubMed:15986350, ECO:0000269|PubMed:17675517, ECO:0000269|PubMed:18003919, ECO:0000269|PubMed:18450470, ECO:0000269|PubMed:25908590, ECO:0000303|PubMed:21965679}.; FUNCTION: Isoform 2: Associates with secreted ligand-bound IL1R2 and increases the affinity of secreted IL1R2 for IL1B; this complex formation may be the dominant mechanism for neutralization of IL1B by secreted/soluble receptors. Enhances the ability of secreted IL1R1 to inhibit IL-33 signaling. {ECO:0000269|PubMed:15986350, ECO:0000269|PubMed:18450470}.; FUNCTION: Isoform 3: Required for Src phosphorylation by IL1B. Required for IL1B-potentiated NMDA-induced calcium influx in neurons acting in cooperation with IL1R1 isoform 2 to mediate Akt kinase activation. {ECO:0000269|PubMed:22159118, ECO:0000269|PubMed:22778412}. SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Isoform 2: Secreted. SUBUNIT: The interleukin-36 receptor complex is a heterodimer of IL1RL2 and IL1RAP; the association is inhibited by IL36RN. The interleukin-1 receptor complex is a heterodimer of IL1R1 and IL1RAP. Associates with IL1R2 to form a non-signaling interleukin-1 receptor complex. Interacts with IL-33-bound IL1RL1 to form the minimal interleukin-33 signaling complex with a 1:1:1 stoichiometry. Interacts with KIT (independently of stimulation with KITLG/SCF). A mast cell-specific KITLG/SCF-induced interleukin-33 signaling complex contains IL1RL1, IL1RAP, KIT and MYD88. Interacts (via the first immunoglobilin domain) with PTPRD (via the third immunoglobilin domain); induces pre- and postsynaptic differentiation of neurons (PubMed:25908590). {ECO:0000269|PubMed:17675517, ECO:0000269|PubMed:18003919, ECO:0000269|PubMed:20200353, ECO:0000269|PubMed:21965679, ECO:0000269|PubMed:25908590, ECO:0000269|PubMed:9862719}. TISSUE SPECIFICITY: Detected in lung, brain, spleen, thymus and liver. Expressed in brain endothelial cells, astrocytes, microglia and neurons. Isoform 3 is predominantly expressed in brain; expressed in hippocampal neurons. {ECO:0000269|PubMed:19481478, ECO:0000269|PubMed:21349253, ECO:0000269|PubMed:22159118, ECO:0000269|PubMed:7775431}. +Q8BX05 GLPK5_MOUSE Putative glycerol kinase 5 (GK 5) (Glycerokinase 5) (EC 2.7.1.30) (ATP:glycerol 3-phosphotransferase 5) 534 59,812 Alternative sequence (2); Binding site (4); Chain (1); Erroneous initiation (1); Nucleotide binding (1); Sequence conflict (1) Polyol metabolism; glycerol degradation via glycerol kinase pathway; sn-glycerol 3-phosphate from glycerol: step 1/1. +P10749 IL1B_MOUSE Interleukin-1 beta (IL-1 beta) 269 30,931 Beta strand (14); Chain (1); Helix (2); Propeptide (1); Site (5); Turn (2) FUNCTION: Potent proinflammatory cytokine. Initially discovered as the major endogenous pyrogen, induces prostaglandin synthesis, neutrophil influx and activation, T-cell activation and cytokine production, B-cell activation and antibody production, and fibroblast proliferation and collagen production. Promotes Th17 differentiation of T-cells. Synergizes with IL12/interleukin-12 to induce IFNG synthesis from T-helper 1 (Th1) cells. {ECO:0000250|UniProtKB:P01584}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:17284521}. Lysosome {ECO:0000250|UniProtKB:P01584}. Secreted, exosome {ECO:0000269|PubMed:17641058}. Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:P01584}. Secreted {ECO:0000269|PubMed:17284521, ECO:0000269|PubMed:17641058}. Note=The precursor is cytosolic. In response to inflammasome-activating signals, such as ATP for NLRP3 inflammasome or bacterial flagellin for NLRC4 inflammasome, cleaved and secreted. IL1B lacks any known signal sequence and the pathway(s) of its secretion is(are) not yet fully understood. On the basis of experimental results, several unconventional secretion mechanisms have been proposed. 1. Secretion via secretory lysosomes: a fraction of CASP1 and IL1B precursor may be incorporated, by a yet undefined mechanism, into secretory lysosomes that undergo Ca(2+)-dependent exocytosis with release of mature IL1B (By similarity). 2. Secretory autophagy: IL1B-containing autophagosomes may fuse with endosomes or multivesicular bodies (MVBs) and then merge with the plasma membrane releasing soluble IL1B or IL1B-containing exosomes (By similarity). However, autophagy impacts IL1B production at several levels and its role in secretion is still controversial. 3. Secretion via exosomes: ATP-activation of P2RX7 leads to the formation of MVBs containing exosomes with entrapped IL1B, CASP1 and other inflammasome components. These MVBs undergo exocytosis with the release of exosomes. The release of soluble IL1B occurs after the lysis of exosome membranes (PubMed:17641058). 4. Secretion by microvesicle shedding: activation of the ATP receptor P2RX7 may induce an immediate shedding of membrane-derived microvesicles containing IL1B and possibly inflammasome components. The cytokine is then released in the extracellular compartment after microvesicle lysis (By similarity). 5. Release by translocation through permeabilized plasma membrane. This may occur in cells undergoing pyroptosis due to sustained activation of the inflammasome (PubMed:17284521). These mechanisms may not be not mutually exclusive. {ECO:0000250|UniProtKB:P01584, ECO:0000269|PubMed:17284521, ECO:0000269|PubMed:17641058}. SUBUNIT: Monomer. Interacts with MEFV. Interacts with integrins ITGAV:ITGBV and ITGA5:ITGB1; integrin-binding is required for IL1B signaling. {ECO:0000250|UniProtKB:P01584}. TISSUE SPECIFICITY: Expressed in activated macrophages (at protein level). {ECO:0000269|PubMed:16407890, ECO:0000269|PubMed:17284521, ECO:0000269|PubMed:17641058}. +Q8R459 IL1FA_MOUSE Interleukin-1 family member 10 (IL-1F10) 152 17,078 Chain (1) FUNCTION: Cytokine with immunomodulatory activity. Alone, does not induce cytokine production, but reduces IL22 and IL17A production by T-cells in response to heat-killed Candida albicans. Reduces IL36G-induced production of IL8 by peripheral blood mononuclear cells. Increases IL6 production by dendritic cells stimulated by bacterial lipopolysaccharides (LPS). Ligand for IL-36R/IL1RL2 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +P13504 IL1R1_MOUSE Interleukin-1 receptor type 1 (IL-1R-1) (IL-1RT-1) (IL-1RT1) (CD121 antigen-like family member A) (Interleukin-1 receptor alpha) (IL-1R-alpha) (Interleukin-1 receptor type I) (p80) (CD antigen CD121a) [Cleaved into: Interleukin-1 receptor type 1, membrane form (mIL-1R1) (mIL-1RI); Interleukin-1 receptor type 1, soluble form (sIL-1R1) (sIL-1RI)] 576 66,698 Alternative sequence (1); Chain (2); Disulfide bond (4); Domain (4); Glycosylation (7); Modified residue (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 339 359 Helical. {ECO:0000255}. TOPO_DOM 20 338 Extracellular. {ECO:0000255}.; TOPO_DOM 360 576 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for IL1A, IL1B and IL1RN. After binding to interleukin-1 associates with the coreceptor IL1RAP to form the high affinity interleukin-1 receptor complex which mediates interleukin-1-dependent activation of NF-kappa-B, MAPK and other pathways. Signaling involves the recruitment of adapter molecules such as TOLLIP, MYD88, and IRAK1 or IRAK2 via the respective TIR domains of the receptor/coreceptor subunits. Binds ligands with comparable affinity and binding of antagonist IL1RN prevents association with IL1RAP to form a signaling complex. Involved in IL1B-mediated costimulation of IFNG production from T-helper 1 (Th1) cells (By similarity). {ECO:0000250|UniProtKB:P14778}.; FUNCTION: Isoform 2: Unable to mediate canonical IL-1 signaling. Cooperates with IL1RAP isoform 3 to mediate IL1B-induced neuronal activity including IL1B-potentiated NMDA-induced calcium influx mediated by Akt kinase activation. {ECO:0000269|PubMed:22778412}. PTM: A soluble form (sIL1R1) is probably produced by proteolytic cleavage at the cell surface (shedding). {ECO:0000250}.; PTM: Rapidly phosphorylated on Tyr-499 in response to IL-1, which creates a SH2 binding site for the PI 3-kinase regulatory subunit PIK3R1. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. Cell membrane {ECO:0000305}. Secreted {ECO:0000250}. SUBUNIT: The interleukin-1 receptor complex is a heterodimer of IL1R1 and IL1RAP. Interacts with PIK3R1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Isoform 2 is expressed in various brain tissues. {ECO:0000269|PubMed:22778412}. +P27931 IL1R2_MOUSE Interleukin-1 receptor type 2 (IL-1R-2) (IL-1RT-2) (IL-1RT2) (CD121 antigen-like family member B) (IL-1 type II receptor) (Interleukin-1 receptor beta) (IL-1R-beta) (Interleukin-1 receptor type II) (CD antigen CD121b) [Cleaved into: Interleukin-1 receptor type 2, membrane form (mIL-1R2) (mIL-1RII); Interleukin-1 receptor type 2, soluble form (sIL-1R2) (sIL-1RII)] 410 45,645 Chain (2); Disulfide bond (4); Domain (3); Glycosylation (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 356 381 Helical. {ECO:0000255}. TOPO_DOM 14 355 Extracellular. {ECO:0000255}.; TOPO_DOM 382 410 Cytoplasmic. {ECO:0000255}. FUNCTION: Non-signaling receptor for IL1A, IL1B and IL1RN. Reduces IL1B activities. Serves as a decoy receptor by competetive binding to IL1B and preventing its binding to IL1R1. Also modulates cellular response through non-signaling association with IL1RAP after binding to IL1B. IL1R2 (membrane and secreted forms) preferentially binds IL1B and poorly IL1A and IL1RN. The secreted IL1R2 recruits secreted IL1RAP with high affinity; this complex formation may be the dominant mechanism for neutralization of IL1B by secreted/soluble receptors (By similarity). {ECO:0000250, ECO:0000269|PubMed:8332913, ECO:0000269|PubMed:9662436}. PTM: A soluble form (sIL1R2) can also be produced by proteolytic cleavage at the cell surface (shedding) involving a metalloproteinase. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. Cell membrane {ECO:0000250}. Secreted {ECO:0000250}. SUBUNIT: Associates with IL1RAP to form a non-signaling interleukin-1 receptor complex. {ECO:0000250}. TISSUE SPECIFICITY: Strongly expressed in B-cells, with levels 21 times higher than IL1R1. In T-cells expressed 5 times more compared with IL1R1. {ECO:0000269|PubMed:15986350}. +Q9JHX3 IL21R_MOUSE Interleukin-21 receptor (IL-21 receptor) (IL-21R) (Lymphocyte receptor beta) (LR-beta) (Novel cytokine receptor 8) (NR8) (Novel interleukin receptor) (CD antigen CD360) 529 58,355 Chain (1); Disulfide bond (3); Domain (2); Glycosylation (6); Motif (2); Natural variant (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 238 258 Helical. {ECO:0000255}. TOPO_DOM 20 237 Extracellular. {ECO:0000255}.; TOPO_DOM 259 529 Cytoplasmic. {ECO:0000255}. FUNCTION: This is a receptor for interleukin-21. PTM: C-mannosylated at Trp-214 in the WSXWS motif, the sugar chain makes extensive hydrogen bonds with Asn-73 sugar, and bridges the two fibronectin domains transforming the V-shaped receptor into an A-frame. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Heterodimer with the common gamma subunit. Associates with JAK1. DOMAIN: The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.; DOMAIN: The box 1 motif is required for JAK interaction and/or activation. TISSUE SPECIFICITY: Selectively expressed in lymphoid tissues. Most highly expressed in thymus and spleen. +Q8K4B4 IL23R_MOUSE Interleukin-23 receptor (IL-23 receptor) (IL-23R) 644 73,453 Chain (1); Domain (2); Glycosylation (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 375 395 Helical. {ECO:0000255}. TOPO_DOM 24 374 Extracellular. {ECO:0000255}.; TOPO_DOM 396 644 Cytoplasmic. {ECO:0000255}. FUNCTION: Associates with IL12RB1 to form the interleukin-23 receptor. Binds IL23 and mediates T-cells, NK cells and possibly certain macrophage/myeloid cells stimulation probably through activation of the Jak-Stat signaling cascade. IL23 functions in innate and adaptive immunity and may participate in acute response to infection in peripheral tissues. IL23 may be responsible for autoimmune inflammatory diseases and be important for tumorigenesis (By similarity). {ECO:0000250}. PTM: Phosphorylated in response to IL23. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Heterodimer with IL12RB1. In presence of IL23, the heterodimer forms the IL23 receptor. Interacts with JAK2 and in presence of IL23 with STAT3 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed by Th1, Th2 and dendritic cells. {ECO:0000269|PubMed:12023369}. +P34902 IL2RG_MOUSE Cytokine receptor common subunit gamma (Interleukin-2 receptor subunit gamma) (IL-2 receptor subunit gamma) (IL-2R subunit gamma) (IL-2RG) (gammaC) (p64) (CD antigen CD132) 369 42,241 Chain (1); Disulfide bond (2); Domain (1); Glycosylation (6); Motif (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 264 284 Helical. {ECO:0000255}. TOPO_DOM 23 263 Extracellular. {ECO:0000255}.; TOPO_DOM 285 369 Cytoplasmic. {ECO:0000255}. FUNCTION: Common subunit for the receptors for a variety of interleukins. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: The gamma subunit is common to the IL2, IL4, IL7, IL15, IL21 and probably also the IL13 receptors. Interacts with SHB upon interleukin stimulation (By similarity). {ECO:0000250}. DOMAIN: The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.; DOMAIN: The box 1 motif is required for JAK interaction and/or activation. +P70338 GFI1_MOUSE Zinc finger protein Gfi-1 (Growth factor independent protein 1) 423 45,944 Chain (1); Compositional bias (1); Modified residue (2); Mutagenesis (5); Region (2); Sequence conflict (2); Zinc finger (6) FUNCTION: Transcription repressor essential for hematopoiesis. Functions in a cell-context and development-specific manner. Binds to 5'-TAAATCAC[AT]GCA-3' in the promoter region of a large number of genes. Component of several complexes, including the EHMT2-GFI1-HDAC1, AJUBA-GFI1-HDAC1 and RCOR-GFI-KDM1A-HDAC complexes, that suppress, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. Regulates neutrophil differentiation, promotes proliferation of lymphoid cells, and is required for granulocyte development. Mediates, together with U2AF1L4, the alternative splicing of CD45 and controls T-cell receptor signaling. Regulates the endotoxin-mediated Toll-like receptor (TLR) inflammatory response by antagonizing RELA. Cooperates with CBFA2T2 to regulate ITGB1-dependent neurite growth. Controls cell-cycle progression by repressing CDKNIA/p21 transcription in response to TGFB1 via recruitment of GFI1 by ZBTB17 to the CDKNIA/p21 and CDKNIB promoters. Required for the maintenance of inner ear hair cells. {ECO:0000269|PubMed:12441305, ECO:0000269|PubMed:17197705, ECO:0000269|PubMed:17707228, ECO:0000269|PubMed:20547752, ECO:0000269|PubMed:8622900}. PTM: Ubiquitinated. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Note=Colocalizes with PIAS3 and RUNX1T1 in nuclear dots. {ECO:0000250}. SUBUNIT: Interacts (via the zinc-finger domain) with ARIH2; the interaction prevents GFI1 ubiquitination and proteasomal degradation. Forms a complex with EHMT2 and HDAC1 to promote 'Lys-9' dimethylation of H3 (H3K9Me2) and repress expression of target genes. Interacts directly with EHMT2. Interacts with RUNX1T1; the interaction represses HDAC-mediated transcriptional activity. Interacts (via the C-terminal zinc fingers) with ZBTB17; the interaction results in the recruitment of GFI1 to the CDKN1A/p21 and CDKNIB promoters and repression of transcription (By similarity). Interacts with U2AF1L4. Component of RCOR-GFI-KDM1A-HDAC complexes. Interacts directly with RCOR1, KDM1A and HDAC2. Also interacts with HDAC1. Component of the GFI1-AJUBA-HDAC1 repressor complex. Interacts directly with AJUBA (via its LIM domains); the interaction results in the HDAC-dependent corepression of a subset of GFI1 target genes and, occurs independently of the SNAG domain. Interacts with SPI1; the interaction inhibits SPI1 transcriptional activity and represses SPI1-regulated macrophage-specific genes required for proper granulocyte development. Interacts with PIAS3; the interaction relieves the inhibitory effect of PIAS3 on STAT3-mediated transcriptional activity. Interacts with RELA; the interaction occurs on liposaccharide (LPS) stimulation and controls RELA DNA binding activity and regulates endotoxin-mediated TOLL-like receptor inflammatory response. {ECO:0000250, ECO:0000269|PubMed:16819553, ECO:0000269|PubMed:17197705, ECO:0000269|PubMed:17707228}. DOMAIN: Zinc fingers 3,4 and 5 are required for DNA binding and for interaction with SPI1. {ECO:0000250}.; DOMAIN: The SNAG domain of GFIs is required for nuclear location and for interaction with some corepressors. {ECO:0000269|PubMed:17197705, ECO:0000269|PubMed:8887656}. +Q9WTN0 GGPPS_MOUSE Geranylgeranyl pyrophosphate synthase (GGPP synthase) (GGPPSase) (EC 2.5.1.-) ((2E,6E)-farnesyl diphosphate synthase) (Dimethylallyltranstransferase) (EC 2.5.1.1) (Farnesyl diphosphate synthase) (Farnesyltranstransferase) (EC 2.5.1.29) (Geranylgeranyl diphosphate synthase) (Geranyltranstransferase) (EC 2.5.1.10) 300 34,707 Binding site (10); Chain (1); Metal binding (5); Modified residue (1) Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis; farnesyl diphosphate from geranyl diphosphate and isopentenyl diphosphate: step 1/1. Isoprenoid biosynthesis; geranyl diphosphate biosynthesis; geranyl diphosphate from dimethylallyl diphosphate and isopentenyl diphosphate: step 1/1. Isoprenoid biosynthesis; geranylgeranyl diphosphate biosynthesis; geranylgeranyl diphosphate from farnesyl diphosphate and isopentenyl diphosphate: step 1/1. FUNCTION: Catalyzes the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate, an important precursor of carotenoids and geranylated proteins. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. SUBUNIT: Homohexamer; trimer of homodimers. {ECO:0000250}. +Q9CYH5 GFOD2_MOUSE Glucose-fructose oxidoreductase domain-containing protein 2 (EC 1.-.-.-) 385 42,242 Chain (1); Signal peptide (1) FUNCTION: Promotes matrix assembly. {ECO:0000269|PubMed:18757743}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:18757743}. +Q8R5F7 IFIH1_MOUSE Interferon-induced helicase C domain-containing protein 1 (EC 3.6.4.13) (Helicase with 2 CARD domains) (Helicard) (Interferon induced with helicase C domain protein 1) (Melanoma differentiation-associated protein 5) (MDA-5) (RIG-I-like receptor 2) (RLR-2) 1025 115,971 Alternative sequence (1); Chain (1); Domain (5); Erroneous initiation (1); Helix (6); Metal binding (4); Modified residue (6); Sequence conflict (9); Site (3) FUNCTION: Innate immune receptor which acts as a cytoplasmic sensor of viral nucleic acids and plays a major role in sensing viral infection and in the activation of a cascade of antiviral responses including the induction of type I interferons and proinflammatory cytokines. Its ligands include mRNA lacking 2'-O-methylation at their 5' cap and long-dsRNA (>1 kb in length). Upon ligand binding it associates with mitochondria antiviral signaling protein (MAVS/IPS1) which activates the IKK-related kinases: TBK1 and IKBKE which phosphorylate interferon regulatory factors: IRF3 and IRF7 which in turn activate transcription of antiviral immunological genes, including interferons (IFNs); IFN-alpha and IFN-beta. Responsible for detecting the Picornaviridae family members such as encephalomyocarditis virus (EMCV), mengo encephalomyocarditis virus (ENMG), and theiler's murine encephalomyelitis virus (TMEV). Can also detect other viruses such as dengue virus (DENV), west Nile virus (WNV), and reovirus. Also involved in antiviral signaling in response to viruses containing a dsDNA genome, such as vaccinia virus. Plays an important role in amplifying innate immune signaling through recognition of RNA metabolites that are produced during virus infection by ribonuclease L (RNase L). May play an important role in enhancing natural killer cell function and may be involved in growth inhibition and apoptosis in several tumor cell lines. {ECO:0000269|PubMed:12015121, ECO:0000269|PubMed:16625202, ECO:0000269|PubMed:17942531, ECO:0000269|PubMed:19656871, ECO:0000269|PubMed:21217758}. PTM: During apoptosis, processed into 3 cleavage products. The helicase-containing fragment, once liberated from the CARD domains, translocate from the cytoplasm to the nucleus. The processed protein significantly sensitizes cells to DNA degradation. {ECO:0000269|PubMed:12015121}.; PTM: Sumoylated. Sumoylation positively regulates its role in type I interferon induction and is enhanced by PIAS2-beta. {ECO:0000250|UniProtKB:Q9BYX4}.; PTM: Ubiquitinated by RNF125, leading to its degradation by the proteasome. USP17/UPS17L2-dependent deubiquitination positively regulates the receptor. Ubiquitinated by TRIM25 via 'Lys-63'-linked ubiquitination, promoting activation of IFIH1/MDA5. {ECO:0000250|UniProtKB:Q9BYX4}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12015121}. Nucleus {ECO:0000305}. Note=May be found in the nucleus, during apoptosis. SUBUNIT: Monomer in the absence of ligands and homodimerizes in the presence of dsRNA ligands. Can assemble into helical or linear polymeric filaments on long dsRNA. Interacts with MAVS/IPS1. Interacts with PCBP2. Interacts with NLRC5. Interacts with PIAS2-beta. Interacts with DDX60. Interacts with ANKRD17. Interacts with IKBKE. Interacts (via the CARD domains) with TKFC, the interaction is inhibited by viral infection (By similarity). Interacts with ATG5 and ATG12, either as ATG5 and ATG12 monomers or as ATG12-ATG5 conjugates (By similarity). Interacts with ZCCHC3; leading to activate IFIH1/MDA5 (By similarity). {ECO:0000250|UniProtKB:Q9BYX4}. TISSUE SPECIFICITY: Expression is prominent in lung, liver, kidney, heart and spleen (at protein level). Widely expressed at low level. {ECO:0000269|PubMed:12015121}. +Q64112 IFIT2_MOUSE Interferon-induced protein with tetratricopeptide repeats 2 (IFIT-2) (Glucocorticoid-attenuated response gene 39 protein) (GARG-39) (Interferon-induced 54 kDa protein) (IFI-54K) (P54) 472 55,021 Chain (1); Initiator methionine (1); Modified residue (1); Repeat (9); Sequence conflict (4) FUNCTION: IFN-induced antiviral protein which inhibits expression of viral messenger RNAs lacking 2'-O-methylation of the 5' cap. The ribose 2'-O-methylation would provide a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Viruses evolved several ways to evade this restriction system such as encoding their own 2'-O-methylase for their mRNAs or by stealing host cap containing the 2'-O-methylation (cap snatching mechanism). Binds AU-rich viral RNAs, with or without 5' triphosphorylation, RNA-binding is required for antiviral activity. Can promote apoptosis. {ECO:0000269|PubMed:21085181, ECO:0000269|PubMed:22615570}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. SUBUNIT: Domain-swapped homodimer. Component of an interferon-dependent multiprotein complex, at least composed of IFIT1, IFIT2 and IFIT3. Interacts with IFIT1 and IFIT3. Interacts with TMEM173/MITA and disrupts its interaction with MAVS or TBK1 (By similarity). Interacts with EIF3C. {ECO:0000250, ECO:0000269|PubMed:16023166}. DOMAIN: The C-terminal part folds into a super-helical structure and has an extensively positively-charged nucleotide-binding channel on its inner surface. {ECO:0000250}. +Q504N7 IFIXL_MOUSE Pyrin and HIN domain-containing protein 1-like 393 43,825 Alternative sequence (2); Chain (1); Domain (2); Sequence conflict (1) SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +Q8BV49 IFIX_MOUSE Pyrin and HIN domain-containing protein 1 (Interferon-inducible protein 209) (Ifi-209) (Interferon-inducible protein X) (Interferon-inducible protein p209) 420 46,887 Chain (1); Compositional bias (1); Domain (2); Sequence conflict (8) SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +Q9D103 IFM1_MOUSE Interferon-induced transmembrane protein 1 (Dispanin subfamily A member 2a) (DSPA2a) (Fragilis protein 2) (Mouse ifitm-like protein 2) (Mil-2) 106 11,524 Chain (1); Intramembrane (1); Lipidation (3); Sequence conflict (2); Topological domain (3); Transmembrane (1) INTRAMEM 36 56 Helical. {ECO:0000250|UniProtKB:P13164}. TRANSMEM 85 105 Helical. {ECO:0000255}. TOPO_DOM 1 35 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 57 84 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 106 106 Extracellular. {ECO:0000255}. FUNCTION: IFN-induced antiviral protein which inhibits the entry of viruses to the host cell cytoplasm, permitting endocytosis, but preventing subsequent viral fusion and release of viral contents into the cytosol. Active against multiple viruses, including influenza A virus, SARS coronavirus (SARS-CoV), Marburg virus (MARV), Ebola virus (EBOV), Dengue virus (DNV) and West Nile virus (WNV). Can inhibit: influenza virus hemagglutinin protein-mediated viral entry, MARV and EBOV GP1,2-mediated viral entry and SARS-CoV S protein-mediated viral entry. Also implicated in cell adhesion and control of cell growth and migration. Plays a key role in the antiproliferative action of IFN-gamma either by inhibiting the ERK activation or by arresting cell growth in G1 phase in a p53-dependent manner. Acts as a positive regulator of osteoblast differentiation. {ECO:0000269|PubMed:18505827, ECO:0000269|PubMed:21253575}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16326387}; Single-pass membrane protein {ECO:0000269|PubMed:16326387}. SUBUNIT: Interacts with CD81. Part of a complex composed of CD19, CR2/CD21, CD81 and IFITM1/CD225 in the membrane of mature B-cells. Interacts with CAV1; this interaction enhances the ability of CAV1 in inhibiting ERK activation. {ECO:0000250|UniProtKB:P13164}. TISSUE SPECIFICITY: Predominantly expressed in nascent primordial germ cells, as well as in gonadal germ cells. {ECO:0000269|PubMed:12659663}. +P07351 IFNA4_MOUSE Interferon alpha-4 (IFN-alpha-4) 186 21,524 Chain (1); Disulfide bond (2); Glycosylation (1); Signal peptide (1) FUNCTION: Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase. SUBCELLULAR LOCATION: Secreted. +Q61716 IFNAB_MOUSE Interferon alpha-11 (IFN-alpha-11) (Limitin) 190 21,736 Chain (1); Disulfide bond (2); Glycosylation (1); Sequence conflict (24); Signal peptide (1) FUNCTION: Has antiviral and antiproliferative activities (PubMed:15254193). Produced by macrophages and stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase (By similarity). During viral infection, mediates antiviral effect, either directly by inducing interferon-stimulated genes, either indirectly through stimulation of natural killer cells enabling them to control viral replication (PubMed:22912583). {ECO:0000250, ECO:0000269|PubMed:15254193, ECO:0000269|PubMed:22912583}. PTM: N-glygosylated (PubMed:15254193). {ECO:0000269|PubMed:15254193}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +Q9D6H2 IFT25_MOUSE Intraflagellar transport protein 25 homolog (Heat shock protein beta-11) (Hspb11) (Placental protein 25) (PP25) 143 16,281 Chain (1); Metal binding (3); Sequence conflict (1) FUNCTION: Component of the IFT complex B required for sonic hedgehog/SHH signaling. May mediate transport of SHH components: required for the export of SMO and PTCH1 receptors out of the cilium and the accumulation of GLI2 at the ciliary tip in response to activation of the SHH pathway, suggesting it is involved in the dynamic transport of SHH signaling molecules within the cilium. Not required for ciliary assembly (PubMed:22595669). Its role in intraflagellar transport is mainly seen in tissues rich in ciliated cells such as kidney and testis. Essential for male fertility, spermiogenesis and sperm flagella formation (PubMed:28430876). Plays a role in the early development of the kidney (PubMed:29626631). May be involved in the regulation of ureteric bud initiation (PubMed:29626631). {ECO:0000269|PubMed:22595669, ECO:0000269|PubMed:28430876, ECO:0000269|PubMed:29626631}. SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000269|PubMed:19253336}. SUBUNIT: Component of the IFT complex B, at least composed of IFT20, IFT22, HSPB11/IFT25, IFT27, IFT46, IFT52, TRAF3IP1/IFT54, IFT57, IFT74, IFT80, IFT81, and IFT88 (PubMed:19253336). Interacts with IFT27 (PubMed:28430876). Interacts with IFT88 (PubMed:19253336). {ECO:0000269|PubMed:19253336, ECO:0000269|PubMed:28430876}. TISSUE SPECIFICITY: Expressed predominantly in the testis (at protein level). {ECO:0000269|PubMed:28430876, ECO:0000269|PubMed:28964737}. +Q9DA69 IFT43_MOUSE Intraflagellar transport protein 43 homolog 206 23,501 Alternative sequence (2); Chain (1); Erroneous initiation (1); Modified residue (2) FUNCTION: As a component of IFT complex A (IFT-A), it is involved in ciliogenesis. Involved in retrograde ciliary transport along microtubules from the ciliary tip to the base. {ECO:0000250|UniProtKB:Q96FT9}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q96FT9}. Cell projection, cilium {ECO:0000269|PubMed:25243405}. Note=Associated with microtubules. Localized at the distal tip of the cilium. {ECO:0000250|UniProtKB:Q96FT9}. SUBUNIT: Component of the IFT complex A (IFT-A) complex. Interacts with WDR35/IFT121 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the retina, iris-ciliary body, lens and cornea. Higher expression is observed in the retina, predominantly in the photoreceptor outer segment. {ECO:0000269|PubMed:28973684}. +Q8BXG3 IFT57_MOUSE Intraflagellar transport protein 57 homolog (HIP1-interacting protein) 429 48,772 Alternative sequence (1); Chain (1); Coiled coil (1); Region (1); Sequence conflict (1) FUNCTION: Required for the formation of cilia. Plays an indirect role in sonic hedgehog signaling, cilia being required for all activity of the hedgehog pathway. Has pro-apoptotic function via its interaction with HIP1, leading to recruit caspase-8 (CASP8) and trigger apoptosis. Has the ability to bind DNA sequence motif 5'-AAAGACATG-3' present in the promoter of caspase genes such as CASP1, CASP8 and CASP10, suggesting that it may act as a transcription regulator; however the relevance of such function remains unclear. {ECO:0000269|PubMed:17027958}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body. Golgi apparatus. Note=Concentrates within the inner segment of cilia. SUBUNIT: Interacts with HIP1. In normal conditions, it poorly interacts with HIP1, HIP1 being strongly associated with HTT. However, in mutant HTT proteins with a long poly-Gln region, interaction between HTT and HIP1 is inhibited, promoting the interaction between HIP1 and IFT57, leading to apoptosis. Interacts with BFAR (By similarity). Component of the IFT complex B, at least composed of IFT20, IFT22, HSPB11/IFT25, IFT27, IFT46, IFT52, TRAF3IP1/IFT54, IFT57, IFT74, IFT80, IFT81, and IFT88. Interacts with IFT20 and IFT88. Interacts with BLOC1S2 and RYBP. Interacts with HOMER1, possibly leading to prevent pro-apoptotic effects of IFT57. Interacts with TTC25 (PubMed:25860617). {ECO:0000250, ECO:0000269|PubMed:11062270, ECO:0000269|PubMed:12821668, ECO:0000269|PubMed:17107665, ECO:0000269|PubMed:17874297, ECO:0000269|PubMed:18188704, ECO:0000269|PubMed:19253336, ECO:0000269|PubMed:25860617}. DOMAIN: The pseudo DED region (pDED) meadiates the interaction with HIP1. {ECO:0000250}. TISSUE SPECIFICITY: Present in retina and testis. In brain, it is present in the cortex, striatum, globus pallidus, hypothalamus and cerebellum. Present at high level in neurons and neuropil throughout the brain (at protein level). Expressed in hippocampal neurons, where it colocalizes with HOMER1 at postsynaptic regions. {ECO:0000269|PubMed:11788820, ECO:0000269|PubMed:11916979, ECO:0000269|PubMed:17107665}. +Q8BKE9 IFT74_MOUSE Intraflagellar transport protein 74 homolog (Capillary morphogenesis gene 1 protein) (CMG-1) (Coiled-coil domain-containing protein 2) 600 69,301 Chain (1); Coiled coil (1); Compositional bias (1); Erroneous initiation (1); Modified residue (2); Region (1) FUNCTION: Component of the intraflagellar transport (IFT) complex B: together with IFT81, forms a tubulin-binding module that specifically mediates transport of tubulin within the cilium. Binds beta-tubulin via its basic region. Required for ciliogenesis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000269|PubMed:16775004}. Cytoplasmic vesicle {ECO:0000250}. Note=Intracellular vesicular compartment. {ECO:0000250}. SUBUNIT: Component of the IFT complex B, at least composed of IFT20, IFT22, HSPB11/IFT25, IFT27, IFT46, IFT52, TRAF3IP1/IFT54, IFT57, IFT74, IFT80, IFT81, and IFT88 (PubMed:16775004). Interacts with IFT81; the interaction is direct: within the IFT complex B, IFT74 and IFT81 mediate the transport of tubulin within the cilium. Interacts (via basic region) with beta-tubulin (via acidic region); interaction is direct. Interacts with ARL13B and IFT88. Interacts (via the IFT74/IFT81 heterodimer) with RABL2B (By similarity). {ECO:0000250|UniProtKB:Q96LB3, ECO:0000269|PubMed:16775004}. +Q8K057 IFT80_MOUSE Intraflagellar transport protein 80 homolog (WD repeat-containing protein 56) 777 87,811 Alternative sequence (2); Chain (1); Erroneous initiation (1); Repeat (7) FUNCTION: Component of the intraflagellar transport (IFT) complex B, which is essential for the development and maintenance of motile and sensory cilia. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton, cilium basal body. Cytoplasm, cytoskeleton, cilium axoneme. Note=Basal body and ciliary axoneme in the chondrocytic ATDC-5 cell line. SUBUNIT: Component of the IFT complex B, at least composed of IFT20, IFT22, HSPB11/IFT25, IFT27, IFT46, IFT52, TRAF3IP1/IFT54, IFT57, IFT74, IFT80, IFT81, and IFT88. Interacts with IFT88. {ECO:0000269|PubMed:19253336}. +P03975 IGEB_MOUSE IgE-binding protein 557 62,747 Chain (1); Domain (1) +P05017 IGF1_MOUSE Insulin-like growth factor I (IGF-I) (Somatomedin) 153 17,093 Alternative sequence (1); Chain (1); Disulfide bond (3); Erroneous initiation (1); Propeptide (2); Region (4); Signal peptide (1) FUNCTION: The insulin-like growth factors, isolated from plasma, are structurally and functionally related to insulin but have a much higher growth-promoting activity. May be a physiological regulator of [1-14C]-2-deoxy-D-glucose (2DG) transport and glycogen synthesis in osteoblasts. Stimulates glucose transport in bone-derived osteoblastic (PyMS) cells and is effective at much lower concentrations than insulin, not only regarding glycogen and DNA synthesis but also with regard to enhancing glucose uptake. May play a role in synapse maturation (By similarity). Ca(2+)-dependent exocytosis of IGF1 is required for sensory perception of smell in the olfactory bulb (PubMed:21496647). Acts as a ligand for IGF1R. Binds to the alpha subunit of IGF1R, leading to the activation of the intrinsic tyrosine kinase activity which autophosphorylates tyrosine residues in the beta subunit thus initiatiating a cascade of down-stream signaling events leading to activation of the PI3K-AKT/PKB and the Ras-MAPK pathways. Binds to integrins ITGAV:ITGB3 and ITGA6:ITGB4. Its binding to integrins and subsequent ternary complex formation with integrins and IGFR1 are essential for IGF1 signaling. Induces the phosphorylation and activation of IGFR1, MAPK3/ERK1, MAPK1/ERK2 and AKT1 (By similarity). {ECO:0000250|UniProtKB:P05019, ECO:0000269|PubMed:21496647}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21496647}. SUBUNIT: Forms a ternary complex with IGFR1 and ITGAV:ITGB3. Forms a ternary complex with IGFR1 and ITGA6:ITGB4. {ECO:0000250|UniProtKB:P05019}. +P09535 IGF2_MOUSE Insulin-like growth factor II (IGF-II) (Multiplication-stimulating polypeptide) [Cleaved into: Insulin-like growth factor II; Preptin] 180 20,030 Alternative sequence (1); Chain (1); Disulfide bond (3); Peptide (1); Propeptide (1); Region (4); Signal peptide (1); Site (4) FUNCTION: The insulin-like growth factors possess growth-promoting activity (Probable). Major fetal growth hormone in mammals. Plays a key role in regulating fetoplacental development (Probable) (PubMed:2330056, PubMed:12087403). IGF-II is influenced by placental lactogen (Probable). Also involved in tissue differentiation (Probable). Positively regulates myogenic transcription factor MYOD1 function by facilitating the recruitment of transcriptional coactivators, thereby controlling muscle terminal differentiation (PubMed:16901893). In adults, involved in glucose metabolism in adipose tissue, skeletal muscle and liver (Probable). Acts as a ligand for integrin which is required for IGF2 signaling (By similarity). {ECO:0000250|UniProtKB:P01344, ECO:0000269|PubMed:12087403, ECO:0000269|PubMed:16901893, ECO:0000269|PubMed:2330056, ECO:0000305|PubMed:24593700, ECO:0000305|PubMed:28522536}.; FUNCTION: Preptin undergoes glucose-mediated co-secretion with insulin, and acts as physiological amplifier of glucose-mediated insulin secretion. Exhibits osteogenic properties by increasing osteoblast mitogenic activity through phosphoactivation of MAPK1 and MAPK3. {ECO:0000269|PubMed:16912056}. PTM: Proteolytically processed by PCSK4, proIGF2 is cleaved at Arg-128 and Arg-92 to generate big-IGF2 and mature IGF2. {ECO:0000250|UniProtKB:P01344}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28522536}. SUBUNIT: Interacts with MYORG; this interaction is required for IGF2 secretion (PubMed:19706595). Interacts with integrins ITGAV:ITGB3 and ITGA6:ITGB4; integrin-binding is required for IGF2 signaling (By similarity). {ECO:0000250|UniProtKB:P01344, ECO:0000269|PubMed:19706595}. +P01837 IGKC_MOUSE Immunoglobulin kappa constant (Ig kappa chain C region MOPC 21) 107 11,934 Beta strand (9); Chain (1); Disulfide bond (2); Domain (1); Helix (3); Non-terminal residue (1); Turn (1) +P15105 GLNA_MOUSE Glutamine synthetase (GS) (EC 6.3.1.2) (Glutamate--ammonia ligase) (Palmitoyltransferase GLUL) (EC 2.3.1.225) 373 42,120 Binding site (5); Chain (1); Initiator methionine (1); Metal binding (6); Modified residue (3); Nucleotide binding (3); Region (1); Sequence conflict (7) FUNCTION: Glutamine synthetase that catalyzes the ATP-dependent conversion of glutamate and ammonia to glutamine (By similarity). Its role depends on tissue localization: in the brain, it regulates the levels of toxic ammonia and converts neurotoxic glutamate to harmless glutamine, whereas in the liver, it is one of the enzymes responsible for the removal of ammonia (PubMed:25870278). Essential for proliferation of fetal skin fibroblasts (By similarity). Independently of its glutamine synthetase activity, required for endothelial cell migration during vascular development (PubMed:30158707). Involved in angiogenesis by regulating membrane localization and activation of the GTPase RHOJ, possibly by promoting RHOJ palmitoylation (By similarity). May act as a palmitoyltransferase for RHOJ: able to autopalmitoylate and then transfer the palmitoyl group to RHOJ (By similarity). {ECO:0000250|UniProtKB:P15104, ECO:0000269|PubMed:25870278, ECO:0000269|PubMed:30158707}. PTM: Palmitoylated; undergoes autopalmitoylation. {ECO:0000250|UniProtKB:P15104}.; PTM: Ubiquitinated by ZNRF1. {ECO:0000269|PubMed:20107048}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P15104}. Microsome {ECO:0000250|UniProtKB:P09606}. Mitochondrion {ECO:0000250|UniProtKB:P09606}. Cell membrane {ECO:0000250|UniProtKB:P15104}; Lipid-anchor {ECO:0000250|UniProtKB:P15104}. Note=Mainly localizes in the cytosol, with a fraction associated with the cell membrane. {ECO:0000250|UniProtKB:P15104}. SUBUNIT: Decamer; composed of two pentamers (By similarity). Interacts with PALMD (PubMed:16323283). Interacrts with RHOJ (By similarity). {ECO:0000250|UniProtKB:P15104, ECO:0000269|PubMed:16323283}. TISSUE SPECIFICITY: Expressed in microvascular endothelial cells. {ECO:0000269|PubMed:30158707}. +Q91WR8 GPX6_MOUSE Glutathione peroxidase 6 (GPx-6) (GSHPx-6) (EC 1.11.1.9) 221 24,903 Active site (1); Chain (1); Sequence conflict (2); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +Q61500 ITM2A_MOUSE Integral membrane protein 2A (Protein E25) 263 29,691 Chain (1); Disulfide bond (1); Domain (1); Glycosylation (1); Sequence conflict (1); Transmembrane (1) TRANSMEM 54 74 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in mandibular condyles, in bone and in hair follicles. Strong expression in osteogenic tissues, such as neonatal calvaria, paws, tail and skin. +Q3TFK5 GPTC4_MOUSE G patch domain-containing protein 4 415 46,554 Alternative sequence (1); Chain (1); Cross-link (1); Domain (1); Frameshift (1); Modified residue (5); Sequence conflict (3) +P46412 GPX3_MOUSE Glutathione peroxidase 3 (GPx-3) (GSHPx-3) (EC 1.11.1.9) (Plasma glutathione peroxidase) (GPx-P) (GSHPx-P) 226 25,424 Active site (1); Chain (1); Non-standard residue (1); Sequence conflict (3); Signal peptide (1) FUNCTION: Protects cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Homotetramer. TISSUE SPECIFICITY: Secreted in plasma. +Q9DAG6 GPRL1_MOUSE GLIPR1-like protein 1 236 27,074 Chain (1); Domain (1); Glycosylation (1); Signal peptide (1) FUNCTION: Plays a role in the binding between sperm and oocytes (PubMed:20219979). Component of epididymosomes, one type of membranous microvesicules which mediate the transfer of lipids and proteins to spermatozoa plasma membrane during epididymal maturation. Also component of the CD9-positive microvesicules found in the cauda region. {ECO:0000250|UniProtKB:Q32LB5, ECO:0000269|PubMed:20219979}. PTM: N-glycosylated (PubMed:20219979). N-glycosylation decreases during the transit in the caput. {ECO:0000250|UniProtKB:Q32LB5, ECO:0000269|PubMed:20219979}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:20219979}. Cell membrane {ECO:0000305|PubMed:20219979}; Peripheral membrane protein {ECO:0000305|PubMed:20219979}; Extracellular side {ECO:0000305|PubMed:20219979}. Membrane raft {ECO:0000250|UniProtKB:Q32LB5}. Secreted {ECO:0000269|PubMed:20219979}. Note=Located in the connecting piece of elongated spermatids and sperm (PubMed:20219979). Also located in the apical region of the sperm head after sperm capacitation (PubMed:20219979). Weakly attached to the cell membrane and later secreted into the extracellular space (PubMed:20219979). Located on sperm equatorial segment and neck (By similarity). Associated with epididymosomes from the caput and cauda epididymis (By similarity). {ECO:0000250|UniProtKB:Q32LB5, ECO:0000269|PubMed:20219979}. TISSUE SPECIFICITY: Expressed in testis (at protein level). Little or no expression in other tissues tested. {ECO:0000269|PubMed:20219979}. +Q3TYR5 GRCR2_MOUSE Glutaredoxin domain-containing cysteine-rich protein 2 (GRXCR1-like protein) (Glutaredoxin domain-containing cysteine-rich protein 1-like protein) 254 28,601 Chain (1) FUNCTION: Could play a role in maintaining cochlear stereocilia bundles that are involved in sound detection. {ECO:0000250}. SUBCELLULAR LOCATION: Cell projection, stereocilium {ECO:0000269|Ref.3}. TISSUE SPECIFICITY: Expressed in sensory hair cells in the cochlea and vestibular organ. {ECO:0000269|Ref.3}. +Q60631 GRB2_MOUSE Growth factor receptor-bound protein 2 (Adapter protein GRB2) (SH2/SH3 adapter GRB2) 217 25,238 Alternative sequence (1); Beta strand (6); Chain (1); Domain (3); Helix (1); Modified residue (5) FUNCTION: Adapter protein that provides a critical link between cell surface growth factor receptors and the Ras signaling pathway.; FUNCTION: Isoform 2 does not bind to phosphorylated epidermal growth factor receptor (EGFR) but inhibits EGF-induced. transactivation of a RAS-responsive element. Isoform 2 acts as a dominant negative protein over GRB2 and by suppressing proliferative signals, may trigger active programmed cell death (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Endosome {ECO:0000250}. Golgi apparatus {ECO:0000269|PubMed:11571277}. SUBUNIT: Associates (via SH2 domain) with activated EGF and PDGF receptors (tyrosine phosphorylated) (By similarity). Interacts with PDGFRA (tyrosine phosphorylated); the interaction may be indirect (PubMed:8943348). Interacts with IRS4 (when Tyr-phosphorylated) (PubMed:11113178). Also associates to other cellular Tyr-phosphorylated proteins such as SIT1, IRS1, SHC and LNK; probably via the concerted action of both its SH2 and SH3 domains (By similarity). It also seems to interact with RAS in the signaling pathway leading to DNA synthesis. Interacts with SOS1 (By similarity). Forms a complex with MUC1 and SOS1, through interaction of the SH3 domains with SOS1 and the SH2 domain with phosphorylated MUC1 (By similarity). Interacts with phosphorylated MET (By similarity). Interacts with phosphorylated TOM1L1 (PubMed:11711534). Interacts with the phosphorylated C-terminus of SH2B2 (By similarity). Interacts with phosphorylated SIT1, LAX1, LAT, LAT2 and LIME1 upon TCR and/or BCR activation (By similarity) (PubMed:16249387, PubMed:14610044, PubMed:15477350, PubMed:15477348, PubMed:22561606). Interacts with NISCH, PTPNS1 and REPS2 (By similarity). Interacts with syntrophin SNTA1 (PubMed:11551227). Interacts (via SH3 domains) with REPS1 (PubMed:9395447). Interacts (via SH3 domains) with PIK3C2B (By similarity). Interacts with CBL and CBLB (By similarity). Interacts with AJUBA and CLNK (PubMed:10330178, PubMed:11463797). Interacts (via SH2 domain) with TEK/TIE2 (tyrosine phosphorylated) (PubMed:10521483). Interacts with SHB, INPP5D/SHIP1, SKAP1 and SKAP2 (By similarity). Interacts with PTPN11 (PubMed:8943348). Interacts with PRNP (PubMed:11571277). Interacts with RALGPS1 (By similarity). Interacts also with HCST (PubMed:16582911). Interacts with KDR (PubMed:16966330). Interacts with FLT1 (tyrosine-phosphorylated) (PubMed:9722576). Interacts with GAPT and PTPRE (By similarity). Interacts (via SH2 domain) with KIF26A (By similarity). Interacts (via SH3 2) with GAB2 (PubMed:10068651). Interacts with ADAM15 (By similarity). Interacts with THEMIS2 (PubMed:20644716). Interacts (via SH2 domain) with AXL (phosphorylated) (By similarity). Interacts (via SH2 domain) with KIT (phosphorylated) (PubMed:10377264). Interacts with PTPRJ and BCR (By similarity). Interacts with PTPN23 (By similarity). Interacts with FLT4 (tyrosine phosphorylated) (By similarity). Interacts with EPHB1 and SHC1; activates the MAPK/ERK cascade to regulate cell migration (PubMed:12925710). Part of a complex including TNK2, GRB2 and one receptor tyrosine kinase (RTK) such as AXL and PDGFRL, in which GRB2 promotes RTK recruitment by TNK2 (By similarity). Interacts (via SH2 domain) with CSF1R (tyrosine phosphorylated) (PubMed:9312046). Interacts with ERBB4 (By similarity). Interacts with NTRK1 (phosphorylated upon ligand-binding) (By similarity). Interacts with PTK2/FAK1 (tyrosine phosphorylated) (PubMed:7997267). Interacts with PTK2B/PYK2 (tyrosine phosphorylated) (By similarity). Interacts with SCIMP (PubMed:21930792). Interacts (via SH3 domains) with GAREM1 (via proline-rich domain and tyrosine phosphorylated); the interaction occurs upon EGF stimulation (By similarity). Interacts with DAB2 (PubMed:9569023). Interacts with TESPA1 (By similarity). Interacts with THEMIS (PubMed:19597498, PubMed:19597497, PubMed:19805304, PubMed:22561606). Interacts with PLCG1, LAT and THEMIS upon TCR activation in thymocytes; the association is weaker in the absence of TESPA1 (PubMed:22561606). Interacts with CD28 (By similarity). Interacts with RAB13; may recruit RAB13 to the leading edge of migrating endothelial cells where it can activate RHOA (PubMed:21543326). Interacts with ASAP3 (phosphorylated form) (By similarity). Interacts (via SH2 domain) with PTPRH (phosphorylated form) (PubMed:20398064). Interacts with PTPRO (phosphorylated form) (PubMed:20398064). Interacts with PTPRB (phosphorylated form) (PubMed:20398064). Interacts (via SH3 domain 2) with PRR14 (via proline-rich region) (By similarity). {ECO:0000250|UniProtKB:P62993, ECO:0000269|PubMed:10068651, ECO:0000269|PubMed:10330178, ECO:0000269|PubMed:10377264, ECO:0000269|PubMed:10521483, ECO:0000269|PubMed:11113178, ECO:0000269|PubMed:11463797, ECO:0000269|PubMed:11551227, ECO:0000269|PubMed:11571277, ECO:0000269|PubMed:11711534, ECO:0000269|PubMed:12925710, ECO:0000269|PubMed:14610044, ECO:0000269|PubMed:15477348, ECO:0000269|PubMed:15477350, ECO:0000269|PubMed:16249387, ECO:0000269|PubMed:16582911, ECO:0000269|PubMed:16966330, ECO:0000269|PubMed:19597497, ECO:0000269|PubMed:19597498, ECO:0000269|PubMed:19805304, ECO:0000269|PubMed:20398064, ECO:0000269|PubMed:20644716, ECO:0000269|PubMed:21543326, ECO:0000269|PubMed:21930792, ECO:0000269|PubMed:22561606, ECO:0000269|PubMed:7997267, ECO:0000269|PubMed:8943348, ECO:0000269|PubMed:9312046, ECO:0000269|PubMed:9395447, ECO:0000269|PubMed:9569023, ECO:0000269|PubMed:9722576}. DOMAIN: The SH3 domains mediate interaction with RALGPS1 and SHB. {ECO:0000250}. +O88273 GREM2_MOUSE Gremlin-2 (Cysteine knot superfamily 1, BMP antagonist 2) (Protein related to DAN and cerberus) (PRDC) 168 19,334 Beta strand (6); Chain (1); Disulfide bond (4); Domain (1); Glycosylation (2); Helix (3); Mutagenesis (8); Signal peptide (1) FUNCTION: Cytokine that inhibits the activity of BMP2 and BMP4 in a dose-dependent manner, and thereby modulates signaling by BMP family members. Contributes to the regulation of embryonic morphogenesis via BMP family members. Antagonizes BMP4-induced suppression of progesterone production in granulosa cells. {ECO:0000269|PubMed:15039429, ECO:0000269|PubMed:23063586, ECO:0000269|PubMed:23850456}. PTM: N-glycosylated. {ECO:0000269|PubMed:23063586}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. SUBUNIT: Homodimer. Interacts with BMP2, BMP4 and BMP7, but has lower affinity for BMP7 than for BMP2 and BMP4. Binds heparin; this impairs the interaction with BMP2. {ECO:0000269|PubMed:15039429, ECO:0000269|PubMed:23063586, ECO:0000269|PubMed:23850456}. TISSUE SPECIFICITY: Highly expressed in the ovary, followed by brain, spleen, colon, kidney and uterus. In ovary expressed in granulosa cells of selective early antral follicles. {ECO:0000269|PubMed:15039429}. +Q6PEM6 GRM2B_MOUSE GRAM domain-containing protein 2B (GRAM domain-containing protein 3) 445 49,272 Chain (1); Domain (1); Modified residue (4); Sequence conflict (1) +Q61625 GRID2_MOUSE Glutamate receptor ionotropic, delta-2 (GluD2) (GluR delta-2 subunit) 1007 113,082 Chain (1); Disulfide bond (3); Glycosylation (2); Modified residue (4); Motif (1); Mutagenesis (1); Natural variant (1); Region (2); Signal peptide (1); Site (1); Topological domain (4); Transmembrane (3) TRANSMEM 567 587 Helical. {ECO:0000255}.; TRANSMEM 636 656 Helical. {ECO:0000255}.; TRANSMEM 831 851 Helical. {ECO:0000255}. TOPO_DOM 24 566 Extracellular. {ECO:0000255}.; TOPO_DOM 588 635 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 657 830 Extracellular. {ECO:0000255}.; TOPO_DOM 852 1007 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for glutamate. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists. Promotes synaptogenesis and mediates the D-Serine-dependent long term depression signals and AMPA receptor endocytosis of cerebellar parallel fiber-Purkinje cell (PF-PC) synapses through the beta-NRX1-CBLN1-GRID2 triad complex. {ECO:0000250|UniProtKB:O43424}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Tetramer; dimer of dimers (By similarity). Interacts with EML2, MAGI2 (via PDZ domains) and AP4M1 (By similarity). Interacts with BECN1, GOPC, GRID2IP, SHANK1 and SHANK2 (PubMed:12372286, PubMed:15207857, PubMed:17027646). Interacts with CBLN2, but not with CBLN4 (PubMed:22220752). Interacts with CBLN1 (via C1q domain); the interaction is CBLN1-NRX1 complex formation-dependent; CBLN1-binding is calcium-independent; CBLN1 hexamers anchor GRID2 N-terminal domain dimers to monomeric NRXN1 isoform beta; promotes synaptogenesis and mediates the D-Serine-dependent long term depression signals and AMPA receptor endocytosis (PubMed:20395510, PubMed:21410790, PubMed:22220752). {ECO:0000250|UniProtKB:O43424, ECO:0000250|UniProtKB:Q63226, ECO:0000269|PubMed:12372286, ECO:0000269|PubMed:15207857, ECO:0000269|PubMed:17027646, ECO:0000269|PubMed:20395510, ECO:0000269|PubMed:21410790, ECO:0000269|PubMed:22220752}. DOMAIN: The PDZ-binding motif mediates interaction with GOPC. {ECO:0000269|PubMed:12372286}. TISSUE SPECIFICITY: Expressed selectively in cerebellar Purkinje cells where it is localized in dendritic spines. {ECO:0000269|PubMed:15207857, ECO:0000269|PubMed:7506541}. DISEASE: Note=Defects in Grid2 are the cause of the Lurcher phenotype. Heterozygous animals display a characteristic swaying of the hind quarters and jerky up and down movements following cerebellar Purkinje cell degeneration during postnatal development. Homozygous animals die shortly after birth because of a massive loss of midbrain and hindbrain neurons during late embryogenesis. +Q9D1U0 GRIFN_MOUSE Grifin (Galectin-related inter-fiber protein) 144 15,971 Chain (1); Domain (1); Modified residue (1) SUBUNIT: Homodimer. {ECO:0000250}. DOMAIN: The galectin domain is atypical and does not bind beta-galactoside sugars. {ECO:0000250}. +Q8VEB1 GRK5_MOUSE G protein-coupled receptor kinase 5 (EC 2.7.11.16) (G protein-coupled receptor kinase GRK5) 590 67,732 Active site (1); Binding site (1); Chain (1); Domain (3); Modified residue (4); Motif (1); Nucleotide binding (1); Region (3); Sequence conflict (4) FUNCTION: Serine/threonine kinase that phosphorylates preferentially the activated forms of a variety of G-protein-coupled receptors (GPCRs). Such receptor phosphorylation initiates beta-arrestin-mediated receptor desensitization, internalization, and signaling events leading to their down-regulation. Phosphorylates a variety of GPCRs, including adrenergic receptors, muscarinic acetylcholine receptors (more specifically Gi-coupled M2/M4 subtypes), dopamine receptors and opioid receptors. In addition to GPCRs, also phosphorylates various substrates: Hsc70-interacting protein/ST13, TP53/p53, HDAC5, and arrestin-1/ARRB1. Phosphorylation of ARRB1 by GRK5 inhibits G-protein independent MAPK1/MAPK3 signaling downstream of 5HT4-receptors. Phosphorylation of HDAC5, a repressor of myocyte enhancer factor 2 (MEF2) leading to nuclear export of HDAC5 and allowing MEF2-mediated transcription. Phosphorylation of TP53/p53, a crucial tumor suppressor, inhibits TP53/p53-mediated apoptosis. Phosphorylation of ST13 regulates internalization of the chemokine receptor. Phosphorylates rhodopsin (RHO) (in vitro) and a non G-protein-coupled receptor, LRP6 during Wnt signaling (in vitro). {ECO:0000269|PubMed:10624964, ECO:0000269|PubMed:14565944, ECO:0000269|PubMed:18711143, ECO:0000269|PubMed:19478075}. PTM: Autophosphorylated. Autophosphorylation may play a critical role in the regulation of GRK5 kinase activity. {ECO:0000250|UniProtKB:P34947}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus. Cell membrane; Peripheral membrane protein. Note=Predominantly localized at the plasma membrane, targeted to the cell surface through the interaction with phospholipids. Nucleus localization is regulated in a GPCR and Ca(2+)/calmodulin-dependent fashion (By similarity). {ECO:0000250}. SUBUNIT: Interacts with ST13 (via the C-terminus 303-319 AA) (By similarity). Interacts with TP53/p53 (By similarity). Interacts with HTR4 (via C-terminus 330-346 AA); this interaction is promoted by 5-HT (serotonin) (By similarity). Interacts with HDAC5. {ECO:0000250, ECO:0000269|PubMed:18711143}. +Q8K5C0 GRHL2_MOUSE Grainyhead-like protein 2 homolog (Brother of mammalian grainyhead) (Transcription factor CP2-like 3) 625 71,195 Chain (1); Region (1); Site (1) FUNCTION: Transcription factor playing an important role in primary neurulation and in epithelial development. Binds directly to the consensus DNA sequence 5'-AACCGGTT-3' acting as an activator and repressor on distinct target genes (PubMed:22696678). During embryogenesis, plays unique and cooperative roles with GRHL3 in establishing distinct zones of primary neurulation. Essential for closure 3 (rostral end of the forebrain), functions cooperatively with GRHL3 in closure 2 (forebrain/midbrain boundary) and posterior neuropore closure (PubMed:20654612). Regulates epithelial morphogenesis acting as a target gene-associated transcriptional activator of apical junctional complex components. Up-regulates of CLDN3 and CLDN4, as well as of RAB25, which increases the CLDN4 protein and its localization at tight junctions (PubMed:22696678). Comprises an essential component of the transcriptional machinery that establishes appropriate expression levels of CLDN4 and CDH1 in different types of epithelia (PubMed:20978075). Exhibits functional redundancy with GRHL3 in epidermal morphogenetic events such as eyelid fusion and epidermal wound repair (PubMed:21081122). In lung, forms a regulatory loop with NKX2-1 that coordinates lung epithelial cell morphogenesis and differentiation (PubMed:22955271). In keratinocytes, plays a role in telomerase activation during cellular proliferation, regulates TERT expression by binding to TERT promoter region and inhibiting DNA methylation at the 5'-CpG island, possibly by interfering with DNMT1 enzyme activity. In addition, impairs keratinocyte differentiation and epidermal function by inhibiting the expression of genes clustered at the epidermal differentiation complex (EDC) as well as GRHL1 and GRHL3 through epigenetic mechanisms (By similarity). {ECO:0000250|UniProtKB:Q6ISB3, ECO:0000269|PubMed:20654612, ECO:0000269|PubMed:20978075, ECO:0000269|PubMed:21081122, ECO:0000269|PubMed:22696678, ECO:0000269|PubMed:22955271}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20978075, ECO:0000269|PubMed:22696678}. Membrane {ECO:0000250|UniProtKB:Q6ISB3}. Note=detected at cell-cell contact areas. {ECO:0000250|UniProtKB:Q6ISB3}. SUBUNIT: Homodimer, also forms heterodimers with GRHL1 or GRHL3. {ECO:0000250|UniProtKB:Q6ISB3}. +P23818 GRIA1_MOUSE Glutamate receptor 1 (GluR-1) (AMPA-selective glutamate receptor 1) (GluR-A) (GluR-K1) (Glutamate receptor ionotropic, AMPA 1) (GluA1) 907 101,569 Binding site (3); Chain (1); Disulfide bond (2); Glycosylation (6); Intramembrane (2); Lipidation (2); Modified residue (4); Motif (1); Mutagenesis (1); Region (2); Signal peptide (1); Topological domain (5); Transmembrane (3) INTRAMEM 585 600 Helical; Pore-forming. {ECO:0000250}.; INTRAMEM 601 603 {ECO:0000250}. TRANSMEM 537 557 Helical. {ECO:0000250}.; TRANSMEM 610 630 Helical. {ECO:0000250}.; TRANSMEM 806 826 Helical; Name=M4. {ECO:0000250}. TOPO_DOM 19 536 Extracellular. {ECO:0000250}.; TOPO_DOM 558 584 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 604 609 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 631 805 Extracellular. {ECO:0000250}.; TOPO_DOM 827 907 Cytoplasmic. {ECO:0000250}. FUNCTION: Ionotropic glutamate receptor. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. In the presence of CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of glutamate. PTM: Palmitoylated. Depalmitoylated upon glutamate stimulation. ZDHHC3/GODZ specifically palmitoylates Cys-603, which leads to Golgi retention and decreased cell surface expression. In contrast, Cys-829 palmitoylation does not affect cell surface expression but regulates stimulation-dependent endocytosis. {ECO:0000269|PubMed:16129400}.; PTM: Phosphorylated at Ser-645. Phosphorylated at Ser-710 by PKC. Phosphorylated at Ser-849 by PKC, PKA and CAMK2. Phosphorylated at Ser-863 by PKC, PKA and PRKG2. {ECO:0000250|UniProtKB:P19490}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21172611}; Multi-pass membrane protein {ECO:0000269|PubMed:21172611}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P19490}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P19490}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000269|PubMed:21172611}; Multi-pass membrane protein {ECO:0000269|PubMed:21172611}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000269|PubMed:21172611}; Multi-pass membrane protein {ECO:0000305}. Cell projection, dendrite {ECO:0000269|PubMed:21172611}. Cell projection, dendritic spine {ECO:0000269|PubMed:21172611}. Early endosome membrane {ECO:0000250|UniProtKB:P19490}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P19490}. Recycling endosome membrane {ECO:0000250|UniProtKB:P19490}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P19490}. Note=Interaction with CACNG2, CNIH2 and CNIH3 promotes cell surface expression. Colocalizes with PDLIM4 in early endosomes. Displays a somatodendritic localization and is excluded from axons in neurons (PubMed:18341993). {ECO:0000250|UniProtKB:P19490, ECO:0000269|PubMed:18341993}. SUBUNIT: Homotetramer or heterotetramer of pore-forming glutamate receptor subunits (By similarity). Tetramers may be formed by the dimerization of dimers (By similarity). Interacts with HIP1 and RASGRF2 (PubMed:12839988, PubMed:16407208). Interacts with SYNDIG1 and GRIA2 (PubMed:20152115). Interacts with DLG1 (via C-terminus). Interacts with LRFN1. Interacts with PRKG2. Interacts with CNIH2 and CACNG2. Interacts with CACNG5. Interacts (via C-terminus) with PDLIM4 (via LIM domain); this interaction as well as the interaction of PDLIM4 with alpha-actinin is required for their colocalization in early endosomes. Found in a complex with GRIA2, GRIA3, GRIA4, CNIH2, CNIH3, CACNG2, CACNG3, CACNG4, CACNG5, CACNG7 and CACNG8 (By similarity). Interacts with SNX27 (via PDZ domain); the interaction is required for recycling to the plasma membrane when endocytosed and prevent degradation in lysosomes (PubMed:23524343). Interacts (via PDZ-binding motif) with SHANK3 (via PDZ domain) (PubMed:16606358). Interacts with CACNG3; associates GRIA1 with the adaptor protein complex 4 (AP-4) to target GRIA1 to the somatodendritic compartment of neurons (PubMed:18341993). {ECO:0000250|UniProtKB:P19490, ECO:0000250|UniProtKB:P42261, ECO:0000269|PubMed:12839988, ECO:0000269|PubMed:16407208, ECO:0000269|PubMed:16606358, ECO:0000269|PubMed:18341993, ECO:0000269|PubMed:20152115, ECO:0000269|PubMed:23524343}. DOMAIN: The M4 transmembrane segment mediates tetramerization and is required for cell surface expression. {ECO:0000250}. +Q8BMF5 GRIK4_MOUSE Glutamate receptor ionotropic, kainate 4 (GluK4) 956 107,264 Chain (1); Compositional bias (1); Glycosylation (8); Sequence conflict (2); Signal peptide (1); Topological domain (4); Transmembrane (3) TRANSMEM 546 566 Helical. {ECO:0000255}.; TRANSMEM 624 644 Helical. {ECO:0000255}.; TRANSMEM 805 825 Helical. {ECO:0000255}. TOPO_DOM 21 545 Extracellular. {ECO:0000255}.; TOPO_DOM 567 623 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 645 804 Extracellular. {ECO:0000255}.; TOPO_DOM 826 956 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for glutamate. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists. This receptor binds kainate > quisqualate > glutamate >> AMPA (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Forms a heteromeric channel with GRIK1 or GRIK3. {ECO:0000250}. +Q14B48 ITPI1_MOUSE Protein ITPRID1 (Coiled-coil domain-containing protein 129) (ITPR-interacting domain-containing protein 1) 1034 115,605 Alternative sequence (1); Chain (1); Coiled coil (1); Erroneous initiation (1) +P11881 ITPR1_MOUSE Inositol 1,4,5-trisphosphate receptor type 1 (IP3 receptor isoform 1) (IP3R 1) (InsP3R1) (Inositol 1,4,5-trisphosphate-binding protein P400) (Protein PCD-6) (Purkinje cell protein 1) (Type 1 inositol 1,4,5-trisphosphate receptor) (Type 1 InsP3 receptor) 2749 313,167 Alternative sequence (4); Beta strand (29); Chain (1); Cross-link (11); Domain (5); Erroneous initiation (2); Helix (17); Lipidation (2); Modified residue (4); Mutagenesis (15); Region (4); Sequence conflict (2); Topological domain (7); Transmembrane (6); Turn (6) TRANSMEM 2274 2294 Helical. {ECO:0000255}.; TRANSMEM 2306 2326 Helical. {ECO:0000255}.; TRANSMEM 2353 2373 Helical. {ECO:0000255}.; TRANSMEM 2397 2417 Helical. {ECO:0000255}.; TRANSMEM 2440 2460 Helical. {ECO:0000255}.; TRANSMEM 2570 2590 Helical. {ECO:0000255}. TOPO_DOM 1 2273 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 2295 2305 Lumenal. {ECO:0000255}.; TOPO_DOM 2327 2352 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 2374 2396 Lumenal. {ECO:0000255}.; TOPO_DOM 2418 2439 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 2461 2569 Lumenal. {ECO:0000255}.; TOPO_DOM 2591 2749 Cytoplasmic. {ECO:0000255}. FUNCTION: Intracellular channel that mediates calcium release from the endoplasmic reticulum following stimulation by inositol 1,4,5-trisphosphate. Involved in the regulation of epithelial secretion of electrolytes and fluid through the interaction with AHCYL1 (PubMed:23542070). Plays a role in ER stress-induced apoptosis. Cytoplasmic calcium released from the ER triggers apoptosis by the activation of CaM kinase II, eventually leading to the activation of downstream apoptosis pathways. {ECO:0000269|PubMed:19752026, ECO:0000269|PubMed:20813840, ECO:0000269|PubMed:23542070, ECO:0000269|PubMed:2554142}. PTM: Phosphorylated by cAMP kinase (PKA). Phosphorylation prevents the ligand-induced opening of the calcium channels. Phosphorylation by PKA increases the interaction with inositol 1,4,5-trisphosphate and decreases the interaction with AHCYL1. {ECO:0000305|PubMed:23542070}.; PTM: Phosphorylated on tyrosine residues. {ECO:0000250|UniProtKB:Q14643}.; PTM: Ubiquitination at multiple lysines targets ITPR1 for proteasomal degradation. Approximately 40% of the ITPR1-associated ubiquitin is monoubiquitin, and polyubiquitins are both 'Lys-48'- and 'Lys-63'-linked (By similarity). {ECO:0000250|UniProtKB:P29994}.; PTM: Palmitoylated by ZDHHC6 in immune cells, leading to regulate ITPR1 stability and function (PubMed:25368151). {ECO:0000269|PubMed:25368151}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305|PubMed:25368151}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:Q9TU34}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q14643}. Note=Endoplasmic reticulum and secretory granules (By similarity). {ECO:0000250|UniProtKB:Q9TU34}. SUBUNIT: Homotetramer. Interacts with TRPC4. The PPXXF motif binds HOM1, HOM2 and HOM3. Interacts with RYR1, RYR2, ITPR1, SHANK1 and SHANK3. Part of cGMP kinase signaling complex at least composed of ACTA2/alpha-actin, CNN1/calponin H1, PLN/phospholamban, PRKG1 and ITPR1 (By similarity). Interacts with ERP44 in a pH-, redox state- and calcium-dependent manner which results in the inhibition the calcium channel activity. The strength of this interaction inversely correlates with calcium concentration. Interacts with MRVI1. Interacts with CABP1 (By similarity). Interacts with TESPA1. Interacts (when not phosphorylated) with AHCYL1 (when phosphorylated); the interaction suppresses inositol 1,4,5-trisphosphate binding to ITPR1 (PubMed:23542070). Interacts with AHCYL2 (with lower affinity than with AHCYL1) (By similarity). Interacts with BOK (via BH4 domain); protects ITPR1 from proteolysis by CASP3 during apoptosis (PubMed:23884412). {ECO:0000250|UniProtKB:Q14643, ECO:0000269|PubMed:12442173, ECO:0000269|PubMed:12525476, ECO:0000269|PubMed:15652484, ECO:0000269|PubMed:16527252, ECO:0000269|PubMed:16990611, ECO:0000269|PubMed:23542070, ECO:0000269|PubMed:23650607, ECO:0000269|PubMed:23884412}. DOMAIN: The receptor contains a calcium channel in its C-terminal extremity. Its large N-terminal cytoplasmic region has the ligand-binding site in the N-terminus and modulatory sites in the middle portion immediately upstream of the channel region. +P21729 GRPR_MOUSE Gastrin-releasing peptide receptor (GRP-R) (GRP-preferring bombesin receptor) 384 43,215 Chain (1); Disulfide bond (1); Glycosylation (3); Lipidation (1); Modified residue (1); Sequence conflict (1); Topological domain (8); Transmembrane (7) TRANSMEM 40 63 Helical; Name=1. {ECO:0000255}.; TRANSMEM 78 97 Helical; Name=2. {ECO:0000255}.; TRANSMEM 116 137 Helical; Name=3. {ECO:0000255}.; TRANSMEM 154 175 Helical; Name=4. {ECO:0000255}.; TRANSMEM 210 235 Helical; Name=5. {ECO:0000255}.; TRANSMEM 266 286 Helical; Name=6. {ECO:0000255}.; TRANSMEM 300 326 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 39 Extracellular. {ECO:0000255}.; TOPO_DOM 64 77 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 98 115 Extracellular. {ECO:0000255}.; TOPO_DOM 138 153 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 176 209 Extracellular. {ECO:0000255}.; TOPO_DOM 236 265 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 287 299 Extracellular. {ECO:0000255}.; TOPO_DOM 327 384 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for gastrin-releasing peptide (GRP) (PubMed:1671171, PubMed:1707129, PubMed:9345264, PubMed:12526815, PubMed:26658875). Signals via association with G proteins that activate a phosphatidylinositol-calcium second messenger system, resulting in Akt phosphorylation (PubMed:26658875). Contributes to the regulation of food intake (PubMed:12176666). Contributes to the perception of prurient stimuli and transmission of itch signals in the spinal cord that promote scratching behavior, but does not play a role in the perception of pain (PubMed:28280205, PubMed:17653196, PubMed:26658875). Contributes primarily to nonhistaminergic itch sensation (PubMed:28280205). Contributes to long-term fear memory, but not normal spatial memory (PubMed:12526815). {ECO:0000269|PubMed:12176666, ECO:0000269|PubMed:12526815, ECO:0000269|PubMed:1671171, ECO:0000269|PubMed:1707129, ECO:0000269|PubMed:17653196, ECO:0000269|PubMed:26658875, ECO:0000269|PubMed:9345264}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1671171, ECO:0000269|PubMed:1707129}; Multi-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Detected in pancreas and brain (PubMed:1671171, PubMed:9345264). Detected in suprachaismatic nucleus neurons (PubMed:28280205). Detected in neurons in the dorsal horn of the spinal cord (PubMed:17653196). Detected in inhibitory GABAergic interneurons in the lateral nuclues of the amydala (PubMed:12526815). {ECO:0000269|PubMed:12526815, ECO:0000269|PubMed:1671171, ECO:0000269|PubMed:17653196, ECO:0000269|PubMed:28280205, ECO:0000269|PubMed:9345264}. +Q9Z0R6 ITSN2_MOUSE Intersectin-2 (EH domain and SH3 domain regulator of endocytosis 2) (EH and SH3 domains protein 2) (SH3 domain-containing protein 1B) 1659 188,908 Alternative sequence (2); Calcium binding (1); Chain (1); Coiled coil (1); Domain (11); Erroneous initiation (1); Modified residue (9); Sequence conflict (2) FUNCTION: Adapter protein that may provide indirect link between the endocytic membrane traffic and the actin assembly machinery. May regulate the formation of clathrin-coated vesicles (CCPs). Seems to be involved in CCPs maturation including invagination or budding. Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR). Plays a role in dendrite formation by melanocytes. {ECO:0000250|UniProtKB:Q9NZM3}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Belongs to a complex that may contain multimers of ITSN1, ITSN2 and EPS15, and different partners according to the step in the endocytic process. Interacts with ADAM15. Interacts with FASLG (By similarity). Interacts with ANKRD54. Interacts with FCHO2. {ECO:0000250, ECO:0000269|PubMed:19064729, ECO:0000269|PubMed:20448150}. TISSUE SPECIFICITY: Widely expressed in adult tissues. +Q3TCV3 GSAP_MOUSE Gamma-secretase-activating protein (GSAP) (Protein pigeon homolog) [Cleaved into: Gamma-secretase-activating protein 16 kDa C-terminal form (GSAP-16K)] 858 98,694 Alternative sequence (4); Chain (2); Erroneous initiation (1); Frameshift (1); Sequence conflict (1) FUNCTION: Regulator of gamma-secretase activity, which specifically activates the production of amyloid-beta protein (amyloid-beta protein 40 and amyloid-beta protein 42), without affecting the cleavage of other gamma-secretase targets such has Notch. The gamma-secretase complex is an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (amyloid-beta precursor protein). Specifically promotes the gamma-cleavage of APP CTF-alpha (also named APP-CTF) by the gamma-secretase complex to generate amyloid-beta, while it reduces the epsilon-cleavage of APP CTF-alpha, leading to a low production of AICD. {ECO:0000269|PubMed:20811458}. PTM: The protein is first synthesized as a holoprotein form of 98 kDa and rapidly processed into the gamma-secretase-activating protein 16 kDa C-terminal form, which constitutes the predominant form. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network {ECO:0000250}. SUBUNIT: Interacts with APP; specifically interacts with the CTF-alpha product of APP. Interacts with the gamma-secretase complex (By similarity). {ECO:0000250}. +Q99MR1 GGYF1_MOUSE GRB10-interacting GYF protein 1 (PERQ amino acid-rich with GYF domain-containing protein 1) 1044 116,238 Chain (1); Compositional bias (9); Domain (1); Erroneous gene model prediction (1); Modified residue (10); Mutagenesis (4); Sequence conflict (6) FUNCTION: May act cooperatively with GRB10 to regulate tyrosine kinase receptor signaling. May increase IGF1 receptor phosphorylation under IGF1 stimulation as well as phosphorylation of IRS1 and SHC1. {ECO:0000269|PubMed:12771153}. SUBUNIT: Interacts with GRB10. This transient binding is increased under IGF1 stimulation and leads to recruitment of GIGYF1/GRB10 complex to IGF1 receptor. {ECO:0000269|PubMed:12771153}. TISSUE SPECIFICITY: Ubiquitous. Lower expression in skeletal muscle, liver and testis. {ECO:0000269|PubMed:12771153}. +Q3URY2 GEMC1_MOUSE Geminin coiled-coil domain-containing protein 1 333 37,758 Alternative sequence (2); Chain (1); Coiled coil (1) FUNCTION: Regulator of DNA replication. Promotes initiation of chromosomal DNA replication by mediating TOPBP1- and CDK2-dependent recruitment of CDC45L onto replication origins (By similarity). {ECO:0000250}. PTM: Highly phosphorylated by CDK2; stimulates initiation of DNA replication. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Associates with chromatin during pre-replication complex (pre-RC) formation. {ECO:0000250}. +P48756 GIP_MOUSE Gastric inhibitory polypeptide (GIP) (Glucose-dependent insulinotropic polypeptide) 144 16,389 Peptide (1); Propeptide (2); Sequence conflict (1); Signal peptide (1) FUNCTION: Potent stimulator of insulin secretion and relatively poor inhibitor of gastric acid secretion. SUBCELLULAR LOCATION: Secreted. +P60843 IF4A1_MOUSE Eukaryotic initiation factor 4A-I (eIF-4A-I) (eIF4A-I) (EC 3.6.4.13) (ATP-dependent RNA helicase eIF4A-1) 406 46,154 Chain (1); Cross-link (6); Domain (2); Erroneous initiation (4); Initiator methionine (1); Modified residue (7); Motif (2); Nucleotide binding (1); Sequence conflict (1) FUNCTION: ATP-dependent RNA helicase which is a subunit of the eIF4F complex involved in cap recognition and is required for mRNA binding to ribosome. In the current model of translation initiation, eIF4A unwinds RNA secondary structures in the 5'-UTR of mRNAs which is necessary to allow efficient binding of the small ribosomal subunit, and subsequent scanning for the initiator codon. SUBUNIT: eIF4F is a multi-subunit complex, the composition of which varies with external and internal environmental conditions. It is composed of at least EIF4A, EIF4E and EIF4G1/EIF4G3. Interacts with PAIP1, EIF4E and UPF2. Found in a complex with XPO7, EIF4A1, ARHGAP1, VPS26A, VPS29, VPS35 and SFN. May interact with NOM1. Interacts with PDCD4; this interferes with the interaction between EIF4A and EIF4G. Interacts with RBM4 (By similarity). {ECO:0000250}. +Q91YI6 GLD2_MOUSE Poly(A) RNA polymerase GLD2 (mGLD-2) (EC 2.7.7.19) (PAP-associated domain-containing protein 4) (Terminal nucleotidyltransferase 2) 484 55,934 Alternative sequence (1); Chain (1); Domain (1); Frameshift (1); Metal binding (2); Modified residue (3); Motif (1); Mutagenesis (1); Sequence conflict (1) FUNCTION: Cytoplasmic poly(A) RNA polymerase that adds successive AMP monomers to the 3'-end of specific RNAs, forming a poly(A) tail. In contrast to the canonical nuclear poly(A) RNA polymerase, it only adds poly(A) to selected cytoplasmic mRNAs. Does not play a role in replication-dependent histone mRNA degradation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16325797}. Nucleus {ECO:0000269|PubMed:16325797}. SUBUNIT: Interacts with CPEB1, CPEB2, CPSF1 and PABPC1. {ECO:0000269|PubMed:17927953}. TISSUE SPECIFICITY: Ubiquitous. In brain, it is highly expressed in the cerebral cortex, cerebellum, hippocampus and olfactory bulb. {ECO:0000269|PubMed:15987818, ECO:0000269|PubMed:16325797}. +Q9EQX0 GHRL_MOUSE Appetite-regulating hormone (Growth hormone secretagogue) (Growth hormone-releasing peptide) (Motilin-related peptide) (Protein M46) [Cleaved into: Ghrelin; Obestatin] 117 13,207 Alternative sequence (1); Beta strand (1); Helix (2); Lipidation (2); Modified residue (1); Peptide (2); Propeptide (2); Signal peptide (1) FUNCTION: Ghrelin is the ligand for growth hormone secretagogue receptor type 1 (GHSR). Induces the release of growth hormone from the pituitary. Has an appetite-stimulating effect, induces adiposity and stimulates gastric acid secretion. Involved in growth regulation.; FUNCTION: Obestatin may be the ligand for GPR39. May have an appetite-reducing effect resulting in decreased food intake. May reduce gastric emptying activity and jejunal motility (By similarity). {ECO:0000250}. PTM: O-octanoylation or O-decanoylation is essential for ghrelin activity (By similarity). The O-decanoylated form ghrelin-C10 differs in the length of the carbon backbone of the carboxylic acid bound to Ser-26 (PubMed:15746259). {ECO:0000250, ECO:0000269|PubMed:15746259}.; PTM: Amidation of Leu-98 is essential for obestatin activity. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10930375}. TISSUE SPECIFICITY: Mainly expressed in the gastrointestinal tract with higher levels in the stomach, medium levels in the duodenum, jejunum, ileum and colon. Low expression in the testis and brain. Not detected in the salivary gland, pancreas, liver and lung. {ECO:0000269|PubMed:10930375}. +Q5FW57 GLYAL_MOUSE Glycine N-acyltransferase-like protein (EC 2.3.1.13) (Acyl-CoA:glycine N-acyltransferase-like) (AAc-like) 296 34,168 Chain (1); Erroneous termination (1); Modified residue (11); Sequence conflict (1) FUNCTION: Mitochondrial acyltransferase which transfers the acyl group to the N-terminus of glycine. Can conjugate a multitude of substrates to form a variety of N-acylglycines (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. +P16872 IL7RA_MOUSE Interleukin-7 receptor subunit alpha (IL-7 receptor subunit alpha) (IL-7R subunit alpha) (IL-7R-alpha) (IL-7RA) (CD antigen CD127) 459 51,605 Beta strand (17); Chain (1); Compositional bias (1); Disulfide bond (3); Domain (1); Glycosylation (3); Helix (3); Modified residue (1); Motif (2); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 240 264 Helical. {ECO:0000255}. TOPO_DOM 21 239 Extracellular. {ECO:0000255}.; TOPO_DOM 265 459 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for interleukin-7. Also acts as a receptor for thymic stromal lymphopoietin (TSLP). PTM: N-glycosylated IL-7Ralpha binds IL7 300-fold more tightly than the unglycosylated form. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: The IL7 receptor is a heterodimer of IL7R and IL2RG. The TSLP receptor is a heterodimer of CRLF2 and IL7R. {ECO:0000269|PubMed:24632570}. DOMAIN: The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.; DOMAIN: The box 1 motif is required for JAK interaction and/or activation. TISSUE SPECIFICITY: Spleen, thymus and fetal liver. +P15247 IL9_MOUSE Interleukin-9 (IL-9) (Cytokine P40) (T-cell growth factor P40) 144 16,075 Chain (1); Glycosylation (4); Modified residue (1); Signal peptide (1) FUNCTION: Supports IL-2 independent and IL-4 independent growth of helper T-cells. SUBCELLULAR LOCATION: Secreted. +Q9D154 ILEUA_MOUSE Leukocyte elastase inhibitor A (Serine protease inhibitor EIA) (Serpin B1a) 379 42,575 Chain (1); Erroneous gene model prediction (1); Frameshift (1); Modified residue (1); Sequence conflict (15); Site (1) FUNCTION: Regulates the activity of the neutrophil proteases and thus, forms complexes with chymotrypsin, elastase, cathepsin G and proteinase-3. {ECO:0000269|PubMed:12189154}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous with higher expression in pancreas, spleen and bone marrow. {ECO:0000269|PubMed:11863365, ECO:0000269|PubMed:12189154}. +Q8VHP7 ILEUB_MOUSE Leukocyte elastase inhibitor B (Serine protease inhibitor EIB) (Serpin B1b) 382 42,887 Chain (1); Site (1) FUNCTION: Regulates the activity of the neutrophil proteases. Forms only a stable complex with CTSG/Cathepsin G. {ECO:0000269|PubMed:12189154}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain with lower expression in lung, spleen and testis. {ECO:0000269|PubMed:12189154}. +Q8R0F6 ILKAP_MOUSE Integrin-linked kinase-associated serine/threonine phosphatase 2C (ILKAP) (EC 3.1.3.16) 392 42,774 Alternative sequence (2); Chain (1); Domain (1); Metal binding (5); Modified residue (2) FUNCTION: Protein phosphatase that may play a role in regulation of cell cycle progression via dephosphorylation of its substrates whose appropriate phosphorylation states might be crucial for cell proliferation. Selectively associates with integrin linked kinase (ILK), to modulate cell adhesion and growth factor signaling. Inhibits the ILK-GSK3B signaling axis and may play an important role in inhibiting oncogenic transformation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with ILK. {ECO:0000250}. +Q9DCQ3 GOT1A_MOUSE Vesicle transport protein GOT1A (Golgi transport 1 homolog A) 133 14,800 Chain (1); Topological domain (5); Transmembrane (4) TRANSMEM 10 30 Helical; Name=1. {ECO:0000255}.; TRANSMEM 32 52 Helical; Name=2. {ECO:0000255}.; TRANSMEM 69 89 Helical; Name=3. {ECO:0000255}.; TRANSMEM 93 113 Helical; Name=4. {ECO:0000255}. TOPO_DOM 1 9 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 31 31 Lumenal. {ECO:0000255}.; TOPO_DOM 53 68 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 90 92 Lumenal. {ECO:0000255}.; TOPO_DOM 114 133 Cytoplasmic. {ECO:0000255}. FUNCTION: May be involved in fusion of ER-derived transport vesicles with the Golgi complex. {ECO:0000250|UniProtKB:Q9Y3E0}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q3UVY1 GP149_MOUSE Probable G-protein coupled receptor 149 (G-protein coupled receptor PGR10) 732 80,520 Chain (1); Disulfide bond (1); Erroneous initiation (1); Glycosylation (1); Sequence conflict (3); Topological domain (8); Transmembrane (7) TRANSMEM 37 57 Helical; Name=1. {ECO:0000255}.; TRANSMEM 70 90 Helical; Name=2. {ECO:0000255}.; TRANSMEM 111 133 Helical; Name=3. {ECO:0000255}.; TRANSMEM 157 177 Helical; Name=4. {ECO:0000255}.; TRANSMEM 191 211 Helical; Name=5. {ECO:0000255}.; TRANSMEM 312 332 Helical; Name=6. {ECO:0000255}.; TRANSMEM 344 364 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 36 Extracellular. {ECO:0000255}.; TOPO_DOM 58 69 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 91 110 Extracellular. {ECO:0000255}.; TOPO_DOM 134 156 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 178 190 Extracellular. {ECO:0000255}.; TOPO_DOM 212 311 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 333 343 Extracellular. {ECO:0000255}.; TOPO_DOM 365 732 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q7TSN6 GP151_MOUSE Probable G-protein coupled receptor 151 protein (G-protein coupled receptor PGR7) (GPCR-2037) 422 46,826 Chain (1); Disulfide bond (1); Glycosylation (2); Topological domain (8); Transmembrane (7) TRANSMEM 46 66 Helical; Name=1. {ECO:0000255}.; TRANSMEM 77 97 Helical; Name=2. {ECO:0000255}.; TRANSMEM 124 144 Helical; Name=3. {ECO:0000255}.; TRANSMEM 158 178 Helical; Name=4. {ECO:0000255}.; TRANSMEM 206 226 Helical; Name=5. {ECO:0000255}.; TRANSMEM 260 280 Helical; Name=6. {ECO:0000255}.; TRANSMEM 291 311 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 45 Extracellular. {ECO:0000255}.; TOPO_DOM 67 76 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 98 123 Extracellular. {ECO:0000255}.; TOPO_DOM 145 157 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 179 205 Extracellular. {ECO:0000255}.; TOPO_DOM 227 259 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 281 290 Extracellular. {ECO:0000255}.; TOPO_DOM 312 422 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q9Z282 GP132_MOUSE Probable G-protein coupled receptor 132 (G2 accumulation protein) 382 42,653 Chain (1); Disulfide bond (1); Glycosylation (1); Mutagenesis (1); Topological domain (8); Transmembrane (7) TRANSMEM 43 65 Helical; Name=1. {ECO:0000255}.; TRANSMEM 77 99 Helical; Name=2. {ECO:0000255}.; TRANSMEM 114 135 Helical; Name=3. {ECO:0000255}.; TRANSMEM 156 175 Helical; Name=4. {ECO:0000255}.; TRANSMEM 199 221 Helical; Name=5. {ECO:0000255}.; TRANSMEM 242 261 Helical; Name=6. {ECO:0000255}.; TRANSMEM 287 309 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 42 Extracellular. {ECO:0000255}.; TOPO_DOM 66 76 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 100 113 Extracellular. {ECO:0000255}.; TOPO_DOM 136 155 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 176 198 Extracellular. {ECO:0000255}.; TOPO_DOM 222 241 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 262 286 Extracellular. {ECO:0000255}.; TOPO_DOM 310 382 Cytoplasmic. {ECO:0000255}. FUNCTION: May be a receptor for oxidized free fatty acids derived from linoleic and arachidonic acids such as 9-hydroxyoctadecadienoic acid (9-HODE). Activates a G alpha protein, most likely G alpha(q). May be involved in apoptosis. Functions at the G2/M checkpoint to delay mitosis. May function as a sensor that monitors the oxidative states and mediates appropriate cellular responses such as secretion of paracrine signals and attenuation of proliferation. May mediate ths accumulation of intracellular inositol phosphates at acidic pH through proton-sensing activity (By similarity). {ECO:0000250, ECO:0000269|PubMed:15728718}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:15728718}; Multi-pass membrane protein {ECO:0000305|PubMed:15728718}. Note=Internalized and accumulated in endosomal compartments. LPC triggers the relocalization from the endosomal compartment to the cell surface. TISSUE SPECIFICITY: Highly expressed in hematopoietic tissues rich in lymphocytes like spleen and thymus. Weakly expressed in heart and lung. Highly expressed in infiltrating macrophages within atherosclerotic lesions. {ECO:0000269|PubMed:12482833}. +Q8C419 GP158_MOUSE Probable G-protein coupled receptor 158 1200 134,426 Chain (1); Cross-link (1); Glycosylation (5); Modified residue (7); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 418 438 Helical; Name=1. {ECO:0000255}.; TRANSMEM 452 472 Helical; Name=2. {ECO:0000255}.; TRANSMEM 484 506 Helical; Name=3. {ECO:0000255}.; TRANSMEM 529 549 Helical; Name=4. {ECO:0000255}.; TRANSMEM 580 600 Helical; Name=5. {ECO:0000255}.; TRANSMEM 614 634 Helical; Name=6. {ECO:0000255}.; TRANSMEM 644 664 Helical; Name=7. {ECO:0000255}. TOPO_DOM 25 417 Extracellular. {ECO:0000255}.; TOPO_DOM 439 451 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 473 483 Extracellular. {ECO:0000255}.; TOPO_DOM 507 528 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 550 579 Extracellular. {ECO:0000255}.; TOPO_DOM 601 613 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 635 643 Extracellular. {ECO:0000255}.; TOPO_DOM 665 1200 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q7TQP2 GP135_MOUSE G-protein coupled receptor 135 457 49,361 Chain (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 65 85 Helical; Name=1. {ECO:0000255}.; TRANSMEM 110 130 Helical; Name=2. {ECO:0000255}.; TRANSMEM 157 177 Helical; Name=3. {ECO:0000255}.; TRANSMEM 190 210 Helical; Name=4. {ECO:0000255}.; TRANSMEM 236 256 Helical; Name=5. {ECO:0000255}.; TRANSMEM 296 316 Helical; Name=6. {ECO:0000255}.; TRANSMEM 330 350 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 64 Extracellular. {ECO:0000255}.; TOPO_DOM 86 109 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 131 156 Extracellular. {ECO:0000255}.; TOPO_DOM 178 189 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 211 235 Extracellular. {ECO:0000255}.; TOPO_DOM 257 295 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 317 329 Extracellular. {ECO:0000255}.; TOPO_DOM 351 457 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan receptor. Has spontaneous activity for beta-arrestin recruitment (By similarity). Shows a reciprocal regulatory interaction with the melatonin receptor MTNR1B most likely through receptor heteromerization (By similarity). {ECO:0000250|UniProtKB:Q8IZ08}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8IZ08}; Multi-pass membrane protein {ECO:0000255}. Endosome membrane {ECO:0000250|UniProtKB:Q8IZ08}; Multi-pass membrane protein {ECO:0000255}. Note=Colocalizes with ARRB2/beta-arrestin-2 in the endosome (By similarity). {ECO:0000250|UniProtKB:Q8IZ08}. SUBUNIT: Interacts with MTNR1B. Interacts with ARRB1 and ARRB2 in a spontaneous and agonist-independent manner; leading to the internalization of GPR135 in the endosomal compartment (By similarity). {ECO:0000250|UniProtKB:Q8IZ08}. +Q80UC8 GP139_MOUSE Probable G-protein coupled receptor 139 (G(q)-coupled orphan receptor GPRg1) (G-protein-coupled receptor PGR3) 345 39,758 Chain (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 22 42 Helical; Name=1. {ECO:0000255}.; TRANSMEM 58 78 Helical; Name=2. {ECO:0000255}.; TRANSMEM 95 115 Helical; Name=3. {ECO:0000255}.; TRANSMEM 141 161 Helical; Name=4. {ECO:0000255}.; TRANSMEM 174 194 Helical; Name=5. {ECO:0000255}.; TRANSMEM 221 241 Helical; Name=6. {ECO:0000255}.; TRANSMEM 261 281 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 21 Extracellular. {ECO:0000255}.; TOPO_DOM 43 57 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 79 94 Extracellular. {ECO:0000255}.; TOPO_DOM 116 140 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 162 173 Extracellular. {ECO:0000255}.; TOPO_DOM 195 220 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 242 260 Extracellular. {ECO:0000255}.; TOPO_DOM 282 345 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan receptor. Seems to act through a G(q/11)-mediated pathway. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed almost exclusively in the brain. Abundantly expressed in the ventrolateral region of caudate putamen, the habenular nucleus, the zona incerta, and the medial mammillary nucleus. {ECO:0000269|PubMed:15845401}. +Q7TQP0 GP141_MOUSE Probable G-protein coupled receptor 141 (G-protein coupled receptor PGR13) 305 35,284 Chain (1); Glycosylation (2); Topological domain (8); Transmembrane (7) TRANSMEM 23 43 Helical; Name=1. {ECO:0000255}.; TRANSMEM 51 71 Helical; Name=2. {ECO:0000255}.; TRANSMEM 92 112 Helical; Name=3. {ECO:0000255}.; TRANSMEM 132 152 Helical; Name=4. {ECO:0000255}.; TRANSMEM 185 205 Helical; Name=5. {ECO:0000255}.; TRANSMEM 228 248 Helical; Name=6. {ECO:0000255}.; TRANSMEM 268 288 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 22 Extracellular. {ECO:0000255}.; TOPO_DOM 44 50 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 72 91 Extracellular. {ECO:0000255}.; TOPO_DOM 113 131 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 153 184 Extracellular. {ECO:0000255}.; TOPO_DOM 206 227 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 249 267 Extracellular. {ECO:0000255}.; TOPO_DOM 289 305 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +B2RPY5 GP161_MOUSE G-protein coupled receptor 161 545 60,303 Alternative sequence (2); Chain (1); Disulfide bond (1); Glycosylation (3); Mutagenesis (7); Topological domain (8); Transmembrane (7) TRANSMEM 47 67 Helical; Name=1. {ECO:0000255}.; TRANSMEM 81 101 Helical; Name=2. {ECO:0000255}.; TRANSMEM 118 139 Helical; Name=3. {ECO:0000255}.; TRANSMEM 160 180 Helical; Name=4. {ECO:0000255}.; TRANSMEM 206 226 Helical; Name=5. {ECO:0000255}.; TRANSMEM 286 306 Helical; Name=6. {ECO:0000255}.; TRANSMEM 323 343 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 46 Extracellular. {ECO:0000255}.; TOPO_DOM 68 80 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 102 117 Extracellular. {ECO:0000255}.; TOPO_DOM 140 159 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 181 205 Extracellular. {ECO:0000255}.; TOPO_DOM 227 285 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 307 322 Extracellular. {ECO:0000255}.; TOPO_DOM 344 545 Cytoplasmic. {ECO:0000255}. FUNCTION: Key negative regulator of Shh signaling, which promotes the processing of GLI3 into GLI3R during neural tube development. Recruited by TULP3 and the IFT-A complex to primary cilia and acts as a regulator of the PKA-dependent basal repression machinery in Shh signaling by increasing cAMP levels, leading to promote the PKA-dependent processing of GLI3 into GLI3R and repress the Shh signaling. In presence of SHH, it is removed from primary cilia and is internalized into recycling endosomes, preventing its activity and allowing activation of the Shh signaling. Its ligand is unknown. {ECO:0000269|PubMed:18250320, ECO:0000269|PubMed:23332756}. SUBCELLULAR LOCATION: Cell projection, cilium membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. Note=Mainly localizes to primary cilium in a TULP3 and IFT-A complex-dependent manner. In presence of SHH, it is removed from primary cilia and is internalized into recycling endosomes and is apparently not degraded. DISEASE: Note=An intragenic deletion in Gpr161 is responsible for the vacuolated lens (vl) phenotype that is characterized by neural tube defects and congenital cataracts. The vl mutation aroses spontaneously. About half of vl/vl embryos display lumbar-sacral spina bifida and die before birth, and the other half have closed neural tubes but show thinning of the midline neuroepithelium and epidermis, dilation of the dorsal ventricle, and presence of ectopic neuroepithelial cells in the ventricle. All surviving adults display congenital cataracts (PubMed:18250320). It is not a null mutant allele (PubMed:23332756). {ECO:0000269|PubMed:18250320, ECO:0000269|PubMed:23332756}. +Q3UN16 GP162_MOUSE Probable G-protein coupled receptor 162 588 64,148 Chain (1); Glycosylation (1); Modified residue (2); Sequence conflict (1); Topological domain (8); Transmembrane (7) TRANSMEM 18 38 Helical; Name=1. {ECO:0000255}.; TRANSMEM 50 70 Helical; Name=2. {ECO:0000255}.; TRANSMEM 92 112 Helical; Name=3. {ECO:0000255}.; TRANSMEM 134 154 Helical; Name=4. {ECO:0000255}.; TRANSMEM 175 195 Helical; Name=5. {ECO:0000255}.; TRANSMEM 276 296 Helical; Name=6. {ECO:0000255}.; TRANSMEM 304 324 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 17 Extracellular. {ECO:0000255}.; TOPO_DOM 39 49 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 71 91 Extracellular. {ECO:0000255}.; TOPO_DOM 113 133 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 155 174 Extracellular. {ECO:0000255}.; TOPO_DOM 196 275 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 297 303 Extracellular. {ECO:0000255}.; TOPO_DOM 325 588 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan receptor. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q8VDV0 ITGBL_MOUSE Integrin beta-like protein 1 494 53,978 Alternative sequence (2); Chain (1); Glycosylation (1); Region (1); Repeat (10); Sequence conflict (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. DOMAIN: Contains ten tandem EGF-like repeats strikingly similar to those found in the cysteine rich 'stalk-like' structure of integrin beta-subunits. +Q61702 ITIH1_MOUSE Inter-alpha-trypsin inhibitor heavy chain H1 (ITI heavy chain H1) (ITI-HC1) (Inter-alpha-inhibitor heavy chain 1) 907 101,067 Chain (1); Domain (2); Glycosylation (5); Modified residue (3); Propeptide (2); Sequence conflict (2); Signal peptide (1) FUNCTION: May act as a carrier of hyaluronan in serum or as a binding protein between hyaluronan and other matrix protein, including those on cell surfaces in tissues to regulate the localization, synthesis and degradation of hyaluronan which are essential to cells undergoing biological processes. {ECO:0000250}. PTM: Heavy chains are linked to bikunin via chondroitin 4-sulfate esterified to the alpha-carboxyl of the C-terminal aspartate after propeptide cleavage. {ECO:0000250}.; PTM: The S-linked glycan is composed of two 6-carbon sugars, possibly Glc or Gal. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: I-alpha-I plasma protease inhibitors are assembled from one or two heavy chains (H1, H2 or H3) and one light chain, bikunin. Inter-alpha-inhibitor (I-alpha-I) is composed of H1, H2 and bikunin, inter-alpha-like inhibitor (I-alpha-LI) of H2 and bikunin, and pre-alpha-inhibitor (P-alpha-I) of H3 and bikunin. TISSUE SPECIFICITY: Liver specific. +Q61703 ITIH2_MOUSE Inter-alpha-trypsin inhibitor heavy chain H2 (ITI heavy chain H2) (ITI-HC2) (Inter-alpha-inhibitor heavy chain 2) 946 105,928 Chain (1); Domain (2); Erroneous initiation (1); Glycosylation (3); Modified residue (6); Propeptide (2); Sequence conflict (1); Signal peptide (1) FUNCTION: May act as a carrier of hyaluronan in serum or as a binding protein between hyaluronan and other matrix protein, including those on cell surfaces in tissues to regulate the localization, synthesis and degradation of hyaluronan which are essential to cells undergoing biological processes. {ECO:0000250}. PTM: Heavy chains are linked to bikunin via chondroitin 4-sulfate esterified to the alpha-carboxyl of the C-terminal aspartate after propeptide cleavage. {ECO:0000250}.; PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000250|UniProtKB:P19823}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: I-alpha-I plasma protease inhibitors are assembled from one or two heavy chains (H1, H2 or H3) and one light chain, bikunin. Inter-alpha-inhibitor (I-alpha-I) is composed of H1, H2 and bikunin, inter-alpha-like inhibitor (I-alpha-LI) of H2 and bikunin, and pre-alpha-inhibitor (P-alpha-I) of H3 and bikunin. TISSUE SPECIFICITY: Expressed in both liver and brain. +Q61704 ITIH3_MOUSE Inter-alpha-trypsin inhibitor heavy chain H3 (ITI heavy chain H3) (ITI-HC3) (Inter-alpha-inhibitor heavy chain 3) 889 99,358 Chain (1); Domain (2); Erroneous initiation (2); Glycosylation (2); Modified residue (1); Propeptide (2); Sequence conflict (7); Signal peptide (1) FUNCTION: May act as a carrier of hyaluronan in serum or as a binding protein between hyaluronan and other matrix protein, including those on cell surfaces in tissues to regulate the localization, synthesis and degradation of hyaluronan which are essential to cells undergoing biological processes. {ECO:0000250}. PTM: Heavy chains are linked to bikunin via chondroitin 4-sulfate esterified to the alpha-carboxyl of the C-terminal aspartate after propeptide cleavage. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: I-alpha-I plasma protease inhibitors are assembled from one or two heavy chains (H1, H2 or H3) and one light chain, bikunin. Inter-alpha-inhibitor (I-alpha-I) is composed of H1, H2 and bikunin, inter-alpha-like inhibitor (I-alpha-LI) of H2 and bikunin, and pre-alpha-inhibitor (P-alpha-I) of H3 and bikunin. TISSUE SPECIFICITY: Expressed in both liver and brain. +A6X935 ITIH4_MOUSE Inter alpha-trypsin inhibitor, heavy chain 4 (ITI heavy chain H4) (ITI-HC4) (Inter-alpha-inhibitor heavy chain 4) 942 104,659 Alternative sequence (1); Chain (1); Coiled coil (1); Compositional bias (1); Disulfide bond (1); Domain (2); Glycosylation (5); Sequence conflict (9); Signal peptide (1) FUNCTION: Type II acute-phase protein (APP) involved in inflammatory responses to trauma. May also play a role in liver development or regeneration. PTM: May be O-glycosylated (By similarity). N-glycosylated. {ECO:0000250, ECO:0000269|PubMed:16944957, ECO:0000269|PubMed:17330941}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Interacts (via C-terminus) with DNAJC1 (via SANT 2 domain). {ECO:0000269|PubMed:16271702}. TISSUE SPECIFICITY: Highly expressed in liver. Weak expression in lung and heart. {ECO:0000269|PubMed:9602042}. +Q80UC6 GPR62_MOUSE G-protein coupled receptor 62 358 37,148 Chain (1); Compositional bias (1); Glycosylation (1); Mutagenesis (2); Topological domain (8); Transmembrane (7) TRANSMEM 18 38 Helical; Name=1. {ECO:0000255}.; TRANSMEM 54 74 Helical; Name=2. {ECO:0000255}.; TRANSMEM 90 110 Helical; Name=3. {ECO:0000255}.; TRANSMEM 129 149 Helical; Name=4. {ECO:0000255}.; TRANSMEM 177 197 Helical; Name=5. {ECO:0000255}.; TRANSMEM 235 255 Helical; Name=6. {ECO:0000255}.; TRANSMEM 269 289 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 17 Extracellular. {ECO:0000255}.; TOPO_DOM 39 53 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 75 89 Extracellular. {ECO:0000255}.; TOPO_DOM 111 128 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 150 176 Extracellular. {ECO:0000255}.; TOPO_DOM 198 234 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 256 268 Extracellular. {ECO:0000255}.; TOPO_DOM 290 358 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan G-protein coupled receptor. Constitutively activates the G(q/11)/inositol phosphate and the G(s)-alpha/cAMP signaling pathways (PubMed:28912303). Has spontaneous activity for beta-arrestin recruitment (By similarity). Shows a reciprocal regulatory interaction with the melatonin receptor MTNR1B most likely through receptor heteromerization (By similarity). {ECO:0000250|UniProtKB:Q9BZJ7, ECO:0000269|PubMed:28912303}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9BZJ7}; Multi-pass membrane protein {ECO:0000255}. Endosome membrane {ECO:0000250|UniProtKB:Q9BZJ7}; Multi-pass membrane protein {ECO:0000255}. Note=Colocalizes with ARRB2 in the endosome. {ECO:0000250|UniProtKB:Q9BZJ7}. SUBUNIT: Homodimer (PubMed:28912303). Forms heterodimer with MTNR1B (By similarity). Interacts with ARRB1 and ARRB2 in a spontaneous and agonist-independent manner; leading to the internalization of GPR62 in the endosomal compartment (By similarity). {ECO:0000250|UniProtKB:Q9BZJ7, ECO:0000269|PubMed:28912303}. DOMAIN: Lacks the conserved DRY and BBXXB motifs. The restoration of these motifs affects its constitutive activity. {ECO:0000269|PubMed:28912303}. TISSUE SPECIFICITY: Expressed in the brain and testes. Expressed widely, in the brain, including the cerebral cortex, cerebellum, hippocampus,thalamus and pituitary gland. In the testes, expressed specifically in the germ cells. {ECO:0000269|PubMed:28912303}. +Q8BJD1 ITIH5_MOUSE Inter-alpha-trypsin inhibitor heavy chain H5 (ITI heavy chain H5) (ITI-HC5) (Inter-alpha-inhibitor heavy chain 5) 952 106,749 Chain (1); Compositional bias (1); Domain (2); Glycosylation (8); Sequence conflict (1); Signal peptide (1) FUNCTION: May act as a tumor suppressor. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +Q6PE65 GPT2L_MOUSE G patch domain-containing protein 2-like 482 53,989 Alternative sequence (1); Chain (1); Erroneous initiation (1); Modified residue (4); Sequence conflict (3) +Q99MT7 GPR87_MOUSE G-protein coupled receptor 87 358 41,414 Chain (1); Disulfide bond (1); Glycosylation (3); Sequence conflict (1); Topological domain (8); Transmembrane (7) TRANSMEM 48 68 Helical; Name=1. {ECO:0000255}.; TRANSMEM 76 96 Helical; Name=2. {ECO:0000255}.; TRANSMEM 117 137 Helical; Name=3. {ECO:0000255}.; TRANSMEM 160 180 Helical; Name=4. {ECO:0000255}.; TRANSMEM 209 229 Helical; Name=5. {ECO:0000255}.; TRANSMEM 257 277 Helical; Name=6. {ECO:0000255}.; TRANSMEM 298 318 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 47 Extracellular. {ECO:0000255}.; TOPO_DOM 69 75 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 97 116 Extracellular. {ECO:0000255}.; TOPO_DOM 138 159 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 181 208 Extracellular. {ECO:0000255}.; TOPO_DOM 230 256 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 278 297 Extracellular. {ECO:0000255}.; TOPO_DOM 319 358 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for lysophosphatidic acid (LPA). Necessary for p53/TP53-dependent survival in response to DNA damage (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Expressed at high levels in testis and brain and to a lesser extent placenta, ovary, prostate, and skeletal muscle but not in heart, lung, kidney, liver or intestine. {ECO:0000269|PubMed:17905198}. +Q60760 GRB10_MOUSE Growth factor receptor-bound protein 10 (GRB10 adapter protein) (Maternally expressed gene 1 protein) 621 70,585 Alternative sequence (2); Beta strand (6); Chain (1); Domain (3); Erroneous initiation (2); Helix (3); Modified residue (5); Sequence conflict (2) FUNCTION: Adapter protein which modulates coupling of a number of cell surface receptor kinases with specific signaling pathways. Binds to, and suppress signals from, activated receptors tyrosine kinases, including the insulin (INSR) and insulin-like growth factor (IGF1R) receptors. The inhibitory effect can be achieved by 2 mechanisms: interference with the signaling pathway and increased receptor degradation. Delays and reduces AKT1 phosphorylation in response to insulin stimulation. Blocks association between INSR and IRS1 and IRS2 and prevents insulin-stimulated IRS1 and IRS2 tyrosine phosphorylation. Recruits NEDD4 to IGF1R, leading to IGF1R ubiquitination, increased internalization and degradation by both the proteasomal and lysosomal pathways. A similar role in the mediation of ubiquitination has also been suggested with INSR. Negatively regulates Wnt signaling by interacting with LRP6 intracellular portion and interfering with the binding of AXIN1 to LRP6. Positive regulator of the KDR/VEGFR-2 signaling pathway. May inhibit NEDD4-mediated degradation of KDR/VEGFR-2. {ECO:0000269|PubMed:12697834, ECO:0000269|PubMed:12829789, ECO:0000269|PubMed:15664450, ECO:0000269|PubMed:17376403, ECO:0000269|PubMed:18286479}. PTM: Phosphorylated on serine residues upon EGF, FGF and PDGF stimulation. {ECO:0000269|PubMed:15722337, ECO:0000269|PubMed:7731717}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18286479}. Note=When complexed with NEDD4 and IGF1R, follows IGF1R internalization, remaining associated with early endosomes. Uncouples from IGF1R before the sorting of the receptor to the lysosomal compartment. SUBUNIT: Interacts with ligand-activated tyrosine kinase receptors, including FGFR1, INSR, IGF1R, MET and PDGFRB in a phosphotyrosine-dependent manner through the SH2 domain. Poorly binds to the EGFR. Directly interacts with MAP3K14/NIK and is recruited to the EGFR-ERBB2 complex (By similarity). Interacts with GIGYF1/PERQ1 and GIGYF2/TNRC15. When unphosphorylated, interacts with AKT1 and when phosphorylated with YWHAE/14-3-3 epsilon. Interacts with NEDD4. Interacts with LRP6, thus interfering with the binding of AXIN1 to LRP6. Binds to activated NRAS (By similarity). {ECO:0000250}. DOMAIN: The PH domain binds relatively non-specifically to several phosphoinositides, including PI(5)P, PI(4,5)P2, PI(3,4)P2 and PI(3,4,5)P3, with modest affinities. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:7731717, ECO:0000269|PubMed:9062339}. +Q640M6 GDPD5_MOUSE Glycerophosphodiester phosphodiesterase domain-containing protein 5 (EC 3.1.4.11) (Glycerophosphodiester phosphodiesterase 2) 607 68,890 Chain (1); Disulfide bond (2); Domain (1); Erroneous initiation (1); Glycosylation (5); Sequence conflict (2); Topological domain (7); Transmembrane (6) TRANSMEM 43 63 Helical. {ECO:0000255}.; TRANSMEM 90 110 Helical. {ECO:0000255}.; TRANSMEM 126 146 Helical. {ECO:0000255}.; TRANSMEM 161 181 Helical. {ECO:0000255}.; TRANSMEM 193 213 Helical. {ECO:0000255}.; TRANSMEM 497 517 Helical. {ECO:0000255}. TOPO_DOM 1 42 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 64 89 Extracellular. {ECO:0000255}.; TOPO_DOM 111 125 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 147 160 Extracellular. {ECO:0000255}.; TOPO_DOM 182 192 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 214 496 Extracellular. {ECO:0000255}.; TOPO_DOM 518 607 Cytoplasmic. {ECO:0000255}. FUNCTION: Glycerophosphodiester phosphodiesterase that promotes neurite formation and drives spinal motor neuron differentiation (PubMed:17275818, PubMed:18667693). Mediates the cleavage of glycosylphosphatidylinositol (GPI) anchor of target proteins: removes the GPI-anchor of RECK, leading to release RECK from the plasma membrane (By similarity). May contribute to the osmotic regulation of cellular glycerophosphocholine (PubMed:18667693). {ECO:0000250|UniProtKB:Q3KTM2, ECO:0000269|PubMed:17275818, ECO:0000269|PubMed:18667693}. PTM: Intramolecular disulfide bond between Cys-25 and Cys-571 is reduced by PRDX1. {ECO:0000250|UniProtKB:Q3KTM2}. SUBCELLULAR LOCATION: Endomembrane system {ECO:0000269|PubMed:17275818, ECO:0000269|PubMed:18667693, ECO:0000305|PubMed:15276213}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:15276213, ECO:0000269|PubMed:17275818, ECO:0000269|PubMed:18667693}. Cell projection, growth cone {ECO:0000269|PubMed:17275818}. SUBUNIT: Interacts with PRDX1; forms a mixed-disulfide with PRDX1, leading to disrupt intramolecular disulfide bond between Cys-25 and Cys-571. {ECO:0000250|UniProtKB:Q3KTM2}. TISSUE SPECIFICITY: Detected in brain, lung, heart, kidney and testis. {ECO:0000269|PubMed:15276213}. +Q9CQQ4 GEMI2_MOUSE Gem-associated protein 2 (Gemin-2) (Component of gems 2) (Survival of motor neuron protein-interacting protein 1) (SMN-interacting protein 1) 269 30,441 Chain (1); Compositional bias (1); Modified residue (2); Sequence conflict (1) FUNCTION: The SMN complex plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, gem {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Localized in subnuclear structures next to coiled bodies, called gems, which are highly enriched in spliceosomal snRNPs. Also found in the cytoplasm (By similarity). {ECO:0000250}. SUBUNIT: Part of the core SMN complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8 and STRAP/UNRIP. Part of the SMN-Sm complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8, STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG. Interacts directly with GEMIN5 (By similarity). {ECO:0000250}. +Q80WJ1 GGN_MOUSE Gametogenetin 673 68,892 Alternative sequence (3); Chain (1); Compositional bias (2); Modified residue (1); Region (2); Sequence conflict (4) FUNCTION: May be involved in spermatogenesis. {ECO:0000269|PubMed:12574169}. SUBCELLULAR LOCATION: Isoform 1: Cytoplasm, perinuclear region. Note=Localizes along the nuclear membrane.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasmic vesicle.; SUBCELLULAR LOCATION: Isoform 3: Nucleus, nucleolus. SUBUNIT: Isoform 1 and isoform 3 interact with FANCL. Isoform 1 interacts with GGNBP1, ZNF403/GGNBP2 and OAZ3. Isoform 2 interacts with GGNBP1. {ECO:0000269|PubMed:12574169, ECO:0000269|PubMed:15642376, ECO:0000269|PubMed:15892049}. TISSUE SPECIFICITY: Testis-specific. Specifically expressed in the germ cells and not in the somatic, Sertoli, or Leydig cells. In adult testis, expression starts in stage VIII pachytene spermatocytes, increases in stage IX and X pachytene spermatocytes, and culminates in stage XI diplotene spermatocytes and the meiotic cells in stage XII. Expression decreases slightly in step 1-3 spermatids, further decreases in step 4-11 spermatids, and is no longer detectable in step 12 spermatids and beyond. Isoform 2 is mainly expressed in testis. {ECO:0000269|PubMed:12574169}. +Q75N62 GIMA8_MOUSE GTPase IMAP family member 8 (mGIMAP8) (Immune-associated nucleotide-binding protein 9) (IAN-9) (Immunity-associated protein 8) 688 76,843 Binding site (2); Chain (1); Compositional bias (2); Domain (3); Nucleotide binding (2); Sequence conflict (1) FUNCTION: Exerts an anti-apoptotic effect in the immune system and is involved in responses to infections. {ECO:0000269|PubMed:16088918}. SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:16088918}. Golgi apparatus {ECO:0000269|PubMed:16088918}. Mitochondrion {ECO:0000269|PubMed:16088918}. Cytoplasm, cytosol {ECO:0000250}. TISSUE SPECIFICITY: Abundantly expressed in the thymus, spleen, lymph node, followed by the bone marrow and lung. {ECO:0000269|PubMed:16088918, ECO:0000269|PubMed:16509771}. +Q3V1M1 IGS10_MOUSE Immunoglobulin superfamily member 10 (IgSF10) 2594 285,598 Chain (1); Disulfide bond (12); Domain (14); Frameshift (1); Glycosylation (9); Modified residue (1); Repeat (7); Sequence conflict (1); Signal peptide (1) FUNCTION: Involved in the control of early migration of neurons expressing gonadotropin-releasing hormone (GNRH neurons) (PubMed:27137492). May be involved in the maintenance of osteochondroprogenitor cells pool (By similarity). {ECO:0000250|UniProtKB:Q6WRH9, ECO:0000269|PubMed:27137492}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q6WRI0}. TISSUE SPECIFICITY: In the embryo, expressed in the nasal mesenchyme. {ECO:0000269|PubMed:27137492}. +Q7TNR6 IGS21_MOUSE Immunoglobulin superfamily member 21 (IgSF21) 468 51,937 Chain (1); Disulfide bond (1); Domain (2); Glycosylation (3); Signal peptide (1) FUNCTION: Involved in synaptic inhibition in the brain. Selectively regulates inhibitory presynaptic differentiation through interacting with presynaptic NRXN2. {ECO:0000269|PubMed:28864826}. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane {ECO:0000269|PubMed:28864826}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:28864826}. SUBUNIT: Interacts (Ig-like 1 domain) with NRXN2 (via Laminin G-like 1 domain) in a trans-interaction manner. {ECO:0000269|PubMed:28864826}. DOMAIN: Ig-like 1 domain is indispensable for synaptogenic activity whereas Ig-like 2 domain is secondarily responsible for the activity. {ECO:0000269|PubMed:28864826}. TISSUE SPECIFICITY: Expressed in brain (at protein levels) (PubMed:28864826). Highly expressed in the pyramidal cell layer of the dorsal and ventral hippocampal CA1 and CA3 regions, layers 5 and 6 of the cortex, the thalamus and the pons and weakly expressed in the cerebellum (PubMed:28864826). Expressed in neurons but not in glia (PubMed:28864826). {ECO:0000269|PubMed:28864826}. +A8E0Y8 IGSF2_MOUSE Immunoglobulin superfamily member 2 (IgSF2) (Glu-Trp-Ile EWI motif-containing protein 101) (EWI-101) (CD antigen CD101) 1033 114,205 Chain (1); Disulfide bond (7); Domain (7); Glycosylation (2); Motif (1); Natural variant (10); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 971 991 Helical. {ECO:0000255}. TOPO_DOM 21 970 Extracellular. {ECO:0000255}.; TOPO_DOM 992 1033 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a role as inhibitor of T-cells proliferation induced by CD3. Inhibits expression of IL2RA on activated T-cells and secretion of IL2. Inhibits tyrosine kinases that are required for IL2 production and cellular proliferation. Inhibits phospholipase C-gamma-1/PLCG1 phosphorylation and subsequent CD3-induced changes in intracellular free calcium. Prevents nuclear translocation of nuclear factor of activated T-cell to the nucleus. Plays a role in the inhibition of T-cell proliferation via IL10 secretion by cutaneous dendritic cells (By similarity). {ECO:0000250}. PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q8K5B1 IL31R_MOUSE Interleukin-31 receptor subunit alpha (IL-31 receptor subunit alpha) (IL-31R subunit alpha) (IL-31R-alpha) (IL-31RA) (GLM-R) (mGLM-R) (Gp130-like monocyte receptor) (Gp130-like receptor) (Novel cytokine receptor 10) (NR10) (ZcytoR17) 716 80,580 Alternative sequence (9); Chain (1); Domain (5); Glycosylation (4); Sequence conflict (13); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 500 520 Helical. {ECO:0000255}. TOPO_DOM 19 499 Extracellular. {ECO:0000255}.; TOPO_DOM 521 716 Cytoplasmic. {ECO:0000255}. FUNCTION: Associates with OSMR to form the interleukin-31 receptor which activates STAT3 and to a lower extent STAT1 and STAT5. May function in skin immunity (PubMed:15184896). Mediates IL31-induced itch, probably in a manner dependent on cation channels TRPA1 and TRPV1 (PubMed:24373353). Positively regulates numbers and cycling status of immature subsets of myeloid progenitor cells in bone marrow in vivo and enhances myeloid progenitor cell survival in vitro (PubMed:17379091). {ECO:0000269|PubMed:15184896, ECO:0000269|PubMed:17379091, ECO:0000269|PubMed:24373353}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q8NI17}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25847241}; Single-pass type I membrane protein {ECO:0000305}. Cell junction, synapse, presynaptic cell membrane {ECO:0000269|PubMed:25381841}. Cell projection, axon {ECO:0000269|PubMed:25381841}. SUBUNIT: Heterodimer with OSMR. Interacts with JAK1 and STAT3. {ECO:0000250|UniProtKB:Q8NI17}. TISSUE SPECIFICITY: Expressed in a subset of dorsal root ganglia neurons (PubMed:16926070, PubMed:24373353, PubMed:25381841). Expressed in spinal cord and trigeminal ganglion (at protein level) (PubMed:25381841). Expressed in skin, testis, bone marrow and thymus (PubMed:15184896). {ECO:0000269|PubMed:15184896, ECO:0000269|PubMed:16926070, ECO:0000269|PubMed:24373353, ECO:0000269|PubMed:25381841}. +Q8BVZ5 IL33_MOUSE Interleukin-33 (IL-33) [Cleaved into: Interleukin-33(102-266); Interleukin-33(109-266)] 266 29,991 Beta strand (13); Chain (3); Helix (2); Propeptide (1); Region (2); Sequence conflict (3); Site (2); Turn (2) "FUNCTION: Cytokine that binds to and signals through the IL1RL1/ST2 receptor which in turn activates NF-kappa-B and MAPK signaling pathways in target cells. Involved in the maturation of Th2 cells inducing the secretion of T-helper type 2-associated cytokines. Also involved in activation of mast cells, basophils, eosinophils and natural killer cells. Acts as a chemoattractant for Th2 cells, and may function as an ""alarmin"", that amplifies immune responses during tissue injury.; FUNCTION: In quiescent endothelia the uncleaved form is constitutively and abundantly expressed, and acts as a chromatin-associated nuclear factor with transcriptional repressor properties, it may sequester nuclear NF-kappaB/RELA, lowering expression of its targets. This form is rapidely lost upon angiogenic or proinflammatory activation." PTM: The full-length protein can be released from cells and is able to signal via the IL1RL1/ST2 receptor. However, proteolytic processing by CSTG/cathepsin G and ELANE/neutrophil elastase produces C-terminal peptides that are more active than the unprocessed full-length protein. May also be proteolytically processed by calpains. Proteolytic cleavage mediated by apoptotic caspases including CASP3 and CASP7 results in IL33 inactivation. In vitro proteolytic cleavage by CASP1 was reported (PubMed:16286016) but could not be confirmed in vivo (PubMed:19465481) suggesting that IL33 is probably not a direct substrate for that caspase. {ECO:0000269|PubMed:16286016, ECO:0000269|PubMed:19465481, ECO:0000269|PubMed:22307629}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19465481}. Chromosome {ECO:0000250|UniProtKB:O95760}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniProtKB:O95760}. Secreted {ECO:0000269|PubMed:19465481}. Note=Associates with heterochromatin and mitotic chromosomes. {ECO:0000250|UniProtKB:O95760}. SUBUNIT: Forms a 1:1:1 heterotrimeric complex with its primary high-affinity receptor IL1RL1 and the coreceptor IL1RAP. {ECO:0000250}. DOMAIN: The homeodomain-like HTH domain mediates nuclear localization and heterochromatin association. {ECO:0000250}. +P48168 GLRB_MOUSE Glycine receptor subunit beta (Glycine receptor 58 kDa subunit) 496 55,951 Chain (1); Disulfide bond (2); Glycosylation (2); Modified residue (1); Natural variant (4); Region (1); Sequence conflict (1); Signal peptide (1); Site (1); Topological domain (4); Transmembrane (4) TRANSMEM 269 290 Helical; Name=1. {ECO:0000250|UniProtKB:P23415}.; TRANSMEM 296 316 Helical; Name=2. {ECO:0000250|UniProtKB:P23415}.; TRANSMEM 328 348 Helical; Name=3. {ECO:0000250|UniProtKB:P23415}.; TRANSMEM 475 495 Helical; Name=4. {ECO:0000250|UniProtKB:P23415}. TOPO_DOM 23 268 Extracellular. {ECO:0000250|UniProtKB:P23415}.; TOPO_DOM 291 295 Cytoplasmic. {ECO:0000250|UniProtKB:P23415}.; TOPO_DOM 317 327 Extracellular. {ECO:0000250|UniProtKB:P23415}.; TOPO_DOM 349 474 Cytoplasmic. {ECO:0000250|UniProtKB:P23415}. FUNCTION: Glycine receptors are ligand-gated chloride channels. GLRB does not form ligand-gated ion channels by itself, but is part of heteromeric ligand-gated chloride channels. Channel opening is triggered by extracellular glycine (PubMed:12809985). Heteropentameric channels composed of GLRB and GLRA1 are activated by lower glycine levels than homopentameric GLRA1. Plays an important role in the down-regulation of neuronal excitability. Contributes to the generation of inhibitory postsynaptic currents (PubMed:12809985, PubMed:16672662). {ECO:0000250|UniProtKB:P48167, ECO:0000269|PubMed:12809985, ECO:0000269|PubMed:16672662}. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane {ECO:0000269|PubMed:22592841}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P23415}. Cell junction, synapse {ECO:0000269|PubMed:19723286, ECO:0000269|PubMed:22592841}. Cell projection, dendrite {ECO:0000269|PubMed:19723286}. Cell membrane {ECO:0000269|PubMed:12809985}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P23415}. Cytoplasm {ECO:0000250|UniProtKB:P48167}. Note=Retained in the cytoplasm upon heterologous expression by itself. Coexpression with GPHN promotes expression at the cell membrane. Coexpression with GLRA1, GLRA2 or GLRA3 promotes expression at the cell membrane. {ECO:0000250|UniProtKB:P20781}. SUBUNIT: Heteropentamer composed of GLRB and GLRA1. Heteropentamer composed of GLRB and GLRA2. Heteropentamer composed of GLRB and GLRA3. Heteropentamer composed of two GLRA1 and three GLRB subunits. Heteropentamer composed of three GLRA1 and two GLRB subunits. Interacts with GPHN. {ECO:0000250|UniProtKB:P48167}. TISSUE SPECIFICITY: Detected in spinal cord, brain and brain stem, especially in the periolivary region, spinal nuclei, trigeminal nucleus, medulla oblongata, pons and midbrain. Detected in the inner plexiform layer of the retina (at protein level) (PubMed:22592841). High levels of expression in cortex, hippocampus, thalamus and cerebellum (PubMed:7920630). Detected in spinal cord (PubMed:7946325). {ECO:0000269|PubMed:22592841, ECO:0000269|PubMed:7920630, ECO:0000269|PubMed:7946325}. DISEASE: Note=Defects in Glrb cause the spastic condition which is characterized by muscle rigidity, tremors, myoclonic jerks, pronounced startle reaction, abnormal gait and impaired righting ability (PubMed:7920630). Neurons from the ventral horn of the spinal cord display reduced inhibitory postsynaptic currents (PubMed:12809985). Likewise, hypoglossal neurons display a dramatic reduction in the frequency and amplitude of postsynaptic inhibitory currents (PubMed:16672662). {ECO:0000269|PubMed:12809985, ECO:0000269|PubMed:16672662, ECO:0000269|PubMed:7920630}. +Q9QUH0 GLRX1_MOUSE Glutaredoxin-1 (Thioltransferase-1) (TTase-1) 107 11,871 Chain (1); Disulfide bond (2); Domain (1); Initiator methionine (1); Modified residue (2); Mutagenesis (2) FUNCTION: Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins. SUBCELLULAR LOCATION: Cytoplasm. +P26952 IL3RA_MOUSE Interleukin-3 receptor subunit alpha (IL-3 receptor subunit alpha) (IL-3R subunit alpha) (IL-3R-alpha) (IL-3RA) (Interleukin-3 receptor class II alpha chain) (CD antigen CD123) 396 43,195 Alternative sequence (2); Chain (1); Glycosylation (5); Motif (2); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 332 355 Helical. {ECO:0000255}. TOPO_DOM 17 331 Extracellular. {ECO:0000255}.; TOPO_DOM 356 396 Cytoplasmic. {ECO:0000255}. FUNCTION: In mouse, there are two classes of high-affinity IL3 receptors. One contains an IL3-specific beta subunit and the other contains the beta subunit also shared by high-affinity IL5 and GM-CSF receptors. SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I membrane protein. Note=Expressed on the cell surface.; SUBCELLULAR LOCATION: Isoform 2: Endomembrane system; Single-pass type I membrane protein. Note=Mostly distributed inside the cells, except in the nuclei and is not transported to the cell surface. SUBUNIT: Heterodimer of an alpha and a beta subunit. DOMAIN: The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.; DOMAIN: The box 1 motif is required for JAK interaction and/or activation. +P26955 IL3RB_MOUSE Cytokine receptor common subunit beta (GM-CSF/IL-3/IL-5 receptor common beta subunit) (CD antigen CD131) 896 99,036 Chain (1); Disulfide bond (5); Domain (2); Glycosylation (3); Modified residue (3); Motif (2); Sequence conflict (6); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 442 463 Helical. {ECO:0000255}. TOPO_DOM 23 441 Extracellular. {ECO:0000255}.; TOPO_DOM 464 896 Cytoplasmic. {ECO:0000255}. FUNCTION: High affinity receptor for interleukin-3, interleukin-5 and granulocyte-macrophage colony-stimulating factor. PTM: May be phosphorylated by LYN. {ECO:0000269|PubMed:10672044}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Heterodimer of an alpha and a beta subunit. The beta subunit is common to the IL3, IL5 and GM-CSF receptors. The signaling GM-CSF receptor complex is a dodecamer of two head-to-head hexamers of two alpha, two beta, and two ligand subunits. Interacts with TMEM102; this interaction occurs preferentially in the absence of CSF2 (By similarity). Interacts with FCER1G; this interaction is direct (PubMed:19098920). Interacts with LYN. {ECO:0000250, ECO:0000269|PubMed:10672044, ECO:0000269|PubMed:19098920}. DOMAIN: The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.; DOMAIN: The box 1 motif is required for JAK interaction and/or activation. +D3Z7P3 GLSK_MOUSE Glutaminase kidney isoform, mitochondrial (GLS) (EC 3.5.1.2) 674 73,964 Alternative sequence (1); Beta strand (15); Binding site (7); Chain (1); Compositional bias (2); Erroneous initiation (1); Helix (21); Modified residue (4); Mutagenesis (1); Repeat (2); Transit peptide (1); Turn (5) FUNCTION: Catalyzes the first reaction in the primary pathway for the renal catabolism of glutamine. Plays a role in maintaining acid-base homeostasis. Regulates the levels of the neurotransmitter glutamate in the brain. {ECO:0000269|PubMed:16641247, ECO:0000269|PubMed:22228304, ECO:0000269|PubMed:22373647}. SUBCELLULAR LOCATION: Isoform 1: Cytoplasm, cytosol {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 2: Mitochondrion. SUBUNIT: Homotetramer. Interacts with ATCAY; the interaction is direct and may control GLS localization, negatively regulating its activity. {ECO:0000269|PubMed:16899818, ECO:0000269|PubMed:22228304}. +Q8K0R6 GLTD2_MOUSE Glycolipid transfer protein domain-containing protein 2 321 34,453 Chain (1) +Q9D2N8 GLT15_MOUSE Polypeptide N-acetylgalactosaminyltransferase 15 (EC 2.4.1.41) (Polypeptide GalNAc transferase-like protein 2) (GalNAc-T-like protein 2) (pp-GaNTase-like protein 2) (Polypeptide N-acetylgalactosaminyltransferase-like protein 2) (Protein-UDP acetylgalactosaminyltransferase-like protein 2) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 2) 638 72,321 Binding site (3); Chain (1); Disulfide bond (5); Domain (1); Glycosylation (1); Metal binding (3); Region (2); Topological domain (2); Transmembrane (1) TRANSMEM 13 35 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 12 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 36 638 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Although it displays a much weaker activity toward all substrates tested compared to GALNT2, it is able to transfer up to seven GalNAc residues to the Muc5AC peptide, suggesting that it can fill vicinal Thr/Ser residues in cooperation with other GALNT proteins. Prefers Muc1a as substrate (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. DOMAIN: There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding. {ECO:0000250}.; DOMAIN: The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity. {ECO:0000250}. TISSUE SPECIFICITY: Specifically expressed in testis. {ECO:0000269|PubMed:12651884}. +O08795 GLU2B_MOUSE Glucosidase 2 subunit beta (80K-H protein) (Glucosidase II subunit beta) (Protein kinase C substrate 60.1 kDa protein heavy chain) (PKCSH) 521 58,793 Alternative sequence (1); Beta strand (5); Binding site (2); Calcium binding (1); Chain (1); Compositional bias (1); Disulfide bond (5); Domain (5); Glycosylation (2); Helix (2); Metal binding (12); Modified residue (7); Motif (1); Signal peptide (1) Glycan metabolism; N-glycan metabolism. FUNCTION: Regulatory subunit of glucosidase II that cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature glycoproteins (PubMed:27462106, PubMed:9148925). Required for efficient PKD1/Polycystin-1 biogenesis and trafficking to the plasma membrane of the primary cilia (PubMed:21685914). {ECO:0000269|PubMed:21685914, ECO:0000269|PubMed:27462106, ECO:0000269|PubMed:9148925}. SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000255|PROSITE-ProRule:PRU10138}. SUBUNIT: Heterodimer of a catalytic alpha subunit (GANAB) and a beta subunit (PRKCSH) (PubMed:9148925, PubMed:27462106). Binds glycosylated PTPRC (PubMed:9148925). {ECO:0000269|PubMed:27462106, ECO:0000269|PubMed:9148925}. TISSUE SPECIFICITY: Expressed in kidney (at protein level). {ECO:0000269|PubMed:21685914}. +Q8K1B9 GLT18_MOUSE Polypeptide N-acetylgalactosaminyltransferase 18 (EC 2.4.1.41) (Polypeptide GalNAc transferase 18) (GalNAc-T18) (Polypeptide GalNAc transferase-like protein 4) (GalNAc-T-like protein 4) (pp-GaNTase-like protein 4) (Polypeptide N-acetylgalactosaminyltransferase-like protein 4) (Protein-UDP acetylgalactosaminyltransferase-like protein 4) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 4) 622 71,096 Binding site (3); Chain (1); Disulfide bond (5); Domain (1); Glycosylation (3); Metal binding (3); Region (2); Topological domain (2); Transmembrane (1) TRANSMEM 13 35 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 12 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 36 622 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. DOMAIN: There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding. {ECO:0000250}.; DOMAIN: The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity. {ECO:0000250}. +P55095 GLUC_MOUSE Glucagon [Cleaved into: Glicentin; Glicentin-related polypeptide (GRPP); Oxyntomodulin (OXM) (OXY); Glucagon; Glucagon-like peptide 1 (GLP-1); Glucagon-like peptide 1(7-37) (GLP-1(7-37)); Glucagon-like peptide 1(7-36) (GLP-1(7-36)); Glucagon-like peptide 2 (GLP-2)] 180 20,906 Modified residue (6); Peptide (8); Propeptide (2); Signal peptide (1); Site (6) FUNCTION: Glucagon plays a key role in glucose metabolism and homeostasis. Regulates blood glucose by increasing gluconeogenesis and decreasing glycolysis. A counterregulatory hormone of insulin, raises plasma glucose levels in response to insulin-induced hypoglycemia (By similarity). {ECO:0000250}.; FUNCTION: GLP-1 is a potent stimulator of glucose-dependent insulin release. Play important roles on gastric motility and the suppression of plasma glucagon levels. May be involved in the suppression of satiety and stimulation of glucose disposal in peripheral tissues, independent of the actions of insulin. Have growth-promoting activities on intestinal epithelium. May also regulate the hypothalamic pituitary axis (HPA) via effects on LH, TSH, CRH, oxytocin, and vasopressin secretion. Increases islet mass through stimulation of islet neogenesis and pancreatic beta cell proliferation (By similarity). {ECO:0000250}.; FUNCTION: GLP-2 stimulates intestinal growth and up-regulates villus height in the small intestine, concomitant with increased crypt cell proliferation and decreased enterocyte apoptosis. The gastrointestinal tract, from the stomach to the colon is the principal target for GLP-2 action. Plays a key role in nutrient homeostasis, enhancing nutrient assimilation through enhanced gastrointestinal function, as well as increasing nutrient disposal. Stimulates intestinal glucose transport and decreases mucosal permeability (By similarity). {ECO:0000250}.; FUNCTION: Oxyntomodulin significantly reduces food intake. {ECO:0000250}.; FUNCTION: Glicentin may modulate gastric acid secretion and gastro-pyloro-duodenal activity. {ECO:0000269|PubMed:1886889}. PTM: Proglucagon is post-translationally processed in a tissue-specific manner in pancreatic A cells and intestinal L cells. In pancreatic A cells, the major bioactive hormone is glucagon cleaved by PCSK2/PC2. In the intestinal L cells PCSK1/PC1 liberates GLP-1, GLP-2, glicentin and oxyntomodulin. GLP-1 is further N-terminally truncated by post-translational processing in the intestinal L cells resulting in GLP-1(7-37) GLP-1-(7-36)amide. The C-terminal amidation is neither important for the metabolism of GLP-1 nor for its effects on the endocrine pancreas (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Glucagon is secreted in the A cells of the islets of Langerhans. GLP-1, GLP-2, oxyntomodulin and glicentin are secreted from enteroendocrine cells throughout the gastrointestinal tract. GLP-1 and GLP-2 are also secreted in selected neurons in the brain. +P04401 IL5_MOUSE Interleukin-5 (IL-5) (B-cell growth factor II) (BCGF-II) (Cytotoxic T-lymphocyte inducer) (Eosinophil differentiation factor) (T-cell replacing factor) (TRF) 133 15,410 Beta strand (3); Chain (1); Disulfide bond (2); Glycosylation (3); Helix (6); Signal peptide (1); Turn (1) FUNCTION: Factor that induces terminal differentiation of late-developing B-cells to immunoglobulin secreting cells. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Homodimer; disulfide-linked. +Q9Z1X4 ILF3_MOUSE Interleukin enhancer-binding factor 3 898 96,021 Alternative sequence (3); Beta strand (17); Chain (1); Compositional bias (5); Cross-link (3); Domain (3); Frameshift (2); Helix (16); Modified residue (18); Motif (1); Region (1); Sequence conflict (1); Turn (6) FUNCTION: RNA-binding protein that plays an essential role in the biogenesis of circular RNAs (circRNAs) which are produced by back-splicing circularization of pre-mRNAs. Within the nucleus, promotes circRNAs processing by stabilizing the regulatory elements residing in the flanking introns of the circularized exons. Plays thereby a role in the back-splicing of a subset of circRNAs. As a consequence, participates in a wide range of transcriptional and post-transcriptional processes. Binds to poly-U elements and AU-rich elements (AREs) in the 3'-UTR of target mRNAs (By similarity). Upon viral infection, ILF3 accumulates in the cytoplasm and participates in the innate antiviral response. Mechanistically, ILF3 becomes phosphorylated and activated by the double-stranded RNA-activated protein kinase/PKR which releases ILF3 from cellular mature circRNAs. In turn, unbound ILF3 molecules are able to interact with and thus inhibit viral mRNAs. {ECO:0000250|UniProtKB:Q12906, ECO:0000269|PubMed:21123651}. PTM: Phosphorylated at Thr-188 and Thr-315 by PKR in response to RNA viruses. This phosphorylation results in the dissociation of ILF2 from the ILF2-ILF3 complex resulting in a cytoplasmic sequestration of ILF3 where it can bind to viral RNAs and impede viral replication. {ECO:0000269|PubMed:21123651}.; PTM: Methylated by protein arginine N-methyltransferase 1. {ECO:0000250|UniProtKB:Q12906}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q12906}. Cytoplasm {ECO:0000269|PubMed:21123651}. Nucleus {ECO:0000269|PubMed:21123651}. Note=Localizes in the cytoplasm in response to viral infection. The unphosphorylated form is retained in the nucleus by ILF2. Phosphorylation at Thr-188 and Thr-315 causes the dissociation of ILF2 from the ILF2-ILF3 complex resulting in a cytoplasmic sequestration of ILF3. Localized in cytoplasmic mRNP granules containing untranslated mRNAs. {ECO:0000269|PubMed:21123651}. SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with FUS and SMN. Interacts (via C-terminus) with PRMT1. Forms a complex with ILF2. Can also bind to PRKDC/XRCC7: this may stabilize the interaction of PRKDC/XRCC7 and the heterodimeric complex of XRCC6/KU70 and XRCC5/KU80. Forms a heteromeric complex with ZNF346 and ILF3. Found in a nuclear export complex with XPO5, ILF3, Ran and double-stranded RNA or double-stranded minihelix VA1 RNA. Found in a nuclear export complex with XPO5, RAN, ILF3, ZNF346 and double-stranded RNA. Interacts with XPO5 and ZNF346. Forms a complex with ILF2, YLPM1, KHDRBS1, RBMX, NCOA5 and PPP1CA. Interacts with AGO1 and AGO2. Interacts with DHX36; this interaction occurs in a RNA-dependent manner. Interacts with ELAVL1; this interaction occurs in a RNA-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q12906}. TISSUE SPECIFICITY: Ubiquitous. Expressed at high levels in the thymus, testis, ovary and at lower levelss in the spleen. +Q9ERS7 ILRL2_MOUSE Interleukin-1 receptor-like 2 (IL-36 receptor) (Interleukin-1 receptor-related protein 2) (IL-1Rrp2) (IL1R-rp2) 574 65,108 Chain (1); Disulfide bond (3); Domain (4); Glycosylation (9); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 339 359 Helical. {ECO:0000255}. TOPO_DOM 22 338 Extracellular. {ECO:0000255}.; TOPO_DOM 360 574 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for interleukin-36 (IL36A, IL36B and IL36G). After binding to interleukin-36 associates with the coreceptor IL1RAP to form the interleukin-36 receptor complex which mediates interleukin-36-dependent activation of NF-kappa-B, MAPK and other pathways. The IL-36 signaling system is thought to be present in epithelial barriers and to take part in local inflammatory response; it is similar to the IL-1 system. Seems to be involved in skin inflammatory response by induction of the IL-23/IL-17/IL-22 pathway. {ECO:0000269|PubMed:21860022, ECO:0000269|PubMed:23064362}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Interacts with IL1RAP; the association is enhanced by IL36B indicative for an functional signaling complex and inhibited by IL36RN. {ECO:0000269|PubMed:21965679}. TISSUE SPECIFICITY: Expressed in bone marrow-derived dendritic cells, splenic CD4(+) T-cells, bone marrow-derived macrophages and bone marrow-derived neutrophils. {ECO:0000269|PubMed:21860022}. +Q7TQC7 GPTC2_MOUSE G patch domain-containing protein 2 527 58,218 Alternative sequence (2); Chain (1); Domain (1); Modified residue (3); Sequence conflict (2) FUNCTION: Enhances the ATPase activity of DHX15 in vitro. {ECO:0000250|UniProtKB:Q9NW75}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q9NW75}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9NW75}. SUBUNIT: Interacts with DHX15. {ECO:0000250|UniProtKB:Q9NW75}. +Q6IR34 GPSM1_MOUSE G-protein-signaling modulator 1 (Activator of G-protein signaling 3) 673 74,362 Alternative sequence (5); Chain (1); Domain (4); Erroneous initiation (2); Modified residue (10); Region (2); Repeat (9); Sequence conflict (1) FUNCTION: Guanine nucleotide dissociation inhibitor (GDI) which functions as a receptor-independent activator of heterotrimeric G-protein signaling. Keeps G(i/o) alpha subunit in its GDP-bound form thus uncoupling heterotrimeric G-proteins signaling from G protein-coupled receptors. Controls spindle orientation and asymmetric cell fate of cerebral cortical progenitors. May also be involved in macroautophagy in intestinal cells. May play a role in drug addiction. {ECO:0000269|PubMed:16009138}. PTM: Phosphorylation regulates interaction with G(i/o) alpha. {ECO:0000269|PubMed:12719437}. SUBCELLULAR LOCATION: Cytoplasm, cytosol. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. SUBUNIT: Interacts with GNAI1 and GNAI2 preferentially in their GDP-bound state. May also interact with GNAO1. Interacts with INSC/inscuteable and FRMPD1 (By similarity). Interacts with GNAI3. Interacts with STK11/LKB1 and MACF1. {ECO:0000250, ECO:0000269|PubMed:12719437, ECO:0000269|PubMed:16009138}. DOMAIN: The GoLoco domains are essential for the GDI activity toward G(i/o) alpha. The GoLoco domains mediate interaction with G(i/o) alpha (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in neural progenitor cells (at protein level). {ECO:0000269|PubMed:16009138}. +Q9CX99 GRAP_MOUSE GRB2-related adapter protein 217 25,277 Chain (1); Domain (3) FUNCTION: Couples signals from receptor and cytoplasmic tyrosine kinases to the Ras signaling pathway. {ECO:0000250}. SUBUNIT: Associates through its SH2 domain with ligand-activated receptors for stem cell factor (KIT) and erythropoietin (EPOR). Also forms a stable complex with the Bcr-Abl oncoprotein. GRAP is associated with the Ras guanine nucleotide exchange factor SOS1, primarily through its N-terminal SH3 domain. Interacts with phosphorylated LAT upon TCR activation. Interacts with SHB (By similarity). {ECO:0000250}. +P04187 GRAB_MOUSE Granzyme B(G,H) (EC 3.4.21.79) (CTLA-1) (Cytotoxic cell protease 1) (CCP1) (Fragmentin-2) 247 27,470 Active site (3); Chain (1); Disulfide bond (3); Domain (1); Glycosylation (2); Propeptide (1); Signal peptide (1); Site (1) FUNCTION: This enzyme is necessary for target cell lysis in cell-mediated immune responses. It cleaves after Asp. Seems to be linked to an activation cascade of caspases (aspartate-specific cysteine proteases) responsible for apoptosis execution. Cleaves caspase-3, -7, -9 and 10 to give rise to active enzymes mediating apoptosis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasmic granule. Note=Cytoplasmic granules of cytolytic T-lymphocytes and natural killer cells. +P11033 GRAD_MOUSE Granzyme D (EC 3.4.21.-) 252 27,955 Active site (3); Chain (1); Disulfide bond (3); Domain (1); Erroneous gene model prediction (1); Glycosylation (5); Propeptide (1); Sequence conflict (2); Signal peptide (1) FUNCTION: This enzyme is probably necessary for target cell lysis in cell-mediated immune responses. SUBCELLULAR LOCATION: Cytoplasmic granule. Note=Cytoplasmic granules of cytolytic T-lymphocytes. +Q9Z2W8 GRIA4_MOUSE Glutamate receptor 4 (GluR-4) (GluR4) (AMPA-selective glutamate receptor 4) (GluR-D) (Glutamate receptor ionotropic, AMPA 4) (GluA4) 902 100,847 Binding site (3); Chain (1); Disulfide bond (2); Glycosylation (5); Intramembrane (2); Lipidation (2); Modified residue (1); Region (2); Sequence conflict (4); Signal peptide (1); Topological domain (5); Transmembrane (3) INTRAMEM 593 608 Helical; Pore-forming. {ECO:0000250}.; INTRAMEM 609 611 {ECO:0000250}. TRANSMEM 545 565 Helical. {ECO:0000250}.; TRANSMEM 618 638 Helical. {ECO:0000250}.; TRANSMEM 814 834 Helical; Name=M4. {ECO:0000250}. TOPO_DOM 22 544 Extracellular. {ECO:0000250}.; TOPO_DOM 566 592 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 612 617 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 639 813 Extracellular. {ECO:0000250}.; TOPO_DOM 835 902 Cytoplasmic. {ECO:0000250}. FUNCTION: Receptor for glutamate that functions as ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. In the presence of CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of glutamate (By similarity). {ECO:0000250}. PTM: Palmitoylated. Depalmitoylated upon glutamate stimulation. Cys-611 palmitoylation leads to Golgi retention and decreased cell surface expression. In contrast, Cys-837 palmitoylation does not affect cell surface expression but regulates stimulation-dependent endocytosis (By similarity). {ECO:0000250}.; PTM: Phosphorylated at Ser-862 by PRKCG; phosphorylation increases plasma membrane-associated GRI4 expression. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein. Cell projection, dendrite. Note=Interaction with CNIH2, CNIH3 and PRKCG promotes cell surface expression. {ECO:0000250}. SUBUNIT: Homotetramer or heterotetramer of pore-forming glutamate receptor subunits. Tetramers may be formed by the dimerization of dimers. Interacts with EPB41L1 via its C-terminus (By similarity). Found in a complex with GRIA1, GRIA2, GRIA3, CNIH2, CNIH3, CACNG2, CACNG3, CACNG4, CACNG5, CACNG7 and CACNG8. Interacts with CACNG5 and PRKCG (By similarity). {ECO:0000250}. DOMAIN: The M4 transmembrane segment mediates tetramerization and is required for cell surface expression. {ECO:0000250}. +Q9D892 ITPA_MOUSE Inosine triphosphate pyrophosphatase (ITPase) (Inosine triphosphatase) (EC 3.6.1.9) (Non-canonical purine NTP pyrophosphatase) (Non-standard purine NTP pyrophosphatase) (Nucleoside-triphosphate diphosphatase) (Nucleoside-triphosphate pyrophosphatase) (NTPase) 198 21,897 Binding site (2); Chain (1); Initiator methionine (1); Metal binding (2); Modified residue (2); Region (4); Sequence conflict (2) FUNCTION: Pyrophosphatase that hydrolyzes the non-canonical purine nucleotides inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) as well as 2'-deoxy-N-6-hydroxylaminopurine triposphate (dHAPTP) and xanthosine 5'-triphosphate (XTP) to their respective monophosphate derivatives. The enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions. {ECO:0000255|HAMAP-Rule:MF_03148, ECO:0000269|PubMed:17090528, ECO:0000269|PubMed:20081199, ECO:0000269|PubMed:20601097}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03148}. SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03148}. +Q3V3G7 GRM2A_MOUSE GRAM domain-containing protein 2A (GRAM domain-containing protein 2) 320 36,441 Alternative sequence (1); Chain (1); Domain (1); Transmembrane (1) TRANSMEM 278 298 Helical. {ECO:0000255}. FUNCTION: Participates in the organization ofendoplasmic reticulum-plasma membrane contact sites (EPCS) with pleiotropic functions including STIM1 recruitment and calcium homeostasis. Constitutive tether that co-localize with ESYT2/3 tethers at endoplasmic reticulum-plasma membrane contact sites in a phosphatidylinositol lipid-dependent manner. Pre-marks the subset of phosphtidylinositol 4,5-biphosphate (PI(4,5)P2)-enriched EPCS destined for the store operated calcium entry pathway (SOCE). {ECO:0000250|UniProtKB:Q8IUY3}. PTM: Phosphorylated. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8IUY3}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8IUY3}. Cell membrane {ECO:0000250|UniProtKB:Q8IUY3}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8IUY3}. Note=Localizes to endoplasmic reticulum-plasma membrane contact sites (EPCS). Anchored at the ER, PM binding is mediated via GRAM domain and phosphatidylinositol lipid interaction. Localizes to distinct EPCS than GRAMD1A. {ECO:0000250|UniProtKB:Q8IUY3}. DOMAIN: GRAM domain is required for specific location to eendoplasmic reticulum-plasma membrane contact sites (EPCS). Mediates interaction to phosphatidylinositol lipids and binding to plasma membrane. {ECO:0000250|UniProtKB:Q8IUY3}. +Q9QYS2 GRM3_MOUSE Metabotropic glutamate receptor 3 (mGluR3) 879 99,114 Binding site (4); Chain (1); Disulfide bond (8); Glycosylation (4); Region (1); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 577 599 Helical; Name=1. {ECO:0000255}.; TRANSMEM 614 634 Helical; Name=2. {ECO:0000255}.; TRANSMEM 646 664 Helical; Name=3. {ECO:0000255}.; TRANSMEM 689 709 Helical; Name=4. {ECO:0000255}.; TRANSMEM 735 756 Helical; Name=5. {ECO:0000255}.; TRANSMEM 770 792 Helical; Name=6. {ECO:0000255}.; TRANSMEM 803 828 Helical; Name=7. {ECO:0000255}. TOPO_DOM 23 576 Extracellular. {ECO:0000255}.; TOPO_DOM 600 613 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 635 645 Extracellular. {ECO:0000255}.; TOPO_DOM 665 688 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 710 734 Extracellular. {ECO:0000255}.; TOPO_DOM 757 769 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 793 802 Extracellular. {ECO:0000255}.; TOPO_DOM 829 879 Cytoplasmic. {ECO:0000255}. FUNCTION: G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Signaling inhibits adenylate cyclase activity. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBUNIT: Interacts with GRASP. {ECO:0000250}. +Q9Z1S3 GRP1_MOUSE RAS guanyl-releasing protein 1 (Calcium and DAG-regulated guanine nucleotide exchange factor II) (CalDAG-GEFII) (Ras guanyl-releasing protein) 795 90,304 Calcium binding (1); Chain (1); Coiled coil (1); Domain (4); Modified residue (2); Mutagenesis (1); Region (3); Sequence conflict (6); Zinc finger (1) FUNCTION: Functions as a calcium- and diacylglycerol (DAG)-regulated nucleotide exchange factor specifically activating Ras through the exchange of bound GDP for GTP. Activates the Erk/MAP kinase cascade. Regulates T-cell/B-cell development, homeostasis and differentiation by coupling T-lymphocyte/B-lymphocyte antigen receptors to Ras. Regulates NK cell cytotoxicity and ITAM-dependent cytokine production by activation of Ras-mediated ERK and JNK pathways (By similarity). Functions in mast cell degranulation and cytokine secretion, regulating FcERI-evoked allergic responses (PubMed:17190838). May also function in differentiation of other cell types. Proto-oncogene, which promotes T-cell lymphomagenesis when its expression is deregulated (PubMed:15829980, PubMed:17210708). {ECO:0000250|UniProtKB:O95267, ECO:0000269|PubMed:11017103, ECO:0000269|PubMed:12433368, ECO:0000269|PubMed:12538669, ECO:0000269|PubMed:12845332, ECO:0000269|PubMed:12932358, ECO:0000269|PubMed:14532295, ECO:0000269|PubMed:14970203, ECO:0000269|PubMed:15829980, ECO:0000269|PubMed:16301621, ECO:0000269|PubMed:16849453, ECO:0000269|PubMed:17190838, ECO:0000269|PubMed:17210708, ECO:0000269|PubMed:9819387}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Golgi apparatus membrane; Peripheral membrane protein. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Found both in the cytosol and associated with membranes. Relocalization to the cell membrane upon activation is F-actin-dependent (By similarity). Translocates to the Golgi in response to phorbol ester or nerve growth factor. Localizes to somata and dendrites but not to axons of hippocampal pyramidal cells (By similarity). {ECO:0000250}. SUBUNIT: Homodimer. Forms a signaling complex with DGKZ and HRAS. Interacts with F-actin. Interacts with SKAP1 (By similarity). {ECO:0000250|UniProtKB:O95267}. DOMAIN: The phorbol-ester/DAG-type zinc finger is the principal mediator of the targeting to membranes and is required for functional activation through DAG-binding.; DOMAIN: Two EF-hand domains are present. However, only EF-hand 1 (and not EF-hand 2) binds calcium. {ECO:0000250|UniProtKB:O95267}. TISSUE SPECIFICITY: Detected in spleen and thymus. Expressed by mature thymocytes and to a lower extent by bone marrow-derived mast cells (at protein level). Detected in B-cells and keratinocytes (at protein level). {ECO:0000269|PubMed:11017103, ECO:0000269|PubMed:12433368, ECO:0000269|PubMed:14532295, ECO:0000269|PubMed:14970203, ECO:0000269|PubMed:17190838, ECO:0000269|PubMed:9819387}. +P28798 GRN_MOUSE Granulins (PC cell-derived growth factor) (PCDGF) (Proepithelin) (PEPI) [Cleaved into: Acrogranin (Progranulin); Granulin-1; Granulin-2; Granulin-3; Granulin-4; Granulin-5; Granulin-6; Granulin-7] 589 63,458 Chain (1); Disulfide bond (10); Glycosylation (4); Peptide (7); Sequence conflict (5); Signal peptide (1) FUNCTION: Granulins have possible cytokine-like activity. They may play a role in inflammation, wound repair, and tissue remodeling. Acts as an autocrine growth factor for PC cells. {ECO:0000269|PubMed:8496151}. PTM: Granulins are disulfide bridged.; PTM: N-glycosylated. {ECO:0000269|PubMed:8496151}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8496151}. SUBUNIT: Acrogranin/Progranulin is secreted as a homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. +Q9Z329 ITPR2_MOUSE Inositol 1,4,5-trisphosphate receptor type 2 (IP3 receptor isoform 2) (IP3R 2) (InsP3R2) (Inositol 1,4,5-trisphosphate type V receptor) (Type 2 inositol 1,4,5-trisphosphate receptor) (Type 2 InsP3 receptor) 2701 307,475 Alternative sequence (3); Chain (1); Domain (5); Modified residue (7); Mutagenesis (8); Region (3); Sequence conflict (8); Topological domain (7); Transmembrane (6) TRANSMEM 2228 2248 Helical. {ECO:0000255}.; TRANSMEM 2261 2281 Helical. {ECO:0000255}.; TRANSMEM 2308 2328 Helical. {ECO:0000255}.; TRANSMEM 2352 2372 Helical. {ECO:0000255}.; TRANSMEM 2395 2415 Helical. {ECO:0000255}.; TRANSMEM 2521 2541 Helical. {ECO:0000255}. TOPO_DOM 1 2227 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 2249 2260 Extracellular. {ECO:0000255}.; TOPO_DOM 2282 2307 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 2329 2351 Extracellular. {ECO:0000255}.; TOPO_DOM 2373 2394 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 2416 2520 Extracellular. {ECO:0000255}.; TOPO_DOM 2542 2701 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for inositol 1,4,5-trisphosphate, a second messenger that mediates the release of intracellular calcium. This release is regulated by cAMP both dependently and independently of PKA. {ECO:0000269|PubMed:15632133, ECO:0000269|PubMed:19608738, ECO:0000269|PubMed:20189985}.; FUNCTION: Isoform 3 has neither inositol 1,4,5-trisphosphate binding activity nor calcium releasing activity. {ECO:0000269|PubMed:15632133}. PTM: Phosphorylation by cAMP-dependent PKA on Ser-937 increases calcium release. {ECO:0000269|PubMed:19608738}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15632133}; Multi-pass membrane protein {ECO:0000269|PubMed:15632133}. SUBUNIT: Homotetramer. Interacts with CABP1. Interacts with BOK; regulates ITPR2 expression. {ECO:0000250|UniProtKB:P29995}. DOMAIN: The receptor contains a calcium channel in its C-terminal extremity. Its large N-terminal cytoplasmic region has the ligand-binding site in the N-terminus and modulatory sites in the middle portion immediately upstream of the channel region. TISSUE SPECIFICITY: Isoforms 1 and 3 are widely expressed. Isoform 2 is found in skeletal muscle and heart. {ECO:0000269|PubMed:15632133}. +P70227 ITPR3_MOUSE Inositol 1,4,5-trisphosphate receptor type 3 (IP3 receptor isoform 3) (IP3R 3) (InsP3R3) (Type 3 inositol 1,4,5-trisphosphate receptor) (Type 3 InsP3 receptor) 2670 304,275 Beta strand (13); Chain (1); Domain (5); Helix (5); Modified residue (7); Mutagenesis (3); Region (3); Sequence conflict (4); Topological domain (7); Transmembrane (6); Turn (3) TRANSMEM 2234 2254 Helical. {ECO:0000255}.; TRANSMEM 2263 2283 Helical. {ECO:0000255}.; TRANSMEM 2293 2310 Helical. {ECO:0000255}.; TRANSMEM 2325 2345 Helical. {ECO:0000255}.; TRANSMEM 2368 2388 Helical. {ECO:0000255}.; TRANSMEM 2496 2516 Helical. {ECO:0000255}. TOPO_DOM 1 2233 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 2255 2262 Extracellular. {ECO:0000255}.; TOPO_DOM 2284 2292 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 2311 2324 Extracellular. {ECO:0000255}.; TOPO_DOM 2346 2367 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 2389 2495 Extracellular. {ECO:0000255}.; TOPO_DOM 2517 2670 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for inositol 1,4,5-trisphosphate, a second messenger that mediates the release of intracellular calcium. {ECO:0000269|PubMed:20813840, ECO:0000269|PubMed:21030605}. PTM: Phosphorylated on tyrosine residues (By similarity). Phosphorylated by AKT1 on serine and/or threonine residues. {ECO:0000250, ECO:0000269|PubMed:21030605}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15632133, ECO:0000269|PubMed:21030605}; Multi-pass membrane protein {ECO:0000269|PubMed:15632133, ECO:0000269|PubMed:21030605}. SUBUNIT: Homotetramer. Interacts with TRPC1, TRPC3, TRPC4. Interacts with TRPV4 (By similarity). Interacts with SIGMAR1 (PubMed:11149946). Interacts with AKT1 and PML (PubMed:21030605). Interacts with LRMP (via coiled-coil domain) (PubMed:20071408). Interacts with CABP1 (By similarity). Interacts with TMBIM4/LFG4 (By similarity). Interacts with CEMIP (By similarity). Interacts with TESPA1 (PubMed:23650607). Interacts with TMEM203 (By similarity). Interacts with BOK; regulates ITPR3 expression (By similarity). {ECO:0000250|UniProtKB:Q14573, ECO:0000250|UniProtKB:Q63269, ECO:0000269|PubMed:11149946, ECO:0000269|PubMed:20071408, ECO:0000269|PubMed:21030605, ECO:0000269|PubMed:23650607}. DOMAIN: The receptor contains a calcium channel in its C-terminal extremity. Its large N-terminal cytoplasmic region has the ligand-binding site in the N-terminus and modulatory sites in the middle portion immediately upstream of the channel region. +Q9CQ35 GRPL2_MOUSE GLIPR1-like protein 2 332 37,784 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (1); Erroneous termination (1); Glycosylation (1); Transmembrane (1) TRANSMEM 253 273 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q8R1I2 GRP_MOUSE Gastrin-releasing peptide (GRP) [Cleaved into: Neuromedin-C (GRP-10)] 146 15,659 Modified residue (1); Peptide (2); Propeptide (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Stimulates the release of gastrin and other gastrointestinal hormones (By similarity). Contributes to the perception of prurient stimuli and to the transmission of itch signals in the spinal cord that promote scratching behavior (PubMed:28280205, PubMed:17653196, PubMed:26658875). Contributes primarily to nonhistaminergic itch sensation (PubMed:28280205). Contributes to long-term fear memory, but not normal spatial memory (PubMed:12526815). Contributes to the regulation of food intake (PubMed:12176666). {ECO:0000250|UniProtKB:P63153, ECO:0000269|PubMed:12176666, ECO:0000269|PubMed:12526815, ECO:0000269|PubMed:17653196, ECO:0000269|PubMed:26658875, ECO:0000269|PubMed:28280205}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P07492}. Cytoplasmic vesicle, secretory vesicle lumen {ECO:0000250|UniProtKB:Q863C3}. TISSUE SPECIFICITY: Detected in the suprachiasmatic nucleus in the hypothalamus (PubMed:28280205). Detected in peptidergic dorsal root ganglion neurons (at protein level) (PubMed:17653196). Highly expressed both in the lateral nucleus of the amygdala, and in regions sending synaptic projections to the lateral nucleus (PubMed:12526815). {ECO:0000269|PubMed:12526815, ECO:0000269|PubMed:17653196, ECO:0000269|PubMed:28280205}. +Q8C5Q4 GRSF1_MOUSE G-rich sequence factor 1 (GRSF-1) 479 53,076 Chain (1); Compositional bias (1); Domain (3); Modified residue (2); Sequence conflict (4); Transit peptide (1) FUNCTION: Regulator of post-transcriptional mitochondrial gene expression, required for assembly of the mitochondrial ribosome and for recruitment of mRNA and lncRNA. Binds RNAs containing the 14 base G-rich element. Preferentially binds RNAs transcribed from three contiguous genes on the light strand of mtDNA, the ND6 mRNA, and the long non-coding RNAs for MT-CYB and MT-ND5, each of which contains multiple consensus binding sequences (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Mitochondrion matrix, mitochondrion nucleoid {ECO:0000250|UniProtKB:Q12849}. Note=Localizes to mitochondrial RNA granules found in close proximity to the mitochondrial nucleoids. {ECO:0000250|UniProtKB:Q12849}. SUBUNIT: Monomer. Found in a complex with DDX28, DHX30, FASTKD2 and FASTKD5. Interacts with the mitochondrial RNase P complex subunit TRMT10C/MRPP1. {ECO:0000250|UniProtKB:Q12849}. +Q9D3N8 GRTP1_MOUSE Growth hormone-regulated TBC protein 1 (TBC1 domain family member 6) 359 40,628 Alternative sequence (3); Chain (1); Domain (1); Sequence conflict (3) FUNCTION: May act as a GTPase-activating protein for Rab family protein(s). TISSUE SPECIFICITY: Highly expressed in testes, expression greatly increased at postnatal day 20 and remained high up to day 90. Moderately expressed in kidney and liver, weakly expressed in intestine, lung, ovaries and stomach. Expression of Growth hormone increased the expression in testis but decreased expression in liver and kidney. {ECO:0000269|PubMed:11564724}. +P10648 GSTA2_MOUSE Glutathione S-transferase A2 (EC 2.5.1.18) (GST class-alpha member 2) (Glutathione S-transferase GT41A) 222 25,542 Beta strand (5); Binding site (2); Chain (1); Domain (2); Helix (13); Initiator methionine (1); Modified residue (2); Region (2); Sequence conflict (1); Turn (1) FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. SUBUNIT: Homodimer. {ECO:0000269|PubMed:12549910}. +O70325 GPX4_MOUSE Phospholipid hydroperoxide glutathione peroxidase (PHGPx) (EC 1.11.1.12) (Glutathione peroxidase 4) (GPx-4) (GSHPx-4) 197 22,229 Active site (1); Alternative sequence (2); Beta strand (9); Chain (1); Helix (9); Modified residue (1); Mutagenesis (2); Non-standard residue (1); Sequence conflict (3); Transit peptide (1); Turn (2) FUNCTION: Essential antioxidant peroxidase that directly reduces phospholipid hydroperoxide even if they are incorporated in membranes and lipoproteins (PubMed:29290465). Can also reduce fatty acid hydroperoxide, cholesterol hydroperoxide and thymine hydroperoxide (By similarity). Plays a key role in protecting cells from oxidative damage by preventing membrane lipid peroxidation (PubMed:12566075). Required to prevent cells from ferroptosis, a non-apoptotic cell death resulting from an iron-dependent accumulation of lipid reactive oxygen species (PubMed:12566075, PubMed:24439385, PubMed:25402683, PubMed:25922076, PubMed:29290465). The presence of selenocysteine (Sec) versus Cys at the active site is essential for life: it provides resistance to overoxidation and prevents cells against ferroptosis (PubMed:29290465). The presence of Sec at the active site is also essential for the survival of a specific type of parvalbumin-positive interneurons, thereby preventing against fatal epileptic seizures (PubMed:29290465). May be required to protect cells from the toxicity of ingested lipid hydroperoxides (PubMed:12566075). Required for normal sperm development and male fertility (PubMed:19783653, PubMed:25922076). Essential for maturation and survival of photoreceptor cells (PubMed:22207760). Plays a role in a primary T-cell response to viral and parasitic infection by protecting T-cells from ferroptosis and by supporting T-cell expansion (PubMed:25824823). {ECO:0000250|UniProtKB:P36968, ECO:0000269|PubMed:12566075, ECO:0000269|PubMed:18762024, ECO:0000269|PubMed:19783653, ECO:0000269|PubMed:22207760, ECO:0000269|PubMed:24439385, ECO:0000269|PubMed:25402683, ECO:0000269|PubMed:25824823, ECO:0000269|PubMed:25922076, ECO:0000269|PubMed:29290465}.; FUNCTION: Isoform Cytoplasmic: Specifically able to suppress the production of leukotriene and prostaglandin in response to several stimuli by reducing fatty acid hydroperoxide. {ECO:0000250|UniProtKB:P36970}.; FUNCTION: Isoform Mitochondrial: Specifically required to prevent mitochondrial cell death by mediating reduction of cardiolipin hydroperoxide (By similarity). Also required for normal sperm development and male fertility (PubMed:19417079). {ECO:0000250|UniProtKB:P36970, ECO:0000269|PubMed:19417079}.; FUNCTION: Isoform Nuclear: Required for male fertility by stabilizing the condensed chromatin in sperm nuclei (PubMed:12566075). {ECO:0000269|PubMed:12566075}. SUBCELLULAR LOCATION: Isoform Mitochondrial: Mitochondrion {ECO:0000269|PubMed:12566075, ECO:0000269|PubMed:22207760}.; SUBCELLULAR LOCATION: Isoform Cytoplasmic: Cytoplasm {ECO:0000269|PubMed:12566075}.; SUBCELLULAR LOCATION: Isoform Nuclear: Nucleus {ECO:0000269|PubMed:11344099}. SUBUNIT: Monomer. Has a tendency to form higher mass oligomers. {ECO:0000250|UniProtKB:P36969}. TISSUE SPECIFICITY: Widely expressed with the highest levels in testis, heart, cerebrum, ileum, stomach, liver, jejunum and epididymis (PubMed:17503194). Expressed primarily in testis and sperm midpiece (at protein level) (PubMed:19417079, PubMed:12566075). Expressed in brain (at protein level) (PubMed:22207760, PubMed:12566075). Expressed in heart, liver and kidney (at protein level) (PubMed:12566075). Expressed in retina, especially in inner segments of photoreceptor cells (at protein level) (PubMed:22207760). Isoform Mitochondrial and isoform Cytoplasmic: Highly expressed during embryogenesis, while isoform Nuclear is weakly expressed (PubMed:1668477). Isoform Mitochondrial and isoform Nuclear are down-regulated between E14.5 and E17.5, while isoform Cytoplasmic remains constant (PubMed:1668477). Isoform Nuclear: Mainly expressed in sperm (PubMed:11344099). {ECO:0000269|PubMed:11344099, ECO:0000269|PubMed:12566075, ECO:0000269|PubMed:1668477, ECO:0000269|PubMed:17503194, ECO:0000269|PubMed:19417079, ECO:0000269|PubMed:22207760}. +Q03160 GRB7_MOUSE Growth factor receptor-bound protein 7 (Epidermal growth factor receptor GRB-7) (GRB7 adapter protein) 535 59,959 Chain (1); Domain (3); Modified residue (3); Mutagenesis (5) FUNCTION: Adapter protein that interacts with the cytoplasmic domain of numerous receptor kinases and modulates down-stream signaling. Promotes activation of down-stream protein kinases, including STAT3, AKT1, MAPK1 and/or MAPK3. Promotes activation of HRAS. Plays a role in signal transduction in response to EGF. Plays a role in the regulation of cell proliferation and cell migration (By similarity). Plays a role in the assembly and stability of RNA stress granules. Binds to the 5'UTR of target mRNA molecules and represses translation of target mRNA species, when not phosphorylated. Phosphorylation impairs RNA binding and promotes stress granule disassembly during recovery after cellular stress. {ECO:0000250, ECO:0000269|PubMed:17318180, ECO:0000269|PubMed:18273060}. PTM: Phosphorylated on serine and threonine residues in response to activation of receptor kinases. Phosphorylated on tyrosine residues by TEK/TIE2. Phosphorylated on tyrosine residues by PTK2/FAK1, and possibly also other kinases. Phosphorylation is enhanced by activation of receptor kinases. Tyrosine phosphorylation is essential for activation of down-stream protein kinases (By similarity). Phosphorylated on tyrosine residues in response to NTN1 signaling. Phosphorylation promotes stress granule disassembly during recovery after cellular stress. {ECO:0000250, ECO:0000269|PubMed:10521483, ECO:0000269|PubMed:17318180, ECO:0000269|PubMed:18273060}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18273060}. Cell projection {ECO:0000250|UniProtKB:Q14451}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q14451}. Cell membrane {ECO:0000250|UniProtKB:Q14451}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q14451}; Cytoplasmic side {ECO:0000250|UniProtKB:Q14451}. Cytoplasmic granule {ECO:0000269|PubMed:18273060}. Note=Predominantly cytoplasmic. Detected in stress granules where mRNA is stored under stress conditions. {ECO:0000269|PubMed:18273060}. SUBUNIT: Homodimer. Interacts (via SH2 domain) with EGFR, ERBB2, ERBB3 (when phosphorylated), ERBB4 (when phosphorylated), EPHB1, INSR, FGFR1, PDGFRA (tyrosine phosphorylated) and PDGFRB (tyrosine phosphorylated). Interacts with SHC1. Interacts with RND1. Interacts (when tyrosine phosphorylated) with FHL2 and HAX1 (By similarity). Interacts (via SH2 domain) with RET and PTK2/FAK1. Interacts (when not phosphorylated) with ELAVL1. In stressed cells, but not in normal cells, part of a complex that contains at least GRB7, PTK2/FAK1, STAU1, ELAVL1 and TIA1. Interacts (via SH2 domain) with KIT (phosphorylated). Interacts (via SH2 domain) with TEK/TIE2 (tyrosine phosphorylated). {ECO:0000250, ECO:0000269|PubMed:10377264, ECO:0000269|PubMed:10521483, ECO:0000269|PubMed:17318180, ECO:0000269|PubMed:18273060, ECO:0000269|PubMed:8631863, ECO:0000269|PubMed:8940081}. DOMAIN: The PH domain mediates interaction with membranes containing phosphoinositides. {ECO:0000250}. +Q3UHK3 GREB1_MOUSE Protein GREB1 1954 216,927 Chain (1); Compositional bias (1); Sequence caution (1); Sequence conflict (16); Transmembrane (1) TRANSMEM 1873 1893 Helical. {ECO:0000255}. FUNCTION: May play a role in estrogen-stimulated cell proliferation. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +O70326 GREM1_MOUSE Gremlin-1 (Cysteine knot superfamily 1, BMP antagonist 1) (Down-regulated in Mos-transformed cells protein) 184 20,710 Chain (1); Disulfide bond (4); Domain (1); Glycosylation (1); Signal peptide (1) FUNCTION: Cytokine that may play an important role during carcinogenesis and metanephric kidney organogenesis, as BMP a antagonist required for early limb outgrowth and patterning in maintaining the FGF4-SHH feedback loop (PubMed:12808456, PubMed:15201225). Down-regulates the BMP4 signaling in a dose-dependent manner (PubMed:15133038). Antagonist of BMP2; inhibits BMP2-mediated differentiation of osteoblasts (in vitro) (By similarity). Acts as inhibitor of monocyte chemotaxis (By similarity). {ECO:0000250|UniProtKB:O35793, ECO:0000250|UniProtKB:O60565, ECO:0000269|PubMed:12808456, ECO:0000269|PubMed:15133038, ECO:0000269|PubMed:15201225}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. SUBUNIT: Homodimer; can also form homooligomers. Interacts with BMP2; can form higher oligomers with BMP2 (By similarity). Interacts with SLIT1 and SLIT2 in a glycosylation-dependent manner (By similarity). {ECO:0000250|UniProtKB:O35793, ECO:0000250|UniProtKB:O60565}. TISSUE SPECIFICITY: Highly expressed in spleen and to a lesser extent in lung, skeletal muscle and kidney. Expressed only in non-transformed cells or primary fibroblasts in culture but not in established transformed or tumor derived cell lines. Broadly expressed in limb bud mesenchyme but restricted to the distal limb bud mesenchyme and concentrated posteriorly. Expressed in ovary especially in granulosa cells of follicles of type 4. {ECO:0000269|PubMed:10965135, ECO:0000269|PubMed:12808456, ECO:0000269|PubMed:15133038}. +Q921D9 GRHL1_MOUSE Grainyhead-like protein 1 homolog (Transcription factor CP2-like 2) (Transcription factor LBP-32) 618 70,176 Alternative sequence (2); Chain (1); Modified residue (1); Region (3) FUNCTION: Transcription factor involved in epithelial development. Binds directly to the consensus DNA sequence 5'-AACCGGTT-3' (PubMed:18288204, PubMed:21081122). Important regulator of DSG1 in the context of hair anchorage and epidermal differentiation, participates in the maintenance of the skin barrier (PubMed:18288204, PubMed:24586629). There is no genetic interaction with GRHL3 no genetic interaction with GRHL3, no functional cooperativity due to diverse target gene selectivity during epithelia development (PubMed:21081122). {ECO:0000269|PubMed:18288204, ECO:0000269|PubMed:21081122, ECO:0000269|PubMed:24586629}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18288204}. SUBUNIT: Binds DNA as homodimer. Homodimer, also forms heterodimers with GRHL2 or GRHL3. {ECO:0000250|UniProtKB:Q9NZI5}. TISSUE SPECIFICITY: Isoform 1 is highly expressed in brain, pancreas, tonsil, placenta and kidney. Isoform 2 is highly expressed in brain and liver. Expression in the skin is confined to the suprabasal layers of the epidermis and to the hair follicles. {ECO:0000269|PubMed:12175488, ECO:0000269|PubMed:18288204}. +O70293 GRK6_MOUSE G protein-coupled receptor kinase 6 (EC 2.7.11.16) (G protein-coupled receptor kinase GRK6) 576 65,979 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Domain (3); Lipidation (3); Modified residue (5); Nucleotide binding (3); Region (1); Sequence conflict (2) FUNCTION: Specifically phosphorylates the activated forms of G protein-coupled receptors. Such receptor phosphorylation initiates beta-arrestin-mediated receptor desensitization, internalization, and signaling events leading to their desensitization. Seems to be involved in the desensitization of D2-like dopamine receptors in striatum and chemokine receptor CXCR4 which is critical for CXCL12-induced cell chemotaxis (By similarity). Phosphorylates rhodopsin (RHO) (in vitro) and a non G-protein-coupled receptor, LRP6 during Wnt signaling (in vitro) (By similarity). {ECO:0000250, ECO:0000269|PubMed:12032308, ECO:0000269|PubMed:12718862, ECO:0000269|PubMed:14634128}. SUBCELLULAR LOCATION: Membrane; Lipid-anchor. TISSUE SPECIFICITY: Expressed in the brain in striatal neurons. {ECO:0000269|PubMed:12718862}. +Q5NCH9 GRM6_MOUSE Metabotropic glutamate receptor 6 (mGluR6) 871 95,193 Binding site (4); Chain (1); Disulfide bond (8); Glycosylation (4); Region (1); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 580 602 Helical; Name=1. {ECO:0000255}.; TRANSMEM 617 637 Helical; Name=2. {ECO:0000255}.; TRANSMEM 649 667 Helical; Name=3. {ECO:0000255}.; TRANSMEM 692 712 Helical; Name=4. {ECO:0000255}.; TRANSMEM 743 764 Helical; Name=5. {ECO:0000255}.; TRANSMEM 778 800 Helical; Name=6. {ECO:0000255}.; TRANSMEM 814 839 Helical; Name=7. {ECO:0000255}. TOPO_DOM 24 579 Extracellular. {ECO:0000255}.; TOPO_DOM 603 616 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 638 648 Extracellular. {ECO:0000255}.; TOPO_DOM 668 691 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 713 742 Extracellular. {ECO:0000255}.; TOPO_DOM 765 777 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 801 813 Extracellular. {ECO:0000255}.; TOPO_DOM 840 871 Cytoplasmic. {ECO:0000255}. FUNCTION: G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity (By similarity). Signaling stimulates TRPM1 channel activity and Ca(2+) uptake. Required for normal vision. {ECO:0000250, ECO:0000269|PubMed:22131384, ECO:0000269|PubMed:9144650}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell projection, dendrite. Note=Subject to trafficking from the endoplasmic reticulum to the Golgi apparatus and then to the cell membrane (By similarity). Detected at dendritic tips of bipolar cells. {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Detected in the outer plexiform layer in retina (at protein level). {ECO:0000269|PubMed:18001285, ECO:0000269|PubMed:7889569}. +P38647 GRP75_MOUSE Stress-70 protein, mitochondrial (75 kDa glucose-regulated protein) (GRP-75) (Heat shock 70 kDa protein 9) (Mortalin) (Peptide-binding protein 74) (PBP74) (p66 MOT) 679 73,461 Chain (1); Modified residue (28); Natural variant (2); Region (2); Sequence conflict (5); Transit peptide (1) FUNCTION: Chaperone protein which plays an important role in mitochondrial iron-sulfur cluster (ISC) biogenesis (PubMed:26702583). Interacts with and stabilizes ISC cluster assembly proteins FXN, NFU1, NFS1 and ISCU (By similarity). Regulates erythropoiesis via stabilization of ISC assembly (PubMed:21123823). May play a role in the control of cell proliferation and cellular aging (PubMed:8454632). {ECO:0000250|UniProtKB:P38646, ECO:0000269|PubMed:21123823, ECO:0000269|PubMed:26702583, ECO:0000269|PubMed:8454632}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:7865888}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P38646}. SUBUNIT: Interacts strongly with the intermediate form of FXN and weakly with its mature form. Interacts with HSCB. Associates with the mitochondrial contact site and cristae organizing system (MICOS) complex, composed of at least MINOS1/MIC10, CHCHD3/MIC19, CHCHD6/MIC25, APOOL/MIC27, IMMT/MIC60, APOO/MIC23/MIC26 and QIL1/MIC13. This complex was also known under the names MINOS or MitOS complex. The MICOS complex associates with mitochondrial outer membrane proteins SAMM50, MTX1, MTX2 and DNAJC11, mitochondrial inner membrane protein TMEM11 and with HSPA9. Interacts with DNLZ, the interaction is required to prevent self-aggregation. Interacts with TESPA1. Interacts with PDPN. Interacts with NFU1, NFS1 and ISCU. {ECO:0000250|UniProtKB:P38646}. TISSUE SPECIFICITY: Found in all the cell types examined. +Q6P6I6 GRL1A_MOUSE DNA-directed RNA polymerase II subunit GRINL1A (DNA-directed RNA polymerase II subunit M) (Glutamate receptor-like protein 1A) 366 41,237 Alternative sequence (1); Chain (1); Coiled coil (2); Sequence conflict (2) FUNCTION: Isoform 1 appears to be stable component of the Pol II(G) complex form of RNA polymerase II. Pol II synthesizes mRNA precursors and many functional non-coding RNAs and is the central component of the basal RNA polymerase II transcription machinery. Isoform 1 may play a role in Mediator-dependent regulation of transcription activation. Isoform 1 acts in vitro as negative regulator of transcriptional activation; this repression is relieved by the Mediator complex, which restores Pol II(G) activator-dependent transcription to a level equivalent to that of Pol II (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Isoform 1 is a component of the Pol II(G) complex, which contains the RNA polymerase II (Pol II) core complex subunits and Polr2m isoform 1 and appears to be an abundant form of Pol II. +P23819 GRIA2_MOUSE Glutamate receptor 2 (GluR-2) (AMPA-selective glutamate receptor 2) (GluR-B) (GluR-K2) (Glutamate receptor ionotropic, AMPA 2) (GluA2) 883 98,662 Alternative sequence (5); Binding site (3); Chain (1); Disulfide bond (2); Glycosylation (4); Intramembrane (2); Lipidation (2); Modified residue (6); Mutagenesis (3); Natural variant (1); Sequence conflict (7); Signal peptide (1); Topological domain (5); Transmembrane (3) INTRAMEM 592 607 Helical; Pore-forming. {ECO:0000250}.; INTRAMEM 608 610 {ECO:0000250}. TRANSMEM 544 564 Helical. {ECO:0000250}.; TRANSMEM 617 637 Helical. {ECO:0000250}.; TRANSMEM 813 833 Helical; Name=M4. {ECO:0000250}. TOPO_DOM 25 543 Extracellular. {ECO:0000250}.; TOPO_DOM 565 591 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 611 616 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 638 812 Extracellular. {ECO:0000250}.; TOPO_DOM 834 883 Cytoplasmic. {ECO:0000250}. FUNCTION: Receptor for glutamate that functions as ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. In the presence of CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of glutamate (By similarity). Through complex formation with NSG1, GRIP1 and STX12 controls the intracellular fate of AMPAR and the endosomal sorting of the GRIA2 subunit toward recycling and membrane targeting (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P19491}. PTM: Palmitoylated. Depalmitoylated upon glutamate stimulation. ZDHHC3/GODZ specifically palmitoylates Cys-610, which leads to Golgi retention and decreased cell surface expression. In contrast, Cys-836 palmitoylation does not affect cell surface expression but regulates stimulation-dependent endocytosis. {ECO:0000269|PubMed:16129400}.; PTM: N-glycosylated. {ECO:0000269|PubMed:14687553}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein. Note=Interaction with CACNG2, CNIH2 and CNIH3 promotes cell surface expression (By similarity). Displays a somatodendritic localization and is excluded from axons in neurons (PubMed:18341993). {ECO:0000250, ECO:0000269|PubMed:18341993}. SUBUNIT: Homotetramer or heterotetramer of pore-forming glutamate receptor subunits. Tetramers may be formed by the dimerization of dimers. May interact with MPP4. Forms a ternary complex with GRIP1 and CSPG4. Interacts with ATAD1 in an ATP-dependent manner. ATAD1-catalyzed ATP hydrolysis disrupts binding to ATAD1 and to GRIP1 and leads to AMPAR complex disassembly. Interacts with GRIP2. Isoform 1, but not isoform 3, interacts with PICK1/PRKCABP. Interacts with GRIA1 and SYNDIG1. Interacts with LRFN1 (By similarity). Found in a complex with GRIA1, GRIA3, GRIA4, CNIH2, CNIH3, CACNG2, CACNG3, CACNG4, CACNG5, CACNG7 and CACNG8. Interacts with CACNG5 (By similarity). Interacts with SNX27 (via PDZ domain); the interaction is required for recycling to the plasma membrane when endocytosed and prevent degradation in lysosomes. Interacts with OLFM2 (PubMed:25218043). Interacts with AP4B1, AP4E1 and AP4M1; probably indirect it mediates the somatodendritic localization of GRIA2 in neurons (PubMed:18341993). Forms a complex with NSG1, GRIP1 and STX12; controls the intracellular fate of AMPAR and the endosomal sorting of the GRIA2 subunit toward recycling and membrane targeting (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P19491, ECO:0000269|PubMed:10558890, ECO:0000269|PubMed:12458226, ECO:0000269|PubMed:15240807, ECO:0000269|PubMed:18341993, ECO:0000269|PubMed:20152115, ECO:0000269|PubMed:21496646, ECO:0000269|PubMed:23524343, ECO:0000269|PubMed:25218043}. DOMAIN: The M4 transmembrane segment mediates tetramerization and is required for cell surface expression. {ECO:0000250}. TISSUE SPECIFICITY: Detected in brain cortex, hippocampus and cerebellum (at protein level). Detected in hippocampus. {ECO:0000269|PubMed:14687553, ECO:0000269|PubMed:15240807}. +O88396 GRPE2_MOUSE GrpE protein homolog 2, mitochondrial (Mt-GrpE#2) 224 25,030 Chain (1); Modified residue (1); Transit peptide (1) FUNCTION: Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. Seems to control the nucleotide-dependent binding of mitochondrial HSP70 to substrate proteins. Stimulates ATPase activity of mt-HSP70. May also serve to modulate the interconversion of oligomeric (inactive) and monomeric (active) forms of mt-HSP70. SUBCELLULAR LOCATION: Mitochondrion matrix. SUBUNIT: Probable component of the PAM complex at least composed of a mitochondrial HSP70 protein, GRPEL1 or GRPEL2, TIMM44, TIMM16/PAM16 and TIMM14/DNAJC19. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. +Q8C1D8 IWS1_MOUSE Protein IWS1 homolog (IWS1-like protein) 766 85,248 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (2); Modified residue (40); Region (1); Sequence conflict (5) FUNCTION: Transcription factor which plays a key role in defining the composition of the RNA polymerase II (RNAPII) elongation complex and in modulating the production of mature mRNA transcripts. Acts as an assembly factor to recruit various factors to the RNAPII elongation complex and is recruited to the complex via binding to the transcription elongation factor SUPT6H bound to the C-terminal domain (CTD) of the RNAPII subunit RPB1 (POLR2A). The SUPT6H:IWS1:CTD complex recruits mRNA export factors (ALYREF/THOC4, EXOSC10) as well as histone modifying enzymes (such as SETD2) to ensure proper mRNA splicing, efficient mRNA export and elongation-coupled H3K36 methylation, a signature chromatin mark of active transcription (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00649}. SUBUNIT: Interacts with SUPT6H; binds preferentially to the POLR2A-bound SUPT6H. Interacts with ALYREF/THOC4, SETD2 and PRMT5 (By similarity). Interacts with HDGFRP2 (By similarity). {ECO:0000250|UniProtKB:Q96ST2}. TISSUE SPECIFICITY: Ubiquitous. Expressed at highest level in kidney, then testicle, large intestine, small intestine, spleen and prostate, whereas the lowest level is detected in heart. {ECO:0000269|PubMed:17184735}. +P56916 GSC2_MOUSE Homeobox protein goosecoid-2 (GSC-2) (Homeobox protein goosecoid-like) (GSC-L) 198 21,765 Chain (1); Compositional bias (1); DNA binding (1) FUNCTION: May have a role in development. May regulate its own transcription. May bind the bicoid consensus sequence TAATCC. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. TISSUE SPECIFICITY: Expressed in adult testis. {ECO:0000269|PubMed:9441739}. +Q5Y4Y6 GSDA3_MOUSE Gasdermin-A3 (Gasdermin-3) 464 52,020 Beta strand (12); Chain (1); Coiled coil (1); Erroneous gene model prediction (1); Helix (18); Mutagenesis (5); Natural variant (5); Region (1); Turn (3) FUNCTION: May play a role in the transition from catagen to telogen at the end of hair follicle morphogenesis (PubMed:15475261). May promote pyroptosis (PubMed:26375003, PubMed:27281216). Upon cleavage in vitro of genetically engineered Gsdma3, the released N-terminal moiety binds to membrane inner leaflet lipids, including bisphosphorylated phosphatidylinositols, such as phosphatidylinositol (4,5)-bisphosphate, as well as phosphatidylinositol (3,4,5)-bisphosphate, and more weakly to monophosphorylated phosphatidylinositols. Homooligomerizes within the membrane and forms pores of 10 -15 nanometers (nm) of inner diameter, triggering pyroptosis. Also binds to bacterial and mitochondrial lipids, including cardiolipin, and exhibits bactericidal activity (PubMed:27281216). The physiological relevance of these observations is unknown (Probable). {ECO:0000269|PubMed:15475261, ECO:0000269|PubMed:26375003, ECO:0000269|PubMed:27281216, ECO:0000305}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:27281216}. Cell membrane {ECO:0000269|PubMed:27281216}. SUBUNIT: The N-terminal moiety forms homooligomer; disulfide-linked. May form an 16-mer complex. Oligomerization occurs in the presence of membranes. {ECO:0000269|PubMed:27281216}. DOMAIN: Intramolecular interactions between N- and C-terminal domains may be important for autoinhibition in the absence of activation signal. The intrinsic pyroptosis-inducing activity is carried by the N-terminal domain. {ECO:0000269|PubMed:26375003}. TISSUE SPECIFICITY: Highest levels in skin with weak expression in placenta and testis. Not detected in the gastrointestinal tract. In skin, expressed in postnatal hair follicles and epidermis as well as sebaceous gland basal cells. {ECO:0000269|PubMed:15475261}. DISEASE: Note=Defects in Gsdma3 are the cause of a number of alopecia phenotypes, bareskin (Bsk), defolliculated (Dfl), finnegan (Fgn) reduced coat 2 (Rco2), Rex-denuded (Re-den) and recombination induced mutation 3 (Rim3). These are dominant conditions characterized by loss of hair. {ECO:0000269|PubMed:15475261, ECO:0000269|PubMed:15737203, ECO:0000269|PubMed:17572385}. +Q9Z2D3 GSDME_MOUSE Gasdermin-E (Non-syndromic hearing impairment protein 5 homolog) [Cleaved into: Gasdermin-E, N-terminal (GSDME-NT); Gasdermin-E, C-terminal (GSDME-CT)] 512 56,631 Chain (3); Region (1); Site (1) FUNCTION: Plays a role in the TP53-regulated cellular response to DNA damage probably by cooperating with TP53. {ECO:0000250|UniProtKB:O60443}.; FUNCTION: Gasdermin-E, N-terminal: Switches CASP3-mediated apoptosis induced by TNF or danger signals, such as chemotherapy drugs, to pyroptosis. Produced by the cleavage of GSDME by CASP3, perforates cell membrane and thereby induces pyroptosis. After cleavage, moves to the plasma membrane where it strongly binds to inner leaflet lipids, bisphosphorylated phosphatidylinositols, such as phosphatidylinositol (4,5)-bisphosphate (By similarity). Mediates secondary necrosis downstream of the mitochondrial apoptotic pathway and CASP3 activation as well as in response to viral agents (PubMed:28045099). Exhibits bactericidal activity (By similarity). {ECO:0000250|UniProtKB:O60443, ECO:0000269|PubMed:28045099}. PTM: Cleavage at Asp-270 by CASP3 (mature and uncleaved precursor forms) relieves autoinhibition and is sufficient to initiate pyroptosis. {ECO:0000250|UniProtKB:O60443}. SUBCELLULAR LOCATION: Gasdermin-E, N-terminal: Cell membrane {ECO:0000250|UniProtKB:O60443}.; SUBCELLULAR LOCATION: Gasdermin-E: Cytoplasm, cytosol {ECO:0000250|UniProtKB:O60443, ECO:0000250|UniProtKB:P57764}. SUBUNIT: The N-terminal moiety forms homooligomer; disulfide-linked. May form an 16-mer complex. Oligomerization occurs in the presence of membranes. {ECO:0000250|UniProtKB:P57764}. DOMAIN: Intramolecular interactions between N- and C-terminal domains may be important for autoinhibition in the absence of activation signal. The intrinsic pyroptosis-inducing activity is carried by the N-terminal domain, that is released upon cleavage by CASP3. {ECO:0000250|UniProtKB:O60443, ECO:0000250|UniProtKB:Q5Y4Y6}. TISSUE SPECIFICITY: Expressed in spleen, kidney, large and small intestine, testicle, stomach and by CD4(+)CD(8+) T cells in thymus (PubMed:28459430). Expressed by macrophages (PubMed:28045099). {ECO:0000269|PubMed:28045099, ECO:0000269|PubMed:28459430}. +Q9DCX8 IYD1_MOUSE Iodotyrosine deiodinase 1 (IYD-1) (EC 1.21.1.1) (Iodotyrosine dehalogenase 1) 285 32,814 Beta strand (7); Binding site (5); Chain (1); Helix (11); Mutagenesis (1); Nucleotide binding (3); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 211 231 Helical. {ECO:0000255}. TOPO_DOM 24 210 Extracellular. {ECO:0000255}.; TOPO_DOM 232 285 Cytoplasmic. {ECO:0000255}. FUNCTION: Catalyzes the oxidative NADPH-dependent deiodination of monoiodotyrosine (L-MIT) or diiodotyrosine (L-DIT) (PubMed:22238141). Acts during the hydrolysis of thyroglobulin to liberate iodide, which can then reenter the hormone-producing pathways. Acts more efficiently on monoiodotyrosine than on diiodotyrosine (By similarity). {ECO:0000250|UniProtKB:Q6PHW0, ECO:0000269|PubMed:22238141}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6PHW0}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q6PHW0}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q6PHW0}. SUBUNIT: Homodimer. {ECO:0000269|PubMed:19436071, ECO:0000269|PubMed:22238141}. +Q99NB5 GSDMC_MOUSE Gasdermin-C (Gasdermin-C1) (Melanoma-derived leucine zipper-containing extranuclear factor) (mMLZE) 468 52,743 Chain (1); Region (1) FUNCTION: The N-terminal moiety promotes pyroptosis and exhibits bactericidal activity. The physiological relevance of these observations is unknown. {ECO:0000250|UniProtKB:Q9BYG8}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9BYG8}. Cell membrane {ECO:0000250|UniProtKB:P57764}. SUBUNIT: The N-terminal moiety forms homooligomer; disulfide-linked. May form an 16-mer complex. Oligomerization occurs in the presence of membranes. {ECO:0000250|UniProtKB:P57764}. DOMAIN: Intramolecular interactions between N- and C-terminal domains may be important for autoinhibition in the absence of activation signal. The intrinsic pyroptosis-inducing activity is carried by the N-terminal domain. {ECO:0000250|UniProtKB:Q5Y4Y6}. +Q3U3C9 GSE1_MOUSE Genetic suppressor element 1 1213 136,228 Alternative sequence (3); Chain (1); Coiled coil (2); Compositional bias (2); Erroneous initiation (1); Frameshift (1); Modified residue (14); Sequence conflict (5) SUBUNIT: May be a component of a BHC histone deacetylase complex that contains HDAC1, HDAC2, HMG20B/BRAF35, KDM1A, RCOR1/CoREST, PHF21A/BHC80, ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I. +Q9DA16 IZUM2_MOUSE Izumo sperm-egg fusion protein 2 220 24,868 Alternative sequence (3); Chain (1); Erroneous initiation (1); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 186 206 Helical. {ECO:0000255}. TOPO_DOM 21 185 Extracellular. {ECO:0000255}.; TOPO_DOM 207 220 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +P97494 GSH1_MOUSE Glutamate--cysteine ligase catalytic subunit (EC 6.3.2.2) (GCS heavy chain) (Gamma-ECS) (Gamma-glutamylcysteine synthetase) 637 72,571 Chain (1); Modified residue (3); Sequence conflict (4) Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 1/2. SUBUNIT: Heterodimer of a catalytic heavy chain and a regulatory light chain. +Q9DCM2 GSTK1_MOUSE Glutathione S-transferase kappa 1 (EC 2.5.1.18) (GST 13-13) (GST class-kappa) (GSTK1-1) (mGSTK1) (Glutathione S-transferase subunit 13) 226 25,704 Binding site (2); Chain (1); Modified residue (20); Region (2) PTM: Acetylation of Lys-93 is observed in liver mitochondria from fasted mice but not from fed mice. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:12720545}. SUBUNIT: Homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Predominantly expressed in heart, kidney, liver and skeletal muscle. {ECO:0000269|PubMed:12720545}. +P31316 GSX2_MOUSE GS homeobox 2 (Genetic-screened homeobox 2) (Homeobox protein GSH-2) 305 32,167 Chain (1); Compositional bias (3); DNA binding (1) FUNCTION: During telencephalic development, causes ventralization of pallial progenitors and, depending on the developmental stage, specifies different neuronal fates. At early stages, necessary and sufficient to correctly specify the ventral lateral ganglionic eminence (LGE) and its major derivatives, the striatal projection neurons. At later stages, may specify LGE progenitors toward dorsal LGE fates, including olfactory bulb interneurons (PubMed:19709628). Transcription factor that binds 5'-CNAATTAG-3' DNA sequence (PubMed:7619729). {ECO:0000269|PubMed:19709628, ECO:0000269|PubMed:7619729}. SUBCELLULAR LOCATION: Nucleus. +P15626 GSTM2_MOUSE Glutathione S-transferase Mu 2 (EC 2.5.1.18) (GST 5-5) (GST class-mu 2) (Glutathione S-transferase pmGT2) 218 25,717 Binding site (2); Chain (1); Domain (2); Initiator methionine (1); Modified residue (3); Region (4) FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Homodimer. +Q99NI3 GT2D2_MOUSE General transcription factor II-I repeat domain-containing protein 2 (GTF2I repeat domain-containing protein 2) (Transcription factor GTF2IRD2) 936 104,578 Chain (1); Repeat (2) SUBCELLULAR LOCATION: Nucleus. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15100712}. +O35660 GSTM6_MOUSE Glutathione S-transferase Mu 6 (EC 2.5.1.18) (GST class-mu 6) (Glutathione-S-transferase class M5) 218 25,621 Binding site (1); Chain (1); Domain (2); Region (4); Sequence conflict (4) FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in liver, stomach and small intestine. Not expressed in spleen, kidney, colon, heart, muscle, brain or lung. {ECO:0000269|PubMed:9480867}. +O08582 GTPB1_MOUSE GTP-binding protein 1 (G-protein 1) (GP-1) (GP1) 668 72,301 Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (2); Frameshift (3); Modified residue (9); Nucleotide binding (3); Region (5); Sequence conflict (1) FUNCTION: Promotes degradation of target mRNA species. Plays a role in the regulation of circadian mRNA stability. Binds GTP and has GTPase activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10938096}. SUBUNIT: Interacts with EXOSC2/RRP4, EXOSC3/RRP40, EXOSC5/RRP46, HNRNPD, HNRNPR and SYNCRIP. Identified in a complex with AANAT mRNA, but does not bind mRNA by itself (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Detected in some neurons in the brain cortex. Detected in small arteries, dendritic cells and macrophages in the thymus. Detected in lung bronchi, in bronchial epithelial cells and in bronchial smooth muscle cells. Detected in smooth muscle cells in a broad range of organs (at protein level). Expressed in brain, thymus, lung, and kidney. {ECO:0000269|PubMed:10938096, ECO:0000269|PubMed:9070279}. +Q9WUR9 KAD4_MOUSE Adenylate kinase 4, mitochondrial (AK 4) (EC 2.7.4.10) (EC 2.7.4.6) (Adenylate kinase 3-like) (Adenylate kinase isoenzyme 4) (GTP:AMP phosphotransferase AK4) 223 25,062 Binding site (6); Chain (1); Modified residue (6); Nucleotide binding (4); Region (2); Sequence conflict (3) FUNCTION: Involved in maintaining the homeostasis of cellular nucleotides by catalyzing the interconversion of nucleoside phosphates. Efficiently phosphorylates AMP and dAMP using ATP as phosphate donor, but phosphorylates only AMP when using GTP as phosphate donor. Also displays broad nucleoside diphosphate kinase activity. {ECO:0000255|HAMAP-Rule:MF_03170}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-Rule:MF_03170}. SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03170}. DOMAIN: Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon GTP/ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent GTP/ATP hydrolysis. {ECO:0000255|HAMAP-Rule:MF_03170}. TISSUE SPECIFICITY: Expressed in the pyramidal cells in the hippocampus. +Q9R111 GUAD_MOUSE Guanine deaminase (Guanase) (Guanine aminase) (EC 3.5.4.3) (Guanine aminohydrolase) (GAH) 454 51,013 Binding site (1); Chain (1); Metal binding (4); Modified residue (1); Region (3) Purine metabolism; guanine degradation; xanthine from guanine: step 1/1. FUNCTION: Catalyzes the hydrolytic deamination of guanine, producing xanthine and ammonia. SUBUNIT: Homodimer. +Q8R5M0 GIPC3_MOUSE PDZ domain-containing protein GIPC3 (Regulator of G-protein signaling 19-interacting protein 3) 297 32,108 Chain (1); Domain (1); Natural variant (1) FUNCTION: Required for postnatal maturation of the hair bundle and long-term survival of hair cells and spiral ganglion. {ECO:0000269|PubMed:21326233}. TISSUE SPECIFICITY: Expressed in adult lung, brain and testis. In the inner ear, it is expressed in the inner and outer hair cells of the organ of Corti. Also expressed in cochlear spiral ganglion neurons. {ECO:0000269|PubMed:11836631, ECO:0000269|PubMed:21326233}. DISEASE: Note=Defects in GIPC3 underlie the age-related hearing loss 5 (ahl5) and juvenile audiogenic monogenic seizure (jams1) phenotypes. Ahl5 mice show irregular structure of the stereocilia bundle of outer and inner hair cells, late-onset degeneration of the organ of Corti. The spiral ganglion exhibits a severe loss of neurons. {ECO:0000269|PubMed:21326233}. +Q9D7M1 GID8_MOUSE Glucose-induced degradation protein 8 homolog (Two hybrid-associated protein 1 with RanBPM) (Twa1) 228 26,779 Chain (1); Domain (2); Region (1) FUNCTION: Core component of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1. Acts as a positive regulator of Wnt signaling pathway by promoting beta-catenin (CTNNB1) nuclear accumulation. {ECO:0000250|UniProtKB:Q9NWU2}. PTM: Polyubiquitinated through 'Lys-48'-polyubiquitin chains, leading to proteasomal degradation in the absence of Wnt stimulation. {ECO:0000250|UniProtKB:Q9NWU2}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NWU2}. Nucleus {ECO:0000250|UniProtKB:Q9NWU2}. Note=Localizes in the cytoplasm in the absence of Wnt stimulation and in the nucleus in the presence of Wnt stimulation. {ECO:0000250|UniProtKB:Q9NWU2}. SUBUNIT: Homodimer; may also form higher oligomers (PubMed:27920276). Identified in the CTLH complex that contains GID4, RANBP9 and/or RANBP10, MKLN1, MAEA, RMND5A (or alternatively its paralog RMND5B), GID8, ARMC8, WDR26 and YPEL5. Within this complex, MAEA, RMND5A (or alternatively its paralog RMND5B), GID8, WDR26, and RANBP9 and/or RANBP10 form the catalytic core, while GID4, MKLN1, ARMC8 and YPEL5 have ancillary roles. Interacts with RANBP9. Part of a complex consisting of RANBP9, MKLN1 and GID8. Interacts with CTNNB1, AXIN1 and GSK3B (By similarity). {ECO:0000250|UniProtKB:Q9NWU2, ECO:0000269|PubMed:27920276}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12559565}. +Q9CQS6 GKN2_MOUSE Gastrokine-2 (Blottin) 184 20,469 Chain (1); Disulfide bond (1); Domain (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16888721}. Golgi apparatus {ECO:0000269|PubMed:16888721}. Note=Secreted into the mucus layer, also present in Golgi apparatus and mucus granules. SUBUNIT: Heterodimer with TFF1; disulfide linked (By similarity). Interacts with TFF2. {ECO:0000250, ECO:0000269|PubMed:16888721}. TISSUE SPECIFICITY: Stomach foveolar epithelium and duodenal Brunner's glands. {ECO:0000269|PubMed:16888721}. +A2RSQ1 GLBL3_MOUSE Beta-galactosidase-1-like protein 3 (EC 3.2.1.-) 649 73,922 Active site (2); Alternative sequence (1); Chain (1) +Q64018 GLRA1_MOUSE Glycine receptor subunit alpha-1 (Glycine receptor 48 kDa subunit) (Glycine receptor strychnine-binding subunit) 457 52,657 Alternative sequence (1); Chain (1); Disulfide bond (2); Glycosylation (1); Metal binding (3); Mutagenesis (2); Natural variant (1); Region (1); Sequence conflict (4); Signal peptide (1); Site (1); Topological domain (5); Transmembrane (4) TRANSMEM 251 272 Helical; Name=1. {ECO:0000250|UniProtKB:O93430}.; TRANSMEM 278 298 Helical; Name=2. {ECO:0000250|UniProtKB:O93430}.; TRANSMEM 310 330 Helical; Name=3. {ECO:0000250|UniProtKB:O93430}.; TRANSMEM 426 446 Helical; Name=4. {ECO:0000250|UniProtKB:O93430}. TOPO_DOM 29 250 Extracellular. {ECO:0000250|UniProtKB:O93430}.; TOPO_DOM 273 277 Cytoplasmic. {ECO:0000250|UniProtKB:O93430}.; TOPO_DOM 299 309 Extracellular. {ECO:0000250|UniProtKB:O93430}.; TOPO_DOM 331 425 Cytoplasmic. {ECO:0000250|UniProtKB:O93430}.; TOPO_DOM 447 457 Extracellular. {ECO:0000250|UniProtKB:O93430}. FUNCTION: Glycine receptors are ligand-gated chloride channels. Channel opening is triggered by extracellular glycine (PubMed:16672662, PubMed:17114051, PubMed:24801766). Channel opening is also triggered by taurine and beta-alanine (By similarity). Channel characteristics depend on the subunit composition; heteropentameric channels are activated by lower glycine levels and display faster desensitization (By similarity). Plays an important role in the down-regulation of neuronal excitability (PubMed:9145798). Contributes to the generation of inhibitory postsynaptic currents (PubMed:16672662, PubMed:17114051, PubMed:24801766). Channel activity is potentiated by ethanol. Potentiation of channel activity by intoxicating levels of ethanol contribute to the sedative effects of ethanol (PubMed:24801766). {ECO:0000250|UniProtKB:P23415, ECO:0000269|PubMed:16672662, ECO:0000269|PubMed:17114051, ECO:0000269|PubMed:24801766, ECO:0000269|PubMed:9145798}. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane {ECO:0000305|PubMed:12975813, ECO:0000305|PubMed:17114051, ECO:0000305|PubMed:24801766}; Multi-pass membrane protein {ECO:0000305}. Cell junction, synapse {ECO:0000269|PubMed:12975813, ECO:0000269|PubMed:17114051, ECO:0000269|PubMed:24801766}. Perikaryon {ECO:0000269|PubMed:24801766}. Cell projection, dendrite {ECO:0000269|PubMed:24801766}. Cell membrane {ECO:0000269|PubMed:16672662, ECO:0000305|PubMed:9145798}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P23415, ECO:0000305}. SUBUNIT: Homopentamer (in vitro). Interacts with GLRB to form heteropentameric channels; this is probably the predominant form in vivo. Heteropentamer composed of two GLRA1 and three GLRB. Heteropentamer composed of three GLRA1 and two GLRB. Both homopentamers and heteropentamers form functional ion channels, but their characteristics are subtly different. {ECO:0000250|UniProtKB:P23415}. DOMAIN: The channel pore is formed by pentameric assembly of the second transmembrane domain from all five subunits. Channel opening is effected by an outward rotation of the transmembrane domains that increases the diameter of the pore. {ECO:0000250|UniProtKB:O93430}. TISSUE SPECIFICITY: Detected in spinal cord neurons (PubMed:9145798, PubMed:17114051, PubMed:24801766). Detected in brain stem neurons (PubMed:16672662, PubMed:24801766). Detected at lower levels in hippocampus and cerebellum (PubMed:24801766). Detected in the inner plexiform layer of the retina (at protein level) (PubMed:12975813). {ECO:0000269|PubMed:12975813, ECO:0000269|PubMed:16672662, ECO:0000269|PubMed:17114051, ECO:0000269|PubMed:24801766, ECO:0000269|PubMed:9145798}. DISEASE: Note=Defects in Glra1 are the cause of the spasmodic (spd) phenotype, a mouse mutant which resembles the human neurological disease, hyperekplexia (or startle disease (STHE)) (PubMed:7920629). Defects in Glra1 are the cause of the lethal oscillator (spd-ot) phenotype. Mutant mice display a fine motor tremor and muscle spasms that begin at 2 weeks of age and progressively worsen, resulting in death by 3 weeks of age (PubMed:7874121). Heterozygous mice show an increased acoustic startle response (PubMed:9145798). Neurons from homozygous oscillator mice have dramatically reduced amplitude and frequency of glycinergic inhibitory postsynaptic currents (PubMed:16672662). The oscillator phenotype is due to the complete absence of Glra1 protein (PubMed:9145798). {ECO:0000269|PubMed:16672662, ECO:0000269|PubMed:7874121, ECO:0000269|PubMed:7920629, ECO:0000269|PubMed:9145798}. +Q923X4 GLRX2_MOUSE Glutaredoxin-2, mitochondrial 156 17,307 Alternative sequence (1); Binding site (3); Chain (1); Disulfide bond (1); Domain (1); Frameshift (1); Metal binding (2); Modified residue (1); Transit peptide (1) FUNCTION: Glutathione-dependent oxidoreductase that facilitates the maintenance of mitochondrial redox homeostasis upon induction of apoptosis by oxidative stress. Involved in response to hydrogen peroxide and regulation of apoptosis caused by oxidative stress. Acts as a very efficient catalyst of monothiol reactions because of its high affinity for protein glutathione-mixed disulfides. Can receive electrons not only from glutathione (GSH), but also from thioredoxin reductase supporting both monothiol and dithiol reactions. Efficiently catalyzes both glutathionylation and deglutathionylation of mitochondrial complex I, which in turn regulates the superoxide production by the complex. Overexpression decreases the susceptibility to apoptosis and prevents loss of cardiolipin and cytochrome c release. {ECO:0000269|PubMed:11397793, ECO:0000269|PubMed:15347644}. SUBCELLULAR LOCATION: Isoform 1: Mitochondrion.; SUBCELLULAR LOCATION: Isoform 2: Nucleus. SUBUNIT: Monomer; active form. Homodimer; inactive form. The homodimer is probably linked by 1 2Fe-2S cluster (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. Highly expressed in testis, and at much lower level in kidney and brain. {ECO:0000269|PubMed:12954614}. +Q80Y14 GLRX5_MOUSE Glutaredoxin-related protein 5, mitochondrial (Monothiol glutaredoxin-5) 152 16,292 Binding site (2); Chain (1); Compositional bias (2); Domain (1); Erroneous initiation (1); Metal binding (1); Modified residue (2); Region (2); Transit peptide (1) FUNCTION: Monothiol glutaredoxin involved in the biogenesis of iron-sulfur clusters (By similarity). Involved in protein lipoylation, acting in the pathway that provides an iron-sulfur cluster to lipoate synthase (By similarity). Required for normal iron homeostasis (By similarity). Required for normal regulation of hemoglobin synthesis by the iron-sulfur protein ACO1 (By similarity). May protect cells against apoptosis due to reactive oxygen species and oxidative stress (PubMed:19442627). {ECO:0000250|UniProtKB:Q86SX6, ECO:0000269|PubMed:19442627}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:Q86SX6}. SUBUNIT: Homodimer. Interacts with ISCU. Interacts with BOLA1. {ECO:0000250|UniProtKB:Q86SX6}. TISSUE SPECIFICITY: Detected in bone, liver, muscle and kidney. {ECO:0000269|PubMed:19442627}. +Q91XP5 GLRA3_MOUSE Glycine receptor subunit alpha-3 464 53,709 Chain (1); Disulfide bond (2); Glycosylation (1); Metal binding (3); Modified residue (2); Region (1); Sequence conflict (3); Signal peptide (1); Site (1); Topological domain (5); Transmembrane (4) TRANSMEM 256 277 Helical; Name=1. {ECO:0000250|UniProtKB:O75311}.; TRANSMEM 283 303 Helical; Name=2. {ECO:0000250|UniProtKB:O75311}.; TRANSMEM 315 335 Helical; Name=3. {ECO:0000250|UniProtKB:O75311}.; TRANSMEM 431 451 Helical; Name=4. {ECO:0000250|UniProtKB:O75311}. TOPO_DOM 34 255 Extracellular. {ECO:0000250|UniProtKB:O75311}.; TOPO_DOM 278 282 Cytoplasmic. {ECO:0000250|UniProtKB:O75311}.; TOPO_DOM 304 314 Extracellular. {ECO:0000250|UniProtKB:O75311}.; TOPO_DOM 336 430 Cytoplasmic. {ECO:0000250|UniProtKB:O75311}.; TOPO_DOM 452 464 Extracellular. {ECO:0000250|UniProtKB:O75311}. FUNCTION: Glycine receptors are ligand-gated chloride channels. Channel opening is triggered by extracellular glycine (PubMed:15131310, PubMed:20978350). Channel characteristics depend on the subunit composition; heteropentameric channels display faster channel closure (By similarity). Plays an important role in the down-regulation of neuronal excitability. Contributes to the generation of inhibitory postsynaptic currents (PubMed:15131310). Contributes to increased pain perception in response to increased prostaglandin E2 levels (PubMed:15131310). Plays a role in the regulation of breathing rhythm, especially of the duration of the postinspiratory phase (PubMed:20978350). Plays a role in cellular responses to ethanol (By similarity). {ECO:0000250|UniProtKB:P24524, ECO:0000269|PubMed:15131310, ECO:0000269|PubMed:20978350}. PTM: Phosphorylated by PKA; this causes down-regulation of channel activity. Dephosphorylated in response to activation of HTR1A signaling; this increases channel activity (PubMed:20978350). {ECO:0000250|UniProtKB:P24524, ECO:0000269|PubMed:20978350}. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane {ECO:0000305|PubMed:12975813, ECO:0000305|PubMed:15131310, ECO:0000305|PubMed:19723286}; Multi-pass membrane protein {ECO:0000305}. Cell junction, synapse {ECO:0000269|PubMed:12975813, ECO:0000269|PubMed:15131310, ECO:0000269|PubMed:19723286}. Perikaryon {ECO:0000269|PubMed:19723286}. Cell projection, dendrite {ECO:0000250|UniProtKB:P24524}. Cell membrane {ECO:0000269|PubMed:20978350}; Multi-pass membrane protein {ECO:0000305}. Note=Partially colocalizes with GPHN that is known to mediate receptor clustering at postsynaptic membranes. {ECO:0000269|PubMed:15131310}. SUBUNIT: Homopentamer (in vitro) (By similarity). Heteropentamer composed of GLRA3 and GLRB. Both homopentamers and heteropentamers form functional ion channels, but their characteristics are subtly different (By similarity). {ECO:0000250|UniProtKB:O75311, ECO:0000250|UniProtKB:P24524}. DOMAIN: The N-terminal domain carries structural determinants essential for agonist and antagonist binding. The channel pore is formed by pentameric assembly of the second transmembrane domain from all five subunits. The cytoplasmic loop is an important determinant of channel inactivation kinetics. {ECO:0000250|UniProtKB:O75311}. TISSUE SPECIFICITY: Detected in brainstem, also in neurons that control rhythmic breathing (PubMed:20978350). Detected in superficial laminae of the dorsal horn of the thoracic spinal cord (PubMed:15131310). Detected in dentate gyrus in hippocampus, especially in stratum granulare (PubMed:19723286). Detected in the inner plexiform layer in the retina (at protein level) (PubMed:12975813). Detected in midbrain, thalamus, brain cortex, hippocampus, and at lower levels in cerebellum (PubMed:19723286). {ECO:0000269|PubMed:12975813, ECO:0000269|PubMed:15131310, ECO:0000269|PubMed:19723286, ECO:0000269|PubMed:20978350}. +Q8R460 IL36G_MOUSE Interleukin-36 gamma (Interleukin-1 family member 9) (IL-1F9) 164 18,733 Chain (1); Propeptide (1) FUNCTION: Functions as an agonist of NF-kappa B activation through the orphan IL-1-receptor-related protein 2/IL1RL2. Part of the IL-36 signaling system that is thought to be present in epithelial barriers and to take part in local inflammatory response; similar to the IL-1 system with which it shares the coreceptor IL1RAP (By similarity). Seems to be involved in skin inflammatory response by acting on keratinocytes, dendritic cells and indirectly on T-cells to drive tissue infiltration, cell maturation and cell proliferation. May play a role in proinflammatory responses during particular neutrophilic airway inflammation. May be involved in the innate immune response to fungal pathogens. Induces the production of proinflammatory cytokines in bone marrow-derived dendritic cells (BMDCs), including IL-12, Il-1 beta, IL-6, TNF-alpha and IL-23. Involved in dendritic cell maturation by stimulating the surface expression of CD80, CD86 and MHC class II. Induces the production of IFN-gamma, IL-4 and IL-17 by cultured CD4(+) T-cells and splenocytes. {ECO:0000250|UniProtKB:Q9NZH8, ECO:0000269|PubMed:21860022, ECO:0000269|PubMed:21965679}. PTM: N-terminal truncation leads to a dramatic enhancement of its activity (>1000-fold). {ECO:0000269|PubMed:21965679}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9NZH8}. +Q921L8 GLT11_MOUSE Polypeptide N-acetylgalactosaminyltransferase 11 (EC 2.4.1.41) (Polypeptide GalNAc transferase 11) (GalNAc-T11) (pp-GaNTase 11) (Protein-UDP acetylgalactosaminyltransferase 11) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11) 608 69,201 Binding site (6); Chain (1); Disulfide bond (5); Domain (1); Erroneous termination (1); Glycosylation (2); Metal binding (3); Modified residue (1); Region (2); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 7 29 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 30 608 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Polypeptide N-acetylgalactosaminyltransferase that catalyzes the initiation of protein O-linked glycosylation and is involved in left/right asymmetry by mediating O-glycosylation of NOTCH1. O-glycosylation of NOTCH1 promotes activation of NOTCH1, modulating the balance between motile and immotile (sensory) cilia at the left-right organiser (LRO). Polypeptide N-acetylgalactosaminyltransferases catalyze the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Displays the same enzyme activity toward MUC1, MUC4, and EA2 than GALNT1. Not involved in glycosylation of erythropoietin (EPO) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. SUBUNIT: Interacts with NOTCH1. {ECO:0000250}. DOMAIN: There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding. {ECO:0000250}.; DOMAIN: The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity. {ECO:0000250}. TISSUE SPECIFICITY: Mainly expressed in kidney. Weakly expressed in other tissues. {ECO:0000269|PubMed:11925450}. +Q571F8 GLSL_MOUSE Glutaminase liver isoform, mitochondrial (GLS) (EC 3.5.1.2) (L-glutaminase) (L-glutamine amidohydrolase) 602 66,366 Binding site (7); Chain (1); Erroneous initiation (1); Modified residue (4); Repeat (2); Sequence conflict (2); Transit peptide (1) FUNCTION: Plays an important role in the regulation of glutamine catabolism. Promotes mitochondrial respiration and increases ATP generation in cells by catalyzing the synthesis of glutamate and alpha-ketoglutarate. Increases cellular anti-oxidant function via NADH and glutathione production (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. SUBUNIT: Interacts with the PDZ domain of the syntrophin SNTA1. Interacts with the PDZ domain of TAX1BP3 (By similarity). {ECO:0000250}. +Q8CF93 GLT13_MOUSE Polypeptide N-acetylgalactosaminyltransferase 13 (EC 2.4.1.41) (Polypeptide GalNAc transferase 13) (GalNAc-T13) (pp-GaNTase 13) (Protein-UDP acetylgalactosaminyltransferase 13) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 13) 556 63,983 Alternative sequence (1); Binding site (5); Chain (1); Disulfide bond (5); Domain (1); Glycosylation (3); Metal binding (3); Region (2); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 5 27 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 4 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 28 556 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has a much stronger activity than GALNT1 to transfer GalNAc to mucin peptides, such as Muc5Ac and Muc7. Able to glycosylate SDC3. Probably responsible for the synthesis of Tn antigen in neuronal cells. {ECO:0000269|PubMed:12407114, ECO:0000269|PubMed:8618846}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. DOMAIN: There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding. {ECO:0000250}.; DOMAIN: The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity. {ECO:0000250}. TISSUE SPECIFICITY: Specifically expressed in neuronal cells. Not expressed in glial cells such as astrocytes. Expressed at low level. {ECO:0000269|PubMed:12407114, ECO:0000269|PubMed:12651884}. +Q8BH86 GLUCM_MOUSE D-glutamate cyclase, mitochondrial (EC 4.2.1.48) 617 66,366 Alternative sequence (2); Chain (1); Modified residue (1); Sequence conflict (4); Transit peptide (1) FUNCTION: D-glutamate cyclase that converts D-glutamate to 5-oxo-D-proline. {ECO:0000269|PubMed:28266638}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:28266638}. +Q9JJ61 GLT16_MOUSE Polypeptide N-acetylgalactosaminyltransferase 16 (EC 2.4.1.41) (Polypeptide GalNAc transferase 16) (GalNAc-T16) (Polypeptide GalNAc transferase-like protein 1) (GalNAc-T-like protein 1) (pp-GaNTase-like protein 1) (Polypeptide N-acetylgalactosaminyltransferase-like protein 1) (Protein-UDP acetylgalactosaminyltransferase-like protein 1) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 1) 558 62,875 Binding site (7); Chain (1); Disulfide bond (5); Domain (1); Metal binding (3); Region (2); Sequence conflict (4); Topological domain (2); Transmembrane (1) TRANSMEM 7 26 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 27 558 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. DOMAIN: There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding. {ECO:0000250}.; DOMAIN: The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity. {ECO:0000250}. TISSUE SPECIFICITY: In the CNS, it is predominantly expressed in several distinct hypothalamic, thalamic and amygdaloid nuclei. The most abundant level of expression is in the paraventricular, ventromedial and arcuate nuclei of the hypothalamus, the anterodorsal and parafascicular nuclei of the thalamus and the central, basomedial and medial nuclei of the amygdala. Also expressed in cerebral cortex, lateral septum, habenula and hippocampus. {ECO:0000269|PubMed:15018805}. +Q3UFS4 GPT11_MOUSE G patch domain-containing protein 11 (Coiled-coil domain-containing protein 75) 262 30,608 Chain (1); Coiled coil (1); Domain (1); Erroneous initiation (4); Modified residue (1); Sequence conflict (2) SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q8N954}. +A2A6A1 GPTC8_MOUSE G patch domain-containing protein 8 1505 164,987 Chain (1); Coiled coil (1); Compositional bias (7); Cross-link (3); Domain (1); Modified residue (14); Sequence conflict (1); Zinc finger (1) +P08882 GRAC_MOUSE Granzyme C (EC 3.4.21.-) (B10) (Cytotoxic cell protease 2) (CCP2) 248 27,311 Active site (3); Beta strand (14); Chain (1); Disulfide bond (3); Domain (1); Helix (3); Propeptide (1); Sequence conflict (2); Signal peptide (1); Turn (4) FUNCTION: This enzyme is probably necessary for target cell lysis in cell-mediated immune responses. SUBCELLULAR LOCATION: Cytoplasmic granule. Note=Cytoplasmic granules of cytolytic T-lymphocytes. +Q5SNZ0 GRDN_MOUSE Girdin (Akt phosphorylation enhancer) (APE) (Coiled-coil domain-containing protein 88A) (G alpha-interacting vesicle-associated protein) (GIV) (Girders of actin filament) (Hook-related protein 1) (HkRP1) 1873 215,918 Alternative sequence (2); Chain (1); Coiled coil (3); Domain (1); Erroneous gene model prediction (1); Erroneous initiation (1); Modified residue (11); Region (1); Sequence conflict (2) FUNCTION: Plays a role as a key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation (PubMed:19778506). Enhances phosphoinositide 3-kinase (PI3K)-dependent phosphorylation and kinase activity of AKT1/PKB, but does not possess kinase activity itself (PubMed:15753085). Phosphorylation of AKT1/PKB thereby induces the phosphorylation of downstream effectors GSK3 and FOXO1/FKHR, and regulates DNA replication and cell proliferation (PubMed:15753085). Essential for the integrity of the actin cytoskeleton and for cell migration (By similarity). Required for formation of actin stress fibers and lamellipodia (By similarity). May be involved in membrane sorting in the early endosome (By similarity). Plays a role in ciliogenesis and cilium morphology and positioning and this may partly be through regulation of the localization of scaffolding protein Crocc/Rootletin (By similarity). {ECO:0000250|UniProtKB:Q3V6T2, ECO:0000269|PubMed:15753085, ECO:0000269|PubMed:19778506}. PTM: Phosphorylation is induced by epidermal growth factor (EGF) in a phosphoinositide 3-kinase (PI3K)-dependent manner. Phosphorylation by AKT1/PKB is necessary for the delocalization from the cell membrane and for cell migration (By similarity). {ECO:0000250|UniProtKB:Q3V6T2}. SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q3V6T2}. Cell membrane {ECO:0000250|UniProtKB:Q3V6T2}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q3V6T2}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q3V6T2}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q3V6T2}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q3V6T2}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q3V6T2}. Note=Localizes to the cell membrane through interaction with phosphoinositides. {ECO:0000250|UniProtKB:Q3V6T2}. SUBUNIT: Homodimer. The non-phosphorylated form interacts with phosphatidylinositol 4-phosphate [Pi(4)P] and weakly with phosphatidylinositol 3-phosphate [Pi(3)P] (By similarity). Interacts with microtubules. Interacts AKT1/PKB (via C-terminus). Interacts (via C-terminus) with DISC1; the interaction is direct. Interacts with AKT proteins; the interaction is inhibited in presence of DISC1. {ECO:0000250, ECO:0000269|PubMed:15753085, ECO:0000269|PubMed:15882442, ECO:0000269|PubMed:19778506}. TISSUE SPECIFICITY: Expressed in the dentate gyrus, pyramidal cell layer of hippocampal regions CA1 and CA3 at postnatal 15. Expressed highly in neurons. Weakly in neuron progenitors (at protein level). Expressed in the dentate granule cell layer of the hippocampus. Expressed highly in the adult testis, moderately in the brain and at a low level in the spleen, lungs and fat. {ECO:0000269|PubMed:15753085, ECO:0000269|PubMed:15882442, ECO:0000269|PubMed:19778506}. +O08742 GPV_MOUSE Platelet glycoprotein V (GPV) (Glycoprotein 5) (CD antigen CD42d) 567 63,468 Chain (1); Domain (2); Glycosylation (7); Repeat (14); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 523 543 Helical. {ECO:0000255}. TOPO_DOM 17 522 Extracellular. {ECO:0000255}.; TOPO_DOM 544 567 Cytoplasmic. {ECO:0000255}. FUNCTION: The GPIb-V-IX complex functions as the vWF receptor and mediates vWF-dependent platelet adhesion to blood vessels. The adhesion of platelets to injured vascular surfaces in the arterial circulation is a critical initiating event in hemostasis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. +Q68EF4 GRM4_MOUSE Metabotropic glutamate receptor 4 (mGluR4) 912 101,824 Alternative sequence (2); Binding site (4); Chain (1); Disulfide bond (8); Glycosylation (2); Region (1); Sequence conflict (1); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 587 607 Helical; Name=1. {ECO:0000255}.; TRANSMEM 625 645 Helical; Name=2. {ECO:0000255}.; TRANSMEM 654 671 Helical; Name=3. {ECO:0000255}.; TRANSMEM 700 720 Helical; Name=4. {ECO:0000255}.; TRANSMEM 752 772 Helical; Name=5. {ECO:0000255}.; TRANSMEM 787 807 Helical; Name=6. {ECO:0000255}.; TRANSMEM 827 847 Helical; Name=7. {ECO:0000255}. TOPO_DOM 33 586 Extracellular. {ECO:0000255}.; TOPO_DOM 608 624 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 646 653 Extracellular. {ECO:0000255}.; TOPO_DOM 672 699 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 721 751 Extracellular. {ECO:0000255}.; TOPO_DOM 773 786 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 808 826 Extracellular. {ECO:0000255}.; TOPO_DOM 848 912 Cytoplasmic. {ECO:0000255}. FUNCTION: G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Signaling inhibits adenylate cyclase activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with PICK1. {ECO:0000250}. +Q60934 GRIK1_MOUSE Glutamate receptor ionotropic, kainate 1 (GluK1) (Glutamate receptor 5) (GluR-5) (GluR5) 836 95,202 Binding site (1); Chain (1); Glycosylation (8); Natural variant (1); Region (2); Signal peptide (1); Topological domain (4); Transmembrane (3) TRANSMEM 562 582 Helical. {ECO:0000255}.; TRANSMEM 639 659 Helical. {ECO:0000255}.; TRANSMEM 722 742 Helical. {ECO:0000255}. TOPO_DOM 31 561 Extracellular. {ECO:0000255}.; TOPO_DOM 583 638 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 660 721 Extracellular. {ECO:0000255}.; TOPO_DOM 743 836 Cytoplasmic. {ECO:0000255}. FUNCTION: Ionotropic glutamate receptor. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. May be involved in the transmission of light information from the retina to the hypothalamus (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein. SUBUNIT: Homotetramer or heterotetramer of pore-forming glutamate receptor subunits. Tetramers may be formed by the dimerization of dimers (Probable). The unedited version (Q) assembles into a functional kainate-gated homomeric channel, whereas the edited version (R) is unable to produce channel activity when expressed alone. Both edited and unedited versions can form functional channels with GRIK4 and GRIK5. Interacts with KLHL17 (By similarity). {ECO:0000250, ECO:0000305}. TISSUE SPECIFICITY: Most abundant in the cerebellum. Also present in the suprachiasmatic nuclei of the hypothalamus. +P11352 GPX1_MOUSE Glutathione peroxidase 1 (GPx-1) (GSHPx-1) (EC 1.11.1.9) (Cellular glutathione peroxidase) (Selenium-dependent glutathione peroxidase 1) 201 22,329 Active site (1); Chain (1); Modified residue (12); Non-standard residue (1); Sequence caution (1); Site (1) FUNCTION: Protects the hemoglobin in erythrocytes from oxidative breakdown. PTM: During periods of oxidative stress, Sec-47 may react with a superoxide radical, irreversibly lose hydroselenide and be converted to dehydroalanine. {ECO:0000269|PubMed:21420488}. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Homotetramer. Interacts with MIEN1. {ECO:0000269|PubMed:17503775}. +P39087 GRIK2_MOUSE Glutamate receptor ionotropic, kainate 2 (GluK2) (Glutamate receptor 6) (GluR-6) (GluR6) (Glutamate receptor beta-2) (GluR beta-2) 908 102,486 Alternative sequence (1); Binding site (2); Chain (1); Cross-link (1); Disulfide bond (1); Glycosylation (8); Modified residue (2); Natural variant (3); Region (2); Sequence conflict (2); Signal peptide (1); Topological domain (4); Transmembrane (3) TRANSMEM 562 582 Helical. {ECO:0000255}.; TRANSMEM 639 659 Helical. {ECO:0000255}.; TRANSMEM 820 840 Helical. {ECO:0000255}. TOPO_DOM 32 561 Extracellular. {ECO:0000255}.; TOPO_DOM 583 638 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 660 819 Extracellular. {ECO:0000255}.; TOPO_DOM 841 908 Cytoplasmic. {ECO:0000255}. FUNCTION: Ionotropic glutamate receptor. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. May be involved in the transmission of light information from the retina to the hypothalamus. Modulates cell surface expression of NETO2. {ECO:0000269|PubMed:19217376}. PTM: Sumoylation mediates kainate receptor-mediated endocytosis and regulates synaptic transmission. Sumoylation is enhanced by PIAS3 and desumoylated by SENP1 (By similarity). {ECO:0000250}.; PTM: Ubiquitinated. Ubiquitination regulates the GRIK2 levels at the synapse by leading kainate receptor degradation through proteasome (By similarity). {ECO:0000250}.; PTM: Phosphorylated by PKC at Ser-868 upon agonist activation, this directly enhance sumoylation. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein. SUBUNIT: Homotetramer or heterotetramer of pore-forming glutamate receptor subunits. Tetramers may be formed by the dimerization of dimers (Probable). Assembles into a kainate-gated homomeric channel that does not bind AMPA. GRIK2 associated to GRIK5 forms functional channels that can be gated by AMPA. Interacts with DLG4 (By similarity). Interacts (via C-terminus) with KLHL17 (via kelch repeats); the interaction targets GRIK2 for degradation via ubiquitin-proteasome pathway (By similarity). Interacts with NETO2. {ECO:0000250, ECO:0000269|PubMed:19217376, ECO:0000305}. TISSUE SPECIFICITY: Most abundant in the cerebellum and the hypothalamus. +Q91Z53 GRHPR_MOUSE Glyoxylate reductase/hydroxypyruvate reductase (EC 1.1.1.79) (EC 1.1.1.81) 328 35,329 Active site (1); Binding site (5); Chain (1); Modified residue (2); Nucleotide binding (2); Region (2); Site (1) FUNCTION: Enzyme with hydroxy-pyruvate reductase, glyoxylate reductase and D-glycerate dehydrogenase enzymatic activities. Reduces hydroxypyruvate to D-glycerate, glyoxylate to glycolate oxidizes D-glycerate to hydroxypyruvate (By similarity). {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +Q8BTM9 GRP4_MOUSE RAS guanyl-releasing protein 4 673 74,907 Alternative sequence (5); Chain (1); Domain (3); Frameshift (1); Sequence conflict (6); Zinc finger (1) FUNCTION: Functions as a cation- and diacylglycerol (DAG)-regulated nucleotide exchange factor activating Ras through the exchange of bound GDP for GTP. May function in mast cells differentiation. {ECO:0000269|PubMed:12817022}. SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Note=Recruited to membranes upon activation by DAG. DOMAIN: The phorbol-ester/DAG-type zinc finger mediates the binding and the functional activation by DAG. TISSUE SPECIFICITY: Expressed by mast cells and their progenitors (at protein level). {ECO:0000269|PubMed:11956218, ECO:0000269|PubMed:12817022}. +Q3UNH4 GRIN1_MOUSE G protein-regulated inducer of neurite outgrowth 1 (GRIN1) 932 95,496 Chain (1); Erroneous initiation (1); Lipidation (2); Modified residue (13); Mutagenesis (1); Region (1); Sequence conflict (2) FUNCTION: May be involved in neurite outgrowth. {ECO:0000269|PubMed:10480904}. PTM: Palmitoylation on Cys-923 and/or Cys-924 is required for membrane targeting. {ECO:0000269|PubMed:15585744}. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. Cell projection, growth cone {ECO:0000250}. Note=Highly enriched in growth cone. SUBUNIT: Interacts with activated forms of GNAI1, GNAO1 and GNAZ. {ECO:0000269|PubMed:10480904, ECO:0000269|PubMed:15585744}. TISSUE SPECIFICITY: Expressed specifically in brain (at protein level). {ECO:0000269|PubMed:10480904}. +Q8BWS5 GRIN3_MOUSE G protein-regulated inducer of neurite outgrowth 3 (GRIN3) 763 80,485 Chain (1); Erroneous initiation (1); Modified residue (2) FUNCTION: May be involved in neurite outgrowth. {ECO:0000250}. +Q922B9 ITPI2_MOUSE Protein ITPRID2 (ITPR-interacting domain-containing protein 2) (Ki-ras-induced actin-interacting protein) (Sperm-specific antigen 2 homolog) 1252 136,947 Alternative sequence (2); Chain (1); Coiled coil (1); Cross-link (1); Erroneous initiation (3); Erroneous termination (1); Modified residue (24); Sequence conflict (10) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14673706}. Note=Located near the plasma membrane. Associated with actin filaments. May also exist as a membrane-bound form with extracellular regions (By similarity). {ECO:0000250}. +Q8BYN3 ITPK1_MOUSE Inositol-tetrakisphosphate 1-kinase (EC 2.7.1.134) (Inositol 1,3,4-trisphosphate 5/6-kinase) (Inositol-triphosphate 5/6-kinase) (Ins(1,3,4)P(3) 5/6-kinase) (EC 2.7.1.159) 419 46,145 Binding site (9); Chain (1); Domain (1); Metal binding (4); Modified residue (3); Nucleotide binding (1) FUNCTION: Kinase that can phosphorylate various inositol polyphosphate such as Ins(3,4,5,6)P4 or Ins(1,3,4)P3. Phosphorylates Ins(3,4,5,6)P4 at position 1 to form Ins(1,3,4,5,6)P5. This reaction is thought to have regulatory importance, since Ins(3,4,5,6)P4 is an inhibitor of plasma membrane Ca(2+)-activated Cl(-) channels, while Ins(1,3,4,5,6)P5 is not. Also phosphorylates Ins(1,3,4)P3 on O-5 and O-6 to form Ins(1,3,4,6)P4, an essential molecule in the hexakisphosphate (InsP6) pathway. Also acts as an inositol polyphosphate phosphatase that dephosphorylate Ins(1,3,4,5)P4 and Ins(1,3,4,6)P4 to Ins(1,3,4)P3, and Ins(1,3,4,5,6)P5 to Ins(3,4,5,6)P4. May also act as an isomerase that interconverts the inositol tetrakisphosphate isomers Ins(1,3,4,5)P4 and Ins(1,3,4,6)P4 in the presence of ADP and magnesium. Probably acts as the rate-limiting enzyme of the InsP6 pathway. Modifies TNF-alpha-induced apoptosis by interfering with the activation of TNFRSF1A-associated death domain (By similarity). Plays an important role in MLKL-mediated necroptosis. Produces highly phosphorylated inositol phosphates such as inositolhexakisphosphate (InsP6) which bind to MLKL mediating the release of an N-terminal auto-inhibitory region leading to its activation. Essential for activated phospho-MLKL to oligomerize and localize to the cell membrane during necroptosis (By similarity). {ECO:0000250|UniProtKB:Q13572}. PTM: Acetylation by EP300 and CREBBP destabilizes ITPK1, and down-regulates enzymatic activity. Deacetylated by SIRT1 (By similarity). {ECO:0000250}. SUBUNIT: Monomer. Interacts with GPS1/COPS1 (By similarity). {ECO:0000250}. +Q9Z0R4 ITSN1_MOUSE Intersectin-1 (EH and SH3 domains protein 1) 1714 194,297 Alternative sequence (1); Beta strand (5); Calcium binding (2); Chain (1); Coiled coil (1); Compositional bias (1); Domain (12); Helix (17); Modified residue (16); Motif (1); Region (1); Sequence conflict (4) FUNCTION: Adapter protein that may provide indirect link between the endocytic membrane traffic and the actin assembly machinery. May regulate the formation of clathrin-coated vesicles. Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but not TFR may involve association with DAB2. Inhibits ARHGAP31 activity toward RAC1. Acts as guanine nucleotide exchange factor (GEF) specific for the CDC42 GTPase. {ECO:0000269|PubMed:20585582}. SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}. Cell junction, synapse, synaptosome {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Membrane, clathrin-coated pit {ECO:0000250}. Note=Colocalizes with SGIP1 at the plasma membrane in structures corresponding most probably to clathrin-coated pits. {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm {ECO:0000250|UniProtKB:Q15811}. Nucleus envelope {ECO:0000250|UniProtKB:Q15811}. Note=Shuttles between the cytoplasm and nucleus in an XPO1/CRM1-dependent manner. {ECO:0000250|UniProtKB:Q15811}. SUBUNIT: Interacts with dynamin, CDC42, SNAP25 and SNAP23 (By similarity). Clusters several dynamin in a manner that is regulated by alternative splicing. Interacts with clathrin-associated proteins and other components of the endocytic machinery, such as SPIN90, EPS15, EPN1, EPN2, STON2, FCHO1, FCHO2 and DAB2 (PubMed:20448150). Interacts (via SH3 domains) with REPS1 and SGIP1 (By similarity). Interacts with ARHGAP31 (PubMed:11744688). Interacts with ADAM15 (By similarity). Interacts with PRRT2 (PubMed:26797119). Isoform 2: Interacts with LMNA (By similarity). Isoform 2: Interacts with importin subunit KPNA1; this is likely to mediate its import into the nucleus (PubMed:29599122). {ECO:0000250|UniProtKB:Q15811, ECO:0000269|PubMed:11744688, ECO:0000269|PubMed:20448150, ECO:0000269|PubMed:26797119, ECO:0000269|PubMed:29599122}. DOMAIN: SH3-3, SH3-4 and SH3-5, but not SH3-1 and SH3-2 domains, bind to dynamin (By similarity). SH3-1 and SH3-4 bind to ARHGAP31. {ECO:0000250}.; DOMAIN: The KLERQ domain binds to SNAP-25 and SNAP-23. {ECO:0000250}.; DOMAIN: In an autoinhibited form the SH3 domain 5 may bind intramolecularly to the DH domain, thus blocking the CDC42-binding site. {ECO:0000269|PubMed:20585582}. TISSUE SPECIFICITY: Widely expressed. Expressed at high levels in brain, heart and skeletal muscle. +Q810D6 GRWD1_MOUSE Glutamate-rich WD repeat-containing protein 1 (Protein A301) 446 49,224 Chain (1); Compositional bias (1); Modified residue (4); Repeat (5); Sequence conflict (1) FUNCTION: Histone binding-protein that regulates chromatin dynamics and minichromosome maintenance (MCM) loading at replication origins, possibly by promoting chromatin openness. {ECO:0000250|UniProtKB:Q9BQ67}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9BQ67}. Nucleus {ECO:0000250|UniProtKB:Q9BQ67}. Chromosome {ECO:0000250|UniProtKB:Q9BQ67}. Note=Present in the nucleus throughout interphase and is detached from chromatin at the onset of mitosis and rebinds at telophase when the pre-replication complexes (pre-RC) is formed (By similarity). {ECO:0000250|UniProtKB:Q9BQ67}. SUBUNIT: Interacts with METTL18. Interacts with CDT1; origin binding of GRWD1 is dependent on CDT1. Interacts with CDC6; origin binding of GRWD1 is dependent on CDC6. Binds to histone H2A-H2B and H3-H4 complexes. {ECO:0000250|UniProtKB:Q9BQ67}. +Q9JHI5 IVD_MOUSE Isovaleryl-CoA dehydrogenase, mitochondrial (IVD) (EC 1.3.8.4) 424 46,325 Active site (1); Binding site (4); Chain (1); Modified residue (10); Nucleotide binding (4); Region (3); Sequence conflict (2); Transit peptide (1) Amino-acid degradation; L-leucine degradation; (S)-3-hydroxy-3-methylglutaryl-CoA from 3-isovaleryl-CoA: step 1/3. PTM: Acetylation of Lys-76 is observed in liver mitochondria from fasted mice but not from fed mice. SUBCELLULAR LOCATION: Mitochondrion matrix. SUBUNIT: Homotetramer. {ECO:0000250}. +Q9EST1 GSDMA_MOUSE Gasdermin-A (Gasdermin-1) (Gasdermin-A1) 446 49,593 Chain (1); Region (1) FUNCTION: May promote pyroptosis. Upon cleavage in vitro of genetically engineered GSDMA, the released N-terminal moiety binds to some types of lipids, such as possibly phosphatidylinositol (4,5)-bisphosphate. Homooligomerizes within the membrane and forms pores of 10 -15 nanometers (nm) of inner diameter, triggering cell death. Also binds to bacterial and mitochondrial lipids, including cardiolipin, and exhibits bactericidal activity. The physiological relevance of these observations is unknown. {ECO:0000250|UniProtKB:Q96QA5}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q96QA5}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P57764}. Cell membrane {ECO:0000250|UniProtKB:P57764}. SUBUNIT: The N-terminal moiety forms homooligomer; disulfide-linked. May form an 16-mer complex. Oligomerization occurs in the presence of membranes. {ECO:0000250|UniProtKB:P57764}. DOMAIN: Intramolecular interactions between N- and C-terminal domains may be important for autoinhibition in the absence of activation signal. The intrinsic pyroptosis-inducing activity is carried by the N-terminal domain. {ECO:0000250|UniProtKB:Q5Y4Y6}. TISSUE SPECIFICITY: Expressed predominantly in the gastrointestinal (GI) tract and in the skin at a lower level. In the GI tract, the expression is highly restricted to the esophagus and forestomach. {ECO:0000269|PubMed:10967128, ECO:0000269|PubMed:17350798}. +Q6NVG7 GT252_MOUSE Procollagen galactosyltransferase 2 (EC 2.4.1.50) (Collagen beta(1-O)galactosyltransferase 2) (Glycosyltransferase 25 family member 2) (Hydroxylysine galactosyltransferase 2) 625 72,788 Chain (1); Glycosylation (4); Motif (1); Sequence conflict (2); Signal peptide (1) FUNCTION: Beta-galactosyltransferase that transfers beta-galactose to hydroxylysine residues of collagen. {ECO:0000250|UniProtKB:Q8IYK4}. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138}. +P19157 GSTP1_MOUSE Glutathione S-transferase P 1 (Gst P1) (EC 2.5.1.18) (GST YF-YF) (GST class-pi) (GST-piB) (Preadipocyte growth factor) 210 23,609 Beta strand (9); Binding site (4); Chain (1); Domain (2); Helix (12); Initiator methionine (1); Mass spectrometry (1); Modified residue (5); Region (2); Turn (1) FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Can metabolize 1-chloro-2,4-dinitrobenzene. Regulates negatively CDK5 activity via p25/p35 translocation to prevent neurodegeneration (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Mitochondrion {ECO:0000250}. Nucleus {ECO:0000250}. Note=The 83 N-terminal amino acids function as un uncleaved transit peptide, and arginine residues within it are crucial for mitochondrial localization. {ECO:0000250}. SUBUNIT: Homodimer. Interacts with CDK5 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed. +Q8BW56 GTDC1_MOUSE Glycosyltransferase-like domain-containing protein 1 445 51,017 Alternative sequence (3); Chain (1); Erroneous initiation (2) +Q9JLF1 GBRT_MOUSE Gamma-aminobutyric acid receptor subunit theta (GABA(A) receptor subunit theta) 638 72,799 Chain (1); Disulfide bond (1); Glycosylation (1); Signal peptide (1); Topological domain (1); Transmembrane (3) TRANSMEM 268 288 Helical. {ECO:0000255}.; TRANSMEM 326 346 Helical. {ECO:0000255}.; TRANSMEM 618 638 Helical. {ECO:0000255}. TOPO_DOM 22 267 Extracellular. {ECO:0000255}. FUNCTION: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. SUBUNIT: Generally pentameric. This subunit coassembles with alpha-2, beta-1 and gamma-1. +P50571 GBRB1_MOUSE Gamma-aminobutyric acid receptor subunit beta-1 (GABA(A) receptor subunit beta-1) 474 54,100 Binding site (1); Chain (1); Disulfide bond (1); Glycosylation (3); Region (3); Signal peptide (1); Topological domain (2); Transmembrane (4) TRANSMEM 246 267 Helical. {ECO:0000305}.; TRANSMEM 271 293 Helical. {ECO:0000305}.; TRANSMEM 305 327 Helical. {ECO:0000305}.; TRANSMEM 452 473 Helical. {ECO:0000305}. TOPO_DOM 26 245 Extracellular. {ECO:0000305}.; TOPO_DOM 328 451 Cytoplasmic. {ECO:0000305}. FUNCTION: Component of the heteropentameric receptor for GABA, the major inhibitory neurotransmitter in the vertebrate brain. Functions also as histamine receptor and mediates cellular responses to histamine (By similarity). Functions as receptor for diazepines and various anesthetics, such as pentobarbital; these are bound at a separate allosteric effector binding site. Functions as ligand-gated chloride channel. {ECO:0000250, ECO:0000269|PubMed:20400944}. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane {ECO:0000269|PubMed:20400944}; Multi-pass membrane protein {ECO:0000269|PubMed:20400944}. Cell membrane {ECO:0000269|PubMed:20400944}; Multi-pass membrane protein {ECO:0000269|PubMed:20400944}. SUBUNIT: Heteropentamer, formed by a combination of alpha, beta, gamma, delta and rho chains. Binds UBQLN1. Interacts with KCTD8, KCTD12, KCTD12B and KCTD16; this interaction determines the pharmacology and kinetics of the receptor response, the KCTD proteins markedly accelerating the GABA-B response, although to different extents. {ECO:0000269|PubMed:11528422, ECO:0000269|PubMed:20400944}. +P48540 GDNF_MOUSE Glial cell line-derived neurotrophic factor (mGDNF) (Astrocyte-derived trophic factor) (ATF) 211 23,662 Alternative sequence (2); Chain (1); Disulfide bond (4); Glycosylation (2); Propeptide (1); Signal peptide (1) FUNCTION: Neurotrophic factor that enhances survival and morphological differentiation of dopaminergic neurons and increases their high-affinity dopamine uptake. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Homodimer; disulfide-linked. TISSUE SPECIFICITY: Expressed in both the central nervous system (CNS) and in non-CNS tissues. Expressed in a highly dynamic pattern in the anterior neuroectoderm during the early stages of neurogenesis between E7.5 and E10.5. Beginning at E10.5, expression begins in mesenchymal tissues of several organs including the digestive tract, kidney, testis, frontonasal mass, tooth primordium, tongue, mandible, whisker follicles, ear, eye, limb bud and in distinct regions of the brain. Also expressed in the heart, ileum, liver and muscle. {ECO:0000269|PubMed:12168040, ECO:0000269|PubMed:8808409}. +Q9ESY9 GILT_MOUSE Gamma-interferon-inducible lysosomal thiol reductase (EC 1.8.-.-) (Gamma-interferon-inducible protein IP-30) (Lysosomal thiol reductase IP30) 248 27,784 Chain (1); Disulfide bond (1); Erroneous initiation (1); Glycosylation (2); Propeptide (2); Sequence conflict (6); Signal peptide (1) FUNCTION: Lysosomal thiol reductase that can reduce protein disulfide bonds. May facilitate the complete unfolding of proteins destined for lysosomal degradation. Plays an important role in antigen processing. Facilitates the generation of MHC class II-restricted epitodes from disulfide bond-containing antigen by the endocytic reduction of disulfide bonds. Facilitates also MHC class I-restricted recognition of exogenous antigens containing disulfide bonds by CD8+ T-cells or crosspresentation. {ECO:0000269|PubMed:11701933, ECO:0000269|PubMed:18815593, ECO:0000269|PubMed:20538950}. PTM: N-glycosylated. Sugar chains contain mannose-6-phosphate (By similarity). {ECO:0000250}.; PTM: Synthesized as a 35 kDa precursor which is then processed into the mature 30 kDa form via cleavage of N-terminal and C-terminal propeptides. Processing of the precursor is mediated by multiple lysosomal proteases (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Lysosome {ECO:0000269|PubMed:11701933}. SUBUNIT: Dimer; disulfide-linked. {ECO:0000250}. +Q0P543 GIPR_MOUSE Gastric inhibitory polypeptide receptor (GIP-R) (Glucose-dependent insulinotropic polypeptide receptor) 460 52,992 Alternative sequence (2); Chain (1); Disulfide bond (3); Glycosylation (3); Sequence conflict (1); Signal peptide (1); Topological domain (7); Transmembrane (6) TRANSMEM 135 155 Helical; Name=1. {ECO:0000255}.; TRANSMEM 223 243 Helical; Name=2. {ECO:0000255}.; TRANSMEM 256 276 Helical; Name=3. {ECO:0000255}.; TRANSMEM 298 318 Helical; Name=4. {ECO:0000255}.; TRANSMEM 338 358 Helical; Name=5. {ECO:0000255}.; TRANSMEM 371 391 Helical; Name=6. {ECO:0000255}. TOPO_DOM 19 134 Extracellular. {ECO:0000255}.; TOPO_DOM 156 222 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 244 255 Extracellular. {ECO:0000255}.; TOPO_DOM 277 297 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 319 337 Extracellular. {ECO:0000255}.; TOPO_DOM 359 370 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 392 460 Extracellular. {ECO:0000255}. FUNCTION: This is a receptor for GIP. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase (By similarity). {ECO:0000250}. PTM: N-glycosylation is required for cell surface expression and lengthens receptor half-life by preventing degradation in the ER. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBUNIT: May form homodimers and heterodimers with GLP1R. {ECO:0000250}. +Q8BWF2 GIMA5_MOUSE GTPase IMAP family member 5 (Immunity-associated nucleotide 4-like 1 protein) (Immunity-associated protein 3) 308 34,653 Binding site (2); Chain (1); Domain (1); Nucleotide binding (2); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 284 304 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 1 283 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 305 308 Mitochondrial intermembrane. {ECO:0000255}. FUNCTION: Required for mitochondrial integrity and T-cell survival. May contribute to T-cell quiescence (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Lysosome {ECO:0000269|PubMed:21487483}. +Q99JP7 GGT7_MOUSE Glutathione hydrolase 7 (EC 3.4.19.13) (Gamma-glutamyltransferase 7) (GGT 7) (EC 2.3.2.2) (Gamma-glutamyltransferase-like 3) (Gamma-glutamyltranspeptidase 7) [Cleaved into: Glutathione hydrolase 7 heavy chain; Glutathione hydrolase 7 light chain] 662 70,251 Chain (2); Glycosylation (9); Modified residue (4); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 107 127 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 106 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 128 662 Extracellular. {ECO:0000255}. Sulfur metabolism; glutathione metabolism. FUNCTION: Cleaves glutathione conjugates. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. SUBUNIT: Heterodimer composed of the light and heavy chains. The active site is located in the light chain. Interacts with FAM57A (By similarity). {ECO:0000250}. +A4FUP9 GL1D1_MOUSE Glycosyltransferase 1 domain-containing protein 1 (EC 2.4.-.-) 346 38,841 Alternative sequence (2); Chain (1); Sequence conflict (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q9BDB7 IF44L_MOUSE Interferon-induced protein 44-like [Cleaved into: Minor histocompatibility antigen HA-28 (HLA-HA28) (IFL8)] 447 49,680 Alternative sequence (1); Chain (1); Frameshift (1); Peptide (1); Sequence conflict (5) FUNCTION: Precursor of the histocompatibility antigen HA-28 in BALB.B mice. More generally, minor histocompatibility antigens refer to immunogenic peptide which, when complexed with MHC, can generate an immune response after recognition by specific T-cells. The peptides are derived from polymorphic intracellular proteins, which are cleaved by normal pathways of antigen processing. The binding of these peptides to MHC molecules and its expression on the cell surface can stimulate T-cell responses and thereby trigger graft rejection or graft-versus-host disease (GVHD). More specifically, HA-28 minor antigen is transcribed in the BALB.B donor but not in host C57BL/6 cells. HA-28 is presented to the donor BALB.B cell surface by Kb MHC. This complex HA-28/Kb MHC elicits cytotoxic T-cell response in C57BL/6 mice immunized with BALB.B spleen cells. It induces C57BL/6 mice cells recognition and lysis by CD8 T-cell from BALB.B mice. {ECO:0000269|PubMed:11021531}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11021531}. SUBUNIT: HA-28 antigen forms a complex with Kb MHC in BALB.B donor cells. TISSUE SPECIFICITY: Expressed on cells of the hematopoietic lineage. Detected in transformed cell lines of the macrophage and B-cell lineage. Expressed in spleen and bone marrow. {ECO:0000269|PubMed:11021531}. +O88513 GEMI_MOUSE Geminin 206 23,300 Chain (1); Coiled coil (1); Helix (2); Modified residue (5); Region (2); Turn (1) FUNCTION: Inhibits DNA replication by preventing the incorporation of MCM complex into pre-replication complex (pre-RC). It is degraded during the mitotic phase of the cell cycle. Its destruction at the metaphase-anaphase transition permits replication in the succeeding cell cycle. {ECO:0000269|PubMed:12192004, ECO:0000269|PubMed:9635433}.; FUNCTION: Inhibits the transcriptional activity of a subset of Hox proteins, enrolling them in cell proliferative control. {ECO:0000250}. PTM: Phosphorylated during mitosis. Phosphorylation at Ser-181 by CK2 results in enhanced binding to Hox proteins and more potent inhibitory effect on Hox transcriptional activity. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Mainly cytoplasmic but can be relocalized to the nucleus. {ECO:0000250}. "SUBUNIT: Homotetramer. Interacts (via coiled-coil domain) with IDAS (via coiled-coil domain); this targets GMNN to the nucleus. The heterodimer formed by GMNN and MCIDAS has much lower affinity for CDT1 than the GMNN homodimer. Interacts with a subset of Hox proteins, affinity increasing from anterior to posterior types, the strongest interaction being with HOXB1, HOXC9 and HOXD10. Interacts with LRWD1 from G1/S to mitosis (By similarity). Interacts with CDT1; this inhibits binding of the MCM complex to origins of replication. The complex with CDT1 exists in two forms, a ""permissive"" heterotrimer and an ""inhibitory"" heterohexamer. {ECO:0000250, ECO:0000269|PubMed:12192004, ECO:0000269|PubMed:15286659}." +Q91WR6 GINM1_MOUSE Glycoprotein integral membrane protein 1 327 36,079 Chain (1); Glycosylation (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 260 280 Helical. {ECO:0000255}. TOPO_DOM 24 259 Extracellular. {ECO:0000255}.; TOPO_DOM 281 327 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q8BMF8 GLDN_MOUSE Gliomedin (Cancer-related gene liver 2 protein) (CRG-L2) [Cleaved into: Gliomedin shedded ectodomain] 549 59,137 Beta strand (20); Chain (2); Compositional bias (1); Domain (3); Erroneous initiation (1); Glycosylation (6); Helix (3); Mutagenesis (2); Sequence conflict (1); Site (2); Topological domain (2); Transmembrane (1); Turn (4) TRANSMEM 18 38 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 17 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 39 549 Extracellular. {ECO:0000255}. FUNCTION: Ligand for NRCAM and NFASC/neurofascin that plays a role in the formation and maintenance of the nodes of Ranvier on myelinated axons. Mediates interaction between Schwann cell microvilli and axons via its interactions with NRCAM and NFASC (PubMed:20188654). Nodes of Ranvier contain clustered sodium channels that are crucial for the saltatory propagation of action potentials along myelinated axons. During development, nodes of Ranvier are formed by the fusion of two heminodes. Required for normal clustering of sodium channels at heminodes; not required for the formation of mature nodes with normal sodium channel clusters (PubMed:20188654). Required, together with NRCAM, for maintaining NFASC and sodium channel clusters at mature nodes of Ranvier (PubMed:24719088). {ECO:0000250|UniProtKB:Q80WL1, ECO:0000269|PubMed:20188654, ECO:0000269|PubMed:24719088}. PTM: N-glycosylated. {ECO:0000269|PubMed:17293346}.; PTM: Proteolytic proccessing by a furin-like protease causes shedding of the ectodomain. Further cleavage by BMP1 releases the olfactomedin-like domain. {ECO:0000269|PubMed:17293346}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17293346}; Single-pass type II membrane protein {ECO:0000305|PubMed:17293346}. Cell projection, axon {ECO:0000269|PubMed:17293346, ECO:0000269|PubMed:20188654}. Note=Localizes to the nodes of Ranvier (PubMed:17293346, PubMed:20188654). Detected at immature heminodes (By similarity). {ECO:0000250|UniProtKB:Q80WL1, ECO:0000269|PubMed:17293346, ECO:0000269|PubMed:20188654}.; SUBCELLULAR LOCATION: Gliomedin shedded ectodomain: Secreted {ECO:0000269|PubMed:17293346}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q80WL1}. Note=Proteolytic processing gives rise to a soluble extracellular domain that is secreted (PubMed:17293346). The gliomedin shedded ectodomain localizes to the nodes of Ranvier (By similarity). {ECO:0000250|UniProtKB:Q80WL1, ECO:0000269|PubMed:17293346}. SUBUNIT: Homotrimer (via collagen-like domains) (PubMed:17293346). Interacts with NRCAM and NFASC/neurofascin (PubMed:16039564, PubMed:20188654). Interaction with glial NRCAM enhances interaction with axonal NFASC (PubMed:20188654). Interacts with MYOC (PubMed:23897819). {ECO:0000269|PubMed:16039564, ECO:0000269|PubMed:17293346, ECO:0000269|PubMed:20188654, ECO:0000269|PubMed:23897819}. DOMAIN: The olfactomedin-like domain mediates NFASC/neurofascin and NRCAM binding. {ECO:0000269|PubMed:20188654}. TISSUE SPECIFICITY: Detected in sciatic nerve (at protein level) (PubMed:17293346, PubMed:20188654, PubMed:24719088). Widely expressed with higher expression in testis and skeletal muscle (PubMed:12642876). {ECO:0000269|PubMed:12642876, ECO:0000269|PubMed:17293346, ECO:0000269|PubMed:20188654, ECO:0000269|PubMed:24719088}. +Q8BGD9 IF4B_MOUSE Eukaryotic translation initiation factor 4B (eIF-4B) 611 68,840 Chain (1); Compositional bias (2); Cross-link (1); Domain (1); Modified residue (23) FUNCTION: Required for the binding of mRNA to ribosomes. Functions in close association with EIF4-F and EIF4-A. Binds near the 5'-terminal cap of mRNA in presence of EIF-4F and ATP. Promotes the ATPase activity and the ATP-dependent RNA unwinding activity of both EIF4-A and EIF4-F (By similarity). {ECO:0000250}. PTM: Phosphorylated at Ser-422 by RPS6KA1 and RPS6KB1; phosphorylation enhances the affinity of EIF4B for the EIF3 complex. {ECO:0000250}. SUBUNIT: Self-associates and interacts with EIF3 p170 subunit. {ECO:0000250}. +Q8BMB3 IF4E2_MOUSE Eukaryotic translation initiation factor 4E type 2 (eIF-4E type 2) (eIF4E type 2) (eIF4E-2) (mRNA cap-binding protein type 2) (Eukaryotic translation initiation factor 4E-like 3) (eIF4E-like protein 4E-LP) 245 28,263 Binding site (1); Chain (1); Cross-link (2); Modified residue (2); Region (7); Sequence conflict (1) FUNCTION: Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation (PubMed:15153109). Acts as a repressor of translation initiation (By similarity). In contrast to EIF4E, it is unable to bind eIF4G (EIF4G1, EIF4G2 or EIF4G3), suggesting that it acts by competing with EIF4E and block assembly of eIF4F at the cap (PubMed:15153109). {ECO:0000250|UniProtKB:O60573, ECO:0000269|PubMed:15153109}. PTM: Ubiquitinated by ARIH1. The consequences of ubiquitination are however unclear: according to a report, EIF4E2 ubiquitination leads to promote EIF4E2 cap-binding and protein translation arrest. According to another report ubiquitination leads to its subsequent degradation. {ECO:0000250|UniProtKB:O60573}.; PTM: ISGylation enhances its cap structure-binding activity and translation-inhibition activity. {ECO:0000250|UniProtKB:O60573}. SUBUNIT: Interacts with EIF4EBP1, EIF4EBP2 and EIF4EBP3 (PubMed:15153109). Does not interact with eIF4G (EIF4G1, EIF4G2 or EIF4G3) (PubMed:15153109). Component of the 4EHP-GYF2 complex, at least composed of EIF4E2, GIGYF2 and ZNF598 (By similarity). Interacts with GIGYF2 (via the 4EHP-binding motif); the interaction is direct (By similarity). {ECO:0000250|UniProtKB:O60573, ECO:0000269|PubMed:15153109}. TISSUE SPECIFICITY: Widely expressed with highest levels in testis, kidney and liver. {ECO:0000269|PubMed:15153109}. +Q9DBB5 IF4E3_MOUSE Eukaryotic translation initiation factor 4E type 3 (eIF-4E type 3) (eIF-4E3) (eIF4E type 3) (eIF4E-3) 207 22,836 Beta strand (9); Chain (1); Helix (8); Region (2); Sequence conflict (1); Turn (6) FUNCTION: Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis. May act as an inhibitor of EIF4E1 activity. {ECO:0000269|PubMed:15153109}. SUBUNIT: eIF4F is a multi-subunit complex, the composition of which varies with external and internal environmental conditions. It is composed of at least eIF4A, eIF4E and eIF4G (By similarity). EIF4E3 interacts with EIF4G1, but not with EIF4EBP1, EIF4EBP2 and EIF4EBP3. {ECO:0000250, ECO:0000269|PubMed:15153109}. TISSUE SPECIFICITY: Only expressed in heart, skeletal muscle, lung and spleen. {ECO:0000269|PubMed:15153109}. +Q8BZR0 GPR82_MOUSE Probable G-protein coupled receptor 82 328 37,555 Chain (1); Glycosylation (2); Topological domain (7); Transmembrane (6) TRANSMEM 12 32 Helical; Name=1. {ECO:0000255}.; TRANSMEM 56 76 Helical; Name=2. {ECO:0000255}.; TRANSMEM 93 115 Helical; Name=3. {ECO:0000255}.; TRANSMEM 157 177 Helical; Name=4. {ECO:0000255}.; TRANSMEM 198 218 Helical; Name=5. {ECO:0000255}.; TRANSMEM 252 272 Helical; Name=6. {ECO:0000255}. TOPO_DOM 1 11 Extracellular. {ECO:0000255}.; TOPO_DOM 33 55 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 77 92 Extracellular. {ECO:0000255}.; TOPO_DOM 116 156 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 178 197 Extracellular. {ECO:0000255}.; TOPO_DOM 219 251 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 273 328 Extracellular. {ECO:0000255}. FUNCTION: Orphan receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q9JHC0 GPX2_MOUSE Glutathione peroxidase 2 (GPx-2) (GSHPx-2) (EC 1.11.1.9) (Glutathione peroxidase-gastrointestinal) (GPx-GI) (GSHPx-GI) 190 21,990 Active site (1); Chain (1); Non-standard residue (1); Sequence conflict (1) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homotetramer. {ECO:0000250}. +Q9D7B7 GPX8_MOUSE Probable glutathione peroxidase 8 (GPx-8) (GSHPx-8) (EC 1.11.1.9) 209 24,148 Active site (1); Chain (1); Modified residue (1); Sequence conflict (1); Transmembrane (1) TRANSMEM 18 40 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q3UVX5 GRM5_MOUSE Metabotropic glutamate receptor 5 (mGluR5) 1203 131,865 Alternative sequence (2); Binding site (5); Chain (1); Compositional bias (3); Disulfide bond (10); Glycosylation (6); Modified residue (5); Region (2); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 580 602 Helical; Name=1. {ECO:0000250}.; TRANSMEM 613 635 Helical; Name=2. {ECO:0000250}.; TRANSMEM 644 666 Helical; Name=3. {ECO:0000250}.; TRANSMEM 693 713 Helical; Name=4. {ECO:0000250}.; TRANSMEM 737 758 Helical; Name=5. {ECO:0000250}.; TRANSMEM 772 794 Helical; Name=6. {ECO:0000250}.; TRANSMEM 798 819 Helical; Name=7. {ECO:0000250}. TOPO_DOM 19 579 Extracellular. {ECO:0000250}.; TOPO_DOM 603 612 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 636 643 Extracellular. {ECO:0000250}.; TOPO_DOM 667 692 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 714 736 Extracellular. {ECO:0000250}.; TOPO_DOM 759 771 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 795 797 Extracellular. {ECO:0000250}.; TOPO_DOM 820 1203 Cytoplasmic. {ECO:0000250}. FUNCTION: G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Signaling activates a phosphatidylinositol-calcium second messenger system and generates a calcium-activated chloride current. Plays an important role in the regulation of synaptic plasticity and the modulation of the neural network activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: The PPXXF motif binds HOMER1, HOMER2 and HOMER3. Interacts with RYR1, RYR2, ITPR1, SHANK1 and SHANK3 (By similarity). Interacts with SIAH1 and GRASP. Interacts with NCDN. Interacts with NECAB2 (By similarity). Interacts with CAMK2A (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P31424, ECO:0000250|UniProtKB:P41594}. +B1AS29 GRIK3_MOUSE Glutamate receptor ionotropic, kainate 3 (GluK3) (Glutamate receptor 7) (GluR-7) (GluR7) 919 104,051 Binding site (3); Chain (1); Cross-link (1); Disulfide bond (1); Glycosylation (6); Modified residue (1); Region (1); Signal peptide (1); Topological domain (4); Transmembrane (3) TRANSMEM 564 584 Helical. {ECO:0000255}.; TRANSMEM 637 657 Helical. {ECO:0000255}.; TRANSMEM 821 841 Helical. {ECO:0000255}. TOPO_DOM 32 563 Extracellular. {ECO:0000250}.; TOPO_DOM 585 636 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 658 820 Extracellular. {ECO:0000255}.; TOPO_DOM 842 919 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for glutamate that functions as ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists. This receptor binds domoate > kainate >> L-glutamate = quisqualate >> AMPA = NMDA (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Homotetramer, and heterotetramer with either GRIK4 or GRIK5. Interacts with PRKCABP (By similarity). Interacts with NETO2 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Detected in whole brain, cerebellum, brain cortex and hippocampus. {ECO:0000269|PubMed:11124978}. +P47743 GRM8_MOUSE Metabotropic glutamate receptor 8 (mGluR8) 908 101,828 Binding site (4); Chain (1); Cross-link (1); Disulfide bond (8); Glycosylation (5); Mutagenesis (3); Region (1); Sequence conflict (7); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 584 608 Helical; Name=1. {ECO:0000255}.; TRANSMEM 621 641 Helical; Name=2. {ECO:0000255}.; TRANSMEM 648 668 Helical; Name=3. {ECO:0000255}.; TRANSMEM 696 716 Helical; Name=4. {ECO:0000255}.; TRANSMEM 747 768 Helical; Name=5. {ECO:0000255}.; TRANSMEM 782 803 Helical; Name=6. {ECO:0000255}.; TRANSMEM 819 843 Helical; Name=7. {ECO:0000255}. TOPO_DOM 34 583 Extracellular. {ECO:0000255}.; TOPO_DOM 609 620 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 642 647 Extracellular. {ECO:0000255}.; TOPO_DOM 669 695 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 717 746 Extracellular. {ECO:0000255}.; TOPO_DOM 769 781 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 804 818 Extracellular. {ECO:0000255}.; TOPO_DOM 844 908 Cytoplasmic. {ECO:0000255}. FUNCTION: G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Signaling inhibits adenylate cyclase activity. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBUNIT: Interacts with PICK1. {ECO:0000250}. TISSUE SPECIFICITY: Strongly expressed in olfactory bulb, accessory olfactory bulb, and mammillary body. Weaker expression in the retina, and in scattered cells in the cortex and hindbrain. +Q61626 GRIK5_MOUSE Glutamate receptor ionotropic, kainate 5 (GluK5) (Glutamate receptor KA-2) (KA2) (Glutamate receptor gamma-2) (GluR gamma-2) 979 109,276 Chain (1); Compositional bias (1); Disulfide bond (3); Glycosylation (10); Sequence conflict (1); Signal peptide (1); Topological domain (4); Transmembrane (3) TRANSMEM 545 565 Helical. {ECO:0000255}.; TRANSMEM 623 643 Helical. {ECO:0000255}.; TRANSMEM 804 824 Helical. {ECO:0000255}. TOPO_DOM 15 544 Extracellular. {ECO:0000255}.; TOPO_DOM 566 622 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 644 803 Extracellular. {ECO:0000255}.; TOPO_DOM 825 979 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for glutamate. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists. This receptor binds kainate > quisqualate = glutamate >> AMPA. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein. SUBUNIT: Tetramer of two or more different subunits. Associates with GRIK1 (both edited and unedited versions), GRIK2, or GRIK3 to form functional channels. Homomeric associations do not produce any channel activity (By similarity). {ECO:0000250}. +P97772 GRM1_MOUSE Metabotropic glutamate receptor 1 (mGluR1) 1199 133,212 Alternative sequence (4); Binding site (5); Chain (1); Compositional bias (4); Disulfide bond (6); Glycosylation (5); Modified residue (8); Region (1); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 593 615 Helical; Name=1. {ECO:0000250}.; TRANSMEM 630 650 Helical; Name=2. {ECO:0000250}.; TRANSMEM 659 680 Helical; Name=3. {ECO:0000250}.; TRANSMEM 704 727 Helical; Name=4. {ECO:0000250}.; TRANSMEM 751 772 Helical; Name=5. {ECO:0000250}.; TRANSMEM 786 807 Helical; Name=6. {ECO:0000250}.; TRANSMEM 816 840 Helical; Name=7. {ECO:0000250}. TOPO_DOM 21 592 Extracellular. {ECO:0000250}.; TOPO_DOM 616 629 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 651 658 Extracellular. {ECO:0000250}.; TOPO_DOM 681 703 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 728 750 Extracellular. {ECO:0000250}.; TOPO_DOM 773 785 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 808 815 Extracellular. {ECO:0000250}.; TOPO_DOM 841 1199 Cytoplasmic. {ECO:0000250}. FUNCTION: G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Signaling activates a phosphatidylinositol-calcium second messenger system. May participate in the central action of glutamate in the CNS, such as long-term potentiation in the hippocampus and long-term depression in the cerebellum (By. similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBUNIT: Homodimer; disulfide-linked. The PPXXF motif binds HOMER1, HOMER2 and HOMER3. Interacts with SIAH1, RYR1, RYR2, ITPR1, SHANK1, SHANK3 and GRASP (By similarity). {ECO:0000250}. +Q9WV60 GSK3B_MOUSE Glycogen synthase kinase-3 beta (GSK-3 beta) (EC 2.7.11.26) (Serine/threonine-protein kinase GSK3B) (EC 2.7.11.1) 420 46,710 Active site (1); Beta strand (10); Binding site (1); Chain (1); Domain (1); Helix (20); Modified residue (3); Mutagenesis (2); Nucleotide binding (1); Turn (4) FUNCTION: Constitutively active protein kinase that acts as a negative regulator in the hormonal control of glucose homeostasis, Wnt signaling and regulation of transcription factors and microtubules, by phosphorylating and inactivating glycogen synthase (GYS1 or GYS2), EIF2B, CTNNB1/beta-catenin, APC, AXIN1, DPYSL2/CRMP2, JUN, NFATC1/NFATC, MAPT/TAU and MACF1. Requires primed phosphorylation of the majority of its substrates. In skeletal muscle, contributes to insulin regulation of glycogen synthesis by phosphorylating and inhibiting GYS1 activity and hence glycogen synthesis. May also mediate the development of insulin resistance by regulating activation of transcription factors. Regulates protein synthesis by controlling the activity of initiation factor 2B (EIF2BE/EIF2B5) in the same manner as glycogen synthase. In Wnt signaling, GSK3B forms a multimeric complex with APC, AXIN1 and CTNNB1/beta-catenin and phosphorylates the N-terminus of CTNNB1 leading to its degradation mediated by ubiquitin/proteasomes. Phosphorylates JUN at sites proximal to its DNA-binding domain, thereby reducing its affinity for DNA. Phosphorylates NFATC1/NFATC on conserved serine residues promoting NFATC1/NFATC nuclear export, shutting off NFATC1/NFATC gene regulation, and thereby opposing the action of calcineurin. Phosphorylates MAPT/TAU on 'Thr-548', decreasing significantly MAPT/TAU ability to bind and stabilize microtubules. Plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. Phosphorylates MACF1, inhibiting its binding to microtubules which is critical for its role in bulge stem cell migration and skin wound repair. Probably regulates NF-kappa-B (NFKB1) at the transcriptional level and is required for the NF-kappa-B-mediated anti-apoptotic response to TNF-alpha (TNF/TNFA). Negatively regulates replication in pancreatic beta-cells, resulting in apoptosis, loss of beta-cells. Through phosphorylation of the anti-apoptotic protein MCL1, may control cell apoptosis in response to growth factors deprivation. Phosphorylates MUC1 in breast cancer cells, decreasing the interaction of MUC1 with CTNNB1/beta-catenin. Is necessary for the establishment of neuronal polarity and axon outgrowth. Phosphorylates MARK2, leading to inhibit its activity. Phosphorylates SIK1 at 'Thr-182', leading to sustain its activity. Phosphorylates ZC3HAV1 which enhances its antiviral activity. Phosphorylates SFPQ at 'Thr-679' upon T-cell activation. Phosphorylates SNAI1, leading to its BTRC-triggered ubiquitination and proteasomal degradation. Phosphorylates NR1D1 st 'Ser-55' and 'Ser-59' and stabilizes it by protecting it from proteasomal degradation. Regulates the circadian clock via phosphorylation of the major clock components including ARNTL/BMAL1, CLOCK and PER2. Phosphorylates CLOCK AT 'Ser-427' and targets it for proteasomal degradation. Phosphorylates ARNTL/BMAL1 at 'Ser-17' and 'Ser-21' and primes it for ubiquitination and proteasomal degradation. Phosphorylates OGT at 'Ser-3' or 'Ser-4' which positively regulates its activity. {ECO:0000269|PubMed:10894547, ECO:0000269|PubMed:15791206, ECO:0000269|PubMed:16543145, ECO:0000269|PubMed:17391670, ECO:0000269|PubMed:18288891, ECO:0000269|PubMed:20049328, ECO:0000269|PubMed:20123978, ECO:0000269|PubMed:21295697, ECO:0000269|PubMed:22057101, ECO:0000269|PubMed:23395175}. PTM: Phosphorylated by AKT1 and ILK1. Upon insulin-mediated signaling, the activated PKB/AKT1 protein kinase phosphorylates and desactivates GSK3B, resulting in the dephosphorylation and activation of GYS1. Activated by phosphorylation at Tyr-216. Phosphorylation of Ser-9 in the hippocampus peaks at CT0, whereas in the liver it peaks at CT12. Inactivated by phosphorylation at Ser-9 (By similarity). {ECO:0000250|UniProtKB:P49841, ECO:0000269|PubMed:22057101, ECO:0000269|PubMed:23395175}.; PTM: Mono-ADP-ribosylation by PARP10 negatively regulates kinase activity. {ECO:0000250|UniProtKB:P49841}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cell membrane {ECO:0000250}. Note=The phosphorylated form shows localization to cytoplasm and cell membrane. The MEMO1-RHOA-DIAPH1 signaling pathway controls localization of the phosphorylated form to the cell membrane (By similarity). {ECO:0000250}. SUBUNIT: Monomer. Interacts with DAB2IP (via C2 domain); the interaction stimulates GSK3B kinase activation. Interacts (via C2 domain) with PPP2CA (By similarity). Interacts with CABYR, MMP2, MUC1, NIN and PRUNE1 (By similarity). Interacts with AXIN1; the interaction mediates hyperphosphorylation of CTNNB1 leading to its ubiquitination and destruction. Interacts with and phosphorylates SNAI1. Interacts with DNM1L (via a C-terminal domain) (By similarity). Interacts with ARRB2 and DISC1. Found in a complex composed of MACF1, APC, AXIN1, CTNNB1 and GSK3B (By similarity). Interacts with SGK3. Interacts with the CLOCK-ARNTL/BMAL1 heterodimer (By similarity). Interacts with AXIN1 and ZBED3. Interacts with the ARNTL/BMAL1. The complex composed, at least, of APC, CTNNB1 and GSK3B interacts with JPT1; the interaction requires the inactive form of GSK3B (phosphorylated at 'Ser-9') (By similarity). Forms a complex composed of PRKAR2A or PRKAR2B, GSK3B and GSKIP through GSKIP interaction; facilitates PKA-induced phosphorylation and regulates GSK3B activity. Interacts with GSK3B; induces GSK3B-mediated phosphorylation of GSKIP (By similarity). Interacts with GID8 (By similarity). {ECO:0000250|UniProtKB:P49841, ECO:0000269|PubMed:16051150, ECO:0000269|PubMed:19141611, ECO:0000269|PubMed:19303846, ECO:0000269|PubMed:20049328}. +Q5RL51 GSTCD_MOUSE Glutathione S-transferase C-terminal domain-containing protein 634 70,618 Alternative sequence (5); Chain (1); Domain (1); Sequence conflict (2) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8NEC7}. +Q61543 GSLG1_MOUSE Golgi apparatus protein 1 (E-selectin ligand 1) (ESL-1) (Selel) (Golgi sialoglycoprotein MG-160) 1175 133,734 Chain (1); Compositional bias (3); Glycosylation (5); Modified residue (1); Repeat (16); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1142 1162 Helical. {ECO:0000255}. TOPO_DOM 28 1141 Extracellular. {ECO:0000255}.; TOPO_DOM 1163 1175 Cytoplasmic. {ECO:0000255}. FUNCTION: Binds fibroblast growth factor (By similarity). Binds E-selectin (cell-adhesion lectin on endothelial cells mediating the binding of neutrophils). {ECO:0000250}. PTM: Fucosylation is essential for binding to E-selectin.; PTM: Contains sialic acid residues. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9099943}; Single-pass type I membrane protein {ECO:0000269|PubMed:9099943}. Golgi apparatus membrane {ECO:0000269|PubMed:9099943}; Single-pass type I membrane protein {ECO:0000269|PubMed:9099943}. Note=Golgi and microvilli on the cell surface. TISSUE SPECIFICITY: Widely expressed; found in myeloid cells, fibroblasts, colon carcinoma, endothelioma, teratocarcinoma, lymphoma, myeloma. +Q61133 GSTT2_MOUSE Glutathione S-transferase theta-2 (EC 2.5.1.18) (GST class-theta-2) 244 27,634 Binding site (1); Chain (1); Domain (2); Region (2); Sequence conflict (4) FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. SUBUNIT: Homodimer. TISSUE SPECIFICITY: In liver, highest expression found in central vein limiting plate hepatocytes. Also expressed in interlobular bile duct epithelial cells. In lung, expressed in Clara cells and ciliated cells of the bronchiolar epithelium and in type II alveolar cells of the lung parenchyma. +P17809 GTR1_MOUSE Solute carrier family 2, facilitated glucose transporter member 1 (Glucose transporter type 1, erythrocyte/brain) (GLUT-1) (GT1) 492 53,985 Binding site (2); Chain (1); Glycosylation (1); Modified residue (4); Region (1); Sequence conflict (4); Topological domain (13); Transmembrane (12) TRANSMEM 12 33 Helical; Name=1. {ECO:0000250}.; TRANSMEM 67 87 Helical; Name=2. {ECO:0000250}.; TRANSMEM 91 112 Helical; Name=3. {ECO:0000250}.; TRANSMEM 121 144 Helical; Name=4. {ECO:0000250}.; TRANSMEM 156 176 Helical; Name=5. {ECO:0000250}.; TRANSMEM 186 206 Helical; Name=6. {ECO:0000250}.; TRANSMEM 272 293 Helical; Name=7. {ECO:0000250}.; TRANSMEM 307 328 Helical; Name=8. {ECO:0000250}.; TRANSMEM 335 355 Helical; Name=9. {ECO:0000250}.; TRANSMEM 366 388 Helical; Name=10. {ECO:0000250}.; TRANSMEM 402 422 Helical; Name=11. {ECO:0000250}.; TRANSMEM 430 450 Helical; Name=12. {ECO:0000250}. TOPO_DOM 1 11 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 34 66 Extracellular. {ECO:0000250}.; TOPO_DOM 88 90 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 113 120 Extracellular. {ECO:0000250}.; TOPO_DOM 145 155 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 177 185 Extracellular. {ECO:0000250}.; TOPO_DOM 207 271 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 294 306 Extracellular. {ECO:0000250}.; TOPO_DOM 329 334 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 356 365 Extracellular. {ECO:0000250}.; TOPO_DOM 389 401 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 423 429 Extracellular. {ECO:0000250}.; TOPO_DOM 451 492 Cytoplasmic. {ECO:0000250}. FUNCTION: Facilitative glucose transporter. This isoform may be responsible for constitutive or basal glucose uptake. Has a very broad substrate specificity; can transport a wide range of aldoses including both pentoses and hexoses. {ECO:0000269|PubMed:17320047}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17320047}; Multi-pass membrane protein {ECO:0000269|PubMed:17320047}. Melanosome {ECO:0000250}. Note=Localizes primarily at the cell surface. {ECO:0000250}. SUBUNIT: Found in a complex with ADD2, DMTN and SLC2A1. Interacts (via C-terminus cytoplasmic region) with DMTN isoform 2. Interacts with SNX27; the interaction is required when endocytosed to prevent degradation in lysosomes and promote recycling to the plasma membrane. Interacts with GIPC (via PDZ domain). Interacts with STOM. Interacts with SGTA (via Gln-rich region). {ECO:0000250|UniProtKB:P11166, ECO:0000250|UniProtKB:P11167}. +Q3U6U5 GTPB6_MOUSE Putative GTP-binding protein 6 514 56,475 Chain (1); Domain (1); Metal binding (2); Sequence conflict (3) +Q9CWD0 GTSFL_MOUSE Gametocyte-specific factor 1-like (Protein FAM112A) 151 17,282 Chain (1); Sequence conflict (1); Zinc finger (2) +Q9JIF3 GTR8_MOUSE Solute carrier family 2, facilitated glucose transporter member 8 (Glucose transporter type 8) (GLUT-8) (Glucose transporter type X1) 477 51,508 Binding site (1); Chain (1); Glycosylation (1); Motif (1); Mutagenesis (1); Region (1); Sequence conflict (4); Topological domain (13); Transmembrane (12) TRANSMEM 26 46 Helical; Name=1. {ECO:0000255}.; TRANSMEM 71 91 Helical; Name=2. {ECO:0000255}.; TRANSMEM 97 117 Helical; Name=3. {ECO:0000255}.; TRANSMEM 128 148 Helical; Name=4. {ECO:0000255}.; TRANSMEM 157 177 Helical; Name=5. {ECO:0000255}.; TRANSMEM 183 203 Helical; Name=6. {ECO:0000255}.; TRANSMEM 258 278 Helical; Name=7. {ECO:0000255}.; TRANSMEM 294 314 Helical; Name=8. {ECO:0000255}.; TRANSMEM 321 341 Helical; Name=9. {ECO:0000255}.; TRANSMEM 368 388 Helical; Name=10. {ECO:0000255}.; TRANSMEM 405 425 Helical; Name=11. {ECO:0000255}.; TRANSMEM 439 459 Helical; Name=12. {ECO:0000255}. TOPO_DOM 1 25 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 47 70 Extracellular. {ECO:0000255}.; TOPO_DOM 92 96 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 118 127 Extracellular. {ECO:0000255}.; TOPO_DOM 149 156 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 178 182 Extracellular. {ECO:0000255}.; TOPO_DOM 204 257 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 279 293 Extracellular. {ECO:0000255}.; TOPO_DOM 315 320 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 342 367 Extracellular. {ECO:0000255}.; TOPO_DOM 389 404 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 426 438 Extracellular. {ECO:0000255}.; TOPO_DOM 460 477 Cytoplasmic. {ECO:0000255}. FUNCTION: Insulin-regulated facilitative glucose transporter. Binds cytochalasin B in a glucose-inhibitable manner. Seems to be a dual-specific sugar transporter as it is inhibitable by fructose. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Principally intracellular. May move between intracellular vesicles and the plasma membrane. The dileucine internalization motif is critical for intracellular sequestration (By similarity). Insulin induces a change in the intracellular localization and gives rise to insertion in the plasma membrane. {ECO:0000250}. SUBUNIT: Interacts with AP2B1. {ECO:0000269|PubMed:16723738}. TISSUE SPECIFICITY: Highest level of expression in placenta and testis. Highly expressed in adult and pubertal testis, but not prepubertal testis. Lower levels of expression in brain, liver, heart, kidney, fat and skeletal muscle. +Q9WTP6 KAD2_MOUSE Adenylate kinase 2, mitochondrial (AK 2) (EC 2.7.4.3) (ATP-AMP transphosphorylase 2) (ATP:AMP phosphotransferase) (Adenylate monophosphate kinase) 239 26,469 Alternative sequence (1); Binding site (7); Chain (1); Disulfide bond (1); Modified residue (8); Nucleotide binding (4); Region (2); Sequence conflict (9) FUNCTION: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. Adenylate kinase activity is critical for regulation of the phosphate utilization and the AMP de novo biosynthesis pathways. Plays a key role in hematopoiesis. {ECO:0000255|HAMAP-Rule:MF_03168}. SUBCELLULAR LOCATION: Mitochondrion intermembrane space {ECO:0000255|HAMAP-Rule:MF_03168}. SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03168}. DOMAIN: Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis. {ECO:0000255|HAMAP-Rule:MF_03168}. TISSUE SPECIFICITY: Present in the inner ear. Not detected in the vestibule at any developmental stage. Present at high level in the cochlea uniquely in the stria vascularis at postnatal day 7 but not at birth. Present within the lumen of the stria vascularis capillaries. Not detected in the capillaries or vessels of the adjacent connective tissue (at protein level). {ECO:0000269|PubMed:19043416}. +Q9WTP7 KAD3_MOUSE GTP:AMP phosphotransferase AK3, mitochondrial (EC 2.7.4.10) (Adenylate kinase 3) (AK 3) (Adenylate kinase 3 alpha-like 1) 227 25,426 Binding site (7); Chain (1); Modified residue (15); Nucleotide binding (4); Region (2); Sequence conflict (2) FUNCTION: Involved in maintaining the homeostasis of cellular nucleotides by catalyzing the interconversion of nucleoside phosphates. Has GTP:AMP phosphotransferase and ITP:AMP phosphotransferase activities. {ECO:0000255|HAMAP-Rule:MF_03169}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-Rule:MF_03169}. SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03169}. DOMAIN: Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon GTP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent GTP hydrolysis. {ECO:0000255|HAMAP-Rule:MF_03169}. +Q3UMU9 HDGR2_MOUSE Hepatoma-derived growth factor-related protein 2 (HRP-2) 669 74,291 Alternative sequence (4); Chain (1); Coiled coil (1); Compositional bias (2); Cross-link (1); Domain (1); Modified residue (27) FUNCTION: Involved in cellular growth control, through the regulation of cyclin D1 expression (By similarity). Associates with chromatin. Isoform 1 and isoform 3 bind to condensed chromatin in mitotic cells. Isoform 4 binds to non-condensed chromatin in the presence of HDGF. {ECO:0000250|UniProtKB:Q7Z4V5, ECO:0000269|PubMed:22212508}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22212508}. Note=Isoform 4 displays a punctate pattern and colocalizes with N-terminally processed HDFG. SUBUNIT: Interacts with HDGF (PubMed:22212508). Isoform 4 selectively interacts with HDGF (N-terminally processed form). Interacts with trimethylated 'Lys-36' of histone H3 (H3K36me3). Interacts with trimethylated 'Lys-79' of histone H3 (H3K79me3), but has higher affinity for H3K36me3 (By similarity). Interacts with IWS1 (By similarity). {ECO:0000250|UniProtKB:Q7Z4V5, ECO:0000269|PubMed:22212508}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:22212508}. +Q8K4P8 HECW1_MOUSE E3 ubiquitin-protein ligase HECW1 (EC 2.3.2.26) (HECT, C2 and WW domain-containing protein 1) (HECT-type E3 ubiquitin transferase HECW1) (NEDD4-like E3 ubiquitin-protein ligase 1) (mNEDL1) 1604 179,467 Active site (1); Alternative sequence (3); Chain (1); Coiled coil (1); Compositional bias (2); Domain (4); Erroneous initiation (1); Modified residue (3); Sequence conflict (6) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent degradation of DVL1. {ECO:0000250, ECO:0000269|PubMed:14684739}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14684739}. SUBUNIT: Interacts with DVL1 and SSR3. {ECO:0000250}. TISSUE SPECIFICITY: Predominantly expressed in neurons of the spinal cord. +Q9WU63 HEBP2_MOUSE Heme-binding protein 2 (Protein SOUL) 205 23,063 Chain (1); Initiator methionine (1); Modified residue (2); Mutagenesis (1) FUNCTION: Can promote mitochondrial permeability transition and facilitate necrotic cell death under different types of stress conditions (By similarity). May have low affinity for heme (PubMed:15518569). {ECO:0000250|UniProtKB:Q9Y5Z4}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y5Z4}. Mitochondrion {ECO:0000250|UniProtKB:Q9Y5Z4}. Note=Mainly localized to the cytoplasm with a much lower abundance in the mitochondrion. {ECO:0000250|UniProtKB:Q9Y5Z4}. SUBUNIT: Monomer. Interacts with LRPPRC. May interact with BCL2L1; an interaction with BCL2L1 was observed using a peptide, but not with the full-length protein. The full-length protein would have to undergo a major conformation change for the interaction to occur. Interacts with PDCD6. {ECO:0000250|UniProtKB:Q9Y5Z4}. DOMAIN: Forms a distorted beta-barrel structure, with two helices that are packed against the outer surface of the barrel. {ECO:0000250|UniProtKB:Q9Y5Z4}. +Q2VPA6 HELQ_MOUSE Helicase POLQ-like (EC 3.6.4.12) (Mus308-like helicase) (POLQ-like helicase) 1069 119,098 Alternative sequence (4); Chain (1); Domain (2); Motif (1); Nucleotide binding (1); Sequence conflict (4) FUNCTION: Single-stranded DNA-dependent ATPase and 5' to 3' DNA helicase. Involved in the repair of DNA cross-links and double-strand break (DSB) resistance. Participates in FANCD2-mediated repair. Forms a complex with POLN polymerase that participates in homologous recombination (HR) repair and is essential for cellular protection against DNA cross-links. {ECO:0000250|UniProtKB:Q8TDG4}. SUBUNIT: Hexamer. Interacts with POLN. {ECO:0000250|UniProtKB:Q8TDG4}. +Q8VC19 HEM1_MOUSE 5-aminolevulinate synthase, nonspecific, mitochondrial (ALAS-H) (EC 2.3.1.37) (5-aminolevulinic acid synthase 1) (Delta-ALA synthase 1) (Delta-aminolevulinate synthase 1) 642 71,018 Active site (1); Binding site (9); Chain (1); Modified residue (1); Sequence conflict (6); Transit peptide (1) Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from glycine: step 1/1. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +Q8BJ66 KAZD1_MOUSE Kazal-type serine protease inhibitor domain-containing protein 1 (Bone and odontoblast-expressed protein 1) (Insulin-like growth factor-binding-related protein 10) (IGFBP-rP10) (IGFBP-related protein 10) (Insulin-like growth factor-binding-related protein 4) 313 34,272 Chain (1); Compositional bias (2); Disulfide bond (2); Domain (3); Glycosylation (3); Sequence conflict (1); Signal peptide (1) FUNCTION: Involved in the proliferation of osteoblasts during bone formation and bone regeneration. Promotes matrix assembly. {ECO:0000269|PubMed:15555553, ECO:0000269|PubMed:18757743}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:18757743}. TISSUE SPECIFICITY: Highly expressed in the spleen. Moderately expressed in the skin, lung and urinary bladder. Weakly expressed in the brain, tongue, esophagus, stomach, large intestine, liver and bone. Expressed in osteoblastic cells during bone regeneration. Expressed in secretory osteoblasts in the tooth. {ECO:0000269|PubMed:15261838, ECO:0000269|PubMed:15555553}. +Q69ZS8 KAZRN_MOUSE Kazrin 779 86,717 Alternative sequence (4); Chain (1); Coiled coil (1); Domain (3); Erroneous initiation (1); Modified residue (3); Sequence conflict (1) FUNCTION: Component of the cornified envelope of keratinocytes. May be involved in the interplay between adherens junctions and desmosomes. The function in the nucleus is not known. SUBCELLULAR LOCATION: Cell junction {ECO:0000269|PubMed:16086310}. Nucleus {ECO:0000269|PubMed:16086310}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16086310}. Note=In an antibody regognizing isoform 2 and isoform 3 has been used. {ECO:0000269|PubMed:16086310}. TISSUE SPECIFICITY: Expressed in skin interfollicular epidermis and hair follicles. Expressed in tongue epithelium basal suprabasal layers. {ECO:0000269|PubMed:15337775}. +O88986 KBL_MOUSE 2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial (AKB ligase) (EC 2.3.1.29) (Aminoacetone synthase) (Glycine acetyltransferase) 416 44,931 Binding site (3); Chain (1); Modified residue (9); Region (3); Transit peptide (1) Amino-acid degradation; L-threonine degradation via oxydo-reductase pathway; glycine from L-threonine: step 2/2. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Nucleus {ECO:0000250}. Note=Translocates to the nucleus upon cold and osmotic stress. {ECO:0000250}. +Q6ZPU9 KBP_MOUSE KIF1-binding protein 617 71,052 Alternative sequence (3); Chain (1); Erroneous initiation (1); Modified residue (1); Sequence caution (1); Sequence conflict (2) FUNCTION: Required for neuronal development and differentiation. Required for organization of axonal microtubules, and axonal outgrowth and maintenance during peripheral and central nervous system development. {ECO:0000269|PubMed:20621975}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. SUBUNIT: Interacts with KIF1B. Interacts with STMN2. {ECO:0000250}. TISSUE SPECIFICITY: In th embryo it is expressed in cortical neurons; expression increases during neuronal development. {ECO:0000269|PubMed:20621975}. +Q8CEC5 KBRS1_MOUSE NF-kappa-B inhibitor-interacting Ras-like protein 1 (I-kappa-B-interacting Ras-like protein 1) (Kappa B-Ras protein 1) (KappaB-Ras1) 192 21,662 Chain (1); Motif (1); Nucleotide binding (3); Region (1); Sequence conflict (1) FUNCTION: Atypical Ras-like protein that acts as a potent regulator of NF-kappa-B activity by preventing the degradation of NF-kappa-B inhibitor beta (NFKBIB) by most signals, explaining why NFKBIB is more resistant to degradation. May act by blocking phosphorylation of NFKBIB and mediating cytoplasmic retention of p65/RELA NF-kappa-B subunit. It is unclear whether it acts as a GTPase. Both GTP- and GDP-bound forms block phosphorylation of NFKBIB (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with both NF-kappa-B inhibitor alpha (NFKBIA) and beta (NFKBIB) in vitro. However, it probably only interacts with NFKBIB in vivo. Forms a complex with NFKBIB and NF-kappa-B heterodimer (p50/NFKB1 and p65/RELA). Also interacts with c-Rel (REL) (By similarity). {ECO:0000250}. DOMAIN: In contrast to other members of the Ras family, the members of the KappaB-Ras subfamily do not contain the conserved Gly and Gln residues in positions 13 and 65, which are replaced by Leu residues, and are therefore similar to the constitutively active forms of oncogenic forms of Ras. This suggests that members of this family are clearly different from other small GTPases proteins. +Q8R179 KBTB4_MOUSE Kelch repeat and BTB domain-containing protein 4 (BTB and kelch domain-containing protein 4) 534 59,857 Alternative sequence (1); Chain (1); Domain (2); Repeat (3) +Q3UQV5 KBTB8_MOUSE Kelch repeat and BTB domain-containing protein 8 599 68,660 Alternative sequence (1); Chain (1); Domain (2); Erroneous initiation (1); Repeat (5); Sequence conflict (1) FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a regulator of neural crest specification. The BCR(KBTBD8) complex acts by mediating monoubiquitination of NOLC1 and TCOF1: monoubiquitination promotes the formation of a NOLC1-TCOF1 complex that acts as a platform to connect RNA polymerase I with enzymes responsible for ribosomal processing and modification, leading to remodel the translational program of differentiating cells in favor of neural crest specification. {ECO:0000250|UniProtKB:Q8NFY9}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q8NFY9}. Golgi apparatus {ECO:0000250|UniProtKB:Q8NFY9}. Note=Translocates to the spindle apparatus during mitosis. {ECO:0000250|UniProtKB:Q8NFY9}. SUBUNIT: Component of the BCR(KBTBD8) E3 ubiquitin ligase complex, at least composed of CUL3, KBTBD8 and RBX1. {ECO:0000250|UniProtKB:Q8NFY9}. +Q8BK63 KC1A_MOUSE Casein kinase I isoform alpha (CKI-alpha) (EC 2.7.11.1) (CK1) 337 38,915 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Domain (1); Initiator methionine (1); Modified residue (3); Nucleotide binding (1); Sequence conflict (2) FUNCTION: Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. Can phosphorylate a large number of proteins. Participates in Wnt signaling. Phosphorylates CTNNB1 at 'Ser-45'. May phosphorylate PER1 and PER2. May play a role in segregating chromosomes during mitosis. May play a role in keratin cytoskeleton disassembly and thereby, it may regulate epithelial cell migration (By similarity). {ECO:0000250|UniProtKB:P48729, ECO:0000269|PubMed:21930935}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P48729}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P48729}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:P48729}. Nucleus speckle {ECO:0000250|UniProtKB:P48729}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:25644602}. Note=Localizes to the centrosome in interphase cells, and to kinetochore fibers during mitosis. Also recruited to the keratin cytoskeleton. {ECO:0000250|UniProtKB:P48729}. SUBUNIT: Monomer. Interacts with the Axin complex. Interacts with TUT1, leading to TUT1 phosphorylation. Interacts with FAM83H; recruits CSNK1A1 to keratin filaments. {ECO:0000250|UniProtKB:P48729}. +Q9DC28 KC1D_MOUSE Casein kinase I isoform delta (CKI-delta) (CKId) (EC 2.7.11.1) (Tau-protein kinase CSNK1D) (EC 2.7.11.26) 415 47,316 Active site (1); Alternative sequence (1); Beta strand (8); Binding site (1); Chain (1); Domain (1); Helix (13); Modified residue (10); Mutagenesis (1); Nucleotide binding (1); Region (2); Sequence conflict (1); Turn (7) FUNCTION: Essential serine/threonine-protein kinase that regulates diverse cellular growth and survival processes including Wnt signaling, DNA repair and circadian rhythms. It can phosphorylate a large number of proteins. Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. Phosphorylates connexin-43/GJA1, MAP1A, SNAPIN, MAPT/TAU, TOP2A, DCK, HIF1A, EIF6, p53/TP53, DVL2, DVL3, ESR1, AIB1/NCOA3, DNMT1, PKD2, YAP1, PER1 and PER2. Central component of the circadian clock. In balance with PP1, determines the circadian period length through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. Controls PER1 and PER2 nuclear transport and degradation. YAP1 phosphorylation promotes its SCF(beta-TRCP) E3 ubiquitin ligase-mediated ubiquitination and subsequent degradation. DNMT1 phosphorylation reduces its DNA-binding activity. Phosphorylation of ESR1 and AIB1/NCOA3 stimulates their activity and coactivation. Phosphorylation of DVL2 and DVL3 regulates WNT3A signaling pathway that controls neurite outgrowth. EIF6 phosphorylation promotes its nuclear export. Triggers down-regulation of dopamine receptors in the forebrain. Activates DCK in vitro by phosphorylation. TOP2A phosphorylation favors DNA cleavable complex formation. May regulate the formation of the mitotic spindle apparatus in extravillous trophoblast. Modulates connexin-43/GJA1 gap junction assembly by phosphorylation. Probably involved in lymphocyte physiology. Regulates fast synaptic transmission mediated by glutamate. {ECO:0000269|PubMed:10848614, ECO:0000269|PubMed:16014721, ECO:0000269|PubMed:17101137, ECO:0000269|PubMed:19414593, ECO:0000269|PubMed:19948962, ECO:0000269|PubMed:20145109, ECO:0000269|PubMed:20192920, ECO:0000269|PubMed:20421981, ECO:0000269|PubMed:21930935}. PTM: Autophosphorylated on serine and threonine residues; this autophosphorylation represses activity. Reactivated by phosphatase-mediated dephosphorylation. May be dephosphorylated by PP1. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000269|PubMed:10848614, ECO:0000269|PubMed:17101137, ECO:0000269|PubMed:19414593}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Golgi apparatus {ECO:0000250}. Note=Localized at mitotic spindle microtubules, and at the centrosomes and interphase in interphase cells. Recruited to the spindle apparatus and the centrosomes in response to DNA-damage. Correct subcellular localization requires kinase activity (By similarity). {ECO:0000250}. SUBUNIT: Binds to MAP1A. Monomer. Component of the circadian core oscillator, which includes the CRY proteins, CLOCK, or NPAS2, ARNTL/BMAL1 or ARNTL2/BMAL2, CSNK1D and/or CSNK1E, TIMELESS and the PER proteins. Interacts with MAPT/TAU, DBNDD2, AIB1/NCOA3 and ESR1. AKAP9/AKAP450 binding promotes centrosomal subcellular location. Binds to tubulins in mitotic cells upon DNA damage. Binds to SNAPIN and DNMT1. {ECO:0000269|PubMed:17101137, ECO:0000269|PubMed:20192920}. TISSUE SPECIFICITY: Expressed ubiquitously. However, kinase activity is not uniform, with highest kinase activity in splenocytes. {ECO:0000269|PubMed:12924632}. +Q9JMK2 KC1E_MOUSE Casein kinase I isoform epsilon (CKI-epsilon) (CKIe) (EC 2.7.11.1) 416 47,322 Active site (1); Binding site (1); Chain (1); Domain (1); Modified residue (8); Mutagenesis (3); Nucleotide binding (1); Sequence conflict (3) FUNCTION: Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. Can phosphorylate a large number of proteins. Participates in Wnt signaling. Phosphorylates DVL1. Central component of the circadian clock. In balance with PP1, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. Controls PER1 and PER2 nuclear transport and degradation. Inhibits cytokine-induced granuloytic differentiation. {ECO:0000269|PubMed:10848614, ECO:0000269|PubMed:14701732, ECO:0000269|PubMed:18400165, ECO:0000269|PubMed:19414593, ECO:0000269|PubMed:21930935}. PTM: Autophosphorylated. Partially dephosphorylated by PPP5C. May be dephosphorylated by PP1. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000269|PubMed:19414593}. SUBUNIT: Monomer. Component of the circadian core oscillator, which includes the CRY proteins, CLOCK, or NPAS2, ARTNL/BMAL1 or ARTNL2/BMAL2, CSNK1D and/or CSNK1E, TIMELESS and the PER proteins. Interacts with ANKRD6, DBNDD2, LRP5, LRP6 and SOCS3. Interacts with SNAI1 (via zinc fingers). Interacts with DDX3X; the interaction greatly improves CSNK1E affinity for ATP and enhances DVL2 phosphorylation (By similarity). {ECO:0000250|UniProtKB:P49674, ECO:0000269|PubMed:12183362}. TISSUE SPECIFICITY: Expressed in all tissues examined, including brain, heart, lung, liver, pancreas, kidney, placenta and skeletal muscle. Expressed in monocytes and lymphocytes but not in granulocytes. {ECO:0000269|PubMed:16790549}. +Q8BTH8 KC1G1_MOUSE Casein kinase I isoform gamma-1 (CKI-gamma 1) (EC 2.7.11.1) 459 52,744 Active site (1); Binding site (1); Chain (1); Domain (1); Modified residue (1); Nucleotide binding (1); Sequence conflict (1) FUNCTION: Serine/threonine-protein kinase. Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. It can phosphorylate a large number of proteins. Participates in Wnt signaling. Phosphorylates CLSPN (By similarity). Regulates fast synaptic transmission mediated by glutamate. {ECO:0000250, ECO:0000269|PubMed:16014721}. PTM: Autophosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in both the striatum and the neocortex. {ECO:0000269|PubMed:16014721}. +Q8BVP5 KC1G2_MOUSE Casein kinase I isoform gamma-2 (CKI-gamma 2) (EC 2.7.11.1) 415 47,582 Active site (1); Binding site (1); Chain (1); Domain (1); Nucleotide binding (1) FUNCTION: Serine/threonine-protein kinase. Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. It can phosphorylate a large number of proteins. Participates in Wnt signaling (By similarity). Phosphorylates COL4A3BP/CERT, MTA1 and SMAD3. Involved in brain development and vesicular trafficking and neurotransmitter releasing from small synaptic vesicles. Regulates fast synaptic transmission mediated by glutamate. SMAD3 phosphorylation promotes its ligand-dependent ubiquitination and subsequent proteasome degradation, thus inhibiting SMAD3-mediated TGF-beta responses. Hyperphosphorylation of the serine-repeat motif of COL4A3BP/CERT leads to its inactivation by dissociation from the Golgi complex, thus down-regulating ER-to-Golgi transport of ceramide and sphingomyelin synthesis. Triggers PER1 proteasomal degradation probably through phosphorylation. {ECO:0000250, ECO:0000269|PubMed:15077195, ECO:0000269|PubMed:16014721}. PTM: Autophosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Monomer. Interacts with MTA1 (short isoform) in the cytoplasm. Interacts with SMAD3. {ECO:0000269|PubMed:15077195}. TISSUE SPECIFICITY: Expressed in both the striatum and the neocortex. {ECO:0000269|PubMed:16014721}. +Q8C4X2 KC1G3_MOUSE Casein kinase I isoform gamma-3 (CKI-gamma 3) (EC 2.7.11.1) 424 48,938 Active site (1); Binding site (3); Chain (1); Compositional bias (1); Domain (1); Modified residue (2); Nucleotide binding (1); Sequence conflict (4) FUNCTION: Serine/threonine-protein kinase. Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. It can phosphorylate a large number of proteins. Participates in Wnt signaling (By similarity). Regulates fast synaptic transmission mediated by glutamate. {ECO:0000250, ECO:0000269|PubMed:16014721}. PTM: Autophosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in both the striatum and the neocortex. {ECO:0000269|PubMed:16014721}. +B2RQA1 KCA10_MOUSE Potassium voltage-gated channel subfamily A member 10 (Voltage-gated potassium channel subunit Kv1.8) 511 57,968 Chain (1); Lipidation (1); Motif (1); Sequence conflict (2); Transmembrane (6) TRANSMEM 218 238 Helical; Name=Segment S1. {ECO:0000255}.; TRANSMEM 271 292 Helical; Name=Segment S2. {ECO:0000255}.; TRANSMEM 303 323 Helical; Name=Segment S3. {ECO:0000255}.; TRANSMEM 339 358 Helical; Voltage-sensor; Name=Segment S4. {ECO:0000255}.; TRANSMEM 375 395 Helical; Name=Segment S5. {ECO:0000255}.; TRANSMEM 436 456 Helical; Name=Segment S6. {ECO:0000255}. FUNCTION: Mediates voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient. The channel activity is up-regulated by cAMP. {ECO:0000250|UniProtKB:Q16322}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Homotetramer. Interacts with KCN4B/POMP. Interaction with KCN4B/POMP is necessary for the modulation of channel activity by cAMP. {ECO:0000250|UniProtKB:Q16322}. DOMAIN: The N-terminus may be important in determining the rate of inactivation of the channel while the tail may play a role in modulation of channel activity and/or targeting of the channel to specific subcellular compartments. {ECO:0000250|UniProtKB:Q16322}.; DOMAIN: The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position. {ECO:0000250|UniProtKB:P63142}. TISSUE SPECIFICITY: Expressed strongly in the inner ear and weakly in skeletal muscle. Not detected in other tissues. {ECO:0000269|PubMed:23528307}. +Q91YS8 KCC1A_MOUSE Calcium/calmodulin-dependent protein kinase type 1 (EC 2.7.11.17) (CaM kinase I) (CaM-KI) (CaM kinase I alpha) (CaMKI-alpha) 374 41,624 Active site (1); Binding site (1); Chain (1); Cross-link (1); Domain (1); Modified residue (1); Motif (1); Nucleotide binding (1); Region (2) FUNCTION: Calcium/calmodulin-dependent protein kinase that operates in the calcium-triggered CaMKK-CaMK1 signaling cascade and, upon calcium influx, regulates transcription activators activity, cell cycle, hormone production, cell differentiation, actin filament organization and neurite outgrowth. Recognizes the substrate consensus sequence [MVLIF]-x-R-x(2)-[ST]-x(3)-[MVLIF]. Regulates axonal extension and growth cone motility in hippocampal and cerebellar nerve cells. Upon NMDA receptor-mediated Ca(2+) elevation, promotes dendritic growth in hippocampal neurons and is essential in synapses for full long-term potentiation (LTP) and ERK2-dependent translational activation. Downstream of NMDA receptors, promotes the formation of spines and synapses in hippocampal neurons by phosphorylating ARHGEF7/BETAPIX on 'Ser-673', which results in the enhancement of ARHGEF7 activity and activation of RAC1. Promotes neuronal differentiation and neurite outgrowth by activation and phosphorylation of MARK2 on 'Ser-91', 'Ser-92', 'Ser-93' and 'Ser-294'. Promotes nuclear export of HDAC5 and binding to 14-3-3 by phosphorylation of 'Ser-259' and 'Ser-498' in the regulation of muscle cell differentiation. Regulates NUMB-mediated endocytosis by phosphorylation of NUMB on 'Ser-276' and 'Ser-295'. Involved in the regulation of basal and estrogen-stimulated migration of medulloblastoma cells through ARHGEF7/BETAPIX phosphorylation. Is required for proper activation of cyclin-D1/CDK4 complex during G1 progression in diploid fibroblasts. Plays a role in K(+) and ANG2-mediated regulation of the aldosterone synthase (CYP11B2) to produce aldosterone in the adrenal cortex. Phosphorylates EIF4G3/eIF4GII. In vitro phosphorylates CREB1, ATF1, CFTR, MYL9 and SYN1/synapsin I (By similarity). {ECO:0000250, ECO:0000269|PubMed:15150258}. PTM: Phosphorylated by CaMKK1 and CaMKK2 on Thr-177.; PTM: Polybiquitinated by the E3 ubiquitin-protein ligase complex SCF(FBXL12), leading to proteasomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Predominantly cytoplasmic. {ECO:0000250}. SUBUNIT: Monomer. Interacts with XPO1 (By similarity). {ECO:0000250}. DOMAIN: The autoinhibitory domain overlaps with the calmodulin binding region and interacts in the inactive folded state with the catalytic domain as a pseudosubstrate. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. +Q91VB2 KCC1G_MOUSE Calcium/calmodulin-dependent protein kinase type 1G (EC 2.7.11.17) (CaM kinase I gamma) (CaM kinase IG) (CaM-KI gamma) (CaMKI gamma) (CaMKIG) (CaMK-like CREB kinase III) (CLICK III) 477 53,296 Active site (1); Binding site (1); Chain (1); Domain (1); Mutagenesis (1); Nucleotide binding (1); Region (2) FUNCTION: Calcium/calmodulin-dependent protein kinase belonging to a proposed calcium-triggered signaling cascade. In vitro phosphorylates transcription factor CREB1. PTM: May be prenylated on Cys-474. {ECO:0000269|PubMed:12637513}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12637513}. Golgi apparatus membrane {ECO:0000269|PubMed:12637513}; Peripheral membrane protein {ECO:0000269|PubMed:12637513}. Cell membrane {ECO:0000269|PubMed:12637513}; Peripheral membrane protein {ECO:0000269|PubMed:12637513}. DOMAIN: The autoinhibitory domain overlaps with the calmodulin binding region and interacts in the inactive folded state with the catalytic domain as a pseudosubstrate. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in brain, in neuronal cell bodies of the central nucleus of amygdala and ventromedial hypothalamic nucleus. Also detected in heart, testis, and kidney. {ECO:0000269|PubMed:12637513}. +Q6PHZ2 KCC2D_MOUSE Calcium/calmodulin-dependent protein kinase type II subunit delta (CaM kinase II subunit delta) (CaMK-II subunit delta) (EC 2.7.11.17) 499 56,369 Active site (1); Alternative sequence (4); Beta strand (7); Binding site (1); Chain (1); Domain (1); Erroneous initiation (1); Helix (15); Initiator methionine (1); Modified residue (15); Nucleotide binding (1); Region (2); Sequence conflict (4); Turn (2) FUNCTION: Calcium/calmodulin-dependent protein kinase involved in the regulation of Ca(2+) homeostatis and excitation-contraction coupling (ECC) in heart by targeting ion channels, transporters and accessory proteins involved in Ca(2+) influx into the myocyte, Ca(2+) release from the sarcoplasmic reticulum (SR), SR Ca(2+) uptake and Na(+) and K(+) channel transport. Targets also transcription factors and signaling molecules to regulate heart function. In its activated form, is involved in the pathogenesis of dilated cardiomyopathy and heart failure. Contributes to cardiac decompensation and heart failure by regulating SR Ca(2+) release via direct phosphorylation of RYR2 Ca(2+) channel on 'Ser-2808'. In the nucleus, phosphorylates the MEF2 repressor HDAC4, promoting its nuclear export and binding to 14-3-3 protein, and expression of MEF2 and genes involved in the hypertrophic program. Is essential for left ventricular remodeling responses to myocardial infarction. In pathological myocardial remodeling acts downstream of the beta adrenergic receptor signaling cascade to regulate key proteins involved in ECC. Regulates Ca(2+) influx to myocytes by binding and phosphorylating the L-type Ca(2+) channel subunit beta-2 CACNB2. In addition to Ca(2+) channels, can target and regulate the cardiac sarcolemmal Na(+) channel Nav1.5/SCN5A and the K+ channel Kv4.3/KCND3, which contribute to arrhythmogenesis in heart failure. Phosphorylates phospholamban (PLN/PLB), an endogenous inhibitor of SERCA2A/ATP2A2, contributing to the enhancement of SR Ca(2+) uptake that may be important in frequency-dependent acceleration of relaxation (FDAR) and maintenance of contractile function during acidosis. May participate in the modulation of skeletal muscle function in response to exercise, by regulating SR Ca(2+) transport through phosphorylation of PLN/PLB and triadin, a ryanodine receptor-coupling factor. {ECO:0000269|PubMed:12676814, ECO:0000269|PubMed:15456698, ECO:0000269|PubMed:15793582, ECO:0000269|PubMed:17124532, ECO:0000269|PubMed:19179290, ECO:0000269|PubMed:19381018, ECO:0000269|PubMed:20194790}. PTM: Autophosphorylation of Thr-287 following activation by Ca(2+)/calmodulin. Phosphorylation of Thr-287 locks the kinase into an activated state (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Sarcoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. SUBUNIT: CAMK2 is composed of 4 different chains: alpha (CAMK2A), beta (CAMK2B), gamma (CAMK2G), and delta (CAMK2D). The different isoforms assemble into homo- or heteromultimeric holoenzymes composed of 12 subunits with two hexameric rings stacked one on top of the other. Interacts with RRAD (By similarity). Interacts with CACNB2. {ECO:0000250, ECO:0000269|PubMed:20194790}. DOMAIN: The CAMK2 protein kinases contain a unique C-terminal subunit association domain responsible for oligomerization. TISSUE SPECIFICITY: Expressed in cardiac muscle and skeletal muscle. Isoform Delta 2, isoform Delta 6, isoform Delta 6 and isoform Delta 10 are expressed in cardiac muscle. Isoform Delta 2 is expressed in skeletal muscle. {ECO:0000269|PubMed:10967556}. +Q6WVG3 KCD12_MOUSE BTB/POZ domain-containing protein KCTD12 (Pfetin) (Predominantly fetal expressed T1 domain) 327 35,892 Chain (1); Initiator methionine (1); Modified residue (7); Sequence conflict (2) FUNCTION: Auxiliary subunit of GABA-B receptors that determine the pharmacology and kinetics of the receptor response. Increases agonist potency and markedly alter the G-protein signaling of the receptors by accelerating onset and promoting desensitization. {ECO:0000269|PubMed:20400944}. SUBCELLULAR LOCATION: Cell junction, synapse, presynaptic cell membrane {ECO:0000269|PubMed:20400944}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000269|PubMed:20400944}. Note=Colocalizes with GABRB1. SUBUNIT: Interacts as a tetramer with GABRB1 and GABRB2. {ECO:0000269|PubMed:20400944}. TISSUE SPECIFICITY: Expressed in the brain, mainly in the hippocampus and cerebellum. {ECO:0000269|PubMed:20400944}. +Q08460 KCMA1_MOUSE Calcium-activated potassium channel subunit alpha-1 (BK channel) (BKCA alpha) (Calcium-activated potassium channel, subfamily M subunit alpha-1) (K(VCA)alpha) (KCa1.1) (Maxi K channel) (MaxiK) (Slo-alpha) (Slo1) (mSlo1) (Slowpoke homolog) (Slo homolog) (mSlo) 1209 134,396 Alternative sequence (7); Chain (1); Compositional bias (3); Domain (1); Erroneous initiation (1); Intramembrane (1); Lipidation (3); Metal binding (7); Modified residue (11); Motif (2); Mutagenesis (15); Region (5); Topological domain (9); Transmembrane (7) INTRAMEM 336 358 Pore-forming; Name=P region. {ECO:0000255}. TRANSMEM 87 107 Helical; Name=Segment S0. {ECO:0000255}.; TRANSMEM 179 199 Helical; Name=Segment S1. {ECO:0000255}.; TRANSMEM 215 235 Helical; Name=Segment S2. {ECO:0000255}.; TRANSMEM 240 260 Helical; Name=Segment S3. {ECO:0000255}.; TRANSMEM 265 285 Helical; Voltage-sensor; Name=Segment S4. {ECO:0000255}.; TRANSMEM 301 321 Helical; Name=Segment S5. {ECO:0000255}.; TRANSMEM 368 388 Helical; Name=Segment S6. {ECO:0000255}. TOPO_DOM 1 86 Extracellular. {ECO:0000255}.; TOPO_DOM 108 178 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 200 214 Extracellular. {ECO:0000255}.; TOPO_DOM 236 239 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 261 264 Extracellular. {ECO:0000255}.; TOPO_DOM 286 300 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 322 335 Extracellular. {ECO:0000255}.; TOPO_DOM 359 367 Extracellular. {ECO:0000255}.; TOPO_DOM 389 1209 Cytoplasmic. {ECO:0000255}. FUNCTION: Potassium channel activated by both membrane depolarization or increase in cytosolic Ca(2+) that mediates export of K(+). It is also activated by the concentration of cytosolic Mg(2+). Its activation dampens the excitatory events that elevate the cytosolic Ca(2+) concentration and/or depolarize the cell membrane. It therefore contributes to repolarization of the membrane potential. Plays a key role in controlling excitability in a number of systems, such as regulation of the contraction of smooth muscle, the tuning of hair cells in the cochlea, regulation of transmitter release, and innate immunity. In smooth muscles, its activation by high level of Ca(2+), caused by ryanodine receptors in the sarcoplasmic reticulum, regulates the membrane potential. In cochlea cells, its number and kinetic properties partly determine the characteristic frequency of each hair cell and thereby helps to establish a tonotopic map. Kinetics of KCNMA1 channels are determined by alternative splicing, phosphorylation status and its combination with modulating beta subunits. Highly sensitive to both iberiotoxin (IbTx) and charybdotoxin (CTX). {ECO:0000269|PubMed:7687074}. PTM: Phosphorylated (Probable). Phosphorylation by kinases such as PKA and/or PKG. In smooth muscles, phosphorylation affects its activity. {ECO:0000305}.; PTM: Palmitoylation by ZDHHC22 and ZDHHC23 within the intracellular linker between the S0 and S1 transmembrane domains regulates localization to the plasma membrane. Depalmitoylated by LYPLA1 and LYPLAL1, leading to retard exit from the trans-Golgi network (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Homotetramer; which constitutes the calcium-activated potassium channel. Interacts with beta subunits KCNMB1, KCNMB2, KCNMB3 and KCNMB4. Interacts with gamma subunits LRRC26, LRRC38, LRRC52 and LRRC55. Beta and gamma subunits are accessory, and modulate its activity (By similarity). Interacts with RAB11B. {ECO:0000250, ECO:0000269|PubMed:10804197, ECO:0000269|PubMed:22935415}. DOMAIN: The S0 segment is essential for the modulation by the accessory beta subunits KCNMB1, KCNMB2, KCNMB3 and KCNMB4.; DOMAIN: The S4 segment, which is characterized by a series of positively charged amino acids at every third position, is part of the voltage-sensor.; DOMAIN: The pore-forming domain (also referred as P region) is imbedded into the membrane, and forms the selectivity filter of the pore. It contains the signature sequence of potassium channels that displays selectivity to potassium.; DOMAIN: The RCK N-terminal domain mediates the homotetramerization, thereby promoting the assembly of monomers into functional potassium channel. It includes binding sites for Ca(2+) and Mg(2+).; DOMAIN: The calcium bowl constitutes one of the Ca(2+) sensors and probably acts as a Ca(2+)-binding site. There are however other Ca(2+) sensors regions required for activation of the channel.; DOMAIN: The heme-binding motif mediates inhibition of channel activation by heme. Carbon monoxide-bound heme leads to increased channel activation (By similarity). {ECO:0000250}. +Q9CZM9 KCMB2_MOUSE Calcium-activated potassium channel subunit beta-2 (BK channel subunit beta-2) (BKbeta2) (Calcium-activated potassium channel, subfamily M subunit beta-2) (Charybdotoxin receptor subunit beta-2) (K(VCA)beta-2) (Maxi K channel subunit beta-2) (Slo-beta-2) 235 27,120 Chain (1); Glycosylation (3); Region (1); Topological domain (3); Transmembrane (2) TRANSMEM 47 67 Helical; Name=1. {ECO:0000255}.; TRANSMEM 195 215 Helical; Name=2. {ECO:0000255}. TOPO_DOM 1 46 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 68 194 Extracellular. {ECO:0000255}.; TOPO_DOM 216 235 Cytoplasmic. {ECO:0000255}. FUNCTION: Regulatory subunit of the calcium activated potassium KCNMA1 (maxiK) channel. Modulates the calcium sensitivity and gating kinetics of KCNMA1, thereby contributing to KCNMA1 channel diversity. Acts as a negative regulator that confers rapid and complete inactivation of KCNMA1 channel complex (By similarity). {ECO:0000250}. PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with KCNMA1 tetramer. There are probably 4 molecules of KCMNB2 per KCNMA1 tetramer (By similarity). {ECO:0000250}. DOMAIN: The ball and chain domain mediates the inactivation of KCNMA1. It occludes the conduction pathway of KCNMA1 channels, and comprises the pore-blocking ball domain (residues 1-17) and the chain domain (residues 20-45) linking it to the transmembrane segment. The ball domain is made up of a flexible N-terminus anchored at a well ordered loop-helix motif. The chain domain consists of a 4-turn helix with an unfolded linker at its C-terminus (By similarity). {ECO:0000250}. +Q80UY2 KCMF1_MOUSE E3 ubiquitin-protein ligase KCMF1 (EC 2.3.2.27) (Differentially expressed in branching tubulogenesis 91) (Debt-91) (RING-type E3 ubiquitin transferase KCMF1) 381 41,791 Alternative sequence (1); Chain (1); Coiled coil (1); Compositional bias (2); Initiator methionine (1); Modified residue (7); Zinc finger (2) FUNCTION: Has intrinsic E3 ubiquitin ligase activity and promotes ubiquitination. {ECO:0000250}. TISSUE SPECIFICITY: Testis, liver, kidney, heart and skeletal muscle. {ECO:0000269|PubMed:12810064}. +Q80T19 HEPC2_MOUSE Hepcidin-2 83 9,410 Disulfide bond (4); Erroneous initiation (2); Peptide (1); Propeptide (1); Signal peptide (1) FUNCTION: Seems to act as a signaling molecule involved in the maintenance of iron homeostasis. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Highly expressed in the liver and to a much lesser extent in the heart. Also expressed in pancreas. {ECO:0000269|PubMed:12729891}. +P60894 GPR85_MOUSE Probable G-protein coupled receptor 85 (Super conserved receptor expressed in brain 2) 370 41,995 Chain (1); Disulfide bond (1); Glycosylation (3); Topological domain (8); Transmembrane (7) TRANSMEM 26 46 Helical; Name=1. {ECO:0000255}.; TRANSMEM 58 78 Helical; Name=2. {ECO:0000255}.; TRANSMEM 97 117 Helical; Name=3. {ECO:0000255}.; TRANSMEM 138 158 Helical; Name=4. {ECO:0000255}.; TRANSMEM 189 209 Helical; Name=5. {ECO:0000255}.; TRANSMEM 287 307 Helical; Name=6. {ECO:0000255}.; TRANSMEM 314 334 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 25 Extracellular. {ECO:0000255}.; TOPO_DOM 47 57 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 79 96 Extracellular. {ECO:0000255}.; TOPO_DOM 118 137 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 159 188 Extracellular. {ECO:0000255}.; TOPO_DOM 210 286 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 308 313 Extracellular. {ECO:0000255}.; TOPO_DOM 335 370 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan receptor. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P60893}. SUBUNIT: Interacts with DLG4 AND DLG3. {ECO:0000250|UniProtKB:P60893}. TISSUE SPECIFICITY: Exclusively expressed in brain. {ECO:0000269|PubMed:10978537}. +Q8BIY1 GPTC3_MOUSE G patch domain-containing protein 3 525 59,180 Chain (1); Compositional bias (1); Domain (1) FUNCTION: Involved in transcriptional regulation. It is able to activate transcription from CXCR4 promoter and therefore it might control neural crest cell migration involved in ocular and craniofacial development. Is a negative regulator of immune antiviral response, acting via down-regulation of RIG-I-like receptors signaling and inhibition of type I interferon production. The control mechanism involves interaction with mitochondrial MAVS and inhibition of MAVS assembly with downstream proteins implicated in antiviral response, such as TBK1 and TRAF6. {ECO:0000250|UniProtKB:Q96I76}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96I76}. Cytoplasm {ECO:0000250|UniProtKB:Q96I76}. SUBUNIT: Interacts with mitochondrial MAVS; the interaction is markedly increased upon viral infection. {ECO:0000250|UniProtKB:Q96I76}. +Q8VDU0 GPSM2_MOUSE G-protein-signaling modulator 2 (Pins homolog) 679 75,591 Beta strand (1); Binding site (4); Chain (1); Domain (4); Erroneous initiation (2); Helix (18); Modified residue (5); Mutagenesis (9); Region (1); Repeat (8) FUNCTION: Plays an important role in mitotic spindle pole organization via its interaction with NUMA1 (PubMed:21816348). Required for cortical dynein-dynactin complex recruitment during metaphase (By similarity). Plays a role in metaphase spindle orientation (By similarity). Plays an important role in asymmetric cell divisions (PubMed:12571286, PubMed:21816348). Has guanine nucleotide dissociation inhibitor (GDI) activity towards G(i) alpha proteins, such as GNAI1 and GNAI3, and thereby regulates their activity (PubMed:22952234). {ECO:0000250|UniProtKB:P81274, ECO:0000269|PubMed:12571286, ECO:0000269|PubMed:21816348, ECO:0000269|PubMed:22952234}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P81274}. Cytoplasm, cell cortex {ECO:0000269|PubMed:26766442}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:P81274}. Lateral cell membrane {ECO:0000269|PubMed:26766442}. Note=Localizes in the cytoplasm during interphase and at cell cortex during metaphase. Colocalizes with NUMA1 to mitotic spindle poles. Localized at the central and lateral cell cortex regions in a RanGTP-dependent manner (By similarity). In horizontally retinal progenitor dividing cells, localized to the lateral cortical region (PubMed:26766442). In vertically retinal progenitor dividing cells, localized at the polar cortical region (PubMed:26766442). {ECO:0000250|UniProtKB:P81274, ECO:0000269|PubMed:26766442}. SUBUNIT: Interacts with the dynein-dynactin complex; this interaction is inhibited in a PLK1-dependent manner (By similarity). Part of a spindle orientation complex at least composed of GNAI1, GPSM2 and NUMA1 (By similarity). Interacts with LLGL2 (By similarity). Interacts (via TPR repeat region) with INSC/inscuteable (PubMed:16094321, PubMed:21816348). Interacts (via TPR repeat region) with NUMA1 (via C-terminus); this interaction is direct, inhibited in a PLK1-dependent manner and promotes spindle pole organization (PubMed:21816348, PubMed:23318951, PubMed:23665171). INSC and NUMA1 compete for the same binding site, but INSC has higher affinity and can displace NUMA1 (in vitro) (PubMed:21816348). Interacts with GNAI2 (By similarity). Interacts (via GoLoco domains) with the GDP-bound form of GNAI1 and GNAI3; has much lower affinity for the GTP-bound form (PubMed:22952234, PubMed:23665171). Interaction with GDP-bound GNAI3 strongly enhances the affinity for NUMA1 (PubMed:23665171). Interacts (via TPR repeat region) with FRMPD1 (PubMed:23318951). INSC and FRMPD1 compete for the same binding site, but INSC has higher affinity and can displace FRMPD1 (in vitro) (PubMed:23318951). Interacts (via TPR repeat region) with FRMPD4. Identified in a complex with INSC and F2RL2/Par3 (By similarity). {ECO:0000250|UniProtKB:P81274, ECO:0000269|PubMed:16094321, ECO:0000269|PubMed:21816348, ECO:0000269|PubMed:22952234, ECO:0000269|PubMed:23318951, ECO:0000269|PubMed:23665171}. DOMAIN: Each GoLoco domain can bind one GNAI3 (PubMed:22952234). In the auto-inhibited conformation, the GoLoco domains interact with the TPR repeat region (PubMed:23665171). {ECO:0000269|PubMed:22952234, ECO:0000269|PubMed:23665171}. TISSUE SPECIFICITY: Detected in brain and liver (at protein level). Detected in brain, spleen, liver and testis, and at lower levels in heart, lung and kidney. Enriched in the ventricular zone of the developing central nervous systems. {ECO:0000269|PubMed:12571286}. +Q50H32 GRCR1_MOUSE Glutaredoxin domain-containing cysteine-rich protein 1 290 32,402 Chain (1); Domain (1) FUNCTION: May play a role in actin filament architecture in developing stereocilia of sensory cells. {ECO:0000269|PubMed:20137774}. SUBCELLULAR LOCATION: Cell projection, stereocilium {ECO:0000269|PubMed:20137774}. Cell projection, microvillus {ECO:0000269|PubMed:20137774}. Cell projection, kinocilium {ECO:0000269|PubMed:20137774}. Note=In the inner ear, localized to stereocilia, apical microvilli of sensory cells and kinocilia. TISSUE SPECIFICITY: In the inner ear, expressed predominantly in sensory hair cells and their stereocilia bundles with higher levels in outer hair cells (OHC) at P1 and in inner hair cells (IHC) at P5. At P1, expression is prominent in each row of stereocilia within bundles including immature shorter stereocilia. Expression is also observed in apical microvilli of sensory cells at P1 and in kinocilia at P1 and P5. In the adult, expression is localized throughout the length of the stereocilia of both OHC and IHC (at protein level). {ECO:0000269|PubMed:20137774}. DISEASE: Note=Defects in Grxcr1 are the cause of the pirouette (pi) phenotype which is characterized by vestibular defects and profound deafness with affected mice displaying abnormally thin and slightly shortened sterocilia. {ECO:0000269|PubMed:11276175, ECO:0000269|PubMed:20137774}. +P08884 GRAE_MOUSE Granzyme E (EC 3.4.21.-) (CTL serine protease 2) (Cytotoxic cell protease 3) (CCP3) (Cytotoxic serine protease 2) (D12) (MCSP2) 248 27,494 Active site (3); Chain (1); Disulfide bond (3); Domain (1); Glycosylation (4); Propeptide (1); Sequence conflict (5); Signal peptide (1) FUNCTION: This enzyme is probably necessary for target cell lysis in cell-mediated immune responses. SUBCELLULAR LOCATION: Cytoplasmic granule. Note=Cytoplasmic granules of cytolytic T-lymphocytes. +P08883 GRAF_MOUSE Granzyme F (EC 3.4.21.-) (C134) (CTL serine protease 3) (Cytotoxic cell protease 4) (CCP4) (Cytotoxic serine protease 3) (MCSP3) 248 27,642 Active site (3); Chain (1); Disulfide bond (3); Domain (1); Glycosylation (3); Propeptide (1); Signal peptide (1) FUNCTION: This enzyme is probably necessary for target cell lysis in cell-mediated immune responses. SUBCELLULAR LOCATION: Cytoplasmic granule. Note=Cytoplasmic granules of cytolytic T-lymphocytes. +P13366 GRAG_MOUSE Granzyme G (EC 3.4.21.-) (CTL serine protease 1) (MCSP-1) 248 27,381 Active site (3); Chain (1); Disulfide bond (3); Domain (1); Glycosylation (3); Propeptide (1); Sequence conflict (5); Signal peptide (1) FUNCTION: This enzyme is probably necessary for target cell lysis in cell-mediated immune responses. SUBCELLULAR LOCATION: Cytoplasmic granule. Note=Cytoplasmic granules of cytolytic T-lymphocytes. +O09131 GSTO1_MOUSE Glutathione S-transferase omega-1 (GSTO-1) (EC 2.5.1.18) (Glutathione S-transferase omega 1-1) (GSTO 1-1) (Glutathione-dependent dehydroascorbate reductase) (EC 1.8.5.1) (Monomethylarsonic acid reductase) (MMA(V) reductase) (EC 1.20.4.2) (S-(Phenacyl)glutathione reductase) (SPG-R) (p28) 240 27,498 Active site (1); Binding site (2); Chain (1); Domain (2); Initiator methionine (1); Modified residue (4); Region (1) FUNCTION: Exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities. Has S-(phenacyl)glutathione reductase activity. Has also glutathione S-transferase activity. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA) and dimethylarsonic acid. {ECO:0000250|UniProtKB:P78417}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P78417}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P78417}. +Q8BGR8 GSKIP_MOUSE GSK3B-interacting protein (GSKIP) 139 15,642 Alternative sequence (1); Chain (1); Region (2); Sequence conflict (1); Site (1) FUNCTION: A-kinase anchoring protein for GSK3B and PKA that regulates or facilitates their kinase activity towards their targets. The ternary complex enhances Wnt-induced signaling by facilitating the GSK3B- and PKA-induced phosphorylation of beta-catenin leading to beta-catenin degradation and stabilization respectively. Upon cAMP activation, the ternary complex contributes to neuroprotection against oxidative stress-induced apoptosis by facilitating the PKA-induced phosphorylation of DML1 and PKA-induced inactivation of GSK3B. During neurite outgrowth promotes neuron proliferation; while increases beta-catenin-induced transcriptional activity through GSK3B kinase activity inhibition, reduces N-cadherin level to promote cell cycle progression (By similarity). May play a role in cleft palate formation and is required for postnatal life through modulation of the activity of GSK3B during development (PubMed:26582204). {ECO:0000250|UniProtKB:Q9P0R6, ECO:0000269|PubMed:26582204}. PTM: Phosphorylated by GSK3B. {ECO:0000250|UniProtKB:Q9P0R6}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9P0R6}. Nucleus {ECO:0000250|UniProtKB:Q9P0R6}. SUBUNIT: Forms a complex composed of PRKAR2A or PRKAR2B, GSK3B and GSKIP through GSKIP interaction; facilitates PKA-induced phosphorylation of GSK3B leading to GSK3B inactivation; recruits DNM1L through GSK3B for PKA-mediated phosphorylation of DNM1L; promotes beta-catenin degradation through GSK3B-induced phosphorylation of beta-catenin; stabilizes beta-catenin and enhances Wnt-induced signaling through PKA-induced phosphorylation of beta-catenin. Interacts with GSK3B; induces GSK3B-mediated phosphorylation of GSKIP and inhibits GSK3B kinase activity. {ECO:0000250|UniProtKB:Q9P0R6}. +P13745 GSTA1_MOUSE Glutathione S-transferase A1 (EC 2.5.1.18) (GST class-alpha member 1) (Glutathione S-transferase Ya) (Glutathione S-transferase Ya1) [Cleaved into: Glutathione S-transferase A1, N-terminally processed] 223 25,608 Beta strand (5); Binding site (2); Chain (2); Domain (2); Helix (12); Initiator methionine (1); Modified residue (3); Region (2); Turn (2) FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. SUBUNIT: Homodimer. {ECO:0000269|PubMed:11027134}. +P46425 GSTP2_MOUSE Glutathione S-transferase P 2 (Gst P2) (EC 2.5.1.18) (GST YF-YF) (GST class-pi) (GST-piA) 210 23,537 Binding site (4); Chain (1); Domain (2); Region (2) FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Cannot metabolize 1-chloro-2,4-dinitrobenzene. SUBUNIT: Homodimer. TISSUE SPECIFICITY: Selectively expressed in gall bladder, colon, heart, and skeletal muscle. +A2AUQ7 GTA1L_MOUSE N-acetyllactosaminide alpha-1,3-galactosyltransferase-like 1 (EC 2.4.1.87) 319 37,953 Active site (1); Chain (1); Glycosylation (2); Region (3); Sequence conflict (3); Topological domain (2); Transmembrane (1) TRANSMEM 7 26 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 27 319 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Synthesizes the galactose-alpha(1,3)-galactose group by catalyzing the transfer of a galactose residue, with an alpha-1,3 linkage, on terminal lactosaminide (Gal-beta-1,4-GlcNAc-R) disaccharide borne by a glycoprotein or a glycolipid. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Membrane-bound form in trans cisternae of Golgi. {ECO:0000250}. DOMAIN: The conserved DXD motif is involved in cofactor binding. The manganese ion interacts with the beta-phosphate group of UDP and may also have a role in catalysis (By similarity). {ECO:0000250}. +P32037 GTR3_MOUSE Solute carrier family 2, facilitated glucose transporter member 3 (Glucose transporter type 3, brain) (GLUT-3) 493 53,479 Binding site (3); Chain (1); Glycosylation (1); Modified residue (4); Region (2); Topological domain (13); Transmembrane (12) TRANSMEM 11 32 Helical; Name=1. {ECO:0000250|UniProtKB:P11169, ECO:0000255}.; TRANSMEM 65 85 Helical; Name=2. {ECO:0000250|UniProtKB:P11169, ECO:0000255}.; TRANSMEM 91 111 Helical; Name=3. {ECO:0000250|UniProtKB:P11169}.; TRANSMEM 119 142 Helical; Name=4. {ECO:0000250|UniProtKB:P11169, ECO:0000255}.; TRANSMEM 154 174 Helical; Name=5. {ECO:0000250|UniProtKB:P11169, ECO:0000255}.; TRANSMEM 184 204 Helical; Name=6. {ECO:0000250|UniProtKB:P11169, ECO:0000255}.; TRANSMEM 270 290 Helical; Name=7. {ECO:0000250|UniProtKB:P11169, ECO:0000255}.; TRANSMEM 305 325 Helical; Name=8. {ECO:0000250|UniProtKB:P11169, ECO:0000255}.; TRANSMEM 332 352 Helical; Name=9. {ECO:0000250|UniProtKB:P11169, ECO:0000255}.; TRANSMEM 364 389 Helical; Name=10. {ECO:0000250|UniProtKB:P11169, ECO:0000255}.; TRANSMEM 400 420 Helical; Name=11. {ECO:0000250|UniProtKB:P11169, ECO:0000255}.; TRANSMEM 430 450 Helical; Name=12. {ECO:0000250|UniProtKB:P11169, ECO:0000255}. TOPO_DOM 1 10 Cytoplasmic. {ECO:0000250|UniProtKB:P11169}.; TOPO_DOM 33 64 Extracellular. {ECO:0000250|UniProtKB:P11169}.; TOPO_DOM 86 90 Cytoplasmic. {ECO:0000250|UniProtKB:P11169}.; TOPO_DOM 112 118 Extracellular. {ECO:0000250|UniProtKB:P11169}.; TOPO_DOM 143 153 Cytoplasmic. {ECO:0000250|UniProtKB:P11169}.; TOPO_DOM 175 183 Extracellular. {ECO:0000250|UniProtKB:P11169}.; TOPO_DOM 205 269 Cytoplasmic. {ECO:0000250|UniProtKB:P11169}.; TOPO_DOM 291 304 Extracellular. {ECO:0000250|UniProtKB:P11169}.; TOPO_DOM 326 331 Cytoplasmic. {ECO:0000250|UniProtKB:P11169}.; TOPO_DOM 353 363 Extracellular. {ECO:0000250|UniProtKB:P11169}.; TOPO_DOM 390 399 Cytoplasmic. {ECO:0000250|UniProtKB:P11169}.; TOPO_DOM 421 429 Extracellular. {ECO:0000250|UniProtKB:P11169}.; TOPO_DOM 451 493 Cytoplasmic. {ECO:0000250|UniProtKB:P11169}. FUNCTION: Facilitative glucose transporter that can also mediate the uptake of various other monosaccharides across the cell membrane. Mediates the uptake of glucose, 2-deoxyglucose, galactose, mannose, xylose and fucose, and probably also dehydroascorbate. Does not mediate fructose transport. {ECO:0000250|UniProtKB:P11169}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1730609}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P11169}. Perikaryon {ECO:0000250|UniProtKB:Q07647}. Cell projection {ECO:0000250|UniProtKB:Q07647}. Note=Localized to densely spaced patches along neuronal processes. {ECO:0000250|UniProtKB:Q07647}. DOMAIN: Transport is mediated via a series of conformation changes, switching between a conformation where the substrate-binding cavity is accessible from the outside, and a another conformation where it is accessible from the cytoplasm. {ECO:0000250|UniProtKB:P11169}. TISSUE SPECIFICITY: Detected in brain (at protein level). Highly expressed in brain. {ECO:0000269|PubMed:1730609}. +Q8BZI6 GUCD1_MOUSE Protein GUCD1 (Guanylyl cyclase domain-containing protein 1) (Protein LLN4) 239 27,264 Chain (1); Erroneous initiation (1); Sequence conflict (1) +Q8K2A1 GULP1_MOUSE PTB domain-containing engulfment adapter protein 1 (Cell death protein 6 homolog) (PTB domain adapter protein CED-6) (Protein GULP) 304 34,470 Alternative sequence (1); Chain (1); Coiled coil (1); Domain (1); Erroneous initiation (1); Modified residue (2); Sequence conflict (2) FUNCTION: Modulates cellular glycosphingolipid and cholesterol transport. May play a role in the internalization of various LRP1 ligands, such as PSAP (By similarity). May function as an adapter protein. Required for efficient phagocytosis of apoptotic cells. Increases cellular levels of GTP-bound ARF6. {ECO:0000250, ECO:0000269|PubMed:17398097}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=May associate with the cytoplasmic side of the plasma membrane and early endosomes. {ECO:0000250}. SUBUNIT: Homodimer. Interacts with clathrin and MEGF10 (By similarity). Interacts with GDP-bound ARF6, but not with GTP-bound ARF6. Part of a complex composed of GULP1, ACAP1 and ARF6. Interacts with ACAP1, LRP1 and STAB2. {ECO:0000250, ECO:0000269|PubMed:11729193, ECO:0000269|PubMed:17398097, ECO:0000269|PubMed:18230608}. TISSUE SPECIFICITY: Detected throughout the brain, particularly in Purkinje cells, hippocampal and cortical neurons (at protein level). {ECO:0000269|PubMed:17007823}. +Q3SXD3 HDDC2_MOUSE HD domain-containing protein 2 199 22,753 Chain (1); Domain (1); Initiator methionine (1); Modified residue (3) +P70288 HDAC2_MOUSE Histone deacetylase 2 (HD2) (EC 3.5.1.98) (YY1 transcription factor-binding protein) 488 55,302 Active site (1); Chain (1); Compositional bias (1); Cross-link (7); Modified residue (8); Mutagenesis (3); Region (1); Sequence conflict (1) FUNCTION: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes (By similarity). Forms transcriptional repressor complexes by associating with MAD, SIN3, YY1 and N-COR. Interacts in the late S-phase of DNA-replication with DNMT1 in the other transcriptional repressor complex composed of DNMT1, DMAP1, PCNA, CAF1. Deacetylates TSHZ3 and regulates its transcriptional repressor activity. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. May be involved in the transcriptional repression of circadian target genes, such as PER1, mediated by CRY1 through histone deacetylation. Involved in MTA1-mediated transcriptional corepression of TFF1 and CDKN1A. {ECO:0000250, ECO:0000269|PubMed:15226430, ECO:0000269|PubMed:17707228, ECO:0000269|PubMed:20071335}. PTM: S-nitrosylated by GAPDH. In neurons, S-Nitrosylation at Cys-262 and Cys-274 does not affect the enzyme activity but abolishes chromatin-binding, leading to increases acetylation of histones and activate genes that are associated with neuronal development. In embryonic cortical neurons, S-Nitrosylation regulates dendritic growth and branching. {ECO:0000269|PubMed:18754010, ECO:0000269|PubMed:20519513, ECO:0000269|PubMed:20972425}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with SNW1, PELP1, ATR, DNMT1, MINT, HDAC10, HCFC1, NRIP1, KDM4A, CHFR and SAP30L. Part of the core histone deacetylase (HDAC) complex composed of HDAC1, HDAC2, RBBP4 and RBBP7. The core complex associates with MTA2, MBD3, MTA1L1, CHD3 and CHD4 to form the nucleosome remodeling and histone deacetylation (NuRD) complex, or with SIN3, SAP18 and SAP30 to form the SIN3 HDAC complex. Interacts (CK2 phosphorylated form) with SP3. Interacts with TSHZ3 (via its N-terminus). Interacts with APEX1; the interaction is not dependent on the acetylated status of APEX1. Component of a BHC histone deacetylase complex that contains HDAC1, HDAC2, HMG20B, KDM1A, RCOR1 and PHF21A. The BHC complex may also contain ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I. Part of a complex containing the core histones H2A, H2B, H3 and H4, DEK and unphosphorylated DAXX. Part of a complex containing ATR and CHD4. Forms a heterologous complex at least with YY1. Component of a mSin3A corepressor complex that contains SIN3A, SAP130, SUDS3, ARID4B, HDAC1 and HDAC2. Interacts with CBFA2T3, HDAC7, PRDM6, SAP30, SETDB1 and SUV39H1. Interacts with the H2AFY (via the non-histone region). Component of a RCOR/GFI/KDM1A/HDAC complex. Interacts directly with GFI1 and GFI1B. Part of a complex composed of TRIM28, HDAC1, HDAC2 and EHMT2. Interacts with PIMREG. Interacts with BCL6 (non-acetylated form). Part of a complex containing at least CDYL, MIER1, MIER2, HDAC1 and HDAC2. Interacts with CRY1, INSM1 and ZNF431. Interacts with NACC2 (By similarity). Interacts with MTA1, with a preference for sumoylated MTA1. Interacts with SIX3. Interacts with BEND3 (By similarity). Component of a histone deacetylase complex containing DNTTIP1, ZNF541, HDAC1 and HDAC2 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q92769, ECO:0000269|PubMed:10984530, ECO:0000269|PubMed:11533236, ECO:0000269|PubMed:11788710, ECO:0000269|PubMed:12398767, ECO:0000269|PubMed:15226430, ECO:0000269|PubMed:16107708, ECO:0000269|PubMed:16537907, ECO:0000269|PubMed:17666527, ECO:0000269|PubMed:17707228, ECO:0000269|PubMed:20519513, ECO:0000269|PubMed:21177534, ECO:0000269|PubMed:22391310, ECO:0000269|PubMed:24227653, ECO:0000269|PubMed:9702189}. +Q6NZM9 HDAC4_MOUSE Histone deacetylase 4 (HD4) (EC 3.5.1.98) 1076 118,562 Active site (1); Alternative sequence (2); Chain (1); Coiled coil (1); Compositional bias (2); Cross-link (1); Metal binding (4); Modified residue (7); Motif (2); Region (2); Sequence conflict (2) FUNCTION: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Involved in muscle maturation via its interaction with the myocyte enhancer factors such as MEF2A, MEF2C and MEF2D. Deacetylates HSPA1A and HSPA1A at 'Lys-77' leading to their preferential binding to co-chaperone STUB1. {ECO:0000250|UniProtKB:P56524}. PTM: Phosphorylated by CaMK4 at Ser-245, Ser-465 and Ser-629. Phosphorylation at other residues by CaMK2D is required for the interaction with 14-3-3. Phosphorylation at Ser-349, within the PxLPxI/L motif, impairs the binding of ANKRA2 but generates a high-affinity docking site for 14-3-3 (By similarity). {ECO:0000250|UniProtKB:P56524}.; PTM: Sumoylation on Lys-556 is promoted by the E3 SUMO-protein ligase RANBP2, and prevented by phosphorylation by CaMK4. {ECO:0000269|PubMed:17468767, ECO:0000269|PubMed:17923476}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Shuttles between the nucleus and the cytoplasm. Upon muscle cells differentiation, it accumulates in the nuclei of myotubes, suggesting a positive role of nuclear HDAC4 in muscle differentiation. The export to cytoplasm depends on the interaction with a 14-3-3 chaperone protein and is due to its phosphorylation at Ser-245, Ser-465 and Ser-629 by CaMK4 and SIK1. The nuclear localization probably depends on sumoylation (By similarity). {ECO:0000250}. SUBUNIT: Homodimer. Homodimerization via its N-terminal domain (By similarity). Interacts with HDAC7 (PubMed:10984530). Interacts with MEF2A, MEF2C, MEF2D, MORC2 and NR2C1. Interacts with a 14-3-3 chaperone protein in a phosphorylation dependent manner. Interacts with BTBD14B. Interacts with KDM5B. Interacts (via PxLPxI/L motif) with ANKRA2 (via ankyrin repeats). Interacts with CUL7 (as part of the 3M complex); negatively regulated by ANKRA2. Interacts with EP300 in the presence of TFAP2C (By similarity). Interacts with AHRR (PubMed:17949687). Interacts with MYOCD (PubMed:15601857). Interacts with HSPA1A and HSPA1B leading to their deacetylation at 'Lys-77' (By similarity). Interacts with ZBTB7B; the interaction allows the recruitment of HDAC4 on CD8 loci for deacetylation and possible inhibition of CD8 genes expression (PubMed:22730529). Interacts with DHX36 (PubMed:21590736). {ECO:0000250|UniProtKB:P56524, ECO:0000250|UniProtKB:Q99P99, ECO:0000269|PubMed:10984530, ECO:0000269|PubMed:15601857, ECO:0000269|PubMed:17949687, ECO:0000269|PubMed:21590736, ECO:0000269|PubMed:22730529}. DOMAIN: The nuclear export sequence mediates the shuttling between the nucleus and the cytoplasm. {ECO:0000250}.; DOMAIN: The PxLPxI/L motif mediates interaction with ankyrin repeats of ANKRA2. {ECO:0000250|UniProtKB:P56524}. +Q9JMG7 HDGR3_MOUSE Hepatoma-derived growth factor-related protein 3 (HRP-3) 202 22,431 Alternative sequence (1); Beta strand (6); Chain (1); Domain (1); Frameshift (1); Helix (3); Modified residue (4); Motif (1); Sequence conflict (1); Turn (1) FUNCTION: Enhances DNA synthesis and may play a role in cell proliferation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +Q8C2B3 HDAC7_MOUSE Histone deacetylase 7 (HD7) (EC 3.5.1.98) (Histone deacetylase 7A) (HD7a) 938 101,287 Active site (1); Alternative sequence (4); Chain (1); Compositional bias (1); Metal binding (4); Modified residue (9); Motif (1); Mutagenesis (7); Region (6); Sequence conflict (9); Site (1) FUNCTION: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Involved in muscle maturation by repressing transcription of myocyte enhancer factors such as MEF2A, MEF2B and MEF2C. During muscle differentiation, it shuttles into the cytoplasm, allowing the expression of myocyte enhancer factors. Positively regulates the transcriptional repressor activity of FOXP3 (By similarity). {ECO:0000250|UniProtKB:Q8WUI4, ECO:0000269|PubMed:10640276}. PTM: May be phosphorylated by CaMK1. Phosphorylated by the PKC kinases PKN1 and PKN2, impairing nuclear import. Phosphorylation at Ser-178 by MARK2, MARK3 and PRKD1 promotes interaction with 14-3-3 proteins and export from the nucleus. Phosphorylation at Ser-178 is a prerequisite for phosphorylation at Ser-204 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=In the nucleus, it associates with distinct subnuclear dot-like structures. Shuttles between the nucleus and the cytoplasm. In muscle cells, it shuttles into the cytoplasm during myocyte differentiation. The export to cytoplasm depends on the interaction with the 14-3-3 protein YWHAE and is due to its phosphorylation. SUBUNIT: Interacts with KDM5B (By similarity). Interacts with KAT5 and EDNRA. Interacts with HDAC1, HDAC2, HDAC3, HDAC4, HDAC5, NCOR1, NCOR2, SIN3A, SIN3B, RBBP4, RBBP7, MTA1L1, SAP30 and MBD3. Interacts with the 14-3-3 protein YWHAE, MEF2A, MEF2B and MEF2C. Interacts with ZMYND15. Interacts with PML (By similarity). Interacts with FOXP3. {ECO:0000250|UniProtKB:Q8WUI4, ECO:0000269|PubMed:10640276, ECO:0000269|PubMed:10984530, ECO:0000269|PubMed:11279209, ECO:0000269|PubMed:11585834, ECO:0000269|PubMed:19696312, ECO:0000269|PubMed:20675388}. DOMAIN: The nuclear export sequence mediates the shuttling between the nucleus and the cytoplasm. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in heart and lung. Expressed at intermediate level in muscle. {ECO:0000269|PubMed:10640276, ECO:0000269|PubMed:11279209}. +Q8VH37 HDAC8_MOUSE Histone deacetylase 8 (HD8) (EC 3.5.1.98) 377 41,772 Active site (1); Alternative sequence (2); Binding site (3); Chain (1); Metal binding (3); Modified residue (1); Region (1); Sequence conflict (5) FUNCTION: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Also involved in the deacetylation of cohesin complex protein SMC3 regulating release of cohesin complexes from chromatin. May play a role in smooth muscle cell contractility (By similarity). {ECO:0000250}. PTM: Phosphorylated by PKA on serine 39. Phosphorylation reduces deacetylase activity observed preferentially on histones H3 and H4 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with CBFA2T3. Interacts with phosphorylated SMG5/EST1B; this interaction protects SMG5 from ubiquitin-mediated degradation. Associates with alpha-SMA (smooth muscle alpha-actin) (By similarity). {ECO:0000250}. +Q5QNV8 HEAT9_MOUSE Protein HEATR9 (HEAT repeat-containing protein 9) 569 65,861 Chain (1) +Q9R257 HEBP1_MOUSE Heme-binding protein 1 (p22HBP) 190 21,067 Beta strand (14); Chain (1); Helix (3); Sequence conflict (4); Turn (1) FUNCTION: May bind free porphyrinogens that may be present in the cell and thus facilitate removal of these potentially toxic compound. Binds with a high affinity to one molecule of heme or porphyrins. It binds metalloporphyrins, free porphyrins and N-methylprotoporphyrin with similar affinities. {ECO:0000269|PubMed:12413491, ECO:0000269|PubMed:16905545}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12413491, ECO:0000269|PubMed:9813049}. SUBUNIT: Monomer. {ECO:0000269|PubMed:12413491, ECO:0000269|PubMed:16905148, ECO:0000269|PubMed:16905545}. DOMAIN: Forms a distorted beta-barrel structure, with two helices that are packed against the outer surface of the barrel. Porphyrins are expected to bind to a hydrophobic patch on the outer surface of the beta-barrel structure. {ECO:0000269|PubMed:16905148, ECO:0000269|PubMed:16905545}. TISSUE SPECIFICITY: Ubiquitously expressed. Extremely abundant in liver. {ECO:0000269|PubMed:9813049}. +Q6DFV5 HELZ_MOUSE Probable helicase with zinc finger domain (EC 3.6.4.-) 1964 219,880 Alternative sequence (3); Chain (1); Erroneous initiation (1); Modified residue (7); Motif (1); Nucleotide binding (1); Sequence conflict (4); Zinc finger (1) FUNCTION: May act as a helicase that plays a role in RNA metabolism in multiple tissues and organs within the developing embryo. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Interacts with POLR2A. Interacts with SMYD3; the interaction may bridge SMYD3 and RNA polymerase II (By similarity). Interacts with SMYD2. {ECO:0000250, ECO:0000269|PubMed:20305823}. +Q640R3 HECAM_MOUSE Hepatocyte cell adhesion molecule (Protein hepaCAM) 418 46,367 Chain (1); Disulfide bond (1); Domain (2); Glycosylation (4); Modified residue (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 241 261 Helical. {ECO:0000255}. TOPO_DOM 34 240 Extracellular. {ECO:0000255}.; TOPO_DOM 262 418 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in regulating cell motility and cell-matrix interactions. May inhibit cell growth through suppression of cell proliferation (By similarity). {ECO:0000250|UniProtKB:Q14CZ8}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q14CZ8}. SUBCELLULAR LOCATION: Cytoplasm. Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250|UniProtKB:Q14CZ8}. Note=Colocalizes with CDH1. {ECO:0000250|UniProtKB:Q14CZ8}. SUBUNIT: Homodimer. Dimer formation occurs predominantly through cis interactions on the cell surface (By similarity). Part of a complex containing MLC1, TRPV4, AQP4 and ATP1B1 (By similarity). {ECO:0000250}. DOMAIN: The cytoplasmic domain plays an important role in regulation of cell-matrix adhesion and cell motility. {ECO:0000250|UniProtKB:Q14CZ8}. +P10518 HEM2_MOUSE Delta-aminolevulinic acid dehydratase (ALADH) (EC 4.2.1.24) (Porphobilinogen synthase) 330 36,024 Active site (2); Beta strand (12); Binding site (4); Chain (1); Helix (17); Metal binding (5); Modified residue (3); Turn (2) Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4. FUNCTION: Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen (By similarity). {ECO:0000250}. SUBUNIT: Homooctamer; active form. Homohexamer; low activity form (By similarity). {ECO:0000250}. +Q8K0T4 KATL1_MOUSE Katanin p60 ATPase-containing subunit A-like 1 (Katanin p60 subunit A-like 1) (EC 5.6.1.1) (p60 katanin-like 1) 488 55,165 Chain (1); Modified residue (2); Mutagenesis (1); Nucleotide binding (1) FUNCTION: Regulates microtubule dynamics in Sertoli cells, a process that is essential for spermiogenesis and male fertility. Severs microtubules in an ATP-dependent manner, promoting rapid reorganization of cellular microtubule arrays (PubMed:22654668). Has microtubule-severing activity in vitro (By similarity). {ECO:0000250|UniProtKB:Q9BW62, ECO:0000269|PubMed:22654668}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03024, ECO:0000269|PubMed:22654668}. Cytoplasm {ECO:0000250|UniProtKB:Q9BW62}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q9BW62}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9BW62}. Note=Colocalizes with microtubules throughout the basal and adluminal compartments of Sertoli cells (PubMed:22654668). Localizes within the cytoplasm, partially overlapping with microtubules, in interphase and to the mitotic spindle and spindle poles during mitosis (By similarity). {ECO:0000250|UniProtKB:Q9BW62, ECO:0000269|PubMed:22654668}. SUBUNIT: Interacts with KATNB1 and KATNBL1. {ECO:0000250|UniProtKB:Q9BW62}. TISSUE SPECIFICITY: Widely expressed, including in testis, brain, heart, lung, kidney, liver, spleen, seminal vesicles and ovary. In testis, restricted to Sertoli cells within the seminiferous epithelium (at protein level). {ECO:0000269|PubMed:22654668}. +P28652 KCC2B_MOUSE Calcium/calmodulin-dependent protein kinase type II subunit beta (CaM kinase II subunit beta) (CaMK-II subunit beta) (EC 2.7.11.17) 542 60,461 Active site (1); Binding site (1); Chain (1); Domain (1); Modified residue (10); Mutagenesis (1); Nucleotide binding (1); Region (2); Sequence conflict (1) FUNCTION: Calcium/calmodulin-dependent protein kinase that functions autonomously after Ca(2+)/calmodulin-binding and autophosphorylation, and is involved in dendritic spine and synapse formation, neuronal plasticity and regulation of sarcoplasmic reticulum Ca(2+) transport in skeletal muscle. In neurons, plays an essential structural role in the reorganization of the actin cytoskeleton during plasticity by binding and bundling actin filaments in a kinase-independent manner. This structural function is required for correct targeting of CaMK2A, which acts downstream of NMDAR to promote dendritic spine and synapse formation and maintain synaptic plasticity which enables long-term potentiation (LTP) and hippocampus-dependent learning. In developing hippocampal neurons, promotes arborization of the dendritic tree and in mature neurons, promotes dendritic remodeling. Also regulates the migration of developing neurons (PubMed:29100089). Participates in the modulation of skeletal muscle function in response to exercise. In slow-twitch muscles, is involved in regulation of sarcoplasmic reticulum (SR) Ca(2+) transport and in fast-twitch muscle participates in the control of Ca(2+) release from the SR through phosphorylation of triadin, a ryanodine receptor-coupling factor, and phospholamban (PLN/PLB), an endogenous inhibitor of SERCA2A/ATP2A2 (PubMed:21752990). {ECO:0000269|PubMed:21752990, ECO:0000269|PubMed:29100089}. PTM: Autophosphorylation of Thr-287 following activation by Ca(2+)/calmodulin. Phosphorylation of Thr-287 locks the kinase into an activated state. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Sarcoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell junction, synapse {ECO:0000250|UniProtKB:P08413}. SUBUNIT: CAMK2 is composed of 4 different chains: alpha (CAMK2A), beta (CAMK2B), gamma (CAMK2G), and delta (CAMK2D). The different isoforms assemble into homo- or heteromultimeric holoenzymes composed of 12 subunits with two hexameric rings stacked one on top of the other. Interacts with SYNGAP1, CAMK2N2 and MPDZ (By similarity). Interacts with FOXO3 (PubMed:23805378). Interacts (when in a kinase inactive state not associated with calmodulin) with ARC; leading to target ARC to inactive synapses (By similarity). {ECO:0000250|UniProtKB:P08413, ECO:0000250|UniProtKB:Q13554, ECO:0000269|PubMed:23805378}. DOMAIN: The CAMK2 protein kinases contain a unique C-terminal subunit association domain responsible for oligomerization. +P36552 HEM6_MOUSE Oxygen-dependent coproporphyrinogen-III oxidase, mitochondrial (COX) (Coprogen oxidase) (Coproporphyrinogenase) (EC 1.3.3.3) 443 49,715 Active site (1); Binding site (1); Chain (1); Erroneous initiation (1); Frameshift (1); Modified residue (3); Region (4); Sequence conflict (7); Site (1); Transit peptide (1) Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrinogen-IX from coproporphyrinogen-III (O2 route): step 1/1. FUNCTION: Involved in the heme biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-IX (By similarity). {ECO:0000250}. PTM: Acetylation of Lys-360 is observed in liver mitochondria from fasted mice but not from fed mice. SUBCELLULAR LOCATION: Mitochondrion intermembrane space. SUBUNIT: Homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Erythroid cells and non erythroid cells such as liver. +Q8K0E1 KCD15_MOUSE BTB/POZ domain-containing protein KCTD15 (Potassium channel tetramerization domain-containing protein 15) 283 31,886 Chain (1); Domain (1); Modified residue (3) FUNCTION: During embryonic development, interferes with neural crest formation. Inhibits AP2 transcriptional activity by interaction with its activation domain (By similarity). {ECO:0000250}. SUBUNIT: Interacts with TFAP2A; this interaction inhibits TFAP2A transcriptional activation. {ECO:0000250}. +Q562E2 KCD19_MOUSE BTB/POZ domain-containing protein KCTD19 927 104,820 Alternative sequence (1); Chain (1); Domain (2); Modified residue (1); Sequence conflict (1) SUBUNIT: Identified in a complex with ZNF541, HDAC1 and HSPA2. {ECO:0000269|PubMed:18849567}. TISSUE SPECIFICITY: Detected in adult testis. {ECO:0000269|PubMed:18849567}. +Q3URF8 KCD21_MOUSE BTB/POZ domain-containing protein KCTD21 (KCASH2 protein) (Potassium channel tetramerization domain-containing protein 21) 260 29,623 Chain (1); Coiled coil (1); Compositional bias (1); Domain (1) Protein modification; protein ubiquitination. FUNCTION: Probable substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex mediating the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes the ubiquitination of HDAC1. Can function as antagonist of the Hedgehog pathway by affecting the nuclear transfer of transcription factor GLI1; the function probably occurs via HDAC1 down-regulation, keeping GLI1 acetylated and inactive. Inhibits cell growth and tumorigenicity of medulloblastoma (MDB). {ECO:0000250|UniProtKB:Q4G0X4}. SUBUNIT: Homopentamer. Interacts with KCTD11; KCTD21 and KCTD11 may associate in pentameric assemblies. Interacts (via BTB domain) with CUL3; indicative for a participation in a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex (PubMed:21472142). {ECO:0000250|UniProtKB:Q4G0X4, ECO:0000305}. TISSUE SPECIFICITY: Highly expressed in cerebellum and brain. Expressed in adult cerebellum (at protein level). {ECO:0000269|PubMed:21472142}. +Q921L7 HEMK1_MOUSE HemK methyltransferase family member 1 (EC 2.1.1.-) 340 38,233 Binding site (2); Chain (1); Region (2); Sequence conflict (5) FUNCTION: N5-glutamine methyltransferase responsible for the methylation of the GGQ triplet of the mitochondrial translation release factor MTRF1L. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. +P49182 HEP2_MOUSE Heparin cofactor 2 (Heparin cofactor II) (HC-II) (Protease inhibitor leuserpin-2) (Serpin D1) 478 54,497 Chain (1); Glycosylation (4); Modified residue (2); Region (2); Repeat (2); Signal peptide (1); Site (1) FUNCTION: Thrombin inhibitor activated by the glycosaminoglycans, heparin or dermatan sulfate. In the presence of the latter, HC-II becomes the predominant thrombin inhibitor in place of antithrombin III (AT). Also inhibits chymotrypsin, but in a glycosaminoglycan-independent manner. PTM: N-glycosylated; different glycan composition appears to lead to two forms of this protein (68 and 72 kDa). {ECO:0000269|PubMed:16944957}. DOMAIN: The N-terminal acidic repeat region mediates, in part, the glycosaminoglycan-accelerated thrombin inhibition. {ECO:0000250}. TISSUE SPECIFICITY: Expressed predominantly in liver. +Q9R1Y5 HIC1_MOUSE Hypermethylated in cancer 1 protein (Hic-1) 733 76,828 Chain (1); Compositional bias (4); Cross-link (1); Domain (1); Erroneous gene model prediction (1); Erroneous initiation (1); Modified residue (6); Region (2); Sequence conflict (4); Zinc finger (5) FUNCTION: Transcriptional repressor. Recognizes and binds to the consensus sequence '5-[CG]NG[CG]GGGCA[CA]CC-3'. May act as a tumor suppressor. May be involved in development of head, face, limbs and ventral body wall. Involved in down-regulation of SIRT1 and thereby is involved in regulation of p53/TP53-dependent apoptotic DNA-damage responses. The specific target gene promoter association seems to be depend on corepressors, such as CTBP1 or CTBP2 and MTA1. The regulation of SIRT1 transcription in response to nutrient deprivation seems to involve CTBP1. In cooperation with MTA1 (indicative for an association with the NuRD complex) represses transcription from CCND1/cyclin-D1 and CDKN1C/p57Kip2 specifically in quiescent cells. Involved in regulation of the Wnt signaling pathway probably by association with TCF7L2 and preventing TCF7L2 and CTNNB1 association with promoters of TCF-responsive genes. Seems to repress transcription from E2F1 and ATOH1 which involves ARID1A, indicative for the participation of a distinct SWI/SNF-type chromatin-remodeling complex. Probably represses transcription from ACKR3, FGFBP1 and EFNA1. {ECO:0000269|PubMed:16269335, ECO:0000269|PubMed:18347096}. PTM: Acetylated on several residues, including Lys-333. Lys-333 is deacetylated by SIRT1 (By similarity). {ECO:0000250}.; PTM: Sumoylated on Lys-333 by a PIAS family member, which enhances interaction with MTA1, positively regulates transcriptional repression activity and is enhanced by HDAC4. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Self-associates. Interacts with HIC2. Interacts with CTBP1 and CTBP2. Interacts with TCF7L2 and ARID1A. Interacts with MTA1 and MBD3; indicative for an association with the NuRD complex (By similarity). {ECO:0000250}. DOMAIN: The BTB domain inhibits the binding to a single consensus binding site, but mediates cooperative binding to multiple binding sites. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed with highest levels in heart and lung. {ECO:0000269|PubMed:10655551}. DISEASE: Note=Defects in Hic1 are the cause of perinatal death with serious developmental anomalies, including acrania, exencephaly, cleft palate, omphalocele, craniofacial and limb anomalies. {ECO:0000269|PubMed:10655551}. +Q3V016 HIPK4_MOUSE Homeodomain-interacting protein kinase 4 (EC 2.7.11.1) 616 69,279 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Compositional bias (2); Domain (1); Modified residue (1); Mutagenesis (1); Nucleotide binding (1); Sequence conflict (4) FUNCTION: Protein kinase that phosphorylates murine TP53 at Ser-9, and thus induces TP53 repression of BIRC5 promoter. May act as a corepressor of transcription factors (Potential). {ECO:0000305}. PTM: Autophosphorylated. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18022393}. TISSUE SPECIFICITY: Expressed at moderate levels in lung and white adipose tissues and weakly in brain and liver. {ECO:0000269|PubMed:18022393}. +P47856 GFPT1_MOUSE Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1 (EC 2.6.1.16) (D-fructose-6-phosphate amidotransferase 1) (Glutamine:fructose-6-phosphate amidotransferase 1) (GFAT 1) (GFAT1) (Hexosephosphate aminotransferase 1) 697 78,539 Active site (1); Alternative sequence (1); Binding site (2); Chain (1); Domain (3); Initiator methionine (1); Modified residue (1); Region (3); Sequence conflict (1) Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; alpha-D-glucosamine 6-phosphate from D-fructose 6-phosphate: step 1/1. FUNCTION: Controls the flux of glucose into the hexosamine pathway. Most likely involved in regulating the availability of precursors for N- and O-linked glycosylation of proteins. Regulates the circadian expression of clock genes ARNTL/BMAL1 and CRY1. {ECO:0000269|PubMed:23395176}. SUBUNIT: Homotetramer, may also exist as homodimers. {ECO:0000250}. TISSUE SPECIFICITY: Isoform 1 is predominantly expressed in hindlimb muscle and is also expressed weakly in the heart. Seems to be selectively expressed in striated muscle. {ECO:0000269|PubMed:11679416}. +Q9Z2Z9 GFPT2_MOUSE Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 2 (EC 2.6.1.16) (D-fructose-6-phosphate amidotransferase 2) (Glutamine:fructose-6-phosphate amidotransferase 2) (GFAT 2) (GFAT2) (Hexosephosphate aminotransferase 2) 682 77,009 Active site (1); Binding site (2); Chain (1); Domain (3); Initiator methionine (1); Modified residue (1); Region (2) Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; alpha-D-glucosamine 6-phosphate from D-fructose 6-phosphate: step 1/1. FUNCTION: Controls the flux of glucose into the hexosamine pathway. Most likely involved in regulating the availability of precursors for N- and O-linked glycosylation of proteins. +O35118 GFRA3_MOUSE GDNF family receptor alpha-3 (GDNF receptor alpha-3) (GDNFR-alpha-3) (GFR-alpha-3) 397 44,307 Chain (1); Glycosylation (3); Lipidation (1); Propeptide (1); Sequence conflict (7); Signal peptide (1) FUNCTION: Receptor for the glial cell line-derived neurotrophic factor, artemin. Mediates the artemin-induced autophosphorylation and activation of the RET receptor tyrosine kinase (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. +Q9Z0G0 GIPC1_MOUSE PDZ domain-containing protein GIPC1 (GAIP C-terminus-interacting protein) (RGS-GAIP-interacting protein) (RGS19-interacting protein 1) (SemaF cytoplasmic domain-associated protein 1) (SEMCAP-1) (Synectin) 333 36,129 Beta strand (13); Chain (1); Domain (1); Helix (8); Modified residue (6); Sequence conflict (4); Turn (2) FUNCTION: Inhibits endothelial cell migration (in vitro). May be involved in G protein-linked signaling (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. SUBUNIT: Interacts with GLUT1 (C-terminus), ACTN1, KIF1B, MYO6 and PLEKHG5 (By similarity). Interacts with RGS19 C-terminus. Interacts with SDC4/syndecan-4 and SEMA4C/semaphorin-4C. {ECO:0000250, ECO:0000269|PubMed:10318831, ECO:0000269|PubMed:10911369, ECO:0000269|PubMed:9770488}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15527962}. +P70224 GIMA1_MOUSE GTPase IMAP family member 1 (Immune-associated protein 38) (IAP38) (Immunity-associated protein 1) 277 30,829 Binding site (2); Chain (1); Domain (1); Erroneous translation (2); Nucleotide binding (2); Topological domain (2); Transmembrane (1) TRANSMEM 251 266 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 1 250 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 267 277 Lumenal. {ECO:0000255}. FUNCTION: May regulate lymphocyte survival. Required for normal levels of mature T-lymphocytes and mature B-cells. {ECO:0000269|PubMed:20194894}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type IV membrane protein. Golgi apparatus membrane. TISSUE SPECIFICITY: Detected in mature B-cells and thymocytes (at protein level). Detected in lymph nodes and thymocytes. {ECO:0000269|PubMed:20194894}. +Q99MI6 GIMA3_MOUSE GTPase IMAP family member 3 (Immunity-associated nucleotide 4 protein) (IAN-4) 301 34,179 Binding site (2); Chain (1); Domain (1); Frameshift (1); Nucleotide binding (2); Sequence conflict (3); Topological domain (2); Transmembrane (1) TRANSMEM 280 300 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 1 279 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 301 301 Lumenal. {ECO:0000255}. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass type IV membrane protein. TISSUE SPECIFICITY: May be restricted to certain hematopoietic cells. +O35594 IFT81_MOUSE Intraflagellar transport protein 81 homolog (Carnitine deficiency-associated protein expressed in ventricle 1) (CDV-1) 676 79,285 Alternative sequence (1); Chain (1); Coiled coil (4); Initiator methionine (1); Modified residue (2); Region (1) FUNCTION: Component of the intraflagellar transport (IFT) complex B: together with IFT74, forms a tubulin-binding module that specifically mediates transport of tubulin within the cilium. Binds tubulin via its CH (calponin-homology)-like region. Required for ciliogenesis. Required for proper regulation of SHH signaling. {ECO:0000250|UniProtKB:Q8WYA0}.; FUNCTION: Isoform CDV-1: May be involved in cardiac hypertrophy caused by carnitine deficiency. {ECO:0000269|PubMed:10210276}.; FUNCTION: Isoform CDV-1R: May play a role in development of the testis and spermatogenesis. {ECO:0000269|PubMed:12549821}. SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000269|PubMed:19253336}. SUBUNIT: Component of the IFT complex B, at least composed of IFT20, IFT22, HSPB11/IFT25, IFT27, IFT46, IFT52, TRAF3IP1/IFT54, IFT57, IFT74, IFT81, and IFT88 (PubMed:19253336). Interacts with IFT74; the interaction is direct: within the IFT complex B, IFT74 and IFT81 mediate the transport of tubulin within the cilium. Interacts with tubulin; the interaction is direct (By similarity). Interacts with RABL2/RABL2A; binding is equal in the presence of GTP or GDP (PubMed:23055941). Interacts with IFT88 (PubMed:19253336). Interacts (via the IFT74/IFT81 heterodimer) with RABL2B (By similarity). {ECO:0000250|UniProtKB:Q8WYA0, ECO:0000269|PubMed:19253336, ECO:0000269|PubMed:23055941}. DOMAIN: The CH (calponin-homology)-like region shows high similarity to a CH (calponin-homology) domain and mediated binding to the globular domain of tubulin. {ECO:0000250}. TISSUE SPECIFICITY: Isoform CDV-1 is expressed specifically in heart and suppressed specifically in ventricles, but not in auricles, of carnitine-deficient juvenile visceral steatosis (JVS) mice. Isoform CDV-1R is expressed predominantly in the testis. Co-localizes with RABL2/RABL2A in the midpiece of elongated spermatids within the testis (at protein level). {ECO:0000269|PubMed:12549821, ECO:0000269|PubMed:23055941, ECO:0000269|PubMed:9187371}. +Q9QZ29 IGB1B_MOUSE Immunoglobulin-binding protein 1b (Alpha 4-b protein) (CD79a-binding protein 1b) (Protein alpha-4-b) 343 39,246 Chain (1) FUNCTION: Associated to surface IgM-receptor; may be involved in signal transduction (By similarity). May be involved in regulation of the catalytic activity of type 2A-related serine/threonine phosphatases. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. SUBUNIT: Associates with PP2A-alpha catalytic subunit. TISSUE SPECIFICITY: Expressed selectively in brain and testis. +Q3U4N7 IGFR1_MOUSE IGF-like family receptor 1 (Transmembrane protein 149) 345 37,172 Alternative sequence (1); Chain (1); Glycosylation (1); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 164 184 Helical. {ECO:0000255}. TOPO_DOM 21 163 Extracellular. {ECO:0000255}.; TOPO_DOM 185 345 Cytoplasmic. {ECO:0000255}. FUNCTION: Probable cell membrane receptor for the IGF-like family protein IGFL. {ECO:0000269|PubMed:21454693}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21454693}; Single-pass type I membrane protein {ECO:0000269|PubMed:21454693}. TISSUE SPECIFICITY: Ubiquitously expressed with higher expression in lymph node. Highly expressed in T-cells and monocytes. {ECO:0000269|PubMed:21454693}. +P01867 IGG2B_MOUSE Ig gamma-2B chain C region 404 44,259 Alternative sequence (2); Beta strand (25); Chain (1); Disulfide bond (8); Domain (3); Glycosylation (2); Helix (7); Natural variant (4); Non-terminal residue (1); Sequence conflict (6); Topological domain (1); Transmembrane (1); Turn (3) TRANSMEM 351 368 Helical. {ECO:0000255}. TOPO_DOM 369 404 Cytoplasmic. {ECO:0000255}. PTM: O-linked glycan consists of Gal-GalNAc disaccharide which is modified with 2 sialic acid residues. {ECO:0000269|PubMed:7512967}. SUBCELLULAR LOCATION: Isoform 1: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: Isoform 2: Secreted. +P01869 IGH1M_MOUSE Ig gamma-1 chain C region, membrane-bound form 393 43,387 Beta strand (19); Chain (1); Disulfide bond (7); Glycosylation (1); Helix (7); Non-terminal residue (1); Region (4); Topological domain (1); Transmembrane (1); Turn (1) TRANSMEM 340 357 Helical. {ECO:0000255}. TOPO_DOM 358 393 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +P01881 IGHD_MOUSE Ig delta chain C region secreted form 257 28,368 Chain (1); Disulfide bond (3); Domain (2); Glycosylation (5); Non-terminal residue (1) SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Cell lines producing IgD contain several mRNA species for Ig delta chains. In plasmacytomas, the secreted form is the major component, and the membrane-bound form is a minor component. In spleen, however, the membrane-bound form is the major component. These two forms differ in their C-terminal segments. +P01872 IGHM_MOUSE Immunoglobulin heavy constant mu [Cleaved into: Mu' chain (55 kDa mu' chain)] 454 49,972 Alternative sequence (1); Beta strand (22); Chain (2); Disulfide bond (8); Glycosylation (6); Helix (6); Mutagenesis (4); Natural variant (6); Non-terminal residue (1); Region (5); Site (1) FUNCTION: IgM antibodies play an important role in primary defense mechanisms. They have been shown to be involved in early recognition of external invaders like bacteria and viruses, cellular waste and modified self, as well as in recognition and elimination of precancerous and cancerous lesions (By similarity). {ECO:0000250}. PTM: Cleaved by a non-enzymatic process after Asn-96, yielding a glycosylated protein of 55 kDa. The process is induced by other proteins, and requires neutral or alkaline pH. {ECO:0000269|PubMed:29323348}. SUBCELLULAR LOCATION: Isoform 1: Secreted {ECO:0000305}. Note=During differentiation, B-lymphocytes switch from expression of membrane-bound IgM to secretion of IgM. {ECO:0000305}.; SUBCELLULAR LOCATION: Isoform 2: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. SUBUNIT: Immunoglobulin (Ig) molecules consist of two chains, one heavy chain (which can be alpha, delta, epsilon, gamma or mu) and one light chain (which can be kappa or lambda) each consisting of a variable and a constant region. An IgM molecule contains thus a mu heavy chain combined with either a kappa or a lambda light chains (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Mu' chain is expressed in bone marrow. {ECO:0000269|PubMed:2415657}. +Q7TQA1 IGSF1_MOUSE Immunoglobulin superfamily member 1 (IgSF1) (Inhibin-binding protein) (InhBP) 1317 147,010 Alternative sequence (6); Chain (1); Disulfide bond (8); Domain (12); Erroneous initiation (1); Glycosylation (6); Sequence conflict (1); Signal peptide (1); Topological domain (3); Transmembrane (2) TRANSMEM 500 520 Helical. {ECO:0000255}.; TRANSMEM 532 552 Helical. {ECO:0000255}. TOPO_DOM 21 499 Extracellular. {ECO:0000255}.; TOPO_DOM 521 531 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 553 1317 Extracellular. {ECO:0000255}. FUNCTION: Seems to be a coreceptor in inhibin signaling, but seems not to be a high-affinity inhibin receptor. Antagonizes activin A signaling in the presence or absence of inhibin B. Necessary to mediate a specific antagonistic effect of inhibin B on activin-stimulated transcription (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Isoform 1: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: Isoform 2: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: Isoform 3: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: Isoform 4: Secreted {ECO:0000305}.; SUBCELLULAR LOCATION: Isoform 5: Secreted {ECO:0000305}. SUBUNIT: Interacts with INHA; the interaction is not confirmed by standard receptor binding assays (By similarity). Interacts with ACVR1B; the interaction appears to be ligand-dependent as it is diminished by inhibin B and activin A. Interacts with ACVR2A, ACVR2B, ACVRL1 and BMPR1B (By similarity). Interacts with HECTD1 (By similarity). {ECO:0000250}. +P0C6B7 IGSF6_MOUSE Immunoglobulin superfamily member 6 (IgSF6) 237 26,354 Chain (1); Disulfide bond (1); Domain (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 153 173 Helical. {ECO:0000255}. TOPO_DOM 28 152 Extracellular. {ECO:0000255}.; TOPO_DOM 174 237 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Ubiquitous with higher expression in immune tissue. {ECO:0000269|PubMed:11132146}. +Q8R366 IGSF8_MOUSE Immunoglobulin superfamily member 8 (IgSF8) (CD81 partner 3) (Glu-Trp-Ile EWI motif-containing protein 2) (EWI-2) (Keratinocyte-associated transmembrane protein 4) (KCT-4) (Prostaglandin regulatory-like protein) (PGRL) (CD antigen CD316) 611 65,011 Chain (1); Disulfide bond (4); Domain (4); Glycosylation (3); Lipidation (2); Modified residue (1); Motif (1); Sequence conflict (13); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 578 598 Helical. {ECO:0000255}. TOPO_DOM 26 577 Extracellular. {ECO:0000255}.; TOPO_DOM 599 611 Cytoplasmic. {ECO:0000255}. FUNCTION: May play a key role in diverse functions ascribed to CD81 and CD9 such as oocytes fertilization or hepatitis C virus function. May regulate proliferation and differentiation of keratinocytes. May be a negative regulator of cell motility: suppresses T-cell mobility coordinately with CD81, associates with CD82 to suppress prostate cancer cell migration, regulates epidermoid cell reaggregation and motility on laminin-5 with CD9 and CD81 as key linkers. May also play a role on integrin-dependent morphology and motility functions. May participate in the regulation of neurite outgrowth and maintenance of the neural network in the adult brain. {ECO:0000269|PubMed:11673522, ECO:0000269|PubMed:16203089}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21609323}; Single-pass membrane protein {ECO:0000269|PubMed:21609323}. SUBUNIT: Interacts directly with CD82 and CD9/tetraspanin-29. Also interacts with integrin alpha-3/beta-1 and integrin alpha-4/beta-1 (By similarity). Interacts with CD81/tetraspanin-28. {ECO:0000250, ECO:0000269|PubMed:11673522}. DOMAIN: The Ig-like C2-type domains 3 and 4 are required for interaction with CD81.; DOMAIN: The short cytoplasmic domain is very basic, interacts with membrane PIPs, and mediates plasma membrane localization. TISSUE SPECIFICITY: Expressed in lymphocytes as well as in many tissues with higher expression in brain. Detected in all regions of the brain with weak expression in the pituitary. Expressed selectively by neurons but not by glial cells. {ECO:0000269|PubMed:16203089}. +Q99KB8 GLO2_MOUSE Hydroxyacylglutathione hydrolase, mitochondrial (EC 3.1.2.6) (Glyoxalase II) (Glx II) 309 34,084 Alternative sequence (1); Chain (1); Erroneous initiation (6); Metal binding (8); Modified residue (4); Region (3); Sequence conflict (6); Transit peptide (1) Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 2/2. FUNCTION: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid. SUBCELLULAR LOCATION: Isoform 1: Mitochondrion matrix {ECO:0000250|UniProtKB:Q16775}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm {ECO:0000250|UniProtKB:Q16775}. +O35659 GLP1R_MOUSE Glucagon-like peptide 1 receptor (GLP-1 receptor) (GLP-1-R) (GLP-1R) 463 53,028 Chain (1); Disulfide bond (4); Frameshift (1); Glycosylation (3); Modified residue (2); Region (1); Signal peptide (1); Site (2); Topological domain (8); Transmembrane (7) TRANSMEM 140 164 Helical; Name=1. {ECO:0000250|UniProtKB:P43220}.; TRANSMEM 176 201 Helical; Name=2. {ECO:0000250|UniProtKB:P43220}.; TRANSMEM 228 251 Helical; Name=3. {ECO:0000250|UniProtKB:P43220}.; TRANSMEM 266 290 Helical; Name=4. {ECO:0000250|UniProtKB:P43220}.; TRANSMEM 306 328 Helical; Name=5. {ECO:0000250|UniProtKB:P43220}.; TRANSMEM 349 370 Helical; Name=6. {ECO:0000250|UniProtKB:P43220}.; TRANSMEM 384 404 Helical; Name=7. {ECO:0000250|UniProtKB:P43220}. TOPO_DOM 22 139 Extracellular. {ECO:0000305}.; TOPO_DOM 165 175 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 202 227 Extracellular. {ECO:0000305}.; TOPO_DOM 252 265 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 291 305 Extracellular. {ECO:0000305}.; TOPO_DOM 329 348 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 371 383 Extracellular. {ECO:0000305}.; TOPO_DOM 405 463 Cytoplasmic. {ECO:0000305}. FUNCTION: G-protein coupled receptor for glucagon-like peptide 1 (GLP-1) (PubMed:9568699). Ligand binding triggers activation of a signaling cascade that leads to the activation of adenylyl cyclase and increased intracellular cAMP levels (By similarity). Plays a role in regulating insulin secretion in response to GLP-1 (PubMed:9568699). {ECO:0000250|UniProtKB:P43220, ECO:0000269|PubMed:9568699}. PTM: N-glycosylation enhances cell surface expression and lengthens receptor half-life by preventing degradation in the ER. {ECO:0000250|UniProtKB:P43220}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:9568699}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P43220}. SUBUNIT: May form homodimers and heterodimers with GIPR. {ECO:0000250|UniProtKB:P43220}. TISSUE SPECIFICITY: Detected in pancreatic islets (at protein level). Detected in pancreatic islets and lungs. {ECO:0000269|PubMed:9568699}. +Q5IXF8 GLP2R_MOUSE Glucagon-like peptide 2 receptor (GLP-2 receptor) (GLP-2-R) (GLP-2R) 512 59,105 Chain (1); Disulfide bond (3); Glycosylation (1); Sequence conflict (3); Topological domain (8); Transmembrane (7) TRANSMEM 136 160 Helical; Name=1. {ECO:0000250}.; TRANSMEM 173 197 Helical; Name=2. {ECO:0000250}.; TRANSMEM 224 247 Helical; Name=3. {ECO:0000250}.; TRANSMEM 262 283 Helical; Name=4. {ECO:0000250}.; TRANSMEM 302 324 Helical; Name=5. {ECO:0000250}.; TRANSMEM 349 367 Helical; Name=6. {ECO:0000250}.; TRANSMEM 380 400 Helical; Name=7. {ECO:0000250}. TOPO_DOM 1 135 Extracellular. {ECO:0000250}.; TOPO_DOM 161 172 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 198 223 Extracellular. {ECO:0000250}.; TOPO_DOM 248 261 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 284 301 Extracellular. {ECO:0000250}.; TOPO_DOM 325 348 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 368 379 Extracellular. {ECO:0000250}.; TOPO_DOM 401 512 Cytoplasmic. {ECO:0000250}. FUNCTION: This is a receptor for glucagon-like peptide 2. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q8R088 GLP3L_MOUSE Golgi phosphoprotein 3-like 285 32,906 Alternative sequence (2); Binding site (4); Chain (1); Modified residue (1); Region (1) FUNCTION: Phosphatidylinositol-4-phosphate-binding protein that may antagonize the action of GOLPH3 which is required for the process of vesicle budding at the Golgi and anterograde transport to the plasma membrane. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Phosphatidylinositol 4-phosphate (PtdIns4P)-binding mediates recruitment to Golgi membranes. {ECO:0000250}. SUBUNIT: Homooligomer. Does not interact MYO18; differs from GOLPH3 by its inability to interact with MYO18. May interact with ARF1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in a subset of tissues tested with higher expression in salivary gland, small intestine and skin (at protein level). {ECO:0000269|PubMed:23345592}. +P14220 GLPA_MOUSE Glycophorin-A (CD antigen CD235a) 168 17,664 Chain (1); Modified residue (4); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 109 131 Helical; Signal-anchor for type III membrane protein. TOPO_DOM 1 108 Extracellular.; TOPO_DOM 132 168 Cytoplasmic. FUNCTION: Glycophorin A is the major intrinsic membrane sialoglycoprotein of the erythrocyte. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved in translocation of SLC4A1 to the plasma membrane (By similarity). {ECO:0000250}. PTM: The N-terminal extracellular domain is heavily glycosylated on serine and threonine residues. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Single-pass type III membrane protein. SUBUNIT: Homodimer. {ECO:0000250}. +Q8C262 IIGP5_MOUSE Interferon-inducible GTPase 5 (EC 3.6.5.-) (Immunity-related GTPase cinema 1) 412 45,145 Chain (1); Domain (1); Modified residue (2); Nucleotide binding (3) +Q9Z1E3 IKBA_MOUSE NF-kappa-B inhibitor alpha (I-kappa-B-alpha) (IkB-alpha) (IkappaBalpha) 314 35,071 Chain (1); Cross-link (2); Modified residue (10); Motif (3); Repeat (5); Sequence conflict (2) FUNCTION: Inhibits the activity of dimeric NF-kappa-B/REL complexes by trapping REL dimers in the cytoplasm through masking of their nuclear localization signals. On cellular stimulation by immune and proinflammatory responses, becomes phosphorylated promoting ubiquitination and degradation, enabling the dimeric RELA to translocate to the nucleus and activate transcription. {ECO:0000269|PubMed:10097128, ECO:0000269|PubMed:9990853}. PTM: Phosphorylated; disables inhibition of NF-kappa-B DNA-binding activity. Phosphorylation at positions 32 and 36 is prerequisite to recognition by UBE2D3 leading to polyubiquitination and subsequent degradation (By similarity). {ECO:0000250}.; PTM: Sumoylated; sumoylation requires the presence of the nuclear import signal. Sumoylation blocks ubiquitination and proteasome-mediated degradation of the protein thereby increasing the protein stability (By similarity). {ECO:0000250}.; PTM: Monoubiquitinated at Lys-21 and/or Lys-22 by UBE2D3. Ubiquitin chain elongation is then performed by CDC34 in cooperation with the SCF(FBXW11) E3 ligase complex, building ubiquitin chains from the UBE2D3-primed NFKBIA-linked ubiquitin. The resulting polyubiquitination leads to protein degradation. Also ubiquitinated by SCF(BTRC) following stimulus-dependent phosphorylation at Ser-32 and Ser-36 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Shuttles between the nucleus and the cytoplasm by a nuclear localization signal (NLS) and a CRM1-dependent nuclear export. {ECO:0000250}. SUBUNIT: Interacts with PRMT2 (By similarity). Interacts with RELA; the interaction requires the nuclear import signal. Interacts with NKIRAS1 and NKIRAS2 (By similarity). Part of a 70-90 kDa complex at least consisting of CHUK, IKBKB, NFKBIA, RELA, ELP1 and MAP3K14 (By similarity). Interacts with RWDD3; the interaction enhances sumoylation (By similarity). Interacts (when phosphorylated at the 2 serine residues in the destruction motif D-S-G-X(2,3,4)-S) with BTRC. Associates with the SCF(BTRC) complex, composed of SKP1, CUL1 and BTRC; the association is mediated via interaction with BTRC (PubMed:10097128). Part of a SCF(BTRC)-like complex lacking CUL1, which is associated with RELA; RELA interacts directly with NFKBIA (PubMed:9990853). Interacts with PRKACA in platelets; this interaction is disrupted by thrombin and collagen (By similarity). Interacts with HIF1AN (By similarity). Interacts with MEFV (By similarity). Interacts with DDRGK1; positively regulates NFKBIA phosphorylation and degradation (By similarity). {ECO:0000250|UniProtKB:P25963, ECO:0000269|PubMed:10097128, ECO:0000269|PubMed:9859996, ECO:0000269|PubMed:9990853}. TISSUE SPECIFICITY: Highly expressed in lymph node, thymus followed by liver, brain, muscle, kidney, gastrointestinal and reproductive tract. +Q78HU7 GLPC_MOUSE Glycophorin-C (CD antigen CD236) 95 10,329 Chain (1); Modified residue (3); Topological domain (2); Transmembrane (1) TRANSMEM 26 46 Helical; Signal-anchor for type III membrane protein. {ECO:0000255}. TOPO_DOM 1 25 Extracellular. {ECO:0000255}.; TOPO_DOM 47 95 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Note=Linked to the membrane via band 4.1. {ECO:0000250}. +P18893 IL10_MOUSE Interleukin-10 (IL-10) (Cytokine synthesis inhibitory factor) (CSIF) 178 20,641 Chain (1); Disulfide bond (2); Glycosylation (2); Helix (11); Signal peptide (1); Turn (1) FUNCTION: Major immune regulatory cytokine that acts on many cells of the immune system where it has profound anti-inflammatory functions, limiting excessive tissue disruption caused by inflammation. Mechanistically, IL10 binds to its heterotetrameric receptor comprising IL10RA and IL10RB leading to JAK1 and STAT2-mediated phosphorylation of STAT3. In turn, STAT3 translocates to the nucleus where it drives expression of anti-inflammatory mediators. Targets antigen-presenting cells (APCs) such as macrophages and monocytes and inhibits their release of pro-inflammatory cytokines including granulocyte-macrophage colony-stimulating factor /GM-CSF, granulocyte colony-stimulating factor/G-CSF, IL-1 alpha, IL-1 beta, IL-6, IL-8 and TNF-alpha. Interferes also with antigen presentation by reducing the expression of MHC-class II and co-stimulatory molecules, thereby inhibiting their ability to induce T cell activation (By similarity). In addition, controls the inflammatory response of macrophages by reprogramming essential metabolic pathways including mTOR signaling (By similarity) (PubMed:28473584). {ECO:0000250|UniProtKB:P22301, ECO:0000269|PubMed:28473584}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P22301}. SUBUNIT: Homodimer. Interacts with IL10RA and IL10RB. {ECO:0000250|UniProtKB:P22301}. +P43432 IL12B_MOUSE Interleukin-12 subunit beta (IL-12B) (Cytotoxic lymphocyte maturation factor 40 kDa subunit) (CLMF p40) (IL-12 subunit p40) 335 38,235 Chain (1); Compositional bias (1); Disulfide bond (2); Domain (2); Glycosylation (4); Natural variant (2); Signal peptide (1) FUNCTION: Cytokine that can act as a growth factor for activated T and NK cells, enhance the lytic activity of NK/lymphokine-activated killer cells, and stimulate the production of IFN-gamma by resting PBMC. {ECO:0000250}.; FUNCTION: Associates with IL23A to form the IL-23 interleukin, a heterodimeric cytokine which functions in innate and adaptive immunity. IL-23 may constitute with IL-17 an acute response to infection in peripheral tissues. IL-23 binds to a heterodimeric receptor complex composed of IL12RB1 and IL23R, activates the Jak-Stat signaling cascade, stimulates memory rather than naive T-cells and promotes production of proinflammatory cytokines. IL-23 induces autoimmune inflammation and thus may be responsible for autoimmune inflammatory diseases and may be important for tumorigenesis. {ECO:0000269|PubMed:11114383}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Heterodimer with IL12A; disulfide-linked. The heterodimer is known as interleukin IL-12. Heterodimer with IL23A; disulfide-linked. The heterodimer is known as interleukin IL-23. Also secreted as a monomer. +P48346 IL15_MOUSE Interleukin-15 (IL-15) 162 18,593 Beta strand (2); Chain (1); Disulfide bond (2); Glycosylation (3); Helix (7); Propeptide (1); Signal peptide (1) FUNCTION: Cytokine that stimulates the proliferation of T-lymphocytes. Stimulation by IL-15 requires interaction of IL-15 with components of IL-2R, including IL-2R beta and probably IL-2R gamma but not IL-2R alpha. SUBCELLULAR LOCATION: Secreted. +O54824 IL16_MOUSE Pro-interleukin-16 [Cleaved into: Interleukin-16 (IL-16) (Lymphocyte chemoattractant factor) (LCF)] 1322 141,435 Alternative sequence (1); Chain (2); Domain (4); Modified residue (1); Region (2); Sequence conflict (6) FUNCTION: Interleukin-16 stimulates a migratory response in CD4+ lymphocytes, monocytes, and eosinophils. Primes CD4+ T-cells for IL-2 and IL-15 responsiveness. Also induces T-lymphocyte expression of interleukin 2 receptor. Ligand for CD4.; FUNCTION: Isoform 1 may act as a scaffolding protein that anchors ion channels in the membrane.; FUNCTION: Isoform 2 is involved in cell cycle progression in T-cells. Appears to be involved in transcriptional regulation of SKP2 and is probably part of a transcriptional repression complex on the core promoter of the SKP2 gene. May act as a scaffold for GABPB1 (the DNA-binding subunit the GABP transcription factor complex) and HDAC3 thus maintaining transcriptional repression and blocking cell cycle progression in resting T-cells. PTM: Synthesized as a chemo-attractant inactive precursor which is proteolytically cleaved by caspase-3 to yield IL-16. {ECO:0000269|PubMed:10479680}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 1: Cytoplasm {ECO:0000269|PubMed:10479680}. Note=Colocalizes with GRIN2C in neuronal cell bodies and neurites.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Nucleus {ECO:0000250}. SUBUNIT: Homotetramer (Probable). Isoform 2 interacts with GRIN2A. Isoform 1 interacts with GRIN2D, KCNJ10, KCNJ15 and CACNA1C. Isoform 2 interacts (via PDZ 3 domain) with PPP1R12A, PPP1R12B and PPP1R12C. Isoform 1 interacts with PPP1R12B. Isoform 3 interacts with GABPB1. Isoform 2 interacts (via PDZ 3 domain) with HDAC3 (By similarity). {ECO:0000250, ECO:0000305}. TISSUE SPECIFICITY: Isoform 1 is expressed in neurons of the cerebellum and hippocampus. Isoform 2 is expressed in thymus, spleen and lung. +Q9QXT6 IL17B_MOUSE Interleukin-17B (IL-17B) (Cytokine CX1) (Cytokine-like protein ZCYTO7) (Neuronal interleukin-17-related factor) 180 20,309 Chain (1); Disulfide bond (2); Glycosylation (1); Sequence conflict (5); Signal peptide (1) FUNCTION: Stimulates the release of tumor necrosis factor alpha and IL-1-beta from the monocytic cell line THP-1. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. +Q8K4C5 IL17C_MOUSE Interleukin-17C (Il-17c) (Cytokine CX2) 194 21,592 Chain (1); Disulfide bond (2); Erroneous initiation (1); Signal peptide (1) FUNCTION: Cytokine that plays a crucial role in innate immunity of the epithelium, including to intestinal bacterial pathogens, in an autocrine manner. Stimulates the production of antibacterial peptides and proinflammatory molecules for host defense by signaling through the NFKB and MAPK pathways. Acts synergically with IL22, TNF and IL1B in inducing antibacterial peptides. May have protective function by maintaining epithelial homeostasis after an inflammatory challenge, such as that caused in the intestine by dextran sulfate sodium in a colitis model. May also promote an inflammatory phenotype, such as skin in a psoriasis model. Enhanced IL17C/IL17RE signaling may also lead to greater susceptibility to autoimmune diseases, such as autoimmune encephalitis. {ECO:0000269|PubMed:21982598, ECO:0000269|PubMed:21993848, ECO:0000269|PubMed:21993849}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. SUBUNIT: Binds to a heterodimer formed by IL17RA and IL17RE. TISSUE SPECIFICITY: Expressed by epithelial cells after bacterial challenge. Low expression, if any, in lymphocytes. {ECO:0000269|PubMed:21993848}. +Q7TNI7 IL17F_MOUSE Interleukin-17F (IL-17F) 161 17,941 Alternative sequence (1); Chain (1); Disulfide bond (4); Glycosylation (1); Signal peptide (1) FUNCTION: Ligand for IL17RA and IL17RC (PubMed:17911633). The heterodimer formed by IL17A and IL17F is a ligand for the heterodimeric complex formed by IL17RA and IL17RC (By similarity). Involved in stimulating the production of other cytokines such as IL6, IL8 and CSF2, and in regulation of cartilage matrix turnover. Also involved in stimulating the proliferation of peripheral blood mononuclear cells and T-cells and in inhibition of angiogenesis (By similarity). Plays a role in the induction of neutrophilia in the lungs and in the exacerbation of antigen-induced pulmonary allergic inflammation (PubMed:15477493). {ECO:0000250|UniProtKB:Q96PD4, ECO:0000269|PubMed:15477493, ECO:0000269|PubMed:17911633}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Homodimer; disulfide-linked. Heterodimer with IL17A. {ECO:0000250|UniProtKB:Q96PD4}. TISSUE SPECIFICITY: Expressed by a subset of activated T-cells in the lamina propria. {ECO:0000269|PubMed:16990136}. +Q62386 IL17_MOUSE Interleukin-17A (IL-17) (IL-17A) (Cytotoxic T-lymphocyte-associated antigen 8) (CTLA-8) 158 17,490 Chain (1); Disulfide bond (2); Glycosylation (1); Signal peptide (1) FUNCTION: Ligand for IL17RA (PubMed:17911633). The heterodimer formed by IL17A and IL17F is a ligand for the heterodimeric complex formed by IL17RA and IL17RC (By similarity). Involved in inducing stromal cells to produce proinflammatory and hematopoietic cytokines (By similarity). {ECO:0000250|UniProtKB:Q16552, ECO:0000269|PubMed:17911633}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Homodimer. Heterodimer with IL17F. {ECO:0000250|UniProtKB:Q16552}. TISSUE SPECIFICITY: Restricted to a subset of activated T-cells. {ECO:0000269|PubMed:16990136}. +P01582 IL1A_MOUSE Interleukin-1 alpha (IL-1 alpha) 270 31,023 Chain (1); Glycosylation (3); Modified residue (1); Propeptide (1) FUNCTION: Produced by activated macrophages, IL-1 stimulates thymocyte proliferation by inducing IL-2 release, B-cell maturation and proliferation, and fibroblast growth factor activity. IL-1 proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin and collagenase from synovial cells. SUBCELLULAR LOCATION: Secreted. Note=The lack of a specific hydrophobic segment in the precursor sequence suggests that IL-1 is released by damaged cells or is secreted by a mechanism differing from that used for other secretory proteins. SUBUNIT: Monomer. DOMAIN: The similarity among the IL-1 precursors suggests that the amino ends of these proteins serve some as yet undefined function. +Q9WU65 GLPK2_MOUSE Glycerol kinase 2 (GK 2) (Glycerokinase 2) (EC 2.7.1.30) (ATP:glycerol 3-phosphotransferase 2) (Glycerol kinase, testis specific 2) 554 60,630 Binding site (7); Chain (1); Nucleotide binding (1) Polyol metabolism; glycerol degradation via glycerol kinase pathway; sn-glycerol 3-phosphate from glycerol: step 1/1. FUNCTION: Key enzyme in the regulation of glycerol uptake and metabolism. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=In sperm the majority of the enzyme is bound to mitochondria. {ECO:0000250}. +P25085 IL1RA_MOUSE Interleukin-1 receptor antagonist protein (IL-1RN) (IL-1ra) (IRAP) (IL1 inhibitor) 178 20,274 Alternative sequence (1); Chain (1); Disulfide bond (1); Glycosylation (1); Signal peptide (1) FUNCTION: Inhibits the activity of interleukin-1 by binding to receptor IL1R1 and preventing its association with the coreceptor IL1RAP for signaling. Has no interleukin-1 like activity. SUBCELLULAR LOCATION: Isoform 1: Secreted.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. +Q9JKV9 IL20_MOUSE Interleukin-20 (IL-20) (Cytokine Zcyto10) 176 20,098 Chain (1); Disulfide bond (3); Signal peptide (1) FUNCTION: Cytokine that may be involved in epidermal function and psoriasis. Acts through STAT3. SUBCELLULAR LOCATION: Secreted. +O35228 IL27B_MOUSE Interleukin-27 subunit beta (IL-27 subunit beta) (IL-27B) (Epstein-Barr virus-induced gene 3 protein homolog) 228 25,353 Chain (1); Domain (2); Glycosylation (2); Signal peptide (1) FUNCTION: Associates with IL27 to form the IL-27 interleukin, a heterodimeric cytokine which functions in innate immunity. IL-27 has pro- and anti-inflammatory properties, that can regulate T-helper cell development, suppress T-cell proliferation, stimulate cytotoxic T-cell activity, induce isotype switching in B-cells, and that has diverse effects on innate immune cells. Among its target cells are CD4 T-helper cells which can differentiate in type 1 effector cells (TH1), type 2 effector cells (TH2) and IL17 producing helper T-cells (TH17). It drives rapid clonal expansion of naive but not memory CD4 T-cells. It also strongly synergizes with IL-12 to trigger interferon-gamma/IFN-gamma production of naive CD4 T-cells, binds to the cytokine receptor WSX-1/TCCR. Another important role of IL-27 is its antitumor activity as well as its antiangiogenic activity with activation of production of antiangiogenic chemokines. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q14213}. SUBUNIT: Heterodimer with IL27/IL27A; not disulfide-linked. This heterodimer is known as interleukin IL-27. Heterodimer with IL12A; not disulfide-linked. This heterodimer is known as interleukin IL-35. Interacts with SQSTM1. {ECO:0000250|UniProtKB:Q14213}. +P01590 IL2RA_MOUSE Interleukin-2 receptor subunit alpha (IL-2 receptor subunit alpha) (IL-2-RA) (IL-2R subunit alpha) (IL2-RA) (p55) (CD antigen CD25) 268 30,723 Chain (1); Disulfide bond (5); Domain (2); Glycosylation (3); Sequence conflict (6); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 237 257 Helical. {ECO:0000255}. TOPO_DOM 22 236 Extracellular. {ECO:0000255}.; TOPO_DOM 258 268 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for interleukin-2. The receptor is involved in the regulation of immune tolerance by controlling regulatory T cells (TREGs) activity. TREGs suppress the activation and expansion of autoreactive T-cells. {ECO:0000250|UniProtKB:P01589}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Non-covalent dimer of an alpha and a beta subunit. IL2R exists in 3 different forms: a high affinity dimer, an intermediate affinity monomer (beta subunit), and a low affinity monomer (alpha subunit). The high and intermediate affinity forms also associate with a gamma subunit. +P16297 IL2RB_MOUSE Interleukin-2 receptor subunit beta (IL-2 receptor subunit beta) (IL-2R subunit beta) (IL-2RB) (High affinity IL-2 receptor subunit beta) (p70-75) (CD antigen CD122) 539 60,539 Chain (1); Disulfide bond (2); Domain (1); Glycosylation (6); Motif (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 241 268 Helical. {ECO:0000255}. TOPO_DOM 27 240 Extracellular. {ECO:0000255}.; TOPO_DOM 269 539 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for interleukin-2. This beta subunit is involved in receptor mediated endocytosis and transduces the mitogenic signals of IL2. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Non-covalent dimer of an alpha and a beta subunit. IL2R exists in 3 different forms: a high affinity dimer, an intermediate affinity monomer (beta subunit), and a low affinity monomer (alpha subunit). The high and intermediate affinity forms also associate with a gamma subunit. Interacts with SHB upon interleukin stimulation (By similarity). {ECO:0000250}. DOMAIN: The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.; DOMAIN: The box 1 motif is required for JAK interaction and/or activation. +Q61606 GLR_MOUSE Glucagon receptor (GL-R) 485 54,929 Chain (1); Disulfide bond (4); Glycosylation (5); Modified residue (2); Region (1); Sequence conflict (5); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 138 162 Helical; Name=1. {ECO:0000250|UniProtKB:P47871}.; TRANSMEM 175 199 Helical; Name=2. {ECO:0000250|UniProtKB:P47871}.; TRANSMEM 227 250 Helical; Name=3. {ECO:0000250|UniProtKB:P47871}.; TRANSMEM 265 286 Helical; Name=4. {ECO:0000250|UniProtKB:P47871}.; TRANSMEM 305 327 Helical; Name=5. {ECO:0000250|UniProtKB:P47871}.; TRANSMEM 352 370 Helical; Name=6. {ECO:0000250|UniProtKB:P47871}.; TRANSMEM 383 403 Helical; Name=7. {ECO:0000250|UniProtKB:P47871}. TOPO_DOM 27 137 Extracellular. {ECO:0000250|UniProtKB:P47871}.; TOPO_DOM 163 174 Cytoplasmic. {ECO:0000250|UniProtKB:P47871}.; TOPO_DOM 200 226 Extracellular. {ECO:0000250|UniProtKB:P47871}.; TOPO_DOM 251 264 Cytoplasmic. {ECO:0000250|UniProtKB:P47871}.; TOPO_DOM 287 304 Extracellular. {ECO:0000250|UniProtKB:P47871}.; TOPO_DOM 328 351 Cytoplasmic. {ECO:0000250|UniProtKB:P47871}.; TOPO_DOM 371 382 Extracellular. {ECO:0000250|UniProtKB:P47871}.; TOPO_DOM 404 485 Cytoplasmic. {ECO:0000250|UniProtKB:P47871}. FUNCTION: G-protein coupled receptor for glucagon that plays a central role in the regulation of blood glucose levels and glucose homeostasis. Regulates the rate of hepatic glucose production by promoting glycogen hydrolysis and gluconeogenesis. Plays an important role in mediating the responses to fasting. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Promotes activation of adenylate cyclase. Besides, plays a role in signaling via a phosphatidylinositol-calcium second messenger system. {ECO:0000269|PubMed:12552113, ECO:0000269|PubMed:19046568}. PTM: Ligand-binding promotes phosphorylation of serine residues in the C-terminal cytoplasmic domain. Phosphorylation is important for receptor endocytosis after ligand-binding (By similarity). {ECO:0000250|UniProtKB:P47871}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12552113}; Multi-pass membrane protein {ECO:0000269|PubMed:12552113}. Note=Is rapidly internalized after ligand-binding. {ECO:0000250|UniProtKB:P47871}. TISSUE SPECIFICITY: Expressed predominantly in liver, kidney, adrenal, lung and stomach, while lower levels of expression are detected in brown and white adipose tissue, cerebellum, duodenum and heart. {ECO:0000269|PubMed:7590348}. +Q9CQM9 GLRX3_MOUSE Glutaredoxin-3 (PKC-interacting cousin of thioredoxin) (PICOT) (PKC-theta-interacting protein) (PKCq-interacting protein) (Thioredoxin-like protein 2) 337 37,778 Beta strand (4); Chain (1); Domain (3); Helix (5); Initiator methionine (1); Metal binding (2); Modified residue (2); Sequence conflict (1); Turn (1) FUNCTION: Together with BOLA2, acts as a cytosolic iron-sulfur (Fe-S) cluster assembly factor that facilitates [2Fe-2S] cluster insertion into a subset of cytosolic proteins (By similarity). Acts as a critical negative regulator of cardiac hypertrophy and a positive inotropic regulator (PubMed:16809552, PubMed:18258855, PubMed:18929570). Required for hemoglobin maturation. Does not possess any thyoredoxin activity since it lacks the conserved motif that is essential for catalytic activity (By similarity). {ECO:0000250|UniProtKB:O76003, ECO:0000269|PubMed:16809552, ECO:0000269|PubMed:18258855, ECO:0000269|PubMed:18929570}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:O76003}. Cytoplasm, cell cortex {ECO:0000269|PubMed:18258855}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:18258855}. Note=Under the plasma membrane (PubMed:18258855). After PMA stimulation, GLRX3 and PRKCQ/PKC-theta translocate to a more extended submembrane area (PubMed:18258855). In the Z line, found associated with CSRP3 (PubMed:18258855). {ECO:0000269|PubMed:18258855}. SUBUNIT: Homodimer; the homodimer is independent of 2Fe-2S clusters. Heterotrimer; forms a heterotrimeric complex composed by two BOLA2 molecules and one GLRX3 molecule; linked by [2Fe-2S] clusters. Interacts (via N-terminus) with PRKCQ/PKC-theta (By similarity). Interacts (via C-terminus) with CSRP3 (PubMed:18258855). Interacts with CSRP2 (PubMed:18258855). {ECO:0000250|UniProtKB:O76003, ECO:0000269|PubMed:18258855}. DOMAIN: The thioredoxin domain lacks the two redox-active cysteines. This strongly suggests that it lacks thioredoxin activity. {ECO:0000305}. +P26954 IL3B2_MOUSE Interleukin-3 receptor class 2 subunit beta (IL-3 receptor class 2 subunit beta) (IL-3R class 2 subunit beta) (Colony-stimulating factor 2 receptor subunit beta-2) (Interleukin-3 receptor class II beta chain) 878 97,195 Beta strand (28); Chain (1); Compositional bias (2); Disulfide bond (4); Domain (2); Glycosylation (2); Helix (4); Modified residue (3); Motif (2); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 441 462 Helical. {ECO:0000255}. TOPO_DOM 23 440 Extracellular. {ECO:0000255}.; TOPO_DOM 463 878 Cytoplasmic. {ECO:0000255}. FUNCTION: In mouse, there are two classes of high-affinity IL3 receptors. One contains this IL3-specific beta subunit and the other contains the beta subunit also shared by high-affinity IL5 and GM-CSF receptors. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Heterodimer of an alpha and a beta subunit. DOMAIN: The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.; DOMAIN: The box 1 motif is required for JAK interaction and/or activation. +Q6P9S7 GLT10_MOUSE Polypeptide N-acetylgalactosaminyltransferase 10 (EC 2.4.1.41) (Polypeptide GalNAc transferase 10) (GalNAc-T10) (pp-GaNTase 10) (Protein-UDP acetylgalactosaminyltransferase 10) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10) 603 69,116 Binding site (6); Chain (1); Disulfide bond (5); Domain (1); Erroneous initiation (2); Glycosylation (3); Metal binding (3); Region (3); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 12 31 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 11 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 32 603 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has activity toward Muc5Ac and EA2 peptide substrates (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. DOMAIN: There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding. {ECO:0000250}.; DOMAIN: The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity. {ECO:0000250}. TISSUE SPECIFICITY: Expressed at higher level than GALNT9. In the developing hindbrain region of E14.5 embryos it accumulates in the rapidly dividing, undifferentiated ventricular zone adjacent to the pons. It also accumulates in the regions immediately rostral and caudal to the dorsal rhombic lips differentiating into the cerebellum. Not expressed in the developing choroid plexus. {ECO:0000269|PubMed:11278534}. +Q9CX63 IL40_MOUSE Protein IL-40 (Interleukin-40) (IL-40) 252 26,851 Chain (1); Glycosylation (2); Signal peptide (1) FUNCTION: Probable B cell-associated cytokine that plays a role in the regulation of humoral immune responses (PubMed:28978694). Involved in lymphocyte B cell development and immunoglobulin/IgA production (PubMed:28978694). {ECO:0000269|PubMed:28978694}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q6UX52}. TISSUE SPECIFICITY: Expressed in bone marrow, spleen and lymph node (PubMed:28978694). {ECO:0000269|PubMed:28978694}. +P16382 IL4RA_MOUSE Interleukin-4 receptor subunit alpha (IL-4 receptor subunit alpha) (IL-4R subunit alpha) (IL-4R-alpha) (IL-4RA) (CD antigen CD124) [Cleaved into: Soluble interleukin-4 receptor subunit alpha (Soluble IL-4 receptor subunit alpha) (Soluble IL-4R-alpha) (sIL4Ralpha/prot) (IL-4-binding protein) (IL4-BP)] 810 87,627 Alternative sequence (3); Chain (2); Compositional bias (2); Disulfide bond (2); Domain (1); Glycosylation (4); Modified residue (5); Motif (3); Natural variant (8); Region (2); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 234 257 Helical. {ECO:0000255}. TOPO_DOM 26 233 Extracellular. {ECO:0000255}.; TOPO_DOM 258 810 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for both interleukin 4 and interleukin 13. Couples to the JAK1/2/3-STAT6 pathway. The IL4 response is involved in promoting Th2 differentiation. The IL4/IL13 responses are involved in regulating IgE production and, chemokine and mucus production at sites of allergic inflammation. In certain cell types, can signal through activation of insulin receptor substrates, IRS1/IRS2. PTM: On IL4 binding, phosphorylated on C-terminal tyrosine residues. {ECO:0000250|UniProtKB:P24394}.; PTM: Soluble IL4R can also be produced by proteolytic cleavage at the cell surface (shedding). {ECO:0000269|PubMed:8757301}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Isoform 2: Secreted. SUBUNIT: The functional IL4 receptor is formed by initial binding of IL4 to IL4R. Subsequent recruitment to the complex of the common gamma chain, in immune cells, creates a type I receptor and, in non-immune cells, of IL13RA1 forms a type II receptor. IL4R can also interact with the IL13/IL13RA1 complex to form a similar type II receptor. Interacts with the SH2-containing phosphatases, PTPN6/SHIP1, PTPN11/SHIP2 and INPP5D/SHIP. Interacts with JAK3 (By similarity). Interacts with PIK3C3 (PubMed:8390454). Interacts with JAK1 through a Box 1-containing region; inhibited by SOCS5 (PubMed:12242343). Interacts with SOCS5; inhibits IL4 signaling (PubMed:12242343). Interacts with CLM1 (PubMed:26124135). {ECO:0000250|UniProtKB:P24394, ECO:0000269|PubMed:12242343, ECO:0000269|PubMed:26124135, ECO:0000269|PubMed:8390454}. DOMAIN: The extracellular domain represents the IL4 binding protein (IL4BP). {ECO:0000250}.; DOMAIN: The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.; DOMAIN: The box 1 motif is required for JAK interaction and/or activation.; DOMAIN: Contains 1 copy of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is involved in modulation of cellular responses. The phosphorylated ITIM motif can bind the SH2 domain of several SH2-containing phosphatases. TISSUE SPECIFICITY: Expressed in both Th1 and Th2 cells. +Q8BGT9 GLT12_MOUSE Polypeptide N-acetylgalactosaminyltransferase 12 (EC 2.4.1.41) (Polypeptide GalNAc transferase 12) (GalNAc-T12) (pp-GaNTase 12) (Protein-UDP acetylgalactosaminyltransferase 12) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 12) 576 66,541 Binding site (4); Chain (1); Disulfide bond (5); Domain (1); Metal binding (3); Region (2); Topological domain (2); Transmembrane (1) TRANSMEM 20 37 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 19 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 38 576 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has activity toward non-glycosylated peptides such as Muc5AC, Muc1a and EA2, and no detectable activity with Muc2 and Muc7. Displays enzymatic activity toward the Gal-NAc-Muc5AC glycopeptide, but no detectable activity to mono-GalNAc-glycosylated Muc1a, Muc2, Muc7 and EA2. May play an important role in the initial step of mucin-type oligosaccharide biosynthesis in digestive organs (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. DOMAIN: There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding. {ECO:0000250}.; DOMAIN: The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity. {ECO:0000250}. +Q8BVG5 GLT14_MOUSE Polypeptide N-acetylgalactosaminyltransferase 14 (EC 2.4.1.41) (Polypeptide GalNAc transferase 14) (GalNAc-T14) (pp-GaNTase 14) (Protein-UDP acetylgalactosaminyltransferase 14) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 14) 550 63,989 Alternative sequence (2); Binding site (7); Chain (1); Disulfide bond (5); Domain (1); Metal binding (3); Region (2); Sequence conflict (5); Topological domain (2); Transmembrane (1) TRANSMEM 7 26 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 27 550 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Displays activity toward mucin-derived peptide substrates such as Muc2, Muc5AC, Muc7, and Muc13 (-58). May be involved in O-glycosylation in kidney (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. DOMAIN: There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding. {ECO:0000250}.; DOMAIN: The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity. {ECO:0000250}. +Q9D4M9 GLTL5_MOUSE Inactive polypeptide N-acetylgalactosaminyltransferase-like protein 5 (Polypeptide GalNAc transferase 15) (GalNAc-T15) (pp-GaNTase 15) (Protein-UDP acetylgalactosaminyltransferase 15) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 15) 431 49,874 Chain (1); Disulfide bond (2); Glycosylation (3); Region (2); Sequence caution (1); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 5 27 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 4 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 28 431 Lumenal. {ECO:0000255}. FUNCTION: Probable inactive glycosyltransferase required during spermatid development. May participate in protein loading into the acrosomes and accumulation of ubiquitin-proteasome systems around the head-tail coupling apparatus region. {ECO:0000269|PubMed:24398516}. SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Note=Localizes to the juxtanuclear region, possibly the late endosome. Not localized in the Golgi apparatus in round spermatids (PubMed:24398516). {ECO:0000269|PubMed:24398516}. DOMAIN: There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in testis. Mainly expressed in the round and elongated spermatids during spermiogenesis, not in the outermost cells of the seminiferous tubules, which contain spermatogonia and somatic Sertoli cells. Present in the juxtanuclear space in the round spermatids, not in the acrosomal vesicles. In the elongating spermatids, localizes strongly in the acroplaxome, the region between the developing acrosome and nucleus. During differentiation, also weakly detected in the transient manchette containing microtubules. In epididymal spermatozoa, weakly detected in the midpiece, but concentrates mainly in the neck region around the head-tail coupling apparatus (at protein level). {ECO:0000269|PubMed:24398516}. +P14142 GLUT4_MOUSE Solute carrier family 2, facilitated glucose transporter member 4 (GT2) (Glucose transporter type 4, insulin-responsive) (GLUT-4) 509 54,755 Binding site (2); Chain (1); Glycosylation (1); Modified residue (4); Motif (1); Region (2); Sequence conflict (6); Topological domain (13); Transmembrane (12) TRANSMEM 24 44 Helical; Name=1. {ECO:0000255}.; TRANSMEM 81 101 Helical; Name=2. {ECO:0000255}.; TRANSMEM 111 131 Helical; Name=3. {ECO:0000255}.; TRANSMEM 142 162 Helical; Name=4. {ECO:0000255}.; TRANSMEM 171 191 Helical; Name=5. {ECO:0000255}.; TRANSMEM 201 221 Helical; Name=6. {ECO:0000255}.; TRANSMEM 287 307 Helical; Name=7. {ECO:0000255}.; TRANSMEM 323 343 Helical; Name=8. {ECO:0000255}.; TRANSMEM 353 373 Helical; Name=9. {ECO:0000255}.; TRANSMEM 385 405 Helical; Name=10. {ECO:0000255}.; TRANSMEM 417 437 Helical; Name=11. {ECO:0000255}.; TRANSMEM 445 465 Helical; Name=12. {ECO:0000255}. TOPO_DOM 1 23 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 45 80 Extracellular. {ECO:0000255}.; TOPO_DOM 102 110 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 132 141 Extracellular. {ECO:0000255}.; TOPO_DOM 163 170 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 192 200 Extracellular. {ECO:0000255}.; TOPO_DOM 222 286 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 308 322 Extracellular. {ECO:0000255}.; TOPO_DOM 344 352 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 374 384 Extracellular. {ECO:0000255}.; TOPO_DOM 406 416 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 438 444 Extracellular. {ECO:0000255}.; TOPO_DOM 466 508 Cytoplasmic. {ECO:0000255}. FUNCTION: Insulin-regulated facilitative glucose transporter. {ECO:0000305|PubMed:26240143, ECO:0000305|PubMed:26629404}. PTM: Sumoylated. {ECO:0000250|UniProtKB:P14672}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21907143, ECO:0000269|PubMed:25586176, ECO:0000269|PubMed:26240143, ECO:0000269|PubMed:26629404, ECO:0000269|PubMed:27739494}; Multi-pass membrane protein {ECO:0000269|PubMed:21907143}. Endomembrane system {ECO:0000269|PubMed:26240143, ECO:0000269|PubMed:26629404}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:26240143, ECO:0000269|PubMed:26629404, ECO:0000269|PubMed:27354378}. Note=Localizes primarily to the perinuclear region, undergoing continued recycling to the plasma membrane where it is rapidly reinternalized (PubMed:26629404, PubMed:26240143, PubMed:27354378). The dileucine internalization motif is critical for intracellular sequestration (By similarity) (PubMed:26240143, PubMed:26629404). Insulin stimulation induces translocation to the cell membrane (PubMed:27739494). {ECO:0000250|UniProtKB:P14672, ECO:0000269|PubMed:26240143, ECO:0000269|PubMed:26629404, ECO:0000269|PubMed:27354378, ECO:0000269|PubMed:27739494}. SUBUNIT: Binds to DAXX (By similarity). Interacts via its N-terminus with SRFBP1 (By similarity). Interacts with NDUFA9 (By similarity). Interacts with TRARG1; the interaction is required for proper SLC2A4 reacycling after insulin stimulation (PubMed:26629404). {ECO:0000250|UniProtKB:P14672, ECO:0000250|UniProtKB:P19357, ECO:0000269|PubMed:26629404}. DOMAIN: The dileucine internalization motif is critical for intracellular sequestration. {ECO:0000250|UniProtKB:P14672}. TISSUE SPECIFICITY: Expressed in skeletal and cardiac muscles (PubMed:2654938, PubMed:26240143). Expressed in brown and white adipose tissues (PubMed:2654938, PubMed:26240143). {ECO:0000269|PubMed:26240143, ECO:0000269|PubMed:2654938}. DISEASE: Note=Defects in Slc2a4 may be the cause of certain post-receptor defects in non-insulin-dependent diabetes mellitus (NIDDM). +Q8CB44 GRAM4_MOUSE GRAM domain-containing protein 4 (Death-inducing protein) 633 72,264 Chain (1); Coiled coil (1); Domain (1); Erroneous initiation (1); Modified residue (2); Sequence caution (1); Transmembrane (3) TRANSMEM 295 315 Helical. {ECO:0000255}.; TRANSMEM 389 409 Helical. {ECO:0000255}.; TRANSMEM 411 431 Helical. {ECO:0000255}. FUNCTION: Plays a role as a mediator of E2F1-induced apoptosis in the absence of p53/TP53. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Colocalizes with COX4I1. {ECO:0000250}. +P30731 GPR83_MOUSE Probable G-protein coupled receptor 83 (Glucocorticoid-induced receptor) 423 48,137 Alternative sequence (3); Chain (1); Disulfide bond (1); Glycosylation (3); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 72 92 Helical; Name=1. {ECO:0000255}.; TRANSMEM 108 129 Helical; Name=2. {ECO:0000255}.; TRANSMEM 146 167 Helical; Name=3. {ECO:0000255}.; TRANSMEM 187 208 Helical; Name=4. {ECO:0000255}.; TRANSMEM 239 260 Helical; Name=5. {ECO:0000255}.; TRANSMEM 294 315 Helical; Name=6. {ECO:0000255}.; TRANSMEM 328 348 Helical; Name=7. {ECO:0000255}. TOPO_DOM 18 71 Extracellular. {ECO:0000255}.; TOPO_DOM 93 107 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 130 145 Extracellular. {ECO:0000255}.; TOPO_DOM 168 186 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 209 238 Extracellular. {ECO:0000255}.; TOPO_DOM 261 293 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 316 327 Extracellular. {ECO:0000255}.; TOPO_DOM 349 423 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan receptor. Could be a neuropeptide Y receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Brain, thymus and spleen. +P30115 GSTA3_MOUSE Glutathione S-transferase A3 (EC 2.5.1.18) (GST class-alpha member 3) (Glutathione S-transferase Ya3) (Glutathione S-transferase Yc) 221 25,361 Binding site (2); Chain (1); Domain (2); Initiator methionine (1); Mass spectrometry (1); Modified residue (2); Region (2) FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. This GST has a high catalytic activity for aflatoxin B1-8,9 epoxide. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Homodimer. +P31315 GSX1_MOUSE GS homeobox 1 (Homeobox protein GSH-1) 261 27,728 Chain (1); Compositional bias (1); DNA binding (1); Region (1) FUNCTION: Probable transcription factor that binds to the DNA sequence 5'-GC[TA][AC]ATTA[GA]-3'. Activates the transcription of the GHRH gene. Plays an important role in pituitary development. {ECO:0000269|PubMed:8631293}. SUBCELLULAR LOCATION: Nucleus. +Q9ESZ8 GTF2I_MOUSE General transcription factor II-I (GTFII-I) (TFII-I) (Bruton tyrosine kinase-associated protein 135) (BAP-135) (BTK-associated protein 135) 998 112,265 Alternative sequence (4); Beta strand (2); Chain (1); Compositional bias (1); Cross-link (34); Erroneous initiation (1); Helix (5); Initiator methionine (1); Modified residue (22); Motif (1); Repeat (6); Sequence conflict (17); Turn (3) FUNCTION: Interacts with the basal transcription machinery by coordinating the formation of a multiprotein complex at the C-FOS promoter, and linking specific signal responsive activator complexes. Promotes the formation of stable high-order complexes of SRF and PHOX1 and interacts cooperatively with PHOX1 to promote serum-inducible transcription of a reporter gene deriven by the C-FOS serum response element (SRE). Acts as a coregulator for USF1 by binding independently two promoter elements, a pyrimidine-rich initiator (Inr) and an upstream E-box (By similarity). Required for the formation of functional ARID3A DNA-binding complexes and for activation of immunoglobulin heavy-chain transcription upon B-lymphocyte activation. {ECO:0000250, ECO:0000269|PubMed:16738337}. PTM: Transiently phosphorylated on tyrosine residues by BTK in response to B-cell receptor stimulation. Phosphorylation on Tyr-248 and Tyr-398, and perhaps, on Tyr-503 contributes to BTK-mediated transcriptional activation (By similarity). {ECO:0000250}.; PTM: Sumoylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Colocalizes with BTK in the cytoplasm. {ECO:0000250}. SUBUNIT: Homodimer (Potential). Interacts with SRF and PHOX1. Binds a pyrimidine-rich initiator (Inr) and a recognition site (E-box) for upstream stimulatory factor 1 (USF1). Associates with the PH domain of Bruton's tyrosine kinase (BTK) (By similarity). May be a component of a BHC histone deacetylase complex that contains HDAC1, HDAC2, HMG20B/BRAF35, KDM1A, RCOR1/CoREST, PHF21A/BHC80, ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I. Interacts with BTK and ARID3A. Interacts with isoform beta of PRKG1 (By similarity). {ECO:0000250, ECO:0000305}. TISSUE SPECIFICITY: Ubiquitous. +Q8K297 GT251_MOUSE Procollagen galactosyltransferase 1 (EC 2.4.1.50) (Collagen beta(1-O)galactosyltransferase 1) (Glycosyltransferase 25 family member 1) (Hydroxylysine galactosyltransferase 1) 617 71,061 Chain (1); Glycosylation (3); Motif (1); Sequence conflict (3); Signal peptide (1) FUNCTION: Beta-galactosyltransferase that transfers beta-galactose to hydroxylysine residues of type I collagen. By acting on collagen glycosylation, facilitates the formation of collagen triple helix. {ECO:0000250|UniProtKB:Q8NBJ5}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q8NBJ5}. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138}. Note=Colocalized with PLOD3 and mannose binding lectin. {ECO:0000250|UniProtKB:Q8NBJ5}. +Q99L20 GSTT3_MOUSE Glutathione S-transferase theta-3 (EC 2.5.1.18) 241 27,403 Chain (1); Domain (2); Region (2); Sequence conflict (1) FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Shows high activity towards 4-nitrobenzyl chloride (4-NBC). Also has lower activity towards 1,2-epoxy-3-(p-nitrophenoxy)propane (EPNP), cumene hydroperoxide, 1-chloro-2,4-dinitrobenzene (CDNB), 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole (NBD-Cl), and ethacrynic acid. {ECO:0000269|PubMed:12038961}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P30711}. TISSUE SPECIFICITY: Expressed strongly in liver, and at lower levels in kidney and testis. {ECO:0000269|PubMed:12038961}. +P14246 GTR2_MOUSE Solute carrier family 2, facilitated glucose transporter member 2 (Glucose transporter type 2, liver) (GLUT-2) 523 57,107 Binding site (2); Chain (1); Glycosylation (1); Modified residue (1); Region (1); Sequence conflict (5); Topological domain (13); Transmembrane (12) TRANSMEM 11 31 Helical; Name=1. {ECO:0000255}.; TRANSMEM 98 118 Helical; Name=2. {ECO:0000255}.; TRANSMEM 127 147 Helical; Name=3. {ECO:0000255}.; TRANSMEM 158 178 Helical; Name=4. {ECO:0000255}.; TRANSMEM 187 207 Helical; Name=5. {ECO:0000255}.; TRANSMEM 217 237 Helical; Name=6. {ECO:0000255}.; TRANSMEM 303 323 Helical; Name=7. {ECO:0000255}.; TRANSMEM 338 358 Helical; Name=8. {ECO:0000255}.; TRANSMEM 368 388 Helical; Name=9. {ECO:0000255}.; TRANSMEM 402 422 Helical; Name=10. {ECO:0000255}.; TRANSMEM 433 453 Helical; Name=11. {ECO:0000255}.; TRANSMEM 461 481 Helical; Name=12. {ECO:0000255}. TOPO_DOM 1 10 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 32 97 Extracellular. {ECO:0000255}.; TOPO_DOM 119 126 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 148 157 Extracellular. {ECO:0000255}.; TOPO_DOM 179 186 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 208 216 Extracellular. {ECO:0000255}.; TOPO_DOM 238 302 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 324 337 Extracellular. {ECO:0000255}.; TOPO_DOM 359 367 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 389 401 Extracellular. {ECO:0000255}.; TOPO_DOM 423 432 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 454 460 Extracellular. {ECO:0000255}.; TOPO_DOM 482 523 Cytoplasmic. {ECO:0000255}. FUNCTION: Facilitative glucose transporter. This isoform likely mediates the bidirectional transfer of glucose across the plasma membrane of hepatocytes and is responsible for uptake of glucose by the beta cells; may comprise part of the glucose-sensing mechanism of the beta cell. May also participate with the Na(+)/glucose cotransporter in the transcellular transport of glucose in the small intestine and kidney. PTM: N-glycosylated; required for stability and retention at the cell surface of pancreatic beta cells. {ECO:0000269|PubMed:16377570}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: In embryo, expressed in endoderm layer of yolk sac and liver primordium. {ECO:0000269|PubMed:1289053}. +Q9CY28 GTPB8_MOUSE GTP-binding protein 8 285 31,872 Alternative sequence (1); Chain (1); Domain (1); Metal binding (2); Nucleotide binding (5) +Q3THK7 GUAA_MOUSE GMP synthase [glutamine-hydrolyzing] (EC 6.3.5.2) (GMP synthetase) (Glutamine amidotransferase) 693 76,723 Active site (3); Binding site (5); Chain (1); Domain (2); Frameshift (1); Initiator methionine (1); Modified residue (5); Nucleotide binding (1); Sequence conflict (9) Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1. FUNCTION: Involved in the de novo synthesis of guanine nucleotides which are not only essential for DNA and RNA synthesis, but also provide GTP, which is involved in a number of cellular processes important for cell division. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +Q8VCP8 KAD6_MOUSE Adenylate kinase isoenzyme 6 (AK6) (EC 2.7.4.3) (Coilin-interacting nuclear ATPase protein) (Dual activity adenylate kinase/ATPase) (AK/ATPase) 172 19,947 Binding site (4); Chain (1); Nucleotide binding (2); Region (2) FUNCTION: Broad-specificity nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. May have a role in nuclear energy homeostasis. Has also ATPase activity. May be involved in regulation of Cajal body (CB) formation. {ECO:0000255|HAMAP-Rule:MF_03173}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000255|HAMAP-Rule:MF_03173}. Nucleus, Cajal body {ECO:0000255|HAMAP-Rule:MF_03173}. Note=Displays widespread diffuse nucleoplasmic distribution but not detected in nucleoli. Detected in Cajal bodies but not in all cells. {ECO:0000255|HAMAP-Rule:MF_03173}. SUBUNIT: Monomer and homodimer. Interacts with COIL (via C-terminus). {ECO:0000255|HAMAP-Rule:MF_03173}. +O09051 GUC2B_MOUSE Guanylate cyclase activator 2B [Cleaved into: Uroguanylin (UGN)] 106 11,628 Disulfide bond (3); Peptide (1); Propeptide (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Endogenous activator of intestinal guanylate cyclase. It stimulates this enzyme through the same receptor binding region as the heat-stable enterotoxins. May be a potent physiological regulator of intestinal fluid and electrolyte transport. May be an autocrine/paracrine regulator of intestinal salt and water transport (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Localized predominantly in intestinal villi and the corticomedullary junction of the kidney. +Q9QYK4 H6ST3_MOUSE Heparan-sulfate 6-O-sulfotransferase 3 (HS6ST-3) (mHS6ST-3) (EC 2.8.2.-) 470 55,037 Active site (1); Binding site (7); Chain (1); Glycosylation (6); Region (4); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 5 27 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 4 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 28 470 Lumenal. {ECO:0000255}. FUNCTION: 6-O-sulfation enzyme which catalyzes the transfer of sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to position 6 of the N-sulfoglucosamine residue (GlcNS) of heparan sulfate. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:10644753}. +P01898 HA10_MOUSE H-2 class I histocompatibility antigen, Q10 alpha chain 325 37,251 Beta strand (17); Chain (1); Disulfide bond (2); Domain (1); Erroneous initiation (2); Glycosylation (2); Helix (6); Region (4); Sequence conflict (2); Signal peptide (1); Topological domain (1); Transmembrane (1); Turn (2) TRANSMEM 311 324 Helical. {ECO:0000255}. TOPO_DOM 25 310 Extracellular. {ECO:0000255}. FUNCTION: Involved in the presentation of foreign antigens to the immune system. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2-microglobulin). +P01899 HA11_MOUSE H-2 class I histocompatibility antigen, D-B alpha chain (H-2D(B)) 362 40,836 Beta strand (22); Chain (1); Cross-link (1); Disulfide bond (2); Domain (1); Erroneous initiation (1); Glycosylation (3); Helix (7); Modified residue (2); Mutagenesis (16); Region (4); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 310 331 Helical. {ECO:0000255}. TOPO_DOM 25 309 Extracellular. {ECO:0000255}.; TOPO_DOM 332 362 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in the presentation of foreign antigens to the immune system. PTM: Polyubiquitinated in case of infection by murid herpesvirus 4, by the viral E3 ligase K3 (mK3). This modification causes the protein to be targeted for rapid degradation by the endoplasmic reticulum-associated degradation (ERAD) system. Ubiquitination occurs on lysine, as well as serine and threonine residues present in the cytoplasmic tail. Serine and threonine residues are subject to ubiquitination via ester bonds instead of the usual isopeptide linkage. {ECO:0000269|PubMed:17502423, ECO:0000269|PubMed:19531064, ECO:0000269|PubMed:19951915}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2-microglobulin). Interacts with murid herpesvirus 4 protein K3 (mK3). {ECO:0000269|PubMed:17502423, ECO:0000269|PubMed:19531064, ECO:0000269|PubMed:19951915}. +P01900 HA12_MOUSE H-2 class I histocompatibility antigen, D-D alpha chain (H-2D(D)) 365 41,110 Beta strand (21); Chain (1); Disulfide bond (2); Domain (1); Glycosylation (2); Helix (6); Modified residue (2); Region (4); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (2) TRANSMEM 312 334 Helical. {ECO:0000255}. TOPO_DOM 25 311 Extracellular. {ECO:0000255}.; TOPO_DOM 335 365 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in the presentation of foreign antigens to the immune system. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2-microglobulin). +P14426 HA13_MOUSE H-2 class I histocompatibility antigen, D-K alpha chain (H-2D(K)) 362 40,620 Chain (1); Disulfide bond (2); Domain (1); Glycosylation (3); Modified residue (2); Region (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 307 333 Helical. {ECO:0000255}. TOPO_DOM 25 306 Extracellular. {ECO:0000255}.; TOPO_DOM 334 362 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in the presentation of foreign antigens to the immune system. PTM: Polyubiquitinated in case of infection by murid herpesvirus 4, by the viral E3 ligase K3 (mK3), leading to target the protein for rapid degradation by the endoplasmic reticulum-associated degradation (ERAD) system. Ubiquitination takes place on lysine, as well as serine and threonine residues present in the cytoplasmic tail. Hydroxylated serine and threonine residues in the cytoplasmic tail are subject to ubiquitination via ester bonds instead of the classical isopeptide linkage (Probable). {ECO:0000305|PubMed:11672544}.; PTM: Hydroxylation of residues in the cytoplasmic tail. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2-microglobulin). +P14427 HA14_MOUSE H-2 class I histocompatibility antigen, D-P alpha chain (H-2D(P)) 368 41,342 Chain (1); Disulfide bond (2); Domain (1); Glycosylation (3); Modified residue (2); Region (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 304 330 Helical. {ECO:0000255}. TOPO_DOM 22 303 Extracellular. {ECO:0000255}.; TOPO_DOM 331 368 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in the presentation of foreign antigens to the immune system. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2-microglobulin). +P06339 HA15_MOUSE H-2 class I histocompatibility antigen, D-37 alpha chain 357 40,875 Beta strand (16); Chain (1); Disulfide bond (2); Domain (1); Glycosylation (2); Helix (7); Modified residue (1); Region (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 305 327 Helical. {ECO:0000255}. TOPO_DOM 21 304 Extracellular. {ECO:0000255}.; TOPO_DOM 328 357 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in the presentation of foreign antigens to the immune system. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2-microglobulin). +P14429 HA17_MOUSE H-2 class I histocompatibility antigen, Q7 alpha chain (QA-2 antigen) 334 37,924 Beta strand (17); Chain (1); Disulfide bond (2); Domain (1); Erroneous initiation (1); Glycosylation (2); Helix (6); Region (4); Sequence conflict (1); Signal peptide (1); Topological domain (1); Transmembrane (1); Turn (1) TRANSMEM 311 332 Helical. {ECO:0000255}. TOPO_DOM 22 310 Extracellular. {ECO:0000255}. FUNCTION: Involved in the presentation of foreign antigens to the immune system. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2-microglobulin). +P14430 HA18_MOUSE H-2 class I histocompatibility antigen, Q8 alpha chain 326 37,411 Chain (1); Disulfide bond (2); Domain (1); Glycosylation (2); Region (4); Signal peptide (1); Topological domain (1); Transmembrane (1) TRANSMEM 306 326 Helical. {ECO:0000255}. TOPO_DOM 22 305 Extracellular. {ECO:0000255}. FUNCTION: Involved in the presentation of foreign antigens to the immune system. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2-microglobulin). +P14431 HA19_MOUSE H-2 class I histocompatibility antigen, Q9 alpha chain (Fragment) 200 23,025 Chain (1); Disulfide bond (1); Erroneous initiation (1); Glycosylation (1); Non-terminal residue (1); Region (2); Signal peptide (1); Topological domain (1) TOPO_DOM 22 >200 Extracellular. {ECO:0000255}. FUNCTION: Involved in the presentation of foreign antigens to the immune system. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2-microglobulin). +P01901 HA1B_MOUSE H-2 class I histocompatibility antigen, K-B alpha chain (H-2K(B)) 369 41,302 Beta strand (22); Chain (1); Disulfide bond (2); Domain (1); Glycosylation (2); Helix (7); Modified residue (2); Region (4); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (2) TRANSMEM 306 328 Helical. {ECO:0000255}. TOPO_DOM 22 305 Extracellular. {ECO:0000255}.; TOPO_DOM 329 369 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in the presentation of foreign antigens to the immune system. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2-microglobulin). {ECO:0000269|PubMed:9806638}. +P01902 HA1D_MOUSE H-2 class I histocompatibility antigen, K-D alpha chain (H-2K(D)) 368 41,490 Beta strand (21); Chain (1); Disulfide bond (2); Domain (1); Glycosylation (3); Helix (8); Modified residue (2); Region (4); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 306 328 Helical. {ECO:0000255}. TOPO_DOM 22 305 Extracellular. {ECO:0000255}.; TOPO_DOM 329 368 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in the presentation of foreign antigens to the immune system. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2-microglobulin). +B1B212 H60B_MOUSE Histocompatibility antigen 60b 251 28,224 Chain (1); Glycosylation (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 213 233 Helical. {ECO:0000255}. TOPO_DOM 25 212 Extracellular. {ECO:0000305}.; TOPO_DOM 234 251 Cytoplasmic. {ECO:0000305}. FUNCTION: Ligand for the KLRK1 immunosurveillance receptor. Binding to KLRK1 stimulates cell lysis in vitro. {ECO:0000269|PubMed:18209064}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18209064}; Single-pass type I membrane protein {ECO:0000255}. TISSUE SPECIFICITY: In strain C57BL/6J, strongly expressed in cardiac muscle and skeletal muscle, with lower expression levels in spleen, liver, kidney and thymus. In strain BALB/cJ, weakly expressed in cardiac muscle, spleen, kidney and thymus. {ECO:0000269|PubMed:18209064}. +P04223 HA1K_MOUSE H-2 class I histocompatibility antigen, K-K alpha chain (H-2K(K)) 369 41,646 Alternative sequence (1); Beta strand (18); Chain (1); Disulfide bond (2); Domain (1); Glycosylation (2); Helix (6); Modified residue (4); Natural variant (1); Region (4); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (2) TRANSMEM 306 328 Helical. {ECO:0000255}. TOPO_DOM 22 305 Extracellular. {ECO:0000255}.; TOPO_DOM 329 369 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in the presentation of foreign antigens to the immune system. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2-microglobulin). +P14428 HA1Q_MOUSE H-2 class I histocompatibility antigen, K-Q alpha chain (H-2K(Q)) (Fragment) 328 36,856 Chain (1); Disulfide bond (2); Domain (1); Glycosylation (2); Modified residue (2); Non-terminal residue (1); Region (4); Topological domain (2); Transmembrane (1) TRANSMEM 266 289 Helical. {ECO:0000255}. TOPO_DOM <1 265 Extracellular. {ECO:0000255}.; TOPO_DOM 290 328 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in the presentation of foreign antigens to the immune system. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2-microglobulin). +P03991 HA1W_MOUSE H-2 class I histocompatibility antigen, K-W28 alpha chain 368 41,104 Chain (1); Disulfide bond (2); Domain (1); Glycosylation (2); Modified residue (2); Region (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 306 329 Helical. {ECO:0000255}. TOPO_DOM 22 305 Extracellular. {ECO:0000255}.; TOPO_DOM 330 368 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in the presentation of foreign antigens to the immune system. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2-microglobulin). +P01904 HA21_MOUSE H-2 class II histocompatibility antigen, E-D alpha chain (H2-IE-alpha) 255 29,117 Beta strand (13); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (1); Helix (2); Region (3); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (3) TRANSMEM 217 242 Helical. {ECO:0000255}. TOPO_DOM 26 216 Extracellular. {ECO:0000255}.; TOPO_DOM 243 255 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +P01910 HA2K_MOUSE H-2 class II histocompatibility antigen, A-K alpha chain 256 28,351 Beta strand (13); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (2); Helix (2); Region (3); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (2) TRANSMEM 219 241 Helical. {ECO:0000255}. TOPO_DOM 24 218 Extracellular. {ECO:0000255}.; TOPO_DOM 242 256 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +P04227 HA2Q_MOUSE H-2 class II histocompatibility antigen, A-Q alpha chain (Fragment) 221 24,464 Chain (1); Disulfide bond (1); Domain (1); Glycosylation (1); Non-terminal residue (1); Region (3); Topological domain (2); Transmembrane (1) TRANSMEM 184 209 Helical. {ECO:0000255}. TOPO_DOM <1 183 Extracellular. {ECO:0000255}.; TOPO_DOM 210 221 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q8K2C9 HACD3_MOUSE Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 3 (EC 4.2.1.134) (3-hydroxyacyl-CoA dehydratase 3) (HACD3) (Butyrate-induced protein 1) (B-ind1) (Protein-tyrosine phosphatase-like A domain-containing protein 1) 362 43,131 Active site (2); Chain (1); Coiled coil (1); Compositional bias (2); Domain (1); Modified residue (3); Sequence conflict (3); Topological domain (7); Transmembrane (6) TRANSMEM 150 170 Helical. {ECO:0000255}.; TRANSMEM 190 210 Helical. {ECO:0000255}.; TRANSMEM 213 233 Helical. {ECO:0000255}.; TRANSMEM 243 263 Helical. {ECO:0000255}.; TRANSMEM 281 301 Helical. {ECO:0000255}.; TRANSMEM 323 343 Helical. {ECO:0000255}. TOPO_DOM 1 149 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 171 189 Lumenal. {ECO:0000255}.; TOPO_DOM 211 212 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 234 242 Lumenal. {ECO:0000255}.; TOPO_DOM 264 280 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 302 322 Lumenal. {ECO:0000255}.; TOPO_DOM 344 362 Cytoplasmic. {ECO:0000255}. Lipid metabolism; fatty acid biosynthesis. FUNCTION: Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. Thereby, it participates in the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. Involved in Rac1-signaling pathways leading to the modulation of gene expression. Promotes insulin receptor/INSR autophosphorylation and is involved in INSR internalization (By similarity). {ECO:0000250|UniProtKB:Q9P035}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9P035}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9P035}. SUBUNIT: May interact with enzymes of the ELO family (including ELOVL1); with those enzymes that mediate condensation, the first of the four steps of the reaction cycle responsible for fatty acids elongation, may be part of a larger fatty acids elongase complex. Interacts with RAC1. Associates with internalized insulin receptor/INSR complexes on Golgi/endosomal membranes; HACD3/PTPLAD1 together with ATIC and PRKAA2/AMPK2 is proposed to be part of a signaling network regulating INSR autophosphorylation and endocytosis (By similarity). {ECO:0000250|UniProtKB:Q9P035}. +A2AKM2 HACD4_MOUSE Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 4 (EC 4.2.1.134) (3-hydroxyacyl-CoA dehydratase 4) (HACD4) (Protein-tyrosine phosphatase-like A domain-containing protein 2) 232 27,235 Active site (2); Alternative sequence (1); Chain (1); Erroneous initiation (2); Topological domain (7); Transmembrane (6) TRANSMEM 20 40 Helical. {ECO:0000255}.; TRANSMEM 57 77 Helical. {ECO:0000255}.; TRANSMEM 113 133 Helical. {ECO:0000255}.; TRANSMEM 136 156 Helical. {ECO:0000255}.; TRANSMEM 158 178 Helical. {ECO:0000255}.; TRANSMEM 190 210 Helical. {ECO:0000255}. TOPO_DOM 1 19 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 41 56 Lumenal. {ECO:0000255}.; TOPO_DOM 78 112 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 134 135 Lumenal. {ECO:0000255}.; TOPO_DOM 157 157 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 179 189 Lumenal. {ECO:0000255}.; TOPO_DOM 211 232 Cytoplasmic. {ECO:0000255}. Lipid metabolism; fatty acid biosynthesis. FUNCTION: Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. Thereby, it participates in the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. {ECO:0000250|UniProtKB:Q5VWC8}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q5VWC8}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5VWC8}. SUBUNIT: May interact with enzymes of the ELO family (including ELOVL1); with those enzymes that mediate condensation, the first of the four steps of the reaction cycle responsible for fatty acids elongation, may be part of a larger fatty acids elongase complex. {ECO:0000250|UniProtKB:Q5VWC8}. +Q3U0D9 HACE1_MOUSE E3 ubiquitin-protein ligase HACE1 (EC 2.3.2.26) (HECT domain and ankyrin repeat-containing E3 ubiquitin-protein ligase 1) (HECT-type E3 ubiquitin transferase HACE1) 909 102,114 Active site (1); Alternative sequence (4); Chain (1); Domain (1); Erroneous initiation (1); Repeat (6); Sequence conflict (1) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase involved in Golgi membrane fusion and regulation of small GTPases. Acts as a regulator of Golgi membrane dynamics during the cell cycle: recruited to Golgi membrane by Rab proteins and regulates postmitotic Golgi membrane fusion. Acts by mediating ubiquitination during mitotic Golgi disassembly, ubiquitination serving as a signal for Golgi reassembly later, after cell division. Specifically interacts with GTP-bound RAC1, mediating ubiquitination and subsequent degradation of active RAC1, thereby playing a role in host defense against pathogens (By similarity). May also act as a transcription regulator via its interaction with RARB. {ECO:0000250|UniProtKB:Q8IYU2, ECO:0000269|PubMed:19350571}. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250}. Cytoplasm {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Note=A significant portion localizes to the endoplasmic reticulum. Targeted to Golgi membrane via its interaction with Rab proteins (By similarity). {ECO:0000250}. SUBUNIT: Interacts with RAB1 (RAB1A, RAB1B or RAB1C), RAB4 (RAB4A or RAB4B) and RAB11 (RAB11A or RAB11B); in a GTP-dependent manner. Interacts with RAC1; in a GTP-dependent manner. Interacts with the 26S proteasomal complex through the 20S core proteasomal subunit (By similarity). Interacts with RARB. {ECO:0000250|UniProtKB:Q8IYU2, ECO:0000269|PubMed:19350571}. +Q8BTY1 KAT1_MOUSE Kynurenine--oxoglutarate transaminase 1 (EC 2.6.1.7) (Cysteine-S-conjugate beta-lyase) (EC 4.4.1.13) (Glutamine transaminase K) (GTK) (Glutamine--phenylpyruvate transaminase) (EC 2.6.1.64) (Kynurenine aminotransferase 1) (Kynurenine aminotransferase I) (KATI) (Kynurenine--oxoglutarate transaminase I) 424 47,564 Binding site (3); Chain (1); Modified residue (3); Sequence conflict (1) Amino-acid degradation; L-kynurenine degradation; kynurenate from L-kynurenine: step 1/2. FUNCTION: Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Metabolizes the cysteine conjugates of certain halogenated alkenes and alkanes to form reactive metabolites. Catalyzes the beta-elimination of S-conjugates and Se-conjugates of L-(seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +P08103 HCK_MOUSE Tyrosine-protein kinase HCK (EC 2.7.10.2) (B-cell/myeloid kinase) (BMK) (Hematopoietic cell kinase) (Hemopoietic cell kinase) (p56-HCK/p59-HCK) 524 59,129 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Domain (3); Initiator methionine (2); Lipidation (3); Modified residue (6); Mutagenesis (1); Nucleotide binding (1); Sequence caution (7) FUNCTION: Non-receptor tyrosine-protein kinase found in hematopoietic cells that transmits signals from cell surface receptors and plays an important role in the regulation of innate immune responses, including neutrophil, monocyte, macrophage and mast cell functions, phagocytosis, cell survival and proliferation, cell adhesion and migration. Acts downstream of receptors that bind the Fc region of immunoglobulins, such as FCGR1A and FCGR2A, but also CSF3R, PLAUR, the receptors for IFNG, IL2, IL6 and IL8, and integrins, such as ITGB1 and ITGB2. During the phagocytic process, mediates mobilization of secretory lysosomes, degranulation, and activation of NADPH oxidase to bring about the respiratory burst. Plays a role in the release of inflammatory molecules. Promotes reorganization of the actin cytoskeleton and actin polymerization, formation of podosomes and cell protrusions. Inhibits TP73-mediated transcription activation and TP73-mediated apoptosis. Phosphorylates CBL in response to activation of immunoglobulin gamma Fc region receptors. Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, GAB2, RAPGEF1, STAT5B, TP73, VAV1 and WAS (By similarity). {ECO:0000250, ECO:0000269|PubMed:10547366, ECO:0000269|PubMed:10799548, ECO:0000269|PubMed:12235133, ECO:0000269|PubMed:14551197, ECO:0000269|PubMed:16809022, ECO:0000269|PubMed:17513616, ECO:0000269|PubMed:18246197, ECO:0000269|PubMed:18625913, ECO:0000269|PubMed:19897576, ECO:0000269|PubMed:19903482, ECO:0000269|PubMed:8125254, ECO:0000269|PubMed:9400828, ECO:0000269|PubMed:9916742}. PTM: Phosphorylated on several tyrosine residues. Autophosphorylated. Becomes rapidly phosphorylated upon activation of the immunoglobulin receptors FCGR1A and FCGR2A. Phosphorylation at Tyr-409 increases kinase activity. Phosphorylation at Tyr-520 inhibits kinase activity. Kinase activity is not required for phosphorylation at Tyr-520, suggesting that this site may be a target of other kinases. {ECO:0000269|PubMed:10934191}.; PTM: Ubiquitinated by CBL, leading to its degradation via the proteasome.; PTM: Isoform 2 palmitoylation at position 2 requires prior myristoylation. Palmitoylation at position 3 is required for caveolar localization of isoform 2. {ECO:0000250|UniProtKB:P08631}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 1: Membrane; Lipid-anchor. Membrane, caveola {ECO:0000250}. Lysosome {ECO:0000250}. Cell projection, podosome membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Note=Associated with specialized secretory lysosomes called azurophil granules. A fraction of this isoform is found in the cytoplasm, some of this fraction is myristoylated (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 2: Cell membrane; Lipid-anchor. Membrane, caveola {ECO:0000250}; Lipid-anchor {ECO:0000250}. Cell junction, focal adhesion {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Golgi apparatus {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Lysosome {ECO:0000250}. Nucleus {ECO:0000250}. Note=20% of this isoform is associated with caveolae. Localization at the cell membrane and at caveolae requires palmitoylation at Cys-3. Colocalizes with the actin cytoskeleton at focal adhesions (By similarity). {ECO:0000250}. SUBUNIT: Interacts with ADAM15. Interacts with FASLG. Interacts with ARRB1 and ARRB2. Interacts with FCGR1A; the interaction may be indirect. Interacts with IL6ST. Interacts (via SH3 domain) with ELMO1. Interacts (via SH3 domain) with TP73. Interacts with YAP1. Interacts with ABL1 and ITGB1, and thereby recruits ABL1 to activated ITGB1 (By similarity). Interacts (via SH2 domain) with FLT3 (tyrosine phosphorylated). Interacts with CBL. Interacts with VAV1, WAS and RAPGEF1. Interacts (via SH3 domain) with WDCP (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P08631, ECO:0000269|PubMed:10799548, ECO:0000269|PubMed:12235133, ECO:0000269|PubMed:14551197, ECO:0000269|PubMed:16684964, ECO:0000269|PubMed:19903482, ECO:0000269|PubMed:9400828}. TISSUE SPECIFICITY: Expressed predominantly in cells of the myeloid and B-lymphoid lineages. +P49710 HCLS1_MOUSE Hematopoietic lineage cell-specific protein (Hematopoietic cell-specific LYN substrate 1) (LckBP1) 486 54,240 Chain (1); Domain (1); Modified residue (12); Mutagenesis (2); Region (1); Repeat (4); Sequence conflict (2) FUNCTION: Substrate of the antigen receptor-coupled tyrosine kinase. Plays a role in antigen receptor signaling for both clonal expansion and deletion in lymphoid cells. May also be involved in the regulation of gene expression (By similarity). {ECO:0000250}. PTM: Phosphorylated by LYN, FYN and FGR after cross-linking of surface IgM on B-cells. Phosphorylation by LYN, FYN and FGR requires prior phosphorylation by SYK (By similarity). Binds to LCK in vivo, and is tyrosine phosphorylated upon TCR stimulation. Phosphorylated by FES. {ECO:0000250, ECO:0000269|PubMed:19001085}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. SUBUNIT: Interacts (via SH2 domain) with FGR (By similarity). Associates with the SH2 and SH3 domains of LCK. Binding to he LCK SH3 domain occurs constitutively, while binding to the LCK SH2 domain occurs only upon TCR stimulation. A similar binding pattern was observed with LYN, but not with FYN in which the FYN SH2 region associates upon TCR stimulation but the FYN SH3 region does not associate regardless of TCR stimulation. Directly associates with HAX1, through binding to its C-terminal region. Interacts with HS1BP3. Interacts with FES/FPS. Forms a multiprotein complex with LYN and ANKRD54. {ECO:0000250, ECO:0000269|PubMed:10590261, ECO:0000269|PubMed:19001085, ECO:0000269|PubMed:19064729, ECO:0000269|PubMed:8943564}. TISSUE SPECIFICITY: Expressed only in tissues and cells of hematopoietic origin. +Q9QUJ0 HCST_MOUSE Hematopoietic cell signal transducer (DNAX-activation protein 10) (Membrane protein DAP10) (Transmembrane adapter protein KAP10) 79 8,114 Alternative sequence (1); Chain (1); Modified residue (1); Region (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 36 56 Helical. {ECO:0000255}. TOPO_DOM 18 35 Extracellular. {ECO:0000255}.; TOPO_DOM 57 79 Cytoplasmic. {ECO:0000255}. FUNCTION: Transmembrane adapter protein which associates with KLRK1 to form an activation receptor KLRK1-HCST in lymphoid and myeloid cells; this receptor plays a major role in triggering cytotoxicity against target cells expressing cell surface ligands such as MHC class I chain-related MICA and MICB, and UL16-binding proteins (ULBPs); these ligands are up-regulated by stress conditions and pathological state such as viral infection and tumor transformation. Functions as docking site for PI3-kinase PIK3R1 and GRB2. Interaction of ULBPs with KLRK1-HCST triggers calcium mobilization and activation of the PIK3R1, MAP2K/ERK, and JAK2/STAT5 signaling pathways. Both PIK3R1 and GRB2 are required for full KLRK1-HCST-mediated activation and ultimate killing of target cells. In NK cells, KLRK1-HCST signaling directly induces cytotoxicity and enhances cytokine production initiated via DAP12/TYROBP-associated receptors. In T-cells, it provides primarily costimulation for TCR-induced signals. KLRK1-HCST receptor plays a role in immune surveillance against tumors and is required for cytolysis of tumors cells; indeed, melanoma cells that do not express KLRK1 ligands escape from immune surveillance mediated by NK cells. {ECO:0000269|PubMed:10528161, ECO:0000269|PubMed:12426565, ECO:0000269|PubMed:15365099, ECO:0000269|PubMed:16086018, ECO:0000269|PubMed:16887996, ECO:0000269|PubMed:17100879}. PTM: Phosphorylated; PIK3R1 and GRB2 associate specifically with tyrosine-phosphorylated HCST. {ECO:0000269|PubMed:10528161}.; PTM: O-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:17100879}; Single-pass type I membrane protein {ECO:0000269|PubMed:17100879}. SUBUNIT: Homodimer; Disulfide-linked. Interacts with KLRK1 to form a stable complex, which results in surface expression of both proteins, whereas alone, it is minimally expressed. Interacts with PIK3R1 and GRB2. Interacts with CLEC5A (By similarity). Forms an CLEC5A/TYROBP/HCST trimolecular complex depending almost solely on TYROBP. Heterohexamer composed of four subunits of HCST/DAP10 and two subunits of KLRK1. Interacts (via transmembrane domain) with KLRK1 isoform 1 (via transmembrane domain); the interaction is required for KLRK1 cell surface expression on naive NK cells and activated CD8(+) T-cells, but is dispensable on activated TYROBP-expressing NK cells. Interacts (via transmembrane domain) with KLRK1 isoform 2 (via transmembrane domain); the interaction is required for KLRK1 NK cell surface expression and induces NK cell-mediated cytotoxicity. Interacts with CD300H (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9UBK5, ECO:0000269|PubMed:10528161, ECO:0000269|PubMed:12426565, ECO:0000269|PubMed:15294961, ECO:0000269|PubMed:16887996, ECO:0000269|PubMed:19251634}. +Q8BRB7 KAT6B_MOUSE Histone acetyltransferase KAT6B (EC 2.3.1.48) (MOZ, YBF2/SAS3, SAS2 and TIP60 protein 4) (MYST-4) (Protein querkopf) 1872 208,526 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Compositional bias (7); Cross-link (1); Domain (2); Modified residue (6); Region (6); Sequence caution (3); Sequence conflict (2); Zinc finger (3) FUNCTION: Histone acetyltransferase which may be involved in both positive and negative regulation of transcription. Required for RUNX2-dependent transcriptional activation. Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity (By similarity). Involved in cerebral cortex development. {ECO:0000250, ECO:0000269|PubMed:10821753}. PTM: Autoacetylation at Lys-633 is required for proper function. {ECO:0000250|UniProtKB:Q9H7Z6}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Component of the MOZ/MORF complex composed at least of ING5, KAT6A, KAT6B, MEAF6 and one of BRPF1, BRD1/BRPF2 and BRPF3. Interacts with RUNX1 and RUNX2. {ECO:0000250|UniProtKB:Q8WYB5}. DOMAIN: The N-terminus is involved in transcriptional activation while the C-terminus is involved in transcriptional repression. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:10821753}. +Q9D1P2 KAT8_MOUSE Histone acetyltransferase KAT8 (EC 2.3.1.48) (Lysine acetyltransferase 8) (MOZ, YBF2/SAS3, SAS2 and TIP60 protein 1) (MYST-1) 458 52,574 Active site (1); Alternative sequence (2); Beta strand (5); Binding site (3); Chain (1); Domain (2); Frameshift (1); Initiator methionine (1); Modified residue (6); Region (3); Sequence conflict (1); Turn (5); Zinc finger (1) FUNCTION: Histone acetyltransferase which may be involved in transcriptional activation. May influence the function of ATM. As part of the MSL complex it is involved in acetylation of nucleosomal histone H4 producing specifically H4K16ac. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. That activity is less specific than the one of the MSL complex. Can also acetylate TP53/p53 at 'Lys-120'. {ECO:0000250|UniProtKB:Q9H7Z6}. PTM: Autoacetylation at Lys-274 is required for binding histone H4 with high affinity and for proper function. {ECO:0000250|UniProtKB:Q9H7Z6}. SUBCELLULAR LOCATION: Nucleus. Chromosome {ECO:0000250}. SUBUNIT: Component of a multisubunit histone acetyltransferase complex (MSL) at least composed of the MOF/KAT8, MSL1/hampin, MSL2L1 and MSL3L1. Component of the NSL complex at least composed of MOF/KAT8, KANSL1, KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT, WDR5 and HCFC1. Interacts with KANSL1; the interaction is direct. Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, MOF/KAT8, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Interacts with the chromodomain of MORF4L1/MRG15. Interacts with ATM through the chromodomain (By similarity). Interacts with MSL1; the interaction is direct. {ECO:0000250, ECO:0000269|PubMed:21217699}. +Q3UGR5 HDHD2_MOUSE Haloacid dehalogenase-like hydrolase domain-containing protein 2 259 28,730 Alternative sequence (2); Beta strand (12); Binding site (1); Chain (1); Coiled coil (1); Frameshift (1); Helix (14); Metal binding (3); Modified residue (1); Region (2); Sequence conflict (4); Turn (1) +Q9CYW4 HDHD3_MOUSE Haloacid dehalogenase-like hydrolase domain-containing protein 3 251 28,027 Chain (1); Modified residue (3) +Q91WM2 HDHD5_MOUSE Haloacid dehalogenase-like hydrolase domain-containing 5 (Cat eye syndrome critical region protein 5 homolog) 419 46,306 Chain (1); Signal peptide (1) +P51859 HDGF_MOUSE Hepatoma-derived growth factor (HDGF) 237 26,269 Binding site (6); Chain (1); Compositional bias (1); Cross-link (2); Domain (1); Modified residue (10); Motif (2); Sequence conflict (4) FUNCTION: Heparin-binding protein, with mitogenic activity for fibroblasts. Acts as a transcriptional repressor (By similarity). {ECO:0000250}. PTM: Sumoylated with SUMO1. Sumoylation prevents binding to chromatin (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Monomer, and domain-swapped homodimer. {ECO:0000250}. DOMAIN: The PWWP domain harbors the heparin-binding sites and is responsible for DNA-binding, while the C-terminal region is essentially unstructured. {ECO:0000250}. TISSUE SPECIFICITY: Expressed predominantly in testis and skeletal muscle, to intermediate extents in heart, brain, lung, liver, and kidney, and to a minimal extent in spleen. +Q9Z2V6 HDAC5_MOUSE Histone deacetylase 5 (HD5) (EC 3.5.1.98) (Histone deacetylase mHDA1) 1113 120,942 Active site (1); Chain (1); Compositional bias (3); Cross-link (1); Metal binding (4); Modified residue (7); Motif (1); Mutagenesis (4); Region (1); Sequence conflict (2) FUNCTION: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Involved in muscle maturation by repressing transcription of myocyte enhancer MEF2C. During muscle differentiation, it shuttles into the cytoplasm, allowing the expression of myocyte enhancer factors (By similarity). {ECO:0000250}. PTM: Phosphorylated by AMPK, CaMK1, SIK1 and PRKD1 at Ser-250 and Ser-488. The phosphorylation is required for the export to the cytoplasm and inhibition. Phosphorylated by the PKC kinases PKN1 and PKN2, impairing nuclear import (By similarity). Phosphorylated by GRK5, leading to nuclear export of HDAC5 and allowing MEF2-mediated transcription. {ECO:0000250, ECO:0000269|PubMed:17468767, ECO:0000269|PubMed:18711143, ECO:0000269|PubMed:21454484}.; PTM: Ubiquitinated. Polyubiquitination however does not lead to its degradation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Shuttles between the nucleus and the cytoplasm. In muscle cells, it shuttles into the cytoplasm during myocyte differentiation. The export to cytoplasm depends on the interaction with a 14-3-3 chaperone protein and is due to its phosphorylation at Ser-250 and Ser-488 by AMPK, CaMK1 and SIK1. SUBUNIT: Interacts with AHRR, BAHD1, BCOR, HDAC7, HDAC9, CTBP1, MEF2C, NCOR2, NRIP1, PHB2 and a 14-3-3 chaperone protein. Interacts with BCL6, DDIT3/CHOP, GRK5, KDM5B and MYOCD. Interacts with EP300 in the presence of TFAP2C. Interacts with ANKRA2. Interacts with CUL7 (as part of the 3M complex); negatively regulated by ANKRA2. Interacts with ZBTB7B; the interaction allows the recruitment of HDAC4 on CD8 loci for deacetylation and possible inhibition of CD8 genes expression (PubMed:22730529). {ECO:0000250|UniProtKB:Q9UQL6, ECO:0000269|PubMed:10640276, ECO:0000269|PubMed:10984530, ECO:0000269|PubMed:11022042, ECO:0000269|PubMed:15060175, ECO:0000269|PubMed:15140878, ECO:0000269|PubMed:15601857, ECO:0000269|PubMed:17949687, ECO:0000269|PubMed:18711143, ECO:0000269|PubMed:22730529}. DOMAIN: The nuclear export sequence mediates the shuttling between the nucleus and the cytoplasm. +Q14B70 HDX_MOUSE Highly divergent homeobox 692 76,861 Alternative sequence (1); Chain (1); Compositional bias (1); Cross-link (9); DNA binding (2) SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. +Q3U487 HECD3_MOUSE E3 ubiquitin-protein ligase HECTD3 (EC 2.3.2.26) (HECT domain-containing protein 3) (HECT-type E3 ubiquitin transferase HECTD3) 861 97,347 Active site (1); Alternative sequence (1); Chain (1); Domain (2); Initiator methionine (1); Modified residue (2); Sequence conflict (2) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin ligases accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates ubiquitination of TRIOBP and its subsequent proteasomal degradation, thus faciliting cell cycle progression by regulating the turn-over of TRIOBP (By imilarity). Mediates also ubiquitination of STX8. {ECO:0000250|UniProtKB:Q5T447, ECO:0000269|PubMed:18821010}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:18821010}. SUBUNIT: Interacts with TRIOBP (By similarity). Interacts with STX8. {ECO:0000250|UniProtKB:Q5T447, ECO:0000269|PubMed:18821010}. +Q99N13 HDAC9_MOUSE Histone deacetylase 9 (HD9) (EC 3.5.1.98) (Histone deacetylase 7B) (HD7b) (Histone deacetylase-related protein) (MEF2-interacting transcription repressor MITR) 588 65,687 Alternative sequence (2); Chain (1); Helix (1); Modified residue (5); Mutagenesis (1); Region (4); Sequence conflict (6) FUNCTION: Devoided of intrinsic deacetylase activity, promotes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4) by recruiting HDAC1 and HDAC3. Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Represses MEF2-dependent transcription, inhibits skeletal myogenesis and may be involved in heart development. Protects neurons from apoptosis, both by inhibiting JUN phosphorylation by MAPK10 and by repressing JUN transcription via HDAC1 recruitment to JUN promoter. {ECO:0000269|PubMed:11390982, ECO:0000269|PubMed:12202037, ECO:0000269|PubMed:15711539, ECO:0000269|PubMed:16611996}. PTM: Sumoylated. {ECO:0000250}.; PTM: Phosphorylated on Ser-220 and Ser-450; which promotes 14-3-3-binding, impairs interaction with MEF2, and antagonizes antimyogenic activity. Phosphorylated on Ser-240 by DYRK1B; which impairs nuclear accumulation. Phosphorylated by the PKC kinases PKN1 and PKN2, impairing nuclear import. {ECO:0000269|PubMed:11390982, ECO:0000269|PubMed:12202037, ECO:0000269|PubMed:15546868}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11390982, ECO:0000269|PubMed:15546868, ECO:0000269|PubMed:15711539}. SUBUNIT: Homodimer. Interacts with ETV6 (By similarity). Interacts with MEF2, HDAC1, HDAC3, HDAC4, HDAC5, CTBP1 and MAPK10. The phosphorylated form interacts with 14-3-3. Interacts with FOXP3 in the absence of T-cell stimulation (By similarity). {ECO:0000250|UniProtKB:Q9UKV0, ECO:0000269|PubMed:11022042, ECO:0000269|PubMed:15567413, ECO:0000269|PubMed:15711539, ECO:0000269|PubMed:16611996}. TISSUE SPECIFICITY: Expressed at high levels in heart, brain and spleen. Expressed in skeletal muscle. {ECO:0000269|PubMed:11390982, ECO:0000269|PubMed:15711539}. +Q6P1G0 HEAT6_MOUSE HEAT repeat-containing protein 6 1184 128,922 Chain (1); Compositional bias (2); Erroneous initiation (1); Modified residue (4); Repeat (4) +E9QAM5 HELZ2_MOUSE Helicase with zinc finger domain 2 (EC 3.6.4.-) (PPAR-gamma DNA-binding domain-interacting protein 1) (PDIP1) (PPAR-gamma DBD-interacting protein 1) 2947 331,563 Chain (1); Modified residue (1); Motif (6); Nucleotide binding (2); Region (2); Sequence conflict (8); Zinc finger (2) FUNCTION: Helicase that acts as a transcriptional coactivator for a number of nuclear receptors including PPARA, PPARG, THRA, THRB and RXRA. {ECO:0000269|PubMed:23525231}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23525231}. SUBUNIT: Interacts with PPARA (via DNA-binding domain) and PPARG; the interaction stimulates the transcriptional activity of PPARA and PPARG. Interacts with THRAP3; the interaction is direct and HELZ2 and THRAP3 synergistically enhance the transcriptional activity of PPARG. It is probably part of the peroxisome proliferator activated receptor alpha interacting complex (PRIC). {ECO:0000269|PubMed:23525231}. DOMAIN: Contains 5 Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs. These motifs are not required for interaction with PPARG (By similarity). {ECO:0000250}. +P08680 HEM0_MOUSE 5-aminolevulinate synthase, erythroid-specific, mitochondrial (ALAS-E) (EC 2.3.1.37) (5-aminolevulinic acid synthase 2) (Delta-ALA synthase 2) (Delta-aminolevulinate synthase 2) 587 64,753 Active site (1); Beta strand (1); Binding site (9); Chain (1); Erroneous initiation (1); Helix (1); Modified residue (1); Mutagenesis (1); Sequence conflict (7); Transit peptide (1); Turn (2) Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from glycine: step 1/1. SUBCELLULAR LOCATION: Mitochondrion matrix. SUBUNIT: Interacts with SUCLA2 (By similarity). Homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Erythroid specific. +Q7TS99 HELT_MOUSE Hairy and enhancer of split-related protein HELT (HES/HEY-like transcription factor) (Protein Hes-like) (Protein megane) 240 26,973 Chain (1); Domain (2); Modified residue (1) FUNCTION: Transcriptional repressor which binds preferentially to the canonical E box sequence 5'-CACGCG-3'. Required for the development of GABAergic neurons. {ECO:0000269|PubMed:14764602, ECO:0000269|PubMed:15071116, ECO:0000269|PubMed:16968817, ECO:0000269|PubMed:17611227}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00380, ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:14764602, ECO:0000269|PubMed:16644143}. SUBUNIT: Self-associates. Interacts with HES5 and HEY2. {ECO:0000269|PubMed:14764602}. TISSUE SPECIFICITY: Expressed in heart and testis. +Q923T9 KCC2G_MOUSE Calcium/calmodulin-dependent protein kinase type II subunit gamma (CaM kinase II subunit gamma) (CaMK-II subunit gamma) (EC 2.7.11.17) 529 59,607 Active site (1); Alternative sequence (2); Binding site (1); Chain (1); Domain (1); Modified residue (8); Nucleotide binding (1); Region (2) FUNCTION: Calcium/calmodulin-dependent protein kinase that functions autonomously after Ca(2+)/calmodulin-binding and autophosphorylation, and is involved in sarcoplasmic reticulum Ca(2+) transport in skeletal muscle and may function in dendritic spine and synapse formation and neuronal plasticity. In slow-twitch muscles, is involved in regulation of sarcoplasmic reticulum (SR) Ca(2+) transport and in fast-twitch muscle participates in the control of Ca(2+) release from the SR through phosphorylation of the ryanodine receptor-coupling factor triadin. In neurons, may participate in the promotion of dendritic spine and synapse formation and maintenance of synaptic plasticity which enables long-term potentiation (LTP) and hippocampus-dependent learning (By similarity). {ECO:0000250}. PTM: Autophosphorylation of Thr-287 following activation by Ca(2+)/calmodulin. Phosphorylation of Thr-287 locks the kinase into an activated state (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. SUBUNIT: CAMK2 is composed of 4 different chains: alpha (CAMK2A), beta (CAMK2B), gamma (CAMK2G), and delta (CAMK2D). The different isoforms assemble into homo- or heteromultimeric holoenzymes composed of 12 subunits with two hexameric rings stacked one on top of the other (By similarity). {ECO:0000250}. DOMAIN: The CAMK2 protein kinases contain a unique C-terminal subunit association domain responsible for oligomerization. +P08414 KCC4_MOUSE Calcium/calmodulin-dependent protein kinase type IV (CaMK IV) (EC 2.7.11.17) (CaM kinase-GR) 469 52,628 Active site (1); Binding site (1); Chain (1); Domain (1); Glycosylation (7); Modified residue (7); Nucleotide binding (1); Region (3); Sequence conflict (2) FUNCTION: Calcium/calmodulin-dependent protein kinase that operates in the calcium-triggered CaMKK-CaMK4 signaling cascade and regulates, mainly by phosphorylation, the activity of several transcription activators, such as CREB1, MEF2D, JUN and RORA, which play pivotal roles in immune response, inflammation, and memory consolidation. In the thymus, regulates the CD4(+)/CD8(+) double positive thymocytes selection threshold during T-cell ontogeny. In CD4 memory T-cells, is required to link T-cell antigen receptor (TCR) signaling to the production of IL2, IFNG and IL4 (through the regulation of CREB and MEF2). Regulates the differentiation and survival phases of osteoclasts and dendritic cells (DCs). Mediates DCs survival by linking TLR4 and the regulation of temporal expression of BCL2. Phosphorylates the transcription activator CREB1 on 'Ser-133' in hippocampal neuron nuclei and contribute to memory consolidation and long term potentiation (LTP) in the hippocampus. Can activate the MAP kinases MAPK1/ERK2, MAPK8/JNK1 and MAPK14/p38 and stimulate transcription through the phosphorylation of ELK1 and ATF2. Can also phosphorylate in vitro CREBBP, PRM2, MEF2A and STMN1/OP18 (By similarity). May be involved in spermatogenesis. {ECO:0000250, ECO:0000269|PubMed:10932193, ECO:0000269|PubMed:11572782, ECO:0000269|PubMed:18829949, ECO:0000269|PubMed:8195196, ECO:0000269|PubMed:9727976}. PTM: Phosphorylated by CaMKK1 and CaMKK2 on Thr-196. Dephosphorylated by protein phosphatase 2A. Autophosphorylated on Ser-11 and Ser-12 (By similarity). {ECO:0000250}.; PTM: Glycosylation at Ser-185 modulates the phosphorylation of CaMK4 at Thr-196 and negatively regulates its activity toward CREB1 in basal conditions and during early inomycin stimulation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10932193}. Nucleus {ECO:0000269|PubMed:10932193}. Note=Localized in hippocampal neuron nuclei (By similarity). In spermatids, associated with chromatin and nuclear matrix. {ECO:0000250}. SUBUNIT: Monomer. Interacts with protein phosphatase 2A (PPP2CA/PPP2CB); the interaction is mutually exclusive with binding to Ca(2+)/calmodulin. {ECO:0000250}. DOMAIN: The autoinhibitory domain overlaps with the calmodulin binding region and interacts in the inactive folded state with the catalytic domain as a pseudosubstrate. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain and testis. {ECO:0000269|PubMed:10932193, ECO:0000269|PubMed:11951046}. +Q9JIN6 KCMB4_MOUSE Calcium-activated potassium channel subunit beta-4 (BK channel subunit beta-4) (BKbeta4) (Calcium-activated potassium channel, subfamily M subunit beta-4) (Charybdotoxin receptor subunit beta-4) (K(VCA)beta-4) (Maxi K channel subunit beta-4) (Slo-beta-4) 210 23,857 Chain (1); Glycosylation (2); Topological domain (3); Transmembrane (2) TRANSMEM 20 40 Helical; Name=1. {ECO:0000255}.; TRANSMEM 168 188 Helical; Name=2. {ECO:0000255}. TOPO_DOM 1 19 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 41 167 Extracellular. {ECO:0000255}.; TOPO_DOM 189 210 Cytoplasmic. {ECO:0000255}. FUNCTION: Regulatory subunit of the calcium activated potassium KCNMA1 (maxiK) channel. Modulates the calcium sensitivity and gating kinetics of KCNMA1, thereby contributing to KCNMA1 channel diversity. Decreases the gating kinetics and calcium sensitivity of the KCNMA1 channel, but with fast deactivation kinetics. May decrease KCNMA1 channel openings at low calcium concentrations but increases channel openings at high calcium concentrations. Makes KCNMA1 channel resistant to 100 nM charybdotoxin (CTX) toxin concentrations (By similarity). {ECO:0000250}. PTM: Phosphorylated. Phosphorylation modulates its effect on KCNMA1 activation kinetics (By similarity). {ECO:0000250}.; PTM: N-glycosylated. A highly glycosylated form is promoted by KCNMA1. Glycosylation, which is not required for the interaction with KCNMA1 and subcellular location, increases protection against charybdotoxin (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with KCNMA1 tetramer (PubMed:10804197). There are probably 4 molecules of KCMNB4 per KCNMA1 tetramer (PubMed:10804197). Interacts with FMR1 (via N-terminus) (PubMed:25561520). {ECO:0000269|PubMed:10804197, ECO:0000269|PubMed:25561520}. DOMAIN: Resistance to charybdotoxin (CTX) toxin is mediated by the extracellular domain. {ECO:0000250}. +P16388 KCNA1_MOUSE Potassium voltage-gated channel subfamily A member 1 (MBK1) (MKI) (Voltage-gated potassium channel subunit Kv1.1) 495 56,409 Chain (1); Glycosylation (1); Intramembrane (2); Lipidation (1); Modified residue (5); Motif (2); Natural variant (1); Region (2); Topological domain (8); Transmembrane (6) INTRAMEM 360 371 Helical; Name=Pore helix. {ECO:0000250|UniProtKB:P63142}.; INTRAMEM 372 379 {ECO:0000250|UniProtKB:P63142}. TRANSMEM 165 186 Helical; Name=Segment S1. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 221 242 Helical; Name=Segment S2. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 254 274 Helical; Name=Segment S3. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 288 308 Helical; Voltage-sensor; Name=Segment S4. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 324 345 Helical; Name=Segment S5. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 387 415 Helical; Name=Segment S6. {ECO:0000250|UniProtKB:P63142}. TOPO_DOM 1 164 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 187 220 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 243 253 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 275 287 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 309 323 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 346 359 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 380 386 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 416 495 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}. FUNCTION: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain and the central nervous system, but also in the kidney. Contributes to the regulation of the membrane potential and nerve signaling, and prevents neuronal hyperexcitability (PubMed:9736643, PubMed:9581771 PubMed:10191303, PubMed:12611922, PubMed:21966978, PubMed:22158511, PubMed:23473320). Forms tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane (PubMed:15361858). Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNA1, KCNA2, KCNA4, KCNA5, KCNA6, KCNA7, and possibly other family members as well; channel properties depend on the type of alpha subunits that are part of the channel. Channel properties are modulated by cytoplasmic beta subunits that regulate the subcellular location of the alpha subunits and promote rapid inactivation of delayed rectifier potassium channels (PubMed:15361858). In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes, making it difficult to assign currents observed in intact tissues to any particular potassium channel family member. Homotetrameric KCNA1 forms a delayed-rectifier potassium channel that opens in response to membrane depolarization, followed by slow spontaneous channel closure (PubMed:7517498, PubMed:15361858). In contrast, a heterotetrameric channel formed by KCNA1 and KCNA4 shows rapid inactivation (By similarity). Regulates neuronal excitability in hippocampus, especially in mossy fibers and medial perforant path axons, preventing neuronal hyperexcitability (PubMed:23466697). May function as down-stream effector for G protein-coupled receptors and inhibit GABAergic inputs to basolateral amygdala neurons (By similarity). May contribute to the regulation of neurotransmitter release, such as gamma-aminobutyric acid (GABA) release (By similarity). Plays a role in regulating the generation of action potentials and preventing hyperexcitability in myelinated axons of the vagus nerve, and thereby contributes to the regulation of heart contraction (PubMed:20392939, PubMed:22641786, PubMed:25377007). Required for normal neuromuscular responses (PubMed:9736643). Regulates the frequency of neuronal action potential firing in response to mechanical stimuli, and plays a role in the perception of pain caused by mechanical stimuli, but does not play a role in the perception of pain due to heat stimuli (PubMed:23473320). Required for normal responses to auditory stimuli and precise location of sound sources, but not for sound perception (PubMed:21966978, PubMed:22396426). The use of toxins that block specific channels suggest that it contributes to the regulation of the axonal release of the neurotransmitter dopamine (PubMed:21233214). Required for normal postnatal brain development and normal proliferation of neuronal precursor cells in the brain (PubMed:8995755, PubMed:17250763, PubMed:17315199, PubMed:22411008). Plays a role in the reabsorption of Mg(2+) in the distal convoluted tubules in the kidney and in magnesium ion homeostasis, probably via its effect on the membrane potential (By similarity). {ECO:0000250|UniProtKB:P10499, ECO:0000250|UniProtKB:Q09470, ECO:0000269|PubMed:10191303, ECO:0000269|PubMed:12611922, ECO:0000269|PubMed:15361858, ECO:0000269|PubMed:17250763, ECO:0000269|PubMed:17315199, ECO:0000269|PubMed:20392939, ECO:0000269|PubMed:21233214, ECO:0000269|PubMed:21966978, ECO:0000269|PubMed:22158511, ECO:0000269|PubMed:22396426, ECO:0000269|PubMed:22411008, ECO:0000269|PubMed:22641786, ECO:0000269|PubMed:23466697, ECO:0000269|PubMed:23473320, ECO:0000269|PubMed:25377007, ECO:0000269|PubMed:7517498, ECO:0000269|PubMed:8995755, ECO:0000269|PubMed:9581771, ECO:0000269|PubMed:9736643}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:P10499}.; PTM: Palmitoylated on Cys-243; which may be required for membrane targeting. {ECO:0000250|UniProtKB:Q09470}.; PTM: Phosphorylated on tyrosine residues. Phosphorylation increases in response to NRG1; this inhibits channel activity (PubMed:22158511). Phosphorylation at Ser-446 regulates channel activity by down-regulating expression at the cell membrane (By similarity). {ECO:0000250|UniProtKB:Q09470, ECO:0000269|PubMed:22158511}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15361858, ECO:0000269|PubMed:7517498}; Multi-pass membrane protein {ECO:0000305}. Cell projection, axon {ECO:0000269|PubMed:20392939, ECO:0000269|PubMed:21233214, ECO:0000269|PubMed:8046438, ECO:0000269|PubMed:8361541, ECO:0000269|PubMed:9581771, ECO:0000269|PubMed:9736643}. Membrane {ECO:0000269|PubMed:22158511}. Perikaryon {ECO:0000269|PubMed:12611922, ECO:0000269|PubMed:8046438}. Cell projection, dendrite {ECO:0000269|PubMed:8046438}. Cell junction {ECO:0000269|PubMed:8046438}. Cell junction, synapse {ECO:0000269|PubMed:8046438}. Cytoplasmic vesicle {ECO:0000269|PubMed:12611922}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P10499}. Cell junction, synapse, presynaptic cell membrane {ECO:0000250|UniProtKB:P10499}. Note=Homotetrameric KCNA1 is primarily located in the endoplasmic reticulum. Interaction with KCNA2 and KCNAB2 or with KCNA4 and KCNAB2 promotes expression at the cell membrane (By similarity). Detected at axon terminals (PubMed:21233214). {ECO:0000250|UniProtKB:P10499, ECO:0000269|PubMed:21233214}. SUBUNIT: Homotetramer and heterotetramer with other channel-forming alpha subunits, such as KCNA2, KCNA4, KCNA5, KCNA6 and KCNA7 (PubMed:8361541). Channel activity is regulated by interaction with the beta subunits KCNAB1 and KCNAB2 (PubMed:15361858). Identified in a complex with KCNA2 and KCNAB2. Interacts (via C-terminus) with the PDZ domains of DLG1, DLG2 and DLG4 (By similarity). Interacts with LGI1 within a complex containing LGI1, KCNA4 and KCNAB1 (By similarity). Interacts (via N-terminus) with STX1A; this promotes channel inactivation (By similarity). Interacts (via N-terminus) with the heterodimer formed by GNB1 and GNG2; this promotes channel inactivation (By similarity). Can interact simultaneously with STX1A and the heterodimer formed by GNB1 and GNG2 (By similarity). Interacts (via cytoplasmic N-terminal domain) with KCNRG; this inhibits channel activity (By similarity). Interacts with ANK3; this inhibits channel activity (PubMed:23903368). {ECO:0000250|UniProtKB:P10499, ECO:0000250|UniProtKB:Q09470, ECO:0000269|PubMed:15361858, ECO:0000269|PubMed:23903368, ECO:0000269|PubMed:8361541, ECO:0000305}. DOMAIN: The cytoplasmic N-terminus is important for tetramerization and for interaction with the beta subunits that promote rapid channel closure. {ECO:0000250|UniProtKB:P10499}.; DOMAIN: The transmembrane segment S4 functions as voltage-sensor and is characterized by a series of positively charged amino acids at every third position. Channel opening and closing is effected by a conformation change that affects the position and orientation of the voltage-sensor paddle formed by S3 and S4 within the membrane. A transmembrane electric field that is positive inside would push the positively charged S4 segment outwards, thereby opening the pore, while a field that is negative inside would pull the S4 segment inwards and close the pore. Changes in the position and orientation of S4 are then transmitted to the activation gate formed by the inner helix bundle via the S4-S5 linker region. {ECO:0000250|UniProtKB:P63142}. TISSUE SPECIFICITY: Detected in brain (PubMed:21483673, PubMed:22158511). Detected in the juxtaparanodal regions of the nodes of Ranvier in myelinated axons (PubMed:8361541, PubMed:8046438). Detected in the paranodal region in sciatic nerve (PubMed:9736643). Detected on cell bodies in cerebellum, dorsal and ventral cochlear nucleus, pontine reticular nucleus, mesencephalic trigeminal nucleus, motor trigeminal nucleus and the pricipal sensory trigeminal nucleus (PubMed:8046438). Detected in terminal fields of basket cells in the cerebellum corpus medullare (PubMed:8361541, PubMed:8046438, PubMed:9581771). Detected in hippocampus CA3 pyramidal neurons and in the hilus and stratum moleculare of the dentate gyrus (PubMed:8046438, PubMed:9581771, PubMed:14686897). Detected in the central nucleus and the external nucleus of the inferior colliculus (PubMed:8046438, PubMed:21966978). Detected in fiber tracts in the optic tract, external medullary lamina, stria terminalis, medulla, ventral pallidum and substantia nigra (PubMed:8046438). Detected in neurons from dorsal root ganglion (PubMed:23473320). Detected in neurons in the medial nucleus of the trapezoid body (PubMed:12611922). Detected in midbrain dopamine neuron axon terminals (PubMed:21233214). Detected in brain cortex (PubMed:8046438, PubMed:14686897). Detected in brainstem (PubMed:8361541). Detected in juxtaparanodal regions of the nodes of Ranvier in the vagus nerve, but only at very low levels in the heart (PubMed:20392939, PubMed:22641786). Detected in the islet of Langerhans (PubMed:21483673). Detected at the luminal membrane in distal convoluted tubules in the kidney (at protein level) (PubMed:19307729). Detected in brain (PubMed:2451788, PubMed:9581771). Detected in hippocampus, thalamus, neocortex and ventral brain cortex, including the piriform and entorhinal cortex and the amygdala (PubMed:14686897). Detected in midbrain dopamine neurons (PubMed:21233214). Detected in heart atrium, ventricle, sinoatrial node and atrioventricular node (PubMed:20392939). Detected in the islet of Langerhans (PubMed:21483673). {ECO:0000269|PubMed:12611922, ECO:0000269|PubMed:14686897, ECO:0000269|PubMed:19307729, ECO:0000269|PubMed:20392939, ECO:0000269|PubMed:21233214, ECO:0000269|PubMed:21483673, ECO:0000269|PubMed:21966978, ECO:0000269|PubMed:22158511, ECO:0000269|PubMed:22641786, ECO:0000269|PubMed:23473320, ECO:0000269|PubMed:2451788, ECO:0000269|PubMed:8046438, ECO:0000269|PubMed:8361541, ECO:0000269|PubMed:9581771, ECO:0000269|PubMed:9736643}. DISEASE: Note=A spontaneous mutation leading to a frameshift and truncation of Kcna2 causes megencephaly with a 25% increase of brain weight relative to wild-type. Especially the hippocampus shows increased proliferation of neurons and astrocytes, leading to increased brain volume (PubMed:17315199). Mutant mice appear normal at birth. After 3-4 weeks, they display low body weight, a subtle shakiness in their gait, a preference for a strange sitting position that is maintained for periods ranging from 30 seconds to several minutes, excessive lacrimation and acoustic startle hypersensitivity (PubMed:8995755, PubMed:21966978). The increase in the acoustic startle response is down-regulated by treatment with the anti-epileptic drug valproate (PubMed:21966978). Mutant mice display an abnormal electro-encephalogram with single spikes and waves, when anesthesized (PubMed:21966978). The electric activity of mossy cells from the dentate hilus region is altered and shows increased firing of action potentials, probably due to the absence of functional Kcna1 channels (PubMed:14686897). Heterozygotes show mechanical allodynia, but no increased sensitivity to heat (PubMed:23473320). Homozygotes show no alteration of the islet of Langerhans structure, of the basal levels of insulin secretion and blood glucose levels (PubMed:21483673). Compared to wild-type, they display moderately increased insulin secretion in response to a glucose stimulus (PubMed:21483673). Besides, the frequency of beta cell action potentials is increased (PubMed:21483673). {ECO:0000269|PubMed:14686897, ECO:0000269|PubMed:17315199, ECO:0000269|PubMed:21483673, ECO:0000269|PubMed:21966978, ECO:0000269|PubMed:8995755}. +P22315 HEMH_MOUSE Ferrochelatase, mitochondrial (EC 4.99.1.1) (Heme synthase) (Protoheme ferro-lyase) 420 47,130 Active site (2); Chain (1); Erroneous initiation (1); Metal binding (4); Modified residue (6); Natural variant (1); Sequence conflict (1); Transit peptide (1) Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1. FUNCTION: Catalyzes the ferrous insertion into protoporphyrin IX. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SUBUNIT: Monomer. {ECO:0000250}. TISSUE SPECIFICITY: Erythroid and hepatic cells. DISEASE: Note=Defects in Fech are the cause of a viable autosomal recessive mutation (named Fechm1Pas or Fch) that causes jaundice and anemia. +P27782 LEF1_MOUSE Lymphoid enhancer-binding factor 1 (LEF-1) 397 44,059 Alternative sequence (1); Beta strand (1); Chain (1); Compositional bias (4); Cross-link (2); DNA binding (1); Helix (4); Modified residue (3); Mutagenesis (5); Region (1); Turn (2) FUNCTION: Participates in the Wnt signaling pathway. Activates transcription of target genes in the presence of CTNNB1 and EP300. May play a role in hair cell differentiation and follicle morphogenesis. TLE1, TLE2, TLE3 and TLE4 repress transactivation mediated by LEF1 and CTNNB1 (By similarity). Regulates T-cell receptor alpha enhancer function. Binds DNA in a sequence-specific manner. PIASG antagonizes both Wnt-dependent and Wnt-independent activation by LEF1. {ECO:0000250, ECO:0000269|PubMed:11445543}. PTM: Phosphorylated at Thr-153 and/or Ser-164 by NLK. Phosphorylation by NLK at these sites represses LEF1-mediated transcriptional activation of target genes of the canonical Wnt signaling pathway (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Note=Found in nuclear bodies upon PIASG binding. SUBUNIT: Binds the armadillo repeat of CTNNB1 and forms a stable complex. Binds TLE1, ALYREF/THOC4, MDFI and MDFIC (By similarity). Interacts with NLK (By similarity). Interacts with EP300 and PIASG. {ECO:0000250, ECO:0000269|PubMed:10966653, ECO:0000269|PubMed:11731474, ECO:0000269|PubMed:12446687}. DOMAIN: Proline-rich and acidic regions are implicated in the activation functions of RNA polymerase II transcription factors. TISSUE SPECIFICITY: Lymphocytes. Found in distinct epithelial cell compartments of the skin and is abundant in the hair-producing progenitors of the follicle. {ECO:0000269|PubMed:10498690}. +Q9QYL0 HILS1_MOUSE Spermatid-specific linker histone H1-like protein (TISP64) 170 19,203 Chain (1); Domain (1); Modified residue (1) FUNCTION: DNA-binding protein that may be implicated in chromatin remodeling and/or transcriptional regulation during spermiogenesis, the process of spermatid maturation into spermatozoa. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14636221}. Chromosome {ECO:0000269|PubMed:14636221}. TISSUE SPECIFICITY: Expressed exclusively in the testis by haploid germ cells (at protein level). {ECO:0000269|PubMed:14636221}. +Q8K2Q2 GSTO2_MOUSE Glutathione S-transferase omega-2 (GSTO-2) (EC 2.5.1.18) (Glutathione S-transferase omega 2-2) (GSTO 2-2) (Glutathione-dependent dehydroascorbate reductase) (EC 1.8.5.1) (Monomethylarsonic acid reductase) (MMA(V) reductase) (EC 1.20.4.2) 248 28,599 Active site (1); Binding site (2); Chain (1); Domain (2); Region (1) FUNCTION: Exhibits glutathione-dependent thiol transferase activity. Has high dehydroascorbate reductase activity and may contribute to the recycling of ascorbic acid. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA). {ECO:0000250|UniProtKB:Q9H4Y5}. +P47791 GSHR_MOUSE Glutathione reductase, mitochondrial (GR) (GRase) (EC 1.8.1.7) 500 53,663 Active site (1); Alternative sequence (1); Chain (1); Disulfide bond (2); Modified residue (1); Nucleotide binding (1); Sequence conflict (5); Transit peptide (1) FUNCTION: Maintains high levels of reduced glutathione in the cytosol. SUBCELLULAR LOCATION: Isoform Mitochondrial: Mitochondrion.; SUBCELLULAR LOCATION: Isoform Cytoplasmic: Cytoplasm. SUBUNIT: Homodimer; disulfide-linked. DOMAIN: Each subunit can be divided into 4 domains that are consecutive along the polypeptide chain. Domains 1 and 2 bind FAD and NADPH, respectively. Domain 4 forms the interface. +P19639 GSTM3_MOUSE Glutathione S-transferase Mu 3 (EC 2.5.1.18) (GST class-mu 3) (Glutathione S-transferase GT9.3) 218 25,702 Chain (1); Cross-link (2); Domain (2); Erroneous initiation (1); Initiator methionine (1); Region (4) FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Homodimer. +Q9D2H2 KAD7_MOUSE Adenylate kinase 7 (AK 7) (EC 2.7.4.3) (EC 2.7.4.6) (ATP-AMP transphosphorylase 7) 614 70,675 Alternative sequence (3); Binding site (3); Chain (1); Coiled coil (1); Compositional bias (3); Nucleotide binding (3); Region (4) FUNCTION: Nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. Has highest activity toward AMP, and weaker activity toward dAMP, CMP and dCMP. Also displays broad nucleoside diphosphate kinase activity. Involved in maintaining ciliary structure and function. {ECO:0000269|PubMed:18776131}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q96M32}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q96M32}. Note=Detected along the full length of sperm flagellum, where it colocalizes with alpha-tubulin. {ECO:0000250|UniProtKB:Q96M32}. +Q8VBV8 GUC1B_MOUSE Guanylyl cyclase-activating protein 2 (GCAP 2) (Guanylate cyclase activator 1B) 201 23,520 Calcium binding (3); Chain (1); Domain (5); Initiator methionine (1); Lipidation (1) FUNCTION: Stimulates guanylyl cyclase 1 (GC1) and GC2 when free calcium ions concentration is low, and GC1 and GC2 when free calcium ions concentration is elevated. This Ca(2+)-sensitive regulation of GC is a key event in recovery of the dark state of rod photoreceptors following light exposure (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Note=Membranes of outer segment. {ECO:0000250}. +Q91X72 HEMO_MOUSE Hemopexin 460 51,318 Chain (1); Disulfide bond (6); Glycosylation (6); Metal binding (4); Repeat (8); Sequence conflict (4); Signal peptide (1) FUNCTION: Binds heme and transports it to the liver for breakdown and iron recovery, after which the free hemopexin returns to the circulation. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma. +Q64221 HEN2_MOUSE Helix-loop-helix protein 2 (HEN-2) (Nescient helix loop helix 2) (NSCL-2) 135 15,004 Chain (1); Compositional bias (1); Domain (1); Sequence conflict (1) FUNCTION: May serve as DNA-binding protein and may be involved in the control of cell-type determination, possibly within the developing nervous system. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}. SUBUNIT: Efficient DNA binding requires dimerization with another bHLH protein. TISSUE SPECIFICITY: In developing neurons. +Q91VD1 LEG12_MOUSE Galectin-12 (Gal-12) 314 35,460 Alternative sequence (1); Chain (1); Domain (2); Sequence conflict (3) FUNCTION: Binds lactose. May participate in the apoptosis of adipocytes. SUBCELLULAR LOCATION: Nucleus. DOMAIN: Contains two homologous but distinct carbohydrate-binding domains. +Q61666 HIRA_MOUSE Protein HIRA (TUP1-like enhancer of split protein 1) 1015 111,767 Alternative sequence (6); Chain (1); Compositional bias (3); Modified residue (12); Region (7); Repeat (7); Sequence conflict (7) FUNCTION: Required for the periodic repression of histone gene transcription during the cell cycle (By similarity). Cooperates with ASF1A to promote replication-independent chromatin assembly. Required for the formation of senescence-associated heterochromatin foci (SAHF) and efficient senescence-associated cell cycle exit. {ECO:0000250, ECO:0000269|PubMed:16399082}. PTM: Sumoylated. {ECO:0000250}.; PTM: Phosphorylated by CDK2/CCNA1 and CDK2/CCNE1 on Thr-554 in vitro (By similarity). Also phosphorylated on Thr-554 in vivo. {ECO:0000250, ECO:0000269|PubMed:11238922}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus, PML body {ECO:0000250}. Note=Primarily, though not exclusively, localized to the nucleus (By similarity). Localizes to PML bodies immediately prior to onset of senescence (By similarity). Localizes specifically to the male nucleus in fertilized eggs. This localization persists from the initiation of sperm nucleus decondensation to pronucleus formation. {ECO:0000250, ECO:0000269|PubMed:15922569, ECO:0000269|PubMed:9731536}. SUBUNIT: Interacts with CCNA1, HIRIP3 and NFU1/HIRIP5. Part of a complex which includes ASF1A, CABIN1, histone H3.3, histone H4 and UBN1 (By similarity). Interacts with histone H2B, histone H3F3B, PAX3 and PAX7. {ECO:0000250, ECO:0000269|PubMed:9731536}. TISSUE SPECIFICITY: Expressed in cerebrum, cerebellum, heart, kidney, liver, lung and spleen. +Q9JKY5 HIP1R_MOUSE Huntingtin-interacting protein 1-related protein (HIP1-related protein) 1068 119,426 Chain (1); Coiled coil (1); Compositional bias (1); Domain (2); Modified residue (1); Region (1); Sequence conflict (1) FUNCTION: Component of clathrin-coated pits and vesicles, that may link the endocytic machinery to the actin cytoskeleton. Binds 3-phosphoinositides (via ENTH domain). May act through the ENTH domain to promote cell survival by stabilizing receptor tyrosine kinases following ligand-induced endocytosis. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Endomembrane system. Cytoplasmic vesicle, clathrin-coated vesicle membrane. Note=Membrane-associated protein, mainly localized at the endocytic compartments and in the perinuclear region. SUBUNIT: Interacts with actin. Does not interact with huntingtin (By similarity). Interacts with CLTB and HIP1. Homodimer. Homodimerization promotes actin binding. {ECO:0000250, ECO:0000269|PubMed:18790740}. DOMAIN: Binds F-actin via the talin-like I/LWEQ domain. TISSUE SPECIFICITY: Widely expressed. Expressed at lower levels in skeletal muscle and heart. The level of expression does not change appreciably during development. +P48774 GSTM5_MOUSE Glutathione S-transferase Mu 5 (EC 2.5.1.18) (Fibrous sheath component 2) (Fsc2) (GST class-mu 5) 224 26,635 Binding site (1); Chain (1); Domain (2); Modified residue (1); Region (4) FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Homodimer (By similarity). Interacts with PFKM isoform 2 and isoform 3 (via N-terminal testis-specific region) (PubMed:19889946). {ECO:0000250, ECO:0000269|PubMed:19889946}. +Q64471 GSTT1_MOUSE Glutathione S-transferase theta-1 (EC 2.5.1.18) (GST class-theta-1) 240 27,374 Binding site (1); Chain (1); Domain (2); Mutagenesis (1); Region (2); Sequence conflict (2) FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Also binds steroids, bilirubin, carcinogens and numerous organic anions. Has dichloromethane dehalogenase activity. {ECO:0000269|PubMed:20097269}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. SUBUNIT: Homodimer. TISSUE SPECIFICITY: In liver, highest expression found in central vein limiting plate hepatocytes. Also expressed in interlobular bile duct epithelial cells. In lung, expressed in Clara cells and ciliated cells of the bronchiolar epithelium and in type II alveolar cells of the lung parenchyma. +Q8VHD6 GTR10_MOUSE Solute carrier family 2, facilitated glucose transporter member 10 (Glucose transporter type 10) (GLUT-10) 536 56,579 Chain (1); Topological domain (13); Transmembrane (12) TRANSMEM 16 36 Helical; Name=1. {ECO:0000255}.; TRANSMEM 49 69 Helical; Name=2. {ECO:0000255}.; TRANSMEM 83 103 Helical; Name=3. {ECO:0000255}.; TRANSMEM 108 128 Helical; Name=4. {ECO:0000255}.; TRANSMEM 133 153 Helical; Name=5. {ECO:0000255}.; TRANSMEM 167 187 Helical; Name=6. {ECO:0000255}.; TRANSMEM 233 253 Helical; Name=7. {ECO:0000255}.; TRANSMEM 270 290 Helical; Name=8. {ECO:0000255}.; TRANSMEM 299 319 Helical; Name=9. {ECO:0000255}.; TRANSMEM 403 423 Helical; Name=10. {ECO:0000255}.; TRANSMEM 443 463 Helical; Name=11. {ECO:0000255}.; TRANSMEM 469 489 Helical; Name=12. {ECO:0000255}. TOPO_DOM 1 15 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 37 48 Extracellular. {ECO:0000255}.; TOPO_DOM 70 82 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 104 107 Extracellular. {ECO:0000255}.; TOPO_DOM 129 132 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 154 166 Extracellular. {ECO:0000255}.; TOPO_DOM 188 232 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 254 269 Extracellular. {ECO:0000255}.; TOPO_DOM 291 298 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 320 402 Extracellular. {ECO:0000255}.; TOPO_DOM 424 442 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 464 468 Extracellular. {ECO:0000255}.; TOPO_DOM 490 536 Cytoplasmic. {ECO:0000255}. FUNCTION: Facilitative glucose transporter. {ECO:0000250}. SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. +P0C6A1 GTR7_MOUSE Solute carrier family 2, facilitated glucose transporter member 7 (Glucose transporter type 7) (GLUT-7) 513 55,886 Binding site (1); Chain (1); Glycosylation (1); Region (1); Topological domain (13); Transmembrane (12) TRANSMEM 22 42 Helical. {ECO:0000255}.; TRANSMEM 79 99 Helical. {ECO:0000255}.; TRANSMEM 108 128 Helical. {ECO:0000255}.; TRANSMEM 139 159 Helical. {ECO:0000255}.; TRANSMEM 173 193 Helical. {ECO:0000255}.; TRANSMEM 199 219 Helical. {ECO:0000255}.; TRANSMEM 283 303 Helical. {ECO:0000255}.; TRANSMEM 323 343 Helical. {ECO:0000255}.; TRANSMEM 352 372 Helical. {ECO:0000255}.; TRANSMEM 381 401 Helical. {ECO:0000255}.; TRANSMEM 417 437 Helical. {ECO:0000255}.; TRANSMEM 447 467 Helical. {ECO:0000255}. TOPO_DOM 1 21 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 43 78 Extracellular. {ECO:0000255}.; TOPO_DOM 100 107 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 129 138 Extracellular. {ECO:0000255}.; TOPO_DOM 160 172 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 194 198 Extracellular. {ECO:0000255}.; TOPO_DOM 220 282 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 304 322 Extracellular. {ECO:0000255}.; TOPO_DOM 344 351 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 373 380 Extracellular. {ECO:0000255}.; TOPO_DOM 402 416 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 438 446 Extracellular. {ECO:0000255}.; TOPO_DOM 468 513 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. +Q920P5 KAD5_MOUSE Adenylate kinase isoenzyme 5 (AK 5) (EC 2.7.4.3) (EC 2.7.4.6) (ATP-AMP transphosphorylase 5) 562 63,323 Alternative sequence (1); Binding site (12); Chain (1); Nucleotide binding (6); Region (6); Sequence conflict (1) FUNCTION: Nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. Active on AMP and dAMP with ATP as a donor. When GTP is used as phosphate donor, the enzyme phosphorylates AMP, CMP, and to a small extent dCMP. Also displays broad nucleoside diphosphate kinase activity. {ECO:0000250|UniProtKB:Q9Y6K8}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y6K8}. SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P00568}. TISSUE SPECIFICITY: Brain specific. {ECO:0000250|UniProtKB:Q9Y6K8}. +Q61191 HCFC1_MOUSE Host cell factor 1 (HCF) (HCF-1) (C1 factor) [Cleaved into: HCF N-terminal chain 1; HCF N-terminal chain 2; HCF N-terminal chain 3; HCF N-terminal chain 4; HCF N-terminal chain 5; HCF N-terminal chain 6; HCF C-terminal chain 1; HCF C-terminal chain 2; HCF C-terminal chain 3; HCF C-terminal chain 4; HCF C-terminal chain 5; HCF C-terminal chain 6] 2045 210,437 Beta strand (8); Chain (12); Compositional bias (3); Cross-link (8); Domain (3); Frameshift (1); Helix (1); Initiator methionine (1); Modified residue (19); Region (4); Repeat (13); Sequence conflict (10); Site (6) FUNCTION: Involved in control of the cell cycle (PubMed:9334261, PubMed:9990006). Also antagonizes transactivation by ZBTB17 and GABP2; represses ZBTB17 activation of the p15(INK4b) promoter and inhibits its ability to recruit p300 (By similarity). Coactivator for EGR2 and GABP2 (By similarity). Tethers the chromatin modifying Set1/Ash2 histone H3 'Lys-4' methyltransferase (H3K4me) and Sin3 histone deacetylase (HDAC) complexes (involved in the activation and repression of transcription respectively) together (By similarity). As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues (By similarity). Recruits KMT2E to E2F1 responsive promoters promoting transcriptional activation and thereby facilitates G1 to S phase transition (By similarity). {ECO:0000250|UniProtKB:P51610, ECO:0000269|PubMed:9334261, ECO:0000269|PubMed:9990006}. PTM: Proteolytically cleaved at one or several PPCE--THET sites within the HCF repeats. Cleavage is promoted by O-glycosylation (By similarity). {ECO:0000250}.; PTM: O-glycosylated. GlcNAcylation by OGT promotes proteolytic processing (By similarity). {ECO:0000250}.; PTM: Ubiquitinated. Lys-1817 and Lys-1818 are ubiquitinated both via 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. BAP1 mediated deubiquitination of 'Lys-48'-linked polyubiquitin chains; deubiquitination by BAP1 does not seem to stabilize the protein (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P51610}. Cytoplasm {ECO:0000269|PubMed:9990006}. Note=HCFC1R1 modulates its subcellular localization and overexpression of HCFC1R1 leads to accumulation of HCFC1 in the cytoplasm (By similarity). Localizes to cytoplasm in trigeminal ganglia (PubMed:9990006). Non-processed HCFC1 associates with chromatin. Colocalizes with CREB3 and CANX in the ER. {ECO:0000250|UniProtKB:P51610, ECO:0000269|PubMed:9990006}.; SUBCELLULAR LOCATION: Note=(Microbial infection) In trigeminal ganglia, becoming nuclear upon HSV reactivation from the latent state. {ECO:0000269|PubMed:9990006}. SUBUNIT: Composed predominantly of six polypeptides ranging from 110 to 150 kDa and a minor 300 kDa polypeptide (PubMed:9334261). The majority of N- and C-terminal cleavage products remain tightly, albeit non-covalently, associated (By similarity). Interacts with POU2F1, CREB3, ZBTB17, EGR2, E2F4, CREBZF, SP1, GABP2, Sin3 HDAC complex (SIN3A, HDAC1, HDAC2, SUDS3), SAP30, SIN3B and FHL2 (By similarity). Component of a MLL1 complex, composed of at least the core components KMT2A/MLL1, ASH2L, HCFC1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, DPY30, E2F6, HCFC2, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MEN1, MGA, KAT8, PELP1, PHF20, PRP31, RING2, RUVBL1, RUVBL2, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10 (By similarity). Component of a THAP1/THAP3-HCFC1-OGT complex that is required for the regulation of the transcriptional activity of RRM1 (By similarity). Interacts directly with THAP3 (via its HBM) (By similarity). Interacts (via the Kelch-repeat domain) with THAP1 (via the HBM); the interaction recruits HCHC1 to the RRM1 (By similarity). Interacts directly with OGT; the interaction, which requires the HCFC1 cleavage site domain, glycosylates and promotes the proteolytic processing of HCFC1 and retains OGT in the nucleus (By similarity). Component of the SET1 complex, at least composed of the catalytic subunit (SETD1A or SETD1B), WDR5, WDR82, RBBP5, ASH2L, CXXC1, HCFC1 and DPY30 (By similarity). Component of the NSL complex at least composed of MOF/KAT8, KANSL1, KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT, WDR5 and HCFC1 (By similarity). Part of a complex composed at least of ASCL2, EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; this complex may have a histone H3-specific methyltransferase activity (By similarity). Interacts with TET2 and TET3 (By similarity). Interacts with HCFC1R1 (By similarity). Interacts with THAP11 (PubMed:18585351). Interacts (via Kelch domain) with KMT2E (via HBM motif) (By similarity). Interacts with E2F1 (By similarity). {ECO:0000250|UniProtKB:P51610, ECO:0000269|PubMed:18585351, ECO:0000269|PubMed:9334261}. DOMAIN: The HCF repeat is a highly specific proteolytic cleavage signal. {ECO:0000250|UniProtKB:P51610}.; DOMAIN: The kelch repeats fold into a 6-bladed kelch beta-propeller called the beta-propeller domain which mediates interaction with HCFC1R1. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in liver, pituitary gland, skeletal muscle, kidney, eye and brain (at protein level). Also observed at low level in heart, spleen and lung. {ECO:0000269|PubMed:9334261, ECO:0000269|PubMed:9990006}. +Q61425 HCDH_MOUSE Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial (HCDH) (EC 1.1.1.35) (Medium and short-chain L-3-hydroxyacyl-coenzyme A dehydrogenase) (Short-chain 3-hydroxyacyl-CoA dehydrogenase) 314 34,464 Binding site (9); Chain (1); Erroneous initiation (1); Modified residue (23); Nucleotide binding (1); Sequence conflict (5); Site (1); Transit peptide (1) Lipid metabolism; fatty acid beta-oxidation. FUNCTION: Plays an essential role in the mitochondrial beta-oxidation of short chain fatty acids. Exerts it highest activity toward 3-hydroxybutyryl-CoA. PTM: Succinylation at Lys-81, adjacent to a coenzyme A binding site. Desuccinylated by SIRT5. SUBCELLULAR LOCATION: Mitochondrion matrix. SUBUNIT: Homodimer. {ECO:0000250}. +Q9JHD1 KAT2B_MOUSE Histone acetyltransferase KAT2B (EC 2.3.1.48) (Histone acetyltransferase PCAF) (Histone acetylase PCAF) (Lysine acetyltransferase 2B) (P300/CBP-associated factor) (P/CAF) (Spermidine acetyltransferase KAT2B) (EC 2.3.1.57) 813 91,769 Active site (1); Chain (1); Compositional bias (1); Domain (2); Helix (6); Region (3); Sequence conflict (5); Turn (1) FUNCTION: Functions as a histone acetyltransferase (HAT) to promote transcriptional activation. Has significant histone acetyltransferase activity with core histones (H3 and H4), and also with nucleosome core particles. Also acetylates non-histone proteins, such as ACLY, PLK4 and TBX5. Inhibits cell-cycle progression and counteracts the mitogenic activity of the adenoviral oncoprotein E1A. Acts as a circadian transcriptional coactivator which enhances the activity of the circadian transcriptional activators: NPAS2-ARNTL/BMAL1 and CLOCK-ARNTL/BMAL1 heterodimers. Involved in heart and limb development by mediating acetylation of TBX5, acetylation regulating nucleocytoplasmic shuttling of TBX5. Acts as a negative regulator of centrosome amplification by mediating acetylation of PLK4. Also acetylates spermidine (By similarity). {ECO:0000250|UniProtKB:Q92831}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92831}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q92831}. Note=Mainly localizes to the nucleus. Also localizes to centrosomes in late G1 and around the G1/S transition, coinciding with the onset of centriole formation. {ECO:0000250|UniProtKB:Q92831}. SUBUNIT: Interacts with BCAS3. Interacts with SIRT1. Interacts with EP300, CREBBP and DDX17. Component of a large chromatin remodeling complex, at least composed of MYSM1, KAT2B/PCAF, RBM10 and KIF11/TRIP5. Interacts with KLF1; the interaction does not acetylate KLF1 and there is no enhancement of its transactivational activity. Interacts with NFE4. Interacts with MECOM. Interacts with NR2C2 (hypophosphorylated and unsumoylated form); the interaction promotes the transactivation activity of NR2C2. Interacts with NFE4. Interacts with MECOM. Interacts with E2F1; the interaction acetylates E2F1 augmenting its DNA-binding and transcriptional activity. Interacts with NPAS2, ARNTL/BMAL1 and CLOCK (By similarity). Interacts (unsumoylated form) with NR2C1; the interaction promotes transactivation activity. Interacts with CEBPB (By similarity). Interacts with NR4A3 (PubMed:12709428). Interacts with TBX5 (By similarity). Interacts with PLK4 (By similarity). {ECO:0000250|UniProtKB:Q92831, ECO:0000269|PubMed:12709428, ECO:0000269|PubMed:17187077, ECO:0000269|PubMed:18682553}. +Q8CHK4 KAT5_MOUSE Histone acetyltransferase KAT5 (EC 2.3.1.48) (60 kDa Tat-interactive protein) (Tip60) (Histone acetyltransferase HTATIP) (Lysine acetyltransferase 5) 513 58,598 Active site (1); Alternative sequence (3); Binding site (2); Chain (1); Cross-link (2); Domain (1); Modified residue (5); Region (3); Zinc finger (1) FUNCTION: Catalytic subunit of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. The NuA4 complex ATPase and helicase activities seem to be, at least in part, contributed by the association of RUVBL1 and RUVBL2 with EP400. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Directly acetylates and activates ATM. Relieves NR1D2-mediated inhibition of APOC3 expression by acetylating NR1D2. Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AFZ from the nucleosome. Promotes FOXP3 acetylation and positively regulates its transcriptional repressor activity. Acetylates RAN at 'Lys-134'. {ECO:0000250|UniProtKB:Q92993}. PTM: Sumoylated by UBE2I at Lys-430 and Lys-451, leading to increase of its histone acetyltransferase activity in UV-induced DNA damage response, as well as its translocation to nuclear bodies. {ECO:0000250}.; PTM: Phosphorylated on Ser-86 and Ser-90; enhanced during G2/M phase. The phosphorylated form has a higher HAT activity. {ECO:0000250|UniProtKB:Q9H7Z6}.; PTM: Ubiquitinated by MDM2, leading to its proteasome-dependent degradation. {ECO:0000250}.; PTM: Autoacetylation at Lys-327 is required for proper function. {ECO:0000250|UniProtKB:Q9H7Z6}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92993}. Nucleus, nucleolus {ECO:0000269|PubMed:12036595}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q92993}. Note=Upon stimulation with EDN1, it is exported from the nucleus to the perinuclear region. {ECO:0000250|UniProtKB:Q92993}. SUBUNIT: Component of the NuA4 histone acetyltransferase complex which contains the catalytic subunit KAT5/TIP60 and the subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6. HTATTIP/TIP60, EPC1, and ING3 together constitute a minimal HAT complex termed Piccolo NuA4. The NuA4 complex interacts with MYC. Interacts with ATM. Interacts with JADE1. Interacts with PLA2G4A/CPLA2, EDNRA and HDAC7. Interacts with the cytoplasmic tail of APP and APBB1/FE65. Interacts with TRIM24 and TRIM68. Forms a complex with SENP6 and UBE2I in response to UV irradiation. Identified in a complex with HINT1. Interacts with ATF2 and CUL3. Interacts with NR1D2 (via N-terminus). Component of a SWR1-like complex (By similarity). Interacts with FOXP3. Interacts with ZBTB49 (By similarity). {ECO:0000250|UniProtKB:Q92993, ECO:0000250|UniProtKB:Q99MK2, ECO:0000269|PubMed:19696312}. TISSUE SPECIFICITY: Expressed in testis, heart, brain, kidney and liver. Weakly expressed in lung. {ECO:0000269|PubMed:12036595}. +Q8BZ21 KAT6A_MOUSE Histone acetyltransferase KAT6A (EC 2.3.1.48) (MOZ, YBF2/SAS3, SAS2 and TIP60 protein 3) (MYST-3) (Monocytic leukemia zinc finger homolog) (Monocytic leukemia zinc finger protein) 2003 224,919 Active site (1); Binding site (1); Chain (1); Compositional bias (10); Cross-link (2); Domain (2); Modified residue (17); Region (11); Zinc finger (3) FUNCTION: Histone acetyltransferase that acetylates lysine residues in histone H3 and histone H4 (in vitro). Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. May act as a transcriptional coactivator for RUNX1 and RUNX2 (By similarity). Acetylates p53/TP53 at 'Lys-120' and 'Lys-382' and controls its transcriptional activity via association with PML (By similarity). {ECO:0000250|UniProtKB:Q92794, ECO:0000269|PubMed:11742995}. PTM: Autoacetylated. Autoacetylation at Lys-603 is required for proper function. {ECO:0000250|UniProtKB:Q9H7Z6}.; PTM: Phosphorylation at Thr-369 by PKB/AKT1 inhibits its interaction with PML and negatively regulates its acetylation activity towards p53/TP53. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00837}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q92794}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q92794}. Nucleus, PML body {ECO:0000250|UniProtKB:Q92794}. Note=Recruited into PML body after DNA damage. {ECO:0000250|UniProtKB:Q92794}. SUBUNIT: Component of the MOZ/MORF complex composed at least of ING5, KAT6A, KAT6B, MEAF6 and one of BRPF1, BRD1/BRPF2 and BRPF3 (By similarity). Interacts with RUNX2 (By similarity). Interacts with RUNX1; phosphorylation of RUNX1 enhances the interaction. Interacts with p53/TP53 (By similarity). Interacts with PML and this interaction positively regulates its acetylation activity towards p53/TP53 (By similarity). {ECO:0000250|UniProtKB:Q92794}. DOMAIN: The N-terminus is involved in transcriptional activation while the C-terminus is involved in transcriptional repression. {ECO:0000250}. +Q91WA3 HDA11_MOUSE Histone deacetylase 11 (HD11) (EC 3.5.1.98) 347 39,157 Active site (1); Chain (1); Region (1) FUNCTION: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with HDAC6. {ECO:0000250}. +Q5DTY9 KCD16_MOUSE BTB/POZ domain-containing protein KCTD16 427 48,972 Chain (1); Domain (1); Modified residue (5); Sequence conflict (1) FUNCTION: Auxiliary subunit of GABA-B receptors that determine the pharmacology and kinetics of the receptor response. Increases agonist potency and markedly alter the G-protein signaling of the receptors by accelerating onset and promoting desensitization. {ECO:0000269|PubMed:20400944}. SUBCELLULAR LOCATION: Cell junction, synapse, presynaptic cell membrane {ECO:0000269|PubMed:20400944}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000269|PubMed:20400944}. Note=Colocalizes with GABRB1. {ECO:0000269|PubMed:20400944}. SUBUNIT: Homopentamer; forms an open pentamer (By similarity). In contrast to other BTB domain-containing proteins, does not interact with CUL3 (By similarity). Interacts as a tetramer with GABRB1 and GABRB2 (PubMed:20400944). {ECO:0000250|UniProtKB:Q68DU8, ECO:0000269|PubMed:20400944}. TISSUE SPECIFICITY: Expressed in the brain, mainly in the hippocampus. {ECO:0000269|PubMed:20400944}. +Q9JJ57 KCIP1_MOUSE Kv channel-interacting protein 1 (KChIP1) (A-type potassium channel modulatory protein 1) (Potassium channel-interacting protein 1) 227 26,831 Alternative sequence (3); Calcium binding (2); Chain (1); Domain (4); Erroneous initiation (1); Region (1); Sequence conflict (2) FUNCTION: Regulatory subunit of Kv4/D (Shal)-type voltage-gated rapidly inactivating A-type potassium channels. Regulates channel density, inactivation kinetics and rate of recovery from inactivation in a calcium-dependent and isoform-specific manner. Modulates KCND2/Kv4.2 currents (PubMed:14572458). In vitro, modulates KCND1/Kv4.1 currents (By similarity). Increases the presence of KCND2 at the cell surface. {ECO:0000250|UniProtKB:Q9NZI2, ECO:0000269|PubMed:14572458}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14572458}; Peripheral membrane protein {ECO:0000269|PubMed:14572458}. Cytoplasm {ECO:0000269|PubMed:14572458}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q8R426}. SUBUNIT: Component of heteromultimeric potassium channels (PubMed:19713751). Identified in potassium channel complexes containing KCND1, KCND2, KCND3, KCNIP1, KCNIP2, KCNIP3, KCNIP4, DPP6 and DPP10 (PubMed:19713751). Part of a heterooctamer composed of the tetrameric channel and four KCNIP1 chains (By similarity). Interacts with KCND3 and the N-terminal domain of KCND2. Probably part of a complex consisting of KCNIP1, KCNIP2 isoform 3 and KCND2. Self-associates to form homodimers and homotetramers. Interacts with KCNIP2 isoform 3 in a calcium-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q9NZI2, ECO:0000269|PubMed:19713751}. TISSUE SPECIFICITY: Expressed in brain. Found in a subpopulation of neurons widely distributed and enriched in Purkinje cells of the cerebellum and in the reticular thalamic and medial habenular nuclei. {ECO:0000269|PubMed:14572458, ECO:0000269|PubMed:15363885}. +Q9JJ69 KCIP2_MOUSE Kv channel-interacting protein 2 (KChIP2) (A-type potassium channel modulatory protein 2) (Potassium channel-interacting protein 2) 270 30,946 Alternative sequence (3); Calcium binding (2); Chain (1); Domain (4); Lipidation (2); Modified residue (1); Region (1); Sequence conflict (17) FUNCTION: Regulatory subunit of Kv4/D (Shal)-type voltage-gated rapidly inactivating A-type potassium channels. Modulates channel density, inactivation kinetics and rate of recovery from inactivation in a calcium-dependent and isoform-specific manner (PubMed:20943905, PubMed:23713033). In vitro, modulates KCND2/Kv4.2 and KCND3/Kv4.3 currents. Involved in KCND2 and KCND3 trafficking to the cell surface. Essential for the expression of I(To) currents in the heart (PubMed:11747815, PubMed:23713033). Required for normal protein levels of KCND2 in the heart ventricle (PubMed:23713033). {ECO:0000250|UniProtKB:Q9NS61, ECO:0000269|PubMed:11747815, ECO:0000269|PubMed:20943905, ECO:0000269|PubMed:23713033}. PTM: Palmitoylated. Palmitoylation enhances association with the plasma membrane. {ECO:0000250|UniProtKB:Q9JM59}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9JM59}; Lipid-anchor {ECO:0000250|UniProtKB:Q9JM59}. Note=Detected on lipid rafts (By similarity). {ECO:0000250|UniProtKB:Q9JM59}. SUBUNIT: Component of heteromultimeric potassium channels (PubMed:19713751, PubMed:20943905). Identified in potassium channel complexes containing KCND1, KCND2, KCND3, KCNIP1, KCNIP2, KCNIP3, KCNIP4, DPP6 and DPP10 (PubMed:19713751). The KCND2-KCNIP2 channel complex contains four KCND2 and four KCNIP2 subunits. Probably part of a complex consisting of KCNIP1, KCNIP2 isoform 3 and KCND2. At least isoform 2 and isoform 3 can self-associate to form homodimers and homotetramers. Isoform 3 interacts with KCNIP1 in a calcium-dependent manner (By similarity). Interacts with KCND2 (PubMed:20943905). Isoform 1 and isoform 3 interact with KCND3 isoform 1. {ECO:0000250|UniProtKB:Q9NS61, ECO:0000269|PubMed:11909823, ECO:0000269|PubMed:19713751, ECO:0000269|PubMed:20943905}. TISSUE SPECIFICITY: Detected in brain (at protein level) (PubMed:23713033). Expressed in brain. Highly expressed in layer IV of the cerebral cortex and in striatum and hippocampus, but expressed at low levels in cerebellum. Also expressed in heart. According to PubMed:11747815 expressed in heart at much higher levels than in brain with a preferential expression in the myocardium. {ECO:0000269|PubMed:11263977, ECO:0000269|PubMed:11747815, ECO:0000269|PubMed:15363885, ECO:0000269|PubMed:23713033}. +Q9JM63 KCJ10_MOUSE ATP-sensitive inward rectifier potassium channel 10 (Inward rectifier K(+) channel Kir4.1) (Potassium channel, inwardly rectifying subfamily J member 10) 379 42,432 Chain (1); Intramembrane (2); Motif (1); Nucleotide binding (1); Site (1); Topological domain (4); Transmembrane (2) INTRAMEM 115 126 Helical; Pore-forming; Name=H5. {ECO:0000250}.; INTRAMEM 127 133 Pore-forming. {ECO:0000250}. TRANSMEM 65 89 Helical; Name=M1. {ECO:0000250}.; TRANSMEM 143 164 Helical; Name=M2. {ECO:0000250}. TOPO_DOM 1 64 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 90 114 Extracellular. {ECO:0000250}.; TOPO_DOM 134 142 Extracellular. {ECO:0000250}.; TOPO_DOM 165 379 Cytoplasmic. {ECO:0000250}. FUNCTION: May be responsible for potassium buffering action of glial cells in the brain. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by extracellular barium and cesium (By similarity). In the kidney, together with KCNJ16, mediates basolateral K(+) recycling in distal tubules; this process is critical for Na(+) reabsorption at the tubules (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P78508}. SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P78508}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P78508}. Basolateral cell membrane {ECO:0000250|UniProtKB:P78508}. Note=In kidney distal convoluted tubules, located in the basolateral membrane where it colocalizes with KCNJ16. {ECO:0000250|UniProtKB:P78508}. SUBUNIT: Heterodimer with Kir5.1/KCNJ16; this interaction is required for KCNJ16 localization to the basolateral membrane in kidney cells. Interacts with MAGI1, alone and possibly as a heterodimer with KCNJ16; this interaction may facilitate KCNJ10/KCNJ16 potassium channel expression at the basolateral membrane in kidney cells (By similarity). Interacts with PATJ (PubMed:9647694). {ECO:0000250|UniProtKB:P78508, ECO:0000269|PubMed:9647694}. TISSUE SPECIFICITY: Widely expressed in adult brain, including in the neocortex, the stratum pyrimadale of the hippocampus and the piriform cortex. Expressed by cultured astrocytes and also by cocultured cortical neurons (at protein level). {ECO:0000269|PubMed:11169792}. +Q76I25 HIG1C_MOUSE HIG1 domain family member 1C 96 10,825 Chain (1); Domain (1); Topological domain (3); Transmembrane (2) TRANSMEM 27 44 Helical. {ECO:0000255|PROSITE-ProRule:PRU00836}.; TRANSMEM 59 81 Helical. {ECO:0000255|PROSITE-ProRule:PRU00836}. TOPO_DOM 1 26 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 45 58 Extracellular. {ECO:0000255}.; TOPO_DOM 82 96 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000255|PROSITE-ProRule:PRU00836}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00836}. +Q9JLZ6 HIC2_MOUSE Hypermethylated in cancer 2 protein (Hic-2) 619 66,766 Alternative sequence (1); Chain (1); Domain (1); Erroneous initiation (1); Modified residue (5); Region (1); Sequence caution (1); Sequence conflict (1); Zinc finger (5) FUNCTION: Transcriptional repressor. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Self-associates. Interacts with HIC1 (By similarity). {ECO:0000250}. +P43120 HHEX_MOUSE Hematopoietically-expressed homeobox protein Hhex (Homeobox protein HEX) (mHex) (Homeobox protein PRH) 271 29,987 Chain (1); Compositional bias (1); DNA binding (1); Frameshift (1); Modified residue (1); Sequence conflict (2) FUNCTION: Recognizes the DNA sequence 5'-ATTAA-3' (By similarity). Transcriptional repressor. May play a role in hematopoietic differentiation. Establishes anterior identity at two levels; acts early to enhance canonical WNT-signaling by repressing expression of TLE4, and acts later to inhibit NODAL-signaling by directly targeting NODAL. {ECO:0000250, ECO:0000269|PubMed:10804173, ECO:0000269|PubMed:16936074}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23665349}. SUBUNIT: Interacts with CD81; the interaction prevents nuclear translocation of HHEX. {ECO:0000269|PubMed:23665349}. +Q9QZR5 HIPK2_MOUSE Homeodomain-interacting protein kinase 2 (EC 2.7.11.1) (Nuclear body-associated kinase 1) (Sialophorin tail-associated nuclear serine/threonine-protein kinase) 1196 130,498 Active site (1); Alternative sequence (6); Binding site (1); Chain (1); Compositional bias (1); Cross-link (5); Domain (1); Frameshift (1); Modified residue (22); Motif (2); Mutagenesis (3); Nucleotide binding (1); Region (13); Sequence conflict (7); Site (2) FUNCTION: Serine/threonine-protein kinase involved in transcription regulation, p53/TP53-mediated cellular apoptosis and regulation of the cell cycle. Acts as a corepressor of several transcription factors, including SMAD1 and POU4F1/Brn3a and probably NK homeodomain transcription factors. Phosphorylates PDX1, ATF1, PML, p53/TP53, CREB1, CTBP1, CBX4, RUNX1, EP300, CTNNB1, HMGA1 and ZBTB4. Inhibits cell growth and promotes apoptosis through the activation of p53/TP53 both at the transcription level and at the protein level (by phosphorylation and indirect acetylation). The phosphorylation of p53/TP53 may be mediated by a p53/TP53-HIPK2-AXIN1 complex. Involved in the response to hypoxia by acting as a transcriptional co-suppressor of HIF1A. Mediates transcriptional activation of TP73. In response to TGFB, cooperates with DAXX to activate JNK. Negative regulator through phosphorylation and subsequent proteasomal degradation of CTNNB1 and the antiapoptotic factor CTBP1. In the Wnt/beta-catenin signaling pathway acts as an intermediate kinase between MAP3K7/TAK1 and NLK to promote the proteasomal degradation of MYB. Phosphorylates CBX4 upon DNA damage and promotes its E3 SUMO-protein ligase activity. Activates CREB1 and ATF1 transcription factors by phosphorylation in response to genotoxic stress. In response to DNA damage, stabilizes PML by phosphorylation. PML, HIPK2 and FBXO3 may act synergically to activate p53/TP53-dependent transactivation. Promotes angiogenesis, and is involved in erythroid differentiation, especially during fetal liver erythropoiesis. Phosphorylation of RUNX1 and EP300 stimulates EP300 transcription regulation activity. Triggers ZBTB4 protein degradation in response to DNA damage. Modulates HMGA1 DNA-binding affinity. In response to high glucose, triggers phosphorylation-mediated subnuclear localization shifting of PDX1. Involved in the regulation of eye size, lens formation and retinal lamination during late embryogenesis. {ECO:0000269|PubMed:11593421, ECO:0000269|PubMed:11780126, ECO:0000269|PubMed:14567915, ECO:0000269|PubMed:15082531, ECO:0000269|PubMed:15492043, ECO:0000269|PubMed:16917507, ECO:0000269|PubMed:20231426, ECO:0000269|PubMed:20307497, ECO:0000269|PubMed:20579985, ECO:0000269|PubMed:20637728}. PTM: Sumoylated. When conjugated it is directed to nuclear speckles. Desumoylated by SENP1. Sumoylation on Lys-32 is promoted by the E3 SUMO-protein ligase CBX4 (By similarity). {ECO:0000250}.; PTM: Autophosphorylation at Tyr-361 in the activation loop activates the kinase and promotes nuclear localization. {ECO:0000269|PubMed:23485397}.; PTM: Ubiquitinated by FBXO3, WSB1 and SIAH1, leading to rapid proteasome-dependent degradation. The degradation mediated by FBXO3, but not ubiquitination, is prevented in the presence of PML. The degradation mediated by WSB1 and SIAH1 is reversibly reduced upon DNA damage (By similarity). {ECO:0000250}.; PTM: Cleaved at Asp-923 and Asp-984 by CASP6 in a p53/TP53-dependent manner. The cleaved form lacks the autoinhibitory C-terminal domain (AID), resulting in a hyperactive kinase, which potentiates p53/TP53 Ser-46 phosphorylation and subsequent activation of the cell death machinery. SUBCELLULAR LOCATION: Nucleus, PML body {ECO:0000269|PubMed:10535925, ECO:0000269|PubMed:11078605, ECO:0000269|PubMed:14990717, ECO:0000269|PubMed:20579985, ECO:0000269|PubMed:9748262}. Cytoplasm {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 2: Nucleus. Cytoplasm. Note=Isoform 2 seems to be both nuclear and cytoplasmic. SUBUNIT: Interacts with CREB1, SIAH1, WSB1, CBX4, TRADD, p53/TP53, TP73, TP63, CREBBP, DAXX, P53DINP1, SKI, SMAD1, SMAD2 and SMAD3, but not SMAD4. Interacts with SP100; positively regulates TP53-dependent transcription (By similarity). Interacts with ATF1, PML, RUNX1, EP300, NKX1-2, NKX2-5, SPN/CD43, UBE2I, HMGA1, CTBP1, AXIN1, NLK, MYB, POU4F1, POU4F2, POU4F3, UBE2I, UBL1 and ZBTB4. Probably part of a complex consisting of p53/TP53, HIPK2 and AXIN1. {ECO:0000250, ECO:0000269|PubMed:10535925, ECO:0000269|PubMed:11078605, ECO:0000269|PubMed:11593421, ECO:0000269|PubMed:11780126, ECO:0000269|PubMed:14567915, ECO:0000269|PubMed:15082531, ECO:0000269|PubMed:15492043, ECO:0000269|PubMed:15526030, ECO:0000269|PubMed:16917507, ECO:0000269|PubMed:9748262}. TISSUE SPECIFICITY: Ubiquitous. Abundant in muscle, heart, small intestine, stomach, kidney and brain; and low in testis, skin and lung. {ECO:0000269|PubMed:11078605, ECO:0000269|PubMed:11798164, ECO:0000269|PubMed:14990717}. +Q9ERH7 HIPK3_MOUSE Homeodomain-interacting protein kinase 3 (EC 2.7.11.1) (Androgen receptor-interacting nuclear protein kinase) (ANPK) (Fas-interacting serine/threonine-protein kinase) (FIST) (Nuclear body-associated kinase 3) (Nbak3) 1192 130,081 Active site (1); Binding site (1); Chain (1); Compositional bias (1); Cross-link (3); Domain (1); Modified residue (1); Mutagenesis (3); Nucleotide binding (1); Region (5); Sequence conflict (9) FUNCTION: Serine/threonine-protein kinase involved in transcription regulation, apoptosis and steroidogenic gene expression. Phosphorylates JUN and RUNX2. Seems to negatively regulate apoptosis by promoting FADD phosphorylation. Enhances androgen receptor-mediated transcription. May act as a transcriptional corepressor for NK homeodomain transcription factors. The phosphorylation of NR5A1 activates SF1 leading to increased steroidogenic gene expression upon cAMP signaling pathway stimulation. In osteoblasts, supports transcription activation: phosphorylates RUNX2 that synergizes with SPEN/MINT to enhance FGFR2-mediated activation of the osteocalcin FGF-responsive element (OCFRE). {ECO:0000269|PubMed:11034606, ECO:0000269|PubMed:17210646, ECO:0000269|PubMed:20484411}. PTM: Autophosphorylated, but autophosphorylation is not required for catalytic activity. {ECO:0000250}.; PTM: May be sumoylated. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. SUBUNIT: Interacts with UBL1/SUMO-1 (By similarity). Interacts with and stabilizes ligand-bound androgen receptor (AR). Interacts with Nkx1-2. Interacts with FAS and DAXX. Probably part of a complex consisting of HIPK3, FAS and FADD. Binds to NR5A1/SF1, SPEN/MINT and RUNX2. {ECO:0000250, ECO:0000269|PubMed:11034606, ECO:0000269|PubMed:17210646, ECO:0000269|PubMed:20484411, ECO:0000269|PubMed:9725910, ECO:0000269|PubMed:9748262}. TISSUE SPECIFICITY: Heart, skeletal muscle, spleen, testis and lung. {ECO:0000269|PubMed:11034606}. +Q9CPS6 HINT3_MOUSE Histidine triad nucleotide-binding protein 3 (HINT-3) (EC 3.-.-.-) (HINT-4) 165 18,788 Active site (1); Chain (1); Domain (1); Initiator methionine (1); Modified residue (1); Motif (1); Nucleotide binding (2) FUNCTION: Hydrolyzes phosphoramidate and acyl-adenylate substrates. SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}. SUBUNIT: Forms dimers to octamers and even larger oligomer. {ECO:0000250}. +Q8VD75 HIP1_MOUSE Huntingtin-interacting protein 1 (HIP-1) (Huntingtin-interacting protein I) (HIP-I) 1029 115,202 Chain (1); Coiled coil (1); Domain (2); Erroneous initiation (1); Modified residue (1); Region (2); Sequence conflict (2) FUNCTION: Plays a role in clathrin-mediated endocytosis and trafficking (PubMed:11577110). Involved in regulating AMPA receptor trafficking in the central nervous system in an NMDA-dependent manner (PubMed:12839988, PubMed:17329427). Regulates presynaptic nerve terminal activity (PubMed:17928447). Enhances androgen receptor (AR)-mediated transcription (By similarity). May act as a proapoptotic protein that induces cell death by acting through the intrinsic apoptosis pathway (By similarity). Binds 3-phosphoinositides (via ENTH domain) (By similarity). May act through the ENTH domain to promote cell survival by stabilizing receptor tyrosine kinases following ligand-induced endocytosis (By similarity). May play a functional role in the cell filament networks (By similarity). May be required for differentiation, proliferation, and/or survival of somatic and germline progenitors (PubMed:11604514, PubMed:14998932, PubMed:16967501, PubMed:17928447). {ECO:0000250|UniProtKB:O00291, ECO:0000269|PubMed:11577110, ECO:0000269|PubMed:11604514, ECO:0000269|PubMed:12839988, ECO:0000269|PubMed:14998932, ECO:0000269|PubMed:16967501, ECO:0000269|PubMed:17329427}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Endomembrane system {ECO:0000250}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250}. Note=Shuttles between cytoplasm and nucleus. Nuclear translocation can be induced by AR (By similarity). {ECO:0000250}. SUBUNIT: Homodimer. Binds actin. Binds HTT (via N-terminus). This interaction is restricted to the brain. Binds to IFT57. In normal conditions, it poorly interacts with IFT57, HIP1 being strongly associated with HTT. However, in mutant HTT proteins with a long poly-Gln region, interaction between HTT and HIP1 is inhibited, promoting the interaction between HIP1 and IFT57. Interacts with CLTB (via N-terminus). Interacts (via coiled coil domain) with AR. Interacts with AP2A1, AP2A2, CLTC and HIP1R (By similarity). Interacts with GRIA1, GRIN2A AND GRIN2B. {ECO:0000250, ECO:0000269|PubMed:12839988, ECO:0000269|PubMed:17329427}. DOMAIN: The pseudo DED region (pDED) mediates the interaction with IFT57. {ECO:0000250|UniProtKB:O00291}.; DOMAIN: Binds F-actin via the talin-like I/LWEQ domain. {ECO:0000250}. TISSUE SPECIFICITY: Most abundantly expressed in brain. In brain, expressed in cortical tissue, hippocampus, the molecular layer of the cerebellum and olfactory bulb. Also expressed in spinal cord and bone marrow (at protein level). Expressed in reproductive tissues. {ECO:0000269|PubMed:11604514, ECO:0000269|PubMed:12839988, ECO:0000269|PubMed:14998932, ECO:0000269|PubMed:16967501, ECO:0000269|PubMed:9140394}. +D3YXG0 HMCN1_MOUSE Hemicentin-1 (Fibulin-6) (FIBL-6) 5634 611,561 Alternative sequence (1); Chain (1); Disulfide bond (76); Domain (59); Glycosylation (8); Signal peptide (1) FUNCTION: Promotes cleavage furrow maturation during cytokinesis in preimplantation embryos (PubMed:21215633). May play a role in the architecture of adhesive and flexible epithelial cell junctions (PubMed:17015624). May play a role during myocardial remodeling by imparting an effect on cardiac fibroblast migration (PubMed:24951538). {ECO:0000269|PubMed:17015624, ECO:0000269|PubMed:21215633, ECO:0000269|PubMed:24951538}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000269|PubMed:17015624, ECO:0000269|PubMed:24951538}. Cytoplasm {ECO:0000269|PubMed:17015624}. Cell junction {ECO:0000269|PubMed:17015624}. Cleavage furrow {ECO:0000269|PubMed:21215633}. Note=The antibody used in PubMed:17015624 and PubMed:21215633 to determine subcellular location does not distinguish between HMCN1 and HMCN2. {ECO:0000269|PubMed:17015624, ECO:0000269|PubMed:21215633}. TISSUE SPECIFICITY: Expressed in vascular endothelial cells in coronary arteries and sparsely in endocardial endothelium (at protein level) (PubMed:24951538). Expressed in skin, tongue, lung and eye (PubMed:17015624). {ECO:0000269|PubMed:17015624, ECO:0000269|PubMed:24951538}. +P51163 HEM4_MOUSE Uroporphyrinogen-III synthase (UROIIIS) (UROS) (EC 4.2.1.75) (Hydroxymethylbilane hydrolyase [cyclizing]) (Uroporphyrinogen-III cosynthase) 265 28,504 Chain (1) Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 3/4. FUNCTION: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III, the branch point for the various sub-pathways leading to the wide diversity of porphyrins. Porphyrins act as cofactors for a multitude of enzymes that perform a variety of processes within the cell such as methionine synthesis (vitamin B12) or oxygen transport (heme) (By similarity). {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. +Q6PHZ8 KCIP4_MOUSE Kv channel-interacting protein 4 (KChIP4) (A-type potassium channel modulatory protein 4) (Calsenilin-like protein) (Potassium channel-interacting protein 4) 250 28,756 Alternative sequence (3); Beta strand (2); Calcium binding (3); Chain (1); Domain (4); Helix (10); Modified residue (2); Region (2); Sequence conflict (2) FUNCTION: Regulatory subunit of Kv4/D (Shal)-type voltage-gated rapidly inactivating A-type potassium channels, such as KCND2/Kv4.2 and KCND3/Kv4.3 (PubMed:19109250). Modulates channel expression at the cell membrane, gating characteristics, inactivation kinetics and rate of recovery from inactivation in a calcium-dependent and isoform-specific manner. {ECO:0000269|PubMed:19109250, ECO:0000269|PubMed:20045463, ECO:0000269|PubMed:20943905}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6PIL6}; Peripheral membrane protein {ECO:0000305}. Cytoplasm {ECO:0000250|UniProtKB:Q6PIL6}. SUBUNIT: Component of heteromultimeric potassium channels (PubMed:19713751, PubMed:20943905). Identified in potassium channel complexes containing KCND1, KCND2, KCND3, KCNIP1, KCNIP2, KCNIP3, KCNIP4, DPP6 and DPP10 (PubMed:19713751). Interacts with the C-terminus of PSEN2 and probably PSEN1 (By similarity). Interacts with KCND2 and KCND3. {ECO:0000250|UniProtKB:Q6PIL6, ECO:0000269|PubMed:11805342, ECO:0000269|PubMed:19109250, ECO:0000269|PubMed:20045463, ECO:0000269|PubMed:20943905}. DOMAIN: The KIS (K-channel inactivation suppressor) domain is required for converting A-type Kv4 current to a slowly inactivating delayed rectifier potassium current. {ECO:0000269|PubMed:11805342}. TISSUE SPECIFICITY: Expressed in brain. Highly expressed by neurons in layers II-IV of cortex and in hippocampus, thalamus and the Purkinje cell layer of the cerebellum. {ECO:0000269|PubMed:11805342, ECO:0000269|PubMed:11847232, ECO:0000269|PubMed:15363885}. +Q61743 KCJ11_MOUSE ATP-sensitive inward rectifier potassium channel 11 (Inward rectifier K(+) channel Kir6.2) (Potassium channel, inwardly rectifying subfamily J member 11) 390 43,562 Chain (1); Intramembrane (2); Modified residue (2); Motif (1); Sequence conflict (1); Site (1); Topological domain (4); Transmembrane (2) INTRAMEM 117 128 Helical; Pore-forming; Name=H5. {ECO:0000250}.; INTRAMEM 129 135 Pore-forming. {ECO:0000250}. TRANSMEM 69 93 Helical; Name=M1. {ECO:0000250}.; TRANSMEM 145 166 Helical; Name=M2. {ECO:0000250}. TOPO_DOM 1 68 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 94 116 Extracellular. {ECO:0000250}.; TOPO_DOM 136 144 Extracellular. {ECO:0000250}.; TOPO_DOM 167 390 Cytoplasmic. {ECO:0000250}. FUNCTION: This receptor is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by extracellular barium. Can form cardiac and smooth muscle-type KATP channels with ABCC9. KCNJ11 forms the channel pore while ABCC9 is required for activation and regulation (By similarity). {ECO:0000250}. PTM: Phosphorylation by MAPK1 results in changes in channel gating that destabilize the closed states and reduce the ATP sensitivity. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SUBUNIT: Interacts with ABCC9/SUR2 (By similarity). Interacts with ABCC8/SUR. {ECO:0000250}. +P52187 KCJ12_MOUSE ATP-sensitive inward rectifier potassium channel 12 (Inward rectifier K(+) channel Kir2.2) (IRK-2) (Potassium channel, inwardly rectifying subfamily J member 12) 427 48,427 Chain (1); Disulfide bond (1); Intramembrane (3); Modified residue (1); Motif (4); Sequence conflict (6); Site (1); Topological domain (4); Transmembrane (2) INTRAMEM 124 128 {ECO:0000250}.; INTRAMEM 129 141 Helical; Pore-forming; Name=H5. {ECO:0000250}.; INTRAMEM 142 151 Pore-forming. {ECO:0000250}. TRANSMEM 83 107 Helical; Name=M1. {ECO:0000250}.; TRANSMEM 157 181 Helical; Name=M2. {ECO:0000250}. TOPO_DOM 1 82 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 108 123 Extracellular. {ECO:0000250}.; TOPO_DOM 152 156 Extracellular. {ECO:0000250}.; TOPO_DOM 182 427 Cytoplasmic. {ECO:0000250}. FUNCTION: Inward rectifying potassium channel that is activated by phosphatidylinositol 4,5-bisphosphate and that probably participates in controlling the resting membrane potential in electrically excitable cells. Probably participates in establishing action potential waveform and excitability of neuronal and muscle tissues. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. {ECO:0000269|PubMed:8083233}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:8083233}; Multi-pass membrane protein {ECO:0000269|PubMed:8083233}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Homotetramer. Forms heteromer with KCNJ4. Association, via its PDZ-recognition domain, with LIN7A, LIN7B, LIN7C, DLG1, CASK and APBA1 plays a key role in its localization and trafficking (By similarity). {ECO:0000250}. DOMAIN: Phosphatidylinositol 4,5-bisphosphate binding to the cytoplasmic side of the channel triggers a conformation change leading to channel opening. {ECO:0000250}. TISSUE SPECIFICITY: Highest level in cerebellum. {ECO:0000269|PubMed:8083233}. +P86046 KCJ13_MOUSE Inward rectifier potassium channel 13 (Inward rectifier K(+) channel Kir7.1) (Potassium channel, inwardly rectifying subfamily J member 13) 360 40,565 Chain (1); Intramembrane (2); Modified residue (1); Motif (1); Site (1); Topological domain (4); Transmembrane (2) INTRAMEM 106 117 Helical; Pore-forming; Name=H5. {ECO:0000250}.; INTRAMEM 118 124 Pore-forming. {ECO:0000250}. TRANSMEM 54 78 Helical; Name=M1. {ECO:0000250}.; TRANSMEM 134 155 Helical; Name=M2. {ECO:0000250}. TOPO_DOM 1 53 Cytoplasmic. {ECO:0000250|UniProtKB:O60928}.; TOPO_DOM 79 105 Extracellular. {ECO:0000250|UniProtKB:O60928}.; TOPO_DOM 125 133 Extracellular. {ECO:0000250|UniProtKB:O60928}.; TOPO_DOM 156 360 Cytoplasmic. {ECO:0000250|UniProtKB:O60928}. FUNCTION: Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. KCNJ13 has a very low single channel conductance, low sensitivity to block by external barium and cesium, and no dependence of its inward rectification properties on the internal blocking particle magnesium (By similarity). {ECO:0000250}. PTM: Phosphorylation at Ser-287 by PKA increases ionic currents. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q8JZN3 KCJ14_MOUSE ATP-sensitive inward rectifier potassium channel 14 (Inward rectifier K(+) channel Kir2.4) (IRK-4) (Potassium channel, inwardly rectifying subfamily J member 14) 434 47,607 Chain (1); Intramembrane (2); Modified residue (1); Motif (1); Sequence conflict (2); Topological domain (4); Transmembrane (2) INTRAMEM 132 143 Helical; Pore-forming; Name=H5. {ECO:0000250}.; INTRAMEM 144 150 Pore-forming. {ECO:0000250}. TRANSMEM 85 109 Helical; Name=M1. {ECO:0000250}.; TRANSMEM 160 181 Helical; Name=M2. {ECO:0000250}. TOPO_DOM 1 84 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 110 131 Extracellular. {ECO:0000250}.; TOPO_DOM 151 159 Extracellular. {ECO:0000250}.; TOPO_DOM 182 434 Cytoplasmic. {ECO:0000250}. FUNCTION: Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. KCNJ14 gives rise to low-conductance channels with a low affinity to the channel blockers Barium and Cesium (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. +O88932 KCJ15_MOUSE ATP-sensitive inward rectifier potassium channel 15 (Inward rectifier K(+) channel Kir4.2) (Potassium channel, inwardly rectifying subfamily J member 15) 375 42,605 Chain (1); Intramembrane (2); Motif (1); Sequence conflict (3); Site (1); Topological domain (4); Transmembrane (2) INTRAMEM 114 125 Helical; Pore-forming; Name=H5. {ECO:0000250}.; INTRAMEM 126 132 Pore-forming. {ECO:0000250}. TRANSMEM 64 88 Helical; Name=M1. {ECO:0000250}.; TRANSMEM 142 163 Helical; Name=M2. {ECO:0000250}. TOPO_DOM 1 63 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 89 113 Extracellular. {ECO:0000250}.; TOPO_DOM 133 141 Extracellular. {ECO:0000250}.; TOPO_DOM 164 375 Cytoplasmic. {ECO:0000250}. FUNCTION: Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SUBUNIT: Interacts with PATJ. {ECO:0000250}. +Q9Z307 KCJ16_MOUSE Inward rectifier potassium channel 16 (Inward rectifier K(+) channel Kir5.1) (Potassium channel, inwardly rectifying subfamily J member 16) 419 48,023 Chain (1); Intramembrane (2); Modified residue (3); Motif (1); Sequence conflict (2); Site (1); Topological domain (4); Transmembrane (2) INTRAMEM 118 129 Helical; Pore-forming; Name=H5. {ECO:0000250}.; INTRAMEM 130 136 Pore-forming. {ECO:0000250}. TRANSMEM 71 95 Helical; Name=M1. {ECO:0000250}.; TRANSMEM 146 167 Helical; Name=M2. {ECO:0000250}. TOPO_DOM 1 70 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 96 117 Extracellular. {ECO:0000250}.; TOPO_DOM 137 145 Extracellular. {ECO:0000250}.; TOPO_DOM 168 419 Cytoplasmic. {ECO:0000250}. FUNCTION: Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. KCNJ16 may be involved in the regulation of fluid and pH balance. In the kidney, together with KCNJ10, mediates basolateral K(+) recycling in distal tubules; this process is critical for Na(+) reabsorption at the tubules. {ECO:0000250|UniProtKB:Q9NPI9}. SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9NPI9}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9NPI9}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q9NPI9}. Note=In kidney distal convoluted tubules, located in the basolateral membrane in the presence of KCNJ10. {ECO:0000250|UniProtKB:Q9NPI9}. SUBUNIT: Heterodimer with Kir4.1/KCNJ10; this interaction is required for KCNJ16 localization to the basolateral membrane in kidney cells. As a heterodimer with KCNJ10, may interact with MAGI1; this interaction may facilitate KCNJ10/KCNJ16 potassium channel expression at the basolateral membrane in kidney cells. May form heterodimers with Kir2.1/KCNJ2. {ECO:0000250|UniProtKB:Q9NPI9}. +Q8CAE3 KCMB1_MOUSE Calcium-activated potassium channel subunit beta-1 (BK channel subunit beta-1) (BKbeta) (BKbeta1) (Calcium-activated potassium channel, subfamily M subunit beta-1) (Calcium-activated potassium channel subunit beta) (Charybdotoxin receptor subunit beta-1) (K(VCA)beta-1) (Maxi K channel subunit beta-1) (Slo-beta-1) (Slo-beta) 191 21,846 Chain (1); Glycosylation (2); Sequence conflict (3); Topological domain (3); Transmembrane (2) TRANSMEM 19 39 Helical; Name=1. {ECO:0000255}.; TRANSMEM 156 176 Helical; Name=2. {ECO:0000255}. TOPO_DOM 1 18 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 40 155 Extracellular. {ECO:0000255}.; TOPO_DOM 177 191 Cytoplasmic. {ECO:0000255}. FUNCTION: Regulatory subunit of the calcium activated potassium KCNMA1 (maxiK) channel. Modulates the calcium sensitivity and gating kinetics of KCNMA1, thereby contributing to KCNMA1 channel diversity. Increases the apparent Ca(2+)/voltage sensitivity of the KCNMA1 channel. It also modifies KCNMA1 channel kinetics and alters its pharmacological properties. It slows down the activation and the deactivation kinetics of the channel. Acts as a negative regulator of smooth muscle contraction by enhancing the calcium sensitivity to KCNMA1. Its presence is also a requirement for internal binding of the KCNMA1 channel opener dehydrosoyasaponin I (DHS-1) triterpene glycoside and for external binding of the agonist hormone 17-beta-estradiol (E2). Increases the binding activity of charybdotoxin (CTX) toxin to KCNMA1 peptide blocker by increasing the CTX association rate and decreasing the dissociation rate. {ECO:0000269|PubMed:11057658}. PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SUBUNIT: Interacts with KCNMA1 tetramer. There are probably 4 molecules of KCMNB1 per KCNMA1 tetramer (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in many tissues containing smooth muscles. In brain and heart, it is not expressed except in the vasculature, such as cerebral arteries, aorta and corona arteries. {ECO:0000269|PubMed:11057658}. +P20060 HEXB_MOUSE Beta-hexosaminidase subunit beta (EC 3.2.1.52) (Beta-N-acetylhexosaminidase subunit beta) (Hexosaminidase subunit B) (N-acetyl-beta-glucosaminidase subunit beta) 536 61,116 Active site (1); Chain (1); Disulfide bond (3); Glycosylation (3); Signal peptide (1) FUNCTION: Responsible for the degradation of GM2 gangliosides, and a variety of other molecules containing terminal N-acetyl hexosamines, in the brain and other tissues. SUBCELLULAR LOCATION: Lysosome. +Q3U4H6 HEXD_MOUSE Hexosaminidase D (EC 3.2.1.52) (Beta-N-acetylhexosaminidase) (Beta-hexosaminidase D) (Hexosaminidase domain-containing protein) (N-acetyl-beta-galactosaminidase) 486 54,576 Active site (1); Alternative sequence (1); Chain (1); Erroneous initiation (1) FUNCTION: Has hexosaminidase activity (PubMed:19040401). Responsible for the cleavage of the monosaccharides N-acetylglucosamine (GlcNAc) and N-acetylgalactosamine (GalNAc) from cellular substrates. Has a preference for galactosaminide over glucosaminide substrates (By similarity). {ECO:0000250|UniProtKB:Q8WVB3, ECO:0000269|PubMed:19040401}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19040401}. Nucleus {ECO:0000269|PubMed:19040401}. Extracellular vesicle {ECO:0000250|UniProtKB:Q8WVB3}. SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:19040401}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:19040401}. +Q99LI8 HGS_MOUSE Hepatocyte growth factor-regulated tyrosine kinase substrate 775 86,015 Chain (1); Compositional bias (2); Domain (2); Modified residue (6); Mutagenesis (7); Region (4); Sequence conflict (2); Zinc finger (1) FUNCTION: Involved in intracellular signal transduction mediated by cytokines and growth factors. When associated with STAM, it suppresses DNA signaling upon stimulation by IL-2 and GM-CSF. Could be a direct effector of PI3-kinase in vesicular pathway via early endosomes and may regulate trafficking to early and late endosomes by recruiting clathrin. May concentrate ubiquitinated receptors within clathrin-coated regions. Involved in down-regulation of receptor tyrosine kinase via multivesicular body (MVBs) when complexed with STAM (ESCRT-0 complex). The ESCRT-0 complex binds ubiquitin and acts as sorting machinery that recognizes ubiquitinated receptors and transfers them to further sequential lysosomal sorting/trafficking processes. May contribute to the efficient recruitment of SMADs to the activin receptor complex. Involved in receptor recycling via its association with the CART complex, a multiprotein complex required for efficient transferrin receptor recycling but not for EGFR degradation. {ECO:0000269|PubMed:11094085}. PTM: Phosphorylated on Tyr-334. This phosphorylation occurs in response to EGF. A minor site of phosphorylation on Tyr-329 is detected. Protein phosphorylation may also be triggered in response to IL-2, GM-CSF and HGF. {ECO:0000269|PubMed:12953068}.; PTM: Ubiquitinated by ITCH. {ECO:0000250|UniProtKB:O14964}. SUBCELLULAR LOCATION: Cytoplasm. Early endosome membrane; Peripheral membrane protein; Cytoplasmic side. Endosome, multivesicular body membrane; Peripheral membrane protein. Note=Colocalizes with UBQLN1 in ubiquitin-rich cytoplasmic aggregates that are not endocytic compartments. {ECO:0000250|UniProtKB:O14964}. SUBUNIT: Component of the ESCRT-0 complex composed of STAM or STAM2 and HGS. Part of a complex at least composed of HSG, STAM2 (or probably STAM) and EPS15 (By similarity). Interacts with STAM (PubMed:9407053, PubMed:19278655). Interacts with STAM2 (PubMed:10651905). Interacts with EPS15; the interaction is direct, calcium-dependent and inhibited by SNAP25 (By similarity). Identified in a complex with STAM and LITAF (By similarity). Found in a complex with STAM and E3 ligase ITCH and DTX3L (By similarity). Interacts with E3 ligase DTX3L; the interaction brings together STAM and HSG, promotes their recruitment to early endosomes and decreases STAM and HGS ubiquitination by ITCH (By similarity). Interacts with NF2; the interaction is direct (By similarity). Interacts with ubiquitin; the interaction is direct (PubMed:11988743). Interacts with VPS37C (By similarity). Interacts with SMAD1, SMAD2 and SMAD3 (PubMed:11094085). Interacts with TSG101; the interaction mediates the association with the ESCRT-I complex (PubMed:12802020). Interacts with SNAP25; the interaction is direct and decreases with addition of increasing concentrations of free calcium (By similarity). Interacts with SNX1; the interaction is direct (By similarity). Component of a 550 kDa membrane complex at least composed of HGS and SNX1 but excluding EGFR (By similarity). Interacts with TRAK1 (By similarity). Interacts with TRAK2 (By similarity). Component of the CART complex, at least composed of ACTN4, HGS/HRS, MYO5B and TRIM3 (By similarity). Interacts with ARRDC3 (By similarity). Identified in a complex containing at least ARRDC4, AVPR2 and HGS (By similarity). Interacts (via UIM domain) with UBQLN1 (via ubiquitin-like domain) (PubMed:16159959). Interacts with LAPTM4B; promotes HGS ubiquitination (By similarity). {ECO:0000250|UniProtKB:O14964, ECO:0000250|UniProtKB:Q9JJ50, ECO:0000269|PubMed:10651905, ECO:0000269|PubMed:11094085, ECO:0000269|PubMed:11988743, ECO:0000269|PubMed:12802020, ECO:0000269|PubMed:16159959, ECO:0000269|PubMed:19278655, ECO:0000269|PubMed:9407053}. DOMAIN: Has a double-sided UIM that can bind 2 ubiquitin molecules, one on each side of the helix. {ECO:0000250}.; DOMAIN: The FYVE-type zinc finger domain mediates interactions with phosphatidylinositol 3-phosphate in membranes of early endosomes and penetrates bilayers. The FYVE domain insertion into PtdIns(3)P-enriched membranes is substantially increased in acidic conditions (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous expression in adult and fetal tissues with higher expression in testis. {ECO:0000269|PubMed:7565774, ECO:0000269|PubMed:9630564}. +Q8K1K9 HINFP_MOUSE Histone H4 transcription factor (Histone nuclear factor P) (HiNF-P) (MBD2-interacting zinc finger protein) (Methyl-CpG-binding protein 2-interacting zinc finger protein) 503 58,076 Chain (1); Compositional bias (1); Region (2); Sequence conflict (2); Zinc finger (9) FUNCTION: Transcriptional repressor that binds to the consensus sequence 5'-CGGACGTT-3' and to the RB1 promoter. Transcriptional activator that promotes histone H4 gene transcription at the G1/S phase transition in conjunction with NPAT. Also activates transcription of the ATM and PRKDC genes. Autoregulates its expression by associating with its own promoter. {ECO:0000269|PubMed:17826007}. PTM: Ubiquitinated. Ubiquitination may lead to proteasome-mediated degradation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Associated with discrete nuclear foci. {ECO:0000250}. SUBUNIT: Binds MBD2 and a histone deacetylase complex. Interacts with NPAT (By similarity). {ECO:0000250}. +Q9D2G9 HIPL2_MOUSE HHIP-like protein 2 717 79,998 Alternative sequence (1); Chain (1); Disulfide bond (4); Glycosylation (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +O54891 LEG6_MOUSE Galectin-6 (Gal-6) 301 34,112 Chain (1); Domain (2); Sequence conflict (1) DOMAIN: Contains two homologous but distinct carbohydrate-binding domains. +Q9JL15 LEG8_MOUSE Galectin-8 (Gal-8) (LGALS-8) 316 36,162 Binding site (3); Chain (1); Domain (2); Region (1); Site (1) FUNCTION: Beta-galactoside-binding lectin that acts as a sensor of membrane damage caused by infection and restricts the proliferation of infecting pathogens by targeting them for autophagy. Detects membrane rupture by binding beta-galactoside ligands located on the lumenal side of the endosome membrane; these ligands becoming exposed to the cytoplasm following rupture. Restricts infection by initiating autophagy via interaction with CALCOCO2/NDP52. Required to restrict infection of bacterial invasion such as S.typhimurium. Also required to restrict infection of Picornaviridae viruses. Has a marked preference for 3'-O-sialylated and 3'-O-sulfated glycans. {ECO:0000250|UniProtKB:O00214}. SUBCELLULAR LOCATION: Cytoplasmic vesicle {ECO:0000250|UniProtKB:O00214}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:O00214}. SUBUNIT: Homodimer. Interacts with CALCOCO2/NDP52. Interacts with PDPN; the interaction is glycosylation-dependent; may participate to connection of the lymphatic endothelium to the surrounding extracellular matrix. {ECO:0000250|UniProtKB:O00214}. DOMAIN: Contains two homologous but distinct carbohydrate-binding domains. +O08573 LEG9_MOUSE Galectin-9 (Gal-9) 353 40,036 Alternative sequence (2); Beta strand (11); Binding site (7); Chain (1); Domain (2); Helix (1); Region (2); Sequence conflict (1) FUNCTION: Binds galactosides (By similarity). Has high affinity for the Forssman pentasaccharide (By similarity). Ligand for HAVCR2/TIM3 (By similarity). Binding to HAVCR2 induces T-helper type 1 lymphocyte (Th1) death (By similarity). Also stimulates bactericidal activity in infected macrophages by causing macrophage activation and IL1B secretion which restricts intracellular bacterial growth (PubMed:20937702). Ligand for P4HB; the interaction retains P4HB at the cell surface of Th2 T-helper cells, increasing disulfide reductase activity at the plasma membrane, altering the plasma membrane redox state and enhancing cell migration (PubMed:21670307). Ligand for CD44; the interaction enhances binding of SMAD3 to the FOXP3 promoter, leading to up-regulation of FOXP3 expression and increased induced regulatory T (iTreg) cell stability and suppressive function (PubMed:25065622). Promotes ability of mesenchymal stromal cells to suppress T-cell proliferation (By similarity). Expands regulatory T-cells and induces cytotoxic T-cell apoptosis following virus infection (By similarity). Activates ERK1/2 phosphorylation inducing cytokine (IL-6, IL-8, IL-12) and chemokine (CCL2) production in mast and dendritic cells (By similarity). Inhibits degranulation and induces apoptosis of mast cells (By similarity). Induces maturation and migration of dendritic cells (By similarity). Inhibits natural killer (NK) cell function (PubMed:23408620). Can transform NK cell phenotype from peripheral to decidual during pregnancy (By similarity). Astrocyte derived galectin-9 enhances microglial TNF production (PubMed:25158758). May play a role in thymocyte-epithelial interactions relevant to the biology of the thymus. May provide the molecular basis for urate flux across cell membranes, allowing urate that is formed during purine metabolism to efflux from cells and serving as an electrogenic transporter that plays an important role in renal and gastrointestinal urate excretion (By similarity). Highly selective to the anion urate (By similarity). {ECO:0000250|UniProtKB:O00182, ECO:0000250|UniProtKB:P97840, ECO:0000269|PubMed:20937702, ECO:0000269|PubMed:21670307, ECO:0000269|PubMed:23408620, ECO:0000269|PubMed:25065622, ECO:0000269|PubMed:25158758}.; FUNCTION: Isoform 2: Acts as an eosinophil chemoattractant (By similarity). It also inhibits angiogenesis (By similarity). Suppresses IFNG production by natural killer cells. {ECO:0000250|UniProtKB:O00182, ECO:0000269|PubMed:23242525}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23242525}. Nucleus {ECO:0000269|PubMed:23242525}. Secreted {ECO:0000250|UniProtKB:O00182}. Note=May also be secreted by a non-classical secretory pathway (PubMed:9038233). Secreted by mesenchymal stromal cells upon IFNG stimulation (By similarity). {ECO:0000250|UniProtKB:O00182, ECO:0000269|PubMed:9038233}. SUBUNIT: Homodimer. {ECO:0000305|PubMed:16990264}. DOMAIN: Contains two homologous but distinct carbohydrate-binding domains. TISSUE SPECIFICITY: Accentuated expression in liver and thymus of embryo, detected in embryonic heart, brain, lung, liver, and kidney. Highly expressed in adult thymus, small intestine, and liver, and to a lesser extent in lung, kidney, spleen, cardiac, and skeletal muscle. Barely detectable in brain and reticulocyte. Expressed in placenta, uterus and decidua during pregnancy (PubMed:23242525). Expressed in CD4+ T-cells with higher levels in iTreg cells than other T-cell types and sustained high levels throughout iTreg cell differentiation (at protein level) (PubMed:25065622). Expressed in myeloid cells in lung (PubMed:20937702). Constitutively expressed in microglia (PubMed:25158758). Isoform 1 is expressed exclusively in the small intestine. Isoform 2 expression in decidua increases in pathological pregnancy from gestation day 7.5 to 13.5 and it is higher than in normal pregnancy (PubMed:23242525). Isoform 3 expression in decidua is higher in normal pregnancy than in pathological pregnancy (PubMed:23242525). {ECO:0000269|PubMed:20937702, ECO:0000269|PubMed:23242525, ECO:0000269|PubMed:25065622, ECO:0000269|PubMed:25158758}. +Q8VED9 LEGL_MOUSE Galectin-related protein (Galectin-related protein A) (Lectin galactoside-binding-like protein A) 172 18,956 Chain (1); Domain (1); Initiator methionine (1); Modified residue (3) FUNCTION: Does not bind lactose, and may not bind carbohydrates. {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. +A2AJ76 HMCN2_MOUSE Hemicentin-2 5100 547,198 Alternative sequence (1); Chain (1); Disulfide bond (57); Domain (50); Frameshift (1); Glycosylation (40); Modified residue (3); Sequence conflict (2); Signal peptide (1) PTM: Reported to be phosphorylated; however as this position is extracellular, the in vivo relevance is unsure. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:17015624}. Cleavage furrow {ECO:0000269|PubMed:21215633}. Note=The antibody used in PubMed:17015624 and PubMed:21215633 to determine subcellular location does not distinguish between HMCN1 and HMCN2. {ECO:0000269|PubMed:17015624, ECO:0000269|PubMed:21215633}. TISSUE SPECIFICITY: Expressed in the pericellular extracellular matrix of epithelial cells in a number of tissues including embryonic trophectoderm and adult skin and tongue. Also present in the extracellular matrix of some, but not all, blood vessels. {ECO:0000269|PubMed:17015624}. +P63141 KCNA2_MOUSE Potassium voltage-gated channel subfamily A member 2 (MK2) (Voltage-gated potassium channel subunit Kv1.2) 499 56,701 Chain (1); Glycosylation (1); Intramembrane (2); Lipidation (1); Modified residue (7); Motif (2); Mutagenesis (1); Region (2); Sequence conflict (1); Site (2); Topological domain (8); Transmembrane (6) INTRAMEM 362 373 Helical; Name=Pore helix. {ECO:0000250|UniProtKB:P63142}.; INTRAMEM 374 381 {ECO:0000250|UniProtKB:P63142}. TRANSMEM 161 182 Helical; Name=Segment S1. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 222 243 Helical; Name=Segment S2. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 255 275 Helical; Name=Segment S3. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 290 310 Helical; Voltage-sensor; Name=Segment S4. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 326 347 Helical; Name=Segment S5. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 389 417 Helical; Name=Segment S6. {ECO:0000250|UniProtKB:P63142}. TOPO_DOM 1 160 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 183 221 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 244 254 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 276 289 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 311 325 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 348 361 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 382 388 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 418 499 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}. FUNCTION: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain and the central nervous system, but also in the cardiovascular system. Prevents aberrant action potential firing and regulates neuronal output. Forms tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane (PubMed:12527813, PubMed:21233214). Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNA1, KCNA2, KCNA4, KCNA5, KCNA6, KCNA7, and possibly other family members as well; channel properties depend on the type of alpha subunits that are part of the channel (PubMed:20696761). Channel properties are modulated by cytoplasmic beta subunits that regulate the subcellular location of the alpha subunits and promote rapid inactivation of delayed rectifier potassium channels (By similarity). In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes, making it difficult to assign currents observed in intact tissues to any particular potassium channel family member. Homotetrameric KCNA2 forms a delayed-rectifier potassium channel that opens in response to membrane depolarization, followed by slow spontaneous channel closure (PubMed:23864368). In contrast, a heteromultimer formed by KCNA2 and KCNA4 shows rapid inactivation (PubMed:23864368). Contributes to the regulation of action potentials in neurons (PubMed:12527813, PubMed:17925011). KCNA2-containing channels play a presynaptic role and prevent hyperexcitability and aberrant action potential firing (PubMed:17634333, PubMed:17925011). Response to toxins that are selective for KCNA1, respectively for KCNA2, suggests that heteromeric potassium channels composed of both KCNA1 and KCNA2 play a role in pacemaking and regulate the output of deep cerebellar nuclear neurons (By similarity). Response to toxins that are selective for KCNA2-containing potassium channels suggests that in Purkinje cells, dendritic subthreshold KCNA2-containing potassium channels prevent random spontaneous calcium spikes, suppressing dendritic hyperexcitability without hindering the generation of somatic action potentials, and thereby play an important role in motor coordination (By similarity). KCNA2-containing channels play a role in GABAergic transmission from basket cells to Purkinje cells in the cerebellum, and thereby play an import role in motor coordination (PubMed:20696761). Plays a role in the induction of long-term potentiation of neuron excitability in the CA3 layer of the hippocampus (PubMed:23981714). May function as down-stream effector for G protein-coupled receptors and inhibit GABAergic inputs to basolateral amygdala neurons (By similarity). May contribute to the regulation of neurotransmitter release, such as gamma-aminobutyric acid (GABA) (By similarity). Contributes to the regulation of the axonal release of the neurotransmitter dopamine (PubMed:21233214). Reduced KCNA2 expression plays a role in the perception of neuropathic pain after peripheral nerve injury, but not acute pain (By similarity). Plays a role in the regulation of the time spent in non-rapid eye movement (NREM) sleep (PubMed:17925011). {ECO:0000250, ECO:0000269|PubMed:12527813, ECO:0000269|PubMed:17634333, ECO:0000269|PubMed:17925011, ECO:0000269|PubMed:20696761, ECO:0000269|PubMed:21233214, ECO:0000269|PubMed:23864368, ECO:0000269|PubMed:23981714, ECO:0000305}. PTM: Phosphorylated on tyrosine residues; phosphorylation increases in response to ischemia (By similarity). Phosphorylated on tyrosine residues by activated PTK2B/PYK2 (By similarity). Phosphorylation on tyrosine residues suppresses ion channel activity (By similarity). Phosphorylated on tyrosine residues in response to CHRM1 activation; this abolishes interaction with CTTN. This is probably due to endocytosis of the phosphorylated channel subunits (By similarity). Phosphorylated on serine residues in response to increased cAMP levels; phosphorylation is apparently not catalyzed by PKA (By similarity). {ECO:0000250|UniProtKB:P63142}.; PTM: N-glycosylated, with complex, sialylated N-glycans. {ECO:0000250|UniProtKB:P63142}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12527813, ECO:0000269|PubMed:18509034, ECO:0000269|PubMed:20696761, ECO:0000269|PubMed:23332758, ECO:0000269|PubMed:23864368}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P63142}. Membrane {ECO:0000269|PubMed:23332758, ECO:0000269|PubMed:8361541, ECO:0000269|PubMed:9852577}. Cell projection, axon {ECO:0000269|PubMed:18509034, ECO:0000269|PubMed:21233214, ECO:0000269|PubMed:8046438, ECO:0000269|PubMed:8361541}. Cell junction, synapse {ECO:0000250|UniProtKB:P63142}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P63142}. Cell projection, lamellipodium membrane {ECO:0000250|UniProtKB:P63142}. Cell junction, synapse, synaptosome {ECO:0000269|PubMed:21233214}. Cell junction, synapse, presynaptic cell membrane {ECO:0000269|PubMed:21233214}. Cell projection, dendrite {ECO:0000269|PubMed:8046438}. Perikaryon {ECO:0000269|PubMed:8046438}. Cell junction, paranodal septate junction {ECO:0000269|PubMed:25378149}. Note=KCNA2 by itself is detected both at the endoplasmic reticulum and at the cell membrane. Coexpression with KCNA4 or with beta subunits promotes expression at the cell membrane. Coexpression with KCNA1 inhibits cell surface expression (By similarity). Cocaine-induced interaction with SIGMAR1 increases expression at the cell surface (PubMed:23332758). In myelinated peripheral axons, clustered in the juxtaparadonal region and at an internodal line located along the mesaxon and below the Schmidt-Lanterman incisures (PubMed:25378149). {ECO:0000250|UniProtKB:P63142, ECO:0000269|PubMed:23332758, ECO:0000269|PubMed:25378149}. SUBUNIT: Homotetramer and heterotetramer with other channel-forming alpha subunits, such as KCNA1, KCNA4, KCNA5, KCNA6 and KCNA7 (PubMed:8361541, PubMed:9852577, PubMed:23864368). Channel activity is regulated by interaction with beta subunits, including KCNAB1 and KCNAB2 (By similarity). Identified in a complex with KCNA1 and KCNAB2 (By similarity). Identified in a complex with KCNA5 and KCNAB1 (By similarity). Identified in a complex with KCNA4 and FYN (By similarity). Interacts with PTK2B (By similarity). Interacts (via C-terminus) with CTTN (By similarity). Interacts with ADAM22 (By similarity). Interacts with CNTNAP2 (By similarity). Interacts (via C-terminus) with the PDZ domains of DLG1, DLG2 and DLG4 (By similarity). Interacts (via N-terminal cytoplasmic domain) with RHOA (GTP-bound form); this regulates channel activity by reducing location at the cell surface in response to CHRM1 activation (PubMed:9635436). Interacts with DRD2 (PubMed:21233214). Interacts with SIGMAR1; cocaine consumption leads to increased interaction (PubMed:23332758). {ECO:0000250|UniProtKB:P16389, ECO:0000250|UniProtKB:P63142, ECO:0000250|UniProtKB:Q09081, ECO:0000269|PubMed:17634333, ECO:0000269|PubMed:21233214, ECO:0000269|PubMed:23332758, ECO:0000269|PubMed:8361541, ECO:0000269|PubMed:9635436, ECO:0000269|PubMed:9852577, ECO:0000305, ECO:0000305|PubMed:23864368}. DOMAIN: The cytoplasmic N-terminus is important for tetramerization. Interactions between the different subunits modulate the gating characteristics (By similarity). Besides, the cytoplasmic N-terminal domain mediates interaction with RHOA and thus is required for RHOA-mediated endocytosis (By similarity). {ECO:0000250|UniProtKB:P63142}.; DOMAIN: The transmembrane segment S4 functions as voltage-sensor and is characterized by a series of positively charged amino acids at every third position. Channel opening and closing is effected by a conformation change that affects the position and orientation of the voltage-sensor paddle formed by S3 and S4 within the membrane. A transmembrane electric field that is positive inside would push the positively charged S4 segment outwards, thereby opening the pore, while a field that is negative inside would pull the S4 segment inwards and close the pore. Changes in the position and orientation of S4 are then transmitted to the activation gate formed by the inner helix bundle via the S4-S5 linker region. {ECO:0000250|UniProtKB:P63142}. TISSUE SPECIFICITY: Detected in brain (PubMed:17634333). Detected in cerebellum (PubMed:20696761). Detected in mitral cells in the olfactory bulb (PubMed:8046438). Detected in cochlea (PubMed:23864368). Detected in cerebellum, particularly in the basket cell axon plexus and in the terminal regions around Purkinje cells (PubMed:8361541, PubMed:8046438, PubMed:18760366). Detected in juxtaparanodal regions in sciatic nerve (PubMed:22649228). Detected in Schwann cells from sciatic nerve (PubMed:9852577). Detected in dopamine neurons in substantia nigra (PubMed:21233214). Detected in large myelinated fibers in juxtaparanodes in the CA3 and CA1 areas of the hippocampus (PubMed:8046438, PubMed:18760366). Detected in brain, in punctae on fiber tracts in brain stem and spinal cord, and on axons in the juxtaparanodal regions of the node of Ranvier (at protein level) (PubMed:8361541). Detected in dopamine neurons in the midbrain (PubMed:21233214). {ECO:0000269|PubMed:17634333, ECO:0000269|PubMed:18760366, ECO:0000269|PubMed:20696761, ECO:0000269|PubMed:22649228, ECO:0000269|PubMed:23864368, ECO:0000269|PubMed:8046438, ECO:0000269|PubMed:8361541, ECO:0000269|PubMed:9852577}. +O09173 HGD_MOUSE Homogentisate 1,2-dioxygenase (EC 1.13.11.5) (Homogentisate oxygenase) (Homogentisic acid oxidase) (Homogentisicase) 445 49,960 Chain (1); Metal binding (3); Modified residue (2); Sequence conflict (1) Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 4/6. SUBUNIT: Homohexamer arranged as a dimer of trimers. {ECO:0000250}. DISEASE: Note=Defects in Hgd are the cause of alkaptonuria (aku). Aku is an autosomal recessive error of metabolism which is characterized by an increase in the level of homogentisic acid. +P26928 HGFL_MOUSE Hepatocyte growth factor-like protein (Macrophage stimulatory protein) (MSP) [Cleaved into: Hepatocyte growth factor-like protein alpha chain; Hepatocyte growth factor-like protein beta chain] 716 80,619 Chain (3); Disulfide bond (20); Domain (6); Glycosylation (4); Sequence conflict (1); Signal peptide (1) PTM: Cleaved after Arg-488, probably by HPN/Hepsin, to yield the active form consisting of two disulfide-linked chains. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. SUBUNIT: Dimer of an alpha chain and a beta chain linked by a disulfide bond. Interacts (via beta chain) with MST1R (via SEMA domain). {ECO:0000250}. TISSUE SPECIFICITY: Liver. Lower levels in lung, placenta and adrenal. +Q8BLR9 HIF1N_MOUSE Hypoxia-inducible factor 1-alpha inhibitor (EC 1.14.11.30) (EC 1.14.11.n4) (Hypoxia-inducible factor asparagine hydroxylase) 349 40,241 Alternative sequence (2); Binding site (8); Chain (1); Domain (1); Initiator methionine (1); Metal binding (3); Modified residue (1); Region (4); Sequence conflict (1); Site (1) FUNCTION: Hydroxylates HIF-1 alpha at 'Asn-799' in the C-terminal transactivation domain (CAD). Functions as an oxygen sensor and, under normoxic conditions, the hydroxylation prevents interaction of HIF-1 with transcriptional coactivators including Cbp/p300-interacting transactivator. Involved in transcriptional repression through interaction with HIF1A, VHL and histone deacetylases. Hydroxylates specific Asn residues within ankyrin repeat domains (ARD) of NFKB1, NFKBIA, NOTCH1, ASB4, PPP1R12A and several other ARD-containing proteins. Also hydroxylates Asp and His residues within ARDs of ANK1 and TNKS2, respectively. Negatively regulates NOTCH1 activity, accelerating myogenic differentiation (By similarity). Positively regulates ASB4 activity, promoting vascular differentiation. {ECO:0000250|UniProtKB:Q9NWT6, ECO:0000269|PubMed:17636018}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NWT6}. Cytoplasm {ECO:0000250|UniProtKB:Q9NWT6}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9NWT6}. SUBUNIT: Homodimer; homodimerization is essential for catalytic activity. Interacts with VHL and HIF1A. Part of a complex with VHL, HIF1A and HDAC1 or HDAC2 or HDAC3. Interacts with NFKB1 and NFKBIA. Interacts with NOTCH1, NOTCH2 and NOTCH3 but not with NOTCH4. Interacts with ABPA3. Interacts with TNKS2. Interacts with PPP1R12A (By similarity). Interacts with UBE3A (By similarity). Interacts with ASB4. Interacts with ANKS3 (PubMed:25671767). Interacts with NECAB3; the interaction is indirect and seems to be mediated by APBA3 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9NWT6, ECO:0000269|PubMed:17636018, ECO:0000269|PubMed:25671767}. +O88904 HIPK1_MOUSE Homeodomain-interacting protein kinase 1 (EC 2.7.11.1) (Nuclear body-associated kinase 2) (Protein kinase Myak) 1210 130,723 Active site (1); Alternative sequence (3); Binding site (1); Chain (1); Cross-link (6); Domain (1); Modified residue (2); Motif (1); Mutagenesis (1); Nucleotide binding (1); Region (3); Sequence conflict (6) FUNCTION: Serine/threonine-protein kinase involved in transcription regulation and TNF-mediated cellular apoptosis. Plays a role as a corepressor for homeodomain transcription factors. Phosphorylates DAXX and MYB. Phosphorylates DAXX in response to stress, and mediates its translocation from the nucleus to the cytoplasm. Inactivates MYB transcription factor activity by phosphorylation. Prevents MAP3K5-JNK activation in the absence of TNF. TNF triggers its translocation to the cytoplasm in response to stress stimuli, thus activating nuclear MAP3K5-JNK by derepression and promoting apoptosis. May be involved in anti-oxidative stress responses. Involved in the regulation of eye size, lens formation and retinal lamination during late embryogenesis. Promotes angiogenesis and to be involved in erythroid differentiation. May be involved in malignant squamous cell tumor formation. {ECO:0000269|PubMed:12702766, ECO:0000269|PubMed:16917507, ECO:0000269|PubMed:20231426, ECO:0000269|PubMed:20579985}. PTM: Phosphorylated and activated by JNK1 (By similarity). Autophosphorylated. {ECO:0000250}.; PTM: Sumoylated. When conjugated it is directed to nuclear speckles. SENP1-mediated desumoylation is mediated by TNF in response to stress stimuli, triggering transient translocation from nucleus to cytoplasm. {ECO:0000269|PubMed:18219322}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Predominantly nuclear. Translocates from nucleus to cytoplasm in response to stress stimuli via SENP1-mediated desumoylation. SUBUNIT: Interacts with Nkx1-2, Nkx2-5, MYB, PARK7, DAXX and p53/TP53. Part of a cytoplasmic complex made of HIPK1, DAB2IP and MAP3K5 in response to TNF. This complex formation promotes MAP3K5-JNK activation and subsequent apoptosis. {ECO:0000269|PubMed:12529400, ECO:0000269|PubMed:12702766, ECO:0000269|PubMed:9748262}. TISSUE SPECIFICITY: Ubiquitously expressed, with high levels in reproductive tissues. Expressed in the epithelial layer of mammary gland, uterus and epididymis, in the corpus luteum, and in post-meiotic round spermatids. {ECO:0000269|PubMed:10694743, ECO:0000269|PubMed:12529400}. +Q8BMT9 HHAT_MOUSE Protein-cysteine N-palmitoyltransferase HHAT (EC 2.3.1.-) (Hedgehog acyltransferase) (Skinny hedgehog protein) 499 57,864 Active site (1); Alternative sequence (2); Chain (1); Intramembrane (2); Lipidation (4); Region (1); Sequence conflict (1); Topological domain (13); Transmembrane (10) INTRAMEM 95 119 {ECO:0000255}.; INTRAMEM 209 223 {ECO:0000255}. TRANSMEM 6 22 Helical. {ECO:0000255}.; TRANSMEM 68 84 Helical. {ECO:0000255}.; TRANSMEM 132 148 Helical. {ECO:0000255}.; TRANSMEM 163 183 Helical. {ECO:0000255}.; TRANSMEM 250 277 Helical. {ECO:0000255}.; TRANSMEM 288 316 Helical. {ECO:0000255}.; TRANSMEM 370 386 Helical. {ECO:0000255}.; TRANSMEM 390 405 Helical. {ECO:0000255}.; TRANSMEM 434 454 Helical. {ECO:0000255}.; TRANSMEM 469 487 Helical. {ECO:0000255}. TOPO_DOM 1 5 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 23 67 Lumenal. {ECO:0000255}.; TOPO_DOM 85 94 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 120 131 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 149 162 Lumenal. {ECO:0000255}.; TOPO_DOM 184 208 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 224 249 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 278 287 Lumenal. {ECO:0000255}.; TOPO_DOM 317 369 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 387 389 Lumenal. {ECO:0000255}.; TOPO_DOM 406 433 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 455 468 Lumenal. {ECO:0000255}.; TOPO_DOM 488 499 Cytoplasmic. {ECO:0000255}. FUNCTION: Catalyzes N-terminal palmitoylation of SHH; which is required for SHH signaling during limb development. May bind GTP. {ECO:0000269|PubMed:15075292}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15075292, ECO:0000269|PubMed:18081866}; Multi-pass membrane protein {ECO:0000269|PubMed:15075292, ECO:0000269|PubMed:18081866}. +P09065 HME1_MOUSE Homeobox protein engrailed-1 (Homeobox protein en-1) (Mo-En-1) 401 40,981 Chain (1); Compositional bias (3); DNA binding (1); Sequence conflict (1) SUBCELLULAR LOCATION: Nucleus. +P49698 HNF4A_MOUSE Hepatocyte nuclear factor 4-alpha (HNF-4-alpha) (Nuclear receptor subfamily 2 group A member 1) (Transcription factor 14) (TCF-14) (Transcription factor HNF-4) 474 52,684 Alternative sequence (1); Chain (1); Cross-link (2); DNA binding (1); Domain (1); Erroneous initiation (1); Modified residue (10); Sequence conflict (3); Zinc finger (2) FUNCTION: Transcriptionally controlled transcription factor. Binds to DNA sites required for the transcription of alpha 1-antitrypsin, apolipoprotein CIII, transthyretin genes and HNF1-alpha. May be essential for development of the liver, kidney and intestine. PTM: Phosphorylated on tyrosine residue(s); phosphorylation is important for its DNA-binding activity. Phosphorylation may directly or indirectly play a regulatory role in the subnuclear distribution. Phosphorylation at Ser-313 by AMPK reduces the ability to form homodimers and bind DNA (By similarity). {ECO:0000250}.; PTM: Acetylation at Lys-458 lowers transcriptional activation by about two-fold. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Homodimerization is required for HNF4-alpha to bind to its recognition site. Interacts with PER2. {ECO:0000269|PubMed:20159955}. +Q9JL35 HMGN5_MOUSE High mobility group nucleosome-binding domain-containing protein 5 (Nucleosome-binding protein 1) (Nucleosome-binding protein 45) (NBP-45) (Protein GARP45) 406 45,344 Chain (1); Cross-link (4); Modified residue (1); Mutagenesis (2); Sequence conflict (2) FUNCTION: Preferentially binds to euchromatin and modulates cellular transcription by counteracting linker histone-mediated chromatin compaction. {ECO:0000269|PubMed:10692437, ECO:0000269|PubMed:19748358}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10692437, ECO:0000269|PubMed:19748358}. Note=Associates with nucleosomes in euchromatin and is largely excluded from constitutive heterochromatin. DOMAIN: Specifically targeted by its C-terminus to nucleosomes in euchromatin. {ECO:0000269|PubMed:19748358}. TISSUE SPECIFICITY: Expressed in liver, spleen, lung, heart, kidney, muscle and brain (at protein level). Widely expressed with highest levels in submaxillary gland, thymus, kidney and liver and lowest levels in brain, lung, pancreas and eye. {ECO:0000269|PubMed:10692437, ECO:0000269|PubMed:19748358}. +Q8HWB0 HMR1_MOUSE Major histocompatibility complex class I-related gene protein (MHC class I-related gene protein) (Class I histocompatibility antigen-like protein) 341 39,391 Alternative sequence (1); Binding site (1); Chain (1); Disulfide bond (2); Domain (1); Glycosylation (1); Mutagenesis (14); Region (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 297 317 Helical. {ECO:0000255}. TOPO_DOM 19 296 Extracellular. {ECO:0000255}.; TOPO_DOM 318 341 Cytoplasmic. {ECO:0000255}. FUNCTION: Antigen-presenting molecule specialized in presenting microbial vitamin B metabolites (By similarity). Involved in the development and expansion of a small population of T-cells expressing an invariant T-cell receptor alpha chain called mucosal-associated invariant T-cells (MAIT). MAIT lymphocytes are preferentially located in the gut lamina propria and therefore may be involved in monitoring commensal flora or serve as a distress signal. Expression and MAIT cell recognition seem to be ligand-dependent. {ECO:0000250, ECO:0000269|PubMed:15802267}. PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Endoplasmic reticulum {ECO:0000250}. SUBUNIT: Heterodimerizes with B2M, this interaction is required for surface expression. Associated with the peptide-loading complex, TAPBP, CALR and PDIA3. DOMAIN: The alpha-3 region and to a lesser extent the transmembrane and cytosolic domains regulate surface expression. The alpha-3 region mediates interaction with B2M.; DOMAIN: The ligand-binding groove is ideally suited to present small organic compounds that can originate from vitamins rather than antigenic peptides. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed thymus. Expressed in liver, kidney, spleen, heart, brain, lung, skeletal muscle and testis. {ECO:0000269|PubMed:12794138, ECO:0000269|PubMed:9325151, ECO:0000269|PubMed:9780177}. +P84075 HPCA_MOUSE Neuron-specific calcium-binding protein hippocalcin 193 22,427 Calcium binding (3); Chain (1); Domain (4); Initiator methionine (1); Lipidation (1) FUNCTION: Calcium-binding protein that may play a role in the regulation of voltage-dependent calcium channels. May also play a role in cyclic-nucleotide-mediated signaling through the regulation of adenylate and guanylate cyclases. {ECO:0000250|UniProtKB:P84074, ECO:0000250|UniProtKB:P84076}. PTM: Myristoylation facilitates association with membranes. {ECO:0000250|UniProtKB:P84076}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P84074, ECO:0000250|UniProtKB:P84076}. Membrane {ECO:0000250|UniProtKB:P84076}; Peripheral membrane protein {ECO:0000250|UniProtKB:P84076}. Note=Association with membranes is calcium-dependent (By similarity). Enriched in the perinuclear region, probably at the trans Golgi network in response to calcium (By similarity). {ECO:0000250|UniProtKB:P84074, ECO:0000250|UniProtKB:P84076}. SUBUNIT: Oligomer; oligomerization is calcium-dependent. May interact with the voltage-dependent P/Q- and N-type calcium channels CACNA1A and CACNA1B. {ECO:0000250|UniProtKB:P84074}. DOMAIN: Binds 3 calcium via EF-hand domains. The cryptic EF-hand 1 does not bind calcium. {ECO:0000250|UniProtKB:P84074}. +Q8K485 KCD11_MOUSE BTB/POZ domain-containing protein KCTD11 (KCASH1 protein) (Potassium channel tetramerization domain-containing protein 11) (RING-type E3 ubiquitin transferase subunit KCTD11) 232 26,300 Chain (1); Domain (1) Protein modification; protein ubiquitination. FUNCTION: Plays a role as a marker and a regulator of neuronal differentiation; Up-regulated by a variety of neurogenic signals, such as retinoic acid, epidermal growth factor/EGF and NGFB/nerve growth factor. Induces apoptosis, growth arrest and the expression of cyclin-dependent kinase inhibitor CDKN1B. Plays a role as a tumor repressor and inhibits cell growth and tumorigenicity of medulloblastoma (MDB). Acts as probable substrate-specific adapter for a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex towards HDAC1. Functions as antagonist of the Hedgehog pathway on cell proliferation and differentiation by affecting the nuclear transfer of transcription factor GLI1, thus maintaining cerebellar granule cells in undifferentiated state, this effect probably occurs via HDAC1 down-regulation, keeping GLI1 acetylated and inactive. When knock-down, Hedgehog antagonism is impaired and proliferation of granule cells is sustained. Activates the caspase cascade. {ECO:0000250|UniProtKB:Q693B1, ECO:0000269|PubMed:12186855, ECO:0000269|PubMed:16148242}. SUBUNIT: Homopentamer. Interacts with KCTD6 and KCTD21; KCTD11 and KCTD6 or KCTD21 may associate in pentameric assemblies. Component of the BCR(KCTD11) E3 ubiquitin ligase complex, at least composed of CUL3 and KCTD11 and RBX1. Interacts (via BTB domain) with CUL3; initially a 4:4 stoichiometry has been reported, however, electron microscopy revealed pentameric states of the BTB domain. {ECO:0000250|UniProtKB:Q693B1}. DOMAIN: The BTB domain is required for growth-suppressing properties. TISSUE SPECIFICITY: Weakly expressed in lung. In the cerebellum, higher expression in non proliferating external granule cells layer than in highly proliferating ones. {ECO:0000269|PubMed:12186855, ECO:0000269|PubMed:16148242}. +Q8CDD8 KCD20_MOUSE BTB/POZ domain-containing protein KCTD20 (Potassium channel tetramerization domain containing 20) 419 47,068 Alternative sequence (1); Chain (1); Domain (1); Erroneous initiation (1) FUNCTION: Promotes the phosphorylation of AKT family members. {ECO:0000269|PubMed:24156551}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24156551}. Note=Colocalizes with BTBD10 in filamentous structures. {ECO:0000269|PubMed:24156551}. SUBUNIT: Interacts with AKT1; AKT2 and AKT3 (PubMed:24156551). Interacts with PPP2CA and PPP1CA (PubMed:24156551). Part of a complex containing MARK4 (By similarity). {ECO:0000250|UniProtKB:Q7Z5Y7, ECO:0000269|PubMed:24156551}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:24156551}. +Q02576 HEN1_MOUSE Helix-loop-helix protein 1 (HEN-1) (Nescient helix loop helix 1) (NSCL-1) 133 14,830 Chain (1); Compositional bias (1); Domain (1) FUNCTION: May serve as DNA-binding protein and may be involved in the control of cell-type determination, possibly within the developing nervous system. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}. SUBUNIT: Efficient DNA binding requires dimerization with another bHLH protein. +D3Z4R1 HFM1_MOUSE Probable ATP-dependent DNA helicase HFM1 (EC 3.6.4.12) 1434 161,379 Chain (1); Domain (3); Motif (1); Nucleotide binding (1) FUNCTION: Required for crossover formation and complete synapsis of homologous chromosomes during meiosis. {ECO:0000269|PubMed:23555294}. +Q3UDW8 HGNAT_MOUSE Heparan-alpha-glucosaminide N-acetyltransferase (EC 2.3.1.78) (Transmembrane protein 76) 656 72,504 Active site (1); Alternative sequence (1); Chain (1); Disulfide bond (1); Erroneous initiation (5); Glycosylation (2); Modified residue (3); Region (1); Sequence conflict (5); Topological domain (12); Transmembrane (11) TRANSMEM 186 206 Helical. {ECO:0000255}.; TRANSMEM 269 289 Helical. {ECO:0000255}.; TRANSMEM 296 316 Helical. {ECO:0000255}.; TRANSMEM 339 359 Helical. {ECO:0000255}.; TRANSMEM 368 388 Helical. {ECO:0000255}.; TRANSMEM 414 434 Helical. {ECO:0000255}.; TRANSMEM 494 514 Helical. {ECO:0000255}.; TRANSMEM 523 543 Helical. {ECO:0000255}.; TRANSMEM 558 578 Helical. {ECO:0000255}.; TRANSMEM 586 606 Helical. {ECO:0000255}.; TRANSMEM 628 648 Helical. {ECO:0000255}. TOPO_DOM 1 185 Lumenal, vesicle. {ECO:0000255}.; TOPO_DOM 207 268 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 290 295 Lumenal, vesicle. {ECO:0000255}.; TOPO_DOM 317 338 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 360 367 Lumenal, vesicle. {ECO:0000255}.; TOPO_DOM 389 413 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 435 493 Lumenal, vesicle. {ECO:0000255}.; TOPO_DOM 515 522 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 544 557 Lumenal, vesicle. {ECO:0000255}.; TOPO_DOM 579 585 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 607 627 Lumenal, vesicle. {ECO:0000255}.; TOPO_DOM 649 656 Cytoplasmic. {ECO:0000255}. FUNCTION: Lysosomal acetyltransferase that acetylates the non-reducing terminal alpha-glucosamine residue of intralysosomal heparin or heparan sulfate, converting it into a substrate for luminal alpha-N-acetyl glucosaminidase. {ECO:0000269|PubMed:16960811}. PTM: Undergoes intralysosomal proteolytic cleavage; occurs within the end of the first and/or the beginning of the second luminal domain and is essential for the activation of the enzyme. {ECO:0000250}.; PTM: Glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:16960811}; Multi-pass membrane protein {ECO:0000269|PubMed:16960811}. Note=Colocalizes with the lysosomal marker LAMP2. The signal peptide is not cleaved upon translocation into the endoplasmic reticulum; the precursor is probably targeted to the lysosomes via the adapter protein complex-mediated pathway that involves tyrosine- and/or dileucine-based conserved amino acid motifs in the last C-terminus 16-amino acid domain (By similarity). {ECO:0000250}. SUBUNIT: Homooligomer. Homooligomerization is necessary for enzyme activity (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the retina. {ECO:0000269|PubMed:25859010}. +Q8R1F6 HID1_MOUSE Protein HID1 (HID1 domain-containing protein) (Protein hid-1 homolog) 788 88,779 Alternative sequence (1); Chain (1); Initiator methionine (1); Lipidation (1); Modified residue (2); Sequence conflict (1) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Note=Shuttles between the cytosol and the Golgi apparatus. {ECO:0000250}. +Q61221 HIF1A_MOUSE Hypoxia-inducible factor 1-alpha (HIF-1-alpha) (HIF1-alpha) (ARNT-interacting protein) 836 93,516 Alternative sequence (1); Chain (1); Cross-link (5); Domain (4); Modified residue (12); Motif (1); Mutagenesis (2); Region (9); Sequence conflict (14) FUNCTION: Functions as a master transcriptional regulator of the adaptive response to hypoxia. Under hypoxic conditions, activates the transcription of over 40 genes, including erythropoietin, glucose transporters, glycolytic enzymes, vascular endothelial growth factor, HILPDA, and other genes whose protein products increase oxygen delivery or facilitate metabolic adaptation to hypoxia. Plays an essential role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease. Heterodimerizes with ARNT; heterodimer binds to core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters (PubMed:26245371). Activation requires recruitment of transcriptional coactivators such as CREBBP and EP300. Activity is enhanced by interaction with both, NCOA1 or NCOA2. Interaction with redox regulatory protein APEX seems to activate CTAD and potentiates activation by NCOA1 and CREBBP. Involved in the axonal distribution and transport of mitochondria in neurons during hypoxia (By similarity). {ECO:0000250, ECO:0000269|PubMed:15225651, ECO:0000269|PubMed:17981124, ECO:0000269|PubMed:22009797, ECO:0000269|PubMed:26245371}. PTM: S-nitrosylation of Cys-810 may be responsible for increased recruitment of p300 coactivator necessary for transcriptional activity of HIF-1 complex. {ECO:0000250}.; PTM: Requires phosphorylation for DNA-binding. Phosphorylation at Ser-247 by CSNK1D/CK1 represses kinase activity and impairs ARNT binding (By similarity). Phosphorylation by GSK3-beta and PLK3 promote degradation by the proteasome. {ECO:0000250, ECO:0000269|PubMed:20889502}.; PTM: Sumoylated; with SUMO1 under hypoxia. Sumoylation is enhanced through interaction with RWDD3. Both sumoylation and desumoylation seem to be involved in the regulation of its stability during hypoxia. Sumoylation can promote either its stabilization or its VHL-dependent degradation by promoting hydroxyproline-independent HIF1A-VHL complex binding, thus leading to HIF1A ubiquitination and proteasomal degradation. Desumoylation by SENP1 increases its stability amd transcriptional activity. There is a disaccord between various publications on the effect of sumoylation and desumoylation on its stability and transcriptional activity. {ECO:0000269|PubMed:15225651, ECO:0000269|PubMed:17981124}.; PTM: Acetylation of Lys-545 by ARD1 increases interaction with VHL and stimulates subsequent proteasomal degradation. Deacetylation of Lys-719 by SIRT2 increases its interaction with and hydroxylation by EGLN1 thereby inactivating HIF1A activity by inducing its proteasomal degradation (By similarity). {ECO:0000250}.; PTM: Ubiquitinated; in normoxia, following hydroxylation and interaction with VHL. Lys-545 appears to be the principal site of ubiquitination. Clioquinol, the Cu/Zn-chelator, inhibits ubiquitination through preventing hydroxylation at Asn-813 (By similarity). {ECO:0000250|UniProtKB:Q16665}.; PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of asparagine is (S) stereospecific within HIF CTAD domains. {ECO:0000250}.; PTM: In normoxia, is hydroxylated on Pro-402 and Pro-577 in the oxygen-dependent degradation domain (ODD) by EGLN1/PHD2 and EGLN2/PHD1. EGLN3/PHD3 has also been shown to hydroxylate Pro-577. The hydroxylated prolines promote interaction with VHL, initiating rapid ubiquitination and subsequent proteasomal degradation. Deubiquitinated by USP20. Under hypoxia, proline hydroxylation is impaired and ubiquitination is attenuated, resulting in stabilization (By similarity). In normoxia, is hydroxylated on Asn-813 by HIF1AN, thus abrogating interaction with CREBBP and EP300 and preventing transcriptional activation. Repressed by iron ion, via Fe(2+) prolyl hydroxylase (PHD) enzymes-mediated hydroxylation and subsequent proteasomal degradation. {ECO:0000250|UniProtKB:Q16665}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15225651}. Nucleus {ECO:0000269|PubMed:15225651, ECO:0000269|PubMed:21546903}. Nucleus speckle {ECO:0000269|PubMed:21546903}. Note=Colocalizes with HIF3A isoform 2 in the nucleus and speckles (PubMed:21546903). Cytoplasmic in normoxia, nuclear translocation in response to hypoxia (By similarity). {ECO:0000250|UniProtKB:Q16665, ECO:0000269|PubMed:21546903}. SUBUNIT: Interacts with HIF3A isoform 2 (PubMed:21546903). Interacts with the ARNT; forms a heterodimer that binds core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters (PubMed:26245371). Interacts with Interacts with NCOA1, NCOA2, APEX and HSP90. Interacts (hydroxylated within the ODD domain) with VHLL (via beta domain); the interaction, leads to polyubiquitination and subsequent HIF1A proteasomal degradation. During hypoxia, sumoylated HIF1A also binds VHL; the interaction promotes the ubiquitination of HIF1A. Interacts with SENP1; the interaction desumoylates HIF1A resulting in stabilization and activation of transcription. Interacts (Via the ODD domain) with ARD1A; the interaction appears not to acetylate HIF1A nor have any affect on protein stability, during hypoxia. Interacts with RWDD3; the interaction enhances HIF1A sumoylation. Interacts with RORA (via the DNA binding domain); the interaction enhances HIF1A transcription under hypoxia through increasing protein stability. Interaction with PSMA7 inhibits the transactivation activity of HIF1A under both normoxic and hypoxia-mimicking conditions. Interacts with USP20. Interacts with RACK1; promotes HIF1A ubiquitination and proteasome-mediated degradation. Interacts with EP300 (via TAZ-type 1 domain); the interaction is stimulated in response to hypoxia and inhibited by CITED2. Interacts with CREBBP (via TAZ-type 1 domain). Interacts with SIRT2. Interacts (deacetylated form) with EGLN1 (By similarity). Interacts with TSGA10. Interacts (via N-terminus) with USP19. Interacts with COPS5; the interaction increases the transcriptional activity of HIF1A through increased stability. Interacts with CBFA2T3. Interacts with HSP90AA1 and HSP90AB1 (By similarity). {ECO:0000250|UniProtKB:Q16665, ECO:0000269|PubMed:11707426, ECO:0000269|PubMed:16777103, ECO:0000269|PubMed:21546903, ECO:0000269|PubMed:26245371}. DOMAIN: Contains two independent C-terminal transactivation domains, NTAD and CTAD, which function synergistically. Their transcriptional activity is repressed by an intervening inhibitory domain (ID) (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. +P16045 LEG1_MOUSE Galectin-1 (Gal-1) (14 kDa lectin) (Beta-galactoside-binding lectin L-14-I) (Galaptin) (Lactose-binding lectin 1) (Lectin galactoside-binding soluble 1) (S-Lac lectin 1) 135 14,866 Beta strand (11); Binding site (2); Chain (1); Domain (1); Frameshift (2); Initiator methionine (1); Modified residue (8); Region (2); Sequence conflict (3) FUNCTION: Lectin that binds beta-galactoside and a wide array of complex carbohydrates. Plays a role in regulating apoptosis, cell proliferation and cell differentiation. Inhibits CD45 protein phosphatase activity and therefore the dephosphorylation of Lyn kinase. Strong inducer of T-cell apoptosis. {ECO:0000250|UniProtKB:P09382, ECO:0000269|PubMed:1986871}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P09382}. SUBUNIT: Homodimer. Binds LGALS3BP. Interacts with CD2, CD3, CD4, CD6, CD7, CD43, ALCAM and CD45. Interacts with laminin (via poly-N-acetyllactosamine). Interacts with SUSD2. {ECO:0000250|UniProtKB:P09382}. +Q0VBL6 HIF3A_MOUSE Hypoxia-inducible factor 3-alpha (HIF-3-alpha) (HIF3-alpha) (Basic-helix-loop-helix-PAS protein MOP7) (HIF3-alpha-1) (Inhibitory PAS domain protein) (IPAS) (Member of PAS protein 7) (Neonatal and embryonic PAS protein) 662 73,044 Alternative sequence (4); Chain (1); Cross-link (2); Domain (3); Modified residue (1); Motif (2); Region (4); Sequence conflict (18) FUNCTION: Acts as a transcriptional regulator in adaptive response to low oxygen tension. Acts as a regulator of hypoxia-inducible gene expression (PubMed:9840812, PubMed:11734856, PubMed:21546903). Plays a role in the development of the cardiorespiratory system (PubMed:18070924). {ECO:0000269|PubMed:11734856, ECO:0000269|PubMed:18070924, ECO:0000269|PubMed:21546903, ECO:0000269|PubMed:9840812}.; FUNCTION: Isoform 1: Acts as positive regulator of hypoxia-inducible gene expression. Associates to core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters in a ARNT-dependent manner, and hence also participates in the transcriptional activation of reporter genes driven by HRE (PubMed:9840812). {ECO:0000269|PubMed:9840812}.; FUNCTION: Isoform 2: Attenuates the ability of transcription factor HIF1A, EPAS1 and the HIF1A-ARNT complex to bind to hypoxia-responsive elements (HRE) located within the enhancer/promoter of hypoxia-inducible target genes and hence inhibits HRE-driven transcriptional activation. Functions as an inhibitor of angiogenesis in hypoxic cells of the cornea. May act as a tumor suppressor (PubMed:11734856). May also be involved in apoptosis (PubMed:21546903). {ECO:0000269|PubMed:11734856, ECO:0000269|PubMed:21546903}.; FUNCTION: Isoform 3: Attenuates the ability of transcription factor HIF1A, EPAS1 and the HIF1A-ARNT complex to bind to hypoxia-responsive elements (HRE) located within the enhancer/promoter of hypoxia-inducible target genes and hence inhibits HRE-driven transcriptional activation (PubMed:18070924). Plays also a role in the development of the lung and heart during embryonic and neonatal stages (PubMed:18070924). {ECO:0000269|PubMed:18070924}. PTM: In normoxia, hydroxylated on Pro-487 in the oxygen-dependent degradation domain (ODD) by PHD. The hydroxylated proline promotes interaction with VHL, initiating rapid ubiquitination and subsequent proteasomal degradation (By similarity). {ECO:0000250|UniProtKB:Q9Y2N7}.; PTM: Ubiquitinated; ubiquitination occurs in a VHL- and oxygen-dependent pathway and subsequently targeted for proteasomal degradation. {ECO:0000250|UniProtKB:Q9Y2N7}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y2N7}. Cytoplasm {ECO:0000250|UniProtKB:Q9Y2N7}. Note=In the nuclei of all periportal and perivenous hepatocytes. In the distal perivenous zone, detected in the cytoplasm of the hepatocytes. Localized in the cytoplasm and nuclei under normoxia, but increased in the nucleus under hypoxic conditions. Colocalized with HIF1A in kidney tumors. {ECO:0000250|UniProtKB:Q9JHS2, ECO:0000250|UniProtKB:Q9Y2N7}.; SUBCELLULAR LOCATION: Isoform 2: Nucleus {ECO:0000269|PubMed:21546903, ECO:0000269|PubMed:24092767}. Cytoplasm {ECO:0000269|PubMed:21546903, ECO:0000269|PubMed:24092767}. Nucleus speckle {ECO:0000269|PubMed:21546903}. Mitochondrion {ECO:0000269|PubMed:21546903}. Note=Colocalizes with BAD in the cytoplasm (PubMed:21546903). Colocalizes with EPAS1 and HIF1A in the nucleus and speckles (PubMed:21546903). Shuttles between the nucleus and the cytoplasm in a CRM1-dependent manner (PubMed:24092767). {ECO:0000269|PubMed:21546903, ECO:0000269|PubMed:24092767}. SUBUNIT: Isoform 1 interacts with ARNT (PubMed:9840812). Isoform 2 interacts with HIF1A (PubMed:11734856, PubMed:21546903). Isoform 2 interacts EPAS1 (PubMed:21546903). Isoform 2 interacts (via C-terminus domain) with BAD; the interaction reduces the binding between BAD and BAX (PubMed:21546903). Isoform 2 (via C-terminus domain) interacts with BCL2L2 and MCL1 (PubMed:21546903). Interacts with VHL (By similarity). {ECO:0000250|UniProtKB:Q9Y2N7, ECO:0000269|PubMed:11734856, ECO:0000269|PubMed:21546903, ECO:0000269|PubMed:9840812}. DOMAIN: Isoform 2 contains a nuclear localization signal between amino acid positions 75 and 98. Isoform 2 contains a nuclear export signal between amino acid positions 228 and 272. {ECO:0000269|PubMed:24092767}. TISSUE SPECIFICITY: Isoform 3 is expressed in endothelial cells of vessels and capillaries in alveoli of the neonatal lung (at protein level) (PubMed:18070924). Expressed in lung, brain, heart and kidney (PubMed:9840812). Isoform 2 is expressed in heart and lung (PubMed:12119283). Isoform 2 is highly expressed in the epithelial cell layer of the cornea with lower expression in the layers of ganglion cells, inner nuclear cells, and rods and cones of the retina (PubMed:11734856). Isoform 2 is expressed in the cerebellum only in the Purkinje cell layer (PubMed:11734856). {ECO:0000269|PubMed:11734856, ECO:0000269|PubMed:12119283, ECO:0000269|PubMed:18070924, ECO:0000269|PubMed:9840812}. +Q8K419 LEG4_MOUSE Galectin-4 (Gal-4) (Lactose-binding lectin 4) 326 36,372 Beta strand (11); Chain (1); Domain (2); Helix (1); Region (1); Sequence conflict (4) FUNCTION: Galectin that binds lactose and a related range of sugars. {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. DOMAIN: Contains two homologous but distinct carbohydrate-binding domains. TISSUE SPECIFICITY: Epithelial cells of the embryonic and adult gastrointestinal tract. Expressed at about equal levels in colon and small intestine but much less in stomach. {ECO:0000269|PubMed:9446608}. +Q9D8V0 HM13_MOUSE Minor histocompatibility antigen H13 (EC 3.4.23.-) (Presenilin-like protein 3) (Signal peptide peptidase) 378 41,748 Active site (2); Alternative sequence (5); Chain (1); Glycosylation (2); Modified residue (1); Motif (1); Sequence conflict (12); Topological domain (10); Transmembrane (9) TRANSMEM 32 52 Helical. {ECO:0000255}.; TRANSMEM 78 98 Helical. {ECO:0000255}.; TRANSMEM 101 121 Helical. {ECO:0000255}.; TRANSMEM 158 178 Helical. {ECO:0000255}.; TRANSMEM 182 202 Helical. {ECO:0000255}.; TRANSMEM 210 230 Helical. {ECO:0000255}.; TRANSMEM 257 277 Helical. {ECO:0000255}.; TRANSMEM 291 311 Helical. {ECO:0000255}.; TRANSMEM 315 335 Helical. {ECO:0000255}. TOPO_DOM 1 31 Lumenal. {ECO:0000250|UniProtKB:Q8TCT9}.; TOPO_DOM 53 77 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 99 100 Lumenal. {ECO:0000255}.; TOPO_DOM 122 157 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 179 181 Lumenal. {ECO:0000255}.; TOPO_DOM 203 209 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 231 256 Lumenal. {ECO:0000250|UniProtKB:Q8TCT9}.; TOPO_DOM 278 290 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 312 314 Lumenal. {ECO:0000255}.; TOPO_DOM 336 378 Cytoplasmic. {ECO:0000250|UniProtKB:Q8TCT9}. FUNCTION: Catalyzes intramembrane proteolysis of some signal peptides after they have been cleaved from a preprotein, resulting in the release of the fragment from the ER membrane into the cytoplasm. Required to generate lymphocyte cell surface (HLA-E) epitopes derived from MHC class I signal peptides. Involved in the intramembrane cleavage of the integral membrane protein PSEN1. Cleaves the integral membrane protein XBP1 isoform 1 in a DERL1/RNF139-dependent manner (By similarity). May play a role in graft rejection (PubMed:9354467). {ECO:0000250|UniProtKB:Q8TCT9, ECO:0000269|PubMed:9354467}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12972007, ECO:0000269|PubMed:16730383}; Multi-pass membrane protein {ECO:0000305}. Membrane {ECO:0000250|UniProtKB:Q8TCT9}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8TCT9}; Lumenal side {ECO:0000250|UniProtKB:Q8TCT9}.; SUBCELLULAR LOCATION: Isoform 4: Cell membrane {ECO:0000269|PubMed:16730383}; Multi-pass membrane protein {ECO:0000305}. SUBUNIT: Monomer. Homodimer (By similarity). Interacts with RNF139 (PubMed:19720873). Interacts with DERL1 and XBP1 isoform 1 (By similarity). {ECO:0000250|UniProtKB:Q8TCT9, ECO:0000269|PubMed:19720873}. DOMAIN: The first transmembrane domain may act as a type I signal anchor. The PAL motif is required for normal active site conformation. {ECO:0000250|UniProtKB:P49768, ECO:0000250|UniProtKB:Q8TCT9}. TISSUE SPECIFICITY: Widely expressed with highest levels in liver and kidney. In the brain, expressed predominantly in hippocampus, amygdala, piriform cortex, choroid plexus and arcuate nucleus of the hypothalamic area. Isoform 1 is more strongly expressed than isoform 4 in most tissues except brain and skeletal muscle where isoform 4 is the dominant isoform and in testis where isoform 1 and isoform 4 are expressed at similar levels. In the brain, isoform 4 is not detected in the choroid plexus. {ECO:0000269|PubMed:12972007, ECO:0000269|PubMed:16730383}. +P43687 HMX2_MOUSE Homeobox protein HMX2 (Homeobox protein Nkx-5.2) 273 29,634 Chain (1); DNA binding (1); Sequence conflict (1) FUNCTION: Transcription factor involved in specification of neuronal cell types and which is required for inner ear and hypothalamus development. {ECO:0000269|PubMed:11748138, ECO:0000269|PubMed:15363417}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: Expressed in the developing CNS, including a specific expression in vestibular structures throughout inner ear development. {ECO:0000269|PubMed:11748138}. +Q9Z2Y3 HOME1_MOUSE Homer protein homolog 1 (Homer-1) (VASP/Ena-related gene up-regulated during seizure and LTP 1) (Vesl-1) 366 41,413 Alternative sequence (6); Chain (1); Coiled coil (1); Domain (1); Initiator methionine (1); Modified residue (2); Region (1); Sequence conflict (3) FUNCTION: Postsynaptic density scaffolding protein. Binds and cross-links cytoplasmic regions of GRM1, GRM5, ITPR1, DNM3, RYR1, RYR2, SHANK1 and SHANK3. By physically linking GRM1 and GRM5 with ER-associated ITPR1 receptors, it aids the coupling of surface receptors to intracellular calcium release. May also couple GRM1 to PI3 kinase through its interaction with AGAP2. Isoform 1 regulates the trafficking and surface expression of GRM5. Differentially regulates the functions of the calcium activated channel ryanodine receptors RYR1 and RYR2. Isoform 1 decreases the activity of RYR2, and increases the activity of RYR1, whereas isoform 5 counteracts the effects by competing for binding sites. Isoform 3 regulates the trafficking and surface expression of GRM5. Isoform 5 acts as a natural dominant negative, in dynamic competition with constitutively expressed isoform 1, isoform 2 and isoform 3 to regulate synaptic metabotropic glutamate function. Isoform 5, may be involved in the structural changes that occur at synapses during long-lasting neuronal plasticity and development (By similarity). Forms a high-order complex with SHANK1, which in turn is necessary for the structural and functional integrity of dendritic spines (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9Z214}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24153177}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000269|PubMed:24153177}. Cell junction, synapse {ECO:0000269|PubMed:24153177}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:Q9Z214}. Note=Isoform 1 inhibits surface expression of GRM5 causing it to be retained in the endoplasmic reticulum. The N-terminal of isoform 2 may facilitate trafficking of the complex with GRM5 from the endoplasmic reticulum (ER) to the plasma membrane (PM). SUBUNIT: Tetramer; this tetrameric structure is critical for forming the high-order complex with SHANK1, which in turn is necessary for the structural and functional integrity of dendritic spines (By similarity). Isoform 1, isoform 2 and isoform 3 encode a coiled-coil structure that mediates homo- and heteromultimerization. Interacts with GRM1, GRM5, ITPR1, DNM3, RYR1, RYR2 and SHANK3. Interacts with IFT57 and OPHN1. Interacts with SHANK1; forms high-order polymerized complex with a mesh-like network structure, at least composed of SHANK1, HOMER1 and DLGAP1; the complex formation is SHANK1 multimerization dependent (By similarity). {ECO:0000250|UniProtKB:Q9Z214, ECO:0000269|PubMed:12379179, ECO:0000269|PubMed:17107665, ECO:0000269|PubMed:21558424, ECO:0000269|PubMed:24153177, ECO:0000269|PubMed:9808459}. DOMAIN: The WH1 domain interacts with the PPXXF motif in GRM1, GRM5, RYR1, RYR2, ITPR1, SHANK 1 and SHANK3. The coiled-Coil domain forms an antiparallel tetrameric arrangement (By similarity). {ECO:0000250|UniProtKB:Q9Z214}. TISSUE SPECIFICITY: Isoform 1, isoform 3 and isoform 5 are expressed in skeletal muscle at the level of the Z line, in heart, forebrain and cerebellum. Isoform 2, is a minor isoform and is expressed in cardiac and skeletal muscle. Isoform 5 is expressed in the postsynaptic region of neurons. {ECO:0000269|PubMed:12379179, ECO:0000269|PubMed:24153177}. +P16882 GHR_MOUSE Growth hormone receptor (GH receptor) (Somatotropin receptor) [Cleaved into: Growth hormone-binding protein (GH-binding protein) (GHBP) (Serum-binding protein)] 650 72,783 Alternative sequence (2); Chain (2); Disulfide bond (3); Domain (1); Glycosylation (4); Modified residue (1); Motif (3); Region (1); Sequence conflict (11); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 274 297 Helical. {ECO:0000255}. TOPO_DOM 25 273 Extracellular. {ECO:0000255}.; TOPO_DOM 298 650 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for pituitary gland growth hormone involved in regulating postnatal body growth. On ligand binding, couples to, and activates the JAK2/STAT5 pathway (By similarity). {ECO:0000250}.; FUNCTION: The soluble form (GHBP) acts as a reservoir of growth hormone in plasma and may be a modulator/inhibitor of GH signaling. PTM: On GH binding, phosphorylated on tyrosine residues in the cytoplasmic domain by JAK2. {ECO:0000250}.; PTM: On ligand binding, ubiquitinated on lysine residues in the cytoplasmic domain. This ubiquitination is not sufficient for GHR internalization (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Note=On growth hormone binding, GHR is ubiquitinated, internalized, down-regulated and transported into a degradative or non-degradative pathway. {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 2: Secreted.; SUBCELLULAR LOCATION: Growth hormone-binding protein: Secreted {ECO:0000250}. Note=Complexed to a substantial fraction of circulating GH. {ECO:0000250}. SUBUNIT: On growth hormone (GH) binding, forms homodimers and binds JAK2 via a box 1-containing domain. Binding to SOCS3 inhibits JAK2 activation, binding to CIS and SOCS2 inhibits STAT5 activation. {ECO:0000250}. DOMAIN: The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.; DOMAIN: The box 1 motif is required for JAK interaction and/or activation.; DOMAIN: The extracellular domain is the ligand-binding domain representing the growth hormone-binding protein (GHBP).; DOMAIN: The ubiquitination-dependent endocytosis motif (UbE) is required for recruitment of the ubiquitin conjugation system on to the receptor and for its internalization. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in all tissues tested including, liver, heart, adipose tissue, mammary gland, testes, ovary, brain, kidney and muscle. Highest levels in liver. +Q99P50 GHSR_MOUSE Growth hormone secretagogue receptor type 1 (GHS-R) (GH-releasing peptide receptor) (GHRP) (Ghrelin receptor) 364 40,969 Chain (1); Disulfide bond (1); Glycosylation (3); Sequence conflict (1); Topological domain (8); Transmembrane (7) TRANSMEM 41 66 Helical; Name=1. {ECO:0000255}.; TRANSMEM 73 96 Helical; Name=2. {ECO:0000255}.; TRANSMEM 118 139 Helical; Name=3. {ECO:0000255}.; TRANSMEM 163 183 Helical; Name=4. {ECO:0000255}.; TRANSMEM 212 235 Helical; Name=5. {ECO:0000255}.; TRANSMEM 264 285 Helical; Name=6. {ECO:0000255}.; TRANSMEM 303 326 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 40 Extracellular. {ECO:0000255}.; TOPO_DOM 67 72 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 97 117 Extracellular. {ECO:0000255}.; TOPO_DOM 140 162 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 184 211 Extracellular. {ECO:0000255}.; TOPO_DOM 236 263 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 286 302 Extracellular. {ECO:0000255}.; TOPO_DOM 327 364 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for ghrelin, coupled to G-alpha-11 proteins. Stimulates growth hormone secretion. Binds also other growth hormone releasing peptides (GHRP) (e.g. Met-enkephalin and GHRP-6) as well as non-peptide, low molecular weight secretagogues (e.g. L-692,429, MK-0677, adenosine) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +P99025 GFRP_MOUSE GTP cyclohydrolase 1 feedback regulatory protein (GFRP) (GTP cyclohydrolase I feedback regulatory protein) (p35) 84 9,584 Chain (1); Initiator methionine (1) FUNCTION: Mediates tetrahydrobiopterin inhibition of GTP cyclohydrolase 1. This inhibition is reversed by L-phenylalanine (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus membrane {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. SUBUNIT: Homopentamer. Forms a complex with GCH1 where a GCH1 homodecamer is sandwiched by two GFRP homopentamers. Interacts with GCH1 (By similarity). {ECO:0000250}. +P58710 GGLO_MOUSE L-gulonolactone oxidase (LGO) (EC 1.1.3.8) (L-gulono-gamma-lactone oxidase) (GLO) 440 50,478 Chain (1); Domain (1); Modified residue (1); Sequence conflict (1); Transmembrane (1) TRANSMEM 251 273 Helical. {ECO:0000255}. Cofactor biosynthesis; L-ascorbate biosynthesis via UDP-alpha-D-glucuronate pathway; L-ascorbate from UDP-alpha-D-glucuronate: step 4/4. FUNCTION: Oxidizes L-gulono-1,4-lactone to hydrogen peroxide and L-xylo-hexulonolactone which spontaneously isomerizes to L-ascorbate. {ECO:0000269|PubMed:14962674}. SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in liver. {ECO:0000269|PubMed:14962674}. +Q8K349 GIMA6_MOUSE GTPase IMAP family member 6 (Immunity-associated nucleotide 6 protein) (IAN-6) (mIAN6) 305 34,145 Binding site (2); Chain (1); Domain (1); Nucleotide binding (2); Sequence caution (1); Sequence conflict (2) SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. +Q3UPY5 GLBL2_MOUSE Beta-galactosidase-1-like protein 2 (EC 3.2.1.-) 636 72,236 Active site (2); Alternative sequence (1); Chain (1); Compositional bias (2); Sequence conflict (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q8BHE1 GEMI8_MOUSE Gem-associated protein 8 (Gemin-8) (Protein FAM51A1) 238 28,396 Chain (1); Coiled coil (1); Erroneous initiation (1); Modified residue (1); Sequence conflict (2) FUNCTION: The SMN complex plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, gem {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Found in nuclear bodies called gems (Gemini of Cajal bodies) that are often in proximity to Cajal (coiled) bodies. Also found in the cytoplasm (By similarity). {ECO:0000250}. SUBUNIT: Part of the core SMN complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8 and STRAP/UNRIP. Part of the SMN-Sm complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8, STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG. Interacts directly with SMN1 and with the GEMIN6-GEMIN7 heterodimer, mediating their interaction (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed in embryonic tissues (at protein level). {ECO:0000269|PubMed:16434402}. +P17439 GLCM_MOUSE Lysosomal acid glucosylceramidase (Lysosomal acid GCase) (EC 3.2.1.45) (Acid beta-glucosidase) (Beta-glucocerebrosidase) (Cholesterol glucosyltransferase) (SGTase) (EC 2.4.1.-) (Cholesteryl-beta-glucosidase) (EC 3.2.1.104) (D-glucosyl-N-acylsphingosine glucohydrolase) 515 57,622 Active site (2); Chain (1); Disulfide bond (2); Glycosylation (5); Signal peptide (1) Steroid metabolism; cholesterol metabolism. Sphingolipid metabolism. FUNCTION: Glucosylceramidase that catalyzes, within the lysosomal compartment, the hydrolysis of glucosylceramide/GlcCer into free ceramide and glucose (PubMed:24211208). Thereby, plays a central role in the degradation of complex lipids and the turnover of cellular membranes (PubMed:27378698). Through the production of ceramides, participates to the PKC-activated salvage pathway of ceramide formation (By similarity). Also plays a role in cholesterol metabolism (PubMed:24211208). May either catalyze the glucosylation of cholesterol, through a transglucosylation reaction that transfers glucose from glucosylceramide to cholesterol (PubMed:24211208). The short chain saturated C8:0-GlcCer and the mono-unsaturated C18:0-GlcCer being the most effective glucose donors for that transglucosylation reaction (By similarity). Under specific conditions, may alternatively catalyze the reverse reaction, transferring glucose from cholesteryl-beta-D-glucoside to ceramide (By similarity). Finally, may also hydrolyze cholesteryl-beta-D-glucoside to produce D-glucose and cholesterol (By similarity). {ECO:0000250|UniProtKB:P04062, ECO:0000269|PubMed:24211208, ECO:0000269|PubMed:27378698}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:P04062}; Peripheral membrane protein {ECO:0000250|UniProtKB:P04062}; Lumenal side {ECO:0000250|UniProtKB:P04062}. Note=Interaction with saposin-C promotes membrane [?]association. Targeting to lysosomes occurs through an alternative MPR-independent mechanism via SCARB2. {ECO:0000250|UniProtKB:P04062}. SUBUNIT: Interacts with saposin-C. Interacts with SCARB2. Interacts with TCP1. {ECO:0000250|UniProtKB:P04062}. +P32082 GHRHR_MOUSE Growth hormone-releasing hormone receptor (GHRH receptor) (Growth hormone-releasing factor receptor) (GRF receptor) (GRFR) 423 47,004 Chain (1); Disulfide bond (3); Glycosylation (2); Natural variant (1); Sequence conflict (1); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 133 152 Helical; Name=1. {ECO:0000255}.; TRANSMEM 163 181 Helical; Name=2. {ECO:0000255}.; TRANSMEM 205 227 Helical; Name=3. {ECO:0000255}.; TRANSMEM 241 262 Helical; Name=4. {ECO:0000255}.; TRANSMEM 281 304 Helical; Name=5. {ECO:0000255}.; TRANSMEM 330 348 Helical; Name=6. {ECO:0000255}.; TRANSMEM 362 381 Helical; Name=7. {ECO:0000255}. TOPO_DOM 23 132 Extracellular. {ECO:0000255}.; TOPO_DOM 153 162 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 182 204 Extracellular. {ECO:0000255}.; TOPO_DOM 228 240 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 263 280 Extracellular. {ECO:0000255}.; TOPO_DOM 305 329 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 349 361 Extracellular. {ECO:0000255}.; TOPO_DOM 382 423 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for GRF, coupled to G proteins which activate adenylyl cyclase. Stimulates somatotroph cell growth, growth hormone gene transcription and growth hormone secretion. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Pituitary gland. DISEASE: Note=Little (lit) mice exhibits anterior pituitary hypoplasia. +Q02596 GLCM1_MOUSE Glycosylation-dependent cell adhesion molecule 1 (GlyCAM-1) (Endothelial ligand FOR L-selectin) (MC26) (SGP50) (Sulfated 50 kDa glycoprotein) 151 16,209 Chain (1); Compositional bias (2); Glycosylation (1); Modified residue (4); Signal peptide (1) FUNCTION: Adhesion molecule that accomplishes cell binding by presenting carbohydrate(s) to the lectin domain of L-selectin. PTM: Extensively O-glycosylated. SUBCELLULAR LOCATION: Cell membrane. TISSUE SPECIFICITY: Lymph nodes. Associated with the lumenal surface of the high endothelial venules of peripheral lymph nodes. +P20764 IGLL1_MOUSE Immunoglobulin lambda-like polypeptide 1 (CD179 antigen-like family member B) (Ig lambda-5) (CD antigen CD179b) 209 22,772 Chain (1); Disulfide bond (2); Domain (1); Region (2); Sequence conflict (3); Signal peptide (1) FUNCTION: Critical for B-cell development. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Associates non-covalently with VPREB1. {ECO:0000250}. TISSUE SPECIFICITY: Selectively expressed in pre-B lymphocytes. {ECO:0000269|PubMed:3024017}. +Q6YNI2 GPR6_MOUSE G-protein coupled receptor 6 (Sphingosine 1-phosphate receptor GPR6) 363 38,085 Chain (1); Compositional bias (2); Glycosylation (3); Lipidation (1); Modified residue (3); Topological domain (8); Transmembrane (7) TRANSMEM 76 95 Helical; Name=1. {ECO:0000255}.; TRANSMEM 108 131 Helical; Name=2. {ECO:0000255}.; TRANSMEM 144 165 Helical; Name=3. {ECO:0000255}.; TRANSMEM 187 206 Helical; Name=4. {ECO:0000255}.; TRANSMEM 232 250 Helical; Name=5. {ECO:0000255}.; TRANSMEM 279 305 Helical; Name=6. {ECO:0000255}.; TRANSMEM 311 332 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 75 Extracellular. {ECO:0000255}.; TOPO_DOM 96 107 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 132 143 Extracellular. {ECO:0000255}.; TOPO_DOM 166 186 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 207 231 Extracellular. {ECO:0000255}.; TOPO_DOM 251 278 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 306 310 Extracellular. {ECO:0000255}.; TOPO_DOM 333 363 Cytoplasmic. {ECO:0000255}. FUNCTION: Orphan receptor with constitutive G(s) signaling activity that activate cyclic AMP. Promotes neurite outgrowth and blocks myelin inhibition in neurons (By similarity). {ECO:0000250, ECO:0000269|PubMed:14592418}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:17284443}; Multi-pass membrane protein {ECO:0000305|PubMed:17284443}. Note=Highly expressed and localized along the cytoplasmic membrane as well as in a perinuclear compartment. TISSUE SPECIFICITY: Mainly expressed in the brain. Selectively expressed in striatopallidal neurons in the striatum. {ECO:0000269|PubMed:17284443, ECO:0000269|PubMed:17934457}. +P21765 GPX5_MOUSE Epididymal secretory glutathione peroxidase (EC 1.11.1.9) (Epididymis-specific glutathione peroxidase-like protein) (EGLP) (Glutathione peroxidase 5) (GPx-5) (GSHPx-5) (Major androgen-regulated protein) (arMEP24) 221 25,393 Active site (1); Chain (1); Sequence conflict (7); Signal peptide (1) FUNCTION: Protects cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione. May constitute a glutathione peroxidase-like protective system against peroxide damage in sperm membrane lipids. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Epididymis. +Q921N8 GPS2_MOUSE G protein pathway suppressor 2 (GPS-2) 327 36,738 Chain (1); Coiled coil (1); Cross-link (2); Modified residue (3); Mutagenesis (8); Region (1) FUNCTION: Key regulator of inflammation, lipid metabolism and mitochondrion homeostasis that acts by inhibiting the activity of the ubiquitin-conjugating enzyme UBE2N/Ubc13, thereby inhibiting 'Lys-63'-linked ubiquitination (PubMed:22424771, PubMed:24953653, PubMed:28039360, PubMed:28123943, PubMed:29499132). In the nucleus, can both acts as a corepressor and coactivator of transcription, depending on the context (PubMed:18218630, PubMed:24953653, PubMed:25519902, PubMed:27270589, PubMed:28039360). Acts as a transcription coactivator in adipocytes by promoting the recruitment of PPARG to promoters: acts by inhibiting the activity of the ubiquitin-conjugating enzyme UBE2N/Ubc13, leading to stabilization of KDM4A and subsequent histone H3 'Lys-9' (H3K9) demethylation (PubMed:22666460, PubMed:24953653). Promotes cholesterol efflux by acting as a transcription coactivator (By similarity). Acts as a regulator of B-cell development by inhibiting UBE2N/Ubc13, thereby restricting the activation of Toll-like receptors (TLRs) and B-cell antigen receptors (BCRs) signaling pathways (PubMed:28039360). Acts as a key mediator of mitochondrial stress response: in response to mitochondrial depolarization, relocates from the mitochondria to the nucleus following desumoylation and specifically promotes expression of nuclear-encoded mitochondrial genes (PubMed:29499132). Promotes transcription of nuclear-encoded mitochondrial genes by inhibiting UBE2N/Ubc13 (PubMed:29499132). Can also act as a corepressor as part of the N-Cor repressor complex by repressing active PPARG (PubMed:25519902). Plays an anti-inflammatory role in macrophages and is required for insulin sensitivity by acting as a corepressor (PubMed:27270589). Plays an anti-inflammatory role during the hepatic acute phase response by interacting with sumoylated NR1H2 and NR5A2 proteins, thereby preventing N-Cor corepressor complex dissociation (By similarity). In the cytosol, also plays a non-transcriptional role by regulating insulin signaling and pro-inflammatory pathways (PubMed:22424771, PubMed:28123943). In the cytoplasm, acts as a negative regulator of inflammation by inhibiting the proinflammatory TNF-alpha pathway; acts by repressing UBE2N/Ubc13 activity (PubMed:22424771). In the cytoplasm of adipocytes, restricts the activation of insulin signaling via inhibition of UBE2N/Ubc13-mediated ubiquitination of AKT (PubMed:28123943). Able to suppress G-protein- and mitogen-activated protein kinase-mediated signal transduction (By similarity). {ECO:0000250|UniProtKB:Q13227, ECO:0000269|PubMed:18218630, ECO:0000269|PubMed:22424771, ECO:0000269|PubMed:22666460, ECO:0000269|PubMed:24953653, ECO:0000269|PubMed:25519902, ECO:0000269|PubMed:27270589, ECO:0000269|PubMed:28039360, ECO:0000269|PubMed:28123943, ECO:0000269|PubMed:29499132}. PTM: Sumoylation regulates its subcellular location (PubMed:26070566, PubMed:29499132). Sumoylation at Lys-45 and Lys-71 regulates the shuttling between the cytoplasm and the nucleus (By similarity). Sumoylation at Lys-71 is required for interaction with TBL1X (PubMed:26070566). Sumoylated at Lys-45 and Lys-71 in mitochondrion (PubMed:29499132). Desumoylation by SENP1 leads to relocation from the mitochondria to the nucleus (PubMed:29499132). {ECO:0000250|UniProtKB:Q13227, ECO:0000269|PubMed:26070566, ECO:0000269|PubMed:29499132}.; PTM: Ubiquitinated at the C-terminus by SIAH2; leading to its degradation by the proteasome. Interaction with TBL1X and methylation at Arg-323 protect GPS2 against ubiquitination and degradation. {ECO:0000269|PubMed:26070566}.; PTM: Methylated at Arg-312 and Arg-323 by PRMT6. Methylation at Arg-323 protects from degradation by the proteasome. {ECO:0000269|PubMed:26070566}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18218630, ECO:0000269|PubMed:22424771, ECO:0000269|PubMed:22666460, ECO:0000269|PubMed:26070566, ECO:0000269|PubMed:29499132}. Mitochondrion {ECO:0000269|PubMed:29499132}. Cytoplasm, cytosol {ECO:0000269|PubMed:22424771}. Note=Sumoylation regulates the subcellular location (PubMed:29499132). Relocates from the mitochondria to the nucleus following desumoylation, leading to mediate mitochondrial stress response (PubMed:29499132). {ECO:0000250|UniProtKB:Q13227, ECO:0000269|PubMed:29499132}. SUBUNIT: Component of the N-Cor repressor complex, at least composed of NCOR1, NCOR2, HDAC3, TBL1X, TBL1R, CORO2A and GPS2 (PubMed:25519902). Interacts (when sumoylated at Lys-71) with TBL1X; leading to protect GPS2 from degradation by the proteasome (PubMed:26070566). Interacts with UBE2N; leading to inhibit UBE2N/Ubc13 activity (PubMed:22424771). Interacts with TRAF1 (PubMed:22424771). Interacts with TRAF2 (PubMed:22424771). Interacts with TRAF6 (PubMed:22424771). Interacts with PPARG (when in the liganded conformation) (PubMed:25519902). Interacts with (sumoylated) NR1H2; interaction with sumoylated NR1H2 and NR5A2 onto hepatic acute phase protein promoters prevents N-Cor corepressor complex dissociation (By similarity). Interacts with (sumoylated) NR5A2; interaction with sumoylated NR1H2 and NR5A2 onto hepatic acute phase protein promoters prevents N-Cor corepressor complex dissociation (By similarity). Interacts with NR1H3 (By similarity). Interacts with RFX4 (PubMed:18218630). Interacts with ANKRD26 (By similarity). {ECO:0000250|UniProtKB:Q13227, ECO:0000269|PubMed:18218630, ECO:0000269|PubMed:22424771, ECO:0000269|PubMed:25519902, ECO:0000269|PubMed:26070566}. +Q8VD04 GRAP1_MOUSE GRIP1-associated protein 1 (GRASP-1) (HCMV-interacting protein) [Cleaved into: GRASP-1 C-terminal chain (30kDa C-terminus form)] 806 92,715 Chain (2); Coiled coil (4); Erroneous initiation (1); Initiator methionine (1); Modified residue (10); Sequence conflict (4); Site (1) FUNCTION: Regulates the endosomal recycling back to the neuronal plasma membrane, possibly by connecting early and late recycling endosomal domains and promoting segregation of recycling endosomes from early endosomal membranes. Involved in the localization of recycling endosomes to dendritic spines, thereby playing a role in the maintenance of dendritic spine morphology. Required for the activity-induced AMPA receptor recycling to dendrite membranes and for long-term potentiation and synaptic plasticity (By similarity). {ECO:0000250|UniProtKB:Q9JHZ4}.; FUNCTION: GRASP-1 C-terminal chain: Functions as a scaffold protein to facilitate MAP3K1/MEKK1-mediated activation of the JNK1 kinase by phosphorylation, possibly by bringing MAP3K1/MEKK1 and JNK1 in close proximity (By similarity). {ECO:0000250|UniProtKB:Q4V328}. PTM: Proteolytically cleaved by caspase-3. A minor C-terminal proteolytic fragment of 30 kDa is produced. Proteolytic cleavage is required for JNK signaling activation. {ECO:0000250|UniProtKB:Q9JHZ4}. SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000250|UniProtKB:Q9JHZ4}; Peripheral membrane protein {ECO:0000305}. Recycling endosome membrane {ECO:0000250|UniProtKB:Q9JHZ4}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9JHZ4}. Cell projection, axon {ECO:0000250|UniProtKB:Q9JHZ4}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9JHZ4}. Cell junction, synapse {ECO:0000250|UniProtKB:Q9JHZ4}. Note=Localizes to recycling endosomal tubules that are emanating from early endosomes. {ECO:0000250|UniProtKB:Q9JHZ4}. SUBUNIT: Interacts with GRIP1, GRIP2 and AMPA receptors. Interacts (via C-terminus) with MAPK8/JNK1 and MAP3K1/MEKK1; the interaction promotes MAP3K1-mediated phosphorylation of MAPK8. Interacts (via N-terminus) with RAB4A (in GTP-bound form) (By similarity). Interacts (via C-terminus) with STX12 (PubMed:20098723). {ECO:0000250|UniProtKB:Q9JHZ4, ECO:0000269|PubMed:20098723}. TISSUE SPECIFICITY: Expressed in the central nervous system, including cortex, cerebellum, midbrain and spinal cord, and in primary cultured hippocampal neurons but absent in non-neuronal tissues and cell types with the exception of neuroendocrine insulinoma cells. {ECO:0000269|PubMed:20098723}. +Q9EPB7 GPR88_MOUSE Probable G-protein coupled receptor 88 (Striatum-specific G-protein coupled receptor) 384 40,240 Chain (1); Glycosylation (1); Topological domain (8); Transmembrane (7) TRANSMEM 36 56 Helical; Name=1. {ECO:0000255}.; TRANSMEM 74 94 Helical; Name=2. {ECO:0000255}.; TRANSMEM 117 136 Helical; Name=3. {ECO:0000255}.; TRANSMEM 159 179 Helical; Name=4. {ECO:0000255}.; TRANSMEM 196 216 Helical; Name=5. {ECO:0000255}.; TRANSMEM 286 306 Helical; Name=6. {ECO:0000255}.; TRANSMEM 311 331 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 35 Extracellular. {ECO:0000255}.; TOPO_DOM 57 73 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 95 116 Extracellular. {ECO:0000255}.; TOPO_DOM 137 158 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 180 195 Extracellular. {ECO:0000255}.; TOPO_DOM 217 285 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 307 310 Extracellular. {ECO:0000255}.; TOPO_DOM 332 384 Cytoplasmic. {ECO:0000255}. FUNCTION: Probable G-protein coupled receptor implicated in a large repertoire of behavioral responses that engage motor activities, spatial learning, and emotional processing. May play a role in the regulation of cognitive and motor function. {ECO:0000250|UniProtKB:Q9ESP4, ECO:0000269|PubMed:26188600}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9ESP4}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:Q9ESP4}. Nucleus {ECO:0000250|UniProtKB:Q9ESP4}. Note=During cortical lamination, subcellular location shifts, on the day of birth, from expression at the plasma membrane and in the cytoplasm to the nuclei of neurons. This intranuclear localization remains throughout adulthood. {ECO:0000250|UniProtKB:Q9ESP4}. TISSUE SPECIFICITY: Expressed predominantly in the striatum. {ECO:0000269|PubMed:11056049}. +Q3U1Z5 GPSM3_MOUSE G-protein-signaling modulator 3 159 17,619 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (3); Frameshift (1); Modified residue (5); Sequence conflict (1) FUNCTION: Interacts with subunit of G(i) alpha proteins and regulates the activation of G(i) alpha proteins. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. DOMAIN: The GoLoco 1 and/or GoLoco 3 domains exhibit GDI activity towards GDP-bound G(i) alpha protein, but not the GoLoco 2 domain. {ECO:0000250}. +Q91VK4 ITM2C_MOUSE Integral membrane protein 2C (Transmembrane protein BRI3) [Cleaved into: CT-BRI3] 269 30,482 Chain (1); Disulfide bond (1); Domain (1); Glycosylation (1); Modified residue (1); Peptide (1); Sequence conflict (2); Site (1); Transmembrane (1) TRANSMEM 57 77 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. FUNCTION: Negative regulator of amyloid-beta peptide production. May inhibit the processing of APP by blocking its access to alpha- and beta-secretase. Binding to the beta-secretase-cleaved APP C-terminal fragment is negligible, suggesting that ITM2C is a poor gamma-secretase cleavage inhibitor. May play a role in TNF-induced cell death and neuronal differentiation. {ECO:0000269|PubMed:14592447}. PTM: Type I membrane-bound, as well as soluble, furin has a pre-eminent role in ITM2C proteolytic processing. PCSK7 and PCSK5 may also be involved although to a lesser extent. The soluble form of PCSK7 is incapable of processing ITM2C. Fails to undergo shedding by ADAM10 and intramembanaire cleavage by SPPL2B (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:14592447}; Single-pass type II membrane protein {ECO:0000269|PubMed:14592447}. Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. SUBUNIT: Interacts with BACE1. Interacts with APP. Interacts with STMN2 (By similarity). {ECO:0000250}. +P24472 GSTA4_MOUSE Glutathione S-transferase A4 (EC 2.5.1.18) (GST A4-4) (GSTA4-4) (GST class-alpha member 4) (Glutathione S-transferase 5.7) (GST 5.7) 222 25,564 Beta strand (7); Binding site (1); Chain (1); Domain (2); Helix (12); Modified residue (1); Natural variant (3); Region (2); Sequence conflict (3); Turn (2) FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. {ECO:0000269|PubMed:10508391}. PTM: The N-terminus is blocked. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Homodimer. {ECO:0000269|PubMed:10508391}. +Q3UJK4 GTPB2_MOUSE GTP-binding protein 2 (GTP-binding-like protein 2) 602 65,754 Chain (1); Domain (1); Erroneous initiation (4); Nucleotide binding (3); Sequence conflict (3) TISSUE SPECIFICITY: Predominantly expressed in thymus, spleen, and testis. Expressed at lower levels in brain, heart, lung, kidney, and skeletal muscle. In testis, specifically expressed in spermatocytes and round spermatids. {ECO:0000269|PubMed:11054535}. +Q3UWA6 GUC2C_MOUSE Heat-stable enterotoxin receptor (STA receptor) (EC 4.6.1.2) (Guanylyl cyclase C) (GC-C) (Intestinal guanylate cyclase) 1072 123,232 Alternative sequence (1); Chain (1); Domain (2); Glycosylation (10); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 434 454 Helical. {ECO:0000255}. TOPO_DOM 20 433 Extracellular. {ECO:0000255}.; TOPO_DOM 455 1072 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for the E.coli heat-stable enterotoxin (E.coli enterotoxin markedly stimulates the accumulation of cGMP in mammalian cells expressing GC-C). Also activated by the endogenous peptide guanylin (By similarity). {ECO:0000250}. PTM: Glycosylation at Asn-75 and/or Asn-79 is required for interaction with VIP36 while glycosylation at Asn-345 and Asn-402 modulates ligand-mediated GC-C activation. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein. Note=The 145 kDa plasma membrane form of GC-C contains sialic acid and galactose residues, while a differencially glycosylated 130 Kda form is a high mannose form that is resident in the endoplasmic reticulum and may serve as the precursor for the cell surface form. {ECO:0000250}. SUBUNIT: Homotrimer. Interacts via its C-terminal region with PDZK2. Interacts with the lectin chaperone VIP36 (By similarity). {ECO:0000250}. DOMAIN: The protein kinase domain is predicted to be catalytically inactive. +Q6TL19 GUC2G_MOUSE Guanylate cyclase 2G (EC 4.6.1.2) (Guanylyl cyclase receptor G) (mGC-G) 1100 122,546 Chain (1); Domain (2); Glycosylation (9); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 482 502 Helical. {ECO:0000255}. TOPO_DOM 44 481 Extracellular. {ECO:0000255}.; TOPO_DOM 503 1100 Cytoplasmic. {ECO:0000255}. FUNCTION: Probably plays a specific functional role in the testis by binding to yet not identified ligand. {ECO:0000269|PubMed:14713286}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Homodimer or heterodimer with NPR1. {ECO:0000269|PubMed:14713286}. TISSUE SPECIFICITY: Testis specific. {ECO:0000269|PubMed:14713286}. +Q810K9 GXLT2_MOUSE Glucoside xylosyltransferase 2 (EC 2.4.2.42) (Glycosyltransferase 8 domain-containing protein 4) 444 51,479 Chain (1); Compositional bias (1); Glycosylation (1); Topological domain (2); Transmembrane (1) TRANSMEM 5 25 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 4 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 26 444 Lumenal. {ECO:0000255}. FUNCTION: Glycosyltransferase which elongates the O-linked glucose attached to EGF-like repeats in the extracellular domain of Notch proteins by catalyzing the addition of xylose. {ECO:0000250|UniProtKB:A0PJZ3}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. +Q9Z1E4 GYS1_MOUSE Glycogen [starch] synthase, muscle (EC 2.4.1.11) 738 83,927 Binding site (1); Chain (1); Modified residue (16); Sequence conflict (12) Glycan biosynthesis; glycogen biosynthesis. FUNCTION: Transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan. {ECO:0000250}. PTM: Primed phosphorylation at Ser-657 (site 5) by CSNK2A1 and CSNK2A2 is required for inhibitory phosphorylation at Ser-641 (site 3a), Ser-645 (site 3b), Ser-649 (site 3c) and Ser-653 (site 4) by GSK3A an GSK3B. Phosphorylated at Ser-641 by PASK, leading to inactivation; phosphorylation by PASK is inhibited by glycogen. Phosphorylated at Ser-641 by DYRK2, leading to inactivation. Dephosphorylation at Ser-641 and Ser-645 by PP1 activates the enzyme (By similarity). Phosphorylation at Ser-8 by AMPK inactivates the enzyme activity. {ECO:0000250, ECO:0000269|PubMed:15561936}. SUBUNIT: Interacts with GYG1. {ECO:0000250}. +Q8VCB3 GYS2_MOUSE Glycogen [starch] synthase, liver (EC 2.4.1.11) 704 80,871 Binding site (1); Chain (1); Modified residue (9); Mutagenesis (8); Sequence conflict (2) Glycan biosynthesis; glycogen biosynthesis. FUNCTION: Transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan. PTM: Primed phosphorylation at Ser-657 (site 5) by CSNK2A1 and CSNK2A2 is required for inhibitory phosphorylation at Ser-641 (site 3a), Ser-645 (site 3b), Ser-649 (site 3c) and Ser-653 (site 4) by GSK3A an GSK3B (By similarity). Dephosphorylation at Ser-641 and Ser-645 by PP1 activates the enzyme (By similarity). Phosphorylation at Ser-8 is not required for interaction with GYG1 (PubMed:24982189). Interaction with GYG1 does not regulate the phosphorylation at Ser-8 and Ser-641 (PubMed:24982189). {ECO:0000250|UniProtKB:P13807, ECO:0000250|UniProtKB:P13834, ECO:0000269|PubMed:24982189}. SUBUNIT: Interacts with GYG1 (via C-terminus); required for GYS2-mediated glycogen synthesis. {ECO:0000269|PubMed:24982189}. +P43275 H11_MOUSE Histone H1.1 (H1 VAR.3) (Histone H1a) (H1a) 213 21,785 Chain (1); Domain (1); Initiator methionine (1); Modified residue (18) FUNCTION: Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity). {ECO:0000250}. PTM: H1 histones are progressively phosphorylated during the cell cycle, becoming maximally phosphorylated during late G2 phase and M phase, and being dephosphorylated sharply thereafter. {ECO:0000269|PubMed:8639656}.; PTM: Citrullination at Arg-56 (H1R54ci) by PADI4 takes place within the DNA-binding site of H1 and results in its displacement from chromatin and global chromatin decondensation, thereby promoting pluripotency and stem cell maintenance. {ECO:0000269|PubMed:24463520}.; PTM: Hydroxybutyrylation of histones is induced by starvation. {ECO:0000250|UniProtKB:P43277}. SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Mainly localizes in euchromatin. {ECO:0000250}. SUBUNIT: Interacts with DFFB. {ECO:0000250}. DOMAIN: The C-terminal domain is required for high-affinity binding to chromatin. {ECO:0000250}. TISSUE SPECIFICITY: Restricted to thymus, testis and spleen. Present also in lymphocytic and neuronal cells. Increases in testis starting with a low level at day 5 and reaching high concentrations in 20-day old and adult animals. {ECO:0000269|PubMed:9655912}. +P10922 H10_MOUSE Histone H1.0 (Histone H1') (Histone H1(0)) (MyD196) [Cleaved into: Histone H1.0, N-terminally processed] 194 20,861 Chain (2); Domain (1); Initiator methionine (1); Modified residue (4); Sequence conflict (2) FUNCTION: Histones H1 are necessary for the condensation of nucleosome chains into higher-order structures. The H1F0 histones are found in cells that are in terminal stages of differentiation or that have low rates of cell division. PTM: ADP-ribosylated on Ser-104 in response to DNA damage. {ECO:0000250|UniProtKB:P07305}. SUBCELLULAR LOCATION: Nucleus. Chromosome. +C0HKE3 H2A1D_MOUSE Histone H2A type 1-D 130 14,135 Chain (1); Cross-link (3); Initiator methionine (1); Modified residue (24) FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. PTM: Deiminated on Arg-4 in granulocytes upon calcium entry. {ECO:0000250|UniProtKB:P0C0S8}.; PTM: Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM27 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is involved in the initiation of both imprinted and random X inactivation. Ubiquitinated H2A is enriched in inactive X chromosome chromatin. Ubiquitination of H2A functions downstream of methylation of 'Lys-27' of histone H3 (H3K27me). H2AK119Ub by RNF2/RING2 can also be induced by ultraviolet and may be involved in DNA repair. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties by the E2 ligase UBE2N and the E3 ligases RNF8 and RNF168, leading to the recruitment of repair proteins to sites of DNA damage. Ubiquitination at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) in response to DNA damage is initiated by RNF168 that mediates monoubiquitination at these 2 sites, and 'Lys-63'-linked ubiquitin are then conjugated to monoubiquitin; RNF8 is able to extend 'Lys-63'-linked ubiquitin chains in vitro. Deubiquitinated by USP51 at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) after damaged DNA is repaired (By similarity). H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination (H2AK13Ub and H2AK15Ub) are distinct events. {ECO:0000250|UniProtKB:P0C0S8, ECO:0000269|PubMed:15509584, ECO:0000269|PubMed:15525528, ECO:0000269|PubMed:24352239}.; PTM: Phosphorylation on Ser-2 (H2AS1ph) is enhanced during mitosis. Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses transcription. Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1. Phosphorylation at Thr-121 (H2AT120ph) by DCAF1 is present in the regulatory region of many tumor suppresor genes and down-regulates their transcription. {ECO:0000250|UniProtKB:P0C0S8, ECO:0000269|PubMed:7217105}.; PTM: Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage. {ECO:0000269|PubMed:16699504}.; PTM: Glutamine methylation at Gln-105 (H2AQ104me) by FBL is specifically dedicated to polymerase I. It is present at 35S ribosomal DNA locus and impairs binding of the FACT complex. {ECO:0000269|PubMed:24352239}.; PTM: Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes. {ECO:0000269|PubMed:21925322}.; PTM: Hydroxybutyrylation of histones is induced by starvation. {ECO:0000269|PubMed:27105115}. SUBCELLULAR LOCATION: Nucleus. Chromosome. SUBUNIT: The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. +C0HKE5 H2A1G_MOUSE Histone H2A type 1-G 130 14,135 Chain (1); Cross-link (3); Initiator methionine (1); Modified residue (24) FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. PTM: Deiminated on Arg-4 in granulocytes upon calcium entry. {ECO:0000250|UniProtKB:P0C0S8}.; PTM: Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM27 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is involved in the initiation of both imprinted and random X inactivation. Ubiquitinated H2A is enriched in inactive X chromosome chromatin. Ubiquitination of H2A functions downstream of methylation of 'Lys-27' of histone H3 (H3K27me). H2AK119Ub by RNF2/RING2 can also be induced by ultraviolet and may be involved in DNA repair. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties by the E2 ligase UBE2N and the E3 ligases RNF8 and RNF168, leading to the recruitment of repair proteins to sites of DNA damage. Ubiquitination at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) in response to DNA damage is initiated by RNF168 that mediates monoubiquitination at these 2 sites, and 'Lys-63'-linked ubiquitin are then conjugated to monoubiquitin; RNF8 is able to extend 'Lys-63'-linked ubiquitin chains in vitro. Deubiquitinated by USP51 at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) after damaged DNA is repaired (By similarity). H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination (H2AK13Ub and H2AK15Ub) are distinct events. {ECO:0000250|UniProtKB:P0C0S8, ECO:0000269|PubMed:15509584, ECO:0000269|PubMed:15525528, ECO:0000269|PubMed:24352239}.; PTM: Phosphorylation on Ser-2 (H2AS1ph) is enhanced during mitosis. Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses transcription. Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1. Phosphorylation at Thr-121 (H2AT120ph) by DCAF1 is present in the regulatory region of many tumor suppresor genes and down-regulates their transcription. {ECO:0000250|UniProtKB:P0C0S8, ECO:0000269|PubMed:7217105}.; PTM: Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage. {ECO:0000269|PubMed:16699504}.; PTM: Glutamine methylation at Gln-105 (H2AQ104me) by FBL is specifically dedicated to polymerase I. It is present at 35S ribosomal DNA locus and impairs binding of the FACT complex. {ECO:0000269|PubMed:24352239}.; PTM: Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes. {ECO:0000269|PubMed:21925322}.; PTM: Hydroxybutyrylation of histones is induced by starvation. {ECO:0000269|PubMed:27105115}. SUBCELLULAR LOCATION: Nucleus. Chromosome. SUBUNIT: The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. +Q6GSS7 H2A2A_MOUSE Histone H2A type 2-A (H2a-614) (H2a-615) (Histone H2A.2) 130 14,095 Chain (1); Cross-link (3); Initiator methionine (1); Modified residue (24) FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. PTM: Deiminated on Arg-4 in granulocytes upon calcium entry. {ECO:0000250|UniProtKB:P0C0S8}.; PTM: Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM27 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is involved in the initiation of both imprinted and random X inactivation. Ubiquitinated H2A is enriched in inactive X chromosome chromatin. Ubiquitination of H2A functions downstream of methylation of 'Lys-27' of histone H3 (H3K27me). H2AK119Ub by RNF2/RING2 can also be induced by ultraviolet and may be involved in DNA repair. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties by the E2 ligase UBE2N and the E3 ligases RNF8 and RNF168, leading to the recruitment of repair proteins to sites of DNA damage. Ubiquitination at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) in response to DNA damage is initiated by RNF168 that mediates monoubiquitination at these 2 sites, and 'Lys-63'-linked ubiquitin are then conjugated to monoubiquitin; RNF8 is able to extend 'Lys-63'-linked ubiquitin chains in vitro. H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination (H2AK13Ub and H2AK15Ub) are distinct events. {ECO:0000250|UniProtKB:P0C0S8, ECO:0000269|PubMed:15509584, ECO:0000269|PubMed:15525528, ECO:0000269|PubMed:24352239}.; PTM: Phosphorylation on Ser-2 (H2AS1ph) is enhanced during mitosis. Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses transcription. Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1. Phosphorylation at Thr-121 (H2AT120ph) by DCAF1 is present in the regulatory region of many tumor suppresor genes and down-regulates their transcription. {ECO:0000250|UniProtKB:P0C0S8}.; PTM: Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage. {ECO:0000269|PubMed:16699504}.; PTM: Glutamine methylation at Gln-105 (H2AQ104me) by FBL is specifically dedicated to polymerase I. It is present at 35S ribosomal DNA locus and impairs binding of the FACT complex. {ECO:0000269|PubMed:24352239}.; PTM: Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes. {ECO:0000269|PubMed:21925322}.; PTM: Hydroxybutyrylation of histones is induced by starvation. {ECO:0000269|PubMed:27105115}. SUBCELLULAR LOCATION: Nucleus. Chromosome. SUBUNIT: The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. +Q8CGP7 H2A1K_MOUSE Histone H2A type 1-K 130 14,150 Chain (1); Cross-link (3); Initiator methionine (1); Modified residue (25) FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. PTM: Deiminated on Arg-4 in granulocytes upon calcium entry. {ECO:0000250|UniProtKB:P0C0S8}.; PTM: Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM27 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is involved in the initiation of both imprinted and random X inactivation. Ubiquitinated H2A is enriched in inactive X chromosome chromatin. Ubiquitination of H2A functions downstream of methylation of 'Lys-27' of histone H3 (H3K27me). H2AK119Ub by RNF2/RING2 can also be induced by ultraviolet and may be involved in DNA repair. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties by the E2 ligase UBE2N and the E3 ligases RNF8 and RNF168, leading to the recruitment of repair proteins to sites of DNA damage. Ubiquitination at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) in response to DNA damage is initiated by RNF168 that mediates monoubiquitination at these 2 sites, and 'Lys-63'-linked ubiquitin are then conjugated to monoubiquitin; RNF8 is able to extend 'Lys-63'-linked ubiquitin chains in vitro. Deubiquitinated by USP51 at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) after damaged DNA is repaired (By similarity). H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination (H2AK13Ub and H2AK15Ub) are distinct events. {ECO:0000250|UniProtKB:P0C0S8, ECO:0000269|PubMed:15509584, ECO:0000269|PubMed:15525528, ECO:0000269|PubMed:24352239}.; PTM: Phosphorylation on Ser-2 (H2AS1ph) is enhanced during mitosis. Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses transcription. Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1. Phosphorylation at Thr-121 (H2AT120ph) by DCAF1 is present in the regulatory region of many tumor suppresor genes and down-regulates their transcription. {ECO:0000250|UniProtKB:P0C0S8}.; PTM: Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage. {ECO:0000269|PubMed:16699504}.; PTM: Glutamine methylation at Gln-105 (H2AQ104me) by FBL is specifically dedicated to polymerase I. It is present at 35S ribosomal DNA locus and impairs binding of the FACT complex. {ECO:0000269|PubMed:24352239}.; PTM: Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes. {ECO:0000269|PubMed:21925322}.; PTM: Hydroxybutyrylation of histones is induced by starvation. {ECO:0000269|PubMed:27105115}. SUBCELLULAR LOCATION: Nucleus. Chromosome. SUBUNIT: The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. +C0HKE7 H2A1N_MOUSE Histone H2A type 1-N 130 14,135 Chain (1); Cross-link (3); Initiator methionine (1); Modified residue (24) FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. PTM: Deiminated on Arg-4 in granulocytes upon calcium entry. {ECO:0000250|UniProtKB:P0C0S8}.; PTM: Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM27 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is involved in the initiation of both imprinted and random X inactivation. Ubiquitinated H2A is enriched in inactive X chromosome chromatin. Ubiquitination of H2A functions downstream of methylation of 'Lys-27' of histone H3 (H3K27me). H2AK119Ub by RNF2/RING2 can also be induced by ultraviolet and may be involved in DNA repair. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties by the E2 ligase UBE2N and the E3 ligases RNF8 and RNF168, leading to the recruitment of repair proteins to sites of DNA damage. Ubiquitination at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) in response to DNA damage is initiated by RNF168 that mediates monoubiquitination at these 2 sites, and 'Lys-63'-linked ubiquitin are then conjugated to monoubiquitin; RNF8 is able to extend 'Lys-63'-linked ubiquitin chains in vitro. Deubiquitinated by USP51 at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) after damaged DNA is repaired (By similarity). H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination (H2AK13Ub and H2AK15Ub) are distinct events. {ECO:0000250|UniProtKB:P0C0S8, ECO:0000269|PubMed:15509584, ECO:0000269|PubMed:15525528, ECO:0000269|PubMed:24352239}.; PTM: Phosphorylation on Ser-2 (H2AS1ph) is enhanced during mitosis. Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses transcription. Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1. Phosphorylation at Thr-121 (H2AT120ph) by DCAF1 is present in the regulatory region of many tumor suppresor genes and down-regulates their transcription. {ECO:0000250|UniProtKB:P0C0S8, ECO:0000269|PubMed:7217105}.; PTM: Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage. {ECO:0000269|PubMed:16699504}.; PTM: Glutamine methylation at Gln-105 (H2AQ104me) by FBL is specifically dedicated to polymerase I. It is present at 35S ribosomal DNA locus and impairs binding of the FACT complex. {ECO:0000269|PubMed:24352239}.; PTM: Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes. {ECO:0000269|PubMed:21925322}.; PTM: Hydroxybutyrylation of histones is induced by starvation. {ECO:0000269|PubMed:27105115}. SUBCELLULAR LOCATION: Nucleus. Chromosome. SUBUNIT: The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. +P27661 H2AX_MOUSE Histone H2AX (H2a/x) (Histone H2A.X) 143 15,143 Chain (1); Cross-link (5); Initiator methionine (1); Modified residue (10); Motif (1); Mutagenesis (9) FUNCTION: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Required for checkpoint-mediated arrest of cell cycle progression in response to low doses of ionizing radiation and for efficient repair of DNA double strand breaks (DSBs) specifically when modified by C-terminal phosphorylation. {ECO:0000269|PubMed:11740565, ECO:0000269|PubMed:11934988, ECO:0000269|PubMed:12034884, ECO:0000269|PubMed:12447390, ECO:0000269|PubMed:12660252, ECO:0000269|PubMed:12689589, ECO:0000269|PubMed:12792649, ECO:0000269|PubMed:12914700, ECO:0000269|PubMed:12914701, ECO:0000269|PubMed:14530383, ECO:0000269|PubMed:15574327, ECO:0000269|PubMed:15580272, ECO:0000269|PubMed:15589157, ECO:0000269|PubMed:15610743, ECO:0000269|PubMed:15632067}. PTM: Phosphorylated on Ser-140 (to form gamma-H2AX or H2AX139ph) in response to DNA double strand breaks (DSBs) generated by exogenous genotoxic agents, by stalled replication forks, by meiotic recombination events and during immunoglobulin class switching in lymphocytes. Phosphorylation can extend up to several thousand nucleosomes from the actual site of the DSB and may mark the surrounding chromatin for recruitment of proteins required for DNA damage signaling and repair. Widespread phosphorylation may also serve to amplify the damage signal or aid repair of persistent lesions. Phosphorylation of Ser-140 (H2AX139ph) in response to ionizing radiation is mediated by both ATM and PRKDC while defects in DNA replication induce Ser-140 phosphorylation (H2AX139ph) subsequent to activation of ATR and PRKDC. Dephosphorylation of Ser-140 by PP2A is required for DNA DSB repair. In meiosis, Ser-140 phosphorylation (H2AX139ph) first occurs at synaptonemal complexes during leptotene and is an ATM-dependent response to the formation of programmed DSBs by SPO11. Ser-140 phosphorylation (H2AX139ph) subsequently occurs at unsynapsed regions of both autosomes and the XY bivalent during zygotene and is ATR- and BRCA1-dependent. Ser-140 phosphorylation (H2AX139ph) may also be required for transcriptional repression of unsynapsed chromatin and meiotic sex chromosome inactivation (MSCI), whereby the X and Y chromosomes condense in pachytene to form the heterochromatic XY-body. During immunoglobulin class switch recombination in lymphocytes, Ser-140 phosphorylation (H2AX139ph) at sites of DNA-recombination requires the activation-induced cytidine deaminase AICDA. Phosphorylation at Tyr-143 (H2AXY142ph) by BAZ1B/WSTF determines the relative recruitment of either DNA repair or pro-apoptotic factors. Phosphorylation at Tyr-143 (H2AXY142ph) favors the recruitment of APBB1/FE65 and pro-apoptosis factors such as MAPK8/JNK1, triggering apoptosis. In contrast, dephosphorylation of Tyr-143 by EYA proteins (EYA1, EYA2, EYA3 or EYA4) favors the recruitment of MDC1-containing DNA repair complexes to the tail of phosphorylated Ser-140 (H2AX139ph). {ECO:0000269|PubMed:11242108, ECO:0000269|PubMed:11571274, ECO:0000269|PubMed:11740565, ECO:0000269|PubMed:12447390, ECO:0000269|PubMed:12660252, ECO:0000269|PubMed:14530383, ECO:0000269|PubMed:15059890, ECO:0000269|PubMed:15580272, ECO:0000269|PubMed:19092802, ECO:0000269|PubMed:7217105, ECO:0000269|PubMed:9488723}.; PTM: Monoubiquitination of Lys-120 (H2AXK119ub) by RING1 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties by the E2 ligase UBE2N and the E3 ligases RNF8 and RNF168, leading to the recruitment of repair proteins to sites of DNA damage. Ubiquitination at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) in response to DNA damage is initiated by RNF168 that mediates monoubiquitination at these 2 sites, and 'Lys-63'-linked ubiquitin are then conjugated to monoubiquitin; RNF8 is able to extend 'Lys-63'-linked ubiquitin chains in vitro. H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination (H2AK13Ub and H2AK15Ub) are distinct events (By similarity). {ECO:0000250}.; PTM: Acetylation at Lys-37 increases in S and G2 phases. This modification has been proposed to be important for DNA double-strand break repair (PubMed:20488183). {ECO:0000269|PubMed:20488183, ECO:0000269|PubMed:7217105}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11242108, ECO:0000269|PubMed:11571274, ECO:0000269|PubMed:11740565, ECO:0000269|PubMed:12034884, ECO:0000269|PubMed:12447390, ECO:0000269|PubMed:15589157}. Chromosome {ECO:0000269|PubMed:11242108, ECO:0000269|PubMed:11571274, ECO:0000269|PubMed:12034884, ECO:0000269|PubMed:15059890, ECO:0000269|PubMed:15589157, ECO:0000269|PubMed:23039116}. SUBUNIT: The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. Interacts with numerous proteins required for DNA damage signaling and repair when phosphorylated on Ser-140. These include MDC1, TP53BP1, BRCA1 and the MRN complex, composed of MRE11, RAD50, and NBN. Interaction with the MRN complex is mediated at least in part by NBN. Also interacts with DHX9/NDHII when phosphorylated on Ser-140 and MCPH1 when phosphorylated at Ser-140 or Tyr-143. Interacts with ARRB2; the interaction is detected in the nucleus upon OR1D2 stimulation. Interacts with WRAP53/TCAB1. {ECO:0000250|UniProtKB:P16104}. DOMAIN: The [ST]-Q motif constitutes a recognition sequence for kinases from the PI3/PI4-kinase family. TISSUE SPECIFICITY: Most abundant in testis, thymus and spleen. {ECO:0000269|PubMed:11242108}. +P0C0S6 H2AZ_MOUSE Histone H2A.Z (H2A/z) 128 13,553 Chain (1); Cross-link (1); Initiator methionine (1); Modified residue (6); Region (4); Sequence conflict (2) FUNCTION: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. May be involved in the formation of constitutive heterochromatin. May be required for chromosome segregation during cell division. Essential for early development. {ECO:0000269|PubMed:11516949, ECO:0000269|PubMed:15195148, ECO:0000269|PubMed:15546624}. PTM: Monoubiquitination of Lys-122 gives a specific tag for epigenetic transcriptional repression. {ECO:0000250|UniProtKB:P0C0S5}.; PTM: Acetylated on Lys-5, Lys-8 and Lys-12 during interphase. Acetylation disappears at mitosis. {ECO:0000269|PubMed:16204459, ECO:0000269|PubMed:7217105}.; PTM: Not phosphorylated. {ECO:0000269|PubMed:7217105}.; PTM: Monomethylated on Lys-5 and Lys-8 by SETD6. SETD6 predominantly methylates Lys-8, lys-5 being a possible secondary site. {ECO:0000250|UniProtKB:P0C0S5}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12660166}. Chromosome {ECO:0000269|PubMed:12660166, ECO:0000269|PubMed:15195148}. Note=Enriched in constitutive heterochromatin (PubMed:12660166, PubMed:15195148). Absent from facultative heterochromatin of the inactive X chromosome (PubMed:12660166). {ECO:0000269|PubMed:12660166, ECO:0000269|PubMed:15195148}. SUBUNIT: Interacts (via M6 cassette) with ANP32E; leading to removal of H2A.Z/H2AFZ from the nucleosome (By similarity). The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. H2A or its variant H2AFZ forms a heterodimer with H2B (By similarity). H2AFZ interacts with INCENP (PubMed:12660166). Interacts with VPS72 (via N-terminal domain). Interacts with PWWP2A (By similarity). {ECO:0000250|UniProtKB:P0C0S5, ECO:0000269|PubMed:12660166}. +Q64478 H2B1H_MOUSE Histone H2B type 1-H (h2B-221) 126 13,920 Chain (1); Cross-link (4); Glycosylation (1); Initiator methionine (1); Modified residue (52); Sequence conflict (1) FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. PTM: Monoubiquitination at Lys-35 (H2BK34Ub) by the MSL1/MSL2 dimer is required for histone H3 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) methylation and transcription activation at specific gene loci, such as HOXA9 and MEIS1 loci. Similarly, monoubiquitination at Lys-121 (H2BK120Ub) by the RNF20/40 complex gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation. It also functions cooperatively with the FACT dimer to stimulate elongation by RNA polymerase II. H2BK120Ub also acts as a regulator of mRNA splicing: deubiquitination by USP49 is required for efficient cotranscriptional splicing of a large set of exons (By similarity). {ECO:0000250|UniProtKB:P33778}.; PTM: Phosphorylated on Ser-15 (H2BS14ph) by STK4/MST1 during apoptosis; which facilitates apoptotic chromatin condensation. Also phosphorylated on Ser-15 in response to DNA double strand breaks (DSBs), and in correlation with somatic hypermutation and immunoglobulin class-switch recombination. Phosphorylation at Ser-37 (H2BS36ph) by AMPK in response to stress promotes transcription. {ECO:0000269|PubMed:15197225, ECO:0000269|PubMed:16039583, ECO:0000269|PubMed:20647423}.; PTM: GlcNAcylation at Ser-113 promotes monoubiquitination of Lys-121. It fluctuates in response to extracellular glucose, and associates with transcribed genes (By similarity). {ECO:0000250|UniProtKB:P62807}.; PTM: Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes. {ECO:0000269|PubMed:21925322}.; PTM: Hydroxybutyrylation of histones is induced by starvation. {ECO:0000269|PubMed:27105115}. SUBCELLULAR LOCATION: Nucleus. Chromosome. SUBUNIT: The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. +Q9D2U9 H2B3A_MOUSE Histone H2B type 3-A 126 13,994 Beta strand (1); Chain (1); Cross-link (3); Helix (4); Initiator methionine (1); Modified residue (47) FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. PTM: Monoubiquitination at Lys-35 (H2BK34Ub) by the MSL1/MSL2 dimer is required for histone H3 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) methylation and transcription activation at specific gene loci, such as HOXA9 and MEIS1 loci. Similarly, monoubiquitination at Lys-121 (H2BK120Ub) by the RNF20/40 complex gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation. It also functions cooperatively with the FACT dimer to stimulate elongation by RNA polymerase II. H2BK120Ub also acts as a regulator of mRNA splicing: deubiquitination by USP49 is required for efficient cotranscriptional splicing of a large set of exons (By similarity). {ECO:0000250|UniProtKB:P33778}.; PTM: Phosphorylated on Ser-15 (H2BS14ph) by STK4/MST1 during apoptosis; which facilitates apoptotic chromatin condensation. Also phosphorylated on Ser-15 in response to DNA double strand breaks (DSBs), and in correlation with somatic hypermutation and immunoglobulin class-switch recombination. Phosphorylation at Ser-37 (H2BS36ph) by AMPK in response to stress promotes transcription. {ECO:0000269|PubMed:15197225, ECO:0000269|PubMed:16039583, ECO:0000269|PubMed:20647423}.; PTM: Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes. {ECO:0000269|PubMed:21925322}.; PTM: Hydroxybutyrylation of histones is induced by starvation. {ECO:0000269|PubMed:27105115}. SUBCELLULAR LOCATION: Nucleus. Chromosome. SUBUNIT: The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. {ECO:0000269|PubMed:16107708}. +Q9D9Z7 H2BV_MOUSE Histone H2B subacrosomal variant 123 14,197 Chain (1) FUNCTION: May act as an acrosome-nuclear docking protein in sperm. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Subacrosomal region. Does not localize in nucleus (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Present in testis (at protein level). {ECO:0000269|PubMed:11784042}. +P68433 H31_MOUSE Histone H3.1 136 15,404 Beta strand (3); Chain (1); Helix (4); Modified residue (91) FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. PTM: Acetylation is generally linked to gene activation. Acetylation on Lys-10 (H3K9ac) impairs methylation at Arg-9 (H3R8me2s). Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac) favors methylation at Arg-18 (H3R17me). Acetylation at Lys-123 (H3K122ac) by EP300/p300 plays a central role in chromatin structure: localizes at the surface of the histone octamer and stimulates transcription, possibly by promoting nucleosome instability. {ECO:0000269|PubMed:11747826, ECO:0000269|PubMed:11751582, ECO:0000269|PubMed:12498683, ECO:0000269|PubMed:13678296, ECO:0000269|PubMed:15485929, ECO:0000269|PubMed:15616592, ECO:0000269|PubMed:17194708}.; PTM: Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by PADI4 impairs methylation and represses transcription. {ECO:0000269|PubMed:11747826, ECO:0000269|PubMed:11751582, ECO:0000269|PubMed:12498683, ECO:0000269|PubMed:15339660, ECO:0000269|PubMed:15485929, ECO:0000269|PubMed:15616592}.; PTM: Asymmetric dimethylation at Arg-18 (H3R17me2a) by CARM1 is linked to gene activation. Symmetric dimethylation at Arg-9 (H3R8me2s) by PRMT5 is linked to gene repression. Asymmetric dimethylation at Arg-3 (H3R2me2a) by PRMT6 is linked to gene repression and is mutually exclusive with H3 Lys-5 methylation (H3K4me2 and H3K4me3). H3R2me2a is present at the 3' of genes regardless of their transcription state and is enriched on inactive promoters, while it is absent on active promoters (By similarity). {ECO:0000250|UniProtKB:P68431}.; PTM: Methylation at Lys-5 (H3K4me), Lys-37 (H3K36me) and Lys-80 (H3K79me) are linked to gene activation. Methylation at Lys-5 (H3K4me) facilitates subsequent acetylation of H3 and H4. Methylation at Lys-80 (H3K79me) is associated with DNA double-strand break (DSB) responses and is a specific target for TP53BP1. Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are linked to gene repression. Methylation at Lys-10 (H3K9me) is a specific target for HP1 proteins (CBX1, CBX3 and CBX5) and prevents subsequent phosphorylation at Ser-11 (H3S10ph) and acetylation of H3 and H4. Methylation at Lys-5 (H3K4me) and Lys-80 (H3K79me) require preliminary monoubiquitination of H2B at 'Lys-120'. Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are enriched in inactive X chromosome chromatin. Monomethylation at Lys-57 (H3K56me1) by EHMT2/G9A in G1 phase promotes interaction with PCNA and is required for DNA replication. {ECO:0000269|PubMed:10464286, ECO:0000269|PubMed:11747826, ECO:0000269|PubMed:11856369, ECO:0000269|PubMed:13678296, ECO:0000269|PubMed:15485929, ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:15735677, ECO:0000269|PubMed:15870105, ECO:0000269|PubMed:17189264, ECO:0000269|PubMed:17194708}.; PTM: Phosphorylated at Thr-4 (H3T3ph) by HASPIN during prophase and dephosphorylated during anaphase. Phosphorylation at Ser-11 (H3S10ph) by AURKB is crucial for chromosome condensation and cell-cycle progression during mitosis and meiosis. In addition phosphorylation at Ser-11 (H3S10ph) by RPS6KA4 and RPS6KA5 is important during interphase because it enables the transcription of genes following external stimulation, like mitogens, stress, growth factors or UV irradiation and result in the activation of genes, such as c-fos and c-jun. Phosphorylation at Ser-11 (H3S10ph), which is linked to gene activation, prevents methylation at Lys-10 (H3K9me) but facilitates acetylation of H3 and H4. Phosphorylation at Ser-11 (H3S10ph) by AURKB mediates the dissociation of HP1 proteins (CBX1, CBX3 and CBX5) from heterochromatin. Phosphorylation at Ser-11 (H3S10ph) is also an essential regulatory mechanism for neoplastic cell transformation. Phosphorylated at Ser-29 (H3S28ph) by MAP3K20 isoform 1, RPS6KA5 or AURKB during mitosis or upon ultraviolet B irradiation. Phosphorylation at Thr-7 (H3T6ph) by PRKCB is a specific tag for epigenetic transcriptional activation that prevents demethylation of Lys-5 (H3K4me) by LSD1/KDM1A. At centromeres, specifically phosphorylated at Thr-12 (H3T11ph) from prophase to early anaphase, by DAPK3 and PKN1. Phosphorylation at Thr-12 (H3T11ph) by PKN1 is a specific tag for epigenetic transcriptional activation that promotes demethylation of Lys-10 (H3K9me) by KDM4C/JMJD2C. Phosphorylation at Thr-12 (H3T11ph) by chromatin-associated CHEK1 regulates the transcription of cell cycle regulatory genes by modulating acetylation of Lys-10 (H3K9ac). Phosphorylation at Tyr-42 (H3Y41ph) by JAK2 promotes exclusion of CBX5 (HP1 alpha) from chromatin. {ECO:0000269|PubMed:10464286, ECO:0000269|PubMed:11441012, ECO:0000269|PubMed:11747826, ECO:0000269|PubMed:11856369, ECO:0000269|PubMed:13678296, ECO:0000269|PubMed:15485929, ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:15684425, ECO:0000269|PubMed:15735677, ECO:0000269|PubMed:15870105, ECO:0000269|PubMed:17194708, ECO:0000269|PubMed:18243098}.; PTM: Ubiquitinated by the CUL4-DDB-RBX1 complex in response to ultraviolet irradiation. This may weaken the interaction between histones and DNA and facilitate DNA accessibility to repair proteins (By similarity). Monoubiquitinated by RAG1 in lymphoid cells, monoubiquitination is required for V(D)J recombination. {ECO:0000250, ECO:0000269|PubMed:20122409}.; PTM: Lysine deamination at Lys-5 (H3K4all) to form allysine is mediated by LOXL2. Allysine formation by LOXL2 only takes place on H3K4me3 and results in gene repression (By similarity). {ECO:0000250|UniProtKB:P68431}.; PTM: Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes. {ECO:0000269|PubMed:21925322}.; PTM: Butyrylation of histones marks active promoters and competes with histone acetylation. It is present during late spermatogenesis. {ECO:0000269|PubMed:27105113}.; PTM: Hydroxybutyrylation of histones is induced by starvation. It is linked to gene activation and may replace histone acetylation on the promoter of specific genes in response to fasting. {ECO:0000269|PubMed:27105115}.; PTM: Succinylation at Lys-80 (H3K79succ) by KAT2A takes place with a maximum frequency around the transcription start sites of genes. It gives a specific tag for epigenetic transcription activation. {ECO:0000250|UniProtKB:P68431}.; PTM: Serine ADP-ribosylation constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage. Serine ADP-ribosylation at Ser-11 (H3S10ADPr) is mutually exclusive with phosphorylation at Ser-11 (H3S10ph) and impairs acetylation at Lys-10 (H3K9ac). {ECO:0000250|UniProtKB:P68431}. SUBCELLULAR LOCATION: Nucleus. Chromosome. SUBUNIT: The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. +Q64279 HAND1_MOUSE Heart- and neural crest derivatives-expressed protein 1 (Extraembryonic tissues, heart, autonomic nervous system and neural crest derivatives-expressed protein 1) (eHAND) (Helix-loop-helix transcription factor expressed in extraembryonic mesoderm and trophoblast) (Thing-1) (Th1) 216 23,806 Chain (1); Compositional bias (2); Domain (1); Modified residue (2); Mutagenesis (4); Sequence conflict (7) FUNCTION: Transcription factor that plays an essential role in both trophoblast-giant cells differentiation and in cardiac morphogenesis. In the adult, could be required for ongoing expression of cardiac-specific genes. Binds the DNA sequence 5'-NRTCTG-3' (non-canonical E-box). {ECO:0000269|PubMed:9500551}. PTM: Phosphorylation by PLK4 disrupts the interaction with MDFIC and leads to translocation into the nucleoplasm, allowing dimerization and transcription factor activity. {ECO:0000269|PubMed:17891141}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:17891141}. Nucleus, nucleolus {ECO:0000269|PubMed:17891141}. Note=Interaction with MDFIC sequesters it into the nucleolus, preventing the transcription factor activity. Phosphorylation by PLK4 disrupts the interaction with MDFIC and releases it from the nucleolus, leading to transcription factor activity. SUBUNIT: Efficient DNA binding requires dimerization with another bHLH protein. Forms homodimers and heterodimers with TCF3 gene products E12 and E47, HAND2 and HEY1, HEY2 and HEYL (hairy-related transcription factors). Interacts with MDFIC. {ECO:0000269|PubMed:10924525, ECO:0000269|PubMed:17891141}. TISSUE SPECIFICITY: Smooth muscle cells of the gut and adrenal tissue. +Q61039 HAND2_MOUSE Heart- and neural crest derivatives-expressed protein 2 (Deciduum, heart, autonomic nervous system and neural crest derivatives-expressed protein 2) (dHAND) (Helix-loop-helix transcription factor expressed in embryo and deciduum) (Thing-2) 217 23,666 Chain (1); Compositional bias (1); Domain (1); Frameshift (2); Sequence conflict (3) FUNCTION: Essential for cardiac morphogenesis, particularly for the formation of the right ventricle and of the aortic arch arteries. Required for vascular development and regulation of angiogenesis, possibly through a VEGF signaling pathway. Plays also an important role in limb development, particularly in the establishment of anterior-posterior polarization, acting as an upstream regulator of sonic hedgehog (SHH) induction in the limb bud. Is involved in the development of branchial arches, which give rise to unique structures in the head and neck. Binds DNA on E-box consensus sequence 5'-CANNTG-3'. {ECO:0000269|PubMed:10769237, ECO:0000269|PubMed:10804186, ECO:0000269|PubMed:9171826, ECO:0000269|PubMed:9671575}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}. SUBUNIT: Efficient DNA binding requires dimerization with another bHLH protein. Forms homodimers and heterodimers with TCF3 gene products E12 and E47, HAND1 and HEY1, HEY2 and HEYL (hairy-related transcription factors). {ECO:0000269|PubMed:10924525}. TISSUE SPECIFICITY: Heart and aorta. +Q8QZX2 HAUS3_MOUSE HAUS augmin-like complex subunit 3 570 66,308 Alternative sequence (1); Chain (1); Coiled coil (4); Erroneous initiation (1); Initiator methionine (1); Modified residue (1); Sequence conflict (1) FUNCTION: Contributes to mitotic spindle assembly, maintenance of centrosome integrity and completion of cytokinesis as part of the HAUS augmin-like complex. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Localizes to interphase centrosomes and to mitotic spindle microtubules. {ECO:0000250}. SUBUNIT: Component of the HAUS augmin-like complex. The complex interacts with the gamma-tubulin ring complex and this interaction is required for spindle assembly (By similarity). {ECO:0000250}. +Q8BKT8 HAUS7_MOUSE HAUS augmin-like complex subunit 7 (26S proteasome-associated UCH37-interacting protein 1) (UCHL5-interacting protein) 364 40,656 Alternative sequence (1); Chain (1); Sequence conflict (1) FUNCTION: Contributes to mitotic spindle assembly, maintenance of centrosome integrity and completion of cytokinesis as part of the HAUS augmin-like complex. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Localizes to interphase centrosomes and to mitotic spindle microtubules. {ECO:0000250}. SUBUNIT: Component of the HAUS augmin-like complex. The complex interacts with the gamma-tubulin ring complex and this interaction is required for spindle assembly. Binds UCHL5 (By similarity). {ECO:0000250}. +Q99L00 HAUS8_MOUSE HAUS augmin-like complex subunit 8 (HEC1/NDC80-interacting centrosome-associated protein 1) (Sarcoma antigen NY-SAR-48 homolog) 373 41,653 Alternative sequence (1); Chain (1); Coiled coil (1); Initiator methionine (1); Modified residue (2); Sequence conflict (2) FUNCTION: Contributes to mitotic spindle assembly, maintenance of centrosome integrity and completion of cytokinesis as part of the HAUS augmin-like complex. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. Note=During interphase, primarily cytoplasmic and associates with centrosomes and with the mitotic spindles, preferentially at the spindle pole vicinity. During anaphase and telophase, additionally associates with the spindle midzone and midbody, respectively (By similarity). {ECO:0000250}. SUBUNIT: Component of the HAUS augmin-like complex. The complex interacts with the gamma-tubulin ring complex and this interaction is required for spindle assembly. Associates with microtubules. The interaction with microtubules is strong during mitosis, while it is weak or absent during interphase. It is unclear whether this interaction is direct or indirect (By similarity). {ECO:0000250}. +P18468 HB2I_MOUSE H-2 class II histocompatibility antigen, I-A beta chain 264 30,232 Beta strand (13); Chain (1); Disulfide bond (2); Domain (1); Glycosylation (1); Helix (5); Region (3); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (2) TRANSMEM 226 248 Helical. {ECO:0000255}. TOPO_DOM 32 225 Extracellular. {ECO:0000255}.; TOPO_DOM 249 264 Cytoplasmic. {ECO:0000255}. PTM: Ubiquitinated in immature dendritic cells leading to down-regulation of MHC class II. {ECO:0000269|PubMed:17051151, ECO:0000269|PubMed:17174123}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +P18469 HB2J_MOUSE H-2 class II histocompatibility antigen, I-E beta chain 264 30,141 Chain (1); Disulfide bond (2); Domain (1); Glycosylation (1); Region (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 226 248 Helical. {ECO:0000255}. TOPO_DOM 32 225 Extracellular. {ECO:0000255}.; TOPO_DOM 249 264 Cytoplasmic. {ECO:0000255}. PTM: Ubiquitinated in immature dendritic cells leading to down-regulation of MHC class II. {ECO:0000269|PubMed:17051151, ECO:0000269|PubMed:17174123}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +P06467 HBAZ_MOUSE Hemoglobin subunit zeta (Alpha-like embryonic globin chain x) (Hemoglobin zeta chain) (Zeta-globin) 142 16,235 Chain (1); Initiator methionine (1); Metal binding (2); Modified residue (4); Sequence conflict (3) FUNCTION: The zeta chain is an alpha-type chain of mammalian embryonic hemoglobin. {ECO:0000250}. SUBUNIT: Heterotetramer of two zeta chains and beta-type chains. {ECO:0000250}. +P11032 GRAA_MOUSE Granzyme A (EC 3.4.21.78) (Autocrine thymic lymphoma granzyme-like serine protease) (CTLA-3) (Fragmentin-1) (T cell-specific serine protease 1) (TSP-1) 260 28,599 Active site (3); Alternative sequence (1); Chain (1); Disulfide bond (4); Domain (1); Glycosylation (2); Propeptide (1); Signal peptide (1) FUNCTION: Abundant protease in the cytosolic granules of cytotoxic T-cells and NK-cells which activates caspase-independent cell death with morphological features of apoptosis when delivered into the target cell through the immunological synapse. It cleaves after Lys or Arg. Cleaves APEX1 after 'Lys-31' and destroys its oxidative repair activity. Cleaves the nucleosome assembly protein SET after 'Lys-189', which disrupts its nucleosome assembly activity and allows the SET complex to translocate into the nucleus to nick and degrade the DNA (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. Cytoplasmic granule. Note=Cytoplasmic granules of cytolytic T-lymphocytes. SUBUNIT: Interacts with APEX1 (By similarity). Homodimer; disulfide-linked. {ECO:0000250}. TISSUE SPECIFICITY: Found in cytotoxic lymphocytes and in normal lymphoid tissues such as thymus and spleen. +B9EJV3 GRB1L_MOUSE GREB1-like protein 1913 213,628 Chain (1); Compositional bias (1); Transmembrane (1) TRANSMEM 1832 1852 Helical. {ECO:0000255}. FUNCTION: Plays a major role in early metanephros and genital development. {ECO:0000269|PubMed:29100091}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q0QWG9 GRD2I_MOUSE Delphilin (Glutamate receptor, ionotropic, delta 2-interacting protein 1) 1203 132,021 Alternative sequence (4); Chain (1); Compositional bias (1); Domain (3); Lipidation (1); Modified residue (5) FUNCTION: Postsynaptic scaffolding protein at the Purkinje cell synapse, where it may serve to link GRID2 with actin cytoskeleton and various signaling molecules. PTM: Isoform 2 is palmitoylated. Palmitoylation of isoform 2 is necessary for the enhanced cell surface expression of GRID2, and is also responsible for the accumulation of isoform 2 within dendritic spines. Isoform 1 and isoform 2 are differentially localized, probably modulating GRID2 signaling in neurons. SUBCELLULAR LOCATION: Isoform 2: Cell junction, synapse, postsynaptic cell membrane. Cell projection, dendritic spine. Note=Localized to the postsynaptic junction site of the parallel fiber-Purkinje cell synapse. Highly present in the dendritic spines.; SUBCELLULAR LOCATION: Isoform 3: Cell junction, synapse. Cell projection, dendritic spine. Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Note=Localized at the dendritic spines, but also in dendritic shafts apart fron spines. SUBUNIT: Interacts with C-terminus of the glutamate receptor GRID2 via PDZ domain. Isoform 2 interacts also with Profilin-2/PFN2 and with the monocarboxylate transporter SLC16A7 via PDZ domain. The interaction of isoform 2 with GRID2 is dependent on GRID2 phosphorylation by PKA. {ECO:0000269|PubMed:11826110, ECO:0000269|PubMed:16168524, ECO:0000269|PubMed:16835239, ECO:0000269|PubMed:17027646, ECO:0000269|PubMed:17425562, ECO:0000269|PubMed:17496809}. DOMAIN: PDZ 1 domain is responsible for cytoplasmic clustering of isoform 1. TISSUE SPECIFICITY: Isoform 1 is expressed in the cerebellum, but not in the cerebral cortex. Isoform 2 is expressed in the cell body of purkinge cells of the cerebellum and weakly expressed in the cerebrum and the brainstem as well as various nuclei of the thalamus. Isoform 2 is highly expressed in the cerebral cortex than in the cerebellum. Isoform 3 is expressed in the cerebellum and cerebrum. {ECO:0000269|PubMed:11826110, ECO:0000269|PubMed:16835239}. +Q02591 GSC_MOUSE Homeobox protein goosecoid 256 27,980 Chain (1); DNA binding (1) FUNCTION: Regulates chordin (CHRD). May play a role in spatial programing within discrete embryonic fields or lineage compartments during organogenesis (By similarity). In concert with NKX3-2, plays a role in defining the structural components of the middle ear; required for the development of the entire tympanic ring. Goosecoid-expressing regions of the gastrulating mouse egg cylinder have organizer-like activity when transplanted into Xenopus embryos. Probably involved in the regulatory networks that define neural crest cell fate specification and determine mesoderm cell lineages in mammals (By similarity). {ECO:0000250, ECO:0000269|PubMed:14973294}. SUBCELLULAR LOCATION: Nucleus. TISSUE SPECIFICITY: In early gastrulation, expressed in the dorsal lip. In later stages of development found in head, limbs and body wall. In the embryo, expressed in the postotic cranial neural crest cells, the frontonasal prominence, the first branchial arch and cleft, and specific regions of large joints. {ECO:0000269|PubMed:24290375}. +Q32M21 GSDA2_MOUSE Gasdermin-A2 (Gasdermin-2) 443 49,844 Alternative sequence (3); Chain (1); Coiled coil (1); Region (1) FUNCTION: May promote pyroptosis. Upon cleavage in vitro of genetically engineered GSDMA, the released N-terminal moiety binds to some types of lipids, such as possibly phosphatidylinositol (4,5)-bisphosphate. Homooligomerizes within the membrane and forms pores of 10 -15 nanometers (nm) of inner diameter, triggering cell death. Also binds to bacterial and mitochondrial lipids, including cardiolipin, and exhibits bactericidal activity. The physiological relevance of these observations is unknown. {ECO:0000250|UniProtKB:Q96QA5}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q96QA5}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P57764}. Cell membrane {ECO:0000250|UniProtKB:P57764}. SUBUNIT: The N-terminal moiety forms homooligomer; disulfide-linked. May form an 16-mer complex. Oligomerization occurs in the presence of membranes. {ECO:0000250|UniProtKB:P57764}. DOMAIN: Intramolecular interactions between N- and C-terminal domains may be important for autoinhibition in the absence of activation signal. The intrinsic pyroptosis-inducing activity is carried by the N-terminal domain. {ECO:0000250|UniProtKB:Q5Y4Y6}. TISSUE SPECIFICITY: Expressed in the gastrointestinal tract, specifically from the middle to the upper region of the gastric mucosa in the glandular stomach. {ECO:0000269|PubMed:17350798}. +Q2KHK6 GSDC2_MOUSE Gasdermin-C2 480 53,952 Chain (1); Region (1); Sequence conflict (12) FUNCTION: The N-terminal moiety promotes pyroptosis and exhibits bactericidal activity. The physiological relevance of these observations is unknown. {ECO:0000250|UniProtKB:Q9BYG8}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9BYG8}. Cell membrane {ECO:0000250|UniProtKB:P57764}. SUBUNIT: The N-terminal moiety forms homooligomer; disulfide-linked. May form an 16-mer complex. Oligomerization occurs in the presence of membranes. {ECO:0000250|UniProtKB:P57764}. DOMAIN: Intramolecular interactions between N- and C-terminal domains may be important for autoinhibition in the absence of activation signal. The intrinsic pyroptosis-inducing activity is carried by the N-terminal domain. {ECO:0000250|UniProtKB:Q5Y4Y6}. +Q8CB12 GSDC3_MOUSE Gasdermin-C3 480 54,188 Chain (1); Region (1); Sequence conflict (1) FUNCTION: The N-terminal moiety promotes pyroptosis and exhibits bactericidal activity. The physiological relevance of these observations is unknown. {ECO:0000250|UniProtKB:Q9BYG8}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9BYG8}. Cell membrane {ECO:0000250|UniProtKB:P57764}. SUBUNIT: The N-terminal moiety forms homooligomer; disulfide-linked. May form an 16-mer complex. Oligomerization occurs in the presence of membranes. {ECO:0000250|UniProtKB:P57764}. DOMAIN: Intramolecular interactions between N- and C-terminal domains may be important for autoinhibition in the absence of activation signal. The intrinsic pyroptosis-inducing activity is carried by the N-terminal domain. {ECO:0000250|UniProtKB:Q5Y4Y6}. +Q3TR54 GSDC4_MOUSE Gasdermin-C4 480 53,992 Chain (1); Region (1); Sequence conflict (2) FUNCTION: The N-terminal moiety promotes pyroptosis and exhibits bactericidal activity. The physiological relevance of these observations is unknown. {ECO:0000250|UniProtKB:Q9BYG8}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9BYG8}. Cell membrane {ECO:0000250|UniProtKB:P57764}. SUBUNIT: The N-terminal moiety forms homooligomer; disulfide-linked. May form an 16-mer complex. Oligomerization occurs in the presence of membranes. {ECO:0000250|UniProtKB:P57764}. DOMAIN: Intramolecular interactions between N- and C-terminal domains may be important for autoinhibition in the absence of activation signal. The intrinsic pyroptosis-inducing activity is carried by the N-terminal domain. {ECO:0000250|UniProtKB:Q5Y4Y6}. +A6PWV3 IZUM3_MOUSE Izumo sperm-egg fusion protein 3 263 30,314 Alternative sequence (1); Chain (1); Frameshift (1); Glycosylation (2); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 177 197 Helical. {ECO:0000255}. TOPO_DOM 23 176 Extracellular. {ECO:0000255}.; TOPO_DOM 198 263 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Monomer and homodimer. {ECO:0000269|PubMed:19658160}. TISSUE SPECIFICITY: Sperm-specific (at protein level). {ECO:0000269|PubMed:19658160}. +D3Z690 IZUM4_MOUSE Izumo sperm-egg fusion protein 4 227 26,332 Alternative sequence (2); Chain (1); Glycosylation (2); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q8K135 K319L_MOUSE Dyslexia-associated protein KIAA0319-like protein (Adeno-associated virus receptor) (AAVR) 1048 115,312 Alternative sequence (1); Chain (1); Domain (6); Glycosylation (2); Modified residue (5); Sequence caution (1); Sequence conflict (4); Topological domain (3); Transmembrane (2) TRANSMEM 30 50 Helical. {ECO:0000255}.; TRANSMEM 929 949 Helical. {ECO:0000255}. TOPO_DOM 1 29 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 51 928 Extracellular. {ECO:0000255}.; TOPO_DOM 950 1048 Cytoplasmic. {ECO:0000255}. FUNCTION: Possible role in axon guidance through interaction with RTN4R. {ECO:0000250|UniProtKB:Q8IZA0}.; FUNCTION: (Microbial infection) Acts as a receptor for adeno-associated virus and is involved in adeno-associated virus infection through endocytosis system. {ECO:0000305|PubMed:26814968}. PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasmic granule membrane {ECO:0000250|UniProtKB:Q8IZA0}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8IZA0}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q8IZA0}; Multi-pass membrane protein. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q8IZA0}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8IZA0}. Cell membrane {ECO:0000250|UniProtKB:Q8IZA0}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8IZA0}. Note=Traffics from the plasma membrane to the trans-Golgi network. {ECO:0000250|UniProtKB:Q8IZA0}. SUBUNIT: Interacts with RTN4R. {ECO:0000250|UniProtKB:Q8IZA0}. +Q810A5 K895L_MOUSE Uncharacterized protein KIAA0895-like 467 53,170 Chain (1); Sequence conflict (2) +A3KGW5 GT253_MOUSE Inactive glycosyltransferase 25 family member 3 (Cerebral endothelial cell adhesion molecule) 592 67,672 Chain (1); Glycosylation (4); Motif (1); Signal peptide (1) FUNCTION: Probable cell adhesion protein involved in leukocyte transmigration across the blood-brain barrier. Does not express any beta-galactosyltransferase activity in vitro. {ECO:0000250|UniProtKB:Q5T4B2}. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138}. +Q80W21 GSTM7_MOUSE Glutathione S-transferase Mu 7 (EC 2.5.1.18) (GST class-mu 7) (GSTM-7) 218 25,710 Beta strand (6); Binding site (1); Chain (1); Domain (2); Helix (9); Region (4); Sequence conflict (2); Turn (2) FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +Q923K4 GTPB3_MOUSE tRNA modification GTPase GTPBP3, mitochondrial (GTP-binding protein 3) 492 52,175 Alternative sequence (2); Chain (1); Domain (1); Nucleotide binding (3); Transit peptide (1) FUNCTION: GTPase involved in the 5-carboxymethylaminomethyl modification (mnm(5)s(2)U34) of the wobble uridine base in mitochondrial tRNAs. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14680828}. TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in tissues with high metabolic rates including heart, liver and brain. Weakly expressed in skeletal muscle. {ECO:0000269|PubMed:14680828}. +Q8K013 GTPBA_MOUSE GTP-binding protein 10 366 40,142 Chain (1); Domain (1); Nucleotide binding (3) FUNCTION: May be involved in the ribosome maturation process. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus. Note=Found in the dense fibrillar compartment region of the nucleolus. {ECO:0000250}. +Q8BFW9 GTR12_MOUSE Solute carrier family 2, facilitated glucose transporter member 12 (Glucose transporter type 12) (GLUT-12) 622 67,336 Chain (1); Glycosylation (5); Sequence conflict (3); Topological domain (13); Transmembrane (12) TRANSMEM 45 65 Helical. {ECO:0000255}.; TRANSMEM 85 105 Helical. {ECO:0000255}.; TRANSMEM 112 132 Helical. {ECO:0000255}.; TRANSMEM 142 162 Helical. {ECO:0000255}.; TRANSMEM 169 189 Helical. {ECO:0000255}.; TRANSMEM 202 222 Helical. {ECO:0000255}.; TRANSMEM 283 303 Helical. {ECO:0000255}.; TRANSMEM 322 342 Helical. {ECO:0000255}.; TRANSMEM 350 370 Helical. {ECO:0000255}.; TRANSMEM 472 492 Helical. {ECO:0000255}.; TRANSMEM 504 524 Helical. {ECO:0000255}.; TRANSMEM 534 554 Helical. {ECO:0000255}. TOPO_DOM 1 44 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 66 84 Extracellular. {ECO:0000255}.; TOPO_DOM 106 111 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 133 141 Extracellular. {ECO:0000255}.; TOPO_DOM 163 168 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 190 201 Extracellular. {ECO:0000255}.; TOPO_DOM 223 282 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 304 321 Extracellular. {ECO:0000255}.; TOPO_DOM 343 349 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 371 471 Extracellular. {ECO:0000255}.; TOPO_DOM 493 503 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 525 533 Extracellular. {ECO:0000255}.; TOPO_DOM 555 622 Cytoplasmic. {ECO:0000255}. FUNCTION: Facilitative glucose transporter. {ECO:0000250}. PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Expressed in skeletal muscle, heart, brain, kidney, spleen, adipose tissues and to a lesser extent in small intestine and lung. {ECO:0000269|PubMed:12890477}. +P52785 GUC2E_MOUSE Guanylyl cyclase GC-E (EC 4.6.1.2) (Guanylate cyclase 2E) 1108 120,638 Chain (1); Disulfide bond (3); Domain (2); Glycosylation (1); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 466 490 Helical. {ECO:0000255}. TOPO_DOM 55 465 Extracellular. {ECO:0000255}.; TOPO_DOM 491 1108 Cytoplasmic. {ECO:0000255}. PTM: There are 9 conserved cysteine residues in sensory guanylate cyclases, 6 in the extracellular domain, which may be involved in intra- or interchain disulfide bonds. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. +Q80SU7 GVIN1_MOUSE Interferon-induced very large GTPase 1 (Very large-inducible GTPase-1) (VLIG-1) 2427 280,815 Chain (1); Domain (1); Erroneous initiation (1); Nucleotide binding (3); Sequence conflict (3) SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12874213}. Nucleus {ECO:0000269|PubMed:12874213}. TISSUE SPECIFICITY: Widely expressed. Expressed at low basal level in lung, heart, thymus and spleen; at still lower level in liver, ovary, kidney and brain. Expressed at very weak level in testis. Undetectable in embryo. {ECO:0000269|PubMed:12874213}. +Q4VBD9 GZF1_MOUSE GDNF-inducible zinc finger protein 1 (Zinc finger protein 336) 706 79,533 Chain (1); Domain (1); Modified residue (1); Sequence conflict (1); Zinc finger (10) FUNCTION: Transcriptional repressor that binds the GZF1 responsive element (GRE) (consensus: 5'-TGCGCN[TG][CA]TATA-3'). May be regulating VSX2/HOX10 expression. {ECO:0000250|UniProtKB:Q9H116}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14522971, ECO:0000269|PubMed:28475863}. Cytoplasm {ECO:0000269|PubMed:14522971, ECO:0000269|PubMed:28475863}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9H116}. Note=Predominantly nuclear. {ECO:0000269|PubMed:14522971}. SUBUNIT: Interacts with NCL. {ECO:0000250|UniProtKB:Q9H116}. TISSUE SPECIFICITY: Expressed in several tissues, with highest levels in liver. Also expressed in embryos from 7 to 17 dpc. {ECO:0000269|PubMed:14522971}. +P15864 H12_MOUSE Histone H1.2 (H1 VAR.1) (H1c) 212 21,267 Chain (1); Domain (1); Initiator methionine (1); Modified residue (44); Mutagenesis (2) FUNCTION: Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity). {ECO:0000250, ECO:0000269|PubMed:12808097, ECO:0000269|PubMed:16377562}. PTM: H1 histones are progressively phosphorylated during the cell cycle, becoming maximally phosphorylated during late G2 phase and M phase, and being dephosphorylated sharply thereafter. {ECO:0000250}.; PTM: Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes. {ECO:0000269|PubMed:21925322}.; PTM: ADP-ribosylated on Ser-187 in response to DNA damage. {ECO:0000250|UniProtKB:P16403}.; PTM: Citrullination at Arg-54 (H1R54ci) by PADI4 takes place within the DNA-binding site of H1 and results in its displacement from chromatin and global chromatin decondensation, thereby promoting pluripotency and stem cell maintenance. {ECO:0000269|PubMed:24463520}.; PTM: Hydroxybutyrylation of histones is induced by starvation. {ECO:0000250|UniProtKB:P43277}. SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Mainly localizes in euchromatin. {ECO:0000250}. DOMAIN: The C-terminal domain is required for high-affinity binding to chromatin. {ECO:0000250}. +P43276 H15_MOUSE Histone H1.5 (H1 VAR.5) (H1b) 223 22,576 Chain (1); Domain (1); Initiator methionine (1); Modified residue (21); Sequence conflict (4) FUNCTION: Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity). {ECO:0000250}. PTM: H1 histones are progressively phosphorylated during the cell cycle, becoming maximally phosphorylated during late G2 phase and M phase, and being dephosphorylated sharply thereafter. {ECO:0000250|UniProtKB:P16401}.; PTM: Citrullination at Arg-54 (H1R54ci) by PADI4 takes place within the DNA-binding site of H1 and results in its displacement from chromatin and global chromatin decondensation, thereby promoting pluripotency and stem cell maintenance. {ECO:0000269|PubMed:24463520}.; PTM: Hydroxybutyrylation of histones is induced by starvation. {ECO:0000250|UniProtKB:P43277}. SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Mainly localizes in heterochromatin. {ECO:0000250}. DOMAIN: The C-terminal domain is required for high-affinity binding to chromatin. {ECO:0000250}. +Q8CJI4 H1FNT_MOUSE Testis-specific H1 histone (Haploid germ cell-specific nuclear protein 1) (Histone H1t2) 398 44,400 Chain (1); Coiled coil (1); Frameshift (1); Modified residue (1); Sequence conflict (2) FUNCTION: Essential for normal spermatogenesis and male fertility. Required for proper cell restructuring and DNA condensation during the elongation phase of spermiogenesis. Involved in the histone-protamine transition of sperm chromatin and the subsequent production of functional sperm. Binds both double-stranded and single-stranded DNA, ATP and protamine-1. {ECO:0000269|PubMed:15710904, ECO:0000269|PubMed:16055721}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15710904, ECO:0000269|PubMed:16055721}. Chromosome {ECO:0000269|PubMed:15710904, ECO:0000269|PubMed:16055721}. Note=In round and elongating spermatids, specifically localizes to a chromatin domain at the apical pole. {ECO:0000269|PubMed:15710904}. TISSUE SPECIFICITY: Testis-specific. Specifically expressed in haploid germ cells. {ECO:0000269|PubMed:15710904, ECO:0000269|PubMed:16055721}. +Q8VIK3 H1FOO_MOUSE Histone H1oo (Oocyte-specific histone H1) (Oocyte-specific linker histone H1) 304 32,223 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (1); Motif (1) FUNCTION: May play a key role in the control of gene expression during oogenesis and early embryogenesis, presumably through the perturbation of chromatin structure. Essential for meiotic maturation of germinal vesicle-stage oocytes. The somatic type linker histone H1c is rapidly replaced by H1oo in a donor nucleus transplanted into an oocyte. The greater mobility of H1oo as compared to H1c may contribute to this rapid replacement and increased instability of the embryonic chromatin structure. The rapid replacement of H1c with H1oo may play an important role in nuclear remodeling. {ECO:0000269|PubMed:11171391, ECO:0000269|PubMed:14729479, ECO:0000269|PubMed:15371275, ECO:0000269|PubMed:17519519}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus. Chromosome. Note=In the germinal vesicle oocyte, localizes to the condensed chromosomes. In the 1-cell embryo found in condensed maternal metaphase chromatin but not in the sperm head. Following second polar body extrusion, detected in the swollen sperm head as well as in the second polar body. Reduced expression in the nucleus in 2-cell embryo is seen as compared to 1-cell embryo. TISSUE SPECIFICITY: Oocyte-specific. {ECO:0000269|PubMed:11171391, ECO:0000269|PubMed:15371275}. +Q9R092 H17B6_MOUSE 17-beta-hydroxysteroid dehydrogenase type 6 (17-beta-HSD 6) (17-beta-HSD6) (EC 1.1.1.105) (EC 1.1.1.239) (EC 1.1.1.62) (17-beta-HSD9) (3-alpha->beta-hydroxysteroid epimerase) (3-alpha->beta-HSE) (Oxidative 3-alpha hydroxysteroid dehydrogenase) 317 36,103 Active site (1); Binding site (1); Chain (1); Glycosylation (2); Nucleotide binding (1); Signal peptide (1) FUNCTION: NAD-dependent oxidoreductase with broad substrate specificity that shows both oxidative and reductive activity (in vitro). Has 17-beta-hydroxysteroid dehydrogenase activity towards various steroids (in vitro). Converts 5-alpha-androstan-3-alpha,17-beta-diol to androsterone and estradiol to estrone (in vitro). Has 3-alpha-hydroxysteroid dehydrogenase activity towards androsterone (in vitro). Has retinol dehydrogenase activity towards all-trans-retinol (in vitro). {ECO:0000269|PubMed:10537158}. SUBCELLULAR LOCATION: Microsome membrane {ECO:0000269|PubMed:10537158}; Peripheral membrane protein {ECO:0000269|PubMed:10537158}; Lumenal side {ECO:0000269|PubMed:10537158}. Early endosome membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Lumenal side {ECO:0000305}. TISSUE SPECIFICITY: Detected in liver. {ECO:0000269|PubMed:10537158}. +Q3TC93 H1BP3_MOUSE HCLS1-binding protein 3 (HS1-binding protein 3) (HSP1BP-3) 395 43,691 Chain (1); Compositional bias (3); Domain (1); Modified residue (5); Sequence conflict (2) FUNCTION: May be a modulator of IL-2 signaling. SUBUNIT: Binds HCLS1. Interacts with the SH3 domain of HCLS1 in vitro. {ECO:0000269|PubMed:10590261}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:10590261}. +C0HKE1 H2A1B_MOUSE Histone H2A type 1-B 130 14,135 Beta strand (3); Chain (1); Cross-link (3); Helix (6); Initiator methionine (1); Modified residue (25); Sequence conflict (1); Turn (2) FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. PTM: Deiminated on Arg-4 in granulocytes upon calcium entry. {ECO:0000250|UniProtKB:P0C0S8}.; PTM: Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM27 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is involved in the initiation of both imprinted and random X inactivation. Ubiquitinated H2A is enriched in inactive X chromosome chromatin. Ubiquitination of H2A functions downstream of methylation of 'Lys-27' of histone H3 (H3K27me). H2AK119Ub by RNF2/RING2 can also be induced by ultraviolet and may be involved in DNA repair. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties by the E2 ligase UBE2N and the E3 ligases RNF8 and RNF168, leading to the recruitment of repair proteins to sites of DNA damage. Ubiquitination at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) in response to DNA damage is initiated by RNF168 that mediates monoubiquitination at these 2 sites, and 'Lys-63'-linked ubiquitin are then conjugated to monoubiquitin; RNF8 is able to extend 'Lys-63'-linked ubiquitin chains in vitro. Deubiquitinated by USP51 at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) after damaged DNA is repaired (By similarity). H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination (H2AK13Ub and H2AK15Ub) are distinct events. {ECO:0000250|UniProtKB:P0C0S8, ECO:0000269|PubMed:15509584, ECO:0000269|PubMed:15525528, ECO:0000269|PubMed:24352239}.; PTM: Phosphorylation on Ser-2 (H2AS1ph) is enhanced during mitosis. Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses transcription. Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1. Phosphorylation at Thr-121 (H2AT120ph) by DCAF1 is present in the regulatory region of many tumor suppresor genes and down-regulates their transcription. {ECO:0000250|UniProtKB:P0C0S8, ECO:0000269|PubMed:7217105}.; PTM: Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage. {ECO:0000269|PubMed:16699504}.; PTM: Glutamine methylation at Gln-105 (H2AQ104me) by FBL is specifically dedicated to polymerase I. It is present at 35S ribosomal DNA locus and impairs binding of the FACT complex. {ECO:0000269|PubMed:24352239}.; PTM: Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes. {ECO:0000269|PubMed:21925322}.; PTM: Hydroxybutyrylation of histones is induced by starvation. {ECO:0000269|PubMed:27105115}. SUBCELLULAR LOCATION: Nucleus. Chromosome. SUBUNIT: The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. +C0HKE2 H2A1C_MOUSE Histone H2A type 1-C 130 14,135 Chain (1); Cross-link (3); Initiator methionine (1); Modified residue (24) FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. PTM: Deiminated on Arg-4 in granulocytes upon calcium entry. {ECO:0000250|UniProtKB:P0C0S8}.; PTM: Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM27 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is involved in the initiation of both imprinted and random X inactivation. Ubiquitinated H2A is enriched in inactive X chromosome chromatin. Ubiquitination of H2A functions downstream of methylation of 'Lys-27' of histone H3 (H3K27me). H2AK119Ub by RNF2/RING2 can also be induced by ultraviolet and may be involved in DNA repair. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties by the E2 ligase UBE2N and the E3 ligases RNF8 and RNF168, leading to the recruitment of repair proteins to sites of DNA damage. Ubiquitination at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) in response to DNA damage is initiated by RNF168 that mediates monoubiquitination at these 2 sites, and 'Lys-63'-linked ubiquitin are then conjugated to monoubiquitin; RNF8 is able to extend 'Lys-63'-linked ubiquitin chains in vitro. Deubiquitinated by USP51 at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) after damaged DNA is repaired (By similarity). H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination (H2AK13Ub and H2AK15Ub) are distinct events. {ECO:0000250|UniProtKB:P0C0S8, ECO:0000269|PubMed:15509584, ECO:0000269|PubMed:15525528, ECO:0000269|PubMed:24352239}.; PTM: Phosphorylation on Ser-2 (H2AS1ph) is enhanced during mitosis. Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses transcription. Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1. Phosphorylation at Thr-121 (H2AT120ph) by DCAF1 is present in the regulatory region of many tumor suppresor genes and down-regulates their transcription. {ECO:0000250|UniProtKB:P0C0S8, ECO:0000269|PubMed:7217105}.; PTM: Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage. {ECO:0000269|PubMed:16699504}.; PTM: Glutamine methylation at Gln-105 (H2AQ104me) by FBL is specifically dedicated to polymerase I. It is present at 35S ribosomal DNA locus and impairs binding of the FACT complex. {ECO:0000269|PubMed:24352239}.; PTM: Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes. {ECO:0000269|PubMed:21925322}.; PTM: Hydroxybutyrylation of histones is induced by starvation. {ECO:0000269|PubMed:27105115}. SUBCELLULAR LOCATION: Nucleus. Chromosome. SUBUNIT: The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. +C0HKE4 H2A1E_MOUSE Histone H2A type 1-E 130 14,135 Chain (1); Cross-link (3); Initiator methionine (1); Modified residue (24) FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. PTM: Deiminated on Arg-4 in granulocytes upon calcium entry. {ECO:0000250|UniProtKB:P0C0S8}.; PTM: Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM27 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is involved in the initiation of both imprinted and random X inactivation. Ubiquitinated H2A is enriched in inactive X chromosome chromatin. Ubiquitination of H2A functions downstream of methylation of 'Lys-27' of histone H3 (H3K27me). H2AK119Ub by RNF2/RING2 can also be induced by ultraviolet and may be involved in DNA repair. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties by the E2 ligase UBE2N and the E3 ligases RNF8 and RNF168, leading to the recruitment of repair proteins to sites of DNA damage. Ubiquitination at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) in response to DNA damage is initiated by RNF168 that mediates monoubiquitination at these 2 sites, and 'Lys-63'-linked ubiquitin are then conjugated to monoubiquitin; RNF8 is able to extend 'Lys-63'-linked ubiquitin chains in vitro. Deubiquitinated by USP51 at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) after damaged DNA is repaired (By similarity). H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination (H2AK13Ub and H2AK15Ub) are distinct events. {ECO:0000250|UniProtKB:P0C0S8, ECO:0000269|PubMed:15509584, ECO:0000269|PubMed:15525528, ECO:0000269|PubMed:24352239}.; PTM: Phosphorylation on Ser-2 (H2AS1ph) is enhanced during mitosis. Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses transcription. Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1. Phosphorylation at Thr-121 (H2AT120ph) by DCAF1 is present in the regulatory region of many tumor suppresor genes and down-regulates their transcription. {ECO:0000250|UniProtKB:P0C0S8, ECO:0000269|PubMed:7217105}.; PTM: Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage. {ECO:0000269|PubMed:16699504}.; PTM: Glutamine methylation at Gln-105 (H2AQ104me) by FBL is specifically dedicated to polymerase I. It is present at 35S ribosomal DNA locus and impairs binding of the FACT complex. {ECO:0000269|PubMed:24352239}.; PTM: Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes. {ECO:0000269|PubMed:21925322}.; PTM: Hydroxybutyrylation of histones is induced by starvation. {ECO:0000269|PubMed:27105115}. SUBCELLULAR LOCATION: Nucleus. Chromosome. SUBUNIT: The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. +Q8CGP5 H2A1F_MOUSE Histone H2A type 1-F 130 14,162 Chain (1); Cross-link (1); Initiator methionine (1); Modified residue (20) FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. PTM: Deiminated on Arg-4 in granulocytes upon calcium entry. {ECO:0000250|UniProtKB:P0C0S8}.; PTM: Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM27 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is involved in the initiation of both imprinted and random X inactivation. Ubiquitinated H2A is enriched in inactive X chromosome chromatin. Ubiquitination of H2A functions downstream of methylation of 'Lys-27' of histone H3 (H3K27me). H2AK119Ub by RNF2/RING2 can also be induced by ultraviolet and may be involved in DNA repair. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties by the E2 ligase UBE2N and the E3 ligases RNF8 and RNF168, leading to the recruitment of repair proteins to sites of DNA damage. Ubiquitination at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) in response to DNA damage is initiated by RNF168 that mediates monoubiquitination at these 2 sites, and 'Lys-63'-linked ubiquitin are then conjugated to monoubiquitin; RNF8 is able to extend 'Lys-63'-linked ubiquitin chains in vitro. H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination (H2AK13Ub and H2AK15Ub) are distinct events. {ECO:0000250|UniProtKB:P0C0S8, ECO:0000269|PubMed:15509584, ECO:0000269|PubMed:15525528, ECO:0000269|PubMed:24352239}.; PTM: Phosphorylation on Ser-2 (H2AS1ph) is enhanced during mitosis. Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses transcription. Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1. Phosphorylation at Thr-121 (H2AT120ph) by DCAF1 is present in the regulatory region of many tumor suppresor genes and down-regulates their transcription. {ECO:0000250|UniProtKB:P0C0S8}.; PTM: Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage. {ECO:0000269|PubMed:16699504}.; PTM: Glutamine methylation at Gln-105 (H2AQ104me) by FBL is specifically dedicated to polymerase I. It is present at 35S ribosomal DNA locus and impairs binding of the FACT complex. {ECO:0000269|PubMed:24352239}.; PTM: Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes. {ECO:0000269|PubMed:21925322}.; PTM: Hydroxybutyrylation of histones is induced by starvation. {ECO:0000269|PubMed:27105115}. SUBCELLULAR LOCATION: Nucleus. Chromosome. SUBUNIT: The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. +Q8CGP6 H2A1H_MOUSE Histone H2A type 1-H 128 13,950 Beta strand (3); Chain (1); Cross-link (3); Helix (6); Initiator methionine (1); Modified residue (23); Turn (1) FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. PTM: Deiminated on Arg-4 in granulocytes upon calcium entry. {ECO:0000250|UniProtKB:P0C0S8}.; PTM: Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM27 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is involved in the initiation of both imprinted and random X inactivation. Ubiquitinated H2A is enriched in inactive X chromosome chromatin. Ubiquitination of H2A functions downstream of methylation of 'Lys-27' of histone H3 (H3K27me). H2AK119Ub by RNF2/RING2 can also be induced by ultraviolet and may be involved in DNA repair. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties by the E2 ligase UBE2N and the E3 ligases RNF8 and RNF168, leading to the recruitment of repair proteins to sites of DNA damage. Ubiquitination at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) in response to DNA damage is initiated by RNF168 that mediates monoubiquitination at these 2 sites, and 'Lys-63'-linked ubiquitin are then conjugated to monoubiquitin; RNF8 is able to extend 'Lys-63'-linked ubiquitin chains in vitro. H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination (H2AK13Ub and H2AK15Ub) are distinct events. {ECO:0000250|UniProtKB:P0C0S8, ECO:0000269|PubMed:15509584, ECO:0000269|PubMed:15525528, ECO:0000269|PubMed:24352239}.; PTM: Phosphorylation on Ser-2 (H2AS1ph) is enhanced during mitosis. Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses transcription. Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1. Phosphorylation at Thr-121 (H2AT120ph) by DCAF1 is present in the regulatory region of many tumor suppresor genes and down-regulates their transcription. {ECO:0000250|UniProtKB:P0C0S8}.; PTM: Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage. {ECO:0000269|PubMed:16699504}.; PTM: Glutamine methylation at Gln-105 (H2AQ104me) by FBL is specifically dedicated to polymerase I. It is present at 35S ribosomal DNA locus and impairs binding of the FACT complex. {ECO:0000269|PubMed:24352239}.; PTM: Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes. {ECO:0000269|PubMed:21925322}.; PTM: Hydroxybutyrylation of histones is induced by starvation. {ECO:0000269|PubMed:27105115}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}. SUBUNIT: The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. +C0HKE6 H2A1I_MOUSE Histone H2A type 1-I 130 14,135 Chain (1); Cross-link (3); Initiator methionine (1); Modified residue (24); Sequence caution (1) FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. PTM: Deiminated on Arg-4 in granulocytes upon calcium entry. {ECO:0000250|UniProtKB:P0C0S8}.; PTM: Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM27 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is involved in the initiation of both imprinted and random X inactivation. Ubiquitinated H2A is enriched in inactive X chromosome chromatin. Ubiquitination of H2A functions downstream of methylation of 'Lys-27' of histone H3 (H3K27me). H2AK119Ub by RNF2/RING2 can also be induced by ultraviolet and may be involved in DNA repair. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties by the E2 ligase UBE2N and the E3 ligases RNF8 and RNF168, leading to the recruitment of repair proteins to sites of DNA damage. Ubiquitination at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) in response to DNA damage is initiated by RNF168 that mediates monoubiquitination at these 2 sites, and 'Lys-63'-linked ubiquitin are then conjugated to monoubiquitin; RNF8 is able to extend 'Lys-63'-linked ubiquitin chains in vitro. Deubiquitinated by USP51 at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) after damaged DNA is repaired (By similarity). H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination (H2AK13Ub and H2AK15Ub) are distinct events. {ECO:0000250|UniProtKB:P0C0S8, ECO:0000269|PubMed:15509584, ECO:0000269|PubMed:15525528, ECO:0000269|PubMed:24352239}.; PTM: Phosphorylation on Ser-2 (H2AS1ph) is enhanced during mitosis. Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses transcription. Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1. Phosphorylation at Thr-121 (H2AT120ph) by DCAF1 is present in the regulatory region of many tumor suppresor genes and down-regulates their transcription. {ECO:0000250|UniProtKB:P0C0S8, ECO:0000269|PubMed:7217105}.; PTM: Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage. {ECO:0000269|PubMed:16699504}.; PTM: Glutamine methylation at Gln-105 (H2AQ104me) by FBL is specifically dedicated to polymerase I. It is present at 35S ribosomal DNA locus and impairs binding of the FACT complex. {ECO:0000269|PubMed:24352239}.; PTM: Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes. {ECO:0000269|PubMed:21925322}.; PTM: Hydroxybutyrylation of histones is induced by starvation. {ECO:0000269|PubMed:27105115}. SUBCELLULAR LOCATION: Nucleus. Chromosome. SUBUNIT: The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. +Q64522 H2A2B_MOUSE Histone H2A type 2-B (H2a-613A) 130 14,013 Chain (1); Cross-link (3); Initiator methionine (1); Modified residue (21) FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. PTM: Deiminated on Arg-4 in granulocytes upon calcium entry. {ECO:0000250|UniProtKB:P0C0S8}.; PTM: Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM27 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is involved in the initiation of both imprinted and random X inactivation. Ubiquitinated H2A is enriched in inactive X chromosome chromatin. Ubiquitination of H2A functions downstream of methylation of 'Lys-27' of histone H3 (H3K27me). H2AK119Ub by RNF2/RING2 can also be induced by ultraviolet and may be involved in DNA repair. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties by the E2 ligase UBE2N and the E3 ligases RNF8 and RNF168, leading to the recruitment of repair proteins to sites of DNA damage. Ubiquitination at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) in response to DNA damage is initiated by RNF168 that mediates monoubiquitination at these 2 sites, and 'Lys-63'-linked ubiquitin are then conjugated to monoubiquitin; RNF8 is able to extend 'Lys-63'-linked ubiquitin chains in vitro. Deubiquitinated by USP51 at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) after damaged DNA is repaired (By similarity). H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination (H2AK13Ub and H2AK15Ub) are distinct events. {ECO:0000250|UniProtKB:P0C0S8, ECO:0000269|PubMed:15509584, ECO:0000269|PubMed:15525528, ECO:0000269|PubMed:24352239}.; PTM: Phosphorylation on Ser-2 (H2AS1ph) is enhanced during mitosis. Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses transcription. Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1. Phosphorylation at Thr-121 (H2AT120ph) by DCAF1 is present in the regulatory region of many tumor suppresor genes and down-regulates their transcription. {ECO:0000250|UniProtKB:P0C0S8}.; PTM: Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage. {ECO:0000269|PubMed:16699504}.; PTM: Glutamine methylation at Gln-105 (H2AQ104me) by FBL is specifically dedicated to polymerase I. It is present at 35S ribosomal DNA locus and impairs binding of the FACT complex. {ECO:0000269|PubMed:24352239}.; PTM: Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes. {ECO:0000250|UniProtKB:P0C0S8}.; PTM: Hydroxybutyrylation of histones is induced by starvation. {ECO:0000269|PubMed:27105115}. SUBCELLULAR LOCATION: Nucleus. Chromosome. SUBUNIT: The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. +C0HKE8 H2A1O_MOUSE Histone H2A type 1-O 130 14,135 Chain (1); Cross-link (3); Initiator methionine (1); Modified residue (24) FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. PTM: Deiminated on Arg-4 in granulocytes upon calcium entry. {ECO:0000250|UniProtKB:P0C0S8}.; PTM: Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM27 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is involved in the initiation of both imprinted and random X inactivation. Ubiquitinated H2A is enriched in inactive X chromosome chromatin. Ubiquitination of H2A functions downstream of methylation of 'Lys-27' of histone H3 (H3K27me). H2AK119Ub by RNF2/RING2 can also be induced by ultraviolet and may be involved in DNA repair. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties by the E2 ligase UBE2N and the E3 ligases RNF8 and RNF168, leading to the recruitment of repair proteins to sites of DNA damage. Ubiquitination at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) in response to DNA damage is initiated by RNF168 that mediates monoubiquitination at these 2 sites, and 'Lys-63'-linked ubiquitin are then conjugated to monoubiquitin; RNF8 is able to extend 'Lys-63'-linked ubiquitin chains in vitro. Deubiquitinated by USP51 at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) after damaged DNA is repaired (By similarity). H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination (H2AK13Ub and H2AK15Ub) are distinct events. {ECO:0000250|UniProtKB:P0C0S8, ECO:0000269|PubMed:15509584, ECO:0000269|PubMed:15525528, ECO:0000269|PubMed:24352239}.; PTM: Phosphorylation on Ser-2 (H2AS1ph) is enhanced during mitosis. Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses transcription. Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1. Phosphorylation at Thr-121 (H2AT120ph) by DCAF1 is present in the regulatory region of many tumor suppresor genes and down-regulates their transcription. {ECO:0000250|UniProtKB:P0C0S8, ECO:0000269|PubMed:7217105}.; PTM: Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage. {ECO:0000269|PubMed:16699504}.; PTM: Glutamine methylation at Gln-105 (H2AQ104me) by FBL is specifically dedicated to polymerase I. It is present at 35S ribosomal DNA locus and impairs binding of the FACT complex. {ECO:0000269|PubMed:24352239}.; PTM: Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes. {ECO:0000269|PubMed:21925322}.; PTM: Hydroxybutyrylation of histones is induced by starvation. {ECO:0000269|PubMed:27105115}. SUBCELLULAR LOCATION: Nucleus. Chromosome. SUBUNIT: The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. +Q64523 H2A2C_MOUSE Histone H2A type 2-C (H2a-613B) 129 13,988 Chain (1); Cross-link (3); Initiator methionine (1); Modified residue (25) FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. PTM: Deiminated on Arg-4 in granulocytes upon calcium entry. {ECO:0000250|UniProtKB:P0C0S8}.; PTM: Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM27 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is involved in the initiation of both imprinted and random X inactivation. Ubiquitinated H2A is enriched in inactive X chromosome chromatin. Ubiquitination of H2A functions downstream of methylation of 'Lys-27' of histone H3 (H3K27me). H2AK119Ub by RNF2/RING2 can also be induced by ultraviolet and may be involved in DNA repair. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties by the E2 ligase UBE2N and the E3 ligases RNF8 and RNF168, leading to the recruitment of repair proteins to sites of DNA damage. Ubiquitination at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) in response to DNA damage is initiated by RNF168 that mediates monoubiquitination at these 2 sites, and 'Lys-63'-linked ubiquitin are then conjugated to monoubiquitin; RNF8 is able to extend 'Lys-63'-linked ubiquitin chains in vitro. Deubiquitinated by USP51 at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) after damaged DNA is repaired (By similarity). H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination (H2AK13Ub and H2AK15Ub) are distinct events. {ECO:0000250|UniProtKB:P0C0S8, ECO:0000269|PubMed:15509584, ECO:0000269|PubMed:15525528, ECO:0000269|PubMed:24352239}.; PTM: Phosphorylation on Ser-2 (H2AS1ph) is enhanced during mitosis. Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses transcription. Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1. Phosphorylation at Thr-121 (H2AT120ph) by DCAF1 is present in the regulatory region of many tumor suppresor genes and down-regulates their transcription. {ECO:0000250|UniProtKB:P0C0S8}.; PTM: Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage. {ECO:0000269|PubMed:16699504}.; PTM: Glutamine methylation at Gln-105 (H2AQ104me) by FBL is specifically dedicated to polymerase I. It is present at 35S ribosomal DNA locus and impairs binding of the FACT complex. {ECO:0000269|PubMed:24352239}.; PTM: Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes. {ECO:0000269|PubMed:21925322}.; PTM: Hydroxybutyrylation of histones is induced by starvation. {ECO:0000269|PubMed:27105115}. SUBCELLULAR LOCATION: Nucleus. Chromosome. SUBUNIT: The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. +Q8CCK0 H2AW_MOUSE Core histone macro-H2A.2 (Histone macroH2A2) (mH2A2) 372 40,092 Chain (1); Cross-link (1); Domain (2); Sequence conflict (2) FUNCTION: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes where it represses transcription. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. May be involved in stable X chromosome inactivation. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11262398}. Chromosome {ECO:0000269|PubMed:11262398}. Note=Enriched in inactive X chromosome chromatin and in senescence-associated heterochromatin. SUBUNIT: The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. TISSUE SPECIFICITY: Present in liver, kidney and adrenal gland (at protein level). In the liver, present in cells of the bile ducts and parenchymal cells, but not in hepatocytes. In the kidney, present in proximal and distal convoluted tubules and in glomeruli. Present at highest levels in the parietal layer of Bowman capsule. In the adrenal gland, present in the outer cells of the capsule. {ECO:0000269|PubMed:11262398}. +P70696 H2B1A_MOUSE Histone H2B type 1-A (Histone H2B, testis) (Testis-specific histone H2B) 127 14,237 Beta strand (1); Chain (1); Cross-link (4); Helix (4); Initiator methionine (1); Modified residue (30) FUNCTION: Variant histone specifically required to direct the transformation of dissociating nucleosomes to protamine in male germ cells (PubMed:23884607, PubMed:28366643). Entirely replaces classical histone H2B prior nucleosome to protamine transition and probably acts as a nucleosome dissociating factor that creates a more dynamic chromatin, facilitating the large-scale exchange of histones (PubMed:23884607). In condensing spermatids, the heterodimer between H2AFB1 and HIST1H2BA/TH2B is loaded onto the nucleosomes and promotes loading of transition proteins (TNP1 and TNP2) onto the nucleosomes (PubMed:28366643). Inclusion of the H2AFB1-HIST1H2BA/TH2B dimer into chromatin opens the nucleosomes, releasing the nucleosomal DNA ends and allowing the invasion of nucleosomes by transition proteins (TNP1 and TNP2) (PubMed:28366643). Then, transition proteins drive the recruitment and processing of protamines, which are responsible for histone eviction (PubMed:28366643). Also expressed maternally and is present in the female pronucleus, suggesting a similar role in protamine replacement by nucleosomes at fertilization (PubMed:23884607). Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. {ECO:0000269|PubMed:23884607, ECO:0000269|PubMed:28366643}. PTM: Monoubiquitination at Lys-36 by the MSL1/MSL2 dimer is required for histone H3 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) methylation and transcription activation at specific gene loci, such as HOXA9 and MEIS1 loci. Similarly, monoubiquitination of Lys-122 (H2BK120Ub) by the RNF20/40 complex gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation. It also functions cooperatively with the FACT dimer to stimulate elongation by RNA polymerase II. H2BK120Ub also acts as a regulator of mRNA splicing: deubiquitination by USP49 is required for efficient cotranscriptional splicing of a large set of exons (By similarity). {ECO:0000250|UniProtKB:Q96A08}.; PTM: Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes. {ECO:0000269|PubMed:21925322}.; PTM: Acetylated during spermatogenesis. Acetylated form is most abundant in spermatogonia compared to spermatocytes and round spermatids (By similarity). {ECO:0000250|UniProtKB:Q00729}.; PTM: Phosphorylated at Thr-117 in spermatogonia, spermatocytes and round spermatids. {ECO:0000250|UniProtKB:Q00729}.; PTM: Methylated at Lys-118 in spermatogonia, spermatocytes and round spermatids. {ECO:0000250|UniProtKB:Q00729}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23884607}. Chromosome {ECO:0000269|PubMed:23884607}. SUBUNIT: The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers (PubMed:23884607). Interacts with H2AFB1; preferentially dimerizes with H2AFB1 to form nucleosomes (PubMed:28366643). {ECO:0000269|PubMed:23884607, ECO:0000269|PubMed:28366643}. TISSUE SPECIFICITY: Mainly expressed in testis, and the corresponding protein is also present in mature sperm. Also present in metaphase oocytes (at protein level). {ECO:0000269|PubMed:23884607, ECO:0000269|PubMed:8672246}. +Q64525 H2B2B_MOUSE Histone H2B type 2-B (H2b 616) 126 13,920 Chain (1); Cross-link (4); Initiator methionine (1); Modified residue (52) FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. PTM: Monoubiquitination at Lys-35 (H2BK34Ub) by the MSL1/MSL2 dimer is required for histone H3 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) methylation and transcription activation at specific gene loci, such as HOXA9 and MEIS1 loci. Similarly, monoubiquitination at Lys-121 (H2BK120Ub) by the RNF20/40 complex gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation. It also functions cooperatively with the FACT dimer to stimulate elongation by RNA polymerase II. H2BK120Ub also acts as a regulator of mRNA splicing: deubiquitination by USP49 is required for efficient cotranscriptional splicing of a large set of exons (By similarity). {ECO:0000250|UniProtKB:P33778}.; PTM: Phosphorylated on Ser-15 (H2BS14ph) by STK4/MST1 during apoptosis; which facilitates apoptotic chromatin condensation. Also phosphorylated on Ser-15 in response to DNA double strand breaks (DSBs), and in correlation with somatic hypermutation and immunoglobulin class-switch recombination. Phosphorylation at Ser-37 (H2BS36ph) by AMPK in response to stress promotes transcription. {ECO:0000269|PubMed:15197225, ECO:0000269|PubMed:16039583, ECO:0000269|PubMed:20647423}.; PTM: Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes. {ECO:0000269|PubMed:21925322}.; PTM: Hydroxybutyrylation of histones is induced by starvation. {ECO:0000269|PubMed:27105115}. SUBCELLULAR LOCATION: Nucleus. Chromosome. SUBUNIT: The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. +Q6ZWY9 H2B1C_MOUSE Histone H2B type 1-C/E/G 126 13,906 Chain (1); Cross-link (4); Glycosylation (1); Initiator methionine (1); Modified residue (52) FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. PTM: Monoubiquitination at Lys-35 (H2BK34Ub) by the MSL1/MSL2 dimer is required for histone H3 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) methylation and transcription activation at specific gene loci, such as HOXA9 and MEIS1 loci. Similarly, monoubiquitination at Lys-121 (H2BK120Ub) by the RNF20/40 complex gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation. It also functions cooperatively with the FACT dimer to stimulate elongation by RNA polymerase II. H2BK120Ub also acts as a regulator of mRNA splicing: deubiquitination by USP49 is required for efficient cotranscriptional splicing of a large set of exons (By similarity). {ECO:0000250|UniProtKB:P33778}.; PTM: Phosphorylated on Ser-15 (H2BS14ph) by STK4/MST1 during apoptosis; which facilitates apoptotic chromatin condensation. Also phosphorylated on Ser-15 in response to DNA double strand breaks (DSBs), and in correlation with somatic hypermutation and immunoglobulin class-switch recombination. Phosphorylation at Ser-37 (H2BS36ph) by AMPK in response to stress promotes transcription. {ECO:0000269|PubMed:15197225, ECO:0000269|PubMed:16039583, ECO:0000269|PubMed:20647423}.; PTM: GlcNAcylation at Ser-113 promotes monoubiquitination of Lys-121. It fluctuates in response to extracellular glucose, and associates with transcribed genes (By similarity). {ECO:0000250|UniProtKB:P62807}.; PTM: Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes. {ECO:0000269|PubMed:21925322}.; PTM: Hydroxybutyrylation of histones is induced by starvation. {ECO:0000269|PubMed:27105115}. SUBCELLULAR LOCATION: Nucleus. Chromosome. SUBUNIT: The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. +P84244 H33_MOUSE Histone H3.3 136 15,328 Beta strand (2); Chain (1); Frameshift (3); Helix (4); Initiator methionine (1); Modified residue (88); Sequence conflict (4); Site (1) FUNCTION: Variant histone H3 which replaces conventional H3 in a wide range of nucleosomes in active genes. Constitutes the predominant form of histone H3 in non-dividing cells and is incorporated into chromatin independently of DNA synthesis. Deposited at sites of nucleosomal displacement throughout transcribed genes, suggesting that it represents an epigenetic imprint of transcriptionally active chromatin. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. {ECO:0000250|UniProtKB:P84243}. PTM: Acetylation is generally linked to gene activation. Acetylation on Lys-10 (H3K9ac) impairs methylation at Arg-9 (H3R8me2s). Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac) favors methylation at Arg-18 (H3R17me). Acetylation at Lys-123 (H3K122ac) by EP300/p300 plays a central role in chromatin structure: localizes at the surface of the histone octamer and stimulates transcription, possibly by promoting nucleosome instability. {ECO:0000269|PubMed:11751582, ECO:0000269|PubMed:12498683, ECO:0000269|PubMed:13678296, ECO:0000269|PubMed:15485929, ECO:0000269|PubMed:15616592, ECO:0000269|PubMed:17194708}.; PTM: Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by PADI4 impairs methylation and represses transcription. {ECO:0000269|PubMed:11751582, ECO:0000269|PubMed:12498683, ECO:0000269|PubMed:15339660, ECO:0000269|PubMed:15485929, ECO:0000269|PubMed:15616592}.; PTM: Asymmetric dimethylation at Arg-18 (H3R17me2a) by CARM1 is linked to gene activation. Symmetric dimethylation at Arg-9 (H3R8me2s) by PRMT5 is linked to gene repression. Asymmetric dimethylation at Arg-3 (H3R2me2a) by PRMT6 is linked to gene repression and is mutually exclusive with H3 Lys-5 methylation (H3K4me2 and H3K4me3). H3R2me2a is present at the 3' of genes regardless of their transcription state and is enriched on inactive promoters, while it is absent on active promoters. {ECO:0000250|UniProtKB:P84243}.; PTM: Specifically enriched in modifications associated with active chromatin such as methylation at Lys-5 (H3K4me), Lys-37 and Lys-80. Methylation at Lys-5 (H3K4me) facilitates subsequent acetylation of H3 and H4. Methylation at Lys-80 (H3K79me) is associated with DNA double-strand break (DSB) responses and is a specific target for TP53BP1. Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me), which are linked to gene repression, are underrepresented. Methylation at Lys-10 (H3K9me) is a specific target for HP1 proteins (CBX1, CBX3 and CBX5) and prevents subsequent phosphorylation at Ser-11 (H3S10ph) and acetylation of H3 and H4. Methylation at Lys-5 (H3K4me) and Lys-80 (H3K79me) require preliminary monoubiquitination of H2B at 'Lys-120'. Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are enriched in inactive X chromosome chromatin. Monomethylation at Lys-57 (H3K56me1) by EHMT2/G9A in G1 phase promotes interaction with PCNA and is required for DNA replication. {ECO:0000269|PubMed:10464286, ECO:0000269|PubMed:11856369, ECO:0000269|PubMed:13678296, ECO:0000269|PubMed:15485929, ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:15735677, ECO:0000269|PubMed:15870105, ECO:0000269|PubMed:17189264, ECO:0000269|PubMed:17194708}.; PTM: Phosphorylated at Thr-4 (H3T3ph) by HASPIN during prophase and dephosphorylated during anaphase. Phosphorylation at Ser-11 (H3S10ph) by AURKB is crucial for chromosome condensation and cell-cycle progression during mitosis and meiosis. In addition phosphorylation at Ser-11 (H3S10ph) by RPS6KA4 and RPS6KA5 is important during interphase because it enables the transcription of genes following external stimulation, like mitogens, stress, growth factors or UV irradiation and result in the activation of genes, such as c-fos and c-jun. Phosphorylation at Ser-11 (H3S10ph), which is linked to gene activation, prevents methylation at Lys-10 (H3K9me) but facilitates acetylation of H3 and H4. Phosphorylation at Ser-11 (H3S10ph) by AURKB mediates the dissociation of HP1 proteins (CBX1, CBX3 and CBX5) from heterochromatin. Phosphorylation at Ser-11 (H3S10ph) is also an essential regulatory mechanism for neoplastic cell transformation. Phosphorylated at Ser-29 (H3S28ph) by MAP3K20 isoform 1, RPS6KA5 or AURKB during mitosis or upon ultraviolet B irradiation. Phosphorylation at Thr-7 (H3T6ph) by PRKCB is a specific tag for epigenetic transcriptional activation that prevents demethylation of Lys-5 (H3K4me) by LSD1/KDM1A. At centromeres, specifically phosphorylated at Thr-12 (H3T11ph) from prophase to early anaphase, by DAPK3 and PKN1. Phosphorylation at Thr-12 (H3T11ph) by PKN1 is a specific tag for epigenetic transcriptional activation that promotes demethylation of Lys-10 (H3K9me) by KDM4C/JMJD2C. Phosphorylation at Tyr-42 (H3Y41ph) by JAK2 promotes exclusion of CBX5 (HP1 alpha) from chromatin. Phosphorylation on Ser-32 (H3S31ph) is specific to regions bordering centromeres in metaphase chromosomes. metaphase chromosomes. {ECO:0000269|PubMed:10464286, ECO:0000269|PubMed:11441012, ECO:0000269|PubMed:11856369, ECO:0000269|PubMed:13678296, ECO:0000269|PubMed:15485929, ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:15684425, ECO:0000269|PubMed:15735677, ECO:0000269|PubMed:15870105, ECO:0000269|PubMed:17194708}.; PTM: Ubiquitinated. Monoubiquitinated by RAG1 in lymphoid cells, monoubiquitination is required for V(D)J recombination. {ECO:0000305|PubMed:20122409}.; PTM: Lysine deamination at Lys-5 (H3K4all) to form allysine is mediated by LOXL2. Allysine formation by LOXL2 only takes place on H3K4me3 and results in gene repression. {ECO:0000250|UniProtKB:P84243}.; PTM: Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes. {ECO:0000269|PubMed:21925322}.; PTM: Butyrylation of histones marks active promoters and competes with histone acetylation. It is present during late spermatogenesis. {ECO:0000269|PubMed:27105113}.; PTM: Hydroxybutyrylation of histones is induced by starvation. It is linked to gene activation and may replace histone acetylation on the promoter of specific genes in response to fasting. {ECO:0000269|PubMed:27105115}.; PTM: Succinylation at Lys-80 (H3K79succ) by KAT2A takes place with a maximum frequency around the transcription start sites of genes. It gives a specific tag for epigenetic transcription activation. {ECO:0000250|UniProtKB:P84243}.; PTM: Serine ADP-ribosylation constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage. Serine ADP-ribosylation at Ser-11 (H3S10ADPr) is mutually exclusive with phosphorylation at Ser-11 (H3S10ph) and impairs acetylation at Lys-10 (H3K9ac). {ECO:0000250|UniProtKB:P68431}. SUBCELLULAR LOCATION: Nucleus. Chromosome. SUBUNIT: The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. Interacts with HIRA, a chaperone required for its incorporation into nucleosomes. Interacts with ZMYND11; when trimethylated at 'Lys-36' (H3.3K36me3). {ECO:0000250|UniProtKB:P84243}. DOMAIN: Specific interaction of trimethylated form at 'Lys-36' (H3.3K36me3) with ZMYND11 is mediated by the encapsulation of Ser-32 residue with a composite pocket formed by the tandem bromo-PWWP domains (By similarity). Interacts with ZMYND11; when trimethylated at 'Lys-36' (H3.3K36me3). {ECO:0000250|UniProtKB:P84243}. +P02301 H3C_MOUSE Histone H3.3C (Embryonic) 136 15,315 Chain (1); Initiator methionine (1); Modified residue (75); Sequence conflict (13) FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. PTM: Acetylation is generally linked to gene activation. Acetylation on Lys-10 (H3K9ac) impairs methylation at Arg-9 (H3R8me2s). Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac) favors methylation at Arg-18 (H3R17me). Acetylation at Lys-123 (H3K122ac) by EP300/p300 plays a central role in chromatin structure: localizes at the surface of the histone octamer and stimulates transcription, possibly by promoting nucleosome instability (By similarity). {ECO:0000250|UniProtKB:P84243}.; PTM: Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by PADI4 impairs methylation and represses transcription. {ECO:0000250|UniProtKB:P84243}.; PTM: Butyrylation of histones marks active promoters and competes with histone acetylation. It is present during late spermatogenesis. {ECO:0000250|UniProtKB:P68433}.; PTM: Asymmetric dimethylation at Arg-18 (H3R17me2a) by CARM1 is linked to gene activation. Symmetric dimethylation at Arg-9 (H3R8me2s) by PRMT5 is linked to gene repression (By similarity). {ECO:0000250|UniProtKB:P84243}.; PTM: Methylation at Lys-5 (H3K4me), Lys-37 and Lys-80 are linked to gene activation. Methylation at Lys-5 (H3K4me) facilitates subsequent acetylation of H3 and H4. Methylation at Lys-80 is associated with DNA double-strand break (DSB) responses and is a specific target for TP53BP1. Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are linked to gene repression. Methylation at Lys-10 (H3K9me) is a specific target for HP1 proteins (CBX1, CBX3 and CBX5) and prevents subsequent phosphorylation at Ser-11 (H3S10ph) and acetylation of H3 and H4. Methylation at Lys-5 (H3K4me) and Lys-80 require preliminary monoubiquitination of H2B at 'Lys-120'. Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are enriched in inactive X chromosome chromatin. Monomethylation at Lys-57 (H3K56me1) by EHMT2/G9A in G1 phase promotes interaction with PCNA and is required for DNA replication (By similarity). {ECO:0000250|UniProtKB:P84243}.; PTM: Phosphorylated at Thr-4 (H3T3ph) by HASPIN during prophase and dephosphorylated during anaphase. Phosphorylation at Ser-11 (H3S10ph) by AURKB is crucial for chromosome condensation and cell-cycle progression during mitosis and meiosis. In addition phosphorylation at Ser-11 (H3S10ph) by RPS6KA4 and RPS6KA5 is important during interphase because it enables the transcription of genes following external stimulation, like mitogens, stress, growth factors or UV irradiation and result in the activation of genes, such as c-fos and c-jun. Phosphorylation at Ser-11 (H3S10ph), which is linked to gene activation, prevents methylation at Lys-10 (H3K9me) but facilitates acetylation of H3 and H4. Phosphorylation at Ser-11 (H3S10ph) by AURKB mediates the dissociation of HP1 proteins (CBX1, CBX3 and CBX5) from heterochromatin. Phosphorylation at Ser-11 (H3S10ph) is also an essential regulatory mechanism for neoplastic cell transformation. Phosphorylated at Ser-29 (H3S28ph) by MAP3K20 isoform 1, RPS6KA5 or AURKB during mitosis or upon ultraviolet B irradiation. Phosphorylation at Thr-7 (H3T6ph) by PRKCB is a specific tag for epigenetic transcriptional activation that prevents demethylation of Lys-5 (H3K4me) by LSD1/KDM1A. At centromeres, specifically phosphorylated at Thr-12 (H3T11ph) from prophase to early anaphase, by DAPK3 and PKN1. Phosphorylation at Thr-12 (H3T11ph) by PKN1 is a specific tag for epigenetic transcriptional activation that promotes demethylation of Lys-10 (H3K9me) by KDM4C/JMJD2C. Phosphorylation at Tyr-42 (H3Y41ph) by JAK2 promotes exclusion of CBX5 (HP1 alpha) from chromatin (By similarity). {ECO:0000250|UniProtKB:P84243}.; PTM: Lysine deamination at Lys-5 (H3K4all) to form allysine is mediated by LOXL2. Allysine formation by LOXL2 only takes place on H3K4me3 and results in gene repression (By similarity). {ECO:0000250|UniProtKB:P84243}.; PTM: Succinylation at Lys-80 (H3K79succ) by KAT2A takes place with a maximum frequency around the transcription start sites of genes. It gives a specific tag for epigenetic transcription activation. {ECO:0000250|UniProtKB:P68431}.; PTM: Serine ADP-ribosylation constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage. Serine ADP-ribosylation at Ser-11 (H3S10ADPr) is mutually exclusive with phosphorylation at Ser-11 (H3S10ph) and impairs acetylation at Lys-10 (H3K9ac). {ECO:0000250|UniProtKB:P68431}. SUBCELLULAR LOCATION: Nucleus. Chromosome. SUBUNIT: The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. +P01756 HVM12_MOUSE Ig heavy chain V region MOPC 104E 117 12,983 Beta strand (10); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (1); Helix (3); Non-terminal residue (1); Turn (1) +P01757 HVM13_MOUSE Ig heavy chain V region J558 117 13,025 Beta strand (9); Chain (1); Disulfide bond (1); Domain (1); Helix (2); Non-terminal residue (1); Turn (3) +P09633 HXC9_MOUSE Homeobox protein Hox-C9 (Homeobox protein Hox-3.2) 260 29,234 Chain (1); DNA binding (1); Modified residue (1) FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with Geminin/GMNN, which inhibits transcriptional activity. {ECO:0000250}. +P01795 HVM26_MOUSE Ig heavy chain V region M167 144 16,219 Chain (1); Domain (1); Non-terminal residue (1); Sequence conflict (1); Signal peptide (1) +P01799 HVM30_MOUSE Ig heavy chain V-III region ABE-47N 113 12,675 Chain (1); Disulfide bond (1); Domain (1); Non-terminal residue (1) +P06327 HVM52_MOUSE Ig heavy chain V region VH558 A1/A4 117 12,971 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (5); Signal peptide (1) +P10284 HXB4_MOUSE Homeobox protein Hox-B4 (Homeobox protein Hox-2.6) 250 27,519 Chain (1); Compositional bias (2); DNA binding (1); Modified residue (1); Motif (1); Sequence conflict (1) FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. SUBCELLULAR LOCATION: Nucleus. +P31245 HXA2_MOUSE Homeobox protein Hox-A2 (Homeobox protein Hox-1.11) (Hox1.11) 372 40,793 Chain (1); DNA binding (1); Motif (1) FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. SUBCELLULAR LOCATION: Nucleus. +P20615 HXB9_MOUSE Homeobox protein Hox-B9 (Homeobox protein Hox-2.5) 250 28,015 Chain (1); Cross-link (1); DNA binding (1); Modified residue (1); Sequence conflict (4) FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. SUBCELLULAR LOCATION: Nucleus. +P01726 LV1D_MOUSE Ig lambda-1 chain V region H2020 129 13,465 Beta strand (10); Chain (1); Domain (1); Helix (2); Modified residue (1); Non-terminal residue (1); Signal peptide (1); Turn (2) +P46694 IEX1_MOUSE Radiation-inducible immediate-early gene IEX-1 (Immediate early protein GLY96) (Immediate early response 3 protein) 153 16,875 Chain (1); Glycosylation (1); Modified residue (1); Topological domain (2); Transmembrane (1) TRANSMEM 86 102 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 85 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 103 153 Extracellular. {ECO:0000255}. FUNCTION: May play a role in the ERK signaling pathway by inhibiting the dephosphorylation of ERK by phosphatase PP2A-PPP2R5C holoenzyme. Acts also as an ERK downstream effector mediating survival (By similarity). As a member of the NUPR1/RELB/IER3 survival pathway, may allow the development of pancreatic intraepithelial neoplasias. {ECO:0000250, ECO:0000269|PubMed:22565310}. PTM: Glycosylated. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. SUBUNIT: Interacts with the PPP2R5C-PP2A holoenzyme and ERK kinases; regulates ERK dephosphorylation. {ECO:0000250}. TISSUE SPECIFICITY: Expressed predominantly in the lung, testes and the uterus. +Q9WTL7 LYPA2_MOUSE Acyl-protein thioesterase 2 (APT-2) (EC 3.1.2.-) (Lysophospholipase 2) (Lysophospholipase II) (LPL-II) (LysoPLA II) (mLyso II) 231 24,794 Active site (3); Chain (1); Lipidation (1); Modified residue (1) FUNCTION: Hydrolyzes fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins, GAP43, ZDHHC6 or HRAS. Deacylates GAP43. Mediates depalmitoylation of ZDHHC6 (By similarity). Has lysophospholipase activity (PubMed:10064901). {ECO:0000250|UniProtKB:O95372, ECO:0000269|PubMed:10064901}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O95372}. TISSUE SPECIFICITY: Ubiquitous; detected at low levels. {ECO:0000269|PubMed:10064901}. +Q8BPP5 LYPD6_MOUSE Ly6/PLAUR domain-containing protein 6 171 19,065 Chain (1); Domain (1); Glycosylation (2); Signal peptide (1) FUNCTION: Acts as a modulator of nicotinic acetylcholine receptors (nAChRs) function in the brain. Enhances nicotine-induced Ca(2+) influx through nAChRs (PubMed:19403274). Acts as a positive regulator of Wnt/beta-catenin signaling (By similarity). {ECO:0000250|UniProtKB:Q66IA6, ECO:0000269|PubMed:19403274}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q86Y78}. Cytoplasm {ECO:0000250|UniProtKB:Q86Y78}. Cell membrane {ECO:0000250|UniProtKB:Q66IA6}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q66IA6}. Cell junction, synapse, synaptosome {ECO:0000250|UniProtKB:D3ZTT2}. Membrane raft {ECO:0000250|UniProtKB:Q66IA6}. SUBUNIT: Interacts with nicotinic acetylcholine receptors (nAChRs) including CHRNA3, CHRNA4, CHRNA5, CHRNA6, CHRNA7, CHRNB2 and CHRNB4. {ECO:0000250|UniProtKB:Q86Y78}. TISSUE SPECIFICITY: Highly expressed in the brain and spinal cord, as well as dorsal root and trigeminal ganglia. {ECO:0000269|PubMed:19403274}. +Q3UFF7 LYPL1_MOUSE Lysophospholipase-like protein 1 (EC 3.1.2.-) 239 26,354 Active site (3); Chain (1); Initiator methionine (1); Modified residue (1); Sequence conflict (3) FUNCTION: Has depalmitoylating activity toward KCNMA1. Does not exhibit phospholipase nor triacylglycerol lipase activity, able to hydrolyze only short chain substrates due to its shallow active site (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +Q80WJ7 LYRIC_MOUSE Protein LYRIC (3D3/LYRIC) (Lysine-rich CEACAM1 co-isolated protein) (Metadherin) (Metastasis adhesion protein) 579 63,846 Chain (1); Compositional bias (3); Modified residue (16); Region (4); Sequence conflict (4); Topological domain (2); Transmembrane (1) TRANSMEM 49 69 Helical. {ECO:0000255}. TOPO_DOM 1 48 Lumenal. {ECO:0000255}.; TOPO_DOM 70 579 Cytoplasmic. {ECO:0000255}. FUNCTION: Downregulates SLC1A2/EAAT2 promoter activity when expressed ectopically. Activates the nuclear factor kappa-B (NF-kappa-B) transcription factor. Promotes anchorage-independent growth of immortalized melanocytes and astrocytes which is a key component in tumor cell expansion. Promotes lung metastasis and also has an effect on bone and brain metastasis, possibly by enhancing the seeding of tumor cells to the target organ endothelium. Induces chemoresistance (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cell junction, tight junction {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=In epithelial cells, recruited to tight junctions (TJ) during the maturation of the TJ complexes. A nucleolar staining may be due to nuclear targeting of an isoform lacking the transmembrane domain. TNF-alpha causes translocation from the cytoplasm to the nucleus (By similarity). {ECO:0000250}. SUBUNIT: Interacts with BCCIP, CREBBP/CBP and RELA/p65. {ECO:0000250}. TISSUE SPECIFICITY: In the mammary gland, expressed at the apical surface of epithelial cells lining ducts, as well as in the mammary fat pad. Not detected in the spleen, kidney, lung, or skin; minute amounts seen in the liver. Expressed in Purkinje neurons in the early postnatal and adult cerebellum. Overexpressed in mammary tumors (at protein level). {ECO:0000269|PubMed:15093543}. +Q9CQB7 LYRM1_MOUSE LYR motif-containing protein 1 122 14,224 Chain (1) FUNCTION: May promote cell proliferation and inhibition of apoptosis of preadipocytes. {ECO:0000250}. +Q8R412 IF27A_MOUSE Interferon alpha-inducible protein 27-like protein 2A (Interferon-stimulated gene 12 protein) (ISG12) 90 7,929 Chain (1); Signal peptide (1); Transmembrane (2) TRANSMEM 28 48 Helical. {ECO:0000255}.; TRANSMEM 67 89 Helical. {ECO:0000255}. FUNCTION: May be involved in the interferon-induced negative regulation of the transcriptional activity of NR4A1, NR4A2 and NR4A3 through the enhancement of XPO1-mediated nuclear export of these nuclear receptors (PubMed:22427340). Through the regulation of NR4A1 transcriptional activity, may play a role in the vascular response to injury (PubMed:22427340). {ECO:0000269|PubMed:22427340}. SUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000305|PubMed:22427340}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Homodimer (By similarity). Interacts with SKP2 (By similarity). Interacts with NR4A1 (By similarity). May interact with BCL2 (By similarity). {ECO:0000250|UniProtKB:P40305}. +P49138 MAPK2_MOUSE MAP kinase-activated protein kinase 2 (MAPK-activated protein kinase 2) (MAPKAP kinase 2) (MAPKAP-K2) (MAPKAPK-2) (MK-2) (MK2) (EC 2.7.11.1) 386 44,050 Active site (1); Binding site (1); Chain (1); Compositional bias (3); Cross-link (1); Domain (1); Modified residue (4); Motif (4); Mutagenesis (6); Nucleotide binding (1); Region (3); Sequence conflict (1) FUNCTION: Stress-activated serine/threonine-protein kinase involved in cytokine production, endocytosis, reorganization of the cytoskeleton, cell migration, cell cycle control, chromatin remodeling, DNA damage response and transcriptional regulation. Following stress, it is phosphorylated and activated by MAP kinase p38-alpha/MAPK14, leading to phosphorylation of substrates. Phosphorylates serine in the peptide sequence, Hyd-X-R-X(2)-S, where Hyd is a large hydrophobic residue. Phosphorylates ALOX5, CDC25B, CDC25C, CEP131, ELAVL1, HNRNPA0, HSP27/HSPB1, KRT18, KRT20, LIMK1, LSP1, PABPC1, PARN, PDE4A, RCSD1, RPS6KA3, TAB3 and TTP/ZFP36. Phosphorylates HSF1; leading to the interaction with HSP90 proteins and inhibiting HSF1 homotrimerization, DNA-binding and transactivation activities (By similarity). Mediates phosphorylation of HSP27/HSPB1 in response to stress, leading to dissociation of HSP27/HSPB1 from large small heat-shock protein (sHsps) oligomers and impairment of their chaperone activities and ability to protect against oxidative stress effectively. Involved in inflammatory response by regulating tumor necrosis factor (TNF) and IL6 production post-transcriptionally: acts by phosphorylating AU-rich elements (AREs)-binding proteins ELAVL1, HNRNPA0, PABPC1 and TTP/ZFP36, leading to regulation of the stability and translation of TNF and IL6 mRNAs. Phosphorylation of TTP/ZFP36, a major post-transcriptional regulator of TNF, promotes its binding to 14-3-3 proteins and reduces its ARE mRNA affinity leading to inhibition of dependent degradation of ARE-containing transcripts. Phosphorylates CEP131 in response to cellular stress following ultraviolet irradiation which promotes binding of CEP131 to 14-3-3 proteins and inhibits formation of novel centriolar satellites (By similarity). Also involved in late G2/M checkpoint following DNA damage through a process of post-transcriptional mRNA stabilization: following DNA damage, relocalizes from nucleus to cytoplasm and phosphorylates HNRNPA0 and PARN, leading to stabilization of GADD45A mRNA. Involved in toll-like receptor signaling pathway (TLR) in dendritic cells: required for acute TLR-induced macropinocytosis by phosphorylating and activating RPS6KA3. {ECO:0000250|UniProtKB:P49137, ECO:0000269|PubMed:10559880, ECO:0000269|PubMed:12456657, ECO:0000269|PubMed:14688255, ECO:0000269|PubMed:15850461, ECO:0000269|PubMed:17906627, ECO:0000269|PubMed:20724476, ECO:0000269|PubMed:21323643, ECO:0000269|PubMed:8093612}. PTM: Sumoylation inhibits the protein kinase activity. {ECO:0000250}.; PTM: Phosphorylated and activated by MAP kinase p38-alpha/MAPK14 at Thr-208; Ser-258 and Thr-320. {ECO:0000269|PubMed:7592979, ECO:0000269|PubMed:9628873}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Phosphorylation and subsequent activation releases the autoinhibitory helix, resulting in the export from the nucleus into the cytoplasm. SUBUNIT: Heterodimer with p38-alpha/MAPK14; this heterodimer forms a stable complex: molecules are positioned 'face to face' so that the ATP-binding sites of both kinases are at the heterodimer interface. Interacts with PHC2. Interacts with HSF1. {ECO:0000250|UniProtKB:P49137}. TISSUE SPECIFICITY: Ubiquitously expressed (at protein level). {ECO:0000269|PubMed:17030606}. +Q3UMW7 MAPK3_MOUSE MAP kinase-activated protein kinase 3 (MAPK-activated protein kinase 3) (MAPKAP kinase 3) (MAPKAP-K3) (MAPKAPK-3) (MK-3) (EC 2.7.11.1) 384 43,293 Active site (1); Alternative sequence (4); Binding site (1); Chain (1); Domain (1); Modified residue (5); Motif (3); Mutagenesis (1); Nucleotide binding (1); Region (2); Sequence conflict (1) FUNCTION: Stress-activated serine/threonine-protein kinase involved in cytokines production, endocytosis, cell migration, chromatin remodeling and transcriptional regulation. Following stress, it is phosphorylated and activated by MAP kinase p38-alpha/MAPK14, leading to phosphorylation of substrates. Phosphorylates serine in the peptide sequence, Hyd-X-R-X(2)-S, where Hyd is a large hydrophobic residue. MAPKAPK2 and MAPKAPK3, share the same function and substrate specificity, but MAPKAPK3 kinase activity and level in protein expression are lower compared to MAPKAPK2. Phosphorylates HSP27/HSPB1, KRT18, KRT20, RCSD1, RPS6KA3, TAB3 and TTP/ZFP36. Mediates phosphorylation of HSP27/HSPB1 in response to stress, leading to dissociate HSP27/HSPB1 from large small heat-shock protein (sHsps) oligomers and impair their chaperone activities and ability to protect against oxidative stress effectively. Involved in inflammatory response by regulating tumor necrosis factor (TNF) and IL6 production post-transcriptionally: acts by phosphorylating AU-rich elements (AREs)-binding proteins, such as TTP/ZFP36, leading to regulate the stability and translation of TNF and IL6 mRNAs. Phosphorylation of TTP/ZFP36, a major post-transcriptional regulator of TNF, promotes its binding to 14-3-3 proteins and reduces its ARE mRNA affinity leading to inhibition of dependent degradation of ARE-containing transcript. Involved in toll-like receptor signaling pathway (TLR) in dendritic cells: required for acute TLR-induced macropinocytosis by phosphorylating and activating RPS6KA3. Also acts as a modulator of Polycomb-mediated repression. {ECO:0000269|PubMed:17906627, ECO:0000269|PubMed:20724476}. PTM: Phosphorylated and activated by MAPK1/ERK2 and MAPK3/ERK1 (By similarity). Phosphorylated and activated by MAP kinase p38-alpha/MAPK14 at Thr-201, Ser-251 and Thr-313. Isoform 3 is degraded following phosphorylation at Thr-203. {ECO:0000250, ECO:0000269|PubMed:17030606, ECO:0000269|PubMed:20570725}. SUBCELLULAR LOCATION: Isoform 1: Nucleus. Cytoplasm. Note=Predominantly located in the nucleus, when activated it translocates to the cytoplasm.; SUBCELLULAR LOCATION: Isoform 3: Nucleus. Cytoplasm. Note=Localizes throughout the cell. Degraded in response to osmotic stress. SUBUNIT: Heterodimer with p38-alpha/MAPK14. The heterodimer with p38-alpha/MAPK14 forms a stable complex: molecules are positioned 'face to face' so that the ATP-binding sites of both kinases are at the heterodimer interface. Interacts with TCF3 and with polycomb proteins, such as PCH2 and BMI1/PCGF4 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed (at protein level). Isoform 3 is expressed in skeletal muscles and heart. {ECO:0000269|PubMed:17030606}. +O54992 MAPK5_MOUSE MAP kinase-activated protein kinase 5 (MAPK-activated protein kinase 5) (MAPKAP kinase 5) (MAPKAPK-5) (EC 2.7.11.1) 473 54,152 Active site (1); Alternative sequence (3); Binding site (1); Chain (1); Coiled coil (1); Domain (1); Modified residue (4); Mutagenesis (6); Nucleotide binding (1) FUNCTION: Tumor suppressor serine/threonine-protein kinase involved in mTORC1 signaling and post-transcriptional regulation. Phosphorylates FOXO3, ERK3/MAPK6, ERK4/MAPK4, HSP27/HSPB1, p53/TP53 and RHEB. Acts as a tumor suppressor by mediating Ras-induced senescence and phosphorylating p53/TP53. Involved in post-transcriptional regulation of MYC by mediating phosphorylation of FOXO3: phosphorylation of FOXO3 leads to promote nuclear localization of FOXO3, enabling expression of miR-34b and miR-34c, 2 post-transcriptional regulators of MYC that bind to the 3'UTR of MYC transcript and prevent MYC translation. Acts as a negative regulator of mTORC1 signaling by mediating phosphorylation and inhibition of RHEB. Part of the atypical MAPK signaling via its interaction with ERK3/MAPK6 or ERK4/MAPK4: the precise role of the complex formed with ERK3/MAPK6 or ERK4/MAPK4 is still unclear, but the complex follows a complex set of phosphorylation events: upon interaction with atypical MAPK (ERK3/MAPK6 or ERK4/MAPK4), ERK3/MAPK6 (or ERK4/MAPK4) is phosphorylated and then mediates phosphorylation and activation of MAPKAPK5, which in turn phosphorylates ERK3/MAPK6 (or ERK4/MAPK4). Mediates phosphorylation of HSP27/HSPB1 in response to PKA/PRKACA stimulation, inducing F-actin rearrangement. {ECO:0000269|PubMed:15538386, ECO:0000269|PubMed:15577943, ECO:0000269|PubMed:16973613, ECO:0000269|PubMed:17254968, ECO:0000269|PubMed:21336308, ECO:0000269|PubMed:21575178}. PTM: Phosphorylated on Thr-182 ERK3/MAPK6 or ERK4/MAPK4; which is the regulatory phosphorylation site and is located on the T-loop/loop 12, leading to activation. Phosphorylation at Thr-182 by p38-alpha/MAPK14, p38-beta/MAPK11 is subject to debate. Phosphorylated at Ser-115 by PKA/PRKACA, leading to localization to the cytoplasm. Autophosphorylated. {ECO:0000269|PubMed:15538386, ECO:0000269|PubMed:15577943, ECO:0000269|PubMed:20734105, ECO:0000269|PubMed:9480836}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Translocates to the cytoplasm following phosphorylation and activation. Interaction with ERK3/MAPK6 or ERK4/MAPK4 and phosphorylation at Thr-182, activates the protein kinase activity, followed by translocation to the cytoplasm. Phosphorylation by PKA/PRKACA at Ser-115 also induces nuclear export. SUBUNIT: Interacts with SQSTM1 (By similarity). Interacts with ERK3/MAPK6 and ERK4/MAPK4 (via FRIEDE motif); the interaction is direct. Interacts with YWHAE; the interaction prevents phosphorylation of HSP27/HSPB1 leading to disrupt F-actin polymerization. {ECO:0000250, ECO:0000269|PubMed:15538386, ECO:0000269|PubMed:15577943, ECO:0000269|PubMed:16973613, ECO:0000269|PubMed:18248330, ECO:0000269|PubMed:18720373, ECO:0000269|PubMed:19473979}. TISSUE SPECIFICITY: Expressed ubiquitously. {ECO:0000269|PubMed:9480836}. +Q9CW42 MARC1_MOUSE Mitochondrial amidoxime-reducing component 1 (mARC1) (EC 1.-.-.-) (Molybdenum cofactor sulfurase C-terminal domain-containing protein 1) (MOSC domain-containing protein 1) (Moco sulfurase C-terminal domain-containing protein 1) 340 37,979 Chain (1); Domain (1); Erroneous initiation (1); Frameshift (1); Initiator methionine (1); Lipidation (1); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 25 44 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 2 24 Mitochondrial matrix. {ECO:0000250}.; TOPO_DOM 45 340 Cytoplasmic. {ECO:0000250}. FUNCTION: As a component of an N-hydroxylated prodrug-converting complex required to reduce N-hydroxylated prodrugs, such as benzamidoxime. Also able to reduce N(omega)-hydroxy-L-arginine (NOHA) and N(omega)-hydroxy-N(delta)-methyl-L-arginine (NHAM) into L-arginine and N(delta)-methyl-L-arginine, respectively (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Membrane {ECO:0000250|UniProtKB:Q5VT66}; Lipid-anchor {ECO:0000250|UniProtKB:Q5VT66}. Note=Mitochondrial import is mediated by AA 1-44 and requires ATP. {ECO:0000250}. SUBUNIT: Component of a complex composed of cytochrome b5, NADH-cytochrome b5 reductase and MARC1. {ECO:0000250}. +Q922Q1 MARC2_MOUSE Mitochondrial amidoxime reducing component 2 (mARC2) (EC 1.-.-.-) (Molybdenum cofactor sulfurase C-terminal domain-containing protein 2) (MOSC domain-containing protein 2) (Moco sulfurase C-terminal domain-containing protein 2) 338 38,194 Chain (1); Cross-link (8); Domain (1); Modified residue (1); Transit peptide (1) FUNCTION: As a component of the benzamidoxime prodrug-converting complex required to reduce N-hydroxylated prodrugs, such as benzamidoxime. Also able to reduce N(omega)-hydroxy-L-arginine (NOHA) and N(omega)-hydroxy-N(delta)-methyl-L-arginine (NHAM) into L-arginine and N(delta)-methyl-L-arginine, respectively (By similarity). {ECO:0000250}. PTM: Ubiquitinated by PRKN during mitophagy, leading to its degradation and enhancement of mitophagy. Deubiquitinated by USP30. {ECO:0000250|UniProtKB:Q969Z3}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:P0C2C3}; Peripheral membrane protein {ECO:0000250|UniProtKB:P0C2C3}. Peroxisome {ECO:0000269|PubMed:17768142}. SUBUNIT: Component of a complex composed of cytochrome b5, NADH-cytochrome b5 reductase (CYB5R3) and MARC2. {ECO:0000250}. +Q60754 MARCO_MOUSE Macrophage receptor MARCO (Macrophage receptor with collagenous structure) 518 52,730 Beta strand (5); Chain (1); Disulfide bond (3); Domain (2); Glycosylation (2); Helix (3); Topological domain (2); Transmembrane (1) TRANSMEM 49 69 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 48 Cytoplasmic. {ECO:0000269|PubMed:7867067}.; TOPO_DOM 70 518 Extracellular. {ECO:0000269|PubMed:7867067}. FUNCTION: Pattern recognition receptor (PRR) which binds Gram-positive and Gram-negative bacteria (PubMed:7867067). Also plays a role in binding of unopsonized particles by alveolar macrophages (By similarity). Binds to the secretoglobin SCGB3A2 (By similarity). {ECO:0000250|UniProtKB:Q9UEW3, ECO:0000250|UniProtKB:Q9WUB9, ECO:0000269|PubMed:7867067}. PTM: N-glycosylated. {ECO:0000269|PubMed:7867067}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7867067}; Single-pass type II membrane protein {ECO:0000305}. SUBUNIT: Homotrimer; disulfide-linked (PubMed:7867067). Trimers may assemble in larger oligomers thus resulting in the creation of a large surface capable of interacting with very large ligands (PubMed:17405873). {ECO:0000269|PubMed:17405873, ECO:0000269|PubMed:7867067}. TISSUE SPECIFICITY: Expressed in subpopulations of macrophages in the spleen and the medullary cord of lymph nodes (at protein level). {ECO:0000269|PubMed:7867067}. +P26645 MARCS_MOUSE Myristoylated alanine-rich C-kinase substrate (MARCKS) 309 29,661 Chain (1); Helix (1); Initiator methionine (1); Lipidation (1); Modified residue (22); Mutagenesis (1); Region (1); Sequence conflict (1) FUNCTION: MARCKS is the most prominent cellular substrate for protein kinase C. This protein binds calmodulin, actin, and synapsin. MARCKS is a filamentous (F) actin cross-linking protein. PTM: Phosphorylation by PKC displaces MARCKS from the membrane. It also inhibits the F-actin cross-linking activity. {ECO:0000269|PubMed:7588787, ECO:0000269|PubMed:8849678}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. Membrane {ECO:0000250|UniProtKB:P29966}; Lipid-anchor {ECO:0000250|UniProtKB:P29966}. TISSUE SPECIFICITY: Brain, spleen, less in kidney and heart, and very low levels in liver. +Q61166 MARE1_MOUSE Microtubule-associated protein RP/EB family member 1 (APC-binding protein EB1) (End-binding protein 1) (EB1) 268 30,016 Beta strand (4); Chain (1); Domain (2); Erroneous initiation (1); Helix (7); Initiator methionine (1); Modified residue (3); Mutagenesis (3); Region (3); Turn (3) FUNCTION: Plus-end tracking protein (+TIP) that binds to the plus-end of microtubules and regulates the dynamics of the microtubule cytoskeleton. Promotes cytoplasmic microtubule nucleation and elongation. May be involved in spindle function by stabilizing microtubules and anchoring them at centrosomes. Also acts as a regulator of minus-end microtubule organization: interacts with the complex formed by AKAP9 and PDE4DIP, leading to recruit CAMSAP2 to the Golgi apparatus, thereby tethering non-centrosomal minus-end microtubules to the Golgi, an important step for polarized cell movement. Promotes elongation of CAMSAP2-decorated microtubule stretches on the minus-end of microtubules. Acts as a regulator of autophagosome transport via interaction with CAMSAP2 (By similarity). May play a role in cell migration (PubMed:15311282). {ECO:0000250|UniProtKB:Q15691, ECO:0000269|PubMed:15311282}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:21357749}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q15691}. Note=Associated with the microtubule network at the growing distal tip of microtubules (PubMed:21357749). Also enriched at the centrosome (By similarity). {ECO:0000250|UniProtKB:Q15691, ECO:0000269|PubMed:21357749}. SUBUNIT: Homodimer (By similarity). Heterodimer with MAPRE3 (By similarity). Interacts with APC (via C-terminal domain), DCTN1, DIAPH1, DIAPH2 (PubMed:15311282). Interacts with DCTN2, TERF1 and dynein intermediate chain (By similarity). Interacts with CLASP2, DST, KIF2C and STIM1; probably required for their targeting to the growing microtubule plus ends (By similarity). Interacts with MTUS2; interaction is direct and probably targets MTUS2 to microtubules (By similarity). Interacts with APC2 (By similarity). Interacts with CLASP1 (By similarity). Interacts (via C-terminus) with CLIP1 (By similarity). Interacts with SLAIN2 and SLAIN1 (PubMed:21646404). Interacts with MACF1 (PubMed:18854161). Interacts with KIF18B; this interaction is required for efficient accumulation of KIF18B at microtubule plus ends (By similarity). Interacts with MISP (By similarity). Interacts with RABL2/RABL2A; binds preferentially to GTP-bound RABL2 (PubMed:23055941). Interacts with KCNAB2 (PubMed:21357749). Interacts with KNSTRN (By similarity). Interacts with NCKAP5L (By similarity). Interacts with AKAP9 (By similarity). Interacts with PDE4DIP isoform 2/MMG8/SMYLE; this interaction is required for its recruitment to the Golgi apparatus. May form a pericentrosomal complex with AKAP9, CDK5RAP2 and PDE4DIP isoform 2/MMG8/SMYLE; within this complex, MAPRE1 binding to CDK5RAP2 may be mediated by PDE4DIP (By similarity). Contrary to other mammalian species, does not interact with CDK5RAP2, possibly due to the lack of conservation of the MAPRE1-binding motif in mouse CDK5RAP2 (PubMed:19553473). {ECO:0000250|UniProtKB:Q15691, ECO:0000269|PubMed:15311282, ECO:0000269|PubMed:18854161, ECO:0000269|PubMed:19553473, ECO:0000269|PubMed:21357749, ECO:0000269|PubMed:21646404, ECO:0000269|PubMed:23055941}. DOMAIN: Composed of two functionally independent domains. The N-terminal domain forms a hydrophobic cleft involved in microtubule binding and the C-terminal is involved in the formation of mutually exclusive complexes with APC and DCTN1. {ECO:0000250|UniProtKB:Q15691}. TISSUE SPECIFICITY: Expressed within the midpiece of sperm tail (at protein level). {ECO:0000269|PubMed:23055941}. +Q8R001 MARE2_MOUSE Microtubule-associated protein RP/EB family member 2 (APC-binding protein EB2) (End-binding protein 2) (EB2) 326 36,946 Alternative sequence (1); Chain (1); Domain (2); Modified residue (3); Region (2); Sequence conflict (4) FUNCTION: May be involved in microtubule polymerization, and spindle function by stabilizing microtubules and anchoring them at centrosomes. May play a role in cell migration (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Associated with the microtubule network. Accumulates at the plus end of microtubules (By similarity). {ECO:0000250}. SUBUNIT: Interacts with DCTN1. Interacts with APC (via C-terminal). Interacts with monomeric and polymerized tubulin (By similarity). Interacts with SLAIN1 (PubMed:21646404). {ECO:0000250|UniProtKB:Q15555, ECO:0000269|PubMed:21646404}. DOMAIN: Composed of two functionally independent domains. The N-terminal domain forms a hydrophobic cleft involved in microtubule binding and the C-terminal is involved in the formation of mutually exclusive complexes with APC and DCTN1 (By similarity). {ECO:0000250}. +Q6PER3 MARE3_MOUSE Microtubule-associated protein RP/EB family member 3 (EB1 protein family member 3) (EBF3) (End-binding protein 3) (EB3) (RP3) 281 31,966 Chain (1); Domain (2); Modified residue (2); Region (2) FUNCTION: Plus-end tracking protein (+TIP) that binds to the plus-end of microtubules and regulates the dynamics of the microtubule cytoskeleton. Promotes microtubule growth. May be involved in spindle function by stabilizing microtubules and anchoring them at centrosomes. Also acts as a regulator of minus-end microtubule organization: interacts with the complex formed by AKAP9 and PDE4DIP, leading to recruit CAMSAP2 to the Golgi apparatus, thereby tethering non-centrosomal minus-end microtubules to the Golgi, an important step for polarized cell movement. Promotes elongation of CAMSAP2-decorated microtubule stretches on the minus-end of microtubules (By similarity). May play a role in cell migration (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9UPY8}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9UPY8}. Note=Associated with the microtubule network. Detected at the plus end of microtubules. {ECO:0000250|UniProtKB:Q9UPY8}. SUBUNIT: Homodimer (By similarity). Heterodimer with MAPRE1 (By similarity). Interacts with DCTN1 and SRCIN1 (By similarity). Binds to the C-terminal domain of APC (By similarity). Binds monomeric and polymerized tubulin. Interacts (via C-terminus) with CLIP1 (By similarity). Interacts with SLAIN2 (By similarity). Interacts with SLAIN1 (PubMed:21646404). Interacts with APC2 (PubMed:17310996). Interacts with AKAP9 (By similarity). Interacts with PDE4DIP isoform 2/MMG8/SMYLE; this interaction is required for its recruitment to the Golgi apparatus (By similarity). {ECO:0000250|UniProtKB:Q9UPY8, ECO:0000269|PubMed:17310996, ECO:0000269|PubMed:21646404}. DOMAIN: Composed of two functionally independent domains. The N-terminal domain forms a hydrophobic cleft involved in microtubule binding and the C-terminal is involved in the formation of mutually exclusive complexes with APC and DCTN1. {ECO:0000250|UniProtKB:Q9UPY8}. +Q8BJ34 MARF1_MOUSE Meiosis regulator and mRNA stability factor 1 (Limkain-b1) (Meiosis arrest female protein 1) 1730 192,064 Alternative sequence (12); Beta strand (9); Chain (1); Compositional bias (1); Domain (10); Erroneous initiation (1); Helix (13); Modified residue (5); Sequence conflict (1); Turn (2) FUNCTION: Essential regulator of oogenesis required for female meiotic progression to repress transposable elements and preventing their mobilization, which is essential for the germline integrity. Probably acts via some RNA metabolic process, equivalent to the piRNA system in males, which mediates the repression of transposable elements during meiosis by forming complexes composed of RNAs and governs the methylation and subsequent repression of transposons. Also required to protect from DNA double-strand breaks. {ECO:0000269|PubMed:22442484, ECO:0000269|PubMed:23090997}. SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}. SUBUNIT: Interacts with LIMK2. {ECO:0000250}. TISSUE SPECIFICITY: Predominantly present in oocytes and barely detectable in granulosa cells (at protein level). {ECO:0000269|PubMed:22442484}. +Q6NZQ8 MARH1_MOUSE E3 ubiquitin-protein ligase MARCH1 (EC 2.3.2.27) (Membrane-associated RING finger protein 1) (Membrane-associated RING-CH protein I) (MARCH-I) (RING-type E3 ubiquitin transferase MARCH1) 289 32,347 Alternative sequence (3); Chain (1); Mutagenesis (3); Region (2); Sequence conflict (1); Transmembrane (2); Zinc finger (1) TRANSMEM 155 175 Helical. {ECO:0000255}.; TRANSMEM 197 217 Helical. {ECO:0000255}. Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination of TFRC, CD86, FAS and MHC class II proteins, such as HLA-DR alpha and beta, and promotes their subsequent endocytosis and sorting to lysosomes via multivesicular bodies. By constitutively ubiquitinating MHC class II proteins in immature dendritic cells, down-regulates their cell surface localization thus sequestering them in the intracellular endosomal system. {ECO:0000269|PubMed:17051151, ECO:0000269|PubMed:17255932, ECO:0000269|PubMed:19880452, ECO:0000269|PubMed:19917682}. PTM: Has a short half-life. Instability/short half-life permits rapid changes that allow efficient induction of antigen presentation once antigen presenting cells, APCs, receive maturation signals. Small changes in protein levels significantly alter the cell surface display of MHC class II proteins. SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000269|PubMed:19880452}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000269|PubMed:19880452}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:19880452}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:19880452}; Multi-pass membrane protein {ECO:0000255}. DOMAIN: The RING-CH-type zinc finger domain is required for E3 ligase activity. {ECO:0000255|PROSITE-ProRule:PRU00623}. +Q99M02 MARH2_MOUSE E3 ubiquitin-protein ligase MARCH2 (EC 2.3.2.27) (Membrane-associated RING finger protein 2) (Membrane-associated RING-CH protein II) (MARCH-II) (RING-type E3 ubiquitin transferase MARCH2) 246 27,186 Chain (1); Frameshift (1); Transmembrane (2); Zinc finger (1) TRANSMEM 138 158 Helical. {ECO:0000255}.; TRANSMEM 175 195 Helical. {ECO:0000255}. Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that may mediate ubiquitination of TFRC and CD86, and promote their subsequent endocytosis and sorting to lysosomes via multivesicular bodies. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates. May be involved in endosomal trafficking through interaction with STX6. {ECO:0000250|UniProtKB:Q9P0N8}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. Lysosome membrane {ECO:0000250|UniProtKB:Q9P0N8}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9P0N8}. Endosome membrane {ECO:0000250|UniProtKB:Q5I0I2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5I0I2}. SUBUNIT: Interacts with STX6 and MARCH3. {ECO:0000250}. DOMAIN: The RING-CH-type zinc finger domain is required for E3 ligase activity. {ECO:0000255|PROSITE-ProRule:PRU00623}. +Q8BRX9 MARH3_MOUSE E3 ubiquitin-protein ligase MARCH3 (EC 2.3.2.27) (Membrane-associated RING finger protein 3) (Membrane-associated RING-CH protein III) (MARCH-III) (RING-type E3 ubiquitin transferase MARCH3) 218 24,491 Chain (1); Transmembrane (2); Zinc finger (1) TRANSMEM 145 165 Helical. {ECO:0000255}.; TRANSMEM 180 200 Helical. {ECO:0000255}. Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase which may be involved in endosomal trafficking. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates. {ECO:0000250|UniProtKB:Q5XIE5}. SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Multi-pass membrane protein. Early endosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with MARCH2 and STX6. {ECO:0000250}. DOMAIN: The RING-CH-type zinc finger domain is required for E3 ligase activity. {ECO:0000255|PROSITE-ProRule:PRU00623}. +Q80TE3 MARH4_MOUSE E3 ubiquitin-protein ligase MARCH4 (EC 2.3.2.27) (Membrane-associated RING finger protein 4) (Membrane-associated RING-CH protein IV) (MARCH-IV) (RING-type E3 ubiquitin transferase MARCH4) 409 45,201 Chain (1); Compositional bias (2); Sequence conflict (1); Signal peptide (1); Transmembrane (2); Zinc finger (1) TRANSMEM 242 262 Helical. {ECO:0000255}.; TRANSMEM 271 291 Helical. {ECO:0000255}. Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that may mediate ubiquitination of MHC-I and CD4, and promote their subsequent endocytosis and sorting to lysosomes via multivesicular bodies. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates. {ECO:0000250|UniProtKB:Q9P2E8}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. DOMAIN: The RING-CH-type zinc finger domain is required for E3 ligase activity. {ECO:0000255|PROSITE-ProRule:PRU00623}. +Q3KNM2 MARH5_MOUSE E3 ubiquitin-protein ligase MARCH5 (EC 2.3.2.27) (Membrane-associated RING finger protein 5) (Membrane-associated RING-CH protein V) (MARCH-V) (RING-type E3 ubiquitin transferase MARCH5) 278 31,232 Chain (1); Sequence conflict (2); Transmembrane (4); Zinc finger (1) TRANSMEM 99 119 Helical. {ECO:0000255}.; TRANSMEM 139 159 Helical. {ECO:0000255}.; TRANSMEM 209 229 Helical. {ECO:0000255}.; TRANSMEM 238 258 Helical. {ECO:0000255}. Protein modification; protein ubiquitination. FUNCTION: Mitochondrial E3 ubiquitin-protein ligase that plays a crucial role in the control of mitochondrial morphology by acting as a positive regulator of mitochondrial fission. May play a role in the prevention of cell senescence acting as a regulator of mitochondrial quality control. Promotes ubiquitination of FIS1, DNM1L and MFN1. {ECO:0000250|UniProtKB:Q9NX47}. PTM: Autoubiquitinated leading to degradation. {ECO:0000250|UniProtKB:Q9NX47}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q9NX47}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9NX47}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Monomer and homodimer. Interacts with MFN1, MFN2, DNM1L and FIS1. {ECO:0000250|UniProtKB:Q9NX47}. DOMAIN: The RING-CH-type zinc finger domain is required for E3 ligase activity. {ECO:0000255|PROSITE-ProRule:PRU00623}. +Q6ZQ89 MARH6_MOUSE E3 ubiquitin-protein ligase MARCH6 (EC 2.3.2.27) (Membrane-associated RING finger protein 6) (Membrane-associated RING-CH protein VI) (MARCH-VI) (RING-type E3 ubiquitin transferase MARCH6) 909 102,273 Alternative sequence (3); Chain (1); Erroneous initiation (1); Modified residue (1); Sequence conflict (1); Topological domain (15); Transmembrane (14); Zinc finger (1) TRANSMEM 92 112 Helical. {ECO:0000255}.; TRANSMEM 143 163 Helical. {ECO:0000255}.; TRANSMEM 284 304 Helical. {ECO:0000255}.; TRANSMEM 337 357 Helical. {ECO:0000255}.; TRANSMEM 377 397 Helical. {ECO:0000255}.; TRANSMEM 422 442 Helical. {ECO:0000255}.; TRANSMEM 481 501 Helical. {ECO:0000255}.; TRANSMEM 520 540 Helical. {ECO:0000255}.; TRANSMEM 632 652 Helical. {ECO:0000255}.; TRANSMEM 678 698 Helical. {ECO:0000255}.; TRANSMEM 721 741 Helical. {ECO:0000255}.; TRANSMEM 764 784 Helical. {ECO:0000255}.; TRANSMEM 815 835 Helical. {ECO:0000255}.; TRANSMEM 848 868 Helical. {ECO:0000255}. TOPO_DOM 1 91 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 113 142 Extracellular. {ECO:0000255}.; TOPO_DOM 164 283 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 305 336 Extracellular. {ECO:0000255}.; TOPO_DOM 358 376 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 398 421 Extracellular. {ECO:0000255}.; TOPO_DOM 443 480 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 502 519 Extracellular. {ECO:0000255}.; TOPO_DOM 541 631 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 653 677 Extracellular. {ECO:0000255}.; TOPO_DOM 699 720 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 742 763 Extracellular. {ECO:0000255}.; TOPO_DOM 785 814 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 836 847 Extracellular. {ECO:0000255}.; TOPO_DOM 869 909 Cytoplasmic. {ECO:0000255}. Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that promotes ubiquitination of DIO2, leading to its degradation. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates. May cooperate with UBE2G1. {ECO:0000250|UniProtKB:O60337}. PTM: Auto-ubiquitinated, which results in proteasomal degradation. {ECO:0000250|UniProtKB:O60337}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O60337}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O60337}. SUBUNIT: Interacts with DIO2. {ECO:0000250|UniProtKB:O60337}. DOMAIN: The RING-CH-type zinc finger domain is required for E3 ligase activity. {ECO:0000255|PROSITE-ProRule:PRU00623}. +Q9WV66 MARH7_MOUSE E3 ubiquitin-protein ligase MARCH7 (EC 2.3.2.27) (Axotrophin) (Membrane-associated RING finger protein 7) (Membrane-associated RING-CH protein VII) (MARCH-VII) (RING-type E3 ubiquitin transferase MARCH7) 693 76,599 Chain (1); Compositional bias (2); Modified residue (5); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase which may specifically enhance the E2 activity of HIP2. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates. May be involved in T-cell proliferation by regulating LIF secretion. {ECO:0000269|PubMed:15670816}. DOMAIN: The RING-CH-type zinc finger domain is required for E3 ligase activity. {ECO:0000255|PROSITE-ProRule:PRU00623}. TISSUE SPECIFICITY: Expressed in brain, thymus, muscle and kidney. {ECO:0000269|PubMed:15670816}. +Q9DBD2 MARH8_MOUSE E3 ubiquitin-protein ligase MARCH8 (EC 2.3.2.27) (Cellular modulator of immune recognition) (c-MIR) (Membrane-associated RING finger protein 8) (Membrane-associated RING-CH protein VIII) (MARCH-VIII) (RING-type E3 ubiquitin transferase MARCH8) 286 32,243 Chain (1); Modified residue (1); Transmembrane (2); Zinc finger (1) TRANSMEM 153 173 Helical. {ECO:0000255}.; TRANSMEM 193 213 Helical. {ECO:0000255}. Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination of CD86 and MHC class II proteins, such as HLA-DR alpha and beta, and promotes their subsequent endocytosis and sorting to lysosomes via multivesicular bodies. May also promote ubiquitination and endocytosis of TFRC and FAS (By similarity). {ECO:0000250, ECO:0000269|PubMed:16785530}. SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q5T0T0}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:Q5T0T0}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:Q5T0T0}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Interacts with CD86. {ECO:0000250|UniProtKB:Q5T0T0}. DOMAIN: The RING-CH-type zinc finger domain is required for E3 ligase activity. +Q3TZ87 MARH9_MOUSE E3 ubiquitin-protein ligase MARCH9 (EC 2.3.2.27) (Membrane-associated RING finger protein 9) (Membrane-associated RING-CH protein IX) (MARCH-IX) (RING-type E3 ubiquitin transferase MARCH9) 348 37,888 Chain (1); Compositional bias (2); Erroneous initiation (1); Transmembrane (2); Zinc finger (1) TRANSMEM 185 205 Helical. {ECO:0000255}.; TRANSMEM 219 239 Helical. {ECO:0000255}. Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that may mediate ubiquitination of MHC-I, CD4 and ICAM1, and promote their subsequent endocytosis and sorting to lysosomes via multivesicular bodies. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates. {ECO:0000250|UniProtKB:Q86YJ5}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q86YJ5}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:Q86YJ5}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q86YJ5}. DOMAIN: The RING-CH-type zinc finger domain is required for E3 ligase activity. +Q8CBH7 MARHB_MOUSE E3 ubiquitin-protein ligase MARCH11 (EC 2.3.2.27) (Membrane-associated RING finger protein 11) (Membrane-associated RING-CH protein XI) (MARCH-XI) (RING-type E3 ubiquitin transferase MARCH11) 400 44,223 Alternative sequence (2); Chain (1); Compositional bias (2); Motif (2); Transmembrane (2); Zinc finger (1) TRANSMEM 243 263 Helical. {ECO:0000255}.; TRANSMEM 276 296 Helical. {ECO:0000255}. Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that mediates polyubiquitination of CD4. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates. May play a role in ubuquitin-dependent protein sorting in developmenting spermatids. {ECO:0000250|UniProtKB:A6P320}. SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:A6P320}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A6P320}. SUBUNIT: Interacts (YXXL motif) with AP1M1. Interacts (via PDZ-binding motif) with LIN7A. Interacts with unidentified fucose glycoproteins. {ECO:0000250|UniProtKB:A6P320}. DOMAIN: The RING-CH-type zinc finger domain is required for E3 ligase activity. {ECO:0000255|PROSITE-ProRule:PRU00623}. +Q8VHJ5 MARK1_MOUSE Serine/threonine-protein kinase MARK1 (EC 2.7.11.1) (EC 2.7.11.26) (ELKL motif serine/threonine-protein kinase 3) (MAP/microtubule affinity-regulating kinase 1) (PAR1 homolog c) (Par-1c) (mPar-1c) 795 88,335 Active site (1); Binding site (1); Chain (1); Domain (3); Modified residue (14); Nucleotide binding (1); Sequence conflict (14) FUNCTION: Serine/threonine-protein kinase (By similarity). Involved in cell polarity and microtubule dynamics regulation. Phosphorylates DCX, MAP2 and MAP4. Phosphorylates the microtubule-associated protein MAPT/TAU (By similarity). Involved in cell polarity by phosphorylating the microtubule-associated proteins MAP2, MAP4 and MAPT/TAU at KXGS motifs, causing detachment from microtubules, and their disassembly. Involved in the regulation of neuronal migration through its dual activities in regulating cellular polarity and microtubule dynamics, possibly by phosphorylating and regulating DCX. Also acts as a positive regulator of the Wnt signaling pathway, probably by mediating phosphorylation of dishevelled proteins (DVL1, DVL2 and/or DVL3). {ECO:0000250|UniProtKB:Q9P0L2}. PTM: Phosphorylated at Thr-215 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. Phosphorylation at Thr-215 by TAOK1 activates the kinase activity, leading to phosphorylation and detachment of MAPT/TAU from microtubules. Phosphorylation at Ser-219 by GSK3-beta (GSK3B) inhibits the kinase activity. Phosphorylation at Thr-613 by PRKCZ/aPKC in polarized epithelial cells inhibits the kinase activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm {ECO:0000250|UniProtKB:Q9P0L2}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9P0L2}. Note=Appears to localize to an intracellular network. {ECO:0000250}. SUBUNIT: Interacts with MAPT/TAU. {ECO:0000250|UniProtKB:Q9P0L2}. DOMAIN: The UBA domain does not seem to bind ubiquitin and ubiquitin-like and might play a role in regulating the enzyme conformation and localization. Activation of the kinase activity following phosphorylation at Thr-208 is accompanied by a conformational change that alters the orientation of the UBA domain with respect to the catalytic domain (By similarity). {ECO:0000250}.; DOMAIN: The KA1 domain mediates binding to phospholipids and targeting to membranes. Binds phosphatidic acid (PA), phosphatidylserine (PtdSer) and phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) (By similarity). {ECO:0000250}. +Q05512 MARK2_MOUSE Serine/threonine-protein kinase MARK2 (EC 2.7.11.1) (EC 2.7.11.26) (ELKL motif kinase 1) (EMK-1) (MAP/microtubule affinity-regulating kinase 2) (PAR1 homolog) (PAR1 homolog b) (Par-1b) (mPar-1b) 776 86,306 Active site (1); Alternative sequence (3); Binding site (1); Chain (1); Domain (3); Frameshift (1); Modified residue (22); Nucleotide binding (1); Sequence conflict (3) FUNCTION: Serine/threonine-protein kinase. Involved in cell polarity and microtubule dynamics regulation. Phosphorylates CRTC2/TORC2, DCX, HDAC7, KIF13B, MAP2, MAP4 and RAB11FIP2. Phosphorylates the microtubule-associated protein MAPT/TAU. Plays a key role in cell polarity by phosphorylating the microtubule-associated proteins MAP2, MAP4 and MAPT/TAU at KXGS motifs, causing detachment from microtubules, and their disassembly. Regulates epithelial cell polarity by phosphorylating RAB11FIP2. Involved in the regulation of neuronal migration through its dual activities in regulating cellular polarity and microtubule dynamics, possibly by phosphorylating and regulating DCX. Regulates axogenesis by phosphorylating KIF13B, promoting interaction between KIF13B and 14-3-3 and inhibiting microtubule-dependent accumulation of KIF13B. Also required for neurite outgrowth and establishment of neuronal polarity. Regulates localization and activity of some histone deacetylases by mediating phosphorylation of HDAC7, promoting subsequent interaction between HDAC7 and 14-3-3 and export from the nucleus. Also acts as a positive regulator of the Wnt signaling pathway, probably by mediating phosphorylation of dishevelled proteins (DVL1, DVL2 and/or DVL3). Modulates the developmental decision to build a columnar versus a hepatic epithelial cell apparently by promoting a switch from a direct to a transcytotic mode of apical protein delivery. Essential for the asymmetric development of membrane domains of polarized epithelial cells. {ECO:0000250|UniProtKB:Q7KZI7}. PTM: Autophosphorylated. Phosphorylated at Thr-208 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. Phosphorylation at Thr-208 by TAOK1 activates the kinase activity, leading to phosphorylation and detachment of MAPT/TAU from microtubules. Phosphorylation at Ser-212 by GSK3-beta (GSK3B) inhibits the kinase activity. Phosphorylation by CaMK1 promotes activity and is required to promote neurite outgrowth. Phosphorylation at Thr-593 by PRKCZ/aPKC in polarized epithelial cells inhibits the kinase activity and promotes binding to 14-3-3 protein YWHAZ, leading to relocation from cell membrane to cytoplasm (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Lateral cell membrane {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q7KZI7}. Cytoplasm {ECO:0000250|UniProtKB:Q7KZI7}. Note=Phosphorylation at Thr-593 by PRKCZ/aPKC and subsequent interaction with 14-3-3 protein YWHAZ promotes relocation from the cell membrane to the cytoplasm. {ECO:0000250}. SUBUNIT: Homodimer. Interacts with PAK5; leading to inhibit the protein kinase activity (By similarity). Interacts with MAPT/TAU. Interacts with MTCL1; the interaction is direct and increases MARK2 microtubule-binding ability. Interacts (when phosphorylated at Thr-593) with YWHAZ (By similarity). {ECO:0000250|UniProtKB:O08679, ECO:0000250|UniProtKB:Q7KZI7}. DOMAIN: The UBA domain does not seem to bind ubiquitin and ubiquitin-like and might play a role in regulating the enzyme conformation and localization. Activation of the kinase activity following phosphorylation at Thr-208 is accompanied by a conformational change that alters the orientation of the UBA domain with respect to the catalytic domain (By similarity). {ECO:0000250}.; DOMAIN: The KA1 domain mediates binding to phospholipids and targeting to membranes. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in adult kidney and testis, lower levels in heart, brain, spleen, lung and liver. Expressed in the head and neural fold in 8 dpc embryos, the limb buds, telencephalic vesicles, eyes, branchial archs and heart at 11.5 dpc, the ectoderm at 13 dpc and epiderm, hair and whisker follicles at 15 dpc. {ECO:0000269|PubMed:10491259}. +Q03141 MARK3_MOUSE MAP/microtubule affinity-regulating kinase 3 (EC 2.7.11.1) (ELKL motif kinase 2) (EMK-2) (MPK-10) 753 84,390 Active site (1); Alternative sequence (2); Beta strand (5); Binding site (1); Chain (1); Compositional bias (1); Domain (3); Erroneous initiation (2); Helix (3); Modified residue (18); Nucleotide binding (1); Sequence conflict (4) FUNCTION: Serine/threonine-protein kinase. Involved in the specific phosphorylation of microtubule-associated proteins for MAPT/TAU, MAP2 and MAP4. Phosphorylates CDC25C. Regulates localization and activity of some histone deacetylases by mediating phosphorylation of HDAC7, promoting subsequent interaction between HDAC7 and 14-3-3 and export from the nucleus. Negatively regulates the Hippo signaling pathway and antagonizes the phosphorylation of LATS1. Cooperates with DLG5 to inhibit the kinase activity of STK3/MST2 toward LATS1. {ECO:0000250|UniProtKB:P27448}. PTM: Phosphorylated at Thr-211 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. Phosphorylation at Thr-564 by PRKCZ/aPKC inhibits the kinase activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P27448}; Peripheral membrane protein {ECO:0000250|UniProtKB:P27448}. Cell projection, dendrite {ECO:0000250|UniProtKB:P27448}. Cytoplasm {ECO:0000250|UniProtKB:P27448}. SUBUNIT: Interacts with MAPT/TAU. Interacts with DLG5 (via coiled-coil domain). Interacts with STK3/MST2 and STK4/MST1 in the presence of DLG5. {ECO:0000250|UniProtKB:P27448}. +Q8CIP4 MARK4_MOUSE MAP/microtubule affinity-regulating kinase 4 (EC 2.7.11.1) 752 82,644 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Domain (3); Modified residue (3); Nucleotide binding (1); Sequence conflict (8) FUNCTION: Serine/threonine-protein kinase (By similarity). Phosphorylates the microtubule-associated protein MAPT/TAU (By similarity). Also phosphorylates the microtubule-associated proteins MAP2 and MAP4 (By similarity). Involved in regulation of the microtubule network, causing reorganization of microtubules into bundles (By similarity). Required for the initiation of axoneme extension during cilium assembly (By similarity). Regulates the centrosomal location of ODF2 and phosphorylates ODF2 in vitro (By similarity). Plays a role in cell cycle progression, specifically in the G1/S checkpoint (By similarity). Reduces neuronal cell survival (By similarity). Plays a role in energy homeostasis by regulating satiety and metabolic rate (PubMed:22992738). Promotes adipogenesis by activating JNK1 and inhibiting the p38MAPK pathway, and triggers apoptosis by activating the JNK1 pathway (PubMed:24989893). Phosphorylates mTORC1 complex member RPTOR and acts as a negative regulator of the mTORC1 complex, probably due to disruption of the interaction between phosphorylated RPTOR and the RRAGA/RRAGC heterodimer which is required for mTORC1 activation (By similarity). {ECO:0000250|UniProtKB:Q96L34, ECO:0000269|PubMed:22992738, ECO:0000269|PubMed:24989893}. PTM: Ubiquitinated with 'Lys-29'- and 'Lys-33'-linked polyubiquitins which appear to impede LKB1-mediated phosphorylation. Deubiquitinated by USP9X (By similarity). {ECO:0000250|UniProtKB:Q96L34}.; PTM: Phosphorylated at Thr-214 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. Phosphorylated throughout the cell cycle. {ECO:0000250|UniProtKB:Q96L34}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q96L34}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000250|UniProtKB:Q96L34}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q96L34}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q96L34}. Cytoplasm {ECO:0000250|UniProtKB:Q96L34}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q96L34}. Note=Localized at the tips of neurite-like processes in differentiated neuroblast cells. Detected in the cytoplasm and neuropil of the hippocampus. {ECO:0000250|UniProtKB:Q96L34}. SUBUNIT: Interacts with MAPT/TAU. Interacts with gamma-tubulin. Interacts with ODF2. Interacts with USP9X. {ECO:0000250|UniProtKB:Q96L34}. TISSUE SPECIFICITY: Isoform 1 and isoform 2 show similar expression patterns in the central nervous system and are present in the same subsets of neurons including pyramidal and non-pyramidal neurons in the cerebral cortex and hippocampus, cerebellar Purkinje cells, and interneurons and motor neurons in the spinal cord but not in glial cells (at protein level) (PubMed:16973293). Isoform 2 is the major isoform in brain and cerebellum (PubMed:16973293, PubMed:15009667). Also expressed in spleen, liver, small intestine, colon, kidney, tongue, testis and lung (PubMed:16973293, PubMed:15009667). Isoform 1 and isoform 2 are expressed at similar levels in heart (PubMed:16973293). {ECO:0000269|PubMed:15009667, ECO:0000269|PubMed:16973293}. +P98064 MASP1_MOUSE Mannan-binding lectin serine protease 1 (EC 3.4.21.-) (Complement factor MASP-3) (Complement-activating component of Ra-reactive factor) (Mannose-binding lectin-associated serine protease 1) (MASP-1) (Mannose-binding protein-associated serine protease) (Ra-reactive factor serine protease p100) (RaRF) (Serine protease 5) [Cleaved into: Mannan-binding lectin serine protease 1 heavy chain; Mannan-binding lectin serine protease 1 light chain] 704 79,968 Active site (3); Alternative sequence (2); Chain (3); Disulfide bond (14); Domain (6); Glycosylation (4); Metal binding (14); Modified residue (1); Region (4); Sequence conflict (5); Signal peptide (1); Site (1) FUNCTION: Functions in the lectin pathway of complement, which performs a key role in innate immunity by recognizing pathogens through patterns of sugar moieties and neutralizing them. The lectin pathway is triggered upon binding of mannan-binding lectin (MBL) and ficolins to sugar moieties which leads to activation of the associated proteases MASP1 and MASP2. Functions as an endopeptidase and may activate MASP2 or C2 or directly activate C3 the key component of complement reaction. Isoform 2 may have an inhibitory effect on the activation of the lectin pathway of complement or may cleave IGFBP5. Also plays a role in development. {ECO:0000250|UniProtKB:P48740, ECO:0000269|PubMed:18424734}. PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}.; PTM: N-glycosylated. Some N-linked glycan are of the complex-type (By similarity). {ECO:0000250}.; PTM: Autoproteolytic processing of the proenzyme produces the active enzyme composed on the heavy and the light chain held together by a disulfide bond. Isoform 1 but not isoform 2 is activated through autoproteolytic processing (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8133044}. SUBUNIT: Homodimer. Interacts with the oligomeric lectins MBL2, FCN2 and FCN3; triggers the lectin pathway of complement through activation of C3. Interacts with SERPING1. Interacts with COLEC11; probably triggers the lectin pathway of complement. {ECO:0000250|UniProtKB:P48740}. TISSUE SPECIFICITY: Protein of the plasma which is primarily expressed by liver. {ECO:0000269|PubMed:18424734, ECO:0000269|PubMed:8133044}. +Q91WP0 MASP2_MOUSE Mannan-binding lectin serine protease 2 (EC 3.4.21.104) (MBL-associated serine protease 2) (Mannose-binding protein-associated serine protease 2) (MASP-2) [Cleaved into: Mannan-binding lectin serine protease 2 A chain; Mannan-binding lectin serine protease 2 B chain] 685 75,517 Active site (3); Alternative sequence (2); Chain (3); Disulfide bond (13); Domain (6); Glycosylation (5); Metal binding (9); Modified residue (1); Sequence conflict (10); Signal peptide (1); Site (1) FUNCTION: Serum protease that plays an important role in the activation of the complement system via mannose-binding lectin. After activation by auto-catalytic cleavage it cleaves C2 and C4, leading to their activation and to the formation of C3 convertase (By similarity). {ECO:0000250}. PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Homodimer; disulfide-linked. Binds MBL2. Isoform 2 binds to MASP1. Binds SERPING1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Plasma. +Q9R1L5 MAST1_MOUSE Microtubule-associated serine/threonine-protein kinase 1 (EC 2.7.11.1) (Syntrophin-associated serine/threonine-protein kinase) 1570 170,997 Active site (1); Binding site (1); Chain (1); Domain (3); Frameshift (1); Modified residue (9); Nucleotide binding (1); Sequence caution (1); Sequence conflict (7) FUNCTION: Appears to link the dystrophin/utrophin network with microtubule filaments via the syntrophins. Phosphorylation of DMD or UTRN may modulate their affinities for associated proteins. {ECO:0000269|PubMed:10404183, ECO:0000303|PubMed:10404183}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10404183}; Peripheral membrane protein {ECO:0000269|PubMed:10404183}; Cytoplasmic side {ECO:0000269|PubMed:10404183}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10404183}. Note=Colocalizes with syntrophins at the cell membrane. SUBUNIT: Part of a low affinity complex that associates with, but is distinct from, the postsynaptic density. Interacts with SNTB2. {ECO:0000269|PubMed:10404183}. TISSUE SPECIFICITY: Expressed in the vascular endothelium and in proximity to neuronal nuclei throughout the cortex and cerebellum. Also detected in ependymal cells, the choroid plexus, in developing spermatid acrosomes and in both the cell bodies and axonal processes of motor neurons. Observed as punctate clusters in the processes of interneurons and along the cell body periphery. {ECO:0000269|PubMed:10404183}. +Q60592 MAST2_MOUSE Microtubule-associated serine/threonine-protein kinase 2 (EC 2.7.11.1) 1734 190,534 Active site (1); Binding site (1); Chain (1); Domain (3); Modified residue (18); Mutagenesis (1); Nucleotide binding (1); Sequence conflict (9) FUNCTION: Appears to link the dystrophin/utrophin network with microtubule filaments via the syntrophins. Phosphorylation of DMD or UTRN may modulate their affinities for associated proteins. Functions in a multi-protein complex in spermatid maturation. Regulates lipopolysaccharide-induced IL-12 synthesis in macrophages by forming a complex with TRAF6, resulting in the inhibition of TRAF6 NF-kappa-B activation. {ECO:0000269|PubMed:10404183, ECO:0000269|PubMed:14764729, ECO:0000269|PubMed:15308666, ECO:0000269|PubMed:8246979, ECO:0000269|PubMed:8902215}. PTM: Phosphorylated and ubiquitinated. N-terminal ubiquitination leads to degradation of MAST2 by proteasome-mediated proteolysis. N-terminal phosphorylation appears to be a prerequisite for ubiquitination. {ECO:0000269|PubMed:14764729, ECO:0000269|PubMed:15308666}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10404183}; Peripheral membrane protein {ECO:0000269|PubMed:10404183}; Cytoplasmic side {ECO:0000269|PubMed:10404183}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10404183}. Cell junction {ECO:0000269|PubMed:10404183}. Note=Colocalizes with beta 2-syntrophin and utrophin at neuromuscular junctions. SUBUNIT: Interacts with CDHR2. {ECO:0000250}. TISSUE SPECIFICITY: Detected in round spermatids and residual bodies but not epididymal spermatozoa (at protein level). Expressed in adult but not fetal testis with levels increasing in parallel with testicular development. Also expressed at high levels in heart, lower levels in all other tissues tested. {ECO:0000269|PubMed:10404183, ECO:0000269|PubMed:8246979, ECO:0000269|PubMed:8902215}. +Q3U214 MAST3_MOUSE Microtubule-associated serine/threonine-protein kinase 3 (EC 2.7.11.1) 1321 144,174 Active site (1); Binding site (1); Chain (1); Compositional bias (3); Domain (3); Modified residue (14); Nucleotide binding (1); Sequence conflict (4) SUBUNIT: Interacts with PTEN. {ECO:0000250}. +Q811L6 MAST4_MOUSE Microtubule-associated serine/threonine-protein kinase 4 (EC 2.7.11.1) 2618 284,004 Active site (1); Alternative sequence (4); Binding site (1); Chain (1); Domain (3); Frameshift (1); Modified residue (17); Nucleotide binding (1); Sequence conflict (7) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q60592}. +Q0ZCJ7 MASTR_MOUSE MEF2-activating motif and SAP domain-containing transcriptional regulator (MEF2-activating SAP transcriptional regulatory protein) 421 45,403 Alternative sequence (2); Chain (1); Domain (1); Motif (1); Region (1); Sequence conflict (5) FUNCTION: Transcriptional coactivator. Stimulates the transcriptional activity of MEF2C. Stimulates MYOD1 activity in part via MEF2, resulting in an enhancement of skeletal muscle differentiation. {ECO:0000269|PubMed:16818234}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16818234}. SUBUNIT: Interacts with MEF2C. {ECO:0000269|PubMed:16818234}. TISSUE SPECIFICITY: Expressed in skeletal muscle, brain, placenta and spleen. {ECO:0000269|PubMed:16818234}. +Q9CWV0 MASU1_MOUSE Mitochondrial assembly of ribosomal large subunit protein 1 228 26,020 Chain (1) FUNCTION: Required for normal mitochondrial ribosome function and mitochondrial translation. May play a role in ribosome biogenesis by preventing premature association of the 28S and 39S ribosomal subunits. Interacts with mitochondrial ribosomal protein L14 (MRPL14), probably blocking formation of intersubunit bridge B8, preventing association of the 28S and 39S ribosomal subunits. Addition to isolated mitochondrial ribosomal subunits partially inhibits translation, probably by interfering with the association of the 28S and 39S ribosomal subunits and the formation of functional ribosomes. May also participate in the assembly and/or regulation of the stability of the large subunit of the mitochondrial ribosome. May function as a ribosomal silencing factor. {ECO:0000250|UniProtKB:Q96EH3}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:Q96EH3}. Note=Colocalizes with MRPL12 and/or MRPL14. {ECO:0000250|UniProtKB:Q96EH3}. SUBUNIT: Associates with the mitochondrial ribosome large subunit (39S) via interaction with MRPL12 and/or MRPL14. The interaction generates steric hindrance that is expected to prevent premature association of the 28S and 39S ribosomal subunits. Intentified in a complex composed of MALSU1, MIEF1 upstream open reading frame protein and NDUFAB1; within the trimeric complex MIEF1 upstream open reading frame protein functions as a bridging scaffold that interacts with MALSU1 on one side, and with NDUFAB1 on the other side. Interacts with MRPL12 and MRPL14. {ECO:0000250|UniProtKB:Q96EH3}. +P30554 MAS_MOUSE Proto-oncogene Mas 324 37,055 Chain (1); Glycosylation (3); Sequence conflict (5); Topological domain (8); Transmembrane (7) TRANSMEM 36 60 Helical; Name=1. {ECO:0000255}.; TRANSMEM 65 86 Helical; Name=2. {ECO:0000255}.; TRANSMEM 104 127 Helical; Name=3. {ECO:0000255}.; TRANSMEM 149 171 Helical; Name=4. {ECO:0000255}.; TRANSMEM 185 205 Helical; Name=5. {ECO:0000255}.; TRANSMEM 224 244 Helical; Name=6. {ECO:0000255}.; TRANSMEM 263 283 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 35 Extracellular. {ECO:0000255}.; TOPO_DOM 61 64 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 87 103 Extracellular. {ECO:0000255}.; TOPO_DOM 128 148 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 172 184 Extracellular. {ECO:0000255}.; TOPO_DOM 206 223 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 245 262 Extracellular. {ECO:0000255}.; TOPO_DOM 284 324 Cytoplasmic. {ECO:0000255}. FUNCTION: Acts specifically as a functional antagonist of AGTR1 (angiotensin-2 type 1 receptor), although it up-regulates AGTR1 receptor levels. Positive regulation of AGTR1 levels occurs through activation of the G-proteins GNA11 and GNAQ, and stimulation of the protein kinase C signaling cascade. The antagonist effect on AGTR1 function is probably due to AGTR1 being physically altered by MAS1 (By similarity). Receptor for angiotensin 1-7. {ECO:0000250, ECO:0000269|PubMed:12829792}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBUNIT: Interacts with AGTR1. Interacts with FLNA (via filamin repeat 21); increases PKA-mediated phosphorylation of FLNA. {ECO:0000250|UniProtKB:P04201}. +P51949 MAT1_MOUSE CDK-activating kinase assembly factor MAT1 (CDK7/cyclin-H assembly factor) (Menage a trois) (RING finger protein MAT1) (p35) (p36) 309 35,848 Chain (1); Domain (1); Modified residue (3); Sequence conflict (5); Zinc finger (1) FUNCTION: Stabilizes the cyclin H-CDK7 complex to form a functional CDK-activating kinase (CAK) enzymatic complex. CAK activates the cyclin-associated kinases CDK1, CDK2, CDK4 and CDK6 by threonine phosphorylation. CAK complexed to the core-TFIIH basal transcription factor activates RNA polymerase II by serine phosphorylation of the repetitive C-terminal domain (CTD) of its large subunit (POLR2A), allowing its escape from the promoter and elongation of the transcripts. Involved in cell cycle control and in RNA transcription by RNA polymerase II. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Associates primarily with CDK7 and cyclin H to form the CAK complex. CAK can further associate with the core-TFIIH to form the TFIIH basal transcription factor. +Q99LB6 MAT2B_MOUSE Methionine adenosyltransferase 2 subunit beta (Methionine adenosyltransferase II beta) (MAT II beta) 334 37,393 Alternative sequence (1); Binding site (4); Chain (1); Erroneous gene model prediction (1); Modified residue (1); Nucleotide binding (3); Region (1); Sequence caution (1); Sequence conflict (3) Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. FUNCTION: Regulatory subunit of S-adenosylmethionine synthetase 2, an enzyme that catalyzes the formation of S-adenosylmethionine from methionine and ATP. Regulates MAT2A catalytic activity by changing its kinetic properties, increasing its affinity for L-methionine. Can bind NADP (in vitro). {ECO:0000250|UniProtKB:Q9NZL9}. SUBUNIT: Heterotrimer; composed of a catalytic MAT2A homodimer that binds one regulatory MAT2B chain. Heterohexamer; composed of a central, catalytic MAT2A homotetramer flanked on either side by a regulatory MAT2B chain. NADP binding increases the affinity for MAT2A. {ECO:0000250|UniProtKB:Q9NZL9}. +Q6KAU4 MB12B_MOUSE Multivesicular body subunit 12B (ESCRT-I complex subunit MVB12B) (Protein FAM125B) 317 35,411 Chain (1); Domain (2); Erroneous initiation (1); Modified residue (6) FUNCTION: Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endosome {ECO:0000250}. Late endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. SUBUNIT: Component of the ESCRT-I complex (endosomal sorting complex required for transport I) which consists of TSG101, VPS28, a VPS37 protein (VPS37A to -D) and MVB12A or MVB12B in a 1:1:1:1 stoichiometry. Interacts with TSG101; the association appears to be mediated by the TSG101-VPS37 binary subcomplex. Interacts with VPS28. Interacts with VPS37B; the association appears to be mediated by the TSG101-VPS37 binary subcomplex. Interacts with VPS37C; the association appears to be mediated by the TSG101-VPS37 binary subcomplex (By similarity). {ECO:0000250}. +O70299 MB211_MOUSE Putative nucleotidyltransferase MAB21L1 (EC 2.7.7.-) (Protein mab-21-like 1) 359 40,956 Binding site (1); Chain (1); Metal binding (2); Nucleotide binding (3) FUNCTION: Required for several aspects of embryonic development including normal development of the eye, notochord, neural tube and other organ tissues, and for embryonic turning (PubMed:11857508, PubMed:12642482). It is unclear whether it displays nucleotidyltransferase activity in vivo (By similarity). Binds single-stranded RNA (ssRNA) (By similarity). {ECO:0000250|UniProtKB:Q13394, ECO:0000269|PubMed:11857508, ECO:0000269|PubMed:12642482}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10556287}. SUBUNIT: Monomer. Homodecamer; composed of 2 back to back homopentamers. The protein may exist as monomer in solution and oiligomerizes upon ligand binding. {ECO:0000250|UniProtKB:Q13394}. TISSUE SPECIFICITY: Expressed in the adult cerebellum and eye, with lower levels in the adult forebrain. {ECO:0000269|PubMed:10349626, ECO:0000269|PubMed:10556287}. +Q9Z2E2 MBD1_MOUSE Methyl-CpG-binding domain protein 1 (Methyl-CpG-binding protein MBD1) 636 70,023 Alternative sequence (4); Chain (1); Cross-link (8); Domain (1); Modified residue (1); Motif (1); Region (1); Sequence conflict (17); Zinc finger (3) FUNCTION: Transcriptional repressor that binds CpG islands in promoters where the DNA is methylated at position 5 of cytosine within CpG dinucleotides. Binding is abolished by the presence of 7-mG that is produced by DNA damage by methylmethanesulfonate (MMS). Acts as transcriptional repressor and plays a role in gene silencing by recruiting AFT7IP, which in turn recruits factors such as the histone methyltransferase SETDB1. Probably forms a complex with SETDB1 and ATF7IP that represses transcription and couples DNA methylation and histone 'Lys-9' trimethylation. Isoform 1 can also repress transcription from unmethylated promoters. {ECO:0000269|PubMed:15060159, ECO:0000269|PubMed:9774669}. PTM: Sumoylated with SUMO1 by PIAS1 and PIAS3. Sumoylation affects transcriptional silencing by preventing the interaction with SETDB1. In contrast, sumoylation may increase interaction with AFT7IP (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Nucleus matrix. Nucleus speckle. Chromosome. Note=Nuclear, in a punctate pattern. Associated with euchromatic regions of the chromosomes. Colocalizes with the Ten-1 ICD form of TENM1 in foci associated with the nuclear matrix. SUBUNIT: Interacts with OASL, AFT7IP, AFT7IP2 and BAHD1. Binds CHAF1A and the SUV39H1-CBX5 complex via the MBD domain. Binds MGP via the TRD domain. May be part of the MeCP1 complex. During DNA replication, it recruits SETDB1 to form a S phase-specific complex that facilitates methylation of H3 'Lys-9' during replication-coupled chromatin assembly and is at least composed of the CAF-1 subunit CHAF1A, MBD1 and SETDB1 (By similarity). Isoform 2 interacts with the Ten-1 ICD form of TENM1. {ECO:0000250, ECO:0000269|PubMed:15777793}. DOMAIN: The methyl-CpG-binding domain (MBD) functions both in binding to methylated DNA and in protein interactions. {ECO:0000250}.; DOMAIN: The third CXXC-type zinc finger mediates binding to non-methylated CpG dinucleotides. {ECO:0000250}.; DOMAIN: The transcriptional repression domain (TRD) is involved in transcription repression and in protein interactions. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in kidney, liver and brain. Detected at lower levels in heart, lung, skeletal muscle, spleen and testis. {ECO:0000269|PubMed:9774669}. +P31257 HXC10_MOUSE Homeobox protein Hox-C10 (Homeobox protein Hox-3.6) 342 38,196 Chain (1); Cross-link (3); DNA binding (1); Modified residue (2); Sequence conflict (1) FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. SUBCELLULAR LOCATION: Nucleus. +P01728 LV2A_MOUSE Ig lambda-2 chain V region 117 12,222 Chain (1); Domain (1); Modified residue (1); Non-terminal residue (1); Signal peptide (1) +Q9Z0M9 I18BP_MOUSE Interleukin-18-binding protein (IL-18BP) (Interferon gamma-inducing factor-binding protein) 193 21,257 Chain (1); Disulfide bond (1); Domain (1); Erroneous initiation (1); Glycosylation (4); Sequence caution (1); Sequence conflict (3); Signal peptide (1) FUNCTION: Binds to IL-18 and inhibits its activity. Functions as an inhibitor of the early TH1 cytokine response (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q7TMY8 HUWE1_MOUSE E3 ubiquitin-protein ligase HUWE1 (EC 2.3.2.26) (E3Histone) (HECT, UBA and WWE domain-containing protein 1) (HECT-type E3 ubiquitin transferase HUWE1) (Upstream regulatory element-binding protein 1) (URE-B1) (URE-binding protein 1) 4377 482,635 Active site (1); Alternative sequence (5); Chain (1); Compositional bias (3); Domain (4); Modified residue (52); Sequence conflict (7) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase which mediates ubiquitination and subsequent proteasomal degradation of target proteins. Regulates apoptosis by catalyzing the polyubiquitination and degradation of MCL1. Mediates monoubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base-excision repair. Also ubiquitinates the p53/TP53 tumor suppressor and core histones including H1, H2A, H2B, H3 and H4. Binds to an upstream initiator-like sequence in the preprodynorphin gene (By similarity). Regulates neural differentiation and proliferation by catalyzing the polyubiquitination and degradation of MYCN. May regulate abundance of CDC6 after DNA damage by polyubiquitinating and targeting CDC6 to degradation. Mediates polyubiquitination of PA2G4 (By similarity). {ECO:0000250|UniProtKB:Q7Z6Z7, ECO:0000269|PubMed:15767685, ECO:0000269|PubMed:18488021}. PTM: Phosphorylated on tyrosine; phosphorylation is probably required for its ability to inhibit TP53 transactivation. {ECO:0000250|UniProtKB:Q7Z6Z7}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17823942}. Nucleus {ECO:0000269|PubMed:17823942}. Note=Mainly expressed in the cytoplasm of most tissues, except in the nucleus of spermatogonia, primary spermatocytes and neuronal cells. SUBUNIT: Interacts with isoform p19ARF of CDKN2A which strongly inhibits HUWE1 ubiquitin ligase activity. Interacts with MYCN, POLB and CDC6. Interacts with PA2G4. {ECO:0000250|UniProtKB:Q7Z6Z7}. DOMAIN: The HECT domain mediates inhibition of the transcriptional activity of p53. {ECO:0000250|UniProtKB:Q7Z6Z7}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:17823942}. +P47877 IBP2_MOUSE Insulin-like growth factor-binding protein 2 (IBP-2) (IGF-binding protein 2) (IGFBP-2) (mIGFBP-2) 305 32,847 Chain (1); Disulfide bond (3); Domain (2); Motif (1); Sequence conflict (2); Signal peptide (1) FUNCTION: Inhibits IGF-mediated growth and developmental rates (By similarity). IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. {ECO:0000250}. PTM: O-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Binds IGF2 more than IGF1. DOMAIN: The C-terminus is required for IGF-binding and growth inhibition. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in adult liver, but also in kidney, lung, brain, spleen, testis and ovary. {ECO:0000269|PubMed:7529732}. +Q8R3Y8 I2BP1_MOUSE Interferon regulatory factor 2-binding protein 1 (IRF-2-binding protein 1) (IRF-2BP1) (Probable E3 ubiquitin-protein ligase IRF2BP1) (EC 2.3.2.27) (Probable RING-type E3 ubiquitin transferase IRF2BP1) 584 61,751 Alternative sequence (1); Chain (1); Coiled coil (1); Cross-link (2); Modified residue (10); Region (1); Sequence conflict (5); Zinc finger (1) FUNCTION: Acts as a transcriptional corepressor in a IRF2-dependent manner; this repression is not mediated by histone deacetylase activities. May act as an E3 ligase towards JDP2, enhancing its polyubiquitination. Represses ATF2-dependent transcriptional activation. {ECO:0000250|UniProtKB:Q8IU81}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8IU81}. SUBUNIT: Interacts with IRF2. Part of a corepressor complex containing IRF2 and IRF2BP2. Interacts with JDP2. {ECO:0000250|UniProtKB:Q8IU81}. +P47878 IBP3_MOUSE Insulin-like growth factor-binding protein 3 (IBP-3) (IGF-binding protein 3) (IGFBP-3) 292 31,687 Chain (1); Disulfide bond (3); Domain (2); Glycosylation (3); Modified residue (2); Sequence conflict (6); Signal peptide (1) FUNCTION: IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. Also exhibits IGF-independent antiproliferative and apoptotic effects mediated by its receptor TMEM219/IGFBP-3R. PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000250|UniProtKB:P17936}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Interacts with XLKD1. Binds IGF2 more than IGF1. Forms a ternary complex of about 140 to 150 kDa with IGF1 or IGF2 and a 85 kDa glycoprotein (ALS). Interacts with HN. Interacts with TMEM219 (By similarity). {ECO:0000250}. +P35461 LY6G_MOUSE Lymphocyte antigen 6G (Ly-6G) (Ly-6G.1) (Fragment) 111 11,798 Chain (1); Disulfide bond (5); Domain (1); Lipidation (1); Non-terminal residue (1); Propeptide (1); Signal peptide (1) SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. TISSUE SPECIFICITY: Expressed in bone marrow. +P35330 ICAM2_MOUSE Intercellular adhesion molecule 2 (ICAM-2) (Lymphocyte function-associated AG-1 counter-receptor) (CD antigen CD102) 277 31,390 Beta strand (1); Chain (1); Disulfide bond (3); Domain (2); Glycosylation (5); Helix (1); Mutagenesis (1); Region (1); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 223 247 Helical. {ECO:0000255}. TOPO_DOM 23 222 Extracellular. {ECO:0000255}.; TOPO_DOM 248 277 Cytoplasmic. {ECO:0000255}. FUNCTION: ICAM proteins are ligands for the leukocyte adhesion protein LFA-1 (integrin alpha-L/beta-2). ICAM2 may play a role in lymphocyte recirculation by blocking LFA-1-dependent cell adhesion. It mediates adhesive interactions important for antigen-specific immune response, NK-cell mediated clearance, lymphocyte recirculation, and other cellular interactions important for immune response and surveillance. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, microvillus {ECO:0000269|PubMed:9472040}. Note=Co-localizes with RDX, EZR and MSN in microvilli. {ECO:0000269|PubMed:9472040}. SUBUNIT: Interacts with RDX, EZR and MSN. {ECO:0000269|PubMed:9472040}. TISSUE SPECIFICITY: Expressed in endothelial cells and leukocytes. High levels found in lung. +P51125 ICAL_MOUSE Calpastatin (Calpain inhibitor) 788 84,922 Alternative sequence (8); Chain (1); Cross-link (1); Modified residue (16); Repeat (4) FUNCTION: Specific inhibition of calpain (calcium-dependent cysteine protease). Plays a key role in postmortem tenderization of meat and have been proposed to be involved in muscle protein degradation in living tissue. DOMAIN: Each of the four flexible inhibitory domains can inhibit one calcium-bound calpain molecule by occupying both sides of the active site. {ECO:0000250}. TISSUE SPECIFICITY: Isoform 2 is the major form in all tissues examined. Isoform 1 accounts for 5-10% in tissues such as skeletal muscle, liver and brain, and 30% in myoblasts. Isoforms 4 and 5 are testis-specific. Isoform 6 is highly expressed in heart and skeletal muscle with lower levels in liver, brain and testis. Isoform 7 is expressed at high levels in liver. {ECO:0000269|PubMed:10403772, ECO:0000269|PubMed:10876161}. +Q9EQK7 ICMT_MOUSE Protein-S-isoprenylcysteine O-methyltransferase (EC 2.1.1.100) (Isoprenylcysteine carboxylmethyltransferase) (Prenylated protein carboxyl methyltransferase) (PPMT) (Prenylcysteine carboxyl methyltransferase) (pcCMT) 283 31,790 Chain (1); Sequence conflict (2); Topological domain (9); Transmembrane (8) TRANSMEM 16 32 Helical. {ECO:0000255}.; TRANSMEM 41 58 Helical. {ECO:0000255}.; TRANSMEM 69 86 Helical. {ECO:0000255}.; TRANSMEM 92 111 Helical. {ECO:0000255}.; TRANSMEM 131 148 Helical. {ECO:0000255}.; TRANSMEM 154 173 Helical. {ECO:0000255}.; TRANSMEM 212 227 Helical. {ECO:0000255}.; TRANSMEM 229 243 Helical. {ECO:0000255}. TOPO_DOM 1 15 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 33 40 Lumenal. {ECO:0000255}.; TOPO_DOM 59 68 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 87 91 Lumenal. {ECO:0000255}.; TOPO_DOM 112 130 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 149 153 Lumenal. {ECO:0000255}.; TOPO_DOM 174 211 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 228 228 Lumenal. {ECO:0000255}.; TOPO_DOM 244 283 Cytoplasmic. {ECO:0000255}. FUNCTION: Catalyzes the post-translational methylation of isoprenylated C-terminal cysteine residues. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Highly enriched in adult cerebellum, with a low level expression in other brain regions. +Q3UZ18 ICE2_MOUSE Little elongation complex subunit 2 (Interactor of little elongator complex ELL subunit 2) (NMDA receptor-regulated protein 2) 988 109,879 Alternative sequence (2); Chain (1); Erroneous initiation (1); Frameshift (1); Modified residue (3); Sequence conflict (3) FUNCTION: Component of the little elongation complex (LEC), a complex required to regulate small nuclear RNA (snRNA) gene transcription by RNA polymerase II and III. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15606750}. Note=Colocalizes with COIL in subnuclear Cajal and histone locus bodies. Translocates in the LEC complex to Cajal and histone locus bodies at snRNA genes in a ICE1-dependent manner. Associates to transcriptionally active chromatin at snRNA genes (By similarity). {ECO:0000250}. SUBUNIT: Component of the little elongation complex (LEC), at least composed of ELL (ELL, ELL2 or ELL3), ZC3H8, ICE1 and ICE2. Interacts with ICE1 (via C-terminus domain). Interacts with ELL (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain, kidney, liver and testis. {ECO:0000269|PubMed:11297529}. +Q9JHJ8 ICOSL_MOUSE ICOS ligand (B7 homolog 2) (B7-H2) (B7-like protein Gl50) (B7-related protein 1) (B7RP-1) (LICOS) (CD antigen CD275) 322 35,960 Alternative sequence (1); Chain (1); Compositional bias (2); Disulfide bond (2); Domain (2); Glycosylation (7); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 278 298 Helical. {ECO:0000255}. TOPO_DOM 47 277 Extracellular. {ECO:0000255}.; TOPO_DOM 299 322 Cytoplasmic. {ECO:0000255}. FUNCTION: Ligand for the T-cell-specific cell surface receptor ICOS. Acts as a costimulatory signal for T-cell proliferation and cytokine secretion; induces also B-cell proliferation and differentiation into plasma cells. Could play an important role in mediating local tissue responses to inflammatory conditions, as well as in modulating the secondary immune response by co-stimulating memory T-cell function. During pregnancy, may function to skew the cytokine of maternal T-cells toward immunoprotective Th2 phenotype. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O75144}; Single-pass type I membrane protein {ECO:0000255}. SUBUNIT: Interacts with CTLA4 (in vitro). {ECO:0000250|UniProtKB:O75144}. TISSUE SPECIFICITY: Isoform 1 highest expression in lymphoid tissues, such as spleen (mostly in the marginal zone), lymph nodes (particularly in the cortex and in both primary and secondary follicles), thymus (predominantly in the medulla) and Peyer patches (mostly in the follicles), lower levels in many non-lymphoid tissues, such as brain, heart, kidney, liver, lung, skeletal muscle and testis. Present on freshly isolated splenic B-cells, T-cells, dendritic cells and macrophages. The expression of isoform 2 is restricted to heart, spleen and kidney. +P54071 IDHP_MOUSE Isocitrate dehydrogenase [NADP], mitochondrial (IDH) (EC 1.1.1.42) (ICD-M) (IDP) (NADP(+)-specific ICDH) (Oxalosuccinate decarboxylase) 452 50,906 Beta strand (14); Binding site (6); Chain (1); Frameshift (1); Helix (17); Metal binding (2); Modified residue (29); Nucleotide binding (2); Region (1); Sequence conflict (11); Site (2); Transit peptide (1); Turn (4) FUNCTION: Plays a role in intermediary metabolism and energy production. It may tightly associate or interact with the pyruvate dehydrogenase complex. PTM: Acetylation at Lys-413 dramatically reduces catalytic activity. Deacetylated by SIRT3 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion. SUBUNIT: Homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Heart > kidney >> other tissues. {ECO:0000269|PubMed:11278619}. +Q9JHR7 IDE_MOUSE Insulin-degrading enzyme (EC 3.4.24.56) (Insulin protease) (Insulinase) (Insulysin) 1019 117,772 Active site (1); Binding site (1); Chain (1); Metal binding (3); Modified residue (2); Motif (1); Mutagenesis (1); Nucleotide binding (1) FUNCTION: Plays a role in the cellular breakdown of insulin, IAPP, glucagon, bradykinin, kallidin and other peptides, and thereby plays a role in intercellular peptide signaling. Degrades amyloid formed by APP and IAPP (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21576244}. Cell membrane {ECO:0000269|PubMed:21576244}. Secreted {ECO:0000269|PubMed:21576244}. SUBUNIT: Homodimer. Can form higher oligomers (By similarity). {ECO:0000250}. DOMAIN: The SlyX motif may be involved in the non-conventional secretion of the protein. +P58044 IDI1_MOUSE Isopentenyl-diphosphate Delta-isomerase 1 (EC 5.3.3.2) (Isopentenyl pyrophosphate isomerase 1) (IPP isomerase 1) (IPPI1) 227 26,289 Active site (2); Binding site (4); Chain (1); Domain (1); Metal binding (4); Modified residue (1); Motif (1) Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate: step 1/1. FUNCTION: Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). {ECO:0000250}. SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. +Q8BMJ3 IF1AX_MOUSE Eukaryotic translation initiation factor 1A, X-chromosomal (eIF-1A X isoform) (Eukaryotic translation initiation factor 4C) (eIF-4C) 144 16,460 Chain (1); Domain (1); Sequence conflict (4) FUNCTION: Seems to be required for maximal rate of protein biosynthesis. Enhances ribosome dissociation into subunits and stabilizes the binding of the initiator Met-tRNA(I) to 40 S ribosomal subunits (By similarity). {ECO:0000250}. +Q60872 IF1A_MOUSE Eukaryotic translation initiation factor 1A (eIF-1A) (Eukaryotic translation initiation factor 4C) (eIF-4C) 144 16,502 Chain (1); Domain (1); Sequence conflict (6) FUNCTION: Seems to be required for maximal rate of protein biosynthesis. Enhances ribosome dissociation into subunits and stabilizes the binding of the initiator Met-tRNA(I) to 40 S ribosomal subunits. +Q8R033 LYRM2_MOUSE LYR motif-containing protein 2 88 10,380 Chain (1) +Q9DA03 LYRM7_MOUSE Complex III assembly factor LYRM7 (LYR motif-containing protein 7) 104 12,047 Chain (1); Erroneous initiation (1); Modified residue (1) FUNCTION: Assembly factor required for Rieske Fe-S protein UQCRFS1 incorporation into the cytochrome b-c1 (CIII) complex. Functions as a chaperone, binding to this subunit within the mitochondrial matrix and stabilizing it prior to its translocation and insertion into the late CIII dimeric intermediate within the mitochondrial inner membrane (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. SUBUNIT: Interacts with UQCRFS1. {ECO:0000250}. +Q3UN90 LYRM9_MOUSE LYR motif-containing protein 9 78 9,310 Chain (1); Sequence conflict (1) +O88477 IF2B1_MOUSE Insulin-like growth factor 2 mRNA-binding protein 1 (IGF2 mRNA-binding protein 1) (IMP-1) (Coding region determinant-binding protein) (CRD-BP) (IGF-II mRNA-binding protein 1) (VICKZ family member 1) (Zipcode-binding protein 1) (ZBP-1) 577 63,451 Chain (1); Domain (6); Modified residue (4); Region (3); Sequence conflict (2) FUNCTION: RNA-binding factor that recruits target transcripts to cytoplasmic protein-RNA complexes (mRNPs). This transcript 'caging' into mRNPs allows mRNA transport and transient storage. It also modulates the rate and location at which target transcripts encounter the translational apparatus and shields them from endonuclease attacks or microRNA-mediated degradation. Regulates localized beta-actin/ACTB mRNA translation, a crucial process for cell polarity, cell migration and neurite outgrowth. Co-transcriptionally associates with the ACTB mRNA in the nucleus. This binding involves a conserved 54-nucleotide element in the ACTB mRNA 3'-UTR, known as the 'zipcode'. The RNP thus formed is exported to the cytoplasm, binds to a motor protein and is transported along the cytoskeleton to the cell periphery. During transport, prevents ACTB mRNA from being translated into protein. When the RNP complex reaches its destination near the plasma membrane, IGF2BP1 is phosphorylated. This releases the mRNA, allowing ribosomal 40S and 60S subunits to assemble and initiate ACTB protein synthesis. Monomeric ACTB then assembles into the subcortical actin cytoskeleton (By similarity). During neuronal development, key regulator of neurite outgrowth, growth cone guidance and neuronal cell migration, presumably through the spatiotemporal fine tuning of protein synthesis, such as that of ACTB (By similarity). May regulate mRNA transport to activated synapses (By similarity). Binds to the 3'-UTR of CD44 mRNA and stabilizes it, hence promotes cell adhesion and invadopodia formation in cancer cells (By similarity). Binds to the oncofetal H19 transcript and regulates its localization (By similarity). Binds to and stabilizes BTRC/FBW1A mRNA (By similarity). Binds to the adenine-rich autoregulatory sequence (ARS) located in PABPC1 mRNA and represses its translation. PABPC1 mRNA-binding is stimulated by PABPC1 protein. Prevents BTRC/FBW1A mRNA degradation by disrupting microRNA-dependent interaction with AGO2 (By similarity). During cellular stress, such as oxidative stress or heat shock, stabilizes target mRNAs that are recruited to stress granules, including CD44, IGF2, MAPK4, MYC, PTEN, RAPGEF2 and RPS6KA5 transcripts (By similarity). Interacts with GAP43 transcript and transports it to axons. Binds to the 3'-UTR of IGF2 mRNA by a mechanism of cooperative and sequential dimerization and regulates IGF2 mRNA subcellular localization and translation. Binds to MYC mRNA, in the coding region instability determinant (CRD) of the open reading frame (ORF), hence prevents MYC cleavage by endonucleases and possibly microRNA targeting to MYC-CRD. Binds to and stabilizes ABCB1/MDR-1 mRNA. Binds to the neuron-specific TAU mRNA and regulates its localization. Plays a direct role in the transport and translation of transcripts required for axonal regeneration in adult sensory neurons. During interstinal wound repair, interacts with and stabilizes PTGS2 transcript. PTGS2 mRNA stabilization may be crucial for colonic mucosal wound healing. {ECO:0000250, ECO:0000269|PubMed:15355996, ECO:0000269|PubMed:17264115, ECO:0000269|PubMed:21964071, ECO:0000269|PubMed:22465430}. PTM: Phosphorylated. Phosphorylation may impair association with ACTB mRNA and hence abolishes translational repression (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, perinuclear region {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cell projection, dendritic spine {ECO:0000250}. Cell projection, growth cone {ECO:0000250}. Cell projection, filopodium {ECO:0000250}. Cell projection, axon {ECO:0000250}. Note=In the nucleus, located in discrete foci, coinciding with the sites of ACTB transcription (By similarity). In the cytoplasm, localizes in cytoplasmic mRNP granules. Colocalizes with microtubules in growth cone filopodia and along neurites in neuronal cells (By similarity). Cytoplasmic colocalization with ACTB mRNA is partially lost at the cell periphery, suggesting release of the transcript (By similarity). In hippocampal neurons, predominantly located within dendrites, particularly at dendritic branching points in young cells, compared to axons (By similarity). In axons, predominantly found in axonal branches and their growth cones (By similarity). In neuronal processes, exhibits fast retrograde and anterograde movements, when associated with ACTB mRNA; this motility is lost when the association is inhibited (By similarity). Dendritic levels are regulated by neuronal activity and glutaminergic signals: they are increased by KCl-induced depolarization, which induces rapid efflux from the cell body into dendrites, and decreased by NMDA receptor agonists (By similarity). In motile cells, such as migrating fibroblasts, localizes to leading edges where it colocalizes with microtubules and microfilaments and to retracting tails (By similarity). In motile cells, transported towards the leading edge into the cortical region of the lamellipodia where it is connected to microfilaments (By similarity). In response to cellular stress, such as oxidative stress or heat shock, recruited to stress granules, but not to processing bodies (By similarity). {ECO:0000250}. SUBUNIT: Can form homodimers and heterodimers with IGF2BP1 and IGF2BP3 (By similarity). Component of the coding region determinant (CRD)-mediated complex, composed of DHX9, HNRNPU, IGF2BP1, SYNCRIP and YBX1 (By similarity). Identified in a mRNP complex, at least composed of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1 (By similarity). Associates with mRNP complex (By similarity). Interacts with FMR1 (By similarity). Component of a multisubunit autoregulatory RNP complex (ARC), at least composed of IGF2BP1, PABPC1 and CSDE1. Interacts with AGO1 and AGO2 (By similarity). Interacts, through domains KH3 and KH4, with PABPC1 in an RNA-independent manner (By similarity). Component of a TAU mRNP complex, at least composed of IGF2BP1, ELAVL4 and G3BP. Interacts with ELAVL4 in an RNA-dependent manner. Associates with microtubules and polysomes. {ECO:0000250, ECO:0000269|PubMed:15086518}. DOMAIN: Domain KH3 and KH4 are the major RNA-binding modules, although KH1 and KH2 may also contribute. KH1 and KH2, and possibly KH3 and KH4, promote the formation of higher ordered protein-RNA complexes, which may be essential for IGF2BP1 cytoplasmic retention. KH domains are required for RNA-dependent homo- and heterooligomerization and for localization to stress granules. KH3 and KH4 mediate association with the cytoskeleton. Two nuclear export signals (NES) have been identified in KH2 and KH4 domains, respectively. Only KH2 NES is XPO1-dependent. Both NES may be redundant, since individual in vitro mutations do not affect subcellular location of the full-length protein. TISSUE SPECIFICITY: Expressed in zygotes and blastocysts (at protein level). Expressed in brain, skeletal muscle, trophoblasts of placenta, oocytes and spermatogonia (at protein level). Expressed in testis and ovary. Following colon injury, expressed in the wound bed mesenchyme during the first phase of repair, probably by colonic mesenchymal stem cells (at protein level). {ECO:0000269|PubMed:16049158, ECO:0000269|PubMed:21964071, ECO:0000269|PubMed:22465430, ECO:0000269|PubMed:9891060}. +Q5SF07 IF2B2_MOUSE Insulin-like growth factor 2 mRNA-binding protein 2 (IGF2 mRNA-binding protein 2) (IMP-2) (IGF-II mRNA-binding protein 2) (VICKZ family member 2) 592 65,584 Alternative sequence (1); Chain (1); Domain (6); Modified residue (4); Sequence conflict (1) FUNCTION: RNA-binding factor that recruits target transcripts to cytoplasmic protein-RNA complexes (mRNPs). This transcript 'caging' into mRNPs allows mRNA transport and transient storage. It also modulates the rate and location at which target transcripts encounter the translational apparatus and shields them from endonuclease attacks or microRNA-mediated degradation (By similarity). Binds to the 5'-UTR of the insulin-like growth factor 2 (IGF2) mRNAs. Binding is isoform-specific. Binds to beta-actin/ACTB and MYC transcripts (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Localizes at the connecting piece and the tail of the spermatozoa. In response to cellular stress, such as oxidative stress, recruited to stress granules (By similarity). {ECO:0000250}. SUBUNIT: Can form homooligomers and heterooligomers with IGF2BP1 and IGF2BP3 in an RNA-dependent manner. Interacts with HNRPD and IGF2BP1. Interacts with ELAVL1, DHX9 and HNRNPU (By similarity). {ECO:0000250}. DOMAIN: Domain KH3 and KH4 are the major RNA-binding modules, although KH1 and KH2 may also contribute. The contribution to RNA-binding of individual KH domains may be target-specific. KH1 and KH2, and possibly KH3 and KH4, promote the formation of higher ordered protein-RNA complexes, which may be essential for IGF2BP1 cytoplasmic retention. KH domains are required for RNA-dependent homo- and heterooligomerization and for localization to stress granules (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in oocytes, granulosa cells of small and growing follicles and Leydig cells of the testis (at protein level). Expressed in testis and ovary. {ECO:0000269|PubMed:16049158}. +O35344 IMA4_MOUSE Importin subunit alpha-4 (Importin alpha Q2) (Qip2) (Karyopherin subunit alpha-3) 521 57,773 Chain (1); Domain (1); Initiator methionine (1); Modified residue (4); Motif (1); Region (2); Repeat (10) FUNCTION: Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. In vitro, mediates the nuclear import of human cytomegalovirus UL84 by recognizing a non-classical NLS. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Forms a complex with importin subunit beta-1. Interacts with NCBP2/CBP20 and NCBP3. {ECO:0000250|UniProtKB:O00505}. DOMAIN: Consists of an N-terminal hydrophilic region, a hydrophobic central region composed of 10 repeats, and a short hydrophilic C-terminus. The N-terminal hydrophilic region contains the importin beta binding domain (IBB domain), which is sufficient for binding importin beta and essential for nuclear protein import.; DOMAIN: The IBB domain is thought to act as an intrasteric autoregulatory sequence by interacting with the internal autoinhibitory NLS. Binding of KPNB1 probably overlaps the internal NLS and contributes to a high affinity for cytoplasmic NLS-containing cargo substrates. After dissociation of the importin/substrate complex in the nucleus the internal autohibitory NLS contributes to a low affinity for nuclear NLS-containing proteins (By similarity). {ECO:0000250}.; DOMAIN: The major and minor NLS binding sites are mainly involved in recognition of simple or bipartite NLS motifs. Structurally located within in a helical surface groove they contain several conserved Trp and Asn residues of the corresponding third helices (H3) of ARM repeats which mainly contribute to binding (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Detected more or less in all tissues examined (Ehrlich ascites tumor cells, testis, kidney, spleen, liver, heart, lung, thymus, skeletal muscle, cerebellum and brain (without cerebellum)). +Q6GQV1 INY2B_MOUSE INSYN2B protein (Inhibitory synaptic factor family member 2B) 535 59,102 Chain (1); Coiled coil (1) +Q9D752 MD2L2_MOUSE Mitotic spindle assembly checkpoint protein MAD2B (Mitotic arrest deficient 2-like protein 2) (MAD2-like protein 2) 211 24,402 Beta strand (11); Chain (1); Domain (1); Helix (8); Region (1); Sequence conflict (1); Turn (2) FUNCTION: Adapter protein able to interact with different proteins and involved in different biological processes. Mediates the interaction between the error-prone DNA polymerase zeta catalytic subunit REV3L and the inserter polymerase REV1, thereby mediating the second polymerase switching in translesion DNA synthesis. Translesion DNA synthesis releases the replication blockade of replicative polymerases, stalled in presence of DNA lesions. Component of the shieldin complex, which plays an important role in repair of DNA double-stranded breaks (DSBs). During G1 and S phase of the cell cycle, the complex functions downstream of TP53BP1 to promote non-homologous end joining (NHEJ) and suppress DNA end resection. Mediates various NHEJ-dependent processes including immunoglobulin class-switch recombination, and fusion of unprotected telomeres. May also regulate another aspect of cellular response to DNA damage through regulation of the JNK-mediated phosphorylation and activation of the transcriptional activator ELK1. Inhibits the FZR1- and probably CDC20-mediated activation of the anaphase promoting complex APC thereby regulating progression through the cell cycle. Regulates TCF7L2-mediated gene transcription and may play a role in epithelial-mesenchymal transdifferentiation. {ECO:0000250|UniProtKB:Q9UI95}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UI95}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9UI95}. Cytoplasm {ECO:0000250|UniProtKB:Q9UI95}. Chromosome {ECO:0000250|UniProtKB:Q9UI95}. Note=Recruited to sites of chromosomal double-stranded breaks during G1 and S phase of the cell cycle. {ECO:0000250|UniProtKB:Q9UI95}. SUBUNIT: Homooligomer (By similarity). Heterodimer with REV3L (By similarity). This dimer forms the minimal DNA polymerase zeta complex (Pol-zeta2), with REV3L bearing DNA polymerase catalytic activity, although its activity is very low in this context (By similarity). Component of the tetrameric Pol-zeta complex (Pol-zeta4), which consists of REV3L, MAD2L2, POLD2 and POLD3; Pol-zeta4 is the fully active form of DNA polymerase zeta (By similarity). Component of the shieldin complex, consisting of SHLD1, SHLD2, SHLD3 and MAD2L2/REV7. Within the complex, SHLD2 forms a scaffold which interacts with a SHLD3-MAD2L2 subcomplex via its N-terminus, and with SHLD1 via its C-terminus (By similarity). Interacts with REV1 (PubMed:14657033). Interacts with ADAM9 (By similarity). Interacts with CHAMP1 (By similarity). Interacts with FZR1 (in complex with the anaphase promoting complex APC) (By similarity). May interact with CDC20 (By similarity). Interacts with RAN (By similarity). Interacts with ELK1; the interaction is direct and recruits MAD2L2 to ELK1-specific promoters (By similarity). May interact with the JNK kinases MAPK8 and/or MAPK9 to stimulate ELK1 phosphorylation and transcriptional activity upon DNA damage (By similarity). Interacts with TCF7L2; prevents its binding to promoters and negatively modulates its transcriptional activity (By similarity). Interacts with YY1AP1 (By similarity). Interacts with PRCC; the interaction is direct (By similarity). Interacts with POGZ (By similarity). {ECO:0000250|UniProtKB:Q9UI95, ECO:0000269|PubMed:14657033}. +Q0PMG2 MDGA1_MOUSE MAM domain-containing glycosylphosphatidylinositol anchor protein 1 956 106,047 Chain (1); Disulfide bond (6); Domain (8); Glycosylation (6); Lipidation (1); Propeptide (1); Sequence conflict (2); Signal peptide (1) FUNCTION: Required for radial migration of cortical neurons in the superficial layer of the neocortex. Plays a role in the formation or maintenance of inhibitory synapses. May function by inhibiting the activity of NLGN2. {ECO:0000269|PubMed:16641224, ECO:0000269|PubMed:23248271}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. Note=Associated with lipid rafts. {ECO:0000250|UniProtKB:Q8NFP4}. SUBUNIT: Interacts heterophilically through its MAM domain with proteins in axon-rich regions and through its Ig-like domains with proteins in differentiating muscle. Interacts (through the Ig-like domains) with NLGN2. {ECO:0000250}. TISSUE SPECIFICITY: Expressed by neurons in layers 2 and 3 of the cortex during their migration and settling in the cortical plate. Also found in layers 4 and 6a. From E9.5-E13.5, detected in the marginal zone of the developing cortex. At E16.5, modest expression is found in the intermediate zone. At postnatal day 0, evident in the superficial cortical plate. By postnatal day 7, expression is limited to layers 2 and 3 throughout most of the cortex. {ECO:0000269|PubMed:16641224, ECO:0000269|PubMed:16959869}. +Q7TS72 IP3KC_MOUSE Inositol-trisphosphate 3-kinase C (EC 2.7.1.127) (Inositol 1,4,5-trisphosphate 3-kinase C) (IP3 3-kinase C) (IP3K C) (InsP 3-kinase C) 678 74,493 Binding site (6); Chain (1); Modified residue (3); Motif (1); Nucleotide binding (1); Region (3); Sequence conflict (1) FUNCTION: Can phosphorylate inositol 2,4,5-triphosphate to inositol 2,4,5,6-tetraphosphate. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Shuttles actively between nucleus and cytoplasm with both nuclear import and nuclear export activity. {ECO:0000250}. +Q5F204 MDH1B_MOUSE Putative malate dehydrogenase 1B (EC 1.1.1.-) 500 56,297 Chain (1); Erroneous initiation (2); Sequence conflict (1) +Q6PD10 IP6K1_MOUSE Inositol hexakisphosphate kinase 1 (InsP6 kinase 1) (EC 2.7.4.21) (Inositol hexaphosphate kinase 1) 433 49,307 Chain (1); Modified residue (1); Region (1); Sequence conflict (1) FUNCTION: Converts inositol hexakisphosphate (InsP6) to diphosphoinositol pentakisphosphate (InsP7/PP-InsP5). Converts 1,3,4,5,6-pentakisphosphate (InsP5) to PP-InsP4. {ECO:0000269|PubMed:10574768}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in brain and testis. Detected at much lower levels in heart, kidney, liver, lung and spleen. {ECO:0000269|PubMed:10574768}. +Q80V72 IP6K2_MOUSE Inositol hexakisphosphate kinase 2 (InsP6 kinase 2) (EC 2.7.4.21) (P(i)-uptake stimulator) (PiUS) 448 51,644 Chain (1); Region (1); Sequence conflict (1) FUNCTION: Converts inositol hexakisphosphate (InsP6) to diphosphoinositol pentakisphosphate (InsP7/PP-InsP5). Converts 1,3,4,5,6-pentakisphosphate (InsP5) to PP-InsP4. Was first identified because of its ability to stimulate Na(+)-dependent phosphate cotransport (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in brain and lung, and at slightly lower levels in liver, kidney and testis. {ECO:0000269|PubMed:10574768}. +Q8BWD2 IP6K3_MOUSE Inositol hexakisphosphate kinase 3 (InsP6 kinase 3) (EC 2.7.4.21) (Inositol hexaphosphate kinase 3) 396 44,418 Chain (1); Region (1) FUNCTION: Converts inositol hexakisphosphate (InsP6) to diphosphoinositol pentakisphosphate (InsP7/PP-InsP5). Converts 1,3,4,5,6-pentakisphosphate (InsP5) to PP-InsP4 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in cerebellum, brain cortex, kidney, thymus and lung. Detected at lower levels in hippocampus, testis, heart and olfactory bulb. {ECO:0000269|PubMed:11502751}. +Q91ZY2 HRH4_MOUSE Histamine H4 receptor (H4R) (HH4R) 391 44,249 Chain (1); Disulfide bond (1); Glycosylation (2); Topological domain (8); Transmembrane (7) TRANSMEM 20 40 Helical; Name=1. {ECO:0000255}.; TRANSMEM 53 73 Helical; Name=2. {ECO:0000255}.; TRANSMEM 88 108 Helical; Name=3. {ECO:0000255}.; TRANSMEM 132 152 Helical; Name=4. {ECO:0000255}.; TRANSMEM 175 195 Helical; Name=5. {ECO:0000255}.; TRANSMEM 307 327 Helical; Name=6. {ECO:0000255}.; TRANSMEM 344 364 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 19 Extracellular. {ECO:0000255}.; TOPO_DOM 41 52 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 74 87 Extracellular. {ECO:0000255}.; TOPO_DOM 109 131 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 153 174 Extracellular. {ECO:0000255}.; TOPO_DOM 196 306 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 328 343 Extracellular. {ECO:0000255}.; TOPO_DOM 365 391 Cytoplasmic. {ECO:0000255}. FUNCTION: The H4 subclass of histamine receptors could mediate the histamine signals in peripheral tissues. Displays a significant level of constitutive activity (spontaneous activity in the absence of agonist) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q9QZS6 HS3SB_MOUSE Heparan sulfate glucosamine 3-O-sulfotransferase 3B1 (EC 2.8.2.30) (Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 3B1) (3-OST-3B) (Heparan sulfate 3-O-sulfotransferase 3B1) (m3-OST-3B) 390 43,296 Binding site (2); Chain (1); Disulfide bond (1); Glycosylation (3); Nucleotide binding (2); Region (3); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 33 53 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 32 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 54 390 Lumenal. {ECO:0000255}. FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to an N-unsubstituted glucosamine linked to a 2-O-sulfo iduronic acid unit on heparan sulfate. Catalyzes the O-sulfation of glucosamine in IdoUA2S-GlcNS and also in IdoUA2S-GlcNH2. Unlike 3-OST-1, does not convert non-anticoagulant heparan sulfate to anticoagulant heparan sulfate (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305|PubMed:10520990}; Single-pass type II membrane protein {ECO:0000305|PubMed:10520990}. +P97292 HRH2_MOUSE Histamine H2 receptor (H2R) (HH2R) (Gastric receptor I) 397 44,794 Chain (1); Disulfide bond (1); Glycosylation (1); Lipidation (1); Sequence conflict (2); Site (3); Topological domain (8); Transmembrane (7) TRANSMEM 23 44 Helical; Name=1. {ECO:0000255}.; TRANSMEM 58 81 Helical; Name=2. {ECO:0000255}.; TRANSMEM 93 114 Helical; Name=3. {ECO:0000255}.; TRANSMEM 135 159 Helical; Name=4. {ECO:0000255}.; TRANSMEM 180 203 Helical; Name=5. {ECO:0000255}.; TRANSMEM 234 257 Helical; Name=6. {ECO:0000255}.; TRANSMEM 267 288 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 22 Extracellular. {ECO:0000255}.; TOPO_DOM 45 57 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 82 92 Extracellular. {ECO:0000255}.; TOPO_DOM 115 134 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 160 179 Extracellular. {ECO:0000255}.; TOPO_DOM 204 233 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 258 266 Extracellular. {ECO:0000255}.; TOPO_DOM 289 397 Cytoplasmic. {ECO:0000255}. FUNCTION: The H2 subclass of histamine receptors mediates gastric acid secretion. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q2TPA8 HSDL2_MOUSE Hydroxysteroid dehydrogenase-like protein 2 (EC 1.-.-.-) 490 54,208 Active site (1); Binding site (3); Chain (1); Compositional bias (1); Domain (1); Frameshift (1); Modified residue (2); Nucleotide binding (1); Sequence conflict (5) FUNCTION: Has apparently no steroid dehydrogenase activity. {ECO:0000250}. SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:16240713}. +Q8BM72 HSP13_MOUSE Heat shock 70 kDa protein 13 (Microsomal stress-70 protein ATPase core) (Stress-70 protein chaperone microsome-associated 60 kDa protein) 471 51,709 Alternative sequence (2); Chain (1); Erroneous initiation (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Has peptide-independent ATPase activity. {ECO:0000250}. SUBCELLULAR LOCATION: Microsome {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. SUBUNIT: Binds UBQLN2. {ECO:0000250}. +Q8K572 HUS1B_MOUSE Checkpoint protein HUS1B (mHUS1B) 276 31,251 Chain (1) SUBUNIT: Interacts with RAD1 and RAD9B. {ECO:0000250}. +Q3UQS2 LSME1_MOUSE Leucine-rich single-pass membrane protein 1 128 14,186 Alternative sequence (1); Chain (1); Coiled coil (1); Modified residue (1); Transmembrane (1) TRANSMEM 66 86 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +P19973 LSP1_MOUSE Lymphocyte-specific protein 1 (52 kDa phosphoprotein) (pp52) (Lymphocyte-specific antigen WP34) (S37 protein) 330 36,714 Alternative sequence (1); Chain (1); Modified residue (9); Mutagenesis (3); Sequence conflict (9) FUNCTION: May play a role in mediating neutrophil activation and chemotaxis. {ECO:0000269|PubMed:17481585}. PTM: Phosphorylated by casein kinase II, protein kinase C and MAPKAPK2. Phosphorylation by PKC induces translocation from membrane to cytoplasm. Phosphorylation by MAPKAPK2 may regulate neutrophil chemotaxis. {ECO:0000269|PubMed:17481585, ECO:0000269|PubMed:7775393, ECO:0000269|PubMed:8340356}. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. TISSUE SPECIFICITY: Isoform 1 is expressed in normal mouse B and T-lymphocytes and in transformed B-cells but not (or in smaller amounts) in nine T-lymphoma lines tested. Isoform 2 is expressed in non-lymphoid cell lines (myocytes, stromal cells, fibroblasts). +P18530 HVM59_MOUSE Ig heavy chain V region 7-39 117 12,972 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (5); Signal peptide (1) +P70321 HXB13_MOUSE Homeobox protein Hox-B13 286 30,963 Chain (1); DNA binding (1); Region (3) FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Binds preferentially to methylated DNA (By similarity). {ECO:0000250|UniProtKB:Q92826}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Heterodimer with MEIS1 and MEIS2. {ECO:0000250|UniProtKB:Q92826}. TISSUE SPECIFICITY: Exhibits both spatial and temporal colinearity within the main body axis. At E12.5, is detected in hindgut, urogenital tract, spinal chord and tailbud. Not detected in secondary axes such as the limb and the genital tubercule. +P28359 HXD10_MOUSE Homeobox protein Hox-D10 (Homeobox protein Hox-4.5) (Homeobox protein Hox-5.3) 340 38,328 Chain (1); DNA binding (1); Modified residue (2); Sequence conflict (6) FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. SUBCELLULAR LOCATION: Nucleus. +P01810 HVM40_MOUSE Ig heavy chain V region J539 119 13,240 Beta strand (12); Chain (1); Helix (2); Non-terminal residue (1); Turn (2) +P70312 HYAS2_MOUSE Hyaluronan synthase 2 (EC 2.4.1.212) (Hyaluronate synthase 2) (Hyaluronic acid synthase 2) (HA synthase 2) 552 63,510 Chain (1); Sequence conflict (1); Topological domain (8); Transmembrane (7) TRANSMEM 12 32 Helical; Name=1. {ECO:0000255}.; TRANSMEM 46 66 Helical; Name=2. {ECO:0000255}.; TRANSMEM 375 395 Helical; Name=3. {ECO:0000255}.; TRANSMEM 403 423 Helical; Name=4. {ECO:0000255}.; TRANSMEM 430 450 Helical; Name=5. {ECO:0000255}.; TRANSMEM 476 496 Helical; Name=6. {ECO:0000255}.; TRANSMEM 511 531 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 11 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 33 45 Extracellular. {ECO:0000255}.; TOPO_DOM 67 374 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 396 402 Extracellular. {ECO:0000255}.; TOPO_DOM 424 429 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 451 475 Extracellular. {ECO:0000255}.; TOPO_DOM 497 510 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 532 552 Extracellular. {ECO:0000255}. Glycan biosynthesis; hyaluronan biosynthesis. FUNCTION: Catalyzes the addition of GlcNAc or GlcUA monosaccharides to the nascent hyaluronan polymer. Therefore, it is essential to hyaluronan synthesis a major component of most extracellular matrices that has a structural role in tissues architectures and regulates cell adhesion, migration and differentiation. This is one of the isozymes catalyzing that reaction and it is particularly responsible for the synthesis of high molecular mass hyaluronan. Required for the transition of endocardial cushion cells into mesenchymal cells, a process crucial for heart development. May also play a role in vasculogenesis. High molecular mass hyaluronan also play a role in early contact inhibition a process which stops cell growth when cells come into contact with each other or the extracellular matrix. {ECO:0000269|PubMed:10930438}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in heart, brain, spleen, lung and skeletal muscle. +Q8R4U7 LUZP1_MOUSE Leucine zipper protein 1 (Leucine zipper motif-containing protein) 1068 119,311 Chain (1); Coiled coil (1); Initiator methionine (1); Modified residue (15); Sequence conflict (27) SUBCELLULAR LOCATION: Nucleus. Note=Also detected in soma and dendrites of neurons. {ECO:0000250}. TISSUE SPECIFICITY: Predominantly expressed in the brain (at protein level). {ECO:0000269|PubMed:8812416}. +P01724 LV1B_MOUSE Ig lambda-1 chain V regions MOPC 104E/RPC20/J558/S104 129 13,479 Beta strand (11); Chain (1); Domain (1); Helix (2); Modified residue (1); Non-terminal residue (1); Signal peptide (1); Turn (2) +Q8K5B8 HXC12_MOUSE Homeobox protein Hox-C12 (Homeobox protein Hox-3.8) 280 30,345 Chain (1); DNA binding (1) FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. +Q8VC12 HUTU_MOUSE Urocanate hydratase (Urocanase) (EC 4.2.1.49) (Imidazolonepropionate hydrolase) 676 74,590 Binding site (4); Chain (1); Modified residue (1); Nucleotide binding (5); Sequence conflict (2) Amino-acid degradation; L-histidine degradation into L-glutamate; N-formimidoyl-L-glutamate from L-histidine: step 2/3. +P70225 I11RB_MOUSE Interleukin-11 receptor subunit alpha-2 (IL-11 receptor subunit alpha-2) (IL-11R subunit alpha-2) (IL-11R-alpha-2) (IL-11RA2) (Interleukin-11 receptor subunit beta) (IL-11 receptor subunit beta) (IL-11R subunit beta) (IL-11R-beta) (IL-11RB) 432 46,731 Chain (1); Disulfide bond (3); Domain (3); Glycosylation (2); Motif (1); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 373 393 Helical. {ECO:0000255}. TOPO_DOM 24 372 Extracellular. {ECO:0000255}.; TOPO_DOM 394 432 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for interleukin-11. The receptor systems for IL6, LIF, OSM, CNTF, IL11 and CT1 can utilize IL6ST for initiating signal transmission. The IL11/IL11RA/IL6ST complex may be involved in the control of proliferation and/or differentiation of skeletogenic progenitor or other mesenchymal cells. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: On ligand binding, forms a multimer complex with IL6ST/gp130. {ECO:0000250}. TISSUE SPECIFICITY: Expression restricted to testis, lymph node and thymus. Highest level in testis. {ECO:0000269|PubMed:9073505}. +Q9Z0N2 IF2H_MOUSE Eukaryotic translation initiation factor 2 subunit 3, Y-linked (Eukaryotic translation initiation factor 2 subunit gamma, Y-linked) (eIF-2-gamma Y) (Spermatogonial proliferation factor) (Spy) 472 51,131 Chain (1); Domain (1); Initiator methionine (1); Modified residue (2); Nucleotide binding (3); Region (5) FUNCTION: As a subunit of eukaryotic initiation factor 2 (eIF2), involved in the early steps of protein synthesis. In the presence of GTP, eIF2 forms a ternary complex with initiator tRNA Met-tRNAi and then recruits the 40S ribosomal complex, a step that determines the rate of protein translation. This step is followed by mRNA binding to form the 43S pre-initiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF2 and release of an eIF2-GDP binary complex. In order for eIF2 to recycle and catalyze another round of initiation, the GDP bound to eIF2 must exchange with GTP by way of a reaction catalyzed by eIF2B (By similarity). Along with its paralog on chromosome X, may contribute to spermatogenesis up to the round spermatid stage (PubMed:26823431). {ECO:0000250, ECO:0000269|PubMed:11528390, ECO:0000269|PubMed:25579647, ECO:0000269|PubMed:26823431}. SUBUNIT: The eukaryotic translation initiation factor 2 complex/eIF2 is a heterotrimer composed of an alpha subunit, also called subunit 1 (encoded by EIF2S1), a beta subunit, also called subunit 2 (encoded by EIF2S2) and a gamma subunit, also called subunit 3 (encoded by 2 homologous genes Eif2s3x and Eif2s3y). {ECO:0000250|UniProtKB:P41091}. TISSUE SPECIFICITY: Widely expressed. In the adult brain, high levels in hippocampus, habenula, hypothalamic nuclei and cerebellum. Also expressed in embryonic brain. {ECO:0000269|PubMed:12023983, ECO:0000269|PubMed:16325480, ECO:0000269|PubMed:9736774}. +O08663 MAP2_MOUSE Methionine aminopeptidase 2 (MAP 2) (MetAP 2) (EC 3.4.11.18) (Initiation factor 2-associated 67 kDa glycoprotein) (p67) (p67eIF2) (Peptidase M) 478 52,922 Binding site (2); Chain (1); Compositional bias (2); Glycosylation (1); Initiator methionine (1); Metal binding (7); Modified residue (2) FUNCTION: Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). {ECO:0000255|HAMAP-Rule:MF_03175}.; FUNCTION: Protects eukaryotic initiation factor EIF2S1 from translation-inhibiting phosphorylation by inhibitory kinases such as EIF2AK2/PKR and EIF2AK1/HCR. Plays a critical role in the regulation of protein synthesis. {ECO:0000255|HAMAP-Rule:MF_03175}. PTM: Contains approximately 12 O-linked N-acetylglucosamine (GlcNAc) residues. O-glycosylation is required for EIF2S1 binding. {ECO:0000255|HAMAP-Rule:MF_03175}. SUBCELLULAR LOCATION: Cytoplasm. Note=About 30% of expressed METAP2 associates with polysomes. {ECO:0000255|HAMAP-Rule:MF_03175}. SUBUNIT: Binds EIF2S1 at low magnesium concentrations. Interacts strongly with the eIF-2 gamma-subunit EIF2S3. {ECO:0000255|HAMAP-Rule:MF_03175}. +O88351 IKKB_MOUSE Inhibitor of nuclear factor kappa-B kinase subunit beta (I-kappa-B-kinase beta) (IKK-B) (IKK-beta) (IkBKB) (EC 2.7.11.10) (I-kappa-B kinase 2) (IKK2) (Nuclear factor NF-kappa-B inhibitor kinase beta) (NFKBIKB) 757 86,690 Active site (1); Binding site (1); Chain (1); Cross-link (1); Domain (1); Modified residue (14); Nucleotide binding (1); Region (2); Sequence conflict (7) FUNCTION: Serine kinase that plays an essential role in the NF-kappa-B signaling pathway which is activated by multiple stimuli such as inflammatory cytokines, bacterial or viral products, DNA damages or other cellular stresses. Acts as part of the canonical IKK complex in the conventional pathway of NF-kappa-B activation and phosphorylates inhibitors of NF-kappa-B on 2 critical serine residues. These modifications allow polyubiquitination of the inhibitors and subsequent degradation by the proteasome. In turn, free NF-kappa-B is translocated into the nucleus and activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis. In addition to the NF-kappa-B inhibitors, phosphorylates several other components of the signaling pathway including NEMO/IKBKG, NF-kappa-B subunits RELA and NFKB1, as well as IKK-related kinases TBK1 and IKBKE. IKK-related kinase phosphorylations may prevent the overproduction of inflammatory mediators since they exert a negative regulation on canonical IKKs. Phosphorylates FOXO3, mediating the TNF-dependent inactivation of this pro-apoptotic transcription factor. Also phosphorylates other substrates including NCOA3, BCL10 and IRS1. Within the nucleus, acts as an adapter protein for NFKBIA degradation in UV-induced NF-kappa-B activation. {ECO:0000250|UniProtKB:O14920}. PTM: Upon cytokine stimulation, phosphorylated on Ser-177 and Ser-181 by MEKK1 and/or MAP3K14/NIK as well as TBK1 and PRKCZ; which enhances activity. Once activated, autophosphorylates on the C-terminal serine cluster; which decreases activity and prevents prolonged activation of the inflammatory response. Phosphorylated by the IKK-related kinases TBK1 and IKBKE, which is associated with reduced CHUK/IKKA and IKBKB activity and NF-kappa-B-dependent gene transcription. Dephosphorylated at Ser-177 and Ser-181 by PPM1A and PPM1B. {ECO:0000250|UniProtKB:O14920}.; PTM: Ubiquitinated. Monoubiquitination involves TRIM21 that leads to inhibition of Tax-induced NF-kappa-B signaling. 'Ser-163' may not serve as a monoubiquitination site. Ubiquitination on 'Ser-163' may modulate phosphorylation on C-terminal serine residues. {ECO:0000250|UniProtKB:O14920}.; PTM: Hydroxylated by PHD1/EGLN2, loss of hydroxylation under hypoxic conditions results in activation of NF-kappa-B. {ECO:0000250|UniProtKB:O14920}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O14920}. Nucleus {ECO:0000250|UniProtKB:O14920}. Membrane raft {ECO:0000250|UniProtKB:O14920}. Note=Colocalized with DPP4 in membrane rafts. {ECO:0000250|UniProtKB:O14920}. SUBUNIT: Component of the I-kappa-B-kinase (IKK) core complex consisting of CHUK, IKBKB and IKBKG; probably four alpha/CHUK-beta/IKBKB dimers are associated with four gamma/IKBKG subunits. The IKK core complex seems to associate with regulatory or adapter proteins to form a IKK-signalosome holo-complex (By similarity). The IKK complex associates with TERF2IP/RAP1, leading to promote IKK-mediated phosphorylation of RELA/p65 (PubMed:20622870). Part of a complex composed of NCOA2, NCOA3, CHUK/IKKA, IKBKB, IKBKG and CREBBP. Part of a 70-90 kDa complex at least consisting of CHUK/IKKA, IKBKB, NFKBIA, RELA, ELP1 and MAP3K14. Found in a membrane raft complex, at least composed of BCL10, CARD11, DPP4 and IKBKB. Interacts with SQSTM1 through PRKCZ or PRKCI. Forms an NGF-induced complex with IKBKB, PRKCI and TRAF6. May interact with MAVS/IPS1. Interacts with NALP2. Interacts with TICAM1. Interacts with FAF1; the interaction disrupts the IKK complex formation. Interacts with ATM. Part of a ternary complex consisting of TANK, IKBKB and IKBKG. Interacts with NIBP; the interaction is direct. Interacts with ARRB1 and ARRB2. Interacts with TRIM21. Interacts with NLRC5; prevents IKBKB phosphorylation and kinase activity. Interacts with PDPK1 (By similarity). Interacts with EIF2AK2/PKR (PubMed:10848580). The phosphorylated form interacts with PPM1A and PPM1B. Interacts with ZNF268 isoform 2; the interaction is further increased in a TNF-alpha-dependent manner. Interacts with IKBKE. Interacts with NAA10, leading to NAA10 degradation. Interacts with FOXO3 (By similarity). Interacts with ZC3H12A (PubMed:22037600). Interacts with AKAP13 (PubMed:23090968). Interacts with LRRC14; disrupts IKBKB-IKBKG interaction preventing I-kappa-B-kinase (IKK) core complex formation and leading to a decrease of IKBKB phosphorylation and NF-kappaB activation (By similarity). {ECO:0000250|UniProtKB:O14920, ECO:0000269|PubMed:10848580, ECO:0000269|PubMed:20622870, ECO:0000269|PubMed:22037600}. DOMAIN: The kinase domain is located in the N-terminal region. The leucine zipper is important to allow homo- and hetero-dimerization. At the C-terminal region is located the region responsible for the interaction with NEMO/IKBKG (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Detected in heart (at protein level) (PubMed:23090968). Expressed in liver, kidney and spleen. {ECO:0000269|PubMed:23090968}. +Q7TSJ2 MAP6_MOUSE Microtubule-associated protein 6 (MAP-6) (Stable tubule-only polypeptide) (STOP) 906 96,450 Alternative sequence (4); Chain (1); Lipidation (3); Modified residue (7); Region (15); Repeat (4); Sequence conflict (8) FUNCTION: Involved in microtubule stabilization in many cell types, including neuronal cells (PubMed:9600916). Specifically has microtubule cold stabilizing activity (PubMed:9600916). Involved in dendrite morphogenesis and maintenance by regulating lysosomal trafficking via its interaction with TMEM106B (By similarity). Regulates KIF5A-mediated axonal cargo transport (By similarity). Regulates axonal growth during neuron polarization (PubMed:28521134). {ECO:0000250|UniProtKB:Q63560, ECO:0000250|UniProtKB:Q96JE9, ECO:0000269|PubMed:28521134, ECO:0000269|PubMed:9600916}. PTM: Palmitoylated. Probably depalmitoylated by ABHD17A, ABHD17B and ABHD17C. During neuronal polarization, palmitoylation and depalmitoylation cycles regulate MAP6 shuttling between secretory vesicles and microtubules, and its polarized distribution in the axon. {ECO:0000250|UniProtKB:Q63560}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9600916}. Golgi apparatus {ECO:0000269|PubMed:16837464}. Cell projection, axon {ECO:0000250|UniProtKB:Q63560}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q63560}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:Q63560}; Lipid-anchor {ECO:0000250|UniProtKB:Q63560}; Cytoplasmic side {ECO:0000250|UniProtKB:Q63560}. Note=Isoform 1 and isoform 2 associate with axonal microtubules in neurons (PubMed:16837464). Isoform 3 associates with microtubules in fibroblasts (PubMed:9600916). Localizes predominantly in the proximal part of the axon (By similarity). Preferentially is concentrated on a portion of the microtubule polymer in which tubulin is modified by detyrosination and acetylation and is also resistant to depolymerization induced by both nocodazole and cold (By similarity). In unpolarized neurons, localizes to the Golgi and to secretory vesicles accumulating transiently at the tips of a subset of neurites (By similarity). Following neuronal polarization and during axon outgrowth, accumulates in the axonal growth cone and subsequently localizes throughout the axon. Partially localizes to dendrites in mature neurons (By similarity). {ECO:0000250|UniProtKB:Q63560, ECO:0000269|PubMed:16837464, ECO:0000269|PubMed:9600916}. SUBUNIT: Interacts with calmodulin (via C-terminus); the interaction is dependent on Ca(2+) (PubMed:14516200). Interacts with TMEM106B (By similarity). Interacts with ZDHHC13 (via ANK repeats) (PubMed:26198635). Interacts with ZDHHC17 (via ANK repeats) (PubMed:26198635). {ECO:0000250|UniProtKB:Q96JE9, ECO:0000269|PubMed:14516200, ECO:0000269|PubMed:26198635}. TISSUE SPECIFICITY: Isoform 1 is specifically expressed in adult brain. Isoform 2 is predominantly expressed in embryonic brain; expression persists at low levels in the adult brain. Isoform 3 is expressed at high levels in lung and at lower levels in testis, heart, muscle and kidney (at protein level). Oligodendrocytes express a major isoform of 89 kDa (O-STOP). Astrocytes also express an isoform of 60 kDa (A-STOP). {ECO:0000269|PubMed:12782132, ECO:0000269|PubMed:15389836}. +Q3TRR0 MAP9_MOUSE Microtubule-associated protein 9 (Aster-associated protein) 646 73,511 Alternative sequence (1); Chain (1); Coiled coil (1); Frameshift (1); Initiator methionine (1); Modified residue (2); Sequence caution (2); Sequence conflict (2) FUNCTION: Involved in organization of the bipolar mitotic spindle. Required for bipolar spindle assembly, mitosis progression and cytokinesis. May act by stabilizing interphase microtubules (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Localizes to microtubules in interphase, associates with the mitotic spindle during mitosis, localizes to the central body during cytokinesis. {ECO:0000250}. SUBUNIT: Binds to purified microtubules via its C-terminus. {ECO:0000250}. +P09632 HXB8_MOUSE Homeobox protein Hox-B8 (Homeobox protein Hox-2.4) 243 27,618 Chain (1); DNA binding (1); Motif (1) FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. SUBCELLULAR LOCATION: Nucleus. +P09021 HXA5_MOUSE Homeobox protein Hox-A5 (Homeobox protein Hox-1.3) (Homeobox protein M2) 270 29,237 Chain (1); DNA binding (1); Motif (1); Sequence conflict (1) FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Also binds to its own promoter. Binds specifically to the motif 5'-CYYNATTA[TG]Y-3'. SUBCELLULAR LOCATION: Nucleus. +P01812 HVM42_MOUSE Ig heavy chain V region MOPC 173 117 13,051 Chain (1); Disulfide bond (1); Domain (1); Non-terminal residue (1); Sequence conflict (1) +Q91ZJ9 HYAL1_MOUSE Hyaluronidase-1 (Hyal-1) (EC 3.2.1.35) (Hyaluronoglucosaminidase-1) 462 52,109 Active site (1); Alternative sequence (1); Chain (1); Disulfide bond (5); Domain (1); Glycosylation (5); Sequence conflict (9); Signal peptide (1) FUNCTION: May have a role in promoting tumor progression. May block the TGFB1-enhanced cell growth. {ECO:0000269|PubMed:11960552}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Lysosome {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in liver, kidney, lung and skin. {ECO:0000269|PubMed:11929860, ECO:0000269|PubMed:9503017}. +Q5U5V2 HYKK_MOUSE Hydroxylysine kinase (5-hydroxy-L-lysine kinase) (EC 2.7.1.81) (Aminoglycoside phosphotransferase domain-containing protein 1) 376 42,357 Active site (1); Alternative sequence (2); Chain (1); Sequence conflict (5) FUNCTION: Catalyzes the GTP-dependent phosphorylation of 5-hydroxy-L-lysine. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. +Q8K1T5 LY65C_MOUSE Lymphocyte antigen 6 complex locus protein G5c 149 16,590 Chain (1); Disulfide bond (5); Domain (1); Glycosylation (1); Signal peptide (1) FUNCTION: May have a role in hematopoietic cell differentiation. PTM: N-glycosylated. {ECO:0000269|PubMed:17008713}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. SUBUNIT: Forms oligomers. {ECO:0000269|PubMed:17008713}. TISSUE SPECIFICITY: Detected in adult brain. {ECO:0000269|PubMed:12079290}. +Q80W15 IBPL1_MOUSE Insulin-like growth factor-binding protein-like 1 (IGFBP-related protein 10) (Insulin-like growth factor-binding-related protein 4) (IGFBP-rP4) 270 28,573 Chain (1); Disulfide bond (2); Domain (3); Glycosylation (1); Signal peptide (1) FUNCTION: IGF-binding proteins prolong the half-life of IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs in cell culture. They alter the interaction of IGFs with their cell surface receptors (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +Q9CWP4 LY6K_MOUSE Lymphocyte antigen 6K (Ly-6K) 154 17,134 Chain (1); Domain (1); Lipidation (1); Propeptide (1); Signal peptide (1) FUNCTION: Required for sperm migration into the oviduct and male fertility by controlling binding of sperm to zona pellucida (PubMed:24501175). May play a role in cell growth (By similarity). {ECO:0000250|UniProtKB:Q17RY6, ECO:0000269|PubMed:24501175}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:27005865}; Lipid-anchor, GPI-anchor {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:27005865}. Membrane raft {ECO:0000269|PubMed:18503752}. SUBUNIT: Interacts with ADAM3 and TEX101. {ECO:0000269|PubMed:18503752, ECO:0000269|PubMed:24501175}. TISSUE SPECIFICITY: Strongly expressed in testes and weakly expressed in the epididymis, ovary, and uterus (PubMed:20920470). Expressed in testicular germ cells (TGCs) (PubMed:24501175). Expressed in the testicular seminiferous tubules, in spermatocytes, spermatids, and testicular spermatozoa (PubMed:27005865). {ECO:0000269|PubMed:20920470, ECO:0000269|PubMed:24501175, ECO:0000269|PubMed:27005865}. +O88188 LY86_MOUSE Lymphocyte antigen 86 (Ly-86) (Protein MD-1) 162 17,811 Beta strand (12); Chain (1); Disulfide bond (3); Glycosylation (2); Signal peptide (1) FUNCTION: May cooperate with CD180 and TLR4 to mediate the innate immune response to bacterial lipopolysaccharide (LPS) and cytokine production. Important for efficient CD180 cell surface expression. {ECO:0000269|PubMed:10925274}. SUBCELLULAR LOCATION: Secreted, extracellular space. Note=Associated with CD180 at the cell surface. SUBUNIT: M-shaped tetramer of two CD180-LY86 heterodimers. {ECO:0000269|PubMed:20595044, ECO:0000269|PubMed:21959264}. TISSUE SPECIFICITY: Highly expressed in spleen, liver, brain and thymus, and at lower levels in kidney. +Q9DBD0 ICA_MOUSE Inhibitor of carbonic anhydrase 700 76,766 Beta strand (39); Chain (1); Disulfide bond (16); Domain (2); Glycosylation (1); Helix (25); Mutagenesis (2); Signal peptide (1); Turn (8) FUNCTION: Inhibitor for carbonic anhydrase 2 (CA2). Does not bind iron ions. {ECO:0000269|PubMed:17511619, ECO:0000269|PubMed:18712936}. PTM: N-glycosylated. {ECO:0000269|PubMed:17330941, ECO:0000269|PubMed:17511619, ECO:0000269|PubMed:18712936}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17511619}. SUBUNIT: Monomer. Interacts (via transferrin-like domain 2) with CA2. {ECO:0000269|PubMed:18712936, ECO:0000269|PubMed:20572014}. TISSUE SPECIFICITY: Detected in blood plasma, heart, kidney, liver, colon, lung, spleen, pancreas and testis (at protein level). {ECO:0000269|PubMed:17511619}. +E9Q286 ICE1_MOUSE Little elongation complex subunit 1 (Interactor of little elongator complex ELL subunit 1) 2241 242,254 Chain (1); Coiled coil (1); Compositional bias (4); Modified residue (14) FUNCTION: Component of the little elongation complex (LEC), a complex required to regulate small nuclear RNA (snRNA) gene transcription by RNA polymerase II and III. Specifically acts as a scaffold protein that promotes the LEC complex formation and recruitment and RNA polymerase II occupancy at snRNA genes in subnuclear bodies (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y2F5}. Nucleus, Cajal body {ECO:0000250|UniProtKB:Q9Y2F5}. Note=Colocalizes with COIL in subnuclear Cajal and histone locus bodies. Associates to transcriptionally active chromatin at snRNA genes. {ECO:0000250|UniProtKB:Q9Y2F5}. SUBUNIT: Component of the little elongation complex (LEC), at least composed of ELL (ELL, ELL2 or ELL3), ZC3H8, ICE1 and ICE2. Interacts (via N-terminus domain) with ELL. Interacts (via C-terminus domain) with ICE2 and ZC3H8 (By similarity). {ECO:0000250}. DOMAIN: The N-termimus domain is necessary and sufficient for its targeting to subnuclear cajal and histone locus bodies. {ECO:0000250}. +Q5DU31 ICEF1_MOUSE Interactor protein for cytohesin exchange factors 1 406 45,812 Alternative sequence (3); Chain (1); Domain (1); Erroneous initiation (3); Modified residue (1) FUNCTION: Enhances the promotion of guanine-nucleotide exchange by PSCD2 on ARF6 in a concentration-dependent manner. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Translocated with PSCD2 to the plasma membrane upon epidermal growth factor (EGF) stimulation. {ECO:0000250}. SUBUNIT: Interacts with guanine-nucleotide exchange factors PSCD1, PSCD2, PSCD3 and PSCD4. {ECO:0000250}. +Q9WVS0 ICOS_MOUSE Inducible T-cell costimulator (Activation-inducible lymphocyte immunomediatory molecule) (CD28 and CTLA-4-like protein) (CCLP) (CD28-related protein 1) (CRP-1) (CD antigen CD278) 200 22,709 Chain (1); Disulfide bond (2); Domain (1); Glycosylation (3); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 145 165 Helical. {ECO:0000255}. TOPO_DOM 21 144 Extracellular. {ECO:0000255}.; TOPO_DOM 166 200 Cytoplasmic. {ECO:0000255}. FUNCTION: Enhances all basic T-cell responses to a foreign antigen, namely proliferation, secretion of lymphokines, up-regulation of molecules that mediate cell-cell interaction, and effective help for antibody secretion by B-cells. Essential both for efficient interaction between T and B-cells and for normal antibody responses to T-cell dependent antigens. Does not up-regulate the production of interleukin-2, but superinduces the synthesis of interleukin-10. Prevents the apoptosis of pre-activated T-cells. Plays a critical role in CD40-mediated class switching of immunoglobin isotypes (By similarity). {ECO:0000250, ECO:0000269|PubMed:10617205, ECO:0000269|PubMed:11343122, ECO:0000269|PubMed:11343123}. PTM: N-glycosylated. {ECO:0000269|PubMed:10760791}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:10760791}. TISSUE SPECIFICITY: Expressed on activated T-cells and resting memory T-cells. High expression seen in the thymic medulla and in the germinal centers and T-cell zones of lymph nodes and Peyer patches. Expressed at low levels in the spleen. {ECO:0000269|PubMed:10617205, ECO:0000269|PubMed:10760791, ECO:0000269|PubMed:11006126}. +P41139 ID4_MOUSE DNA-binding protein inhibitor ID-4 (Inhibitor of DNA binding 4) (Inhibitor of differentiation 4) 161 16,596 Chain (1); Compositional bias (2); Domain (1) FUNCTION: Transcriptional regulator (lacking a basic DNA binding domain) which negatively regulates the basic helix-loop-helix (bHLH) transcription factors by forming heterodimers and inhibiting their DNA binding and transcriptional activity. Implicated in regulating a variety of cellular processes, including cellular growth, senescence, differentiation, apoptosis, angiogenesis, and neoplastic transformation. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Heterodimer with other HLH proteins. +P0DP60 LYNX1_MOUSE Ly-6/neurotoxin-like protein 1 (GC26) 116 12,835 Chain (1); Disulfide bond (5); Domain (1); Lipidation (1); Propeptide (1); Signal peptide (1) FUNCTION: Acts in different tissues through interaction to nicotinic acetylcholine receptors (nAChRs) (PubMed:10402197). The proposed role as modulator of nAChR activity seems to be dependent on the nAChR subtype and stoichiometry, and to involve an effect on nAChR trafficking and its cell surface expression, and on single channel properties of the nAChR inserted in the plasma membrane.Modulates functional properties of nicotinic acetylcholine receptors (nAChRs) to prevent excessive excitation, and hence neurodegeneration. Enhances desensitization by increasing both the rate and extent of desensitization of alpha-4:beta-2-containing nAChRs and slowing recovery from desensitization. Promotes large amplitude ACh-evoked currents through alpha-4:beta-2 nAChRs (PubMed:10402197, PubMed:11906696). Is involved in regulation of the nAChR pentameric assembly in the endoplasmic reticulum. Shifts stoichiometry from high sensitivity alpha-4(2):beta-2(3) to low sensitivity alpha-4(3):beta-2(2) nAChR (PubMed:25193667). In vitro modulates alpha-3:beta-4-containing nAChRs. Reduces cell surface expression of (alpha-3:beta-4)(2):beta-4 and (alpha-3:beta-4)(2):alpha-5 nAChRs suggesting an interaction with nAChR alpha-3(-):(+)beta-4 subunit interfaces and an allosteric mode. Corresponding single channel effects characterized by decreased unitary conductance, altered burst proportions and enhanced desensitization/inactivation seem to depend on nAChR alpha:alpha subunit interfaces and are greater in (alpha-3:beta-2)(2):alpha-3 when compared to (alpha-3:beta-2)(2):alpha-5 nAChRs (By similarity). Prevents plasticity in the primary visual cortex late in life (PubMed:21071629). {ECO:0000250|UniProtKB:P0DP58, ECO:0000269|PubMed:10402197, ECO:0000269|PubMed:11906696, ECO:0000269|PubMed:21071629, ECO:0000269|PubMed:25193667}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Lipid-anchor, GPI-anchor {ECO:0000255}. Cell projection, dendrite {ECO:0000269|PubMed:10402197}. Endoplasmic reticulum {ECO:0000269|PubMed:25193667}. Note=Detected in Purkinje cells soma and proximal dendrites. {ECO:0000269|PubMed:10402197}. SUBUNIT: Interacts with nAChRs containing alpha-4:beta-2 (CHRNA4:CHRNB2) and alpha-7 (CHRNA7) subunits (PubMed:11906696). Interacts with CHRNA4 probably in the endoplasmic reticulum prior to nAChR pentameric assembly (PubMed:19468303). {ECO:0000269|PubMed:11906696, ECO:0000269|PubMed:19468303}. TISSUE SPECIFICITY: Expressed in neurons of multiple regions in the CNS, including the cerebral cortex, thalamus, substantia nigra, cerebellum, amygdala and hippocampus (PubMed:10402197, PubMed:11906696). Also expressed in kidney, heart and thymus, but at lower levels than in the brain (PubMed:10402197). Expressed in the primary visual cortex (V1) and the lateral geniculate nucleus (at protein level) (PubMed:21071629). {ECO:0000269|PubMed:10402197, ECO:0000269|PubMed:11906696, ECO:0000269|PubMed:21071629}. +P25911 LYN_MOUSE Tyrosine-protein kinase Lyn (EC 2.7.10.2) (V-yes-1 Yamaguchi sarcoma viral related oncogene homolog) (p53Lyn) (p56Lyn) 512 58,812 Active site (1); Alternative sequence (1); Beta strand (15); Binding site (1); Chain (1); Domain (3); Helix (16); Initiator methionine (1); Lipidation (2); Modified residue (9); Mutagenesis (1); Nucleotide binding (1); Sequence conflict (11); Turn (1) FUNCTION: Non-receptor tyrosine-protein kinase that transmits signals from cell surface receptors and plays an important role in the regulation of innate and adaptive immune responses, hematopoiesis, responses to growth factors and cytokines, integrin signaling, but also responses to DNA damage and genotoxic agents. Functions primarily as negative regulator, but can also function as activator, depending on the context. Required for the initiation of the B-cell response, but also for its down-regulation and termination. Plays an important role in the regulation of B-cell differentiation, proliferation, survival and apoptosis, and is important for immune self-tolerance. Acts downstream of several immune receptors, including the B-cell receptor, CD79A, CD79B, CD5, CD19, CD22, FCER1, FCGR2, FCGR1A, TLR2 and TLR4. Plays a role in the inflammatory response to bacterial lipopolysaccharide. Mediates the responses to cytokines and growth factors in hematopoietic progenitors, platelets, erythrocytes, and in mature myeloid cells, such as dendritic cells, neutrophils and eosinophils. Acts downstream of EPOR, KIT, MPL, the chemokine receptor CXCR4, as well as the receptors for IL3, IL5 and CSF2. Plays an important role in integrin signaling. Regulates cell proliferation, survival, differentiation, migration, adhesion, degranulation, and cytokine release. Down-regulates signaling pathways by phosphorylation of immunoreceptor tyrosine-based inhibitory motifs (ITIM), that then serve as binding sites for phosphatases, such as PTPN6/SHP-1, PTPN11/SHP-2 and INPP5D/SHIP-1, that modulate signaling by dephosphorylation of kinases and their substrates. Phosphorylates LIME1 in response to CD22 activation. Phosphorylates BTK, CBL, CD5, CD19, CD72, CD79A, CD79B, CSF2RB, DOK1, HCLS1, LILRB3/PIR-B, MS4A2/FCER1B, SYK and TEC. Promotes phosphorylation of SIRPA, PTPN6/SHP-1, PTPN11/SHP-2 and INPP5D/SHIP-1. Required for rapid phosphorylation of FER in response to FCER1 activation. Mediates KIT phosphorylation. Acts as an effector of EPOR (erythropoietin receptor) in controlling KIT expression and may play a role in erythroid differentiation during the switch between proliferation and maturation. Depending on the context, activates or inhibits several signaling cascades. Regulates phosphatidylinositol 3-kinase activity and AKT1 activation. Regulates activation of the MAP kinase signaling cascade, including activation of MAP2K1/MEK1, MAPK1/ERK2, MAPK3/ERK1, MAPK8/JNK1 and MAPK9/JNK2. Mediates activation of STAT5A and/or STAT5B. Phosphorylates LPXN on 'Tyr-72'. Kinase activity facilitates TLR4-TLR6 heterodimerization and signal initiation. {ECO:0000250|UniProtKB:P07948, ECO:0000269|PubMed:10327049, ECO:0000269|PubMed:10594694, ECO:0000269|PubMed:10640270, ECO:0000269|PubMed:10672044, ECO:0000269|PubMed:11007759, ECO:0000269|PubMed:11435302, ECO:0000269|PubMed:11672542, ECO:0000269|PubMed:12077122, ECO:0000269|PubMed:12874221, ECO:0000269|PubMed:14525964, ECO:0000269|PubMed:14726379, ECO:0000269|PubMed:15335855, ECO:0000269|PubMed:16034130, ECO:0000269|PubMed:16116174, ECO:0000269|PubMed:16249387, ECO:0000269|PubMed:16272347, ECO:0000269|PubMed:16731527, ECO:0000269|PubMed:17640867, ECO:0000269|PubMed:19492092, ECO:0000269|PubMed:20189992, ECO:0000269|PubMed:20385881, ECO:0000269|PubMed:7513017, ECO:0000269|PubMed:7584145, ECO:0000269|PubMed:7585947, ECO:0000269|PubMed:8128248, ECO:0000269|PubMed:8621063, ECO:0000269|PubMed:8629002, ECO:0000269|PubMed:9036984, ECO:0000269|PubMed:9064343, ECO:0000269|PubMed:9252121, ECO:0000269|PubMed:9469421, ECO:0000269|PubMed:9480991, ECO:0000269|PubMed:9547345, ECO:0000269|PubMed:9573010, ECO:0000269|PubMed:9590210, ECO:0000269|PubMed:9601638}. PTM: Ubiquitinated by CBL, leading to its degradation. {ECO:0000269|PubMed:15304502}.; PTM: Phosphorylated on tyrosine residues in response to KIT signaling (By similarity). Autophosphorylated. Phosphorylation at Tyr-397 is required for optimal activity. Phosphorylation at Tyr-508 inhibits kinase activity. Phosphorylated at Tyr-508 by CSK. Dephosphorylated by PTPRC/CD45. Becomes rapidly phosphorylated upon activation of the B-cell receptor and the immunoglobulin receptor FCGR1A. {ECO:0000250, ECO:0000269|PubMed:10415030, ECO:0000269|PubMed:16272347, ECO:0000269|PubMed:9252121}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Golgi apparatus {ECO:0000250}. Membrane {ECO:0000250|UniProtKB:P07948}; Lipid-anchor {ECO:0000250|UniProtKB:P07948}. Note=Accumulates in the nucleus by inhibition of Crm1-mediated nuclear export. Nuclear accumulation is increased by inhibition of its kinase activity. The trafficking from the Golgi apparatus to the cell membrane occurs in a kinase domain-dependent but kinase activity independent manner and is mediated by exocytic vesicular transport (By similarity). {ECO:0000250}. SUBUNIT: Interacts with TEC. Interacts (via SH2 domain) with FLT3 (tyrosine phosphorylated). Interacts with LIME1 and with CD79A upon activation of the B-cell antigen receptor. Interacts with the B-cell receptor complex. Interacts with phosphorylated THEMIS2. Interacts with EPOR. Interacts with MS4A2/FCER1B. Interaction (via the SH2 and SH3 domains) with MUC1 is stimulated by IL7 and the subsequent phosphorylation increases the binding between MUC1 and CTNNB1/beta-catenin. Interacts with ADAM15. Interacts with NDFIP2 and more weakly with NDFIP1. Interacts with FASLG. Interacts with KIT. Interacts with HCLS1. Interacts with FCGR2B. Interacts with FCGR1A; the interaction may be indirect. Interacts with CD19, CD22, CD79A and CD79B. Interacts (via SH3 domain) with CBLC, PPP1R15A and PDE4A. Interacts with TGFB1I1. Interacts (via SH3 domain) with PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase; this interaction enhances phosphatidylinositol 3-kinase activity. Interacts with CSF2RB, the common subunit of the IL3, IL5 and CSF2 receptors. Interacts with PAG1; identified in a complex with PAG1 and STAT3. Interacts with ABL1. Interacts with PTPN6/SHP-1. Interacts (via SH3 domain) with SCIMP (via proline-rich region). Interacts with LPXN (via LD motif 3) and the interaction is induced upon B-cell antigen receptor (BCR) activation. Interacts (via SH3-domain) with ANKRD54 (via ankyrin repeat region) in an activation-independent status of LYN. Forms a multiprotein complex with ANKRD54 and HCLS1. Interacts (via SH2 and SH3 domains) with UNC119; leading to LYN activation (By similarity). Interacts with CD36. Interacts with LYN (PubMed:22496641). {ECO:0000250|UniProtKB:P07948, ECO:0000269|PubMed:10672044, ECO:0000269|PubMed:11517336, ECO:0000269|PubMed:15335855, ECO:0000269|PubMed:16249387, ECO:0000269|PubMed:16272347, ECO:0000269|PubMed:16684964, ECO:0000269|PubMed:1702903, ECO:0000269|PubMed:17233630, ECO:0000269|PubMed:17640867, ECO:0000269|PubMed:19064729, ECO:0000269|PubMed:20644716, ECO:0000269|PubMed:22496641, ECO:0000269|PubMed:7782294, ECO:0000269|PubMed:8128248, ECO:0000269|PubMed:8168489, ECO:0000269|PubMed:8621063, ECO:0000269|PubMed:9469421, ECO:0000269|PubMed:9573010}. DOMAIN: The protein kinase domain plays an important role in its localization in the cell membrane. {ECO:0000250}. TISSUE SPECIFICITY: Detected in bone marrow-derived monocytes (at protein level). Expressed predominantly in B-lymphoid and myeloid cells. {ECO:0000269|PubMed:2017160}. +Q6ZWX6 IF2A_MOUSE Eukaryotic translation initiation factor 2 subunit 1 (Eukaryotic translation initiation factor 2 subunit alpha) (eIF-2-alpha) (eIF-2A) (eIF-2alpha) 315 36,108 Chain (1); Domain (1); Modified residue (6) FUNCTION: Functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form a 43S pre-initiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by eIF-2B (By similarity). {ECO:0000250}. PTM: Substrate for at least 4 kinases: EIF2AK1/HRI, EIF2AK2/PKR, EIF2AK3/PERK and EIF2AK4/GCN2. Phosphorylation stabilizes the eIF-2/GDP/eIF-2B complex and prevents GDP/GTP exchange reaction, thus impairing the recycling of eIF-2 between successive rounds of initiation and leading to global inhibition of translation (By similarity). Phosphorylated; phosphorylation on Ser-52 by the EIF2AK4/GCN2 protein kinase occurs in response to amino acid starvation and UV irradiation (PubMed:10504407, PubMed:11106749, PubMed:12176355, PubMed:15213227, PubMed:16054071). {ECO:0000250|UniProtKB:P05198, ECO:0000269|PubMed:10504407, ECO:0000269|PubMed:11106749, ECO:0000269|PubMed:12176355, ECO:0000269|PubMed:15213227, ECO:0000269|PubMed:16054071}. SUBCELLULAR LOCATION: Cytoplasm, Stress granule {ECO:0000269|PubMed:19861488}. Note=Colocalizes with NANOS3 in the stress granules. {ECO:0000269|PubMed:19861488}. SUBUNIT: Heterotrimer composed of an alpha, a beta and a gamma chain. Interacts with ABCF1. Associates with ribosomes. Interaction with METAP2 protects EIF2S1 from inhibitory phosphorylation (By similarity). Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5. {ECO:0000250, ECO:0000269|PubMed:16931514}. +Q9D9H3 MB3L1_MOUSE Methyl-CpG-binding domain protein 3-like 1 (MBD3-like protein 1) 186 20,676 Chain (1); Region (1); Sequence conflict (2) FUNCTION: Transcriptional repressor. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Nuclear, in large foci. {ECO:0000250}. DOMAIN: The N-terminal half of the protein mediates transcription repression. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in testis. Not detected in the other tissues tested. {ECO:0000269|PubMed:12504854}. +Q9Z2D8 MBD3_MOUSE Methyl-CpG-binding domain protein 3 (Methyl-CpG-binding protein MBD3) 285 32,168 Alternative sequence (1); Chain (1); Coiled coil (1); Compositional bias (1); Cross-link (3); Domain (1); Modified residue (3) FUNCTION: Acts as transcriptional repressor and plays a role in gene silencing. Does not bind DNA by itself. Binds to DNA with a preference for sites containing methylated CpG dinucleotides (in vitro). Binds to a lesser degree DNA containing unmethylated CpG dinucleotides (By similarity). Recruits histone deacetylases and DNA methyltransferases. {ECO:0000250, ECO:0000269|PubMed:9774669}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14610093, ECO:0000269|PubMed:9774669}. Chromosome {ECO:0000250}. Note=Detected on chromatin, at promoter regions of active genes (By similarity). Nuclear, in discrete foci. {ECO:0000250}. SUBUNIT: Heterodimer with MBD2. Part of the NuRD and the MeCP1 complex. Interacts with BCL6, HDAC1, MTA2, DNMT1, p66-alpha and p66-beta (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in brain, heart, kidney, liver, lung, skeletal muscle, spleen and testis. Detected at lower levels in embryonic stem cells. {ECO:0000269|PubMed:9774669}. +P70168 IMB1_MOUSE Importin subunit beta-1 (Karyopherin subunit beta-1) (Nuclear factor p97) (Pore targeting complex 97 kDa subunit) (PTAC97) (SCG) 876 97,184 Beta strand (8); Chain (1); Compositional bias (1); Domain (1); Helix (55); Modified residue (5); Region (2); Repeat (19); Sequence conflict (1); Turn (6) FUNCTION: Functions in nuclear protein import, either in association with an adapter protein, like an importin-alpha subunit, which binds to nuclear localization signals (NLS) in cargo substrates, or by acting as autonomous nuclear transport receptor. Acting autonomously, serves itself as NLS receptor. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Mediates autonomously the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5. Binds to a beta-like import receptor binding (BIB) domain of RPL23A. In association with IPO7 mediates the nuclear import of H1 histone. In vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones. Imports SNAI1 and PRKCI into the nucleus (By similarity). {ECO:0000250|UniProtKB:Q14974, ECO:0000269|PubMed:11493596}. PTM: Mono-ADP-ribosylated by PARP16. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus envelope {ECO:0000250}. SUBUNIT: Forms a complex with an importin alpha subunit. Forms a heterodimer with IPO7. Interacts with IPO7, SNUPN, RPL23A and XPO1. The KPNB1/IPO7 heterodimer interacts with H1 histone. Interacts with H2A, H2B, H3 and H4 histones (By similarity). Component of an import snRNP complex composed of KPNB1, SNUPN, SMN1 and ZNF259. Component of a nuclear export receptor complex composed of KPNB1, Ran, SNUPN and XPO1. Interacts with SRY. Interacts with PRKCI/atypical protein kinase C iota (By similarity). Interacts with KPNA7. Interacts with SNAI1 (via zinc fingers) and SNAI2 (via zinc fingers) (By similarity). Interacts with SLC35G1 and STIM1 (By similarity). Interacts with DCAF8. Interacts with RAN (PubMed:25946333). Interacts with NUMA1 (via C-terminus); this interaction is inhibited by RanGTP (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q14974, ECO:0000269|PubMed:25946333}. +P50096 IMDH1_MOUSE Inosine-5'-monophosphate dehydrogenase 1 (IMP dehydrogenase 1) (IMPD 1) (IMPDH 1) (EC 1.1.1.205) (IMPDH-I) 514 55,279 Active site (2); Binding site (2); Chain (1); Domain (2); Metal binding (6); Modified residue (3); Nucleotide binding (2); Region (3); Sequence conflict (3) Purine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1. FUNCTION: Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Could also have a single-stranded nucleic acid-binding activity and could play a role in RNA and/or DNA metabolism. It may also have a role in the development of malignancy and the growth progression of some tumors. {ECO:0000255|HAMAP-Rule:MF_03156}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03156}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03156}. SUBUNIT: Homotetramer. +O35664 INAR2_MOUSE Interferon alpha/beta receptor 2 (IFN-R-2) (IFN-alpha/beta receptor 2) (Type I interferon receptor 2) 513 56,578 Alternative sequence (4); Chain (1); Disulfide bond (3); Glycosylation (8); Modified residue (5); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 243 263 Helical. {ECO:0000255}. TOPO_DOM 22 242 Extracellular. {ECO:0000255}.; TOPO_DOM 264 513 Cytoplasmic. {ECO:0000255}. FUNCTION: Associates with IFNAR1 to form the type I interferon receptor. Receptor for interferons alpha and beta. Involved in IFN-mediated STAT1, STAT2 and STAT3 activation. Isoform 1 and isoform 2 are directly involved in signal transduction due to their association with the TYR kinase, JAK1. Isoform 2 and isoform 3 may be potent inhibitors of type I IFN receptor activity. {ECO:0000250|UniProtKB:P48551, ECO:0000305|PubMed:9295335, ECO:0000305|PubMed:9322767}. PTM: Phosphorylated on tyrosine residues upon interferon binding. Phosphorylation at Tyr-335 or Tyr-510 are sufficient to mediate interferon dependent activation of STAT1, STAT2 and STAT3 leading to antiproliferative effects on many different cell types (By similarity). {ECO:0000250}.; PTM: Glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Isoform 1: Cell membrane {ECO:0000305|PubMed:9295335, ECO:0000305|PubMed:9322767}; Single-pass type I membrane protein {ECO:0000305|PubMed:9322767}.; SUBCELLULAR LOCATION: Isoform 2: Secreted {ECO:0000305|PubMed:9322767}.; SUBCELLULAR LOCATION: Isoform 3: Secreted {ECO:0000305|PubMed:9295335, ECO:0000305|PubMed:9322767}. SUBUNIT: Heterodimer with IFNAR1. Isoform 1 interacts with the transcriptional factors STAT1 and STAT2. Interacts with JAK1. {ECO:0000250|UniProtKB:P48551, ECO:0000305|PubMed:9322767}. TISSUE SPECIFICITY: Widely expressed. Detected in liver, testis, kidney, salivary gland, thymus, brain, lung and placenta. Isoform 1, isoform 2 and isoform 3 are expressed in brain. {ECO:0000269|PubMed:9295335, ECO:0000269|PubMed:9322767}. +O55091 IMPCT_MOUSE Protein IMPACT (Imprinted and ancient gene protein) 318 36,276 Chain (1); Domain (1); Modified residue (1); Sequence conflict (1) FUNCTION: Translational regulator that ensures constant high levels of translation upon a variety of stress conditions, such as amino acid starvation, UV-C irradiation, proteasome inhibitor treatment and glucose deprivation. Plays a role as a negative regulator of the EIF2AK4/GCN2 kinase activity; impairs GCN1-mediated EIF2AK4/GCN2 activation, and hence EIF2AK4/GCN2-mediated eIF-2-alpha phosphorylation and subsequent down-regulation of protein synthesis (PubMed:15937339, PubMed:23447528, PubMed:24333428). May be required to regulate translation in specific neuronal cells under amino acid starvation conditions by preventing GCN2 activation and therefore ATF4 synthesis (PubMed:15937339, PubMed:23447528). Through its inhibitory action on EIF2AK4/GCN2, plays a role in differentiation of neuronal cells by stimulating neurite outgrowth (PubMed:23447528). {ECO:0000269|PubMed:15937339, ECO:0000269|PubMed:23447528, ECO:0000269|PubMed:24333428}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:23447528}. SUBUNIT: Interacts with GCN1; prevents the interaction of GCN1 with EIF2AK4/GCN2 and inhibits EIF2AK4/GCN2 kinase activity (PubMed:15937339, PubMed:22404850). Interaction with RPL39; this interaction occurs in a GCN1-independent manner (PubMed:22404850). Associates with ribosomes; this interaction occurs in a GCN1-independent manner (PubMed:22404850). Associates with actin; this interaction occurs in a GCN1-independent manner (PubMed:22404850). {ECO:0000269|PubMed:15937339, ECO:0000269|PubMed:22404850}. TISSUE SPECIFICITY: Present in neurons in most areas of the brain. Present at high level in hypothalamus, particularly in the suprachiasmatic nucleus (at protein level) (PubMed:15937339, PubMed:18260151). Preferentially expressed in brain, with a weaker expression in other tissues (PubMed:9256468). {ECO:0000269|PubMed:15937339, ECO:0000269|PubMed:18260151, ECO:0000269|PubMed:9256468}. +Q8R1W8 IMPG1_MOUSE Interphotoreceptor matrix proteoglycan 1 (Interphotoreceptor matrix proteoglycan of 150 kDa) (IPM-150) (Sialoprotein associated with cones and rods) 798 89,474 Alternative sequence (2); Chain (1); Domain (2); Glycosylation (12); Sequence conflict (3); Signal peptide (1) FUNCTION: May interact with hyaluronan which may serve to form a basic macromolecular scaffold comprising the insoluble interphotoreceptor matrix. {ECO:0000250|UniProtKB:Q17R60}. PTM: Highly glycosylated (N- and O-linked carbohydrates and sialic acid). {ECO:0000250|UniProtKB:Q17R60}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Abundantly expressed in retina. {ECO:0000269|PubMed:10958699, ECO:0000269|PubMed:10995555}. +Q63ZW7 INADL_MOUSE InaD-like protein (Inadl protein) (Channel-interacting PDZ domain-containing protein) (Pals1-associated tight junction protein) (Protein associated to tight junctions) 1834 198,517 Alternative sequence (9); Chain (1); Domain (11); Helix (3); Modified residue (7); Sequence conflict (2) FUNCTION: Scaffolding protein that may bring different proteins into adjacent positions at the cell membrane. May regulate protein targeting, cell polarity and integrity of tight junctions. May regulate the surface expression and/or function of ASIC3 in sensory neurons. May recruit ARHGEF18 to apical cell-cell boundaries (By similarity). {ECO:0000250|UniProtKB:Q8NI35, ECO:0000269|PubMed:11872753}. SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000250|UniProtKB:Q8NI35}. Cell membrane; Peripheral membrane protein. Apical cell membrane; Peripheral membrane protein. Cytoplasm, perinuclear region {ECO:0000269|PubMed:14988405}. Note=Localizes to tight junctions in epithelial cells. Also found at the apical plasma membrane (By similarity). Localized in the paranodal region of myelinating Schwann cells. {ECO:0000250|UniProtKB:Q8NI35}.; SUBCELLULAR LOCATION: Isoform 3: Cytoplasm. Cytoplasm, perinuclear region. Note=Concentrates around the nucleus upon HTR2A coexpression. Cytoplasm, perinuclear region. SUBUNIT: Forms a ternary complex with MPP5 and CRB1. Interacts with TJP3/ZO-3 and CLDN1/claudin-1. Component of a complex whose core is composed of ARHGAP17, AMOT, MPP5/PALS1, INADL/PATJ and PARD3/PAR3 (By similarity). Interacts with ASIC3, KCNJ10, KCNJ15, GRIN2A, GRIN2B, GRIN2C, GRIN2D, NLGN2, MPP7 and HTR2A. Isoform 2 interacts with NRXN2. Directly interacts with HTR4. Interacts (via PDZ domain 8) with WWC1 (via the ADDV motif) (By similarity). Interacts with SLC6A4. Interacts (via C-terminus) with ARHGEF18 (By similarity). {ECO:0000250|UniProtKB:Q8NI35, ECO:0000269|PubMed:11872753, ECO:0000269|PubMed:14988405, ECO:0000269|PubMed:15466885, ECO:0000269|PubMed:17452640, ECO:0000269|PubMed:9647694}. DOMAIN: The L27 domain (also called Maguk recruitment domain) is required for interaction with MPP5 and CRB3, and MPP5 localization to tight junctions. {ECO:0000250}.; DOMAIN: The PDZ domain 6 mediates interaction with the C-terminus of TJP3 and is crucial for localization to the tight junctions. The PDZ domain 8 interacts with CLDN1 but is not required for proper localization (By similarity). The PDZ domain 2 of isoform 3 mediates interactions with KCNJ10, KCNJ15, GRIN2B and NLGN2. The PDZ domain 3 of isoform 3 mediates interactions with KCNJ15, GRIN2A, GRIN2B, GRIN2C, GRIN2D and NRXN2. The PDZ domain 4 of isoform 3 mediates interaction with ASIC3. {ECO:0000250, ECO:0000269|PubMed:11872753, ECO:0000269|PubMed:9647694}. TISSUE SPECIFICITY: Expressed exclusively in brain and kidney. Isoform 3 might be brain-specific. In brain, high levels are detected in the cerebellum, inferior colliculus, vestibular nucleus, facial nucleus and thalamus. Also detected in deep cerebellar nuclei, superior colliculus, dorsal transition zone, brain stem, as well as the glomerular and mitral cell layers of the olfactory bulb. Within the cerebellum it is expressed in both Purkinje and granule cell layers. {ECO:0000269|PubMed:9647694}. +P83891 IMPL_MOUSE Implantin (Fragment) 20 2,217 Chain (1); Non-terminal residue (1) FUNCTION: Binds DNA. {ECO:0000269|Ref.1, ECO:0000305}. PTM: Phosphorylated. {ECO:0000269|Ref.1, ECO:0000305}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|Ref.1}. Nucleus {ECO:0000269|Ref.1}. TISSUE SPECIFICITY: Uterus and embryo. {ECO:0000269|Ref.1, ECO:0000305}. +Q9WU62 INCE_MOUSE Inner centromere protein 880 101,209 Alternative sequence (1); Chain (1); Coiled coil (1); Glycosylation (1); Modified residue (30); Region (2); Sequence conflict (4) FUNCTION: Component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Acts as a scaffold regulating CPC localization and activity. The C-terminus associates with AURKB or AURKC, the N-terminus associated with BIRC5/survivin and CDCA8/borealin tethers the CPC to the inner centromere, and the microtubule binding activity within the central SAH domain directs AURKB/C toward substrates near microtubules. The flexibility of the SAH domain is proposed to allow AURKB/C to follow substrates on dynamic microtubules while ensuring CPC docking to static chromatin (By similarity). Activates AURKB and AURKC. Controls the kinetochore localization of BUB1. {ECO:0000250|UniProtKB:P53352, ECO:0000250|UniProtKB:Q9NQS7}. PTM: Phosphorylation by AURKB at its C-terminal part is important for AURKB activation by INCENP. {ECO:0000250}. SUBCELLULAR LOCATION: Chromosome, centromere {ECO:0000269|PubMed:12584241}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:12584241}. Nucleus {ECO:0000269|PubMed:12584241}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:12584241}. Midbody {ECO:0000250|UniProtKB:Q9NQS7}. Note=Localizes to inner kinetochore. Localizes on chromosome arms and inner centromeres from prophase through metaphase and then transferring to the spindle midzone and midbody from anaphase through cytokinesis. Colocalizes to the equatorial cell cortex at anaphase (By similarity). Localized at synaptonemal complex central element from zygotene up to late pachytene when it begins to relocalize to heterochromatic chromocenters (PubMed:12584241). Colocalizes with AURKB at a connecting strand traversing the centromere region and joining sister kinetochores, in metaphase II centromeres. This strand disappears at the metaphase II/anaphase II transition and relocalizes to the spindle midzone (PubMed:12584241). {ECO:0000250|UniProtKB:Q9NQS7, ECO:0000269|PubMed:12584241}. SUBUNIT: Component of the chromosomal passenger complex (CPC) composed of at least BIRC5/survivin, CDCA8/borealin, INCENP, AURKB or AURKC; in the complex binds directly to AURKB or AURKC via the IN box, and forms a triple-helix bundle-based subcomplex with BIRC5 and CDCA8 via its N-terminus. The reported homodimerization is questioned as the SAH domain is shown to be monomeric. Interacts with H2AFZ. Interacts with CBX1 and CBX3. Interacts with tubulin beta chain. Interacts with EVI5. Interacts with CBX5; POGZ and INCENP compete for interaction with CBX5. Interacts with POGZ. Interacts with JTB. {ECO:0000250|UniProtKB:P53352, ECO:0000250|UniProtKB:Q9NQS7, ECO:0000269|PubMed:12660166}. DOMAIN: The IN box mediates interaction with AURKB and AURKC. {ECO:0000250|UniProtKB:O13024, ECO:0000250|UniProtKB:Q9NQS7}.; DOMAIN: The SAH (single alpha-helix) region is characterized by a high content of charged residues which are predicted to stabilize the alpha-helical structure by ionic bonds. It can refold after extension suggesting an in vivo force-dependent function. The isolated SAH domain is monomeric. {ECO:0000250|UniProtKB:P53352}. +P21843 MCPT3_MOUSE Mast cell protease 3 (mMCP-3) (EC 3.4.21.-) (Fragment) 21 2,328 Chain (1); Domain (1); Non-terminal residue (1) FUNCTION: Thrombin inactivating protease. Displays chymotrypsin-like substrate specificity. +Q6ZPV2 INO80_MOUSE Chromatin-remodeling ATPase INO80 (EC 3.6.4.-) (DNA helicase-related INO80 complex homolog 1) (DNA helicase-related protein INO80) 1559 176,520 Alternative sequence (1); Chain (1); Domain (3); Modified residue (2); Nucleotide binding (1); Region (3) FUNCTION: ATPase component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and DNA repair. Binds DNA. As part of the INO80 complex, remodels chromatin by shifting nucleosomes. Regulates transcription upon recruitment by YY1 to YY1-activated genes, where it acts as an essential coactivator. Involved in UV-damage excision DNA repair. The contribution to DNA double-strand break repair appears to be largely indirect through transcriptional regulation. Involved in DNA replication. Required for microtubule assembly during mitosis thereby regulating chromosome segregation cycle. {ECO:0000250|UniProtKB:Q9ULG1}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9ULG1}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00746, ECO:0000269|PubMed:20971067}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9ULG1}. Chromosome {ECO:0000250|UniProtKB:Q9ULG1}. Note=Localizes to the cytoplasm in quiescent cell. Associates with spindle microtubules during mitosis. Colocalizes with PCNA at replication forks during S-phase. Recruited to DNA damage sites in a ACTR8-dependent manner. {ECO:0000250|UniProtKB:Q9ULG1}. SUBUNIT: Component of the chromatin remodeling INO80 complex; three different complex modules assemble on different domains of INO80. Interacts with DDB1. Interacts with transcriptional repressor protein YY1; the interaction recruits the INO80 complex to YY1 target genes. Interacts with YY1AP1. Interacts with tubulin alpha. {ECO:0000250|UniProtKB:Q9ULG1}. DOMAIN: The DBINO region is involved in binding to DNA. {ECO:0000250|UniProtKB:Q9ULG1}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:16298340}. +Q9WTL4 INSRR_MOUSE Insulin receptor-related protein (IRR) (EC 2.7.10.1) (IR-related receptor) [Cleaved into: Insulin receptor-related protein alpha chain; Insulin receptor-related protein beta chain] 1300 144,875 Active site (1); Binding site (1); Chain (3); Disulfide bond (10); Domain (4); Glycosylation (11); Modified residue (2); Nucleotide binding (1); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 922 943 Helical. {ECO:0000255}. TOPO_DOM 747 921 Extracellular. {ECO:0000255}.; TOPO_DOM 944 1300 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor with tyrosine-protein kinase activity. Functions as a pH sensing receptor which is activated by increased extracellular pH. Activates an intracellular signaling pathway that involves IRS1 and AKT1/PKB. {ECO:0000269|PubMed:21641549}. PTM: Autophosphorylated on tyrosine residues between pH 7.9 and pH 10.5. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Probable tetramer of 2 alpha and 2 beta chains linked by disulfide bonds. The alpha chains contribute to the formation of the ligand-binding domain, while the beta chains carry the kinase domain (By similarity). {ECO:0000250}. DOMAIN: The extracellular domain is required for sensing alterations in external pH. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in the islets as well as in pancreatic beta-cells. {ECO:0000269|PubMed:10342810}. +Q99L90 MCRS1_MOUSE Microspherule protein 1 (58 kDa microspherule protein) 462 51,692 Chain (1); Coiled coil (1); Compositional bias (1); Domain (1); Modified residue (8); Motif (1); Sequence conflict (5) FUNCTION: Modulates the transcription repressor activity of DAXX by recruiting it to the nucleolus. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. Putative regulatory component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. May also be an inhibitor of TERT telomerase activity. Binds to G-quadruplex structures in mRNA. Binds to RNA homopolymer poly(G) and poly(U). {ECO:0000250|UniProtKB:Q96EZ8}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96EZ8}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q96EZ8}. Cytoplasm {ECO:0000250|UniProtKB:Q96EZ8}. Note=In microspherules in the nucleolus. {ECO:0000250|UniProtKB:Q96EZ8}. SUBUNIT: Component of the chromatin remodeling INO80 complex; specifically part of a complex module associated with the N-terminus of INO80. Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, KAT8/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Component of the NSL complex at least composed of MOF/KAT8, KANSL1, KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT, WDR5 and HCFC1. Interacts with NOP2. Interacts with PINX1. Interacts with TERT. Interacts with CCDC85B. Interacts with DAXX. Interacts (via N-terminus) with FMR1 (via phosphorylated form). Interacts with FXR1 AND FXR2. {ECO:0000250|UniProtKB:Q96EZ8}. +P49442 INPP_MOUSE Inositol polyphosphate 1-phosphatase (IPP) (IPPase) (EC 3.1.3.57) 396 43,346 Binding site (2); Chain (1); Metal binding (6); Modified residue (1); Region (1); Sequence conflict (2) Signal transduction; phosphatidylinositol signaling pathway. SUBUNIT: Monomer. {ECO:0000250}. +Q8QZV7 INT13_MOUSE Integrator complex subunit 13 (Cell cycle regulator Mat89Bb homolog) (Protein asunder homolog) (Spermatogenesis-associated protein 30) 732 82,780 Chain (1); Cross-link (1); Modified residue (2); Motif (1); Mutagenesis (1); Sequence conflict (3) FUNCTION: Crucial regulator of the mitotic cell cycle and development. At prophase, required for dynein anchoring to the nuclear envelope important for proper centrosome-nucleus coupling. At G2/M phase, may be required for proper spindle formation and execution of cytokinesis. Probable component of the Integrator (INT) complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. {ECO:0000250|UniProtKB:Q9NVM9}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23904267}. Cytoplasm {ECO:0000269|PubMed:23097494, ECO:0000269|PubMed:23904267}. Note=Nuclear location is required for recruitment of dynein motors to nuclear envelope at G2/M. {ECO:0000250|UniProtKB:Q9NVM9}. SUBUNIT: Interacts with PAFAH1B1; this interaction may be required for proper recruitment of dynein complexes to the nuclear envelope at prophase. {ECO:0000269|PubMed:23097494}. +Q8K114 INT9_MOUSE Integrator complex subunit 9 (Int9) 658 74,078 Alternative sequence (2); Chain (1); Cross-link (1); Erroneous initiation (1) FUNCTION: Component of the Integrator (INT) complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes. Mediates recruitment of cytoplasmic dynein to the nuclear envelope, probably as component of the INT complex. {ECO:0000250|UniProtKB:Q9NV88}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NV88}. SUBUNIT: Belongs to the multiprotein complex Integrator, at least composed of INTS1, INTS2, INTS3, INTS4, INTS5, INTS6, INTS7, INTS8, INTS9/RC74, INTS10, INTS11/CPSF3L and INTS12 (By similarity). Interacts with ESRRB, ESRRB is probably not a core component of the multiprotein complex Integrator and this association is a bridge for the interaction with the multiprotein complex Integrator; attracts the transcriptional machinery (PubMed:26206133). {ECO:0000250|UniProtKB:Q9NV88, ECO:0000269|PubMed:26206133}. +Q6P4S8 INT1_MOUSE Integrator complex subunit 1 (Int1) 2195 245,168 Chain (1); Erroneous initiation (1); Modified residue (9); Sequence caution (1); Sequence conflict (2); Transmembrane (1) TRANSMEM 1165 1185 Helical. {ECO:0000255}. FUNCTION: Component of the Integrator (INT) complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes. Mediates recruitment of cytoplasmic dynein to the nuclear envelope, probably as component of the INT complex. {ECO:0000250|UniProtKB:Q8N201}. SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. SUBUNIT: Belongs to the multiprotein complex Integrator, at least composed of INTS1, INTS2, INTS3, INTS4, INTS5, INTS6, INTS7, INTS8, INTS9/RC74, INTS10, INTS11/CPSF3L and INTS12 (By similarity). Interacts with ESRRB, ESRRB is probably not a core component of the multiprotein complex Integrator and this association is a bridge for the interaction with the multiprotein complex Integrator; attracts the transcriptional machinery (PubMed:26206133). {ECO:0000250|UniProtKB:Q8N201, ECO:0000269|PubMed:26206133}. +Q6PCM2 INT6_MOUSE Integrator complex subunit 6 (Int6) (DBI-1) (Protein DDX26) 883 99,661 Alternative sequence (4); Chain (1); Domain (1); Modified residue (1); Sequence caution (1); Sequence conflict (3) FUNCTION: Component of the Integrator (INT) complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes. Mediates recruitment of cytoplasmic dynein to the nuclear envelope, probably as component of the INT complex. {ECO:0000250|UniProtKB:Q9UL03}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UL03}. SUBUNIT: Belongs to the multiprotein complex Integrator, at least composed of INTS1, INTS2, INTS3, INTS4, INTS5, INTS6, INTS7, INTS8, INTS9/RC74, INTS10, INTS11/CPSF3L and INTS12. {ECO:0000250|UniProtKB:Q9UL03}. +Q7TQK1 INT7_MOUSE Integrator complex subunit 7 (Int7) 966 106,861 Alternative sequence (2); Chain (1); Compositional bias (1); Frameshift (1); Modified residue (2); Sequence conflict (3) FUNCTION: Component of the Integrator (INT) complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes. Plays a role in DNA damage response (DDR) signaling during the S phase. May be not involved in the recruitment of cytoplasmic dynein to the nuclear envelope by different components of the INT complex. {ECO:0000250|UniProtKB:Q9NVH2}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NVH2}. Chromosome {ECO:0000250|UniProtKB:Q9NVH2}. Cytoplasm {ECO:0000250|UniProtKB:Q9NVH2}. Note=Localizes to sites of DNA damage in a H2AX-independent manner. {ECO:0000250|UniProtKB:Q9NVH2}. SUBUNIT: Belongs to the multiprotein complex Integrator, at least composed of INTS1, INTS2, INTS3, INTS4, INTS5, INTS6, INTS7, INTS8, INTS9/RC74, INTS10, INTS11/CPSF3L and INTS12. Interacts with NABP2. {ECO:0000250|UniProtKB:Q9NVH2}. +P17919 HXB1_MOUSE Homeobox protein Hox-B1 (Homeobox protein Hox-2.9) 297 31,672 Chain (1); DNA binding (1); Motif (1); Sequence conflict (6) FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Acts on the anterior body structures. SUBCELLULAR LOCATION: Nucleus. +P01819 HVM43_MOUSE Ig heavy chain V region MOPC 141 144 15,759 Chain (1); Domain (1); Non-terminal residue (1); Signal peptide (1) +P02830 HXA7_MOUSE Homeobox protein Hox-A7 (Homeobox protein Hox-1.1) (Homeobox protein M6-12) (M6) 229 25,682 Chain (1); Compositional bias (3); DNA binding (1); Motif (1); Sequence conflict (1) FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. SUBCELLULAR LOCATION: Nucleus. +P01822 HVM46_MOUSE Ig heavy chain V region MOPC 315 137 15,399 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (7); Sequence conflict (5); Signal peptide (1) +P18524 HVM53_MOUSE Ig heavy chain V region RF 117 12,866 Beta strand (9); Chain (1); Disulfide bond (1); Helix (3); Non-terminal residue (1); Region (5); Signal peptide (1); Turn (1) +Q8R0V5 I23O2_MOUSE Indoleamine 2,3-dioxygenase 2 (IDO-2) (EC 1.13.11.-) (Indoleamine 2,3-dioxygenase-like protein 1) (Indoleamine-pyrrole 2,3-dioxygenase-like protein 1) 405 45,255 Chain (1); Erroneous initiation (1); Metal binding (1); Sequence conflict (1) Amino-acid degradation; L-tryptophan degradation via kynurenine pathway; L-kynurenine from L-tryptophan: step 1/2. FUNCTION: Catalyzes the first and rate-limiting step in the kynurenine pathway of tryptophan catabolism (PubMed:17499941, PubMed:17499941). Involved in immune regulation (PubMed:25477879). {ECO:0000269|PubMed:17499941, ECO:0000303|PubMed:25477879}. TISSUE SPECIFICITY: Expressed mainly in antigen-presenting immune cells, liver, kidney, brain, and placenta (PubMed:25691885, PubMed:17671174). Highly expressed in kidney, followed by epididymis and liver (at protein level) (PubMed:17499941). Detected in the tails of the spermatozoa in the testis and in the kidney tubules (at protein level) (PubMed:17499941). Constitutively expressed in brain. {ECO:0000269|PubMed:17499941, ECO:0000269|PubMed:17671174, ECO:0000303|PubMed:25691885}. +Q9Z1Q4 LY66C_MOUSE Lymphocyte antigen 6 complex locus protein G6c 126 14,066 Chain (1); Disulfide bond (4); Domain (1); Glycosylation (1); Lipidation (1); Propeptide (1); Signal peptide (1) PTM: N-glycosylated. {ECO:0000269|PubMed:16170054, ECO:0000269|PubMed:17008713}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000269|PubMed:17008713}. TISSUE SPECIFICITY: Highly expressed at the leading edges of cells, on filopodia. {ECO:0000269|PubMed:17008713}. +O08528 HXK2_MOUSE Hexokinase-2 (EC 2.7.1.1) (Hexokinase type II) (HK II) 917 102,535 Binding site (13); Chain (1); Domain (2); Modified residue (1); Nucleotide binding (6); Region (19) Carbohydrate metabolism; hexose metabolism. SUBUNIT: Monomer. Interacts with TIGAR; the interaction increases hexokinase HK2 activity in a hypoxia- and HIF1A-dependent manner. {ECO:0000250|UniProtKB:P35557, ECO:0000250|UniProtKB:P52789}. DOMAIN: The N- and C-terminal halves of this hexokinase show extensive sequence similarity to each other. The catalytic activity is associated with the C-terminus while regulatory function is associated with the N-terminus. +Q8JZL1 I17RD_MOUSE Interleukin-17 receptor D (IL-17 receptor D) (IL-17RD) (Interleukin-17 receptor-like protein) (Sef homolog) (mSef) 738 82,348 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (1); Glycosylation (8); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 300 320 Helical. {ECO:0000255}. TOPO_DOM 17 299 Extracellular. {ECO:0000255}.; TOPO_DOM 321 738 Cytoplasmic. {ECO:0000255}. FUNCTION: Feedback inhibitor of fibroblast growth factor mediated Ras-MAPK signaling and ERK activation. May inhibit FGF-induced FGFR1 tyrosine phosphorylation. Regulates the nuclear ERK signaling pathway by spatially blocking nuclear translocation of activated ERK (By similarity). Mediates JNK activation and may be involved in apoptosis. Might have a role in the early stages of fate specification of GnRH-secreting neurons. {ECO:0000250, ECO:0000269|PubMed:12604616, ECO:0000269|PubMed:15277532}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Associated with the Golgi apparatus and is partially translocated to the plasma membrane upon stimulation. {ECO:0000250}. SUBUNIT: Self-associates. Interacts with FGFR2 and phosphorylated MAP2K1 or MAP2K2. Associates with a MAP2K1/2-MAPK1/3 complex (By similarity). Interacts with FGFR1 and MAP3K7. {ECO:0000250, ECO:0000269|PubMed:12604616, ECO:0000269|PubMed:15277532}. +O54910 IKBE_MOUSE NF-kappa-B inhibitor epsilon (NF-kappa-BIE) (I-kappa-B-epsilon) (IkB-E) (IkB-epsilon) (IkappaBepsilon) 364 39,200 Chain (1); Modified residue (1); Repeat (6); Sequence conflict (4) FUNCTION: Inhibits NF-kappa-B by complexing with and trapping it in the cytoplasm. Inhibits DNA-binding of NF-kappa-B p50-p65 and p50-c-Rel complexes (By similarity). {ECO:0000250}. PTM: Serine phosphorylated; followed by proteasome-dependent degradation. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Interacts with RELA, REL, NFKB1 nuclear factor NF-kappa-B p50 subunit and NFKB2 nuclear factor NF-kappa-B p52 subunit. {ECO:0000250}. +O88995 IKBL1_MOUSE NF-kappa-B inhibitor-like protein 1 (Inhibitor of kappa B-like protein) (I-kappa-B-like protein) (IkappaBL) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells inhibitor-like 1) 381 43,202 Chain (1); Modified residue (1); Repeat (2); Sequence conflict (1) FUNCTION: Involved in the regulation of innate immune response. Acts as negative regulator of Toll-like receptor and interferon-regulatory factor (IRF) signaling pathways. Contributes to the negative regulation of transcriptional activation of NF-kappa-B target genes in response to endogenous proinflammatory stimuli (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Nuclear localization with a speckled expression pattern in some cells. Colocalizes with CACTIN in the nucleus (By similarity). {ECO:0000250}. SUBUNIT: Interacts with CACTIN (via N-terminal domain); the interaction occurs in a proinflammatory-independent manner. {ECO:0000250}. TISSUE SPECIFICITY: High expression found in heart muscle, liver, kidney and skin. Not detected in spleen, lung and brain. +Q9ESJ7 IKBP1_MOUSE Interleukin-1 receptor-associated kinase 1-binding protein 1 (IRAK1-binding protein 1) (ActA-binding protein 70) (PLK-interacting protein) (Signaling molecule that associates with the mouse pelle-like kinase) (SIMPL) 259 28,861 Chain (1); Erroneous initiation (1); Modified residue (7); Region (2); Sequence conflict (8) FUNCTION: Component of the IRAK1-dependent TNFRSF1A signaling pathway that leads to NF-kappa-B activation and is required for cell survival. Acts by enhancing RELA transcriptional activity. {ECO:0000269|PubMed:11096118, ECO:0000269|PubMed:15485901}. PTM: Phosphorylation at Ser-55, Ser-61 and/or Ser-63 is required for full activity. Phosphorylated on at least one of Ser-234, Thr-236, Ser-241 and Thr-246 upon TNF-alpha activation, which favors nuclear translocation. {ECO:0000269|PubMed:17079333}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15485901}. Nucleus {ECO:0000269|PubMed:15485901}. SUBUNIT: Interacts with IRAK1 and RELA. Interacts with HSPA8 and HSPA1. May interact with Listeria monocytogenes actA. {ECO:0000269|PubMed:11096118, ECO:0000269|PubMed:15485901, ECO:0000269|PubMed:17233114}. DOMAIN: The intrinsically disordered region interacts with HSPA1 and HSPA8. TISSUE SPECIFICITY: Expressed in testis, brain, kidney, liver and heart. {ECO:0000269|PubMed:11096118}. +Q9EST8 IKBZ_MOUSE NF-kappa-B inhibitor zeta (I-kappa-B-zeta) (IkB-zeta) (IkappaBzeta) (IL-1 inducible nuclear ankyrin-repeat protein) (INAP) (Molecule possessing ankyrin repeats induced by lipopolysaccharide) (MAIL) 728 79,007 Alternative sequence (2); Chain (1); Frameshift (1); Motif (1); Mutagenesis (3); Region (2); Repeat (7); Sequence conflict (14) FUNCTION: Involved in regulation of NF-kappa-B transcription factor complexes. Inhibits NF-kappa-B activity without affecting its nuclear translocation upon stimulation. Inhibits DNA-binding of RELA and NFKB1/p50, and of the NF-kappa-B p65-p50 heterodimer and the NF-kappa-B p50-p50 homodimer. Seems also to activate NF-kappa-B-mediated transcription. In vitro, upon association with NFKB1/p50 has transcriptional activation activity and, together with NFKB1/p50 and RELA, is recruited to LCN2 promoters. Promotes transcription of LCN2 and DEFB4. Is recruited to IL-6 promoters and activates IL-6 but decreases TNF-alpha production in response to LPS. Seems to be involved in the induction of inflammatory genes activated through TLR/IL-1 receptor signaling. May promote apoptosis (By similarity). Involved in the induction of T helper 17 cells (Th17) differentiation upon recognition of antigen by T cell antigen receptor (TCR) (PubMed:25282160). {ECO:0000250, ECO:0000269|PubMed:11356851, ECO:0000269|PubMed:15241416, ECO:0000269|PubMed:15618216, ECO:0000269|PubMed:17447895, ECO:0000269|PubMed:25282160}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11086164, ECO:0000269|PubMed:11278262, ECO:0000269|PubMed:11356851, ECO:0000269|PubMed:15618216}. SUBUNIT: Interacts with NFKB1/p50. Interacts with RELA; the interaction was not detected in (PubMed:11356851) (By similarity). {ECO:0000250, ECO:0000269|PubMed:11356851}. TISSUE SPECIFICITY: Expressed in kidney, liver, lung and heart. Expressed at very low levels in skeletal muscle, spleen and brain. {ECO:0000269|PubMed:11356851}. +Q9DBZ1 IKIP_MOUSE Inhibitor of nuclear factor kappa-B kinase-interacting protein (I kappa-B kinase-interacting protein) (IKBKB-interacting protein) (IKK-interacting protein) 373 42,532 Alternative sequence (1); Chain (1); Coiled coil (2); Frameshift (1); Glycosylation (1); Sequence conflict (9); Transmembrane (1) TRANSMEM 43 59 Helical. {ECO:0000255}. FUNCTION: Target of p53/TP53 with pro-apoptotic function. {ECO:0000250}. PTM: N-glycosylated at Asn-151. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. +Q60680 IKKA_MOUSE Inhibitor of nuclear factor kappa-B kinase subunit alpha (I-kappa-B kinase alpha) (IKK-A) (IKK-alpha) (IkBKA) (IkappaB kinase) (EC 2.7.11.10) (Conserved helix-loop-helix ubiquitous kinase) (I-kappa-B kinase 1) (IKK1) (Nuclear factor NF-kappa-B inhibitor kinase alpha) (NFKBIKA) 745 84,729 Active site (1); Alternative sequence (4); Binding site (1); Chain (1); Domain (1); Modified residue (3); Nucleotide binding (1); Region (2); Sequence conflict (2) FUNCTION: Serine kinase that plays an essential role in the NF-kappa-B signaling pathway which is activated by multiple stimuli such as inflammatory cytokines, bacterial or viral products, DNA damages or other cellular stresses. Acts as part of the canonical IKK complex in the conventional pathway of NF-kappa-B activation and phosphorylates inhibitors of NF-kappa-B on serine residues. These modifications allow polyubiquitination of the inhibitors and subsequent degradation by the proteasome. In turn, free NF-kappa-B is translocated into the nucleus and activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis. Negatively regulates the pathway by phosphorylating the scaffold protein TAXBP1 and thus promoting the assembly of the A20/TNFAIP3 ubiquitin-editing complex (composed of A20/TNFAIP3, TAX1BP1, and the E3 ligases ITCH and RNF11). Therefore, CHUK plays a key role in the negative feedback of NF-kappa-B canonical signaling to limit inflammatory gene activation. As part of the non-canonical pathway of NF-kappa-B activation, the MAP3K14-activated CHUK/IKKA homodimer phosphorylates NFKB2/p100 associated with RelB, inducing its proteolytic processing to NFKB2/p52 and the formation of NF-kappa-B RelB-p52 complexes. In turn, these complexes regulate genes encoding molecules involved in B-cell survival and lymphoid organogenesis. Participates also in the negative feedback of the non-canonical NF-kappa-B signaling pathway by phosphorylating and destabilizing MAP3K14/NIK. Within the nucleus, phosphorylates CREBBP and consequently increases both its transcriptional and histone acetyltransferase activities. Modulates chromatin accessibility at NF-kappa-B-responsive promoters by phosphorylating histones H3 at 'Ser-10' that are subsequently acetylated at 'Lys-14' by CREBBP. Additionally, phosphorylates the CREBBP-interacting protein NCOA3. Also phosphorylates FOXO3 and may regulate this pro-apoptotic transcription factor. {ECO:0000250|UniProtKB:O15111, ECO:0000269|PubMed:12789342}. PTM: Phosphorylated by MAP3K14/NIK, AKT and to a lesser extent by MEKK1, and dephosphorylated by PP2A. Autophosphorylated. {ECO:0000269|PubMed:9520401}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12789342}. Nucleus {ECO:0000269|PubMed:12789342}. Note=Shuttles between the cytoplasm and the nucleus. SUBUNIT: Component of the I-kappa-B-kinase (IKK) core complex consisting of CHUK, IKBKB and IKBKG; probably four alpha/CHUK-beta/IKBKB dimers are associated with four gamma/IKBKG subunits. The IKK core complex seems to associate with regulatory or adapter proteins to form a IKK-signalosome holo-complex (PubMed:10195894). The IKK complex associates with TERF2IP/RAP1, leading to promote IKK-mediated phosphorylation of RELA/p65 (PubMed:20622870). Part of a complex composed of NCOA2, NCOA3, CHUK/IKKA, IKBKB, IKBKG and CREBBP. Part of a 70-90 kDa complex at least consisting of CHUK/IKKA, IKBKB, NFKBIA, RELA, ELP1 and MAP3K14 (By similarity). Directly interacts with TRPC4AP (PubMed:14585990). May interact with TRAF2. Interacts with NALP2. May interact with MAVS/IPS1 (By similarity). Interacts with ARRB1 and ARRB2 (PubMed:18194271). Interacts with NLRC5; prevents CHUK phosphorylation and kinase activity. Interacts with PIAS1; this interaction induces PIAS1 phosphorylation. Interacts with ZNF268 isoform 2; the interaction is further increased in a TNF-alpha-dependent manner (By similarity). Interacts with LRRC14 (By similarity). {ECO:0000250|UniProtKB:O15111, ECO:0000269|PubMed:10195894, ECO:0000269|PubMed:14585990, ECO:0000269|PubMed:18194271, ECO:0000269|PubMed:20622870}. DOMAIN: The kinase domain is located in the N-terminal region. The leucine zipper is important to allow homo- and hetero-dimerization. At the C-terminal region is located the region responsible for the interaction with NEMO/IKBKG. TISSUE SPECIFICITY: Ubiquitous only for isoform 1, isoforms 2 and 3 are expressed predominantly in brain and T-lymphocytes. +P27546 MAP4_MOUSE Microtubule-associated protein 4 (MAP-4) 1125 117,429 Alternative sequence (9); Chain (1); Cross-link (1); Erroneous initiation (2); Initiator methionine (1); Modified residue (37); Repeat (4); Sequence conflict (13) FUNCTION: Non-neuronal microtubule-associated protein. Promotes microtubule assembly. PTM: Phosphorylated at serine residues in K-X-G-S motifs by MAP/microtubule affinity-regulating kinase (MARK1 or MARK2), causing detachment from microtubules, and their disassembly (By similarity). Phosphorylation on Ser-760 negatively regulates MAP4 activity to promote microtubule assembly. Isoform 4 is phosphorylated on Ser-333 and Ser-334 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SUBUNIT: Interacts with SEPT2; this interaction impedes tubulin-binding. Interacts with TRAF3IP1 (PubMed:26487268). {ECO:0000250, ECO:0000269|PubMed:26487268}. TISSUE SPECIFICITY: Testis, striated and cardiac muscle. +Q9R0T8 IKKE_MOUSE Inhibitor of nuclear factor kappa-B kinase subunit epsilon (I-kappa-B kinase epsilon) (IKK-E) (IKK-epsilon) (IkBKE) (EC 2.7.11.10) (Inducible I kappa-B kinase) (IKK-i) 717 80,953 Active site (1); Binding site (1); Chain (1); Cross-link (3); Domain (1); Modified residue (3); Mutagenesis (1); Nucleotide binding (1); Region (2); Sequence conflict (2) FUNCTION: Serine/threonine kinase that plays an essential role in regulating inflammatory responses to viral infection, through the activation of the type I IFN, NF-kappa-B and STAT signaling. Also involved in TNFA and inflammatory cytokines, like Interleukin-1, signaling. Following activation of viral RNA sensors, such as RIG-I-like receptors, associates with DDX3X and phosphorylates interferon regulatory factors (IRFs), IRF3 and IRF7, as well as DDX3X. This activity allows subsequent homodimerization and nuclear translocation of the IRF3 leading to transcriptional activation of pro-inflammatory and antiviral genes including IFNB. In order to establish such an antiviral state, IKBKE forms several different complexes whose composition depends on the type of cell and cellular stimuli. Thus, several scaffolding molecules including IPS1/MAVS, TANK, AZI2/NAP1 or TBKBP1/SINTBAD can be recruited to the IKBKE-containing-complexes. Activated by polyubiquitination in response to TNFA and interleukin-1, regulates the NF-kappa-B signaling pathway through, at least, the phosphorylation of CYLD. Phosphorylates inhibitors of NF-kappa-B thus leading to the dissociation of the inhibitor/NF-kappa-B complex and ultimately the degradation of the inhibitor. In addition, is also required for the induction of a subset of ISGs which displays antiviral activity, may be through the phosphorylation of STAT1 at 'Ser-708'. Phosphorylation of STAT1 at 'Ser-708' seems also to promote the assembly and DNA binding of ISGF3 (STAT1:STAT2:IRF9) complexes compared to GAF (STAT1:STAT1) complexes, in this way regulating the balance between type I and type II IFN responses. Protects cells against DNA damage-induced cell death. Also plays an important role in energy balance regulation by sustaining a state of chronic, low-grade inflammation in obesity, wich leads to a negative impact on insulin sensitivity. Phosphorylates AKT1. {ECO:0000269|PubMed:15210742, ECO:0000269|PubMed:17332413, ECO:0000269|PubMed:19737522, ECO:0000269|PubMed:22065572, ECO:0000269|PubMed:22171011, ECO:0000269|PubMed:23396211}. PTM: Sumoylation by TOPORS upon DNA damage is required for protection of cells against DNA damage-induced cell death. Desumoylated by SENP1 (By similarity). {ECO:0000250}.; PTM: Autophosphorylated and phosphorylated by IKBKB/IKKB. Phosphorylation at Ser-172 is enhanced by the interaction with DDX3X. Phosphorylated at Thr-503 upon IFN activation. {ECO:0000269|PubMed:17332413}.; PTM: 'Lys-63'-linked polyubiquitinated at Lys-30 and Lys-403 by TRAF2:BIRC2 and TRAF2:BIRC3 complexes. Ubiquitination is induced by LPS, TNFA and interleukin-1 and required for full kinase activity and KF-kappa-B pathway activation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14164}. Nucleus {ECO:0000250|UniProtKB:Q14164}. Nucleus, PML body {ECO:0000250|UniProtKB:Q14164}. Note=Targeting to PML nuclear bodies upon DNA damage is TOPORS-dependent. Located diffusely throughout the cytoplasm but locates to punctate cytoplasmic bodies when coexpressed with TRIM6. {ECO:0000250|UniProtKB:Q14164}. SUBUNIT: Homodimer. Interacts with MAVS/IPS1. Interacts with the adapter proteins AZI2/NAP1, TANK and TBKBP1/SINTBAD. Interacts with SIKE1. Interacts with TICAM1/TRIF, IRF3 and DDX58/RIG-I; interactions are disrupted by the interaction besotween IKBKE and SIKE1. Interacts with TOPORS; induced by DNA damage. Interacts with CYLD, IKBKB, IKBKG and MYD88. Interacts with IFIH1. Interacts with DDX3X; the interaction is found to be induced upon virus infection. Interacts with TRIM6 (via SPRY box). Interacts with unanchored K48-linked polyubiquitin chains; this leads to IKBKE activation (By similarity). {ECO:0000250|UniProtKB:Q14164, ECO:0000269|PubMed:17568778}. TISSUE SPECIFICITY: Expressed in bone marrow-derived macrophages and at low levels in liver and white adipose tissue (at protein level). Detected in muscle and lung. {ECO:0000269|PubMed:17332413, ECO:0000269|PubMed:19737522, ECO:0000269|PubMed:23396211}. +O88735 MAP7_MOUSE Ensconsin (Epithelial microtubule-associated protein of 115 kDa) (E-MAP-115) (Microtubule-associated protein 7) (MAP-7) 730 82,022 Alternative sequence (1); Chain (1); Coiled coil (2); Cross-link (5); Initiator methionine (1); Modified residue (14); Sequence caution (1); Sequence conflict (8) FUNCTION: Microtubule-stabilizing protein that may play an important role during reorganization of microtubules during polarization and differentiation of epithelial cells. Associates with microtubules in a dynamic manner. May play a role in the formation of intercellular contacts. Colocalization with TRPV4 results in the redistribution of TRPV4 toward the membrane and may link cytoskeletal microfilaments. {ECO:0000269|PubMed:14517216}. PTM: The association with microtubules is regulated by phosphorylation during the cell cycle. During interphase only phosphorylated on serine. Phosphorylated on threonine in mitosis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:14517216}. Basolateral cell membrane {ECO:0000269|PubMed:14517216}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:14517216}. Note=Colocalized on microtubules. An intracellular redistribution is triggered during induction of keratinocyte terminal differentiation from microtubules with a perinuclear localization to cortical microtubules organized in spike-like bundles facing intercellular contacts. SUBUNIT: Interacts with TRPV4. {ECO:0000269|PubMed:14517216}. TISSUE SPECIFICITY: Highly expressed in the epithelial cells of the kidney tubules and in the absorptive cells of the intestine, and widely distributed in the testis. Expression correlates with the differentiation of certain epithelial cell types: in the adult intestine, more abundantly expressed in the differentiating than in the proliferative cell compartment. The expression clearly correlates with the degree of cellular apicobasal polarity. Expressed in lung, kidney, brain and fat. Colocalized with TRPV4 in ependymal cells, in the choroid plexus, in bronchial and renal cortical tubular cells. Widely expressed in excitable neuronal cells, vascular cells as well as in epithelial cells. In seminiferous epithelium, associated with the microtubule of the spermatid manchette. {ECO:0000269|PubMed:12755995, ECO:0000269|PubMed:14517216, ECO:0000269|PubMed:9745708}. +Q8BU33 ILVBL_MOUSE Acetolactate synthase-like protein (EC 2.2.1.-) (IlvB-like protein) 632 68,156 Alternative sequence (4); Binding site (1); Chain (1); Metal binding (2); Modified residue (1); Region (1); Transmembrane (1) TRANSMEM 13 33 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. +P56671 MAZ_MOUSE Myc-associated zinc finger protein (MAZI) (Pur-1) (Purine-binding transcription factor) 477 48,770 Chain (1); Compositional bias (6); Modified residue (1); Sequence conflict (1); Zinc finger (6) FUNCTION: Transcriptional activator that binds to purine-rich GAGA sites found in the promoter of many genes including insulin I and II and islet amyloid polypeptide. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with BPTF. {ECO:0000250}. +Q78HU3 MB12A_MOUSE Multivesicular body subunit 12A (ESCRT-I complex subunit MVB12A) (Protein FAM125A) 271 28,705 Chain (1); Domain (2); Modified residue (7); Motif (1); Region (1) FUNCTION: Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies. May be involved in the ligand-mediated internalization and down-regulation of EGF receptor (By similarity). {ECO:0000250}. PTM: Phosphorylated on Tyr-202 upon EGF stimulation. Phosphorylation is required for interaction with CD2AP and CIN85/SH3KBP1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Nucleus {ECO:0000250}. Endosome. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Late endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Colocalizes with F-actin. Some fraction may be nuclear (By similarity). {ECO:0000250}. SUBUNIT: Component of the ESCRT-I complex (endosomal sorting complex required for transport I) which consists of TSG101, VPS28, a VPS37 protein (VPS37A to -D) and MVB12A or MVB12B in a 1:1:1:1 stoichiometry. Interacts with CD2AP and CIN85/SH3KBP1. Interacts with CD2AP (via one of the SH3 domains). Interacts with TSG101; the association appears to be mediated by the TSG101-VPS37 binary subcomplex. Interacts with VPS28. Interacts with VPS37B; the association appears to be mediated by the TSG101-VPS37 binary subcomplex. Interacts with VPS37C; the association appears to be mediated by the TSG101-VPS37 binary subcomplex. Interacts with VPS37D; the association appears to be mediated by the TSG101-VPS37 binary subcomplex. Interacts with CEP55 (By similarity). {ECO:0000250}. +Q8BPP1 MB212_MOUSE Protein mab-21-like 2 359 40,907 Chain (1); Sequence conflict (3) FUNCTION: Required for several aspects of embryonic development including normal development of the eye, notochord, neural tube and other organ tissues, and for embryonic turning. {ECO:0000269|PubMed:11857508, ECO:0000269|PubMed:15385160}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10556287}. Cytoplasm {ECO:0000250|UniProtKB:Q9Y586}. Note=Predominantly localizes to the nucleus, with some cytoplasmic localization. {ECO:0000250|UniProtKB:Q9Y586}. TISSUE SPECIFICITY: Expressed in the adult cerebellum and eye, with lower levels in the adult forebrain (PubMed:10556287). In embryos at 10.5 days post-coitum strongly expressed in the rostral and distal regions of the developing neural retina, with no expression immediately adjacent to the closing optic fissure. Expression is also observed in the dorsal and ventral aspects of the developing forelimb bud and in the developing pharyngeal arches, as well as in the midbrain (PubMed:24906020). {ECO:0000269|PubMed:10556287, ECO:0000269|PubMed:24906020}. +Q7TPV4 MBB1A_MOUSE Myb-binding protein 1A (Myb-binding protein of 160 kDa) 1344 152,037 Chain (1); Compositional bias (1); Cross-link (1); Initiator methionine (1); Modified residue (20); Motif (2); Mutagenesis (4); Region (2); Sequence conflict (5) FUNCTION: May activate or repress transcription via interactions with sequence specific DNA-binding proteins (PubMed:9447996, PubMed:11956195, PubMed:14744933). Repression may be mediated at least in part by histone deacetylase activity (HDAC activity) (PubMed:14744933). Acts as a corepressor and in concert with CRY1, represses the transcription of the core circadian clock component PER2 (PubMed:19129230). Preferentially binds to dimethylated histone H3 'Lys-9' (H3K9me2) on the PER2 promoter (PubMed:19129230). Has a role in rRNA biogenesis together with PWP1 (By similarity). {ECO:0000250|UniProtKB:Q9BQG0, ECO:0000269|PubMed:11956195, ECO:0000269|PubMed:14744933, ECO:0000269|PubMed:19129230, ECO:0000269|PubMed:9447996}. PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12941609}. Nucleus, nucleolus {ECO:0000269|PubMed:12941609, ECO:0000269|PubMed:19129230}. Cytoplasm {ECO:0000269|PubMed:12941609}. Note=Predominantly nucleolar. Also shuttles between the nucleus and cytoplasm. Nuclear import may be mediated by KPNA2, while export appears to depend partially on XPO1/CRM1. {ECO:0000269|PubMed:12941609}. SUBUNIT: Component of the B-WICH complex, at least composed of SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21 (By similarity). Binds to and represses JUN and MYB via the leucine zipper regions present in these proteins. Also binds to and represses PPARGC1A: this interaction is abrogated when PPARGC1A is phosphorylated by MAPK1/ERK. Binds to and stimulates transcription by AHR. Binds to KPNA2. Interacts with CLOCK and CRY1. {ECO:0000250|UniProtKB:Q9BQG0, ECO:0000269|PubMed:11956195, ECO:0000269|PubMed:12941609, ECO:0000269|PubMed:14744933, ECO:0000269|PubMed:19129230, ECO:0000269|PubMed:9447996}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:9447996}. +B1AYB6 MBD5_MOUSE Methyl-CpG-binding domain protein 5 (Methyl-CpG-binding protein MBD5) 1498 160,292 Chain (1); Compositional bias (1); Domain (2) FUNCTION: Binds to heterochromatin. Does not interact with either methylated or unmethylated DNA (in vitro) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}. Note=Associated with pericentric heterochromatin. {ECO:0000250}. DOMAIN: Both MBD and PWWP domains are necessary for chromocentric localization. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:20700456}. +Q99LQ1 MBIP1_MOUSE MAP3K12-binding inhibitory protein 1 (MAPK upstream kinase-binding inhibitory protein) (MUK-binding inhibitory protein) 341 38,333 Chain (1); Cross-link (8); Modified residue (2); Region (3) FUNCTION: Inhibits the MAP3K12 activity to induce the activation of the JNK/SAPK pathway. Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Shows a cytoplasmic localization when co-expressed with MAP3K12. {ECO:0000250}. SUBUNIT: Component of the ADA2A-containing complex (ATAC), composed of KAT14, KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1. In the complex, it probably interacts directly with KAT2A, KAT14 and WDR5. {ECO:0000250}. +Q8R3I2 MBOA2_MOUSE Lysophospholipid acyltransferase 2 (LPLAT 2) (EC 2.3.1.-) (1-acylglycerophosphocholine O-acyltransferase) (EC 2.3.1.23) (1-acylglycerophosphoethanolamine O-acyltransferase) (EC 2.3.1.n7) (Lysophosphatidylcholine acyltransferase) (LPCAT) (Lyso-PC acyltransferase) (Lysophosphatidylcholine acyltransferase 4) (Lyso-PC acyltransferase 4) (mLPCAT4) (Lysophosphatidylethanolamine acyltransferase) (LPEAT) (Lyso-PE acyltransferase) (Membrane-bound O-acyltransferase domain-containing protein 2) (O-acyltransferase domain-containing protein 2) 519 58,995 Active site (2); Alternative sequence (3); Chain (1); Erroneous initiation (1); Sequence conflict (2); Transmembrane (9) TRANSMEM 22 42 Helical. {ECO:0000255}.; TRANSMEM 61 81 Helical. {ECO:0000255}.; TRANSMEM 88 108 Helical. {ECO:0000255}.; TRANSMEM 184 204 Helical. {ECO:0000255}.; TRANSMEM 236 256 Helical. {ECO:0000255}.; TRANSMEM 263 283 Helical. {ECO:0000255}.; TRANSMEM 365 385 Helical. {ECO:0000255}.; TRANSMEM 415 435 Helical. {ECO:0000255}.; TRANSMEM 443 463 Helical. {ECO:0000255}. Lipid metabolism; phospholipid metabolism. FUNCTION: Acyltransferase which mediates the conversion of lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) into phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC) (LPCAT activity). To a lesser extent, also catalyzes the acylation of lysophosphatidylethanolamine (1-acyl-sn-glycero-3-phosphoethanolamine or LPE) into phosphatidylethanolamine (1,2-diacyl-sn-glycero-3-phosphoethanolamine or PE) (LPEAT activity). Prefers oleoyl-CoA as the acyl donor. Lysophospholipid acyltransferases (LPLATs) catalyze the reacylation step of the phospholipid remodeling pathway also known as the Lands cycle. {ECO:0000269|PubMed:18287005}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Endoplasmic reticulum {ECO:0000269|PubMed:18287005}. TISSUE SPECIFICITY: Highly expressed in epididymis, brain, testis, and ovary. {ECO:0000269|PubMed:18287005}. +P0C7A3 MBOA4_MOUSE Ghrelin O-acyltransferase (EC 2.3.1.-) (Membrane-bound O-acyltransferase domain-containing protein 4) (O-acyltransferase domain-containing protein 4) 435 49,879 Active site (2); Chain (1); Erroneous initiation (2); Mutagenesis (3); Sequence conflict (4); Transmembrane (7) TRANSMEM 6 26 Helical. {ECO:0000255}.; TRANSMEM 45 65 Helical. {ECO:0000255}.; TRANSMEM 163 183 Helical. {ECO:0000255}.; TRANSMEM 241 261 Helical. {ECO:0000255}.; TRANSMEM 331 351 Helical. {ECO:0000255}.; TRANSMEM 377 397 Helical. {ECO:0000255}.; TRANSMEM 408 428 Helical. {ECO:0000255}. FUNCTION: Mediates the octanoylation of ghrelin at 'Ser-3'. Can use a variety of fatty acids as substrates including octanoic acid, decanoic acid and tetradecanoic acid. {ECO:0000269|PubMed:18267071, ECO:0000269|PubMed:18443287}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18267071}; Multi-pass membrane protein {ECO:0000269|PubMed:18267071}. TISSUE SPECIFICITY: Highly expressed in stomach. Lower expression in small intestine and colon. Very low expression in testis. {ECO:0000269|PubMed:18267071}. +Q91V01 MBOA5_MOUSE Lysophospholipid acyltransferase 5 (LPLAT 5) (EC 2.3.1.-) (1-acylglycerophosphocholine O-acyltransferase) (EC 2.3.1.23) (1-acylglycerophosphoethanolamine O-acyltransferase) (EC 2.3.1.n7) (1-acylglycerophosphoserine O-acyltransferase) (EC 2.3.1.n6) (Lysophosphatidylcholine acyltransferase) (LPCAT) (Lyso-PC acyltransferase) (Lysophosphatidylcholine acyltransferase 3) (Lyso-PC acyltransferase 3) (mLPCAT3) (Lysophosphatidylethanolamine acyltransferase) (LPEAT) (Lyso-PE acyltransferase) (Lysophosphatidylserine acyltransferase) (LPSAT) (Lyso-PS acyltransferase) (Membrane-bound O-acyltransferase domain-containing protein 5) (O-acyltransferase domain-containing protein 5) 487 56,147 Active site (2); Chain (1); Glycosylation (3); Initiator methionine (1); Modified residue (1); Motif (1); Sequence conflict (1); Transmembrane (9) TRANSMEM 44 64 Helical. {ECO:0000255}.; TRANSMEM 84 104 Helical. {ECO:0000255}.; TRANSMEM 111 131 Helical. {ECO:0000255}.; TRANSMEM 180 200 Helical. {ECO:0000255}.; TRANSMEM 236 256 Helical. {ECO:0000255}.; TRANSMEM 285 305 Helical. {ECO:0000255}.; TRANSMEM 364 384 Helical. {ECO:0000255}.; TRANSMEM 422 442 Helical. {ECO:0000255}.; TRANSMEM 453 473 Helical. {ECO:0000255}. Lipid metabolism; phospholipid metabolism. FUNCTION: Acyltransferase which mediates the conversion of lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) into phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC) (LPCAT activity). To a lesser extent, also catalyzes the acylation of lysophosphatidylethanolamine (1-acyl-sn-glycero-3-phosphoethanolamine or LPE) into phosphatidylethanolamine (1,2-diacyl-sn-glycero-3-phosphoethanolamine or PE) (LPEAT activity), and the conversion of lysophosphatidylserine (1-acyl-2-hydroxy-sn-glycero-3-phospho-L-serine or LPS) into phosphatidylserine (1,2-diacyl-sn-glycero-3-phospho-L-serine or PS) (LPSAT activity). Favors polyunsaturated fatty acyl-CoAs as acyl donors compared to saturated fatty acyl-CoAs. Seems to be the major enzyme contributing to LPCAT activity in the liver. Lysophospholipid acyltransferases (LPLATs) catalyze the reacylation step of the phospholipid remodeling pathway also known as the Lands cycle. {ECO:0000269|PubMed:18287005}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18287005}; Multi-pass membrane protein {ECO:0000269|PubMed:18287005}. DOMAIN: The di-lysine motif confers endoplasmic reticulum localization. {ECO:0000250}. TISSUE SPECIFICITY: Detected ubiquitously, with high expression levels in testis. {ECO:0000269|PubMed:18287005}. +Q8CHK3 MBOA7_MOUSE Lysophospholipid acyltransferase 7 (LPLAT 7) (EC 2.3.1.-) (1-acylglycerophosphatidylinositol O-acyltransferase) (EC 2.3.1.n4) (Bladder and breast carcinoma-overexpressed gene 1 protein) (Leukocyte receptor cluster member 4) (Lysophosphatidylinositol acyltransferase 1) (LPIAT1) (Membrane-bound O-acyltransferase domain-containing protein 7) (O-acyltransferase domain-containing protein 7) (m-mboa-7) 473 53,436 Chain (1); Glycosylation (1); Sequence conflict (6); Transmembrane (7) TRANSMEM 9 29 Helical. {ECO:0000255}.; TRANSMEM 44 64 Helical. {ECO:0000255}.; TRANSMEM 74 94 Helical. {ECO:0000255}.; TRANSMEM 197 217 Helical. {ECO:0000255}.; TRANSMEM 247 267 Helical. {ECO:0000255}.; TRANSMEM 355 375 Helical. {ECO:0000255}.; TRANSMEM 429 449 Helical. {ECO:0000255}. Lipid metabolism; phospholipid metabolism. FUNCTION: Acyltransferase which contributes to the regulation of free arachidonic acid (AA) in the cell through the remodeling of phospholipids. Mediates the conversion of lysophosphatidylinositol (1-acylglycerophosphatidylinositol or LPI) into phosphatidylinositol (1,2-diacyl-sn-glycero-3-phosphoinositol or PI) (LPIAT activity). Prefers arachidonoyl-CoA as the acyl donor (PubMed:23097495). Lysophospholipid acyltransferases (LPLATs) catalyze the reacylation step of the phospholipid remodeling pathway also known as the Lands cycle (By similarity). Required for cortical lamination during brain development (PubMed:23097495). {ECO:0000250|UniProtKB:Q96N66, ECO:0000269|PubMed:23097495}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q5FW53 MBPHL_MOUSE Myosin-binding protein H-like 355 38,760 Chain (1); Disulfide bond (1); Domain (3); Modified residue (2) +P04370 MBP_MOUSE Myelin basic protein (MBP) (Myelin A1 protein) 250 27,168 Alternative sequence (9); Beta strand (1); Chain (1); Helix (1); Initiator methionine (6); Modified residue (42); Sequence conflict (1) FUNCTION: The classic group of MBP isoforms (isoform 4-isoform 13) are with PLP the most abundant protein components of the myelin membrane in the CNS. They have a role in both its formation and stabilization. The non-classic group of MBP isoforms (isoform 1-isoform 3/Golli-MBPs) may preferentially have a role in the early developing brain long before myelination, maybe as components of transcriptional complexes, and may also be involved in signaling pathways in T-cells and neural cells. Differential splicing events combined to optional post-translational modifications give a wide spectrum of isomers, with each of them potentially having a specialized function. {ECO:0000269|PubMed:11145205}. PTM: As in other animals, several charge isomers may be produced as a result of optional post-translational modifications, such as phosphorylation of serine or threonine residues, deamidation of glutamine or asparagine residues, citrullination and methylation of arginine residues.; PTM: Methylated on arginine residues; decreases with the age of the animal, making MBP more cationic.; PTM: Phosphorylated by TAOK2, VRK2, MAPK11, MAPK12, MAPK14 and MINK1. {ECO:0000250}. SUBCELLULAR LOCATION: Isoform 13: Myelin membrane; Peripheral membrane protein; Cytoplasmic side.; SUBCELLULAR LOCATION: Isoform 12: Myelin membrane; Peripheral membrane protein; Cytoplasmic side.; SUBCELLULAR LOCATION: Isoform 11: Myelin membrane; Peripheral membrane protein; Cytoplasmic side.; SUBCELLULAR LOCATION: Isoform 10: Myelin membrane; Peripheral membrane protein; Cytoplasmic side.; SUBCELLULAR LOCATION: Isoform 9: Myelin membrane; Peripheral membrane protein; Cytoplasmic side.; SUBCELLULAR LOCATION: Isoform 8: Myelin membrane; Peripheral membrane protein; Cytoplasmic side.; SUBCELLULAR LOCATION: Isoform 7: Myelin membrane; Peripheral membrane protein; Cytoplasmic side.; SUBCELLULAR LOCATION: Isoform 6: Myelin membrane; Peripheral membrane protein; Cytoplasmic side.; SUBCELLULAR LOCATION: Isoform 5: Myelin membrane; Peripheral membrane protein; Cytoplasmic side.; SUBCELLULAR LOCATION: Isoform 4: Myelin membrane; Peripheral membrane protein; Cytoplasmic side.; SUBCELLULAR LOCATION: Isoform 3: Cytoplasm. Nucleus.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Nucleus.; SUBCELLULAR LOCATION: Isoform 1: Cytoplasm. Nucleus. SUBUNIT: Homodimer. {ECO:0000250}. TISSUE SPECIFICITY: In the embryo, isoform 1-isoform 3 are found in neurons within the central nervous system (primarily in pioneer neurons important in the formation of the cortex) and the peripheral nervous system. They are also expressed in the thymus, gut, lung and kidney. In the adult, isoform 1-isoform 3 are highly expressed in the brain (mainly in brain regions rich in oligodendrocytes) and spleen. Lower levels are seen in the heart, kidney and lung. Isoform 2 is also found in cells of the immune system. The isoforms missing the 134 first amino acids (isoform 4-isoform 13) are almost exclusively produced in the myelin-forming cells, the mature oligodendrocytes. DISEASE: Note=Defects in Mbp are a cause of dysmyelinating diseases such as the shiverer (SHI) and myelin deficient (MLD) diseases characterized by decreased myelination in the CNS, tremors, and convulsions of progressively increasing severity leading to early death. The shiverer mice only express isoform 2, the MLD mice have a reduced amount of Mbp. +Q8CIV2 MBRL_MOUSE Membralin (Transmembrane protein 259) 574 63,561 Alternative sequence (1); Chain (1); Erroneous initiation (1); Glycosylation (1); Initiator methionine (1); Modified residue (1); Sequence conflict (11); Transmembrane (4) TRANSMEM 69 89 Helical. {ECO:0000255}.; TRANSMEM 293 313 Helical. {ECO:0000255}.; TRANSMEM 337 357 Helical. {ECO:0000255}.; TRANSMEM 417 437 Helical. {ECO:0000255}. FUNCTION: May have a role in the ERAD pathway required for clearance of misfolded proteins in the endoplasmic reticulum (ER). Promotes survival of motor neurons, probably by protecting against ER stress. {ECO:0000269|PubMed:25977983}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:25977983}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Interacts with ERLIN2. {ECO:0000269|PubMed:25977983}. TISSUE SPECIFICITY: Detected in brain, spinal cord, lung, liver and kidney. {ECO:0000269|PubMed:25977983}. +P97311 MCM6_MOUSE DNA replication licensing factor MCM6 (EC 3.6.4.12) (Mis5 homolog) 821 92,867 Chain (1); Domain (1); Modified residue (10); Motif (1); Nucleotide binding (1) FUNCTION: Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. PTM: O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Binds to chromatin during G1 and detach from it during S phase. {ECO:0000250}. SUBUNIT: Component of the MCM2-7 complex. The complex forms a toroidal hexameric ring with the proposed subunit order MCM2-MCM6-MCM4-MCM7-MCM3-MCM5 (Probable). May interact with MCM10. Interacts with TIPIN. Interacts with MCMBP (By similarity). {ECO:0000250, ECO:0000305}. +Q61881 MCM7_MOUSE DNA replication licensing factor MCM7 (EC 3.6.4.12) (CDC47 homolog) 719 81,211 Chain (1); Cross-link (2); Domain (1); Initiator methionine (1); Modified residue (5); Motif (1); Nucleotide binding (1); Region (2) FUNCTION: Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. Required for S-phase checkpoint activation upon UV-induced damage. PTM: O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the MCM2-7 complex. The complex forms a toroidal hexameric ring with the proposed subunit order MCM2-MCM6-MCM4-MCM7-MCM3-MCM5. Interacts with the ATR-ATRIP complex and with RAD17. Interacts with TIPIN. Interacts with MCMBP (By similarity). Interacts with ANKRD17. Component of the replisome complex composed of at least DONSON, MCM2, MCM7, PCNA and TICRR (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P33993}. +Q9CWV1 MCM8_MOUSE DNA helicase MCM8 (EC 3.6.4.12) (Minichromosome maintenance 8) 833 92,371 Alternative sequence (1); Chain (1); Domain (1); Modified residue (1); Nucleotide binding (1); Sequence conflict (3) FUNCTION: Component of the MCM8-MCM9 complex, a complex involved in the repair of double-stranded DNA breaks (DBSs) and DNA interstrand cross-links (ICLs) by homologous recombination (HR). Required for DNA resection by the MRE11-RAD50-NBN/NBS1 (MRN) complex by recruiting the MRN complex to the repair site and by promoting the complex nuclease activity. Probably by regulating the localization of the MNR complex, indirectly regulates the recruitment of downstream effector RAD51 to DNA damage sites including DBSs and ICLs. The MCM8-MCM9 complex is dispensable for DNA replication and S phase progression. However, may play a non-essential for DNA replication: may be involved in the activation of the prereplicative complex (pre-RC) during G(1) phase by recruiting CDC6 to the origin recognition complex (ORC) (By similarity). Probably by regulating HR, plays a key role during gametogenesis (PubMed:22771120). Stabilizes MCM9 protein (By similarity). {ECO:0000250|UniProtKB:Q9UJA3, ECO:0000269|PubMed:22771120}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UJA3}. Chromosome {ECO:0000250|UniProtKB:Q9UJA3}. Note=Localizes to nuclear foci. Localizes to double-stranded DNA breaks. Binds chromatin throughout the cell cycle. {ECO:0000250|UniProtKB:Q9UJA3}. SUBUNIT: Component of the MCM8-MCM9 complex, which forms a hexamer composed of MCM8 and MCM9. Interacts with the DNA mismatch repair (MMR) complex composed at least of MSH2, MSH3, MSH6, PMS1 and MLH1. Interacts with RAD51; the interaction recruits RAD51 to DNA damage sites. Interacts with the MRN complex composed of MRE11, RAD50 and NBN/NBS1. Interacts with CDC6 and ORC2. {ECO:0000250|UniProtKB:Q9UJA3}. +Q2KHI9 MCM9_MOUSE DNA helicase MCM9 (EC 3.6.4.12) (Mini-chromosome maintenance deficient domain-containing protein 1) (Minichromosome maintenance 9) 1134 125,814 Alternative sequence (3); Chain (1); Domain (1); Modified residue (2); Nucleotide binding (1); Sequence conflict (4) FUNCTION: Component of the MCM8-MCM9 complex, a complex involved in the repair of double-stranded DNA breaks (DBSs) and DNA interstrand cross-links (ICLs) by homologous recombination (HR) (PubMed:23401855, PubMed:22771120). Required for DNA resection by the MRE11-RAD50-NBN/NBS1 (MRN) complex at double-stranded DNA breaks to generate ssDNA by recruiting the MRN complex to the repair site and by promoting the complex nuclease activity (By similarity). Probably by regulating the localization of the MNR complex, indirectly regulates the recruitment of downstream effector RAD51 to DNA damage sites including DBSs and ICLs (PubMed:22771120, PubMed:23401855). Acts as an helicase in DNA mismatch repair (MMR) following DNA replication errors to unwind the mismatch containing DNA strand (PubMed:22771120, PubMed:26300262). In addition, recruits MLH1, a component of the MMR complex, to chromatin (By similarity). The MCM8-MCM9 complex is dispensable for DNA replication and S phase progression (PubMed:21987787). Probably by regulating HR, plays a key role during gametogenesis (PubMed:21987787, PubMed:22771120). {ECO:0000250|UniProtKB:Q9NXL9, ECO:0000269|PubMed:21987787, ECO:0000269|PubMed:22771120, ECO:0000269|PubMed:23401855, ECO:0000269|PubMed:26300262}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23401855}. Chromosome {ECO:0000269|PubMed:23401855}. Note=Colocalizes to nuclear foci with RPA1 following DNA damage (PubMed:23401855). Localizes to double-stranded DNA breaks (By similarity). Recruited to chromatin by MSH2 (By similarity). {ECO:0000250|UniProtKB:Q9NXL9, ECO:0000269|PubMed:23401855}. SUBUNIT: Component of the MCM8-MCM9 complex, which forms a hexamer composed of MCM8 and MCM9 (PubMed:22771120). Interacts with the DNA mismatch repair (MMR) complex composed at least of MSH2, MSH3, MSH6, PMS1 and MLH1 (By similarity). Interacts with MLH1; the interaction recruits MLH1 to chromatin (By similarity). Interacts with MSH2; the interaction recruits MCM9 to chromatin (By similarity). Interacts with MSH6 (By similarity). Interacts with the MRN complex composed of MRE11, RAD50 and NBN/NBS1; the interaction recruits the MRN complex to DNA damage sites (By similarity). Interacts with RAD51; the interaction recruits RAD51 to DNA damage sites (By similarity). {ECO:0000250|UniProtKB:Q9NXL9, ECO:0000269|PubMed:22771120}. TISSUE SPECIFICITY: Ubiquitously expressed. {ECO:0000269|PubMed:21987787}. +P09602 HMGN2_MOUSE Non-histone chromosomal protein HMG-17 (High mobility group nucleosome-binding domain-containing protein 2) 90 9,423 Chain (1); Cross-link (1); Initiator methionine (1); Modified residue (4) FUNCTION: Binds to the inner side of the nucleosomal DNA thus altering the interaction between the DNA and the histone octamer. May be involved in the process which maintains transcribable genes in a unique chromatin conformation (By similarity). {ECO:0000250}. PTM: Phosphorylation favors cytoplasmic localization. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Cytoplasmic enrichment upon phosphorylation. {ECO:0000250}. +Q7TMK9 HNRPQ_MOUSE Heterogeneous nuclear ribonucleoprotein Q (hnRNP Q) (Glycine- and tyrosine-rich RNA-binding protein) (GRY-RBP) (NS1-associated protein 1) (Synaptotagmin-binding, cytoplasmic RNA-interacting protein) (pp68) 623 69,633 Alternative sequence (2); Chain (1); Compositional bias (1); Cross-link (2); Domain (3); Erroneous initiation (2); Initiator methionine (1); Modified residue (18); Motif (1); Region (4); Repeat (11); Sequence conflict (14) FUNCTION: Heterogeneous nuclear ribonucleoprotein (hnRNP) implicated in mRNA processing mechanisms. Component of the CRD-mediated complex that promotes MYC mRNA stability. Isoform 1 and isoform 2 are associated in vitro with pre-mRNA, splicing intermediates and mature mRNA protein complexes. Isoform 1 binds to apoB mRNA AU-rich sequences (By similarity). Isoform 1 is part of the APOB mRNA editosome complex and may modulate the postranscriptional C to U RNA-editing of the APOB mRNA through either by binding to A1CF (APOBEC1 complementation factor), to APOBEC1 or to RNA itself (By similarity). May be involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain (By similarity). Interacts in vitro preferentially with poly(A) and poly(U) RNA sequences. Isoform 2 may be involved in cytoplasmic vesicle-based mRNA transport through interaction with synaptotagmins. {ECO:0000250}. PTM: Phosphorylated on tyrosine. The membrane-bound form found in microsomes is phosphorylated in vitro by insulin receptor tyrosine kinase (INSR). Phosphorylation is inhibited upon binding to RNA, whereas the cytoplasmic form is poorly phosphorylated. {ECO:0000269|PubMed:11994298}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10734137, ECO:0000269|PubMed:11994298}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:O43390}. Microsome {ECO:0000269|PubMed:11994298}. Cytoplasm {ECO:0000269|PubMed:10734137}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs (By similarity). Isoforms 1 and 2 are expressed predominantly in the nucleoplasm. According to PubMed:10734137, isoform 2 is predominantly found in cytoplasm. The tyrosine phosphorylated form bound to RNA is found in microsomes. {ECO:0000250|UniProtKB:O43390, ECO:0000269|PubMed:10734137}. SUBUNIT: Identified in the spliceosome C complex. Component of the coding region determinant (CRD)-mediated complex, composed of DHX9, HNRNPU, IGF2BP1, SYNCRIP and YBX1. Identified in a mRNP complex, at least composed of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1. Identified in a mRNP granule complex, at least composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8, RPS9, SYNCRIP, TROVE2, YBX1 and untranslated mRNAs. Interacts with GTPBP1 (By similarity). Isoform 1 is a component of the APOB mRNA editosome complex. Isoform 1 interacts with APOBEC1 and A1CF. Part of a complex associated with the FOS mCRD domain and consisting of PABPC1, PAIP1, CSDE1/UNR, HNRPD and SYNCRIP. Isoform 2 interacts with HNRPR. Interacts with POLR2A hyperphosphorylated C-terminal domain. Interacts with HABP4 (By similarity). Identified in a histone pre-mRNA complex, at least composed of ERI1, LSM11, SLBP, SNRPB, SYNCRIP and YBX1. Isoform 1 and isoform 2 interact with SMN. Isoform 2 interacts through its C-terminal domain with SYT7, SYT8 and SYT9. The non-phosphorylated and phosphorylated forms are colocalized with PAIP1 in polysomes. {ECO:0000250|UniProtKB:O60506, ECO:0000269|PubMed:10734137, ECO:0000269|PubMed:11773003, ECO:0000269|PubMed:19470752}. DOMAIN: The domain containing eight Arg-Gly-Gly repeats (RGG/RXR-box) may be involved in RNA-binding and protein-protein interactions. It is methylated by PRMT1, and essential for nuclear localization (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. Detected in heart, brain, spleen, lung, liver, skeletal muscle, adipocytes, kidney and testis. {ECO:0000269|PubMed:10734137, ECO:0000269|PubMed:11773003, ECO:0000269|PubMed:9847309}. +O35047 HOP2_MOUSE Homologous-pairing protein 2 homolog (PSMC3-interacting protein) (Proteasome 26S ATPase subunit 3-interacting protein) (Tat-binding protein 1-interacting protein) (TBP-1-interacting protein) 217 24,748 Beta strand (2); Chain (1); Coiled coil (1); Helix (3); Mutagenesis (1); Region (1); Sequence conflict (1); Turn (1) FUNCTION: Plays an important role in meiotic recombination. Stimulates DMC1-mediated strand exchange required for pairing homologous chromosomes during meiosis. The complex PSMC3IP/MND1 binds DNA, stimulates the recombinase activity of DMC1 as well as DMC1 D-loop formation from double-strand DNA. This complex stabilizes presynaptic RAD51 and DMC1 filaments formed on single strand DNA to capture double-strand DNA. This complex stimulates both synaptic and presynaptic critical steps in RAD51 and DMC1-promoted homologous pairing. May inhibit HIV-1 viral protein TAT activity and modulate the activity of proteasomes through association with PSMC3. {ECO:0000269|PubMed:15192114, ECO:0000269|PubMed:16675459, ECO:0000269|PubMed:17426123, ECO:0000269|PubMed:17639080, ECO:0000269|PubMed:17639081, ECO:0000269|PubMed:9345291}. PTM: Phosphorylated by PKA, PKC and MAPK. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11739747}. SUBUNIT: Interacts with the DNA-binding domain of the nuclear receptors NR3C1/GR, ESR2/ER-beta, THRB and RXRA (By similarity). Forms a stable heterodimer with MND1. Interacts with PSMC3/TBP1. {ECO:0000250, ECO:0000269|PubMed:16675459, ECO:0000269|PubMed:9345291}. TISSUE SPECIFICITY: Highly expressed in testis and more specifically in spermatocytes. Detected in spleen, ovary and thymus. {ECO:0000269|PubMed:11739747, ECO:0000269|PubMed:9345291}. +Q8R1H0 HOP_MOUSE Homeodomain-only protein (Homeobox-only protein) (Odd homeobox protein 1) (mOB1) 73 8,282 Beta strand (1); Chain (1); DNA binding (1); Helix (3); Mutagenesis (2); Sequence conflict (2) FUNCTION: Atypical homeodomain protein which does not bind DNA and is required to modulate cardiac growth and development. Acts via its interaction with SRF, thereby modulating the expression of SRF-dependent cardiac-specific genes and cardiac development. Prevents SRF-dependent transcription either by inhibiting SRF binding to DNA or by recruiting histone deacetylase (HDAC) proteins that prevent transcription by SRF. Overexpression causes cardiac hypertrophy (PubMed:12297045, PubMed:12297046). Acts as a co-chaperone for HSPA1A and HSPA1B chaperone proteins and assists in chaperone-mediated protein refolding (By similarity). {ECO:0000250|UniProtKB:Q9BPY8, ECO:0000269|PubMed:12297045, ECO:0000269|PubMed:12297046}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12297045}. Cytoplasm {ECO:0000269|PubMed:14516659}. Note=According to PubMed:14516659 it is cytoplasmic. {ECO:0000269|PubMed:14516659}. SUBUNIT: Interacts with serum response factor (SRF) (PubMed:12297045, PubMed:12297046). Component of a large complex containing histone deacetylases such as HDAC2 (PubMed:12975471). Interacts with the acetylated forms of HSPA1A and HSPA1B. Interacts with HSPA8 (By similarity). {ECO:0000250|UniProtKB:Q9BPY8, ECO:0000269|PubMed:12297045, ECO:0000269|PubMed:12297046, ECO:0000269|PubMed:12975471}. TISSUE SPECIFICITY: Expressed in the embryonic and adult heart and in the adult brain, liver, lung, skeletal muscle, intestine and spleen. Throughout embryonic and postnatal development, it is expressed in the myocardium. {ECO:0000269|PubMed:12297045, ECO:0000269|PubMed:12297046, ECO:0000269|PubMed:14516659}. +P01803 HVM34_MOUSE Ig heavy chain V region AMPC1 113 12,691 Chain (1); Disulfide bond (1); Domain (1); Non-terminal residue (1) +P31311 HXA11_MOUSE Homeobox protein Hox-A11 (Homeobox protein Hox-1.9) 313 34,484 Chain (1); Compositional bias (5); DNA binding (1) FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. SUBCELLULAR LOCATION: Nucleus. +P01807 HVM37_MOUSE Ig heavy chain V region X44 119 13,246 Chain (1); Domain (1); Non-terminal residue (1) +P01821 HVM45_MOUSE Ig heavy chain V region MC101 116 12,593 Beta strand (9); Chain (1); Domain (1); Helix (1); Non-terminal residue (1); Signal peptide (1); Turn (4) +Q8R1F5 HYI_MOUSE Putative hydroxypyruvate isomerase (EC 5.3.1.22) 277 30,449 Active site (2); Chain (1); Erroneous gene model prediction (1); Sequence conflict (4) FUNCTION: Catalyzes the reversible isomerization between hydroxypyruvate and 2-hydroxy-3-oxopropanoate (also termed tartronate semialdehyde). {ECO:0000250}. +Q812F3 HYAL5_MOUSE Hyaluronidase-5 (Hyal-5) (EC 3.2.1.35) (Hyaluronoglucosaminidase-5) 526 60,808 Active site (1); Chain (1); Disulfide bond (5); Glycosylation (2); Signal peptide (1) FUNCTION: Catalyzes the hydrolysis of hyaluronan into smaller oligosaccharide fragments (PubMed:16330764, PubMed:16925524, PubMed:19605784). Does not appear to be essential for fertilization (PubMed:19605784). {ECO:0000269|PubMed:16330764, ECO:0000269|PubMed:16925524, ECO:0000269|PubMed:19605784}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16330764, ECO:0000269|PubMed:16925524}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:16330764, ECO:0000269|PubMed:16925524}. Cytoplasmic vesicle, secretory vesicle, acrosome membrane {ECO:0000269|PubMed:16330764}. Secreted {ECO:0000269|PubMed:16330764}. Note=Located on the plasma and acrosomal membranes of acrosome-intact (AI) sperm and released during the acrosome reaction. {ECO:0000269|PubMed:16330764}. TISSUE SPECIFICITY: Expressed in testis, epididymal sperm and epididymides (at protein level) (PubMed:16330764, PubMed:19605784). Expressed at highest levels in testis with lesser amounts in epididymal sperm (PubMed:16925524, PubMed:16330764, PubMed:19605784). {ECO:0000269|PubMed:16330764, ECO:0000269|PubMed:16925524, ECO:0000269|PubMed:19605784}. +Q8VCZ9 HYPDH_MOUSE Hydroxyproline dehydrogenase (HYPDH) (EC 1.5.5.3) (Kidney and liver proline oxidase 1) (MmPOX1) (Probable proline dehydrogenase 2) (EC 1.5.5.2) (Probable proline oxidase 2) (Proline oxidase-like protein) (PO) (Proline oxidase) 456 50,723 Chain (1); Erroneous initiation (2); Modified residue (2); Sequence conflict (2) FUNCTION: Dehydrogenase that converts trans-4-L-hydroxyproline to delta-1-pyrroline-3-hydroxy-5-carboxylate (Hyp) using ubiquinone-10 as the terminal electron acceptor. Can also use proline as a substrate but with a very much lower efficiency. Does not react with other diastereomers of Hyp: trans-4-D-hydroxyproline and cis-4-L-hydroxyproline. Ubiquininone analogs such as menadione, duroquinone and ubiquinone-1 react more efficiently than oxygen as the terminal electron acceptor during catalysis. {ECO:0000250|UniProtKB:Q9UF12}. +Q61727 I10R1_MOUSE Interleukin-10 receptor subunit alpha (IL-10 receptor subunit alpha) (IL-10R subunit alpha) (IL-10RA) (CDw210a) (Interleukin-10 receptor subunit 1) (IL-10R subunit 1) (IL-10R1) (CD antigen CD210) 575 64,248 Chain (1); Disulfide bond (1); Glycosylation (5); Modified residue (2); Mutagenesis (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 242 262 Helical. {ECO:0000255}. TOPO_DOM 17 241 Extracellular. {ECO:0000255}.; TOPO_DOM 263 575 Cytoplasmic. {ECO:0000255}. FUNCTION: Cell surface receptor for the cytokine IL10 that participates in IL10-mediated anti-inflammatory functions, limiting excessive tissue disruption caused by inflammation. Upon binding to IL10, induces a conformational change in IL10RB, allowing IL10RB to bind IL10 as well. In turn, the heterotetrameric assembly complex, composed of two subunits of IL10RA and IL10RB, activates the kinases JAK1 and TYK2 that are constitutively associated with IL10RA and IL10RB respectively. These kinases then phosphorylate specific tyrosine residues in the intracellular domain in IL10RA leading to the recruitment and subsequent phosphorylation of STAT3 (PubMed:8910398). Once phosphorylated, STAT3 homodimerizes, translocates to the nucleus and activates the expression of anti-inflammatory genes. In addition, IL10RA-mediated activation of STAT3 inhibits starvation-induced autophagy (By similarity). {ECO:0000250|UniProtKB:Q13651, ECO:0000269|PubMed:8910398}. PTM: Phosphorylated. Phosphorylation of the cytoplasmic tail induced STAT3 activation. {ECO:0000269|PubMed:8910398}.; PTM: Ubiquitinated by BTRC; ubiquitination leads to endocytosis and subsequent degradation of IL10RA. {ECO:0000250|UniProtKB:Q13651}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q13651}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q13651}. Cytoplasm {ECO:0000250|UniProtKB:Q13651}. SUBUNIT: Interacts with IL10. Interacts with IL10RB. Interacts (via its cytoplasmic domain) with JAK1 (via N-terminus). Interacts with BTRC; this interaction leads to IL10RA ubiquitination and subsequent degradation (By similarity). Interacts with STAT3 (PubMed:8910398). {ECO:0000250|UniProtKB:Q13651, ECO:0000269|PubMed:8910398}. +Q61190 I10R2_MOUSE Interleukin-10 receptor subunit beta (IL-10 receptor subunit beta) (IL-10R subunit beta) (IL-10RB) (Cytokine receptor class-II member 4) (Cytokine receptor family 2 member 4) (CRF2-4) (Interleukin-10 receptor subunit 2) (IL-10R subunit 2) (IL-10R2) (CD antigen CDw210b) 349 39,774 Chain (1); Disulfide bond (2); Domain (2); Glycosylation (4); Modified residue (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 221 241 Helical. {ECO:0000255}. TOPO_DOM 20 220 Extracellular. {ECO:0000255}.; TOPO_DOM 242 349 Cytoplasmic. {ECO:0000255}. FUNCTION: Shared cell surface receptor required for the activation of five class 2 cytokines: IL10, IL22, IL26, IL28, and IFNL1. The IFNLR1/IL10RB dimer is a receptor for the cytokine ligands IFNL2 and IFNL3 and mediates their antiviral activity. The ligand/receptor complex stimulate the activation of the JAK/STAT signaling pathway leading to the expression of IFN-stimulated genes (ISG), which contribute to the antiviral state (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Heterodimer with IFNLR1. {ECO:0000250}. +Q3TY65 ICA1L_MOUSE Islet cell autoantigen 1-like protein (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 15 protein homolog) (Ica69-related protein) 431 48,160 Chain (1); Domain (1); Erroneous initiation (1); Sequence conflict (4) +P35459 LY6D_MOUSE Lymphocyte antigen 6D (Ly-6D) (Thymocyte B-cell antigen) (ThB) 127 13,396 Chain (1); Disulfide bond (5); Domain (1); Erroneous initiation (1); Lipidation (1); Propeptide (1); Signal peptide (1) FUNCTION: May act as a specification marker at earliest stage specification of lymphocytes between B- and T-cell development. Marks the earliest stage of B-cell specification. {ECO:0000269|PubMed:19833765}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. TISSUE SPECIFICITY: Lymphoid cells lacking Ly6d, called ALP (all-lymphoid progenitor), retain full lymphoid potential and early thymic seeding activity, whereas cells containing Ly6d, called BLP (B-cell-biased lymphoid progenitor), up-regulate the B-cell specifying factors Ebf1 and Pax5 and behave essentially as B-cell progenitors (at protein level). Thymocytes and B-cells. {ECO:0000269|PubMed:19833765}. +Q99KE1 MAOM_MOUSE NAD-dependent malic enzyme, mitochondrial (NAD-ME) (EC 1.1.1.38) (Malic enzyme 2) 589 65,799 Active site (2); Binding site (3); Chain (1); Metal binding (3); Modified residue (5); Nucleotide binding (1); Site (1); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. SUBUNIT: Homotetramer. {ECO:0000250}. +Q8CI17 MB213_MOUSE Protein mab-21-like 3 429 49,776 Chain (1); Sequence conflict (5) +Q8CEZ4 MB214_MOUSE Protein mab-21-like 4 (Uncharacterized protein C2orf54 homolog) 452 50,535 Chain (1); Sequence conflict (3) +C0LLJ0 IMA8_MOUSE Importin subunit alpha-8 (Karyopherin subunit alpha-7) 499 55,458 Alternative sequence (1); Chain (1); Domain (1); Repeat (8); Sequence conflict (2) FUNCTION: Functions in nuclear protein import. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20699224}. Note=In MII-stage oocytes, localizes to the spindle. SUBUNIT: Binds very efficiently to importin subunit beta-1/KPNB1 via the IBB domain. This complex dissociates in the presence of RAN-GTP (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed predominantly in ovary. Isoform 1 is the predominant form. {ECO:0000269|PubMed:20699224}. +P33896 INAR1_MOUSE Interferon alpha/beta receptor 1 (IFN-R-1) (IFN-alpha/beta receptor 1) (Type I interferon receptor 1) 590 65,796 Beta strand (26); Chain (1); Cross-link (1); Disulfide bond (4); Domain (4); Glycosylation (8); Helix (2); Modified residue (1); Mutagenesis (1); Region (1); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (2) TRANSMEM 430 449 Helical. {ECO:0000255}. TOPO_DOM 27 429 Extracellular. {ECO:0000255}.; TOPO_DOM 450 590 Cytoplasmic. {ECO:0000255}. FUNCTION: Component of the receptor for type I interferons, including interferons alpha, IFNB1 and IFNW1 (PubMed:1533935, PubMed:14532120, PubMed:23872679). Functions in general as heterodimer with IFNAR2 (By similarity). Type I interferon binding activates the JAK-STAT signaling cascade, and triggers tyrosine phosphorylation of a number of proteins including JAKs, TYK2, STAT proteins and the IFNR alpha- and beta-subunits themselves (PubMed:14532120). Can form an active IFNB1 receptor by itself and activate a signaling cascade that does not involve activation of the JAK-STAT pathway (PubMed:23872679). Contributes to modulate the innate immune response to bacterial lipopolysaccharide (PubMed:23872679). {ECO:0000250|UniProtKB:P17181, ECO:0000269|PubMed:14532120, ECO:0000269|PubMed:1533935, ECO:0000269|PubMed:23872679, ECO:0000269|PubMed:24075985}. PTM: Ubiquitinated (PubMed:14532120). This leads to its internalization and lysosomal degradation. The 'Lys-63'-linked ubiquitin chains are cleaved off by the BRISC complex; this prevents receptor internalization and degradation. Probable ubiquitination sites have been identified in human, but are poorly conserved across species. {ECO:0000250|UniProtKB:P17181, ECO:0000269|PubMed:14532120}.; PTM: Phosphorylated on serine residues in response to interferon binding; this promotes interaction with FBXW11 and ubiquitination (PubMed:14532120). Phosphorylated on tyrosine residues by TYK2 tyrosine kinase. Phosphorylated on tyrosine residues in response to interferon (By similarity). {ECO:0000250|UniProtKB:P17181, ECO:0000269|PubMed:14532120}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14532120, ECO:0000269|PubMed:1533935, ECO:0000269|PubMed:24075985}; Single-pass type I membrane protein {ECO:0000305}. Late endosome {ECO:0000305|PubMed:14532120}. Lysosome {ECO:0000305|PubMed:14532120}. Note=Interferon binding triggers internalization of the receptor from the cell membrane into endosomes and then into lysosomes. {ECO:0000305|PubMed:14532120, ECO:0000305|PubMed:24075985}. SUBUNIT: Heterodimer with IFNAR2. Interacts (serine-phosphorylated form) with FBXW11, the substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex (PubMed:14532120). Interacts with SHMT2; this promotes interaction with ABRAXAS2 and the BRISC complex (By similarity). Interacts with TYK2 (By similarity). {ECO:0000250|UniProtKB:P17181, ECO:0000269|PubMed:14532120, ECO:0000305}. +Q0GNC1 INF2_MOUSE Inverted formin-2 1273 138,560 Alternative sequence (1); Chain (1); Coiled coil (1); Compositional bias (1); Domain (4); Erroneous initiation (2); Initiator methionine (1); Modified residue (9); Mutagenesis (3); Sequence conflict (4) FUNCTION: Severs actin filaments and accelerates their polymerization and depolymerization. {ECO:0000269|PubMed:16818491}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}. SUBUNIT: Interacts with profilin and actin at the FH1 and FH2 domains respectively. {ECO:0000269|PubMed:16818491}. DOMAIN: The WH2 domain acts as the DAD (diaphanous autoregulatory) domain and binds to actin monomers. {ECO:0000269|PubMed:16818491}.; DOMAIN: Regulated by autoinhibition due to intramolecular GBD-DAD binding. {ECO:0000269|PubMed:16818491}.; DOMAIN: The severing activity is dependent on covalent attachment of the FH2 domain to the C-terminus. {ECO:0000269|PubMed:16818491}. +Q99PT3 IN80B_MOUSE INO80 complex subunit B (High mobility group AT-hook 1-like 4) (PAP-1-associated protein 1) (PAPA-1) (Zinc finger HIT domain-containing protein 4) 375 40,565 Chain (1); Coiled coil (1); Compositional bias (2); Erroneous initiation (2); Frameshift (1); Modified residue (5); Zinc finger (1) FUNCTION: Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. {ECO:0000250, ECO:0000269|PubMed:15556297}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9C086}. Nucleus, nucleolus {ECO:0000269|PubMed:15556297}. SUBUNIT: Component of the chromatin remodeling INO80 complex; specifically part of a complex module associated with the helicase ATP-binding and the helicase C-terminal domain of INO80 (By similarity). Interacts with RP9. {ECO:0000250, ECO:0000269|PubMed:15556297}. TISSUE SPECIFICITY: Expressed strongly in the testis and moderately in the kidney, skeletal muscle, liver and lung. {ECO:0000269|PubMed:15556297}. +P21812 MCPT4_MOUSE Mast cell protease 4 (mMCP-4) (EC 3.4.21.-) (MSMCP) (Myonase) (Serosal mast cell protease) 246 27,204 Active site (3); Chain (1); Disulfide bond (3); Domain (1); Erroneous initiation (1); Mass spectrometry (1); Natural variant (3); Propeptide (1); Signal peptide (1) FUNCTION: Has chymotrypsin-like activity. Hydrolyzes the amide bonds of synthetic substrates having Tyr and Phe residues at the P1 position. Preferentially hydrolyzes the 'Tyr-4-|-Ile-5' bond of angiotensin I and the 'Phe-20-|-Ala-21' bond of amyloid beta-protein, and is less active towards the 'Phe-8-|-His-9' bond of angiotensin I and the 'Phe-4-|-Ala-5' and 'Tyr-10-|-Glu-11' bonds of amyloid beta-protein. Involved in thrombin regulation and fibronectin processing. {ECO:0000269|PubMed:12900518, ECO:0000269|PubMed:9538257}. SUBUNIT: Monomer. {ECO:0000269|PubMed:9538257}. TISSUE SPECIFICITY: Submucosal mast cells. In femoral muscle, detected in myocytes but not in mast cells. {ECO:0000269|PubMed:9538257}. +P15261 INGR1_MOUSE Interferon gamma receptor 1 (IFN-gamma receptor 1) (IFN-gamma-R1) (Interferon gamma receptor alpha-chain) (IFN-gamma-R-alpha) (CD antigen CD119) 477 52,343 Chain (1); Disulfide bond (4); Erroneous initiation (1); Glycosylation (2); Modified residue (7); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 255 275 Helical. {ECO:0000255}. TOPO_DOM 26 254 Extracellular. {ECO:0000255}.; TOPO_DOM 276 477 Cytoplasmic. {ECO:0000255}. FUNCTION: Associates with IFNGR2 to form a receptor for the cytokine interferon gamma (IFNG) (PubMed:2530582, PubMed:2532365, PubMed:2137461, PubMed:2531896, PubMed:2530216). Ligand binding stimulates activation of the JAK/STAT signaling pathway (By similarity). {ECO:0000250|UniProtKB:P15260, ECO:0000269|PubMed:2137461, ECO:0000269|PubMed:2530216, ECO:0000269|PubMed:2530582, ECO:0000269|PubMed:2531896, ECO:0000269|PubMed:2532365}. PTM: Phosphorylated at Ser/Thr residues. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2137461, ECO:0000269|PubMed:2530216, ECO:0000269|PubMed:2530582, ECO:0000269|PubMed:2531896, ECO:0000269|PubMed:2532365}; Single-pass type I membrane protein {ECO:0000255}. SUBUNIT: Monomer. Heterodimer with IFNGR2, to form the IFNG receptor complex. Interacts with JAK1. {ECO:0000250|UniProtKB:P15260}. +B2RY83 HPSE2_MOUSE Inactive heparanase-2 (Hpa2) 592 66,685 Chain (1); Glycosylation (2); Signal peptide (1) FUNCTION: Binds heparin and heparan sulfate with high affinity, but lacks heparanase activity. Inhibits HPSE, possibly by competing for its substrates (in vitro) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. SUBUNIT: Interacts with HPSE. Interacts with SDC1 (via glycan chains) (By similarity). {ECO:0000250}. +Q8BGC0 HTSF1_MOUSE HIV Tat-specific factor 1 homolog 757 86,240 Alternative sequence (2); Chain (1); Compositional bias (2); Cross-link (1); Domain (2); Erroneous initiation (2); Initiator methionine (1); Modified residue (21); Region (1) FUNCTION: Functions as a general transcription factor playing a role in the process of transcriptional elongation. May mediate the reciprocal stimulatory effect of splicing on transcriptional elongation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of a complex which is at least composed of HTATSF1/Tat-SF1, the P-TEFb complex components CDK9 and CCNT1, RNA polymerase II, SUPT5H, and NCL/nucleolin. Interacts with GTF2F2/RAP30 and POLR2A. Interacts with SF3A2/SAP62 and the spliceosomal U small nuclear ribonucleoproteins (snRNPs) (By similarity). Interacts with TCERG1/CA150. {ECO:0000250, ECO:0000269|PubMed:15485897}. DOMAIN: The RRM domains mediate interaction with U snRNPs. {ECO:0000250}. +O88866 HUNK_MOUSE Hormonally up-regulated neu tumor-associated kinase (EC 2.7.11.1) (Serine/threonine-protein kinase MAK-V) 714 79,603 Active site (1); Binding site (1); Chain (1); Domain (1); Nucleotide binding (1); Sequence conflict (1) +Q9D2U5 LSMD1_MOUSE N-alpha-acetyltransferase 38, NatC auxiliary subunit (LSM domain-containing protein 1) 125 13,430 Alternative sequence (1); Chain (1); Compositional bias (1); Initiator methionine (1); Modified residue (4) FUNCTION: Auxillary component of the N-terminal acetyltransferase C (NatC) complex which catalyzes acetylation of N-terminal methionine residues. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Component of the N-terminal acetyltransferase C (NatC) complex, which is composed of NAA35, NAA38 and NAA30. {ECO:0000250}. +Q9DBA8 HUTI_MOUSE Probable imidazolonepropionase (EC 3.5.2.7) (Amidohydrolase domain-containing protein 1) 426 46,489 Binding site (5); Chain (1); Metal binding (4) Amino-acid degradation; L-histidine degradation into L-glutamate; N-formimidoyl-L-glutamate from L-histidine: step 3/3. +P01745 HVM01_MOUSE Ig heavy chain V region MPC 11 121 13,135 Chain (1); Domain (1); Non-terminal residue (1) +P01747 HVM03_MOUSE Ig heavy chain V region 36-65 120 13,307 Beta strand (11); Chain (1); Domain (1); Helix (2); Non-terminal residue (1); Turn (3) +P01748 HVM04_MOUSE Ig heavy chain V region 23 117 12,772 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (5); Signal peptide (1) +P01749 HVM05_MOUSE Ig heavy chain V region 3 117 13,016 Beta strand (8); Chain (1); Disulfide bond (1); Helix (3); Non-terminal residue (1); Region (5); Signal peptide (1); Turn (4) +P01753 HVM09_MOUSE Ig heavy chain V region 186-1 117 12,890 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (5); Signal peptide (1) +P01754 HVM10_MOUSE Ig heavy chain V region 1-62-3 (Ig heavy chain V region 145) 117 12,921 Chain (1); Non-terminal residue (1); Region (5); Signal peptide (1) +Q01822 HXD1_MOUSE Homeobox protein Hox-D1 (Homeobox protein Hox-4.9) 328 34,180 Chain (1); DNA binding (1); Motif (1); Sequence conflict (3) FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Acts on the anterior body structures. SUBCELLULAR LOCATION: Nucleus. +Q8BH06 I17RE_MOUSE Interleukin-17 receptor E (IL-17 receptor E) (IL-17RE) 637 70,833 Alternative sequence (4); Chain (1); Domain (1); Frameshift (1); Glycosylation (2); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 415 435 Helical. {ECO:0000255}. TOPO_DOM 24 414 Extracellular. {ECO:0000255}.; TOPO_DOM 436 637 Cytoplasmic. {ECO:0000255}. FUNCTION: Specific functional receptor for IL17C, signaling through the NF-kappa-B and MAPK pathways. Requires TRAF3IP2 /ACT1 for signaling. Crucial regulator in innate immunity to bacterial pathogens, such as Citrobacter rodentium. Isoform 4 and isoform 5 may be either cytoplasmic inactive or dominant active forms. Isoform 2 and isoform 3 may act as soluble decoy receptors. {ECO:0000269|PubMed:16310341, ECO:0000269|PubMed:21982598, ECO:0000269|PubMed:21993849}. SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Isoform 2: Secreted {ECO:0000305}.; SUBCELLULAR LOCATION: Isoform 3: Secreted {ECO:0000305}.; SUBCELLULAR LOCATION: Isoform 4: Cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: Isoform 5: Cytoplasm {ECO:0000305}. SUBUNIT: Forms heterodimers with IL17RA; the heterodimer binds IL17C. TISSUE SPECIFICITY: Predominantly expressed in mucosal tissues, including trachea, lung, kidney and stomach. Highly expressed in colon epithelial cells. Also expressed in testis. Low expression, if any, in heart, liver, spleen, or brain. Among CD4 T-helper cells, expressed at high levels in Th17 cells. {ECO:0000269|PubMed:16310341, ECO:0000269|PubMed:21982598, ECO:0000269|PubMed:21993848, ECO:0000269|PubMed:21993849}. +P50207 HXC13_MOUSE Homeobox protein Hox-C13 328 35,193 Chain (1); Compositional bias (1); DNA binding (1) FUNCTION: Transcription factor which plays a role in hair follicle differentiation. Regulates FOXQ1 expression and that of other hair-specific genes. {ECO:0000269|PubMed:11290294, ECO:0000269|PubMed:16835220}. SUBCELLULAR LOCATION: Nucleus. TISSUE SPECIFICITY: Expressed in differentiating keratinocytes. In the hair follicle lower matrix, expressed in all 3 hair shaft-forming compartments, i.e. cuticle, cortex and medulla. Expression stops sharply at the boundary with the germinal matrix compartment. {ECO:0000269|PubMed:11290294, ECO:0000269|PubMed:16835220}. +Q3U2S8 HVCN1_MOUSE Voltage-gated hydrogen channel 1 (Hydrogen voltage-gated channel 1) (HV1) (Voltage sensor domain-only protein) (mVSOP) 269 31,242 Chain (1); Coiled coil (1); Compositional bias (2); Helix (5); Mutagenesis (5); Sequence conflict (1); Topological domain (5); Transmembrane (4) TRANSMEM 97 117 Helical; Name=Segment S1.; TRANSMEM 135 157 Helical; Name=Segment S2.; TRANSMEM 166 186 Helical; Name=Segment S3.; TRANSMEM 194 214 Helical; Name=Segment S4. TOPO_DOM 1 96 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 118 134 Extracellular. {ECO:0000255}.; TOPO_DOM 158 165 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 187 193 Extracellular. {ECO:0000255}.; TOPO_DOM 215 269 Cytoplasmic. {ECO:0000255}. FUNCTION: Mediates the voltage-dependent proton permeability of excitable membranes. Forms a proton-selective channel through which protons may pass in accordance with their electrochemical gradient. Proton efflux, accompanied by membrane depolarization, facilitates acute production of reactive oxygen species in phagocytosis. {ECO:0000269|PubMed:16556803, ECO:0000269|PubMed:19805063, ECO:0000269|PubMed:22569364, ECO:0000269|PubMed:23165764, ECO:0000269|PubMed:24584463}. PTM: Phosphorylation may enhance channel gating. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. SUBUNIT: Homodimer. {ECO:0000269|PubMed:22569364, ECO:0000269|PubMed:23165764, ECO:0000269|PubMed:24584463}. DOMAIN: The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position. Unlike other voltage-gated ion channels it lacks the pore domain. {ECO:0000269|PubMed:16556803}.; DOMAIN: The C-terminal coiled coil region mediates homodimerization and cooperative channel gating. It is essential for normal subcellular localization. {ECO:0000269|PubMed:16556803}. TISSUE SPECIFICITY: Enriched in immune tissues, such as bone marrow, macrophages and spleen. {ECO:0000269|PubMed:16556803}. +Q3U1G5 I20L2_MOUSE Interferon-stimulated 20 kDa exonuclease-like 2 (EC 3.1.-.-) 368 41,020 Chain (1); Domain (1); Sequence caution (1); Sequence conflict (4) FUNCTION: 3'-> 5'-exoribonuclease involved in ribosome biogenesis in the processing of the 12S pre-rRNA. Displays a strong specificity for a 3'-end containing a free hydroxyl group. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. +E9Q1P8 I2BP2_MOUSE Interferon regulatory factor 2-binding protein 2 (IRF-2-binding protein 2) (IRF-2BP2) 570 59,292 Chain (1); Compositional bias (2); Cross-link (5); Initiator methionine (1); Modified residue (12); Zinc finger (1) FUNCTION: Acts as a transcriptional corepressor in a IRF2-dependent manner, this repression is not mediated by histone deacetylase activities. Represses the NFAT1-dependent transactivation of NFAT-responsive promoters. Acts as a coactivator of VEGFA expression in cardiac and skeletal muscles. Plays a role in immature B-cell differentiation (By similarity). {ECO:0000250|UniProtKB:Q7Z5L9}. PTM: Phosphorylation at Ser-343 is required for nuclear targeting. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Interacts with IRF2. Part of a corepressor complex containing IRF2 and IRF2BP1. Interacts with VGLL4 (By similarity). {ECO:0000250}. DOMAIN: The C-terminal RING-type zinc finger domain is sufficient for interaction with IRF2. {ECO:0000250}. +Q9WU67 LY6I_MOUSE Lymphocyte antigen 6I (Ly-6I) (Lymphocyte antigen 6M) (Ly-6M) 134 14,714 Chain (1); Disulfide bond (5); Domain (1); Glycosylation (1); Lipidation (1); Natural variant (2); Propeptide (1); Signal peptide (1) SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. TISSUE SPECIFICITY: Expressed in hematopoietic tissue (spleen, thymus, bone marrow). Also found in peritoneal macrophages, peripheral blood leukocytes, liver, heart, brain, kidney and lung. +Q9ERM2 ICAM4_MOUSE Intercellular adhesion molecule 4 (ICAM-4) (CD antigen CD242) 262 28,495 Alternative sequence (1); Chain (1); Disulfide bond (4); Domain (2); Glycosylation (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 232 252 Helical. {ECO:0000255}. TOPO_DOM 23 231 Extracellular. {ECO:0000255}.; TOPO_DOM 253 262 Cytoplasmic. {ECO:0000255}. FUNCTION: Adhesion molecule that binds to leukocyte adhesion LFA-1 protein LFA-1 (integrin alpha-L/beta-2). ICAM4 is also a ligand for alpha-4/beta-1 and alpha-V integrins (By similarity). Isoform 2 may modulate binding of membrane-associated ICAM4. {ECO:0000250, ECO:0000269|PubMed:12406883}. SUBCELLULAR LOCATION: Isoform 1: Cell membrane {ECO:0000269|PubMed:12406883}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: Isoform 2: Secreted {ECO:0000269|PubMed:12406883}. +Q60625 ICAM5_MOUSE Intercellular adhesion molecule 5 (ICAM-5) (Telencephalin) 917 96,946 Chain (1); Disulfide bond (10); Domain (9); Glycosylation (14); Modified residue (1); Mutagenesis (1); Sequence conflict (6); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 834 854 Helical. {ECO:0000255}. TOPO_DOM 32 833 Extracellular. {ECO:0000255}.; TOPO_DOM 855 917 Cytoplasmic. {ECO:0000255}. FUNCTION: ICAM proteins are ligands for the leukocyte adhesion protein LFA-1 (integrin alpha-L/beta-2). {ECO:0000269|PubMed:7794412}. PTM: Glycosylation at Asn-54 is critical for functional folding. {ECO:0000269|PubMed:22187327}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:7794412}; Single-pass type I membrane protein {ECO:0000269|PubMed:7794412}. TISSUE SPECIFICITY: Expressed on neurons in the most rostral segment of the mammalian brain, the telencephalon. {ECO:0000269|PubMed:7794412}. +Q01965 LY9_MOUSE T-lymphocyte surface antigen Ly-9 (Cell surface molecule Ly-9) (Lymphocyte antigen 9) (SLAM family member 3) (SLAMF3) (Signaling lymphocytic activation molecule 3) (CD antigen CD229) 654 73,143 Chain (1); Disulfide bond (4); Domain (4); Glycosylation (8); Modified residue (2); Motif (2); Natural variant (11); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 454 474 Helical. {ECO:0000255}. TOPO_DOM 48 453 Extracellular. {ECO:0000255}.; TOPO_DOM 475 654 Cytoplasmic. {ECO:0000255}. FUNCTION: Self-ligand receptor of the signaling lymphocytic activation molecule (SLAM) family. SLAM receptors triggered by homo- or heterotypic cell-cell interactions are modulating the activation and differentiation of a wide variety of immune cells and thus are involved in the regulation and interconnection of both innate and adaptive immune response. Activities are controlled by presence or absence of small cytoplasmic adapter proteins, SH2D1A/SAP and/or SH2D1B/EAT-2 (PubMed:19648922). May participate in adhesion reactions between T lymphocytes and accessory cells by homophilic interaction. Promotes T-cell differentiation into a helper T-cell Th17 phenotype leading to increased IL-17 secretion; the costimulatory activity requires SH2D1A. Promotes recruitment of RORC to the IL-17 promoter (By similarity). May be involved in the maintenance of peripheral cell tolerance by serving as a negative regulator of the immune response. May disable autoantibody responses and inhibit IFN-gamma secretion by CD4(+) T-cells (PubMed:23914190). May negatively regulate the size of thymic innate CD8(+) T-cells and the development of invariant natural killer T (iNKT) cells (PubMed:23225888). Can promote natural killer (NK) cell activation (PubMed:19648922). {ECO:0000250|UniProtKB:Q9HBG7, ECO:0000269|PubMed:19648922, ECO:0000269|PubMed:23225888, ECO:0000269|PubMed:23914190}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. Cell membrane {ECO:0000305}. SUBUNIT: Interacts with SH2D1A and INPP5D. Interacts (via phosphorylated cytoplasmic domain) with PTPN11; the interaction is blocked by SH2D1A. {ECO:0000250|UniProtKB:Q9HBG7}. DOMAIN: The ITSMs (immunoreceptor tyrosine-based switch motifs) with the consensus sequence T-X-Y-X-X-[VI] present in SLAM family receptors have overlapping specificity for activating and inhibitory SH2 domain-containing binding partners. Especially they mediate the interaction with the SH2 domain of SH2D1A and SH2D1B. A 'three-pronged' mechanism is proposed involving threonine (position -2), phosphorylated tyrosine (position 0) and valine/isoleucine (position +3). {ECO:0000250|UniProtKB:Q13291}. TISSUE SPECIFICITY: Lymphocytes. +Q8R035 ICT1_MOUSE Peptidyl-tRNA hydrolase ICT1, mitochondrial (EC 3.1.1.29) (39S ribosomal protein L58, mitochondrial) (MRP-L58) (Immature colon carcinoma transcript 1 protein homolog) 206 23,477 Alternative sequence (1); Beta strand (4); Chain (1); Helix (3); Transit peptide (1); Turn (2) FUNCTION: Essential peptidyl-tRNA hydrolase component of the mitochondrial large ribosomal subunit (PubMed:20869366). Acts as a codon-independent translation release factor that has lost all stop codon specificity and directs the termination of translation in mitochondrion, possibly in case of abortive elongation. May be involved in the hydrolysis of peptidyl-tRNAs that have been prematurely terminated and thus in the recycling of stalled mitochondrial ribosomes (By similarity). {ECO:0000250|UniProtKB:Q14197, ECO:0000269|PubMed:20869366}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q14197}. SUBUNIT: Component of the mitochondrial ribosome large subunit (39S) which comprises a 16S rRNA and about 50 distinct proteins. {ECO:0000250|UniProtKB:Q14197}. +P20067 ID1_MOUSE DNA-binding protein inhibitor ID-1 (Inhibitor of DNA binding 1) (Inhibitor of differentiation 1) 168 17,914 Alternative sequence (1); Chain (1); Domain (1); Erroneous initiation (1); Motif (1); Region (1); Sequence conflict (1) FUNCTION: Transcriptional regulator (lacking a basic DNA binding domain) which negatively regulates the basic helix-loop-helix (bHLH) transcription factors by forming heterodimers and inhibiting their DNA binding and transcriptional activity. Implicated in regulating a variety of cellular processes, including cellular growth, senescence, differentiation, apoptosis, angiogenesis, and neoplastic transformation. Inhibits skeletal muscle and cardiac myocyte differentiation. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer. {ECO:0000269|PubMed:16556596, ECO:0000269|PubMed:19217292}. PTM: Polyubiquitinated; which is favored by Ifi204 and leads to proteasomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16516211}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:16516211}. SUBUNIT: Heterodimer with other HLH proteins. Interacts with CLOCK and ARNTL/BMAL1 (By similarity). Interacts with COPS5, IFI204, GATA4 and NKX2-5. {ECO:0000250, ECO:0000269|PubMed:11940648, ECO:0000269|PubMed:15451666, ECO:0000269|PubMed:16556596}. +Q61647 HYAS1_MOUSE Hyaluronan synthase 1 (EC 2.4.1.212) (Hyaluronate synthase 1) (Hyaluronic acid synthase 1) (HA synthase 1) 583 65,545 Chain (1); Compositional bias (2); Glycosylation (1); Mutagenesis (10); Topological domain (8); Transmembrane (7) TRANSMEM 25 45 Helical; Name=1. {ECO:0000255}.; TRANSMEM 52 72 Helical; Name=2. {ECO:0000255}.; TRANSMEM 405 425 Helical; Name=3. {ECO:0000255}.; TRANSMEM 436 456 Helical; Name=4. {ECO:0000255}.; TRANSMEM 463 483 Helical; Name=5. {ECO:0000255}.; TRANSMEM 502 522 Helical; Name=6. {ECO:0000255}.; TRANSMEM 546 566 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 24 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 46 51 Extracellular. {ECO:0000255}.; TOPO_DOM 73 404 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 426 435 Extracellular. {ECO:0000255}.; TOPO_DOM 457 462 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 484 501 Extracellular. {ECO:0000255}.; TOPO_DOM 523 545 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 567 583 Extracellular. {ECO:0000255}. Glycan biosynthesis; hyaluronan biosynthesis. FUNCTION: Catalyzes the addition of GlcNAc or GlcUA monosaccharides to the nascent hyaluronan polymer. Therefore, it is essential to hyaluronan synthesis a major component of most extracellular matrices that has a structural role in tissues architectures and regulates cell adhesion, migration and differentiation. This is one of the isozymes catalyzing that reaction. Also able to catalyze the synthesis of chito-oligosaccharide depending on the substrate. {ECO:0000269|PubMed:10455188}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +P01802 HVM33_MOUSE Ig heavy chain V-III region W3082 115 12,887 Chain (1); Disulfide bond (1); Domain (1); Non-terminal residue (1) +P06328 HVM49_MOUSE Ig heavy chain V region 1-72 (Ig heavy chain V region VH558 B4) 117 12,877 Chain (1); Disulfide bond (1); Non-terminal residue (1); Region (5); Sequence conflict (3); Signal peptide (1) +P01725 LV1C_MOUSE Ig lambda-1 chain V region S178 110 11,654 Chain (1); Domain (1); Non-terminal residue (1) +P48794 HYALP_MOUSE Hyaluronidase PH-20 (Hyal-PH20) (EC 3.2.1.35) (Hyaluronoglucosaminidase PH-20) (Sperm adhesion molecule 1) (Sperm surface protein PH-20) 512 58,498 Active site (1); Chain (1); Disulfide bond (5); Glycosylation (4); Propeptide (1); Sequence conflict (4); Signal peptide (1) FUNCTION: Involved in sperm-egg adhesion. Upon fertilization sperm must first penetrate a layer of cumulus cells that surrounds the egg before reaching the zona pellucida. The cumulus cells are embedded in a matrix containing hyaluronic acid which is formed prior to ovulation. This protein aids in penetrating the layer of cumulus cells by digesting hyaluronic acid. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. +Q9CR41 HYPK_MOUSE Huntingtin-interacting protein K (Huntingtin yeast partner K) 129 14,679 Alternative sequence (1); Chain (1); Coiled coil (1); Erroneous initiation (1); Modified residue (1) FUNCTION: Has a chaperone-like activity preventing polyglutamine (polyQ) aggregation of HTT. Protects against HTT polyQ-mediated apoptosis in neuronal cells. Required for optimal NAA10-NAA15 complex-mediated N-terminal acetylation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with HTT (via N-terminus). Associates with the NAA10-NAA15 complex and with the ribosome. Interacts with NAA15 (By similarity). {ECO:0000250}. +O09030 I13R1_MOUSE Interleukin-13 receptor subunit alpha-1 (IL-13 receptor subunit alpha-1) (IL-13R subunit alpha-1) (IL-13R-alpha-1) (IL-13RA1) (Interleukin-13-binding protein) (Novel cytokine receptor 4) (NR4) (CD antigen CD213a1) 424 48,402 Chain (1); Disulfide bond (3); Domain (2); Glycosylation (6); Motif (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 341 364 Helical. {ECO:0000255}. TOPO_DOM 26 340 Extracellular. {ECO:0000255}.; TOPO_DOM 365 424 Cytoplasmic. {ECO:0000255}. FUNCTION: Binds with low affinity to interleukin-13 (IL13). Together with IL4RA can form a functional receptor for IL13. Also serves as an alternate accessory protein to the common cytokine receptor gamma chain for interleukin-4 (IL4) signaling, but cannot replace the function of IL2RG in allowing enhanced interleukin-2 (IL2) binding activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Interleukin-13 receptor is a complex of IL4R, IL13RA1, and possibly other components. Interacts with TRAF3IP1 (By similarity). {ECO:0000250}. DOMAIN: The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.; DOMAIN: The box 1 motif is required for JAK interaction and/or activation. TISSUE SPECIFICITY: Spleen, liver, thymus, heart, lung, kidney, testis, stomach, brain, skin, and colon; but not skeletal muscle. +Q9Z1Q3 LY66D_MOUSE Lymphocyte antigen 6 complex locus protein G6d 135 14,092 Chain (1); Disulfide bond (5); Domain (1); Glycosylation (1); Lipidation (1); Propeptide (1); Signal peptide (1) PTM: O-glycosylated. {ECO:0000269|PubMed:17008713}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17008713}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:17008713}. Cell projection, filopodium {ECO:0000269|PubMed:17008713}. SUBUNIT: Homodimer. {ECO:0000269|PubMed:17008713}. TISSUE SPECIFICITY: Expressed in embryonic tissue and adult lung, kidney, brain, liver and spleen. {ECO:0000269|PubMed:12079290}. +P0CW02 LY6C1_MOUSE Lymphocyte antigen 6C1 (Ly-6C1) 131 14,193 Chain (1); Disulfide bond (5); Domain (1); Lipidation (1); Propeptide (1); Sequence conflict (5); Signal peptide (1) SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}. +P0CW03 LY6C2_MOUSE Lymphocyte antigen 6C2 (Ly-6C2) 131 14,090 Chain (1); Disulfide bond (5); Domain (1); Lipidation (1); Propeptide (1); Signal peptide (1) SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}. +P35460 LY6F_MOUSE Lymphocyte antigen 6F (Ly-6F) (Ly-6F.1) 134 14,599 Chain (1); Disulfide bond (5); Domain (1); Lipidation (1); Propeptide (1); Signal peptide (1) SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. +Q9JKV2 ICK_MOUSE Serine/threonine-protein kinase ICK (EC 2.7.11.1) (Intestinal cell kinase) (mICK) (MAK-related kinase) (MRK) 629 70,592 Active site (1); Binding site (1); Chain (1); Domain (1); Modified residue (3); Mutagenesis (10); Nucleotide binding (1); Sequence conflict (2) FUNCTION: Has an essential role in ciliogenesis, particularly in neuronal and retinal progenitor cells (PubMed:24797473). Phosphorylates KIF3A (PubMed:24797473). Involved in the control of ciliary length (PubMed:24853502). Regulates the ciliary localization of SHH pathway components as well as the localization of IFT components at ciliary tips (PubMed:24797473, PubMed:24853502). May play a role in cardiac development (By similarity). Regulates intraflagellar transport (IFT) speed and negatively regulates cilium length in a cAMP and mTORC1 signaling -dependent manner and this regulation requires its kinase activity (PubMed:25243405). {ECO:0000250|UniProtKB:Q62726, ECO:0000269|PubMed:24797473, ECO:0000269|PubMed:24853502, ECO:0000269|PubMed:25243405}. PTM: Autophosphorylated on serine and threonine residues. Phosphorylation at Thr-157 by CDK7/Cak1p increases kinase activity. {ECO:0000269|PubMed:15988018}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q62726}. Cell projection, cilium {ECO:0000269|PubMed:24797473, ECO:0000269|PubMed:25243405}. Nucleus {ECO:0000269|PubMed:15988018, ECO:0000269|PubMed:25243405}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:24853502}. Note=Also found at the ciliary tip (PubMed:24797473). Predominant nuclear localization has been observed with a N-terminally GFP-tagged construct in transfected COS-7 cells (PubMed:15988018). {ECO:0000269|PubMed:15988018, ECO:0000269|PubMed:24797473}. TISSUE SPECIFICITY: Highly expressed in colon and lung, lower levels present in heart, esophagus, stomach, small intestine and ovary. Localizes to the crypt region of large and small intestine. {ECO:0000269|PubMed:10699974}. +Q60767 LY75_MOUSE Lymphocyte antigen 75 (Ly-75) (DEC-205) (CD antigen CD205) 1723 197,352 Chain (1); Disulfide bond (13); Domain (11); Glycosylation (14); Modified residue (3); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1668 1692 Helical. {ECO:0000255}. TOPO_DOM 28 1667 Extracellular. {ECO:0000255}.; TOPO_DOM 1693 1723 Cytoplasmic. {ECO:0000255}. FUNCTION: Acts as an endocytic receptor to direct captured antigens from the extracellular space to a specialized antigen-processing compartment. Causes reduced proliferation of B lymphocytes (By similarity). {ECO:0000250}. PTM: N-glycosylated. {ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:19656770, ECO:0000269|PubMed:7553896, ECO:0000269|PubMed:7753172}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:7553896}; Single-pass type I membrane protein {ECO:0000269|PubMed:7553896}. TISSUE SPECIFICITY: Expressed in dendritic and thymic epithelial cells and lymph nodes. {ECO:0000269|PubMed:7553896, ECO:0000269|PubMed:7753172}. +Q9JHF9 LY96_MOUSE Lymphocyte antigen 96 (Ly-96) (ESOP-1) (Protein MD-2) 160 18,394 Beta strand (10); Chain (1); Disulfide bond (3); Glycosylation (3); Helix (1); Mutagenesis (1); Region (1); Signal peptide (1); Turn (1) FUNCTION: Binds bacterial lipopolysaccharide (LPS) (PubMed:22532668). Cooperates with TLR4 in the innate immune response to bacterial lipopolysaccharide (LPS), and with TLR2 in the response to cell wall components from Gram-positive and Gram-negative bacteria. Enhances TLR4-dependent activation of NF-kappa-B. Cells expressing both LY96 and TLR4, but not TLR4 alone, respond to LPS (PubMed:10725698). {ECO:0000250|UniProtKB:Q9Y6Y9, ECO:0000269|PubMed:10725698, ECO:0000269|PubMed:20133493, ECO:0000269|PubMed:24380872}. PTM: N-glycosylated. {ECO:0000269|PubMed:17803912}. SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000269|PubMed:10725698, ECO:0000269|PubMed:20133493, ECO:0000305|PubMed:24380872}. Secreted {ECO:0000269|PubMed:10891475}. Note=Retained in the extracellular space at the cell surface by interaction with TLR4. {ECO:0000269|PubMed:10725698, ECO:0000269|PubMed:20133493, ECO:0000305|PubMed:24380872}. SUBUNIT: Heterogeneous homopolymer formed from homodimers; disulfide-linked (By similarity). Belongs to the lipopolysaccharide (LPS) receptor, a multi-protein complex containing at least CD14, LY96 and TLR4 (PubMed:10725698, PubMed:20133493, PubMed:24380872). Binds to the extracellular domain of TLR4 (PubMed:10725698, PubMed:20133493, PubMed:24380872, PubMed:17803912, PubMed:22532668). Binds to the extracellular domain of TLR2 (By similarity). Ligand binding induces interaction with TLR4 and oligomerization of the complex (PubMed:20133493, PubMed:24380872, PubMed:22532668). {ECO:0000250|UniProtKB:Q9Y6Y9, ECO:0000269|PubMed:10725698, ECO:0000269|PubMed:17803912, ECO:0000269|PubMed:20133493, ECO:0000269|PubMed:22532668, ECO:0000269|PubMed:24380872}. TISSUE SPECIFICITY: Highly expressed in spleen, bone marrow, thymus, liver, kidney, ovary and decidua. Detected at lower levels in testis, small intestine and skin. {ECO:0000269|PubMed:10891475}. +P70699 LYAG_MOUSE Lysosomal alpha-glucosidase (EC 3.2.1.20) (Acid maltase) 953 106,248 Active site (2); Binding site (4); Chain (1); Disulfide bond (5); Domain (1); Glycosylation (7); Propeptide (1); Sequence conflict (13); Signal peptide (1) FUNCTION: Essential for the degradation of glycogen in lysosomes. Has highest activity on alpha-1,4-linked glycosidic linkages, but can also hydrolyze alpha-1,6-linked glucans. {ECO:0000250|UniProtKB:P10253}. SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:P10253}. Lysosome membrane {ECO:0000250|UniProtKB:P10253}. +P98154 IDD_MOUSE Integral membrane protein DGCR2/IDD (Seizure-related membrane-bound adhesion protein) 548 60,697 Chain (1); Disulfide bond (5); Domain (3); Glycosylation (2); Modified residue (1); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 348 366 Helical. {ECO:0000255}. TOPO_DOM 25 347 Extracellular. {ECO:0000255}.; TOPO_DOM 367 548 Cytoplasmic. {ECO:0000255}. FUNCTION: Probably plays a role in neural crest cell migration. May play a role in delivery of extracellular signals. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. TISSUE SPECIFICITY: Ubiquitous in various organs with low abundance. +Q9D7Q0 LYG1_MOUSE Lysozyme g-like protein 1 (EC 3.2.1.-) 197 21,870 Active site (1); Chain (1); Disulfide bond (2); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q3V1I0 LYG2_MOUSE Lysozyme g-like protein 2 (EC 3.2.1.-) 213 23,762 Active site (1); Chain (1); Disulfide bond (2); Signal peptide (1) FUNCTION: May act as a potent antibacterial protein that may play a role in the innate immunity. {ECO:0000250|UniProtKB:Q86SG7}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +P27792 LYL1_MOUSE Protein lyl-1 (Lymphoblastic leukemia-derived sequence 1) 278 30,142 Chain (1); Domain (1); Modified residue (1); Sequence conflict (11) SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}. SUBUNIT: Efficient DNA binding requires dimerization with another bHLH protein. +Q8BPC6 IDHG2_MOUSE Probable isocitrate dehydrogenase [NAD] gamma 2, mitochondrial (Isocitric dehydrogenase subunit gamma 2) (NAD(+)-specific ICDH subunit gamma 2) 396 43,850 Binding site (5); Chain (1); Metal binding (1); Transit peptide (1) FUNCTION: Regulatory subunit which plays a role in the allosteric regulation of the enzyme catalyzing the decarboxylation of isocitrate (ICT) into alpha-ketoglutarate. The heterodimer composed of the alpha (IDH3A) and beta (IDH3B) subunits and the heterodimer composed of the alpha (IDH3A) and gamma (IDH3G) subunits, have considerable basal activity but the full activity of the heterotetramer (containing two subunits of IDH3A, one of IDH3B and one of IDH3G) requires the assembly and cooperative function of both heterodimers. {ECO:0000250|UniProtKB:P51553}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:18614015}. SUBUNIT: Heterooligomer of subunits alpha (IDH3A), beta (IDH3B), and gamma (IDH3G) in the apparent ratio of 2:1:1. The heterodimer containing one IDH3A and one IDH3B subunit and the heterodimer containing one IDH3A and one IDH3G subunit assemble into a heterotetramer (which contains two subunits of IDH3A, one of IDH3B and one of IDH3G) and further into the heterooctamer. {ECO:0000250|UniProtKB:P51553}. +P17950 IER2_MOUSE Immediate early response gene 2 protein (CHX1) (Cycloheximide-induced gene protein) (Growth factor-inducible immediate early protein) (Proline-rich-induced protein 92) (Pip92) (T-lymphocyte-activated protein) 221 24,459 Chain (1); Modified residue (1); Sequence conflict (11) FUNCTION: DNA-binding protein that seems to act as a transcription factor (By similarity). Involved in the regulation of neuronal differentiation, acts upon JNK-signaling pathway activation and plays a role in neurite outgrowth in hippocampal cells (By similarity). May mediate with FIBP FGF-signaling in the establishment of laterality in the embryo (By similarity). Promotes cell motility, seems to stimulate tumor metastasis (By similarity). {ECO:0000250|UniProtKB:B7SXM5, ECO:0000250|UniProtKB:Q6P7D3, ECO:0000250|UniProtKB:Q9BTL4}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BTL4}. Nucleus {ECO:0000250|UniProtKB:Q9BTL4}. Note=Cytoplasmic during quiescence, translocates to the nucleus upon stimulation. {ECO:0000250|UniProtKB:Q9BTL4}. +Q99J55 IER5L_MOUSE Immediate early response gene 5-like protein 406 42,530 Chain (1); Compositional bias (2); Frameshift (2); Sequence conflict (2) +Q08890 IDS_MOUSE Iduronate 2-sulfatase (EC 3.1.6.13) (Alpha-L-iduronate sulfate sulfatase) 552 62,186 Active site (2); Chain (1); Frameshift (1); Glycosylation (6); Metal binding (5); Modified residue (1); Propeptide (1); Sequence conflict (3); Signal peptide (1) FUNCTION: Required for the lysosomal degradation of heparan sulfate and dermatan sulfate. {ECO:0000269|PubMed:15149955}. PTM: The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity. {ECO:0000250}. SUBCELLULAR LOCATION: Lysosome. TISSUE SPECIFICITY: Found to be expressed in alpha and beta pancreatic cells. {ECO:0000269|PubMed:15149955}. +P48441 IDUA_MOUSE Alpha-L-iduronidase (EC 3.2.1.76) 634 71,254 Active site (2); Binding site (5); Chain (1); Disulfide bond (1); Region (1); Sequence conflict (2); Signal peptide (1) PTM: N-glycosylation contributes to substrate binding and is required for full enzymatic activity. {ECO:0000250}. SUBCELLULAR LOCATION: Lysosome {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:7698753}. +P97823 LYPA1_MOUSE Acyl-protein thioesterase 1 (APT-1) (EC 3.1.2.-) (Lysophospholipase 1) (Lysophospholipase I) (LPL-I) (LysoPLA I) 230 24,688 Active site (3); Alternative sequence (1); Chain (1); Erroneous initiation (1); Modified residue (1); Mutagenesis (3); Sequence conflict (1) FUNCTION: Hydrolyzes fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS. Has depalmitoylating activity toward KCNMA1. Has low lysophospholipase activity (By similarity). {ECO:0000250, ECO:0000269|PubMed:9139730}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +Q6NWV3 IF122_MOUSE Intraflagellar transport protein 122 homolog (WD repeat-containing protein 10) 1182 134,798 Alternative sequence (1); Chain (1); Erroneous initiation (1); Repeat (8); Sequence conflict (6) FUNCTION: Required for cilia formation during neuronal patterning. Acts as a negative regulator of Shh signaling. Required to recruit TULP3 to primary cilia. {ECO:0000269|PubMed:19000668, ECO:0000269|PubMed:21209331}. SUBCELLULAR LOCATION: Cell projection, cilium. Cytoplasm, cytoskeleton, cilium basal body. Note=Localizes to photoreceptor connecting cilia. SUBUNIT: Component of the IFT complex A (IFT-A) complex. {ECO:0000250}. +Q9D7Z7 LYPD5_MOUSE Ly6/PLAUR domain-containing protein 5 256 27,450 Chain (1); Domain (1); Glycosylation (2); Lipidation (1); Propeptide (1); Signal peptide (1) SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}. +E9PY46 IF140_MOUSE Intraflagellar transport protein 140 homolog (WD and tetratricopeptide repeats protein 2) 1464 165,875 Chain (1); Modified residue (1); Natural variant (1); Repeat (15); Sequence conflict (6) FUNCTION: Component of the IFT complex A (IFT-A), a complex required for retrograde ciliary transport (By similarity). Plays a pivotal role in proper development and function of ciliated cells through its role in ciliogenesis and/or cilium maintenance (PubMed:22282595). Required for the development and maintenance of the outer segments of rod and cone photoreceptor cells. Plays a role in maintenance and the delivery of opsin to the outer segment of photoreceptor cells (PubMed:24619649). {ECO:0000250|UniProtKB:Q96RY7, ECO:0000269|PubMed:22282595, ECO:0000269|PubMed:24619649}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:22282595, ECO:0000269|PubMed:24009529, ECO:0000269|PubMed:24619649}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q96RY7}. Cell projection, cilium {ECO:0000269|PubMed:22282595, ECO:0000269|PubMed:24009529, ECO:0000269|PubMed:24619649}. SUBUNIT: Component of the IFT complex A (IFT-A). Interacts with TTC25. {ECO:0000250|UniProtKB:Q96RY7}. DISEASE: Note=Defects in Ift140 are the cause of cauliflower (cauli) phenotype, a mouse model for human asphyxiating thoracic dystrophy (Jeune syndrome). Embryos die at E13.5 and exhibit exencephaly, anophthalmia, severely disorganized ribs with extensive exostoses, vertebral and palatal defects, agenesis/hypoplasia of the craniofacial skeleton, and polydactyly of the hindlimbs. Cilia morphology in limb buds is severely disrupted with a broader and bulbous appearance. {ECO:0000269|PubMed:24009529}. +Q6VH22 IF172_MOUSE Intraflagellar transport protein 172 homolog (Protein wimple) 1749 197,548 Alternative sequence (1); Chain (1); Cross-link (1); Modified residue (2); Mutagenesis (1); Repeat (23); Sequence caution (1); Sequence conflict (3) FUNCTION: Required for the maintenance and formation of cilia. Plays an indirect role in hedgehog (Hh) signaling, cilia being required for all activity of the hedgehog pathway. {ECO:0000269|PubMed:14603322, ECO:0000269|PubMed:16061793}. SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000305}. SUBUNIT: Interacts with IFT88. Interacts with RABL2/RABL2A; binds preferentially to GDP-bound RABL2. {ECO:0000269|PubMed:11062270, ECO:0000269|PubMed:23055941}. TISSUE SPECIFICITY: Co-localizes with RABL2/RABL2A in the midpiece of elongated spermatids within the testis (at protein level). Expressed in the flagellum of elongated spermatids and sperm in the testis lumen (at protein level) (PubMed:24339785). {ECO:0000269|PubMed:23055941, ECO:0000269|PubMed:24339785}. +Q8VC49 IF27B_MOUSE Interferon alpha-inducible protein 27-like protein 2B (Interferon-stimulated gene 12 protein B2) (ISG12(b2)) 283 27,772 Chain (1); Transit peptide (1); Transmembrane (3) TRANSMEM 130 150 Helical. {ECO:0000255}.; TRANSMEM 176 196 Helical. {ECO:0000255}.; TRANSMEM 202 222 Helical. {ECO:0000255}. FUNCTION: Functions in the intrinsic apoptotic signaling pathway and may have an interferon-induced antiviral activity. {ECO:0000269|PubMed:21151029}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:21151029}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Homooligomer (PubMed:21151029). Interacts with BAK1 (PubMed:21151029). Interacts with BAX (PubMed:21151029). Interacts with adenine nucleotide translocase (PubMed:21151029). {ECO:0000269|PubMed:21151029}. +Q05D44 IF2P_MOUSE Eukaryotic translation initiation factor 5B (eIF-5B) (EC 3.6.5.3) (Translation initiation factor IF-2) 1216 137,616 Chain (1); Compositional bias (2); Domain (1); Modified residue (27); Nucleotide binding (1); Region (5); Sequence caution (4); Sequence conflict (4) FUNCTION: Plays a role in translation initiation. Translational GTPase that catalyzes the joining of the 40S and 60S subunits to form the 80S initiation complex with the initiator methionine-tRNA in the P-site base paired to the start codon. GTP binding and hydrolysis induces conformational changes in the enzyme that renders it active for productive interactions with the ribosome. The release of the enzyme after formation of the initiation complex is a prerequisite to form elongation-competent ribosomes. {ECO:0000250|UniProtKB:P39730}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12426392}. SUBUNIT: Interacts with ANXA5 in a calcium and phospholipid-dependent manner. {ECO:0000250}. +Q61012 GBG1_MOUSE Guanine nucleotide-binding protein G(T) subunit gamma-T1 (Transducin gamma chain) 74 8,528 Chain (1); Initiator methionine (1); Lipidation (1); Mass spectrometry (2); Modified residue (1); Propeptide (1) FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. SUBUNIT: G proteins are composed of 3 units, alpha, beta and gamma. TISSUE SPECIFICITY: Retinal rod outer segment. +Q8CHG3 GCC2_MOUSE GRIP and coiled-coil domain-containing protein 2 (185 kDa Golgi coiled-coil protein) (GCC185) 1679 194,445 Chain (1); Coiled coil (1); Domain (1); Erroneous initiation (1); Modified residue (3); Region (2); Sequence conflict (1) FUNCTION: Golgin which probably tethers transport vesicles to the trans-Golgi network (TGN) and regulates vesicular transport between the endosomes and the Golgi. As a RAB9A effector it is involved in recycling of the mannose 6-phosphate receptor from the late endosomes to the TGN. May also play a role in transport between the recycling endosomes and the Golgi. Required for maintenance of the Golgi structure, it is involved in the biogenesis of noncentrosomal, Golgi-associated microtubules through recruitment of CLASP1 and CLASP2 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. SUBUNIT: Homodimer. Interacts (via GRIP domain) with RAB6A (preferentially in its GTP-bound form). May interact (RAB6A-dependent) with ARL1; might be involved in GCC2 Golgi localization. Interacts (probably via GRIP domain) with RAB9A (preferentially in its GTP-bound form). Interacts with CLASP1 and CLASP2; recruits both proteins to membranes of the TGN. Interacts with STX16 (By similarity). {ECO:0000250}. DOMAIN: Extended rod-like protein with coiled-coil domains. +Q8BUV3 GEPH_MOUSE Gephyrin [Includes: Molybdopterin adenylyltransferase (MPT adenylyltransferase) (EC 2.7.7.75) (Domain G); Molybdopterin molybdenumtransferase (MPT Mo-transferase) (EC 2.10.1.1) (Domain E)] 769 83,282 Chain (1); Compositional bias (2); Modified residue (10); Region (3); Sequence conflict (2) Cofactor biosynthesis; molybdopterin biosynthesis. FUNCTION: Microtubule-associated protein involved in membrane protein-cytoskeleton interactions. It is thought to anchor the inhibitory glycine receptor (GLYR) to subsynaptic microtubules. Catalyzes two steps in the biosynthesis of the molybdenum cofactor. In the first step, molybdopterin is adenylated. Subsequently, molybdate is inserted into adenylated molybdopterin and AMP is released. {ECO:0000250|UniProtKB:Q03555}. SUBCELLULAR LOCATION: Cell junction, synapse {ECO:0000269|PubMed:27609886}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000250|UniProtKB:Q03555}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q03555}; Cytoplasmic side {ECO:0000250|UniProtKB:Q03555}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000269|PubMed:27609886}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q03555}. Cell membrane {ECO:0000250|UniProtKB:Q03555}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q03555}; Cytoplasmic side {ECO:0000250|UniProtKB:Q03555}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9NQX3}. Note=Cytoplasmic face of glycinergic postsynaptic membranes. {ECO:0000250|UniProtKB:Q03555}. SUBUNIT: Homotrimer, homodimer and homooligomer (By similarity). Interacts with SRGAP2 (via SH3 domain) (PubMed:22126966). Interacts with GLRB (By similarity). Interacts with GABARAP (By similarity). Interacts with GABRA3 (By similarity). GABRA3 and GLRB occupy overlapping binding sites (By similarity). Interacts with ARHGAP32; IQSEC3, INSYN1 and INSYN2 (PubMed:27609886). {ECO:0000250|UniProtKB:Q03555, ECO:0000250|UniProtKB:Q9NQX3, ECO:0000269|PubMed:22126966, ECO:0000269|PubMed:27609886}. +Q6P5E6 GGA2_MOUSE ADP-ribosylation factor-binding protein GGA2 (Gamma-adaptin-related protein 2) (Golgi-localized, gamma ear-containing, ARF-binding protein 2) 603 66,049 Alternative sequence (1); Chain (1); Domain (3); Erroneous initiation (2); Region (1); Sequence conflict (2) FUNCTION: Plays a role in protein sorting and trafficking between the trans-Golgi network (TGN) and endosomes. Mediates the ARF-dependent recruitment of clathrin to the TGN and binds ubiquitinated proteins and membrane cargo molecules with a cytosolic acidic cluster-dileucine (DXXLL) motif. Mediates export of the GPCR receptor ADRA2B to the cell surface. Regulates retrograde transport of phosphorylated form of BACE1 from endosomes to the trans-Golgi network. {ECO:0000250|UniProtKB:Q9UJY4}. PTM: Ubiquitinated. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q9UJY4}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9UJY4}. Endosome membrane {ECO:0000250|UniProtKB:Q9UJY4}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9UJY4}. Early endosome membrane {ECO:0000250|UniProtKB:Q9UJY4}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9UJY4}. SUBUNIT: Monomer (By similarity). Interacts with NECAP1, TSG101, UBC and AFTPH/aftiphilin. Interacts with CNST (PubMed:19864490). Interacts with GGA1 and GGA3 (By similarity). Binds to clathrin and activated ARFs, such as ARF1, ARF5 and ARF6 (PubMed:11950392). Binds RABEP1 and RABGEF1. Interacts with the type-I membrane proteins SORT1, SORL1, LRP3, M6PR/CD-MPR, IGF2R/CI-MPR and BACE1. Binds the accessory proteins CCDC91, P200, SYNRG, EPN4 and NECAP2. Interacts with ADRA2B. Interacts (via VHS domain) with PIK4B; the interaction is important for PIK4B location at the Golgi apparatus membrane (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9UJY4, ECO:0000269|PubMed:11950392, ECO:0000269|PubMed:19864490}. DOMAIN: The VHS domain functions as a recognition module for sorting signals composed of an acidic cluster followed by two leucines (DXXLL motif). {ECO:0000250|UniProtKB:Q9UJY4}.; DOMAIN: The GAT domain is responsible for interaction with ARF-GTP, UBC and RABEP1. Required for recruitment to the TGN it prevents ARF-GTP hydrolysis. {ECO:0000250|UniProtKB:Q9UJY4}.; DOMAIN: The unstructured hinge region contains clathrin-binding but no autoinhibitory (DXXLL) motifs. {ECO:0000250|UniProtKB:Q9UJY4}.; DOMAIN: The GAE domain binds accessory proteins regulating GGAs function. {ECO:0000250|UniProtKB:Q9UJY4}. +Q9ESM6 GDPD2_MOUSE Glycerophosphoinositol inositolphosphodiesterase GDPD2 (EC 3.1.4.43) (Glycerophosphodiester phosphodiesterase 3) (Glycerophosphodiester phosphodiesterase domain-containing protein 2) (Osteoblast differentiation promoting factor) 539 61,165 Chain (1); Domain (1); Glycosylation (1); Metal binding (3); Mutagenesis (1); Topological domain (7); Transmembrane (6) TRANSMEM 41 61 Helical. {ECO:0000255}.; TRANSMEM 84 104 Helical. {ECO:0000255}.; TRANSMEM 122 142 Helical. {ECO:0000255}.; TRANSMEM 155 175 Helical. {ECO:0000255}.; TRANSMEM 190 210 Helical. {ECO:0000255}.; TRANSMEM 492 512 Helical. {ECO:0000255}. TOPO_DOM 1 40 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 62 83 Extracellular. {ECO:0000255}.; TOPO_DOM 105 121 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 143 154 Extracellular. {ECO:0000255}.; TOPO_DOM 176 189 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 211 491 Extracellular. {ECO:0000255}.; TOPO_DOM 513 539 Cytoplasmic. {ECO:0000255}. FUNCTION: Has glycerophosphoinositol inositolphosphodiesterase activity and specifically hydrolyzes glycerophosphoinositol, with no activity for other substrates such as glycerophosphoinositol 4-phosphate, glycerophosphocholine, glycerophosphoethanolamine, and glycerophosphoserine. Accelerates the program of osteoblast differentiation and growth. May play a role in remodeling of the actin cytoskeleton. {ECO:0000269|PubMed:12933806, ECO:0000269|PubMed:19596859}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12933806}; Multi-pass membrane protein {ECO:0000269|PubMed:12933806}. Cytoplasm {ECO:0000269|PubMed:12933806}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12933806}. Note=Colocalizes with the actin cytoskeleton. TISSUE SPECIFICITY: Detected in spleen, femur and calvaria. {ECO:0000269|PubMed:12933806, ECO:0000269|PubMed:15276213}. +Q99LY2 GDPD3_MOUSE Lysophospholipase D GDPD3 (EC 3.1.4.-) (Glycerophosphodiester phosphodiesterase 7) (Glycerophosphodiester phosphodiesterase domain-containing protein 3) 330 38,488 Chain (1); Domain (1); Metal binding (3); Sequence caution (1); Topological domain (3); Transmembrane (2) TRANSMEM 2 22 Helical. {ECO:0000255}.; TRANSMEM 201 221 Helical. {ECO:0000255}. TOPO_DOM 1 1 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 23 200 Extracellular. {ECO:0000255}.; TOPO_DOM 222 330 Cytoplasmic. {ECO:0000255}. FUNCTION: Hydrolyzes lysoglycerophospholipids to produce lysophosphatidic acid (LPA) and the corresponding amines (PubMed:25528375). Shows a preference for 1-O-alkyl-sn-glycero-3-phosphocholine (lyso-PAF) and lysophosphatidylcholine (lyso-PC), and to a lesser extent for lysophosphatidylethanolamine (lyso-PE) (PubMed:25528375). Does not display glycerophosphodiester phosphodiesterase activity, since it cannot hydrolyze either glycerophosphoinositol or glycerophosphocholine (PubMed:25528375). {ECO:0000269|PubMed:25528375}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:25528375}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:25528375}; Multi-pass membrane protein {ECO:0000305}. Note=Partially colocalized with CANX (PubMed:25528375). {ECO:0000269|PubMed:25528375}. TISSUE SPECIFICITY: Highly expressed in stomach and kidney. In stomach detected in the glandular epithelium. Predominantly expressed in the stomach (at protein level). {ECO:0000269|PubMed:25528375}. +Q6K1E7 GGNB1_MOUSE Gametogenetin-binding protein 1 370 40,505 Chain (1); Region (2); Sequence conflict (2) FUNCTION: Induces mitochondrial fragmentation, possibly by promoting DNM1L-dependent fission and may play a role in mitochondrial morphogenesis during spermatogenesis. {ECO:0000269|PubMed:19208545}. SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein. Golgi apparatus. Mitochondrion intermembrane space. SUBUNIT: Interacts with isoform 1 and isoform 2 of GGN. {ECO:0000269|PubMed:15642376, ECO:0000269|PubMed:15892049}. DOMAIN: The N-terminal domain is required for targeting to the mitochondrion. TISSUE SPECIFICITY: Testis-specific. In the testis, expressed only in germ cells and not in somatic cells. Expression starts in late primary spermatocytes in stage X-XII tubules and gradually increases towards step 1-3 spermatids in stage I-III tubules. Expression then declines continuously and disappears after step 7 spermatids in stage VII tubules (at protein level). {ECO:0000269|PubMed:19208545}. +P03995 GFAP_MOUSE Glial fibrillary acidic protein (GFAP) 430 49,900 Alternative sequence (1); Chain (1); Domain (1); Erroneous initiation (1); Modified residue (17); Region (9); Sequence conflict (11) FUNCTION: GFAP, a class-III intermediate filament, is a cell-specific marker that, during the development of the central nervous system, distinguishes astrocytes from other glial cells. PTM: Phosphorylated by PKN1. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Associated with intermediate filaments. {ECO:0000250}. SUBUNIT: Interacts with SYNM. {ECO:0000269|PubMed:17356066}. TISSUE SPECIFICITY: Brain; isoform 2 expressed at 20-fold lower level than isoform 1. {ECO:0000269|PubMed:12058025}. +Q8K259 GIN1_MOUSE Gypsy retrotransposon integrase-like protein 1 (GIN-1) (Zinc finger H2C2 domain-containing protein) 518 58,789 Alternative sequence (3); Chain (1); Domain (1); Modified residue (1); Sequence conflict (3) +Q9CWY4 GEMI7_MOUSE Gem-associated protein 7 (Gemin-7) 129 14,251 Chain (1); Modified residue (1) FUNCTION: The SMN complex plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}. Nucleus, gem {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Found both in the nucleoplasm and in nuclear bodies called gems (Gemini of Cajal bodies) that are often in proximity to Cajal (coiled) bodies. Also found in the cytoplasm (By similarity). {ECO:0000250}. SUBUNIT: Part of the core SMN complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8 and STRAP/UNRIP. Part of the SMN-Sm complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8, STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG. Interacts directly with GEMIN6, SNRPB, SNRPD2, SNRPD3 and SNRPE (By similarity). {ECO:0000250}. +O35368 IFI3_MOUSE Interferon-activable protein 203 (Ifi-203) (Interferon-inducible protein p203) 408 46,300 Alternative sequence (3); Chain (1); Compositional bias (2); Domain (2); Erroneous initiation (1); Sequence conflict (12) SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17981725}. TISSUE SPECIFICITY: Constitutively expressed in the thymus, bone marrow and spleen. Isoform 1 and isoform 3 are present in liver (at protein level). {ECO:0000269|PubMed:17981725}. +Q8CGE8 IFI5A_MOUSE Interferon-activable protein 205-A (Ifi-205-A) (Interferon-inducible protein p205-A) (Protein D3') 404 45,176 Chain (1); Domain (2); Sequence conflict (1) FUNCTION: May act as a transcriptional regulator in the myeloid lineage. Inhibits cell growth via p53/TP53 and RB1-dependent and independent pathways (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +Q9CQW9 IFM3_MOUSE Interferon-induced transmembrane protein 3 (Dispanin subfamily A member 2b) (DSPA2b) (Fragilis protein) (Interferon-inducible protein 15) (Mouse ifitm-like protein 1) (Mil-1) 137 14,954 Chain (1); Cross-link (4); Intramembrane (1); Lipidation (3); Modified residue (1); Region (1); Sequence conflict (1); Topological domain (3); Transmembrane (1) INTRAMEM 58 78 Helical. {ECO:0000255}. TRANSMEM 110 130 Helical. {ECO:0000255}. TOPO_DOM 1 57 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 79 109 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 131 137 Extracellular. {ECO:0000255}. FUNCTION: IFN-induced antiviral protein which inhibits the entry of viruses to the host cell cytoplasm, permitting endocytosis, but preventing subsequent viral fusion and release of viral contents into the cytosol. Active against multiple viruses, including influenza A virus, SARS coronavirus (SARS-CoV), Marburg virus (MARV) and Ebola virus (EBOV), Dengue virus (DNV), West Nile virus (WNV) and human immunodeficiency virus type 1 (HIV-1). Can inhibit: influenza virus hemagglutinin protein-mediated viral entry, MARV and EBOV GP1,2-mediated viral entry and SARS-CoV S protein-mediated viral entry. Plays a critical role in the structural stability and function of vacuolar ATPase (v-ATPase). Establishes physical contact with the v-ATPase of endosomes which is critical for proper clathrin localization and is also required for the function of the v-ATPase to lower the pH in phagocytic endosomes thus establishing an antiviral state. Involved in initiating germ cell competence and specification, and in the demarcation of PGCs from their somatic neighbors. {ECO:0000269|PubMed:12124616, ECO:0000269|PubMed:18505827, ECO:0000269|PubMed:21253575, ECO:0000269|PubMed:22467717}. PTM: Polyubiquitinated with both 'Lys-48' and 'Lys-63' linkages. Ubiquitination negatively regulates antiviral activity. Lys-24 is the most prevalent ubiquitination site (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein. Late endosome membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Lysosome membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. SUBUNIT: Interacts with SPP1; the interaction reduces OPN expression (By similarity). Interacts with ATP6V0B and CD81. {ECO:0000250, ECO:0000269|PubMed:16395393, ECO:0000269|PubMed:22467717}. TISSUE SPECIFICITY: Expressed in acinar cell. Predominantly expressed in nascent primordial germ cells, as well as in gonadal germ cells. {ECO:0000269|PubMed:12659663, ECO:0000269|PubMed:15184081}. +P01575 IFNB_MOUSE Interferon beta (IFN-beta) 182 22,127 Chain (1); Glycosylation (3); Helix (10); Modified residue (1); Signal peptide (1); Turn (1) FUNCTION: Has antiviral, antibacterial and anticancer activities. PTM: This beta interferon does not have a disulfide bond. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Monomer. Signals mostly via binding to a IFNAR1-IFNAR2 heterodimeric receptor, but can also function with IFNAR1 alone and independently of Jak-STAT pathways. {ECO:0000269|PubMed:23872679}. +Q4VK74 IFNL2_MOUSE Interferon lambda-2 (IFN-lambda-2) (Interleukin-28A) (IL-28A) 193 21,740 Chain (1); Glycosylation (1); Sequence conflict (5); Signal peptide (1) FUNCTION: Cytokine with antiviral, antitumour and immunomodulatory activities. Plays a critical role in the antiviral host defense, predominantly in the epithelial tissues. Acts as a ligand for the heterodimeric class II cytokine receptor composed of IL10RB and IFNLR1, and receptor engagement leads to the activation of the JAK/STAT signaling pathway resulting in the expression of IFN-stimulated genes (ISG), which mediate the antiviral state. Has a restricted receptor distribution and therefore restricted targets: is primarily active in epithelial cells and this cell type-selective action is because of the epithelial cell-specific expression of its receptor IFNLR1. Seems not to be essential for early virus-activated host defense in vaginal infection, but plays an important role in Toll-like receptor (TLR)-induced antiviral defense. Plays a significant role in the antiviral immune defense in the intestinal epithelium. Exerts an immunomodulatory effect by up-regulating MHC class I antigen expression. {ECO:0000269|PubMed:15914836, ECO:0000269|PubMed:16618774, ECO:0000269|PubMed:18250457, ECO:0000269|PubMed:21518880}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8IZJ0}. +P19182 IFRD1_MOUSE Interferon-related developmental regulator 1 (Nerve growth factor-inducible protein PC4) (TPA-induced sequence 7) (TIS7 protein) 449 49,935 Chain (1); Compositional bias (2); Sequence conflict (3) FUNCTION: Could play a role in regulating gene activity in the proliferative and/or differentiative pathways induced by NGF. May be an autocrine factor that attenuates or amplifies the initial ligand-induced signal. SUBUNIT: Interacts with PSIP1/LEDGF. {ECO:0000250}. +Q9D0P8 IFT27_MOUSE Intraflagellar transport protein 27 homolog (Putative GTP-binding protein RAY-like) (Rab-like protein 4) 186 20,814 Chain (1); Nucleotide binding (3) FUNCTION: Small GTPase-like component of the intraflagellar transport (IFT) complex B that promotes the exit of the BBSome complex from cilia via its interaction with ARL6 (PubMed:25446516). Not involved in entry of the BBSome complex into cilium. Prevents aggregation of GTP-free ARL6. Required for hedgehog signaling (PubMed:25446516). Forms a subcomplex within the IFT complex B with IFT25 (By similarity). Its role in intraflagellar transport is mainly seen in tissues rich in ciliated cells such as kidney and testis. Essential for male fertility, spermiogenesis and sperm flagella formation (PubMed:28964737). Plays a role in the early development of the kidney (PubMed:29626631). May be involved in the regulation of ureteric bud initiation (PubMed:29626631). {ECO:0000250|UniProtKB:A8HN58, ECO:0000269|PubMed:25446516, ECO:0000269|PubMed:28964737, ECO:0000269|PubMed:29626631}. SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000269|PubMed:19253336}. Cytoplasm {ECO:0000269|PubMed:28964737}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:28964737}. Note=Localizes to the sperm flagellum. {ECO:0000269|PubMed:28964737}. SUBUNIT: Component of the IFT complex B, at least composed of IFT20, IFT22, HSPB11/IFT25, IFT27, IFT46, IFT52, TRAF3IP1/IFT54, IFT57, IFT74, IFT80, IFT81, and IFT88 (PubMed:19253336). Interacts with HSPB11/IFT25 (PubMed:28430876). Interacts with RABL2/RABL2A; binding is equal in the presence of GTP or GDP (PubMed:23055941). Interacts with IFT88 (PubMed:19253336). Interacts with ARL6; recognizes and binds with the GTP-free form of ARL6 (By similarity). {ECO:0000250|UniProtKB:Q9BW83, ECO:0000269|PubMed:19253336, ECO:0000269|PubMed:23055941, ECO:0000269|PubMed:28430876}. TISSUE SPECIFICITY: Expressed predominantly in the testis (at protein level) (PubMed:28964737). Co-localizes with RABL2/RABL2A in the midpiece of elongated spermatids within the testis (at protein level). {ECO:0000269|PubMed:23055941, ECO:0000269|PubMed:28964737}. +Q62559 IFT52_MOUSE Intraflagellar transport protein 52 homolog (Protein NGD5) 426 48,248 Beta strand (13); Chain (1); Frameshift (1); Helix (8); Sequence conflict (1); Turn (5) FUNCTION: Involved in ciliogenesis as part of a complex involved in intraflagellar transport (IFT), the bi-directional movement of particles required for the assembly, maintenance and functioning of primary cilia (PubMed:19253336). Required for the anterograde transport of IFT88 (By similarity). {ECO:0000250|UniProtKB:Q9Y366, ECO:0000269|PubMed:19253336}. SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000269|PubMed:19253336}. SUBUNIT: Component of the IFT complex B, at least composed of IFT20, IFT22, HSPB11/IFT25, IFT27, IFT46, IFT52, TRAF3IP1/IFT54, IFT57, IFT74, IFT80, IFT81, and IFT88. Interacts with IFT88. Interacts with TTC25 (PubMed:25860617). {ECO:0000269|PubMed:19253336, ECO:0000269|PubMed:25860617}. +Q8BS45 IFT56_MOUSE Intraflagellar transport protein 56 (Protein hop-sterile) (Tetratricopeptide repeat protein 26) (TPR repeat protein 26) 554 64,151 Chain (1); Repeat (4) FUNCTION: Component of the intraflagellar transport (IFT) complex B required for transport of proteins in the motile cilium. Required for transport of specific ciliary cargo proteins related to motility, while it is neither required for IFT complex B assembly or motion nor for cilium assembly. Required for efficient coupling between the accumulation of GLI2 and GLI3 at the ciliary tips and their dissociation from the negative regulator SUFU (PubMed:22718903, PubMed:25340710). Plays a key role in maintaining the integrity of the IFT complex B and the proper ciliary localization of the IFT complex B components. Not required for IFT complex A ciliary localization or function. Essential for maintaining proper microtubule organization within the ciliary axoneme (PubMed:28264835). {ECO:0000269|PubMed:22718903, ECO:0000269|PubMed:25340710, ECO:0000269|PubMed:28264835}. SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000269|PubMed:22718903, ECO:0000269|PubMed:24596149}. Note=Localizes at the base to the ciliary transition zone. {ECO:0000269|PubMed:22718903, ECO:0000269|PubMed:24596149}. SUBUNIT: Component of the IFT complex B. Interacts with IFT46; the interaction is direct. {ECO:0000269|PubMed:24596149}. TISSUE SPECIFICITY: High expression detected in testis. Detected also retina, kidney, lung and brain tissue. The expression level is low in liver and spleen (PubMed:22718903). Present in the airway epithelial cells and the testes (at protein level) (PubMed:25340710). {ECO:0000269|PubMed:22718903, ECO:0000269|PubMed:25340710}. +Q61371 IFT88_MOUSE Intraflagellar transport protein 88 homolog (Recessive polycystic kidney disease protein Tg737) (Tetratricopeptide repeat protein 10) (TPR repeat protein 10) (TgN(Imorpk)737Rpw) 824 92,994 Chain (1); Erroneous initiation (1); Repeat (11); Sequence conflict (5) FUNCTION: Involved in primary cilium biogenesis. Also involved in autophagy since it is required for trafficking of ATG16L and the expansion of the autophagic compartment. {ECO:0000269|PubMed:11062270, ECO:0000269|PubMed:21289087}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:20230748, ECO:0000269|PubMed:23386061}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:19253336, ECO:0000269|PubMed:20230748}. Cell projection, cilium {ECO:0000250|UniProtKB:Q13099}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q13099}. Cytoplasm {ECO:0000269|PubMed:27682589}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:27682589}. Note=Colocalizes with ENTR1 and gamma-tubulin at the basal body of primary cilia. Colocalizes with ENTR1 and pericentrin at the centrosome. {ECO:0000250|UniProtKB:Q13099}. SUBUNIT: Component of the IFT complex B, at least composed of IFT20, IFT22, HSPB11/IFT25, IFT27, IFT46, IFT52, TRAF3IP1/IFT54, IFT57, IFT74, IFT80, IFT81, and IFT88. Interacts with IFT20, IFT22, HSPB11, IFT27, IFT46, IFT52, TRAF3IP1, IFT57, IFT74, IFT80, IFT81, IFT88 AND IFT172. Interacts with C2CD3. Interacts with ENTR1 (via N-terminus) (By similarity). {ECO:0000250|UniProtKB:Q13099, ECO:0000269|PubMed:11062270, ECO:0000269|PubMed:17312020, ECO:0000269|PubMed:19253336, ECO:0000269|PubMed:24469809}. TISSUE SPECIFICITY: Testis. {ECO:0000269|PubMed:27682589}. DISEASE: Note=Defects in Ift88 are the cause of recessive bilateral polycystic kidney disease (PKD) with collecting duct and tubule ectasia, and a liver lesion involving biliary dysplasia and/or portal fibrosis. +P52787 IF_MOUSE Cobalamin binding intrinsic factor (Gastric intrinsic factor) (Intrinsic factor) (IF) (INF) 417 45,497 Binding site (3); Chain (1); Disulfide bond (3); Glycosylation (3); Modified residue (1); Region (2); Sequence conflict (6); Signal peptide (1) FUNCTION: Promotes absorption of the essential vitamin cobalamin (Cbl) in the ileum. After interaction with CUBN, the CBLIF-cobalamin complex is internalized via receptor-mediated endocytosis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Interacts with CUBN (via CUB domains). {ECO:0000250}. TISSUE SPECIFICITY: Gastric mucosa. +Q61249 IGBP1_MOUSE Immunoglobulin-binding protein 1 (Alpha4 phosphoprotein) (CD79a-binding protein 1) (Lymphocyte signal transduction molecule alpha 4) (Protein phosphatase 2/4/6 regulatory subunit) (p52) 340 38,971 Beta strand (1); Chain (1); Domain (1); Helix (8); Modified residue (1); Region (2); Site (1); Turn (2) FUNCTION: Associated to surface IgM-receptor; may be involved in signal transduction. Involved in regulation of the catalytic activity of the phosphatases PP2A, PP4 and PP6 by protecting their partially folded catalytic subunits from degradative polyubiquitination until they associate with regulatory subunits. PTM: Phosphorylated.; PTM: Monoubiquitination by MID1 triggers calpain-mediated cleavage and switches IGBP1 activity from protective to destructive. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. SUBUNIT: Interacts with PPP2CB, and with PP4 and PP6. Interacts with MID2. Interacts with ubiquitin (By similarity). Interacts with partially folded PPP2CA, but not with the fully active protein. Interacts with MID1. {ECO:0000250, ECO:0000269|PubMed:21454489}. DOMAIN: The UIM domain is required for protective effect on PP2A. TISSUE SPECIFICITY: Expressed in spleen, thymus, liver and brain. Ubiquitously expressed in B lineage cell lines. +Q8BQC3 IGDC3_MOUSE Immunoglobulin superfamily DCC subclass member 3 (Putative neuronal cell adhesion molecule) 813 86,460 Alternative sequence (1); Chain (1); Disulfide bond (4); Domain (6); Glycosylation (7); Signal peptide (1); Transmembrane (1) TRANSMEM 653 673 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. TISSUE SPECIFICITY: Detected in cerebellum, kidney, heart, lung, skeletal muscle and spleen. {ECO:0000269|PubMed:9507132, ECO:0000269|PubMed:9922388}. +Q9EQS9 IGDC4_MOUSE Immunoglobulin superfamily DCC subclass member 4 (Neighbor of punc e11) (Protein DDM36) 1252 134,765 Alternative sequence (2); Chain (1); Compositional bias (2); Disulfide bond (4); Domain (9); Glycosylation (2); Modified residue (1); Sequence conflict (10); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 957 977 Helical. {ECO:0000255}. TOPO_DOM 23 956 Extracellular. {ECO:0000255}.; TOPO_DOM 978 1252 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in skeletal muscle, heart and brain. Brain expression is hippocampus-specific. {ECO:0000269|PubMed:10708514}. +P01868 IGHG1_MOUSE Ig gamma-1 chain C region secreted form 324 35,705 Beta strand (10); Chain (1); Disulfide bond (7); Glycosylation (1); Helix (2); Non-terminal residue (1); Region (4); Sequence conflict (2); Turn (1) SUBCELLULAR LOCATION: Isoform Secreted: Secreted. +P03987 IGHG3_MOUSE Ig gamma-3 chain C region 398 43,929 Alternative sequence (1); Chain (1); Glycosylation (3); Non-terminal residue (1); Region (4); Sequence conflict (2); Topological domain (1); Transmembrane (1) TRANSMEM 350 370 Helical. {ECO:0000255}. TOPO_DOM 371 398 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Isoform 1: Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 2: Secreted. +Q923B0 GGACT_MOUSE Gamma-glutamylaminecyclotransferase (GGACT) (EC 4.3.2.8) (AIG2-like domain-containing protein 1) (Gamma-glutamylamine cyclotransferase) 149 17,080 Active site (1); Alternative sequence (2); Beta strand (9); Chain (1); Helix (4); Region (1); Turn (3) FUNCTION: Contributes to degradation of proteins cross-linked by transglutaminases by degrading the cross-link between a lysine and a glutamic acid residue. Catalyzes the formation of 5-oxo-L-proline from L-gamma-glutamyl-L-epsilon-lysine. Inactive with L-gamma-glutamyl-alpha-amino acid substrates such as L-gamma-glutamyl-L-alpha-cysteine and L-gamma-glutamyl-L-alpha-alanine. {ECO:0000250|UniProtKB:Q9BVM4}. SUBUNIT: Monomer. {ECO:0000305|PubMed:16224779}. +Q9DB41 GHC2_MOUSE Mitochondrial glutamate carrier 2 (GC-2) (Glutamate/H(+) symporter 2) (Solute carrier family 25 member 18) 320 34,166 Alternative sequence (1); Chain (1); Modified residue (1); Repeat (3); Transmembrane (6) TRANSMEM 17 37 Helical; Name=1. {ECO:0000255}.; TRANSMEM 66 86 Helical; Name=2. {ECO:0000255}.; TRANSMEM 110 128 Helical; Name=3. {ECO:0000255}.; TRANSMEM 190 210 Helical; Name=4. {ECO:0000255}.; TRANSMEM 230 250 Helical; Name=5. {ECO:0000255}.; TRANSMEM 293 313 Helical; Name=6. {ECO:0000255}. FUNCTION: Involved in the transport of glutamate across the inner mitochondrial membrane. Glutamate is cotransported with H(+) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q6NSU3 GL8D1_MOUSE Glycosyltransferase 8 domain-containing protein 1 (EC 2.4.1.-) 371 41,990 Alternative sequence (2); Chain (1); Glycosylation (1); Sequence conflict (3); Topological domain (2); Transmembrane (1) TRANSMEM 8 28 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 7 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 29 371 Lumenal. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. +Q9CX53 GEMI6_MOUSE Gem-associated protein 6 (Gemin-6) 166 18,750 Chain (1); Modified residue (2); Sequence conflict (2) FUNCTION: The SMN complex plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}. Nucleus, gem {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Found both in the nucleoplasm and in nuclear bodies called gems (Gemini of Cajal bodies) that are often in proximity to Cajal (coiled) bodies. Also found in the cytoplasm (By similarity). {ECO:0000250}. SUBUNIT: Part of the core SMN complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8 and STRAP/UNRIP. Part of the SMN-Sm complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8, STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG. Interacts directly with GEMIN7, SNRPB, SNRPD2, SNRPD3 and SNRPE (By similarity). {ECO:0000250}. +Q9JLQ2 GIT2_MOUSE ARF GTPase-activating protein GIT2 (ARF GAP GIT2) (Cool-interacting tyrosine-phosphorylated protein 2) (CAT-2) (CAT2) (G protein-coupled receptor kinase-interactor 2) (GRK-interacting protein 2) 708 78,766 Chain (1); Domain (1); Modified residue (8); Repeat (3); Sequence conflict (1); Zinc finger (1) FUNCTION: GTPase-activating protein for the ADP ribosylation factor family. {ECO:0000250}. PTM: Tyrosine phosphorylated when coexpressed in cells with PTK2/FAK1 and SRC. SUBUNIT: Interacts with G protein-coupled receptor kinases. Associates with PXN. Also interacts with PIX exchange factors. Identified in a complex with ARHGEF6 and BIN2 (By similarity). Interacts with TGFB1I1. {ECO:0000250, ECO:0000269|PubMed:10330411}. +Q8VC60 GLB1L_MOUSE Beta-galactosidase-1-like protein (EC 3.2.1.-) 646 73,279 Active site (2); Alternative sequence (3); Chain (1); Glycosylation (2); Sequence conflict (1); Signal peptide (1) FUNCTION: Probable glycosyl hydrolase. {ECO:0000305}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +P23336 GGTA1_MOUSE N-acetyllactosaminide alpha-1,3-galactosyltransferase (EC 2.4.1.87) (UDP-galactose:beta-D-galactosyl-1,4-N-acetyl-D-glucosaminide alpha-1,3-galactosyltransferase) (Galactosyltransferase) 394 46,475 Active site (1); Alternative sequence (2); Binding site (1); Chain (1); Glycosylation (2); Metal binding (2); Region (4); Topological domain (2); Transmembrane (1) TRANSMEM 42 60 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 41 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 61 394 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Synthesizes the galactose-alpha(1,3)-galactose group by catalyzing the transfer of a galactose residue, with an alpha-1,3 linkage, on terminal lactosaminide (Gal-beta-1,4-GlcNAc-R) disaccharide borne by a glycoprotein or a glycolipid. Preferentially glycosylates proteins, can synthesize galactose-alpha(1,3)-galactose on glycoproteins but cannot synthesize the glycolipid called isoglobotrihexosylceramide or isogloboside 3 (iGb3). {ECO:0000269|PubMed:12626403}. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. Note=Membrane-bound form in trans cisternae of Golgi. DOMAIN: The conserved DXD motif is involved in cofactor binding. The manganese ion interacts with the beta-phosphate group of UDP and may also have a role in catalysis. +Q9D6Y9 GLGB_MOUSE 1,4-alpha-glucan-branching enzyme (EC 2.4.1.18) (Brancher enzyme) (Glycogen-branching enzyme) 702 80,364 Active site (2); Chain (1); Initiator methionine (1); Modified residue (2); Region (4) Glycan biosynthesis; glycogen biosynthesis. FUNCTION: Required for normal glycogen accumulation. The alpha 1-6 branches of glycogen play an important role in increasing the solubility of the molecule. {ECO:0000250|UniProtKB:Q04446}. SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q04446}. DOMAIN: Binds its carbohydrate substrate close to the active site, but also via regions close to the N-terminus; this may result in increased affinity and therefore increased catalytic efficiency. {ECO:0000250|UniProtKB:Q04446}. +Q62448 IF4G2_MOUSE Eukaryotic translation initiation factor 4 gamma 2 (eIF-4-gamma 2) (eIF-4G 2) (eIF4G 2) (Novel APOBEC-1 target 1) (Translation repressor NAT1) (p97) 906 102,106 Alternative sequence (1); Chain (1); Cross-link (1); Domain (3); Erroneous initiation (1); Modified residue (11); Sequence conflict (27) FUNCTION: Appears to play a role in the switch from cap-dependent to IRES-mediated translation during mitosis, apoptosis and viral infection. Cleaved by some caspases and viral proteases. {ECO:0000250|UniProtKB:P78344, ECO:0000269|PubMed:9030685}. PTM: Phosphorylation; hyperphosphorylated during mitosis. {ECO:0000250|UniProtKB:P78344}. SUBUNIT: Interacts with the serine/threonine protein kinases MKNK1 and MKNK2. Binds EIF4A and EIF3. Interacts with MIF4GD (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed in all tissues examined. {ECO:0000269|PubMed:9027506}. +P01216 GLHA_MOUSE Glycoprotein hormones alpha chain (Anterior pituitary glycoprotein hormones common subunit alpha) (Follicle-stimulating hormone alpha chain) (FSH-alpha) (Follitropin alpha chain) (Luteinizing hormone alpha chain) (LSH-alpha) (Lutropin alpha chain) (Thyroid-stimulating hormone alpha chain) (TSH-alpha) (Thyrotropin alpha chain) 120 13,565 Chain (1); Disulfide bond (5); Glycosylation (2); Sequence conflict (1); Signal peptide (1) FUNCTION: Shared alpha chain of the active heterodimeric glycoprotein hormones thyrotropin/thyroid stimulating hormone/TSH, lutropin/luteinizing hormone/LH and follitropin/follicle stimulating hormone/FSH. These hormones bind specific receptors on target cells that in turn activate downstream signaling pathways. {ECO:0000250|UniProtKB:P01215}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01215}. SUBUNIT: Heterodimer. The active hormones thyrotropin, lutropin and follitropin are heterodimers composed of CGA, a common alpha chain described here and a unique beta chain which confers their biological specificity to the hormones: TSHB for thyrotropin, LHB for lutropin and FSHB for follitropin. {ECO:0000250|UniProtKB:P01215}. +Q0VGT2 GLI2_MOUSE Zinc finger protein GLI2 (Tax helper protein) 1544 165,031 Chain (1); Compositional bias (1); Modified residue (9); Sequence conflict (1); Zinc finger (5) FUNCTION: Functions as transcription regulator in the hedgehog (Hh) pathway (PubMed:9006072). Functions as transcriptional activator (PubMed:10806483). May also function as transcriptional repressor (PubMed:10433919). Requires STK36 for full transcriptional activator activity (PubMed:10806483). Binds to the DNA sequence 5'-GAACCACCCA-3' which is part of the TRE-2S regulatory element (By similarity). Is involved in the smoothened (SHH) signaling pathway (PubMed:10433919). Required for normal skeleton development (PubMed:9006072). {ECO:0000250|UniProtKB:P10070, ECO:0000269|PubMed:10806483, ECO:0000269|PubMed:9006072, ECO:0000305|PubMed:10433919}. PTM: Phosphorylated in vitro by ULK3. Phosphorylated by DYRK2; this inhibits GLI2 transcription factor activity and promotes proteasomal degradation of GLI2. {ECO:0000250|UniProtKB:P10070}.; PTM: Acetylation at Lys-740 inhibits Hh target gene expression, probably by impeding entry into chromatin thus preventing promoter occupancy. {ECO:0000250|UniProtKB:P10070}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10806483}. Cytoplasm {ECO:0000269|PubMed:10806483}. Cell projection, cilium {ECO:0000269|PubMed:25644602}. Note=STK36 promotes translocation to the nucleus (PubMed:10806483). In keratinocytes, it is sequestered in the cytoplasm by SUFU. In the absence of SUFU, it translocates to the nucleus (PubMed:23034632). {ECO:0000269|PubMed:10806483, ECO:0000269|PubMed:23034632}. SUBUNIT: Interacts with ZIC1 and ZIC2 (PubMed:11238441). Interacts with STK36 (PubMed:10806483). Interacts with SUFU; this inhibits transcriptional activation mediated by GLI2 (PubMed:10806483, PubMed:23034632). Interacts (via C-terminal internal region) with FOXC1 (via N-terminus); this interaction is direct and increases GLI2 DNA-binding and transcriptional activity through a smoothened (SMO)-independent Hedgehog (Hh) signaling pathway (PubMed:26565916, PubMed:25808752). {ECO:0000250|UniProtKB:P10070, ECO:0000269|PubMed:10806483, ECO:0000269|PubMed:11238441, ECO:0000269|PubMed:23034632, ECO:0000269|PubMed:25808752, ECO:0000269|PubMed:26565916}. DOMAIN: The N-terminal domain confers transcriptional repressor activity, while the C-terminal domain mediates transcriptional activation. {ECO:0000269|PubMed:10433919}. +P59325 IF5_MOUSE Eukaryotic translation initiation factor 5 (eIF-5) 429 48,968 Chain (1); Compositional bias (3); Cross-link (2); Domain (1); Modified residue (7); Nucleotide binding (1) FUNCTION: Catalyzes the hydrolysis of GTP bound to the 40S ribosomal initiation complex (40S.mRNA.Met-tRNA[F].eIF-2.GTP) with the subsequent joining of a 60S ribosomal subunit resulting in the release of eIF-2 and the guanine nucleotide. The subsequent joining of a 60S ribosomal subunit results in the formation of a functional 80S initiation complex (80S.mRNA.Met-tRNA[F]). SUBUNIT: Interacts with FMR1; this interaction occurs in a RNA-dependent manner. {ECO:0000250|UniProtKB:P55010}. +Q6XP49 GLIS3_MOUSE Zinc finger protein GLIS3 (GLI-similar 3) 780 83,882 Alternative sequence (3); Chain (1); Compositional bias (2); Erroneous initiation (1); Motif (1); Sequence conflict (2); Zinc finger (5) FUNCTION: Acts as both a repressor and activator of transcription. Binds to the consensus sequence 5'-GACCACCCAC-3'. {ECO:0000269|PubMed:14500813}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14500813}. TISSUE SPECIFICITY: In the embryo, expressed at high levels in the kidney and testis. In the adult, expressed at high levels in the kidney and uterus and at lower levels in the brain, lung, skeletal muscle and pancreas. {ECO:0000269|PubMed:14500813}. +Q8R2V2 IFFO2_MOUSE Intermediate filament family orphan 2 512 56,994 Chain (1); Domain (1); Erroneous initiation (1); Sequence caution (1) +Q9ER81 IFG15_MOUSE Torsin-1A-interacting protein 2, isoform IFRG15 (15 kDa interferon-responsive protein) (IFRG15) 131 15,278 Chain (1); Sequence conflict (4) +Q9R002 IFI2_MOUSE Interferon-activable protein 202 (Ifi-202) (Interferon-inducible protein p202) (Lupus susceptibility protein p202) 445 50,466 Beta strand (29); Chain (1); Domain (2); Helix (8); Mutagenesis (17); Sequence conflict (42); Site (2); Turn (4) FUNCTION: Inhibits the transcriptional activity of several transcription factors, including NF-kappa-B p50 and p65, FOS, JUN, E2F1, E2F4, MYOD1 and myogenin. Has anti-apoptotic effects due to inhibition of the transcriptional activity of p53. Binds dsDNA in the cytosol. Is involved in innate immune response and has anti-inflammatory activity. Inhibits caspase activation in response to cytosolic DNA and inhibits the activation of the AIM2 inflammasome, probably by sequestering cytoplasmic DNA and preventing its being bound by AIM2. {ECO:0000269|PubMed:16670293, ECO:0000269|PubMed:19131592, ECO:0000269|PubMed:23567559}. PTM: Phosphorylated. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19131592}. Nucleus {ECO:0000269|PubMed:19131592}. Note=Accumulates first in the cytoplasm, and is translocated to the nucleus after a delay, where it is primarily chromatin-associated. SUBUNIT: Binds to several transcription factors, including NF-kappa-B p50 and p65, FOS, JUN, E2F1, E2F4, MYOD1 and myogenin. Also binds p53, the hypophosphorylated, growth-inhibitory form of the retinoblastoma protein and the p53-binding protein 1 (53BP1). {ECO:0000269|PubMed:23567559}. DOMAIN: The HIN-20 domains mediate dsDNA binding via electrostatic interactions. {ECO:0000269|PubMed:23567559}. +Q64282 IFIT1_MOUSE Interferon-induced protein with tetratricopeptide repeats 1 (IFIT-1) (Glucocorticoid-attenuated response gene 16 protein) (GARG-16) (Interferon-induced 56 kDa protein) (IFI-56K) (P56) 463 53,737 Chain (1); Region (1); Repeat (10); Sequence conflict (2); Site (6) FUNCTION: Interferon-induced antiviral RNA-binding protein that specifically binds single-stranded RNA bearing a 5'-triphosphate group (PPP-RNA), thereby acting as a sensor of viral single-stranded RNAs and inhibiting expression of viral messenger RNAs. Single-stranded PPP-RNAs, which lack 2'-O-methylation of the 5' cap and bear a 5'-triphosphate group instead, are specific from viruses, providing a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Directly binds PPP-RNA in a non-sequence-specific manner. Viruses evolved several ways to evade this restriction system such as encoding their own 2'-O-methylase for their mRNAs or by stealing host cap containing the 2'-O-methylation (cap snatching mechanism). {ECO:0000269|PubMed:21085181, ECO:0000269|PubMed:22589727}. PTM: Phosphorylated. {ECO:0000250}.; PTM: ISGylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19856081}. SUBUNIT: Component of an interferon-dependent multiprotein complex, at least composed of IFIT1, IFIT2 and IFIT3. Interacts with IFIT2 and IFIT3 (By similarity). Interacts with EIF3E (By similarity). Interacts (via TPR repeats 1-4) with RPL15 (By similarity). Interacts with TMEM173/MITA and disrupts its interaction with MAVS or TBK1 (By similarity). Interacts with EIF3C. Interacts (via TPR repeats 4-7) with EEF1A1. {ECO:0000250, ECO:0000269|PubMed:16023166, ECO:0000269|PubMed:19856081}. DOMAIN: RNA recognition is mediated by a convoluted intramolecular fold of the TPR repeats (TPR eddy), which scaffolds unique additional helices that form an RNA binding cleft. {ECO:0000250}. +Q99J93 IFM2_MOUSE Interferon-induced transmembrane protein 2 (Dispanin subfamily A member 2c) (DSPA2c) (Fragilis protein 3) 144 15,743 Chain (1); Intramembrane (1); Lipidation (3); Modified residue (1); Topological domain (3); Transmembrane (1) INTRAMEM 57 77 Helical. {ECO:0000250|UniProtKB:P13164}. TRANSMEM 111 131 Helical. {ECO:0000255}. TOPO_DOM 1 56 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 78 110 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 132 144 Extracellular. {ECO:0000255}. FUNCTION: IFN-induced antiviral protein which inhibits the entry of viruses to the host cell cytoplasm, permitting endocytosis, but preventing subsequent viral fusion and release of viral contents into the cytosol. Active against multiple viruses, including influenza A virus, SARS coronavirus (SARS-CoV), Marburg virus (MARV) and Ebola virus (EBOV), Dengue virus (DNV) and West Nile virus (WNV). Can inhibit: influenza virus hemagglutinin protein-mediated viral entry, MARV and EBOV GP1,2-mediated viral entry and SARS-CoV S protein-mediated viral entry. Induces cell cycle arrest and mediates apoptosis by caspase activation and in p53-independent manner. {ECO:0000269|PubMed:21253575}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. SUBUNIT: Interacts with CD81. {ECO:0000269|PubMed:16395393}. TISSUE SPECIFICITY: Predominantly expressed in nascent primordial germ cells, as well as in gonadal germ cells. {ECO:0000269|PubMed:12659663}. +O88728 IFM5_MOUSE Interferon-induced transmembrane protein 5 (Bone-restricted interferon-induced transmembrane protein-like protein) (Bril) (Dispanin subfamily A member 1) (DSPA1) (Fragilis family member 4) 134 14,667 Chain (1); Lipidation (3); Mutagenesis (4); Topological domain (3); Transmembrane (2) TRANSMEM 40 60 Helical. {ECO:0000255}.; TRANSMEM 89 109 Helical. {ECO:0000255}. TOPO_DOM 1 39 Extracellular. {ECO:0000255}.; TOPO_DOM 61 88 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 110 134 Extracellular. {ECO:0000255, ECO:0000269|PubMed:18442316, ECO:0000269|PubMed:24715519}. FUNCTION: Required for normal bone mineralization. {ECO:0000269|PubMed:18442316, ECO:0000269|PubMed:20838829, ECO:0000269|PubMed:24058703, ECO:0000269|PubMed:24715519}. PTM: Palmitoylated. {ECO:0000269|PubMed:24058703, ECO:0000269|PubMed:24715519}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18442316, ECO:0000269|PubMed:24715519}; Multi-pass membrane protein {ECO:0000255, ECO:0000269|PubMed:18442316}. SUBUNIT: Interacts with FKBP11. {ECO:0000269|PubMed:20838829, ECO:0000269|PubMed:24058703}. TISSUE SPECIFICITY: Detected in embryonic bone (at protein level) (PubMed:18442316). Highly expressed in osteoblasts of adults and embryos. Expressed in primitive hemopoietic cells. {ECO:0000269|PubMed:11106657, ECO:0000269|PubMed:18442316}. +P01572 IFNA1_MOUSE Interferon alpha-1 (IFN-alpha-1) 189 21,646 Chain (1); Disulfide bond (2); Glycosylation (1); Sequence conflict (10); Signal peptide (1) FUNCTION: Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase. {ECO:0000269|PubMed:15254193}. PTM: Glycosylated. {ECO:0000269|PubMed:15254193}. SUBCELLULAR LOCATION: Secreted. +P07349 IFNA5_MOUSE Interferon alpha-5 (IFN-alpha-5) 189 21,514 Chain (1); Disulfide bond (2); Glycosylation (1); Helix (8); Signal peptide (1); Turn (2) FUNCTION: Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase. SUBCELLULAR LOCATION: Secreted. +P07350 IFNA6_MOUSE Interferon alpha-6 (IFN-alpha-6) (Interferon alpha-8) (IFN-alpha-8) 189 21,499 Chain (1); Disulfide bond (2); Glycosylation (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase. SUBCELLULAR LOCATION: Secreted. +P06799 IFNA7_MOUSE Interferon alpha-7 (IFN-alpha-7) 190 21,603 Chain (1); Disulfide bond (2); Glycosylation (1); Signal peptide (1) FUNCTION: Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase. SUBCELLULAR LOCATION: Secreted. +P09235 IFNA9_MOUSE Interferon alpha-9 (IFN-alpha-9) 190 21,684 Chain (1); Disulfide bond (2); Glycosylation (1); Signal peptide (1) FUNCTION: Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase. SUBCELLULAR LOCATION: Secreted. +Q80SS5 IFNAC_MOUSE Interferon alpha-12 (IFN-alpha-12) 189 21,752 Chain (1); Disulfide bond (2); Glycosylation (1); Signal peptide (1) FUNCTION: Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +Q80SU4 IFNAD_MOUSE Interferon alpha-13 (IFN-alpha-13) 189 21,567 Chain (1); Disulfide bond (2); Glycosylation (2); Signal peptide (1) FUNCTION: Exhibits antiviral activity against Theiler's virus, Mengo virus and vesicular stomatitis virus. Interferons alpha stimulate the production of two enzymes: a protein kinase and an oligoadenylate synthetase. {ECO:0000269|PubMed:12930842}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +Q80ZF2 IFNE_MOUSE Interferon epsilon (IFN-epsilon) (Interferon epsilon-1) (Interferon tau-1) 192 22,372 Chain (1); Disulfide bond (1); Signal peptide (1) FUNCTION: Type I interferon required for maintaining basal levels of IFN-regulated genes, including 2'-5'-oligoadenylate synthetase, IRF7 and ISG15, in the female reproductive tract. Directly mediates protection against viral, including HSV-2, and bacterial, including Chlamydia muridarum, genital infections. {ECO:0000269|PubMed:23449591}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Expressed at very high levels in uterus and, at much lower levels, in ovary and cervix. Very low levels, if any, in other organs. In the endometrium, expressed in the luminal and glandular epithelial cells (at protein level). {ECO:0000269|PubMed:15233997, ECO:0000269|PubMed:23449591}. +Q9JHJ3 GLMP_MOUSE Glycosylated lysosomal membrane protein (Lysosomal protein NCU-G1) 404 43,804 Chain (1); Glycosylation (6); Motif (1); Mutagenesis (1); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 371 391 Helical. {ECO:0000255}. TOPO_DOM 36 370 Lumenal. {ECO:0000255}.; TOPO_DOM 392 404 Cytoplasmic. {ECO:0000255}. PTM: Highly N-glycosylated. {ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:19489740}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:19489740}; Single-pass type I membrane protein {ECO:0000269|PubMed:19489740}. TISSUE SPECIFICITY: Detected in brain, heart, liver, kidney, lung, intestine, testis and spleen (PubMed:11444019, PubMed:19489740, PubMed:24487409). Expressed at highest levels in kidney cortex (PubMed:11444019, PubMed:19489740). However, another study reports highest expression levels in lung (PubMed:24487409). {ECO:0000269|PubMed:11444019, ECO:0000269|PubMed:19489740, ECO:0000269|PubMed:24487409}. +P01580 IFNG_MOUSE Interferon gamma (IFN-gamma) 155 17,907 Chain (1); Glycosylation (2); Signal peptide (1) FUNCTION: Produced by lymphocytes activated by specific antigens or mitogens. IFN-gamma, in addition to having antiviral activity, has important immunoregulatory functions. It is a potent activator of macrophages, it has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I interferons. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Homodimer. TISSUE SPECIFICITY: Released primarily from activated T lymphocytes. +Q7TSL0 IFNK_MOUSE Interferon kappa (IFN-kappa) 199 23,581 Chain (1); Disulfide bond (2); Signal peptide (1) FUNCTION: May play a role in the regulation of immune cell function. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. TISSUE SPECIFICITY: Expressed at low levels in peritoneal macrophages. {ECO:0000269|PubMed:12759458}. +Q61025 IFT20_MOUSE Intraflagellar transport protein 20 homolog (mIFT20) 132 15,237 Alternative sequence (1); Chain (1); Coiled coil (1); Erroneous gene model prediction (1); Region (1) FUNCTION: Part of intraflagellar transport (IFT) particles involved in ciliary process assembly. May play a role in the trafficking of ciliary membrane proteins from the Golgi complex to the cilium (PubMed:16775004). Regulates the ciliary platelet-derived growth factor receptor-alpha (PDGFRA) signaling pathway. Required for protein stability of E3 ubiquitin ligases CBL and CBLB that mediate ubiquitination and internalization of PDGFRA for proper feedback inhibition of PDGFRA signaling (PubMed:29237719). Essential for male fertility. Plays an important role in spermatogenesis, particularly spermiogenesis, when germ cells form flagella. May play a role in the transport of flagellar proteins ODF2 and SPAG16 to build sperm flagella and in the removal of redundant sperm cytoplasm (PubMed:27682589). Also involved in autophagy since it is required for trafficking of ATG16L and the expansion of the autophagic compartment (PubMed:24089209). {ECO:0000269|PubMed:16775004, ECO:0000269|PubMed:24089209, ECO:0000269|PubMed:27682589, ECO:0000269|PubMed:29237719}. SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network {ECO:0000269|PubMed:16775004, ECO:0000269|PubMed:19253336, ECO:0000269|PubMed:19889948, ECO:0000269|PubMed:28619825}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:15337773}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:15337773, ECO:0000269|PubMed:16775004}. Cell projection, cilium {ECO:0000269|PubMed:25243405, ECO:0000269|PubMed:29237719}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19889948, ECO:0000269|PubMed:28619825}. Golgi apparatus {ECO:0000269|PubMed:29237719}. Note=Present at the centrosomes during the cell cycle and associated with the proximal portion of the mother centriole and the lateral aspect of the daughter centriole (PubMed:15337773). Associated with basal body at the base of primary cilia (PubMed:15337773). Detected in the Golgi apparatus of round spermatids and late spermatocytes (PubMed:19889948, PubMed:28619825). Also detected in the manchette of step 10-12 spermatids (PubMed:19889948, PubMed:28619825). In step 14 spermatids, found in the basal body of the sperm tail (PubMed:19889948). {ECO:0000269|PubMed:15337773, ECO:0000269|PubMed:19889948, ECO:0000269|PubMed:28619825}. SUBUNIT: Component of the IFT complex B, at least composed of IFT20, IFT22, HSPB11/IFT25, IFT27, IFT46, IFT52, TRAF3IP1/IFT54, IFT57, IFT74, IFT80, IFT81, and IFT88 (PubMed:12821668, PubMed:16775004, PubMed:19253336). Interacts directly with IFT57 and KIF3B/Kinesin II subunit (PubMed:12821668). Interacts with IFT88 (PubMed:19253336). Interacts with CEP83 (By similarity). Interacts with SPEF2 (via C-terminus) (PubMed:19889948). Interacts with CBL and CBLB (By similarity). {ECO:0000250|UniProtKB:Q8IY31, ECO:0000269|PubMed:12821668, ECO:0000269|PubMed:16775004, ECO:0000269|PubMed:19253336, ECO:0000269|PubMed:19889948}. TISSUE SPECIFICITY: Expressed predominantly in the testis (at protein level). Expressed in kidney and retina. Expression is up-regulated during spermiogenesis. {ECO:0000269|PubMed:11916979, ECO:0000269|PubMed:12821668, ECO:0000269|PubMed:27682589}. +Q9DAI2 IFT22_MOUSE Intraflagellar transport protein 22 homolog (Rab-like protein 5) 185 20,833 Chain (1); Modified residue (1); Nucleotide binding (3) FUNCTION: Small GTPase-like component of the intraflagellar transport (IFT) complex B. {ECO:0000269|PubMed:19253336}. SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000269|PubMed:19253336}. SUBUNIT: Component of the IFT complex B, at least composed of IFT20, IFT22, HSPB11/IFT25, IFT27, IFT46, IFT52, TRAF3IP1/IFT54, IFT57, IFT74, IFT80, IFT81, and IFT88. Interacts with IFT88. {ECO:0000269|PubMed:19253336}. +Q9DB07 IFT46_MOUSE Intraflagellar transport protein 46 homolog 301 34,054 Chain (1); Compositional bias (1); Modified residue (1); Sequence conflict (2) FUNCTION: Forms part of a complex involved in intraflagellar transport (IFT), the bi-directional movement of particles required for the assembly, maintenance and functioning of primary cilia. May play a role in chondrocyte maturation and skeletogenesis. {ECO:0000269|PubMed:17720815, ECO:0000269|PubMed:21289087}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body. Cell projection, cilium. Note=Expression is concentrated at the cilium basal body but is also detected along the length of the cilium. SUBUNIT: Component of the IFT complex B, at least composed of IFT20, IFT22, HSPB11/IFT25, IFT27, IFT46, IFT52, TRAF3IP1/IFT54, IFT57, IFT74, IFT80, IFT81, and IFT88. Interacts with IFT57, IFT88 and DAW1. Interacts with ARL13B. Interacts with TTC26/IFT56. Interacts with TTC25 (PubMed:25860617). {ECO:0000269|PubMed:17312020, ECO:0000269|PubMed:18852297, ECO:0000269|PubMed:19253336, ECO:0000269|PubMed:25340710, ECO:0000269|PubMed:25860617}. TISSUE SPECIFICITY: Strongly expressed in ovary and testis, moderately expressed in kidney and brain, and weakly expressed in thymus, heart, lung, liver, spleen and muscle. Expressed in embryonic bone and cartilage, with high expression in non-hypertrophic chondrocytes and weaker expression in hypertrophic chondrocytes. {ECO:0000269|PubMed:17720815}. +Q3TT99 GDPD4_MOUSE Glycerophosphodiester phosphodiesterase domain-containing protein 4 (EC 3.1.-.-) (Glycerophosphodiester phosphodiesterase 6) 632 73,220 Chain (1); Domain (1); Frameshift (1); Glycosylation (4); Metal binding (3); Sequence conflict (1); Topological domain (7); Transmembrane (6) TRANSMEM 65 85 Helical. {ECO:0000255}.; TRANSMEM 115 135 Helical. {ECO:0000255}.; TRANSMEM 148 168 Helical. {ECO:0000255}.; TRANSMEM 181 201 Helical. {ECO:0000255}.; TRANSMEM 241 261 Helical. {ECO:0000255}.; TRANSMEM 543 563 Helical. {ECO:0000255}. TOPO_DOM 1 64 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 86 114 Extracellular. {ECO:0000255}.; TOPO_DOM 136 147 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 169 180 Extracellular. {ECO:0000255}.; TOPO_DOM 202 240 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 262 542 Extracellular. {ECO:0000255}.; TOPO_DOM 564 632 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15276213}. Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Detected in testis, in particular in spermatocytes. {ECO:0000269|PubMed:15276213}. +Q6PDE7 GGT6_MOUSE Glutathione hydrolase 6 (EC 3.4.19.13) (Gamma-glutamyltransferase 6) (GGT 6) (EC 2.3.2.2) (Gamma-glutamyltranspeptidase 6) [Cleaved into: Glutathione hydrolase 6 heavy chain; Glutathione hydrolase 6 light chain] 497 51,467 Alternative sequence (1); Chain (2); Compositional bias (1); Erroneous termination (1); Frameshift (1); Glycosylation (4); Sequence conflict (6); Topological domain (2); Transmembrane (1) TRANSMEM 52 72 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 51 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 73 497 Extracellular. {ECO:0000255}. Sulfur metabolism; glutathione metabolism. FUNCTION: Cleaves glutathione conjugates. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. SUBUNIT: Heterodimer composed of the light and heavy chains. The active site is located in the light chain (By similarity). {ECO:0000250}. +E9PW74 GIMD1_MOUSE GTPase IMAP family member GIMD1 (GIMAP family P-loop NTPase domain-containing protein 1) 217 24,219 Binding site (1); Chain (1); Domain (1); Nucleotide binding (2) +Q68FF6 GIT1_MOUSE ARF GTPase-activating protein GIT1 (ARF GAP GIT1) (G protein-coupled receptor kinase-interactor 1) (GRK-interacting protein 1) 770 85,300 Chain (1); Domain (1); Modified residue (24); Region (3); Repeat (3); Zinc finger (1) FUNCTION: GTPase-activating protein for the ADP ribosylation factor family. May serve as a scaffold to bring together molecules to form signaling modules controlling vesicle trafficking, adhesion and cytoskeletal organization. Increases the speed of cell migration, as well as the size and rate of formation of protrusions, possibly by targeting PAK1 to adhesions and the leading edge of lamellipodia. Sequesters inactive non-tyrosine-phosphorylated paxillin in cytoplasmic complexes (By similarity). Involved in the regulation of cytokinesis; the function may involve ENTR1 and PTPN13 (PubMed:23108400). {ECO:0000250, ECO:0000269|PubMed:23108400}. PTM: Phosphorylated on tyrosine residues by PTK2/FAK1 and SRC in growing fibroblasts. Tyrosine-phosphorylation is increased following cell spreading on fibronectin, decreased in cells arrested in mitosis and increased in the ensuing G1 phase (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Cycles between at least 3 distinct intracellular compartments, including focal adhesions, cytoplasmic complexes and membrane protrusions. During cell migration, when cells detach, moves from the adhesions into the cytoplasmic complexes towards the leading edge, while, when cells adhere, it is found in vinculin-containing adhesions. Recruitment to adhesions may be mediated by active tyrosine-phosphorylated paxillin (By similarity). {ECO:0000250}. SUBUNIT: Interacts with G protein-coupled receptor kinases: GRK2, PPFIA1 and PPFIA4, with ARHGEF6/alpha-PIX, with ARHGEF7/beta-PIX, with PXN/paxillin and with PTK2/FAK1. Component of cytoplasmic complexes, which also contain PXN, ARHGEF6 and PAK1. Interacts with SCRIB (By similarity). Interacts with TGFB1I1. Interacts (via N- and C-terminus) with ENTR1 (via N-terminus); this interaction is direct (By similarity). Found in a complex with ENTR1, PTPN13 and GIT1 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9Y2X7, ECO:0000269|PubMed:12153727}. +Q9EPS3 GLCE_MOUSE D-glucuronyl C5-epimerase (EC 5.1.3.17) (Heparan sulfate C5-epimerase) (Hsepi) (Heparin sulfate C5-epimerase) (Heparin/heparan sulfate:glucuronic acid C5-epimerase) (Heparosan-N-sulfate-glucuronate 5-epimerase) 618 70,089 Binding site (4); Chain (1); Region (3); Sequence conflict (1); Site (4); Topological domain (2); Transmembrane (1) TRANSMEM 12 29 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 11 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 30 618 Lumenal. {ECO:0000255}. Glycan metabolism; heparan sulfate biosynthesis. Glycan metabolism; heparin biosynthesis. FUNCTION: Converts D-glucuronic acid residues adjacent to N-sulfate sugar residues to L-iduronic acid residues, both in maturing heparan sulfate (HS) and heparin chains. This is important for further modifications that determine the specificity of interactions between these glycosaminoglycans and proteins. {ECO:0000269|PubMed:11274177, ECO:0000269|PubMed:11279150, ECO:0000269|PubMed:16532012, ECO:0000269|PubMed:20208005}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:11279150}; Single-pass type II membrane protein {ECO:0000269|PubMed:11279150}. SUBUNIT: Homodimer (By similarity). Interacts with HS2ST1 (PubMed:11687650). {ECO:0000250|UniProtKB:F1QR43, ECO:0000269|PubMed:11687650}. TISSUE SPECIFICITY: Widely expressed with highest levels in lung and lowest levels in spleen. {ECO:0000269|PubMed:11274177}. +Q91VC3 IF4A3_MOUSE Eukaryotic initiation factor 4A-III (eIF-4A-III) (eIF4A-III) (EC 3.6.4.13) (ATP-dependent RNA helicase DDX48) (ATP-dependent RNA helicase eIF4A-3) (DEAD box protein 48) (Eukaryotic translation initiation factor 4A isoform 3) [Cleaved into: Eukaryotic initiation factor 4A-III, N-terminally processed] 411 46,840 Binding site (3); Chain (2); Cross-link (5); Domain (2); Initiator methionine (1); Modified residue (9); Motif (2); Nucleotide binding (2); Sequence conflict (13) FUNCTION: ATP-dependent RNA helicase. Involved in pre-mRNA splicing as component of the spliceosome. Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). Its RNA-dependent ATPase and RNA-helicase activities are induced by CASC3, but abolished in presence of the MAGOH-RBM8A heterodimer, thereby trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The inhibition of ATPase activity by the MAGOH-RBM8A heterodimer increases the RNA-binding affinity of the EJC. Involved in translational enhancement of spliced mRNAs after formation of the 80S ribosome complex. Binds spliced mRNA in sequence-independent manner, 20-24 nucleotides upstream of mRNA exon-exon junctions. Shows higher affinity for single-stranded RNA in an ATP-bound core EJC complex than after the ATP is hydrolyzed. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms; the function is different from the established EJC assembly. Involved in craniofacial development. {ECO:0000250|UniProtKB:P38919}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q3B8Q2}. Nucleus speckle {ECO:0000250|UniProtKB:P38919}. Cytoplasm {ECO:0000250|UniProtKB:Q3B8Q2}. Note=Nucleocytoplasmic shuttling protein. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. Detected in dendritic layer as well as the nuclear and cytoplasmic (somatic) compartments of neurons. Colocalizes with STAU1 and FMR1 in dendrites. {ECO:0000250|UniProtKB:Q3B8Q2}. SUBUNIT: Identified in the spliceosome C complex. Part of the mRNA splicing-dependent exon junction complex (EJC) complex; the core complex contains CASC3, EIF4A3, MAGOH and RBM8A. Interacts with CASC3, MAGOH, NXF1, RBM8A and ALYREF/THOC4. May interact with NOM1. Interacts with POLDIP3. Interacts with CWC22 and PRPF19 in an RNA-independent manner. Direct interaction with CWC22 is mediated by the helicase C-terminal domain. Full interaction with CWC22 occurs only when EIF4A3 is not part of the EJC and prevents EIF4A3 binding to RNA. Interacts with NCBP3. {ECO:0000250|UniProtKB:P38919}. +Q8QZY2 GLCTK_MOUSE Glycerate kinase (EC 2.7.1.31) 523 55,293 Alternative sequence (1); Chain (1); Compositional bias (1); Erroneous initiation (1); Frameshift (1); Modified residue (2); Sequence conflict (15) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8IVS8}. TISSUE SPECIFICITY: Expressed in the hippocampus, callus, brain, cerebellum, renal cortex interstitial cells, epithelium of interlobular bile duct and skeletal muscle. {ECO:0000269|PubMed:16753811}. +Q80XI3 IF4G3_MOUSE Eukaryotic translation initiation factor 4 gamma 3 (eIF-4-gamma 3) (eIF-4G 3) (eIF4G 3) (eIF-4-gamma II) (eIF4GII) 1579 174,890 Alternative sequence (3); Chain (1); Coiled coil (3); Domain (3); Erroneous initiation (1); Modified residue (10); Region (5); Repeat (5); Sequence caution (1); Sequence conflict (5) FUNCTION: Probable component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome. Thought to be a functional homolog of EIF4G1 (By similarity). {ECO:0000250}. SUBUNIT: Interacts with EIF4A, EIF4E, eIF3 and PABPC1. Part of a complex with EIF4E. eIF4F is a multi-subunit complex, the composition of which varies with external and internal environmental conditions. It is composed of at least EIF4A, EIF4E and EIF4G1/EIF4G3. EIF4G1/EIF4G3 interacts through its C-terminus with the serine/threonine kinases MKNK1, and with MKNK2. Appears to act as a scaffold protein, holding these enzymes in place to phosphorylate eIF4E. Non-phosphorylated EIF4EBP1 competes with EIF4G1/EIFG3 to interact with EIF4E; insulin stimulated MAP-kinase (MAPK1 and MAPK3) phosphorylation of EIF4EBP1 causes dissociation of the complex allowing EIF4G1/EIF4G3 to bind and consequent initiation of translation. EIF4G1/EIF4G3 interacts with PABPC1 to bring about circularization of the mRNA (By similarity). {ECO:0000250}. +P63242 IF5A1_MOUSE Eukaryotic translation initiation factor 5A-1 (eIF-5A-1) (eIF-5A1) (Eukaryotic initiation factor 5A isoform 1) (eIF-5A) (eIF-4D) 154 16,832 Chain (1); Erroneous gene model prediction (1); Initiator methionine (1); Modified residue (4); Region (1); Sequence conflict (4) FUNCTION: mRNA-binding protein involved in translation elongation. Has an important function at the level of mRNA turnover, probably acting downstream of decapping. Involved in actin dynamics and cell cycle progression, mRNA decay and probably in a pathway involved in stress response and maintenance of cell wall integrity. With syntenin SDCBP, functions as a regulator of p53/TP53 and p53/TP53-dependent apoptosis. Regulates also TNF-alpha-mediated apoptosis. Mediates effects of polyamines on neuronal process extension and survival. May play an important role in brain development and function, and in skeletal muscle stem cell differentiation (By similarity). {ECO:0000250, ECO:0000269|PubMed:15377278}. PTM: Acetylated. Deacetylated by SIRT2 (By similarity). {ECO:0000250}.; PTM: eIF-5A seems to be the only eukaryotic protein to have a hypusine residue which is a post-translational modification of a lysine by the addition of a butylamino group (from spermidine). SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17707773}. Nucleus {ECO:0000269|PubMed:17707773}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250}. Note=The N-terminal extension contributes in signaling this protein to nuclear localization. SUBUNIT: Interacts with DHPS, with SDCBP and DOHH. Found in a complex with Ran and XPO4. The hypusine modification increases the interaction with XPO4 (By similarity). {ECO:0000250}. +Q8K1M4 GLIS1_MOUSE Zinc finger protein GLIS1 (GLI-similar 1) (Gli homologous protein 1) (GliH1) 789 84,172 Alternative sequence (1); Chain (1); Compositional bias (1); Erroneous initiation (1); Motif (1); Sequence conflict (7); Zinc finger (5) FUNCTION: Acts as both a repressor and activator of transcription. Binds to the consensus sequence 5'-GACCACCCAC-3'. {ECO:0000269|PubMed:12042312, ECO:0000269|PubMed:12385751}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12042312}. TISSUE SPECIFICITY: In the adult, expressed highly in placenta and kidney and at lower levels in the testis, brain, colon, brown fat tissue and thymus. During embryo development, expressed in the frontal nasal region, branchial arches, somites, vibrissal and hair follicles, limb buds, craniofacial regions, ventral part of the tail, intervertebral disks, teeth, eyes and kidney. {ECO:0000269|PubMed:12042312, ECO:0000269|PubMed:12385751}. +Q8VDL9 GLIS2_MOUSE Zinc finger protein GLIS2 (GLI-similar 2) (Neuronal Krueppel-like protein) (Zinc finger protein GLI5) 521 55,842 Chain (1); Compositional bias (2); Mutagenesis (4); Region (3); Sequence conflict (8); Site (1); Zinc finger (5) FUNCTION: Can act either as a transcriptional repressor or as a transcriptional activator, depending on the cell context. Acts as a repressor of the Hedgehog signaling pathway. Represses the Hedgehog-dependent expression of Wnt4. Necessary to maintain the differentiated epithelial phenotype in renal cells through the inhibition of SNAI1, which itself induces the epithelial-to-mesenchymal transition. Represses transcriptional activation by CTNNB1 in the Wnt signaling pathway. May act by recruiting the corepressors CTBP1 and HDAC3. May be involved in neuron differentiation. {ECO:0000269|PubMed:11262234, ECO:0000269|PubMed:11741991, ECO:0000269|PubMed:16326862, ECO:0000269|PubMed:17289029, ECO:0000269|PubMed:17344476, ECO:0000269|PubMed:21816948}. PTM: C-terminus cleavage is induced by interaction with CTNND1 and enhances by Src tyrosine kinase. {ECO:0000269|PubMed:16326862, ECO:0000269|PubMed:17344476}. SUBCELLULAR LOCATION: Nucleus speckle. Cytoplasm. SUBUNIT: Interacts with CTBP1 and HDAC3. Interacts with CTNNB1 and CTNND1. Interacts with SUFU. {ECO:0000269|PubMed:16326862, ECO:0000269|PubMed:17289029, ECO:0000269|PubMed:17344476, ECO:0000269|PubMed:21816948}. DOMAIN: The C2H2-type zinc finger 1 has a major repressor function and is required for CTNNB1 binding. TISSUE SPECIFICITY: Expressed at high levels in kidney, and at lower levels in heart and lung. {ECO:0000269|PubMed:11741991}. +P01882 IGHDM_MOUSE Ig delta chain C region membrane-bound form 290 32,353 Chain (1); Disulfide bond (3); Domain (2); Glycosylation (5); Non-terminal residue (1); Topological domain (1); Transmembrane (1) TRANSMEM 262 279 Helical. {ECO:0000255}. TOPO_DOM 280 290 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Cell lines producing IgD contain several mRNA species for Ig delta chains. In plasmacytomas, the secreted form is the major component, and the membrane-bound form is a minor component. In spleen, however, the membrane-bound form is the major component. These two forms differ in their C-terminal segments. +Q8HW98 IGLO5_MOUSE IgLON family member 5 336 36,767 Chain (1); Disulfide bond (3); Domain (3); Glycosylation (5); Sequence conflict (2); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +P0C673 IGS11_MOUSE Immunoglobulin superfamily member 11 (IgSF11) (Brain and testis-specific immunoglobulin superfamily protein) (Bt-IGSF) 428 46,067 Chain (1); Disulfide bond (2); Domain (2); Glycosylation (1); Modified residue (1); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 241 261 Helical. {ECO:0000255}. TOPO_DOM 23 240 Extracellular. {ECO:0000255}.; TOPO_DOM 262 428 Cytoplasmic. {ECO:0000255}. FUNCTION: Functions as a cell adhesion molecule through homophilic interaction. Stimulates cell growth (By similarity). {ECO:0000250}. PTM: N-glycosylated. {ECO:0000269|PubMed:12207903}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. TISSUE SPECIFICITY: Highly expressed in testis and detected in kidney and adrenal gland. In brain, expressed in commissure fibers of the corpus callosum and pyramidal cell layers of the dentate gyrus and hippocampus where it is probably expressed by both neurons and glial cells. {ECO:0000269|PubMed:12207903}. +Q6ZQA6 IGSF3_MOUSE Immunoglobulin superfamily member 3 (IgSF3) 1194 134,710 Chain (1); Disulfide bond (8); Domain (8); Erroneous initiation (1); Glycosylation (4); Motif (1); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1125 1145 Helical. {ECO:0000255}. TOPO_DOM 20 1124 Extracellular. {ECO:0000255}.; TOPO_DOM 1146 1194 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in the lacrimal duct and lacrimal gland. {ECO:0000269|PubMed:24372406}. +Q8VDC1 FYCO1_MOUSE FYVE and coiled-coil domain-containing protein 1 1437 162,336 Chain (1); Coiled coil (4); Domain (2); Helix (1); Initiator methionine (1); Modified residue (4); Sequence caution (1); Sequence conflict (1); Zinc finger (1) FUNCTION: May mediate microtubule plus end-directed vesicle transport. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome {ECO:0000250}. Endosome {ECO:0000250}. Lysosome {ECO:0000250}. Note=Localizes to the external but not to the internal membrane of autophagosomes, and upon autophagosome/late endosome/lysosome fusion, it stays on the external surface of autolysosomes. {ECO:0000250}. SUBUNIT: Can form homodimers. Interacts (via C-terminus) with MAP1LC3B. Interacts with RAB7A; the interaction with RAB7A induces FYCO1 recruitment to late endosomal/lysosomal compartments. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in heart and testis. Expressed in the eye lens. {ECO:0000269|PubMed:12461651, ECO:0000269|PubMed:21636066}. +P02319 HSP1_MOUSE Sperm protamine P1 (Cysteine-rich protamine) 51 6,958 Chain (1); Disulfide bond (5) FUNCTION: Protamines substitute for histones in the chromatin of sperm during the haploid phase of spermatogenesis. They compact sperm DNA into a highly condensed, stable and inactive complex. PTM: Phosphorylated by SRPK1. {ECO:0000269|PubMed:10390541}. SUBCELLULAR LOCATION: Nucleus. Chromosome. SUBUNIT: Cross-linked by interchain disulfide bonds around the DNA-helix. {ECO:0000250}. TISSUE SPECIFICITY: Testis. +Q5EBG6 HSPB6_MOUSE Heat shock protein beta-6 (HspB6) 162 17,521 Chain (1); Domain (1); Modified residue (2); Region (1) FUNCTION: Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding-competent state. Seems to have versatile functions in various biological processes. Plays a role in regulating muscle function such as smooth muscle vasorelaxation and cardiac myocyte contractility. May regulate myocardial angiogenesis implicating KDR. Overexpression mediates cardioprotection and angiogenesis after induced damage. Stabilizes monomeric YWHAZ thereby supporting YWHAZ chaperone-like activity. {ECO:0000250|UniProtKB:O14558}. PTM: Phosphorylated at Ser-16 by PKA and probably PKD1K; required to protect cardiomyocytes from apoptosis. {ECO:0000250|UniProtKB:O14558, ECO:0000250|UniProtKB:P97541, ECO:0000269|PubMed:21334344}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O14558}. Nucleus {ECO:0000250|UniProtKB:O14558}. Secreted {ECO:0000250|UniProtKB:O14558}. Note=Translocates to nuclear foci during heat shock. {ECO:0000250|UniProtKB:O14558}. SUBUNIT: Homodimer. Small heat shock proteins form high molecular mass oligomers containing variable number of monomers; these oligomers display a very flexible quaternary structure easily exchanging their subunits. Heterooligomer with HSPB1; formed through oligomerization of HSPB1:HSBP6 dimers; subunit exchange leads to formation of at least two different heterooligomeric complexes, differing in variable quantities of HSPB1 and HSPB6 homodimers in addition to HSPB1:HSPB6 heterodimers. Heterooligomer with CRYAB; large heterooligomers consist of CRYAB homodimers and HSPB5:HSPB6 heterodimers but lacking HSPB6 homodimers. Interacts with BAG3. Interacts (phosphorylated) with YWHAZ. Interacts with PDE4A and PDE4D; required for maintenance of the non-phosphorylated state of HSPB6 under basal conditions. Interacts with KDR. Interacts with PRKD1. {ECO:0000250|UniProtKB:O14558, ECO:0000250|UniProtKB:P97541}. +Q99JT1 GATB_MOUSE Glutamyl-tRNA(Gln) amidotransferase subunit B, mitochondrial (Glu-AdT subunit B) (EC 6.3.5.-) (Cytochrome c oxidase assembly factor PET112 homolog) 557 62,118 Chain (1); Modified residue (1); Sequence conflict (2); Transit peptide (1) FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). {ECO:0000255|HAMAP-Rule:MF_03147}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03147}. SUBUNIT: Subunit of the heterotrimeric GatCAB amidotransferase (AdT) complex, composed of A (QRSL1), B (GATB) and C (GATC) subunits. {ECO:0000255|HAMAP-Rule:MF_03147}. +Q61016 GBG7_MOUSE Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-7 68 7,480 Chain (1); Initiator methionine (1); Lipidation (1); Modified residue (2); Propeptide (1) FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. Plays a role in the regulation of adenylyl cyclase signaling in certain regions of the brain. Plays a role in the formation or stabilzation of a G protein heterotrimer (G(olf) subunit alpha-beta-gamma-7) that is required for adenylyl cyclase activity in the striatum. {ECO:0000269|PubMed:12488442}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. SUBUNIT: G proteins are composed of 3 units, alpha, beta and gamma. TISSUE SPECIFICITY: Brain. Found in the hippocampus, striatum, midbrain and cortex. {ECO:0000269|PubMed:12488442}. +Q01514 GBP1_MOUSE Guanylate-binding protein 1 (EC 3.6.5.-) (GTP-binding protein 1) (GBP-1) (mGBP-1) (mGBP1) (Guanine nucleotide-binding protein 1) (Interferon-gamma-inducible protein MAG-1) (Interferon-induced guanylate-binding protein 1) 589 67,712 Chain (1); Domain (1); Lipidation (1); Nucleotide binding (3); Region (1) FUNCTION: Hydrolyzes GTP to GMP in 2 consecutive cleavage reactions. Exhibits antiviral activity against influenza virus (By similarity). Promote oxidative killing and deliver antimicrobial peptides to autophagolysosomes, providing broad host protection against different pathogen classes. {ECO:0000250|UniProtKB:P32455, ECO:0000269|PubMed:21551061}. PTM: Isoprenylation of mouse GBP1 is incomplete. It persistently exists in the cell as a mixture of C20-modified and (more predominantly) unmodified form. Prenylation is required for proper subcellular location (By similarity). {ECO:0000250|UniProtKB:P32455, ECO:0000269|PubMed:10888661}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P32455}. Golgi apparatus membrane; Lipid-anchor {ECO:0000250|UniProtKB:P32455}; Cytoplasmic side. Cell membrane {ECO:0000250|UniProtKB:P32455}. Secreted {ECO:0000250}. Note=Secreted from endothelial cells in the cerebrospinal fluid, upon bacterial challenge and independently of IFNG induction. Golgi membrane localization requires isoprenylation and the presence of another IFNG-induced factor (By similarity). SUBUNIT: Homodimer; homodimerization occurs upon GTP-binding and is required for the second hydrolysis step from GDP to GMP. Heterodimer with other family members, including GBP2, GBP3, GBP4 and GBP5. Dimerization regulates subcellular location to membranous structures. {ECO:0000250|UniProtKB:P32455}. +Q8BHJ7 GBRA5_MOUSE Gamma-aminobutyric acid receptor subunit alpha-5 (GABA(A) receptor subunit alpha-5) 463 52,274 Chain (1); Cross-link (1); Disulfide bond (1); Glycosylation (4); Signal peptide (1); Topological domain (2); Transmembrane (4) TRANSMEM 260 281 Helical. {ECO:0000255}.; TRANSMEM 286 307 Helical. {ECO:0000255}.; TRANSMEM 319 341 Helical. {ECO:0000255}.; TRANSMEM 429 450 Helical. {ECO:0000255}. TOPO_DOM 26 259 Extracellular. {ECO:0000255}.; TOPO_DOM 342 428 Cytoplasmic. {ECO:0000255}. FUNCTION: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel. {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Generally pentameric. There are five types of GABA(A) receptor chains: alpha, beta, gamma, delta, and rho (By similarity). {ECO:0000250}. +Q9DAS9 GBG12_MOUSE Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-12 72 7,997 Chain (1); Initiator methionine (1); Lipidation (1); Modified residue (6); Propeptide (1) FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. SUBUNIT: G proteins are composed of 3 units, alpha, beta and gamma. +P26048 GBRA2_MOUSE Gamma-aminobutyric acid receptor subunit alpha-2 (GABA(A) receptor subunit alpha-2) 451 51,139 Chain (1); Disulfide bond (1); Glycosylation (2); Helix (8); Signal peptide (1); Topological domain (2); Transmembrane (4) TRANSMEM 252 273 Helical. {ECO:0000305}.; TRANSMEM 279 300 Helical. {ECO:0000305}.; TRANSMEM 313 334 Helical. {ECO:0000305}.; TRANSMEM 420 441 Helical. {ECO:0000305}. TOPO_DOM 29 251 Extracellular. {ECO:0000305}.; TOPO_DOM 335 419 Cytoplasmic. {ECO:0000305}. FUNCTION: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane {ECO:0000269|PubMed:11528422}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:11528422, ECO:0000269|PubMed:28978485}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P23576}. Cell projection, dendrite {ECO:0000269|PubMed:28978485}. SUBUNIT: Generally pentameric. There are five types of GABA(A) receptor chains: alpha, beta, gamma, delta, and rho. Interacts with UBQLN1 (PubMed:11528422). Interacts with KIF21B (By similarity). Interacts with LHFPL4 (PubMed:28978485). {ECO:0000250|UniProtKB:P23576, ECO:0000269|PubMed:11528422, ECO:0000269|PubMed:28978485}. +P50153 GBG4_MOUSE Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-4 75 8,405 Chain (1); Lipidation (1); Modified residue (1); Propeptide (1) FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. {ECO:0000305}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. SUBUNIT: G proteins are composed of 3 units, alpha, beta and gamma. Interacts with beta-1 and beta-2, but not with beta-3 (By similarity). Interacts with KCNK1. {ECO:0000250|UniProtKB:P50150, ECO:0000269|PubMed:24496152}. TISSUE SPECIFICITY: Brain. {ECO:0000269|PubMed:7488078}. +P22723 GBRG2_MOUSE Gamma-aminobutyric acid receptor subunit gamma-2 (GABA(A) receptor subunit gamma-2) 474 55,099 Alternative sequence (1); Chain (1); Disulfide bond (1); Glycosylation (3); Modified residue (1); Natural variant (1); Signal peptide (1); Topological domain (2); Transmembrane (4) TRANSMEM 273 295 Helical. {ECO:0000305}.; TRANSMEM 299 321 Helical. {ECO:0000305}.; TRANSMEM 333 355 Helical. {ECO:0000305}.; TRANSMEM 451 474 Helical. {ECO:0000305}. TOPO_DOM 39 272 Extracellular. {ECO:0000305}.; TOPO_DOM 356 450 Cytoplasmic. {ECO:0000305}. FUNCTION: Component of the heteropentameric receptor for GABA, the major inhibitory neurotransmitter in the vertebrate brain. Functions also as histamine receptor and mediates cellular responses to histamine. Functions as receptor for diazepines and various anesthetics, such as pentobarbital; these are bound at a separate allosteric effector binding site. Functions as ligand-gated chloride channel. {ECO:0000269|PubMed:18281286}. PTM: Palmitoylated by ZDHHC3/GODZ; which may affect presynaptic clustering and/or cell surface stability. {ECO:0000269|PubMed:15207850, ECO:0000269|PubMed:15229235}. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane {ECO:0000269|PubMed:18281286}; Multi-pass membrane protein {ECO:0000269|PubMed:18281286}. Cell membrane {ECO:0000269|PubMed:18281286, ECO:0000269|PubMed:25172774, ECO:0000269|PubMed:28279354}; Multi-pass membrane protein {ECO:0000269|PubMed:18281286}. Cell projection, dendrite {ECO:0000269|PubMed:25172774}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P18508}. SUBUNIT: Interacts with GABARAP (By similarity). Heteropentamer, formed by a combination of alpha, beta, gamma, delta and rho chains (PubMed:18281286). Interacts with KIF21B (By similarity). Identified in a complex of 720 kDa composed of LHFPL4, NLGN2, GABRA1, GABRB2, GABRG2 and GABRB3 (By similarity). Interacts with LHFPL4 (PubMed:28978485, PubMed:29742426). {ECO:0000250|UniProtKB:P18507, ECO:0000250|UniProtKB:P18508, ECO:0000269|PubMed:18281286, ECO:0000269|PubMed:28978485, ECO:0000269|PubMed:29742426}. TISSUE SPECIFICITY: Expressed in brain neurons (at protein level). {ECO:0000269|PubMed:25172774}. +Q9JL56 GDE1_MOUSE Glycerophosphodiester phosphodiesterase 1 (EC 3.1.4.-) (EC 3.1.4.44) (Membrane-interacting protein of RGS16) 331 37,629 Chain (1); Domain (1); Glycosylation (1); Metal binding (3); Sequence conflict (1); Topological domain (3); Transmembrane (2) TRANSMEM 4 24 Helical. {ECO:0000255}.; TRANSMEM 249 269 Helical. {ECO:0000255}. TOPO_DOM 1 3 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 25 248 Lumenal. {ECO:0000255}.; TOPO_DOM 270 331 Cytoplasmic. {ECO:0000255}. FUNCTION: Has glycerophosphoinositol phosphodiesterase activity. Hydrolyzes lysoglycerophospholipids to produce lysophosphatidic acid (LPA) and the corresponding amines (PubMed:25596343). Has little or no activity towards glycerophosphocholine. GDE1 activity can be modulated by G-protein signaling pathways (By similarity). {ECO:0000250|UniProtKB:Q9JL55, ECO:0000269|PubMed:25596343}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9JL55}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9JL55}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q9JL55}; Multi-pass membrane protein {ECO:0000255}. Note=Perinuclear vesicles and cell membrane. {ECO:0000250|UniProtKB:Q9JL55}. SUBUNIT: Interacts with PRAF2 (By similarity). Interacts with RGS16 (By similarity). {ECO:0000250|UniProtKB:Q9JL55, ECO:0000250|UniProtKB:Q9NZC3}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10760272}. +P97785 GFRA1_MOUSE GDNF family receptor alpha-1 (GDNF receptor alpha-1) (GDNFR-alpha-1) (GFR-alpha-1) (TGF-beta-related neurotrophic factor receptor 1) 468 51,752 Alternative sequence (1); Chain (1); Compositional bias (1); Disulfide bond (14); Glycosylation (3); Lipidation (1); Propeptide (1); Repeat (3); Sequence conflict (1); Signal peptide (1) FUNCTION: Receptor for GDNF. Mediates the GDNF-induced autophosphorylation and activation of the RET receptor (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. SUBUNIT: 2 molecules of GDNFR-alpha are thought to form a complex with the disulfide-linked GDNF dimer and with 2 molecules of RET. {ECO:0000250}. TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in heart, brain, lung, liver, kidney and testis. {ECO:0000269|PubMed:9592044}. +Q6PB97 FXL19_MOUSE F-box/LRR-repeat protein 19 (F-box and leucine-rich repeat protein 19) 674 73,788 Alternative sequence (2); Chain (1); Compositional bias (5); Domain (1); Repeat (6); Sequence conflict (1); Zinc finger (2) FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. {ECO:0000250}. SUBUNIT: Directly interacts with SKP1 and CUL1. {ECO:0000250}. +Q8CA72 GAN_MOUSE Gigaxonin 597 67,671 Chain (1); Domain (2); Repeat (6) Protein modification; protein ubiquitination. FUNCTION: Probable cytoskeletal component that directly or indirectly plays an important role in neurofilament architecture. May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Controls degradation of TBCB (By similarity). Controls degradation of MAP1B and MAP1S, and is critical for neuronal maintenance and survival. {ECO:0000250, ECO:0000269|PubMed:16227972, ECO:0000269|PubMed:16565160}. PTM: Ubiquitinated by E3 ubiquitin ligase complex formed by CUL3 and RBX1 and probably targeted for proteasome-independent degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12147674}. SUBUNIT: Interacts with TBCB. Interacts with CUL3. Part of a complex that contains CUL3, RBX1 and GAN. Interacts (via BTB domain) with UBA1 (By similarity). Interacts (via Kelch domains) with MAP1B (via C-terminus) and MAP1S (via C-terminus). {ECO:0000250|UniProtKB:Q9H2C0, ECO:0000269|PubMed:12147674, ECO:0000269|PubMed:16565160}. TISSUE SPECIFICITY: Expressed in brain, heart and muscle (at protein level). {ECO:0000269|PubMed:12147674}. +Q08369 GATA4_MOUSE Transcription factor GATA-4 (GATA-binding factor 4) 441 44,580 Chain (1); Compositional bias (4); Frameshift (1); Modified residue (1); Sequence conflict (2); Zinc finger (2) FUNCTION: Transcriptional activator that binds to the consensus sequence 5'-AGATAG-3' and plays a key role in cardiac development (By similarity). In cooperation with TBX5, it binds to cardiac super-enhancers and promotes cardiomyocyte gene expression, while it downregulates endocardial and endothelial gene expression (By similarity). Involved in bone morphogenetic protein (BMP)-mediated induction of cardiac-specific gene expression (By similarity). Binds to BMP response element (BMPRE) DNA sequences within cardiac activating regions (By similarity). Acts as a transcriptional activator of ANF in cooperation with NKX2-5 (PubMed:9584153). Promotes cardiac myocyte enlargement (By similarity). Required during testicular development (By similarity). May play a role in sphingolipid signaling by regulating the expression of sphingosine-1-phosphate degrading enzyme, spingosine-1-phosphate lyase (By similarity). {ECO:0000250|UniProtKB:P43694, ECO:0000250|UniProtKB:P46152, ECO:0000269|PubMed:9584153}. PTM: Methylation at Lys-299 attenuates transcriptional activity. {ECO:0000269|PubMed:22215809}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P43694}. SUBUNIT: Interacts with ZNF260 (By similarity). Interacts with the homeobox domain of NKX2-5 through its C-terminal zinc finger. Also interacts with JARID2 which represses its ability to activate transcription of ANF. Interacts with NFATC4 and LMCD1. Forms a complex made of CDK9, CCNT1/cyclin-T1, EP300 and GATA4 that stimulates hypertrophy in cardiomyocytes. Interacts with NR5A1, ZFPM2 and TBX5. Interacts with TBX18. {ECO:0000250|UniProtKB:P43694, ECO:0000269|PubMed:15542826, ECO:0000269|PubMed:16199866, ECO:0000269|PubMed:17584735, ECO:0000269|PubMed:9568714, ECO:0000269|PubMed:9584153}. TISSUE SPECIFICITY: Heart, intestine, liver, primative endoderm and gonads. +P97489 GATA5_MOUSE Transcription factor GATA-5 (GATA-binding factor 5) 404 42,114 Chain (1); Sequence conflict (2); Zinc finger (2) FUNCTION: Transcription factor required during cardiovascular development (By similarity). Plays an important role in the transcriptional program(s) that underlies smooth muscle cell diversity (PubMed:9119112). Binds to the functionally important CEF-1 nuclear protein binding site in the cardiac-specific slow/cardiac troponin C transcriptional enhancer (By similarity). {ECO:0000250|UniProtKB:Q9BWX5, ECO:0000269|PubMed:9119112}. SUBCELLULAR LOCATION: Nucleus. +Q6PB93 GALT2_MOUSE Polypeptide N-acetylgalactosaminyltransferase 2 (EC 2.4.1.41) (Polypeptide GalNAc transferase 2) (GalNAc-T2) (pp-GaNTase 2) (Protein-UDP acetylgalactosaminyltransferase 2) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 2) [Cleaved into: Polypeptide N-acetylgalactosaminyltransferase 2 soluble form] 570 64,514 Alternative sequence (1); Binding site (8); Chain (2); Disulfide bond (5); Domain (1); Glycosylation (1); Metal binding (3); Modified residue (1); Region (2); Sequence conflict (4); Topological domain (2); Transmembrane (1) TRANSMEM 7 24 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 25 570 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b. Probably involved in O-linked glycosylation of the immunoglobulin A1 (IgA1) hinge region (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. Secreted. Note=Resides preferentially in the trans and medial parts of the Golgi stack. A secreted form also exists. DOMAIN: There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding. {ECO:0000250}.; DOMAIN: The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed at high level. {ECO:0000269|PubMed:12651884}. +P70419 GALT3_MOUSE Polypeptide N-acetylgalactosaminyltransferase 3 (EC 2.4.1.41) (Polypeptide GalNAc transferase 3) (GalNAc-T3) (pp-GaNTase 3) (Protein-UDP acetylgalactosaminyltransferase 3) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3) 633 72,932 Binding site (4); Chain (1); Disulfide bond (5); Domain (1); Glycosylation (2); Metal binding (3); Region (2); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 20 37 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 19 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 38 633 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has activity toward HIV envelope glycoprotein gp120, EA2, Muc2 and Muc5. Glycosylates FGF23 (By similarity). Probably glycosylates fibronectin in vivo. May be involved in phosphate homeostasis. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Resides preferentially in the trans and medial parts of the Golgi stack. {ECO:0000250}. DOMAIN: There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding. {ECO:0000250}.; DOMAIN: The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in the reproductive tract, principally in the testis and uterus, and to a lesser degree in the cervix with only trace levels in the ovary. Also expressed at high level in sublingual gland, stomach and colon, with more moderate amounts present in the submandibular and parotid gland as well as the kidney. {ECO:0000269|PubMed:8912633}. +Q61286 HTF4_MOUSE Transcription factor 12 (TCF-12) (Class A helix-loop-helix transcription factor ME1) (DNA-binding protein HTF4) (E-box-binding protein) (Transcription factor HTF-4) 706 75,811 Alternative sequence (1); Chain (1); Cross-link (6); Domain (1); Modified residue (13); Motif (1); Region (2); Sequence conflict (4) FUNCTION: Transcriptional regulator. Involved in the initiation of neuronal differentiation. Activates transcription by binding to the E box (5'-CANNTG-3'). {ECO:0000269|PubMed:18214987}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Efficient DNA binding requires dimerization with another bHLH protein. Forms homo- or heterooligomers with myogenin, E12 and ITF2 proteins and RUNX1T1 (By similarity). Interacts with PTF1A. Interacts with NEUROD2. Interacts with BHLHA9. {ECO:0000250|UniProtKB:Q99081, ECO:0000269|PubMed:11562365, ECO:0000269|PubMed:18214987}. TISSUE SPECIFICITY: Widely expressed. +Q8CBY0 GATC_MOUSE Glutamyl-tRNA(Gln) amidotransferase subunit C, mitochondrial (Glu-AdT subunit C) (EC 6.3.5.-) 155 16,667 Chain (1); Sequence conflict (5); Transit peptide (1) FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). {ECO:0000255|HAMAP-Rule:MF_03149}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03149}. SUBUNIT: Subunit of the heterotrimeric GatCAB amidotransferase (AdT) complex, composed of A (QRSL1), B (GATB) and C (GATC) subunits. {ECO:0000255|HAMAP-Rule:MF_03149}. +Q9D964 GATM_MOUSE Glycine amidinotransferase, mitochondrial (EC 2.1.4.1) (L-arginine:glycine amidinotransferase) (Transamidinase) 423 48,297 Active site (3); Chain (1); Modified residue (3); Sequence conflict (2); Transit peptide (1) Amine and polyamine biosynthesis; creatine biosynthesis; creatine from L-arginine and glycine: step 1/2. FUNCTION: Catalyzes the biosynthesis of guanidinoacetate, the immediate precursor of creatine. Creatine plays a vital role in energy metabolism in muscle tissues. May play a role in embryonic and central nervous system development. {ECO:0000269|PubMed:12671064}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in kidney, brain, gonads, uterus, and embryonic head, chest and abdomen. Maternally expressed in the placenta and yolk sac of embryos. {ECO:0000269|PubMed:12671064}. +P29387 GBB4_MOUSE Guanine nucleotide-binding protein subunit beta-4 (Transducin beta chain 4) 340 37,379 Chain (1); Initiator methionine (1); Modified residue (3); Repeat (7); Sequence conflict (7) FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. SUBUNIT: G proteins are composed of 3 units, alpha, beta and gamma. +P63078 GBG8_MOUSE Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-8 (Gamma-9) 70 7,843 Chain (1); Lipidation (1); Modified residue (1); Propeptide (1) FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. This subunit may have a very specific role in the development and turnover of olfactory and vomeronasal neurons. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. SUBUNIT: G proteins are composed of 3 units, alpha, beta and gamma. +Q8R3R8 GBRL1_MOUSE Gamma-aminobutyric acid receptor-associated protein-like 1 (GABA(A) receptor-associated protein-like 1) (Glandular epithelial cell protein 1) (GEC-1) 117 14,044 Beta strand (4); Chain (1); Erroneous initiation (1); Helix (4); Lipidation (1); Propeptide (1); Region (2); Sequence conflict (2); Site (1) FUNCTION: Ubiquitin-like modifier that increases cell-surface expression of kappa-type opioid receptor through facilitating anterograde intracellular trafficking of the receptor. Involved in formation of autophagosomal vacuoles. Whereas LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation (By similarity). {ECO:0000250}. PTM: The precursor molecule is cleaved by ATG4B to form the cytosolic form, GABARAPL1-I. This is activated by APG7L/ATG7, transferred to ATG3 and conjugated to phospholipid to form the membrane-bound form, GABARAPL1-II (By similarity). ATG4B also mediates the delipidation required for GABARAPL1 recycling when autophagosomes fuse with lysosomes. {ECO:0000250, ECO:0000269|PubMed:14530254, ECO:0000269|PubMed:16704426}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Golgi apparatus {ECO:0000250}. Cytoplasmic vesicle, autophagosome {ECO:0000250}. SUBUNIT: Interacts with GABRG2 and beta-tubulin (By similarity). Interacts with ATG13, OPRK1, RB1CC1 and ULK1 (By similarity). Interacts with TP53INP1 and TP53INP2 (By similarity). Directly interacts with SQSTM1 (By similarity). Interacts with MAP15 (By similarity). Interacts with TECPR2 (By similarity). Interacts with ATG3 AND ATG7. Interacts with TBC1D5 (By similarity). Interacts with TRIM5 (By similarity). Interacts with MEFV and TRIM21 (By similarity). Interacts with WDFY3 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9H0R8, ECO:0000269|PubMed:16704426}. TISSUE SPECIFICITY: Expressed in testis and heart at high levels. {ECO:0000269|PubMed:11414770}. +Q61107 GBP4_MOUSE Guanylate-binding protein 4 (EC 3.6.5.-) (GTP-binding protein 3) (GBP-3) (GTP-binding protein 4) (GBP-4) (Guanine nucleotide-binding protein 4) (Guanylate-binding protein 3) 620 70,801 Chain (1); Coiled coil (2); Domain (1); Nucleotide binding (3); Region (1); Sequence conflict (11) FUNCTION: Binds GTP, GDP and GMP. Hydrolyzes GTP very efficiently; GDP rather than GMP is the major reaction product. Plays a role in erythroid differentiation. {ECO:0000269|PubMed:9659399}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96PP9}. Nucleus {ECO:0000250|UniProtKB:Q96PP9}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q96PP9}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q96PP9}. Note=Heterodimers with GBP1, GBP2 and GBP5 localize in the compartment of the prenylated GBPs: with GBP1 in a vesicle-like compartment, with GBP2, around the nucleus and with GBP-5, at the Golgi apparatus. {ECO:0000250|UniProtKB:Q96PP9}. SUBUNIT: Heterodimer with other family members, including GBP1, GBP2 and GBP5. Dimerization regulates subcellular location. {ECO:0000250|UniProtKB:Q96PP9}. TISSUE SPECIFICITY: Brain, lung, heart, spleen, kidney, liver and intestine. {ECO:0000269|PubMed:9659399}. +Q8CFB4 GBP5_MOUSE Guanylate-binding protein 5 (EC 3.6.5.-) (GTP-binding protein 5) (GBP-5) (MuGBP-5) (Guanine nucleotide-binding protein 5) 590 66,930 Alternative sequence (2); Chain (1); Domain (1); Lipidation (1); Modified residue (1); Nucleotide binding (3); Propeptide (1); Region (3); Sequence conflict (7) FUNCTION: As an activator of NLRP3 inflammasome assembly, plays a role in innate immunity and inflammation. Promotes selective NLRP3 inflammasome assembly in response to microbial and soluble, but not crystalline, inflammasome activating agents (PubMed:22461501). Hydrolyzes GTP, but in contrast to other family members, such as GBP1 and GBP2, does not produce GMP (By similarity). {ECO:0000250|UniProtKB:Q96PP8, ECO:0000269|PubMed:22461501}. PTM: Isoprenylation is required for proper subcellular location. {ECO:0000250|UniProtKB:Q96PP8}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96PP8}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q96PP8}; Lipid-anchor {ECO:0000250|UniProtKB:Q96PP8}. SUBUNIT: Homodimer. Heterodimer with other family members, including GBP1, GBP2, GBP3 and GBP4 (By similarity). Dimerization is nucleotide-dependent (By similarity). Dimerization regulates subcellular location. May also form tetramers (dimer of dimers) in the presence of GTP (By similarity). Interacts with NLRP3, possibly in its tetrameric form, and promotes PYCARD/ASC polymerization (PubMed:22461501). {ECO:0000250|UniProtKB:Q96PP8, ECO:0000269|PubMed:22461501}. TISSUE SPECIFICITY: Low expression, if any, in many tissues in the absence of stimulation. {ECO:0000269|PubMed:12396730}. +Q9CXP8 GBG10_MOUSE Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-10 68 7,229 Chain (1); Initiator methionine (1); Lipidation (1); Modified residue (2); Propeptide (1) FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. Interacts with beta-1 and beta-2, but not with beta-3 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. SUBUNIT: G proteins are composed of 3 units, alpha, beta and gamma. +P61953 GBG11_MOUSE Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-11 73 8,481 Chain (1); Lipidation (1); Modified residue (1); Propeptide (1) FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. SUBUNIT: G proteins are composed of 3 units, alpha, beta and gamma. Interacts with beta-1 and beta-3, but not with beta-2 (By similarity). {ECO:0000250}. +P48755 FOSL1_MOUSE Fos-related antigen 1 (FRA-1) 273 29,800 Chain (1); Compositional bias (2); Domain (1); Modified residue (1); Region (2); Sequence conflict (4) SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Heterodimer. {ECO:0000250}. +Q9QXW4 FSCN3_MOUSE Fascin-3 (Testis fascin) 498 56,443 Chain (1); Sequence conflict (1) FUNCTION: Acts as an actin bundling protein. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. TISSUE SPECIFICITY: Expressed in testis. +Q8BYN5 FSD1L_MOUSE FSD1-like protein (Coiled-coil domain-containing protein 10) (FSD1 N-terminal-like protein) 507 56,886 Alternative sequence (3); Chain (1); Coiled coil (1); Domain (3); Modified residue (2) +Q7TPM6 FSD1_MOUSE Fibronectin type III and SPRY domain-containing protein 1 496 55,525 Alternative sequence (1); Chain (1); Coiled coil (1); Domain (3); Modified residue (2) FUNCTION: May be involved in microtubule organization and stabilization. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cleavage furrow {ECO:0000250}. Note=Cell-cycle-dependent association with the centrosome. Colocalizes with a subpopulation of microtubules. Does not associates with microtubules during mitosis but reassociates with microtubules during cytokinesis. Localizes to the central portions of a small subset of microtubules in interphase cells and a subpopulation of microtubules in the cleavage furrow, not present in the mitotic spindle (By similarity). {ECO:0000250}. SUBUNIT: Oligomerization is required for binding to microtubules. {ECO:0000250}. DOMAIN: B30.2 box contains a microtubule-binding site. +P47931 FST_MOUSE Follistatin (FS) (Activin-binding protein) 344 37,866 Chain (1); Compositional bias (1); Disulfide bond (18); Domain (7); Glycosylation (2); Sequence conflict (1); Signal peptide (1) FUNCTION: Binds directly to activin and functions as an activin antagonist. Specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (FSH). SUBCELLULAR LOCATION: Secreted. SUBUNIT: Monomer. {ECO:0000305}. +Q9D5H4 FTMT_MOUSE Ferritin, mitochondrial (EC 1.16.3.1) 237 27,158 Chain (1); Domain (1); Erroneous initiation (1); Metal binding (6); Sequence conflict (3); Transit peptide (1) FUNCTION: Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. SUBUNIT: Homooligomer of 24 subunits. The functional molecule is roughly spherical and contains a central cavity into which the polymeric mineral iron core is deposited (By similarity). {ECO:0000250}. +Q3U0V1 FUBP2_MOUSE Far upstream element-binding protein 2 (FUSE-binding protein 2) (KH type-splicing regulatory protein) (KSRP) 748 76,775 Chain (1); Compositional bias (3); Cross-link (2); Domain (4); Initiator methionine (1); Modified residue (15); Region (1); Repeat (4); Sequence conflict (1) FUNCTION: Binds to the dendritic targeting element and may play a role in mRNA trafficking. Part of a ternary complex that binds to the downstream control sequence (DCS) of the pre-mRNA. Mediates exon inclusion in transcripts that are subject to tissue-specific alternative splicing. May interact with single-stranded DNA from the far-upstream element (FUSE). May activate gene expression. Also involved in degradation of inherently unstable mRNAs that contain AU-rich elements (AREs) in their 3'-UTR, possibly by recruiting degradation machinery to ARE-containing mRNAs (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=A small proportion is also found in the cytoplasm of neuronal cell bodies and dendrites. {ECO:0000250}. SUBUNIT: Part of a ternary complex containing FUBP2, PTBP1, PTBP2 and HNRPH1. Interacts with PARN. Interacts with PQBP1. {ECO:0000250|UniProtKB:Q92945}. +Q9CQE9 FWCH2_MOUSE FLYWCH family member 2 139 14,458 Chain (1); Sequence conflict (1) +P81069 GABP2_MOUSE GA-binding protein subunit beta-2 (GABP subunit beta-2) (GABPB-2) (GA-binding protein beta-2-1) (GABP subunit beta-2-1) (GABPB2-1) 414 45,658 Alternative sequence (1); Chain (1); Coiled coil (1); Compositional bias (1); Modified residue (1); Repeat (5); Sequence conflict (7) FUNCTION: Transcription factor capable of interacting with purine rich repeats (GA repeats). Must associate with GABP-alpha to bind DNA. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Heterotetramer of two alpha and two beta subunits. The C-terminal is necessary for the formation of a heterotetrameric GABP-alpha-2/beta-2 complex, and also facilitates homotypic dimerization. Interacts with ADGRB2 (PubMed:16412436). {ECO:0000269|PubMed:16412436}. TISSUE SPECIFICITY: High levels in thymus, spleen, kidney and intestine. +Q9WU81 G6PT3_MOUSE Glucose-6-phosphate exchanger SLC37A2 (Solute carrier family 37 member 2) (cAMP-inducible protein 2) 501 55,073 Alternative sequence (1); Chain (1); Frameshift (1); Glycosylation (3); Sequence conflict (2); Transmembrane (12) TRANSMEM 19 39 Helical. {ECO:0000255}.; TRANSMEM 88 108 Helical. {ECO:0000255}.; TRANSMEM 118 140 Helical. {ECO:0000255}.; TRANSMEM 142 164 Helical. {ECO:0000255}.; TRANSMEM 179 199 Helical. {ECO:0000255}.; TRANSMEM 210 230 Helical. {ECO:0000255}.; TRANSMEM 303 323 Helical. {ECO:0000255}.; TRANSMEM 334 354 Helical. {ECO:0000255}.; TRANSMEM 362 382 Helical. {ECO:0000255}.; TRANSMEM 391 411 Helical. {ECO:0000255}.; TRANSMEM 434 454 Helical. {ECO:0000255}.; TRANSMEM 462 482 Helical. {ECO:0000255}. FUNCTION: Inorganic phosphate and glucose-6-phosphate antiporter. May transport cytoplasmic glucose-6-phosphate into the lumen of the endoplasmic reticulum and translocate inorganic phosphate into the opposite direction. Independent of a lumenal glucose-6-phosphatase. May not play a role in homeostatic regulation of blood glucose levels. {ECO:0000250|UniProtKB:Q8TED4}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8TED4}; Multi-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Highly expressed in bone marrow derived macrophages, and weakly in spleen. {ECO:0000269|PubMed:11004510}. +Q68FH4 GALK2_MOUSE N-acetylgalactosamine kinase (EC 2.7.1.157) (GalNAc kinase) (Galactokinase 2) 458 50,503 Active site (1); Binding site (1); Chain (1); Nucleotide binding (1); Region (2); Site (1) FUNCTION: Acts on GalNAc. Also acts as a galactokinase when galactose is present at high concentrations (By similarity). {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. +Q8BFQ8 GALD1_MOUSE Glutamine amidotransferase-like class 1 domain-containing protein 1 (Parkinson disease 7 domain-containing protein 1) 220 23,277 Chain (1); Frameshift (1); Glycosylation (1); Sequence conflict (3); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +O35969 GAMT_MOUSE Guanidinoacetate N-methyltransferase (EC 2.1.1.2) 236 26,336 Alternative sequence (1); Binding site (5); Chain (1); Domain (1); Initiator methionine (1); Modified residue (2); Region (4) Amine and polyamine biosynthesis; creatine biosynthesis; creatine from L-arginine and glycine: step 2/2. FUNCTION: Converts guanidinoacetate to creatine, using S-adenosylmethionine as the methyl donor. Important in nervous system development. {ECO:0000250|UniProtKB:Q14353}. SUBCELLULAR LOCATION: Cell projection, microvillus {ECO:0000269|PubMed:8312439}. Note=Detected in microvilli of the epithelial cells lining the caput epididymis. SUBUNIT: Monomer. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in testis, caput epididymis, ovary, and liver. In the testis, localized primarily in Sertoli cells. Expressed in brain with high levels in oligodendrocytes and olfactory ensheathing glia. Moderate levels of expression in astrocytes. {ECO:0000269|PubMed:15245487, ECO:0000269|PubMed:8312439}. +Q9CY66 GAR1_MOUSE H/ACA ribonucleoprotein complex subunit 1 (Nucleolar protein family A member 1) (snoRNP protein GAR1) 231 23,474 Alternative sequence (2); Chain (1); Cross-link (1); Region (2); Sequence conflict (1) "FUNCTION: Required for ribosome biogenesis and telomere maintenance. Part of the H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Each rRNA can contain up to 100 pseudouridine (""psi"") residues, which may serve to stabilize the conformation of rRNAs. May also be required for correct processing or intranuclear trafficking of TERC, the RNA component of the telomerase reverse transcriptase (TERT) holoenzyme (By similarity). {ECO:0000250}." SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Nucleus, Cajal body {ECO:0000250}. Note=Also localized to Cajal bodies (coiled bodies). {ECO:0000250}. SUBUNIT: Part of the H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which contains NHP2/NOLA2, GAR1/NOLA1, NOP10/NOLA3, and DKC1/NOLA4, which is presumed to be the catalytic subunit. The complex contains a stable core formed by binding of one or two NOP10-DKC1 heterodimers to NHP2; GAR1 subsequently binds to this core via DKC1. The complex binds a box H/ACA small nucleolar RNA (snoRNA), which may target the specific site of modification within the RNA substrate. The complex also interacts with TERC, which contains a 3'-terminal domain related to the box H/ACA snoRNAs. Specific interactions with snoRNAs or TERC are mediated by GAR1 and NHP2. Associates with NOLC1/NOPP140. H/ACA snoRNPs interact with the SMN complex, consisting of SMN1 or SMN2, GEMIN2/SIP1, DDX20/GEMIN3, and GEMIN4. This is mediated by interaction between GAR1 and SMN1 or SMN2. The SMN complex may be required for correct assembly of the H/ACA snoRNP complex. Component of the telomerase holoenzyme complex composed of one molecule of TERT, one molecule of WRAP53/TCAB1, two molecules of H/ACA ribonucleoprotein complex subunits DKC1, NOP10, NHP2 and GAR1, and a telomerase RNA template component (TERC). The telomerase holoenzyme complex is associated with TEP1, SMG6/EST1A and POT1. {ECO:0000250|UniProtKB:Q9NY12}. DOMAIN: Interaction with SMN1 requires at least one of the RGG-box regions. {ECO:0000250}. +Q61592 GAS6_MOUSE Growth arrest-specific protein 6 (GAS-6) (AXL receptor tyrosine kinase ligand) 674 74,610 Chain (1); Disulfide bond (16); Domain (7); Glycosylation (2); Metal binding (4); Modified residue (6); Sequence conflict (1); Signal peptide (1) FUNCTION: Ligand for tyrosine-protein kinase receptors AXL, TYRO3 and MER whose signaling is implicated in cell growth and survival, cell adhesion and cell migration. GAS6/AXL signaling plays a role in various processes such as endothelial cell survival during acidification by preventing apoptosis, optimal cytokine signaling during human natural killer cell development, hepatic regeneration, gonadotropin-releasing hormone neuron survival and migration, platelet activation, or regulation of thrombotic responses. {ECO:0000269|PubMed:11175853}. PTM: Gamma-carboxyglutamate residues are formed by vitamin K dependent carboxylation. These residues are essential for the binding of calcium. {ECO:0000255|PROSITE-ProRule:PRU00463}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Heterodimer and heterotetramer with AXL. +Q80SZ7 GBG5_MOUSE Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-5 68 7,318 Chain (1); Initiator methionine (1); Lipidation (1); Modified residue (3); Propeptide (1) FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. SUBUNIT: G proteins are composed of 3 units, alpha, beta and gamma. +Q8BKT3 GCFC2_MOUSE GC-rich sequence DNA-binding factor 2 (GC-rich sequence DNA-binding factor) (Transcription factor 9) (TCF-9) 769 87,442 Alternative sequence (2); Chain (1); Coiled coil (1); Erroneous initiation (1); Modified residue (9); Sequence conflict (1) FUNCTION: Factor that represses transcription. It binds to the GC-rich sequences (5'-GCGGGGC-3') present in the epidermal growth factor receptor, beta-actin, and calcium-dependent protease promoters. Involved in pre-mRNA splicing through regulating spliceosome C complex formation. May play a role during late-stage splicing events and turnover of excised inrons (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. SUBUNIT: Found in the Intron Large (IL) complex, a post-mRNA release spliceosomal complex containing the excised intron, U2, U5 and U6 snRNPs, and splicing factors. Interacts with TFIP11 and DHX15 (By similarity). {ECO:0000250}. +Q05915 GCH1_MOUSE GTP cyclohydrolase 1 (EC 3.5.4.16) (GTP cyclohydrolase I) (GTP-CH-I) 241 27,014 Chain (1); Metal binding (3); Modified residue (2); Propeptide (1); Sequence conflict (3); Site (2) Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1. FUNCTION: May positively regulate nitric oxide synthesis in endothelial cells. May be involved in dopamine synthesis. May modify pain sensitivity and persistence. {ECO:0000250|UniProtKB:P30793}. PTM: Phosphorylated. {ECO:0000250|UniProtKB:P30793}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P30793}. Nucleus {ECO:0000250|UniProtKB:P30793}. SUBUNIT: Toroid-shaped homodecamer, composed of two pentamers of five dimers. Interacts with AHSA1 and GCHFR/GFRP. {ECO:0000250|UniProtKB:P30793}. +P55041 GEM_MOUSE GTP-binding protein GEM (GTP-binding mitogen-induced T-cell protein) (RAS-like protein KIR) 295 33,725 Chain (1); Mutagenesis (1); Nucleotide binding (2); Region (1); Sequence conflict (6) FUNCTION: Could be a regulatory protein, possibly participating in receptor-mediated signal transduction at the plasma membrane. Has guanine nucleotide-binding activity but undetectable intrinsic GTPase activity. PTM: Phosphorylated on tyrosine residues. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. SUBUNIT: Interacts with calmodulin in a Ca(2+)-dependent manner. Calmodulin binding significantly decreases GTP binding. Binds ROCK1 (By similarity). {ECO:0000250}. +Q60928 GGT1_MOUSE Glutathione hydrolase 1 proenzyme (EC 3.4.19.13) (Gamma-glutamyltransferase 1) (Gamma-glutamyltranspeptidase 1) (GGT 1) (EC 2.3.2.2) (Leukotriene-C4 hydrolase) (EC 3.4.19.14) (CD antigen CD224) [Cleaved into: Glutathione hydrolase 1 heavy chain; Glutathione hydrolase 1 light chain] 568 61,563 Active site (1); Binding site (3); Chain (2); Disulfide bond (2); Glycosylation (6); Region (1); Topological domain (2); Transmembrane (1) TRANSMEM 5 26 Helical; Signal-anchor for type II membrane protein. {ECO:0000305}. TOPO_DOM 1 4 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 27 568 Extracellular. {ECO:0000255}. Sulfur metabolism; glutathione metabolism. FUNCTION: Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracellular GSH level. It is part of the cell antioxidant defense mechanism. Indirectly regulates multiple aspects of skeletal biology. {ECO:0000269|PubMed:12810527}. PTM: N-glycosylated on both chains. {ECO:0000250|UniProtKB:P19440}.; PTM: Cleaved by autocatalysis into a large and a small subunit and the autocatalytic cleavage is essential to the functional activation of the enzyme. {ECO:0000250|UniProtKB:P19440}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P19440}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P19440}. SUBUNIT: Heterodimer composed of the light and heavy chains. The active site is located in the light chain. {ECO:0000250|UniProtKB:P19440}. DISEASE: Note=Defects in Ggt1 are a cause of glutathionuria, severe growth failure, reduced life spans and infertility. Ggt1-deficient mice have multiple metabolic abnormalities and are dwarf. Some abnormalities can be ameliorated by N-acetylcysteine treatment. {ECO:0000269|PubMed:12810527, ECO:0000269|PubMed:9139708}. +Q9JJT2 GFRA4_MOUSE GDNF family receptor alpha-4 (GDNF receptor alpha-4) (GDNFR-alpha-4) (GFR-alpha-4) (Persephin receptor) 260 27,990 Alternative sequence (4); Chain (1); Glycosylation (1); Lipidation (1); Propeptide (1); Signal peptide (1) FUNCTION: Receptor for persephin. Mediates the GDNF-induced autophosphorylation and activation of the RET receptor. May be important in C-cell development and, in the postnatal development of the adrenal medulla. SUBCELLULAR LOCATION: Isoform a1: Cell membrane; Lipid-anchor, GPI-anchor.; SUBCELLULAR LOCATION: Isoform b1: Cell membrane; Lipid-anchor, GPI-anchor.; SUBCELLULAR LOCATION: Isoform a3: Secreted {ECO:0000305}.; SUBCELLULAR LOCATION: Isoform b3: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Expressed in many tissues including adrenal medulla, brain neurons, with highest levels in the cerebral cortex and hippocampus. Moderate levels found in the gut circular muscle and myenteric ganglia as well as in other peripheral ganglia, including the sensory dorsal root and trigeminal as well as superior cervical and sympathetic chain ganglia. Isoform a1, isoform a2, isoform b1 and isoform b2 are exclusively found in the thyroid, parthyroid and pituitary glands. +Q9D7X8 GGCT_MOUSE Gamma-glutamylcyclotransferase (EC 4.3.2.9) 188 21,166 Active site (1); Chain (1); Modified residue (1); Region (1); Sequence conflict (2) FUNCTION: Catalyzes the formation of 5-oxoproline from gamma-glutamyl dipeptides and may play a significant role in glutathione homeostasis. Induces release of cytochrome c from mitochondria with resultant induction of apoptosis. {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +Q61660 FOXJ1_MOUSE Forkhead box protein J1 (Hepatocyte nuclear factor 3 forkhead homolog 4) (HFH-4) 421 45,474 Chain (1); DNA binding (1); Sequence conflict (2) FUNCTION: Transcription factor specifically required for the formation of motile cilia (PubMed:9096351, PubMed:9739041, PubMed:10873152, PubMed:14996907, PubMed:22357932, PubMed:27965440). Acts by activating transcription of genes that mediate assembly of motile cilia, such as CFAP157 (PubMed:27965440). Binds the DNA consensus sequences 5'-HWDTGTTTGTTTA-3' or 5'-KTTTGTTGTTKTW-3' (where H is not G, W is A or T, D is not C, and K is G or T) (PubMed:9096351). Activates the transcription of a variety of ciliary proteins in the developing brain and lung (PubMed:28666954, PubMed:27914912). {ECO:0000269|PubMed:10873152, ECO:0000269|PubMed:14996907, ECO:0000269|PubMed:22357932, ECO:0000269|PubMed:27914912, ECO:0000269|PubMed:27965440, ECO:0000269|PubMed:28666954, ECO:0000269|PubMed:9096351, ECO:0000269|PubMed:9739041}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:9096351}. TISSUE SPECIFICITY: Predominantly expressed in tissues containing motile cilia. {ECO:0000269|PubMed:27914912, ECO:0000269|PubMed:28666954}. +Q61850 FOXC2_MOUSE Forkhead box protein C2 (Brain factor 3) (BF-3) (Forkhead-related protein FKHL14) (Mesenchyme fork head protein 1) (MFH-1 protein) (Transcription factor FKH-14) 494 52,874 Chain (1); Compositional bias (3); Cross-link (2); DNA binding (1); Modified residue (12); Sequence conflict (3) FUNCTION: Transcriptional activator. Might be involved in the formation of special mesenchymal tissues. {ECO:0000269|PubMed:9169153}. PTM: Phosphorylation regulates FOXC2 transcriptional activity by promoting its recruitment to chromatin. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089}. +Q9CZS3 FOPNL_MOUSE LisH domain-containing protein FOPNL (FGFR1OP N-terminal-like protein) (FOP-related protein of 20 kDa) 174 19,642 Chain (1); Domain (1); Modified residue (1); Region (1); Sequence conflict (1) FUNCTION: Involved in the biogenesis of cilia (By similarity). Required for the recruitement of PLK1 to centrosomes and S phase progression (By similarity). {ECO:0000250|UniProtKB:Q96NB1}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q96NB1}. Cell projection, cilium {ECO:0000269|PubMed:20551181}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:20551181}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasmic granule {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000250|UniProtKB:Q96NB1}. Note=Localization to centrioles and pericentriolar satellites may be mediated by KIAA0753/OFIP. {ECO:0000250|UniProtKB:Q96NB1}. SUBUNIT: Homooligomer; probably required for localization to centrosomes (By similarity). Forms a complex with KIAA0753/OFIP and OFD1; within this complex may stabilize the interaction between OFD1 and KIAA0753/OFIP (PubMed:26643951). Interacts with PCM1; this interaction may be mediated by KIAA0753/OFIP (PubMed:26643951). {ECO:0000250|UniProtKB:Q96NB1, ECO:0000269|PubMed:26643951}. +P35584 FOXA3_MOUSE Hepatocyte nuclear factor 3-gamma (HNF-3-gamma) (HNF-3G) (Forkhead box protein A3) 353 37,601 Chain (1); DNA binding (1) FUNCTION: Transcription factor that is thought to act as a 'pioneer' factor opening the compacted chromatin for other proteins through interactions with nucleosomal core histones and thereby replacing linker histones at target enhancer and/or promoter sites (By similarity). Originally described as a transcription activator for a number of liver genes such as AFP, albumin, tyrosine aminotransferase, PEPCK, etc. Interacts with the cis-acting regulatory regions of these genes. Involved in glucose homeostasis; activates GLUT2 transcription. Involved in regulation of neuronal-specific transcription. Involved in regulation of spermatogenesis; required for the maintenance of the testicular germ cell population and male fertility. {ECO:0000250, ECO:0000269|PubMed:11546810, ECO:0000269|PubMed:17488644, ECO:0000269|PubMed:9632808}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with FOXA2. {ECO:0000250}. TISSUE SPECIFICITY: Restricted mainly to endoderm-derived tissues (lung, liver, stomach, and small intestine), also present additionally in ovary, testis, heart, and adipose tissue, but missing from lung. {ECO:0000269|PubMed:17488644}. +Q61080 FOXF1_MOUSE Forkhead box protein F1 (Forkhead-related protein FKHL5) (Forkhead-related transcription factor 1) (FREAC-1) (Hepatocyte nuclear factor 3 forkhead homolog 8) (HFH-8) 378 39,958 Chain (1); DNA binding (1); Erroneous initiation (3); Sequence conflict (2) FUNCTION: Probable transcription activator for a number of lung-specific genes. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089}. DOMAIN: Activation domains C-terminal of (and distinct from) the forkhead domains are necessary for transcriptional activation. {ECO:0000250}. TISSUE SPECIFICITY: Expressed primarily in lung in alveolar type II pneumocyte cells, and to a lesser extent in placenta, stomach, intestine and colon. {ECO:0000269|PubMed:11313147, ECO:0000269|PubMed:7958446}. +O08696 FOXM1_MOUSE Forkhead box protein M1 (Forkhead homolog 16) (Winged-helix transcription factor Trident) 760 83,694 Chain (1); Compositional bias (1); Cross-link (5); DNA binding (1); Erroneous termination (1); Modified residue (7) FUNCTION: Transcriptional factor regulating the expression of cell cycle genes essential for DNA replication and mitosis. Plays a role in the control of cell proliferation. Plays also a role in DNA breaks repair participating in the DNA damage checkpoint response. {ECO:0000269|PubMed:17101782}. PTM: Phosphorylated in M (mitotic) phase. Phosphorylation by the checkpoint kinase CHEK2 in response to DNA damage increases the FOXM1 protein stability probably stimulating the transcription of genes involved in DNA repair. Phosphorylated by CDK1 in late S and G2 phases, creating docking sites for the POLO box domains of PLK1. Subsequently, PLK1 binds and phosphorylates FOXM1, leading to activation of transcriptional activity and subsequent enhanced expression of key mitotic regulators (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089}. TISSUE SPECIFICITY: Expressed in fetal heart, brain, liver, lung, kidney and limb, but only in adult thymus. Appears to be expressed only in adult organs containing proliferating/cycling cells or in response to growth factors. +Q920E5 FPPS_MOUSE Farnesyl pyrophosphate synthase (FPP synthase) (FPS) (EC 2.5.1.10) ((2E,6E)-farnesyl diphosphate synthase) (Cholesterol-regulated 39 kDa protein) (CR 39) (Dimethylallyltranstransferase) (EC 2.5.1.1) (Farnesyl diphosphate synthase) (Geranyltranstransferase) 353 40,582 Binding site (10); Chain (1); Metal binding (5); Modified residue (1); Site (2) Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis; farnesyl diphosphate from geranyl diphosphate and isopentenyl diphosphate: step 1/1. Isoprenoid biosynthesis; geranyl diphosphate biosynthesis; geranyl diphosphate from dimethylallyl diphosphate and isopentenyl diphosphate: step 1/1. FUNCTION: Key enzyme in isoprenoid biosynthesis which catalyzes the formation of farnesyl diphosphate (FPP), a precursor for several classes of essential metabolites including sterols, dolichols, carotenoids, and ubiquinones. FPP also serves as substrate for protein farnesylation and geranylgeranylation. Catalyzes the sequential condensation of isopentenyl pyrophosphate with the allylic pyrophosphates, dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homodimer. Interacts with RSAD2 (By similarity). {ECO:0000250}. +P97376 FRG1_MOUSE Protein FRG1 (FSHD region gene 1 protein) 258 29,127 Beta strand (17); Chain (1); Compositional bias (1); Helix (1); Motif (2); Sequence conflict (1); Turn (3) FUNCTION: Binds to mRNA in a sequence-independent manner. May play a role in regulation of pre-mRNA splicing or in the assembly of rRNA into ribosomal subunits. May be involved in mRNA transport. May be involved in epigenetic regulation of muscle differentiation through regulation of activity of the histone-lysine N-methyltransferase KMT5B. {ECO:0000269|PubMed:23720823}. SUBCELLULAR LOCATION: Nucleus, Cajal body {ECO:0000250|UniProtKB:Q14331}. Nucleus, nucleolus {ECO:0000269|PubMed:16341202, ECO:0000269|PubMed:20970242}. Cytoplasm {ECO:0000269|PubMed:20970242}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:20970242}. Note=Localization changes during myogenesis from mainly cytoplasmic in undifferentiated myoblasts, to strongly nucleolar in early myotubes and back to cytoplasmic 5 days post-differentiation. Localized at the Z-line in the sarcomere of matured myotubes 8 days post-differentiation. {ECO:0000269|PubMed:20970242}. SUBUNIT: Homodimer and homotetramer in solution. Identified in the spliceosome C complex. Interacts (via N-terminus) with KPNA2 and NXF1/TAP. Interacts with F-actin with a stoichiometry of 2:1 (By similarity). Interacts with KMT5B (via C-terminus). {ECO:0000250, ECO:0000269|PubMed:23720823}. +Q3UFK8 FRMD8_MOUSE FERM domain-containing protein 8 466 51,828 Chain (1); Domain (1); Modified residue (7); Sequence conflict (6) +Q0VAX3 FS2P1_MOUSE Fatty acid desaturase 2-like protein FADS2P1 487 57,082 Chain (1); Domain (1); Metal binding (2); Motif (3); Topological domain (5); Transmembrane (4) TRANSMEM 176 196 Helical. {ECO:0000255}.; TRANSMEM 202 222 Helical. {ECO:0000255}.; TRANSMEM 308 328 Helical. {ECO:0000255}.; TRANSMEM 350 370 Helical. {ECO:0000255}. TOPO_DOM 1 175 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 197 201 Lumenal. {ECO:0000255}.; TOPO_DOM 223 307 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 329 349 Lumenal. {ECO:0000255}.; TOPO_DOM 371 487 Cytoplasmic. {ECO:0000255}. Lipid metabolism; polyunsaturated fatty acid biosynthesis. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. DOMAIN: The histidine box domains may contain the active site and/or be involved in metal ion binding. +Q920B0 FRM4B_MOUSE FERM domain-containing protein 4B (GRP1-binding protein GRSP1) (Golgi-associated band 4.1-like protein) (GOBLIN) 1035 118,007 Alternative sequence (1); Chain (1); Coiled coil (2); Cross-link (2); Domain (1); Erroneous initiation (1); Modified residue (4); Region (1); Sequence conflict (5) FUNCTION: Member of GRP1 signaling complexes that are acutely recruited to plasma membrane ruffles in response to insulin receptor signaling. May function as a scaffolding protein that regulates epithelial cell polarity by connecting ARF6 activation with the PAR3 complex (PubMed:20080746). Plays a redundant role with FRMD4A in epithelial polarization (PubMed:20080746). {ECO:0000269|PubMed:20080746}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11445584}. Cell junction, tight junction {ECO:0000269|PubMed:20080746}. Cell junction, adherens junction {ECO:0000269|PubMed:20080746}. Note=Colocalized with PARD3 at adherens junction and tight junction (PubMed:20080746). {ECO:0000269|PubMed:20080746}. SUBUNIT: Interacts with CYTH3 (PubMed:11445584, PubMed:20080746). Interacts with PARD3 (PubMed:20080746). Interacts with CYTH1. {ECO:0000269|PubMed:11445584, ECO:0000269|PubMed:20080746}. TISSUE SPECIFICITY: Isoform 1 is expressed in the brain. Isoform 2 is expressed in the lung (at protein level). {ECO:0000269|PubMed:11445584}. +Q6NVD0 FREM2_MOUSE FRAS1-related extracellular matrix protein 2 (ECM3 homolog) (NV domain-containing protein 1) 3160 350,640 Alternative sequence (3); Chain (1); Domain (5); Glycosylation (5); Repeat (12); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 3106 3126 Helical. {ECO:0000255}. TOPO_DOM 40 3105 Extracellular. {ECO:0000255}.; TOPO_DOM 3127 3160 Cytoplasmic. {ECO:0000255}. FUNCTION: Extracellular matrix protein required for maintenance of the integrity of the skin epithelium and for maintenance of renal epithelia. May be required for epidermal adhesion. {ECO:0000269|PubMed:15838507}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}; Extracellular side {ECO:0000305}. DOMAIN: The Calx-beta domains bind calcium with high affinity and undergo a major conformational shift upon binding. {ECO:0000250}. TISSUE SPECIFICITY: First expressed from E10 in the mesodermal core of the branchial arches, developing lens, otic vesicle and limb apical ectodermal ridge. Later, it is expressed in the vibrissae and vibrissae pad, eyelids ear and pelage follicles and, at low levels, in the epidermis. Also expressed in caudal somites and, in later embryos, in facial, limb and intercostal muscles. In contrast to Frem1, it is not expressed in the developing mammary glands or in the caecum. Restricted to the epithelia in a pattern complementary to that of Frem1 (which is generally expressed in the dermis and mesenchyme). In the developing kidney, it is expressed At in the mesonephric and metanephric epithelia at E11.5, with a highest expression at the tips of the developing ureteric buds. At E12.5 and E13.5, it is still expressed throughout the epithelial components of the kidney, including epithelia fated to form nephrons, which are induced by the ureter tips to differentiate from the mesenchymal condensations that surround them. {ECO:0000269|PubMed:15838507}. +Q8BGW1 FTO_MOUSE Alpha-ketoglutarate-dependent dioxygenase FTO (Fat mass and obesity-associated protein) (Protein fatso) (U6 small nuclear RNA (2'-O-methyladenosine-N(6)-)-demethylase FTO) (EC 1.14.11.-) (U6 small nuclear RNA N(6)-methyladenosine-demethylase FTO) (EC 1.14.11.-) (mRNA (2'-O-methyladenosine-N(6)-)-demethylase FTO) (m6A(m)-demethylase FTO) (EC 1.14.11.-) (mRNA N(6)-methyladenosine demethylase FTO) (EC 1.14.11.53) (tRNA N1-methyl adenine demethylase FTO) (EC 1.14.11.-) 502 58,007 Alternative sequence (5); Binding site (6); Chain (1); Erroneous initiation (1); Metal binding (3); Modified residue (1); Mutagenesis (4); Region (4); Sequence conflict (10) FUNCTION: RNA demethylase that mediates oxidative demethylation of different RNA species, such as mRNAs, tRNAs and snRNAs, and acts as a regulator of fat mass, adipogenesis and energy homeostasis (PubMed:17991826, PubMed:18775698, PubMed:28002401). Specifically demethylates N(6)-methyladenosine (m6A) RNA, the most prevalent internal modification of messenger RNA (mRNA) in higher eukaryotes (PubMed:28002401). M6A demethylation by FTO affects mRNA expression and stability (By similarity). Also able to demethylate m6A in U6 small nuclear RNA (snRNA) (By similarity). Mediates demethylation of N(6),2'-O-dimethyladenosine cap (m6A(m)), by demethylating the N(6)-methyladenosine at the second transcribed position of mRNAs and U6 snRNA (PubMed:28002401). Demethylation of m6A(m) in the 5'-cap by FTO affects mRNA stability by promoting susceptibility to decapping (By similarity). Also acts as a tRNA demethylase by removing N(1)-methyladenine from various tRNAs (By similarity). Has no activity towards 1-methylguanine (By similarity). Has no detectable activity towards double-stranded DNA (By similarity). Also able to repair alkylated DNA and RNA by oxidative demethylation: demethylates single-stranded RNA containing 3-methyluracil, single-stranded DNA containing 3-methylthymine and has low demethylase activity towards single-stranded DNA containing 1-methyladenine or 3-methylcytosine (PubMed:17991826, PubMed:18775698). Ability to repair alkylated DNA and RNA is however unsure in vivo (PubMed:17991826, PubMed:18775698). Involved in the regulation of fat mass, adipogenesis and body weight, thereby contributing to the regulation of body size and body fat accumulation (PubMed:19234441, PubMed:19680540, PubMed:21076408, PubMed:23817550, PubMed:23300482). Involved in the regulation of thermogenesis and the control of adipocyte differentiation into brown or white fat cells (PubMed:19234441, PubMed:19680540). Regulates activity of the dopaminergic midbrain circuitry via its ability to demethylate m6A in mRNAs (PubMed:23817550). {ECO:0000250|UniProtKB:Q9C0B1, ECO:0000269|PubMed:17991826, ECO:0000269|PubMed:18775698, ECO:0000269|PubMed:19234441, ECO:0000269|PubMed:19680540, ECO:0000269|PubMed:21076408, ECO:0000269|PubMed:23300482, ECO:0000269|PubMed:23817550, ECO:0000269|PubMed:28002401}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17991826, ECO:0000269|PubMed:19234441, ECO:0000269|PubMed:19680540}. Nucleus speckle {ECO:0000250|UniProtKB:Q9C0B1}. Cytoplasm {ECO:0000250|UniProtKB:Q9C0B1}. Note=Localizes mainly in the nucleus, where it is able to demethylate N(6)-methyladenosine (m6A) and N(6),2'-O-dimethyladenosine cap (m6A(m)) in U6 small nuclear RNA (snRNA), N(1)-methyladenine from tRNAs and internal m6A in mRNAs. In the cytoplasm, mediates demethylation of m6A and m6A(m) in mRNAs and N(1)-methyladenine from tRNAs. {ECO:0000250|UniProtKB:Q9C0B1}. SUBUNIT: Monomer (PubMed:19680540). May also exist as homodimer (PubMed:19680540). {ECO:0000269|PubMed:19680540}. DOMAIN: The 3D-structure of the Fe2OG dioxygenase domain is similar to that of the Fe2OG dioxygenase domain found in the bacterial DNA repair dioxygenase alkB and its mammalian orthologs, but sequence similarity is very low. As a consequence, the domain is not detected by protein signature databases. {ECO:0000250|UniProtKB:Q9C0B1}. TISSUE SPECIFICITY: Ubiquitous. Detected in brain, brain cortex, hypothalamus, cerebellum, liver, pancreas, heart, kidney, white adipose tissue and skeletal muscle. Most abundant in the brain, particularly in hypothalamic nuclei governing energy balance. {ECO:0000269|PubMed:17991826, ECO:0000269|PubMed:19234441}. +Q99KY4 GAK_MOUSE Cyclin-G-associated kinase (EC 2.7.11.1) 1305 143,641 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Domain (4); Initiator methionine (1); Modified residue (14); Nucleotide binding (1); Sequence conflict (5) FUNCTION: Associates with cyclin G and CDK5. Seems to act as an auxilin homolog that is involved in the uncoating of clathrin-coated vesicles by Hsc70 in non-neuronal cells. Expression oscillates slightly during the cell cycle, peaking at G1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Cell junction, focal adhesion {ECO:0000250}. Note=Localizes to the perinuclear area and to the trans-Golgi network. Also seen on the plasma membrane, probably at focal adhesions (By similarity). {ECO:0000250}. +Q9DCD6 GBRAP_MOUSE Gamma-aminobutyric acid receptor-associated protein (GABA(A) receptor-associated protein) 117 13,918 Beta strand (4); Chain (1); Helix (4); Lipidation (1); Propeptide (1); Region (3); Sequence conflict (1); Site (1) FUNCTION: Ubiquitin-like modifier that plays a role in intracellular transport of GABA(A) receptors and its interaction with the cytoskeleton. Involved in apoptosis. Involved in autophagy. Whereas LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation (By similarity). {ECO:0000250}. PTM: The precursor molecule is cleaved by ATG4B to form the cytosolic form, GABARAP-I. This is activated by APG7L/ATG7, transferred to ATG3 and conjugated to phospholipid to form the membrane-bound form, GABARAP-II. {ECO:0000269|PubMed:14530254}. SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10899939}. Golgi apparatus membrane {ECO:0000250}. Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:O95166}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:P60517}. Note=Largely associated with intracellular membrane structures including the Golgi apparatus and postsynaptic cisternae. Colocalizes with microtubules (PubMed:10899939). Localizes also to discrete punctae along the ciliary axoneme (PubMed:24089209). {ECO:0000269|PubMed:10899939, ECO:0000269|PubMed:14530254, ECO:0000269|PubMed:24089209}. SUBUNIT: Interacts with GPHN (PubMed:10900017). Interacts with NSF (By similarity). Interacts with ATG7 (PubMed:11890701). Interacts with ATG3 and ATG13 (By similarity). Interacts with alpha-tubulin (By similarity). Interacts with beta-tubulin (PubMed:10899939). Interacts with GABRG2 (By similarity). Interacts with RB1CC1 (By similarity). Interacts with ULK1 (By similarity). Interacts with CALR (By similarity). Interacts with DDX47 (By similarity). Interacts with TP53INP1 and TP53INP2 (By similarity). Interacts with TBC1D5 (By similarity). Interacts with TBC1D25 (PubMed:21383079). Directly interacts with SQSTM1 (By similarity). Interacts with MAPK15 (By similarity). Interacts with TECPR2 (By similarity). Interacts with PCM1 (By similarity). Interacts with TRIM5 and TRIM21 (By similarity). Interacts with MEFV (By similarity). Interacts with KIF21B (By similarity). Interacts with WDFY3; this interaction is required for WDFY3 recruitment to MAP1LC3B-positive p62/SQSTM1 bodies (By similarity). {ECO:0000250|UniProtKB:O95166, ECO:0000250|UniProtKB:P60517, ECO:0000269|PubMed:10899939, ECO:0000269|PubMed:10900017, ECO:0000269|PubMed:11890701, ECO:0000269|PubMed:21383079}. +P01864 GCAB_MOUSE Ig gamma-2A chain C region secreted form (B allele) 335 36,596 Beta strand (19); Chain (1); Domain (3); Glycosylation (1); Helix (4); Non-terminal residue (1); Turn (6) SUBCELLULAR LOCATION: Isoform Secreted: Secreted {ECO:0000305}. +P01865 GCAM_MOUSE Ig gamma-2A chain C region, membrane-bound form 398 43,949 Beta strand (17); Chain (1); Disulfide bond (7); Domain (3); Glycosylation (1); Helix (5); Non-terminal residue (1); Topological domain (1); Transmembrane (1); Turn (4) TRANSMEM 345 362 Helical. {ECO:0000255}. TOPO_DOM 363 398 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +P82976 GBX1_MOUSE Homeobox protein GBX-1 (Gastrulation and brain-specific homeobox protein 1) 418 43,710 Chain (1); Compositional bias (1); DNA binding (1) SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. TISSUE SPECIFICITY: Expressed in CNS including rhombomeres 3 and 5, optic vesicles, and the medial ganglionic eminence. {ECO:0000269|PubMed:12799077}. +P63213 GBG2_MOUSE Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 (G gamma-I) 71 7,850 Chain (1); Initiator methionine (1); Lipidation (1); Modified residue (2); Propeptide (1) FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. SUBUNIT: G proteins are composed of 3 units, alpha, beta and gamma. The heterodimer formed by GNB1 and GNG2 interacts with ARHGEF5. {ECO:0000250|UniProtKB:P59768, ECO:0000250|UniProtKB:P63212}. TISSUE SPECIFICITY: Adrenal gland and brain. +O88819 FUT9_MOUSE Alpha-(1,3)-fucosyltransferase 9 (EC 2.4.1.-) (Fucosyltransferase 9) (Fucosyltransferase IX) (Fuc-TIX) (FucT-IX) (Galactoside 3-L-fucosyltransferase) 359 42,041 Chain (1); Glycosylation (3); Topological domain (2); Transmembrane (1) TRANSMEM 12 32 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 11 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 33 359 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Transfers a fucose to lacto-N-neotetraose but not to either alpha2,3-sialyl lacto-N-neotetraose or lacto-N-tetraose. Can catalyze the last step in the biosynthesis of Lewis antigen, the addition of a fucose to precursor polysaccharides. {ECO:0000269|PubMed:9756916}. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Membrane-bound form in trans cisternae of Golgi. {ECO:0000250}. TISSUE SPECIFICITY: Mainly detected in brain and kidney. {ECO:0000269|PubMed:9756916}. +O35601 FYB1_MOUSE FYN-binding protein 1 (Adhesion and degranulation promoting adaptor protein) (ADAP) (FYB-120/130) (p120/p130) (FYN-T-binding protein) (SLAP-130) (SLP-76-associated phosphoprotein) 819 90,055 Alternative sequence (1); Chain (1); Coiled coil (1); Compositional bias (5); Domain (2); Modified residue (10); Motif (4) FUNCTION: May play a role in linking T-cell signaling to remodeling of the actin cytoskeleton (By similarity). Acts as an adapter protein of the FYN and LCP2 signaling cascades in T-cells. Modulates the expression of interleukin-2 (IL-2). Involved in platelet activation. Prevents the degradation of SKAP1 and SKAP2. {ECO:0000250, ECO:0000269|PubMed:10497204, ECO:0000269|PubMed:17003372, ECO:0000269|PubMed:9207119}. PTM: T-cell receptor ligation leads to increased tyrosine phosphorylation. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell junction {ECO:0000269|PubMed:21881001}. Note=Colocalizes with TMEM47 at cell-cell contacts in podocytes. {ECO:0000269|PubMed:21881001}. SUBUNIT: Interacts with FYN, LCP2, SKAP1 and SKAP2. Part of a complex consisting of SKAP2, FYB1 and PTPNS1. Part of a complex consisting of SKAP2, FYB1 and LILRB3. Interacts with FASLG. Interacts with EVL (By similarity). Interacts with TMEM47 (PubMed:21881001). Interacts with LCK (By similarity). {ECO:0000250|UniProtKB:O15117, ECO:0000269|PubMed:21881001}. TISSUE SPECIFICITY: Expressed in hematopoietic tissues such as myeloid and T-cells, spleen and thymus. Not expressed in B-cells, nor in non-lymphoid tissues. FYB-130 is preferentially expressed in mature T-cells compared to FYB-120, whereas thymocytes showed a greater relative amount of FYB-120. Expressed in podocytes. {ECO:0000269|PubMed:21881001}. +P56959 FUS_MOUSE RNA-binding protein FUS (Protein pigpen) 518 52,673 Chain (1); Compositional bias (3); Cross-link (1); Domain (1); Modified residue (31); Zinc finger (1) FUNCTION: DNA/RNA-binding protein that plays a role in various cellular processes such as transcription regulation, RNA splicing, RNA transport, DNA repair and damage response. Binds to nascent pre-mRNAs and acts as a molecular mediator between RNA polymerase II and U1 small nuclear ribonucleoprotein thereby coupling transcription and splicing. Binds also its own pre-mRNA and autoregulates its expression; this autoregulation mechanism is mediated by non-sense-mediated decay. Plays a role in DNA repair mechanisms by promoting D-loop formation and homologous recombination during DNA double-strand break repair (By similarity). In neuronal cells, plays crucial roles in dendritic spine formation and stability, RNA transport, mRNA stability and synaptic homeostasis (PubMed:16317045, PubMed:25968143). {ECO:0000250|UniProtKB:P35637, ECO:0000269|PubMed:16317045, ECO:0000269|PubMed:25968143}. PTM: Phosphorylated in its N-terminal serine residues upon induced DNA damage. ATM and DNA-PK are able to phosphorylate FUS N-terminal region. {ECO:0000250|UniProtKB:P35637}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P35637}. Note=Displays a punctate pattern inside the nucleus and is excluded from nucleoli. {ECO:0000250|UniProtKB:P35637}. SUBUNIT: Self-oligomerizes (via N-terminal region). Oligomerization is essential for chromatin binding. Component of nuclear riboprotein complexes. Interacts with ILF3, TDRD3 and SF1. Interacts through its C-terminus with SFRS13A. Interacts with OTUB1 and SARNP. Interacts with LRSAM1. Interacts with SAFB1 in a DNA-dependent manner; this interaction tethers FUS to chromatin. Interacts with MATR3. Interacts with SNRNP70 and POLR2A; these interactions couple RNA transcription and splicing. Interacts (through its RNA-binding domain) with RALY (through its RNA-binding domain); both are components of the same RNPs. {ECO:0000250|UniProtKB:P35637}. +A2A995 FYB2_MOUSE FYN-binding protein 2 (Activation-dependent, raft-recruited ADAP-like phosphoprotein) 729 82,296 Chain (1); Compositional bias (3); Domain (1); Modified residue (2); Motif (1); Sequence conflict (1) FUNCTION: Adapter protein that plays a role in T-cell receptor (TCR)-mediated activation of signaling pathways. Required for T-cell activation and integrin-mediated T-cell adhesion in response to TCR stimulation. {ECO:0000250|UniProtKB:Q5VWT5}. PTM: Phosphorylation is required for its function in T-cell activation. {ECO:0000250|UniProtKB:Q5VWT5}. SUBCELLULAR LOCATION: Membrane raft {ECO:0000250|UniProtKB:Q5VWT5}. Note=Recruited to membrane rafts and immunological synapse after TCR stimulation. {ECO:0000250|UniProtKB:Q5VWT5}. SUBUNIT: Interacts with SKAP1, LCK and FYN. The phosphorylated form interacts with LCP2. {ECO:0000250|UniProtKB:Q5VWT5}. +Q8BFZ4 FXL21_MOUSE F-box/LRR-repeat protein 21 (F-box and leucine-rich repeat protein 21) (F-box and leucine-rich repeat protein 3B) (F-box/LRR-repeat protein 3B) 434 49,154 Alternative sequence (2); Chain (1); Domain (1); Erroneous initiation (1); Mutagenesis (1); Repeat (6) Protein modification; protein ubiquitination. FUNCTION: Substrate-recognition component of the SCF(FBXL21) E3 ubiquitin ligase complex involved in circadian rhythm function. Plays a key role in the maintenance of both the speed and the robustness of the circadian clock oscillation. The SCF(FBXL21) complex mainly acts in the cytosol and mediates ubiquitination of CRY proteins (CRY1 and CRY2), leading to CRY proteins stabilization. The SCF(FBXL21) complex counteracts the activity of the SCF(FBXL3) complex and protects CRY proteins from degradation. Involved in the hypothalamic suprachiasmatic nucleus (SCN) clock regulating temporal organization of the daily activities. {ECO:0000269|PubMed:18953409, ECO:0000269|PubMed:23452855, ECO:0000269|PubMed:23452856}. SUBCELLULAR LOCATION: Cytoplasm, cytosol. Nucleus. Note=Mainly localizes in the cytosol. Present at low level in the nucleus. SUBUNIT: Part of the SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase complex SCF(FBXL21) composed of CUL1, SKP1, RBX1 and FBXL21. Interacts with CRY1 and CRY2. {ECO:0000269|PubMed:18953409, ECO:0000269|PubMed:23452855, ECO:0000269|PubMed:23452856}. TISSUE SPECIFICITY: Expressed in the hypothalamus, especially in the suprachiasmatic nucleus (SCN). Expression is driven by the core-clock. There is a pronounced diurnal and circadian expression rhythms rising rapidly at the start of the day and declining at the onset of the night. {ECO:0000269|PubMed:18953409}. +P70213 FV1_MOUSE Friend virus susceptibility protein 1 459 51,997 Chain (1); Natural variant (3) FUNCTION: Retroviral restriction factor that prevents infection by gammaretroviruses. Acts by interacting with the capsid protein ca after entry of the virus into the cell. This interaction presumably disrupt the capsid thereby inactivating the viral genome, making it unable to enter host nucleus and integrate into host genome. {ECO:0000269|PubMed:16474118}. +Q80WP8 GADL1_MOUSE Acidic amino acid decarboxylase GADL1 (Aspartate 1-decarboxylase) (ADC) (EC 4.1.1.11) (Cysteine sulfinic acid decarboxylase) (CSADC) (EC 4.1.1.29) (Glutamate decarboxylase-like protein 1) 550 62,519 Alternative sequence (1); Chain (1); Modified residue (1); Sequence conflict (1) FUNCTION: Catalyzes the decarboxylation of L-aspartate, 3-sulfino-L-alanine (cysteine sulfinic acid), and L-cysteate to beta-alanine, hypotaurine and taurine, respectively. The preferred substrate is L-aspartate. Does not exhibit any decarboxylation activity toward glutamate. {ECO:0000269|PubMed:26327310}. SUBUNIT: Homodimer. {ECO:0000269|PubMed:26327310, ECO:0000269|PubMed:29372909}. TISSUE SPECIFICITY: Expressed in skeletal muscles and kidney (at protein level). Expressed in skeletal muscle and weakly in brain. Not expressed in liver or kidney. Expressed in brain, olfactory bulb, liver, muscle and kidney with the highest expression in olfactory bulb and almost not detected in liver (at protein level) (PubMed:26327310). {ECO:0000269|PubMed:23038267, ECO:0000269|PubMed:26327310}. +Q8C7U7 GALT6_MOUSE Polypeptide N-acetylgalactosaminyltransferase 6 (EC 2.4.1.41) (Polypeptide GalNAc transferase 6) (GalNAc-T6) (pp-GaNTase 6) (Protein-UDP acetylgalactosaminyltransferase 6) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 6) 622 71,537 Binding site (4); Chain (1); Disulfide bond (5); Domain (1); Frameshift (1); Glycosylation (2); Metal binding (3); Region (2); Sequence conflict (11); Topological domain (2); Transmembrane (1) TRANSMEM 9 28 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 8 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 29 622 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. May participate in synthesis of oncofetal fibronectin. Has activity toward Muc1a, Muc2, EA2 and fibronectin peptides (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. DOMAIN: There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding. {ECO:0000250}.; DOMAIN: The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity. {ECO:0000250}. +P54818 GALC_MOUSE Galactocerebrosidase (GALCERase) (EC 3.2.1.46) (Galactocerebroside beta-galactosidase) (Galactosylceramidase) (Galactosylceramide beta-galactosidase) 684 77,256 Active site (2); Beta strand (41); Binding site (4); Chain (1); Disulfide bond (1); Erroneous initiation (3); Glycosylation (6); Helix (13); Sequence conflict (1); Signal peptide (1); Turn (6) FUNCTION: Hydrolyzes the galactose ester bonds of galactosylceramide, galactosylsphingosine, lactosylceramide, and monogalactosyldiglyceride. Enzyme with very low activity responsible for the lysosomal catabolism of galactosylceramide, a major lipid in myelin, kidney and epithelial cells of small intestine and colon. {ECO:0000269|PubMed:8769874}. SUBCELLULAR LOCATION: Lysosome {ECO:0000250}. TISSUE SPECIFICITY: Detected in brain and kidney. {ECO:0000269|PubMed:8769874}. DISEASE: Note=Defects in Galc are the cause of the 'twitcher' phenotype; an autosomal recessive leukodystrophy similar to the human disease (Krabbe disease). This deficiency results in the insufficient catabolism of several galactolipids that are important in the production of normal myelin. +Q8BHN3 GANAB_MOUSE Neutral alpha-glucosidase AB (EC 3.2.1.84) (Alpha-glucosidase 2) (Glucosidase II subunit alpha) 944 106,911 Active site (2); Alternative sequence (2); Beta strand (52); Binding site (4); Chain (1); Disulfide bond (2); Erroneous initiation (1); Glycosylation (1); Helix (25); Modified residue (1); Mutagenesis (3); Sequence conflict (1); Signal peptide (1); Turn (10) Glycan metabolism; N-glycan metabolism. FUNCTION: Catalytic subunit of glucosidase II that cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature glycoproteins (PubMed:27462106). Required for PKD1/Polycystin-1 and PKD2/Polycystin-2 maturation and localization to the cell surface and cilia (PubMed:28375157). {ECO:0000269|PubMed:27462106, ECO:0000269|PubMed:28375157}. SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:Q14697}. Golgi apparatus {ECO:0000250|UniProtKB:P79403}. Melanosome {ECO:0000250|UniProtKB:Q14697}. SUBUNIT: Heterodimer of a catalytic alpha subunit (GANAB) and a beta subunit (PRKCSH) (PubMed:9148925, PubMed:10921916, PubMed:27462106). Binds glycosylated PTPRC (PubMed:9148925, PubMed:10921916). {ECO:0000269|PubMed:10921916, ECO:0000269|PubMed:27462106, ECO:0000269|PubMed:9148925}. +P23772 GATA3_MOUSE Trans-acting T-cell-specific transcription factor GATA-3 (GATA-binding factor 3) 443 47,968 Beta strand (2); Chain (1); Compositional bias (2); Helix (2); Modified residue (2); Motif (1); Mutagenesis (5); Region (2); Turn (1); Zinc finger (2) FUNCTION: Transcriptional activator which binds to the enhancer of the T-cell receptor alpha and delta genes. Binds to the consensus sequence 5'-AGATAG-3'. Required for the T-helper 2 (Th2) differentiation process following immune and inflammatory responses. {ECO:0000269|PubMed:17056504}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15662016}. SUBUNIT: Interacts with TBX21 ('Tyr-525' phosphorylated form). {ECO:0000269|PubMed:15662016, ECO:0000269|PubMed:21690296, ECO:0000269|PubMed:23616576}. DOMAIN: Binds DNA via the 2 GATA-type zinc fingers. Each zinc finger may bind either adjacent sites in a palindromic motif, or a different DNA molecule allowing looping and long-range gene regulation (By similarity). {ECO:0000250}.; DOMAIN: The YxKxHxxxRP motif is critical for DNA-binding and function. {ECO:0000269|PubMed:18621058}. TISSUE SPECIFICITY: T-cell specific. +Q8BUY8 GASP2_MOUSE G-protein coupled receptor-associated sorting protein 2 (GASP-2) 826 92,802 Chain (1); Modified residue (2) FUNCTION: May play a role in regulation of a variety of G-protein coupled receptors. {ECO:0000250}. SUBUNIT: Interacts with cytoplasmic tails of a variety of G-protein coupled receptors such as muscarinic acetylcholine receptor M1/CHRM1 and calcitonin receptor/CALCR. {ECO:0000250}. +P48757 GAST_MOUSE Gastrin [Cleaved into: Gastrin-71 (G71); Big gastrin (Gastrin-34) (G34); Gastrin] 101 11,590 Modified residue (3); Peptide (3); Propeptide (1); Sequence conflict (7); Signal peptide (1) FUNCTION: Gastrin stimulates the stomach mucosa to produce and secrete hydrochloric acid and the pancreas to secrete its digestive enzymes. It also stimulates smooth muscle contraction and increases blood circulation and water secretion in the stomach and intestine. PTM: Sulfation enhances proteolytic processing, and blocks peptide degradation. Levels of sulfation differ between proteolytically-cleaved gastrins and between tissues (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Abundantly expressed in the stomach and duodenum. Low levels in brain, ovary and pancreas. {ECO:0000269|PubMed:8647266}. +O08912 GALT1_MOUSE Polypeptide N-acetylgalactosaminyltransferase 1 (EC 2.4.1.41) (Polypeptide GalNAc transferase 1) (GalNAc-T1) (pp-GaNTase 1) (Protein-UDP acetylgalactosaminyltransferase 1) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1) [Cleaved into: Polypeptide N-acetylgalactosaminyltransferase 1 soluble form] 559 64,255 Beta strand (25); Binding site (5); Chain (2); Disulfide bond (5); Domain (1); Glycosylation (2); Helix (19); Metal binding (3); Mutagenesis (24); Region (2); Sequence conflict (1); Topological domain (2); Transmembrane (1); Turn (3) TRANSMEM 10 28 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 9 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 29 559 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b and Muc7. {ECO:0000269|PubMed:9153242}. SUBCELLULAR LOCATION: Polypeptide N-acetylgalactosaminyltransferase 1: Golgi apparatus, Golgi stack membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: Polypeptide N-acetylgalactosaminyltransferase 1 soluble form: Secreted {ECO:0000250}. DOMAIN: There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding. {ECO:0000269|PubMed:10037781}.; DOMAIN: The ricin B-type lectin domain directs the glycopeptide specificity. It is required in the glycopeptide specificity of enzyme activity but not for activity with naked peptide substrates, suggesting that it triggers the catalytic domain to act on GalNAc-glycopeptide substrates (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed at high level. Higher expression in kidney, heart, small intestine and cervix and to a lesser extent in all the other tissues tested. {ECO:0000269|PubMed:12651884, ECO:0000269|PubMed:9153242}. +O08832 GALT4_MOUSE Polypeptide N-acetylgalactosaminyltransferase 4 (EC 2.4.1.41) (Polypeptide GalNAc transferase 4) (GalNAc-T4) (pp-GaNTase 4) (Protein-UDP acetylgalactosaminyltransferase 4) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 4) 578 66,555 Binding site (4); Chain (1); Disulfide bond (5); Domain (1); Glycosylation (1); Metal binding (3); Region (2); Site (3); Topological domain (2); Transmembrane (1) TRANSMEM 13 35 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 12 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 36 578 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has a highest activity toward EA2 peptide substrate and a much lower activity with EPO-T, Muc2, Muc1a, Muc1b. {ECO:0000269|PubMed:9153242}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. DOMAIN: There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding. {ECO:0000250}.; DOMAIN: The ricin B-type lectin domain directs the glycopeptide specificity. It is required in the glycopeptide specificity of enzyme activity but not for activity with naked peptide substrates, suggesting that it triggers the catalytic domain to act on GalNAc-glycopeptide substrates. {ECO:0000250|UniProtKB:Q8N4A0}. TISSUE SPECIFICITY: Highly expressed in sublingual gland, stomach, colon, small intestine and cervix. Expressed at intermediate levels in kidney, ovary, lung and uterus. Weakly expressed in spleen, liver, heart and brain. Not expressed in submandibular and parotid glands, skeletal muscle and testis. {ECO:0000269|PubMed:9153242}. +Q9D6F4 GBRA4_MOUSE Gamma-aminobutyric acid receptor subunit alpha-4 (GABA(A) receptor subunit alpha-4) 552 60,878 Chain (1); Disulfide bond (1); Glycosylation (3); Signal peptide (1); Topological domain (2); Transmembrane (4) TRANSMEM 259 280 Helical. {ECO:0000305}.; TRANSMEM 285 306 Helical. {ECO:0000305}.; TRANSMEM 318 340 Helical. {ECO:0000305}.; TRANSMEM 522 541 Helical. {ECO:0000305}. TOPO_DOM 36 258 Extracellular. {ECO:0000305}.; TOPO_DOM 341 521 Cytoplasmic. {ECO:0000305}. FUNCTION: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. SUBUNIT: Generally pentameric. There are five types of GABA(A) receptor chains: alpha, beta, gamma, delta, and rho. +P60521 GBRL2_MOUSE Gamma-aminobutyric acid receptor-associated protein-like 2 (GABA(A) receptor-associated protein-like 2) (Golgi-associated ATPase enhancer of 16 kDa) (GATE-16) 117 13,667 Chain (1); Lipidation (1); Modified residue (2); Propeptide (1); Region (2); Sequence conflict (1); Site (1) FUNCTION: Ubiquitin-like modifier involved in intra-Golgi traffic. Modulates intra-Golgi transport through coupling between NSF activity and SNAREs activation. It first stimulates the ATPase activity of NSF which in turn stimulates the association with GOSR1 (By similarity). Involved in autophagy. Plays a role in mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Whereas LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation. {ECO:0000250}. PTM: The precursor molecule is cleaved by ATG4B to form the cytosolic form, GABARAPL2-I. This is activated by APG7L/ATG7, transferred to ATG3 and conjugated to phospholipid to form the membrane-bound form, GABARAPL2-II. ATG4B also mediates the delipidation required for GABARAPL1 recycling when autophagosomes fuse with lysosomes. {ECO:0000269|PubMed:14530254}. SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250}. Cytoplasmic vesicle, autophagosome {ECO:0000250}. SUBUNIT: Monomer. Interacts with GABRG2, NSF, GOSR1 and beta-tubulin. Interacts with ATG3, ATG13 and ULK1. Interacts with TP53INP1 and TP53INP2. Interacts with TBC1D25 and ATG7. Directly interacts with SQSTM1 and BNIP3. Interacts with TECPR2 and PCM1. Interacts with TBC1D5. Interacts with TRIM5. Interacts with MEFV and TRIM21. Interacts with WDFY3. {ECO:0000250|UniProtKB:P60520}. TISSUE SPECIFICITY: Ubiquitous. A high level expression is seen in brain, thymus, lung, heart, liver and kidney. {ECO:0000269|PubMed:11414770}. +P16305 GBRA6_MOUSE Gamma-aminobutyric acid receptor subunit alpha-6 (GABA(A) receptor subunit alpha-6) 453 51,106 Alternative sequence (2); Chain (1); Disulfide bond (1); Glycosylation (3); Modified residue (1); Sequence conflict (7); Signal peptide (1); Topological domain (2); Transmembrane (4) TRANSMEM 243 264 Helical. {ECO:0000305}.; TRANSMEM 269 290 Helical. {ECO:0000305}.; TRANSMEM 301 324 Helical. {ECO:0000305}.; TRANSMEM 420 441 Helical. {ECO:0000305}. TOPO_DOM 20 242 Extracellular. {ECO:0000305}.; TOPO_DOM 325 419 Cytoplasmic. {ECO:0000305}. FUNCTION: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. SUBUNIT: Generally pentameric. There are five types of GABA(A) receptor chains: alpha, beta, gamma, delta, and rho. Binds UBQLN1. TISSUE SPECIFICITY: Only found in cerebellar granule cells. +Q9D4H2 GCC1_MOUSE GRIP and coiled-coil domain-containing protein 1 (Golgi coiled-coil protein 1) 778 87,678 Chain (1); Coiled coil (2); Domain (1); Sequence conflict (1) FUNCTION: Probably involved in maintaining Golgi structure. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. DOMAIN: Extended rod-like protein with coiled-coil domains. +P48031 GBX2_MOUSE Homeobox protein GBX-2 (Gastrulation and brain-specific homeobox protein 2) (Stimulated by retinoic acid gene 7 protein) 348 37,359 Chain (1); Compositional bias (3); DNA binding (1) FUNCTION: May act as a transcription factor for cell pluripotency and differentiation in the embryo. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: Expressed in adult brain, spleen and female genital tract. No expression in heart, liver, lung, kidney, or testis. +P63080 GBRB3_MOUSE Gamma-aminobutyric acid receptor subunit beta-3 (GABA(A) receptor subunit beta-3) 473 54,166 Binding site (1); Chain (1); Disulfide bond (1); Glycosylation (3); Region (3); Signal peptide (1); Topological domain (4); Transmembrane (4) TRANSMEM 246 267 Helical. {ECO:0000250}.; TRANSMEM 271 293 Helical. {ECO:0000250}.; TRANSMEM 305 327 Helical. {ECO:0000250}.; TRANSMEM 451 472 Helical. {ECO:0000250}. TOPO_DOM 26 245 Extracellular. {ECO:0000250}.; TOPO_DOM 268 270 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 294 304 Extracellular. {ECO:0000250}.; TOPO_DOM 328 450 Cytoplasmic. {ECO:0000250}. FUNCTION: Component of the heteropentameric receptor for GABA, the major inhibitory neurotransmitter in the vertebrate brain. Functions also as histamine receptor and mediates cellular responses to histamine. Functions as receptor for diazepines and various anesthetics, such as pentobarbital; these are bound at a separate allosteric effector binding site. Functions as ligand-gated chloride channel. {ECO:0000269|PubMed:10670447, ECO:0000269|PubMed:9108119}. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane {ECO:0000250|UniProtKB:P28472}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:28978485}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P63079}. SUBUNIT: Heteropentamer, formed by a combination of alpha, beta, gamma, delta and rho chains. Can form functional homopentamers (in vitro). Interacts with UBQLN1. May interact with KIF21B. Identified in a complex of 720 kDa composed of LHFPL4, NLGN2, GABRA1, GABRB2, GABRG2 and GABRB3 (By similarity). Interacts with LHFPL4 (PubMed:28978485). {ECO:0000250|UniProtKB:P28472, ECO:0000250|UniProtKB:P63079, ECO:0000269|PubMed:28978485}. +P26049 GBRA3_MOUSE Gamma-aminobutyric acid receptor subunit alpha-3 (GABA(A) receptor subunit alpha-3) 492 55,398 Chain (1); Disulfide bond (1); Glycosylation (4); Modified residue (4); Natural variant (1); Signal peptide (1); Topological domain (2); Transmembrane (4) TRANSMEM 277 298 Helical. {ECO:0000305}.; TRANSMEM 304 325 Helical. {ECO:0000305}.; TRANSMEM 338 359 Helical. {ECO:0000305}.; TRANSMEM 458 479 Helical. {ECO:0000305}. TOPO_DOM 29 276 Extracellular. {ECO:0000305}.; TOPO_DOM 360 457 Cytoplasmic. {ECO:0000305}. FUNCTION: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. SUBUNIT: Generally pentameric. There are five types of GABA(A) receptor chains: alpha, beta, gamma, delta, and rho. Binds UBQLN1 (PubMed:11528422). Interacts with GPHN (By similarity). {ECO:0000250|UniProtKB:P34903, ECO:0000269|PubMed:11528422}. +Q9D1H7 GET4_MOUSE Golgi to ER traffic protein 4 homolog 327 36,525 Alternative sequence (1); Chain (1); Initiator methionine (1); Modified residue (1); Region (1) FUNCTION: As part of a cytosolic protein quality control complex, the BAG6/BAT3 complex, maintains misfolded and hydrophobic patches-containing proteins in a soluble state and participates to their proper delivery to the endoplasmic reticulum or alternatively can promote their sorting to the proteasome where they undergo degradation. The BAG6/BAT3 complex is involved in the post-translational delivery of tail-anchored/type II transmembrane proteins to the endoplasmic reticulum membrane. Recruited to ribosomes, it interacts with the transmembrane region of newly synthesized tail-anchored proteins and together with SGTA and ASNA1 mediates their delivery to the endoplasmic reticulum. Client proteins that cannot be properly delivered to the endoplasmic reticulum are ubiquitinated and sorted to the proteasome. Similarly, the BAG6/BAT3 complex also functions as a sorting platform for proteins of the secretory pathway that are mislocalized to the cytosol either delivering them to the proteasome for degradation or to the endoplasmic reticulum. The BAG6/BAT3 complex also plays a role in the endoplasmic reticulum-associated degradation (ERAD), a quality control mechanism that eliminates unwanted proteins of the endoplasmic reticulum through their retrotranslocation to the cytosol and their targeting to the proteasome. It maintains these retrotranslocated proteins in an unfolded yet soluble state condition in the cytosol to ensure their proper delivery to the proteasome. {ECO:0000250|UniProtKB:Q7L5D6}. PTM: Ubiquitinated by RNF12, leading to proteasomal degradation. When unassembled from BAG6; ubiquitinylation is modulated by BAG6 quality control role and effectuated by RNF126. {ECO:0000250|UniProtKB:Q7L5D6}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q7L5D6}. SUBUNIT: Component of the BAG6/BAT3 complex, at least composed of BAG6, UBL4A and GET4/TRC35. Interacts with BAG6; the interaction is direct and localizes BAG6 in the cytosol. {ECO:0000250|UniProtKB:Q7L5D6}. +Q07235 GDN_MOUSE Glia-derived nexin (GDN) (Peptidase inhibitor 7) (PI-7) (Protease nexin 1) (PN-1) (Protease nexin I) (Serine protease-inhibitor 4) (Serpin E2) 397 44,207 Chain (1); Glycosylation (1); Sequence conflict (1); Signal peptide (1); Site (1) FUNCTION: Serine protease inhibitor with activity toward thrombin, trypsin, and urokinase. Promotes neurite extension by inhibiting thrombin. Binds heparin. SUBCELLULAR LOCATION: Secreted, extracellular space. TISSUE SPECIFICITY: Most abundant in seminal vesicles. +Q9CRY7 GDPD1_MOUSE Lysophospholipase D GDPD1 (EC 3.1.4.39) (Glycerophosphodiester phosphodiesterase 4) (Glycerophosphodiester phosphodiesterase domain-containing protein 1) 314 35,867 Chain (1); Domain (1); Frameshift (1); Metal binding (3); Sequence conflict (2); Topological domain (3); Transmembrane (2) TRANSMEM 4 24 Helical. {ECO:0000255}.; TRANSMEM 196 216 Helical. {ECO:0000255}. TOPO_DOM 1 3 Extracellular. {ECO:0000255}.; TOPO_DOM 25 195 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 217 314 Extracellular. {ECO:0000255}. FUNCTION: Hydrolyzes lysoglycerophospholipids to produce lysophosphatidic acid (LPA) and the corresponding amines (PubMed:25528375, PubMed:25596343). Shows a preference for 1-O-alkyl-sn-glycero-3-phosphocholine (lyso-PAF), lysophosphatidylethanolamine (lyso-PE) and lysophosphatidylcholine (lyso-PC) (PubMed:25528375, PubMed:25596343). May be involved in bioactive N-acylethanolamine biosynthesis (PubMed:25596343). Does not display glycerophosphodiester phosphodiesterase activity, since it cannot hydrolyze either glycerophosphoinositol or glycerophosphocholine (PubMed:25528375). {ECO:0000269|PubMed:25528375, ECO:0000269|PubMed:25596343}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:25528375}. TISSUE SPECIFICITY: Widely expressed (PubMed:25528375, PubMed:25596343). {ECO:0000269|PubMed:25528375, ECO:0000269|PubMed:25596343}. +Q8BMI4 GEN_MOUSE Flap endonuclease GEN homolog 1 (EC 3.1.-.-) 908 101,779 Alternative sequence (1); Chain (1); Metal binding (7); Modified residue (2); Region (4); Sequence conflict (2) FUNCTION: Endonuclease which resolves Holliday junctions (HJs) by the introduction of symmetrically related cuts across the junction point, to produce nicked duplex products in which the nicks can be readily ligated. Four-way DNA intermediates, also known as Holliday junctions, are formed during homologous recombination and DNA repair, and their resolution is necessary for proper chromosome segregation. Cleaves HJs by a nick and counter-nick mechanism involving dual coordinated incisions that lead to the formation of ligatable nicked duplex products. Cleavage of the first strand is rate limiting, while second strand cleavage is rapid. Largely monomeric, dimerizes on the HJ and the first nick occurs upon dimerization at the junction. Efficiently cleaves both single and double HJs contained within large recombination intermediates. Exhibits a weak sequence preference for incision between two G residues that reside in a T-rich region of DNA. Has also endonuclease activity on 5'-flap and replication fork (RF) DNA substrates. {ECO:0000250|UniProtKB:Q17RS7}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q17RS7}. SUBUNIT: Largely monomeric, dimerizes on the Holliday junction and the first nick occurs upon dimerization at the junction. {ECO:0000250|UniProtKB:Q17RS7}. DOMAIN: XPG-N, XPG-I,5'-3' exonuclease domains interact with DNA. Contains a chromodomain that acts as additional DNA interaction site and is required for efficient DNA recognition and cleavage. {ECO:0000250|UniProtKB:Q17RS7}. TISSUE SPECIFICITY: Expressed in bone marrow and testis and to a lesser extent in thymus, spleen, brain and colon. {ECO:0000269|PubMed:27010503}. +Q6Y7W8 GGYF2_MOUSE GRB10-interacting GYF protein 2 (PERQ amino acid-rich with GYF domain-containing protein 2) (Trinucleotide repeat-containing gene 15 protein) 1291 149,193 Alternative sequence (1); Chain (1); Compositional bias (5); Cross-link (1); Domain (1); Initiator methionine (1); Modified residue (16); Region (1); Sequence conflict (2) FUNCTION: Key component of the 4EHP-GYF2 complex, a multiprotein complex that acts as a repressor of translation initiation (PubMed:26763119). In 4EHP-GYF2 the complex, acts as a factor that bridges EIF4E2 to ZFP36/TTP, linking translation repression with mRNA decay (PubMed:26763119). May act cooperatively with GRB10 to regulate tyrosine kinase receptor signaling, including IGF1 and insulin receptors (PubMed:12771153). {ECO:0000269|PubMed:12771153, ECO:0000269|PubMed:26763119}. SUBUNIT: Component of the 4EHP-GYF2 complex, at least composed of EIF4E2, GIGYF2 and ZNF598 (PubMed:26763119). Interacts (via the 4EHP-binding motif) with EIF4E2; the interaction is direct (By similarity). Interacts with ZFP36/TTP (via P-P-P-P-G repeats); the interaction is direct (PubMed:26763119). Interacts with GRB10 (PubMed:12771153). {ECO:0000250|UniProtKB:Q6Y7W6, ECO:0000269|PubMed:12771153, ECO:0000269|PubMed:26763119}. TISSUE SPECIFICITY: Expressed in heart, liver, kidney and brain as well as in testis (PubMed:12771153). {ECO:0000269|PubMed:12771153}. +Q3TLS3 GDPP1_MOUSE GDP-D-glucose phosphorylase 1 (EC 2.7.7.78) 386 42,515 Active site (1); Chain (1); Frameshift (1); Sequence conflict (7) FUNCTION: Specific and highly efficient GDP-D-glucose phosphorylase regulating the levels of GDP-D-glucose in cells. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in the nervous and male reproductive systems compared to kidney, liver and heart. {ECO:0000269|PubMed:21507950}. +Q6SJE0 GFRAL_MOUSE GDNF family receptor alpha-like 393 43,964 Alternative sequence (2); Chain (1); Disulfide bond (11); Glycosylation (4); Region (1); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 350 370 Helical. {ECO:0000255}. TOPO_DOM 20 349 Extracellular. {ECO:0000255}.; TOPO_DOM 371 393 Cytoplasmic. {ECO:0000255}. FUNCTION: Brainstem-restricted receptor for GDF15 which regulates food intake, energy expenditure and body weight in response to metabolic and toxin-induced stresses (PubMed:28953886, PubMed:28846099, PubMed:28846097, PubMed:28846098). Upon interaction with its ligand, GDF15, interacts with RET and induces cellular signaling through activation of MAPK- and AKT- signaling pathways (PubMed:28846098, PubMed:28846099). {ECO:0000269|PubMed:28846097, ECO:0000269|PubMed:28846098, ECO:0000269|PubMed:28846099, ECO:0000269|PubMed:28953886}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}; Extracellular side {ECO:0000305}. SUBUNIT: Interacts (via the extracellular domain) with GDF15 and RET; receptor of GDF15, mediates cellular signaling through interaction with RET after GDF15-binding (PubMed:28846098, PubMed:28846099). Interaction with RET requires previous GDF15-binding (PubMed:28846099). {ECO:0000269|PubMed:28846098, ECO:0000269|PubMed:28846099}. TISSUE SPECIFICITY: Expressed in the brainstem, restricted to cells in the area postrema and the immediately adjacent region of the nucleus tractus solitarius. {ECO:0000269|PubMed:28846097, ECO:0000269|PubMed:28846099, ECO:0000269|PubMed:28953886}. +Q9Z2A9 GGT5_MOUSE Glutathione hydrolase 5 proenzyme (EC 3.4.19.13) (Gamma-glutamyl leukotrienase) (GGL) (Gamma-glutamyltransferase 5) (GGT 5) (EC 2.3.2.2) (Gamma-glutamyltransferase-like activity 1) (Gamma-glutamyltranspeptidase 5) (Leukotriene-C4 hydrolase) (EC 3.4.19.14) [Cleaved into: Glutathione hydrolase 5 heavy chain; Glutathione hydrolase 5 light chain] 573 61,674 Active site (1); Alternative sequence (2); Binding site (3); Chain (2); Glycosylation (7); Region (1); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 9 29 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 8 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 30 573 Extracellular. {ECO:0000255}. Sulfur metabolism; glutathione metabolism. Lipid metabolism; leukotriene D4 biosynthesis. FUNCTION: Cleaves the gamma-glutamyl peptide bond of glutathione conjugates, but maybe not glutathione itself. Converts leukotriene C4 (LTC4) to leukotriene D4 (LTD4). PTM: Cleaved by autocatalysis into a large and a small subunit. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. SUBUNIT: Heterodimer composed of the light and heavy chains. The active site is located in the light chain (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Very low level of expression. Detected in spleen lymphocytes, medullary and paracortical thymic lymphocytes, lung interstitial cells, bronchial epithelium, proximal tubules in kidney, crypt cells in small intestine, neurons in brain stem and cerebral cortex and in Purkinje cells. +Q9Z0L8 GGH_MOUSE Gamma-glutamyl hydrolase (EC 3.4.19.9) (Conjugase) (FGPH) (Folylpolyglutamate hydrolase) (GH) (Gamma-Glu-x carboxypeptidase) 317 35,470 Active site (2); Alternative sequence (1); Chain (1); Domain (1); Glycosylation (5); Sequence conflict (12); Signal peptide (1) FUNCTION: Hydrolyzes the polyglutamate sidechains of pteroylpolyglutamates. Progressively removes gamma-glutamyl residues from pteroylpoly-gamma-glutamate to yield pteroyl-alpha-glutamate (folic acid) and free glutamate. May play an important role in the bioavailability of dietary pteroylpolyglutamates and in the metabolism of pteroylpolyglutamates and antifolates. Acts as endopeptidase. Lysosomal enzyme is activated by sulfhydryl compounds. SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250|UniProtKB:Q92820}. Lysosome {ECO:0000250|UniProtKB:Q92820}. Melanosome {ECO:0000250|UniProtKB:Q92820}. Note=While its intracellular location is primarily the lysosome, most of the enzyme activity is secreted. {ECO:0000250|UniProtKB:Q92820}. SUBUNIT: Homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Isoform I (more expressed than isoform II in all tissues) is highly expressed in salivary gland, followed by kidney, liver, lung, stomach and uterus, and weakly expressed in small intestine, brain and fetal liver. Also expressed at a lower level in thymus, spleen and skeletal muscle. Also expressed in tumors. +Q8BMI3 GGA3_MOUSE ADP-ribosylation factor-binding protein GGA3 (Golgi-localized, gamma ear-containing, ARF-binding protein 3) 718 77,973 Chain (1); Compositional bias (1); Domain (3); Erroneous initiation (1); Modified residue (2); Motif (1); Region (1); Sequence conflict (2) FUNCTION: Plays a role in protein sorting and trafficking between the trans-Golgi network (TGN) and endosomes. Mediates the ARF-dependent recruitment of clathrin to the TGN and binds ubiquitinated proteins and membrane cargo molecules with a cytosolic acidic cluster-dileucine (DXXLL) motif (By similarity). {ECO:0000250}.; FUNCTION: Plays a role in protein sorting and trafficking between the trans-Golgi network (TGN) and endosomes. Mediates the ARF-dependent recruitment of clathrin to the TGN and binds ubiquitinated proteins and membrane cargo molecules with a cytosolic acidic cluster-dileucine (DXXLL) motif. Mediates export of the GPCR receptor ADRA2B to the cell surface. Involved in BACE1 transport and sorting as well as regulation of BACE1 protein levels. Regulates retrograde transport of BACE1 from endosomes to the trans-Golgi network via interaction through the VHS motif and dependent of BACE1 phosphorylation. Modulates BACE1 protein levels intedepently of the interaction between VHS domain and DXXLL motif through recognition of ubiquitination (By similarity). Key player in a novel DXXLL-mediated endosomal sorting machinery to the recycling pathway that targets NTRK1 to the plasma membrane (By similarity). {ECO:0000250|UniProtKB:A0A0G2JV04, ECO:0000250|UniProtKB:Q9NZ52}. PTM: Phosphorylated by CK2 and dephosphorylated by PP2A. Phosphorylation of GGA3 allows the internal DXXLL motif to bind the VHS domain and to inhibit the recognition of cargo signals (By similarity). {ECO:0000250}.; PTM: Ubiquitinated. {ECO:0000250}.; PTM: Proteolytically cleaved during apoptosis by CASP3. {ECO:0000250|UniProtKB:Q9NZ52}. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q9NZ52}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9NZ52}. Endosome membrane {ECO:0000250|UniProtKB:Q9NZ52}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9NZ52}. Early endosome membrane {ECO:0000250|UniProtKB:A0A0G2JV04}; Peripheral membrane protein {ECO:0000305}. Recycling endosome membrane {ECO:0000250|UniProtKB:A0A0G2JV04}; Peripheral membrane protein {ECO:0000305}. SUBUNIT: Monomer. Interacts with GGA1 and GGA2 (By similarity). Binds to clathrin and activated ARFs, such as ARF1, ARF5 and ARF6 (PubMed:11950392). Binds RABEP1 and RABGEF1. Interacts with the membrane proteins M6PR/CD-MPR and IGF2R/CI-MPR and the accessory proteins SYNRG, EPN4, NECAP1, NECAP2 and AFTPH/aftiphilin. Interacts with TSG101 and UBC. Interacts with ADRA2B. Interacts with NTRK1; the interaction is independent of NTRK1 activation and ubiquitination. Interacts (via VHS domain) with BACE1 (via DXXLL motif) (By similarity). {ECO:0000250|UniProtKB:A0A0G2JV04, ECO:0000250|UniProtKB:Q9NZ52, ECO:0000269|PubMed:11950392}. DOMAIN: The VHS domain functions as a recognition module for sorting signals composed of an acidic cluster followed by two leucines (DXXLL motif). {ECO:0000250}.; DOMAIN: The GAT domain is responsible for interaction with ARF-GTP, UBC and RABEP1. Required for recruitment to the TGN it prevents ARF-GTP hydrolysis (By similarity). {ECO:0000250}.; DOMAIN: The unstructured hinge region contains clathrin-binding and an autoinhibitory (DXXLL) motifs. {ECO:0000250}.; DOMAIN: The GAE domain binds accessory proteins regulating GGAs function. {ECO:0000250}. +Q9Z2H7 GIPC2_MOUSE PDZ domain-containing protein GIPC2 (SemaF cytoplasmic domain-associated protein 2) (SEMCAP-2) 314 34,118 Chain (1); Domain (1); Sequence conflict (1) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. SUBUNIT: Probably interacts with SEMA5A. {ECO:0000269|PubMed:10318831}. TISSUE SPECIFICITY: Expressed in kidney and lung (at protein level). {ECO:0000269|PubMed:10318831}. +Q8BX17 GEMI5_MOUSE Gem-associated protein 5 (Gemin5) 1502 166,592 Chain (1); Coiled coil (1); Compositional bias (1); Cross-link (1); Modified residue (6); Region (2); Repeat (13); Sequence conflict (1); Site (14) FUNCTION: Required for the assembly of the SMN complex that plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus. GEMIN5 acts as the snRNA-binding protein of the SMN complex. Binds to the 7-methylguanosine cap of RNA molecules (By similarity). Binds to the 3'-UTR of SMN1 mRNA and regulates its translation; does not affect mRNA stability (PubMed:25911097). May play a role in the regulation of protein synthesis via its interaction with ribosomes (By similarity). {ECO:0000250|UniProtKB:Q8TEQ6, ECO:0000269|PubMed:25911097}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q8TEQ6}. Nucleus, gem {ECO:0000250|UniProtKB:Q8TEQ6}. Cytoplasm {ECO:0000250|UniProtKB:Q8TEQ6}. Note=Found both in the nucleoplasm and in nuclear bodies called gems (Gemini of Cajal bodies) that are often in proximity to Cajal (coiled) bodies. Also found in the cytoplasm. {ECO:0000250|UniProtKB:Q8TEQ6}. SUBUNIT: Part of the core SMN complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8 and STRAP/UNRIP. Part of the SMN-Sm complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8, STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG. Interacts directly with SMN1, SNRPB, SNRPD1, SNRPD2, SNRPD3 and SNRPE. Identified in a SMN complex that contains GEMIN2/SIP1. Interacts with cytosolic DDX20/GEMIN3 and GEMIN4. Interacts with SNRNP70 and HNRNPU. Identified in a complex with 80S ribosomes; binds to the 60S large ribosomal subunit. Interacts with the ribosomal subunits RPL3 and RPL4. {ECO:0000250|UniProtKB:Q8TEQ6}. DOMAIN: The WD repeat domain mediates binding to U1 snRNA and to U4 snRNA. The WD repeat domain also mediates binding to the 7-methylguanosine cap that is found both on mRNA and snRNA molecules. The regions that bind snRNA molecules and the isolated 7-methylguanosine cap overlap at least partially. Besides, the WD repeat domain mediates interaction with the 60S large ribosomal subunit. {ECO:0000250|UniProtKB:Q8TEQ6}. +Q91WG8 GLCNE_MOUSE Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (UDP-GlcNAc-2-epimerase/ManAc kinase) [Includes: UDP-N-acetylglucosamine 2-epimerase (hydrolyzing) (EC 3.2.1.183) (UDP-GlcNAc-2-epimerase) (Uridine diphosphate-N-acetylglucosamine-2-epimerase); N-acetylmannosamine kinase (EC 2.7.1.60) (ManAc kinase)] 722 79,199 Active site (1); Binding site (6); Chain (1); Metal binding (4); Nucleotide binding (2); Region (2); Sequence conflict (2) Amino-sugar metabolism; N-acetylneuraminate biosynthesis. FUNCTION: Regulates and initiates biosynthesis of N-acetylneuraminic acid (NeuAc), a precursor of sialic acids. Required for normal sialylation in hematopoietic cells (By similarity). Sialylation is implicated in cell adhesion, signal transduction, tumorigenicity and metastatic behavior of malignant cells. Plays an essential role in early development. {ECO:0000250, ECO:0000269|PubMed:11929971}. PTM: Phosphorylated by PKC. {ECO:0000269|PubMed:10745088}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homodimer and homohexamer. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. Highest expression in liver. Also found at high levels in lung, brain and kidney. {ECO:0000269|PubMed:10103025}. +P63073 IF4E_MOUSE Eukaryotic translation initiation factor 4E (eIF-4E) (eIF4E) (mRNA cap-binding protein) (eIF-4F 25 kDa subunit) 217 25,053 Beta strand (10); Chain (1); Helix (9); Initiator methionine (1); Modified residue (3); Mutagenesis (1); Region (7); Sequence conflict (1); Turn (3) FUNCTION: Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures. May play an important role in spermatogenesis through translational regulation of stage-specific mRNAs during germ cell development (By similarity). Its translation stimulation activity is repressed by binding to the complex CYFIP1-FMR1. Component of the CYFIP1-EIF4E-FMR1 complex which binds to the mRNA cap and mediates translational repression. In the CYFIP1-EIF4E-FMR1 complex this subunit mediates the binding to the mRNA cap. {ECO:0000250, ECO:0000269|PubMed:18805096}. PTM: Phosphorylation increases the ability of the protein to bind to mRNA caps and to form the eIF4F complex. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:22900038}. SUBUNIT: eIF4F is a multi-subunit complex, the composition of which varies with external and internal environmental conditions. It is composed of at least EIF4A, EIF4E and EIF4G1/EIF4G3. EIF4E is also known to interact with other partners. The interaction with EIF4ENIF1 mediates the import into the nucleus. Hypophosphorylated EIF4EBP1, EIF4EBP2 and EIF4EBP3 compete with EIF4G1/EIF4G3 to interact with EIF4E; insulin stimulated MAP-kinase (MAPK1 and MAPK3) phosphorylation of EIF4EBP1 causes dissociation of the complex allowing EIF4G1/EIF4G3 to bind and consequent initiation of translation. Rapamycin can attenuate insulin stimulation, mediated by FKBPs. Interacts mutually exclusive with EIF4A1 or EIF4A2. Binds to MKNK2 in nucleus (By similarity). Interacts with NGDN and PIWIL2. Component of the CYFIP1-EIF4E-FMR1 complex composed of CYFIP, EIF4E and FMR1. Interacts directly with CYFIP1. Interacts with LIMD1, WTIP and AJUBA (By similarity). Interacts with APOBEC3G in an RNA-dependent manner. Interacts with LARP1 (By similarity). Interacts with CLOCK. Interacts with METTL3 (By similarity). Interacts with RBM24; this interaction prevents EIF4E from binding to p53/TP53 mRNA and inhibits the assembly of translation initiation complex (By similarity). {ECO:0000250|UniProtKB:P06730, ECO:0000269|PubMed:10394359, ECO:0000269|PubMed:16705177, ECO:0000269|PubMed:18805096, ECO:0000269|PubMed:19114715, ECO:0000269|PubMed:22900038, ECO:0000269|PubMed:9200613}. +Q6NZJ6 IF4G1_MOUSE Eukaryotic translation initiation factor 4 gamma 1 (eIF-4-gamma 1) (eIF-4G 1) (eIF-4G1) 1600 176,077 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (3); Modified residue (26); Region (5) FUNCTION: Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome. {ECO:0000250}. PTM: Phosphorylated at multiple sites in vivo. Phosphorylation at Ser-1187 by PRKCA induces binding to MKNK1 (By similarity). {ECO:0000250}. SUBUNIT: eIF4F is a multi-subunit complex, the composition of which varies with external and internal environmental conditions. It is composed of at least EIF4A, EIF4E and EIF4G1/EIF4G3. Interacts with eIF3, mutually exclusive with EIF4A1 or EIFA2, EIF4E and through its N-terminus with PAPBC1. Interacts through its C-terminus with the serine/threonine kinases MKNK1, and with MKNK2. Appears to act as a scaffold protein, holding these enzymes in place to phosphorylate EIF4E. Non-phosphorylated EIF4EBP1 competes with EIF4G1/EIF4G3 to interact with EIF4E; insulin stimulated MAP-kinase (MAPK1 and MAPK3) phosphorylation of EIF4EBP1 causes dissociation of the complex allowing EIF4G1/EIF4G3 to bind and consequent initiation of translation. Interacts with CIRBP and MIF4GD. Interacts with RBM4. Interacts with EIF4E3. Interacts with HNRNPD/AUF1; the interaction requires RNA. {ECO:0000269|PubMed:15153109}. +O55135 IF6_MOUSE Eukaryotic translation initiation factor 6 (eIF-6) (B4 integrin interactor) (CAB) (p27(BBP)) 245 26,511 Chain (1); Modified residue (8); Mutagenesis (1) FUNCTION: Binds to the 60S ribosomal subunit and prevents its association with the 40S ribosomal subunit to form the 80S initiation complex in the cytoplasm. Behaves as a stimulatory translation initiation factor downstream insulin/growth factors. Is also involved in ribosome biogenesis. Associates with pre-60S subunits in the nucleus and is involved in its nuclear export. Cytoplasmic release of TIF6 from 60S subunits and nuclear relocalization is promoted by a RACK1 (RACK1)-dependent protein kinase C activity. In tissues responsive to insulin, controls fatty acid synthesis and glycolysis by exerting translational control of adipogenic transcription factors such as CEBPB, CEBPD and ATF4 that have G/C rich or uORF in their 5'UTR (PubMed:26383020). Required for ROS-dependent megakaryocyte maturation and platelets formation, controls the expression of mitochondrial respiratory chain genes involved in reactive oxygen species (ROS) synthesis (PubMed:26391622). Involved in miRNA-mediated gene silencing by the RNA-induced silencing complex (RISC). Required for both miRNA-mediated translational repression and miRNA-mediated cleavage of complementary mRNAs by RISC (By similarity). Modulates cell cycle progression and global translation of pre-B cells, its activation seems to be rate-limiting in tumorigenesis and tumor growth (PubMed:21665150). {ECO:0000255|HAMAP-Rule:MF_03132, ECO:0000269|PubMed:18784653, ECO:0000269|PubMed:21665150, ECO:0000269|PubMed:26383020, ECO:0000269|PubMed:26391622}. PTM: Phosphorylation at Ser-174 and Ser-175 by CSNK1D/CK1 promotes nuclear export. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus. Note=Shuttles between cytoplasm and nucleus/nucleolus. SUBUNIT: Monomer. Associates with the 60S ribosomal subunit. Interacts with RACK1. Interacts with DICER1, AGO2, TARBP2, MOV10 and RPL7A; they form a large RNA-induced silencing complex (RISC). {ECO:0000255|HAMAP-Rule:MF_03132}. TISSUE SPECIFICITY: Detected in bladder, duodenum, liver, esophagus, pancreas, adipose tissue, megakaryocytes and testis with lower levels in muscle (at protein level). {ECO:0000269|PubMed:11290417, ECO:0000269|PubMed:26383020, ECO:0000269|PubMed:26391622}. +Q8BXL9 IFFO1_MOUSE Intermediate filament family orphan 1 562 62,415 Alternative sequence (4); Chain (1); Coiled coil (3); Compositional bias (1); Domain (1); Sequence conflict (5) +Q8BV66 IFI44_MOUSE Interferon-induced protein 44 (Microtubule-associated protein 44) 422 47,852 Chain (1); Sequence conflict (2) FUNCTION: This protein aggregates to form microtubular structures. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. +P0DOV2 IFI4_MOUSE Interferon-activable protein 204 (Ifi-204) (Interferon-inducible protein p204) 619 69,438 Chain (1); Domain (3); Motif (2); Region (2); Repeat (3); Sequence conflict (13) FUNCTION: Inhibits the transcription of ribosomal RNA. May inhibit DNA binding by UBTF. Inhibits cell growth via p53/TP53 and RB1-dependent and independent pathways. Acts as a coactivator of RUNX2 during osteogenesis. May be involved in macrophage differentiation. Enables skeletal muscle and cardiac myocyte differentiation by sequestring Id proteins in the cytosol and promoting their ubiquitination and subsequent degradation. {ECO:0000269|PubMed:10329630, ECO:0000269|PubMed:11940648, ECO:0000269|PubMed:15557274, ECO:0000269|PubMed:16244109, ECO:0000269|PubMed:16458891, ECO:0000269|PubMed:16556595, ECO:0000269|PubMed:16556596}. SUBCELLULAR LOCATION: Nucleus. Nucleus, nucleolus. Cytoplasm. Note=Nuclear in proliferating cells, translocates to cytosol during cell differentiation. SUBUNIT: Interacts with UBTF. Interacts with RUNX2. Interacts with ID1, ID2 and ID3. {ECO:0000269|PubMed:11940648, ECO:0000269|PubMed:15557274}. DOMAIN: The 2 HIN-200 domains are able to interact with RUNX2. TISSUE SPECIFICITY: Present in osteoblasts (at protein level). {ECO:0000269|PubMed:15557274}. +P0DOV1 IFI5B_MOUSE Interferon-activable protein 205-B (Ifi-205-B) (Interferon-inducible protein p205-B) (Myeloid cell nuclear differentiation antigen) (Protein D3) 425 46,977 Alternative sequence (1); Beta strand (1); Chain (1); Domain (2); Erroneous initiation (1); Helix (4); Region (1); Repeat (4); Sequence conflict (6); Turn (4) FUNCTION: May act as a transcriptional regulator in the myeloid lineage. Inhibits cell growth via p53/TP53 and RB1-dependent and independent pathways. {ECO:0000269|PubMed:15342947, ECO:0000269|PubMed:16458891}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15342947}. SUBUNIT: Interacts with TP53, RB1, CDK1, CDK2 and HOXB2. {ECO:0000269|PubMed:16458891}. TISSUE SPECIFICITY: Mononuclear phagocytes. {ECO:0000269|PubMed:7684766}. +Q64345 IFIT3_MOUSE Interferon-induced protein with tetratricopeptide repeats 3 (IFIT-3) (Glucocorticoid-attenuated response gene 49 protein) (GARG-49) (P49) (IRG2) 403 47,223 Chain (1); Repeat (4); Sequence conflict (1) FUNCTION: IFN-induced antiviral protein which acts as an inhibitor of cellular as well as viral processes, cell migration, proliferation, signaling, and viral replication. Enhances MAVS-mediated host antiviral responses by serving as an adapter bridging TBK1 to MAVS which leads to the activation of TBK1 and phosphorylation of IRF3 and phosphorylated IRF3 translocates into nucleus to promote antiviral gene transcription. Exihibits an antiproliferative activity via the up-regulation of cell cycle negative regulators CDKN1A/p21 and CDKN1B/p27. Normally, CDKN1B/p27 turnover is regulated by COPS5, which binds CDKN1B/p27 in the nucleus and exports it to the cytoplasm for ubiquitin-dependent degradation. IFIT3 sequesters COPS5 in the cytoplasm, thereby increasing nuclear CDKN1B/p27 protein levels. Upregulates CDKN1A/p21 by downregulating MYC, a repressor of CDKN1A/p21. Can negatively regulate the apoptotic effects of IFIT2 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Mitochondrion {ECO:0000250}. SUBUNIT: Component of an interferon-dependent multiprotein complex, at least composed of IFIT1, IFIT2 and IFIT3. Interacts with IFIT1 and IFIT2 (By similarity). Interacts (via N-terminus) with MAVS, TBK1, TRAF6 and DDX58 (By similarity). Interacts with COPS5 (By similarity). {ECO:0000250}. +Q8BR26 IFM10_MOUSE Interferon-induced transmembrane protein 10 (Dispanin subfamily A member 3) (DSPA3) 201 21,555 Alternative sequence (2); Chain (1); Lipidation (2); Topological domain (3); Transmembrane (2) TRANSMEM 128 148 Helical. {ECO:0000255}.; TRANSMEM 174 194 Helical. {ECO:0000255}. TOPO_DOM 1 127 Extracellular. {ECO:0000255}.; TOPO_DOM 149 173 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 195 201 Extracellular. {ECO:0000255}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q3UYI6 FUZZY_MOUSE Protein fuzzy homolog 415 45,588 Alternative sequence (2); Chain (1); Compositional bias (1); Sequence conflict (1) FUNCTION: Probable planar cell polarity effector involved in cilium biogenesis. May regulate protein and membrane transport to the cilium. Proposed to function as core component of the CPLANE (ciliogenesis and planar polarity effectors) complex involved in the recruitment of peripheral IFT-A proteins to basal bodies (PubMed:19877275, PubMed:19767740, PubMed:27158779). May regulate the morphogenesis of hair follicles which depends on functional primary cilia (PubMed:20962855). {ECO:0000269|PubMed:19767740, ECO:0000269|PubMed:19877275, ECO:0000269|PubMed:20962855, ECO:0000305|PubMed:27158779}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q2HZX7}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q2HZX7}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000305}. SUBUNIT: Interacts with CPLANE1. Interacts with INTU and WDPCP; FUZ, INTU and WDPCP probably form the core CPLANE (ciliogenesis and planar polarity effectors) complex. {ECO:0000269|PubMed:27158779}. TISSUE SPECIFICITY: Expressed in dermal and epidermal cells. {ECO:0000269|PubMed:20962855}. +P23188 FURIN_MOUSE Furin (EC 3.4.21.75) (Dibasic-processing enzyme) (Paired basic amino acid residue-cleaving enzyme) (PACE) (Prohormone convertase 3) 793 86,772 Active site (3); Beta strand (21); Binding site (6); Chain (1); Disulfide bond (3); Domain (2); Glycosylation (2); Helix (14); Metal binding (12); Modified residue (2); Motif (2); Propeptide (1); Region (4); Repeat (2); Sequence conflict (1); Signal peptide (1); Site (2); Topological domain (2); Transmembrane (1); Turn (9) TRANSMEM 715 735 Helical. {ECO:0000255}. TOPO_DOM 108 714 Lumenal. {ECO:0000305}.; TOPO_DOM 736 793 Cytoplasmic. {ECO:0000305}. FUNCTION: Ubiquitous endoprotease within constitutive secretory pathways capable of cleavage at the RX(K/R)R consensus motif. Mediates processing of TGFB1, an essential step in TGF-beta-1 activation. {ECO:0000250|UniProtKB:P09958}. PTM: The inhibition peptide, which plays the role of an intramolecular chaperone, is autocatalytically removed in the endoplasmic reticulum (ER) and remains non-covalently bound to furin as a potent autoinhibitor. Following transport to the trans Golgi, a second cleavage within the inhibition propeptide results in propeptide dissociation and furin activation. {ECO:0000250|UniProtKB:P09958}.; PTM: Phosphorylation is required for TGN localization of the endoprotease. In vivo, exists as di-, mono- and non-phosphorylated forms. {ECO:0000250|UniProtKB:P09958}. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:P09958}; Single-pass type I membrane protein {ECO:0000305}. Cell membrane {ECO:0000250|UniProtKB:P09958}; Single-pass type I membrane protein {ECO:0000305}. Secreted {ECO:0000250|UniProtKB:Q28193}. Endosome membrane {ECO:0000250|UniProtKB:P09958}; Single-pass type I membrane protein {ECO:0000305}. Note=Shuttles between the trans-Golgi network and the cell surface. Propeptide cleavage is a prerequisite for exit of furin molecules out of the endoplasmic reticulum (ER). A second cleavage within the propeptide occurs in the trans Golgi network (TGN), followed by the release of the propeptide and the activation of furin. {ECO:0000250|UniProtKB:P09958}. SUBUNIT: Interacts with FLNA (PubMed:9412467). Binds to PACS1 which mediates TGN localization and connection to clathrin adapters (By similarity). {ECO:0000250|UniProtKB:P09958, ECO:0000269|PubMed:9412467}. DOMAIN: Contains a cytoplasmic domain responsible for its TGN localization and recycling from the cell surface. {ECO:0000250|UniProtKB:P09958}. TISSUE SPECIFICITY: Seems to be expressed ubiquitously. {ECO:0000269|PubMed:2266110}. +Q61584 FXR1_MOUSE Fragile X mental retardation syndrome-related protein 1 (mFxr1p) 677 76,222 Alternative sequence (5); Chain (1); Compositional bias (2); Cross-link (1); Domain (4); Initiator methionine (1); Modified residue (15); Region (1); Sequence conflict (1) FUNCTION: RNA-binding protein required for embryonic and postnatal development of muscle tissue. May regulate intracellular transport and local translation of certain mRNAs. {ECO:0000269|PubMed:15128702}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with FMR1 (By similarity). Interacts with FRX2 (By similarity). Interacts with TDRD3 (By similarity). Interacts with HABP4 (By similarity). Interacts with CYFIP2 but not with CYFIP1 (PubMed:11438699). {ECO:0000250|UniProtKB:P51114, ECO:0000269|PubMed:11438699}. DOMAIN: The tandem Agenet-like domains preferentially recognize trimethylated histone peptides. {ECO:0000250}. TISSUE SPECIFICITY: In early embryogenesis, highest expression in somites and central nervous system. Also expressed in spinal cord, surrounding mesenchymal tissue and undifferentiated gonad. In mid-embryogenesis, most prominent in gonad and muscle tissue. Also expressed in liver, retina, telencephalon and mesencephalon. In late embryogenesis, restricted to skeletal muscle and proliferative active layers of brain. After birth, highly expressed in postmeiotic spermatids. Intermediate levels are found in heart, liver and kidney with lower levels in brain and skeletal muscle. Isoform(s) containing the 27 amino acid pocket (residues 564-590) are present in adult heart and muscle. {ECO:0000269|PubMed:10409431, ECO:0000269|PubMed:16000371}. +P39688 FYN_MOUSE Tyrosine-protein kinase Fyn (EC 2.7.10.2) (Proto-oncogene c-Fyn) (p59-Fyn) 537 60,675 Active site (1); Alternative sequence (2); Beta strand (12); Binding site (1); Chain (1); Domain (3); Helix (3); Initiator methionine (1); Lipidation (3); Modified residue (6); Mutagenesis (5); Nucleotide binding (1); Sequence conflict (3); Turn (1) FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in many biological processes including regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. Inactive FYN is phosphorylated on its C-terminal tail within the catalytic domain. Following activation by PKA, the protein subsequently associates with PTK2/FAK1, allowing PTK2/FAK1 phosphorylation, activation and targeting to focal adhesions. Involved in the regulation of cell adhesion and motility through phosphorylation of CTNNB1 (beta-catenin) and CTNND1 (delta-catenin). Regulates cytoskeletal remodeling by phosphorylating several proteins including the actin regulator WAS and the microtubule-associated proteins MAP2 and MAPT. Promotes cell survival by phosphorylating AGAP2/PIKE-A and preventing its apoptotic cleavage. Participates in signal transduction pathways that regulate the integrity of the glomerular slit diaphragm (an essential part of the glomerular filter of the kidney) by phosphorylating several slit diaphragm components including NPHS1, KIRREL1 and TRPC6. Plays a role in neural processes by phosphorylating DPYSL2, a multifunctional adapter protein within the central nervous system, ARHGAP32, a regulator for Rho family GTPases implicated in various neural functions, and SNCA, a small pre-synaptic protein. Participates in the downstream signaling pathways that lead to T-cell differentiation and proliferation following T-cell receptor (TCR) stimulation. Phosphorylates PTK2B/PYK2 in response to T-cell receptor activation. Also participates in negative feedback regulation of TCR signaling through phosphorylation of PAG1, thereby promoting interaction between PAG1 and CSK and recruitment of CSK to lipid rafts. CSK maintains LCK and FYN in an inactive form. Promotes CD28-induced phosphorylation of VAV1. {ECO:0000250|UniProtKB:P06241, ECO:0000269|PubMed:12218089, ECO:0000269|PubMed:12640114, ECO:0000269|PubMed:14999081, ECO:0000269|PubMed:8007959}. PTM: Autophosphorylated at Tyr-420. Phosphorylation on the C-terminal tail at Tyr-531 by CSK maintains the enzyme in an inactive state. PTPRC/CD45 dephosphorylates Tyr-531 leading to activation. Ultraviolet B (UVB) strongly increase phosphorylation at Thr-15 and kinase activity, and promotes translocation from the cytoplasm to the nucleus. Dephosphorylation at Tyr-420 by PTPN2 negatively regulates T-cell receptor signaling (By similarity). {ECO:0000250}.; PTM: Palmitoylation at Cys-3 and Cys-6 regulates subcellular location. {ECO:0000269|PubMed:7980442, ECO:0000269|PubMed:8413237, ECO:0000269|PubMed:9201723}.; PTM: Myristoylation is required prior to palmitoylation. {ECO:0000269|PubMed:8655574}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Present and active in lipid rafts. Palmitoylation is crucial for proper trafficking (By similarity). {ECO:0000250}. SUBUNIT: Interacts (via its SH3 domain) with PIK3R1 and PRMT8 (By similarity). Interacts with FYB1, PAG1, and SH2D1A (By similarity). Interacts with CD79A (tyrosine-phosphorylated form); the interaction increases FYN activity (PubMed:8168489). Interacts with TOM1L1 (phosphorylated form) (PubMed:11711534). Interacts with SH2D1A and SLAMF1 (By similarity). Interacts with and phosphorylates ITCH, down-regulating its activity (By similarity). Interacts with FASLG (By similarity). Interacts with RUNX3 (By similarity). Interacts with KIT (By similarity). Interacts with EPHA8; possible downstream effector of EPHA8 in regulation of cell adhesion (By similarity). Interacts with PTK2/FAK1; this interaction leads to PTK2/FAK1 phosphorylation and activation (By similarity). Interacts with CAV1; this interaction couples integrins to the Ras-ERK pathway (By similarity). Interacts (via SH3 domain) with KLHL2 (via N-terminus) (By similarity). Interacts with KDR (tyrosine phosphorylated) (PubMed:16966330). Interacts (via SH2 domain) with CSF1R (tyrosine phosphorylated) (PubMed:7681396, PubMed:9312046). Interacts with UNC119 (By similarity). Interacts (via SH2 domain) with PTPRH (phosphorylated form) (PubMed:20398064). Interacts with PTPRO (phosphorylated form) (PubMed:20398064). Interacts with PTPRB (phosphorylated form) (PubMed:20398064). Interacts with FYB2 (By similarity). {ECO:0000250|UniProtKB:P06241, ECO:0000250|UniProtKB:Q62844, ECO:0000269|PubMed:11711534, ECO:0000269|PubMed:16966330, ECO:0000269|PubMed:20398064, ECO:0000269|PubMed:7681396, ECO:0000269|PubMed:8168489, ECO:0000269|PubMed:9312046}. TISSUE SPECIFICITY: Isoform 1 is highly expressed in the brain, isoform 2 is expressed in cells of hemopoietic lineages, especially T-lymphocytes. {ECO:0000269|PubMed:1361685, ECO:0000269|PubMed:8007959}. +Q9D164 FXYD6_MOUSE FXYD domain-containing ion transport regulator 6 (PLM-like protein) (Phosphohippolin) 94 10,374 Alternative sequence (1); Chain (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 35 57 Helical. {ECO:0000255}. TOPO_DOM 18 34 Extracellular. {ECO:0000255}.; TOPO_DOM 58 94 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q8BHC9 FUT11_MOUSE Alpha-(1,3)-fucosyltransferase 11 (EC 2.4.1.-) (Fucosyltransferase XI) (Fuc-TXI) (FucT-XI) (Galactoside 3-L-fucosyltransferase 11) (Fucosyltransferase 11) 489 55,533 Chain (1); Disulfide bond (2); Glycosylation (1); Sequence conflict (4); Topological domain (2); Transmembrane (1) TRANSMEM 8 24 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 7 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 25 489 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Probable fucosyltransferase. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. Expressed at slightly higher level in heart, kidney and lung. {ECO:0000269|PubMed:12370785}. +Q00420 GABP1_MOUSE GA-binding protein subunit beta-1 (GABP subunit beta-1) (GABPB-1) (GABP subunit beta-2) (GABPB-2) 383 41,358 Alternative sequence (4); Chain (1); Helix (10); Initiator methionine (1); Modified residue (1); Repeat (5); Turn (2) FUNCTION: Transcription factor capable of interacting with purine rich repeats (GA repeats). SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with HCFC1, causing repression of transcriptional activity (By similarity). Heterotetramer of two alpha and two beta subunits. {ECO:0000250}. +Q9D172 GAL3A_MOUSE Glutamine amidotransferase-like class 1 domain-containing protein 3A, mitochondrial 266 28,090 Chain (1); Modified residue (10); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}. +Q80VA0 GALT7_MOUSE N-acetylgalactosaminyltransferase 7 (EC 2.4.1.-) (Polypeptide GalNAc transferase 7) (GalNAc-T7) (pp-GaNTase 7) (Protein-UDP acetylgalactosaminyltransferase 7) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 7) 657 75,419 Alternative sequence (2); Binding site (4); Chain (1); Disulfide bond (5); Domain (1); Erroneous initiation (1); Metal binding (3); Region (2); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 7 29 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 30 657 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Glycopeptide transferase involved in O-linked oligosaccharide biosynthesis, which catalyzes the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide. In contrast to other proteins of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Some peptide transferase activity is however not excluded, considering that its appropriate peptide substrate may remain unidentified (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. DOMAIN: There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding. {ECO:0000250}.; DOMAIN: The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in sublingual gland. Expressed at lower level in stomach, small intestiine and colon. {ECO:0000269|PubMed:10488133}. +Q8K157 GALM_MOUSE Aldose 1-epimerase (EC 5.1.3.3) (Galactose mutarotase) 342 37,799 Active site (2); Binding site (1); Chain (1); Modified residue (1); Region (1) Carbohydrate metabolism; hexose metabolism. FUNCTION: Mutarotase converts alpha-aldose to the beta-anomer. It is active on D-glucose, L-arabinose, D-xylose, D-galactose, maltose and lactose (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. SUBUNIT: Monomer. {ECO:0000250}. +P01863 GCAA_MOUSE Ig gamma-2A chain C region, A allele (Immunoglobulin heavy chain gamma polypeptide) 330 36,389 Beta strand (22); Chain (1); Disulfide bond (7); Domain (3); Glycosylation (1); Helix (8); Non-terminal residue (1); Turn (3) +P35492 HUTH_MOUSE Histidine ammonia-lyase (Histidase) (EC 4.3.1.3) 657 72,258 Chain (1); Cross-link (1); Modified residue (5); Natural variant (1) Amino-acid degradation; L-histidine degradation into L-glutamate; N-formimidoyl-L-glutamate from L-histidine: step 1/3. PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ala-Ser-Gly. {ECO:0000250}. DISEASE: Note=Defects in Hal are the cause of histidinemia (His). +Q9R0Y8 GBRG1_MOUSE Gamma-aminobutyric acid receptor subunit gamma-1 (GABA(A) receptor subunit gamma-1) 465 53,407 Chain (1); Disulfide bond (1); Glycosylation (3); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (4) TRANSMEM 273 294 Helical. {ECO:0000305}.; TRANSMEM 299 320 Helical. {ECO:0000305}.; TRANSMEM 332 354 Helical. {ECO:0000305}.; TRANSMEM 445 465 Helical. {ECO:0000305}. TOPO_DOM 36 272 Extracellular. {ECO:0000305}.; TOPO_DOM 355 444 Cytoplasmic. {ECO:0000305}. FUNCTION: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel. PTM: May be palmitoylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. SUBUNIT: Generally pentameric. There are five types of GABA(A) receptor chains: alpha, beta, gamma, delta, and rho. +P27681 GBRG3_MOUSE Gamma-aminobutyric acid receptor subunit gamma-3 (GABA(A) receptor subunit gamma-3) 467 54,334 Chain (1); Disulfide bond (1); Glycosylation (2); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (4) TRANSMEM 255 277 Helical. {ECO:0000305}.; TRANSMEM 281 303 Helical. {ECO:0000305}.; TRANSMEM 315 337 Helical. {ECO:0000305}.; TRANSMEM 444 467 Helical. {ECO:0000305}. TOPO_DOM 18 254 Extracellular. {ECO:0000305}.; TOPO_DOM 338 443 Cytoplasmic. {ECO:0000305}. FUNCTION: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel. PTM: May be palmitoylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. SUBUNIT: Generally pentameric. There are five types of GABA(A) receptor chains: alpha, beta, gamma, delta, and rho. +Q91WK5 GCSH_MOUSE Glycine cleavage system H protein, mitochondrial (Lipoic acid-containing protein) 170 18,637 Beta strand (10); Chain (1); Domain (1); Helix (4); Modified residue (1); Sequence conflict (2); Transit peptide (1); Turn (2) FUNCTION: The glycine cleavage system catalyzes the degradation of glycine. The H protein (GCSH) shuttles the methylamine group of glycine from the P protein (GLDC) to the T protein (GCST) (By similarity). {ECO:0000250|UniProtKB:P11183}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P20821}. SUBUNIT: The glycine cleavage system is composed of four proteins: P (GLDC), T (GCST), L (DLD) and H (GCSH). Interacts with GLDC (By similarity). {ECO:0000250|UniProtKB:P11183}. +P13020 GELS_MOUSE Gelsolin (Actin-depolymerizing factor) (ADF) (Brevin) 780 85,942 Alternative sequence (1); Beta strand (27); Chain (1); Disulfide bond (1); Helix (15); Metal binding (11); Modified residue (7); Region (5); Repeat (6); Sequence conflict (10); Signal peptide (1); Turn (4) FUNCTION: Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed. Plays a role in ciliogenesis. PTM: Phosphorylated on tyrosine residues in vitro. {ECO:0000250}. SUBCELLULAR LOCATION: Isoform 2: Cytoplasm, cytoskeleton.; SUBCELLULAR LOCATION: Isoform 1: Secreted. SUBUNIT: Binds to actin and to fibronectin. Identified in a complex composed of ACTA1, COBL, GSN AND TMSB4X (By similarity). Interacts with the inactive form of EIF2AK2/PKR. {ECO:0000250, ECO:0000269|PubMed:22633459}. +Q9D6M3 GHC1_MOUSE Mitochondrial glutamate carrier 1 (GC-1) (Glutamate/H(+) symporter 1) (Solute carrier family 25 member 22) 323 34,670 Chain (1); Repeat (3); Transmembrane (6) TRANSMEM 12 32 Helical; Name=1. {ECO:0000255}.; TRANSMEM 62 82 Helical; Name=2. {ECO:0000255}.; TRANSMEM 107 127 Helical; Name=3. {ECO:0000255}.; TRANSMEM 189 209 Helical; Name=4. {ECO:0000255}.; TRANSMEM 223 243 Helical; Name=5. {ECO:0000255}.; TRANSMEM 292 312 Helical; Name=6. {ECO:0000255}. FUNCTION: Involved in the transport of glutamate across the inner mitochondrial membrane. Glutamate is cotransported with H(+) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q91VC9 GHITM_MOUSE Growth hormone-inducible transmembrane protein (Mitochondrial morphology and cristae structure 1) (MICS1) 346 37,275 Chain (1); Sequence conflict (3); Topological domain (8); Transit peptide (1); Transmembrane (7) TRANSMEM 84 104 Helical. {ECO:0000255}.; TRANSMEM 127 147 Helical. {ECO:0000255}.; TRANSMEM 161 181 Helical. {ECO:0000255}.; TRANSMEM 192 212 Helical. {ECO:0000255}.; TRANSMEM 215 235 Helical. {ECO:0000255}.; TRANSMEM 246 266 Helical. {ECO:0000255}.; TRANSMEM 273 293 Helical. {ECO:0000255}. TOPO_DOM 46 83 Mitochondrial matrix. {ECO:0000255}.; TOPO_DOM 105 126 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 148 160 Mitochondrial matrix. {ECO:0000255}.; TOPO_DOM 182 191 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 213 214 Mitochondrial matrix. {ECO:0000255}.; TOPO_DOM 236 245 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 267 272 Mitochondrial matrix. {ECO:0000255}.; TOPO_DOM 294 346 Mitochondrial intermembrane. {ECO:0000255}. FUNCTION: Required for the mitochondrial tubular network and cristae organization. Involved in apoptotic release of cytochrome c (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q9CPY6 GID4_MOUSE Glucose-induced degradation protein 4 homolog (Vacuolar import and degradation protein 24 homolog) 217 24,863 Chain (1); Compositional bias (1); Erroneous termination (1); Sequence conflict (1); Site (3) FUNCTION: Substrate-recognition subunit of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1. Binds proteins and peptides with a Pro/N-degron consisting of an unmodified N-terminal Pro followed by a small residue, and has the highest affinity for the peptide Pro-Gly-Leu-Trp. Binds peptides with an N-terminal sequence of the type Pro-[Ala,Gly]-[Leu,Met,Gln,Ser,Tyr]-[Glu,Gly,His,Ser,Val,Trp,Tyr]. Does not bind peptides with an acetylated N-terminal Pro residue. {ECO:0000250|UniProtKB:Q8IVV7}. SUBUNIT: Identified in the CTLH complex that contains GID4, RANBP9 and/or RANBP10, MKLN1, MAEA, RMND5A (or alternatively its paralog RMND5B), GID8, ARMC8, WDR26 and YPEL5. Within this complex, MAEA, RMND5A (or alternatively its paralog RMND5B), GID8, WDR26, and RANBP9 and/or RANBP10 form the catalytic core, while GID4, MKLN1, ARMC8 and YPEL5 have ancillary roles. {ECO:0000250|UniProtKB:Q8IVV7}. DOMAIN: The first four residues of target peptides with a free N-terminal Pro (a Pro/N-degron) are bound inside a deep and narrow beta-barrel structure. {ECO:0000250|UniProtKB:Q8IVV7}. +Q5SV77 GGNB2_MOUSE Gametogenetin-binding protein 2 (Dioxin-inducible factor 3) (DIF-3) (Protein ZNF403) 696 78,970 Alternative sequence (2); Chain (1); Erroneous gene model prediction (3); Modified residue (2); Sequence caution (1); Sequence conflict (3) FUNCTION: May be involved in spermatogenesis. SUBCELLULAR LOCATION: Cytoplasmic vesicle {ECO:0000269|PubMed:15642376}. Note=Associated with vesicular structures. SUBUNIT: Interacts with isoform 1 of GGN. {ECO:0000269|PubMed:15642376}. TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:11728448}. +Q7TN16 HHIP_MOUSE Hedgehog-interacting protein (HHIP) (HIP) 700 78,513 Chain (1); Compositional bias (1); Disulfide bond (10); Domain (2); Glycosylation (4); Metal binding (1); Region (1); Sequence conflict (3); Signal peptide (1) FUNCTION: Modulates hedgehog signaling in several cell types, including brain and lung through direct interaction with members of the hedgehog family. Soluble forms inhibit Shh-induced differentiation in the fibroblast cell line C3H/10T1/2. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10050855}; Peripheral membrane protein {ECO:0000269|PubMed:10050855}. Secreted {ECO:0000269|PubMed:10050855}. Note=The last 22 C-terminal amino acids may participate in cell membrane attachment. SUBUNIT: Interacts with all three hedgehog family members, SHH, IHH and DHH. {ECO:0000269|PubMed:10050855}. DOMAIN: A flexible loop interacts with the SHH zinc binding site and contributes to zinc binding. {ECO:0000250}. TISSUE SPECIFICITY: In the adult brain, high expression found in the ventral cochlear nucleus, medial habenula, indusium griseum and tenia tecta. Some expression also in the caudate putamen, the nucleus accumbens, the ventral pallidum and in the superficial layers of the surerior colliculus. {ECO:0000269|PubMed:15019948}. +O54974 LEG7_MOUSE Galectin-7 (Gal-7) 136 15,173 Chain (1); Domain (1); Region (1) FUNCTION: Could be involved in cell-cell and/or cell-matrix interactions necessary for normal growth control. Pro-apoptotic protein that functions intracellularly upstream of JNK activation and cytochrome c release (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Secreted {ECO:0000250}. Note=May be secreted by a non-classical secretory pathway. {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. +Q7TPX9 LEGLB_MOUSE Galectin-related protein B (Lectin galactoside-binding-like protein B) 165 18,270 Chain (1); Domain (1) FUNCTION: Does not bind lactose, and may not bind carbohydrates. {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. +Q60668 HNRPD_MOUSE Heterogeneous nuclear ribonucleoprotein D0 (hnRNP D0) (AU-rich element RNA-binding protein 1) 355 38,354 Alternative sequence (2); Chain (1); Cross-link (3); Domain (2); Frameshift (2); Initiator methionine (1); Modified residue (24); Sequence caution (2); Sequence conflict (6) FUNCTION: Binds with high affinity to RNA molecules that contain AU-rich elements (AREs) found within the 3'-UTR of many proto-oncogenes and cytokine mRNAs. Also binds to double- and single-stranded DNA sequences in a specific manner and functions a transcription factor. Each of the RNA-binding domains specifically can bind solely to a single-stranded non-monotonous 5'-UUAG-3' sequence and also weaker to the single-stranded 5'-TTAGGG-3' telomeric DNA repeat. Binds RNA oligonucleotides with 5'-UUAGGG-3' repeats more tightly than the telomeric single-stranded DNA 5'-TTAGGG-3' repeats. Binding of RRM1 to DNA inhibits the formation of DNA quadruplex structure which may play a role in telomere elongation. May be involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. May play a role in the regulation of the rhythmic expression of circadian clock core genes. Directly binds to the 3'UTR of CRY1 mRNA and induces CRY1 rhythmic translation. May also be involved in the regulation of PER2 translation. {ECO:0000250|UniProtKB:Q14103}. PTM: Methylated by PRMT1, in an insulin-dependent manner. The PRMT1-mediated methylation regulates its phosphorylation (By similarity). {ECO:0000250|UniProtKB:Q14103}.; PTM: Arg-345 is dimethylated, probably to asymmetric dimethylarginine. {ECO:0000250|UniProtKB:Q14103}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q14103}. Cytoplasm {ECO:0000250|UniProtKB:Q14103}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Component of ribonucleosomes. Cytoplasmic localization oscillates diurnally. {ECO:0000250|UniProtKB:Q14103}. SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Part of a complex associated with the FOS mCRD domain and consisting of PABPC1, PAIP1, CSDE1/UNR and SYNCRIP. Interacts with IGF2BP2. Interacts with GTPBP1. Interacts with EIF4G1; the interaction requires RNA. Interacts with EIF3B and RPS3. {ECO:0000250|UniProtKB:Q14103}. +P61979 HNRPK_MOUSE Heterogeneous nuclear ribonucleoprotein K (hnRNP K) 463 50,976 Alternative sequence (2); Chain (1); Compositional bias (2); Cross-link (11); Domain (3); Modified residue (19); Region (6); Repeat (9); Sequence conflict (5) FUNCTION: One of the major pre-mRNA-binding proteins. Binds tenaciously to poly(C) sequences. Likely to play a role in the nuclear metabolism of hnRNAs, particularly for pre-mRNAs that contain cytidine-rich sequences. Can also bind poly(C) single-stranded DNA. Plays an important role in p53/TP53 response to DNA damage, acting at the level of both transcription activation and repression. When sumoylated, acts as a transcriptional coactivator of p53/TP53, playing a role in p21/CDKN1A and 14-3-3 sigma/SFN induction (By similarity). As far as transcription repression is concerned, acts by interacting with long intergenic RNA p21 (lincRNA-p21), a non-coding RNA induced by p53/TP53. This interaction is necessary for the induction of apoptosis, but not cell cycle arrest. {ECO:0000250, ECO:0000269|PubMed:20673990}. PTM: Sumoylated by CBX4. Sumoylation is increased upon DNA damage, such as that produced by doxorubicin, etoposide, UV light and camptothecin, due to enhanced CBX4 phosphorylation by HIPK2 under these conditions (By similarity). {ECO:0000250}.; PTM: Ubiquitinated by MDM2. Doxorubicin treatment does not affect monoubiquitination, but slightly decreases HNRNPK poly-ubiquitination (By similarity). {ECO:0000250}.; PTM: O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P61978}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P61978}. Cell projection, podosome {ECO:0000250|UniProtKB:P61978}. SUBUNIT: Identified in the spliceosome C complex (By similarity). Interacts with ANKRD28 and RBM42 (By similarity). Interacts with DDX1 (By similarity). Interacts with MDM2; this interaction leads to ubiquitination and proteasomal degradation (By similarity). Interacts with p53/TP53 (By similarity). Interacts with ZIK1 (PubMed:8910362). Interacts with BRDT (PubMed:22570411). Interacts with IVNS1ABP (By similarity). {ECO:0000250|UniProtKB:P61978, ECO:0000250|UniProtKB:P61980, ECO:0000269|PubMed:22570411, ECO:0000269|PubMed:8910362}. +O35737 HNRH1_MOUSE Heterogeneous nuclear ribonucleoprotein H (hnRNP H) [Cleaved into: Heterogeneous nuclear ribonucleoprotein H, N-terminally processed] 449 49,199 Chain (2); Cross-link (3); Domain (3); Initiator methionine (1); Modified residue (9); Region (2); Repeat (4) FUNCTION: This protein is a component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes which provide the substrate for the processing events that pre-mRNAs undergo before becoming functional, translatable mRNAs in the cytoplasm. Mediates pre-mRNA alternative splicing regulation. Inhibits, together with CUGBP1, insulin receptor (IR) pre-mRNA exon 11 inclusion in myoblast. Binds to the IR RNA. Binds poly(RG) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}. SUBUNIT: Part of a ternary complex containing FUBP2, PTBP1, PTBP2 and HNRNPH1. Identified in the spliceosome C complex. Interacts with IGF2BP1. Interacts with CUGBP1; the interaction is RNA-dependent. Interacts with MBNL1; the interaction in RNA-independent (By similarity). {ECO:0000250}. DOMAIN: Each quasi-RRM repeat bound poly(RG), while only the N-terminal QRRM bound poly(RC) and poly(RU). None of the repeats bound detectable amounts of poly(RA). +Q9D0E1 HNRPM_MOUSE Heterogeneous nuclear ribonucleoprotein M (hnRNP M) 729 77,649 Alternative sequence (1); Chain (1); Compositional bias (1); Cross-link (22); Domain (3); Initiator methionine (1); Modified residue (24); Region (1); Repeat (27); Sequence conflict (1) FUNCTION: Pre-mRNA binding protein in vivo, binds avidly to poly(G) and poly(U) RNA homopolymers in vitro. Involved in splicing. Acts as a receptor for carcinoembryonic antigen in Kupffer cells, may initiate a series of signaling events leading to tyrosine phosphorylation of proteins and induction of IL-1 alpha, IL-6, IL-10 and tumor necrosis factor alpha cytokines (By similarity). {ECO:0000250}. PTM: Sumoylated. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Identified in the spliceosome C complex. {ECO:0000250}. +Q9D8M3 HRG1_MOUSE Heme transporter HRG1 (Heme-responsive gene 1 protein homolog) (HRG-1) (Solute carrier family 48 member 1) 146 16,489 Chain (1); Motif (1); Sequence conflict (2); Transmembrane (4) TRANSMEM 12 32 Helical. {ECO:0000255}.; TRANSMEM 40 60 Helical. {ECO:0000255}.; TRANSMEM 74 94 Helical. {ECO:0000255}.; TRANSMEM 110 130 Helical. {ECO:0000255}. FUNCTION: Heme transporter that regulates intracellular heme availability through the endosomal or lysosomal compartment. {ECO:0000250}. SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Lysosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q8K0U4 HS12A_MOUSE Heat shock 70 kDa protein 12A 675 74,871 Chain (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (1); Sequence conflict (2) TISSUE SPECIFICITY: Expressed most strongly in brain, kidney and heart with little or no expression in other tissues. In the aorta, preferentially expressed in lesions. {ECO:0000269|PubMed:12552099}. +O35310 HS3S1_MOUSE Heparan sulfate glucosamine 3-O-sulfotransferase 1 (EC 2.8.2.23) (Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 1) (Heparan sulfate 3-O-sulfotransferase 1) 311 35,899 Beta strand (8); Binding site (3); Chain (1); Disulfide bond (1); Glycosylation (4); Helix (14); Mutagenesis (20); Nucleotide binding (2); Signal peptide (1); Turn (2) FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to position 3 of glucosamine residues in heparan. Catalyzes the rate limiting step in the biosynthesis of heparan sulfate (HSact). This modification is a crucial step in the biosynthesis of anticoagulant heparan sulfate as it completes the structure of the antithrombin pentasaccharide binding site. {ECO:0000269|PubMed:9346953}. SUBCELLULAR LOCATION: Golgi apparatus lumen {ECO:0000305}. +Q61696 HS71A_MOUSE Heat shock 70 kDa protein 1A (Heat shock 70 kDa protein 3) (HSP70.3) (Hsp68) 641 70,079 Binding site (1); Chain (1); Initiator methionine (1); Modified residue (12); Nucleotide binding (4); Region (2); Sequence conflict (11) FUNCTION: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The co-chaperones have been shown to not only regulate different steps of the ATPase cycle, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The co-chaperones are of three types: J-domain co-chaperones such as HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1. Maintains protein homeostasis during cellular stress through two opposing mechanisms: protein refolding and degradation. Its acetylation/deacetylation state determines whether it functions in protein refolding or protein degradation by controlling the competitive binding of co-chaperones HOPX and STUB1. During the early stress response, the acetylated form binds to HOPX which assists in chaperone-mediated protein refolding, thereafter, it is deacetylated and binds to ubiquitin ligase STUB1 that promotes ubiquitin-mediated protein degradation. Regulates centrosome integrity during mitosis, and is required for the maintenance of a functional mitotic centrosome that supports the assembly of a bipolar mitotic spindle. Enhances STUB1-mediated SMAD3 ubiquitination and degradation and facilitates STUB1-mediated inhibition of TGF-beta signaling. Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation. Negatively regulates heat shock-induced HSF1 transcriptional activity during the attenuation and recovery phase period of the heat shock response. {ECO:0000250|UniProtKB:P0DMV8}. PTM: In response to cellular stress, acetylated at Lys-77 by NA110 and then gradually deacetylated by HDAC4 at later stages. Acetylation enhances its chaperone activity and also determines whether it will function as a chaperone for protein refolding or degradation by controlling its binding to co-chaperones HOPX and STUB1. The acetylated form and the non-acetylated form bind to HOPX and STUB1 respectively. Acetylation also protects cells against various types of cellular stress. {ECO:0000250|UniProtKB:P0DMV8}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0DMV8}. Nucleus {ECO:0000250|UniProtKB:P0DMV8}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P0DMV8}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. {ECO:0000250|UniProtKB:P0DMV8}. SUBUNIT: Component of the CatSper complex (By similarity). Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs (By similarity). Interacts with CHCHD3, DNAJC7, IRAK1BP1, PPP5C and TSC2 (By similarity). Interacts with TERT; the interaction occurs in the absence of the RNA component, TERC, and dissociates once the TERT complex has formed (By similarity). Interacts with METTL21A (By similarity). Interacts with DNAAF2 (PubMed:19052621). Interacts with TRIM5 (via B30.2/SPRY domain) (By similarity). Interacts with PRKN (By similarity). Interacts with FOXP3 (PubMed:23973223). Interacts with NOD2; the interaction enhances NOD2 stability (By similarity). Interacts with DNAJC9 (via J domain) (By similarity). Interacts with ATF5; the interaction protects ATF5 from degradation via proteasome-dependent and caspase-dependent processes (By similarity). Interacts with RNF207 (via the C-terminus); this interaction additively increases KCNH2 expression (By similarity). Interacts with HSF1 (via transactivation domain); this interaction results in the inhibition of heat shock- and HSF1-induced transcriptional activity during the attenuation and recovery phase period of the heat shock response. Interacts with NAA10, HSP40, HSP90 and HDAC4. The acetylated form and the non-acetylated form interact with HOPX and STUB1 respectively. Interacts with NEDD1 and SMAD3. Interacts (via NBD) with BAG1, BAG2, BAG3 and HSPH1/HSP105. Interacts with DNAJC8 (By similarity). {ECO:0000250|UniProtKB:P0DMV8, ECO:0000269|PubMed:19052621, ECO:0000269|PubMed:23973223}. DOMAIN: The N-terminal nucleotide binding domain (NBD) (also known as the ATPase domain) is responsible for binding and hydrolyzing ATP. The C-terminal substrate-binding domain (SBD) (also known as peptide-binding domain) binds to the client/substrate proteins. The two domains are allosterically coupled so that, when ATP is bound to the NBD, the SBD binds relatively weakly to clients. When ADP is bound in the NBD, a conformational change enhances the affinity of the SBD for client proteins. {ECO:0000250|UniProtKB:P0DMV8}. +Q8BTX9 HSDL1_MOUSE Inactive hydroxysteroid dehydrogenase-like protein 1 330 36,868 Binding site (2); Chain (1); Initiator methionine (1); Modified residue (1); Nucleotide binding (1); Region (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. SUBUNIT: Interacts with STYXL1. {ECO:0000250}. +Q5ND04 HSF5_MOUSE Heat shock factor protein 5 (HSF 5) (Heat shock transcription factor 5) (HSTF 5) (Protein expressed in male leptotene and zygotene spermatocytes 220) (MLZ-220) 624 67,316 Chain (1); Compositional bias (1); DNA binding (1); Modified residue (1) FUNCTION: May act as a transcriptional factor. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: Expressed in adult but not fetal testis. Not expressed in ovary. {ECO:0000269|PubMed:20339383}. +P70387 HFE_MOUSE Hereditary hemochromatosis protein homolog 359 40,534 Chain (1); Disulfide bond (2); Domain (1); Glycosylation (4); Region (4); Sequence conflict (5); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 319 339 Helical. {ECO:0000255}. TOPO_DOM 25 318 Extracellular. {ECO:0000250|UniProtKB:Q30201}.; TOPO_DOM 340 359 Cytoplasmic. {ECO:0000250|UniProtKB:Q30201}. FUNCTION: Binds to transferrin receptor (TFR) and reduces its affinity for iron-loaded transferrin. {ECO:0000250|UniProtKB:Q30201}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q30201}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q30201}. SUBUNIT: Binds TFR through the extracellular domain in a pH-dependent manner. {ECO:0000250|UniProtKB:Q30201}. +P04441 HG2A_MOUSE H-2 class II histocompatibility antigen gamma chain (Ia antigen-associated invariant chain) (Ii) (MHC class II-associated invariant chain) (CD antigen CD74) 279 31,557 Alternative sequence (1); Chain (1); Disulfide bond (3); Domain (1); Glycosylation (3); Modified residue (1); Mutagenesis (1); Sequence conflict (3); Topological domain (2); Transmembrane (1) TRANSMEM 30 55 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 29 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 56 279 Extracellular. {ECO:0000255}. FUNCTION: Plays a critical role in MHC class II antigen processing by stabilizing peptide-free class II alpha/beta heterodimers in a complex soon after their synthesis and directing transport of the complex from the endoplasmic reticulum to compartments where peptide loading of class II takes place. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. SUBUNIT: Nonamer composed of three alpha/beta/gamma heterotrimers. {ECO:0000250}. +Q8R409 HEXI1_MOUSE Protein HEXIM1 (Cardiac lineage protein 1) 356 40,243 Chain (1); Coiled coil (1); Modified residue (7); Region (5) FUNCTION: Transcriptional regulator which functions as a general RNA polymerase II transcription inhibitor. In cooperation with 7SK snRNA sequesters P-TEFb in a large inactive 7SK snRNP complex preventing RNA polymerase II phosphorylation and subsequent transcriptional elongation. May also regulate NF-kappa-B, ESR1, NR3C1 and CIITA-dependent transcriptional activity. Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway. {ECO:0000250|UniProtKB:O94992}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O94992}. Cytoplasm {ECO:0000250|UniProtKB:O94992}. Note=Binds alpha-importin and is mostly nuclear. {ECO:0000250|UniProtKB:O94992}. SUBUNIT: Homooligomer and heterooligomer with HEXIM2; probably dimeric. Component of the 7SK snRNP complex at least composed of P-TEFb (composed of CDK9 and CCNT1/cyclin-T1), HEXIM1, HEXIM2, BCDIN3, SART3 proteins and 7SK and U6 snRNAs. Interacts with the N-CoR complex through NCOR1. Interacts with ESR1 and NR3C1. May interact with NF-kappa-B through RELA. Interacts with CCNT2; mediates formation of a tripartite complex with KPNA2. Part of the HDP-RNP complex composed of at least HEXIM1, PRKDC, XRCC5, XRCC6, paraspeckle proteins (SFPQ, NONO, PSPC1, RBM14, and MATR3) and NEAT1 non-coding RNA. {ECO:0000250|UniProtKB:O94992}. DOMAIN: The coiled-coil domain mediates oligomerization. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed with higher expression in heart, skeletal muscle and brain (at protein level). {ECO:0000269|PubMed:12119119}. +Q9JLR9 HIG1A_MOUSE HIG1 domain family member 1A, mitochondrial (Hypoxia-inducible gene 1 protein) 95 10,425 Chain (1); Domain (1); Initiator methionine (1); Modified residue (2); Transmembrane (2) TRANSMEM 28 48 Helical. {ECO:0000255|PROSITE-ProRule:PRU00836}.; TRANSMEM 69 89 Helical. {ECO:0000255|PROSITE-ProRule:PRU00836}. FUNCTION: Proposed subunit of cytochrome c oxidase (COX, complex IV), which is the terminal component of the mitochondrial respiratory chain that catalyzes the reduction of oxygen to water. May play a role in the assembly of respiratory supercomplexes (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000255|PROSITE-ProRule:PRU00836}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00836}. Mitochondrion inner membrane {ECO:0000250}. SUBUNIT: Associates with cytochrome c oxidase (COX, complex IV); proposed complex component. Also associates with respiratory chain supercomplexes (By similarity). {ECO:0000250}. +Q9CQJ1 HIG2A_MOUSE HIG1 domain family member 2A 106 11,368 Chain (1); Domain (1); Initiator methionine (1); Modified residue (1); Transmembrane (2) TRANSMEM 47 67 Helical. {ECO:0000255|PROSITE-ProRule:PRU00836}.; TRANSMEM 83 103 Helical. {ECO:0000255|PROSITE-ProRule:PRU00836}. FUNCTION: Proposed subunit of cytochrome c oxidase (COX, complex IV), which is the terminal component of the mitochondrial respiratory chain that catalyzes the reduction of oxygen to water. May be involved in cytochrome c oxidase activity. May play a role in the assembly of respiratory supercomplexes (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000255|PROSITE-ProRule:PRU00836}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00836}. Mitochondrion inner membrane {ECO:0000250}. SUBUNIT: Associates with cytochrome c oxidase (COX, complex IV); proposed complex component. {ECO:0000250}. +Q9R098 HGFA_MOUSE Hepatocyte growth factor activator (HGF activator) (HGFA) (EC 3.4.21.-) [Cleaved into: Hepatocyte growth factor activator short chain; Hepatocyte growth factor activator long chain] 653 70,568 Active site (3); Chain (2); Disulfide bond (19); Domain (6); Glycosylation (6); Propeptide (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Activates hepatocyte growth factor (HGF) by converting it from a single chain to a heterodimeric form. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Secreted as an inactive single-chain precursor and is then activated to a heterodimeric form. {ECO:0000250}. SUBUNIT: Heterodimer of a short chain and a long chain linked by a disulfide bond. {ECO:0000250}. +Q9JLS0 HLPDA_MOUSE Hypoxia-inducible lipid droplet-associated protein (Hypoxia-inducible gene 2 protein) 64 7,007 Chain (1); Region (1); Sequence conflict (1); Transmembrane (1) TRANSMEM 7 24 Helical. {ECO:0000255}. FUNCTION: Increases intracellular lipid accumulation. Stimulates expression of cytokines including IL6, MIF and VEGFA. Enhances cell growth and proliferation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Lipid droplet {ECO:0000250}. Secreted {ECO:0000250}. Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q9DC33 HM20A_MOUSE High mobility group protein 20A (HMG box-containing protein 20A) (HMG domain-containing protein HMGX1) (Inhibitor of BRAF35) (iBRAF) 346 39,917 Alternative sequence (5); Chain (1); Coiled coil (1); DNA binding (1); Erroneous initiation (1); Modified residue (1); Sequence conflict (2) FUNCTION: Plays a role in neuronal differentiation as chromatin-associated protein. Acts as inhibitor of HMG20B. Overcomes the repressive effects of the neuronal silencer REST and induces the activation of neuronal-specific genes. Involved in the recruitment of the histone methyltransferase KMT2A/MLL1 and consequent increased methylation of histone H3 lysine 4. {ECO:0000269|PubMed:16227968}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}. TISSUE SPECIFICITY: Expressed in brain. Detected in mature neurons. {ECO:0000269|PubMed:16227968}. +Q9Z104 HM20B_MOUSE SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1-related (SMARCE1-related protein) (BRCA2-associated factor 35) (HMG box-containing protein 20B) (Structural DNA-binding protein BRAF35) 317 35,870 Chain (1); Coiled coil (1); Cross-link (1); DNA binding (1); Helix (4); Modified residue (1) FUNCTION: Required for correct progression through G2 phase of the cell cycle and entry into mitosis. Required for RCOR1/CoREST mediated repression of neuronal specific gene promoters (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}. Chromosome {ECO:0000250}. Note=Localized to condensed chromosomes in mitosis in conjunction with BRCA2. {ECO:0000250}. SUBUNIT: Component of a BHC histone deacetylase complex that contains HDAC1, HDAC2, HMG20B/BRAF35, KDM1A, RCOR1/CoREST and PHF21A/BHC80. The BHC complex may also contain ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I. Interacts with the BRCA2 tumor suppressor protein (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed in adult tissues, particularly kidney, skin, testis and uterus. Highly expressed in embryonic tissues with high mitotic index, such as the proliferating ventricular zones of the fore-, mid- and hindbrain. +Q61670 HLX_MOUSE H2.0-like homeobox protein (Homeobox protein HLX1) 476 50,079 Chain (1); Compositional bias (3); DNA binding (1) FUNCTION: Transcription factor required for TBX21/T-bet-dependent maturation of Th1 cells as well as maintenance of Th1-specific gene expression. Involved in embryogenesis and hematopoiesis. {ECO:0000269|PubMed:12055627}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: Expressed in Th1 cells, CD8-positive T-cells, B-cells and NK cells. {ECO:0000269|PubMed:12055627}. +P09066 HME2_MOUSE Homeobox protein engrailed-2 (Homeobox protein en-2) (Mo-En-2) 324 33,817 Chain (1); Compositional bias (2); DNA binding (1) SUBCELLULAR LOCATION: Nucleus. TISSUE SPECIFICITY: Cerebellar granule cells. +Q9WV93 HEY1_MOUSE Hairy/enhancer-of-split related with YRPW motif protein 1 (Hairy and enhancer of split-related protein 1) (HESR-1) (Hairy-related transcription factor 1) (HRT-1) (mHRT1) 299 32,063 Chain (1); Domain (2); Motif (1); Region (1) FUNCTION: Transcriptional repressor which binds preferentially to the canonical E box sequence 5'-CACGTG-3'. Downstream effector of Notch signaling required for cardiovascular development. Specifically required for the Notch-induced endocardial epithelial to mesenchymal transition, which is itself criticial for cardiac valve and septum development. May be required in conjunction with HEY2 to specify arterial cell fate or identity. Promotes maintenance of neuronal precursor cells and glial versus neuronal fate specification. Represses transcription by the cardiac transcriptional activators GATA4 and GATA6 and by the neuronal bHLH factors ASCL1/MASH1 and NEUROD4/MATH3. {ECO:0000269|PubMed:11095750, ECO:0000269|PubMed:11486045, ECO:0000269|PubMed:12947105, ECO:0000269|PubMed:15107403, ECO:0000269|PubMed:15680351, ECO:0000269|PubMed:16199874, ECO:0000269|PubMed:17259303, ECO:0000269|PubMed:17303760}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00380, ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:11486044, ECO:0000269|PubMed:11741889}. SUBUNIT: May self-associate (By similarity). Interacts with HES1, NCOR1 and SIN3A (By similarity). Interacts with GATA4, GATA6 and HDAC1 and HEYL. Interacts with CCDC89/BOIP. {ECO:0000250, ECO:0000269|PubMed:11486045, ECO:0000269|PubMed:14648848, ECO:0000269|PubMed:16199874, ECO:0000269|PubMed:17303760}. TISSUE SPECIFICITY: Expressed in somitic mesoderm, brain, central nervous system, kidney, heart, nasal epithelium, limbs, lung, muscle, ovary and testis. {ECO:0000269|PubMed:10860664, ECO:0000269|PubMed:12947105}. +P29416 HEXA_MOUSE Beta-hexosaminidase subunit alpha (EC 3.2.1.52) (Beta-N-acetylhexosaminidase subunit alpha) (Hexosaminidase subunit A) (N-acetyl-beta-glucosaminidase subunit alpha) 528 60,613 Active site (1); Chain (1); Disulfide bond (3); Glycosylation (4); Propeptide (1); Region (1); Sequence conflict (6); Signal peptide (1) FUNCTION: Responsible for the degradation of GM2 gangliosides, and a variety of other molecules containing terminal N-acetyl hexosamines, in the brain and other tissues. SUBCELLULAR LOCATION: Lysosome. SUBUNIT: There are 3 forms of beta-hexosaminidase: hexosaminidase A is a trimer composed of one alpha chain, one beta-A chain and one beta-B chain; hexosaminidase B is a tetramer of two beta-A and two beta-B chains; hexosaminidase S is a homodimer of two alpha chains. The two beta chains are derived from the cleavage of a precursor chain (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. Most abundant in testis, adrenal, epididymis and heart. Low levels seen in the liver. {ECO:0000269|PubMed:7896264}. +Q3TVI4 HEXI2_MOUSE Protein HEXIM2 313 35,397 Chain (1); Coiled coil (1); Frameshift (1); Modified residue (4); Region (2) FUNCTION: Transcriptional regulator which functions as a general RNA polymerase II transcription inhibitor. In cooperation with 7SK snRNA sequesters P-TEFb in a large inactive 7SK snRNP complex preventing RNA polymerase II phosphorylation and subsequent transcriptional elongation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Homooligomer and heterooligomer with HEXIM1; probably dimeric. Component of the 7SK snRNP complex at least composed of P-TEFb (composed of CDK9 and CCNT1/cyclin-T1), HEXIM1, HEXIM2, BCDIN3, SART3 proteins and 7SK and U6 snRNAs. Interacts with CCNT2. {ECO:0000250|UniProtKB:Q96MH2}. DOMAIN: The coiled-coil domain mediates oligomerization. {ECO:0000250}. +Q99JY6 HIG1B_MOUSE HIG1 domain family member 1B 98 10,940 Chain (1); Domain (1); Sequence conflict (1); Topological domain (3); Transmembrane (2) TRANSMEM 29 46 Helical. {ECO:0000255|PROSITE-ProRule:PRU00836}.; TRANSMEM 61 83 Helical. {ECO:0000255|PROSITE-ProRule:PRU00836}. TOPO_DOM 1 28 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 47 60 Extracellular. {ECO:0000255}.; TOPO_DOM 84 98 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000255|PROSITE-ProRule:PRU00836}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00836}. +Q75VT8 HIDE1_MOUSE Protein HIDE1 (Highly expressed in immature dendritic cell transcript 1 protein) 222 23,594 Alternative sequence (1); Chain (1); Compositional bias (1); Glycosylation (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 121 141 Helical. {ECO:0000255}. TOPO_DOM 22 120 Extracellular. {ECO:0000255}.; TOPO_DOM 142 222 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. +Q14DK5 HIPL1_MOUSE HHIP-like protein 1 791 87,528 Alternative sequence (2); Chain (1); Compositional bias (1); Disulfide bond (7); Domain (1); Glycosylation (3); Sequence conflict (2); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +P97400 LEG10_MOUSE Galectin-10 (Gal-10) (Charcot-Leyden crystal protein homolog) (CLC) (Fragment) 68 8,037 Chain (1); Domain (1); Non-terminal residue (2) FUNCTION: Regulates immune responses through the recognition of cell-surface glycans. Essential for the anergy and suppressive function of CD25-positive regulatory T-cells (Treg) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Cytoplasmic granule {ECO:0000250}. Note=Localized in granules from where it may be secreted or transported to other locations in the cell. {ECO:0000250}. SUBUNIT: Interacts with CEL. {ECO:0000250}. +Q9D1G3 HHATL_MOUSE Protein-cysteine N-palmitoyltransferase HHAT-like protein (Glycerol uptake/transporter homolog) (Hedgehog acyltransferase-like protein) 503 56,431 Chain (1); Sequence conflict (1); Transmembrane (8) TRANSMEM 12 31 Helical. {ECO:0000255}.; TRANSMEM 65 87 Helical. {ECO:0000255}.; TRANSMEM 100 122 Helical. {ECO:0000255}.; TRANSMEM 127 149 Helical. {ECO:0000255}.; TRANSMEM 250 272 Helical. {ECO:0000255}.; TRANSMEM 287 309 Helical. {ECO:0000255}.; TRANSMEM 426 445 Helical. {ECO:0000255}.; TRANSMEM 460 482 Helical. {ECO:0000255}. FUNCTION: Negatively regulates N-terminal palmitoylation of SHH by HHAT/SKN. {ECO:0000269|PubMed:18081866}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18081866}; Multi-pass membrane protein {ECO:0000269|PubMed:18081866}. SUBUNIT: Interacts with SHH. {ECO:0000269|PubMed:18081866}. +P16110 LEG3_MOUSE Galectin-3 (Gal-3) (35 kDa lectin) (Carbohydrate-binding protein 35) (CBP 35) (Galactose-specific lectin 3) (IgE-binding protein) (L-34 galactoside-binding lectin) (Laminin-binding protein) (Lectin L-29) (Mac-2 antigen) 264 27,515 Chain (1); Disulfide bond (1); Domain (1); Initiator methionine (1); Modified residue (3); Motif (1); Region (2); Repeat (9); Sequence conflict (5) FUNCTION: Galactose-specific lectin which binds IgE. May mediate with the alpha-3, beta-1 integrin the stimulation by CSPG4 of endothelial cells migration. Together with DMBT1, required for terminal differentiation of columnar epithelial cells during early embryogenesis. In the nucleus: acts as a pre-mRNA splicing factor. Involved in acute inflammatory responses including neutrophil activation and adhesion, chemoattraction of monocytes macrophages, opsonization of apoptotic neutrophils, and activation of mast cells. Together with TRIM16, coordinates the recognition of membrane damage with mobilization of the core autophagy regulators ATG16L1 and BECN1 in response to damaged endomembranes. {ECO:0000250, ECO:0000269|PubMed:15181153}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Secreted. Note=Secreted by a non-classical secretory pathway and associates with the cell surface. SUBUNIT: Probably forms homo- or heterodimers. Interacts with DMBT1 (By similarity). Interacts with CD6 and ALCAM. Forms a complex with the ITGA3, ITGB1 and CSPG4. Interacts with LGALS3BP, LYPD3, CYHR1 and UACA. Interacts with TRIM16; this interaction mediates autophagy of damage endomembranes (By similarity). {ECO:0000250|UniProtKB:P08699, ECO:0000250|UniProtKB:P17931, ECO:0000269|PubMed:10745073, ECO:0000269|PubMed:14961764, ECO:0000269|PubMed:15181153}. TISSUE SPECIFICITY: The highest levels are found in activated macrophages. +Q8QZS1 HIBCH_MOUSE 3-hydroxyisobutyryl-CoA hydrolase, mitochondrial (EC 3.1.2.4) (3-hydroxyisobutyryl-coenzyme A hydrolase) (HIB-CoA hydrolase) (HIBYL-CoA-H) 385 43,038 Binding site (4); Chain (1); Modified residue (19); Transit peptide (1) Amino-acid degradation; L-valine degradation. FUNCTION: Hydrolyzes 3-hydroxyisobutyryl-CoA (HIBYL-CoA), a saline catabolite. Has high activity toward isobutyryl-CoA. Could be an isobutyryl-CoA dehydrogenase that functions in valine catabolism. Also hydrolyzes 3-hydroxypropanoyl-CoA (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. +Q8BJA3 HMBX1_MOUSE Homeobox-containing protein 1 419 47,116 Alternative sequence (3); Chain (1); Cross-link (8); DNA binding (1); Modified residue (2); Site (1) FUNCTION: Binds directly to 5'-TTAGGG-3' repeats in telomeric DNA (By similarity). Associates with the telomerase complex at sites of active telomere processing and positively regulates telomere elongation (By similarity). Important for TERT binding to chromatin, indicating a role in recruitment of the telomerase complex to telomeres (PubMed:23685356). Also plays a role in the alternative lengthening of telomeres (ALT) pathway in telomerase-negative cells where it promotes formation and/or maintenance of ALT-associated promyelocytic leukemia bodies (APBs) (By similarity). Enhances formation of telomere C-circles in ALT cells, suggesting a possible role in telomere recombination (By similarity). Might also be involved in the DNA damage response at telomeres (By similarity). {ECO:0000250|UniProtKB:Q6NT76, ECO:0000269|PubMed:23685356}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23685356}. Cytoplasm {ECO:0000250|UniProtKB:Q6NT76}. Chromosome, telomere {ECO:0000269|PubMed:23685356}. Nucleus, Cajal body {ECO:0000250|UniProtKB:Q6NT76}. Nucleus, PML body {ECO:0000250|UniProtKB:Q6NT76}. Note=Predominantly detected in cytoplasm. Localizes in a dynamic manner to actively processed telomeres. Localizes to the periphery of Cajal bodies. Associates with PML nuclear bodies in telomerase-negative cells. {ECO:0000250|UniProtKB:Q6NT76}. SUBUNIT: Associates with the telomerase holoenzyme complex. Interacts with DKC1, XRCC6 and COIL. {ECO:0000250|UniProtKB:Q6NT76}. DOMAIN: The homeobox domain is required for binding to 5'-TTAGGG-3' repeats in telomeres, and for telomere localization. {ECO:0000250|UniProtKB:Q6NT76}. +Q8JZK9 HMCS1_MOUSE Hydroxymethylglutaryl-CoA synthase, cytoplasmic (HMG-CoA synthase) (EC 2.3.3.10) (3-hydroxy-3-methylglutaryl coenzyme A synthase) 520 57,569 Active site (3); Binding site (4); Chain (1); Modified residue (5); Region (1) Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 2/3. FUNCTION: This enzyme condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA, which is the substrate for HMG-CoA reductase. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q01581}. +P38060 HMGCL_MOUSE Hydroxymethylglutaryl-CoA lyase, mitochondrial (HL) (HMG-CoA lyase) (EC 4.1.3.4) (3-hydroxy-3-methylglutarate-CoA lyase) 325 34,239 Active site (1); Binding site (1); Chain (1); Disulfide bond (1); Domain (1); Metal binding (4); Modified residue (8); Motif (1); Sequence conflict (4); Transit peptide (1) Metabolic intermediate metabolism; (S)-3-hydroxy-3-methylglutaryl-CoA degradation; acetoacetate from (S)-3-hydroxy-3-methylglutaryl-CoA: step 1/1. FUNCTION: Key enzyme in ketogenesis (ketone body formation). Terminal step in leucine catabolism. Ketone bodies (beta-hydroxybutyrate, acetoacetate and acetone) are essential as an alternative source of energy to glucose, as lipid precursors and as regulators of metabolism (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:7527399}. Peroxisome {ECO:0000269|PubMed:7527399}. Note=Unprocessed form is peroxisomal. SUBUNIT: Homodimer; disulfide-linked. Can also form homotetramers. {ECO:0000250}. +Q8VHD8 HORN_MOUSE Hornerin 2496 247,587 Calcium binding (2); Chain (1); Domain (2); Modified residue (19); Region (2); Repeat (28) FUNCTION: Component of the epidermal cornified cell envelopes. PTM: Processed during the process of epidermal differentiation.; PTM: Forms covalent cross-links mediated by transglutaminase TGM3, between glutamine and the epsilon-amino group of lysine residues (in vitro). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasmic granule. Note=Found in keratohyalin granules of the granular cells of the epidermis. TISSUE SPECIFICITY: Embryonic skin. Highest level in the adult forestomach followed by the skin. Lower levels in the tongue, esophagus. Detected in the granular and cornified layers of the mature epidermis. {ECO:0000269|PubMed:12642627}. +P18608 HMGN1_MOUSE Non-histone chromosomal protein HMG-14 (High mobility group nucleosome-binding domain-containing protein 1) 96 10,152 Chain (1); Initiator methionine (1); Modified residue (10) FUNCTION: Binds to the inner side of the nucleosomal DNA thus altering the interaction between the DNA and the histone octamer. May be involved in the process which maintains transcribable genes in a unique chromatin conformation. Inhibits the phosphorylation of nucleosomal histones H3 and H2A by RPS6KA5/MSK1 and RPS6KA3/RSK2. {ECO:0000269|PubMed:15327773}. PTM: Phosphorylation favors cytoplasmic localization (By similarity). Phosphorylation on Ser-20 and Ser-24 weakens binding to nucleosomes and increases the rate of H3 phosphorylation. {ECO:0000250, ECO:0000269|PubMed:15327773, ECO:0000269|PubMed:7925294}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm {ECO:0000250}. Note=Cytoplasmic enrichment upon phosphorylation. {ECO:0000250}. +Q8VEK3 HNRPU_MOUSE Heterogeneous nuclear ribonucleoprotein U (hnRNP U) (Scaffold-attachment factor A) (SAF-A) 800 87,918 Alternative sequence (1); Chain (1); Coiled coil (1); Compositional bias (2); Cross-link (14); Domain (2); Initiator methionine (1); Modified residue (35); Nucleotide binding (1); Region (3); Site (1) FUNCTION: DNA- and RNA-binding protein involved in several cellular processes such as nuclear chromatin organization, telomere-length regulation, transcription, mRNA alternative splicing and stability, Xist-mediated transcriptional silencing and mitotic cell progression (PubMed:20833368, PubMed:21235343, PubMed:22162999, PubMed:26244333). Plays a role in the regulation of interphase large-scale gene-rich chromatin organization through chromatin-associated RNAs (caRNAs) in a transcription-dependent manner, and thereby maintains genomic stability (By similarity). Required for the localization of the long non-coding Xist RNA on the inactive chromosome X (Xi) and the subsequent initiation and maintenance of X-linked transcriptional gene silencing during X-inactivation (PubMed:20833368, PubMed:26244333). Plays a role as a RNA polymerase II (Pol II) holoenzyme transcription regulator (PubMed:21235343, PubMed:22162999). Promotes transcription initiation by direct association with the core-TFIIH basal transcription factor complex for the assembly of a functional pre-initiation complex with Pol II in a actin-dependent manner. Blocks Pol II transcription elongation activity by inhibiting the C-terminal domain (CTD) phosphorylation of Pol II and dissociates from Pol II pre-initiation complex prior to productive transcription elongation. Positively regulates CBX5-induced transcriptional gene silencing and retention of CBX5 in the nucleus. Negatively regulates glucocorticoid-mediated transcriptional activation (By similarity). Key regulator of transcription initiation and elongation in embryonic stem cells upon leukemia inhibitory factor (LIF) signaling (PubMed:21235343). Involved in the long non-coding RNA H19-mediated Pol II transcriptional repression (By similarity). Participates in the circadian regulation of the core clock component ARNTL/BMAL1 transcription (PubMed:18332112). Plays a role in the regulation of telomere length. Plays a role as a global pre-mRNA alternative splicing modulator by regulating U2 small nuclear ribonucleoprotein (snRNP) biogenesis. Plays a role in mRNA stability. Component of the CRD-mediated complex that promotes MYC mRNA stabilization. Enhances the expression of specific genes, such as tumor necrosis factor TNFA, by regulating mRNA stability, possibly through binding to the 3'-untranslated region (UTR). Plays a role in mitotic cell cycle regulation. Involved in the formation of stable mitotic spindle microtubules (MTs) attachment to kinetochore, spindle organization and chromosome congression. Phosphorylation at Ser-58 by PLK1 is required for chromosome alignement and segregation and progression through mitosis. Contributes also to the targeting of AURKA to mitotic spindle MTs. Binds to double- and single-stranded DNA and RNA, poly(A), poly(C) and poly(G) oligoribonucleotides. Binds to chromatin-associated RNAs (caRNAs). Associates with chromatin to scaffold/matrix attachment region (S/MAR) elements in a chromatin-associated RNAs (caRNAs)-dependent manner (By similarity). Binds (via RNA-binding RGG-box region) to the long non-coding Xist RNA; this binding is direct and bridges the Xist RNA and the inactive chromosome X (Xi) (PubMed:20833368, PubMed:26244333). Binds the long non-coding H19 RNA. Binds to SMN1/2 pre-mRNAs at G/U-rich regions. Binds to small nuclear RNAs (snRNAs). Binds to the 3'-UTR of TNFA mRNA (By similarity). Also negatively regulates embryonic stem cell differentiation upon LIF signaling (PubMed:21235343). Required for embryonic development (PubMed:16022389). Binds to brown fat long non-coding RNA 1 (Blnc1); facilitates the recruitment of Blnc1 by ZBTB7B required to drive brown and beige fat development and thermogenesis (PubMed:28784777). {ECO:0000250|UniProtKB:Q00839, ECO:0000269|PubMed:16022389, ECO:0000269|PubMed:18332112, ECO:0000269|PubMed:20833368, ECO:0000269|PubMed:21235343, ECO:0000269|PubMed:22162999, ECO:0000269|PubMed:26244333, ECO:0000269|PubMed:28784777}. PTM: Cleaved at Asp-94 by CASP3 during T-cell apoptosis, resulting in a loss of DNA- and chromatin-binding activities. {ECO:0000250|UniProtKB:Q00839}.; PTM: Extensively phosphorylated. Phosphorylated on Ser-58 by PLK1 and dephosphorylated by protein phosphatase 2A (PP2A) in mitosis. {ECO:0000250|UniProtKB:Q00839}.; PTM: Arg-709 and Arg-715 are dimethylated, probably to asymmetric dimethylarginine.; PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18332112, ECO:0000269|PubMed:22162999}. Nucleus matrix {ECO:0000250|UniProtKB:Q00839}. Chromosome {ECO:0000269|PubMed:20833368}. Nucleus speckle {ECO:0000250|UniProtKB:Q00839}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q00839}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q00839}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q00839}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q00839}. Midbody {ECO:0000250|UniProtKB:Q00839}. Cytoplasm {ECO:0000250|UniProtKB:Q00839}. Cell surface {ECO:0000250|UniProtKB:Q00839}. Cytoplasmic granule {ECO:0000250|UniProtKB:Q00839}. Note=Localizes at inactive X chromosome (Xi) regions (PubMed:20833368). Localizes in the nucleus during interphase. At metaphase, localizes with mitotic spindle microtubules (MTs). At anaphase, localizes in the mitotic spindle midzone. Localizes in spindle MTs proximal to spindle poles in a TPX2- and AURKA-dependent manner. The Ser-58 phosphorylated form localizes to centrosomes during prophase and metaphase, to mitotic spindles in anaphase and to the midbody during cytokinesis (By similarity). Colocalizes with SMARCA4 in the nucleus (PubMed:22162999). Colocalizes with CBX5 in the nucleus. Colocalizes with NR3C1 in nuclear speckles. Localized in cytoplasmic ribonucleoprotein (RNP) granules containing untranslated mRNAs (By similarity). {ECO:0000250|UniProtKB:Q00839, ECO:0000269|PubMed:20833368, ECO:0000269|PubMed:22162999}. SUBUNIT: Oligomer (via ATPase domain and RNA-binding RGG-box region); oligomerization occurs upon ATP-binding in a chromatin-associated RNAs (caRNAs)- and transcription-dependent manner and is required for chromatin decompaction. ATP hydrolysis is required to cycle from an oligomeric to monomeric state to compact chromatin. Component of the coding region determinant (CRD)-mediated complex, composed of DHX9, HNRNPU, IGF2BP1, SYNCRIP and YBX1. Identified in the spliceosome C complex. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Associates with heterogeneous nuclear ribonucleoprotein (hnRNP) particles (By similarity). Associates (via middle region) with the C-terminal domain (CTD) RNA polymerase II (Pol II) holoenzyme; this association occurs in a RNA-independent manner (PubMed:21235343). Associates (via middle region) with the core-TFIIH basal transcription factor complex; this association inhibits the CTD phosphorylation of RNA polymerase II holoenzyme by downregulating TFIIH kinase activity. Associates with the telomerase holoenzyme complex. Associates with spindle microtubules (MTs) in a TPX2-dependent manner. Interacts (via C-terminus) with actin; this interaction is direct and mediates association with the phosphorylated CTD of RNA polymerase II and is disrupted in presence of the long non-coding H19 RNA. Interacts with AURKA. Interacts (via C-terminus) with CBX5; this interaction is, at least in part, RNA-dependent. Interacts with CR2 (By similarity). Interacts with CRY1 (PubMed:19129230). Interacts (via C-terminus) with EP300; this interaction enhances DNA-binding to nuclear scaffold/matrix attachment region (S/MAR) elements. Interacts with ERBB4. Interacts with GEMIN5. Interacts with IGF2BP1. Interacts with IGF2BP2 and IGF2BP3. Interacts with NCL; this interaction occurs during mitosis. Interacts (via C-terminus) with NR3C1 (via C-terminus). Interacts with PLK1; this interaction induces phosphorylation of HNRNPU at Ser-58 in mitosis. Interacts with POU3F4 (By similarity). Interacts with SMARCA4; this interaction occurs in embryonic stem cells and stimulates global Pol II-mediated transcription (PubMed:22162999). Interacts (via C-terminus) with TOP2A; this interaction protects the topoisomerase TOP2A from degradation and positively regulates the relaxation of supercoiled DNA by TOP2A in a RNA-dependent manner. Interacts with TPX2; this interaction recruits HNRNPU to spindle microtubules (MTs). Interacts with UBQLN2 (By similarity). Interacts (via RNA-binding RGG-box region) with ZBTB7B; the interaction facilitates the recruitment of long non-coding RNA Blnc1 by ZBTB7B (PubMed:28784777). {ECO:0000250|UniProtKB:Q00839, ECO:0000250|UniProtKB:Q6IMY8, ECO:0000269|PubMed:19129230, ECO:0000269|PubMed:21235343, ECO:0000269|PubMed:22162999, ECO:0000269|PubMed:28784777}. DOMAIN: The SAP domain is necessary for specific binding to nuclear scaffold/matrix attachment region (S/MAR) elements in DNA. The RNA-binding RGG-box region is necessary for its association with inactive X chromosome (Xi) regions and to chromatin-associated RNAs (caRNAs) (By similarity). Both the DNA-binding domain SAP and the RNA-binding RGG-box region are necessary for the localization of Xist RNA on the Xi (PubMed:20833368). The ATPase and RNA-binding RGG-box regions are necessary for oligomerization (By similarity). {ECO:0000250|UniProtKB:Q00839, ECO:0000269|PubMed:20833368}. +O08983 HPS1_MOUSE Hermansky-Pudlak syndrome 1 protein homolog 704 79,853 Chain (1); Compositional bias (2); Erroneous initiation (1); Natural variant (4); Repeat (3); Sequence conflict (2) FUNCTION: Component of the BLOC-3 complex, a complex that acts as a guanine exchange factor (GEF) for RAB32 and RAB38, promotes the exchange of GDP to GTP, converting them from an inactive GDP-bound form into an active GTP-bound form. The BLOC-3 complex plays an important role in the control of melanin production and melanosome biogenesis and promotes the membrane localization of RAB32 and RAB38. {ECO:0000250|UniProtKB:Q92902}. SUBUNIT: Component of the biogenesis of lysosome-related organelles complex-3 (or BLOC-3), a heterodimer of HPS1 and HPS4. HPS1 cannot but BLOC-3 complex (heterodimer of HPS1 and HPS4) can interact with the GTP-bound form of RAB9A and RAB9B. HPS1 and BLOC-3 complex do not interact with the GDP-bound form of RAB9A and RAB9B. {ECO:0000250|UniProtKB:Q92902}. TISSUE SPECIFICITY: Expressed in all tissues examined with the possible exception of skeletal muscle. The highest expression was observed in lung, liver, kidney and spleen. DISEASE: Note=Defects in Hps1 are the cause of the pale ear (ep) mutant which exhibits hypopigmentation associated with defects of multiple cytoplasmic organelles, including melanosomes, lysosomes, and granular elements of platelets (PubMed:9256466). {ECO:0000269|PubMed:9256466}. +Q3TBD2 HMHA1_MOUSE Rho GTPase-activating protein 45 (Minor histocompatibility protein HA-1) 1116 122,902 Alternative sequence (4); Chain (1); Coiled coil (1); Domain (2); Modified residue (12); Sequence conflict (7); Zinc finger (1) FUNCTION: Contains a GTPase activator for the Rho-type GTPases (RhoGAP) domain that would be able to negatively regulate the actin cytoskeleton as well as cell spreading. However, also contains N-terminally a BAR-domin which is able to play an autoinhibitory effect on this RhoGAP activity. {ECO:0000250|UniProtKB:Q92619}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q92619}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q92619}. DOMAIN: Rho-GAP domain is able to regulate RhoGTPase activity, actin cytoskeleton and cell spreading. However N-terminally BAR domain plays an autoinhibitory role. {ECO:0000250|UniProtKB:Q92619}. +O70218 HMX1_MOUSE Homeobox protein HMX1 (Homeobox protein H6) 332 35,054 Chain (1); Compositional bias (4); DNA binding (1); Motif (2) FUNCTION: DNA-binding protein that binds to the 5'-CAAG-3' core sequence. May function as a transcriptional repressor. Seems to act as a transcriptional antagonist of NKX2-5. May play an important role in the development of craniofacial structures such as the eye and ear. {ECO:0000269|PubMed:9628823}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: Expressed in neural crest-derived tissues, including, nerve ganglia and cranial mesenchyme. {ECO:0000269|PubMed:9628823}. +Q9WUU6 HNF4G_MOUSE Hepatocyte nuclear factor 4-gamma (HNF-4-gamma) (Nuclear receptor subfamily 2 group A member 2) 408 45,897 Chain (1); DNA binding (1); Domain (1); Erroneous initiation (1); Modified residue (4); Zinc finger (2) FUNCTION: Transcription factor. Has a lower transcription activation potential than HNF4-alpha (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}. +O08755 HNF6_MOUSE Hepatocyte nuclear factor 6 (HNF-6) (One cut domain family member 1) (One cut homeobox 1) 465 50,952 Beta strand (3); Chain (1); Compositional bias (3); DNA binding (2); Helix (7) FUNCTION: Transcriptional activator. Binds the consensus sequence 5'-DHWATTGAYTWWD-3' on a variety of gene promoters such as those of HNF3B and TTR. Important for liver genes transcription. Stimulates the expression of Onecut3 in the developing endoderm. {ECO:0000269|PubMed:15381696}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Binds DNA as a monomer. {ECO:0000269|PubMed:15169783}. +Q5SQP1 HORM2_MOUSE HORMA domain-containing protein 2 306 34,812 Alternative sequence (2); Chain (1); Domain (1); Modified residue (1) FUNCTION: Essential for synapsis surveillance during meiotic prophase via the recruitment of ATR activity. Plays a key role in the male mid-pachytene checkpoint and the female meiotic prophase checkpoint: required for efficient build-up of ATR activity on unsynapsed chromosome regions, a process believed to form the basis of meiotic silencing of unsynapsed chromatin (MSUC) and meiotic prophase quality control in both sexes. Required for the DNA double-strand break-independent, BRCA1-dependent activation of ATR on the sex chromosomes that is essential for normal sex body formation. {ECO:0000269|PubMed:22549958, ECO:0000269|PubMed:23039116}. PTM: Phosphorylated in a SPO11-dependent manner. {ECO:0000269|PubMed:22346761, ECO:0000269|PubMed:23039116}. SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Preferentially localizes to unsynapsed or desynapsed chromosomal regions during the male and female prophase I stage of meiosis. TRIP13 is required for depletion from synapsed chromosomes. SUBUNIT: Interacts with HORMAD1. {ECO:0000269|PubMed:22549958}. TISSUE SPECIFICITY: Specifically expressed in meiotic germ cells. {ECO:0000269|PubMed:19851446}. +Q9Z130 HNRDL_MOUSE Heterogeneous nuclear ribonucleoprotein D-like (hnRNP D-like) (hnRNP DL) (JKT41-binding protein) 301 33,559 Chain (1); Compositional bias (3); Cross-link (1); Domain (2); Modified residue (6); Region (1) FUNCTION: Acts as a transcriptional regulator. Promotes transcription repression (By similarity). Promotes transcription activation in differentiated myotubes. Binds to double- and single-stranded DNA sequences (By similarity). Binds to the transcription suppressor CATR sequence of the COX5B promoter. Binds with high affinity to RNA molecules that contain AU-rich elements (AREs) found within the 3'-UTR of many proto-oncogenes and cytokine mRNAs (By similarity). Binds both to nuclear and cytoplasmic poly(A) mRNAs (By similarity). Binds to poly(G) and poly(A), but not to poly(U) or poly(C) RNA homopolymers (By similarity). Binds to the 5'-ACUAGC-3' RNA consensus sequence (By similarity). {ECO:0000250, ECO:0000269|PubMed:15190078}. PTM: Dimethylation of Arg-289 is probably of the asymmetric type. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10717477, ECO:0000269|PubMed:15190078}. Cytoplasm {ECO:0000250|UniProtKB:O14979}. Note=Shuttles between the nucleus and the cytoplasm in a TNPO1-dependent manner. {ECO:0000250|UniProtKB:O14979}. SUBUNIT: Interacts with TNPO1 (By similarity). Interacts with ZNF148. {ECO:0000250, ECO:0000269|PubMed:15190078}. TISSUE SPECIFICITY: Expressed in skeletal muscle, myoblast, myotube, heart, brain, liver, kidney, heart, lung, stomach, small intestine, large intestine, spleen, and testis (at protein level). Expressed in brain, skeletal muscle, heart, lung, liver, stomach, small intestine, large intestine, kidney, spleen and testis. {ECO:0000269|PubMed:10717477}. +Q8R081 HNRPL_MOUSE Heterogeneous nuclear ribonucleoprotein L (hnRNP L) 586 63,964 Beta strand (11); Chain (1); Compositional bias (2); Cross-link (5); Domain (4); Erroneous initiation (1); Helix (5); Modified residue (9); Sequence conflict (1); Turn (2) FUNCTION: Splicing factor binding to exonic or intronic sites and acting as either an activator or repressor of exon inclusion (PubMed:22523384). Exhibits a binding preference for CA-rich elements. Component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes and associated with most nascent transcripts. Associates, together with APEX1, to the negative calcium responsive element (nCaRE) B2 of the APEX2 promoter. {ECO:0000250|UniProtKB:P14866, ECO:0000269|PubMed:22523384}. PTM: Phosphorylation at Ser-541 by CaMK4 enhances interaction with a CaMK4-responsive RNA element (CaRRE1), and prevents inclusion of the stress axis-regulated exon (STREX) of the KCNMA1 potassium channel transcripts upon membrane depolarization. {ECO:0000250|UniProtKB:P14866}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P14866}. Cytoplasm {ECO:0000250|UniProtKB:P14866}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. These granules are not identical with P bodies or stress granules. {ECO:0000250|UniProtKB:P14866}. SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with HNRNPLL. Interacts with APEX1; the interaction is DNA-dependent. Component of a complex with SETD2 (By similarity). Interacts with ELAVL1 (By similarity). {ECO:0000250|UniProtKB:F1LQ48, ECO:0000250|UniProtKB:P14866}. DOMAIN: RRM domain 2 has moderate RNA-binding affinity. RRM domains 3 and 4 may facilitate RNA looping when binding to two appropriately separated binding sites within the same target pre-mRNA. {ECO:0000250|UniProtKB:P14866}. TISSUE SPECIFICITY: Detected in hematopoietic cells, including lymphoid progenitor cells. {ECO:0000269|PubMed:22523384}. +Q9JHF7 HPGDS_MOUSE Hematopoietic prostaglandin D synthase (H-PGDS) (EC 5.3.99.2) (GST class-sigma) (Glutathione S-transferase) (EC 2.5.1.18) (Glutathione-dependent PGD synthase) (Glutathione-requiring prostaglandin D synthase) (Prostaglandin-H2 D-isomerase) 199 23,227 Binding site (3); Chain (1); Domain (2); Region (2); Sequence conflict (1) FUNCTION: Bifunctional enzyme which catalyzes both the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation, and the conjugation of glutathione with a wide range of aryl halides and organic isothiocyanates. Also exhibits low glutathione-peroxidase activity. {ECO:0000269|PubMed:10824118, ECO:0000269|PubMed:16547010}. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in skin and oviduct. {ECO:0000269|PubMed:10824118}. +Q91VB4 HPS3_MOUSE Hermansky-Pudlak syndrome 3 protein homolog (Cocoa protein) 1002 113,182 Chain (1); Sequence conflict (4) FUNCTION: Involved in early stages of melanosome biogenesis and maturation. {ECO:0000269|PubMed:11707070}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11707070}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q969F9}. SUBUNIT: Component of the biogenesis of lysosome-related organelles complex-2 (or BLOC2) composed of HPS3, HPS5 and HPS6. Interacts with HPS5 and HPS6. {ECO:0000250|UniProtKB:Q969F9}. TISSUE SPECIFICITY: Found in heart, brain, spleen, liver, lung, kidney and testis. {ECO:0000269|PubMed:11707070}. DISEASE: Note=Defects in Hps3 are the cause of the cocoa (coa) mutant, which is characterized by hypopigmentation and platelet dysfunction (PubMed:11707070). {ECO:0000269|PubMed:11707070}. +Q9QZU4 HRSL1_MOUSE Phospholipid-metabolizing enzyme A-C1 (EC 2.3.1.-) (EC 3.1.1.-) (HRAS-like suppressor 1) (HRSL1) 167 18,810 Active site (2); Chain (1); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 140 163 Helical. {ECO:0000255}. TOPO_DOM 1 139 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 164 167 Lumenal. {ECO:0000255}. FUNCTION: Exhibits calcium-independent phospholipase activity towards phosphatidylcholine (PC) and phosphatidylethanolamine (PE). Also shows acyltransferase activities, transferring an acyl group of PCs to the amino group of PEs and the hydroxyl group of lyso PCs. {ECO:0000269|PubMed:21880860}. SUBCELLULAR LOCATION: Cytoplasm. Membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Expressed in skeletal muscle, heart, brain and bone marrow. +Q61699 HS105_MOUSE Heat shock protein 105 kDa (42 degrees C-HSP) (Heat shock 110 kDa protein) (Heat shock-related 100 kDa protein E7I) (HSP-E7I) 858 96,407 Alternative sequence (1); Chain (1); Initiator methionine (1); Modified residue (8); Sequence conflict (16) FUNCTION: Acts as a nucleotide-exchange factor (NEF) for chaperone proteins HSPA1A and HSPA1B, promoting the release of ADP from HSPA1A/B thereby triggering client/substrate protein release (By similarity). Prevents the aggregation of denatured proteins in cells under severe stress, on which the ATP levels decrease markedly. Inhibits HSPA8/HSC70 ATPase and chaperone activities (PubMed:14644449, PubMed:15292236). {ECO:0000250|UniProtKB:Q92598, ECO:0000269|PubMed:14644449, ECO:0000269|PubMed:15292236}. PTM: Phosphorylation on Ser-509 may be important for regulation of the HSPA8/HSC70 chaperone activity. {ECO:0000269|PubMed:10772927, ECO:0000269|PubMed:12558502}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10865058}. Nucleus {ECO:0000269|PubMed:10865058}. Note=Strictly cytoplasmic in neurons. SUBUNIT: Interacts with HSPA8/HSC70 (PubMed:15292236, PubMed:9675148). Interacts with HSPA1A (via NBD) and HSPA1B (via NBD) (By similarity). {ECO:0000250|UniProtKB:Q92598, ECO:0000269|PubMed:15292236, ECO:0000269|PubMed:9675148}. TISSUE SPECIFICITY: Highly expressed in testis. Present at lower levels in most brain regions, except cerebellum. Within the brain, expression is restricted to neurons (at protein level). Overexpressed in cancer cells. {ECO:0000269|PubMed:10865058, ECO:0000269|PubMed:16232202}. +B2RXB2 HSBPL_MOUSE Heat shock factor-binding protein 1-like protein 1 72 8,101 Chain (1); Coiled coil (1) +Q8R3H7 HS2ST_MOUSE Heparan sulfate 2-O-sulfotransferase 1 (2-O-sulfotransferase) (2-OST) (2OST) (EC 2.8.2.-) 356 41,813 Active site (1); Chain (1); Disulfide bond (2); Glycosylation (2); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 12 28 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 11 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 29 356 Lumenal. {ECO:0000255}. FUNCTION: Catalyzes the transfer of sulfate to the C2-position of selected hexuronic acid residues within the maturing heparan sulfate (HS). 2-O-sulfation within HS, particularly of iduronate residues, is essential for HS to participate in a variety of high-affinity ligand-binding interactions and signaling processes. Required for metanephric development of kidney formation, suggesting that 2-O-sulfation within HS is essential for signaling between ureteric bud and metanephric mesenchyme. Mediates 2-O-sulfation of both L-iduronyl and D-glucuronyl residues. {ECO:0000269|PubMed:11331020, ECO:0000269|PubMed:11457822, ECO:0000269|PubMed:9637690}. PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:11687650}; Single-pass type II membrane protein {ECO:0000269|PubMed:11687650}. SUBUNIT: Homotrimer (By similarity). Interacts with the C5-epimerase GLCE. {ECO:0000250, ECO:0000269|PubMed:11687650}. TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in lung and brain. Weakly expressed in spleen. {ECO:0000269|PubMed:11331020, ECO:0000269|PubMed:9637690}. +P07901 HS90A_MOUSE Heat shock protein HSP 90-alpha (Heat shock 86 kDa) (HSP 86) (HSP86) (Tumor-specific transplantation 86 kDa antigen) (TSTA) 733 84,788 Beta strand (8); Binding site (5); Chain (1); Helix (9); Initiator methionine (1); Modified residue (17); Motif (1); Region (5); Sequence conflict (3); Turn (2) FUNCTION: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle. Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels. In the first place, they alter the steady-state levels of certain transcription factors in response to various physiological cues. Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes. Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation. {ECO:0000250|UniProtKB:P07900}. PTM: ISGylated. {ECO:0000269|PubMed:16139798}.; PTM: S-nitrosylated; negatively regulates the ATPase activity and the activation of eNOS by HSP90AA1. {ECO:0000250|UniProtKB:P07900}.; PTM: Ubiquitinated via 'Lys-63'-linked polyubiquitination by HECTD1. Ubiquitination promotes translocation into the cytoplasm away from the membrane and secretory pathways. {ECO:0000269|PubMed:22431752}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22431752}. Cytoplasm {ECO:0000269|PubMed:11751894, ECO:0000269|PubMed:22431752}. Melanosome {ECO:0000250|UniProtKB:P07900}. Cell membrane {ECO:0000250|UniProtKB:P07900}. SUBUNIT: Homodimer (PubMed:8289821). Identified in NR3C1/GCR steroid receptor-chaperone complexes formed at least by NR3C1, HSP90AA1 and a variety of proteins containing TPR repeats such as FKBP4, FKBP5, PPID, PPP5C or STIP1 (PubMed:9195923, PubMed:11278753, PubMed:11751894). Forms a complex containing HSP90AA1, TSC1 and TSC2; TSC1 is required to recruit TCS2 to the complex (By similarity). The closed form interacts (via the middle domain and TPR repeat-binding motif) with co-chaperone TSC1 (via C-terminus) (PubMed:29127155). Interacts with TOM34 (By similarity). Interacts with TERT; the interaction, together with PTGES3, is required for correct assembly and stabilization of the TERT holoenzyme complex (By similarity). Interacts with CHORDC1 and DNAJC7 (By similarity). Interacts with STUB1 and UBE2N; may couple the chaperone and ubiquitination systems (By similarity). Interacts (via TPR repeat-binding motif) with PPP5C (via TPR repeats); the interaction is direct and activates PPP5C phosphatase activity (By similarity). Following LPS binding, may form a complex with CXCR4, GDF5 and HSPA8 (By similarity). Interacts with KSR1 (PubMed:10409742). Interacts with co-chaperone CDC37 (via C-terminus); the interaction inhibits HSP90AA1 ATPase activity (By similarity). May interact with NWD1 (By similarity). Interacts with FNIP1 and FNIP2; the interaction inhibits HSP90AA1 ATPase activity (By similarity). Interacts with co-chaperone AHSA1 (phosphorylated on 'Tyr-223'); the interaction activates HSP90AA1 ATPase activity and results in the dissociation of TSC1 from HSP90AA1 (PubMed:29127155). Interacts with FLCN in the presence of FNIP1 (By similarity). Interacts with HSP70, STIP1 and PTGES3 (By similarity). Interacts with SMYD3; this interaction enhances SMYD3 histone-lysine N-methyltransferase (By similarity). Interacts with SGTA (via TPR repeats) (By similarity). Interacts with TTC1 (via TPR repeats) (By similarity). Interacts with HSF1 in an ATP-dependent manner (By similarity). Interacts with MET; the interaction suppresses MET kinase activity (By similarity). Interacts with ERBB2 in an ATP-dependent manner; the interaction suppresses ERBB2 kinase activity (By similarity). Interacts with HIF1A, KEAP1 and RHOBTB2 (By similarity). Interacts with HSF1; this interaction is decreased in a IER5-dependent manner, promoting HSF1 accumulation in the nucleus, homotrimerization and DNA-binding activities (By similarity). Interacts with STUB1 and SMAD3 (By similarity). Interacts with HSP90AB1; interaction is constitutive (By similarity). Interacts with HECTD1 (via N-terminus) (PubMed:22431752). {ECO:0000250|UniProtKB:P07900, ECO:0000269|PubMed:10409742, ECO:0000269|PubMed:11278753, ECO:0000269|PubMed:11751894, ECO:0000269|PubMed:22431752, ECO:0000269|PubMed:29127155, ECO:0000269|PubMed:8289821, ECO:0000269|PubMed:9195923}. DOMAIN: The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins like the co-chaperone STUB1. {ECO:0000250|UniProtKB:P07900}. +P38533 HSF2_MOUSE Heat shock factor protein 2 (HSF 2) (Heat shock transcription factor 2) (HSTF 2) 535 60,225 Alternative sequence (1); Chain (1); Cross-link (8); DNA binding (1); Region (2) FUNCTION: DNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription. In higher eukaryotes, HSF is unable to bind to the HSE unless the cells are heat shocked. HSF2 is expressed in a form that binds DNA constitutively but loses DNA binding by incubation at greater than 41 degrees C. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Cytoplasmic during normal growth and moves to the nucleus upon activation. SUBUNIT: DNA-binding homotrimer in stressed or heat shocked cells, otherwise found as a homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Isoform alpha is expressed predominantly in testis while isoform beta is expressed predominantly in heart and brain. {ECO:0000269|PubMed:7565677}. +P06798 HXA4_MOUSE Homeobox protein Hox-A4 (Homeobox protein Hox-1.4) (Homeobox protein MH-3) 285 30,468 Chain (1); DNA binding (1); Motif (1); Sequence conflict (11) FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Binds to sites in the 5'-flanking sequence of its coding region with various affinities. The consensus sequences of the high and low affinity binding sites are 5'-TAATGA[CG]-3' and 5'-CTAATTTT-3'. SUBCELLULAR LOCATION: Nucleus. DISEASE: Note=Overexpression results in abnormal gut development (megacolon). +P01806 HVM36_MOUSE Ig heavy chain V region 441 116 12,911 Chain (1); Domain (1); Non-terminal residue (1); Signal peptide (1) +P09631 HXA9_MOUSE Homeobox protein Hox-A9 (Homeobox protein Hox-1.7) 271 29,917 Alternative sequence (2); Chain (1); DNA binding (1); Helix (3); Modified residue (1); Turn (1) FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Required for induction of E-selectin and VCAM-1, on the endothelial cells surface at sites of inflammation (By similarity). {ECO:0000250}. PTM: Methylated on Arg-140 by PRMT5; methylation is critical for E-selectin induction. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Transiently interacts with PRMT5 in TNF-alpha stimulated endothelial cells. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in high level in the embryonic and adult spinal cord with a preference in the posterior region. +Q8VEI3 HYAL3_MOUSE Hyaluronidase-3 (Hyal-3) (EC 3.2.1.35) (Hyaluronoglucosaminidase-3) 412 46,132 Active site (1); Chain (1); Disulfide bond (5); Domain (1); Glycosylation (2); Sequence conflict (9); Signal peptide (1) FUNCTION: Facilitates sperm penetration into the layer of cumulus cells surrounding the egg by digesting hyaluronic acid. Involved in induction of the acrosome reaction in the sperm (PubMed:20586096). Involved in follicular atresia, the breakdown of immature ovarian follicles that are not selected to ovulate. Induces ovarian granulosa cell apoptosis, possibly via apoptotic signaling pathway involving CASP8 and CASP3 activation, and poly(ADP-ribose) polymerase (PARP) cleavage (PubMed:18653706). Has no hyaluronidase activity in embryonic fibroblasts in vitro (PubMed:18234732). Has no hyaluronidase activity in granulosa cells in vitro (PubMed:18653706). {ECO:0000269|PubMed:18234732, ECO:0000269|PubMed:18653706, ECO:0000269|PubMed:20586096}. PTM: N-glycosylated. {ECO:0000269|PubMed:18234732}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20586096}. Cell membrane {ECO:0000269|PubMed:20586096}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:20586096}. Endoplasmic reticulum {ECO:0000269|PubMed:18234732}. Early endosome {ECO:0000269|PubMed:18234732}. Note=Mostly present in low-density vesicles. Low levels in higher density vesicles of late endosomes and lysosomes. Localized in punctate cytoplasmic vesicles and in perinuclear structures, but does not colocalize with LAMP1 (PubMed:18234732). Localized on the plasma membrane over the acrosome and on the surface of the midpiece of the sperm tail (PubMed:20586096). {ECO:0000269|PubMed:18234732, ECO:0000269|PubMed:20586096}. TISSUE SPECIFICITY: Expressed in testis, epididymal tissue, epididymal luminal fluid (ELF), acrosome-intact (AI) sperm and caput (CAP), corpus (COR) and caudal (CAU) sperm. Higher expression in sperm than testis (at protein level) (PubMed:20586096). Liver, kidney, skin, brain, stomach and testis (PubMed:11929860). Expressed mainly in granulosa cells of the ovaries. Expressed in small and large antral follicles. Not present in theca or stroma cells (PubMed:18653706). Expressed in testis and liver (PubMed:18762256). Expressed in testis and CAP, COR, and CAU epididymis tissue (PubMed:20586096). {ECO:0000269|PubMed:11929860, ECO:0000269|PubMed:18653706, ECO:0000269|PubMed:18762256, ECO:0000269|PubMed:20586096}. +Q64385 I11RA_MOUSE Interleukin-11 receptor subunit alpha-1 (IL-11 receptor subunit alpha-1) (IL-11R subunit alpha-1) (IL-11R-alpha-1) (IL-11RA1) (Enhancer trap locus homolog 2) (Etl-2) (Novel cytokine receptor 1) (NR-1) (NR1) 432 46,655 Chain (1); Disulfide bond (3); Domain (3); Glycosylation (2); Motif (1); Sequence conflict (6); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 373 393 Helical. {ECO:0000255}. TOPO_DOM 24 372 Extracellular. {ECO:0000255}.; TOPO_DOM 394 432 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for interleukin-11. The receptor systems for IL6, LIF, OSM, CNTF, IL11 and CT1 can utilize IL6ST for initiating signal transmission. The IL11/IL11RA/IL6ST complex may be involved in the control of proliferation and/or differentiation of skeletogenic progenitor or other mesenchymal cells. Essential for the normal development of craniofacial bones and teeth.; FUNCTION: A soluble form (sIL11RA) can act as an antagonist of IL11-dependent cell differentiation in cells where both transmembrane IL11RA and IL6ST are present. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: On ligand binding, forms a multimer complex with IL6ST/gp130. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed in all adult tissues and in embryos. Highest levels in kidney, skeletal muscle and embryo. {ECO:0000269|PubMed:8662802}. +Q9QYY1 I36RA_MOUSE Interleukin-36 receptor antagonist protein (IL-36Ra) (Interleukin-1 HY1) (IL-1HY1) (Interleukin-1 delta) (IL-1 delta) (Interleukin-1 family member 5) (IL-1F5) (Interleukin-1 homolog 3) (IL-1H3) (Interleukin-1-like protein 1) (IL-1L1) 156 17,136 Beta strand (15); Chain (1); Disulfide bond (1); Erroneous initiation (1); Helix (4); Initiator methionine (1); Sequence conflict (1); Turn (1) FUNCTION: Inhibits the activity of interleukin-36 (IL36A,IL36B and IL36G) by binding to receptor IL1RL2/IL-36R and preventing its association with the coreceptor IL1RAP for signaling. Part of the IL-36 signaling system that is thought to be present in epithelial barriers and to take part in local inflammatory response; similar to the IL-1 system with which it shares the coreceptor. Proposed to play a role in skin inflammation. May be involved in the innate immune response to fungal pathogens. May activate an anti-inflammatory signaling pathway by recruiting SIGIRR. {ECO:0000269|PubMed:17908936, ECO:0000269|PubMed:18284608, ECO:0000269|PubMed:21860022, ECO:0000269|PubMed:21965679}. PTM: Removal of N-terminal methionine is necessary for full antagonistic activity. {ECO:0000269|PubMed:21965679}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. TISSUE SPECIFICITY: Highly abundant in embryonic tissue and tissues containing epithelial cells. +Q9JIP3 I17RB_MOUSE Interleukin-17 receptor B (IL-17 receptor B) (IL-17RB) (IL-17 receptor homolog 1) (IL-17ER) (IL-17Rh1) (IL17Rh1) (Interleukin-17B receptor) (IL-17B receptor) 499 55,617 Alternative sequence (2); Beta strand (6); Chain (1); Domain (1); Glycosylation (4); Helix (9); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 287 307 Helical. {ECO:0000255}. TOPO_DOM 18 286 Extracellular. {ECO:0000255}.; TOPO_DOM 308 499 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for the proinflammatory cytokines IL17B and IL17E. May play a role in controlling the growth and/or differentiation of hematopoietic cells. SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Isoform 2: Secreted. SUBUNIT: Interacts with DAZAP2. {ECO:0000250}. TISSUE SPECIFICITY: Liver and testis. Expressed at lower level in kidney and lung. Expressed in selected T-cell, B-cell and myeloid cell lines. +Q8K4C2 I17RC_MOUSE Interleukin-17 receptor C (IL-17 receptor C) (IL-17RC) (Interleukin-17 receptor-like protein) (IL-17RL) (ZcytoR14) 698 77,148 Alternative sequence (4); Chain (1); Domain (1); Glycosylation (5); Sequence conflict (9); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 465 485 Helical. {ECO:0000255}. TOPO_DOM 22 464 Extracellular. {ECO:0000255}.; TOPO_DOM 486 698 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for IL17A and IL17F homodimers as part of a heterodimeric complex with IL17RA (PubMed:17911633, PubMed:20554964). Receptor for the heterodimer formed by IL17A and IL17B as part of a heterodimeric complex with IL17RA (By similarity). Has also been shown to be the cognate receptor for IL17F and to bind IL17A with high affinity without the need for IL17RA (By similarity). {ECO:0000250|UniProtKB:Q8NAC3, ECO:0000269|PubMed:17911633, ECO:0000269|PubMed:20554964}. SUBCELLULAR LOCATION: Isoform 1: Cell membrane {ECO:0000269|PubMed:17911633}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: Isoform 2: Cell membrane {ECO:0000269|PubMed:17911633}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: Isoform 3: Cell membrane {ECO:0000269|PubMed:17911633}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: Isoform 4: Cell membrane {ECO:0000269|PubMed:17911633}; Single-pass type I membrane protein {ECO:0000255}. SUBUNIT: Heterodimer with IL17RA. Heterodimerization with IL17RA is independent of the cytoplasmic tail. Associates with non-glycosylated IL17RA constitutively. Binding of IL17A and IL17F induces association with glycosylated IL17RA. Interacts (via SEFIR domain and extended downstream region) with TRAF3IP2/ACT1 (phosphorylated). {ECO:0000269|PubMed:20554964}. +Q8K1T6 LY66E_MOUSE Lymphocyte antigen 6G6e (Lymphocyte antigen 6 complex locus protein G6e) 166 18,197 Alternative sequence (1); Chain (1); Compositional bias (1); Disulfide bond (4); Domain (1); Signal peptide (1) FUNCTION: Believed to act as a modulator of nicotinic acetylcholine receptors (nAChRs) activity. In vitro potentiates alpha-3:beta-4-containing nAChRs maximum response by increasing peak current and slowing down receptor desensitization; the activity is dependent on its cell surface localization. {ECO:0000269|PubMed:26276394}. PTM: O-glycosylated. Contains sialic acid residues. {ECO:0000269|PubMed:17008713}. SUBCELLULAR LOCATION: Cell surface {ECO:0000305|PubMed:26276394}. Cell membrane {ECO:0000269|PubMed:17008713, ECO:0000305|PubMed:26276394}. Cell projection {ECO:0000269|PubMed:17008713}. SUBUNIT: Interacts with CHRNA4. {ECO:0000269|PubMed:26276394}. +P05533 LY6A_MOUSE Lymphocyte antigen 6A-2/6E-1 (Ly-6A.2/Ly-6E.1) (Stem cell antigen 1) (SCA-1) (T-cell-activating protein) (TAP) 134 14,377 Chain (1); Disulfide bond (5); Domain (1); Lipidation (1); Natural variant (2); Propeptide (1); Sequence conflict (4); Signal peptide (1) FUNCTION: T-cell activation. PTM: O-glycosylated. Not N-glycosylated. {ECO:0000269|PubMed:3033645}.; PTM: Not phosphorylated. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15930324, ECO:0000269|PubMed:2660142}. +Q8K3X4 I2BPL_MOUSE Interferon regulatory factor 2-binding protein-like (Enhanced at puberty protein 1) 775 80,565 Chain (1); Coiled coil (2); Compositional bias (5); Cross-link (1); Erroneous initiation (1); Modified residue (9); Sequence conflict (6); Zinc finger (1) FUNCTION: May contribute to the control of female reproductive function. May play a role in gene transcription by transactivating GNRH1 promoter and repressing PENK promoter (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +Q9WUC3 LY6H_MOUSE Lymphocyte antigen 6H (Ly-6H) 139 14,669 Chain (1); Disulfide bond (5); Domain (1); Erroneous initiation (1); Glycosylation (1); Lipidation (1); Propeptide (1); Signal peptide (1) FUNCTION: Believed to act as modulator of nicotinic acetylcholine receptors (nAChRs) activity. In vitro inhibits alpha-3:beta-4-containing nAChRs maximum response. In vitro inhibits alpha-3:beta-4-containing nAChRs maximum response (PubMed:26276394). May play a role in the intracellular trafficking of alpha-7-containing nAChRs and may inhibit their expression at the cell surface (PubMed:25716842). Seems to inhibit alpha-7/CHRNA7 signaling in hippocampal neurons (By similarity). {ECO:0000250|UniProtKB:F1LNW6, ECO:0000269|PubMed:25716842, ECO:0000269|PubMed:26276394}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. SUBUNIT: Interacts with CHRNA4 and CHRNA7. {ECO:0000269|PubMed:25716842, ECO:0000269|PubMed:26276394}. TISSUE SPECIFICITY: Strongly expressed in brain, also found in lower levels in eye and reproductive tissues. +Q07079 IBP5_MOUSE Insulin-like growth factor-binding protein 5 (IBP-5) (IGF-binding protein 5) (IGFBP-5) 271 30,372 Chain (1); Disulfide bond (5); Domain (2); Modified residue (1); Sequence conflict (1); Signal peptide (1) FUNCTION: IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Most abundant in kidney, uterus and gastrocnemius muscle. +Q8BW74 HLF_MOUSE Hepatic leukemia factor 295 33,149 Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (1); Region (2); Sequence conflict (2) SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Binds DNA specifically as homodimer or heterodimer with other PAR factors. {ECO:0000250}. +P54869 HMCS2_MOUSE Hydroxymethylglutaryl-CoA synthase, mitochondrial (HMG-CoA synthase) (EC 2.3.3.10) (3-hydroxy-3-methylglutaryl coenzyme A synthase) 508 56,823 Active site (3); Binding site (4); Chain (1); Modified residue (33); Mutagenesis (2); Sequence conflict (2); Transit peptide (1) Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 2/3. FUNCTION: This enzyme condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA, which is the substrate for HMG-CoA reductase. {ECO:0000269|PubMed:24315375}. PTM: Acetylation of Lys-427 is observed in liver mitochondria from fasted mice but not from fed mice.; PTM: Succinylated. Desuccinylated by SIRT5. Succinylation, at least at Lys-83 and Lys-310, inhibits the enzymatic activity. {ECO:0000269|PubMed:24315375}. SUBCELLULAR LOCATION: Mitochondrion. SUBUNIT: Homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Liver and kidney. +Q9WUB0 HOIL1_MOUSE RanBP-type and C3HC4-type zinc finger-containing protein 1 (EC 2.3.2.31) (Heme-oxidized IRP2 ubiquitin ligase 1 homolog) (HOIL-1) (RING-type E3 ubiquitin transferase HOIL-1) (UbcM4-interacting protein 28) (Ubiquitin-conjugating enzyme 7-interacting protein 3) 508 57,534 Active site (1); Beta strand (7); Chain (1); Coiled coil (1); Domain (1); Erroneous initiation (2); Helix (6); Metal binding (20); Modified residue (3); Region (4); Sequence conflict (2); Turn (2); Zinc finger (4) FUNCTION: E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, such as UBE2L3/UBCM4, and then transfers it to substrates. Functions as an E3 ligase for oxidized IREB2 and both heme and oxygen are necessary for IREB2 ubiquitination. Promotes ubiquitination of TAB2 and IRF3 and their degradation by the proteasome. Component of the LUBAC complex which conjugates linear ('Met-1'-linked) polyubiquitin chains to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation. LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways. Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation. LUBAC is recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex. Together with OTULIN, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis. Binds polyubiquitin of different linkage types (By similarity). {ECO:0000250|UniProtKB:Q9BYM8}. PTM: Auto-ubiquitinated. Auto-ubiquitination leads to degradation by the proteasome (By similarity). {ECO:0000250|UniProtKB:Q62921}.; PTM: Phosphorylated. In vitro, phosphorylation inhibits auto-ubiquitination activity (By similarity). {ECO:0000250|UniProtKB:Q62921}. SUBUNIT: Component of the LUBAC complex (linear ubiquitin chain assembly complex) which consists of SHARPIN, RBCK1 and RNF31 (By similarity). LUBAC has a MW of approximately 600 kDa suggesting a heteromultimeric assembly of its subunits (By similarity). Interacts with beta-I-type (PRKCB1) and zeta-type protein kinase C (PRKCZ) and with UBE2L3 (By similarity). Interacts with IREB2 only in iron-rich conditions (By similarity). Associates with the TNF-R1 signaling complex (TNF-RSC) in a stimulation-dependent manner (By similarity). Interacts with EYA1, TAB2, TAB3, MAP3K7 TRAF6 and RIPK1 (PubMed:20956555). Interacts with IRF3 (By similarity). {ECO:0000250|UniProtKB:Q9BYM8, ECO:0000269|PubMed:20956555}. DOMAIN: The RanBP2-type zinc finger, also called Npl4 zinc finger (NZF), mediates binding to 'Met-1'-linked polyubiquitins. {ECO:0000269|PubMed:22139374}.; DOMAIN: The UBL domain mediates association with RNF31 via interaction with its UBA domain. {ECO:0000250|UniProtKB:Q9BYM8}. +P14901 HMOX1_MOUSE Heme oxygenase 1 (HO-1) (EC 1.14.14.18) (P32 protein) 289 32,929 Binding site (3); Chain (1); Metal binding (1); Modified residue (2) FUNCTION: Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Exhibits cytoprotective effects since excess of free heme sensitizes cells to undergo apoptosis. SUBCELLULAR LOCATION: Microsome. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein; Cytoplasmic side. +P27889 HNF1B_MOUSE Hepatocyte nuclear factor 1-beta (HNF-1-beta) (HNF-1B) (Homeoprotein LFB3) (Transcription factor 2) (TCF-2) 558 61,588 Alternative sequence (2); Chain (1); DNA binding (1); Erroneous initiation (1); Modified residue (4); Natural variant (1); Region (1); Sequence conflict (3) FUNCTION: Transcription factor, probably binds to the inverted palindrome 5'-GTTAATNATTAAC-3'. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Binds DNA as a dimer. Can form homodimer or heterodimer with HNF1-alpha. +P70333 HNRH2_MOUSE Heterogeneous nuclear ribonucleoprotein H2 (hnRNP H2) (Heterogeneous nuclear ribonucleoprotein H') (hnRNP H') [Cleaved into: Heterogeneous nuclear ribonucleoprotein H2, N-terminally processed] 449 49,280 Chain (2); Cross-link (3); Domain (3); Initiator methionine (1); Modified residue (10); Region (2); Repeat (4) FUNCTION: This protein is a component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes which provide the substrate for the processing events that pre-mRNAs undergo before becoming functional, translatable mRNAs in the cytoplasm. Binds poly(RG) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}. SUBUNIT: Interacts with TXNL4/DIM1. {ECO:0000250}. +Q8R0N6 HOT_MOUSE Hydroxyacid-oxoacid transhydrogenase, mitochondrial (HOT) (EC 1.1.99.24) (Alcohol dehydrogenase iron-containing protein 1) (ADHFe1) 465 49,937 Alternative sequence (1); Chain (1); Modified residue (2); Transit peptide (1) FUNCTION: Catalyzes the cofactor-independent reversible oxidation of gamma-hydroxybutyrate (GHB) to succinic semialdehyde (SSA) coupled to reduction of 2-ketoglutarate (2-KG) to D-2-hydroxyglutarate (D-2-HG). L-3-hydroxybutyrate (L-3-OHB) is also a substrate for HOT when using 2-KG as hydrogen acceptor, resulting in the formation of D-2-HG (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:17559793}. TISSUE SPECIFICITY: Expressed in white and brown adipose tissues, liver, and kidney. Expression is differentiation-dependent during in vitro brown and white adipogenesis. {ECO:0000269|PubMed:17559793}. +Q8VDM6 HNRL1_MOUSE Heterogeneous nuclear ribonucleoprotein U-like protein 1 859 96,002 Alternative sequence (3); Chain (1); Compositional bias (5); Cross-link (9); Domain (2); Erroneous initiation (1); Modified residue (11); Region (5); Repeat (5); Sequence conflict (4) FUNCTION: Acts as a basic transcriptional regulator. Represses basic transcription driven by several virus and cellular promoters. When associated with BRD7, activates transcription of glucocorticoid-responsive promoter in the absence of ligand-stimulation. Plays also a role in mRNA processing and transport. Binds avidly to poly(G) and poly(C) RNA homopolymers in vitro (By similarity). {ECO:0000250}. PTM: Methylated. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with BRD7, PRMT2, TP53 and NXF1. Associates with histones and BRD7 (By similarity). {ECO:0000250}. DOMAIN: The RGG-box domain is methylated. {ECO:0000250}. +Q921F4 HNRLL_MOUSE Heterogeneous nuclear ribonucleoprotein L-like 591 64,125 Alternative sequence (4); Beta strand (10); Chain (1); Compositional bias (2); Cross-link (2); Domain (3); Erroneous initiation (1); Helix (4); Modified residue (5); Mutagenesis (1); Sequence conflict (2); Turn (3) FUNCTION: RNA-binding protein that functions as regulator of alternative splicing for multiple target mRNAs, including PTPRC/CD45 and STAT5A. Required for alternative splicing of PTPRC. {ECO:0000269|PubMed:19100700}. SUBUNIT: Interacts with HNRNPL. {ECO:0000250}. +Q8K248 HPDL_MOUSE 4-hydroxyphenylpyruvate dioxygenase-like protein (EC 1.13.-.-) (Glyoxalase domain-containing protein 1) 371 39,909 Chain (1); Domain (2); Metal binding (3) FUNCTION: May have dioxygenase activity. {ECO:0000305}. +Q3TEA8 HP1B3_MOUSE Heterochromatin protein 1-binding protein 3 554 60,867 Alternative sequence (2); Chain (1); Compositional bias (3); Cross-link (3); Domain (3); Frameshift (1); Initiator methionine (1); Modified residue (13); Motif (1); Sequence conflict (18) FUNCTION: Component of heterochromatin that maintains heterochromatin integrity during G1/S progression and regulates the duration of G1 phase to critically influence cell proliferative capacity. May play a role in hypoxia-induced oncogenesis. {ECO:0000250|UniProtKB:Q5SSJ5, ECO:0000269|PubMed:8978696}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5SSJ5}. Chromosome {ECO:0000250|UniProtKB:Q5SSJ5}. Note=localized in nuclei but not in nucleoli in interphase. Colocalized with chromosomes in mitosis, with a gradually increased during G1 progression and a maximum level during late G1 phase (G1/S). {ECO:0000250|UniProtKB:Q5SSJ5}. SUBUNIT: Interacts (via PxVxL motif) with CBX5 (via Trp-174). {ECO:0000250|UniProtKB:Q5SSJ5, ECO:0000269|PubMed:8978696}. DOMAIN: A central region that included the first H15 (linker histone H1/H5 globular) domain binds at the entry/exit site of the nucleosomal DNA. {ECO:0000250|UniProtKB:Q5SSJ5}. +Q9ESB3 HRG_MOUSE Histidine-rich glycoprotein (Histidine-proline-rich glycoprotein) (HPRG) 525 59,163 Chain (1); Compositional bias (4); Disulfide bond (5); Domain (2); Erroneous gene model prediction (1); Erroneous initiation (1); Glycosylation (5); Modified residue (1); Region (2); Sequence conflict (2); Signal peptide (1); Site (1) FUNCTION: Plasma glycoprotein that binds a number of ligands such as heme, heparin, heparan sulfate, thrombospondin, plasminogen, and divalent metal ions. Binds heparin and heparin/glycosaminoglycans in a zinc-dependent manner. Binds heparan sulfate on the surface of liver, lung, kidney and heart endothelial cells. Binds to N-sulfated polysaccharide chains on the surface of liver endothelial cells. Inhibits rosette formation. Acts as an adapter protein and is implicated in regulating many processes such as immune complex and pathogen clearance, cell chemotaxis, cell adhesion, angiogenesis, coagulation and fibrinolysis. Mediates clearance of necrotic cells through enhancing the phagocytosis of necrotic cells in a heparan sulfate-dependent pathway. This process can be regulated by the presence of certain HRG ligands such as heparin and zinc ions. Binds to IgG subclasses of immunoglobins containing kappa and lambda light chains with different affinities regulating their clearance and inhibiting the formation of insoluble immune complexes. Tethers plasminogen to the cell surface. Binds T-cells and alters the cell morphology. Acts as a regulator of the vascular endothelial growth factor (VEGF) signaling pathway; inhibits endothelial cell motility by reducing VEGF-induced complex formation between PXN/paxillin and ILK/integrin-linked protein kinase and by promoting inhibition of VEGF-induced tyrosine phosphorylation of focal adhesion kinases and alpha-actinins in endothelial cells. Also plays a role in the regulation of tumor angiogenesis and tumor immune surveillance. Normalizes tumor vessels and promotes antitumor immunity by polarizing tumor-associated macrophages, leading to decreased tumor growth and metastasis (By similarity). Modulates angiogenesis by blocking the CD6-mediated antiangiongenic effect of thrombospondins, THBS1 and THBS2. {ECO:0000250, ECO:0000269|PubMed:15748999, ECO:0000269|PubMed:15869579, ECO:0000269|PubMed:18797515, ECO:0000269|PubMed:19903770, ECO:0000269|PubMed:22374984}. PTM: Proteolytic cleavage produces several HRG fragments which are mostly disulfide-linked and, therefore, not released. Cleavage by plasmin is inhibited in the presence of heparin, zinc ions or in an acidic environment. Cleavage reduces binding of HRG to heparan sulfate, but enhances the ability of HRG to bind and tether plasminogen to the cell surface. On platelet activation, releases a 33 kDa antiangiogenic peptide which encompasses the HRR. Also cleaved in the C-terminal by plasmin (By similarity). {ECO:0000250}.; PTM: N-glycosylated. {ECO:0000269|PubMed:17330941}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Interacts with THBS1 (via the TSP type I repeats); the interaction blocks the antiangiogenic effect of THBS1 with CD36. Interacts with HPSE; the interaction is enhanced at acidic pH, partially inhibits binding of HPSE to cell surface receptors and modulates its enzymatic activity. Interacts (via the HRR domain) with TMP1; the interaction partially mediates the antiangiogenic properties of HRG. Interacts with kappa and lambda light chains of IgG molecules. Interacts with ATP5F1A; the interaction occurs on the surface of T-cells and alters their cell morphology in concert with CONA. Binds IgG molecules containing kappa and lambda light chains and inhibits the formation of insoluble immunoglobulin complexes. Interacts with F12; the interaction, which is enhanced in the presence of zinc ions and inhibited by heparin-binding to HRG, inhibits factor XII autoactivation and contact-initiated coagulation (By similarity). Interacts with PLG (via its Kringle domains); the interaction tethers PLG to the cell surface and enhances its activation. Interacts (via the HRR domain) with TPM1; the interaction appears to contribute to the antiangiogenic properties of the HRR domain (By similarity). Interacts with THBS2; the interaction blocks the antiangiogenic effect of THBS2 with CD36. {ECO:0000250, ECO:0000269|PubMed:15748999}. DOMAIN: The His-rich (HRR) region contains approximately 12 tandem internal repeats of the 5-residue G[H/P][H/P]PH consensus sequence. HRR binds heparan sulfate and possesses antiangiogenic, antibacterial and antifungal properties through binding Candida cells, and preferentially lysing the ergosterol-containing liposomes at low pH. The tandem repeats also bind divalent metal ions and heme.; DOMAIN: The cystatin domains can also bind heparan sulfate. Binding is enhanced in the presence of zinc ions (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in liver, blood plasma, serum and in platelets. Also present in fibrin clots, wound fluid from acute wounds and chronic leg ulcers. {ECO:0000269|PubMed:10849117, ECO:0000269|PubMed:18797515}. +P62816 HRK_MOUSE Activator of apoptosis harakiri (BH3-interacting domain-containing protein 3) (Neuronal death protein DP5) 92 10,078 Chain (1); Motif (1); Transmembrane (1) TRANSMEM 70 88 Helical. {ECO:0000255}. FUNCTION: Promotes apoptosis. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Mitochondrion {ECO:0000250}. SUBUNIT: Interacts with BCL2 and BCL2L1. Interacts with C1QBP (By similarity). {ECO:0000250}. DOMAIN: The BH3 motif is required for the induction of cell death. {ECO:0000250}. +Q9CZJ2 HS12B_MOUSE Heat shock 70 kDa protein 12B 685 76,119 Chain (1); Modified residue (6) TISSUE SPECIFICITY: Expressed most strongly in heart with little or no expression in other tissues. In the aorta, preferentially expressed in lesions. {ECO:0000269|PubMed:12552099}. +P48722 HS74L_MOUSE Heat shock 70 kDa protein 4L (Heat shock 70-related protein APG-1) (Osmotic stress protein 94) 838 94,382 Alternative sequence (1); Chain (1); Modified residue (4); Sequence conflict (11) FUNCTION: Possesses chaperone activity in vitro where it inhibits aggregation of citrate synthase. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=May translocate to the nucleus after heat shock. {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in testis. Also expressed in renal medulla of water-restricted animals. {ECO:0000269|PubMed:8647834}. +P70174 HRH1_MOUSE Histamine H1 receptor (H1R) (HH1R) 488 55,682 Chain (1); Disulfide bond (2); Glycosylation (2); Modified residue (9); Natural variant (3); Region (2); Sequence conflict (10); Topological domain (8); Transmembrane (7) TRANSMEM 30 52 Helical; Name=1. {ECO:0000250}.; TRANSMEM 63 83 Helical; Name=2. {ECO:0000250}.; TRANSMEM 102 123 Helical; Name=3. {ECO:0000250}.; TRANSMEM 144 164 Helical; Name=4. {ECO:0000250}.; TRANSMEM 190 210 Helical; Name=5. {ECO:0000250}.; TRANSMEM 418 439 Helical; Name=6. {ECO:0000250}.; TRANSMEM 452 471 Helical; Name=7. {ECO:0000250}. TOPO_DOM 1 29 Extracellular. {ECO:0000250}.; TOPO_DOM 53 62 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 84 101 Extracellular. {ECO:0000250}.; TOPO_DOM 124 143 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 165 189 Extracellular. {ECO:0000250}.; TOPO_DOM 211 417 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 440 451 Extracellular. {ECO:0000250}.; TOPO_DOM 472 488 Cytoplasmic. {ECO:0000250}. FUNCTION: In peripheral tissues, the H1 subclass of histamine receptors mediates the contraction of smooth muscles, increase in capillary permeability due to contraction of terminal venules, and catecholamine release from adrenal medulla, as well as mediating neurotransmission in the central nervous system. Involved in circadian rhythm of locomotor activity and exploratory behavior. Also involved in responsiveness to pertussis toxin through its control of susceptibility to histamine hypersensitivity and enhancement of antigen-specific delayed-type hypersensitivity responses. {ECO:0000269|PubMed:12595443, ECO:0000269|PubMed:8917588}. PTM: Phosphorylation at sites in the second and third cytoplasmic loops independently contribute to agonist-induced receptor downregulation. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +Q9R0L1 HSF4_MOUSE Heat shock factor protein 4 (HSF 4) (mHSF4) (Heat shock transcription factor 4) (HSTF 4) 492 53,255 Alternative sequence (1); Chain (1); Cross-link (1); DNA binding (1); Modified residue (1); Region (3) FUNCTION: DNA-binding protein that specifically binds heat shock promoter elements (HSE). The HSF4A isoform represses transcription while the HSF4B isoform activates transcription. PTM: Phosphorylated mainly on serine residues. Phosphorylation on Ser-298 promotes sumoylation on Lys-293 (By similarity). {ECO:0000250}.; PTM: Isoform HSF4B is constitutively sumoylated. Sumoylation represses the transcriptional activity and is promoted by phosphorylation on Ser-298. HSFA is not sumoylated (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Homotrimer. Exhibits constitutive DNA binding and forms trimers even in the absence of stress. Interacts with ALKBH4, DUSP26, MAPK1, MAPK2 and MAP kinase p38 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Preferentially expressed in brain and lung. Also found in the eye. Slightly detected in liver and skeletal muscle. Isoform B is the major species in various tissues. {ECO:0000269|PubMed:16581800}. +Q6VYH9 HSH2D_MOUSE Hematopoietic SH2 domain-containing protein (Hematopoietic SH2 protein) (Adaptor in lymphocytes of unknown function X) 334 37,233 Chain (1); Compositional bias (1); Domain (1); Sequence conflict (8) FUNCTION: Adapter protein involved in tyrosine kinase and CD28 signaling (By similarity). May be a modulator of the apoptotic response through its ability to affect mitochondrial stability. {ECO:0000250, ECO:0000269|PubMed:15569688}. PTM: May be phosphorylated by FES and ACK1. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15569688}. Mitochondrion {ECO:0000269|PubMed:15569688}. SUBUNIT: Interacts with FES and TNK2. {ECO:0000250}. TISSUE SPECIFICITY: Predominantly expressed in spleen and thymus. Appears not to be expressed in heart, brain, liver, kidney, embryo, lung and ovary. {ECO:0000269|PubMed:12960172}. +Q8CAE2 HENMT_MOUSE Small RNA 2'-O-methyltransferase (EC 2.1.1.n8) (HEN1 methyltransferase homolog 1) (mHEN1) 395 44,921 Alternative sequence (1); Binding site (2); Chain (1); Frameshift (1); Metal binding (4); Mutagenesis (1); Sequence conflict (1) FUNCTION: Methyltransferase that adds a 2'-O-methyl group at the 3'-end of piRNAs, a class of 24 to 30 nucleotide RNAs that are generated by a Dicer-independent mechanism and are primarily derived from transposons and other repeated sequence elements. This probably protects the 3'-end of piRNAs from uridylation activity and subsequent degradation. Stabilization of piRNAs is essential for gametogenesis. {ECO:0000269|PubMed:17652135, ECO:0000269|PubMed:18029764}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q568P9}. Note=Component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis. {ECO:0000250|UniProtKB:Q568P9}. TISSUE SPECIFICITY: Specifically expressed in testis. {ECO:0000269|PubMed:17652135, ECO:0000269|PubMed:18029764}. +P16390 KCNA3_MOUSE Potassium voltage-gated channel subfamily A member 3 (MK3) (Voltage-gated potassium channel subunit Kv1.3) 528 58,564 Chain (1); Glycosylation (1); Lipidation (1); Modified residue (1); Motif (2); Sequence conflict (2); Topological domain (7); Transmembrane (6) TRANSMEM 188 206 Helical; Name=Segment S1. {ECO:0000255}.; TRANSMEM 248 269 Helical; Name=Segment S2. {ECO:0000255}.; TRANSMEM 281 301 Helical; Name=Segment S3. {ECO:0000255}.; TRANSMEM 316 334 Helical; Voltage-sensor; Name=Segment S4. {ECO:0000255}.; TRANSMEM 351 370 Helical; Name=Segment S5. {ECO:0000255}.; TRANSMEM 412 434 Helical; Name=Segment S6. {ECO:0000255}. TOPO_DOM 1 187 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 207 247 Extracellular. {ECO:0000255}.; TOPO_DOM 270 280 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 302 315 Extracellular. {ECO:0000255}.; TOPO_DOM 335 350 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 371 411 Extracellular. {ECO:0000255}.; TOPO_DOM 435 528 Cytoplasmic. {ECO:0000255}. FUNCTION: Mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient. PTM: N-glycosylation promotes the cell surface expression. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein. SUBUNIT: Heterotetramer of potassium channel proteins. Binds PDZ domains of DLG4 (By similarity). {ECO:0000250}. DOMAIN: The N-terminus may be important in determining the rate of inactivation of the channel while the tail may play a role in modulation of channel activity and/or targeting of the channel to specific subcellular compartments.; DOMAIN: The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position. +P70349 HINT1_MOUSE Histidine triad nucleotide-binding protein 1 (EC 3.-.-.-) (Adenosine 5'-monophosphoramidase) (Protein kinase C inhibitor 1) (Protein kinase C-interacting protein 1) (PKCI-1) 126 13,777 Active site (1); Binding site (1); Chain (1); Domain (1); Initiator methionine (1); Modified residue (5); Motif (1); Nucleotide binding (3) FUNCTION: Hydrolyzes purine nucleotide phosphoramidates with a single phosphate group, including adenosine 5'monophosphoramidate (AMP-NH2), adenosine 5'monophosphomorpholidate (AMP-morpholidate) and guanosine 5'monophosphomorpholidate (GMP-morpholidate). Hydrolyzes lysyl-AMP (AMP-N-epsilon-(N-alpha-acetyl lysine methyl ester)) generated by lysine tRNA ligase, as well as Met-AMP, His-AMP and Asp-AMP, lysyl-GMP (GMP-N-epsilon-(N-alpha-acetyl lysine methyl ester)) and AMP-N-alanine methyl ester. Can also convert adenosine 5'-O-phosphorothioate and guanosine 5'-O-phosphorothioate to the corresponding nucleoside 5'-O-phosphates with concomitant release of hydrogen sulfide. In addition, functions as scaffolding protein that modulates transcriptional activation by the LEF1/TCF1-CTNNB1 complex and by the complex formed with MITF and CTNNB1. Modulates p53/TP53 levels and p53/TP53-mediated apoptosis. Modulates proteasomal degradation of target proteins by the SCF (SKP2-CUL1-F-box protein) E3 ubiquitin-protein ligase complex (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. SUBUNIT: Homodimer. Interacts with CDK7. Interacts with RUVBL1 and RUVBL2 and is associated with the LEF1/TCF1-CTNNB1 complex and with a KAT5 histone acetyltransferase complex. Identified in a complex with MITF and CTNNB1. Interacts with CDC34 and RBX1, and is part of a SCF (SKP2-CUL1-F-box protein) E3 ubiquitin-protein ligase complex (By similarity). {ECO:0000250}. +Q08048 HGF_MOUSE Hepatocyte growth factor (Hepatopoietin-A) (Scatter factor) (SF) [Cleaved into: Hepatocyte growth factor alpha chain; Hepatocyte growth factor beta chain] 728 82,945 Alternative sequence (3); Beta strand (15); Chain (2); Disulfide bond (19); Domain (6); Erroneous initiation (1); Glycosylation (4); Helix (4); Modified residue (1); Sequence conflict (8); Signal peptide (1); Turn (5) FUNCTION: Potent mitogen for mature parenchymal hepatocyte cells, seems to be a hepatotrophic factor, and acts as a growth factor for a broad spectrum of tissues and cell types. Activating ligand for the receptor tyrosine kinase MET by binding to it and promoting its dimerization. {ECO:0000269|PubMed:20624990}. SUBUNIT: Dimer of an alpha chain and a beta chain linked by a disulfide bond. Interacts with SRPX2; the interaction increases HGF mitogenic activity. +Q6PCN7 HLTF_MOUSE Helicase-like transcription factor (EC 2.3.2.27) (EC 3.6.4.-) (P113) (RING-type E3 ubiquitin transferase HLTF) (SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 3) (Sucrose nonfermenting protein 2-like 3) (TNF-response element-binding protein) 1003 113,317 Chain (1); Cross-link (2); Domain (2); Modified residue (6); Motif (1); Nucleotide binding (1); Region (2); Sequence caution (1); Sequence conflict (11); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: Has both helicase and E3 ubiquitin ligase activities. Possesses intrinsic ATP-dependent nucleosome-remodeling activity. This activity may be required for transcriptional activation or repression of specific target promoters (By similarity). These may include the SERPINE1, to which this protein can bind directly. Plays a role in error-free postreplication repair (PRR) of damaged DNA and maintains genomic stability through acting as a ubiquitin ligase for 'Lys-63'-linked polyubiquitination of chromatin-bound PCNA (By similarity). {ECO:0000250, ECO:0000269|PubMed:9126292, ECO:0000269|PubMed:9427542}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000269|PubMed:9427542}. Nucleus, nucleolus {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Note=Nuclear localization is stimulated by progesterone. {ECO:0000250}. SUBUNIT: Interacts with SP1 and SP3 independently of DNA; the interaction with these transcriptional factors may be required for basal transcription of target genes. Interacts with EGR1; the interaction requires prior binding to DNA and represses c-Rel via a DNA looping mechanism. Interacts with GATA4. Interacts with PCNA; the interaction promotes polyubiquitination of PCNA through association with the UBE2B-RAD18 and UBE2V2-UBE2N ubiquitin ligase complexes. Interacts with RAD18, SHPRH, UBE2V2 and UBE2N (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver, lung, pancreas, placenta and skeletal muscle. {ECO:0000269|PubMed:9126292}. +Q9Z204 HNRPC_MOUSE Heterogeneous nuclear ribonucleoproteins C1/C2 (hnRNP C1/C2) 313 34,385 Alternative sequence (3); Chain (1); Coiled coil (1); Compositional bias (1); Cross-link (13); Domain (1); Initiator methionine (1); Modified residue (18); Motif (1); Sequence conflict (1) FUNCTION: Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles. Interacts with poly-U tracts in the 3'-UTR or 5'-UTR of mRNA and modulates the stability and the level of translation of bound mRNA molecules. Single HNRNPC tetramers bind 230-240 nucleotides. Trimers of HNRNPC tetramers bind 700 nucleotides. May play a role in the early steps of spliceosome assembly and pre-mRNA splicing. N6-methyladenosine (m6A) has been shown to alter the local structure in mRNAs and long non-coding RNAs (lncRNAs) via a mechanism named 'm(6)A-switch', facilitating binding of HNRNPC, leading to regulation of mRNA splicing. {ECO:0000250|UniProtKB:P07910}. PTM: Phosphorylated on Ser-268 and Ser-306 in resting cells. {ECO:0000250|UniProtKB:P07910}.; PTM: Sumoylated. Sumoylation reduces affinity for mRNA. {ECO:0000250|UniProtKB:P07910}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07910}. Note=Component of ribonucleosomes. {ECO:0000250|UniProtKB:P07910}. SUBUNIT: Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. Assembly of 3 tetramers with bound pre-mRNA gives rise to a 19S complex that interacts with HNRNPA2B1 tetramers. Component of the 40S hnRNP particle. Identified in the spliceosome C complex. Interacts with IGF2BP1. Interacts with DHX9; this interaction is direct, enhanced probably by their concomitant binding to RNA and mediates the attachment to actin filaments. {ECO:0000250|UniProtKB:P07910}. +Q9DCU9 HOGA1_MOUSE 4-hydroxy-2-oxoglutarate aldolase, mitochondrial (EC 4.1.3.16) (Dihydrodipicolinate synthase-like) (DHDPS-like protein) (Probable 2-keto-4-hydroxyglutarate aldolase) (Probable KHG-aldolase) 321 34,644 Active site (1); Binding site (2); Chain (1); Erroneous termination (1); Frameshift (1); Region (1); Sequence conflict (1); Site (1); Transit peptide (1) FUNCTION: Catalyzes the final step in the metabolic pathway of hydroxyproline. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q0P5I5}. SUBUNIT: Homotetramer. {ECO:0000250}. +Q9QWW1 HOME2_MOUSE Homer protein homolog 2 (Homer-2) (Cupidin) (VASP/Ena-related gene up-regulated during seizure and LTP 2) (Vesl-2) 354 40,570 Alternative sequence (1); Beta strand (6); Chain (1); Coiled coil (1); Domain (1); Helix (1); Sequence conflict (1); Turn (2) FUNCTION: Postsynaptic density scaffolding protein. Binds and cross-links cytoplasmic regions of GRM1, GRM5, ITPR1, DNM3, RYR1, RYR2, SHANK1 and SHANK3. By physically linking GRM1 and GRM5 with ER-associated ITPR1 receptors, it aids the coupling of surface receptors to intracellular calcium release. May also couple GRM1 to PI3 kinase through its interaction with AGAP2 (By similarity). Isoforms can be differently regulated and may play an important role in maintaining the plasticity at glutamatergic synapses (By similarity) Required for normal hearing (PubMed:25816005). Negatively regulates T cell activation through negative regulation of IL2 expression by inhibiting calcineurin-NFAT pathway activation through interaction with NFATC2 (By similarity). {ECO:0000250|UniProtKB:Q9NSB8, ECO:0000269|PubMed:25816005}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NSB8}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density. Cell junction, synapse. Cell projection, stereocilium {ECO:0000269|PubMed:25816005}. Note=Postsynaptic density of neuronal cells. The stabilization and clustering of the metabotropic glutamate receptors appears to be mediated by isoform 1 and isoform 2 at the cell surface. SUBUNIT: Forms coiled-coil structures coiled-coil structures that mediate homo- and heteromultimerization. Interacts with NFATC2; interaction is reduced by AKT activation. Interacts with NFATC1 and NFATC4 (By similarity). {ECO:0000250|UniProtKB:Q9NSB8}. TISSUE SPECIFICITY: Expressed in olfactory bulb, hippocampus, thalamus and heart (PubMed:9808459). Expressed in the cochlea, organ of Corti. Expression is particularly enriched in the tips of stereocilia of both inner and outer hair cells (PubMed:25816005). {ECO:0000269|PubMed:25816005, ECO:0000269|PubMed:9808459}. +Q9DCB1 HMGN3_MOUSE High mobility group nucleosome-binding domain-containing protein 3 99 10,769 Alternative sequence (4); Chain (1); Modified residue (4) FUNCTION: Binds to nucleosomes, regulating chromatin structure and consequently, chromatin-dependent processes such as transcription, DNA replication and DNA repair. Affects both insulin and glucagon levels and modulates the expression of pancreatic genes involved in insulin secretion. Regulates the expression of the glucose transporter SLC2A2 by binding specifically to its promoter region and recruiting PDX1 and additional transcription factors. Regulates the expression of SLC6A9, a glycine transporter which regulates the glycine concentration in synaptic junctions in the central nervous system, by binding to its transcription start site. May play a role in ocular development and astrocyte function. {ECO:0000269|PubMed:12185205, ECO:0000269|PubMed:15082770, ECO:0000269|PubMed:18502697, ECO:0000269|PubMed:19651901, ECO:0000269|PubMed:19885867}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with the ligand binding domain of the thyroid receptor (TR) (in vitro). Requires the presence of thyroid hormone for its interaction. Interacts with nucleosomes (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the brain, eye, prostate, thyroid, kidney, testis, glial cells and insulin-producing cells of the Langerhans pancreatic islets. In the brain, expressed in the lateral olfactory tract, anterior commissure, corpus callosum, internal capsule, fornix, stria medullans, optic tract, axon bundles, Purkinje cell layer and granular layer of the cerebellum. In retina, expressed in the nuclei of cells in the inner nuclear layer including amacrine, bipolar and horizontal neurons and in the nuclei of ganglion neurons. Detected at low levels in the liver. {ECO:0000269|PubMed:11356838, ECO:0000269|PubMed:12185205, ECO:0000269|PubMed:15082770, ECO:0000269|PubMed:18502697, ECO:0000269|PubMed:19651901, ECO:0000269|PubMed:19885867}. +Q99JP6 HOME3_MOUSE Homer protein homolog 3 (Homer-3) 356 39,694 Alternative sequence (1); Chain (1); Coiled coil (2); Domain (1); Modified residue (2); Region (1); Sequence conflict (2) FUNCTION: Postsynaptic density scaffolding protein. Binds and cross-links cytoplasmic regions of GRM1, GRM5, ITPR1, DNM3, RYR1, RYR2, SHANK1 and SHANK3. By physically linking GRM1 and GRM5 with ER-associated ITPR1 receptors, it aids the coupling of surface receptors to intracellular calcium release. Isoforms can be differently regulated and may play an important role in maintaining the plasticity at glutamatergic synapses (By similarity). Negatively regulates T cell activation through negative regulation of IL2 expression by inhibiting calcineurin-NFAT pathway activation through interaction with NFATC2 leading to reduction of interaction between NFATC2 and PPP3CA (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9NSC5}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250}. Cell junction, synapse {ECO:0000250}. Note=Postsynaptic density of neuronal cells. {ECO:0000250}. SUBUNIT: Tetramer (By similarity). Isoform 1 and isoform 2 encode coiled-coil structures that mediate homo- and heteromultimerization. Interacts with NFATC2; interaction is calcium independent; interaction competes with PPP3CA for NFATC2 binding; interaction is reduced by AKT activation (PubMed:18218901). Interacts with NFATC1 and NFATC4. Interacts with SHANK1; forms a high-order complex at least composed of SHANK1 and HOMER3; the complex formation is regulated by CAMK2A-mediated phosphorylation (By similarity). {ECO:0000250|UniProtKB:Q9NSC5, ECO:0000269|PubMed:18218901}. DOMAIN: The WH1 domain interacts with the PPXXF motif in GRM1, GRM5, RYR1, RYR2, ITPR1, SHANK 1 and SHANK3. TISSUE SPECIFICITY: Expressed in the cerebellum, hippocampus, lung and thymus. +P22361 HNF1A_MOUSE Hepatocyte nuclear factor 1-alpha (HNF-1-alpha) (HNF-1A) (Liver-specific transcription factor LF-B1) (LFB1) (Transcription factor 1) (TCF-1) 628 67,253 Chain (1); Compositional bias (1); DNA binding (1); Helix (2); Modified residue (5); Motif (1); Region (7); Sequence conflict (1) FUNCTION: Transcriptional activator that regulates the tissue specific expression of multiple genes, especially in pancreatic islet cells and in liver. Required for the expression of several liver specific genes. Binds to the inverted palindrome 5'-GTTAATNATTAAC-3'. {ECO:0000269|PubMed:10966642, ECO:0000269|PubMed:19289501}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Binds DNA as a dimer. Interacts with PCBD1. Heterotetramer with PCBD1; formed by a dimer of dimers. {ECO:0000269|PubMed:10966642, ECO:0000269|PubMed:11106484, ECO:0000269|PubMed:11439029}. TISSUE SPECIFICITY: Liver. +Q80W88 HOMEZ_MOUSE Homeobox and leucine zipper protein Homez (Homeodomain leucine zipper-containing factor) 542 60,914 Alternative sequence (1); Chain (1); Compositional bias (3); Cross-link (2); DNA binding (3); Erroneous initiation (2); Modified residue (2); Motif (1); Sequence conflict (3) FUNCTION: May function as a transcriptional regulator. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. SUBUNIT: Homodimer or heterodimer (Potential). Interacts with HOXC8 (By similarity). {ECO:0000250, ECO:0000305}. TISSUE SPECIFICITY: Ubiquitous. Strongly expressed in testis. {ECO:0000269|PubMed:12925734}. +Q8BIL5 HOOK1_MOUSE Protein Hook homolog 1 (mHK1) 728 84,439 Alternative sequence (2); Beta strand (1); Chain (1); Coiled coil (2); Domain (1); Erroneous initiation (1); Helix (10); Modified residue (4); Region (2); Sequence conflict (2); Turn (3) FUNCTION: Required for spermatid differentiation. Probably involved in the positioning of the microtubules of the manchette and the flagellum in relation to the membrane skeleton (PubMed:12075009). Component of the FTS/Hook/FHIP complex (FHF complex). The FHF complex may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting complex (the HOPS complex) (By similarity). {ECO:0000250|UniProtKB:Q9UJC3, ECO:0000269|PubMed:12075009}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12075009}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12075009, ECO:0000269|PubMed:28003339}. Note=Localizes to punctate cytoplasmic foci which do not appear to overlap with early or late endosomes, the endoplasmic reticulum, multivesicular bodies (MVBs), lysosomes, or mitochondria (PubMed:12075009). Often found in close association with microtubules (PubMed:12075009). Does not associate with the Golgi complex (PubMed:12075009). During spermiogenesis, it localizes to the manchette in spermatids from steps 8-10 (PubMed:12075009). It is also present between the microtubule manchette and the nucleus (PubMed:12075009). During manchette elongation, it is preferentially localized to the nuclear ring of the manchette, whereas the strong localization to the manchette decreases (PubMed:12075009). In more mature spermatids, while the manchette migrates posteriorly, it localizes to punctuates spots (PubMed:12075009). At later stages of spermatid differentiation, the punctuate expression pattern is found at both the attachment site and the proximal end of the elongated manchette (PubMed:12075009). In contrast, it is not present in mature spermatozoa (PubMed:12075009). {ECO:0000269|PubMed:12075009}. SUBUNIT: Self-associates (By similarity). Component of the FTS/Hook/FHIP complex (FHF complex), composed of AKTIP/FTS, FAM160A2, and one or more members of the Hook family of proteins HOOK1, HOOK2, and HOOK3 (By similarity). May interact directly with AKTIP/FTS, HOOK2 and HOOK3 (By similarity). Associates with several subunits of the homotypic vesicular sorting complex (the HOPS complex) including VPS16, VPS18, VPS39 and VPS41; these interactions may be indirect (By similarity). Interacts with CCDC181 (PubMed:28283191). Interacts (via coiled-coil region) with RIMBP3 (via C-terminus) (PubMed:19091768). Interacts with LRGUK (via guanylate kinase-like domain) (PubMed:28003339). Interacts with microtubules (By similarity). {ECO:0000250|UniProtKB:Q9UJC3, ECO:0000269|PubMed:19091768, ECO:0000269|PubMed:28003339, ECO:0000269|PubMed:28283191}. TISSUE SPECIFICITY: Mainly expressed in testis. {ECO:0000269|PubMed:12075009}. DISEASE: Note=Defects in Hook1 are the cause of the azh (abnormal spermatozoon head shape) mutant phenotype, which induces spermatozoa with highly abnormal head morphology that differs drastically from the compact and hook-shaped head of the normal sperm, leading to a strong decrease of fertility. {ECO:0000269|PubMed:12075009}. +Q8BGZ1 HPCL4_MOUSE Hippocalcin-like protein 4 (Neural visinin-like protein 2) (NVP-2) 191 22,215 Calcium binding (3); Chain (1); Domain (4); Initiator methionine (1); Lipidation (1) FUNCTION: May be involved in the calcium-dependent regulation of rhodopsin phosphorylation. {ECO:0000250}. +Q9CYQ5 HPIP_MOUSE Host cell factor C1 regulator 1 (HCF-1 beta-propeller-interacting protein) 120 13,359 Chain (1); Motif (1); Region (1) FUNCTION: Regulates HCFC1 activity by modulating its subcellular localization. Overexpression of HCFC1R1 leads to accumulation of HCFC1 in the cytoplasm. HCFC1R1-mediated export may provide the pool of cytoplasmic HCFC1 required for import of virion-derived VP16 into the nucleus (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Shuttles between the nucleus and cytoplasm in a CRM1-dependent manner. {ECO:0000250}. SUBUNIT: Interacts with HCFC1. {ECO:0000250}. +P01746 HVM02_MOUSE Ig heavy chain V region 93G7 140 15,514 Chain (1); Domain (1); Non-terminal residue (1); Signal peptide (1) +P01750 HVM06_MOUSE Ig heavy chain V region 102 117 12,867 Beta strand (9); Chain (1); Disulfide bond (1); Helix (1); Non-terminal residue (1); Region (5); Signal peptide (1); Turn (3) +P01758 HVM14_MOUSE Ig heavy chain V region 108A 117 12,972 Chain (1); Domain (1); Non-terminal residue (1); Signal peptide (1) +P01759 HVM15_MOUSE Ig heavy chain V region BCL1 136 15,078 Chain (1); Domain (1); Non-terminal residue (1); Signal peptide (1) +P01786 HVM17_MOUSE Ig heavy chain V region MOPC 47A 117 12,975 Chain (1); Domain (1); Non-terminal residue (1) +P01787 HVM18_MOUSE Ig heavy chain V regions TEPC 15/S107/HPCM1/HPCM2/HPCM3 123 13,777 Chain (1); Domain (1); Non-terminal residue (1) +P31310 HXA10_MOUSE Homeobox protein Hox-A10 (Homeobox protein Hox-1.8) 416 43,292 Alternative sequence (2); Chain (1); Compositional bias (5); DNA binding (1); Erroneous initiation (2); Sequence conflict (2) FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Binds to the DNA sequence 5'-AA[AT]TTTTATTAC-3'. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with SIRT2; the interaction is direct. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the developing limb bud where it is restricted to the mesenchyme along the proximal-distal axis. Also found in developing gut and urogenital tract. In adult tissue, both forms found in kidney but only isoform 1 is expressed in skeletal muscle. +P01804 HVM35_MOUSE Ig heavy chain V-III region HPC76 (Fragment) 111 12,304 Chain (1); Domain (1); Non-terminal residue (2) +Q9JKR6 HYOU1_MOUSE Hypoxia up-regulated protein 1 (GRP-170) (140 kDa Ca(2+)-binding protein) (CBP-140) 999 111,181 Chain (1); Compositional bias (1); Glycosylation (9); Modified residue (2); Motif (1); Sequence conflict (13); Signal peptide (1) FUNCTION: Has a pivotal role in cytoprotective cellular mechanisms triggered by oxygen deprivation. May play a role as a molecular chaperone and participate in protein folding (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000269|PubMed:7641295}. SUBUNIT: Part of a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX. +P23813 HXD11_MOUSE Homeobox protein Hox-D11 (Homeobox protein Hox-4.6) (Homeobox protein Hox-5.5) 323 33,546 Chain (1); Compositional bias (2); DNA binding (1); Erroneous initiation (1) FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. SUBCELLULAR LOCATION: Nucleus. +P09022 HXA1_MOUSE Homeobox protein Hox-A1 (Early retinoic acid 1) (Homeobox protein Hox-1.6) (Homeoboxless protein ERA-1-399) (Homeotic protein ERA-1-993) 331 36,037 Alternative sequence (2); Chain (1); Compositional bias (2); DNA binding (1); Glycosylation (1); Motif (1); Mutagenesis (8); Region (1) FUNCTION: Sequence-specific transcription factor (PubMed:29465778). Regulates multiple developmental processes including brainstem, inner and outer ear, abducens nerve and cardiovascular development and morphogenesis as well as cognition and behavior (By similarity). Also part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Acts on the anterior body structures. Seems to act in the maintenance and/or generation of hindbrain segments (By similarity). Activates transcription in the presence of PBX1A and PKNOX1 (PubMed:29465778). {ECO:0000250|UniProtKB:P49639, ECO:0000250|UniProtKB:Q90423, ECO:0000269|PubMed:29465778}.; FUNCTION: The homeobox domain presumably directs sequence-specific DNA binding. The N-terminal portion of ERA-1-993 may be involved in interactions with one or more other regulatory proteins. Such an interaction could regulate either the DNA-binding activity or the transcriptional regulatory activity of ERA-1-993.; FUNCTION: The homeoboxless ERA-1-399 protein could act as a competitive inhibitor of the ERA-1-993 protein by competing for interaction with regulatory protein(s) while being unable to bind to DNA. PTM: Glycosylated by OGT. {ECO:0000269|PubMed:29465778}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29465778}. SUBUNIT: Interacts with OGT (via TPR repeats domain); the interaction takes place mainly in the nucleus. {ECO:0000269|PubMed:29465778}. +P18528 HVM57_MOUSE Ig heavy chain V region 6.96 98 11,007 Chain (1); Domain (1); Non-terminal residue (1) +P09079 HXB5_MOUSE Homeobox protein Hox-B5 (Homeobox protein H24.1) (Homeobox protein Hox-2.1) (Homeobox protein Mu-1) 269 29,464 Chain (1); DNA binding (1); Motif (1); Sequence conflict (1) FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. SUBCELLULAR LOCATION: Nucleus. TISSUE SPECIFICITY: Expressed in a broad spectrum of tissues. +P01727 LV1E_MOUSE Ig lambda-1 chain V region S43 129 13,529 Beta strand (10); Chain (1); Domain (1); Helix (2); Modified residue (1); Non-terminal residue (1); Signal peptide (1); Turn (2) +Q80XZ4 I22R1_MOUSE Interleukin-22 receptor subunit alpha-1 (IL-22 receptor subunit alpha-1) (IL-22R-alpha-1) (IL-22RA1) 581 63,795 Chain (1); Disulfide bond (2); Domain (2); Glycosylation (2); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 231 251 Helical. {ECO:0000255}. TOPO_DOM 16 230 Extracellular. {ECO:0000255}.; TOPO_DOM 252 581 Cytoplasmic. {ECO:0000255}. FUNCTION: Component of the receptor for IL20, IL22 and IL24. Component of IL22 receptor formed by IL22RA1 and IL10RB enabling IL22 signaling via JAK/STAT pathways. IL22 also induces activation of MAPK1/MAPK3 and Akt kinases pathways. Component of one of the receptor for IL20 and IL24 formed by IL22RA1 and IL20RB also signaling through STATs activation. Mediates IL24 antiangiogenic activity as well as IL24 inhibitory effect on endothelial cell tube formation and differentiation. {ECO:0000269|PubMed:12618864}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Heterodimer with IL10RB and with IL20RB. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in kidney, liver and lung. {ECO:0000269|PubMed:12618864}. +P97378 I12R2_MOUSE Interleukin-12 receptor subunit beta-2 (IL-12 receptor subunit beta-2) (IL-12R subunit beta-2) (IL-12R-beta-2) (IL-12RB2) 874 98,197 Chain (1); Domain (5); Glycosylation (14); Modified residue (3); Motif (2); Mutagenesis (10); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 638 658 Helical. {ECO:0000255}. TOPO_DOM 24 637 Extracellular. {ECO:0000255}.; TOPO_DOM 659 874 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for interleukin-12. This subunit is the signaling component coupling to the JAK2/STAT4 pathway. Promotes the proliferation of T-cells as well as NK cells. Induces the promotion of T-cells towards the Th1 phenotype by strongly enhancing IFN-gamma production. Can also activate STAT3. {ECO:0000269|PubMed:12370372}. PTM: On IL12 stimulation, phosphorylated on C-terminal tyrosine residues. Phosphorylation of any one of Tyr-757, Tyr-804 or Tyr-811 can activate STAT4, IFN-gamma production, and T-cell proliferation. Tyr-811 is the dominant site of cell proliferation. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Heterodimer/heterooligomer; disulfide-linked. The functional high affinity IL12 receptor is composed of I12RB1 and IL12RB2. Il12RB2 binds JAK2 (via its N-terminal) through a membrane-proximal region of the cytoplasmic domain (By similarity). {ECO:0000250}. DOMAIN: The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.; DOMAIN: The box 1 motif is required for JAK interaction and/or activation. TISSUE SPECIFICITY: Expressed in developing T-helper (TH) cells. +Q9DB29 IAH1_MOUSE Isoamyl acetate-hydrolyzing esterase 1 homolog (EC 3.1.-.-) 249 27,974 Active site (3); Binding site (2); Chain (1); Modified residue (1) FUNCTION: Probable lipase. {ECO:0000250}. +P12968 IAPP_MOUSE Islet amyloid polypeptide (Amylin) (Diabetes-associated peptide) (DAP) 93 10,022 Disulfide bond (1); Modified residue (1); Peptide (1); Propeptide (2); Signal peptide (1) FUNCTION: Selectively inhibits insulin-stimulated glucose utilization and glycogen deposition in muscle, while not affecting adipocyte glucose metabolism. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Interacts with IDE and INS. {ECO:0000250}. DOMAIN: The mature protein is largely unstructured in the absence of a cognate ligand, but contrary to the human protein, it does not easily form fibrillar aggregates. +Q9QUS4 HEY2_MOUSE Hairy/enhancer-of-split related with YRPW motif protein 2 (HES-related repressor protein 2) (Hairy and enhancer of split-related protein 2) (HESR-2) (Hairy-related transcription factor 2) (HRT-2) (mHRT2) (Protein gridlock homolog) 339 35,873 Chain (1); Compositional bias (2); Domain (2); Motif (1); Mutagenesis (2); Region (1); Sequence conflict (2) FUNCTION: Transcriptional repressor which functions as a downstream effector of Notch signaling in cardiovascular development. Specifically required for the Notch-induced endocardial epithelial to mesenchymal transition, which is itself criticial for cardiac valve and septum development. May be required in conjunction with HEY1 to specify arterial cell fate or identity. Promotes maintenance of neuronal precursor cells and glial versus neuronal fate specification. Binds preferentially to the canonical E box sequence 5'-CACGTG-3'. Represses transcription by the cardiac transcriptional activators GATA4 and GATA6 and by the neuronal bHLH factors ASCL1/MASH1 and NEUROD4/MATH3. {ECO:0000269|PubMed:10692439, ECO:0000269|PubMed:11095750, ECO:0000269|PubMed:11160397, ECO:0000269|PubMed:11486045, ECO:0000269|PubMed:12372253, ECO:0000269|PubMed:12372254, ECO:0000269|PubMed:12454287, ECO:0000269|PubMed:12947105, ECO:0000269|PubMed:15107403, ECO:0000269|PubMed:15297376, ECO:0000269|PubMed:15345511, ECO:0000269|PubMed:15485867, ECO:0000269|PubMed:15680351, ECO:0000269|PubMed:16199874, ECO:0000269|PubMed:17259303, ECO:0000269|PubMed:17303760, ECO:0000269|PubMed:17332425}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00380, ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:11741889}. SUBUNIT: May self-associate (By similarity). Interacts with ARNT (By similarity). Interacts with GATA4, GATA6, HES1 and HEYL. Interacts with HDAC1, NCOR1 and SIN3A. {ECO:0000250, ECO:0000269|PubMed:11486045, ECO:0000269|PubMed:15485867, ECO:0000269|PubMed:16199874, ECO:0000269|PubMed:17303760}. TISSUE SPECIFICITY: Highly expressed in the aorta, lower expression detected in the heart, brain, kidney, lung, muscle, ovary and testis. {ECO:0000269|PubMed:10588864, ECO:0000269|PubMed:10692439, ECO:0000269|PubMed:10860664, ECO:0000269|PubMed:12947105}. +Q9DBX7 HEYL_MOUSE Hairy/enhancer-of-split related with YRPW motif-like protein (Hairy and enhancer of split-related protein 3) (Hairy-related transcription factor 3) (HRT-3) (mHRT3) 326 34,929 Chain (1); Compositional bias (1); Domain (2); Region (1); Sequence conflict (2) FUNCTION: Transcriptional repressor which binds preferentially to the canonical E box sequence 5'-CACGTG-3' (By similarity). Downstream effector of Notch signaling required for cardiovascular development. Specifically required for the Notch-induced endocardial epithelial to mesenchymal transition, which is itself criticial for cardiac valve and septum development. Represses transcription by the cardiac transcriptional activators GATA4 and GATA6. {ECO:0000250, ECO:0000269|PubMed:16199874, ECO:0000269|PubMed:17303760}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00380, ECO:0000255|PROSITE-ProRule:PRU00981}. SUBUNIT: Interacts with HES1, HDAC1, NCOR1 and SIN3A (By similarity). Self-associates. Interacts with GATA4, GATA6, HEY1 and HEY2. {ECO:0000250, ECO:0000269|PubMed:16199874, ECO:0000269|PubMed:17303760}. TISSUE SPECIFICITY: Expressed in heart and at lower levels in brain, lung, muscle, ovary and testis. {ECO:0000269|PubMed:10860664}. +Q8C3I8 HGH1_MOUSE Protein HGH1 homolog 393 42,916 Chain (1); Compositional bias (1); Modified residue (1); Sequence conflict (2) +Q3TYV2 HHLA1_MOUSE HERV-H LTR-associating protein 1 homolog 514 56,354 Chain (1); Glycosylation (9); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q9DD02 HIKES_MOUSE Protein Hikeshi (Lethal gene on chromosome 7 Rinchik 6 protein) 197 21,619 Alternative sequence (1); Chain (1); Region (2); Sequence conflict (1) FUNCTION: Acts as a specific nuclear import carrier for HSP70 proteins following heat-shock stress: acts by mediating the nucleoporin-dependent translocation of ATP-bound HSP70 proteins into the nucleus. HSP70 proteins import is required to protect cells from heat shock damages. Does not translocate ADP-bound HSP70 proteins into the nucleus (By similarity). May also be indirectly required for organization and/or function of the secretory apparatus in Clara cells in lung. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16157679}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q53FT3}. Nucleus {ECO:0000250|UniProtKB:Q53FT3}. SUBUNIT: Forms an asymmetric homodimer; required for binding and nuclear import of HSP70 proteins. Interacts with ATP-bound HSP70 proteins. Interacts with NUP62 and NUP153 (via F-X-F-G repeats). Interacts with HSPA8. {ECO:0000250|UniProtKB:Q53FT3}. TISSUE SPECIFICITY: Expressed in the central white matter of newborn and adult brain, particularly in regions where oligodendrocytes are generated (PubMed:26545878). {ECO:0000269|PubMed:26545878}. +Q9D0S9 HINT2_MOUSE Histidine triad nucleotide-binding protein 2, mitochondrial (HINT-2) (EC 3.-.-.-) (HINT-3) 163 17,320 Active site (1); Binding site (3); Chain (1); Domain (1); Modified residue (5); Motif (1); Nucleotide binding (2); Transit peptide (1) FUNCTION: Hydrolase probably involved in steroid biosynthesis. May play a role in apoptosis. Has adenosine phosphoramidase activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. +Q8C6C9 LEG1H_MOUSE Protein LEG1 homolog 337 38,284 Chain (1); Erroneous initiation (3); Glycosylation (1); Sequence conflict (14); Signal peptide (1) FUNCTION: May be involved in early liver development. {ECO:0000250|UniProtKB:A5PF61, ECO:0000250|UniProtKB:Q4QRF7}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:A5PF61, ECO:0000250|UniProtKB:Q4QRF7}. +Q9CQW5 LEG2_MOUSE Galectin-2 (Gal-2) 130 14,880 Chain (1); Domain (1); Region (1); Sequence conflict (2) FUNCTION: This protein binds beta-galactoside. Its physiological function is not yet known. SUBUNIT: Homodimer. {ECO:0000250}. +Q8BLH7 HIRP3_MOUSE HIRA-interacting protein 3 601 65,215 Chain (1); Compositional bias (2); Modified residue (29) FUNCTION: May play a role in chromatin function and histone metabolism via its interaction with HIRA and histones. {ECO:0000250|UniProtKB:Q9BW71}. PTM: Phosphorylated by CK2. {ECO:0000250|UniProtKB:Q9BW71}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BW71}. Note=Nuclear throughout the cell cycle and is excluded from condensed chromatin during mitosis. {ECO:0000250|UniProtKB:Q9BW71}. SUBUNIT: Interacts with HIRA. Weak interaction with histones H2B and H3. Interacts with CK2 (By similarity). {ECO:0000250|UniProtKB:Q9BW71}. +Q9DAE3 LELP1_MOUSE Late cornified envelope-like proline-rich protein 1 120 12,755 Chain (1); Compositional bias (1); Sequence conflict (1) +Q8R1M0 HMCES_MOUSE Embryonic stem cell-specific 5-hydroxymethylcytosine-binding protein (ES cell-specific 5hmC-binding protein) (Putative peptidase SRAPD1) (EC 3.4.-.-) (SRAP domain-containing protein 1) 353 40,169 Chain (1); Cross-link (7); Modified residue (3) FUNCTION: Specifically binds 5-hydroxymethylcytosine (5hmC)-containing DNA in stem cells, suggesting that it acts as a specific reader of 5hmC in stem cells (PubMed:23434322). May act as a peptidase; experimental evidences are however required to confirm this prediction. {ECO:0000269|PubMed:23434322}. +Q91VF2 HNMT_MOUSE Histamine N-methyltransferase (HMT) (EC 2.1.1.8) 295 33,665 Binding site (7); Chain (1) FUNCTION: Inactivates histamine by N-methylation. Plays an important role in degrading histamine and in regulating the airway response to histamine. {ECO:0000269|PubMed:11475331}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P50135}. SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P50135}. +Q8BUK6 HOOK3_MOUSE Protein Hook homolog 3 (mHK3) 718 83,218 Chain (1); Coiled coil (2); Domain (1); Modified residue (5); Region (3); Sequence conflict (1) FUNCTION: Component of the FTS/Hook/FHIP complex (FHF complex). The FHF complex may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting complex (the HOPS complex). May regulate clearance of endocytosed receptors such as MSR1. Participates in defining the architecture and localization of the Golgi complex (By similarity). Serves as a target for the spiC protein from Salmonella typhimurium, which inactivates it, leading to a strong alteration in cellular trafficking (PubMed:12950921). Acts as an adapter protein linking the dynein motor complex to various cargos and converts dynein from a non-processive to a highly processive motor in the presence of dynactin. Facilitates the interaction between dynein and dynactin and activates dynein processivity (the ability to move along a microtubule for a long distance without falling off the track) (By similarity). {ECO:0000250|UniProtKB:Q86VS8, ECO:0000269|PubMed:12950921}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15075236, ECO:0000269|PubMed:28003339}. Golgi apparatus {ECO:0000269|PubMed:15075236}. Note=Enriched at the cis-face of the Golgi complex (By similarity). Localizes to microtubule asters in prophase (By similarity). Localizes to the manchette in elongating spermatids (PubMed:28003339). {ECO:0000250|UniProtKB:Q86VS8, ECO:0000269|PubMed:28003339}. SUBUNIT: Self-associates (By similarity). Component of the FTS/Hook/FHIP complex (FHF complex), composed of AKTIP/FTS, FAM160A2, and one or more members of the Hook family of proteins HOOK1, HOOK2, and HOOK3 (By similarity). May interact directly with AKTIP/FTS, HOOK1 and HOOK2 (By similarity). Associates with several subunits of the homotypic vesicular sorting complex (the HOPS complex) including VPS16 and VPS41; these interactions may be indirect (By similarity). Interacts with MSR1, and this association is stimulated by ligand binding to MSR1 (PubMed:17237231). Interacts with microtubules (By similarity). Interacts with IIGP1 (PubMed:15075236). Interacts with Salmonella typhimurium spiC (PubMed:12950921). Interacts with dynein intermediate chain and dynactin (DCTN1) (By similarity). Interacts with CCDC181 (PubMed:28283191). Interacts with LRGUK (PubMed:28003339). {ECO:0000250|UniProtKB:Q86VS8, ECO:0000269|PubMed:12950921, ECO:0000269|PubMed:15075236, ECO:0000269|PubMed:17237231, ECO:0000269|PubMed:28003339, ECO:0000269|PubMed:28283191}. TISSUE SPECIFICITY: Expressed in brain, cerebellum, heart, intestine, kidney, liver, lung, skeletal muscle, spleen and stomach (at protein level). {ECO:0000269|PubMed:11238449, ECO:0000269|PubMed:17140400}. +Q3V1H3 HPHL1_MOUSE Hephaestin-like protein 1 (EC 1.-.-.-) 1159 130,888 Chain (1); Compositional bias (1); Disulfide bond (5); Domain (6); Erroneous initiation (1); Glycosylation (6); Metal binding (19); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1115 1135 Helical. {ECO:0000255}. TOPO_DOM 24 1114 Extracellular. {ECO:0000255}.; TOPO_DOM 1136 1159 Cytoplasmic. {ECO:0000255}. FUNCTION: May function as a ferroxidase and may be involved in copper transport and homeostasis. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +P00493 HPRT_MOUSE Hypoxanthine-guanine phosphoribosyltransferase (HGPRT) (HGPRTase) (EC 2.4.2.8) (HPRT B) 218 24,570 Active site (1); Binding site (3); Chain (1); Cross-link (2); Metal binding (1); Modified residue (2); Nucleotide binding (2); Sequence conflict (1) Purine metabolism; IMP biosynthesis via salvage pathway; IMP from hypoxanthine: step 1/1. FUNCTION: Converts guanine to guanosine monophosphate, and hypoxanthine to inosine monophosphate. Transfers the 5-phosphoribosyl group from 5-phosphoribosylpyrophosphate onto the purine. Plays a central role in the generation of purine nucleotides through the purine salvage pathway (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Homotetramer. {ECO:0000250}. +Q9D6B9 HRCT1_MOUSE Histidine-rich carboxyl terminus protein 1 109 13,009 Chain (1); Compositional bias (1); Sequence conflict (1); Transmembrane (1) TRANSMEM 13 33 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q8K3A0 HSC20_MOUSE Iron-sulfur cluster co-chaperone protein HscB, mitochondrial (Hsc20) 234 26,645 Chain (1); Domain (1); Erroneous initiation (1); Metal binding (4); Sequence conflict (1); Transit peptide (1) Cofactor biosynthesis; iron-sulfur cluster biosynthesis. FUNCTION: Acts as a co-chaperone in iron-sulfur cluster assembly in mitochondria. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Mitochondrion {ECO:0000250}. SUBUNIT: Interacts with ISCU and HSPA9. {ECO:0000250}. +P62313 LSM6_MOUSE U6 snRNA-associated Sm-like protein LSm6 80 9,128 Chain (1); Modified residue (1) FUNCTION: Plays role in pre-mRNA splicing as component of the U4/U6-U5 tri-snRNP complex that is involved in spliceosome assembly, and as component of the precatalytic spliceosome (spliceosome B complex). The heptameric LSM2-8 complex binds specifically to the 3'-terminal U-tract of U6 snRNA. Component of LSm protein complexes, which are involved in RNA processing and may function in a chaperone-like manner, facilitating the efficient association of RNA processing factors with their substrates. Component of the cytoplasmic LSM1-LSM7 complex, which is thought to be involved in mRNA degradation by activating the decapping step in the 5'-to-3' mRNA decay pathway. {ECO:0000250|UniProtKB:P62312}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P62312}. Nucleus {ECO:0000250|UniProtKB:P62312}. SUBUNIT: Component of the precatalytic spliceosome (spliceosome B complex). Component of the U4/U6-U5 tri-snRNP complex, a building block of the precatalytic spliceosome (spliceosome B complex). The U4/U6-U5 tri-snRNP complex is composed of the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39, plus LSM2, LSM3, LSM4, LSM5, LSM6, LSM7 and LSM8. LSM2, LSM3, LSM4, LSM5, LSM6, LSM7 and LSM8 form a heptameric, ring-shaped subcomplex (the LSM2-8 complex) that is part of the U4/U6-U5 tri-snRNP complex and the precatalytic spliceosome. Component of the heptameric LSM1-LSM7 complex, which consists of LSM1, LSM2, LSM3, LSM4, LSM5, LSM6 and LSM7. {ECO:0000250|UniProtKB:P62312}. +Q8BQY8 HUS1_MOUSE Checkpoint protein HUS1 (mHUS1) 280 31,680 Alternative sequence (2); Chain (1) FUNCTION: Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair. The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex. Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3'-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage activity on substrates with double, nick, or gap flaps of distinct sequences and lengths; and DNA ligase I (LIG1) on long-patch base excision repair substrates. The 9-1-1 complex is necessary for the recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring during the S phase (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O60921}. Cytoplasm {ECO:0000250|UniProtKB:O60921}. Note=In discrete nuclear foci upon DNA damage. DNA damage induces its nuclear translocation. Shuttles between the nucleus and the cytoplasm. {ECO:0000250|UniProtKB:O60921}. SUBUNIT: Component of the toroidal 9-1-1 (RAD9-RAD1-HUS1) complex, composed of RAD9A, RAD1 and HUS1. The 9-1-1 complex associates with LIG1, POLB, FEN1, RAD17, HDAC1, RPA1 and RPA2. The 9-1-1 complex associates with the RAD17-RFC complex. HUS1 interacts with POLB, HDAC1, FEN1, PCNA, RAD1, RAD9A and RAD9B. HUS1 does not interact with RAD17. Interacts with DNAJC7 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10395797}. +Q6ZWM4 LSM8_MOUSE U6 snRNA-associated Sm-like protein LSm8 96 10,403 Chain (1); Initiator methionine (1); Modified residue (1) FUNCTION: Plays role in pre-mRNA splicing as component of the U4/U6-U5 tri-snRNP complex that is involved in spliceosome assembly, and as component of the precatalytic spliceosome (spliceosome B complex). The heptameric LSM2-8 complex binds specifically to the 3'-terminal U-tract of U6 snRNA. {ECO:0000250|UniProtKB:O95777}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O95777}. SUBUNIT: Component of the precatalytic spliceosome (spliceosome B complex). Component of the U4/U6-U5 tri-snRNP complex, a building block of the precatalytic spliceosome (spliceosome B complex). The U4/U6-U5 tri-snRNP complex is composed of the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39, plus LSM2, LSM3, LSM4, LSM5, LSM6, LSM7 and LSM8. LSM2, LSM3, LSM4, LSM5, LSM6, LSM7 and LSM8 form a heptameric, ring-shaped subcomplex (the LSM2-8 complex) that is part of the U4/U6-U5 tri-snRNP complex and the precatalytic spliceosome. {ECO:0000250|UniProtKB:O95777}. +P18531 HVM60_MOUSE Ig heavy chain V region 3-6 (Ig heavy chain V region M315) 116 13,095 Beta strand (9); Chain (1); Disulfide bond (1); Helix (1); Non-terminal residue (1); Region (5); Signal peptide (1); Turn (3) +P01789 HVM20_MOUSE Ig heavy chain V region M603 122 13,626 Beta strand (12); Chain (1); Domain (1); Helix (4); Non-terminal residue (1); Site (2); Turn (3) +P34914 HYES_MOUSE Bifunctional epoxide hydrolase 2 [Includes: Cytosolic epoxide hydrolase 2 (CEH) (EC 3.3.2.10) (Epoxide hydratase) (Soluble epoxide hydrolase) (SEH); Lipid-phosphate phosphatase (EC 3.1.3.76)] 554 62,515 Active site (3); Alternative sequence (1); Beta strand (21); Binding site (1); Chain (1); Domain (1); Helix (32); Lipidation (1); Metal binding (3); Modified residue (13); Motif (1); Region (3); Sequence conflict (1); Turn (8) FUNCTION: Bifunctional enzyme. The C-terminal domain has epoxide hydrolase activity and acts on epoxides (alkene oxides, oxiranes) and arene oxides. Plays a role in xenobiotic metabolism by degrading potentially toxic epoxides. Also determines steady-state levels of physiological mediators. The N-terminal domain has lipid phosphatase activity, with the highest activity towards threo-9,10-phosphonooxy-hydroxy-octadecanoic acid, followed by erythro-9,10-phosphonooxy-hydroxy-octadecanoic acid, 12-phosphonooxy-octadec-9Z-enoic acid and 12-phosphonooxy-octadec-9E-enoic acid. {ECO:0000250|UniProtKB:P34913, ECO:0000250|UniProtKB:P80299}. PTM: The N-terminus is blocked.; PTM: The covalent modification of cysteine by 15-deoxy-Delta12,14-prostaglandin-J2 is autocatalytic and reversible. It may occur as an alternative to other cysteine modifications, such as S-nitrosylation and S-palmitoylation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Peroxisome. SUBUNIT: Homodimer. {ECO:0000269|PubMed:10747889}. DOMAIN: The N-terminal domain has phosphatase activity. The C-terminal domain has epoxide hydrolase activity. TISSUE SPECIFICITY: Detected in liver, intestine, ovary and kidney. Detected at low levels in heart and muscle. {ECO:0000269|PubMed:15601917, ECO:0000269|PubMed:8750907}. +P01800 HVM31_MOUSE Ig heavy chain V-III region T957 113 12,732 Chain (1); Disulfide bond (1); Domain (1); Non-terminal residue (1) +P01801 HVM32_MOUSE Ig heavy chain V-III region J606 115 12,810 Beta strand (11); Chain (1); Disulfide bond (1); Domain (1); Helix (3); Non-terminal residue (1); Turn (3) +P01809 HVM39_MOUSE Ig heavy chain V region X24 118 13,105 Chain (1); Domain (1); Non-terminal residue (1) +Q62424 HXA13_MOUSE Homeobox protein Hox-A13 (Homeobox protein Hox-1.10) 386 39,567 Chain (1); Compositional bias (7); DNA binding (1); Helix (3); Mutagenesis (3) FUNCTION: Sequence-specific, AT-rich binding transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Binds DNA as a homodimer. Interacts with MEIS1, MEIS2 and MEIS3. {ECO:0000269|PubMed:15617687, ECO:0000269|PubMed:21829694}. DISEASE: Note=Defects in Hoxa13 are the cause of hypodactyly (Hd), a condition characterized by profound deficiency of digital arch structures. +Q80W93 HYDIN_MOUSE Hydrocephalus-inducing protein (Protein Hy-3) 5154 581,523 Alternative sequence (5); Chain (1); Coiled coil (3); Erroneous initiation (2); Sequence caution (1); Sequence conflict (5) FUNCTION: Required for ciliary motility. {ECO:0000269|PubMed:18250199}. SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000305}. TISSUE SPECIFICITY: Expressed in brain and testis. Expressed in ciliated epithelial cells lining bronchi and oviduct, and in spermatocytes. {ECO:0000269|PubMed:12719380}. DISEASE: Note=Defects in Hydin are the cause of spontaneous hydrocephalus 3, a lethal communicating hydrocephalus with perinatal onset. There is lethality in the first weeks of life because of hydrocephalus caused by abnormal ependymal ciliary motility. Cilia are unable to bend normally, ciliary beat frequency is reduced, and the cilia tend to stall. As a result, these cilia are incapable of generating fluid flow. Similar defects are observed for cilia in trachea. Mice do not exhibit randomization of left-right body asymmetry or situs inversus. {ECO:0000269|PubMed:12719380, ECO:0000269|PubMed:18250199}. +P09027 HXD3_MOUSE Homeobox protein Hox-D3 (Homeobox protein Hox-4.1) (Homeobox protein MH-19) 433 45,976 Chain (1); DNA binding (1); Erroneous initiation (4); Frameshift (1); Motif (1); Sequence conflict (7) FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. SUBCELLULAR LOCATION: Nucleus. TISSUE SPECIFICITY: Detected in adult kidney, but not in other adult tissues tested. {ECO:0000269|PubMed:8710855}. +Q05A56 HYAL4_MOUSE Hyaluronidase-4 (Hyal-4) (EC 3.2.1.35) (Chondroitin sulfate endo-beta-N-acetylgalactosaminidase) (Chondroitin sulfate hydrolase) (CSHY) (Hyaluronoglucosaminidase-4) 481 54,385 Active site (1); Chain (1); Compositional bias (1); Disulfide bond (5); Glycosylation (4); Sequence conflict (3); Topological domain (3); Transmembrane (2) TRANSMEM 12 32 Helical. {ECO:0000255}.; TRANSMEM 456 476 Helical. {ECO:0000255}. TOPO_DOM 1 11 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 33 455 Extracellular. {ECO:0000255}.; TOPO_DOM 477 481 Cytoplasmic. {ECO:0000255}. FUNCTION: Endo-hyaluronidase that degrades hyaluronan to smaller oligosaccharide fragments. Has also chondroitin sulfate hydrolase activity, The best substrate being the galactosaminidic linkage in the sequence of a trisulfated tetrasaccharide (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q7TMK6 HOOK2_MOUSE Protein Hook homolog 2 (mHK2) 716 83,366 Chain (1); Coiled coil (2); Domain (1); Erroneous initiation (1); Modified residue (1); Region (4); Sequence conflict (6) FUNCTION: Component of the FTS/Hook/FHIP complex (FHF complex). The FHF complex may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting complex (the HOPS complex). Contributes to the establishment and maintenance of centrosome function. May function in the positioning or formation of aggresomes, which are pericentriolar accumulations of misfolded proteins, proteasomes and chaperones. {ECO:0000250|UniProtKB:Q96ED9}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:17140400, ECO:0000269|PubMed:25781171}. Cytoplasm {ECO:0000269|PubMed:17140400}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17140400, ECO:0000269|PubMed:28003339}. Note=Localizes to punctate cytoplasmic foci which do not appear to overlap with early or late endosomes, the endoplasmic reticulum, the Golgi complex, multivesicular bodies (MVBs), lysosomes, or mitochondria. Often found in close association with microtubules (By similarity). Localizes to the manchette in elongating spermatids (PubMed:28003339). {ECO:0000250|UniProtKB:Q96ED9, ECO:0000269|PubMed:28003339}. SUBUNIT: Self-associates (By similarity). Component of the FTS/Hook/FHIP complex (FHF complex), composed of AKTIP/FTS, FAM160A2, and one or more members of the Hook family of proteins HOOK1, HOOK2, and HOOK3 (By similarity). May interact directly with AKTIP/FTS, HOOK1 and HOOK3 (By similarity). Associates with several subunits of the homotypic vesicular sorting complex (the HOPS complex) including VPS16 and VPS41; these interactions may be indirect (By similarity). Interacts with CNTRL (By similarity). Interacts with microtubules (By similarity). Interacts with ZC3H14 (By similarity). Interacts with LRGUK (via guanylate kinase-like domain) (PubMed:25781171, PubMed:28003339). Interacts with CCDC181 (PubMed:28283191). {ECO:0000250|UniProtKB:Q96ED9, ECO:0000269|PubMed:25781171, ECO:0000269|PubMed:28003339, ECO:0000269|PubMed:28283191}. TISSUE SPECIFICITY: Expressed in brain, cerebellum, kidney, liver and heart, with highest levels in heart and kidney (at protein level). {ECO:0000269|PubMed:17140400}. +Q9D5T7 HORM1_MOUSE HORMA domain-containing protein 1 (Newborn ovary HORMA protein) 392 44,933 Alternative sequence (1); Chain (1); Domain (1); Modified residue (1); Motif (1); Sequence conflict (1) FUNCTION: Plays a key role in meiotic progression (PubMed:19686734, PubMed:21079677, PubMed:21478856). Regulates 3 different functions during meiosis: ensures that sufficient numbers of processed DNA double-strand breaks (DSBs) are available for successful homology search by increasing the steady-state numbers of single-stranded DSB ends (PubMed:19686734, PubMed:21079677). Promotes synaptonemal-complex formation independently of its role in homology search (PubMed:19686734, PubMed:21079677). Plays a key role in the male mid-pachytene checkpoint and the female meiotic prophase checkpoint: required for efficient build-up of ATR activity on unsynapsed chromosome regions, a process believed to form the basis of meiotic silencing of unsynapsed chromatin (MSUC) and meiotic prophase quality control in both sexes (PubMed:21478856). {ECO:0000269|PubMed:19686734, ECO:0000269|PubMed:21079677, ECO:0000269|PubMed:21478856}. PTM: Phosphorylated at Ser-375 in a SPO11-dependent manner. {ECO:0000269|PubMed:19686734, ECO:0000269|PubMed:22346761}. SUBCELLULAR LOCATION: Isoform 1: Nucleus {ECO:0000269|PubMed:19686734, ECO:0000269|PubMed:19851446}. Chromosome {ECO:0000269|PubMed:19686734, ECO:0000269|PubMed:19851446, ECO:0000269|PubMed:22346761, ECO:0000269|PubMed:22549958, ECO:0000269|PubMed:27723721}. Note=Preferentially localizes to unsynapsed or desynapsed chromosomal regions during the prophase I stage of meiosis (PubMed:19851446, PubMed:19686734, PubMed:27723721). Accumulates on the chromosomes during the leptotene to zygotene stages of meiotic prophase I (PubMed:19851446, PubMed:19686734, PubMed:27723721). As germ cells progress into the pachytene stage, disappears from the synapsed chromosomal regions (PubMed:19851446, PubMed:19686734, PubMed:27723721). Once the chromosomes desynapse during the diplotene stage, it again accumulates on the chromosome axis of the desynapsed homologs (PubMed:19851446, PubMed:19686734, PubMed:27723721). TRIP13 is required for depletion from synapsed chromosomes (PubMed:19851446). The expression of the phosphorylated form at Ser-375 is restricted to unsynapsed chromosomal regions (PubMed:22346761). {ECO:0000269|PubMed:19686734, ECO:0000269|PubMed:19851446, ECO:0000269|PubMed:22346761, ECO:0000269|PubMed:27723721}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm {ECO:0000269|PubMed:19686734}. SUBUNIT: Interacts with HORMAD2 (PubMed:22549958). Interacts with IHO1/CCDC36 (PubMed:27723721). {ECO:0000269|PubMed:22549958, ECO:0000269|PubMed:27723721}. TISSUE SPECIFICITY: Specifically expressed in meiotic germ cells. {ECO:0000269|PubMed:15567723, ECO:0000269|PubMed:19686734, ECO:0000269|PubMed:19851446, ECO:0000269|PubMed:21079677}. +Q99P31 HPBP1_MOUSE Hsp70-binding protein 1 (HspBP1) (Heat shock protein-binding protein 1) (Hsp70-interacting protein 1) 357 39,167 Chain (1); Frameshift (1); Modified residue (2); Repeat (4); Sequence conflict (1) FUNCTION: Inhibits HSPA1A chaperone activity by changing the conformation of the ATP-binding domain of HSPA1A and interfering with ATP binding. Interferes with ubiquitination mediated by STUB1 and inhibits chaperone-assisted degradation of target proteins (By similarity). {ECO:0000250}. SUBUNIT: Interacts with the ATP-binding domain of HSPA1A. Detected in a ternary complex containing STUB1, HSPA1A and HSPBP1 (By similarity). {ECO:0000250}. +P49429 HPPD_MOUSE 4-hydroxyphenylpyruvate dioxygenase (EC 1.13.11.27) (4-hydroxyphenylpyruvic acid oxidase) (4HPPD) (HPD) (HPPDase) (F Alloantigen) (F protein) 393 45,054 Chain (1); Domain (2); Initiator methionine (1); Metal binding (3); Modified residue (5); Natural variant (1); Sequence conflict (4) Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 3/6. FUNCTION: Key enzyme in the degradation of tyrosine. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. DISEASE: Note=Defects in Hpd are the cause of tyrosinemia type III. +Q80WM5 HPLN3_MOUSE Hyaluronan and proteoglycan link protein 3 359 40,740 Chain (1); Disulfide bond (5); Domain (3); Sequence conflict (2); Signal peptide (1) FUNCTION: May function in hyaluronic acid binding. {ECO:0000303|PubMed:12663660}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. +P59438 HPS5_MOUSE Hermansky-Pudlak syndrome 5 protein homolog (Ruby-eye protein 2) (Ru2) 1126 126,337 Alternative sequence (3); Chain (1); Compositional bias (1); Modified residue (3); Sequence conflict (4) FUNCTION: May regulate the synthesis and function of lysosomes and of highly specialized organelles, such as melanosomes and platelet dense granules. Regulates intracellular vesicular trafficking in fibroblasts. May be involved in the regulation of general functions of integrins. {ECO:0000250|UniProtKB:Q9UPZ3}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9UPZ3}. SUBUNIT: Component of the biogenesis of lysosome-related organelles complex-2 (or BLOC2) composed of HPS3, HPS5 and HPS6. Interacts with HPS6 and HPS3. May interact with all alpha-integrin chains that have an aromatic residue before the first lysine of the conserved KXGFFKR motif, including ITGA2, ITGA3, ITGA5 and ITGA6. {ECO:0000250|UniProtKB:Q9UPZ3}. TISSUE SPECIFICITY: Widely expressed, with lowest expression in skeletal muscle and spleen. "DISEASE: Note=Defects in Hps5 are the cause of Hermansky-Pudlak-like syndrome, a syndrome characterized by hypopigmented eyes and coat, melanosomes greatly reduced in number and morphologically bizarre, kidney proximal tubules secreting lysosomal enzymes into urine at greatly reduced rates, platelet dense granules deficient in critical components, such as serotonin and adenine nucleotides, leading to functionally abnormal platelets and prolonged bleeding times, and mast cell granules undergoing unregulated ""kiss-and-run"" fusion at the plasma membrane. {ECO:0000269|PubMed:12548288}." +Q8BLY7 HPS6_MOUSE Hermansky-Pudlak syndrome 6 protein homolog (Ruby-eye protein) (Ru) 805 87,341 Chain (1); Natural variant (1); Sequence conflict (3) FUNCTION: May regulate the synthesis and function of lysosomes and of highly specialized organelles, such as melanosomes and platelet dense granules (By similarity). Acts as cargo adapter for the dynein-dynactin motor complex to mediate the transport of lysosomes from the cell periphery to the perinuclear region. Facilitates retrograde lysosomal trafficking by linking the motor complex to lysosomes, and perinuclear positioning of lysosomes is crucial for the delivery of endocytic cargos to lysosomes, for lysosome maturation and functioning (PubMed:25189619). {ECO:0000250|UniProtKB:Q86YV9, ECO:0000269|PubMed:25189619}. SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250|UniProtKB:Q86YV9}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q86YV9}. Early endosome membrane {ECO:0000250|UniProtKB:Q86YV9}. Lysosome membrane {ECO:0000250|UniProtKB:Q86YV9}. SUBUNIT: Component of the biogenesis of lysosome-related organelles complex-2 (or BLOC2) composed of HPS3, HPS5 and HPS6. Interacts with HPS5 and HPS3. Interacts with biogenesis of lysosome-related organelles complex-1 (BLOC1). Interacts with dynein intermediate chain (By similarity). Interacts with AP-3 complex (PubMed:19010779). Interacts with DCTN1 (PubMed:25189619). {ECO:0000250|UniProtKB:Q86YV9, ECO:0000269|PubMed:19010779, ECO:0000269|PubMed:25189619}. TISSUE SPECIFICITY: Widely expressed, with lowest expression in skeletal muscle. "DISEASE: Note=Defects in Hps6 are the cause of Hermansky-Pudlak-like syndrome, a syndrome characterized by hypopigmented eyes and coat, melanosomes greatly reduced in number and morphologically bizarre, kidney proximal tubules secreting lysosomal enzymes into urine at greatly reduced rates, platelet dense granules deficient in critical components, such as serotonin and adenine nucleotides, leading to functionally abnormal platelets and prolonged bleeding times, and mast cell granules undergoing unregulated ""kiss-and-run"" fusion at the plasma membrane. {ECO:0000269|PubMed:12548288}." +Q6YGZ1 HPSE_MOUSE Heparanase (EC 3.2.1.166) (Endo-glucoronidase) [Cleaved into: Heparanase 8 kDa subunit; Heparanase 50 kDa subunit] 535 60,066 Active site (2); Binding site (3); Chain (2); Disulfide bond (2); Glycosylation (3); Propeptide (1); Region (7); Sequence conflict (7); Signal peptide (1) FUNCTION: Endoglycosidase that cleaves heparan sulfate proteoglycans (HSPGs) into heparan sulfate side chains and core proteoglycans. Participates in extracellular matrix (ECM) degradation and remodeling. Selectively cleaves the linkage between a glucuronic acid unit and an N-sulfo glucosamine unit carrying either a 3-O-sulfo or a 6-O-sulfo group. Can also cleave the linkage between a glucuronic acid unit and an N-sulfo glucosamine unit carrying a 2-O-sulfo group, but not linkages between a glucuronic acid unit and a 2-O-sulfated iduronic acid moiety. It is essentially inactive at neutral pH but becomes active under acidic conditions such as during tumor invasion and in inflammatory processes. Facilitates cell migration associated with metastasis, wound healing and inflammation. Enhances shedding of syndecans, and increases endothelial invasion and angiogenesis in myelomas. Acts as procoagulant by increasing the generation of activation factor X in the presence of tissue factor and activation factor VII. Increases cell adhesion to the extracellular matrix (ECM), independent of its enzymatic activity. Induces AKT1/PKB phosphorylation via lipid rafts increasing cell mobility and invasion. Heparin increases this AKT1/PKB activation. Regulates osteogenesis. Enhances angiogenesis through up-regulation of SRC-mediated activation of VEGF. Implicated in hair follicle inner root sheath differentiation and hair homeostasis. {ECO:0000269|PubMed:15677344, ECO:0000269|PubMed:15793281, ECO:0000269|PubMed:17689495, ECO:0000269|PubMed:18589009}. PTM: Proteolytically processed. The cleavage of the 65 kDa form leads to the generation of a linker peptide, and the 8 kDa and 50 kDa products. The active form, the 8/50 kDa heterodimer, is resistant to degradation. Complete removal of the linker peptide appears to be a prerequisite to the complete activation of the enzyme (By similarity). {ECO:0000250}.; PTM: N-glycosylated. Glycosylation of the 50 kDa subunit appears to be essential for its solubility. {ECO:0000269|PubMed:12460766}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Secreted {ECO:0000269|PubMed:15793281}. Nucleus {ECO:0000269|PubMed:15793281}. Note=Proheparanase is secreted via vesicles of the Golgi. Interacts with cell membrane heparan sulfate proteoglycans (HSPGs). Endocytosed and accumulates in endosomes. Transferred to lysosomes where it is proteolytically cleaved to produce the active enzyme. Under certain stimuli, transferred to the cell surface. Colocalizes with SDC1 in endosomal/lysosomal vesicles. Accumulates in perinuclear lysosomal vesicles. Heparin retains proheparanase in the extracellular medium (By similarity). Associates with lipid rafts. {ECO:0000250}. SUBUNIT: Heterodimer; heterodimer formation between the 8 kDa and the 50 kDa subunits is required for enzyme activity. Interacts with TF; the interaction, inhibited by heparin, enhances the generation of activated factor X and activates coagulation. Interacts with HRG; the interaction is enhanced at acidic pH, partially inhibits binding of HPSE to cell surface receptors and modulates its enzymatic activity. Interacts with SDC1; the interaction enhances the shedding of SDC1 (By similarity). Interacts with HPSE2 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in skin, mainly in the stratum granulosum and the first layer of the stratum corneum in the upper part of the epidermis. Also detected in hair follicles and in sebaceous glands. {ECO:0000269|PubMed:15793281, ECO:0000269|PubMed:18589009}. +Q9CPX5 HRSL5_MOUSE Ca(2+)-independent N-acyltransferase (iNAT) (EC 2.3.1.-) (H-rev107-like protein 5) (HRAS-like suppressor 5) (HRSL5) 270 29,866 Alternative sequence (4); Chain (1); Erroneous initiation (2); Sequence conflict (2) FUNCTION: catalyzes N-acylation of phosphatidylethanolamine (PE) to generate N-Acylphosphatidylethanolamine (NAPE) a precursor of bioactive N-acylethanolamines, including the endocannabinoid anandamide. {ECO:0000269|PubMed:17158102, ECO:0000269|PubMed:19000777}. TISSUE SPECIFICITY: Highest expression level in testis. {ECO:0000269|PubMed:19000777}. +Q673U1 HS3S2_MOUSE Heparan sulfate glucosamine 3-O-sulfotransferase 2 (EC 2.8.2.29) (Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 2) (Heparan sulfate 3-O-sulfotransferase 2) 367 41,378 Alternative sequence (4); Binding site (2); Chain (1); Disulfide bond (1); Glycosylation (4); Nucleotide binding (2); Region (3); Topological domain (2); Transmembrane (1) TRANSMEM 20 39 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 19 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 40 367 Lumenal. {ECO:0000255}. FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to an N-unsubstituted glucosamine linked to a 2-O-sulfo iduronic acid unit on heparan sulfate. Catalyzes the O-sulfation of glucosamine in GlcA2S-GlcNS. Unlike 3-OST-1, does not convert non-anticoagulant heparan sulfate to anticoagulant heparan sulfate (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. +Q8BKN6 HS3SA_MOUSE Heparan sulfate glucosamine 3-O-sulfotransferase 3A1 (EC 2.8.2.23) (Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 3A1) (Heparan sulfate 3-O-sulfotransferase 3A1) 393 43,483 Binding site (2); Chain (1); Disulfide bond (1); Glycosylation (2); Nucleotide binding (2); Region (3); Topological domain (2); Transmembrane (1) TRANSMEM 25 43 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 24 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 44 393 Lumenal. {ECO:0000255}. FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to an N-unsubstituted glucosamine linked to a 2-O-sulfo iduronic acid unit on heparan sulfate. Catalyzes the O-sulfation of glucosamine in IdoUA2S-GlcNS and also in IdoUA2S-GlcNH2. Unlike 3-OST-1, does not convert non-anticoagulant heparan sulfate to anticoagulant heparan sulfate (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. +P11499 HS90B_MOUSE Heat shock protein HSP 90-beta (Heat shock 84 kDa) (HSP 84) (HSP84) (Tumor-specific transplantation 84 kDa antigen) (TSTA) 724 83,281 Binding site (5); Chain (1); Glycosylation (2); Initiator methionine (1); Modified residue (22); Motif (1); Region (3); Sequence conflict (14); Site (1) FUNCTION: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle. Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels. In the first place, they alter the steady-state levels of certain transcription factors in response to various physiological cues. Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression. Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation. Promotes cell differentiation by chaperoning BIRC2 and thereby protecting from auto-ubiquitination and degradation by the proteasomal machinery. Main chaperone that is involved in the phosphorylation/activation of the STAT1 by chaperoning both JAK2 and PRKCE under heat shock and in turn, activates its own transcription. {ECO:0000250|UniProtKB:P08238}. PTM: ISGylated. {ECO:0000269|PubMed:16139798}.; PTM: Ubiquitinated in the presence of STUB1-UBE2D1 complex (in vitro). {ECO:0000250|UniProtKB:P08238}.; PTM: S-nitrosylated; negatively regulates the ATPase activity. {ECO:0000250|UniProtKB:P08238}.; PTM: Phosphorylation at Tyr-301 by SRC is induced by lipopolysaccharide. Phosphorylation at Ser-226 and Ser-255 inhibits AHR interaction. {ECO:0000250|UniProtKB:P08238}.; PTM: Methylated by SMYD2; facilitates dimerization and chaperone complex formation; promotes cancer cell proliferation. {ECO:0000250|UniProtKB:P08238}.; PTM: Cleaved following oxidative stress resulting in HSP90AB1 protein radicals formation; disrupts the chaperoning function and the degradation of its client proteins. {ECO:0000250|UniProtKB:P08238}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P08238}. Melanosome {ECO:0000250|UniProtKB:P08238}. Nucleus {ECO:0000250|UniProtKB:P08238}. Secreted {ECO:0000250|UniProtKB:P08238}. Cell membrane {ECO:0000250|UniProtKB:P08238}. Note=Translocates with BIRC2 from the nucleus to the cytoplasm during differentiation. Secreted when associated with TGFB1 processed form (LAP). {ECO:0000250|UniProtKB:P08238}. SUBUNIT: Monomer (By similarity). Homodimer (PubMed:8289821). Forms a complex with CDK6 and CDC37. Interacts with UNC45A; binding to UNC45A involves 2 UNC45A monomers per HSP90AB1 dimer (By similarity). Interacts with CHORDC1 (PubMed:15642353). Interacts with DNAJC7. Interacts with FKBP4. May interact with NWD1. Interacts with SGTA. Interacts with HSF1 in an ATP-dependent manner. Interacts with MET; the interaction suppresses MET kinase activity. Interacts with ERBB2 in an ATP-dependent manner; the interaction suppresses ERBB2 kinase activity. Interacts with HIF1A, KEAP1 and RHOBTB2. Interacts with STUB1 and SMAD3. Interacts with XPO1 and AHSA1. Interacts with BIRC2. Interacts with KCNQ4; promotes cell surface expression of KCNQ4. Interacts with BIRC2; prevents auto-ubiquitination and degradation of its client protein BIRC2. Interacts with NOS3. Interacts with AHR; interaction is inhibited by HSP90AB1 phosphorylation on Ser-226 and Ser-255. Interacts with STIP1 and CDC37; upon SMYD2-dependent methylation. Interacts with JAK2 and PRKCE; promotes functional activation in a heat shock-dependent manner. Interacts with HSP90AA1; interaction is constitutive. HSP90AB1-CDC37 chaperone complex interacts with inactive MAPK7 (via N-terminal half) in resting cells; the interaction is MAP2K5-independent and prevents from ubiquitination and proteasomal degradation. Interacts with CDC25A; prevents heat shock-mediated CDC25A degradation and contributes to cell cycle progression. Interacts with TP53 (via DNA binding domain); suppresses TP53 aggregation and prevents from irreversible thermal inactivation. Interacts with TGFB1 processed form (LAP); inhibits latent TGFB1 activation (By similarity). Interacts with TRIM8; prevents nucleus translocation of phosphorylated STAT3 and HSP90AB1 (PubMed:21689689). {ECO:0000250|UniProtKB:P08238, ECO:0000269|PubMed:15642353, ECO:0000269|PubMed:21689689, ECO:0000269|PubMed:8289821}. DOMAIN: The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins. {ECO:0000250|UniProtKB:P07900}. +P17879 HS71B_MOUSE Heat shock 70 kDa protein 1B (Heat shock 70 kDa protein 1) (HSP70.1) 642 70,176 Binding site (1); Chain (1); Initiator methionine (1); Modified residue (11); Nucleotide binding (4); Region (2) FUNCTION: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The co-chaperones have been shown to not only regulate different steps of the ATPase cycle, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The co-chaperones are of three types: J-domain co-chaperones such as HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1. Maintains protein homeostasis during cellular stress through two opposing mechanisms: protein refolding and degradation. Its acetylation/deacetylation state determines whether it functions in protein refolding or protein degradation by controlling the competitive binding of co-chaperones HOPX and STUB1. During the early stress response, the acetylated form binds to HOPX which assists in chaperone-mediated protein refolding, thereafter, it is deacetylated and binds to ubiquitin ligase STUB1 that promotes ubiquitin-mediated protein degradation. Regulates centrosome integrity during mitosis, and is required for the maintenance of a functional mitotic centrosome that supports the assembly of a bipolar mitotic spindle. Enhances STUB1-mediated SMAD3 ubiquitination and degradation and facilitates STUB1-mediated inhibition of TGF-beta signaling. Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation. {ECO:0000250|UniProtKB:P0DMV9}. PTM: In response to cellular stress, acetylated at Lys-77 by NA110 and then gradually deacetylated by HDAC4 at later stages. Acetylation enhances its chaperone activity and also determines whether it will function as a chaperone for protein refolding or degradation by controlling its binding to co-chaperones HOPX and STUB1. The acetylated form and the non-acetylated form bind to HOPX and STUB1 respectively. Acetylation also protects cells against various types of cellular stress. {ECO:0000250|UniProtKB:P0DMV9}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0DMV9}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P0DMV9}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. {ECO:0000250|UniProtKB:P0DMV9}. SUBUNIT: Component of the CatSper complex (PubMed:17478420, PubMed:19516020). Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs (By similarity). Interacts with CHCHD3, DNAJC7, IRAK1BP1, PPP5C and TSC2 (By similarity). Interacts with TERT; the interaction occurs in the absence of the RNA component, TERC, and dissociates once the TERT complex has formed (By similarity). Interacts with TRIM5 (via B30.2/SPRY domain) (By similarity). Interacts with METTL21A (By similarity). Interacts with PRKN (By similarity). Interacts with FOXP3 (PubMed:23973223). Interacts with NOD2; the interaction enhances NOD2 stability (By similarity). Interacts with DNAJC9 (via J domain) (By similarity). Interacts with ATF5; the interaction protects ATF5 from degradation via proteasome-dependent and caspase-dependent processes. Interacts with NAA10, HSP40, HSP90 and HDAC4. The acetylated form and the non-acetylated form interact with HOPX and STUB1 respectively. Interacts with NEDD1 and SMAD3. Interacts (via NBD) with BAG1, BAG2, BAG3 and HSPH1/HSP105. Interacts with DNAJC8 (By similarity). {ECO:0000250|UniProtKB:P0DMV9, ECO:0000269|PubMed:17478420, ECO:0000269|PubMed:19516020, ECO:0000269|PubMed:23973223}. DOMAIN: The N-terminal nucleotide binding domain (NBD) (also known as the ATPase domain) is responsible for binding and hydrolyzing ATP. The C-terminal substrate-binding domain (SBD) (also known as peptide-binding domain) binds to the client/substrate proteins. The two domains are allosterically coupled so that, when ATP is bound to the NBD, the SBD binds relatively weakly to clients. When ADP is bound in the NBD, a conformational change enhances the affinity of the SBD for client proteins. {ECO:0000250|UniProtKB:P0DMV9}. TISSUE SPECIFICITY: Testis-specific. +P38532 HSF1_MOUSE Heat shock factor protein 1 (HSF 1) (Heat shock transcription factor 1) (HSTF 1) 525 57,223 Alternative sequence (1); Chain (1); Cross-link (7); Modified residue (25); Motif (1); Region (6) FUNCTION: Function as a stress-inducible and DNA-binding transcription factor that plays a central role in the transcriptional activation of the heat shock response (HSR), leading to the expression of a large class of molecular chaperones heat shock proteins (HSPs) that protect cells from cellular insults' damage. In unstressed cells, is present in a HSP90-containing multichaperone complex that maintains it in a non-DNA-binding inactivated monomeric form. Upon exposure to heat and other stress stimuli, undergoes homotrimerization and activates HSP gene transcription through binding to site-specific heat shock elements (HSEs) present in the promoter regions of HSP genes. Activation is reversible, and during the attenuation and recovery phase period of the HSR, returns to its unactivated form. Binds to inverted 5'-NGAAN-3' pentamer DNA sequences. Binds to chromatin at heat shock gene promoters. Plays also several other functions independently of its transcriptional activity. Involved in the repression of Ras-induced transcriptional activation of the c-fos gene in heat-stressed cells. Positively regulates pre-mRNA 3'-end processing and polyadenylation of HSP70 mRNA upon heat-stressed cells in a symplekin (SYMPK)-dependent manner. Plays a role in nuclear export of stress-induced HSP70 mRNA. Plays a role in the regulation of mitotic progression. Plays also a role as a negative regulator of non-homologous end joining (NHEJ) repair activity in a DNA damage-dependent manner. Involved in stress-induced cancer cell proliferation in a IER5-dependent manner. {ECO:0000250|UniProtKB:Q00613}. PTM: Phosphorylated. Phosphorylated in unstressed cells; this phosphorylation is constitutive and implicated in the repression of HSF1 transcriptional activity. Phosphorylated on Ser-121 by MAPKAPK2; this phosphorylation promotes interaction with HSP90 proteins and inhibits HSF1 homotrimerization, DNA-binding and transactivation activities. Phosphorylation on Ser-303 by GSK3B/GSK3-beat and on Ser-307 by MAPK3 within the regulatory domain is involved in the repression of HSF1 transcriptional activity and occurs in a RAF1-dependent manner. Phosphorylation on Ser-303 and Ser-307 increases HSF1 nuclear export in a YWHAE- and XPO1/CRM1-dependent manner. Phosphorylation on Ser-307 is a prerequisite for phosphorylation on Ser-303. According to, Ser-303 is not phosphorylated in unstressed cells. Phosphorylated on Ser-415 by PLK1; phosphorylation promotes nuclear translocation upon heat shock. Hyperphosphorylated upon heat shock and during the attenuation and recovery phase period of the heat shock response. Phosphorylated on Thr-142; this phosphorylation increases HSF1 transactivation activity upon heat shock. Phosphorylation on Ser-230 by CAMK2A; this phosphorylation enhances HSF1 transactivation activity upon heat shock. Phosphorylation on Ser-326 by MAPK12; this phosphorylation enhances HSF1 nuclear translocation, homotrimerization and transactivation activities upon heat shock. Phosphorylated on Ser-320 by PRKACA/PKA; this phosphorylation promotes nuclear localization and transcriptional activity upon heat shock. Phosphorylated by MAPK8; this phosphorylation occurs upon heat shock, induces HSF1 translocation into nuclear stress bodies and negatively regulates transactivation activity. Neither basal nor stress-inducible phosphorylation on Ser-230, Ser-292, Ser-303, Ser-307, Ser-314, Ser-319, Ser-320, Thr-323, Ser-326, Ser-338, Ser-345, Ser-364 and Thr-365 within the regulatory domain is involved in the regulation of HSF1 subcellular localization or DNA-binding activity; however, it negatively regulates HSF1 transactivation activity. Phosphorylated on Ser-216 by PLK1 in the early mitotic period; this phosphorylation regulates HSF1 localization to the spindle pole, the recruitment of the SCF(BTRC) ubiquitin ligase complex inducing HSF1 degradation, and hence mitotic progression. Dephosphorylated on Ser-121, Ser-307, Ser-314 and Thr-323 by phosphatase PPP2CA in an IER5-dependent manner, leading to HSF1-mediated transactivation activity. {ECO:0000250|UniProtKB:Q00613}.; PTM: Sumoylated with SUMO1 and SUMO2 upon heat shock in a ERK2-dependent manner. Sumoylated by SUMO1 on Lys-298; sumoylation occurs upon heat shock and promotes its localization to nuclear stress bodies and DNA-binding activity. Phosphorylation on Ser-303 and Ser-307 is probably a prerequisite for sumoylation. {ECO:0000250|UniProtKB:Q00613}.; PTM: Acetylated on Lys-118; this acetylation is decreased in a IER5-dependent manner. Acetylated on Lys-118, Lys-208 and Lys-298; these acetylations occur in a EP300-dependent manner. Acetylated on Lys-80; this acetylation inhibits DNA-binding activity upon heat shock. Deacetylated on Lys-80 by SIRT1; this deacetylation increases DNA-binding activity. {ECO:0000250|UniProtKB:Q00613}.; PTM: Ubiquitinated by SCF(BTRC) and degraded following stimulus-dependent phosphorylation at Ser-216 by PLK1 in mitosis. Polyubiquitinated. Undergoes proteasomal degradation upon heat shock and during the attenuation and recovery phase period of the heat shock response. {ECO:0000250|UniProtKB:Q00613}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26159920}. Cytoplasm {ECO:0000269|PubMed:26159920}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q00613}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q00613}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q00613}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q00613}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q00613}. Note=The monomeric form is cytoplasmic in unstressed cells (PubMed:26159920). Predominantly nuclear protein in both unstressed and heat shocked cells. Translocates in the nucleus upon heat shock. Nucleocytoplasmic shuttling protein. Colocalizes with IER5 in the nucleus. Colocalizes with BAG3 to the nucleus upon heat stress. Localizes in subnuclear granules called nuclear stress bodies (nSBs) upon heat shock. Colocalizes with SYMPK and SUMO1 in nSBs upon heat shock. Colocalizes with PRKACA/PKA in the nucleus and nSBs upon heat shock. Relocalizes from the nucleus to the cytoplasm during the attenuation and recovery phase period of the heat shock response. Translocates in the cytoplasm in a YWHAE- and XPO1/CRM1-dependent manner. Together with histone H2AX, redistributed in discrete nuclear DNA damage-induced foci after ionizing radiation (IR). Colocalizes with calcium-responsive transactivator SS18L1 at kinetochore region on the mitotic chromosomes. Colocalizes with gamma tubulin at centrosome. Localizes at spindle pole in metaphase. Colocalizes with PLK1 at spindle poles during prometaphase. {ECO:0000250|UniProtKB:Q00613, ECO:0000269|PubMed:26159920}. SUBUNIT: Monomer; cytoplasmic latent and transcriptionally inactive monomeric form in unstressed cells. Homotrimer; in response to stress, such as heat shock, homotrimerizes and translocates into the nucleus, binds to heat shock element (HSE) sequences in promoter of heat shock protein (HSP) genes and acquires transcriptional ability. Interacts (via monomeric form) with FKBP4; this interaction occurs in unstressed cells. Associates (via monomeric form) with HSP90 proteins in a multichaperone complex in unnstressed cell; this association maintains HSF1 in a non-DNA-binding and transcriptional inactive form by preventing HSF1 homotrimerization. Homotrimeric transactivation activity is modulated by protein-protein interactions and post-translational modifications. Interacts with HSP90AA1; this interaction is decreased in a IER5-dependent manner, promoting HSF1 accumulation in the nucleus, homotrimerization and DNA-binding activities. Part (via regulatory domain in the homotrimeric form) of a large heat shock-induced HSP90-dependent multichaperone complex at least composed of FKBP4, FKBP5, HSP90 proteins, PPID, PPP5C and PTGES3; this association maintains the HSF1 homotrimeric DNA-bound form in a transcriptionally inactive form. Interacts with BAG3 (via BAG domain); this interaction occurs in normal and heat-shocked cells promoting nuclear shuttling of HSF1 in a BAG3-dependent manner. Interacts (via homotrimeric and hyperphosphorylated form) with FKBP4; this interaction occurs upon heat shock in a HSP90-dependent multichaperone complex. Interacts (via homotrimeric form preferentially) with EEF1A proteins. In heat shocked cells, stress-denatured proteins compete with HSF1 homotrimeric DNA-bound form for association of the HSP90-dependent multichaperone complex, and hence alleviating repression of HSF1-mediated transcriptional activity. Interacts (via homotrimeric form preferentially) with DAXX; this interaction relieves homotrimeric HSF1 from repression of its transcriptional activity by HSP90-dependent multichaperone complex upon heat shock. Interacts (via D domain and preferentially with hyperphosphorylated form) with JNK1; this interaction occurs under both normal growth conditions and immediately upon heat shock. Interacts (via D domain and preferentially with hyperphosphorylated form) with MAPK3; this interaction occurs upon heat shock. Interacts with IER5 (via central region); this interaction promotes PPP2CA-induced dephosphorylation on Ser-121, Ser-307, Ser-314 and Thr-323 and HSF1 transactivation activity. Found in a ribonucleoprotein complex composed of the HSF1 homotrimeric form, translation elongation factor eEF1A proteins and non-coding RNA heat shock RNA-1 (HSR1); this complex occurs upon heat shock and stimulates HSF1 DNA-binding activity. Interacts (via transactivation domain) with HSPA1A/HSP70 and DNAJB1; these interactions result in the inhibition of heat shock- and HSF1-induced transcriptional activity during the attenuation and recovery phase from heat shock. Interacts (via Ser-303 and Ser-307 phosphorylated form) with YWHAE; this interaction promotes HSF1 sequestration in the cytoplasm in an ERK-dependent manner. Found in a complex with IER5 and PPP2CA. Interacts with TPR; this interaction increases upon heat shock and stimulates export of HSP70 mRNA. Interacts with SYMPK (via N-terminus) and CSTF2; these interactions occur upon heat shock. Interacts (via transactivation domain) with HSPA8. Interacts with EEF1D; this interaction occurs at heat shock promoter element (HSE) sequences. Interacts with MAPKAPK2. Interacts with PRKACA/PKA. Interacts (via transactivation domain) with GTF2A2. Interacts (via transactivation domain) with GTF2B. Interacts (via transactivation domain) with TBP. Interacts with CDK9, CCNT1 and EP300. Interacts (via N-terminus) with XRCC5 (via N-terminus) and XRCC6 (via N-terminus); these interactions are direct and prevent XRCC5/XRCC6 heterodimeric binding and non-homologous end joining (NHEJ) repair activities induced by ionizing radiation (IR). Interacts with PLK1; this interaction occurs during the early mitotic period, increases upon heat shock but does not modulate neither HSF1 homotrimerization and DNA-binding activities. Interacts (via Ser-216 phosphorylated form) with CDC20; this interaction occurs in mitosis in a MAD2L1-dependent manner and prevents PLK1-stimulated degradation of HSF1 by blocking the recruitment of the SCF(BTRC) ubiquitin ligase complex. Interacts with MAD2L1; this interaction occurs in mitosis. Interacts with BTRC; this interaction occurs during mitosis, induces its ubiquitin-dependent degradation following stimulus-dependent phosphorylation at Ser-216, a process inhibited by CDC20. Interacts with HSP90AA1 and HSP90AB1. {ECO:0000250|UniProtKB:Q00613}. DOMAIN: In unstressed cells, spontaneous homotrimerization is inhibited. Intramolecular interactions between the hydrophobic repeat HR-A/B and HR-C regions are necessary to maintain HSF1 in the inactive, monomeric conformation. Furthermore, intramolecular interactions between the regulatory domain and the nonadjacent transactivation domain prevents transcriptional activation, a process that is relieved upon heat shock. The regulatory domain is necessary for full repression of the transcriptional activation domain in unstressed cells through its phosphorylation on Ser-303 and Ser-307. In heat stressed cells, HSF1 homotrimerization occurs through formation of a three-stranded coiled-coil structure generated by intermolecular interactions between HR-A/B regions allowing DNA-binding activity. The D domain is necessary for translocation to the nucleus, interaction with JNK1 and MAPK3 and efficient JNK1- and MAPK3-dependent phosphorylation. The regulatory domain confers heat shock inducibility on the transcriptional transactivation domain. The regulatory domain is necessary for transcriptional activation through its phosphorylation on Ser-230 upon heat shock. 9aaTAD is a transactivation motif present in a large number of yeast and animal transcription factors. {ECO:0000250|UniProtKB:Q00613}. +D0VYS2 HSF3_MOUSE Heat shock factor protein 3 (HSF 3) (Heat shock transcription factor 3) (HSTF 3) (mHSF3) 492 57,302 Alternative sequence (3); Chain (1); DNA binding (1); Region (1); Sequence conflict (1) FUNCTION: DNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription of non-classical heat-shock genes such as PDZD2 and PROM2. Protects cells against heat shock and proteotoxic stress. {ECO:0000269|PubMed:19864465}. SUBCELLULAR LOCATION: Isoform 1: Cytoplasm {ECO:0000269|PubMed:19864465}. Nucleus {ECO:0000269|PubMed:19864465}. Note=Cytoplasmic under normal conditions. Translocates to the nucleus in response to heat shock. {ECO:0000269|PubMed:19864465}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm {ECO:0000269|PubMed:19864465}. Note=Does not translocate to the nucleus in response to heat shock. {ECO:0000269|PubMed:19864465}. +P09024 HXB7_MOUSE Homeobox protein Hox-B7 (Homeobox protein Hox-2.3) (Homeobox protein MH-22B) (Homeobox protein MuB1) 217 23,967 Chain (1); Compositional bias (1); DNA binding (1); Motif (1); Sequence conflict (9) FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. SUBCELLULAR LOCATION: Nucleus. +P01788 HVM19_MOUSE Ig heavy chain V region H8 123 13,805 Chain (1); Domain (1); Non-terminal residue (1) +P01790 HVM21_MOUSE Ig heavy chain V region M511 122 13,652 Chain (1); Domain (1); Non-terminal residue (1) +P01792 HVM23_MOUSE Ig heavy chain V region HPCG8 123 13,880 Chain (1); Domain (1); Non-terminal residue (1) +P01798 HVM29_MOUSE Ig heavy chain V-III region E109 113 12,647 Chain (1); Disulfide bond (1); Domain (1); Non-terminal residue (1) +O70252 HMOX2_MOUSE Heme oxygenase 2 (HO-2) (EC 1.14.14.18) 315 35,739 Chain (1); Initiator methionine (1); Metal binding (1); Modified residue (2); Repeat (2); Sequence conflict (2) FUNCTION: Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Heme oxygenase 2 could be implicated in the production of carbon monoxide in brain where it could act as a neurotransmitter. SUBCELLULAR LOCATION: Microsome. Endoplasmic reticulum. +Q00PI9 HNRL2_MOUSE Heterogeneous nuclear ribonucleoprotein U-like protein 2 (MLF1-associated nuclear protein) 745 84,940 Chain (1); Compositional bias (2); Domain (2); Modified residue (11); Sequence conflict (1) SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17008314}. SUBUNIT: Binds to MLF1 and retains it in the nucleus. {ECO:0000269|PubMed:17008314}. +Q8CFE2 HPF1_MOUSE Histone PARylation factor 1 346 39,291 Chain (1); Compositional bias (1); Modified residue (5); Region (1) FUNCTION: Acts as a cofactor for serine ADP-ribosylation by conferring serine specificity on PARP1 and PARP2: interacts with PARP1 and PARP2 and is able to change amino acid specificity toward serine. Promotes histone serine ADP-ribosylation in response to DNA damage, limiting DNA damage-induced PARP1 hyper-automodification, and ensuring genome stability. Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage. HPF1 also promotes tyrosine ADP-ribosylation, probably by conferring tyrosine specificity on PARP1. {ECO:0000250|UniProtKB:Q9NWY4}. SUBUNIT: Interacts with PARP1 (via the PARP catalytic domain). Interacts with histone H2A and histone H3 in a PARP1-dependent manner. Weakly interacts with PARP2 (via the PARP catalytic domain). {ECO:0000250|UniProtKB:Q9NWY4}. +P62748 HPCL1_MOUSE Hippocalcin-like protein 1 (Neural visinin-like protein 3) (NVL-3) (NVP-3) (Visinin-like protein 3) (VILIP-3) 193 22,338 Calcium binding (3); Chain (1); Domain (4); Initiator methionine (1); Lipidation (1) FUNCTION: May be involved in the calcium-dependent regulation of rhodopsin phosphorylation. SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P37235}; Lipid-anchor {ECO:0000250|UniProtKB:P37235}. +Q99KG7 HPS4_MOUSE Hermansky-Pudlak syndrome 4 protein homolog (Light-ear protein) (Le protein) 671 72,662 Chain (1); Natural variant (1); Sequence conflict (1) FUNCTION: Component of the BLOC-3 complex, a complex that acts as a guanine exchange factor (GEF) for RAB32 and RAB38, promotes the exchange of GDP to GTP, converting them from an inactive GDP-bound form into an active GTP-bound form. The BLOC-3 complex plays an important role in the control of melanin production and melanosome biogenesis and promotes the membrane localization of RAB32 and RAB38. {ECO:0000250|UniProtKB:Q9NQG7}. SUBUNIT: Component of the biogenesis of lysosome-related organelles complex-3 (or BLOC-3), a heterodimer of HPS1 and HPS4. HPS4 and the BLOC-3 complex interact with the GTP-bound form of RAB9B but not with the GDP-bound form of RAB9B (By similarity). HPS4 and the BLOC-3 complex interact with the GTP-bound form of RAB9A but not with the GDP-bound form of RAB9A (PubMed:20048159, PubMed:26620560,). HPS4 does not interact RAB4A and RAB7A (PubMed:26620560). {ECO:0000250|UniProtKB:Q9NQG7, ECO:0000269|PubMed:20048159, ECO:0000269|PubMed:26620560}. TISSUE SPECIFICITY: Highly expressed in heart, brain, liver and testis. Expressed at lower level in skeletal muscle. DISEASE: Note=Defects in Hps4 are the cause of the light ear (le) mutant which exhibits hypopigmentation associated with defects of multiple cytoplasmic organelles, including melanosomes, lysosomes, and granular elements of platelets (PubMed:11836498). {ECO:0000269|PubMed:11836498}. +Q61646 HPT_MOUSE Haptoglobin [Cleaved into: Haptoglobin alpha chain; Haptoglobin beta chain] 347 38,752 Chain (3); Disulfide bond (5); Domain (2); Glycosylation (4); Region (1); Signal peptide (1) FUNCTION: As a result of hemolysis, hemoglobin is found to accumulate in the kidney and is secreted in the urine. Haptoglobin captures, and combines with free plasma hemoglobin to allow hepatic recycling of heme iron and to prevent kidney damage. Haptoglobin also acts as an antioxidant, has antibacterial activity and plays a role in modulating many aspects of the acute phase response. Hemoglobin/haptoglobin complexes are rapidly cleared by the macrophage CD163 scavenger receptor expressed on the surface of liver Kupfer cells through an endocytic lysosomal degradation pathway (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Tetramer of two alpha and two beta chains; disulfide-linked. The hemoglobin/haptoglobin complex is composed of a haptoglobin dimer bound to two hemoglobin alpha-beta dimers. Interacts with CD163 (By similarity). {ECO:0000250}. DOMAIN: The beta chain mediates most of the interactions with both subunits of hemoglobin, while the alpha chain forms the homodimeric interface. {ECO:0000250}. TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma. +Q8BSL4 HS3S5_MOUSE Heparan sulfate glucosamine 3-O-sulfotransferase 5 (EC 2.8.2.23) (Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 5) (Heparan sulfate 3-O-sulfotransferase 5) 346 40,471 Binding site (3); Chain (1); Disulfide bond (1); Glycosylation (4); Nucleotide binding (2); Region (3); Topological domain (2); Transmembrane (1) TRANSMEM 13 32 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 12 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 33 346 Lumenal. {ECO:0000255}. FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to position 3 of glucosamine residues in heparan. Catalyzes the rate limiting step in the biosynthesis of heparan sulfate (HSact). This modification is a crucial step in the biosynthesis of anticoagulant heparan sulfate as it completes the structure of the antithrombin pentasaccharide binding site. Also generates GlcUA-GlcNS or IdoUA-GlcNS and IdoUA2S-GlcNH2 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. +Q5GFD5 HS3S6_MOUSE Heparan sulfate glucosamine 3-O-sulfotransferase 6 (EC 2.8.2.23) (Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 6) (3-OST-6) (Heparan sulfate 3-O-sulfotransferase 6) 342 37,415 Binding site (2); Chain (1); Disulfide bond (1); Glycosylation (1); Nucleotide binding (2); Region (3); Topological domain (2); Transmembrane (1) TRANSMEM 32 49 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 31 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 50 342 Lumenal. {ECO:0000255}. FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to heparan sulfate. Unlike 3-OST-1, does not convert non-anticoagulant heparan sulfate to anticoagulant heparan sulfate. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in liver and kidney, followed by heart, brain, lung and testis. {ECO:0000269|PubMed:15303968}. +P58406 HRH3_MOUSE Histamine H3 receptor (H3R) (HH3R) 445 48,541 Chain (1); Compositional bias (1); Glycosylation (1); Modified residue (1); Topological domain (8); Transmembrane (7) TRANSMEM 40 60 Helical; Name=1. {ECO:0000255}.; TRANSMEM 71 91 Helical; Name=2. {ECO:0000255}.; TRANSMEM 109 129 Helical; Name=3. {ECO:0000255}.; TRANSMEM 157 177 Helical; Name=4. {ECO:0000255}.; TRANSMEM 197 217 Helical; Name=5. {ECO:0000255}.; TRANSMEM 360 380 Helical; Name=6. {ECO:0000255}.; TRANSMEM 397 417 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 39 Extracellular. {ECO:0000255}.; TOPO_DOM 61 70 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 92 108 Extracellular. {ECO:0000255}.; TOPO_DOM 130 156 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 178 196 Extracellular. {ECO:0000255}.; TOPO_DOM 218 359 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 381 396 Extracellular. {ECO:0000255}.; TOPO_DOM 418 445 Cytoplasmic. {ECO:0000255}. FUNCTION: The H3 subclass of histamine receptors could mediate the histamine signals in CNS and peripheral nervous system. Signals through the inhibition of adenylate cyclase and displays high constitutive activity (spontaneous activity in the absence of agonist) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +P16627 HS71L_MOUSE Heat shock 70 kDa protein 1-like (Heat shock 70 kDa protein 1L) (Heat shock 70 kDa-like protein 1) (Spermatid-specific heat shock protein 70) 641 70,637 Binding site (1); Chain (1); Nucleotide binding (4); Region (2); Sequence conflict (2) FUNCTION: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. Positive regulator of PRKN translocation to damaged mitochondria. {ECO:0000250|UniProtKB:P34931}. SUBUNIT: Interacts with PRKN. {ECO:0000250|UniProtKB:P34931}. DOMAIN: The N-terminal nucleotide binding domain (NBD) (also known as the ATPase domain) is responsible for binding and hydrolyzing ATP. The C-terminal substrate-binding domain (SBD) (also known as peptide-binding domain) binds to the client/substrate proteins. The two domains are allosterically coupled so that, when ATP is bound to the NBD, the SBD binds relatively weakly to clients. When ADP is bound in the NBD, a conformational change enhances the affinity of the SBD for client proteins. {ECO:0000250|UniProtKB:P34931}. TISSUE SPECIFICITY: Expressed in spermatids. +Q9D4G2 HSF2B_MOUSE Heat shock factor 2-binding protein 338 37,963 Chain (1); Coiled coil (1) FUNCTION: Inhibits BNC1 transcriptional activity during spermatogenesis, probably by sequestering it in the cytoplasm (PubMed:23707421). May be involved in modulating HSF2 activation in testis (By similarity). {ECO:0000250|UniProtKB:O75031, ECO:0000269|PubMed:23707421}. PTM: Sumoylated by UBE2I in response to MEKK1-mediated stimuli. {ECO:0000250|UniProtKB:O75031}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23707421}. SUBUNIT: Interacts (via C-terminus) with BNC1 (PubMed:23707421). Associates with HSF2. The interaction seems to occur between the trimerization domain of HSF2 and the N-terminal hydrophilic region of HSF2BP (By similarity). {ECO:0000250|UniProtKB:O75031, ECO:0000269|PubMed:23707421}. TISSUE SPECIFICITY: Expressed in testis and, to a lesser extent, in lung and muscle. {ECO:0000269|PubMed:23707421}. +Q9CQQ8 LSM7_MOUSE U6 snRNA-associated Sm-like protein LSm7 103 11,636 Chain (1); Initiator methionine (1); Modified residue (1) FUNCTION: Plays role in pre-mRNA splicing as component of the U4/U6-U5 tri-snRNP complex that is involved in spliceosome assembly, and as component of the precatalytic spliceosome (spliceosome B complex). The heptameric LSM2-8 complex binds specifically to the 3'-terminal U-tract of U6 snRNA. {ECO:0000250|UniProtKB:Q9UK45}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UK45}. SUBUNIT: Component of the precatalytic spliceosome (spliceosome B complex). Component of the U4/U6-U5 tri-snRNP complex, a building block of the precatalytic spliceosome (spliceosome B complex). The U4/U6-U5 tri-snRNP complex is composed of the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39, plus LSM2, LSM3, LSM4, LSM5, LSM6, LSM7 and LSM8. LSM2, LSM3, LSM4, LSM5, LSM6, LSM7 and LSM8 form a heptameric, ring-shaped subcomplex (the LSM2-8 complex) that is part of the U4/U6-U5 tri-snRNP complex and the precatalytic spliceosome. Interacts with TACC1. {ECO:0000250|UniProtKB:Q9UK45}. +P01741 HVM00_MOUSE Ig heavy chain V region (Anti-arsonate antibody) 114 12,555 Chain (1); Domain (1); Non-terminal residue (1) +P18532 HVM61_MOUSE Ig heavy chain V region 1B43 116 13,158 Beta strand (9); Chain (1); Disulfide bond (1); Helix (1); Non-terminal residue (1); Region (5); Signal peptide (1); Turn (3) +P84751 HVM63_MOUSE Ig heavy chain Mem5 (Fragment) 237 25,350 Beta strand (19); Chain (1); Disulfide bond (6); Domain (2); Helix (8); Non-terminal residue (1); Region (2); Turn (4) FUNCTION: Anti-influenza H3N2 neuraminidase antibody. {ECO:0000269|PubMed:12414967}. SUBCELLULAR LOCATION: Secreted. +Q6P9N1 HYCCI_MOUSE Hyccin (Down-regulated by CTNNB1 protein A) (Protein FAM126A) 521 57,321 Alternative sequence (4); Chain (1); Modified residue (7); Sequence conflict (1) FUNCTION: Component of a complex required to localize phosphatidylinositol 4-kinase (PI4K) to the plasma membrane. The complex acts as a regulator of phosphatidylinositol 4-phosphate (PtdIns(4)P) synthesis. FAM126A plays a key role in oligodendrocytes formation, a cell type with expanded plasma membrane that requires generation of PtdIns(4)P. Its role in oligodendrocytes formation probably explains its importance in myelination of the central and peripheral nervous system. May also have a role in the beta-catenin/Lef signaling pathway. {ECO:0000250|UniProtKB:Q9BYI3}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9BYI3}. Cell membrane {ECO:0000250|UniProtKB:Q9BYI3}. Note=Localizes to the cytosol and is recruited to the plasma membrane following interaction with other components of the phosphatidylinositol 4-kinase (PI4K) complex. {ECO:0000250|UniProtKB:Q9BYI3}. SUBUNIT: Component of a phosphatidylinositol 4-kinase (PI4K) complex, composed of PI4KA, EFR3 (EFR3A or EFR3B), TTC7 (TTC7A or TTC7B) and FAM126 (FAM126A or FAM126B). Interacts with TTC7 (TTC7A or TTC7B), interaction is direct. {ECO:0000250|UniProtKB:Q9BYI3}. TISSUE SPECIFICITY: Predominantly expressed in the central nervous system, where it is found in neurons but not in myelinating cells. Lower abundance is observed in peripheral neurons, where it is detectable only at early postnatal ages (PubMed:22461884). Expressed in both oligodendrocytes and neurons (PubMed:26571211). {ECO:0000269|PubMed:22461884, ECO:0000269|PubMed:26571211}. +Q3TRM8 HXK3_MOUSE Hexokinase-3 (EC 2.7.1.1) (Hexokinase type III) (HK III) 922 100,101 Chain (1); Domain (2); Nucleotide binding (2); Region (8); Sequence conflict (6) Carbohydrate metabolism; hexose metabolism. SUBUNIT: Monomer. {ECO:0000250}. DOMAIN: The N- and C-terminal halves of this hexokinase show extensive sequence similarity to each other. The catalytic activity is associated with the C-terminus while regulatory function is associated with the N-terminus. +P01808 HVM38_MOUSE Ig heavy chain V region T601 119 13,169 Beta strand (11); Chain (1); Domain (1); Helix (4); Non-terminal residue (1); Turn (2) +P11835 ITB2_MOUSE Integrin beta-2 (Cell surface adhesion glycoproteins LFA-1/CR3/p150,95 subunit beta) (Complement receptor C3 subunit beta) (CD antigen CD18) 771 85,026 Chain (1); Disulfide bond (28); Domain (1); Glycosylation (6); Metal binding (4); Modified residue (5); Region (1); Repeat (4); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 703 725 Helical. {ECO:0000255}. TOPO_DOM 24 702 Extracellular. {ECO:0000255}.; TOPO_DOM 726 771 Cytoplasmic. {ECO:0000255}. FUNCTION: Integrin ITGAL/ITGB2 is a receptor for ICAM1, ICAM2, ICAM3 and ICAM4. Integrins ITGAM/ITGB2 and ITGAX/ITGB2 are receptors for the iC3b fragment of the third complement component and for fibrinogen. Integrin ITGAX/ITGB2 recognizes the sequence G-P-R in fibrinogen alpha-chain. Integrin ITGAM/ITGB2 recognizes P1 and P2 peptides of fibrinogen gamma chain. Integrin ITGAM/ITGB2 is also a receptor for factor X. Integrin ITGAD/ITGB2 is a receptor for ICAM3 and VCAM1. Contributes to natural killer cell cytotoxicity (By similarity). Involved in leukocyte adhesion and transmigration of leukocytes including T-cells and neutrophils (By similarity). Triggers neutrophil transmigration during lung injury through PTK2B/PYK2-mediated activation (PubMed:18587400). Integrin ITGAL/ITGB2 in association with ICAM3, contributes to apoptotic neutrophil phagocytosis by macrophages (By similarity). In association with alpha subunit ITGAM/CD11b, required for CD177-PRTN3-mediated activation of TNF primed neutrophils (By similarity). Alpha-M/beta-2 play a critical role in mast cell development and in immune complex-mediated glomerulonephritis. Mice expressing a null mutation of the alpha-M subunit gene demonstrate increase in neutrophil accumulation, in response to a impaired degranulation and phagocytosis, events that apparently accelerate apoptosis in neutrophils. These mice develop obesity. {ECO:0000250|UniProtKB:P05107, ECO:0000269|PubMed:18587400, ECO:0000269|PubMed:19903482}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P05107}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P05107}. Membrane raft {ECO:0000250|UniProtKB:P05107}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P05107}. SUBUNIT: Heterodimer of an alpha and a beta subunit. ITGB2 associates with either ITGAL, ITGAM, ITGAX or ITGAD. Found in a complex with CD177 and ITGAM/CD11b (By similarity). Interacts with FGR (PubMed:19903482). Interacts with COPS5 and RANBP9 (By similarity). Interacts with FLNA (via filamin repeats 4, 9, 12, 17, 19, 21, and 23) (By similarity). {ECO:0000250|UniProtKB:P05107, ECO:0000269|PubMed:19903482}. +Q9CX00 IST1_MOUSE IST1 homolog 362 39,468 Chain (1); Modified residue (2); Sequence conflict (1) FUNCTION: ESCRT-III-like protein involved in specific functions of the ESCRT machinery. Is required for efficient abscission during cytokinesis, but not for HIV-1 budding. The involvement in the MVB pathway is not established. Involved in recruiting VPS4A and/or VPS4B to the midbody of dividing cells. During late anaphase, involved in nuclear envelope reassembly and mitotic spindle disassembly together with the ESCRT-III complex: IST1 acts by mediating the recruitment of SPAST to the nuclear membrane, leading to microtubule severing. Regulates early endosomal tubulation together with the ESCRT-III complex by mediating the recruitment of SPAST. {ECO:0000250|UniProtKB:P53990}. SUBCELLULAR LOCATION: Cytoplasmic vesicle {ECO:0000250|UniProtKB:P53990}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P53990}. Midbody {ECO:0000250|UniProtKB:P53990}. Nucleus envelope {ECO:0000250|UniProtKB:P53990}. Note=Localizes to centrosome and midbody of dividing cells. Colocalized with SPART to the ends of Flemming bodies during cytokinesis. Localizes to the nuclear envelope during late anaphase. {ECO:0000250|UniProtKB:P53990}. SUBUNIT: Interacts with CHMP1A, CHMP1B, VPS4A and VTA1. Interacts with SPAST, STAMBP, and USP8. May interact with VPS37B. May associate with the ESCRT-I complex. Interacts with MITD1, in competition with VSP4. Interacts with SPART (via MIT domain); leading to the recruitment of SPART to midbodies. Interacts with SPAST. {ECO:0000250|UniProtKB:P53990}. +Q3V3R4 ITA1_MOUSE Integrin alpha-1 (CD49 antigen-like family member A) (Laminin and collagen receptor) (VLA-1) (CD antigen CD49a) 1179 130,810 Calcium binding (3); Chain (1); Disulfide bond (7); Domain (1); Glycosylation (23); Motif (1); Repeat (7); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1142 1164 Helical. {ECO:0000255}. TOPO_DOM 29 1141 Extracellular. {ECO:0000255}.; TOPO_DOM 1165 1179 Cytoplasmic. {ECO:0000255}. FUNCTION: Integrin alpha-1/beta-1 is a receptor for laminin and collagen. It recognizes the proline-hydroxylated sequence G-F-P-G-E-R in collagen. Involved in anchorage-dependent, negative regulation of EGF-stimulated cell growth. {ECO:0000269|PubMed:15592458}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Heterodimer of an alpha and a beta subunit. Alpha-1 associates with beta-1 (By similarity). Interacts with RAB21 (By similarity). Interacts (via cytoplasmic domain) with PTPN2; activates PTPN2 phosphatase activity towards EGFR and negatively regulates EGF signaling (By similarity). {ECO:0000250}. DOMAIN: The integrin I-domain (insert) is a VWFA domain. Integrins with I-domains do not undergo protease cleavage. +Q6ZPI0 JADE1_MOUSE Protein Jade-1 (Jade family PHD finger protein 1) (PHD finger protein 17) 834 93,897 Alternative sequence (2); Chain (1); Cross-link (2); Erroneous initiation (2); Modified residue (6); Sequence conflict (1); Zinc finger (3) FUNCTION: Component of the HBO1 complex which has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3 and is responsible for the bulk of histone H4 acetylation in vivo. Transcriptional coactivator, it may also promote acetylation of nucleosomal histone H4 by KAT5. Promotes apoptosis. May act as a renal tumor suppressor. Negatively regulates canonical Wnt signaling; at least in part, cooperates with NPHP4 in this function (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14612400}. Nucleus {ECO:0000269|PubMed:14612400}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q6IE81}. Note=Localizes to the ciliary transition zone. {ECO:0000250|UniProtKB:Q6IE81}. SUBUNIT: Component of the HBO1 complex composed at least of ING4 or ING5, MYST2/HBO1, MEAF6, and one of JADE1, JADE2 and JADE3. Isoform 2 interacts with VHL and KAT5. Interacts with NPHP4 (By similarity). {ECO:0000250|UniProtKB:Q6IE81}. DOMAIN: The 2 PHD-type zinc fingers are required for transcriptional activity. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in kidney. Also present in liver (at protein level). {ECO:0000269|PubMed:12169691}. +Q91WI7 ITFG2_MOUSE KICSTOR complex protein ITFG2 (Integrin-alpha FG-GAP repeat-containing protein 2) 443 48,971 Alternative sequence (1); Chain (1); Modified residue (2); Repeat (2); Sequence conflict (1) FUNCTION: As part of the KICSTOR complex functions in the amino acid-sensing branch of the TORC1 signaling pathway. Recruits, in an amino acid-independent manner, the GATOR1 complex to the lysosomal membranes and allows its interaction with GATOR2 and the RAG GTPases. Functions upstream of the RAG GTPases and is required to negatively regulate mTORC1 signaling in absence of amino acids. In absence of the KICSTOR complex mTORC1 is constitutively localized to the lysosome and activated. The KICSTOR complex is also probably involved in the regulation of mTORC1 by glucose. {ECO:0000250|UniProtKB:Q969R8}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q969R8}. Note=Localization to lysosomes is amino acid-independent. {ECO:0000250|UniProtKB:Q969R8}. SUBUNIT: Part of the KICSTOR complex composed of KPTN, ITFG2, C12orf66 and SZT2. SZT2 probably serves as a link between the other three proteins in the KICSTOR complex and may mediate the direct interaction with the GATOR complex via GATOR1. The KICSTOR complex interacts directly with the GATOR1 complex and most probably indirectly with the GATOR2 complexe in an amino acid-independent manner. {ECO:0000250|UniProtKB:Q969R8}. +E9Q793 JHY_MOUSE Jhy protein (Juvenile hydrocephalus protein) 770 87,417 Chain (1) FUNCTION: Required for the normal development of cilia in brain ependymal cells lining the ventricular surfaces. {ECO:0000269|PubMed:23906841}. TISSUE SPECIFICITY: Expressed in the brain, specifically in hypothalamus, pineal gland, and ependymal cells of the aqueduct of Sylvius, as well as in the choroid plexus of the third ventricle. Expressed in the ependymal cells lining the lateral ventricles (at protein level). {ECO:0000269|PubMed:23906841}. +P97875 JDP2_MOUSE Jun dimerization protein 2 163 18,675 Chain (1); Cross-link (1); Domain (1); Modified residue (1); Mutagenesis (1); Region (2) FUNCTION: Component of the AP-1 transcription factor that represses transactivation mediated by the Jun family of proteins. Involved in a variety of transcriptional responses associated with AP-1, such as UV-induced apoptosis, cell differentiation, tumorigenesis and antitumogeneris. Can also function as a repressor by recruiting histone deacetylase 3/HDAC3 to the promoter region of JUN. May control transcription via direct regulation of the modification of histones and the assembly of chromatin (By similarity). {ECO:0000250, ECO:0000269|PubMed:12707301, ECO:0000269|PubMed:14627710}. PTM: Phosphorylation of Thr-148 by MAPK8 in response to different stress conditions such as, UV irradiation, oxidatives stress and anisomycin treatments. {ECO:0000269|PubMed:11602244, ECO:0000269|PubMed:18307971}.; PTM: Polyubiquitinated; probably by IRF2BP1. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Forms a homodimer or heterodimer with JUN, JUNB, JUND, CEBPG and ATF2 thereby inhibiting transactivation by JUN, ATF2 and CEBPG (By similarity). Binds multiple DNA elements such as cAMP-response element (CRE) and TPA response element (TRE) either as homodimer or heterodimer. Interacts with IRF2BP1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed in all adult tissues tested as well in embryos. {ECO:0000269|PubMed:11231009}. +Q8K177 KCP3_MOUSE Keratinocyte-associated protein 3 (KCP-3) 240 25,687 Alternative sequence (1); Chain (1); Erroneous initiation (4); Sequence conflict (1); Transmembrane (4) TRANSMEM 21 41 Helical. {ECO:0000255}.; TRANSMEM 63 83 Helical. {ECO:0000255}.; TRANSMEM 95 115 Helical. {ECO:0000255}.; TRANSMEM 163 183 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. +O88335 KCNJ1_MOUSE ATP-sensitive inward rectifier potassium channel 1 (ATP-regulated potassium channel ROM-K) (Inward rectifier K(+) channel Kir1.1) (Potassium channel, inwardly rectifying subfamily J member 1) 372 42,776 Chain (1); Glycosylation (1); Intramembrane (2); Modified residue (1); Motif (1); Nucleotide binding (1); Site (1); Topological domain (4); Transmembrane (2) INTRAMEM 109 120 Helical; Pore-forming; Name=H5. {ECO:0000250}.; INTRAMEM 121 127 Pore-forming. {ECO:0000250}. TRANSMEM 59 83 Helical; Name=M1. {ECO:0000250}.; TRANSMEM 137 158 Helical; Name=M2. {ECO:0000250}. TOPO_DOM 1 58 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 84 108 Extracellular. {ECO:0000250}.; TOPO_DOM 128 136 Extracellular. {ECO:0000250}.; TOPO_DOM 159 372 Cytoplasmic. {ECO:0000250}. FUNCTION: In the kidney, probably plays a major role in potassium homeostasis. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. This channel is activated by internal ATP and can be blocked by external barium (By similarity). {ECO:0000250}. PTM: Phosphorylation at Ser-25 by SGK1 is necessary for its expression at the cell membrane. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Note=Phosphorylation at Ser-44 by SGK1 is necessary for its expression at the cell membrane. {ECO:0000250}. SUBUNIT: Interacts with SGK1 and SLC9A3R2/NHERF2. {ECO:0000250}. +O35173 KCNS1_MOUSE Potassium voltage-gated channel subfamily S member 1 (Delayed-rectifier K(+) channel alpha subunit 1) (Voltage-gated potassium channel subunit Kv9.1) 497 54,918 Chain (1); Compositional bias (1); Intramembrane (2); Motif (1); Sequence conflict (1); Topological domain (8); Transmembrane (6) INTRAMEM 380 391 Helical; Name=Pore helix. {ECO:0000250|UniProtKB:P63142}.; INTRAMEM 392 399 {ECO:0000250|UniProtKB:P63142}. TRANSMEM 187 208 Helical; Name=Segment S1. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 240 262 Helical; Name=Segment S2. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 274 291 Helical; Name=Segment S3. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 310 330 Helical; Voltage-sensor; Name=Segment S4. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 346 367 Helical; Name=Segment S5. {ECO:0000250|UniProtKB:P63142}.; TRANSMEM 407 435 Helical; Name=Segment S6. {ECO:0000250|UniProtKB:P63142}. TOPO_DOM 1 186 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 209 239 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 263 273 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 292 309 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 331 345 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 368 379 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 400 406 Extracellular. {ECO:0000250|UniProtKB:P63142}.; TOPO_DOM 436 497 Cytoplasmic. {ECO:0000250|UniProtKB:P63142}. FUNCTION: Potassium channel subunit that does not form functional channels by itself. Can form functional heterotetrameric channels with KCNB1 and KCNB2; modulates the delayed rectifier voltage-gated potassium channel activation and deactivation rates of KCNB1 and KCNB2 (PubMed:9305895). {ECO:0000269|PubMed:9305895}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9305895}; Multi-pass membrane protein {ECO:0000305}. Note=May not reach the plasma membrane but remain in an intracellular compartment in the absence of KCNB1 or KCNB2 (PubMed:9305895). {ECO:0000269|PubMed:9305895}. SUBUNIT: Heterotetramer with KCNB1 and KCNB2 (PubMed:9305895). Does not form homomultimers (PubMed:9305895). {ECO:0000269|PubMed:9305895}. DOMAIN: The transmembrane segment S4 functions as voltage-sensor and is characterized by a series of positively charged amino acids at every third position. Channel opening and closing is effected by a conformation change that affects the position and orientation of the voltage-sensor paddle formed by S3 and S4 within the membrane. A transmembrane electric field that is positive inside would push the positively charged S4 segment outwards, thereby opening the pore, while a field that is negative inside would pull the S4 segment inwards and close the pore. Changes in the position and orientation of S4 are then transmitted to the activation gate formed by the inner helix bundle via the S4-S5 linker region. {ECO:0000250|UniProtKB:P63142}. TISSUE SPECIFICITY: Detected in brain, but not in the other tissues tested. The highest levels of expression are in olfactory bulb, cerebral cortex, hippocampus, habenula, basolateral amygdaloid nuclei and cerebellum (PubMed:9305895). {ECO:0000269|PubMed:9305895}. +Q8BZN2 KCNV1_MOUSE Potassium voltage-gated channel subfamily V member 1 (Voltage-gated potassium channel subunit Kv8.1) 503 56,669 Chain (1); Motif (1); Sequence conflict (6); Topological domain (6); Transmembrane (6) TRANSMEM 214 234 Helical; Name=Segment S1. {ECO:0000255}.; TRANSMEM 242 262 Helical; Name=Segment S2. {ECO:0000255}.; TRANSMEM 280 300 Helical; Name=Segment S3. {ECO:0000255}.; TRANSMEM 313 334 Helical; Voltage-sensor; Name=Segment S4. {ECO:0000255}.; TRANSMEM 349 369 Helical; Name=Segment S5. {ECO:0000255}.; TRANSMEM 410 430 Helical; Name=Segment S6. {ECO:0000255}. TOPO_DOM 3 213 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 235 241 Extracellular. {ECO:0000255}.; TOPO_DOM 263 279 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 301 312 Extracellular. {ECO:0000255}.; TOPO_DOM 335 348 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 431 503 Cytoplasmic. {ECO:0000255}. FUNCTION: Potassium channel subunit that does not form functional channels by itself. Modulates KCNB1 and KCNB2 channel activity by shifting the threshold for inactivation to more negative values and by slowing the rate of inactivation. Can down-regulate the channel activity of KCNB1, KCNB2, KCNC4 and KCND1, possibly by trapping them in intracellular membranes (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Has to be associated with another potassium channel subunit to get inserted in the plasma membrane. Remains intracellular in the absence of KCNB2 (By similarity). {ECO:0000250}. SUBUNIT: Heteromultimer with KCNB1 and KCNB2. Interacts with KCNC4 and KCND1 (By similarity). {ECO:0000250}. DOMAIN: The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position. {ECO:0000250}. +Q8CFS6 KCNV2_MOUSE Potassium voltage-gated channel subfamily V member 2 (Voltage-gated potassium channel subunit Kv8.2) 562 64,461 Chain (1); Glycosylation (1); Intramembrane (1); Motif (1); Topological domain (8); Transmembrane (6) INTRAMEM 462 482 Pore-forming; Name=Segment H5. {ECO:0000255}. TRANSMEM 164 184 Helical; Name=Segment S1. {ECO:0000255}.; TRANSMEM 270 290 Helical; Name=Segment S2. {ECO:0000255}.; TRANSMEM 345 365 Helical; Name=Segment S3. {ECO:0000255}.; TRANSMEM 392 412 Helical; Voltage-sensor; Name=Segment S4. {ECO:0000255}.; TRANSMEM 428 448 Helical; Name=Segment S5. {ECO:0000255}.; TRANSMEM 489 509 Helical; Name=Segment S6. {ECO:0000255}. TOPO_DOM 1 163 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 185 269 Extracellular. {ECO:0000255}.; TOPO_DOM 291 344 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 366 391 Extracellular. {ECO:0000255}.; TOPO_DOM 413 427 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 449 461 Extracellular. {ECO:0000255}.; TOPO_DOM 483 488 Extracellular. {ECO:0000255}.; TOPO_DOM 510 562 Cytoplasmic. {ECO:0000255}. FUNCTION: Potassium channel subunit. Modulates channel activity by shifting the threshold and the half-maximal activation to more negative values (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Heteromultimer with KCNB1, KCNC1 and KCNF1. Does not form homomultimers (By similarity). {ECO:0000250}. DOMAIN: The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position. {ECO:0000250}. +Q60603 KCNH1_MOUSE Potassium voltage-gated channel subfamily H member 1 (Ether-a-go-go potassium channel 1) (EAG channel 1) (EAG1) (m-eag) (Voltage-gated potassium channel subunit Kv10.1) 989 111,282 Beta strand (15); Chain (1); Domain (2); Glycosylation (2); Helix (13); Intramembrane (1); Modified residue (3); Motif (1); Mutagenesis (14); Region (4); Sequence conflict (2); Topological domain (8); Transmembrane (6); Turn (2) INTRAMEM 449 470 Pore-forming; Name=Segment H5. {ECO:0000250|UniProtKB:Q63472}. TRANSMEM 221 241 Helical; Name=Segment S1. {ECO:0000250|UniProtKB:Q63472}.; TRANSMEM 249 269 Helical; Name=Segment S2. {ECO:0000250|UniProtKB:Q63472}.; TRANSMEM 291 309 Helical; Name=Segment S3. {ECO:0000250|UniProtKB:Q63472}.; TRANSMEM 346 368 Helical; Voltage-sensor; Name=Segment S4. {ECO:0000250|UniProtKB:Q63472}.; TRANSMEM 378 399 Helical; Name=Segment S5. {ECO:0000250|UniProtKB:Q63472}.; TRANSMEM 478 498 Helical; Name=Segment S6. {ECO:0000250|UniProtKB:Q63472}. TOPO_DOM 1 220 Cytoplasmic. {ECO:0000250|UniProtKB:Q63472}.; TOPO_DOM 242 248 Extracellular. {ECO:0000250|UniProtKB:Q63472}.; TOPO_DOM 270 290 Cytoplasmic. {ECO:0000250|UniProtKB:Q63472}.; TOPO_DOM 310 345 Extracellular. {ECO:0000250|UniProtKB:Q63472}.; TOPO_DOM 369 377 Cytoplasmic. {ECO:0000250|UniProtKB:Q63472}.; TOPO_DOM 400 448 Extracellular. {ECO:0000250|UniProtKB:Q63472}.; TOPO_DOM 471 477 Extracellular. {ECO:0000250|UniProtKB:Q63472}.; TOPO_DOM 499 989 Cytoplasmic. {ECO:0000250|UniProtKB:Q63472}. FUNCTION: Pore-forming (alpha) subunit of a voltage-gated delayed rectifier potassium channel (PubMed:19671703, PubMed:23975098). Channel properties are modulated by subunit assembly. Mediates IK(NI) current in myoblasts. Involved in the regulation of cell proliferation and differentiation, in particular adipogenic and osteogenic differentiation in bone marrow-derived mesenchymal stem cells (MSCs) (By similarity). {ECO:0000250|UniProtKB:O95259, ECO:0000269|PubMed:19671703, ECO:0000269|PubMed:23975098}. PTM: Channel activity is regulated via tyrosine phosphorylation/dephosphorylation by SRC and PTPN6. {ECO:0000250|UniProtKB:O95259}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19671703, ECO:0000269|PubMed:23975098}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O95259}. Nucleus inner membrane {ECO:0000250|UniProtKB:O95259}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O95259}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q63472}. Cell projection, axon {ECO:0000250|UniProtKB:Q63472}. Cell junction, synapse, presynaptic cell membrane {ECO:0000269|PubMed:25556795}. Perikaryon {ECO:0000250|UniProtKB:Q63472}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250|UniProtKB:Q63472}. Early endosome membrane {ECO:0000250|UniProtKB:O95259}. Note=Perinuclear KCNH1 is located to NPC-free islands. {ECO:0000250|UniProtKB:O95259}. SUBUNIT: The potassium channel is composed of a homo- or heterotetrameric complex of pore-forming alpha subunits that can associate with modulating beta subunits. Heteromultimer with KCNH5/EAG2 (By similarity). Interacts with ALG10B (By similarity). Interacts with RABEP1 (PubMed:22841712). Interacts (via C-terminus) with CTTN. Interacts (via C-terminal cytoplasmic region) with Ca(2+)-bound calmodulin (PubMed:27618660). {ECO:0000250|UniProtKB:O95259, ECO:0000269|PubMed:22841712, ECO:0000269|PubMed:27618660}. DOMAIN: The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position. {ECO:0000250|UniProtKB:Q63472}.; DOMAIN: The C-terminal region interacts with the cyclic nucleotide-binding domain and contributes to regulate channel gating. {ECO:0000269|PubMed:23975098, ECO:0000305|PubMed:22732247}.; DOMAIN: The PAS and PAC domain interact with the cyclic nucleotide-binding domain and contribute to the regulation of channel gating (PubMed:23975098). Calmodulin binding clamps together the PAS and PAC domain with the cyclic nucleotide-binding domain from a neighboring subunit and causes a conformation change that leads to channel closure. {ECO:0000250|UniProtKB:Q63472, ECO:0000269|PubMed:23975098}.; DOMAIN: The cyclic nucleotide-binding domain lacks residues that are essential for nucleotide-binding and cannot bind cyclic nucleotides (PubMed:19671703). Instead, residues from the C-terminal domain (the so-called intrinsic ligand) bind in the cavity that would be expected to bind cyclic nucleotides. Interaction with the C-terminal region hinders interaction with CALM and reduces the affinity for CALM. {ECO:0000269|PubMed:19671703, ECO:0000269|PubMed:22732247, ECO:0000269|PubMed:23975098}. TISSUE SPECIFICITY: Detected in brain (at protein level) (PubMed:23424202, PubMed:25556795). Highly expressed in olfactory bulb. Detected in brain cortex, hippocampus, brain stem, striatum, thalamus, hypothalamus and spinal cord (PubMed:23424202). {ECO:0000269|PubMed:23424202, ECO:0000269|PubMed:25556795}. +O08581 KCNK1_MOUSE Potassium channel subfamily K member 1 (Inward rectifying potassium channel protein TWIK-1) 336 38,201 Chain (1); Cross-link (1); Disulfide bond (1); Glycosylation (1); Intramembrane (4); Modified residue (1); Mutagenesis (3); Region (3); Sequence conflict (3); Site (3); Topological domain (7); Transmembrane (4) INTRAMEM 104 116 Helical; Name=Pore helix 1. {ECO:0000250|UniProtKB:O00180}.; INTRAMEM 117 122 {ECO:0000250|UniProtKB:O00180}.; INTRAMEM 212 224 Helical; Name=Pore helix 2. {ECO:0000250|UniProtKB:O00180}.; INTRAMEM 225 231 {ECO:0000250|UniProtKB:O00180}. TRANSMEM 21 41 Helical. {ECO:0000250|UniProtKB:O00180}.; TRANSMEM 133 156 Helical. {ECO:0000250|UniProtKB:O00180}.; TRANSMEM 182 202 Helical. {ECO:0000250|UniProtKB:O00180}.; TRANSMEM 244 267 Helical. {ECO:0000250|UniProtKB:O00180}. TOPO_DOM 1 20 Cytoplasmic. {ECO:0000250|UniProtKB:O00180}.; TOPO_DOM 42 103 Extracellular. {ECO:0000250|UniProtKB:O00180}.; TOPO_DOM 123 132 Extracellular. {ECO:0000250|UniProtKB:O00180}.; TOPO_DOM 157 181 Cytoplasmic. {ECO:0000250|UniProtKB:O00180}.; TOPO_DOM 203 211 Extracellular. {ECO:0000250|UniProtKB:O00180}.; TOPO_DOM 232 243 Extracellular. {ECO:0000250|UniProtKB:O00180}.; TOPO_DOM 268 336 Cytoplasmic. {ECO:0000250|UniProtKB:O00180}. FUNCTION: Ion channel that contributes to passive transmembrane potassium transport and to the regulation of the resting membrane potential in brain astrocytes, but also in kidney and in other tissues (PubMed:16847696, PubMed:22431633, PubMed:24368895). Forms dimeric channels through which potassium ions pass in accordance with their electrochemical gradient. The channel is selective for K(+) ions at physiological potassium concentrations and at neutral pH, but becomes permeable to Na(+) at subphysiological K(+) levels and upon acidification of the extracellular medium. The homodimer has very low potassium channel activity, when expressed in heterologous systems, and can function as weakly inward rectifying potassium channel (PubMed:9013852, PubMed:24496152). Channel activity is modulated by activation of serotonin receptors (PubMed:24368895). Heterodimeric channels containing KCNK1 and KCNK2 have much higher activity, and may represent the predominant form in astrocytes (PubMed:24496152). Heterodimeric channels containing KCNK1 and KCNK3 or KCNK9 have much higher activity. Heterodimeric channels formed by KCNK1 and KCNK9 may contribute to halothane-sensitive currents (By similarity). Mediates outward rectifying potassium currents in dentate gyrus granule cells and contributes to the regulation of their resting membrane potential (PubMed:25406588). Contributes to the regulation of action potential firing in dentate gyrus granule cells and down-regulates their intrinsic excitability (PubMed:25406588). In astrocytes, the heterodimer formed by KCNK1 and KCNK2 is required for rapid glutamate release in response to activation of G-protein coupled receptors, such as F2R and CNR1 (PubMed:24496152). Required for normal ion and water transport in the kidney (PubMed:16025300). Contributes to the regulation of the resting membrane potential of pancreatic beta cells (PubMed:22431633). The low channel activity of homodimeric KCNK1 may be due to sumoylation. The low channel activity may be due to rapid internalization from the cell membrane and retention in recycling endosomes (PubMed:15540117). {ECO:0000250|UniProtKB:O00180, ECO:0000250|UniProtKB:Q9Z2T2, ECO:0000269|PubMed:15540117, ECO:0000269|PubMed:16025300, ECO:0000269|PubMed:16847696, ECO:0000269|PubMed:22431633, ECO:0000269|PubMed:24368895, ECO:0000269|PubMed:24496152, ECO:0000269|PubMed:9013852}. PTM: Sumoylation is controversial. Sumoylated by UBE2I. Not sumoylated when expressed in xenopus oocytes or mammalian cells. Sumoylation inactivates the channel, but does not interfere with expression at the cell membrane. Sumoylation of a single subunit is sufficient to silence the dimeric channel. Sumoylation of KCNK1 is sufficient to silence heterodimeric channels formed by KCNK1 and KCNK3 or KCNK9. Desumoylated by SENP1; this activates the channel. Desumoylated by SENP1; this strongly increases halothane-mediated activation of heterodimeric channels formed with KCNK9. SENP1 treatment has no effect. {ECO:0000250|UniProtKB:O00180}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15540117, ECO:0000269|PubMed:19959478, ECO:0000269|PubMed:24368895, ECO:0000269|PubMed:24496152, ECO:0000269|PubMed:9013852}; Multi-pass membrane protein {ECO:0000305}. Recycling endosome {ECO:0000269|PubMed:15540117}. Apical cell membrane {ECO:0000269|PubMed:12855359, ECO:0000305|PubMed:16025300}. Cytoplasmic vesicle {ECO:0000269|PubMed:16025300, ECO:0000269|PubMed:24368895}. Perikaryon {ECO:0000269|PubMed:12855359, ECO:0000269|PubMed:17079103, ECO:0000269|PubMed:25406588}. Cell projection, dendrite {ECO:0000269|PubMed:25406588}. Cell projection {ECO:0000269|PubMed:17079103}. Cell junction, synapse {ECO:0000250|UniProtKB:Q9Z2T2}. Note=The heterodimer with KCNK2 is detected at the astrocyte cell membrane (PubMed:24496152). Not detected at the astrocyte cell membrane when KCNK2 is absent (PubMed:24496152). Detected on neuronal cell bodies, and to a lesser degree on neuronal cell projections (PubMed:12855359, PubMed:17079103). Detected on hippocampus dentate gyrus granule cell bodies and to a lesser degree on proximal dendrites (PubMed:25406588). Detected in synaptic membranes. Detected at the apical cell membrane in stria vascularis in the cochlea (By similarity). Detected at the apical cell membrane of vestibular dark cells situated between the crista and the utricle in the inner ear (PubMed:12855359). Detected at the apical cell membrane in stria vascularis in the cochlea (PubMed:12855359). Detected at the apical cell membrane in kidney proximal tubule segment S1 and in subapical compartments in segments S1, S2 and S3 (PubMed:16025300). Predominantly in cytoplasmic structures in kidney distal convoluted tubules and collecting ducts (PubMed:16025300). Predominantly in cytoplasmic structures in hippocampus astrocytes; only a minor proportion of the protein is present at the cell membrane (PubMed:24368895). {ECO:0000250|UniProtKB:Q9Z2T2, ECO:0000269|PubMed:16025300, ECO:0000269|PubMed:17079103, ECO:0000269|PubMed:24368895, ECO:0000269|PubMed:24496152, ECO:0000269|PubMed:25406588}. SUBUNIT: Homodimer; disulfide-linked (PubMed:9013852). Heterodimer with KCNK2; disulfide-linked (PubMed:24496152). In astrocytes, forms mostly heterodimeric potassium channels with KCNK2, with only a minor proportion of functional channels containing homodimeric KCNK1 (By similarity). Interacts with KCNK3 and KCNK9, forming functional heterodimeric channels (By similarity). Interacts with GNG4 (PubMed:24496152). Identified in a complex with PSD and ARF6; interacts only with PSD that is bound to ARF6 (PubMed:15540117). Interacts with UBE2I (By similarity). {ECO:0000250|UniProtKB:O00180, ECO:0000269|PubMed:15540117, ECO:0000269|PubMed:24496152, ECO:0000269|PubMed:9013852}. TISSUE SPECIFICITY: Detected in spiral ganglion neurons (PubMed:17079103). Detected in hippocampus CA1 and CA1 regions and in the molecular layer of the dentate gyrus (PubMed:24368895, PubMed:25406588). Detected on hippocampus astrocytes (PubMed:24368895, PubMed:24496152). Highly expressed in the stria vascularis in the cochlea (PubMed:12855359). Detected in pancreas islet beta cells (PubMed:22431633). Detected in kidney, at brush border membranes in proximal tubules and in cytoplasmic structures in distal convoluted tubules, thick ascending limbs and collecting ducts (at protein level) (PubMed:15540117, PubMed:16025300). Widely expressed. Detected in spiral ganglion cells (PubMed:17079103). Highest expression in brain, kidney, thyroid, salivary gland, adrenal gland, prostate, epididymis, uterus, placenta, colon and jejunum. Moderate expression in eyes, pituitary, pancreas, smooth muscle, testis and ovary. Very low levels in lung, aorta, liver, heart, skeletal muscle, thymus and spleen. In the brain, highest expression in cerebellar granule cells, brainstem, hippocampus and cerebral cortex (PubMed:18222039). {ECO:0000269|PubMed:15540117, ECO:0000269|PubMed:16025300, ECO:0000269|PubMed:18222039, ECO:0000269|PubMed:22431633, ECO:0000269|PubMed:24368895, ECO:0000269|PubMed:25406588, ECO:0000269|PubMed:9013852, ECO:0000269|PubMed:9559671}. +Q8BRH4 KMT2C_MOUSE Histone-lysine N-methyltransferase 2C (Lysine N-methyltransferase 2C) (EC 2.1.1.43) (Myeloid/lymphoid or mixed-lineage leukemia protein 3 homolog) 4903 540,187 Alternative sequence (5); Binding site (1); Chain (1); Coiled coil (6); Compositional bias (7); DNA binding (1); Domain (5); Erroneous initiation (1); Metal binding (4); Modified residue (23); Region (1); Sequence conflict (21); Zinc finger (11) FUNCTION: Histone methyltransferase. Methylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Central component of the MLL2/3 complex, a coactivator complex of nuclear receptors, involved in transcriptional coactivation. KMT2C/MLL3 may be a catalytic subunit of this complex (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Component of the MLL2/3 complex (also named ASCOM complex), at least composed of KMT2D/MLL2 or KMT2C/MLL3, ASH2L, RBBP5, WDR5, NCOA6, DPY30, KDM6A, PAXIP1/PTIP, PAGR1 and alpha- and beta-tubulin. Interacts with histone H3. {ECO:0000250}. DOMAIN: The SET domain interacts with histone H3 but not H2A, H2B and H4, and may have a H3 lysine specific methylation activity. {ECO:0000250}. TISSUE SPECIFICITY: In adult, detected in testis, kidney, spleen and lung, weakly expressed in brain and absent in heart and liver. First detected throughout the embryo at 8 dpc when expression is strong in forebrain neuroepithelium and absent in heart. Expressed in the eye lens between 10 and 14.5 dpc. By 13 dpc, expressed strongly in spinal cord, hand/foot plates and gonads. {ECO:0000269|PubMed:16459028}. +Q6PDK2 KMT2D_MOUSE Histone-lysine N-methyltransferase 2D (Lysine N-methyltransferase 2D) (EC 2.1.1.43) (ALL1-related protein) (Myeloid/lymphoid or mixed-lineage leukemia protein 2) 5588 600,245 Binding site (1); Chain (1); Coiled coil (6); Compositional bias (8); Cross-link (2); Domain (4); Metal binding (4); Modified residue (31); Motif (6); Region (2); Repeat (13); Zinc finger (13) FUNCTION: Histone methyltransferase. Methylates 'Lys-4' of histone H3 (H3K4me). H3K4me represents a specific tag for epigenetic transcriptional activation. Acts as a coactivator for estrogen receptor by being recruited by ESR1, thereby activating transcription (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with ESR1; interaction is direct (By similarity). Component of the MLL2/3 complex (also named ASCOM complex), at least composed of KMT2D/MLL2 or KMT2C/MLL3, ASH2L, RBBP5, WDR5, NCOA6, DPY30, KDM6A, PAXIP1/PTIP, PAGR1 and alpha- and beta-tubulin. {ECO:0000250, ECO:0000269|PubMed:21335234}. DOMAIN: LXXLL motifs 5 and 6 are essential for the association with ESR1 nuclear receptor. {ECO:0000250}. +P18826 KPB1_MOUSE Phosphorylase b kinase regulatory subunit alpha, skeletal muscle isoform (Phosphorylase kinase alpha M subunit) 1241 138,825 Alternative sequence (1); Chain (1); Lipidation (1); Modified residue (14); Region (2); Sequence conflict (6) Glycan biosynthesis; glycogen metabolism. FUNCTION: Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I. The alpha chain may bind calmodulin. PTM: Although the final Cys may be farnesylated, the terminal tripeptide is probably not removed, and the C-terminus is not methylated. {ECO:0000250|UniProtKB:P18688}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. SUBUNIT: Hexadecamer of 4 heterotetramers, each composed of alpha, beta, gamma, and delta subunits. Alpha (PHKA1 or PHKA2) and beta (PHKB) are regulatory subunits, gamma (PHKG1 or PHKG2) is the catalytic subunit, and delta is calmodulin. TISSUE SPECIFICITY: Both isoforms are expressed in muscle. DISEASE: Note=Defects in Phka1 are the cause of phosphorylase kinase deficiency in I-strain mice. {ECO:0000269|PubMed:8298647}. +Q7TSH2 KPBB_MOUSE Phosphorylase b kinase regulatory subunit beta (Phosphorylase kinase subunit beta) 1085 123,889 Chain (1); Lipidation (1); Modified residue (3); Region (2) Glycan biosynthesis; glycogen metabolism. FUNCTION: Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I. The beta chain acts as a regulatory unit and modulates the activity of the holoenzyme in response to phosphorylation (By similarity). {ECO:0000250}. PTM: Although the final Cys may be farnesylated, the terminal tripeptide is probably not removed, and the C-terminus is not methylated. {ECO:0000250|UniProtKB:P12798}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. SUBUNIT: Hexadecamer of 4 heterotetramers, each composed of alpha, beta, gamma, and delta subunits. Alpha (PHKA1 or PHKA2) and beta (PHKB) are regulatory subunits, gamma (PHKG1 or PHKG2) is the catalytic subunit, and delta is calmodulin (By similarity). {ECO:0000250}. +P20444 KPCA_MOUSE Protein kinase C alpha type (PKC-A) (PKC-alpha) (EC 2.7.11.13) 672 76,852 Active site (1); Binding site (3); Chain (1); Domain (3); Initiator methionine (1); Metal binding (13); Modified residue (14); Natural variant (4); Nucleotide binding (1); Sequence conflict (14); Zinc finger (2) FUNCTION: Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that is involved in positive and negative regulation of cell proliferation, apoptosis, differentiation, migration and adhesion, cardiac hypertrophy, angiogenesis, platelet function and inflammation, by directly phosphorylating targets such as RAF1, BCL2, CSPG4, TNNT2/CTNT, or activating signaling cascades involving MAPK1/3 (ERK1/2) and RAP1GAP. Depending on the cell type, is involved in cell proliferation and cell growth arrest by positive and negative regulation of the cell cycle. Can promote cell growth by phosphorylating and activating RAF1, which mediates the activation of the MAPK/ERK signaling cascade, and/or by up-regulating CDKN1A, which facilitates active cyclin-dependent kinase (CDK) complex formation. In cells stimulated by the phorbol ester PMA, can trigger a cell cycle arrest program which is associated with the accumulation of the hyper-phosphorylated growth-suppressive form of RB1 and induction of the CDK inhibitors CDKN1A and CDKN1B. Depending on the cell type, exhibits anti-apoptotic function and protects cells from apoptosis by suppressing the p53/TP53-mediated activation of IGFBP3, or mediates anti-apoptotic action by phosphorylating BCL2. During macrophage differentiation induced by macrophage colony-stimulating factor (CSF1), is translocated to the nucleus and is associated with macrophage development. After wounding, translocates from focal contacts to lamellipodia and participates in the modulation of desmosomal adhesion. Plays a role in cell motility by phosphorylating CSPG4, which induces association of CSPG4 with extensive lamellipodia at the cell periphery and polarization of the cell accompanied by increases in cell motility. During chemokine-induced CD4(+) T cell migration, phosphorylates CDC42-guanine exchange factor DOCK8 resulting in its dissociation from LRCH1 and the activation of GTPase CDC42 (By similarity). Negatively regulates myocardial contractility and positively regulates angiogenesis, platelet aggregation and thrombus formation in arteries. Mediates hypertrophic growth of neonatal cardiomyocytes, in part through a MAPK1/3 (ERK1/2)-dependent signaling pathway, and upon PMA treatment, is required to induce cardiomyocyte hypertrophy up to heart failure and death, by increasing protein synthesis, protein-DNA ratio and cell surface area. Regulates cardiomyocyte function by phosphorylating cardiac troponin T (TNNT2/CTNT), which induces significant reduction in actomyosin ATPase activity, myofilament calcium sensitivity and myocardial contractility. In angiogenesis, is required for full endothelial cell migration, adhesion to vitronectin (VTN), and vascular endothelial growth factor A (VEGFA)-dependent regulation of kinase activation and vascular tube formation. Involved in the stabilization of VEGFA mRNA at post-transcriptional level and mediates VEGFA-induced cell proliferation. In the regulation of calcium-induced platelet aggregation, mediates signals from the CD36/GP4 receptor for granule release, and activates the integrin heterodimer ITGA2B-ITGB3 through the RAP1GAP pathway for adhesion. During response to lipopolysaccharides (LPS), may regulate selective LPS-induced macrophage functions involved in host defense and inflammation. But in some inflammatory responses, may negatively regulate NF-kappa-B-induced genes, through IL1A-dependent induction of NF-kappa-B inhibitor alpha (NFKBIA/IKBA). Upon stimulation with 12-O-tetradecanoylphorbol-13-acetate (TPA), phosphorylates EIF4G1, which modulates EIF4G1 binding to MKNK1 and may be involved in the regulation of EIF4E phosphorylation. Phosphorylates KIT, leading to inhibition of KIT activity. Phosphorylates ATF2 which promotes cooperation between ATF2 and JUN, activating transcription. {ECO:0000250|UniProtKB:P17252, ECO:0000269|PubMed:19147982, ECO:0000269|PubMed:8321321, ECO:0000269|PubMed:9508782}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10092232, ECO:0000269|PubMed:20093473}. Cell membrane {ECO:0000269|PubMed:10092232}; Peripheral membrane protein {ECO:0000305|PubMed:10092232}. Mitochondrion membrane {ECO:0000250|UniProtKB:P17252}; Peripheral membrane protein {ECO:0000250|UniProtKB:P17252}. Nucleus {ECO:0000269|PubMed:20093473}. Note=Translocated to the cell periphery upon tetradecanoyl phorbol acetate (TPA) treatment. SUBUNIT: Interacts with ADAP1/CENTA1 and CSPG4 (By similarity). Interacts with PRKCABP (PubMed:7844141). Binds to CAVIN2 in the presence of phosphatidylserine. Interacts with PICK1 (via PDZ domain). Interacts with TRIM41 (By similarity). Recruited in a circadian manner into a nuclear complex which also includes BMAL1 and RACK1 (PubMed:20093473). Interacts with PARD3 (By similarity). {ECO:0000250|UniProtKB:P05696, ECO:0000250|UniProtKB:P17252, ECO:0000269|PubMed:20093473, ECO:0000269|PubMed:7844141}. DISEASE: Note=Expression of the mutant form UV25 causes malignant transformation of cells. +P68404 KPCB_MOUSE Protein kinase C beta type (PKC-B) (PKC-beta) (EC 2.7.11.13) 671 76,751 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Domain (3); Initiator methionine (1); Metal binding (14); Modified residue (19); Nucleotide binding (1); Zinc finger (2) FUNCTION: Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase involved in various cellular processes such as regulation of the B-cell receptor (BCR) signalosome, oxidative stress-induced apoptosis, androgen receptor-dependent transcription regulation, insulin signaling and endothelial cells proliferation. Plays a key role in B-cell activation by regulating BCR-induced NF-kappa-B activation. Mediates the activation of the canonical NF-kappa-B pathway (NFKB1) by direct phosphorylation of CARD11/CARMA1 at 'Ser-559', 'Ser-644' and 'Ser-652'. Phosphorylation induces CARD11/CARMA1 association with lipid rafts and recruitment of the BCL10-MALT1 complex as well as MAP3K7/TAK1, which then activates IKK complex, resulting in nuclear translocation and activation of NFKB1. Plays a direct role in the negative feedback regulation of the BCR signaling, by down-modulating BTK function via direct phosphorylation of BTK at 'Ser-180', which results in the alteration of BTK plasma membrane localization and in turn inhibition of BTK activity. Involved in apoptosis following oxidative damage: in case of oxidative conditions, specifically phosphorylates 'Ser-36' of isoform p66Shc of SHC1, leading to mitochondrial accumulation of p66Shc, where p66Shc acts as a reactive oxygen species producer. Acts as a coactivator of androgen receptor (ANDR)-dependent transcription, by being recruited to ANDR target genes and specifically mediating phosphorylation of 'Thr-6' of histone H3 (H3T6ph), a specific tag for epigenetic transcriptional activation that prevents demethylation of histone H3 'Lys-4' (H3K4me) by LSD1/KDM1A. In insulin signaling, may function downstream of IRS1 in muscle cells and mediate insulin-dependent DNA synthesis through the RAF1-MAPK/ERK signaling cascade. May participate in the regulation of glucose transport in adipocytes by negatively modulating the insulin-stimulated translocation of the glucose transporter SLC2A4/GLUT4. Under high glucose in pancreatic beta-cells, is probably involved in the inhibition of the insulin gene transcription, via regulation of MYC expression. In endothelial cells, activation of PRKCB induces increased phosphorylation of RB1, increased VEGFA-induced cell proliferation, and inhibits PI3K/AKT-dependent nitric oxide synthase (NOS3/eNOS) regulation by insulin, which causes endothelial dysfunction. Also involved in triglyceride homeostasis. Phosphorylates ATF2 which promotes cooperation between ATF2 and JUN, activating transcription (By similarity). {ECO:0000250, ECO:0000269|PubMed:10499500, ECO:0000269|PubMed:11805327, ECO:0000269|PubMed:12070292, ECO:0000269|PubMed:12118249, ECO:0000269|PubMed:16301747, ECO:0000269|PubMed:16356855, ECO:0000269|PubMed:16505232, ECO:0000269|PubMed:17272725, ECO:0000269|PubMed:8670417}. PTM: Phosphorylation on Thr-500 within the activation loop renders it competent to autophosphorylate. Subsequent autophosphorylation of Thr-642 maintains catalytic competence, and autophosphorylation on Ser-661 appears to release the kinase into the cytosol. Autophosphorylation on other sites i.e. in the N-terminal and hinge regions have no effect on enzyme activity (By similarity). Phosphorylation at Tyr-662 by SYK induces binding with GRB2 and contributes to the activation of MAPK/ERK signaling cascade. {ECO:0000250, ECO:0000269|PubMed:12881490}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. SUBUNIT: Interacts with PDK1. Interacts in vitro with PRKCBP1. Interacts with PHLPP1 and PHLPP2; both proteins mediate its dephosphorylation. Interacts with KDM1A/LSD1, PKN1 and ANDR (By similarity). {ECO:0000250}. +Q62101 KPCD1_MOUSE Serine/threonine-protein kinase D1 (EC 2.7.11.13) (Protein kinase C mu type) (Protein kinase D) (nPKC-D1) (nPKC-mu) 918 102,037 Active site (1); Binding site (1); Chain (1); Compositional bias (2); Domain (2); Modified residue (17); Mutagenesis (4); Nucleotide binding (1); Sequence conflict (1); Zinc finger (2) FUNCTION: Serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of MAPK8/JNK1 and Ras signaling, Golgi membrane integrity and trafficking, cell survival through NF-kappa-B activation, cell migration, cell differentiation by mediating HDAC7 nuclear export, cell proliferation via MAPK1/3 (ERK1/2) signaling, and plays a role in cardiac hypertrophy, VEGFA-induced angiogenesis, genotoxic-induced apoptosis and flagellin-stimulated inflammatory response. Phosphorylates the epidermal growth factor receptor (EGFR) on dual threonine residues, which leads to the suppression of epidermal growth factor (EGF)-induced MAPK8/JNK1 activation and subsequent JUN phosphorylation. Phosphorylates RIN1, inducing RIN1 binding to 14-3-3 proteins YWHAB, YWHAE and YWHAZ and increased competition with RAF1 for binding to GTP-bound form of Ras proteins (NRAS, HRAS and KRAS). Acts downstream of the heterotrimeric G-protein beta/gamma-subunit complex to maintain the structural integrity of the Golgi membranes, and is required for protein transport along the secretory pathway. In the trans-Golgi network (TGN), regulates the fission of transport vesicles that are on their way to the plasma membrane. May act by activating the lipid kinase phosphatidylinositol 4-kinase beta (PI4KB) at the TGN for the local synthesis of phosphorylated inositol lipids, which induces a sequential production of DAG, phosphatidic acid (PA) and lyso-PA (LPA) that are necessary for membrane fission and generation of specific transport carriers to the cell surface. Under oxidative stress, is phosphorylated at Tyr-469 via SRC-ABL1 and contributes to cell survival by activating IKK complex and subsequent nuclear translocation and activation of NFKB1. Involved in cell migration by regulating integrin alpha-5/beta-3 recycling and promoting its recruitment in newly forming focal adhesion. In osteoblast differentiation, mediates the bone morphogenetic protein 2 (BMP2)-induced nuclear export of HDAC7, which results in the inhibition of HDAC7 transcriptional repression of RUNX2. In neurons, plays an important role in neuronal polarity by regulating the biogenesis of TGN-derived dendritic vesicles, and is involved in the maintenance of dendritic arborization and Golgi structure in hippocampal cells. May potentiate mitogenesis induced by the neuropeptide bombesin or vasopressin by mediating an increase in the duration of MAPK1/3 (ERK1/2) signaling, which leads to accumulation of immediate-early gene products including FOS that stimulate cell cycle progression. Plays an important role in the proliferative response induced by low calcium in keratinocytes, through sustained activation of MAPK1/3 (ERK1/2) pathway. Downstream of novel PKC signaling, plays a role in cardiac hypertrophy by phosphorylating HDAC5, which in turn triggers XPO1/CRM1-dependent nuclear export of HDAC5, MEF2A transcriptional activation and induction of downstream target genes that promote myocyte hypertrophy and pathological cardiac remodeling. Mediates cardiac troponin I (TNNI3) phosphorylation at the PKA sites, which results in reduced myofilament calcium sensitivity, and accelerated crossbridge cycling kinetics. The PRKD1-HDAC5 pathway is also involved in angiogenesis by mediating VEGFA-induced specific subset of gene expression, cell migration, and tube formation. In response to VEGFA, is necessary and required for HDAC7 phosphorylation which induces HDAC7 nuclear export and endothelial cell proliferation and migration. During apoptosis induced by cytarabine and other genotoxic agents, PRKD1 is cleaved by caspase-3 at Asp-378, resulting in activation of its kinase function and increased sensitivity of cells to the cytotoxic effects of genotoxic agents. In epithelial cells, is required for transducing flagellin-stimulated inflammatory responses by binding and phosphorylating TLR5, which contributes to MAPK14/p38 activation and production of inflammatory cytokines. May play a role in inflammatory response by mediating activation of NF-kappa-B. May be involved in pain transmission by directly modulating TRPV1 receptor. Plays a role in activated KRAS-mediated stabilization of ZNF304 in colorectal cancer (CRC) cells (By similarity). Regulates nuclear translocation of transcription factor TFEB in macrophages upon live S.enterica infection (PubMed:27184844). {ECO:0000250|UniProtKB:Q15139, ECO:0000269|PubMed:11239398, ECO:0000269|PubMed:11784866, ECO:0000269|PubMed:12407104, ECO:0000269|PubMed:14963034, ECO:0000269|PubMed:15192707, ECO:0000269|PubMed:19029091, ECO:0000269|PubMed:20463010, ECO:0000269|PubMed:24161911, ECO:0000269|PubMed:27184844}. PTM: Phosphorylated at Ser-403 and Ser-407 by MAPK13 during regulation of insulin secretion in pancreatic beta cells (By similarity). Phosphorylated by DAPK1 (By similarity). Phosphorylated at Tyr-93 and by ABL at Tyr-469, which primes the kinase in response to oxidative stress, and promotes a second step activating phosphorylation at Ser-744/Ser-748 by PKRD (By similarity). Phosphorylated at Ser-916 upon S.enterica infection in macrophages (PubMed:27184844). {ECO:0000250|UniProtKB:Q15139, ECO:0000269|PubMed:27184844}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q15139}. Cell membrane {ECO:0000250|UniProtKB:Q15139}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:11239398}. Note=Translocation to the cell membrane is required for kinase activation. {ECO:0000250}. SUBUNIT: Interacts (via N-terminus) with ADAP1/CENTA1. Interacts with MAPK13. Interacts with DAPK1 in an oxidative stress-regulated manner. Interacts with USP28; the interaction induces phosphorylation of USP28 and activated KRAS-mediated stabilization of ZNF304 (By similarity). Interacts with AKAP13 (via C-terminal domain) (PubMed:24161911). {ECO:0000250|UniProtKB:Q15139, ECO:0000269|PubMed:24161911}. +Q9D0M1 KPRA_MOUSE Phosphoribosyl pyrophosphate synthase-associated protein 1 (PRPP synthase-associated protein 1) (39 kDa phosphoribosypyrophosphate synthase-associated protein) (PAP39) 356 39,432 Chain (1); Modified residue (3) FUNCTION: Seems to play a negative regulatory role in 5-phosphoribose 1-diphosphate synthesis. {ECO:0000250}. SUBUNIT: Binds to PRPS1 and PRPS2. {ECO:0000250}. +Q8R574 KPRB_MOUSE Phosphoribosyl pyrophosphate synthase-associated protein 2 (PRPP synthase-associated protein 2) (41 kDa phosphoribosypyrophosphate synthetase-associated protein) (PAP41) 369 40,881 Chain (1); Modified residue (4) FUNCTION: Seems to play a negative regulatory role in 5-phosphoribose 1-diphosphate synthesis. {ECO:0000250}. SUBUNIT: Binds to PRPS1 and PRPS2. {ECO:0000250}. +Q62074 KPCI_MOUSE Protein kinase C iota type (EC 2.7.11.13) (Atypical protein kinase C-lambda/iota) (aPKC-lambda/iota) (nPKC-iota) 595 68,203 Active site (1); Beta strand (7); Binding site (1); Chain (1); Domain (3); Erroneous initiation (2); Helix (17); Initiator methionine (1); Modified residue (10); Motif (1); Mutagenesis (9); Nucleotide binding (1); Region (3); Turn (5); Zinc finger (1) FUNCTION: Calcium- and diacylglycerol-independent serine/ threonine-protein kinase that plays a general protective role against apoptotic stimuli, is involved in NF-kappa-B activation, cell survival, differentiation and polarity, and contributes to the regulation of microtubule dynamics in the early secretory pathway. Is necessary for BCR-ABL oncogene-mediated resistance to apoptotic drug in leukemia cells, protecting leukemia cells against drug-induced apoptosis. In cultured neurons, prevents amyloid beta protein-induced apoptosis by interrupting cell death process at a very early step. In glioblastoma cells, may function downstream of phosphatidylinositol 3-kinase (PI3K) and PDPK1 in the promotion of cell survival by phosphorylating and inhibiting the pro-apoptotic factor BAD. Can form a protein complex in non-small cell lung cancer (NSCLC) cells with PARD6A and ECT2 and regulate ECT2 oncogenic activity by phosphorylation, which in turn promotes transformed growth and invasion. In response to nerve growth factor (NGF), acts downstream of SRC to phosphorylate and activate IRAK1, allowing the subsequent activation of NF-kappa-B and neuronal cell survival. Functions in the organization of the apical domain in epithelial cells by phosphorylating EZR. This step is crucial for activation and normal distribution of EZR at the early stages of intestinal epithelial cell differentiation. Forms a protein complex with LLGL1 and PARD6B independently of PARD3 to regulate epithelial cell polarity. Plays a role in microtubule dynamics in the early secretory pathway through interaction with RAB2A and GAPDH and recruitment to vesicular tubular clusters (VTCs). In human coronary artery endothelial cells (HCAEC), is activated by saturated fatty acids and mediates lipid-induced apoptosis (By similarity). Downstream of PI3K is required for insulin-stimulated glucose transport. Activates RAB4A and promotes its association with KIF3A which is required for the insulin-induced SLC2A4/GLUT4 translocation in adipocytes. Is essential in early embryogenesis and development of differentiating photoreceptors by playing a role in the establishment of epithelial and neuronal polarity. Involved in early synaptic long term potentiation phase in CA1 hippocampal cells and short term memory formation (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:F1M7Y5, ECO:0000269|PubMed:12832475, ECO:0000269|PubMed:14615604, ECO:0000269|PubMed:15322187, ECO:0000269|PubMed:16267237, ECO:0000269|PubMed:9971737}. PTM: Phosphorylation at Thr-411 in the activation loop is not mandatory for activation (PubMed:22579248). Upon neuronal growth factor (NGF) stimulation, phosphorylated by SRC at Tyr-264, Tyr-279 and Tyr-333 (By similarity). Phosphorylation on Tyr-264 facilitates binding to KPNB1/importin-beta regulating entry of PRKCI into the nucleus (By similarity). Phosphorylation on Tyr-333 is important for NF-kappa-B stimulation (By similarity). Phosphorylated at Thr-563 during the initial phase of long term potentiation (By similarity). {ECO:0000250|UniProtKB:F1M7Y5, ECO:0000250|UniProtKB:P41743, ECO:0000269|PubMed:22579248}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P41743}. Membrane {ECO:0000250|UniProtKB:P41743}. Endosome {ECO:0000250|UniProtKB:P41743}. Nucleus {ECO:0000250|UniProtKB:P41743}. Note=Transported into the endosome through interaction with SQSTM1/p62. After phosphorylation by SRC, transported into the nucleus through interaction with KPNB1. Colocalizes with CDK7 in the cytoplasm and nucleus. Transported to vesicular tubular clusters (VTCs) through interaction with RAB2A. {ECO:0000250|UniProtKB:P41743}. SUBUNIT: Forms a complex with SQSTM1 and MP2K5 (PubMed:12813044). Interacts directly with SQSTM1 (Probable). Interacts with IKBKB. Interacts with PARD6A, PARD6B and PARD6G. Part of a quaternary complex containing aPKC, PARD3, a PARD6 protein (PARD6A, PARD6B or PARD6G) and a GTPase protein (CDC42 or RAC1) (PubMed:10934474). Part of a complex with LLGL1 and PARD6B. Interacts with ADAP1/CENTA1. Interaction with SMG1, through the ZN-finger domain, activates the kinase activity. Interacts with CDK7. Forms a complex with RAB2A and GAPDH involved in recruitment onto the membrane of vesicular tubular clusters (VTCs). Interacts with ECT2 ('Thr-359' phosphorylated form) (By similarity). Interacts with VAMP2 (PubMed:17313651). Interacts with WDFY2 (via WD repeats 1-3) (PubMed:16792529). {ECO:0000250|UniProtKB:P41743, ECO:0000269|PubMed:10934474, ECO:0000269|PubMed:12813044, ECO:0000269|PubMed:16792529, ECO:0000269|PubMed:17313651, ECO:0000305}. DOMAIN: The PB1 domain mediates interaction with SQSTM1.; DOMAIN: The C1 zinc finger does not bind diacylglycerol (DAG). {ECO:0000250}.; DOMAIN: The pseudosubstrate motif resembles the sequence around sites phosphorylated on target proteins, except the presence of a non-phosphorylatable residue in place of Ser, it modulates activity by competing with substrates. +Q9QZU5 KR151_MOUSE Keratin-associated protein 15-1 (Keratin-associated protein 15) (Pubertal mammary gland-specific protein 2) 150 16,242 Chain (1) FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins. {ECO:0000305}. SUBUNIT: Interacts with hair keratins. {ECO:0000305}. TISSUE SPECIFICITY: Expressed at high levels in skin and at lower levels in the developing mammary gland. {ECO:0000269|PubMed:10446281}. +A2A5X5 KR161_MOUSE Keratin-associated protein 16-1 502 52,020 Chain (1); Region (1); Repeat (15) FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins. SUBUNIT: Interacts with hair keratins. {ECO:0000250}. +Q8C1I6 KR163_MOUSE Keratin-associated protein 16-3 (Keratin-associated protein 16-10) (Keratin-associated protein 16.3) 86 8,433 Chain (1); Frameshift (1); Region (1); Sequence conflict (7) FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins. {ECO:0000305}. SUBUNIT: Interacts with hair keratins. {ECO:0000250}. TISSUE SPECIFICITY: Strong expression in narrowly defined pattern restricted to the lower and middle cortical regions of the hair shaft in both developing and cycling hair. During hair follicle regression (catagen), expression levels decrease until expression is no longer detectable in follicles at resting stage (telogen). {ECO:0000269|PubMed:15385554}. +Q925H6 KR193_MOUSE Keratin-associated protein 19-3 (Keratin-associated protein 16-5) (Keratin-associated protein 16.5) 87 8,823 Chain (1); Region (1) FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins. {ECO:0000305}. SUBUNIT: Interacts with hair keratins. {ECO:0000250}. TISSUE SPECIFICITY: Strong expression in narrowly defined pattern restricted to the lower and middle cortical regions of the hair shaft in both developing and cycling hair. During hair follicle regression (catagen), expression levels decrease until expression is no longer detectable in follicles at resting stage (telogen). {ECO:0000269|PubMed:15385554}. +P53657 KPYR_MOUSE Pyruvate kinase PKLR (EC 2.7.1.40) (L-PK) (Pyruvate kinase isozymes L/R) 574 62,309 Binding site (6); Chain (1); Metal binding (6); Modified residue (5); Region (2); Site (1) Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5. FUNCTION: Plays a key role in glycolysis. {ECO:0000250}. SUBUNIT: Homotetramer. {ECO:0000250}. +A2A591 KRA31_MOUSE Keratin-associated protein 3-1 (High-sulfur keratin protein) 98 10,271 Chain (1); Initiator methionine (1); Modified residue (1); Region (1); Repeat (4) FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins (By similarity). {ECO:0000250}. SUBUNIT: Interacts with hair keratins. {ECO:0000250}. +Q9D638 KRA32_MOUSE Keratin-associated protein 3-2 (Keratin-associated protein 3-3) 99 10,574 Chain (1); Initiator methionine (1); Modified residue (1); Region (1); Repeat (3); Sequence conflict (1) FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins (By similarity). {ECO:0000250}. SUBUNIT: Interacts with hair keratins. {ECO:0000250}. +Q62220 KRA54_MOUSE Keratin-associated protein 5-4 (Ultra high sulfur serine protein 2) (UHS-Ser-2) 223 21,442 Chain (1); Compositional bias (1); Region (1); Repeat (14) FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated protein (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins. {ECO:0000305}. SUBUNIT: Interacts with hair keratins. {ECO:0000305}. TISSUE SPECIFICITY: Expressed during the active phases of the hair cycle in the medulla and the inner root sheath of the forming hair. Also expressed in the upper layers of the epidermis of skin. {ECO:0000269|PubMed:2250030}. +Q2TA51 KRA55_MOUSE Keratin-associated protein 5-5 241 23,063 Chain (1); Compositional bias (1); Region (1); Repeat (15) FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated protein (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins. {ECO:0000305}. SUBUNIT: Interacts with hair keratins. {ECO:0000305}. +O08884 KRA62_MOUSE Keratin-associated protein 6-2 (High-glycine tyrosine keratin type II.4) (HGTp type II.4) (HgtpII.4) 159 15,262 Chain (1); Region (1) FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins. {ECO:0000305}. SUBUNIT: Interacts with hair keratins. {ECO:0000305}. TISSUE SPECIFICITY: Expressed in skin during two hair growth cycles. Expression restricted to the cortical cells of hair follicles, appearing first in the cortical cells processing the flat nuclei located a few cells above the dermal papilla. {ECO:0000269|PubMed:9374545}. +Q925H3 KRA65_MOUSE Keratin-associated protein 6-5 (Keratin-associated protein 16-8) (Keratin-associated protein 16.8) 78 7,945 Chain (1); Region (1) FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins. {ECO:0000305}. SUBUNIT: Interacts with hair keratins. {ECO:0000250}. TISSUE SPECIFICITY: Strong expression in narrowly defined pattern restricted to the lower and middle cortical regions of the hair shaft in both developing and cycling hair. During hair follicle regression (catagen), expression levels decrease until expression is no longer detectable in follicles at resting stage (telogen). {ECO:0000269|PubMed:15385554, ECO:0000269|PubMed:15489334}. +Q3V2C1 KRA93_MOUSE Keratin-associated protein 9-3 (Keratin-associated protein 9.3) (Ultrahigh sulfur keratin-associated protein 9.3) 136 13,902 Chain (1); Region (1); Repeat (11); Sequence conflict (2) FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins (By similarity). {ECO:0000250}. SUBUNIT: Interacts with hair keratins. {ECO:0000250}. +Q8K1S7 KREM2_MOUSE Kremen protein 2 (Dickkopf receptor 2) (Kringle domain-containing transmembrane protein 2) (Kringle-containing protein marking the eye and the nose) 461 49,170 Chain (1); Disulfide bond (4); Domain (3); Glycosylation (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 364 386 Helical. {ECO:0000255}. TOPO_DOM 25 363 Extracellular. {ECO:0000255}.; TOPO_DOM 387 461 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for Dickkopf proteins. Cooperates with DKK1/2 to inhibit Wnt/beta-catenin signaling by promoting the endocytosis of Wnt receptors LRP5 and LRP6 (PubMed:12050670). Plays a role in limb development; attenuates Wnt signaling in the developing limb to allow normal limb patterning and can also negatively regulate bone formation (PubMed:18505822). {ECO:0000269|PubMed:12050670, ECO:0000269|PubMed:18505822}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Interacts with ERLEC1 (PubMed:16531414). Forms a ternary complex with DKK1 and LRP6 (PubMed:12050670). {ECO:0000269|PubMed:12050670, ECO:0000269|PubMed:16531414}. DOMAIN: Binding to ERLEC1 is mediated by the oligosaccharides linked to the kringle domain. {ECO:0000269|PubMed:16531414}. +Q8BGA5 KRR1_MOUSE KRR1 small subunit processome component homolog (HIV-1 Rev-binding protein 2 homolog) (KRR-R motif-containing protein 1) 380 43,538 Chain (1); Compositional bias (1); Cross-link (3); Domain (1); Frameshift (1); Modified residue (1); Sequence conflict (3) FUNCTION: Required for 40S ribosome biogenesis. Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13601}. Nucleus {ECO:0000250|UniProtKB:Q13601}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q13601}. SUBUNIT: Component of the ribosomal small subunit (SSU) processome. {ECO:0000250}. +Q9D646 KRT34_MOUSE Keratin, type I cuticular Ha4 (Hair keratin, type I Ha4) (Keratin-34) (K34) 392 44,560 Chain (1); Domain (1); Region (7); Site (1) TISSUE SPECIFICITY: Expressed in the hair root in the hair shaft cuticle and cortex. {ECO:0000269|PubMed:1689759}. +Q497I4 KRT35_MOUSE Keratin, type I cuticular Ha5 (Hair keratin, type I Ha5) (Keratin-35) (K35) 455 50,530 Chain (1); Domain (1); Erroneous initiation (2); Region (7); Sequence conflict (3); Site (1) +P18654 KS6A3_MOUSE Ribosomal protein S6 kinase alpha-3 (S6K-alpha-3) (EC 2.7.11.1) (90 kDa ribosomal protein S6 kinase 3) (p90-RSK 3) (p90RSK3) (MAP kinase-activated protein kinase 1b) (MAPK-activated protein kinase 1b) (MAPKAP kinase 1b) (MAPKAPK-1b) (Ribosomal S6 kinase 2) (RSK-2) (pp90RSK2) 740 83,694 Active site (2); Beta strand (18); Binding site (2); Chain (1); Domain (3); Helix (30); Modified residue (9); Mutagenesis (4); Nucleotide binding (2); Turn (5) FUNCTION: Serine/threonine-protein kinase that acts downstream of ERK (MAPK1/ERK2 and MAPK3/ERK1) signaling and mediates mitogenic and stress-induced activation of the transcription factors CREB1, ETV1/ER81 and NR4A1/NUR77, regulates translation through RPS6 and EIF4B phosphorylation, and mediates cellular proliferation, survival, and differentiation by modulating mTOR signaling and repressing pro-apoptotic function of BAD and DAPK1. In fibroblast, is required for EGF-stimulated phosphorylation of CREB1 and histone H3 at 'Ser-10', which results in the subsequent transcriptional activation of several immediate-early genes. In response to mitogenic stimulation (EGF and PMA), phosphorylates and activates NR4A1/NUR77 and ETV1/ER81 transcription factors and the cofactor CREBBP. Upon insulin-derived signal, acts indirectly on the transcription regulation of several genes by phosphorylating GSK3B at 'Ser-9' and inhibiting its activity. Phosphorylates RPS6 in response to serum or EGF via an mTOR-independent mechanism and promotes translation initiation by facilitating assembly of the preinitiation complex. In response to insulin, phosphorylates EIF4B, enhancing EIF4B affinity for the EIF3 complex and stimulating cap-dependent translation. Is involved in the mTOR nutrient-sensing pathway by directly phosphorylating TSC2 at 'Ser-1798', which potently inhibits TSC2 ability to suppress mTOR signaling, and mediates phosphorylation of RPTOR, which regulates mTORC1 activity and may promote rapamycin-sensitive signaling independently of the PI3K/AKT pathway. Mediates cell survival by phosphorylating the pro-apoptotic proteins BAD and DAPK1 and suppressing their pro-apoptotic function. Promotes the survival of hepatic stellate cells by phosphorylating CEBPB in response to the hepatotoxin carbon tetrachloride (CCl4). Is involved in cell cycle regulation by phosphorylating the CDK inhibitor CDKN1B, which promotes CDKN1B association with 14-3-3 proteins and prevents its translocation to the nucleus and inhibition of G1 progression. In LPS-stimulated dendritic cells, is involved in TLR4-induced macropinocytosis, and in myeloma cells, acts as effector of FGFR3-mediated transformation signaling, after direct phosphorylation at Tyr-529 by FGFR3. Phosphorylates DAPK1 (By similarity). Negatively regulates EGF-induced MAPK1/3 phosphorylation via phosphorylation of SOS1. Phosphorylates SOS1 at 'Ser-1134' and 'Ser-1161' that create YWHAB and YWHAE binding sites and which contribute to the negative regulation of MAPK1/3 phosphorylation (PubMed:22827337). Phosphorylates EPHA2 at 'Ser-897',the RPS6KA-EPHA2 signaling pathway controls cell migration (By similarity). {ECO:0000250|UniProtKB:P51812, ECO:0000269|PubMed:10856237, ECO:0000269|PubMed:14504289, ECO:0000269|PubMed:17785202, ECO:0000269|PubMed:17906627, ECO:0000269|PubMed:22827337}. PTM: Activated by phosphorylation at Ser-227 by PDPK1. Autophosphorylated on Ser-386, as part of the activation process. May be phosphorylated at Thr-365 and Ser-369 by MAPK1/ERK2 and MAPK3/ERK1. Can also be activated via phosphorylation at Ser-386 by MAPKAPK2. {ECO:0000269|PubMed:10480933, ECO:0000269|PubMed:17785202, ECO:0000269|PubMed:17906627}.; PTM: N-terminal myristoylation results in an activated kinase in the absence of added growth factors. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. SUBUNIT: Forms a complex with either MAPK1/ERK2 or MAPK3/ERK1 in quiescent cells. Transiently dissociates following mitogenic stimulation (By similarity). Interacts with NFATC4, ETV1/ER81 and FGFR1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Intestine, thymus, lung, heart and brain. +Q61097 KSR1_MOUSE Kinase suppressor of Ras 1 (mKSR1) (Protein Hb) 873 96,755 Alternative sequence (2); Beta strand (4); Chain (1); Compositional bias (3); Domain (1); Helix (13); Metal binding (8); Modified residue (9); Mutagenesis (14); Region (1); Turn (6); Zinc finger (1) FUNCTION: Scaffolding protein that is part of a multiprotein signaling complex. Promotes phosphorylation of Raf family members and activation of downstream MAP kinases (PubMed:10409742, PubMed:12932319, PubMed:21102438). Promotes activation of MAPK1 and/or MAPK3, both in response to EGF and to cAMP (PubMed:21102438). Does not have kinase activity by itself (Probable). {ECO:0000269|PubMed:10409742, ECO:0000269|PubMed:12932319, ECO:0000269|PubMed:21102438, ECO:0000305}. PTM: Phosphorylated on Ser-297 and, to a higher extent, on Ser-392 by MARK3 (PubMed:11741534). Dephosphorylated on Ser-392 by PPP2CA (PubMed:12932319). Phosphorylated KSR1 is cytoplasmic and dephosphorylated KSR1 is membrane-associated (Probable). Phosphorylated by PKA at Ser-838. Phosphorylation at Ser-838 is required for cAMP-dependent activation of MAPK1 and/or MAPK3 (PubMed:21102438). {ECO:0000269|PubMed:10409742, ECO:0000269|PubMed:10891492, ECO:0000269|PubMed:11741534, ECO:0000269|PubMed:12932319, ECO:0000269|PubMed:21102438, ECO:0000305}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742, ECO:0000269|PubMed:11741534, ECO:0000269|PubMed:12932319, ECO:0000269|PubMed:23250398}. Membrane {ECO:0000269|PubMed:10409742}; Peripheral membrane protein {ECO:0000269|PubMed:10409742}. Cell membrane {ECO:0000269|PubMed:11741534, ECO:0000269|PubMed:12932319, ECO:0000269|PubMed:23250398}; Peripheral membrane protein {ECO:0000269|PubMed:11741534, ECO:0000269|PubMed:12932319, ECO:0000269|PubMed:23250398}. Cell projection, ruffle membrane {ECO:0000269|PubMed:23250398}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8IVT5}. Note=In unstimulated cells, where the phosphorylated form is bound to a 14-3-3 protein, sequestration in the cytoplasm occurs. Following growth factor treatment, the protein is free for membrane translocation, and it moves from the cytoplasm to the cell periphery. {ECO:0000305|PubMed:12932319}. SUBUNIT: Interacts with HSP90AA1/HSP90, YWHAB/14-3-3, CDC37, MAP2K1/MEK-1, MAP2K2/MEK-2, MARK3, PPP2R1A and PPP2CA (PubMed:10891492, PubMed:10409742, PubMed:11741534, PubMed:12932319). Interacts with YWHAE (PubMed:10409742). Also interacts with RAF and MAPK/ERK, in a Ras-dependent manner. The binding of 14-3-3 proteins to phosphorylated KSR prevents the membrane localization (PubMed:8521512). Interacts with VRK2 (By similarity). Interacts with AKAP13 and BRAF. Identified in a complex with AKAP13, MAP2K1 and BRAF (PubMed:21102438, PubMed:23250398). {ECO:0000250|UniProtKB:Q8IVT5, ECO:0000269|PubMed:10409742, ECO:0000269|PubMed:21102438, ECO:0000269|PubMed:23250398}. DOMAIN: The protein kinase domain is predicted to be catalytically inactive. The domain is sufficient for KSR1 and KSR1-mediated MAP2K1 and MAP2K2 membrane localization. The domain is required but not sufficient for MAP kinase-mediated inhibition of ELK1 phosphorylation (PubMed:10409742). {ECO:0000255, ECO:0000269|PubMed:10409742}.; DOMAIN: The N-terminal region mediates interaction with BRAF and with membranes. {ECO:0000269|PubMed:23250398}. TISSUE SPECIFICITY: Expressed in brain, spleen and testis. Isoform 1 is highly expressed spleen and weakly in testis, and isoform 2 is highly expressed in brain and weakly in testis. {ECO:0000269|PubMed:10891492}. +Q8BLK9 KS6C1_MOUSE Ribosomal protein S6 kinase delta-1 (S6K-delta-1) (EC 2.7.11.1) (52 kDa ribosomal protein S6 kinase) 1056 115,712 Active site (1); Alternative sequence (9); Binding site (1); Chain (1); Domain (4); Erroneous initiation (1); Modified residue (17); Nucleotide binding (1); Sequence conflict (2) FUNCTION: May be involved in transmitting sphingosine-1 phosphate (SPP)-mediated signaling into the cell. Plays a role in the recruitment of PRDX3 to early endosomes. {ECO:0000250|UniProtKB:Q96S38}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96S38}. Membrane {ECO:0000250|UniProtKB:Q96S38}. Early endosome {ECO:0000250|UniProtKB:Q96S38}. SUBUNIT: Interacts with SPHK1 and phosphatidylinositol 3-phosphate. Interacts (via PX domain) with PRDX3. {ECO:0000250|UniProtKB:Q96S38}. DOMAIN: The PX domain is essential for its localization to the early endosomes. {ECO:0000250|UniProtKB:Q96S38}.; DOMAIN: The first protein kinase domain appears to be a pseudokinase domain as it does not contain the classical characteristics, such as the ATP-binding motif, ATP-binding site and active site. +Q5SYL1 KS6R_MOUSE Ribosomal protein S6 kinase-related protein (EC 2.7.11.1) 278 31,682 Active site (1); Binding site (1); Chain (1); Domain (1); Nucleotide binding (1) +Q8CCX5 KT222_MOUSE Keratin-like protein KRT222 (Keratin-222) 294 34,198 Alternative sequence (1); Chain (1); Coiled coil (1); Domain (1); Erroneous termination (1) +Q8K0Y2 KT33A_MOUSE Keratin, type I cuticular Ha3-I (Hair keratin, type I Ha3-I) (Keratin-33A) (K33A) 404 46,137 Chain (1); Compositional bias (1); Domain (1); Region (7); Sequence conflict (1); Site (1) +Q61897 KT33B_MOUSE Keratin, type I cuticular Ha3-II (Hair keratin, type I Ha3) (Keratin, type I cuticular Ha3) (Keratin-33B) (K33B) 404 45,864 Chain (1); Compositional bias (1); Domain (1); Region (7); Sequence conflict (6); Site (1) TISSUE SPECIFICITY: Expressed strongly in cortex cells in newborn back skin and in the central unit of the lingual filiform papillae. {ECO:0000269|PubMed:7514534}. +Q3V2T4 KTDAP_MOUSE Keratinocyte differentiation-associated protein 102 11,497 Alternative sequence (1); Chain (1); Sequence conflict (1); Signal peptide (1) FUNCTION: May act as a soluble regulator of keratinocyte differentiation. May play an important role in embryonic skin morphogenesis (By similarity). {ECO:0000250|UniProtKB:P60985, ECO:0000250|UniProtKB:P85411}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15256262}. TISSUE SPECIFICITY: Expression restricted to suprabasal keratinocytes of the epidermis. {ECO:0000269|PubMed:15256262}. +Q61865 MIA_MOUSE Melanoma-derived growth regulatory protein (Cartilage-derived retinoic acid-sensitive protein) (CD-RAP) (Melanoma inhibitory activity protein) 130 14,593 Chain (1); Disulfide bond (2); Domain (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Elicits growth inhibition on melanoma cells in vitro as well as some other neuroectodermal tumors, including gliomas. {ECO:0000250}. PTM: May possess two intramolecular disulfide bonds. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Interacts with FASLG. {ECO:0000250}. TISSUE SPECIFICITY: All malignant melanoma cell lines tested and infrequently in glioma cell lines. +Q7TNS2 MIC10_MOUSE MICOS complex subunit Mic10 (Mitochondrial inner membrane organizing system protein 1) 76 8,567 Chain (1); Initiator methionine (1); Modified residue (1); Topological domain (1); Transmembrane (1) TRANSMEM 17 36 Helical. {ECO:0000255}. TOPO_DOM 37 76 Mitochondrial intermembrane. {ECO:0000255}. FUNCTION: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. {ECO:0000250|UniProtKB:Q5TGZ0}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q5TGZ0}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q5TGZ0}. Note=The C-terminus is located in the intermembrane space, while the location of the N-terminus has not been determined yet. As some programs predict the presence of 2 closely apposed membrane domains, it has been proposed that the protein may cross the membrane twice and that both termini may face the intermembrane space. {ECO:0000250|UniProtKB:Q5TGZ0}. SUBUNIT: Component of the mitochondrial contact site and cristae organizing system (MICOS) complex, composed of at least MINOS1/MIC10, CHCHD3/MIC19, CHCHD6/MIC25, APOOL/MIC27, IMMT/MIC60, APOO/MIC23/MIC26 and QIL1/MIC13. This complex was also known under the names MINOS or MitOS complex. The MICOS complex associates with mitochondrial outer membrane proteins SAMM50, MTX1 and MTX2 (together described as components of the mitochondrial outer membrane sorting assembly machinery (SAM) complex) and DNAJC11, mitochondrial inner membrane protein TMEM11 and with HSPA9. The MICOS and SAM complexes together with DNAJC11 are part of a large protein complex spanning both membranes termed the mitochondrial intermembrane space bridging (MIB) complex. Interacts with IMMT/MIC60 and QIL1/MIC13. Interacts with APOO/MIC23/MIC26 and APOOL/MIC27. {ECO:0000250|UniProtKB:Q5TGZ0}. +Q8R404 MIC13_MOUSE MICOS complex subunit MIC13 119 13,373 Chain (1); Transmembrane (1) TRANSMEM 8 26 Helical. {ECO:0000255}. FUNCTION: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. Constituent of mature MICOS complex, it is required for the formation of cristae junction (CJ) and maintenance of cristae morphology. Required for the incorporation of MINOS1/MIC10 into the MICOS complex. {ECO:0000250|UniProtKB:Q5XKP0}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q5XKP0}; Single-pass membrane protein {ECO:0000255}. Note=Enriched at crista junctions. {ECO:0000250|UniProtKB:Q5XKP0}. SUBUNIT: Component of the mitochondrial contact site and cristae organizing system (MICOS) complex, composed of at least MINOS1/MIC10, CHCHD3/MIC19, CHCHD6/MIC25, APOO/MIC26, QIL1/MIC13, APOOL/MIC27 and IMMT/MIC60. The MICOS complex associates with mitochondrial outer membrane proteins SAMM50, MTX1 and MTX2 (together described as components of the mitochondrial outer membrane sorting assembly machinery (SAM) complex) and DNAJC11, mitochondrial inner membrane protein TMEM11 and with HSPA9. The MICOS and SAM complexes together with DNAJC11 are part of a large protein complex spanning both membranes termed the mitochondrial intermembrane space bridging (MIB) complex. {ECO:0000250|UniProtKB:Q5XKP0}. +Q8VCX5 MICU1_MOUSE Calcium uptake protein 1, mitochondrial (Calcium-binding atopy-related autoantigen 1 homolog) 477 54,353 Alternative sequence (2); Calcium binding (2); Chain (1); Disulfide bond (1); Domain (3); Mutagenesis (8); Region (2); Sequence conflict (1); Topological domain (1); Transit peptide (1); Transmembrane (1) TRANSMEM 34 52 Helical. {ECO:0000255}. TOPO_DOM 53 477 Mitochondrial intermembrane. {ECO:0000250|UniProtKB:Q9BPX6}. FUNCTION: Key regulator of mitochondrial calcium uniporter (MCU) that senses calcium level via its EF-hand domains (PubMed:24560927). MICU1 and MICU2 form a disulfide-linked heterodimer that stimulates and inhibits MCU activity, depending on the concentration of calcium (PubMed:24560927). MICU1 acts both as an activator or inhibitor of mitochondrial calcium uptake (By similarity). Acts as a gatekeeper of MCU at low concentration of calcium, preventing channel opening (By similarity). Enhances MCU opening at high calcium concentration, allowing a rapid response of mitochondria to calcium signals generated in the cytoplasm (PubMed:24560927). Regulates glucose-dependent insulin secretion in pancreatic beta-cells by regulating mitochondrial calcium uptake (By similarity). Induces T-helper 1-mediated autoreactivity, which is accompanied by the release of IFNG (By similarity). {ECO:0000250|UniProtKB:Q9BPX6}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9BPX6}; Single-pass membrane protein {ECO:0000255}. Mitochondrion intermembrane space {ECO:0000250|UniProtKB:Q9BPX6}. Note=The topology is subject to debate. {ECO:0000250|UniProtKB:Q9BPX6}. SUBUNIT: Homohexamer; in absence of calcium (By similarity). Forms a homohexamer in absence of calcium and rearranges into a heterodimer in presence of calcium (By similarity). Heterodimer; disulfide-linked; heterodimerizes with MICU2 (PubMed:23409044, PubMed:24560927). The heterodimer formed with MICU2 associates with MCU at low calcium concentration and dissociates from MCU at high calcium level (By similarity). Component of the uniplex complex, composed of MCU, MCUB, MICU1, MICU2 and EMRE/SMDT1 (By similarity). Interacts (via polybasic region) with EMRE/SMDT1; the interaction is direct (By similarity). Interacts (via polybasic region) with MCU (via coiled coil domains); the interaction is direct and precedes formation of the heterodimer with MICU2 (PubMed:23409044). Interacts with SLC25A23 (By similarity). Interacts with CHCHD4/MIA40; which introduces the interchain disulfide bond with MICU2 (By similarity). {ECO:0000250|UniProtKB:Q9BPX6, ECO:0000269|PubMed:23409044, ECO:0000269|PubMed:24560927}. DOMAIN: The EF-hand domains have high affinity for calcium and act as sensors of mitochondrial matrix calcium levels. {ECO:0000269|PubMed:24560927}.; DOMAIN: The C-helix is required for assembling the Ca(2+)-free homohexamer. It also plays a key role in mitochondrial calcium uptake, probably by mediating interaction with MICU2. {ECO:0000250|UniProtKB:Q9BPX6}.; DOMAIN: The EF-hand domains have high affinity for calcium and act as sensors of calcium levels. {ECO:0000250|UniProtKB:Q9BPX6}. TISSUE SPECIFICITY: Expressed in skeletal muscle, heart, kidney, liver, brain, lung, fat and spleen. {ECO:0000269|PubMed:21685888, ECO:0000269|PubMed:23409044}. +Q9CTY5 MICU3_MOUSE Calcium uptake protein 3, mitochondrial (EF-hand domain-containing family member A2) 523 59,810 Calcium binding (2); Chain (1); Compositional bias (2); Domain (3); Erroneous initiation (1); Transmembrane (1) TRANSMEM 66 82 Helical. {ECO:0000255}. FUNCTION: May play a role in mitochondrial calcium uptake. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}. Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Predominantly expressed in skeletal muscle and central nervous system. {ECO:0000269|PubMed:23409044}. +Q3TPJ7 MIDN_MOUSE Midnolin (Midbrain nucleolar protein) 465 49,192 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (1); Region (1) FUNCTION: Facilitates ubiquitin-independent proteasomal degradation of polycomb protein CBX4 (PubMed:27326929). Plays a role in inhibiting the activity of glucokinase GCK and both glucose-induced and basal insulin secretion (By similarity). {ECO:0000250|UniProtKB:D4AE48, ECO:0000269|PubMed:27326929}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10974535, ECO:0000269|PubMed:24187134}. Cytoplasm, cytosol {ECO:0000269|PubMed:24187134}. Nucleus, nucleolus {ECO:0000269|PubMed:10974535}. Note=Detected in the nucleus and nucleolus with no expression in the cytoplasm (PubMed:10974535). However, a later study finds expression in the nucleus and cytoplasm with no expression in the nucleolus (PubMed:24187134). {ECO:0000269|PubMed:10974535, ECO:0000269|PubMed:24187134}. SUBUNIT: Interacts with GCK; the interaction occurs preferentially at low glucose levels. {ECO:0000250|UniProtKB:D4AE48, ECO:0000250|UniProtKB:Q504T8}. TISSUE SPECIFICITY: Expressed at high levels in brain and liver with significantly lower levels in muscle. {ECO:0000269|PubMed:24187134}. +Q9WV86 KTNA1_MOUSE Katanin p60 ATPase-containing subunit A1 (Katanin p60 subunit A1) (EC 5.6.1.1) (Lipotransin) (p60 katanin) 491 55,949 Chain (1); Helix (3); Modified residue (1); Mutagenesis (2); Nucleotide binding (1); Region (3) FUNCTION: Catalytic subunit of a complex which severs microtubules in an ATP-dependent manner. Microtubule severing may promote rapid reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. Microtubule release from the mitotic spindle poles may allow depolymerization of the microtubule end proximal to the spindle pole, leading to poleward microtubule flux and poleward motion of chromosome. The function in regulating microtubule dynamics at spindle poles seems to depend on the association of the katanin KATNA1:KATNB1 complex with ASPM which recruits it to microtubules. Reversely KATNA1:KATNB1 can enhance ASPM blocking activity on microtubule minus-end growth. Microtubule release within the cell body of neurons may be required for their transport into neuronal processes by microtubule-dependent motor proteins. This transport is required for axonal growth. {ECO:0000255|HAMAP-Rule:MF_03023, ECO:0000269|PubMed:28436967}. PTM: Phosphorylation by DYRK2 triggers ubiquitination and subsequent degradation. {ECO:0000255|HAMAP-Rule:MF_03023}.; PTM: Ubiquitinated by the BCR(KLHL42) E3 ubiquitin ligase complex, leading to its proteasomal degradation. Ubiquitinated by the EDVP E3 ligase complex and subsequently targeted for proteasomal degradation. {ECO:0000255|HAMAP-Rule:MF_03023}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03023}. Midbody {ECO:0000255|HAMAP-Rule:MF_03023}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03023}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000255|HAMAP-Rule:MF_03023}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:O75449}. Note=Predominantly cytoplasmic. Localized diffusely in the cytoplasm during the interphase. During metaphase is localized throughout the cell and more widely dispersed than the microtubules. In anaphase and telophase is localized at the midbody region. Also localized to the interphase centrosome and the mitotic spindle poles. Enhanced recruitment to the mitotic spindle poles requires microtubules and interaction with KATNB1 (By similarity). Localizes within the cytoplasm, partially overlapping with microtubules, in interphase and to the mitotic spindle and spindle poles during mitosis (By similarity). {ECO:0000250|UniProtKB:O75449, ECO:0000255|HAMAP-Rule:MF_03023}. SUBUNIT: Can homooligomerize into hexameric rings, which may be promoted by interaction with microtubules. Interacts with KATNB1, which may serve as a targeting subunit (By similarity). Interacts with ASPM; the katanin complex formation KATNA1:KATNB1 is required for the association of ASPM (PubMed:28436967). Interacts with dynein and NDEL1. Associates with the E3 ligase complex containing DYRK2, EDD/UBR5, DDB1 and DCAF1 proteins (EDVP complex). Interacts with KLHL42 (via the kelch domains). Interacts with CUL3; the interaction is enhanced by KLHL42 (By similarity). Interacts with KATNB1 and KATNBL1 (By similarity). Interacts with CAMSAP2 and CAMSAP3; leading to regulate the length of CAMSAP-decorated microtubule stretches (By similarity). {ECO:0000250|UniProtKB:O75449, ECO:0000255|HAMAP-Rule:MF_03023, ECO:0000269|PubMed:28436967}. DOMAIN: The N-terminus is sufficient for interaction with microtubules, although high affinity binding to microtubules also requires an intact C-terminal domain and ATP, which promotes oligomerization. {ECO:0000255|HAMAP-Rule:MF_03023}. +P11438 LAMP1_MOUSE Lysosome-associated membrane glycoprotein 1 (LAMP-1) (Lysosome-associated membrane protein 1) (120 kDa lysosomal membrane glycoprotein) (CD107 antigen-like family member A) (LGP-120) (Lysosomal membrane glycoprotein A) (LGP-A) (P2B) (CD antigen CD107a) 406 43,865 Beta strand (14); Chain (1); Disulfide bond (4); Glycosylation (18); Helix (1); Region (3); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 371 394 Helical. {ECO:0000255|PROSITE-ProRule:PRU00740}. TOPO_DOM 25 370 Lumenal. {ECO:0000255}.; TOPO_DOM 395 406 Cytoplasmic. {ECO:0000255|PROSITE-ProRule:PRU00740}. FUNCTION: Presents carbohydrate ligands to selectins. Also implicated in tumor cell metastasis. PTM: O- and N-glycosylated; some of the N-glycans attached to LAMP-1 are polylactosaminoglycans. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P05300}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P11279}. Endosome membrane {ECO:0000250|UniProtKB:P11279}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P11279}. Lysosome membrane {ECO:0000250|UniProtKB:P11279}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P11279}. Late endosome {ECO:0000250|UniProtKB:P11279}. Note=This protein shuttles between lysosomes, endosomes, and the plasma membrane. Colocalizes with OSBPL1A at the late endosome. {ECO:0000250|UniProtKB:P05300, ECO:0000250|UniProtKB:P11279}. +Q61029 LAP2B_MOUSE Lamina-associated polypeptide 2, isoforms beta/delta/epsilon/gamma (Thymopoietin isoforms beta/delta/epsilon/gamma) (TP beta/delta/epsilon/gamma) 452 50,373 Alternative sequence (3); Chain (1); Cross-link (1); Domain (2); Modified residue (38); Region (5); Sequence conflict (8); Topological domain (1); Transmembrane (1) TRANSMEM 410 430 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 431 452 Lumenal. {ECO:0000255}. FUNCTION: May help direct the assembly of the nuclear lamina and thereby help maintain the structural organization of the nuclear envelope. Possible receptor for attachment of lamin filaments to the inner nuclear membrane. May be involved in the control of initiation of DNA replication through its interaction with NAKAP95 (By similarity). {ECO:0000250}. PTM: Mitosis-specific phosphorylation specifically abolishes its binding to lamin B and chromosomes. {ECO:0000250}.; PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}. SUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Chromosome {ECO:0000250}. Note=Tightly associated with the nuclear lamina. {ECO:0000250}. SUBUNIT: Interacts with LMNB1, LMNB2, BANF1, AKAP8L, GMCL and chromosomes. {ECO:0000250}. DOMAIN: Has two structurally independent, non-interacting domains: LEM-like (also called LAP2-N or LEM-D) and LEM (also called LAP2-C or LEM-B). LEM-like binds DNA while LEM interacts with BANF1 (By similarity). {ECO:0000250}. +Q60961 LAP4A_MOUSE Lysosomal-associated transmembrane protein 4A (Golgi 4-transmembrane-spanning transporter) (Mouse transporter protein) (MTP) 233 26,858 Alternative sequence (1); Chain (1); Compositional bias (1); Modified residue (1); Transmembrane (4) TRANSMEM 29 49 Helical. {ECO:0000255}.; TRANSMEM 82 102 Helical. {ECO:0000255}.; TRANSMEM 108 128 Helical. {ECO:0000255}.; TRANSMEM 160 180 Helical. {ECO:0000255}. FUNCTION: May function in the transport of nucleosides and/or nucleoside derivatives between the cytosol and the lumen of an intracellular membrane-bound compartment. SUBCELLULAR LOCATION: Endomembrane system {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=May reside in an intracellular membrane-bound compartment. {ECO:0000305}.; SUBCELLULAR LOCATION: Isoform Short: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. DOMAIN: The C-terminal domain is necessary for retention within intracellular membranes. +Q6ZQ58 LARP1_MOUSE La-related protein 1 (La ribonucleoprotein domain family member 1) 1072 121,125 Alternative sequence (1); Chain (1); Compositional bias (1); Cross-link (4); Domain (1); Initiator methionine (1); Modified residue (36); Region (1) FUNCTION: RNA-binding protein that promotes translation of specific classes of mRNAs downstream of the mTORC1 complex. Associates with the mRNA 5'cap in an MTOR-dependent manner and associates with mRNAs containing a 5' terminal oligopyrimidine (5'TOP) motif, which is present in mRNAs encoding for ribosomal proteins and several components of the translation machinery. Associates with actively translating ribosomes via interaction with PABPC1/PABP and stimulates translation of mRNAs containing a 5'TOP, thereby regulating cell growth and proliferation. Positively regulates the replication of dengue virus (DENV). {ECO:0000250|UniProtKB:Q6PKG0}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10878606}. Cytoplasmic granule {ECO:0000250|UniProtKB:Q6PKG0}. Note=Colocalizes with RPTOR and PABPC1 in cytoplasmic granules that resemble stress granules. {ECO:0000250|UniProtKB:Q6PKG0}. SUBUNIT: Interacts with PABPC1/PABP. Associates with the mTORC1 complex via interaction with RPTOR. Interacts with EIF4E. Found in a complex with PABPC1 and RYDEN. {ECO:0000250|UniProtKB:Q6PKG0}. +Q8BWW4 LARP4_MOUSE La-related protein 4 (La ribonucleoprotein domain family member 4) 719 79,763 Chain (1); Domain (2); Modified residue (11); Region (2) FUNCTION: RNA binding protein that binds to the poly-A tract of mRNA molecules. Associates with the 40S ribosomal subunit and with polysomes. Plays a role in the regulation of mRNA translation. Plays a role in the regulation of cell morphology and cytoskeletal organization. {ECO:0000250|UniProtKB:Q71RC2}. SUBCELLULAR LOCATION: Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q71RC2}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q71RC2}. Note=Localized throughout the cytosol. Partially localized in stress granules in response to arsenite treatment. {ECO:0000250|UniProtKB:Q71RC2}. SUBUNIT: Interacts (via N-terminal region) with PABPC1. Interacts with RACK1. {ECO:0000250|UniProtKB:Q71RC2}. +Q05CL8 LARP7_MOUSE La-related protein 7 (La ribonucleoprotein domain family member 7) 570 64,802 Alternative sequence (2); Chain (1); Compositional bias (1); Cross-link (2); Domain (2); Modified residue (9); Sequence conflict (3) FUNCTION: Negative transcriptional regulator of polymerase II genes, acting by means of the 7SK RNP system. Within the 7SK RNP complex, the positive transcription elongation factor b (P-TEFb) is sequestered in an inactive form, preventing RNA polymerase II phosphorylation and subsequent transcriptional elongation. {ECO:0000250|UniProtKB:Q4G0J3}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q4G0J3}. SUBUNIT: Integral part of the 7SK RNP complex. Specifically binds to the highly conserved 3'-terminal U-rich stretch of 7SK RNA. On stimulation, remains associated with 7SK RNA, whereas P-TEFb is released from the complex. Interacts with METTL16. {ECO:0000250|UniProtKB:Q4G0J3}. +Q8BSM7 LAT3_MOUSE Large neutral amino acids transporter small subunit 3 (L-type amino acid transporter 3) (Solute carrier family 43 member 1) 564 62,644 Chain (1); Frameshift (1); Glycosylation (4); Modified residue (3); Transmembrane (12) TRANSMEM 20 40 Helical. {ECO:0000255}.; TRANSMEM 78 98 Helical. {ECO:0000255}.; TRANSMEM 105 124 Helical. {ECO:0000255}.; TRANSMEM 131 151 Helical. {ECO:0000255}.; TRANSMEM 165 185 Helical. {ECO:0000255}.; TRANSMEM 191 211 Helical. {ECO:0000255}.; TRANSMEM 303 323 Helical. {ECO:0000255}.; TRANSMEM 357 377 Helical. {ECO:0000255}.; TRANSMEM 424 444 Helical. {ECO:0000255}.; TRANSMEM 451 471 Helical. {ECO:0000255}.; TRANSMEM 490 510 Helical. {ECO:0000255}.; TRANSMEM 515 535 Helical. {ECO:0000255}. FUNCTION: Sodium-independent, high affinity transport of large neutral amino acids. Has narrower substrate selectivity compared to SLC7A5 and SLC7A8 and mainly transports branched-chain amino acids and phenylalanine (By similarity). {ECO:0000250|UniProtKB:O75387}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8CB14 LAS2_MOUSE Lung adenoma susceptibility protein 2 526 59,107 Alternative sequence (2); Chain (1); Modified residue (1); Signal peptide (1) FUNCTION: Might play a role in cell proliferation. {ECO:0000269|PubMed:19622765}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Widely expressed with highest levels in lung and spleen. Also expressed during embryonic development, at least from 7 to 17 dpc. {ECO:0000269|PubMed:19622765}. +P32067 LA_MOUSE Lupus La protein homolog (La autoantigen homolog) (La ribonucleoprotein) 415 47,756 Chain (1); Domain (2); Modified residue (8) FUNCTION: Binds to the 3' poly(U) terminus of nascent RNA polymerase III transcripts, protecting them from exonuclease digestion and facilitating their folding and maturation. PTM: Phosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Interacts with DDX15. May interact with RUFY1 (By similarity). {ECO:0000250}. +Q80ST9 LCA5_MOUSE Lebercilin (Leber congenital amaurosis 5 protein homolog) 704 80,162 Alternative sequence (2); Chain (1); Coiled coil (2); Erroneous initiation (1); Modified residue (2); Sequence conflict (2) FUNCTION: Might be involved in minus end-directed microtubule transport. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250}. SUBUNIT: Interacts with NINL. Interacts with OFD1. Interacts with FAM161A. {ECO:0000250}. TISSUE SPECIFICITY: Detected in several tissues. {ECO:0000269|PubMed:17546029}. +Q8K1G2 LBN_MOUSE Limbin 1220 137,639 Chain (1); Coiled coil (4); Erroneous initiation (1); Glycosylation (3); Mutagenesis (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 211 231 Helical. {ECO:0000255}. TOPO_DOM 30 210 Extracellular. {ECO:0000255}.; TOPO_DOM 232 1220 Cytoplasmic. {ECO:0000255}. FUNCTION: Component of the EvC complex that positively regulates ciliary Hedgehog (Hh) signaling (PubMed:21356043, PubMed:24582806). Plays a critical role in bone formation and skeletal development (PubMed:21356043). May be involved in early embryonic morphogenesis (PubMed:21356043). {ECO:0000269|PubMed:21356043, ECO:0000269|PubMed:24582806}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21356043}; Single-pass type I membrane protein {ECO:0000269|PubMed:21356043}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:21356043}. Cell projection, cilium {ECO:0000269|PubMed:21356043}. Cell projection, cilium membrane {ECO:0000269|PubMed:21356043, ECO:0000269|PubMed:24582806}. Nucleus {ECO:0000269|PubMed:21356043}. Note=The EvC complex localizes at the base of cilia in the EvC zone of primary cilia in a EFCAB7-dependent manner (PubMed:24582806). {ECO:0000269|PubMed:24582806}. SUBUNIT: Component of the EvC complex composed of EFCAB7, IQCE, EVC2 and EVC; built from two subcomplexes, EVC2:EVC and EFCAB7:IQCE (PubMed:24582806). Interacts with EVC (PubMed:21356043, PubMed:24582806). Interacts (via N-terminal end) with EFCAB7 (PubMed:24582806). Interacts (via N-terminal end) with IQCE (PubMed:24582806). {ECO:0000269|PubMed:24582806}. TISSUE SPECIFICITY: Expressed in long and cranial bones, kidney and heart. Strongly expressed in proliferating chondrocytes, osteoblasts and osteoclasts. {ECO:0000269|PubMed:12136126}. +Q61805 LBP_MOUSE Lipopolysaccharide-binding protein (LBP) 481 53,055 Beta strand (26); Chain (1); Disulfide bond (1); Glycosylation (2); Helix (8); Sequence conflict (12); Signal peptide (1); Turn (4) FUNCTION: Plays a role in the innate immune response. Binds to the lipid A moiety of bacterial lipopolysaccharides (LPS), a glycolipid present in the outer membrane of all Gram-negative bacteria (PubMed:9144073). Acts as an affinity enhancer for CD14, facilitating its association with LPS (By similarity). Promotes the release of cytokines in response to bacterial lipopolysaccharide (PubMed:24380872). {ECO:0000250|UniProtKB:P18428, ECO:0000269|PubMed:24380872, ECO:0000269|PubMed:9144073}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P18428}. Cytoplasmic granule membrane {ECO:0000250|UniProtKB:P17213}. Note=Membrane-associated in polymorphonuclear Leukocytes (PMN) granules. {ECO:0000250|UniProtKB:P17213}. SUBUNIT: When bound to LPS, interacts (via C-terminus) with soluble and membrane-bound CD14. {ECO:0000250|UniProtKB:P18428}. +Q3U9G9 LBR_MOUSE Lamin-B receptor (Integral nuclear envelope inner membrane protein) 626 71,440 Chain (1); Domain (1); Glycosylation (1); Modified residue (13); Sequence conflict (6); Topological domain (1); Transmembrane (8) TRANSMEM 222 242 Helical. {ECO:0000255}.; TRANSMEM 269 289 Helical. {ECO:0000255}.; TRANSMEM 310 330 Helical. {ECO:0000255}.; TRANSMEM 337 357 Helical. {ECO:0000255}.; TRANSMEM 427 447 Helical. {ECO:0000255}.; TRANSMEM 458 478 Helical. {ECO:0000255}.; TRANSMEM 492 512 Helical. {ECO:0000255}.; TRANSMEM 572 592 Helical. {ECO:0000255}. TOPO_DOM 1 221 Nuclear. {ECO:0000255}. FUNCTION: Anchors the lamina and the heterochromatin to the inner nuclear membrane. {ECO:0000250}. PTM: Phosphorylated by CDK1 in mitosis when the inner nuclear membrane breaks down into vesicles that dissociate from the lamina and the chromatin. It is phosphorylated by different protein kinases in interphase when the membrane is associated with these structures. Phosphorylation of LBR and HP1 proteins may be responsible for some of the alterations in chromatin organization and nuclear structure which occur at various times during the cell cycle. Phosphorylated by SRPK1. In late anaphase LBR is dephosphorylated, probably by PP1 and/or PP2A, allowing reassociation with chromatin (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts directly with CBX5. Can interact with chromodomain proteins. Interacts directly with DNA. Interaction with DNA is sequence independent with higher affinity for supercoiled and relaxed circular DNA than linear DNA (By similarity). {ECO:0000250}. DOMAIN: The Tudor domain may not recognize methylation marks, but rather bind unassembled free histone H3. {ECO:0000250}. +Q7TNG8 LDHD_MOUSE Probable D-lactate dehydrogenase, mitochondrial (DLD) (Lactate dehydrogenase D) (EC 1.1.2.4) 484 51,848 Chain (1); Domain (1); Frameshift (2); Modified residue (6); Sequence conflict (1); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:12127981}. SUBUNIT: Interacts with CSRP3. {ECO:0000269|PubMed:12127981}. TISSUE SPECIFICITY: Readily detected in liver and kidney, with a weaker signal observed in heart, skeletal muscle, stomach, brain, and lung. {ECO:0000269|PubMed:12127981}. +Q8VBZ3 CLPT1_MOUSE Cleft lip and palate transmembrane protein 1 homolog (Thymic epithelial cell surface antigen) 664 75,291 Chain (1); Frameshift (1); Glycosylation (6); Initiator methionine (1); Modified residue (2); Sequence conflict (2); Topological domain (6); Transmembrane (5) TRANSMEM 355 375 Helical. {ECO:0000255}.; TRANSMEM 391 411 Helical. {ECO:0000255}.; TRANSMEM 417 437 Helical. {ECO:0000255}.; TRANSMEM 478 498 Helical. {ECO:0000255}.; TRANSMEM 503 523 Helical. {ECO:0000255}. TOPO_DOM 2 354 Extracellular. {ECO:0000255}.; TOPO_DOM 376 390 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 412 416 Extracellular. {ECO:0000255}.; TOPO_DOM 438 477 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 499 502 Extracellular. {ECO:0000255}.; TOPO_DOM 524 664 Cytoplasmic. {ECO:0000255}. FUNCTION: May play a role in T-cell development. {ECO:0000269|PubMed:9218588}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Widely expressed. Expressed by subcapsular and outer cortical thymic cells. {ECO:0000269|PubMed:9218588}. +Q3U2J5 CMKMT_MOUSE Calmodulin-lysine N-methyltransferase (CLNMT) (CaM KMT) (EC 2.1.1.60) 323 35,887 Alternative sequence (2); Chain (1) FUNCTION: Catalyzes the trimethylation of 'Lys-116' in calmodulin. {ECO:0000250}. SUBCELLULAR LOCATION: Isoform 1: Cytoplasm {ECO:0000250|UniProtKB:Q7Z624}. Nucleus {ECO:0000250|UniProtKB:Q7Z624}.; SUBCELLULAR LOCATION: Isoform 2: Golgi apparatus {ECO:0000250|UniProtKB:Q7Z624}. SUBUNIT: Monomer. Interacts with HSP90, probably as a client (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Detected in most of the tissues examined, with the highest expression in the brain and muscle (at protein level). {ECO:0000269|PubMed:23285036}. +P97468 CML1_MOUSE Chemokine-like receptor 1 (G-protein coupled receptor DEZ) 371 41,815 Chain (1); Disulfide bond (1); Glycosylation (2); Modified residue (6); Topological domain (8); Transmembrane (7) TRANSMEM 40 62 Helical; Name=1. {ECO:0000255}.; TRANSMEM 74 95 Helical; Name=2. {ECO:0000255}.; TRANSMEM 113 133 Helical; Name=3. {ECO:0000255}.; TRANSMEM 153 174 Helical; Name=4. {ECO:0000255}.; TRANSMEM 223 243 Helical; Name=5. {ECO:0000255}.; TRANSMEM 260 280 Helical; Name=6. {ECO:0000255}.; TRANSMEM 299 318 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 39 Extracellular. {ECO:0000255}.; TOPO_DOM 63 73 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 96 112 Extracellular. {ECO:0000255}.; TOPO_DOM 134 152 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 175 222 Extracellular. {ECO:0000255}.; TOPO_DOM 244 259 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 281 298 Extracellular. {ECO:0000255}.; TOPO_DOM 319 371 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for the chemoattractant adipokine chemerin/RARRES2 and for the omega-3 fatty acid derived molecule resolvin E1. Interaction with RARRES2 induces activation of intracellular signaling molecules, such as SKY, MAPK1/3 (ERK1/2), MAPK14/P38MAPK and PI3K leading to multifunctional effects, like reduction of immune responses, enhancing of adipogenesis and angionesis. Resolvin E1 down-regulates cytokine production in macrophages by reducing the activation of MAPK1/3 (ERK1/2) and NF-kappa-B (By similarity). Positively regulates adipogenesis and adipocyte metabolism. {ECO:0000250, ECO:0000269|PubMed:15753205, ECO:0000269|PubMed:16863918, ECO:0000269|PubMed:17635925}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16863918}; Multi-pass membrane protein {ECO:0000269|PubMed:16863918}. TISSUE SPECIFICITY: Expressed in the differentiated adipocytes (at protein level). Ubiquitous. Highly expressed in adipose tissue and immature plasmacytoid dendritic cells (DCs) and at lower levels in myeloid DCs, macrophages, and NK cells. Expressed on macrophages isolated from different tissues, including peritoneal cavities, pleural cavities and spleen. {ECO:0000269|PubMed:16863918, ECO:0000269|PubMed:17635925, ECO:0000269|PubMed:17767914, ECO:0000269|PubMed:18242188, ECO:0000269|PubMed:19841182}. +Q9JIZ0 CMLO1_MOUSE Probable N-acetyltransferase CML1 (EC 2.3.1.-) (Camello-like protein 1) 222 25,014 Chain (1); Domain (1); Sequence conflict (1); Transmembrane (1) TRANSMEM 53 73 Helical. {ECO:0000255}. FUNCTION: May play a role in regulation of gastrulation. {ECO:0000269|PubMed:11397015}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. +P56480 ATPB_MOUSE ATP synthase subunit beta, mitochondrial (EC 7.1.2.2) (ATP synthase F1 subunit beta) 529 56,300 Binding site (1); Chain (1); Erroneous initiation (1); Glycosylation (1); Modified residue (19); Nucleotide binding (1); Sequence conflict (17); Transit peptide (1) FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. PTM: Acetylation of Lys-133 is observed in liver mitochondria from fasted mice but not from fed mice. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P00829}; Peripheral membrane protein {ECO:0000250|UniProtKB:P00829}; Matrix side {ECO:0000250|UniProtKB:P00829}. SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Component of an ATP synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MD and MP68 (By similarity). Interacts with PPIF (PubMed:21281446). Interacts with BCL2L1 isoform BCL-X(L); the interaction mediates the association of BCL2L1 isoform BCL-X(L) with the mitochondrial membrane F(1)F(0) ATP synthase and enhances neurons metabolic efficency (By similarity). Interacts with CLN5 and PPT1 (PubMed:19941651). {ECO:0000250|UniProtKB:P00829, ECO:0000250|UniProtKB:P10719, ECO:0000269|PubMed:19941651, ECO:0000269|PubMed:21281446}. +P53996 CNBP_MOUSE Cellular nucleic acid-binding protein (CNBP) (Zinc finger protein 9) 178 19,592 Alternative sequence (2); Chain (1); Compositional bias (1); Initiator methionine (1); Modified residue (10); Sequence conflict (4); Zinc finger (7) FUNCTION: Single-stranded DNA-binding protein, with specificity to the sterol regulatory element (SRE). Involved in sterol-mediated repression. PTM: Arginine methylation by PRMT1 in the Arg/Gly-rich region impedes RNA binding. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Endoplasmic reticulum. TISSUE SPECIFICITY: Present in all tissues examined. +Q8C156 CND2_MOUSE Condensin complex subunit 2 (Barren homolog protein 1) (Chromosome-associated protein H) (mCAP-H) (Non-SMC condensin I complex subunit H) (XCAP-H homolog) 731 82,303 Chain (1); Cross-link (1); Erroneous initiation (2); Erroneous termination (1); Modified residue (16) FUNCTION: Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases. Early in neurogenesis, may play an essential role to ensure accurate mitotic chromosome condensation in neuron stem cells, ultimately affecting neuron pool and cortex size. {ECO:0000250|UniProtKB:Q15003}. PTM: Phosphorylated by CDK1. Its phosphorylation, as well as that of NCAPD2 and NCAPG subunits, activates the condensin complex and is required for chromosome condensation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Chromosome {ECO:0000250}. Note=In interphase cells, the majority of the condensin complex is found in the cytoplasm, while a minority of the complex is associated with chromatin. A subpopulation of the complex however remains associated with chromosome foci in interphase cells. During mitosis, most of the condensin complex is associated with the chromatin. At the onset of prophase, the regulatory subunits of the complex are phosphorylated by CDK1, leading to condensin's association with chromosome arms and to chromosome condensation. Dissociation from chromosomes is observed in late telophase (By similarity). {ECO:0000250}. SUBUNIT: Component of the condensin complex, which contains the SMC2 and SMC4 heterodimer, and three non SMC subunits that probably regulate the complex: NCAPH/BRRN1, NCAPD2/CAPD2 and NCAPG. {ECO:0000250}. +Q63870 CO7A1_MOUSE Collagen alpha-1(VII) chain (Long-chain collagen) (LC collagen) 2944 295,232 Chain (1); Disulfide bond (6); Domain (12); Glycosylation (3); Modified residue (9); Motif (5); Region (4); Sequence conflict (3); Signal peptide (1); Site (1) FUNCTION: Stratified squamous epithelial basement membrane protein that forms anchoring fibrils which may contribute to epithelial basement membrane organization and adherence by interacting with extracellular matrix (ECM) proteins such as type IV collagen. {ECO:0000250|UniProtKB:Q02388, ECO:0000269|PubMed:10523500}. PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. {ECO:0000305}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000250}. SUBUNIT: Homotrimer. Interacts with MIA3/TANGO1; facilitating its loading into transport carriers and subsequent secretion (By similarity). {ECO:0000250}. +Q00780 CO8A1_MOUSE Collagen alpha-1(VIII) chain [Cleaved into: Vastatin] 744 73,607 Beta strand (8); Chain (2); Domain (1); Helix (1); Region (3); Sequence conflict (11); Signal peptide (1); Turn (1) FUNCTION: Macromolecular component of the subendothelium. Major component of the Descemet's membrane (basement membrane) of corneal endothelial cells. Also component of the endothelia of blood vessels. Necessary for migration and proliferation of vascular smooth muscle cells and thus, has a potential role in the maintenance of vessel wall integrity and structure, in particular in atherogenesis. {ECO:0000269|PubMed:15063777, ECO:0000269|PubMed:16269661, ECO:0000269|PubMed:19401424}.; FUNCTION: Vastatin, the C-terminal fragment comprising the NC1 domain, inhibits aortic endothelial cell proliferation and causes cell apoptosis. {ECO:0000250}. PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.; PTM: Proteolytically cleaved by neutrophil elastase, in vitro. Proteolytic processing produces the C-terminal NC1 domain fragment, vastatin (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane. SUBUNIT: Homotrimers, or heterotrimers in association with alpha 2(VIII) type collagens. Four homotrimers can form a tetrahedron stabilized by central interacting C-terminal NC1 trimers (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: High levels in calvarium, eye and skin of newborn mice; also in various epithelial, endothelial and mesenchymal cells. {ECO:0000269|PubMed:15063777, ECO:0000269|PubMed:19401424}. +Q8BH35 CO8B_MOUSE Complement component C8 beta chain (Complement component 8 subunit beta) 589 66,229 Alternative sequence (1); Chain (1); Disulfide bond (12); Domain (5); Glycosylation (6); Modified residue (1); Natural variant (11); Propeptide (1); Signal peptide (1) FUNCTION: Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Heterotrimer of 3 chains: alpha, beta and gamma. The alpha and gamma chains are disulfide bonded. Component of the membrane attack complex (MAC). MAC assembly is initiated by proteolytic cleavage of C5 into C5a and C5b. C5b sequentially binds C6, C7, C8 and multiple copies of the pore-forming subunit C9 (By similarity). {ECO:0000250}. +Q8VCG4 CO8G_MOUSE Complement component C8 gamma chain 202 22,508 Chain (1); Disulfide bond (2); Glycosylation (3); Modified residue (1); Signal peptide (1) FUNCTION: C8 is a constituent of the membrane attack complex. C8 binds to the C5B-7 complex, forming the C5B-8 complex. C5-B8 binds C9 and acts as a catalyst in the polymerization of C9. The gamma subunit seems to be able to bind retinol (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: C8 is composed of three chains: alpha, beta and gamma. The alpha and gamma chains are disulfide bonded (By similarity). {ECO:0000250}. +Q05722 CO9A1_MOUSE Collagen alpha-1(IX) chain 921 92,092 Alternative sequence (2); Chain (1); Disulfide bond (4); Domain (10); Metal binding (3); Region (7); Sequence conflict (9); Signal peptide (1) FUNCTION: Structural component of hyaline cartilage and vitreous of the eye. PTM: Covalently linked to the telopeptides of type II collagen by lysine-derived cross-links.; PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. SUBUNIT: Heterotrimer of an alpha 1(IX), an alpha 2(IX) and an alpha 3(IX) chain. DOMAIN: Each subunit is composed of three triple-helical domains interspersed with non-collagenous domains. The globular domain at the N-terminus of type IX collagen molecules represents the NC4 domain which may participate in electrostatic interactions with polyanionic glycosaminoglycans in cartilage. +Q07643 CO9A2_MOUSE Collagen alpha-2(IX) chain 688 65,321 Chain (1); Disulfide bond (2); Glycosylation (1); Natural variant (3); Region (8); Signal peptide (1) FUNCTION: Structural component of hyaline cartilage and vitreous of the eye. PTM: Covalently linked to the telopeptides of type II collagen by lysine-derived cross-links.; PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. SUBUNIT: Heterotrimer of an alpha 1(IX), an alpha 2(IX) and an alpha 3(IX) chain. +P06683 CO9_MOUSE Complement component C9 548 62,002 Beta strand (21); Chain (1); Disulfide bond (11); Domain (4); Erroneous initiation (1); Glycosylation (3); Helix (14); Sequence conflict (8); Signal peptide (1); Transmembrane (2); Turn (3) TRANSMEM 312 328 Beta stranded. {ECO:0000255}.; TRANSMEM 333 352 Beta stranded. {ECO:0000255}. FUNCTION: Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells. C9 is the pore-forming subunit of the MAC. {ECO:0000250|UniProtKB:P02748}. PTM: Initially, positions and connectivity of disulfide bonds were based on peptide sequencing done for the human protein. The high-resolution crystal structure for the mouse protein corrected the positions and connectivities of some disulfide bonds (PubMed:30111885). The distance between Cys-55 and Cys-92 in the monomeric mouse protein precludes formation of a disulfide bond, contrary to what is seen in the structure of the human polymeric form of the protein (Probable). {ECO:0000269|PubMed:30111885, ECO:0000305|PubMed:30111885}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02748}. Target cell membrane {ECO:0000250|UniProtKB:P02748}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P02748}. Note=Secreted as soluble monomer. Oligomerizes at target membranes, forming a pre-pore. A conformation change then leads to the formation of a 100 Angstrom diameter pore. {ECO:0000250|UniProtKB:P02748}. SUBUNIT: Component of the membrane attack complex (MAC). MAC assembly is initiated by proteolytic cleavage of C5 into C5a and C5b. C5b binds sequentially C6, C7, C8 and multiple copies of the pore-forming subunit C9. About 20 C9 chains oligomerize to give rise to a huge beta-barrel that forms a 100 Angstrom diameter pore in target membranes. {ECO:0000250|UniProtKB:P02748}. +Q91VR2 ATPG_MOUSE ATP synthase subunit gamma, mitochondrial (ATP synthase F1 subunit gamma) (F-ATPase gamma subunit) 298 32,886 Chain (1); Modified residue (11); Transit peptide (1) FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha(3)beta(3). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. {ECO:0000250|UniProtKB:P05631}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P05631}; Peripheral membrane protein {ECO:0000250|UniProtKB:P05631}; Matrix side {ECO:0000250|UniProtKB:P05631}. SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Component of an ATP synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MD and MP68 (By similarity). {ECO:0000250|UniProtKB:P05631}. +P56135 ATPK_MOUSE ATP synthase subunit f, mitochondrial (ATP synthase membrane subunit f) 88 10,344 Chain (1); Initiator methionine (1); Modified residue (3); Transmembrane (1) TRANSMEM 57 76 Helical. {ECO:0000255}. FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane. SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(0) seems to have nine subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L). Component of an ATP synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MD and MP68 (By similarity). {ECO:0000250}. +Q3UMF0 COBL1_MOUSE Cordon-bleu protein-like 1 (Cobl-related protein 1) 1273 137,382 Alternative sequence (3); Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (2); Frameshift (1); Modified residue (31); Motif (2); Sequence conflict (24) TISSUE SPECIFICITY: Detected in embryonic first branchial arc, branchial clefts and limb buds. {ECO:0000269|PubMed:14512015}. +Q8K4M5 COMD1_MOUSE COMM domain-containing protein 1 (Protein Murr1) 188 20,996 Chain (1); Domain (1); Metal binding (3); Region (2); Sequence conflict (1) FUNCTION: Proposed scaffold protein that is implicated in diverse physiological processes and whose function may be in part linked to its ability to regulate ubiquitination of specific cellular proteins. Can modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes by displacing CAND1; in vitro promotes CRL E3 activity and dissociates CAND1 from CUL1 and CUL2. Promotes ubiquitination of NF-kappa-B subunit RELA and its subsequent proteasomal degradation. Down-regulates NF-kappa-B activity. Involved in the regulation of membrane expression and ubiquitination of SLC12A2. Modulates Na(+) transport in epithelial cells by regulation of apical cell surface expression of amiloride-sensitive sodium channel (ENaC) subunits and by promoting their ubiquitination presumably involving NEDD4L. Promotes the localization of SCNN1D to recycling endosomes. Promotes CFTR cell surface expression through regulation of its ubiquitination. Down-regulates SOD1 activity by interfering with its homodimerization. Plays a role in copper ion homeostasis. Involved in copper-dependent ATP7A trafficking between the trans-Golgi network and vesicles in the cell periphery; the function is proposed to depend on its association within the CCC complex and cooperation with the WASH complex on early endosomes. Can bind one copper ion per monomer. May function to facilitate biliary copper excretion within hepatocytes. Binds to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Involved in the regulation of HIF1A-mediated transcription; competes with ARNT/Hif-1-beta for binding to HIF1A resulting in decreased DNA binding and impaired transcriptional activation by HIF-1. Negatively regulates neuroblastoma G1/S phase cell cycle progression and cell proliferation by stimulating ubiquitination of NF-kappa-B subunit RELA and NF-kappa-B degradation in a FAM107A- and actin-dependent manner. {ECO:0000250|UniProtKB:Q8N668}. PTM: Ubiquitinated; undergoes both 'Lys-63'- and 'Lys-48'-linked polyubiquitination. Ubiquitinated by XIAP, leading to its proteasomal degradation (By similarity). {ECO:0000250|UniProtKB:Q8N668}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8N668}. Cytoplasm {ECO:0000250|UniProtKB:Q8N668}. Endosome membrane {ECO:0000250|UniProtKB:Q8N668}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q8N668}. Early endosome {ECO:0000250|UniProtKB:Q8N668}. Recycling endosome {ECO:0000250|UniProtKB:Q8N668}. Note=Shuttles between nucleus and cytosol. Detected in perinuclear foci that may be aggresomes containing misfolded, ubiquitinated proteins (By similarity). {ECO:0000250|UniProtKB:Q8N668}. SUBUNIT: Monomer, homodimer. Can form heterodimers with other COMM domain-containing proteins but only certain combinations may exist in vivo. Interacts (via COMM domain) with COMMD2, COMMD3, COMMD4, COMMD5, COMMD6, COMMD7, COMMD8 and COMMD10 (via COMM domain). Identified in a complex with an E3 ubiquitin ligase complex composed of TCEB1/elongin C, CUL2, SOCS1 and RBX1; in the complex interacts directly with SOCS1 and CUL2. Interacts directly with ATP7B (via the N-terminal region). Interacts with CCS, CDKN2A, RELA, REL, RELB, NFKB1/p105, NFKB2/p100, NFKBIB, SCNN1D, SCNN1B, CFTR, CLU, SGK1, AKT1, CUL1, CUL2, CUL3, CUL4A, CUL4B, CUL5, CUL7, HIF1A. Identified in a complex with NF-kappa-B. Interacts directly with SLC12A2. Interacts with CCDC22, CCDC93 and C16orf62 homolog; proposed to be a component of the CCC (COMMD/CCDC22/CCDC93) complex which contains at least COMMD1 (and possibly other COMM domain-containing proteins), CCDC22, CCDC93 and C16orf62 homolog. Interacts with ATP7A. Interacts with FAM107A; this interaction stabilizes COMMD1 in the nucleus (By similarity). {ECO:0000250|UniProtKB:Q8N668}. +Q8BXC6 COMD2_MOUSE COMM domain-containing protein 2 199 22,848 Chain (1); Domain (1); Sequence conflict (1) FUNCTION: May modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes. May down-regulate activation of NF-kappa-B. {ECO:0000250|UniProtKB:Q86X83}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q86X83}. SUBUNIT: Interacts (via COMM domain) with COMMD1 (via COMM domain). Interacts with RELA, RELB, NFKB1/p105, NFKB2/p100. Interacts with CCDC22, CCDC93, SCNN1B, CUL3, CUL4B, CUL5, CUL7. {ECO:0000250|UniProtKB:Q86X83}. +Q63829 COMD3_MOUSE COMM domain-containing protein 3 (Bmi-1 upstream gene protein) (Bup protein) 195 22,037 Chain (1); Domain (1) FUNCTION: May modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes. May down-regulate activation of NF-kappa-B. Modulates Na(+) transport in epithelial cells by regulation of apical cell surface expression of amiloride-sensitive sodium channel (ENaC) subunits. {ECO:0000250|UniProtKB:Q9UBI1}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UBI1}. Nucleus {ECO:0000250|UniProtKB:Q9UBI1}. SUBUNIT: Interacts (via COMM domain) with COMMD1 (via COMM domain). Interacts with NFKB1/p105. Interacts with CCDC22, CCDC93, SCNN1B, CUL3, CUL4A, CUL4B, CUL5. {ECO:0000250|UniProtKB:Q9UBI1}. +Q9CQ02 COMD4_MOUSE COMM domain-containing protein 4 199 21,860 Chain (1); Domain (1) FUNCTION: May modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes. Down-regulates activation of NF-kappa-B. {ECO:0000250|UniProtKB:Q9H0A8}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H0A8}. Nucleus {ECO:0000250|UniProtKB:Q9H0A8}. SUBUNIT: Interacts (via COMM domain) with COMMD1 (via COMM domain). Interacts with RELA, RELB, NFKB1/p105. Interacts with CCDC22, CCDC93, SCNN1B, CUL2, CUL3, CUL4A, CUL5, CUL7. {ECO:0000250|UniProtKB:Q9H0A8}. +Q8R395 COMD5_MOUSE COMM domain-containing protein 5 224 24,493 Chain (1); Domain (1); Initiator methionine (1); Modified residue (1); Sequence conflict (1) FUNCTION: May modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes. Negatively regulates cell proliferation. Negatively regulates cell cycle G2/M phase transition probably by transactivating p21/CDKN1A through the p53/TP53-independent signaling pathway. Involved in kidney proximal tubule morphogenesis. Down-regulates activation of NF-kappa-B. {ECO:0000250|UniProtKB:Q9ERR2, ECO:0000250|UniProtKB:Q9GZQ3}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9GZQ3}. Cytoplasm {ECO:0000250|UniProtKB:Q9GZQ3}. SUBUNIT: Interacts (via COMM domain) with COMMD1 (via COMM domain). Interacts with RELA, RELB, NFKB1/p105. Interacts with CCDC22, CCDC93, SCNN1B, CUL2, CUL3, CUL4A, CUL4B, CUL7. {ECO:0000250|UniProtKB:Q9GZQ3}. +Q8BG94 COMD7_MOUSE COMM domain-containing protein 7 200 22,652 Chain (1); Domain (1); Erroneous initiation (1) FUNCTION: May modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes. Associates with the NF-kappa-B complex and suppresses its transcriptional activity. {ECO:0000250|UniProtKB:Q86VX2}. SUBCELLULAR LOCATION: Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q86VX2}. SUBUNIT: Interacts (via COMM domain) with COMMD1 (via COMM domain). Interacts with RELA. Interacts with CCDC22, CCDC93, SCNN1B, CUL7. {ECO:0000250|UniProtKB:Q86VX2}. +Q9Z0F3 B2L10_MOUSE Bcl-2-like protein 10 (Bcl2-L-10) (Anti-apoptotic protein Boo) (Apoptosis regulator Bcl-B) (Bcl-2 homolog Diva) 191 22,302 Beta strand (3); Chain (1); Helix (7); Motif (2); Sequence conflict (1); Transmembrane (1); Turn (1) TRANSMEM 166 183 Helical. {ECO:0000255}. FUNCTION: Promotes cell survival. Suppresses apoptosis. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Nucleus membrane {ECO:0000250}. SUBUNIT: Binds to Bcl-2, Bcl-X and BAX. Interacts with APAF1. TISSUE SPECIFICITY: Expressed in multiple embryonic tissues. Restricted to the ovary and testis in adult mice. +O54918 B2L11_MOUSE Bcl-2-like protein 11 (Bcl2-L-11) (Bcl2-interacting mediator of cell death) 196 22,067 Alternative sequence (2); Chain (1); Helix (1); Modified residue (4); Motif (1); Mutagenesis (5) FUNCTION: Induces apoptosis and anoikis. The isoforms vary in cytotoxicity with isoform BimS being the most potent and isoform BimEL being the least potent. {ECO:0000269|PubMed:9430630}. PTM: Phosphorylation at Ser-65 by MAPK1/MAPK3 leads interaction with TRIM2 and ubiquitination, followed by proteasomal degradation (PubMed:21478148). Deubiquitination catalyzed by USP27X stabilizes the protein (PubMed:27013495). {ECO:0000269|PubMed:21478148, ECO:0000269|PubMed:27013495}.; PTM: Ubiquitination by TRIM2 following phosphorylation by MAPK1/MAPK3 leads to proteasomal degradation. Conversely, deubiquitination catalyzed by USP27X stabilizes the protein. {ECO:0000269|PubMed:21478148, ECO:0000269|PubMed:27013495}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:9430630}; Peripheral membrane protein {ECO:0000269|PubMed:9430630}. Mitochondrion {ECO:0000250}. Note=Associated with intracytoplasmic membranes. SUBUNIT: Forms heterodimers with a number of antiapoptotic Bcl-2 proteins, including MCL1, BCL2, BCL2L1 isoform Bcl-X(L), BCL2A1/BFL-1, and BCL2L2/BCLW (PubMed:16543145, PubMed:27013495, PubMed:14499110). Interacts with BAX (in vitro); this interaction may induce the conformationally active form of BAX (PubMed:14499110). Does not heterodimerize with proapoptotic proteins such as BAD, BOK or BAK. Identified in a complex containing BCL2L11, DYNLL1 and BCL2L1 isoform Bcl-X(L); BH3 integrity is required for BCL2L1-binding (PubMed:21478148, PubMed:27013495, PubMed:14499110). Interacts with YWHAZ. When phosphorylated, interacts with TRIM2; this interaction is associated with ubiquitination and degradation (PubMed:21478148). Interacts (via BH3) with MCL1; this interaction may sequester BCL2L11 and prevent its pro-apoptotic activity (PubMed:16543145, PubMed:27013495). When phosphorylated, isoform BimEL interacts with USP27X; this interaction leads to BCL2L11 deubiquitination and stabilization (PubMed:27013495). {ECO:0000269|PubMed:14499110, ECO:0000269|PubMed:16543145, ECO:0000269|PubMed:21478148, ECO:0000269|PubMed:27013495}. DOMAIN: The BH3 motif is required for the interaction with Bcl-2 proteins and cytotoxicity. {ECO:0000269|PubMed:14499110, ECO:0000269|PubMed:27013495}. TISSUE SPECIFICITY: Expressed in a number of B- and T-lymphoid cell lines. {ECO:0000269|PubMed:9430630}. +P59017 B2L13_MOUSE Bcl-2-like protein 13 (Bcl2-L-13) (Bcl-rambo) (Protein Mil1) 434 46,719 Chain (1); Compositional bias (2); Modified residue (8); Motif (4); Repeat (2); Sequence conflict (3); Transmembrane (1) TRANSMEM 409 429 Helical. {ECO:0000255}. FUNCTION: May promote the activation of caspase-3 and apoptosis. SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000305}. +Q9CPT0 B2L14_MOUSE Apoptosis facilitator Bcl-2-like protein 14 (Bcl2-L-14) 328 36,992 Chain (1); Modified residue (1); Motif (2); Sequence conflict (4) FUNCTION: Plays a role in apoptosis. PTM: Phosphorylated by MELK, leading to inhibit its pro-apoptotic function. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +Q08ED0 B2L15_MOUSE Bcl-2-like protein 15 (Bcl2-L-15) 167 18,300 Chain (1); Erroneous initiation (5); Sequence conflict (1) +Q07440 B2LA1_MOUSE Bcl-2-related protein A1 (A1-A) (Hemopoietic-specific early response protein) (Protein BFL-1) 172 19,914 Chain (1); Compositional bias (1); Helix (7); Motif (2); Turn (1) FUNCTION: Retards apoptosis induced by IL-3 deprivation. May function in the response of hemopoietic cells to external signals and in maintaining endothelial survival during infection. Can inhibit apoptosis induced by serum starvation in the mammary epithelial cell line HC11 (PubMed:11888890). {ECO:0000269|PubMed:11888890}. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Interacts directly with BCL2L11/BIM and PMAIP1 (By similarity). Interacts directly with BAK1, BID, BMF and BBC3. Interacts with BOP (By similarity). Interacts with isoform 3, isoform 4 and isoform 5 of ING4. {ECO:0000250|UniProtKB:Q16548, ECO:0000269|PubMed:11888890}. TISSUE SPECIFICITY: Expressed in hemopoietic tissues, including bone marrow, spleen and thymus. +P01887 B2MG_MOUSE Beta-2-microglobulin 119 13,779 Beta strand (11); Chain (1); Disulfide bond (1); Domain (1); Natural variant (6); Signal peptide (1); Turn (1) FUNCTION: Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Heterodimer of an alpha chain and a beta chain. Beta-2-microglobulin is the beta-chain of major histocompatibility complex class I molecules. +Q8K4G2 CONA1_MOUSE Collagen alpha-1(XXIII) chain 532 51,476 Chain (1); Domain (6); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 24 45 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 23 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 46 532 Extracellular. {ECO:0000255}. PTM: Undergoes proteolytic cleavage by furin protease to yield a 60 kDa soluble form that forms a homotrimer and exhibits a low affinity interaction with heparin. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}; Extracellular side {ECO:0000250}. SUBUNIT: Homotrimer. {ECO:0000250}. +P04919 B3AT_MOUSE Band 3 anion transport protein (Anion exchange protein 1) (AE 1) (Anion exchanger 1) (MEB3) (Solute carrier family 4 member 1) (CD antigen CD233) 929 103,136 Alternative sequence (1); Chain (1); Glycosylation (1); Intramembrane (1); Lipidation (1); Modified residue (10); Region (3); Sequence conflict (1); Topological domain (12); Transmembrane (12) INTRAMEM 857 887 Discontinuously helical. {ECO:0000250|UniProtKB:P02730}. TRANSMEM 423 446 Helical; Name=1. {ECO:0000250|UniProtKB:P02730}.; TRANSMEM 455 475 Helical; Name=2. {ECO:0000250|UniProtKB:P02730}.; TRANSMEM 479 495 Discontinuously helical; Name=3. {ECO:0000250|UniProtKB:P02730}.; TRANSMEM 505 525 Helical; Name=4. {ECO:0000250|UniProtKB:P02730}.; TRANSMEM 538 560 Helical; Name=5. {ECO:0000250|UniProtKB:P02730}.; TRANSMEM 589 609 Helical; Name=6. {ECO:0000250|UniProtKB:P02730}.; TRANSMEM 621 641 Helical; Name=7. {ECO:0000250|UniProtKB:P02730}.; TRANSMEM 682 702 Helical; Name=8. {ECO:0000250|UniProtKB:P02730}.; TRANSMEM 719 737 Helical; Name=9. {ECO:0000250|UniProtKB:P02730}.; TRANSMEM 738 755 Discontinuously helical; Name=10. {ECO:0000250|UniProtKB:P02730}.; TRANSMEM 779 799 Helical; Name=11. {ECO:0000250|UniProtKB:P02730}.; TRANSMEM 800 818 Helical; Name=12. {ECO:0000250|UniProtKB:P02730}. TOPO_DOM 1 422 Cytoplasmic. {ECO:0000250|UniProtKB:P02730}.; TOPO_DOM 447 454 Extracellular. {ECO:0000250|UniProtKB:P02730}.; TOPO_DOM 476 478 Cytoplasmic. {ECO:0000250|UniProtKB:P02730}.; TOPO_DOM 496 504 Extracellular. {ECO:0000250|UniProtKB:P02730}.; TOPO_DOM 526 537 Cytoplasmic. {ECO:0000250|UniProtKB:P02730}.; TOPO_DOM 561 588 Extracellular. {ECO:0000250|UniProtKB:P02730}.; TOPO_DOM 610 620 Cytoplasmic. {ECO:0000250|UniProtKB:P02730}.; TOPO_DOM 642 681 Extracellular. {ECO:0000250|UniProtKB:P02730}.; TOPO_DOM 703 718 Cytoplasmic. {ECO:0000250|UniProtKB:P02730}.; TOPO_DOM 756 778 Cytoplasmic. {ECO:0000250|UniProtKB:P02730}.; TOPO_DOM 819 856 Cytoplasmic. {ECO:0000250|UniProtKB:P02730}.; TOPO_DOM 888 929 Cytoplasmic. {ECO:0000250|UniProtKB:P02730}. FUNCTION: Functions both as a transporter that mediates electroneutral anion exchange across the cell membrane and as a structural protein. Major integral membrane glycoprotein of the erythrocyte membrane; required for normal flexibility and stability of the erythrocyte membrane and for normal erythrocyte shape via the interactions of its cytoplasmic domain with cytoskeletal proteins, glycolytic enzymes, and hemoglobin. Functions as a transporter that mediates the 1:1 exchange of inorganic anions across the erythrocyte membrane. Mediates chloride-bicarbonate exchange in the kidney, and is required for normal acidification of the urine. {ECO:0000250|UniProtKB:P02730}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2713407}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P02730}. Basolateral cell membrane {ECO:0000250|UniProtKB:P02730}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P02730}. Note=Detected in the erythrocyte cell membrane and on the basolateral membrane of alpha-intercalated cells in the collecting duct in the kidney. {ECO:0000250|UniProtKB:P02730}. SUBUNIT: A dimer in solution, but in its membrane environment, it exists primarily as a mixture of dimers and tetramers and spans the membrane asymmetrically. Interacts (via cytoplasmic N-terminal domain) with ANK1 (via N-terminal ANK repeats); tetramer formation is critical for ankyrin association. Interacts with STOM. Isoform 2 interacts with TMEM139. {ECO:0000250|UniProtKB:P02730}. TISSUE SPECIFICITY: Detected in erythrocytes (at protein level). {ECO:0000269|PubMed:2713407}. +Q9R1A8 COP1_MOUSE E3 ubiquitin-protein ligase COP1 (EC 2.3.2.27) (Constitutive photomorphogenesis protein 1 homolog) (mCOP1) (RING finger and WD repeat domain protein 2) (RING-type E3 ubiquitin transferase RFWD2) 733 80,441 Chain (1); Coiled coil (1); Compositional bias (1); Motif (3); Mutagenesis (5); Region (1); Repeat (7); Site (2); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Involved in JUN ubiquitination and degradation. Directly involved in p53 (TP53) ubiquitination and degradation, thereby abolishing p53-dependent transcription and apoptosis. Ubiquitinates p53 independently of MDM2 or RCHY1. Probably mediates E3 ubiquitin ligase activity by functioning as the essential RING domain subunit of larger E3 complexes. In contrast, it does not constitute the catalytic RING subunit in the DCX DET1-COP1 complex that negatively regulates JUN, the ubiquitin ligase activity being mediated by RBX1. Involved in 14-3-3 protein sigma/SFN ubiquitination and proteasomal degradation, leading to AKT activation and promotion of cell survival. Ubiquitinates MTA1 leading to its proteasomal degradation. Upon binding to TRIB1, ubiquitinates CEBPA, which lacks a canonical COP1-binding motif. {ECO:0000250|UniProtKB:Q8NHY2}. SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:10395541}. Cytoplasm {ECO:0000269|PubMed:10395541}. Note=In the nucleus, it forms nuclear speckles. SUBUNIT: Homodimer. Homodimerization is mediated by the coiled coil domain. Component of the DCX DET1-COP1 ubiquitin ligase complex at least composed of RBX1, DET1, DDB1, CUL4A and COP1. Isoform 2 does not interact with CUL4A but still binds to RBX1, suggesting that the interaction may be mediated by another cullin protein. Isoform 1 and isoform 2 interact with CUL5 but not with CUL1, CUL2 not CUL3. Interacts with bZIP transcription factors JUN, JUNB and JUND but not with FOS, ATF2 nor XBP1. Interacts with p53 (TP53). Interacts with COPS6; this interaction stabilizes RFWD2 through reducing its auto-ubiquitination and decelerating its turnover rate. Interacts with SFN; this interaction leads to SFN degradation. Interacts with p53/TP53 and MTA1. Interacts with TRIB1 (via C-terminus) and TRIB2. {ECO:0000250|UniProtKB:Q8NHY2}. DOMAIN: The RING finger domain, in addition to its role in ubiquitination, functions as a structural scaffold to bring two clusters of positive-charged residues within spatial proximity to mimic a bipartite nuclear localization signal (NLS). {ECO:0000269|PubMed:10395541}.; DOMAIN: The WD40 domain (386-731) is necessary and sufficient for TRIB1 binding. {ECO:0000250|UniProtKB:Q8NHY2}. +P59270 B3GA2_MOUSE Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 2 (EC 2.4.1.135) (Beta-1,3-glucuronyltransferase 2) (GlcAT-D) (UDP-glucuronosyltransferase S) (GlcAT-S) (Glucuronosyltransferase S) 324 37,132 Active site (1); Alternative sequence (2); Binding site (3); Chain (1); Glycosylation (2); Metal binding (1); Nucleotide binding (3); Region (1); Sequence conflict (1); Site (2); Topological domain (2); Transmembrane (1) TRANSMEM 3 23 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 2 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 24 324 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Involved in the biosynthesis of L2/HNK-1 carbohydrate epitope on both glycolipids and glycoproteins. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000305}. TISSUE SPECIFICITY: Expressed in brain, but not in liver and kidney. +P58158 B3GA3_MOUSE Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3 (EC 2.4.1.135) (Beta-1,3-glucuronyltransferase 3) (Glucuronosyltransferase I) (GlcAT-I) (UDP-GlcUA:Gal beta-1,3-Gal-R glucuronyltransferase) (GlcUAT-I) 335 37,067 Active site (1); Binding site (3); Chain (1); Disulfide bond (1); Glycosylation (1); Metal binding (1); Nucleotide binding (3); Region (1); Site (2); Topological domain (2); Transmembrane (1) TRANSMEM 8 28 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 7 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 29 335 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Glycosaminoglycans biosynthesis. Involved in forming the linkage tetrasaccharide present in heparan sulfate and chondroitin sulfate. Transfers a glucuronic acid moiety from the uridine diphosphate-glucuronic acid (UDP-GlcUA) to the common linkage region trisaccharide Gal-beta-1,3-Gal-beta-1,4-Xyl covalently bound to a Ser residue at the glycosaminylglycan attachment site of proteoglycans. Can also play a role in the biosynthesis of l2/HNK-1 carbohydrate epitope on glycoproteins. Stimulates 2-phosphoxylose phosphatase activity of PXYLP1 in presence of uridine diphosphate-glucuronic acid (UDP-GlcUA) during completion of linkage region formation. {ECO:0000250|UniProtKB:O94766}. PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:O94766}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:O94766}. Golgi apparatus, cis-Golgi network {ECO:0000250|UniProtKB:O94766}. SUBUNIT: Homodimer; disulfide-linked. Interacts with PXYLP1; the interaction increases the 2-phosphoxylose phosphatase activity of PXYLP1 during completion of linkage region formation in a B3GAT3-mediated manner. {ECO:0000250|UniProtKB:O94766}. TISSUE SPECIFICITY: Expressed in heart, aorta, bone, and also in osteoblasts. {ECO:0000269|PubMed:21763480}. +Q920V1 B3GL1_MOUSE UDP-GalNAc:beta-1,3-N-acetylgalactosaminyltransferase 1 (Beta-1,3-GalNAc-T1) (EC 2.4.1.79) (Beta-1,3-galactosyltransferase 3) (Beta-1,3-GalTase 3) (Beta3Gal-T3) (Beta3GalT3) (b3Gal-T3) (Beta-3-Gx-T3) (Brainiac 1) (Galactosylgalactosylglucosylceramide beta-D-acetyl-galactosaminyltransferase) (Globoside synthase) (UDP-N-acetylgalactosamine:globotriaosylceramide beta-1,3-N-acetylgalactosaminyltransferase) 331 39,371 Chain (1); Glycosylation (5); Natural variant (3); Topological domain (2); Transmembrane (1) TRANSMEM 21 43 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 20 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 44 331 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Transfers N-acetylgalactosamine onto globotriaosylceramide (PubMed:9417047). Plays a critical role in preimplantation stage embryonic development (PubMed:11463849). {ECO:0000269|PubMed:11463849, ECO:0000269|PubMed:9417047}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:O75752}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:O75752}. TISSUE SPECIFICITY: Detected in brain, ovary, kidney, uterus and stomach (PubMed:9417047, PubMed:11463849). In ovary, specifically expressed in follicular granulosa cells and shows particularly strong expression at later stages of follicle development (PubMed:11463849). {ECO:0000269|PubMed:11463849, ECO:0000269|PubMed:9417047}. +Q8BG28 B3GL2_MOUSE UDP-GalNAc:beta-1,3-N-acetylgalactosaminyltransferase 2 (Beta-1,3-GalNAc-T2) (EC 2.4.1.313) (Beta-1,3-N-acetylgalactosaminyltransferase II) 504 57,219 Alternative sequence (2); Chain (1); Glycosylation (2); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 4 24 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 3 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 25 504 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Beta-1,3-N-acetylgalactosaminyltransferase that synthesizes a unique carbohydrate structure, GalNAc-beta-1-3GlcNAc, on N- and O-glycans. Has no galactose nor galactosaminyl transferase activity toward any acceptor substrate. Involved in alpha-dystroglycan (DAG1) glycosylation: acts coordinately with GTDC2/POMGnT2 to synthesize a GalNAc-beta3-GlcNAc-beta-terminus at the 4-position of protein O-mannose in the biosynthesis of the phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-3-N-acetylglucosamine-beta-4-(phosphate-6-)mannose), a carbohydrate structure present in alpha-dystroglycan, which is required for binding laminin G-like domain-containing extracellular proteins with high affinity (By similarity). {ECO:0000250}. PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. TISSUE SPECIFICITY: Present in testis (at protein level). In testis, it is mainly detected in the middle layers of seminiferous tubules at stages XII to II. Strongly expressed in primary and secondary spermatocytes and early round spermatids, but not in spermatogonia, elongating or elongated spermatids, or in Leydig or Sertoli cells. {ECO:0000269|PubMed:14724282}. +Q8BHT6 B3GLT_MOUSE Beta-1,3-glucosyltransferase (Beta3Glc-T) (EC 2.4.1.-) (Beta 3-glucosyltransferase) (Beta-3-glycosyltransferase-like) 489 55,358 Alternative sequence (1); Chain (1); Glycosylation (1); Motif (1); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 2 22 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 1 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 23 489 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: O-glucosyltransferase that transfers glucose toward fucose with a beta-1,3 linkage. Specifically glucosylates O-linked fucosylglycan on TSP type-1 domains of proteins, thereby contributing to elongation of O-fucosylglycan (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU10138}; Single-pass type II membrane protein {ECO:0000250}. +Q9Z222 B3GN2_MOUSE N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2 (EC 2.4.1.149) (Beta-1,3-N-acetylglucosaminyltransferase 1) (BGnT-1) (Beta-1,3-Gn-T1) (Beta3Gn-T1) (Beta-1,3-galactosyltransferase 7) (Beta-1,3-GalTase 7) (Beta3Gal-T7) (Beta3GalT7) (b3Gal-T7) (Beta-3-Gx-T7) (UDP-Gal:beta-GlcNAc beta-1,3-galactosyltransferase 7) (UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2) (BGnT-2) (Beta-1,3-Gn-T2) (Beta-1,3-N-acetylglucosaminyltransferase 2) (Beta3Gn-T2) (UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase 7) 397 45,883 Chain (1); Glycosylation (6); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 8 28 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 7 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 29 325 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Beta-1,3-N-acetylglucosaminyltransferase involved in the synthesis of poly-N-acetyllactosamine. Catalyzes the initiation and elongation of poly-N-acetyllactosamine chains (PubMed:9892646). Probably constitutes the main polylactosamine synthase (PubMed:17890318). {ECO:0000269|PubMed:17890318, ECO:0000269|PubMed:9892646}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. SUBUNIT: Interacts with B3GNT8; this interaction greatly increases B3GNT2 catalytic activity, independently of B3GNT8 enzymatic activity. {ECO:0000269|PubMed:18826941}. TISSUE SPECIFICITY: Expressed in heart, brain, lung, kidney and testis and, to a lesser extent, in liver and skeletal muscle. No expression in spleen. {ECO:0000269|PubMed:9892646}. +Q5JCS9 B3GN3_MOUSE N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 3 (EC 2.4.1.149) (Core 1 extending beta-1,3-N-acetylglucosaminyltransferase) (EC 2.4.1.146) (Core1-beta3GlcNAcT) (UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 3) (BGnT-3) (Beta-1,3-Gn-T3) (Beta-1,3-N-acetylglucosaminyltransferase 3) (Beta3Gn-T3) 372 42,586 Chain (1); Glycosylation (3); Sequence conflict (5); Topological domain (2); Transmembrane (1) TRANSMEM 11 31 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 10 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 32 372 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Beta-1,3-N-acetylglucosaminyltransferase involved in the synthesis of poly-N-acetyllactosamine. Has activity for type 2 oligosaccharides. Also acts as a core1-1,3-N-acetylglucosaminyltransferase (Core1-beta3GlcNAcT) to form the 6-sulfo sialyl Lewis x on extended core1 O-glycans. {ECO:0000250|UniProtKB:Q9Y2A9}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. +Q1RLK6 B3GN4_MOUSE N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 4 (EC 2.4.1.149) (UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 4) (BGnT-4) (Beta-1,3-Gn-T4) (Beta-1,3-N-acetylglucosaminyltransferase 4) (Beta3Gn-T4) (EC 2.4.1.-) 350 39,873 Chain (1); Glycosylation (2); Sequence conflict (6); Topological domain (2); Transmembrane (1) TRANSMEM 5 25 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 4 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 26 350 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Beta-1,3-N-acetylglucosaminyltransferase involved in the synthesis of poly-N-acetyllactosamine. Has activity for type 2 oligosaccharides. {ECO:0000250|UniProtKB:Q9C0J1}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. +Q3USF0 B3GN6_MOUSE Acetylgalactosaminyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase (EC 2.4.1.147) (Core 3 synthase) (UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 6) (BGnT-6) (Beta-1,3-Gn-T6) (Beta-1,3-N-acetylglucosaminyltransferase 6) (Beta3Gn-T6) 391 43,951 Chain (1); Glycosylation (2); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 12 32 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 11 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 33 391 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Beta-1,3-N-acetylglucosaminyltransferase that synthesizes the core 3 structure of the O-glycan, an important precursor in the biosynthesis of mucin-type glycoproteins. Plays an important role in the synthesis of mucin-type O-glycans in digestive organs. {ECO:0000250|UniProtKB:Q6ZMB0}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. +Q9JIF7 COPB_MOUSE Coatomer subunit beta (Beta-coat protein) (Beta-COP) 953 107,066 Chain (1); Initiator methionine (1); Modified residue (2); Repeat (6); Sequence conflict (1) FUNCTION: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors. Involved in the Golgi disassembly and reassembly processes during cell cycle. Involved in autophagy by playing a role in early endosome function. Plays a role in organellar compartmentalization of secretory compartments including endoplasmic reticulum (ER)-Golgi intermediate compartment (ERGIC), Golgi, trans-Golgi network (TGN) and recycling endosomes, and in biosynthetic transport of CAV1 (By similarity). Plays a functional role in facilitating the transport of kappa-type opioid receptor mRNAs into axons and enhances translation of these proteins in cortical neurons. Required for limiting lipid storage in lipid droplets. Involved in lipid homeostasis by regulating the presence of perilipin family members PLIN2 and PLIN3 at the lipid droplet surface and promoting the association of adipocyte triglyceride lipase (PNPLA2) with the lipid droplet surface to mediate lipolysis. {ECO:0000250, ECO:0000269|PubMed:17698811, ECO:0000269|PubMed:19067489}. PTM: Proteolytically cleaved between Ser-528 and Ser-529 by CAPN8. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P23514}. Golgi apparatus membrane {ECO:0000269|PubMed:16476741, ECO:0000269|PubMed:19587158, ECO:0000269|PubMed:7593324}; Peripheral membrane protein {ECO:0000250|UniProtKB:P53618}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000269|PubMed:7593324}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell membrane {ECO:0000250|UniProtKB:P53618}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000269|PubMed:7593324}. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it (By similarity). Proteolytic cleavage by CAPN8 triggers translocation from Golgi to cytoplasm (PubMed:16476741). Found in perinuclear vesicular-tubular clusters (VTCs) and in the Golgi region where associated with vesicles, buds and rims of the Golgi stack (By similarity). Occasionally present at the trans-side of Golgi, but mainly present at the cis- Golgi side in transitional areas (TA), on so-called peripheral elements (PE) consisting of tubules and vesicles located between the cup-shaped transitional elements (TE) of the rough endoplasmic reticulum (RER) and the cis-most Golgi cisternae (By similarity). Present in cytoplasm, not associated with visible coats or membranes, with a minor fraction present on small clusters of tubules and vesicles (By similarity). Some association with high-density and low-density microsomes and mitochondria/nuclei fraction (By similarity). Very little found in plasma membrane fraction (By similarity). {ECO:0000250|UniProtKB:P23514, ECO:0000269|PubMed:16476741}. SUBUNIT: Oligomeric complex that consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits (By similarity). Interacts with CAPN8. Interacts with SCYL1 and PRKCE (By similarity). Interacts with COPG1 (By similarity). Interacts with ARF1 (myristoylated); this interaction is required for binding of COPB1 to Golgi membranes (By similarity). Interacts (via trunk domain) with ARF1 (via switch I region); the interaction is direct (By similarity). Interacts with KCNK2 (via N-terminus); this interaction increases the channel-mediated whole cell currents and promotes plasma membrane expression of KCNK2 (By similarity). Interacts with STX17 (By similarity). Interacts with TMEM115 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Predominantly expressed in the upper one-third of the oxyntic mucosa and in most regions of the pyloric mucosa (PubMed:16476741). Ubiquitiously expressed including platelet, liver, heart, spleen, lung and kidney (PubMed:11441537). {ECO:0000269|PubMed:11441537, ECO:0000269|PubMed:16476741}. +Q766D5 B4GN4_MOUSE N-acetyl-beta-glucosaminyl-glycoprotein 4-beta-N-acetylgalactosaminyltransferase 1 (NGalNAc-T1) (EC 2.4.1.244) (Beta-1,4-N-acetylgalactosaminyltransferase IV) (Beta4GalNAc-T4) (Beta4GalNAcT4) 1034 117,373 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (1); Glycosylation (2); Topological domain (2); Transmembrane (1) TRANSMEM 13 31 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 12 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 32 1034 Lumenal. {ECO:0000255}. FUNCTION: Transfers N-acetylgalactosamine (GalNAc) from UDP-GalNAc to N-acetylglucosamine-beta-benzyl with a beta-1,4-linkage to form N,N'-diacetyllactosediamine, GalNAc-beta-1,4-GlcNAc structures in N-linked glycans and probably O-linked glycans. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. +Q5XJY5 COPD_MOUSE Coatomer subunit delta (Archain) (Delta-coat protein) (Delta-COP) 511 57,229 Chain (1); Domain (1); Modified residue (7); Sequence conflict (1) FUNCTION: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. {ECO:0000250}. SUBUNIT: Oligomeric complex that consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits. {ECO:0000250}. +O89079 COPE_MOUSE Coatomer subunit epsilon (Epsilon-coat protein) (Epsilon-COP) 308 34,567 Chain (1); Modified residue (3); Sequence conflict (1) FUNCTION: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. The coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated with ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). {ECO:0000250}. PTM: Phosphorylated by PKA. {ECO:0000250}.; PTM: Polyubiquitinated by RCHY1 in the presence of androgen, leading to proteasomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. {ECO:0000250}. SUBUNIT: Oligomeric complex that consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits. +Q9R1S0 B9D1_MOUSE B9 domain-containing protein 1 (Endothelial precursor cells protein B9) 204 22,592 Chain (1); Domain (1) FUNCTION: Component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. Required for ciliogenesis and sonic hedgehog/SHH signaling. {ECO:0000269|PubMed:21725307, ECO:0000269|PubMed:21763481, ECO:0000269|PubMed:22179047}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:21725307, ECO:0000269|PubMed:22179047}. Note=Localizes at the transition zone, a region between the basal body and the ciliary axoneme. SUBUNIT: Part of the tectonic-like complex (also named B9 complex). {ECO:0000269|PubMed:21725307, ECO:0000269|PubMed:21763481, ECO:0000269|PubMed:22179047}. +Q3UK10 B9D2_MOUSE B9 domain-containing protein 2 (Stumpy) 175 19,250 Chain (1); Domain (1); Sequence conflict (1) FUNCTION: Component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. {ECO:0000269|PubMed:18287022, ECO:0000269|PubMed:22179047}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:18287022}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:18287022}. Nucleus {ECO:0000269|PubMed:18287022}. SUBUNIT: Part of the tectonic-like complex (also named B9 complex). Interacts with TUBG1. {ECO:0000269|PubMed:18287022, ECO:0000269|PubMed:21763481, ECO:0000269|PubMed:22179047}. TISSUE SPECIFICITY: Highest expression in thymus and skeletal muscle. Also expressed in spleen, kidney, lung, heart, microglia and liver. Detected in brain (at protein level). {ECO:0000269|PubMed:18287022}. +Q8VHV1 BAALC_MOUSE Brain and acute leukemia cytoplasmic protein 145 15,515 Alternative sequence (2); Chain (1); Initiator methionine (1); Lipidation (2); Region (1) FUNCTION: May play a synaptic role at the postsynaptic lipid rafts possibly through interaction with CAMK2A. {ECO:0000250|UniProtKB:Q920K5}. PTM: Palmitoylation and myristoylation target the protein to the lipid rafts. {ECO:0000250|UniProtKB:Q920K5}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15749074}. Cell junction, synapse, synaptosome {ECO:0000250|UniProtKB:Q920K5}. Membrane raft {ECO:0000250|UniProtKB:Q920K5}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250|UniProtKB:Q920K5}. Note=In neurons, localizes to postsynaptic lipid rafts (By similarity). In myocardial and skeletal muscle cells, localizes to the cytoplasm adjacent to the inner cell membrane, polarized to one end of the myocyte (PubMed:15749074). {ECO:0000250|UniProtKB:Q920K5, ECO:0000269|PubMed:15749074}. SUBUNIT: Interacts with CAMK2A. {ECO:0000250|UniProtKB:Q920K5}. TISSUE SPECIFICITY: At the mRNA level, predominantly expressed in the brain (PubMed:11707601). At the protein level, mainly expressed in muscle tissues. In skeletal muscles, expressed in cranial and facial muscles, muscles of the neck, back, thoracic wall, and thigh. Also found in the contractile myoepithelial cell layer of salivary glands. In smooth muscles, expressed in the gastric wall, uterus, urinary bladder, as well as in the muscular lining around seminiferous tubules, prostatic ducts, epididymis, vas deferens, walls of small blood vessels in the dermis, and fascial layers between muscle fibers, brain, and around the spinal cord. Strongly expressed in myocardium. High expression levels are observed in placental spongiotrophoblast and adjacent myometrium. Also expressed in bone marrow hematopoietic cells. In the mature thymus, expressed in rare scattered cells. Weakly expressed in the brain neuropil, particularly near the hippocampus, and spinal cord white matter. Not detected in skin keratinocytes or lung (at protein level) (PubMed:15749074). {ECO:0000269|PubMed:11707601, ECO:0000269|PubMed:15749074}. +Q9QXK3 COPG2_MOUSE Coatomer subunit gamma-2 (Gamma-2-coat protein) (Gamma-2-COP) 871 97,681 Alternative sequence (5); Chain (1); Modified residue (1); Repeat (6) FUNCTION: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:17360540}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. Tends to be more abundant in the trans-Golgi network compared to the cis-Golgi. {ECO:0000250}. SUBUNIT: Oligomeric complex. Binds to CDC42. Interacts with JAGN1. {ECO:0000250|UniProtKB:Q9UBF2}. +Q91X34 BAAT_MOUSE Bile acid-CoA:amino acid N-acyltransferase (BACAT) (BAT) (EC 2.3.1.65) (Glycine N-choloyltransferase) (Long-chain fatty-acyl-CoA hydrolase) (EC 3.1.2.2) 420 46,482 Active site (3); Chain (1); Frameshift (2); Modified residue (6); Sequence conflict (5) FUNCTION: Involved in bile acid metabolism. In liver hepatocytes catalyzes the second step in the conjugation of C24 bile acids (choloneates) to taurine before excretion into bile canaliculi. The major components of bile are cholic acid and chenodeoxycholic acid. In a first step the bile acids are converted to an acyl-CoA thioester, either in peroxisomes (primary bile acids deriving from the cholesterol pathway), or cytoplasmic at the endoplasmic reticulum (secondary bile acids). May catalyze the conjugation of primary or secondary bile acids, or both. The conjugation increases the detergent properties of bile acids in the intestine, which facilitates lipid and fat-soluble vitamin absorption. In turn, bile acids are deconjugated by bacteria in the intestine and are recycled back to the liver for reconjugation (secondary bile acids). May also act as an acyl-CoA thioesterase that regulates intracellular levels of free fatty acids. In vitro, catalyzes the hydrolysis of long- and very long-chain saturated acyl-CoAs to the free fatty acid and coenzyme A (CoASH), and conjugates glycine to these acyl-CoAs. {ECO:0000250|UniProtKB:Q14032}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14032}. Peroxisome {ECO:0000250|UniProtKB:Q63276}. Note=Cytoplasmic or/and peroxisomal. {ECO:0000250|UniProtKB:Q14032, ECO:0000250|UniProtKB:Q63276}. SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q14032}. TISSUE SPECIFICITY: Highly expressed in liver, kidney, gallbladder, proximal intestine and distal intestine. Weakly expressed in adrenal gland, lung, brain and muscle. {ECO:0000269|PubMed:12810727, ECO:0000269|PubMed:9215542}. +Q9WVK5 B4GT6_MOUSE Beta-1,4-galactosyltransferase 6 (Beta-1,4-GalTase 6) (Beta4Gal-T6) (b4Gal-T6) (EC 2.4.1.-) (Glucosylceramide beta-1,4-galactosyltransferase) (EC 2.4.1.274) (Lactosylceramide synthase) (LacCer synthase) (UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 6) (UDP-Gal:glucosylceramide beta-1,4-galactosyltransferase) (UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 6) 382 44,759 Binding site (3); Chain (1); Disulfide bond (2); Glycosylation (8); Metal binding (2); Region (5); Topological domain (2); Transmembrane (1) TRANSMEM 16 35 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 15 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 36 382 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. Sphingolipid metabolism. FUNCTION: Catalyzes the synthesis of lactosylceramide (LacCer) via the transfer of galactose from UDP-galactose to glucosylceramide (GlcCer) (PubMed:23882130, PubMed:30114188). LacCer is the starting point in the biosynthesis of all gangliosides (membrane-bound glycosphingolipids) which play pivotal roles in the CNS including neuronal maturation and axonal and myelin formation (PubMed:30114188). {ECO:0000269|PubMed:23882130, ECO:0000269|PubMed:30114188}. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:P15291}; Single-pass type II membrane protein. Note=Trans cisternae of Golgi stack. {ECO:0000250|UniProtKB:P15291}. TISSUE SPECIFICITY: Brain and kidney. {ECO:0000269|PubMed:23882130}. +Q9CQ13 COPRS_MOUSE Coordinator of PRMT5 and differentiation stimulator (Cooperator of PRMT5) 173 18,666 Chain (1); Modified residue (3) FUNCTION: Histone-binding protein required for histone H4 methyltransferase activity of PRMT5. Specifically required for histone H4 'Arg-3' methylation mediated by PRMT5, but not histone H3 'Arg-8' methylation, suggesting that it modulates the substrate specificity of PRMT5. Specifically interacts with the N-terminus of histone H4 but not with histone H3, suggesting that it acts by promoting the association between histone H4 and PRMT5. Involved in CCNE1 promoter repression (By similarity). Plays a role in muscle cell differentiation by modulating the recruitment of PRMT5 to the promoter of genes involved in the coordination between cell cycle exit and muscle differentiation. {ECO:0000250, ECO:0000269|PubMed:22193545}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with PRMT5. Interacts with histone H4; specifically interacts with the N-terminus of histone H4 but not with histone H3 (By similarity). Interacts with CBFB. Found in a complex with PRMT5, RUNX1 and CBFB. {ECO:0000250, ECO:0000269|PubMed:22193545}. +Q9CPU9 COPT2_MOUSE Probable low affinity copper uptake protein 2 (Copper transporter 2) (CTR2) (Solute carrier family 31 member 2) 143 16,069 Chain (1); Modified residue (2); Transmembrane (3) TRANSMEM 23 43 Helical. {ECO:0000255}.; TRANSMEM 94 114 Helical. {ECO:0000255}.; TRANSMEM 120 140 Helical. {ECO:0000255}. FUNCTION: Involved in low-affinity copper uptake. {ECO:0000305}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q8K3W0 BABA2_MOUSE BRISC and BRCA1-A complex member 2 (BRCA1-A complex subunit BRE) (BRCA1/BRCA2-containing complex subunit 45) (Brain and reproductive organ-expressed protein) 383 43,545 Alternative sequence (4); Chain (1); Modified residue (2); Region (2); Sequence caution (1); Sequence conflict (1) FUNCTION: Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). The BRCA1-A complex also possesses deubiquitinase activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. In the BRCA1-A complex, it acts as an adapter that bridges the interaction between BABAM1/NBA1 and the rest of the complex, thereby being required for the complex integrity and modulating the E3 ubiquitin ligase activity of the BRCA1-BARD1 heterodimer. Probably also plays a role as a component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin (By similarity). May regulate TNF-alpha signaling through its interactions with TNFRSF1A. {ECO:0000250, ECO:0000269|PubMed:9737713}.; FUNCTION: Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). The BRCA1-A complex also possesses deubiquitinase activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. In the BRCA1-A complex, it acts as an adapter that bridges the interaction between BABAM1/NBA1 and the rest of the complex, thereby being required for the complex integrity and modulating the E3 ubiquitin ligase activity of the BRCA1-BARD1 heterodimer. Component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates. Within the BRISC complex, acts as an adapter that bridges the interaction between BABAM1/NBA1 and the rest of the complex, thereby being required for the complex integrity. The BRISC complex is required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating NUMA1. The BRISC complex plays a role in interferon signaling via its role in the deubiquitination of the interferon receptor IFNAR1; deubiquitination increases IFNAR1 activity by enhancing its stability and cell surface expression. Down-regulates the response to bacterial lipopolysaccharide (LPS) via its role in IFNAR1 deubiquitination. May play a role in homeostasis or cellular differentiation in cells of neural, epithelial and germline origins (By similarity). May also act as a death receptor-associated anti-apoptotic protein, which inhibits the mitochondrial apoptotic pathway. May regulate TNF-alpha signaling through its interactions with TNFRSF1A; however these effects may be indirect (PubMed:9737713). {ECO:0000250|UniProtKB:Q9NXR7, ECO:0000305|PubMed:9737713}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NXR7}. Nucleus {ECO:0000250|UniProtKB:Q9NXR7}. Note=Localizes at sites of DNA damage at double-strand breaks (DSBs). {ECO:0000250|UniProtKB:Q9NXR7}. SUBUNIT: Component of the ARISC complex, at least composed of UIMC1/RAP80, ABRAXAS1, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1. Component of the BRCA1-A complex, at least composed of BRCA1, BARD1, UIMC1/RAP80, ABRAXAS1, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1. In the BRCA1-A complex, interacts directly with ABRAXAS1, BRCC3/BRCC36 and BABAM1/NBA1. Binds polyubiquitin. Component of the BRISC complex, at least composed of ABRAXAS2, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1. Identified in a complex with SHMT2 and the other subunits of the BRISC complex. Component of the BRCA1/BRCA2 containing complex (BRCC), which also contains BRCA1, BRCA2, BARD1, BRCC3/BRCC36 and RAD51. BRCC is a ubiquitin E3 ligase complex that enhances cellular survival following DNA damage. May interact with FAS and TNFRSF1A (PubMed:9737713). {ECO:0000250|UniProtKB:Q9NXR7, ECO:0000305|PubMed:9737713}. DOMAIN: Contains 2 ubiquitin-conjugating enzyme family-like (UEV-like) regions. These regions lack the critical Cys residues required for ubiquitination but retain the ability to bind ubiquitin (By similarity). {ECO:0000250}.; DOMAIN: Contains 2 ubiquitin-conjugating enzyme family-like (UEV-like) regions. These regions lack the critical Cys residues required for ubiquitination but retain the ability to bind ubiquitin. {ECO:0000250|UniProtKB:Q9NXR7}. TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver, lung, testis, germinal center B-cells and various mouse cell lines. {ECO:0000269|PubMed:11676476, ECO:0000269|PubMed:14565866}. +P61924 COPZ1_MOUSE Coatomer subunit zeta-1 (Zeta-1-coat protein) (Zeta-1 COP) 177 20,198 Chain (1); Modified residue (1) FUNCTION: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). {ECO:0000250}.; FUNCTION: The zeta subunit may be involved in regulating the coat assembly and, hence, the rate of biosynthetic protein transport due to its association-dissociation properties with the coatomer complex. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. {ECO:0000250}. SUBUNIT: Oligomeric complex that consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits. {ECO:0000250}. +P97302 BACH1_MOUSE Transcription regulator protein BACH1 (BTB and CNC homolog 1) 739 81,374 Beta strand (3); Chain (1); Domain (2); Helix (7); Modified residue (2); Region (2); Turn (1) FUNCTION: Transcriptional regulator that acts as repressor or activator, depending on the context (PubMed:8887638, PubMed:19170764). Binds to NF-E2 DNA binding sites (PubMed:8887638, PubMed:19170764). Play important roles in coordinating transcription activation and repression by MAFK (PubMed:8887638). Together with MAF, represses the transcription of genes under the control of the NFE2L2 oxidative stress pathway (By similarity). {ECO:0000250|UniProtKB:O14867, ECO:0000269|PubMed:19170764, ECO:0000269|PubMed:8887638}. PTM: Ubiquitinated by the SCF(FBXL17) complex, leading to its degradation by the proteasome. {ECO:0000250|UniProtKB:O14867}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:8887638}. SUBUNIT: Heterodimer of BACH1 and MAFK. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:8887638}. +Q8BMS4 COQ3_MOUSE Ubiquinone biosynthesis O-methyltransferase, mitochondrial (3-demethylubiquinol 3-O-methyltransferase) (EC 2.1.1.64) (Polyprenyldihydroxybenzoate methyltransferase) (EC 2.1.1.114) 370 40,957 Binding site (4); Chain (1); Erroneous initiation (1); Modified residue (3); Sequence conflict (1); Transit peptide (1) Cofactor biosynthesis; ubiquinone biosynthesis. FUNCTION: O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway. {ECO:0000255|HAMAP-Rule:MF_03190}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03190}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03190}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03190}. SUBUNIT: Component of a multi-subunit COQ enzyme complex, composed of at least COQ3, COQ4, COQ5, COQ6, COQ7 and COQ9. {ECO:0000255|HAMAP-Rule:MF_03190}. +Q9JLV1 BAG3_MOUSE BAG family molecular chaperone regulator 3 (BAG-3) (Bcl-2-associated athanogene 3) (Bcl-2-binding protein Bis) 577 61,860 Beta strand (2); Chain (1); Compositional bias (1); Cross-link (2); Domain (3); Helix (3); Initiator methionine (1); Modified residue (14); Sequence conflict (3) FUNCTION: Co-chaperone for HSP70 and HSC70 chaperone proteins. Acts as a nucleotide-exchange factor (NEF) promoting the release of ADP from the HSP70 and HSC70 proteins thereby triggering client/substrate protein release. Nucleotide release is mediated via its binding to the nucleotide-binding domain (NBD) of HSPA8/HSC70 where as the substrate release is mediated via its binding to the substrate-binding domain (SBD) of HSPA8/HSC70. Has anti-apoptotic activity. Plays a role in the HSF1 nucleocytoplasmic transport. {ECO:0000250|UniProtKB:O95817}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O95817}. Cytoplasm {ECO:0000250|UniProtKB:O95817}. Note=Colocalizes with HSF1 to the nucleus upon heat stress. {ECO:0000250|UniProtKB:O95817}. SUBUNIT: Binds to the ATPase domain of HSP70/HSC70 chaperones. Interacts with BCL2. Interacts with phospholipase C-gamma proteins. Interacts with DNAJB6. Interacts (via BAG domain) with HSF1; this interaction occurs in normal and heat-shocked cells. Interacts with HSPA8 (via NBD), HSPA1A (via NBD) and HSPA1B (via NBD). Interacts (via WW domain 1) with SYNPO2 (via PPPY motif). {ECO:0000250|UniProtKB:O95817}. +Q8BGB8 COQ4_MOUSE Ubiquinone biosynthesis protein COQ4 homolog, mitochondrial (Coenzyme Q biosynthesis protein 4 homolog) 266 30,084 Chain (1); Modified residue (1); Transit peptide (1) Cofactor biosynthesis; ubiquinone biosynthesis. FUNCTION: Component of the coenzyme Q biosynthetic pathway. May play a role in organizing a multi-subunit COQ enzyme complex required for coenzyme Q biosynthesis. Required for steady-state levels of other COQ polypeptides. {ECO:0000255|HAMAP-Rule:MF_03111}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03111}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03111}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03111}. SUBUNIT: Component of a multi-subunit COQ enzyme complex, composed of at least COQ3, COQ4, COQ5, COQ6, COQ7 and COQ9. {ECO:0000255|HAMAP-Rule:MF_03111}. +Q60739 BAG1_MOUSE BAG family molecular chaperone regulator 1 (BAG-1) (Bcl-2-associated athanogene 1) 355 39,740 Alternative sequence (1); Beta strand (10); Chain (1); Domain (2); Helix (5); Region (3); Repeat (7); Sequence conflict (3); Turn (1) FUNCTION: Co-chaperone for HSP70 and HSC70 chaperone proteins (PubMed:9873016). Acts as a nucleotide-exchange factor (NEF) promoting the release of ADP from the HSP70 and HSC70 proteins thereby triggering client/substrate protein release. Nucleotide release is mediated via its binding to the nucleotide-binding domain (NBD) of HSPA8/HSC70 where as the substrate release is mediated via its binding to the substrate-binding domain (SBD) of HSPA8/HSC70. Inhibits the pro-apoptotic function of PPP1R15A, and has anti-apoptotic activity. Markedly increases the anti-cell death function of BCL2 induced by various stimuli (By similarity). {ECO:0000250|UniProtKB:Q99933, ECO:0000269|PubMed:9873016}. PTM: Ubiquitinated; mediated by SIAH1 or SIAH2 and leading to its subsequent proteasomal degradation. {ECO:0000305|PubMed:11257006}. SUBCELLULAR LOCATION: Isoform 1: Nucleus.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. SUBUNIT: Homodimer. Forms a heteromeric complex with HSP70/HSC70. Binds to the ATPase domain of HSP/HSC70 chaperones. Interacts with NR3C1. Interacts with the N-terminal region of STK19. Interacts with PPP1R15A. Interacts with BCL2 in an ATP-dependent manner. Interacts with SIAH1, HSPA8 (via NBD), HSPA1A (via NBD) and HSPA1B (via NBD) (By similarity). Interacts with SIAH2 (PubMed:11257006). {ECO:0000250|UniProtKB:Q99933, ECO:0000269|PubMed:11257006}. TISSUE SPECIFICITY: Isoform 2 is expressed in the heart, lung, kidney and spinal cord. Isoform 1 and isoform 2 are expressed in hematopoietic cell lines. The levels of isoform 2 are relatively constant in all the cell lines examined while the levels of isoform 1 are more variable (at protein level). Isoform 1 is expressed in the lung and kidney. Isoform 2 is expressed in various tissues, with highest levels in testis and stomach. {ECO:0000269|PubMed:9396724, ECO:0000269|PubMed:9679980}. +Q9Z1R2 BAG6_MOUSE Large proline-rich protein BAG6 (BAG family molecular chaperone regulator 6) (BCL2-associated athanogene 6) (BAG-6) (HLA-B-associated transcript 3) (Protein Scythe) 1154 121,037 Chain (1); Compositional bias (3); Domain (1); Modified residue (8); Motif (1); Region (4); Repeat (4); Sequence conflict (2); Site (1) FUNCTION: ATP-independent molecular chaperone preventing the aggregation of misfolded and hydrophobic patches-containing proteins (PubMed:18056262, PubMed:18678708, PubMed:20713601). Functions as part of a cytosolic protein quality control complex, the BAG6/BAT3 complex, which maintains these client proteins in a soluble state and participates to their proper delivery to the endoplasmic reticulum or alternatively can promote their sorting to the proteasome where they undergo degradation (PubMed:20713601). The BAG6/BAT3 complex is involved in the post-translational delivery of tail-anchored/type II transmembrane proteins to the endoplasmic reticulum membrane. Recruited to ribosomes, it interacts with the transmembrane region of newly synthesized tail-anchored proteins and together with SGTA and ASNA1 mediates their delivery to the endoplasmic reticulum. Client proteins that cannot be properly delivered to the endoplasmic reticulum are ubiquitinated by RNF126, an E3 ubiquitin-protein ligase associated with BAG6 and are sorted to the proteasome. SGTA which prevents the recruitment of RNF126 to BAG6 may negatively regulate the ubiquitination and the proteasomal degradation of client proteins. Similarly, the BAG6/BAT3 complex also functions as a sorting platform for proteins of the secretory pathway that are mislocalized to the cytosol either delivering them to the proteasome for degradation or to the endoplasmic reticulum. The BAG6/BAT3 complex also plays a role in the endoplasmic reticulum-associated degradation (ERAD), a quality control mechanism that eliminates unwanted proteins of the endoplasmic reticulum through their retrotranslocation to the cytosol and their targeting to the proteasome. It maintains these retrotranslocated proteins in an unfolded yet soluble state condition in the cytosol to ensure their proper delivery to the proteasome (By similarity). BAG6 is also required for selective ubiquitin-mediated degradation of defective nascent chain polypeptides by the proteasome. In this context, it may participate to the production of antigenic peptides and play a role in antigen presentation in immune response (PubMed:20713601). BAG6 is also involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for proteasomal degradation. BAG6 may ensure the proper degradation of these proteins and thereby protects the endoplasmic reticulum from protein overload upon stress (By similarity). By inhibiting the polyubiquitination and subsequent proteasomal degradation of HSPA2 it may also play a role in the assembly of the synaptonemal complex during spermatogenesis (PubMed:18678708). Also positively regulates apoptosis by interacting with and stabilizing the proapoptotic factor AIFM1 (PubMed:18056262). By controlling the steady-state expression of the IGF1R receptor, indirectly regulates the insulin-like growth factor receptor signaling pathway (By similarity). {ECO:0000250|UniProtKB:P46379, ECO:0000269|PubMed:18056262, ECO:0000269|PubMed:18678708, ECO:0000269|PubMed:20713601}.; FUNCTION: Involved in DNA damage-induced apoptosis: following DNA damage, accumulates in the nucleus and forms a complex with p300/EP300, enhancing p300/EP300-mediated p53/TP53 acetylation leading to increase p53/TP53 transcriptional activity. When nuclear, may also act as a component of some chromatin regulator complex that regulates histone 3 'Lys-4' dimethylation (H3K4me2). {ECO:0000250|UniProtKB:P46379}.; FUNCTION: Released extracellularly via exosomes, it is a ligand of the natural killer/NK cells receptor NCR3 and stimulates NK cells cytotoxicity. It may thereby trigger NK cells cytotoxicity against neighboring tumor cells and immature myeloid dendritic cells (DC). {ECO:0000250|UniProtKB:P46379}.; FUNCTION: May mediate ricin-induced apoptosis. {ECO:0000250|UniProtKB:P46379}. PTM: Ricin can induce a cleavage by the caspase CASP3. The released C-terminal peptide induces apoptosis. {ECO:0000250|UniProtKB:P46379}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:18056262}. Nucleus {ECO:0000250|UniProtKB:P46379}. Secreted, exosome {ECO:0000250|UniProtKB:P46379}. Note=Normally localized in cytosol and nucleus, it can also be released extracellularly, in exosomes, by tumor and myeloid dendritic cells. {ECO:0000250|UniProtKB:P46379}. SUBUNIT: Component of the BAG6/BAT3 complex, also named BAT3 complex, at least composed of BAG6, UBL4A and GET4/TRC35. Interacts with GET4; the interaction is direct and localizes BAG6 in the cytosol (By similarity). Interacts with UBL4A; the interaction is direct and required for UBL4A protein stability (By similarity). Interacts with AIFM1 (PubMed:18056262). Interacts with HSPA2 (PubMed:18678708). Interacts with CTCFL. Interacts with p300/EP300. Interacts (via ubiquitin-like domain) with RNF126; required for BAG6-dependent ubiquitination of proteins mislocalized to the cytosol. Interacts (via ubiquitin-like domain) with SGTA; SGTA competes with RNF126 by binding the same region of BAG6, thereby promoting deubiquitination of BAG6-target proteins and rescuing them from degradation. Interacts with ricin A chain. Interacts with VCP and AMFR; both form the VCP/p97-AMFR/gp78 complex. Interacts with SYVN1. Interacts with USP13; the interaction is direct and may mediate UBL4A deubiquitination (By similarity). Interacts with ZFAND2B (PubMed:24160817, PubMed:26337389, PubMed:26876100). Interacts with KPNA2 (By similarity). {ECO:0000250|UniProtKB:P46379, ECO:0000269|PubMed:18056262, ECO:0000269|PubMed:18678708, ECO:0000269|PubMed:24160817, ECO:0000269|PubMed:26337389, ECO:0000269|PubMed:26876100}. DOMAIN: The ubiquitin-like domain mediates interaction with the E3 ubiquitin-protein ligase RNF126 which is responsible for the BAG6-dependent ubiquitination of client proteins. SGTA also binds this domain and competes with RNF126 to antagonize client protein ubiquitination and degradation. The ubiquitin-like domain also mediates the interaction with USP13. {ECO:0000250|UniProtKB:P46379}. +Q8BKX1 BAIP2_MOUSE Brain-specific angiogenesis inhibitor 1-associated protein 2 (BAI-associated protein 2) (BAI1-associated protein 2) (Insulin receptor substrate protein of 53 kDa) (IRSp53) (Insulin receptor substrate p53) (Insulin receptor tyrosine kinase 53 kDa substrate) 535 59,237 Alternative sequence (3); Chain (1); Coiled coil (1); Domain (2); Modified residue (11); Sequence conflict (3) FUNCTION: Adapter protein that links membrane-bound small G-proteins to cytoplasmic effector proteins. Necessary for CDC42-mediated reorganization of the actin cytoskeleton and for RAC1-mediated membrane ruffling. Involved in the regulation of the actin cytoskeleton by WASF family members and the Arp2/3 complex. Plays a role in neurite growth. Acts syngeristically with ENAH to promote filipodia formation. Plays a role in the reorganization of the actin cytoskeleton in response to bacterial infection. Participates in actin bundling when associated with EPS8, promoting filopodial protrusions. {ECO:0000269|PubMed:17115031}. PTM: Phosphorylated on tyrosine residues by INSR in response to insulin treatment. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell projection, filopodium {ECO:0000250}. Cell projection, ruffle {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Detected throughout the cytoplasm in the absence of specific binding partners. Detected in filopodia and close to membrane ruffles. Recruited to actin pedestals that are formed upon infection by bacteria at bacterial attachment sites (By similarity). {ECO:0000250}. SUBUNIT: Homodimer. Interacts with CDC42 and RAC1 that have been activated by GTP binding. Binds DIAPH1. Interacts with ATN1, ADGRB1, SHANK1, SHANK2, SHANK3, TIAM1, WASF1 and WASF2. Interacts with ENAH after recruitment of CDC42 (By similarity). Interacts with EPS8. {ECO:0000250, ECO:0000269|PubMed:10814512, ECO:0000269|PubMed:17115031}. DOMAIN: The IMD domain forms a coiled coil. The isolated domain can induce actin bundling and filopodia formation. In the absence of G-proteins intramolecular interaction between the IMD and the SH3 domain gives rise to an auto-inhibited state of the protein. Interaction of the IMD with RAC1 or CDC42 leads to activation (By similarity). {ECO:0000250}.; DOMAIN: The SH3 domain interacts with ATN1, ADGRB1, WASF1, WASF2, SHANK1, DIAPH1 and ENAH. {ECO:0000250}. TISSUE SPECIFICITY: Detected in liver, brain, olfactory bulb, brain cortex, caudate putamen, hypothalamus and cerebellum. {ECO:0000269|PubMed:12006592}. +Q80TT2 BAIP3_MOUSE BAI1-associated protein 3 (BAP3) (Brain-specific angiogenesis inhibitor I-associated protein 3) (Baiap3) 1134 127,075 Chain (1); Domain (4); Erroneous initiation (1); Sequence conflict (8) FUNCTION: Functions in endosome to Golgi retrograde transport. In response to calcium influx, may interact with SNARE fusion receptors and membrane phospholipids to mediate endosome fusion with the trans-Golgi network. By promoting the recycling of secretory vesicle transmembrane proteins, it indirectly controls dense-core secretory vesicle biogenesis, maturation and their ability to mediate the constitutive and regulated secretion of neurotransmitters and hormones. May regulate behavior and food intake by controlling calcium-stimulated exocytosis of neurotransmitters including NPY and serotonin and hormones like insulin (By similarity). Proposed to play a role in hypothalamic neuronal firing by modulating gamma-aminobutyric acid (GABA)ergic inhibitory neurotransmission (Probable). {ECO:0000250|UniProtKB:O94812, ECO:0000305|PubMed:23698091}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12498718}. Recycling endosome membrane {ECO:0000250|UniProtKB:O94812}; Peripheral membrane protein {ECO:0000250|UniProtKB:O94812}. Late endosome membrane {ECO:0000250|UniProtKB:O94812}; Peripheral membrane protein {ECO:0000250|UniProtKB:O94812}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:O94812}; Peripheral membrane protein {ECO:0000250|UniProtKB:O94812}. Cell membrane {ECO:0000250|UniProtKB:O94812}; Peripheral membrane protein {ECO:0000250|UniProtKB:O94812}. Note=Rapidly recruited to the plasma membrane and to Golgi structures in response to increased intracellular calcium concentration. {ECO:0000250|UniProtKB:O94812}. SUBUNIT: Interacts with ADGRB1, this interaction is direct. Interacts with endosomal SNARE proteins VAMP3, VAMP4, STX6 and STX16; this interaction is increased in the presence of calcium. {ECO:0000250|UniProtKB:O94812}. TISSUE SPECIFICITY: Prominently expressed in brain structures including hypothalamus, amygdala, stria terminalis and periaqueductal gray (at protein level). Expressed in nonneuronal tissues, including placenta, lung, pancreas, spleen, and testes. Within placenta, expression is restricted to the syncytiotrophoblasts. {ECO:0000269|PubMed:12498718, ECO:0000269|PubMed:23698091}. +Q3UHR0 BAHC1_MOUSE BAH and coiled-coil domain-containing protein 1 2643 282,520 Chain (1); Coiled coil (2); Compositional bias (2); Domain (1); Erroneous initiation (4); Frameshift (1); Modified residue (1); Sequence conflict (10) +Q497V6 BAHD1_MOUSE Bromo adjacent homology domain-containing 1 protein (BAH domain-containing protein 1) 772 83,871 Alternative sequence (1); Chain (1); Compositional bias (2); Domain (1); Erroneous gene model prediction (1); Erroneous initiation (1); Modified residue (6); Sequence conflict (2) FUNCTION: Heterochromatin protein that acts as a transcription repressor and has the ability to promote the formation of large heterochromatic domains. May act by recruiting heterochromatin proteins such as CBX5 (HP1 alpha), HDAC5 and MBD1. Represses IGF2 expression by binding to its CpG-rich P3 promoter and recruiting heterochromatin proteins (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Localizes to heterochromatin and inactive X chromosome. Colocalizes with histone H3 trimethylated at 'Lys-27' (H3K27me3) (By similarity). {ECO:0000250}. SUBUNIT: Interacts with CBX5 (HP1 alpha), HDAC5, MBD1 and SP1. {ECO:0000250}. DOMAIN: The BAH domain is required for localization at H3K27me3. {ECO:0000250}. +Q8R1S0 COQ6_MOUSE Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial (EC 1.14.13.-) (Coenzyme Q10 monooxygenase 6) 476 51,393 Chain (1); Modified residue (1); Sequence conflict (2); Transit peptide (1) Cofactor biosynthesis; ubiquinone biosynthesis. FUNCTION: FAD-dependent monooxygenase required for the C5-ring hydroxylation during ubiquinone biosynthesis. Catalyzes the hydroxylation of 3-polyprenyl-4-hydroxybenzoic acid to 3-polyprenyl-4,5-dihydroxybenzoic acid. The electrons required for the hydroxylation reaction may be funneled indirectly from NADPH via a ferredoxin/ferredoxin reductase system to COQ6. {ECO:0000255|HAMAP-Rule:MF_03193}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03193}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03193}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03193}. Golgi apparatus {ECO:0000255|HAMAP-Rule:MF_03193, ECO:0000269|PubMed:21540551}. Cell projection {ECO:0000255|HAMAP-Rule:MF_03193}. Note=Localizes to cell processes and Golgi apparatus in podocytes. {ECO:0000255|HAMAP-Rule:MF_03193}. SUBUNIT: Component of a multi-subunit COQ enzyme complex, composed of at least COQ3, COQ4, COQ5, COQ6, COQ7 and COQ9. Interacts with COQ8B and COQ7. {ECO:0000255|HAMAP-Rule:MF_03193}. TISSUE SPECIFICITY: Expressed in the kidney, in podocytes. {ECO:0000269|PubMed:21540551}. +Q9D0L6 BAMBI_MOUSE BMP and activin membrane-bound inhibitor homolog (Putative transmembrane protein NMA) 260 29,198 Chain (1); Glycosylation (1); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 153 173 Helical. {ECO:0000255}. TOPO_DOM 27 152 Extracellular. {ECO:0000255}.; TOPO_DOM 174 260 Cytoplasmic. {ECO:0000255}. FUNCTION: Negatively regulates TGF-beta signaling. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +P97478 COQ7_MOUSE 5-demethoxyubiquinone hydroxylase, mitochondrial (DMQ hydroxylase) (EC 1.14.13.-) (Timing protein clk-1 homolog) (Ubiquinone biosynthesis monooxygenase COQ7) 217 24,042 Chain (1); Metal binding (8); Region (1); Repeat (2); Transit peptide (1) Cofactor biosynthesis; ubiquinone biosynthesis. FUNCTION: Catalyzes the hydroxylation of 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2) during ubiquinone biosynthesis. Has also a structural role in the COQ enzyme complex, stabilizing other COQ polypeptides (By similarity). Involved in lifespan determination in a ubiquinone-independent manner (PubMed:19478076). {ECO:0000255|HAMAP-Rule:MF_03194, ECO:0000269|PubMed:19478076}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03194, ECO:0000269|PubMed:11387338}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03194, ECO:0000269|PubMed:11387338}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03194, ECO:0000269|PubMed:11387338}. SUBUNIT: Component of a multi-subunit COQ enzyme complex, composed of at least COQ3, COQ4, COQ5, COQ6, COQ7 and COQ9. Interacts with COQ8B and COQ6. Interacts with COQ9. {ECO:0000255|HAMAP-Rule:MF_03194}. TISSUE SPECIFICITY: Highly expressed in tissues with high energy demand such as heart, muscle, liver, and kidney. {ECO:0000269|PubMed:11511092}. +Q60936 COQ8A_MOUSE Atypical kinase COQ8A, mitochondrial (EC 2.7.-.-) (Chaperone activity of bc1 complex-like) (Chaperone-ABC1-like) (Coenzyme Q protein 8A) (aarF domain-containing protein kinase 3) 645 71,743 Active site (1); Alternative sequence (1); Binding site (4); Chain (1); Domain (1); Motif (2); Nucleotide binding (1); Sequence conflict (3); Transit peptide (1); Transmembrane (1) TRANSMEM 211 227 Helical. {ECO:0000255}. Cofactor biosynthesis; ubiquinone biosynthesis. FUNCTION: Atypical kinase involved in the biosynthesis of coenzyme Q, also named ubiquinone, an essential lipid-soluble electron transporter for aerobic cellular respiration (PubMed:27499294). Its substrate specificity is unclear: does not show any protein kinase activity (PubMed:27499294). Probably acts as a small molecule kinase, possibly a lipid kinase that phosphorylates a prenyl lipid in the ubiquinone biosynthesis pathway, as suggested by its ability to bind coenzyme Q lipid intermediates (By similarity). Shows an unusual selectivity for binding ADP over ATP (By similarity). {ECO:0000250|UniProtKB:Q8NI60, ECO:0000269|PubMed:27499294}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q8NI60}. Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8NI60, ECO:0000255}. SUBUNIT: Homodimer; homodimerizes via its transmembrane region. Interacts with the multi-subunit COQ enzyme complex, composed of at least COQ3, COQ4, COQ5, COQ6, COQ7 and COQ9. {ECO:0000250|UniProtKB:Q8NI60}. DOMAIN: Adopts an atypical protein kinase-like fold: while it adopts a core fold similar to that of well-characterized protein kinase-like domains, a number of features are positioned to inhibit the kinase activity: (1) an atypical AAAS motif in an alanine-rich (A-rich) loop that replaces the canonical glycine-rich (G-rich) nucleotide-binding loop and limits ATP binding by establishing an unusual selectivity for ADP and (2) an N-terminal domain, containing the KxGQ motif, that completely occludes the typical substrate binding pocket. Nucleotide-binding opens the substrate binding pocket and flips the active site from inside the hydrophobic core into a catalytically competent, solvent-exposed posture. {ECO:0000250|UniProtKB:Q8NI60}. TISSUE SPECIFICITY: Present in various tissues (at protein level). {ECO:0000269|PubMed:27499294}. +Q99PU7 BAP1_MOUSE Ubiquitin carboxyl-terminal hydrolase BAP1 (EC 3.4.19.12) (BRCA1-associated protein 1) (Ubiquitin C-terminal hydrolase X4) (UCH-X4) 728 80,492 Active site (2); Chain (1); Coiled coil (1); Erroneous initiation (1); Modified residue (6); Motif (2); Mutagenesis (2); Region (1); Sequence conflict (1); Site (1) FUNCTION: Deubiquitinating enzyme that plays a key role in chromatin by mediating deubiquitination of histone H2A and HCFC1. Catalytic component of the PR-DUB complex, a complex that specifically mediates deubiquitination of histone H2A monoubiquitinated at 'Lys-119' (H2AK119ub1). Does not deubiquitinate monoubiquitinated histone H2B. Acts as a regulator of cell growth by mediating deubiquitination of HCFC1 N-terminal and C-terminal chains, with some specificity toward 'Lys-48'-linked polyubiquitin chains compared to 'Lys-63'-linked polyubiquitin chains. Deubiquitination of HCFC1 does not lead to increase stability of HCFC1. Interferes with the BRCA1 and BARD1 heterodimer activity by inhibiting their ability to mediate ubiquitination and autoubiquitination. It however does not mediate deubiquitination of BRCA1 and BARD1. Able to mediate autodeubiquitination via intramolecular interactions to couteract monoubiquitination at the nuclear localization signal (NLS), thereby protecting it from cytoplasmic sequestration. Acts as a tumor suppressor (By similarity). {ECO:0000250}. PTM: Ubiquitinated: monoubiquitinated at multiple site of its nuclear localization signal (NLS) by UBE2O, leading to cytoplasmic retention. Able to mediate autodeubiquitination via intramolecular interactions to couteract cytoplasmic retention (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q92560}. Nucleus {ECO:0000250|UniProtKB:Q92560}. Note=Mainly nuclear. Binds to chromatin. Localizes to the cytoplasm when monoubiquitinated by the E2/E3 hybrid ubiquitin-protein ligase UBE2O. {ECO:0000250|UniProtKB:Q92560}. SUBUNIT: Component of the PR-DUB complex, at least composed of BAP1 and ASXL1. Interacts with BRCA1 (via the RING finger). Interacts (via HBM-like motif) with HCFC1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in mammary glands, testis and ovary. Up-regulated in mammary glands during puberty, pregnancy, and as a result of parity. {ECO:0000269|PubMed:9528852}. +Q566J8 COQ8B_MOUSE Atypical kinase COQ8B, mitochondrial (EC 2.7.-.-) (AarF domain-containing protein kinase 4) (Coenzyme Q protein 8B) 533 59,232 Active site (1); Binding site (4); Chain (1); Domain (1); Erroneous initiation (1); Motif (2); Nucleotide binding (1); Sequence conflict (2); Transmembrane (1) TRANSMEM 93 109 Helical. {ECO:0000255}. FUNCTION: Atypical kinase involved in the biosynthesis of coenzyme Q, also named ubiquinone, an essential lipid-soluble electron transporter for aerobic cellular respiration. Its substrate specificity is unclear: does not show any protein kinase activity. Probably acts as a small molecule kinase, possibly a lipid kinase that phosphorylates a prenyl lipid in the ubiquinone biosynthesis pathway. Required for podocyte migration. {ECO:0000250|UniProtKB:Q8NI60, ECO:0000250|UniProtKB:Q96D53}. SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250|UniProtKB:Q96D53}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q96D53}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q96D53}. Cell membrane {ECO:0000250|UniProtKB:Q96D53}. SUBUNIT: Homodimer; homodimerizes via its transmembrane region. Interacts with COQ6 and COQ7. Interacts with the multi-subunit COQ enzyme complex, composed of at least COQ3, COQ4, COQ5, COQ6, COQ7 and COQ9. {ECO:0000250|UniProtKB:Q96D53}. DOMAIN: Adopts an atypical protein kinase-like fold: while it adopts a core fold similar to that of well-characterized protein kinase-like domains. The KxGQ motif completely occludes the typical substrate binding pocket. Nucleotide-binding opens the substrate binding pocket and flips the active site from inside the hydrophobic core into a catalytically competent, solvent-exposed posture. {ECO:0000250|UniProtKB:Q8NI60}. +Q61334 BAP29_MOUSE B-cell receptor-associated protein 29 (BCR-associated protein 29) (Bap29) 240 27,964 Chain (1); Coiled coil (1); Motif (1); Topological domain (4); Transmembrane (3) TRANSMEM 7 27 Helical. {ECO:0000255}.; TRANSMEM 44 64 Helical. {ECO:0000255}.; TRANSMEM 104 124 Helical. {ECO:0000255}. TOPO_DOM 1 6 Lumenal. {ECO:0000255}.; TOPO_DOM 28 43 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 65 103 Lumenal. {ECO:0000255}.; TOPO_DOM 125 240 Cytoplasmic. {ECO:0000255}. FUNCTION: May play a role in anterograde transport of membrane proteins from the endoplasmic reticulum to the Golgi. May be involved in CASP8-mediated apoptosis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SUBUNIT: Homodimer and heterodimer with BCAP31. Binds CASP8 as a complex containing BCAP31, BCAP29, BCL2 and/or BCL2L1. Interacts with VAMP3, VAMP1 and membrane IgD immunoglobulins. May interact with ACTG1 and non-muscle myosin II (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in brain and testis; detected at lower levels in thymus, spleen, liver, lung and bone marrow. +Q8K1Z0 COQ9_MOUSE Ubiquinone biosynthesis protein COQ9, mitochondrial 313 35,083 Chain (1); Modified residue (2); Region (1); Sequence conflict (1); Transit peptide (1) Cofactor biosynthesis; ubiquinone biosynthesis. FUNCTION: Lipid-binding protein involved in the biosynthesis of coenzyme Q, also named ubiquinone, an essential lipid-soluble electron transporter for aerobic cellular respiration (PubMed:25339443). Binds a phospholipid of at least 10 carbons in each acyl group. May be required to present its bound-lipid to COQ7 (By similarity). {ECO:0000250|UniProtKB:O75208, ECO:0000269|PubMed:23255162, ECO:0000269|PubMed:25339443}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:18614015}. SUBUNIT: Homodimer. Interacts with COQ7. {ECO:0000250|UniProtKB:O75208}. DOMAIN: Structurally similar to the bacterial FadR protein (fatty acid metabolism regulator protein). {ECO:0000250|UniProtKB:O75208}. +Q61335 BAP31_MOUSE B-cell receptor-associated protein 31 (BCR-associated protein 31) (Bap31) (p28) 245 27,957 Chain (1); Coiled coil (1); Initiator methionine (1); Motif (1); Sequence conflict (2); Site (1); Topological domain (4); Transmembrane (3) TRANSMEM 7 27 Helical. {ECO:0000255}.; TRANSMEM 44 64 Helical. {ECO:0000255}.; TRANSMEM 103 123 Helical. {ECO:0000255}. TOPO_DOM 2 6 Lumenal. {ECO:0000255}.; TOPO_DOM 28 43 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 65 102 Lumenal. {ECO:0000255}.; TOPO_DOM 124 245 Cytoplasmic. {ECO:0000255}. FUNCTION: Functions as a chaperone protein. Is one of the most abundant endoplasmic reticulum (ER) proteins. Plays a role in the export of secreted proteins in the ER, the recognition of abnormally folded protein and their targeting to the ER associated-degradation (ERAD). Also serves as a cargo receptor for the export of transmembrane proteins. May be involved in CASP8-mediated apoptosis. {ECO:0000269|PubMed:15187134, ECO:0000269|PubMed:9396746}. PTM: Cleaved by CASP8 and other caspases. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P51572}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:P51572}; Multi-pass membrane protein {ECO:0000255}. Note=May shuttle between the ER and the intermediate compartment/cis-Golgi complex. {ECO:0000250|UniProtKB:P51572}. SUBUNIT: Homodimer and heterodimer with BCAP29. Binds CASP8 as a complex containing BCAP31, BCAP29, BCL2 and/or BCL2L1. Interacts with VAMP3, VAMP1 and membrane IgD immunoglobulins. May interact with ACTG1 and non-muscle myosin II. Interacts with HACD2 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P51572}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:8612576}. +Q9ER42 BARX1_MOUSE Homeobox protein BarH-like 1 254 27,282 Chain (1); Compositional bias (1); DNA binding (1) FUNCTION: Transcription factor, which is involved in craniofacial development, in odontogenesis and in stomach organogenesis. May have a role in the differentiation of molars from incisors. Plays a role in suppressing endodermal Wnt activity. Binds to a regulatory module of the NCAM promoter. {ECO:0000269|PubMed:15809042, ECO:0000269|PubMed:17855428}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. TISSUE SPECIFICITY: Expressed predominantly in the facial primordia, developing stomach, and proximal limbs. +O08686 BARX2_MOUSE Homeobox protein BarH-like 2 283 31,534 Chain (1); Compositional bias (1); DNA binding (1); Erroneous initiation (2); Sequence conflict (4) FUNCTION: Transcription factor. Binds optimally to the DNA consensus sequence 5'-YYTAATGRTTTTY-3'. May control the expression of neural adhesion molecules such as L1 or Ng-CAM during embryonic development of both the central and peripherical nervous system. May be involved in controlling adhesive processes in keratinizing epithelia. SUBCELLULAR LOCATION: Nucleus. TISSUE SPECIFICITY: Nervous system, particularly in the telencephalon, spinal cord, and dorsal root ganglia. +Q9WUM4 COR1C_MOUSE Coronin-1C (Coronin-3) 474 53,121 Chain (1); Coiled coil (1); Modified residue (1); Mutagenesis (3); Repeat (5); Sequence conflict (2) FUNCTION: Plays a role in directed cell migration by regulating the activation and subcellular location of RAC1 (PubMed:25074804, PubMed:25925950). Increases the presence of activated RAC1 at the leading edge of migrating cells (PubMed:25074804, PubMed:25925950). Required for normal organization of the cytoskeleton, including the actin cytoskeleton, microtubules and the vimentin intermediate filaments (PubMed:27178841). Required for normal cell proliferation, cell migration, and normal formation of lamellipodia (PubMed:27178841). Plays a role in endoplasmic reticulum-associated endosome fission: localizes to endosome membrane tubules and promotes recruitment of TMCC1, leading to recruitment of the endoplasmic reticulum to endosome tubules for fission. Endosome membrane fission of early and late endosomes is essential to separate regions destined for lysosomal degradation from carriers to be recycled to the plasma membrane (By similarity). Required for normal distribution of mitochondria within cells (PubMed:27178841). {ECO:0000250|UniProtKB:Q9ULV4, ECO:0000269|PubMed:25074804, ECO:0000269|PubMed:25925950, ECO:0000269|PubMed:27178841}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19651142, ECO:0000269|PubMed:22364218, ECO:0000269|PubMed:25074804, ECO:0000269|PubMed:25925950}; Peripheral membrane protein {ECO:0000269|PubMed:19651142, ECO:0000269|PubMed:22364218, ECO:0000269|PubMed:25074804, ECO:0000269|PubMed:25925950}; Cytoplasmic side {ECO:0000269|PubMed:19651142, ECO:0000269|PubMed:22364218, ECO:0000269|PubMed:25074804, ECO:0000269|PubMed:25925950}. Cell projection, lamellipodium {ECO:0000269|PubMed:22364218, ECO:0000269|PubMed:27178841}. Cell projection, ruffle membrane {ECO:0000269|PubMed:25074804}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19651142, ECO:0000269|PubMed:22364218, ECO:0000269|PubMed:25074804, ECO:0000269|PubMed:27178841}. Cytoplasm, cell cortex {ECO:0000269|PubMed:19651142, ECO:0000269|PubMed:22364218}. Endosome membrane {ECO:0000250|UniProtKB:Q9ULV4}. Note=Colocalizes with the actin cytoskeleton in the cytosol, and especially in the cell cortex (PubMed:19651142, PubMed:22364218, PubMed:25074804, PubMed:27178841). Colocalizes with F-actin at the leading edge of lamellipodia (PubMed:22364218). Partially colocalizes with microtubules and vimentin intermediate filaments (PubMed:27178841). Localizes to endosome membrane tubules/buds (By similarity). {ECO:0000250|UniProtKB:Q9ULV4, ECO:0000269|PubMed:19651142, ECO:0000269|PubMed:22364218, ECO:0000269|PubMed:25074804, ECO:0000269|PubMed:27178841}. SUBUNIT: Homotrimer (By similarity). Binds F-actin (PubMed:22364218). Interacts with RCC2 (PubMed:25074804). Interacts preferentially with nucleotide-free and GDP-bound RAC1 (PubMed:25074804). Interacts with VIM (via head domain) (PubMed:27178841). {ECO:0000250|UniProtKB:Q9ULV4, ECO:0000269|PubMed:22364218, ECO:0000269|PubMed:25074804, ECO:0000269|PubMed:27178841}. DOMAIN: The C-terminal coiled-coil domain is essential for cortical membrane localization and oligomerization. {ECO:0000250}. TISSUE SPECIFICITY: Detected in skeletal muscle (at protein level) (PubMed:19651142). Detected in fibroblasts (at protein level) (PubMed:27178841). Ubiquitous (PubMed:9778037). {ECO:0000269|PubMed:19651142, ECO:0000269|PubMed:27178841, ECO:0000269|PubMed:9778037}. +P18572 BASI_MOUSE Basigin (Basic immunoglobulin superfamily) (HT7 antigen) (Membrane glycoprotein gp42) (CD antigen CD147) 389 42,445 Alternative sequence (1); Chain (1); Disulfide bond (2); Domain (2); Glycosylation (3); Modified residue (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 326 349 Helical. {ECO:0000255}. TOPO_DOM 22 325 Extracellular. {ECO:0000255}.; TOPO_DOM 350 389 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays an important role in targeting the monocarboxylate transporters SLC16A1, SLC16A3, SLC16A8, SLC16A11 and SLC16A12 to the plasma membrane. Plays pivotal roles in spermatogenesis, embryo implantation, neural network formation and tumor progression. Stimulates adjacent fibroblasts to produce matrix metalloproteinases (MMPS). Seems to be a receptor for oligomannosidic glycans. In vitro, promotes outgrowth of astrocytic processes. {ECO:0000250|UniProtKB:P35613, ECO:0000269|PubMed:12558975, ECO:0000269|PubMed:12601063, ECO:0000269|PubMed:21792931}. PTM: N-glycosylated. During spermatogenesis, probably deglycosylated during epididymal transit. {ECO:0000269|PubMed:12558975, ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:19656770}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12601063}; Single-pass type I membrane protein. Melanosome {ECO:0000250|UniProtKB:P35613}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV (By similarity). In spermatozoa, localized on the principal piece of caput and in the middle piece during transit in the corpus and cauda epididymides (PubMed:11882021). {ECO:0000250|UniProtKB:P35613, ECO:0000269|PubMed:11882021}. SUBUNIT: Forms homooligomers in a cis-dependent manner on the plasma membrane. Forms a complex with MMP1 at the tumor cell surface (By similarity). Interacts with AJAP1 (By similarity). Interacts with ATP1B2, MAG and L1CAM. Interacts with SLC16A1, SLC16A7 and SLC1A3; probably a BSG dimer is associated with a monocarboxylate transporter dimer. Interacts with PPIL2; regulates BSG transport to the cell membrane. Interacts with SLC16A11 (By similarity). Interacts with SLC16A12 (By similarity). {ECO:0000250|UniProtKB:P26453, ECO:0000250|UniProtKB:P35613, ECO:0000269|PubMed:12558975, ECO:0000269|PubMed:21792931}. TISSUE SPECIFICITY: Isoform 1 is specifically expressed in retina. Isoform 2 is widely expressed, including adult organs, embryos and EC cells. Expressed in spermatozoa. {ECO:0000269|PubMed:12939332, ECO:0000269|PubMed:21792931}. +Q5QNQ9 CORA1_MOUSE Collagen alpha-1(XXVII) chain 1845 186,319 Chain (1); Disulfide bond (5); Domain (17); Glycosylation (3); Metal binding (4); Propeptide (2); Region (1); Sequence conflict (3); Signal peptide (1) FUNCTION: Plays a role during the calcification of cartilage and the transition of cartilage to bone. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793, ECO:0000269|PubMed:17693149}. Note=Found on some small banded collagen fibrils and filamentous meshworks. DOMAIN: The C-terminal propeptide, also known as COLFI domain, have crucial roles in tissue growth and repair by controlling both the intracellular assembly of procollagen molecules and the extracellular assembly of collagen fibrils. It binds a calcium ion which is essential for its function (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in cartilage, eye and ear. {ECO:0000269|PubMed:12714037}. +Q8CDM1 ATAD2_MOUSE ATPase family AAA domain-containing protein 2 (EC 3.6.1.3) 1040 117,943 Alternative sequence (4); Chain (1); Coiled coil (2); Compositional bias (2); Cross-link (2); Domain (1); Modified residue (10); Nucleotide binding (1) FUNCTION: May be a transcriptional coactivator of the nuclear receptor ESR1 required to induce the expression of a subset of estradiol target genes, such as CCND1, MYC and E2F1. May play a role in the recruitment or occupancy of CREBBP at some ESR1 target gene promoters. May be required for histone hyperacetylation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with ESR1 and NCOA3 and these interactions are enhanced by estradiol. Interacts with acetylated lysine residues on histone H1.4, H2A, H2B and H3 (in vitro) (By similarity). {ECO:0000250}. +Q06507 ATF4_MOUSE Cyclic AMP-dependent transcription factor ATF-4 (cAMP-dependent transcription factor ATF-4) (Activating transcription factor 4) (C/EBP-related ATF) (C/ATF) (Tax-responsive enhancer element-binding protein 67 homolog) (TaxREB67 homolog) 349 38,355 Chain (1); Cross-link (2); Domain (1); Erroneous initiation (1); Modified residue (6); Motif (1); Mutagenesis (6); Region (3); Sequence conflict (1) FUNCTION: Transcriptional activator. Binds the cAMP response element (CRE) (consensus: 5'-GTGACGT[AC][AG]-3'), a sequence present in many viral and cellular promoters. Binds to asymmetric CRE's as a heterodimer and to palindromic CRE's as a homodimer. Cooperates with FOXO1 in osteoblasts to regulate glucose homeostasis through suppression of beta-cell production and decrease in insulin production. Regulates the induction of DDIT3/CHOP and asparagine synthetase (ASNS) in response to ER stress. In concert with DDIT3/CHOP, activates the transcription of TRIB3 and promotes ER stress-induced neuronal apoptosis by regulating the transcriptional induction of BBC3/PUMA. Activates transcription of SIRT4. Regulates the circadian expression of the core clock component PER2 and the serotonin transporter SLC6A4. Binds in a circadian time-dependent manner to the cAMP response elements (CRE) in the SLC6A4 and PER2 promoters and periodically activates the transcription of these genes. {ECO:0000269|PubMed:15775988, ECO:0000269|PubMed:21159964, ECO:0000269|PubMed:21768648, ECO:0000269|PubMed:22298775, ECO:0000269|PubMed:22572884, ECO:0000269|PubMed:23663782, ECO:0000269|PubMed:8506317}. PTM: Ubiquitinated by SCF(BTRC) in response to mTORC1 signal, followed by proteasomal degradation and leading to down-regulate expression of SIRT4. {ECO:0000269|PubMed:23663782}.; PTM: Phosphorylated by NEK6 (By similarity). Phosphorylated on the betaTrCP degron motif at Ser-218, followed by phosphorylation at Thr-212, Ser-223, Ser-230, Ser-234 and Ser-247, promoting interaction with BTRC and ubiquitination. Phosphorylation is promoted by mTORC1. {ECO:0000250, ECO:0000269|PubMed:23663782}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19232401}. Cell membrane {ECO:0000250|UniProtKB:Q9ES19}. Nucleus {ECO:0000269|PubMed:19232401, ECO:0000269|PubMed:22974638}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P18848}. Note=Colocalizes with GABBR1 in hippocampal neuron dendritic membranes. Colocalizes with NEK6 in the centrosome (By similarity). {ECO:0000250|UniProtKB:P18848, ECO:0000250|UniProtKB:Q9ES19}. SUBUNIT: Binds DNA as a homodimer and as a heterodimer (By similarity). Interacts with CEBPB and binds DNA as a heterodimer with CEBPB (PubMed:11018027). Interacts with CEP290 (via an N-terminal region). Interacts with NEK6, DAPK2 (isoform 2) and ZIPK/DAPK3. Interacts (via its leucine zipper domain) with GABBR1 and GABBR2 (via their C-termini) (By similarity). Forms a heterodimer with TXLNG in osteoblasts (PubMed:15911876). Interacts (via its DNA binding domain) with FOXO1 (C-terminal half); the interaction occurs in osteoblasts and regulates glucose homeostasis through suppression of beta-cell proliferation and a decrease in insulin production (PubMed:22298775). Interacts with SATB2; the interaction results in enhanced DNA binding and transactivation by these transcription factors (PubMed:16751105). Interacts with DDIT3/CHOP (By similarity). Interacts with ABRAXAS2 (PubMed:22974638). {ECO:0000250|UniProtKB:P18848, ECO:0000250|UniProtKB:Q9ES19, ECO:0000269|PubMed:11018027, ECO:0000269|PubMed:15911876, ECO:0000269|PubMed:16751105, ECO:0000269|PubMed:22298775, ECO:0000269|PubMed:22974638}. DOMAIN: The BetaTrCP degron motif promotes binding to BTRC when phosphorylated. {ECO:0000269|PubMed:23663782}. +Q9CZU6 CISY_MOUSE Citrate synthase, mitochondrial (EC 2.3.3.1) (Citrate (Si)-synthase) 464 51,737 Active site (3); Chain (1); Modified residue (19); Transit peptide (1) Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 1/2. PTM: Methylated. Trimethylation at Lys-395 by CSKMT decreases citrate synthase activity. {ECO:0000250|UniProtKB:O75390}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. +Q8R0S1 ATF7_MOUSE Cyclic AMP-dependent transcription factor ATF-7 (cAMP-dependent transcription factor ATF-7) (Activating transcription factor 7) (Transcription factor ATF-A) 413 44,608 Chain (1); Compositional bias (2); Cross-link (1); Domain (1); Modified residue (3); Region (3); Zinc finger (1) FUNCTION: Plays important functions in early cell signaling. Binds the cAMP response element (CRE) (consensus: 5'-GTGACGT[AG][AG]-3'), a sequence present in many viral and cellular promoters. Activator of the NF-ELAM1/delta-A site of the E-selectin promoter. Has no intrinsic transcriptional activity, but activates transcription on formation of JUN or FOS heterodimers. Also can bind TRE promoter sequences when heterodimerized with members of the JUN family (By similarity). {ECO:0000250}. PTM: On EGF stimulation, phosphorylated first on Thr-53 allowing subsequent phosphorylation on Thr-51. This latter phosphorylation prevents sumoylation, increases binding to TAF12 and enhances transcriptional activity (By similarity). {ECO:0000250}.; PTM: Sumoylation delays nuclear localization and inhibits transactivation activity through preventing binding to TAF12. RANBP2 appears to be the specific E3 ligase (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}. Nucleus, nucleoplasm {ECO:0000250}. Note=Mainly nucleoplasmic. Restricted distribution to the perinuculear region. The sumoylated form locates to the nuclear peiphery (By similarity). {ECO:0000250}. SUBUNIT: Homodimer; binds DNA as homodimer (By similarity). Heterodimer; heterodimerizes with other members of ATF family and with JUN family members (By similarity). Interacts with JNK2; the interaction does not phosphorylate ATF7 but acts as a docking site for other ATF-associated partners such as JUN family members. Interacts (via its transactivation domain) with TAF12 the interaction potentiates the transactivation activity and is inhibited by ATF7 sumoylation. Interacts with TAF4; the interaction inhibits the TAF12-dependent transactivation. Interacts with MAPK9; the interaction does not phosphorylate ATF7 but acts as a docking site for ATF7-associated partners such as JUN (By similarity). {ECO:0000250}. +Q811C2 ATG4C_MOUSE Cysteine protease ATG4C (EC 3.4.22.-) (AUT-like 3 cysteine endopeptidase) (Autophagin-3) (Autophagy-related cysteine endopeptidase 3) (Autophagy-related protein 4 homolog C) 458 52,056 Active site (3); Chain (1); Modified residue (3); Sequence conflict (2) FUNCTION: Cysteine protease required for the cytoplasm to vacuole transport (Cvt) and autophagy. Cleaves the C-terminal amino acid of ATG8 family proteins MAP1LC3 and GABARAPL2, to reveal a C-terminal glycine. Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy. Has also an activity of delipidating enzyme for the PE-conjugated forms (By similarity). Is not essential for autophagy development under normal conditions but is required for a proper autophagic response under stressful conditions such as prolonged starvation. {ECO:0000250, ECO:0000269|PubMed:17442669}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +Q8BGV9 ATG4D_MOUSE Cysteine protease ATG4D (EC 3.4.22.-) (AUT-like 4 cysteine endopeptidase) (Autophagin-4) (Autophagy-related cysteine endopeptidase 4) (Autophagy-related protein 4 homolog D) [Cleaved into: Cysteine protease ATG4D, mitochondrial] 474 52,910 Active site (3); Chain (2); Modified residue (1); Region (1); Sequence conflict (2); Site (1) FUNCTION: Cysteine protease ATG4D: Cysteine protease required for the cytoplasm to vacuole transport (Cvt) and autophagy. Cleaves the C-terminal amino acid of ATG8 family proteins MAP1LC3 and GABARAPL2, to reveal a C-terminal glycine. Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy. Has also an activity of delipidating enzyme for the PE-conjugated forms. {ECO:0000250|UniProtKB:Q86TL0}.; FUNCTION: Cysteine protease ATG4D, mitochondrial: Plays a role as an autophagy regulator that links mitochondrial dysfunction with apoptosis. The mitochondrial import of ATG4D during cellular stress and differentiation may play important roles in the regulation of mitochondrial physiology, ROS, mitophagy and cell viability (By similarity). {ECO:0000250}. PTM: Cleaved by CASP3 during apoptosis which leads to increased activity. The cleavage by CASP3 reveals a cryptic mitochondrial targeting sequence immediately downstream of their canonical caspase cleavage sites which leads to mitochondrial import of the protein. {ECO:0000250}. SUBCELLULAR LOCATION: Cysteine protease ATG4D: Cytoplasm {ECO:0000250|UniProtKB:Q86TL0}.; SUBCELLULAR LOCATION: Cysteine protease ATG4D, mitochondrial: Cytoplasm {ECO:0000250|UniProtKB:Q86TL0}. Mitochondrion matrix {ECO:0000250|UniProtKB:Q86TL0}. Note=Imported into mitochondrial matrix after cleavage by CASP3 during oxidative stress and cell death. {ECO:0000250|UniProtKB:Q86TL0}. DOMAIN: Residues 64 to 103 constitute a cryptic mitochondrial transit peptide which is revealed after cleavage by caspase of residues 1 to 63 upon oxidative stress and cell death. It acts then as a functional transit peptide, and allows the import of the cleaved protein into the mitochondria (By similarity). {ECO:0000250}. +Q9D131 CK001_MOUSE UPF0686 protein C11orf1 homolog 166 19,527 Alternative sequence (1); Chain (1); Natural variant (1); Sequence conflict (5) SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. +Q8BHR8 CK049_MOUSE UPF0705 protein C11orf49 homolog 331 37,550 Alternative sequence (2); Chain (1); Frameshift (1); Modified residue (1) +Q9D906 ATG7_MOUSE Ubiquitin-like modifier-activating enzyme ATG7 (ATG12-activating enzyme E1 ATG7) (Autophagy-related protein 7) (APG7-like) (mAGP7) (Ubiquitin-activating enzyme E1-like protein) 698 77,520 Active site (1); Chain (1); Modified residue (1); Motif (1); Mutagenesis (1); Sequence conflict (1) FUNCTION: E1-like activating enzyme involved in the 2 ubiquitin-like systems required for cytoplasm to vacuole transport (Cvt) and autophagy. Activates ATG12 for its conjugation with ATG5 as well as the ATG8 family proteins for their conjugation with phosphatidylethanolamine. Both systems are needed for the ATG8 association to Cvt vesicles and autophagosomes membranes. Required for autophagic death induced by caspase-8 inhibition. Required for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Modulates p53/TP53 activity to regulate cell cycle and survival during metabolic stress. Plays also a key role in the maintenance of axonal homeostasis, the prevention of axonal degeneration, the maintenance of hematopoietic stem cells, the formation of Paneth cell granules, as well as in adipose differentiation. Plays a role in regulating the liver clock and glucose metabolism by mediating the autophagic degradation of CRY1 (clock repressor) in a time-dependent manner (PubMed:29937374). {ECO:0000269|PubMed:11890701, ECO:0000269|PubMed:15131264, ECO:0000269|PubMed:15866887, ECO:0000269|PubMed:16704426, ECO:0000269|PubMed:17726112, ECO:0000269|PubMed:19417210, ECO:0000269|PubMed:19855132, ECO:0000269|PubMed:19910529, ECO:0000269|PubMed:20723759, ECO:0000269|PubMed:21339326, ECO:0000269|PubMed:21617129, ECO:0000269|PubMed:22291845, ECO:0000269|PubMed:22499945, ECO:0000269|PubMed:29937374}. PTM: Acetylated by EP300. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Preautophagosomal structure {ECO:0000250}. Note=Localizes also to discrete punctae along the ciliary axoneme and to the base of the ciliary axoneme. {ECO:0000269|PubMed:24089209}. SUBUNIT: Homodimer. Interacts with ATG3, FOXO1 and EP300 acetyltransferase. The complex, composed of ATG3 and ATG7, plays a role in the conjugation of ATG12 to ATG5. Interacts with FOXO1 (By similarity). Forms intermediate conjugates with ATG8 family proteins such as GABARAP, GABARAPL1, GABARAPL2, MAP1LC3A, or GABARAPL1. Interacts with ATG12. {ECO:0000250, ECO:0000269|PubMed:11890701, ECO:0000269|PubMed:12482611, ECO:0000269|PubMed:16704426}. DOMAIN: The C-terminal part of the protein is essential for the dimerization and interaction with ATG3 and ATG12. {ECO:0000250}.; DOMAIN: The N-terminal FAP motif (residues 11 to 13) is essential for the formation of the ATG89-PE and ATG5-ATG12 conjugates. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed, especially in kidney, liver, lymph nodes and bone marrow. {ECO:0000269|PubMed:11890701}. +Q9D1Z2 CK091_MOUSE Uncharacterized protein C11orf91 homolog 194 20,754 Chain (1); Compositional bias (1) +Q4VA45 CK095_MOUSE Uncharacterized protein C11orf95 homolog 678 73,710 Chain (1); Compositional bias (4); Cross-link (1); Sequence caution (1) +Q3UPL5 CK096_MOUSE Uncharacterized protein C11orf96 homolog (Protein Ag2 homolog) 249 27,072 Chain (1); Compositional bias (1); Modified residue (4) +Q9Z0S7 CLD9_MOUSE Claudin-9 217 22,897 Chain (1); Sequence conflict (3); Topological domain (5); Transmembrane (4) TRANSMEM 13 33 Helical. {ECO:0000255}.; TRANSMEM 82 102 Helical. {ECO:0000255}.; TRANSMEM 117 137 Helical. {ECO:0000255}.; TRANSMEM 160 180 Helical. {ECO:0000255}. TOPO_DOM 1 12 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 34 81 Extracellular. {ECO:0000255}.; TOPO_DOM 103 116 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 138 159 Extracellular. {ECO:0000255}.; TOPO_DOM 181 217 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, tight junction. Cell membrane {ECO:0000250|UniProtKB:O95484}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Interacts with CLDN1, CD81 and OCLN. {ECO:0000250|UniProtKB:O95484}. +Q9CQX5 CLDN1_MOUSE Claudin domain-containing protein 1 (Claudin-25) 253 28,572 Chain (1); Glycosylation (2); Transmembrane (4) TRANSMEM 5 25 Helical. {ECO:0000255}.; TRANSMEM 141 161 Helical. {ECO:0000255}.; TRANSMEM 175 195 Helical. {ECO:0000255}.; TRANSMEM 216 236 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +P52194 CLGN_MOUSE Calmegin (A2/6) (Calnexin-T) (MEG 1 antigen) 611 69,431 Chain (1); Disulfide bond (2); Modified residue (8); Region (1); Repeat (8); Sequence conflict (18); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 472 492 Helical. {ECO:0000255}. TOPO_DOM 20 471 Lumenal. {ECO:0000255}.; TOPO_DOM 493 611 Cytoplasmic. {ECO:0000255}. FUNCTION: Functions during spermatogenesis as a chaperone for a range of client proteins that are important for sperm adhesion onto the egg zona pellucida and for subsequent penetration of the zona pellucida. Required for normal sperm migration from the uterus into the oviduct. Required for normal male fertility. Binds calcium ions. {ECO:0000269|PubMed:11784061, ECO:0000269|PubMed:15151931, ECO:0000269|PubMed:16870943, ECO:0000269|PubMed:9177349}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10495883}; Single-pass type I membrane protein {ECO:0000269|PubMed:10495883}. SUBUNIT: Interacts with PDILT and PPIB (By similarity). Interacts with ADAM2. Interacts with ADAM1A, ADAM1B and ADAM3; these are protein-coding genes in mouse but may be pseudogenes in other organisms. {ECO:0000250, ECO:0000269|PubMed:11784061}. TISSUE SPECIFICITY: Detected in testis (at protein level). Detected in testis. {ECO:0000269|PubMed:11784061, ECO:0000269|PubMed:8126001, ECO:0000269|PubMed:8188695, ECO:0000269|PubMed:9177349, ECO:0000269|PubMed:9434179}. +Q922J3 CLIP1_MOUSE CAP-Gly domain-containing linker protein 1 (Cytoplasmic linker protein 170) (CLIP-170) (Restin) 1391 155,814 Alternative sequence (1); Beta strand (6); Chain (1); Coiled coil (1); Compositional bias (1); Domain (2); Erroneous initiation (1); Helix (1); Modified residue (14); Region (1); Sequence conflict (1); Zinc finger (1) FUNCTION: Binds to the plus end of microtubules and regulates the dynamics of the microtubule cytoskeleton. Promotes microtubule growth and microtubule bundling. Links cytoplasmic vesicles to microtubules and thereby plays an important role in intracellular vesicle trafficking. Plays a role macropinocytosis and endosome trafficking. {ECO:0000250|UniProtKB:P30622}. PTM: Phosphorylated (PubMed:26972003). Phosphorylation induces conformational changes by increasing the affinity of the N-terminus for C-terminus, resulting in inhibition of its function thus decreasing its binding to microtubules and DCTN1. Exhibits a folded, autoinhibited conformation when phosphorylated and an open conformation when dephosphorylated with increased binding affinity to microtubules and DCTN1. Phosphorylation regulates its recruitment to tyrosinated microtubules and the recruitment of vesicular cargo to microtubules in neurons. Phosphorylation by MTOR may positively regulate CLIP1 association with microtubules (By similarity). {ECO:0000250|UniProtKB:P30622, ECO:0000250|UniProtKB:Q9JK25, ECO:0000269|PubMed:26972003}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P30622}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16954346}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P30622}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell projection, ruffle {ECO:0000250|UniProtKB:P30622}. Note=Localizes to microtubule plus ends. Localizes preferentially to the ends of tyrosinated microtubules (PubMed:16954346). Accumulates in plasma membrane regions with ruffling and protrusions. Associates with the membranes of intermediate macropinocytic vesicles (By similarity). {ECO:0000250|UniProtKB:P30622, ECO:0000269|PubMed:16954346}. SUBUNIT: Interacts with MTOR; phosphorylates and regulates CLIP1. Interacts (via CAP-Gly domains) with tubulin. Interacts with SLAIN2. Interacts with TUBA1B, MAPRE1 and MAPRE3. Interacts (via zinc finger) with DCTN1 (By similarity). Binds preferentially to tyrosinated microtubules, and only marginally to detyrosinated microtubules (PubMed:16954346). {ECO:0000250|UniProtKB:P30622, ECO:0000269|PubMed:16954346}. DOMAIN: Intramolecular interaction between the zinc finger domain and the CAP-Gly domains may inhibit interaction with tubulin. {ECO:0000250|UniProtKB:P30622}. +Q8K249 CLM2_MOUSE CMRF35-like molecule 2 (CLM-2) (CD300 antigen-like family member E) (CD antigen CD300e) 196 21,822 Chain (1); Disulfide bond (1); Domain (1); Glycosylation (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 172 192 Helical. {ECO:0000255}. TOPO_DOM 18 171 Extracellular. {ECO:0000255}.; TOPO_DOM 193 196 Cytoplasmic. {ECO:0000255}. FUNCTION: Probably acts as an activating receptor. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Interacts with TYROBP. {ECO:0000250}. +Q8VCH2 CLM5_MOUSE CMRF35-like molecule 5 (CLM-5) (CD300 antigen like family member D) (Leukocyte mono-Ig-like receptor 4) (Myeloid-associated immunoglobulin-like receptor 4) (MAIR-4) (MAIR-IV) 221 24,954 Chain (1); Disulfide bond (1); Domain (1); Mutagenesis (2); Region (3); Sequence conflict (10); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 178 198 Helical. {ECO:0000255}. TOPO_DOM 19 177 Extracellular. {ECO:0000255}.; TOPO_DOM 199 221 Cytoplasmic. {ECO:0000255}. FUNCTION: Acts as an activating receptor in myeloid cells and mast cells. {ECO:0000269|PubMed:16940041, ECO:0000269|PubMed:17438331}.; FUNCTION: (Microbial infection) Acts as a functional murine norovirus (MNV) receptor. Primary determinant of MNV species tropism and is sufficient to render cells permissive to infection by MNV. Can render nonmurine mammalian cells susceptible to MNV infection (PubMed:27681626, PubMed:27540007). {ECO:0000269|PubMed:27540007, ECO:0000269|PubMed:27681626}. PTM: O-glycosylated. {ECO:0000269|PubMed:17438331}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16940041}; Single-pass type I membrane protein {ECO:0000269|PubMed:16940041}. SUBUNIT: Interacts with FCER1G. {ECO:0000269|PubMed:16940041, ECO:0000269|PubMed:17438331, ECO:0000269|PubMed:20817736}. TISSUE SPECIFICITY: Expressed in dendritic cells, macrophages and granulocytes. Present on the surface of granulocytes and monocytes/macrophages (at protein level). {ECO:0000269|PubMed:16940041, ECO:0000269|PubMed:17438331}. +A2A7V7 CLM6_MOUSE CMRF35-like molecule 6 (CLM-6) (CD300 antigen-like family member C) (CD antigen CD300c) 229 25,336 Chain (1); Disulfide bond (1); Domain (1); Glycosylation (2); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 189 209 Helical. {ECO:0000255}. TOPO_DOM 22 188 Extracellular. {ECO:0000255}.; TOPO_DOM 210 229 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +O08785 CLOCK_MOUSE Circadian locomoter output cycles protein kaput (mCLOCK) (EC 2.3.1.48) 855 96,393 Alternative sequence (1); Beta strand (16); Chain (1); Compositional bias (5); Cross-link (2); Domain (4); Helix (17); Modified residue (7); Motif (1); Mutagenesis (15); Region (3); Site (4); Turn (1) FUNCTION: Transcriptional activator which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, ARNTL/BMAL1, ARNTL2/BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and ARNTL/BMAL1 or ARNTL2/BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-ARNTL/BMAL1|ARNTL2/BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress ARNTL/BMAL1 transcription, respectively. Regulates the circadian expression of ICAM1, VCAM1, CCL2, THPO and MPL and also acts as an enhancer of the transactivation potential of NF-kappaB. Plays an important role in the homeostatic regulation of sleep. The CLOCK-ARNTL/BMAL1 heterodimer regulates the circadian expression of SERPINE1/PAI1, VWF, B3, CCRN4L/NOC, NAMPT, DBP, MYOD1, PPARGC1A, PPARGC1B, SIRT1, GYS2, F7, NGFR, GNRHR, BHLHE40/DEC1, ATF4, MTA1, KLF10 and also genes implicated in glucose and lipid metabolism. Promotes rhythmic chromatin opening, regulating the DNA accessibility of other transcription factors. May play a role in spermatogenesis; contributes to the chromatoid body assembly and physiology. The CLOCK-ARNTL2/BMAL2 heterodimer activates the transcription of SERPINE1/PAI1 and BHLHE40/DEC1. The preferred binding motif for the CLOCK-ARNTL/BMAL1 heterodimer is 5'-CACGTGA-3', which contains a flanking Ala residue in addition to the canonical 6-nucleotide E-box sequence (By similarity). CLOCK specifically binds to the half-site 5'-CAC-3', while ARNTL binds to the half-site 5'-GTGA-3' (By similarity). The CLOCK-ARNTL/BMAL1 heterodimer also recognizes the non-canonical E-box motifs 5'-AACGTGA-3' and 5'-CATGTGA-3'. CLOCK has an intrinsic acetyltransferase activity, which enables circadian chromatin remodeling by acetylating histones and nonhistone proteins, including its own partner ARNTL/BMAL1. Represses glucocorticoid receptor NR3C1/GR-induced transcriptional activity by reducing the association of NR3C1/GR to glucocorticoid response elements (GREs) via the acetylation of multiple lysine residues located in its hinge region. The acetyltransferase activity of CLOCK is as important as its transcription activity in circadian control. Acetylates metabolic enzymes IMPDH2 and NDUFA9 in a circadian manner (By similarity). Facilitated by BMAL1, rhythmically interacts and acetylates argininosuccinate synthase 1 (ASS1) leading to enzymatic inhibition of ASS1 as well as the circadian oscillation of arginine biosynthesis and subsequent ureagenesis (PubMed:28985504). {ECO:0000250|UniProtKB:O15516, ECO:0000269|PubMed:12738229, ECO:0000269|PubMed:14672706, ECO:0000269|PubMed:16678094, ECO:0000269|PubMed:17417633, ECO:0000269|PubMed:18075593, ECO:0000269|PubMed:18316400, ECO:0000269|PubMed:19141540, ECO:0000269|PubMed:19286518, ECO:0000269|PubMed:19299583, ECO:0000269|PubMed:19605937, ECO:0000269|PubMed:20385766, ECO:0000269|PubMed:20430893, ECO:0000269|PubMed:20562852, ECO:0000269|PubMed:20658528, ECO:0000269|PubMed:20956306, ECO:0000269|PubMed:21768648, ECO:0000269|PubMed:22284746, ECO:0000269|PubMed:22653727, ECO:0000269|PubMed:22895791, ECO:0000269|PubMed:22900038, ECO:0000269|PubMed:22981862, ECO:0000269|PubMed:23291174, ECO:0000269|PubMed:23785138, ECO:0000269|PubMed:24089055, ECO:0000269|PubMed:24270424, ECO:0000269|PubMed:24333415, ECO:0000269|PubMed:24378737, ECO:0000269|PubMed:24385426, ECO:0000269|PubMed:24395244, ECO:0000269|PubMed:24442997, ECO:0000269|PubMed:28985504}. PTM: Ubiquitinated, leading to its proteasomal degradation. {ECO:0000269|PubMed:16980631}.; PTM: O-glycosylated; contains O-GlcNAc. O-glycosylation by OGT prevents protein degradation by inhibiting ubiquitination. It also stabilizes the CLOCK-ARNTL/BMAL1 heterodimer thereby increasing CLOCK-ARNTL/BMAL1-mediated transcriptional activation of PER1/2/3 and CRY1/2. {ECO:0000269|PubMed:23395175, ECO:0000269|PubMed:23395176}.; PTM: Phosphorylation is dependent on the CLOCK-ARNTL/BMAL1 heterodimer formation. Phosphorylation enhances the transcriptional activity, alters the subcellular localization and decreases the stability of the heterodimer by promoting its degradation. Phosphorylation shows circadian variations in the liver: the hyperphosphorylated form peaks at midnight (CT18), while the hypophosphorylated form is abundant throughout the day. May be phosphorylated by CSNK1D and CKSN1E. {ECO:0000269|PubMed:11779462, ECO:0000269|PubMed:12897057, ECO:0000269|PubMed:19414601, ECO:0000269|PubMed:19946213, ECO:0000269|PubMed:21930935, ECO:0000269|PubMed:24235147}.; PTM: Sumoylation enhances its transcriptional activity and interaction with ESR1, resulting in up-regulation of ESR1 activity. Estrogen stimulates sumoylation. Desumoylation by SENP1 negatively regulates its transcriptional activity. {ECO:0000269|PubMed:23160374}.; PTM: Undergoes lysosome-mediated degradation in a time-dependent manner in the liver. {ECO:0000269|PubMed:29937374}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11779462, ECO:0000269|PubMed:12897057, ECO:0000269|PubMed:16980631, ECO:0000269|PubMed:17310242, ECO:0000269|PubMed:18662546, ECO:0000269|PubMed:19414601}. Cytoplasm {ECO:0000269|PubMed:12897057, ECO:0000269|PubMed:16980631}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:O15516}. Note=Localizes to sites of DNA damage in a H2AX-independent manner (By similarity). Shuffling between the cytoplasm and the nucleus is under circadian regulation and is ARNTL/BMAL1-dependent. Phosphorylated form located in the nucleus predominantly between CT12 and CT21. Nonphosphorylated form found only in the cytoplasm. Sequestered to the cytoplasm in the presence of ID2. {ECO:0000250|UniProtKB:O15516, ECO:0000269|PubMed:11779462, ECO:0000269|PubMed:16980631, ECO:0000269|PubMed:20861012}. SUBUNIT: Component of the circadian clock oscillator which includes the CRY proteins, CLOCK or NPAS2, ARNTL/BMAL1 or ARNTL2/BMAL2, CSNK1D and/or CSNK1E, TIMELESS and the PER proteins (PubMed:11779462). Forms a heterodimer with ARNTL/BMAL1 (PubMed:9616112, PubMed:12897057, PubMed:16717091, PubMed:16980631, PubMed:18662546, PubMed:19946213, PubMed:22653727). The CLOCK-ARNTL/BMAL1 heterodimer is required for E-box-dependent transactivation, for CLOCK nuclear translocation and degradation, and for phosphorylation of both CLOCK and ARNTL/BMAL1 (PubMed:12897057). Interacts with NR3C1 in a ligand-dependent fashion (PubMed:19141540). Interacts with ESR1 and estrogen stimulates this interaction (By similarity). Interacts with the complex p35/CDK5 (PubMed:24235147). Interacts with RELA/p65 (PubMed:22895791). Interacts with KAT2B, CREBBP and EP300 (By similarity). Interacts with ID1 and ID3 (PubMed:20861012). Interacts with ID2 (PubMed:20861012). Interacts with MTA1 (PubMed:24089055). Interacts with OGA (PubMed:23395175). Interacts with SIRT1 (PubMed:18662546, PubMed:18662547). Interacts with CIPC (PubMed:17310242). Interacts with EZH2 (PubMed:16717091). Interacts with EIF4E, PIWIL1 and DDX4 (PubMed:22900038). Interacts with PER1, PER2, CRY1 and CRY2 and this interaction requires a translocation to the nucleus (PubMed:16717091, PubMed:18430226, PubMed:18662546). Interaction of the CLOCK-ARNTL/BMAL1 heterodimer with PER or CRY inhibits transcription activation. Interaction of the CLOCK-ARNTL/BMAL1 with CRY1 is independent of DNA but with PER2 is off DNA (By similarity). The CLOCK-ARNTL/BMAL1 heterodimer interacts with GSK3B (PubMed:19946213). Interacts with KDM5A (PubMed:21960634). Interacts with KMT2A; in a circadian manner (PubMed:21113167). Interacts with MYBBP1A (PubMed:19129230). Interacts with THRAP3 (PubMed:24043798). Interacts with MED1; this interaction requires the presence of THRAP3 (PubMed:24043798). Interacts with NCOA2 (PubMed:24529706). The CLOCK-ARNTL/BMAL1 heterodimer interacts with PASD1. Interacts with NDUFA9. Interacts with IMPDH2; in a circadian manner (By similarity). Interacts with ASS1; in a circadian manner (PubMed:28985504). {ECO:0000250|UniProtKB:O15516, ECO:0000269|PubMed:11779462, ECO:0000269|PubMed:12897057, ECO:0000269|PubMed:16717091, ECO:0000269|PubMed:16980631, ECO:0000269|PubMed:17310242, ECO:0000269|PubMed:18430226, ECO:0000269|PubMed:18662546, ECO:0000269|PubMed:18662547, ECO:0000269|PubMed:19129230, ECO:0000269|PubMed:19141540, ECO:0000269|PubMed:19946213, ECO:0000269|PubMed:20861012, ECO:0000269|PubMed:21113167, ECO:0000269|PubMed:21960634, ECO:0000269|PubMed:22653727, ECO:0000269|PubMed:22895791, ECO:0000269|PubMed:22900038, ECO:0000269|PubMed:23160374, ECO:0000269|PubMed:23395175, ECO:0000269|PubMed:24043798, ECO:0000269|PubMed:24089055, ECO:0000269|PubMed:24154698, ECO:0000269|PubMed:24235147, ECO:0000269|PubMed:24529706, ECO:0000269|PubMed:28985504, ECO:0000269|PubMed:9616112}. DOMAIN: Contains a Gln-rich C-terminal domain which could correspond to the transactivation domain. TISSUE SPECIFICITY: Expressed equally in brain, eye, testes, ovaries, liver, heart, lung, kidney. In the brain, expression is abundant in the suprachiasmatic nuclei (SCN), in the pyriform cortex, and in the hippocampus. Low expression throughout the rest of the brain. Expression does not appear to undergo circadian oscillations. {ECO:0000269|PubMed:22900038, ECO:0000269|PubMed:24154698, ECO:0000269|PubMed:9160755}. +P03930 ATP8_MOUSE ATP synthase protein 8 (A6L) (F-ATPase subunit 8) 67 7,766 Chain (1); Modified residue (3); Transmembrane (1) TRANSMEM 8 24 Helical. {ECO:0000255}. FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion membrane; Single-pass membrane protein. SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. Component of an ATP synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MD and MP68 (By similarity). {ECO:0000250}. +Q9D4C9 CLVS1_MOUSE Clavesin-1 (Retinaldehyde-binding protein 1-like 1) 354 40,613 Alternative sequence (2); Chain (1); Domain (1); Erroneous initiation (1); Sequence conflict (1) FUNCTION: Required for normal morphology of late endosomes and/or lysosomes in neurons. Binds phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Early endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250}. SUBUNIT: Forms a complex with clathrin heavy chain and gamma-adaptin. {ECO:0000250}. DOMAIN: The CRAL-TRIO domain is required for targeting to the membrane and for binding PtdIns(3,5)P2. {ECO:0000250}. +Q8R4N0 CLYBL_MOUSE Citramalyl-CoA lyase, mitochondrial (EC 4.1.3.25) (Beta-methylmalate synthase) (EC 2.3.3.-) (Citrate lyase subunit beta-like protein, mitochondrial) (Citrate lyase beta-like) (Malate synthase) (EC 2.3.3.9) 338 37,549 Active site (1); Binding site (4); Chain (1); Metal binding (2); Modified residue (8); Region (1); Sequence conflict (1); Transit peptide (1) FUNCTION: Mitochondrial citramalyl-CoA lyase indirectly involved in the vitamin B12 metabolism (PubMed:29056341). Converts citramalyl-CoA into acetyl-CoA and pyruvate in the C5-dicarboxylate catabolism pathway (By similarity). The C5-dicarboxylate catabolism pathway is required to detoxify itaconate, a vitamin B12-poisoning metabolite (PubMed:29056341). Also acts as a malate synthase in vitro, converting glyoxylate and acetyl-CoA to malate (By similarity). Also acts as a beta-methylmalate synthase in vitro, by mediating conversion of glyoxylate and propionyl-CoA to beta-methylmalate (By similarity). Also has very weak citramalate synthase activity in vitro (By similarity). {ECO:0000250|UniProtKB:Q8N0X4, ECO:0000269|PubMed:29056341}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:18614015}. SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:Q8N0X4}. TISSUE SPECIFICITY: Detected in brown fat, brain, liver, kidney, heart, skeletal muscle and ovary (at protein level). {ECO:0000269|PubMed:11741334, ECO:0000269|PubMed:24334609}. +P21844 CMA1_MOUSE Chymase (EC 3.4.21.39) (Alpha-chymase) (Mast cell chymase 1) (Mast cell protease 5) (mMCP-5) (Mast cell protease I) 247 27,586 Active site (3); Chain (1); Disulfide bond (3); Domain (1); Erroneous initiation (1); Glycosylation (1); Propeptide (1); Sequence conflict (3); Signal peptide (1) FUNCTION: Major secreted protease of mast cells with suspected roles in vasoactive peptide generation, extracellular matrix degradation, and regulation of gland secretion. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1527387}. Cytoplasmic granule {ECO:0000269|PubMed:1527387}. Note=Secretory granules. TISSUE SPECIFICITY: Mast cells. +Q9D486 CMIP_MOUSE C-Maf-inducing protein (c-Mip) 773 86,259 Alternative sequence (2); Chain (1); Domain (1); Modified residue (4); Repeat (4); Sequence caution (1); Sequence conflict (2) FUNCTION: Plays a role in T-cell signaling pathway. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8IY22}. Cytoplasm {ECO:0000250|UniProtKB:Q8IY22}. Note=Isoform 2 is translocated to the nucleus and is specifically recruited during minimal change nephrotic syndrome (MCNS). Detected in nuclear and cytoplasmic compartments during MCNS relapse. Expressed in cytoplasm only during MCNS remission and absent in normal patients. {ECO:0000250|UniProtKB:Q8IY22}. SUBUNIT: Interacts with FLNA. {ECO:0000250}. +A2A891 CMTA1_MOUSE Calmodulin-binding transcription activator 1 1682 184,319 Alternative sequence (5); Chain (1); Compositional bias (1); DNA binding (1); Domain (4); Erroneous gene model prediction (1); Motif (1); Repeat (3); Sequence conflict (8) FUNCTION: Transcriptional activator. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y6Y1, ECO:0000255|PROSITE-ProRule:PRU00767}. Cytoplasm {ECO:0000250|UniProtKB:Q9Y6Y1}. SUBUNIT: May interact with calmodulin. {ECO:0000250|UniProtKB:Q9Y6Y1}. +Q80Y50 CMTA2_MOUSE Calmodulin-binding transcription activator 2 1208 132,010 Alternative sequence (6); Chain (1); Compositional bias (1); DNA binding (1); Domain (3); Motif (1); Repeat (3); Sequence conflict (2) FUNCTION: Transcription activator. May act as tumor suppressor (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: May interact with calmodulin. {ECO:0000305}. +Q8BWQ4 CMTR2_MOUSE Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 2 (EC 2.1.1.296) (Cap methyltransferase 2) (Cap2 2'O-ribose methyltransferase 2) (MTr2) (FtsJ methyltransferase domain-containing protein 1) 767 87,143 Active site (3); Binding site (3); Chain (1); Domain (1); Sequence conflict (1) FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that mediates mRNA cap2 2'-O-ribose methylation to the 5'-cap structure of mRNAs. Methylates the ribose of the second nucleotide of a m(7)GpppG-capped mRNA and small nuclear RNA (snRNA) (cap0) to produce m(7)GpppRmpNm (cap2). Recognizes a guanosine cap on RNA independently of its N(7) methylation status. Display cap2 methylation on both cap0 and cap1. Displays a preference for cap1 RNAs. {ECO:0000250|UniProtKB:Q8IYT2}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8IYT2}. Cytoplasm {ECO:0000250|UniProtKB:Q8IYT2}. +Q9JJ93 CN119_MOUSE Uncharacterized protein C14orf119 homolog 142 16,005 Chain (1); Sequence conflict (2) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. +P16330 CN37_MOUSE 2',3'-cyclic-nucleotide 3'-phosphodiesterase (CNP) (CNPase) (EC 3.1.4.37) 420 47,123 Active site (2); Alternative sequence (1); Beta strand (10); Binding site (2); Chain (1); Helix (10); Lipidation (1); Modified residue (7); Propeptide (1); Sequence conflict (4); Turn (2) FUNCTION: May participate in RNA metabolism in the myelinating cell, CNP is the third most abundant protein in central nervous system myelin. {ECO:0000269|PubMed:22393399}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:18076147}; Lipid-anchor {ECO:0000269|PubMed:18076147}. Melanosome {ECO:0000250}. Note=Firmly bound to membrane structures of brain white matter. SUBUNIT: Exists as monomers and homodimers. {ECO:0000269|PubMed:22393399}. +Q9D5U8 CNBD2_MOUSE Cyclic nucleotide-binding domain-containing protein 2 (Cyclic nucleotide receptor involved in sperm function) 673 77,892 Alternative sequence (1); Chain (1); Erroneous initiation (1); Nucleotide binding (1); Sequence conflict (4) FUNCTION: Essential for male fertility. Plays an important role in spermatogenesis and regulates sperm motility by controlling the development of the flagellar bending of sperm (PubMed:24339785). {ECO:0000269|PubMed:24339785}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:24339785}. TISSUE SPECIFICITY: Testis-specific. Exclusively expressed in testicular germ cells while it is not present in mature sperm (at protein level). {ECO:0000269|PubMed:24339785}. +Q9JJN6 CNBP1_MOUSE Beta-catenin-interacting protein 1 (Inhibitor of beta-catenin and Tcf-4) 81 9,174 Chain (1); Modified residue (1); Mutagenesis (1) FUNCTION: Prevents the interaction between CTNNB1 and TCF family members, and acts as negative regulator of the Wnt signaling pathway. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. SUBUNIT: Binds CTNNB1. TISSUE SPECIFICITY: Highly expressed in heart, brain, liver and skeletal muscle. Detected at low levels in kidney, testis and lung. +Q6ZQK0 CNDD3_MOUSE Condensin-2 complex subunit D3 (Non-SMC condensin II complex subunit D3) 1506 169,432 Chain (1); Coiled coil (1); Modified residue (5); Repeat (4); Sequence conflict (3) FUNCTION: Regulatory subunit of the condensin-2 complex, a complex which establishes mitotic chromosome architecture and is involved in physical rigidity of the chromatid axis. May promote the resolution of double-strand DNA catenanes (intertwines) between sister chromatids. Condensin-mediated compaction likely increases tension in catenated sister chromatids, providing directionality for type II topoisomerase-mediated strand exchanges toward chromatid decatenation. Specifically required for decatenation of centromeric ultrafine DNA bridges during anaphase. Early in neurogenesis, may play an essential role to ensure accurate mitotic chromosome condensation in neuron stem cells, ultimately affecting neuron pool and cortex size. {ECO:0000250|UniProtKB:P42695}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the condensin-2 complex, which contains the SMC2 and SMC4 heterodimer, and 3 non SMC subunits that probably regulate the complex: NCAPH2, NCAPD3 and NCAPG2. {ECO:0000250}. +Q6DFV1 CNDG2_MOUSE Condensin-2 complex subunit G2 (Chromosome-associated protein G2) (CAP-G2) (Leucine zipper protein 5) (More than blood protein) (Non-SMC condensin II complex subunit G2) 1138 130,894 Chain (1); Frameshift (1); Modified residue (2); Repeat (1); Sequence conflict (5) FUNCTION: Regulatory subunit of the condensin-2 complex, a complex which establishes mitotic chromosome architecture and is involved in physical rigidity of the chromatid axis. Is required for early embryonic development and is essential for viability and expansion of the inner cell mass (ICM) of the implanting blastocyst. {ECO:0000269|PubMed:14729962}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the condensin-2 complex, which contains the SMC2 and SMC4 heterodimer, and 3 non SMC subunits that probably regulate the complex: NCAPH2, NCAPD3 and NCAPG2. TISSUE SPECIFICITY: Expressed in spleen, lung and testis as well as in hematopoietic cell lines. {ECO:0000269|PubMed:14729962}. +Q9JJZ9 CNGB3_MOUSE Cyclic nucleotide-gated cation channel beta-3 (Cone photoreceptor cGMP-gated channel subunit beta) (Cyclic nucleotide-gated cation channel modulatory subunit) (Cyclic nucleotide-gated channel beta-3) (CNG channel beta-3) (Cyclic nucleotide-gated channel subunit CNG6) 694 79,722 Binding site (2); Chain (1); Glycosylation (1); Nucleotide binding (1); Topological domain (7); Transmembrane (6) TRANSMEM 210 230 Helical; Name=H1. {ECO:0000255}.; TRANSMEM 243 263 Helical; Name=H2. {ECO:0000255}.; TRANSMEM 295 315 Helical; Name=H3. {ECO:0000255}.; TRANSMEM 352 372 Helical; Name=H4. {ECO:0000255}.; TRANSMEM 410 430 Helical; Name=H5. {ECO:0000255}.; TRANSMEM 569 589 Helical; Name=H6. {ECO:0000255}. TOPO_DOM 1 209 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 231 242 Extracellular. {ECO:0000255}.; TOPO_DOM 264 294 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 316 351 Extracellular. {ECO:0000255}.; TOPO_DOM 373 409 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 431 568 Extracellular. {ECO:0000255}.; TOPO_DOM 590 694 Cytoplasmic. {ECO:0000255}. FUNCTION: Visual signal transduction is mediated by a G-protein coupled cascade using cGMP as second messenger. This protein can be activated by cGMP which leads to an opening of the cation channel and thereby causing a depolarization of rod photoreceptors. Essential for the generation of light-evoked electrical responses in the red-, green- and blue sensitive cones (By similarity). Induced a flickering channel gating, weakened the outward rectification in the presence of extracellular calcium, increased sensitivity for L-cis diltiazem and enhanced the cAMP efficacy of the channel when coexpressed with CNGA3. {ECO:0000250, ECO:0000269|PubMed:10662822}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SUBUNIT: Tetramer formed of three CNGA3 and one CNGB3 modulatory subunits. {ECO:0000250}. TISSUE SPECIFICITY: Small subset of retinal photorecptor cells and testis. {ECO:0000269|PubMed:10662822}. +O35089 CNIH2_MOUSE Protein cornichon homolog 2 (CNIH-2) (Cornichon family AMPA receptor auxiliary protein 2) (Cornichon-like protein) 160 18,931 Chain (1); Topological domain (4); Transmembrane (3) TRANSMEM 11 31 Helical. {ECO:0000255}.; TRANSMEM 73 93 Helical. {ECO:0000255}.; TRANSMEM 139 159 Helical. {ECO:0000255}. TOPO_DOM 1 10 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 32 72 Lumenal. {ECO:0000255}.; TOPO_DOM 94 138 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 160 160 Lumenal. {ECO:0000255}. FUNCTION: Regulates the trafficking and gating properties of AMPA-selective glutamate receptors (AMPARs). Promotes their targeting to the cell membrane and synapses and modulates their gating properties by regulating their rates of activation, deactivation and desensitization. Blocks CACNG8-mediated resensitization of AMPA receptors. {ECO:0000269|PubMed:20805473, ECO:0000269|PubMed:21172611}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000269|PubMed:21172611}. Cell projection, dendrite {ECO:0000269|PubMed:21172611}. Cell projection, dendritic spine {ECO:0000269|PubMed:21172611}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Also localizes to the cell membrane of extrasynaptic sites (dendritic shafts, spines of pyramidal cells). {ECO:0000250}. SUBUNIT: Acts as an auxiliary subunit for AMPA-selective glutamate receptors (AMPARs). Found in a complex with GRIA1, GRIA2, GRIA3, GRIA4, CNIH3, CACNG2, CACNG3, CACNG4, CACNG5, CACNG7 and CACNG8. Interacts with GRIA1 (By similarity). Interacts with CACGN8. {ECO:0000250, ECO:0000269|PubMed:21172611}. TISSUE SPECIFICITY: Brain. Highest levels seen in the hippocampus, intermediate levels in the cerebral cortex, striatum olfactory bulb, and thalamus and lower levels in the cerebellum (at protein level). Also expressed in the lung. {ECO:0000269|PubMed:10022955, ECO:0000269|PubMed:21172611}. +Q8BMA3 CNKR3_MOUSE Connector enhancer of kinase suppressor of ras 3 (Connector enhancer of KSR 3) (CNK homolog protein 3) (CNK3) (CNKSR family member 3) (Maguin-like protein) 555 61,870 Alternative sequence (2); Chain (1); Domain (4); Modified residue (2); Sequence conflict (2) FUNCTION: Involved in transepithelial sodium transport. Regulates aldosterone-induced and epithelial sodium channel (ENaC)-mediated sodium transport through regulation of ENaC cell surface expression. Acts as a scaffold protein coordinating the assembly of an ENaC-regulatory complex (ERC). {ECO:0000269|PubMed:19567370, ECO:0000269|PubMed:22851176}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22851176}. Apical cell membrane {ECO:0000269|PubMed:22851176}; Peripheral membrane protein {ECO:0000269|PubMed:22851176}. SUBUNIT: Interacts with epithelial sodium channel ENaC. Interacts directly with SCNN1A (ENaC subunit alpha) and SCNN1B (ENaC subunit beta) C-terminal tails. Interacts with ENaC regulatory proteins NEDD4L, RAF1 and SGK1. {ECO:0000250|UniProtKB:Q6P9H4}. DOMAIN: The PDZ domain is required for interaction with ENaC and SGK1, but not for interaction with NEDDL4 and RAF1. {ECO:0000250|UniProtKB:Q6P9H4}. TISSUE SPECIFICITY: Expressed in kidney. {ECO:0000269|PubMed:19567370}. +Q9Z1F6 CNMD_MOUSE Leukocyte cell-derived chemotaxin 1 (Chondromodulin) [Cleaved into: Chondrosurfactant protein (CH-SP); Chondromodulin-1 (Chondromodulin-I) (ChM-I)] 334 37,225 Chain (2); Disulfide bond (5); Domain (1); Glycosylation (1); Propeptide (1); Sequence conflict (4); Transmembrane (1) TRANSMEM 46 66 Helical. {ECO:0000255}. FUNCTION: Bifunctional growth regulator that stimulates the growth of cultured chondrocytes in the presence of basic fibroblast growth factor (FGF) but inhibits the growth of cultured vascular endothelial cells. May contribute to the rapid growth of cartilage and vascular invasion prior to the replacement of cartilage by bone during endochondral bone development (By similarity). Inhibits in vitro tube formation and mobilization of endothelial cells (By similarity). Plays a role as antiangiogenic factor in cardiac valves to suppress neovascularization. {ECO:0000250, ECO:0000269|PubMed:16980969}. PTM: After cleavage, the post-translationally modified ChM-I is secreted as a glycoprotein. {ECO:0000250}. SUBCELLULAR LOCATION: Chondromodulin-1: Secreted, extracellular space, extracellular matrix {ECO:0000250}. Note=Accumulated in the inter-territorial matrix of cartilage. {ECO:0000250}.; SUBCELLULAR LOCATION: Chondrosurfactant protein: Endomembrane system {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Detected in the four cardiac valves, valvular interstitial cells and extracellular matrix (at protein level). {ECO:0000269|PubMed:16980969}. +Q8BH15 CNO10_MOUSE CCR4-NOT transcription complex subunit 10 744 81,818 Alternative sequence (6); Chain (1); Coiled coil (1); Initiator methionine (1); Modified residue (1) FUNCTION: Component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. Additional complex functions may be a consequence of its influence on mRNA expression. Is not required for association of CNOT7 to the CCR4-NOT complex (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Component of the CCR4-NOT complex; distinct complexes seem to exist that differ in the participation of probably mutually exclusive catalytic subunits. CNOT10 and CNOT11 form a subcomplex docked to the CNOT1 scaffold (By similarity). {ECO:0000250}. +Q4VAB4 CNPY1_MOUSE Protein canopy homolog 1 94 11,249 Alternative sequence (1); Chain (1) +Q9DAU1 CNPY3_MOUSE Protein canopy homolog 3 (Protein associated with Tlr4) (Trinucleotide repeat-containing gene 5 protein) 276 30,538 Alternative sequence (1); Chain (1); Coiled coil (1); Disulfide bond (3); Domain (1); Glycosylation (1); Mutagenesis (3); Sequence conflict (1); Signal peptide (1) FUNCTION: Toll-like receptor (TLR)-specific co-chaperone for HSP90B1. Required for proper TLR folding, except that of TLR3, and hence controls TLR exit from the endoplasmic reticulum. Consequently, required for both innate and adaptive immune responses. {ECO:0000269|PubMed:16849487, ECO:0000269|PubMed:17998391, ECO:0000269|PubMed:20865800}. SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:17998391, ECO:0000269|PubMed:20865800}. SUBUNIT: Interacts with HSP90B1; this interaction is disrupted in the presence of ATP. Interacts with TLR1, TLR2, TLR4 and TLR9. Strongest interaction with TLR4. {ECO:0000269|PubMed:16338228, ECO:0000269|PubMed:16849487, ECO:0000269|PubMed:17998391, ECO:0000269|PubMed:18780723, ECO:0000269|PubMed:20865800}. +P09174 CNRG_MOUSE Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma (GMP-PDE gamma) (EC 3.1.4.35) 87 9,637 Chain (1); Compositional bias (1); Modified residue (1) FUNCTION: Participates in processes of transmission and amplification of the visual signal. cGMP-PDEs are the effector molecules in G-protein-mediated phototransduction in vertebrate rods and cones. SUBUNIT: Oligomer composed of two catalytic chains (alpha and beta), an inhibitory chain (gamma) and the delta chain. DISEASE: Note=Deficiency in GMP-PDE activity cause accumulation of cGMP in visual cells. The elevated cGMP levels are associated with degeneration of the photoreceptors and blindness. {ECO:0000303|PubMed:2835267}. +Q8CBC4 CNST_MOUSE Consortin 711 76,866 Alternative sequence (3); Chain (1); Mutagenesis (1); Topological domain (2); Transmembrane (1) TRANSMEM 651 671 Helical. {ECO:0000255}. TOPO_DOM 1 650 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 672 711 Extracellular. {ECO:0000255}. FUNCTION: Required for targeting of connexins to the plasma membrane. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250}. Note=Located predominantly in the trans-Golgi network. Probably trafficks between the trans-Golgi network and the cell membrane via the secretory pathway (By similarity). {ECO:0000250}. SUBUNIT: Interacts with connexins GJA1/CX43, GJB1/CX32, GJB2/CX26, GJB3/CX31, GJB6/CX30 and GJC1/CX45. Also interacts with GGA1 and GGA2. Does not interact with PANX1. {ECO:0000269|PubMed:19864490}. +P51642 CNTF_MOUSE Ciliary neurotrophic factor (CNTF) 198 22,587 Chain (1) FUNCTION: CNTF is a survival factor for various neuronal cell types. Seems to prevent the degeneration of motor axons after axotomy. SUBCELLULAR LOCATION: Cytoplasm. TISSUE SPECIFICITY: Nervous system. +Q61330 CNTN2_MOUSE Contactin-2 (Axonal glycoprotein TAG-1) (Axonin-1) (Transient axonal glycoprotein 1) (TAX-1) 1040 113,217 Beta strand (23); Chain (1); Compositional bias (1); Disulfide bond (4); Domain (10); Glycosylation (11); Helix (2); Lipidation (1); Motif (1); Propeptide (1); Sequence conflict (3); Signal peptide (1); Turn (1) FUNCTION: In conjunction with another transmembrane protein, CNTNAP2, contributes to the organization of axonal domains at nodes of Ranvier by maintaining voltage-gated potassium channels at the juxtaparanodal region. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. Note=Attached to the neuronal membrane by a GPI-anchor and is also released from neurons. {ECO:0000250}. +Q9CPW0 CNTP2_MOUSE Contactin-associated protein-like 2 (Cell recognition molecule Caspr2) 1332 148,197 Alternative sequence (1); Chain (1); Disulfide bond (11); Domain (8); Erroneous initiation (1); Glycosylation (11); Modified residue (2); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1263 1283 Helical. {ECO:0000255}. TOPO_DOM 28 1262 Extracellular. {ECO:0000255}.; TOPO_DOM 1284 1332 Cytoplasmic. {ECO:0000255}. FUNCTION: Required, with CNTNAP1, for radial and longitudinal organization of myelinated axons (PubMed:25378149). Plays a role in the formation of functional distinct domains critical for saltatory conduction of nerve impulses in myelinated nerve fibers. Demarcates the juxtaparanodal region of the axo-glial junction (Probable) (PubMed:25378149). {ECO:0000269|PubMed:25378149, ECO:0000305|PubMed:11567047}. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11567047}; Single-pass type I membrane protein {ECO:0000305}. Cell projection, axon {ECO:0000269|PubMed:11567047, ECO:0000269|PubMed:25378149}. Cell junction, paranodal septate junction {ECO:0000269|PubMed:25378149}. Note=Expressed in the juxtaparadonal region. {ECO:0000269|PubMed:25378149}. SUBUNIT: Interacts (via C-terminus) with KCNA2. {ECO:0000269|PubMed:11567047}. TISSUE SPECIFICITY: In sciatic nerve predominantly found at the juxtaparanodal regions (at protein level). {ECO:0000269|PubMed:11567047, ECO:0000269|PubMed:25378149}. +Q3TEI4 CO039_MOUSE Uncharacterized protein C15orf39 homolog 1023 108,224 Alternative sequence (1); Chain (1); Modified residue (9); Sequence conflict (15) +Q3U4G0 CO041_MOUSE Uncharacterized protein C15orf41 homolog 281 32,113 Alternative sequence (1); Chain (1); Frameshift (1); Modified residue (1); Sequence conflict (1) +Q0VG49 CO061_MOUSE Uncharacterized protein C15orf61 homolog 157 17,987 Alternative sequence (1); Chain (1); Frameshift (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q8CE97 CO062_MOUSE Uncharacterized protein C15orf62 homolog, mitochondrial 175 19,657 Chain (1); Erroneous initiation (2); Transit peptide (1) SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}. +P28481 CO2A1_MOUSE Collagen alpha-1(II) chain (Alpha-1 type II collagen) [Cleaved into: Collagen alpha-1(II) chain; Chondrocalcin] 1487 141,973 Alternative sequence (6); Chain (2); Disulfide bond (5); Domain (2); Erroneous initiation (1); Glycosylation (7); Metal binding (5); Modified residue (28); Natural variant (1); Propeptide (1); Region (2); Sequence conflict (25); Signal peptide (1); Site (2) FUNCTION: Type II collagen is specific for cartilaginous tissues. It is essential for the normal embryonic development of the skeleton, for linear growth and for the ability of cartilage to resist compressive forces. PTM: Contains mostly 4-hydroxyproline. Prolines at the third position of the tripeptide repeating unit (G-X-P) are 4-hydroxylated in some or all of the chains. {ECO:0000250|UniProtKB:P05539}.; PTM: Contains 3-hydroxyproline at a few sites. This modification occurs on the first proline residue in the sequence motif Gly-Pro-Hyp, where Hyp is 4-hydroxyproline. {ECO:0000250|UniProtKB:P05539}.; PTM: Lysine residues at the third position of the tripeptide repeating unit (G-X-Y) are 5-hydroxylated in some or all of the chains. {ECO:0000250|UniProtKB:P05539}.; PTM: O-glycosylated on hydroxylated lysine residues. The O-linked glycan consists of a Glc-Gal disaccharide. {ECO:0000250|UniProtKB:P05539}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}. SUBUNIT: Homotrimers of alpha 1(II) chains. DOMAIN: The C-terminal propeptide, also known as COLFI domain, have crucial roles in tissue growth and repair by controlling both the intracellular assembly of procollagen molecules and the extracellular assembly of collagen fibrils. It binds a calcium ion which is essential for its function (By similarity). {ECO:0000250}. DISEASE: Note=Defects in Col2a1 are the cause of a phenotype resembling human spondyloepiphyseal dysplasia congenita (sedc). Homozygous sedc mice can be identified at birth by their small size and shortened trunk. Adults have shortened noses, dysplastic vertebrae, femora and tibias, and retinoschisis and hearing loss. +P08121 CO3A1_MOUSE Collagen alpha-1(III) chain 1464 138,943 Chain (1); Disulfide bond (7); Domain (2); Glycosylation (1); Metal binding (5); Modified residue (6); Propeptide (2); Region (2); Signal peptide (1) FUNCTION: Collagen type III occurs in most soft connective tissues along with type I collagen. Involved in regulation of cortical development. Is the major ligand of ADGRG1 in the developing brain and binding to ADGRG1 inhibits neuronal migration and activates the RhoA pathway by coupling ADGRG1 to GNA13 and possibly GNA12. {ECO:0000269|PubMed:21768377}. PTM: Proline residues at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.; PTM: O-linked glycan consists of a Glc-Gal disaccharide bound to the oxygen atom of a post-translationally added hydroxyl group. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}. SUBUNIT: Trimers of identical alpha 1(III) chains. The chains are linked to each other by interchain disulfide bonds. Trimers are also cross-linked via hydroxylysines. DOMAIN: The C-terminal propeptide, also known as COLFI domain, have crucial roles in tissue growth and repair by controlling both the intracellular assembly of procollagen molecules and the extracellular assembly of collagen fibrils. It binds a calcium ion which is essential for its function (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in embryonic brain, specifically in the meninges, pial basement membrane and blood vessels (at protein level). {ECO:0000269|PubMed:21768377}. +P01029 CO4B_MOUSE Complement C4-B [Cleaved into: Complement C4 beta chain; Complement C4 alpha chain; C4a anaphylatoxin; Complement C4 gamma chain] 1738 192,915 Chain (4); Cross-link (1); Disulfide bond (5); Domain (2); Glycosylation (4); Modified residue (3); Propeptide (2); Sequence conflict (42); Signal peptide (1) FUNCTION: Non-enzymatic component of C3 and C5 convertases and thus essential for the propagation of the classical complement pathway. Covalently binds to immunoglobulins and immune complexes and enhances the solubilization of immune aggregates and the clearance of IC through CR1 on erythrocytes. Catalyzes the transacylation of the thioester carbonyl group to form ester bonds with carbohydrate antigens (By similarity). {ECO:0000250}. PTM: Prior to secretion, the single-chain precursor is enzymatically cleaved to yield non-identical chains alpha, beta and gamma. During activation, the alpha chain is cleaved by C1 into C4a and C4b, and C4b stays linked to the beta and gamma chains. Further degradation of C4b by C1 into the inactive fragments C4c and C4d blocks the generation of C3 convertase. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P0C0L5}. Cell junction, synapse {ECO:0000250|UniProtKB:P0C0L5}. Cell projection, axon {ECO:0000250|UniProtKB:P0C0L5}. Cell projection, dendrite {ECO:0000250|UniProtKB:P0C0L5}. SUBUNIT: Circulates in blood as a disulfide-linked trimer of an alpha, beta and gamma chain. +Q02788 CO6A2_MOUSE Collagen alpha-2(VI) chain 1034 110,334 Chain (1); Domain (3); Erroneous initiation (2); Frameshift (1); Glycosylation (5); Modified residue (2); Motif (5); Region (3); Sequence conflict (10); Signal peptide (1) FUNCTION: Collagen VI acts as a cell-binding protein. PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Recruited on membranes by CSPG4. {ECO:0000250}. SUBUNIT: Trimers composed of three different chains: alpha-1(VI), alpha-2(VI), and alpha-3(VI) or alpha-4(VI) or alpha-5(VI) or alpha-6(VI). Interacts with CSPG4 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in adipose tissue, lung, adrenal glands and ovary. Lower levels in testis, tongue, skin, kidney, heart, intestine and spleen. No expression in skeletal muscle or liver. +Q8C6K9 CO6A6_MOUSE Collagen alpha-6(VI) chain 2265 246,323 Alternative sequence (2); Chain (1); Domain (9); Glycosylation (4); Motif (1); Region (3); Sequence conflict (1); Signal peptide (1) FUNCTION: Collagen VI acts as a cell-binding protein. {ECO:0000250}. PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:18276594}. Note=Deposed in the extracellular matrix of skeletal muscle. SUBUNIT: Trimers composed of three different chains: alpha-1(VI), alpha-2(VI), and alpha-3(VI) or alpha-4(VI) or alpha-5(VI) or alpha-6(VI). {ECO:0000305|PubMed:18276594}. TISSUE SPECIFICITY: In newborn, it is expressed in lung, heart, kidney, muscle, brain, intestine, skin, femur and sternum. In adult, it is expressed in lung, heart, muscle, ovary, brain, liver and sternum. {ECO:0000269|PubMed:18276594}. +P25318 CO8A2_MOUSE Collagen alpha-2(VIII) chain (Endothelial collagen) 699 66,943 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (1); Region (3); Sequence conflict (1); Signal peptide (1) FUNCTION: Macromolecular component of the subendothelium. Major component of the Descemet's membrane (basement membrane) of corneal endothelial cells. Also component of the endothelia of blood vessels. Necessary for migration and proliferation of vascular smooth muscle cells and thus, has a potential role in the maintenance of vessel wall integrity and structure, in particular in atherogenesis (By similarity). {ECO:0000250, ECO:0000269|PubMed:19401424}. PTM: Proteolytically cleaved by neutrophil elastase, in vitro. {ECO:0000250}.; PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane. SUBUNIT: Homotrimers, or heterotrimers in association with alpha 2(VIII) type collagens. Four homotrimers can form a tetrahedron stabilized by central interacting C-terminal NC1 trimers (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: In the kidney, expressed in mesangial cells, glomerular endothelial cells, and tubular epithelial cells. {ECO:0000269|PubMed:19401424}. +Q8K182 CO8A_MOUSE Complement component C8 alpha chain (Complement component 8 subunit alpha) 587 66,080 Chain (1); Disulfide bond (9); Domain (5); Glycosylation (5); Natural variant (5); Propeptide (1); Signal peptide (1) FUNCTION: Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells. C8A inserts into the target membrane, but does not form pores by itself (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Secreted as soluble protein. Inserts into the cell membrane of target cells (By similarity). {ECO:0000250}. SUBUNIT: Heterotrimer of 3 chains: alpha, beta and gamma. The alpha and gamma chains are disulfide bonded. Component of the membrane attack complex (MAC). MAC assembly is initiated by proteolytic cleavage of C5 into C5a and C5b. C5b sequentially binds C6, C7, C8 and multiple copies of the pore-forming subunit C9 (By similarity). {ECO:0000250}. +Q9D2R6 COA3_MOUSE Cytochrome c oxidase assembly factor 3 homolog, mitochondrial (Coiled-coil domain-containing protein 56) 108 11,987 Chain (1); Coiled coil (1); Initiator methionine (1); Modified residue (1); Topological domain (2); Transmembrane (1) TRANSMEM 58 80 Helical. {ECO:0000255}. TOPO_DOM 2 57 Mitochondrial matrix. {ECO:0000255}.; TOPO_DOM 81 108 Mitochondrial intermembrane. {ECO:0000255}. FUNCTION: Core component of the MITRAC (mitochondrial translation regulation assembly intermediate of cytochrome c oxidase complex) complex, that regulates cytochrome c oxidase assembly. MITRAC complexes regulate both translation of mitochondrial encoded components and assembly of nuclear-encoded components imported in mitochondrion. Required for efficient translation of MT-CO1 and mitochondrial respiratory chain complex IV assembly. {ECO:0000250|UniProtKB:Q9Y2R0}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. SUBUNIT: Along with COX14, core component of the MITRAC (mitochondrial translation regulation assembly intermediate of cytochrome c oxidase complex) complex. Interacts with MT-CO1/COX1, SMIM20, SURF1 and TIMM21. {ECO:0000250|UniProtKB:Q9Y2R0}. +Q8BT51 COA4_MOUSE Cytochrome c oxidase assembly factor 4 homolog, mitochondrial (Coiled-coil-helix-coiled-coil-helix domain-containing protein 8) 87 10,135 Chain (1); Disulfide bond (2); Domain (1); Motif (2); Sequence conflict (1) FUNCTION: Putative COX assembly factor. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9NYJ1}. +Q99M07 COA5_MOUSE Cytochrome c oxidase assembly factor 5 74 8,359 Chain (1); Disulfide bond (2); Domain (1); Modified residue (1); Motif (2) FUNCTION: Involved in an early step of the mitochondrial complex IV assembly process. {ECO:0000250}. +Q8BGD8 COA6_MOUSE Cytochrome c oxidase assembly factor 6 homolog 79 9,298 Chain (1); Disulfide bond (2); Domain (1); Motif (2) FUNCTION: Involved in the maturation of the mitochondrial respiratory chain complex IV subunit MT-CO2/COX2. Thereby, may regulate early steps of complex IV assembly. Mitochondrial respiratory chain complex IV or cytochrome c oxidase is the component of the respiratory chain that catalyzes the transfer of electrons from intermembrane space cytochrome c to molecular oxygen in the matrix and as a consequence contributes to the proton gradient involved in mitochondrial ATP synthesis. May also be required for efficient formation of respiratory supercomplexes comprised of complexes III and IV. {ECO:0000250|UniProtKB:Q5JTJ3}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:18614015}. Mitochondrion intermembrane space {ECO:0000250|UniProtKB:Q5JTJ3}. SUBUNIT: Found in a complex with TMEM177, COX20, MT-CO2/COX2, COX18, SCO1 and SCO2. Interacts with COA1, MT-CO2/COX2, SCO1, SCO2 and COX20. Interacts with COX20 in a MT-CO2/COX2- and COX18-dependent manner. Interacts with COX16. {ECO:0000250|UniProtKB:Q5JTJ3}. +Q921H9 COA7_MOUSE Cytochrome c oxidase assembly factor 7 (Beta-lactamase hcp-like protein) (Respiratory chain assembly factor 1) (Sel1 repeat-containing protein 1) 231 25,617 Chain (1); Initiator methionine (1); Modified residue (1); Repeat (5) FUNCTION: Required for assembly of mitochondrial respiratory chain complex I and complex IV. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion intermembrane space {ECO:0000250}. +Q05306 COAA1_MOUSE Collagen alpha-1(X) chain 680 66,775 Chain (1); Domain (1); Metal binding (5); Region (3); Sequence conflict (16); Signal peptide (1) FUNCTION: Type X collagen is a product of hypertrophic chondrocytes and has been localized to presumptive mineralization zones of hyaline cartilage. PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. SUBUNIT: Homotrimer. +Q5NBX1 COBL_MOUSE Protein cordon-bleu 1337 143,865 Alternative sequence (7); Beta strand (1); Chain (1); Compositional bias (3); Domain (3); Erroneous initiation (1); Frameshift (1); Helix (3); Modified residue (15); Motif (2); Sequence conflict (12); Turn (2) FUNCTION: Plays an important role in the reorganization of the actin cytoskeleton. Binds to and sequesters actin monomers (G actin). Nucleates actin polymerization by assembling three actin monomers in cross-filament orientation and thereby promotes growth of actin filaments at the barbed end. Can also mediate actin depolymerization at barbed ends and severing of actin filaments. Promotes formation of cell ruffles. Regulates neuron morphogenesis and increases branching of axons and dendrites. Regulates dendrite branching in Purkinje cells. {ECO:0000269|PubMed:17956734, ECO:0000269|PubMed:23223303}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, cytoskeleton. Cell projection, ruffle. Cytoplasm. Note=Recruited to the cell membrane via interaction with PACSIN1 (By similarity). Colocalizes with the actin cytoskeleton. Detected throughout the neuron cell body, as well as in axons and dendrites. {ECO:0000250}. SUBUNIT: Identified in a complex composed of COBL, PACSIN1 and WASL. Interacts with PACSIN1, PACSIN2 and PACSIN3 (By similarity). Identified in a complex composed of ACTA1, COBL, GSN AND TMSB4X. Interacts (via WH2 domains) with actin monomers. Interacts with DBNL. {ECO:0000250, ECO:0000269|PubMed:17956734, ECO:0000269|PubMed:23009842, ECO:0000269|PubMed:23223303}. TISSUE SPECIFICITY: Detected in brain cortex and in the Purkinje cell layer in the cerebellum. Detected in hippocampus neurons, and at lower levels in testis, lung and spleen (at protein level). Detected in embryonic neural tube. {ECO:0000269|PubMed:14512015, ECO:0000269|PubMed:17956734, ECO:0000269|PubMed:23223303, ECO:0000269|PubMed:7586755}. +Q9DB20 ATPO_MOUSE ATP synthase subunit O, mitochondrial (ATP synthase peripheral stalk subunit OSCP) (Oligomycin sensitivity conferral protein) (OSCP) 213 23,364 Chain (1); Modified residue (15); Transit peptide (1) FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements. PTM: Acetylation of Lys-70 and Lys-158 is observed in liver mitochondria from fasted mice but not from fed mice.; PTM: Acetylation at Lys-162 decreases ATP production. Deacetylated by SIRT3 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Mitochondrion inner membrane {ECO:0000250}. SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Component of an ATP synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MD and MP68 (By similarity). {ECO:0000250}. +Q9WU60 ATRN_MOUSE Attractin (Protein mahogany) 1428 158,058 Chain (1); Disulfide bond (16); Domain (9); Frameshift (1); Glycosylation (25); Propeptide (1); Repeat (6); Sequence conflict (12); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1279 1299 Helical. {ECO:0000255}. TOPO_DOM 83 1278 Extracellular. {ECO:0000255}.; TOPO_DOM 1300 1428 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in the initial immune cell clustering during inflammatory response and may regulate chemotactic activity of chemokines (By similarity). May play a role in melanocortin signaling pathways that regulate energy homeostasis and hair color. Low-affinity receptor for agouti. Has a critical role in normal myelination in the central nervous system (By similarity). {ECO:0000250, ECO:0000269|PubMed:11137996}. PTM: Heavily glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O75882}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:O75882}. SUBUNIT: Monomer and homotrimer. {ECO:0000250}. +P59511 ATS20_MOUSE A disintegrin and metalloproteinase with thrombospondin motifs 20 (ADAM-TS 20) (ADAM-TS20) (ADAMTS-20) (EC 3.4.24.-) 1906 212,068 Active site (1); Alternative sequence (2); Chain (1); Compositional bias (1); Disulfide bond (11); Domain (18); Glycosylation (10); Metal binding (3); Propeptide (1); Region (1); Sequence conflict (3); Signal peptide (1) FUNCTION: May play a role in tissue-remodeling process occurring in both normal and pathological conditions. May have a protease-independent function in the transport from the endoplasmic reticulum to the Golgi apparatus of secretory cargos, mediated by the GON domain. PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}.; PTM: Glycosylated. Can be O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS family members. Also can be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated. These other glycosylations can also facilitate secretion (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. TISSUE SPECIFICITY: Expressed at low level in testis and brain. DISEASE: Note=Defects in Adamts20 are the cause of the belted (bt) phenotype. It is a pigmental defect which occurs as a result of a defect in melanocyte development. {ECO:0000269|PubMed:12925592}. +Q4VC17 ATS18_MOUSE A disintegrin and metalloproteinase with thrombospondin motifs 18 (ADAM-TS 18) (ADAM-TS18) (ADAMTS-18) (EC 3.4.24.-) 1219 135,244 Active site (1); Chain (1); Compositional bias (1); Disulfide bond (11); Domain (7); Glycosylation (6); Metal binding (3); Propeptide (1); Sequence conflict (3); Signal peptide (1) PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}.; PTM: Glycosylated. Can be O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS family members. Also can be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated. These other glycosylations can also facilitate secretion (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. +P59509 ATS19_MOUSE A disintegrin and metalloproteinase with thrombospondin motifs 19 (ADAM-TS 19) (ADAM-TS19) (ADAMTS-19) (EC 3.4.24.-) 1210 134,561 Active site (1); Chain (1); Compositional bias (1); Disulfide bond (14); Domain (8); Glycosylation (7); Metal binding (4); Motif (1); Propeptide (1); Region (1); Signal peptide (1) PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}.; PTM: Glycosylated. Can be O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS family members. Also can be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated. These other glycosylations can also facilitate secretion (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. DOMAIN: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme. TISSUE SPECIFICITY: Expressed predominantly in fetal ovary, low levels of expression is also detected in kidney, heart, skeletal muscle, lung and testis. +P28658 ATX10_MOUSE Ataxin-10 (Brain protein E46) (Spinocerebellar ataxia type 10 protein homolog) 475 53,707 Chain (1); Frameshift (1); Modified residue (3); Sequence conflict (1) FUNCTION: Necessary for the survival of cerebellar neurons. Induces neuritogenesis by activating the Ras-MAP kinase pathway. May play a role in the maintenance of a critical intracellular glycosylation level and homeostasis. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}. SUBUNIT: Homooligomer (By similarity). Interacts with GNB2 (By similarity). Interacts with OGT. Interacts with IQCB1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: In high cell density areas; cerebellar cortex, dentate gyrus, hippocampus, anterior olfactory nucleus, primary olfactory cortex. {ECO:0000269|PubMed:15201271}. +Q99LS0 AUGN_MOUSE Augurin (Esophageal cancer-related gene 4 protein homolog) 148 16,992 Peptide (1); Propeptide (2); Sequence conflict (1); Signal peptide (1) FUNCTION: Probable hormone that may attenuate cell proliferation and induce senescence of oligodendrocyte and neural precursor cells in the central nervous system (PubMed:20404145). ECRG4-induced senescence is characterized by G1 arrest, RB1 dephosphorylation and accelerated CCND1 and CCND3 proteasomal degradation (PubMed:20404145). {ECO:0000269|PubMed:20404145}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17284679, ECO:0000269|PubMed:20404145}. Cytoplasm {ECO:0000250|UniProtKB:Q9H1Z8}. Apical cell membrane {ECO:0000250|UniProtKB:Q9H1Z8}. TISSUE SPECIFICITY: Expressed in the intermediate lobe of pituitary, glomerular layer of adrenal cortex, choroid plexus and atrioventricular node of the heart (PubMed:17284679). Expressed in the brain with high expression in the choroid plexus and the epithelial lining of the central canal and expression in the gray matter of the spinal cord (at protein level) (PubMed:21349154). {ECO:0000269|PubMed:17284679, ECO:0000269|PubMed:21349154}. +Q9JLZ3 AUHM_MOUSE Methylglutaconyl-CoA hydratase, mitochondrial (EC 4.2.1.18) (AU-specific RNA-binding enoyl-CoA hydratase) (AU-binding enoyl-CoA hydratase) (muAUH) (Itaconyl-CoA hydratase) (EC 4.2.1.56) 314 33,395 Alternative sequence (4); Chain (1); Modified residue (14); Region (1); Sequence conflict (4); Transit peptide (1) Amino-acid degradation; L-leucine degradation; (S)-3-hydroxy-3-methylglutaryl-CoA from 3-isovaleryl-CoA: step 3/3. FUNCTION: Catalyzes the conversion of 3-methylglutaconyl-CoA to 3-hydroxy-3-methylglutaryl-CoA (By similarity). Also has itaconyl-CoA hydratase activity by converting itaconyl-CoA into citramalyl-CoA in the C5-dicarboxylate catabolism pathway (By similarity). The C5-dicarboxylate catabolism pathway is required to detoxify itaconate, a vitamin B12-poisoning metabolite (By similarity). Has very low enoyl-CoA hydratase activity (PubMed:10072761). Was originally identified as RNA-binding protein that binds in vitro to clustered 5'-AUUUA-3' motifs (PubMed:10072761). {ECO:0000250|UniProtKB:Q13825, ECO:0000269|PubMed:10072761}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:10072761}. SUBUNIT: Homohexamer. {ECO:0000250|UniProtKB:Q13825}. TISSUE SPECIFICITY: Detected in heart, brain, liver, spleen, skeletal muscle and kidney. {ECO:0000269|PubMed:10072761}. +O70126 AURKB_MOUSE Aurora kinase B (EC 2.7.11.1) (Aurora 1) (Aurora- and IPL1-like midbody-associated protein 1) (Aurora/IPL1-related kinase 2) (ARK-2) (Aurora-related kinase 2) (STK-1) (Serine/threonine-protein kinase 12) (Serine/threonine-protein kinase 5) (Serine/threonine-protein kinase aurora-B) 345 39,384 Active site (1); Binding site (1); Chain (1); Domain (1); Modified residue (4); Nucleotide binding (1); Sequence conflict (4) FUNCTION: Serine/threonine-protein kinase component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Involved in the bipolar attachment of spindle microtubules to kinetochores and is a key regulator for the onset of cytokinesis during mitosis. Required for central/midzone spindle assembly and cleavage furrow formation. Key component of the cytokinesis checkpoint, a process required to delay abscission to prevent both premature resolution of intercellular chromosome bridges and accumulation of DNA damage: phosphorylates CHMP4C, leading to retain abscission-competent VPS4 (VPS4A and/or VPS4B) at the midbody ring until abscission checkpoint signaling is terminated at late cytokinesis. AURKB phosphorylates the CPC complex subunits BIRC5/survivin, CDCA8/borealin and INCENP. Phosphorylation of INCENP leads to increased AURKB activity. Other known AURKB substrates involved in centromeric functions and mitosis are CENPA, DES/desmin, GPAF, KIF2C, NSUN2, RACGAP1, SEPT1, VIM/vimentin, HASPIN and histone H3. A positive feedback loop involving HASPIN and AURKB contributes to localization of CPC to centromeres. Phosphorylation of VIM controls vimentin filament segregation in cytokinetic process, whereas histone H3 is phosphorylated at 'Ser-10' and 'Ser-28' during mitosis (H3S10ph and H3S28ph, respectively). AURKB is also required for kinetochore localization of BUB1 and SGO1. Phosphorylation of p53/TP53 negatively regulates its transcriptional activity. Key regulator of active promoters in resting B- and T-lymphocytes: acts by mediating phosphorylation of H3S28ph at active promoters in resting B-cells, inhibiting RNF2/RING1B-mediated ubiquitination of histone H2A and enhancing binding and activity of the USP16 deubiquitinase at transcribed genes. {ECO:0000269|PubMed:11784863, ECO:0000269|PubMed:24034696}. PTM: The phosphorylation of Thr-237 requires the binding to INCENP and occurs by means of an autophosphorylation mechanism. Thr-237 phosphorylation is indispensable for the AURKB kinase activity (By similarity). {ECO:0000250}.; PTM: Ubiquitinated by different BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complexes. Ubiquitinated by the BCR(KLHL9-KLHL13) E3 ubiquitin ligase complex, ubiquitination leads to removal from mitotic chromosomes and is required for cytokinesis. During anaphase, the BCR(KLHL21) E3 ubiquitin ligase complex recruits the CPC complex from chromosomes to the spindle midzone and mediates the ubiquitination of AURKB. Ubiquitination of AURKB by BCR(KLHL21) E3 ubiquitin ligase complex may not lead to its degradation by the proteasome (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}. Chromosome, centromere {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Midbody {ECO:0000250}. Note=Localizes on chromosome arms and inner centromeres from prophase through metaphase and then transferring to the spindle midzone and midbody from anaphase through cytokinesis. Colocalized with gamma tubulin in the mid-body (By similarity). Proper localization of the active, Thr-237-phosphorylated form during metaphase may be dependent upon interaction with SPDYC. Colocalized with SIRT2 during cytokinesis with the midbody. Localization (and probably targeting of the CPC) to the inner centromere occurs predominantly in regions with overlapping mitosis-specific histone phosphorylations H3pT3 and H2ApT12 (By similarity). {ECO:0000250}. SUBUNIT: Component of the chromosomal passenger complex (CPC) composed of at least BIRC5/survivin, CDCA8/borealin, INCENP, AURKB or AURKC; predominantly independent AURKB- and AURKC-containing complexes exist (By similarity). Associates with RACGAP1 during M phase. Interacts with CDCA1, EVI5, JTB, NDC80, PSMA3, SEPT1, SIRT2 and TACC1 (By similarity). Interacts with SPDYC; this interaction may be required for proper localization of active, Thr-237-phosphorylated AURKB form during prometaphase and metaphase. Interacts with p53/TP53. Interacts (via the middle kinase domain) with NOC2L (via the N- and C-terminus domains) (By similarity). Interacts with TTC28 (By similarity). Interacts with RNF2/RING1B. {ECO:0000250, ECO:0000269|PubMed:24034696}. TISSUE SPECIFICITY: Expressed in testis, intestine and spleen. All of them are tissues that contain a large number of proliferating cells. Expressed during S phase, in a cell-cycle-dependent fashion. +O88445 AURKC_MOUSE Aurora kinase C (EC 2.7.11.1) (Aurora 3) (Aurora/IPL1-related kinase 3) (ARK-3) (Aurora-related kinase 3) (Aurora/IPL1/Eg2 protein 1) (Serine/threonine-protein kinase 13) (Serine/threonine-protein kinase aurora-C) 282 32,907 Active site (1); Binding site (1); Chain (1); Domain (1); Modified residue (1); Mutagenesis (2); Nucleotide binding (1); Sequence conflict (1) FUNCTION: Serine/threonine-protein kinase component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Plays also a role in meiosis and more particularly in spermatogenesis. Has redundant cellular functions with AURKB and can rescue an AURKB knockdown. Like AURKB, AURKC phosphorylates histone H3 at 'Ser-10' and 'Ser-28'. AURKC phosphorylates the CPC complex subunits BIRC5/survivin and INCENP leading to increased AURKC activity. Phosphorylates TACC1, another protein involved in cell division, at 'Ser-228'. {ECO:0000269|PubMed:11879579, ECO:0000269|PubMed:21613325}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}. Chromosome, centromere {ECO:0000250|UniProtKB:Q9UQB9}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9UQB9}. Note=Distributes in the condensed chromosomes during prophase to metaphase. After entering anaphase, there is a dissociation from separated chromosomes and a redistribution to midzone microtubules, and finally remains in the midbody during cytokinesis (By similarity). {ECO:0000250|UniProtKB:Q9UQB9}. SUBUNIT: Component of the chromosomal passenger complex (CPC) composed of at least BIRC5/survivin, CDCA8/borealin, INCENP, AURKB or AURKC; predominantly independent AURKB- and AURKC-containing complexes exist; in the complex interacts directly with BIRC5/survivin and INCENP. Interacts with TACC1. {ECO:0000250|UniProtKB:Q9UQB9}. TISSUE SPECIFICITY: Expressed only in testis. +Q60847 COCA1_MOUSE Collagen alpha-1(XII) chain 3120 340,214 Alternative sequence (5); Chain (1); Compositional bias (1); Domain (27); Glycosylation (8); Modified residue (14); Motif (3); Region (5); Sequence conflict (22); Signal peptide (1) FUNCTION: Type XII collagen interacts with type I collagen-containing fibrils, the COL1 domain could be associated with the surface of the fibrils, and the COL2 and NC3 domains may be localized in the perifibrillar matrix. {ECO:0000250}. PTM: The triple-helical tail is stabilized by disulfide bonds at each end. {ECO:0000250}.; PTM: Hydroxylation on proline residues within the sequence motif, GXPG, is most likely to be 4-hydroxy as this fits the requirement for 4-hydroxylation in vertebrates. {ECO:0000250}.; PTM: O-glycosylation of isoform 2; glycosaminoglycan of chondroitin-sulfate type. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. SUBUNIT: Trimer of identical chains each containing 190 kDa of non-triple-helical sequences. {ECO:0000250}. TISSUE SPECIFICITY: Highest expression in tendons, perichondrium, skin, cornea, sclera, blood vessels, and periosteum. +Q62507 COCH_MOUSE Cochlin (COCH-5B2) 552 59,950 Chain (1); Disulfide bond (2); Domain (3); Glycosylation (2); Signal peptide (1) FUNCTION: Plays a role in the control of cell shape and motility in the trabecular meshwork. {ECO:0000250}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:O43405}. SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250|UniProtKB:O43405}. SUBUNIT: Monomer. May form homodimer. Interacts with type II collagen. Interacts with SLC44A2. Interacts with ANXA2. {ECO:0000250|UniProtKB:O43405}. TISSUE SPECIFICITY: Expressed in inner ear structures. +Q9R1N9 CODA1_MOUSE Collagen alpha-1(XIII) chain 751 73,172 Alternative sequence (1); Chain (1); Glycosylation (1); Region (7); Topological domain (2); Transmembrane (1) TRANSMEM 41 59 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 40 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 60 751 Extracellular. {ECO:0000255}. FUNCTION: Involved in cell-matrix and cell-cell adhesion interactions that are required for normal development. May participate in the linkage between muscle fiber and basement membrane. May play a role in endochondral ossification of bone and branching morphogenesis of lung. Binds heparin. At neuromuscular junctions, may play a role in acetylcholine receptor clustering (PubMed:26626625). {ECO:0000250|UniProtKB:Q5TAT6, ECO:0000269|PubMed:11566879, ECO:0000269|PubMed:11583983, ECO:0000269|PubMed:16007336, ECO:0000269|PubMed:26626625}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9624150}; Single-pass type II membrane protein {ECO:0000269|PubMed:9624150}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000250|UniProtKB:Q5TAT6}. SUBUNIT: Homotrimer; disulfide-linked. Nucleation of the type XIII collagen triple helix is likely to occur at the N-terminal region with triple helix formation proceeding from the N- to the C-terminus. Interacts with FN1, perlecan/HSPG2 and NID2 (By similarity). {ECO:0000250}. +Q9D9K3 AVEN_MOUSE Cell death regulator Aven 342 37,195 Chain (1); Compositional bias (1); Modified residue (2); Sequence conflict (1) FUNCTION: Protects against apoptosis mediated by Apaf-1. {ECO:0000250}. SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Associated with intracellular membranes. {ECO:0000250}. SUBUNIT: Binds Apaf-1, BCL-2 and BAD (Bcl-xl). {ECO:0000250}. +Q80U56 AVL9_MOUSE Late secretory pathway protein AVL9 homolog 649 72,186 Chain (1); Domain (3); Erroneous initiation (1); Modified residue (2); Transmembrane (1) TRANSMEM 204 229 Helical. {ECO:0000255}. FUNCTION: Functions in cell migration. {ECO:0000250}. SUBCELLULAR LOCATION: Recycling endosome {ECO:0000250}. Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q9D7H4 AVPI1_MOUSE Arginine vasopressin-induced protein 1 (AVP-induced protein 1) (Arginine vasopressin-induced transcript 32 protein) (VIP32) (VIT32) 142 15,802 Chain (1) FUNCTION: May be involved in MAP kinase activation, epithelial sodium channel (ENaC) down-regulation and cell cycling. {ECO:0000269|PubMed:12356727}. +Q07802 COE1_MOUSE Transcription factor COE1 (O/E-1) (OE-1) (Early B-cell factor) 591 64,464 Alternative sequence (1); Beta strand (24); Chain (1); Compositional bias (1); Cross-link (2); Domain (1); Helix (8); Modified residue (1); Mutagenesis (5); Region (3); Sequence conflict (2); Site (2); Turn (5); Zinc finger (1) FUNCTION: Transcriptional activator which recognizes variations of the palindromic sequence 5'-ATTCCCNNGGGAATT-3'. {ECO:0000269|PubMed:20876732}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Interacts with ZNF423 and ZNF521, leading to prevent EBF1 to bind DNA and activate target genes (By similarity). Forms either a homodimer or a heterodimer with a related family member. {ECO:0000250, ECO:0000269|PubMed:20876732, ECO:0000269|PubMed:9151732}. TISSUE SPECIFICITY: Expressed at high levels in early B-cells, spleen, lymph node and adipose tissue, and at low levels in heart, brain, skeletal muscle and kidney. In adult expressed in olfactory epithelium, in spleen, and at a lesser extent in Purkinje cells of the cerebellum, heart, kidney, lung, thymus and testis. In embryo expressed in dorsal thalamus and epithalamus, at a lower level in mesencephalon and in the caudal rhombencephalon, in the postmitotic cells of developing retina, highly in developing spinal cord, dorsal root ganglia, trigeminal ganglia and in glossopharyngeal nerve ganglia, in developing inner ear. +O08792 COE2_MOUSE Transcription factor COE2 (Early B-cell factor 2) (EBF-2) (Metencephalon-mesencephalon-olfactory transcription factor 1) (MET-mesencephalon-olfactory TF1) (MET-mesencephalon-olfactory transcription factor 1) (Olf-1/EBF-like 3) (O/E-3) (OE-3) 575 62,606 Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (1); Region (3); Sequence conflict (1); Site (2); Zinc finger (1) FUNCTION: Transcription factor that, in osteoblasts, activates the decoy receptor for RANKL, TNFRSF11B, which in turn regulates osteoclast differentiation. Acts in synergy with the Wnt-responsive LEF1/CTNNB1 pathway. Recognizes variations of the palindromic sequence 5'-ATTCCCNNGGGAATT-3'. {ECO:0000269|PubMed:16326388}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Forms either a homodimer or a heterodimer with a related family member. {ECO:0000269|PubMed:9151732}. TISSUE SPECIFICITY: In adult expressed in olfactory epithelium and at a much lower level in Purkinje cells of the cerebellum. In embryo expressed in epithalamus, in cells near the ventricular zone of mesencephalon and on the ventral surface of rhombencephalon, in the developing vomeronasal organ, at a lower level in developing spinal cord. Not expressed in developing retina, inner ear, dorsal root ganglia, trigeminal ganglia and glossopharyngeal ganglia. +O08791 COE3_MOUSE Transcription factor COE3 (Early B-cell factor 3) (EBF-3) (Olf-1/EBF-like 2) (O/E-2) (OE-2) 596 64,878 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (1); Region (3); Site (2); Zinc finger (1) FUNCTION: Transcriptional activator (PubMed:9151732). Recognizes variations of the palindromic sequence 5'-ATTCCCNNGGGAATT-3' (By similarity). {ECO:0000250|UniProtKB:Q07802, ECO:0000269|PubMed:9151732}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H4W6}. SUBUNIT: Forms either a homodimer or a heterodimer with a related family member. {ECO:0000269|PubMed:9151732}. TISSUE SPECIFICITY: Highly expressed in adult olfactory epithelium. In embryo, expressed in epithalamus, hypothalamus, throughout the brainstem and near the ventricular zones of mesencephalon, in rostral rhombencephalon, in vomeronasal organ, at high level in developing retina, developing spinal cord, at low level in dorsal root ganglia, trigeminal ganglia, glossopharyngeal nerve ganglia. Not expressed in developing inner eat. +Q80X19 COEA1_MOUSE Collagen alpha-1(XIV) chain 1797 193,013 Alternative sequence (1); Chain (1); Domain (16); Glycosylation (5); Motif (1); Region (3); Sequence conflict (4); Signal peptide (1) FUNCTION: Plays an adhesive role by integrating collagen bundles. It is probably associated with the surface of interstitial collagen fibrils via COL1. The COL2 domain may then serve as a rigid arm which sticks out from the fibril and protrudes the large N-terminal globular domain into the extracellular space, where it might interact with other matrix molecules or cell surface receptors (By similarity). {ECO:0000250}. PTM: Lysines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in all cases and bind carbohydrates. {ECO:0000250|UniProtKB:P32018}.; PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. {ECO:0000250|UniProtKB:P32018}.; PTM: May contain numerous cysteine residues involved in inter- and intramolecular disulfide bonding. {ECO:0000250|UniProtKB:P32018}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P32018}. SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:P32018}. +Q6E1M8 AWAT2_MOUSE Acyl-CoA wax alcohol acyltransferase 2 (EC 2.3.1.75) (Acyl-CoA retinol O-fatty-acyltransferase) (ARAT) (Retinol O-fatty-acyltransferase) (EC 2.3.1.76) (Diacylglycerol O-acyltransferase 2-like protein 4) (Long-chain-alcohol O-fatty-acyltransferase 2) (Wax synthase) (mWS) 333 38,145 Alternative sequence (1); Chain (1); Transmembrane (3) TRANSMEM 15 35 Helical. {ECO:0000255}.; TRANSMEM 38 58 Helical. {ECO:0000255}.; TRANSMEM 130 150 Helical. {ECO:0000255}. FUNCTION: Acyltransferase that predominantly esterify long chain (wax) alcohols with acyl-CoA-derived fatty acids to produce wax esters. Wax esters are enriched in sebum, suggesting that it plays a central role in lipid metabolism in skin. Has no activity using decyl alcohol and significantly prefers the C16 and C18 alcohols. May also have 2-acylglycerol O-acyltransferase (MGAT) and acyl-CoA:retinol acyltransferase (ARAT) activities, to catalyze the synthesis of diacylglycerols and retinyl esters; however this activity is unclear in vivo (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +P18760 COF1_MOUSE Cofilin-1 (Cofilin, non-muscle isoform) 166 18,560 Chain (1); Cross-link (1); Domain (1); Initiator methionine (1); Modified residue (11); Motif (1) FUNCTION: Binds to F-actin and exhibits pH-sensitive F-actin depolymerizing activity (PubMed:11809832). Regulates actin cytoskeleton dynamics. Important for normal progress through mitosis and normal cytokinesis. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required for the up-regulation of atypical chemokine receptor ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation (By similarity). Required for neural tube morphogenesis and neural crest cell migration (PubMed:15649475). {ECO:0000250|UniProtKB:P23528, ECO:0000269|PubMed:11809832, ECO:0000269|PubMed:15649475}. PTM: Inactivated by phosphorylation on Ser-3. Phosphorylated on Ser-3 in resting cells (PubMed:25107909). Dephosphorylated by PDXP/chronophin; this restores its activity in promoting actin filament depolymerization. The phosphorylation of Ser-24 may prevent recognition of the nuclear localization signal (By similarity). Phosphorylated via a ARRB1-RAC1-LIMK1-PAK1 cascade upon active ligand stimulation of atypical chemokine receptor ACKR2 (By similarity). {ECO:0000250, ECO:0000269|PubMed:25107909}. SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000250|UniProtKB:P10668}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P10668}. Cell projection, ruffle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250|UniProtKB:P10668}; Cytoplasmic side {ECO:0000250|UniProtKB:P10668}. Cell projection, lamellipodium membrane {ECO:0000250|UniProtKB:P10668}; Peripheral membrane protein {ECO:0000250|UniProtKB:P10668}; Cytoplasmic side {ECO:0000250|UniProtKB:P10668}. Cell projection, lamellipodium {ECO:0000269|PubMed:25107909}. Note=Colocalizes with the actin cytoskeleton in membrane ruffles and lamellipodia. Detected at the cleavage furrow and contractile ring during cytokinesis. Almost completely in nucleus in cells exposed to heat shock (By similarity). {ECO:0000250|UniProtKB:P10668}. SUBUNIT: Can bind G- and F-actin in a 1:1 ratio of cofilin to actin. It is a major component of intranuclear and cytoplasmic actin rods. {ECO:0000250|UniProtKB:P10668}. TISSUE SPECIFICITY: Widely distributed in various tissues. Not found in skeletal muscle. {ECO:0000269|PubMed:11809832}. +P45591 COF2_MOUSE Cofilin-2 (Cofilin, muscle isoform) 166 18,710 Chain (1); Domain (1); Initiator methionine (1); Modified residue (3); Motif (1) FUNCTION: Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. It is the major component of intranuclear and cytoplasmic actin rods. Required for muscle maintenance. May play a role during the exchange of alpha-actin forms during the early postnatal remodeling of the sarcomere. {ECO:0000269|PubMed:11809832, ECO:0000269|PubMed:22343409, ECO:0000269|PubMed:24598388}. PTM: The phosphorylation of Ser-24 may prevent recognition of the nuclear localization signal. SUBCELLULAR LOCATION: Nucleus matrix. Cytoplasm, cytoskeleton. Note=Colocalizes with CSPR3 in the Z line of sarcomeres. {ECO:0000250|UniProtKB:Q9Y281}. SUBUNIT: Interacts with CSRP3; possibly two molecules of CFL2 can interact with one molecule if CSRP3. {ECO:0000250|UniProtKB:Q9Y281}. TISSUE SPECIFICITY: Predominantly expressed in skeletal muscle. {ECO:0000269|PubMed:11809832}. +O35625 AXIN1_MOUSE Axin-1 (Axis inhibition protein 1) (Protein Fused) 863 96,276 Alternative sequence (1); Beta strand (1); Chain (1); Cross-link (2); Domain (2); Erroneous initiation (1); Modified residue (8); Motif (1); Mutagenesis (8); Region (6); Sequence conflict (3) FUNCTION: Component of the beta-catenin destruction complex required for regulating CTNNB1 levels through phosphorylation and ubiquitination, and modulating Wnt-signaling (By similarity). Controls dorsoventral patterning via two opposing effects; down-regulates CTNNB1 to inhibit the Wnt signaling pathway and ventralize embryos, but also dorsalizes embryos by activating a Wnt-independent JNK signaling pathway. In Wnt signaling, probably facilitates the phosphorylation of CTNNB1 and APC by GSK3B. Likely to function as a tumor suppressor. Facilitates the phosphorylation of TP53 by HIPK2 upon ultraviolet irradiation. Enhances TGF-beta signaling by recruiting the RNF111 E3 ubiquitin ligase and promoting the degradation of inhibitory SMAD7 (By similarity). Also component of the AXIN1-HIPK2-TP53 complex which controls cell growth, apoptosis and development. {ECO:0000250, ECO:0000269|PubMed:12223491, ECO:0000269|PubMed:15526030, ECO:0000269|PubMed:17681137}. PTM: Phosphorylation and dephosphorylation of AXIN1 regulates assembly and function of the beta-catenin complex. Phosphorylated by CK1 and GSK3B. Dephosphorylated by PPP1CA and PPP2CA. Phosphorylation by CK1 enhances binding of GSK3B to AXIN1 (By similarity). Also phosphorylated by CDK2 which regulates interaction with CTNBB1. {ECO:0000250, ECO:0000269|PubMed:10581160, ECO:0000269|PubMed:15063782}.; PTM: ADP-ribosylated by tankyrase TNKS and TNKS2. Poly-ADP-ribosylated protein is recognized by RNF146, followed by ubiquitination and subsequent activation of the Wnt signaling pathway (By similarity). {ECO:0000250}.; PTM: Ubiquitinated by RNF146 when poly-ADP-ribosylated, leading to its degradation and subsequent activation of the Wnt signaling pathway. Deubiquitinated by USP34, deubiquitinated downstream of beta-catenin stabilization step: deubiquitination is important for nuclear accumulation during Wnt signaling to positively regulate beta-catenin (CTNBB1)-mediated transcription (By similarity). Sumoylation at Lys-858 and Lys-861 prevents ubiquitination and degradation. Sumoylation is required for AXIN1-mediated JNK activation. {ECO:0000250, ECO:0000269|PubMed:12223491, ECO:0000269|PubMed:18632848}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16815997, ECO:0000269|PubMed:19141611}. Nucleus {ECO:0000250|UniProtKB:O15169}. Cell membrane {ECO:0000269|PubMed:16815997}. Membrane {ECO:0000269|PubMed:19141611}. Note=On UV irradiation, translocates to the nucleus and colocalizes with DAAX (By similarity). MACF1 is required for its translocation to cell membrane (PubMed:16815997). {ECO:0000250|UniProtKB:O15169, ECO:0000269|PubMed:16815997}. SUBUNIT: Homodimer (PubMed:17681137). Component of the beta-catenin destruction complex, containing at least CTNNB1, an axin and GSK3B, that regulates CTNNB1 protein levels through phosphorylation and ubiquitination (By similarity). Interacts with GSK3B; the interaction hyperphosphorylates CTNNB1 leading to its ubiquitination and destruction (By similarity). Interacts with DAXX; the interaction stimulates the interaction of DAXX with TP53, stimulates 'Ser-46' phosphorylation of TP53 and induces cell death on UV irradiation (By similarity). Also interacts with APC, RNF111, SMAD6 and SMAD7 (By similarity). Interacts (via the C-terminal) with PPP1CA; the interaction dephosphorylates AXIN1 and regulates interaction with GSK3B (By similarity). Interacts with PPP2CA; the interaction dephosphorylates AXIN1 (By similarity). Interacts with MDFI; the interaction decreases AXIN1-mediated JUN N-terminal kinase (JNK) activation (By similarity). Interacts with MDFIC; the interaction inhibits beta-cateninin-mediated signaling and AXIN1-mediated JUN N-terminal kinase (JNK) activation (By similarity). Binds ANKRD6, PIAS1, PIAS2, PIAS4, SUMO1, MAP3K1 and MAP3K4 (PubMed:12183362, PubMed:12223491). Component of the AXIN1-HIPK2-TP53 complex (PubMed:15526030). Interacts directly in the complex with TP53 and HIPK2 (PubMed:15526030). Interacts with DIXDC1; the interaction prevents interaction with MAP3K1 (PubMed:15262978). Interacts with AIDA; the interaction blocks the AXIN1-mediated JNK activation through disrupting AXIN1 homodimerization and Wnt signaling (PubMed:17681137). Interacts with LRP5 (via its phosphorylated PPPSP motifs); the interaction is stimulated by WNT1 and GSK3B and activates beta-catenin signaling (PubMed:11336703). Interacts with CTNNB1 (via the armadillo repeats 2-7) (PubMed:10581160, PubMed:15063782). Interacts with MACF1 (By similarity). Found in a complex composed of MACF1, APC, AXIN1, CTNNB1 and GSK3B (By similarity). Interacts with TNKS (By similarity). Interacts with DAB2; the interaction is mutually exclusive with the AXIN1:PPP1CA interaction (PubMed:19581931). Interacts with ZBED3 (via PPPSP motif); the interaction is direct, enhanced by protein kinase GSK3B and casein kinase CSNK1E activities and decreases GSK3B-induced beta-catenin serine and threonine phosphorylations (PubMed:19141611). Interacts with WDR26 (By similarity). Interacts with GID8 (By similarity). {ECO:0000250|UniProtKB:O15169, ECO:0000250|UniProtKB:O70239, ECO:0000269|PubMed:10581160, ECO:0000269|PubMed:11336703, ECO:0000269|PubMed:12183362, ECO:0000269|PubMed:12223491, ECO:0000269|PubMed:15063782, ECO:0000269|PubMed:15262978, ECO:0000269|PubMed:15526030, ECO:0000269|PubMed:17681137, ECO:0000269|PubMed:19141611, ECO:0000269|PubMed:19581931}. DOMAIN: The tankyrase-binding motif (also named TBD) is required for interaction with tankyrase TNKS and TNKS2. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in embryonic stem cells. +O88566 AXIN2_MOUSE Axin-2 (Axin-like protein) (Axil) (Axis inhibition protein 2) (Conductin) 840 92,906 Chain (1); Compositional bias (1); Domain (2); Motif (1); Region (2); Sequence conflict (7) FUNCTION: Inhibitor of the Wnt signaling pathway. Down-regulates beta-catenin. Probably facilitate the phosphorylation of beta-catenin and APC by GSK3B (By similarity). {ECO:0000250}. PTM: Probably phosphorylated by GSK3B and dephosphorylated by PP2A. {ECO:0000250}.; PTM: ADP-ribosylated by tankyrase TNKS and TNKS2. Poly-ADP-ribosylated protein is recognized by RNF146, followed by ubiquitination and subsequent activation of the Wnt signaling pathway (By similarity). {ECO:0000250}.; PTM: Ubiquitinated by RNF146 when poly-ADP-ribosylated, leading to its degradation and subsequent activation of the Wnt signaling pathway. Deubiquitinated by USP34, deubiquitinated downstream of beta-catenin stabilization step: deubiquitination is important Wnt signaling to positively regulate beta-catenin (CTNBB1)-mediated transcription (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with glycogen synthase kinase-3 beta (GSK3B) and beta-catenin. The interaction between axin and beta-catenin occurs via the armadillo repeats contained in beta-catenin. Interacts with SMAD7 and RNF111 (By similarity). Interacts with ANKRD6. {ECO:0000250, ECO:0000269|PubMed:12183362}. DOMAIN: The tankyrase-binding motif (also named TBD) is required for interaction with tankyrase TNKS and TNKS2. {ECO:0000250}. +Q8BVM4 AZIN2_MOUSE Antizyme inhibitor 2 (AzI2) (Arginine decarboxylase-like protein) (ADC) (ARGDC) (Ornithine decarboxylase-like protein) (ODC-like protein) (ornithine decarboxylase paralog) (ODC-p) 459 49,503 Chain (1); Mutagenesis (5); Region (1); Sequence conflict (1) FUNCTION: Antizyme inhibitor (AZI) protein that positively regulates ornithine decarboxylase (ODC) activity and polyamine uptake. AZI is an enzymatically inactive ODC homolog that counteracts the negative effect of ODC antizymes (AZs) OAZ1, OAZ2 and OAZ3 on ODC activity by competing with ODC for antizyme-binding (PubMed:18062773, PubMed:18508777, PubMed:18973822). Inhibits antizyme-dependent ODC degradation and releases ODC monomers from their inactive complex with antizymes, leading to formation of the catalytically active ODC homodimer and restoring polyamine production (PubMed:16916800, PubMed:24967154). Participates in the morphological integrity of the trans-Golgi network (TGN) and functions as a regulator of intracellular secretory vesicle trafficking (By similarity). {ECO:0000250|UniProtKB:Q96A70, ECO:0000269|PubMed:16916800, ECO:0000269|PubMed:18062773, ECO:0000269|PubMed:18508777, ECO:0000269|PubMed:18973822, ECO:0000269|PubMed:24967154}. PTM: Ubiquitinated, leading to its proteosomal degradation; a process that is reduced in presence of antizymes. May also be degraded through the lysosomal degradative pathway in a proteosomal-independent manner. {ECO:0000269|PubMed:18062773}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, perinuclear region {ECO:0000250}. Membrane. Cytoplasmic vesicle {ECO:0000250}. Endoplasmic reticulum-Golgi intermediate compartment. Golgi apparatus, cis-Golgi network. Golgi apparatus, trans-Golgi network {ECO:0000250}. Cytoplasmic granule. Cell projection, axon {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Perikaryon {ECO:0000250}. Note=Detected as vesicle-like pattern in neurite outgrowths. Localizes to the vesicular compartments of the secretory pathway, predominantly in the trans-Golgi network (TGN). Localizes with vesicle-associated membrane protein VAMP8 in the vicinity of the plasma membrane within serotonin-containing secretory granules (By similarity). Colocalizes with KDEL receptors in ER-Golgi intermediate compartment (ERGIC). Translocates from the ERGIC structure to the cytoplasm in a antizyme-dependent manner. Localizes with vesicle-associated membrane protein VAMP8 in the vicinity of the plasma membrane within serotonin-containing secretory granules. {ECO:0000250}. SUBUNIT: Monomer. Interacts with OAZ1, OAZ2 and OAZ3; this interaction disrupts the interaction between the antizyme and ODC1. Does not form a heterodimer with ODC1. {ECO:0000269|PubMed:16916800, ECO:0000269|PubMed:18062773, ECO:0000269|PubMed:18973822, ECO:0000269|PubMed:24967154}. DOMAIN: The N-terminus domain is necessary for its localization to the ER-Golgi intermediate compartment (ERGIC). TISSUE SPECIFICITY: Expressed in the medulla and chromaffin cells of the adrenal gland. Expressed in the Langerhans islets of the pancreas. Expressed in the inner part of the seminiferous tubules and in spermatozoa located in the lumen of the epididymis of the testis. Expressed in the cortex, hippocampus and cerebellum of the brain. Expressed in normal and neoplastic mast cells (MC) (at protein level). Expressed in testis, pancreas and brain. Expressed throughout the differentiation process from spermatids to spermatozoa in the inner part of the seminiferous tubules. Expressed in the kidney: expressed in the superficial (Cs) and the deep layer (Cd) of the cortex region and in the outer stripe (OS), inner stripe (IS) and the inner medulla papilla (IM) of the medulla region. {ECO:0000269|PubMed:16916800, ECO:0000269|PubMed:18508777, ECO:0000269|PubMed:18973822, ECO:0000269|PubMed:22562773, ECO:0000269|PubMed:23874910}. +Q99LI9 CLP1_MOUSE Polyribonucleotide 5'-hydroxyl-kinase Clp1 (EC 2.7.1.78) (Polyadenylation factor Clp1) (Polynucleotide kinase Clp1) (Pre-mRNA cleavage complex II protein Clp1) 425 47,738 Binding site (2); Chain (1); Mutagenesis (1); Nucleotide binding (1); Sequence conflict (3) FUNCTION: Polynucleotide kinase that can phosphorylate the 5'-hydroxyl groups of double-stranded RNA (dsRNA), single-stranded RNA (ssRNA), double-stranded DNA (dsDNA) and double-stranded DNA:RNA hybrids. dsRNA is phosphorylated more efficiently than dsDNA, and the RNA component of a DNA:RNA hybrid is phosphorylated more efficiently than the DNA component. Plays a key role in both tRNA splicing and mRNA 3'-end formation. Component of the tRNA splicing endonuclease complex: phosphorylates the 5'-terminus of the tRNA 3'-exon during tRNA splicing; this phosphorylation event is a prerequisite for the subsequent ligation of the two exon halves and the production of a mature tRNA (PubMed:23474986, PubMed:24766809). Its role in tRNA splicing and maturation is required for cerebellar development (PubMed:24766809). Component of the pre-mRNA cleavage complex II (CF-II), which seems to be required for mRNA 3'-end formation. Also phosphorylates the 5'-terminus of exogenously introduced short interfering RNAs (siRNAs), which is a necessary prerequisite for their incorporation into the RNA-induced silencing complex (RISC). However, endogenous siRNAs and microRNAs (miRNAs) that are produced by the cleavage of dsRNA precursors by DICER1 already contain a 5'-phosphate group, so this protein may be dispensible for normal RNA-mediated gene silencing. {ECO:0000269|PubMed:23474986, ECO:0000269|PubMed:24766809}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03035}. SUBUNIT: Component of the tRNA splicing endonuclease complex, composed of CLP1, TSEN2, TSEN15, TSEN34 and TSEN54. Component of pre-mRNA cleavage complex II (CF-II). Also associates with numerous components of the pre-mRNA cleavage complex I (CF-I/CFIm), including NUDT21, CPSF2, CPSF3, CPSF6 and CPSF7. Interacts with CSTF2 and SYMPK. {ECO:0000255|HAMAP-Rule:MF_03035}. +Q60649 CLPB_MOUSE Caseinolytic peptidase B protein homolog (EC 3.6.1.3) (Suppressor of potassium transport defect 3) 677 76,004 Chain (1); Modified residue (1); Nucleotide binding (1); Repeat (4); Transit peptide (1) FUNCTION: May function as a regulatory ATPase and be related to secretion/protein trafficking process. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9H078}. TISSUE SPECIFICITY: Widely expressed, with highest levels in testis. Also expressed in heart, skeletal muscle and kidney. +Q03265 ATPA_MOUSE ATP synthase subunit alpha, mitochondrial (ATP synthase F1 subunit alpha) 553 59,753 Chain (1); Glycosylation (1); Modified residue (37); Nucleotide binding (2); Sequence conflict (8); Site (1); Transit peptide (1) FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity). Binds the bacterial siderophore enterobactin and can promote mitochondrial accumulation of enterobactin-derived iron ions (By similarity). {ECO:0000250|UniProtKB:P19483, ECO:0000250|UniProtKB:P25705}. PTM: Acetylated on lysine residues. BLOC1S1 is required for acetylation (By similarity). Acetylation of Lys-132, Lys-230 and Lys-498 is observed in liver mitochondria from fasted mice but not from fed mice. {ECO:0000250|UniProtKB:P25705}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P19483}; Peripheral membrane protein {ECO:0000250|UniProtKB:P19483}; Matrix side {ECO:0000250|UniProtKB:P19483}. Cell membrane {ECO:0000250|UniProtKB:P25705}; Peripheral membrane protein {ECO:0000250|UniProtKB:P25705}; Extracellular side {ECO:0000250|UniProtKB:P25705}. Note=Colocalizes with HRG on the cell surface of T-cells. {ECO:0000250|UniProtKB:P25705}. SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c (By similarity). Interacts with ATPAF2. Interacts with HRG; the interaction occurs on the surface of T-cells and alters the cell morphology when associated with concanavalin (in vitro). Interacts with PLG (angiostatin peptide); the interaction inhibits most of the angiogenic properties of angiostatin (By similarity). Component of an ATP synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MD and MP68 (By similarity). Interacts with BLOC1S1 (By similarity). Interacts with BCL2L1 isoform BCL-X(L); the interaction mediates the association of BCL2L1 isoform BCL-X(L) with the mitochondrial membrane F(1)F(0) ATP synthase and enhances neurons metabolic efficency (By similarity). Interacts with CLN5 and PPT1 (PubMed:19941651). {ECO:0000250|UniProtKB:P15999, ECO:0000250|UniProtKB:P19483, ECO:0000250|UniProtKB:P25705, ECO:0000269|PubMed:19941651}. +Q9JHS4 CLPX_MOUSE ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial 634 69,229 Chain (1); Modified residue (2); Mutagenesis (1); Nucleotide binding (1); Sequence conflict (5); Transit peptide (1); Zinc finger (1) FUNCTION: ATP-dependent specificity component of the Clp protease complex. Hydrolyzes ATP. Targets specific substrates for degradation by the Clp complex. Can perform chaperone functions in the absence of CLPP. Enhances the DNA-binding activity of TFAM and is required for maintaining a normal mitochondrial nucleoid structure (PubMed:10347188). ATP-dependent unfoldase that stimulates the incorporation of the pyridoxal phosphate cofactor into 5-aminolevulinate synthase, thereby activating 5-aminolevulinate (ALA) synthesis, the first step in heme biosynthesis. Important for efficient erythropoiesis through upregulation of heme biosynthesis (By similarity). {ECO:0000250|UniProtKB:O76031, ECO:0000269|PubMed:10347188}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:22710082}. Mitochondrion matrix, mitochondrion nucleoid {ECO:0000250}. SUBUNIT: Homohexamer that forms a ring structure; this hexamerization requires ATP binding. Component of the Clp complex formed by the assembly of two CLPP heptameric rings with two CLPX hexameric rings, giving rise to a symmetrical structure with two central CLPP rings flanked by a CLPX ring at either end of the complex (PubMed:22710082). Interacts with TFAM (By similarity). {ECO:0000250|UniProtKB:O76031, ECO:0000269|PubMed:22710082}. TISSUE SPECIFICITY: Detected in liver (at protein level). {ECO:0000269|PubMed:22710082}. +Q8K445 CLRN1_MOUSE Clarin-1 (Usher syndrome type-3 protein homolog) 232 25,804 Alternative sequence (1); Chain (1); Glycosylation (2); Transmembrane (4) TRANSMEM 8 28 Helical. {ECO:0000255}.; TRANSMEM 101 121 Helical. {ECO:0000255}.; TRANSMEM 135 155 Helical. {ECO:0000255}.; TRANSMEM 186 206 Helical. {ECO:0000255}. FUNCTION: May have a role in the excitatory ribbon synapse junctions between hair cells and cochlear ganglion cells and presumably also in analogous synapses within the retina. {ECO:0000269|PubMed:12080385}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P58418}; Multi-pass membrane protein {ECO:0000255}. +Q8BHH8 CLRN3_MOUSE Clarin-3 (Transmembrane protein 12) 226 25,350 Chain (1); Glycosylation (1); Transmembrane (4) TRANSMEM 8 28 Helical. {ECO:0000255}.; TRANSMEM 92 112 Helical. {ECO:0000255}.; TRANSMEM 128 148 Helical. {ECO:0000255}.; TRANSMEM 181 201 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q99JA4 CLTR1_MOUSE Cysteinyl leukotriene receptor 1 (CysLTR1) (Cysteinyl leukotriene D4 receptor) (LTD4 receptor) 352 40,715 Alternative sequence (1); Chain (1); Disulfide bond (1); Glycosylation (4); Sequence conflict (1); Topological domain (8); Transmembrane (7) TRANSMEM 44 64 Helical; Name=1. {ECO:0000255}.; TRANSMEM 73 93 Helical; Name=2. {ECO:0000255}.; TRANSMEM 122 142 Helical; Name=3. {ECO:0000255}.; TRANSMEM 157 177 Helical; Name=4. {ECO:0000255}.; TRANSMEM 209 229 Helical; Name=5. {ECO:0000255}.; TRANSMEM 246 266 Helical; Name=6. {ECO:0000255}.; TRANSMEM 292 312 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 43 Extracellular. {ECO:0000255}.; TOPO_DOM 65 72 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 94 121 Extracellular. {ECO:0000255}.; TOPO_DOM 143 156 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 178 208 Extracellular. {ECO:0000255}.; TOPO_DOM 230 245 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 267 291 Extracellular. {ECO:0000255}.; TOPO_DOM 313 352 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for cysteinyl leukotrienes mediating constriction of the microvascular smooth muscle during an inflammatory response. This response is mediated via a G-protein that activates a phosphatidylinositol-calcium second messenger system. The rank order of affinities for the leukotrienes is LTD4 >> LTE4 = LTC4 >> LTB4. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Widely expressed, with higher expression in the lung and skin, intermediate levels in the heart, kidney and stomach and lower levels in several other tissues. Isoform 1 is the most abundant form in all tested tissues. +Q9CZT6 CMS1_MOUSE Protein CMSS1 (Cms1 ribosomal small subunit homolog) 276 31,594 Chain (1); Modified residue (4); Sequence conflict (1) +Q9DBC3 CMTR1_MOUSE Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1 (EC 2.1.1.57) (Cap methyltransferase 1) (Cap1 2'O-ribose methyltransferase 1) (MTr1) (FtsJ methyltransferase domain-containing protein 2) 837 95,676 Active site (3); Binding site (3); Chain (1); Domain (3); Frameshift (1); Modified residue (5); Motif (1); Region (5); Sequence conflict (8) FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that mediates mRNA cap1 2'-O-ribose methylation to the 5'-cap structure of mRNAs. Methylates the ribose of the first nucleotide of a m(7)GpppG-capped mRNA and small nuclear RNA (snRNA) to produce m(7)GpppRm (cap1). Displays a preference for cap0 transcripts. Cap1 modification is linked to higher levels of translation. May be involved in the interferon response pathway. {ECO:0000250|UniProtKB:Q8N1G2}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8N1G2}. SUBUNIT: Interacts with POLR2A (via C-terminus). {ECO:0000250|UniProtKB:Q8N1G2}. +Q8K2W9 CN093_MOUSE Uncharacterized protein C14orf93 homolog 541 58,780 Chain (1); Compositional bias (1); Cross-link (2); Modified residue (4); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +O35372 CNIH1_MOUSE Protein cornichon homolog 1 (CNIH-1) (Cornichon family AMPA receptor auxiliary protein 1) (Protein cornichon homolog) 144 16,699 Chain (1); Sequence conflict (1); Topological domain (4); Transmembrane (3) TRANSMEM 11 31 Helical. {ECO:0000255}.; TRANSMEM 57 77 Helical. {ECO:0000255}.; TRANSMEM 123 143 Helical. {ECO:0000255}. TOPO_DOM 1 10 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 32 56 Lumenal. {ECO:0000255}.; TOPO_DOM 78 122 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 144 144 Lumenal. {ECO:0000255}. FUNCTION: Involved in the selective transport and maturation of TGF-alpha family proteins. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus membrane. Note=Located primarily in the ER; may cycle between the ER and the Golgi apparatus. {ECO:0000250}. SUBUNIT: Interacts with AREG immature precursor and with immature TGFA, i.e. with a prosegment and lacking full N-glycosylation, but not with the fully N-glycosylated form. In the Golgi apparatus, may form a complex with GORASP55 and transmembrane TGFA (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in oocytes, and at a basal level in ovarian somatic cells of 6-week-old mouse. Expressed in adult brain. +Q9CX13 CNIH4_MOUSE Protein cornichon homolog 4 (CNIH-4) (Cornichon family AMPA receptor auxiliary protein 4) 139 16,089 Chain (1); Transmembrane (3) TRANSMEM 5 25 Helical. {ECO:0000255}.; TRANSMEM 57 77 Helical. {ECO:0000255}.; TRANSMEM 118 138 Helical. {ECO:0000255}. FUNCTION: Involved in G protein-coupled receptors (GPCRs) trafficking from the endoplasmic reticulum to the cell surface; it promotes the exit of GPCRs from the early secretory pathway, likely through interaction with the COPII machinery. {ECO:0000250|UniProtKB:Q9P003}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9P003}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250|UniProtKB:Q9P003}. SUBUNIT: Interacts with Sec23/24 complex components SEC24B and SEC24D (By similarity). Interacts with CCR5 (By similarity). Interacts with ADRB2 in the early secretory pathway (By similarity). {ECO:0000250|UniProtKB:Q9P003}. +Q08093 CNN2_MOUSE Calponin-2 (Calponin H2, smooth muscle) (Neutral calponin) 305 33,156 Chain (1); Domain (1); Initiator methionine (1); Modified residue (4); Repeat (3) FUNCTION: Thin filament-associated protein that is implicated in the regulation and modulation of smooth muscle contraction. It is capable of binding to actin, calmodulin, troponin C and tropomyosin. The interaction of calponin with actin inhibits the actomyosin Mg-ATPase activity. TISSUE SPECIFICITY: Smooth muscle, and tissues containing significant amounts of smooth muscle. +Q9DAW9 CNN3_MOUSE Calponin-3 (Calponin, acidic isoform) 330 36,429 Chain (1); Compositional bias (1); Domain (1); Modified residue (2); Repeat (3) FUNCTION: Thin filament-associated protein that is implicated in the regulation and modulation of smooth muscle contraction. It is capable of binding to actin, calmodulin, troponin C and tropomyosin. The interaction of calponin with actin inhibits the actomyosin Mg-ATPase activity (By similarity). {ECO:0000250}. +Q0GA42 CNNM1_MOUSE Metal transporter CNNM1 (Ancient conserved domain-containing protein 1) (mACDP1) (Cyclin-M1) (Cyclin-like protein 1) (CLP-1) 951 103,980 Chain (1); Domain (3); Erroneous initiation (1); Frameshift (1); Modified residue (3); Sequence conflict (3); Transmembrane (4) TRANSMEM 23 43 Helical. {ECO:0000255}.; TRANSMEM 222 242 Helical. {ECO:0000255}.; TRANSMEM 282 302 Helical. {ECO:0000255}.; TRANSMEM 319 339 Helical. {ECO:0000255}. FUNCTION: Probable metal transporter. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14723793}; Multi-pass membrane protein {ECO:0000269|PubMed:14723793}. TISSUE SPECIFICITY: Predominantly expressed in brain and testis, and, at lower levels, in kidney. In the brain, expressed in hippocampal neurons (at protein level). {ECO:0000269|PubMed:14723793, ECO:0000269|PubMed:22399287}. +Q3TWN3 CNNM2_MOUSE Metal transporter CNNM2 (Ancient conserved domain-containing protein 2) (mACDP2) (Cyclin-M2) 875 96,704 Alternative sequence (1); Beta strand (8); Chain (1); Domain (3); Erroneous initiation (2); Glycosylation (1); Helix (9); Intramembrane (1); Modified residue (1); Mutagenesis (7); Sequence caution (1); Sequence conflict (3); Topological domain (5); Transmembrane (3); Turn (1) INTRAMEM 314 334 Helical. {ECO:0000255}. TRANSMEM 251 271 Helical. {ECO:0000255}.; TRANSMEM 339 359 Helical. {ECO:0000255}.; TRANSMEM 369 389 Helical. {ECO:0000255}. TOPO_DOM 1 250 Extracellular. {ECO:0000255}.; TOPO_DOM 272 313 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 335 338 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 360 368 Extracellular. {ECO:0000255}.; TOPO_DOM 390 875 Cytoplasmic. {ECO:0000255}. FUNCTION: Divalent metal cation transporter. Mediates transport of divalent metal cations in an order of Mg(2+) > Co(2+) > Mn(2+) > Sr(2+) > Ba(2+) > Cu(2+) > Fe(2+). {ECO:0000269|PubMed:15899945}. PTM: The N-terminus is cleaved within the endoplasmic reticulum. The signal peptidase complex seems to be involved in the processing, but the exact cleavage site has not been identified (PubMed:22399287). {ECO:0000269|PubMed:22399287}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22399287}; Multi-pass membrane protein {ECO:0000269|PubMed:22399287}. SUBUNIT: Isoform 1 and isoform 2 may interact with each other. TISSUE SPECIFICITY: Widely expressed, with highest levels in kidney, lung, spleen and testis. In the kidney, predominantly expressed in the distal convoluted tubule and, at lower levels, in the connecting tubule (at protein level). {ECO:0000269|PubMed:14723793, ECO:0000269|PubMed:15899945, ECO:0000269|PubMed:22399287}. +Q32NY4 CNNM3_MOUSE Metal transporter CNNM3 (Ancient conserved domain-containing protein 3) (mACDP3) (Cyclin-M3) 713 76,279 Alternative sequence (1); Beta strand (6); Chain (1); Domain (3); Erroneous initiation (2); Glycosylation (1); Helix (7); Modified residue (2); Sequence conflict (1); Transmembrane (5); Turn (1) TRANSMEM 7 29 Helical. {ECO:0000255}.; TRANSMEM 137 157 Helical. {ECO:0000255}.; TRANSMEM 199 219 Helical. {ECO:0000255}.; TRANSMEM 227 247 Helical. {ECO:0000255}.; TRANSMEM 267 287 Helical. {ECO:0000255}. FUNCTION: Probable metal transporter. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed with highest levels in brain, kidney, liver, lung and heart. {ECO:0000269|PubMed:22399287}. +Q69ZF7 CNNM4_MOUSE Metal transporter CNNM4 (Ancient conserved domain-containing protein 4) (mACDP4) (Cyclin-M4) 771 86,626 Chain (1); Domain (3); Erroneous initiation (2); Glycosylation (1); Intramembrane (1); Modified residue (3); Topological domain (5); Transmembrane (3) INTRAMEM 238 258 Helical. {ECO:0000255}. TRANSMEM 176 196 Helical. {ECO:0000255}.; TRANSMEM 262 282 Helical. {ECO:0000255}.; TRANSMEM 291 313 Helical. {ECO:0000255}. TOPO_DOM 1 175 Extracellular. {ECO:0000255}.; TOPO_DOM 197 237 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 259 261 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 283 290 Extracellular. {ECO:0000255}.; TOPO_DOM 314 771 Cytoplasmic. {ECO:0000255}. FUNCTION: Probable metal transporter. The interaction with the metal ion chaperone COX11 suggests that it may play a role in sensory neuron functions (By similarity). May play a role in biomineralization and retinal function. {ECO:0000250, ECO:0000269|PubMed:19200525, ECO:0000269|PubMed:19200527}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with COX11. {ECO:0000250}. TISSUE SPECIFICITY: Cornea, retina, teeth (at protein level). In the retina it is predominantly localized to the outer plexiform layer, inner plexiform layer and ganglion cell layer. In the tooth strongest expression is observed in the cell body of the ameloblasts. Expressed at high levels in the gastrointestinal tract and testis. {ECO:0000269|PubMed:14723793, ECO:0000269|PubMed:19200525, ECO:0000269|PubMed:19200527, ECO:0000269|PubMed:22399287}. +Q6ZQ08 CNOT1_MOUSE CCR4-NOT transcription complex subunit 1 (CCR4-associated factor 1) 2375 266,808 Alternative sequence (3); Chain (1); Compositional bias (1); Erroneous initiation (3); Modified residue (2); Motif (7); Region (2); Sequence conflict (3) FUNCTION: Scaffolding component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. Additional complex functions may be a consequence of its influence on mRNA expression. Its scaffolding function implies its interaction with the catalytic complex module and diverse RNA-binding proteins mediating the complex recruitment to selected mRNA 3'UTRs. Involved in degradation of AU-rich element (ARE)-containing mRNAs probably via association with ZFP36. Mediates the recruitment of the CCR4-NOT complex to miRNA targets and to the RISC complex via association with TNRC6A, TNRC6B or TNRC6C. Acts as a transcriptional repressor. Represses the ligand-dependent transcriptional activation by nuclear receptors. Involved in the maintenance of emryonic stem (ES) cell identity; prevents their differentiation towards extraembryonic trophectoderm lineages. {ECO:0000269|PubMed:22367759}. SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:20133598}. Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=NANOS2 promotes its localization to P-body. SUBUNIT: Component of the CCR4-NOT complex; distinct complexes seem to exist that differ in the participation of probably mutually exclusive catalytic subunits (By similarity). In the complex, interacts directly with CNOT6, CNOT6L, CNOT7 or CNOT8. Interacts in a ligand-dependent fashion with ESR1 and RXRA. Interacts with NANOS2, TOB1 and ZFP36. Interacts with TNRC6A, TNRC6B and TNRC6C; the interactions are direct. {ECO:0000250, ECO:0000269|PubMed:20133598}. DOMAIN: Contains Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs, a motif known to be important for the association with nuclear receptors. {ECO:0000250}. +Q8K0V4 CNOT3_MOUSE CCR4-NOT transcription complex subunit 3 (CCR4-associated factor 3) 751 81,946 Chain (1); Compositional bias (2); Modified residue (3); Region (1) FUNCTION: Component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. Additional complex functions may be a consequence of its influence on mRNA expression. May be involved in metabolic regulation; may be involved in recruitment of the CCR4-NOT complex to deadenylation target mRNAs involved in energy metabolism. Involved in mitotic progression and regulation of the spindle assembly checkpoint by regulating the stability of MAD1L1 mRNA. Can repress transcription and may link the CCR4-NOT complex to transcriptional regulation; the repressive function may involve histone deacetylases. Involved in the maintenance of emryonic stem (ES) cell identity; prevents their differentiation towards extraembryonic trophectoderm lineages. {ECO:0000269|PubMed:21897366, ECO:0000269|PubMed:22367759}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:20133598}. Cytoplasm, P-body {ECO:0000269|PubMed:20133598}. Note=NANOS2 promotes its localization to P-body. SUBUNIT: Component of the CCR4-NOT complex; distinct complexes seem to exist that differ in the participation of probably mutually exclusive catalytic subunits. In the complex interacts directly with CNOT2. Interacts with TIP120B and NANOS2. {ECO:0000269|PubMed:20133598}. +Q8BT14 CNOT4_MOUSE CCR4-NOT transcription complex subunit 4 (EC 2.3.2.27) (CCR4-associated factor 4) (E3 ubiquitin-protein ligase CNOT4) (Potential transcriptional repressor NOT4Hp) (RING-type E3 ubiquitin transferase CNOT4) 575 63,474 Alternative sequence (2); Beta strand (6); Chain (1); Coiled coil (1); Domain (1); Helix (2); Modified residue (10); Sequence conflict (4); Turn (2); Zinc finger (2) Protein modification; protein ubiquitination. FUNCTION: Has E3 ubiquitin ligase activity, promoting ubiquitination and degradation of target proteins. Involved in activation of the JAK/STAT pathway. Catalyzes ubiquitination of methylated RBM15. {ECO:0000250|UniProtKB:O95628}. PTM: Autoubiquitinated. {ECO:0000250|UniProtKB:O95628}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}. SUBUNIT: Interacts with CNOT1 via its C-terminus but does not stably associate with the CCR4-NOT complex. Binds E2 ubiquitin ligases via its RING domain. Interacts (via RING domain) with UBE2D2. {ECO:0000250|UniProtKB:O95628}. +Q8K3P5 CNOT6_MOUSE CCR4-NOT transcription complex subunit 6 (EC 3.1.13.4) (CCR4 carbon catabolite repression 4-like) (Carbon catabolite repressor protein 4 homolog) (Cytoplasmic deadenylase) 557 63,304 Active site (3); Alternative sequence (2); Chain (1); Erroneous initiation (1); Metal binding (5); Region (1); Repeat (4); Sequence conflict (1) FUNCTION: Poly(A) nuclease with 3'-5' RNase activity. Catalytic component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. Additional complex functions may be a consequence of its influence on mRNA expression. Involved in mRNA decay mediated by the major-protein-coding determinant of instability (mCRD) of the FOS gene in the cytoplasm. In the presence of ZNF335, enhances ligand-dependent transcriptional activity of nuclear hormone receptors. Mediates cell proliferation and cell survival and prevents cellular senescence (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}. SUBUNIT: Component of the CCR4-NOT complex; distinct complexes seem to exist that differ in the participation of probably mutually exclusive catalytic subunits; the complex contains two deadenylase subunits, CNOT6 or CNOT6L, and CNOT7 or CNOT8. Interacts with CNOT7 and CNOT8 (By similarity). Interacts with UNR (PubMed:15314026). Interacts with ZFP36L1 (via N-terminus). Interacts with ZNF335 (By similarity). {ECO:0000250|UniProtKB:Q9ULM6, ECO:0000269|PubMed:15314026}. +Q9QXT0 CNPY2_MOUSE Protein canopy homolog 2 (MIR-interacting saposin-like protein) (Putative secreted protein ZSIG9) (Transmembrane protein 4) 182 20,767 Chain (1); Disulfide bond (3); Domain (1); Modified residue (1); Motif (1); Signal peptide (1) FUNCTION: Positive regulator of neurite outgrowth by stabilizing myosin regulatory light chain (MRLC). It prevents MIR-mediated MRLC ubiquitination and its subsequent proteasomal degradation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000255|PROSITE-ProRule:PRU10138}. SUBUNIT: Interacts with MYLIP/MIR. {ECO:0000250}. +P47746 CNR1_MOUSE Cannabinoid receptor 1 (CB-R) (CB1) (Brain-type cannabinoid receptor) 473 52,831 Chain (1); Glycosylation (2); Lipidation (1); Modified residue (2); Mutagenesis (1); Region (1); Sequence conflict (3); Topological domain (8); Transmembrane (7) TRANSMEM 122 142 Helical. {ECO:0000250|UniProtKB:P21554}.; TRANSMEM 156 176 Helical. {ECO:0000250|UniProtKB:P21554}.; TRANSMEM 189 209 Helical. {ECO:0000250|UniProtKB:P21554}.; TRANSMEM 234 254 Helical. {ECO:0000250|UniProtKB:P21554}.; TRANSMEM 279 299 Helical. {ECO:0000250|UniProtKB:P21554}.; TRANSMEM 346 366 Helical. {ECO:0000250|UniProtKB:P21554}.; TRANSMEM 379 399 Helical. {ECO:0000250|UniProtKB:P21554}. TOPO_DOM 1 121 Extracellular. {ECO:0000250|UniProtKB:P21554}.; TOPO_DOM 143 155 Cytoplasmic. {ECO:0000250|UniProtKB:P21554}.; TOPO_DOM 177 188 Extracellular. {ECO:0000250|UniProtKB:P21554}.; TOPO_DOM 210 233 Cytoplasmic. {ECO:0000250|UniProtKB:P21554}.; TOPO_DOM 255 278 Extracellular. {ECO:0000250|UniProtKB:P21554}.; TOPO_DOM 300 345 Cytoplasmic. {ECO:0000250|UniProtKB:P21554}.; TOPO_DOM 367 378 Extracellular. {ECO:0000250|UniProtKB:P21554}.; TOPO_DOM 400 473 Cytoplasmic. {ECO:0000250|UniProtKB:P21554}. FUNCTION: G-protein coupled receptor for cannabinoids, including endocannabinoids (eCBs), such as N-arachidonoylethanolamide (also called anandamide or AEA) and 2-arachidonoylglycerol (2-AG) (PubMed:9888857, PubMed:22388959). Mediates many cannabinoid-induced effects, acting, among others, on food intake, memory loss, gastrointestinal motility, catalepsy, ambulatory activity, anxiety, chronic pain (PubMed:9888857, PubMed:27828947). Signaling typically involves reduction in cyclic AMP (PubMed:8832654, PubMed:27828947). Signaling typically involves reduction in cyclic AMP (By similarity). In the hypothalamus, may have a dual effect on mitochondrial respiration depending upon the agonist dose and possibly upon the cell type. Increases respiration at low doses, while decreases respiration at high doses (PubMed:25707796, PubMed:27828947). At high doses, CNR1 signal transduction involves G-protein alpha-i protein activation and subsequent inhibition of mitochondrial soluble adenylate cyclase, decrease in cyclic AMP concentration, inhibition of protein kinase A (PKA)-dependent phosphorylation of specific subunits of the mitochondrial electron transport system, including NDUFS2 (PubMed:27828947). In the hypothalamus, inhibits leptin-induced reactive oxygen species (ROS) formation and mediates cannabinoid-induced increase in SREBF1 and FASN gene expression (PubMed:25869131). In response to cannabinoids, drives the release of orexigenic beta-endorphin, but not that of melanocyte-stimulating hormone alpha/alpha-MSH, from hypothalamic POMC neurons, hence promoting food intake (PubMed:25707796). In the hippocampus, regulates cellular respiration and energy production in response to cannabinoids. Involved in cannabinoid-dependent depolarization-induced suppression of inhibition (DSI), a process in which depolarization of CA1 postsynaptic pyramidal neurons mobilizes eCBs, which retrogradely activate presynaptic CB1 receptors, transiently decreasing GABAergic inhibitory neurotransmission (PubMed:22388959). Also reduces excitatory synaptic transmission (PubMed:27828947). In superior cervical ganglions and cerebral vascular smooth muscle cells, inhibits voltage-gated Ca(2+) channels in a constitutive, as well as agonist-dependent manner (By similarity). In cerebral vascular smooth muscle cells, cannabinoid-induced inhibition of voltage-gated Ca(2+) channels leads to vasodilation and decreased vascular tone (By similarity). Induces leptin production in adipocytes and reduces LRP2-mediated leptin clearance in the kidney, hence participating in hyperleptinemia (PubMed:22841573). In adipose tissue, CNR1 signaling leads to increased expression of SREBF1, ACACA and FASN genes (PubMed:15864349). In the liver, activation by endocannabinoids leads to increased de novo lipogenesis and reduced fatty acid catabolism, associated with increased expression of SREBF1/SREBP-1, GCK, ACACA, ACACB and FASN genes (PubMed:15864349, PubMed:21987372). May also affect de novo cholesterol synthesis and HDL-cholesteryl ether uptake (PubMed:21987372). Peripherally modulates energy metabolism. In high carbohydrate diet-induced obesity, may decrease the expression of mitochondrial dihydrolipoyl dehydrogenase/DLD in striated muscles, as well as that of selected glucose/ pyruvate metabolic enzymes, hence affecting energy expenditure through mitochondrial metabolism (PubMed:26671069). In response to cannabinoid anandamide, elicits a proinflammatory response in macrophages, which involves NLRP3 inflammasome activation and IL1B and IL18 secretion. In macrophages infiltrating pancreatic islets, this process may participate in the progression of type-2 diabetes and associated loss of pancreatic beta-cells (PubMed:23955712). {ECO:0000250|UniProtKB:O02777, ECO:0000250|UniProtKB:P21554, ECO:0000269|PubMed:15864349, ECO:0000269|PubMed:21987372, ECO:0000269|PubMed:22388959, ECO:0000269|PubMed:22841573, ECO:0000269|PubMed:23955712, ECO:0000269|PubMed:25707796, ECO:0000269|PubMed:25869131, ECO:0000269|PubMed:26671069, ECO:0000269|PubMed:27828947, ECO:0000269|PubMed:8832654, ECO:0000269|PubMed:9888857}. PTM: Palmitoylation at Cys-416 is important for recruitment at both plasma membrane and lipid rafts and association with G protein alpha subunits. {ECO:0000250|UniProtKB:P20272}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15864349, ECO:0000269|PubMed:25707796, ECO:0000269|PubMed:27828947}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P21554}. Mitochondrion outer membrane {ECO:0000269|PubMed:22388959, ECO:0000269|PubMed:25707796, ECO:0000269|PubMed:26671069, ECO:0000269|PubMed:27826249, ECO:0000269|PubMed:27828947}. Cell projection, axon {ECO:0000250|UniProtKB:P20272}. Note=In CA1 hippocampal neurons, 15.5% of total protein is localized in mitochondria (PubMed:22388959). Found on presynaptic axon terminals in some GABAergic neurons in the somatosensory cortex (By similarity). In striated muscles, predominantly located in mitochondria (PubMed:27826249). Unexpectedly, in the mitochondria, the C-terminus is located in the mitochondrial intermembrane space, a compartment topologically considered as extracellular. In canonical seven-transmembrane G-protein coupled receptors, the C-terminus is cytosolic (PubMed:22388959). {ECO:0000250|UniProtKB:P20272, ECO:0000269|PubMed:22388959, ECO:0000269|PubMed:27826249}. SUBUNIT: Interacts (via C-terminus) with CNRIP1 (By similarity). Associates with G protein alpha subunits, including G(i) alpha-1/GNAI1, G(i) alpha-3/GNAI3 and G(o) alpha/GNAO1; palmitoylation is important for interaction with GNAI3 and GNAO1 (PubMed:27828947). {ECO:0000250|UniProtKB:P21554, ECO:0000269|PubMed:27828947}. TISSUE SPECIFICITY: Expressed in brain neurons (at protein level) (PubMed:22388959). Detected throughout the striatum, cortex and hippocampus, with highest levels in the lateral striatum (PubMed:15606779, PubMed:10891614, PubMed:22388959). In rostral brain regions, high expression levels in the dorsal lateral striatum, while in the caudal brain regions, high levels are observed in the ventral lateral striatum (PubMed:10891614). Expressed in neurons (PubMed:10891614). In the hypothalamus, expressed in both GABAergic and glutamatergic presynaptic terminals of POMC neurons (at protein level) (PubMed:25869131, PubMed:25707796). Expressed in striated muscles, including skeletal muscles (gastrocnemius and rectus abdominis) and myocardium (at protein level) (PubMed:26671069, PubMed:27826249). Expressed in the liver, with highest levels in Kupffer cells and lower levels in endothelial cells as well as hepatocytes, particularly in perivascular areas (at protein level) (PubMed:15864349, PubMed:21987372). The hepatic expression level is up-regulated in obese mice compared to lean animals (PubMed:21987372). {ECO:0000269|PubMed:10891614, ECO:0000269|PubMed:15606779, ECO:0000269|PubMed:15864349, ECO:0000269|PubMed:21987372, ECO:0000269|PubMed:22388959, ECO:0000269|PubMed:25707796, ECO:0000269|PubMed:25869131, ECO:0000269|PubMed:26671069, ECO:0000269|PubMed:27826249}. DISEASE: Note=May contribute to the development of diet-induced obesity and several obesity-associated features, such as dyslipidemia and liver steatosis, regulating peripheral lipogenesis, energy expenditure and feeding behavior. In the liver, mediates cannabinoid-induced de novo lipogenesis and reduces fatty acid catabolism (PubMed:15864349, PubMed:21987372). In muscles, affects energy expenditure through mitochondrial metabolism (PubMed:22841573, PubMed:26671069). Induces leptin production by adipocytes and reduces LRP2-mediated leptin clearance in the kidney. The resulting hyperleptinemia causes resistance to the anorexic and weight-reducing effects of leptin (PubMed:22841573). In response to cannabinoids, drives the release of orexigenic beta-endorphin from hypothalamic POMC neurons, hence promoting food intake (PubMed:25707796). The use of peripherally-restricted inverse agonists in diet-induced obese mice reduces appetite, body weight, hepatic steatosis, and insulin resistance (PubMed:22841573). {ECO:0000269|PubMed:15864349, ECO:0000269|PubMed:21987372, ECO:0000269|PubMed:22841573, ECO:0000269|PubMed:25707796, ECO:0000269|PubMed:26671069}. +P47936 CNR2_MOUSE Cannabinoid receptor 2 (CB-2) (CB2) (mCB2) 347 38,213 Chain (1); Glycosylation (1); Modified residue (3); Sequence conflict (4); Topological domain (8); Transmembrane (7) TRANSMEM 34 59 Helical; Name=1. {ECO:0000255}.; TRANSMEM 72 92 Helical; Name=2. {ECO:0000255}.; TRANSMEM 105 129 Helical; Name=3. {ECO:0000255}.; TRANSMEM 150 172 Helical; Name=4. {ECO:0000255}.; TRANSMEM 189 214 Helical; Name=5. {ECO:0000255}.; TRANSMEM 247 267 Helical; Name=6. {ECO:0000255}.; TRANSMEM 280 301 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 33 Extracellular. {ECO:0000255}.; TOPO_DOM 60 71 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 93 104 Extracellular. {ECO:0000255}.; TOPO_DOM 130 149 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 173 188 Extracellular. {ECO:0000255}.; TOPO_DOM 215 246 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 268 279 Extracellular. {ECO:0000255}.; TOPO_DOM 302 347 Cytoplasmic. {ECO:0000255}. FUNCTION: Heterotrimeric G protein-coupled receptor for endocannabinoid 2-arachidonoylglycerol mediating inhibition of adenylate cyclase. May function in inflammatory response, nociceptive transmission and bone homeostasis. {ECO:0000269|PubMed:10822068, ECO:0000269|PubMed:11929767, ECO:0000269|PubMed:16407142, ECO:0000269|PubMed:16563625, ECO:0000269|PubMed:16924491, ECO:0000269|PubMed:17401376, ECO:0000269|PubMed:18286196, ECO:0000269|PubMed:8679694}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Perikaryon {ECO:0000250}. Note=Localizes to apical dendrite of pyramidal neurons. {ECO:0000250}. TISSUE SPECIFICITY: Expressed by cells of hematopoietic origin. Expressed in skin in suprabasal layers and hair follicles, in brain by neurons and glial cells and by osteoblasts, osteocytes, osteoclasts (at protein level). {ECO:0000269|PubMed:11929767, ECO:0000269|PubMed:12511587, ECO:0000269|PubMed:16407142, ECO:0000269|PubMed:16924491, ECO:0000269|PubMed:18286196}. +A2AM05 CNTLN_MOUSE Centlein (Centrosomal protein) 1397 160,747 Alternative sequence (4); Chain (1); Coiled coil (5); Erroneous initiation (1); Initiator methionine (1); Modified residue (6); Sequence caution (1); Sequence conflict (4) FUNCTION: Required for centrosome cohesion and recruitment of CEP68 to centrosomes. {ECO:0000250|UniProtKB:Q9NXG0}. PTM: Phosphorylated directly or indirectly by NEK2. {ECO:0000250|UniProtKB:Q9NXG0}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:A9ZSY0}. Note=Colocalizes with gamma-tubulin during interphase and mitosis. Appears to associate with the mother centriole during G1 phase and with daughter centrioles towards G1/S phase. Localizes to the proximal ends of the centrioles. Levels are high at interphase centrosomes but are reduced on mitotic spindle poles. {ECO:0000250|UniProtKB:A9ZSY0, ECO:0000250|UniProtKB:Q9NXG0}. SUBUNIT: Interacts with CEP250 and CEP68. Interacts with NEK2; the interaction leads to phosphorylation of CNTLN. {ECO:0000250|UniProtKB:Q9NXG0}. +P12960 CNTN1_MOUSE Contactin-1 (Neural cell surface protein F3) 1020 113,388 Chain (1); Compositional bias (1); Disulfide bond (6); Domain (10); Glycosylation (9); Lipidation (1); Propeptide (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Contactins mediate cell surface interactions during nervous system development. Involved in the formation of paranodal axo-glial junctions in myelinated peripheral nerves and in the signaling between axons and myelinating glial cells via its association with CNTNAP1. Participates in oligodendrocytes generation by acting as a ligand of NOTCH1. Its association with NOTCH1 promotes NOTCH1 activation through the released notch intracellular domain (NICD) and subsequent translocation to the nucleus. Interaction with TNR induces a repulsion of neurons and an inhibition of neurite outgrowth. {ECO:0000269|PubMed:11395001, ECO:0000269|PubMed:14567914, ECO:0000269|PubMed:7678967}. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. SUBUNIT: Monomer. Interacts with CNTNAP1 in cis form (By similarity). Binds to the carbonic-anhydrase like domain of PTPRZ1 (PubMed:20133774). Interacts with NOTCH1 and TNR (PubMed:7678967, PubMed:14567914). Detected in a complex with NRCAM and PTPRB (PubMed:11564762). {ECO:0000250, ECO:0000269|PubMed:14567914, ECO:0000269|PubMed:20133774, ECO:0000269|PubMed:7678967}. +Q07409 CNTN3_MOUSE Contactin-3 (Brain-derived immunoglobulin superfamily protein 1) (BIG-1) (Plasmacytoma-associated neuronal glycoprotein) 1028 113,232 Beta strand (59); Chain (1); Disulfide bond (6); Domain (10); Glycosylation (11); Helix (8); Lipidation (1); Propeptide (1); Sequence conflict (2); Signal peptide (1); Turn (1) FUNCTION: Contactins mediate cell surface interactions during nervous system development. Has some neurite outgrowth-promoting activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. SUBUNIT: Interacts with PTPRG. {ECO:0000269|PubMed:20133774}. TISSUE SPECIFICITY: Specifically expressed in brain. Ectopically expressed in tumors expressing endogenous intracisternal A-type particles (IAPs). {ECO:0000269|PubMed:8108413}. +P68500 CNTN5_MOUSE Contactin-5 (Neural recognition molecule NB-2) 1098 120,746 Beta strand (35); Chain (1); Disulfide bond (6); Domain (10); Glycosylation (9); Helix (5); Lipidation (1); Propeptide (1); Signal peptide (1); Turn (3) FUNCTION: Contactins mediate cell surface interactions during nervous system development. Has some neurite outgrowth-promoting activity in the cerebral cortical neurons but not in hippocampal neurons (By similarity). Involved in neuronal activity in the auditory system. {ECO:0000250, ECO:0000269|PubMed:12653969}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. SUBUNIT: Interacts with PTPRG. {ECO:0000269|PubMed:20133774}. TISSUE SPECIFICITY: Expressed in the nervous system. Preferentially expressed in the central auditory pathways. {ECO:0000269|PubMed:12653969}. +Q9JMB8 CNTN6_MOUSE Contactin-6 (Neural recognition molecule NB-3) (mNB-3) 1028 113,761 Alternative sequence (1); Beta strand (42); Chain (1); Disulfide bond (6); Domain (10); Glycosylation (13); Helix (3); Lipidation (1); Modified residue (1); Propeptide (1); Sequence conflict (3); Signal peptide (1); Turn (3) FUNCTION: Contactins mediate cell surface interactions during nervous system development. Participates in oligodendrocytes generation by acting as a ligand of NOTCH1. Its association with NOTCH1 promotes NOTCH1 activation through the released notch intracellular domain (NICD) and subsequent translocation to the nucleus (By similarity). Involved in motor coordination. {ECO:0000250, ECO:0000269|PubMed:12884264}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. SUBUNIT: Interacts with PTPRG. {ECO:0000269|PubMed:20133774}. TISSUE SPECIFICITY: Expressed in brain. In brain, it is preferentially expressed in the accessory olfactory bulb, layers II/III and V of the cerebral cortex, piriform cortex, anterior thalamic nuclei, locus coeruleus of the pons and mesencephalic trigeminal nucleus and in Purkinje cells of the cerebellum. {ECO:0000269|PubMed:10717476}. +Q99P47 CNTP4_MOUSE Contactin-associated protein-like 4 (Cell recognition molecule Caspr4) 1310 144,730 Chain (1); Disulfide bond (11); Domain (8); Glycosylation (13); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1244 1264 Helical. {ECO:0000255}. TOPO_DOM 28 1243 Extracellular. {ECO:0000255}.; TOPO_DOM 1265 1310 Cytoplasmic. {ECO:0000255}. FUNCTION: Presynaptic protein involved in both dopaminergic synaptic transmission and GABAergic system, thereby participating in the structural maturation of inhibitory interneuron synapses. Involved in the dopaminergic synaptic transmission by attenuating dopamine release through a presynaptic mechanism. Also participates in the GABAergic system. {ECO:0000269|PubMed:24870235}. SUBCELLULAR LOCATION: Cell junction, synapse, presynaptic cell membrane {ECO:0000269|PubMed:24870235}; Single-pass type I membrane protein {ECO:0000269|PubMed:24870235}. Note=Specifically present within the presynaptic compartment of synapses. SUBUNIT: Interacts with TIAM1. {ECO:0000250}. TISSUE SPECIFICITY: Specifically present in developing cortical interneurons: highly expressed in cortical parvalbumin (PV) cells and midbrain dopaminergic neurons and is localized presynaptically (at protein level). Also present in the substantia nigra pars compacta (SnC) and ventral tegmental area (VTA) midbrain dopaminergic projection populations. {ECO:0000269|PubMed:24870235}. +A2AL36 CNTRL_MOUSE Centriolin (Centrosomal protein 1) (Centrosomal protein of 110 kDa) (Cep110) 2334 268,880 Alternative sequence (2); Chain (1); Coiled coil (4); Compositional bias (2); Domain (1); Erroneous gene model prediction (2); Modified residue (2); Region (2); Repeat (4); Sequence conflict (3) FUNCTION: Involved in cell cycle progression and cytokinesis. During the late steps of cytokinesis, anchors exocyst and SNARE complexes at the midbody, thereby allowing secretory vesicle-mediated abscission (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q7Z7A1}. Midbody, Midbody ring {ECO:0000250|UniProtKB:Q7Z7A1}. SUBUNIT: Interacts with HOOK2. Interacts with EXOC6 and SNAPIN. Associates with the exocyst complex (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in liver. {ECO:0000269|PubMed:10688839}. +P11087 CO1A1_MOUSE Collagen alpha-1(I) chain (Alpha-1 type I collagen) 1453 138,032 Alternative sequence (1); Chain (1); Disulfide bond (5); Domain (2); Erroneous gene model prediction (1); Glycosylation (4); Metal binding (5); Modified residue (123); Motif (2); Propeptide (2); Region (3); Sequence conflict (10); Signal peptide (1) FUNCTION: Type I collagen is a member of group I collagen (fibrillar forming collagen). PTM: Contains mostly 4-hydroxyproline. Proline residues at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. {ECO:0000269|PubMed:25645914}.; PTM: Contains 3-hydroxyproline at a few sites. This modification occurs on the first proline residue in the sequence motif Gly-Pro-Hyp, where Hyp is 4-hydroxyproline. {ECO:0000269|PubMed:25645914}.; PTM: Lysine residues at the third position of the tripeptide repeating unit (G-X-Y) are 5-hydroxylated in some or all of the chains. {ECO:0000269|PubMed:27119146, ECO:0000305|PubMed:25645914}.; PTM: O-glycosylated on hydroxylated lysine residues. The O-linked glycan consists of a Glc-Gal disaccharide. {ECO:0000269|PubMed:25645914, ECO:0000269|PubMed:27119146}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}. SUBUNIT: Trimers of one alpha 2(I) and two alpha 1(I) chains. Interacts with MRC2. Interacts with TRAM2. Interacts with MFAP4 in a Ca (2+)-dependent manner. {ECO:0000250|UniProtKB:P02452, ECO:0000250|UniProtKB:P02453, ECO:0000250|UniProtKB:P02454}. DOMAIN: The C-terminal propeptide, also known as COLFI domain, have crucial roles in tissue growth and repair by controlling both the intracellular assembly of procollagen molecules and the extracellular assembly of collagen fibrils. It binds a calcium ion which is essential for its function (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Forms the fibrils of tendon, ligaments and bones. In bones the fibrils are mineralized with calcium hydroxyapatite. +P21180 CO2_MOUSE Complement C2 (EC 3.4.21.43) (C3/C5 convertase) [Cleaved into: Complement C2b fragment; Complement C2a fragment] 760 84,741 Active site (3); Alternative sequence (1); Chain (3); Disulfide bond (8); Domain (5); Glycosylation (8); Metal binding (3); Motif (1); Sequence conflict (12); Signal peptide (1) FUNCTION: Component C2 which is part of the classical pathway of the complement system is cleaved by activated factor C1 into two fragments: C2b and C2a. C2a, a serine protease, then combines with complement factor C4b to generate the C3 or C5 convertase. SUBCELLULAR LOCATION: Secreted. DOMAIN: The MIDAS-like motif in the VWFA domain binds divalent metal cations. {ECO:0000250}. +P08122 CO4A2_MOUSE Collagen alpha-2(IV) chain [Cleaved into: Canstatin] 1707 167,325 Chain (2); Disulfide bond (6); Domain (1); Glycosylation (2); Propeptide (1); Region (1); Sequence caution (2); Sequence conflict (14); Signal peptide (1) FUNCTION: Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen. {ECO:0000269|PubMed:3597383}.; FUNCTION: Canstatin, a cleavage product corresponding to the collagen alpha 2(IV) NC1 domain, possesses both anti-angiogenic and anti-tumor cell activity. It inhibits proliferation and migration of endothelial cells, reduces mitochondrial membrane potential, and induces apoptosis. Specifically induces Fas-dependent apoptosis and activates procaspase-8 and -9 activity. Ligand for alphavbeta3 and alphavbeta5 integrins (By similarity). {ECO:0000250}. PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.; PTM: Type IV collagens contain numerous cysteine residues which are involved in inter- and intramolecular disulfide bonding. 12 of these, located in the NC1 domain, are conserved in all known type IV collagens.; PTM: Proteolytic processing produces the C-terminal NC1 peptide, canstatin. {ECO:0000250}.; PTM: The trimeric structure of the NC1 domains is stabilized by covalent bonds between Lys and Met residues. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000255|PROSITE-ProRule:PRU00736}. SUBUNIT: There are six type IV collagen isoforms, alpha 1(IV)-alpha 6(IV), each of which can form a triple helix structure with 2 other chains to generate type IV collagen network. DOMAIN: Alpha chains of type IV collagen have a non-collagenous domain (NC1) at their C-terminus, frequent interruptions of the G-X-Y repeats in the long central triple-helical domain (which may cause flexibility in the triple helix), and a short N-terminal triple-helical 7S domain. +Q9QZS0 CO4A3_MOUSE Collagen alpha-3(IV) chain [Cleaved into: Tumstatin] 1669 161,726 Chain (2); Cross-link (2); Disulfide bond (6); Domain (1); Glycosylation (2); Motif (4); Region (5); Sequence conflict (2); Signal peptide (1); Site (1) FUNCTION: Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen. {ECO:0000250|UniProtKB:Q01955, ECO:0000269|PubMed:7962065}.; FUNCTION: Tumstatin, a cleavage fragment corresponding to the collagen alpha 3(IV) NC1 domain, possesses both anti-angiogenic and anti-tumor cell activity; these two anti-tumor properties may be regulated via RGD-independent ITGB3-mediated mechanisms. {ECO:0000250|UniProtKB:Q01955, ECO:0000269|PubMed:12842087, ECO:0000269|PubMed:7962065}. PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. {ECO:0000250|UniProtKB:Q01955, ECO:0000255|PROSITE-ProRule:PRU00736}.; PTM: Type IV collagens contain numerous cysteine residues which are involved in inter- and intramolecular disulfide bonding. 12 of these, located in the NC1 domain, are conserved in all known type IV collagens. {ECO:0000250|UniProtKB:Q01955, ECO:0000255|PROSITE-ProRule:PRU00736}.; PTM: The trimeric structure of the NC1 domains is stabilized by covalent bonds between Lys and Met residues. {ECO:0000250}.; PTM: Phosphorylated by the Goodpasture antigen-binding protein/COL4A3BP. {ECO:0000250|UniProtKB:Q01955}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000255|PROSITE-ProRule:PRU00736, ECO:0000269|PubMed:7962065}. Note=Colocalizes with COL4A4 and COL4A5 in GBM, tubular basement membrane (TBM) and synaptic basal lamina (BL). {ECO:0000250|UniProtKB:Q01955, ECO:0000269|PubMed:7962065}. SUBUNIT: There are six type IV collagen isoforms, alpha 1(IV)-alpha 6(IV), each of which can form a triple helix structure with 2 other chains to generate type IV collagen network. The alpha 3(IV) chain forms a triple helical protomer with alpha 4(IV) and alpha 5(IV); this triple helical structure dimerizes through NC1-NC1 domain interactions such that the alpha 3(IV), alpha 4(IV) and alpha 5(IV) chains of one protomer connect with the alpha 5(IV), alpha 4(IV) and alpha 3(IV) chains of the opposite promoter, respectively. Interacts with COL4A3BP and ITGB3 (By similarity). Associates with LAMB2 at the neuromuscular junction and in GBM. {ECO:0000250|UniProtKB:Q01955, ECO:0000269|PubMed:14633121, ECO:0000269|PubMed:7962065}. DOMAIN: Alpha chains of type IV collagen have a non-collagenous domain (NC1) at their C-terminus, frequent interruptions of the G-X-Y repeats in the long central triple-helical domain (which may cause flexibility in the triple helix), and a short N-terminal triple-helical 7S domain. {ECO:0000250|UniProtKB:Q01955, ECO:0000255|PROSITE-ProRule:PRU00736}. TISSUE SPECIFICITY: Highly expressed in kidney and lung. Detected at lower levels in heart, muscle and skin. {ECO:0000269|PubMed:7962065}. +P06684 CO5_MOUSE Complement C5 (Hemolytic complement) [Cleaved into: Complement C5 beta chain; Complement C5 alpha chain; C5a anaphylatoxin; Complement C5 alpha' chain] 1680 188,878 Beta strand (2); Chain (4); Disulfide bond (5); Domain (2); Glycosylation (4); Helix (4); Propeptide (1); Region (1); Signal peptide (1) FUNCTION: Activation of C5 by a C5 convertase initiates the spontaneous assembly of the late complement components, C5-C9, into the membrane attack complex. C5b has a transient binding site for C6. The C5b-C6 complex is the foundation upon which the lytic complex is assembled.; FUNCTION: Derived from proteolytic degradation of complement C5, C5 anaphylatoxin is a mediator of local inflammatory process. Binding to the receptor C5AR1 induces a variety of responses including intracellular calcium release, contraction of smooth muscle, increased vascular permeability, and histamine release from mast cells and basophilic leukocytes. C5a is also a potent chemokine which stimulates the locomotion of polymorphonuclear leukocytes and directs their migration toward sites of inflammation. {ECO:0000250|UniProtKB:P01031}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: C5 precursor is first processed by the removal of 4 basic residues, forming two chains, beta and alpha, linked by a disulfide bond. C5 convertase activates C5 by cleaving the alpha chain, releasing C5a anaphylatoxin and generating C5b (beta chain + alpha' chain). The C5a anaphylatoxin interacts with C5AR1. {ECO:0000250|UniProtKB:P01031}. DISEASE: Note=Murine C5 deficiency is caused by a 2 base-pairs deletion resulting in frameshift and premature truncation. All C5-deficient strains contain this mutation. {ECO:0000269|PubMed:2303408}. +Q91YY4 ATPF2_MOUSE ATP synthase mitochondrial F1 complex assembly factor 2 289 33,289 Chain (1); Erroneous initiation (2); Modified residue (1); Transit peptide (1) FUNCTION: May play a role in the assembly of the F1 component of the mitochondrial ATP synthase (ATPase). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. SUBUNIT: Interacts with ATP5F1A. Interacts with FMC1. {ECO:0000250|UniProtKB:Q8N5M1}. +Q9DBL7 COASY_MOUSE Bifunctional coenzyme A synthase (CoA synthase) [Includes: Phosphopantetheine adenylyltransferase (EC 2.7.7.3) (Dephospho-CoA pyrophosphorylase) (Pantetheine-phosphate adenylyltransferase) (PPAT); Dephospho-CoA kinase (DPCK) (EC 2.7.1.24) (Dephosphocoenzyme A kinase) (DPCOAK)] 563 62,023 Beta strand (6); Chain (1); Domain (1); Erroneous initiation (1); Helix (11); Modified residue (3); Mutagenesis (1); Nucleotide binding (1); Region (1); Turn (1) Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5. Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5. FUNCTION: Bifunctional enzyme that catalyzes the fourth and fifth sequential steps of CoA biosynthetic pathway. The fourth reaction is catalyzed by the phosphopantetheine adenylyltransferase, coded by the coaD domain; the fifth reaction is catalyzed by the dephospho-CoA kinase, coded by the coaE domain. May act as a point of CoA biosynthesis regulation. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Mitochondrion matrix {ECO:0000250}. Note=The protein is mainly present in the mitochondrial matrix, probably anchored to the inner mitochondrial membrane, but this protein is also present in cell lysate. {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed with highest levels in kidney and lowest levels in colon, lung, intestine, and spleen. {ECO:0000269|PubMed:11980892}. +Q61245 COBA1_MOUSE Collagen alpha-1(XI) chain 1804 181,032 Alternative sequence (1); Chain (1); Disulfide bond (6); Domain (8); Glycosylation (1); Metal binding (5); Modified residue (2); Propeptide (2); Region (6); Sequence conflict (6); Signal peptide (1) FUNCTION: May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils. PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.; PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}. SUBUNIT: Trimers composed of three different chains: alpha 1(XI), alpha 2(XI), and alpha 3(XI). Alpha 3(XI) is a post-translational modification of alpha 1(II). Alpha 1(V) can also be found instead of alpha 3(XI)=1(II) (By similarity). {ECO:0000250}. DOMAIN: The C-terminal propeptide, also known as COLFI domain, have crucial roles in tissue growth and repair by controlling both the intracellular assembly of procollagen molecules and the extracellular assembly of collagen fibrils. It binds a calcium ion which is essential for its function (By similarity). {ECO:0000250}. DISEASE: Note=Defects in Col11a1 are associated with chondrodysplasia, an autosomal recessive disease characterized by skeletal defects caused by abnormalities in the cartilage of limbs, ribs, mandibles and trachea. {ECO:0000269|PubMed:7859283}. +Q64739 COBA2_MOUSE Collagen alpha-2(XI) chain 1736 171,535 Alternative sequence (3); Chain (1); Disulfide bond (5); Domain (13); Glycosylation (1); Metal binding (5); Propeptide (1); Region (2); Sequence conflict (13); Signal peptide (1) FUNCTION: May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils. {ECO:0000250}. PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}. SUBUNIT: Trimers composed of three different chains: alpha 1(XI), alpha 2(XI), and alpha 3(XI). Alpha 3(XI) is a post-translational modification of alpha 1(II). Alpha 1(V) can also be found instead of alpha 3(XI)=1(II) (By similarity). {ECO:0000250}. DOMAIN: The C-terminal propeptide, also known as COLFI domain, have crucial roles in tissue growth and repair by controlling both the intracellular assembly of procollagen molecules and the extracellular assembly of collagen fibrils. It binds a calcium ion which is essential for its function (By similarity). {ECO:0000250}. +Q8BZB2 COAC_MOUSE Phosphopantothenoylcysteine decarboxylase (PPC-DC) (EC 4.1.1.36) (CoaC) 204 22,344 Active site (1); Binding site (2); Chain (1); Nucleotide binding (1) Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 3/5. FUNCTION: Necessary for the biosynthesis of coenzyme A. Catalyzes the decarboxylation of 4-phosphopantothenoylcysteine to form 4'-phosphopantotheine (By similarity). {ECO:0000250}. SUBUNIT: Homotrimer. {ECO:0000305}. +Q811I0 ATPF1_MOUSE ATP synthase mitochondrial F1 complex assembly factor 1 324 36,355 Chain (1); Transit peptide (1) FUNCTION: May play an essential role for the assembly of the mitochondrial F1-F0 complex. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. SUBUNIT: Interacts with ATP5B. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed but with low level. {ECO:0000269|PubMed:12965202}. +Q9WVK0 ATRAP_MOUSE Type-1 angiotensin II receptor-associated protein (AT1 receptor-associated protein) 161 17,525 Chain (1); Modified residue (3); Region (1); Sequence conflict (4); Topological domain (4); Transmembrane (3) TRANSMEM 27 47 Helical. {ECO:0000255}.; TRANSMEM 54 74 Helical. {ECO:0000255}.; TRANSMEM 87 107 Helical. {ECO:0000255}. TOPO_DOM 1 26 Extracellular. {ECO:0000255}.; TOPO_DOM 48 53 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 75 86 Extracellular. {ECO:0000255}.; TOPO_DOM 108 161 Cytoplasmic. {ECO:0000255}. FUNCTION: Appears to be a negative regulator of type-1 angiotensin II receptor-mediated signaling by regulating receptor internalisation as well as mechanism of receptor desensitization such as phosphorylation. Induces also a decrease in angiotensin II-stimulated transcriptional activity. May play a role of negative regulator in cardiomyocyte hypertrophy induced by angiotensin II through an inhibition of p38 mitogen-activated protein kinase pathway. {ECO:0000269|PubMed:10358057, ECO:0000269|PubMed:15757644}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Present in perinuclear vesicular membranes, Endoplasmic reticulum, Golgi and endocytic vesicles. {ECO:0000250}. SUBUNIT: Interacts with RACK1 (By similarity), and with the C-terminal region of AGTR1. {ECO:0000250, ECO:0000269|PubMed:10358057}. TISSUE SPECIFICITY: Ubiquitous but more abundant in kidney, testis and heart. {ECO:0000269|PubMed:10358057}. +Q8BMG1 ATRIP_MOUSE ATR-interacting protein (ATM and Rad3-related-interacting protein) 785 85,548 Chain (1); Coiled coil (1); Motif (1); Region (1); Sequence conflict (2) FUNCTION: Required for checkpoint signaling after DNA damage. Required for ATR expression, possibly by stabilizing the protein (By similarity). {ECO:0000250}. PTM: Phosphorylated by ATR. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Redistributes to discrete nuclear foci upon DNA damage. Interacts with CEP164 (via N-terminus) (By similarity). {ECO:0000250}. SUBUNIT: Heterodimer with ATR. The heterodimer binds the RPA complex and is then recruited to single-stranded DNA. Interacts with CINP (By similarity). Interacts with ATR. {ECO:0000250, ECO:0000269|PubMed:20801936}. DOMAIN: The EEXXXDDL motif is required for the interaction with catalytic subunit PRKDC and its recruitment to sites of DNA damage. {ECO:0000250}. +Q68SA9 ATS7_MOUSE A disintegrin and metalloproteinase with thrombospondin motifs 7 (ADAM-TS 7) (ADAM-TS7) (ADAMTS-7) (EC 3.4.24.-) (COMPase) 1657 182,313 Active site (1); Alternative sequence (1); Chain (1); Compositional bias (2); Disulfide bond (11); Domain (11); Glycosylation (2); Metal binding (4); Motif (1); Propeptide (1); Region (1); Sequence conflict (6); Signal peptide (1) FUNCTION: Metalloprotease that may play a role in the degradation of COMP. {ECO:0000269|PubMed:15192113}. PTM: May be cleaved by a furin endopeptidase (By similarity). The precursor is sequentially processed. {ECO:0000250, ECO:0000269|PubMed:15192113}.; PTM: N-glycosylated. Can be O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS family members. Also can be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs. N- and C-glycosylations can also facilitate secretion (By similarity). O-glycosylated proteoglycan. Contains chondroitin sulfate. {ECO:0000250, ECO:0000269|PubMed:15192113}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:15192113}. Note=Also found associated with the external cell surface. SUBUNIT: Interacts with COMP. {ECO:0000250}. DOMAIN: The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix. {ECO:0000250}.; DOMAIN: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme (By similarity). {ECO:0000250}. +P57110 ATS8_MOUSE A disintegrin and metalloproteinase with thrombospondin motifs 8 (ADAM-TS 8) (ADAM-TS8) (ADAMTS-8) (EC 3.4.24.-) (METH-2) 905 98,880 Active site (1); Chain (1); Compositional bias (1); Disulfide bond (10); Domain (4); Glycosylation (4); Metal binding (3); Propeptide (1); Region (1); Signal peptide (1) FUNCTION: Has anti-angiogenic properties. {ECO:0000250}. PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}.; PTM: Glycosylated. Can be O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS family members. Also can be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated. These other glycosylations can also facilitate secretion (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. DOMAIN: The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix. TISSUE SPECIFICITY: Expressed specifically in adult lung and heart and low expression during mouse development. +Q9JKK8 ATR_MOUSE Serine/threonine-protein kinase ATR (EC 2.7.11.1) (Ataxia telangiectasia and Rad3-related protein) 2635 300,224 Chain (1); Domain (3); Modified residue (3); Repeat (2); Sequence conflict (8) FUNCTION: Serine/threonine protein kinase which activates checkpoint signaling upon genotoxic stresses such as ionizing radiation (IR), ultraviolet light (UV), or DNA replication stalling, thereby acting as a DNA damage sensor. Recognizes the substrate consensus sequence [ST]-Q. Phosphorylates BRCA1, CHEK1, MCM2, RAD17, RPA2, SMC1 and p53/TP53, which collectively inhibit DNA replication and mitosis and promote DNA repair, recombination and apoptosis. Phosphorylates Ser-139 of histone variant H2AX/H2AFX at sites of DNA damage, thereby regulating DNA damage response mechanism. Required for FANCD2 ubiquitination. Critical for maintenance of fragile site stability and efficient regulation of centrosome duplication (By similarity). Essential for preventing the occurrence of DNA damage during early embryogenesis. {ECO:0000250|UniProtKB:Q13535, ECO:0000269|PubMed:10691732, ECO:0000269|PubMed:10801416, ECO:0000269|PubMed:12629044, ECO:0000269|PubMed:8843195}. PTM: Phosphorylated; autophosphorylates in vitro. {ECO:0000250|UniProtKB:Q13535}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000269|PubMed:22549958, ECO:0000269|PubMed:23039116, ECO:0000269|PubMed:8843195}. Note=Recruited to chromatin during S-phase. Redistributes to discrete nuclear foci upon DNA damage, hypoxia or replication fork stalling (By similarity). {ECO:0000250|UniProtKB:Q13535}. SUBUNIT: Forms a heterodimer with ATRIP. Binds to DNA, and to UV-damaged DNA with higher affinity. Interacts with RAD17, MSH2 and HDAC2. Present in a complex containing ATRIP and RPA-coated single-stranded DNA. Present in a complex containing CHD4 and HDAC2. Interacts with EEF1E1. This interaction is enhanced by UV irradiation. Interacts with CLSPN and CEP164 (By similarity). Interacts with TELO2 AND TTI1 (By similarity). Interacts with ATRIP (PubMed:20801936). {ECO:0000250|UniProtKB:Q13535, ECO:0000269|PubMed:20801936}. TISSUE SPECIFICITY: Ubiquitous. Expression is highest in testis, where it is restricted to primary spermatocytes. Expression decreases as spermiogenesis proceeds (at protein level). {ECO:0000269|PubMed:8843195}. +Q69Z28 ATS16_MOUSE A disintegrin and metalloproteinase with thrombospondin motifs 16 (ADAM-TS 16) (ADAM-TS16) (ADAMTS-16) (EC 3.4.24.-) 1222 136,282 Active site (1); Alternative sequence (2); Chain (1); Compositional bias (1); Disulfide bond (11); Domain (9); Glycosylation (9); Metal binding (4); Motif (1); Propeptide (1); Region (1); Signal peptide (1) PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}.; PTM: Glycosylated. Can be O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS family members. Also can be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated. These other glycosylations can also facilitate secretion (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. DOMAIN: The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix. {ECO:0000250}.; DOMAIN: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme. +P97857 ATS1_MOUSE A disintegrin and metalloproteinase with thrombospondin motifs 1 (ADAM-TS 1) (ADAM-TS1) (ADAMTS-1) (EC 3.4.24.-) 968 105,801 Active site (1); Chain (1); Compositional bias (2); Disulfide bond (11); Domain (5); Erroneous initiation (1); Frameshift (1); Glycosylation (5); Metal binding (12); Motif (1); Mutagenesis (1); Propeptide (1); Region (1); Sequence conflict (6); Signal peptide (1) FUNCTION: Cleaves aggrecan, a cartilage proteoglycan, at the '1691-Glu-|-Leu-1692' site (within the chondroitin sulfate attachment domain), and may be involved in its turnover. Has angiogenic inhibitor activity (By similarity). Active metalloprotease, which may be associated with various inflammatory processes as well as development of cancer cachexia. May play a critical role in follicular rupture (By similarity). {ECO:0000250, ECO:0000269|PubMed:10781075, ECO:0000269|PubMed:10930576}. PTM: The precursor is cleaved by a furin endopeptidase.; PTM: Glycosylated. Can be O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS family members. Also can be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated. These other glycosylations can also facilitate secretion (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. DOMAIN: The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix.; DOMAIN: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme. +P0C7T6 ATX1L_MOUSE Ataxin-1-like (Brother of ataxin-1) 687 73,374 Chain (1); Domain (1); Modified residue (3); Region (2) FUNCTION: Chromatin-binding factor that repress Notch signaling in the absence of Notch intracellular domain by acting as a CBF1 corepressor. Binds to the HEY promoter and might assist, along with NCOR2, RBPJ-mediated repression (By similarity). Can suppress the cytotoxicity of ATXN1 in spinocerebellar ataxia type 1 (SCA1) (PubMed:16121196). In concert with CIC and ATXN1, involved in brain development (PubMed:28288114). {ECO:0000250|UniProtKB:P0C7T5, ECO:0000269|PubMed:16121196, ECO:0000269|PubMed:28288114}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16121196}. Cell projection, dendrite {ECO:0000269|PubMed:16121196}. Note=Forms nuclear foci. Colocalizes with NCOR2 and HDAC3. Distributed beyond the nucleus into the cell body and dendrites in Purkinje cells and in inferior olive cells. SUBUNIT: Homodimer. Interacts (via AXH domain) with NCOR2 (By similarity). Interacts with ATXN1 and CIC. Directly interacts with RBPJ; this interaction is disrupted in the presence of Notch intracellular domain. Competes with ATXN1 for RBPJ-binding (By similarity). Found in a complex with CIC and ATXN1 (PubMed:28288114). {ECO:0000250|UniProtKB:P0C7T5, ECO:0000269|PubMed:28288114}. TISSUE SPECIFICITY: Expressed in the cortex and hypothalamus (at protein level). Expressed in neuronal cells. Highly expressed in Purkinje cells of cerebellum. {ECO:0000269|PubMed:16121196, ECO:0000269|PubMed:28288114}. +P54254 ATX1_MOUSE Ataxin-1 (Spinocerebellar ataxia type 1 protein homolog) 791 83,793 Chain (1); Compositional bias (1); Cross-link (5); Domain (1); Modified residue (6); Motif (1); Mutagenesis (1); Region (3); Sequence conflict (8) FUNCTION: Chromatin-binding factor that repress Notch signaling in the absence of Notch intracellular domain by acting as a CBF1 corepressor. Binds to the HEY promoter and might assist, along with NCOR2, RBPJ-mediated repression (By similarity). May be involved in RNA metabolism (By similarity). In concert with CIC and ATXN1L, involved in brain development (PubMed:28288114). {ECO:0000250|UniProtKB:P54253, ECO:0000269|PubMed:28288114}. PTM: Ubiquitinated by UBE3A, leading to its degradation by the proteasome. The presence of poly-Gln repeats in trangenic models developed to replicate phenotypes of the spinocerebellar ataxia 1 disease (SCA1) impair ubiquitination and degradation, leading to accumulation of Atxn1 in neurons and subsequent toxicity. {ECO:0000269|PubMed:10624951}.; PTM: Sumoylation is dependent on nuclear localization and phosphorylation at Ser-751. {ECO:0000250|UniProtKB:P54253}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P54253}. Nucleus {ECO:0000269|PubMed:9778246}. Note=Colocalizes with USP7 in the nucleus. {ECO:0000250|UniProtKB:P54253}. SUBUNIT: Homooligomer (By similarity). Interacts with PQBP1, UBQLN4 and USP7 (By similarity). Interacts with ANP32A (PubMed:9353121). Interacts with CIC (PubMed:17190598). Directly interacts with RBPJ; this interaction is disrupted in the presence of Notch intracellular domain. Interacts with ATXN1L; competes with ATXN1L for RBPJ-binding (PubMed:17322884). Found in a complex with CIC and ATXN1L (PubMed:28288114). {ECO:0000250|UniProtKB:P54253, ECO:0000269|PubMed:17190598, ECO:0000269|PubMed:17322884, ECO:0000269|PubMed:28288114, ECO:0000269|PubMed:9353121}. DOMAIN: The AXH domain is required for interaction with CIC. {ECO:0000269|PubMed:17190598}. TISSUE SPECIFICITY: Expressed in the cortex and hypothalamus (at protein level). Widely expressed. In brain, the pattern of distribution is limited to neuron populations. {ECO:0000269|PubMed:28288114, ECO:0000269|PubMed:8789437}. +Q7TQH0 ATX2L_MOUSE Ataxin-2-like protein 1049 110,649 Alternative sequence (2); Chain (1); Compositional bias (1); Cross-link (1); Modified residue (28); Region (1) FUNCTION: Involved in the regulation of stress granule and P-body formation. {ECO:0000250|UniProtKB:Q8WWM7}. PTM: Thrombopoietin triggers the phosphorylation on tyrosine residues in a way that is dependent on MPL C-terminal domain. {ECO:0000250}.; PTM: Asymmetrically dimethylated. Probably methylated by PRMT1. {ECO:0000250|UniProtKB:Q8WWM7}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250|UniProtKB:Q8WWM7}. Nucleus speckle {ECO:0000250|UniProtKB:Q8WWM7}. Cytoplasmic granule {ECO:0000250|UniProtKB:Q8WWM7}. Note=Predominantly cytoplasmic but is also detected in nuclear speckles. Component of cytoplasmic stress granules. Inhibition of methylation alters nuclear localization. Methylation does not seem to be required for localization to stress granules under stress conditions. {ECO:0000250|UniProtKB:Q8WWM7}. SUBUNIT: Interacts with MPL/TPOR and EPOR and dissociates after ligand stimulation. Interacts with DDX6, G3BP, and ATXN2. Interacts with PRMT1 (By similarity). Interacts with CIC and ATXN1 (PubMed:17322884). {ECO:0000250|UniProtKB:Q8WWM7, ECO:0000269|PubMed:17322884}. TISSUE SPECIFICITY: Expressed in cerebellum. {ECO:0000269|PubMed:17322884}. +O70305 ATX2_MOUSE Ataxin-2 (Spinocerebellar ataxia type 2 protein homolog) 1285 136,485 Alternative sequence (2); Chain (1); Compositional bias (4); Cross-link (1); Modified residue (22); Sequence conflict (4) FUNCTION: Involved in EGFR trafficking, acting as negative regulator of endocytic EGFR internalization at the plasma membrane. {ECO:0000269|PubMed:18602463}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9668173}. SUBUNIT: Interacts with RBFOX1 (By similarity). Monomer. Can also form homodimers. Interacts with polyribosomes (By similarity). Interacts with EGFR (By similarity). Interacts with SH3GL3 (By similarity). Interacts with SH3GL2, SH3KBP1 and CBL (PubMed:18602463). Interacts with ATXN2L (By similarity). {ECO:0000250|UniProtKB:Q99700, ECO:0000269|PubMed:18602463, ECO:0000269|PubMed:9668173}. TISSUE SPECIFICITY: Expressed in the heart, lung, liver, kidney, skeletal muscle, spleen and intestine. Predominant expression was seen in the brain where a high level expression was found in the pyramidal cortical neurons, large brain stem neurons and cerebellar Purkinje cells. All three isoforms were found in all the tissues except skeletal muscle where only isoform 1 was found. {ECO:0000269|PubMed:9668173}. +Q9CVD2 ATX3_MOUSE Ataxin-3 (EC 3.4.19.12) (Machado-Joseph disease protein 1 homolog) 355 40,533 Active site (3); Chain (1); Compositional bias (2); Cross-link (2); Domain (4); Modified residue (5); Mutagenesis (1) FUNCTION: Deubiquitinating enzyme involved in protein homeostasis maintenance, transcription, cytoskeleton regulation, myogenesis and degradation of misfolded chaperone substrates (By similarity). Binds long polyubiquitin chains and trims them, while it has weak or no activity against chains of 4 or less ubiquitins (By similarity). Involved in degradation of misfolded chaperone substrates via its interaction with STUB1/CHIP: recruited to monoubiquitinated STUB1/CHIP, and restricts the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension (PubMed:21855799). Interacts with key regulators of transcription and represses transcription: acts as a histone-binding protein that regulates transcription (By similarity). Regulates autophagy via the deubiquitination of 'Lys-402' of BECN1 leading to the stabilization of BECN1 (PubMed:28445460). {ECO:0000250|UniProtKB:P54252, ECO:0000269|PubMed:21855799, ECO:0000269|PubMed:28445460}. PTM: Monoubiquitinated by UBE2W, possibly leading to activate the deubiquitinating enzyme activity (By similarity). {ECO:0000250|UniProtKB:P54252}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P54252}. SUBUNIT: Interacts with DNA repair proteins RAD23A and RAD23B (By similarity). Interacts with STUB1/CHIP (when monoubiquitinated) (PubMed:21855799). Interacts with BECN1 (via its poly-Gln domain) (PubMed:28445460). {ECO:0000250|UniProtKB:P54252, ECO:0000269|PubMed:21855799, ECO:0000269|PubMed:28445460}. DOMAIN: The UIM domains bind ubiquitin and interact with various E3 ubiquitin-protein ligase, such as STUB1/CHIP. They are essential to limit the length of ubiquitin chains (PubMed:21855799). {ECO:0000269|PubMed:21855799}. +E9Q6Z5 AUNIP_MOUSE Aurora kinase A and ninein-interacting protein 340 37,684 Chain (1); Modified residue (1); Region (2); Sequence conflict (5) FUNCTION: DNA-binding protein that accumulates at DNA double-strand breaks (DSBs) following DNA damage and promotes DNA resection and homologous recombination. Serves as a sensor of DNA damage: binds DNA with a strong preference for DNA substrates that mimic structures generated at stalled replication forks, and anchors RBBP8/CtIP to DSB sites to promote DNA end resection and ensuing homologous recombination repair. Inhibits non-homologous end joining (NHEJ). Required for the dynamic movement of AURKA at the centrosomes and spindle apparatus during the cell cycle. {ECO:0000250|UniProtKB:Q9H7T9}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H7T9}. Chromosome {ECO:0000250|UniProtKB:Q9H7T9}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9H7T9}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q9H7T9}. Note=Accumulates at sites of DNA damage by binding to DNA substrates that mimick structures generated at stalled replication forks. Localizes to the centrosome in interphase and to the spindle pole in metaphase. {ECO:0000250|UniProtKB:Q9H7T9}. SUBUNIT: Interacts (via C-terminus) with AURKA (via C-terminus). Interacts (via N-terminus) with NIN; this interaction blocks NIN phosphorylation by both AURKA and GSK3B. Identified in a complex with NIN and AURKA. Interacts with RBBP8/CtIP. {ECO:0000250|UniProtKB:Q9H7T9}. +P97477 AURKA_MOUSE Aurora kinase A (EC 2.7.11.1) (Aurora 2) (Aurora family kinase 1) (Aurora/IPL1-related kinase 1) (ARK-1) (Aurora-related kinase 1) (Ipl1- and aurora-related kinase 1) (Serine/threonine-protein kinase 6) (Serine/threonine-protein kinase Ayk1) (Serine/threonine-protein kinase aurora-A) 395 44,772 Active site (1); Alternative sequence (1); Beta strand (8); Binding site (3); Chain (1); Cross-link (1); Domain (1); Frameshift (1); Helix (15); Modified residue (5); Nucleotide binding (2); Region (1); Sequence conflict (1); Turn (1) FUNCTION: Mitotic serine/threonine kinases that contributes to the regulation of cell cycle progression. Associates with the centrosome and the spindle microtubules during mitosis and plays a critical role in various mitotic events including the establishment of mitotic spindle, centrosome duplication, centrosome separation as well as maturation, chromosomal alignment, spindle assembly checkpoint, and cytokinesis. Required for initial activation of CDK1 at centrosomes. Phosphorylates numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B, DLGP5, HDAC6, KIF2A, LATS2, NDEL1, PARD3, PPP1R2, PLK1, RASSF1, TACC3, p53/TP53 and TPX2. Regulates KIF2A tubulin depolymerase activity. Required for normal axon formation. Plays a role in microtubule remodeling during neurite extension. Important for microtubule formation and/or stabilization. Also acts as a key regulatory component of the p53/TP53 pathway, and particularly the checkpoint-response pathways critical for oncogenic transformation of cells, by phosphorylating and stabilizing p53/TP53. Phosphorylates its own inhibitors, the protein phosphatase type 1 (PP1) isoforms, to inhibit their activity. Necessary for proper cilia disassembly prior to mitosis. {ECO:0000269|PubMed:19075002, ECO:0000269|PubMed:19668197, ECO:0000269|PubMed:20643351, ECO:0000269|PubMed:9245792}. PTM: Activated by phosphorylation at Thr-279; this brings about a change in the conformation of the activation segment. Phosphorylation at Thr-279 varies during the cell cycle and is highest during M phase. Autophosphorylated at Thr-279 upon TPX2 binding. Thr-279 can be phosphorylated by several kinases, including PAK and PKA. Protein phosphatase type 1 (PP1) binds AURKA and inhibits its activity by dephosphorylating Thr-279 during mitosis. Phosphorylation at Ser-333 decreases the kinase activity. PPP2CA controls degradation by dephosphorylating Ser-52 at the end of mitosis (By similarity). {ECO:0000250}.; PTM: Ubiquitinated by the anaphase-promoting complex (APC), leading to its degradation by the proteasome (By similarity). Ubiquitinated by CHFR, leading to its degradation by the proteasome. Ubiquitinated by the E3 ubiquitin-protein ligase complex SCF(FBXL7) during mitosis, leading to its degradation by the proteasome. {ECO:0000250, ECO:0000269|PubMed:15793587, ECO:0000269|PubMed:22306998}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:19668197, ECO:0000269|PubMed:20643351}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:19075002, ECO:0000269|PubMed:9245792}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:23807208}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:23807208}. Note=Localizes on centrosomes in interphase cells and at each spindle pole in mitosis (PubMed:9245792). Associates with both the pericentriolar material (PCM) and centrioles (By similarity). Colocalized with SIRT2 at centrosome (By similarity). Detected at the neurite hillock in developing neurons (PubMed:19668197). {ECO:0000250|UniProtKB:O14965, ECO:0000269|PubMed:19668197, ECO:0000269|PubMed:9245792}. SUBUNIT: Interacts with CPEB1, JTB, TACC1, TPX2, PPP2CA, as well as with the protein phosphatase type 1 (PP1) isoforms PPP1CA, PPP1CB and PPP1CC (By similarity). Interacts also with its substrates ARHGEF2, BORA, BRCA1, KIF2A, PARD3, and p53/TP53. Interaction with BORA promotes phosphorylation of PLK1. Interacts with GADD45A, competing with its oligomerization (By similarity). Interacts with FBXL7 and PIFO. Interacts (via C-terminus) with AUNIP (via C-terminus) (By similarity). Identified in a complex with AUNIP and NIN (By similarity). Interacts with SIRT2 (By similarity). Interacts with FRY; this interaction facilitates AURKA-mediated PLK1 phosphorylation. Interacts with MYCN; interaction is phospho-independent and triggers AURKA activation; AURKA competes with FBXW7 for binding to unphosphorylated MYCN but not for binding to phosphorylated MYCN (By similarity). Interacts with HNRNPU (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O14965, ECO:0000269|PubMed:18579375, ECO:0000269|PubMed:18678489, ECO:0000269|PubMed:20643351, ECO:0000269|PubMed:22306998, ECO:0000269|PubMed:22753416}. TISSUE SPECIFICITY: Detected in embryonic neurons in dorsal root ganglia and brain cortex (at protein level). Highly expressed in testis, in about one third of the seminiferous tubules. Expression is restricted to specific spermatocytes nearing completion of prophase, with levels falling off on transition to elongated spermatids. Highly expressed in the ovary, expression in the oocyte starts around the transition to large growing follicle. Abundant expression is seen in the proliferating granulosa and thecal cells of the growing follicle, and in the young corpus luteum. Very weakly expressed in spleen and intestine. {ECO:0000269|PubMed:19668197, ECO:0000269|PubMed:9245792}. +A0A087WPF7 AUTS2_MOUSE Autism susceptibility gene 2 protein homolog 1261 138,920 Alternative sequence (4); Chain (1); Compositional bias (2); Modified residue (2); Region (1) FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. The PRC1-like complex that contains PCGF5, RNF2, CSNK2B, RYBP and AUTS2 has decreased histone H2A ubiquitination activity, due to the phosphorylation of RNF2 by CSNK2B. As a consequence, the complex mediates transcriptional activation (By similarity). In the cytoplasm, plays a role in axon and dendrite elongation and in neuronal migration during embryonic brain development. Promotes reorganization of the actin cytoskeleton, lamellipodia formation and neurite elongation via its interaction with RAC guanine nucleotide exchange factors, which then leads to the activation of RAC1 (PubMed:25533347). {ECO:0000250|UniProtKB:Q8WXX7, ECO:0000269|PubMed:25533347}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19948250, ECO:0000269|PubMed:25519132, ECO:0000269|PubMed:25533347}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:25533347}. Cell projection, growth cone {ECO:0000269|PubMed:25533347}. Note=Detected both in cytoplasm and nucleus (PubMed:25533347). Colocalizes with RAC1 at actin-rich growth cones (PubMed:25533347). Detected on the promoter region of actively transcribed genes (PubMed:25519132). {ECO:0000269|PubMed:25519132, ECO:0000269|PubMed:25533347}. SUBUNIT: Component of a PRC1-like complex that contains PCGF5, RNF2, CSNK2B, RYBP and AUTS2 (PubMed:25519132). Within this complex, interacts directly with PCGF5 and CSNK2B (By similarity). Interacts with the histone acetyltransferase EP300/p300 (By similarity). Interacts (via Pro-rich region) with PREX1, DOCK1 and ELMO2 (PubMed:25533347). {ECO:0000250|UniProtKB:Q8WXX7, ECO:0000269|PubMed:25533347, ECO:0000305|PubMed:25519132}. DOMAIN: The Pro-rich region is important for the interaction with RAC guanine nucleotide exchange factors and the subsequent activation of RAC1, which then promotes lamellipodia formation. {ECO:0000269|PubMed:25533347}. TISSUE SPECIFICITY: Detected in brain cortex in embryo, neonates and adults (at protein level) (PubMed:19948250, PubMed:25533347, PubMed:25519132). Detected in embryonic and adult Purkinje cells in the cerebellum (PubMed:19948250). Detected in dorsal thalamus and in dopaminergic neurons in substantia nigra (PubMed:19948250). {ECO:0000269|PubMed:19948250, ECO:0000269|PubMed:25519132, ECO:0000269|PubMed:25533347}. +Q80TZ3 AUXI_MOUSE Putative tyrosine-protein phosphatase auxilin (EC 3.1.3.48) (DnaJ homolog subfamily C member 6) 938 102,299 Active site (1); Alternative sequence (2); Chain (1); Compositional bias (1); Domain (3); Erroneous initiation (1); Modified residue (4); Motif (1); Region (1); Repeat (3); Sequence conflict (1) FUNCTION: Recruits HSPA8/HSC70 to clathrin-coated vesicles and promotes uncoating of clathrin-coated vesicles. Plays a role in clathrin-mediated endocytosis in neurons. {ECO:0000269|PubMed:20160091}. SUBUNIT: Interacts with HSPA8/HSC70. Interacts with CLTC. Interacts with AP2A2 (By similarity). {ECO:0000250|UniProtKB:Q27974}. +P01193 COLI_MOUSE Pro-opiomelanocortin (POMC) (Corticotropin-lipotropin) [Cleaved into: NPP; Melanotropin gamma (Gamma-MSH); Corticotropin (Adrenocorticotropic hormone) (ACTH); Melanocyte-stimulating hormone alpha (Alpha-MSH) (Melanotropin alpha); Corticotropin-like intermediary peptide (CLIP); Lipotropin beta (Beta-LPH); Lipotropin gamma (Gamma-LPH); Melanocyte-stimulating hormone beta (Beta-MSH) (Melanotropin beta); Beta-endorphin; Met-enkephalin] 235 26,707 Glycosylation (2); Modified residue (4); Peptide (10); Propeptide (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Corticotropin: Stimulates the adrenal glands to release cortisol.; FUNCTION: Melanocyte-stimulating hormone alpha: Anorexigenic peptide. Increases the pigmentation of skin by increasing melanin production in melanocytes.; FUNCTION: Melanocyte-stimulating hormone beta: Increases the pigmentation of skin by increasing melanin production in melanocytes.; FUNCTION: Beta-endorphin: Endogenous orexigenic opiate.; FUNCTION: Met-enkephalin: Endogenous opiate. PTM: Specific enzymatic cleavages at paired basic residues yield the different active peptides. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25707796}. Note=Melanocyte-stimulating hormone alpha and beta-endorphin are stored in separate granules in hypothalamic POMC neurons, suggesting that secretion may be under the control of different regulatory mechanisms. {ECO:0000269|PubMed:25707796}. TISSUE SPECIFICITY: ACTH and MSH are produced by the pituitary gland. +Q3UW21 COLL2_MOUSE Colipase-like protein 2 102 11,027 Chain (1); Disulfide bond (5); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q64373 B2CL1_MOUSE Bcl-2-like protein 1 (Bcl2-L-1) (Apoptosis regulator Bcl-X) 233 26,132 Alternative sequence (3); Chain (1); Helix (11); Modified residue (2); Motif (4); Sequence conflict (1); Transmembrane (1); Turn (1) TRANSMEM 210 226 Helical. {ECO:0000255}. FUNCTION: Potent inhibitor of cell death. Inhibits activation of caspases. Appears to regulate cell death by blocking the voltage-dependent anion channel (VDAC) by binding to it and preventing the release of the caspase activator, CYC1, from the mitochondrial membrane. Also acts as a regulator of G2 checkpoint and progression to cytokinesis during mitosis. {ECO:0000269|PubMed:9390687}.; FUNCTION: Isoform Bcl-X(L) also regulates presynaptic plasticity, including neurotransmitter release and recovery, number of axonal mitochondria as well as size and number of synaptic vesicle clusters. During synaptic stimulation, increases ATP availability from mitochondria through regulation of mitochondrial membrane ATP synthase F(1)F(0) activity and regulates endocytic vesicle retrieval in hippocampal neurons through association with DMN1L and stimulation of its GTPase activity in synaptic vesicles (By similarity). May attenuate inflammation impairing NLRP1-inflammasome activation, hence CASP1 activation and IL1B release (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q07817}.; FUNCTION: Isoform Bcl-X(S) promotes apoptosis. {ECO:0000250}. PTM: Proteolytically cleaved by caspases during apoptosis. The cleaved protein, lacking the BH4 motif, has pro-apoptotic activity. {ECO:0000250}.; PTM: Phosphorylated on Ser-62 by CDK1. This phosphorylation is partial in normal mitotic cells, but complete in G2-arrested cells upon DNA-damage, thus promoting subsequent apoptosis probably by triggering caspases-mediated proteolysis. Phosphorylated by PLK3, leading to regulate the G2 checkpoint and progression to cytokinesis during mitosis. Phosphorylation at Ser-49 appears during the S phase and G2, disappears rapidly in early mitosis during prometaphase, metaphase and early anaphase, and re-appears during telophase and cytokinesis (By similarity). {ECO:0000250}.; PTM: Ubiquitinated by RNF183 during prolonged ER stress, leading to degradation by the proteosome. {ECO:0000250|UniProtKB:Q07817}. SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000269|PubMed:7607090}; Single-pass membrane protein {ECO:0000269|PubMed:7607090}. Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:7607090}. Note=Localizes to the centrosome when phosphorylated at Ser-49.; SUBCELLULAR LOCATION: Isoform Bcl-X(L): Mitochondrion inner membrane. Mitochondrion outer membrane. Mitochondrion matrix {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Note=After neuronal stimulation, translocates from cytosol to synaptic vesicle and mitochondrion membrane in a calmodulin-dependent manner. {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform Bcl-X(delta-TM): Cytoplasm. SUBUNIT: Homodimer. Isoform Bcl-X(L) forms heterodimers with BAX, BAK or BCL2. Heterodimerization with BAX does not seem to be required for anti-apoptotic activity. Interacts with BAD. Interacts (isoform Bcl-X(L)) with SIVA1 (isoform 1); the interaction inhibits the anti-apoptotic activity. Interacts with BECN1 and PGAM5. Isoform Bcl-X(L) interacts with IKZF3. Interacts with HEBP2. Isoform Bcl-X(L) interacts with BOP. Interacts with p53/TP53 and BBC3; interaction with BBC3 disrupts the interaction with p53/TP53. Isoform Bcl-X(L) interacts with DNM1L and CLTA; DNM1L and BCL2L1 isoform BCL-X(L) may form a complex in synaptic vesicles that also contains clathrin and MFF. Interacts with ATP5F1A and ATP5F1B; the interactions mediate the association of isoform Bcl-X(L) with the mitochondrial membrane ATP synthase F(1)F(0) ATP synthase (By similarity). Interacts with VDAC1 (By similarity). Isoform Bcl-X(L) interacts (via the loop between motifs BH4 and BH3) with NLRP1 (via LRR repeats), but not with NLRP2, NLRP3, NLRP4, PYCARD, nor MEFV. Interacts with BCL2L11 (via BH3) (PubMed:27013495, PubMed:14499110). Interacts with RNF183 (By similarity). {ECO:0000250|UniProtKB:P53563, ECO:0000250|UniProtKB:Q07817, ECO:0000269|PubMed:14499110, ECO:0000269|PubMed:27013495}. DOMAIN: The BH4 motif is required for anti-apoptotic activity. The BH1 and BH2 motifs are required for both heterodimerization with other Bcl-2 family members and for repression of cell death.; DOMAIN: The loop between motifs BH4 and BH3 is required for the interaction with NLRP1. {ECO:0000250|UniProtKB:Q07817}. TISSUE SPECIFICITY: Widely expressed, with highest levels in the brain, thymus, bone marrow, and kidney. Bcl-X(L) and Bcl-X(delta-TM) expression is enhanced in B- and T-lymphocytes that have been activated. {ECO:0000269|PubMed:7607090}. +Q3V4B5 COMD6_MOUSE COMM domain-containing protein 6 87 9,795 Chain (1); Domain (1); Modified residue (1) FUNCTION: May modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes. Inhibits TNF-induced NFKB1 activation. {ECO:0000250|UniProtKB:Q7Z4G1}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q7Z4G1}. Cytoplasm {ECO:0000250|UniProtKB:Q7Z4G1}. SUBUNIT: Homodimer. Interacts (via COMM domain) with COMMD1 (via COMM domain). Does not interact with NFKBIB. Interacts with RELA, RELB, NFKB1/p105. Does not interact with NFKBIB. Interacts with CCDC22, CCDC93, SCNN1B, CUL4A. {ECO:0000250|UniProtKB:Q7Z4G1}. +P70345 B2CL2_MOUSE Bcl-2-like protein 2 (Bcl2-L-2) (Apoptosis regulator Bcl-W) (c98) 193 20,790 Alternative sequence (1); Chain (1); Frameshift (1); Initiator methionine (1); Modified residue (1); Motif (3); Sequence conflict (8) FUNCTION: Promotes cell survival. Blocks dexamethasone-induced apoptosis. Mediates survival of postmitotic Sertoli cells by suppressing death-promoting activity of BAX. {ECO:0000269|PubMed:11784036, ECO:0000269|PubMed:14746907, ECO:0000269|PubMed:8761287}. SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Loosely associated with the mitochondrial membrane in healthy cells. During apoptosis, tightly bound to the membrane (By similarity). {ECO:0000250}. SUBUNIT: Interacts with HIF3A isoform 2 (via C-terminus domain) (PubMed:21546903). Interacts with BOP (By similarity). {ECO:0000250, ECO:0000269|PubMed:21546903}. DOMAIN: The BH4 motif seems to be involved in the anti-apoptotic function.; DOMAIN: The BH1 and BH2 motifs form a hydrophobic groove which acts as a docking site for the BH3 domain of some pro-apoptotic proteins. The C-terminal residues of BCL2L2 fold into the BH3-binding cleft and modulate pro-survival activity by regulating ligand access. When BH3 domain-containing proteins bind, they displace the C-terminus, allowing its insertion into the membrane and neutralizing the pro-survival activity of BCL2L2 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in almost all myeloid cell lines and in a wide range of tissues, with highest levels in brain, colon, and salivary gland. +Q9CZG3 COMD8_MOUSE COMM domain-containing protein 8 183 20,852 Chain (1); Domain (1); Sequence conflict (1) FUNCTION: May modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes. May down-regulate activation of NF-kappa-B. {ECO:0000250|UniProtKB:Q9NX08}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NX08}. Nucleus {ECO:0000250|UniProtKB:Q9NX08}. SUBUNIT: Interacts (via COMM domain) with COMMD1 (via COMM domain). Interacts with RELA, RELB, NFKB1/p105. Interacts with CCDC22, CCDC93, SCNN1B, CUL1, CUL2, CUL3, CUL4A, CUL4B, CUL5. {ECO:0000250|UniProtKB:Q9NX08}. +Q8K2Q0 COMD9_MOUSE COMM domain-containing protein 9 198 21,850 Chain (1); Domain (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (1); Sequence conflict (1) FUNCTION: May modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes. May down-regulate activation of NF-kappa-B. Modulates Na(+) transport in epithelial cells by regulation of apical cell surface expression of amiloride-sensitive sodium channel (ENaC) subunits. {ECO:0000250|UniProtKB:Q9P000}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9P000}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q9P000}. SUBUNIT: Interacts with RELB and NFKB1/p105. Interacts with CCDC22, CCDC93, SCNN1B, CUL1. {ECO:0000250|UniProtKB:Q9P000}. +Q8JZY2 COMDA_MOUSE COMM domain-containing protein 10 (Down-regulated in W/WV mouse stomach 2) (mDRWMS2) 202 22,812 Chain (1); Domain (1); Initiator methionine (1); Modified residue (2) FUNCTION: May modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes. May down-regulate activation of NF-kappa-B. {ECO:0000250|UniProtKB:Q9Y6G5}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y6G5}. Nucleus {ECO:0000250|UniProtKB:Q9Y6G5}. SUBUNIT: Interacts (via COMM domain) with COMMD1 (via COMM domain). Interacts with RELA, RELB, NFKB1/p105, NFKB2/p100. Interacts with CCDC22, CCDC93, SCNN1B, CUL1, CUL2, CUL3, CUL4A, CUL4B, CUL7. {ECO:0000250|UniProtKB:Q9Y6G5}. +Q9R0G6 COMP_MOUSE Cartilage oligomeric matrix protein (COMP) 755 82,342 Chain (1); Disulfide bond (23); Domain (5); Glycosylation (2); Helix (1); Modified residue (1); Region (2); Repeat (8); Sequence conflict (1); Signal peptide (1) FUNCTION: May play a role in the structural integrity of cartilage via its interaction with other extracellular matrix proteins such as the collagens and fibronectin. Can mediate the interaction of chondrocytes with the cartilage extracellular matrix through interaction with cell surface integrin receptors. Could play a role in the pathogenesis of osteoarthritis. Potent suppressor of apoptosis in both primary chondrocytes and transformed cells. Suppresses apoptosis by blocking the activation of caspase-3 and by inducing the IAP family of survival proteins (BIRC3, BIRC2, BIRC5 and XIAP). Essential for maintaining a vascular smooth muscle cells (VSMCs) contractile/differentiated phenotype under physiological and pathological stimuli. Maintains this phenotype of VSMCs by interacting with ITGA7 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. SUBUNIT: Pentamer; disulfide-linked. Exists in a more compact conformation in the presence of calcium and shows a more extended conformation in the absence of calcium. Interacts with ITGB3, ITGA5 and FN1. Binding to FN1 requires the presence of divalent cations (Ca(2+), Mg(2+) or Mn(2+)). The greatest amount of binding is seen in the presence of Mn(2+). Interacts with MATN1, MATN3, MATN4 and ACAN. Binds heparin, heparan sulfate and chondroitin sulfate. EDTA dimishes significantly its binding to ACAN and abolishes its binding to MATN3, MATN4 and chondroitin sulfate. Interacts with collagen I, II and IX and interaction with these collagens is dependent on the presence of zinc ions. Interacts with ADAMTS12. Interacts with ITGA7 (By similarity). {ECO:0000250}. DOMAIN: The cell attachment motif mediates the attachment to chondrocytes. It mediates the induction of both the IAP family of survival proteins and the antiapoptotic response (By similarity). {ECO:0000250}.; DOMAIN: The TSP C-terminal domain mediates interaction with FN1 and ACAN. {ECO:0000250}.; DOMAIN: Each of the eight TSP type-3 repeats binds two calcium ions. The TSP C-terminal domain binds three calcium ions (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed only in cartilage, including nasal, knee epiphyseal and rib tissues. {ECO:0000269|PubMed:21624478}. +O88587 COMT_MOUSE Catechol O-methyltransferase (EC 2.1.1.6) 265 29,486 Alternative sequence (1); Beta strand (10); Binding site (10); Chain (1); Helix (13); Metal binding (3); Modified residue (3); Mutagenesis (1); Region (1); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 3 19 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 2 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 20 265 Extracellular. {ECO:0000255}. FUNCTION: Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones. Also shortens the biological half-lives of certain neuroactive drugs, like L-DOPA, alpha-methyl DOPA and isoproterenol. SUBCELLULAR LOCATION: Isoform Soluble: Cytoplasm.; SUBCELLULAR LOCATION: Isoform Membrane-bound: Cell membrane; Single-pass type II membrane protein; Extracellular side. +P13808 B3A2_MOUSE Anion exchange protein 2 (AE 2) (Anion exchanger 2) (Band 3-related protein) (B3RP) (Non-erythroid band 3-like protein) (Solute carrier family 4 member 2) 1237 136,814 Alternative sequence (5); Chain (1); Compositional bias (3); Glycosylation (3); Lipidation (1); Modified residue (9); Region (1); Sequence conflict (5); Topological domain (3); Transmembrane (10) TRANSMEM 704 727 Helical. {ECO:0000255}.; TRANSMEM 733 770 Helical. {ECO:0000255}.; TRANSMEM 790 812 Helical. {ECO:0000255}.; TRANSMEM 822 843 Helical. {ECO:0000255}.; TRANSMEM 897 914 Helical. {ECO:0000255}.; TRANSMEM 930 950 Helical. {ECO:0000255}.; TRANSMEM 984 1006 Helical. {ECO:0000255}.; TRANSMEM 1032 1053 Helical. {ECO:0000255}.; TRANSMEM 1087 1132 Helical. {ECO:0000255}.; TRANSMEM 1159 1195 Helical. {ECO:0000255}. TOPO_DOM 1 703 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 844 896 Extracellular. {ECO:0000255}.; TOPO_DOM 915 929 Cytoplasmic. {ECO:0000255}. FUNCTION: Plasma membrane anion exchange protein of wide distribution. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Isoform a is widely expressed at similar levels in all tissues examined. Isoforms B1 and B2 are predominantly expressed in stomach although they are also detected at lower levels in other tissues. Isoform C1 is stomach-specific. Isoform C2 is expressed at slightly higher levels in lung and stomach than in other tissues. {ECO:0000269|PubMed:11006093}. +P16283 B3A3_MOUSE Anion exchange protein 3 (AE 3) (Anion exchanger 3) (Neuronal band 3-like protein) (Solute carrier family 4 member 3) 1227 135,373 Alternative sequence (4); Chain (1); Compositional bias (1); Glycosylation (1); Lipidation (1); Modified residue (5); Region (1); Sequence conflict (4); Topological domain (2); Transmembrane (10) TRANSMEM 708 730 Helical. {ECO:0000255}.; TRANSMEM 736 773 Helical. {ECO:0000255}.; TRANSMEM 793 815 Helical. {ECO:0000255}.; TRANSMEM 825 846 Helical. {ECO:0000255}.; TRANSMEM 888 905 Helical. {ECO:0000255}.; TRANSMEM 921 941 Helical. {ECO:0000255}.; TRANSMEM 975 997 Helical. {ECO:0000255}.; TRANSMEM 1023 1044 Helical. {ECO:0000255}.; TRANSMEM 1078 1123 Helical. {ECO:0000255}.; TRANSMEM 1150 1186 Helical. {ECO:0000255}. TOPO_DOM 1 707 Cytoplasmic.; TOPO_DOM 906 920 Cytoplasmic. {ECO:0000255}. FUNCTION: Plasma membrane anion exchange protein. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Neuronal. +Q30D77 COOA1_MOUSE Collagen alpha-1(XXIV) chain 1733 175,733 Chain (1); Domain (17); Glycosylation (4); Sequence conflict (2); Signal peptide (1) FUNCTION: Involved in osteoblast differentiation. {ECO:0000269|PubMed:16373341}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. TISSUE SPECIFICITY: Expressed in skeleton. Found at ossification centers of the craniofacial, axial and appendicular skeleton. Also expressed in retina and to a lower extent in cornea, skin and tendon. {ECO:0000269|PubMed:16373341}. +Q9CW73 B3GA1_MOUSE Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 1 (EC 2.4.1.135) (Beta-1,3-glucuronyltransferase 1) (Glucuronosyltransferase P) (GlcAT-P) (UDP-GlcUA:glycoprotein beta-1,3-glucuronyltransferase) (GlcUAT-P) 334 38,237 Active site (1); Alternative sequence (1); Binding site (3); Chain (1); Erroneous initiation (1); Glycosylation (3); Metal binding (1); Modified residue (2); Nucleotide binding (3); Region (2); Sequence conflict (1); Site (2); Topological domain (2); Transmembrane (1) TRANSMEM 7 27 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 28 334 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Involved in the biosynthesis of L2/HNK-1 carbohydrate epitope on glycoproteins. Can also play a role in glycosaminoglycan biosynthesis. Substrates include asialo-orosomucoid (ASOR), asialo-fetuin, and asialo-neural cell adhesion molecule. Requires sphingomyelin for activity: stearoyl-sphingomyelin was the most effective, followed by palmitoyl-sphingomyelin and lignoceroyl-sphingomyelin. Activity was demonstrated only for sphingomyelin with a saturated fatty acid and not for that with an unsaturated fatty acid, regardless of the length of the acyl group. {ECO:0000250|UniProtKB:O35789}. PTM: The soluble form derives from the membrane form by proteolytic processing. {ECO:0000250|UniProtKB:O35789}. SUBCELLULAR LOCATION: Isoform 1: Golgi apparatus membrane {ECO:0000250|UniProtKB:O35789}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:O35789}. Secreted {ECO:0000250|UniProtKB:O35789}.; SUBCELLULAR LOCATION: Isoform 2: Golgi apparatus membrane {ECO:0000250|UniProtKB:O35789}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:O35789}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O35789}. Secreted {ECO:0000250|UniProtKB:O35789}. SUBUNIT: Homodimer. Interacts with SAR1A. {ECO:0000250|UniProtKB:O35789}. +Q99MQ5 COPA1_MOUSE Collagen alpha-1(XXV) chain (CLAC-P) [Cleaved into: Collagen-like Alzheimer amyloid plaque component (CLAC)] 666 65,377 Chain (2); Domain (8); Region (1); Sequence conflict (3); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 34 54 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 33 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 55 666 Extracellular. {ECO:0000255}. FUNCTION: Inhibits fibrillization of amyloid-beta peptide during the elongation phase. Has also been shown to assemble amyloid fibrils into protease-resistant aggregates. Binds heparin (By similarity). {ECO:0000250|UniProtKB:Q9BXS0}. PTM: Undergoes proteolytic cleavage by furin protease to yield the soluble collagen-like Alzheimer amyloid plaque component. {ECO:0000250|UniProtKB:Q9BXS0}.; PTM: Glycosylated. {ECO:0000250|UniProtKB:Q9BXS0}.; PTM: Hydroxylated on proline and lysine residues. {ECO:0000250|UniProtKB:Q9BXS0}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Note=After proteolytic cleavage, CLAC is secreted. {ECO:0000250}. SUBUNIT: Forms homodimers and homotrimers. Binds to the fibrillized forms of amyloid-beta protein 40 (beta-APP40) and amyloid-betad protein 42 (beta-APP42). Found associated with beta-APP42 more frequently than with beta-APP40 (By similarity). {ECO:0000250|UniProtKB:Q9BXS0}. TISSUE SPECIFICITY: Expressed predominantly in neurons with low levels also detected in heart, testis and eye. {ECO:0000269|PubMed:11927537}. +Q8CIE6 COPA_MOUSE Coatomer subunit alpha (Alpha-coat protein) (Alpha-COP) [Cleaved into: Xenin (Xenopsin-related peptide); Proxenin] 1224 138,432 Chain (1); Modified residue (6); Peptide (2); Repeat (6); Sequence conflict (2) FUNCTION: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). {ECO:0000250}.; FUNCTION: Xenin stimulates exocrine pancreatic secretion. It inhibits pentagastrin-stimulated secretion of acid, to induce exocrine pancreatic secretion and to affect small and large intestinal motility. In the gut, xenin interacts with the neurotensin receptor (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. {ECO:0000250}.; SUBCELLULAR LOCATION: Xenin: Secreted {ECO:0000250}. SUBUNIT: Oligomeric complex that consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits. Probably interacts with PEX11A. Interacts with SCYL1. Interacts with JAGN1 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P53621}. +Q8VI16 B3GN9_MOUSE UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 9 (BGnT-9) (Beta-1,3-Gn-T9) (Beta-1,3-N-acetylglucosaminyltransferase 9) (Beta3Gn-T9) (EC 2.4.1.-) 399 44,231 Chain (1); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 13 29 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 12 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 30 399 Lumenal. {ECO:0000255}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000255}. +O54904 B3GT1_MOUSE Beta-1,3-galactosyltransferase 1 (Beta-1,3-GalTase 1) (Beta3Gal-T1) (Beta3GalT1) (EC 2.4.1.86) (UDP-Gal:betaGlcNAc beta 1,3-galactosyltransferase-I) (UDP-galactose:beta-N-acetyl-glucosamine-beta-1,3-galactosyltransferase 1) 326 37,993 Chain (1); Glycosylation (2); Natural variant (1); Topological domain (2); Transmembrane (1) TRANSMEM 7 26 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 27 326 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Beta-1,3-galactosyltransferase that transfers galactose from UDP-alpha-D-galactose to substrates with a terminal beta-N-acetylglucosamine (beta-GlcNAc) residue. Involved in the biosynthesis of the carbohydrate moieties of glycolipids and glycoproteins. {ECO:0000269|PubMed:9417047}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9417047}. +O54905 B3GT2_MOUSE Beta-1,3-galactosyltransferase 2 (Beta-1,3-GalTase 2) (Beta3Gal-T2) (Beta3GalT2) (EC 2.4.1.86) (UDP-Gal:betaGlcNAc beta 1,3-galactosyltransferase-II) 422 49,095 Chain (1); Glycosylation (5); Natural variant (5); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 21 43 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 20 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 44 422 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Beta-1,3-galactosyltransferase that transfers galactose from UDP-galactose to substrates with a terminal beta-N-acetylglucosamine (beta-GlcNAc) residue. Can also utilize substrates with a terminal galactose residue, albeit with lower efficiency. Involved in the biosynthesis of the carbohydrate moieties of glycolipids and glycoproteins. {ECO:0000269|PubMed:9417047}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Detected in brain and heart. {ECO:0000269|PubMed:9417047}. +Q8K0J2 B3GN7_MOUSE UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 7 (BGnT-7) (Beta-1,3-Gn-T7) (Beta-1,3-N-acetylglucosaminyltransferase 7) (Beta3Gn-T7) (EC 2.4.1.-) 397 45,379 Chain (1); Glycosylation (4); Sequence conflict (6); Topological domain (2); Transmembrane (1) TRANSMEM 7 26 Helical. {ECO:0000255}. TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 27 397 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: May be involved in keratane sulfate biosynthesis. Transfers N-acetylgalactosamine on to keratan sulfate-related glycans. May play a role in preventing cells from migrating out of the original tissues and invading surrounding tissues (By similarity). {ECO:0000250, ECO:0000269|PubMed:12061784}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Strongly expressed in placenta and colon. Moderately expressed in lung, stomach, small intestine and kidney. Very weakly expressed in cerebrum, cerebellum, heart and testis. {ECO:0000269|PubMed:12061784}. +Q8R3I9 B3GN8_MOUSE UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 8 (BGnT-8) (Beta-1,3-Gn-T8) (Beta-1,3-N-acetylglucosaminyltransferase 8) (Beta3Gn-T8) (EC 2.4.1.-) 389 43,370 Chain (1); Compositional bias (1); Glycosylation (2); Topological domain (2); Transmembrane (1) TRANSMEM 8 24 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 7 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 25 389 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Beta-1,3-N-acetylglucosaminyltransferase that plays a role in the elongation of specific branch structures of multiantennary N-glycans. Has strong activity towards tetraantennary N-glycans and 2,6 triantennary glycans (By similarity). {ECO:0000250|UniProtKB:Q7Z7M8}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9NY97}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9NY97}. SUBUNIT: Interacts with B3GNT2; this interaction greatly increases B3GNT2 catalytic activity, independently of B3GNT8 enzymatic activity. {ECO:0000269|PubMed:18826941}. +P15535 B4GT1_MOUSE Beta-1,4-galactosyltransferase 1 (Beta-1,4-GalTase 1) (Beta4Gal-T1) (b4Gal-T1) (EC 2.4.1.-) (Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase) (Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase) (EC 2.4.1.38) (Lactose synthase A protein) (EC 2.4.1.22) (N-acetyllactosamine synthase) (EC 2.4.1.90) (Nal synthase) (UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 1) (UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 1) [Cleaved into: Processed beta-1,4-galactosyltransferase 1] 399 44,411 Alternative sequence (1); Binding site (2); Chain (2); Disulfide bond (2); Glycosylation (1); Metal binding (2); Region (5); Topological domain (2); Transmembrane (1) TRANSMEM 25 44 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 24 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 45 399 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: The Golgi complex form catalyzes the production of lactose in the lactating mammary gland and could also be responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids.; FUNCTION: The cell surface form functions as a recognition molecule during a variety of cell to cell and cell to matrix interactions, as those occurring during development and egg fertilization, by binding to specific oligosaccharide ligands on opposing cells or in the extracellular matrix. PTM: The soluble form derives from the membrane forms by proteolytic processing. SUBCELLULAR LOCATION: Isoform Long: Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:18511602}; Single-pass type II membrane protein. Cell membrane; Single-pass type II membrane protein. Cell surface. Cell projection, filopodium {ECO:0000269|PubMed:18511602}. Note=Found in trans cisternae of Golgi. B4GALT1 cell surface expression is regulated by UBE2Q1 (PubMed:18511602). {ECO:0000269|PubMed:18511602}.; SUBCELLULAR LOCATION: Isoform Short: Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:3149531}; Single-pass type II membrane protein {ECO:0000269|PubMed:3149531}. Note=Found in trans cisternae of Golgi. {ECO:0000269|PubMed:3149531}.; SUBCELLULAR LOCATION: Processed beta-1,4-galactosyltransferase 1: Secreted {ECO:0000250|UniProtKB:P15291}. Note=Soluble form found in body fluids. {ECO:0000250|UniProtKB:P15291}. SUBUNIT: Homodimer; and heterodimer with alpha-lactalbumin to form lactose synthase (By similarity). Interacts (via N-terminal cytoplasmic domain) with UBE2Q1 (via N-terminus); the interaction is direct (PubMed:18511602). {ECO:0000250|UniProtKB:P15291, ECO:0000269|PubMed:18511602}. +Q9Z2Y2 B4GT2_MOUSE Beta-1,4-galactosyltransferase 2 (Beta-1,4-GalTase 2) (Beta4Gal-T2) (b4Gal-T2) (EC 2.4.1.-) (Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase) (Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase) (EC 2.4.1.38) (Lactose synthase A protein) (EC 2.4.1.22) (N-acetyllactosamine synthase) (EC 2.4.1.90) (Nal synthase) (UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 2) (UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 2) 369 41,909 Binding site (2); Chain (1); Disulfide bond (2); Glycosylation (3); Metal binding (2); Region (5); Topological domain (2); Transmembrane (1) TRANSMEM 16 36 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 15 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 37 369 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. Can produce lactose (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Trans cisternae of Golgi stack. {ECO:0000250}. +Q9JJ04 B4GT4_MOUSE Beta-1,4-galactosyltransferase 4 (Beta-1,4-GalTase 4) (Beta4Gal-T4) (b4Gal-T4) (EC 2.4.1.-) (Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase) (Lactotriaosylceramide beta-1,4-galactosyltransferase) (EC 2.4.1.275) (N-acetyllactosamine synthase) (EC 2.4.1.90) (Nal synthase) (UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 4) (UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 4) 344 39,700 Binding site (3); Chain (1); Disulfide bond (2); Frameshift (1); Glycosylation (2); Metal binding (2); Region (5); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 13 38 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 12 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 39 344 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Trans cisternae of Golgi stack. {ECO:0000250}. +Q9JL18 BACE2_MOUSE Beta-secretase 2 (EC 3.4.23.45) (Aspartyl protease 1) (ASP1) (Asp 1) (Beta-site amyloid precursor protein cleaving enzyme 2) (Beta-site APP cleaving enzyme 2) (Memapsin-1) (Membrane-associated aspartic protease 1) (Theta-secretase) 514 55,800 Active site (2); Chain (1); Disulfide bond (3); Domain (1); Glycosylation (2); Propeptide (1); Sequence conflict (9); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 470 490 Helical. {ECO:0000255}. TOPO_DOM 20 469 Extracellular. {ECO:0000255}.; TOPO_DOM 491 514 Cytoplasmic. {ECO:0000255}. FUNCTION: Responsible for the proteolytic processing of the amyloid precursor protein (APP). Cleaves APP, between residues 690 and 691, leading to the generation and extracellular release of beta-cleaved soluble APP, and a corresponding cell-associated C-terminal fragment which is later released by gamma-secretase. It has also been shown that it can cleave APP between residues 671 and 672 (By similarity). Responsible also for the proteolytic processing of CLTRN in pancreatic beta cells (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9Y5Z0}. PTM: Undergoes autoproteolytic cleavage. {ECO:0000250|UniProtKB:Q9Y5Z0}.; PTM: Glycosylated. {ECO:0000250|UniProtKB:Q9Y5Z0}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21907142}; Single-pass type I membrane protein {ECO:0000250}. Golgi apparatus {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Endosome {ECO:0000250}. Cell surface {ECO:0000250}. Note=Colocalized with CLTRN. {ECO:0000269|PubMed:21907142}. SUBUNIT: Monomer. Interacts ith RTN3 and RTN4. {ECO:0000250|UniProtKB:Q9Y5Z0}. TISSUE SPECIFICITY: High expression in pancreatic islets. Expressed at much lower levels in the pituitary, colon, and ovaries and is nearly absent from all the other tissues. {ECO:0000269|PubMed:21907142}. +Q8BGV7 BACD1_MOUSE BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 1 (BTB/POZ domain-containing protein KCTD13) (Polymerase delta-interacting protein 1) 329 36,442 Chain (1); Domain (1) Protein modification; protein ubiquitination. FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex required for synaptic transmission (PubMed:29088697). The BCR(KCTD13) E3 ubiquitin ligase complex mediates the ubiquitination of RHOA, leading to its degradation by the proteasome, thereby regulating the actin cytoskeleton and promoting synaptic transmission (PubMed:29088697). {ECO:0000269|PubMed:29088697}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8WZ19}. SUBUNIT: Homotetramer; forms a two-fold symmetric tetramer in solution. Interacts with CUL3; interaction is direct and forms a 5:5 heterodecamer. Component of the BCR(KCTD13) E3 ubiquitin ligase complex, at least composed of CUL3, KCTD13/BACURD1 and RBX1. Interacts with RHOA; with a preference for RhoA-GDP. Interacts with POLD2 and PCNA. Interacts with SPRTN. {ECO:0000250|UniProtKB:Q8WZ19}. +P56818 BACE1_MOUSE Beta-secretase 1 (EC 3.4.23.46) (Aspartyl protease 2) (ASP2) (Asp 2) (Beta-site amyloid precursor protein cleaving enzyme 1) (Beta-site APP cleaving enzyme 1) (Memapsin-2) (Membrane-associated aspartic protease 2) 501 55,748 Active site (2); Chain (1); Cross-link (1); Disulfide bond (3); Domain (1); Glycosylation (4); Lipidation (4); Modified residue (8); Motif (1); Mutagenesis (8); Propeptide (1); Region (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 458 478 Helical. {ECO:0000255}. TOPO_DOM 22 457 Extracellular. {ECO:0000255}.; TOPO_DOM 479 501 Cytoplasmic. {ECO:0000255}. FUNCTION: Responsible for the proteolytic processing of the amyloid precursor protein (APP). Cleaves at the N-terminus of the A-beta peptide sequence, between residues 671 and 672 of APP, leads to the generation and extracellular release of beta-cleaved soluble APP, and a corresponding cell-associated C-terminal fragment which is later released by gamma-secretase. Cleaves APP with much more catalytic efficiency than for the wild-type. {ECO:0000250|UniProtKB:P56817}. PTM: N-Glycosylated (By similarity). Addition of a bisecting N-acetylglucosamine by MGAT3 blocks lysosomal targeting, further degradation and is required for maintaining stability under stress conditions (PubMed:25592972, PubMed:26467158). {ECO:0000250, ECO:0000250|UniProtKB:P56817, ECO:0000269|PubMed:25592972, ECO:0000269|PubMed:26467158}.; PTM: Palmitoylation mediates lipid raft localization. {ECO:0000269|PubMed:19074428}.; PTM: Acetylated in the endoplasmic reticulum at Lys-126, Lys-275, Lys-279, Lys-285, Lys-299, Lys-300 and Lys-307. Acetylation by NAT8 and NAT8B is transient and deacetylation probably occurs in the Golgi. Acetylation regulates the maturation, the transport to the plasma membrane, the stability and the expression of the protein. {ECO:0000250|UniProtKB:P56817}.; PTM: Ubiquitinated at Lys-501, ubiquitination leads to lysosomal degradation. Monoubiquitinated and 'Lys-63'-linked polyubitinated. Deubiquitnated by USP8; inhibits lysosomal degradation. {ECO:0000250|UniProtKB:P56817}.; PTM: Phosphorylation at Ser-498 is required for interaction with GGA1 and retrograded transport from endosomal compartments to the trans-Golgi network. Non-phosphorylated BACE1 enters a direct recycling route to the cell surface. {ECO:0000250|UniProtKB:P56817}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:19074428}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P56817}. Endosome {ECO:0000269|PubMed:19074428}. Late endosome {ECO:0000269|PubMed:25592972}. Early endosome {ECO:0000269|PubMed:25592972}. Cell surface {ECO:0000269|PubMed:26467158}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P56817}. Membrane raft {ECO:0000269|PubMed:19074428}. Lysosome {ECO:0000269|PubMed:25592972}. Recycling endosome {ECO:0000269|PubMed:23931995}. Note=Predominantly localized to the later Golgi/trans-Golgi network (TGN) and minimally detectable in the early Golgi compartments. A small portion is also found in the endoplasmic reticulum, endosomes and on the cell surface (By similarity). Colocalization with APP in early endosomes is due to addition of bisecting N-acetylglucosamine wich blocks targeting to late endosomes and lysosomes (PubMed:25592972). Retrogradly transported from endosomal compartments to the trans-Golgi network in a phosphorylation- and GGA1- dependent manner (By similarity). {ECO:0000250|UniProtKB:P56817, ECO:0000269|PubMed:25592972}. SUBUNIT: Monomer. Interacts (via DXXLL motif) with GGA1, GGA2 and GGA3 (via their VHS domain); the interaction highly increases when BACE1 is phosphorylated at Ser-498. Interacts with RTN3 and RTN4. Interacts with SNX6. Interacts with PCSK9. Interacts with NAT8 and NAT8B. Interacts with BIN1 (By similarity). {ECO:0000250|UniProtKB:P56817}. DOMAIN: DXXLL motif is required for a proper endocytosis and retrograde transport to the trans-Golgi network, as well as for regulation of lysosomal degradation. {ECO:0000250|UniProtKB:P56817}.; DOMAIN: The transmembrane domain is necessary for its activity. It determines its late Golgi localization and access to its substrate, APP. {ECO:0000250|UniProtKB:P56817}. TISSUE SPECIFICITY: Brain. +Q8BVR0 BAFL_MOUSE Barrier-to-autointegration factor-like protein (BAF-L) (Barrier-to-autointegration factor 2) 90 10,267 Chain (1) FUNCTION: May play a role in BANF1 regulation and influence tissue-specific roles of BANF1. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm {ECO:0000250}. SUBUNIT: Homodimer. Heterodimerizes with BANF1 (By similarity). {ECO:0000250}. +Q8CI32 BAG5_MOUSE BAG family molecular chaperone regulator 5 (BAG-5) (Bcl-2-associated athanogene 5) 447 50,943 Chain (1); Domain (5); Erroneous initiation (1); Frameshift (1); Helix (4); Sequence conflict (7) FUNCTION: May function as a nucleotide exchange factor for HSP/HSP70, promoting ADP release, and activating Hsp70-mediated refolding. Inhibits both auto-ubiquitination of PRKN and ubiquitination of target proteins by PRKN (By similarity). {ECO:0000250}. SUBUNIT: Binds to the ATPase domain of HSP/HSC70 chaperones. Binds PRKN (By similarity). {ECO:0000250}. DOMAIN: The fifth BAG domain is responsible for the interaction with HSP70 nucleotide-binding domain. {ECO:0000250}. +Q9CXI0 COQ5_MOUSE 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial (EC 2.1.1.201) (Ubiquinone biosynthesis methyltransferase COQ5) 327 37,336 Binding site (2); Chain (1); Frameshift (1); Region (1); Sequence conflict (6); Transit peptide (1) Cofactor biosynthesis; ubiquinone biosynthesis. FUNCTION: Methyltransferase required for the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2). {ECO:0000255|HAMAP-Rule:MF_03191}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03191}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03191}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03191}. SUBUNIT: Component of a multi-subunit COQ enzyme complex, composed of at least COQ3, COQ4, COQ5, COQ6, COQ7 and COQ9. {ECO:0000255|HAMAP-Rule:MF_03191}. +Q8CDJ3 BAKOR_MOUSE Beclin 1-associated autophagy-related key regulator (Barkor) (Autophagy-related protein 14-like protein) (Atg14L) 492 55,388 Chain (1); Coiled coil (1); Modified residue (3); Region (1) FUNCTION: Required for both basal and inducible autophagy (PubMed:19270696, PubMed:19270693). Determines the localization of the autophagy-specific PI3-kinase complex PI3KC3-C1 (By similarity). Plays a role in autophagosome formation and MAP1LC3/LC3 conjugation to phosphatidylethanolamine (PubMed:19270696, PubMed:19270693). Promotes BECN1 translocation from the trans-Golgi network to autophagosomes (By similarity). Enhances PIK3C3 activity in a BECN1-dependent manner. Essential for the autophagy-dependent phosphorylation of BECN1 (By similarity). Stimulates the phosphorylation of BECN1, but suppresses the phosphorylation of PIK3C3 by AMPK (PubMed:23332761). Binds to STX17-SNAP29 binary t-SNARE complex on autophagosomes and primes it for VAMP8 interaction to promote autophagosome-endolysosome fusion (By similarity). Modulates the hepatic lipid metabolism (PubMed:22992773). {ECO:0000250|UniProtKB:Q6ZNE5, ECO:0000269|PubMed:19270693, ECO:0000269|PubMed:19270696, ECO:0000269|PubMed:22992773, ECO:0000269|PubMed:23332761}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20639694}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:20639694}; Peripheral membrane protein {ECO:0000305}. Preautophagosomal structure membrane {ECO:0000269|PubMed:19270693, ECO:0000269|PubMed:20639694, ECO:0000269|PubMed:22863730}; Peripheral membrane protein {ECO:0000305}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:Q6ZNE5}; Peripheral membrane protein {ECO:0000305}. Note=Cytosolic under nutrient-rich conditions (PubMed:20639694). Following autophagy stimuli, such as starvation or rapamycin induction, predominantly detected in cytoplasmic foci, identified as isolation membranes and autophagosomes (PubMed:20639694). Accumulates on highly curved PtdIns(3)P enriched autophagic membrane via its BATS domain to sense and maintain membrane curvature (PubMed:21518905). Localizes also to discrete punctae along the ciliary axoneme and to the base of the ciliary axoneme (PubMed:24089209). {ECO:0000269|PubMed:20639694, ECO:0000269|PubMed:21518905, ECO:0000269|PubMed:24089209}. SUBUNIT: Forms homooligomers; homo-oligomerization is essential for the roles in membrane tethering and enhancement of SNARE-mediated fusion (By similarity). Component of the PI3K (PI3KC3/PI3K-III/class III phosphatidylinositol 3-kinase) complex I (PI3KC3-C1) in which the core composed of the catalytic subunit PIK3C3, the regulatory subunit PIK3R4 and BECN1 is associated with ATG14 (PubMed:19270693, PubMed:22745922, PubMed:23332761). PI3KC3-C1 displays a V-shaped architecture with PIK3R4 serving as a bridge between PIK3C3 and the ATG14:BECN1 subcomplex (By similarity). PI3KC3-C1 can associate with further regulatory subunits (PubMed:24849286). Interacts with PIK3CB (PubMed:21059846). Interacts (via coiled-coil domain) with BECN2 (via coiled-coil domain); this interaction is tighter than BECN2 self-association (By similarity). Interacts with the STX17-SNAP29 binary t-SNARE complex (By similarity). Interacts with NRBF2 (PubMed:24849286). {ECO:0000250|UniProtKB:Q6ZNE5, ECO:0000269|PubMed:19270693, ECO:0000269|PubMed:21059846, ECO:0000269|PubMed:22745922, ECO:0000269|PubMed:23332761, ECO:0000269|PubMed:24849286}. DOMAIN: The coiled-coil domain is required for BECN1- and PIK3C3-binding and for autophagy. {ECO:0000250|UniProtKB:Q6ZNE5}.; DOMAIN: The final 80 residues in the C-terminus define a minimum required region for autophagosome binding called BATS. {ECO:0000269|PubMed:21518905}.; DOMAIN: The N-terminal cysteine repeats are required for proper localization to the endoplasmic reticulum. {ECO:0000250|UniProtKB:Q6ZNE5}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:18843052}. +Q8VBU8 BANP_MOUSE Protein BANP (Btg3-associated nuclear protein) (Scaffold/matrix-associated region-1-binding protein) 548 59,657 Alternative sequence (3); Chain (1); Coiled coil (1); Compositional bias (2); Cross-link (1); Domain (1); Modified residue (5); Mutagenesis (4); Region (3); Sequence conflict (2) FUNCTION: Controls V(D)J recombination during T-cell development by repressing T-cell receptor (TCR) beta enhancer function. Binds to scaffold/matrix attachment region beta (S/MARbeta), an ATC-rich DNA sequence located upstream of the TCR beta enhancer. Represses cyclin D1 transcription by recruiting HDAC1 to its promoter, thereby diminishing H3K9ac, H3S10ph and H4K8ac levels. Promotes TP53 'Ser-15' phosphorylation and nuclear accumulation, which causes cell cycle arrest and inhibits tumor growth. {ECO:0000269|PubMed:10950932, ECO:0000269|PubMed:12494467, ECO:0000269|PubMed:15371550, ECO:0000269|PubMed:15623522, ECO:0000269|PubMed:15701641, ECO:0000269|PubMed:16166625, ECO:0000269|PubMed:17229733}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10940556, ECO:0000269|PubMed:12494467, ECO:0000269|PubMed:15371550, ECO:0000269|PubMed:15701641, ECO:0000269|PubMed:16166625}. SUBUNIT: Interacts with TP53, CUX1/CDP and HDAC1. Part of a corepressor complex containing BANP, HDAC1, SIN3A, SIN3B, RBL1 and RBL2. {ECO:0000269|PubMed:12494467, ECO:0000269|PubMed:15371550, ECO:0000269|PubMed:15701641, ECO:0000269|PubMed:16166625}. TISSUE SPECIFICITY: Highly expressed in heart, spleen, and thymus. Isoform 1 is highly expressed in kidney, brain and testis. Isoform 3 is highly expressed in kidney and lung. {ECO:0000269|PubMed:10940556, ECO:0000269|PubMed:10950932, ECO:0000269|PubMed:12494467}. +Q80VH0 BANK1_MOUSE B-cell scaffold protein with ankyrin repeats (Protein AVIEF) 783 89,406 Chain (1); Domain (1); Erroneous initiation (1); Erroneous termination (1); Frameshift (1); Modified residue (1); Region (1); Repeat (2); Sequence conflict (8) FUNCTION: Involved in B-cell receptor (BCR)-induced Ca(2+) mobilization from intracellular stores. Promotes Lyn-mediated phosphorylation of IP3 receptors 1 and 2 (By similarity). {ECO:0000250}. PTM: Phosphorylated on tyrosines upon BCR activation. {ECO:0000250}. SUBUNIT: Interacts with LYN, ITPR1 and ITPR2. {ECO:0000250}. TISSUE SPECIFICITY: Specifically expressed in spleen. Highly expressed in immature B-cells and recirculating B-cells, and at low levels in pro-B and pre-B cells. {ECO:0000269|PubMed:11782428}. +P63157 BARH1_MOUSE BarH-like 1 homeobox protein (Bar-class homeodomain protein MBH2) (BarH-related homeobox protein 1) 327 35,136 Chain (1); DNA binding (1) SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q8VIB5 BARH2_MOUSE BarH-like 2 homeobox protein (Bar-class homeodomain protein MBH1) (Homeobox protein B-H1) 384 41,459 Chain (1); Compositional bias (4); DNA binding (1) FUNCTION: Potential regulator of neural basic helix-loop-helix genes. It may down-regulate expression of ASCL1 and, within the thalamus, up-regulate NGN2, thereby regulating distinct patterns of neuronal differentiation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. +O89053 COR1A_MOUSE Coronin-1A (Coronin-like protein A) (Clipin-A) (Coronin-like protein p57) (Tryptophan aspartate-containing coat protein) (TACO) 461 50,989 Beta strand (31); Chain (1); Coiled coil (1); Helix (5); Initiator methionine (1); Modified residue (5); Repeat (7); Sequence conflict (3); Turn (6) FUNCTION: May be a crucial component of the cytoskeleton of highly motile cells, functioning both in the invagination of large pieces of plasma membrane, as well as in forming protrusions of the plasma membrane involved in cell locomotion. In mycobacteria-infected cells, its retention on the phagosomal membrane prevents fusion between phagosomes and lysosomes. {ECO:0000269|PubMed:10338208}. PTM: phosphorylation at Ser-412 by PKC strongly down-regulates the association with actin. {ECO:0000250}.; PTM: Polyubiquitinated by RNF128 with 'Lys-48'-linked chains, leading to proteasomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10338208}. Cytoplasm, cell cortex {ECO:0000269|PubMed:10338208}. Cytoplasmic vesicle, phagosome membrane {ECO:0000269|PubMed:10338208}. Note=In non-infected macrophages, associated with the cortical microtubule network. In mycobacteria-infected macrophages, becomes progressively relocalized and retained around the mycobacterial phagosomes. Retention on the phagosomal membrane is strictly dependent on mycobacterial viability and not due to impaired acidification. SUBUNIT: Binds actin. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in spleen, lymph nodes, thymus, brain and at very lower levels in lung. Also expressed in cells of the lymphoid/myeloid lineage. Not expressed in Kuffper cells. {ECO:0000269|PubMed:10338208}. +Q9WUM3 COR1B_MOUSE Coronin-1B (Coronin-2) 484 53,912 Chain (1); Coiled coil (1); Modified residue (1); Repeat (5); Sequence conflict (1) FUNCTION: Regulates leading edge dynamics and cell motility in fibroblasts. May be involved in cytokinesis and signal transduction (By similarity). {ECO:0000250}. PTM: Phosphorylation on Ser-2 regulates the interaction with the Arp2/3 complex and cell motility in fibroblasts. Phosphorylation does not seem to affect subcellular location (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9BR76}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:Q9BR76}. Note=Localized to the leading edge in fibroblasts, as well as weakly along actin stress fibers. {ECO:0000250|UniProtKB:Q9BR76}. SUBUNIT: Forms homooligomers, but does not form complexes with the other coronins. Interacts with Arp2/3 complex components, including ACTR2, ARPC1B and ARPC2. Binds actin (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:16027158}. +Q8BH44 COR2B_MOUSE Coronin-2B 480 54,936 Chain (1); Coiled coil (1); Erroneous initiation (3); Repeat (5); Sequence conflict (1) FUNCTION: May play a role in the reorganization of neuronal actin structure. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. SUBUNIT: Binds to F-actin and to vinculin. {ECO:0000250}. +Q9QXA6 BAT1_MOUSE b(0,+)-type amino acid transporter 1 (b(0,+)AT1) (Glycoprotein-associated amino acid transporter b0,+AT1) (Solute carrier family 7 member 9) 487 53,747 Chain (1); Modified residue (1); Topological domain (13); Transmembrane (12) TRANSMEM 30 50 Helical. {ECO:0000255}.; TRANSMEM 64 84 Helical. {ECO:0000255}.; TRANSMEM 100 120 Helical. {ECO:0000255}.; TRANSMEM 124 144 Helical. {ECO:0000255}.; TRANSMEM 148 168 Helical. {ECO:0000255}.; TRANSMEM 179 199 Helical. {ECO:0000255}.; TRANSMEM 255 275 Helical. {ECO:0000255}.; TRANSMEM 297 317 Helical. {ECO:0000255}.; TRANSMEM 349 369 Helical. {ECO:0000255}.; TRANSMEM 375 395 Helical. {ECO:0000255}.; TRANSMEM 410 430 Helical. {ECO:0000255}.; TRANSMEM 435 455 Helical. {ECO:0000255}. TOPO_DOM 1 29 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 51 63 Extracellular. {ECO:0000255}.; TOPO_DOM 85 99 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 121 123 Extracellular. {ECO:0000255}.; TOPO_DOM 145 147 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 169 178 Extracellular. {ECO:0000255}.; TOPO_DOM 200 254 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 276 296 Extracellular. {ECO:0000255}.; TOPO_DOM 318 348 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 370 374 Extracellular. {ECO:0000255}.; TOPO_DOM 396 409 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 431 434 Extracellular. {ECO:0000255}.; TOPO_DOM 456 487 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in the high-affinity, sodium-independent transport of cystine and neutral and dibasic amino acids (system B(0,+)-like activity). Thought to be responsible for the high-affinity reabsorption of cystine in the kidney proximal tubule. {ECO:0000269|PubMed:10588648}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000305|PubMed:12167606}; Multi-pass membrane protein {ECO:0000305|PubMed:12167606}. SUBUNIT: Disulfide-linked heterodimer with the amino acid transport protein SLC3A1. Interacts with CAV1. {ECO:0000250|UniProtKB:P82252}. TISSUE SPECIFICITY: Expressed in the brush border membrane in the kidney (at protein level). {ECO:0000269|PubMed:12167606}. +Q9Z277 BAZ1B_MOUSE Tyrosine-protein kinase BAZ1B (EC 2.7.10.2) (Bromodomain adjacent to zinc finger domain protein 1B) (Williams syndrome transcription factor homolog) (Williams-Beuren syndrome chromosomal region 9 protein homolog) 1479 170,651 Alternative sequence (1); Chain (1); Coiled coil (4); Compositional bias (1); Cross-link (6); Domain (3); Modified residue (18); Motif (1); Sequence conflict (3); Zinc finger (1) FUNCTION: Atypical tyrosine-protein kinase that plays a central role in chromatin remodeling and acts as a transcription regulator. Involved in DNA damage response by phosphorylating 'Tyr-142' of histone H2AX (H2AXY142ph). H2AXY142ph plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress. Essential component of the WICH complex, a chromatin remodeling complex that mobilizes nucleosomes and reconfigures irregular chromatin to a regular nucleosomal array structure. The WICH complex regulates the transcription of various genes, has a role in RNA polymerase I and RNA polymerase III transcription, mediates the histone H2AX phosphorylation at 'Tyr-142', and is involved in the maintenance of chromatin structures during DNA replication processes. In the complex, it mediates the recruitment of the WICH complex to replication foci during DNA replication. {ECO:0000250, ECO:0000269|PubMed:16514417}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00063, ECO:0000255|PROSITE-ProRule:PRU00475}. Note=Accumulates in pericentromeric heterochromatin during replication. Targeted to replication foci throughout S phase via its association with PCNA (By similarity). {ECO:0000250}. SUBUNIT: Interacts with MYO1C (PubMed:16514417). Interacts with CDT1 (By similarity). Interacts with SMARCA5/SNF2H; the interaction is direct and forms the WICH complex (By similarity). Component of the B-WICH complex, at least composed of SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21 (By similarity). Interacts with PCNA; the interaction is direct (By similarity). {ECO:0000250|UniProtKB:Q9UIG0, ECO:0000269|PubMed:16514417}. +Q8R1H8 BATF2_MOUSE Basic leucine zipper transcriptional factor ATF-like 2 (B-ATF-2) 277 29,703 Alternative sequence (1); Chain (1); Domain (1); Region (2) FUNCTION: AP-1 family transcription factor that controls the differentiation of lineage-specific cells in the immune system. Selectively suppresses CYR61/CCN1 transcription and hence blocks the downstream cell proliferation signals produced by CYR61 and inhibits CYR61-induced anchorage-independent growth and invasion in several cancer types. Possibly acts by interfering with AP-1 binding to CYR61 promoter (By similarity). Following infection, participates in the differentiation of CD8(+) thymic conventional dendritic cells in the immune system. Acts via the formation of a heterodimer with JUN family proteins that recognizes and binds DNA sequence 5'-TGA[CG]TCA-3' and regulates expression of target genes. {ECO:0000250, ECO:0000269|PubMed:22992524}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}. SUBUNIT: Heterodimer; heterodimerizes with JUN family proteins. {ECO:0000250}. +Q9D275 BATF3_MOUSE Basic leucine zipper transcriptional factor ATF-like 3 (B-ATF-3) 118 13,657 Chain (1); Domain (1); Modified residue (2); Region (2) FUNCTION: AP-1 family transcription factor that controls the differentiation of CD8(+) thymic conventional dendritic cells in the immune system. Acts via the formation of a heterodimer with JUN family proteins that recognizes and binds DNA sequence 5'-TGA[CG]TCA-3' and regulates expression of target genes. Required for development of CD8-alpha(+) classical dendritic cells (cDCs) and related CD103(+) dendritic cells that cross-present antigens to CD8 T-cells and produce interleukin-12 (IL12) in response to pathogens. {ECO:0000269|PubMed:19008445, ECO:0000269|PubMed:20351058, ECO:0000269|PubMed:21867928}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}. SUBUNIT: Heterodimer; heterodimerizes with JUN family proteins. Interacts with JUN. TISSUE SPECIFICITY: Highly expressed in CD8-alpha(+) classical dendritic cells (cDCs), with low to absent expression in other immune cells and non-immune tissues. {ECO:0000269|PubMed:19008445}. +Q920M5 CORO6_MOUSE Coronin-6 (Coronin-like protein E) (Clipin-E) 471 52,599 Alternative sequence (3); Chain (1); Coiled coil (1); Repeat (5) +Q9R069 BCAM_MOUSE Basal cell adhesion molecule (B-CAM cell surface glycoprotein) (Lutheran antigen) (CD antigen CD239) 622 67,670 Chain (1); Disulfide bond (5); Domain (5); Glycosylation (4); Modified residue (4); Sequence conflict (5); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 542 562 Helical. {ECO:0000255}. TOPO_DOM 26 541 Extracellular. {ECO:0000255}.; TOPO_DOM 563 622 Cytoplasmic. {ECO:0000255}. FUNCTION: Laminin alpha-5 receptor. May mediate intracellular signaling (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. +Q9QZK2 BCAR3_MOUSE Breast cancer anti-estrogen resistance protein 3 (p130Cas-binding protein AND-34) 820 92,263 Alternative sequence (1); Chain (1); Domain (2); Initiator methionine (1); Modified residue (12); Sequence conflict (3) FUNCTION: May act as an adapter protein and couple activated growth factor receptors to signaling molecules that regulate src kinase activity and promote cell migration. {ECO:0000269|PubMed:10896938, ECO:0000269|PubMed:12517963}. PTM: Phosphorylated on tyrosine. {ECO:0000269|PubMed:10438950}. SUBUNIT: Interacts with BCAR1, NEDD9, PTK2/FAK1 and PTPN1. {ECO:0000269|PubMed:10438950, ECO:0000269|PubMed:10896938, ECO:0000269|PubMed:12517963}. TISSUE SPECIFICITY: Expressed in B-cells. {ECO:0000269|PubMed:10438950, ECO:0000269|PubMed:12517963}. +Q9CWI3 BCCIP_MOUSE BRCA2 and CDKN1A-interacting protein 316 35,942 Chain (1); Modified residue (3); Region (2); Sequence conflict (2) FUNCTION: During interphase, required for microtubule organizing and anchoring activities. During mitosis, required for the organization and stabilization of the spindle pole (PubMed:28394342). May promote cell cycle arrest by enhancing the inhibition of CDK2 activity by CDKN1A. May be required for repair of DNA damage by homologous recombination in conjunction with BRCA2. May not be involved in non-homologous end joining (NHEJ) (By similarity). {ECO:0000250|UniProtKB:Q9P287, ECO:0000269|PubMed:28394342}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9P287}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:28394342}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:28394342}. Note=Colocalizes with BRCA2 in discrete nuclear foci (By similarity). In interphase, preferential localizes to the mother centriole (PubMed:28394342). Recruited to the spindle pole matrix and centrosome by microtubules and dynein/dynactin activity (By similarity). {ECO:0000250|UniProtKB:Q9P287, ECO:0000269|PubMed:28394342}. SUBUNIT: Interacts with BRCA2, CDKN1A and MTDH/LYRIC. Interacts with DCTN1/p150-glued and ACTR1A/ARP1. Interacts with alpha-, beta- and gamma-tubulins. Interacts with TENT5C; the interaction has no effect on TENT5C poly(A) polymerase function (By similarity). {ECO:0000250|UniProtKB:Q9P287}. +Q2UY11 COSA1_MOUSE Collagen alpha-1(XXVIII) chain 1141 118,749 Alternative sequence (2); Chain (1); Disulfide bond (3); Domain (8); Signal peptide (1) FUNCTION: May act as a cell-binding protein. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000269|PubMed:16330543}. SUBUNIT: Trimer or homomer. Secreted into as a 135 kDa monomer under reducing conditions and as a homotrimer under non-reducing conditions. {ECO:0000269|PubMed:16330543}. TISSUE SPECIFICITY: Expressed in skin, intestine, sternum, brain and kidney. Lower expression is also observed in heart, lung, sciatic nerve, dorsal root ganglia, peripheral nerves and calvaria of newborn mice and in intestine and brain of adult mice. Found in basement membrane surrounding a particular subset of Schwann cells in adult sciatic nerve. {ECO:0000269|PubMed:16330543}. +P24288 BCAT1_MOUSE Branched-chain-amino-acid aminotransferase, cytosolic (BCAT(c)) (EC 2.6.1.42) (Protein ECA39) 386 42,791 Chain (1); Frameshift (1); Modified residue (2); Sequence conflict (2) FUNCTION: Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain and kidney. Overexpressed in MYC-induced brain tumors, lymphomas, as well as in a teratocarcinoma cell line. +Q60632 COT1_MOUSE COUP transcription factor 1 (COUP-TF1) (COUP transcription factor I) (COUP-TF I) (Nuclear receptor subfamily 2 group F member 1) (V-erbA-related protein 3) (EAR-3) 422 46,085 Chain (1); Compositional bias (1); DNA binding (1); Domain (1); Region (1); Sequence conflict (2); Zinc finger (2) FUNCTION: Coup (chicken ovalbumin upstream promoter) transcription factor binds to the ovalbumin promoter and, in conjunction with another protein (S300-II) stimulates initiation of transcription. Binds to both direct repeats and palindromes of the 5'-AGGTCA-3' motif. Represses transcriptional activity of LHCG (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Binds DNA as dimer; homodimer and probable heterodimer with NR2F6. Interacts with GTF2B; this interaction is direct. Interacts with COPS2. {ECO:0000250|UniProtKB:P10589}. +Q3UFB2 BCD1_MOUSE Box C/D snoRNA protein 1 (Zinc finger HIT domain-containing protein 6) 460 52,213 Alternative sequence (1); Chain (1); Compositional bias (1); Cross-link (10); Modified residue (1); Sequence conflict (1); Zinc finger (1) FUNCTION: Required for box C/D snoRNAs accumulation involved in snoRNA processing, snoRNA transport to the nucleolus and ribosome biogenesis. {ECO:0000250}. SUBUNIT: Interacts with FBL, SNU13, NOP58, NUFIP1, RUVBL1, RUVBL2 and TAF9. {ECO:0000250}. +Q99NF1 BCDO2_MOUSE Beta,beta-carotene 9',10'-oxygenase (EC 1.13.11.71) (B-diox-II) (Beta-carotene dioxygenase 2) 532 60,142 Chain (1); Metal binding (4) FUNCTION: Asymmetrically cleaves beta-carotene at the 9',10' double bond resulting in the formation of beta-apo-10'-carotenal and beta-ionone. Besides beta-carotene, lycopene is also oxidatively cleaved. The apocarotenals formed by this enzyme may be the precursors for the biosynthesis of retinoic acid or exert unknown physiological effects. {ECO:0000269|PubMed:21106934}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:21106934}. +Q8K2G4 BBS7_MOUSE Bardet-Biedl syndrome 7 protein homolog (BBS2-like protein 1) 715 80,320 Alternative sequence (3); Chain (1); Modified residue (1) FUNCTION: The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor, which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane and binds to RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the Rab8-GTP localizes to the cilium and promotes docking and fusion of carrier vesicles to the base of the ciliary membrane. The BBSome complex, together with the LTZL1, controls SMO ciliary trafficking and contributes to the sonic hedgehog (SHH) pathway regulation. Required for BBSome complex ciliary localization but not for the proper complex assembly (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell projection, cilium membrane {ECO:0000250|UniProtKB:Q8IWZ6}. Cytoplasm {ECO:0000250|UniProtKB:Q8IWZ6}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000250|UniProtKB:Q8IWZ6}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:23807208}. SUBUNIT: Part of BBSome complex, that contains BBS1, BBS2, BBS4, BBS5, BBS7, BBS8/TTC8, BBS9 and BBIP10. Interacts with BBS2 (via C-terminus). Interacts with CCDC28B. Interacts with SMO; the interaction is indicative for the association of SMO with the BBsome complex to facilitate ciliary localization of SMO. {ECO:0000269|PubMed:22072986}. +Q8K019 BCLF1_MOUSE Bcl-2-associated transcription factor 1 (Btf) 919 106,002 Alternative sequence (3); Chain (1); Compositional bias (2); Cross-link (25); Modified residue (51); Sequence conflict (2) FUNCTION: Death-promoting transcriptional repressor. May be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA (By similarity). {ECO:0000250}. PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Nucleus speckle {ECO:0000250|UniProtKB:Q9NYF8}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9NYF8}. SUBUNIT: Interacts with Bcl-2 related proteins, EMD, with the adenovirus E1B 19 kDa protein and with DNA. Component of the SNARP complex which consists at least of SNIP1, SNW1, THRAP3, BCLAF1 and PNN (By similarity). Component of a MACOM-like complex, named WTAP complex, composed of WTAP, ZC3H13, CBLL1, KIAA1429, RBM15, BCLAF1 and THRAP3 (By similarity). {ECO:0000250|UniProtKB:Q9NYF8}. +Q8VBW5 BBX_MOUSE HMG box transcription factor BBX (Bobby sox homolog) (HMG box-containing protein 2) 907 100,783 Alternative sequence (6); Beta strand (1); Chain (1); Compositional bias (3); Cross-link (3); DNA binding (1); Erroneous initiation (1); Helix (3); Modified residue (6); Natural variant (2); Sequence caution (1); Sequence conflict (6) FUNCTION: Transcription factor that is necessary for cell cycle progression from G1 to S phase. {ECO:0000269|PubMed:11680820}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q9QYE3 BC11A_MOUSE B-cell lymphoma/leukemia 11A (BCL-11A) (B-cell CLL/lymphoma 11A) (COUP-TF-interacting protein 1) (Ecotropic viral integration site 9 protein) (EVI-9) 773 83,855 Alternative sequence (9); Chain (1); Compositional bias (2); Cross-link (4); Erroneous initiation (1); Frameshift (1); Modified residue (13); Mutagenesis (2); Region (1); Sequence conflict (7); Zinc finger (3) FUNCTION: Functions as a myeloid and B-cell proto-oncogene. May play important roles in leukemogenesis and hematopoiesis. An essential factor in lymphopoiesis, is required for B-cell formation in fetal liver. May function as a modulator of the transcriptional repression activity of ARP1. {ECO:0000269|PubMed:12717432}. PTM: Sumoylated with SUMO1. {ECO:0000269|PubMed:18681895}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18681895}. Nucleus {ECO:0000269|PubMed:18681895}. Note=Associates with the nuclear body. Colocalizes with SUMO1 and SENP2 in nuclear speckles. SUBUNIT: Interacts with TFCOUP1, PIAS3, ARP1 and EAR2. {ECO:0000269|PubMed:10744719, ECO:0000269|PubMed:18681895}. DOMAIN: The N-terminus is involved in protein dimerization and in transactivation of transcription. {ECO:0000250|UniProtKB:Q9H165}. TISSUE SPECIFICITY: Isoforms are expressed in a tissue-specific fashion. Isoforms 1, isoform 2, and isoform 3 are expressed at similar levels in testis, kidney and spleen. Isoform 1 is expressed in the stomach, and isoform 2 is expressed exclusively in the lung. Overexpression following proviral integration in hematopoietic cells results in the generation of myeloid leukemia. +P10417 BCL2_MOUSE Apoptosis regulator Bcl-2 236 26,407 Alternative sequence (1); Chain (1); Modified residue (3); Motif (4); Mutagenesis (1); Sequence conflict (4); Site (1); Transmembrane (1) TRANSMEM 209 230 Helical. {ECO:0000255}. FUNCTION: Suppresses apoptosis in a variety of cell systems including factor-dependent lymphohematopoietic and neural cells. Regulates cell death by controlling the mitochondrial membrane permeability. Appears to function in a feedback loop system with caspases. Inhibits caspase activity either by preventing the release of cytochrome c from the mitochondria and/or by binding to the apoptosis-activating factor (APAF-1). May attenuate inflammation by impairing NLRP1-inflammasome activation, hence CASP1 activation and IL1B release (PubMed:17418785). {ECO:0000269|PubMed:17418785}. PTM: Phosphorylation/dephosphorylation on Ser-70 regulates anti-apoptotic activity. Growth factor-stimulated phosphorylation on Ser-70 by PKC is required for the anti-apoptosis activity and occurs during the G2/M phase of the cell cycle. In the absence of growth factors, BCL2 appears to be phosphorylated by other protein kinases such as ERKs and stress-activated kinases. Phosphorylated by MAPK8/JNK1 at Thr-69, Ser-70 and Ser-84, wich stimulates starvation-induced autophagy (By similarity). Dephosphorylated by protein phosphatase 2A (PP2A). {ECO:0000250, ECO:0000269|PubMed:9115213}.; PTM: Proteolytically cleaved by caspases during apoptosis. The cleaved protein, lacking the BH4 motif, has pro-apoptotic activity, causes the release of cytochrome c into the cytosol promoting further caspase activity.; PTM: Monoubiquitinated by PRKN, leading to increase its stability. Ubiquitinated by SCF(FBXO10), leading to its degradation by the proteasome. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass membrane protein. Nucleus membrane; Single-pass membrane protein. Endoplasmic reticulum membrane; Single-pass membrane protein. SUBUNIT: Forms homodimers, and heterodimers with BAX, BAD, BAK and Bcl-X(L). Heterodimerization with BAX requires intact BH1 and BH2 motifs, and is necessary for anti-apoptotic activity (By similarity). Also interacts with APAF1, BBC3, BCL2L1, BNIPL, MRPL41 and TP53BP2. Binding to FKBP8 seems to target BCL2 to the mitochondria and probably interferes with the binding of BCL2 to its targets. Interacts with BAG1 in an ATP-dependent manner. Interacts with RAF1 (the 'Ser-338' and 'Ser-339' phosphorylated form). Interacts (via the BH4 domain) with EGLN3; the interaction prevents the formation of the BAX-BCL2 complex and inhibits the anti-apoptotic activity of BCL2 (By similarity). Interacts with EI24. Interacts with G0S2; this interaction also prevents the formation of the anti-apoptotic BAX-BCL2 complex. Interacts with PPIF; the interaction is impaired by CsA (By similarity). Interacts with BOP (By similarity). Interacts with the SCF(FBXO10) complex (By similarity). Interacts (via the loop between motifs BH4 and BH3) with NLRP1 (via LRR repeats) (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P10415}. DOMAIN: The BH4 motif is required for anti-apoptotic activity and for interaction with RAF1 and EGLN3.; DOMAIN: BH1 and BH2 domains are required for the interaction with BAX and for anti-apoptotic activity. {ECO:0000250|UniProtKB:P10415}.; DOMAIN: The loop between motifs BH4 and BH3 is required for the interaction with NLRP1. {ECO:0000250|UniProtKB:P10415}. TISSUE SPECIFICITY: Expressed in a variety of tissues. +Q8JZV9 BDH2_MOUSE 3-hydroxybutyrate dehydrogenase type 2 (EC 1.1.1.-) (EC 1.1.1.30) (Dehydrogenase/reductase SDR family member 6) (R-beta-hydroxybutyrate dehydrogenase) 245 26,753 Active site (1); Binding site (6); Chain (1); Mutagenesis (1); Nucleotide binding (2) Siderophore biosynthesis. FUNCTION: Dehydrogenase that mediates the formation of 2,5-dihydroxybenzoic acid (2,5-DHBA), a siderophore that shares structural similarities with bacterial enterobactin and associates with LCN2, thereby playing a key role in iron assimilation and homeostasis (PubMed:20550936, PubMed:24863067). Plays a role in susceptibility to bacterial infection by providing an assimilable source of iron that is exploited by pathogenic bacteria (PubMed:24863067). Also acts as a 3-hydroxybutyrate dehydrogenase (By similarity). {ECO:0000250|UniProtKB:Q9BUT1, ECO:0000269|PubMed:20550936, ECO:0000269|PubMed:24863067}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BUT1}. SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q9BUT1}. TISSUE SPECIFICITY: Detected in liver, spleen and macrophages (PubMed:24863067). Widely expressed. {ECO:0000269|PubMed:20550936, ECO:0000269|PubMed:24863067}. +Q571C7 BDP1_MOUSE Transcription factor TFIIIB component B'' homolog (Transcription factor IIIB 150) (TFIIIB150) (Transcription factor-like nuclear regulator) 2467 270,790 Alternative sequence (1); Chain (1); Coiled coil (2); Compositional bias (1); Domain (1); Region (2); Sequence caution (1); Sequence conflict (1) FUNCTION: General activator of RNA polymerase III transcription. Requires for transcription from all three types of polymerase III promoters. Requires for transcription of genes with internal promoter elements and with promoter elements upstream of the initiation site (By similarity). {ECO:0000250}. PTM: Phosphorylated by CSNK2A1 during mitosis, resulting in its release from chromatin and suppression of polymerase III transcription. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of TFIIIB complex. The TFIIIB complex has two activities, alpha and beta. The TFIIIB-alpha and TFIIIB-beta activities are required for transcription of genes with TFIIIC-bound internal promoters and PSE transcription factor-bound external promoters, respectively. The TFIIIB-alpha activity complex is composed of TBP, BDP1, and a complex containing both BRF2 and at least four stably associated proteins; YY1 facilitates the formation of TFIIIB-alpha activity complex. The TFIIIB-beta activity complex is composed of TBP, BDP1, and BRF1. Interacts with BRF1; this interaction diminishes during mitosis resulting in the release of BDP1 from chromosomal templates. Component of TFIIIC complex. The TFIIIC complex has two activities, C1 and C2. The TFIIIC2 activity complex is only required for transcription of the 'classical' pol III genes whereas the TFIIIC1 activity complex is required for transcription of all pol III genes. The TFIIIC1 activity complex is composed at least of BDP1. Interacts with ZBTB43 (By similarity). {ECO:0000250}. +P19783 COX41_MOUSE Cytochrome c oxidase subunit 4 isoform 1, mitochondrial (Cytochrome c oxidase polypeptide IV) (Cytochrome c oxidase subunit IV isoform 1) (COX IV-1) 169 19,530 Chain (1); Modified residue (7); Sequence conflict (2); Transit peptide (1) FUNCTION: This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. SUBCELLULAR LOCATION: Mitochondrion inner membrane. +P86174 BEND4_MOUSE BEN domain-containing protein 4 541 58,721 Chain (1); Coiled coil (1); Compositional bias (1); Domain (1) +Q8C6D4 BEND5_MOUSE BEN domain-containing protein 5 421 48,227 Alternative sequence (1); Chain (1); Coiled coil (1); Cross-link (1); Domain (1); Modified residue (1) FUNCTION: Acts as a transcriptional repressor. {ECO:0000250|UniProtKB:Q7L4P6}. DOMAIN: The BEN domain mediates DNA-binding. {ECO:0000250|UniProtKB:Q7L4P6}. +O88870 BEST1_MOUSE Bestrophin-1 (Vitelliform macular dystrophy protein 2 homolog) 551 63,684 Chain (1); Intramembrane (1); Sequence conflict (2); Topological domain (6); Transmembrane (4) INTRAMEM 229 249 {ECO:0000255}. TRANSMEM 26 46 Helical. {ECO:0000255}.; TRANSMEM 71 91 Helical. {ECO:0000255}.; TRANSMEM 179 199 Helical. {ECO:0000255}.; TRANSMEM 271 291 Helical. {ECO:0000255}. TOPO_DOM 1 25 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 47 70 Extracellular. {ECO:0000255}.; TOPO_DOM 92 178 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 200 228 Extracellular. {ECO:0000255}.; TOPO_DOM 250 270 Extracellular. {ECO:0000255}.; TOPO_DOM 292 551 Cytoplasmic. {ECO:0000255}. FUNCTION: Forms calcium-sensitive chloride channels. Permeable to bicarbonate (By similarity). {ECO:0000250}. PTM: Phosphorylated by PP2A. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Basolateral cell membrane {ECO:0000250}. SUBUNIT: Tetramer or pentamers. May interact with PPP2CB and PPP2R1B (By similarity). {ECO:0000250}. +O35153 BET1L_MOUSE BET1-like protein (Golgi SNARE with a size of 15 kDa) (GOS-15) (GS15) (Vesicle transport protein GOS15) 111 12,428 Chain (1); Domain (1); Modified residue (2); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 87 107 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 1 86 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 108 111 Lumenal. {ECO:0000255}. FUNCTION: Vesicle SNARE required for targeting and fusion of retrograde transport vesicles with the Golgi complex. Required for the integrity of the Golgi complex (By similarity). {ECO:0000250|UniProtKB:O35152}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250}. Note=Present throughout the Golgi apparatus, with increasing concentration from cis-Golgi to the trans-Golgi face of the stacks. {ECO:0000250}. SUBUNIT: Component of a SNARE complex consisting of STX5, YKT6, GOSR2 and BET1L. {ECO:0000250}. +Q9CPQ1 COX6C_MOUSE Cytochrome c oxidase subunit 6C (Cytochrome c oxidase polypeptide VIc) 76 8,469 Chain (1); Topological domain (2); Transmembrane (1) TRANSMEM 15 55 Helical. {ECO:0000250}. TOPO_DOM 4 14 Mitochondrial matrix. {ECO:0000250}.; TOPO_DOM 56 76 Mitochondrial intermembrane. {ECO:0000250}. FUNCTION: This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. {ECO:0000250}. PTM: Acetylation of Lys-61 is observed in liver mitochondria from fasted mice but not from fed mice. SUBCELLULAR LOCATION: Mitochondrion inner membrane. +P56393 COX7B_MOUSE Cytochrome c oxidase subunit 7B, mitochondrial (Cytochrome c oxidase polypeptide VIIb) 80 9,011 Chain (1); Topological domain (2); Transit peptide (1); Transmembrane (1) TRANSMEM 33 59 Helical. {ECO:0000250}. TOPO_DOM 25 32 Mitochondrial matrix. {ECO:0000250}.; TOPO_DOM 60 80 Mitochondrial intermembrane. {ECO:0000250}. FUNCTION: This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. Plays a role in proper central nervous system (CNS) development in vertebrates (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}. +Q61387 COX7R_MOUSE Cytochrome c oxidase subunit 7A-related protein, mitochondrial (Cytochrome c oxidase subunit VIIa-related protein) (Silica-induced gene 81 protein) (SIG-81) (Supercomplex assembly factor I) 111 12,399 Chain (1); Modified residue (1); Transit peptide (1) FUNCTION: Involved in the regulation of oxidative phosphorylation and energy metabolism (PubMed:23857330, PubMed:23812712). Necessary for the assembly of mitochondrial respiratory supercomplex (PubMed:23857330, PubMed:23812712). {ECO:0000269|PubMed:23812712, ECO:0000269|PubMed:23857330}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}. SUBUNIT: Interacts with the mitochondrial respiratory supercomplex. {ECO:0000269|PubMed:23812712}. +A6H666 COX8C_MOUSE Cytochrome c oxidase subunit 8C, mitochondrial (Cytochrome c oxidase polypeptide 8 isoform 3) (Cytochrome c oxidase polypeptide VIII isoform 3) (COX VIII-3) (Cytochrome c oxidase subunit 8-3) 72 8,009 Chain (1); Topological domain (2); Transit peptide (1); Transmembrane (1) TRANSMEM 41 64 Helical. {ECO:0000250}. TOPO_DOM 30 40 Mitochondrial matrix. {ECO:0000250}.; TOPO_DOM 65 72 Mitochondrial intermembrane. {ECO:0000250}. FUNCTION: This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}. +Q9WTZ8 BEX2_MOUSE Protein BEX2 (Brain-expressed X-linked protein 2 homolog) 129 15,452 Chain (1); Modified residue (1) FUNCTION: Regulator of mitochondrial apoptosis and G1 cell cycle. Regulates the level of PP2A regulatory subunit B and PP2A phosphatase activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with LMO2, possibly leading to regulate the transcriptional activity of a DNA-binding complex containing LMO2 (By similarity). Interacts with OMP. {ECO:0000250, ECO:0000269|PubMed:12911636, ECO:0000269|PubMed:15198671}. TISSUE SPECIFICITY: Primarily localized to neuronal cells within several regions of the brain, including the olfactory epithelium, bulb, peri/paraventricular nuclei, suprachiasmatic nucleus, arcuate nucleus, median eminence, lateral hypothalamic area, thalamus, hippocampus and cerebellum (at protein level). {ECO:0000269|PubMed:15861462}. +Q9WTZ9 BEX3_MOUSE Protein BEX3 (Brain-expressed X-linked protein 3 homolog) (Nerve growth factor receptor-associated protein 1) (p75NTR-associated cell death executor) 124 14,542 Alternative sequence (1); Chain (1); Compositional bias (1); Erroneous termination (1); Motif (1); Mutagenesis (4); Region (2); Sequence conflict (2) FUNCTION: May be a signaling adapter molecule involved in p75NTR-mediated apoptosis induced by NGF. Plays a role in zinc-triggered neuronal death. {ECO:0000269|PubMed:10764727}. PTM: Ubiquitinated (Probable). Degraded by the proteasome. {ECO:0000305}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Shuttles between the cytoplasm and the nucleus. Associates with replicating mitochondria. SUBUNIT: Self-associates (PubMed:11830582). Binds to the DEATH domain of p75NTR/NGFR (PubMed:11830582). Interacts with 14-3-3 epsilon (YWHAE) (PubMed:11278287). Interacts with DIABLO/SMAC (PubMed:15178455). {ECO:0000269|PubMed:11278287, ECO:0000269|PubMed:11830582, ECO:0000269|PubMed:15178455}. DOMAIN: The nuclear export signal is required for export from the nucleus and the interactions with itself and p75NTR/NGFR. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12935912, ECO:0000269|PubMed:15563833}. +Q9CWT2 BEX4_MOUSE Protein BEX4 (Brain-expressed X-linked protein 4) 118 13,820 Chain (1); Region (2) FUNCTION: May play a role in microtubule deacetylation by negatively regulating the SIRT2 deacetylase activity toward alpha-tubulin and thereby participate to the control of cell cycle progression and genomic stability. {ECO:0000250|UniProtKB:Q9NWD9}. PTM: Ubiquitinated and degraded by the proteasome. {ECO:0000250|UniProtKB:Q3MKP9}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q9NWD9}. Nucleus {ECO:0000250|UniProtKB:Q9NWD9}. Cytoplasm {ECO:0000269|PubMed:28295929}. Note=Also localizes to microtubules. {ECO:0000250|UniProtKB:Q9NWD9}. SUBUNIT: Interacts with alpha-tubulin. Interacts with SIRT2. {ECO:0000250|UniProtKB:Q9NWD9}. TISSUE SPECIFICITY: Expressed in both Sertoli and germ cells as well as interstitial area of the testis (at protein level). {ECO:0000269|PubMed:28295929}. +A2AMT1 BFSP1_MOUSE Filensin (Beaded filament structural protein 1) (Lens fiber cell beaded-filament structural protein CP 95) (CP95) 669 73,669 Alternative sequence (1); Chain (1); Domain (1); Modified residue (1); Region (7); Sequence conflict (6) SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q06002}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q06002}; Cytoplasmic side {ECO:0000250|UniProtKB:Q06002}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q06002}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q06002}. Note=Detected adjacent to the cell membrane. {ECO:0000250|UniProtKB:Q06002}. SUBUNIT: Associates with BFSP2 to form long fibrils (By similarity). Identified in complexes that contain VIM, EZR, AHNAK, BFSP1, BFSP2, ANK2, PLEC, PRX and spectrin (PubMed:21745462). {ECO:0000250|UniProtKB:Q06002, ECO:0000269|PubMed:21745462}. TISSUE SPECIFICITY: Detected in eye lens fiber cells (at protein level) (PubMed:21745462). {ECO:0000269|PubMed:21745462}. +Q9WTY4 AQP5_MOUSE Aquaporin-5 (AQP-5) 265 28,274 Chain (1); Glycosylation (1); Motif (2); Topological domain (7); Transmembrane (6) TRANSMEM 13 33 Helical. {ECO:0000255}.; TRANSMEM 37 57 Helical. {ECO:0000255}.; TRANSMEM 88 108 Helical. {ECO:0000255}.; TRANSMEM 127 147 Helical. {ECO:0000255}.; TRANSMEM 162 182 Helical. {ECO:0000255}.; TRANSMEM 206 226 Helical. {ECO:0000255}. TOPO_DOM 1 12 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 34 36 Extracellular. {ECO:0000255}.; TOPO_DOM 58 87 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 109 126 Extracellular. {ECO:0000255}.; TOPO_DOM 148 161 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 183 205 Extracellular. {ECO:0000255}.; TOPO_DOM 227 265 Cytoplasmic. {ECO:0000255}. FUNCTION: Forms a water-specific channel. Implicated in the generation of saliva, tears, and pulmonary secretions. Required for TRPV4 activation by hypotonicity (PubMed:16571723). Together with TRPV4, controls regulatory volume decrease in salivary epithelial cells (PubMed:16571723). {ECO:0000269|PubMed:16571723}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:16571723}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Interacts with TRPV4; the interaction is probably indirect and regulates TRPV4 activation by hypotonicity. {ECO:0000269|PubMed:16571723}. DOMAIN: Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA). TISSUE SPECIFICITY: Expressed in salivary glands (at protein level). {ECO:0000269|PubMed:16571723}. +Q9DCL2 CIA2A_MOUSE Cytosolic iron-sulfur assembly component 2A (MIP18 family protein FAM96A) 160 18,418 Chain (1); Metal binding (8) FUNCTION: Component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into extramitochondrial Fe/S proteins (PubMed:23891004). As a CIA complex component and in collaboration with CIAO1 specifically matures ACO1 and stabilizes IREB2 (PubMed:23891004). May play a role in chromosome segregation through establishment of sister chromatid cohesion. May induce apoptosis in collaboration with APAF1 (PubMed:25716227). {ECO:0000250, ECO:0000269|PubMed:23891004, ECO:0000269|PubMed:25716227}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. SUBUNIT: Monomer and homodimer (By similarity). Component of the CIA complex (PubMed:23891004). Interacts with CIAO1 (PubMed:23891004). Interacts with IREB2 (PubMed:23891004). Interacts with APAF1 (By similarity). {ECO:0000250|UniProtKB:Q9H5X1, ECO:0000269|PubMed:23891004}. TISSUE SPECIFICITY: Expressed in interstitial cell lineages. {ECO:0000269|PubMed:25716227}. +Q9CWX2 CIA30_MOUSE Complex I intermediate-associated protein 30, mitochondrial (NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 1) 328 37,810 Chain (1); Erroneous initiation (2); Modified residue (1); Sequence conflict (3); Transit peptide (1) FUNCTION: Chaperone protein involved in the assembly of the mitochondrial NADH:ubiquinone oxidoreductase complex (complex I). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. SUBUNIT: Part of the mitochondrial complex I assembly (MCIA) complex. The complex comprises at least TMEM126B, CIA30, ECSIT, and ACAD9 (By similarity). Interacts with ECSIT (By similarity). Interacts with ACAD9 (By similarity). {ECO:0000250|UniProtKB:Q9Y375}. +Q924A2 CIC_MOUSE Protein capicua homolog 2510 258,130 Alternative sequence (3); Chain (1); Compositional bias (5); DNA binding (1); Modified residue (28); Region (1); Sequence caution (1); Sequence conflict (8) FUNCTION: Transcriptional repressor which plays a role in development of the central nervous system (CNS) (PubMed:17190598). In concert with ATXN1 and ATXN1L, involved in brain development (PubMed:28288114). {ECO:0000269|PubMed:17190598, ECO:0000269|PubMed:28288114}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}. SUBUNIT: Isoform 1: Interacts with ATXN1 (PubMed:17190598). Isoform 2: Interacts with ATXN1 (PubMed:17190598). Interacts with ATXN1L (PubMed:17322884). Found in a complex with ATXN1 and ATXN1L (PubMed:28288114). {ECO:0000269|PubMed:17190598, ECO:0000269|PubMed:17322884, ECO:0000269|PubMed:28288114}. TISSUE SPECIFICITY: Expressed in the cortex and hypothalamus (at protein level). Isoform 1: Present in cerebellum (at protein level) (PubMed:17190598). Isoform 2: Present in cerebellum (at protein level) (PubMed:17190598). {ECO:0000269|PubMed:17190598, ECO:0000269|PubMed:28288114}. +O70302 CIDEA_MOUSE Cell death activator CIDE-A (Cell death-inducing DFFA-like effector A) 217 24,669 Chain (1); Domain (1); Mutagenesis (3); Sequence conflict (1) FUNCTION: Binds to lipid droplets and regulates their enlargement, thereby restricting lipolysis and favoring storage. At focal contact sites between lipid droplets, promotes directional net neutral lipid transfer from the smaller to larger lipid droplets. The transfer direction may be driven by the internal pressure difference between the contacting lipid droplet pair and occurs at a lower rate than that promoted by CIDEC. Acts as a CEBPB coactivator in mammary epithelial cells to control the expression of a subset of CEBPB downstream target genes, including ID2, IGF1, PRLR, SOCS1, SOCS3, XDH, but not casein. By interacting with CEBPB, strengthens the association of CEBPB with the XDH promoter, increases histone acetylation and dissociates HDAC1 from the promoter. When overexpressed, induces apoptosis. The physiological significance of its role in apoptosis is unclear. {ECO:0000269|PubMed:18509062, ECO:0000269|PubMed:22144693, ECO:0000269|PubMed:22245780, ECO:0000269|PubMed:9564035}. SUBCELLULAR LOCATION: Lipid droplet. Nucleus. Note=Enriched at lipid droplet contact sites. Using a GFP-tagged construct, has been shown to localize to mitonchondria, where it could interact with UCP1 and hence inhibit UCP1 uncoupling activity (PubMed:12910269). These data could not be confirmed (PubMed:22245780, PubMed:18509062). {ECO:0000269|PubMed:12910269, ECO:0000269|PubMed:18509062, ECO:0000269|PubMed:22245780}. SUBUNIT: Interacts with CIDEC (By similarity). Directly interacts with CEBPB. {ECO:0000250, ECO:0000269|PubMed:22245780}. TISSUE SPECIFICITY: Highly expressed in brown adipose tissue and, at lower levels, in white adipose tissue (at protein level). Expressed in mammary gland during pregnancy and lactation, in epithelial cells, but not in the surrounding adipose tissue. Secreted into milk via milk fat globules. Undetectable in undifferentiated preadipocytes. {ECO:0000269|PubMed:12910269, ECO:0000269|PubMed:18509062, ECO:0000269|PubMed:22245780}. +Q8BWY9 CIP2A_MOUSE Protein CIP2A (Cancerous inhibitor of PP2A) (p90 autoantigen homolog) 907 102,043 Chain (1); Coiled coil (1); Erroneous initiation (1); Modified residue (2); Region (2); Sequence conflict (3); Transmembrane (1) TRANSMEM 194 214 Helical. {ECO:0000255}. FUNCTION: Promotes anchorage-independent cell growth and tumor formation. {ECO:0000250|UniProtKB:Q8TCG1}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Cytoplasm {ECO:0000250|UniProtKB:Q8TCG1}. Note=Slightly concentrates in the perinuclear region. {ECO:0000250|UniProtKB:Q8TCG1}. SUBUNIT: Homodimer. Interacts with MYC. Interacts with PPP2R5C; this interaction stabilizes CIP2A. Interacts with PPP2R1A; this interaction stabilizes CIP2A. {ECO:0000250|UniProtKB:Q8TCG1}. TISSUE SPECIFICITY: Highly expressed in E17.5 and E18.5 liver but not pexpressed in adult liver. Expressed at moderate level in embryonic brain, muscle and epidermal layers. {ECO:0000269|PubMed:12118381}. +Q8CJ53 CIP4_MOUSE Cdc42-interacting protein 4 (Thyroid receptor-interacting protein 10) (TR-interacting protein 10) (TRIP-10) 603 68,489 Alternative sequence (2); Chain (1); Coiled coil (2); Domain (3); Modified residue (6); Mutagenesis (1); Region (10); Sequence conflict (1); Site (1) FUNCTION: Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during endocytosis. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also promotes CDC42-induced actin polymerization by recruiting WASL/N-WASP which in turn activates the Arp2/3 complex. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. Required for the formation of podosomes, actin-rich adhesion structures specific to monocyte-derived cells. May be required for the lysosomal retention of FASLG/FASL (By similarity). Required for translocation of GLUT4 to the plasma membrane in response to insulin signaling. {ECO:0000250, ECO:0000269|PubMed:12242347, ECO:0000269|PubMed:16418535}. PTM: Tyrosine phosphorylated. Also phosphorylated by PKA (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cell cortex. Lysosome. Golgi apparatus {ECO:0000250}. Cell membrane. Cell projection, phagocytic cup {ECO:0000250}. Note=Localizes to cortical regions coincident with F-actin, to lysosomes and to sites of phagocytosis in macrophages. Also localizes to the Golgi, and this requires AKAP9 (By similarity). Translocates to the plasma membrane in response to insulin stimulation, and this may require active RHOQ. {ECO:0000250}. SUBUNIT: Homodimerizes, the dimers can polymerize end-to-end to form filamentous structures (By similarity). Interacts with AKAP9, ARHGAP17, DAAM1, DIAPH1, DIAPH2, DNM1, FASLG/FASL, GAPVD1, LYN, microtubules, PDE6G, SRC and WAS/WASP. Interacts with the ligand binding domain of the thyroid receptor (TR) in the presence of thyroid hormone. May interact with CTNNB1 and HD/HTT (By similarity). Interacts specifically with GTP-bound CDC42 and RHOQ. Interacts with DNM2 and WASL. {ECO:0000250, ECO:0000269|PubMed:12242347, ECO:0000269|PubMed:16418535, ECO:0000269|PubMed:17189207}. DOMAIN: The F-BAR domain binds the phospholipid membrane with its concave surface. The end-to-end polymerization of dimers of these domains provides a curved surface that fits best membranes with around 600 A diameter, and may drive tubulation (By similarity). {ECO:0000250}. +Q6ZWX0 ASTER_MOUSE Protein Asterix (Protein WDR83OS homolog) 106 12,068 Chain (1); Initiator methionine (1); Modified residue (1); Transmembrane (2) TRANSMEM 40 62 Helical. {ECO:0000255}.; TRANSMEM 80 97 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q6HA09 ASTL_MOUSE Astacin-like metalloendopeptidase (EC 3.4.-.-) (Oocyte astacin) (Ovastacin) (Sperm acrosomal SLLP1-binding protein) 435 47,455 Active site (1); Alternative sequence (4); Chain (1); Disulfide bond (2); Domain (1); Metal binding (3); Sequence conflict (6); Signal peptide (1) FUNCTION: Oocyte-specific oolemmal receptor involved in sperm and egg adhesion and fertilization. Plays a role in the polyspermy inhibition. Probably acts as a protease for the post-fertilization cleavage of ZP2. Cleaves the sperm-binding ZP2 at the surface of the zona pellucida after fertilization and cortical granule exocytosis, rendering the zona pellucida unable to support further sperm binding. {ECO:0000269|PubMed:22206759, ECO:0000269|PubMed:22472438}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22206759, ECO:0000269|PubMed:22472438}. Cell membrane {ECO:0000269|PubMed:22206759}. Cytoplasmic granule {ECO:0000269|PubMed:22472438}. Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:22472438}. Note=Secretory granules. Localizes to the peripheral cortical granules of ovulated eggs. Probably exocytosed from cortical granules during post-fertilization. Detected throughout the ooplasm of germinal vesicle stage oocytes in early bilaminar secondary follicles at postnatal (PN) day 3. Detected in the microvillar domain of the oolemma in arrested ovulated secondary oocytes and in the first polar body prior to fertilization. Upon fertilization, detected in the perivitelline space (PVS) and occasionally on the oolemma in 2-cell through morulae stages. Colocalizes with SPACA3 at the microvillar domain of the oolemma and in the perivitelline space (PVS). {ECO:0000269|PubMed:22472438}. SUBUNIT: Interacts (via N-terminal domain) with SPACA3; the interaction occurs during fertilization. {ECO:0000269|PubMed:22206759}. TISSUE SPECIFICITY: Ovary-specific. Expressed in secondary, antral and Graafian follicle oocytes. Expressed in the egg cells. Not detected in two-cell embryos. Not detected in naked oocytes, oocytes in primordial or unilaminar primary follicles, or in any other ovarian cells at pre-pubertal, pubertal or adult stages (at protein level). Ovary-specific. {ECO:0000269|PubMed:22206759, ECO:0000269|PubMed:22472438}. +O54827 AT10A_MOUSE Probable phospholipid-transporting ATPase VA (EC 7.6.2.1) (ATPase class V type 10A) (P-locus fat-associated ATPase) (P4-ATPase flippase complex alpha subunit ATP10A) 1508 168,788 Active site (1); Chain (1); Compositional bias (2); Metal binding (2); Modified residue (1); Sequence conflict (8); Topological domain (11); Transmembrane (10) TRANSMEM 80 101 Helical. {ECO:0000255}.; TRANSMEM 108 129 Helical. {ECO:0000255}.; TRANSMEM 314 335 Helical. {ECO:0000255}.; TRANSMEM 367 388 Helical. {ECO:0000255}.; TRANSMEM 1102 1122 Helical. {ECO:0000255}.; TRANSMEM 1135 1154 Helical. {ECO:0000255}.; TRANSMEM 1185 1206 Helical. {ECO:0000255}.; TRANSMEM 1214 1236 Helical. {ECO:0000255}.; TRANSMEM 1243 1263 Helical. {ECO:0000255}.; TRANSMEM 1282 1306 Helical. {ECO:0000255}. TOPO_DOM 1 79 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 102 107 Exoplasmic loop. {ECO:0000255}.; TOPO_DOM 130 313 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 336 366 Exoplasmic loop. {ECO:0000255}.; TOPO_DOM 389 1101 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1123 1134 Exoplasmic loop. {ECO:0000255}.; TOPO_DOM 1155 1184 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1207 1213 Exoplasmic loop. {ECO:0000255}.; TOPO_DOM 1237 1242 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1264 1281 Exoplasmic loop. {ECO:0000255}.; TOPO_DOM 1307 1508 Cytoplasmic. {ECO:0000255}. FUNCTION: Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}. Note=Exit from the endoplasmic reticulum requires the presence of TMEM30A. {ECO:0000250}. SUBUNIT: Component of a P4-ATPase flippase complex which consists of a catalytic alpha subunit and an accessory beta subunit. {ECO:0000250}. TISSUE SPECIFICITY: Found in testis and in white adipose tissue. Also detected in fetal tissues. {ECO:0000269|PubMed:11074018}. +Q8BZ32 ASXL2_MOUSE Putative Polycomb group protein ASXL2 (Additional sex combs-like protein 2) 1370 147,107 Chain (1); Compositional bias (5); Modified residue (9); Motif (2); Sequence conflict (6); Zinc finger (1) FUNCTION: Putative Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. PcG proteins are not required to initiate repression, but to maintain it during later stages of development. They probably act via methylation of histones, rendering chromatin heritably changed in its expressibility. Involved in transcriptional regulation mediated by ligand-bound nuclear hormone receptors, such as peroxisome proliferator-activated receptor gamma (PPARG). Acts as coactivator for PPARG and enhances its adipocyte differentiation-inducing activity; the function seems to involve differential recruitment of acetylated and methylated histone H3 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Interacts with PPARA and PPARG. {ECO:0000250}. DOMAIN: Contains one Leu-Xaa-Xaa-Leu-Leu (LXXLL) motif, which may be required for an association with nuclear receptors. {ECO:0000250}. +P98197 AT11A_MOUSE Probable phospholipid-transporting ATPase IH (EC 7.6.2.1) (ATPase IS) (ATPase class VI type 11A) (P4-ATPase flippase complex alpha subunit ATP11A) 1187 135,502 Active site (1); Chain (1); Metal binding (2); Modified residue (3); Topological domain (11); Transmembrane (10) TRANSMEM 62 82 Helical. {ECO:0000255}.; TRANSMEM 89 110 Helical. {ECO:0000255}.; TRANSMEM 297 318 Helical. {ECO:0000255}.; TRANSMEM 350 372 Helical. {ECO:0000255}.; TRANSMEM 885 905 Helical. {ECO:0000255}.; TRANSMEM 918 937 Helical. {ECO:0000255}.; TRANSMEM 968 989 Helical. {ECO:0000255}.; TRANSMEM 1004 1026 Helical. {ECO:0000255}.; TRANSMEM 1033 1053 Helical. {ECO:0000255}.; TRANSMEM 1072 1096 Helical. {ECO:0000255}. TOPO_DOM 1 61 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 83 88 Extracellular. {ECO:0000255}.; TOPO_DOM 111 296 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 319 349 Extracellular. {ECO:0000255}.; TOPO_DOM 373 884 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 906 917 Extracellular. {ECO:0000255}.; TOPO_DOM 938 967 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 990 1003 Extracellular. {ECO:0000255}.; TOPO_DOM 1027 1032 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1054 1071 Extracellular. {ECO:0000255}.; TOPO_DOM 1097 1138 Cytoplasmic. {ECO:0000255}. FUNCTION: Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Early endosome {ECO:0000250}. Recycling endosome {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Note=Exit from the endoplasmic reticulum requires the presence of TMEM30A, but not TMEM30B. In the presence of TMEM30A, predominantly located in the plasma membrane (By similarity). {ECO:0000250}. SUBUNIT: Component of a P4-ATPase flippase complex which consists of a catalytic alpha subunit and an accessory beta subunit. Interacts with TMEM30A (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Found in heart, muscle, liver and brain. Most abundant in heart. Also detected in fetal tissues. +Q9QZW0 AT11C_MOUSE Phospholipid-transporting ATPase 11C (EC 7.6.2.1) (ATPase class VI type 11C) (P4-ATPase flippase complex alpha subunit ATP11C) 1129 129,240 Active site (1); Alternative sequence (2); Chain (1); Coiled coil (2); Metal binding (2); Modified residue (4); Sequence conflict (1); Topological domain (10); Transmembrane (9) TRANSMEM 84 104 Helical. {ECO:0000255}.; TRANSMEM 288 308 Helical. {ECO:0000255}.; TRANSMEM 344 364 Helical. {ECO:0000255}.; TRANSMEM 877 897 Helical. {ECO:0000255}.; TRANSMEM 906 926 Helical. {ECO:0000255}.; TRANSMEM 953 973 Helical. {ECO:0000255}.; TRANSMEM 989 1009 Helical. {ECO:0000255}.; TRANSMEM 1024 1044 Helical. {ECO:0000255}.; TRANSMEM 1067 1087 Helical. {ECO:0000255}. TOPO_DOM 1 83 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 105 287 Extracellular. {ECO:0000255}.; TOPO_DOM 309 343 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 365 876 Extracellular. {ECO:0000255}.; TOPO_DOM 898 905 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 927 952 Extracellular. {ECO:0000255}.; TOPO_DOM 974 988 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1010 1023 Extracellular. {ECO:0000255}.; TOPO_DOM 1045 1066 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1088 1129 Extracellular. {ECO:0000255}. FUNCTION: Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. In the cell membrane of erythrocytes, it is required to maintain phosphatidylserine (PS) in the inner leaflet preventing its exposure on the surface. This asymmetric distribution is critical for the survival of erythrocytes in circulation since externalized PS is a phagocytic signal for splenic macrophages (By similarity). Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. Required for B cell differentiation past the pro-B cell stage (PubMed:21423173). Seems to mediate phosphatidylserine (PS) flipping in pro-B cells (PubMed:21423172). May be involved in the transport of cholestatic bile acids (PubMed:21518881). {ECO:0000250|UniProtKB:Q8NB49, ECO:0000269|PubMed:21423172, ECO:0000269|PubMed:21423173, ECO:0000269|PubMed:21518881}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}. Note=Efficient exit from the endoplasmic reticulum requires the presence of TMEM30A. Some cell membrane localization observed in the presence of TMEM30B (By similarity). {ECO:0000250}. SUBUNIT: Component of a P4-ATPase flippase complex which consists of a catalytic alpha subunit and an accessory beta subunit. Interacts with TMEM30A (By similarity). {ECO:0000250}. DISEASE: Note=Mice defective in Atp11c show defective B lymphopoiesis, specifically in mature bone marrow, hyperbilirubinemia linked to mild cholestasis and hepatocellular carcinoma. {ECO:0000269|PubMed:21423173, ECO:0000269|PubMed:21518881}. +Q8VD46 ASZ1_MOUSE Ankyrin repeat, SAM and basic leucine zipper domain-containing protein 1 (Germ cell-specific ankyrin, SAM and basic leucine zipper domain-containing protein) 475 52,984 Chain (1); Domain (1); Erroneous gene model prediction (1); Modified residue (3); Repeat (6); Sequence conflict (3) FUNCTION: Plays a central role during spermatogenesis by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons. Its association with pi-bodies suggests a participation in the primary piRNAs metabolic process. Required prior to the pachytene stage to facilitate the production of multiple types of piRNAs, including those associated with repeats involved in regulation of retrotransposons. May act by mediating protein-protein interactions during germ cell maturation. {ECO:0000269|PubMed:19730684}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12040005, ECO:0000269|PubMed:19730684}. Note=Component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis. Specifically localizes to pi-bodies, a subset of the nuage which contains primary piRNAs. SUBUNIT: Interacts with DDX4, PIWIL1, RANBP9 and TDRD1. {ECO:0000269|PubMed:19730684}. TISSUE SPECIFICITY: Expressed exclusively in testis and ovary with higher levels in testis. {ECO:0000269|PubMed:12040005}. +Q6PIC6 AT1A3_MOUSE Sodium/potassium-transporting ATPase subunit alpha-3 (Na(+)/K(+) ATPase alpha-3 subunit) (EC 3.6.3.9) (Na(+)/K(+) ATPase alpha(III) subunit) (Sodium pump subunit alpha-3) 1013 111,692 Active site (1); Chain (1); Metal binding (2); Modified residue (7); Region (1); Topological domain (11); Transmembrane (10) TRANSMEM 78 98 Helical. {ECO:0000255}.; TRANSMEM 122 142 Helical. {ECO:0000255}.; TRANSMEM 279 298 Helical. {ECO:0000255}.; TRANSMEM 311 328 Helical. {ECO:0000255}.; TRANSMEM 763 782 Helical. {ECO:0000255}.; TRANSMEM 793 813 Helical. {ECO:0000255}.; TRANSMEM 834 856 Helical. {ECO:0000255}.; TRANSMEM 909 928 Helical. {ECO:0000255}.; TRANSMEM 942 960 Helical. {ECO:0000255}.; TRANSMEM 976 996 Helical. {ECO:0000255}. TOPO_DOM 1 77 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 99 121 Extracellular. {ECO:0000255}.; TOPO_DOM 143 278 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 299 310 Extracellular. {ECO:0000255}.; TOPO_DOM 329 762 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 783 792 Extracellular. {ECO:0000255}.; TOPO_DOM 814 833 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 857 908 Extracellular. {ECO:0000255}.; TOPO_DOM 929 941 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 961 975 Extracellular. {ECO:0000255}.; TOPO_DOM 997 1013 Cytoplasmic. {ECO:0000255}. FUNCTION: This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: The sodium/potassium-transporting ATPase is composed of a catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an additional regulatory subunit. Interacts with regulatory subunit FXYD1. {ECO:0000250|UniProtKB:P06687}. +Q5XF89 AT133_MOUSE Probable cation-transporting ATPase 13A3 (EC 3.6.3.-) 1219 137,469 Active site (1); Alternative sequence (1); Chain (1); Compositional bias (1); Metal binding (2); Modified residue (1); Transmembrane (11) TRANSMEM 29 49 Helical. {ECO:0000255}.; TRANSMEM 202 222 Helical. {ECO:0000255}.; TRANSMEM 229 249 Helical. {ECO:0000255}.; TRANSMEM 406 426 Helical. {ECO:0000255}.; TRANSMEM 445 465 Helical. {ECO:0000255}.; TRANSMEM 937 957 Helical. {ECO:0000255}.; TRANSMEM 959 979 Helical. {ECO:0000255}.; TRANSMEM 996 1016 Helical. {ECO:0000255}.; TRANSMEM 1067 1087 Helical. {ECO:0000255}.; TRANSMEM 1099 1119 Helical. {ECO:0000255}.; TRANSMEM 1137 1157 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Expression is greatest in liver, followed by kidney, colon, stomach, brain and small intestine. Isoform 1 is highly expressed in the kidney while isoform 2 is highly expressed in the brain. {ECO:0000269|PubMed:15381061}. +Q5XF90 AT134_MOUSE Probable cation-transporting ATPase 13A4 (EC 3.6.3.-) (P5-ATPase isoform 4) 1193 132,804 Active site (1); Alternative sequence (4); Chain (1); Metal binding (2); Sequence conflict (6); Topological domain (12); Transmembrane (11) TRANSMEM 33 53 Helical. {ECO:0000255}.; TRANSMEM 199 219 Helical. {ECO:0000255}.; TRANSMEM 225 245 Helical. {ECO:0000255}.; TRANSMEM 402 422 Helical. {ECO:0000255}.; TRANSMEM 438 458 Helical. {ECO:0000255}.; TRANSMEM 902 922 Helical. {ECO:0000255}.; TRANSMEM 934 954 Helical. {ECO:0000255}.; TRANSMEM 974 994 Helical. {ECO:0000255}.; TRANSMEM 1037 1057 Helical. {ECO:0000255}.; TRANSMEM 1072 1092 Helical. {ECO:0000255}.; TRANSMEM 1106 1126 Helical. {ECO:0000255}. TOPO_DOM 1 32 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 54 198 Extracellular. {ECO:0000255}.; TOPO_DOM 220 224 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 246 401 Extracellular. {ECO:0000255}.; TOPO_DOM 423 437 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 459 901 Extracellular. {ECO:0000255}.; TOPO_DOM 923 933 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 955 973 Extracellular. {ECO:0000255}.; TOPO_DOM 995 1036 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1058 1071 Extracellular. {ECO:0000255}.; TOPO_DOM 1093 1105 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1127 1193 Extracellular. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in brain and stomach. {ECO:0000269|PubMed:15381061}. +Q3TYU2 AT135_MOUSE Probable cation-transporting ATPase 13A5 (EC 3.6.3.-) (P5-ATPase isoform 5) 1216 136,760 Active site (1); Alternative sequence (1); Chain (1); Glycosylation (2); Metal binding (2); Sequence conflict (4); Transmembrane (11) TRANSMEM 33 53 Helical. {ECO:0000255}.; TRANSMEM 198 218 Helical. {ECO:0000255}.; TRANSMEM 222 242 Helical. {ECO:0000255}.; TRANSMEM 401 421 Helical. {ECO:0000255}.; TRANSMEM 433 453 Helical. {ECO:0000255}.; TRANSMEM 896 916 Helical. {ECO:0000255}.; TRANSMEM 933 950 Helical. {ECO:0000255}.; TRANSMEM 971 991 Helical. {ECO:0000255}.; TRANSMEM 1040 1060 Helical. {ECO:0000255}.; TRANSMEM 1075 1095 Helical. {ECO:0000255}.; TRANSMEM 1113 1133 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Specifically expressed in brain and stomach. {ECO:0000269|PubMed:15381061}. +P14094 AT1B1_MOUSE Sodium/potassium-transporting ATPase subunit beta-1 (Sodium/potassium-dependent ATPase subunit beta-1) 304 35,195 Chain (1); Disulfide bond (3); Glycosylation (3); Modified residue (2); Region (1); Topological domain (2); Transmembrane (1) TRANSMEM 35 62 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 34 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 63 304 Extracellular. {ECO:0000255}. FUNCTION: This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The beta subunit regulates, through assembly of alpha/beta heterodimers, the number of sodium pumps transported to the plasma membrane.; FUNCTION: Involved in cell adhesion and establishing epithelial cell polarity. {ECO:0000250}. PTM: Glutathionylated. {ECO:0000269|PubMed:21454534}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000255}. Cell membrane, sarcolemma {ECO:0000269|PubMed:23392350}. Note=Colocalizes with OBSCN at the intercalated disk and sarcolemma in cardiomyocytes. Localizes in long striations at the level of Z and M lines. {ECO:0000269|PubMed:23392350}. SUBUNIT: The sodium/potassium-transporting ATPase is composed of a catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an additional regulatory subunit. Interacts with regulatory subunit FXYD1 (By similarity). Interacts with regulatory subunit FXYD3 (PubMed:15743908). Interacts with NKAIN1, NKAIN2 and NKAIN4 (PubMed:17606467). Interacts with MLC1 (By similarity). Part of a complex containing MLC1, TRPV4, AQP4 and HEPACAM (By similarity). Interacts with KIRREL3 (By similarity). Interacts with OBSCN (via protein kinase domain 1) (PubMed:23392350). {ECO:0000250|UniProtKB:P05026, ECO:0000250|UniProtKB:P07340, ECO:0000269|PubMed:15743908, ECO:0000269|PubMed:17606467, ECO:0000269|PubMed:23392350}. DOMAIN: The C-terminal lobe folds into an immunoglobulin-like domain and mediates cell adhesion properties. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in cardiac muscle and in flexor digitorum brevis (FDB) muscle (at protein level). {ECO:0000269|PubMed:23392350}. +B1AR13 CISD3_MOUSE CDGSH iron-sulfur domain-containing protein 3, mitochondrial (Melanoma nuclear protein 13) 137 15,676 Chain (1); Erroneous gene model prediction (2); Metal binding (8); Modified residue (5); Transit peptide (1) FUNCTION: Can transfer its iron-sulfur clusters to the apoferrodoxins FDX1 and FDX2. Contributes to mitochondrial iron homeostasis and in maintaining normal levels of free iron and reactive oxygen species, and thereby contributes to normal mitochondrial function. {ECO:0000250|UniProtKB:P0C7P0}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P0C7P0}. SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P0C7P0}. +Q9CZ05 AT7L1_MOUSE Ataxin-7-like protein 1 (Ataxin-7-like protein 4) 146 16,186 Alternative sequence (1); Chain (1); Erroneous initiation (2) +Q9CR84 AT5G1_MOUSE ATP synthase F(0) complex subunit C1, mitochondrial (ATP synthase lipid-binding protein) (ATP synthase membrane subunit c locus 1) (ATP synthase proteolipid P1) (ATPase protein 9) (ATPase subunit c) 136 14,200 Chain (1); Sequence conflict (1); Site (1); Transit peptide (1); Transmembrane (2) TRANSMEM 77 97 Helical. {ECO:0000255}.; TRANSMEM 112 132 Helical. {ECO:0000255}. FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. A homomeric c-ring of probably 10 subunits is part of the complex rotary element (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Component of an ATP synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MD and MP68 (By similarity). {ECO:0000250}. DISEASE: Note=This protein is the major protein stored in the storage bodies of animals or humans affected with ceroid lipofuscinosis (Batten disease). +Q9D5T0 ATAD1_MOUSE ATPase family AAA domain-containing protein 1 (EC 3.6.1.3) (Thorase) 361 40,744 Chain (1); Modified residue (1); Nucleotide binding (1); Sequence conflict (2) FUNCTION: ATPase that plays a critical role in regulating the surface expression of AMPA receptors (AMPAR), thereby regulating synaptic plasticity and learning and memory. Required for NMDA-stimulated AMPAR internalization and inhibition of GRIA1 and GRIA2 recycling back to the plasma membrane; these activities are ATPase-dependent. {ECO:0000269|PubMed:21496646}. SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:17768142}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000269|PubMed:21496646}. SUBUNIT: Interacts with GRIA2 and GRIP1 in an ATP-dependent manner. ATAD1-catalyzed ATP hydrolysis disrupts not only its binding to GRIA2 and GRIP1, but also interaction between GRIP1 and GRIA2, leading to AMPAR complex disassembly. {ECO:0000269|PubMed:21496646}. TISSUE SPECIFICITY: Widely expressed with the highest expression in the brain and testis. In the brain, relatively high expression in hippocampal CA1 pyramidal cells (at protein level). {ECO:0000269|PubMed:21496646}. +F6VAN0 ATF6A_MOUSE Cyclic AMP-dependent transcription factor ATF-6 alpha (cAMP-dependent transcription factor ATF-6 alpha) (Activating transcription factor 6 alpha) (ATF6-alpha) [Cleaved into: Processed cyclic AMP-dependent transcription factor ATF-6 alpha] 656 72,694 Chain (2); Compositional bias (1); Cross-link (1); Domain (1); Erroneous initiation (1); Glycosylation (3); Region (4); Sequence conflict (3); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 378 398 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 377 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 399 656 Lumenal. {ECO:0000255}. FUNCTION: Transmembrane glycoprotein of the endoplasmic reticulum that functions as a transcription activator and initiates the unfolded protein response (UPR) during endoplasmic reticulum stress. Cleaved upon ER stress, the N-terminal processed cyclic AMP-dependent transcription factor ATF-6 alpha translocates to the nucleus where it activates transcription of genes involved in the UPR. Binds DNA on the 5'-CCAC[GA]-3'half of the ER stress response element (ERSE) (5'-CCAAT-N(9)-CCAC[GA]-3') and of ERSE II (5'-ATTGG-N-CCACG-3'). Binding to ERSE requires binding of NF-Y to ERSE. Could also be involved in activation of transcription by the serum response factor. May play a role in foveal development and cone function in the retina (By similarity). {ECO:0000250|UniProtKB:P18850}. PTM: During unfolded protein response, a fragment of approximately 50 kDa containing the cytoplasmic transcription factor domain is released by proteolysis. The cleavage seems to be performed sequentially by site-1 and site-2 proteases (By similarity). {ECO:0000250}.; PTM: N-glycosylated. The glycosylation status may serve as a sensor for ER homeostasis, resulting in ATF6 activation to trigger the unfolded protein response (UPR) (By similarity). {ECO:0000250}.; PTM: Phosphorylated in vitro by MAPK14/P38MAPK. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: Processed cyclic AMP-dependent transcription factor ATF-6 alpha: Nucleus. Note=Under ER stress the cleaved N-terminal cytoplasmic domain translocates into the nucleus. THBS4 promotes its nuclear shuttling. SUBUNIT: Homodimer and heterodimer with ATF6-beta. The dimer interacts with the nuclear transcription factor Y (NF-Y) trimer through direct binding to NF-Y subunit C (NF-YC). Interacts also with the transcription factors GTF2I, YY1 and SRF. Interacts with XBP1 isoform 2; the interaction occurs in a ER stress-dependent manner (By similarity). Interacts (via lumenal domain) with THBS1 (PubMed:22682248). Interacts with THBS4 (via EGF-like 3; calcium-binding domain) which facilitates its processing, activation and nuclear translocation (PubMed:22682248). {ECO:0000250|UniProtKB:P18850, ECO:0000269|PubMed:22682248}. DOMAIN: The basic domain functions as a nuclear localization signal. {ECO:0000250}.; DOMAIN: The basic leucine-zipper domain is sufficient for association with the NF-Y trimer and binding to ERSE. {ECO:0000250}. +Q9Z2A5 ATE1_MOUSE Arginyl-tRNA--protein transferase 1 (Arginyltransferase 1) (R-transferase 1) (EC 2.3.2.8) (Arginine-tRNA--protein transferase 1) 516 59,146 Alternative sequence (1); Chain (1); Sequence conflict (2) FUNCTION: Involved in the post-translational conjugation of arginine to the N-terminal aspartate or glutamate of a protein. This arginylation is required for degradation of the protein via the ubiquitin pathway. Does not arginylate cysteine residues. {ECO:0000269|PubMed:9858543}. SUBCELLULAR LOCATION: Isoform ATE1-1: Nucleus {ECO:0000269|PubMed:9858543}. Cytoplasm {ECO:0000269|PubMed:9858543}.; SUBCELLULAR LOCATION: Isoform ATE1-2: Cytoplasm {ECO:0000269|PubMed:9858543}. SUBUNIT: Monomer. Interacts with LIAT1. {ECO:0000269|PubMed:25369936, ECO:0000305}. TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9858543}. +Q9CQY1 ATG12_MOUSE Ubiquitin-like protein ATG12 (Autophagy-related protein 12) (APG12-like) 141 15,207 Chain (1); Cross-link (1); Sequence conflict (1) FUNCTION: Ubiquitin-like protein involved in autophagy vesicles formation. Conjugation with ATG5 through a ubiquitin-like conjugating system involving also ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate acts as an E3-like enzyme which is required for lipidation of ATG8 family proteins and their association to the vesicle membranes. {ECO:0000269|PubMed:11266458, ECO:0000269|PubMed:12890687, ECO:0000269|PubMed:20723759}.; FUNCTION: (Microbial infection) May act as a proviral factor. In association with ATG5, negatively regulates the innate antiviral immune response by impairing the type I IFN production pathway upon vesicular stomatitis virus (VSV) infection. {ECO:0000269|PubMed:17709747}. PTM: Acetylated by EP300. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Preautophagosomal structure membrane {ECO:0000250|UniProtKB:O94817}; Peripheral membrane protein {ECO:0000250|UniProtKB:O94817}. Note=TECPR1 recruits the ATG12-ATG5 conjugate to the autolysosomal membrane. {ECO:0000250|UniProtKB:O94817}. SUBUNIT: Forms a conjugate with ATG5 (PubMed:11266458, PubMed:12482611, PubMed:12890687, PubMed:12665549, PubMed:18768753, PubMed:19417210). The ATG12-ATG5 conjugate forms a complex with several units of ATG16L (PubMed:12665549). Interacts with DHX58/RIG-1, IFIH1/MDA5 and MAVS/IPS-1 in monomeric form as well as in ATG12-ATG5 conjugate. The interaction with MAVS is further enhanced upon vesicular stomatitis virus (VSV) infection. Interacts with ATG3 and ATG7 (By similarity). Interacts with ATG10 (PubMed:12482611). Interacts with TECPR1 (By similarity). {ECO:0000250|UniProtKB:O94817, ECO:0000269|PubMed:11266458, ECO:0000269|PubMed:12482611, ECO:0000269|PubMed:12665549, ECO:0000269|PubMed:12890687, ECO:0000269|PubMed:18768753, ECO:0000269|PubMed:19417210}. DOMAIN: Shares weak sequence similarity with ubiquitin family, but contains an 'ubiquitin superfold' and the C-terminal Gly is required for isopeptide linkage. {ECO:0000269|PubMed:18704115}. TISSUE SPECIFICITY: Ubiquitous. +Q8R1P4 ATG10_MOUSE Ubiquitin-like-conjugating enzyme ATG10 (EC 2.3.2.-) (Autophagy-related protein 10) (APG10-like) (mAPG10) 215 24,577 Active site (1); Chain (1); Mutagenesis (1); Sequence conflict (7) FUNCTION: E2-like enzyme involved in autophagy. Acts as an E2-like enzyme that catalyzes the conjugation of ATG12 to ATG5. ATG12 conjugation to ATG5 is required for autophagy. Likely serves as an ATG5-recognition molecule. Not involved in ATG12 conjugation to ATG3. Plays a role in adenovirus-mediated cell lysis. {ECO:0000269|PubMed:12890687, ECO:0000269|PubMed:20723759, ECO:0000269|PubMed:21367888}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. SUBUNIT: Interacts with MAP1LC3A. By interacting with MAP1LC3A, it plays a role in the conjugation of ATG12 to ATG5. Also able to directly interact either with ATG5 or ATG7. {ECO:0000269|PubMed:12482611, ECO:0000269|PubMed:12890687}. +Q64436 ATP4A_MOUSE Potassium-transporting ATPase alpha chain 1 (EC 3.6.3.10) (Gastric H(+)/K(+) ATPase subunit alpha) (Proton pump) 1033 114,016 Active site (1); Chain (1); Metal binding (2); Modified residue (7); Sequence conflict (2); Topological domain (11); Transmembrane (10) TRANSMEM 97 117 Helical. {ECO:0000255}.; TRANSMEM 141 161 Helical. {ECO:0000255}.; TRANSMEM 298 317 Helical. {ECO:0000255}.; TRANSMEM 330 347 Helical. {ECO:0000255}.; TRANSMEM 782 801 Helical. {ECO:0000255}.; TRANSMEM 812 832 Helical. {ECO:0000255}.; TRANSMEM 853 875 Helical. {ECO:0000255}.; TRANSMEM 928 947 Helical. {ECO:0000255}.; TRANSMEM 962 980 Helical. {ECO:0000255}.; TRANSMEM 996 1016 Helical. {ECO:0000255}. TOPO_DOM 1 96 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 118 140 Lumenal. {ECO:0000255}.; TOPO_DOM 162 297 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 318 329 Lumenal. {ECO:0000255}.; TOPO_DOM 348 781 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 802 811 Lumenal. {ECO:0000255}.; TOPO_DOM 833 852 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 876 927 Lumenal. {ECO:0000255}.; TOPO_DOM 948 961 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 981 995 Lumenal. {ECO:0000255}.; TOPO_DOM 1017 1033 Cytoplasmic. {ECO:0000255}. FUNCTION: Catalyzes the hydrolysis of ATP coupled with the exchange of H(+) and K(+) ions across the plasma membrane. Responsible for acid production in the stomach. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBUNIT: Composed of two subunits: alpha (catalytic) and beta. +P50992 ATP4B_MOUSE Potassium-transporting ATPase subunit beta (Gastric H(+)/K(+) ATPase subunit beta) (Proton pump beta chain) 294 33,566 Chain (1); Disulfide bond (3); Glycosylation (7); Region (1); Sequence conflict (3); Topological domain (2); Transmembrane (1) TRANSMEM 37 57 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 36 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 58 294 Extracellular. {ECO:0000255}. FUNCTION: Required for stabilization and maturation of the catalytic proton pump alpha subunit and may also involved in cell adhesion and establishing epithelial cell polarity. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein. SUBUNIT: Composed of two subunits: alpha (catalytic) and beta. DOMAIN: The C-terminal lobe folds into an immunoglobulin-like domain and mediates cell adhesion properties. {ECO:0000250}. +Q6IRU5 CLCB_MOUSE Clathrin light chain B (Lcb) 229 25,172 Alternative sequence (2); Chain (1); Disulfide bond (1); Modified residue (5); Region (1) FUNCTION: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Membrane, coated pit; Peripheral membrane protein; Cytoplasmic side. Note=Cytoplasmic face of coated pits and vesicles. SUBUNIT: Clathrin coats are formed from molecules containing 3 heavy chains and 3 light chains. Interacts (via N-terminus) with HIP1. Interacts with HIP1R. +Q9DCX2 ATP5H_MOUSE ATP synthase subunit d, mitochondrial (ATPase subunit d) (ATP synthase peripheral stalk subunit d) 161 18,749 Chain (1); Initiator methionine (1); Modified residue (16); Sequence conflict (2) FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements. SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane. SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(0) seems to have nine subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L). Component of an ATP synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MD and MP68 (By similarity). {ECO:0000250}. +Q06185 ATP5I_MOUSE ATP synthase subunit e, mitochondrial (ATPase subunit e) (ATP synthase membrane subunit e) 71 8,236 Chain (1); Initiator methionine (1); Modified residue (2); Sequence conflict (2) FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane. SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane. SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(0) seems to have nine subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L). Component of an ATP synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MD and MP68 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Mammary gland, liver, kidney, heart, spleen, brain and lung. +Q64347 CLCN1_MOUSE Chloride channel protein 1 (ClC-1) (Chloride channel protein, skeletal muscle) 994 109,794 Binding site (3); Chain (1); Domain (2); Intramembrane (4); Modified residue (1); Motif (3); Mutagenesis (1); Sequence conflict (17); Topological domain (13); Transmembrane (10) INTRAMEM 184 195 Helical. {ECO:0000250|UniProtKB:P35523}.; INTRAMEM 269 290 Helical. {ECO:0000250|UniProtKB:P35523}.; INTRAMEM 415 426 Helical. {ECO:0000250|UniProtKB:P35523}.; INTRAMEM 522 554 Helical. {ECO:0000250|UniProtKB:P35523}. TRANSMEM 119 150 Helical. {ECO:0000250|UniProtKB:P35523}.; TRANSMEM 159 179 Helical. {ECO:0000250|UniProtKB:P35523}.; TRANSMEM 209 228 Helical. {ECO:0000250|UniProtKB:P35523}.; TRANSMEM 229 246 Helical. {ECO:0000250|UniProtKB:P35523}.; TRANSMEM 302 321 Helical. {ECO:0000250|UniProtKB:P35523}.; TRANSMEM 348 376 Helical. {ECO:0000250|UniProtKB:P35523}.; TRANSMEM 391 408 Helical. {ECO:0000250|UniProtKB:P35523}.; TRANSMEM 458 478 Helical. {ECO:0000250|UniProtKB:P35523}.; TRANSMEM 479 498 Helical. {ECO:0000250|UniProtKB:P35523}.; TRANSMEM 558 578 Helical. {ECO:0000250|UniProtKB:P35523}. TOPO_DOM 1 118 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 151 158 Extracellular. {ECO:0000305}.; TOPO_DOM 180 183 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 196 208 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 247 268 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 291 301 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 322 347 Extracellular. {ECO:0000305}.; TOPO_DOM 377 390 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 409 414 Extracellular. {ECO:0000305}.; TOPO_DOM 427 457 Extracellular. {ECO:0000305}.; TOPO_DOM 499 521 Extracellular. {ECO:0000305}.; TOPO_DOM 555 557 Extracellular. {ECO:0000305}.; TOPO_DOM 579 994 Cytoplasmic. {ECO:0000305}. FUNCTION: Voltage-gated chloride channel (By similarity). Plays an important role in membrane repolarization in skeletal muscle cells after muscle contraction (Probable) (PubMed:8119941). {ECO:0000250|UniProtKB:P35523, ECO:0000269|PubMed:8119941, ECO:0000305|PubMed:1659665}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P35523}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P35523}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P35523}. TISSUE SPECIFICITY: Predominantly expressed in skeletal muscles. {ECO:0000269|PubMed:1659665}. +P51791 CLCN3_MOUSE H(+)/Cl(-) exchange transporter 3 (Chloride channel protein 3) (ClC-3) (Chloride transporter ClC-3) 818 90,869 Alternative sequence (1); Binding site (3); Chain (1); Domain (2); Glycosylation (3); Intramembrane (6); Motif (3); Nucleotide binding (2); Site (2); Topological domain (2); Transmembrane (10) INTRAMEM 241 248 Helical. {ECO:0000250}.; INTRAMEM 313 325 Helical. {ECO:0000250}.; INTRAMEM 329 337 Helical. {ECO:0000250}.; INTRAMEM 572 586 Helical. {ECO:0000250}.; INTRAMEM 590 601 Helical. {ECO:0000250}.; INTRAMEM 602 605 Note=Loop between two helices. {ECO:0000250}. TRANSMEM 126 163 Helical. {ECO:0000250}.; TRANSMEM 209 232 Helical. {ECO:0000250}.; TRANSMEM 258 276 Helical. {ECO:0000250}.; TRANSMEM 282 301 Helical. {ECO:0000250}.; TRANSMEM 349 367 Helical. {ECO:0000250}.; TRANSMEM 391 416 Helical. {ECO:0000250}.; TRANSMEM 423 443 Helical. {ECO:0000250}.; TRANSMEM 500 520 Helical. {ECO:0000250}.; TRANSMEM 525 544 Helical. {ECO:0000250}.; TRANSMEM 606 624 Helical. {ECO:0000250}. TOPO_DOM 1 125 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 625 818 Cytoplasmic. {ECO:0000250}. FUNCTION: Mediates the exchange of chloride ions against protons. Functions as antiporter and contributes to the acidification of the endosome and synaptic vesicle lumen, and may thereby affect vesicle trafficking and exocytosis. May play an important role in neuronal cell function through regulation of membrane excitability by protein kinase C. It could help neuronal cells to establish short-term memory. {ECO:0000269|PubMed:15504734, ECO:0000269|PubMed:18923035}. PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000269|PubMed:16222710}; Multi-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000269|PubMed:16222710}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000269|PubMed:18923035}; Multi-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Detected in kidney, in the apical part of proximal tubule cells (at protein level). Expressed at high levels in the kidney while a low level expression is seen in the brain. Within the brain, it is prominent in the hippocampus, cerebral cortex and olfactory bulb. {ECO:0000269|PubMed:18923035}. +Q61418 CLCN4_MOUSE H(+)/Cl(-) exchange transporter 4 (Chloride channel protein 4) (ClC-4) (Chloride transporter ClC-4) 747 83,733 Binding site (4); Chain (1); Domain (2); Intramembrane (6); Motif (3); Nucleotide binding (2); Region (1); Sequence conflict (4); Site (2); Topological domain (2); Transmembrane (10) INTRAMEM 170 177 Helical. {ECO:0000250}.; INTRAMEM 242 254 Helical. {ECO:0000250}.; INTRAMEM 258 266 Helical. {ECO:0000250}.; INTRAMEM 501 515 Helical. {ECO:0000250}.; INTRAMEM 519 530 Helical. {ECO:0000250}.; INTRAMEM 531 534 Note=Loop between two helices. {ECO:0000250}. TRANSMEM 55 92 Helical. {ECO:0000250}.; TRANSMEM 138 161 Helical. {ECO:0000250}.; TRANSMEM 187 205 Helical. {ECO:0000250}.; TRANSMEM 211 230 Helical. {ECO:0000250}.; TRANSMEM 278 296 Helical. {ECO:0000250}.; TRANSMEM 320 345 Helical. {ECO:0000250}.; TRANSMEM 352 372 Helical. {ECO:0000250}.; TRANSMEM 429 449 Helical. {ECO:0000250}.; TRANSMEM 454 473 Helical. {ECO:0000250}.; TRANSMEM 535 553 Helical. {ECO:0000250}. TOPO_DOM 1 54 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 554 747 Cytoplasmic. {ECO:0000250}. FUNCTION: Proton-coupled chloride transporter. Functions as antiport system and exchanges chloride ions against protons (By similarity). {ECO:0000250|UniProtKB:P51793}. SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000250|UniProtKB:P51794}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P51794}. Late endosome membrane {ECO:0000250|UniProtKB:P51794}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P51794}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P51793}. TISSUE SPECIFICITY: Predominantly present in excitable tissues such as nervous system and skeletal muscle. Not detected in heart. {ECO:0000269|PubMed:17023393}. +O70496 CLCN7_MOUSE H(+)/Cl(-) exchange transporter 7 (Chloride channel 7 alpha subunit) (Chloride channel protein 7) (ClC-7) 803 88,713 Binding site (3); Chain (1); Domain (2); Intramembrane (7); Modified residue (2); Motif (3); Nucleotide binding (2); Site (2); Topological domain (2); Transmembrane (10) INTRAMEM 204 211 Helical. {ECO:0000250}.; INTRAMEM 286 298 Helical. {ECO:0000250}.; INTRAMEM 302 310 Helical. {ECO:0000250}.; INTRAMEM 543 557 Helical. {ECO:0000250}.; INTRAMEM 558 560 Note=Loop between two helices. {ECO:0000250}.; INTRAMEM 561 572 Helical. {ECO:0000250}.; INTRAMEM 573 576 Note=Loop between two helices. {ECO:0000250}. TRANSMEM 125 157 Helical. {ECO:0000250}.; TRANSMEM 172 195 Helical. {ECO:0000250}.; TRANSMEM 221 239 Helical. {ECO:0000250}.; TRANSMEM 245 262 Helical. {ECO:0000250}.; TRANSMEM 320 339 Helical. {ECO:0000250}.; TRANSMEM 373 403 Helical. {ECO:0000250}.; TRANSMEM 408 430 Helical. {ECO:0000250}.; TRANSMEM 485 505 Helical. {ECO:0000250}.; TRANSMEM 510 533 Helical. {ECO:0000250}.; TRANSMEM 577 595 Helical. {ECO:0000250}. TOPO_DOM 1 124 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 596 803 Cytoplasmic. {ECO:0000250}. FUNCTION: Slowly voltage-gated channel mediating the exchange of chloride ions against protons. Functions as antiporter and contributes to the acidification of the lysosome lumen. {ECO:0000269|PubMed:16525474, ECO:0000269|PubMed:19661288}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:16525474}; Multi-pass membrane protein {ECO:0000269|PubMed:16525474}. SUBUNIT: Chloride channel 7 are heteromers of alpha (CLCN7) and beta (OSTM1) subunits. {ECO:0000269|PubMed:16525474}. +Q9Z0S5 CLD15_MOUSE Claudin-15 227 24,280 Beta strand (6); Chain (1); Disulfide bond (1); Helix (5); Modified residue (4); Mutagenesis (5); Region (1); Sequence conflict (2); Site (3); Topological domain (5); Transmembrane (4) TRANSMEM 2 24 Helical.; TRANSMEM 75 99 Helical.; TRANSMEM 116 140 Helical.; TRANSMEM 160 182 Helical. TOPO_DOM 1 1 Cytoplasmic. {ECO:0000269|PubMed:24744376}.; TOPO_DOM 25 74 Extracellular. {ECO:0000269|PubMed:24744376}.; TOPO_DOM 100 115 Cytoplasmic. {ECO:0000269|PubMed:24744376}.; TOPO_DOM 141 159 Extracellular. {ECO:0000269|PubMed:24744376}.; TOPO_DOM 183 227 Cytoplasmic. {ECO:0000269|PubMed:24744376}. FUNCTION: Claudins function as major constituents of the tight junction complexes that regulate the permeability of epithelia. While some claudin family members function as impermeable barriers, others mediate the permeability to ions and small molecules. Often, several claudin family members are coexpressed and interact with each other, and this determines the overall permeability. CLDN15 forms tight junctions that mediate the paracellular transport of small monovalent cations along a concentration gradient, due to selective permeability for Na(+), Li(+) and K(+) ions, but selects against Cl(-) ions. Plays an important role in paracellular Na(+) transport in the intestine and in Na(+) homeostasis. Required for normal Na(+)-dependent intestinal nutrient uptake. {ECO:0000269|PubMed:18242218, ECO:0000269|PubMed:20727355, ECO:0000269|PubMed:23089202}. PTM: Palmitoylated when heterogeneously expressed in S.frugiperda cells. {ECO:0000269|PubMed:24744376}. SUBCELLULAR LOCATION: Cell junction, tight junction. Cell membrane; Multi-pass membrane protein. Note=Tight junctions form continuous circumferential cell-cell contacts at the borders of apical and lateral cell membranes that seal the intercellular space and show up as strand-like structures in electron microscopy. SUBUNIT: Can form linear homooligomers in the membrane, giving rise to tight junction strand-like structures. {ECO:0000269|PubMed:24744376}. TISSUE SPECIFICITY: Detected in duodenum, jejunum and ileum. Detected on intestinal villi and crypts (at protein level). Ubiquitous. Detected in small intestine, colon, jejunum, heart, kidney and lung. {ECO:0000269|PubMed:16505581, ECO:0000269|PubMed:18242218, ECO:0000269|PubMed:20727355, ECO:0000269|PubMed:23089202}. +O88552 CLD2_MOUSE Claudin-2 230 24,484 Beta strand (1); Chain (1); Cross-link (1); Disulfide bond (1); Modified residue (2); Region (1); Topological domain (5); Transmembrane (4) TRANSMEM 8 28 Helical. {ECO:0000255}.; TRANSMEM 82 102 Helical. {ECO:0000255}.; TRANSMEM 117 137 Helical. {ECO:0000255}.; TRANSMEM 163 183 Helical. {ECO:0000255}. TOPO_DOM 1 7 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 29 81 Extracellular. {ECO:0000255}.; TOPO_DOM 103 116 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 138 162 Extracellular. {ECO:0000255}.; TOPO_DOM 184 230 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. {ECO:0000269|PubMed:10508613}. PTM: The disulfide bond is necessary for pore formation, but is not required for correct protein trafficking. {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000269|PubMed:11934881}. Cell membrane {ECO:0000269|PubMed:11934881}; Multi-pass membrane protein {ECO:0000269|PubMed:11934881}. SUBUNIT: Can form homo- and heteropolymers with other CLDN. Homopolymers interact with CLDN3, but not CLDN1, homopolymers. Directly interacts with TJP1/ZO-1, TJP2/ZO-2 and TJP3/ZO-3. {ECO:0000269|PubMed:10562289, ECO:0000269|PubMed:10601346}. TISSUE SPECIFICITY: Expressed in the kidney, liver and intestine, with higher levels in the ileum than in the jejunum. Low levels in the brain. {ECO:0000269|PubMed:11934881, ECO:0000269|PubMed:9647647}. +Q5M6W3 CLHC1_MOUSE Clathrin heavy chain linker domain-containing protein 1 596 69,414 Chain (1); Coiled coil (1); Sequence conflict (1) +P22518 CLK1_MOUSE Dual specificity protein kinase CLK1 (EC 2.7.12.1) (CDC-like kinase 1) (Protein kinase STY) 483 57,093 Active site (1); Alternative sequence (2); Binding site (1); Chain (1); Domain (1); Modified residue (2); Motif (1); Mutagenesis (1); Nucleotide binding (1); Sequence conflict (4) FUNCTION: Dual specificity kinase acting on both serine/threonine and tyrosine-containing substrates. Phosphorylates serine- and arginine-rich (SR) proteins of the spliceosomal complex and may be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing. Phosphorylates: SRSF1, SRSF3 and PTPN1. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells and adenovirus E1A pre-mRNA. {ECO:0000269|PubMed:9307018, ECO:0000269|PubMed:9315658}. PTM: Autophosphorylates on all three types of residues. {ECO:0000269|PubMed:9307018}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9307018}. SUBUNIT: Interacts with PPIG and UBL5. {ECO:0000250}. +O35491 CLK2_MOUSE Dual specificity protein kinase CLK2 (EC 2.7.12.1) (CDC-like kinase 2) 499 59,987 Active site (1); Binding site (1); Chain (1); Domain (1); Modified residue (7); Mutagenesis (1); Nucleotide binding (1); Sequence conflict (2) FUNCTION: Dual specificity kinase acting on both serine/threonine and tyrosine-containing substrates. Phosphorylates serine- and arginine-rich (SR) proteins of the spliceosomal complex. May be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing and can cause redistribution of SR proteins from speckles to a diffuse nucleoplasmic distribution. Acts as a suppressor of hepatic gluconeogenesis and glucose output by repressing PPARGC1A transcriptional activity on gluconeogenic genes via its phosphorylation. Phosphorylates PPP2R5B thereby stimulating the assembly of PP2A phosphatase with the PPP2R5B-AKT1 complex leading to dephosphorylation of AKT1. Phosphorylates: PTPN1, SRSF1 and SRSF3. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells. {ECO:0000269|PubMed:20074525, ECO:0000269|PubMed:21329884, ECO:0000269|PubMed:9307018}. PTM: Autophosphorylates on all three types of residues. Phosphorylation on Ser-34 and Thr-127 by AKT1 is induced by ionizing radiation or insulin. Phosphorylation plays a critical role in cell proliferation following low dose radiation and prevents cell death following high dose radiation. Phosphorylation at Thr-343 by PKB/AKT2 induces its kinase activity which is required for its stability. The phosphorylation status at Ser-141 influences its subnuclear localization; inhibition of phosphorylation at Ser-141 results in accumulation in the nuclear speckle. {ECO:0000269|PubMed:20074525, ECO:0000269|PubMed:9852100}. SUBCELLULAR LOCATION: Nucleus. Nucleus speckle. Note=Inhibition of phosphorylation at Ser-141 results in accumulation in the nuclear speckle. SUBUNIT: Interacts with RBMX and UBL5 (By similarity). Interacts with AKT1. {ECO:0000250, ECO:0000269|PubMed:20074525}. +O35493 CLK4_MOUSE Dual specificity protein kinase CLK4 (EC 2.7.12.1) (CDC-like kinase 4) 481 57,345 Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Domain (1); Modified residue (2); Mutagenesis (1); Nucleotide binding (1); Sequence conflict (3) FUNCTION: Dual specificity kinase acting on both serine/threonine and tyrosine-containing substrates. Phosphorylates serine- and arginine-rich (SR) proteins of the spliceosomal complex and may be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing. Phosphorylates SRSF1 and SRSF3. Required for the regulation of alternative splicing of MAPT/TAU. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells. {ECO:0000269|PubMed:11461155, ECO:0000269|PubMed:9307018}. PTM: Autophosphorylates on all three types of residues. {ECO:0000269|PubMed:9307018}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9307018}. SUBUNIT: Interacts with UBL5. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in the hippocampus, the cerebellum and the olfactory bulb. {ECO:0000269|PubMed:12169693}. +Q61124 CLN3_MOUSE Battenin (Protein CLN3) 438 47,657 Chain (1); Glycosylation (3); Lipidation (1); Modified residue (2); Propeptide (1); Sequence conflict (5); Topological domain (7); Transmembrane (6) TRANSMEM 38 58 Helical. {ECO:0000255}.; TRANSMEM 128 148 Helical. {ECO:0000255}.; TRANSMEM 152 172 Helical. {ECO:0000255}.; TRANSMEM 183 203 Helical. {ECO:0000255}.; TRANSMEM 278 298 Helical. {ECO:0000255}.; TRANSMEM 347 367 Helical. {ECO:0000255}. TOPO_DOM 1 37 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 59 127 Lumenal. {ECO:0000255}.; TOPO_DOM 149 151 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 173 182 Lumenal. {ECO:0000255}.; TOPO_DOM 204 277 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 299 346 Lumenal. {ECO:0000255}.; TOPO_DOM 368 438 Cytoplasmic. {ECO:0000255}. FUNCTION: Involved in microtubule-dependent, anterograde transport of late endosomes and lysosomes. {ECO:0000250|UniProtKB:Q13286}. PTM: Highly glycosylated. {ECO:0000250|UniProtKB:Q13286}.; PTM: Farnesylation is important for trafficking to lysosomes. {ECO:0000250|UniProtKB:Q13286}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q13286}; Multi-pass membrane protein {ECO:0000255}. Late endosome {ECO:0000250|UniProtKB:Q13286}. Lysosome {ECO:0000269|PubMed:19941651}. SUBUNIT: Interacts with DCTN1, KIF3A, RAB7A and RILP (By similarity). Interacts with CLN5 (PubMed:19941651). {ECO:0000250|UniProtKB:Q13286, ECO:0000269|PubMed:19941651}. +Q3UMW8 CLN5_MOUSE Ceroid-lipofuscinosis neuronal protein 5 homolog (Protein CLN5) [Cleaved into: Ceroid-lipofuscinosis neuronal protein 5 homolog, secreted form] 341 39,329 Chain (2); Glycosylation (7); Region (1); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 14 30 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 13 Cytoplasmic. {ECO:0000250|UniProtKB:O75503}.; TOPO_DOM 31 341 Lumenal. {ECO:0000250|UniProtKB:O75503}. FUNCTION: Plays a role in influencing the retrograde trafficking of lysosomal sorting receptors SORT1 and IGF2R from the endosomes to the trans-Golgi network by controlling the recruitment of retromer complex to the endosomal membrane. Regulates the localization and activation of RAB7A which is required to recruit the retromer complex to the endosomal membrane. {ECO:0000250|UniProtKB:O75503}. PTM: N-glycosylated with both high mannose and complex type sugars. Glycosylation is important for proper folding and trafficking to the lysosomes. {ECO:0000250|UniProtKB:O75503}.; PTM: Ceroid-lipofuscinosis neuronal protein 5 homolog: The type II membrane signal anchor is proteolytically cleaved to produce a mature form that is transported to the lysosomes (Ceroid-lipofuscinosis neuronal protein 5 homolog, secreted form). {ECO:0000250|UniProtKB:O75503}.; PTM: Can undergo proteolytic cleavage at the C-terminus, probably by a cysteine protease and may involve the removal of approximately 10-15 residues from the C-terminal end (PubMed:26342652). {ECO:0000269|PubMed:26342652}. SUBCELLULAR LOCATION: Ceroid-lipofuscinosis neuronal protein 5 homolog, secreted form: Lysosome {ECO:0000269|PubMed:20052765}.; SUBCELLULAR LOCATION: Ceroid-lipofuscinosis neuronal protein 5 homolog: Membrane {ECO:0000250|UniProtKB:O75503}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:O75503}. Note=An amphipathic anchor region facilitates its association with the membrane. {ECO:0000250|UniProtKB:O75503}. SUBUNIT: Interacts with PPT1, TPP1, CLN3, CLN6, CLN8, ATP5F1A and ATP5F1B (PubMed:19941651). Interacts with SORT1, RAB5A and RAB7A (By similarity). {ECO:0000250|UniProtKB:O75503, ECO:0000269|PubMed:19941651}. TISSUE SPECIFICITY: Heart, kidney, liver, spleen, muscle and rectum (at protein level). {ECO:0000269|PubMed:26342652}. +Q9QUK3 CLN8_MOUSE Protein CLN8 288 33,109 Chain (1); Domain (1); Motif (1); Transmembrane (5) TRANSMEM 26 46 Helical. {ECO:0000255}.; TRANSMEM 71 91 Helical. {ECO:0000255}.; TRANSMEM 103 123 Helical. {ECO:0000255}.; TRANSMEM 131 151 Helical. {ECO:0000255}.; TRANSMEM 225 245 Helical. {ECO:0000255}. FUNCTION: Could play a role in cell proliferation during neuronal differentiation and in protection against cell death. {ECO:0000250|UniProtKB:Q9UBY8}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9UBY8}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q9UBY8}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum {ECO:0000269|PubMed:19941651}. SUBUNIT: Interacts with CLN5 (PubMed:19941651). {ECO:0000269|PubMed:19941651}. DISEASE: Note=Defects in Cln8 are the cause of the phenotype motor neuron degeneration (mnd). Mnd is a naturally occurring mutant It is characterized by progressive motor system degeneration. It has intracellular autofluorescent inclusions similar to those seen in human Cln8. {ECO:0000269|PubMed:10508524}. +Q9QZE2 CLNK_MOUSE Cytokine-dependent hematopoietic cell linker (Mast cell immunoreceptor signal transducer) 435 49,492 Alternative sequence (1); Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (1); Modified residue (2); Mutagenesis (6); Region (2); Sequence conflict (5) FUNCTION: Plays a role in the regulation of immunoreceptor signaling, including PLC-gamma-mediated B-cell antigen receptor (BCR) signaling and FC-epsilon R1-mediated mast cell degranulation. Involved in phosphorylation of LAT. {ECO:0000269|PubMed:10562326, ECO:0000269|PubMed:10744659, ECO:0000269|PubMed:11463797}. PTM: Tyrosine-phosphorylated upon BCR cross-linking. Tyrosine phosphorylation at both Tyr-69 and Tyr-96 are required for BCR-induced calcium response and are essential to restore PLCG2-mediated signaling in BLNK-deficient DT40 cells, but this phosphorylation is dispensable in cells expressing LAT. Interacts with the SH2 domain of PLCG1 via phosphorylated Tyr-96. {ECO:0000269|PubMed:10744659, ECO:0000269|PubMed:11463797}. SUBUNIT: When phosphorylated, interacts with PLCG1, PLCG2, GRB2, VAV and LAT. Associated with a tyrosine-phosphorylated polypeptide (p92) in response to immunoreceptor stimulation. {ECO:0000269|PubMed:10562326, ECO:0000269|PubMed:10744659, ECO:0000269|PubMed:11463797}. DOMAIN: The N-terminal proline-rich region interacts with the SH3 domain of PLCG1. {ECO:0000269|PubMed:11463797}.; DOMAIN: The SH2 domain is important for restoration of BCR-induced calcium response and JNK2 activation in BLNK-deficient DT40 cells expressing LAT. {ECO:0000269|PubMed:11463797}. TISSUE SPECIFICITY: Expressed in mast cells of the skin (at protein level). Expressed in cytokine-stimulated hemopoietic cells. {ECO:0000269|PubMed:10562326, ECO:0000269|PubMed:10744659}. +Q8BXA5 CLP1L_MOUSE Cleft lip and palate transmembrane protein 1-like protein (CLPTM1-like protein) 539 62,183 Chain (1); Erroneous initiation (1); Frameshift (1); Glycosylation (2); Sequence conflict (1); Topological domain (6); Transmembrane (5) TRANSMEM 11 31 Helical. {ECO:0000255}.; TRANSMEM 286 306 Helical. {ECO:0000255}.; TRANSMEM 326 342 Helical. {ECO:0000255}.; TRANSMEM 404 424 Helical. {ECO:0000255}.; TRANSMEM 430 450 Helical. {ECO:0000255}. TOPO_DOM 1 10 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 32 285 Extracellular. {ECO:0000255}.; TOPO_DOM 307 325 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 343 403 Extracellular. {ECO:0000255}.; TOPO_DOM 425 429 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 451 539 Extracellular. {ECO:0000255}. FUNCTION: Enhances cisplatin-mediated apoptosis, when overexpressed. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +O88696 CLPP_MOUSE ATP-dependent Clp protease proteolytic subunit, mitochondrial (EC 3.4.21.92) (Endopeptidase Clp) 272 29,800 Active site (2); Chain (1); Modified residue (2); Transit peptide (1) FUNCTION: Protease component of the Clp complex that cleaves peptides and various proteins in an ATP-dependent process. Has low peptidase activity in the absence of CLPX. The Clp complex can degrade CSN1S1, CSN2 and CSN3, as well as synthetic peptides (in vitro) and may be responsible for a fairly general and central housekeeping function rather than for the degradation of specific substrates (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:10754102, ECO:0000269|PubMed:22710082}. SUBUNIT: Fourteen CLPP subunits assemble into 2 heptameric rings which stack back to back to give a disk-like structure with a central cavity. Component of the Clp complex formed by the assembly of two CLPP heptameric rings with two CLPX hexameric rings, giving rise to a symmetrical structure with two central CLPP rings flanked by a CLPX ring at either end of the complex. {ECO:0000269|PubMed:22710082}. TISSUE SPECIFICITY: Detected in liver (at protein level). High levels found in heart, liver and skeletal muscle. {ECO:0000269|PubMed:10754102, ECO:0000269|PubMed:22710082}. +Q80YR7 CLSPN_MOUSE Claspin 1315 146,715 Chain (1); Coiled coil (3); Modified residue (30); Repeat (3); Sequence conflict (2) FUNCTION: Required for checkpoint mediated cell cycle arrest in response to inhibition of DNA replication or to DNA damage induced by both ionizing and UV irradiation. Adapter protein which binds to BRCA1 and the checkpoint kinase CHEK1 and facilitates the ATR-dependent phosphorylation of both proteins. Can also bind specifically to branched DNA structures and may associate with S-phase chromatin following formation of the pre-replication complex (pre-RC). This may indicate a role for this protein as a sensor which monitors the integrity of DNA replication forks (By similarity). {ECO:0000250}. PTM: Phosphorylated. Undergoes ATR-dependent phosphorylation by CHEK1 during activation of DNA replication or damage checkpoints. Phosphorylation by CSNK1G1/CK1 promotes CHEK1 binding (By similarity). {ECO:0000250}.; PTM: Ubiquitinated by the anaphase promoting complex/cyclosome (APC/C) during G1 phase, leading to its degradation by the proteasome. Ubiquitination is mediated via its interaction with FZR1/CDH1. Following DNA damage, it is deubiquitinated by USP28 in G2 phase, preventing its degradation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}. SUBUNIT: Interacts (phosphorylation-dependent) with CHEK1; regulates CLSPN function in checkpoint for DNA damage and replication. Interacts with ATR and RAD9A and these interactions are slightly reduced during checkpoint activation. Interacts with BRCA1 and this interaction increases during checkpoint activation. Interacts with TIMELESS (By similarity). {ECO:0000250}. DOMAIN: The C-terminus of the protein contains 3 potential CHEK1-binding motifs (CKB motifs). Potential phosphorylation sites within CKB motif 1 and CKB motif 2 are required for interaction with CHEK1 (By similarity). {ECO:0000250}. +Q920A1 CLTR2_MOUSE Cysteinyl leukotriene receptor 2 (CysLTR2) 309 35,213 Chain (1); Disulfide bond (1); Glycosylation (1); Sequence conflict (1); Topological domain (8); Transmembrane (7) TRANSMEM 27 47 Helical; Name=1. {ECO:0000255}.; TRANSMEM 57 77 Helical; Name=2. {ECO:0000255}.; TRANSMEM 99 119 Helical; Name=3. {ECO:0000255}.; TRANSMEM 139 159 Helical; Name=4. {ECO:0000255}.; TRANSMEM 188 208 Helical; Name=5. {ECO:0000255}.; TRANSMEM 230 250 Helical; Name=6. {ECO:0000255}.; TRANSMEM 272 292 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 26 Extracellular. {ECO:0000255}.; TOPO_DOM 48 56 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 78 98 Extracellular. {ECO:0000255}.; TOPO_DOM 120 138 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 160 187 Extracellular. {ECO:0000255}.; TOPO_DOM 209 229 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 251 271 Extracellular. {ECO:0000255}.; TOPO_DOM 293 309 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for cysteinyl leukotrienes. The response is mediated via a G-protein that activates a phosphatidylinositol-calcium second messenger system. The rank order of affinities for the leukotrienes is LTC4 = LTD4 >> LTE4. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Widely expressed at low levels, with highest expression in the spleen, thymus and adrenal gland, and lower in the kidney, brain and peripheral blood leukocytes. +Q9ESG4 CLTRN_MOUSE Collectrin (Transmembrane protein 27) 222 25,070 Chain (1); Glycosylation (2); Modified residue (2); Sequence conflict (1); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 142 162 Helical. {ECO:0000255}. TOPO_DOM 15 141 Extracellular. {ECO:0000250|UniProtKB:Q9HBJ8}.; TOPO_DOM 163 222 Cytoplasmic. {ECO:0000250|UniProtKB:Q9HBJ8}. FUNCTION: Plays an important role in amino acid transport by acting as binding partner of amino acid transporters SLC6A18 and SLC6A19, regulating their trafficking on the cell surface and their activity (PubMed:17167413). Regulator of SNARE complex function (PubMed:16330323). Stimulator of beta cell replication (PubMed:16330324). {ECO:0000269|PubMed:16330323, ECO:0000269|PubMed:16330324, ECO:0000269|PubMed:17167413}. PTM: Glycosylated. Glycosylation is required for plasma membrane localization and for its cleavage by BACE2. {ECO:0000250|UniProtKB:Q9HBJ8}.; PTM: Proteolytically processed in pancreatic beta cells by BACE2 leading to the generation and extracellular release of soluble CLTRN, and a corresponding cell-associated C-terminal fragment which is later cleaved by gamma-secretase (PubMed:16330324, PubMed:21907142). This shedding process inactivates CLTRN (PubMed:16330324). Three cleavage sites have been identified for BACE2, two clustered sites after Phe-116 and Leu-118 and a more membrane proximal site at Phe-125; the preferred BACE2 cleavage site seems to be between Phe-125 and Leu-126, Phe-116 and Leu-118 act as alternative sites (By similarity). {ECO:0000250|UniProtKB:Q9HBJ8, ECO:0000269|PubMed:16330324, ECO:0000269|PubMed:21907142}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16330324, ECO:0000269|PubMed:17167413}; Single-pass type I membrane protein {ECO:0000255}. Note=Localizes to the brush border membranes of cells in the proximal tubules of kidney (PubMed:17167413). Colocalizes with SLC6A19 in the early proximal S1 tubule (PubMed:17167413). {ECO:0000269|PubMed:17167413}. SUBUNIT: Monomer (PubMed:16330324). Homodimer (PubMed:16330324). Homodimer; dimerization prevents CLTRN cleavage by BACE2 (PubMed:16330324). Interacts with SNAPIN (PubMed:16330323). Interacts with SLC6A18; this interaction regulates the trafficking of SLC6A18 to the cell membrane and its amino acid transporter activity (PubMed:17167413, PubMed:19478081). Interacts with SLC6A19; this interaction regulates the trafficking of SLC6A19 to the cell membrane and its amino acid transporter activity (PubMed:17167413). Interacts with SLC6A20B (PubMed:17167413). {ECO:0000269|PubMed:16330323, ECO:0000269|PubMed:16330324, ECO:0000269|PubMed:17167413, ECO:0000269|PubMed:19478081}. DOMAIN: The cleavage site containing the double Phe-Phe motif acts as negative regulator of shedding by BACE2. {ECO:0000250|UniProtKB:Q9HBJ8}. TISSUE SPECIFICITY: Kidney; collecting ducts and proximal tubule (PubMed:17167413, PubMed:11278314). Pancreas; beta cells of islets (PubMed:16330323, PubMed:16330324). {ECO:0000269|PubMed:11278314, ECO:0000269|PubMed:16330323, ECO:0000269|PubMed:16330324, ECO:0000269|PubMed:17167413}. +Q8R3P7 CLUA1_MOUSE Clusterin-associated protein 1 413 47,953 Chain (1); Coiled coil (1); Compositional bias (1); Modified residue (4) FUNCTION: Required for cilia biogenesis. Appears to function within the multiple intraflagellar transport complex B (IFT-B). Key regulator of hedgehog signaling. {ECO:0000269|PubMed:23351563}. SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000269|PubMed:23351563}. Nucleus {ECO:0000250|UniProtKB:Q96AJ1}. SUBUNIT: Interacts with CLU/clusterin. Interacts with UBXN10; the interaction is direct. {ECO:0000250|UniProtKB:Q96AJ1}. TISSUE SPECIFICITY: Expressed in all tissues tested including heart, kidney, skeletal muscle, eye, liver, ovary, oviduct, testes, lung and brain. Elevated levels in multiciliated cells such as the bronchioles of the lungs, ependymal cells of the brain and cells with a single primary cilia of heart and kidney. {ECO:0000269|PubMed:23351563}. +Q3ZRW6 CLUL1_MOUSE Clusterin-like protein 1 464 53,733 Chain (1); Coiled coil (1); Disulfide bond (5); Glycosylation (6); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q06890 CLUS_MOUSE Clusterin (Apolipoprotein J) (Apo-J) (Clustrin) (Sulfated glycoprotein 2) (SGP-2) [Cleaved into: Clusterin beta chain; Clusterin alpha chain] 448 51,656 Chain (3); Disulfide bond (5); Glycosylation (6); Modified residue (2); Motif (2); Mutagenesis (6); Sequence conflict (3); Signal peptide (1) FUNCTION: Functions as extracellular chaperone that prevents aggregation of nonnative proteins. Prevents stress-induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself. Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation. When secreted, protects cells against apoptosis and against cytolysis by complement. Intracellular forms interact with ubiquitin and SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes and promote the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes proteasomal degradation of COMMD1 and IKBKB. Modulates NF-kappa-B transcriptional activity. Promotes apoptosis when in the nucleus. Inhibits apoptosis when associated with the mitochondrial membrane by interference with BAX-dependent release of cytochrome c into the cytoplasm. Plays a role in the regulation of cell proliferation (By similarity). {ECO:0000250}. PTM: Extensively glycosylated with sulfated N-linked carbohydrates. {ECO:0000269|PubMed:16944957, ECO:0000269|PubMed:17330941}.; PTM: Proteolytically cleaved on its way through the secretory system, probably within the Golgi lumen. {ECO:0000250}.; PTM: Polyubiquitinated, leading to proteasomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12551933}. Nucleus {ECO:0000269|PubMed:12551933}. Cytoplasm {ECO:0000269|PubMed:12551933}. Mitochondrion membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, cytosol {ECO:0000269|PubMed:12551933}. Microsome {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle, chromaffin granule {ECO:0000250}. Note=Can retrotranslocate from the secretory compartments to the cytosol upon cellular stress. Detected in perinuclear foci that may be aggresomes containing misfolded, ubiquitinated proteins. Detected at the mitochondrion membrane upon induction of apoptosis (By similarity). {ECO:0000250}. SUBUNIT: Antiparallel disulfide-linked heterodimer of an alpha chain and a beta chain. Self-associates and forms higher oligomers. Interacts with a broad range of misfolded proteins, including APP, APOC2 and LYZ. Slightly acidic pH promotes interaction with misfolded proteins. Forms high-molecular weight oligomers upon interaction with misfolded proteins. Interacts with APOA1, LRP2, CLUAP1 AND PON1. Interacts with the complement complex. Interacts with SYVN1, COMMD1, BTRC, CUL1 and with ubiquitin and SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes. Interacts (via alpha chain) with BAX in stressed cells, where BAX undergoes a conformation change leading to association with the mitochondrial membrane. Does not interact with BAX in unstressed cells (By similarity). Interacts (via alpha chain) with XRCC6. Found in a complex with LTF, CLU, EPPIN and SEMG1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Most abundant in stomach, liver, brain, and testis, with intermediate levels in heart, ovary and kidney. +Q5SW19 CLU_MOUSE Clustered mitochondria protein homolog 1315 148,068 Alternative sequence (3); Chain (1); Domain (1); Erroneous gene model prediction (2); Erroneous initiation (5); Modified residue (4); Repeat (4); Sequence conflict (4) FUNCTION: mRNA-binding protein involved in proper cytoplasmic distribution of mitochondria. Specifically binds mRNAs of nuclear-encoded mitochondrial proteins in the cytoplasm and regulates transport or translation of these transcripts close to mitochondria, playing a role in mitochondrial biogenesis. {ECO:0000255|HAMAP-Rule:MF_03013}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03013}. Cytoplasmic granule {ECO:0000255|HAMAP-Rule:MF_03013}. +Q8BG92 CLVS2_MOUSE Clavesin-2 (Retinaldehyde-binding protein 1-like 2) 327 37,954 Alternative sequence (2); Chain (1); Domain (1) FUNCTION: Required for normal morphology of late endosomes and/or lysosomes in neurons. Binds phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Early endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250}. SUBUNIT: Forms a complex with clathrin heavy chain and gamma-adaptin. {ECO:0000250}. DOMAIN: The CRAL-TRIO domain is required for targeting to the membrane and for binding PtdIns(3,5)P2. {ECO:0000250}. +P26339 CMGA_MOUSE Chromogranin-A (CgA) [Cleaved into: Pancreastatin; Beta-granin; WE-14; Catestatin; GE-25; Serpinin-RRG; Serpinin (AL26); p-Glu serpinin precursor] 463 51,789 Chain (1); Compositional bias (3); Disulfide bond (1); Mass spectrometry (5); Modified residue (13); Peptide (8); Signal peptide (1) FUNCTION: Pancreastatin: Strongly inhibits glucose induced insulin release from the pancreas.; FUNCTION: Catestatin: Inhibits catecholamine release from chromaffin cells and noradrenergic neurons by acting as a non-competitive nicotinic cholinergic antagonist. Can induce mast cell migration, degranulation and production of cytokines and chemokines. {ECO:0000250|UniProtKB:P10645}.; FUNCTION: Serpinin: Regulates granule biogenesis in endocrine cells by up-regulating the transcription of protease nexin 1 (SERPINE2) via a cAMP-PKA-SP1 pathway. This leads to inhibition of granule protein degradation in the Golgi complex which in turn promotes granule formation (PubMed:21436258). Pyroglutaminated (pGlu)-serpinin exerts an antiapoptotic effect on cells exposed to oxidative stress (PubMed:21537909). {ECO:0000269|PubMed:21436258, ECO:0000269|PubMed:21537909}. PTM: CgA is O-glycosylated. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:12388744}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000269|PubMed:12388744}. Secreted {ECO:0000269|PubMed:12388744}. Note=Associated with the secretory granule membrane through direct interaction to SCG3 that in turn binds to cholesterol-enriched lipid rafts in intragranular conditions.; SUBCELLULAR LOCATION: Serpinin: Secreted {ECO:0000269|PubMed:21436258, ECO:0000269|PubMed:21537909}. Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:21537909}. Note=Pyroglutaminated serpinin localizes to secretory vesicle. {ECO:0000269|PubMed:21537909}. SUBUNIT: Interacts with SCG3; this interaction is optimal in conditions mimicking the lumenal milieu of the trans-Golgi network, i.e. pH 5.5 and 10 mM Ca(+2). {ECO:0000269|PubMed:12388744}. +Q9QXS8 CMLO5_MOUSE Probable N-acetyltransferase CML5 (EC 2.3.1.-) (Camello-like protein 5) 227 25,735 Chain (1); Domain (1); Sequence conflict (4); Transmembrane (3) TRANSMEM 29 49 Helical. {ECO:0000255}.; TRANSMEM 53 73 Helical. {ECO:0000255}.; TRANSMEM 201 221 Helical. {ECO:0000255}. FUNCTION: May play a role in regulation of gastrulation. {ECO:0000269|PubMed:11397015}. SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. +Q3U5Q7 CMPK2_MOUSE UMP-CMP kinase 2, mitochondrial (EC 2.7.4.14) (Nucleoside-diphosphate kinase) (EC 2.7.4.6) (Thymidylate kinase LPS-inducible member) (TYKi) 447 50,036 Chain (1); Coiled coil (1); Erroneous initiation (7); Frameshift (1); Nucleotide binding (1); Sequence caution (1); Sequence conflict (4); Transit peptide (1) FUNCTION: May participate in dUTP and dCTP synthesis in mitochondria. Is able to phosphorylate dUMP, dCMP, CMP, UMP and monophosphates of the pyrimidine nucleoside analogs ddC, dFdC, araC, BVDU and FdUrd with ATP as phosphate donor. Also displays broad nucleoside diphosphate kinase activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. +Q8BIG7 CMTD1_MOUSE Catechol O-methyltransferase domain-containing protein 1 (EC 2.1.1.-) 262 28,961 Binding site (8); Chain (1); Region (1); Transmembrane (1) TRANSMEM 12 32 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. FUNCTION: Putative O-methyltransferase. {ECO:0000305}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. SUBUNIT: Homodimer. {ECO:0000250}. +Q70KF4 CMYA5_MOUSE Cardiomyopathy-associated protein 5 (Heart and skeletal muscle-specific and sprouty domain-containing) (Myospryn) (Stretch-response protein 553) (Stretch-responsive fibronectin protein type 3) (TRIM-like protein) 3739 413,040 Chain (1); Coiled coil (3); Compositional bias (3); Domain (3); Modified residue (6); Mutagenesis (3); Region (6); Repeat (19); Sequence conflict (55) FUNCTION: May serve as an anchoring protein that mediates the subcellular compartmentation of protein kinase A (PKA) via binding to PRKAR2A. May attenuate calcineurin ability to induce slow-fiber gene program in muscle and may negatively modulate skeletal muscle regeneration. Plays a role in the assembly of ryanodine receptor (RYR2) clusters in striated muscle. {ECO:0000269|PubMed:17499862, ECO:0000269|PubMed:18252718, ECO:0000269|PubMed:21427212, ECO:0000269|PubMed:28740084}. PTM: Phosphorylated by PKA. {ECO:0000269|PubMed:17499862}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:A0A286XF80}. Cytoplasm. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:A0A286XF80}. Cytoplasm, myofibril, sarcomere, M line. Sarcoplasmic reticulum {ECO:0000250|UniProtKB:A0A286XF80}. Note=Found predominantly at the periphery of the nucleus but also throughout the cell. Localized in lysosomes. In skeletal muscles, localizes along myofiber periphery, at costameres. Predominantly flanks Z-disks (By similarity). Occasionally present at the M-band level. In the mdx mouse model for Duchenne muscular dystrophy, exhibits a discontinuous localization at the myofiber periphery with extensive regions devoid of CMYA5. This highly irregular pattern is associated with an increased cytoplasmic localization, particularly in discrete foci within myofibers. Colocalized with RYR2 in the sarcoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:A0A286XF80}. SUBUNIT: Interacts with PRKAR2A. Interacts with ACTN2, DES and DTNBP1/dysbindin. Interacts with DMD/dystrophin. Interacts with the calcineurin catalytic subunit PPP3CA. Interacts with TTN (By similarity). Interacts with CAPN3; this interaction, which results in CMYA5 proteolysis, may protect CAPN3 from autolysis (By similarity). Interacts with FSD2 (PubMed:28740084). In cardiac muscles, identified in a complex composed of FSD2, CMYA5 and RYR2 (PubMed:28740084). {ECO:0000250, ECO:0000269|PubMed:28740084}. DOMAIN: Amphipathic helix regions act as an anchoring domain for PKA, and appear to be responsible of the interaction between myospryn and PRKAR2A. TISSUE SPECIFICITY: Expressed in skin as well as in cardiac muscle. Expressed in skeletal muscle (at protein level). {ECO:0000269|PubMed:14688250, ECO:0000269|PubMed:16407236, ECO:0000269|PubMed:18252718, ECO:0000269|PubMed:28740084}. +Q4KL13 CN028_MOUSE Uncharacterized protein C14orf28 homolog 310 36,304 Chain (1) +P61249 CNCG_MOUSE Retinal cone rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma (GMP-PDE gamma) (EC 3.1.4.35) 83 9,028 Chain (1); Compositional bias (1); Sequence conflict (1) FUNCTION: Participates in processes of transmission and amplification of the visual signal. cGMP-PDEs are the effector molecules in G-protein-mediated phototransduction in vertebrate rods and cones. SUBUNIT: Tetramer composed of two catalytic chains (alpha and beta), and two inhibitory chains (gamma). DOMAIN: The C-terminal region is important in conferring inhibition. {ECO:0000250}. +Q8K2Z4 CND1_MOUSE Condensin complex subunit 1 (Chromosome condensation-related SMC-associated protein 1) (Chromosome-associated protein D2) (mCAP-D2) (Non-SMC condensin I complex subunit D2) (XCAP-D2 homolog) 1392 155,665 Alternative sequence (1); Chain (1); Erroneous initiation (1); Erroneous termination (1); Modified residue (14); Motif (1); Region (1); Sequence caution (1); Sequence conflict (3) FUNCTION: Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases. May target the condensin complex to DNA via its C-terminal domain. May promote the resolution of double-strand DNA catenanes (intertwines) between sister chromatids. Condensin-mediated compaction likely increases tension in catenated sister chromatids, providing directionality for type II topoisomerase-mediated strand exchanges toward chromatid decatenation. Required for decatenation of non-centromeric ultrafine DNA bridges during anaphase. Early in neurogenesis, may play an essential role to ensure accurate mitotic chromosome condensation in neuron stem cells, ultimately affecting neuron pool and cortex size. {ECO:0000250|UniProtKB:Q15021}. PTM: Phosphorylated by CDK1. Its phosphorylation, as well as that of NCAPH and NCAPG subunits, activates the condensin complex and is required for chromosome condensation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Chromosome {ECO:0000250}. Note=In interphase cells, the majority of the condensin complex is found in the cytoplasm, while a minority of the complex is associated with chromatin. A subpopulation of the complex however remains associated with chromosome foci in interphase cells. During mitosis, most of the condensin complex is associated with the chromatin. At the onset of prophase, the regulatory subunits of the complex are phosphorylated by CDK1, leading to condensin's association with chromosome arms and to chromosome condensation. Dissociation from chromosomes is observed in late telophase (By similarity). {ECO:0000250}. SUBUNIT: Component of the condensin complex, which contains the SMC2 and SMC4 heterodimer, and three non SMC subunits that probably regulate the complex: NCAPH/BRRN1, NCAPD2/CAPD2 and NCAPG. Interacts with histones H1 and H3 (By similarity). {ECO:0000250}. DOMAIN: The C-terminal domain interacts with histones H1 and H3, and may be responsible for condensin complex targeting to mitotic chromosomes. This domain is independent from the bipartite nuclear localization signal, although they are contained within the same region (By similarity). {ECO:0000250}. +Q8BSP2 CNDH2_MOUSE Condensin-2 complex subunit H2 (Kleisin-beta) (Non-SMC condensin II complex subunit H2) 607 68,945 Alternative sequence (2); Chain (1); Erroneous initiation (1); Modified residue (6); Natural variant (1); Sequence conflict (3) FUNCTION: Regulatory subunit of the condensin-2 complex, a complex that seems to provide chromosomes with an additional level of organization and rigidity and in establishing mitotic chromosome architecture (By similarity). May promote the resolution of double-strand DNA catenanes (intertwines) between sister chromatids. Condensin-mediated compaction likely increases tension in catenated sister chromatids, providing directionality for type II topoisomerase-mediated strand exchanges toward chromatid decatenation. Required for decatenation of chromatin bridges at anaphase. Early in neurogenesis, may play an essential role to ensure accurate mitotic chromosome condensation in neuron stem cells, ultimately affecting neuron pool and cortex size (PubMed:27737959). Seems to have lineage-specific role in T-cell development (By similarity). {ECO:0000250|UniProtKB:Q6IBW4, ECO:0000269|PubMed:27737959}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: Component of the condensin-2 complex, which contains the SMC2 and SMC4 heterodimer, and three non SMC subunits, NCAPG2, NCAPH2 and NCAPD3 that probably regulate the complex. {ECO:0000250}. DISEASE: Note=Defects in Ncaph2 are the cause of the nessy phenotype which is characterized by a specific defect in T-cell development. Nessy thymuses are smaller, with corticomedullary junctions less well defined, and cortical cells sparser than in wild-type. The thymocyte defect is typified by an increased proportion of CD4-CD8- DN T-cell progenitors. Only thymocyte differentiation is affected in Nessy mice and not cell differentiation. +Q6ZWS4 CNIH3_MOUSE Protein cornichon homolog 3 (CNIH-3) (Cornichon family AMPA receptor auxiliary protein 3) 160 18,976 Chain (1); Topological domain (4); Transmembrane (3) TRANSMEM 11 31 Helical. {ECO:0000255}.; TRANSMEM 73 93 Helical. {ECO:0000255}.; TRANSMEM 139 159 Helical. {ECO:0000255}. TOPO_DOM 1 10 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 32 72 Lumenal. {ECO:0000255}.; TOPO_DOM 94 138 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 160 160 Lumenal. {ECO:0000255}. FUNCTION: Regulates the trafficking and gating properties of AMPA-selective glutamate receptors (AMPARs). Promotes their targeting to the cell membrane and synapses and modulates their gating properties by regulating their rates of activation, deactivation and desensitization (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Also localizes to the cell membrane of extrasynaptic sites (dendritic shafts, spines of pyramidal cells). {ECO:0000250}. SUBUNIT: Acts as an auxiliary subunit for AMPA-selective glutamate receptors (AMPARs). Found in a complex with GRIA1, GRIA2, GRIA3, GRIA4, CNIH2, CACNG2, CACNG3, CACNG4, CACNG5, CACNG7 and CACNG8 (By similarity). {ECO:0000250}. +Q80YA9 CNKR2_MOUSE Connector enhancer of kinase suppressor of ras 2 (Connector enhancer of KSR 2) (CNK homolog protein 2) (CNK2) 1032 117,396 Alternative sequence (1); Chain (1); Coiled coil (1); Compositional bias (3); Domain (5); Erroneous initiation (1); Modified residue (9) FUNCTION: May function as an adapter protein or regulator of Ras signaling pathways. PTM: Phosphorylated on tyrosine. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. SUBUNIT: Interacts with RAF1, RAB2L and RAL GTPase proteins. {ECO:0000250}. +Q08091 CNN1_MOUSE Calponin-1 (Basic calponin) (Calponin H1, smooth muscle) 297 33,356 Alternative sequence (1); Chain (1); Domain (1); Modified residue (5); Repeat (3); Sequence conflict (2) FUNCTION: Thin filament-associated protein that is implicated in the regulation and modulation of smooth muscle contraction. It is capable of binding to actin, calmodulin, troponin C and tropomyosin. The interaction of calponin with actin inhibits the actomyosin Mg-ATPase activity. SUBUNIT: Part of cGMP kinase signaling complex at least composed of ACTA2/alpha-actin, CNN1/calponin H1, PLN/phospholamban, PRKG1 and ITPR1. {ECO:0000250}. TISSUE SPECIFICITY: Smooth muscle, and tissues containing significant amounts of smooth muscle. +Q9CWN7 CNO11_MOUSE CCR4-NOT transcription complex subunit 11 505 54,959 Chain (1); Compositional bias (1); Modified residue (1) FUNCTION: Component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. Additional complex functions may be a consequence of its influence on mRNA expression. Is required for the association of CNOT10 with the CCR4-NOT complex. Seems not to be required for complex deadenylase function (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Component of the CCR4-NOT complex; distinct complexes seem to exist that differ in the participation of probably mutually exclusive catalytic subunits. CNOT10 and CNOT11 form a subcomplex docke to the CNOT1 scaffold (By similarity). {ECO:0000250}. +Q8VEG6 CNO6L_MOUSE CCR4-NOT transcription complex subunit 6-like (EC 3.1.13.4) 555 63,023 Active site (3); Alternative sequence (3); Chain (1); Frameshift (1); Metal binding (4); Region (2); Repeat (4); Sequence conflict (1) FUNCTION: Poly(A) nuclease with 3'-5' RNase activity. Catalytic component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. Additional complex functions may be a consequence of its influence on mRNA expression. Involved in mRNA decay mediated by the major-protein-coding determinant of instability (mCRD) of the FOS gene in the cytoplasm. Involved in deadenylation-dependent degradation of CDKN1B mRNA. Its mRNA deadenylase activity can be inhibited by TOB1. Mediates cell proliferation and cell survival and prevents cellular senescence (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Component of the CCR4-NOT complex; distinct complexes seem to exist that differ in the participation of probably mutually exclusive catalytic subunits; the complex contains two deadenylase subunits, CNOT6 or CNOT6L, and CNOT7 or CNOT8 (By similarity). Interacts with CNOT1, CNOT3, CNOT7, CNOT8 and CNOT9 (By similarity). Interacts with TOB1 (By similarity). Interacts with NANOS2 (PubMed:20133598). Interacts with ZFP36 (PubMed:21078877). {ECO:0000250|UniProtKB:Q96LI5, ECO:0000269|PubMed:20133598, ECO:0000269|PubMed:21078877}. +Q8C5L3 CNOT2_MOUSE CCR4-NOT transcription complex subunit 2 (CCR4-associated factor 2) 540 59,711 Alternative sequence (2); Chain (1); Frameshift (1); Modified residue (7); Sequence conflict (2) FUNCTION: Component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. Additional complex functions may be a consequence of its influence on mRNA expression. Required for the CCR4-NOT complex structural integrity. Can repress transcription and may link the CCR4-NOT complex to transcriptional regulation; the repressive function may specifically involve the N-Cor repressor complex containing HDAC3, NCOR1 and NCOR2. Involved in the maintenance of emryonic stem (ES) cell identity; prevents their differentiation towards extraembryonic trophectoderm lineages. {ECO:0000269|PubMed:22367759}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000305}. SUBUNIT: Component of the CCR4-NOT complex; distinct complexes seem to exist that differ in the participation of probably mutually exclusive catalytic subunits. In the complex interacts directly with CNOT3. Interacts with NCOR1, NCOR2. HDAC3 and GPS2 (By similarity). {ECO:0000250}. +Q60809 CNOT7_MOUSE CCR4-NOT transcription complex subunit 7 (EC 3.1.13.4) (CCR4-associated factor 1) (CAF-1) 285 32,718 Chain (1); Metal binding (6) FUNCTION: Has 3'-5' poly(A) exoribonuclease activity for synthetic poly(A) RNA substrate. Its function seems to be partially redundant with that of CNOT8. Catalytic component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. During miRNA-mediated repression the complex seems also to act as translational repressor during translational initiation. Additional complex functions may be a consequence of its influence on mRNA expression. Required for miRNA-mediated mRNA deadenylation. Associates with members of the BTG family such as TOB1 and BTG2 and is required for their anti-proliferative activity. {ECO:0000269|PubMed:19716330, ECO:0000269|PubMed:22367759}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20133598}. Cytoplasm, P-body {ECO:0000269|PubMed:20133598}. Note=NANOS2 promotes its localization to P-body. SUBUNIT: Component of the CCR4-NOT complex; distinct complexes seem to exist that differ in the participation of probably mutually exclusive catalytic subunits; the complex contains two deadenylase subunits, CNOT6 or CNOT6L, and CNOT7 or CNOT8 (By similarity). In the complex, interacts directly with CNOT1 (By similarity). Interacts with AGO2 (PubMed:19716330). Interacts with TOB1; recruited by TOB1 to a ternary complex with CPEB3 which is required for mRNA deadenylation and decay (By similarity). Interacts with BTG1 (PubMed:9712883). Interacts with BTG2 (PubMed:9712883). Interacts with NANOS2 (PubMed:20133598). Interacts with ZFP36, ZFP36L1 and ZFP36L2; these interactions are inhibited in response to phorbol 12-myristate 13-acetate (PMA) treatment in a p38 MAPK-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q9UIV1, ECO:0000269|PubMed:19716330, ECO:0000269|PubMed:20133598, ECO:0000269|PubMed:9712883}. +Q9D8X5 CNOT8_MOUSE CCR4-NOT transcription complex subunit 8 (EC 3.1.13.4) (CCR4-associated factor 8) 292 33,574 Chain (1); Metal binding (5) FUNCTION: Has 3'-5' poly(A) exoribonuclease activity for synthetic poly(A) RNA substrate. Its function seems to be partially redundant with that of CNOT7. Catalytic component of the CCR4-NOT complex which is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. During miRNA-mediated repression the complex seems also to act as translational repressor during translational initiation. Additional complex functions may be a consequence of its influence on mRNA expression. Associates with members of the BTG family such as TOB1 and BTG2 and is required for their anti-proliferative activity. {ECO:0000269|PubMed:22367759}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Component of the CCR4-NOT complex; distinct complexes seem to exist that differ in the participation of probably mutually exclusive catalytic subunits; the complex contains two deadenylase subunits, CNOT6 or CNOT6L, and CNOT7 or CNOT8. In the complex interacts directly with CNOT1. Interacts with BTG1, BTG2 and TOB1 (By similarity). {ECO:0000250}. +Q9JKY0 CNOT9_MOUSE CCR4-NOT transcription complex subunit 9 (Cell differentiation protein RQCD1 homolog) (Rcd-1) (EPO-induced protein FL10) 299 33,601 Chain (1); Modified residue (1) FUNCTION: Component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. Additional complex functions may be a consequence of its influence on mRNA expression. Involved in down-regulation of MYB- and JUN-dependent transcription. May play a role in cell differentiation. Required for retinoic acid-induced differentiation of F9 teratocarcinoma cells. Does not bind DNA by itself. Enhances ligand-dependent transcriptional activity of nuclear hormone receptors. May play a role in cell differentiation. {ECO:0000269|PubMed:12356739, ECO:0000269|PubMed:15209511}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15209511}. Cytoplasm, P-body {ECO:0000269|PubMed:20133598}. Note=NANOS2 promotes its localization to P-body. {ECO:0000269|PubMed:20133598}. SUBUNIT: Homodimer. Component of the CCR4-NOT complex; distinct complexes seem to exist that differ in the participation of probably mutually exclusive catalytic subunits. Interacts with MYB, ATF2, RARA, RARB, RARG, RXRA, RXRB and RXRG. Identified in a complex with ATF2 bound to target DNA. Interacts with NANOS2. Directly interacts with ZNF335 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Detected at low levels in bone marrow and thymus. {ECO:0000269|PubMed:10880228}. +Q8K158 CNPD1_MOUSE Protein CNPPD1 407 44,915 Chain (1); Compositional bias (1); Transmembrane (1) TRANSMEM 233 253 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q8BQ47 CNPY4_MOUSE Protein canopy homolog 4 (Protein associated with Tlr4) 245 28,094 Chain (1); Coiled coil (1); Disulfide bond (3); Frameshift (2); Sequence conflict (3); Signal peptide (1) FUNCTION: Plays a role in the regulation of the cell surface expression of TLR4. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. SUBUNIT: Interacts with TLR4. {ECO:0000269|PubMed:16338228}. TISSUE SPECIFICITY: Highly expressed in lung, spleen, thymus, and uterus. Moderately expressed in kidney, stomach and placenta. Weakly expressed in brain, heart, liver, small intestine, skeletal muscle and testis. {ECO:0000269|PubMed:16338228}. +Q5M8N0 CNRP1_MOUSE CB1 cannabinoid receptor-interacting protein 1 (CRIP-1) 164 18,612 Chain (1); Sequence conflict (1) FUNCTION: Suppresses cannabinoid receptor CNR1-mediated tonic inhibition of voltage-gated calcium channels. {ECO:0000250}. SUBUNIT: Interacts with the cannabinoid receptor CNR1 (via C-terminus). Does not interact with cannabinoid receptor CNR2 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in brain. Also detected in heart, lung, intestine, kidney, testis, spleen, liver and muscle (at protein level). {ECO:0000269|PubMed:17895407}. +Q9D3D9 ATPD_MOUSE ATP synthase subunit delta, mitochondrial (ATP synthase F1 subunit delta) (F-ATPase delta subunit) 168 17,600 Chain (1); Modified residue (4); Transit peptide (1) FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP turnover in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane. SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) seems to have nine subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L). Component of an ATP synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MD and MP68 (By similarity). {ECO:0000250}. +Q9D995 CNTD1_MOUSE Cyclin N-terminal domain-containing protein 1 334 37,222 Chain (1); Domain (1); Sequence caution (1); Sequence conflict (2) +O88507 CNTFR_MOUSE Ciliary neurotrophic factor receptor subunit alpha (CNTF receptor subunit alpha) (CNTFR-alpha) 372 40,801 Chain (1); Disulfide bond (1); Domain (3); Glycosylation (4); Lipidation (1); Motif (1); Propeptide (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Binds to CNTF. The alpha subunit provides the receptor specificity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. SUBUNIT: Heterotrimer of the alpha subunit, LIFR and IL6ST. {ECO:0000250}. DOMAIN: The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding. {ECO:0000250}. +Q69Z26 CNTN4_MOUSE Contactin-4 (Brain-derived immunoglobulin superfamily protein 2) (BIG-2) 1026 113,490 Alternative sequence (4); Beta strand (24); Chain (1); Disulfide bond (6); Domain (10); Glycosylation (13); Helix (2); Lipidation (1); Propeptide (1); Sequence conflict (16); Signal peptide (1) FUNCTION: Contactins mediate cell surface interactions during nervous system development. Has some neurite outgrowth-promoting activity. May be involved in synaptogenesis. {ECO:0000269|PubMed:9733924}. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. Secreted {ECO:0000250}. SUBUNIT: Interacts with PTPRG. {ECO:0000269|PubMed:20133774}. TISSUE SPECIFICITY: Expressed in the region of developing olfactory neurons. Isoform 2 is expressed in mature sensory cells of the vomeronasal neuroepithelium and at lower level in olfactory neuroepithelium. {ECO:0000269|PubMed:9733924}. +O54991 CNTP1_MOUSE Contactin-associated protein 1 (Caspr) (Caspr1) (MHDNIV) (NCP1) (Neurexin IV) (Neurexin-4) (Paranodin) 1385 156,312 Chain (1); Disulfide bond (11); Domain (8); Glycosylation (17); Modified residue (1); Motif (1); Sequence conflict (7); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1285 1305 Helical. {ECO:0000255}. TOPO_DOM 21 1284 Extracellular. {ECO:0000255}.; TOPO_DOM 1306 1385 Cytoplasmic. {ECO:0000255}. FUNCTION: Required, with CNTNAP2, for radial and longitudinal organization of myelinated axons (PubMed:25378149). Plays a role in the formation of functional distinct domains critical for saltatory conduction of nerve impulses in myelinated nerve fibers. Demarcates the paranodal region of the axo-glial junction. In association with contactin involved in the signaling between axons and myelinating glial cells (PubMed:25378149, PubMed:11395000). {ECO:0000269|PubMed:11395000, ECO:0000269|PubMed:25378149}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Cell junction, paranodal septate junction {ECO:0000269|PubMed:25378149}. SUBUNIT: Interacts with CNTN1/contactin in cis form. {ECO:0000250|UniProtKB:P97846}. TISSUE SPECIFICITY: Expressed in brain. In myelinated nerve fibers predominantly found in paranodal axoglial junctions. In the internodal region of myelinated axons in the CNS and the PNS also found as a thin line apposing the inner mesaxon of the myelin sheath. In PNS neurons this line forms a circumferential ring that apposes the innermost aspect of Schmidt-Lanterman incisures. {ECO:0000269|PubMed:11512672, ECO:0000269|PubMed:25378149}. +Q8CB62 CNTRB_MOUSE Centrobin (Centrosomal BRCA2-interacting protein) (LYST-interacting protein 8) 887 99,404 Alternative sequence (1); Chain (1); Coiled coil (1); Compositional bias (1); Erroneous initiation (1); Modified residue (2); Region (1) FUNCTION: Required for centriole duplication. Inhibition of centriole duplication leading to defects in cytokinesis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250}. Note=Centriole-associated, asymmetrically localizes to the daughter centriole. {ECO:0000250}. SUBUNIT: Interacts with LYST. {ECO:0000250}. +Q9CRC3 CO040_MOUSE UPF0235 protein C15orf40 homolog 126 13,189 Chain (1); Modified residue (1); Sequence conflict (1) +Q01149 CO1A2_MOUSE Collagen alpha-2(I) chain (Alpha-2 type I collagen) 1372 129,557 Chain (1); Disulfide bond (3); Domain (1); Glycosylation (2); Metal binding (5); Modified residue (3); Propeptide (2); Sequence conflict (2); Signal peptide (1) FUNCTION: Type I collagen is a member of group I collagen (fibrillar forming collagen). PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}. SUBUNIT: Trimers of one alpha 2(I) and two alpha 1(I) chains. DOMAIN: The C-terminal propeptide, also known as COLFI domain, have crucial roles in tissue growth and repair by controlling both the intracellular assembly of procollagen molecules and the extracellular assembly of collagen fibrils. It binds a calcium ion which is essential for its function. {ECO:0000250}. TISSUE SPECIFICITY: Forms the fibrils of tendon, ligaments and bones. In bones the fibrils are mineralized with calcium hydroxyapatite. +P01027 CO3_MOUSE Complement C3 (HSE-MSF) [Cleaved into: Complement C3 beta chain; C3-beta-c (C3bc); Complement C3 alpha chain; C3a anaphylatoxin; Acylation stimulating protein (ASP) (C3adesArg); Complement C3b alpha' chain; Complement C3c alpha' chain fragment 1; Complement C3dg fragment; Complement C3g fragment; Complement C3d fragment; Complement C3f fragment; Complement C3c alpha' chain fragment 2] 1663 186,484 Alternative sequence (1); Chain (12); Cross-link (1); Disulfide bond (13); Domain (2); Glycosylation (2); Modified residue (5); Peptide (1); Region (1); Sequence conflict (4); Signal peptide (1); Site (5) FUNCTION: C3 plays a central role in the activation of the complement system. Its processing by C3 convertase is the central reaction in both classical and alternative complement pathways. After activation C3b can bind covalently, via its reactive thioester, to cell surface carbohydrates or immune aggregates.; FUNCTION: Derived from proteolytic degradation of complement C3, C3a anaphylatoxin is a mediator of local inflammatory process. In chronic inflammation, acts as a chemoattractant for neutrophils (By similarity). It induces the contraction of smooth muscle, increases vascular permeability and causes histamine release from mast cells and basophilic leukocytes. The short isoform has B-cell stimulatory activity. {ECO:0000250}.; FUNCTION: C3-beta-c: Acts as a chemoattractant for neutrophils in chronic inflammation. {ECO:0000250}.; FUNCTION: Acylation stimulating protein: adipogenic hormone that stimulates triglyceride (TG) synthesis and glucose transport in adipocytes, regulating fat storage and playing a role in postprandial TG clearance. Appears to stimulate TG synthesis via activation of the PLC, MAPK and AKT signaling pathways. Ligand for C5AR2. Promotes the phosphorylation, ARRB2-mediated internalization and recycling of C5AR2. PTM: C3b is rapidly split in two positions by factor I and a cofactor to form iC3b (inactivated C3b) and C3f which is released. Then iC3b is slowly cleaved (possibly by factor I) to form C3c (beta chain + alpha' chain fragment 1 + alpha' chain fragment 2), C3dg and C3f. Other proteases produce other fragments such as C3d or C3g. C3a is further processed by carboxypeptidases to release the C-terminal arginine residue generating the acylation stimulating protein (ASP). Levels of ASP are increased in adipocytes in the postprandial period and by dietary chylomicrons.; PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000250|UniProtKB:P01024}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: C3 precursor is first processed by the removal of 4 Arg residues, forming two chains, beta and alpha, linked by a disulfide bond. C3 convertase activates C3 by cleaving the alpha chain, releasing C3a anaphylatoxin and generating C3b (beta chain + alpha' chain). C3b interacts with CR1 (via Sushi 8 and Sushi 9 domains). C3b interacts with CFH. C3d interacts with CFH. C3dg interacts with CR2 (via the N-terminal Sushi domains 1 and 2). During pregnancy, C3dg exists as a complex (probably a 2:2:2 heterohexamer) with AGT and the proform of PRG2. Interacts with VSIG4. Interacts with S.aureus immunoglobulin-binding protein sbi, this prevents interaction between C3dg and CR2. Interacts with S.aureus fib. Interacts (both C3a and ASP) with C5AR2; the interaction occurs with higher affinity for ASP, enhancing the phosphorylation and activation of C5AR2, recruitment of ARRB2 to the cell surface and endocytosis of GRP77. {ECO:0000250|UniProtKB:P01024}. +P02463 CO4A1_MOUSE Collagen alpha-1(IV) chain [Cleaved into: Arresten] 1669 160,679 Chain (2); Cross-link (2); Disulfide bond (6); Domain (1); Frameshift (1); Glycosylation (1); Modified residue (15); Propeptide (1); Region (1); Sequence caution (1); Sequence conflict (12); Signal peptide (1) FUNCTION: Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen. {ECO:0000305|PubMed:28424209}.; FUNCTION: Arresten, comprising the C-terminal NC1 domain, inhibits angiogenesis and tumor formation. The C-terminal half is found to possess the anti-angiogenic activity. Specifically inhibits endothelial cell proliferation, migration and tube formation. Inhibits expression of hypoxia-inducible factor 1alpha and ERK1/2 and p38 MAPK activation. Ligand for alpha1/beta1 integrin. {ECO:0000250|UniProtKB:P02462}. PTM: Lysines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated. The modified lysines can be O-glycosylated. {ECO:0000269|PubMed:25645914}.; PTM: Contains 4-hydroxyproline. Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. {ECO:0000269|PubMed:25645914}.; PTM: Contains 3-hydroxyproline. This modification occurs on the first proline residue in the sequence motif Gly-Pro-Hyp, where Hyp is 4-hydroxyproline. {ECO:0000269|PubMed:24368846, ECO:0000269|PubMed:25645914}.; PTM: Type IV collagens contain numerous cysteine residues which are involved in inter- and intramolecular disulfide bonding. 12 of these, located in the NC1 domain, are conserved in all known type IV collagens. {ECO:0000250|UniProtKB:P02462}.; PTM: The trimeric structure of the NC1 domains is stabilized by covalent bonds (sulfilimine cross-links) between Lys and Met residues. These cross-links are important for the mechanical stability of the basement membrane. {ECO:0000269|PubMed:28424209}.; PTM: Proteolytic processing produces the C-terminal NC1 peptide, arresten. {ECO:0000250|UniProtKB:P02462}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000269|PubMed:24368846}. SUBUNIT: There are six type IV collagen isoforms, alpha 1(IV)-alpha 6(IV), each of which can form a triple helix structure with 2 other chains to generate type IV collagen network. {ECO:0000250|UniProtKB:Q7SIB2}. DOMAIN: Alpha chains of type IV collagen have a non-collagenous domain (NC1) at their C-terminus, frequent interruptions of the G-X-Y repeats in the long central triple-helical domain (which may cause flexibility in the triple helix), and a short N-terminal triple-helical 7S domain. {ECO:0000305}. TISSUE SPECIFICITY: Detected in the basement membrane of the cornea (at protein level). {ECO:0000269|PubMed:24368846}. +Q9QZR9 CO4A4_MOUSE Collagen alpha-4(IV) chain 1682 164,096 Alternative sequence (2); Chain (1); Disulfide bond (6); Domain (1); Glycosylation (3); Motif (9); Region (2); Sequence conflict (2); Signal peptide (1); Site (1) FUNCTION: Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen. {ECO:0000250|UniProtKB:P53420, ECO:0000269|PubMed:10639489, ECO:0000269|PubMed:7962065}. PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. {ECO:0000250|UniProtKB:P53420, ECO:0000255|PROSITE-ProRule:PRU00736}.; PTM: Type IV collagens contain numerous cysteine residues which are involved in inter- and intramolecular disulfide bonding. 12 of these, located in the NC1 domain, are conserved in all known type IV collagens. {ECO:0000250|UniProtKB:P53420, ECO:0000255|PROSITE-ProRule:PRU00736}.; PTM: The trimeric structure of the NC1 domains is stabilized by covalent bonds between Lys and Met residues. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000255|PROSITE-ProRule:PRU00736, ECO:0000269|PubMed:7962065}. Note=Colocalizes with COL4A3 and COL4A5 in GBM, tubular basement membrane (TBM) and synaptic basal lamina (BL). {ECO:0000250|UniProtKB:P53420, ECO:0000269|PubMed:7962065}. SUBUNIT: There are six type IV collagen isoforms, alpha 1(IV)-alpha 6(IV), each of which can form a triple helix structure with 2 other chains to generate type IV collagen network. The alpha 3(IV) chain forms a triple helical protomer with alpha 4(IV) and alpha 5(IV); this triple helical structure dimerizes through NC1-NC1 domain interactions such that the alpha 3(IV), alpha 4(IV) and alpha 5(IV) chains of one protomer connect with the alpha 5(IV), alpha 4(IV) and alpha 3(IV) chains of the opposite protomer, respectively (By similarity). Associates with LAMB2 at the neuromuscular junction and in GBM. {ECO:0000250|UniProtKB:P53420, ECO:0000269|PubMed:7962065}. DOMAIN: Alpha chains of type IV collagen have a non-collagenous domain (NC1) at their C-terminus, frequent interruptions of the G-X-Y repeats in the long central triple-helical domain (which may cause flexibility in the triple helix), and a short N-terminal triple-helical 7S domain. {ECO:0000250|UniProtKB:P53420, ECO:0000255|PROSITE-ProRule:PRU00736}. TISSUE SPECIFICITY: Highly expressed in kidney and lung. Detected at lower levels in heart, muscle and skin. {ECO:0000269|PubMed:7962065}. +O88207 CO5A1_MOUSE Collagen alpha-1(V) chain 1838 183,677 Alternative sequence (1); Chain (1); Domain (2); Modified residue (65); Region (4); Sequence conflict (1); Signal peptide (1) FUNCTION: Type V collagen is a member of group I collagen (fibrillar forming collagen). It is a minor connective tissue component of nearly ubiquitous distribution. Type V collagen binds to DNA, heparan sulfate, thrombospondin, heparin, and insulin (By similarity). Transcriptionally activated by CEBPZ, which recognizes a CCAAT-like motif, CAAAT in the COL5A1 promoter. {ECO:0000250, ECO:0000269|PubMed:15246108}. PTM: Hydroxylation on proline residues within the sequence motif, GXPG, is most likely to be 4-hydroxy as this fits the requirement for 4-hydroxylation in vertebrates. {ECO:0000250}.; PTM: Sulfated on 40% of tyrosines. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}. SUBUNIT: Trimers of two alpha 1(V) and one alpha 2(V) chains in most tissues and trimers of one alpha 1(V), one alpha 2(V), and one alpha 3(V) chains in placenta. Interacts with CSPG4 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed (PubMed:22149965). Isoform 2 is more highly expressed in liver, kidney and lung (PubMed:22149965). {ECO:0000269|PubMed:22149965}. +Q3U962 CO5A2_MOUSE Collagen alpha-2(V) chain 1497 145,018 Chain (1); Disulfide bond (3); Domain (2); Erroneous initiation (1); Glycosylation (2); Metal binding (4); Modified residue (5); Motif (7); Propeptide (1); Sequence conflict (21); Signal peptide (1) FUNCTION: Type V collagen is a member of group I collagen (fibrillar forming collagen). It is a minor connective tissue component of nearly ubiquitous distribution. Type V collagen binds to DNA, heparan sulfate, thrombospondin, heparin, and insulin. Type V collagen is a key determinant in the assembly of tissue-specific matrices. {ECO:0000250|UniProtKB:P05997, ECO:0000269|PubMed:1297453, ECO:0000269|PubMed:7704020, ECO:0000269|PubMed:9642685}. PTM: Prolines at the third position of the tripeptide repeating unit (G-X-P) are hydroxylated in some or all of the chains. Probably 3-hydroxylated on prolines by LEPREL1.; PTM: Hydroxylation on proline residues within the sequence motif, GXPG, is most likely to be 4-hydroxy as this fits the requirement for 4-hydroxylation in vertebrates. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}. SUBUNIT: Trimers of two alpha 1(V) and one alpha 2(V) chains expressed in most tissues and trimers of one alpha 1(V), one alpha 2(V), and one alpha 3(V) chains with a more limited distribution of expression. {ECO:0000250|UniProtKB:P05997, ECO:0000269|PubMed:15199158}. DOMAIN: The C-terminal propeptide, also known as COLFI domain, have crucial roles in tissue growth and repair by controlling both the intracellular assembly of procollagen molecules and the extracellular assembly of collagen fibrils. It binds a calcium ion which is essential for its function (By similarity). {ECO:0000250}. +Q04857 CO6A1_MOUSE Collagen alpha-1(VI) chain 1025 108,489 Chain (1); Domain (3); Glycosylation (5); Motif (3); Region (3); Sequence conflict (4); Signal peptide (1) FUNCTION: Collagen VI acts as a cell-binding protein. PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. SUBUNIT: Trimers composed of three different chains: alpha-1(VI), alpha-2(VI), and alpha-3(VI) or alpha-4(VI) or alpha-5(VI) or alpha-6(VI). +A2AX52 CO6A4_MOUSE Collagen alpha-4(VI) chain 2309 250,798 Chain (1); Domain (8); Glycosylation (3); Motif (2); Region (3); Sequence conflict (30); Signal peptide (1) FUNCTION: Collagen VI acts as a cell-binding protein. {ECO:0000250}. PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. SUBUNIT: Trimers composed of three different chains: alpha-1(VI), alpha-2(VI), and alpha-3(VI) or alpha-4(VI) or alpha-5(VI) or alpha-6(VI). {ECO:0000269|PubMed:18276594}. TISSUE SPECIFICITY: In newborn, it is expressed in lung, kidney, brain, intestine, skin, sternum and, at weak level, calvaria. In adult, it is almost absent with some weak expression in ovary and very weak expression in spleen, lung, uterus and brain. {ECO:0000269|PubMed:18276594}. +A6H584 CO6A5_MOUSE Collagen alpha-5(VI) chain (Collagen alpha-1(XXIX) chain) 2640 289,575 Chain (1); Domain (15); Glycosylation (4); Motif (3); Region (3); Sequence conflict (2); Signal peptide (1) FUNCTION: Collagen VI acts as a cell-binding protein. {ECO:0000250}. PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:18276594}. Note=Deposed in the extracellular matrix of skeletal muscle. SUBUNIT: Trimers composed of three different chains: alpha-1(VI), alpha-2(VI), and alpha-3(VI) or alpha-4(VI) or alpha-5(VI) or alpha-6(VI). {ECO:0000305|PubMed:18276594}. TISSUE SPECIFICITY: In newborn, it is expressed in lung, heart, kidney, muscle, brain, intestine, skin, femur, sternum and calvaria. In adult, it is widely expressed and is detected in lung, heart, kidney, spleen, muscle, ovary, uterus, brain, skin, liver and sternum. {ECO:0000269|PubMed:18276594}. +Q99MK8 ARBK1_MOUSE Beta-adrenergic receptor kinase 1 (Beta-ARK-1) (EC 2.7.11.15) (G-protein-coupled receptor kinase 2) 689 79,639 Active site (1); Binding site (1); Chain (1); Domain (4); Modified residue (1); Nucleotide binding (1); Region (1); Sequence conflict (5); Site (3) FUNCTION: Specifically phosphorylates the agonist-occupied form of the beta-adrenergic and closely related receptors, probably inducing a desensitization of them. Key regulator of LPAR1 signaling. Competes with RALA for binding to LPAR1 thus affecting the signaling properties of the receptor. Desensitizes LPAR1 and LPAR2 in a phosphorylation-independent manner. Positively regulates ciliary smoothened (SMO)-dependent Hedgehog (Hh) signaling pathway by faciltating the trafficking of SMO into the cilium and the stimulation of SMO activity. {ECO:0000250|UniProtKB:P21146, ECO:0000250|UniProtKB:P25098}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P21146}. Cell membrane {ECO:0000250|UniProtKB:P21146}. SUBUNIT: Interacts with GIT1. Interacts with, and phosphorylates chemokine-stimulated CCR5. Interacts with ARRB1. Interacts with LPAR1 and LPAR2. Interacts with RALA in response to LPAR1 activation. ADRBK1 and RALA mutually inhibit each other's binding to LPAR1. Interacts with ADRB2. {ECO:0000250|UniProtKB:P21146, ECO:0000250|UniProtKB:P25098}. DOMAIN: The PH domain binds anionic phospholipids and helps recruiting ADRBK1 from the cytoplasm to plasma membrane close to activated receptors. It mediates binding to G protein beta and gamma subunits, competing with G-alpha subunits and other G-betagamma effectors. {ECO:0000250|UniProtKB:P21146}. +Q4LDD4 ARAP1_MOUSE Arf-GAP with Rho-GAP domain, ANK repeat and PH domain-containing protein 1 (Centaurin-delta-2) (Cnt-d2) 1452 162,276 Alternative sequence (2); Chain (1); Domain (8); Modified residue (6); Sequence conflict (4); Zinc finger (1) FUNCTION: Phosphatidylinositol 3,4,5-trisphosphate-dependent GTPase-activating protein that modulates actin cytoskeleton remodeling by regulating ARF and RHO family members. Is activated by phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) binding. Can be activated by phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4,5)P2) binding, albeit with lower efficiency. Has a preference for ARF1 and ARF5 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96P48}. Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:Q96P48}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q96P48}. Cell membrane {ECO:0000250|UniProtKB:Q96P48}. SUBUNIT: Interacts with TNFRSF10A. {ECO:0000250|UniProtKB:Q96P48}. +P61750 ARF4_MOUSE ADP-ribosylation factor 4 180 20,397 Chain (1); Initiator methionine (1); Lipidation (1); Modified residue (1); Nucleotide binding (3); Sequence conflict (2) FUNCTION: GTP-binding protein that functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. Involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus. SUBCELLULAR LOCATION: Golgi apparatus. Membrane {ECO:0000250|UniProtKB:P18085}; Lipid-anchor {ECO:0000250|UniProtKB:P18085}. +Q8C025 CHPT1_MOUSE Cholinephosphotransferase 1 (mCHPT1) (EC 2.7.8.2) (Diabetic nephropathy-associated gene transcript 1) (Diacylglycerol cholinephosphotransferase 1) 398 44,608 Alternative sequence (4); Chain (1); Initiator methionine (1); Modified residue (1); Sequence conflict (3); Transmembrane (8) TRANSMEM 66 86 Helical. {ECO:0000255}.; TRANSMEM 93 113 Helical. {ECO:0000255}.; TRANSMEM 160 180 Helical. {ECO:0000255}.; TRANSMEM 193 213 Helical. {ECO:0000255}.; TRANSMEM 226 248 Helical. {ECO:0000255}.; TRANSMEM 261 281 Helical. {ECO:0000255}.; TRANSMEM 295 315 Helical. {ECO:0000255}.; TRANSMEM 349 369 Helical. {ECO:0000255}. Phospholipid metabolism; phosphatidylcholine biosynthesis; phosphatidylcholine from phosphocholine: step 2/2. FUNCTION: Catalyzes phosphatidylcholine biosynthesis from CDP-choline. It thereby plays a central role in the formation and maintenance of vesicular membranes (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain, heart, lung, liver, spleen, intestine and muscle. Down-regulated in kidney of type 2 diabetic KK/Ta mice. {ECO:0000269|PubMed:15254874}. +P59999 ARPC4_MOUSE Actin-related protein 2/3 complex subunit 4 (Arp2/3 complex 20 kDa subunit) (p20-ARC) 168 19,667 Chain (1); Initiator methionine (1); Modified residue (1) FUNCTION: Actin-binding component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility. In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA. The Arp2/3 complex promotes homologous recombination (HR) repair in response to DNA damage by promoting nuclear actin polymerization, leading to drive motility of double-strand breaks (DSBs). {ECO:0000250|UniProtKB:P59998}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P59998}. Cell projection {ECO:0000250|UniProtKB:P59998}. Nucleus {ECO:0000250|UniProtKB:P59998}. SUBUNIT: Component of the Arp2/3 complex composed of ACTR2/ARP2, ACTR3/ARP3, ARPC1B/p41-ARC, ARPC2/p34-ARC, ARPC3/p21-ARC, ARPC4/p20-ARC and ARPC5/p16-ARC. {ECO:0000250|UniProtKB:P59998}. +Q9JKP8 CHRC1_MOUSE Chromatin accessibility complex protein 1 (CHRAC-1) (DNA polymerase epsilon subunit p15) (NF-YC-like protein) (YC-like protein 1) (YCL1) 129 14,127 Chain (1); Coiled coil (1); Initiator methionine (1); Modified residue (3) FUNCTION: Forms a complex with DNA polymerase epsilon subunit POLE3 and binds naked DNA, which is then incorporated into chromatin, aided by the nucleosome remodeling activity of ISWI/SNF2H and ACF1. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Interacts with POLE3. Together with POLE3, ACF1 and ISWI/SNF2H proteins, it forms the ISWI chromatin-remodeling complex, CHRAC (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitously expressed. +Q8BWG8 ARRB1_MOUSE Beta-arrestin-1 (Arrestin beta-1) 418 46,973 Alternative sequence (1); Binding site (4); Chain (1); Modified residue (2); Region (3) FUNCTION: Functions in regulating agonist-mediated G-protein coupled receptor (GPCR) signaling by mediating both receptor desensitization and resensitization processes. During homologous desensitization, beta-arrestins bind to the GPRK-phosphorylated receptor and sterically preclude its coupling to the cognate G-protein; the binding appears to require additional receptor determinants exposed only in the active receptor conformation. The beta-arrestins target many receptors for internalization by acting as endocytic adapters (CLASPs, clathrin-associated sorting proteins) and recruiting the GPRCs to the adapter protein 2 complex 2 (AP-2) in clathrin-coated pits (CCPs). However, the extent of beta-arrestin involvement appears to vary significantly depending on the receptor, agonist and cell type. Internalized arrestin-receptor complexes traffic to intracellular endosomes, where they remain uncoupled from G-proteins. Two different modes of arrestin-mediated internalization occur. Class A receptors, like ADRB2, OPRM1, ENDRA, D1AR and ADRA1B dissociate from beta-arrestin at or near the plasma membrane and undergo rapid recycling. Class B receptors, like AVPR2, AGTR1, NTSR1, TRHR and TACR1 internalize as a complex with arrestin and traffic with it to endosomal vesicles, presumably as desensitized receptors, for extended periods of time. Receptor resensitization then requires that receptor-bound arrestin is removed so that the receptor can be dephosphorylated and returned to the plasma membrane. Involved in internalization of P2RY4 and UTP-stimulated internalization of P2RY2. Involved in phosphorylation-dependent internalization of OPRD1 ands subsequent recycling. Involved in the degradation of cAMP by recruiting cAMP phosphodiesterases to ligand-activated receptors. Beta-arrestins function as multivalent adapter proteins that can switch the GPCR from a G-protein signaling mode that transmits short-lived signals from the plasma membrane via small molecule second messengers and ion channels to a beta-arrestin signaling mode that transmits a distinct set of signals that are initiated as the receptor internalizes and transits the intracellular compartment. Acts as signaling scaffold for MAPK pathways such as MAPK1/3 (ERK1/2). ERK1/2 activated by the beta-arrestin scaffold is largely excluded from the nucleus and confined to cytoplasmic locations such as endocytic vesicles, also called beta-arrestin signalosomes. Recruits c-Src/SRC to ADRB2 resulting in ERK activation. GPCRs for which the beta-arrestin-mediated signaling relies on both ARRB1 and ARRB2 (codependent regulation) include ADRB2, F2RL1 and PTH1R. For some GPCRs the beta-arrestin-mediated signaling relies on either ARRB1 or ARRB2 and is inhibited by the other respective beta-arrestin form (reciprocal regulation). Inhibits ERK1/2 signaling in AGTR1- and AVPR2-mediated activation (reciprocal regulation). Is required for SP-stimulated endocytosis of NK1R and recruits c-Src/SRC to internalized NK1R resulting in ERK1/2 activation, which is required for the antiapoptotic effects of SP. Is involved in proteinase-activated F2RL1-mediated ERK activity. Acts as signaling scaffold for the AKT1 pathway. Is involved in alpha-thrombin-stimulated AKT1 signaling. Is involved in IGF1-stimulated AKT1 signaling leading to increased protection from apoptosis. Involved in activation of the p38 MAPK signaling pathway and in actin bundle formation. Involved in F2RL1-mediated cytoskeletal rearrangement and chemotaxis. Involved in AGTR1-mediated stress fiber formation by acting together with GNAQ to activate RHOA. Appears to function as signaling scaffold involved in regulation of MIP-1-beta-stimulated CCR5-dependent chemotaxis. Involved in attenuation of NF-kappa-B-dependent transcription in response to GPCR or cytokine stimulation by interacting with and stabilizing CHUK. May serve as nuclear messenger for GPCRs. Involved in OPRD1-stimulated transcriptional regulation by translocating to CDKN1B and FOS promoter regions and recruiting EP300 resulting in acetylation of histone H4. Involved in regulation of LEF1 transcriptional activity via interaction with DVL1 and/or DVL2 Also involved in regulation of receptors other than GPCRs. Involved in Toll-like receptor and IL-1 receptor signaling through the interaction with TRAF6 which prevents TRAF6 autoubiquitination and oligomerization required for activation of NF-kappa-B and JUN. Involved in IL8-mediated granule release in neutrophils. Binds phosphoinositides. Binds inositolhexakisphosphate (InsP6) (By similarity). Required for atypical chemokine receptor ACKR2-induced RAC1-LIMK1-PAK1-dependent phosphorylation of cofilin (CFL1) and for the up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. Involved in the internalization of the atypical chemokine receptor ACKR3 (By similarity). Negatively regulates the NOTCH signaling pathway by mediating the ubiquitination and degradation of NOTCH1 by ITCH. Participates to the recruitment of the ubiquitin-protein ligase to the receptor (PubMed:23886940). {ECO:0000250, ECO:0000269|PubMed:14534298, ECO:0000269|PubMed:18337459, ECO:0000269|PubMed:23886940}. PTM: Constitutively phosphorylated at in the cytoplasm. At the plasma membrane, is rapidly dephosphorylated, a process that is required for clathrin binding and ADRB2 endocytosis but not for ADRB2 binding and desensitization. Once internalized, is rephosphorylated (By similarity). {ECO:0000250}.; PTM: The ubiquitination status appears to regulate the formation and trafficking of beta-arrestin-GPCR complexes and signaling. Ubiquitination appears to occur GPCR-specific. Ubiquitinated by MDM2; the ubiquitination is required for rapid internalization of ADRB2. Deubiquitinated by USP33; the deubiquitination leads to a dissociation of the beta-arrestin-GPCR complex. Stimulation of a class A GPCR, such as ADRB2, induces transient ubiquitination and subsequently promotes association with USP33 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cell membrane {ECO:0000250}. Membrane, clathrin-coated pit {ECO:0000305}. Cell projection, pseudopodium {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Note=Translocates to the plasma membrane and colocalizes with antagonist-stimulated GPCRs. The monomeric form is predominantly located in the nucleus. The oligomeric form is located in the cytoplasm. Translocates to the nucleus upon stimulation of OPRD1 (By similarity). {ECO:0000250}. SUBUNIT: Monomer. Homodimer. Homooligomer; the self-association is mediated by InsP6-binding. Heterooligomer with ARRB2; the association is mediated by InsP6-binding. Interacts with ADRB2 (phosphorylated). Interacts with CHRM2 (phosphorylated). Interacts with LHCGR. Interacts with CYTH2 and CASR. Interacts with AP2B1 (dephosphorylated); phosphorylation of AP2B1 disrupts the interaction. Interacts (dephosphorylated at Ser-412) with CLTC. Interacts with CCR2 and GRK2. Interacts with CRR5. Interacts with PTAFR (phosphorylated on serine residues). Interacts with CLTC and MAP2K3. Interacts with CREB1. Interacts with TRAF6. Interacts with IGF1R and MDM2. Interacts with C5AR1. Interacts with PDE4D. Interacts with SRC (via the SH3 domain and the protein kinase domain); the interaction is independent of the phosphorylation state of SRC C-terminus. Interacts with TACR1. Interacts with RAF1. Interacts with DVL1; the interaction is enhanced by phosphorylation of DVL1. Interacts with DVL2; the interaction is enhanced by phosphorylation of DVL2. Interacts with IGF1R. Interacts with CHUK, IKBKB and MAP3K14. Associates with MAP kinase p38. Part of a MAPK signaling complex consisting of TACR1, ARRB1, SRC, MAPK1 (activated) and MAPK3 (activated). Part of a MAPK signaling complex consisting of F2RL1, ARRB1, RAF1, MAPK1 (activated) and MAPK3 (activated). Interacts with GPR143 (By similarity). Interacts with MAP2K4/MKK4. Interacts with HCK and CXCR1 (phosphorylated) (By similarity). Interacts with ACKR3 and ACKR4 (By similarity). Interacts with ARRDC1; the interaction is direct (PubMed:23886940). Interacts with GPR61, GPR62 and GPR135 (By similarity). {ECO:0000250|UniProtKB:P49407, ECO:0000269|PubMed:23886940}. DOMAIN: The [DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif mediates interaction the AP-2 complex subunit AP2B1. Binding to phosphorylated GPCRs induces a conformationanl change that exposes the motif to the surface (By similarity). {ECO:0000250}.; DOMAIN: The N-terminus binds InsP6 with low affinity. {ECO:0000250}.; DOMAIN: The C-terminus binds InsP6 with high affinity. {ECO:0000250}. +P50429 ARSB_MOUSE Arylsulfatase B (ASB) (EC 3.1.6.12) (N-acetylgalactosamine-4-sulfatase) (G4S) 534 59,647 Active site (2); Alternative sequence (2); Binding site (3); Chain (1); Disulfide bond (4); Glycosylation (6); Metal binding (5); Modified residue (1); Sequence conflict (4); Signal peptide (1) FUNCTION: Removes sulfate groups from chondroitin-4-sulfate (C4S) and regulates its degradation (By similarity). Involved in the regulation of cell adhesion, cell migration and invasion in colonic epithelium (By similarity). In the central nervous system, is a regulator of neurite outgrowth and neuronal plasticity, acting through the control of sulfate glycosaminoglycans and neurocan levels (By similarity). {ECO:0000250|UniProtKB:P15848, ECO:0000250|UniProtKB:P50430}. PTM: The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity. {ECO:0000250}. SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:19536613}. Cell surface {ECO:0000269|PubMed:19536613}. SUBUNIT: Homodimer. {ECO:0000250}. +Q9CVB6 ARPC2_MOUSE Actin-related protein 2/3 complex subunit 2 (Arp2/3 complex 34 kDa subunit) (p34-ARC) 300 34,357 Chain (1); Modified residue (2) FUNCTION: Actin-binding component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility. Seems to contact the mother actin filament. In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA. The Arp2/3 complex promotes homologous recombination (HR) repair in response to DNA damage by promoting nuclear actin polymerization, leading to drive motility of double-strand breaks (DSBs). {ECO:0000250|UniProtKB:O15144}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O15144}. Cell projection {ECO:0000250|UniProtKB:O15144}. Cell junction, synapse, synaptosome {ECO:0000269|PubMed:24153177}. Nucleus {ECO:0000250|UniProtKB:O15144}. SUBUNIT: Component of the Arp2/3 complex composed of ACTR2/ARP2, ACTR3/ARP3, ARPC1B/p41-ARC, ARPC2/p34-ARC, ARPC3/p21-ARC, ARPC4/p20-ARC and ARPC5/p16-ARC (By similarity). Interacts with SHANK3; the interaction probably mediates the association of SHANK3 with the Arp2/3 complex (PubMed:24153177). {ECO:0000250|UniProtKB:O15144, ECO:0000269|PubMed:24153177}. TISSUE SPECIFICITY: Expressed in hippocampal neurons (at protein level). {ECO:0000269|PubMed:24153177}. +Q9Z0L2 ARTN_MOUSE Artemin 224 23,726 Alternative sequence (4); Chain (1); Compositional bias (1); Disulfide bond (4); Glycosylation (1); Propeptide (1); Signal peptide (1) FUNCTION: Ligand for the GFR-alpha-3-RET receptor complex but can also activate the GFR-alpha-1-RET receptor complex. Supports the survival of sensory and sympathetic peripheral neurons in culture and also supports the survival of dopaminergic neurons of the ventral mid-brain (By similarity). Strong attractant of gut hematopoietic cells thus promoting the formation Peyer's patch-like structures, a major component of the gut-associated lymphoid tissue. {ECO:0000250, ECO:0000269|PubMed:17322904}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Homodimer; disulfide-linked (By similarity). Binds to RET. {ECO:0000250}. +Q9CQ31 ASB11_MOUSE Ankyrin repeat and SOCS box protein 11 (ASB-11) 323 35,331 Alternative sequence (1); Chain (1); Domain (1); Repeat (7) Protein modification; protein ubiquitination. FUNCTION: May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000250}. DOMAIN: The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin-protein ligase complexes. {ECO:0000250}. +C0HK79 ARXS1_MOUSE Adipocyte-related X-chromosome expressed sequence 1 180 20,146 Chain (1); Glycosylation (1); Topological domain (2); Transmembrane (1) TRANSMEM 12 32 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 11 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 33 180 Lumenal. {ECO:0000255}. FUNCTION: Plays a role in adipogenesis. {ECO:0000269|PubMed:21177646}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21177646}; Single-pass type II membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Strongly expressed in epididymal white and brown adipose tissue with low levels in heart. {ECO:0000269|PubMed:21177646}. +Q9JHE3 ASAH2_MOUSE Neutral ceramidase (N-CDase) (NCDase) (EC 3.5.1.23) (Acylsphingosine deacylase 2) (N-acylsphingosine amidohydrolase 2) [Cleaved into: Neutral ceramidase soluble form] 756 83,509 Active site (1); Chain (2); Disulfide bond (3); Glycosylation (7); Metal binding (8); Region (1); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 12 32 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 11 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 33 756 Lumenal. {ECO:0000255}. FUNCTION: Hydrolyzes the sphingolipid ceramide into sphingosine and free fatty acid at an optimal pH of 6.5-8.5. Acts as a key regulator of sphingolipid signaling metabolites by generating sphingosine at the cell surface. Acts as a repressor of apoptosis both by reducing C16-ceramide, thereby preventing ceramide-induced apoptosis, and generating sphingosine, a precursor of the antiapoptotic factor sphingosine 1-phosphate. Probably involved in the digestion of dietary sphingolipids in intestine by acting as a key enzyme for the catabolism of dietary sphingolipids and regulating the levels of bioactive sphingolipid metabolites in the intestinal tract. {ECO:0000269|PubMed:14557071, ECO:0000269|PubMed:16126722, ECO:0000269|PubMed:16380386}. PTM: N-glycosylated. Required for enzyme activity. {ECO:0000269|PubMed:10652340, ECO:0000269|PubMed:10753931}.; PTM: O-glycosylated. Required to retain it as a type II membrane protein at the cell surface. {ECO:0000250|UniProtKB:Q9NR71}.; PTM: Phosphorylated. May prevent ubiquitination and subsequent degradation. {ECO:0000250|UniProtKB:Q91XT9}.; PTM: Ubiquitinated, leading to its degradation by the proteasome. Ubiquitination is triggered by nitric oxid. {ECO:0000250|UniProtKB:Q91XT9}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11591392, ECO:0000269|PubMed:12921776}; Single-pass type II membrane protein {ECO:0000269|PubMed:11591392, ECO:0000269|PubMed:12921776}. Note=The neutral ceramidase soluble form is a secreted protein. TISSUE SPECIFICITY: Widely expressed. Strongly expressed in liver and kidney. Highly expressed in the small intestine along the brush border. Localizes in the apical membranes of proximal and distal tubules, collecting ducts of kidney, endosome-like organelles of hepatocytes, and in the epithelia of the jejunum and ileum. {ECO:0000269|PubMed:10753931, ECO:0000269|PubMed:16380386}. +Q8VHP9 ASB17_MOUSE Ankyrin repeat and SOCS box protein 17 (ASB-17) 295 34,471 Chain (1); Domain (1); Repeat (1) Protein modification; protein ubiquitination. FUNCTION: May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000250}. DOMAIN: The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin-protein ligase complexes. {ECO:0000250}. TISSUE SPECIFICITY: Specifically expressed in testis (PubMed:15460110). Localizes to spermatogenic cells in testis, with highest expression in round spermatids and condensing spermatids and lower expression in pachytene spermatocytes (PubMed:15204681, PubMed:15460110). {ECO:0000269|PubMed:15204681, ECO:0000269|PubMed:15460110}. +Q7SIG6 ASAP2_MOUSE Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2 (Development and differentiation-enhancing factor 2) (Paxillin-associated protein with ARF GAP activity 3) (PAG3) (Pyk2 C-terminus-associated protein) (PAP) 958 106,805 Alternative sequence (2); Beta strand (4); Chain (1); Coiled coil (1); Compositional bias (1); Domain (3); Helix (14); Modified residue (2); Mutagenesis (6); Repeat (2); Turn (7) FUNCTION: Activates the small GTPases ARF1, ARF5 and ARF6. Regulates the formation of post-Golgi vesicles and modulates constitutive secretion. Modulates phagocytosis mediated by Fc gamma receptor and ARF6. Modulates PXN recruitment to focal contacts and cell migration (By similarity). {ECO:0000250, ECO:0000269|PubMed:10022920, ECO:0000269|PubMed:11304556}. PTM: Phosphorylated on tyrosine residues by SRC and PTK2B. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus, Golgi stack membrane; Peripheral membrane protein. Cell membrane; Peripheral membrane protein. Note=Colocalizes with F-actin and ARF6 in phagocytic cups. SUBUNIT: Binds PXN, ARF1, ARF5, ARF6, PTK2B and SRC. {ECO:0000269|PubMed:10601011}. DOMAIN: The conserved Arg-467 in the Arf-GAP domain probably becomes part of the active site of bound small GTPases and is necessary for GTP hydrolysis. +Q8K0L0 ASB2_MOUSE Ankyrin repeat and SOCS box protein 2 (ASB-2) 634 70,221 Alternative sequence (2); Chain (1); Domain (2); Erroneous initiation (1); Repeat (12); Sequence conflict (1) Protein modification; protein ubiquitination. FUNCTION: Probable substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000250}. SUBUNIT: Component of a probable ECS E3 ubiquitin-protein ligase complex which contains CUL5, either RBX1 or RNF7/RBX2, Elongin BC complex (ELOB and ELOC) and ASB2. {ECO:0000250}. DOMAIN: The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin-protein ligase complexes. {ECO:0000250}. TISSUE SPECIFICITY: Highest expression in muscle, heart and spleen. {ECO:0000269|PubMed:11111040}. +Q91WR3 ASCC2_MOUSE Activating signal cointegrator 1 complex subunit 2 (ASC-1 complex subunit p100) (Trip4 complex subunit p100) 749 85,653 Alternative sequence (2); Chain (1); Domain (1); Modified residue (2) FUNCTION: Plays a role in DNA damage repair as component of the ASCC complex. Recruits ASCC3 and ALKBH3 to sites of DNA damage by binding to polyubiquitinated proteins that have 'Lys-63'-linked polyubiquitin chains. Part of the ASC-1 complex that enhances NF-kappa-B, SRF and AP1 transactivation. {ECO:0000250|UniProtKB:Q9H1I8}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H1I8}. Nucleus speckle {ECO:0000250|UniProtKB:Q9H1I8}. Note=Colocalizes with the spliceosomal components PRPF8 and SNRNP200/BRR2 in nuclear foci when cells have been exposed to alkylating agents that cause DNA damage. Colocalizes with RNF113A and 'Lys-63'-linked polyubiquitinated proteins, ALKBH3 and ASCC3 in nuclear foci when cells have been exposed to alkylating agents that cause DNA damage. {ECO:0000250|UniProtKB:Q9H1I8}. SUBUNIT: Identified in the ASCC complex that contains ASCC1, ASCC2 and ASCC3. Interacts directly with ASCC3. The ASCC complex interacts with ALKBH3. Interacts (via CUE domain) with 'Lys-63'-linked polyubiquitin chains, but not with 'Lys-48'-linked polyubiquitin chains. Part of the ASC-1 complex, that contains TRIP4, ASCC1, ASCC2 and ASCC3. Interacts with CSRP1. Interacts with PRPF8, a component of the spliceosome. {ECO:0000250|UniProtKB:Q9H1I8}. +Q9WV71 ASB4_MOUSE Ankyrin repeat and SOCS box protein 4 (ASB-4) 426 48,098 Chain (1); Domain (1); Modified residue (1); Mutagenesis (7); Region (2); Repeat (6); Site (1) Protein modification; protein ubiquitination. FUNCTION: Probable substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes differentiation and maturation of the vascular lineage by an oxygen-dependent mechanism. {ECO:0000269|PubMed:17636018}. PTM: Hydroxylation at Asn-246 by HIF1AN may provide an oxygen-dependent regulation mechanism for the function of ASB4 in promoting vascular differentiation. {ECO:0000269|PubMed:17636018}. SUBUNIT: Interacts with HIF1AN. Component of an ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex formed of CUL2 or CUL5, Elongin BC (ELOB and ELOC), RBX1 and ASB4. {ECO:0000269|PubMed:17636018}. DOMAIN: The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin-protein ligase complexes. {ECO:0000250}. TISSUE SPECIFICITY: Highest expression detected in testis, with some expression detected in ovary and heart. Not detected in lung, kidney, liver, spleen and bone marrow. {ECO:0000269|PubMed:11111040, ECO:0000269|PubMed:17636018}. +Q91ZT7 ASB10_MOUSE Ankyrin repeat and SOCS box protein 10 (ASB-10) 467 51,583 Chain (1); Domain (1); Repeat (7) Protein modification; protein ubiquitination. FUNCTION: May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. DOMAIN: The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin-protein ligase complexes. {ECO:0000250}. +E9PZJ8 ASCC3_MOUSE Activating signal cointegrator 1 complex subunit 3 (EC 3.6.4.12) 2198 250,557 Alternative sequence (1); Chain (1); Coiled coil (2); Domain (6); Erroneous initiation (1); Modified residue (2); Motif (2); Nucleotide binding (2); Sequence conflict (1) FUNCTION: 3'-5' DNA helicase involved in repair of alkylated DNA. Promotes DNA unwinding to generate single-stranded substrate needed for ALKBH3, enabling ALKBH3 to process alkylated N3-methylcytosine (3mC) within double-stranded regions. Part of the ASC-1 complex that enhances NF-kappa-B, SRF and AP1 transactivation. {ECO:0000250|UniProtKB:Q8N3C0}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8N3C0}. Nucleus speckle {ECO:0000250|UniProtKB:Q8N3C0}. Note=Colocalizes with ALKBH3 and ASCC2 in nuclear foci when cells have been exposed to alkylating agents that cause DNA damage. {ECO:0000250|UniProtKB:Q8N3C0}. SUBUNIT: Identified in the ASCC complex that contains ASCC1, ASCC2 and ASCC3. Functions as scaffolding subunit that interacts directly with both ASCC1 and ASCC2. Interacts directly with ALKBH3, and thereby recruits ALKBH3 to the ASCC complex. Part of the ASC-1/TRIP4 complex, that contains TRIP4, ASCC1, ASCC2 and ASCC3. {ECO:0000250|UniProtKB:Q8N3C0}. +Q91ZU1 ASB6_MOUSE Ankyrin repeat and SOCS box protein 6 (ASB-6) 418 46,276 Chain (1); Domain (1); Repeat (6); Sequence conflict (1) Protein modification; protein ubiquitination. FUNCTION: Probable substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. {ECO:0000250, ECO:0000269|PubMed:15231829}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15231829}. SUBUNIT: Binds APS. Identified in a complex with ELOB and ELOC. Interacts with CUL5 and RNF7 (By similarity). {ECO:0000250}. DOMAIN: The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin-protein ligase complexes. {ECO:0000250}. TISSUE SPECIFICITY: Detected in adipocytes. {ECO:0000269|PubMed:15231829}. +Q91ZT8 ASB9_MOUSE Ankyrin repeat and SOCS box protein 9 (ASB-9) 290 31,656 Chain (1); Domain (1); Modified residue (1); Repeat (6); Sequence conflict (1); Site (1) Protein modification; protein ubiquitination. FUNCTION: Substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Recognizes at least two forms of creatine kinase, CKB and CKMT1A (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. DOMAIN: The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin-protein ligase complexes. {ECO:0000250}. +O35885 ASCL2_MOUSE Achaete-scute homolog 2 (ASH-2) (mASH-2) (mASH2) 263 27,784 Chain (1); Compositional bias (2); Domain (1); Sequence conflict (6) FUNCTION: AS-C proteins are involved in the determination of the neuronal precursors in the peripheral nervous system and the central nervous system. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Efficient DNA binding requires dimerization with another bHLH protein. Part of a complex composed at least of ASCL2, EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; this complex may have a histone H3-specific methyltransferase activity. {ECO:0000250}. +Q9JJR7 ASCL3_MOUSE Achaete-scute homolog 3 (ASH-3) (mASH-3) (mASH3) (bHLH transcriptional regulator Sgn-1) 174 20,245 Chain (1); Domain (1) FUNCTION: Transcriptional repressor. Inhibits myogenesis. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Efficient DNA binding requires dimerization with another bHLH protein. TISSUE SPECIFICITY: Specifically expressed in the salivary duct cells. +Q925H0 ASIC2_MOUSE Acid-sensing ion channel 2 (ASIC2) (Amiloride-sensitive brain sodium channel) (Amiloride-sensitive cation channel 1, neuronal) (Brain sodium channel 1) (BNC1) (BNaC1) 512 57,739 Alternative sequence (2); Chain (1); Disulfide bond (7); Glycosylation (2); Modified residue (2); Topological domain (3); Transmembrane (2) TRANSMEM 38 58 Helical. {ECO:0000255}.; TRANSMEM 428 448 Helical. {ECO:0000255}. TOPO_DOM 1 37 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 59 427 Extracellular. {ECO:0000250}.; TOPO_DOM 449 512 Cytoplasmic. {ECO:0000250}. FUNCTION: Cation channel with high affinity for sodium, which is gated by extracellular protons and inhibited by the diuretic amiloride. Also permeable for Li(+) and K(+). Generates a biphasic current with a fast inactivating and a slow sustained phase. Heteromeric channel assembly seems to modulate. {ECO:0000269|PubMed:14762118}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15537887, ECO:0000269|PubMed:15708491}; Multi-pass membrane protein {ECO:0000269|PubMed:15537887, ECO:0000269|PubMed:15708491}. Note=Localized at the plasma membrane, in the soma and punctated peripheral processes of neurons. SUBUNIT: Homotrimer or heterotrimer with other ASIC proteins (By similarity). Interacts with PRKCABP and ASIC3 (By similarity). Interacts with STOM; this regulates channel activity (PubMed:15471860, PubMed:22850675). Heterotrimer of Asic1a-Asic2a interacts with the snake venom mambalgin-1, mambalgin-2 and mambalgin-3 (By similarity). Heterotrimer of Asic1a-Asic2b interacts with the snake venom mambalgin-1 and mambalgin-2 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q62962, ECO:0000269|PubMed:15471860, ECO:0000269|PubMed:22850675}. TISSUE SPECIFICITY: Expressed by sensory neurons. Expressed by nociceptive sensory neurons, spiral ganglion (SG) neurons and the retina (at protein level). Isoform 1 and isoform 2 are expressed in outer nuclear layer of retina (photoreceptors) and to a lower extent in distal and proximal inner nuclear layer. {ECO:0000269|PubMed:14762118, ECO:0000269|PubMed:15537887}. +Q99MY8 ASH1L_MOUSE Histone-lysine N-methyltransferase ASH1L (EC 2.1.1.43) (ASH1-like protein) (Absent small and homeotic disks protein 1 homolog) 2958 331,333 Chain (1); Compositional bias (2); Cross-link (2); DNA binding (3); Domain (5); Erroneous initiation (2); Modified residue (8); Region (1); Sequence conflict (6); Zinc finger (1) FUNCTION: Histone methyltransferase specifically methylating 'Lys-36' of histone H3 (H3K36me). {ECO:0000250|UniProtKB:Q9NR48}. PTM: Methylated at Gln-1218 by N6AMT1. {ECO:0000250|UniProtKB:Q9NR48}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NR48}. Cell junction, tight junction {ECO:0000250|UniProtKB:Q9NR48}. Chromosome {ECO:0000250|UniProtKB:Q9NR48}. Note=The relevance of tight junction localization is however unclear. {ECO:0000250|UniProtKB:Q9NR48}. +Q9DAP7 ASF1B_MOUSE Histone chaperone ASF1B (Anti-silencing function protein 1 homolog B) (mCIA-II) 202 22,464 Chain (1); Modified residue (1); Region (1); Sequence conflict (2) FUNCTION: Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly. Cooperates with chromatin assembly factor 1 (CAF-1) to promote replication-dependent chromatin assembly. Does not participate in replication-independent nucleosome deposition which is mediated by ASF1A and HIRA. {ECO:0000269|PubMed:17054786}. PTM: Phosphorylated by TLK2 (By similarity). Phosphorylated by TLK1. {ECO:0000250|UniProtKB:Q9NVP2, ECO:0000269|PubMed:17054786}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NVP2}. SUBUNIT: Interacts with histone H3 (including both histone H3.1 and H3.3) and histone H4. Interacts with the CHAF1A, CHAF1B and RBBP4 subunits of the CAF-1 complex. Interacts with HAT1, NASP, TAF1, TLK1 and TLK2 (By similarity). Interacts with CDAN1 (By similarity). Found in a cytosolic complex with CDAN1, ASF1A, IPO4 and histones H3.1 and H4. Interacts with CREBBP (By similarity). {ECO:0000250|UniProtKB:Q9NVP2}. TISSUE SPECIFICITY: Highly expressed in testis. Restricted to premeiotic to meiotic stages during spermatogenesis. {ECO:0000269|PubMed:12842904}. +D3KU66 ASMT_MOUSE Acetylserotonin O-methyltransferase (EC 2.1.1.4) (Hydroxyindole O-methyltransferase) 387 40,925 Active site (1); Binding site (6); Chain (1); Natural variant (2); Region (1) Aromatic compound metabolism; melatonin biosynthesis; melatonin from serotonin: step 1/2. FUNCTION: Catalyzes the transfer of a methyl group onto N-acetylserotonin, producing melatonin (N-acetyl-5-methoxytryptamine). {ECO:0000250}. SUBUNIT: Homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Expressed predominantly in the pineal gland. very low expression, if any, in the retina. {ECO:0000269|PubMed:20308563}. +Q922M7 ASHWN_MOUSE Ashwin 232 26,031 Chain (1); Modified residue (7) SUBUNIT: Component of the tRNA-splicing ligase complex. {ECO:0000250}. +Q04519 ASM_MOUSE Sphingomyelin phosphodiesterase (EC 3.1.4.12) (Acid sphingomyelinase) (ASMase) 627 69,927 Beta strand (17); Chain (1); Disulfide bond (8); Domain (1); Glycosylation (6); Helix (24); Metal binding (8); Mutagenesis (8); Sequence conflict (2); Signal peptide (1); Turn (9) FUNCTION: Converts sphingomyelin to ceramide. Also has phospholipase C activities toward 1,2-diacylglycerolphosphocholine and 1,2-diacylglycerolphosphoglycerol. {ECO:0000269|PubMed:27435900}. SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:P17405}. Secreted {ECO:0000269|PubMed:8702487}. SUBUNIT: Monomer. {ECO:0000269|PubMed:27435900}. +Q80WV3 CHST2_MOUSE Carbohydrate sulfotransferase 2 (EC 2.8.2.-) (Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 2) (GST-2) (N-acetylglucosamine 6-O-sulfotransferase 1) (GlcNAc6ST-1) (Gn6st-1) 530 57,828 Chain (1); Erroneous initiation (4); Glycosylation (3); Nucleotide binding (2); Sequence conflict (4); Topological domain (2); Transmembrane (1) TRANSMEM 55 75 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 54 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 76 530 Lumenal. {ECO:0000255}. FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of non-reducing N-acetylglucosamine (GlcNAc) residues within keratan-like structures on N-linked glycans and within mucin-associated glycans that can ultimately serve as SELL ligands. SELL ligands are present in high endothelial cells (HEVs) and play a central role in lymphocyte homing at sites of inflammation. Participates in biosynthesis of the SELL ligand sialyl 6-sulfo Lewis X and in lymphocyte homing to Peyer patches. Has no activity toward O-linked sugars. Its substrate specificity may be influenced by its subcellular location. Sulfates GlcNAc residues at terminal, non-reducing ends of oligosaccharide chains. {ECO:0000269|PubMed:15175329, ECO:0000269|PubMed:9712885}. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. SUBUNIT: Homodimer; disulfide-linked. Homodimerization is not essential for enzyme activity (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: In brain, it is expressed in pyramidal cells in the CA3 subregion of the hippocampus, cerebellar nucleus and Purkinje cells. {ECO:0000269|PubMed:9712885, ECO:0000269|PubMed:9722682}. +O88199 CHST3_MOUSE Carbohydrate sulfotransferase 3 (EC 2.8.2.17) (Chondroitin 6-O-sulfotransferase 1) (C6ST-1) (Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 0) (GST-0) 472 53,997 Chain (1); Glycosylation (6); Nucleotide binding (2); Topological domain (2); Transmembrane (1) TRANSMEM 20 38 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 19 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 39 472 Lumenal. {ECO:0000255}. FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of the N-acetylgalactosamine (GalNAc) residue of chondroitin. Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage and is distributed on the surfaces of many cells and extracellular matrices. Can also sulfate Gal residues of keratan sulfate, another glycosaminoglycan, and the Gal residues in sialyl N-acetyllactosamine (sialyl LacNAc) oligosaccharides. May play a role in the maintenance of naive T-lymphocytes in the spleen. {ECO:0000269|PubMed:11696535, ECO:0000269|PubMed:9597547}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. Highly expressed in spleen, lung, eye and stomach. Constitutively expressed at low level during the mid- to late-gestation period. Expressed in the brain in a temporally controlled manner: peaks at 2 weeks after birth in the cerebellum, but at 3 weeks in the cerebrum. Localizes to stromal cells in the bone marrow, and stromal cells in the marginal zone and red pulp of the spleen, but the sense probe did not. {ECO:0000269|PubMed:9597547}. +Q9QUP4 CHST5_MOUSE Carbohydrate sulfotransferase 5 (EC 2.8.2.-) (Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 4) (GST4) (Intestinal N-acetylglucosamine-6-O-sulfotransferase) (I-GlcNAc6ST) (Intestinal GlcNAc-6-sulfotransferase) (mIGn6ST) (N-acetylglucosamine 6-O-sulfotransferase 3) (GlcNAc6ST-3) (Gn6st-3) 395 44,537 Chain (1); Glycosylation (4); Nucleotide binding (2); Topological domain (2); Transmembrane (1) TRANSMEM 8 26 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 7 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 27 395 Lumenal. {ECO:0000255}. FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of non-reducing N-acetylglucosamine (GlcNAc) residues of keratan. Mediates sulfation of keratan in cornea. Keratan sulfate plays a central role in maintaining corneal transparency. Acts on the non-reducing terminal GlcNAc of short and long carbohydrate substrates that have poly-N-acetyllactosamine structures. May also have activity toward O-linked sugars of mucin-type acceptors. {ECO:0000269|PubMed:12218059}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Golgi membrane, early secretory pathway. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in cornea. {ECO:0000269|PubMed:11278593}. +Q61024 ASNS_MOUSE Asparagine synthetase [glutamine-hydrolyzing] (EC 6.3.5.4) (Glutamine-dependent asparagine synthetase) 561 64,283 Active site (1); Binding site (3); Chain (1); Domain (2); Initiator methionine (1); Modified residue (3); Nucleotide binding (1); Region (2); Sequence conflict (1); Site (1) Amino-acid biosynthesis; L-asparagine biosynthesis; L-asparagine from L-aspartate (L-Gln route): step 1/1. +Q91XQ5 CHSTF_MOUSE Carbohydrate sulfotransferase 15 (EC 2.8.2.33) (B-cell RAG-associated gene protein) (N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase) (GalNAc4S-6ST) 561 64,986 Binding site (2); Chain (1); Erroneous initiation (1); Glycosylation (1); Nucleotide binding (1); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 81 101 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 80 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 102 561 Lumenal. {ECO:0000255}. FUNCTION: Sulfotransferase that transfers sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to the C-6 hydroxyl group of the GalNAc 4-sulfate residue of chondroitin sulfate A and forms chondroitin sulfate E containing GlcA-GalNAc(4,6-SO(4)) repeating units. It also transfers sulfate to a unique non-reducing terminal sequence, GalNAc(4SO4)-GlcA(2SO4)-GalNAc(6SO4), to yield a highly sulfated structure similar to the structure found in thrombomodulin chondroitin sulfate. May also act as a B-cell receptor involved in BCR ligation-mediated early activation that mediate regulatory signals key to B-cell development and/or regulation of B-cell-specific RAG expression; however such results are unclear in vivo (By similarity). {ECO:0000250}. PTM: Glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Note=A small fraction may also be present at the cell surface, where it acts as a B-cell receptor. SUBUNIT: Homodimer; disulfide-linked (Potential). The relevance of homodimerization is however unsure. May interact with phosphorylated proteins in resting B-cells, including HCK (By similarity). {ECO:0000250, ECO:0000305}. +Q9CY57 CHTOP_MOUSE Chromatin target of PRMT1 protein (Friend of PRMT1 protein) (Small arginine- and glycine-rich protein) (SRAG) 249 26,585 Alternative sequence (3); Chain (1); Compositional bias (1); Cross-link (1); Erroneous initiation (3); Initiator methionine (1); Modified residue (5); Motif (1); Region (1); Sequence conflict (1) FUNCTION: Plays an important role in the ligand-dependent activation of estrogen receptor target genes (By similarity). May play a role in the silencing of fetal globin genes (PubMed:20688955). Recruits the 5FMC complex to ZNF148, leading to desumoylation of ZNF148 and subsequent transactivation of ZNF148 target genes (PubMed:22872859). Required for the tumorigenicity of glioblastoma cells. Binds to 5-hydroxymethylcytosine (5hmC) and associates with the methylosome complex containing PRMT1, PRMT5, MEP50 and ERH. The CHTOP-methylosome complex associated with 5hmC methylates H4R3 and transactivates genes involved in glioblastomagenesis (PubMed:25284789). {ECO:0000250|UniProtKB:Q9Y3Y2, ECO:0000269|PubMed:20688955, ECO:0000269|PubMed:22872859, ECO:0000269|PubMed:25284789}. PTM: Asymmetrically methylated by PRMT1. Symmetrically methylated by PRMT5. {ECO:0000269|PubMed:19858291}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19254951}. Nucleus, nucleolus {ECO:0000269|PubMed:19254951}. Nucleus, nucleoplasm {ECO:0000269|PubMed:19858291, ECO:0000269|PubMed:22872859}. Nucleus speckle {ECO:0000269|PubMed:19858291}. Note=Mostly associated with facultative heterochromatin. Localizes to regions surrounding nuclear speckles known as perispeckles in which TREX complex assembly seems to occur (By similarity). {ECO:0000250|UniProtKB:Q9Y3Y2, ECO:0000269|PubMed:19858291}. SUBUNIT: Interacts with PRMT1 and PRMT5 (PubMed:19858291, PubMed:22872859). Interacts with the 5FMC complex; the interaction is methylation-dependent. Interacts with FYTTD1, SET and PRC1 complex members CBX4, RNF2 and PHC2; the interactions are methylation-independent. Interacts with ZNF148 (PubMed:22872859). Interacts with WDR77 and ERH (By similarity). {ECO:0000250|UniProtKB:Q9Y3Y2, ECO:0000269|PubMed:19858291, ECO:0000269|PubMed:22872859}. TISSUE SPECIFICITY: Broadly expressed with highest levels found in thymus, spleen, and lymph nodes. Expressed in an erythroid progenitor cell line derived from fetal liver. {ECO:0000269|PubMed:19254951, ECO:0000269|PubMed:20688955}. +Q9DCQ2 ASPD_MOUSE Putative L-aspartate dehydrogenase (EC 1.4.1.21) (Aspartate dehydrogenase domain-containing protein) 287 30,270 Binding site (2); Chain (1); Modified residue (2); Sequence conflict (2) Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (dehydrogenase route): step 1/1. FUNCTION: Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate. {ECO:0000250}. +Q5BN45 CI116_MOUSE UPF0691 protein C9orf116 homolog (p53-induced expression in RB-null cells protein 1) (Pierce1) 167 18,836 Chain (1) TISSUE SPECIFICITY: Expressed in brain, lung, kidney and testis. {ECO:0000269|PubMed:18182857}. +Q3V0E1 CI131_MOUSE Uncharacterized protein C9orf131 homolog 1183 130,387 Chain (1); Sequence conflict (1) +Q9D187 CIA2B_MOUSE Cytosolic iron-sulfur assembly component 2B (Mitotic spindle-associated MMXD complex subunit MIP18) 163 17,667 Chain (1) FUNCTION: Component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into extramitochondrial Fe/S proteins. As a CIA complex component and in collaboration with CIAO1 and MMS19, binds to and facilitates the assembly of most cytosolic-nuclear Fe/S proteins. As part of the mitotic spindle-associated MMXD complex it plays a role in chromosome segregation, probably by facilitating iron-sulfur cluster assembly into ERCC2/XPD. {ECO:0000250|UniProtKB:Q9Y3D0}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y3D0}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9Y3D0}. SUBUNIT: Component of the CIA complex. Component of the MMXD complex, which includes CIAO1, ERCC2, CIAO2B, MMS19 and SLC25A5. Interacts with CIAO1, ERCC2 and MMS19; the interactions are direct. {ECO:0000250|UniProtKB:Q9Y3D0}. +P60824 CIRBP_MOUSE Cold-inducible RNA-binding protein (A18 hnRNP) (Glycine-rich RNA-binding protein CIRP) 172 18,607 Chain (1); Compositional bias (1); Domain (1); Modified residue (6); Mutagenesis (11) FUNCTION: Cold-inducible mRNA binding protein that plays a protective role in the genotoxic stress response by stabilizing transcripts of genes involved in cell survival. Promotes assembly of stress granules (SGs), when overexpressed. Seems to play an essential role in cold-induced suppression of cell proliferation. Acts as a translational repressor. Acts as a translational activator. Binds specifically to the 3'-untranslated regions (3'-UTRs) of stress-responsive transcripts RPA2 and TXN. {ECO:0000269|PubMed:17967451, ECO:0000269|PubMed:9151692}. PTM: Methylated on arginine residues. Methylation of the RGG motifs is a prerequisite for recruitment into SGs. {ECO:0000269|PubMed:17967451}.; PTM: Phosphorylated by CK2, GSK3A and GSK3B. Phosphorylation by GSK3B increases RNA-binding activity to the TXN 3'-UTR transcript upon exposure to UV radiation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:17967451}. Cytoplasm {ECO:0000269|PubMed:17967451}. Note=Translocates from the nucleus to the cytoplasm after exposure to UV radiation (By similarity). Translocates from the nucleus to the cytoplasm into stress granules upon various cytoplasmic stresses, such as osmotic and heat shocks. Its recruitment into stress granules occurs in the absence of TIAR proteins. {ECO:0000250}. SUBUNIT: Interacts with EIF4G1. Associates with ribosomes (By similarity). {ECO:0000250}. DOMAIN: Both the RRM domain and the arginine, glycine (RGG) rich domain are necessary for binding to the TXN 3'-untranslated region (By similarity). Both the RRM domain and the arginine, glycine (RGG) rich domain (RGG repeats) are necessary for optimal recruitment into SGs upon cellular stress. The C-terminal domain containing RGG repeats is necessary for translational repression. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. +Q91WS0 CISD1_MOUSE CDGSH iron-sulfur domain-containing protein 1 (MitoNEET) 108 12,097 Chain (1); Cross-link (9); Metal binding (4); Modified residue (3); Topological domain (1); Transmembrane (1) TRANSMEM 14 31 Helical; Signal-anchor for type III membrane protein. {ECO:0000255}. TOPO_DOM 32 108 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a key role in regulating maximal capacity for electron transport and oxidative phosphorylation. May be involved in Fe-S cluster shuttling and/or in redox reactions (By similarity). {ECO:0000250, ECO:0000269|PubMed:17376863}. PTM: Ubiquitinated by PRKN during mitophagy, leading to its degradation and enhancement of mitophagy. Deubiquitinated by USP30. {ECO:0000250|UniProtKB:Q9NZ45}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:17376863}; Single-pass type III membrane protein {ECO:0000269|PubMed:17376863}. SUBUNIT: Homodimer. {ECO:0000250}. TISSUE SPECIFICITY: Liver, adipose, skeletal muscle and heart (at protein level). Widely expressed. Expressed at the highest levels in the heart. {ECO:0000269|PubMed:17376863}. +P97370 AT1B3_MOUSE Sodium/potassium-transporting ATPase subunit beta-3 (Sodium/potassium-dependent ATPase subunit beta-3) (ATPB-3) (CD antigen CD298) 278 31,776 Chain (1); Disulfide bond (3); Glycosylation (2); Region (1); Topological domain (2); Transmembrane (1) TRANSMEM 36 56 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 35 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 57 278 Extracellular. {ECO:0000255}. FUNCTION: This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The exact function of the beta-3 subunit is not known. SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein. Melanosome {ECO:0000250}. SUBUNIT: The sodium/potassium-transporting ATPase is composed of a catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an additional regulatory subunit. {ECO:0000305}. DOMAIN: The C-terminal lobe folds into an immunoglobulin-like domain and may mediate cell adhesion properties. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. +Q9CQB5 CISD2_MOUSE CDGSH iron-sulfur domain-containing protein 2 (MitoNEET-related 1 protein) (Miner1) (Nervous system overexpressed protein 70) 135 15,242 Chain (1); Metal binding (4); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 38 60 Helical. {ECO:0000255}. TOPO_DOM 1 37 Lumenal. {ECO:0000255}.; TOPO_DOM 61 135 Cytoplasmic. {ECO:0000255}. FUNCTION: Regulator of autophagy that contributes to antagonize BECN1-mediated cellular autophagy at the endoplasmic reticulum. Participates in the interaction of BCL2 with BECN1 and is required for BCL2-mediated depression of endoplasmic reticulum Ca(2+) stores during autophagy. Contributes to BIK-initiated autophagy, while it is not involved in BIK-dependent activation of caspases. Involved in life span control, probably via its function as regulator of autophagy (By similarity). {ECO:0000250, ECO:0000269|PubMed:19451219}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19451219}; Single-pass membrane protein {ECO:0000269|PubMed:19451219}. Mitochondrion outer membrane {ECO:0000269|PubMed:19451219}; Single-pass membrane protein {ECO:0000269|PubMed:19451219}. Note=According to PubMed:19451219, it mainly localizes to the mitochondrion outer membrane and localizes only at low level to the endoplasmic reticulum. However, inverse results are observed in human cells. SUBUNIT: Homodimer. Interacts with BCL2; the interaction is direct and disrupted by BIK interaction with BCL2. Interacts with BCL2L1. Interacts with ITPR1 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Brain. {ECO:0000269|PubMed:17029606}. +Q62225 CISH_MOUSE Cytokine-inducible SH2-containing protein (CIS) (CIS-1) (Suppressor of cytokine signaling) (SOCS) 257 28,537 Chain (1); Domain (2) Protein modification; protein ubiquitination. FUNCTION: SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. CIS is involved in the negative regulation of cytokines that signal through the JAK-STAT5 pathway such as erythropoietin, prolactin and interleukin 3 (IL3) receptor. Inhibits STAT5 trans-activation by suppressing its tyrosine phosphorylation. May be a substrate-recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). {ECO:0000250, ECO:0000269|PubMed:9129017}. SUBUNIT: Stably associated with the tyrosine-phosphorylated IL3 receptor beta chain and tyrosine-phosphorylated EPO receptor (EPOR). TISSUE SPECIFICITY: Expressed in kidney, lung and liver. Detected to a lower extent in stomach and heart. +Q8R1K4 AT2L2_MOUSE 5-phosphohydroxy-L-lysine phospho-lyase (EC 4.2.3.134) (Alanine--glyoxylate aminotransferase 2-like 2) 467 51,966 Alternative sequence (3); Chain (1); Modified residue (1) FUNCTION: Catalyzes the pyridoxal-phosphate-dependent breakdown of 5-phosphohydroxy-L-lysine, converting it to ammonia, inorganic phosphate and 2-aminoadipate semialdehyde. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}. SUBUNIT: Homotetramer. {ECO:0000250}. +Q148W0 AT8B1_MOUSE Phospholipid-transporting ATPase IC (EC 7.6.2.1) (ATPase class I type 8B member 1) (P4-ATPase flippase complex alpha subunit ATP8B1) 1251 143,798 Active site (1); Chain (1); Metal binding (2); Modified residue (1); Mutagenesis (1); Sequence conflict (11); Topological domain (11); Transmembrane (10) TRANSMEM 122 142 Helical. {ECO:0000255}.; TRANSMEM 145 165 Helical. {ECO:0000255}.; TRANSMEM 340 360 Helical. {ECO:0000255}.; TRANSMEM 386 406 Helical. {ECO:0000255}.; TRANSMEM 953 973 Helical. {ECO:0000255}.; TRANSMEM 983 1003 Helical. {ECO:0000255}.; TRANSMEM 1033 1053 Helical. {ECO:0000255}.; TRANSMEM 1072 1092 Helical. {ECO:0000255}.; TRANSMEM 1095 1115 Helical. {ECO:0000255}.; TRANSMEM 1143 1163 Helical. {ECO:0000255}. TOPO_DOM 1 121 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 143 144 Exoplasmic loop. {ECO:0000255}.; TOPO_DOM 166 339 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 361 385 Exoplasmic loop. {ECO:0000255}.; TOPO_DOM 407 952 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 974 982 Exoplasmic loop. {ECO:0000255}.; TOPO_DOM 1004 1032 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1054 1071 Exoplasmic loop. {ECO:0000255}.; TOPO_DOM 1093 1094 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1116 1142 Exoplasmic loop. {ECO:0000255}.; TOPO_DOM 1164 1251 Cytoplasmic. {ECO:0000255}. FUNCTION: Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. May play a role in asymmetric distribution of phospholipids in the canicular membrane. Plays a role in bile salt homeostasis. In cooperation with ABCB4 may be involved in establishing integrity of the canalicular membrane thus protecting hepatocytes from bile salts. Involved in the microvillus formation in polarized epithelial cells; the function seems to be independent from its flippase activity. Required for the preservation of cochlear hair cells in the inner ear. Required for the preservation of cochlear hair cells in the inner ear. According PubMed:20852622 is proposed to act as cardiolipin transporter during inflammatory injury; the function is questioned by PubMed:21475228. {ECO:0000269|PubMed:14976163, ECO:0000269|PubMed:19478059, ECO:0000269|PubMed:20852622, ECO:0000269|PubMed:21475228, ECO:0000269|PubMed:21820390}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20852622}; Multi-pass membrane protein {ECO:0000269|PubMed:20852622}. Apical cell membrane {ECO:0000250|UniProtKB:O43520}. Cell projection, stereocilium {ECO:0000269|PubMed:20852622}. Endoplasmic reticulum {ECO:0000250|UniProtKB:O43520}. Golgi apparatus {ECO:0000250|UniProtKB:O43520}. Note=Exit from the endoplasmic reticulum requires the presence of TMEM30A or TMEM30B. Localizes to apical membranes in epithelial cells. {ECO:0000250|UniProtKB:O43520}. SUBUNIT: Component of a P4-ATPase flippase complex which consists of a catalytic alpha subunit and an accessory beta subunit. The probable flippase ATP8B1:TMEM30A complex can form an intermediate phosphoenzyme in vitro. Also interacts with beta subunit TMEM30B (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Hepatocytes, bile duct, intestinal epithelial cells (cholangiocytes and ileocytes), and pancreatic acinar cells. {ECO:0000269|PubMed:14976163}. +Q9CQQ7 AT5F1_MOUSE ATP synthase F(0) complex subunit B1, mitochondrial (ATP synthase peripheral stalk-membrane subunit b) (ATP synthase subunit b) (ATPase subunit b) 256 28,949 Chain (1); Modified residue (8); Transit peptide (1) FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements. SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane. SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Component of an ATP synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MD and MP68 (By similarity). {ECO:0000250}. +A3FIN4 AT8B5_MOUSE Phospholipid-transporting ATPase FetA (EC 7.6.2.1) (ATPase class I type 8B member 2-like protein) (ATPase class I type 8B member 5) (Flippase expressed in testis A) 1183 135,899 Active site (1); Alternative sequence (4); Chain (1); Metal binding (2); Sequence conflict (1); Transmembrane (9) TRANSMEM 96 116 Helical. {ECO:0000255}.; TRANSMEM 299 319 Helical. {ECO:0000255}.; TRANSMEM 348 368 Helical. {ECO:0000255}.; TRANSMEM 904 924 Helical. {ECO:0000255}.; TRANSMEM 927 947 Helical. {ECO:0000255}.; TRANSMEM 981 1001 Helical. {ECO:0000255}.; TRANSMEM 1014 1034 Helical. {ECO:0000255}.; TRANSMEM 1049 1069 Helical. {ECO:0000255}.; TRANSMEM 1090 1110 Helical. {ECO:0000255}. FUNCTION: P4-ATPase flippase which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. May play a role in phospholid transport across membranes and in acrosome formation. {ECO:0000269|PubMed:19657017}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome membrane {ECO:0000269|PubMed:19657017}; Multi-pass membrane protein {ECO:0000269|PubMed:19657017}. TISSUE SPECIFICITY: Highly expressed in testis. {ECO:0000269|PubMed:19657017}. +Q925I1 ATAD3_MOUSE ATPase family AAA domain-containing protein 3 (AAA-ATPase TOB3) 591 66,742 Alternative sequence (1); Chain (1); Coiled coil (1); Initiator methionine (1); Modified residue (5); Nucleotide binding (1); Region (2); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 246 263 Helical. {ECO:0000255}. TOPO_DOM 2 245 Mitochondrial intermembrane. {ECO:0000255}.; TOPO_DOM 264 586 Mitochondrial matrix. {ECO:0000255}. FUNCTION: Essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organism and cellular level. May play an important role in mitochondrial protein synthesis. May also participate in mitochondrial DNA replication. May bind to mitochondrial DNA D-loops and contribute to nucleoid stability. Required for enhanced channeling of cholesterol for hormone-dependent steroidogenesis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Mitochondrion matrix, mitochondrion nucleoid {ECO:0000250}. Note=In the mitochondrial inner membrane, enriched in sites with the potential to form contacts with the outer membrane. The N-terminal domain interacts with the inner surface of the mitochondrial outer membrane and the C-terminal domain localizes in a specific matrix compartment, where it is associated with nucleoids (By similarity). {ECO:0000250}. SUBUNIT: Can form homooligomers. Homodimer formation at the N-terminus may be regulated by ATP and is required for the interaction with the inner surface of the mitochondrial outer membrane and correct mitochondrial homeostasis. Interacts with components of the mitochondrial ribosome and with other proteins involved in mitochondrial RNA metabolism. May also interact with protein involved in lipid metabolism, including STARD9. May interact with FAM210A. Interacts with GADD45GIP1. Interacts with S100B in a Ca(+2)- and Zn(+2)-dependent manner; this interaction probably occurs in the cytosol prior to mitochondrial targeting. S100B could assist ATAD3A cytoplasmic processing, preventing aggregation and favoring mitochondrial localization. Interacts with HSP60/HSPD1. Forms heterooligomers with ATAD3B; this interaction may affect ATAD3A activity (By similarity). {ECO:0000250}. DOMAIN: The transmembrane domain and a C-terminal adjacent region contain all information necessary for mitochondrial targeting. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in heart, spleen, kidney, liver and at smaller levels, in lung and muscle (at protein level). {ECO:0000269|PubMed:20332122}. +O70191 ATF5_MOUSE Cyclic AMP-dependent transcription factor ATF-5 (cAMP-dependent transcription factor ATF-5) (Activating transcription factor 5-alpha/beta) (BZIP protein ATF7) (NAP1) (NRIF3-associated protein) (Transcription factor ATFx) (Transcription factor-like protein ODA-10) 283 30,331 Chain (1); Compositional bias (1); Domain (1); Modified residue (2); Mutagenesis (2); Region (4); Sequence conflict (1) FUNCTION: Transcription factor that either stimulates or represses gene transcription through binding of different DNA regulatory elements such as cAMP response element (CRE) (consensus: 5'-GTGACGT[AC][AG]-3'), ATF5-specific response element (ARE) (consensus: 5'-C[CT]TCT[CT]CCTT[AT]-3') but also the amino acid response element (AARE), present in many viral and cellular promoters. Critically involved, often in a cell type-dependent manner, in cell survival, proliferation, and differentiation. Its transcriptional activity is enhanced by CCND3 and slightly inhibited by CDK4 (By similarity). Important regulator of the cerebral cortex formation, functions in cerebral cortical neuroprogenitor cells to maintain proliferation and to block differentiation into neurons. Must be down-regulated in order for such cells to exit the cycle and differentiate. Participates in the pathways by which SHH promotes cerebellar granule neuron progenitor cells proliferation (PubMed:22095825). Critical for survival of mature olfactory sensory neurons (OSN), directs expression of OSN-specific genes (PubMed:23090999). May be involved in osteogenic differentiation. Promotes cell proliferation and survival by inducing the expression of EGR1 sinergistically with ELK1. Once acetylated by EP300, binds to ARE sequences on target genes promoters, such as BCL2 and EGR1 (By similarity). Plays an anti-apoptotic role through the transcriptional regulation of BCL2, this function seems to be cell type-dependent (By similarity) (PubMed:12130540). Cooperates with NR1I3/CAR in the transcriptional activation of CYP2B6 in liver. In hepatic cells, represses CRE-dependent transcription and inhibits proliferation by blocking at G2/M phase. May act as a negative regulator of IL1B transduction pathway in liver. Upon IL1B stimulus, cooperates with NLK to activate the transactivation activity of C/EBP subfamily members. Besides its function of transcription factor, acts as a cofactor of CEBPB to activate CEBPA and promote adipocyte differentiation. Regulates centrosome dynamics in a cell-cycle- and centriole-age-dependent manner. Forms 9-foci symmetrical ring scaffold around the mother centriole to control centrosome function and the interaction between centrioles and pericentriolar material (By similarity). {ECO:0000250|UniProtKB:Q6P788, ECO:0000250|UniProtKB:Q9Y2D1, ECO:0000269|PubMed:12130540, ECO:0000269|PubMed:22095825, ECO:0000269|PubMed:23090999}. PTM: Acetylated at Lys-29 by EP300, the acetylation enhances the interaction with CEBPB, DNA-binding and transactivation activity. {ECO:0000269|PubMed:24216764}.; PTM: Ubiquitinated by CDC34 and UBE2B in order to be degraded by the proteasome. Cisplatin inhibits ubiquitination and proteasome-mediated degradation by inhibiting the interaction with CDC34. Ubiquitination and degradation by the proteasome are inhibited by NLK in a kinase-independent manner. {ECO:0000250|UniProtKB:Q9Y2D1}.; PTM: Phosphorylated by NLK, probably at Ser-92 and Ser-126. {ECO:0000250|UniProtKB:Q9Y2D1}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y2D1}. Nucleus {ECO:0000269|PubMed:22095825}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9Y2D1}. Note=Actively transported to the centrosome and accumulated in the pericentriolar material (PCM) during G1 to M phase via a microtubule-dependent mechanism. During late telophase and cytokinesis, translocates from the centrosome to the midbody. {ECO:0000250|UniProtKB:Q9Y2D1}. SUBUNIT: Binds DNA as a dimer. Interacts with PTP4A1/PRL-1 (By similarity). Interacts with CCND3, but not with CCND1 or CCND2. Interacts with HSPA1A or HSPA1B; the interaction protects ATF5 from degradation via proteasome-dependent and caspase-dependent processes. Interacts (via C-terminal region) with NPM1 (via C-terminal region); the interaction leads to loss of association between HSPA1A or HSPA1B and ATF5 and promotes ATF5 degradation via proteasome-dependent and caspase-dependent processes. Interacts with NLK; the interaction stabilizes ATF5 at the protein level in a kinase-independent manner. Interacts with alpha-tubulin, gamma-tubulin members TUBGCP2 and TUBGCP4, PCNT; the ATF5:PCNT:polyglutamylated tubulin (PGT) tripartite unites the mother centriole and the pericentriolar material (PCM) in the centrosome (By similarity). Interacts with CEBPB and EP300; EP300 is required for ATF5 and CEBPB interaction and DNA binding (PubMed:24216764). {ECO:0000250|UniProtKB:Q9Y2D1, ECO:0000269|PubMed:11278933, ECO:0000269|PubMed:24216764}. TISSUE SPECIFICITY: Highly expressed in liver and at lower levels in heart, brain, lung, kidney, adipose tissue, and skeletal muscle. Expressed in some immature and in all mature olfactory sensory neurons (at protein level) (PubMed:23090999). {ECO:0000269|PubMed:11278933, ECO:0000269|PubMed:12213205, ECO:0000269|PubMed:23090999}. +Q8BHE3 ATCAY_MOUSE Caytaxin 372 42,178 Chain (1); Domain (1); Modified residue (1); Region (2); Site (1) FUNCTION: Functions in the development of neural tissues, particularly the postnatal maturation of the cerebellar cortex. May play a role in neurotransmission through regulation of glutaminase/GLS, an enzyme responsible for the production in neurons of the glutamate neurotransmitter. Alternatively, may regulate the localization of mitochondria within axons and dendrites. {ECO:0000269|PubMed:19861499}. PTM: Cleaved by CASP3 and CASP7. The potential C-terminal product released by CASP3 cleavage may inhibit the ERK signaling pathway through MAP2K2. {ECO:0000269|PubMed:21369758}.; PTM: May be ubiquitinated by STUB1. {ECO:0000250}. SUBCELLULAR LOCATION: Cell projection, axon {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cell junction, synapse {ECO:0000250}. Cytoplasm. Mitochondrion envelope. Note=Localizes presynaptically into neuron projections. SUBUNIT: Interacts with KLC1; may link mitochondria to KLC1 and regulate mitochondria localization into neuron projections. Interacts with GLS; the interaction is direct and may control GLS localization, negatively regulating its activity. Interacts with PIN1 (via WW domain); upon NGF stimulation (By similarity). The interaction with PIN1 and GLS is competitive (By similarity). {ECO:0000250}. DOMAIN: The CRAL-TRIO domain is known to bind small hydrophobic molecules. {ECO:0000250}. TISSUE SPECIFICITY: Neuronal tissues specific. Strongly expressed in brain. Expressed in virtually all parts of the adult brain, including cortex, cerebellum and olfactory bulbs. Enriched in hippocampus, cerebellar cortex, deep cerebellar nuclei, and pontine nuclei (at protein level). {ECO:0000269|PubMed:14556008, ECO:0000269|PubMed:16899818, ECO:0000269|PubMed:17157273}. DISEASE: Note=Defects in Atcay are the cause of jittery phenotype, which is characterized by severe truncal and limb ataxia and death due to starvation and dehydration by 3-4 weeks of age. {ECO:0000269|PubMed:14556008}. +Q91YI1 ATG13_MOUSE Autophagy-related protein 13 516 56,441 Alternative sequence (1); Chain (1); Modified residue (4); Motif (1); Region (1); Sequence caution (1) FUNCTION: Autophagy factor required for autophagosome formation and mitophagy. Target of the TOR kinase signaling pathway that regulates autophagy through the control of the phosphorylation status of ATG13 and ULK1, and the regulation of the ATG13-ULK1-RB1CC1 complex. Through its regulation of ULK1 activity, plays a role in the regulation of the kinase activity of mTORC1 and cell proliferation. {ECO:0000269|PubMed:19258318}. PTM: Phosphorylated by ULK1, ULK2 and mTOR. Phosphorylation status depends on nutrient-rich conditions; dephosphorylated during starvation or following treatment with rapamycin. ULK1-mediated phosphorylation of ATG13 at Ser-354 is required for efficient clearance of depolarized mitochondria. {ECO:0000250|UniProtKB:O75143}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:19211835, ECO:0000269|PubMed:19258318}. Preautophagosomal structure {ECO:0000269|PubMed:19211835, ECO:0000269|PubMed:19258318}. Note=Under starvation conditions, is localized to puncate structures primarily representing the isolation membrane that sequesters a portion of the cytoplasm resulting in the formation of an autophagosome. {ECO:0000269|PubMed:19211835, ECO:0000269|PubMed:19258318}. SUBUNIT: Part of a complex consisting of ATG13, ULK1 and RB1CC1 (PubMed:19258318, PubMed:19211835). Interacts with ATG101 (By similarity). Interacts with ULK1 (via C-terminus) (By similarity). Interacts with ULK2 (via C-terminus) (By similarity). Interacts (via the LIR motif) with GABARAP, GABARAPL and GABARAPL2 (By similarity). Interacts (via the LIR motif) with MAP1LC3A, MAP1LC3B and MAP1LC3C (By similarity). Interacts with TAB2 and TAB3 (By similarity). Interacts with C9orf72 (By similarity). {ECO:0000250|UniProtKB:O75143, ECO:0000269|PubMed:19211835, ECO:0000269|PubMed:19258318}. DOMAIN: The LIR motif (LC3-interacting region) is required for the interaction with the ATG8 family proteins GABARAP, GABARAPL, GABARAPL2, and MAP1LC3A. {ECO:0000250|UniProtKB:O75143}. +Q60765 ATF3_MOUSE Cyclic AMP-dependent transcription factor ATF-3 (cAMP-dependent transcription factor ATF-3) (Activating transcription factor 3) (Transcription factor LRG-21) 181 20,722 Chain (1); Cross-link (2); Domain (1); Modified residue (1); Region (2) FUNCTION: This protein binds the cAMP response element (CRE) (consensus: 5'-GTGACGT[AC][AG]-3'), a sequence present in many viral and cellular promoters. Represses transcription from promoters with ATF sites. It may repress transcription by stabilizing the binding of inhibitory cofactors at the promoter (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Binds DNA as a homodimer or a heterodimer. +P97769 CITE1_MOUSE Cbp/p300-interacting transactivator 1 (Melanocyte-specific protein 1) 203 20,800 Chain (1); Compositional bias (1); Motif (1) FUNCTION: Transcriptional coactivator of the p300/CBP-mediated transcription complex. Enhances SMAD-mediated transcription by strengthening the functional link between the DNA-binding SMAD transcription factors and the p300/CBP transcription coactivator complex. Stimulates estrogen-dependent transactivation activity mediated by estrogen receptors signaling; stabilizes the interaction of estrogen receptor ESR1 and histone acetyltransferase EP300. Positively regulates TGF-beta signaling through its association with the SMAD/p300/CBP-mediated transcriptional coactivator complex. Induces transcription from estrogen-responsive promoters and protection against cell death. Potentiates EGR2-mediated transcriptional activation activity from the ERBB2 promoter. Acts as an inhibitor of osteoblastic mineralization through a cAMP-dependent parathyroid hormone receptor signaling. May play a role in pigmentation of melanocytes. Associates with chromatin to the estrogen-responsive TGF-alpha promoter region in a estrogen-dependent manner. {ECO:0000269|PubMed:10722728, ECO:0000269|PubMed:14673158, ECO:0000269|PubMed:18187554}. PTM: Phosphorylated. Phosphorylation changes in a cell cycle-dependent manner and reduces its transcriptional cofactor activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11581164, ECO:0000269|PubMed:14673158, ECO:0000269|PubMed:17938205}. Cytoplasm {ECO:0000250}. Note=Shuttles between the nucleus and the cytoplasm by a nuclear export signal (NES) and in a CRM1-dependent manner. {ECO:0000250}. SUBUNIT: Homodimer. Binds to RBM14. Interacts (via N-terminus) with HSPA8; the interaction suppresses the association of CITED1 with p300/CBP and SMAD-mediated transcription transactivation. Interacts (via C-terminus) with TOX3 (via HGM box); the interaction increases estrogen-response element (ERE)-dependent transcription and protection against cell death. Interacts with ESR1; the interaction occurs in a estrogen-dependent manner (By similarity). Interacts (unphosphorylated form preferentially and via C-terminus) with EP300. Interacts (via C-terminus) with CREBBP. Interacts with EGR2. {ECO:0000250, ECO:0000269|PubMed:10722728, ECO:0000269|PubMed:17938205}. TISSUE SPECIFICITY: Expressed in calvarial osteoblasts. Expressed in nulliparous mammary epithelial cells; absent in pregnant mice and in lacting mammary glands. Also expressed in mammary tumors (at protein level). Expressed only in melanocytes and testis. Expressed at high levels in the strongly pigmented melanoma cells but at low levels in the weakly pigmented cells. {ECO:0000269|PubMed:11581164, ECO:0000269|PubMed:17938205, ECO:0000269|PubMed:18187554}. +O35740 CITE2_MOUSE Cbp/p300-interacting transactivator 2 (MSG-related protein 1) (MRG-1) (P35srj) 269 28,321 Alternative sequence (3); Chain (1); Compositional bias (3); Sequence conflict (2) FUNCTION: Transcriptional coactivator of the p300/CBP-mediated transcription complex. Acts as a bridge, linking TFAP2 transcription factors and the p300/CBP transcriptional coactivator complex in order to stimulate TFAP2-mediated transcriptional activation. Positively regulates TGF-beta signaling through its association with the SMAD/p300/CBP-mediated transcriptional coactivator complex. Stimulates the peroxisome proliferator-activated receptors PPARA transcriptional activity. Enhances estrogen-dependent transactivation mediated by estrogen receptors. Acts also as a transcriptional corepressor; interferes with the binding of the transcription factors HIF1A or STAT2 and the p300/CBP transcriptional coactivator complex. Participates in sex determination and early gonad development by stimulating transcription activation of SRY. Plays a role in controlling left-right patterning during embryogenesis; potentiates transcriptional activation of NODAL-mediated gene transcription in the left lateral plate mesoderm (LPM). Plays an essential role in differentiation of the adrenal cortex from the adrenogonadal primordium (AGP); stimulates WT1-mediated transcription activation thereby up-regulating the nuclear hormone receptor NR5A1 promoter activity. Associates with chromatin to the PITX2 P1 promoter region. {ECO:0000269|PubMed:10593900, ECO:0000269|PubMed:15475956, ECO:0000269|PubMed:15750185, ECO:0000269|PubMed:16619037, ECO:0000269|PubMed:17537799, ECO:0000269|PubMed:19457926, ECO:0000269|PubMed:21224256}. SUBCELLULAR LOCATION: Nucleus. Note=Colocalizes with EP300 in dot-like structures. {ECO:0000250}. SUBUNIT: Interacts (via C-terminus) with EP300 (via CH1 domain); the interaction is stimulated in response to hypoxia. Interacts with PPARA. Interacts (via C-terminus) with TFAP2A, TFAP2B and TFAP2C (By similarity). Interacts (via C-terminus) with SMAD2. Interacts (via C-terminus) with SMAD3 (via MH2 domain). Interacts with LHX2 (via LIM domains). Interacts with WT1 isoform 1 and isoform 3. {ECO:0000250, ECO:0000269|PubMed:10593900, ECO:0000269|PubMed:16619037, ECO:0000269|PubMed:17537799}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15051727}. +Q8CF31 CK094_MOUSE Uncharacterized protein C11orf94 homolog 99 11,064 Chain (1); Erroneous gene model prediction (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q9DAE7 CK097_MOUSE Uncharacterized protein C11orf97 homolog 121 13,565 Chain (1) SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:27914912, ECO:0000269|PubMed:28666954}. TISSUE SPECIFICITY: Predominantly expressed in tissues containing motile cilia (PubMed:28666954, PubMed:27914912). Also expressed in non-motile ciliated adult olfactory bulbs (PubMed:28666954). {ECO:0000269|PubMed:27914912, ECO:0000269|PubMed:28666954}. +Q9D937 CK098_MOUSE Uncharacterized protein C11orf98 homolog 123 14,099 Chain (1) +Q6QWF9 CK2N1_MOUSE Calcium/calmodulin-dependent protein kinase II inhibitor 1 (calcium/calmodulin-dependent protein kinase II inhibitor alpha) (mCaMKIINalpha) 78 8,513 Chain (1); Region (1) FUNCTION: Potent and specific inhibitor of CaM-kinase II (CAMK2). {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, synapse, synaptosome {ECO:0000269|PubMed:17350603}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000269|PubMed:17350603}. SUBUNIT: Interacts with CAMK2B; the presence of Ca(2+)/calmodulin increases the interaction but is not essential. Interacts with CAMK2A; this interaction requires CAMK2A activation by Ca(2+) (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Brain specific (at protein level). {ECO:0000269|PubMed:17350603}. +Q68FE2 ATG9A_MOUSE Autophagy-related protein 9A (APG9-like 1) 551 63,138 Chain (1); Glycosylation (1); Initiator methionine (1); Modified residue (5); Transmembrane (5) TRANSMEM 73 93 Helical. {ECO:0000255}.; TRANSMEM 132 152 Helical. {ECO:0000255}.; TRANSMEM 290 310 Helical. {ECO:0000255}.; TRANSMEM 372 392 Helical. {ECO:0000255}.; TRANSMEM 401 421 Helical. {ECO:0000255}. FUNCTION: Involved in autophagy and cytoplasm to vacuole transport (Cvt) vesicle formation. Plays a key role in the organization of the preautophagosomal structure/phagophore assembly site (PAS), the nucleating site for formation of the sequestering vesicle. Cycles between a juxta-nuclear trans-Golgi network compartment and late endosomes. Nutrient starvation induces accumulation on autophagosomes. Starvation-dependent trafficking requires ULK1, ATG13 and SUPT20H (By similarity). Required for carbonyl cyanide m-chlorophenylhydrazone (CCCP)-induced ATG8 family proteins lipidation, a key autophagy step. {ECO:0000250, ECO:0000269|PubMed:23402761}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Late endosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with SUPT20H. {ECO:0000250}. +Q6EBV9 ATG9B_MOUSE Autophagy-related protein 9B (APG9-like 2) (Nitric oxide synthase 3-overlapping antisense gene protein) 922 101,913 Chain (1); Compositional bias (1); Erroneous initiation (1); Sequence conflict (2); Topological domain (7); Transmembrane (6) TRANSMEM 207 227 Helical. {ECO:0000255}.; TRANSMEM 276 296 Helical. {ECO:0000255}.; TRANSMEM 438 458 Helical. {ECO:0000255}.; TRANSMEM 524 544 Helical. {ECO:0000255}.; TRANSMEM 551 571 Helical. {ECO:0000255}.; TRANSMEM 625 645 Helical. {ECO:0000255}. TOPO_DOM 1 206 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 228 275 Lumenal. {ECO:0000250}.; TOPO_DOM 297 437 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 459 523 Lumenal. {ECO:0000250}.; TOPO_DOM 545 550 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 572 624 Lumenal. {ECO:0000250}.; TOPO_DOM 646 922 Cytoplasmic. {ECO:0000250}. FUNCTION: Involved in autophagy and cytoplasm to vacuole transport (Cvt) vesicle formation. Plays a key role in the organization of the preautophagosomal structure/phagophore assembly site (PAS), the nucleating site for formation of the sequestering vesicle. {ECO:0000269|PubMed:15755735}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:15755735}; Multi-pass membrane protein {ECO:0000269|PubMed:15755735}. TISSUE SPECIFICITY: Expressed in heart, brain, and placenta and testis. {ECO:0000269|PubMed:15234981, ECO:0000269|PubMed:15755735}. +Q8BMK4 CKAP4_MOUSE Cytoskeleton-associated protein 4 (63-kDa cytoskeleton-linking membrane protein) (Climp-63) (p63) 575 63,692 Chain (1); Coiled coil (3); Erroneous initiation (2); Lipidation (1); Modified residue (7); Sequence caution (1); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 86 108 Helical. {ECO:0000255}. TOPO_DOM 1 85 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 109 575 Extracellular. {ECO:0000255}. FUNCTION: High-affinity epithelial cell surface receptor for APF. {ECO:0000250}.; FUNCTION: Mediates the anchoring of the endoplasmic reticulum to microtubules. {ECO:0000250}. PTM: Reversibly palmitoylated. Palmitoylation at Cys-79 by DHHC2 is required for its trafficking from the ER to the plasma membrane and for its perinuclear localization (By similarity). {ECO:0000250}.; PTM: Increased phosphorylation during mitosis prevents binding to microtubules. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein. Cell membrane; Single-pass type II membrane protein. Cytoplasm, cytoskeleton. Cytoplasm, perinuclear region. Note=Translocates to the perinuclear region upon APF-stimulation. {ECO:0000250}. +A2AGT5 CKAP5_MOUSE Cytoskeleton-associated protein 5 2032 225,635 Alternative sequence (2); Chain (1); Modified residue (4); Region (6); Repeat (10); Sequence caution (1); Sequence conflict (15) FUNCTION: Binds to the plus end of microtubules and regulates microtubule dynamics and microtubule organization. Acts as processive microtubule polymerase. Promotes cytoplasmic microtubule nucleation and elongation. Plays a major role in organizing spindle poles. In spindle formation protects kinetochore microtubules from depolymerization by KIF2C and has an essential role in centrosomal microtubule assembly independently of KIF2C activity. Contributes to centrosome integrity. Acts as component of the TACC3/ch-TOG/clathrin complex proposed to contribute to stabilization of kinetochore fibers of the mitotic spindle by acting as inter-microtubule bridge. The TACC3/ch-TOG/clathrin complex is required for the maintenance of kinetochore fiber tension. Enhances the strength of NDC80 complex-mediated kinetochore-tip microtubule attachments. {ECO:0000250|UniProtKB:Q14008}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q14008}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q14008}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q14008}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q14008}. Note=Detected on centrosomes and kinetochores during interphase and mitosis independently from TACC3 and clathrin. Located to spindle poles and microtubules during mitosis. In complex with TACC3 localized to microtubule plus-ends in mitosis and interphase. In complex with TACC3 and clathrin localized to inter-microtubule bridges in mitotic spindles. Accumulation sites at microtubule plus ends protruded approximately 100 nm from MAPRE1/EB1 sites in interphase cells. {ECO:0000250|UniProtKB:Q14008}. SUBUNIT: Interacts with TACC1. Interacts with HNRNPA2B1. Interacts with TACC3 independently of clathrin. Interacts with TACC3 and clathrin forming the TACC3/ch-TOG/clathrin complex located at spindle inter-microtubules bridges. Interacts with NDC80; indicative for an association with the NDC80 complex. Interacts with SLAIN2 (By similarity). Interacts with SLAIN1 (PubMed:21646404). {ECO:0000250|UniProtKB:Q14008, ECO:0000269|PubMed:21646404}. DOMAIN: The TOG (tumor overexpressed gene) domains are arranged in a N-terminal pentameric array with each domain composed of six (for the most part non-canonical) HEAT repeats forming a oblong paddle-like structure. Intra-HEAT loops are positioned along a face of the TOG domain and bind to a single alpha/beta-tubulin heterodimer. The TOG domains in the array seem to be structurally and functionally polarized. Differential functions may range from microtubule (MT) lattice binding and/or free tubulin heterodimer binding to potentiating stable incorporation of tubulin into the MT lattice. {ECO:0000250|UniProtKB:Q14008}. +Q8BLI0 ATL1_MOUSE ADAMTS-like protein 1 (ADAMTSL-1) (Punctin-1) 1745 192,008 Alternative sequence (2); Chain (1); Disulfide bond (13); Domain (14); Glycosylation (4); Signal peptide (1) PTM: Glycosylated (By similarity). O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS family members. Also can be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated. These other glycosylations can also facilitate secretion (By similarity). {ECO:0000250}.; PTM: Disulfide bonds are present. {ECO:0000250|UniProtKB:Q96RW4}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q96RW4}. +Q7TSK7 ATL2_MOUSE ADAMTS-like protein 2 (ADAMTSL-2) (TSP1-repeat-containing protein 1) (TCP-1) 957 105,647 Chain (1); Disulfide bond (3); Domain (8); Glycosylation (10); Sequence conflict (2); Signal peptide (1) PTM: Glycosylated (By similarity). Can be O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS family members. Also can be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated. These other glycosylations can also facilitate secretion (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. SUBUNIT: Interacts with LTBP1. {ECO:0000250}. +Q8CCC3 CL056_MOUSE Uncharacterized protein C12orf56 homolog 530 59,886 Chain (1) +Q810N5 CL060_MOUSE Uncharacterized protein C12orf60 homolog 247 28,062 Chain (1); Sequence conflict (5) +Q80VP5 CL065_MOUSE Probable peptide chain release factor C12orf65 homolog, mitochondrial 184 20,787 Alternative sequence (2); Beta strand (4); Chain (1); Coiled coil (1); Helix (2); Region (1); Sequence conflict (1); Transit peptide (1); Turn (1) FUNCTION: May act as a codon-independent translation release factor that has lost all stop codon specificity and directs the termination of translation in mitochondrion. May help rescuing stalled mitoribosomes during translation (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. DOMAIN: The GGQ domain may interact with the peptidyltransferase center (PTC) of the large ribosomal subunit to trigger peptidyl-tRNA hydrolysis. {ECO:0000269|PubMed:22821833}. +Q6P1I3 CL066_MOUSE KICSTOR complex protein C12orf66 homolog 445 50,256 Alternative sequence (2); Beta strand (6); Chain (1); Frameshift (2); Helix (15); Sequence conflict (1); Turn (3) FUNCTION: As part of the KICSTOR complex functions in the amino acid-sensing branch of the TORC1 signaling pathway. Recruits, in an amino acid-independent manner, the GATOR1 complex to the lysosomal membranes and allows its interaction with GATOR2 and the RAG GTPases. Functions upstream of the RAG GTPases and is required to negatively regulate mTORC1 signaling in absence of amino acids. In absence of the KICSTOR complex mTORC1 is constitutively localized to the lysosome and activated. The KICSTOR complex is also probably involved in the regulation of mTORC1 by glucose. {ECO:0000250|UniProtKB:Q96MD2}. SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q96MD2}. SUBUNIT: Part of the KICSTOR complex composed of KPTN, ITFG2, C12orf66 and SZT2. SZT2 probably serves as a link between the other three proteins in the KICSTOR complex and may mediate the direct interaction with the GATOR complex via GATOR1. The KICSTOR complex interacts directly with the GATOR1 complex and most probably indirectly with the GATOR2 complexe in an amino acid-independent manner. {ECO:0000250|UniProtKB:Q96MD2}. +Q80W69 CL071_MOUSE Uncharacterized protein C12orf71 homolog 301 34,755 Alternative sequence (1); Chain (1); Sequence conflict (4) +Q8BTC1 CL073_MOUSE Uncharacterized protein C12orf73 homolog 67 7,540 Chain (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q149M0 CL12B_MOUSE C-type lectin domain family 12 member B 275 31,186 Chain (1); Disulfide bond (2); Domain (1); Glycosylation (3); Modified residue (1); Motif (1); Sequence conflict (7); Topological domain (2); Transmembrane (1) TRANSMEM 42 64 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 41 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 65 275 Extracellular. {ECO:0000255}. FUNCTION: Cell surface receptor that protects target cells against natural killer cell-mediated lysis. Modulates signaling cascades and mediates tyrosine phosphorylation of target MAP kinases (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. SUBUNIT: Homodimer. Interacts with PTPN6 and PTPN11 (By similarity). {ECO:0000250}. DOMAIN: Contains 1 copy of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is involved in modulation of cellular responses. The phosphorylated ITIM motif can bind the SH2 domain of several SH2-containing phosphatases (By similarity). {ECO:0000250}. +Q6PA06 ATLA2_MOUSE Atlastin-2 (EC 3.6.5.-) (ADP-ribosylation factor-like protein 6-interacting protein 2) (ARL-6-interacting protein 2) (Aip-2) 583 66,224 Alternative sequence (1); Chain (1); Coiled coil (1); Compositional bias (1); Domain (1); Modified residue (2); Nucleotide binding (4); Sequence conflict (1); Topological domain (3); Transmembrane (2) TRANSMEM 477 497 Helical. {ECO:0000255}.; TRANSMEM 500 520 Helical. {ECO:0000255}. TOPO_DOM 1 476 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 498 499 Lumenal. {ECO:0000255}.; TOPO_DOM 521 583 Cytoplasmic. {ECO:0000250}. FUNCTION: GTPase tethering membranes through formation of trans-homooligomers and mediating homotypic fusion of endoplasmic reticulum membranes. Functions in endoplasmic reticulum tubular network biogenesis. {ECO:0000250|UniProtKB:Q8NHH9}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8NHH9}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8NHH9}. Note=Localizes at endoplasmic reticulum (ER) three-way tubular junctions. {ECO:0000250|UniProtKB:Q8NHH9}. SUBUNIT: Interacts with REEP5 and RTN3 (PubMed:19665976). Interacts with ZFYVE27 (By similarity). {ECO:0000250|UniProtKB:Q8NHH9, ECO:0000269|PubMed:19665976}. +Q91YH5 ATLA3_MOUSE Atlastin-3 (EC 3.6.5.-) 541 60,575 Alternative sequence (1); Chain (1); Domain (1); Erroneous initiation (1); Modified residue (1); Nucleotide binding (4); Sequence conflict (3); Topological domain (3); Transmembrane (2) TRANSMEM 446 466 Helical. {ECO:0000255}.; TRANSMEM 468 488 Helical. {ECO:0000255}. TOPO_DOM 1 445 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 467 467 Lumenal. {ECO:0000255}.; TOPO_DOM 489 541 Cytoplasmic. {ECO:0000250}. FUNCTION: GTPase tethering membranes through formation of trans-homooligomers and mediating homotypic fusion of endoplasmic reticulum membranes. Functions in endoplasmic reticulum tubular network biogenesis (By similarity). {ECO:0000250|UniProtKB:Q6DD88}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q6DD88}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to endoplasmic reticulum tubules and accumulates in punctuate structures corresponding to 3-way junctions, which represent crossing-points at which the tubules build a polygonal network. {ECO:0000250|UniProtKB:Q6DD88}. SUBUNIT: Interacts with ZFYVE27. {ECO:0000250|UniProtKB:Q6DD88}. +Q8C1T8 CLC2H_MOUSE C-type lectin domain family 2 member H (C-type lectin-related protein F) (Clr-f) 218 24,162 Chain (1); Disulfide bond (2); Domain (1); Erroneous initiation (1); Glycosylation (1); Natural variant (1); Topological domain (2); Transmembrane (1) TRANSMEM 53 73 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 52 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 74 218 Extracellular. {ECO:0000255}. FUNCTION: Lectin-type cell surface receptor. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Detected in ileum, liver, kidney and in IL2-activated natural killer cells. {ECO:0000269|PubMed:11398965}. +P0C7M9 CLC2L_MOUSE C-type lectin domain family 2 member L 211 23,653 Chain (1); Compositional bias (1); Disulfide bond (2); Domain (1); Modified residue (1); Transmembrane (1) TRANSMEM 66 86 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +P48985 ATOH1_MOUSE Protein atonal homolog 1 (Helix-loop-helix protein mATH-1) (mATH1) 351 37,854 Chain (1); Compositional bias (1); Domain (1) FUNCTION: Transcriptional regulator. Activates E box-dependent transcription in collaboration with TCF3/E47, but the activity is completely antagonized by the negative regulator of neurogenesis HES1. Plays a role in the differentiation of subsets of neural cells by activating E box-dependent transcription. {ECO:0000269|PubMed:10648228}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:10648228}. SUBUNIT: Efficient DNA binding requires dimerization with another bHLH protein. TISSUE SPECIFICITY: Developing nervous system, and in adult epithelial cells of the gastrointestinal tract. +Q9WUB6 CLCKB_MOUSE Chloride channel protein ClC-Kb (Chloride channel Kb) (ClC-K2) 687 75,009 Alternative sequence (2); Binding site (2); Chain (1); Domain (2); Intramembrane (4); Metal binding (4); Sequence conflict (13); Topological domain (2); Transmembrane (10) INTRAMEM 116 127 Helical. {ECO:0000250|UniProtKB:P35523}.; INTRAMEM 203 224 Helical. {ECO:0000250|UniProtKB:P35523}.; INTRAMEM 349 360 Helical. {ECO:0000250|UniProtKB:P35523}.; INTRAMEM 464 496 Helical. {ECO:0000250|UniProtKB:P35523}. TRANSMEM 51 82 Helical. {ECO:0000250|UniProtKB:P35523}.; TRANSMEM 91 111 Helical. {ECO:0000250|UniProtKB:P35523}.; TRANSMEM 141 160 Helical. {ECO:0000250|UniProtKB:P35523}.; TRANSMEM 161 180 Helical. {ECO:0000250|UniProtKB:P35523}.; TRANSMEM 236 255 Helical. {ECO:0000250|UniProtKB:P35523}.; TRANSMEM 282 310 Helical. {ECO:0000250|UniProtKB:P35523}.; TRANSMEM 325 342 Helical. {ECO:0000250|UniProtKB:P35523}.; TRANSMEM 400 420 Helical. {ECO:0000250|UniProtKB:P35523}.; TRANSMEM 421 440 Helical. {ECO:0000250|UniProtKB:P35523}.; TRANSMEM 500 520 Helical. {ECO:0000250|UniProtKB:P35523}. TOPO_DOM 1 50 Cytoplasmic. {ECO:0000250|UniProtKB:P35523}.; TOPO_DOM 521 687 Cytoplasmic. {ECO:0000250|UniProtKB:P35523}. FUNCTION: Voltage-gated chloride channel. Chloride channels have several functions including the regulation of cell volume; membrane potential stabilization, signal transduction and transepithelial transport. May be important in urinary concentrating mechanisms. May be the basolateral chloride channel mediating net chloride absorption in CTAL cells. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11734858}; Multi-pass membrane protein {ECO:0000269|PubMed:11734858}. SUBUNIT: Interacts with BSND. Forms heteromers with BSND in the thick ascending limb of Henle and more distal segments. {ECO:0000269|PubMed:11734858}. TISSUE SPECIFICITY: Specifically expressed in the kidney. All nephron segments expressing BSND also express CLCNK proreins. {ECO:0000269|PubMed:11014860, ECO:0000269|PubMed:11734858}. +Q9CPQ8 ATP5L_MOUSE ATP synthase subunit g, mitochondrial (ATPase subunit g) (ATP synthase membrane subunit g) 103 11,425 Chain (1); Initiator methionine (1); Modified residue (5); Sequence conflict (1) FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane. SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane. SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(0) seems to have nine subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L). Component of an ATP synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MD and MP68 (By similarity). {ECO:0000250}. +Q9WVD4 CLCN5_MOUSE H(+)/Cl(-) exchange transporter 5 (Chloride channel protein 5) (ClC-5) (Chloride transporter ClC-5) 746 83,101 Binding site (4); Chain (1); Domain (2); Intramembrane (7); Motif (3); Nucleotide binding (2); Site (2); Topological domain (2); Transmembrane (10) INTRAMEM 170 177 Helical. {ECO:0000250}.; INTRAMEM 242 254 Helical. {ECO:0000250}.; INTRAMEM 258 266 Helical. {ECO:0000250}.; INTRAMEM 500 514 Helical. {ECO:0000250}.; INTRAMEM 515 517 Note=Loop between two helices. {ECO:0000250}.; INTRAMEM 518 529 Helical. {ECO:0000250}.; INTRAMEM 530 534 Note=Loop between two helices. {ECO:0000250}. TRANSMEM 55 92 Helical. {ECO:0000250}.; TRANSMEM 138 161 Helical. {ECO:0000250}.; TRANSMEM 186 205 Helical. {ECO:0000250}.; TRANSMEM 211 230 Helical. {ECO:0000250}.; TRANSMEM 278 296 Helical. {ECO:0000250}.; TRANSMEM 319 344 Helical. {ECO:0000250}.; TRANSMEM 352 372 Helical. {ECO:0000250}.; TRANSMEM 428 448 Helical. {ECO:0000250}.; TRANSMEM 453 472 Helical. {ECO:0000250}.; TRANSMEM 535 552 Helical. {ECO:0000250}. TOPO_DOM 1 54 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 553 746 Cytoplasmic. {ECO:0000250}. FUNCTION: Proton-coupled chloride transporter. Functions as antiport system and exchanges chloride ions against protons. Important for normal acidification of the endosome lumen. May play an important role in renal tubular function (By similarity). {ECO:0000250}. PTM: Ubiquitinated by NEDD4L in the presence of albumin; which promotes endocytosis and proteasomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with NEDD4 and NEDD4L. {ECO:0000250}. TISSUE SPECIFICITY: Kidney specific. +O35454 CLCN6_MOUSE Chloride transport protein 6 (Chloride channel protein 6) (ClC-6) 870 96,980 Binding site (3); Chain (1); Domain (2); Glycosylation (3); Intramembrane (7); Modified residue (1); Motif (3); Nucleotide binding (2); Site (2); Topological domain (2); Transmembrane (10) INTRAMEM 159 166 Helical. {ECO:0000250}.; INTRAMEM 241 253 Helical. {ECO:0000250}.; INTRAMEM 257 265 Helical. {ECO:0000250}.; INTRAMEM 520 534 Helical. {ECO:0000250}.; INTRAMEM 535 537 Note=Loop between two helices. {ECO:0000250}.; INTRAMEM 538 549 Helical. {ECO:0000250}.; INTRAMEM 550 553 Note=Loop between two helices. {ECO:0000250}. TRANSMEM 81 113 Helical. {ECO:0000250}.; TRANSMEM 128 150 Helical. {ECO:0000250}.; TRANSMEM 176 194 Helical. {ECO:0000250}.; TRANSMEM 200 217 Helical. {ECO:0000250}.; TRANSMEM 277 294 Helical. {ECO:0000250}.; TRANSMEM 335 364 Helical. {ECO:0000250}.; TRANSMEM 371 392 Helical. {ECO:0000250}.; TRANSMEM 463 482 Helical. {ECO:0000250}.; TRANSMEM 488 512 Helical. {ECO:0000250}.; TRANSMEM 554 572 Helical. {ECO:0000250}. TOPO_DOM 1 80 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 573 870 Cytoplasmic. {ECO:0000250}. FUNCTION: Chloride transport protein, initially identified as voltage-gated chloride channel. The presence of the conserved gating glutamate residues suggests that is functions as antiporter. {ECO:0000269|PubMed:16950870}. PTM: N-glycosylated on several asparagine residues. {ECO:0000250}. SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:16950870}; Multi-pass membrane protein {ECO:0000269|PubMed:16950870}. TISSUE SPECIFICITY: Detected in whole brain and in hippocampus neurons (at protein level). Detected in brain, trigeminus, dorsal root ganglion, spinal cord, eye, kidney, testis, skeletal muscle, thymus and pancreas. Isoform ClC-6c is expressed only in kidney. {ECO:0000269|PubMed:16950870, ECO:0000269|PubMed:9224655}. +Q9Z0S6 CLD10_MOUSE Claudin-10 231 24,695 Alternative sequence (3); Chain (1); Sequence conflict (8); Topological domain (4); Transmembrane (4) TRANSMEM 1 21 Helical. {ECO:0000255}.; TRANSMEM 81 101 Helical. {ECO:0000255}.; TRANSMEM 116 136 Helical. {ECO:0000255}.; TRANSMEM 161 181 Helical. {ECO:0000255}. TOPO_DOM 22 80 Extracellular. {ECO:0000255}.; TOPO_DOM 102 115 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 137 160 Extracellular. {ECO:0000255}.; TOPO_DOM 182 231 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. Involved in the regulation of paracellular epithelia permeability to ions in multiple organs. It acts as a paracellular ion channel probably forming permselective pores; isoform 1 appears to create pores preferentially permeable to cations and isoform 2 for anions. In sweat glands and in the thick ascending limb (TAL) of Henle's loop in kidney, it controls paracellular sodium permeability which is essential for proper sweat production and renal function. {ECO:0000250|UniProtKB:P78369, ECO:0000269|PubMed:16804102, ECO:0000269|PubMed:19383724, ECO:0000269|PubMed:22891322}. SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000269|PubMed:16804102, ECO:0000269|PubMed:19383724}. Cell membrane {ECO:0000269|PubMed:19383724}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum {ECO:0000269|PubMed:19383724}. Note=Isoform 1, isoform 2 and isoform 4 localize in the cell membrane and at epithelial tight junctions, whereas isoform 3, isoform 5 and isoform 6 are detected in the endoplasmic reticulum. {ECO:0000269|PubMed:19383724}. SUBUNIT: Can form homodimers both in trans (interaction between CLDN10 molecules in opposing membranes) and in cis (interaction between CLDN10 molecules within one membrane). {ECO:0000250|UniProtKB:P78369}. DOMAIN: The fourth transmembrane region (161-181), which is missing in isoform 3, isoform 5 and isoform 6, is necessary for integration into tight junctions. {ECO:0000269|PubMed:19383724}. TISSUE SPECIFICITY: Strong expression detected in brain cortex and kidney and weak expression in lung and cecum. In kidney, detected in thick ascending limb (TAL) of Henle's loop and proximal convoluted tubule (PCT). Isoform 1 is widely expressed, with highest expression detected in brain cortex, kidney and lung. Isoform 2, isoform 3, isoform 4 and isoform 5 are only detected in kidney and uterus. In kidney, the expression of isoform 1 is highest in medulla, with transcripts being detected in medullary thick ascending limb of Henle's loop (mTAL) and outer and inner medullary collecting ducts, whereas isoform 2 (along with isoform 4) is more highly expressed in cortex, with transcripts being detected in PCT, mTAL and cortical collecting duct. Expressed in the inner ear where it is detected in organ of Corti, marginal cells of stria vascularis, Reissner's membrane and spiral limbus (at protein level) (PubMed:14698084). Expressed in salivary glands and skin (PubMed:28771254). {ECO:0000269|PubMed:14698084, ECO:0000269|PubMed:16804102, ECO:0000269|PubMed:19383724, ECO:0000269|PubMed:22891322, ECO:0000269|PubMed:28771254}. +Q9ET43 CLD12_MOUSE Claudin-12 244 26,995 Chain (1); Modified residue (2); Topological domain (5); Transmembrane (4) TRANSMEM 11 31 Helical. {ECO:0000255}.; TRANSMEM 88 108 Helical. {ECO:0000255}.; TRANSMEM 136 156 Helical. {ECO:0000255}.; TRANSMEM 175 195 Helical. {ECO:0000255}. TOPO_DOM 1 10 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 32 87 Extracellular. {ECO:0000255}.; TOPO_DOM 109 135 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 157 174 Extracellular. {ECO:0000255}.; TOPO_DOM 196 244 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000250}. Cell membrane {ECO:0000250|UniProtKB:P56749}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Interacts with OCLN. {ECO:0000250|UniProtKB:P56749}. +Q9Z0S4 CLD13_MOUSE Claudin-13 211 23,504 Chain (1); Topological domain (5); Transmembrane (4) TRANSMEM 9 29 Helical. {ECO:0000255}.; TRANSMEM 81 101 Helical. {ECO:0000255}.; TRANSMEM 119 139 Helical. {ECO:0000255}.; TRANSMEM 166 186 Helical. {ECO:0000255}. TOPO_DOM 1 8 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 30 80 Extracellular. {ECO:0000255}.; TOPO_DOM 102 118 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 140 165 Extracellular. {ECO:0000255}.; TOPO_DOM 187 211 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, tight junction. Cell membrane; Multi-pass membrane protein. +Q9Z0S3 CLD14_MOUSE Claudin-14 239 25,614 Chain (1); Sequence conflict (5); Topological domain (5); Transmembrane (4) TRANSMEM 8 28 Helical. {ECO:0000255}.; TRANSMEM 82 102 Helical. {ECO:0000255}.; TRANSMEM 116 136 Helical. {ECO:0000255}.; TRANSMEM 163 183 Helical. {ECO:0000255}. TOPO_DOM 1 7 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 29 81 Extracellular. {ECO:0000255}.; TOPO_DOM 103 115 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 137 162 Extracellular. {ECO:0000255}.; TOPO_DOM 184 239 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, tight junction. Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed in all sensory epithelia of the inner ear vestibular organs, as well as in liver and kidney. {ECO:0000269|PubMed:11163249}. +O88551 CLD1_MOUSE Claudin-1 211 22,881 Chain (1); Disulfide bond (1); Region (1); Topological domain (5); Transmembrane (4) TRANSMEM 8 28 Helical. {ECO:0000255}.; TRANSMEM 82 102 Helical. {ECO:0000255}.; TRANSMEM 116 136 Helical. {ECO:0000255}.; TRANSMEM 164 184 Helical. {ECO:0000255}. TOPO_DOM 1 7 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 29 81 Extracellular. {ECO:0000255}.; TOPO_DOM 103 115 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 137 163 Extracellular. {ECO:0000255}.; TOPO_DOM 185 211 Cytoplasmic. {ECO:0000250}. FUNCTION: Claudins function as major constituents of the tight junction complexes that regulate the permeability of epithelia. While some claudin family members play essential roles in the formation of impermeable barriers, others mediate the permeability to ions and small molecules. Often, several claudin family members are coexpressed and interact with each other, and this determines the overall permeability. CLDN1 is required to prevent the paracellular diffusion of small molecules through tight junctions in the epidermis and is required for the normal barrier function of the skin. Required for normal water homeostasis and to prevent excessive water loss through the skin, probably via an indirect effect on the expression levels of other proteins, since CLDN1 itself seems to be dispensable for water barrier formation in keratinocyte tight junctions. {ECO:0000269|PubMed:10508613, ECO:0000269|PubMed:11889141, ECO:0000269|PubMed:23407391}. SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000269|PubMed:10508613, ECO:0000269|PubMed:10562289, ECO:0000269|PubMed:9647647}. Cell membrane {ECO:0000269|PubMed:11889141}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:O95832}. Note=Associates with CD81 and the CLDN1-CD81 complex localizes to the basolateral cell membrane. {ECO:0000250|UniProtKB:O95832}. SUBUNIT: Can form homo- and heteropolymers with other CLDN. Homopolymers interact with CLDN3, but not CLDN2, homopolymers. Directly interacts with TJP1/ZO-1, TJP2/ZO-2 and TJP3/ZO-3. Interacts with MPDZ and PATJ. Interacts with OCLN, CD81, CLDN4, CLDN6 and CLDN9 (By similarity). {ECO:0000250|UniProtKB:O95832, ECO:0000269|PubMed:10508613, ECO:0000269|PubMed:10562289, ECO:0000269|PubMed:10601346, ECO:0000269|PubMed:11489913, ECO:0000269|PubMed:12021270}. TISSUE SPECIFICITY: Detected in epidermis and liver (at protein level). Widely expressed, with highest levels in liver and kidney. {ECO:0000269|PubMed:11889141, ECO:0000269|PubMed:9647647}. +Q9Z262 CLD6_MOUSE Claudin-6 (Skullin) 219 23,388 Chain (1); Modified residue (4); Region (1); Sequence conflict (1); Topological domain (5); Transmembrane (4) TRANSMEM 8 28 Helical. {ECO:0000255}.; TRANSMEM 82 102 Helical. {ECO:0000255}.; TRANSMEM 117 137 Helical. {ECO:0000255}.; TRANSMEM 164 184 Helical. {ECO:0000255}. TOPO_DOM 1 7 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 29 81 Extracellular. {ECO:0000255}.; TOPO_DOM 103 116 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 138 163 Extracellular. {ECO:0000255}.; TOPO_DOM 185 219 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000269|PubMed:9892664}. Cell membrane {ECO:0000269|PubMed:9892664}; Multi-pass membrane protein {ECO:0000269|PubMed:9892664}. SUBUNIT: Directly interacts with TJP1/ZO-1, TJP2/ZO-2 and TJP3/ZO-3 (PubMed:10601346). Interacts with CLDN1, CD81 and OCLN (By similarity). {ECO:0000250|UniProtKB:P56747, ECO:0000269|PubMed:10601346}. TISSUE SPECIFICITY: Expressed mostly in embryonic tissues. {ECO:0000269|PubMed:9892664}. +Q9Z261 CLD7_MOUSE Claudin-7 211 22,359 Chain (1); Region (1); Topological domain (5); Transmembrane (4) TRANSMEM 8 28 Helical. {ECO:0000255}.; TRANSMEM 82 102 Helical. {ECO:0000255}.; TRANSMEM 120 140 Helical. {ECO:0000255}.; TRANSMEM 161 181 Helical. {ECO:0000255}. TOPO_DOM 1 7 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 29 81 Extracellular. {ECO:0000255}.; TOPO_DOM 103 119 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 141 160 Extracellular. {ECO:0000255}.; TOPO_DOM 182 211 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. {ECO:0000250}. PTM: Phosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O95471}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:O95471}. Cell junction, tight junction {ECO:0000250|UniProtKB:O95471}. Note=Colocalizes with EPCAM at the basolateral cell membrane and tight junction. {ECO:0000250|UniProtKB:O95471}. SUBUNIT: Directly interacts with TJP1/ZO-1, TJP2/ZO-2 and TJP3/ZO-3 (PubMed:10601346). The phosphorylated form interacts with EPCAM (By similarity). {ECO:0000250|UniProtKB:O95471, ECO:0000269|PubMed:10601346}. TISSUE SPECIFICITY: Expressed predominantly in lung and kidney. {ECO:0000269|PubMed:9892664}. +Q9Z260 CLD8_MOUSE Claudin-8 225 24,947 Chain (1); Cross-link (1); Mutagenesis (1); Region (1); Topological domain (5); Transmembrane (4) TRANSMEM 8 28 Helical. {ECO:0000255}.; TRANSMEM 82 102 Helical. {ECO:0000255}.; TRANSMEM 118 138 Helical. {ECO:0000255}.; TRANSMEM 167 187 Helical. {ECO:0000255}. TOPO_DOM 1 7 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 29 81 Extracellular. {ECO:0000255}.; TOPO_DOM 103 117 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 139 166 Extracellular. {ECO:0000255}.; TOPO_DOM 188 225 Cytoplasmic. {ECO:0000255}. FUNCTION: Tight-junction protein required for paracellular chloride transport in the kidney (PubMed:20921420, PubMed:25831548). Mediates recruitment of CLDN4 to tight junction in the kidney (PubMed:20921420, PubMed:25831548). Claudins play a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. {ECO:0000269|PubMed:20921420, ECO:0000269|PubMed:25831548}. PTM: Ubiquitinated by the BCR(KLHL3) E3 ubiquitin ligase complex in the kidney, leading to its degradation. {ECO:0000269|PubMed:25831548}. SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000269|PubMed:20921420, ECO:0000269|PubMed:25831548, ECO:0000269|PubMed:9892664}. Cell membrane {ECO:0000269|PubMed:20921420, ECO:0000269|PubMed:9892664}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Directly interacts with TJP1/ZO-1, TJP2/ZO-2 and TJP3/ZO-3 (PubMed:10601346). Interacts with CLDN4 (PubMed:20921420). Interacts with KLHL3 (PubMed:25831548). {ECO:0000269|PubMed:10601346, ECO:0000269|PubMed:20921420, ECO:0000269|PubMed:25831548}. TISSUE SPECIFICITY: Expressed primarily in lung and kidney (PubMed:9892664). Present in both cortical and medullar collecting ducts (at protein level) (PubMed:20921420). {ECO:0000269|PubMed:20921420, ECO:0000269|PubMed:9892664}. +Q9D9H2 CLDN2_MOUSE Claudin domain-containing protein 2 167 18,250 Chain (1); Transmembrane (4) TRANSMEM 13 32 Helical. {ECO:0000255}.; TRANSMEM 61 81 Helical. {ECO:0000255}.; TRANSMEM 96 116 Helical. {ECO:0000255}.; TRANSMEM 130 150 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +Q68FD5 CLH1_MOUSE Clathrin heavy chain 1 1675 191,557 Beta strand (28); Chain (1); Helix (19); Initiator methionine (1); Modified residue (18); Region (15); Repeat (7); Turn (7) FUNCTION: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. Two different adapter protein complexes link the clathrin lattice either to the plasma membrane or to the trans-Golgi network. Acts as component of the TACC3/ch-TOG/clathrin complex proposed to contribute to stabilization of kinetochore fibers of the mitotic spindle by acting as inter-microtubule bridge. The TACC3/ch-TOG/clathrin complex is required for the maintenance of kinetochore fiber tension. Plays a role in early autophagosome formation. {ECO:0000250|UniProtKB:P11442, ECO:0000250|UniProtKB:Q00610}. SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Membrane, coated pit {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Melanosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q00610}. Note=Cytoplasmic face of coated pits and vesicles. In complex with TACC3 and CKAP5 (forming the TACC3/ch-TOG/clathrin complex) localized to inter-microtubule bridges in mitotic spindles. {ECO:0000250, ECO:0000250|UniProtKB:Q00610}. SUBUNIT: Clathrin triskelions, composed of 3 heavy chains and 3 light chains, are the basic subunits of the clathrin coat (By similarity). In the presence of light chains, hub assembly is influenced by both the pH and the concentration of calcium (By similarity). Interacts with HIP1 (By similarity). Interacts with DENND1A, DENND1B and DENND1C (By similarity). Interacts with ERBB2 (By similarity). Interacts with FKBP6 (By similarity). Interacts with OCRL (PubMed:20133602). Interacts with CKAP5 and TACC3 forming the TACC3/ch-TOG/clathrin complex located at spindle inter-microtubules bridges; the complex implicates clathrin triskelions; TACC3 and CLTC are proposed to form a composite microtubule interaction surface (By similarity). Plays a role in early autopahgosome formation (By similarity). Interacts with ATG16L1 (via N-terminus) (By similarity). Interacts with RFTN1; the interaction occurs in response to pathogens (By similarity). Interacts with USP2 isoform 2 (PubMed:26756164). {ECO:0000250|UniProtKB:P49951, ECO:0000250|UniProtKB:Q00610, ECO:0000269|PubMed:20133602, ECO:0000269|PubMed:26756164}. DOMAIN: The N-terminal seven-bladed beta-propeller is formed by WD40-like repeats, and projects inward from the polyhedral outer clathrin coat. It constitutes a major protein-protein interaction node (By similarity). {ECO:0000250}. +Q9Z1Q5 CLIC1_MOUSE Chloride intracellular channel protein 1 (Nuclear chloride ion channel 27) (NCC27) 241 27,013 Chain (1); Disulfide bond (1); Domain (1); Initiator methionine (1); Modified residue (8); Region (1); Transmembrane (1) TRANSMEM 26 46 Helical; Note=After insertion into the membrane. {ECO:0000255}. FUNCTION: Can insert into membranes and form chloride ion channels. Channel activity depends on the pH. Membrane insertion seems to be redox-regulated and may occur only under oxydizing conditions (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=Mostly in the nucleus including in the nuclear membrane. Small amount in the cytoplasm and the plasma membrane. Exists both as soluble cytoplasmic protein and as membrane protein with probably a single transmembrane domain (By similarity). {ECO:0000250}. SUBUNIT: Monomer. Homodimer (in vitro). Interacts with TRAPPC2. Dimerization requires a conformation change that leads to the exposure of a large hydrophobic surface. In vivo, this may lead to membrane insertion. Interacts with AKAP9 (By similarity). {ECO:0000250}. DOMAIN: Members of this family may change from a globular, soluble state to a state where the N-terminal domain is inserted into the membrane and functions as chloride channel. A conformation change of the N-terminal domain is thought to expose hydrophobic surfaces that trigger membrane insertion (By similarity). {ECO:0000250}. +Q9D7P7 CLIC3_MOUSE Chloride intracellular channel protein 3 237 26,846 Chain (1); Disulfide bond (1); Domain (2); Modified residue (1); Region (1); Transmembrane (1) TRANSMEM 25 45 Helical. {ECO:0000255}. FUNCTION: Can insert into membranes and form chloride ion channels. May participate in cellular growth control (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Predominantly nuclear. Some protein was found in the cytoplasm. Exists both as soluble cytoplasmic protein and as membrane protein with probably a single transmembrane domain (By similarity). {ECO:0000250}. SUBUNIT: Associated with the C-terminal of MAPK15. {ECO:0000250|UniProtKB:O95833}. DOMAIN: Members of this family may change from a globular, soluble state to a state where the N-terminal domain is inserted into the membrane and functions as chloride channel. A conformation change of the N-terminal domain is thought to expose hydrophobic surfaces that trigger membrane insertion (By similarity). {ECO:0000250}. +Q8BXK9 CLIC5_MOUSE Chloride intracellular channel protein 5 251 28,287 Chain (1); Domain (1); Region (1); Transmembrane (1) TRANSMEM 34 54 Helical; Note=After insertion into the membrane. {ECO:0000255}. FUNCTION: Required for normal hearing (By similarity). It is necessary for the formation of stereocilia in the inner ear and normal development of the organ of Corti. Can insert into membranes and form poorly selective ion channels that may also transport chloride ions. May play a role in the regulation of transepithelial ion absorption and secretion. Is required for the development and/or maintenance of the proper glomerular endothelial cell and podocyte architecture (PubMed:17021174). {ECO:0000250|UniProtKB:Q9NZA1, ECO:0000269|PubMed:17021174}. SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Colocalized with AKAP9 at the Golgi apparatus as well as, to a lesser extent, the centrosome. Exists both as soluble cytoplasmic protein and as membrane protein with probably a single transmembrane domain (By similarity). {ECO:0000250}. SUBUNIT: Component of a multimeric complex consisting of several cytoskeletal proteins, including actin, ezrin, alpha-actinin, gelsolin, and IQGAP1. Interacts with AKAP9 (By similarity). {ECO:0000250}. DOMAIN: Members of this family may change from a globular, soluble state to a state where the N-terminal domain is inserted into the membrane and functions as chloride channel. A conformation change of the N-terminal domain is thought to expose hydrophobic surfaces that trigger membrane insertion (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Detected in lung and inner ear. Detected in embryonic cochlea, on microvilli-covered apical surfaces of interdental cells, columnar cells of Kolliker's organ, and on stereocilia of inner and outer hair cells (at protein level). {ECO:0000269|PubMed:17021174}. DISEASE: Note=Defects in Clic5 are a cause of the jitterbug (jbg) phenotype. Jbg is the result of a spontaneous mutation that leads to severe degeneration of the organ of Corti in the inner ear. Jbg leads to progressive degeneration of inner ear hair cells. Affected mice are identified by head bobbing, circling behavior and their inability to swim. They cannot hear well when young, and become completely deaf after 5 months. {ECO:0000269|PubMed:17021174}. +Q8BHB9 CLIC6_MOUSE Chloride intracellular channel protein 6 596 62,886 Beta strand (6); Chain (1); Compositional bias (1); Domain (1); Helix (11); Modified residue (2); Transmembrane (1); Turn (2) TRANSMEM 381 401 Helical; Note=After insertion into the membrane. {ECO:0000255}. FUNCTION: May insert into membranes and form chloride ion channels. May play a critical role in water-secreting cells, possibly through the regulation of chloride ion transport (By similarity). {ECO:0000250}. PTM: Phosphorylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=Predominantly cytoplasmic. Upon chloride ion efflux from the cell, it is translocated to the plasma membrane (By similarity). {ECO:0000250}. SUBUNIT: Interacts with dopamine receptors DRD2, DRD3 and DRD4. {ECO:0000250}. DOMAIN: Members of this family may change from a globular, soluble state to a state where the N-terminal domain is inserted into the membrane and functions as chloride channel. A conformation change of the N-terminal domain is thought to expose hydrophobic surfaces that trigger membrane insertion (By similarity). {ECO:0000250}. +B9EHT4 CLIP3_MOUSE CAP-Gly domain-containing linker protein 3 (Cytoplasmic linker protein 170-related 59 kDa protein) (CLIP-170-related 59 kDa protein) (CLIPR-59) 547 59,587 Beta strand (8); Chain (1); Compositional bias (1); Domain (2); Erroneous initiation (1); Helix (1); Lipidation (2); Modified residue (3); Region (1); Repeat (3); Turn (2) FUNCTION: Functions as a cytoplasmic linker protein. Involved in TGN-endosome dynamics. May modulate the cellular compartmentalization of AKT kinase family and promote its cell membrane localization, thereby playing a role in glucose transport in adipocytes (By similarity). {ECO:0000250}. PTM: Palmitoylation by ZDHHC17 regulates association with the plasma membrane. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Cytoplasm {ECO:0000250}. Golgi apparatus, Golgi stack {ECO:0000250}. Note=Localized to Golgi stacks as well as on tubulovesicular elements juxtaposed to Golgi cisternae. {ECO:0000250}. SUBUNIT: Homodimer. Interacts with AKT1 and AKT2; when AKT1 and AKT2 are phosphorylated and activated, affinity is higher for AKT2 (By similarity). Interacts with ZDHHC13 (via ANK repeats) (PubMed:26198635). Interacts with ZDHHC17 (via ANK repeats) (PubMed:26198635). {ECO:0000250|UniProtKB:Q96DZ5, ECO:0000269|PubMed:26198635}. DOMAIN: Microtubule association is inhibited by the ANK repeats and the Golgi localization region (GoLD). {ECO:0000250}. +Q6SJQ7 CLM1_MOUSE CMRF35-like molecule 1 (CLM-1) (CD300 antigen-like family member F) (Leukocyte mono-Ig-like receptor 3) (Myeloid-associated immunoglobulin-like receptor 5) (MAIR-5) (MAIR-V) (CD antigen CD300f) 337 36,715 Alternative sequence (2); Beta strand (12); Chain (1); Disulfide bond (2); Domain (1); Helix (3); Region (1); Sequence conflict (8); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 194 214 Helical. {ECO:0000255}. TOPO_DOM 20 193 Extracellular. {ECO:0000255}.; TOPO_DOM 215 337 Cytoplasmic. {ECO:0000255}. FUNCTION: Acts as an inhibitory receptor for myeloid cells and mast cells (PubMed:17438331). Positively regulates the phagocytosis of apoptotic cells (efferocytosis) via phosphatidylserine (PS) recognition; recognizes and binds PS as a ligand which is expressed on the surface of apoptotic cells (PubMed:21865548). Plays an important role in the maintenance of immune homeostasis, by promoting macrophage-mediated efferocytosis and by inhibiting dendritic cell-mediated efferocytosis (PubMed:26768664). Negatively regulates Fc epsilon receptor-dependent mast cell activation and allergic responses via binding to ceramide which acts as a ligand (PubMed:23123064). May act as a coreceptor for interleukin 4 (IL-4). Associates with and regulates IL-4 receptor alpha-mediated responses by augmenting IL-4- and IL-13-induced signaling (PubMed:26124135). Negatively regulates the Toll-like receptor (TLR) signaling mediated by MYD88 and TRIF through activation of PTPN6/SHP-1 and PTPN11/SHP-2 (By similarity). Inhibits osteoclast formation (PubMed:14662855). Induces macrophage cell death upon engagement (PubMed:18097021). {ECO:0000250|UniProtKB:Q8TDQ1, ECO:0000269|PubMed:14662855, ECO:0000269|PubMed:17438331, ECO:0000269|PubMed:18097021, ECO:0000269|PubMed:21865548, ECO:0000269|PubMed:23123064, ECO:0000269|PubMed:26124135, ECO:0000269|PubMed:26768664}.; FUNCTION: (Microbial infection) Acts as a functional murine norovirus (MNV) receptor that mediates binding to the cell surface and is both necessary and sufficient for viral entry and replication. Primary determinant of MNV species tropism and is sufficient to render cells permissive to infection by MNV. Can render nonmurine mammalian cells susceptible to MNV infection (PubMed:27681626, PubMed:27540007). {ECO:0000269|PubMed:27540007, ECO:0000269|PubMed:27681626}. PTM: Phosphorylated on tyrosine. {ECO:0000269|PubMed:23123064}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Interacts with PTPN6/SHP-1 in a tyrosine phosphorylation dependent manner (PubMed:14662855). Interacts with IL4R (PubMed:26124135). {ECO:0000269|PubMed:14662855, ECO:0000269|PubMed:26124135}. TISSUE SPECIFICITY: Expressed in myeloid cells. Present on the surface of macrophages (at protein level). Highly expressed by alveolar, splenic macrophages and bone marrow-derived dendritic cells. Expression is increased following aeroallergen challenge in macrophages, mast cells, and eosinophils. {ECO:0000269|PubMed:14662855, ECO:0000269|PubMed:18097021, ECO:0000269|PubMed:26124135, ECO:0000269|PubMed:26768664}. +Q6SJQ5 CLM3_MOUSE CMRF35-like molecule 3 (CLM-3) (CD300 antigen-like family member H) (CD300 molecule-like family member D3) 245 27,312 Chain (1); Compositional bias (1); Disulfide bond (1); Domain (1); Mutagenesis (2); Region (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 190 210 Helical. {ECO:0000255}. TOPO_DOM 19 189 Extracellular. {ECO:0000255}.; TOPO_DOM 211 245 Cytoplasmic. {ECO:0000255}. FUNCTION: Acts as an activating receptor inducing cytokine production in mast cells. Can act as a positive regulator of TLR9 signaling in macrophages, leading to enhanced production of proinflammatory cytokines. {ECO:0000269|PubMed:20817736, ECO:0000269|PubMed:21940676}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Early endosome {ECO:0000269|PubMed:21940676}. Lysosome {ECO:0000269|PubMed:21940676}. SUBUNIT: Interacts with FCER1G; the interaction may be indirect. Interacts with TLR9. {ECO:0000269|PubMed:20817736, ECO:0000269|PubMed:21940676}. TISSUE SPECIFICITY: Highly expressed in bone marrow-derived mast cells and macrophages, peripheral blood monocytes and CD11c+ cells, with weaker expression detected in CD11b cells in bone marrow and peripheral blood. Not detected in B220+ cells in bone marrow or spleen, in Thy-1.2+ or CD3+ cells in peripheral blood, spleen or thymus, or in NK1.1+ cells in spleen (at protein level). Widely expressed in various tissues including heart, liver, spleen, lung, kidney, brain, bone marrow, thymus, axillary lymph node and mesenteric lymph node. Highly expressed in macrophage cell lines J774.1 and RAW 264.7 and in mast cell line MC/9. Weak expression detected in B-lineage cell lines WEHI-231 and A20 and in dendritic cell line DC2.4. Not detected in other myeloid cell lines or T-lineage cell lines. {ECO:0000269|PubMed:20817736, ECO:0000269|PubMed:21940676}. +Q3U497 CLM7_MOUSE CMRF35-like molecule 7 (CLM-7) (CD300 antigen-like family member B) (Immune receptor expressed on myeloid cells 3) (IREM-3) (Leukocyte mono-Ig-like receptor 5) (CD antigen CD300b) 209 23,755 Chain (1); Disulfide bond (1); Domain (1); Erroneous initiation (1); Frameshift (1); Glycosylation (1); Modified residue (1); Natural variant (1); Sequence conflict (3); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 158 178 Helical. {ECO:0000255}. TOPO_DOM 18 157 Extracellular. {ECO:0000255}.; TOPO_DOM 179 209 Cytoplasmic. {ECO:0000255}. FUNCTION: Acts as an activating immune receptor in mast cells through its interaction with ITAM-bearing adapter TYROBP. {ECO:0000269|PubMed:17928527}. PTM: N-glycosylated. {ECO:0000269|PubMed:17928527}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17928527}; Single-pass type I membrane protein {ECO:0000269|PubMed:17928527}. SUBUNIT: Interacts with TYROBP, which enhances cell surface expression and activation properties. May interact with HCST. {ECO:0000269|PubMed:17928527}. TISSUE SPECIFICITY: Expressed in myeloid cells (at protein level). {ECO:0000269|PubMed:17928527}. +Q1ERP8 CLM9_MOUSE CMRF35-like molecule 9 (CLM-9) (CD300 antigen-like family member G) (Nepmucin) (CD antigen CD300g) 331 36,756 Alternative sequence (5); Chain (1); Disulfide bond (1); Domain (1); Erroneous gene model prediction (1); Glycosylation (11); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 205 225 Helical. {ECO:0000255}. TOPO_DOM 19 204 Extracellular. {ECO:0000255}.; TOPO_DOM 226 331 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor which may mediate L-selectin-dependent lymphocyte rollings. Binds SELL in a calcium dependent manner. Binds lymphocyte. {ECO:0000269|PubMed:16754720, ECO:0000269|PubMed:16876123}. PTM: O-glycosylated with sialylated oligosaccharides. {ECO:0000269|PubMed:16754720}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:16754720, ECO:0000269|PubMed:16876123}; Single-pass type I membrane protein {ECO:0000305|PubMed:16754720}. Basolateral cell membrane {ECO:0000269|PubMed:16754720, ECO:0000269|PubMed:16876123}; Single-pass type I membrane protein {ECO:0000305|PubMed:16754720}. Endosome, multivesicular body membrane {ECO:0000269|PubMed:16876123}; Single-pass type I membrane protein {ECO:0000305|PubMed:16754720}. Note=Exclusively localized on capillary endothelium. Transcytoses across the cytoplasm in the capillary endothelium. {ECO:0000269|PubMed:16876123}. DOMAIN: Ig-like V-type domain mediates binding to lymphocyte. TISSUE SPECIFICITY: Expressed in monocyte cell lines. Expressed in certain types of endothelial and myeloid lineage cells. Expressed in mesenteric lymph nodes (LNs), spleen, thymus, lung, heart and kidney. Expressed in high endothelial venules (HEVs) in peripheral and mesenteric LNs (at protein level). Highly expressed in heart. Slightly expressed in spleen and thymus. Isoform 5 is expressed preferentially in heart. Isoform 1 is expressed predominantly in kidney and liver. {ECO:0000269|PubMed:14662855, ECO:0000269|PubMed:16754720, ECO:0000269|PubMed:16876123}. +Q8R373 CLMP_MOUSE CXADR-like membrane protein (Adipocyte adhesion molecule) (Adipocyte-specific protein 5) (Coxsackie- and adenovirus receptor-like membrane protein) (CAR-like membrane protein) 373 41,215 Chain (1); Compositional bias (1); Disulfide bond (2); Domain (2); Glycosylation (2); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 235 255 Helical. {ECO:0000255}. TOPO_DOM 18 234 Extracellular. {ECO:0000255}.; TOPO_DOM 256 373 Cytoplasmic. {ECO:0000255}. FUNCTION: May be involved in the cell-cell adhesion. May play a role in adipocyte differentiation and development of obesity. Is required for normal small intestine development (By similarity). {ECO:0000250, ECO:0000269|PubMed:14573622, ECO:0000269|PubMed:15563274}. SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000269|PubMed:14573622}. Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Predominantly expressed in epithelial cells within different tissues and in the white adipose tissue. Expressed at high levels in the heart and brain, at intermediate levels in the lung, skeletal muscle, kidney and testis and at low levels in the liver and spleen. {ECO:0000269|PubMed:14573622, ECO:0000269|PubMed:15563274}. +Q64430 ATP7A_MOUSE Copper-transporting ATPase 1 (EC 7.2.2.8) (Copper pump 1) (Menkes disease-associated protein homolog) 1491 161,959 Active site (1); Chain (1); Compositional bias (1); Domain (6); Glycosylation (2); Metal binding (2); Modified residue (17); Motif (1); Natural variant (2); Region (1); Sequence conflict (23); Topological domain (9); Transmembrane (8) TRANSMEM 645 666 Helical. {ECO:0000255}.; TRANSMEM 706 725 Helical. {ECO:0000255}.; TRANSMEM 733 753 Helical. {ECO:0000255}.; TRANSMEM 773 793 Helical. {ECO:0000255}.; TRANSMEM 927 950 Helical. {ECO:0000255}.; TRANSMEM 981 1002 Helical. {ECO:0000255}.; TRANSMEM 1348 1365 Helical. {ECO:0000255}.; TRANSMEM 1377 1396 Helical. {ECO:0000255}. TOPO_DOM 1 644 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 667 705 Extracellular. {ECO:0000255}.; TOPO_DOM 726 732 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 754 772 Extracellular. {ECO:0000255}.; TOPO_DOM 794 926 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 951 980 Extracellular. {ECO:0000255}.; TOPO_DOM 1003 1347 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1366 1376 Extracellular. {ECO:0000255}.; TOPO_DOM 1397 1491 Cytoplasmic. {ECO:0000255}. FUNCTION: May supply copper to copper-requiring proteins within the secretory pathway, when localized in the trans-Golgi network. Under conditions of elevated extracellular copper, it relocalized to the plasma membrane where it functions in the efflux of copper from cells (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q04656}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q04656}; Multi-pass membrane protein {ECO:0000255}. Note=Cycles constitutively between the trans-Golgi network (TGN) and the plasma membrane. Predominantly found in the TGN and relocalized to the plasma membrane in response to elevated copper levels. {ECO:0000250|UniProtKB:Q04656}. SUBUNIT: Monomer. Interacts with PDZD11 (By similarity). Interacts with ATOX1 and COMMD1 (By similarity). {ECO:0000250|UniProtKB:Q04656}. DOMAIN: The C-terminal di-leucine, 1478-Leu-Leu-1479, is an endocytic targeting signal which functions in retrieving recycling from the plasma membrane to the TGN. Mutation of the di-leucine signal results in the accumulation of the protein in the plasma membrane (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Found in most tissues except liver. In the kidney, it is detected in the proximal and distal tubules. DISEASE: Note=Defects in Atp7a are associated with mottled, an X-linked recessive condition characterized by mottled pigmentation of the coat, defects in connective tissue and neonatal or fetal death. It is due to a defect in absorption and transport of copper. The mottled mutants exhibit a diversity of phenotypes. Two of these mutants are called brindled and blotchy and their phenotypes resemble classical Menkes disease (MD) and occipital horn syndrome (OHS) in humans, respectively. Other mutants are called dappled, mosaic, tortoiseshell, pewter, etc. {ECO:0000269|PubMed:8054976, ECO:0000269|PubMed:8054977, ECO:0000269|PubMed:9215672, ECO:0000269|PubMed:9385451}. +Q64446 ATP7B_MOUSE Copper-transporting ATPase 2 (EC 7.2.2.8) (Copper pump 2) (Wilson disease-associated protein homolog) 1462 157,190 Active site (1); Chain (1); Domain (6); Metal binding (13); Modified residue (4); Natural variant (1); Sequence conflict (1); Topological domain (9); Transmembrane (8) TRANSMEM 656 677 Helical. {ECO:0000255}.; TRANSMEM 700 719 Helical. {ECO:0000255}.; TRANSMEM 727 747 Helical. {ECO:0000255}.; TRANSMEM 767 787 Helical. {ECO:0000255}.; TRANSMEM 922 944 Helical. {ECO:0000255}.; TRANSMEM 975 996 Helical. {ECO:0000255}.; TRANSMEM 1320 1337 Helical. {ECO:0000255}.; TRANSMEM 1349 1368 Helical. {ECO:0000255}. TOPO_DOM 1 655 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 678 699 Extracellular. {ECO:0000255}.; TOPO_DOM 720 726 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 748 766 Extracellular. {ECO:0000255}.; TOPO_DOM 788 921 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 945 974 Extracellular. {ECO:0000255}.; TOPO_DOM 997 1319 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1338 1348 Extracellular. {ECO:0000255}.; TOPO_DOM 1369 1462 Cytoplasmic. {ECO:0000255}. FUNCTION: Copper ion transmembrane transporter involved in the export of copper out of the cells, such as the efflux of hepatic copper into the bile. {ECO:0000250|UniProtKB:P35670}. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:P35670}; Multi-pass membrane protein {ECO:0000255}. Late endosome {ECO:0000250|UniProtKB:P35670}. Note=Predominantly found in the trans-Golgi network (TGN). Not redistributed to the plasma membrane in response to elevated copper levels. {ECO:0000250|UniProtKB:P35670}. SUBUNIT: Monomer. Interacts with COMMD1/MURR1 (By similarity). Interacts with DCTN4, in a copper-dependent manner (By similarity). Interacts with ATOX1 (By similarity). Interacts (via C-terminus) with ZBTB16/PLZF (By similarity). {ECO:0000250|UniProtKB:P35670}. DOMAIN: Each HMA domain can bind a copper ion, they are tightly packed and closely interact with each other. Wild-type ATP7B can usually be loaded with an average 5.5 copper atoms per molecule (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Detected in liver and kidney. DISEASE: Note=Defects in Atp7b are the cause of the toxic milk mouse mutant (tx) phenotype, characterized by accumulation of copper in the liver in a manner similar to that observed in patients with Wilson disease. {ECO:0000269|PubMed:8894697}. +Q6A051 ATRN1_MOUSE Attractin-like protein 1 1378 152,467 Alternative sequence (4); Chain (1); Disulfide bond (15); Domain (11); Erroneous initiation (1); Glycosylation (8); Region (1); Repeat (6); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 1230 1250 Helical. {ECO:0000255}. TOPO_DOM 52 1229 Extracellular. {ECO:0000255}.; TOPO_DOM 1251 1378 Cytoplasmic. {ECO:0000255}. FUNCTION: May play a role in melanocortin signaling pathways that regulate energy homeostasis. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. SUBUNIT: Interacts with MC4R. {ECO:0000269|PubMed:14531729}. TISSUE SPECIFICITY: Highly expressed in brain, heart, lung, kidney and liver. In the central nervous system, it is highly expressed in the dentate gyrus, CA1-3 regions of the hippocampus, and the ventral taenia tecta. {ECO:0000269|PubMed:18064672}. +Q8C9W3 ATS2_MOUSE A disintegrin and metalloproteinase with thrombospondin motifs 2 (ADAM-TS 2) (ADAM-TS2) (ADAMTS-2) (EC 3.4.24.14) (Procollagen I N-proteinase) (PC I-NP) (Procollagen I/II amino propeptide-processing enzyme) (Procollagen N-endopeptidase) (pNPI) 1213 135,299 Active site (1); Chain (1); Compositional bias (1); Disulfide bond (13); Domain (7); Glycosylation (9); Metal binding (3); Motif (1); Propeptide (1); Region (1); Signal peptide (1) FUNCTION: Cleaves the propeptides of type I and II collagen prior to fibril assembly. Does not act on type III collagen. May also play a role in development that is independent of its role in collagen biosynthesis (By similarity). {ECO:0000250}. PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}.; PTM: Glycosylated. Can be O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS family members. Also can be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated. These other glycosylations can also facilitate secretion (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. SUBUNIT: May belong to a multimeric complex. Binds specifically to collagen type XIV (By similarity). {ECO:0000250}. DOMAIN: The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix. +Q8BNJ2 ATS4_MOUSE A disintegrin and metalloproteinase with thrombospondin motifs 4 (ADAM-TS 4) (ADAM-TS4) (ADAMTS-4) (EC 3.4.24.82) (Aggrecanase-1) 833 90,070 Active site (1); Chain (1); Disulfide bond (11); Domain (3); Erroneous initiation (1); Glycosylation (2); Metal binding (4); Motif (1); Propeptide (1); Region (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Cleaves aggrecan, a cartilage proteoglycan, and may be involved in its turnover. May play an important role in the destruction of aggrecan in arthritic diseases. Cleaves aggrecan at the '392-Glu-|-Ala-393' site (By similarity). {ECO:0000250}. PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}.; PTM: Glycosylated. Can be O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS family members. Also can be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated. These other glycosylations can also facilitate secretion (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. SUBUNIT: Interacts with SRPX2. {ECO:0000250}. DOMAIN: The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix. {ECO:0000250}.; DOMAIN: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme. +Q61687 ATRX_MOUSE Transcriptional regulator ATRX (EC 3.6.4.12) (ATP-dependent helicase ATRX) (HP1 alpha-interacting protein) (HP1-BP38 protein) (Heterochromatin protein 2) (X-linked nuclear protein) 2476 278,587 Chain (1); Compositional bias (11); Cross-link (10); Domain (3); Modified residue (46); Motif (2); Mutagenesis (2); Nucleotide binding (1); Region (2); Sequence conflict (2); Zinc finger (2) FUNCTION: Involved in transcriptional regulation and chromatin remodeling. Facilitates DNA replication in multiple cellular environments and is required for efficient replication of a subset of genomic loci. Binds to DNA tandem repeat sequences in both telomeres and euchromatin and in vitro binds DNA quadruplex structures. May help stabilizing G-rich regions into regular chromatin structures by remodeling G4 DNA and incorporating H3.3-containing nucleosomes. Catalytic component of the chromatin remodeling complex ATRX:DAXX which has ATP-dependent DNA translocase activity and catalyzes the replication-independent deposition of histone H3.3 in pericentric DNA repeats outside S-phase and telomeres, and the in vitro remodeling of H3.3-containing nucleosomes. Its heterochromatin targeting is proposed to involve a combinatorial readout of histone H3 modifications (specifically methylation states of H3K9 and H3K4) and association with CBX5. Involved in maintaining telomere structural integrity in embryonic stem cells probably implying recruitment of CBX5 to telomers. Reports on the involvement in transcriptional regulation of telomeric repeat-containing RNA (TERRA) are conflicting; according (PubMed:20211137) is required for its transcriptional repression in embryonic stem cells. Acts as negative regulator of chromatin incorporation of transcriptionally repressive histone H2AFY, particularily at telomeres. Participates in the allele-specific gene expression at the imprinted IGF2/H19 gene locus. On the maternal allele, required for the chromatin occupancy of SMC1 and CTCTF within the H19 imprinting control region (ICR) and involved in esatblishment of histone tails modifications in the ICR. Binds to zinc-finger coding genes with atypical chromatin signatures and regulates its H3K9me3 levels. Forms a complex with ZNF274, TRIM28 and SETDB1 to facilitate the deposition and maintenance of H3K9me3 at the 3' exons of zinc-finger genes (By similarity). {ECO:0000250|UniProtKB:P46100, ECO:0000269|PubMed:20110566, ECO:0000269|PubMed:20211137, ECO:0000269|PubMed:21029860, ECO:0000269|PubMed:24651726}. PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}. SUBCELLULAR LOCATION: Nucleus. Chromosome, telomere. Nucleus, PML body {ECO:0000250}. Note=Associated with pericentromeric heterochromatin during interphase and mitosis, probably by interacting with CBX5/HP1 alpha. Colocalizes with histone H3.3, DAXX, HIRA and ASF1A at PML-nuclear bodies (By similarity). In embryonic stem cells localized to telomeres; localization is reduced after 12 d of induction of cell differentiation. Colocalizes with cohesin (SMC1 and SMC3) and MECP2 at the maternal H19 ICR and the Gtl2/Dlk1 imprinted cluster in the brain. {ECO:0000250}. SUBUNIT: Interacts with DAXX to form the chromatin remodeling complex ATRX:DAXX. Probably binds EZH2. Binds annexin V in a calcium and phosphatidylcholine/phosphatidylserine-dependent manner. Interacts directly with CBX5 via the PxVxL motif. Interacts with RAD50, MRE11 and NBN; indicative for an association with the MRN complex. Interacts with histone H2AFY. Interacts with histone H3 peptides methylated at 'Lys-10' with preferences H3K9me3 > H3K9me2 > H3K9me1. Interacts with histone H3 peptides unmethylated at 'Lys-5' (H3K4me0). Interacts with MECP2, SMC1 and SMC3. Interacts with SETDB1, TRIM28 and ZNF274 (By similarity). {ECO:0000250|UniProtKB:P46100, ECO:0000269|PubMed:17296936, ECO:0000269|PubMed:20110566, ECO:0000269|PubMed:20159591, ECO:0000269|PubMed:24651726}. DOMAIN: The ADD domain predominantly interacts with histone H3 trimethylated at 'Lys-10'(H3K9me3) (and to a lesser extent H3 mono-or dimethylated at 'Lys-10') and simultanously to histone H3 unmethylated at 'Lys-5' (H3K4me0). The interaction with H3K9me3 is disrupted by the presence of H3K4me3 suggesting a readout of the combined histone H3 methylation state (By similarity). {ECO:0000250}.; DOMAIN: Contains one Pro-Xaa-Val-Xaa-Leu (PxVxL) motif, which is required for interaction with chromoshadow domains. This motif requires additional residues -7, -6, +4 and +5 of the central Val which contact the chromoshadow domain. +Q9R001 ATS5_MOUSE A disintegrin and metalloproteinase with thrombospondin motifs 5 (ADAM-TS 5) (ADAM-TS5) (ADAMTS-5) (EC 3.4.24.-) (ADMP-2) (Aggrecanase-2) (Implantin) 930 101,844 Active site (1); Chain (1); Compositional bias (3); Disulfide bond (11); Domain (4); Glycosylation (7); Metal binding (4); Motif (1); Propeptide (1); Region (1); Sequence conflict (4); Signal peptide (1) FUNCTION: Metalloproteinase that plays an important role in connective tissue organization, development, inflammation, arthritis, and cell migration. ADAMTS5 is an extracellular matrix (ECM) degrading enzyme that show proteolytic activity toward the hyalectan group of chondroitin sulfate proteoglycans (CSPGs) including aggrecan, versican, brevican and neurocan. Cleavage within the hyalectans occurs at Glu-Xaa recognition motifs. Plays a role in embryonic development, including limb and cardiac morphogenesis, and skeletal muscle development through its versican remodeling properties. Participates in the development of brown adipose tissue and browning of white adipose tissue (PubMed:28702327). Plays an important role for T-lymphocyte migration from draining lymph nodes following viral infection (PubMed:27855162). {ECO:0000269|PubMed:15800625, ECO:0000269|PubMed:27855162, ECO:0000269|PubMed:28702327}. PTM: The precursor is cleaved by furin and PCSK7 outside of the cell. {ECO:0000250|UniProtKB:Q9UNA0}.; PTM: C- and O-glycosylated (By similarity). O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation can mediate the efficient secretion of ADAMTS family members. Can be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated. These other glycosylations can also facilitate secretion. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q9UNA0}. DOMAIN: The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix.; DOMAIN: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme. +P58459 ATS10_MOUSE A disintegrin and metalloproteinase with thrombospondin motifs 10 (ADAM-TS 10) (ADAM-TS10) (ADAMTS-10) (EC 3.4.24.-) 1104 121,086 Active site (1); Alternative sequence (5); Chain (1); Compositional bias (2); Disulfide bond (14); Domain (8); Erroneous gene model prediction (1); Erroneous initiation (1); Frameshift (1); Glycosylation (5); Metal binding (3); Propeptide (1); Region (1); Signal peptide (1) FUNCTION: Metalloprotease that participate in microfibrils assembly. Microfibrils are extracellular matrix components occurring independently or along with elastin in the formation of elastic tissues (By similarity). {ECO:0000250}. PTM: Glycosylated. Can be O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS family members. Also can be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated. These other glycosylations can also facilitate secretion (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. SUBUNIT: Interacts with FBN1; this interaction promotes microfibrils assembly. {ECO:0000250}. DOMAIN: The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed in adult tissues. {ECO:0000269|PubMed:15355968}. +Q811B3 ATS12_MOUSE A disintegrin and metalloproteinase with thrombospondin motifs 12 (ADAM-TS 12) (ADAM-TS12) (ADAMTS-12) (EC 3.4.24.-) 1600 177,769 Active site (1); Alternative sequence (2); Chain (1); Compositional bias (2); Disulfide bond (11); Domain (11); Glycosylation (1); Metal binding (4); Motif (1); Propeptide (1); Region (2); Sequence conflict (1); Signal peptide (1) FUNCTION: Metalloprotease that plays a role in the degradation of COMP (By similarity). Cleaves also alpha-2 macroglobulin and aggregan. Has anti-tumorigenic properties (By similarity). {ECO:0000250}. PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}.; PTM: Subjected to an intracellular maturation process yielding a 120 kDa N-terminal fragment containing the metalloproteinase, disintegrin, one TSP type-1 and the Cys-rich domains and a 83 kDa C-terminal fragment containing the spacer 2 and four TSP type-1 domains. {ECO:0000250}.; PTM: Glycosylated. Can be O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS family members. Also can be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated. These other glycosylations can also facilitate secretion (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. SUBUNIT: Interacts with COMP. {ECO:0000250}. DOMAIN: The C-terminal four TSP1-like repeats are necessary and sufficient for binding COMP. {ECO:0000250}.; DOMAIN: The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix. {ECO:0000250}.; DOMAIN: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme. +Q769J6 ATS13_MOUSE A disintegrin and metalloproteinase with thrombospondin motifs 13 (ADAM-TS 13) (ADAM-TS13) (ADAMTS-13) (EC 3.4.24.87) (von Willebrand factor-cleaving protease) (vWF-CP) (vWF-cleaving protease) 1426 155,357 Active site (1); Chain (1); Disulfide bond (14); Domain (12); Glycosylation (14); Metal binding (11); Motif (1); Natural variant (2); Propeptide (1); Region (2); Sequence conflict (1); Signal peptide (1) FUNCTION: Cleaves the vWF multimers in plasma into smaller forms thereby controlling vWF-mediated platelet thrombus formation. {ECO:0000269|PubMed:15869605}. PTM: The precursor is processed by a furin endopeptidase which cleaves off the pro-domain. {ECO:0000250}.; PTM: O-glycosylated (By similarity). O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS13. May also be C-glycosylated on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and also N-glycosylated. These other glycosylations can also facilitate secretion (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15136581}. Note=Secretion enhanced by O-fucosylation of TSP type-1 repeats. {ECO:0000250}. DOMAIN: The pro-domain is not required for folding or secretion and does not perform the common function of maintening enzyme latency. {ECO:0000250}.; DOMAIN: The globular cysteineless spacer domain adopts a jelly-roll topology, and is necessary to recognize and cleave vWF. The C-terminal TSP type-1 and CUB domains may modulate this interaction (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Plasma. Expression is consistently high in liver, medium in lung and spleen, low in skeletal muscle and undetectable in heart, brain, kidney and testis. {ECO:0000269|PubMed:15136581, ECO:0000269|PubMed:15869605}. +Q8QZR1 ATTY_MOUSE Tyrosine aminotransferase (TAT) (EC 2.6.1.5) (L-tyrosine:2-oxoglutarate aminotransferase) 454 50,565 Beta strand (14); Chain (1); Helix (15); Modified residue (3); Sequence conflict (3); Turn (6) Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 2/6. FUNCTION: Transaminase involved in tyrosine breakdown. Converts tyrosine to p-hydroxyphenylpyruvate. Can catalyze the reverse reaction, using glutamic acid, with 2-oxoglutarate as cosubstrate (in vitro). Has much lower affinity and transaminase activity for phenylalanine. {ECO:0000269|PubMed:21153519}. SUBUNIT: Homodimer. {ECO:0000250}. +P59384 ATS15_MOUSE A disintegrin and metalloproteinase with thrombospondin motifs 15 (ADAM-TS 15) (ADAM-TS15) (ADAMTS-15) (EC 3.4.24.-) 950 103,938 Active site (1); Chain (1); Compositional bias (1); Disulfide bond (11); Domain (5); Glycosylation (4); Metal binding (4); Motif (1); Propeptide (1); Region (1); Sequence conflict (3); Signal peptide (1) PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}.; PTM: Glycosylated. Can be O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS family members. Also can be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated. These other glycosylations can also facilitate secretion (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. DOMAIN: The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix. {ECO:0000250}.; DOMAIN: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme. +Q8R4I1 ATX7_MOUSE Ataxin-7 (Spinocerebellar ataxia type 7 protein homolog) 867 92,697 Chain (1); Compositional bias (6); Cross-link (2); Domain (1); Modified residue (1); Sequence conflict (4) FUNCTION: Involved in neurodegeneration. Acts as component of the STAGA transcription coactivator-HAT complex. Mediates the interaction of STAGA complex with the CRX and is involved in CRX-dependent gene activation (By similarity). Necessary for microtubule cytoskeleton stabilization (By similarity). {ECO:0000250}. PTM: Proteolytically cleaved. {ECO:0000250}.; PTM: Sumoylation has no effect on subcellular location or interaction with components of the STAGA complex. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Nucleus, nucleolus {ECO:0000250}. Nucleus matrix {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=In addition to a diffuse distribution throughout the nucleus, it is associated with the nuclear matrix and the nucleolus. It is able to shuttle between the nucleus and cytoplasm (By similarity). {ECO:0000250}. SUBUNIT: Component of the STAGA transcription coactivator-HAT complex, at least composed of SUPT3H, GCN5L2, TAF5L, TAF6L, SUPT7L, TADA3L, TAD1L, TAF10, TAF12, TRRAP, TAF9 and ATXN7. The STAGA core complex is associated with a subcomplex required for histone deubiquitination composed of ATXN7L3, ENY2 and USP22. Interacts with SORBS1, PSMC1 and CRX. Interacts with TRRAP, GCN5L2 and TAF10 (By similarity). Interacts with alpha tubulin (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed in adult tissues, with the highest expression in heart, brain, liver and kidney. +P70295 AUP1_MOUSE Ancient ubiquitous protein 1 410 46,121 Chain (1); Domain (1); Modified residue (4); Topological domain (2); Transmembrane (1) TRANSMEM 21 41 Helical; Signal-anchor for type III membrane protein. {ECO:0000255}. TOPO_DOM 1 20 Lumenal. {ECO:0000255}.; TOPO_DOM 42 410 Cytoplasmic. {ECO:0000255}. FUNCTION: May play a role in the translocation of terminally misfolded proteins from the endoplasmic reticulum lumen to the cytoplasm and their degradation by the proteasome. {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. SUBUNIT: Identified in a complex that contains SEL1L, OS9, FAF2/UBXD8, UBE2J1/UBC6E and AUP1. Interacts with the cytoplasmic tail of ITGA2B, ITGA1, ITGA2, ITGA5, ITGAV and ITGAM (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. +O88398 AVIL_MOUSE Advillin (Actin-binding protein DOC6) (p92) 819 92,032 Chain (1); Domain (1); Modified residue (3); Region (4); Repeat (6); Sequence conflict (5) FUNCTION: Ca(2+)-regulated actin-binding protein. May have a unique function in the morphogenesis of neuronal cells which form ganglia. Required for SREC1-mediated regulation of neurite-like outgrowth. Plays a role in regenerative sensory axon outgrowth and remodeling processes after peripheral injury in neonates. Involved in the formation of long fine actin-containing filopodia-like structures in fibroblast. Plays a role in ciliogenesis. {ECO:0000269|PubMed:15247299, ECO:0000269|PubMed:18160648}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell projection {ECO:0000250}. Cell projection, axon {ECO:0000250}. SUBUNIT: Associates (via C-terminus) with actin. Interacts with F-actin (By similarity). Interacts with SCARF1; the interaction occurs in embryonic dorsal root ganglions at 18 dpc and induces neurite-like outgrowth. {ECO:0000250, ECO:0000269|PubMed:15247299}. TISSUE SPECIFICITY: Most highly expressed in the endometrium of the uterus, the intestinal villi and the testes. Weaker expression also detected in the brain, dorsal root ganglions and on the surface of the tongue. {ECO:0000269|PubMed:15247299, ECO:0000269|PubMed:18160648, ECO:0000269|PubMed:9664034}. +P27038 AVR2A_MOUSE Activin receptor type-2A (EC 2.7.11.30) (Activin receptor type IIA) (ACTR-IIA) 513 57,890 Active site (1); Beta strand (8); Binding site (1); Chain (1); Disulfide bond (5); Domain (1); Glycosylation (2); Helix (3); Nucleotide binding (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 136 161 Helical. {ECO:0000255}. TOPO_DOM 20 135 Extracellular. {ECO:0000255}.; TOPO_DOM 162 513 Cytoplasmic. {ECO:0000255}. FUNCTION: On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for activin A, activin B and inhibin A. Mediates induction of adipogenesis by GDF6 (PubMed:23527555). {ECO:0000269|PubMed:23527555}. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Interacts with AIP1. Part of a complex consisting of AIP1, ACVR2A, ACVR1B and SMAD3. {ECO:0000269|PubMed:10681527}. TISSUE SPECIFICITY: Brain, testis, intestine, liver and kidney. +P27040 AVR2B_MOUSE Activin receptor type-2B (EC 2.7.11.30) (Activin receptor type IIB) (ACTR-IIB) 536 60,542 Active site (1); Alternative sequence (2); Beta strand (8); Binding site (1); Chain (1); Disulfide bond (5); Domain (1); Glycosylation (2); Helix (1); Nucleotide binding (1); Region (1); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (2) TRANSMEM 138 158 Helical. {ECO:0000255}. TOPO_DOM 19 137 Extracellular. {ECO:0000255}.; TOPO_DOM 159 536 Cytoplasmic. {ECO:0000255}. FUNCTION: Transmembrane serine/threonine kinase activin type-2 receptor forming an activin receptor complex with activin type-1 serine/threonine kinase receptors (ACVR1, ACVR1B or ACVR1c). Transduces the activin signal from the cell surface to the cytoplasm and is thus regulating many physiological and pathological processes including neuronal differentiation and neuronal survival, hair follicle development and cycling, FSH production by the pituitary gland, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. Activin is also thought to have a paracrine or autocrine role in follicular development in the ovary. Within the receptor complex, the type-2 receptors act as a primary activin receptors (binds activin-A/INHBA, activin-B/INHBB as well as inhibin-A/INHA-INHBA). The type-1 receptors like ACVR1B act as downstream transducers of activin signals. Activin binds to type-2 receptor at the plasma membrane and activates its serine-threonine kinase. The activated receptor type-2 then phosphorylates and activates the type-1 receptor. Once activated, the type-1 receptor binds and phosphorylates the SMAD proteins SMAD2 and SMAD3, on serine residues of the C-terminal tail. Soon after their association with the activin receptor and subsequent phosphorylation, SMAD2 and SMAD3 are released into the cytoplasm where they interact with the common partner SMAD4. This SMAD complex translocates into the nucleus where it mediates activin-induced transcription. Inhibitory SMAD7, which is recruited to ACVR1B through FKBP1A, can prevent the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. Activin signal transduction is also antagonized by the binding to the receptor of inhibin-B via the IGSF1 inhibin coreceptor (By similarity). {ECO:0000250}. PTM: Phosphorylated. Constitutive phosphorylation is in part catalyzed by its own kinase activity (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Forms an activin receptor complex with activin type II receptors such as ACVR1B. Interacts with VPS39. Interacts with DYNLT1. {ECO:0000250, ECO:0000269|PubMed:27502274}. +Q8K4J2 COE4_MOUSE Transcription factor COE4 (Early B-cell factor 4) (EBF-4) (Olf-1/EBF-like 4) (O/E-4) (OE-4) 599 64,624 Alternative sequence (8); Chain (1); Domain (1); Region (3); Site (2); Zinc finger (1) FUNCTION: Seems to weakly activate transcription. Binds an Olf-1 consensus site in vitro. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Forms either a homodimer or a heterodimer with a related family member. TISSUE SPECIFICITY: Expressed in the neuronal and basal cell layers of olfactory epithelium. Absent in the vomeronasal organ. {ECO:0000269|PubMed:12139918}. +A2ADU9 AWAT1_MOUSE Acyl-CoA wax alcohol acyltransferase 1 (EC 2.3.1.75) (Diacylglycerol O-acyltransferase 2-like protein 3) (Long-chain-alcohol O-fatty-acyltransferase 1) 328 37,573 Chain (1); Transmembrane (2) TRANSMEM 12 32 Helical. {ECO:0000255}.; TRANSMEM 34 53 Helical. {ECO:0000255}. FUNCTION: Acyltransferase that predominantly esterify long chain (wax) alcohols with acyl-CoA-derived fatty acids to produce wax esters. Wax esters are enriched in sebum, suggesting that it plays a central role in lipid metabolism in skin. Has a preference for arachidyl alcohol as well as decyl alcohol, demonstrating its relatively poor activity using saturated long chain alcohols (C16, C18, and C20) (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q3UZ57 AXDN1_MOUSE Axonemal dynein light chain domain-containing protein 1 424 49,806 Chain (1); Coiled coil (1) +O35206 COFA1_MOUSE Collagen alpha-1(XV) chain [Cleaved into: Restin (Endostatin-XV)] 1367 140,472 Beta strand (10); Chain (2); Disulfide bond (2); Domain (5); Glycosylation (9); Helix (6); Region (15); Sequence conflict (11); Signal peptide (1); Turn (1) FUNCTION: Structural protein that stabilizes microvessels and muscle cells, both in heart and in skeletal muscle.; FUNCTION: Restin potently inhibits angiogenesis. PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. {ECO:0000250}.; PTM: O-glycosylated; contains chondroitin sulfate. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. SUBUNIT: Trimer; disulfide-linked. {ECO:0000250}. TISSUE SPECIFICITY: Detected in testis, brain, heart, kidney, skeletal muscle and skin (at protein level). Detected in heart and skeletal muscle. {ECO:0000269|PubMed:9339358}. +Q9QYP6 AZI2_MOUSE 5-azacytidine-induced protein 2 (NF-kappa-B-activating kinase-associated protein 1) (Nak-associated protein 1) 405 46,091 Alternative sequence (3); Chain (1); Coiled coil (1); Modified residue (2); Mutagenesis (5); Region (2) FUNCTION: Adapter protein which binds TBK1 and IKBKE playing a role in antiviral innate immunity. Activates serine/threonine-protein kinase TBK1 and facilitates its oligomerization. Enhances the phosphorylation of NF-kappa-B p65 subunit RELA by TBK1. Promotes TBK1-induced as well as TNF-alpha or PMA-induced activation of NF-kappa-B. Participates in IFNB promoter activation via TICAM1. {ECO:0000269|PubMed:17568778}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10580148}. SUBUNIT: Homodimer. Interacts with IKBKE, TBK1 and TICAM1. {ECO:0000269|PubMed:17568778}. TISSUE SPECIFICITY: Testis, ovary, heart, lung, kidney and brain. Expressed mainly in the spermatocytes or spermatids in the testis. {ECO:0000269|PubMed:10580148}. +O35484 AZIN1_MOUSE Antizyme inhibitor 1 (AZI) (Ornithine decarboxylase antizyme inhibitor) 448 49,549 Beta strand (17); Chain (1); Helix (17); Sequence conflict (2); Site (1); Turn (2) FUNCTION: Antizyme inhibitor (AZI) protein that positively regulates ornithine decarboxylase (ODC) activity and polyamine uptake. AZI is an enzymatically inactive ODC homolog that counteracts the negative effect of ODC antizymes (AZs) OAZ1, OAZ2 and OAZ3 on ODC activity by competing with ODC for antizyme-binding (PubMed:16916800, PubMed:18062773, PubMed:18508777). Inhibits antizyme-dependent ODC degradation and releases ODC monomers from their inactive complex with antizymes, leading to formation of the catalytically active ODC homodimer and restoring polyamine production (PubMed:10698696, PubMed:18062773, PubMed:18369191). {ECO:0000269|PubMed:10698696, ECO:0000269|PubMed:16916800, ECO:0000269|PubMed:18062773, ECO:0000269|PubMed:18369191, ECO:0000269|PubMed:18508777}. PTM: Ubiquitinated, leading to its proteasomal degradation; a process that is reduced in presence of antizyme OAZ1. {ECO:0000269|PubMed:18062773}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19449338}. SUBUNIT: Monomer (PubMed:18369191). Interacts with OAZ1 and OAZ3; this interaction disrupts the interaction between the antizyme and ODC1 (PubMed:18062773, PubMed:18369191). {ECO:0000269|PubMed:18062773, ECO:0000269|PubMed:18369191}. TISSUE SPECIFICITY: Expressed during testis development. {ECO:0000269|PubMed:18508777, ECO:0000269|PubMed:18973822}. +Q9Z160 COG1_MOUSE Conserved oligomeric Golgi complex subunit 1 (COG complex subunit 1) (Component of oligomeric Golgi complex 1) (Low density lipoprotein receptor defect B-complementing protein) 980 109,050 Chain (1); Initiator methionine (1); Modified residue (3); Sequence conflict (5) FUNCTION: Required for normal Golgi function. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. SUBUNIT: Component of the conserved oligomeric Golgi complex which is composed of eight different subunits and is required for normal Golgi morphology and localization. {ECO:0000250}. +Q921L5 COG2_MOUSE Conserved oligomeric Golgi complex subunit 2 (COG complex subunit 2) (Component of oligomeric Golgi complex 2) (Low density lipoprotein receptor defect C-complementing protein) 731 82,040 Chain (1); Sequence conflict (3) FUNCTION: Required for normal Golgi morphology and function. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. SUBUNIT: Component of the conserved oligomeric Golgi complex which is composed of eight different subunits and is required for normal Golgi morphology and localization. {ECO:0000250}. +Q8CI04 COG3_MOUSE Conserved oligomeric Golgi complex subunit 3 (COG complex subunit 3) (Component of oligomeric Golgi complex 3) 820 93,283 Chain (1); Modified residue (1) FUNCTION: Involved in ER-Golgi transport. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Associated with the peripheral membrane of cis/medial cisternae. {ECO:0000250}. SUBUNIT: Component of the conserved oligomeric Golgi complex which is composed of eight different subunits and is required for normal Golgi morphology and localization. Interacts with TMEM115. {ECO:0000250}. +Q8R1U1 COG4_MOUSE Conserved oligomeric Golgi complex subunit 4 (COG complex subunit 4) (Component of oligomeric Golgi complex 4) 785 88,661 Chain (1); Initiator methionine (1); Modified residue (2); Region (4) FUNCTION: Required for normal Golgi function. Plays a role in SNARE-pin assembly and Golgi-to-ER retrograde transport via its interaction with SCFD1 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. SUBUNIT: Monomer. Component of the conserved oligomeric Golgi (COG) complex which is composed of eight different subunits and is required for normal Golgi morphology and localization. Mediates interaction of SCFD1 with the COG complex. Interacts with STX5 (By similarity). {ECO:0000250}. +Q8C0L8 COG5_MOUSE Conserved oligomeric Golgi complex subunit 5 (COG complex subunit 5) (Component of oligomeric Golgi complex 5) 829 91,391 Chain (1); Erroneous initiation (1); Modified residue (1); Sequence conflict (4) FUNCTION: Required for normal Golgi function. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. SUBUNIT: Component of the conserved oligomeric Golgi complex which is composed of eight different subunits and is required for normal Golgi morphology and localization. {ECO:0000250}. +Q8R3I3 COG6_MOUSE Conserved oligomeric Golgi complex subunit 6 (COG complex subunit 6) (Component of oligomeric Golgi complex 6) 657 73,040 Chain (1); Erroneous initiation (1); Sequence conflict (9) FUNCTION: Required for normal Golgi function. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. SUBUNIT: Component of the conserved oligomeric Golgi complex which is composed of eight different subunits and is required for normal Golgi morphology and localization. {ECO:0000250}. +Q3UM29 COG7_MOUSE Conserved oligomeric Golgi complex subunit 7 (COG complex subunit 7) (Component of oligomeric Golgi complex 7) 770 86,073 Chain (1); Sequence conflict (2) FUNCTION: Required for normal Golgi function. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. SUBUNIT: Component of the conserved oligomeric Golgi complex which is composed of eight different subunits and is required for normal Golgi morphology and localization. {ECO:0000250}. +Q9JJA2 COG8_MOUSE Conserved oligomeric Golgi complex subunit 8 (COG complex subunit 8) (Component of oligomeric Golgi complex 8) 640 71,602 Chain (1); Sequence conflict (2) FUNCTION: Required for normal Golgi function. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. SUBUNIT: Component of the conserved oligomeric Golgi complex which is composed of eight different subunits and is required for normal Golgi morphology and localization. {ECO:0000250}. +Q8BLX7 COGA1_MOUSE Collagen alpha-1(XVI) chain 1580 155,805 Alternative sequence (1); Chain (1); Domain (10); Glycosylation (2); Motif (3); Region (19); Sequence conflict (2); Signal peptide (1) FUNCTION: Involved in mediating cell attachment and inducing integrin-mediated cellular reactions, such as cell spreading and alterations in cell morphology. {ECO:0000250|UniProtKB:Q07092}. PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. {ECO:0000305}.; PTM: Glycosylated. {ECO:0000250|UniProtKB:Q07092}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. SUBUNIT: Homotrimer. Interacts with FBN1, fibronectin and integrins ITGA1/ITGB1 and ITGA2/ITGB1. Integrin ITGA1/ITGB1 binds to a unique site within COL16A1 located close to its C-terminal end between collagenous domains COL1-COL3 (By similarity). {ECO:0000250|UniProtKB:Q07092}. DOMAIN: This sequence defines eighteen different domains, nine triple-helical domains (COL9 to COL1) and ten non-triple-helical domains (NC10 to NC1). The numerous interruptions in the triple helix may make this molecule either elastic or flexible. {ECO:0000255}. TISSUE SPECIFICITY: Expressed in most tissues examined with highest levels of expression observed in heart. Strongly expressed in cortical and medullar regions of kidney and more weakly expressed in lung. Also detected in the ciliary muscle of the eye, on the serosa layer lining the muscularis externa of intestinal tissue, and in the perimysium membrane lining both the cardiac muscle bundle and the smooth muscle tissue of the small intestine. Strongly stained in particulate or granular structures. Not detected in brain or skeletal muscle. {ECO:0000269|PubMed:8650669}. +Q07563 COHA1_MOUSE Collagen alpha-1(XVII) chain (180 kDa bullous pemphigoid antigen 2) (Bullous pemphigoid antigen 2) [Cleaved into: 120 kDa linear IgA disease antigen homolog] 1470 147,975 Alternative sequence (1); Chain (2); Glycosylation (2); Modified residue (1); Region (4); Sequence conflict (13); Topological domain (2); Transmembrane (1) TRANSMEM 477 497 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 476 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 498 1470 Extracellular. {ECO:0000255}. FUNCTION: May play a role in the integrity of hemidesmosome and the attachment of basal keratinocytes to the underlying basement membrane. {ECO:0000250}.; FUNCTION: The 120 kDa linear IgA disease antigen homolog is an anchoring filament component involved in dermal-epidermal cohesion. {ECO:0000250}. PTM: The intracellular/endo domain is disulfide-linked. {ECO:0000250}.; PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.; PTM: The ectodomain is shedded from the surface of keratinocytes resulting in a 120-kDa soluble form, also named as 120 kDa linear IgA disease antigen homolog. The shedding is mediated by membrane-bound metalloproteases. This cleavage is inhibited by phosphorylation at Ser-551 (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, hemidesmosome. Membrane; Single-pass type II membrane protein. Note=Localized along the plasma membrane of the hemidesmosome. {ECO:0000250}.; SUBCELLULAR LOCATION: 120 kDa linear IgA disease antigen homolog: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000250}. SUBUNIT: Homotrimers of alpha 1(XVII)chains. Interacts (via cytoplasmic region) with ITGB4 (via cytoplasmic region). Interacts (via cytoplasmic region) with DST (via N-terminus). Interacts (via N-terminus) with PLEC. Interacts (via cytoplasmic region) with DSP (By similarity). {ECO:0000250}. +P39061 COIA1_MOUSE Collagen alpha-1(XVIII) chain [Cleaved into: Endostatin; Non-collagenous domain 1 (NC1)] 1774 182,172 Alternative sequence (3); Beta strand (10); Chain (3); Disulfide bond (7); Domain (9); Glycosylation (4); Helix (6); Metal binding (5); Modified residue (1); Motif (1); Mutagenesis (4); Region (23); Sequence conflict (13); Signal peptide (1); Turn (2) FUNCTION: Probably plays a major role in determining the retinal structure as well as in the closure of the neural tube. {ECO:0000250|UniProtKB:P39060}.; FUNCTION: Non-collagenous domain 1: May regulate extracellular matrix-dependent motility and morphogenesis of endothelial and non-endothelial cells; the function requires homotrimerization and implicates MAPK signaling. {ECO:0000250|UniProtKB:P39060}.; FUNCTION: Endostatin: Potently inhibits endothelial cell proliferation and angiogenesis. May inhibit angiogenesis by binding to the heparan sulfate proteoglycans involved in growth factor signaling (PubMed:9008168). Inhibits VEGFA isoform VEGF165-induced endothelial cell proliferation and migration. Seems to inhibit VEGFA-mediated signaling by blocking the interaction of VEGFA to its receptor KDR/VEGFR2 (PubMed:12029087). Modulates endothelial cell migration in an integrin-dependent manner implicating integrin ITGA5:ITGB1 and to a lesser extent ITGAV:ITGB3 and ITGAV:ITGB5 (PubMed:11158588). May negatively regulate the activity of homotrimeric non-collagenous domain 1 (By similarity). {ECO:0000250|UniProtKB:P39060, ECO:0000269|PubMed:11158588, ECO:0000269|PubMed:9008168}. PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) of the triple-helical regions are hydroxylated.; PTM: Undergoes proteolytic processing by cathepsin-L and elastase-like proteases to generate both non-collagenous domain 1 trimers and endostatin monomers. In tissue extracts (brain, skeletal muscle, heart, kidney, testis and liver) predominantly bands of approximately 38 kDa are detected; recombinant non-collagenous domain 1 shows similar mobility. In vitro, several proteolytic cleavage sites in the non-collagenous domain 1 hinge region generating different endostatin-like peptides are reported. {ECO:0000250|UniProtKB:P39060, ECO:0000269|PubMed:10626789, ECO:0000269|PubMed:10716919, ECO:0000305|PubMed:9687493}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000269|PubMed:9687493}.; SUBCELLULAR LOCATION: Non-collagenous domain 1: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000305|PubMed:9687493}. Secreted {ECO:0000269|PubMed:10626789}.; SUBCELLULAR LOCATION: Endostatin: Secreted {ECO:0000269|PubMed:10626789, ECO:0000305|PubMed:9008168}. Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000305}. SUBUNIT: Non-collagenous domain 1 forms homotrimers. Endostatin is monomeric (PubMed:9687493). Recombinant non-collagenous domain 1 has stronger affinity to NID1, HSPG2 and laminin-1:NID1 complex and lower affinity to FBLN1 and FBLN2 than endostatin (PubMed:10966814). Endostatin interacts with KDR/VEGFR2 (PubMed:12029087). Endostatin interacts with the ITGA5:ITGB1 complex (PubMed:11158588). {ECO:0000269|PubMed:10966814, ECO:0000269|PubMed:11158588, ECO:0000269|PubMed:12029087, ECO:0000269|PubMed:9687493}. TISSUE SPECIFICITY: Expressed in liver, kidney, lung, skeletal muscle and testis. {ECO:0000269|PubMed:7876242}. +Q5SU73 COIL_MOUSE Coilin (p80-coilin) 570 61,917 Chain (1); Compositional bias (2); Cross-link (8); Domain (1); Modified residue (9); Region (2); Repeat (8); Sequence conflict (16) FUNCTION: Component of nuclear coiled bodies, also known as Cajal bodies or CBs, which are involved in the modification and assembly of nucleoplasmic snRNPs. {ECO:0000250|UniProtKB:P38432}. PTM: Symmetrical dimethylation of arginine residues within the RG repeat region enhances affinity for SMN, and thus localization of SMN complexes to CBs. {ECO:0000250}.; PTM: Phosphorylation during mitosis is associated with disassembly of CBs. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10806077}. Nucleus, Cajal body {ECO:0000250|UniProtKB:P38432}. SUBUNIT: Interacts with ANKS1B. Interacts with SMN1 (via Tudor domain). Interacts (via C-terminus) with AK6. Interacts with WRAP53/TCAB1. Interacts with HMBOX1. Interacts with PSME3; the interaction is inhibited by FAM192A. {ECO:0000250|UniProtKB:P38432}. DOMAIN: The atypical Tudor domain at the C-terminus contains two large unstructured loops, and does not bind methylated residues. {ECO:0000250}. TISSUE SPECIFICITY: Detectable in all tissues analyzed, with the highest levels in brain and testis. {ECO:0000269|PubMed:10806077}. +Q0VF58 COJA1_MOUSE Collagen alpha-1(XIX) chain (Collagen alpha-1(Y) chain) 1136 114,197 Chain (1); Domain (10); Glycosylation (1); Motif (1); Region (6); Sequence conflict (7); Signal peptide (1) FUNCTION: May act as a cross-bridge between fibrils and other extracellular matrix molecules. Involved in skeletal myogenesis in the developing esophagus. May play a role in organization of the pericellular matrix or the sphinteric smooth muscle. {ECO:0000269|PubMed:15302855, ECO:0000305}. PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. {ECO:0000305}. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. SUBUNIT: Oligomer; disulfide-linked. {ECO:0000250|UniProtKB:Q14993}. DOMAIN: The numerous interruptions in the triple helix may make this molecule either elastic or flexible. {ECO:0000250|UniProtKB:Q14993}. +Q923P0 COKA1_MOUSE Collagen alpha-1(XX) chain 1320 140,926 Alternative sequence (1); Chain (1); Domain (11); Erroneous initiation (2); Glycosylation (4); Sequence conflict (3); Signal peptide (1) FUNCTION: Probable collagen protein. SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000305}. +Q8CF98 COL10_MOUSE Collectin-10 (Collectin liver protein 1) (CL-L1) 277 30,524 Chain (1); Disulfide bond (2); Domain (2); Glycosylation (2); Sequence conflict (1); Signal peptide (1) FUNCTION: Lectin that binds to various sugars: galactose > mannose = fucose > N-acetylglucosamine > N-acetylgalactosamine. Acts as a chemoattractant, probably involved in the regulation of cell migration. {ECO:0000250|UniProtKB:Q9Y6Z7}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9Y6Z7}. Golgi apparatus {ECO:0000269|PubMed:28301481}. Cytoplasm {ECO:0000250|UniProtKB:Q9Y6Z7}. TISSUE SPECIFICITY: Expressed mainly in the liver and stomach, but also in muscles, testes, and intestines. {ECO:0000269|PubMed:12450124}. +Q3SXB8 COL11_MOUSE Collectin-11 (Collectin kidney protein 1) (CL-K1) 272 28,989 Alternative sequence (1); Binding site (3); Chain (1); Coiled coil (1); Disulfide bond (2); Domain (2); Metal binding (13); Region (1); Sequence conflict (1); Signal peptide (1) FUNCTION: Lectin that plays a role in innate immunity, apoptosis and embryogenesis. Calcium-dependent lectin that binds self and non-self glycoproteins presenting high mannose oligosaccharides with at least one terminal alpha-1,2-linked mannose epitope. Primarily recognizes the terminal disaccharide of the glycan. Also recognizes a subset of fucosylated glycans and lipopolysaccharides. Plays a role in innate immunity through its ability to bind non-self sugars presented by microorganisms and to activate the complement through the recruitment of MAPS1. Also plays a role in apoptosis through its ability to bind in a calcium-independent manner the DNA present at the surface of apoptotic cells and to activate the complement in response to this binding. Finally, plays a role in development, probably serving as a guidance cue during the migration of neural crest cells and other cell types during embryogenesis. {ECO:0000250|UniProtKB:Q9BWP8}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9BWP8}. SUBUNIT: Homotrimer; disulfide-linked. Interacts with MASP1; probably triggers the lectin pathway of complement. {ECO:0000250|UniProtKB:Q9BWP8}. TISSUE SPECIFICITY: Highly expressed in embryonic murine craniofacial cartilage, heart, bronchi, kidney and vertebral bodies. {ECO:0000269|PubMed:21258343}. +Q8K4Q8 COL12_MOUSE Collectin-12 (Collectin placenta protein 1) (CL-P1) (Scavenger receptor with C-type lectin) 742 81,304 Beta strand (8); Binding site (6); Chain (1); Coiled coil (2); Disulfide bond (3); Domain (3); Glycosylation (4); Helix (3); Metal binding (14); Sequence conflict (7); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 38 58 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 37 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 59 742 Extracellular. {ECO:0000255}. FUNCTION: Scavenger receptor that displays several functions associated with host defense. Promotes binding and phagocytosis of Gram-positive, Gram-negative bacteria and yeast. Binds also to sialyl Lewis X or a trisaccharide and asialo-orosomucoid (ASOR). Mediates the recognition, internalization and degradation of oxidatively modified low density lipoprotein (oxLDL) by vascular endothelial cells (By similarity). Binds to several carbohydrates including Gal-type ligands, D-galactose, L- and D-fucose, GalNAc, T and Tn antigens in a calcium-dependent manner and internalizes specifically GalNAc in nurse-like cells (By similarity). {ECO:0000250, ECO:0000269|PubMed:11718900}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Forms clusters on the cell surface. {ECO:0000250}. SUBUNIT: The extracellular domain forms a stable trimer (By similarity). The extracellular domain interacts with fibrillar amyloid-beta peptide. {ECO:0000250, ECO:0000269|PubMed:16868960, ECO:0000269|PubMed:17420244}. TISSUE SPECIFICITY: Expressed in vascular endothelial cells in the heart, in perivascular macrophage and smooth muscle cells. Expressed in plaques-surrounding reactive astrocytes located in cerebral cortex and hippocampus and in leptomeningeal vessels showing characteristics of cerebral amyloid angiopathy (CAA) in a double transgenic mouse model of Alzheimer disease (at protein level). Strongly expressed in lung. Moderately expressed in heart, skeletal muscle, spleen, liver, brain, colon, testis, stomach and kidney. Expressed in neonatal astrocytes. Expressed in reactive astrocytes and vascular/perivascular cells in the brain of a double transgenic mouse model of Alzheimer disease. {ECO:0000269|PubMed:11564734, ECO:0000269|PubMed:11718900, ECO:0000269|PubMed:16868960}. +O35348 COLQ_MOUSE Acetylcholinesterase collagenic tail peptide (AChE Q subunit) (Acetylcholinesterase-associated collagen) 457 47,684 Chain (1); Disulfide bond (5); Domain (2); Region (3); Sequence conflict (3); Signal peptide (1) FUNCTION: Anchors the catalytic subunits of asymmetric AChE to the synaptic basal lamina. {ECO:0000250}. PTM: The triple-helical tail is stabilized by disulfide bonds at each end. {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, synapse {ECO:0000250}. SUBUNIT: Homotrimer. Component of the asymmetric form of AChE, a disulfide-bonded oligomer composed of the collagenic subunits (Q) and a variable number of asymmetric catalytic subunits (T). The N-terminal of a collagenic subunit (Q) associates with the C-terminal of a catalytic subunit (T) (By similarity). {ECO:0000250}. DOMAIN: The proline-rich attachment domain (PRAD) binds the AChE catalytic subunits. {ECO:0000250}. +Q9CQC2 COL_MOUSE Colipase 113 12,445 Chain (1); Disulfide bond (5); Propeptide (1); Signal peptide (1) FUNCTION: Colipase is a cofactor of pancreatic lipase. It allows the lipase to anchor itself to the lipid-water interface. Without colipase the enzyme is washed off by bile salts, which have an inhibitory effect on the lipase.; FUNCTION: Enterostatin has a biological activity as a satiety signal. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted. SUBUNIT: Forms a 1:1 stoichiometric complex with pancreatic lipase. {ECO:0000255|PROSITE-ProRule:PRU00674}. TISSUE SPECIFICITY: Expressed by the pancreas. +Q3U129 B3GNL_MOUSE UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase-like protein 1 (BGnT-like protein 1) (Beta1,3-N-acetylglucosaminyltransferase-like protein 1) (Beta3Gn-T-like protein 1) (Beta3GnTL1) (EC 2.4.1.-) 357 40,644 Alternative sequence (3); Chain (1); Sequence conflict (1) FUNCTION: Putative glycosyltransferase. {ECO:0000305}. +Q8BGY6 B3GN5_MOUSE Lactosylceramide 1,3-N-acetyl-beta-D-glucosaminyltransferase (EC 2.4.1.206) (Lactotriaosylceramide synthase) (Lc(3)Cer synthase) (Lc3 synthase) (UDP-GlcNAc:beta-Gal beta-1,3-N-acetylglucosaminyltransferase 5) (BGnT-5) (Beta-1,3-Gn-T5) (Beta-1,3-N-acetylglucosaminyltransferase 5) (Beta3Gn-T5) 376 43,914 Chain (1); Glycosylation (1); Sequence conflict (2); Topological domain (2); Transmembrane (1) TRANSMEM 14 34 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 13 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 35 376 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Beta-1,3-N-acetylglucosaminyltransferase that plays a key role in the synthesis of lacto- or neolacto-series carbohydrate chains on glycolipids, notably by participating in biosynthesis of HNK-1 and Lewis X carbohydrate structures. Has strong activity toward lactosylceramide (LacCer) and neolactotetraosylceramide (nLc(4)Cer; paragloboside), resulting in the synthesis of Lc(3)Cer and neolactopentaosylceramide (nLc(5)Cer), respectively. Plays a central role in regulating neolacto-series glycolipid synthesis during embryonic development. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in adult spleen, placenta and cerebellar Purkinje cells where it colocalized with HNK-1. Expressed at lower level in brain, lung, thymus and muscle. {ECO:0000269|PubMed:11384981}. +Q9Z0F0 B3GT4_MOUSE Beta-1,3-galactosyltransferase 4 (Beta-1,3-GalTase 4) (Beta3Gal-T4) (Beta3GalT4) (b3Gal-T4) (EC 2.4.1.62) (Gal-T2) (Ganglioside galactosyltransferase) (UDP-galactose:beta-N-acetyl-galactosamine-beta-1,3-galactosyltransferase) 371 41,236 Chain (1); Glycosylation (1); Natural variant (2); Topological domain (2); Transmembrane (1) TRANSMEM 5 25 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 4 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 26 371 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Involved in GM1/GD1B/GA1 ganglioside biosynthesis. {ECO:0000269|PubMed:10502288}. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein. TISSUE SPECIFICITY: Expressed in heart, brain, spleen, kidney, lung and testis. {ECO:0000269|PubMed:10502288}. +Q9JI67 B3GT5_MOUSE Beta-1,3-galactosyltransferase 5 (Beta-1,3-GalTase 5) (Beta3Gal-T5) (Beta3GalT5) (b3Gal-T5) (EC 2.4.1.-) (Beta-3-Gx-T5) (Stage-specific embryonic antigen 3 synthase) (SSEA-3 synthase) (UDP-Gal:beta-GlcNAc beta-1,3-galactosyltransferase 5) (UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase 5) 308 35,964 Chain (1); Glycosylation (3); Topological domain (2); Transmembrane (1) TRANSMEM 8 25 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 7 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 26 308 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Catalyzes the transfer of Gal to GlcNAc-based acceptors with a preference for the core3 O-linked glycan GlcNAc(beta1,3)GalNAc structure. Can use glycolipid LC3Cer as an efficient acceptor. Also catalyzes the transfer of Gal to the terminal GalNAc unit of the globoside GB4, thereby synthesizing the glycolipid GB5, also known as the stage-specific embryonic antigen-3 (SSEA-3). SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. TISSUE SPECIFICITY: Expressed in brain and kidney. +O55029 COPB2_MOUSE Coatomer subunit beta' (Beta'-coat protein) (Beta'-COP) (p102) 905 102,449 Chain (1); Coiled coil (1); Modified residue (2); Mutagenesis (1); Repeat (9); Sequence conflict (3) FUNCTION: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). {ECO:0000250}.; FUNCTION: This coatomer complex protein, essential for Golgi budding and vesicular trafficking, is a selective binding protein (RACK) for protein kinase C, epsilon type. It binds to Golgi membranes in a GTP-dependent manner. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:17360540}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. Shows only a slight preference for the cis-Golgi apparatus, compared with the trans-Golgi. {ECO:0000250}. SUBUNIT: Oligomeric complex that consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits. Probably interacts with PEX11A. Interacts with SCYL1. Interacts with JAGN1 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P35606}. +Q91Z92 B3GT6_MOUSE Beta-1,3-galactosyltransferase 6 (Beta-1,3-GalTase 6) (Beta3Gal-T6) (Beta3GalT6) (EC 2.4.1.134) (GAG GalTII) (Galactosyltransferase II) (Galactosylxylosylprotein 3-beta-galactosyltransferase) (UDP-Gal:betaGal beta 1,3-galactosyltransferase polypeptide 6) 325 37,021 Chain (1); Glycosylation (1); Topological domain (2); Transmembrane (1) TRANSMEM 12 30 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 11 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 31 325 Lumenal. {ECO:0000255}. Glycan metabolism; chondroitin sulfate biosynthesis. Glycan metabolism; heparan sulfate biosynthesis. FUNCTION: Beta-1,3-galactosyltransferase that transfers galactose from UDP-galactose to substrates with a terminal beta-linked galactose residue. Has a preference for galactose-beta-1,4-xylose that is found in the linker region of glycosaminoglycans, such as heparan sulfate and chondroitin sulfate. Has no activity towards substrates with terminal glucosamine or galactosamine residues (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. +Q8BWP8 B4GA1_MOUSE Beta-1,4-glucuronyltransferase 1 (EC 2.4.1.-) (I-beta-1,3-N-acetylglucosaminyltransferase) (iGnT) (N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase) (Poly-N-acetyllactosamine extension enzyme) (UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 1) 415 47,384 Alternative sequence (2); Chain (1); Glycosylation (2); Metal binding (2); Mutagenesis (1); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 9 36 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 8 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 37 415 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Beta-1,4-glucuronyltransferase involved in O-mannosylation of alpha-dystroglycan (DAG1). Transfers a glucuronic acid (GlcA) residue onto a xylose (Xyl) acceptor to produce the glucuronyl-beta-1,4-xylose-beta disaccharide primer, which is further elongated by LARGE1, during synthesis of phosphorylated O-mannosyl glycan. Phosphorylated O-mannosyl glycan is a carbohydrate is a carbohydrate structure present in alpha-dystroglycan (DAG1), which is required for binding laminin G-like domain-containing extracellular proteins with high affinity (PubMed:25279699). Required for axon guidance; via its function in O-mannosylation of alpha-dystroglycan (DAG1) (PubMed:23217742). {ECO:0000269|PubMed:23217742, ECO:0000269|PubMed:25279699}. SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:23217742}; Single-pass type II membrane protein. Note=Localizes near the trans-Golgi apparatus. {ECO:0000250|UniProtKB:O43505}. SUBUNIT: Interacts with LARGE1 and LARGE2. {ECO:0000250|UniProtKB:O43505}. +Q09200 B4GN1_MOUSE Beta-1,4 N-acetylgalactosaminyltransferase 1 (EC 2.4.1.92) ((N-acetylneuraminyl)-galactosylglucosylceramide) (GM2/GD2 synthase) (GalNAc-T) 533 59,212 Chain (1); Disulfide bond (5); Glycosylation (3); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 8 25 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 7 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 26 533 Lumenal. {ECO:0000255}. Sphingolipid metabolism. FUNCTION: Involved in the biosynthesis of gangliosides GM2, GD2 and GA2. {ECO:0000269|PubMed:8855236}. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein. SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}. TISSUE SPECIFICITY: Most abundant in brain, liver, lung, spleen and testis. {ECO:0000269|PubMed:7558008}. +Q09199 B4GN2_MOUSE Beta-1,4 N-acetylgalactosaminyltransferase 2 (EC 2.4.1.-) 510 58,317 Chain (1); Glycosylation (1); Topological domain (2); Transmembrane (1) TRANSMEM 16 32 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 15 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 33 510 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Responsible for synthesis of murine T-lymphocyte CT antigen. Can transfer N-acetylgalactosamine moiety from UDP-GalNAc to the low molecular weight acceptor 3'-sialyl-N-acetyllactosamine, to form a non-reducing terminal tetrasaccharide Sda blood group structure. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein. +Q6L8S8 B4GN3_MOUSE Beta-1,4-N-acetylgalactosaminyltransferase 3 (Beta4GalNAc-T3) (Beta4GalNAcT3) (EC 2.4.1.244) (Beta-1,4-N-acetylgalactosaminyltransferase III) (N-acetyl-beta-glucosaminyl-glycoprotein 4-beta-N-acetylgalactosaminyltransferase 2) (NGalNAc-T2) 986 113,509 Chain (1); Domain (1); Topological domain (2); Transmembrane (1) TRANSMEM 25 45 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 24 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 46 986 Lumenal. {ECO:0000255}. FUNCTION: Transfers N-acetylgalactosamine (GalNAc) from UDP-GalNAc to N-acetylglucosamine-beta-benzyl with a beta-1,4-linkage to form N,N'-diacetyllactosediamine, GalNAc-beta-1,4-GlcNAc structures in N-linked glycans and probably O-linked glycans. Mediates the N,N'-diacetyllactosediamine formation on gastric mucosa (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. Note=Localizes to apical Golgi. {ECO:0000250}. +Q9QZE5 COPG1_MOUSE Coatomer subunit gamma-1 (Gamma-1-coat protein) (Gamma-1-COP) 874 97,513 Chain (1); Frameshift (1); Modified residue (1); Region (1); Repeat (4); Sequence conflict (5) FUNCTION: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). Required for limiting lipid storage in lipid droplets. Involved in lipid homeostasis by regulating the presence of perilipin family members PLIN2 and PLIN3 at the lipid droplet surface and promoting the association of adipocyte triglyceride lipase (PNPLA2) with the lipid droplet surface to mediate lipolysis. {ECO:0000250, ECO:0000269|PubMed:19067489}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:17360540}. Golgi apparatus membrane {ECO:0000269|PubMed:17360540}; Peripheral membrane protein {ECO:0000269|PubMed:17360540}; Cytoplasmic side {ECO:0000269|PubMed:17360540}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. Predominantly located in the cis-Golgi apparatus. {ECO:0000250}. SUBUNIT: Oligomeric complex that consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits. Interacts with ZNF289/ARFGAP2 through its C-terminal appendage domain (By similarity). Interacts with EGFR upon EGF treatment; interaction is essential for regulation of EGF-dependent nuclear transport of EGFR by retrograde trafficking from the Golgi to the ER (By similarity). Interacts with COPB1 (By similarity). Interacts with TMED10 (via C-terminus). Interacts with TMED2, TMED3, TMED7 and TMED9 (By similarity). {ECO:0000250}. +Q91YY2 B4GT3_MOUSE Beta-1,4-galactosyltransferase 3 (Beta-1,4-GalTase 3) (Beta4Gal-T3) (b4Gal-T3) (EC 2.4.1.-) (Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase) (Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase) (EC 2.4.1.38) (N-acetyllactosamine synthase) (EC 2.4.1.90) (Nal synthase) (UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 3) (UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 3) 395 44,084 Binding site (3); Chain (1); Disulfide bond (2); Glycosylation (4); Metal binding (2); Region (5); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 11 31 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 10 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 32 395 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Trans cisternae of Golgi stack. {ECO:0000250}. +Q9JMK0 B4GT5_MOUSE Beta-1,4-galactosyltransferase 5 (Beta-1,4-GalTase 5) (Beta4Gal-T5) (b4Gal-T5) (EC 2.4.1.-) (Beta-1,4-GalT II) (Glucosylceramide beta-1,4-galactosyltransferase) (EC 2.4.1.274) (Lactosylceramide synthase) (LacCer synthase) (UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 5) (UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 5) 388 44,814 Binding site (3); Chain (1); Disulfide bond (2); Glycosylation (7); Metal binding (2); Region (5); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 15 35 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 14 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 36 388 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. Sphingolipid metabolism. FUNCTION: Catalyzes the synthesis of lactosylceramide (LacCer) via the transfer of galactose from UDP-galactose to glucosylceramide (GlcCer) (PubMed:21057870, PubMed:23882130, PubMed:30114188). LacCer is the starting point in the biosynthesis of all gangliosides (membrane-bound glycosphingolipids) which play pivotal roles in the CNS including neuronal maturation and axonal and myelin formation (PubMed:30114188). Plays a role in the glycosylation of BMPR1A and regulation of its protein stability (PubMed:29415997). Essential for extraembryonic development during early embryogenesis (PubMed:20574042, PubMed:21057870). {ECO:0000269|PubMed:20574042, ECO:0000269|PubMed:21057870, ECO:0000269|PubMed:23882130, ECO:0000269|PubMed:29415997, ECO:0000269|PubMed:30114188}. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:P15291}; Single-pass type II membrane protein. Golgi apparatus {ECO:0000250|UniProtKB:A0A1S6M251}. Note=Trans cisternae of Golgi stack. {ECO:0000250|UniProtKB:P15291}. TISSUE SPECIFICITY: Highest levels in heart, brain, liver and kidney with lower levels in spleen, lung and testis. {ECO:0000269|PubMed:11145975, ECO:0000269|PubMed:23882130}. +Q3UI43 BABA1_MOUSE BRISC and BRCA1-A complex member 1 (Mediator of RAP80 interactions and targeting subunit of 40 kDa) (New component of the BRCA1-A complex) 333 36,793 Chain (1); Modified residue (4); Region (1); Sequence conflict (4) FUNCTION: Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). The BRCA1-A complex also possesses deubiquitinase activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. In the BRCA1-A complex, it is required for the complex integrity and its localization at DSBs. Component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates. In these 2 complexes, it is probably required to maintain the stability of BABAM2 and help the 'Lys-63'-linked deubiquitinase activity mediated by BRCC3/BRCC36 component. The BRISC complex is required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating NUMA1. Plays a role in interferon signaling via its role in the deubiquitination of the interferon receptor IFNAR1; deubiquitination increases IFNAR1 activity by enhancing its stability and cell surface expression. Down-regulates the response to bacterial lipopolysaccharide (LPS) via its role in IFNAR1 deubiquitination. {ECO:0000250|UniProtKB:Q9NWV8}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NWV8}. Nucleus {ECO:0000250|UniProtKB:Q9NWV8}. Note=Localizes at sites of DNA damage at double-strand breaks (DSBs). {ECO:0000250|UniProtKB:Q9NWV8}. SUBUNIT: Component of the ARISC complex, at least composed of UIMC1/RAP80, ABRAXAS1, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1. Component of the BRCA1-A complex, at least composed of BRCA1, BARD1, UIMC1/RAP80, ABRAXAS1, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1. In the BRCA1-A complex, interacts directly with ABRAXAS1 and BABAM2. Component of the BRISC complex, at least composed of ABRAXAS2, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1. Identified in a complex with SHMT2 and the other subunits of the BRISC complex. {ECO:0000250|UniProtKB:Q9NWV8}. DOMAIN: The VWFA-like region is similar to the VWFA domain. Its presence reveals similarities between the structure of the 19S proteasome and the BRCA1-A complexes. {ECO:0000250|UniProtKB:Q9NWV8}. +Q8R087 B4GT7_MOUSE Beta-1,4-galactosyltransferase 7 (Beta-1,4-GalTase 7) (Beta4Gal-T7) (b4Gal-T7) (EC 2.4.1.-) (Proteoglycan UDP-galactose:beta-xylose beta1,4-galactosyltransferase I) (UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 7) (UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 7) (UDP-galactose:beta-xylose beta-1,4-galactosyltransferase) (XGPT) (XGalT-1) (Xylosylprotein 4-beta-galactosyltransferase) (EC 2.4.1.133) (Xylosylprotein beta-1,4-galactosyltransferase) 327 37,754 Alternative sequence (1); Binding site (3); Chain (1); Glycosylation (1); Metal binding (2); Region (5); Topological domain (2); Transmembrane (1) TRANSMEM 31 51 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 30 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 52 327 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. FUNCTION: Required for the biosynthesis of the tetrasaccharide linkage region of proteoglycans, especially for small proteoglycans in skin fibroblasts. {ECO:0000250}. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Cis cisternae of Golgi stack. {ECO:0000250}. +Q8K211 COPT1_MOUSE High affinity copper uptake protein 1 (Copper transporter 1) (CTR1) (Solute carrier family 31 member 1) 196 21,961 Chain (1); Glycosylation (2); Modified residue (1); Sequence conflict (1); Topological domain (4); Transmembrane (3) TRANSMEM 75 95 Helical. {ECO:0000255}.; TRANSMEM 139 159 Helical. {ECO:0000255}.; TRANSMEM 163 183 Helical. {ECO:0000255}. TOPO_DOM 1 74 Extracellular. {ECO:0000255}.; TOPO_DOM 96 138 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 160 162 Extracellular. {ECO:0000255}.; TOPO_DOM 184 196 Cytoplasmic. {ECO:0000255}. FUNCTION: High-affinity, saturable copper transporter involved in dietary copper uptake. {ECO:0000269|PubMed:20699218}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20699218}; Multi-pass membrane protein {ECO:0000269|PubMed:20699218}. Note=Localizes to the apical membrane in intestinal epithelial cells. SUBUNIT: Homotrimer. {ECO:0000250}. +Q9JHH9 COPZ2_MOUSE Coatomer subunit zeta-2 (Zeta-2-coat protein) (Zeta-2 COP) 205 22,934 Chain (1) FUNCTION: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. The zeta subunit may be involved in regulating the coat assembly and, hence, the rate of biosynthetic protein transport due to its association-dissociation properties with the coatomer complex (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:17360540}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Golgi apparatus membrane {ECO:0000269|PubMed:17360540}; Peripheral membrane protein {ECO:0000269|PubMed:17360540}; Cytoplasmic side {ECO:0000269|PubMed:17360540}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. Shows a significant preference for ERGIC and cis-Golgi apparatus compared with trans-Golgi network. {ECO:0000250}. SUBUNIT: Oligomeric complex. +P97303 BACH2_MOUSE Transcription regulator protein BACH2 (BTB and CNC homolog 2) 839 91,836 Alternative sequence (1); Chain (1); Compositional bias (1); Cross-link (2); Disulfide bond (1); Domain (2); Modified residue (2); Motif (1); Region (2); Sequence conflict (4) FUNCTION: Transcriptional regulator that acts as repressor or activator (PubMed:8887638). Binds to Maf recognition elements (MARE) (PubMed:8887638). Plays an important role in coordinating transcription activation and repression by MAFK (PubMed:8887638). Induces apoptosis in response to oxidative stress through repression of the antiapoptotic factor HMOX1 (By similarity). Positively regulates the nuclear import of actin (PubMed:26021350). {ECO:0000250|UniProtKB:Q9BYV9, ECO:0000269|PubMed:26021350}. PTM: The reversible disulfide bond may provide a mechanism to regulate the activity in oxidative stress responses. {ECO:0000250|UniProtKB:Q9BYV9}.; PTM: Phosphorylation at Ser-520 downstream of the PI-3K pathway promotes nuclear export. {ECO:0000250|UniProtKB:Q9BYV9}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10809773}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:10809773}. Note=Nucleocytoplasmic shuttling is controlled by phosphorylation. {ECO:0000250|UniProtKB:Q9BYV9}. SUBUNIT: Homodimer; disulfide-linked (By similarity). Heterodimer of BACH2 and Maf-related transcription factors (PubMed:8887638). {ECO:0000250|UniProtKB:Q9BYV9, ECO:0000269|PubMed:8887638}. TISSUE SPECIFICITY: Detected in brain and spleen. {ECO:0000269|PubMed:8887638}. +O70479 BACD2_MOUSE BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 2 (BTB/POZ domain-containing protein TNFAIP1) (Tumor necrosis factor, alpha-induced protein 1, endothelial) 316 36,134 Chain (1); Domain (1); Modified residue (2); Sequence conflict (3) Protein modification; protein ubiquitination. FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex involved in regulation of cytoskeleton structure. The BCR(TNFAIP1) E3 ubiquitin ligase complex mediates the ubiquitination of RHOA, leading to its degradation by the proteasome, thereby regulating the actin cytoskeleton and cell migration. Its interaction with RHOB may regulate apoptosis. May enhance the PCNA-dependent DNA polymerase delta activity (By similarity). {ECO:0000250}. PTM: Phosphorylation at Ser-280 by CK2 facilitates the nucleus localization and increases interaction with PCNA. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Endosome {ECO:0000250}. Note=Colocalizes with RHOB in endosomes. {ECO:0000250}. SUBUNIT: Component of the BCR(TNFAIP1) E3 ubiquitin ligase complex, at least composed of CUL3, TNFAIP1/BACURD2 and RBX1. Interacts with RHOA; with a preference for RhoA-GDP. Interacts with RHOB. Interacts with PCNA. Interacts with CSNK2B (By similarity). {ECO:0000250}. +Q922M3 BACD3_MOUSE BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 3 (mBACURD3) (BTB/POZ domain-containing protein KCTD10) 315 35,701 Chain (1); Domain (1); Modified residue (2); Motif (1) Protein modification; protein ubiquitination. FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex. The BCR(BACURD3) E3 ubiquitin ligase complex mediates the ubiquitination of target proteins, leading to their degradation by the proteasome (By similarity). {ECO:0000250|UniProtKB:Q8WZ19}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H3F6}. SUBUNIT: Homotetramer; forms a two-fold symmetric tetramer in solution. Interacts with CUL3; interaction is direct and forms a 5:5 heterodecamer (By similarity). Component of the BCR(BACURD3) E3 ubiquitin ligase complex, at least composed of CUL3, KCTD10/BACURD3 and RBX1 (By similarity). Interacts with DNA polymerase delta subunit 2/POLD2 (By similarity). Interacts with PCNA (By similarity). Associated with the tectonic-like complex (also named B9 complex); however as Kctd10 has not been identified in all tectonic-like complexes purifications it is unclear whether it is really part of the complex (PubMed:22179047). {ECO:0000250|UniProtKB:Q7TPL3, ECO:0000250|UniProtKB:Q8WZ19, ECO:0000250|UniProtKB:Q9H3F6, ECO:0000269|PubMed:22179047}. +Q91V12 BACH_MOUSE Cytosolic acyl coenzyme A thioester hydrolase (EC 3.1.2.2) (Acyl-CoA thioesterase 7) (Brain acyl-CoA hydrolase) (BACH) (CTE-IIa) (CTE-II) (Long chain acyl-CoA thioester hydrolase) 381 42,537 Active site (2); Alternative sequence (3); Beta strand (12); Chain (1); Domain (2); Helix (7); Modified residue (3); Mutagenesis (2); Sequence conflict (1); Turn (2) FUNCTION: Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. May play an important physiological function in brain. May play a regulatory role by modulating the cellular levels of fatty acyl-CoA ligands for certain transcription factors as well as the substrates for fatty acid metabolizing enzymes, contributing to lipid homeostasis. Has broad specificity, active towards fatty acyl-CoAs with chain-lengths of C8-C18. Has a maximal activity toward palmitoyl-CoA. {ECO:0000269|PubMed:11834298}. SUBCELLULAR LOCATION: Isoform A: Cytoplasm.; SUBCELLULAR LOCATION: Isoform D: Cytoplasm. SUBUNIT: Homohexamer. {ECO:0000269|PubMed:17563367}. DOMAIN: Both HotDog ACOT-type hydrolase domains are required for efficient activity. TISSUE SPECIFICITY: Widely expressed with highest levels in brain. High levels also found in thymus, large intestine and testis. Negligible in muscle and adipose tissue. In the central and peripheral nervous systems, displays a predominantly neuronal localization with highest expression in cell bodies and neurites. {ECO:0000269|PubMed:11834298}. +Q66JT7 COQ2_MOUSE 4-hydroxybenzoate polyprenyltransferase, mitochondrial (4-HB polyprenyltransferase) (EC 2.5.1.39) (Para-hydroxybenzoate--polyprenyltransferase) (PHB:PPT) (PHB:polyprenyltransferase) 374 40,504 Chain (1); Erroneous termination (1); Region (1); Sequence conflict (2); Topological domain (9); Transit peptide (1); Transmembrane (8) TRANSMEM 84 104 Helical. {ECO:0000255|HAMAP-Rule:MF_03189}.; TRANSMEM 109 129 Helical. {ECO:0000255|HAMAP-Rule:MF_03189}.; TRANSMEM 149 169 Helical. {ECO:0000255|HAMAP-Rule:MF_03189}.; TRANSMEM 173 193 Helical. {ECO:0000255|HAMAP-Rule:MF_03189}.; TRANSMEM 201 221 Helical. {ECO:0000255|HAMAP-Rule:MF_03189}.; TRANSMEM 231 251 Helical. {ECO:0000255|HAMAP-Rule:MF_03189}.; TRANSMEM 278 298 Helical. {ECO:0000255|HAMAP-Rule:MF_03189}.; TRANSMEM 333 353 Helical. {ECO:0000255|HAMAP-Rule:MF_03189}. TOPO_DOM 35 83 Mitochondrial matrix. {ECO:0000250|UniProtKB:Q96H96}.; TOPO_DOM 105 108 Mitochondrial intermembrane. {ECO:0000250|UniProtKB:Q96H96}.; TOPO_DOM 130 148 Mitochondrial matrix. {ECO:0000250|UniProtKB:Q96H96}.; TOPO_DOM 170 172 Mitochondrial intermembrane. {ECO:0000250|UniProtKB:Q96H96}.; TOPO_DOM 194 200 Mitochondrial matrix. {ECO:0000250|UniProtKB:Q96H96}.; TOPO_DOM 222 230 Mitochondrial intermembrane. {ECO:0000250|UniProtKB:Q96H96}.; TOPO_DOM 252 277 Mitochondrial matrix. {ECO:0000250|UniProtKB:Q96H96}.; TOPO_DOM 299 332 Mitochondrial intermembrane. {ECO:0000250|UniProtKB:Q96H96}.; TOPO_DOM 354 374 Mitochondrial matrix. {ECO:0000250|UniProtKB:Q96H96}. Cofactor biosynthesis; ubiquinone biosynthesis. FUNCTION: Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of coenzyme Q (CoQ) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate. {ECO:0000255|HAMAP-Rule:MF_03189}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03189}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03189}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03189}. +Q61337 BAD_MOUSE Bcl2-associated agonist of cell death (BAD) (Bcl-2-binding component 6) (Bcl-xL/Bcl-2-associated death promoter) (Bcl2 antagonist of cell death) 204 22,080 Chain (1); Helix (2); Modified residue (10); Motif (1); Mutagenesis (6) FUNCTION: Promotes cell death. Successfully competes for the binding to Bcl-X(L), Bcl-2 and Bcl-W, thereby affecting the level of heterodimerization of these proteins with BAX. Can reverse the death repressor activity of Bcl-X(L), but not that of Bcl-2. Appears to act as a link between growth factor receptor signaling and the apoptotic pathways. PTM: Phosphorylated on one or more of Ser-112, Ser-136, Ser-155 and Ser-170 in response to survival stimuli, which blocks its pro-apoptotic activity. Phosphorylation on Ser-136 or Ser-112 promotes heterodimerization with 14-3-3 proteins. This interaction then facilitates the phosphorylation at Ser-155, a site within the BH3 motif, leading to the release of Bcl-X(L) and the promotion of cell survival. Ser-136 is the major site of AKT/PKB phosphorylation, Ser-155 the major site of protein kinase A (CAPK) phosphorylation. {ECO:0000269|PubMed:10611223, ECO:0000269|PubMed:10679322, ECO:0000269|PubMed:11278362, ECO:0000269|PubMed:11342610, ECO:0000269|PubMed:11493700, ECO:0000269|PubMed:11717309, ECO:0000269|PubMed:12954615, ECO:0000269|PubMed:15849194, ECO:0000269|PubMed:9381178}.; PTM: Methylation at Arg-131 and Arg-133 by PRMT1 inhibits Akt-mediated phosphorylation at Ser-136. {ECO:0000269|PubMed:10611223, ECO:0000269|PubMed:10679322, ECO:0000269|PubMed:11342610, ECO:0000269|PubMed:11493700, ECO:0000269|PubMed:9381178}. SUBCELLULAR LOCATION: Mitochondrion outer membrane. Cytoplasm {ECO:0000269|PubMed:21546903}. Note=Colocalizes with HIF3A isoform 2 in the cytoplasm (PubMed:21546903). Upon phosphorylation, locates to the cytoplasm. {ECO:0000269|PubMed:21546903}. SUBUNIT: Forms heterodimers with the anti-apoptotic proteins, Bcl-X(L), Bcl-2 and Bcl-W. Also binds protein S100A10 (By similarity). The Ser-112/Ser-136 phosphorylated form binds 14-3-3 proteins. Interacts with AKT1 and PIM3 (By similarity). Interacts (via BH3 domain) with NOL3 (via CARD domain); preventing the association of BAD with BCL2 (By similarity). Interacts with HIF3A isoform 2 (via C-terminus domain); the interaction reduces the binding between BAD and BAX (PubMed:21546903). {ECO:0000250|UniProtKB:O35147, ECO:0000269|PubMed:21546903}. DOMAIN: Intact BH3 motif is required by BIK, BID, BAK, BAD and BAX for their pro-apoptotic activity and for their interaction with anti-apoptotic members of the Bcl-2 family. +Q8CI61 BAG4_MOUSE BAG family molecular chaperone regulator 4 (BAG-4) (Bcl-2-associated athanogene 4) (Silencer of death domains) 457 49,095 Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (1); Modified residue (5); Mutagenesis (3) FUNCTION: Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release. Prevents constitutive TNFRSF1A signaling (By similarity). Negative regulator of PRKN translocation to damaged mitochondria (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Binds to the ATPase domain of HSP/HSC70 chaperones. Binds to the death domain of TNFRSF12 (By similarity). Binds to the death domain of TNFRSF1A in the absence of TNF and thereby prevents binding of adapter molecules such as TRADD or TRAF2. Interacts with PRKN (By similarity). {ECO:0000250}. +O54962 BAF_MOUSE Barrier-to-autointegration factor (Breakpoint cluster region protein 1) (LAP2-binding protein 1) [Cleaved into: Barrier-to-autointegration factor, N-terminally processed] 89 10,103 Chain (2); Domain (1); Initiator methionine (1); Modified residue (5) FUNCTION: Plays fundamental roles in nuclear assembly, chromatin organization, gene expression and gonad development. May potently compress chromatin structure and be involved in membrane recruitment and chromatin decondensation during nuclear assembly. Contains 2 non-specific dsDNA-binding sites which may promote DNA cross-bridging. {ECO:0000250|UniProtKB:O75531}. PTM: Ser-4 is the major site of phosphorylation as compared to Thr-2 and Thr-3. Phosphorylation on Thr-2; Thr-3 and Ser-4 disrupts its ability to bind DNA and reduces its ability to bind LEM domain-containing proteins. Non phosphorylated BAF seems to enhance binding between EMD and LMNA. Dephosphorylated by protein phosphatase 2A (PP2A) following interaction with ANKLE2/LEM4 during mitotic exit, leading to mitotic nuclear envelope reassembly. {ECO:0000250|UniProtKB:O75531}. SUBCELLULAR LOCATION: Barrier-to-autointegration factor, N-terminally processed: Nucleus {ECO:0000250|UniProtKB:O75531}. Cytoplasm {ECO:0000250|UniProtKB:O75531}. Chromosome {ECO:0000250|UniProtKB:O75531}. Nucleus envelope {ECO:0000250|UniProtKB:O75531}. Note=Significantly enriched at the nuclear inner membrane, diffusely throughout the nucleus during interphase and concentrated at the chromosomes during the M-phase. The phosphorylated form (by VRK1) shows a cytoplasmic localization whereas the unphosphorylated form locates almost exclusively in the nucleus. {ECO:0000250|UniProtKB:O75531}. SUBUNIT: Homodimer. Heterodimerizes with BAFL. Interacts with ANKLE2/LEM4, leading to decreased phosphorylation by VRK1 and promoting dephosphorylation by protein phosphatase 2A (PP2A). Binds non-specifically to double-stranded DNA, and is found as a hexamer or dodecamer upon DNA binding. Binds to LEM domain-containing nuclear proteins such as LEMD3/MAN1, TMPO/LAP2 and EMD (emerin). Interacts with ANKLE1 (via LEM domain); the interaction may favor BANF1 dimerization. Interacts with CRX and LMNA (lamin-A). Binds linker histone H1.1 and core histones H3. {ECO:0000250|UniProtKB:O75531}. DOMAIN: Has a helix-hairpin-helix (HhH) structural motif conserved among proteins that bind non-specifically to DNA. {ECO:0000250|UniProtKB:O75531}.; DOMAIN: LEM domain proteins bind centrally on the BAF dimer. {ECO:0000250|UniProtKB:O75531}. +Q91YN9 BAG2_MOUSE BAG family molecular chaperone regulator 2 (BAG-2) (Bcl-2-associated athanogene 2) 210 23,474 Chain (1); Coiled coil (1); Domain (1); Helix (3); Initiator methionine (1); Modified residue (4) FUNCTION: Co-chaperone for HSP70 and HSC70 chaperone proteins. Acts as a nucleotide-exchange factor (NEF) promoting the release of ADP from the HSP70 and HSC70 proteins thereby triggering client/substrate protein release. {ECO:0000250|UniProtKB:O95816}. SUBUNIT: Binds to the ATPase domain of HSP/HSC70 chaperones. May interact with NWD1. Interacts with HSPA1A (via NBD), HSPA1B (via NBD) and HSPA8. {ECO:0000250|UniProtKB:O95816}. +O08734 BAK_MOUSE Bcl-2 homologous antagonist/killer (Apoptosis regulator BAK) 209 23,295 Chain (1); Frameshift (1); Helix (3); Initiator methionine (1); Metal binding (2); Modified residue (1); Motif (3); Sequence conflict (4); Transmembrane (1) TRANSMEM 186 203 Helical. {ECO:0000255}. FUNCTION: In the presence of an appropriate stimulus, accelerates programmed cell death by binding to, and antagonizing the anti-apoptotic action of BCL2. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q16611}; Single-pass membrane protein {ECO:0000255}. SUBUNIT: Homodimer. Formation of the homodimer is zinc-dependent. Forms heterodimers with BCL2 and BCL2L1 isoform Bcl-X(L). Forms heterooligomers with BAX (By similarity). Interacts with BCL2A1 (PubMed:18462686). Interacts withRTL10/BOP (PubMed:18462686). Interacts with VDAC1 (By similarity). {ECO:0000250|UniProtKB:Q16611, ECO:0000269|PubMed:18462686}.; SUBUNIT: (Microbial infection) Interacts with gamma-herpesvirus 68 protein vBCL2. {ECO:0000269|PubMed:18248095}. DOMAIN: Intact BH3 motif is required by BIK, BID, BAK, BAD and BAX for their pro-apoptotic activity and for their interaction with anti-apoptotic members of the Bcl-2 family. {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed. +Q9DCT6 BAP18_MOUSE Chromatin complexes subunit BAP18 (BPTF-associated protein of 18 kDa) 171 17,996 Alternative sequence (2); Chain (1); Domain (1); Modified residue (1) FUNCTION: Component of chromatin complexes such as the MLL1/MLL and NURF complexes. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. SUBUNIT: Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Component of the nucleosome-remodeling factor (NURF) complex (By similarity). {ECO:0000250}. +O70445 BARD1_MOUSE BRCA1-associated RING domain protein 1 (BARD-1) (EC 2.3.2.27) (RING-type E3 ubiquitin transferase BARD1) 765 84,254 Chain (1); Compositional bias (1); Cross-link (2); Domain (2); Modified residue (2); Region (2); Repeat (4); Zinc finger (1) Protein modification; protein ubiquitination. FUNCTION: E3 ubiquitin-protein ligase. The BRCA1-BARD1 heterodimer specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability. Plays a central role in the control of the cell cycle in response to DNA damage. Acts by mediating ubiquitin E3 ligase activity that is required for its tumor suppressor function. Also forms a heterodimer with CSTF1/CSTF-50 to modulate mRNA processing and RNAP II stability by inhibiting pre-mRNA 3' cleavage. {ECO:0000250|UniProtKB:Q99728}. PTM: Processed during apoptosis. The homodimer is more susceptible to proteolytic cleavage than the BARD1/BRCA1 heterodimer. {ECO:0000250|UniProtKB:Q99728}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15077185}. Cytoplasm {ECO:0000269|PubMed:15077185}. Note=Can translocate to the cytoplasm. Localizes at sites of DNA damage at double-strand breaks (DSBs); recruitment to DNA damage sites is mediated by the BRCA1-A complex. {ECO:0000250|UniProtKB:Q99728}. SUBUNIT: Homo- and heterodimer. Heterodimer (RING-type zinc finger) with BRCA1. Heterodimer (via ANK repeats and BRCT domains) with CSTF1/CSTF-50. Component of the BRCA1-A complex, at least composed of the BRCA1, BARD1, UIMC1/RAP80, ABRAXAS1, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1. Interacts with UBXN1. {ECO:0000250|UniProtKB:Q99728}. +Q91VF6 COQA1_MOUSE Collagen alpha-1(XXVI) chain (Alpha-1 type XXVI collagen) (EMI domain-containing protein 2) (Emilin and multimerin domain-containing protein 2) (Emu2) 440 45,810 Alternative sequence (1); Chain (1); Disulfide bond (3); Domain (3); Glycosylation (2); Signal peptide (1) PTM: Hydroxylated on proline residues.; PTM: N-glycosylated. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SUBUNIT: Homotrimer or heterotrimer. TISSUE SPECIFICITY: Specifically expressed in the testis and ovary in adult tissues. {ECO:0000269|PubMed:12145293}. +Q8C0P5 COR2A_MOUSE Coronin-2A 524 59,573 Chain (1); Coiled coil (1); Repeat (5); Sequence conflict (1) SUBUNIT: Binds actin. Component of the N-Cor repressor complex, at least composed of NCOR1, NCOR2, HDAC3, TBL1X, TBL1R, CORO2A and GPS2. {ECO:0000250}. +Q07813 BAX_MOUSE Apoptosis regulator BAX 192 21,395 Chain (1); Helix (10); Modified residue (1); Motif (3); Transmembrane (1); Turn (2) TRANSMEM 172 192 Helical. {ECO:0000255}. FUNCTION: Accelerates programmed cell death by binding to, and antagonizing the apoptosis repressor BCL2 or its adenovirus homolog E1B 19k protein. Under stress conditions, undergoes a conformation change that causes translocation to the mitochondrion membrane, leading to the release of cytochrome c that then triggers apoptosis. Promotes activation of CASP3, and thereby apoptosis. BAX deficiency leads to lymphoid hyperplasia and male sterility, because of the cessation of sperm production. {ECO:0000269|PubMed:21060336, ECO:0000269|PubMed:8358790}. SUBCELLULAR LOCATION: Isoform Alpha: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q07812}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:Q07812}. Note=Colocalizes with 14-3-3 proteins in the cytoplasm. Under stress conditions, undergoes a conformation change that causes release from JNK-phosphorylated 14-3-3 proteins and translocation to the mitochondrion membrane (By similarity). {ECO:0000250|UniProtKB:Q07812}.; SUBCELLULAR LOCATION: Isoform Beta: Cytoplasm {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform Gamma: Cytoplasm {ECO:0000250}. SUBUNIT: Homodimer. Forms higher oligomers under stress conditions. Forms heterooligomers with BAK (By similarity). Interacts with BCL2L11. Interaction with BCL2L11 promotes BAX oligomerization and association with mitochondrial membranes, with subsequent release of cytochrome c (PubMed:21060336). Forms heterodimers with BCL2 (PubMed:8358790, PubMed:21060336). Forms heterodimers with BCL2L1 isoform Bcl-X(L), BCL2L2, MCL1 and A1. Interacts with SH3GLB1 and HN. Interacts with SFN and YWHAZ; the interaction occurs in the cytoplasm. Under stress conditions, JNK-mediated phosphorylation of SFN and YWHAZ, releases BAX to mitochondria. Interacts with RNF144B, which regulates the ubiquitin-dependent stability of BAX. Interacts with CLU under stress conditions that cause a conformation change leading to BAX oligomerization and association with mitochondria. Does not interact with CLU in unstressed cells (By similarity). Interacts with FAIM2/LFG2 (By similarity). Interacts with BOP (By similarity). Interacts (via a C-terminal 33 residues) with NOL3 (via CARD domain); inhibits BAX activation and translocationand consequently cytochrome c release from mitochondria (PubMed:15383280). {ECO:0000250|UniProtKB:Q07812, ECO:0000269|PubMed:15383280, ECO:0000269|PubMed:21060336, ECO:0000269|PubMed:8358790}.; SUBUNIT: (Microbial infection) Interacts with gamma-herpesvirus 68 protein vBCL2. {ECO:0000269|PubMed:18248095}. DOMAIN: Intact BH3 motif is required by BIK, BID, BAK, BAD and BAX for their pro-apoptotic activity and for their interaction with anti-apoptotic members of the Bcl-2 family. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in a wide variety of tissues. +Q91XV3 BASP1_MOUSE Brain acid soluble protein 1 (22 kDa neuronal tissue-enriched acidic protein) (Neuronal axonal membrane protein NAP-22) 226 22,087 Chain (1); Cross-link (3); Initiator methionine (1); Lipidation (1); Modified residue (12) SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. Cell projection, growth cone. Note=Associated with the membranes of growth cones that form the tips of elongating axons. +Q3V3N7 BBS1_MOUSE Bardet-Biedl syndrome 1 protein homolog 593 65,094 Chain (1); Initiator methionine (1); Modified residue (1); Mutagenesis (1) FUNCTION: The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor, which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane and binds to RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the Rab8-GTP localizes to the cilium and promotes docking and fusion of carrier vesicles to the base of the ciliary membrane. The BBSome complex, together with the LTZL1, controls SMO ciliary trafficking and contributes to the sonic hedgehog (SHH) pathway regulation. Required for proper BBSome complex assembly (By similarity). Plays a role in olfactory cilium biogenesis/maintenance and trafficking and is essential for the localization of the BBSome complex in the olfactory sensory neurons cilia (PubMed:15322545, PubMed:28237838). {ECO:0000250|UniProtKB:Q8NFJ9, ECO:0000269|PubMed:15322545, ECO:0000269|PubMed:28237838}. SUBCELLULAR LOCATION: Cell projection, cilium membrane {ECO:0000250|UniProtKB:Q8NFJ9}. Cytoplasm {ECO:0000250|UniProtKB:Q8NFJ9}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000250|UniProtKB:Q8NFJ9}. SUBUNIT: Part of BBSome complex, that contains BBS1, BBS2, BBS4, BBS5, BBS7, BBS8/TTC8, BBS9 and BBIP10. Interacts with the C-terminus of RAB3IP. Interacts with CCDC28B and ALDOB. Interacts with PKD1. {ECO:0000250|UniProtKB:Q8NFJ9}. +Q5SUD9 BBS12_MOUSE Bardet-Biedl syndrome 12 protein homolog 708 78,335 Chain (1); Erroneous initiation (2); Sequence conflict (5) FUNCTION: Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Involved in adipogenic differentiation. {ECO:0000250|UniProtKB:Q6ZW61}. SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000250|UniProtKB:Q6ZW61}. Note=Located within the basal body of the primary cilium of differentiating preadipocytes. {ECO:0000250|UniProtKB:Q6ZW61}. SUBUNIT: Component of the chaperonin-containing T-complex (TRiC), a heterooligomeric complex of about 850 to 900 kDa that forms two stacked rings, 12 to 16 nm in diameter. Interacts with MKKS. {ECO:0000250|UniProtKB:Q6ZW61}. +P56469 CORT_MOUSE Cortistatin [Cleaved into: Cortistatin-14] 109 11,613 Disulfide bond (1); Peptide (1); Propeptide (1); Sequence conflict (2); Signal peptide (1) SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Expressed in a subset of GABAergic cells in the cortex and hippocampus. +Q80YN3 BCAS1_MOUSE Breast carcinoma-amplified sequence 1 homolog (Novel amplified in breast cancer 1 homolog) 633 67,378 Chain (1); Modified residue (10); Region (1); Sequence conflict (5) FUNCTION: Required for myelination. {ECO:0000269|PubMed:28230289}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q3ZB98}. SUBUNIT: Homodimer. Interacts with DYNLL1 and DYNLL2. {ECO:0000250|UniProtKB:O75363, ECO:0000250|UniProtKB:Q3ZB98}. TISSUE SPECIFICITY: Highly expressed in the brain and, more specifically, in oligodendrocytes. Expressed in the Schwann cells (at protein level). {ECO:0000269|PubMed:28230289, ECO:0000269|PubMed:29212715}. +O35855 BCAT2_MOUSE Branched-chain-amino-acid aminotransferase, mitochondrial (BCAT(m)) (EC 2.6.1.42) 393 44,127 Chain (1); Modified residue (2); Sequence conflict (1); Transit peptide (1) FUNCTION: Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine. May also function as a transporter of branched chain alpha-keto acids. SUBCELLULAR LOCATION: Mitochondrion. SUBUNIT: Homodimer. {ECO:0000250}. +P43135 COT2_MOUSE COUP transcription factor 2 (COUP-TF2) (Apolipoprotein AI regulatory protein 1) (ARP-1) (COUP transcription factor II) (COUP-TF II) (Nuclear receptor subfamily 2 group F member 2) 414 45,571 Chain (1); Compositional bias (1); DNA binding (1); Domain (1); Modified residue (1); Mutagenesis (1); Region (2); Sequence conflict (1); Zinc finger (2) FUNCTION: Ligand-activated transcription factor. Activated by high concentrations of 9-cis-retinoic acid and all-trans-retinoic acid, but not by dexamethasone, cortisol or progesterone (in vitro). Regulation of the apolipoprotein A-I gene transcription. Binds to DNA site A (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus. SUBUNIT: Interacts with SQSTM1. Binds DNA as a dimer; homodimer or heterodimer with NR2F6. Interacts with NCOA1, NCOA2, NCOA3 and PPARGC1A (By similarity). Interacts with ZFPM2. {ECO:0000250, ECO:0000269|PubMed:11382775}. +Q8C1Z7 BBS4_MOUSE Bardet-Biedl syndrome 4 protein homolog 520 58,255 Chain (1); Region (3); Repeat (10); Sequence conflict (1) FUNCTION: The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor, which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane and binds to RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the Rab8-GTP localizes to the cilium and promotes docking and fusion of carrier vesicles to the base of the ciliary membrane. The BBSome complex, together with the LTZL1, controls SMO ciliary trafficking and contributes to the sonic hedgehog (SHH) pathway regulation. Required for proper BBSome complex assembly and its ciliary localization. Required for microtubule anchoring at the centrosome but not for microtubule nucleation. May be required for the dynein-mediated transport of pericentriolar proteins to the centrosome (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cell projection, cilium membrane {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000250}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:15107855, ECO:0000269|PubMed:22072986}. Cell projection, cilium {ECO:0000269|PubMed:23943788}. Note=Localizes to the pericentriolar material. Centrosomal localization requires dynein (By similarity). Localizes to the connecting cilium of photoreceptor cells (PubMed:23943788). SUBUNIT: Part of BBSome complex, that contains BBS1, BBS2, BBS4, BBS5, BBS7, BBS8/TTC8, BBS9 and BBIP10. Interacts with PCM1 and DCTN1. Interacts with DC28B. Interacts with ALDOB and C2CD3. Interacts with PKD1 (By similarity). Interacts with CEP290 (By similarity). {ECO:0000250|UniProtKB:Q96RK4, ECO:0000269|PubMed:22072986, ECO:0000269|PubMed:24469809}. TISSUE SPECIFICITY: Expressed in the hippocampus and dentate gyrus, the columnar epithelial cells of bronchioles, the olfactory epithelium and the inner segment and outer nuclear layer of the retina. Expressed in testis. {ECO:0000269|PubMed:15107855, ECO:0000269|PubMed:22072986}. +Q9Z0H7 BCL10_MOUSE B-cell lymphoma/leukemia 10 (B-cell CLL/lymphoma 10) (Bcl-10) (CARD-containing molecule enhancing NF-kappa-B) (CARD-like apoptotic protein) (mCLAP) (CED-3/ICH-1 prodomain homologous E10-like regulator) (mCIPER) (Cellular homolog of vCARMEN) (cCARMEN) (Cellular-E10) (c-E10) (Mammalian CARD-containing adapter molecule E10) (mE10) 233 25,948 Chain (1); Domain (1); Modified residue (2) FUNCTION: Involved in adaptive immune response. Promotes apoptosis, pro-caspase-9 maturation and activation of NF-kappa-B via NIK and IKK. May be an adapter protein between upstream TNFR1-TRADD-RIP complex and the downstream NIK-IKK-IKAP complex. Is a substrate for MALT1. {ECO:0000250|UniProtKB:O95999}. PTM: Phosphorylated by IKBKB/IKKB. {ECO:0000250|UniProtKB:O95999}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O95999}. Membrane raft {ECO:0000250|UniProtKB:O95999}. Note=Colocalized with DPP4 in membrane rafts. {ECO:0000250|UniProtKB:O95999}. SUBUNIT: Found in a membrane raft complex, at least composed of BCL10, CARD11, DPP4 and IKBKB. Self-associates by CARD-CARD interaction and interacts with other CARD-proteins such as CARD9, CARD10, CARD11 and CARD14. Forms a complex with CARD14 and MALT1; resulting in the formation of a CBM (CARD14-BCL10-MALT1) complex. Binds caspase-9 with its C-terminal domain. Interacts with TRAF2 and BIRC2/c-IAP2 (By similarity). Interacts with PELI2 and SOCS3; these interactions may be mutually exclusive (PubMed:15213237). Interacts with CARD11 and MALT1; as part of a CBM (CARD11-BCL10-MALT1) complex involved in NF-kappa-B activation (By similarity). {ECO:0000250|UniProtKB:O95999, ECO:0000269|PubMed:15213237}. TISSUE SPECIFICITY: Highly expressed in heart, brain, spleen, lung, liver, skeletal muscle, kidney and testis. Detected in developing brain, olfactory epithelium, tongue, whisker follicles, salivary gland, heart, lung, liver and intestinal epithelia of stage 15 embryos. +Q9CXE2 BCL7A_MOUSE B-cell CLL/lymphoma 7 protein family member A 210 22,781 Alternative sequence (2); Chain (1); Cross-link (1); Modified residue (2); Sequence conflict (2) +O08664 BCL7C_MOUSE B-cell CLL/lymphoma 7 protein family member C (B-cell chronic lymphocytic leukemia/lymphoma 7C protein) 217 23,445 Chain (1); Compositional bias (1); Modified residue (7) FUNCTION: May play an anti-apoptotic role. {ECO:0000269|PubMed:15270555}. +P21237 BDNF_MOUSE Brain-derived neurotrophic factor (BDNF) 249 28,123 Chain (1); Disulfide bond (3); Glycosylation (1); Mutagenesis (2); Propeptide (1); Signal peptide (1); Site (1) FUNCTION: During development, promotes the survival and differentiation of selected neuronal populations of the peripheral and central nervous systems. Participates in axonal growth, pathfinding and in the modulation of dendritic growth and morphology. Major regulator of synaptic transmission and plasticity at adult synapses in many regions of the CNS. PTM: Converted into mature BDNF by plasmin (PLG). SUBCELLULAR LOCATION: Secreted. SUBUNIT: Monomers and homodimers. Binds to NTRK2/TRKB. {ECO:0000269|PubMed:7957235}. +P00416 COX3_MOUSE Cytochrome c oxidase subunit 3 (Cytochrome c oxidase polypeptide III) 261 29,923 Chain (1); Erroneous termination (1); Sequence conflict (2); Transmembrane (7) TRANSMEM 15 35 Helical. {ECO:0000255}.; TRANSMEM 38 58 Helical. {ECO:0000255}.; TRANSMEM 81 101 Helical. {ECO:0000255}.; TRANSMEM 127 147 Helical. {ECO:0000255}.; TRANSMEM 162 182 Helical. {ECO:0000255}.; TRANSMEM 197 217 Helical. {ECO:0000255}.; TRANSMEM 239 259 Helical. {ECO:0000255}. FUNCTION: Subunits I, II and III form the functional core of the enzyme complex. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +P0DM65 BECN2_MOUSE Beclin-2 447 50,287 Chain (1); Coiled coil (1); Region (1) FUNCTION: Involved in 2 distinct lysosomal degradation pathways: acts as a regulator of autophagy and as a regulator of G-protein coupled receptors turnover. Regulates degradation in lysosomes of a variety of G-protein coupled receptors via its interaction with GPRASP1/GASP1. {ECO:0000269|PubMed:23954414}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. SUBUNIT: Homodimer (via coiled-coil domain) (By similarity). Interacts (via coiled-coil domain) with ATG14 (via coiled-coil domain); this interaction is tighter than BECN2 self-association (PubMed:23954414). Interacts with AMBRA1, UVRAG and PIK3C3/VPS34; these interactions are not disrupted by starvation (PubMed:23954414). Does not interact with RUBCN. Interacts (via N-terminus) with GPRASP1/GASP1; the interaction is direct (PubMed:23954414). {ECO:0000250|UniProtKB:A8MW95, ECO:0000269|PubMed:23954414}. TISSUE SPECIFICITY: Expressed in brain, skeletal muscle, placenta, thymus and uterus. Expressed at a lower level in liver, testis, stomach, and 17-day-old embryos. {ECO:0000269|PubMed:23954414}. +Q6PFX2 BEND6_MOUSE BEN domain-containing protein 6 281 31,270 Alternative sequence (3); Chain (1); Coiled coil (1); Domain (1) FUNCTION: Acts as a corepressor of recombining binding protein suppressor hairless (RBPJ) and inhibits Notch signaling in neural stem cells, thereby opposing their self-renewal and promoting neurogenesis (PubMed:23571214, PubMed:25561495). {ECO:0000269|PubMed:23571214, ECO:0000269|PubMed:25561495}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23571214}. SUBUNIT: Interacts (via BEN domain) with RBPJ. {ECO:0000250|UniProtKB:Q5SZJ8}. +Q6H1V1 BEST3_MOUSE Bestrophin-3 (Vitelliform macular dystrophy 2-like protein 3) 669 76,431 Chain (1); Intramembrane (1); Topological domain (6); Transmembrane (4) INTRAMEM 229 249 {ECO:0000255}. TRANSMEM 26 46 Helical. {ECO:0000255}.; TRANSMEM 71 91 Helical. {ECO:0000255}.; TRANSMEM 179 199 Helical. {ECO:0000255}.; TRANSMEM 271 291 Helical. {ECO:0000255}. TOPO_DOM 1 25 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 47 70 Extracellular. {ECO:0000255}.; TOPO_DOM 92 178 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 200 228 Extracellular. {ECO:0000255}.; TOPO_DOM 250 270 Extracellular. {ECO:0000255}.; TOPO_DOM 292 669 Cytoplasmic. {ECO:0000255}. FUNCTION: Forms calcium-sensitive chloride channels. Permeable to bicarbonate (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +O35623 BET1_MOUSE BET1 homolog (mBET1) (Golgi vesicular membrane-trafficking protein p18) 118 13,274 Chain (1); Domain (1); Modified residue (1); Topological domain (2); Transmembrane (1) TRANSMEM 95 115 Helical; Anchor for type IV membrane protein. {ECO:0000255}. TOPO_DOM 1 94 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 116 118 Vesicular. {ECO:0000255}. FUNCTION: Required for vesicular transport from the ER to the Golgi complex. Functions as a SNARE involved in the docking process of ER-derived vesicles with the cis-Golgi membrane (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Golgi apparatus, cis-Golgi network membrane {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}. Note=Concentrated most in the intermediate compartment/cis-Golgi network and the cis-Golgi cisternae 1 and 2. Greatly reduced in concentration at the trans end of the Golgi apparatus (By similarity). {ECO:0000250}. SUBUNIT: Interacts with STX17. {ECO:0000250}. +P12787 COX5A_MOUSE Cytochrome c oxidase subunit 5A, mitochondrial (Cytochrome c oxidase polypeptide Va) 146 16,101 Chain (1); Modified residue (3); Sequence conflict (1); Transit peptide (1) FUNCTION: This is the heme A-containing chain of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. SUBCELLULAR LOCATION: Mitochondrion inner membrane. SUBUNIT: Interacts with AFG1L. {ECO:0000250|UniProtKB:P20674}. +Q64445 COX8A_MOUSE Cytochrome c oxidase subunit 8A, mitochondrial (Cytochrome c oxidase polypeptide VIII-liver) (Cytochrome c oxidase subunit 8-2) 69 7,648 Chain (1); Topological domain (2); Transit peptide (1); Transmembrane (1) TRANSMEM 37 60 Helical. {ECO:0000250}. TOPO_DOM 26 36 Mitochondrial matrix. {ECO:0000250}.; TOPO_DOM 61 69 Mitochondrial intermembrane. {ECO:0000250}. FUNCTION: This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. SUBCELLULAR LOCATION: Mitochondrion inner membrane. +Q9CPZ8 COXM1_MOUSE COX assembly mitochondrial protein homolog (Cmc1p) 106 12,553 Chain (1); Disulfide bond (2); Domain (1); Erroneous initiation (1); Initiator methionine (1); Modified residue (1); Motif (2); Sequence conflict (1) FUNCTION: Component of the MITRAC (mitochondrial translation regulation assembly intermediate of cytochrome c oxidase complex) complex, that regulates cytochrome c oxidase assembly. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q7Z7K0}. Note=Colocalizes with MT-CO1. {ECO:0000250|UniProtKB:Q7Z7K0}. SUBUNIT: Component of the MITRAC (mitochondrial translation regulation assembly intermediate of cytochrome c oxidase complex) complex, the core components of this complex being COA3/MITRAC12 and COX14. {ECO:0000250|UniProtKB:Q7Z7K0}. +Q8K199 COXM2_MOUSE COX assembly mitochondrial protein 2 homolog 79 9,419 Chain (1); Disulfide bond (2); Domain (1); Motif (2) FUNCTION: May be involved in cytochrome c oxidase biogenesis. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. +Q9R224 BEX1_MOUSE Protein BEX1 (Brain-expressed X-linked protein 1 homolog) (Reduced expression protein 3) (REX-3) 128 15,119 Chain (1); Erroneous initiation (1); Modified residue (1); Sequence conflict (2) FUNCTION: Signaling adapter molecule involved in p75NTR/NGFR signaling. Plays a role in cell cycle progression and neuronal differentiation. Inhibits neuronal differentiation in response to nerve growth factor (NGF). May act as a link between the cell cycle and neurotrophic factor signaling, possibly by functioning as an upstream modulator of receptor signaling, coordinating biological responses to external signals with internal cellular states (By similarity). {ECO:0000250}. PTM: Phosphorylated. Phosphorylation of Ser-105 protects it from the proteasome (By similarity). {ECO:0000250}.; PTM: Ubiquitinated. Degraded by the proteasome (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12911636}. Cytoplasm {ECO:0000269|PubMed:12911636}. Note=Shuttles between the cytoplasm and the nucleus. SUBUNIT: Interacts with neurotrophin receptor p75NTR/NGFR (By similarity). Interacts with OMP. {ECO:0000250, ECO:0000269|PubMed:12054873, ECO:0000269|PubMed:12911636, ECO:0000269|PubMed:15198671}. TISSUE SPECIFICITY: Primarily localized to neuronal cells within several regions of the brain, including the olfactory epithelium, bulb, peri/paraventricular nuclei, suprachiasmatic nucleus, arcuate nucleus, median eminence, lateral hypothalamic area, thalamus, hippocampus and cerebellum (at protein level). Expressed in brain, mid term embryos and to a lesser extent in ovary. In testis, it is expressed in the pachytene spermatocytes and spermatids but not in spermatogonia. {ECO:0000269|PubMed:10072429, ECO:0000269|PubMed:11989783, ECO:0000269|PubMed:15861462, ECO:0000269|PubMed:9806360}. +Q3TZW7 BEX6_MOUSE Protein BEX6 (Brain-expressed X-linked protein 6 homolog) 114 13,353 Chain (1) PTM: Ubiquitinated (Probable). Degraded by the proteasome. {ECO:0000305}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15958283}. +Q8R079 BFAR_MOUSE Bifunctional apoptosis regulator 450 52,968 Alternative sequence (1); Chain (1); Domain (1); Glycosylation (2); Helix (8); Sequence conflict (1); Topological domain (5); Transmembrane (4); Turn (1); Zinc finger (1) TRANSMEM 141 161 Helical. {ECO:0000255}.; TRANSMEM 332 352 Helical. {ECO:0000255}.; TRANSMEM 361 381 Helical. {ECO:0000255}.; TRANSMEM 405 425 Helical. {ECO:0000255}. TOPO_DOM 1 140 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 162 331 Extracellular. {ECO:0000255}.; TOPO_DOM 353 360 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 382 404 Extracellular. {ECO:0000255}.; TOPO_DOM 426 450 Cytoplasmic. {ECO:0000255}. FUNCTION: Apoptosis regulator. Has anti-apoptotic activity, both for apoptosis triggered via death-receptors and via mitochondrial factors (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: Interacts with CASP8, BCL2 and BCL2L1 through SAM domain and also with HIP1, IFT57, ESRRBL1 and BCAP31. {ECO:0000250}. +P38649 BGAT_MOUSE Histo-blood group ABO system transferase (Cis-AB transferase) (Fucosylglycoprotein 3-alpha-galactosyltransferase) (Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase) (Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase) (EC 2.4.1.40) (Glycoprotein-fucosylgalactoside alpha-galactosyltransferase) (EC 2.4.1.37) (Histo-blood group A transferase) (A transferase) (Histo-blood group B transferase) (B transferase) (NAGAT) 332 38,777 Active site (1); Binding site (5); Chain (1); Erroneous gene model prediction (1); Glycosylation (1); Metal binding (2); Region (2); Sequence conflict (3); Topological domain (2); Transmembrane (1) TRANSMEM 14 34 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 13 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 35 332 Lumenal. {ECO:0000255}. Protein modification; protein glycosylation. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. Secreted. Note=Membrane-bound form in trans cisternae of Golgi. Secreted into the body fluid (By similarity). {ECO:0000250}. DOMAIN: The conserved DXD motif is involved in cofactor binding. The manganese ion interacts with the beta-phosphate group of UDP and may also have a role in catalysis. TISSUE SPECIFICITY: Submaxillary glands (at protein level). {ECO:0000269|PubMed:11278752}. +Q9DBJ3 BI2L1_MOUSE Brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 1 (BAI1-associated protein 2-like protein 1) (Insulin receptor tyrosine kinase substrate) 514 57,188 Beta strand (5); Chain (1); Coiled coil (1); Domain (2); Helix (1); Modified residue (9); Region (1); Turn (1) FUNCTION: May function as adapter protein. Involved in the formation of clusters of actin bundles. Plays a role in the reorganization of the actin cytoskeleton in response to bacterial infection (By similarity). {ECO:0000250}. PTM: Phosphorylated on tyrosine in response to insulin. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Note=Recruited to actin pedestals that are formed upon infection by bacteria at bacterial attachment sites. {ECO:0000250}. SUBUNIT: Interacts with RAC1. Binds to F-actin. Interacts with FASLG (By similarity). {ECO:0000250}. DOMAIN: The IMD domain is predicted to have a helical structure. It may induce actin bundling and filopodia formation (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Detected in bladder, liver, testes, heart, lung, spleen, brain and skeletal muscle (at protein level). {ECO:0000269|PubMed:17430976}. +Q91W64 CP270_MOUSE Cytochrome P450 2C70 (EC 1.14.14.1) (CYPIIC70) 489 56,020 Chain (1); Erroneous initiation (1); Metal binding (1); Sequence conflict (3) FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. {ECO:0000250|UniProtKB:P19225}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. +Q3UGY8 BIG3_MOUSE Brefeldin A-inhibited guanine nucleotide-exchange protein 3 (ARFGEF family member 3) 2170 240,091 Chain (1); Domain (1); Modified residue (12); Transmembrane (1) TRANSMEM 1488 1508 Helical. {ECO:0000255}. FUNCTION: Participates in the regulation of systemic glucose homeostasis, where it negatively regulates insulin granule biogenesis in pancreatic islet beta cells (PubMed:24711543). Also regulates glucagon granule production in pancreatic alpha cells (PubMed:25737957). Inhibits nuclear translocation of the transcriptional coregulator PHB2 and may enhance estrogen receptor alpha (ESR1) transcriptional activity in breast cancer cells (By similarity). {ECO:0000250|UniProtKB:Q5TH69, ECO:0000269|PubMed:24711543, ECO:0000269|PubMed:25737957}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:24711543}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000305|PubMed:24711543}; Single-pass membrane protein {ECO:0000305}. SUBUNIT: Interacts with PHB2 (By similarity). {ECO:0000250|UniProtKB:Q5TH69}. TISSUE SPECIFICITY: Expressed in pancreatic islet (insulin granules of islet alpha and beta cells) and brain (at protein level). {ECO:0000269|PubMed:24711543, ECO:0000269|PubMed:25737957}. +Q5RJB0 BHA09_MOUSE Class A basic helix-loop-helix protein 9 (bHLHa9) (Class B basic helix-loop-helix factor 42) (bHLHf42) 231 25,115 Chain (1); Domain (1); Erroneous initiation (2); Sequence conflict (1) FUNCTION: Transcription factor, which play a role in limb development. Is an essential player in the regulatory network governing transcription of genes implicated in limb morphogenesis. {ECO:0000250|UniProtKB:Q7RTU4}. SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}. SUBUNIT: Heterodimer. Efficient DNA binding requires dimerization with another bHLH protein. Interacts with TCF3, TCF4, and TCF12. {ECO:0000250|UniProtKB:Q7RTU4}. +P15392 CP2A4_MOUSE Cytochrome P450 2A4 (EC 1.14.14.1) (CYPIIA4) (Cytochrome P450-15-alpha) (Cytochrome P450-IIA3.1) (Testosterone 15-alpha-hydroxylase) 494 56,782 Chain (1); Metal binding (1); Modified residue (2); Sequence conflict (16) FUNCTION: Highly active in the 15-alpha-hydroxylation of testosterone. Also active in the 15-alpha-hydroxylation of progesterone and androstenedione. Little or no activity on corticosterone, pregnenolone, dehydroepiandrosterone, estradiol or estriol. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. TISSUE SPECIFICITY: Kidney and lung. Expressed in liver, with a strong circadian rhythmicity. Circadian expression is regulated by DBP. {ECO:0000269|PubMed:10490589}. +F8VPZ9 BICRA_MOUSE BRD4-interacting chromatin-remodeling complex-associated protein (Glioma tumor suppressor candidate region gene 1 protein) 1578 161,354 Chain (1); Cross-link (1); Modified residue (4) FUNCTION: Component of SWI/SNF chromatin remodeling subcomplex GBAF that carries out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner (PubMed:29374058). May play a role in BRD4-mediated gene transcription (By similarity). {ECO:0000250|UniProtKB:Q9NZM4, ECO:0000269|PubMed:29374058}. SUBUNIT: Component of the multiprotein chromatin-remodeling complexes SWI/SNF: SWI/SNF-A (BAF), SWI/SNF-B (PBAF) and related complexes. The canonical complex contains a catalytic subunit (either SMARCA4/BRG1/BAF190A or SMARCA2/BRM/BAF190B) and at least SMARCE1, ACTL6A/BAF53, SMARCC1/BAF155, SMARCC2/BAF170, and SMARCB1/SNF5/BAF47. Other subunits specific to each of the complexes may also be present permitting several possible combinations developmentally and tissue specific. Component of the SWI/SNF (GBAF) subcomplex, which includes at least BICRA or BICRAL (mutually exclusive), BRD9, SS18, the core BAF subunits, SMARCA2/BRM, SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, SMARCC1/BAF155, and SMARCD1/BAF60A (PubMed:29374058). Interacts with BRD4; the interaction bridges BRD4 to the GBAF complex (By similarity). {ECO:0000250|UniProtKB:Q9NZM4, ECO:0000269|PubMed:29374058}. +O55071 CP2BJ_MOUSE Cytochrome P450 2B19 (EC 1.14.14.1) (CYPIIB19) 492 55,997 Chain (1); Metal binding (1); Modified residue (1) FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. TISSUE SPECIFICITY: Expressed only in differentiated keratinocytes in skin. +Q811D2 ANR26_MOUSE Ankyrin repeat domain-containing protein 26 1581 180,647 Chain (1); Coiled coil (4); Modified residue (4); Natural variant (5); Repeat (5); Sequence conflict (5) FUNCTION: Acts as a regulator of adipogenesis. Involved in the regulation of the feeding behavior. {ECO:0000269|PubMed:22666460, ECO:0000269|PubMed:24633808}. SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:18162531}. Note=Located just near the plasma membrane in close association with filamentous actin. {ECO:0000269|PubMed:18162531}. SUBUNIT: Interacts with TRIO. Interacts with GPS2. Interacts with CCDC85B. Interacts with HMMR. {ECO:0000250|UniProtKB:Q9UPS8}. TISSUE SPECIFICITY: Widely expressed (PubMed:18162531). Expressed in the arcuate and ventromedial nuclei within the hypothalamus and in the ependyma and the circumventricular organs (at protein level) (PubMed:18162531). {ECO:0000269|PubMed:18162531, ECO:0000269|PubMed:24633808}. +Q8C5H1 ANO4_MOUSE Anoctamin-4 (Transmembrane protein 16D) 955 111,544 Alternative sequence (4); Chain (1); Compositional bias (1); Glycosylation (3); Sequence conflict (1); Topological domain (9); Transmembrane (8) TRANSMEM 353 373 Helical. {ECO:0000255}.; TRANSMEM 425 445 Helical. {ECO:0000255}.; TRANSMEM 506 526 Helical. {ECO:0000255}.; TRANSMEM 548 568 Helical. {ECO:0000255}.; TRANSMEM 596 616 Helical. {ECO:0000255}.; TRANSMEM 716 736 Helical. {ECO:0000255}.; TRANSMEM 769 789 Helical. {ECO:0000255}.; TRANSMEM 886 906 Helical. {ECO:0000255}. TOPO_DOM 1 352 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 374 424 Extracellular. {ECO:0000255}.; TOPO_DOM 446 505 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 527 547 Extracellular. {ECO:0000255}.; TOPO_DOM 569 595 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 617 715 Extracellular. {ECO:0000255}.; TOPO_DOM 737 768 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 790 885 Extracellular. {ECO:0000255}.; TOPO_DOM 907 955 Cytoplasmic. {ECO:0000255}. FUNCTION: Has calcium-dependent phospholipid scramblase activity; scrambles phosphatidylserine, phosphatidylcholine and galactosylceramide. Does not exhibit calcium-activated chloride channel (CaCC) activity. {ECO:0000269|PubMed:23532839}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q32M45}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q32M45}. Note=Shows an intracellular localization according to PubMed:22075693. {ECO:0000269|PubMed:22075693}. TISSUE SPECIFICITY: Predominantly expressed in neuronal tissues. Expressed at low levels in ovary, uterus, heart and brain. {ECO:0000269|PubMed:20056604, ECO:0000269|PubMed:23532839}. +Q61315 APC_MOUSE Adenomatous polyposis coli protein (Protein APC) (mAPC) 2845 311,089 Alternative sequence (2); Chain (1); Coiled coil (2); Compositional bias (4); Initiator methionine (1); Modified residue (42); Motif (2); Natural variant (9); Region (1); Repeat (7) FUNCTION: Tumor suppressor. Promotes rapid degradation of CTNNB1 and participates in Wnt signaling as a negative regulator. APC activity is correlated with its phosphorylation state. Activates the GEF activity of SPATA13 and ARHGEF4. Plays a role in hepatocyte growth factor (HGF)-induced cell migration (By similarity). Required for MMP9 up-regulation via the JNK signaling pathway in colorectal tumor cells. Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. It is required for the localization of MACF1 to the cell membrane and this localization of MACF1 is critical for its function in microtubule stabilization (By similarity). {ECO:0000250|UniProtKB:P25054, ECO:0000269|PubMed:19893577}. PTM: Phosphorylated by GSK3B. {ECO:0000250}.; PTM: Ubiquitinated, leading to its degradation by the proteasome. Ubiquitination is facilitated by Axin. Deubiquitinated by ZRANB1/TRABID (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, adherens junction {ECO:0000250|UniProtKB:P25054}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P25054}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:P25054}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:P25054}. Cytoplasm {ECO:0000250|UniProtKB:P25054}. Cell membrane {ECO:0000250|UniProtKB:P25054}. Note=Associated with the microtubule network at the growing distal tip of microtubules. Accumulates in the lamellipodium and ruffle membrane in response to hepatocyte growth factor (HGF) treatment. The MEMO1-RHOA-DIAPH1 signaling pathway controls localization of the phosphorylated form to the cell membrane. {ECO:0000250|UniProtKB:P25054}. SUBUNIT: Forms homooligomers and heterooligomers with APC2. Interacts with PDZ domains of DLG1 and DLG3. Associates with catenins. Binds axin. Interacts with MAPRE2 and MAPRE3 (via C-terminus). Found in a complex consisting of ARHGEF4, APC and CTNNB1. Interacts with ARHGEF4 (via N-terminus) (By similarity). Interacts with MAPRE1 (via C-terminus); probably required for APC targeting to the growing microtubule plus ends (PubMed:15311282). Interacts with DIAPH1 and DIAPH2 (PubMed:15311282). Interacts with SCRIB; may mediate targeting to adherens junctions of epithelial cells (PubMed:16611247). Interacts with SPATA13 (via N-terminus and SH3 domain). Interacts with ASAP1 (via SH3 domain) (By similarity). Found in a complex composed of MACF1, APC, AXIN1, CTNNB1 and GSK3B. Interacts at the cell membrane with AMER1 and AMER2 (via ARM repeats) (By similarity). Interacts with KHDRBS1 (By similarity). The complex composed, at least, of APC, CTNNB1 and GSK3B interacts with JPT1; the interaction requires the inactive form of GSK3B (phosphorylated at 'Ser-9') (By similarity). {ECO:0000250|UniProtKB:P25054, ECO:0000269|PubMed:15311282, ECO:0000269|PubMed:16611247}. DOMAIN: The microtubule tip localization signal (MtLS) motif; mediates interaction with MAPRE1 and targeting to the growing microtubule plus ends. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in liver, spleen, kidney, heart, lung, brain, stomach, intestine, testis and ovary. +Q9D2X0 ANR39_MOUSE Ankyrin repeat domain-containing protein 39 183 19,639 Chain (1); Modified residue (1); Repeat (4) +P17427 AP2A2_MOUSE AP-2 complex subunit alpha-2 (100 kDa coated vesicle protein C) (Adaptor protein complex AP-2 subunit alpha-2) (Adaptor-related protein complex 2 subunit alpha-2) (Alpha-adaptin C) (Alpha2-adaptin) (Clathrin assembly protein complex 2 alpha-C large chain) (Plasma membrane adaptor HA2/AP2 adaptin alpha C subunit) 938 104,017 Beta strand (24); Binding site (5); Chain (1); Helix (46); Mutagenesis (19); Region (1); Sequence conflict (3); Turn (9) FUNCTION: Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. The AP-2 alpha subunit binds polyphosphoinositide-containing lipids, positioning AP-2 on the membrane. The AP-2 alpha subunit acts via its C-terminal appendage domain as a scaffolding platform for endocytic accessory proteins. The AP-2 alpha and AP-2 sigma subunits are thought to contribute to the recognition of the [ED]-X-X-X-L-[LI] motif. {ECO:0000269|PubMed:10459011, ECO:0000269|PubMed:14745134, ECO:0000269|PubMed:15473838}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14530274, ECO:0000269|PubMed:17035303}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Membrane, coated pit {ECO:0000269|PubMed:17035303}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=AP-2 appears to be excluded from internalizing CCVs and to disengage from sites of endocytosis seconds before internalization of the nascent CCV. {ECO:0000269|PubMed:17035303}. SUBUNIT: Adaptor protein complex 2 (AP-2) is a heterotetramer composed of two large adaptins (alpha-type subunit AP2A1 or AP2A2 and beta-type subunit AP2B1), a medium adaptin (mu-type subunit AP2M1) and a small adaptin (sigma-type subunit AP2S1). Binds EPN1, EPS15, AMPH, SNAP91 and BIN1. Interacts with HIP1 (By similarity). Interacts with DGKD isoform 2. Interacts with DENND1A, DENND1B and DENND1C. Interacts with FCHO1 and DAB2. Interacts with ATAT1; this interaction is required for efficient alpha-tubulin acetylation by ATAT1. Interacts with KIAA1107 (PubMed:29262337). {ECO:0000250, ECO:0000269|PubMed:10380931, ECO:0000269|PubMed:10430869, ECO:0000269|PubMed:10459011, ECO:0000269|PubMed:11247302, ECO:0000269|PubMed:12057195, ECO:0000269|PubMed:12086608, ECO:0000269|PubMed:17880279, ECO:0000269|PubMed:19140243, ECO:0000269|PubMed:20154091, ECO:0000269|PubMed:22484487, ECO:0000269|PubMed:24097348, ECO:0000269|PubMed:29262337}. +P56402 AQP2_MOUSE Aquaporin-2 (AQP-2) (ADH water channel) (Aquaporin-CD) (AQP-CD) (Collecting duct water channel protein) (WCH-CD) (Water channel protein for renal collecting duct) 271 28,965 Chain (1); Glycosylation (1); Modified residue (2); Motif (2); Sequence conflict (3); Topological domain (7); Transmembrane (6) TRANSMEM 17 34 Helical. {ECO:0000255}.; TRANSMEM 41 59 Helical. {ECO:0000255}.; TRANSMEM 86 107 Helical. {ECO:0000255}.; TRANSMEM 128 148 Helical. {ECO:0000255}.; TRANSMEM 157 176 Helical. {ECO:0000255}.; TRANSMEM 203 224 Helical. {ECO:0000255}. TOPO_DOM 1 16 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 35 40 Extracellular. {ECO:0000255}.; TOPO_DOM 60 85 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 108 127 Extracellular. {ECO:0000255}.; TOPO_DOM 149 156 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 177 202 Extracellular. {ECO:0000255}.; TOPO_DOM 225 271 Cytoplasmic. {ECO:0000255}. FUNCTION: Forms a water-specific channel that provides the plasma membranes of renal collecting duct with high permeability to water, thereby permitting water to move in the direction of an osmotic gradient. {ECO:0000250}. PTM: Ser-256 phosphorylation is necessary and sufficient for expression at the apical membrane. Endocytosis is not phosphorylation-dependent (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Basolateral cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Shuttles from vesicles to the apical membrane. Vasopressin-regulated phosphorylation is required for translocation to the apical cell membrane. PLEKHA8/FAPP2 is required to transport AQP2 from the TGN to sites where AQP2 is phosphorylated (By similarity). {ECO:0000250}. DOMAIN: Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA). TISSUE SPECIFICITY: Expressed in kidney. Expressed in a radial pattern from the cortex through the outer medulla into the inner medulla. Higher levels in the inner medulla. Located in tubules suggestive of collecting ducts. {ECO:0000269|PubMed:10191086, ECO:0000269|PubMed:12426236}. +P08030 APT_MOUSE Adenine phosphoribosyltransferase (APRT) (EC 2.4.2.7) 180 19,724 Chain (1); Initiator methionine (1); Modified residue (7); Sequence conflict (7) Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. FUNCTION: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Homodimer. +Q8R1T1 CHMP7_MOUSE Charged multivesicular body protein 7 (Chromatin-modifying protein 7) 451 50,633 Alternative sequence (2); Chain (1); Coiled coil (1); Modified residue (5) FUNCTION: ESCRT-III-like protein required to recruit the ESCRT-III complex to the nuclear envelope during late anaphase. Together with SPAST, the ESCRT-III complex promotes nuclear envelope sealing and mitotic spindle disassembly during late anaphase. Plays a role in the endosomal sorting pathway. {ECO:0000250|UniProtKB:Q8WUX9}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8WUX9}. Nucleus envelope {ECO:0000250|UniProtKB:Q8WUX9}. Note=Diffused localization, with some punctate distribution, especially in the perinuclear area. Localizes to the nucleus envelope during late anaphase. {ECO:0000250|UniProtKB:Q8WUX9}. SUBUNIT: Interacts with CHMP4B, but not with VPS25. {ECO:0000250|UniProtKB:Q8WUX9}. +Q9JKL5 CHP3_MOUSE Calcineurin B homologous protein 3 (Tescalcin) (TE-1) (TSC) 214 24,600 Calcium binding (1); Chain (1); Domain (1); Initiator methionine (1); Lipidation (1); Mutagenesis (1); Sequence conflict (2) FUNCTION: Functions as an integral cofactor in cell pH regulation by controlling plasma membrane-type Na(+)/H(+) exchange activity. Promotes the maturation, transport, cell surface stability and exchange activity of SLC9A1/NHE1 at the plasma membrane. Promotes the induction of hematopoietic stem cell differentiation toward megakaryocytic lineage. Essential for the coupling of ERK cascade activation with the expression of ETS family genes in megakaryocytic differentiation. Also involved in granulocytic differentiation in a ERK-dependent manner. Inhibits the phosphatase activity of calcineurin. {ECO:0000269|PubMed:14661968}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14661968}. Cytoplasm {ECO:0000269|PubMed:14661968}. Membrane {ECO:0000250|UniProtKB:Q96BS2}; Lipid-anchor {ECO:0000250|UniProtKB:Q96BS2}. Cell membrane {ECO:0000250|UniProtKB:Q96BS2}. Cell projection, lamellipodium {ECO:0000269|PubMed:14661968}. Cell projection, ruffle membrane {ECO:0000269|PubMed:14661968}. Note=Colocalizes with SLC9A1 at the cell membrane. {ECO:0000250|UniProtKB:Q96BS2}. SUBUNIT: Interacts with SLC9A1/NHE1 (via juxtamembrane region of the cytoplasmic C-terminus); the interaction enable an optimal Na(+)/H(+) exchange activity (By similarity). Monomer. Homodimer; disulfide-linked. {ECO:0000250}. DOMAIN: Binds calcium via its EF-hands. Calcium-binding mediates a conformational change. Can also bind magnesium. TISSUE SPECIFICITY: Expressed in embryonic, newborn and adult testis, but not in prepubertal testis. Expressed in the embryonic testis during testis determination but is not expressed at any time in the embryonic ovary. In embryonic testis, expression is restricted to the testis cords and is seen in both Sertoli cells and germ cells. Expression is excluded from the myoid cells which surround the cords. Expressed in the embryonic adrenal after the initial stages of differentiation. Expressed at a lower level in the embryonic brain, heart and lung but not in liver or gut. May be expressed at a very low level in the embryonic kidney. In the embryonic brain, expressed in the nasal placode and in fibers extending from the olfactory epithelium to the primordial olfactory bulb. In adults, expressed in the heart, and weakly in the brain and kidney. Highly expressed in terminally differentiated megakaryocytes (at protein level). Not detected in fetal liver cells (at protein level). {ECO:0000269|PubMed:11145610, ECO:0000269|PubMed:14661968, ECO:0000269|PubMed:17717601, ECO:0000269|PubMed:19345287}. +Q9QZB7 ARP10_MOUSE Actin-related protein 10 (Actin-related protein 11) 417 46,208 Chain (1); Sequence conflict (1) SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. +Q9D864 ARP6_MOUSE Actin-related protein 6 (mArp6) 396 45,785 Chain (1); Initiator methionine (1); Modified residue (2); Sequence conflict (2) SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Nucleus {ECO:0000250}. Note=Colocalizes with HP1 family proteins at pericentric heterochromatin. {ECO:0000250}. SUBUNIT: Interacts with CBX1, CBX3 and CBX5. {ECO:0000250}. +Q9D0A3 ARPIN_MOUSE Arpin (Arp2/3 inhibition protein) 226 25,193 Chain (1); Region (1); Sequence conflict (2) FUNCTION: Regulates actin polymerization by inhibiting the actin-nucleating activity of the Arp2/3 complex; the function is competetive with nucleation promoting factors. Participates in an incoherent feedforward loop at the lamellipodium tip where it inhibits the ARP2/2 complex in response to Rac signaling and where Rac also stimulates actin polymerization through the WAVE complex. Involved in steering cell migration by controlling its directional persistence (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell projection, lamellipodium {ECO:0000269|PubMed:24132237}. Note=Colocalized with the WAVE complex at lamellipodium tip. SUBUNIT: Associates with the Arp2/3 complex. Interacts with ARPC2; enhanced by activated RAC1. Interacts with ARPC5; the interaction is dependent on RAC1. {ECO:0000269|PubMed:24132237}. DOMAIN: The acidic C-terminus is necessary and sufficient to inhibit ARP2/3 complex activity. {ECO:0000250}. +P50428 ARSA_MOUSE Arylsulfatase A (ASA) (EC 3.1.6.8) (Cerebroside-sulfatase) 506 53,748 Active site (2); Binding site (4); Chain (1); Disulfide bond (6); Glycosylation (3); Metal binding (5); Modified residue (1); Sequence conflict (4); Signal peptide (1) FUNCTION: Hydrolyzes cerebroside sulfate. {ECO:0000250|UniProtKB:P15289}. PTM: The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity. This post-translational modification is severely defective in multiple sulfatase deficiency (MSD). {ECO:0000250|UniProtKB:P15289}. SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:P15289}. Lysosome {ECO:0000250|UniProtKB:P15289}. SUBUNIT: Homodimer at neutral pH and homooctamer at acidic pH. Exists both as a single chain of 58 kDa (component A) or as a chain of 50 kDa (component B) linked by disulfide bond(s) to a 7 kDa chain (component C). Interacts with SUMF1 (By similarity). {ECO:0000250|UniProtKB:P15289}. +Q9Z0E2 CHRD_MOUSE Chordin 948 101,513 Chain (1); Domain (8); Glycosylation (3); Signal peptide (1) FUNCTION: Dorsalizing factor. Key developmental protein that dorsalizes early vertebrate embryonic tissues by binding to ventralizing TGF-beta family bone morphogenetic proteins (BMPs) and sequestering them in latent complexes. PTM: Cleaved by tolloid proteases; cleavage participates in dorsoventral patterning during early development. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. SUBUNIT: Interacts with TWSG1 and/or BMP4. {ECO:0000269|PubMed:11260715}. +Q8BM89 ARSJ_MOUSE Arylsulfatase J (ASJ) (EC 3.1.6.-) 598 67,354 Active site (2); Binding site (3); Chain (1); Glycosylation (7); Metal binding (5); Modified residue (1); Signal peptide (1) PTM: The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity. {ECO:0000250}. SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q6PIE5 AT1A2_MOUSE Sodium/potassium-transporting ATPase subunit alpha-2 (Na(+)/K(+) ATPase alpha-2 subunit) (EC 3.6.3.9) (Na(+)/K(+) ATPase alpha(+) subunit) (Sodium pump subunit alpha-2) 1020 112,217 Active site (1); Chain (1); Metal binding (2); Modified residue (10); Propeptide (1); Region (1); Topological domain (11); Transmembrane (10) TRANSMEM 86 106 Helical. {ECO:0000255}.; TRANSMEM 130 150 Helical. {ECO:0000255}.; TRANSMEM 287 306 Helical. {ECO:0000255}.; TRANSMEM 319 336 Helical. {ECO:0000255}.; TRANSMEM 770 789 Helical. {ECO:0000255}.; TRANSMEM 800 820 Helical. {ECO:0000255}.; TRANSMEM 841 863 Helical. {ECO:0000255}.; TRANSMEM 916 935 Helical. {ECO:0000255}.; TRANSMEM 949 967 Helical. {ECO:0000255}.; TRANSMEM 983 1003 Helical. {ECO:0000255}. TOPO_DOM 6 85 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 107 129 Extracellular. {ECO:0000255}.; TOPO_DOM 151 286 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 307 318 Extracellular. {ECO:0000255}.; TOPO_DOM 337 769 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 790 799 Extracellular. {ECO:0000255}.; TOPO_DOM 821 840 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 864 915 Extracellular. {ECO:0000255}.; TOPO_DOM 936 948 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 968 982 Extracellular. {ECO:0000255}.; TOPO_DOM 1004 1020 Cytoplasmic. {ECO:0000255}. FUNCTION: This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: The sodium/potassium-transporting ATPase is composed of a catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an additional regulatory subunit. Interacts with regulatory subunit FXYD1. {ECO:0000250|UniProtKB:A2VDL6}. +Q9EPE9 AT131_MOUSE Manganese-transporting ATPase 13A1 (CATP) (EC 3.6.3.-) 1200 132,388 Active site (1); Chain (1); Glycosylation (2); Metal binding (2); Modified residue (2); Sequence conflict (1); Topological domain (11); Transmembrane (10) TRANSMEM 64 84 Helical. {ECO:0000255}.; TRANSMEM 93 113 Helical. {ECO:0000255}.; TRANSMEM 241 261 Helical. {ECO:0000255}.; TRANSMEM 441 461 Helical. {ECO:0000255}.; TRANSMEM 986 1006 Helical. {ECO:0000255}.; TRANSMEM 1008 1028 Helical. {ECO:0000255}.; TRANSMEM 1048 1068 Helical. {ECO:0000255}.; TRANSMEM 1093 1113 Helical. {ECO:0000255}.; TRANSMEM 1129 1149 Helical. {ECO:0000255}.; TRANSMEM 1163 1183 Helical. {ECO:0000255}. TOPO_DOM 1 63 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 85 92 Extracellular. {ECO:0000255}.; TOPO_DOM 114 240 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 262 440 Extracellular. {ECO:0000255}.; TOPO_DOM 462 985 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1007 1007 Extracellular. {ECO:0000255}.; TOPO_DOM 1029 1047 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1069 1092 Extracellular. {ECO:0000255}.; TOPO_DOM 1114 1128 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1150 1162 Extracellular. {ECO:0000255}.; TOPO_DOM 1184 1200 Cytoplasmic. {ECO:0000255}. FUNCTION: Mediates manganese transport into the endoplasmic reticulum. The ATPase activity is required for cellular manganese homeostasis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q9CTG6 AT132_MOUSE Cation-transporting ATPase 13A2 (EC 3.6.3.-) 1169 126,443 Active site (1); Chain (1); Metal binding (2); Sequence conflict (8); Topological domain (13); Transmembrane (12) TRANSMEM 13 34 Helical. {ECO:0000255}.; TRANSMEM 46 66 Helical. {ECO:0000255}.; TRANSMEM 226 248 Helical. {ECO:0000255}.; TRANSMEM 252 271 Helical. {ECO:0000255}.; TRANSMEM 421 440 Helical. {ECO:0000255}.; TRANSMEM 455 475 Helical. {ECO:0000255}.; TRANSMEM 922 941 Helical. {ECO:0000255}.; TRANSMEM 953 970 Helical. {ECO:0000255}.; TRANSMEM 987 1007 Helical. {ECO:0000255}.; TRANSMEM 1036 1055 Helical. {ECO:0000255}.; TRANSMEM 1069 1086 Helical. {ECO:0000255}.; TRANSMEM 1103 1123 Helical. {ECO:0000255}. TOPO_DOM 1 12 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 35 45 Extracellular. {ECO:0000255}.; TOPO_DOM 67 225 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 249 251 Extracellular. {ECO:0000255}.; TOPO_DOM 272 420 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 441 454 Extracellular. {ECO:0000255}.; TOPO_DOM 476 921 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 942 952 Extracellular. {ECO:0000255}.; TOPO_DOM 971 986 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1008 1035 Extracellular. {ECO:0000255}.; TOPO_DOM 1056 1068 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1087 1102 Extracellular. {ECO:0000255}.; TOPO_DOM 1124 1169 Cytoplasmic. {ECO:0000255}. FUNCTION: ATPase that plays a role in intracellular cation homeostasis and the maintenance of neuronal integrity. Required for a proper lysosomal and mitochondrial maintenance. {ECO:0000250|UniProtKB:Q9NQ11}. PTM: Autophosphorylated. {ECO:0000250|UniProtKB:Q9NQ11}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Lysosome {ECO:0000250|UniProtKB:Q9NQ11}. Lysosome membrane {ECO:0000250|UniProtKB:Q9NQ11}. +Q9WV27 AT1A4_MOUSE Sodium/potassium-transporting ATPase subunit alpha-4 (Na(+)/K(+) ATPase alpha-4 subunit) (EC 3.6.3.9) (Sodium pump subunit alpha-4) 1032 114,887 Active site (1); Chain (1); Metal binding (2); Modified residue (1); Region (1); Sequence conflict (3); Topological domain (11); Transmembrane (10) TRANSMEM 97 117 Helical. {ECO:0000255}.; TRANSMEM 142 162 Helical. {ECO:0000255}.; TRANSMEM 299 318 Helical. {ECO:0000255}.; TRANSMEM 331 348 Helical. {ECO:0000255}.; TRANSMEM 782 801 Helical. {ECO:0000255}.; TRANSMEM 812 832 Helical. {ECO:0000255}.; TRANSMEM 853 875 Helical. {ECO:0000255}.; TRANSMEM 928 947 Helical. {ECO:0000255}.; TRANSMEM 961 979 Helical. {ECO:0000255}.; TRANSMEM 995 1015 Helical. {ECO:0000255}. TOPO_DOM 1 96 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 118 141 Extracellular. {ECO:0000255}.; TOPO_DOM 163 298 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 319 330 Extracellular. {ECO:0000255}.; TOPO_DOM 349 781 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 802 811 Extracellular. {ECO:0000255}.; TOPO_DOM 833 852 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 876 927 Extracellular. {ECO:0000255}.; TOPO_DOM 948 960 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 980 994 Extracellular. {ECO:0000255}.; TOPO_DOM 1016 1032 Cytoplasmic. {ECO:0000255}. FUNCTION: This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients. Plays a role in sperm motility (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBUNIT: The sodium/potassium-transporting ATPase is composed of a catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an additional regulatory subunit. {ECO:0000305}. TISSUE SPECIFICITY: Expressed at high levels in the testis and at low levels in the epididymis. +G5E829 AT2B1_MOUSE Plasma membrane calcium-transporting ATPase 1 (PMCA1) (EC 3.6.3.8) (Plasma membrane calcium ATPase isoform 1) (Plasma membrane calcium pump isoform 1) 1220 134,747 Active site (1); Chain (1); Initiator methionine (1); Metal binding (2); Modified residue (10); Region (1); Topological domain (11); Transmembrane (10) TRANSMEM 109 129 Helical. {ECO:0000255}.; TRANSMEM 152 172 Helical. {ECO:0000255}.; TRANSMEM 379 399 Helical. {ECO:0000255}.; TRANSMEM 419 439 Helical. {ECO:0000255}.; TRANSMEM 856 876 Helical. {ECO:0000255}.; TRANSMEM 884 904 Helical. {ECO:0000255}.; TRANSMEM 931 951 Helical. {ECO:0000255}.; TRANSMEM 970 989 Helical. {ECO:0000255}.; TRANSMEM 1007 1027 Helical. {ECO:0000255}.; TRANSMEM 1041 1061 Helical. {ECO:0000255}. TOPO_DOM 2 108 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 130 151 Extracellular. {ECO:0000255}.; TOPO_DOM 173 378 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 400 418 Extracellular. {ECO:0000255}.; TOPO_DOM 440 855 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 877 883 Extracellular. {ECO:0000255}.; TOPO_DOM 905 930 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 952 969 Extracellular. {ECO:0000255}.; TOPO_DOM 990 1006 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1028 1040 Extracellular. {ECO:0000255}.; TOPO_DOM 1062 1220 Cytoplasmic. {ECO:0000255}. FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium. Involved in bone homeostasis. Has a role in osteoclastogenesis where it regulates RANKL-induced calcium oscillation, a key step in the differentiation process. Also promotes survival of mature osteoclasts, probably by preventing toxic accumulation of intracellular calcium. {ECO:0000255|RuleBase:RU361146, ECO:0000269|PubMed:23266958}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Cell junction, synapse {ECO:0000269|PubMed:12209837}. Note=Colocalizes with SV2A in photoreceptor synaptic terminals. {ECO:0000269|PubMed:12209837}. SUBUNIT: Interacts with PDZD11. Interacts with SLC35G1 and STIM1. {ECO:0000250|UniProtKB:P20020}. TISSUE SPECIFICITY: Expressed in the retina, with strongest expression in the outer plexiform layer and lower expression levels in the inner nuclear layer and the inner plexiform layer (PubMed:12209837). Specifically expressed in the following retinal cell types: photoreceptor cells, cone bipolar cells and horizontal cells (PubMed:12209837). Expressed in osteoclasts (at protein level) (PubMed:23266958). Expressed at highest levels in brain, intestine, kidney, and stomach, and at lower levels in liver, lung, aorta, portal vein, urinary bladder, diaphragm, seminal vesicles and testes (PubMed:15178683). {ECO:0000269|PubMed:12209837, ECO:0000269|PubMed:15178683, ECO:0000269|PubMed:23266958}. +Q6Q477 AT2B4_MOUSE Plasma membrane calcium-transporting ATPase 4 (PMCA4) (EC 3.6.3.8) 1205 133,069 Active site (1); Alternative sequence (2); Chain (1); Metal binding (2); Modified residue (7); Region (2); Topological domain (11); Transmembrane (10) TRANSMEM 101 121 Helical. {ECO:0000255}.; TRANSMEM 148 168 Helical. {ECO:0000255}.; TRANSMEM 370 390 Helical. {ECO:0000255}.; TRANSMEM 410 430 Helical. {ECO:0000255}.; TRANSMEM 845 865 Helical. {ECO:0000255}.; TRANSMEM 873 893 Helical. {ECO:0000255}.; TRANSMEM 920 942 Helical. {ECO:0000255}.; TRANSMEM 957 979 Helical. {ECO:0000255}.; TRANSMEM 996 1016 Helical. {ECO:0000255}.; TRANSMEM 1030 1050 Helical. {ECO:0000255}. TOPO_DOM 1 100 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 122 147 Extracellular. {ECO:0000305}.; TOPO_DOM 169 369 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 391 409 Extracellular. {ECO:0000305}.; TOPO_DOM 431 844 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 866 872 Extracellular. {ECO:0000305}.; TOPO_DOM 894 919 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 943 956 Extracellular. {ECO:0000305}.; TOPO_DOM 980 995 Cytoplasmic. {ECO:0000305}.; TOPO_DOM 1017 1029 Extracellular. {ECO:0000305}.; TOPO_DOM 1051 1205 Cytoplasmic. {ECO:0000305}. FUNCTION: Calcium/calmodulin-regulated and magnesium-dependent enzyme that catalyzes the hydrolysis of ATP coupled with the transport of calcium out of the cell (By similarity). By regulating sperm cell calcium homeostasis, may play a role in sperm motility (PubMed:15078889). {ECO:0000250|UniProtKB:P23634, ECO:0000269|PubMed:15078889}. SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P23634}; Multi-pass membrane protein {ECO:0000255}. Cell projection, cilium, flagellum membrane {ECO:0000269|PubMed:15078889}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Interacts with PDZD11. Interacts with SLC35G1 and STIM1. Interacts with calmodulin. {ECO:0000250|UniProtKB:P23634}. TISSUE SPECIFICITY: Specifically expressed by sperm in testis (at protein level). {ECO:0000269|PubMed:15078889}. +P56384 AT5G3_MOUSE ATP synthase F(0) complex subunit C3, mitochondrial (ATP synthase lipid-binding protein) (ATP synthase membrane subunit c locus 3) (ATP synthase proteolipid P3) (ATPase protein 9) (ATPase subunit c) 141 14,745 Chain (1); Site (1); Transit peptide (1); Transmembrane (2) TRANSMEM 82 102 Helical. {ECO:0000255}.; TRANSMEM 117 137 Helical. {ECO:0000255}. FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. A homomeric c-ring of probably 10 subunits is part of the complex rotary element. SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. DISEASE: Note=This protein is the major protein stored in the storage bodies of animals or humans affected with ceroid lipofuscinosis (Batten disease). +A7L9Z8 AT2C2_MOUSE Calcium-transporting ATPase type 2C member 2 (ATPase 2C2) (EC 3.6.3.8) (Secretory pathway Ca(2+)-ATPase 2) 944 102,528 Active site (1); Chain (1); Compositional bias (1); Metal binding (8); Modified residue (2); Topological domain (11); Transmembrane (10) TRANSMEM 105 125 Helical; Name=1. {ECO:0000255}.; TRANSMEM 128 148 Helical; Name=2. {ECO:0000255}.; TRANSMEM 230 250 Helical; Name=3. {ECO:0000255}.; TRANSMEM 292 312 Helical; Name=4. {ECO:0000255}.; TRANSMEM 330 350 Helical; Name=5. {ECO:0000255}.; TRANSMEM 749 769 Helical; Name=6. {ECO:0000255}.; TRANSMEM 803 823 Helical; Name=7. {ECO:0000255}.; TRANSMEM 836 853 Helical; Name=8. {ECO:0000255}.; TRANSMEM 873 893 Helical; Name=9. {ECO:0000255}.; TRANSMEM 904 924 Helical; Name=10. {ECO:0000255}. TOPO_DOM 1 104 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 126 127 Extracellular. {ECO:0000255}.; TOPO_DOM 149 229 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 251 291 Extracellular. {ECO:0000255}.; TOPO_DOM 313 329 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 351 748 Extracellular. {ECO:0000255}.; TOPO_DOM 770 802 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 824 835 Extracellular. {ECO:0000255}.; TOPO_DOM 854 872 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 894 903 Extracellular. {ECO:0000255}.; TOPO_DOM 925 944 Cytoplasmic. {ECO:0000255}. FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. +O55143 AT2A2_MOUSE Sarcoplasmic/endoplasmic reticulum calcium ATPase 2 (SERCA2) (SR Ca(2+)-ATPase 2) (EC 3.6.3.8) (Calcium pump 2) (Calcium-transporting ATPase sarcoplasmic reticulum type, slow twitch skeletal muscle isoform) (Endoplasmic reticulum class 1/2 Ca(2+) ATPase) 1044 114,858 Active site (1); Alternative sequence (1); Chain (1); Metal binding (13); Modified residue (8); Region (4); Topological domain (11); Transmembrane (10) TRANSMEM 49 69 Helical; Name=1. {ECO:0000250}.; TRANSMEM 90 110 Helical; Name=2. {ECO:0000250}.; TRANSMEM 254 273 Helical; Name=3. {ECO:0000250}.; TRANSMEM 296 313 Helical; Name=4. {ECO:0000250}.; TRANSMEM 757 776 Helical; Name=5. {ECO:0000250}.; TRANSMEM 787 807 Helical; Name=6. {ECO:0000250}.; TRANSMEM 828 850 Helical; Name=7. {ECO:0000250}.; TRANSMEM 897 916 Helical; Name=8. {ECO:0000250}.; TRANSMEM 930 948 Helical; Name=9. {ECO:0000250}.; TRANSMEM 964 984 Helical; Name=10. {ECO:0000250}. TOPO_DOM 1 48 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 70 89 Lumenal. {ECO:0000250}.; TOPO_DOM 111 253 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 274 295 Lumenal. {ECO:0000250}.; TOPO_DOM 314 756 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 777 786 Lumenal. {ECO:0000250}.; TOPO_DOM 808 827 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 851 896 Lumenal. {ECO:0000250}.; TOPO_DOM 917 929 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 949 963 Lumenal. {ECO:0000250}.; TOPO_DOM 985 1044 Cytoplasmic. {ECO:0000250}. FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Isoform SERCA2A is involved in the regulation of the contraction/relaxation cycle. Acts as a regulator of TNFSF11-mediated Ca(2+) signaling pathways via its interaction with TMEM64 which is critical for the TNFSF11-induced CREB1 activation and mitochondrial ROS generation necessary for proper osteoclast generation. Association between TMEM64 and SERCA2 in the ER leads to cytosolic Ca (2+) spiking for activation of NFATC1 and production of mitochondrial ROS, thereby triggering Ca (2+) signaling cascades that promote osteoclast differentiation and activation (PubMed:23395171). {ECO:0000269|PubMed:22355118, ECO:0000269|PubMed:22971924, ECO:0000269|PubMed:23395171}. PTM: Nitrated under oxidative stress. Nitration on the two tyrosine residues inhibits catalytic activity. {ECO:0000250|UniProtKB:P16615}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23395171}; Multi-pass membrane protein {ECO:0000255}. Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:22355118}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Interacts with sarcolipin (SLN) (By similarity). Interacts with phospholamban (PLN) (PubMed:22971924). Interacts with myoregulin (MRLN) (By similarity). Interacts with DWORF (By similarity). Isoform 1 interacts with TRAM2 (via C-terminus) (PubMed:14749390). Interacts with HAX1. Interacts with S100A8 and S100A9 (PubMed:18403730). Interacts with SLC35G1 and STIM1. Interacts with TMEM203 (By similarity). Interacts with TMEM64 and PDIA3 (PubMed:23395171). {ECO:0000250|UniProtKB:P04191, ECO:0000250|UniProtKB:P16615, ECO:0000250|UniProtKB:Q8R429, ECO:0000269|PubMed:14749390, ECO:0000269|PubMed:18403730, ECO:0000269|PubMed:22971924, ECO:0000269|PubMed:23395171}. TISSUE SPECIFICITY: Isoform 2 is highly expressed in heart and slow twitch skeletal muscle. Isoform 2 is widely expressed. +Q64518 AT2A3_MOUSE Sarcoplasmic/endoplasmic reticulum calcium ATPase 3 (SERCA3) (SR Ca(2+)-ATPase 3) (EC 3.6.3.8) (Calcium pump 3) 1038 113,638 Active site (1); Alternative sequence (2); Binding site (1); Chain (1); Metal binding (13); Modified residue (6); Region (2); Sequence conflict (2); Topological domain (11); Transmembrane (10) TRANSMEM 49 69 Helical; Name=1. {ECO:0000250}.; TRANSMEM 90 110 Helical; Name=2. {ECO:0000250}.; TRANSMEM 254 273 Helical; Name=3. {ECO:0000250}.; TRANSMEM 296 313 Helical; Name=4. {ECO:0000250}.; TRANSMEM 758 777 Helical; Name=5. {ECO:0000250}.; TRANSMEM 788 808 Helical; Name=6. {ECO:0000250}.; TRANSMEM 829 851 Helical; Name=7. {ECO:0000250}.; TRANSMEM 898 917 Helical; Name=8. {ECO:0000250}.; TRANSMEM 931 949 Helical; Name=9. {ECO:0000250}.; TRANSMEM 965 985 Helical; Name=10. {ECO:0000250}. TOPO_DOM 1 48 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 70 89 Lumenal. {ECO:0000250}.; TOPO_DOM 111 253 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 274 295 Lumenal. {ECO:0000250}.; TOPO_DOM 314 757 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 778 787 Lumenal. {ECO:0000250}.; TOPO_DOM 809 828 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 852 897 Lumenal. {ECO:0000250}.; TOPO_DOM 918 930 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 950 964 Lumenal. {ECO:0000250}.; TOPO_DOM 986 1038 Cytoplasmic. {ECO:0000250}. FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium. Transports calcium ions from the cytosol into the sarcoplasmic/endoplasmic reticulum lumen. Contributes to calcium sequestration involved in muscular excitation/contraction. {ECO:0000250|UniProtKB:Q93084}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q93084}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q93084}. Sarcoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q93084}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q93084}. SUBUNIT: Interacts with sarcolipin (SLN) (By similarity). Interacts with phospholamban (PLN) (By similarity). Interacts with myoregulin (MRLN). Interacts with DWORF (By similarity). {ECO:0000250|UniProtKB:P04191, ECO:0000250|UniProtKB:Q8R429}. +Q6UQ17 AT8B3_MOUSE Phospholipid-transporting ATPase IK (EC 7.6.2.1) (ATPase, class I, type 8B, member 3) (Sperm aminophospholipid transporter) (SAPLT) 1335 151,955 Active site (1); Chain (1); Metal binding (2); Topological domain (10); Transmembrane (9) TRANSMEM 75 95 Helical. {ECO:0000255}.; TRANSMEM 296 316 Helical. {ECO:0000255}.; TRANSMEM 340 360 Helical. {ECO:0000255}.; TRANSMEM 918 938 Helical. {ECO:0000255}.; TRANSMEM 947 967 Helical. {ECO:0000255}.; TRANSMEM 996 1016 Helical. {ECO:0000255}.; TRANSMEM 1034 1054 Helical. {ECO:0000255}.; TRANSMEM 1056 1076 Helical. {ECO:0000255}.; TRANSMEM 1105 1125 Helical. {ECO:0000255}. TOPO_DOM 1 74 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 96 295 Exoplasmic loop. {ECO:0000255}.; TOPO_DOM 317 339 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 361 917 Exoplasmic loop. {ECO:0000255}.; TOPO_DOM 939 946 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 968 995 Exoplasmic loop. {ECO:0000255}.; TOPO_DOM 1017 1033 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1055 1055 Exoplasmic loop. {ECO:0000255}.; TOPO_DOM 1077 1104 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1126 1335 Exoplasmic loop. {ECO:0000255}. FUNCTION: P4-ATPase flippase which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. May be responsible for the maintenance of asymmetric distribution of phosphatidylserine (PS) in spermatozoa membranes. Involved in acrosome reactions and binding of spermatozoa to zona pellucida. {ECO:0000269|PubMed:14975727}. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome membrane {ECO:0000269|PubMed:14975727, ECO:0000269|PubMed:19017724}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O60423}; Multi-pass membrane protein {ECO:0000255}. TISSUE SPECIFICITY: Expressed in testis, specifically in spermatids within seminiferous tubules (at protein level). {ECO:0000269|PubMed:14975727, ECO:0000269|PubMed:19017724}. +P56383 AT5G2_MOUSE ATP synthase F(0) complex subunit C2, mitochondrial (ATP synthase lipid-binding protein) (ATP synthase membrane subunit c locus 2) (ATP synthase proteolipid P2) (ATPase protein 9) (ATPase subunit c) 146 15,476 Chain (1); Site (1); Transit peptide (1); Transmembrane (2) TRANSMEM 87 107 Helical. {ECO:0000255}.; TRANSMEM 122 142 Helical. {ECO:0000255}. FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. A homomeric c-ring of probably 10 subunits is part of the complex rotary element. SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane protein. SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Interacts with DNAJC30; interaction is direct. {ECO:0000250|UniProtKB:Q06055}. DISEASE: Note=This protein is the major protein stored in the storage bodies of animals or humans affected with ceroid lipofuscinosis (Batten disease). +Q8C9S8 ATG4A_MOUSE Cysteine protease ATG4A (EC 3.4.22.-) (AUT-like 2 cysteine endopeptidase) (Autophagin-2) (Autophagy-related cysteine endopeptidase 2) (Autophagy-related protein 4 homolog A) 396 45,095 Active site (3); Chain (1); Sequence conflict (4) FUNCTION: Cysteine protease required for the cytoplasm to vacuole transport (Cvt) and autophagy. Cleaves the C-terminal amino acid of ATG8 family proteins to reveal a C-terminal glycine. Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy. Preferred substrate is GABARAPL2 followed by MAP1LC3A and GABARAP. Has also an activity of delipidating enzyme for the PE-conjugated forms (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. +Q9CPX6 ATG3_MOUSE Ubiquitin-like-conjugating enzyme ATG3 (EC 2.3.2.-) (Autophagy-related protein 3) (APG3-like) 314 35,796 Active site (1); Chain (1); Cross-link (1); Modified residue (1); Mutagenesis (6); Site (1) FUNCTION: E2 conjugating enzyme required for the cytoplasm to vacuole transport (Cvt), autophagy, and mitochondrial homeostasis. Responsible for the E2-like covalent binding of phosphatidylethanolamine to the C-terminal Gly of ATG8-like proteins (GABARAP, GABARAPL1, GABARAPL2 or MAP1LC3A). The ATG12-ATG5 conjugate plays a role of an E3 and promotes the transfer of ATG8-like proteins from ATG3 to phosphatidylethanolamine (PE). This step is required for the membrane association of ATG8-like proteins. The formation of the ATG8-phosphatidylethanolamine conjugates is essential for autophagy and for the cytoplasm to vacuole transport (Cvt). Preferred substrate is MAP1LC3A. Also acts as an autocatalytic E2-like enzyme, catalyzing the conjugation of ATG12 to itself, ATG12 conjugation to ATG3 playing a role in mitochondrial homeostasis but not in autophagy. ATG7 (E1-like enzyme) facilitates this reaction by forming an E1-E2 complex with ATG3. ATG12-ATG3 conjugate is also formed upon viccina virus infection, leading to the disruption the cellular autophagy which is not necessary for vaccinia survival and proliferation. Promotes primary ciliogenesis by removing OFD1 from centriolar satellites via the autophagic pathway. {ECO:0000269|PubMed:11825910, ECO:0000269|PubMed:18768753, ECO:0000269|PubMed:20723759, ECO:0000269|PubMed:24089205}. PTM: Conjugated to ATG12 at Lys-243. ATG12-conjugation plays a role in regulation of mitochondrial homeostasis and cell death, while it is not involved in PE-conjugation to ATG8-like proteins and autophagy.; PTM: Cleaved by CASP8 upon death ligand binding such as tumor necrosis factor-alpha. CASP8 cleavage blocks survival-related autophagy and favors apoptosis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. SUBUNIT: Interacts with ATG7 and ATG12. The complex composed of ATG3 and ATG7 plays a role in the conjugation of ATG12 to ATG5. Interacts with FNBP1L (By similarity). {ECO:0000250}. +Q3KNL4 CJ053_MOUSE UPF0728 protein C10orf53 homolog 93 10,386 Chain (1) +Q80Y39 CJ062_MOUSE Uncharacterized protein C10orf62 homolog 304 34,025 Chain (1); Compositional bias (1); Modified residue (2) +Q9CQT6 CJ082_MOUSE Uncharacterized protein C10orf82 homolog 229 25,817 Chain (1); Erroneous initiation (3) +D2J0Y4 CJ090_MOUSE (E2-independent) E3 ubiquitin-conjugating enzyme FATS (EC 2.3.2.-) (Centrosomal protein C10orf90 homolog) (E2/E3 hybrid ubiquitin-protein ligase FATS) (Fragile-site associated tumor suppressor homolog) (FATS) 644 71,521 Chain (1); Coiled coil (1); Compositional bias (1); Mutagenesis (4); Region (3) FUNCTION: Tumor suppressor that is required to sustain G2/M checkpoint after DNA damage (PubMed:20843368, PubMed:20154723, PubMed:24240685). Acts as a p53/TP53 activator by inhibiting MDM2 binding to p53/TP53 and stimulating non-proteolytic polyubiquitination of p53/TP53. Exhibits ubiquitin ligase (E3) activity and assemble ubiquitin polymers through 'Lys-11'- (K11-), 'Lys-29'- (K29-) and 'Lys-63'- (K63)-linkages, independently of the ubiquitin-conjugating enzyme (E2). Promotes p53/TP53-dependent transcription of CDKN1A/p21, leading to robust checkpoint response (PubMed:24240685). Mediates CDKN1A/p21 protein stability in a ubiquitin-independent manner. Interacts with HDAC1 and prevents binding of HDAC1 to CDKN1A/p21 and facilitates the acetylation and stabilization of CDKN1A/p21 (PubMed:20154723). May have a role in the assembly of primary cilia (By similarity). {ECO:0000250|UniProtKB:Q96M02, ECO:0000269|PubMed:20154723, ECO:0000269|PubMed:20843368, ECO:0000269|PubMed:24240685}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96M02}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q96M02}. Note=Localizes to the actin cytoskeleton in a proportion of cells. Colocalizes with centriolar acetylated tubulin (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q96M02}. SUBUNIT: Interacts with HDAC1; the interaction prevents binding of HDAC1 to CDKN1A/p21 and facilitates the acetylation and stabilization of CDKN1A/p21 (PubMed:20154723). Interacts with p53/TP53; the interaction inhibits binding of p53/TP53 and MDM2 (PubMed:24240685). {ECO:0000269|PubMed:20154723, ECO:0000269|PubMed:24240685}. TISSUE SPECIFICITY: Highly expressed in testis. Weak expression found in brain, lung, heart, ovary, thymus, spleen and kidney. {ECO:0000269|PubMed:20843368}. +Q9CX25 CJ143_MOUSE Uncharacterized protein C10orf143 homolog 107 11,786 Chain (1) +Q9JJR6 CK016_MOUSE Uncharacterized protein C11orf16 homolog 402 44,484 Chain (1); Erroneous gene model prediction (1) +Q9D8N1 CK024_MOUSE Uncharacterized protein C11orf24 homolog 392 41,095 Chain (1); Glycosylation (2); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 343 363 Helical. {ECO:0000255}. TOPO_DOM 24 342 Extracellular. {ECO:0000255}.; TOPO_DOM 364 392 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Cycles to the plasma membrane via endosomes in a pH sensitive manner. Associated with Rab6-positive vesicles (By similarity). {ECO:0000250}. +Q9D8L0 CK052_MOUSE Uncharacterized protein C11orf52 homolog 127 14,283 Alternative sequence (1); Chain (1); Modified residue (2) +Q9D8Q6 CK053_MOUSE Uncharacterized protein C11orf53 homolog 235 25,445 Chain (1); Compositional bias (1) +Q8VD62 CK068_MOUSE UPF0696 protein C11orf68 homolog (Basophilic leukemia-expressed protein Bles03) (Protein WF-3) 298 31,846 Alternative sequence (2); Chain (1); Erroneous translation (1); Sequence conflict (1) +Q8VC23 CK086_MOUSE Uncharacterized protein C11orf86 homolog 124 14,068 Chain (1); Sequence conflict (4) +Q32M26 CK087_MOUSE Uncharacterized protein C11orf87 homolog 199 20,718 Chain (1); Frameshift (1); Glycosylation (2); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 61 81 Helical. {ECO:0000255}. TOPO_DOM 24 60 Extracellular. {ECO:0000255}.; TOPO_DOM 82 199 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. +Q80Y73 CK088_MOUSE UPF0722 protein C11orf88 homolog 168 19,068 Chain (1); Sequence conflict (7) +Q8BTW8 CK5P1_MOUSE CDK5 regulatory subunit-associated protein 1 (CDK5 activator-binding protein C42) 588 66,110 Chain (1); Domain (2); Metal binding (6); Sequence conflict (1) FUNCTION: Probable regulator of CDK5 activity. May inhibit CDK5 function via its interaction with CDK5R1 (By similarity). {ECO:0000250}. SUBUNIT: Interacts with CDK5R1 (p35 form). CDK5RAP1, CDK5RAP2 and CDK5RAP3 show competitive binding to CDK5R1. Probably forms a complex with CDK5R1 and CDK5 (By similarity). {ECO:0000250}. +Q99LM2 CK5P3_MOUSE CDK5 regulatory subunit-associated protein 3 503 56,991 Chain (1); Cross-link (1); Region (1) FUNCTION: Probable tumor suppressor initially identified as a CDK5R1 interactor controlling cell proliferation. Negatively regulates NF-kappa-B-mediated gene transcription through the control of RELA phosphorylation. Also regulates mitotic G2/M transition checkpoint and mitotic G2 DNA damage checkpoint. Through its interaction with CDKN2A/ARF and MDM2 may induce MDM2-dependent p53/TP53 ubiquitination, stabilization and activation in the nucleus, thereby promoting G1 cell cycle arrest and inhibition of cell proliferation. May play a role in the unfolded protein response, mediating the ufmylation of multiple proteins in response to endoplasmic reticulum stress. May also play a role in the rupture of the nuclear envelope during apoptosis. May regulate MAPK14 activity by regulating its dephosphorylation by PPM1D/WIP1. {ECO:0000250|UniProtKB:Q96JB5}. PTM: May be phosphorylated by CDK5. {ECO:0000250|UniProtKB:Q9JLH7}.; PTM: May be ufmylated. {ECO:0000305|PubMed:21494687}.; PTM: Ubiquitinated. Probably triggers proteasomal degradation and is negatively regulated by UFL1. {ECO:0000250|UniProtKB:Q96JB5}.; PTM: Cleaved by caspases early during apoptosis, the resulting peptides may play a role in rupture of the nuclear envelope. {ECO:0000250|UniProtKB:Q96JB5}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96JB5}. Cytoplasm {ECO:0000250|UniProtKB:Q96JB5}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q96JB5}. Note=Colocalizes and associates with microtubules. {ECO:0000250|UniProtKB:Q96JB5}. SUBUNIT: Interacts with CDK5R1; competes with CDK5RAP1 and CDK5RAP2. Interacts with RELA. Interacts with CHEK1; may negatively regulate CHEK1 and thereby stimulate entry into mitosis. Interacts with CDKN2A/ARF and MDM2; forms a ternary complex involved in regulation of p53/TP53 (By similarity). Interacts with UFL1; the interaction is direct (PubMed:21494687). Interacts with DDRGK1. Interacts with MAPK14. Interacts with CCNB1. Interacts with TUBG1; may regulate CDK5RAP3 in mitotic G2/M transition checkpoint (By similarity). {ECO:0000250|UniProtKB:Q96JB5, ECO:0000269|PubMed:21494687}. TISSUE SPECIFICITY: Widely expressed with higher expression in secretory tissues. {ECO:0000269|PubMed:21494687}. +O35143 ATIF1_MOUSE ATPase inhibitor, mitochondrial (ATP synthase F1 subunit epsilon) (Inhibitor of F(1)F(o)-ATPase) (IF(1)) (IF1) 106 12,159 Chain (1); Coiled coil (1); Modified residue (2); Region (2); Sequence conflict (1); Transit peptide (1) FUNCTION: Endogenous F(1)F(o)-ATPase inhibitor limiting ATP depletion when the mitochondrial membrane potential falls below a threshold and the F(1)F(o)-ATP synthase starts hydrolyzing ATP to pump protons out of the mitochondrial matrix. Required to avoid the consumption of cellular ATP when the F(1)F(o)-ATP synthase enzyme acts as an ATP hydrolase (By similarity). Indirectly acts as a regulator of heme synthesis in erythroid tissues: regulates heme synthesis by modulating the mitochondrial pH and redox potential, allowing FECH to efficiently catalyze the incorporation of iron into protoporphyrin IX to produce heme. {ECO:0000250, ECO:0000269|PubMed:23135403}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. SUBUNIT: Homodimer; represents the active form and is present at a pH value below 6.5. Homotetramer; represents the inactive form and is present at a pH value above 7.0 (By similarity). {ECO:0000250}. DOMAIN: Forms an alpha-helical dimer with monomers associated via an antiparallel alpha-helical coiled coil composed of residues 74-106, leaving each N-terminal inhibitory region (residues 26-52) accessible for interaction with an F1 catalytic domain. The inhibitory N-terminal region (residues 26-52) binds the alpha(ADP-bound)-beta(ADP-bound) (ATP5F1A-ATP5F1B) interface of F1-ATPase, and also contact the central gamma subunit (ATP5F1C). This dimeric state is favored by pH values below 7.0, and at higher values the dimers associate to form inactive homotetramer, where the inhibitory region is occluded, masking its inhibitory activity (By similarity). {ECO:0000250}. +Q3V1H1 CKAP2_MOUSE Cytoskeleton-associated protein 2 664 74,029 Chain (1); Erroneous initiation (1); Modified residue (5); Region (1); Sequence conflict (2) FUNCTION: Possesses microtubule stabilizing properties. Involved in regulating aneuploidy, cell cycling, and cell death in a p53-dependent manner. {ECO:0000269|PubMed:15504249, ECO:0000269|PubMed:16061649}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, spindle pole. Note=Contrary to the ectopically expressed protein, endogenous CKAP2 does not colocalize with microtubules in G1, S and early G2. At late G2 and prophase after separation of duplicated centrosomes, colocalizes with gamma-tubulin and centrosome-proximal microtubules. From prometaphase through anaphase B, colocalizes with mitotic spindle poles and spindle microtubules. During cytokinesis, absent from midbody microtubules (By similarity). {ECO:0000250}. SUBUNIT: Associates with alpha- and beta-tubulins. +Q80U30 CL16A_MOUSE Protein CLEC16A 1036 116,232 Alternative sequence (9); Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (1); Sequence conflict (1) FUNCTION: Regulator of mitophagy through the upstream regulation of the RNF41/NRDP1-PRKN pathway. Mitophagy is a selective form of autophagy necessary for mitochondrial quality control. The RNF41/NRDP1-PRKN pathway regulates autophagosome-lysosome fusion during late mitophagy. May protect RNF41/NRDP1 from proteosomal degradation, RNF41/NRDP1 which regulates proteosomal degradation of PRKN. Plays a key role in beta cells functions by regulating mitophagy/autophagy and mitochondrial health. {ECO:0000269|PubMed:24949970}. SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:24949970}; Peripheral membrane protein {ECO:0000269|PubMed:24949970}. Lysosome membrane {ECO:0000269|PubMed:24949970}; Peripheral membrane protein {ECO:0000269|PubMed:24949970}. Note=Associates with the endolysosome membrane. {ECO:0000269|PubMed:24949970}. SUBUNIT: Interacts with RNF41/NRDP1. {ECO:0000269|PubMed:24949970}. TISSUE SPECIFICITY: Ubiquitously expressed. Expressed in pancreatic islets. {ECO:0000269|PubMed:19855005, ECO:0000269|PubMed:24949970}. +Q6Q473 CLA4A_MOUSE Calcium-activated chloride channel regulator 4A (EC 3.4.-.-) (Calcium-activated chloride channel regulator 6) (mClca6) [Cleaved into: Calcium-activated chloride channel regulator 4A, 110 kDa form; Calcium-activated chloride channel regulator 4A, 30 kDa form] 924 101,872 Active site (1); Alternative sequence (2); Chain (3); Domain (1); Glycosylation (12); Metal binding (3); Region (1); Signal peptide (1); Site (1); Transmembrane (1) TRANSMEM 884 904 Helical. {ECO:0000255}. FUNCTION: May be involved in mediating calcium-activated chloride conductance. {ECO:0000269|PubMed:15284223, ECO:0000269|PubMed:18285349}. PTM: N-Glycosylated. {ECO:0000269|PubMed:15284223, ECO:0000269|PubMed:18285349}.; PTM: The translation product is autoproteolytically cleaved by the metalloprotease domain in the endoplasmic reticulum into a N-terminal and a C-terminal products that remain physically associated with each other. The cleavage is necessary for calcium-activated chloride channel (CaCC) activation activity. {ECO:0000250|UniProtKB:A8K7I4}. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. Apical cell membrane. Secreted. Note=The C-terminus 30 kDa form is anchored to the membrane. The N-terminus 110 kDa form is released from the membrane triggered by an unknown stimulus. Associated with the microvilli of non-goblet cell enterocytes in the small and large intestine. Colocalizes with CFTR. DOMAIN: The metalloprotease region is responsible for autoproteolytic processing. It can also cross-cleave other CLCA substrates. {ECO:0000250|UniProtKB:A8K7I4}. TISSUE SPECIFICITY: Expressed in the non-goblet intestinal cells. High levels in intestine and stomach, and lower levels in eye, liver and spleen. Increasing expression from the duodenum to the ilium, and decreasing expression to the colon. Isoform 2 is expressed in intestine and stomach but at lower levels than isoform 1. {ECO:0000269|PubMed:15284223, ECO:0000269|PubMed:18285349}. +Q80TV8 CLAP1_MOUSE CLIP-associating protein 1 (Cytoplasmic linker-associated protein 1) 1535 169,227 Alternative sequence (3); Chain (1); Coiled coil (1); Compositional bias (1); Erroneous initiation (1); Modified residue (28); Region (4); Repeat (7); Sequence caution (1); Sequence conflict (2) FUNCTION: Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules. Involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). Required for the polarization of the cytoplasmic microtubule arrays in migrating cells towards the leading edge of the cell. May act at the cell cortex to enhance the frequency of rescue of depolymerizing microtubules by attaching their plus-ends to cortical platforms composed of ERC1 and PHLDB2. This cortical microtubule stabilizing activity is regulated at least in part by phosphatidylinositol 3-kinase signaling. Also performs a similar stabilizing function at the kinetochore which is essential for the bipolar alignment of chromosomes on the mitotic spindle (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Note=Localizes to microtubule plus ends. Localizes to centrosomes, kinetochores and the mitotic spindle from prometaphase. Subsequently localizes to the spindle midzone from anaphase and to the midbody from telophase. In migrating cells localizes to the plus ends of microtubules within the cell body and to the entire microtubule lattice within the lamella. Localizes to the cell cortex and this requires ERC1 and PHLDB2. {ECO:0000250}. SUBUNIT: Interacts with ERC1, MAPRE1, MAPRE3, microtubules, and PHLDB2. The interaction with ERC1 may be mediated by PHLDB2. Interacts with GCC2; recruits CLASP1 to Golgi membranes (By similarity). Interacts with CLIP2 and RSN. Interacts with MACF1. {ECO:0000250, ECO:0000269|PubMed:11290329, ECO:0000269|PubMed:18854161}. TISSUE SPECIFICITY: Highly expressed in brain and heart and at lower levels in kidney, lung, skeletal muscle and testis. {ECO:0000269|PubMed:11290329}. +Q8BHN9 CLBA1_MOUSE Uncharacterized protein CLBA1 (Clathrin-binding box of aftiphilin-containing protein 1) 321 34,683 Chain (1); Sequence conflict (3) +Q62388 ATM_MOUSE Serine-protein kinase ATM (EC 2.7.11.1) (Ataxia telangiectasia mutated homolog) (A-T mutated homolog) 3066 349,418 Chain (1); Domain (3); Initiator methionine (1); Modified residue (6); Mutagenesis (3); Region (1); Sequence conflict (1) FUNCTION: Serine/threonine protein kinase which activates checkpoint signaling upon double strand breaks (DSBs), apoptosis and genotoxic stresses such as ionizing ultraviolet A light (UVA), thereby acting as a DNA damage sensor. Recognizes the substrate consensus sequence [ST]-Q. Phosphorylates 'Ser-139' of histone variant H2AX/H2AFX at double strand breaks (DSBs), thereby regulating DNA damage response mechanism. Also plays a role in pre-B cell allelic exclusion, a process leading to expression of a single immunoglobulin heavy chain allele to enforce clonality and monospecific recognition by the B-cell antigen receptor (BCR) expressed on individual B-lymphocytes. After the introduction of DNA breaks by the RAG complex on one immunoglobulin allele, acts by mediating a repositioning of the second allele to pericentromeric heterochromatin, preventing accessibility to the RAG complex and recombination of the second allele. Also involved in signal transduction and cell cycle control. May function as a tumor suppressor. Necessary for activation of ABL1 and SAPK. Phosphorylates DYRK2, CHEK2, p53/TP53, FANCD2, NFKBIA, BRCA1, CTIP, nibrin (NBN), TERF1, RAD9 and DCLRE1C. May play a role in vesicle and/or protein transport. Could play a role in T-cell development, gonad and neurological function. Binds DNA ends. Plays a role in replication-dependent histone mRNA degradation. Phosphorylation of DYRK2 in nucleus in response to genotoxic stress prevents its MDM2-mediated ubiquitination and subsequent proteasome degradation. Phosphorylates ATF2 which stimulates its function in DNA damage response. {ECO:0000269|PubMed:11571274, ECO:0000269|PubMed:19047460, ECO:0000269|PubMed:19448632}. PTM: Phosphorylated by NUAK1/ARK5 (By similarity). Autophosphorylation on Ser-367, Ser-1899, Ser-1987 correlates with DNA damage-mediated activation of the kinase. {ECO:0000250, ECO:0000269|PubMed:19047460}.; PTM: Acetylated by KAT5 upon DNA damage; which is required for autophosphorylation and subsequent activation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13315}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q13315}. Note=Primarily nuclear. Found also in endocytic vesicles in association with beta-adaptin. {ECO:0000250|UniProtKB:Q13315}. SUBUNIT: Dimers or tetramers in inactive state. On DNA damage, autophosphorylation dissociates ATM into monomers rendering them catalytically active. Binds DNA ends, p53/TP53, ABL1, BRCA1, NBN/nibrin and TERF1. Part of the BRCA1-associated genome surveillance complex (BASC), which contains BRCA1, MSH2, MSH6, MLH1, ATM, BLM, PMS2 and the RAD50-MRE11-NBN protein complex. This association could be a dynamic process changing throughout the cell cycle and within subnuclear domains. DNA damage promotes association with RAD17. Interacts with EEF1E1; the interaction, induced on DNA damage, up-regulates TP53. Interacts with DCLRE1C, MYST1, KAT5, NABP2, ATMIN and CEP164 (By similarity). Interacts with AP2B1 AND AP3B2; the interaction occurs in cytoplasmic vesicles (PubMed:9707615). Interacts with TELO2 AND TTI1. Interacts with DDX1 (By similarity). Interacts with BRAT1 (By similarity). {ECO:0000250|UniProtKB:Q13315, ECO:0000269|PubMed:9707615}. DOMAIN: The FATC domain is required for interaction with KAT5. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in brain, skeletal muscle, testis, followed by spleen, lung, kidney, heart, liver and thymus. Ubiquitously expressed in embryonal tissues. +O35126 ATN1_MOUSE Atrophin-1 (Dentatorubral-pallidoluysian atrophy protein homolog) 1175 123,724 Chain (1); Compositional bias (14); Cross-link (1); Modified residue (16); Motif (2); Region (2); Sequence conflict (7); Site (1) FUNCTION: Transcriptional corepressor. Corepressor of MTG8 transcriptional repression. Has some intrinsic repression activity which is independent of the number of the poly-Q repeats (By similarity). Recruits NR2E1 to repress transcription. Promotes vascular smooth cell (VSMC) migration and orientation. {ECO:0000250, ECO:0000269|PubMed:16702404, ECO:0000269|PubMed:19131340}. PTM: Phosphorylated in vitro by MAPK8/JNK1 on Ser-724. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}. Cell junction {ECO:0000250}. Nucleus {ECO:0000250}. Note=Shuttles between nucleus and cytoplasm. Colocalizes with FAT1 in the perinuclear area, at cell-cell junctions and leading edges of cells. Colocalizes with MTG8 in discrete nuclear dots (By similarity). {ECO:0000250}. SUBUNIT: Interacts with BAIAP2, WWP1, WWP2, WWP3 and RERE. Interacts (via its N-terminus) with MTG8; the interaction enhances transcriptional repression of MTG8. Interacts with PQBP1 (By similarity). Interacts with NR2E1; the interaction represses the transcriptional activity of NR2E1. Interacts with FAT1 (via a C-terminal domain). {ECO:0000250, ECO:0000269|PubMed:16702404, ECO:0000269|PubMed:19131340}. TISSUE SPECIFICITY: Widely expressed. Most abundant in the brain. {ECO:0000269|PubMed:9070948}. +Q8VI21 CLC2F_MOUSE C-type lectin domain family 2 member F (C-type lectin-related protein C) (Clr-c) 196 22,205 Chain (1); Disulfide bond (2); Domain (1); Glycosylation (1); Topological domain (2); Transmembrane (1) TRANSMEM 42 62 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 41 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 63 196 Extracellular. {ECO:0000255}. FUNCTION: Lectin-type cell surface receptor. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. +Q9D676 CLC2G_MOUSE C-type lectin domain family 2 member G (DDV10) (Osteoclast inhibitory lectin-related protein 1) (Ocil-related protein 1) 269 30,884 Alternative sequence (1); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (1); Sequence conflict (4); Topological domain (2); Transmembrane (1) TRANSMEM 108 128 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 107 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 129 269 Extracellular. {ECO:0000255}. FUNCTION: Inhibits osteoclast formation. {ECO:0000269|PubMed:12374791}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Detected in vagina, eye, tongue, stomach and spleen. {ECO:0000269|PubMed:12374791, ECO:0000269|PubMed:12746323}. +Q9WVF9 CLC2I_MOUSE C-type lectin domain family 2 member I (C-type lectin-related protein DCL1) (C-type lectin-related protein G) (Clr-g) (Lymphoid-derived C-type lectin-1) (LCL-1) (Osteoclast inhibitory lectin-related protein 2) (Ocil-related protein 2) 217 24,671 Alternative sequence (3); Beta strand (7); Chain (1); Disulfide bond (2); Domain (1); Erroneous initiation (1); Glycosylation (1); Helix (2); Topological domain (2); Transmembrane (1); Turn (1) TRANSMEM 54 74 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 53 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 75 217 Extracellular. {ECO:0000255}. FUNCTION: Inhibits osteoclast formation. Receptor for KLRB1F. Enhances T-cell activation. Plays a role in splenocyte activation, T-cell responses and IL-2 production. {ECO:0000269|PubMed:12374791, ECO:0000269|PubMed:15963483}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Detected in osteoblasts, growth plate chondrocytes and skeletal muscle overlying the bone (at protein level). Detected in spleen, B-cells, dendritic cells, thymus, and in IL2-activated natural killer cells. {ECO:0000269|PubMed:11398965, ECO:0000269|PubMed:12374791, ECO:0000269|PubMed:15963483}. +Q04646 ATNG_MOUSE Sodium/potassium-transporting ATPase subunit gamma (Na(+)/K(+) ATPase subunit gamma) (FXYD domain-containing ion transport regulator 2) (Sodium pump gamma chain) 70 7,520 Alternative sequence (2); Chain (1); Erroneous initiation (1); Transmembrane (1) TRANSMEM 33 50 Helical. {ECO:0000255}. FUNCTION: May be involved in forming the receptor site for cardiac glycoside binding or may modulate the transport function of the sodium ATPase. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type III membrane protein {ECO:0000305}. SUBUNIT: Regulatory subunit of the sodium/potassium-transporting ATPase which is composed of a catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an additional regulatory subunit. {ECO:0000250|UniProtKB:O13001}. TISSUE SPECIFICITY: Highest levels expressed in the kidney and spleen. Restricted to the basolateral membrane in renal epithelial cells and varies in its level of expression along the nephron. +Q9Z2E5 ATOH7_MOUSE Protein atonal homolog 7 (Helix-loop-helix protein mATH-5) (mATH5) 149 16,569 Chain (1); Domain (1) FUNCTION: Transcription factor involved in the differentiation of most retinal ganglion cells, including those constituting the retino-hypothalamic tract. {ECO:0000269|PubMed:11156601, ECO:0000269|PubMed:11493566, ECO:0000269|PubMed:12451142, ECO:0000269|PubMed:9806930}. SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. +Q99NA2 ATOH8_MOUSE Protein atonal homolog 8 (Helix-loop-helix protein mATH-6) (mATH6) (Okadin) 322 34,785 Chain (1); Compositional bias (1); Domain (1); Region (2); Sequence conflict (1) FUNCTION: Transcription factor that binds a palindromic (canonical) core consensus DNA sequence 5'-CANNTG- 3' known as an E-box element, possibly as a heterodimer with other bHLH proteins (By similarity). Regulates endothelial cell proliferation, migration and tube-like structures formation (By similarity). Modulates endothelial cell differentiation through NOS3 (By similarity). May be implicated in specification and differentiation of neuronal cell lineages in the brain (PubMed:11733035). May participate in kidney development and may be involved in podocyte differentiation (PubMed:16937370). During early embryonic development is involved in tissue-specific differentiation processes that are dependent on class II bHLH factors and namely modulates the differentiation program initiated by the pro-endocrine factor NEUROG3 (PubMed:18560595). During myogenesis, may play a role during the transition of myoblasts from the proliferative phase to the differentiation phase (PubMed:24186058). Positively regulates HAMP transcription in two ways, firstly by acting directly on the HAMP promoter via E-boxes binding and indirectly through increased phosphorylation of SMAD protein complex (By similarity). Repress NEUROG3-dependent gene activation in a gene-specific manner through at least two mechanisms; requires only either the sequestering of a general partner such as TCF3 through heterodimerization, either also requires binding of the bHLH domain to DNA via a basic motif (PubMed:23938248). {ECO:0000250|UniProtKB:Q96SQ7, ECO:0000269|PubMed:11733035, ECO:0000269|PubMed:16937370, ECO:0000269|PubMed:18560595, ECO:0000269|PubMed:23938248}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24186058}. Nucleus speckle {ECO:0000250|UniProtKB:Q96SQ7}. Cytoplasm {ECO:0000269|PubMed:24186058}. SUBUNIT: Efficient DNA binding requires dimerization with another bHLH protein. Interacts with NEUROG3 AND NEUROD1. Interacts with ZFPM2; mediates indirect interaction with GATA4. Forms a heterodimer with TCF3; repress transcription of TCF3 and TCF3/NEUROG3 dimer-induced transactivation of E box-dependent promoters. {ECO:0000250, ECO:0000269|PubMed:18560595, ECO:0000269|PubMed:23836893, ECO:0000269|PubMed:23938248}. DOMAIN: The bHLH domain mediates transcriptional repression by inhibiting TCF3 transcriptional activity through heterodimerization. {ECO:0000269|PubMed:23938248}. TISSUE SPECIFICITY: Expressed by subsets of mature neurons (PubMed:11733035). Expressed in kidney (podocytes) (PubMed:16937370). Expression is restricted to the atria, lung mesenchyme, and vascular smooth muscle (PubMed:23836893). {ECO:0000269|PubMed:11733035, ECO:0000269|PubMed:16937370, ECO:0000269|PubMed:23836893}. +P70194 CLC4F_MOUSE C-type lectin domain family 4 member F (C-type lectin superfamily member 13) (C-type lectin 13) (Kupffer cell receptor) 548 61,269 Chain (1); Disulfide bond (2); Domain (1); Glycosylation (6); Sequence conflict (1); Topological domain (2); Transmembrane (1) TRANSMEM 43 69 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 42 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 70 548 Extracellular. {ECO:0000255}. FUNCTION: Receptor with an affinity for galactose and fucose. Could be involved in endocytosis. SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. TISSUE SPECIFICITY: Kupffer cells. +Q9R007 CLC5A_MOUSE C-type lectin domain family 5 member A (C-type lectin superfamily member 5) (Myeloid DAP12-associating lectin 1) (MDL-1) 190 21,696 Alternative sequence (2); Chain (1); Disulfide bond (2); Domain (1); Glycosylation (3); Topological domain (2); Transmembrane (1) TRANSMEM 5 25 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 4 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 26 190 Extracellular. {ECO:0000255}. FUNCTION: Functions as a positive regulator of osteoclastogenesis (PubMed:19251634). Cell surface receptor that signals via TYROBP (PubMed:10449773). Regulates inflammatory responses (PubMed:20212065). {ECO:0000269|PubMed:10449773, ECO:0000269|PubMed:19251634, ECO:0000269|PubMed:20212065}. PTM: N-glycosylated (PubMed:19074552, PubMed:19251634). Contains sialic acid residues (PubMed:19074552). {ECO:0000269|PubMed:19074552, ECO:0000269|PubMed:19251634}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19074552}; Single-pass type II membrane protein {ECO:0000269|PubMed:19074552}. SUBUNIT: Monomer (By similarity). Homodimer (By similarity). The majority of CLEC5A is expressed as a monomeric form on macrophages (By similarity). Interacts with TYROBP/DAP12 (PubMed:10449773). The interaction with TYROBP is required for CLEC5 cell surface expression (PubMed:10449773). Interacts with HCST/DAP10 (PubMed:19074552, PubMed:19251634). Forms a CLEC5A/TYROBP/HCST trimolecular complex depending almost solely on TYROBP (PubMed:19251634). {ECO:0000250|UniProtKB:Q9NY25, ECO:0000269|PubMed:10449773, ECO:0000269|PubMed:19074552, ECO:0000269|PubMed:19251634}. TISSUE SPECIFICITY: Strong expression in bone marrow cells and thioglycollate-induced neutrophils (at protein level) (PubMed:19074552). Expressed on granulocytes and monocytes from bone marrow and peripheral blood (PubMed:20212065). Expressed in macrophage cell line J-774, but not in T-cell lines, B-cell lines, or mast cell lines (PubMed:10449773). {ECO:0000269|PubMed:10449773, ECO:0000269|PubMed:19074552, ECO:0000269|PubMed:20212065}. DISEASE: Note=Involved in the pathogenetic mechanisms of Japanese encephalitis virus (JEV) infection of the brain. JEV infection of young mice results in increased expression of CLEC5A in spleen and brain with consequent activation of proinflammatory cytokine secretion. {ECO:0000269|PubMed:20637688}. +Q9D7Z6 CLCA1_MOUSE Calcium-activated chloride channel regulator 1 (EC 3.4.-.-) (Calcium-activated chloride channel family member 3) (mCLCA3) (Protein gob-5) 913 100,071 Active site (1); Chain (1); Domain (1); Glycosylation (6); Metal binding (3); Region (1); Sequence conflict (1); Signal peptide (1); Site (1) FUNCTION: May be involved in mediating calcium-activated chloride conductance. May play critical roles in goblet cell metaplasia, mucus hypersecretion, cystic fibrosis and AHR. May be involved in the regulation of mucus production and/or secretion by goblet cells. Involved in the regulation of tissue inflammation in the innate immune response. May play a role as a tumor suppressor. Induces MUC5AC. {ECO:0000269|PubMed:11296262, ECO:0000269|PubMed:11694454, ECO:0000269|PubMed:16645179}. PTM: The 110 kDa translation product is autoproteolytically cleaved by the metalloprotease domain in the endoplasmic reticulum into a 75 kDa N-terminal and a 35 kDa C-terminal products that remain physically associated with each other. The cleavage is necessary for calcium-activated chloride channel (CaCC) activation activity. {ECO:0000250|UniProtKB:A8K7I4, ECO:0000269|PubMed:12019299}.; PTM: Glycosylated. {ECO:0000269|PubMed:12019299, ECO:0000269|PubMed:16895902}. SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000269|PubMed:12019299, ECO:0000269|PubMed:15919655, ECO:0000269|PubMed:16895902}. Note=The 75 kDa N-terminal and a 35 kDa C-terminal products are fully secreted into extracellular environment as a soluble complex of two glycoproteins. DOMAIN: The metalloprotease region is responsible for autoproteolytic processing. It can also cross-cleave other CLCA substrates. {ECO:0000250|UniProtKB:A8K7I4}. TISSUE SPECIFICITY: Exclusively expressed in the digestive and respiratory tracts and in the uterus (at protein level). Expressed in small intestine, colon, stomach, and uterus and slightly expressed in trachea tissue. Exclusively expressed in the mucin granule membranes of gastrointestinal, respiratory, and uterine goblet cells and other mucin-producing cells. In the colon, expressed in the surface mucous cells. In the stomach highly expressed in the surface epithelium in the pylorus. Strongly expressed in the airway epithelium of lung tissues associated with airway hyperresponsiveness (AHR). {ECO:0000269|PubMed:10049711, ECO:0000269|PubMed:11296262, ECO:0000269|PubMed:12019299}. +Q8BG22 CLCA2_MOUSE Calcium-activated chloride channel regulator 2 (EC 3.4.-.-) (Calcium-activated chloride channel family member 5) (mCLCA5) 942 103,626 Active site (1); Alternative sequence (1); Chain (1); Domain (1); Glycosylation (10); Metal binding (3); Region (1); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 906 926 Helical. {ECO:0000255}. TOPO_DOM 33 905 Extracellular. {ECO:0000255}.; TOPO_DOM 927 942 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a role in modulating chloride current across the plasma membrane in a calcium-dependent manner, and cell adhesion. Involved in basal cell adhesion and/or stratification of squamous epithelia. May act as a tumor suppressor in breast and colorectal cancer. Plays a key role for cell adhesion in the beginning stages of lung metastasis via the binding to ITGB4. {ECO:0000269|PubMed:15284223, ECO:0000269|PubMed:15292178}. PTM: The translation product is autoproteolytically cleaved by the metalloprotease domain in the endoplasmic reticulum into a N-terminal and a C-terminal products that remain physically associated with each other. The cleavage is necessary for calcium-activated chloride channel (CaCC) activation activity. {ECO:0000250|UniProtKB:A8K7I4}.; PTM: N-glycosylated. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15284223}; Single-pass type I membrane protein {ECO:0000269|PubMed:15284223}. Basal cell membrane {ECO:0000269|PubMed:15284223}; Single-pass type I membrane protein {ECO:0000269|PubMed:15284223}. Cell junction {ECO:0000269|PubMed:15284223}. DOMAIN: The metalloprotease region is responsible for autoproteolytic processing. It can also cross-cleave other CLCA substrates. {ECO:0000250|UniProtKB:A8K7I4}. TISSUE SPECIFICITY: Highly expressed in eye, spleen, lung, kidney, uterus, and endothelial cells. Weakly expressed in heart and throughout the gastrointestinal tract. Highly expressed in mammary cell lines. Its expression in immortalized cell line HC11 correlates with slow or arrested growth. Re-expression in mammary tumor cells reduces colony survival. {ECO:0000269|PubMed:15284223, ECO:0000269|PubMed:15292178}. +Q9CWQ3 ATP23_MOUSE Mitochondrial inner membrane protease ATP23 homolog (EC 3.4.24.-) (XRCC6-binding protein 1) 201 21,710 Active site (1); Chain (1); Metal binding (2) SUBUNIT: Interacts with XRCC6. {ECO:0000250}. +O08585 CLCA_MOUSE Clathrin light chain A (Lca) 235 25,604 Chain (1); Modified residue (5); Region (1); Sequence conflict (6) FUNCTION: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. Acts as component of the TACC3/ch-TOG/clathrin complex proposed to contribute to stabilization of kinetochore fibers of the mitotic spindle by acting as inter-microtubule bridge (By similarity). {ECO:0000250|UniProtKB:P09496}. SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Membrane, coated pit; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P09496}. Note=Cytoplasmic face of coated pits and vesicles.In complex with TACC3 and CKAP5 (forming the TACC3/ch-TOG/clathrin complex) localized to inter-microtubule bridges in mitotic spindles. {ECO:0000250|UniProtKB:P09496}. SUBUNIT: Clathrin coats are formed from molecules containing 3 heavy chains and 3 light chains. Interacts with CALY; the interaction stimulates clathrin self-assembly and clathrin-mediated endocytosis (By similarity). Interacts with CKAP5 and TACC3 forming the TACC3/ch-TOG/clathrin complex located at spindle inter-microtubules bridges; the complex implicates clathrin triskelions (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P09496}. +P56382 ATP5E_MOUSE ATP synthase subunit epsilon, mitochondrial (ATPase subunit epsilon) (ATP synthase F1 subunit epsilon) 52 5,838 Chain (1); Modified residue (7) FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane. SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) seems to have nine subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L). Component of an ATP synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MD and MP68 (By similarity). {ECO:0000250}. +Q99LI2 CLCC1_MOUSE Chloride channel CLIC-like protein 1 539 60,621 Chain (1); Erroneous gene model prediction (1); Modified residue (7); Signal peptide (1); Transmembrane (3) TRANSMEM 185 205 Helical. {ECO:0000255}.; TRANSMEM 216 236 Helical. {ECO:0000255}.; TRANSMEM 330 350 Helical. {ECO:0000255}. FUNCTION: Seems to act as a chloride ion channel. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Endoplasmic reticulum {ECO:0000250}. Golgi apparatus {ECO:0000250}. Nucleus {ECO:0000250}. +Q9QZM3 CLCF1_MOUSE Cardiotrophin-like cytokine factor 1 (B-cell-stimulating factor 3) (BSF-3) (Novel neurotrophin-1) (NNT-1) 225 25,261 Chain (1); Glycosylation (1); Signal peptide (1) FUNCTION: Cytokine with B-cell stimulating capability. Binds to and activates the ILST/gp130 receptor. {ECO:0000269|PubMed:10500198}. SUBCELLULAR LOCATION: Secreted {ECO:0000250}. +Q9WUB7 CLCKA_MOUSE Chloride channel protein ClC-Ka (Chloride channel Ka) (ClC-K1) 687 75,684 Chain (1); Domain (2); Metal binding (4); Sequence conflict (3); Topological domain (1); Transmembrane (11) TRANSMEM 52 72 Helical. {ECO:0000255}.; TRANSMEM 94 114 Helical. {ECO:0000255}.; TRANSMEM 161 181 Helical. {ECO:0000255}.; TRANSMEM 204 224 Helical. {ECO:0000255}.; TRANSMEM 236 256 Helical. {ECO:0000255}.; TRANSMEM 282 302 Helical. {ECO:0000255}.; TRANSMEM 325 345 Helical. {ECO:0000255}.; TRANSMEM 396 416 Helical. {ECO:0000255}.; TRANSMEM 417 437 Helical. {ECO:0000255}.; TRANSMEM 458 478 Helical. {ECO:0000255}.; TRANSMEM 486 506 Helical. {ECO:0000255}. TOPO_DOM 507 687 Cytoplasmic. {ECO:0000255}. FUNCTION: Voltage-gated chloride channel. Chloride channels have several functions including the regulation of cell volume; membrane potential stabilization, signal transduction and transepithelial transport. May be important in urinary concentrating mechanisms. May be the basolateral chloride channel mediating net chloride absorption in CTAL cells. SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11734858}; Multi-pass membrane protein {ECO:0000269|PubMed:11734858}. SUBUNIT: Homodimer (By similarity). Interacts with BSND. Forms heteromers with BSND in the thin ascending limb of Henle. {ECO:0000250, ECO:0000269|PubMed:11734858}. TISSUE SPECIFICITY: Specifically expressed in the kidney. All nephron segments expressing BSND also express CLCNK proreins. {ECO:0000269|PubMed:11014860, ECO:0000269|PubMed:11734858}. +P97450 ATP5J_MOUSE ATP synthase-coupling factor 6, mitochondrial (ATPase subunit F6) (ATP synthase peripheral stalk subunit F6) 108 12,496 Chain (1); Modified residue (11); Transit peptide (1) FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements. Also involved in the restoration of oligomycin-sensitive ATPase activity to depleted F1-F0 complexes. SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane. SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(0) seems to have nine subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L). Component of an ATP synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MD and MP68 (By similarity). {ECO:0000250}. +Q9R0A1 CLCN2_MOUSE Chloride channel protein 2 (ClC-2) 908 99,447 Binding site (3); Chain (1); Compositional bias (1); Domain (2); Intramembrane (7); Modified residue (2); Motif (3); Sequence conflict (1); Topological domain (2); Transmembrane (10) INTRAMEM 172 179 Helical. {ECO:0000255}.; INTRAMEM 247 259 Helical. {ECO:0000250}.; INTRAMEM 263 271 Helical. {ECO:0000250}.; INTRAMEM 505 519 Helical. {ECO:0000250}.; INTRAMEM 520 521 Note=Loop between two helices. {ECO:0000250}.; INTRAMEM 522 533 Helical. {ECO:0000250}.; INTRAMEM 534 538 Note=Loop between two helices. {ECO:0000250}. TRANSMEM 96 129 Helical. {ECO:0000250}.; TRANSMEM 138 163 Helical. {ECO:0000250}.; TRANSMEM 188 206 Helical. {ECO:0000250}.; TRANSMEM 213 231 Helical. {ECO:0000250}.; TRANSMEM 283 303 Helical. {ECO:0000250}.; TRANSMEM 329 357 Helical. {ECO:0000250}.; TRANSMEM 366 385 Helical. {ECO:0000250}.; TRANSMEM 437 457 Helical. {ECO:0000250}.; TRANSMEM 465 488 Helical. {ECO:0000250}.; TRANSMEM 539 556 Helical. {ECO:0000250}. TOPO_DOM 1 95 Cytoplasmic. {ECO:0000250}.; TOPO_DOM 557 908 Cytoplasmic. {ECO:0000250}. FUNCTION: Voltage-gated chloride channel. Chloride channels have several functions including the regulation of cell volume, membrane potential stabilization, signal transduction and transepithelial transport (By similarity). Involved in the regulation of aldosterone production. The opening of CLCN2 channels at hyperpolarized membrane potentials in the glomerulosa causes cell membrane depolarization, activation of voltage-gated Ca2+ channels and increased expression of aldosterone synthase, the rate-limiting enzyme for aldosterone biosynthesis (By similarity). {ECO:0000250|UniProtKB:P35525, ECO:0000250|UniProtKB:P51788}. PTM: Phosphorylated. Activated by dephosphorylation. {ECO:0000250|UniProtKB:P35525}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P35525}; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed in the adrenal gland and brain. {ECO:0000269|PubMed:29403011, ECO:0000269|PubMed:29403012}. +Q9CRA7 ATP5S_MOUSE ATP synthase subunit s, mitochondrial (ATP synthase-coupling factor B) (Distal membrane arm assembly complex 2-like protein) (Mitochondrial ATP synthase regulatory component factor B) 200 23,275 Chain (1); Metal binding (2); Region (1); Repeat (4); Sequence conflict (1); Transit peptide (1) FUNCTION: Involved in regulation of mitochondrial membrane ATP synthase. Necessary for H(+) conduction of ATP synthase. Facilitates energy-driven catalysis of ATP synthesis by blocking a proton leak through an alternative proton exit pathway. {ECO:0000250|UniProtKB:P22027}. SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P22027}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:P22027}. SUBUNIT: Homotetramer. Associates with ATP synthase. {ECO:0000250|UniProtKB:P22027}. +Q60771 CLD11_MOUSE Claudin-11 (Oligodendrocyte transmembrane protein) (Oligodendrocyte-specific protein) 207 22,114 Chain (1); Modified residue (4); Sequence conflict (1); Topological domain (5); Transmembrane (4) TRANSMEM 2 22 Helical. {ECO:0000255}.; TRANSMEM 83 103 Helical. {ECO:0000255}.; TRANSMEM 123 143 Helical. {ECO:0000255}.; TRANSMEM 158 178 Helical. {ECO:0000255}. TOPO_DOM 1 1 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 23 82 Extracellular. {ECO:0000255}.; TOPO_DOM 104 122 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 144 157 Extracellular. {ECO:0000255}.; TOPO_DOM 179 207 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, tight junction. Cell membrane {ECO:0000250|UniProtKB:O75508}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Interacts with tetraspanin-3/TSPAN3 (PubMed:11309411). Interacts with OCLN (By similarity). {ECO:0000250|UniProtKB:O75508, ECO:0000269|PubMed:11309411}. +Q925N4 CLD16_MOUSE Claudin-16 (Paracellin-1) 235 26,100 Chain (1); Topological domain (5); Transmembrane (4) TRANSMEM 4 24 Helical. {ECO:0000255}.; TRANSMEM 80 100 Helical. {ECO:0000255}.; TRANSMEM 116 136 Helical. {ECO:0000255}.; TRANSMEM 170 190 Helical. {ECO:0000255}. TOPO_DOM 1 3 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 25 79 Extracellular. {ECO:0000255}.; TOPO_DOM 101 115 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 137 169 Extracellular. {ECO:0000255}.; TOPO_DOM 191 235 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. Involved in paracellular magnesium reabsorption. Required for a selective paracellular conductance. May form, alone or in partnership with other constituents, an intercellular pore permitting paracellular passage of magnesium and calcium ions down their electrochemical gradients. Alternatively, it could be a sensor of magnesium concentration that could alter paracellular permeability mediated by other factors (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, tight junction. Cell membrane; Multi-pass membrane protein. +Q8BXA6 CLD17_MOUSE Claudin-17 224 24,653 Chain (1); Topological domain (5); Transmembrane (4) TRANSMEM 8 28 Helical. {ECO:0000255}.; TRANSMEM 82 102 Helical. {ECO:0000255}.; TRANSMEM 125 145 Helical. {ECO:0000255}.; TRANSMEM 165 185 Helical. {ECO:0000255}. TOPO_DOM 1 7 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 29 81 Extracellular. {ECO:0000255}.; TOPO_DOM 103 124 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 146 164 Extracellular. {ECO:0000255}.; TOPO_DOM 186 224 Cytoplasmic. {ECO:0000255}. FUNCTION: Channel-forming tight junction protein with selectivity for anions, including chloride and bicarbonate, and for solutes smaller than 9 Angstrom in diameter. In the kidney proximal tubule, may be involved in quantitative reabsorption of filtered anions. Does not affect water permeability. {ECO:0000250|UniProtKB:P56750}. SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000269|PubMed:22402829}. Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. SUBUNIT: Interacts with OCLN. {ECO:0000250|UniProtKB:P56750}. TISSUE SPECIFICITY: Expressed at high levels in the kidney and at mucher lower levels in the brain. In the kidney, expression gradually decreases from the proximal tubule downstream to the distal convoluted tubule. Expressed in the thin ascending limb of Henle's loop, as well as in the thick ascending limb of Henle's loop. In the distal convoluted tubules, expressed only in a few tubules. Not detected in the collecting duct. In the brain, expressed in blood vessels (at protein level). {ECO:0000269|PubMed:22402829}. +P56857 CLD18_MOUSE Claudin-18 264 28,122 Alternative sequence (3); Chain (1); Modified residue (1); Topological domain (5); Transmembrane (4) TRANSMEM 7 27 Helical. {ECO:0000255}.; TRANSMEM 81 101 Helical. {ECO:0000255}.; TRANSMEM 123 143 Helical. {ECO:0000255}.; TRANSMEM 177 197 Helical. {ECO:0000255}. TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 28 80 Extracellular. {ECO:0000255}.; TOPO_DOM 102 122 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 144 176 Extracellular. {ECO:0000255}.; TOPO_DOM 198 264 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000269|PubMed:11585919}. Cell membrane {ECO:0000269|PubMed:11585919}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to tight junctions in epithelial cells. {ECO:0000269|PubMed:11585919}. TISSUE SPECIFICITY: Isoform A1.1: Expressed in lung (PubMed:11585919). Isoform A1.2: Expressed in lung (PubMed:11585919). Isoform A2.1: Expressed in stomach (PubMed:11585919). Isoform A2.2: Expressed in stomach (PubMed:11585919). +Q9ET38 CLD19_MOUSE Claudin-19 224 23,343 Alternative sequence (1); Chain (1); Disulfide bond (1); Mutagenesis (26); Topological domain (5); Transmembrane (4) TRANSMEM 8 28 Helical. {ECO:0000255}.; TRANSMEM 82 102 Helical. {ECO:0000255}.; TRANSMEM 118 138 Helical. {ECO:0000255}.; TRANSMEM 161 181 Helical. {ECO:0000255}. TOPO_DOM 1 7 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 29 81 Extracellular. {ECO:0000255}.; TOPO_DOM 103 117 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 139 160 Extracellular. {ECO:0000255}.; TOPO_DOM 182 224 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. {ECO:0000305|PubMed:25678664}. SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000269|PubMed:25678664}. Cell membrane {ECO:0000269|PubMed:25678664}; Multi-pass membrane protein {ECO:0000269|PubMed:25678664}. SUBUNIT: (Microbial infection) Interacts (via both extracellular domains) with Clostridium perfringens enterotoxin CPE; the interaction disrupts claudin assembly in tight junctions. {ECO:0000269|PubMed:25678664}. +Q9D7U6 CLD22_MOUSE Claudin-22 220 24,310 Chain (1); Topological domain (5); Transmembrane (4) TRANSMEM 11 31 Helical. {ECO:0000255}.; TRANSMEM 82 102 Helical. {ECO:0000255}.; TRANSMEM 121 141 Helical. {ECO:0000255}.; TRANSMEM 165 185 Helical. {ECO:0000255}. TOPO_DOM 1 10 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 32 81 Extracellular. {ECO:0000255}.; TOPO_DOM 103 120 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 142 164 Extracellular. {ECO:0000255}.; TOPO_DOM 186 220 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000250}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q9D7D7 CLD23_MOUSE Claudin-23 296 32,461 Chain (1); Topological domain (5); Transmembrane (4) TRANSMEM 3 23 Helical. {ECO:0000255}.; TRANSMEM 82 102 Helical. {ECO:0000255}.; TRANSMEM 112 132 Helical. {ECO:0000255}.; TRANSMEM 161 181 Helical. {ECO:0000255}. TOPO_DOM 1 2 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 24 81 Extracellular. {ECO:0000255}.; TOPO_DOM 103 111 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 133 160 Extracellular. {ECO:0000255}.; TOPO_DOM 182 296 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000250}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. +Q9Z0G9 CLD3_MOUSE Claudin-3 (Clostridium perfringens enterotoxin receptor 2) (CPE-R 2) (CPE-receptor 2) 219 23,285 Alternative sequence (1); Chain (1); Modified residue (2); Region (1); Topological domain (5); Transmembrane (4) TRANSMEM 9 29 Helical. {ECO:0000255}.; TRANSMEM 81 101 Helical. {ECO:0000255}.; TRANSMEM 116 136 Helical. {ECO:0000255}.; TRANSMEM 160 180 Helical. {ECO:0000255}. TOPO_DOM 1 8 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 30 80 Extracellular. {ECO:0000255}.; TOPO_DOM 102 115 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 137 159 Extracellular. {ECO:0000255}.; TOPO_DOM 181 219 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. {ECO:0000269|PubMed:10508613}. SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000269|PubMed:9892664}. Cell membrane {ECO:0000269|PubMed:9892664}; Multi-pass membrane protein {ECO:0000269|PubMed:9892664}. SUBUNIT: Can form homo- and heteropolymers with other CLDN. Homopolymers interact with CLDN1 and CLDN2 homopolymers. Directly interacts with TJP1/ZO-1, TJP2/ZO-2 and TJP3/ZO-3. {ECO:0000269|PubMed:10562289, ECO:0000269|PubMed:10601346}.; SUBUNIT: (Microbial infection) Interacts with Clostridium perfringens enterotoxin CPE; the interaction may disrupt claudin assembly in tight junctions. {ECO:0000269|PubMed:25678664}. TISSUE SPECIFICITY: Expressed at high levels in liver and lung and, at lower levels, in kidney and testis. {ECO:0000269|PubMed:9892664}. +O35054 CLD4_MOUSE Claudin-4 (Clostridium perfringens enterotoxin receptor) (CPE-R) (CPE-receptor) 210 22,339 Chain (1); Disulfide bond (1); Modified residue (1); Mutagenesis (5); Region (2); Topological domain (5); Transmembrane (4) TRANSMEM 8 28 Helical. {ECO:0000255}.; TRANSMEM 82 102 Helical. {ECO:0000255}.; TRANSMEM 117 137 Helical. {ECO:0000255}.; TRANSMEM 161 181 Helical. {ECO:0000255}. TOPO_DOM 1 7 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 29 81 Extracellular. {ECO:0000255}.; TOPO_DOM 103 116 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 138 160 Extracellular. {ECO:0000255}.; TOPO_DOM 182 210 Cytoplasmic. {ECO:0000255}. FUNCTION: Channel-forming tight junction protein that mediates paracellular chloride transport in the kidney (PubMed:20921420). Plays a critical role in the paracellular reabsorption of filtered chloride in the kidney collecting ducts (PubMed:20921420). Claudins play a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. {ECO:0000269|PubMed:20921420}. PTM: Phosphorylated. Phosphorylation by EPHA2 is stimulated by EFNA1 and alters interaction with TJP1 (By similarity). {ECO:0000250|UniProtKB:O14493}. SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000269|PubMed:20921420, ECO:0000269|PubMed:25831548, ECO:0000269|PubMed:9892664}. Cell membrane {ECO:0000269|PubMed:20921420, ECO:0000269|PubMed:9892664}; Multi-pass membrane protein {ECO:0000255}. Note=CLDN4 is required for tight junction localization in the kidney (PubMed:20921420, PubMed:25831548). {ECO:0000269|PubMed:20921420, ECO:0000269|PubMed:25831548}. SUBUNIT: Interacts with EPHA2; phosphorylates CLDN4 and may regulate tight junctions (By similarity). Directly interacts with TJP1/ZO-1, TJP2/ZO-2 and TJP3/ZO-3 (PubMed:10601346, PubMed:16236711). Interacts with CLDN1 (By similarity). Interacts with CLDN8 (PubMed:20921420). {ECO:0000250|UniProtKB:O14493, ECO:0000269|PubMed:10601346, ECO:0000269|PubMed:16236711, ECO:0000269|PubMed:20921420}. TISSUE SPECIFICITY: Expressed primarily in lung and kidney (PubMed:9892664). Present in both cortical and medullar collecting ducts (at protein level) (PubMed:20921420). {ECO:0000269|PubMed:20921420, ECO:0000269|PubMed:9892664}. +O54942 CLD5_MOUSE Claudin-5 (Brain endothelial cell clone 1 protein) (Lung-specific membrane protein) 218 23,054 Chain (1); Region (1); Sequence conflict (1); Topological domain (5); Transmembrane (4) TRANSMEM 8 28 Helical. {ECO:0000255}.; TRANSMEM 82 102 Helical. {ECO:0000255}.; TRANSMEM 124 144 Helical. {ECO:0000255}.; TRANSMEM 161 181 Helical. {ECO:0000255}. TOPO_DOM 1 7 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 29 81 Extracellular. {ECO:0000255}.; TOPO_DOM 103 123 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 145 160 Extracellular. {ECO:0000255}.; TOPO_DOM 182 218 Cytoplasmic. {ECO:0000255}. FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. {ECO:0000250}. SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000269|PubMed:9892664}. Cell membrane {ECO:0000269|PubMed:9892664}; Multi-pass membrane protein {ECO:0000269|PubMed:9892664}. SUBUNIT: Interacts with MPDZ (By similarity). Directly interacts with TJP1/ZO-1, TJP2/ZO-2 and TJP3/ZO-3. {ECO:0000250, ECO:0000269|PubMed:10601346}. TISSUE SPECIFICITY: Widely expressed with highest levels in the lung. {ECO:0000269|PubMed:9892664}. +Q9DAR1 CLF2A_MOUSE CKLF-like MARVEL transmembrane domain-containing protein 2A (Chemokine-like factor superfamily member 2A) 169 19,553 Alternative sequence (3); Chain (1); Domain (1); Transmembrane (4) TRANSMEM 40 60 Helical. {ECO:0000255}.; TRANSMEM 69 89 Helical. {ECO:0000255}.; TRANSMEM 98 118 Helical. {ECO:0000255}.; TRANSMEM 136 156 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. +Q9DAC0 CLF2B_MOUSE CKLF-like MARVEL transmembrane domain-containing protein 2B (Chemokine-like factor superfamily member 2B) 210 24,366 Chain (1); Domain (1); Transmembrane (4) TRANSMEM 35 55 Helical. {ECO:0000255}.; TRANSMEM 65 85 Helical. {ECO:0000255}.; TRANSMEM 103 123 Helical. {ECO:0000255}.; TRANSMEM 127 147 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. +P00848 ATP6_MOUSE ATP synthase subunit a (F-ATPase protein 6) 226 25,096 Chain (1); Transmembrane (6) TRANSMEM 6 26 Helical. {ECO:0000255}.; TRANSMEM 68 88 Helical. {ECO:0000255}.; TRANSMEM 97 117 Helical. {ECO:0000255}.; TRANSMEM 138 158 Helical. {ECO:0000255}.; TRANSMEM 164 184 Helical. {ECO:0000255}.; TRANSMEM 189 209 Helical. {ECO:0000255}. FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Component of an ATP synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MD and MP68 (By similarity). Interacts with DNAJC30; interaction is direct (By similarity). {ECO:0000250|UniProtKB:P00846, ECO:0000250|UniProtKB:P00847}. +Q9QYB1 CLIC4_MOUSE Chloride intracellular channel protein 4 (mc3s5/mtCLIC) 253 28,729 Chain (1); Domain (1); Initiator methionine (1); Modified residue (8); Region (1); Sequence conflict (1); Transmembrane (1) TRANSMEM 37 57 Helical; Note=After insertion into the membrane. {ECO:0000255}. FUNCTION: Can insert into membranes and form poorly selective ion channels that may also transport chloride ions. Channel activity depends on the pH. Membrane insertion seems to be redox-regulated and may occur only under oxydizing conditions. Promotes cell-surface expression of HRH3 (By similarity). May play a role in angiogenesis. {ECO:0000250, ECO:0000269|PubMed:19197003}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Nucleus {ECO:0000250}. Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Mitochondrion {ECO:0000269|PubMed:10593946, ECO:0000269|PubMed:17636002}. Note=Exists both as soluble cytoplasmic protein and as membrane protein with probably a single transmembrane domain. Present in an intracellular vesicular compartment that likely represent trans-Golgi network vesicles (By similarity). {ECO:0000250}. SUBUNIT: Monomer. Interacts with HRH30. Interacts with AKAP9 (By similarity). {ECO:0000250}. DOMAIN: Members of this family may change from a globular, soluble state to a state where the N-terminal domain is inserted into the membrane and functions as chloride channel. A conformation change of the N-terminal domain is thought to expose hydrophobic surfaces that trigger membrane insertion (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Detected in blood vessels in the retina (at protein level). Expressed to the greatest extent in vivo in heart, lung, liver, kidney, and skin. {ECO:0000269|PubMed:10593946, ECO:0000269|PubMed:17636002, ECO:0000269|PubMed:19197003}. +Q9Z0H8 CLIP2_MOUSE CAP-Gly domain-containing linker protein 2 (Cytoplasmic linker protein 115) (CLIP-115) (Cytoplasmic linker protein 2) 1047 115,910 Alternative sequence (1); Chain (1); Coiled coil (3); Compositional bias (1); Domain (2); Modified residue (8); Sequence conflict (19) FUNCTION: Seems to link microtubules to dendritic lamellar body (DLB), a membranous organelle predominantly present in bulbous dendritic appendages of neurons linked by dendrodendritic gap junctions. May operate in the control of brain-specific organelle translocations (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O55156}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16954346}. Note=Localizes preferentially to the ends of tyrosinated microtubules. {ECO:0000269|PubMed:16954346}. SUBUNIT: Interacts with CLASP1 and CLASP2 (PubMed:11290329). Binds preferentially to tyrosinated microtubules, and only marginally to detyrosinated microtubules (PubMed:16954346). {ECO:0000269|PubMed:11290329, ECO:0000269|PubMed:16954346}. TISSUE SPECIFICITY: Expressed in the brain, and very low levels in kidneys. {ECO:0000269|PubMed:9427243}. +Q8CI96 CLIP4_MOUSE CAP-Gly domain-containing linker protein 4 (Restin-like protein 2) 704 75,789 Alternative sequence (4); Beta strand (14); Chain (1); Compositional bias (1); Domain (3); Helix (3); Modified residue (2); Repeat (3); Sequence conflict (4); Turn (2) +O35492 CLK3_MOUSE Dual specificity protein kinase CLK3 (EC 2.7.12.1) (CDC-like kinase 3) 638 73,798 Active site (1); Binding site (1); Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (6); Frameshift (1); Modified residue (8); Nucleotide binding (1); Sequence conflict (4) FUNCTION: Dual specificity kinase acting on both serine/threonine and tyrosine-containing substrates. Phosphorylates serine- and arginine-rich (SR) proteins of the spliceosomal complex. May be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing and can cause redistribution of SR proteins from speckles to a diffuse nucleoplasmic distribution. Phosphorylates SRSF1 and SRSF3. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells. {ECO:0000269|PubMed:9307018}. PTM: Autophosphorylates on all three types of residues. {ECO:0000269|PubMed:9307018}. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasmic vesicle, secretory vesicle, acrosome. TISSUE SPECIFICITY: Present at high levels in testis and ovary. In testis, expression is restricted to elongated, maturing spermatozoa. Also present in spleen, brain, lung and liver (at protein level). {ECO:0000269|PubMed:10585269}. +Q6SJQ0 CLM8_MOUSE CMRF35-like molecule 8 (CLM-8) (CD300 antigen-like family member A) (Leukocyte mono-Ig-like receptor 1) (Mast cell-derived paired immunoglobulin-like receptor 1) (Myeloid-associated immunoglobulin-like receptor 1) (MAIR-1) (MAIR-I) (CD antigen CD300a) 318 35,629 Alternative sequence (1); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (1); Modified residue (1); Mutagenesis (1); Sequence conflict (9); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 186 206 Helical. {ECO:0000255}. TOPO_DOM 28 185 Extracellular. {ECO:0000255}.; TOPO_DOM 207 318 Cytoplasmic. {ECO:0000255}. FUNCTION: Inhibitory receptor which may contribute to the down-regulation of cytolytic activity in natural killer (NK) cells, and to the down-regulation of mast cell degranulation (PubMed:12874256, PubMed:12893283, PubMed:16339535). Negatively regulates the Toll-like receptor (TLR) signaling mediated by MYD88 but not TRIF through activation of PTPN6 (By similarity). {ECO:0000250|UniProtKB:Q9UGN4, ECO:0000269|PubMed:12874256, ECO:0000269|PubMed:12893283, ECO:0000269|PubMed:16339535}. PTM: Phosphorylated on tyrosine. {ECO:0000269|PubMed:12874256, ECO:0000269|PubMed:12893283}.; PTM: N-glycosylated. {ECO:0000269|PubMed:12874256}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12874256, ECO:0000269|PubMed:12893283}; Single-pass type I membrane protein {ECO:0000269|PubMed:12874256, ECO:0000269|PubMed:12893283}. SUBUNIT: Upon tyrosine-phosphorylation, interacts with PTN6/SHP-1 and PTPN11/SHP-2 and INPP5D. {ECO:0000269|PubMed:12893283}. TISSUE SPECIFICITY: Present on the surface of the majority of myeloid cells and a subset of B-cells. Present on the surface of NK cells after IL-12 stimulation. {ECO:0000269|PubMed:12874256, ECO:0000269|PubMed:12893283, ECO:0000269|PubMed:16339535}. +Q8C5W0 CLMN_MOUSE Calmin (Calponin-like transmembrane domain protein) 1052 117,227 Alternative sequence (5); Chain (1); Domain (2); Modified residue (6); Region (1); Sequence conflict (2); Transmembrane (1) TRANSMEM 1027 1047 Helical; Anchor for type IV membrane protein. {ECO:0000255}. SUBCELLULAR LOCATION: Isoform 1: Membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}. Note=Shows a reticular pattern in the cytoplasm.; SUBCELLULAR LOCATION: Isoform 4: Membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}. Note=Shows a reticular pattern in the cytoplasm.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm.; SUBCELLULAR LOCATION: Isoform 3: Cytoplasm. TISSUE SPECIFICITY: Expressed in testis. Expressed during testis maturation process and in maturing spermatids. In brain, it is expressed in neurons of the hippocampus, cerebral cortex, and thalamus, Purkinje cells, and also in the choroid plexus and ependymal cells. Expressed predominantly in dendrites and cell bodies of the neurons, but not in axons. The level of expression increases during the period of maturation of the mouse brain after birth. {ECO:0000269|PubMed:11386753, ECO:0000269|PubMed:12670712}. +Q7TSN2 CLM_MOUSE CMRF35-like molecule (CLM) (Dendritic cell-derived Ig-like receptor 1) (DIgR1) (Immunoglobulin superfamily member 7) (IgSF7) (Leukocyte mono-Ig-like receptor 2) (Myeloid-associated immunoglobulin-like receptor 2) (MAIR-2) (MAIR-II) 230 25,402 Alternative sequence (1); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (1); Mutagenesis (1); Sequence conflict (6); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 190 210 Helical. {ECO:0000255}. TOPO_DOM 25 189 Extracellular. {ECO:0000255}.; TOPO_DOM 211 230 Cytoplasmic. {ECO:0000255}. FUNCTION: Acts as an activating receptor in mast cells and macrophages. {ECO:0000269|PubMed:12874256, ECO:0000269|PubMed:12893283, ECO:0000269|PubMed:17202337}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11549249, ECO:0000269|PubMed:12893283}; Single-pass type I membrane protein {ECO:0000269|PubMed:11549249, ECO:0000269|PubMed:12893283}. SUBUNIT: Interacts with TYROBP, HCST and FcR gamma. {ECO:0000269|PubMed:12874256, ECO:0000269|PubMed:12893283, ECO:0000269|PubMed:17202337}. TISSUE SPECIFICITY: Present on the surface of mast cells, dendritic cells, peritoneal macrophages and a subset of B-cells (at protein level). {ECO:0000269|PubMed:11549249, ECO:0000269|PubMed:12874256, ECO:0000269|PubMed:12893283}. +O70228 ATP9A_MOUSE Probable phospholipid-transporting ATPase IIA (EC 7.6.2.1) (ATPase class II type 9A) 1047 118,609 Active site (1); Chain (1); Initiator methionine (1); Metal binding (2); Modified residue (1); Sequence conflict (17); Topological domain (11); Transmembrane (10) TRANSMEM 70 91 Helical. {ECO:0000255}.; TRANSMEM 97 119 Helical. {ECO:0000255}.; TRANSMEM 304 325 Helical. {ECO:0000255}.; TRANSMEM 333 354 Helical. {ECO:0000255}.; TRANSMEM 842 862 Helical. {ECO:0000255}.; TRANSMEM 875 893 Helical. {ECO:0000255}.; TRANSMEM 924 942 Helical. {ECO:0000255}.; TRANSMEM 950 972 Helical. {ECO:0000255}.; TRANSMEM 979 999 Helical. {ECO:0000255}.; TRANSMEM 1007 1030 Helical. {ECO:0000255}. TOPO_DOM 2 69 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 92 96 Extracellular. {ECO:0000255}.; TOPO_DOM 120 303 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 326 332 Extracellular. {ECO:0000255}.; TOPO_DOM 355 841 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 863 874 Extracellular. {ECO:0000255}.; TOPO_DOM 894 923 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 943 949 Extracellular. {ECO:0000255}.; TOPO_DOM 973 978 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1000 1006 Extracellular. {ECO:0000255}.; TOPO_DOM 1031 1047 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Recycling endosome {ECO:0000250}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250}. TISSUE SPECIFICITY: Found in most tissues except spleen. Most abundant in brain. Also detected in fetal tissues. +P98195 ATP9B_MOUSE Probable phospholipid-transporting ATPase IIB (EC 7.6.2.1) (ATPase class II type 9B) 1146 129,017 Active site (1); Alternative sequence (1); Chain (1); Metal binding (2); Sequence conflict (2); Topological domain (11); Transmembrane (10) TRANSMEM 144 164 Helical. {ECO:0000255}.; TRANSMEM 173 193 Helical. {ECO:0000255}.; TRANSMEM 382 402 Helical. {ECO:0000255}.; TRANSMEM 408 427 Helical. {ECO:0000255}.; TRANSMEM 939 959 Helical. {ECO:0000255}.; TRANSMEM 962 982 Helical. {ECO:0000255}.; TRANSMEM 1012 1032 Helical. {ECO:0000255}.; TRANSMEM 1041 1061 Helical. {ECO:0000255}.; TRANSMEM 1066 1086 Helical. {ECO:0000255}.; TRANSMEM 1106 1128 Helical. {ECO:0000255}. TOPO_DOM 1 143 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 165 172 Extracellular. {ECO:0000255}.; TOPO_DOM 194 381 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 403 407 Extracellular. {ECO:0000255}.; TOPO_DOM 428 938 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 960 961 Extracellular. {ECO:0000255}.; TOPO_DOM 983 1011 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1033 1040 Extracellular. {ECO:0000255}.; TOPO_DOM 1062 1065 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 1087 1105 Extracellular. {ECO:0000255}.; TOPO_DOM 1129 1146 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. TISSUE SPECIFICITY: Found in most tissues except spleen and muscle. Most abundant in testis. Also detected in fetal tissues. +Q80VC9 CAMP3_MOUSE Calmodulin-regulated spectrin-associated protein 3 (Marshalin) (Protein Nezha) 1252 135,175 Alternative sequence (6); Beta strand (8); Chain (1); Coiled coil (3); Compositional bias (2); Domain (2); Helix (4); Modified residue (17); Mutagenesis (1); Sequence conflict (2); Turn (3) FUNCTION: Key microtubule-organizing protein that specifically binds the minus-end of non-centrosomal microtubules and regulates their dynamics and organization (PubMed:23169647, PubMed:24706919, PubMed:26715742). Specifically recognizes growing microtubule minus-ends and autonomously decorates and stabilizes microtubule lattice formed by microtubule minus-end polymerization (PubMed:24706919). Acts on free microtubule minus-ends that are not capped by microtubule-nucleating proteins or other factors and protects microtubule minus-ends from depolymerization (PubMed:24706919). In addition, it also reduces the velocity of microtubule polymerization (PubMed:24706919). Required for the biogenesis and the maintenance of zonula adherens by anchoring the minus-end of microtubules to zonula adherens and by recruiting the kinesin KIFC3 to those junctional sites (By similarity). Required for orienting the apical-to-basal polarity of microtubules in epithelial cells: acts by tethering non-centrosomal microtubules to the apical cortex, leading to their longitudinal orientation (PubMed:26715742). Plays a key role in early embryos, which lack centrosomes: accumulates at the microtubule bridges that connect pairs of cells and enables the formation of a non-centrosomal microtubule-organizing center that directs intracellular transport in the early embryo (PubMed:28860385). Couples non-centrosomal microtubules with actin: interaction with MACF1 at the minus ends of non-centrosomal microtubules, tethers the microtubules to actin filaments, regulating focal adhesion size and cell migration (By similarity). Plays a key role in the generation of non-centrosomal microtubules by accumulating in the pericentrosomal region and cooperating with KATNA1 to release non-centrosomal microtubules from the centrosome (By similarity). Through the microtubule cytoskeleton, also regulates the organization of cellular organelles including the Golgi and the early endosomes (By similarity). Through the microtubule cytoskeleton, also regulates the organization of cellular organelles including the Golgi and the early endosomes (By similarity). Through interaction with AKAP9, involved in translocation of Golgi vesicles in epithelial cells, where microtubules are mainly non-centrosomal (By similarity). {ECO:0000250|UniProtKB:Q9P1Y5, ECO:0000269|PubMed:23169647, ECO:0000269|PubMed:24706919, ECO:0000269|PubMed:26715742, ECO:0000269|PubMed:28860385}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:24244856, ECO:0000269|PubMed:24706919, ECO:0000269|PubMed:26715742, ECO:0000269|PubMed:28860385}. Cell junction, adherens junction {ECO:0000250|UniProtKB:Q9P1Y5}. Cytoplasm {ECO:0000250|UniProtKB:Q9P1Y5}. Note=Scattered in the cytoplasm, associated with the minus-end of microtubules and also detected at the centrosomes (PubMed:24706919, PubMed:26715742). Decorates the minus-end of microtubules by decreasing the rate of tubulin incorporation and remaining bound (By similarity). Localizes along zonula adherens only at mature cell-cell contacts (By similarity). In early embryos, accumulates at the microtubule bridges that connect pairs of cells: this structure is present in early embryos, which lack centrosomes (PubMed:28860385). This cytokinetic bridge does not undergo stereotypical abscission after cell division (PubMed:28860385). Accumulates to the pericentrosomal region following interaction with KATNA1 (By similarity). {ECO:0000250|UniProtKB:Q9P1Y5, ECO:0000269|PubMed:28860385}. SUBUNIT: Interacts with PLEKHA7 (By similarity). Interacts with CAMSAP2 (PubMed:23169647). Interacts with KATNA1 and KATNB1; leading to regulate the length of CAMSAP3-decorated microtubule stretches (By similarity). Interacts with AKAP9; regulating Golgi assembly in epithelial cells (By similarity). Interacts with MACF1 (By similarity). Interacts with isoform C of CDH23; leading to inhibit CAMSAP3 ability to induce microtubule bundle formation (PubMed:27349180). {ECO:0000250|UniProtKB:Q9P1Y5, ECO:0000269|PubMed:23169647, ECO:0000269|PubMed:27349180}. DOMAIN: The CKK domain binds microtubules and specifically recognizes the minus-end of microtubules. {ECO:0000250|UniProtKB:Q9P1Y5, ECO:0000255|PROSITE-ProRule:PRU00841}. TISSUE SPECIFICITY: In cochlea, restricted to the organ of Corti and increases during development (at protein level) (PubMed:24244856). Highly expressed in both sensory hair cells and supporting cells (PubMed:24244856). {ECO:0000269|PubMed:24244856}. +Q80TJ1 CAPS1_MOUSE Calcium-dependent secretion activator 1 (Calcium-dependent activator protein for secretion 1) (CAPS-1) 1355 153,113 Alternative sequence (4); Chain (1); Domain (3); Erroneous initiation (1); Modified residue (4); Region (2); Sequence caution (1); Sequence conflict (7) FUNCTION: Calcium-binding protein involved in exocytosis of vesicles filled with neurotransmitters and neuropeptides. Probably acts upstream of fusion in the biogenesis or maintenance of mature secretory vesicles. Regulates catecholamine loading of DCVs. May specifically mediate the Ca(2+)-dependent exocytosis of large dense-core vesicles (DCVs) and other dense-core vesicles by acting as a PtdIns(4,5)P2-binding protein that acts at prefusion step following ATP-dependent priming and participates in DCVs-membrane fusion. However, it may also participate in small clear synaptic vesicles (SVs) exocytosis and it is unclear whether its function is related to Ca(2+) triggering (By similarity). {ECO:0000250, ECO:0000269|PubMed:15820695}. SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell junction, synapse {ECO:0000250}. Note=Membrane-associated to vesicles. Strongly enriched in synaptic fractions. May preferentially binds to DCVs but not to SVs. Probably localizes to different vesicles compared to CADPS2. Binds phosphoinosides, with a strong selectivity for PtdIns(4,5)P2 over PtdIns(3,4,5)P3. {ECO:0000269|PubMed:14530279, ECO:0000269|PubMed:15820695}. SUBUNIT: Homodimer. Interacts with the dopamine receptor DRD2 (By similarity). Interacts with RASL10B. {ECO:0000250, ECO:0000269|PubMed:17984325}. DOMAIN: The PH domain is essential for regulated exocytosis and binds phospholipids and plasma membrane. It however does not mediate binding to DCVs (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Present in brain and adrenal glands (at protein level). Specifically expressed in neural and endocrine secretory tissues. Strongly expressed in almost all nerve cells of the brain, although it is absent from glial cells. Expressed in the cardiac atria, but not ventricles. {ECO:0000269|PubMed:14530279, ECO:0000269|PubMed:15820695, ECO:0000269|PubMed:17984325}. +P06796 CASK_MOUSE Kappa-casein 181 20,030 Chain (1); Glycosylation (4); Modified residue (3); Sequence conflict (1); Signal peptide (1); Site (1) FUNCTION: Kappa-casein stabilizes micelle formation, preventing casein precipitation in milk. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Mammary gland specific. Secreted in milk. +O08738 CASP6_MOUSE Caspase-6 (CASP-6) (EC 3.4.22.59) (Apoptotic protease Mch-2) [Cleaved into: Caspase-6 subunit p18; Caspase-6 subunit p11] 276 31,595 Active site (2); Chain (2); Modified residue (2); Propeptide (2) FUNCTION: Involved in the activation cascade of caspases responsible for apoptosis execution. Cleaves poly(ADP-ribose) polymerase in vitro, as well as lamins. Overexpression promotes programmed cell death (By similarity). {ECO:0000250}. PTM: Cleavages by caspase-3, caspase-8 or -10 generate the two active subunits. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm. SUBUNIT: Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a 18 kDa (p18) and a 11 kDa (p11) subunit. Interacts with BIRC6/bruce. {ECO:0000250}. TISSUE SPECIFICITY: Highly expressed in lung, liver, kidney, testis, and heart. Lower levels in spleen, skeletal muscle and brain. +P56203 CATW_MOUSE Cathepsin W (EC 3.4.22.-) (Lymphopain) 371 42,120 Active site (3); Chain (1); Disulfide bond (3); Glycosylation (4); Propeptide (1); Signal peptide (1) FUNCTION: May have a specific function in the mechanism or regulation of T-cell cytolytic activity. {ECO:0000250}. +Q9JL96 CATM_MOUSE Cathepsin M (EC 3.4.22.-) 333 37,409 Active site (3); Chain (1); Disulfide bond (3); Glycosylation (3); Natural variant (1); Propeptide (1); Sequence conflict (5); Signal peptide (1) SUBCELLULAR LOCATION: Lysosome {ECO:0000305}. TISSUE SPECIFICITY: Placenta. {ECO:0000269|PubMed:10760593}. +A2AMM0 CAVN4_MOUSE Caveolae-associated protein 4 (Muscle-related coiled-coil protein) (Muscle-restricted coiled-coil protein) 362 41,008 Chain (1); Coiled coil (1); Erroneous initiation (1); Frameshift (1); Modified residue (6); Sequence conflict (1) FUNCTION: Modulates the morphology of formed caveolae in cardiomyocytes, but is not required for caveolar formation. Facilitates the recruitment of MAPK1/3 to caveolae within cardiomyocytes and regulates alpha-1 adrenergic receptor-induced hypertrophic responses in cardiomyocytes through MAPK1/3 activation (PubMed:24567387). Contributes to proper membrane localization and stabilization of caveolin-3 (CAV3) in cardiomyocytes (PubMed:26497963). Induces RHOA activation and activates NPPA transcription and myofibrillar organization through the Rho/ROCK signaling pathway (PubMed:18332105). {ECO:0000269|PubMed:18332105, ECO:0000269|PubMed:24567387, ECO:0000269|PubMed:26497963}. SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere {ECO:0000269|PubMed:18332105}. Cytoplasm {ECO:0000269|PubMed:18332105}. Cytoplasm, cytosol {ECO:0000269|PubMed:19546242}. Membrane, caveola {ECO:0000269|PubMed:19546242, ECO:0000269|PubMed:24567387}. Cell membrane, sarcolemma {ECO:0000269|PubMed:19546242}. Cell membrane {ECO:0000269|PubMed:26497963}. Note=In cardiomyocytes, accumulates in the Z-line of the sarcomere. In vascular smooth muscle cells, detected diffusely throughout the cytoplasm (PubMed:18332105). Localizes in the caveolae in a caveolin-dependent manner (PubMed:19546242). {ECO:0000269|PubMed:18332105, ECO:0000269|PubMed:19546242}. SUBUNIT: Component of the CAVIN complex composed of CAVIN1, CAVIN2, CAVIN3 and CAVIN4. Interacts with CAVIN1 (PubMed:19546242). Interacts with CAVIN2; this augments the transactivation of NPPA. Interacts with CAV3, ADRA1A, ADRA1B, MAPK1 and MAPK3 (By similarity). {ECO:0000250|UniProtKB:B1PRL5, ECO:0000250|UniProtKB:Q5BKX8, ECO:0000269|PubMed:19546242}. DOMAIN: The coiled coil domain (residues 44-77) is essential for membrane-targeting in cardiomyocytes. {ECO:0000250|UniProtKB:Q5BKX8}. TISSUE SPECIFICITY: Abundantly expressed in cardiac and skeletal muscle (at protein level). Weaker expression in aorta and lung. In heart, expressed in cardiomyocytes and vascular smooth muscle cells but not in other surrounding cells including vascular endothelial cells. {ECO:0000269|PubMed:18332105, ECO:0000269|PubMed:19546242}. +O08736 CASPC_MOUSE Caspase-12 (CASP-12) (EC 3.4.22.-) 419 47,854 Active site (2); Chain (1); Domain (1); Modified residue (1); Propeptide (1) FUNCTION: Involved in the activation cascade of caspases responsible for apoptosis execution. {ECO:0000250}. SUBUNIT: Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by two subunits (Potential). Interacts with TRAF2 under resting conditions; this interaction is reduced in ER stress conditions. {ECO:0000269|PubMed:11278723, ECO:0000305}. TISSUE SPECIFICITY: Mainly expressed in skeletal muscle and lung. +Q8BUG5 CAYP2_MOUSE Calcyphosin-2 (Calcyphosine-2) 550 62,726 Alternative sequence (2); Calcium binding (2); Chain (1); Domain (3); Sequence conflict (3) +O09161 CASQ2_MOUSE Calsequestrin-2 (Calsequestrin, cardiac muscle isoform) 415 48,176 Chain (1); Compositional bias (1); Glycosylation (1); Modified residue (1); Mutagenesis (1); Sequence conflict (3); Signal peptide (1) FUNCTION: Calsequestrin is a high-capacity, moderate affinity, calcium-binding protein and thus acts as an internal calcium store in muscle. Calcium ions are bound by clusters of acidic residues at the protein surface, especially at the interface between subunits. Can bind around 60 Ca(2+) ions. Regulates the release of lumenal Ca(2+) via the calcium release channel RYR2; this plays an important role in triggering muscle contraction. Plays a role in excitation-contraction coupling in the heart and in regulating the rate of heart beats. {ECO:0000269|PubMed:16932808, ECO:0000269|PubMed:17607358, ECO:0000269|PubMed:19920148}. PTM: Phosphorylation in the C-terminus moderately increases calcium buffering capacity. {ECO:0000250|UniProtKB:O14958}.; PTM: N-glycosylated. {ECO:0000250|UniProtKB:O14958}. SUBCELLULAR LOCATION: Sarcoplasmic reticulum lumen {ECO:0000269|PubMed:16932808, ECO:0000269|PubMed:19920148}. Note=This isoform of calsequestrin occurs in the sarcoplasmic reticulum's terminal cisternae luminal spaces of cardiac and slow skeletal muscle cells. {ECO:0000269|PubMed:16932808, ECO:0000269|PubMed:19920148}. SUBUNIT: Monomer, homodimer and homooligomer. Mostly monomeric in the absence of calcium. Forms higher oligomers in a calcium-dependent manner. Dimers associate to form tetramers, that then form linear homopolymer chains. Interacts with ASPH and TRDN (By similarity). {ECO:0000250|UniProtKB:O14958}. TISSUE SPECIFICITY: Detected in heart (at protein level). Detected in heart. {ECO:0000269|PubMed:16932808, ECO:0000269|PubMed:19920148, ECO:0000269|PubMed:9795116}. +Q9CYS6 CB072_MOUSE Uncharacterized protein C2orf72 homolog 286 30,320 Alternative sequence (1); Chain (1); Erroneous initiation (1) +Q9CRW3 CB076_MOUSE UPF0538 protein C2orf76 homolog 126 14,588 Alternative sequence (1); Chain (1) +Q9QY96 CASR_MOUSE Extracellular calcium-sensing receptor (CaSR) (Parathyroid cell calcium-sensing receptor) (PCaR1) 1079 120,903 Alternative sequence (1); Binding site (4); Chain (1); Disulfide bond (10); Glycosylation (10); Metal binding (9); Modified residue (2); Region (6); Sequence conflict (17); Signal peptide (1); Topological domain (8); Transmembrane (7) TRANSMEM 613 635 Helical; Name=1. {ECO:0000255}.; TRANSMEM 650 670 Helical; Name=2. {ECO:0000255}.; TRANSMEM 682 700 Helical; Name=3. {ECO:0000255}.; TRANSMEM 725 745 Helical; Name=4. {ECO:0000255}.; TRANSMEM 770 792 Helical; Name=5. {ECO:0000255}.; TRANSMEM 806 828 Helical; Name=6. {ECO:0000255}.; TRANSMEM 837 862 Helical; Name=7. {ECO:0000255}. TOPO_DOM 20 612 Extracellular. {ECO:0000255}.; TOPO_DOM 636 649 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 671 681 Extracellular. {ECO:0000255}.; TOPO_DOM 701 724 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 746 769 Extracellular. {ECO:0000255}.; TOPO_DOM 793 805 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 829 836 Extracellular. {ECO:0000255}.; TOPO_DOM 863 1079 Cytoplasmic. {ECO:0000255}. FUNCTION: G-protein-coupled receptor that senses changes in the extracellular concentration of calcium ions and plays a key role in maintaining calcium homeostasis (By similarity). Senses fluctuations in the circulating calcium concentration and modulates the production of parathyroid hormone (PTH) in parathyroid glands (PubMed:7493018). The activity of this receptor is mediated by a G-protein that activates a phosphatidylinositol-calcium second messenger system (By similarity). The G-protein-coupled receptor activity is activated by a co-agonist mechanism: aromatic amino acids, such as Trp or Phe, act concertedly with divalent cations, such as calcium or magnesium, to achieve full receptor activation (By similarity). {ECO:0000250|UniProtKB:P41180, ECO:0000269|PubMed:7493018}. PTM: N-glycosylated. {ECO:0000250|UniProtKB:P41180}.; PTM: Ubiquitinated by RNF19A; which induces proteasomal degradation. {ECO:0000250|UniProtKB:P41180}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P41180}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P41180}. SUBUNIT: Homodimer; disulfide-linked. Interacts with VCP and RNF19A (By similarity). Interacts with ARRB1 (By similarity). {ECO:0000250|UniProtKB:P41180, ECO:0000250|UniProtKB:P48442}. DOMAIN: The extracellular regions of the homodimer interact in a side-by-side fashion while facing opposite directions. Each extracellular region consists of three domains, LB1 (ligand-binding 1), LB2 and CR (cysteine-rich). The two lobe-shaped domains LB1 and LB2 form a venus flytrap module. In the inactive configuration, the venus flytrap modules of both protomers are in the open conformation associated with the resting state (open-open) and the interdomain cleft is empty. In addition, each protomer contains three anions, which reinforce the inactive conformation, and one calcium ion. In the active configuration, both protomers of extracellular regions have the closed conformation associated with agonist-binding (closed-closed). The ligand-binding cleft of each protomer is solely occupied by an aromatic amino-acid. Calcium is bound at four novel sites, including one at the homodimer interface. Agonist-binding induces large conformational changes within the extracellular region homodimer: first, the venus flytrap module of each protomer undergoes domain closure. Second, the LB2 regions of the two protomers approach each other, resulting in an expansion of the homodimer interactions involving LB2 domains. Third, the CR regions of the two subunits interact to form a large homodimer interface that is unique to the active state. The CR regions are brought into close contact by the motion involving LB2 since the two domains are rigidly associated within each subunit. {ECO:0000250|UniProtKB:P41180}. TISSUE SPECIFICITY: Epidermis, kidney and cartilage. {ECO:0000269|PubMed:10579354, ECO:0000269|PubMed:10625662, ECO:0000269|PubMed:10652312, ECO:0000269|PubMed:9076582}. +Q5NCY3 CB5D1_MOUSE Cytochrome b5 domain-containing protein 1 228 26,719 Alternative sequence (2); Chain (1); Compositional bias (1); Domain (1); Metal binding (1) +Q8R4H4 CBPA5_MOUSE Carboxypeptidase A5 (EC 3.4.17.-) 436 49,151 Active site (1); Binding site (2); Chain (1); Disulfide bond (1); Metal binding (3); Propeptide (1); Region (3); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000250}. TISSUE SPECIFICITY: Detected in testis germ cells. {ECO:0000269|PubMed:11836249}. +Q9CVN6 CBY3_MOUSE Protein chibby homolog 3 235 26,690 Chain (1); Erroneous gene model prediction (1); Sequence conflict (1) +Q9JHH6 CBPB2_MOUSE Carboxypeptidase B2 (EC 3.4.17.20) (Carboxypeptidase R) (CPR) (Carboxypeptidase U) (CPU) (Thrombin-activable fibrinolysis inhibitor) (TAFI) 422 48,871 Active site (1); Binding site (2); Chain (1); Disulfide bond (3); Glycosylation (6); Metal binding (3); Propeptide (1); Region (3); Sequence conflict (3); Signal peptide (1); Site (1) FUNCTION: Cleaves C-terminal arginine or lysine residues from biologically active peptides such as kinins or anaphylatoxins in the circulation thereby regulating their activities. Down-regulates fibrinolysis by removing C-terminal lysine residues from fibrin that has already been partially degraded by plasmin. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10739389}. TISSUE SPECIFICITY: Plasma; synthesized in the liver. {ECO:0000269|PubMed:10739389}. +O89001 CBPD_MOUSE Carboxypeptidase D (EC 3.4.17.22) (Metallocarboxypeptidase D) (gp180) 1377 152,406 Active site (1); Chain (1); Glycosylation (15); Lipidation (3); Metal binding (6); Modified residue (6); Motif (1); Region (3); Sequence conflict (2); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 1297 1317 Helical. {ECO:0000255}. TOPO_DOM 38 1296 Extracellular. {ECO:0000255}.; TOPO_DOM 1318 1377 Cytoplasmic. {ECO:0000255}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q90240}; Single-pass type I membrane protein {ECO:0000255}. DOMAIN: There are 3 carboxypeptidase-like domains. Only the first two domains seem to have kept a catalytic activity. +Q8CDN1 CC020_MOUSE Uncharacterized protein C3orf20 homolog 933 104,228 Chain (1); Transmembrane (1) TRANSMEM 771 791 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +Q8C5T8 CC113_MOUSE Coiled-coil domain-containing protein 113 377 44,215 Chain (1); Coiled coil (2) FUNCTION: Component of centriolar satellites contributing to primary cilium formation. {ECO:0000250|UniProtKB:Q9H0I3}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000250|UniProtKB:Q9H0I3}. Note=Colocalized with HAP1 at centriolar satellites. Centriolar satellite localization requires PCM1. {ECO:0000250|UniProtKB:Q9H0I3}. SUBUNIT: Interacts with HAP1 AND PCM1. {ECO:0000250|UniProtKB:Q9H0I3}. +Q6P5U8 CC148_MOUSE Coiled-coil domain-containing protein 148 527 63,396 Alternative sequence (2); Chain (1); Coiled coil (2); Compositional bias (1) +Q91WT9 CBS_MOUSE Cystathionine beta-synthase (EC 4.2.1.22) (Beta-thionase) (Serine sulfhydrase) 561 61,544 Alternative sequence (1); Binding site (2); Chain (1); Cross-link (1); Domain (1); Metal binding (2); Modified residue (2); Region (1) Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-homocysteine and L-serine: step 1/2. FUNCTION: Hydro-lyase catalyzing the first step of the transsulfuration pathway, where the hydroxyl group of L-serine is displaced by L-homocysteine in a beta-replacement reaction to form L-cystathionine, the precursor of L-cysteine. This catabolic route allows the elimination of L-methionine and the toxic metabolite L-homocysteine (By similarity). Also involved in the production of hydrogen sulfide, a gasotransmitter with signaling and cytoprotective effects on neurons (By similarity). {ECO:0000250|UniProtKB:P32232, ECO:0000250|UniProtKB:P35520}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P35520}. Nucleus {ECO:0000250|UniProtKB:P35520}. SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P35520}. +P23198 CBX3_MOUSE Chromobox protein homolog 3 (Heterochromatin protein 1 homolog gamma) (HP1 gamma) (M32) (Modifier 2 protein) 183 20,855 Chain (1); Cross-link (5); Domain (2); Initiator methionine (1); Modified residue (10) FUNCTION: Component of heterochromatin. Recognizes and binds histone H3 tails methylated at 'Lys-9', leading to epigenetic repression. Probably involved in the repression of many genes located in euchromatin, such as E2F1, MYC and CDC25A. Involved in the formation of functional kinetochore through interaction with MIS12 complex proteins. Contributes to the conversion of local chromatin to a heterochromatin-like repressive state through H3 'Lys-9' trimethylation, mediates the recruitment of the methyltransferases SUV39H1 and/or SUV39H2 by the PER complex to the E-box elements of the circadian target genes such as PER2 itself or PER1 (PubMed:24413057). Mediates the recruitement of NIPBL to sites of DNA damage at double-strand breaks (DSBs) (By similarity). {ECO:0000250|UniProtKB:Q13185, ECO:0000269|PubMed:24413057}. PTM: Phosphorylated by PIM1. Phosphorylated during interphase and possibly hyper-phosphorylated during mitosis (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8751383}. Note=May be associated with microtubules and mitotic poles during mitosis (Potential). Associates with euchromatin and is largely excluded from constitutive heterochromatin. {ECO:0000305}. SUBUNIT: Binds directly to CHAF1A. Interacts with histone H3 methylated at 'Lys-9' (By similarity). Part of the E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1, RING1, RNF2, MBLR, L3MBTL2 and YAF2 (By similarity). Interacts with LBR, INCENP, TRIM28/TIF1B and SP100 (By similarity). Interacts with TIF1/TIF1A (PubMed:8978696). Interacts with MIS12 and DSN1 (By similarity). Can interact directly with CBX5 via the chromoshadow domain (By similarity). Interacts with KMT5B and KMT5C (PubMed:15145825). Interacts with POGZ (By similarity). Interacts with CHAMP1 (By similarity). The large PER complex involved in the histone methylation is composed of at least PER2, CBX3, TRIM28, SUV39H1 and/or SUV39H2; CBX3 mediates the formation of the complex (PubMed:24413057). Interacts with INCENP (By similarity). Interacts with NIPBL (via PxVxL motif) (By similarity). Interacts with LRIF1 (via PxVxL motif) (By similarity). {ECO:0000250|UniProtKB:Q13185, ECO:0000269|PubMed:15145825, ECO:0000269|PubMed:24413057, ECO:0000269|PubMed:8978696}. +Q8R344 CCD12_MOUSE Coiled-coil domain-containing protein 12 166 18,891 Chain (1); Coiled coil (2); Cross-link (1); Modified residue (4); Sequence conflict (2) +Q3ULM0 CC106_MOUSE Coiled-coil domain-containing protein 106 279 32,098 Alternative sequence (2); Chain (1); Coiled coil (1); Modified residue (1); Motif (1); Sequence conflict (2) FUNCTION: Promotes the degradation of p53/TP53 protein and inhibits its transactivity. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Colocalizes with p53/TP53. {ECO:0000250}. SUBUNIT: Interacts with p53/TP53. {ECO:0000250}. +Q9D5W4 CCD81_MOUSE Coiled-coil domain-containing protein 81 654 75,826 Chain (1); Coiled coil (1); Modified residue (5) SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q6ZN84}. +Q9D541 CCDC7_MOUSE Coiled-coil domain-containing protein 7 (Protein BIOT2) 371 42,515 Chain (1); Coiled coil (1) FUNCTION: May play a role in tumorigenesis. {ECO:0000269|PubMed:19277478}. TISSUE SPECIFICITY: Exclusively expressed in the testes. Abundantly expressed in mouse cancer cell line derived from epithelial cells. {ECO:0000269|PubMed:19277478}. +Q8BI79 CCD40_MOUSE Coiled-coil domain-containing protein 40 (Protein links) 1192 136,772 Alternative sequence (5); Chain (1); Coiled coil (7); Erroneous initiation (1); Modified residue (1); Sequence conflict (7) FUNCTION: Required for assembly of dynein regulatory complex (DRC) and inner dynein arm (IDA) complexes, which are responsible for ciliary beat regulation, thereby playing a central role in motility in cilia and flagella. Probably acts together with CCDC39 to form a molecular ruler that determines the 96 nanometer (nm) repeat length and arrangements of components in cilia and flagella. Not required for outer dynein arm complexes assembly. Required for axonemal recruitment of CCDC39. {ECO:0000250|UniProtKB:A8IQT2, ECO:0000250|UniProtKB:Q4G0X9}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21131972}. Cell projection, cilium {ECO:0000269|PubMed:21131972}. Note=Localizes to cytoplasm and motile cilium. {ECO:0000269|PubMed:21131972}. TISSUE SPECIFICITY: Specifically expressed in the embryonic node and midline. {ECO:0000269|PubMed:21131972}. +Q8VHW3 CCG6_MOUSE Voltage-dependent calcium channel gamma-6 subunit (Neuronal voltage-gated calcium channel gamma-6 subunit) 260 28,145 Chain (1); Transmembrane (4) TRANSMEM 43 63 Helical. {ECO:0000255}.; TRANSMEM 143 163 Helical. {ECO:0000255}.; TRANSMEM 169 189 Helical. {ECO:0000255}.; TRANSMEM 221 241 Helical. {ECO:0000255}. FUNCTION: Regulates the activity of L-type calcium channels that contain CACNA1C as pore-forming subunit. {ECO:0000250|UniProtKB:Q9BXT2}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9BXT2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9BXT2}. SUBUNIT: Interacts with CACNA1C (PubMed:21127204). Identified in a complex with the L-type calcium channel subunits CACNA1C, CACNA2D1 and either CACNB1 or CACNB2 (By similarity). {ECO:0000250|UniProtKB:Q9BXT2, ECO:0000269|PubMed:21127204}. TISSUE SPECIFICITY: Detected in brain and heart (at protein level). {ECO:0000269|PubMed:21127204}. +Q8CDV6 CCD63_MOUSE Coiled-coil domain-containing protein 63 558 65,274 Alternative sequence (1); Chain (1); Coiled coil (3); Erroneous initiation (1) FUNCTION: Plays a role in spermiogenesis (PubMed:26501274). Involved in the elongation of flagella and the formation of sperm heads (PubMed:26501274). {ECO:0000269|PubMed:26501274}. TISSUE SPECIFICITY: Expressed in testis, brain, thymus and lung (PubMed:26501274). {ECO:0000269|PubMed:26501274}. +Q8VHW2 CCG8_MOUSE Voltage-dependent calcium channel gamma-8 subunit (Neuronal voltage-gated calcium channel gamma-8 subunit) (Transmembrane AMPAR regulatory protein gamma-8) (TARP gamma-8) 423 43,453 Chain (1); Compositional bias (1); Modified residue (2); Transmembrane (5) TRANSMEM 19 39 Helical. {ECO:0000255}.; TRANSMEM 127 147 Helical. {ECO:0000255}.; TRANSMEM 157 177 Helical. {ECO:0000255}.; TRANSMEM 207 227 Helical. {ECO:0000255}.; TRANSMEM 318 338 Helical. {ECO:0000255}. FUNCTION: Regulates the activity of L-type calcium channels that contain CACNA1C as pore-forming subunit (PubMed:21127204). Regulates the trafficking and gating properties of AMPA-selective glutamate receptors (AMPARs). Promotes their targeting to the cell membrane and synapses and modulates their gating properties by slowing their rates of activation, deactivation and desensitization and by mediating their resensitization. Does not show subunit-specific AMPA receptor regulation and regulates all AMPAR subunits. Thought to stabilize the calcium channel in an inactivated (closed) state. {ECO:0000269|PubMed:21127204, ECO:0000269|PubMed:21172611}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:21127204, ECO:0000305|PubMed:21172611}; Multi-pass membrane protein {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000269|PubMed:21172611}. SUBUNIT: Interacts with CACNA1C. Identified in a complex with the L-type calcium channel subunits CACNA1C, CACNA2D1 and either CACNB1 or CACNB2 (PubMed:21127204). Acts as an auxiliary subunit for AMPA-selective glutamate receptors (AMPARs). Found in a complex with GRIA1, GRIA2, GRIA3, GRIA4, CNIH2, CNIH3, CACNG2, CACNG3, CACNG4, CACNG5 and CACNG7. Interacts with CNIH2. {ECO:0000269|PubMed:21127204, ECO:0000269|PubMed:21172611}. +O08786 CCKAR_MOUSE Cholecystokinin receptor type A (CCK-A receptor) (CCK-AR) (Cholecystokinin-1 receptor) (CCK1-R) 436 48,437 Chain (1); Compositional bias (2); Disulfide bond (2); Glycosylation (3); Lipidation (1); Sequence conflict (3); Topological domain (8); Transmembrane (7) TRANSMEM 42 67 Helical; Name=1. {ECO:0000255}.; TRANSMEM 78 104 Helical; Name=2. {ECO:0000255}.; TRANSMEM 116 137 Helical; Name=3. {ECO:0000255}.; TRANSMEM 158 178 Helical; Name=4. {ECO:0000255}.; TRANSMEM 211 234 Helical; Name=5. {ECO:0000255}.; TRANSMEM 322 342 Helical; Name=6. {ECO:0000255}.; TRANSMEM 358 381 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 41 Extracellular. {ECO:0000255}.; TOPO_DOM 68 77 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 105 115 Extracellular. {ECO:0000255}.; TOPO_DOM 138 157 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 179 210 Extracellular. {ECO:0000255}.; TOPO_DOM 235 321 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 343 357 Extracellular. {ECO:0000255}.; TOPO_DOM 382 436 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for cholecystokinin. Mediates pancreatic growth and enzyme secretion, smooth muscle contraction of the gall bladder and stomach. Has a 1000-fold higher affinity for CCK rather than for gastrin. It modulates feeding and dopamine-induced behavior in the central and peripheral nervous system. This receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. +O89093 CCL20_MOUSE C-C motif chemokine 20 (Beta-chemokine exodus-1) (CC chemokine LARC) (CC chemokine ST38) (Liver and activation-regulated chemokine) (Macrophage inflammatory protein 3 alpha) (MIP-3-alpha) (Small-inducible cytokine A20) 97 10,826 Alternative sequence (1); Beta strand (4); Chain (1); Disulfide bond (2); Helix (2); Signal peptide (1) FUNCTION: Acts as a ligand for C-C chemokine receptor CCR6. Signals through binding and activation of CCR6 and induces a strong chemotactic response and mobilization of intracellular calcium ions (PubMed:9862452, PubMed:20068036). The ligand-receptor pair CCL20-CCR6 is responsible for the chemotaxis of dendritic cells (DC), effector/memory T-cells and B-cells and plays an important role at skin and mucosal surfaces under homeostatic and inflammatory conditions, as well as in pathology, including cancer and autoimmune diseases (PubMed:21376174). CCL20 acts as a chemotactic factor that attracts lymphocytes and, slightly, neutrophils, but not monocytes (By similarity). Involved in the recruitment of both the proinflammatory IL17 producing helper T-cells (Th17) and the regulatory T-cells (Treg) to sites of inflammation (PubMed:19050256). Required for optimal migration of thymic natural regulatory T cells (nTregs) and DN1 early thymocyte progenitor cells (PubMed:24638065). Positively regulates sperm motility and chemotaxis via its binding to CCR6 which triggers Ca2+ mobilization in the sperm which is important for its motility (PubMed:25122636). May be involved in formation and function of the mucosal lymphoid tissues by attracting lymphocytes and dendritic cells towards epithelial cells (PubMed:10064080). {ECO:0000250|UniProtKB:P78556, ECO:0000269|PubMed:10064080, ECO:0000269|PubMed:19050256, ECO:0000269|PubMed:20068036, ECO:0000269|PubMed:24638065, ECO:0000269|PubMed:25122636, ECO:0000269|PubMed:9862452, ECO:0000303|PubMed:21376174}. SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P78556}. TISSUE SPECIFICITY: Thymic medulla (at protein level). Prominently expressed in the small intestine, colon and appendix. Also found in thymus, spleen, lymph node and lung. The long form might be dominant in intestinal, and the short form in lymphoid tissues. Expressed by IL17 producing helper T-cells (Th17). {ECO:0000269|PubMed:19050256, ECO:0000269|PubMed:24638065}. +P10855 CCL3_MOUSE C-C motif chemokine 3 (Heparin-binding chemotaxis protein) (L2G25B) (Macrophage inflammatory protein 1-alpha) (MIP-1-alpha) (SIS-alpha) (Small-inducible cytokine A3) (TY-5) 92 10,345 Beta strand (5); Chain (1); Disulfide bond (2); Helix (2); Sequence conflict (2); Signal peptide (1) FUNCTION: Monokine with inflammatory, pyrogenic and chemokinetic properties. Has a potent chemotactic activity for eosinophils. Binding to a high-affinity receptor activates calcium release in neutrophils. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Expressed in lung, spleen, and pancreas. +P51675 CCR1_MOUSE C-C chemokine receptor type 1 (C-C CKR-1) (CC-CKR-1) (CCR-1) (CCR1) (Macrophage inflammatory protein 1-alpha receptor) (MIP-1alpha-R) (RANTES-R) (CD antigen CD191) 355 40,895 Chain (1); Disulfide bond (1); Sequence conflict (5); Topological domain (8); Transmembrane (7) TRANSMEM 35 60 Helical; Name=1. {ECO:0000255}.; TRANSMEM 65 91 Helical; Name=2. {ECO:0000255}.; TRANSMEM 108 129 Helical; Name=3. {ECO:0000255}.; TRANSMEM 147 171 Helical; Name=4. {ECO:0000255}.; TRANSMEM 198 223 Helical; Name=5. {ECO:0000255}.; TRANSMEM 240 264 Helical; Name=6. {ECO:0000255}.; TRANSMEM 282 305 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 34 Extracellular. {ECO:0000255}.; TOPO_DOM 61 64 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 92 107 Extracellular. {ECO:0000255}.; TOPO_DOM 130 146 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 172 197 Extracellular. {ECO:0000255}.; TOPO_DOM 224 239 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 265 281 Extracellular. {ECO:0000255}.; TOPO_DOM 306 355 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for a C-C type chemokine. Binds to MIP-1-alpha, RANTES, and less efficiently, to MIP-1-beta or MCP-1 and subsequently transduces a signal by increasing the intracellular calcium ions level. Responsible for affecting stem cell proliferation. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBUNIT: Interacts with CREB3. {ECO:0000250}. TISSUE SPECIFICITY: Detected in the heart, spleen, lung, peritoneal exudate cells and leukocytes. +Q640L3 CCPG1_MOUSE Cell cycle progression protein 1 753 86,126 Alternative sequence (2); Chain (1); Coiled coil (2); Compositional bias (1); Erroneous initiation (1); Modified residue (1); Region (1); Sequence conflict (5); Topological domain (2); Transmembrane (1) TRANSMEM 219 239 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 218 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 240 753 Lumenal. {ECO:0000255}. FUNCTION: Acts as an assembly platform for Rho protein signaling complexes. Limits guanine nucleotide exchange activity of MCF2L toward RHOA, which results in an inhibition of both its transcriptional activation ability and its transforming activity. Does not inhibit activity of MCF2L toward CDC42, or activity of MCF2 toward either RHOA or CDC42. May be involved in cell cycle regulation. {ECO:0000269|PubMed:17000758}. SUBCELLULAR LOCATION: Cytoplasmic granule membrane {ECO:0000269|PubMed:17000758}; Single-pass type II membrane protein {ECO:0000269|PubMed:17000758}. SUBUNIT: Interacts with MCF2L. May interact with MCF2, ARHGEF1, BCR, VAV1 and FGD1, but not with TIAM1. Interacts with GTP-bound CDC42 and SRC. {ECO:0000269|PubMed:17000758}. +Q52KE7 CCNL1_MOUSE Cyclin-L1 (Cyclin-L) (Cyclin Ania-6a) 532 60,133 Alternative sequence (2); Chain (1); Cross-link (3); Frameshift (1); Modified residue (7); Region (3); Sequence conflict (3) FUNCTION: Involved in pre-mRNA splicing. Functions in association with cyclin-dependent kinases (CDKs). May play a role in the regulation of RNA polymerase II (pol II). Inhibited by the CDK-specific inhibitor CDKN1A/p21. {ECO:0000250|UniProtKB:Q9UK58}. SUBCELLULAR LOCATION: Isoform 1: Nucleus speckle {ECO:0000269|PubMed:11683997}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9UK58}. Note=Found in nuclear intrachromatin granules clusters (IGC), also called nuclear speckles, which are storage compartments for nuclear proteins involved in mRNA processing.; SUBCELLULAR LOCATION: Isoform 2: Nucleus {ECO:0000269|PubMed:11683997}. Cytoplasm {ECO:0000269|PubMed:11683997}. SUBUNIT: Interacts with POLR2A via its hyperphosphorylated C-terminal domain (CTD) (By similarity). Interacts with CDK11A, CDK11B, CDK12 and CDK13. May form a ternary complex with CDK11B and casein kinase II (CKII). Interacts with pre-mRNA-splicing factors, including at least SRSF1, SRSF2 AND SRSF7/SLU7 (By similarity) (PubMed:17261272). {ECO:0000250|UniProtKB:Q9R1Q2, ECO:0000250|UniProtKB:Q9UK58, ECO:0000269|PubMed:17261272}. DOMAIN: Contains a RS region (arginine-serine dipeptide repeat) within the C-terminal domain which is the hallmark of the SR family of splicing factors. This region probably plays a role in protein-protein interactions (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Widely expressed (at protein level). {ECO:0000269|PubMed:18216018}. +P51678 CCR3_MOUSE Probable C-C chemokine receptor type 3 (C-C CKR-3) (CC-CKR-3) (CCR-3) (CCR3) (CKR3) (Macrophage inflammatory protein 1-alpha receptor-like 2) (MIP-1 alpha RL2) (CD antigen CD193) 359 41,783 Chain (1); Disulfide bond (1); Sequence conflict (7); Topological domain (8); Transmembrane (7) TRANSMEM 39 64 Helical; Name=1. {ECO:0000255}.; TRANSMEM 69 95 Helical; Name=2. {ECO:0000255}.; TRANSMEM 112 133 Helical; Name=3. {ECO:0000255}.; TRANSMEM 151 175 Helical; Name=4. {ECO:0000255}.; TRANSMEM 202 227 Helical; Name=5. {ECO:0000255}.; TRANSMEM 244 268 Helical; Name=6. {ECO:0000255}.; TRANSMEM 286 309 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 38 Extracellular. {ECO:0000255}.; TOPO_DOM 65 68 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 96 111 Extracellular. {ECO:0000255}.; TOPO_DOM 134 150 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 176 201 Extracellular. {ECO:0000255}.; TOPO_DOM 228 243 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 269 285 Extracellular. {ECO:0000255}.; TOPO_DOM 310 359 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for a C-C type chemokine. Binds to eotaxin, MCP-3, MCP-4 and RANTES and subsequently transduces a signal by increasing the intracellular calcium ions level. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Detected in skeletal muscle and in trace amounts in leukocytes. +P0C242 CCNO_MOUSE Cyclin-O 352 38,822 Chain (1); Compositional bias (1); Frameshift (1); Modified residue (1) FUNCTION: Specifically required for generation of multiciliated cells, possibly by promoting a cell cycle state compatible with centriole amplification and maturation. Acts downstream of MCIDAS to promote mother centriole amplification and maturation in preparation for apical docking (By similarity). May be involved in apoptosis in lymphoid cells; however, this result requires additional evidences in vivo. May be involved in oocyte meiotic resumption in oocytes. {ECO:0000250, ECO:0000269|PubMed:18927588, ECO:0000269|PubMed:19609756, ECO:0000269|PubMed:26777464}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24747639, ECO:0000269|PubMed:26777464}. Note=Localizes to the apical part of cytoplasm. {ECO:0000269|PubMed:24747639}. TISSUE SPECIFICITY: Present in respiratory cells (at protein level). Expressed in multiciliated tissue in brain and fallopian tube (at protein level) (PubMed:26777464). Highly expressed in oocytes. {ECO:0000269|PubMed:19609756, ECO:0000269|PubMed:24747639, ECO:0000269|PubMed:26777464}. +Q3UR78 CD048_MOUSE Neuropeptide-like protein C4orf48 homolog 90 9,806 Alternative sequence (1); Chain (1); Erroneous initiation (3); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. TISSUE SPECIFICITY: Specifically expressed during neocortex and cerebellum development. {ECO:0000269|PubMed:21287218}. +Q7TQK0 CCNT2_MOUSE Cyclin-T2 (CycT2) 723 80,252 Alternative sequence (2); Chain (1); Compositional bias (1); Cross-link (1); Domain (1); Modified residue (2); Region (2); Sequence conflict (2) FUNCTION: Regulatory subunit of the cyclin-dependent kinase pair (CDK9/cyclin T) complex, also called positive transcription elongation factor B (P-TEFB), which is proposed to facilitate the transition from abortive to production elongation by phosphorylating the CTD (carboxy-terminal domain) of the large subunit of RNA polymerase II (RNAP II). The activity of this complex is regulated by binding with 7SK snRNA (By similarity). Plays a role during muscle differentiation; P-TEFB complex interacts with MYOD1; this tripartite complex promotes the transcriptional activity of MYOD1 through its CDK9-mediated phosphorylation and binds the chromatin of promoters and enhancers of muscle-specific genes; this event correlates with hyperphosphorylation of the CTD domain of RNA pol II (PubMed:16245309, PubMed:23060074, PubMed:12037670). In addition, enhances MYOD1-dependent transcription through interaction with PKN1 (By similarity). Involved in early embryo development (PubMed:19364821). {ECO:0000250|UniProtKB:O60583, ECO:0000269|PubMed:12037670, ECO:0000269|PubMed:16245309, ECO:0000269|PubMed:19364821, ECO:0000269|PubMed:23060074}. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:23060074}. Nucleus {ECO:0000269|PubMed:23060074}. Note=Nucleus in differentiating cells. {ECO:0000269|PubMed:23060074}. SUBUNIT: Interacts with CDK9 to form P-TEFb. Interacts with POLR2A (via the C-terminal domain (CTD)); mediates transcriptional activity. Interacts with HEXIM1; mediates formation of a tripartite complex with KPNA2. Interacts with HEXIM2. Interacts with PKN1; enhances MYOD1-dependent transcription. P-TEFB complex interacts with RB1; promotes phosphorylation of RB1 (By similarity). P-TEFB complex interacts with MYOD1; promotes the transcriptional activity of MYOD1 through its CDK9-mediated phosphorylation (PubMed:12037670). Interacts with MDFI and MDFIC (By similarity). {ECO:0000250|UniProtKB:O60583, ECO:0000269|PubMed:12037670}. TISSUE SPECIFICITY: Isoform 2: Highly expressed in all phases of skeletal muscle differentiation, particularly in later stages (PubMed:23060074). Highly expressed in skeletal muscle. Significantly expressed in heart, brain, kidney, liver, testis, and pancreas (PubMed:19364821). {ECO:0000269|PubMed:19364821, ECO:0000269|PubMed:23060074}. +Q8R422 CD109_MOUSE CD109 antigen (GPI-anchored alpha-2 macroglobulin-related protein) (CD antigen CD109) 1442 161,659 Chain (1); Cross-link (1); Erroneous initiation (1); Glycosylation (7); Lipidation (1); Propeptide (1); Region (1); Signal peptide (1) FUNCTION: Modulates negatively TGFB1 signaling in keratinocytes. {ECO:0000250}. PTM: N-glycosylated. {ECO:0000250}.; PTM: 2 forms of 150 (p150) and 120 kDa (p120) exist due to proteolytic degradation from a 180 kDa form. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. SUBUNIT: Heterodimer; disulfide-linked. Interacts with TGFB1 and TGFBR1. Forms a heteromeric complex with TGFBR1, TGFBR2 and TGFBR3 in a ligand-independent manner (By similarity). {ECO:0000250}. +Q8K3W3 CASC3_MOUSE Protein CASC3 (Cancer susceptibility candidate gene 3 protein homolog) (Metastatic lymph node gene 51 protein homolog) (MLN 51 homolog) (Protein barentsz) (Btz) (mBtz) 698 75,770 Chain (1); Coiled coil (1); Compositional bias (3); Erroneous initiation (1); Modified residue (9); Motif (3); Mutagenesis (1); Region (3); Sequence conflict (5) FUNCTION: Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). Stimulates the ATPase and RNA-helicase activities of EIF4A3. Plays a role in the stress response by participating in cytoplasmic stress granules assembly and by favoring cell recovery following stress. Component of the dendritic ribonucleoprotein particles (RNPs) in hippocampal neurons. May play a role in mRNA transport. Binds spliced mRNA in sequence-independent manner, 20-24 nucleotides upstream of mRNA exon-exon junctions. Binds poly(G) and poly(U) RNA homopolymer (By similarity). {ECO:0000250}. PTM: ADP-ribosylated by tankyrase TNKS and TNKS2. Poly-ADP-ribosylated protein is recognized by RNF146, followed by ubiquitination (By similarity). {ECO:0000250}.; PTM: Ubiquitinated by RNF146 when poly-ADP-ribosylated, leading to its degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12843282}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:12843282}. Nucleus {ECO:0000269|PubMed:12843282}. Nucleus speckle {ECO:0000250|UniProtKB:O15234}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:O15234}. Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000269|PubMed:12843282}. Cell projection, dendrite {ECO:0000269|PubMed:12843282}. Note=Shuttles between the nucleus and the cytoplasm in a XPO1/CRM1-dependent manner (PubMed:12843282). Transported to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. In nuclear speckles, colocalizes with MAGOH. Under stress conditions, colocalizes with FMR1 and TIA1, but not MAGOH and RBM8A EJC core factors, in cytoplasmic stress granules (By similarity). In the dendrites of hippocampal neurons, localizes to dendritic ribonucleoprotein granules (Probable). {ECO:0000250|UniProtKB:O15234, ECO:0000269|PubMed:12843282, ECO:0000305|PubMed:12843282}. SUBUNIT: Component of the mRNA splicing-dependent exon junction complex (EJC), which contains at least CASC3, EIF4A3, MAGOH, NXF1 and RBM8A/Y14 (By similarity). Forms homooligomers (By similarity). Interacts with STAU in an RNA-dependent manner (PubMed:12843282). {ECO:0000250|UniProtKB:O15234, ECO:0000250|UniProtKB:Q8K3X0, ECO:0000269|PubMed:12843282}. DOMAIN: The coiled coil domain may be involved in oligomerization. {ECO:0000250}. TISSUE SPECIFICITY: High levels in heart, brain, including hippocampus and cerebellum, liver, kidney and testis; lower levels in muscle, lung and spleen. {ECO:0000269|PubMed:12843282}. +O70370 CATS_MOUSE Cathepsin S (EC 3.4.22.27) 340 38,475 Active site (3); Beta strand (10); Chain (1); Disulfide bond (4); Frameshift (1); Glycosylation (1); Helix (9); Propeptide (1); Sequence conflict (8); Signal peptide (1); Turn (3) FUNCTION: Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond-specificity of this proteinase is in part similar to the specificities of cathepsin L. SUBCELLULAR LOCATION: Lysosome. TISSUE SPECIFICITY: Widely expressed with highest expression found in non-skeletal tissues. Relatively high levels found in skeletal tissues. {ECO:0000269|PubMed:10395917}. +Q3V0A6 CB078_MOUSE Uncharacterized protein C2orf78 homolog 857 93,729 Chain (1) +Q8CAI1 CC142_MOUSE Coiled-coil domain-containing protein 142 738 79,817 Alternative sequence (2); Chain (1); Coiled coil (1) +Q6NZQ0 CC189_MOUSE Coiled-coil domain-containing protein 189 333 37,873 Chain (1); Coiled coil (1); Modified residue (1) +Q9D162 CC167_MOUSE Coiled-coil domain-containing protein 167 97 11,475 Alternative sequence (2); Chain (1); Coiled coil (1); Erroneous initiation (3); Transmembrane (1) TRANSMEM 78 95 Helical. {ECO:0000255}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. +A0A140LIT1 CC194_MOUSE Coiled-coil domain-containing protein 194 234 25,521 Chain (1); Coiled coil (1); Signal peptide (1) +Q810N9 CC172_MOUSE Coiled-coil domain-containing protein 172 (TEKT2-binding protein 2) 267 31,483 Alternative sequence (1); Chain (1); Coiled coil (2) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24394471}. Cell projection, cilium {ECO:0000250|UniProtKB:Q6AXT4}. Note=In caput spermatozoa, localized in the middle piece, predominantly concentrated at the mitochondrial sheath of the flagella and to a lesser extent with outer dense fibers (ODF) (By similarity). Colocalized with TEKT2 at the perinuclear region (PubMed:24394471). {ECO:0000250|UniProtKB:Q6AXT4, ECO:0000269|PubMed:24394471}. SUBUNIT: May interact with TEKT2. {ECO:0000269|PubMed:24394471}. +Q8VEH6 CBWD1_MOUSE COBW domain-containing protein 1 (Cobalamin synthase W domain-containing protein 1) 393 43,772 Alternative sequence (1); Chain (1); Domain (1); Nucleotide binding (3) +A2AEV7 CC120_MOUSE Coiled-coil domain-containing protein 120 629 67,407 Chain (1); Coiled coil (1); Modified residue (3); Region (1) FUNCTION: Centriolar protein required for centriole subdistal appendage assembly and microtubule anchoring in interphase cells (PubMed:28422092). Together with CCDC68, cooperate with subdistal appendage components ODF2, NIN and CEP170 for hierarchical subdistal appendage assembly (PubMed:28422092). Recruits NIN and CEP170 to centrosomes (PubMed:28422092). Also required for neurite growth (By similarity). Localizes CYTH2 to vesicles to allow its transport along neurites, and subsequent ARF6 activation and neurite growth (By similarity). {ECO:0000250|UniProtKB:Q96HB5, ECO:0000269|PubMed:28422092}. PTM: Ubiquitinated; interaction with CYTH2 may prevent ubiquitination. {ECO:0000250|UniProtKB:Q96HB5}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q96HB5}. Cytoplasm {ECO:0000250|UniProtKB:Q96HB5}. Cell projection {ECO:0000250|UniProtKB:Q96HB5}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q96HB5}. Endosome {ECO:0000250|UniProtKB:Q96HB5}. Note=Localizes to the subdistal appendages of mother centrioles and proximal ends of both centrioles in interphase cells (By similarity). Recruited to subdistal appendages by ODF2 (By similarity). In differentiating neuroblastoma cells, colocalizes with CYTH2 in both neurite shaft and growth cone areas (By similarity). Partially colocalizes with endosomes along neurites in differentiating neuroblastoma cells (By similarity). {ECO:0000250|UniProtKB:Q96HB5}. SUBUNIT: Interacts with NIN and CEP170; leading to recruit them to centrosomes (By similarity). Interacts with CYTH2; this interaction is direct and stabilizes CCDC120, possibly by preventing ubiquitination (By similarity). {ECO:0000250|UniProtKB:Q96HB5}. +A2AJB1 CC183_MOUSE Coiled-coil domain-containing protein 183 534 62,117 Alternative sequence (2); Chain (1); Coiled coil (3); Compositional bias (1) +Q8C5V8 CC187_MOUSE Coiled-coil domain-containing protein 187 958 104,957 Chain (1); Coiled coil (1) +Q5SP85 CC85A_MOUSE Coiled-coil domain-containing protein 85A 500 54,483 Alternative sequence (2); Chain (1); Coiled coil (3); Compositional bias (1); Erroneous initiation (1); Modified residue (1); Sequence caution (2); Sequence conflict (1) +Q6PDY0 CC85B_MOUSE Coiled-coil domain-containing protein 85B (Hepatitis delta antigen-interacting protein A homolog) (Delta-interacting protein A homolog) 202 22,133 Chain (1); Coiled coil (2); Modified residue (1) FUNCTION: Functions as a transcriptional repressor. May inhibit the activity of CTNNB1 in a TP53-dependent manner and thus regulate cell growth. May function in adipocyte differentiation, negatively regulating mitotic clonal expansion (PubMed:15644333, PubMed:22666460). {ECO:0000269|PubMed:15644333, ECO:0000269|PubMed:22666460}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q15834}. Nucleus {ECO:0000269|PubMed:15644333, ECO:0000269|PubMed:22666460}. SUBUNIT: Interacts with MCRS1 (By similarity). Interacts with TCF7L2; competes with CTNNB1 (By similarity). Interacts with CEBPB (PubMed:15644333). May interact with CEBPD (PubMed:15644333). Interacts with ANKRD26 (By similarity). Interacts with EURL (PubMed:27404227). {ECO:0000250|UniProtKB:Q15834, ECO:0000269|PubMed:15644333, ECO:0000269|PubMed:27404227}. TISSUE SPECIFICITY: Expressed in white and brown adipose tissue. {ECO:0000269|PubMed:15644333}. +Q6PHN1 CCD57_MOUSE Coiled-coil domain-containing protein 57 1016 116,194 Chain (1); Coiled coil (3) +Q9D5Y1 CCD39_MOUSE Coiled-coil domain-containing protein 39 937 110,072 Chain (1); Coiled coil (4); Modified residue (2); Sequence conflict (2) FUNCTION: Required for assembly of dynein regulatory complex (DRC) and inner dynein arm (IDA) complexes, which are responsible for ciliary beat regulation, thereby playing a central role in motility in cilia and flagella. Probably acts together with CCDC40 to form a molecular ruler that determines the 96 nanometer (nm) repeat length and arrangements of components in cilia and flagella. Not required for outer dynein arm complexes assembly. {ECO:0000250|UniProtKB:A8IQT2, ECO:0000250|UniProtKB:Q9UFE4}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q9UFE4}. Note=CCDC40 is required for localization to axonemes. {ECO:0000250|UniProtKB:Q9UFE4}. TISSUE SPECIFICITY: Strongly expressed in tissues rich in ciliated cells. Expressed in olfactory and vomeronasal sensory neurons and the respiratory epithelium. Expressed in node cells carrying motile cilia, in upper and lower airways, and in ependymal and choroid plexus cells. {ECO:0000269|PubMed:21131972}. +P53702 CCHL_MOUSE Cytochrome c-type heme lyase (CCHL) (EC 4.4.1.17) (Holocytochrome c-type synthase) 272 30,978 Chain (1); Initiator methionine (1); Lipidation (1); Repeat (2); Sequence conflict (1) FUNCTION: Links covalently the heme group to the apoprotein of cytochrome c. {ECO:0000250}. SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305}. Membrane {ECO:0000250|UniProtKB:P53701}; Lipid-anchor {ECO:0000250|UniProtKB:P53701}. +P51943 CCNA2_MOUSE Cyclin-A2 (Cyclin-A) 422 47,269 Beta strand (2); Chain (1); Helix (19); Modified residue (2); Sequence conflict (3); Turn (1) FUNCTION: Cyclin which controls both the G1/S and the G2/M transition phases of the cell cycle. Functions through the formation of specific serine/threonine kinase holoenzyme complexes with the cyclin-dependent protein kinases CDK1 and CDK2. The cyclin subunit confers the substrate specificity of these complexes and differentially interacts with and activates CDK1 and CDK2 throughout the cell cycle. {ECO:0000250|UniProtKB:P20248}. PTM: Polyubiquitinated via 'Lys-11'-linked ubiquitin by the anaphase-promoting complex (APC/C), leading to its degradation by the proteasome. Deubiquitinated and stabilized by USP37 enables entry into S phase. {ECO:0000250|UniProtKB:P20248}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P20248}. Cytoplasm {ECO:0000250|UniProtKB:P20248}. Note=Exclusively nuclear during interphase. Detected in the nucleus and the cytoplasm at prophase. Cytoplasmic when associated with SCAPER. {ECO:0000250|UniProtKB:P20248}. SUBUNIT: Interacts with the CDK1 and CDK2 protein kinases to form serine/threonine kinase holoenzyme complexes (PubMed:10068472). Interacts with CDK1 (hyperphosphorylated form in G1 and underphosphorylated forms in S and G2). Interacts with CDK2; the interaction increases from G1 to G2. Interacts (associated with CDK2 but not with CDK1) with SCAPER; regulates the activity of CCNA2/CDK2 by transiently maintaining CCNA2 in the cytoplasm. Forms a ternary complex with CDK2 and CDKN1B; CDKN1B inhibits the kinase activity of CDK2 through conformational rearrangements (By similarity). Interacts with INCA1 (By similarity). {ECO:0000250|UniProtKB:P20248, ECO:0000269|PubMed:10068472}. TISSUE SPECIFICITY: Ubiquitous (PubMed:8565853). In the testis, expressed in germ cells and in the ovary, in both germline and somatic cells (PubMed:8575639, PubMed:10068472). {ECO:0000269|PubMed:10068472, ECO:0000269|PubMed:8565853, ECO:0000269|PubMed:8575639}. +P30282 CCND3_MOUSE G1/S-specific cyclin-D3 292 32,411 Chain (1); Domain (1); Modified residue (2); Sequence conflict (1) FUNCTION: Regulatory component of the cyclin D3-CDK4 (DC) complex that phosphorylates and inhibits members of the retinoblastoma (RB) protein family including RB1 and regulates the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complex and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also substrate for SMAD3, phosphorylating SMAD3 in a cell-cycle-dependent manner and repressing its transcriptional activity. Component of the ternary complex, cyclin D3/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex. PTM: Polyubiquitinated by the SCF(FBXL2) complex, leading to proteasomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}. Note=Cyclin D-CDK4 complexes accumulate at the nuclear membrane and are then translocated to the nucleus through interaction with KIP/CIP family members. {ECO:0000250}. SUBUNIT: Interacts with the CDK4 and CDK6 protein kinases to form a serine/threonine kinase holoenzyme complex. The cyclin subunit imparts substrate specificity to the complex. Component of the ternary complex cyclin D/CDK4/CDKN1B required for nuclear translocation and modulation of CDK4-mediated kinase activity. Can form similar complexes with either CDKN1A or CDKN2A. Interacts with ATF5 and EIF3K (By similarity). {ECO:0000250}. +P51683 CCR2_MOUSE C-C chemokine receptor type 2 (C-C CKR-2) (CC-CKR-2) (CCR-2) (CCR2) (JE/FIC receptor) (MCP-1 receptor) (CD antigen CD192) 373 42,783 Chain (1); Disulfide bond (1); Modified residue (1); Sequence conflict (3); Topological domain (8); Transmembrane (7) TRANSMEM 56 83 Helical; Name=1. {ECO:0000255}.; TRANSMEM 94 114 Helical; Name=2. {ECO:0000255}.; TRANSMEM 128 149 Helical; Name=3. {ECO:0000255}.; TRANSMEM 167 191 Helical; Name=4. {ECO:0000255}.; TRANSMEM 220 239 Helical; Name=5. {ECO:0000255}.; TRANSMEM 257 281 Helical; Name=6. {ECO:0000255}.; TRANSMEM 299 322 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 55 Extracellular. {ECO:0000255}.; TOPO_DOM 84 93 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 115 127 Extracellular. {ECO:0000255}.; TOPO_DOM 150 166 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 192 219 Extracellular. {ECO:0000255}.; TOPO_DOM 240 256 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 282 298 Extracellular. {ECO:0000255}.; TOPO_DOM 323 373 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for the CCL2, CCL7 and CCL12 chemokines (PubMed:8996246). Receptor for the beta-defensin DEFB106A/DEFB106B (By similarity). Transduces a signal by increasing intracellular calcium ion levels (PubMed:8996246). Upon CCL2 ligation, mediates chemotaxis and migration induction through the activation of the PI3K cascade, the small G protein Rac and lamellipodium protrusion (By similarity). {ECO:0000250|UniProtKB:P41597, ECO:0000269|PubMed:8996246}. PTM: Sulfation increases the affinity for both monomeric and dimeric CCL2 with stronger binding to the monomeric form. Binding of sulfated CCR2 to CCL2 promotes conversion of CCL2 from dimer to monomer. {ECO:0000250|UniProtKB:P41597}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8996246}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P41597}. Note=The chemoattractant receptors are reportedly distributed throughout the cell surface; after stimulation with a ligand, such as CCL2, they are rapidly recruited into microdomain clusters at the cell membrane. {ECO:0000250|UniProtKB:P41597}. SUBUNIT: Interacts with ARRB1. Interacts (via extracellular N-terminal region) with beta-defensin DEFB106A/DEFB106B; this interaction may preferentially require specific tyrosine sulfation on CCR2. Interacts with NUP85; the interaction is required for CCR2 clusters formation on the cell membrane and CCR2 signaling (By similarity). {ECO:0000250|UniProtKB:P41597}. TISSUE SPECIFICITY: Detected in monocyte/macrophage cell lines, but not in nonhematopoietic cell lines. +O35457 CCRL2_MOUSE C-C chemokine receptor-like 2 (Chemokine receptor CCR11) (G-protein coupled beta chemokine receptor) (Lipopolysaccharide-inducible C-C chemokine receptor) (L-CCR) 360 40,745 Chain (1); Disulfide bond (1); Glycosylation (2); Sequence conflict (8); Topological domain (8); Transmembrane (7) TRANSMEM 43 63 Helical; Name=1. {ECO:0000255}.; TRANSMEM 74 94 Helical; Name=2. {ECO:0000255}.; TRANSMEM 110 130 Helical; Name=3. {ECO:0000255}.; TRANSMEM 142 162 Helical; Name=4. {ECO:0000255}.; TRANSMEM 203 223 Helical; Name=5. {ECO:0000255}.; TRANSMEM 244 264 Helical; Name=6. {ECO:0000255}.; TRANSMEM 286 307 Helical; Name=7. {ECO:0000255}. TOPO_DOM 1 42 Extracellular. {ECO:0000255}.; TOPO_DOM 64 73 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 95 109 Extracellular. {ECO:0000255}.; TOPO_DOM 131 141 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 163 202 Extracellular. {ECO:0000255}.; TOPO_DOM 224 243 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 265 285 Extracellular. {ECO:0000255}.; TOPO_DOM 308 360 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for CCL19 and chemerin/RARRES2. Does not appear to be a signaling receptor, but may have a role in modulating chemokine-triggered immune responses by capturing and internalizing CCL19 or by presenting RARRES2 ligand to CMKLR1, a functional signaling receptor. Plays a critical role for the development of Th2 responses (By similarity). {ECO:0000250, ECO:0000269|PubMed:12885941, ECO:0000269|PubMed:18794339, ECO:0000269|PubMed:20606167}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. DOMAIN: Lacks the conserved DRYLAIV motif in the second intracellular loop that is required for signaling of functional chemokine receptors. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in macrophages, astrocytes, in glial cells. Constitutively expressed by mast cells. Detected in bronchial epithelium in OVA-induced airway inflammation. Up-regulated during dendritic cell (DC) maturation. {ECO:0000269|PubMed:12555200, ECO:0000269|PubMed:14966207, ECO:0000269|PubMed:14999816, ECO:0000269|PubMed:20606167, ECO:0000269|PubMed:9563519}. +Q61490 CD166_MOUSE CD166 antigen (Activated leukocyte cell adhesion molecule) (BEN) (Protein DM-GRASP) (CD antigen CD166) 583 65,092 Chain (1); Disulfide bond (5); Domain (5); Glycosylation (8); Sequence conflict (6); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 528 549 Helical. {ECO:0000255}. TOPO_DOM 28 527 Extracellular. {ECO:0000255}.; TOPO_DOM 550 583 Cytoplasmic. {ECO:0000255}. FUNCTION: Cell adhesion molecule that mediates both heterotypic cell-cell contacts via its interaction with CD6, as well as homotypic cell-cell contacts. Promotes T-cell activation and proliferation via its interactions with CD6 (By similarity). Contributes to the formation and maturation of the immunological synapse via its interactions with CD6 (By similarity). Mediates homotypic interactions with cells that express ALCAM (PubMed:24740813). Mediates attachment of dendritic cells onto endothelial cells via homotypic interaction. Inhibits endothelial cell migration and promotes endothelial tube formation via homotypic interactions (PubMed:23169771). Required for normal organization of the lymph vessel network (PubMed:23169771). Required for normal hematopoietic stem cell engraftment in the bone marrow (PubMed:24740813). Plays a role in hematopoiesis; required for normal numbers of hematopoietic stem cells in bone marrow (PubMed:25730656). Promotes in vitro osteoblast proliferation and differentiation (PubMed:25730656). Promotes neurite extension, axon growth and axon guidance; axons grow preferentially on surfaces that contain ALCAM (By similarity). Mediates outgrowth and pathfinding for retinal ganglion cell axons (PubMed:15345243). {ECO:0000250|UniProtKB:P42292, ECO:0000250|UniProtKB:Q13740, ECO:0000269|PubMed:15345243, ECO:0000269|PubMed:23169771}. PTM: Glycosylated. {ECO:0000250|UniProtKB:Q13740}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15345243, ECO:0000269|PubMed:16914752, ECO:0000269|PubMed:23169771, ECO:0000269|PubMed:9209500}; Single-pass type I membrane protein {ECO:0000305}. Cell projection, axon {ECO:0000269|PubMed:15345243}. Cell projection, dendrite {ECO:0000269|PubMed:15345243}. Note=Detected at the immunological synapse, i.e, at the contact zone between antigen-presenting dendritic cells and T-cells. Colocalizes with CD6 and the TCR/CD3 complex at the immunological synapse. {ECO:0000250|UniProtKB:Q13740}. SUBUNIT: Homodimer (By similarity). Interacts (via extracellular domain) with CD6 (via extracellular domain) (PubMed:9209500, PubMed:16914752). Homodimerization and interaction with CD6 involve the same region and cannot occur simultaneously. The affinity for CD6 is much higher than the affinity for self-association. Interacts (via glycosylated extracellular domain) with LGALS1 and LGALS3. Interaction with LGALS1 or LGALS3 inhibits interaction with CD6. {ECO:0000250|UniProtKB:Q13740, ECO:0000269|PubMed:16914752, ECO:0000269|PubMed:9209500}. DOMAIN: The CD6 binding site is located in the N-terminal Ig-like domain. {ECO:0000269|PubMed:9209500}. TISSUE SPECIFICITY: Detected on brain motor neurons, in differentiating retinal ganglion cells and in adult retina (PubMed:15345243). Detected on leukocytes and on lymphatic endothelial cells (PubMed:23169771). Detected in spleen B cells and T-cells (at protein level) (PubMed:9209500). Detected in adult brain and embryonic spinal cord (PubMed:15345243). Expressed at high levels in the brain, and lung, and at lower levels in the liver, and the kidney, as well as by activated leukocytes (PubMed:9209500). {ECO:0000269|PubMed:15345243, ECO:0000269|PubMed:23169771, ECO:0000269|PubMed:9209500}. +Q922M5 CDA7L_MOUSE Cell division cycle-associated 7-like protein (Transcription factor RAM2) 438 50,248 Chain (1); Cross-link (2); Modified residue (11); Region (2) FUNCTION: Plays a role in transcriptional regulation as a repressor that inhibits monoamine oxidase A (MAOA) activity and gene expression by binding to the promoter. Plays an important oncogenic role in mediating the full transforming effect of MYC in medulloblastoma cells (By similarity). Involved in apoptotic signaling pathways; May act downstream of P38-kinase and BCL-2, but upstream of CASP3/caspase-3 as well as CCND1/cyclin D1 and E2F1. {ECO:0000250, ECO:0000269|PubMed:16829576}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Associates with chromatin. Translocates from cytoplasm to nucleus under dexamethasone induction (By similarity). {ECO:0000250}. SUBUNIT: Interacts with MYC and PSIP1. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in all tissues but not detected in total brain. {ECO:0000269|PubMed:15994933}. +P50283 CD7_MOUSE T-cell antigen CD7 (CD antigen CD7) 210 23,153 Chain (1); Disulfide bond (1); Domain (1); Glycosylation (3); Lipidation (1); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 151 171 Helical. {ECO:0000255}. TOPO_DOM 24 150 Extracellular. {ECO:0000255}.; TOPO_DOM 172 210 Cytoplasmic. {ECO:0000255}. FUNCTION: Not yet known. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Interacts with SECTM1. {ECO:0000269|PubMed:10652336}. +P27548 CD40L_MOUSE CD40 ligand (CD40-L) (T-cell antigen Gp39) (TNF-related activation protein) (TRAP) (Tumor necrosis factor ligand superfamily member 5) (CD antigen CD154) [Cleaved into: CD40 ligand, membrane form; CD40 ligand, soluble form] 260 29,370 Chain (2); Disulfide bond (1); Glycosylation (1); Sequence conflict (1); Site (1); Topological domain (2); Transmembrane (1) TRANSMEM 23 46 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 22 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 47 260 Extracellular. {ECO:0000255}. FUNCTION: Cytokine that binds to CD40/TNFRSF5. Costimulates T-cell proliferation and cytokine production. Its cross-linking on T-cells generates a costimulatory signal which enhances the production of IL4 and IL10 in conjunction with the TCR/CD3 ligation and CD28 costimulation. Induces the activation of NF-kappa-B and kinases MAPK8 and PAK2 in T-cells (By similarity). Mediates B-cell proliferation in the absence of co-stimulus as well as IgE production in the presence of IL4. Involved in immunoglobulin class switching (PubMed:1374165). {ECO:0000250|UniProtKB:P29965, ECO:0000269|PubMed:1374165}.; FUNCTION: Release of soluble CD40L from platelets is partially regulated by GP IIb/IIIa, actin polymerization, and a matrix metalloproteinases (MMP) inhibitor-sensitive pathway. {ECO:0000250|UniProtKB:P29965}. PTM: The soluble form derives from the membrane form by proteolytic processing. {ECO:0000250|UniProtKB:P29965}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P29965}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P29965}. Cell surface {ECO:0000250|UniProtKB:P29965}.; SUBCELLULAR LOCATION: CD40 ligand, soluble form: Secreted {ECO:0000250|UniProtKB:P29965}. SUBUNIT: Homotrimer (PubMed:8095800). Interacts with CD28 (By similarity). {ECO:0000250|UniProtKB:P29965, ECO:0000303|PubMed:8095800}. TISSUE SPECIFICITY: Specifically expressed on activated CD4+ T-lymphocytes. +Q8VE98 CD276_MOUSE CD276 antigen (B7 homolog 3) (B7-H3) (Costimulatory molecule) (CD antigen CD276) 316 34,001 Beta strand (13); Chain (1); Disulfide bond (1); Domain (2); Glycosylation (3); Helix (2); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (4) TRANSMEM 249 269 Helical. {ECO:0000255}. TOPO_DOM 29 248 Extracellular. {ECO:0000255}.; TOPO_DOM 270 316 Cytoplasmic. {ECO:0000255}. FUNCTION: Modulates T-cell-mediated immune responses and the development of acute and chronic transplant rejection. Plays a positive regulatory role in bone formation and has a dual role in the bone-immune interface. Induces antitumor immunity as it activates both acquired and innate immunity leading to natural killer cell and CD8 T-cell dependent killing of tumor cells. {ECO:0000269|PubMed:12055244, ECO:0000269|PubMed:12925852, ECO:0000269|PubMed:12939639, ECO:0000269|PubMed:15294965, ECO:0000269|PubMed:15682454}. SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Interacts with TREML2 and this interaction enhances T-cell activation. {ECO:0000250}. TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12055244}. +Q9QWK4 CD5L_MOUSE CD5 antigen-like (Apoptosis inhibitor expressed by macrophages) (mAIM) (Apoptosis inhibitory 6) (SP-alpha) 352 38,863 Chain (1); Disulfide bond (11); Domain (3); Glycosylation (2); Mutagenesis (3); Natural variant (3); Sequence conflict (2); Signal peptide (1); Site (1) FUNCTION: Secreted protein that acts as a key regulator of lipid synthesis: mainly expressed by macrophages in lymphoid and inflammed tissues and regulates mechanisms in inflammatory responses, such as infection or atherosclerosis (PubMed:26048980). Able to inhibit lipid droplet size in adipocytes (PubMed:20519120, PubMed:22579686). Following incorporation into mature adipocytes via CD36-mediated endocytosis, associates with cytosolic FASN, inhibiting fatty acid synthase activity and leading to lipolysis, the degradation of triacylglycerols into glycerol and free fatty acids (FFA) (PubMed:20519120). CD5L-induced lipolysis occurs with progression of obesity: participates in obesity-associated inflammation following recruitment of inflammatory macrophages into adipose tissues, a cause of insulin resistance and obesity-related metabolic disease (PubMed:21730133). Regulation of intracellular lipids mediated by CD5L has a direct effect on transcription regulation mediated by nuclear receptors ROR-gamma (RORC) (PubMed:22579686, PubMed:26607793). Acts as a key regulator of metabolic switch in T-helper Th17 cells (PubMed:26607794, PubMed:26607793). Regulates the expression of pro-inflammatory genes in Th17 cells by altering the lipid content and limiting synthesis of cholesterol ligand of RORC, the master transcription factor of Th17-cell differentiation (PubMed:26607793). CD5L is mainly present in non-pathogenic Th17 cells, where it decreases the content of polyunsaturated fatty acyls (PUFA), affecting two metabolic proteins MSMO1 and CYP51A1, which synthesize ligands of RORC, limiting RORC activity and expression of pro-inflammatory genes (PubMed:26607793). Participates in obesity-associated autoimmunity via its association with IgM, interfering with the binding of IgM to Fcalpha/mu receptor and enhancing the development of long-lived plasma cells that produce high-affinity IgG autoantibodies (PubMed:23562157). Also acts as an inhibitor of apoptosis in macrophages: promotes macrophage survival from the apoptotic effects of oxidized lipids in case of atherosclerosis (PubMed:9892623, PubMed:16054063). Involved in early response to microbial infection against various pathogens by acting as a pattern recognition receptor and by promoting autophagy (By similarity). {ECO:0000250|UniProtKB:O43866, ECO:0000269|PubMed:16054063, ECO:0000269|PubMed:20519120, ECO:0000269|PubMed:21730133, ECO:0000269|PubMed:22579686, ECO:0000269|PubMed:23562157, ECO:0000269|PubMed:26607793, ECO:0000269|PubMed:26607794, ECO:0000269|PubMed:9892623, ECO:0000303|PubMed:26048980}. PTM: N-glycosylated (PubMed:10651944, PubMed:23236605). N-glycan at Asn-99 possesses only alpha2,6-sialylated terminals, while Asn-229 possesses both alpha2,6-sialylated and non-sialylated terminals (PubMed:23236605). N-glycosylation increases secretion. {ECO:0000269|PubMed:10651944, ECO:0000269|PubMed:23236605}. SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20519120, ECO:0000269|PubMed:23236605, ECO:0000269|PubMed:9892623}. Cytoplasm {ECO:0000269|PubMed:20519120}. Note=Secreted by macrophages and circulates in the blood (PubMed:20519120). Transported in the cytoplasm via CD36-mediated endocytosis (PubMed:20519120). {ECO:0000269|PubMed:20519120}. SUBUNIT: Interacts with FASN; the interaction is direct (PubMed:20519120). Interacts with IgM; protecting CD5L from renal excretion and leading to increased CD5L levels in circulating blood (PubMed:23562157). {ECO:0000269|PubMed:20519120, ECO:0000269|PubMed:23562157}. TISSUE SPECIFICITY: Specifically expressed in tissue macrophages (PubMed:9892623). Expressed in thymus, liver, spleen and lymph nodes (PubMed:10651944). Present in Th17 cells; mainly present in non-pathogenic Th17 cells (PubMed:26607793). {ECO:0000269|PubMed:10651944, ECO:0000269|PubMed:26607793, ECO:0000269|PubMed:9892623}. +P41272 CD27_MOUSE CD27 antigen (CD27L receptor) (T-cell activation antigen CD27) (Tumor necrosis factor receptor superfamily member 7) (CD antigen CD27) 250 28,164 Chain (1); Disulfide bond (8); Glycosylation (2); Repeat (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 183 203 Helical. {ECO:0000255}. TOPO_DOM 24 182 Extracellular. {ECO:0000255}.; TOPO_DOM 204 250 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor for CD70/CD27L. May play a role in survival of activated T-cells. May play a role in apoptosis through association with SIVA1. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SUBUNIT: Homodimer. Interacts with SIVA1 and TRAF2 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: In thymus and spleen, but not in non-lymphoid tissues. +O88324 CD83_MOUSE CD83 antigen (mCD83) (CD antigen CD83) 196 21,313 Chain (1); Disulfide bond (1); Domain (1); Glycosylation (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 134 154 Helical. {ECO:0000255}. TOPO_DOM 22 133 Extracellular. {ECO:0000255}.; TOPO_DOM 155 196 Cytoplasmic. {ECO:0000255}. FUNCTION: May play a significant role in antigen presentation or the cellular interactions that follow lymphocyte activation. {ECO:0000250}. SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Monomer. {ECO:0000250}. TISSUE SPECIFICITY: Abundantly expressed in spleen and brain, but is also detected in most tissues analyzed. {ECO:0000269|PubMed:9799334}. +P42082 CD86_MOUSE T-lymphocyte activation antigen CD86 (Activation B7-2 antigen) (Early T-cell costimulatory molecule 1) (ETC-1) (CD antigen CD86) 309 34,666 Alternative sequence (1); Chain (1); Disulfide bond (2); Domain (2); Erroneous initiation (1); Glycosylation (9); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 245 265 Helical. {ECO:0000255}. TOPO_DOM 24 244 Extracellular. {ECO:0000255}.; TOPO_DOM 266 309 Cytoplasmic. {ECO:0000255}. FUNCTION: Receptor involved in the costimulatory signal essential for T-lymphocyte proliferation and interleukin-2 production, by binding CD28 or CTLA-4. May play a critical role in the early events of T-cell activation and costimulation of naive T-cells, such as deciding between immunity and anergy that is made by T-cells within 24 hours after activation. PTM: Polyubiquitinated; which is promoted by MARCH8 and results in endocytosis and lysosomal degradation. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. SUBUNIT: Homodimer. Interacts with MARCH8 (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed on activated B-cells. +Q9CWK3 CD2B2_MOUSE CD2 antigen cytoplasmic tail-binding protein 2 (CD2 cytoplasmic domain-binding protein 2) (CD2 tail-binding protein 2) 342 37,694 Chain (1); Cross-link (1); Domain (1); Modified residue (5) FUNCTION: Involved in pre-mRNA splicing as component of the U5 snRNP complex that is involved in spliceosome assembly. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Predominantly nuclear. {ECO:0000250}. SUBUNIT: Component of the U5 snRNP complex composed of the U5 snRNA and at least PRPF6, PRPF8, SNRNP200, EFTUD2, SNRNP40, DDX23, TXNL4A and CD2BP2. Interacts directly with TXNL4A and PRPF6. Interacts (via GYF domain) with CD2 (via Pro-rich sequence in the cytoplasmic domain). Interacts with PQBP1 (By similarity). {ECO:0000250}. +Q8BGZ4 CDC23_MOUSE Cell division cycle protein 23 homolog (Anaphase-promoting complex subunit 8) (APC8) (Cyclosome subunit 8) 597 68,562 Alternative sequence (1); Chain (1); Cross-link (1); Initiator methionine (1); Modified residue (9); Repeat (13); Sequence conflict (2) Protein modification; protein ubiquitination. FUNCTION: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By similarity). {ECO:0000250}. PTM: Phosphorylated. Phosphorylation on Thr-562 occurs specifically during mitosis (By similarity). {ECO:0000250}. SUBUNIT: The mammalian APC/C is composed at least of 14 distinct subunits ANAPC1, ANAPC2, CDC27/APC3, ANAPC4, ANAPC5, CDC16/APC6, ANAPC7, CDC23/APC8, ANAPC10, ANAPC11, CDC26/APC12, ANAPC13, ANAPC15 and ANAPC16 that assemble into a complex of at least 19 chains with a combined molecular mass of around 1.2 MDa; APC/C interacts with FZR1 and FBXO5. {ECO:0000250|UniProtKB:Q9UJX2}. +P08920 CD2_MOUSE T-cell surface antigen CD2 (LFA-2) (LFA-3 receptor) (Lymphocyte antigen 37) (Ly-37) (T-cell surface antigen T11/Leu-5) (CD antigen CD2) 344 38,415 Chain (1); Compositional bias (1); Disulfide bond (2); Domain (2); Glycosylation (4); Region (2); Sequence conflict (10); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 204 229 Helical. {ECO:0000255}. TOPO_DOM 23 203 Extracellular. {ECO:0000255}.; TOPO_DOM 230 344 Cytoplasmic. {ECO:0000255}. FUNCTION: CD2 interacts with lymphocyte function-associated antigen CD58 (LFA-3) and CD48/BCM1 to mediate adhesion between T-cells and other cell types. CD2 is implicated in the triggering of T-cells, the cytoplasmic domain is implicated in the signaling function. PTM: N-glycosylated. {ECO:0000269|PubMed:2440689}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2440689}; Single-pass type I membrane protein {ECO:0000305}. SUBUNIT: Interacts with CD48 (By similarity). Interacts with CD58 (LFA-3) (By similarity). Interacts with CD2AP (PubMed:9741631). Interacts with PSTPIP1 (PubMed:12530983). {ECO:0000250|UniProtKB:P06729, ECO:0000250|UniProtKB:P08921, ECO:0000269|PubMed:12530983, ECO:0000269|PubMed:9741631}. TISSUE SPECIFICITY: Detected in thymus and spleen. {ECO:0000269|PubMed:2440689}. +Q99JP4 CDC26_MOUSE Anaphase-promoting complex subunit CDC26 (Cell division cycle protein 26 homolog) 85 9,761 Chain (1); Coiled coil (1); Modified residue (1) Protein modification; protein ubiquitination. FUNCTION: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. May recruit the E2 ubiquitin-conjugating enzymes to the complex (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SUBUNIT: V-shaped homodimer. Interacts with CDC16. The mammalian APC/C is composed at least of 14 distinct subunits ANAPC1, ANAPC2, CDC27/APC3, ANAPC4, ANAPC5, CDC16/APC6, ANAPC7, CDC23/APC8, ANAPC10, ANAPC11, CDC26/APC12, ANAPC13, ANAPC15 and ANAPC16 that assemble into a complex of at least 19 chains with a combined molecular mass of around 1.2 MDa; APC/C interacts with FZR1 and FBXO5. {ECO:0000250|UniProtKB:Q8NHZ8}. +O55237 CD70_MOUSE CD70 antigen (CD27 ligand) (CD27-L) (Tumor necrosis factor ligand superfamily member 7) (CD antigen CD70) 195 21,919 Chain (1); Disulfide bond (1); Glycosylation (3); Topological domain (2); Transmembrane (1) TRANSMEM 24 44 Helical; Signal-anchor for type II membrane protein. {ECO:0000255}. TOPO_DOM 1 23 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 45 195 Extracellular. {ECO:0000255}. FUNCTION: Cytokine that binds to CD27. Plays a role in T-cell activation. Induces the proliferation of costimulated T-cells and enhances the generation of cytolytic T-cells. {ECO:0000269|PubMed:9620608}. PTM: N-glycosylated. SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. SUBUNIT: Homotrimer. {ECO:0000305}. TISSUE SPECIFICITY: Very low level of expression. Detected in splenocytes and thymocytes. +P40240 CD9_MOUSE CD9 antigen (CD antigen CD9) 226 25,258 Chain (1); Disulfide bond (2); Glycosylation (1); Lipidation (6); Mutagenesis (2); Topological domain (5); Transmembrane (4) TRANSMEM 13 33 Helical. {ECO:0000255}.; TRANSMEM 54 74 Helical. {ECO:0000255}.; TRANSMEM 86 109 Helical. {ECO:0000255}.; TRANSMEM 194 219 Helical. {ECO:0000255}. TOPO_DOM 1 12 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 34 53 Extracellular. {ECO:0000255}.; TOPO_DOM 75 85 Cytoplasmic. {ECO:0000255}.; TOPO_DOM 110 193 Extracellular. {ECO:0000255}.; TOPO_DOM 220 226 Cytoplasmic. {ECO:0000255}. FUNCTION: Integral membrane protein associated with integrins, which regulates different processes, such as sperm-egg fusion, platelet activation and aggregation, and cell adhesion (PubMed:10700183, PubMed:10634790, PubMed:10634791, PubMed:14715942). Present at the cell surface of oocytes and plays a key role in sperm-egg fusion, possibly by organizing multiprotein complexes and the morphology of the membrane required for the fusion (PubMed:10700183, PubMed:10634790, PubMed:10634791, PubMed:21690351). Acts as a receptor for PSG17 (PubMed:11805154). Involved in platelet activation and aggregation (PubMed:14715942). Regulates paranodal junction formation (PubMed:14715942). Involved in cell adhesion, cell motility and tumor metastasis (By similarity). {ECO:0000250|UniProtKB:P21926, ECO:0000269|PubMed:10634790, ECO:0000269|PubMed:10634791, ECO:0000269|PubMed:10700183, ECO:0000269|PubMed:11805154, ECO:0000269|PubMed:14715942, ECO:0000269|PubMed:21690351}. PTM: Palmitoylated at a low, basal level in unstimulated platelets. The level of palmitoylation increases when platelets are activated by thrombin (in vitro). The protein exists in three forms with molecular masses between 22 and 27 kDa, and is known to carry covalently linked fatty acids. {ECO:0000250|UniProtKB:P21926}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10518536, ECO:0000269|PubMed:10634791, ECO:0000269|PubMed:11805154, ECO:0000269|PubMed:23213457}; Multi-pass membrane protein {ECO:0000269|PubMed:11805154}. Membrane {ECO:0000269|PubMed:11805154}; Multi-pass membrane protein {ECO:0000269|PubMed:11805154}. Secreted, exosome {ECO:0000269|PubMed:26109643}. Note=Present at the cell surface of oocytes (PubMed:10518536, PubMed:10634791, PubMed:23213457). Accumulates in the adhesion area between the sperm and egg following interaction between IZUMO1 and its receptor IZUMO1R/JUNO (PubMed:25209248). {ECO:0000269|PubMed:10518536, ECO:0000269|PubMed:10634791, ECO:0000269|PubMed:23213457, ECO:0000269|PubMed:25209248}. SUBUNIT: Forms both disulfide-linked homodimers and higher homooligomers as well as heterooligomers with other members of the tetraspanin family (By similarity). Interacts (via the second extracellular domain) with integrin ITGAV:ITGB3 (By similarity). Interacts with integrin ITGA6:ITGB1; interaction takes place in oocytes and is involved in sperm-egg fusion (PubMed:10634791). Interacts with CD63; identified in a complex with CD63 and ITGB3 (By similarity). Associates with CR2/CD21 and with PTGFRN/CD9P1 (By similarity). Interacts directly with IGSF8 (By similarity). Interacts with PDPN; this interaction is homophilic and attenuates platelet aggregation and pulmonary metastasis induced by PDPN (By similarity). {ECO:0000250|UniProtKB:P21926, ECO:0000269|PubMed:10634791}. TISSUE SPECIFICITY: Expressed predominantly in the peripheral nervous system (PubMed:14715942). Highly expressed in oocytes and blastocysts (at protein level) (PubMed:10518536, PubMed:10634790, PubMed:10634791, PubMed:23213457). Expression is also observed on follicular oocytes in the ovary, whereas no expression is found on follicular cells (at protein level) (PubMed:10518536, PubMed:10634790). {ECO:0000269|PubMed:10518536, ECO:0000269|PubMed:10634790, ECO:0000269|PubMed:10634791, ECO:0000269|PubMed:14715942, ECO:0000269|PubMed:23213457}. +Q8K0D0 CDK17_MOUSE Cyclin-dependent kinase 17 (EC 2.7.11.22) (Cell division protein kinase 17) (PCTAIRE-motif protein kinase 2) (Serine/threonine-protein kinase PCTAIRE-2) 523 59,506 Active site (1); Alternative sequence (2); Binding site (1); Chain (1); Domain (1); Erroneous initiation (1); Modified residue (8); Nucleotide binding (1) FUNCTION: May play a role in terminally differentiated neurons. Has a Ser/Thr-phosphorylating activity for histone H1 (By similarity). {ECO:0000250}. SUBUNIT: Found in a complex containing CABLES1, CDK16 and TDRD7. Interacts with TDRD7. {ECO:0000269|PubMed:11527406}. +Q91WE6 CDKAL_MOUSE Threonylcarbamoyladenosine tRNA methylthiotransferase (EC 2.8.4.5) (CDK5 regulatory subunit-associated protein 1-like 1) (tRNA-t(6)A37 methylthiotransferase) 578 65,289 Alternative sequence (7); Chain (1); Domain (2); Metal binding (6); Modified residue (2); Transmembrane (1) TRANSMEM 553 570 Helical. {ECO:0000255}. FUNCTION: Catalyzes the methylthiolation of N6-threonylcarbamoyladenosine (t(6)A), leading to the formation of 2-methylthio-N6-threonylcarbamoyladenosine (ms(2)t(6)A) at position 37 in tRNAs that read codons beginning with adenine. {ECO:0000250|UniProtKB:Q5VV42}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=Is a tail-anchored protein that exploits the TCR40 assisted pathway for insertion into the endoplasmic reticulum. {ECO:0000250}. TISSUE SPECIFICITY: Expressed in pancreas, liver and skeletal muscle, especially in white muscle fibers. {ECO:0000269|PubMed:23048041}. +E9Q7P9 CDHR2_MOUSE Cadherin-related family member 2 1308 142,633 Beta strand (25); Chain (1); Domain (9); Helix (4); Modified residue (2); Region (1); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (5) TRANSMEM 1153 1173 Helical. {ECO:0000255}. TOPO_DOM 21 1152 Extracellular. {ECO:0000305}.; TOPO_DOM 1174 1308 Cytoplasmic. {ECO:0000305}. FUNCTION: Intermicrovillar adhesion molecule that forms, via its extracellular domain, calcium-dependent heterophilic complexes with CDHR5 on adjacent microvilli. Thereby, controls the packing of microvilli at the apical membrane of epithelial cells. Through its cytoplasmic domain, interacts with microvillus cytoplasmic proteins to form the intermicrovillar adhesion complex/IMAC. This complex plays a central role in microvilli and epithelial brush border differentiation. May also play a role in cell-cell adhesion and contact inhibition in epithelial cells. {ECO:0000250|UniProtKB:Q9BYE9}. SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:Q9BYE9}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9BYE9}. Cell projection, microvillus membrane {ECO:0000250|UniProtKB:Q9BYE9}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9BYE9}. Cell junction {ECO:0000250|UniProtKB:Q9BYE9}. SUBUNIT: Part of the IMAC/intermicrovillar adhesion complex/intermicrovillar tip-link complex composed of ANKS4B, MYO7B, USH1C, CDHR2 and CDHR5. Interacts with MAST2 (By similarity). Interacts (via cytoplasmic domain) with USH1C and MYO7B; required for proper localization of CDHR2 to microvilli tips and its function in brush border differentiation (Probable). {ECO:0000250|UniProtKB:Q9BYE9, ECO:0000305|PubMed:26812017}. DOMAIN: The cadherin 1 domain is required for binding to CDHR5. {ECO:0000250|UniProtKB:Q9BYE9}. +P60766 CDC42_MOUSE Cell division control protein 42 homolog (G25K GTP-binding protein) 191 21,259 Alternative sequence (2); Beta strand (7); Chain (1); Helix (10); Lipidation (1); Modified residue (2); Motif (1); Mutagenesis (3); Nucleotide binding (3); Propeptide (1); Sequence conflict (5); Turn (2) FUNCTION: Plasma membrane-associated small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses. Involved in epithelial cell polarization processes. Regulates the bipolar attachment of spindle microtubules to kinetochores before chromosome congression in metaphase. Plays a role in the extension and maintenance of the formation of thin, actin-rich surface projections called filopodia. Mediates CDC42-dependent cell migration (By similarity). Required for DOCK10-mediated spine formation in Purkinje cells and hippocampal neurons (PubMed:25851601). Facilitates filopodia formation upon DOCK11-activation (PubMed:22494997). Also plays a role in phagocytosis through organization of the F-actin cytoskeleton associated with forming phagocytic cups (By similarity). {ECO:0000250|UniProtKB:P60953, ECO:0000269|PubMed:22494997, ECO:0000269|PubMed:25851601}. PTM: Phosphorylated by SRC in an EGF-dependent manner, this stimulates the binding of the Rho-GDP dissociation inhibitor RhoGDI. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22461490}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Midbody {ECO:0000250|UniProtKB:P60953}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P60953}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P60953}. Cytoplasm {ECO:0000269|PubMed:22461490}. Cell projection, lamellipodium membrane {ECO:0000269|PubMed:22461490}; Peripheral membrane protein {ECO:0000305|PubMed:22461490}; Cytoplasmic side {ECO:0000305|PubMed:22461490}. Note=Localizes to spindle during prometaphase cells (By similarity). Moves to the central spindle as cells progressed through anaphase to telophase. Localizes at the end of cytokinesis in the intercellular bridge formed between two daughter cells (By similarity). Its localization is regulated by the activities of guanine nucleotide exchange factor ECT2 and GTPase activating protein RACGAP1. Colocalizes with NEK6 in the centrosome (By similarity). In its active GTP-bound form localizes to the leading edge membrane of migrating dendritic cells (PubMed:22461490). {ECO:0000250|UniProtKB:P60953, ECO:0000269|PubMed:22461490}. SUBUNIT: Interacts with CDC42EP1, CDC42EP2, CDC42EP3, CDC42EP4, CDC42EP5, CDC42SE1, CDC42SE2, PARD6A, PARD6B and PARD6G (in a GTP-dependent manner) (PubMed:10490598, PubMed:10934474). Interacts with activated CSPG4 and with BAIAP2 (By similarity). Interacts with DOCK11/Zizimin2; the interaction activates CDC42 by exchanging GDP for GTP (PubMed:15710388, PubMed:16968698). Interacts with DOCK9; the interaction activates CDC42 by exchanging GDP for GTP (By similarity). Interacts with DOCK8 (via DHR-2 domain); the interaction activates CDC42 by exchanging GDP for GTP (PubMed:22461490). Interacts with IQGAP1 (PubMed:16968698). Interacts with NET1 and ARHGAP33/TCGAP (PubMed:9535835, PubMed:12773384). Part of a complex with PARD3, PARD6A or PARD6B and PRKCI or PRKCZ (PubMed:10934474). The GTP-bound form interacts with CCPG1 (PubMed:17000758). Interacts with USP6 (By similarity). Interacts with NEK6 (By similarity). Part of a collagen stimulated complex involved in cell migration composed of CDC42, CRK, TNK2 and BCAR1/p130cas (By similarity). Interacts with ITGB1BP1 (By similarity). Interacts with ARHGDIA; this interaction inactivates and stabilizes CDC42. Interacts with ARHGDIB; this maintains CDC42 in the inactive, GDP-bound form (By similarity). Interacts in (GTP-bound form) with FNBP1L and ABI1, but only in the presence of FNBP1L (By similarity). {ECO:0000250|UniProtKB:P60953, ECO:0000269|PubMed:10490598, ECO:0000269|PubMed:10934474, ECO:0000269|PubMed:12773384, ECO:0000269|PubMed:15710388, ECO:0000269|PubMed:16968698, ECO:0000269|PubMed:17000758, ECO:0000269|PubMed:22461490, ECO:0000269|PubMed:9535835}. +P51480 CDN2A_MOUSE Cyclin-dependent kinase inhibitor 2A (Cyclin-dependent kinase 4 inhibitor A) (CDK4I) (p16-INK4a) (p16-INK4) 168 17,941 Alternative sequence (1); Chain (1); Modified residue (2); Mutagenesis (3); Natural variant (10); Repeat (4); Sequence conflict (1) FUNCTION: Acts as a negative regulator of the proliferation of normal cells by interacting strongly with CDK4 and CDK6. This inhibits their ability to interact with cyclins D and to phosphorylate the retinoblastoma protein. PTM: Phosphorylation seems to increase interaction with CDK4. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. SUBUNIT: Heterodimer with CDK4 or CDK6. Predominamt P16 complexes contained CDK6. Interacts with CDK4 (both 'T-172'-phosphorylated and non-phosphorylated forms); the interaction inhibits cyclin D-CDK4 kinase activity. Interacts with ISCO2 (By similarity). {ECO:0000250}. +Q3TZA2 CDKL4_MOUSE Cyclin-dependent kinase-like 4 (EC 2.7.11.22) 342 39,446 Active site (1); Binding site (1); Chain (1); Domain (1); Motif (1); Nucleotide binding (1) SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. DOMAIN: The [NKR]KIAxRE motif seems to be a cyclin-binding region. +Q3V2D2 CE046_MOUSE Uncharacterized protein C5orf46 homolog 93 10,038 Chain (1); Signal peptide (1) SUBCELLULAR LOCATION: Secreted {ECO:0000305}. +Q3UKK2 CEAM5_MOUSE Carcinoembryonic antigen-related cell adhesion molecule 5 (Pregnancy-specific glycoprotein 30) 947 106,270 Chain (1); Disulfide bond (1); Domain (8); Glycosylation (13); Signal peptide (1) FUNCTION: Cell surface glycoprotein that plays a role in cell adhesion, intracellular signaling and tumor progression. Mediates homophilic and heterophilic cell adhesion with other carcinoembryonic antigen-related cell adhesion molecules, such as CEACAM6. Plays a role as an oncogene by promoting tumor progression; induces resistance to anoikis of colorectal carcinoma cells. {ECO:0000250|UniProtKB:P06731}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P06731}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P06731}. Apical cell membrane {ECO:0000250|UniProtKB:P06731}. Cell surface {ECO:0000250|UniProtKB:P06731}. Note=Localized to the apical glycocalyx surface. {ECO:0000250|UniProtKB:P06731}. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P06731}. +Q9D2Z1 CEA20_MOUSE Carcinoembryonic antigen-related cell adhesion molecule 20 577 63,444 Chain (1); Disulfide bond (3); Domain (4); Glycosylation (3); Modified residue (2); Mutagenesis (2); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1) TRANSMEM 431 451 Helical. {ECO:0000255}. TOPO_DOM 31 430 Extracellular. {ECO:0000305}.; TOPO_DOM 452 577 Cytoplasmic. {ECO:0000305}. FUNCTION: Together with the tyrosine-protein kinase SYK, enhances production of the cytokine CXCL8/IL-8 via the NFKB pathway and may thus have a role in the intestinal immune response. {ECO:0000269|PubMed:26195794}. PTM: Phosphorylated on tyrosine residues by SYK, SRC and FYN in vitro. {ECO:0000269|PubMed:26195794}. SUBCELLULAR LOCATION: Cell projection, microvillus membrane {ECO:0000269|PubMed:25908210, ECO:0000269|PubMed:26195794}; Single-pass type I membrane protein {ECO:0000305}. Apical cell membrane {ECO:0000269|PubMed:25908210, ECO:0000269|PubMed:26195794}; Single-pass type I membrane protein {ECO:0000305}. Note=Colocalizes with PTPRH and CEACAM1 at the apical brush border of intestinal cells. {ECO:0000269|PubMed:25908210, ECO:0000269|PubMed:26195794}. SUBUNIT: Interacts (via extracellular domain) with PTPRH (via extracellular domain); the interaction dephosphorylates CEACAM20. Interacts (phosphorylated form) with SYK (via SH2 domains); the interaction further enhances CEACAM20 phosphorylation. {ECO:0000269|PubMed:26195794}. TISSUE SPECIFICITY: Strongly expressed in the small intestine and colon (at protein level) (PubMed:25908210, PubMed:26195794). Minimal expression in other tissues (at protein level) (PubMed:26195794). Highly expressed in cecum, colon, ileum, jejunum, and testis, and also detected at lower levels in salivary gland and thymus (PubMed:16139472). {ECO:0000269|PubMed:16139472, ECO:0000269|PubMed:25908210, ECO:0000269|PubMed:26195794}. +Q9CQA0 CENPM_MOUSE Centromere protein M (CENP-M) (Proliferation-associated nuclear element protein 1) 180 20,039 Alternative sequence (1); Chain (1); Sequence conflict (4) FUNCTION: Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres (By similarity). {ECO:0000250}. SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12881717}. Cytoplasm {ECO:0000269|PubMed:12881717}. Chromosome, centromere, kinetochore {ECO:0000250}. Note=Nuclear in non-confluent cells and cytoplasmic in confluent or dividing cells. Localizes in the kinetochore domain of centromeres (By similarity). {ECO:0000250}. SUBUNIT: Component of the CENPA-NAC complex, at least composed of CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and CENPU. The CENPA-NAC complex interacts with the CENPA-CAD complex, composed of CENPI, CENPK, CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS (By similarity). {ECO:0000250}. +Q9D084 CENPS_MOUSE Centromere protein S (CENP-S) (Apoptosis-inducing TAF9-like domain-containing protein 1 homolog) (FANCM-interacting histone fold protein 1) 142 16,335 Alternative sequence (2); Chain (1); Frameshift (2) FUNCTION: DNA-binding component of the Fanconi anemia (FA) core complex. Required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. In complex with CENPX (MHF heterodimer), crucial cofactor for FANCM in both binding and ATP-dependent remodeling of DNA. Stabilizes FANCM. In complex with CENPX and FANCM (but not other FANC proteins), rapidly recruited to blocked forks and promotes gene conversion at blocked replication forks. In complex with CENPT, CENPW and CENPX (CENP-T-W-S-X heterotetramer), involved in the formation of a functional kinetochore outer plate, which is essential for kinetochore-microtubule attachment and faithful mitotic progression. As a component of MHF and CENP-T-W-S-X complexes, binds DNA and bends it to form a nucleosome-like structure. DNA-binding function is fulfilled in the presence of CENPX, with the following preference for DNA substates: Holliday junction > double-stranded > splay arm > single-stranded. Does not bind DNA on its own. {ECO:0000250|UniProtKB:Q8N2Z9}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8N2Z9}. Chromosome, centromere {ECO:0000250|UniProtKB:Q8N2Z9}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q8N2Z9}. Note=Assembly of CENPS and CENPX and its partner subunits CENPT and CENPW at centromeres occurs through a dynamic exchange mechanism. Although exchange is continuous in the cell cycle, de novo assembly starts principally during mid-late S phase and is complete by G2. CENPS is more stably bound at the kinetochore than CENPX. During S phase, rapidly recruited to DNA interstrand cross-links that block replication. Recruited to DNA damage sites about 20 minutes following UV irradiation, reaching a plateau after approximately 40 minutes. {ECO:0000250|UniProtKB:Q8N2Z9}. SUBUNIT: Heterodimer with CENPX, sometimes called MHF; this interaction stabilizes both partners. MHF heterodimers can assemble to form tetrameric structures. MHF also coassemble with CENPT-CENPW heterodimers at centromeres to form the tetrameric CENP-T-W-S-X complex. Forms a discrete complex with FANCM and CENPX, called FANCM-MHF; this interaction, probably mediated by direct binding between CENPS and FANCM, leads to synergistic activation of double-stranded DNA binding and strongly stimulates FANCM-mediated DNA remodeling. Recruited by FANCM to the Fanconi anemia (FA) core complex, which consists of CENPS, CENPX, FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL, FANCM, FAAP24 and FAAP100. The FA core complex associates with Bloom syndrome (BLM) complex, which consists of at least BLM, DNA topoisomerase 3-alpha (TOP3A), RMI1/BLAP75, RPA1/RPA70 and RPA2/RPA32. The super complex between FA and BLM is called BRAFT. Component of the CENPA-CAD complex, composed of CENPI, CENPK, CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS. The CENPA-CAD complex is probably recruited on centromeres by the CENPA-NAC complex, at least composed of CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and CENPU. {ECO:0000250|UniProtKB:Q8N2Z9}. +Q9CZ62 CEP97_MOUSE Centrosomal protein of 97 kDa (Cep97) (Leucine-rich repeat and IQ domain-containing protein 2) 856 94,641 Alternative sequence (1); Chain (1); Domain (2); Frameshift (1); Modified residue (6); Region (1); Repeat (8) FUNCTION: Acts as a key negative regulator of ciliogenesis in collaboration with CCP110 by capping the mother centriole thereby preventing cilia formation. Required for recruitment of CCP110 to the centrosome (By similarity). {ECO:0000250|UniProtKB:Q8IW35}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q8IW35}. SUBUNIT: Interacts with CALM1, CEP76, CCP110, KIF24, TALPID3. Via its interaction with CCP110, may indirectly interact with HERC2 and NEURL4. {ECO:0000250|UniProtKB:Q8IW35}. +Q9CPQ5 CENPQ_MOUSE Centromere protein Q (CENP-Q) 267 30,501 Alternative sequence (2); Chain (1); Coiled coil (1); Erroneous initiation (5); Frameshift (1); Modified residue (1); Sequence conflict (8) FUNCTION: Component of the CENPA-CAD (nucleosome distal) complex, a complex recruited to centromeres which is involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation. May be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex. Plays an important role in chromosome congression and in the recruitment of CENP-O complex (which comprises CENPO, CENPP, CENPQ and CENPU), CENPE and PLK1 to the kinetochores. {ECO:0000250|UniProtKB:Q7L2Z9}. PTM: Phosphorylation at Ser-49 is essential for CENPE recruitment to kinetochores and orderly chromosome congression. {ECO:0000250|UniProtKB:Q7L2Z9}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q7L2Z9}. Chromosome, centromere {ECO:0000250|UniProtKB:Q7L2Z9}. Note=Localizes exclusively in the centromeres. The CENPA-CAD complex is probably recruited on centromeres by the CENPA-NAC complex. {ECO:0000250|UniProtKB:Q7L2Z9}. SUBUNIT: Component of the CENPA-CAD complex, composed of CENPI, CENPK, CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS. The CENPA-CAD complex interacts with the CENPA-NAC complex, at least composed of CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and CENPU. {ECO:0000250|UniProtKB:Q7L2Z9}. +Q569L8 CENPJ_MOUSE Centromere protein J (CENP-J) 1344 153,079 Chain (1); Modified residue (6); Region (2); Sequence conflict (1) FUNCTION: Plays an important role in cell division and centrosome function by participating in centriole duplication. Inhibits microtubule nucleation from the centrosome. Involved in the regulation of slow processive growth of centriolar microtubules. Acts as microtubule plus-end tracking protein that stabilizes centriolar microtubules and inhibits microtubule polymerization and extension from the distal ends of centrioles. Required for centriole elongation and for STIL-mediated centriole amplification. Required for the recruitment of CEP295 to the proximal end of new-born centrioles at the centriolar microtubule wall during early S phase in a PLK4-dependent manner. May be involved in the control of centriolar-microtubule growth by acting as a regulator of tubulin release (By similarity). {ECO:0000250|UniProtKB:Q9HC77}. PTM: Phosphorylation at Ser-577 and Ser-583 by PLK2 is required for procentriole formation and centriole elongation. Phosphorylation by PLK2 oscillates during the cell cycle: it increases at G1/S transition and decreases during the exit from mitosis. Phosphorylation at Ser-583 is also mediated by PLK4 but is not a critical step in PLK4 function in procentriole assembly. {ECO:0000250|UniProtKB:Q9HC77}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9HC77}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q9HC77}. Note=Localized within the center of microtubule asters. During centriole biogenesis, it is concentrated within the proximal lumen of both parental centrioles and procentrioles (By similarity). {ECO:0000250|UniProtKB:Q9HC77}. SUBUNIT: Forms homodimers. Associates with microtubules plus ends; binds to beta-tublin subunits exposed on microtubule outer surface at its distal tip; also associates with microtubule lattice. Associated with the gamma-tubulin complex. Interacts with the head domain of EPB41. Interacts with LYST. Interacts with CEP152 (via C-terminus). Interacts with STIL. Forms a complex with STIL and SASS6 (By similarity). {ECO:0000250|UniProtKB:Q9HC77}. +Q8C4X1 CENPX_MOUSE Centromere protein X (CENP-X) (FANCM-interacting histone fold protein 2) (Fanconi anemia-associated polypeptide of 10 kDa) (Immediate-early-response protein D9) (Retinoic acid-inducible gene D9 protein) (Stimulated by retinoic acid gene 13 protein homolog) 78 8,926 Alternative sequence (3); Chain (1); Modified residue (1); Sequence conflict (3) FUNCTION: DNA-binding component of the Fanconi anemia (FA) core complex. Required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. In complex with CENPS (MHF heterodimer), crucial cofactor for FANCM in both binding and ATP-dependent remodeling of DNA. Stabilizes FANCM. In complex with CENPS and FANCM (but not other FANC proteins), rapidly recruited to blocked forks and promotes gene conversion at blocked replication forks. In complex with CENPS, CENPT and CENPW (CENP-T-W-S-X heterotetramer), involved in the formation of a functional kinetochore outer plate, which is essential for kinetochore-microtubule attachment and faithful mitotic progression. As a component of MHF and CENP-T-W-S-X complexes, binds DNA and bends it to form a nucleosome-like structure. DNA-binding function is fulfilled in the presence of CENPS, with the following preference for DNA substates: Holliday junction > double-stranded > splay arm > single-stranded. Does not bind DNA on its own. {ECO:0000250|UniProtKB:A8MT69}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:A8MT69}. Chromosome, centromere {ECO:0000250|UniProtKB:A8MT69}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:A8MT69}. Note=Assembly of CENPS and CENPX and its partner subunits CENPT and CENPW at centromeres occurs through a dynamic exchange mechanism. Although exchange is continuous in the cell cycle, de novo assembly starts principally during mid-late S phase and is complete by G2. CENPX being less stably bound at the kinetochore than CENPS. {ECO:0000250|UniProtKB:A8MT69}. SUBUNIT: Heterodimer with CENPX, sometimes called MHF; this interaction stabilizes both partners. MHF heterodimers can assemble to form tetrameric structures. MHF also coassemble with CENPT-CENPW heterodimers at centromeres to form the tetrameric CENP-T-W-S-X complex. Forms a discrete complex with FANCM and CENPX, called FANCM-MHF; this interaction, probably mediated by direct binding between CENPS and FANCM, leads to synergistic activation of double-stranded DNA binding and strongly stimulates FANCM-mediated DNA remodeling. Recruited by FANCM to the Fanconi anemia (FA) core complex, which consists of CENPS, CENPX, FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL, FANCM, FAAP24 and FAAP100. The FA core complex associates with Bloom syndrome (BLM) complex, which consists of at least BLM, DNA topoisomerase 3-alpha (TOP3A), RMI1/BLAP75, RPA1/RPA70 and RPA2/RPA32. The super complex between FA and BLM is called BRAFT. {ECO:0000250|UniProtKB:A8MT69}. +Q3TT38 CF106_MOUSE Uncharacterized protein C6orf106 homolog 291 32,082 Chain (1); Modified residue (3); Sequence conflict (5) +Q8VCT4 CES1D_MOUSE Carboxylesterase 1D (Carboxylesterase 3) (EC 3.1.1.1) (EC 3.1.1.67) (Fatty acid ethyl ester synthase) (FAEE synthase) (Triacylglycerol hydrolase) (TGH) 565 61,788 Active site (3); Chain (1); Disulfide bond (2); Glycosylation (2); Modified residue (1); Motif (1); Sequence conflict (7); Signal peptide (1) FUNCTION: Major lipase in white adipose tissue. Involved in the metabolism of xenobiotics and of natural substrates. Hydrolyzes triacylglycerols and monoacylglycerols, with a preference for monoacylglycerols. The susceptibility of the substrate increases with decreasing acyl chain length of the fatty acid moiety. Catalyzes the synthesis of fatty acid ethyl esters. {ECO:0000269|PubMed:15220344}. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000269|PubMed:15220344}. Cytoplasm, cytosol {ECO:0000269|PubMed:15220344}. Lipid droplet {ECO:0000269|PubMed:15220344}. SUBUNIT: Homotrimer. {ECO:0000269|PubMed:15269189}. TISSUE SPECIFICITY: Highest expression occurs in liver with lower levels in adipose tissue, kidney, heart, intestine, lung, testis and thymus. {ECO:0000269|PubMed:11470237, ECO:0000269|PubMed:15269189}. +O35648 CETN3_MOUSE Centrin-3 167 19,519 Calcium binding (2); Chain (1); Domain (4); Modified residue (1) FUNCTION: Plays a fundamental role in microtubule-organizing center structure and function.; FUNCTION: Component of the TREX-2 complex (transcription and export complex 2), composed of at least ENY2, GANP, PCID2, SEM1, and either centrin CETN2 or CETN3. The TREX-2 complex functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket). TREX-2 participates in mRNA export and accurate chromatin positioning in the nucleus by tethering genes to the nuclear periphery. {ECO:0000250|UniProtKB:O15182}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:O15182}. Nucleus, nucleolus {ECO:0000250|UniProtKB:O15182}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:O15182}. Note=Centrosome of interphase and mitotic cells. Localizes to centriole distal lumen. {ECO:0000250|UniProtKB:O15182}. SUBUNIT: Monomer (By similarity). Component of the TREX-2 complex (transcription and export complex 2), composed of at least ENY2, GANP, PCID2, SEM1, and either centrin CETN2 or CETN3. {ECO:0000250, ECO:0000250|UniProtKB:O15182}. +Q8K4K1 CETN4_MOUSE Centrin-4 (Centrin4) 168 19,200 Alternative sequence (2); Calcium binding (2); Chain (1); Domain (4); Modified residue (1); Sequence conflict (4) FUNCTION: Ca(2+)-binding protein that may be involved in basal body assembly or in a subsequent step of ciliogenesis. {ECO:0000269|PubMed:12802058}. PTM: Phosphorylated on Thr-134 by casein kinase II (CK2) in a light-dependent manner. {ECO:0000269|PubMed:18269917}. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:12802058, ECO:0000269|PubMed:15347651, ECO:0000269|PubMed:18269917}. Cytoplasm {ECO:0000269|PubMed:12802058, ECO:0000269|PubMed:15347651, ECO:0000269|PubMed:18269917}. Note=Accumulates at procentrioles during their elongation. Isoform 3 is not observed in the centriole. SUBUNIT: Interacts with G-protein beta-gamma dimers in a calcium-dependent manner. {ECO:0000269|PubMed:15347651}. DOMAIN: The fourth EF-hand domain has been proven to bind calcium. TISSUE SPECIFICITY: In brain, specifically expressed in ciliated cells. In retina, expression is localized to the connecting cilium and basal body of photoreceptors (at protein level). Highly expressed in brain, kidney, lung, retina and ovary, and weakly expressed in spleen. Not detected in testis, colon, stomach, thymus, skeletal muscle, heart, intestine or liver. {ECO:0000269|PubMed:12802058, ECO:0000269|PubMed:15347651}. +Q91Z58 CF132_MOUSE Uncharacterized protein C6orf132 homolog 1206 127,881 Alternative sequence (2); Chain (1); Compositional bias (5); Modified residue (5)